LOCUS       NP_001161940             505 aa            linear   PRI 27-APR-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF4 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001161940
VERSION     NP_001161940.1
DBSOURCE    REFSEQ: accession NM_001168468.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Pouly,D., Chenaux,S., Martin,V., Babis,M., Koch,R., Nagoshi,E.,
            Katanaev,V.L., Gachon,F. and Staub,O.
  TITLE     USP2-45 Is a Circadian Clock Output Effector Regulating Calcium
            Absorption at the Post-Translational Level
  JOURNAL   PLoS One 11 (1), e0145155 (2016)
   PUBMED   26756164
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Reid,H.M., Turner,E.C., Mulvaney,E.P., Hyland,P.B., McLean,C. and
            Kinsella,B.T.
  TITLE     Interaction of the human prostacyclin receptor and the NHERF4
            family member intestinal and kidney enriched PDZ protein (IKEPP)
  JOURNAL   Biochim Biophys Acta 1823 (10), 1998-2012 (2012)
   PUBMED   22884631
  REMARK    GeneRIF: IKEPP was also found to be expressed in vascular
            endothelial cells where it co-localizes and complexes with the hIP
            Erratum:[Biochim Biophys Acta. 2015 Jan;1853(1):63-4]
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Lee,J.H., Nam,J.H., Park,J., Kang,D.W., Kim,J.Y., Lee,M.G. and
            Yoon,J.S.
  TITLE     Regulation of SLC26A3 activity by NHERF4 PDZ-mediated interaction
  JOURNAL   Cell Signal 24 (9), 1821-1830 (2012)
   PUBMED   22627094
  REMARK    GeneRIF: The NHERF4 is a novel modulator of luminal fluidity in the
            intestine by adjusting SLC26A3 expression and activity through a
            phosphorylation-dependent mechanism.
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Zachos,N.C., Hodson,C., Kovbasnjuk,O., Li,X., Thelin,W.R., Cha,B.,
            Milgram,S. and Donowitz,M.
  TITLE     Elevated intracellular calcium stimulates NHE3 activity by an IKEPP
            (NHERF4) dependent mechanism
  JOURNAL   Cell Physiol Biochem 22 (5-6), 693-704 (2008)
   PUBMED   19088451
  REMARK    GeneRIF: Regulation of NHE3 depends on the nature of the NHERF
            family member associating with NHE3 and the accompanying NHE3
            complexes.
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Thelin,W.R., Hodson,C.A. and Milgram,S.L.
  TITLE     Beyond the brush border: NHERF4 blazes new NHERF turf
  JOURNAL   J Physiol 567 (Pt 1), 13-19 (2005)
   PUBMED   15994182
  REMARK    Review article
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Kato,Y., Sai,Y., Yoshida,K., Watanabe,C., Hirata,T. and Tsuji,A.
  TITLE     PDZK1 directly regulates the function of organic cation/carnitine
            transporter OCTN2
  JOURNAL   Mol Pharmacol 67 (3), 734-743 (2005)
   PUBMED   15523054
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Hegedus,T., Sessler,T., Scott,R., Thelin,W., Bakos,E., Varadi,A.,
            Szabo,K., Homolya,L., Milgram,S.L. and Sarkadi,B.
  TITLE     C-terminal phosphorylation of MRP2 modulates its interaction with
            PDZ proteins
  JOURNAL   Biochem Biophys Res Commun 302 (3), 454-461 (2003)
   PUBMED   12615054
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Scott,R.O., Thelin,W.R. and Milgram,S.L.
  TITLE     A novel PDZ protein regulates the activity of guanylyl cyclase C,
            the heat-stable enterotoxin receptor
  JOURNAL   J Biol Chem 277 (25), 22934-22941 (2002)
   PUBMED   11950846
  REMARK    GeneRIF: A novel PDZ protein regulates the activity of guanylyl
            cyclase C, the heat-stable enterotoxin receptor.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA381610.1, AY047359.1 and AB094096.1.
            
            Summary: Guanylyl cyclase C (GCC, or GUCY2C; MIM 601330) produces
            cGMP following the binding of either endogenous ligands or
            heat-stable enterotoxins secreted by E. coli and other enteric
            bacteria. Activation of GCC initiates a signaling cascade that
            leads to phosphorylation of the cystic fibrosis transmembrane
            conductance regulator (CFTR; MIM 602421), followed by a net efflux
            of ions and water into the intestinal lumen. IKEPP is a regulatory
            protein that associates with GCC and regulates the amount of cGMP
            produced following receptor stimulation (Scott et al., 2002 [PubMed
            11950846]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315403.1, AY047359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355547.10/ ENSP00000347742.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..505
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF4
                     isoform 1"
                     /note="PDZ domain containing 2; natrium-phosphate
                     cotransporter IIa C-terminal-associated protein 2;
                     sodium-hydrogen exchanger regulatory factor 4; Na(+)/H(+)
                     exchange regulatory cofactor NHE-RF4; intestinal and
                     kidney enriched PDZ protein; NHERF-4; naPi-Cap2; PDZ
                     domain-containing protein 2; PDZ domain-containing protein
                     3; PDZ domain containing 3; na/Pi cotransporter
                     C-terminal-associated protein 2; Na(+)/H(+) exchange
                     regulatory cofactor 4"
                     /calculated_mol_wt=54086
     Region          48..127
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(59..65,76,79,108,112,115..116)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          156..233
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(166..170,181,184,213,217,220..221)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          262..344
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(272..278,292,295,324,328,331..332)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          409..478
                     /region_name="PDZ"
                     /note="Domain present in PSD-95, Dlg, and ZO-1/2;
                     smart00228"
                     /db_xref="CDD:214570"
     CDS             1..505
                     /gene="NHERF4"
                     /gene_synonym="IKEPP; PDZD3; PDZK2"
                     /coded_by="NM_001168468.2:21..1538"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53719.1"
                     /db_xref="GeneID:79849"
                     /db_xref="HGNC:HGNC:19891"
                     /db_xref="MIM:607146"
ORIGIN      
        1 mekaadlqdt asltlkfkfn pklgidnpvl slaedhdpyd pwslerprfc llskeegksf
       61 gfhlqqelgr aghvvcrvdp gtsaqrqglq egdrilavnn dvvehedyav vvrrirassp
      121 rvlltvlarh ahdvaraqlg edahlcptlg pgvrprlchi vkdeggfgfs vthgnqgpfw
      181 lvlstggaae ragvppgarl levngvsvek fthnqltrkl wqsgqqvtll vagpeveeqc
      241 rqlglplaap laegwalptk prclhlekgp qgfgfllree kgldgrpgqf lwevdpglpa
      301 kkagmqagdr lvavagesve glgheetvsr iqgqgscvsl tvvdpeadrf fsmvrlspll
      361 flenteapas prgsssaslv etedpsledt svpsvplgsr qcflypgpgg sygfrlscva
      421 sgprlfisqv tpggsaarag lqvgdvilev ngypvggqnd lerlqqlpea epplclklaa
      481 rslrgleawi ppgaaedwal asdll
//
LOCUS       NP_032284                154 aa            linear   ROD 27-APR-2025
DEFINITION  jupiter microtubule associated homolog 1 [Mus musculus].
ACCESSION   NP_032284
VERSION     NP_032284.1
DBSOURCE    REFSEQ: accession NM_008258.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Hupe,M., Li,M.X., Gertow Gillner,K., Adams,R.H. and Stenman,J.M.
  TITLE     Evaluation of TRAP-sequencing technology with a versatile
            conditional mouse model
  JOURNAL   Nucleic Acids Res 42 (2), e14 (2014)
   PUBMED   24165879
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Laughlin,K.M., Luo,D., Liu,C., Shaw,G., Warrington,K.H. Jr.,
            Qiu,J., Yachnis,A.T. and Harrison,J.K.
  TITLE     Hematopoietic- and neurologic-expressed sequence 1 expression in
            the murine GL261 and high-grade human gliomas
  JOURNAL   Pathol Oncol Res 15 (3), 437-444 (2009)
   PUBMED   19145478
  REMARK    GeneRIF: These data suggest a role for Hn1 in the biology of
            malignant brain tumors.
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Laughlin,K.M., Luo,D., Liu,C., Shaw,G., Warrington,K.H. Jr.,
            Law,B.K. and Harrison,J.K.
  TITLE     Hematopoietic- and neurologic-expressed sequence 1 (Hn1) depletion
            in B16.F10 melanoma cells promotes a differentiated phenotype that
            includes increased melanogenesis and cell cycle arrest
  JOURNAL   Differentiation 78 (1), 35-44 (2009)
   PUBMED   19427096
  REMARK    GeneRIF: Hn1 depletion in B16.F10 melanoma cells promotes a
            differentiated phenotype that includes increased melanogenesis and
            cell cycle arrest.
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Sone,M., Hayashi,T., Tarui,H., Agata,K., Takeichi,M. and
            Nakagawa,S.
  TITLE     The mRNA-like noncoding RNA Gomafu constitutes a novel nuclear
            domain in a subset of neurons
  JOURNAL   J Cell Sci 120 (Pt 15), 2498-2506 (2007)
   PUBMED   17623775
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Onodera,K., Shavit,J.A., Motohashi,H., Katsuoka,F., Akasaka,J.E.,
            Engel,J.D. and Yamamoto,M.
  TITLE     Characterization of the murine mafF gene
  JOURNAL   J Biol Chem 274 (30), 21162-21169 (1999)
   PUBMED   10409670
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Tang,W., Lai,Y.H., Han,X.D., Wong,P.M., Peters,L.L. and Chui,D.H.
  TITLE     Murine Hn1 on chromosome 11 is expressed in hemopoietic and brain
            tissues
  JOURNAL   Mamm Genome 8 (9), 695-696 (1997)
   PUBMED   9271675
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL645470.20.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U90123.1, BC003758.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 80.84 cM"
     Protein         1..154
                     /product="jupiter microtubule associated homolog 1"
                     /note="hematological and neurological expressed 1 protein;
                     hematological and neurological expressed sequence 1"
                     /calculated_mol_wt=15949
     Region          1..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97825.3)"
     Region          1..>58
                     /region_name="JUPITER"
                     /note="Microtubule-Associated protein Jupiter; pfam17054"
                     /db_xref="CDD:293659"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9UK76; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in Hematological and
                     neurological expressed 1 protein, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:Q9UK76; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UK76; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UK76; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UK76; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UK76; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UK76; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     Site            148
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P97825.3)"
     CDS             1..154
                     /gene="Jpt1"
                     /gene_synonym="Hn1"
                     /coded_by="NM_008258.2:119..583"
                     /db_xref="CCDS:CCDS25638.1"
                     /db_xref="GeneID:15374"
                     /db_xref="MGI:MGI:1096361"
ORIGIN      
        1 mtttttfkgv dpnsrnssrv lrppgggsnf slgfdepaeq pvrknkmasn ifgtpeenpp
       61 swaksagsks sggredsesp gtqrsnssea ssgdfldlkg egdmhenvdt dfqanlaqme
      121 ekpvpaapvp spvapapvps rrnppggkss lvlg
//
LOCUS       NP_001020601            1164 aa            linear   ROD 27-APR-2025
DEFINITION  C-Jun-amino-terminal kinase-interacting protein 4 isoform 4 [Mus
            musculus].
ACCESSION   NP_001020601
VERSION     NP_001020601.1
DBSOURCE    REFSEQ: accession NM_001025430.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Tian,M., Zhang,L., Zhang,M., Qiao,L., Xu,B., Li,C., Liu,S.,
            Song,Y., Wei,Z., Wang,Y. and Wang,H.
  TITLE     JLP/Foxk1/N-cadherin axis fosters a partial epithelial-mesenchymal
            transition state in epithelial tubular cells
  JOURNAL   iScience 26 (4), 106396 (2023)
   PUBMED   37013185
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Mohan,R.A., Bosada,F.M., van Weerd,J.H., van Duijvenboden,K.,
            Wang,J., Mommersteeg,M.T.M., Hooijkaas,I.B., Wakker,V., de Gier-de
            Vries,C., Coronel,R., Boink,G.J.J., Bakkers,J., Barnett,P.,
            Boukens,B.J. and Christoffels,V.M.
  TITLE     T-box transcription factor 3 governs a transcriptional program for
            the function of the mouse atrioventricular conduction system
  JOURNAL   Proc Natl Acad Sci U S A 117 (31), 18617-18626 (2020)
   PUBMED   32675240
REFERENCE   4  (residues 1 to 1164)
  AUTHORS   Hanata,N., Shoda,H., Hatano,H., Nagafuchi,Y., Komai,T., Okamura,T.,
            Suzuki,A., Gunarta,I.K., Yoshioka,K., Yamamoto,K. and Fujio,K.
  TITLE     Peptidylarginine Deiminase 4 Promotes the Renal Infiltration of
            Neutrophils and Exacerbates the TLR7 Agonist-Induced Lupus Mice
  JOURNAL   Front Immunol 11, 1095 (2020)
   PUBMED   32655553
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1164)
  AUTHORS   Yan,Q., Zhu,K., Zhang,L., Fu,Q., Chen,Z., Liu,S., Fu,D.,
            Nakazato,R., Yoshioka,K., Diao,B., Ding,G., Li,X. and Wang,H.
  TITLE     A negative feedback loop between JNK-associated leucine zipper
            protein and TGF-beta1 regulates kidney fibrosis
  JOURNAL   Commun Biol 3 (1), 288 (2020)
   PUBMED   32504044
  REMARK    GeneRIF: A negative feedback loop between JNK-associated leucine
            zipper protein and TGF-beta1 regulates kidney fibrosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1164)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   7  (residues 1 to 1164)
  AUTHORS   Kelkar,N., Delmotte,M.H., Weston,C.R., Barrett,T., Sheppard,B.J.,
            Flavell,R.A. and Davis,R.J.
  TITLE     Morphogenesis of the telencephalic commissure requires scaffold
            protein JNK-interacting protein 3 (JIP3)
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 9843-9848 (2003)
   PUBMED   12897243
REFERENCE   8  (residues 1 to 1164)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 1164)
  AUTHORS   Lee,C.M., Onesime,D., Reddy,C.D., Dhanasekaran,N. and Reddy,E.P.
  TITLE     JLP: A scaffolding protein that tethers JNK/p38MAPK signaling
            modules and transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14189-14194 (2002)
   PUBMED   12391307
  REMARK    GeneRIF: describe a protein, JLP, which acts as a scaffolding
            protein to bring mitogen-activated protein kinases and their target
            transcription factors together for the execution of specific
            signaling pathways
REFERENCE   10 (residues 1 to 1164)
  AUTHORS   Bowman,A.B., Kamal,A., Ritchings,B.W., Philp,A.V., McGrail,M.,
            Gindhart,J.G. and Goldstein,L.S.
  TITLE     Kinesin-dependent axonal transport is mediated by the sunday driver
            (SYD) protein
  JOURNAL   Cell 103 (4), 583-594 (2000)
   PUBMED   11106729
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CJ123181.1, AK014060.1, BC094670.1 and CO044222.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.190464.1, BC094670.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 58.9 cM"
     Protein         1..1164
                     /product="C-Jun-amino-terminal kinase-interacting protein
                     4 isoform 4"
                     /note="JNK-interacting protein 4; C-jun-amino-terminal
                     kinase-interacting protein 4; JNK-interacting leucine
                     zipper; JNK/SAPK-associated protein 2; JNK-associated
                     leucine-zipper protein; mitogen-activated protein kinase
                     8-interacting protein 4"
                     /calculated_mol_wt=127113
     Region          <151..329
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Region          249..317
                     /region_name="JIP_LZII"
                     /note="JNK-interacting protein leucine zipper II;
                     pfam16471"
                     /db_xref="CDD:465127"
     Region          <292..>485
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          797..>1015
                     /region_name="WD40_2"
                     /note="WD40 repeated domain; pfam19056"
                     /db_xref="CDD:465964"
     CDS             1..1164
                     /gene="Spag9"
                     /gene_synonym="3110018C07Rik; 4733401I23Rik;
                     4831406C20Rik; JIP-4; Jip4; JLP; JSAP2; JSAP2a; Mapk8ip4;
                     syd1"
                     /coded_by="NM_001025430.2:236..3730"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS25249.1"
                     /db_xref="GeneID:70834"
                     /db_xref="MGI:MGI:1918084"
ORIGIN      
        1 mnpgcmllfv fgfvggavvi nsailvslsv lllvhfsist gvpaltqnlp rilrkerpis
       61 lgifplpagd glltpdtqkg getpgseqwk fqelsqprsh tslkdelsdi sqggskattp
      121 astansdvsa ippdtpsked negfvkgtdt snkseiskhi evqvaqetrn vstesgenee
      181 ksevqaiies tpeldmdkdl sgykgsstpt kgienkafdr nteslfeels sagsgligdv
      241 degadllgmg revenlilen tqlletknal nvvkndliak vdeltcekdv lqgeleavkq
      301 aklkledknr eleeelrkar aeaedarqka kddddsdipt aqrkrftrve marvlmernq
      361 ykerlmelqe avrwtemira srenpamqek krssiwqffs rlfssssnat kkpeppvnlk
      421 ynaptshvtp svkkrsstls qlpgdkskaf dflseeteas lasrreqkre qyrqvkahvq
      481 kedgrvqafg wslpqkykqv angqgetkmk nlpvpvylrp ldekdasmkl wcavgvnlsg
      541 gktrdggsvv gasvfykdia gldtegskqr sasqssldkl dqelkeqqke fknqeelssq
      601 vwictsthst tkviiidavq pgnildsftv cnshvlcias vpgaretdyp ageelsesgq
      661 vdkaslcgsm tsnssaemds llggitvvgc stegltgaat spstngaspv iekppemete
      721 nsevdenipt aeeateateg nagstedtvd isqpgvyteh vftdplgvqi pedlspvfqs
      781 sndsdvykdq isvlpneqdl areeaqkmss llptmwlgaq ngclyvhssv aqwrkclhsi
      841 klkdsilsiv hvkgivlval adgtlaifhr gvdgqwdlsn yhlldlgrph hsircmtvvh
      901 dkvwcgyrnk iyvvqpkamk ieksfdahpr kesqvrqlaw vgdgvwvsir ldstlrlyha
      961 htyqhlqdvd iepyvskmlg tgklgfsfvr italmvscnr lwvgtgngvi isipltetnk
     1021 tsgtpgnrpg svirvygden sdkvtpgtfi pycsmahaql cfhghrdavk ffvavpgqvi
     1081 spqsssggad ltadkagssa qepssqtplk smlvisggeg yidfrmgdeg gesellgedl
     1141 plepsvtkae rshlivwqvm cgne
//
LOCUS       NP_006570                230 aa            linear   PRI 27-APR-2025
DEFINITION  3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase [Homo sapiens].
ACCESSION   NP_006570
VERSION     NP_006570.1
DBSOURCE    REFSEQ: accession NM_006579.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Yao,H., Cai,H. and Li,D.
  TITLE     Thermostabilization of Membrane Proteins by Consensus Mutation: A
            Case Study for a Fungal Delta8-7 Sterol Isomerase
  JOURNAL   J Mol Biol 432 (18), 5162-5183 (2020)
   PUBMED   32105736
  REMARK    GeneRIF: Thermostabilization of Membrane Proteins by Consensus
            Mutation: A Case Study for a Fungal Delta8-7 Sterol Isomerase.
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Cai,H., Yao,H., Li,T., Tang,Y. and Li,D.
  TITLE     High-level heterologous expression of the human transmembrane
            sterol Delta8,Delta7-isomerase in Pichia pastoris
  JOURNAL   Protein Expr Purif 164, 105463 (2019)
   PUBMED   31381990
  REMARK    GeneRIF: The human sterol delta(8)-Delta(7) isomerase was expressed
            in P. pastoris to 200mgL-1.  The membrane protein enzyme could be
            solubilized readily in dodecyl maltoside. The solubilized protein
            displayed a symmetric peak on size exclusion chromatography.
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Long,T., Hassan,A., Thompson,B.M., McDonald,J.G., Wang,J. and Li,X.
  TITLE     Structural basis for human sterol isomerase in cholesterol
            biosynthesis and multidrug recognition
  JOURNAL   Nat Commun 10 (1), 2452 (2019)
   PUBMED   31165728
  REMARK    GeneRIF: EBP adopts an unreported fold involving five
            transmembrane-helices (TMs) that creates a membrane cavity
            presenting a pharmacological binding site that accommodates
            multiple different ligands. Mutagenesis studies on specific
            residues abolish the isomerase activity and decrease the multidrug
            binding capacity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Derry,J.M., Gormally,E., Means,G.D., Zhao,W., Meindl,A.,
            Kelley,R.I., Boyd,Y. and Herman,G.E.
  TITLE     Mutations in a delta 8-delta 7 sterol isomerase in the tattered
            mouse and X-linked dominant chondrodysplasia punctata.
            jderry@immunex.com
  JOURNAL   Nat Genet 22 (3), 286-290 (1999)
   PUBMED   10391218
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Moebius,F.F., Soellner,K.E., Fiechtner,B., Huck,C.W., Bonn,G. and
            Glossmann,H.
  TITLE     Histidine77, glutamic acid81, glutamic acid123, threonine126,
            asparagine194, and tryptophan197 of the human emopamil binding
            protein are required for in vivo sterol delta 8-delta 7
            isomerization
  JOURNAL   Biochemistry 38 (3), 1119-1127 (1999)
   PUBMED   9894009
REFERENCE   8  (residues 1 to 230)
  AUTHORS   Schindelhauer,D., Hellebrand,H., Grimm,L., Bader,I., Meitinger,T.,
            Wehnert,M., Ross,M. and Meindl,A.
  TITLE     Long-range map of a 3.5-Mb region in Xp11.23-22 with a
            sequence-ready map from a 1.1-Mb gene-rich interval
  JOURNAL   Genome Res 6 (11), 1056-1069 (1996)
   PUBMED   8938429
REFERENCE   9  (residues 1 to 230)
  AUTHORS   Hanner,M., Moebius,F.F., Weber,F., Grabner,M., Striessnig,J. and
            Glossmann,H.
  TITLE     Phenylalkylamine Ca2+ antagonist binding protein. Molecular
            cloning, tissue distribution, and heterologous expression
  JOURNAL   J Biol Chem 270 (13), 7551-7557 (1995)
   PUBMED   7706302
REFERENCE   10 (residues 1 to 230)
  AUTHORS   Kumble,S. and Savarirayan,R.
  TITLE     Chondrodysplasia Punctata 2, X-Linked
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634086
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CA488777.1, BC001572.1 and
            BC001549.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is an integral membrane
            protein of the endoplasmic reticulum. It is a high affinity binding
            protein for the antiischemic phenylalkylamine Ca2+ antagonist
            [3H]emopamil and the photoaffinity label [3H]azidopamil. It is
            similar to sigma receptors and may be a member of a superfamily of
            high affinity drug-binding proteins in the endoplasmic reticulum of
            different tissues. This protein shares structural features with
            bacterial and eukaryontic drug transporting proteins. It has four
            putative transmembrane segments and contains two conserved
            glutamate residues which may be involved in the transport of
            cationic amphiphilics. Another prominent feature of this protein is
            its high content of aromatic amino acid residues (>23%) in its
            transmembrane segments. These aromatic amino acid residues have
            been suggested to be involved in the drug transport by the
            P-glycoprotein. Mutations in this gene cause Chondrodysplasia
            punctata 2 (CDPX2; also known as Conradi-Hunermann syndrome).
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.191296.1,
                                           SRR5189658.116351.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000495186.6/ ENSP00000417052.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..230
                     /product="3-beta-hydroxysteroid-Delta(8),
                     Delta(7)-isomerase"
                     /EC_number="5.3.3.5"
                     /EC_number="3.3.2.11"
                     /note="3-beta-hydroxysteroid-delta-8,delta-7-isomerase;
                     sterol 8-isomerase; Chondrodysplasia punctata-2, X-linked
                     dominant (Happle syndrome); D8-D7 sterol isomerase;
                     cholestenol Delta-isomerase; delta(8)-Delta(7) sterol
                     isomerase; cholesterol-5,6-epoxide hydrolase subunit EBP;
                     emopamil-binding protein; emopamil binding protein (sterol
                     isomerase)"
                     /calculated_mol_wt=26222
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q15125.3)"
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15125.3)"
     Site            66..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15125.3)"
     Region          96..207
                     /region_name="EBP"
                     /note="EXPERA (EXPanded EBP superfamily); pfam05241"
                     /db_xref="CDD:461600"
     Site            121..141
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15125.3)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15125.3)"
     CDS             1..230
                     /gene="EBP"
                     /gene_synonym="CDPX2; CHO2; CPX; CPXD; MEND"
                     /coded_by="NM_006579.3:174..866"
                     /db_xref="CCDS:CCDS14300.1"
                     /db_xref="GeneID:10682"
                     /db_xref="HGNC:HGNC:3133"
                     /db_xref="MIM:300205"
ORIGIN      
        1 mttnagplhp ywpqhlrldn fvpndrptwh ilaglfsvtg vlvvttwlls graavvplgt
       61 wrrlslcwfa vcgfihlvie gwfvlyyedl lgdqaflsql wkeyakgdsr yilgdnftvc
      121 metitaclwg plslwvviaf lrqhplrfil qlvvsvgqiy gdvlyflteh rdgfqhgelg
      181 hplyfwfyfv fmnalwlvlp gvlvldavkh lthaqstlda katkakskkn
//
LOCUS       NP_005079                695 aa            linear   PRI 27-APR-2025
DEFINITION  A-kinase anchor protein 17A isoform 1 [Homo sapiens].
ACCESSION   NP_005079
VERSION     NP_005079.2
DBSOURCE    REFSEQ: accession NM_005088.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Lee,B.P., Pilling,L.C., Bandinelli,S., Ferrucci,L., Melzer,D. and
            Harries,L.W.
  TITLE     The transcript expression levels of HNRNPM, HNRNPA0 and AKAP17A
            splicing factors may be predictively associated with ageing
            phenotypes in human peripheral blood
  JOURNAL   Biogerontology 20 (5), 649-663 (2019)
   PUBMED   31292793
  REMARK    GeneRIF: The expression of splicing factor gene AKAP17A was
            associated with Cognitive Decline as measured by the Mini-Mental
            State Examinations and also with a decline in Physical Ability as
            measured by hand-grip strength in ageing human population.
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Jarnaess,E., Stokka,A.J., Kvissel,A.K., Skalhegg,B.S.,
            Torgersen,K.M., Scott,J.D., Carlson,C.R. and Tasken,K.
  TITLE     Splicing factor arginine/serine-rich 17A (SFRS17A) is an A-kinase
            anchoring protein that targets protein kinase A to splicing factor
            compartments
  JOURNAL   J Biol Chem 284 (50), 35154-35164 (2009)
   PUBMED   19840947
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Mangs,A.H., Speirs,H.J., Goy,C., Adams,D.J., Markus,M.A. and
            Morris,B.J.
  TITLE     XE7: a novel splicing factor that interacts with ASF/SF2 and ZNF265
  JOURNAL   Nucleic Acids Res 34 (17), 4976-4986 (2006)
   PUBMED   16982639
  REMARK    GeneRIF: The spliceosomal component XE7 resembles an SR-related
            splicing protein, and can influence alternative splicing.
REFERENCE   8  (residues 1 to 695)
  AUTHORS   Ried,K., Rao,E., Schiebel,K. and Rappold,G.A.
  TITLE     Gene duplications as a recurrent theme in the evolution of the
            human pseudoautosomal region 1: isolation of the gene ASMTL
  JOURNAL   Hum Mol Genet 7 (11), 1771-1778 (1998)
   PUBMED   9736779
REFERENCE   9  (residues 1 to 695)
  AUTHORS   Ellison,J.W., Ramos,C., Yen,P.H. and Shapiro,L.J.
  TITLE     Structure and expression of the human pseudoautosomal gene XE7
  JOURNAL   Hum Mol Genet 1 (9), 691-696 (1992)
   PUBMED   1302606
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Voland,J.R., Wyzykowski,R.J., Huang,M. and Dutton,R.W.
  TITLE     Cloning and sequencing of a trophoblast-endothelial-activated
            lymphocyte surface protein: cDNA sequence and genomic structure
  JOURNAL   Proc Natl Acad Sci U S A 89 (21), 10425-10429 (1992)
   PUBMED   1438229
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC016935.1, BC028151.1,
            BC015800.1, BM713425.1, M99578.1 and BM046630.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 23, 2004 this sequence version replaced NP_005079.1.
            
            Summary: This locus encodes a protein kinase A anchoring protein.
            The encoded protein is part of the spliceosome complex and is
            involved in the regulation of alternate splicing in some mRNA
            precursors. Alternatively spliced transcript variants have been
            identified for this gene.[provided by RefSeq, Sep 2010].
            
            Transcript Variant: This variant (1) encodes the functional
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.115823.1,
                                           SRR3476690.948348.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313871.9/ ENSP00000324827.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /chromosome="Y"
                     /map="X"
                     /map="Y"
     Protein         1..695
                     /product="A-kinase anchor protein 17A isoform 1"
                     /note="splicing factor, arginine/serine-rich 17A; A-kinase
                     anchor protein 17A; B-lymphocyte surface antigen;
                     pseudoautosomal gene XE7; protein kinase A-anchoring
                     protein 17A; A kinase (PRKA) anchor protein 17A"
                     /calculated_mol_wt=80605
     Region          83..112
                     /region_name="PKA-RI and PKA-RII subunit binding domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02040.2)"
     Region          143..265
                     /region_name="RRM_AKAP17A"
                     /note="RNA recognition motif (RRM) found in A-kinase
                     anchor protein 17A (AKAP-17A) and similar proteins;
                     cd12264"
                     /db_xref="CDD:409708"
     Region          279..337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02040.2)"
     Region          <329..>443
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          425..454
                     /region_name="PKA-RI-alpha subunit binding domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02040.2)"
     Region          482..695
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02040.2)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q02040.2)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q02040.2)"
     CDS             1..695
                     /gene="AKAP17A"
                     /gene_synonym="721P; AKAP-17A; CCDC133; CXYorf3; DXYS155E;
                     PRKA17A; SFRS17A; XE7; XE7Y"
                     /coded_by="NM_005088.3:186..2273"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14116.1"
                     /db_xref="GeneID:8227"
                     /db_xref="HGNC:HGNC:18783"
                     /db_xref="MIM:312095"
                     /db_xref="MIM:465000"
ORIGIN      
        1 maaativhdt seavelcpay glylkpitkm tisvalpqlk qpgksisnwe vmerlkgmvq
       61 nhqfstlris kstmdfirfe gevenkslvk sflacldgkt iklsgfsdil kvraaefkid
      121 fptrhdwdsf frdakdmnet lpgerpdtih leglpckwfa lkesgsekps edvlvkvfek
      181 fgeirnvdip mldpyreemt grnfhtfsfg ghlnfeayvq yreymgfiqa msalrgmklm
      241 ykgedgkava cnikvsfdst khlsdasikk rqlerqklqe leqqreeqkr rekeaeerqr
      301 aeerkqkele elererkree klrkreqkqr drelrrnqkk leklqaeeqk qlqekiklee
      361 rklllaqrnl qsirliaell srakavklre qeqkeeklrl qqqeerrrlq eaelrrveee
      421 keralglqrk erelrerlls illskkpdds hthdelgvah adllqpvldi lqtvssgcvs
      481 attlhplggq ppagapkesp ahpeadgapk svngsvaeea pckevqsscr vvpedgspek
      541 rcpggvlsci pdnnqqpkgi paceqnvsrk dtrseqdkcn repskgrgra tgdgladrhk
      601 rersrarras sredgrprke rrphkkhayk ddsprrrsts pdhtrsrrsh skdrhrrers
      661 rerrgsasrk hsrhrrrser srsrspsrhr stwnr
//
LOCUS       NP_057126                275 aa            linear   PRI 27-APR-2025
DEFINITION  exosome complex component RRP40 isoform 1 [Homo sapiens].
ACCESSION   NP_057126
VERSION     NP_057126.2
DBSOURCE    REFSEQ: accession NM_016042.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Lu,G., Liu,H., Wang,H., Tang,X., Luo,S., Du,M., Christiani,D.C. and
            Wei,Q.
  TITLE     Potentially functional variants of INPP5D and EXOSC3 in immunity B
            cell-related genes are associated with non-small cell lung cancer
            survival
  JOURNAL   Front Immunol 15, 1440454 (2024)
   PUBMED   39176091
  REMARK    GeneRIF: Potentially functional variants of INPP5D and EXOSC3 in
            immunity B cell-related genes are associated with non-small cell
            lung cancer survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Van Quekelberghe,C., Latta,K., Kunzmann,S., Grohmann,M. and
            Hansen,M.
  TITLE     Atypical hemolytic uremic syndrome induced by SARS-CoV2 infection
            in infants with EXOSC3 mutation
  JOURNAL   Pediatr Nephrol 37 (11), 2781-2784 (2022)
   PUBMED   35522339
  REMARK    GeneRIF: Atypical hemolytic uremic syndrome induced by SARS-CoV2
            infection in infants with EXOSC3 mutation.
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Tsuda,M., Noguchi,M., Kurai,T., Ichihashi,Y., Ise,K., Wang,L.,
            Ishida,Y., Tanino,M., Hirano,S., Asaka,M. and Tanaka,S.
  TITLE     Aberrant expression of MYD88 via RNA-controlling CNOT4 and EXOSC3
            in colonic mucosa impacts generation of colonic cancer
  JOURNAL   Cancer Sci 112 (12), 5100-5113 (2021)
   PUBMED   34626022
  REMARK    GeneRIF: Aberrant expression of MYD88 via RNA-controlling CNOT4 and
            EXOSC3 in colonic mucosa impacts generation of colonic cancer.
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Mu,W., Heller,T. and Baranano,K.W.
  TITLE     Two siblings with a novel variant of EXOSC3 extended phenotypic
            spectrum of pontocerebellar hypoplasia 1B to an exceptionally mild
            form
  JOURNAL   BMJ Case Rep 14 (1), e236732 (2021)
   PUBMED   33462000
  REMARK    GeneRIF: Two siblings with a novel variant of EXOSC3 extended
            phenotypic spectrum of pontocerebellar hypoplasia 1B to an
            exceptionally mild form.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Mukherjee,D., Gao,M., O'Connor,J.P., Raijmakers,R., Pruijn,G.,
            Lutz,C.S. and Wilusz,J.
  TITLE     The mammalian exosome mediates the efficient degradation of mRNAs
            that contain AU-rich elements
  JOURNAL   EMBO J 21 (1-2), 165-174 (2002)
   PUBMED   11782436
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Allmang,C., Petfalski,E., Podtelejnikov,A., Mann,M., Tollervey,D.
            and Mitchell,P.
  TITLE     The yeast exosome and human PM-Scl are related complexes of 3' -->
            5' exonucleases
  JOURNAL   Genes Dev 13 (16), 2148-2158 (1999)
   PUBMED   10465791
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Baas,F. and van Dijk,T.
  TITLE     EXOSC3 Pontocerebellar Hypoplasia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25144110
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF281132.1, AK290864.1 and
            BE048144.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 22, 2004 this sequence version replaced NP_057126.1.
            
            Summary: This gene encodes a non-catalytic component of the human
            exosome, a complex with 3'-5' exoribonuclease activity that plays a
            role in numerous RNA processing and degradation activities. Related
            pseudogenes of this gene are found on chromosome 19 and 21.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.56586.1,
                                           SRR1660803.163190.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153932, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327304.10/ ENSP00000323046.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.2"
     Protein         1..275
                     /product="exosome complex component RRP40 isoform 1"
                     /note="exosome complex exonuclease RRP40; exosome complex
                     component RRP40; ribosomal RNA-processing protein 40"
                     /calculated_mol_wt=29441
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NQT5.3)"
     Region          108..193
                     /region_name="S1_Rrp40"
                     /note="Rrp40 S1-like RNA-binding domain. S1-like
                     RNA-binding domains are found in a wide variety of
                     RNA-associated proteins. Rrp4 protein is a subunit of the
                     exosome complex. The exosome plays a central role in 3' to
                     5' RNA processing and degradation in...; cd05790"
                     /db_xref="CDD:240216"
     Site            order(108,132,136..137,159..161)
                     /site_type="other"
                     /note="subunit interface [polypeptide binding]"
                     /db_xref="CDD:240216"
     Site            order(122,130,140,142)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:240216"
     Region          196..273
                     /region_name="KH-I_Rrp40"
                     /note="type I K homology (KH) RNA-binding domain found in
                     exosome complex component Rrp40 and similar proteins;
                     cd22526"
                     /db_xref="CDD:411954"
     Site            order(196..198,248)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:411954"
     CDS             1..275
                     /gene="EXOSC3"
                     /gene_synonym="bA3J10.7; CGI-102; hRrp-40; p10; PCH1B;
                     RRP40; Rrp40p"
                     /coded_by="NM_016042.4:21..848"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35016.1"
                     /db_xref="GeneID:51010"
                     /db_xref="HGNC:HGNC:17944"
                     /db_xref="MIM:606489"
ORIGIN      
        1 maepasvaae slagsraraa rtvlgqvvlp geelllpeqe daegpggave rplslnarac
       61 srvrvvcgpg lrrcgdrllv tkcgrlrhke pgsgsgggvy wvdsqqkryv pvkgdhvigi
      121 vtaksgdifk vdvggsepas lsylsfegat krnrpnvqvg dliygqfvva nkdmepemvc
      181 idscgrangm gvigqdgllf kvtlglirkl lapdceiiqe vgklypleiv fgmngriwvk
      241 aktiqqtlil anileacehm tsdqrkqifs rlaes
//
LOCUS       NP_001352158             258 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-dependent glucokinase isoform 3 [Homo sapiens].
ACCESSION   NP_001352158 XP_024305852
VERSION     NP_001352158.1
DBSOURCE    REFSEQ: accession NM_001365229.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Herrera-Morande,A., Vallejos-Baccelliere,G., Cea,P.A., Zamora,R.A.,
            Cid,D., Maturana,P., Gonzalez-Ordenes,F., Castro-Fernandez,V. and
            Guixe,V.
  TITLE     Kinetic characterization and phylogenetic analysis of human
            ADP-dependent glucokinase reveal new insights into its regulatory
            properties
  JOURNAL   Arch Biochem Biophys 741, 109602 (2023)
   PUBMED   37084804
  REMARK    GeneRIF: Kinetic characterization and phylogenetic analysis of
            human ADP-dependent glucokinase reveal new insights into its
            regulatory properties.
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Tandon,A., Birkenhagen,J., Nagalla,D., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase as a novel onco-target for haematological
            malignancies
  JOURNAL   Sci Rep 10 (1), 13584 (2020)
   PUBMED   32788680
  REMARK    GeneRIF: ADP-dependent glucokinase as a novel onco-target for
            haematological malignancies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Jiang,H.Y. and Wang,Z.J.
  TITLE     ADPGK-AS1 promotes the progression of colorectal cancer via
            sponging miR-525 to upregulate FUT1
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2380-2386 (2020)
   PUBMED   32196589
  REMARK    GeneRIF: ADPGK-AS1 promotes the progression of colorectal cancer
            via sponging miR-525 to upregulate FUT1.
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Imle,R., Wang,B.T., Stutzenberger,N., Birkenhagen,J., Tandon,A.,
            Carl,M., Himmelreich,N., Thiel,C., Grone,H.J., Poschet,G.,
            Volkers,M., Gulow,K., Schroder,A., Carillo,S., Mittermayr,S.,
            Bones,J., Kaminski,M.M., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing
  JOURNAL   Sci Rep 9 (1), 14248 (2019)
   PUBMED   31582762
  REMARK    GeneRIF: ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Richter,J.P., Goroncy,A.K., Ronimus,R.S. and Sutherland-Smith,A.J.
  TITLE     The Structural and Functional Characterization of Mammalian
            ADP-dependent Glucokinase
  JOURNAL   J Biol Chem 291 (8), 3694-3704 (2016)
   PUBMED   26555263
  REMARK    GeneRIF: ADPGK is substrate inhibited by high glucose concentration
            and shows high specificity for glucose, with no activity for other
            sugars, as determined by NMR spectroscopy, including 2-deoxyglucose
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Cuesta-Munoz,A.L., Tuomi,T., Cobo-Vuilleumier,N., Koskela,H.,
            Odili,S., Stride,A., Buettger,C., Otonkoski,T., Froguel,P.,
            Grimsby,J., Garcia-Gimeno,M. and Matschinsky,F.M.
  TITLE     Clinical heterogeneity in monogenic diabetes caused by mutations in
            the glucokinase gene (GCK-MODY)
  JOURNAL   Diabetes Care 33 (2), 290-292 (2010)
   PUBMED   19903754
  REMARK    GeneRIF: Glucose and insulin response to oral glucose is higher in
            GCK(261) carriers, indicating clinical heterogeneity in GCK
            maturity diabetes carriers.
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Codner,E., Rocha,A., Deng,L., Martinez-Aguayo,A., Godoy,C.,
            Mericq,V. and Chung,W.K.
  TITLE     Mild fasting hyperglycemia in children: high rate of glucokinase
            mutations and some risk of developing type 1 diabetes mellitus
  JOURNAL   Pediatr Diabetes 10 (6), 382-388 (2009)
   PUBMED   19309449
  REMARK    GeneRIF: The presence of mild persistent hyperglycemia in any
            patient without autoantibodies should lead to genetic analysis of
            glucokinase, particularly if there is a positive family history.
REFERENCE   9  (residues 1 to 258)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 258)
  AUTHORS   Ronimus,R.S. and Morgan,H.W.
  TITLE     Cloning and biochemical characterization of a novel mouse
            ADP-dependent glucokinase
  JOURNAL   Biochem Biophys Res Commun 315 (3), 652-658 (2004)
   PUBMED   14975750
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009712.22.
            
            On Aug 9, 2018 this sequence version replaced XP_024305852.1.
            
            Summary: ADPGK (EC 2.7.1.147) catalyzes the ADP-dependent
            phosphorylation of glucose to glucose-6-phosphate and may play a
            role in glycolysis, possibly during ischemic conditions (Ronimus
            and Morgan, 2004 [PubMed 14975750]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.5476.1,
                                           SRR1803616.38675.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..258
                     /product="ADP-dependent glucokinase isoform 3"
                     /EC_number="2.7.1.147"
                     /note="ATP-dependent glucokinase; rbBP-35"
                     /calculated_mol_wt=28282
     Region          <1..253
                     /region_name="ribokinase_pfkB_like"
                     /note="ribokinase/pfkB superfamily: Kinases that accept a
                     wide variety of substrates, including carbohydrates and
                     aromatic small molecules, all are phosphorylated at a
                     hydroxyl group. The superfamily includes ribokinase,
                     fructokinase, ketohexokinase; cl00192"
                     /db_xref="CDD:469648"
     Site            order(86,143,237,240..241,244)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238177"
     CDS             1..258
                     /gene="ADPGK"
                     /gene_synonym="2610017G09Rik; ADP-GK"
                     /coded_by="NM_001365229.1:772..1548"
                     /note="isoform 3 is encoded by transcript variant 8"
                     /db_xref="GeneID:83440"
                     /db_xref="HGNC:HGNC:25250"
                     /db_xref="MIM:611861"
ORIGIN      
        1 mnmlevfvss leefqpdlvv lsglhmmegq skelqrkrll evvtsisdip tgipvhlela
       61 smtnrelmss ivhqqvfpav tslglneqel lfltqsasgp hsslsswngv pdvgmvsdil
      121 fwilkehgrs ksrasdltri hfhtlvyhil atvdghwanq laavaagarv agtqacatet
      181 idtsrvslra pqefmtshse agsrivlnpn kpvvewhreg isfhftpvlv ckdpirtvgl
      241 gdaisaeglf ysevhphy
//
LOCUS       NP_443171                734 aa            linear   PRI 27-APR-2025
DEFINITION  Fc receptor-like protein 3 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_443171
VERSION     NP_443171.2
DBSOURCE    REFSEQ: accession NM_052939.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Yu,K., Jiang,R., Li,Z., Ren,X., Jiang,H. and Zhao,Z.
  TITLE     Integrated analyses of single-cell transcriptome and Mendelian
            randomization reveal the protective role of FCRL3 in multiple
            sclerosis
  JOURNAL   Front Immunol 15, 1428962 (2024)
   PUBMED   39076991
  REMARK    GeneRIF: Integrated analyses of single-cell transcriptome and
            Mendelian randomization reveal the protective role of FCRL3 in
            multiple sclerosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Bahabayi,A., Zhang,Y.H., Yuan,Z., Wang,Y., Zhang,Z., Zeng,X.,
            Guan,Z., Wang,P. and Liu,C.
  TITLE     FCRL3 expression is upregulated and closely correlates with TIGIT
            expression in regulatory T cells of patients with systemic lupus
            erythematosus
  JOURNAL   Eur J Immunol 54 (5), e2350739 (2024)
   PUBMED   38461541
  REMARK    GeneRIF: FCRL3 expression is upregulated and closely correlates
            with TIGIT expression in regulatory T cells of patients with
            systemic lupus erythematosus.
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Bianchi,E., Jimenez-Movilla,M., Cots-Rodriguez,P., Viola,C. and
            Wright,G.J.
  TITLE     No evidence for a direct extracellular interaction between human Fc
            receptor-like 3 (MAIA) and the sperm ligand IZUMO1
  JOURNAL   Sci Adv 10 (8), eadk6352 (2024)
   PUBMED   38381819
  REMARK    GeneRIF: No evidence for a direct extracellular interaction between
            human Fc receptor-like 3 (MAIA) and the sperm ligand IZUMO1.
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Balunathan,N., Rani,G. U, Perumal,V. and Kumarasamy,P.
  TITLE     Single nucleotide polymorphisms of Interleukin - 4, Interleukin-18,
            FCRL3 and sPLA2IIa genes and their association in pathogenesis of
            endometriosis
  JOURNAL   Mol Biol Rep 50 (5), 4239-4252 (2023)
   PUBMED   36905404
  REMARK    GeneRIF: Single nucleotide polymorphisms of Interleukin - 4,
            Interleukin-18, FCRL3 and sPLA2IIa genes and their association in
            pathogenesis of endometriosis.
REFERENCE   5  (residues 1 to 734)
  AUTHORS   Zhong,Z., Shi,D., Xiao,M., Fu,D., Feng,S., Kong,Q., Li,J. and Li,Z.
  TITLE     Expression profile of Fc receptor-like molecules in patients with
            IgA nephropathy
  JOURNAL   Hum Immunol 82 (3), 186-192 (2021)
   PUBMED   33597097
  REMARK    GeneRIF: Expression profile of Fc receptor-like molecules in
            patients with IgA nephropathy.
REFERENCE   6  (residues 1 to 734)
  AUTHORS   Kochi,Y., Yamada,R., Suzuki,A., Harley,J.B., Shirasawa,S.,
            Sawada,T., Bae,S.C., Tokuhiro,S., Chang,X., Sekine,A.,
            Takahashi,A., Tsunoda,T., Ohnishi,Y., Kaufman,K.M., Kang,C.P.,
            Kang,C., Otsubo,S., Yumura,W., Mimori,A., Koike,T., Nakamura,Y.,
            Sasazuki,T. and Yamamoto,K.
  TITLE     A functional variant in FCRL3, encoding Fc receptor-like 3, is
            associated with rheumatoid arthritis and several autoimmunities
  JOURNAL   Nat Genet 37 (5), 478-485 (2005)
   PUBMED   15838509
  REMARK    Erratum:[Nat Genet. 2005 Jun;37(6):652]
REFERENCE   7  (residues 1 to 734)
  AUTHORS   Xu,M.J., Zhao,R., Cao,H. and Zhao,Z.J.
  TITLE     SPAP2, an Ig family receptor containing both ITIMs and ITAMs
  JOURNAL   Biochem Biophys Res Commun 293 (3), 1037-1046 (2002)
   PUBMED   12051764
  REMARK    GeneRIF: molecular cloning and characterization of SPAP2
REFERENCE   8  (residues 1 to 734)
  AUTHORS   Miller,I., Hatzivassiliou,G., Cattoretti,G., Mendelsohn,C. and
            Dalla-Favera,R.
  TITLE     IRTAs: a new family of immunoglobulinlike receptors differentially
            expressed in B cells
  JOURNAL   Blood 99 (8), 2662-2669 (2002)
   PUBMED   11929751
REFERENCE   9  (residues 1 to 734)
  AUTHORS   Davis,R.S., Dennis,G. Jr., Kubagawa,H. and Cooper,M.D.
  TITLE     Fc receptor homologs (FcRH1-5) extend the Fc receptor family
  JOURNAL   Curr Top Microbiol Immunol 266, 85-112 (2002)
   PUBMED   12014205
  REMARK    Review article
REFERENCE   10 (residues 1 to 734)
  AUTHORS   Davis,R.S., Wang,Y.H., Kubagawa,H. and Cooper,M.D.
  TITLE     Identification of a family of Fc receptor homologs with
            preferential B cell expression
  JOURNAL   Proc Natl Acad Sci U S A 98 (17), 9772-9777 (2001)
   PUBMED   11493702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF459027.1, CD690165.1 and
            AL356276.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 3, 2002 this sequence version replaced NP_443171.1.
            
            Summary: This gene encodes a member of the immunoglobulin receptor
            superfamily and is one of several Fc receptor-like glycoproteins
            clustered on the long arm of chromosome 1. The encoded protein
            contains immunoreceptor-tyrosine activation motifs and
            immunoreceptor-tyrosine inhibitory motifs in its cytoplasmic domain
            and may play a role in regulation of the immune system. Mutations
            in this gene have been associated with rheumatoid arthritis,
            autoimmune thyroid disease, and systemic lupus erythematosus.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF459027.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368184.8/ ENSP00000357167.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.1"
     Protein         1..734
                     /product="Fc receptor-like protein 3 isoform 1 precursor"
                     /note="SH2 domain-containing phosphatase anchor protein 2;
                     Fc receptor homolog 3; immunoglobulin superfamily receptor
                     translocation associated protein 3; hIFGP3; fcR-like
                     protein 3; IFGP family protein 3; immune receptor
                     translocation-associated protein 3"
                     /calculated_mol_wt=79634
     sig_peptide     1..10
                     /calculated_mol_wt=1241
     mat_peptide     11..734
                     /product="Fc receptor-like protein 3 isoform 1"
                     /calculated_mol_wt=79634
     Region          23..97
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          40..44
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          55..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          70..74
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          79..84
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          90..93
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          101..185
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          116..120
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          130..134
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          146..150
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          160..165
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          178..181
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          192..280
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Region          292..366
                     /region_name="ig"
                     /note="Immunoglobulin domain; pfam00047"
                     /db_xref="CDD:395002"
     Region          305..309
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          319..323
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          341..345
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          355..360
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          383..469
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Region          475..548
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            561
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96P31.1)"
     Site            574..594
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P31.1)"
     Region          603..655
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P31.1)"
     Region          648..653
                     /region_name="ITIM motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P31.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:19843936; propagated from
                     UniProtKB/Swiss-Prot (Q96P31.1)"
     Region          660..665
                     /region_name="ITIM motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P31.1)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:19843936; propagated from
                     UniProtKB/Swiss-Prot (Q96P31.1)"
     Region          690..695
                     /region_name="ITIM motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P31.1)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:19843936; propagated from
                     UniProtKB/Swiss-Prot (Q96P31.1)"
     Region          695..734
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P31.1)"
     Region          720..725
                     /region_name="ITIM motif 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P31.1)"
     Site            722
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:19843936; propagated from
                     UniProtKB/Swiss-Prot (Q96P31.1)"
     CDS             1..734
                     /gene="FCRL3"
                     /gene_synonym="CD307c; FCRH3; IFGP3; IRTA3; MAIA; SPAP2"
                     /coded_by="NM_052939.4:205..2409"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1167.1"
                     /db_xref="GeneID:115352"
                     /db_xref="HGNC:HGNC:18506"
                     /db_xref="MIM:606510"
ORIGIN      
        1 mllwllllil tpgreqsgva pkavlllnpp wstafkgekv alicssishs laqgdtywyh
       61 dekllkikhd kiqitepgny qcktrgssls davhvefspd wlilqalhpv fegdnvilrc
      121 qgkdnknthq kvyykdgkql pnsynlekit vnsvsrdnsk yhctayrkfy ildievtskp
      181 lniqvqelfl hpvlrassst piegspmtlt cetqlspqrp dvqlqfslfr dsqtlglgws
      241 rsprlqipam wtedsgsywc evetvthsik krslrsqirv qrvpvsnvnl eirptggqli
      301 egenmvlics vaqgsgtvtf swhkegrvrs lgrktqrsll aelhvltvke sdagryycaa
      361 dnvhspilst wirvtvripv shpvltfrap rahtvvgdll elhceslrgs ppilyrfyhe
      421 dvtlgnssap sgggasfnls ltaehsgnys cdadnglgaq hshgvslrvt vpvsrpvltl
      481 rapgaqavvg dllelhcesl rgsfpilywf yheddtlgni sahsgggasf nlslttehsg
      541 nysceadngl gaqhskvvtl nvtgtsrnrt gltaagitgl vlsilvlaaa aallhyarar
      601 rkpgglsatg tsshspsecq epsssrpsri dpqepthskp lapmelepmy snvnpgdsnp
      661 iysqiwsiqh tkensancpm mhqeheeltv lyselkkthp ddsageassr graheeddee
      721 nyenvprvll asdh
//
LOCUS       NP_057191               1074 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger RNA-binding protein [Homo sapiens].
ACCESSION   NP_057191
VERSION     NP_057191.2
DBSOURCE    REFSEQ: accession NM_016107.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Zhang,L., He,S., Guan,H., Zhao,Y. and Zhang,D.
  TITLE     Circulating RNA ZFR promotes hepatocellular carcinoma cell
            proliferation and epithelial-mesenchymal transition process through
            miR-624-3p/WEE1 axis
  JOURNAL   Hepatobiliary Pancreat Dis Int 23 (1), 52-63 (2024)
   PUBMED   37516591
  REMARK    GeneRIF: Circulating RNA ZFR promotes hepatocellular carcinoma cell
            proliferation and epithelial-mesenchymal transition process through
            miR-624-3p/WEE1 axis.
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Xu,R., Yin,S., Zheng,M., Pei,X. and Ji,X.
  TITLE     Circular RNA circZFR Promotes Hepatocellular Carcinoma Progression
            by Regulating miR-375/HMGA2 Axis
  JOURNAL   Dig Dis Sci 66 (12), 4361-4373 (2021)
   PUBMED   33433801
  REMARK    GeneRIF: Circular RNA circZFR Promotes Hepatocellular Carcinoma
            Progression by Regulating miR-375/HMGA2 Axis.
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Zhou,M., Yang,Z., Wang,D., Chen,P. and Zhang,Y.
  TITLE     The circular RNA circZFR phosphorylates Rb promoting cervical
            cancer progression by regulating the SSBP1/CDK2/cyclin E1 complex
  JOURNAL   J Exp Clin Cancer Res 40 (1), 48 (2021)
   PUBMED   33516252
  REMARK    GeneRIF: The circular RNA circZFR phosphorylates Rb promoting
            cervical cancer progression by regulating the SSBP1/CDK2/cyclin E1
            complex.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1074)
  AUTHORS   Long,Y., Marian,T.A. and Wei,Z.
  TITLE     ZFR promotes cell proliferation and tumor development in colorectal
            and liver cancers
  JOURNAL   Biochem Biophys Res Commun 513 (4), 1027-1034 (2019)
   PUBMED   31010678
  REMARK    GeneRIF: overexpression of ZFR in CRC and liver cancer cells led to
            accelerated tumor development. Consistently, knockdown of ZFR
            resulted in significantly decelerated tumor development.
REFERENCE   5  (residues 1 to 1074)
  AUTHORS   Xing,X., Wang,H., Zhang,Y., Niu,T., Jiang,Y., Shi,X., Wang,C. and
            Liu,K.
  TITLE     O- glycosylation can regulate the proliferation and migration of
            human retinal microvascular endothelial cells through ZFR in high
            glucose condition
  JOURNAL   Biochem Biophys Res Commun 512 (3), 552-557 (2019)
   PUBMED   30914198
  REMARK    GeneRIF: Hyperglycaemia elevates ZFR in vivo and in vitro. ZFR can
            promote the proliferation and migration of human retinal
            microvascular endothelial cells cultured in high glucose condition.
REFERENCE   6  (residues 1 to 1074)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 1074)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 1074)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1074)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   10 (residues 1 to 1074)
  AUTHORS   Kleines,M., Gartner,A., Ritter,K. and Schaade,L.
  TITLE     Cloning and expression of the human single copy homologue of the
            mouse zinc finger protein zfr
  JOURNAL   Gene 275 (1), 157-162 (2001)
   PUBMED   11574164
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA691446.1, BC017879.1,
            BC030540.1, AJ314790.1, BC051893.1 and AL137258.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 22, 2003 this sequence version replaced NP_057191.1.
            
            Summary: This gene encodes an RNA-binding protein characterized by
            its DZF (domain associated with zinc fingers) domain. The encoded
            protein may play a role in the nucleocytoplasmic shuttling of
            another RNA-binding protein, Staufen homolog 2, in neurons.
            Expression of this gene is regulated through alternative
            polyadenylation that mediates differential microRNA targeting.
            Elevated expression of this gene has been observed in human
            patients with pancreatic cancer and knockdown of this gene may
            result in reduced viability and invasion of pancreatic cancer
            cells. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.68649.1,
                                           SRR1660809.166613.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265069.13/ ENSP00000265069.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.3"
     Protein         1..1074
                     /product="zinc finger RNA-binding protein"
                     /note="M-phase phosphoprotein homolog"
                     /calculated_mol_wt=116881
     Region          120..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KR1.2)"
     Region          331..360
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          333..355
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(340..342,344..345,349,354,389,392..396,398..399)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          349..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KR1.2)"
     Region          382..>551
                     /region_name="PHA03255"
                     /note="BDLF3; Provisional"
                     /db_xref="CDD:165513"
     Region          384..406
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          421..447
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KR1.2)"
     Site            509
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96KR1.2)"
     Site            516
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O88532; propagated from
                     UniProtKB/Swiss-Prot (Q96KR1.2)"
     Region          581..612
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          584..606
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          702..723
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KR1.2)"
     Region          761..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KR1.2)"
     Region          784..1038
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Region          1040..1074
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KR1.2)"
     Site            1054
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96KR1.2)"
     CDS             1..1074
                     /gene="ZFR"
                     /gene_synonym="SPG71; ZFR1"
                     /coded_by="NM_016107.5:83..3307"
                     /db_xref="CCDS:CCDS34139.1"
                     /db_xref="GeneID:51663"
                     /db_xref="HGNC:HGNC:17277"
                     /db_xref="MIM:615635"
ORIGIN      
        1 mipicpvvsf tyvpsrlged akmatgnyfg fthsgaaaaa aaaqysqqpa sgvayshptt
       61 vasytvhqap vaahtvtaay apaaatvava rpapvavaaa ataaayggyp tahtatdygy
      121 tqrqqeappp pppattqnyq dsysyvrsta pavaydskqy yqqptataaa vaaaaqpqps
      181 vaetyyqtap kagysqgatq ytqaqqtrqv taikpatpsp atttfsiypv sstvqpvaaa
      241 atvvpsytqs atysttavty sgtsysgyea avysaassyy qqqqqqqkqa aaaaaaaaat
      301 aawtgttftk kapfqnkqlk pkqppkppqi hycdvckisc agpqtykehl egqkhkkkea
      361 alkasqntss snsstrgtqn qlrcelcdvs ctgadayaah irgakhqkvv klhtklgkpi
      421 pstepnvvsq atsstavsas kptaspssia annctvntss vatssmkglt ttgnsslnst
      481 sntkvsavpt nmaakktstp kinfvggnkl qstgnkaedi kgtecvkstp vtsavqipev
      541 kqdtvsepvt paslaalqsd vqpvghdyve evrndegkvi rfhcklcecs fndpnakemh
      601 lkgrrhrlqy kkkvnpdlqv evkpsirark iqeekmrkqm qkeeywrrre eeerwrmemr
      661 ryeedmywrr meeeqhhwdd rrrmpdggyp hgppgplgll gvrpgmppqp qgpaplrrpd
      721 ssddryvmtk hatiypteee lqavqkivsi teralklvsd slseheknkn kegddkkegg
      781 kdralkgvlr vgvlakglll rgdrnvnlvl lcsekpsktl lsriaenlpk qlavispeky
      841 dikcavseaa iilnscvepk mqvtitltsp iireenmreg dvtsgmvkdp pdvldrqkcl
      901 dalaalrhak wfqaranglq scviiirilr dlcqrvptws dfpswamell vekaissass
      961 pqspgdalrr vfecissgii lkgspglldp cekdpfdtla tmtdqqredi tssaqfalrl
     1021 lafrqihkvl gmdplpqmsq rfnihnnrkr rrdsdgvdgf eaegkkdkkd ydnf
//
LOCUS       NP_938039                187 aa            linear   ROD 27-APR-2025
DEFINITION  T-cell receptor-associated transmembrane adapter 1 [Mus musculus].
ACCESSION   NP_938039
VERSION     NP_938039.3
DBSOURCE    REFSEQ: accession NM_198297.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Koelsch,U., Schraven,B. and Simeoni,L.
  TITLE     SIT and TRIM determine T cell fate in the thymus
  JOURNAL   J Immunol 181 (9), 5930-5939 (2008)
   PUBMED   18941181
  REMARK    GeneRIF: TRIM and Src homology domain-containing tyrosine
            phosphatase 2-interacting transmembrane adaptor protein (SIT)
            regulate cell fate of developing thymocytes and are essential
            regulators of central tolerance.
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Kolsch,U., Arndt,B., Reinhold,D., Lindquist,J.A., Juling,N.,
            Kliche,S., Pfeffer,K., Bruyns,E., Schraven,B. and Simeoni,L.
  TITLE     Normal T-cell development and immune functions in TRIM-deficient
            mice
  JOURNAL   Mol Cell Biol 26 (9), 3639-3648 (2006)
   PUBMED   16612002
  REMARK    GeneRIF: TRIM is dispensable for T-cell development and peripheral
            immune functions.
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Huynh,T., Wurch,A., Bruyns,E., Korinek,V., Schraven,B. and
            Eichmann,K.
  TITLE     Developmentally regulated expression of the transmembrane adaptor
            protein trim in fetal and adult T cells
  JOURNAL   Scand J Immunol 54 (1-2), 146-154 (2001)
   PUBMED   11439161
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Kirchgessner,H., Dietrich,J., Scherer,J., Isomaki,P., Korinek,V.,
            Hilgert,I., Bruyns,E., Leo,A., Cope,A.P. and Schraven,B.
  TITLE     The transmembrane adaptor protein TRIM regulates T cell receptor
            (TCR) expression and TCR-mediated signaling via an association with
            the TCR zeta chain
  JOURNAL   J Exp Med 193 (11), 1269-1284 (2001)
   PUBMED   11390434
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC166114.5.
            
            On Feb 22, 2019 this sequence version replaced NP_938039.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK138735.1, AK030807.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="16"
                     /map="16 30.75 cM"
     Protein         1..187
                     /product="T-cell receptor-associated transmembrane adapter
                     1"
                     /note="T-cell receptor-interacting molecule"
                     /calculated_mol_wt=21199
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UU67.2)"
     Region          18..121
                     /region_name="SIT"
                     /note="SHP2-interacting transmembrane adaptor protein,
                     SIT; pfam15330"
                     /db_xref="CDD:464650"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UU67.2)"
     Region          80..83
                     /region_name="Interaction with PIK3R1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UU67.2)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q6PIZ9; propagated from
                     UniProtKB/Swiss-Prot (Q3UU67.2)"
     Region          117..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UU67.2)"
     CDS             1..187
                     /gene="Trat1"
                     /gene_synonym="C030046M14Rik; Tcrim; Trim"
                     /coded_by="NM_198297.4:143..706"
                     /db_xref="CCDS:CCDS37352.1"
                     /db_xref="GeneID:77647"
                     /db_xref="MGI:MGI:1924897"
ORIGIN      
        1 msgssgcpff lwgllaflgl alvislifni shyvekqrrd eiyrysddyi prvdeyyved
       61 apiygnleni ipepldency eqmkgrpqrs asdpqevaap aqvpaeaqmc yasldhsvkg
      121 krrrprkqnt nvsdrgkdtq vytmdanvsq inmvesfppd nqvveesihd dparlfglir
      181 akrepvi
//
LOCUS       NP_689732                987 aa            linear   PRI 27-APR-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1-like protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_689732
VERSION     NP_689732.2
DBSOURCE    REFSEQ: accession NM_152519.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Smith,E.R., Cayrou,C., Huang,R., Lane,W.S., Cote,J. and
            Lucchesi,J.C.
  TITLE     A human protein complex homologous to the Drosophila MSL complex is
            responsible for the majority of histone H4 acetylation at lysine 16
  JOURNAL   Mol Cell Biol 25 (21), 9175-9188 (2005)
   PUBMED   16227571
  REMARK    Erratum:[Mol Cell Biol. 2006 Jan;26(1):387]
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006994.4, DR002867.1, BC032837.1, AK074441.1, AL133053.1,
            CA393360.1, BQ948513.1, AI289109.1 and BU568066.1.
            
            On Dec 19, 2003 this sequence version replaced NP_689732.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.132720.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281772.14/ ENSP00000281772.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..987
                     /product="KAT8 regulatory NSL complex subunit 1-like
                     protein isoform 1"
                     /note="male-specific lethal 1 homolog; KAT8 regulatory NSL
                     complex subunit 1-like protein; KIAA1267-like"
                     /calculated_mol_wt=112122
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5DTI6; propagated from
                     UniProtKB/Swiss-Prot (A0AUZ9.2)"
     Region          708..738
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0AUZ9.2)"
     Region          795..915
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     Site            859
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (A0AUZ9.2)"
     Region          949..972
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0AUZ9.2)"
     CDS             1..987
                     /gene="KANSL1L"
                     /gene_synonym="C2orf67; MSL1v2"
                     /coded_by="NM_152519.4:291..3254"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33370.1"
                     /db_xref="GeneID:151050"
                     /db_xref="HGNC:HGNC:26310"
                     /db_xref="MIM:613833"
ORIGIN      
        1 mtpalreata kgisfsslps tmesdkmlym esprtvdekl kgdtfsqmlg fptpeptlnt
       61 nfvnlkhfgs pqsskhyqtv flmrsnstln khnenykqkk lgepscnklk nilyngsniq
      121 lskiclshse efikkeplsd ttsqcmkdvq iildsnitkd tnvdkvqlqn ckwyqenall
      181 dkvtdaeikk gllhctqkki vpghsnvpvs ssaaekeeev harllhcvsk qkillsqarr
      241 tqkhlqmlla khvvkhygqq mklsmkhqlp kmktfheptt ilgnslpkct eikpevntlt
      301 aenklwddak ngfarctaae iqrfafsatg llshveegld sdatdsssdd dldeytlrkn
      361 vavncstewk wlvdrarvgs rwtwlqaqis dleckiqqlt dihrqirask givvleecql
      421 pkdilkkqmq fadqaaslni lgnpqvpqec qdpvpeqdfe mspssptlll rniekqsaql
      481 teiinsliap lnlsptsspl sskscshkcl angiyrsase nldelsssss wllnqkhskk
      541 krkdrtrlks ssltfmstsa rtrplqsfhk rklyrlsptf ywtpqtlpsk etaflnttqm
      601 pclqsastws syehnsesyl lrehvselds sfhsvlslps dvplhfhfet llkkteikgn
      661 laenkfvdey iispspvhst lnqwrngysp ickpqirses saqllqgrkk rhlsetalge
      721 rtkleesdfq htesgshsnf tavsnvnvls riqnssrnta rrrlrsessy didnivipms
      781 lvapaklekl qykeiltpsw rmvvlqplde ynlgkeeied lsdevfslrh kkyeereqar
      841 wslweqskwh rrnsrayskn vegqdlllke ypnnfsssqq caaasppglp senqdlcayg
      901 lpslnqsqet kslwwerraf plkgedmaal lcqdekkdqv ersstafhge ifgtsvpeng
      961 hhpkkqsdgm eeyktfglgl tnvkknr
//
LOCUS       NP_062547                822 aa            linear   PRI 27-APR-2025
DEFINITION  sushi domain-containing protein 2 precursor [Homo sapiens].
ACCESSION   NP_062547
VERSION     NP_062547.1
DBSOURCE    REFSEQ: accession NM_019601.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Bai,H., Xian,N., Zhao,F., Zhou,Y. and Qin,S.
  TITLE     The dual role of SUSD2 in cancer development
  JOURNAL   Eur J Pharmacol 977, 176754 (2024)
   PUBMED   38897441
  REMARK    GeneRIF: The dual role of SUSD2 in cancer development.
            Review article
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Wu,Y., Duan,Y., Li,X., Zhao,R., Lan,B., Zhang,X., Wang,X., Chen,H.,
            Feng,S., Liu,Z., Cheng,Y., Xi,L., Wang,Y., Xue,F. and Xuan,C.
  TITLE     CBX8 Together with SET Facilitates Ovarian Carcinoma Growth and
            Metastasis by Suppressing the Transcription of SUSD2
  JOURNAL   Mol Cancer Res 20 (11), 1611-1622 (2022)
   PUBMED   35894945
  REMARK    GeneRIF: CBX8 Together with SET Facilitates Ovarian Carcinoma
            Growth and Metastasis by Suppressing the Transcription of SUSD2.
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Liu,S. and Wen,C.
  TITLE     miR-141-3p promotes retinoblastoma progression via inhibiting sushi
            domain-containing protein 2
  JOURNAL   Bioengineered 13 (3), 7410-7424 (2022)
   PUBMED   35259051
  REMARK    GeneRIF: miR-141-3p promotes retinoblastoma progression via
            inhibiting sushi domain-containing protein 2.
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Xia,L., Zhu,G., Huang,H., He,Y. and Liu,X.
  TITLE     LncRNA small nucleolar RNA host gene 16 (SNHG16) silencing protects
            lipopolysaccharide (LPS)-induced cell injury in human lung
            fibroblasts WI-38 through acting as miR-141-3p sponge
  JOURNAL   Biosci Biotechnol Biochem 85 (5), 1077-1087 (2021)
   PUBMED   33836533
  REMARK    GeneRIF: LncRNA small nucleolar RNA host gene 16 (SNHG16) silencing
            protects lipopolysaccharide (LPS)-induced cell injury in human lung
            fibroblasts WI-38 through acting as miR-141-3p sponge.
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Sang,J., Li,X., Lv,L., Zhang,C., Zhang,X. and Li,G.
  TITLE     Circ-TOP2A acts as a ceRNA for miR-346 and contributes to glioma
            progression via the modulation of sushi domain-containing 2
  JOURNAL   Mol Med Rep 23 (4) (2021)
   PUBMED   33537815
  REMARK    GeneRIF: CircTOP2A acts as a ceRNA for miR346 and contributes to
            glioma progression via the modulation of sushi domaincontaining 2.
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Sivasubramaniyan,K., Harichandan,A., Schumann,S., Sobiesiak,M.,
            Lengerke,C., Maurer,A., Kalbacher,H. and Buhring,H.J.
  TITLE     Prospective isolation of mesenchymal stem cells from human bone
            marrow using novel antibodies directed against Sushi domain
            containing 2
  JOURNAL   Stem Cells Dev 22 (13), 1944-1954 (2013)
   PUBMED   23406305
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Watson,A.P., Evans,R.L. and Egland,K.A.
  TITLE     Multiple functions of sushi domain containing 2 (SUSD2) in breast
            tumorigenesis
  JOURNAL   Mol Cancer Res 11 (1), 74-85 (2013)
   PUBMED   23131994
  REMARK    GeneRIF: Authors found significantly fewer CD4 tumor infiltrating
            lymphocytes in breast tumors expressing Susd2.
REFERENCE   8  (residues 1 to 822)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 822)
  AUTHORS   Liu,T., Qian,W.J., Gritsenko,M.A., Camp,D.G. 2nd, Monroe,M.E.,
            Moore,R.J. and Smith,R.D.
  TITLE     Human plasma N-glycoproteome analysis by immunoaffinity
            subtraction, hydrazide chemistry, and mass spectrometry
  JOURNAL   J Proteome Res 4 (6), 2070-2080 (2005)
   PUBMED   16335952
REFERENCE   10 (residues 1 to 822)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC033107.1 and BI822588.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033107.1, SRR1803615.96957.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358321.4/ ENSP00000351075.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.23"
     Protein         1..822
                     /product="sushi domain-containing protein 2 precursor"
                     /note="Sushi domain (SCR repeat) containing; sushi
                     domain-containing protein 2; testicular tissue protein Li
                     190"
                     /calculated_mol_wt=87570
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2656
     mat_peptide     28..822
                     /product="Sushi domain-containing protein 2.
                     /id=PRO_0000249439"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGT4.1)"
                     /calculated_mol_wt=87570
     Region          29..64
                     /region_name="Somatomedin_B"
                     /note="Somatomedin B domain; pfam01033"
                     /db_xref="CDD:460034"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UGT4.1)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UGT4.1)"
     Region          289..429
                     /region_name="AMOP"
                     /note="AMOP domain; pfam03782"
                     /db_xref="CDD:461048"
     Region          448..613
                     /region_name="VWD"
                     /note="von Willebrand factor type D domain; pfam00094"
                     /db_xref="CDD:459671"
     Site            522
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9UGT4.1)"
     Region          725..779
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(735,752)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Site            786..806
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGT4.1)"
     CDS             1..822
                     /gene="SUSD2"
                     /gene_synonym="BK65A6.2; W5C5"
                     /coded_by="NM_019601.4:34..2502"
                     /db_xref="CCDS:CCDS13824.1"
                     /db_xref="GeneID:56241"
                     /db_xref="HGNC:HGNC:30667"
                     /db_xref="MIM:615825"
ORIGIN      
        1 mkpallpwal lllatalgpg pgptadaqes csmrcgaldg pcschptcsg lgtccldfrd
       61 fcleilpysg smmggkdfvv rhfkmssptd asvicrfkds iqtlghvdss gqvhcvspll
      121 yesgripftv sldnghsfpr agtwlavhpn kvsmmeksel vnetrwqyyg tantsgnlsl
      181 twhvkslptq titielwgye etgmpysqew takwsylypl athipnsgsf tftpkpapps
      241 yqrwrvgalr iidsknyagq kdvqalwtnd halawhlsdd fredpvawar tqcqaweele
      301 dqlpnfleel pdcpctltqa radsgrfftd ygcdmeqgsv ctyhpgavhc vrsvqaslry
      361 gsgqqccyta dgtqlltads sggstpdrgh dwgappfrtp prvpsmshwl ydvlsfyycc
      421 lwapdcprym qrrpsndcrn yrpprlasaf gdphfvtfdg tnftfngrge yvlleaaltd
      481 lrvqaraqpg tmsngtetrg tgltavavqe gnsdvvevrl anrtgglevl lnqevlsfte
      541 qswmdlkgmf lsvaagdrvs imlasgagle vsvqgpflsv svllpekflt hthgllgtln
      601 ndptddftlh sgrvlppgts pqelflfgan wtvhnassll tydswflvhn flyqpkhdpt
      661 feplfpsett lnpslaqeaa klcgddhfcn fdvaatgsls tgtatrvahq lhqrrmqslq
      721 pvvscgwlap ppngqkegnr ylagstiyfh cdngyslaga etstcqadgt wssptpkcqp
      781 grsyavllgi ifgglavvaa valvyvllrr rkgnthvwga qp
//
LOCUS       NP_001351257             402 aa            linear   ROD 27-APR-2025
DEFINITION  malonyl-CoA decarboxylase, mitochondrial isoform 2 [Mus musculus].
ACCESSION   NP_001351257 XP_006531283
VERSION     NP_001351257.1
DBSOURCE    REFSEQ: accession NM_001364328.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Li,C., Zhang,Y., Shen,J., Bao,H., Zhao,Y., Li,D., Li,S., Liu,Y.,
            Yang,J., Zhou,Z., Gao,K., Zhao,L., Pei,Y., Lu,Y., Pan,Z. and Cai,B.
  TITLE     Cfp1 Controls Cardiomyocyte Maturation by Modifying Histone H3K4me3
            of Structural, Metabolic, and Contractile Related Genes
  JOURNAL   Adv Sci (Weinh) 11 (11), e2305992 (2024)
   PUBMED   38196272
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Guilherme,A., Rowland,L.A., Wetoska,N., Tsagkaraki,E., Santos,K.B.,
            Bedard,A.H., Henriques,F., Kelly,M., Munroe,S., Pedersen,D.J.,
            Ilkayeva,O.R., Koves,T.R., Tauer,L., Pan,M., Han,X., Kim,J.K.,
            Newgard,C.B., Muoio,D.M. and Czech,M.P.
  TITLE     Acetyl-CoA carboxylase 1 is a suppressor of the adipocyte
            thermogenic program
  JOURNAL   Cell Rep 42 (5), 112488 (2023)
   PUBMED   37163372
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Fisher-Wellman,K.H., Draper,J.A., Davidson,M.T., Williams,A.S.,
            Narowski,T.M., Slentz,D.H., Ilkayeva,O.R., Stevens,R.D.,
            Wagner,G.R., Najjar,R., Hirschey,M.D., Thompson,J.W., Olson,D.P.,
            Kelly,D.P., Koves,T.R., Grimsrud,P.A. and Muoio,D.M.
  TITLE     Respiratory Phenomics across Multiple Models of Protein
            Hyperacylation in Cardiac Mitochondria Reveals a Marginal Impact on
            Bioenergetics
  JOURNAL   Cell Rep 26 (6), 1557-1572 (2019)
   PUBMED   30726738
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Zhou,L., Dai,H., Wu,J., Zhou,M., Yuan,H., Du,J., Yang,L., Wu,X.,
            Xu,H., Hua,Y., Xu,J., Zheng,L. and Shen,B.
  TITLE     Role of FEN1 S187 phosphorylation in counteracting oxygen-induced
            stress and regulating postnatal heart development
  JOURNAL   FASEB J 31 (1), 132-147 (2017)
   PUBMED   27694478
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Ussher,J.R., Fillmore,N., Keung,W., Zhang,L., Mori,J., Sidhu,V.K.,
            Fukushima,A., Gopal,K., Lopaschuk,D.G., Wagg,C.S., Jaswal,J.S.,
            Dyck,J.R. and Lopaschuk,G.D.
  TITLE     Genetic and Pharmacological Inhibition of Malonyl CoA Decarboxylase
            Does Not Exacerbate Age-Related Insulin Resistance in Mice
  JOURNAL   Diabetes 65 (7), 1883-1891 (2016)
   PUBMED   27207536
  REMARK    GeneRIF: Decreased fat oxidation in MCD(-/-) mice resulted in the
            accumulation of lipid intermediates in peripheral tissues, but this
            was not associated with a worsening of age-associated insulin
            resistance and, conversely, improved longevity.
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Sutendra,G., Bonnet,S., Rochefort,G., Haromy,A., Folmes,K.D.,
            Lopaschuk,G.D., Dyck,J.R. and Michelakis,E.D.
  TITLE     Fatty acid oxidation and malonyl-CoA decarboxylase in the vascular
            remodeling of pulmonary hypertension
  JOURNAL   Sci Transl Med 2 (44), 44ra58 (2010)
   PUBMED   20702857
  REMARK    GeneRIF: This study of fatty acid oxidation and malonyl-CoA
            decarboxylase identifies a critical role for metabolism in both the
            normal pulmonary circulation (hypoxic pulmonary vasoconstriction)
            and pulmonary hypertension
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Ussher,J.R., Koves,T.R., Jaswal,J.S., Zhang,L., Ilkayeva,O.,
            Dyck,J.R., Muoio,D.M. and Lopaschuk,G.D.
  TITLE     Insulin-stimulated cardiac glucose oxidation is increased in
            high-fat diet-induced obese mice lacking malonyl CoA decarboxylase
  JOURNAL   Diabetes 58 (8), 1766-1775 (2009)
   PUBMED   19478144
  REMARK    GeneRIF: Mcd deficiency is not detrimental to the heart in obesity
            in mice.
            Erratum:[Diabetes. 2009 Oct;58(10):2425]
REFERENCE   8  (residues 1 to 402)
  AUTHORS   Koves,T.R., Ussher,J.R., Noland,R.C., Slentz,D., Mosedale,M.,
            Ilkayeva,O., Bain,J., Stevens,R., Dyck,J.R., Newgard,C.B.,
            Lopaschuk,G.D. and Muoio,D.M.
  TITLE     Mitochondrial overload and incomplete fatty acid oxidation
            contribute to skeletal muscle insulin resistance
  JOURNAL   Cell Metab 7 (1), 45-56 (2008)
   PUBMED   18177724
REFERENCE   9  (residues 1 to 402)
  AUTHORS   Harada,N., Oda,Z., Hara,Y., Fujinami,K., Okawa,M., Ohbuchi,K.,
            Yonemoto,M., Ikeda,Y., Ohwaki,K., Aragane,K., Tamai,Y. and
            Kusunoki,J.
  TITLE     Hepatic de novo lipogenesis is present in liver-specific
            ACC1-deficient mice
  JOURNAL   Mol Cell Biol 27 (5), 1881-1888 (2007)
   PUBMED   17210641
  REMARK    Erratum:[Mol Cell Biol. 2007 May;27(9):3556]
REFERENCE   10 (residues 1 to 402)
  AUTHORS   Dyck,J.R., Hopkins,T.A., Bonnet,S., Michelakis,E.D., Young,M.E.,
            Watanabe,M., Kawase,Y., Jishage,K. and Lopaschuk,G.D.
  TITLE     Absence of malonyl coenzyme A decarboxylase in mice increases
            cardiac glucose oxidation and protects the heart from ischemic
            injury
  JOURNAL   Circulation 114 (16), 1721-1728 (2006)
   PUBMED   17030679
  REMARK    GeneRIF: In vivo and ex vivo cardiac function is similar in
            wild-type and mcd-deficient mice; however, deletion of MCD markedly
            increases glucose oxidation and improves functional recovery of the
            heart after ischemia.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC166781.7.
            
            On Jun 14, 2018 this sequence version replaced XP_006531283.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.2826523.1, FO711520.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 67.64 cM"
     Protein         1..402
                     /product="malonyl-CoA decarboxylase, mitochondrial isoform
                     2"
                     /EC_number="4.1.1.9"
                     /note="malonyl-CoA decarboxylase, mitochondrial"
                     /calculated_mol_wt=44254
     Region          94..175
                     /region_name="MCD_N"
                     /note="Malonyl-CoA decarboxylase N-terminal domain;
                     pfam17408"
                     /db_xref="CDD:465421"
     Region          <182..365
                     /region_name="MCD"
                     /note="Malonyl-CoA decarboxylase C-terminal domain;
                     pfam05292"
                     /db_xref="CDD:461613"
     CDS             1..402
                     /gene="Mlycd"
                     /gene_synonym="Mcd"
                     /coded_by="NM_001364328.1:53..1261"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:56690"
                     /db_xref="MGI:MGI:1928485"
ORIGIN      
        1 mrglgpglra rrllplrspp rppgprgrrl cgglaasamd ellrravppt payelrektp
       61 apaegqcadf vsfygglaea sqraellgrl aqgfgvdhgq vaeqsagvlq lrqqareaav
      121 llqaedrlry alvpryrglf hhiskldggv rflvqlradl leaqalklve gphvrgivke
      181 cppteteern riaaaifysi sltqqglqgv elgtflikrv vkelqkefpq lgafsslspi
      241 pgftkwllgl lnvqgkehgr nelftdsecq eisavtgnpv heslkgflss gewvkseklt
      301 qalqgplmrl cawylygekh rgyalnpvan fhlqngavmw rinwmadssl kgltsscglm
      361 vnyryyleet gpnsisylgs knikaseqil slvaqfqnns kl
//
LOCUS       NP_079217                417 aa            linear   PRI 27-APR-2025
DEFINITION  trafficking protein particle complex subunit 13 isoform 2 [Homo
            sapiens].
ACCESSION   NP_079217
VERSION     NP_079217.2
DBSOURCE    REFSEQ: accession NM_024941.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Gupta,R., Somyajit,K., Narita,T., Maskey,E., Stanlie,A., Kremer,M.,
            Typas,D., Lammers,M., Mailand,N., Nussenzweig,A., Lukas,J. and
            Choudhary,C.
  TITLE     DNA Repair Network Analysis Reveals Shieldin as a Key Regulator of
            NHEJ and PARP Inhibitor Sensitivity
  JOURNAL   Cell 173 (4), 972-988 (2018)
   PUBMED   29656893
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Ramirez-Peinado,S., Ignashkova,T.I., van Raam,B.J., Baumann,J.,
            Sennott,E.L., Gendarme,M., Lindemann,R.K., Starnbach,M.N. and
            Reiling,J.H.
  TITLE     TRAPPC13 modulates autophagy and the response to Golgi stress
  JOURNAL   J Cell Sci 130 (14), 2251-2265 (2017)
   PUBMED   28536105
  REMARK    GeneRIF: Results lend support for the existence of a mammalian
            TRAPPIII complex containing TRAPPC13, which is important for
            autophagic flux under certain stress conditions.
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Kim,J.J., Lipatova,Z. and Segev,N.
  TITLE     TRAPP Complexes in Secretion and Autophagy
  JOURNAL   Front Cell Dev Biol 4, 20 (2016)
   PUBMED   27066478
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Bassik,M.C., Kampmann,M., Lebbink,R.J., Wang,S., Hein,M.Y.,
            Poser,I., Weibezahn,J., Horlbeck,M.A., Chen,S., Mann,M.,
            Hyman,A.A., Leproust,E.M., McManus,M.T. and Weissman,J.S.
  TITLE     A systematic mammalian genetic interaction map reveals pathways
            underlying ricin susceptibility
  JOURNAL   Cell 152 (4), 909-922 (2013)
   PUBMED   23394947
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Choi,C., Davey,M., Schluter,C., Pandher,P., Fang,Y., Foster,L.J.
            and Conibear,E.
  TITLE     Organization and assembly of the TRAPPII complex
  JOURNAL   Traffic 12 (6), 715-725 (2011)
   PUBMED   21453443
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB145758.1, AK023673.1, BC117128.1, AL713699.1, N67829.1,
            BM664695.1 and AC008560.6.
            
            On May 23, 2007 this sequence version replaced NP_079217.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1,
            resulting in a shorter protein (isoform 2).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.664281.1, AK023673.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399438.8/ ENSP00000382367.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..417
                     /product="trafficking protein particle complex subunit 13
                     isoform 2"
                     /note="UPF0533 protein C5orf44; Trs65-related;
                     REV7-interacting novel NHEJ regulator 1; trafficking
                     protein particle complex 13"
                     /calculated_mol_wt=46393
     Region          65..298
                     /region_name="DUF974"
                     /note="Protein of unknown function (DUF974); pfam06159"
                     /db_xref="CDD:461841"
     CDS             1..417
                     /gene="TRAPPC13"
                     /gene_synonym="C5orf44; SHLD3"
                     /coded_by="NM_024941.4:35..1288"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47222.1"
                     /db_xref="GeneID:80006"
                     /db_xref="HGNC:HGNC:25828"
ORIGIN      
        1 mevnppkqeh llalkvmrlt kptlftnipv tceekdlpgd lfnqlmrddp stvngaevlm
       61 lgemltlpqn fgniflgetf ssyisvhnds nqvvkdilvk adlqtssqrl nlsasnaava
      121 elkpdccidd vihhevkeig thilvcavsy ttqagekmyf rkffkfqvlk pldvktkfyn
      181 aesdlssvtd evfleaqiqn mttspmfmek vslepsimyn vtelnsvsqa gecvstfgsr
      241 aylqpmdtrq ylyclkpkne faekagiikg vtvigkldiv wktnlgergr lqtsqlqrma
      301 pgygdvrlsl eaipdtvnle epfhitckit ncsertmdlv lemcntnsih wcgisgrqlg
      361 klhpssslcl altllssvqg lqsisglrlt dtflkrtyey ddiaqvcvvs saikves
//
LOCUS       NP_001355969             456 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 9 isoform 9 [Homo sapiens].
ACCESSION   NP_001355969
VERSION     NP_001355969.1
DBSOURCE    REFSEQ: accession NM_001369040.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Ma,X., Yan,W., Xu,P., Ma,L., Zan,Y., Huang,L., Wang,G., Liu,L. and
            Hui,W.
  TITLE     LncRNA-p21 suppresses cell proliferation and induces apoptosis in
            gastric cancer by sponging miR-514b-3p and up-regulating ARHGEF9
            expression
  JOURNAL   Biol Chem 403 (10), 945-958 (2022)
   PUBMED   35947460
  REMARK    GeneRIF: LncRNA-p21 suppresses cell proliferation and induces
            apoptosis in gastric cancer by sponging miR-514b-3p and
            up-regulating ARHGEF9 expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Yang,H., Liao,H., Gan,S., Xiao,T. and Wu,L.
  TITLE     ARHGEF9 gene variant leads to developmental and epileptic
            encephalopathy: Genotypic phenotype analysis and treatment
            exploration
  JOURNAL   Mol Genet Genomic Med 10 (7), e1967 (2022)
   PUBMED   35638461
  REMARK    GeneRIF: ARHGEF9 gene variant leads to developmental and epileptic
            encephalopathy: Genotypic phenotype analysis and treatment
            exploration.
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Hines,D.J., Contreras,A., Garcia,B., Barker,J.S., Boren,A.J.,
            Moufawad El Achkar,C., Moss,S.J. and Hines,R.M.
  TITLE     Human ARHGEF9 intellectual disability syndrome is phenocopied by a
            mutation that disrupts collybistin binding to the GABAA receptor
            alpha2 subunit
  JOURNAL   Mol Psychiatry 27 (3), 1729-1741 (2022)
   PUBMED   35169261
  REMARK    GeneRIF: Human ARHGEF9 intellectual disability syndrome is
            phenocopied by a mutation that disrupts collybistin binding to the
            GABAA receptor alpha2 subunit.
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Ghesh,L., Besnard,T., Nizon,M., Trochu,E., Landeau-Trottier,G.,
            Breheret,F., Thauvin-Robinet,C., Bruel,A.L., Kuentz,P., Coubes,C.,
            Cuisset,L., Mignot,C., Keren,B., Bezieau,S. and Cogne,B.
  TITLE     Loss-of-function variants in ARHGEF9 are associated with an
            X-linked intellectual disability dominant disorder
  JOURNAL   Hum Mutat 42 (5), 498-505 (2021)
   PUBMED   33600053
  REMARK    GeneRIF: Loss-of-function variants in ARHGEF9 are associated with
            an X-linked intellectual disability dominant disorder.
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Scala,M., Zonneveld-Huijssoon,E., Brienza,M., Mecarelli,O., van der
            Hout,A.H., Zambrelli,E., Turner,K., Zara,F., Peron,A., Vignoli,A.
            and Striano,P.
  TITLE     De novo ARHGEF9 missense variants associated with
            neurodevelopmental disorder in females: expanding the genotypic and
            phenotypic spectrum of ARHGEF9 disease in females
  JOURNAL   Neurogenetics 22 (1), 87-94 (2021)
   PUBMED   32939676
  REMARK    GeneRIF: De novo ARHGEF9 missense variants associated with
            neurodevelopmental disorder in females: expanding the genotypic and
            phenotypic spectrum of ARHGEF9 disease in females.
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Harrington,A.W., Kim,J.Y. and Yoon,S.O.
  TITLE     Activation of Rac GTPase by p75 is necessary for c-jun N-terminal
            kinase-mediated apoptosis
  JOURNAL   J Neurosci 22 (1), 156-166 (2002)
   PUBMED   11756498
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Grosskreutz,Y., Hermann,A., Kins,S., Fuhrmann,J.C., Betz,H. and
            Kneussel,M.
  TITLE     Identification of a gephyrin-binding motif in the GDP/GTP exchange
            factor collybistin
  JOURNAL   Biol Chem 382 (10), 1455-1462 (2001)
   PUBMED   11727829
  REMARK    GeneRIF: Here we identified residues critical for interaction with
            gephyrin in the linker region between the SH3 and the DH domains of
            collybistin.
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Kins,S., Betz,H. and Kirsch,J.
  TITLE     Collybistin, a newly identified brain-specific GEF, induces
            submembrane clustering of gephyrin
  JOURNAL   Nat Neurosci 3 (1), 22-29 (2000)
   PUBMED   10607391
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Reid,T., Bathoorn,A., Ahmadian,M.R. and Collard,J.G.
  TITLE     Identification and characterization of hPEM-2, a guanine nucleotide
            exchange factor specific for Cdc42
  JOURNAL   J Biol Chem 274 (47), 33587-33593 (1999)
   PUBMED   10559246
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Balint,B. and Thomas,R.
  TITLE     Hereditary Hyperekplexia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL451106.9, AL355142.11 and
            AL391277.16.
            
            Summary: The protein encoded by this gene is a Rho-like GTPase that
            switches between the active (GTP-bound) state and inactive
            (GDP-bound) state to regulate CDC42 and other genes. This
            brain-specific protein also acts as an adaptor protein for the
            recruitment of gephyrin and together these proteins facilitate
            receceptor recruitement in GABAnergic and glycinergic synapses.
            Defects in this gene are the cause of startle disease with epilepsy
            (STHEE), also known as hyperekplexia with epilepsy, as well as
            several other types of cognitive disability. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.120764.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq11.1"
     Protein         1..456
                     /product="rho guanine nucleotide exchange factor 9 isoform
                     9"
                     /note="hPEM-2 collybistin; rho guanine nucleotide exchange
                     factor 9; PEM-2 homolog; rac/Cdc42 guanine nucleotide
                     exchange factor 9; Cdc42 guanine nucleotide exchange
                     factor (GEF) 9"
                     /calculated_mol_wt=54139
     Region          47..226
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; smart00325"
                     /db_xref="CDD:214619"
     Site            order(50,54,149,176..177,180..181,183..184,187..188,
                     191..192,195,221,225)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          231..370
                     /region_name="PH_Collybistin_ASEF"
                     /note="Collybistin/APC-stimulated guanine nucleotide
                     exchange factor pleckstrin homology (PH) domain; cd01224"
                     /db_xref="CDD:269931"
     CDS             1..456
                     /gene="ARHGEF9"
                     /gene_synonym="COLLYBISTIN; DEE8; EIEE8; HPEM-2; PEM-2;
                     PEM2"
                     /coded_by="NM_001369040.1:564..1934"
                     /note="isoform 9 is encoded by transcript variant 22"
                     /db_xref="GeneID:23229"
                     /db_xref="HGNC:HGNC:14561"
                     /db_xref="MIM:300429"
ORIGIN      
        1 mydlwvnqed eveegpsdvq nghldpnsdc lclgrplqnr dqmranvine imsterhyik
       61 hlkdicegyl kqcrkrrdmf sdeqlkvifg niediyrfqm gfvrdlekqy nnddphlsei
      121 gpcflehqdg fwiyseycnn hldacmelsk lmkdsryqhf feacrllqqm idiaidgfll
      181 tpvqkickyp lqlaellkyt aqdhsdyryv aaalavmrnv tqqinerkrr lenidkiaqw
      241 qasvldwege dildrsseli ytgemawiyq pygrnqqrvf flfdhqmvlc kkdlirrdil
      301 yykgridmdk yevvdiedgr dddfnvsmkn afklhnkete eihlffakkl eekirwlraf
      361 reerkmvqed ekigfeisen qkrqaamtvr kvpkqkgvns arsvppsypp pqdplnhgqy
      421 lvpdgiaqsq vfeftepkrs qspfwqnfsr ltpfkk
//
LOCUS       NP_005853               1258 aa            linear   PRI 27-APR-2025
DEFINITION  cohesin subunit SA-1 [Homo sapiens].
ACCESSION   NP_005853
VERSION     NP_005853.2
DBSOURCE    REFSEQ: accession NM_005862.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1258)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   2  (residues 1 to 1258)
  AUTHORS   Alonso-Gil,D., Cuadrado,A., Gimenez-Llorente,D.,
            Rodriguez-Corsino,M. and Losada,A.
  TITLE     Different NIPBL requirements of cohesin-STAG1 and cohesin-STAG2
  JOURNAL   Nat Commun 14 (1), 1326 (2023)
   PUBMED   36898992
  REMARK    GeneRIF: Different NIPBL requirements of cohesin-STAG1 and
            cohesin-STAG2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1258)
  AUTHORS   Saitta,C., Rebellato,S., Bettini,L.R., Giudici,G., Panini,N.,
            Erba,E., Massa,V., Auer,F., Friedrich,U., Hauer,J., Biondi,A.,
            Fazio,G. and Cazzaniga,G.
  TITLE     Potential role of STAG1 mutations in genetic predisposition to
            childhood hematological malignancies
  JOURNAL   Blood Cancer J 12 (6), 88 (2022)
   PUBMED   35654786
  REMARK    GeneRIF: Potential role of STAG1 mutations in genetic
            predisposition to childhood hematological malignancies.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1258)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1258)
  AUTHORS   Richart,L., Lapi,E., Pancaldi,V., Cuenca-Ardura,M., Pau,E.C.,
            Madrid-Mencia,M., Neyret-Kahn,H., Radvanyi,F., Rodriguez,J.A.,
            Cuartero,Y., Serra,F., Le Dily,F., Valencia,A., Marti-Renom,M.A.
            and Real,F.X.
  TITLE     STAG2 loss-of-function affects short-range genomic contacts and
            modulates the basal-luminal transcriptional program of bladder
            cancer cells
  JOURNAL   Nucleic Acids Res 49 (19), 11005-11021 (2021)
   PUBMED   34648034
  REMARK    GeneRIF: STAG2 loss-of-function affects short-range genomic
            contacts and modulates the basal-luminal transcriptional program of
            bladder cancer cells.
REFERENCE   6  (residues 1 to 1258)
  AUTHORS   Anazawa,Y., Arakawa,H., Nakagawa,H. and Nakamura,Y.
  TITLE     Identification of STAG1 as a key mediator of a p53-dependent
            apoptotic pathway
  JOURNAL   Oncogene 23 (46), 7621-7627 (2004)
   PUBMED   15361841
  REMARK    GeneRIF: STAG1, a novel transcriptional target for p53, mediates
            p53-dependent apoptosis, and might be a good candidate for
            next-generation gene therapy in cancer.
REFERENCE   7  (residues 1 to 1258)
  AUTHORS   Prieto,I., Pezzi,N., Buesa,J.M., Kremer,L., Barthelemy,I.,
            Carreiro,C., Roncal,F., Martinez,A., Gomez,L., Fernandez,R.,
            Martinez-A,C. and Barbero,J.L.
  TITLE     STAG2 and Rad21 mammalian mitotic cohesins are implicated in
            meiosis
  JOURNAL   EMBO Rep 3 (6), 543-550 (2002)
   PUBMED   12034751
REFERENCE   8  (residues 1 to 1258)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   9  (residues 1 to 1258)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   10 (residues 1 to 1258)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC064699.1, BC017735.1 and
            AC069524.18.
            
            On Apr 6, 2005 this sequence version replaced NP_005853.1.
            
            Summary: This gene is a member of the SCC3 family and is expressed
            in the nucleus. It encodes a component of cohesin, a multisubunit
            protein complex that provides sister chromatid cohesion along the
            length of a chromosome from DNA replication through prophase and
            prometaphase, after which it is dissociated in preparation for
            segregation during anaphase. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.23828.1,
                                           SRR7346977.2569678.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000383202.7/ ENSP00000372689.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..1258
                     /product="cohesin subunit SA-1"
                     /note="nuclear protein stromal antigen 1; SCC3 homolog 1;
                     sister chromatid cohesion 3 homolog A"
                     /calculated_mol_wt=144297
     Region          1..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVM7.3)"
     Region          12..>398
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8WVM7.3)"
     Region          160..273
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WVM7.3)"
     Region          1055..1096
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVM7.3)"
     Site            1062
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8WVM7.3)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D3E6; propagated from
                     UniProtKB/Swiss-Prot (Q8WVM7.3)"
     Site            1093
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WVM7.3)"
     Region          1129..1148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVM7.3)"
     CDS             1..1258
                     /gene="STAG1"
                     /gene_synonym="MRD47; SA1; SCC3A"
                     /coded_by="NM_005862.3:268..4044"
                     /db_xref="CCDS:CCDS3090.1"
                     /db_xref="GeneID:10274"
                     /db_xref="HGNC:HGNC:11354"
                     /db_xref="MIM:604358"
ORIGIN      
        1 mitselpvlq dstnettahs dagseleete vkgkrkrgrp grppstnkkp rkspgeksri
       61 eagirgagrg ranghpqqng egepvtlfev vklgksamqs vvddwiesyk qdrdialldl
      121 inffiqcsgc rgtvriemfr nmqnaeiirk mteefdedsg dypltmpgpq wkkfrsnfce
      181 figvlirqcq ysiiydeymm dtvislltgl sdsqvrafrh tstlaamklm talvnvalnl
      241 sihqdntqrq yeaernkmig kranerlell lqkrkelqen qdeienmmns ifkgifvhry
      301 rdaiaeirai cieeigvwmk mysdaflnds ylkyvgwtlh drqgevrlkc lkalqslytn
      361 relfpklelf tnrfkdrivs mtldkeydva veairlvtli lhgseealsn edcenvyhlv
      421 ysahrpvava ageflhkklf srhdpqaeea lakrrgrnsp ngnlirmlvl ffleselheh
      481 aaylvdslwe ssqellkdwe cmtellleep vqgeeamsdr qesalielmv ctirqaaeah
      541 ppvgrgtgkr vltakerktq iddrnklteh fiitlpmlls kysadaekva nllqipqyfd
      601 leiystgrme khldallkqi kfvvekhves dvleacskty silcseeyti qnrvdiarsq
      661 lidefvdrfn hsvedllqeg eeaddddiyn vlstlkrlts fhnahdltkw dlfgncyrll
      721 ktgiehgamp eqivvqalqc shysilwqlv kitdgspske dllvlrktvk sflavcqqcl
      781 snvntpvkeq afmllcdllm ifshqlmtgg reglqplvfn pdtglqsell sfvmdhvfid
      841 qdeenqsmeg deedeankie alhkrrnlla afskliiydi vdmhaaadif khymkyyndy
      901 gdiiketlsk trqidkiqca ktlilslqql fnelvqeqgp nldrtsahvs gikelarrfa
      961 ltfgldqikt reavatlhkd giefafkyqn qkgqeypppn laflevlsef sskllrqdkk
     1021 tvhsylekfl teqmmerred vwlplisyrn slvtggeddr msvnsgssss ktssvrnkkg
     1081 rpplhkkrve desldntwln rtdtmiqtpg plpapqltst vlrensrpmg dqiqepeseh
     1141 gsepdflhnp qmqiswlgqp kledlnrkdr tgmnymkvrt gvrhavrglm eedaepifed
     1201 vmmssrsqle dmneefedtm vidlppsrnr reraelrpdf fdsaaiiedd sgfgmpmf
//
LOCUS       NP_032829                823 aa            linear   ROD 27-APR-2025
DEFINITION  high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic
            phosphodiesterase 8A [Mus musculus].
ACCESSION   NP_032829 XP_917087
VERSION     NP_032829.1
DBSOURCE    REFSEQ: accession NM_008803.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Qiu,N.Z., Hou,H.M., Guo,T.Y., Lv,Y.L., Zhou,Y., Zhang,F.F.,
            Zhang,F., Wang,X.D., Chen,W., Gao,Y.F., Chen,M.H., Zhang,X.H.,
            Zhang,H.T. and Wang,H.
  TITLE     Phosphodiesterase 8 (PDE8): Distribution and Cellular Expression
            and Association with Alzheimer's Disease
  JOURNAL   Neurochem Res 49 (8), 1993-2004 (2024)
   PUBMED   38782837
  REMARK    GeneRIF: Phosphodiesterase 8 (PDE8): Distribution and Cellular
            Expression and Association with Alzheimer's Disease.
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Qasim,H., Rajaei,M., Xu,Y., Reyes-Alcaraz,A., Abdelnasser,H.Y.,
            Stewart,M.D., Lahiri,S.K., Wehrens,X.H.T. and McConnell,B.K.
  TITLE     AKAP12 Upregulation Associates With PDE8A to Accelerate Cardiac
            Dysfunction
  JOURNAL   Circ Res 134 (8), 1006-1022 (2024)
   PUBMED   38506047
  REMARK    GeneRIF: AKAP12 Upregulation Associates With PDE8A to Accelerate
            Cardiac Dysfunction.
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 823)
  AUTHORS   Basole,C.P., Nguyen,R.K., Lamothe,K., Vang,A., Clark,R.,
            Baillie,G.S., Epstein,P.M. and Brocke,S.
  TITLE     PDE8 controls CD4+ T cell motility through the PDE8A-Raf-1 kinase
            signaling complex
  JOURNAL   Cell Signal 40, 62-72 (2017)
   PUBMED   28851628
  REMARK    GeneRIF: our studies demonstrate that PDE8A inhibition by enzymatic
            inhibitors or PDE8A-Raf-1 kinase complex disruptors decreases Teff
            cell adhesion and migration under flow, and represents a novel
            approach to target T cells in inflammation
REFERENCE   5  (residues 1 to 823)
  AUTHORS   Isidori,A.M., Cornacchione,M., Barbagallo,F., Di Grazia,A.,
            Barrios,F., Fassina,L., Monaco,L., Giannetta,E., Gianfrilli,D.,
            Garofalo,S., Zhang,X., Chen,X., Xiang,Y.K., Lenzi,A., Pellegrini,M.
            and Naro,F.
  TITLE     Inhibition of type 5 phosphodiesterase counteracts beta2-adrenergic
            signalling in beating cardiomyocytes
  JOURNAL   Cardiovasc Res 106 (3), 408-420 (2015)
   PUBMED   25852085
REFERENCE   6  (residues 1 to 823)
  AUTHORS   Omori,K. and Kotera,J.
  TITLE     Overview of PDEs and their regulation
  JOURNAL   Circ Res 100 (3), 309-327 (2007)
   PUBMED   17307970
  REMARK    Review article
REFERENCE   7  (residues 1 to 823)
  AUTHORS   Vasta,V., Shimizu-Albergine,M. and Beavo,J.A.
  TITLE     Modulation of Leydig cell function by cyclic nucleotide
            phosphodiesterase 8A
  JOURNAL   Proc Natl Acad Sci U S A 103 (52), 19925-19930 (2006)
   PUBMED   17172443
  REMARK    GeneRIF: pharmacological manipulation of PDE8A, alone or in
            combination with other PDEs present in Leydig cells, may be
            exploited to modulate testosterone synthesis
REFERENCE   8  (residues 1 to 823)
  AUTHORS   Dong,H., Osmanova,V., Epstein,P.M. and Brocke,S.
  TITLE     Phosphodiesterase 8 (PDE8) regulates chemotaxis of activated
            lymphocytes
  JOURNAL   Biochem Biophys Res Commun 345 (2), 713-719 (2006)
   PUBMED   16696947
REFERENCE   9  (residues 1 to 823)
  AUTHORS   Glavas,N.A., Ostenson,C., Schaefer,J.B., Vasta,V. and Beavo,J.A.
  TITLE     T cell activation up-regulates cyclic nucleotide phosphodiesterases
            8A1 and 7A3
  JOURNAL   Proc Natl Acad Sci U S A 98 (11), 6319-6324 (2001)
   PUBMED   11371644
REFERENCE   10 (residues 1 to 823)
  AUTHORS   Soderling,S.H., Bayuga,S.J. and Beavo,J.A.
  TITLE     Cloning and characterization of a cAMP-specific cyclic nucleotide
            phosphodiesterase
  JOURNAL   Proc Natl Acad Sci U S A 95 (15), 8991-8996 (1998)
   PUBMED   9671792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO808457.1, AK148238.1, BC125578.1, AF067806.1 and AV272936.1.
            
            On Dec 7, 2005 this sequence version replaced XP_917087.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK148238.1, AF067806.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 45.71 cM"
     Protein         1..823
                     /product="high affinity cAMP-specific and IBMX-insensitive
                     3',5'-cyclic phosphodiesterase 8A"
                     /EC_number="3.1.4.53"
                     /calculated_mol_wt=93041
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88502.1)"
     Region          78..>165
                     /region_name="PleD"
                     /note="Two-component response regulator, PleD family,
                     consists of two REC domains and a diguanylate cyclase
                     (GGDEF) domain [Signal transduction mechanisms,
                     Transcription]; COG3706"
                     /db_xref="CDD:442920"
     Region          215..>320
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          338..373
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88502.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:O60658; propagated from
                     UniProtKB/Swiss-Prot (O88502.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O88502.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O88502.1)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19144319; propagated from
                     UniProtKB/Swiss-Prot (O88502.1)"
     Region          550..800
                     /region_name="PDEase_I"
                     /note="3'5'-cyclic nucleotide phosphodiesterase;
                     pfam00233"
                     /db_xref="CDD:459723"
     CDS             1..823
                     /gene="Pde8a"
                     /gene_synonym="Pde8"
                     /coded_by="NM_008803.3:651..3122"
                     /db_xref="CCDS:CCDS40005.1"
                     /db_xref="GeneID:18584"
                     /db_xref="MGI:MGI:1277116"
ORIGIN      
        1 mgcapsihts enrtfshsdg ededvdvdvp gpaprsiqrw stapglvepq prdngaskvs
       61 vadvqfgpmr fhqdqlqvll vftkedsqcn gfhracekag fkctvtkevq tvltcfqdkl
      121 hdiiiidhry prqmdaetlc rsirsskfse ntvivgvvrr vdkeesslmp flaagftrrf
      181 ienpnvmacy nellqlacge vrsqlklrac nsvftaleks qeaieitsed hiiqyanpaf
      241 estmgyqsge ligkelaqvp inekkgdlld ainscvtvdk ewqgvyhtqk kngdniqqnv
      301 kiipvigqgg kirhyvsiir vcngnnkvet ttecvqtdsq tdnqagkhkd rrkhsmdaka
      361 vssrtsdvss qrrhsslari hsmmieapit kviniinaaq enspvpvtea lnrvldilrt
      421 telyspqfna qddphatdlv gglmsdglrr fsgneyilat knlpplsnnl atpvslhdvp
      481 prialaiene eqwdfdifel evatqnrpli ylglktfarf gmceflqcse ttlrswfqmi
      541 esnyhssnpy hnsthaadvl hatayflsrd kiketldrid evaaliaatv hdvdhpgrtn
      601 sflcnagnql avlyndtavl eshhvalafq ltlendqcni fkqmerndyr tlrqsiidmv
      661 latemtkhfe hvnkfinsin kpltaqesee pdrsledika mlktpesral ikrmmikcad
      721 vsnpcrpleh ciewaarise eyfsqtdeek qldlpvvmpv fdrntcsipk sqisfidyfi
      781 tdmfdawdaf vdlpnlmqhl ddnfrywkgl dekklrslrp ppe
//
LOCUS       NP_001347292             655 aa            linear   ROD 27-APR-2025
DEFINITION  double zinc ribbon and ankyrin repeat-containing protein 1 isoform
            4 [Mus musculus].
ACCESSION   NP_001347292 XP_006499579
VERSION     NP_001347292.1
DBSOURCE    REFSEQ: accession NM_001360363.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Shen,A.L., Moran,S.A., Glover,E.A., Drinkwater,N.R.,
            Swearingen,R.E., Teixeira,L.B. and Bradfield,C.A.
  TITLE     Association of a Chromosomal Rearrangement Event with Mouse
            Posterior Polymorphous Corneal Dystrophy and Alterations in
            Csrp2bp, Dzank1, and Ovol2 Gene Expression
  JOURNAL   PLoS One 11 (6), e0157577 (2016)
   PUBMED   27310661
  REMARK    GeneRIF: Association of a chromosomal rearrangement event with
            mouse posterior polymorphous corneal dystrophy and alterations in
            Csrp2bp, Dzank1, and Ovol2 gene expression have been reported.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Trinidad,J.C., Specht,C.G., Thalhammer,A., Schoepfer,R. and
            Burlingame,A.L.
  TITLE     Comprehensive identification of phosphorylation sites in
            postsynaptic density preparations
  JOURNAL   Mol Cell Proteomics 5 (5), 914-922 (2006)
   PUBMED   16452087
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY254795.1, AK163994.1, AL808119.6 and CJ256961.1.
            
            On Feb 1, 2018 this sequence version replaced XP_006499579.1.
            
            Transcript Variant: This variant (4) lacks two alternate exons,
            resulting in a frameshift and a novel 3' UTR, compared to variant
            1. The encoded isoform (4) is shorter, and has a novel C-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK163994.1, SRR9219381.179236.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 71.02 cM"
     Protein         1..655
                     /product="double zinc ribbon and ankyrin repeat-containing
                     protein 1 isoform 4"
                     /note="ankyrin repeat-containing protein C20orf12 homolog;
                     likely ortholog of H. sapiens chromosome 20 open reading
                     frame 12 (C20orf12); double zinc ribbon and ankyrin
                     repeat-containing protein 1"
                     /calculated_mol_wt=72087
     Region          32..100
                     /region_name="Fn3_assoc"
                     /note="Fn3 associated; pfam13287"
                     /db_xref="CDD:463829"
     Region          229..249
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     Region          230..289
                     /region_name="DZR"
                     /note="Double zinc ribbon; pfam12773"
                     /db_xref="CDD:432773"
     Region          272..289
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     Region          310..328
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     Region          311..365
                     /region_name="DZR"
                     /note="Double zinc ribbon; pfam12773"
                     /db_xref="CDD:432773"
     Region          346..364
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     CDS             1..655
                     /gene="Dzank1"
                     /gene_synonym="2810039F03Rik; 6330439K17Rik; Ankrd64"
                     /coded_by="NM_001360363.1:144..2111"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:241688"
                     /db_xref="MGI:MGI:2139080"
ORIGIN      
        1 mtagsvcapq iiplrvpqpg kanheidtnt llemksdtpd vniyytldgs kpdflkkvgs
       61 genntfkyvk pitlpdgkiq vkavavskdc rqsgivtkvf qvdyeppkmv ssednvedal
      121 kgfskqelkn gfvgpklrkk yknaenkstw nvnlrrladl kvgeradpkt lkdlrfaesp
      181 leipayhega sarlpthqaq spgfahitgq ksltsteimr iqretdflkc ahclasrpsd
      241 pfarfchecg apvppifgyr lpppegaqmg lcaecgsmvp mntpicvvce aplapqlrpq
      301 aslylkervi crtcgtgnpa hlrycvtceg plpptqelgi sashsvcpkc gasnhltarf
      361 cgscgiyvks itrfrmhnsl aivagaprpf peprsawqsl nvplptsasg skkdtgtqts
      421 glfypsgkll akkeleaash rqrqekmsdh rpvltavspg rgywrkqldh isahlrsyaq
      481 nnpefralia eprmgklisa tvhedgyevs irlnyiqvsn kslyfnksvn lsdhflssvt
      541 eggnglydsr sslvsaysqs vsdtpesikk mknlkaksfl vnpepltpen kllleevgss
      601 gkgrlsvleq lldevqkhss srsnstwpgr kgehrhftgm qckrpkeehk rpdsi
//
LOCUS       NP_000620                557 aa            linear   PRI 27-APR-2025
DEFINITION  interferon alpha/beta receptor 1 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_000620
VERSION     NP_000620.2
DBSOURCE    REFSEQ: accession NM_000629.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Woon,S.T., Tjandra,F., Mackay,J., Lumley,T., Grainger,P., Wood,A.,
            Hsiao,K.C. and Ameratunga,R.
  TITLE     Detection of interferon alpha and beta receptor subunit 1 (IFNAR1)
            loss-of-function Glu386 * variant by tri-allelic genotyping
  JOURNAL   Pathology 56 (1), 92-97 (2024)
   PUBMED   37973454
  REMARK    GeneRIF: Detection of interferon alpha and beta receptor subunit 1
            (IFNAR1) loss-of-function Glu386 * variant by tri-allelic
            genotyping.
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Yaugel-Novoa,M., Bourlet,T., Longet,S., Botelho-Nevers,E. and
            Paul,S.
  TITLE     Association of IFNAR1 and IFNAR2 with COVID-19 severity
  JOURNAL   Lancet Microbe 4 (7), e487 (2023)
   PUBMED   37028439
  REMARK    GeneRIF: Association of IFNAR1 and IFNAR2 with COVID-19 severity.
            Erratum:[Lancet Microbe. 2023 Jun;4(6):e394. doi:
            10.1016/S2666-5247(23)00116-7. PMID: 37068499]
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Xiong,J., Jiang,Y., Zhang,J., Chen,Y. and Hu,Y.
  TITLE     CK1alpha upregulates the IFNAR1 expression to prompt the anti-HBV
            effect of type I IFN in hepatoma carcinoma cells
  JOURNAL   Virol Sin 37 (6), 894-903 (2022)
   PUBMED   35985475
  REMARK    GeneRIF: CK1alpha upregulates the IFNAR1 expression to prompt the
            anti-HBV effect of type I IFN in hepatoma carcinoma cells.
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Yang,L., Zhang,X., Huang,X., Dong,X., Jing,S., Zhang,Y., Zhao,B.,
            Wang,Z. and Qu,H.
  TITLE     Correlation between IFNAR1 expression in peripheral blood T
            lymphocytes and inflammatory cytokines, tumor-infiltrating
            lymphocytes, and chemosensitivity in patients with colorectal
            cancer
  JOURNAL   Cytokine 159, 156008 (2022)
   PUBMED   36063748
  REMARK    GeneRIF: Correlation between IFNAR1 expression in peripheral blood
            T lymphocytes and inflammatory cytokines, tumor-infiltrating
            lymphocytes, and chemosensitivity in patients with colorectal
            cancer.
REFERENCE   5  (residues 1 to 557)
  AUTHORS   C West,R., Ezashi,T., B Schoolcraft,W. and Yuan,Y.
  TITLE     Beyond fusion: A novel role for ERVW-1 in trophoblast proliferation
            and type I interferon receptor expression
  JOURNAL   Placenta 126, 150-159 (2022)
   PUBMED   35816776
  REMARK    GeneRIF: Beyond fusion: A novel role for ERVW-1 in trophoblast
            proliferation and type I interferon receptor expression.
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Colamonici,O., Yan,H., Domanski,P., Handa,R., Smalley,D.,
            Mullersman,J., Witte,M., Krishnan,K. and Krolewski,J.
  TITLE     Direct binding to and tyrosine phosphorylation of the alpha subunit
            of the type I interferon receptor by p135tyk2 tyrosine kinase
  JOURNAL   Mol Cell Biol 14 (12), 8133-8142 (1994)
   PUBMED   7526154
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Lutfalla,G., Gardiner,K., Proudhon,D., Vielh,E. and Uze,G.
  TITLE     The structure of the human interferon alpha/beta receptor gene
  JOURNAL   J Biol Chem 267 (4), 2802-2809 (1992)
   PUBMED   1370833
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Flores,I., Mariano,T.M. and Pestka,S.
  TITLE     Human interferon omega (omega) binds to the alpha/beta receptor
  JOURNAL   J Biol Chem 266 (30), 19875-19877 (1991)
   PUBMED   1834641
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Lutfalla,G., Roeckel,N., Mogensen,K.E., Mattei,M.G. and Uze,G.
  TITLE     Assignment of the human interferon-alpha receptor gene to
            chromosome 21q22.1 by in situ hybridization
  JOURNAL   J Interferon Res 10 (5), 515-517 (1990)
   PUBMED   2148760
REFERENCE   10 (residues 1 to 557)
  AUTHORS   Uze,G., Lutfalla,G. and Gresser,I.
  TITLE     Genetic transfer of a functional human interferon alpha receptor
            into mouse cells: cloning and expression of its cDNA
  JOURNAL   Cell 60 (2), 225-234 (1990)
   PUBMED   2153461
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG548299.1, BC021825.1,
            J03171.1, BG116121.1, CA309858.1, BX537636.1, AK123813.1,
            BC035603.1, R15745.1 and AP000298.1.
            
            On Apr 22, 2004 this sequence version replaced NP_000620.1.
            
            Summary: The protein encoded by this gene is a type I membrane
            protein that forms one of the two chains of a receptor for
            interferons alpha and beta. Binding and activation of the receptor
            stimulates Janus protein kinases, which in turn phosphorylate
            several proteins, including STAT1 and STAT2. The protein belongs to
            the type II cytokine receptor family and functions as an antiviral
            factor. [provided by RefSeq, Jul 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.34674.1,
                                           SRR1803614.24038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000270139.8/ ENSP00000270139.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..557
                     /product="interferon alpha/beta receptor 1 isoform 2
                     precursor"
                     /note="alpha-type antiviral protein; beta-type antiviral
                     protein; interferon-beta receptor 1; interferon-alpha/beta
                     receptor alpha chain; interferon alpha/beta receptor 1;
                     CRF2-1; IFN-R-1; IFN-alpha/beta receptor 1; type I
                     interferon receptor 1; cytokine receptor class-II member
                     1; cytokine receptor family 2 member 1; interferon (alpha,
                     beta and omega) receptor 1; IFNalpha/beta receptor 1"
                     /calculated_mol_wt=60932
     sig_peptide     1..27
                     /calculated_mol_wt=2611
     Region          20..114
                     /region_name="Tissue_fac"
                     /note="Tissue factor; pfam01108"
                     /db_xref="CDD:460067"
     mat_peptide     28..557
                     /product="interferon alpha/beta receptor 1 isoform 2"
                     /calculated_mol_wt=60932
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Region          126..224
                     /region_name="Interfer-bind"
                     /note="Interferon-alpha/beta receptor, fibronectin type
                     III; pfam09294"
                     /db_xref="CDD:462746"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21854986,
                     ECO:0007744|PDB:3S98; propagated from UniProtKB/Swiss-Prot
                     (P17181.3)"
     Region          228..318
                     /region_name="Tissue_fac"
                     /note="Tissue factor; pfam01108"
                     /db_xref="CDD:460067"
     Site            254
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Site            313
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Site            314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Region          334..430
                     /region_name="Interfer-bind"
                     /note="Interferon-alpha/beta receptor, fibronectin type
                     III; pfam09294"
                     /db_xref="CDD:462746"
     Site            376
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Site            416
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Site            437..457
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P17181.3)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by TYK2.
                     /evidence=ECO:0000305|PubMed:7526154; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by TYK2.
                     /evidence=ECO:0000305|PubMed:7526154; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Region          491..500
                     /region_name="Important for interaction with TYK2.
                     /evidence=ECO:0000269|PubMed:24704786"
                     /note="propagated from UniProtKB/Swiss-Prot (P17181.3)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     Region          516..557
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17181.3)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14532120,
                     ECO:0000269|PubMed:15337770, ECO:0000269|PubMed:18056411,
                     ECO:0000269|PubMed:24075985; propagated from
                     UniProtKB/Swiss-Prot (P17181.3)"
     CDS             1..557
                     /gene="IFNAR1"
                     /gene_synonym="AVP; IFN-alpha-REC; IFNAR; IFNBR; IFRC;
                     IMD106"
                     /coded_by="NM_000629.3:87..1760"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS13624.1"
                     /db_xref="GeneID:3454"
                     /db_xref="HGNC:HGNC:5432"
                     /db_xref="MIM:107450"
ORIGIN      
        1 mmvvllgatt lvlvavapwv lsaaaggknl kspqkvevdi iddnfilrwn rsdesvgnvt
       61 fsfdyqktgm dnwiklsgcq nitstkcnfs slklnvyeei klriraeken tsswyevdsf
      121 tpfrkaqigp pevhleaedk aivihispgt kdsvmwaldg lsftyslviw knssgveeri
      181 eniysrhkiy klspettycl kvkaalltsw kigvyspvhc ikttvenelp ppenievsvq
      241 nqnyvlkwdy tyanmtfqvq wlhaflkrnp gnhlykwkqi pdcenvkttq cvfpqnvfqk
      301 giyllrvqas dgnntsfwse eikfdteiqa fllppvfnir slsdsfhiyi gapkqsgntp
      361 viqdypliye iifwentsna erkiiekktd vtvpnlkplt vycvkaraht mdeklnkssv
      421 fsdavcektk pgntskiwli vgicialfal pfviyaakvf lrcinyvffp slkpssside
      481 yfseqplknl llstseeqie kcfiienist iatveetnqt dedhkkyssq tsqdsgnysn
      541 edesesktse elqqdfv
//
LOCUS       NP_653217                331 aa            linear   PRI 27-APR-2025
DEFINITION  junctional sarcoplasmic reticulum protein 1 [Homo sapiens].
ACCESSION   NP_653217
VERSION     NP_653217.1
DBSOURCE    REFSEQ: accession NM_144616.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Yasuda,T., Delbono,O., Wang,Z.M., Messi,M.L., Girard,T.,
            Urwyler,A., Treves,S. and Zorzato,F.
  TITLE     JP-45/JSRP1 variants affect skeletal muscle excitation-contraction
            coupling by decreasing the sensitivity of the dihydropyridine
            receptor
  JOURNAL   Hum Mutat 34 (1), 184-190 (2013)
   PUBMED   22927026
  REMARK    GeneRIF: Data indicate that the presence of either one of these
            JP-45 variants decreased the sensitivity of the dihydropyridine
            receptor DHPR to activation.
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Newby,P.R., Pickles,O.J., Mazumdar,S., Brand,O.J., Carr-Smith,J.D.,
            Pearce,S.H., Franklyn,J.A., Evans,D.M., Simmonds,M.J. and
            Gough,S.C.
  CONSRTM   Wellcome Trust Case-Control Consortium (WTCCC)
  TITLE     Follow-up of potential novel Graves' disease susceptibility loci,
            identified in the UK WTCCC genome-wide nonsynonymous SNP study
  JOURNAL   Eur J Hum Genet 18 (9), 1021-1026 (2010)
   PUBMED   20442750
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Gouadon,E., Schuhmeier,R.P., Ursu,D., Anderson,A.A., Treves,S.,
            Zorzato,F., Lehmann-Horn,F. and Melzer,W.
  TITLE     A possible role of the junctional face protein JP-45 in modulating
            Ca2+ release in skeletal muscle
  JOURNAL   J Physiol 572 (Pt 1), 269-280 (2006)
   PUBMED   16423849
  REMARK    GeneRIF: The results may be explained by a modulatory effect of
            JP-45 related to its reported in vitro interaction with the
            dihydropyridine receptor and the SR Ca(2+) binding protein
            calsequestrin (CSQ).
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Anderson,A.A., Treves,S., Biral,D., Betto,R., Sandona,D., Ronjat,M.
            and Zorzato,F.
  TITLE     The novel skeletal muscle sarcoplasmic reticulum JP-45 protein.
            Molecular cloning, tissue distribution, developmental expression,
            and interaction with alpha 1.1 subunit of the voltage-gated calcium
            channel
  JOURNAL   J Biol Chem 278 (41), 39987-39992 (2003)
   PUBMED   12871958
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA897543.1, DA898560.1,
            AK056978.1 and AW137573.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is involved in
            excitation-contraction coupling at the sarcoplasmic reticulum. The
            encoded protein can interact with CACNA1S, CACNB1, and
            calsequestrin to help regulate calcium influx and efflux in
            skeletal muscle. [provided by RefSeq, Jul 2012].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056978.1, SRR1163658.99742.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300961.10/ ENSP00000300961.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..331
                     /product="junctional sarcoplasmic reticulum protein 1"
                     /note="2310032K21Rik; homolog of mouse skeletal muscle
                     sarcoplasmic reticulum protein JP-45; junctional-face
                     membrane protein of 45 kDa homolog"
                     /calculated_mol_wt=36188
     Region          1..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MG2.1)"
     Region          3..76
                     /region_name="Mediates interaction with CACNA1S.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MG2.1)"
     Region          115..177
                     /region_name="JSRP"
                     /note="Junctional sarcoplasmic reticulum protein;
                     pfam15312"
                     /db_xref="CDD:464637"
     Region          157..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MG2.1)"
     Region          <199..>323
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     CDS             1..331
                     /gene="JSRP1"
                     /gene_synonym="JP-45; JP45"
                     /coded_by="NM_144616.4:66..1061"
                     /db_xref="CCDS:CCDS12086.1"
                     /db_xref="GeneID:126306"
                     /db_xref="HGNC:HGNC:24963"
                     /db_xref="MIM:608743"
ORIGIN      
        1 msmttrawee ldgglgscqa ledhsalaet qedrasatpr ladsgsvphd sqvaegpsvd
       61 trpkkmekep aargtpgtgk erlkagaspr svparkkaqt applqppppp palseelpwg
      121 dlslnkclvl aslvallgsa fqlcrdavpg eaalqarvpe pwvppssapr epssplpkfe
      181 aqappsappa praeaevrpk ipgsreaaen deeepgeatg eavredrvtl adrgpkerpr
      241 regkprkekp rkeerpkker prkeerpraa reprealpqr wesregghrp wardsrdaep
      301 rkkqawvspr rpdeeqrpgs rqklragkgr d
//
LOCUS       NP_001355299             128 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF166 isoform 2 [Mus musculus].
ACCESSION   NP_001355299 XP_006531399
VERSION     NP_001355299.1
DBSOURCE    REFSEQ: accession NM_001368370.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Oh,C.K., Choi,Y.K., Hwang,I.Y., Ko,Y.U., Chung,I.K., Yun,N. and
            Oh,Y.J.
  TITLE     RING-finger protein 166 plays a novel pro-apoptotic role in
            neurotoxin-induced neurodegeneration via ubiquitination of XIAP
  JOURNAL   Cell Death Dis 11 (10), 939 (2020)
   PUBMED   33130818
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Manzanares,M., Blanco,M.J. and Nieto,M.A.
  TITLE     Snail3 orthologues in vertebrates: divergent members of the Snail
            zinc-finger gene family
  JOURNAL   Dev Genes Evol 214 (1), 47-53 (2004)
   PUBMED   14655014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114917.2.
            
            On Feb 8, 2019 this sequence version replaced XP_006531399.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.20435.1,
                                           SRR11927934.7246480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849383
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 71.17 cM"
     Protein         1..128
                     /product="E3 ubiquitin-protein ligase RNF166 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="zinc finger protein 313; zinc finger protein 228;
                     RING-type E3 ubiquitin transferase RNF166; E3
                     ubiquitin-protein ligase RNF166"
                     /calculated_mol_wt=14249
     Region          40..99
                     /region_name="zf-Di19"
                     /note="Drought induced 19 protein (Di19), zinc-binding;
                     pfam05605"
                     /db_xref="CDD:428539"
     CDS             1..128
                     /gene="Rnf166"
                     /gene_synonym="1110031E24Rik; Zfp313l"
                     /coded_by="NM_001368370.1:253..639"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:68718"
                     /db_xref="MGI:MGI:1915968"
ORIGIN      
        1 mrahissclk vqeqmancpk fvpvvptsqp ipsnipnrst facpycgarn ldqqelvkhc
       61 veshrsdpnr vvcpicsamp wgdpsyksan flqhllhrhk fsydtfvdys ideeaafqaa
      121 lalslsen
//
LOCUS       NP_001245177             376 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor Sp6 [Homo sapiens].
ACCESSION   NP_001245177
VERSION     NP_001245177.1
DBSOURCE    REFSEQ: accession NM_001258248.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Sipeky,C., Tammela,T.L.J., Auvinen,A. and Schleutker,J.
  TITLE     Novel prostate cancer susceptibility gene SP6 predisposes patients
            to aggressive disease
  JOURNAL   Prostate Cancer Prostatic Dis 24 (4), 1158-1166 (2021)
   PUBMED   34012061
  REMARK    GeneRIF: Novel prostate cancer susceptibility gene SP6 predisposes
            patients to aggressive disease.
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Kim,Y.J., Lee,Y., Zhang,H., Song,J.S., Hu,J.C., Simmer,J.P. and
            Kim,J.W.
  TITLE     A Novel De Novo SP6 Mutation Causes Severe Hypoplastic Amelogenesis
            Imperfecta
  JOURNAL   Genes (Basel) 12 (3), 346 (2021)
   PUBMED   33652941
  REMARK    GeneRIF: A Novel De Novo SP6 Mutation Causes Severe Hypoplastic
            Amelogenesis Imperfecta
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Smith,C.E.L., Whitehouse,L.L.E., Poulter,J.A., Wilkinson Hewitt,L.,
            Nadat,F., Jackson,B.R., Manfield,I.W., Edwards,T.A., Rodd,H.D.,
            Inglehearn,C.F. and Mighell,A.J.
  TITLE     A missense variant in specificity protein 6 (SP6) is associated
            with amelogenesis imperfecta
  JOURNAL   Hum Mol Genet 29 (9), 1417-1425 (2020)
   PUBMED   32167558
  REMARK    GeneRIF: A missense variant in specificity protein 6 (SP6) is
            associated with amelogenesis imperfecta.
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Nakamura,T., Yoshitomi,Y., Sakai,K., Patel,V., Fukumoto,S. and
            Yamada,Y.
  TITLE     Epiprofin orchestrates epidermal keratinocyte proliferation and
            differentiation
  JOURNAL   J Cell Sci 127 (Pt 24), 5261-5272 (2014)
   PUBMED   25344255
  REMARK    GeneRIF: epiprofin (Epfn, also known as Sp6) plays crucial distinct
            roles in these transition stages as a cell cycle regulator and a
            transcription factor.
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Sherva,R., Tripodis,Y., Bennett,D.A., Chibnik,L.B., Crane,P.K., de
            Jager,P.L., Farrer,L.A., Saykin,A.J., Shulman,J.M., Naj,A. and
            Green,R.C.
  CONSRTM   GENAROAD Consortium; Alzheimer's Disease Neuroimaging Initiative;
            Alzheimer's Disease Genetics Consortium
  TITLE     Genome-wide association study of the rate of cognitive decline in
            Alzheimer's disease
  JOURNAL   Alzheimers Dement 10 (1), 45-52 (2014)
   PUBMED   23535033
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Nakamura,T., Unda,F., de-Vega,S., Vilaxa,A., Fukumoto,S.,
            Yamada,K.M. and Yamada,Y.
  TITLE     The Kruppel-like factor epiprofin is expressed by epithelium of
            developing teeth, hair follicles, and limb buds and promotes cell
            proliferation
  JOURNAL   J Biol Chem 279 (1), 626-634 (2004)
   PUBMED   14551215
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Scohy,S., Gabant,P., Van Reeth,T., Hertveldt,V., Dreze,P.L., Van
            Vooren,P., Riviere,M., Szpirer,J. and Szpirer,C.
  TITLE     Identification of KLF13 and KLF14 (SP6), novel members of the
            SP/XKLF transcription factor family
  JOURNAL   Genomics 70 (1), 93-101 (2000)
   PUBMED   11087666
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC003665.1 and AK127707.1.
            
            Summary: SP6 belongs to a family of transcription factors that
            contain 3 classical zinc finger DNA-binding domains consisting of a
            zinc atom tetrahedrally coordinated by 2 cysteines and 2 histidines
            (C2H2 motif). These transcription factors bind to GC-rich sequences
            and related GT and CACCC boxes (Scohy et al., 2000 [PubMed
            11087666]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127707.1, DB134308.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000536300.2/ ENSP00000438209.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..376
                     /product="transcription factor Sp6"
                     /note="Kruppel-like factor 14; krueppel-like factor 14"
                     /calculated_mol_wt=39709
     Region          1..255
                     /region_name="SP6_N"
                     /note="N-terminal domain of transcription factor
                     Specificity Protein (SP) 6; cd22544"
                     /db_xref="CDD:411693"
     Region          1..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SY56.1)"
     Region          118..126
                     /region_name="9aaTAD.
                     /evidence=ECO:0000269|PubMed:31375868"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SY56.1)"
     Region          167..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SY56.1)"
     Region          259..278
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <261..>336
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Site            order(263,265,267,269..270,273..274,277,293,295,299..300,
                     303..304,307,321,323,325,327..328,331..332,335)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          286..308
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          316..336
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          333..376
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SY56.1)"
     CDS             1..376
                     /gene="SP6"
                     /gene_synonym="AI1K; EPFN; EPIPROFIN; KLF14"
                     /coded_by="NM_001258248.2:303..1433"
                     /db_xref="CCDS:CCDS11520.1"
                     /db_xref="GeneID:80320"
                     /db_xref="HGNC:HGNC:14530"
                     /db_xref="MIM:608613"
ORIGIN      
        1 mltavcgslg sqhteaphas pprldlqplq tyqghtspea gdypsplqpg elqslplgpe
       61 vdfsqgyelp gassrvtced lesdsplapg pfskllqpdm shhyeswfrp thpgaedgsw
      121 wdlhpgtswm dlphtqgalt spghpgalqa glggyvgdhq lcappphpha hhllpaaggq
      181 hllgppdgak alevaapesq gldssldgaa rpkgsrrsvp rssgqtvcrc pncleaerlg
      241 apcgpdggkk khlhnchipg cgkayaktsh lkahlrwhsg drpfvcnwlf cgkrftrsde
      301 lqrhlqthtg tkkfpcavcs rvfmrsdhla khmkthegak eeaagaasge gkaggavepp
      361 ggkgkreaeg svapsn
//
LOCUS       NP_005957                487 aa            linear   PRI 27-APR-2025
DEFINITION  NGFI-A-binding protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_005957
VERSION     NP_005957.2
DBSOURCE    REFSEQ: accession NM_005966.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Zhang,J., Zhang,Y. and Zhang,J.
  TITLE     N6-Methyladenosine modified circ-NAB1 modulates cell cycle and
            epithelial-mesenchymal transition via CDKN3 in endometrial cancer
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 161-169 (2024)
   PUBMED   38814199
  REMARK    GeneRIF: N6-Methyladenosine modified circ-NAB1 modulates cell cycle
            and epithelial-mesenchymal transition via CDKN3 in endometrial
            cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Kearney,S.J., Delgado,C., Eshleman,E.M., Hill,K.K., O'Connor,B.P.
            and Lenz,L.L.
  TITLE     Type I IFNs downregulate myeloid cell IFN-gamma receptor by
            inducing recruitment of an early growth response 3/NGFI-A binding
            protein 1 complex that silences ifngr1 transcription
  JOURNAL   J Immunol 191 (6), 3384-3392 (2013)
   PUBMED   23935197
  REMARK    GeneRIF: These data suggest that type I IFN stimulation induces a
            rapid recruitment of a repressive Egr3/Nab1 complex that silences
            transcription from the ifngr1 promoter.
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Mells,G.F., Floyd,J.A., Morley,K.I., Cordell,H.J., Franklin,C.S.,
            Shin,S.Y., Heneghan,M.A., Neuberger,J.M., Donaldson,P.T., Day,D.B.,
            Ducker,S.J., Muriithi,A.W., Wheater,E.F., Hammond,C.J.,
            Dawwas,M.F., Jones,D.E., Peltonen,L., Alexander,G.J., Sandford,R.N.
            and Anderson,C.A.
  CONSRTM   UK PBC Consortium; Wellcome Trust Case Control Consortium 3
  TITLE     Genome-wide association study identifies 12 new susceptibility loci
            for primary biliary cirrhosis
  JOURNAL   Nat Genet 43 (4), 329-332 (2011)
   PUBMED   21399635
  REMARK    Erratum:[Nat Genet. 2011 Nov;43(11):1164. Richardson,Paul [added];
            Nasr, Ikram [added]; Aspinall,Richard [added]]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Zayed,N., El Mansouri,F.E., Chabane,N., Kapoor,M.,
            Martel-Pelletier,J., Benderdour,M., Pelletier,J.P., Duval,N. and
            Fahmi,H.
  TITLE     Valproic acid suppresses interleukin-1ss-induced microsomal
            prostaglandin E2 synthase-1 expression in chondrocytes through
            upregulation of NAB1
  JOURNAL   J Rheumatol 38 (3), 492-502 (2011)
   PUBMED   21239760
  REMARK    GeneRIF: Data show that the suppressive effect of valproic acid on
            chondrocytes is not due to reduced expression or recruitment of
            Egr-1 to the mPGES-1 promoter and involves upregulation of NAB1.
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Moser,D., Molitor,A., Kumsta,R., Tatschner,T., Riederer,P. and
            Meyer,J.
  TITLE     The glucocorticoid receptor gene exon 1-F promoter is not
            methylated at the NGFI-A binding site in human hippocampus
  JOURNAL   World J Biol Psychiatry 8 (4), 262-268 (2007)
   PUBMED   17853270
  REMARK    GeneRIF: Methylation pattern of the corresponding NGFI-A binding
            site in the human glucocorticoid receptor exon 1-F specific
            promoter in post mortem hippocampal tissue.
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Qiu,F.H., Devchand,P.R., Wada,K. and Serhan,C.N.
  TITLE     Aspirin-triggered lipoxin A4 and lipoxin A4 up-regulate
            transcriptional corepressor NAB1 in human neutrophils
  JOURNAL   FASEB J 15 (14), 2736-2738 (2001)
   PUBMED   11687510
REFERENCE   7  (residues 1 to 487)
  AUTHORS   Thiel,G., Kaufmann,K., Magin,A., Lietz,M., Bach,K. and Cramer,M.
  TITLE     The human transcriptional repressor protein NAB1: expression and
            biological activity
  JOURNAL   Biochim Biophys Acta 1493 (3), 289-301 (2000)
   PUBMED   11018254
REFERENCE   8  (residues 1 to 487)
  AUTHORS   Swirnoff,A.H., Apel,E.D., Svaren,J., Sevetson,B.R., Zimonjic,D.B.,
            Popescu,N.C. and Milbrandt,J.
  TITLE     Nab1, a corepressor of NGFI-A (Egr-1), contains an active
            transcriptional repression domain
  JOURNAL   Mol Cell Biol 18 (1), 512-524 (1998)
   PUBMED   9418898
REFERENCE   9  (residues 1 to 487)
  AUTHORS   Svaren,J., Sevetson,B.R., Apel,E.D., Zimonjic,D.B., Popescu,N.C.
            and Milbrandt,J.
  TITLE     NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by
            proliferative and differentiative stimuli
  JOURNAL   Mol Cell Biol 16 (7), 3545-3553 (1996)
   PUBMED   8668170
REFERENCE   10 (residues 1 to 487)
  AUTHORS   Russo,M.W., Sevetson,B.R. and Milbrandt,J.
  TITLE     Identification of NAB1, a repressor of NGFI-A- and Krox20-mediated
            transcription
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 6873-6877 (1995)
   PUBMED   7624335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006460.4, CF137213.1, CN288145.1, BC035724.1, AF045451.1 and
            U47007.1.
            
            On Apr 4, 2002 this sequence version replaced NP_005957.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035724.1, ERR3218372.444766.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337386.10/ ENSP00000336894.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..487
                     /product="NGFI-A-binding protein 1 isoform 1"
                     /note="EGR1 binding protein 1; EGR-1-binding protein 1;
                     transcriptional regulatory protein p54"
                     /calculated_mol_wt=54270
     mat_peptide     1..486
                     /product="NGFI-A-binding protein 1. /id=PRO_0000077038"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13506.2)"
                     /calculated_mol_wt=54245
     Region          4..82
                     /region_name="NCD1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13506.2)"
     Region          5..83
                     /region_name="NCD1"
                     /note="NAB conserved region 1 (NCD1); pfam04904"
                     /db_xref="CDD:461473"
     Region          162..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13506.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61122; propagated from
                     UniProtKB/Swiss-Prot (Q13506.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61122; propagated from
                     UniProtKB/Swiss-Prot (Q13506.2)"
     Region          190..318
                     /region_name="NCD2"
                     /note="NAB conserved region 2 (NCD2); pfam04905"
                     /db_xref="CDD:461474"
     Region          221..310
                     /region_name="NCD2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13506.2)"
     Region          307..338
                     /region_name="Necessary for nuclear localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13506.2)"
     Region          322..486
                     /region_name="Nab1"
                     /note="Conserved region in Nab1; pfam04902"
                     /db_xref="CDD:461472"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q13506.2)"
     Region          399..434
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13506.2)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61122; propagated from
                     UniProtKB/Swiss-Prot (Q13506.2)"
     CDS             1..487
                     /gene="NAB1"
                     /coded_by="NM_005966.4:612..2075"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2307.1"
                     /db_xref="GeneID:4664"
                     /db_xref="HGNC:HGNC:7626"
                     /db_xref="MIM:600800"
ORIGIN      
        1 maaalprtlg elqlyrilqk anllsyfdaf iqqggddvqq lceageeefl eimalvgmas
       61 kplhvrrlqk alrdwvtnpg lfnqpltslp vssipiyklp egsptwlgis cssyerssna
      121 rephlkipkc aattcvqslg qgksdvvgsl alqsvgesrl wqghhatese hslspadlgs
      181 paspkessea ldaaaalsva ecvermaptl pksdlnevke llktnkklak mighifemnd
      241 ddphkeeeir kysaiygrfd skrkdgkhlt lheltvneaa aqlcvkdnal ltrrdelfal
      301 arqisrevty kytyrttksk cgerdelspk rikvedgfpd fqdsvqtlfq qarakseela
      361 alssqqpekv makqmeflcn qagyerlqha errlsaglyr qsseehspng ltsdnsdgqg
      421 erplnlrmpn lqnrqphhfv vdgelsrlyp seakshsses lgilkdyphs aftlekkvik
      481 tepedsr
//
LOCUS       NP_002072                558 aa            linear   PRI 27-APR-2025
DEFINITION  glypican-1 precursor [Homo sapiens].
ACCESSION   NP_002072
VERSION     NP_002072.2
DBSOURCE    REFSEQ: accession NM_002081.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Cheng,F., Fransson,L.A. and Mani,K.
  TITLE     Interplay between glypican-1, amyloid-beta and tau phosphorylation
            in human neural stem cells
  JOURNAL   Neuroscience 553, 121-127 (2024)
   PUBMED   38992568
  REMARK    GeneRIF: Interplay between glypican-1, amyloid-beta and tau
            phosphorylation in human neural stem cells.
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Cao,L., Li,F., Cai,S., Zhang,J., Guo,C., Ali,S., Zhou,J., Jing,X.,
            Wang,X., Qin,Y. and Wu,F.
  TITLE     Pan-cancer analysis and the oncogenic role of Glypican 1 in
            hepatocellular carcinoma
  JOURNAL   Sci Rep 14 (1), 15870 (2024)
   PUBMED   38982153
  REMARK    GeneRIF: Pan-cancer analysis and the oncogenic role of Glypican 1
            in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Li,H., Chiang,C.L., Kwak,K.J., Wang,X., Doddi,S., Ramanathan,L.V.,
            Cho,S.M., Hou,Y.C., Cheng,T.S., Mo,X., Chang,Y.S., Chang,H.L.,
            Cheng,W., Tsai,W.N., Nguyen,L.T.H., Pan,J., Ma,Y., Rima,X.Y.,
            Zhang,J., Reategui,E., Chu,Y.S., Chang,P.M., Chang,P.H.,
            Huang,C.F., Wang,C.H., Shan,Y.S., Li,C.P., Fleisher,M. and Lee,L.J.
  TITLE     Extracellular Vesicular Analysis of Glypican 1 mRNA and Protein for
            Pancreatic Cancer Diagnosis and Prognosis
  JOURNAL   Adv Sci (Weinh) 11 (11), e2306373 (2024)
   PUBMED   38204202
  REMARK    GeneRIF: Extracellular Vesicular Analysis of Glypican 1 mRNA and
            Protein for Pancreatic Cancer Diagnosis and Prognosis.
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Wang,C., Han,Y. and Li,X.
  TITLE     Glypican-1 may be a plasma biomarker for predicting the rupture of
            small intracranial aneurysms
  JOURNAL   J Proteomics 293, 105060 (2024)
   PUBMED   38154549
  REMARK    GeneRIF: Glypican-1 may be a plasma biomarker for predicting the
            rupture of small intracranial aneurysms.
REFERENCE   5  (residues 1 to 558)
  AUTHORS   Cheng,F., Hansson,V.C., Georgolopoulos,G. and Mani,K.
  TITLE     Attenuation of cancer proliferation by suppression of glypican-1
            and its pleiotropic effects in neoplastic behavior
  JOURNAL   Oncotarget 14, 219-235 (2023)
   PUBMED   36944188
  REMARK    GeneRIF: Attenuation of cancer proliferation by suppression of
            glypican-1 and its pleiotropic effects in neoplastic behavior.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 558)
  AUTHORS   Gengrinovitch,S., Berman,B., David,G., Witte,L., Neufeld,G. and
            Ron,D.
  TITLE     Glypican-1 is a VEGF165 binding proteoglycan that acts as an
            extracellular chaperone for VEGF165
  JOURNAL   J Biol Chem 274 (16), 10816-10822 (1999)
   PUBMED   10196157
REFERENCE   7  (residues 1 to 558)
  AUTHORS   Kleeff,J., Ishiwata,T., Kumbasar,A., Friess,H., Buchler,M.W.,
            Lander,A.D. and Korc,M.
  TITLE     The cell-surface heparan sulfate proteoglycan glypican-1 regulates
            growth factor action in pancreatic carcinoma cells and is
            overexpressed in human pancreatic cancer
  JOURNAL   J Clin Invest 102 (9), 1662-1673 (1998)
   PUBMED   9802880
REFERENCE   8  (residues 1 to 558)
  AUTHORS   Vermeesch,J.R., Mertens,G., David,G. and Marynen,P.
  TITLE     Assignment of the human glypican gene (GPC1) to 2q35-q37 by
            fluorescence in situ hybridization
  JOURNAL   Genomics 25 (1), 327-329 (1995)
   PUBMED   7774946
REFERENCE   9  (residues 1 to 558)
  AUTHORS   Karthikeyan,L., Maurel,P., Rauch,U., Margolis,R.K. and
            Margolis,R.U.
  TITLE     Cloning of a major heparan sulfate proteoglycan from brain and
            identification as the rat form of glypican
  JOURNAL   Biochem Biophys Res Commun 188 (1), 395-401 (1992)
   PUBMED   1417860
REFERENCE   10 (residues 1 to 558)
  AUTHORS   David,G., Lories,V., Decock,B., Marynen,P., Cassiman,J.J. and Van
            den Berghe,H.
  TITLE     Molecular cloning of a phosphatidylinositol-anchored membrane
            heparan sulfate proteoglycan from human lung fibroblasts
  JOURNAL   J Cell Biol 111 (6 Pt 2), 3165-3176 (1990)
   PUBMED   2148568
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC110619.3, X54232.1 and
            BG825129.1.
            
            On Feb 6, 2008 this sequence version replaced NP_002072.1.
            
            Summary: Cell surface heparan sulfate proteoglycans are composed of
            a membrane-associated protein core substituted with a variable
            number of heparan sulfate chains. Members of the glypican-related
            integral membrane proteoglycan family (GRIPS) contain a core
            protein anchored to the cytoplasmic membrane via a glycosyl
            phosphatidylinositol linkage.  These proteins may play a role in
            the control of cell division and growth regulation. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X54232.1, BC051279.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264039.7/ ENSP00000264039.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..558
                     /product="glypican-1 precursor"
                     /note="glypican proteoglycan 1; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=59210
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2489
     Region          22..533
                     /region_name="Glypican"
                     /note="pfam01153"
                     /db_xref="CDD:460084"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21932778,
                     ECO:0000269|PubMed:22351761; propagated from
                     UniProtKB/Swiss-Prot (P35052.2)"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:2148568,
                     ECO:0000269|PubMed:21932778, ECO:0000269|PubMed:22351761;
                     propagated from UniProtKB/Swiss-Prot (P35052.2)"
     Region          341..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35052.2)"
     Site            486
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (heparan sulfate) serine.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P35052.2)"
     Site            488
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (heparan sulfate) serine.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P35052.2)"
     Site            490
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (heparan sulfate) serine.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P35052.2)"
     Region          505..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35052.2)"
     CDS             1..558
                     /gene="GPC1"
                     /gene_synonym="glypican"
                     /coded_by="NM_002081.3:257..1933"
                     /db_xref="CCDS:CCDS2534.1"
                     /db_xref="GeneID:2817"
                     /db_xref="HGNC:HGNC:4449"
                     /db_xref="MIM:600395"
ORIGIN      
        1 melrargwwl lcaaaalvac argdpasksr scgevrqiyg akgfslsdvp qaeisgehlr
       61 icpqgytcct semeenlanr shaeletalr dssrvlqaml atqlrsfddh fqhllndser
      121 tlqatfpgaf gelytqnara frdlyselrl yyrganlhle etlaefwarl lerlfkqlhp
      181 qlllpddyld clgkqaealr pfgeaprelr lratrafvaa rsfvqglgva sdvvrkvaqv
      241 plgpecsrav mklvycahcl gvpgarpcpd ycrnvlkgcl anqadldaew rnlldsmvli
      301 tdkfwgtsgv esvigsvhtw laeainalqd nrdtltakvi qgcgnpkvnp qgpgpeekrr
      361 rgklaprerp psgtleklvs eakaqlrdvq dfwislpgtl csekmalsta sddrcwngma
      421 rgrylpevmg dglanqinnp evevditkpd mtirqqimql kimtnrlrsa yngndvdfqd
      481 asddgsgsgs gdgclddlcs rkvsrkssss rtplthalpg lseqegqkts aascpqpptf
      541 llplllflal tvarprwr
//
LOCUS       NP_001074248            1063 aa            linear   PRI 27-APR-2025
DEFINITION  unconventional myosin-Ic isoform a [Homo sapiens].
ACCESSION   NP_001074248
VERSION     NP_001074248.1
DBSOURCE    REFSEQ: accession NM_001080779.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Elmubarak,I., Shril,S., Mansour,B., Bao,A., Kolvenbach,C.M.,
            Kari,J.A., Shalaby,M.A., El Desoky,S., Hildebrandt,F. and
            Schneider,R.
  TITLE     Recessive variants in MYO1C as a potential novel cause of
            proteinuric kidney disease
  JOURNAL   Pediatr Nephrol 39 (10), 2939-2945 (2024)
   PUBMED   38904753
  REMARK    GeneRIF: Recessive variants in MYO1C as a potential novel cause of
            proteinuric kidney disease.
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Xiong,S., Li,S., Li,Z., Song,Y., Yang,L., Yang,H., Xiong,J.,
            Pan,W., Guo,J., Fu,B. and Xu,S.
  TITLE     A noncanonical E3 ubiquitin ligase RNF41-mediated MYO1C stability
            promotes prostate cancer metastasis by inducing actin remodeling
  JOURNAL   Oncogene 43 (36), 2696-2707 (2024)
   PUBMED   39112516
  REMARK    GeneRIF: A noncanonical E3 ubiquitin ligase RNF41-mediated MYO1C
            stability promotes prostate cancer metastasis by inducing actin
            remodeling.
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Suo,J., Wang,Y., Wang,L., Qiu,B., Wang,Z., Yan,A., Qiang,B., Han,W.
            and Peng,X.
  TITLE     RAB31 in glioma-derived endothelial cells promotes glioma cell
            invasion via extracellular vesicle-mediated enrichment of MYO1C
  JOURNAL   FEBS Open Bio 14 (1), 138-147 (2024)
   PUBMED   37953466
  REMARK    GeneRIF: RAB31 in glioma-derived endothelial cells promotes glioma
            cell invasion via extracellular vesicle-mediated enrichment of
            MYO1C.
REFERENCE   4  (residues 1 to 1063)
  AUTHORS   Kit,Y., Starykovych,M., Manko,N., Orfin,A., Alexanyan,T.,
            Bozhko,L., Turchyna,T., Kit,O., Krishnankutty,R., Anand,A.,
            Sibirny,A., Souchelnytskyi,S. and Stoika,R.
  TITLE     Elevation of truncated (48 kDa) form of unconventional myosin 1C in
            blood serum correlates with severe Covid-19
  JOURNAL   J Immunol Methods 514, 113437 (2023)
   PUBMED   36736950
  REMARK    GeneRIF: Elevation of truncated (48 kDa) form of unconventional
            myosin 1C in blood serum correlates with severe Covid-19.
REFERENCE   5  (residues 1 to 1063)
  AUTHORS   Guan,H., Tian,K., Luo,W. and Li,M.
  TITLE     m6A-modified circRNA MYO1C participates in the tumor immune
            surveillance of pancreatic ductal adenocarcinoma through m6A/PD-L1
            manner
  JOURNAL   Cell Death Dis 14 (2), 120 (2023)
   PUBMED   36781839
  REMARK    GeneRIF: m[6]A-modified circRNA MYO1C participates in the tumor
            immune surveillance of pancreatic ductal adenocarcinoma through
            m[6]A/PD-L1 manner.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1063)
  AUTHORS   Fan,H.Y., He,X., Kingston,R.E. and Narlikar,G.J.
  TITLE     Distinct strategies to make nucleosomal DNA accessible
  JOURNAL   Mol Cell 11 (5), 1311-1322 (2003)
   PUBMED   12769854
REFERENCE   7  (residues 1 to 1063)
  AUTHORS   Pestic-Dragovich,L., Stojiljkovic,L., Philimonenko,A.A., Nowak,G.,
            Ke,Y., Settlage,R.E., Shabanowitz,J., Hunt,D.F., Hozak,P. and de
            Lanerolle,P.
  TITLE     A myosin I isoform in the nucleus
  JOURNAL   Science 290 (5490), 337-341 (2000)
   PUBMED   11030652
REFERENCE   8  (residues 1 to 1063)
  AUTHORS   Crozet,F., el Amraoui,A., Blanchard,S., Lenoir,M., Ripoll,C.,
            Vago,P., Hamel,C., Fizames,C., Levi-Acobas,F., Depetris,D.,
            Mattei,M.G., Weil,D., Pujol,R. and Petit,C.
  TITLE     Cloning of the genes encoding two murine and human cochlear
            unconventional type I myosins
  JOURNAL   Genomics 40 (2), 332-341 (1997)
   PUBMED   9119401
REFERENCE   9  (residues 1 to 1063)
  AUTHORS   Hasson,T., Skowron,J.F., Gilbert,D.J., Avraham,K.B., Perry,W.L.,
            Bement,W.M., Anderson,B.L., Sherr,E.H., Chen,Z.Y., Greene,L.A.,
            Ward,D.C., Corey,D.P., Mooseker,M.S., Copeland,N.G. and
            Jenkins,N.A.
  TITLE     Mapping of unconventional myosins in mouse and human
  JOURNAL   Genomics 36 (3), 431-439 (1996)
   PUBMED   8884266
REFERENCE   10 (residues 1 to 1063)
  AUTHORS   Ruppert,C., Godel,J., Muller,R.T., Kroschewski,R., Reinhard,J. and
            Bahler,M.
  TITLE     Localization of the rat myosin I molecules myr 1 and myr 2 and in
            vivo targeting of their tail domains
  JOURNAL   J Cell Sci 108 (Pt 12), 3775-3786 (1995)
   PUBMED   8719884
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC068013.1, DB241937.1,
            CA422782.1 and AI220881.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the unconventional myosin
            protein family, which are actin-based molecular motors. The protein
            is found in the cytoplasm, and one isoform with a unique N-terminus
            is also found in the nucleus. The nuclear isoform associates with
            RNA polymerase I and II and functions in transcription initiation.
            The mouse ortholog of this protein also functions in intracellular
            vesicle transport to the plasma membrane. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            The related gene myosin IE has been referred to as myosin IC in the
            literature, but it is a distinct locus on chromosome 19. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292910.1, SRR1803613.175300.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000648651.1/ ENSP00000496954.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..1063
                     /product="unconventional myosin-Ic isoform a"
                     /note="myosin-I beta; myosin-Ic; nuclear myosin I;
                     unconventional myosin-Ic"
                     /calculated_mol_wt=121551
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O00159.4)"
     Region          62..718
                     /region_name="MYSc_Myo1"
                     /note="class I myosin, motor domain; cd01378"
                     /db_xref="CDD:276829"
     Site            order(88..91,96,140..147,187..197,421..426)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276829"
     Site            order(88..91,96)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276829"
     Site            140..147
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276829"
     Site            187..197
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276829"
     Site            383
                     /site_type="methylation"
                     /note="N6-methyllysine. /evidence=ECO:0000269|Ref.7;
                     propagated from UniProtKB/Swiss-Prot (O00159.4)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00159.4)"
     Site            421..426
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276829"
     Site            order(450..461,464..471,473)
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276829"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTI7; propagated from
                     UniProtKB/Swiss-Prot (O00159.4)"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63355; propagated from
                     UniProtKB/Swiss-Prot (O00159.4)"
     Region          608..630
                     /region_name="Actin-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00782"
                     /note="propagated from UniProtKB/Swiss-Prot (O00159.4)"
     Site            650..660
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276829"
     Site            order(662..688,705..718)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276829"
     Region          751..781
                     /region_name="IQCG"
                     /note="IQ (isoleucine-glutamine) motif containing G
                     (IQCG); cd23766"
                     /db_xref="CDD:467744"
     Site            864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63355; propagated from
                     UniProtKB/Swiss-Prot (O00159.4)"
     Region          874..1055
                     /region_name="Myosin_TH1"
                     /note="Unconventional myosin tail, actin- and
                     lipid-binding; pfam06017"
                     /db_xref="CDD:461801"
     Site            1041
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63355; propagated from
                     UniProtKB/Swiss-Prot (O00159.4)"
     CDS             1..1063
                     /gene="MYO1C"
                     /gene_synonym="MMI-beta; MMIb; MyoIC; myr2; NMI"
                     /coded_by="NM_001080779.2:200..3391"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42226.1"
                     /db_xref="GeneID:4641"
                     /db_xref="HGNC:HGNC:7597"
                     /db_xref="MIM:606538"
ORIGIN      
        1 malqvelvpt geiirvvhph rpcklalgsd gvrvtmesal tardrvgvqd fvllenftse
       61 aafienlrrr frenliytyi gpvlvsvnpy rdlqiysrqh meryrgvsfy evpphlfava
      121 dtvyralrte rrdqavmisg esgagkteat krllqfyaet cpaperggav rdrllqsnpv
      181 leafgnaktl rndnssrfgk ymdvqfdfkg apvgghilsy lleksrvvhq nhgernfhif
      241 yqlleggeee tlrrlglern pqsylylvkg qcakvssind ksdwkvvrka ltvidftede
      301 vedllsivas vlhlgnihfa aneesnaqvt tenqlkyltr llsvegstlr ealthrkiia
      361 kgeellspln leqaayarda lakavysrtf twlvgkinrs laskdvesps wrsttvlgll
      421 diygfevfqh nsfeqfciny cneklqqlfi eltlkseqee yeaegiawep vqyfnnkiic
      481 dlveekfkgi isildeeclr pgeatdltfl ekledtvkhh phflthklad qrtrkslgrg
      541 efrllhyage vtysvtgfld knndllfrnl ketmcssknp imsqcfdrse lsdkkrpetv
      601 atqfkmsllq lveilqskep ayvrcikpnd akqpgrfdev lirhqvkylg llenlrvrra
      661 gfayrrkyea flqrykslcp etwptwagrp qdgvavlvrh lgykpeeykm grtkifirfp
      721 ktlfatedal evrrqslatk iqaawrgfhw rqkflrvkrs aiciqswwrg tlgrrkaakr
      781 kwaaqtirrl irgfvlrhap rcpenaffld hvrtsfllnl rrqlpqnvld tswptpppal
      841 reasellrel ciknmvwkyc rsispewkqq lqqkavasei fkgkkdnypq svprlfistr
      901 lgtdeisprv lqalgsepiq yavpvvkydr kgykprsrql lltpnavviv edakvkqrid
      961 yanltgisvs slsdslfvlh vqradnkqkg dvvlqsdhvi etltktalsa nrvnsininq
     1021 gsitfaggpg rdgtidftpg sellitkakn ghlavvaprl nsr
//
LOCUS       NP_001346812             459 aa            linear   ROD 27-APR-2025
DEFINITION  3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial precursor
            [Mus musculus].
ACCESSION   NP_001346812 XP_006518163
VERSION     NP_001346812.1
DBSOURCE    REFSEQ: accession NM_001359883.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Gao,T., Qian,S., Shen,S., Zhang,X., Liu,J., Jia,W., Chen,Z. and
            Ye,J.
  TITLE     Reduction of mitochondrial 3-oxoacyl-ACP synthase (OXSM) by
            hyperglycemia is associated with deficiency of alpha-lipoic acid
            synthetic pathway in kidney of diabetic mice
  JOURNAL   Biochem Biophys Res Commun 512 (1), 106-111 (2019)
   PUBMED   30871779
  REMARK    GeneRIF: LA (alpha-lipoic acid) deficiency was observed with a
            reduction in lipoylation of pyruvate dehydrogenase in the kidney of
            streptozotocin-induced diabetic mice. Proteins of three enzymes
            (MCAT, OXSM and LIAS) in the LA synthetic pathway were examined in
            the kidney. A reduction was observed in OXSM, but not in the other
            two.
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zhang,L., Joshi,A.K., Hofmann,J., Schweizer,E. and Smith,S.
  TITLE     Cloning, expression, and characterization of the human
            mitochondrial beta-ketoacyl synthase. Complementation of the yeast
            CEM1 knock-out strain
  JOURNAL   J Biol Chem 280 (13), 12422-12429 (2005)
   PUBMED   15668256
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK084829.1, AK034243.1, BG229916.1 and AC173482.1.
            
            On Jan 18, 2018 this sequence version replaced XP_006518163.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK084829.1, AK034243.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 7.08 cM"
     Protein         1..459
                     /product="3-oxoacyl-[acyl-carrier-protein] synthase,
                     mitochondrial precursor"
                     /EC_number="2.3.1.41"
                     /note="3-oxoacyl-[acyl-carrier-protein] synthase,
                     mitochondrial; beta-ketoacyl-ACP synthase"
                     /calculated_mol_wt=45523
     transit_peptide 1..27
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9D404.1)"
                     /calculated_mol_wt=3123
     mat_peptide     28..459
                     /product="3-oxoacyl-[acyl-carrier-protein] synthase,
                     mitochondrial. /id=PRO_0000232661"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D404.1)"
                     /calculated_mol_wt=45523
     Region          42..456
                     /region_name="KAS_I_II"
                     /note="Beta-ketoacyl-acyl carrier protein (ACP) synthase
                     (KAS), type I and II. KASs are responsible for the
                     elongation steps in fatty acid biosynthesis. KASIII
                     catalyses the initial condensation and KAS I and II
                     catalyze further elongation steps by Claisen...; cd00834"
                     /db_xref="CDD:238430"
     Site            109
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9D404.1)"
     Site            order(153,160..161,165,167..168,180,186,190,194,200,202,
                     204..206,218,221..222,225,246..247,250..251,308..312,326,
                     448,450)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238430"
     Site            174
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9D404.1)"
     Site            order(209,348,385)
                     /site_type="active"
                     /db_xref="CDD:238430"
     CDS             1..459
                     /gene="Oxsm"
                     /gene_synonym="4933425A18Rik"
                     /coded_by="NM_001359883.1:74..1453"
                     /db_xref="CCDS:CCDS26831.1"
                     /db_xref="GeneID:71147"
                     /db_xref="MGI:MGI:1918397"
ORIGIN      
        1 mlskclqhfl katishpypa syswliskhr fygtvpaaml rrrvvitgig lvtplgvgtq
       61 lvwdrllrge sgivsvvgde yknipcsvaa yvprgphegq fneenfvsks daksmsssti
      121 mavgaaelal kdsgwhpkre adqvatgvai gmgmvplevi setallfqtk gynkvspffv
      181 pkilinmaag qvsiryklkg pnhsvstact tgahavgdsf rfiahgdadv mvaggtdsci
      241 splslagfsr aralssnpdp klacrpfhpe rdgfvmgega avlvleeheh avqrgariya
      301 eilgyglsgd aghitapdpe gegalrcmaa avkdagvspe qisyvnahat stplgdaaen
      361 raikrlfrdh acalaisstk gatghllgaa gaveatftal acyhqklppt lnldctepef
      421 dlnyvplesq ewkaegrcig ltnsfgfggt natlciagm
//
LOCUS       NP_001137305             107 aa            linear   PRI 27-APR-2025
DEFINITION  IQ domain-containing protein F6 isoform 3 [Homo sapiens].
ACCESSION   NP_001137305 XP_001723435 XP_496643 XP_946510
VERSION     NP_001137305.2
DBSOURCE    REFSEQ: accession NM_001143833.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099050.2.
            
            On Jul 16, 2009 this sequence version replaced NP_001137305.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3) is
            shorter at the N-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX093815.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..107
                     /product="IQ domain-containing protein F6 isoform 3"
                     /note="IQ domain-containing protein F6"
                     /calculated_mol_wt=12928
     CDS             1..107
                     /gene="IQCF6"
                     /coded_by="NM_001143833.4:111..434"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS54590.1"
                     /db_xref="GeneID:440956"
                     /db_xref="HGNC:HGNC:35158"
ORIGIN      
        1 mvrrtllqaa lrawviqcww rsmqakmleq rrrlalrlyt cqewavvkvq aqvrmwqarr
       61 rflqarqaac iiqshwrwha sqtrglirgh yevrasrlel dieilmt
//
LOCUS       NP_004874                850 aa            linear   PRI 27-APR-2025
DEFINITION  pro-neuregulin-2, membrane-bound isoform isoform 1 [Homo sapiens].
ACCESSION   NP_004874
VERSION     NP_004874.1
DBSOURCE    REFSEQ: accession NM_004883.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 850)
  AUTHORS   Chien,W.H., Chen,C.H., Cheng,M.C., Wu,Y.Y. and Gau,S.S.
  TITLE     Neuregulin 2 Is a Candidate Gene for Autism Spectrum Disorder
  JOURNAL   Int J Mol Sci 25 (10), 5547 (2024)
   PUBMED   38791584
  REMARK    GeneRIF: Neuregulin 2 Is a Candidate Gene for Autism Spectrum
            Disorder.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 850)
  AUTHORS   Latorre,J., Martinez,C., Ortega,F., Oliveras-Canellas,N.,
            Diaz-Saez,F., Aragones,J., Camps,M., Guma,A., Ricart,W.,
            Fernandez-Real,J.M. and Moreno-Navarrete,J.M.
  TITLE     The relevance of EGFR, ErbB receptors and neuregulins in human
            adipocytes and adipose tissue in obesity
  JOURNAL   Biomed Pharmacother 156, 113972 (2022)
   PUBMED   36411648
  REMARK    GeneRIF: The relevance of EGFR, ErbB receptors and neuregulins in
            human adipocytes and adipose tissue in obesity.
REFERENCE   3  (residues 1 to 850)
  AUTHORS   Nagasaka,M. and Ou,S.I.
  TITLE     NRG1 and NRG2 fusion positive solid tumor malignancies: a paradigm
            of ligand-fusion oncogenesis
  JOURNAL   Trends Cancer 8 (3), 242-258 (2022)
   PUBMED   34996744
  REMARK    GeneRIF: NRG1 and NRG2 fusion positive solid tumor malignancies: a
            paradigm of ligand-fusion oncogenesis.
            Review article
REFERENCE   4  (residues 1 to 850)
  AUTHORS   Ponomareva,O.N., Ma,H., Dakour,R., Raabe,T.D., Lai,C. and Rimer,M.
  TITLE     Stimulation of acetylcholine receptor transcription by neuregulin-2
            requires an N-box response element and is regulated by alternative
            splicing
  JOURNAL   Neuroscience 134 (2), 495-503 (2005)
   PUBMED   15961242
  REMARK    GeneRIF: Nrg-2-induced Acetylcholine Receptor transcription
            requires an N-box motif and is regulated by alternative splicing.
REFERENCE   5  (residues 1 to 850)
  AUTHORS   Yamada,K., Ichino,N., Nishii,K., Sawada,H., Higashiyama,S.,
            Ishiguro,H. and Nagatsu,T.
  TITLE     Characterization of the human NTAK gene structure and distribution
            of the isoforms for rat NTAK mRNA
  JOURNAL   Gene 255 (1), 15-24 (2000)
   PUBMED   10974560
REFERENCE   6  (residues 1 to 850)
  AUTHORS   Ring,H.Z., Chang,H., Guilbot,A., Brice,A., LeGuern,E. and
            Francke,U.
  TITLE     The human neuregulin-2 (NRG2) gene: cloning, mapping and evaluation
            as a candidate for the autosomal recessive form of
            Charcot-Marie-Tooth disease linked to 5q
  JOURNAL   Hum Genet 104 (4), 326-332 (1999)
   PUBMED   10369162
REFERENCE   7  (residues 1 to 850)
  AUTHORS   Reddy,P.H., Stockburger,E., Gillevet,P. and Tagle,D.A.
  TITLE     Mapping and characterization of novel (CAG)n repeat cDNAs from
            adult human brain derived by the oligo capture method
  JOURNAL   Genomics 46 (2), 174-182 (1997)
   PUBMED   9417904
REFERENCE   8  (residues 1 to 850)
  AUTHORS   Higashiyama,S., Horikawa,M., Yamada,K., Ichino,N., Nakano,N.,
            Nakagawa,T., Miyagawa,J., Matsushita,N., Nagatsu,T., Taniguchi,N.
            and Ishiguro,H.
  TITLE     A novel brain-derived member of the epidermal growth factor family
            that interacts with ErbB3 and ErbB4
  JOURNAL   J Biochem 122 (3), 675-680 (1997)
   PUBMED   9348101
REFERENCE   9  (residues 1 to 850)
  AUTHORS   Busfield,S.J., Michnick,D.A., Chickering,T.W., Revett,T.L., Ma,J.,
            Woolf,E.A., Comrack,C.A., Dussault,B.J., Woolf,J., Goodearl,A.D.
            and Gearing,D.P.
  TITLE     Characterization of a neuregulin-related gene, Don-1, that is
            highly expressed in restricted regions of the cerebellum and
            hippocampus
  JOURNAL   Mol Cell Biol 17 (7), 4007-4014 (1997)
   PUBMED   9199335
REFERENCE   10 (residues 1 to 850)
  AUTHORS   Carraway,K.L. 3rd, Weber,J.L., Unger,M.J., Ledesma,J., Yu,N.,
            Gassmann,M. and Lai,C.
  TITLE     Neuregulin-2, a new ligand of ErbB3/ErbB4-receptor tyrosine kinases
  JOURNAL   Nature 387 (6632), 512-516 (1997)
   PUBMED   9168115
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA090538.1, AB005060.1,
            AC008667.10 and AI271427.1.
            
            Summary: This gene encodes a novel member of the neuregulin family
            of growth and differentiation factors. Through interaction with the
            ERBB family of receptors, this protein induces the growth and
            differentiation of epithelial, neuronal, glial, and other types of
            cells. The gene consists of 12 exons and the genomic structure is
            similar to that of neuregulin 1, another member of the neuregulin
            family of ligands. The products of these genes mediate distinct
            biological processes by acting at different sites in tissues and
            eliciting different biological responses in cells. This gene is
            located close to the region for demyelinating Charcot-Marie-Tooth
            disease locus, but is not responsible for this disease. Alternative
            transcript variants encoding distinct isoforms have been described.
            [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) encodes isoform 1, which is
            also known as isoform alpha or alpha2. This variant is supported by
            data in PMID:10369162.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB005060.1, ERR4368409.206198.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361474.6/ ENSP00000354910.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..850
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.2"
     Protein         1..850
                     /product="pro-neuregulin-2, membrane-bound isoform isoform
                     1"
                     /note="neural- and thymus-derived activator for ErbB
                     kinases; divergent of neuregulin-1; pro-NRG2"
                     /calculated_mol_wt=91548
     Region          1..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14511.1)"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14511.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14511.1)"
     Site            147
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14511.1)"
     Region          237..328
                     /region_name="Ig_Pro_neuregulin"
                     /note="Immunoglobulin (Ig)-like domain in neuregulins;
                     cd05750"
                     /db_xref="CDD:409408"
     Region          237..243
                     /region_name="putative Ig strand A"
                     /note="putative Ig strand A [structural motif]"
                     /db_xref="CDD:409408"
     Region          253..257
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409408"
     Region          267..271
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409408"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14511.1)"
     Region          294..298
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409408"
     Region          308..313
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409408"
     Region          321..324
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409408"
     Site            346
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14511.1)"
     Site            406..426
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14511.1)"
     Region          430..831
                     /region_name="Neuregulin"
                     /note="Neuregulin intracellular region; pfam02158"
                     /db_xref="CDD:426627"
     Region          492..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14511.1)"
     Region          566..585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14511.1)"
     Region          647..681
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14511.1)"
     Region          700..788
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14511.1)"
     Region          801..850
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14511.1)"
     CDS             1..850
                     /gene="NRG2"
                     /gene_synonym="DON1; HRG2; NTAK"
                     /coded_by="NM_004883.3:231..2783"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4217.1"
                     /db_xref="GeneID:9542"
                     /db_xref="HGNC:HGNC:7998"
                     /db_xref="MIM:603818"
ORIGIN      
        1 mrqvccsalp ppplekgrcs sysdssssss erssssssss sesgsssrss snnssisrpa
       61 appeprpqqq pqprspaarr aaarsraaaa ggmrrdpapg fsmllfgvsl acyspslksv
      121 qdqaykapvv vegkvqglvp aggsssnstr eppasgrval vkvldkwplr sgglqreqvi
      181 svgscvpler nqryifflep teqplvfkta fapldtngkn lkkevgkilc tdcatrpklk
      241 kmksqtgqvg ekqslkceaa agnpqpsyrw fkdgkelnrs rdirikygng rknsrlqfnk
      301 vkvedageyv ceaenilgkd tvrgrlyvns vsttlsswsg harkcnetak sycvnggvcy
      361 yieginqlsc kcpngffgqr cleklplrly mpdpkqkaee lyqkrvltit gicvallvvg
      421 ivcvvayckt kkqrkqmhnh lrqnmcpahq nrslangpsh prldpeeiqm adyisknvpa
      481 tdhvirrete ttfsgshscs pshhcstatp tsshrhesht wslerseslt sdsqsgimls
      541 svgtskcnsp acveararra aaynleerrr atappyhdsv dslrdsphse ryvsalttpa
      601 rlspvdfhys latqvptfei tspnsahavs lppaapisyr laeqqpllrh pappgpgpgp
      661 gpgpgpgadm qrsydsyyyp aagpgprrgt calggslgsl paspfriped deyettqeca
      721 ppppprprar gasrrtsagp rrwrrsrlng laaqraraar dslslssgsg ggsasasddd
      781 addadgalaa estpflglrg ahdalrsdsp plcpaadsrt yysldshstr assrhsrgpp
      841 prakqdsapl
//
LOCUS       NP_001135888             312 aa            linear   PRI 27-APR-2025
DEFINITION  aminoacyl tRNA synthase complex-interacting multifunctional protein
            1 precursor [Homo sapiens].
ACCESSION   NP_001135888
VERSION     NP_001135888.2
DBSOURCE    REFSEQ: accession NM_001142416.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Yuan,C., Liu,X., Cai,S., Zhang,L., Guo,R., Jia,Z., Sun,Y. and Li,B.
  TITLE     Secreted aminoacyl-tRNA synthetase-interacting multifunctional
            protein-1 (AIMP1) is a promising predictor for the severity of
            acute AQP4-IgG positive neuromyelitis optica spectrum disorder
  JOURNAL   Mult Scler Relat Disord 70, 104504 (2023)
   PUBMED   36623394
  REMARK    GeneRIF: Secreted aminoacyl-tRNA synthetase-interacting
            multifunctional protein-1 (AIMP1) is a promising predictor for the
            severity of acute AQP4-IgG positive neuromyelitis optica spectrum
            disorder.
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Tantawy,A.A.G., Tadros,M.A.R., Adly,A.A.M., Ismail,E.A.R.,
            Ibrahim,F.A., Salah Eldin,N.M., Hussein,M.M., Alfeky,M.A.,
            Ibrahim,S.M., Hashem,M.A. and Ebeid,F.S.E.
  TITLE     Endothelin-1 gene polymorphism (G8002A) and endothelial
            monocyte-activating polypeptide II: Role in vascular dysfunction in
            pediatric patients with beta-thalassemia major
  JOURNAL   Cytokine 161, 156048 (2023)
   PUBMED   36279697
  REMARK    GeneRIF: Endothelin-1 gene polymorphism (G8002A) and endothelial
            monocyte-activating polypeptide II: Role in vascular dysfunction in
            pediatric patients with beta-thalassemia major.
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Wei,R., Zhu,Y., Zhang,Y., Zhao,W., Yu,X., Wang,L., Gu,C., Gu,X. and
            Yang,Y.
  TITLE     AIMP1 promotes multiple myeloma malignancy through interacting with
            ANP32A to mediate histone H3 acetylation
  JOURNAL   Cancer Commun (Lond) 42 (11), 1185-1206 (2022)
   PUBMED   36042007
  REMARK    GeneRIF: AIMP1 promotes multiple myeloma malignancy through
            interacting with ANP32A to mediate histone H3 acetylation.
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Saber,M.M.
  TITLE     EMAP II Expression Is Increased on Peripheral Blood Cells from
            Non-Hodgkin Lymphoma
  JOURNAL   J Immunol Res 2022, 7219207 (2022)
   PUBMED   36132984
  REMARK    GeneRIF: EMAP II Expression Is Increased on Peripheral Blood Cells
            from Non-Hodgkin Lymphoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Jaramillo Ponce,J.R., Kapps,D., Paulus,C., Chicher,J. and
            Frugier,M.
  TITLE     Discovery of two distinct aminoacyl-tRNA synthetase complexes
            anchored to the Plasmodium surface tRNA import protein
  JOURNAL   J Biol Chem 298 (6), 101987 (2022)
   PUBMED   35487244
  REMARK    GeneRIF: Discovery of two distinct aminoacyl-tRNA synthetase
            complexes anchored to the Plasmodium surface tRNA import protein.
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Kao,J., Houck,K., Fan,Y., Haehnel,I., Libutti,S.K., Kayton,M.L.,
            Grikscheit,T., Chabot,J., Nowygrod,R., Greenberg,S. et al.
  TITLE     Characterization of a novel tumor-derived cytokine.
            Endothelial-monocyte activating polypeptide II
  JOURNAL   J Biol Chem 269 (40), 25106-25119 (1994)
   PUBMED   7929199
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Lamour,V., Quevillon,S., Diriong,S., N'Guyen,V.C., Lipinski,M. and
            Mirande,M.
  TITLE     Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme
            as a case of horizontal gene transfer
  JOURNAL   Proc Natl Acad Sci U S A 91 (18), 8670-8674 (1994)
   PUBMED   8078941
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Shiba,K., Suzuki,N., Shigesada,K., Namba,Y., Schimmel,P. and
            Noda,T.
  TITLE     Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence
            of the anticodon-binding domain and acquisition of a new structural
            unit
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7435-7439 (1994)
   PUBMED   8052601
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Kao,J., Fan,Y.G., Haehnel,I., Brett,J., Greenberg,S., Clauss,M.,
            Kayton,M., Houck,K., Kisiel,W., Seljelid,R. et al.
  TITLE     A peptide derived from the amino terminus of
            endothelial-monocyte-activating polypeptide II modulates
            mononuclear and polymorphonuclear leukocyte functions, defines an
            apparently novel cellular interaction site, and induces an acute
            inflammatory response
  JOURNAL   J Biol Chem 269 (13), 9774-9782 (1994)
   PUBMED   7545917
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Kao,J., Ryan,J., Brett,G., Chen,J., Shen,H., Fan,Y.G., Godman,G.,
            Familletti,P.C., Wang,F., Pan,Y.C. et al.
  TITLE     Endothelial monocyte-activating polypeptide II. A novel
            tumor-derived polypeptide that activates host-response mechanisms
  JOURNAL   J Biol Chem 267 (28), 20239-20247 (1992)
   PUBMED   1400342
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK303965.1, U10117.1 and
            AC093680.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 8, 2019 this sequence version replaced NP_001135888.1.
            
            Summary: The protein encoded by this gene is a cytokine that is
            specifically induced by apoptosis, and it is involved in the
            control of angiogenesis, inflammation, and wound healing. The
            release of this cytokine renders the tumor-associated vasculature
            sensitive to tumor necrosis factor. The precursor protein is
            identical to the p43 subunit, which is associated with the
            multi-tRNA synthetase complex, and it modulates aminoacylation
            activity of tRNA synthetase in normal cells. This protein is also
            involved in the stimulation of inflammatory responses after
            proteolytic cleavage in tumor cells. Multiple transcript variants
            encoding different isoforms have been found for this gene. A
            pseudogene has been identified on chromosome 20. [provided by
            RefSeq, Dec 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR.
            Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000672341.1/
                                                ENSP00000500620.1
            RefSeq Select criteria           :: based on manual assertion,
                                                conservation, expression,
                                                longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..312
                     /product="aminoacyl tRNA synthase complex-interacting
                     multifunctional protein 1 precursor"
                     /note="small inducible cytokine subfamily E, member 1
                     (endothelial monocyte-activating); endothelial
                     monocyte-activating polypeptide 2; endothelial-monocyte
                     activating polypeptide II; multisynthetase complex
                     auxiliary component p43; ARS-interacting multifunctional
                     protein 1; aminoacyl tRNA synthase complex-interacting
                     multifunctional protein 1; multisynthase complex auxiliary
                     component p43"
                     /calculated_mol_wt=34222
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:37316325; propagated from
                     UniProtKB/Swiss-Prot (Q12904.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:24312579,
                     ECO:0000269|PubMed:37316325, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q12904.2)"
     Region          3..>79
                     /region_name="PRK05431"
                     /note="seryl-tRNA synthetase; Provisional"
                     /db_xref="CDD:235461"
     Region          6..46
                     /region_name="Required for fibroblast proliferation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12904.2)"
     Region          54..194
                     /region_name="Interaction with HSP90B1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12904.2)"
     Region          101..114
                     /region_name="Required for endothelial cell death"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12904.2)"
     Region          107..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12904.2)"
     Region          114..192
                     /region_name="Required for endothelial cell migration"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12904.2)"
     Region          <140..312
                     /region_name="PLN02610"
                     /note="probable methionyl-tRNA synthetase"
                     /db_xref="CDD:215329"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12904.2)"
     mat_peptide     147..312
                     /product="aminoacyl tRNA synthase complex-interacting
                     multifunctional protein 1"
                     /calculated_mol_wt=18218
     CDS             1..312
                     /gene="AIMP1"
                     /gene_synonym="EMAP2; EMAPII; HLD3; p43; SCYE1"
                     /coded_by="NM_001142416.2:71..1009"
                     /db_xref="CCDS:CCDS3674.1"
                     /db_xref="GeneID:9255"
                     /db_xref="HGNC:HGNC:10648"
                     /db_xref="MIM:603605"
ORIGIN      
        1 manndavlkr leqkgaeadq iieylkqqvs llkekailqa tlreekklrv enaklkkeie
       61 elkqeliqae iqngvkqipf psgtplhans mvsenviqst avttvssgtk eqikggtgde
      121 kkakekiekk gekkekkqqs iagsadskpi dvsrldlrig ciitarkhpd adslyveevd
      181 vgeiaprtvv sglvnhvple qmqnrmvill cnlkpakmrg vlsqamvmca sspekieila
      241 ppngsvpgdr itfdafpgep dkelnpkkki weqiqpdlht ndecvatykg vpfevkgkgv
      301 craqtmsnsg ik
//
LOCUS       NP_004432                984 aa            linear   PRI 27-APR-2025
DEFINITION  ephrin type-B receptor 1 precursor [Homo sapiens].
ACCESSION   NP_004432
VERSION     NP_004432.1
DBSOURCE    REFSEQ: accession NM_004441.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Kundu,S., Nunes,L., Adler,J., Mathot,L., Stoimenov,I. and
            Sjoblom,T.
  TITLE     Recurring EPHB1 mutations in human cancers alter receptor
            signalling and compartmentalisation of colorectal cancer cells
  JOURNAL   Cell Commun Signal 21 (1), 354 (2023)
   PUBMED   38102712
  REMARK    GeneRIF: Recurring EPHB1 mutations in human cancers alter receptor
            signalling and compartmentalisation of colorectal cancer cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Ahmed,M.S., Wang,P., Nguyen,N.U.N., Nakada,Y., Menendez-Montes,I.,
            Ismail,M., Bachoo,R., Henkemeyer,M., Sadek,H.A. and Kandil,E.S.
  TITLE     Identification of tetracycline combinations as EphB1 tyrosine
            kinase inhibitors for treatment of neuropathic pain
  JOURNAL   Proc Natl Acad Sci U S A 118 (10) (2021)
   PUBMED   33627480
  REMARK    GeneRIF: Identification of tetracycline combinations as EphB1
            tyrosine kinase inhibitors for treatment of neuropathic pain.
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Jin,F., Zhao,L., Hu,Q. and Qi,F.
  TITLE     Peripheral EphrinB1/EphB1 signalling attenuates muscle hyperalgesia
            in MPS patients and a rat model of taut band-associated persistent
            muscle pain
  JOURNAL   Mol Pain 16, 1744806920984079 (2020)
   PUBMED   33356837
  REMARK    GeneRIF: Peripheral EphrinB1/EphB1 signalling attenuates muscle
            hyperalgesia in MPS patients and a rat model of taut
            band-associated persistent muscle pain.
REFERENCE   4  (residues 1 to 984)
  AUTHORS   Trease,A.J., Li,H., Spagnol,G., Zheng,L., Stauch,K.L. and
            Sorgen,P.L.
  TITLE     Regulation of Connexin32 by ephrin receptors and T-cell
            protein-tyrosine phosphatase
  JOURNAL   J Biol Chem 294 (1), 341-350 (2019)
   PUBMED   30401746
  REMARK    GeneRIF: EphB1 and EphA1 phosphorylate the Cx32CT domain residue
            Tyr(243) Unlike for Cx43, the tyrosine phosphorylation of the
            Cx32CT increased gap junction intercellular communication.
REFERENCE   5  (residues 1 to 984)
  AUTHORS   Chen,Q., Deng,R., Zhao,X., Yuan,H., Zhang,H., Dou,J., Chen,R.,
            Jin,H., Wang,Y., Huang,J. and Yu,J.
  TITLE     Sumoylation of EphB1 Suppresses Neuroblastoma Tumorigenesis via
            Inhibiting PKCgamma Activation
  JOURNAL   Cell Physiol Biochem 45 (6), 2283-2292 (2018)
   PUBMED   29550816
  REMARK    GeneRIF: SUMOylation of EphB1 repressed activation of its
            downstream signaling molecule PKC-gamma, and consequently inhibited
            neuroblastoma tumorigenesis.
REFERENCE   6  (residues 1 to 984)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   7  (residues 1 to 984)
  AUTHORS   Cerretti,D.P., Vanden Bos,T., Nelson,N., Kozlosky,C.J., Reddy,P.,
            Maraskovsky,E., Park,L.S., Lyman,S.D., Copeland,N.G., Gilbert,D.J.
            et al.
  TITLE     Isolation of LERK-5: a ligand of the eph-related receptor tyrosine
            kinases
  JOURNAL   Mol Immunol 32 (16), 1197-1205 (1995)
   PUBMED   8559144
REFERENCE   8  (residues 1 to 984)
  AUTHORS   Tang,X.X., Biegel,J.A., Nycum,L.M., Yoshioka,A., Brodeur,G.M.,
            Pleasure,D.E. and Ikegaki,N.
  TITLE     cDNA cloning, molecular characterization, and chromosomal
            localization of NET(EPHT2), a human EPH-related receptor
            protein-tyrosine kinase gene preferentially expressed in brain
  JOURNAL   Genomics 29 (2), 426-437 (1995)
   PUBMED   8666391
REFERENCE   9  (residues 1 to 984)
  AUTHORS   Davis,S., Gale,N.W., Aldrich,T.H., Maisonpierre,P.C., Lhotak,V.,
            Pawson,T., Goldfarb,M. and Yancopoulos,G.D.
  TITLE     Ligands for EPH-related receptor tyrosine kinases that require
            membrane attachment or clustering for activity
  JOURNAL   Science 266 (5186), 816-819 (1994)
   PUBMED   7973638
REFERENCE   10 (residues 1 to 984)
  AUTHORS   Beckmann,M.P., Cerretti,D.P., Baum,P., Vanden Bos,T., James,L.,
            Farrah,T., Kozlosky,C., Hollingsworth,T., Shilling,H.,
            Maraskovsky,E. et al.
  TITLE     Molecular characterization of a family of ligands for eph-related
            tyrosine kinase receptors
  JOURNAL   EMBO J 13 (16), 3757-3762 (1994)
   PUBMED   8070404
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016931.21, AC016951.9,
            AC073244.13 and AC092969.7.
            
            Summary: Ephrin receptors and their ligands, the ephrins, mediate
            numerous developmental processes, particularly in the nervous
            system. Based on their structures and sequence relationships,
            ephrins are divided into the ephrin-A (EFNA) class, which are
            anchored to the membrane by a glycosylphosphatidylinositol linkage,
            and the ephrin-B (EFNB) class, which are transmembrane proteins.
            The Eph family of receptors are divided into 2 groups based on the
            similarity of their extracellular domain sequences and their
            affinities for binding ephrin-A and ephrin-B ligands. Ephrin
            receptors make up the largest subgroup of the receptor tyrosine
            kinase (RTK) family. The protein encoded by this gene is a receptor
            for ephrin-B family members. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.66964.1,
                                           SRR1803614.251394.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398015.8/ ENSP00000381097.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.2"
     Protein         1..984
                     /product="ephrin type-B receptor 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-B receptor 1; eph tyrosine kinase 2;
                     EK6; EPH-like kinase 6; tyrosine-protein kinase receptor
                     EPH-2; neuronally-expressed EPH-related tyrosine kinase"
                     /calculated_mol_wt=108143
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1761
     mat_peptide     18..984
                     /product="ephrin type-B receptor 1"
                     /calculated_mol_wt=108143
     Region          20..195
                     /region_name="EphR_LBD_B1"
                     /note="Ligand Binding Domain of Ephrin type-B Receptor 1;
                     cd10476"
                     /db_xref="CDD:198444"
     Site            order(27..29,31,43..46,48,52,54,56,59,92..94,98,100,146,
                     148,154..155,157..158,183,185,187)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198444"
     Site            order(323,398,411)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          326..412
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54762.1)"
     Site            order(412..413,415..416)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            order(417,498,513)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            426
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54762.1)"
     Region          435..518
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54762.1)"
     Site            order(514..515,517..518)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            541..563
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54762.1)"
     Region          542..616
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P54753; propagated from
                     UniProtKB/Swiss-Prot (P54762.1)"
     Region          614..882
                     /region_name="PTKc_EphR_B"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphB Ephrin Receptors; cd05065"
                     /db_xref="CDD:173638"
     Site            order(625..629,633,649,651,697..698,700,704,744,748..749,
                     751,762,783..787,796,830)
                     /site_type="active"
                     /db_xref="CDD:173638"
     Site            order(625..627,629,633,649,651,697..698,700,704,749,751,
                     762)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173638"
     Site            order(744,748,783..787,796,830)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173638"
     Site            761..789
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173638"
     Region          908..975
                     /region_name="SAM_EPH-B1"
                     /note="SAM domain of EPH-B1 subfamily of tyrosine kinase
                     receptors; cd09551"
                     /db_xref="CDD:188950"
     Site            order(928,961)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188950"
     Site            928
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P54762.1)"
     Region          982..984
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P54762.1)"
     CDS             1..984
                     /gene="EPHB1"
                     /gene_synonym="ELK; EPHT2; Hek6; NET"
                     /coded_by="NM_004441.5:373..3327"
                     /db_xref="CCDS:CCDS46921.1"
                     /db_xref="GeneID:2047"
                     /db_xref="HGNC:HGNC:3392"
                     /db_xref="MIM:600600"
ORIGIN      
        1 maldylllll lasavaamee tlmdtrtata elgwtanpas gweevsgyde nlntirtyqv
       61 cnvfepnqnn wllttfinrr gahriytemr ftvrdcsslp nvpgscketf nlyyyetdsv
      121 iatkksafws eapylkvdti aadesfsqvd fggrlmkvnt evrsfgpltr ngfylafqdy
      181 gacmsllsvr vffkkcpsiv qnfavfpetm tgaestslvi argtcipnae evdvpiklyc
      241 ngdgewmvpi grctckpgye pensvackac pagtfkasqe aegcshcpsn srspaeaspi
      301 ctcrtgyyra dfdppevact svpsgprnvi sivnetsiil ewhppretgg rddvtyniic
      361 kkcradrrsc srcddnvefv prqlgltecr vsisslwaht pytfdiqain gvsskspfpp
      421 qhvsvnittn qaapstvpim hqvsatmrsi tlswpqpeqp ngiildyeir yyekehnefn
      481 ssmarsqtnt aridglrpgm vyvvqvrart vagygkfsgk mcfqtltddd ykselreqlp
      541 liagsaaagv vfvvslvais ivcsrkrays keavysdklq hystgrgspg mkiyidpfty
      601 edpneavref akeidvsfvk ieevigagef gevykgrlkl pgkreiyvai ktlkagysek
      661 qrrdflseas imgqfdhpni irlegvvtks rpvmiitefm engaldsflr qndgqftviq
      721 lvgmlrgiaa gmkylaemny vhrdlaarni lvnsnlvckv sdfglsrylq ddtsdptyts
      781 slggkipvrw tapeaiayrk ftsasdvwsy givmwevmsf gerpywdmsn qdvinaieqd
      841 yrlpppmdcp aalhqlmldc wqkdrnsrpr faeivntldk mirnpaslkt vatitavpsq
      901 plldrsipdf tafttvddwl saikmvqyrd sfltagftsl qlvtqmtsed llrigitlag
      961 hqkkilnsih smrvqisqsp tama
//
LOCUS       NP_057131                125 aa            linear   PRI 27-APR-2025
DEFINITION  splicing factor 3B subunit 6 [Homo sapiens].
ACCESSION   NP_057131
VERSION     NP_057131.1
DBSOURCE    REFSEQ: accession NM_016047.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Kato,K., Udagawa,R., Hayashi,Y., Maki,M., Yanagida,M.,
            Higashiura,S., Yagishita,R., Shimamoto,H. and Kimura,K.
  TITLE     SF3B14 is involved in the centrosome regulation through splicing of
            TUBGCP6 pre-mRNA
  JOURNAL   Biochem Biophys Res Commun 588, 133-139 (2022)
   PUBMED   34954520
  REMARK    GeneRIF: SF3B14 is involved in the centrosome regulation through
            splicing of TUBGCP6 pre-mRNA.
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Tholen,J., Razew,M., Weis,F. and Galej,W.P.
  TITLE     Structural basis of branch site recognition by the human
            spliceosome
  JOURNAL   Science 375 (6576), 50-57 (2022)
   PUBMED   34822310
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Li,J., Tong,H., Li,D., Jiang,Q., Zhang,Y., Tang,W., Jin,D.,
            Chen,S., Qin,X., Zhang,S. and Xue,R.
  TITLE     The long non-coding RNA DKFZp434J0226 regulates the alternative
            splicing process through phosphorylation of SF3B6 in PDAC
  JOURNAL   Mol Med 27 (1), 95 (2021)
   PUBMED   34470609
  REMARK    GeneRIF: The long non-coding RNA DKFZp434J0226 regulates the
            alternative splicing process through phosphorylation of SF3B6 in
            PDAC.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Zhang,Z., Will,C.L., Bertram,K., Dybkov,O., Hartmuth,K.,
            Agafonov,D.E., Hofele,R., Urlaub,H., Kastner,B., Luhrmann,R. and
            Stark,H.
  TITLE     Molecular architecture of the human 17S U2 snRNP
  JOURNAL   Nature 583 (7815), 310-313 (2020)
   PUBMED   32494006
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Will,C.L., Urlaub,H., Achsel,T., Gentzel,M., Wilm,M. and
            Luhrmann,R.
  TITLE     Characterization of novel SF3b and 17S U2 snRNP proteins, including
            a human Prp5p homologue and an SF3b DEAD-box protein
  JOURNAL   EMBO J 21 (18), 4978-4988 (2002)
   PUBMED   12234937
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R.
  TITLE     Comprehensive proteomic analysis of the human spliceosome
  JOURNAL   Nature 419 (6903), 182-185 (2002)
   PUBMED   12226669
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Will,C.L., Schneider,C., MacMillan,A.M., Katopodis,N.F.,
            Neubauer,G., Wilm,M., Luhrmann,R. and Query,C.C.
  TITLE     A novel U2 and U11/U12 snRNP protein that associates with the
            pre-mRNA branch site
  JOURNAL   EMBO J 20 (16), 4536-4546 (2001)
   PUBMED   11500380
REFERENCE   9  (residues 1 to 125)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC015463.1 and BG200650.1.
            
            Summary: This gene encodes a 14 kDa protein subunit of the splicing
            factor 3b complex. Splicing factor 3b associates with both the U2
            and U11/U12 small nuclear ribonucleoprotein complexes (U2 snRNP) of
            spliceosomes. This 14 kDa protein interacts directly with subunit 1
            of the splicing factor 3b complex. This 14 kDa protein also
            interacts directly with the adenosine that carries out the first
            transesterification step of splicing at the pre-mRNA branch site.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.172119.1,
                                           SRR1163657.34312.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000233468.5/ ENSP00000233468.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..125
                     /product="splicing factor 3B subunit 6"
                     /note="spliceosome-associated protein, 14 kDa subunit;
                     pre-mRNA branch site protein p14; SF3b 14 kDa subunit;
                     splicing factor 3B, 14 kDa subunit; spliceosome-associated
                     protein, 14-kDa; splicing factor 3b, subunit 6, 14kDa"
                     /calculated_mol_wt=14454
     Region          16..29
                     /region_name="Interaction with pre-mRNA branch site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3B4.1)"
     Region          17..93
                     /region_name="RRM_SF3B14"
                     /note="RNA recognition motif (RRM) found in pre-mRNA
                     branch site protein p14 (SF3B14) and similar proteins;
                     cd12241"
                     /db_xref="CDD:409687"
     Site            order(17,19..20,22,32,46..53,56,59,61,65..67,92)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409687"
     Site            order(22,61,91..93)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409687"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3B4.1)"
     Site            41
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3B4.1)"
     CDS             1..125
                     /gene="SF3B6"
                     /gene_synonym="CGI-110; HSPC175; Ht006; P14; SAP14;
                     SAP14a; SF3B14; SF3B14a"
                     /coded_by="NM_016047.4:98..475"
                     /db_xref="CCDS:CCDS1707.1"
                     /db_xref="GeneID:51639"
                     /db_xref="HGNC:HGNC:30096"
                     /db_xref="MIM:607835"
ORIGIN      
        1 mamqaakran irlppevnri lyirnlpyki taeemydifg kygpirqirv gntpetrgta
       61 yvvyedifda knacdhlsgf nvcnrylvvl yynanrafqk mdtkkkeeql kllkekygin
      121 tdppk
//
LOCUS       NP_000658                375 aa            linear   PRI 27-APR-2025
DEFINITION  alcohol dehydrogenase 1A [Homo sapiens].
ACCESSION   NP_000658
VERSION     NP_000658.1
DBSOURCE    REFSEQ: accession NM_000667.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Khmelinskii,I. and Makarov,V.I.
  TITLE     Contrary to consensus, oxidation of ethanol by human alcohol
            dehydrogenase (ADH) 1A is activated by ATP
  JOURNAL   Biochimie 195, 67-70 (2022)
   PUBMED   34742856
  REMARK    GeneRIF: Contrary to consensus, oxidation of ethanol by human
            alcohol dehydrogenase (ADH) 1A is activated by ATP.
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Lee,Y.J., Yoo,M.G., Kim,H.K., Jang,H.B., Park,K.J., Lee,H.J.,
            Kim,S.G. and Park,S.I.
  TITLE     The association between alcohol metabolism and genetic variants of
            ADH1A, SRPRB, and PGM1 in Korea
  JOURNAL   Alcohol 79, 137-145 (2019)
   PUBMED   31002879
  REMARK    GeneRIF: Variation of ADH1A was significantly associated with blood
            acetaldehyde concentrations, which may contribute to slow alcohol
            metabolism and result in increased blood acetaldehyde levels in
            Korean subjects.
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Cui,Q., Peng,L., Wei,L., Chang,J., Tan,W., Luo,Y., Huang,X.,
            Zhao,Y., Li,J., Chu,J., Shao,M., Zhang,C., Li,C., Tan,W., Lin,D.
            and Wu,C.
  TITLE     Genetic variant repressing ADH1A expression confers susceptibility
            to esophageal squamous-cell carcinoma
  JOURNAL   Cancer Lett 421, 43-50 (2018)
   PUBMED   29248712
  REMARK    GeneRIF: We demonstrated for the first time that rs1154402C>G
            change in in intron 1 of ADH5 might create a silencer, repressing
            ADH1A transcription via long-range interaction with ADH1A promoter
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Jelski,W., Wolszczak-Biedrzycka,B., Zasimowicz-Majewska,E.,
            Orywal,K., Piechota,J., Lapinski,T.W., Bednarczyk,M. and
            Szmitkowski,M.
  TITLE     The Activity of Alcohol Dehydrogenase Isoenzymes and Aldehyde
            Dehydrogenase in the Sera of Patients with Autoimmune Hepatitis
  JOURNAL   Clin Lab 64 (4), 477-481 (2018)
   PUBMED   29739065
  REMARK    GeneRIF: The activity of total alcohol dehydrogenase (ADH) and
            class I isoenzymes in the sera of autoimmune hepatitis patients is
            increased and aldehyde dehydrogenase (ALDH) levels were unchanged.
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Orywal,K., Jelski,W., Werel,T. and Szmitkowski,M.
  TITLE     The Diagnostic Significance of Serum Alcohol Dehydrogenase
            Isoenzymes and Aldehyde Dehydrogenase Activity in Prostate Cancer
            Patients
  JOURNAL   Anticancer Res 37 (9), 4961-4965 (2017)
   PUBMED   28870918
  REMARK    GeneRIF: High ADH expression is associated with Prostate Cancer.
REFERENCE   6  (residues 1 to 375)
  AUTHORS   van Ooij,C., Snyder,R.C., Paeper,B.W. and Duester,G.
  TITLE     Temporal expression of the human alcohol dehydrogenase gene family
            during liver development correlates with differential promoter
            activation by hepatocyte nuclear factor 1, CCAAT/enhancer-binding
            protein alpha, liver activator protein, and D-element-binding
            protein
  JOURNAL   Mol Cell Biol 12 (7), 3023-3031 (1992)
   PUBMED   1620113
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Stewart,M.J., McBride,M.S., Winter,L.A. and Duester,G.
  TITLE     Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and
            ADH3: interaction of CCAAT/enhancer-binding protein with elements
            flanking the ADH2 TATA box
  JOURNAL   Gene 90 (2), 271-279 (1990)
   PUBMED   2169444
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Yasunami,M., Kikuchi,I., Sarapata,D. and Yoshida,A.
  TITLE     The human class I alcohol dehydrogenase gene cluster: three genes
            are tandemly organized in an 80-kb-long segment of the genome
  JOURNAL   Genomics 7 (2), 152-158 (1990)
   PUBMED   2347582
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Tsukahara,M. and Yoshida,A.
  TITLE     Chromosomal assignment of the alcohol dehydrogenase cluster locus
            to human chromosome 4q21-23 by in situ hybridization
  JOURNAL   Genomics 4 (2), 218-220 (1989)
   PUBMED   2737681
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Lange,L.G., Sytkowski,A.J. and Vallee,B.L.
  TITLE     Human liver alcohol dehydrogenase: purification, composition, and
            catalytic features
  JOURNAL   Biochemistry 15 (21), 4687-4693 (1976)
   PUBMED   9982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290558.1.
            
            Summary: This gene encodes a member of the alcohol dehydrogenase
            family. The encoded protein is the alpha subunit of class I alcohol
            dehydrogenase, which consists of several homo- and heterodimers of
            alpha, beta and gamma subunits. Alcohol dehydrogenases catalyze the
            oxidation of alcohols to aldehydes. This gene is active in the
            liver in early fetal life but only weakly active in adult liver.
            This gene is found in a cluster with six additional alcohol
            dehydrogenase genes, including those encoding the beta and gamma
            subunits, on the long arm of chromosome 4. Mutations in this gene
            may contribute to variation in certain personality traits and
            substance dependence. [provided by RefSeq, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290558.1, M12963.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000209668.3/ ENSP00000209668.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..375
                     /product="alcohol dehydrogenase 1A"
                     /EC_number="1.1.1.1"
                     /note="ADH, alpha subunit; alcohol dehydrogenase 1 (class
                     I), alpha polypeptide; aldehyde reductase; alcohol
                     dehydrogenase subunit alpha"
                     /calculated_mol_wt=39728
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:3013304; propagated from
                     UniProtKB/Swiss-Prot (P07327.2)"
     Region          3..375
                     /region_name="alcohol_DH_class_I_II_IV"
                     /note="class I, II, IV alcohol dehydrogenases; cd08299"
                     /db_xref="CDD:176259"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00325; propagated from
                     UniProtKB/Swiss-Prot (P07327.2)"
     Site            order(47,68,175)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176259"
     Site            order(48..49,175,179,200..204,224..225,229,269..270,
                     274..275,293..294,318..320,370)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176259"
     Site            order(49,68,94,117,142,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176259"
     Site            order(98..99,101,104,112)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176259"
     Site            order(102..103,106,111,261..262,273,286..287,292..293,
                     301..306,309..319)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176259"
     CDS             1..375
                     /gene="ADH1A"
                     /gene_synonym="ADH1"
                     /coded_by="NM_000667.4:72..1199"
                     /db_xref="CCDS:CCDS3648.1"
                     /db_xref="GeneID:124"
                     /db_xref="HGNC:HGNC:249"
                     /db_xref="MIM:103700"
ORIGIN      
        1 mstagkvikc kaavlwelkk pfsieeveva ppkahevrik mvavgicgtd dhvvsgtmvt
       61 plpvilghea agivesvgeg vttvkpgdkv iplaipqcgk cricknpesn yclkndvsnp
      121 qgtlqdgtsr ftcrrkpihh flgistfsqy tvvdenavak idaasplekv cligcgfstg
      181 ygsavnvakv tpgstcavfg lggvglsaim gckaagaari iavdinkdkf akakelgate
      241 cinpqdykkp iqevlkemtd ggvdfsfevi grldtmmasl lccheacgts vivgvppdsq
      301 nlsmnpmlll tgrtwkgail ggfkskecvp klvadfmakk fsldalithv lpfekinegf
      361 dllhsgksir tilmf
//
LOCUS       NP_003603                666 aa            linear   PRI 27-APR-2025
DEFINITION  semaphorin-7A isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_003603
VERSION     NP_003603.1
DBSOURCE    REFSEQ: accession NM_003612.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Huang,J., Zhao,C. and Zhang,S.
  TITLE     Semaphorin 7A promotes endothelial permeability and inflammation
            via plexin C1 and integrin beta1 in Kawasaki disease
  JOURNAL   BMC Pediatr 24 (1), 285 (2024)
   PUBMED   38678170
  REMARK    GeneRIF: Semaphorin 7A promotes endothelial permeability and
            inflammation via plexin C1 and integrin beta1 in Kawasaki disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Scott,G.A., McClelland,L.A., Fricke,A.F. and Fender,A.
  TITLE     Plexin C1, a receptor for semaphorin 7a, inactivates cofilin and is
            a potential tumor suppressor for melanoma progression
  JOURNAL   J Invest Dermatol 129 (4), 954-963 (2009)
   PUBMED   18987670
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Scott,G.A., McClelland,L.A. and Fricke,A.F.
  TITLE     Semaphorin 7a promotes spreading and dendricity in human
            melanocytes through beta1-integrins
  JOURNAL   J Invest Dermatol 128 (1), 151-161 (2008)
   PUBMED   17671519
  REMARK    GeneRIF: beta1-integrins and Plexin C1 receptors are ligands for
            Semaphorin 7a, and that signaling by these receptors has opposing
            effects on Semaphorin 7a-induced dendrite formation.
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Koh,J.M., Oh,B., Lee,J.Y., Lee,J.K., Kimm,K., Kim,G.S., Park,B.L.,
            Cheong,H.S., Shin,H.D., Hong,J.M., Kim,T.H., Park,E.K. and Kim,S.Y.
  TITLE     Association study of semaphorin 7a (sema7a) polymorphisms with bone
            mineral density and fracture risk in postmenopausal Korean women
  JOURNAL   J Hum Genet 51 (2), 112-117 (2006)
   PUBMED   16372136
  REMARK    GeneRIF: Polymorphisms in SEMA7A may play a role in decreased bone
            mineral density and increased risk of vertebral fracture.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Maurin,J.C., Delorme,G., Machuca-Gayet,I., Couble,M.L.,
            Magloire,H., Jurdic,P. and Bleicher,F.
  TITLE     Odontoblast expression of semaphorin 7A during innervation of human
            dentin
  JOURNAL   Matrix Biol 24 (3), 232-238 (2005)
   PUBMED   15907379
  REMARK    GeneRIF: SEMA 7A might be a molecule involved in the terminal
            innervation of the dentin-pulp complex.
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Holmes,S., Downs,A.M., Fosberry,A., Hayes,P.D., Michalovich,D.,
            Murdoch,P., Moores,K., Fox,J., Deen,K., Pettman,G., Wattam,T. and
            Lewis,C.
  TITLE     Sema7A is a potent monocyte stimulator
  JOURNAL   Scand J Immunol 56 (3), 270-275 (2002)
   PUBMED   12193228
  REMARK    GeneRIF: Sema7A is a potent stimulator of cytokine production,
            chemotaxis and superoxide release in monocytes
REFERENCE   7  (residues 1 to 666)
  AUTHORS   Angelisova,P., Drbal,K., Cerny,J., Hilgert,I. and Horejsi,V.
  TITLE     Characterization of the human leukocyte GPI-anchored glycoprotein
            CDw108 and its relation to other similar molecules
  JOURNAL   Immunobiology 200 (2), 234-245 (1999)
   PUBMED   10416131
REFERENCE   8  (residues 1 to 666)
  AUTHORS   Yamada,A., Kubo,K., Takeshita,T., Harashima,N., Kawano,K., Mine,T.,
            Sagawa,K., Sugamura,K. and Itoh,K.
  TITLE     Molecular cloning of a glycosylphosphatidylinositol-anchored
            molecule CDw108
  JOURNAL   J Immunol 162 (7), 4094-4100 (1999)
   PUBMED   10201933
REFERENCE   9  (residues 1 to 666)
  AUTHORS   Xu,X., Ng,S., Wu,Z.L., Nguyen,D., Homburger,S., Seidel-Dugan,C.,
            Ebens,A. and Luo,Y.
  TITLE     Human semaphorin K1 is glycosylphosphatidylinositol-linked and
            defines a new subfamily of viral-related semaphorins
  JOURNAL   J Biol Chem 273 (35), 22428-22434 (1998)
   PUBMED   9712866
REFERENCE   10 (residues 1 to 666)
  AUTHORS   Lange,C., Liehr,T., Goen,M., Gebhart,E., Fleckenstein,B. and
            Ensser,A.
  TITLE     New eukaryotic semaphorins with close homology to semaphorins of
            DNA viruses
  JOURNAL   Genomics 51 (3), 340-350 (1998)
   PUBMED   9721204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK312257.1, AK001895.1,
            AC090826.15, BF792612.1 and AI972833.1.
            
            Summary: This gene encodes a member of the semaphorin family of
            proteins. The encoded preproprotein is proteolytically processed to
            generate the mature glycosylphosphatidylinositol (GPI)-anchored
            membrane glycoprotein. The encoded protein is found on activated
            lymphocytes and erythrocytes and may be involved in
            immunomodulatory and neuronal processes. The encoded protein
            carries the John Milton Hagen (JMH) blood group antigens. Mutations
            in this gene may be associated with reduced bone mineral density
            (BMD). Alternative splicing results in multiple transcript
            variants, at least one of which encodes an isoform that is
            proteolytically processed. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record represents the SEMA7A*001.1.1
            allele.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK312257.1, AF069493.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261918.9/ ENSP00000261918.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..666
                     /product="semaphorin-7A isoform 1 preproprotein"
                     /note="sema domain, immunoglobulin domain (Ig), and GPI
                     membrane anchor, (semaphorin) 7A (JMH blood group); John
                     Milton Hagen blood group H-Sema K1; sema domain,
                     immunoglobulin domain (Ig), and GPI membrane anchor, 7A;
                     semaphorin 7A (John Milton Hagen blood group);
                     semaphorin-7A; sema L; sema K1; semaphorin-K1;
                     semaphorin-L; JMH blood group antigen; john-Milton-Hargen
                     human blood group Ag; semaphorin 7A, GPI membrane anchor
                     (John Milton Hagen blood group)"
                     /calculated_mol_wt=70324
     sig_peptide     1..44
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75326.1)"
                     /calculated_mol_wt=4519
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75326.1)"
     mat_peptide     45..648
                     /product="Semaphorin-7A. /id=PRO_0000032347"
                     /note="propagated from UniProtKB/Swiss-Prot (O75326.1)"
                     /calculated_mol_wt=68438
     Region          72..491
                     /region_name="Sema_7A"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 7A (Sema7A, also called CD108); cd11243"
                     /db_xref="CDD:200504"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20727575; propagated from
                     UniProtKB/Swiss-Prot (O75326.1)"
     Site            order(121..124,167..168,172,193,195..196,203,210,213..214,
                     216,221,249,273..276,278,280,375,379,382)
                     /site_type="other"
                     /note="putative plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200504"
     Site            135
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUR8; propagated from
                     UniProtKB/Swiss-Prot (O75326.1)"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20727575; propagated from
                     UniProtKB/Swiss-Prot (O75326.1)"
     Site            order(250..251,253,256..258,293,296..298,300,302,327..331,
                     388,405)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200504"
     Site            258
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20727575; propagated from
                     UniProtKB/Swiss-Prot (O75326.1)"
     Region          267..269
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75326.1)"
     Region          267..269
                     /region_name="Interaction with integrins"
                     /note="propagated from UniProtKB/Swiss-Prot (O75326.1)"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20727575; propagated from
                     UniProtKB/Swiss-Prot (O75326.1)"
     Region          493..>520
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          549..619
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          562..566
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409456"
     Region          574..578
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409456"
     Region          596..600
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409456"
     Site            602
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:10201933; propagated from
                     UniProtKB/Swiss-Prot (O75326.1)"
     Region          610..615
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409456"
     CDS             1..666
                     /gene="SEMA7A"
                     /gene_synonym="CD108; CDw108; H-SEMA-K1; H-Sema-L; JMH;
                     PFIC11; SEMAK1; SEMAL"
                     /coded_by="NM_003612.5:41..2041"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10262.1"
                     /db_xref="GeneID:8482"
                     /db_xref="HGNC:HGNC:10741"
                     /db_xref="MIM:607961"
ORIGIN      
        1 mtppppgraa psaprarvpg pparlglplr lrlllllwaa aasaqghlrs gprifavwkg
       61 hvgqdrvdfg qtephtvlfh epgsssvwvg grgkvylfdf pegknasvrt vnigstkgsc
      121 ldkrdcenyi tllerrsegl lacgtnarhp scwnlvngtv vplgemrgya pfspdenslv
      181 lfegdevyst irkqeyngki prfrrirges elytsdtvmq npqfikativ hqdqayddki
      241 yyffrednpd knpeaplnvs rvaqlcrgdq ggesslsvsk wntflkamlv csdaatnknf
      301 nrlqdvfllp dpsgqwrdtr vygvfsnpwn ysavcvyslg didkvfrtss lkgyhsslpn
      361 prpgkclpdq qpiptetfqv adrhpevaqr vepmgplktp lfhskyhyqk vavhrmqash
      421 getfhvlylt tdrgtihkvv epgeqehsfa fnimeiqpfr raaaiqtmsl daerrklyvs
      481 sqwevsqvpl dlcevygggc hgclmsrdpy cgwdqgrcis iyssersvlq sinpaephke
      541 cpnpkpdkap lqkvslapns ryylscpmes rhatyswrhk enveqscepg hqspncilfi
      601 enltaqqygh yfceaqegsy freaqhwqll pedgimaehl lghacalaas lwlgvlptlt
      661 lgllvh
//
LOCUS       NP_006234                486 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
            alpha isoform isoform 1 [Homo sapiens].
ACCESSION   NP_006234
VERSION     NP_006234.1
DBSOURCE    REFSEQ: accession NM_006243.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Ambjorn,S.M., Duxin,J.P., Hertz,E.P.T., Nasa,I., Duro,J., Kruse,T.,
            Lopez-Mendez,B., Rymarczyk,B., Cressey,L.E., van Overeem Hansen,T.,
            Kettenbach,A.N., Oestergaard,V.H., Lisby,M. and Nilsson,J.
  TITLE     A complex of BRCA2 and PP2A-B56 is required for DNA repair by
            homologous recombination
  JOURNAL   Nat Commun 12 (1), 5748 (2021)
   PUBMED   34593815
  REMARK    GeneRIF: A complex of BRCA2 and PP2A-B56 is required for DNA repair
            by homologous recombination.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Salamango,D.J., McCann,J.L., Demir,O., Becker,J.T., Wang,J.,
            Lingappa,J.R., Temiz,N.A., Brown,W.L., Amaro,R.E. and Harris,R.S.
  TITLE     Functional and Structural Insights into a Vif/PPP2R5 Complex
            Elucidated Using Patient HIV-1 Isolates and Computational Modeling
  JOURNAL   J Virol 94 (21), e00631-20 (2020)
   PUBMED   32847850
  REMARK    GeneRIF: Functional and Structural Insights into a Vif/PPP2R5
            Complex Elucidated Using Patient HIV-1 Isolates and Computational
            Modeling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 486)
  AUTHORS   McCright,B., Rivers,A.M., Audlin,S. and Virshup,D.M.
  TITLE     The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
            encodes differentiation-induced phosphoproteins that target PP2A to
            both nucleus and cytoplasm
  JOURNAL   J Biol Chem 271 (36), 22081-22089 (1996)
   PUBMED   8703017
REFERENCE   7  (residues 1 to 486)
  AUTHORS   McCright,B., Brothman,A.R. and Virshup,D.M.
  TITLE     Assignment of human protein phosphatase 2A regulatory subunit genes
            b56alpha, b56beta, b56gamma, b56delta, and b56epsilon
            (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to
            chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 --> p12
  JOURNAL   Genomics 36 (1), 168-170 (1996)
   PUBMED   8812429
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Fuhrer,D.K. and Yang,Y.C.
  TITLE     Complex formation of JAK2 with PP2A, P13K, and Yes in response to
            the hematopoietic cytokine interleukin-11
  JOURNAL   Biochem Biophys Res Commun 224 (2), 289-296 (1996)
   PUBMED   8702385
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Zolnierowicz,S., Van Hoof,C., Andjelkovic,N., Cron,P., Stevens,I.,
            Merlevede,W., Goris,J. and Hemmings,B.A.
  TITLE     The variable subunit associated with protein phosphatase 2A0
            defines a novel multimember family of regulatory subunits
  JOURNAL   Biochem J 317 (Pt 1) (Pt 1), 187-194 (1996)
   PUBMED   8694763
REFERENCE   10 (residues 1 to 486)
  AUTHORS   McCright,B. and Virshup,D.M.
  TITLE     Identification of a new family of protein phosphatase 2A regulatory
            subunits
  JOURNAL   J Biol Chem 270 (44), 26123-26128 (1995)
   PUBMED   7592815
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL451060.13 and L42373.1.
            
            Summary: The product of this gene belongs to the phosphatase 2A
            regulatory subunit B family. Protein phosphatase 2A is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes an alpha isoform of the regulatory subunit B56 subfamily.
            Alternative transcript variants encoding distinct isoforms have
            been found for this gene. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110883.1, L42373.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261461.7/ ENSP00000261461.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..486
                     /product="serine/threonine-protein phosphatase 2A 56 kDa
                     regulatory subunit alpha isoform isoform 1"
                     /note="PR61alpha; protein phosphatase 2 regulatory subunit
                     B', alpha"
                     /calculated_mol_wt=56063
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15172.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q15172.1)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15172.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15172.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15172.1)"
     Region          64..442
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); pfam01603"
                     /db_xref="CDD:460264"
     CDS             1..486
                     /gene="PPP2R5A"
                     /gene_synonym="B56A; B56alpha; PR61A"
                     /coded_by="NM_006243.4:702..2162"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1503.1"
                     /db_xref="GeneID:5525"
                     /db_xref="HGNC:HGNC:9309"
                     /db_xref="MIM:601643"
ORIGIN      
        1 mssssppaga asaaisasek vdgftrksvr kaqrqkrsqg ssqfrsqgsq aelhplpqlk
       61 datsneqqel fcqklqqcci lfdfmdsvsd lkskeikrat lnelveyvst nrgvivesay
      121 sdivkmisan ifrtlppsdn pdfdpeedep tleaswphiq lvyefflrfl espdfqpsia
      181 kryidqkfvq qllelfdsed prerdflktv lhriygkflg lrafirkqin niflrfiyet
      241 ehfngvaell eilgsiingf alplkaehkq flmkvlipmh takglalfha qlaycvvqfl
      301 ekdttltepv irgllkfwpk tcsqkevmfl geieeildvi eptqfkkiee plfkqiskcv
      361 ssshfqvaer alyfwnneyi lslieenidk ilpimfasly kiskehwnpt ivalvynvlk
      421 tlmemngklf ddltssykae rqrekkkele reelwkklee lklkkalekq nsaynmhsil
      481 sntsae
//
LOCUS       NP_057400               1251 aa            linear   PRI 27-APR-2025
DEFINITION  DNA repair protein REV1 isoform 1 [Homo sapiens].
ACCESSION   NP_057400
VERSION     NP_057400.1
DBSOURCE    REFSEQ: accession NM_016316.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1251)
  AUTHORS   Zhu,N., Ding,Y., Mi,M., Yang,J., Yang,M., Li,D., Zhang,Y., Fang,X.,
            Weng,S. and Yuan,Y.
  TITLE     Loss-of-function mutation of REV1 (p.R704Q) mediates cetuximab
            primary resistance by activating autophagy in RAS-wild type
            metastatic colorectal cancer
  JOURNAL   Cancer Lett 598, 217103 (2024)
   PUBMED   38969162
  REMARK    GeneRIF: Loss-of-function mutation of REV1 (p.R704Q) mediates
            cetuximab primary resistance by activating autophagy in RAS-wild
            type metastatic colorectal cancer.
REFERENCE   2  (residues 1 to 1251)
  AUTHORS   Stolyarenko,A.D., Novikova,A.A., Shilkin,E.S., Poltorachenko,V.A.
            and Makarova,A.V.
  TITLE     The Catalytic Activity of Human REV1 on Undamaged and Damaged DNA
  JOURNAL   Int J Mol Sci 25 (7), 4107 (2024)
   PUBMED   38612916
  REMARK    GeneRIF: The Catalytic Activity of Human REV1 on Undamaged and
            Damaged DNA.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1251)
  AUTHORS   Chen,Y., Jie,X., Xing,B., Wu,Z., Yang,X., Rao,X., Xu,Y., Zhou,D.,
            Dong,X., Zhang,T., Yang,K., Li,Z. and Wu,G.
  TITLE     REV1 promotes lung tumorigenesis by activating the Rad18/SERTAD2
            axis
  JOURNAL   Cell Death Dis 13 (2), 110 (2022)
   PUBMED   35115490
  REMARK    GeneRIF: REV1 promotes lung tumorigenesis by activating the
            Rad18/SERTAD2 axis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1251)
  AUTHORS   Bi,T., Niu,X., Qin,C. and Xiao,W.
  TITLE     Genetic and physical interactions between Poleta and Rev1 in
            response to UV-induced DNA damage in mammalian cells
  JOURNAL   Sci Rep 11 (1), 21364 (2021)
   PUBMED   34725419
  REMARK    GeneRIF: Genetic and physical interactions between Poleta and Rev1
            in response to UV-induced DNA damage in mammalian cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1251)
  AUTHORS   Taglialatela,A., Leuzzi,G., Sannino,V., Cuella-Martin,R.,
            Huang,J.W., Wu-Baer,F., Baer,R., Costanzo,V. and Ciccia,A.
  TITLE     REV1-Polzeta maintains the viability of homologous
            recombination-deficient cancer cells through mutagenic repair of
            PRIMPOL-dependent ssDNA gaps
  JOURNAL   Mol Cell 81 (19), 4008-4025 (2021)
   PUBMED   34508659
  REMARK    GeneRIF: REV1-Polzeta maintains the viability of homologous
            recombination-deficient cancer cells through mutagenic repair of
            PRIMPOL-dependent ssDNA gaps.
REFERENCE   6  (residues 1 to 1251)
  AUTHORS   Masuda,Y., Takahashi,M., Tsunekuni,N., Minami,T., Sumii,M.,
            Miyagawa,K. and Kamiya,K.
  TITLE     Deoxycytidyl transferase activity of the human REV1 protein is
            closely associated with the conserved polymerase domain
  JOURNAL   J Biol Chem 276 (18), 15051-15058 (2001)
   PUBMED   11278384
REFERENCE   7  (residues 1 to 1251)
  AUTHORS   Wixler,V., Geerts,D., Laplantine,E., Westhoff,D., Smyth,N.,
            Aumailley,M., Sonnenberg,A. and Paulsson,M.
  TITLE     The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of
            several alpha and beta integrin chains and is recruited to adhesion
            complexes
  JOURNAL   J Biol Chem 275 (43), 33669-33678 (2000)
   PUBMED   10906324
REFERENCE   8  (residues 1 to 1251)
  AUTHORS   Gibbs,P.E., Wang,X.D., Li,Z., McManus,T.P., McGregor,W.G.,
            Lawrence,C.W. and Maher,V.M.
  TITLE     The function of the human homolog of Saccharomyces cerevisiae REV1
            is required for mutagenesis induced by UV light
  JOURNAL   Proc Natl Acad Sci U S A 97 (8), 4186-4191 (2000)
   PUBMED   10760286
REFERENCE   9  (residues 1 to 1251)
  AUTHORS   Lin,W., Xin,H., Zhang,Y., Wu,X., Yuan,F. and Wang,Z.
  TITLE     The human REV1 gene codes for a DNA template-dependent dCMP
            transferase
  JOURNAL   Nucleic Acids Res 27 (22), 4468-4475 (1999)
   PUBMED   10536157
REFERENCE   10 (residues 1 to 1251)
  AUTHORS   Wixler,V., Laplantine,E., Geerts,D., Sonnenberg,A., Petersohn,D.,
            Eckes,B., Paulsson,M. and Aumailley,M.
  TITLE     Identification of novel interaction partners for the conserved
            membrane proximal region of alpha-integrin cytoplasmic domains
  JOURNAL   FEBS Lett 445 (2-3), 351-355 (1999)
   PUBMED   10094488
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY010913.1, AF151538.1,
            AC018690.5 and BM683065.1.
            
            Summary: This gene encodes a protein with similarity to the S.
            cerevisiae mutagenesis protein Rev1. The Rev1 proteins contain a
            BRCT domain, which is important in protein-protein interactions. A
            suggested role for the human Rev1-like protein is as a scaffold
            that recruits DNA polymerases involved in translesion synthesis
            (TLS) of damaged DNA. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.2340.1,
                                           SRR1803614.166936.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258428.8/ ENSP00000258428.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..1251
                     /product="DNA repair protein REV1 isoform 1"
                     /note="REV1- like; DNA repair protein REV1; alpha
                     integrin-binding protein 80; rev1-like terminal
                     deoxycytidyl transferase; REV1 homolog; REV1, polymerase
                     (DNA directed)"
                     /calculated_mol_wt=138118
     Region          48..131
                     /region_name="BRCT_Rev1"
                     /note="BRCT domain of DNA repair protein Rev1 and similar
                     proteins; cd17719"
                     /db_xref="CDD:349351"
     Region          206..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Region          282..342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Region          348..824
                     /region_name="PolY_Rev1"
                     /note="DNA polymerase Rev1; cd01701"
                     /db_xref="CDD:176455"
     Site            order(351..353,355..359,361..362,369,423..428,448,
                     509..510,513,516,522..523,525,567..568,570..571,625,
                     649..656,659,685..686,710..718,752,773..775,779..783,785)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176455"
     Region          352..362
                     /region_name="Interaction with target DNA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Site            order(357,423..428,509..510,513,516,522,570..571,625)
                     /site_type="active"
                     /db_xref="CDD:176455"
     Region          653..656
                     /region_name="Interaction with target DNA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Region          709..717
                     /region_name="Interaction with target DNA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Site            770
                     /site_type="other"
                     /note="Interaction with target DNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Site            783
                     /site_type="other"
                     /note="Interaction with target DNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Region          929..962
                     /region_name="Rev1_UBM2"
                     /note="Ubiquitin-Binding Motif 2 (UBM2) of Y-family
                     polymerase Rev1; cd19318"
                     /db_xref="CDD:412037"
     Site            order(931..933,937..939,941..942,945..947,949..950,953,
                     957)
                     /site_type="other"
                     /note="ubiquitin binding interface [polypeptide binding]"
                     /db_xref="CDD:412037"
     Region          1005..1040
                     /region_name="Rev1_UBM2"
                     /note="Ubiquitin-Binding Motif 2 (UBM2) of Y-family
                     polymerase Rev1; cd19318"
                     /db_xref="CDD:412037"
     Site            order(1009..1011,1015..1017,1019..1020,1023..1025,
                     1027..1028,1031,1035)
                     /site_type="other"
                     /note="ubiquitin binding interface [polypeptide binding]"
                     /db_xref="CDD:412037"
     Region          1035..1096
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Region          1071..1078
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Region          1119..1147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Region          1150..1249
                     /region_name="Protein interaction domain, mediates
                     interaction with DNA polymerase zeta"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBZ9.1)"
     Region          1157..1250
                     /region_name="Rev1_C"
                     /note="C-terminal domain of the Y-family polymerase Rev1;
                     cd12145"
                     /db_xref="CDD:213388"
     Site            order(1158..1163,1171..1172,1175,1179,1181..1183,
                     1185..1186,1189..1190)
                     /site_type="other"
                     /note="Polymerase eta interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:213388"
     CDS             1..1251
                     /gene="REV1"
                     /gene_synonym="AIBP80; REV1L"
                     /coded_by="NM_016316.4:212..3967"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2045.1"
                     /db_xref="GeneID:51455"
                     /db_xref="HGNC:HGNC:14060"
                     /db_xref="MIM:606134"
ORIGIN      
        1 mrrggwrkra endgwetwgg ymaakvqkle eqfrsdaamq kdgtsstifs gvaiyvngyt
       61 dpsaeelrkl mmlhggqyhv yysrsktthi iatnlpnaki kelkgekvir pewivesika
      121 grllsyipyq lytkqssvqk glsfnpvcrp edplpgpsni akqlnnrvnh ivkkietene
      181 vkvngmnswn eedenndfsf vdleqtspgr kqngiphprg staifnghtp ssngalktqd
      241 clvpmvnsva srlspafsqe edkaeksstd frdctlqqlq qstrntdalr nphrtnsfsl
      301 splhsntkin gahhstvqgp sstkstssvs tfskaapsvp skpsdcnfis nfyshsrlhh
      361 ismwkcelte fvntlqrqsn gifpgreklk kmktgrsalv vtdtgdmsvl nsprhqscim
      421 hvdmdcffvs vgirnrpdlk gkpvavtsnr gtgraplrpg anpqlewqyy qnkilkgkaa
      481 dipdsslwen pdsaqangid svlsraeias csyearqlgi kngmffghak qlcpnlqavp
      541 ydfhaykeva qtlyetlasy thnieavscd ealvditeil aetkltpdef anavrmeikd
      601 qtkcaasvgi gsnillarma trkakpdgqy hlkpeevddf irgqlvtnlp gvghsmeskl
      661 aslgiktcgd lqymtmaklq kefgpktgqm lyrfcrgldd rpvrtekerk svsaeinygi
      721 rftqpkeaea fllslseeiq rrleatgmkg krltlkimvr kpgapvetak fgghgicdni
      781 artvtldqat dnakiigkam lnmfhtmkln isdmrgvgih vnqlvptnln pstcpsrpsv
      841 qsshfpsgsy svrdvfqvqk akksteeehk evfraavdle issasrtctf lppfpahlpt
      901 spdtnkaess gkwnglhtpv svqsrlnlsi evpspsqldq svlealppdl reqveqvcav
      961 qqaeshgdkk kepvngcntg ilpqpvgtvl lqipepqesn sdaginlial pafsqvdpev
     1021 faalpaelqr elkaaydqrq rqgensthqq sasasvpknp llhlkaavke kkrnkkkkti
     1081 gspkriqspl nnkllnspak tlpgacgspq klidgflkhe gppaekplee lsastsgvpg
     1141 lsslqsdpag cvrppapnla gavefndvkt llrewittis dpmeedilqv vkyctdliee
     1201 kdlekldlvi kymkrlmqqs vesvwnmafd fildnvqvvl qqtygstlkv t
//
LOCUS       NP_000175                147 aa            linear   PRI 27-APR-2025
DEFINITION  hemoglobin subunit gamma-2 [Homo sapiens].
ACCESSION   NP_000175
VERSION     NP_000175.1
DBSOURCE    REFSEQ: accession NM_000184.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Kotepui,M., Mahittikorn,A., Wilairatana,P., Masangkay,F.R.,
            Wangdi,K. and Kotepui,K.U.
  TITLE     Methemoglobin levels in malaria: a systematic review and
            meta-analysis of its association with Plasmodium falciparum and
            Plasmodium vivax infections and disease severity
  JOURNAL   Sci Rep 14 (1), 3276 (2024)
   PUBMED   38332023
  REMARK    GeneRIF: Methemoglobin levels in malaria: a systematic review and
            meta-analysis of its association with Plasmodium falciparum and
            Plasmodium vivax infections and disease severity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Vardar,G., Rzayev,T., Tezel,K.G. and Ozek,E.
  TITLE     Can We Estimate Late-Onset Sepsis by Serial Methemoglobin Levels?
            An Observational Study in Preterm Neonates
  JOURNAL   Fetal Pediatr Pathol 42 (5), 753-765 (2023)
   PUBMED   37318102
  REMARK    GeneRIF: Can We Estimate Late-Onset Sepsis by Serial Methemoglobin
            Levels? An Observational Study in Preterm Neonates.
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Lin,J., Ye,Y., Shang,X., Zhang,Y., Wei,X. and Xu,X.
  TITLE     TEA domain transcription factor 4 modulates repression of fetal
            haemoglobin by direct binding to the gamma-globin gene promoters
  JOURNAL   Br J Haematol 195 (5), 764-769 (2021)
   PUBMED   34569056
  REMARK    GeneRIF: TEA domain transcription factor 4 modulates repression of
            fetal haemoglobin by direct binding to the gamma-globin gene
            promoters.
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Eernstman,J., Veldhuisen,B., Ligthart,P., von Lindern,M., van der
            Schoot,C.E. and van den Akker,E.
  TITLE     Novel variants in Krueppel like factor 1 that cause persistence of
            fetal hemoglobin in In(Lu) individuals
  JOURNAL   Sci Rep 11 (1), 18557 (2021)
   PUBMED   34535703
  REMARK    GeneRIF: Novel variants in Krueppel like factor 1 that cause
            persistence of fetal hemoglobin in In(Lu) individuals.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Doerfler,P.A., Feng,R., Li,Y., Palmer,L.E., Porter,S.N., Bell,H.W.,
            Crossley,M., Pruett-Miller,S.M., Cheng,Y. and Weiss,M.J.
  TITLE     Activation of gamma-globin gene expression by GATA1 and NF-Y in
            hereditary persistence of fetal hemoglobin
  JOURNAL   Nat Genet 53 (8), 1177-1186 (2021)
   PUBMED   34341563
  REMARK    GeneRIF: Activation of gamma-globin gene expression by GATA1 and
            NF-Y in hereditary persistence of fetal hemoglobin.
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Fucharoen,S., Shimizu,K. and Fukumaki,Y.
  TITLE     A novel C-T transition within the distal CCAAT motif of the G
            gamma-globin gene in the Japanese HPFH: implication of factor
            binding in elevated fetal globin expression
  JOURNAL   Nucleic Acids Res 18 (17), 5245-5253 (1990)
   PUBMED   1698280
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Marotta,C.A., Forget,B.G., Cohne-Solal,M., Wilson,J.T. and
            Weissman,S.M.
  TITLE     Human beta-globin messenger RNA. I. Nucleotide sequences derived
            from complementary RNA
  JOURNAL   J Biol Chem 252 (14), 5019-5031 (1977)
   PUBMED   873928
REFERENCE   8  (residues 1 to 147)
  AUTHORS   Frier,J.A. and Perutz,M.F.
  TITLE     Structure of human foetal deoxyhaemoglobin
  JOURNAL   J Mol Biol 112 (1), 97-112 (1977)
   PUBMED   881729
REFERENCE   9  (residues 1 to 147)
  AUTHORS   Brennan,S.O., Smith,M.B. and Carrell,R.W.
  TITLE     Haemoglobin F Melbourne Ggamma 16 Gly leads to Arg and haemoglobin
            F carlton Ggamma 121 Glu leads to Lys. Further evidence for varied
            activity of gamma-chain genes
  JOURNAL   Biochim Biophys Acta 490 (2), 452-455 (1977)
   PUBMED   836882
REFERENCE   10 (residues 1 to 147)
  AUTHORS   Lee-Potter,J.P., Deacon-Smith,R.A., Simpkiss,M.J., Kamuzora,H. and
            Lehmann,H.
  TITLE     A new cause of haemolytic anaemia in the newborn. A description of
            an unstable fetal haemoglobin: F Poole, alpha2-G-gamma2 130
            trptophan yeilds glycine
  JOURNAL   J Clin Pathol 28 (4), 317-320 (1975)
   PUBMED   1127124
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104389.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The gamma globin genes (HBG1 and HBG2) are normally
            expressed in the fetal liver, spleen and bone marrow. Two gamma
            chains together with two alpha chains constitute fetal hemoglobin
            (HbF) which is normally replaced by adult hemoglobin (HbA) at
            birth. In some beta-thalassemias and related conditions, gamma
            chain production continues into adulthood. The two types of gamma
            chains differ at residue 136 where glycine is found in the G-gamma
            product (HBG2) and alanine is found in the A-gamma product (HBG1).
            The former is predominant at birth. The order of the genes in the
            beta-globin cluster is: 5'- epsilon -- gamma-G -- gamma-A -- delta
            -- beta--3'. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG619575.1, SRR5189661.69806.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336906.6/ ENSP00000338082.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..147
                     /product="hemoglobin subunit gamma-2"
                     /note="G-gamma globin Paulinia; methemoglobin; abnormal
                     hemoglobin; hb F Ggamma; gamma-2-globin; hemoglobin
                     gamma-2 chain; hemoglobin gamma-G chain; hemoglobin, gamma
                     G; gamma-globin chain; fetal hemoglobin F subunit gamma 2"
                     /calculated_mol_wt=15995
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine, in form Hb F1.
                     /evidence=ECO:0000269|PubMed:5554303; propagated from
                     UniProtKB/Swiss-Prot (P69892.2)"
     Region          8..146
                     /region_name="Hb-beta-like"
                     /note="Hemoglobin beta, gamma, delta, epsilon, and related
                     Hb subunits; cd08925"
                     /db_xref="CDD:381262"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P68871; propagated from
                     UniProtKB/Swiss-Prot (P69892.2)"
     Site            order(31,34..35,38,41,98,100,103,109,112..113,116..117,
                     120,123..125,128..129,132)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381262"
     Site            order(32,42..43,64,67..68,71,89,93,97,99,103..104,107,142)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381262"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P69892.2)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P69892.2)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P69892.2)"
     Site            60
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P68871; propagated from
                     UniProtKB/Swiss-Prot (P69892.2)"
     Site            83
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P68871; propagated from
                     UniProtKB/Swiss-Prot (P69892.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P69892.2)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P69892.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P69892.2)"
     CDS             1..147
                     /gene="HBG2"
                     /gene_synonym="HBG-T1; TNCY"
                     /coded_by="NM_000184.3:54..497"
                     /db_xref="CCDS:CCDS7755.1"
                     /db_xref="GeneID:3048"
                     /db_xref="HGNC:HGNC:4832"
                     /db_xref="MIM:142250"
ORIGIN      
        1 mghfteedka titslwgkvn vedaggetlg rllvvypwtq rffdsfgnls sasaimgnpk
       61 vkahgkkvlt slgdaikhld dlkgtfaqls elhcdklhvd penfkllgnv lvtvlaihfg
      121 keftpevqas wqkmvtgvas alssryh
//
LOCUS       NP_001851                143 aa            linear   PRI 27-APR-2025
DEFINITION  protein SLC31A2 [Homo sapiens].
ACCESSION   NP_001851
VERSION     NP_001851.1
DBSOURCE    REFSEQ: accession NM_001860.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Li,T., Peng,J., Zeng,F., Zhang,K., Liu,J., Li,X., Ouyang,Q.,
            Wang,G., Wang,L., Liu,Z. and Liu,Y.
  TITLE     Association between polymorphisms in CTR1, CTR2, ATP7A, and ATP7B
            and platinum resistance in epithelial ovarian cancer
  JOURNAL   Int J Clin Pharmacol Ther 55 (10), 774-780 (2017)
   PUBMED   28737129
  REMARK    GeneRIF: 11 single-nucleotide polymorphisms (SNPs) in CTR1, CTR2,
            ATP7A, and ATP7B were genotyped in these patients.
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Logeman,B.L., Wood,L.K., Lee,J. and Thiele,D.J.
  TITLE     Gene duplication and neo-functionalization in the evolutionary and
            functional divergence of the metazoan copper transporters Ctr1 and
            Ctr2
  JOURNAL   J Biol Chem 292 (27), 11531-11546 (2017)
   PUBMED   28507097
  REMARK    GeneRIF: Gene duplication and neo-functionalization in the
            evolutionary and functional divergence of the metazoan copper
            transporters Ctr1 and Ctr2
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Xia,Y., Liu,L., Long,Q., Bai,Q., Wang,J., Xu,J. and Guo,J.
  TITLE     Decreased expression of CTR2 predicts poor prognosis of patients
            with clear cell renal cell carcinoma
  JOURNAL   Urol Oncol 34 (1), 5 (2016)
   PUBMED   26411550
  REMARK    GeneRIF: Decreased expression of CTR2 is associated with clear cell
            renal cell carcinoma.
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Tsai,C.Y., Liebig,J.K., Tsigelny,I.F. and Howell,S.B.
  TITLE     The copper transporter 1 (CTR1) is required to maintain the
            stability of copper transporter 2 (CTR2)
  JOURNAL   Metallomics 7 (11), 1477-1487 (2015)
   PUBMED   26205368
  REMARK    GeneRIF: Studied the interaction of CTR1 and CTR2 in fully
            malignant HEK293T and OVCAR8 human ovarian cancer cells using a
            CRISPR-Cas9 knock out system.
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Yoshida,H., Teramae,M., Yamauchi,M., Fukuda,T., Yasui,T., Sumi,T.,
            Honda,K. and Ishiko,O.
  TITLE     Association of copper transporter expression with platinum
            resistance in epithelial ovarian cancer
  JOURNAL   Anticancer Res 33 (4), 1409-1414 (2013)
   PUBMED   23564780
  REMARK    GeneRIF: Increased CTR2 expression is associated with platinum
            resistance in epithelial ovarian cancer.
REFERENCE   7  (residues 1 to 143)
  AUTHORS   Blair,B.G., Larson,C.A., Safaei,R. and Howell,S.B.
  TITLE     Copper transporter 2 regulates the cellular accumulation and
            cytotoxicity of Cisplatin and Carboplatin
  JOURNAL   Clin Cancer Res 15 (13), 4312-4321 (2009)
   PUBMED   19509135
  REMARK    GeneRIF: CTR2 functions by limiting drug accumulation, and its
            expression correlates with the sensitivity of human ovarian
            carcinoma cell lines to cisplatin.
REFERENCE   8  (residues 1 to 143)
  AUTHORS   Bertinato,J., Swist,E., Plouffe,L.J., Brooks,S.P. and L'abbe,M.R.
  TITLE     Ctr2 is partially localized to the plasma membrane and stimulates
            copper uptake in COS-7 cells
  JOURNAL   Biochem J 409 (3), 731-740 (2008)
   PUBMED   17944601
  REMARK    GeneRIF: Ctr2 promotes copper uptake at the plasma membrane and
            plays a role in regulating copper levels in COS-7 cells
REFERENCE   9  (residues 1 to 143)
  AUTHORS   van den Berghe,P.V., Folmer,D.E., Malingre,H.E., van Beurden,E.,
            Klomp,A.E., van de Sluis,B., Merkx,M., Berger,R. and Klomp,L.W.
  TITLE     Human copper transporter 2 is localized in late endosomes and
            lysosomes and facilitates cellular copper uptake
  JOURNAL   Biochem J 407 (1), 49-59 (2007)
   PUBMED   17617060
  REMARK    GeneRIF: hCTR2 is as an oligomeric membrane protein localized in
            lysosomes, which stimulates copper delivery to the cytosol of human
            cells at relatively high copper concentrations.
REFERENCE   10 (residues 1 to 143)
  AUTHORS   Zhou,B. and Gitschier,J.
  TITLE     hCTR1: a human gene for copper uptake identified by complementation
            in yeast
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7481-7486 (1997)
   PUBMED   9207117
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP341248.1, U83461.1, AL449105.22 and CN480022.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK057903.1, SRR1660807.166777.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259392.8/ ENSP00000259392.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..143
                     /product="protein SLC31A2"
                     /note="copper transporter 2; probable low affinity copper
                     uptake protein 2; solute carrier family 31 (copper
                     transporters), member 2; solute carrier family 31 (copper
                     transporter), member 2"
                     /calculated_mol_wt=15550
     Region          3..135
                     /region_name="Ctr"
                     /note="Ctr copper transporter family; pfam04145"
                     /db_xref="CDD:461194"
     Site            23..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15432.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CPU9; propagated from
                     UniProtKB/Swiss-Prot (O15432.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15432.1)"
     Site            120..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15432.1)"
     CDS             1..143
                     /gene="SLC31A2"
                     /gene_synonym="COPT2; CTR2; hCTR2"
                     /coded_by="NM_001860.3:69..500"
                     /db_xref="CCDS:CCDS6788.1"
                     /db_xref="GeneID:1318"
                     /db_xref="HGNC:HGNC:11017"
                     /db_xref="MIM:603088"
ORIGIN      
        1 mamhfifsdt avllfdfwsv hspagmalsv lvllllavly egikvgkakl lnqvlvnlpt
       61 sisqqtiaet dgdsagsdsf pvgrthhrwy lchfgqslih viqvvigyfi mlavmsyntw
      121 iflgvvlgsa vgyylaypll sta
//
LOCUS       NP_002427                466 aa            linear   PRI 27-APR-2025
DEFINITION  55 kDa erythrocyte membrane protein isoform 1 [Homo sapiens].
ACCESSION   NP_002427
VERSION     NP_002427.1
DBSOURCE    REFSEQ: accession NM_002436.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Pitre,A., Ge,Y., Lin,W., Wang,Y., Fukuda,Y., Temirov,J.,
            Phillips,A.H., Peters,J.L., Fan,Y., Ma,J., Nourse,A., Sinha,C.,
            Lin,H., Kriwacki,R., Downing,J.R., Gruber,T.A., Centonze,V.E.,
            Naren,A.P., Chen,T. and Schuetz,J.D.
  TITLE     An unexpected protein interaction promotes drug resistance in
            leukemia
  JOURNAL   Nat Commun 8 (1), 1547 (2017)
   PUBMED   29146910
  REMARK    GeneRIF: Data suggest that targeting the ATP binding cassette
            subfamily C member 4 (ABCC4)-membrane palmitoylated protein 1
            (MPP1) protein complex can lead to new therapies to improve
            treatment outcome of acute myeloid leukemia (AML).
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Biernatowska,A., Augoff,K., Podkalicka,J., Tabaczar,S.,
            Gajdzik-Nowak,W., Czogalla,A. and Sikorski,A.F.
  TITLE     MPP1 directly interacts with flotillins in erythrocyte membrane -
            Possible mechanism of raft domain formation
  JOURNAL   Biochim Biophys Acta Biomembr 1859 (11), 2203-2212 (2017)
   PUBMED   28865798
  REMARK    GeneRIF: A new perspective on the role of MPP1 in erythroid cells
            suggests that direct MPP1-flotillins interactions could be the
            major driving-force behind the formation of raft domains in red
            blood cells.
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Elderdfi,M., Zegarlinska,J., Jones,W. and Sikorski,A.F.
  TITLE     MPP1 interacts with DOPC/SM/Cholesterol in an artificial membrane
            system using Langmuir-Blodgett monolayer
  JOURNAL   Gen Physiol Biophys 36 (4), 443-454 (2017)
   PUBMED   28653654
  REMARK    GeneRIF: conclusion, the data demonstrates that MPP1 interacts with
            lipid mixtures in two different model membrane systems.
REFERENCE   6  (residues 1 to 466)
  AUTHORS   Kim,A.C., Metzenberg,A.B., Sahr,K.E., Marfatia,S.M. and
            Chishti,A.H.
  TITLE     Complete genomic organization of the human erythroid p55 gene
            (MPP1), a membrane-associated guanylate kinase homologue
  JOURNAL   Genomics 31 (2), 223-229 (1996)
   PUBMED   8824805
REFERENCE   7  (residues 1 to 466)
  AUTHORS   Marfatia,S.M., Leu,R.A., Branton,D. and Chishti,A.H.
  TITLE     Identification of the protein 4.1 binding interface on glycophorin
            C and p55, a homologue of the Drosophila discs-large tumor
            suppressor protein
  JOURNAL   J Biol Chem 270 (2), 715-719 (1995)
   PUBMED   7822301
REFERENCE   8  (residues 1 to 466)
  AUTHORS   Metzenberg,A.B. and Gitschier,J.
  TITLE     The gene encoding the palmitoylated erythrocyte membrane protein,
            p55, originates at the CpG island 3' to the factor VIII gene
  JOURNAL   Hum Mol Genet 1 (2), 97-101 (1992)
   PUBMED   1301163
REFERENCE   9  (residues 1 to 466)
  AUTHORS   Bryant,P.J. and Woods,D.F.
  TITLE     A major palmitoylated membrane protein of human erythrocytes shows
            homology to yeast guanylate kinase and to the product of a
            Drosophila tumor suppressor gene
  JOURNAL   Cell 68 (4), 621-622 (1992)
   PUBMED   1310897
REFERENCE   10 (residues 1 to 466)
  AUTHORS   Ruff,P., Speicher,D.W. and Husain-Chishti,A.
  TITLE     Molecular identification of a major palmitoylated erythrocyte
            membrane protein containing the src homology 3 motif
  JOURNAL   Proc Natl Acad Sci U S A 88 (15), 6595-6599 (1991)
   PUBMED   1713685
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA074686.1 and BC002392.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the prototype of the membrane-associated
            guanylate kinase (MAGUK) family proteins. MAGUKs interact with the
            cytoskeleton and regulate cell proliferation, signaling pathways,
            and intercellular junctions. The encoded protein is an extensively
            palmitoylated membrane phosphoprotein containing a PDZ domain, a
            Src homology 3 (SH3) motif, and a guanylate kinase domain. This
            gene product interacts with various cytoskeletal proteins and cell
            junctional proteins in different tissue and cell types, and may be
            involved in the regulation of cell shape, hair cell development,
            neural patterning of the retina, and apico-basal polarity and tumor
            suppression pathways in non-erythroid cells. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.691793.1,
                                           SRR3476690.938605.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369534.8/ ENSP00000358547.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..466
                     /product="55 kDa erythrocyte membrane protein isoform 1"
                     /note="erythrocyte membrane protein p55; 55 kDa
                     erythrocyte membrane protein; palmitoylated erythrocyte
                     membrane protein; migration-related gene 1;
                     aging-associated gene 12; membrane protein, palmitoylated
                     1, 55kDa; membrane palmitoylated protein 1"
                     /calculated_mol_wt=52166
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q00013.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00013.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00013.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q00013.2)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70290; propagated from
                     UniProtKB/Swiss-Prot (Q00013.2)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00013.2)"
     Region          70..150
                     /region_name="PDZ_MPP1-like"
                     /note="PDZ domain of membrane palmitoylated protein1
                     (MPP1), and related domains; cd10830"
                     /db_xref="CDD:467266"
     Site            order(81..87,97,100,130,134,137..138)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467266"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00013.2)"
     Region          162..223
                     /region_name="SH3_MPP1"
                     /note="Src Homology 3 domain of Membrane Protein,
                     Palmitoylated 1 (or MAGUK p55 subfamily member 1);
                     cd12080"
                     /db_xref="CDD:213013"
     Site            order(164,188..189)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:213013"
     Site            order(167,169,172,183,201..202,219,221..222)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213013"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00013.2)"
     Region          268..466
                     /region_name="Interaction with PALS1.
                     /evidence=ECO:0000269|PubMed:17584769"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00013.2)"
     Region          281..453
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..466
                     /gene="MPP1"
                     /gene_synonym="AAG12; DXS552E; EMP55; MRG1; PEMP"
                     /coded_by="NM_002436.4:113..1513"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14762.1"
                     /db_xref="GeneID:4354"
                     /db_xref="HGNC:HGNC:7219"
                     /db_xref="MIM:305360"
ORIGIN      
        1 mtlkaseges ggsmhtalsd lylehllqkr srpeavshpl ntvtedmytn gspapgspaq
       61 vkgqevrkvr liqfekvtee pmgitlklne kqsctvaril hggmihrqgs lhvgdeilei
      121 ngtnvtnhsv dqlqkamket kgmislkvip nqqsrlpalq mfmraqfdyd pkkdnlipck
      181 eaglkfatgd iiqiinkdds nwwqgrvegs skesaglips pelqewrvas maqsapseap
      241 scspfgkkkk ykdkylakhs sifdqldvvs yeevvrlpaf krktlvliga sgvgrshikn
      301 allsqnpekf vypvpyttrp prkseedgke yhfisteemt rnisanefle fgsyqgnmfg
      361 tkfetvhqih kqnkiaildi epqtlkivrt aelspfivfi aptdqgtqte alqqlqkdse
      421 airsqyahyf dlslvnngvd etlkklqeaf dqacsspqwv pvswvy
//
LOCUS       NP_001309863             900 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear factor NF-kappa-B p100 subunit isoform a [Homo sapiens].
ACCESSION   NP_001309863 XP_005269917
VERSION     NP_001309863.1
DBSOURCE    REFSEQ: accession NM_001322934.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 900)
  AUTHORS   De Paolis,V., Troisi,V., Bordin,A., Pagano,F., Caputo,V. and
            Parisi,C.
  TITLE     Unconventional p65/p52 NF-kappaB module regulates key tumor
            microenvironment-related genes in breast tumor-associated
            macrophages (TAMs)
  JOURNAL   Life Sci 357, 123059 (2024)
   PUBMED   39278618
  REMARK    GeneRIF: Unconventional p65/p52 NF-kappaB module regulates key
            tumor microenvironment-related genes in breast tumor-associated
            macrophages (TAMs).
REFERENCE   2  (residues 1 to 900)
  AUTHORS   Yu,X., Zhao,P., Luo,Q., Wu,X., Wang,Y., Nan,Y., Liu,S., Gao,W.,
            Li,B., Liu,Z. and Cui,Z.
  TITLE     RUNX1-IT1 acts as a scaffold of STAT1 and NuRD complex to promote
            ROS-mediated NF-kappaB activation and ovarian cancer progression
  JOURNAL   Oncogene 43 (6), 420-433 (2024)
   PUBMED   38092960
  REMARK    GeneRIF: RUNX1-IT1 acts as a scaffold of STAT1 and NuRD complex to
            promote ROS-mediated NF-kappaB activation and ovarian cancer
            progression.
REFERENCE   3  (residues 1 to 900)
  AUTHORS   Vallabhapurapu,S. and Karin,M.
  TITLE     Regulation and function of NF-kappaB transcription factors in the
            immune system
  JOURNAL   Annu Rev Immunol 27, 693-733 (2009)
   PUBMED   19302050
  REMARK    Review article
REFERENCE   4  (residues 1 to 900)
  AUTHORS   Heusch,M., Lin,L., Geleziunas,R. and Greene,W.C.
  TITLE     The generation of nfkb2 p52: mechanism and efficiency
  JOURNAL   Oncogene 18 (46), 6201-6208 (1999)
   PUBMED   10597218
REFERENCE   5  (residues 1 to 900)
  AUTHORS   Lombardi,L., Ciana,P., Cappellini,C., Trecca,D., Guerrini,L.,
            Migliazza,A., Maiolo,A.T. and Neri,A.
  TITLE     Structural and functional characterization of the promoter regions
            of the NFKB2 gene
  JOURNAL   Nucleic Acids Res 23 (12), 2328-2336 (1995)
   PUBMED   7541912
REFERENCE   6  (residues 1 to 900)
  AUTHORS   Liptay,S., Schmid,R.M., Nabel,E.G. and Nabel,G.J.
  TITLE     Transcriptional regulation of NF-kappa B2: evidence for kappa
            B-mediated positive and negative autoregulation
  JOURNAL   Mol Cell Biol 14 (12), 7695-7703 (1994)
   PUBMED   7969113
REFERENCE   7  (residues 1 to 900)
  AUTHORS   Potter,D.A., Larson,C.J., Eckes,P., Schmid,R.M., Nabel,G.J.,
            Verdine,G.L. and Sharp,P.A.
  TITLE     Purification of the major histocompatibility complex class I
            transcription factor H2TF1. The full-length product of the nfkb2
            gene
  JOURNAL   J Biol Chem 268 (25), 18882-18890 (1993)
   PUBMED   8360178
REFERENCE   8  (residues 1 to 900)
  AUTHORS   Bours,V., Burd,P.R., Brown,K., Villalobos,J., Park,S., Ryseck,R.P.,
            Bravo,R., Kelly,K. and Siebenlist,U.
  TITLE     A novel mitogen-inducible gene product related to p50/p105-NF-kappa
            B participates in transactivation through a kappa B site
  JOURNAL   Mol Cell Biol 12 (2), 685-695 (1992)
   PUBMED   1531086
REFERENCE   9  (residues 1 to 900)
  AUTHORS   Schreck,R., Albermann,K. and Baeuerle,P.A.
  TITLE     Nuclear factor kappa B: an oxidative stress-responsive
            transcription factor of eukaryotic cells (a review)
  JOURNAL   Free Radic Res Commun 17 (4), 221-237 (1992)
   PUBMED   1473734
  REMARK    Review article
REFERENCE   10 (residues 1 to 900)
  AUTHORS   Schmid,R.M., Perkins,N.D., Duckett,C.S., Andrews,P.C. and
            Nabel,G.J.
  TITLE     Cloning of an NF-kappa B subunit which stimulates HIV transcription
            in synergy with p65
  JOURNAL   Nature 352 (6337), 733-736 (1991)
   PUBMED   1876189
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121928.13, KT935449.1 and
            AK098415.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 15, 2016 this sequence version replaced XP_005269917.1.
            
            Summary: This gene encodes a subunit of the transcription factor
            complex nuclear factor-kappa-B (NFkB). The NFkB complex is
            expressed in numerous cell types and functions as a central
            activator of genes involved in inflammation and immune function.
            The protein encoded by this gene can function as both a
            transcriptional activator or repressor depending on its
            dimerization partner. The p100 full-length protein is
            co-translationally processed into a p52 active form. Chromosomal
            rearrangements and translocations of this locus have been observed
            in B cell lymphomas, some of which may result in the formation of
            fusion proteins. There is a pseudogene for this gene on chromosome
            18. Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2013].
            
            Transcript Variant: This variant (5) and variant 1 both encode the
            same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1966682,
                              SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000661543.1/ ENSP00000499294.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..900
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..900
                     /product="nuclear factor NF-kappa-B p100 subunit isoform
                     a"
                     /note="nuclear factor NF-kappa-B p100 subunit; oncogene
                     Lyt-10; DNA-binding factor KBF2; lymphocyte translocation
                     chromosome 10 protein; transcription factor NFKB2; NFKB,
                     p52/p100 subunit; nuclear factor Kappa-B, subunit 2;
                     nuclear factor of kappa light polypeptide gene enhancer in
                     B-cells 2 (p49/p100); nuclear factor of Kappa light chain
                     gene enhancer in B cells 2; nuclear factor NF-kappa-B p52
                     subunit"
                     /calculated_mol_wt=96618
     mat_peptide     1..454
                     /product="Nuclear factor NF-kappa-B p52 subunit.
                     /id=PRO_0000030322"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
                     /calculated_mol_wt=49423
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          38..221
                     /region_name="RHD-n_NFkB2"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor kappa B2 (NF-kappa B2); cd07934"
                     /db_xref="CDD:143650"
     Site            order(52,54..55,57..58,61..63,140,142..143,221)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143650"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          228..327
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(229,231..233,235..237,275..277,290,302,321,324,326)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(231..232,234,247,249,251,282..283,286,288)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(252,254,283..284)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Region          337..341
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          346..377
                     /region_name="GRR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          404..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          438..706
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            454..455
                     /site_type="cleavage"
                     /note="Cleavage (when cotranslationally processed);
                     propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            order(487,489,493..494,497..499,501..502,506,509,524,526,
                     528,532..533,536..538,540..541,545,548,557,559,561,
                     565..566,571..573,575..576,580,583)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          487..524
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          487..519
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            490..491
                     /site_type="other"
                     /note="Breakpoint for translocation to form NFKB2-IGHA1
                     oncogene; propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          526..557
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          526..555
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          559..591
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          559..586
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(599,601,605..606,609..611,613..614,618,621,630,633,
                     635,639..640,643..645,647..648,652,655,665,667,669,
                     673..674,677..679,681..682,686,689,698)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          599..630
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          599..628
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          633..665
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          633..663
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          667..698
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          667..696
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          698..734
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            717
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          729..758
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          774..849
                     /region_name="Death_NFkB2_p100"
                     /note="Death domain of the Nuclear Factor-KappaB2
                     precursor protein p100; cd08798"
                     /db_xref="CDD:176776"
     Site            812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          849..900
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:11239468; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            870
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:11239468; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     CDS             1..900
                     /gene="NFKB2"
                     /gene_synonym="CVID10; H2TF1; LYT-10; LYT10; NF-kB2; p100;
                     p49/p100; p52"
                     /coded_by="NM_001322934.2:165..2867"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS41564.1"
                     /db_xref="GeneID:4791"
                     /db_xref="HGNC:HGNC:7795"
                     /db_xref="MIM:164012"
ORIGIN      
        1 mescynpgld giieyddfkl nssivepkep apetadgpyl viveqpkqrg frfrygcegp
       61 shgglpgass ekgrktyptv kicnyegpak ievdlvthsd pprahahslv gkqcselgic
      121 avsvgpkdmt aqfnnlgvlh vtkknmmgtm iqklqrqrlr srpqglteae qreleqeake
      181 lkkvmdlsiv rlrfsaflra sdgsfslplk pvisqpihds kspgasnlki srmdktagsv
      241 rggdevyllc dkvqkddiev rfyeddengw qafgdfsptd vhkqyaivfr tppyhkmkie
      301 rpvtvflqlk rkrggdvsds kqftyyplve dkeevqrkrr kalptfsqpf gggshmgggs
      361 ggaaggygga ggggslgffp sslayspyqs gagpmgcypg ggggaqmaat vpsrdsgeea
      421 aepsapsrtp qcepqapeml qrareynarl fglaqrsara lldygvtada rallagqrhl
      481 ltaqdengdt plhlaiihgq tsvieqivyv ihhaqdlgvv nltnhlhqtp lhlavitgqt
      541 svvsfllrvg adpalldrhg dsamhlalra gagapellra llqsgapavp qllhmpdfeg
      601 lypvhlavra rspecldllv dsgaeveate rqggrtalhl atemeelglv thlvtklran
      661 vnartfagnt plhlaaglgy ptltrlllka gadihaenee plcplpsppt sdsdsdsegp
      721 ekdtrssfrg htpldltcst kvktlllnaa qntmeppltp pspagpglsl gdtalqnleq
      781 lldgpeaqgs waelaerlgl rslvdtyrqt tspsgsllrs yelaggdlag llealsdmgl
      841 eegvrllrgp etrdklpsta evkedsaygs qsveqeaekl gpppeppggl chghpqpqvh
//
LOCUS       NP_001039605             359 aa            linear   MAM 27-APR-2025
DEFINITION  endosome-associated-trafficking regulator 1 [Bos taurus].
ACCESSION   NP_001039605 XP_590826
VERSION     NP_001039605.1
DBSOURCE    REFSEQ: accession NM_001046140.2
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105395.1.
            
            On Sep 7, 2006 this sequence version replaced XP_590826.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105395.1, GGUY01133125.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA6648753,
                                           SAMEA6648754 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="11"
                     /map="11"
                     /breed="mixed"
     Protein         1..359
                     /product="endosome-associated-trafficking regulator 1"
                     /note="serologically defined colon cancer antigen 3
                     homolog"
                     /calculated_mol_wt=39740
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C92; propagated from
                     UniProtKB/Swiss-Prot (Q2KJD6.1)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C92; propagated from
                     UniProtKB/Swiss-Prot (Q2KJD6.1)"
     Region          100..125
                     /region_name="Required for interaction with PTPN13.
                     /evidence=ECO:0000250|UniProtKB:Q96C92"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJD6.1)"
     Region          153..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJD6.1)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C92; propagated from
                     UniProtKB/Swiss-Prot (Q2KJD6.1)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C92; propagated from
                     UniProtKB/Swiss-Prot (Q2KJD6.1)"
     Region          <185..>358
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..359
                     /gene="ENTR1"
                     /gene_synonym="SDCCAG3"
                     /coded_by="NM_001046140.2:148..1227"
                     /db_xref="BGD:BT29967"
                     /db_xref="GeneID:513180"
                     /db_xref="VGNC:VGNC:54703"
ORIGIN      
        1 magyarrpgv tplsrarslv ipdddklgdl eaanpfsfke flktknlsls kedtdsrvys
       61 qeatrhslgl drtspasqtv gygleyqqpf fedptgagdl ldededeedg wngaylpsam
      121 eqthssrvaa stspcstyvs ffsnpselvg peslppwtls dsdsrisptg spsadftahg
      181 eslgdrhlrt lqisyealkd ensklrrklt eiqsfsetqt emvrtlerkl eakmikeesd
      241 yhdlesvvqq veqnlelmtk ravkaenhvl klrqevsllq aqvsdfkren ealrsgqgas
      301 ltvvkqntdv alqnlrvvmn nahasikqlv sgaetlnlva eilksidris eikdqgees
//
LOCUS       NP_001129080             759 aa            linear   PRI 27-APR-2025
DEFINITION  rho GTPase-activating protein 26 isoform b [Homo sapiens].
ACCESSION   NP_001129080
VERSION     NP_001129080.1
DBSOURCE    REFSEQ: accession NM_001135608.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Zhu,Q. and Taylor,J.M.
  TITLE     ARHGAP26/GRAF1 orchestrates actin remodeling and membrane dynamics
            to drive mitochondrial clearance and promote fuel flexibility
  JOURNAL   Autophagy 20 (8), 1906-1908 (2024)
   PUBMED   38855880
  REMARK    GeneRIF: ARHGAP26/GRAF1 orchestrates actin remodeling and membrane
            dynamics to drive mitochondrial clearance and promote fuel
            flexibility.
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    GeneRIF: GRAF1 integrates PINK1-Parkin signaling and actin dynamics
            to mediate cardiac mitochondrial homeostasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Xu,G., Zhao,L., Hua,Q., Wang,L., Liu,H., Lin,Z., Jin,M., Wang,J.,
            Zhou,P., Yang,K., Wu,G., Yu,D., Zhang,D. and Zhang,T.
  TITLE     CEMIP, acting as a scaffold protein for bridging GRAF1 and MIB1,
            promotes colorectal cancer metastasis via activating CDC42/MAPK
            pathway
  JOURNAL   Cell Death Dis 14 (2), 167 (2023)
   PUBMED   36849460
  REMARK    GeneRIF: CEMIP, acting as a scaffold protein for bridging GRAF1 and
            MIB1, promotes colorectal cancer metastasis via activating
            CDC42/MAPK pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Al-Hamed,M.H., Sayer,J.A., Alsahan,N., Edwards,N., Ali,W.,
            Tulbah,M. and Imtiaz,F.
  TITLE     Missense Variants in GFRA1 and NPNT Are Associated with Congenital
            Anomalies of the Kidney and Urinary Tract
  JOURNAL   Genes (Basel) 13 (10), 1687 (2022)
   PUBMED   36292572
  REMARK    GeneRIF: Missense Variants in <i>GFRA1</i> and <i>NPNT</i> Are
            Associated with Congenital Anomalies of the Kidney and Urinary
            Tract.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Wang,K., Lu,Y., Morrow,D.F., Xiao,D. and Xu,C.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     Associations of ARHGAP26 Polymorphisms with Alzheimer's Disease and
            Cardiovascular Disease
  JOURNAL   J Mol Neurosci 72 (5), 1085-1097 (2022)
   PUBMED   35171450
  REMARK    GeneRIF: Associations of ARHGAP26 Polymorphisms with Alzheimer's
            Disease and Cardiovascular Disease.
REFERENCE   6  (residues 1 to 759)
  AUTHORS   Taylor,J.M., Macklem,M.M. and Parsons,J.T.
  TITLE     Cytoskeletal changes induced by GRAF, the GTPase regulator
            associated with focal adhesion kinase, are mediated by Rho
  JOURNAL   J Cell Sci 112 (Pt 2), 231-242 (1999)
   PUBMED   9858476
  REMARK    GeneRIF: GRAF is a negative regulator of RhoA in vivo, it acts as a
            GTP-ase activating protein (GAP) for RhoA and may be a downstream
            effector of RhoA in certain cell types.
REFERENCE   7  (residues 1 to 759)
  AUTHORS   Billuart,P., Bienvenu,T., Ronce,N., des Portes,V., Vinet,M.C.,
            Zemni,R., Roest Crollius,H., Carrie,A., Fauchereau,F., Cherry,M.,
            Briault,S., Hamel,B., Fryns,J.P., Beldjord,C., Kahn,A., Moraine,C.
            and Chelly,J.
  TITLE     Oligophrenin-1 encodes a rhoGAP protein involved in X-linked mental
            retardation
  JOURNAL   Nature 392 (6679), 923-926 (1998)
   PUBMED   9582072
REFERENCE   8  (residues 1 to 759)
  AUTHORS   Taylor,J.M., Hildebrand,J.D., Mack,C.P., Cox,M.E. and Parsons,J.T.
  TITLE     Characterization of graf, the GTPase-activating protein for rho
            associated with focal adhesion kinase. Phosphorylation and possible
            regulation by mitogen-activated protein kinase
  JOURNAL   J Biol Chem 273 (14), 8063-8070 (1998)
   PUBMED   9525907
REFERENCE   9  (residues 1 to 759)
  AUTHORS   Hildebrand,J.D., Taylor,J.M. and Parsons,J.T.
  TITLE     An SH3 domain-containing GTPase-activating protein for Rho and
            Cdc42 associates with focal adhesion kinase
  JOURNAL   Mol Cell Biol 16 (6), 3169-3178 (1996)
   PUBMED   8649427
REFERENCE   10 (residues 1 to 759)
  AUTHORS   Pillay,T.S., Sasaoka,T. and Olefsky,J.M.
  TITLE     Insulin stimulates the tyrosine dephosphorylation of pp125 focal
            adhesion kinase
  JOURNAL   J Biol Chem 270 (3), 991-994 (1995)
   PUBMED   7836419
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008533.9, BX342449.2,
            BC068555.1, AC012630.7, AC004782.1 and AI888512.1.
            
            Summary: Interaction of a cell with the extracellular matrix
            triggers integrin cell surface receptors to begin signaling
            cascades that regulate the organization of the actin-cytoskeleton.
            One of the proteins involved in these cascades is focal adhesion
            kinase. The protein encoded by this gene is a GTPase activating
            protein that binds to focal adhesion kinase and mediates the
            activity of the GTP binding proteins RhoA and Cdc42. Defects in
            this gene are a cause of juvenile myelomonocytic leukemia (JMML).
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site compared to variant 1. The resulting isoform (b) has
            the same N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068555.1, KU178561.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000645722.2/ ENSP00000495131.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..759
                     /product="rho GTPase-activating protein 26 isoform b"
                     /note="GTPase regulator associated with focal adhesion
                     kinase pp125(FAK); oligophrenin-1-like protein"
                     /calculated_mol_wt=86034
     Region          19..225
                     /region_name="BAR_GRAF"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of GTPase
                     Regulator Associated with Focal adhesion kinase; cd07636"
                     /db_xref="CDD:153320"
     Site            order(28,31..32,36,38..39,42..43,45..46,49..50,52..53,
                     56..57,59..60,63,90,93..94,186,189..190,192,197,200..201,
                     203..204,208..209,212..213,215..216,218..219,221..222)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153320"
     Region          267..371
                     /region_name="BAR-PH_GRAF_family"
                     /note="GTPase Regulator Associated with Focal adhesion and
                     related proteins Pleckstrin homology (PH) domain; cd01249"
                     /db_xref="CDD:269953"
     Region          364..563
                     /region_name="RhoGAP_Graf"
                     /note="GTPase-activator protein (GAP) domain for Rho-like
                     GTPases found in GRAF (GTPase regulator associated with
                     focal adhesion kinase); Graf is a multi-domain protein,
                     containing SH3 and PH domains, that binds focal adhesion
                     kinase and influences cytoskeletal...; cd04374"
                     /db_xref="CDD:239839"
     Site            order(412,454,458,527,530..531,554)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239839"
     Site            412
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239839"
     Region          704..759
                     /region_name="SH3_GRAF"
                     /note="Src Homology 3 domain of GTPase Regulator
                     Associated with Focal adhesion kinase; cd12064"
                     /db_xref="CDD:212997"
     Site            order(710,712,715,719,738..739,752,754..755)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212997"
     CDS             1..759
                     /gene="ARHGAP26"
                     /gene_synonym="GRAF; GRAF1; OPHN1L; OPHN1L1"
                     /coded_by="NM_001135608.3:386..2665"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47297.1"
                     /db_xref="GeneID:23092"
                     /db_xref="HGNC:HGNC:17073"
                     /db_xref="MIM:605370"
ORIGIN      
        1 mglpalefsd ccldsphfre tlksheaeld ktnkfikeli kdgkslisal knlssakrkf
       61 adslnefkfq cigdaetdde mciarslqef atvlrnlede rirmienase vlitplekfr
      121 keqigaakea kkkydketek ycgilekhln lsskkkesql qeadsqvdlv rqhfyevsle
      181 yvfkvqevqe rkmfefvepl laflqglftf yhhgyelakd fgdfktqlti siqntrnrfe
      241 gtrseveslm kkmkenpleh ktispytmeg ylyvqekrhf gtswvkhyct yqrdskqitm
      301 vpfdqksggk ggedesvilk sctrrktdsi ekrfcfdvea vdrpgvitmq alseedrrlw
      361 meamdgrepv ynsnkdsqse gtaqldsigf siirkcihav etrgineqgl yrivgvnsrv
      421 qkllsvlmdp ktasetetdi caeweiktit salktylrml pgplmmyqfq rsfikaakle
      481 nqesrvseih slvhrlpekn rqmlqllmnh lanvannhkq nlmtvanlgv vfgptllrpq
      541 eetvaaimdi kfqnivieil ienhekifnt vpdmpltnaq lhlsrkkssd skppscserp
      601 ltlfhtvqst ekqeqrnsii nsslesvssn pnsilnssss lqpnmnssdp dlavvkptrp
      661 nslppnpspt splspswpmf sapsspmpts stssdsspvs tpfrkakaly ackaehdsel
      721 sftagtvfdn vhpsqepgwl egtlngktgl ipenyvefl
//
LOCUS       NP_057551                153 aa            linear   PRI 27-APR-2025
DEFINITION  ORM1-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_057551
VERSION     NP_057551.1
DBSOURCE    REFSEQ: accession NM_016467.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Zhu,T., Chen,Y., Min,S., Li,F. and Tian,Y.
  TITLE     Expression Patterns and Prognostic Values of ORMDL1 in Different
            Cancers
  JOURNAL   Biomed Res Int 2020, 5178397 (2020)
   PUBMED   33145351
  REMARK    GeneRIF: Expression Patterns and Prognostic Values of ORMDL1 in
            Different Cancers.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Cai,L., Oyeniran,C., Biswas,D.D., Allegood,J., Milstien,S.,
            Kordula,T., Maceyka,M. and Spiegel,S.
  TITLE     ORMDL proteins regulate ceramide levels during sterile inflammation
  JOURNAL   J Lipid Res 57 (8), 1412-1422 (2016)
   PUBMED   27313060
  REMARK    GeneRIF: ORMDL1 downregulation modestly increased levels of
            sphingosine, S1P, and ceramide in HepG2 cells.
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Siow,D., Sunkara,M., Dunn,T.M., Morris,A.J. and Wattenberg,B.
  TITLE     ORMDL/serine palmitoyltransferase stoichiometry determines effects
            of ORMDL3 expression on sphingolipid biosynthesis
  JOURNAL   J Lipid Res 56 (4), 898-908 (2015)
   PUBMED   25691431
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Gupta,S.D., Gable,K., Alexaki,A., Chandris,P., Proia,R.L.,
            Dunn,T.M. and Harmon,J.M.
  TITLE     Expression of the ORMDLS, modulators of serine
            palmitoyltransferase, is regulated by sphingolipids in mammalian
            cells
  JOURNAL   J Biol Chem 290 (1), 90-98 (2015)
   PUBMED   25395622
  REMARK    GeneRIF: Expression of the ORMDLS, modulators of serine
            palmitoyltransferase, is regulated by sphingolipids in mammalian
            cells.
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Siow,D.L. and Wattenberg,B.W.
  TITLE     Mammalian ORMDL proteins mediate the feedback response in ceramide
            biosynthesis
  JOURNAL   J Biol Chem 287 (48), 40198-40204 (2012)
   PUBMED   23066021
  REMARK    GeneRIF: ORMDL1, ORMDL2 and ORMDL3 mediate the feedback response in
            ceramide biosynthesis.
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Kang,T.W., Kim,H.J., Ju,H., Kim,J.H., Jeon,Y.J., Lee,H.C.,
            Kim,K.K., Kim,J.W., Lee,S., Kim,J.Y., Kim,S.Y. and Kim,Y.S.
  TITLE     Genome-wide association of serum bilirubin levels in Korean
            population
  JOURNAL   Hum Mol Genet 19 (18), 3672-3678 (2010)
   PUBMED   20639394
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Breslow,D.K., Collins,S.R., Bodenmiller,B., Aebersold,R.,
            Simons,K., Shevchenko,A., Ejsing,C.S. and Weissman,J.S.
  TITLE     Orm family proteins mediate sphingolipid homeostasis
  JOURNAL   Nature 463 (7284), 1048-1053 (2010)
   PUBMED   20182505
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Araki,W., Takahashi-Sasaki,N., Chui,D.H., Saito,S., Takeda,K.,
            Shirotani,K., Takahashi,K., Murayama,K.S., Kametani,F.,
            Shiraishi,H., Komano,H. and Tabira,T.
  TITLE     A family of membrane proteins associated with presenilin expression
            and gamma-secretase function
  JOURNAL   FASEB J 22 (3), 819-827 (2008)
   PUBMED   17928364
  REMARK    GeneRIF: Adoplin-1/ORMDL-1 displays reduced expression in
            association with presenilin mutations; Adoplin-1 & two highly
            homologous genes (adoplin-2, -3) are a gene family that encodes
            transmembrane proteins that may play roles in gamma-secretase
            complex maturation
REFERENCE   10 (residues 1 to 153)
  AUTHORS   Hjelmqvist,L., Tuson,M., Marfany,G., Herrero,E., Balcells,S. and
            Gonzalez-Duarte,R.
  TITLE     ORMDL proteins are a conserved new family of endoplasmic reticulum
            membrane proteins
  JOURNAL   Genome Biol 3 (6), RESEARCH0027 (2002)
   PUBMED   12093374
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB122266.1, AF395704.1, AC013468.12, AI674061.1 and AA603217.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.28817.1,
                                           SRR1803614.159363.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392349.9/ ENSP00000376160.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..153
                     /product="ORM1-like protein 1 isoform 1"
                     /note="ORM1-like protein 1; adoplin-1"
                     /calculated_mol_wt=17240
     Region          11..146
                     /region_name="ORMDL"
                     /note="ORMDL family; pfam04061"
                     /db_xref="CDD:461151"
     Site            27..46
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0S3.1)"
     Site            47..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0S3.1)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0S3.1)"
     Site            124..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0S3.1)"
     CDS             1..153
                     /gene="ORMDL1"
                     /coded_by="NM_016467.5:189..650"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2301.1"
                     /db_xref="GeneID:94101"
                     /db_xref="HGNC:HGNC:16036"
                     /db_xref="MIM:610073"
ORIGIN      
        1 mnvgvahsev npntrvmnsr gmwltyalgv gllhivllsi pffsvpvawt ltniihnlgm
       61 yvflhavkgt pfetpdqgka rllthweqld ygvqftssrk fftispiily flasfytkyd
      121 pthfilntas llsvlipkmp qlhgvrifgi nky
//
LOCUS       NP_002348                221 aa            linear   PRI 27-APR-2025
DEFINITION  max dimerization protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_002348
VERSION     NP_002348.1
DBSOURCE    REFSEQ: accession NM_002357.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Li,S., He,X., Gan,Y., Zhang,J., Gao,F., Lin,L., Qiu,X., Yu,T.,
            Zhang,X., Chen,P., Tong,J., Qian,W. and Xu,Y.
  TITLE     Targeting miR-21 with NL101 blocks c-Myc/Mxd1 loop and inhibits the
            growth of B cell lymphoma
  JOURNAL   Theranostics 11 (7), 3439-3451 (2021)
   PUBMED   33537096
  REMARK    GeneRIF: Targeting miR-21 with NL101 blocks c-Myc/Mxd1 loop and
            inhibits the growth of B cell lymphoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Du,F., Dong,D., Zhang,X. and Jia,J.
  TITLE     MXD1 is a Potential Prognostic Biomarker and Correlated With
            Specific Molecular Change and Tumor Microenvironment Feature in
            Esophageal Squamous Cell Carcinoma
  JOURNAL   Technol Cancer Res Treat 20, 15330338211052142 (2021)
   PUBMED   34761715
  REMARK    GeneRIF: MXD1 is a Potential Prognostic Biomarker and Correlated
            With Specific Molecular Change and Tumor Microenvironment Feature
            in Esophageal Squamous Cell Carcinoma.
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Jiang,K., Hein,N., Eckert,K., Luscher-Firzlaff,J. and Luscher,B.
  TITLE     Regulation of the MAD1 promoter by G-CSF
  JOURNAL   Nucleic Acids Res 36 (5), 1517-1531 (2008)
   PUBMED   18203738
  REMARK    GeneRIF: Results suggest STAT3 functions as a C/EBPbeta cofactor in
            the regulation of the MAD1 gene.
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Guo,X.L., Pan,L., Zhang,X.J., Suo,X.H., Niu,Z.Y., Zhang,J.Y.,
            Wang,F., Dong,Z.R., Da,W. and Ohno,R.
  TITLE     Expression and mutation analysis of genes that encode the Myc
            antagonists Mad1, Mxi1 and Rox in acute leukaemia
  JOURNAL   Leuk Lymphoma 48 (6), 1200-1207 (2007)
   PUBMED   17577784
  REMARK    GeneRIF: Mad1, Mxi1 and Rox genes were expressed and displayed
            mutations in haematological malignancies.
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Hassig,C.A., Fleischer,T.C., Billin,A.N., Schreiber,S.L. and
            Ayer,D.E.
  TITLE     Histone deacetylase activity is required for full transcriptional
            repression by mSin3A
  JOURNAL   Cell 89 (3), 341-347 (1997)
   PUBMED   9150133
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Ayer,D.E., Lawrence,Q.A. and Eisenman,R.N.
  TITLE     Mad-Max transcriptional repression is mediated by ternary complex
            formation with mammalian homologs of yeast repressor Sin3
  JOURNAL   Cell 80 (5), 767-776 (1995)
   PUBMED   7889570
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Shapiro,D.N., Valentine,V., Eagle,L., Yin,X., Morris,S.W. and
            Prochownik,E.V.
  TITLE     Assignment of the human MAD and MXI1 genes to chromosomes 2p12-p13
            and 10q24-q25
  JOURNAL   Genomics 23 (1), 282-285 (1994)
   PUBMED   7829091
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Edelhoff,S., Ayer,D.E., Zervos,A.S., Steingrimsson,E.,
            Jenkins,N.A., Copeland,N.G., Eisenman,R.N., Brent,R. and
            Disteche,C.M.
  TITLE     Mapping of two genes encoding members of a distinct subfamily of
            MAX interacting proteins: MAD to human chromosome 2 and mouse
            chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome
            19
  JOURNAL   Oncogene 9 (2), 665-668 (1994)
   PUBMED   8290278
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Ayer,D.E., Kretzner,L. and Eisenman,R.N.
  TITLE     Mad: a heterodimeric partner for Max that antagonizes Myc
            transcriptional activity
  JOURNAL   Cell 72 (2), 211-222 (1993)
   PUBMED   8425218
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC098396.1 and AC019206.4.
            
            Summary: This gene encodes a member of the MYC/MAX/MAD network of
            basic helix-loop-helix leucine zipper transcription factors. The
            MYC/MAX/MAD transcription factors mediate cellular proliferation,
            differentiation and apoptosis. The encoded protein antagonizes
            MYC-mediated transcriptional activation of target genes by
            competing for the binding partner MAX and recruiting repressor
            complexes containing histone deacetylases. Mutations in this gene
            may play a role in acute leukemia, and the encoded protein is a
            potential tumor suppressor. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene. [provided by RefSeq, Feb 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098396.1, SRR1803611.16788.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264444.7/ ENSP00000264444.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..221
                     /product="max dimerization protein 1 isoform 1"
                     /note="MAX-binding protein; antagonizer of myc
                     transcriptional activity; max dimerizer 1"
                     /calculated_mol_wt=25123
     Region          21..49
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05195.1)"
     Region          30..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05195.1)"
     Region          60..136
                     /region_name="bHLHzip_Mad1"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max-associated protein 1 (Mad1) and
                     similar proteins; cd18931"
                     /db_xref="CDD:381501"
     Site            order(61..62,65..66,68..69,73,92..94)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381501"
     Site            order(72..73,75..80,82..83,95,98,102,104..106,108..109,
                     111..112,115,119,122..123,125..126,129..130,132..133)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381501"
     Site            order(72,75..76,78..79,82..83,95,98,102,104..106,108..109,
                     111..112,115,119,122..123,125..126,129..130,132..133)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381501"
     Region          173..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05195.1)"
     CDS             1..221
                     /gene="MXD1"
                     /gene_synonym="BHLHC58; MAD; MAD1"
                     /coded_by="NM_002357.4:223..888"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1896.1"
                     /db_xref="GeneID:4084"
                     /db_xref="HGNC:HGNC:6761"
                     /db_xref="MIM:600021"
ORIGIN      
        1 maaavrmniq mlleaadyle rrereaehgy asmlpynnkd rdalkrrnks kknnsssrst
       61 hnemeknrra hlrlcleklk glvplgpess rhttlslltk aklhikkled cdrkavhqid
      121 qlqreqrhlk rqleklgier irmdsigstv ssersdsdre eidvdvestd yltgdldwss
      181 ssvsdsderg smqslgsdeg ysstsikrik lqdshkaclg l
//
LOCUS       NP_061134                127 aa            linear   PRI 27-APR-2025
DEFINITION  basic leucine zipper transcriptional factor ATF-like 3 [Homo
            sapiens].
ACCESSION   NP_061134
VERSION     NP_061134.1
DBSOURCE    REFSEQ: accession NM_018664.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Dabbaghipour,R., Khaze Shahgoli,V., Safaei,S., Amini,M., Tabei,S.,
            Shanehbandi,D., Rahbar Farzam,O., Baradaran,B. and Entezam,M.
  TITLE     siRNA-mediated downregulation of BATF3 diminished proliferation and
            induced apoptosis through downregulating c-Myc expression in
            chronic myelogenous leukemia cells
  JOURNAL   Mol Biol Rep 51 (1), 100 (2024)
   PUBMED   38217769
  REMARK    GeneRIF: siRNA-mediated downregulation of BATF3 diminished
            proliferation and induced apoptosis through downregulating c-Myc
            expression in chronic myelogenous leukemia cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Irfan Afridi,M., Zheng,Z., Liu,J., Liu,L., Zhang,S., Zhu,Z.,
            Peng,Y., Zhou,D. and Tu,H.
  TITLE     The bZIP transcription factor BATF3/ZIP-10 suppresses innate
            immunity by attenuating PMK-1/p38 signaling
  JOURNAL   Int Immunol 35 (4), 181-196 (2023)
   PUBMED   36409527
  REMARK    GeneRIF: The bZIP transcription factor BATF3/ZIP-10 suppresses
            innate immunity by attenuating PMK-1/p38 signaling.
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Liang,H.C., Costanza,M., Prutsch,N., Zimmerman,M.W., Gurnhofer,E.,
            Montes-Mojarro,I.A., Abraham,B.J., Prokoph,N., Stoiber,S.,
            Tangermann,S., Lobello,C., Oppelt,J., Anagnostopoulos,I.,
            Hielscher,T., Pervez,S., Klapper,W., Zammarchi,F., Silva,D.A.,
            Garcia,K.C., Baker,D., Janz,M., Schleussner,N., Fend,F.,
            Pospisilova,S., Janikova,A., Wallwitz,J., Stoiber,D.,
            Simonitsch-Klupp,I., Cerroni,L., Pileri,S., de Leval,L., Sibon,D.,
            Fataccioli,V., Gaulard,P., Assaf,C., Knorr,F., Damm-Welk,C.,
            Woessmann,W., Turner,S.D., Look,A.T., Mathas,S., Kenner,L. and
            Merkel,O.
  TITLE     Super-enhancer-based identification of a BATF3/IL-2R-module reveals
            vulnerabilities in anaplastic large cell lymphoma
  JOURNAL   Nat Commun 12 (1), 5577 (2021)
   PUBMED   34552066
  REMARK    GeneRIF: Super-enhancer-based identification of a
            BATF3/IL-2R-module reveals vulnerabilities in anaplastic large cell
            lymphoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Bower,K.E., Fritz,J.M. and McGuire,K.L.
  TITLE     Transcriptional repression of MMP-1 by p21SNFT and reduced in vitro
            invasiveness of hepatocarcinoma cells
  JOURNAL   Oncogene 23 (54), 8805-8814 (2004)
   PUBMED   15467742
  REMARK    GeneRIF: overexpression of p21SNFT in HepG2 cells leads to
            repression of matrix metalloproteinase-1 by 70-80%
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Bower,K.E., Zeller,R.W., Wachsman,W., Martinez,T. and McGuire,K.L.
  TITLE     Correlation of transcriptional repression by p21(SNFT) with changes
            in DNA.NF-AT complex interactions
  JOURNAL   J Biol Chem 277 (38), 34967-34977 (2002)
   PUBMED   12087103
  REMARK    GeneRIF: correlation of transcriptional repression by p21(SNFT)
            with changes in DNA.NF-AT complex interactions
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Iacobelli,M., Wachsman,W. and McGuire,K.L.
  TITLE     Repression of IL-2 promoter activity by the novel basic leucine
            zipper p21SNFT protein
  JOURNAL   J Immunol 165 (2), 860-868 (2000)
   PUBMED   10878360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF255346.1, BC117491.1 and
            BG184570.1.
            
            Summary: This gene encodes a member of the basic leucine zipper
            protein family. The encoded protein functions as a transcriptional
            repressor when heterodimerizing with JUN. The protein may play a
            role in repression of interleukin-2 and matrix metalloproteinase-1
            transcription.[provided by RefSeq, Feb 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF255346.1, BC117491.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000243440.2/ ENSP00000243440.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..127
                     /product="basic leucine zipper transcriptional factor
                     ATF-like 3"
                     /note="Jun dimerization protein 1; Jun dimerization
                     protein p21SNFT; 21-kD small nuclear factor isolated from
                     T cells; B-ATF-3; 21 kDa small nuclear factor isolated
                     from T-cells; basic leucine zipper transcription factor,
                     ATF-like 3"
                     /calculated_mol_wt=14336
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR55.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NR55.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NR55.1)"
     Region          35..92
                     /region_name="bZIP"
                     /note="Basic leucine zipper (bZIP) domain of bZIP
                     transcription factors: a DNA-binding and dimerization
                     domain; cl21462"
                     /db_xref="CDD:473870"
     Region          37..62
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR55.1)"
     Region          38..89
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269834"
     Site            order(41..42,44..46,48..53,55..57)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269834"
     Site            order(56,59..60,63..64,66..67,70..71,73..74,77..78,80..81,
                     84..85,87..88)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269834"
     Region          63..91
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR55.1)"
     CDS             1..127
                     /gene="BATF3"
                     /gene_synonym="JDP1; JUNDM1; SNFT"
                     /coded_by="NM_018664.3:79..462"
                     /db_xref="CCDS:CCDS1508.1"
                     /db_xref="GeneID:55509"
                     /db_xref="HGNC:HGNC:28915"
                     /db_xref="MIM:612470"
ORIGIN      
        1 msqglpaags vlqrsvaapg nqpqpqpqqq spedddrkvr rreknrvaaq rsrkkqtqka
       61 dklheeyesl eqentmlrre igklteelkh ltealkehek mcplllcpmn fvpvpprpdp
      121 vagclpr
//
LOCUS       NP_002471               1030 aa            linear   PRI 27-APR-2025
DEFINITION  protein phosphatase 1 regulatory subunit 12A isoform a [Homo
            sapiens].
ACCESSION   NP_002471
VERSION     NP_002471.1
DBSOURCE    REFSEQ: accession NM_002480.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Tong,L., Wang,X., Wang,H., Yang,R., Li,X. and Yin,X.
  TITLE     Functional analysis of a novel nonsense PPP1R12A variant in a
            Chinese family with infantile epilepsy
  JOURNAL   BMC Med Genomics 17 (1), 236 (2024)
   PUBMED   39334371
  REMARK    GeneRIF: Functional analysis of a novel nonsense PPP1R12A variant
            in a Chinese family with infantile epilepsy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Frew,E., Sainty,R., Chappell-Maor,L., Bone,C., Daskeviciute,D.,
            Russell,S., Buhigas,C., Iglesias-Platas,I., Lartey,J. and Monk,D.
  TITLE     Differential expression of PPP1R12A transcripts, including those
            harbouring alternatively spliced micro-exons, in placentae from
            complicated pregnancies
  JOURNAL   Placenta 151, 1-9 (2024)
   PUBMED   38615553
  REMARK    GeneRIF: Differential expression of PPP1R12A transcripts, including
            those harbouring alternatively spliced micro-exons, in placentae
            from complicated pregnancies.
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Inoue,C., Mukai,K., Matsudaira,T., Nakayama,J., Kono,N., Aoki,J.,
            Arai,H., Uchida,Y. and Taguchi,T.
  TITLE     PPP1R12A is a recycling endosomal phosphatase that facilitates YAP
            activation
  JOURNAL   Sci Rep 13 (1), 19740 (2023)
   PUBMED   37957190
  REMARK    GeneRIF: PPP1R12A is a recycling endosomal phosphatase that
            facilitates YAP activation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1030)
  AUTHORS   Machida,H., Ito,M., Okamoto,R., Shiraki,K., Isaka,N.,
            Hartshorne,D.J. and Nakano,T.
  TITLE     Molecular cloning and analysis of the 5'-flanking region of the
            human MYPT1 gene
  JOURNAL   Biochim Biophys Acta 1517 (3), 424-429 (2001)
   PUBMED   11342221
REFERENCE   5  (residues 1 to 1030)
  AUTHORS   Takahashi,N., Ito,M., Tanaka,J., Nakano,T., Kaibuchi,K., Odai,H.
            and Takemura,K.
  TITLE     Localization of the gene coding for myosin phosphatase, target
            subunit 1 (MYPT1) to human chromosome 12q15-q21
  JOURNAL   Genomics 44 (1), 150-152 (1997)
   PUBMED   9286714
REFERENCE   6  (residues 1 to 1030)
  AUTHORS   Kimura,K., Ito,M., Amano,M., Chihara,K., Fukata,Y., Nakafuku,M.,
            Yamamori,B., Feng,J., Nakano,T., Okawa,K., Iwamatsu,A. and
            Kaibuchi,K.
  TITLE     Regulation of myosin phosphatase by Rho and Rho-associated kinase
            (Rho-kinase)
  JOURNAL   Science 273 (5272), 245-248 (1996)
   PUBMED   8662509
REFERENCE   7  (residues 1 to 1030)
  AUTHORS   Alkhunaizi,E. and Chitayat,D.
  TITLE     PPP1R12A-Related Urogenital and/or Brain Malformation Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34499436
REFERENCE   8  (residues 1 to 1030)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
REFERENCE   9  (residues 1 to 1030)
  AUTHORS   Slee,J.J., Smart,R.D. and Viljoen,D.L.
  TITLE     Deletion of chromosome 13 in Moebius syndrome
  JOURNAL   J Med Genet 28 (6), 413-414 (1991)
   PUBMED   1870098
REFERENCE   10 (residues 1 to 1030)
  AUTHORS   Ziter,F.A., Wiser,W.C. and Robinson,A.
  TITLE     Three-generation pedigree of a Mobius syndrome variant with
            chromosome translocation
  JOURNAL   Arch Neurol 34 (7), 437-442 (1977)
   PUBMED   880069
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC350703.1, AK314193.1,
            BC111752.1 and AC073569.26.
            
            Summary: Myosin phosphatase target subunit 1, which is also called
            the myosin-binding subunit of myosin phosphatase, is one of the
            subunits of myosin phosphatase. Myosin phosphatase regulates the
            interaction of actin and myosin downstream of the guanosine
            triphosphatase Rho. The small guanosine triphosphatase Rho is
            implicated in myosin light chain (MLC) phosphorylation, which
            results in contraction of smooth muscle and interaction of actin
            and myosin in nonmuscle cells. The guanosine triphosphate
            (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted
            with the myosin-binding subunit (MBS) of myosin phosphatase, which
            regulates the extent of phosphorylation of MLC. Rho-associated
            kinase (Rho-kinase), which is activated by GTP. RhoA,
            phosphorylated MBS and consequently inactivated myosin phosphatase.
            Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased
            phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin
            phosphatase through the action of Rho-kinase. Several transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1 and 2
            both encode isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.233653.1,
                                           SRR1803616.198139.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000450142.7/ ENSP00000389168.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2-q21.31"
     Protein         1..1030
                     /product="protein phosphatase 1 regulatory subunit 12A
                     isoform a"
                     /note="myosin phosphatase, target subunit 1; myosin
                     phosphatase-targeting subunit 1; protein phosphatase
                     myosin-binding subunit; myosin binding subunit; protein
                     phosphatase 1, regulatory (inhibitor) subunit 12A"
                     /calculated_mol_wt=115150
     Region          35..38
                     /region_name="KVKF motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Region          39..68
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Region          <44..298
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(49..51,53..54,58,61,70,72,74,78..79,82..84,86..87,
                     91,94,103,105,107,111..112,115..117,119..120,124,127,136)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Site            67
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN, partial.
                     /evidence=ECO:0000269|PubMed:19245366; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Region          72..103
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          72..101
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Site            100
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN, partial.
                     /evidence=ECO:0000269|PubMed:19245366; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Region          105..136
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          105..134
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Region          138..229
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          138..164
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Region          198..227
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Site            226
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN, partial.
                     /evidence=ECO:0000269|PubMed:19245366; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Region          231..262
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          231..260
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Region          290..628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18477460; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NUAK1.
                     /evidence=ECO:0000269|PubMed:20354225,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NUAK1.
                     /evidence=ECO:0000269|PubMed:20354225; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:18477460,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18477460; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Region          643..928
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Region          658..714
                     /region_name="IPD_MYPT1"
                     /note="inhibitory phosphorylation domain of myosin
                     phosphatase targeting subunit 1(MYPT1); cd21944"
                     /db_xref="CDD:412019"
     Region          682..864
                     /region_name="Interaction with ROCK2.
                     /evidence=ECO:0000269|PubMed:19131646"
                     /note="propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKG, in vitro.
                     /evidence=ECO:0000269|PubMed:15194681; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKG, in vitro.
                     /evidence=ECO:0000269|PubMed:15194681; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK1, ROCK2, CDC42BP,
                     ZIPK/DAPK3 and RAF1.
                     /evidence=ECO:0000269|PubMed:11719507,
                     ECO:0000269|PubMed:15194681, ECO:0000269|PubMed:15723050,
                     ECO:0000269|PubMed:19701943, ECO:0000269|PubMed:19997641,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Site            802
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR7; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            852
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ROCK2.
                     /evidence=ECO:0000269|PubMed:11331307,
                     ECO:0000269|PubMed:15194681; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            862
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (O14974.1)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Site            910
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NUAK1.
                     /evidence=ECO:0000269|PubMed:20354225,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     Region          931..1030
                     /region_name="PRKG1_interact"
                     /note="cGMP-dependent protein kinase interacting domain;
                     pfam15898"
                     /db_xref="CDD:464927"
     Site            995
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14974.1)"
     CDS             1..1030
                     /gene="PPP1R12A"
                     /gene_synonym="GUBS; M130; MBS; MYPT1"
                     /coded_by="NM_002480.3:167..3259"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44947.1"
                     /db_xref="GeneID:4659"
                     /db_xref="HGNC:HGNC:7618"
                     /db_xref="MIM:602021"
ORIGIN      
        1 mkmadakqkr neqlkrwigs etdleppvvk rqktkvkfdd gavflaacss gdtdevlkll
       61 hrgadinyan vdgltalhqa ciddnvdmvk flvenganin qpdnegwipl haaascgyld
      121 iaefligqga hvgavnsegd tpldiaeeea meellqnevn rqgvdieaar keeerimlrd
      181 arqwlnsghi ndvrhaksgg talhvaaakg ytevlklliq agydvnikdy dgwtplhaaa
      241 hwgkeeacri lvdnlcdmem vnkvgqtafd vadedilgyl eelqkkqnll hsekrdkksp
      301 liestanmdn nqsqktfknk etliiepekn asriesleqe kvdeeeegkk desscsseed
      361 eeddseseae tdktkplasv tnantsstqa apvavttptv ssgqatptsp ikkfpttatk
      421 ispkeeerkd espatwrlgl rktgsygala eitaskegqk ekdtagvtrs assprlsssl
      481 dnkekekdsk gtrlayvapt iprrlastsd ieekenrdss slrtsssytr rkweddlkkn
      541 ssvnegstyh kscsfgrrqd dlisssvpst tstptvtsaa glqksllsst stttkittgs
      601 ssagtqssts nrlwaedste kekdsvptav tipvaptvvn aaastttltt ttagtvsstt
      661 evrerrrsyl tpvrdeeses qrkarsrqar qsrrstqgvt ltdlqeaekt igrsrstrtr
      721 eqeneekeke ekekqdkekq eekkesetsr edeykqkysr tydetyqryr pvstsssttp
      781 ssslstmsss lyassqlnrp nslvgitsay srgitkener egekreeeke gedksqpksi
      841 rerrrprekr rstgvsfwtq dsdeneqeqq sdteegsnkk etqtdsisry etsstsagdr
      901 ydsllgrsgs ysyleerkpy ssrlekddst dfkklyeqil aeneklkaql hdtnmeltdl
      961 klqlekatqr qerfadrsll emekrerral errisemeee lkmlpdlkad nqrlkdenga
     1021 lirvisklsk
//
LOCUS       NP_057327                305 aa            linear   PRI 27-APR-2025
DEFINITION  NADH-cytochrome b5 reductase 1 [Homo sapiens].
ACCESSION   NP_057327
VERSION     NP_057327.2
DBSOURCE    REFSEQ: accession NM_016243.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Proskurnina,E.V., Fedorova,M.V., Sozarukova,M.M., Mitichkin,A.E.,
            Panteleev,I.V. and Svetlov,E.V.
  TITLE     Microsomal reductase activity in patients with thyroid neoplasms
  JOURNAL   Endocrine 72 (3), 735-743 (2021)
   PUBMED   33011882
  REMARK    GeneRIF: Microsomal reductase activity in patients with thyroid
            neoplasms.
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Yan,B., Ai,Y., Sun,Q., Ma,Y., Cao,Y., Wang,J., Zhang,Z. and Wang,X.
  TITLE     Membrane Damage during Ferroptosis Is Caused by Oxidation of
            Phospholipids Catalyzed by the Oxidoreductases POR and CYB5R1
  JOURNAL   Mol Cell 81 (2), 355-369 (2021)
   PUBMED   33321093
  REMARK    GeneRIF: Membrane Damage during Ferroptosis Is Caused by Oxidation
            of Phospholipids Catalyzed by the Oxidoreductases POR and CYB5R1.
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Woischke,C., Blaj,C., Schmidt,E.M., Lamprecht,S., Engel,J.,
            Hermeking,H., Kirchner,T. and Horst,D.
  TITLE     CYB5R1 links epithelial-mesenchymal transition and poor prognosis
            in colorectal cancer
  JOURNAL   Oncotarget 7 (21), 31350-31360 (2016)
   PUBMED   27120783
  REMARK    GeneRIF: Data show that cytochrome b5 reductase 1 (CYB5R1) gene
            expression is strongly linked to epithelial-mesenchymal transition
            (EMT) in colon cancer.
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 305)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 305)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   9  (residues 1 to 305)
  AUTHORS   Zhu,H., Qiu,H., Yoon,H.W., Huang,S. and Bunn,H.F.
  TITLE     Identification of a cytochrome b-type NAD(P)H oxidoreductase
            ubiquitously expressed in human cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 14742-14747 (1999)
   PUBMED   10611283
REFERENCE   10 (residues 1 to 305)
  AUTHORS   Qian,W., Sun,Y.L., Wang,Y.H., Zhuang,J.H., Xie,Y. and Huang,Z.X.
  TITLE     The influence of mutation at Glu44 and Glu56 of cytochrome b5 on
            the protein's stabilization and interaction between cytochrome c
            and cytochrome b5
  JOURNAL   Biochemistry 37 (40), 14137-14150 (1998)
   PUBMED   9760250
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY359026.1 and BC018732.1.
            
            On Jul 1, 2004 this sequence version replaced NP_057327.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223416.1, SRR3476690.63487.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367249.9/ ENSP00000356218.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..305
                     /product="NADH-cytochrome b5 reductase 1"
                     /EC_number="1.6.2.2"
                     /note="NAD(P)H:quinone oxidoreductase type 3, polypeptide
                     A2"
                     /calculated_mol_wt=33964
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHQ9.1)"
     Region          <38..300
                     /region_name="PLN02252"
                     /note="nitrate reductase [NADPH]"
                     /db_xref="CDD:215141"
     CDS             1..305
                     /gene="CYB5R1"
                     /gene_synonym="B5R.1; B5R1; B5R2; humb5R2; NQO3A2"
                     /coded_by="NM_016243.3:53..970"
                     /db_xref="CCDS:CCDS1431.1"
                     /db_xref="GeneID:51706"
                     /db_xref="HGNC:HGNC:13397"
                     /db_xref="MIM:608341"
ORIGIN      
        1 mgiqtspvll aslgvglvtl lglavgsylv rrsrrpqvtl ldpnekyllr lldkttvshn
       61 tkrfrfalpt ahhtlglpvg khiylstrid gslvirpytp vtsdedqgyv dlvikvylkg
      121 vhpkfpeggk msqyldslkv gdvvefrgps glltytgkgh fniqpnkksp peprvakklg
      181 miaggtgitp mlqlirailk vpedptqcfl lfanqtekdi ilredleelq arypnrfklw
      241 ftldhppkdw ayskgfvtad mirehlpapg ddvlvllcgp ppmvqlachp nldklgysqk
      301 mrfty
//
LOCUS       NP_054884                175 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor
            4 [Homo sapiens].
ACCESSION   NP_054884
VERSION     NP_054884.1
DBSOURCE    REFSEQ: accession NM_014165.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Long,T., Li,J., Yin,T., Liu,K., Wang,Y., Long,J., Wang,J. and
            Cheng,L.
  TITLE     A genetic variant in gene NDUFAF4 confers the risk of non-small
            cell lung cancer by perturbing hsa-miR-215 binding
  JOURNAL   Mol Carcinog 63 (1), 145-159 (2024)
   PUBMED   37787384
  REMARK    GeneRIF: A genetic variant in gene NDUFAF4 confers the risk of
            non-small cell lung cancer by perturbing hsa-miR-215 binding.
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Pan,W., Shen,Z., Wang,H. and He,H.
  TITLE     The host cellular protein Ndufaf4 interacts with the vesicular
            stomatitis virus M protein and affects viral propagation
  JOURNAL   Virus Genes 57 (3), 250-257 (2021)
   PUBMED   33635491
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Ugarteburu,O., Teresa Garcia-Silva,M., Aldamiz-Echevarria,L.,
            Gort,L., Garcia-Villoria,J., Tort,F. and Ribes,A.
  TITLE     Complex I deficiency, due to NDUFAF4 mutations, causes severe
            mitochondrial dysfunction and is associated to early death and
            dysmorphia
  JOURNAL   Mitochondrion 55, 78-84 (2020)
   PUBMED   32949790
  REMARK    GeneRIF: Complex I deficiency, due to NDUFAF4 mutations, causes
            severe mitochondrial dysfunction and is associated to early death
            and dysmorphia.
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Saada,A., Edvardson,S., Rapoport,M., Shaag,A., Amry,K., Miller,C.,
            Lorberboum-Galski,H. and Elpeleg,O.
  TITLE     C6ORF66 is an assembly factor of mitochondrial complex I
  JOURNAL   Am J Hum Genet 82 (1), 32-38 (2008)
   PUBMED   18179882
  REMARK    GeneRIF: Homozygosity mapping of 5 patients from a consanguineous
            family with infantile mitochondrial encephalomyopathy resulted in
            the identification of a missense mutation in a conserved residue of
            the C6ORF66.
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Tozlu-Kara,S., Roux,V., Andrieu,C., Vendrell,J., Vacher,S.,
            Lazar,V., Spyratos,F., Tubiana-Hulin,M., Cohen,P., Dessen,P.,
            Lidereau,R. and Bieche,I.
  TITLE     Oligonucleotide microarray analysis of estrogen receptor
            alpha-positive postmenopausal breast carcinomas: identification of
            HRPAP20 and TIMELESS as outstanding candidate markers to predict
            the response to tamoxifen
  JOURNAL   J Mol Endocrinol 39 (4), 305-318 (2007)
   PUBMED   17909269
  REMARK    GeneRIF: HRPAP20 and TIMELESS as promising markers of tamoxifen
            resistance in women with ER alpha-positive breast tumors.
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Karp,C.M., Shukla,M.N., Buckley,D.J. and Buckley,A.R.
  TITLE     HRPAP20: a novel calmodulin-binding protein that increases breast
            cancer cell invasion
  JOURNAL   Oncogene 26 (12), 1780-1788 (2007)
   PUBMED   17001319
  REMARK    GeneRIF: observations suggest that HRPAP20 may be an important
            regulator of breast tumor cell invasion by a CaM-mediated mechanism
            that leads to increased MMP-9 secretion
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Karp,C.M., Pan,H., Zhang,M., Buckley,D.J., Schuler,L.A. and
            Buckley,A.R.
  TITLE     Identification of HRPAP20: a novel phosphoprotein that enhances
            growth and survival in hormone-responsive tumor cells
  JOURNAL   Cancer Res 64 (3), 1016-1025 (2004)
   PUBMED   14871833
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB253189.1, BC018802.1 and
            AL159985.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: NADH:ubiquinone oxidoreductase (complex I) catalyzes the
            transfer of electrons from NADH to ubiquinone (coenzyme Q) in the
            first step of the mitochondrial respiratory chain, resulting in the
            translocation of protons across the inner mitochondrial membrane.
            This gene encodes a complex I assembly factor. Mutations in this
            gene are a cause of mitochondrial complex I deficiency. [provided
            by RefSeq, Oct 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.801582.1,
                                           SRR1660809.258294.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146, SAMEA2467148
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000316149.8/
                                                  ENSP00000358272.4
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.1"
     Protein         1..175
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex assembly factor 4"
                     /note="hormone-regulated proliferation-associated protein,
                     20 kDa; hormone-regulated proliferation-associated protein
                     of 20 kDa; NADH dehydrogenase (ubiquinone) 1 alpha
                     subcomplex, assembly factor 4; NADH dehydrogenase
                     (ubiquinone) complex I, assembly factor 4"
                     /calculated_mol_wt=20135
     Region          1..167
                     /region_name="UPF0240"
                     /note="Uncharacterized protein family (UPF0240);
                     pfam06784"
                     /db_xref="CDD:462009"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P032.1)"
     CDS             1..175
                     /gene="NDUFAF4"
                     /gene_synonym="bA22L21.1; C6orf66; HRPAP20; HSPC125;
                     MC1DN15; My013"
                     /coded_by="NM_014165.4:91..618"
                     /db_xref="CCDS:CCDS5037.1"
                     /db_xref="GeneID:29078"
                     /db_xref="HGNC:HGNC:21034"
                     /db_xref="MIM:611776"
ORIGIN      
        1 mgalvirgir nfnlenraer eiskmkpsva prhpstnsll reqislypev kgeiarkdek
       61 llsflkdvyv dskdpvsslq vkaaetcqep kefrlpkdhh fdminiksip kgkisiveal
      121 tllnnhklfp etwtaekimq eyqleqkdvn sllkyfvtfe veifppedkk airsk
//
LOCUS       NP_001352718             207 aa            linear   PRI 27-APR-2025
DEFINITION  acyl-coenzyme A thioesterase 6 isoform 2 [Homo sapiens].
ACCESSION   NP_001352718
VERSION     NP_001352718.1
DBSOURCE    REFSEQ: accession NM_001365789.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Xu,B., Roos,J.L., Dexheimer,P., Boone,B., Plummer,B., Levy,S.,
            Gogos,J.A. and Karayiorgou,M.
  TITLE     Exome sequencing supports a de novo mutational paradigm for
            schizophrenia
  JOURNAL   Nat Genet 43 (9), 864-868 (2011)
   PUBMED   21822266
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Hunt,M.C., Rautanen,A., Westin,M.A., Svensson,L.T. and Alexson,S.E.
  TITLE     Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene
            clusters shows that convergent, functional evolution results in a
            reduced number of human peroxisomal ACOTs
  JOURNAL   FASEB J 20 (11), 1855-1864 (2006)
   PUBMED   16940157
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Hunt,M.C., Yamada,J., Maltais,L.J., Wright,M.W., Podesta,E.J. and
            Alexson,S.E.
  TITLE     A revised nomenclature for mammalian acyl-CoA
            thioesterases/hydrolases
  JOURNAL   J Lipid Res 46 (9), 2029-2032 (2005)
   PUBMED   16103133
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005225.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CA454440.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162328 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..207
                     /product="acyl-coenzyme A thioesterase 6 isoform 2"
                     /EC_number="3.1.2.2"
                     /note="putative acyl-coenzyme A thioesterase 6; putative
                     acyl-CoA thioesterase 6"
                     /calculated_mol_wt=22860
     Region          1..198
                     /region_name="BAAT_C"
                     /note="BAAT / Acyl-CoA thioester hydrolase C terminal;
                     pfam08840"
                     /db_xref="CDD:430252"
     CDS             1..207
                     /gene="ACOT6"
                     /gene_synonym="C14orf42; c14_5530"
                     /coded_by="NM_001365789.1:365..988"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS32118.1"
                     /db_xref="GeneID:641372"
                     /db_xref="HGNC:HGNC:33159"
                     /db_xref="MIM:614267"
ORIGIN      
        1 mlqhpkvkgp siallgfskg gdlclsmasf lkgitatvli nacvantvap lhykdmiipk
       61 lvddlgkvki tksgfltfmd twsnpleehn hqslvpleka qvpflfivgm ddqswksefy
      121 aqiaserlqa hgkerpqiic ypetghcidp pyfppsrasv havlgeaify ggepkahska
      181 qvdawqqiqt ffhkhlngkk svkhski
//
LOCUS       NP_689922                989 aa            linear   PRI 27-APR-2025
DEFINITION  storkhead-box protein 1 isoform a [Homo sapiens].
ACCESSION   NP_689922
VERSION     NP_689922.3
DBSOURCE    REFSEQ: accession NM_152709.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Sammar,M., Apicella,C., Altevogt,P., Meiri,H. and Vaiman,D.
  TITLE     Modeling Preeclampsia In Vitro: Polymorphic Variants of STOX1-A/B
            Genes Can Downregulate CD24 in Trophoblast Cell Lines
  JOURNAL   Int J Mol Sci 23 (24), 15927 (2022)
   PUBMED   36555567
  REMARK    GeneRIF: Modeling Preeclampsia In Vitro: Polymorphic Variants of
            STOX1-A/B Genes Can Downregulate CD24 in Trophoblast Cell Lines.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Akin,S., Pinarbasi,E., Bildirici,A.E. and Cekin,N.
  TITLE     STOX1 promotor region -922 T > C polymorphism is associated with
            Early-Onset preeclampsia
  JOURNAL   J Obstet Gynaecol 42 (8), 3464-3470 (2022)
   PUBMED   36369889
  REMARK    GeneRIF: STOX1 promotor region -922 T > C polymorphism is
            associated with Early-Onset preeclampsia.
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   4  (residues 1 to 989)
  AUTHORS   Dunk,C.E., van Dijk,M., Choudhury,R., Wright,T.J., Cox,B.,
            Leavey,K., Harris,L.K., Jones,R.L. and Lye,S.J.
  TITLE     Functional Evaluation of STOX1 (STORKHEAD-BOX PROTEIN 1) in
            Placentation, Preeclampsia, and Preterm Birth
  JOURNAL   Hypertension 77 (2), 475-490 (2021)
   PUBMED   33356399
  REMARK    GeneRIF: Functional Evaluation of STOX1 (STORKHEAD-BOX PROTEIN 1)
            in Placentation, Preeclampsia, and Preterm Birth.
REFERENCE   5  (residues 1 to 989)
  AUTHORS   Li,Z., Zhou,G., Tao,F., Cao,Y., Han,W. and Li,Q.
  TITLE     circ-ZUFSP regulates trophoblasts migration and invasion through
            sponging miR-203 to regulate STOX1 expression
  JOURNAL   Biochem Biophys Res Commun 531 (4), 472-479 (2020)
   PUBMED   32807495
  REMARK    GeneRIF: circ-ZUFSP regulates trophoblasts migration and invasion
            through sponging miR-203 to regulate STOX1 expression.
REFERENCE   6  (residues 1 to 989)
  AUTHORS   Rigourd,V., Chauvet,C., Chelbi,S.T., Rebourcet,R., Mondon,F.,
            Letourneur,F., Mignot,T.M., Barbaux,S. and Vaiman,D.
  TITLE     STOX1 overexpression in choriocarcinoma cells mimics
            transcriptional alterations observed in preeclamptic placentas
  JOURNAL   PLoS One 3 (12), e3905 (2008)
   PUBMED   19079545
  REMARK    GeneRIF: Anomalies in STOX1 expression are associated with the
            onset of preeclampsia.
REFERENCE   7  (residues 1 to 989)
  AUTHORS   Berends,A.L., Bertoli-Avella,A.M., de Groot,C.J., van Duijn,C.M.,
            Oostra,B.A. and Steegers,E.A.
  TITLE     STOX1 gene in pre-eclampsia and intrauterine growth restriction
  JOURNAL   BJOG 114 (9), 1163-1167 (2007)
   PUBMED   17617193
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 989)
  AUTHORS   Kivinen,K., Peterson,H., Hiltunen,L., Laivuori,H., Heino,S.,
            Tiala,I., Knuutila,S., Rasi,V. and Kere,J.
  TITLE     Evaluation of STOX1 as a preeclampsia candidate gene in a
            population-wide sample
  JOURNAL   Eur J Hum Genet 15 (4), 494-497 (2007)
   PUBMED   17290274
  REMARK    GeneRIF: In conclusion, we are unable to validate STOX1 as a common
            preeclampsia susceptibility gene.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 989)
  AUTHORS   van Dijk,M., Mulders,J., Poutsma,A., Konst,A.A., Lachmeijer,A.M.,
            Dekker,G.A., Blankenstein,M.A. and Oudejans,C.B.
  TITLE     Maternal segregation of the Dutch preeclampsia locus at 10q22 with
            a new member of the winged helix gene family
  JOURNAL   Nat Genet 37 (5), 514-519 (2005)
   PUBMED   15806103
REFERENCE   10 (residues 1 to 989)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391539.27, BC140011.1 and
            AY842014.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 4, 2005 this sequence version replaced NP_689922.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a). Variants 1 and 2
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY842014.1, ERR3218373.84465.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298596.11/ ENSP00000298596.6
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..989
                     /product="storkhead-box protein 1 isoform a"
                     /note="storkhead-box protein 1; winged-helix
                     domain-containing protein"
                     /calculated_mol_wt=110831
     Region          111..189
                     /region_name="Stork_head"
                     /note="Winged helix Storkhead-box1 domain; pfam10264"
                     /db_xref="CDD:431182"
     Region          327..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVD7.2)"
     Region          389..470
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVD7.2)"
     Region          497..556
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVD7.2)"
     Region          631..651
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVD7.2)"
     Region          926..948
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVD7.2)"
     CDS             1..989
                     /gene="STOX1"
                     /gene_synonym="C10orf24"
                     /coded_by="NM_152709.5:94..3063"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41535.1"
                     /db_xref="GeneID:219736"
                     /db_xref="HGNC:HGNC:23508"
                     /db_xref="MIM:609397"
ORIGIN      
        1 marpvqlapg slalvlcrle aqkaagaaee pggravfraf rranarcfwn arlaraasrl
       61 afqgwlrrgv llvrappacl qvlrdawrrr alrpprgfri ravgdvfpvq mnpitqsqfv
      121 plgevlccai sdmntaqivv tqesllerlm khypgiaips edilyttlgt likerkiyht
      181 gegyfivtpq tyfitntttq enkrmlpsde srlmpasmty lvsmescaes aqenaapish
      241 cqscqcfrdm htqdvqeapv aaevtrkshr glgesvswvq ngavsvsaeh hicestkplp
      301 ytrdkekgkk fgfsllwrsl srkekpkteh ssfsaqfppe ewpvrdeddl dniprdvehe
      361 iikrinpilt vdnlikhtvl mqkyeeqkky nsqgtstdml tighkypske gvkkrqglsa
      421 kpqgqghsrr drhkarnqgs efqpgsirle khpklpatqp iprikspnem vgqkplgeit
      481 tvlgshliyk krisnpfqgl shrgstiskg hkiqktsdlk psqtgpkekp fqkprsldss
      541 rifdgkakep yaeqpndkme aesiyindpt vkpinddfrg hlfshpqqsm lqndgkccpf
      601 mesmlryevy ggenevipev lrkshshfdk lgetkqtphs lpsrgasfsd rtpsacrlvd
      661 ntihqfqnlg lldypvgvnp lrqaarqdkd seellrkgfv qdaettslen eqlsnddqal
      721 yqnevedddg acsslyleed disenddlrq mlpghsqysf tggsqgnhlg kqkvierslt
      781 eynstmerve sqvlkrnecy kptglhatpg esqepnlsae scglnsgaqf gfnyeeepsv
      841 akcvqasapa derifdyysa rkasfeaevi qdtigdtgkk paswsqspqn qemrkhfpqk
      901 fqlfntshmp vlaqdvqyeh shlegtenhs magdsgidsp rtqslgsnns vildglkrrq
      961 nflqnvegtk ssqpltsnsl lpltpvinv
//
LOCUS       NP_001350092             911 aa            linear   ROD 27-APR-2025
DEFINITION  oxysterol-binding protein 2 isoform 4 [Mus musculus].
ACCESSION   NP_001350092 XP_017170297
VERSION     NP_001350092.1
DBSOURCE    REFSEQ: accession NM_001363163.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Ge,T., Yuan,L., Xu,L., Yang,F., Xu,W., Niu,C., Li,G., Zhou,H. and
            Zheng,Y.
  TITLE     Coiled-coil domain containing 159 is required for spermatid head
            and tail assembly in micedagger
  JOURNAL   Biol Reprod 110 (5), 877-894 (2024)
   PUBMED   38236177
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Udagawa,O., Ito,C., Ogonuki,N., Sato,H., Lee,S., Tripvanuntakul,P.,
            Ichi,I., Uchida,Y., Nishimura,T., Murakami,M., Ogura,A., Inoue,T.,
            Toshimori,K. and Arai,H.
  TITLE     Oligo-astheno-teratozoospermia in mice lacking ORP4, a
            sterol-binding protein in the OSBP-related protein family
  JOURNAL   Genes Cells 19 (1), 13-27 (2014)
   PUBMED   24245814
  REMARK    GeneRIF: ORP4 is essential for the postmeiotic differentiation of
            germ cells
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Anniss,A.M., Apostolopoulos,J., Dworkin,S., Purton,L.E. and
            Sparrow,R.L.
  TITLE     An oxysterol-binding protein family identified in the mouse
  JOURNAL   DNA Cell Biol 21 (8), 571-580 (2002)
   PUBMED   12215260
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL731853.9 and AL691413.5.
            
            On May 10, 2018 this sequence version replaced XP_017170297.1.
            
            Summary: The protein encoded by this gene belongs to the
            oxysterol-binding protein-related family of proteins, which are
            defined by a C-terminal sterol domain with a highly conserved
            EQVSHHPP motif. Oxysterols are oxygenated derivatives of
            cholesterol that are involved in mechanisms that include apoptosis,
            cholesterol homeostasis, lipid trafficking and cell
            differentiation. This protein is selectively expressed at high
            levels in the brain and testis. Within the testis, the mRNA is
            localized to postmeiotic germ cells, including spermatids and
            spermatozoa, but is not detectable in somatic cells. Mice
            homozygous mutant for a targeted deletion in this gene do not
            exhibit overt developmental phenotypes but are male sterile.
            Females display normal fertility. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660811.144627.1,
                                           SRR7345562.4916183.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 2.6 cM"
     Protein         1..911
                     /product="oxysterol-binding protein 2 isoform 4"
                     /calculated_mol_wt=101554
     Region          42..112
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QNQ6.1)"
     Region          182..278
                     /region_name="PH_OSBP_ORP4"
                     /note="Human Oxysterol binding protein and OSBP-related
                     protein 4 Pleckstrin homology (PH) domain; cd13284"
                     /db_xref="CDD:270101"
     Region          279..299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QNQ6.1)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q5QNQ6.1)"
     Region          413..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QNQ6.1)"
     Region          522..900
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     Region          825..846
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QNQ6.1)"
     CDS             1..911
                     /gene="Osbp2"
                     /gene_synonym="1700095P05Rik; C630001G20Rik; Gm244; ORP-4;
                     OSBPL1"
                     /coded_by="NM_001363163.1:37..2772"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:74309"
                     /db_xref="MGI:MGI:1921559"
ORIGIN      
        1 mgkaaalsrg ggcagrsrgl sslftvvpcl schtaapgmn ssafgsgpas kpqlqpvqap
       61 erellskqvc qpisepasrs epgsqttsvp rpsgvgqese lqglwpgsen gtrsvsiika
      121 spelampspl qstvgslpvt kpesklvpkt qsflrqgqak isvgtpvsgi gvqmvsppld
      181 sykgwllkwt nylkgyqrrw fvlgngllsy yrnqgemaht cratinlast hfetedscgi
      241 llcngartyh lkassevdrq hwitalelak akairvmktq sddsgdddee paapadnsel
      301 hhtlktlslk lndlstcndl iakhgaalqr slneldslki psecgeklkv vneratlfri
      361 tsnaminacr dflelaeths rkwqralnye qeqrvhleet ieqlakqhns lerafcntpg
      421 gpasssksfs egsfltskge nseededtey fdamedstsf itvvteaked rkpesgpgtt
      481 tvdwtsadnv cevldgasfm pknsckvkrr vripdkpnys lnlwsimknc igrelsripm
      541 pvnfneplsm lqrltedley hhlldkavnc tssveqmclv aafsvssyst tvhriakpfn
      601 pmlgetfeld rmedmglrsl ceqvshhpps aahhvfskhg wslwqeitia skfrgkyisi
      661 mplgaihlef qasgnhyvwr kststvhnii vgklwidqsg dieivnhktk drcqlkfvpy
      721 syfskeaark vtgvvsdsqg kahyvlsgsw ddqmecskiv hsspssdgrq ktvyqtlpak
      781 llwrkyplpe naenmyyfse laltlneqed gvaptdsrlr pdqrlmergr wdeantekqr
      841 leekqrlsrr rrlesctagc ggeeekesdg yvplwfekrl dpltgemacm ykggyweake
      901 kkdwhmcpni f
//
LOCUS       NP_258411                638 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM47 [Homo sapiens].
ACCESSION   NP_258411
VERSION     NP_258411.2
DBSOURCE    REFSEQ: accession NM_033452.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Yeung,S.H., Lee,R.H., Cheng,G.W., Ma,I.W., Kofler,J., Kent,C.,
            Ma,F., Herrup,K., Fornage,M., Arai,K. and Tse,K.H.
  TITLE     White matter hyperintensity genetic risk factor TRIM47 regulates
            autophagy in brain endothelial cells
  JOURNAL   FASEB J 38 (19), e70059 (2024)
   PUBMED   39331575
  REMARK    GeneRIF: White matter hyperintensity genetic risk factor TRIM47
            regulates autophagy in brain endothelial cells.
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Zhang,J., Yimamu,M., Cheng,Z., Ji,J., Wu,L., Feng,J., Xu,X., Wu,J.
            and Guo,C.
  TITLE     TRIM47-CDO1 axis dictates hepatocellular carcinoma progression by
            modulating ferroptotic cell death through the ubiquitin-proteasome
            system
  JOURNAL   Free Radic Biol Med 219, 31-48 (2024)
   PUBMED   38614226
  REMARK    GeneRIF: TRIM47-CDO1 axis dictates hepatocellular carcinoma
            progression by modulating ferroptotic cell death through the
            ubiquitin-proteasome system.
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Wang,X., Fu,Y. and Xing,Y.
  TITLE     TRIM47 promotes ovarian cancer cell proliferation, migration, and
            invasion by activating STAT3 signaling
  JOURNAL   Clinics (Sao Paulo) 77, 100122 (2022)
   PUBMED   36288633
  REMARK    GeneRIF: TRIM47 promotes ovarian cancer cell proliferation,
            migration, and invasion by activating STAT3 signaling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Wang,Z., Li,Z., Han,C., Cheng,Y. and Wang,K.
  TITLE     TRIM47 promotes glioma angiogenesis by suppressing Smad4
  JOURNAL   In Vitro Cell Dev Biol Anim 58 (9), 771-779 (2022)
   PUBMED   36203070
  REMARK    GeneRIF: TRIM47 promotes glioma angiogenesis by suppressing Smad4.
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Azuma,K., Ikeda,K., Suzuki,T., Aogi,K., Horie-Inoue,K. and Inoue,S.
  TITLE     TRIM47 activates NF-kappaB signaling via PKC-epsilon/PKD3
            stabilization and contributes to endocrine therapy resistance in
            breast cancer
  JOURNAL   Proc Natl Acad Sci U S A 118 (35) (2021)
   PUBMED   34433666
  REMARK    GeneRIF: TRIM47 activates NF-kappaB signaling via PKC-epsilon/PKD3
            stabilization and contributes to endocrine therapy resistance in
            breast cancer.
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Huang,W.Q., Ye,H.M., Li,F.F., Yi,K.H., Zhang,Y., Cai,L.L.,
            Lin,H.N., Lin,Q. and Tzeng,C.M.
  TITLE     Analysis of genetic polymorphisms associated with leukoaraiosis in
            the southern Chinese population: A case-control study
  JOURNAL   Medicine (Baltimore) 95 (35), e3857 (2016)
   PUBMED   27583843
  REMARK    GeneRIF: These results suggest that rs1055129 in TRIM47 is not
            associated with leukoaraiosis (LA) risk in the Chinese population.
            However, the association of rs1055129 (TRIM47) with LA before
            Bonferroni correction and Sidak correction is worth highlighting.
REFERENCE   7  (residues 1 to 638)
  AUTHORS   Fujimura,T., Inoue,S., Urano,T., Takayama,K., Yamada,Y., Ikeda,K.,
            Obinata,D., Ashikari,D., Takahashi,S. and Homma,Y.
  TITLE     Increased Expression of Tripartite Motif (TRIM) 47 Is a Negative
            Prognostic Predictor in Human Prostate Cancer
  JOURNAL   Clin Genitourin Cancer 14 (4), 298-303 (2016)
   PUBMED   26873435
  REMARK    GeneRIF: Study shows that protein and gene expression level of
            TRIM47 are up-regulated in prostate neoplasm.
REFERENCE   8  (residues 1 to 638)
  AUTHORS   Fornage,M., Debette,S., Bis,J.C., Schmidt,H., Ikram,M.A.,
            Dufouil,C., Sigurdsson,S., Lumley,T., DeStefano,A.L., Fazekas,F.,
            Vrooman,H.A., Shibata,D.K., Maillard,P., Zijdenbos,A., Smith,A.V.,
            Gudnason,H., de Boer,R., Cushman,M., Mazoyer,B., Heiss,G.,
            Vernooij,M.W., Enzinger,C., Glazer,N.L., Beiser,A., Knopman,D.S.,
            Cavalieri,M., Niessen,W.J., Harris,T.B., Petrovic,K., Lopez,O.L.,
            Au,R., Lambert,J.C., Hofman,A., Gottesman,R.F., Garcia,M.,
            Heckbert,S.R., Atwood,L.D., Catellier,D.J., Uitterlinden,A.G.,
            Yang,Q., Smith,N.L., Aspelund,T., Romero,J.R., Rice,K.,
            Taylor,K.D., Nalls,M.A., Rotter,J.I., Sharrett,R., van Duijn,C.M.,
            Amouyel,P., Wolf,P.A., Gudnason,V., van der Lugt,A., Boerwinkle,E.,
            Psaty,B.M., Seshadri,S., Tzourio,C., Breteler,M.M., Mosley,T.H.,
            Schmidt,R., Longstreth,W.T., DeCarli,C. and Launer,L.J.
  TITLE     Genome-wide association studies of cerebral white matter lesion
            burden: the CHARGE consortium
  JOURNAL   Ann Neurol 69 (6), 928-939 (2011)
   PUBMED   21681796
REFERENCE   9  (residues 1 to 638)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 638)
  AUTHORS   Vandeputte,D.A., Meije,C.B., van Dartel,M., Leenstra,S.,
            IJlst-Keizers,H., Das,P.K., Troost,D., Bosch,D.A., Baas,F. and
            Hulsebos,T.J.
  TITLE     GOA, a novel gene encoding a ring finger B-box coiled-coil protein,
            is overexpressed in astrocytoma
  JOURNAL   Biochem Biophys Res Commun 286 (3), 574-579 (2001)
   PUBMED   11511098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087289.9, AY026763.1 and BG385464.1.
            
            On Oct 28, 2004 this sequence version replaced NP_258411.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY026763.1, SRR3476690.997518.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2151358
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254816.6/ ENSP00000254816.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..638
                     /product="E3 ubiquitin-protein ligase TRIM47"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 47; RING finger
                     protein 100; gene overexpressed in astrocytoma protein"
                     /calculated_mol_wt=69401
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96LD4.2)"
     Region          7..>134
                     /region_name="rad18"
                     /note="DNA repair protein rad18; TIGR00599"
                     /db_xref="CDD:273165"
     Region          7..62
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(9,12,24,26,29,32,54,57)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438111"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0E3; propagated from
                     UniProtKB/Swiss-Prot (Q96LD4.2)"
     Region          79..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LD4.2)"
     Region          128..177
                     /region_name="Bbox1_TRIM25-like_C-IV"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing proteins, TRIM25, TRIM47 and similar
                     proteins; cd19842"
                     /db_xref="CDD:380900"
     Region          180..225
                     /region_name="Bbox2_TRIM16-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins, TRIM16, TRIM29, TRIM47 and
                     similar proteins; cd19769"
                     /db_xref="CDD:380827"
     Region          300..322
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LD4.2)"
     Region          384..411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LD4.2)"
     Region          421..626
                     /region_name="SPRY_PRY_TRIM47"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 47 (TRIM47), also known as RING finger protein 100
                     (RNF100) or Gene overexpressed in astrocytoma protein
                     (GOA); cd15808"
                     /db_xref="CDD:293980"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q96LD4.2)"
     Site            582
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q96LD4.2)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96LD4.2)"
     CDS             1..638
                     /gene="TRIM47"
                     /gene_synonym="GOA; RNF100"
                     /coded_by="NM_033452.3:34..1950"
                     /db_xref="CCDS:CCDS32737.1"
                     /db_xref="GeneID:91107"
                     /db_xref="HGNC:HGNC:19020"
                     /db_xref="MIM:611041"
ORIGIN      
        1 mdgsgpfscp icleplrepv tlpcghnfcl aclgalwphr gasgaggpgg aarcplcqep
       61 fpdglqlrkn htlsellqlr qgsgpgsgpg papalapeps apsalpsvpe psapcapepw
      121 pageepvrcd acpegaalpa alsclsclas fcpahlgphe rspalrghrl vpplrrlees
      181 lcprhlrple rycraervcl ceacaaqehr ghelvpleqe ralqeaeqsk vlsavedrmd
      241 elgagiaqsr rtvaliksaa vaerervsrl fadaaaalqg fqtqvlgfie egeaamlgrs
      301 qgdlrrqeeq rsrlsrarqn lsqvpeadsv sflqellalr laledgcgpg pgpprelsft
      361 kssqavravr dmlavacvnq weqlrgpggn edgpqkldse adaepqdles tnlleseapr
      421 dyflkfayiv dldsdtadkf lqlfgtkgvk rvlcpinypl sptrfthceq vlgegaldrg
      481 tyyweveiie gwvsmgvmae dfspqepydr grlgrnahsc clqwngrsfs vwfhgleapl
      541 phpfsptvgv cleyadrala fyavrdgkms llrrlkasrp rrggipaspi dpfqsrldsh
      601 faglfthrlk pafflesvda hlqigplkks cisvlkrr
//
LOCUS       NP_078948                903 aa            linear   PRI 27-APR-2025
DEFINITION  DNA transposase THAP9 isoform 1 [Homo sapiens].
ACCESSION   NP_078948
VERSION     NP_078948.3
DBSOURCE    REFSEQ: accession NM_024672.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Yang,S., Wang,B., Liu,C., Wang,Q., Wang,R., Su,W., Zhu,Y., Li,M.,
            Guo,Z., Wu,X. and Chen,F.
  TITLE     THAP9-AS1 Promotes Tumorigenesis and Reduces ROS Generation through
            the JAK2/STAT3 Signaling Pathway by Increasing SOCS3 Promoter
            Methylation in Osteosarcoma
  JOURNAL   Oxid Med Cell Longev 2021, 5620475 (2021)
   PUBMED   34691358
  REMARK    GeneRIF: THAP9-AS1 Promotes Tumorigenesis and Reduces ROS
            Generation through the JAK2/STAT3 Signaling Pathway by Increasing
            SOCS3 Promoter Methylation in Osteosarcoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Sanghavi,H.M. and Majumdar,S.
  TITLE     Oligomerization of THAP9 Transposase via Amino-Terminal Domains
  JOURNAL   Biochemistry 60 (23), 1822-1835 (2021)
   PUBMED   34033475
  REMARK    GeneRIF: Oligomerization of THAP9 Transposase via Amino-Terminal
            Domains.
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Sharma,V., Thakore,P. and Majumdar,S.
  TITLE     THAP9 Transposase Cleaves DNA via Conserved Acidic Residues in an
            RNaseH-Like Domain
  JOURNAL   Cells 10 (6), 1351 (2021)
   PUBMED   34072453
  REMARK    GeneRIF: THAP9 Transposase Cleaves DNA via Conserved Acidic
            Residues in an RNaseH-Like Domain.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Cheng,J., Ma,H., Yan,M. and Xing,W.
  TITLE     THAP9-AS1/miR-133b/SOX4 positive feedback loop facilitates the
            progression of esophageal squamous cell carcinoma
  JOURNAL   Cell Death Dis 12 (4), 401 (2021)
   PUBMED   33854048
  REMARK    GeneRIF: THAP9-AS1/miR-133b/SOX4 positive feedback loop facilitates
            the progression of esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Majumdar,S., Singh,A. and Rio,D.C.
  TITLE     The human THAP9 gene encodes an active P-element DNA transposase
  JOURNAL   Science 339 (6118), 446-448 (2013)
   PUBMED   23349291
  REMARK    GeneRIF: results indicate that human THAP9 is an active DNA
            transposase that, although 'domesticated,' still retains the
            catalytic activity to mobilize P transposable elements across
            species
REFERENCE   7  (residues 1 to 903)
  AUTHORS   Sabogal,A., Lyubimov,A.Y., Corn,J.E., Berger,J.M. and Rio,D.C.
  TITLE     THAP proteins target specific DNA sites through bipartite
            recognition of adjacent major and minor grooves
  JOURNAL   Nat Struct Mol Biol 17 (1), 117-123 (2010)
   PUBMED   20010837
REFERENCE   8  (residues 1 to 903)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 903)
  AUTHORS   Hammer,S.E., Strehl,S. and Hagemann,S.
  TITLE     Homologs of Drosophila P transposons were mobile in zebrafish but
            have been domesticated in a common ancestor of chicken and human
  JOURNAL   Mol Biol Evol 22 (4), 833-844 (2005)
   PUBMED   15616143
REFERENCE   10 (residues 1 to 903)
  AUTHORS   Roussigne,M., Kossida,S., Lavigne,A.C., Clouaire,T., Ecochard,V.,
            Glories,A., Amalric,F. and Girard,J.P.
  TITLE     The THAP domain: a novel protein motif with similarity to the
            DNA-binding domain of P element transposase
  JOURNAL   Trends Biochem Sci 28 (2), 66-69 (2003)
   PUBMED   12575992
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA317935.1, DB154392.1, AC021105.13 and AA478110.1.
            
            On May 4, 2006 this sequence version replaced NP_078948.2.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The extent of this transcript
            is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.156336.1,
                                           SRR1660805.76018.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302236.10/ ENSP00000305533.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..903
                     /product="DNA transposase THAP9 isoform 1"
                     /note="THAP domain-containing protein 9; DNA transposase
                     THAP9"
                     /calculated_mol_wt=103280
     Region          5..88
                     /region_name="THAP"
                     /note="THAP domain; pfam05485"
                     /db_xref="CDD:461662"
     Region          123..126
                     /region_name="HCFC1-binding motif (HBM).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5L6.2)"
     Region          <216..388
                     /region_name="Tnp_P_element"
                     /note="Transposase protein; pfam12017"
                     /db_xref="CDD:288840"
     CDS             1..903
                     /gene="THAP9"
                     /gene_synonym="hTh9"
                     /coded_by="NM_024672.6:69..2780"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3598.1"
                     /db_xref="GeneID:79725"
                     /db_xref="HGNC:HGNC:23192"
                     /db_xref="MIM:612537"
ORIGIN      
        1 mtrscsavgc strdtvlsre rglsfhqfpt dtiqrskwir avnrvdprsk kiwipgpgai
       61 lcskhfqesd fesygirrkl kkgavpsvsl ykipqgvhlk gkarqkilkq plpdnsqeva
      121 tedhnyslkt pltigaekla evqqmlqvsk krlisvknyr mikkrkglrl idalveekll
      181 seetecllra qfsdfkwely nwretdeysa emkqfactly lcsskvydyv rkilklphss
      241 ilrtwlskcq pspgfnsnif sflqrrveng dqlyqycsll iksmplkqql qwdpsshslq
      301 gfmdfglgkl dadetplase tvllmavgif ghwrtplgyf fvnrasgylq aqllrltigk
      361 lsdigitvla vtsdatahsv qmakalgihi dgddmkctfq hpssssqqia yffdschllr
      421 lirnafqnfq siqfingiah wqhlvelval eeqelsnmer ipstlanlkn hvlkvnsatq
      481 lfsesvasal eyllsldlpp fqncigtihf lrlinnlfdi fnsrncygkg lkgpllpety
      541 skinhvliea ktifvtlsdt snnqiikgkq klgflgflln aeslkwlyqn yvfpkvmpfp
      601 ylltykfshd hlelflkmlr qvlvtssspt cmafqkayyn letrykfqde vflskvsifd
      661 isiarrkdla lwtvqrqygv svtktvfhee gicqdwshcs lsealldlsd hrrnlicyag
      721 yvanklsall tcedcitaly asdlkaskig sllfvkkkng lhfpseslcr vinicervvr
      781 thsrmaifel vskqrelylq qkilcelsgh inlfvdvnkh lfdgevcain hfvkllkdii
      841 icflnirakn vaqnplkhhs ertdmktlsr khwssvqdyk cssfantssk frhllsndgy
      901 pfk
//
LOCUS       NP_055926                544 aa            linear   PRI 27-APR-2025
DEFINITION  NEDD4-binding protein 3 [Homo sapiens].
ACCESSION   NP_055926 XP_038920
VERSION     NP_055926.1
DBSOURCE    REFSEQ: accession NM_015111.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Luo,M., Li,J., Yang,Q., Xu,S., Zhang,K., Chen,J., Zhang,S.,
            Zheng,S. and Zhou,J.
  TITLE     N4BP3 promotes breast cancer metastasis via NEDD4-mediated
            E-cadherin ubiquitination and degradation
  JOURNAL   Cancer Lett 550, 215926 (2022)
   PUBMED   36162713
  REMARK    GeneRIF: N4BP3 promotes breast cancer metastasis via NEDD4-mediated
            E-cadherin ubiquitination and degradation.
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Han,H., Zhu,W., Lin,T., Liu,C. and Zhai,H.
  TITLE     N4BP3 promotes angiogenesis in hepatocellular carcinoma by binding
            with KAT2B
  JOURNAL   Cancer Sci 113 (10), 3390-3404 (2022)
   PUBMED   35848906
  REMARK    GeneRIF: N4BP3 promotes angiogenesis in hepatocellular carcinoma by
            binding with KAT2B.
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Wang,C., Ling,T., Zhong,N. and Xu,L.G.
  TITLE     N4BP3 Regulates RIG-I-Like Receptor Antiviral Signaling Positively
            by Targeting Mitochondrial Antiviral Signaling Protein
  JOURNAL   Front Microbiol 12, 770600 (2021)
   PUBMED   34880843
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 544)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 544)
  AUTHORS   Zhou,J., Liu,X., Wang,C. and Li,C.
  TITLE     The correlation analysis of miRNAs and target genes in metastasis
            of cervical squamous cell carcinoma
  JOURNAL   Epigenomics 10 (3), 259-275 (2018)
   PUBMED   29343084
  REMARK    GeneRIF: N4BP3 was associated with the survival time of cervical
            squamous cell carcinoma patients. mir-451 and mir-486 were related
            to tumor differentiation stage.
REFERENCE   6  (residues 1 to 544)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 544)
  AUTHORS   Liu,S., Chen,J., Cai,X., Wu,J., Chen,X., Wu,Y.T., Sun,L. and
            Chen,Z.J.
  TITLE     MAVS recruits multiple ubiquitin E3 ligases to activate antiviral
            signaling cascades
  JOURNAL   Elife 2, e00785 (2013)
   PUBMED   23951545
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 544)
  AUTHORS   Murillas,R., Simms,K.S., Hatakeyama,S., Weissman,A.M. and
            Kuehn,M.R.
  TITLE     Identification of developmentally expressed proteins that
            functionally interact with Nedd4 ubiquitin ligase
  JOURNAL   J Biol Chem 277 (4), 2897-2907 (2002)
   PUBMED   11717310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC136632.3.
            
            On Apr 4, 2005 this sequence version replaced XP_038920.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053323.1, SRR1163657.454904.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274605.6/ ENSP00000274605.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..544
                     /product="NEDD4-binding protein 3"
                     /calculated_mol_wt=60339
     Region          61..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15049.3)"
     Region          116..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15049.3)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15049.3)"
     Region          260..>438
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          335..365
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15049.3)"
     Region          368..526
                     /region_name="Fez1"
                     /note="pfam06818"
                     /db_xref="CDD:462015"
     Region          430..465
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15049.3)"
     CDS             1..544
                     /gene="N4BP3"
                     /gene_synonym="LZTS4"
                     /coded_by="NM_015111.2:271..1905"
                     /db_xref="CCDS:CCDS34307.1"
                     /db_xref="GeneID:23138"
                     /db_xref="HGNC:HGNC:29852"
                     /db_xref="MIM:619140"
ORIGIN      
        1 matapgpagi amgsvgslle rqdfspeelr aalagsrgsr qpdgllrkgl gqreflsylh
       61 lpkkdskstk ntkraprnep adyatlyyre hsragdfskt slpergrfdk crirpsvfkp
      121 tagngkgfls mqslashkgq klwrsngslh tlachpplsp gprasqaraq llhalsldeg
      181 gpepepslsd sssggsfgrs pgtgpspfss slghlnhlgg sldrasqgpk eagppavlsc
      241 lpeppppyef scssaeemga vlpetceelk rglgdedgsn pftqvleerq rlwlaelkrl
      301 yverlhevtq kaersernlq lqlfmaqqeq rrlrkelraq qglapeprap gtlpeadpsa
      361 rpeeearwev cqktaeisll kqqlreaqae laqklaeifs lktqlrgsra qaqaqdaelv
      421 rlreavrslq eqapreeapg scetddcksr gllgeaggse ardsaeqlra ellqerlrgq
      481 eqalrfeqer rtwqeekerv lryqreiqgg ymdmyrrnqa leqelralre pptpwsprle
      541 sski
//
LOCUS       NP_001353515             791 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 19 [Homo
            sapiens].
ACCESSION   NP_001353515 XP_016855522
VERSION     NP_001353515.1
DBSOURCE    REFSEQ: accession NM_001366586.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 791)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 791)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 791)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 791)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 791)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855522.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.15411.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..791
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 19"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=88809
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <38..126
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <493..>627
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..791
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366586.1:2055..4430"
                     /note="isoform 19 is encoded by transcript variant 24"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rtksrspspa pekkektpel pepsvkvkep
      121 svqeatstsd ilkvpkpepi pepkepspek nskkekekek trprsrsrsk srsrtrsrsp
      181 shtrprrrhr srsrsysprr rpsprrrpsp rrrtpprrmp ppprhrrsrs pvrrrrrssa
      241 slsgssssss ssrsrsppkk ppkrtssppr ktrrlspsas pprrrhrpsp patpppktrh
      301 sptpqqsnrt rksrvsvspg rtsgkvtkhk gtekrespsp apkprkvels eseedkggkm
      361 aaadsvqqrr qyrrqnqqss sdsgssssse derpkrshvk ngevgrrrrh spsrsaspsp
      421 rkrqketspr grrrrspspp ptrrrrspsp appprrrrtp tppprrrtps ppprrrspsp
      481 rrysppiqrr yspspppkrr taspppppkr raspspppkr rvshspppkq rsspvtkrrs
      541 pslsskhrkg sspsrstrea rspqpnkrhs psprprapqt ssspppvrrg assspqrrqs
      601 pspstrpirr vsrtpepkki kkaaspspqs vrrvsssrsv sgspepaakk ppappspvqs
      661 qspstnwspa vpvkkakspt pspspprnsd qegggkkkkk kkdkkhkkdk khkkhkkhkk
      721 ekavaaaaaa avtpaaiaaa tttlaqeepv aapepkkete seaednlddl ekhlrekalr
      781 smrkaqvspq s
//
LOCUS       NP_006031                456 aa            linear   PRI 27-APR-2025
DEFINITION  heparan sulfate glucosamine 3-O-sulfotransferase 4 [Homo sapiens].
ACCESSION   NP_006031 XP_056254
VERSION     NP_006031.2
DBSOURCE    REFSEQ: accession NM_006040.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Ohka,S., Yamada,S., Nishizawa,D., Fukui,Y., Arita,H., Hanaoka,K.,
            Iseki,M., Kato,J., Ogawa,S., Hiranuma,A., Kasai,S., Hasegawa,J.,
            Hayashida,M., Fukushi,S., Saijo,M. and Ikeda,A.K.
  TITLE     Heparan sulfate 3-O-sulfotransferase 4 is genetically associated
            with herpes zoster and enhances varicella-zoster virus-mediated
            fusogenic activity
  JOURNAL   Mol Pain 17, 17448069211052171 (2021)
   PUBMED   34904858
  REMARK    GeneRIF: Heparan sulfate 3-O-sulfotransferase 4 is genetically
            associated with herpes zoster and enhances varicella-zoster
            virus-mediated fusogenic activity.
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Debette,S., Ibrahim Verbaas,C.A., Bressler,J., Schuur,M., Smith,A.,
            Bis,J.C., Davies,G., Wolf,C., Gudnason,V., Chibnik,L.B., Yang,Q.,
            deStefano,A.L., de Quervain,D.J., Srikanth,V., Lahti,J.,
            Grabe,H.J., Smith,J.A., Priebe,L., Yu,L., Karbalai,N., Hayward,C.,
            Wilson,J.F., Campbell,H., Petrovic,K., Fornage,M., Chauhan,G.,
            Yeo,R., Boxall,R., Becker,J., Stegle,O., Mather,K.A., Chouraki,V.,
            Sun,Q., Rose,L.M., Resnick,S., Oldmeadow,C., Kirin,M., Wright,A.F.,
            Jonsdottir,M.K., Au,R., Becker,A., Amin,N., Nalls,M.A.,
            Turner,S.T., Kardia,S.L., Oostra,B., Windham,G., Coker,L.H.,
            Zhao,W., Knopman,D.S., Heiss,G., Griswold,M.E., Gottesman,R.F.,
            Vitart,V., Hastie,N.D., Zgaga,L., Rudan,I., Polasek,O.,
            Holliday,E.G., Schofield,P., Choi,S.H., Tanaka,T., An,Y.,
            Perry,R.T., Kennedy,R.E., Sale,M.M., Wang,J., Wadley,V.G.,
            Liewald,D.C., Ridker,P.M., Gow,A.J., Pattie,A., Starr,J.M.,
            Porteous,D., Liu,X., Thomson,R., Armstrong,N.J., Eiriksdottir,G.,
            Assareh,A.A., Kochan,N.A., Widen,E., Palotie,A., Hsieh,Y.C.,
            Eriksson,J.G., Vogler,C., van Swieten,J.C., Shulman,J.M.,
            Beiser,A., Rotter,J., Schmidt,C.O., Hoffmann,W., Nothen,M.M.,
            Ferrucci,L., Attia,J., Uitterlinden,A.G., Amouyel,P.,
            Dartigues,J.F., Amieva,H., Raikkonen,K., Garcia,M., Wolf,P.A.,
            Hofman,A., Longstreth,W.T. Jr., Psaty,B.M., Boerwinkle,E.,
            DeJager,P.L., Sachdev,P.S., Schmidt,R., Breteler,M.M., Teumer,A.,
            Lopez,O.L., Cichon,S., Chasman,D.I., Grodstein,F.,
            Muller-Myhsok,B., Tzourio,C., Papassotiropoulos,A., Bennett,D.A.,
            Ikram,M.A., Deary,I.J., van Duijn,C.M., Launer,L.,
            Fitzpatrick,A.L., Seshadri,S. and Mosley,T.H. Jr.
  CONSRTM   Cohorts for Heart and Aging Research in Genomic Epidemiology
            Consortium
  TITLE     Genome-wide studies of verbal declarative memory in nondemented
            older people: the Cohorts for Heart and Aging Research in Genomic
            Epidemiology consortium
  JOURNAL   Biol Psychiatry 77 (8), 749-763 (2015)
   PUBMED   25648963
  REMARK    GeneRIF: This study provided that additional genome-wide
            associations, near HS3ST4 were identified and other putative
            modulators of memory performance were revealed by a pathway
            approach and hippocampal gene expression analyses.
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Deng,X., Sabino,E.C., Cunha-Neto,E., Ribeiro,A.L., Ianni,B.,
            Mady,C., Busch,M.P. and Seielstad,M.
  CONSRTM   REDSII Chagas Study Group from the NHLBI Retrovirus Epidemiology
            Donor Study-II Component International
  TITLE     Genome wide association study (GWAS) of Chagas cardiomyopathy in
            Trypanosoma cruzi seropositive subjects
  JOURNAL   PLoS One 8 (11), e79629 (2013)
   PUBMED   24324551
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Mochizuki,H., Yoshida,K., Shibata,Y. and Kimata,K.
  TITLE     Tetrasulfated disaccharide unit in heparan sulfate: enzymatic
            formation and tissue distribution
  JOURNAL   J Biol Chem 283 (45), 31237-31245 (2008)
   PUBMED   18757372
  REMARK    GeneRIF: The 3OST-2 and -4 are specifically expressed in brain.
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Lawrence,R., Yabe,T., Hajmohammadi,S., Rhodes,J., McNeely,M.,
            Liu,J., Lamperti,E.D., Toselli,P.A., Lech,M., Spear,P.G.,
            Rosenberg,R.D. and Shworak,N.W.
  TITLE     The principal neuronal gD-type 3-O-sulfotransferases and their
            products in central and peripheral nervous system tissues
  JOURNAL   Matrix Biol 26 (6), 442-455 (2007)
   PUBMED   17482450
  REMARK    GeneRIF: 3-OST-2 and 3-OST-4 are the major neural gD-type 3-OSTs,
            and so are prime candidates for participating in HS-dependent
            neurobiologic events.
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Tiwari,V., O'Donnell,C.D., Oh,M.J., Valyi-Nagy,T. and Shukla,D.
  TITLE     A role for 3-O-sulfotransferase isoform-4 in assisting HSV-1 entry
            and spread
  JOURNAL   Biochem Biophys Res Commun 338 (2), 930-937 (2005)
   PUBMED   16259945
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Liu,J., Shriver,Z., Pope,R.M., Thorp,S.C., Duncan,M.B.,
            Copeland,R.J., Raska,C.S., Yoshida,K., Eisenberg,R.J., Cohen,G.,
            Linhardt,R.J. and Sasisekharan,R.
  TITLE     Characterization of a heparan sulfate octasaccharide that binds to
            herpes simplex virus type 1 glycoprotein D
  JOURNAL   J Biol Chem 277 (36), 33456-33467 (2002)
   PUBMED   12080045
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Shworak,N.W., Liu,J., Petros,L.M., Zhang,L., Kobayashi,M.,
            Copeland,N.G., Jenkins,N.A. and Rosenberg,R.D.
  TITLE     Multiple isoforms of heparan sulfate D-glucosaminyl
            3-O-sulfotransferase. Isolation, characterization, and expression
            of human cdnas and identification of distinct genomic loci
  JOURNAL   J Biol Chem 274 (8), 5170-5184 (1999)
   PUBMED   9988767
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092141.4, AF105378.2 and
            AC093511.4.
            
            On May 31, 2006 this sequence version replaced NP_006031.1.
            
            Summary: This gene encodes the enzyme heparan sulfate
            D-glucosaminyl 3-O-sulfotransferase 4. This enzyme generates
            3-O-sulfated glucosaminyl residues in heparan sulfate. Cell surface
            heparan sulfate is used as a receptor by herpes simplex virus type
            1 (HSV-1), and expression of this gene is thought to play a role in
            HSV-1 pathogenesis. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL834283.1, AF105378.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331351.6/ ENSP00000330606.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.1"
     Protein         1..456
                     /product="heparan sulfate glucosamine 3-O-sulfotransferase
                     4"
                     /EC_number="2.8.2.23"
                     /note="heparan sulfate 3-O-sulfotransferase 4; heparan
                     sulfate D-glucosaminyl 3-O-sulfotransferase 4; heparan
                     sulfate (glucosamine) 3-O-sulfotransferase 4"
                     /calculated_mol_wt=49668
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y661.3)"
     Site            35..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y661.3)"
     Region          68..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y661.3)"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y661.3)"
     Region          154..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y661.3)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y661.3)"
     Region          197..434
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; pfam00685"
                     /db_xref="CDD:425820"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y661.3)"
     Site            389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y661.3)"
     CDS             1..456
                     /gene="HS3ST4"
                     /gene_synonym="3-OST-4; 30ST4; 3OST4; h3-OST-4"
                     /coded_by="NM_006040.3:460..1830"
                     /db_xref="CCDS:CCDS53995.1"
                     /db_xref="GeneID:9951"
                     /db_xref="HGNC:HGNC:5200"
                     /db_xref="MIM:604059"
ORIGIN      
        1 marwpapppp pppppplaap pppgasakgp parkllfmct lslsvtylcy sllggsgslq
       61 fplalqespg aaaepppspp ppsllptpvr lgapsqppap ppldnashge ppeppeqpaa
      121 pgtdgwglps ggggaqdawl rtplapsemi taqsalpere aqessttded lagrraangs
      181 serggavstp dygekklpqa liigvkkggt ralleairvh pdvravgvep hffdrnyekg
      241 lewyrnvmpk tldgqitmek tpsyfvtnea pkrihsmakd iklivvvrnp vtraisdytq
      301 tlskkpeipt fevlafknrt lglidaswsa irigiyalhl enwlqyfpls qilfvsgerl
      361 ivdpagemak vqdflglkrv vtekhfyfnk tkgfpclkkp edssaprclg kskgrthpri
      421 dpdvihrlrk fykpfnlmfy qmtgqdfqwe qeegdk
//
LOCUS       NP_005583                869 aa            linear   PRI 27-APR-2025
DEFINITION  muscle, skeletal receptor tyrosine-protein kinase isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_005583
VERSION     NP_005583.1
DBSOURCE    REFSEQ: accession NM_005592.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 869)
  AUTHORS   Uyen Dao,T.M., Barbeau,S., Messeant,J., Della-Gaspera,B.,
            Bouceba,T., Semprez,F., Legay,C. and Dobbertin,A.
  TITLE     The collagen ColQ binds to LRP4 and regulates the activation of the
            Muscle-Specific Kinase-LRP4 receptor complex by agrin at the
            neuromuscular junction
  JOURNAL   J Biol Chem 299 (8), 104962 (2023)
   PUBMED   37356721
  REMARK    GeneRIF: The collagen ColQ binds to LRP4 and regulates the
            activation of the Muscle-Specific Kinase-LRP4 receptor complex by
            agrin at the neuromuscular junction.
REFERENCE   2  (residues 1 to 869)
  AUTHORS   Zhang,S., Ohkawara,B., Ito,M., Huang,Z., Zhao,F., Nakata,T.,
            Takeuchi,T., Sakurai,H., Komaki,H., Kamon,M., Araki,T. and Ohno,K.
  TITLE     A mutation in DOK7 in congenital myasthenic syndrome forms
            aggresome in cultured cells, and reduces DOK7 expression and MuSK
            phosphorylation in patient-derived iPS cells
  JOURNAL   Hum Mol Genet 32 (9), 1511-1523 (2023)
   PUBMED   36579833
  REMARK    GeneRIF: A mutation in DOK7 in congenital myasthenic syndrome forms
            aggresome in cultured cells, and reduces DOK7 expression and MuSK
            phosphorylation in patient-derived iPS cells.
REFERENCE   3  (residues 1 to 869)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 869)
  AUTHORS   Mori,S., Suzuki,S., Konishi,T., Kawaguchi,N., Kishi,M.,
            Kuwabara,S., Ishizuchi,K., Zhou,H., Shibasaki,F., Tsumoto,H.,
            Omura,T., Miura,Y., Mori,S., Higashihara,M., Murayama,S. and
            Shigemoto,K.
  TITLE     Proteolytic ectodomain shedding of muscle-specific tyrosine kinase
            in myasthenia gravis
  JOURNAL   Exp Neurol 361, 114300 (2023)
   PUBMED   36525997
  REMARK    GeneRIF: Proteolytic ectodomain shedding of muscle-specific
            tyrosine kinase in myasthenia gravis.
REFERENCE   5  (residues 1 to 869)
  AUTHORS   Chevessier,F., Faraut,B., Ravel-Chapuis,A., Richard,P., Gaudon,K.,
            Bauche,S., Prioleau,C., Herbst,R., Goillot,E., Ioos,C.,
            Azulay,J.P., Attarian,S., Leroy,J.P., Fournier,E., Legay,C.,
            Schaeffer,L., Koenig,J., Fardeau,M., Eymard,B., Pouget,J. and
            Hantai,D.
  TITLE     MUSK, a new target for mutations causing congenital myasthenic
            syndrome
  JOURNAL   Hum Mol Genet 13 (24), 3229-3240 (2004)
   PUBMED   15496425
  REMARK    GeneRIF: Missense mutation does not affect MuSK catalytic kinase
            activity but diminishes expression and stability.
REFERENCE   6  (residues 1 to 869)
  AUTHORS   Apel,E.D., Glass,D.J., Moscoso,L.M., Yancopoulos,G.D. and
            Sanes,J.R.
  TITLE     Rapsyn is required for MuSK signaling and recruits synaptic
            components to a MuSK-containing scaffold
  JOURNAL   Neuron 18 (4), 623-635 (1997)
   PUBMED   9136771
REFERENCE   7  (residues 1 to 869)
  AUTHORS   DeChiara,T.M., Bowen,D.C., Valenzuela,D.M., Simmons,M.V.,
            Poueymirou,W.T., Thomas,S., Kinetz,E., Compton,D.L., Rojas,E.,
            Park,J.S., Smith,C., DiStefano,P.S., Glass,D.J., Burden,S.J. and
            Yancopoulos,G.D.
  TITLE     The receptor tyrosine kinase MuSK is required for neuromuscular
            junction formation in vivo
  JOURNAL   Cell 85 (4), 501-512 (1996)
   PUBMED   8653786
REFERENCE   8  (residues 1 to 869)
  AUTHORS   Valenzuela,D.M., Stitt,T.N., DiStefano,P.S., Rojas,E., Mattsson,K.,
            Compton,D.L., Nunez,L., Park,J.S., Stark,J.L., Gies,D.R. et al.
  TITLE     Receptor tyrosine kinase specific for the skeletal muscle lineage:
            expression in embryonic muscle, at the neuromuscular junction, and
            after injury
  JOURNAL   Neuron 15 (3), 573-584 (1995)
   PUBMED   7546737
REFERENCE   9  (residues 1 to 869)
  AUTHORS   Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of 21 novel human protein kinases, including 3
            members of a family related to the cell cycle regulator nimA of
            Aspergillus nidulans
  JOURNAL   Cell Growth Differ 4 (10), 821-830 (1993)
   PUBMED   8274451
REFERENCE   10 (residues 1 to 869)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513328.12 and AL157881.14.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a muscle-specific tyrosine kinase
            receptor. The encoded protein may play a role in clustering of the
            acetylcholine receptor in the postsynaptic neuromuscular junction.
            Mutations in this gene have been associated with congenital
            myasthenic syndrome. Alternatively spliced transcript variants have
            been described.[provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF006464.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374448.9/ ENSP00000363571.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..869
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..869
                     /product="muscle, skeletal receptor tyrosine-protein
                     kinase isoform 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="muscle, skeletal receptor tyrosine-protein kinase;
                     muscle-specific kinase receptor; muscle-specific
                     tyrosine-protein kinase receptor; muscle, skeletal,
                     receptor tyrosine kinase"
                     /calculated_mol_wt=94494
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O15146.1)"
                     /calculated_mol_wt=2581
     mat_peptide     24..869
                     /product="Muscle, skeletal receptor tyrosine-protein
                     kinase. /id=PRO_0000024446"
                     /note="propagated from UniProtKB/Swiss-Prot (O15146.1)"
                     /calculated_mol_wt=94494
     Region          28..117
                     /region_name="IgI_1_MuSK"
                     /note="agrin-responsive first immunoglobulin-like domains
                     (Ig1) of the MuSK ectodomain; a member of the I-set of
                     IgSF domains; cd20970"
                     /db_xref="CDD:409562"
     Region          28..31
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409562"
     Region          35..39
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409562"
     Region          45..52
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409562"
     Region          58..63
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409562"
     Region          65..67
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409562"
     Region          75..78
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409562"
     Region          82..88
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409562"
     Region          95..102
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409562"
     Region          109..117
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409562"
     Region          122..209
                     /region_name="IgI_2_MuSK"
                     /note="agrin-responsive second immunoglobulin-like domains
                     (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a
                     member of the I-set of Ig superfamily domains; cd20968"
                     /db_xref="CDD:409560"
     Region          122..125
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409560"
     Region          129..131
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409560"
     Region          137..145
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409560"
     Region          151..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409560"
     Region          158..161
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409560"
     Region          166..170
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409560"
     Region          173..179
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409560"
     Region          186..194
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409560"
     Region          197..202
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409560"
     Region          204..209
                     /region_name="Ig strand G'"
                     /note="Ig strand G' [structural motif]"
                     /db_xref="CDD:409560"
     Region          218..286
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O15146.1)"
     Region          315..457
                     /region_name="CRD_FZ"
                     /note="CRD_domain cysteine-rich domain, also known as Fz
                     (frizzled) domain; cl02447"
                     /db_xref="CDD:470581"
     Site            order(324,326..327,332..334)
                     /site_type="other"
                     /note="putative Wnt binding site [polypeptide binding]"
                     /db_xref="CDD:143549"
     Site            338
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O15146.1)"
     Site            496..516
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15146.1)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q61006; propagated from
                     UniProtKB/Swiss-Prot (O15146.1)"
     Region          569..858
                     /region_name="PTKc_Musk"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Muscle-specific kinase; cd05050"
                     /db_xref="CDD:133181"
     Site            order(581..585,589,607,609,655..658,661..662,725,729..730,
                     732,743,761..765,774,808)
                     /site_type="active"
                     /db_xref="CDD:133181"
     Site            order(581..582,584..585,589,607,609,655..658,661..662,
                     729..730,732,743)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133181"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:Q61006; propagated from
                     UniProtKB/Swiss-Prot (O15146.1)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:Q61006; propagated from
                     UniProtKB/Swiss-Prot (O15146.1)"
     Site            order(725,729,761..765,774,808)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133181"
     Site            742..767
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133181"
     Site            755
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62838; propagated from
                     UniProtKB/Swiss-Prot (O15146.1)"
     CDS             1..869
                     /gene="MUSK"
                     /gene_synonym="CMS9; FADS; FADS1"
                     /coded_by="NM_005592.4:115..2724"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS48005.1"
                     /db_xref="GeneID:4593"
                     /db_xref="HGNC:HGNC:7525"
                     /db_xref="MIM:601296"
ORIGIN      
        1 mrelvniplv hiltlvafsg teklpkapvi ttpletvdal veevatfmca vesypqpeis
       61 wtrnkilikl fdtrysiren gqlltilsve dsddgiycct anngvggave scgalqvkmk
      121 pkitrppinv kiieglkavl pcttmgnpkp svswikgdsp lrensriavl esgslrihnv
      181 qkedagqyrc vaknslgtay skvvklevev farilrapes hnvtfgsfvt lhctatgipv
      241 ptitwiengn avssgsiqes vkdrvidsrl qlfitkpgly tciatnkhge kfstakaaat
      301 isiaewskpq kdnkgycaqy rgevcnavla kdalvflnts yadpeeaqel lvhtawnelk
      361 vvspvcrpaa eallcnhifq ecspgvvptp ipicreycla vkelfcakew lvmeekthrg
      421 lyrsemhlls vpecsklpsm hwdptacarl phldynkenl ktfppmtssk psvdipnlps
      481 sssssfsvsp tysmtviisi mssfaifvll tittlyccrr rkqwknkkre saavtlttlp
      541 sellldrlhp npmyqrmpll lnpkllsley prnnieyvrd igegafgrvf qarapgllpy
      601 epftmvavkm lkeeasadmq adfqreaalm aefdnpnivk llgvcavgkp mcllfeymay
      661 gdlneflrsm sphtvcslsh sdlsmraqvs spgppplsca eqlciarqva agmaylserk
      721 fvhrdlatrn clvgenmvvk iadfglsrni ysadyykane ndaipirwmp pesifynryt
      781 tesdvwaygv vlweifsygl qpyygmahee viyyvrdgni lscpencpve lynlmrlcws
      841 klpadrpsft sihrilermc eraegtvsv
//
LOCUS       NP_009120                623 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-binding cassette sub-family F member 2 [Homo sapiens].
ACCESSION   NP_009120
VERSION     NP_009120.1
DBSOURCE    REFSEQ: accession NM_007189.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Li,W., Li,G. and Cao,L.
  TITLE     Circular RNA Eps15-homology domain-containing protein 2 induce
            resistance of renal cell carcinoma to sunitinib via
            microRNA-4731-5p/ABCF2 axis
  JOURNAL   Bioengineered 13 (4), 9729-9740 (2022)
   PUBMED   35412955
  REMARK    GeneRIF: Circular RNA Eps15-homology domain-containing protein 2
            induce resistance of renal cell carcinoma to sunitinib via
            microRNA-4731-5p/ABCF2 axis.
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Bao,L., Wu,J., Dodson,M., Rojo de la Vega,E.M., Ning,Y., Zhang,Z.,
            Yao,M., Zhang,D.D., Xu,C. and Yi,X.
  TITLE     ABCF2, an Nrf2 target gene, contributes to cisplatin resistance in
            ovarian cancer cells
  JOURNAL   Mol Carcinog 56 (6), 1543-1553 (2017)
   PUBMED   28112439
  REMARK    GeneRIF: The NRF2-overexpressing cell line, containing high levels
            of ABCF2, was more resistant to cisplatin-induced apoptosis
            compared to its control ovarian cancer cell line; whereas the NRF2
            knockdown cell line with low levels of ABCF2, was more sensitive to
            cisplatin treatment than its control cell line.
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Lauc,G., Huffman,J.E., Pucic,M., Zgaga,L., Adamczyk,B., Muzinic,A.,
            Novokmet,M., Polasek,O., Gornik,O., Kristic,J., Keser,T.,
            Vitart,V., Scheijen,B., Uh,H.W., Molokhia,M., Patrick,A.L.,
            McKeigue,P., Kolcic,I., Lukic,I.K., Swann,O., van Leeuwen,F.N.,
            Ruhaak,L.R., Houwing-Duistermaat,J.J., Slagboom,P.E., Beekman,M.,
            de Craen,A.J., Deelder,A.M., Zeng,Q., Wang,W., Hastie,N.D.,
            Gyllensten,U., Wilson,J.F., Wuhrer,M., Wright,A.F., Rudd,P.M.,
            Hayward,C., Aulchenko,Y., Campbell,H. and Rudan,I.
  TITLE     Loci associated with N-glycosylation of human immunoglobulin G show
            pleiotropy with autoimmune diseases and haematological cancers
  JOURNAL   PLoS Genet 9 (1), e1003225 (2013)
   PUBMED   23382691
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Ando-Akatsuka,Y., Shimizu,T., Numata,T. and Okada,Y.
  TITLE     Involvements of the ABC protein ABCF2 and alpha-actinin-4 in
            regulation of cell volume and anion channels in human epithelial
            cells
  JOURNAL   J Cell Physiol 227 (10), 3498-3510 (2012)
   PUBMED   22252987
  REMARK    GeneRIF: Overexpression of ABCF2 suppressed RVD.
REFERENCE   5  (residues 1 to 623)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 623)
  AUTHORS   Cheng,J., Kapranov,P., Drenkow,J., Dike,S., Brubaker,S., Patel,S.,
            Long,J., Stern,D., Tammana,H., Helt,G., Sementchenko,V.,
            Piccolboni,A., Bekiranov,S., Bailey,D.K., Ganesh,M., Ghosh,S.,
            Bell,I., Gerhard,D.S. and Gingeras,T.R.
  TITLE     Transcriptional maps of 10 human chromosomes at 5-nucleotide
            resolution
  JOURNAL   Science 308 (5725), 1149-1154 (2005)
   PUBMED   15790807
REFERENCE   7  (residues 1 to 623)
  AUTHORS   Dean,M., Rzhetsky,A. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Genome Res 11 (7), 1156-1166 (2001)
   PUBMED   11435397
  REMARK    Review article
REFERENCE   8  (residues 1 to 623)
  AUTHORS   Zhang,F., Hogue,D.L., Liu,L., Fisher,C.L., Hui,D., Childs,S. and
            Ling,V.
  TITLE     M-ABC2, a new human mitochondrial ATP-binding cassette membrane
            protein
  JOURNAL   FEBS Lett 478 (1-2), 89-94 (2000)
   PUBMED   10922475
REFERENCE   9  (residues 1 to 623)
  AUTHORS   Klein,I., Sarkadi,B. and Varadi,A.
  TITLE     An inventory of the human ABC proteins
  JOURNAL   Biochim Biophys Acta 1461 (2), 237-262 (1999)
   PUBMED   10581359
  REMARK    Review article
REFERENCE   10 (residues 1 to 623)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY165500.1, AC021097.5,
            BG720644.1 and BC001661.2.
            
            Summary: This gene encodes a member of the ATP-binding cassette
            (ABC) transporter superfamily. ATP-binding cassette proteins
            transport various molecules across extra- and intracellular
            membranes. Alterations in this gene may be involved in cancer
            progression. Related pseudogenes have been identified on
            chromosomes 3 and 7. [provided by RefSeq, Mar 2019].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.178542.1,
                                           SRR1803613.268729.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287844.7/ ENSP00000287844.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..623
                     /product="ATP-binding cassette sub-family F member 2"
                     /note="ABC-type transport protein; iron-inhibited ABC
                     transporter 2; ATP-binding cassette, sub-family F (GCN20),
                     member 2"
                     /calculated_mol_wt=71159
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG63.2)"
     Region          90..604
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UG63.2)"
     Site            304
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UG63.2)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UG63.2)"
     CDS             1..623
                     /gene="ABCF2"
                     /gene_synonym="ABC28; EST133090; HUSSY-18; HUSSY18"
                     /coded_by="NM_007189.3:86..1957"
                     /db_xref="CCDS:CCDS5923.1"
                     /db_xref="GeneID:10061"
                     /db_xref="HGNC:HGNC:71"
                     /db_xref="MIM:612510"
ORIGIN      
        1 mpsdlakkka akkkeaakar qrprkgheen gdvvtepqva ekneangret tevdlltkel
       61 edfemkkaaa ravtgvlash pnstdvhiin lsltfhgqel lsdtklelns grrygligln
      121 gigksmllsa igkrevpipe hidiyhltre mppsdktplh cvmevdtera mlekeaerla
      181 hedaeceklm elyerleeld adkaemrasr ilhglgftpa mqrkklkdfs ggwrmrvala
      241 ralfirpfml lldeptnhld ldacvwleee lktfkrilvl vshsqdflng vctniihmhn
      301 kklkyytgny dqyvktrlel eenqmkrfhw eqdqiahmkn yiarfghgsa klarqaqske
      361 ktlqkmmasg ltervvsdkt lsfyfppcgk ipppvimvqn vsfkytkdgp ciynnlefgi
      421 dldtrvalvg pngagkstll klltgellpt dgmirkhshv kigryhqhlq eqldldlspl
      481 eymmkcypei kekeemrkii grygltgkqq vspirnlsdg qkcrvclawl awqnphmlfl
      541 deptnhldie tidaladain efeggmmlvs hdfrliqqva qeiwvcekqt itkwpgdila
      601 ykehlksklv deepqltkrt hnv
//
LOCUS       NP_612432                436 aa            linear   PRI 27-APR-2025
DEFINITION  protein GOLM2 isoform a [Homo sapiens].
ACCESSION   NP_612432
VERSION     NP_612432.2
DBSOURCE    REFSEQ: accession NM_138423.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Li,R., Dong,X., Chen,S., Tan,J., Chen,X., Liu,J., Wen,T. and Ru,X.
  TITLE     Tn antigen promotes breast cancer metastasis via impairment of
            CASC4
  JOURNAL   Cell Biol Int 47 (11), 1854-1867 (2023)
   PUBMED   37493437
  REMARK    GeneRIF: Tn antigen promotes breast cancer metastasis via
            impairment of CASC4.
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Duval,S., Abu-Thuraia,A., Elkholi,I.E., Chen,R., Seebun,D.,
            Mayne,J., Cote,J.F., Figeys,D. and Seidah,N.G.
  TITLE     Shedding of cancer susceptibility candidate 4 by the convertases
            PC7/furin unravels a novel secretory protein implicated in cancer
            progression
  JOURNAL   Cell Death Dis 11 (8), 665 (2020)
   PUBMED   32820145
  REMARK    GeneRIF: Shedding of cancer susceptibility candidate 4 by the
            convertases PC7/furin unravels a novel secretory protein implicated
            in cancer progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Anczukow,O., Akerman,M., Clery,A., Wu,J., Shen,C., Shirole,N.H.,
            Raimer,A., Sun,S., Jensen,M.A., Hua,Y., Allain,F.H. and
            Krainer,A.R.
  TITLE     SRSF1-Regulated Alternative Splicing in Breast Cancer
  JOURNAL   Mol Cell 60 (1), 105-117 (2015)
   PUBMED   26431027
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Sato,T., Peiper,M., Heinecke,A., Zurakowski,D., Eisenberger,C.F.,
            Hosch,S., Knoefel,W.T. and Izbicki,J.R.
  TITLE     Expression of HER2/neu does not correlate with survival in soft
            tissue sarcoma
  JOURNAL   Onkologie 26 (3), 268-271 (2003)
   PUBMED   12845212
  REMARK    GeneRIF: Of 62 analyzed specimens, 43 tumors were HER2/neu negative
            compared to 19 HER2/neu positive tumors. Kaplan-Meier analysis
            indicated no difference in survival according to HER2/neu
            expression (p = 0.31, log-rank test = 1.10
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Scheer,M., Prange,W., Petmecky,K., Schirmacher,P., Zoller,J.E. and
            Kubler,A.C.
  TITLE     [Evaluation of her-2/neu amplification/overexpression in OSCC with
            fluorescence in situ hybridization (FISH) and immunohistochemistry]
  JOURNAL   Mund Kiefer Gesichtschir 7 (3), 138-145 (2003)
   PUBMED   12764679
  REMARK    GeneRIF: In spite of missing correlation between survival and
            her-2/ neu overexpression in our study, the predictive value of the
            her-2/ neu protooncogene in adjuvant therapy in OSCC needs further
            investigation.
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Oh,J.J., Grosshans,D.R., Wong,S.G. and Slamon,D.J.
  TITLE     Identification of differentially expressed genes associated with
            HER-2/neu overexpression in human breast cancer cells
  JOURNAL   Nucleic Acids Res 27 (20), 4008-4017 (1999)
   PUBMED   10497265
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB229269.1, BC012124.1,
            AL832840.1 and BI467176.1.
            
            On Apr 14, 2003 this sequence version replaced NP_612432.1.
            
            Summary: The increased expression level of this gene is associated
            with HER-2/neu proto-oncogene overexpression. Amplification and
            resulting overexpression of this proto-oncogene are found in
            approximately 30% of human breast and 20% of human ovarian cancers.
            Alternatively spliced variants encoding different isoforms have
            been identified for this gene. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript, and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.32507.1,
                                           SRR1803611.134875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299957.11/ ENSP00000299957.6
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.3"
     Protein         1..436
                     /product="protein GOLM2 isoform a"
                     /note="gene associated with HER-2/neu overexpression;
                     protein CASC4; cancer susceptibility candidate gene 4
                     protein; cancer susceptibility candidate 4; cancer
                     susceptibility 4; protein GOLM2"
                     /calculated_mol_wt=49367
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:25732826,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q6P4E1.2)"
     Site            15..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P4E1.2)"
     Region          <42..>200
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          225..436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P4E1.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P4E1.2)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P4E1.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P4E1.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P4E1.2)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q6P4E1.2)"
     CDS             1..436
                     /gene="GOLM2"
                     /gene_synonym="CASC4; H63"
                     /coded_by="NM_138423.4:312..1622"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10108.1"
                     /db_xref="GeneID:113201"
                     /db_xref="HGNC:HGNC:24892"
ORIGIN      
        1 mvgfganrra grlpslvlvv llvvivvlaf nywsissrhv llqeevaelq gqvqrtevar
       61 grlekrnsdl lllvdthkkq idqkeadygr lssrlqareg lgkrceddkv klqnnisyqm
      121 adihhlkeql aelrqeflrq edqlqdyrkn ntylvkrley esfqcgqqmk elraqheeni
      181 kkladqflee qkqetqkiqs ndgkeldinn qvvpknipkv aenvadknee pssnhiphgk
      241 eqikrggdag mpgieendla kvddlppalr kppisvsqhe shqaishlpt gqplspnmpp
      301 dshinhngnp gtskqnpssp lqrlipgsnl dsepriqtdi lkqatkdrvs dfhklkqsrf
      361 fdenespvdp qhgskladyn gddgnvgeye adkqaelayn eeedgdggee dvqddeerel
      421 qmdpadygkq hfndvl
//
LOCUS       NP_660287                193 aa            linear   PRI 27-APR-2025
DEFINITION  DNA damage-inducible transcript 4-like protein [Homo sapiens].
ACCESSION   NP_660287
VERSION     NP_660287.1
DBSOURCE    REFSEQ: accession NM_145244.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Simonson,B., Subramanya,V., Chan,M.C., Zhang,A., Franchino,H.,
            Ottaviano,F., Mishra,M.K., Knight,A.C., Hunt,D., Ghiran,I.,
            Khurana,T.S., Kontaridis,M.I., Rosenzweig,A. and Das,S.
  TITLE     DDiT4L promotes autophagy and inhibits pathological cardiac
            hypertrophy in response to stress
  JOURNAL   Sci Signal 10 (468) (2017)
   PUBMED   28246202
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Koga,Y., Pelizzola,M., Cheng,E., Krauthammer,M., Sznol,M.,
            Ariyan,S., Narayan,D., Molinaro,A.M., Halaban,R. and Weissman,S.M.
  TITLE     Genome-wide screen of promoter methylation identifies novel markers
            in melanoma
  JOURNAL   Genome Res 19 (8), 1462-1470 (2009)
   PUBMED   19491193
  REMARK    GeneRIF: Promoter methylation and differential gene expression of
            five markers: COL1A2, NPM2, HSPB6, DDIT4L and MT1G were validated
            by sequencing of bisulfite-modified DNA and real-time reverse
            transcriptase PCR, respectively.
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Imen,J.S., Billiet,L., Cuaz-Perolin,C., Michaud,N. and Rouis,M.
  TITLE     The regulated in development and DNA damage response 2 (REDD2) gene
            mediates human monocyte cell death through a reduction in
            thioredoxin-1 expression
  JOURNAL   Free Radic Biol Med 46 (10), 1404-1410 (2009)
   PUBMED   19268525
  REMARK    GeneRIF: mediates monocyte cell death through a reduction in
            thioredoxin-1 expression
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Corradetti,M.N., Inoki,K. and Guan,K.L.
  TITLE     The stress-inducted proteins RTP801 and RTP801L are negative
            regulators of the mammalian target of rapamycin pathway
  JOURNAL   J Biol Chem 280 (11), 9769-9772 (2005)
   PUBMED   15632201
  REMARK    GeneRIF: RTP801 and RTP801L work downstream of AKT and upstream of
            TSC2 to inhibit mTOR functions
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Cuaz-Perolin,C., Furman,C., Larigauderie,G., Legedz,L.,
            Lasselin,C., Copin,C., Jaye,M., Searfoss,G., Yu,K.T., Duverger,N.,
            Negre-Salvayre,A., Fruchart,J.C. and Rouis,M.
  TITLE     REDD2 gene is upregulated by modified LDL or hypoxia and mediates
            human macrophage cell death
  JOURNAL   Arterioscler Thromb Vasc Biol 24 (10), 1830-1835 (2004)
   PUBMED   15308555
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Ellisen,L.W., Ramsayer,K.D., Johannessen,C.M., Yang,A., Beppu,H.,
            Minda,K., Oliner,J.D., McKeon,F. and Haber,D.A.
  TITLE     REDD1, a developmentally regulated transcriptional target of p63
            and p53, links p63 to regulation of reactive oxygen species
  JOURNAL   Mol Cell 10 (5), 995-1005 (2002)
   PUBMED   12453409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK094236.1 and BC013592.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK094236.1, SRR1803611.125486.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674, SAMN03267753
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000273990.6/ ENSP00000354830.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..193
                     /product="DNA damage-inducible transcript 4-like protein"
                     /note="homolog of mouse SMHS1; regulated in development
                     and DNA damage response 2; REDD-2; HIF-1 responsive
                     protein RTP801-like; protein regulated in development and
                     DNA damage response 2"
                     /calculated_mol_wt=21609
     Region          65..183
                     /region_name="RTP801_C"
                     /note="RTP801 C-terminal region; pfam07809"
                     /db_xref="CDD:462274"
     CDS             1..193
                     /gene="DDIT4L"
                     /gene_synonym="REDD2; Rtp801L"
                     /coded_by="NM_145244.4:216..797"
                     /db_xref="CCDS:CCDS34036.1"
                     /db_xref="GeneID:115265"
                     /db_xref="HGNC:HGNC:30555"
                     /db_xref="MIM:607730"
ORIGIN      
        1 mvatgslssk npasiselld cgyhpeslls dfdywdyvvp epnlnevife estcqnlvkm
       61 lenclskskq tklgcskvlv pekltqriaq dvlrlsstep cglrgcvmhv nleienvckk
      121 ldrivcdssv vptfeltlvf kqencswtsf rdfffsrgrf ssgfrrtlil ssgfrlvkkk
      181 lysligttvi egs
//
LOCUS       NP_001356045             896 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 618 isoform f [Mus musculus].
ACCESSION   NP_001356045
VERSION     NP_001356045.1
DBSOURCE    REFSEQ: accession NM_001369116.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 896)
  AUTHORS   Lee,D.J., Kim,H.Y., Lee,S.J. and Jung,H.S.
  TITLE     Spatiotemporal Changes in Transcriptome of Odontogenic and
            Non-odontogenic Regions in the Dental Arch of Mus musculus
  JOURNAL   Front Cell Dev Biol 9, 723326 (2021)
   PUBMED   34722506
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 896)
  AUTHORS   Quina,L.A., Wang,S., Ng,L. and Turner,E.E.
  TITLE     Brn3a and Nurr1 mediate a gene regulatory pathway for habenula
            development
  JOURNAL   J Neurosci 29 (45), 14309-14322 (2009)
   PUBMED   19906978
REFERENCE   3  (residues 1 to 896)
  AUTHORS   Georgas,K., Rumballe,B., Valerius,M.T., Chiu,H.S.,
            Thiagarajan,R.D., Lesieur,E., Aronow,B.J., Brunskill,E.W.,
            Combes,A.N., Tang,D., Taylor,D., Grimmond,S.M., Potter,S.S.,
            McMahon,A.P. and Little,M.H.
  TITLE     Analysis of early nephron patterning reveals a role for distal RV
            proliferation in fusion to the ureteric tip via a cap
            mesenchyme-derived connecting segment
  JOURNAL   Dev Biol 332 (2), 273-286 (2009)
   PUBMED   19501082
REFERENCE   4  (residues 1 to 896)
  AUTHORS   Long,J.E., Cobos,I., Potter,G.B. and Rubenstein,J.L.
  TITLE     Dlx1&2 and Mash1 transcription factors control MGE and CGE
            patterning and differentiation through parallel and overlapping
            pathways
  JOURNAL   Cereb Cortex 19 Suppl 1 (Suppl 1), i96-i106 (2009)
   PUBMED   19386638
REFERENCE   5  (residues 1 to 896)
  AUTHORS   Kumar,S., Tomooka,Y. and Noda,M.
  TITLE     Identification of a set of genes with developmentally
            down-regulated expression in the mouse brain
  JOURNAL   Biochem Biophys Res Commun 185 (3), 1155-1161 (1992)
   PUBMED   1378265
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL691431.20 and AL691496.13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.4444021.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..896
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 33.82 cM"
     Protein         1..896
                     /product="zinc finger protein 618 isoform f"
                     /note="neural precursor cell expressed, developmentally
                     down-regulated gene 10"
                     /calculated_mol_wt=98965
     Region          92..112
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          133..153
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..896
                     /gene="Zfp618"
                     /gene_synonym="2810031P15Rik; 2810040O04Rik; bM257P7.1;
                     D430033D05Rik; Nedd10; Znf618"
                     /coded_by="NM_001369116.1:368..3058"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:72701"
                     /db_xref="MGI:MGI:1919950"
ORIGIN      
        1 mtevkvktev pddyiqeviw qgeakeekag gkdstgdvpa eicvviggvr nqqtldgkap
       61 egsphggsvr srysgtwifd qalkyasgsy ecgicgkkyk yyncfqthvr ahrdteatsg
      121 egvsqsnnfr ytcdicgkky kyyscfqehr dlhavdvfsv egapenradp fdqgvvatde
      181 vkeeppepfq kigpktgnyt cefcgkqyky ytpyqehval hapistapgw eppedpdtgs
      241 ecshpevtps prfvaaktqs nqsgkkapas vvrctsllhr tppatqtqtf rapnsgspas
      301 kaaaentfsr rveskaqnhf eetnsssqns sepytcgacg iqfqfysnll ehmqshaadn
      361 ennitsnqsr sppaaveekw kpqaqrnsan ntttsgltpn svipekerqn iaerllrvmc
      421 adlgalsvvs gkeflklaqt lvdsgaryga fsvteilgnf ntlalkhlpr mynqvkvkvt
      481 calgsnaclg igvtchsqsv gpdscyilta yqaegnhiks yvlgvkgadi rdsgdlvhhw
      541 vqnvlsefvm seirtvyvtd crvstsafsk agmclrcsac alnsvvqsvl skrtlqarsm
      601 heviellnvc edlagstgla ketfgsleet spppcwnsvt dslllvhery eqicefysra
      661 kkmnliqsln khllsnlaai ltpvkqavie lsnesqptlq lvlptyvrle klftakanda
      721 gtvsklchlf lealkenfkv hpahkvamil dpqqklrpvp pyqheeiisk vcelinevke
      781 swaeeadfep aakkarsatg ehpaaqeedr lgknevydyl qeplfqatpd lfqywscvtq
      841 khtklaklaf wllavpavga rsgcvnmceq allikrrrll spedmnklmf lksnml
//
LOCUS       NP_079133               1844 aa            linear   PRI 27-APR-2025
DEFINITION  ATPase family AAA domain-containing protein 5 [Homo sapiens].
ACCESSION   NP_079133 XP_947519 XP_951057
VERSION     NP_079133.3
DBSOURCE    REFSEQ: accession NM_024857.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1844)
  AUTHORS   Park,S.H., Kim,N., Kang,N., Ryu,E., Lee,E.A., Ra,J.S., Gartner,A.,
            Kang,S., Myung,K. and Lee,K.Y.
  TITLE     Short-range end resection requires ATAD5-mediated PCNA unloading
            for faithful homologous recombination
  JOURNAL   Nucleic Acids Res 51 (19), 10519-10535 (2023)
   PUBMED   37739427
  REMARK    GeneRIF: Short-range end resection requires ATAD5-mediated PCNA
            unloading for faithful homologous recombination.
REFERENCE   2  (residues 1 to 1844)
  AUTHORS   Itzkovich,Z., Choudhary,K., Arbel,M. and Kupiec,M.
  TITLE     Effects of Defective Unloading and Recycling of PCNA Revealed by
            the Analysis of ELG1 Mutants
  JOURNAL   Int J Mol Sci 24 (2), 1568 (2023)
   PUBMED   36675081
  REMARK    GeneRIF: Effects of Defective Unloading and Recycling of PCNA
            Revealed by the Analysis of ELG1 Mutants.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1844)
  AUTHORS   Park,S.H., Kim,Y., Ra,J.S., Wie,M.W., Kang,M.S., Kang,S., Myung,K.
            and Lee,K.Y.
  TITLE     Timely termination of repair DNA synthesis by ATAD5 is important in
            oxidative DNA damage-induced single-strand break repair
  JOURNAL   Nucleic Acids Res 49 (20), 11746-11764 (2021)
   PUBMED   34718749
  REMARK    GeneRIF: Timely termination of repair DNA synthesis by ATAD5 is
            important in oxidative DNA damage-induced single-strand break
            repair.
REFERENCE   4  (residues 1 to 1844)
  AUTHORS   Kim,S.J., Wie,M., Park,S.H., Kim,T.M., Park,J.H., Kim,S., Myung,K.
            and Lee,K.Y.
  TITLE     ATAD5 suppresses centrosome over-duplication by regulating UAF1 and
            ID1
  JOURNAL   Cell Cycle 19 (15), 1952-1968 (2020)
   PUBMED   32594826
  REMARK    GeneRIF: ATAD5 suppresses centrosome over-duplication by regulating
            UAF1 and ID1.
REFERENCE   5  (residues 1 to 1844)
  AUTHORS   Kim,S., Kang,N., Park,S.H., Wells,J., Hwang,T., Ryu,E., Kim,B.G.,
            Hwang,S., Kim,S.J., Kang,S., Lee,S., Stirling,P., Myung,K. and
            Lee,K.Y.
  TITLE     ATAD5 restricts R-loop formation through PCNA unloading and RNA
            helicase maintenance at the replication fork
  JOURNAL   Nucleic Acids Res 48 (13), 7218-7238 (2020)
   PUBMED   32542338
  REMARK    GeneRIF: ATAD5 restricts R-loop formation through PCNA unloading
            and RNA helicase maintenance at the replication fork.
REFERENCE   6  (residues 1 to 1844)
  AUTHORS   Gudbjartsson,D.F., Walters,G.B., Thorleifsson,G., Stefansson,H.,
            Halldorsson,B.V., Zusmanovich,P., Sulem,P., Thorlacius,S.,
            Gylfason,A., Steinberg,S., Helgadottir,A., Ingason,A.,
            Steinthorsdottir,V., Olafsdottir,E.J., Olafsdottir,G.H.,
            Jonsson,T., Borch-Johnsen,K., Hansen,T., Andersen,G., Jorgensen,T.,
            Pedersen,O., Aben,K.K., Witjes,J.A., Swinkels,D.W., den Heijer,M.,
            Franke,B., Verbeek,A.L., Becker,D.M., Yanek,L.R., Becker,L.C.,
            Tryggvadottir,L., Rafnar,T., Gulcher,J., Kiemeney,L.A., Kong,A.,
            Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Many sequence variants affecting diversity of adult human height
  JOURNAL   Nat Genet 40 (5), 609-615 (2008)
   PUBMED   18391951
REFERENCE   7  (residues 1 to 1844)
  AUTHORS   Douglas,J., Cilliers,D., Coleman,K., Tatton-Brown,K., Barker,K.,
            Bernhard,B., Burn,J., Huson,S., Josifova,D., Lacombe,D., Malik,M.,
            Mansour,S., Reid,E., Cormier-Daire,V., Cole,T. and Rahman,N.
  CONSRTM   Childhood Overgrowth Collaboration
  TITLE     Mutations in RNF135, a gene within the NF1 microdeletion region,
            cause phenotypic abnormalities including overgrowth
  JOURNAL   Nat Genet 39 (8), 963-965 (2007)
   PUBMED   17632510
REFERENCE   8  (residues 1 to 1844)
  AUTHORS   Ishii,H., Inageta,T., Mimori,K., Saito,T., Sasaki,H., Isobe,M.,
            Mori,M., Croce,C.M., Huebner,K., Ozawa,K. and Furukawa,Y.
  TITLE     Frag1, a homolog of alternative replication factor C subunits,
            links replication stress surveillance with apoptosis
  JOURNAL   Proc Natl Acad Sci U S A 102 (27), 9655-9660 (2005)
   PUBMED   15983387
  REMARK    GeneRIF: The Frag1 signal pathway, by linking replication stress
            surveillance with apoptosis induction, plays a central role in
            determining whether DNA damage is compatible with cell survival or
            whether it requires cell elimination by apoptosis.
REFERENCE   9  (residues 1 to 1844)
  AUTHORS   Jenne,D.E., Tinschert,S., Reimann,H., Lasinger,W., Thiel,G.,
            Hameister,H. and Kehrer-Sawatzki,H.
  TITLE     Molecular characterization and gene content of breakpoint
            boundaries in patients with neurofibromatosis type 1 with 17q11.2
            microdeletions
  JOURNAL   Am J Hum Genet 69 (3), 516-527 (2001)
   PUBMED   11468690
REFERENCE   10 (residues 1 to 1844)
  AUTHORS   Jenne,D.E., Tinschert,S., Stegmann,E., Reimann,H., Nurnberg,P.,
            Horn,D., Naumann,I., Buske,A. and Thiel,G.
  TITLE     A common set of at least 11 functional genes is lost in the
            majority of NF1 patients with gross deletions
  JOURNAL   Genomics 66 (1), 93-97 (2000)
   PUBMED   10843809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC127024.4, AL832103.1, AJ314648.2, DR159473.1 and DB527289.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_947519.1, XP_951057.1, NP_079133.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ314648.2, AY557611.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321990.5/ ENSP00000313171.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1844
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..1844
                     /product="ATPase family AAA domain-containing protein 5"
                     /note="enhanced level of genomic instability 1 homolog;
                     chromosome fragility-associated gene 1 protein; chromosome
                     fragility associated gene 1"
                     /calculated_mol_wt=207440
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          178..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4QY64; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          368..384
                     /region_name="Interaction with WDR48.
                     /evidence=ECO:0000269|PubMed:20147293"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          477..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          580..623
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          658..700
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            817
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          987..1047
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1051..>1167
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          1092..1118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            1116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1203..1235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1272..1292
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1428..1432
                     /region_name="LXCXE motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1591..1635
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1630..1719
                     /region_name="Interaction with RAD51 and RFC5.
                     /evidence=ECO:0000269|PubMed:31844045"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     CDS             1..1844
                     /gene="ATAD5"
                     /gene_synonym="C17orf41; ELG1; FRAG1"
                     /coded_by="NM_024857.5:383..5917"
                     /db_xref="CCDS:CCDS11260.1"
                     /db_xref="GeneID:79915"
                     /db_xref="HGNC:HGNC:25752"
                     /db_xref="MIM:609534"
ORIGIN      
        1 mvgvlamaaa aapppvkdce iepckkrkkd ddtstcktit kylsplgktr drvfappkps
       61 nildyfrkts ptnektqlgk eckikspesv pvdsnkdctt plemfsnvef kkkrkrvnls
      121 hqlnnikten eapieissdd skedyslnnd fvesstsvlr ykkqvevlae niqdtksqpn
      181 tmtslqnskk vnpkqgttkn dfkklrkrkc rdvvdlsesl plaeelnllk kdgkdtkqme
      241 nttshansrd nvteaaqlnd siitvsyeef lkshkenkve eipdstmsic vpsetvdeiv
      301 ksgyisesen seisqqvrfk tvtvlaqvhp ippkktgkip riflkqkqfe menslsdpen
      361 eqtvqkrksn vviqeeelel avleagssea vkpkctleer qqfmkafrqp asdalkngvk
      421 kssdkqkdln ekclyevgrd dnskkimens giqmvskngn lqlhtdkgsf lkeknkklkk
      481 knkktldtga ipgknregnt qkkettfflk ekqyqnrmsl rqrkteffks stlfnneslv
      541 yedianddll kvsslcnnnk lsrktsipvk dikltqskae seasllnvst pkstrrsgri
      601 sstpttetir gidsddvqdn sqlkastqka anlsekhsly taelitvpfd sespirmkft
      661 ristpkkskk ksnkrsekse atdggftsqi rkasntskni skakqlieka kalhisrskv
      721 teeiaiplrr ssrhqtlper kklsetedsv iiidssptal khpeknqkkl qclndvlgkk
      781 lntstknvpg kmkvaplflv rkaqkaadpv psfdessqdt seksqdcdvq ckakrdflms
      841 glpdllkrqi akkaaaldvy navstsfqrv vhvqqkddgc clwhlkppsc plltkfkeln
      901 tkvidlskcg ialgefstln sklksgnsaa vfmrtrkeft eevrnlllee irwsnpefsl
      961 kkyfplllkk qiehqvlsse chskqelead vshketkrkl veaenskskr kkpneysknl
     1021 ektnrkseel skrnnssgik ldsskdsgte dmlwtekyqp qtaseligne laikklhswl
     1081 kdwkrraele erqnlkgkrd ekhedfsggi dfkgssddee esrlcntvli tgptgvgkta
     1141 avyacaqelg fkifevnass qrsgrqilsq lkeatqshqv dkqgvnsqkp cffnsyyigk
     1201 spkkisspkk vvtsprkvpp pspkssgpkr alppktlany fkvspkpknn eeigmllenn
     1261 kgiknsfeqk qitqtkstna tnsnvkdvga eepsrknats lilfeevdvi fdedagflna
     1321 iktfmattkr pvilttsdpt fslmfdgcfe eikfstpsll nvasylqmic ltenfrtdvk
     1381 dfvtlltant cdirksilyl qfwirsgggv leerpltlyr gnsrnvqlvc sehgldnkiy
     1441 pkntkkkrvd lpkcdsgcae tlfglknifs psedlfsflk hkitmkeewh kfiqlltefq
     1501 mrnvdflysn lefilplpvd tipetknfcg psvtvdasaa tksmnclark hsereqplkk
     1561 sqkkkqkktl vilddsdlfd tdldfpdqsi slssvssssn aeesktgdee skardkgnnp
     1621 etkksipcpp kttagkkcsa lvshclnsls efmdnmsfld alltdvreqn kygrndfswt
     1681 ngkvtsglcd efslesndgw tsqssgelka aaealsftkc ssaiskalet lnsckklgrd
     1741 ptndltfyvs qkrnnvyfsq saanldnawk risviksvfs srsllyvgnr qasiieylpt
     1801 lrnicktekl keqgkskrrf lhyfegihld ipketvntla adfp
//
LOCUS       NP_001350086            1311 aa            linear   ROD 27-APR-2025
DEFINITION  C-Jun-amino-terminal kinase-interacting protein 4 isoform 8 [Mus
            musculus].
ACCESSION   NP_001350086 XP_017170249
VERSION     NP_001350086.1
DBSOURCE    REFSEQ: accession NM_001363157.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1311)
  AUTHORS   Tian,M., Zhang,L., Zhang,M., Qiao,L., Xu,B., Li,C., Liu,S.,
            Song,Y., Wei,Z., Wang,Y. and Wang,H.
  TITLE     JLP/Foxk1/N-cadherin axis fosters a partial epithelial-mesenchymal
            transition state in epithelial tubular cells
  JOURNAL   iScience 26 (4), 106396 (2023)
   PUBMED   37013185
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1311)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1311)
  AUTHORS   Mohan,R.A., Bosada,F.M., van Weerd,J.H., van Duijvenboden,K.,
            Wang,J., Mommersteeg,M.T.M., Hooijkaas,I.B., Wakker,V., de Gier-de
            Vries,C., Coronel,R., Boink,G.J.J., Bakkers,J., Barnett,P.,
            Boukens,B.J. and Christoffels,V.M.
  TITLE     T-box transcription factor 3 governs a transcriptional program for
            the function of the mouse atrioventricular conduction system
  JOURNAL   Proc Natl Acad Sci U S A 117 (31), 18617-18626 (2020)
   PUBMED   32675240
REFERENCE   4  (residues 1 to 1311)
  AUTHORS   Hanata,N., Shoda,H., Hatano,H., Nagafuchi,Y., Komai,T., Okamura,T.,
            Suzuki,A., Gunarta,I.K., Yoshioka,K., Yamamoto,K. and Fujio,K.
  TITLE     Peptidylarginine Deiminase 4 Promotes the Renal Infiltration of
            Neutrophils and Exacerbates the TLR7 Agonist-Induced Lupus Mice
  JOURNAL   Front Immunol 11, 1095 (2020)
   PUBMED   32655553
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1311)
  AUTHORS   Yan,Q., Zhu,K., Zhang,L., Fu,Q., Chen,Z., Liu,S., Fu,D.,
            Nakazato,R., Yoshioka,K., Diao,B., Ding,G., Li,X. and Wang,H.
  TITLE     A negative feedback loop between JNK-associated leucine zipper
            protein and TGF-beta1 regulates kidney fibrosis
  JOURNAL   Commun Biol 3 (1), 288 (2020)
   PUBMED   32504044
  REMARK    GeneRIF: A negative feedback loop between JNK-associated leucine
            zipper protein and TGF-beta1 regulates kidney fibrosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1311)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   7  (residues 1 to 1311)
  AUTHORS   Kelkar,N., Delmotte,M.H., Weston,C.R., Barrett,T., Sheppard,B.J.,
            Flavell,R.A. and Davis,R.J.
  TITLE     Morphogenesis of the telencephalic commissure requires scaffold
            protein JNK-interacting protein 3 (JIP3)
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 9843-9848 (2003)
   PUBMED   12897243
REFERENCE   8  (residues 1 to 1311)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 1311)
  AUTHORS   Lee,C.M., Onesime,D., Reddy,C.D., Dhanasekaran,N. and Reddy,E.P.
  TITLE     JLP: A scaffolding protein that tethers JNK/p38MAPK signaling
            modules and transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14189-14194 (2002)
   PUBMED   12391307
  REMARK    GeneRIF: describe a protein, JLP, which acts as a scaffolding
            protein to bring mitogen-activated protein kinases and their target
            transcription factors together for the execution of specific
            signaling pathways
REFERENCE   10 (residues 1 to 1311)
  AUTHORS   Bowman,A.B., Kamal,A., Ritchings,B.W., Philp,A.V., McGrail,M.,
            Gindhart,J.G. and Goldstein,L.S.
  TITLE     Kinesin-dependent axonal transport is mediated by the sunday driver
            (SYD) protein
  JOURNAL   Cell 103 (4), 583-594 (2000)
   PUBMED   11106729
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL662838.12.
            
            On May 10, 2018 this sequence version replaced XP_017170249.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164131,
                              SAMN01164132 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1311
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 58.9 cM"
     Protein         1..1311
                     /product="C-Jun-amino-terminal kinase-interacting protein
                     4 isoform 8"
                     /note="JNK-interacting protein 4; C-jun-amino-terminal
                     kinase-interacting protein 4; JNK-interacting leucine
                     zipper; JNK/SAPK-associated protein 2; JNK-associated
                     leucine-zipper protein; mitogen-activated protein kinase
                     8-interacting protein 4"
                     /calculated_mol_wt=145010
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          24..178
                     /region_name="Jnk-SapK_ap_N"
                     /note="JNK_SAPK-associated protein-1; pfam09744"
                     /db_xref="CDD:462875"
     Region          <33..>539
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          308..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          396..464
                     /region_name="JIP_LZII"
                     /note="JNK-interacting protein leucine zipper II;
                     pfam16471"
                     /db_xref="CDD:465127"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          463..490
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          553..590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            722
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          843..873
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          944..>1162
                     /region_name="WD40_2"
                     /note="WD40 repeated domain; pfam19056"
                     /db_xref="CDD:465964"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          1229..1257
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            1254
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     CDS             1..1311
                     /gene="Spag9"
                     /gene_synonym="3110018C07Rik; 4733401I23Rik;
                     4831406C20Rik; JIP-4; Jip4; JLP; JSAP2; JSAP2a; Mapk8ip4;
                     syd1"
                     /coded_by="NM_001363157.1:181..4116"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:70834"
                     /db_xref="MGI:MGI:1918084"
ORIGIN      
        1 meledgvvyq eepggsgavm servsglags iyreferlig rydeevvkel mplvvavlen
       61 ldsvfaqdqe hqvelellrd dneqlitqye rekalrkhae ekfiefedsq eqekkdlqtr
      121 veslesqtrq lelkaknyad qisrleerea elkkeynalh qrhtemihny mehlertklh
      181 qlsgsdqlea tahsrirker pislgifplp agdglltpdt qkggetpgse qwkfqelsqp
      241 rshtslkdel sdisqggska ttpastansd vsaippdtps kednegfvkg tdtsnkseis
      301 khievqvaqe trnvstesge neeksevqai iestpeldmd kdlsgykgss tptkgienka
      361 fdrnteslfe elssagsgli gdvdegadll geysgmgrev enlilentql letknalnvv
      421 kndliakvde ltcekdvlqg eleavkqakl kledknrele eelrkaraea edarqkakdd
      481 ddsdiptaqr krftrvemar vlmernqyke rlmelqeavr wtemirasre npamqekkrs
      541 siwqffsrlf ssssnatkkp eppvnlkyna ptshvtpsvk krsstlsqlp gdkskafdfl
      601 seeteaslas rreqkreqyr qvkahvqked grvqafgwsl pqkykqvang qgetkmknlp
      661 vpvylrplde kdasmklwca vgvnlsggkt rdggsvvgas vfykdiagld tegskqrsas
      721 qssldkldqe lkeqqkefkn qeelssqvwi ctsthsttkv iiidavqpgn ildsftvcns
      781 hvlciasvpg aretdypage elsesgqvdk aslcgsmtsn ssaemdsllg gitvvgcste
      841 gltgaatsps tngaspviek ppemetense vdeniptaee ateategnag stedtvdisq
      901 pgvytehvft dplgvqiped lspvfqssnd sdvykdqisv lpneqdlare eaqkmssllp
      961 tmwlgaqngc lyvhssvaqw rkclhsiklk dsilsivhvk givlvaladg tlaifhrgvd
     1021 gqwdlsnyhl ldlgrphhsi rcmtvvhdkv wcgyrnkiyv vqpkamkiek sfdahprkes
     1081 qvrqlawvgd gvwvsirlds tlrlyhahty qhlqdvdiep yvskmlgtgk lgfsfvrita
     1141 lmvscnrlwv gtgngviisi pltetnktsg tpgnrpgsvi rvygdensdk vtpgtfipyc
     1201 smahaqlcfh ghrdavkffv avpgqvispq sssggadlta dkagssaqep ssqtplksml
     1261 visggegyid frmgdegges ellgedlple psvtkaersh livwqvmcgn e
//
LOCUS       NP_005830                904 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_005830
VERSION     NP_005830.2
DBSOURCE    REFSEQ: accession NM_005839.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 904)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 904)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 904)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 904)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 904)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 904)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 904)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 904)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 904)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 904)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC036187.1, BC017315.2, AF048977.1 and CX782666.1.
            
            On Feb 12, 2004 this sequence version replaced NP_005830.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region compared to variant 1. The
            encoded isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036187.1, AF419855.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323848.14/ ENSP00000326261.8
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..904
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..904
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 2"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=102204
     Region          1..156
                     /region_name="Necessary for mRNA 3'-end cleavage and
                     cytoplasmic accumulation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          1..151
                     /region_name="Necessary for DNA and RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          139..904
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          300..688
                     /region_name="Necessary for speckles and matrix
                     localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            581
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          <606..>740
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            607
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            707
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            748
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            754
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            769
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            773
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            777
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            781
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            793
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            797
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            802
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            874
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     CDS             1..904
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_005839.4:26..2740"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS255.1"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkekt pelpepsvkv kepsvqeats
      241 tsdilkvpkp epipepkeps peknskkeke kektrprsrs rsksrsrtrs rspshtrprr
      301 rhrsrsrsys prrrpsprrr psprrrtppr rmpppprhrr srspvrrrrr ssaslsgsss
      361 sssssrsrsp pkkppkrtss pprktrrlsp saspprrrhr psppatpppk trhsptpqqs
      421 nrtrksrvsv spgrtsgkvt khkgtekres pspapkprkv elseseedkg gkmaaadsvq
      481 qrrqyrrqnq qsssdsgsss ssederpkrs hvkngevgrr rrhspsrsas psprkrqket
      541 sprgrrrrsp sppptrrrrs pspappprrr rtptppprrr tpsppprrrs psprrysppi
      601 qrryspsppp krrtaspppp pkrraspspp pkrrvshspp pkqrsspvtk rrspslsskh
      661 rkgsspsrst rearspqpnk rhspsprpra pqtssspppv rrgassspqr rqspspstrp
      721 irrvsrtpep kkikkaasps pqsvrrvsss rsvsgspepa akkppappsp vqsqspstnw
      781 spavpvkkak sptpspsppr nsdqegggkk kkkkkdkkhk kdkkhkkhkk hkkekavaaa
      841 aaaavtpaai aaatttlaqe epvaapepkk eteseaednl ddlekhlrek alrsmrkaqv
      901 spqs
//
LOCUS       NP_038470                356 aa            linear   PRI 27-APR-2025
DEFINITION  stomatin-like protein 2, mitochondrial isoform a [Homo sapiens].
ACCESSION   NP_038470
VERSION     NP_038470.1
DBSOURCE    REFSEQ: accession NM_013442.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Gong,H., Chen,S., Liu,S., Hu,Q., Li,Y., Li,Y., Li,G., Huang,K.,
            Li,R. and Fang,L.
  TITLE     Overexpressing lipid raft protein STOML2 modulates the tumor
            microenvironment via NF-kappaB signaling in colorectal cancer
  JOURNAL   Cell Mol Life Sci 81 (1), 39 (2024)
   PUBMED   38214751
  REMARK    GeneRIF: Overexpressing lipid raft protein STOML2 modulates the
            tumor microenvironment via NF-kappaB signaling in colorectal
            cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Attia,A.S., Hussein,S., Sameh,H., Khalil,A., Waley,A.B., Matar,I.
            and Sameh,R.
  TITLE     Diagnostic and prognostic utility of TROP-2, SLP-2, and CXCL12
            expression in papillary thyroid carcinoma
  JOURNAL   Cancer Biomark 39 (3), 211-221 (2024)
   PUBMED   38073379
  REMARK    GeneRIF: Diagnostic and prognostic utility of TROP-2, SLP-2, and
            CXCL12 expression in papillary thyroid carcinoma.
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Qin,C., Wang,Y., Zhao,B., Li,Z., Li,T., Yang,X., Zhao,Y. and
            Wang,W.
  TITLE     STOML2 restricts mitophagy and increases chemosensitivity in
            pancreatic cancer through stabilizing PARL-induced PINK1
            degradation
  JOURNAL   Cell Death Dis 14 (3), 191 (2023)
   PUBMED   36906621
  REMARK    GeneRIF: STOML2 restricts mitophagy and increases chemosensitivity
            in pancreatic cancer through stabilizing PARL-induced PINK1
            degradation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Genin,E.C., Bannwarth,S., Ropert,B., Lespinasse,F.,
            Mauri-Crouzet,A., Auge,G., Fragaki,K., Cochaud,C., Donnarumma,E.,
            Lacas-Gervais,S., Wai,T. and Paquis-Flucklinger,V.
  TITLE     CHCHD10 and SLP2 control the stability of the PHB complex: a key
            factor for motor neuron viability
  JOURNAL   Brain 145 (10), 3415-3430 (2022)
   PUBMED   35656794
  REMARK    GeneRIF: CHCHD10 and SLP2 control the stability of the PHB complex:
            a key factor for motor neuron viability.
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Zhang,L., Ding,F., Cao,W., Liu,Z., Liu,W., Yu,Z., Wu,Y., Li,W.,
            Li,Y. and Liu,Z.
  TITLE     Stomatin-like protein 2 is overexpressed in cancer and involved in
            regulating cell growth and cell adhesion in human esophageal
            squamous cell carcinoma
  JOURNAL   Clin Cancer Res 12 (5), 1639-1646 (2006)
   PUBMED   16533792
  REMARK    GeneRIF: overexpression of stomatin-like protein 2 is associated
            with neoplasms
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Guo,D., Han,J., Adam,B.L., Colburn,N.H., Wang,M.H., Dong,Z.,
            Eizirik,D.L., She,J.X. and Wang,C.Y.
  TITLE     Proteomic analysis of SUMO4 substrates in HEK293 cells under serum
            starvation-induced stress
  JOURNAL   Biochem Biophys Res Commun 337 (4), 1308-1318 (2005)
   PUBMED   16236267
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Owczarek,C.M., Treutlein,H.R., Portbury,K.J., Gulluyan,L.M.,
            Kola,I. and Hertzog,P.J.
  TITLE     A novel member of the STOMATIN/EPB72/mec-2 family, stomatin-like 2
            (STOML2), is ubiquitously expressed and localizes to HSA chromosome
            9p13.1
  JOURNAL   Cytogenet Cell Genet 92 (3-4), 196-203 (2001)
   PUBMED   11435687
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Wang,Y. and Morrow,J.S.
  TITLE     Identification and characterization of human SLP-2, a novel
            homologue of stomatin (band 7.2b) present in erythrocytes and other
            tissues
  JOURNAL   J Biol Chem 275 (11), 8062-8071 (2000)
   PUBMED   10713127
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF190167.1, AW273545.1, AA657517.1 and HY367065.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.63930.1,
                                           SRR5189658.32931.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155984 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356493.10/ ENSP00000348886.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..356
                     /product="stomatin-like protein 2, mitochondrial isoform
                     a"
                     /note="paratarg-7; paraprotein target 7; EPB72-like 2;
                     stomatin-like protein 2, mitochondrial; EPB72-like protein
                     2; stomatin (EPB72)-like 2"
                     /calculated_mol_wt=35689
     transit_peptide 1..28
                     /note="Mitochondrion. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (Q9UJZ1.1)"
                     /calculated_mol_wt=2863
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCZ.
                     /evidence=ECO:0000269|PubMed:21791414; propagated from
                     UniProtKB/Swiss-Prot (Q9UJZ1.1)"
     mat_peptide     29..356
                     /product="Stomatin-like protein 2, mitochondrial.
                     /id=PRO_0000094031"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJZ1.1)"
                     /calculated_mol_wt=35689
     Region          41..300
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q9UJZ1.1)"
     Site            145
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UJZ1.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UJZ1.1)"
     Region          321..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJZ1.1)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UJZ1.1)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UJZ1.1)"
     CDS             1..356
                     /gene="STOML2"
                     /gene_synonym="HSPC108; SLP-2"
                     /coded_by="NM_013442.3:38..1108"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6577.1"
                     /db_xref="GeneID:30968"
                     /db_xref="HGNC:HGNC:14559"
                     /db_xref="MIM:608292"
ORIGIN      
        1 mlaraargtg alllrgslla sgraprrass glprntvvlf vpqqeawvve rmgrfhrile
       61 pglnilipvl driryvqslk eivinvpeqs avtldnvtlq idgvlylrim dpykasygve
      121 dpeyavtqla qttmrselgk lsldkvfrer eslnasivda inqaadcwgi rclryeikdi
      181 hvpprvkesm qmqveaerrk ratvlesegt resainvaeg kkqaqilase aekaeqinqa
      241 ageasavlak akakaeairi laaaltqhng daaasltvae qyvsafskla kdsntillps
      301 npgdvtsmva qamgvygalt kapvpgtpds lssgssrdvq gtdasldeel drvkms
//
LOCUS       NP_001350691            2199 aa            linear   PRI 27-APR-2025
DEFINITION  dedicator of cytokinesis protein 10 isoform 3 [Homo sapiens].
ACCESSION   NP_001350691 XP_005246730
VERSION     NP_001350691.1
DBSOURCE    REFSEQ: accession NM_001363762.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2199)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 2199)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 2199)
  AUTHORS   Parrado,A.
  TITLE     Expression of DOCK10.1 protein revealed with a specific antiserum:
            insights into regulation of first exon isoforms of DOCK10
  JOURNAL   Mol Biol Rep 47 (4), 3003-3010 (2020)
   PUBMED   32112301
  REMARK    GeneRIF: Expression of DOCK10.1 protein revealed with a specific
            antiserum: insights into regulation of first exon isoforms of
            DOCK10.
REFERENCE   4  (residues 1 to 2199)
  AUTHORS   Shin,S., Buel,G.R., Nagiec,M.J., Han,M.J., Roux,P.P., Blenis,J. and
            Yoon,S.O.
  TITLE     ERK2 regulates epithelial-to-mesenchymal plasticity through
            DOCK10-dependent Rac1/FoxO1 activation
  JOURNAL   Proc Natl Acad Sci U S A 116 (8), 2967-2976 (2019)
   PUBMED   30728292
  REMARK    GeneRIF: we identified the transcription factor FoxO1 as a
            potential mediator of ERK2-induced EMT, and thus we investigated
            the mechanism by which ERK2 regulates FoxO1. Additionally, our
            analysis revealed that ERK2 induced the expression of Dock10, a
            Rac1/Cdc42 GEF, during EMT
REFERENCE   5  (residues 1 to 2199)
  AUTHORS   Kim,J.H., Cheong,H.S., Park,J.S., Jang,A.S., Uh,S.T., Kim,Y.H.,
            Kim,M.K., Choi,I.S., Cho,S.H., Choi,B.W., Bae,J.S., Park,C.S. and
            Shin,H.D.
  TITLE     A genome-wide association study of total serum and mite-specific
            IgEs in asthma patients
  JOURNAL   PLoS One 8 (8), e71958 (2013)
   PUBMED   23967269
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2199)
  AUTHORS   Alcaraz-Garcia,M.J., Ruiz-Lafuente,N., Sebastian-Ruiz,S.,
            Majado,M.J., Gonzalez-Garcia,C., Bernardo,M.V., Alvarez-Lopez,M.R.
            and Parrado,A.
  TITLE     Human and mouse DOCK10 splicing isoforms with alternative first
            coding exon usage are differentially expressed in T and B
            lymphocytes
  JOURNAL   Hum Immunol 72 (7), 531-537 (2011)
   PUBMED   21514340
  REMARK    GeneRIF: T cells and B cells exhibited inverse expression patterns
            of the DOCK10 isoforms
REFERENCE   7  (residues 1 to 2199)
  AUTHORS   Gadea,G., Sanz-Moreno,V., Self,A., Godi,A. and Marshall,C.J.
  TITLE     DOCK10-mediated Cdc42 activation is necessary for amoeboid invasion
            of melanoma cells
  JOURNAL   Curr Biol 18 (19), 1456-1465 (2008)
   PUBMED   18835169
  REMARK    GeneRIF: Silencing DOCK10 expression in melanoma promotes
            conversion to mesenchymal migration and is associated with
            decreased MLC2 phosphorylation and increased Rac1 activation.
REFERENCE   8  (residues 1 to 2199)
  AUTHORS   Yelo,E., Bernardo,M.V., Gimeno,L., Alcaraz-Garcia,M.J., Majado,M.J.
            and Parrado,A.
  TITLE     Dock10, a novel CZH protein selectively induced by interleukin-4 in
            human B lymphocytes
  JOURNAL   Mol Immunol 45 (12), 3411-3418 (2008)
   PUBMED   18499258
  REMARK    GeneRIF: Dock10 could represent a point of convergence for
            interleukin 4 signalling and small Rho GTPase function in B cells.
REFERENCE   9  (residues 1 to 2199)
  AUTHORS   Nishikimi,A., Meller,N., Uekawa,N., Isobe,K., Schwartz,M.A. and
            Maruyama,M.
  TITLE     Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide
            exchange factor expressed predominantly in lymphocytes
  JOURNAL   FEBS Lett 579 (5), 1039-1046 (2005)
   PUBMED   15710388
REFERENCE   10 (residues 1 to 2199)
  AUTHORS   Cote,J.F. and Vuori,K.
  TITLE     Identification of an evolutionarily conserved superfamily of
            DOCK180-related proteins with guanine nucleotide exchange activity
  JOURNAL   J Cell Sci 115 (Pt 24), 4901-4913 (2002)
   PUBMED   12432077
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093806.2 and AC011739.7.
            
            On May 30, 2018 this sequence version replaced XP_005246730.1.
            
            Summary: This gene encodes a member of the dedicator of cytokinesis
            protein family. Members of this family are guanosine nucleotide
            exchange factors for Rho GTPases and defined by the presence of
            conserved DOCK-homology regions. The encoded protein belongs to the
            D (or Zizimin) subfamily of DOCK proteins, which also contain an
            N-terminal pleckstrin homology domain. Alternatively spliced
            transcript variants that encode different isoforms have been
            described. [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (3) represents use of an alternate
            promoter, differs in the 5' UTR and 5' coding region, and initiates
            translation at a distinct start codon, compared to variant 1. The
            resulting protein (isoform 3) is longer and has a distinct
            N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.240663.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2199
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q36.2"
     Protein         1..2199
                     /product="dedicator of cytokinesis protein 10 isoform 3"
                     /note="zizimin3; dopamine receptor interacting protein 2"
                     /calculated_mol_wt=251185
     Region          58..168
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          195..315
                     /region_name="PH_DOCK-D"
                     /note="Dedicator of cytokinesis-D subfamily Pleckstrin
                     homology (PH) domain; cd13267"
                     /db_xref="CDD:270087"
     Region          684..873
                     /region_name="C2_Dock-D"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08697"
                     /db_xref="CDD:176079"
     Region          1709..2154
                     /region_name="DHR2_DOCK10"
                     /note="Dock Homology Region 2, a GEF domain, of Class D
                     Dedicator of Cytokinesis 10; cd11699"
                     /db_xref="CDD:212572"
     Site            order(1847,1857,1859..1860,1862..1863,1866..1867,
                     1869..1870,1873..1874)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212572"
     Site            order(1881..1884,1915..1916,1918..1921,1923..1924,
                     1943..1945,1962,1964,1993,1995,2002..2003,2009,2011,
                     2048..2049,2052,2066,2068,2072,2075..2077,2080..2086,2089,
                     2117,2135..2136,2138..2139,2142)
                     /site_type="other"
                     /note="Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212572"
     Site            2080..2085
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212572"
     CDS             1..2199
                     /gene="DOCK10"
                     /gene_synonym="DRIP2; Nbla10300; ZIZ3"
                     /coded_by="NM_001363762.1:60..6659"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS86925.1"
                     /db_xref="GeneID:55619"
                     /db_xref="HGNC:HGNC:23479"
                     /db_xref="MIM:611518"
ORIGIN      
        1 mgctasivll qafrsvvqrs cphicrrrqe epsheilple sddemnrprt liimqekprl
       61 lepldyetvi eelektyrnd plqdllffps ddfsaatvsw dirtlystvp edaehkaenl
      121 lvkeackfys sqwhvvnyky eqysgdirql praeykpekl pshsfeidhe dadkdedtts
      181 hssskgggga ggtgvfksgw lykgnfnstv nntvtvrsfk kryfqltqlp dnsyimnfyk
      241 dekiskepkg cifldsctgv vqnnrlrkya felkmndlty fvlaaetesd mdewihtlnr
      301 ilqispegpl qgrrsteltd lgldsldnsv tcectpeetd ssennlhadf akyltetedt
      361 vkttrnmerl nlfsldpdid tlklqkkdll epesvikpfe ekaakrimii ckalnsnlqg
      421 cvtenendpi tniepffvsv alydlrdsrk isadfhvdln haavrqmllg asvalengni
      481 dtitprqsee phikglpeew lkfpkqavfs vsnphseivl vakiekvlmg niasgaepyi
      541 knpdsnkyaq kilksnrqfc sklgkyrmpf awavrsvfkd nqgnvdrdsr fsplfrqess
      601 kistedlvkl vsdyrradri skmqtipgsl diavdnvple hpncvtssfi pvkpfnmmaq
      661 teptveveef vydstkycrp yrvyknqiyi ypkhlkydsq kcfnkarnit vciefknsde
      721 esakplkciy gkpggplfts aaytavlhhs qnpdfsdevk ielptqlhek hhilfsfyhv
      781 tcdinakana kkkealetsv gyawlplmkh dqiasqeyni piatslppny lsfqdsasgk
      841 hggsdikwvd ggkplfkvst fvvstvntqd phvnaffqec qkrekdmsqs ptsnfirsck
      901 nllnvekiha imsflpiiln qlfkvlvqne edeitttvtr vltdivakch eeqldhsvqs
      961 yikfvfktra ckertvheel aknvtgllks ndsttvkhvl khswfffaii lksmaqhlid
     1021 tnkiqlprpq rfpesyqnel dnlvmvlsdh viwkykdale etrranhsva rflkrcftfm
     1081 drgyvfkmvn nyismfssgd lktlcqykfd flqevcqheh fiplclpirs anipdpltps
     1141 estqelhasd mpeysvtnef crkhfligil lrevgfalqe dqdvrhlala vlknlmakhs
     1201 fddryreprk qaqiaslymp lygmlldnmp riylkdlypf tvntsnqgsr ddlstnggfq
     1261 sqtaikhans vdtsfskdvl nsiaafssia istvnhadsr aslasldsnp stnekssekt
     1321 dncekiprpl sligstlrfd kldqaetrsl lmcflhimkt isyetliayw qrapspevsd
     1381 ffsildvclq nfrylgkrni irkiaaafkf vqstqnngtl kgsnpscqts gllsqwmhst
     1441 ssheghkqhr sqtlpiirgk nalsnpkllq mldntmtsns neidivhhvd teaniatevc
     1501 ltildllslf tqthqrqlqq cdcqnslmkr vfdtymlffq vnqsatalkh vfaslrlfvc
     1561 kfpsaffqgp adlcgsfcye vlkccnhrsr stqteasall yffmrknfef nkqksivrsh
     1621 lqlikavsql iadagiggsr fqhslaitnn fangdkqmkn snfpaevkdl tkrirtvlma
     1681 taqmkehekd pemlvdlqys lansyastpe lrrtwlesma kiharngdls eaamcyihia
     1741 aliaeylkrk gywkvekict asllsedthp cdsnsllttp sggsmfsmgw paflsitpni
     1801 keegamkeds gmqdtpynen ilveqlymcv eflwkserye liadvnkpii avfekqrdfk
     1861 klsdlyydih rsylkvaevv nsekrlfgry yrvafygqgf feeeegkeyi ykepkltgls
     1921 eisqrllkly adkfgadnvk iiqdsnkvnp kdldpkyayi qvtyvtpffe ekeiedrktd
     1981 femhhninrf vfetpftlsg kkhggvaeqc krrtilttsh lfpyvkkriq visqssteln
     2041 pievaidems kkvselnqlc tmeevdmirl qlklqgsvsv kvnagpmaya rafleetnak
     2101 kypdnqvkll keifrqfada cgqaldvner likedqleyq eelrshykdm lselstvmne
     2161 qitgrddlsk rgvdqtctrv iskatpalpt vsisssaev
//
LOCUS       NP_005547                469 aa            linear   PRI 27-APR-2025
DEFINITION  keratin, type II cytoskeletal 7 [Homo sapiens].
ACCESSION   NP_005547
VERSION     NP_005547.3
DBSOURCE    REFSEQ: accession NM_005556.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Ismael,A.T., Abdulhameed,R.A., Jalal,J.A., Tawfeeq,R.D., Ommar,A.
            and Jalal,A.
  TITLE     Expression of cytokeratin 7/20 and Ki67 in Helicobacter
            pylori-associated gastritis and intestinal metaplasia
  JOURNAL   J Infect Dev Ctries 18 (7), 1032-1040 (2024)
   PUBMED   39078783
  REMARK    GeneRIF: Expression of cytokeratin 7/20 and Ki67 in Helicobacter
            pylori-associated gastritis and intestinal metaplasia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Wang,S., Li,H., Li,M., Liu,X., Yu,S., Huang,H. and Wang,X.
  TITLE     Role of the KRT7 Biomarker in Immune Infiltration and Paclitaxel
            Resistance in Ovarian
  JOURNAL   Altern Ther Health Med 29 (5), 132-140 (2023)
   PUBMED   37023314
  REMARK    GeneRIF: Role of the KRT7 Biomarker in Immune Infiltration and
            Paclitaxel Resistance in Ovarian.
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Polari,L., Tenhami,M., Anttila,S., Helenius,T., Kujari,H.,
            Kallajoki,M., Voutilainen,M. and Toivola,D.M.
  TITLE     Colonocyte keratin 7 is expressed de novo in inflammatory bowel
            diseases and associated with pathological changes and
            drug-resistance
  JOURNAL   Sci Rep 12 (1), 22213 (2022)
   PUBMED   36564440
  REMARK    GeneRIF: Colonocyte keratin 7 is expressed de novo in inflammatory
            bowel diseases and associated with pathological changes and
            drug-resistance.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Liu,H.L., Yang,A.Y., Xiong,Q.F., Zhong,Y.D., Liu,D.X., Huang,P.,
            Feng,X.N., Zhang,Y. and Yang,Y.F.
  TITLE     Aberrant cytokeratin 7 expression by hepatocytes can predict the
            ductopenia grade in primary biliary cholangitis
  JOURNAL   BMC Gastroenterol 22 (1), 443 (2022)
   PUBMED   36324070
  REMARK    GeneRIF: Aberrant cytokeratin 7 expression by hepatocytes can
            predict the ductopenia grade in primary biliary cholangitis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Yu,Z., Ding,J., Pang,H., Fang,H., He,F., Xu,C., Li,X. and Ren,K.
  TITLE     A triple-classification for differentiating renal oncocytoma from
            renal cell carcinoma subtypes and CK7 expression evaluation: a
            radiomics analysis
  JOURNAL   BMC Urol 22 (1), 147 (2022)
   PUBMED   36096829
  REMARK    GeneRIF: A triple-classification for differentiating renal
            oncocytoma from renal cell carcinoma subtypes and CK7 expression
            evaluation: a radiomics analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 469)
  AUTHORS   Gress,T.M., Muller-Pillasch,F., Geng,M., Zimmerhackl,F.,
            Zehetner,G., Friess,H., Buchler,M., Adler,G. and Lehrach,H.
  TITLE     A pancreatic cancer-specific expression profile
  JOURNAL   Oncogene 13 (8), 1819-1830 (1996)
   PUBMED   8895530
REFERENCE   7  (residues 1 to 469)
  AUTHORS   Rosenberg,M., Fuchs,E., Le Beau,M.M., Eddy,R.L. and Shows,T.B.
  TITLE     Three epidermal and one simple epithelial type II keratin genes map
            to human chromosome 12
  JOURNAL   Cytogenet Cell Genet 57 (1), 33-38 (1991)
   PUBMED   1713141
REFERENCE   8  (residues 1 to 469)
  AUTHORS   Glass,C. and Fuchs,E.
  TITLE     Isolation, sequence, and differential expression of a human K7 gene
            in simple epithelial cells
  JOURNAL   J Cell Biol 107 (4), 1337-1350 (1988)
   PUBMED   2459129
REFERENCE   9  (residues 1 to 469)
  AUTHORS   Ramaekers,F., Huysmans,A., Schaart,G., Moesker,O. and Vooijs,P.
  TITLE     Tissue distribution of keratin 7 as monitored by a monoclonal
            antibody
  JOURNAL   Exp Cell Res 170 (1), 235-249 (1987)
   PUBMED   2436934
REFERENCE   10 (residues 1 to 469)
  AUTHORS   Glass,C., Kim,K.H. and Fuchs,E.
  TITLE     Sequence and expression of a human type II mesothelial keratin
  JOURNAL   J Cell Biol 101 (6), 2366-2373 (1985)
   PUBMED   2415537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Michael Rogers. The reference sequence was
            derived from AC021066.37, BE744321.1, BE740515.1 and BC002700.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 15, 2005 this sequence version replaced NP_005547.2.
            
            Summary: The protein encoded by this gene is a member of the
            keratin gene family. The type II cytokeratins consist of basic or
            neutral proteins which are arranged in pairs of heterotypic keratin
            chains coexpressed during differentiation of simple and stratified
            epithelial tissues. This type II cytokeratin is specifically
            expressed in the simple epithelia lining the cavities of the
            internal organs and in the gland ducts and blood vessels. The genes
            encoding the type II cytokeratins are clustered in a region of
            chromosome 12q12-q13. Alternative splicing may result in several
            transcript variants; however, not all variants have been fully
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK025881.1, BC002700.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331817.6/ ENSP00000329243.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..469
                     /product="keratin, type II cytoskeletal 7"
                     /note="cytokeratin 7; sarcolectin; keratin, 55K type II
                     cytoskeletal; type II mesothelial keratin K7; keratin,
                     simple epithelial type I, K7; CK-7; type-II keratin Kb7;
                     keratin 7, type II"
                     /calculated_mol_wt=51255
     Region          2..90
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P08729.5)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.7;
                     propagated from UniProtKB/Swiss-Prot (P08729.5)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Site            12
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:26237509; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Region          <18..87
                     /region_name="Keratin_2_head"
                     /note="Keratin type II head; pfam16208"
                     /db_xref="CDD:465068"
     Site            20
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|Ref.7; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0000269|Ref.7; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Region          90..402
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          90..126
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P08729.5)"
     Region          92..97
                     /region_name="Interaction with HPV16 E7.
                     /evidence=ECO:0000269|PubMed:12072504"
                     /note="propagated from UniProtKB/Swiss-Prot (P08729.5)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Region          127..144
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P08729.5)"
     Region          145..236
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P08729.5)"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Region          237..260
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P08729.5)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Region          261..399
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P08729.5)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08729.5)"
     Site            343
                     /site_type="other"
                     /note="Stutter; propagated from UniProtKB/Swiss-Prot
                     (P08729.5)"
     Region          400..469
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P08729.5)"
     CDS             1..469
                     /gene="KRT7"
                     /gene_synonym="CK7; K2C7; K7; SCL"
                     /coded_by="NM_005556.4:55..1464"
                     /db_xref="CCDS:CCDS8822.1"
                     /db_xref="GeneID:3855"
                     /db_xref="HGNC:HGNC:6445"
                     /db_xref="MIM:148059"
ORIGIN      
        1 msihfsspvf tsrsaafsgr gaqvrlssar pgglgsssly glgasrprva vrsayggpvg
       61 agirevtinq sllaplrlda dpslqrvrqe eseqiktlnn kfasfidkvr fleqqnklle
      121 tkwtllqeqk sakssrlpdi feaqiaglrg qlealqvdgg rleaelrsmq dvvedfknky
      181 edeinhrtaa enefvvlkkd vdaaymskve leakvdalnd einflrtlne teltelqsqi
      241 sdtsvvlsmd nsrsldldgi iaevkaqyee makcsraeae awyqtkfetl qaqagkhgdd
      301 lrntrneise mnraiqrlqa eidniknqra kleaaiaeae ergelalkda rakqeeleaa
      361 lqrgkqdmar qlreyqelms vklaldieia tyrkllegee srlagdgvga vnisvmnstg
      421 gsssgggigl tlggtmgsna lsfsssagpg llkaysirta sasrrsard
//
LOCUS       NP_954713                434 aa            linear   PRI 27-APR-2025
DEFINITION  probable G-protein coupled receptor 150 [Homo sapiens].
ACCESSION   NP_954713 XP_209675
VERSION     NP_954713.1
DBSOURCE    REFSEQ: accession NM_199243.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Martin,A.L., Steurer,M.A. and Aronstam,R.S.
  TITLE     Constitutive Activity among Orphan Class-A G Protein Coupled
            Receptors
  JOURNAL   PLoS One 10 (9), e0138463 (2015)
   PUBMED   26384023
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Kakarala,K.K. and Jamil,K.
  TITLE     Sequence-structure based phylogeny of GPCR Class A Rhodopsin
            receptors
  JOURNAL   Mol Phylogenet Evol 74, 66-96 (2014)
   PUBMED   24503482
  REMARK    Erratum:[Mol Phylogenet Evol. 2014 Jul;76:293-7]
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Cai,L.Y., Abe,M., Izumi,S., Imura,M., Yasugi,T. and Ushijima,T.
  TITLE     Identification of PRTFDC1 silencing and aberrant promoter
            methylation of GPR150, ITGA8 and HOXD11 in ovarian cancers
  JOURNAL   Life Sci 80 (16), 1458-1465 (2007)
   PUBMED   17303177
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Gloriam,D.E., Schioth,H.B. and Fredriksson,R.
  TITLE     Nine new human Rhodopsin family G-protein coupled receptors:
            identification, sequence characterisation and evolutionary
            relationship
  JOURNAL   Biochim Biophys Acta 1722 (3), 235-246 (2005)
   PUBMED   15777626
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Vassilatis,D.K., Hohmann,J.G., Zeng,H., Li,F., Ranchalis,J.E.,
            Mortrud,M.T., Brown,A., Rodriguez,S.S., Weller,J.R., Wright,A.C.,
            Bergmann,J.E. and Gaitanaris,G.A.
  TITLE     The G protein-coupled receptor repertoires of human and mouse
  JOURNAL   Proc Natl Acad Sci U S A 100 (8), 4903-4908 (2003)
   PUBMED   12679517
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC030197.1, BK005422.1,
            AC008547.6 and CR744504.1.
            
            On Jan 1, 2004 this sequence version replaced XP_209675.2.
            
            Summary: This gene encodes an orphan member of the class A
            rhodopsin-like family of G-protein-coupled receptors (GPCRs).
            Within the rhodopsin-like family, this gene is a member of the
            vasopressin-like subfamily that also includes vasopressin and
            oxytocin receptors. The silencing of this gene, due to promoter
            methylation, is associated with ovarian cancer progression. All
            GPCRs have a transmembrane domain that includes seven transmembrane
            alpha-helices. A general feature of GPCR signaling is the
            agonist-induced conformational change in the receptor, leading to
            activation of the heterotrimeric G protein. The activated G protein
            then binds to and activates numerous downstream effector proteins,
            which generate second messengers that mediate a broad range of
            cellular and physiological processes. [provided by RefSeq, Jul
            2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BK005422.1, JF810884.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380007.3/ ENSP00000369344.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q15"
     Protein         1..434
                     /product="probable G-protein coupled receptor 150"
                     /note="seven transmembrane helix receptor"
                     /calculated_mol_wt=46222
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGU9.1)"
     Region          43..360
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGU9.1)"
     Region          45..69
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGU9.1)"
     Region          83..106
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          123..145
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            163..183
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGU9.1)"
     Region          163..179
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          188..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGU9.1)"
     Region          230..253
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGU9.1)"
     Region          294..316
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            294..314
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGU9.1)"
     Region          331..356
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            335..355
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGU9.1)"
     Region          398..434
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGU9.1)"
     CDS             1..434
                     /gene="GPR150"
                     /gene_synonym="PGR11"
                     /coded_by="NM_199243.3:190..1494"
                     /db_xref="CCDS:CCDS4074.1"
                     /db_xref="GeneID:285601"
                     /db_xref="HGNC:HGNC:23628"
ORIGIN      
        1 medlfspsil ppapnisvpi llgwglnltl gqgapasgpp srrvrlvflg vilvvavagn
       61 ttvlcrlcgg ggpwagpkrr kmdfllvqla ladlyacggt alsqlawell gepraatgdl
      121 acrflqllqa sgrgasahlv vlialerrra vrlphgrplp aralaalgwl lalllalppa
      181 fvvrgdspsp lpppppptsl qpgappaara wpgerrchgi faplprwhlq vyafyeavag
      241 fvapvtvlgv acghllsvww rhrpqapaaa apwsaspgra papsalprak vqslkmslll
      301 allfvgcelp yfaarlaaaw ssgpagdweg eglsaalrvv amansalnpf vylffqagdc
      361 rlrrqlrkrl gslccapqgg aedeegprgh qalyrqrwph phyhharrep ldegglrppp
      421 prprplpcsc esaf
//
LOCUS       NP_004646                843 aa            linear   PRI 27-APR-2025
DEFINITION  axin-2 isoform 1 [Homo sapiens].
ACCESSION   NP_004646
VERSION     NP_004646.3
DBSOURCE    REFSEQ: accession NM_004655.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Alhazmi,N., Alaqla,A., Almuzzaini,B., Aldrees,M., Alnaqa,G.,
            Almasoud,F., Aldibasi,O. and Alshamlan,H.
  TITLE     What could be the role of genetic tests and machine learning of
            AXIN2 variant dominance in non-syndromic hypodontia? A case-control
            study in orthodontically treated patients
  JOURNAL   Prog Orthod 25 (1), 31 (2024)
   PUBMED   39183201
  REMARK    GeneRIF: What could be the role of genetic tests and machine
            learning of AXIN2 variant dominance in non-syndromic hypodontia? A
            case-control study in orthodontically treated patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Zheng,Y., Wang,Y., Qi,B., Gao,W., Liu,Y. and Li,T.
  TITLE     Axin2 depletion in macrophages alleviated senescence and increased
            immune response after myocardial infarction
  JOURNAL   Inflamm Res 73 (3), 407-414 (2024)
   PUBMED   38158447
  REMARK    GeneRIF: Axin2 depletion in macrophages alleviated senescence and
            increased immune response after myocardial infarction.
REFERENCE   3  (residues 1 to 843)
  AUTHORS   Cao,W., Dai,S., Ruan,W., Long,T., Zeng,Z. and Lei,S.
  TITLE     Pancreatic stellate cell-derived exosomal tRF-19-PNR8YPJZ promotes
            proliferation and mobility of pancreatic cancer through AXIN2
  JOURNAL   J Cell Mol Med 27 (17), 2533-2546 (2023)
   PUBMED   37488774
  REMARK    GeneRIF: Pancreatic stellate cell-derived exosomal tRF-19-PNR8YPJZ
            promotes proliferation and mobility of pancreatic cancer through
            AXIN2.
REFERENCE   4  (residues 1 to 843)
  AUTHORS   Zhai,J., Chen,H., Wong,C.C., Peng,Y., Gou,H., Zhang,J., Pan,Y.,
            Chen,D., Lin,Y., Wang,S., Kang,W., To,K.F., Chen,Z., Nie,Y.,
            He,H.H., Sung,J.J. and Yu,J.
  TITLE     ALKBH5 Drives Immune Suppression Via Targeting AXIN2 to Promote
            Colorectal Cancer and Is a Target for Boosting Immunotherapy
  JOURNAL   Gastroenterology 165 (2), 445-462 (2023)
   PUBMED   37169182
  REMARK    GeneRIF: ALKBH5 Drives Immune Suppression Via Targeting AXIN2 to
            Promote Colorectal Cancer and Is a Target for Boosting
            Immunotherapy.
REFERENCE   5  (residues 1 to 843)
  AUTHORS   Wang,L., Guo,M., Gao,L., Liu,K., Bai,J. and Liu,Z.
  TITLE     JNK2 Promotes Progression of Esophageal Squamous Cell Carcinoma via
            Inhibiting Axin2
  JOURNAL   Curr Pharm Des 29 (37), 2977-2987 (2023)
   PUBMED   37957865
  REMARK    GeneRIF: JNK2 Promotes Progression of Esophageal Squamous Cell
            Carcinoma via Inhibiting Axin2.
REFERENCE   6  (residues 1 to 843)
  AUTHORS   von Kries,J.P., Winbeck,G., Asbrand,C., Schwarz-Romond,T.,
            Sochnikova,N., Dell'Oro,A., Behrens,J. and Birchmeier,W.
  TITLE     Hot spots in beta-catenin for interactions with LEF-1, conductin
            and APC
  JOURNAL   Nat Struct Biol 7 (9), 800-807 (2000)
   PUBMED   10966653
REFERENCE   7  (residues 1 to 843)
  AUTHORS   Ikeda,S., Kishida,M., Matsuura,Y., Usui,H. and Kikuchi,A.
  TITLE     GSK-3beta-dependent phosphorylation of adenomatous polyposis coli
            gene product can be modulated by beta-catenin and protein
            phosphatase 2A complexed with Axin
  JOURNAL   Oncogene 19 (4), 537-545 (2000)
   PUBMED   10698523
REFERENCE   8  (residues 1 to 843)
  AUTHORS   Kikuchi,A.
  TITLE     Modulation of Wnt signaling by Axin and Axil
  JOURNAL   Cytokine Growth Factor Rev 10 (3-4), 255-265 (1999)
   PUBMED   10647780
  REMARK    Review article
REFERENCE   9  (residues 1 to 843)
  AUTHORS   Mai,M., Qian,C., Yokomizo,A., Smith,D.I. and Liu,W.
  TITLE     Cloning of the human homolog of conductin (AXIN2), a gene mapping
            to chromosome 17q23-q24
  JOURNAL   Genomics 55 (3), 341-344 (1999)
   PUBMED   10049590
REFERENCE   10 (residues 1 to 843)
  AUTHORS   Hart,M.J., de los Santos,R., Albert,I.N., Rubinfeld,B. and
            Polakis,P.
  TITLE     Downregulation of beta-catenin by human Axin and its association
            with the APC tumor suppressor, beta-catenin and GSK3 beta
  JOURNAL   Curr Biol 8 (10), 573-581 (1998)
   PUBMED   9601641
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA754981.1, DA785881.1,
            BC101533.1, DA839648.1, CX759580.1, CX756263.1 and BE670767.1.
            
            On Aug 6, 2008 this sequence version replaced NP_004646.2.
            
            Summary: The Axin-related protein, Axin2, presumably plays an
            important role in the regulation of the stability of beta-catenin
            in the Wnt signaling pathway, like its rodent homologs, mouse
            conductin/rat axil. In mouse, conductin organizes a multiprotein
            complex of APC (adenomatous polyposis of the colon), beta-catenin,
            glycogen synthase kinase 3-beta, and conductin, which leads to the
            degradation of beta-catenin. Apparently, the deregulation of
            beta-catenin is an important event in the genesis of a number of
            malignancies. The AXIN2 gene has been mapped to 17q23-q24, a region
            that shows frequent loss of heterozygosity in breast cancer,
            neuroblastoma, and other tumors. Mutations in this gene have been
            associated with colorectal cancer with defective mismatch repair.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR933657.1, SRR11853561.13223.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307078.10/ ENSP00000302625.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.1"
     Protein         1..843
                     /product="axin-2 isoform 1"
                     /note="conductin; axin-like protein; axis inhibition
                     protein 2"
                     /calculated_mol_wt=93437
     Region          1..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T1.2)"
     Region          10..75
                     /region_name="AXIN1_TNKS_BD"
                     /note="Axin-1 tankyrase binding domain; pfam16646"
                     /db_xref="CDD:465215"
     Region          21..30
                     /region_name="Tankyrase-binding motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T1.2)"
     Region          82..198
                     /region_name="RGS_Axin"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the Axin protein; cd08707"
                     /db_xref="CDD:188662"
     Site            order(86..89,92,109,112..113,116..117,119,129..130,
                     132..134,136..137)
                     /site_type="other"
                     /note="APC binding site [polypeptide binding]"
                     /db_xref="CDD:188662"
     Region          327..413
                     /region_name="Interaction with GSK3B.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T1.2)"
     Region          334..393
                     /region_name="Interaction with SIAH1 and SIAH2.
                     /evidence=ECO:0000269|PubMed:28546513"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T1.2)"
     Region          396..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T1.2)"
     Region          413..476
                     /region_name="Interaction with beta-catenin.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T1.2)"
     Region          433..468
                     /region_name="Axin_b-cat_bind"
                     /note="Axin beta-catenin binding motif; pfam08833"
                     /db_xref="CDD:462616"
     Region          447..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T1.2)"
     Region          561..674
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T1.2)"
     Region          718..748
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T1.2)"
     Region          761..843
                     /region_name="DAX"
                     /note="Domain present in Dishevelled and axin; smart00021"
                     /db_xref="CDD:197474"
     CDS             1..843
                     /gene="AXIN2"
                     /gene_synonym="AXIL; ODCRCS"
                     /coded_by="NM_004655.4:316..2847"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11662.1"
                     /db_xref="GeneID:8313"
                     /db_xref="HGNC:HGNC:904"
                     /db_xref="MIM:604025"
ORIGIN      
        1 mssamlvtcl pdpsssfred aprppvpgee getppcqpgv gkgqvtkpmp vssntrrned
       61 glgepegras pdspltrwtk slhsllgdqd gaylfrtfle rekcvdtldf wfacngfrqm
      121 nlkdtktlrv akaiykryie nnsivskqlk patktyirdg ikkqqidsim fdqaqteiqs
      181 vmeenayqmf ltsdiyleyv rsggentaym sngglgslkv vcgylptlne eeewtcadfk
      241 cklsptvvgl ssktlratas vrstetvdsg yrsfkrsdpv npyhigsgyv fapatsands
      301 eissdaltdd smsmtdssvd gippyrvgsk kqlqremhrs vkangqvslp hfprthrlpk
      361 emtpvepatf aaelisrlek lklelesrhs leerlqqire deeregselt lnsregaptq
      421 hplsllpsgs yeedpqtild dhlsrvlktp gcqspgvgry sprsrspdhh hhhhsqyhsl
      481 lppggklppa aaspgacpll ggkgfvtkqt tkhvhhhyih hhavpktkee ieaeatqrvh
      541 cfcpggseyy cyskckshsk apetmpseqf ggsrgstlpk rngkgtepgl alpareggap
      601 ggagalqlpr eegdrsqdvw qwmleserqs kpkphsaqst kkayplesar sspgerasrh
      661 hlwggnsghp rttprahlft qdpamppltp pntlaqleea crrlaevskp pkqrccvasq
      721 qrdrnhsatv qtgatpfsnp slapedhkep kklagvhalq aselvvtyff cgeeipyrrm
      781 lkaqsltlgh fkeqlskkgn yryyfkkasd efacgavfee iwedetvlpm yegrilgkve
      841 rid
//
LOCUS       NP_001350696             215 aa            linear   PRI 27-APR-2025
DEFINITION  doublesex- and mab-3-related transcription factor 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001350696 XP_024303201
VERSION     NP_001350696.1
DBSOURCE    REFSEQ: accession NM_001363767.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Ishikawa,N., Fujitani,K., Okano,N., Hayashi,S., Sakabe,N.,
            Inazumi,S., Okuyama,H., Seki,K., Suda,K., Tsukamoto,D., Matsuo,T.,
            Tamura,K. and Ito,M.
  TITLE     Diversity of transactivation regions of DMRT1 in vertebrates
  JOURNAL   Mol Biol Rep 51 (1), 1077 (2024)
   PUBMED   39432160
  REMARK    GeneRIF: Diversity of transactivation regions of DMRT1 in
            vertebrates.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Irie,N., Lee,S.M., Lorenzi,V., Xu,H., Chen,J., Inoue,M.,
            Kobayashi,T., Sancho-Serra,C., Drousioti,E., Dietmann,S.,
            Vento-Tormo,R., Song,C.X. and Surani,M.A.
  TITLE     DMRT1 regulates human germline commitment
  JOURNAL   Nat Cell Biol 25 (10), 1439-1452 (2023)
   PUBMED   37709822
  REMARK    GeneRIF: DMRT1 regulates human germline commitment.
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Emich,J., Gaikwad,A.S., Stallmeyer,B., Fietz,D., Schuppe,H.C.,
            Oud,M.S., Kliesch,S., Gromoll,J., Friedrich,C. and Tuttelmann,F.
  TITLE     Functional assessment of DMRT1 variants and their pathogenicity for
            isolated male infertility
  JOURNAL   Fertil Steril 119 (2), 219-228 (2023)
   PUBMED   36572623
  REMARK    GeneRIF: Functional assessment of DMRT1 variants and their
            pathogenicity for isolated male infertility.
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Roth,L.M., Michal,M., Michal,M. Jr. and Cheng,L.
  TITLE     Protein expression of the transcription factors DMRT1, TCLF5, and
            OCT4 in selected germ cell neoplasms of the testis
  JOURNAL   Hum Pathol 82, 68-75 (2018)
   PUBMED   30067948
  REMARK    GeneRIF: Report differential expression of DMRT1 in normal human
            spermatogenesis, testicular mixed germ cell-sex cord stromal tumor,
            spermatocytic tumor, and seminoma.
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Macdonald,J., Kilcoyne,K.R., Sharpe,R.M., Kavanagh,A.,
            Anderson,R.A., Brown,P., Smith,L.B., Jorgensen,A. and Mitchell,R.T.
  TITLE     DMRT1 repression using a novel approach to genetic manipulation
            induces testicular dysgenesis in human fetal gonads
  JOURNAL   Hum Reprod 33 (11), 2107-2121 (2018)
   PUBMED   30272154
  REMARK    GeneRIF: DMRT1 is required for testicular differentiation in
            humans. DMRT1 repression results in alterations in expression of
            key genes involved in gonadal development.  Repression of DMRT1
            results in focal dysgenesis in the human fetal testis
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Calvari,V., Bertini,V., De Grandi,A., Peverali,G., Zuffardi,O.,
            Ferguson-Smith,M., Knudtzon,J., Camerino,G., Borsani,G. and
            Guioli,S.
  TITLE     A new submicroscopic deletion that refines the 9p region for sex
            reversal
  JOURNAL   Genomics 65 (3), 203-212 (2000)
   PUBMED   10857744
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Smith,C.A., McClive,P.J., Western,P.S., Reed,K.J. and Sinclair,A.H.
  TITLE     Conservation of a sex-determining gene
  JOURNAL   Nature 402 (6762), 601-602 (1999)
   PUBMED   10604464
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Raymond,C.S., Parker,E.D., Kettlewell,J.R., Brown,L.G., Page,D.C.,
            Kusz,K., Jaruzelska,J., Reinberg,Y., Flejter,W.L., Bardwell,V.J.,
            Hirsch,B. and Zarkower,D.
  TITLE     A region of human chromosome 9p required for testis development
            contains two genes related to known sexual regulators
  JOURNAL   Hum Mol Genet 8 (6), 989-996 (1999)
   PUBMED   10332030
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Raymond,C.S., Shamu,C.E., Shen,M.M., Seifert,K.J., Hirsch,B.,
            Hodgkin,J. and Zarkower,D.
  TITLE     Evidence for evolutionary conservation of sex-determining genes
  JOURNAL   Nature 391 (6668), 691-695 (1998)
   PUBMED   9490411
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Mohnach,L., Fechner,P.Y. and Keegan,C.E.
  TITLE     Nonsyndromic Disorders of Testicular Development Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301714
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136365.9.
            
            On May 30, 2018 this sequence version replaced XP_024303201.1.
            
            Summary: This gene is found in a cluster with two other members of
            the gene family, having in common a zinc finger-like DNA-binding
            motif (DM domain). The DM domain is an ancient, conserved component
            of the vertebrate sex-determining pathway that is also a key
            regulator of male development in flies and nematodes. This gene
            exhibits a gonad-specific and sexually dimorphic expression
            pattern. Defective testicular development and XY feminization occur
            when this gene is hemizygous. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.256168.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.3"
     Protein         1..215
                     /product="doublesex- and mab-3-related transcription
                     factor 1 isoform 2"
                     /note="DM domain expressed in testis 1; DM domain
                     expressed in testis protein 1"
                     /calculated_mol_wt=23043
     Region          <1..44
                     /region_name="Dmrt1"
                     /note="Double-sex mab3 related transcription factor 1;
                     pfam12374"
                     /db_xref="CDD:463555"
     CDS             1..215
                     /gene="DMRT1"
                     /gene_synonym="CT154; DMT1"
                     /coded_by="NM_001363767.1:388..1035"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS87636.1"
                     /db_xref="GeneID:1761"
                     /db_xref="HGNC:HGNC:2934"
                     /db_xref="MIM:602424"
ORIGIN      
        1 mtecsgtsqp ppasvpttaa segrmviqdi pavtsrghve ntpdlvsdst yyssfyqpsl
       61 fpyynnlync pqysmalaad sasgevgnpl ggspvknslr glpgpyvpgq tgnqwqmknm
      121 enrhamssqy rmhsyyppps ylgqsvpqff tfedapsype arasvfspps sqdsglvsls
      181 ssspisnkst kavlecepas epssftvtpv ieede
//
LOCUS       NP_037015                295 aa            linear   ROD 27-APR-2025
DEFINITION  sulfotransferase 1E1 [Rattus norvegicus].
ACCESSION   NP_037015 NP_001007719 XP_001081145 XP_346462
VERSION     NP_037015.2
DBSOURCE    REFSEQ: accession NM_012883.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Ihunnah,C.A., Wada,T., Philips,B.J., Ravuri,S.K., Gibbs,R.B.,
            Kirisci,L., Rubin,J.P., Marra,K.G. and Xie,W.
  TITLE     Estrogen sulfotransferase/SULT1E1 promotes human adipogenesis
  JOURNAL   Mol Cell Biol 34 (9), 1682-1694 (2014)
   PUBMED   24567372
REFERENCE   2  (residues 1 to 295)
  AUTHORS   McGill,M.R. and Jaeschke,H.
  TITLE     Metabolism and disposition of acetaminophen: recent advances in
            relation to hepatotoxicity and diagnosis
  JOURNAL   Pharm Res 30 (9), 2174-2187 (2013)
   PUBMED   23462933
  REMARK    Review article
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Kurogi,K., Davidson,G., Mohammed,Y.I., Williams,F.E., Liu,M.Y.,
            Sakakibara,Y., Suiko,M. and Liu,M.C.
  TITLE     Ethanol sulfation by the human cytosolic sulfotransferases: a
            systematic analysis
  JOURNAL   Biol Pharm Bull 35 (12), 2180-2185 (2012)
   PUBMED   23207770
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Purohit,A., Woo,L.W. and Potter,B.V.
  TITLE     Steroid sulfatase: a pivotal player in estrogen synthesis and
            metabolism
  JOURNAL   Mol Cell Endocrinol 340 (2), 154-160 (2011)
   PUBMED   21693170
  REMARK    Review article
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Brand,W., Boersma,M.G., Bik,H., Hoek-van den Hil,E.F., Vervoort,J.,
            Barron,D., Meinl,W., Glatt,H., Williamson,G., van Bladeren,P.J. and
            Rietjens,I.M.
  TITLE     Phase II metabolism of hesperetin by individual
            UDP-glucuronosyltransferases and sulfotransferases and rat and
            human tissue samples
  JOURNAL   Drug Metab Dispos 38 (4), 617-625 (2010)
   PUBMED   20056724
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Song,W.C., Qian,Y., Sun,X. and Negishi,M.
  TITLE     Cellular localization and regulation of expression of testicular
            estrogen sulfotransferase
  JOURNAL   Endocrinology 138 (11), 5006-5012 (1997)
   PUBMED   9348232
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Rikke,B.A. and Roy,A.K.
  TITLE     Structural relationships among members of the mammalian
            sulfotransferase gene family
  JOURNAL   Biochim Biophys Acta 1307 (3), 331-338 (1996)
   PUBMED   8688469
REFERENCE   8  (residues 1 to 295)
  AUTHORS   Falany,J.L., Krasnykh,V., Mikheeva,G. and Falany,C.N.
  TITLE     Isolation and expression of an isoform of rat estrogen
            sulfotransferase
  JOURNAL   J Steroid Biochem Mol Biol 52 (1), 35-44 (1995)
   PUBMED   7857871
REFERENCE   9  (residues 1 to 295)
  AUTHORS   Demyan,W.F., Song,C.S., Kim,D.S., Her,S., Gallwitz,W., Rao,T.R.,
            Slomczynska,M., Chatterjee,B. and Roy,A.K.
  TITLE     Estrogen sulfotransferase of the rat liver: complementary DNA
            cloning and age- and sex-specific regulation of messenger RNA
  JOURNAL   Mol Endocrinol 6 (4), 589-597 (1992)
   PUBMED   1374839
REFERENCE   10 (residues 1 to 295)
  AUTHORS   Bajoriniene,D., Balkevicius,B., Rockiene,A. and Dautartiene,A.
  TITLE     Trichinellosis in Lithuania (1978-1987)
  JOURNAL   Wiad Parazytol 38 (3-4), 151-152 (1992)
   PUBMED   1299062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Sep 13, 2018 this sequence version replaced NP_037015.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088157.1, M86758.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..295
                     /product="sulfotransferase 1E1"
                     /EC_number="2.8.2.4"
                     /note="estrone sulfotransferase; sulfotransferase,
                     estrogen-preferring; sulfotransferase family 1E,
                     estrogen-preferring, member 1; estrogen sulfotransferase"
                     /calculated_mol_wt=35231
     Region          38..288
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; pfam00685"
                     /db_xref="CDD:425820"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P52844.2)"
     CDS             1..295
                     /gene="Sult1e1"
                     /gene_synonym="EST-1; EST-2; EST-3; EST-6; ESTSUL; rEST-6;
                     ST1E1; Ste; Ste1; ste2"
                     /coded_by="NM_012883.2:116..1003"
                     /db_xref="GeneID:360268"
                     /db_xref="RGD:3776"
ORIGIN      
        1 metsmpeyye vfgdfhgvlm dklftkywed vetfsarpdd llvvtypksg stwigeivdm
       61 iykegdvekc kedaifnrip ylecrnedli ngikqlkeke sprivkthlp akllpasfwe
      121 knckiiylcr nakdvvvsyy yffliiksyp npksfsefve kfmegqvpyg swydhvksww
      181 eksknsrvlf mfyedmkedi rrevvklief lerdplaelv dkiiqhtsfq emknnpctny
      241 smlpetmidl kvspfmrkgi vgdwrnhfpe alrerfeehy qrhmkdcpvk frael
//
LOCUS       NP_001123363             535 aa            linear   PRI 27-APR-2025
DEFINITION  protein INSYN2B [Homo sapiens].
ACCESSION   NP_001123363 XP_001719762
VERSION     NP_001123363.1
DBSOURCE    REFSEQ: accession NM_001129891.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK055998.1, AC008449.6 and AI889725.1.
            
            On Jul 3, 2008 this sequence version replaced XP_001719762.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants, 1 and 2, encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.2132.1,
                                           SRR1660809.127468.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377365.4/ ENSP00000366582.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.1"
     Protein         1..535
                     /product="protein INSYN2B"
                     /note="protein FAM196B; family with sequence similarity
                     196 member B"
                     /calculated_mol_wt=59073
     Region          3..535
                     /region_name="FAM196"
                     /note="FAM196 family; pfam15265"
                     /db_xref="CDD:464603"
     Region          24..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NMK8.1)"
     Region          215..388
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NMK8.1)"
     Region          492..529
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NMK8.1)"
     CDS             1..535
                     /gene="INSYN2B"
                     /gene_synonym="C5orf57; FAM196B"
                     /coded_by="NM_001129891.3:1138..2745"
                     /db_xref="CCDS:CCDS47336.1"
                     /db_xref="GeneID:100131897"
                     /db_xref="HGNC:HGNC:37271"
ORIGIN      
        1 maqqnmkvrp vllkrnsles vefvkqphhr rsksqqvrfk edgttknptg laevdvqtpe
       61 dpavmgktqa trhhlpptys lsfprsqkag gfrniaiqts pslrkhfpvf krkrltasks
      121 lvemptasqs aiqvngnlse qdivssdlay lrlaqhledg prrvkvshaf lprvpkvqsn
      181 gpvsicleag twrslekata aiqvpddiyh spswearesa lspdrsaevs nsihplddtr
      241 pgdgrrvtpl dsekstscln atsvashtpg teelkpelll pkdnsddkdl gslssqsket
      301 cvpssprths spsqgshsqp ahpgrasdcp sssnnhqnlv slktnsasks apgcqeqtan
      361 nptesdtlef pncpgsnhlp sslsrsetkl qsnreisdin qihlargelc dlqgrlqsve
      421 eslhsnqeki kvllnviqdl ekaraltegr nfyrtgqdln ncstcqntac iiysveydfr
      481 qqegrfhevl qsleeaepve easpppkspa eppapekqdl rrktkkvkkk cfwwi
//
LOCUS       NP_083209                285 aa            linear   ROD 27-APR-2025
DEFINITION  reticulophagy regulator 3 isoform 2 [Mus musculus].
ACCESSION   NP_083209
VERSION     NP_083209.1
DBSOURCE    REFSEQ: accession NM_028933.4
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Iavarone,F., Zaninello,M., Perrone,M., Monaco,M., Barth,E.,
            Gaedke,F., Pizzo,M.T., Di Lorenzo,G., Desiderio,V., Sommella,E.,
            Merciai,F., Salviati,E., Campiglia,P., Luongo,L., De Leonibus,E.,
            Rugarli,E. and Settembre,C.
  TITLE     Fam134c and Fam134b shape axonal endoplasmic reticulum architecture
            in vivo
  JOURNAL   EMBO Rep 25 (8), 3651-3677 (2024)
   PUBMED   39039299
  REMARK    GeneRIF: Fam134c and Fam134b shape axonal endoplasmic reticulum
            architecture in vivo.
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Di Lorenzo,G., Iavarone,F., Maddaluno,M., Plata-Gomez,A.B.,
            Aureli,S., Quezada Meza,C.P., Cinque,L., Palma,A., Reggio,A.,
            Cirillo,C., Sacco,F., Stolz,A., Napolitano,G., Marin,O.,
            Pinna,L.A., Ruzzene,M., Limongelli,V., Efeyan,A., Grumati,P. and
            Settembre,C.
  TITLE     Phosphorylation of FAM134C by CK2 controls starvation-induced
            ER-phagy
  JOURNAL   Sci Adv 8 (35), eabo1215 (2022)
   PUBMED   36044577
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Reggio,A., Buonomo,V., Berkane,R., Bhaskara,R.M., Tellechea,M.,
            Peluso,I., Polishchuk,E., Di Lorenzo,G., Cirillo,C., Esposito,M.,
            Hussain,A., Huebner,A.K., Hubner,C.A., Settembre,C., Hummer,G.,
            Grumati,P. and Stolz,A.
  TITLE     Role of FAM134 paralogues in endoplasmic reticulum remodeling,
            ER-phagy, and Collagen quality control
  JOURNAL   EMBO Rep 22 (9), e52289 (2021)
   PUBMED   34338405
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Fu,B., Wang,L., Li,S. and Dorf,M.E.
  TITLE     ZMPSTE24 defends against influenza and other pathogenic viruses
  JOURNAL   J Exp Med 214 (4), 919-929 (2017)
   PUBMED   28246125
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Kurth,I., Pamminger,T., Hennings,J.C., Soehendra,D., Huebner,A.K.,
            Rotthier,A., Baets,J., Senderek,J., Topaloglu,H., Farrell,S.A.,
            Nurnberg,G., Nurnberg,P., De Jonghe,P., Gal,A., Kaether,C.,
            Timmerman,V. and Hubner,C.A.
  TITLE     Mutations in FAM134B, encoding a newly identified Golgi protein,
            cause severe sensory and autonomic neuropathy
  JOURNAL   Nat Genet 41 (11), 1179-1181 (2009)
   PUBMED   19838196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX255926.10.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK051025.1, SRR17784646.1357639.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 64.2 cM"
     Protein         1..285
                     /product="reticulophagy regulator 3 isoform 2"
                     /note="protein FAM134C; family with sequence similarity
                     134, member C; reticulophagy regulator 3"
                     /calculated_mol_wt=31201
     Region          <1..51
                     /region_name="Arl6IP1_RETR3-like"
                     /note="ADP-ribosylation factor-like protein 6-interacting
                     protein 1, Reticulophagy regulator 3, and similar
                     proteins; cl41772"
                     /db_xref="CDD:425403"
     CDS             1..285
                     /gene="Retreg3"
                     /gene_synonym="1300010M03Rik; 4933404C01Rik; Fam134c"
                     /coded_by="NM_028933.4:479..1336"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS25450.1"
                     /db_xref="GeneID:67998"
                     /db_xref="MGI:MGI:1915248"
ORIGIN      
        1 mlgryipgll lsylmlviim mwplavyhrl wdrayvrlkp vlqrldfsvr gymmskqrer
       61 qlrrralhse ratdshsdse eelaafcpql ddstvarela itdsehsdae vsctengtfn
      121 lsrgqtplte gsedldghsd peesfardlp dfpsinvdpa glddeddtsi gmpslmyrsp
      181 pgagdtqvlp asrneaalpe lllsslpggs nltsnlaslv sqgmiqlals easqtdpsgp
      241 pprratrgfl rapssdldtd aegddfelld qselnqldpa ssrsh
//
LOCUS       NP_115609                594 aa            linear   PRI 27-APR-2025
DEFINITION  actin-histidine N-methyltransferase isoform a [Homo sapiens].
ACCESSION   NP_115609
VERSION     NP_115609.2
DBSOURCE    REFSEQ: accession NM_032233.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Gao,R., Yang,H. and Wang,Y.
  TITLE     SETD3 functions beyond histidine methylation
  JOURNAL   Life Sci 357, 123064 (2024)
   PUBMED   39299385
  REMARK    GeneRIF: SETD3 functions beyond histidine methylation.
            Review article
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Maas,M.N., Bilgin,N., Moesgaard,L., Hintzen,J.C.J., Drozak,A.,
            Drozak,J., Kongsted,J. and Mecinovic,J.
  TITLE     Examining prestructured beta-actin peptides as substrates of
            histidine methyltransferase SETD3
  JOURNAL   Sci Rep 14 (1), 26439 (2024)
   PUBMED   39488591
  REMARK    GeneRIF: Examining prestructured beta-actin peptides as substrates
            of histidine methyltransferase SETD3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Gao,X., Wang,B., Zhu,K., Wang,L., Qin,B., Shang,K., Ding,W.,
            Wang,J. and Cui,S.
  TITLE     The EV71 2A protease occupies the central cleft of SETD3 and
            disrupts SETD3-actin interaction
  JOURNAL   Nat Commun 15 (1), 4176 (2024)
   PUBMED   38755176
  REMARK    GeneRIF: The EV71 2A protease occupies the central cleft of SETD3
            and disrupts SETD3-actin interaction.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Al-Fakhar,M.S.Q., Bilgin,N., Moesgaard,L., Witecka,A., Drozak,J.,
            Kongsted,J. and Mecinovic,J.
  TITLE     The Role of Trp79 in beta-Actin on Histidine Methyltransferase
            SETD3 Catalysis
  JOURNAL   Chembiochem 24 (21), e202300490 (2023)
   PUBMED   37581408
  REMARK    GeneRIF: The Role of Trp79 in beta-Actin on Histidine
            Methyltransferase SETD3 Catalysis.
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Wen,C., Li,Y., Huang,Y., Wang,N., He,S., Bao,M., Zhou,H. and Wu,L.
  TITLE     CircSETD3 mediates acquired resistance to gefitinib in non-small
            lung cancer cells by FXR1/ECT2 pathway
  JOURNAL   Int J Biochem Cell Biol 154, 106344 (2023)
   PUBMED   36503048
  REMARK    GeneRIF: CircSETD3 mediates acquired resistance to gefitinib in
            non-small lung cancer cells by FXR1/ECT2 pathway.
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Cooper,S.E., Hodimont,E. and Green,C.M.
  TITLE     A fluorescent bimolecular complementation screen reveals MAF1, RNF7
            and SETD3 as PCNA-associated proteins in human cells
  JOURNAL   Cell Cycle 14 (15), 2509-2519 (2015)
   PUBMED   26030842
  REMARK    GeneRIF: MAF1, RNF7 and SETD3 are identified as PCNA-associated
            proteins in human cells and given this interaction with PCNA, Maf1,
            RNF7, and SetD3 are potentially involved in DNA replication, DNA
            repair, or associated processes.
REFERENCE   7  (residues 1 to 594)
  AUTHORS   Pires-Luis,A.S., Vieira-Coimbra,M., Vieira,F.Q., Costa-Pinheiro,P.,
            Silva-Santos,R., Dias,P.C., Antunes,L., Lobo,F., Oliveira,J.,
            Goncalves,C.S., Costa,B.M., Henrique,R. and Jeronimo,C.
  TITLE     Expression of histone methyltransferases as novel biomarkers for
            renal cell tumor diagnosis and prognostication
  JOURNAL   Epigenetics 10 (11), 1033-1043 (2015)
   PUBMED   26488939
  REMARK    GeneRIF: Results show that high expression levels of SMYD2, SETD3,
            and NO66 in renal cell tumors. Their low expression levels were
            significantly associated with shorter disease-specific and
            disease-free survival.
REFERENCE   8  (residues 1 to 594)
  AUTHORS   Eom,G.H., Kim,K.B., Kim,J.H., Kim,J.Y., Kim,J.R., Kee,H.J.,
            Kim,D.W., Choe,N., Park,H.J., Son,H.J., Choi,S.Y., Kook,H. and
            Seo,S.B.
  TITLE     Histone methyltransferase SETD3 regulates muscle differentiation
  JOURNAL   J Biol Chem 286 (40), 34733-34742 (2011)
   PUBMED   21832073
REFERENCE   9  (residues 1 to 594)
  AUTHORS   Tao,W.A., Wollscheid,B., O'Brien,R., Eng,J.K., Li,X.J.,
            Bodenmiller,B., Watts,J.D., Hood,L. and Aebersold,R.
  TITLE     Quantitative phosphoproteome analysis using a dendrimer conjugation
            chemistry and tandem mass spectrometry
  JOURNAL   Nat Methods 2 (8), 591-598 (2005)
   PUBMED   16094384
REFERENCE   10 (residues 1 to 594)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB988965.1, BX161471.1, AK026680.1 and BC037395.1.
            
            On Dec 18, 2003 this sequence version replaced NP_115609.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC142995.1, BX161471.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331768.10/ ENSP00000327436.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.2"
     Protein         1..594
                     /product="actin-histidine N-methyltransferase isoform a"
                     /EC_number="2.1.1.85"
                     /note="SET domain-containing protein 3; histone-lysine
                     N-methyltransferase setd3; actin-histidine
                     N-methyltransferase; protein-L-histidine
                     N-tele-methyltransferase; SET domain containing 3, actin
                     histidine methyltransferase"
                     /calculated_mol_wt=67126
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TU7.1)"
     Region          80..329
                     /region_name="SET_SETD3"
                     /note="SET domain found in SET domain-containing protein 3
                     (SETD3) and similar proteins; cd19176"
                     /db_xref="CDD:380953"
     Site            order(104,106,180,253..254,275..279,313,325,327,329)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380953"
     Site            order(105..106,123,251..256,275..279,286,311..314)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380953"
     Region          344..475
                     /region_name="Rubis-subs-bind"
                     /note="Rubisco LSMT substrate-binding; pfam09273"
                     /db_xref="CDD:462737"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86TU7.1)"
     Region          549..594
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TU7.1)"
     CDS             1..594
                     /gene="SETD3"
                     /gene_synonym="C14orf154; hSETD3"
                     /coded_by="NM_032233.3:141..1925"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9951.1"
                     /db_xref="GeneID:84193"
                     /db_xref="HGNC:HGNC:20493"
                     /db_xref="MIM:615671"
ORIGIN      
        1 mgkksrvktq ksgtgatatv spkeilnlts ellqkcsspa pgpgkeweey vqirtlveki
       61 rkkqkglsvt fdgkredyfp dlmkwaseng asvegfemvn fkeegfglra trdikaeelf
      121 lwvprkllmt vesaknsvlg plysqdrilq amgnialafh llceraspns fwqpyiqtlp
      181 seydtplyfe edevrylqst qaihdvfsqy kntarqyayf ykviqthpha nklplkdsft
      241 yedyrwavss vmtrqnqipt edgsrvtlal iplwdmcnht nglittgynl eddrcecval
      301 qdfrageqiy ifygtrsnae fvihsgfffd nnshdrvkik lgvsksdrly amkaevlara
      361 giptssvfal hfteppisaq llaflrvfcm teeelkehll gdsaidrift lgnsefpvsw
      421 dnevklwtfl edraslllkt ykttieedks vlknhdlsvr akmaiklrlg ekeilekavk
      481 saavnreyyr qqmeekaplp kyeesnlgll essvgdsrlp lvlrnleeea gvqdalnire
      541 aiskakaten glvngensip ngtrsenesl nqeskraved akgsssdsta gvke
//
LOCUS       NP_444281                335 aa            linear   PRI 27-APR-2025
DEFINITION  transcriptional adapter 1 [Homo sapiens].
ACCESSION   NP_444281
VERSION     NP_444281.1
DBSOURCE    REFSEQ: accession NM_053053.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Gloria-Bottini,F., Nicotra,M., Amante,A., Ambrosi,S., Cozzoli,E.,
            Saccucci,P., Bottini,E. and Magrini,A.
  TITLE     Effect of ADA1 mother-fetus and wife-husband phenotypic differences
            on the ratio birth weight/placental weight in fertile women and on
            reproductive success in couples with RSA
  JOURNAL   Am J Hum Biol 24 (2), 177-182 (2012)
   PUBMED   22287124
  REMARK    GeneRIF: Differences between mother and fetus in ADA(1) phenotype
            may influence the ratio BW/PW in healthy women and reproductive
            success in RSA women.
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Nagy,Z., Riss,A., Romier,C., le Guezennec,X., Dongre,A.R.,
            Orpinell,M., Han,J., Stunnenberg,H. and Tora,L.
  TITLE     The human SPT20-containing SAGA complex plays a direct role in the
            regulation of endoplasmic reticulum stress-induced genes
  JOURNAL   Mol Cell Biol 29 (6), 1649-1660 (2009)
   PUBMED   19114550
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Zhao,Y., Lang,G., Ito,S., Bonnet,J., Metzger,E., Sawatsubashi,S.,
            Suzuki,E., Le Guezennec,X., Stunnenberg,H.G., Krasnov,A.,
            Georgieva,S.G., Schule,R., Takeyama,K., Kato,S., Tora,L. and
            Devys,D.
  TITLE     A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
            coactivates nuclear receptors, and counteracts heterochromatin
            silencing
  JOURNAL   Mol Cell 29 (1), 92-101 (2008)
   PUBMED   18206972
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Martinez,E., Kundu,T.K., Fu,J. and Roeder,R.G.
  TITLE     A human SPT3-TAFII31-GCN5-L acetylase complex distinct from
            transcription factor IID
  JOURNAL   J Biol Chem 273 (37), 23781-23785 (1998)
   PUBMED   9726987
  REMARK    Erratum:[J Biol Chem 1998 Oct 16;273(42):27755]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN399642.1 and BC015401.2.
            
            Summary: TADA1L is a protein subunit of the human STAGA complex
            (SPT3; (MIM 602947)/TAF9 (MIM 600822)/GCN5 (MIM 602301)
            acetyltransferase complex), which is a chromatin-modifying
            multiprotein complex (Martinez et al., 2001 [PubMed
            11564863]).[supplied by OMIM, Apr 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015401.2, AK291922.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367874.5/ ENSP00000356848.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.1"
     Protein         1..335
                     /product="transcriptional adapter 1"
                     /note="transcriptional adaptor 1 (HFI1 homolog, yeast);
                     SPT3-associated factor 42 (STAF42); transcriptional
                     adapter 1-like protein"
                     /calculated_mol_wt=37251
     Region          7..193
                     /region_name="SAGA-Tad1"
                     /note="Transcriptional regulator of RNA polII, SAGA,
                     subunit; pfam12767"
                     /db_xref="CDD:463692"
     Region          83..103
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BN2.1)"
     Region          145..227
                     /region_name="HFD_TADA1"
                     /note="histone-fold domain found in transcriptional
                     adapter 1 (TADA1) and similar proteins; cd22934"
                     /db_xref="CDD:467058"
     CDS             1..335
                     /gene="TADA1"
                     /gene_synonym="ADA1; hADA1; HFI1; STAF42; TADA1L"
                     /coded_by="NM_053053.4:32..1039"
                     /db_xref="CCDS:CCDS1255.1"
                     /db_xref="GeneID:117143"
                     /db_xref="HGNC:HGNC:30631"
                     /db_xref="MIM:612763"
ORIGIN      
        1 matfvselea akknlsealg dnvkqywanl klwfkqkisk eefdleahrl ltqdnvhshn
       61 dfllailtrc qilvstpdga gslpwpggsa akpgkpkgkk klssvrqkfd hrfqpqnpls
      121 gaqqfvakdp qddddlklcs htmmlptrgq legrmivtay ehgldnvtee avsavvyave
      181 nhlkdiltsv vsrrkayrlr dghfkyafgs nvtpqpylkn svvaynnlie sppaftapca
      241 gqnpashppp ddaeqqaall lacsgdtlpa slppvnmydl fealqvhrev ipthtvyaln
      301 ieriitklwh pnheelqqdk vhrqrlaake glllc
//
LOCUS       NP_689683                346 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase ARK2C isoform 1 [Homo sapiens].
ACCESSION   NP_689683
VERSION     NP_689683.2
DBSOURCE    REFSEQ: accession NM_152470.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wright,J.D., Mace,P.D. and Day,C.L.
  TITLE     Secondary ubiquitin-RING docking enhances Arkadia and Ark2C E3
            ligase activity
  JOURNAL   Nat Struct Mol Biol 23 (1), 45-52 (2016)
   PUBMED   26656854
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Kelly,C.E., Thymiakou,E., Dixon,J.E., Tanaka,S., Godwin,J. and
            Episkopou,V.
  TITLE     Rnf165/Ark2C enhances BMP-Smad signaling to mediate motor axon
            extension
  JOURNAL   PLoS Biol 11 (4), e1001538 (2013)
   PUBMED   23610558
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Pickard,B.S., Malloy,M.P., Clark,L., Lehellard,S., Ewald,H.L.,
            Mors,O., Porteous,D.J., Blackwood,D.H. and Muir,W.J.
  TITLE     Candidate psychiatric illness genes identified in patients with
            pericentric inversions of chromosome 18
  JOURNAL   Psychiatr Genet 15 (1), 37-44 (2005)
   PUBMED   15722956
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC015959.9, AK127467.1, AK122819.1, BM680948.1, AW160725.1 and
            AC018931.9.
            
            On Jan 6, 2005 this sequence version replaced NP_689683.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127467.1, BK005135.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269439.12/ ENSP00000269439.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..346
                     /product="E3 ubiquitin-protein ligase ARK2C isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF165; lncRNA
                     activated in metastatic PCa; ring finger protein 165; E3
                     ubiquitin-protein ligase ARK2C"
                     /calculated_mol_wt=39395
     Region          23..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSG1.1)"
     Region          266..268
                     /region_name="Ubiquitin binding.
                     /evidence=ECO:0000269|PubMed:26656854,
                     ECO:0007744|PDB:5D0K"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSG1.1)"
     Region          267..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSG1.1)"
     Region          285..343
                     /region_name="RING-H2_RNF165"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 165 (RNF165) and similar proteins; cd16682"
                     /db_xref="CDD:438344"
     Site            order(295..296,298..299,320,323..324,327,332,335)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438344"
     Site            order(309..311,313..314,334)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438344"
     Region          309..313
                     /region_name="Ubiquitin binding.
                     /evidence=ECO:0000269|PubMed:26656854,
                     ECO:0007744|PDB:5D0K"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSG1.1)"
     CDS             1..346
                     /gene="ARK2C"
                     /gene_synonym="ARKL2; lncAMPC; RNF111L2; RNF165"
                     /coded_by="NM_152470.3:258..1298"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32823.1"
                     /db_xref="GeneID:494470"
                     /db_xref="HGNC:HGNC:31696"
ORIGIN      
        1 mvlvhvgylv lpvfgsvrnr gapfqrsqhp hatscrhfhl gppqpqqlap dfplahpvqs
       61 qpglsahmap ahqhsgalhq sltplptlqf qdvtgpsflp qalhqqyllq qqlleaqhrr
      121 lvshprrsqe rvsvhphrlh psfdfgqlqt pqprylaegt dwdlsvdagl spaqfqvrpi
      181 pqhyqhylat prmhhfprns sstqmvvhei rnypypqlhf lalqglnpsr htsavresye
      241 ellqledrlg nvtrgavqnt ierftfphky kkrrpqdgkg kkdegeesdt dekcticlsm
      301 ledgedvrrl pcmhlfhqlc vdqwlamskk cpicrvdiet qlgads
//
LOCUS       NP_005286                433 aa            linear   PRI 27-APR-2025
DEFINITION  G-protein coupled receptor 22 [Homo sapiens].
ACCESSION   NP_005286
VERSION     NP_005286.2
DBSOURCE    REFSEQ: accession NM_005295.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Chang,C.C., Chen,C.H., Hsu,S.Y. and Leu,S.
  TITLE     Cardiomyocyte-specific overexpression of GPR22 ameliorates cardiac
            injury in mice with acute myocardial infarction
  JOURNAL   BMC Cardiovasc Disord 24 (1), 287 (2024)
   PUBMED   38816768
  REMARK    GeneRIF: Cardiomyocyte-specific overexpression of GPR22 ameliorates
            cardiac injury in mice with acute myocardial infarction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Evangelou,E., Valdes,A.M., Kerkhof,H.J., Styrkarsdottir,U., Zhu,Y.,
            Meulenbelt,I., Lories,R.J., Karassa,F.B., Tylzanowski,P., Bos,S.D.,
            Akune,T., Arden,N.K., Carr,A., Chapman,K., Cupples,L.A., Dai,J.,
            Deloukas,P., Doherty,M., Doherty,S., Engstrom,G., Gonzalez,A.,
            Halldorsson,B.V., Hammond,C.L., Hart,D.J., Helgadottir,H.,
            Hofman,A., Ikegawa,S., Ingvarsson,T., Jiang,Q., Jonsson,H.,
            Kaprio,J., Kawaguchi,H., Kisand,K., Kloppenburg,M., Kujala,U.M.,
            Lohmander,L.S., Loughlin,J., Luyten,F.P., Mabuchi,A., McCaskie,A.,
            Nakajima,M., Nilsson,P.M., Nishida,N., Ollier,W.E.,
            Panoutsopoulou,K., van de Putte,T., Ralston,S.H., Rivadeneira,F.,
            Saarela,J., Schulte-Merker,S., Shi,D., Slagboom,P.E., Sudo,A.,
            Tamm,A., Tamm,A., Thorleifsson,G., Thorsteinsdottir,U., Tsezou,A.,
            Wallis,G.A., Wilkinson,J.M., Yoshimura,N., Zeggini,E., Zhai,G.,
            Zhang,F., Jonsdottir,I., Uitterlinden,A.G., Felson,D.T., van
            Meurs,J.B., Stefansson,K., Ioannidis,J.P. and Spector,T.D.
  CONSRTM   arcOGEN Consortium; Translation Research in Europe Applied
            Technologies for Osteoarthritis (TreatOA)
  TITLE     Meta-analysis of genome-wide association studies confirms a
            susceptibility locus for knee osteoarthritis on chromosome 7q22
  JOURNAL   Ann Rheum Dis 70 (2), 349-355 (2011)
   PUBMED   21068099
  REMARK    GeneRIF: Meta-analysis and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Kerkhof,H.J., Lories,R.J., Meulenbelt,I., Jonsdottir,I.,
            Valdes,A.M., Arp,P., Ingvarsson,T., Jhamai,M., Jonsson,H.,
            Stolk,L., Thorleifsson,G., Zhai,G., Zhang,F., Zhu,Y., van der
            Breggen,R., Carr,A., Doherty,M., Doherty,S., Felson,D.T.,
            Gonzalez,A., Halldorsson,B.V., Hart,D.J., Hauksson,V.B., Hofman,A.,
            Ioannidis,J.P., Kloppenburg,M., Lane,N.E., Loughlin,J.,
            Luyten,F.P., Nevitt,M.C., Parimi,N., Pols,H.A., Rivadeneira,F.,
            Slagboom,E.P., Styrkarsdottir,U., Tsezou,A., van de Putte,T.,
            Zmuda,J., Spector,T.D., Stefansson,K., Uitterlinden,A.G. and van
            Meurs,J.B.
  TITLE     A genome-wide association study identifies an osteoarthritis
            susceptibility locus on chromosome 7q22
  JOURNAL   Arthritis Rheum 62 (2), 499-510 (2010)
   PUBMED   20112360
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Adams,J.W., Wang,J., Davis,J.R., Liaw,C., Gaidarov,I., Gatlin,J.,
            Dalton,N.D., Gu,Y., Ross,J. Jr., Behan,D., Chien,K. and Connolly,D.
  TITLE     Myocardial expression, signaling, and function of GPR22: a
            protective role for an orphan G protein-coupled receptor
  JOURNAL   Am J Physiol Heart Circ Physiol 295 (2), H509-H521 (2008)
   PUBMED   18539757
  REMARK    GeneRIF: Demonstrate GRR22 expression in human heart.
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Lee,J., Hever,A., Willhite,D., Zlotnik,A. and Hevezi,P.
  TITLE     Effects of RNA degradation on gene expression analysis of human
            postmortem tissues
  JOURNAL   FASEB J 19 (10), 1356-1358 (2005)
   PUBMED   15955843
REFERENCE   6  (residues 1 to 433)
  AUTHORS   O'Dowd,B.F., Nguyen,T., Jung,B.P., Marchese,A., Cheng,R.,
            Heng,H.H., Kolakowski,L.F. Jr., Lynch,K.R. and George,S.R.
  TITLE     Cloning and chromosomal mapping of four putative novel human
            G-protein-coupled receptor genes
  JOURNAL   Gene 187 (1), 75-81 (1997)
   PUBMED   9073069
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA519131.1, AK122621.1,
            BC107128.2, U66581.1 and AC002381.1.
            
            On Apr 5, 2006 this sequence version replaced NP_005286.1.
            
            Summary: This gene is a member of the G-protein coupled receptor 1
            family and encodes a multi-pass membrane protein. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.61439.1,
                                           SRR1660807.64017.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304402.6/ ENSP00000302676.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..433
                     /product="G-protein coupled receptor 22"
                     /note="probable G-protein coupled receptor 22"
                     /calculated_mol_wt=49135
     Site            16
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99680.2)"
     Region          44..370
                     /region_name="7tm_classA_rhodopsin-like"
                     /note="rhodopsin receptor-like class A family of the
                     seven-transmembrane G protein-coupled receptor
                     superfamily; cd00637"
                     /db_xref="CDD:410626"
     Region          44..69
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410626"
     Site            46..66
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99680.2)"
     Region          77..103
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410626"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99680.2)"
     Site            order(99,102..103,115..120,122..123,126,169,171..175,208,
                     211..213,215..217,219..220,326,329..330,332..333,345..346,
                     348..350,353,356..357)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:410626"
     Region          115..145
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410626"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99680.2)"
     Region          156..175
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410626"
     Site            157..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99680.2)"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99680.2)"
     Region          208..233
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410626"
     Site            209..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99680.2)"
     Region          306..335
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410626"
     Site            316..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99680.2)"
     Region          346..370
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410626"
     Site            350..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99680.2)"
     CDS             1..433
                     /gene="GPR22"
                     /coded_by="NM_005295.3:1347..2648"
                     /db_xref="CCDS:CCDS5744.1"
                     /db_xref="GeneID:2845"
                     /db_xref="HGNC:HGNC:4477"
                     /db_xref="MIM:601910"
ORIGIN      
        1 mcfspilein mqsesnitvr ddiddintnm yqplsyplsf qvsltgflml eivlglgsnl
       61 tvlvlycmks nlinsvsnii tmnlhvldvi icvgciplti villlslesn taliccfhea
      121 cvsfasvsta invfaitldr ydisvkpanr iltmgravml misiwifsff sflipfievn
      181 ffslqsgntw enktllcvst neyytelgmy yhllvqipif fftvvvmlit ytkilqalni
      241 rigtrfstgq kkkarkkkti slttqheatd msqssggrnv vfgvrtsvsv iialrravkr
      301 hrerrerqkr vfrmslliis tfllcwtpis vlnttilclg psdllvklrl cflvmaygtt
      361 ifhpllyaft rqkfqkvlks kmkkrvvsiv eadplpnnav ihnswidpkr nkkitfedse
      421 irekclvpqv vtd
//
LOCUS       NP_057537                722 aa            linear   PRI 27-APR-2025
DEFINITION  NCK-interacting protein with SH3 domain isoform 1 [Homo sapiens].
ACCESSION   NP_057537
VERSION     NP_057537.1
DBSOURCE    REFSEQ: accession NM_016453.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Kim,H., Oh,H., Oh,Y.S., Bae,J., Hong,N.H., Park,S.J., Ahn,S.,
            Lee,M., Rhee,S., Lee,S.H., Jun,Y., Kim,S.H., Huh,Y.H. and Song,W.K.
  TITLE     SPIN90, an adaptor protein, alters the proximity between Rab5 and
            Gapex5 and facilitates Rab5 activation during EGF endocytosis
  JOURNAL   Exp Mol Med 51 (7), 1-14 (2019)
   PUBMED   31358736
  REMARK    GeneRIF: The findings suggest that SPIN90, as an adaptor protein,
            simultaneously binds inactive Rab5 and Gapex5, thereby altering
            their spatial proximity and facilitating Rab5 activation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 722)
  AUTHORS   Luan,Q., Liu,S.L., Helgeson,L.A. and Nolen,B.J.
  TITLE     Structure of the nucleation-promoting factor SPIN90 bound to the
            actin filament nucleator Arp2/3 complex
  JOURNAL   EMBO J 37 (22) (2018)
   PUBMED   30322896
  REMARK    GeneRIF: Structure of the nucleation-promoting factor SPIN90 bound
            to the actin filament nucleator Arp2/3 complex.
REFERENCE   6  (residues 1 to 722)
  AUTHORS   Lim,C.S., Park,E.S., Kim,D.J., Song,Y.H., Eom,S.H., Chun,J.S.,
            Kim,J.H., Kim,J.K., Park,D. and Song,W.K.
  TITLE     SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adaptor
            protein that is developmentally regulated during cardiac myocyte
            differentiation
  JOURNAL   J Biol Chem 276 (16), 12871-12878 (2001)
   PUBMED   11278500
REFERENCE   7  (residues 1 to 722)
  AUTHORS   Hayakawa,A., Matsuda,Y., Daibata,M., Nakamura,H. and Sano,K.
  TITLE     Genomic organization, tissue expression, and cellular localization
            of AF3p21, a fusion partner of MLL in therapy-related leukemia
  JOURNAL   Genes Chromosomes Cancer 30 (4), 364-374 (2001)
   PUBMED   11241789
REFERENCE   8  (residues 1 to 722)
  AUTHORS   Fukuoka,M., Suetsugu,S., Miki,H., Fukami,K., Endo,T. and
            Takenawa,T.
  TITLE     A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding
            protein, WISH, induces Arp2/3 complex activation independent of
            Cdc42
  JOURNAL   J Cell Biol 152 (3), 471-482 (2001)
   PUBMED   11157975
REFERENCE   9  (residues 1 to 722)
  AUTHORS   Sano,K., Hayakawa,A., Piao,J.H., Kosaka,Y. and Nakamura,H.
  TITLE     Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed
            lineage leukemia protein in a therapy-related leukemia with t(3;11)
            (p21;q23)
  JOURNAL   Blood 95 (3), 1066-1068 (2000)
   PUBMED   10648423
REFERENCE   10 (residues 1 to 722)
  AUTHORS   de Bernard,M., Moschioni,M., Napolitani,G., Rappuoli,R. and
            Montecucco,C.
  TITLE     The VacA toxin of Helicobacter pylori identifies a new intermediate
            filament-interacting protein
  JOURNAL   EMBO J 19 (1), 48-56 (2000)
   PUBMED   10619843
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY010884.1, HY050918.1 and
            AF303581.1.
            
            Summary: The protein encoded by this gene contains a nuclear
            localization signal. It plays a role in signal transduction, and
            may function in the maintenance of sarcomeres and in the assembly
            of myofibrils into sarcomeres. It also plays an important role in
            stress fiber formation This protein is involved in the formation
            and maintenance of dendritic spines, and modulates synaptic
            activity in neurons. The gene is involved in therapy-related
            leukemia by a chromosomal translocation t(3;11)(p21;q23) that
            involves this gene and the myeloid/lymphoid leukemia gene.
            Alternative splicing results in multiple transcript variants of
            this gene. [provided by RefSeq, Aug 2019].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF178432.1, SRR1803615.191540.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294129.7/ ENSP00000294129.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..722
                     /product="NCK-interacting protein with SH3 domain isoform
                     1"
                     /note="SH3 protein interacting with Nck, 90 kDa; dia
                     interacting protein; diaphanous protein interacting
                     protein; dia-interacting protein 1; SH3 adapter protein
                     SPIN90; 54 kDa VacA-interacting protein; 90 kDa SH3
                     protein interacting with Nck; 54 kDa vimentin-interacting
                     protein; WASP-interacting SH3-domain protein;
                     wiskott-Aldrich syndrome protein-interacting protein"
                     /calculated_mol_wt=78829
     Region          1..54
                     /region_name="SH3_SPIN90"
                     /note="Src homology 3 domain of SH3 protein interacting
                     with Nck, 90 kDa (SPIN90); cd11849"
                     /db_xref="CDD:212783"
     Site            order(6,8,11,15,33..34,49,51..52)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212783"
     Site            57..58
                     /site_type="other"
                     /note="Breakpoint for translocation to form
                     KMT2A/MLL1-AF3P21 oncogene; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Region          101..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESJ4; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Region          149..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Region          175..192
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESJ4; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Region          <570..683
                     /region_name="SPIN90_LRD"
                     /note="SPIN90/Ldb17, leucine-rich domain; pfam09431"
                     /db_xref="CDD:462796"
     CDS             1..722
                     /gene="NCKIPSD"
                     /gene_synonym="AF3P21; DIP; DIP1; ORF1; SPIN90; VIP54;
                     WASLBP; WISH"
                     /coded_by="NM_016453.4:109..2277"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2776.1"
                     /db_xref="GeneID:51517"
                     /db_xref="HGNC:HGNC:15486"
                     /db_xref="MIM:606671"
ORIGIN      
        1 myralyafrs aepnalafaa getflvlers sahwwlaara rsgetgyvpp aylrrlqgle
       61 qdvlqaidra ieavhntamr dggkysleqr gvlqklihhr ketlsrrgps assvavmtss
      121 tsdhhldaaa arqpngvcra gferqhslps sehlgadggl yqiplpssqi ppqprraapt
      181 tppppvkrrd realmasgsg ghntmpsggn svssgssvss tsldtlytss spsepgsscs
      241 ptpppvprrg thttvsqvqp ppskasapep paeeevatgt tsasddleal gtlslgttee
      301 kaaaeaavpr tigaelmelv rrntglshel crvaigiivg hiqasvpass pvmeqvllsl
      361 vegkdlsmal psgqvchdqq rlevifadla rrkddaqqrs walyedegvi rcyleellhi
      421 ltdadpevck kmckrnefes vlalvayyqm ehraslrlll lkcfgamcsl daaiistlvs
      481 svlpvelard mqtdtqdhqk lcysalilam vfsmgeavpy ahyehlgtpf aqfllnived
      541 glpldtteql pdlcvnllla lnlhlpaadq nvimaalskh anvkifsekl llllnrgddp
      601 vrifkhepqp phsvlkflqd vfgspataai fyhtdmmali ditvrhiadl spgdklrmey
      661 lslmhaivrt tpylqhrhrl pdlqailrri lneeetspqc qmdrmivrem ckeflvlgea
      721 ps
//
LOCUS       NP_689704                502 aa            linear   PRI 27-APR-2025
DEFINITION  N-fatty-acyl-amino acid synthase/hydrolase PM20D1 precursor [Homo
            sapiens].
ACCESSION   NP_689704 XP_946313
VERSION     NP_689704.4
DBSOURCE    REFSEQ: accession NM_152491.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Huang,X., He,P. and Wu,L.
  TITLE     Clinical Significance of Peptidase M20 Domain Containing 1 Ii
            Patients with Carotid Atherosclerosis
  JOURNAL   Arq Bras Cardiol 119 (3), 372-379 (2022)
   PUBMED   35544855
  REMARK    GeneRIF: Clinical Significance of Peptidase M20 Domain Containing 1
            Ii Patients with Carotid Atherosclerosis.', trans 'Significado
            Clinico do Dominio da Peptidase M20 Contendo 1 em Pacientes com
            Aterosclerose Carotidea.
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Yang,R., Hu,Y., Lee,C.H., Liu,Y., Diaz-Canestro,C., Fong,C.H.Y.,
            Lin,H., Cheng,K.K.Y., Pravelil,A.P., Song,E., Lam,K.S.L. and Xu,A.
  TITLE     PM20D1 is a circulating biomarker closely associated with obesity,
            insulin resistance and metabolic syndrome
  JOURNAL   Eur J Endocrinol 186 (2), 151-161 (2021)
   PUBMED   34757919
  REMARK    GeneRIF: PM20D1 is a circulating biomarker closely associated with
            obesity, insulin resistance and metabolic syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Wang,Q., Chen,Y., Readhead,B., Chen,K., Su,Y., Reiman,E.M. and
            Dudley,J.T.
  TITLE     Longitudinal data in peripheral blood confirm that PM20D1 is a
            quantitative trait locus (QTL) for Alzheimer's disease and
            implicate its dynamic role in disease progression
  JOURNAL   Clin Epigenetics 12 (1), 189 (2020)
   PUBMED   33298155
  REMARK    GeneRIF: Longitudinal data in peripheral blood confirm that PM20D1
            is a quantitative trait locus (QTL) for Alzheimer's disease and
            implicate its dynamic role in disease progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Kim,J.T., Terrell,S.M., Li,V.L., Wei,W., Fischer,C.R. and Long,J.Z.
  TITLE     Cooperative enzymatic control of N-acyl amino acids by PM20D1 and
            FAAH
  JOURNAL   Elife 9, e55211 (2020)
   PUBMED   32271712
  REMARK    GeneRIF: Cooperative enzymatic control of N-acyl amino acids by
            PM20D1 and FAAH.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Sanchez-Mut,J.V., Glauser,L., Monk,D. and Graff,J.
  TITLE     Comprehensive analysis of PM20D1 QTL in Alzheimer's disease
  JOURNAL   Clin Epigenetics 12 (1), 20 (2020)
   PUBMED   32014019
  REMARK    GeneRIF: Comprehensive analysis of PM20D1 QTL in Alzheimer's
            disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Sun,J., Tao,S., Gao,Y., Peng,T., Tan,A., Zhang,H., Yang,X., Qin,X.,
            Hu,Y., Feng,J., Kim,S.T., Lin,X., Wu,Y., Zhang,J., Li,Z., Li,L.,
            Mo,L., Liang,Z., Shi,D., Huang,Z., Huang,X., Liu,M., Liu,Q.,
            Zhang,S., Lilly Zheng,S., Xu,J. and Mo,Z.
  TITLE     Genome-wide association study identified novel genetic variant on
            SLC45A3 gene associated with serum levels prostate-specific antigen
            (PSA) in a Chinese population
  JOURNAL   Hum Genet 132 (4), 423-429 (2013)
   PUBMED   23269536
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Yan,Y.P., Mo,X.Y., Tian,J., Zhao,G.H., Yin,X.Z., Jin,F.Y. and
            Zhang,B.R.
  TITLE     An association between the PARK16 locus and Parkinson's disease in
            a cohort from eastern China
  JOURNAL   Parkinsonism Relat Disord 17 (10), 737-739 (2011)
   PUBMED   21840748
REFERENCE   8  (residues 1 to 502)
  AUTHORS   Satake,W., Nakabayashi,Y., Mizuta,I., Hirota,Y., Ito,C., Kubo,M.,
            Kawaguchi,T., Tsunoda,T., Watanabe,M., Takeda,A., Tomiyama,H.,
            Nakashima,K., Hasegawa,K., Obata,F., Yoshikawa,T., Kawakami,H.,
            Sakoda,S., Yamamoto,M., Hattori,N., Murata,M., Nakamura,Y. and
            Toda,T.
  TITLE     Genome-wide association study identifies common variants at four
            loci as genetic risk factors for Parkinson's disease
  JOURNAL   Nat Genet 41 (12), 1303-1307 (2009)
   PUBMED   19915576
REFERENCE   9  (residues 1 to 502)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   10 (residues 1 to 502)
  AUTHORS   Brass,A.L., Dykxhoorn,D.M., Benita,Y., Yan,N., Engelman,A.,
            Xavier,R.J., Lieberman,J. and Elledge,S.J.
  TITLE     Identification of host proteins required for HIV infection through
            a functional genomic screen
  JOURNAL   Science 319 (5865), 921-926 (2008)
   PUBMED   18187620
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA387977.1, BC063477.1, AC119673.3 and BM987801.1.
            
            On Nov 24, 2009 this sequence version replaced NP_689704.3.
            
            Transcript Variant: This variant (1) encodes the supported protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290786.1, BC063477.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367136.5/ ENSP00000356104.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..502
                     /product="N-fatty-acyl-amino acid synthase/hydrolase
                     PM20D1 precursor"
                     /EC_number="3.5.1.14"
                     /EC_number="3.5.1.114"
                     /note="probable carboxypeptidase PM20D1; peptidase M20
                     domain-containing protein 1; N-fatty-acyl-amino acid
                     synthase/hydrolase PM20D1"
                     /calculated_mol_wt=53038
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2721
     mat_peptide     26..502
                     /product="N-fatty-acyl-amino acid synthase/hydrolase
                     PM20D1. /id=PRO_0000321928"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GTS8.3)"
                     /calculated_mol_wt=53038
     Region          53..487
                     /region_name="M20_yscS"
                     /note="M20 Peptidase, carboxypeptidase yscS; cd05674"
                     /db_xref="CDD:349923"
     Site            252
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6GTS8.3)"
     CDS             1..502
                     /gene="PM20D1"
                     /gene_synonym="Cps1"
                     /coded_by="NM_152491.5:61..1569"
                     /db_xref="CCDS:CCDS1460.1"
                     /db_xref="GeneID:148811"
                     /db_xref="HGNC:HGNC:26518"
                     /db_xref="MIM:617124"
ORIGIN      
        1 maqrcvcvla lvamlllvfp tvsrsmgprs gehqrasrip sqfskeerva mkealkgaiq
       61 iptvtfssek snttalaefg kyihkvfptv vstsfiqhev veeyshlfti qgsdpslqpy
      121 llmahfdvvp apeegwevpp fsglerdgii ygrgtlddkn svmallqale lllirkyipr
      181 rsffislghd eessgtgaqr isallqsrgv qlafivdegg filddfipnf kkpialiavs
      241 ekgsmnlmlq vnmtsghssa ppketsigil aaavsrleqt pmpiifgsgt vvtvlqqlan
      301 efpfpvniil snpwlfepli srfmernplt naiirtttal tifkagvkfn vippvaqatv
      361 nfrihpgqtv qevleltkni vadnrvqfhv lsafdplpvs psddkalgyq llrqtvqsvf
      421 pevnitapvt signtdsrff tnlttgiyrf ypiyiqpedf krihgvneki svqayetqvk
      481 fifeliqnad tdqepvshlh kl
//
LOCUS       NP_037396                483 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX25 isoform 1 [Homo sapiens].
ACCESSION   NP_037396
VERSION     NP_037396.3
DBSOURCE    REFSEQ: accession NM_013264.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Kavarthapu,R., Anbazhagan,R., Raju,M., Morris,C.T., Pickel,J. and
            Dufau,M.L.
  TITLE     Targeted knock-in mice with a human mutation in GRTH/DDX25 reveals
            the essential role of phosphorylated GRTH in spermatid development
            during spermatogenesis
  JOURNAL   Hum Mol Genet 28 (15), 2561-2572 (2019)
   PUBMED   31009948
  REMARK    GeneRIF: Targeted knock-in mice with a human mutation in GRTH/DDX25
            reveals the essential role of phosphorylated GRTH in spermatid
            development during spermatogenesis.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Raju,M., Hassan,S.A., Kavarthapu,R., Anbazhagan,R. and Dufau,M.L.
  TITLE     Characterization of the Phosphorylation Site of GRTH/DDX25 and
            Protein Kinase A Binding Interface Provides Structural Basis for
            the Design of a Non-Hormonal Male Contraceptive
  JOURNAL   Sci Rep 9 (1), 6705 (2019)
   PUBMED   31040297
  REMARK    GeneRIF: Characterization of the Phosphorylation Site of GRTH/DDX25
            and Protein Kinase A Binding Interface Provides Structural Basis
            for the Design of a Non-Hormonal Male Contraceptive.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Jaiswal,D., Trivedi,S., Agrawal,N.K. and Singh,K.
  TITLE     Association of the gonadotrophin-regulated testicular RNA helicase
            gene polymorphism with human male infertility
  JOURNAL   Andrologia 46 (9), 1063-1066 (2014)
   PUBMED   24168058
  REMARK    GeneRIF: Analysed the association of GRTH gene IVS6+55G/T and
            c.852C/T polymorphisms with male infertility. The c.852 T allele
            was associated with an increased risk of male infertility (OR:
            3.16, P = 0.008), whereas IVS6+55G/T allele conferred no risk.
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Aston,K.I., Krausz,C., Laface,I., Ruiz-Castane,E. and Carrell,D.T.
  TITLE     Evaluation of 172 candidate polymorphisms for association with
            oligozoospermia or azoospermia in a large cohort of men of European
            descent
  JOURNAL   Hum Reprod 25 (6), 1383-1397 (2010)
   PUBMED   20378615
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Tsai-Morris,C.H., Koh,E., Sheng,Y., Maeda,Y., Gutti,R., Namiki,M.
            and Dufau,M.L.
  TITLE     Polymorphism of the GRTH/DDX25 gene in normal and infertile
            Japanese men: a missense mutation associated with loss of GRTH
            phosphorylation
  JOURNAL   Mol Hum Reprod 13 (12), 887-892 (2007)
   PUBMED   17848414
  REMARK    GeneRIF: Data show that the Arg(242)His missense mutation of the
            GRTH/DDX25 gene associated with expression of a protein with
            reduced basicity, and the absence of the phospho-GRTH species,
            could impact on germ cell development and/or function.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 483)
  AUTHORS   A,Z., Zhang,S., Yang,Y., Ma,Y., Lin,L. and Zhang,W.
  TITLE     Single nucleotide polymorphisms of the gonadotrophin-regulated
            testicular helicase (GRTH) gene may be associated with the human
            spermatogenesis impairment
  JOURNAL   Hum Reprod 21 (3), 755-759 (2006)
   PUBMED   16293649
  REMARK    GeneRIF: SNP IVS6+55G-->T and c.852C-->T of GRTH gene may be
            associated with male infertility with azoospermia or severe
            oligozoospermia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Tsai-Morris,C.H., Lei,S., Jiang,Q., Sheng,Y. and Dufau,M.L.
  TITLE     Genomic organization and transcriptional analysis of
            gonadotropin-regulated testicular RNA helicase--GRTH/DDX25 gene
  JOURNAL   Gene 331, 83-94 (2004)
   PUBMED   15094194
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Tsai-Morris,C.H., Sheng,Y., Lee,E., Lei,K.J. and Dufau,M.L.
  TITLE     Gonadotropin-regulated testicular RNA helicase (GRTH/Ddx25) is
            essential for spermatid development and completion of
            spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 101 (17), 6373-6378 (2004)
   PUBMED   15096601
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Tang,P.Z., Tsai-Morris,C.H. and Dufau,M.L.
  TITLE     A novel gonadotropin-regulated testicular RNA helicase. A new
            member of the dead-box family
  JOURNAL   J Biol Chem 274 (53), 37932-37940 (1999)
   PUBMED   10608860
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC050360.1, AL563479.3,
            AF155140.3 and AP000842.6.
            
            On Jan 2, 2008 this sequence version replaced NP_037396.2.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure, such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of the DEAD box
            protein family are believed to be involved in embryogenesis,
            spermatogenesis, and cellular growth and division. This gene
            encodes a member of this family. The encoded protein is a
            gonadotropin-regulated and developmentally expressed testicular RNA
            helicase. It may serve to maintain testicular functions related to
            steroidogenesis and spermatogenesis. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.234420.1,
                                           SRR1803617.138928.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263576.11/ ENSP00000263576.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.2"
     Protein         1..483
                     /product="ATP-dependent RNA helicase DDX25 isoform 1"
                     /EC_number="3.6.4.13"
                     /note="DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 25;
                     gonadotropin-regulated testicular RNA helicase;
                     ATP-dependent RNA helicase DDX25; DEAD (Asp-Glu-Ala-Asp)
                     box polypeptide 25; DEAD box protein 25; DEAD
                     (Asp-Glu-Ala-Asp) box helicase 25; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=54561
     Region          61..74
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHL0.2)"
     Region          80..308
                     /region_name="DEADc_DDX25"
                     /note="DEAD-box helicase domain of DEAD box protein 25;
                     cd18048"
                     /db_xref="CDD:350806"
     Region          97..125
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHL0.2)"
     Region          100..114
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHL0.2)"
     Site            order(117,119,124,144..150,248,280)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350806"
     Site            order(175..177,204,222..225,228,232,258,261)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350806"
     Region          247..250
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHL0.2)"
     Region          312..448
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(401,403,434,437..438)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     CDS             1..483
                     /gene="DDX25"
                     /gene_synonym="GRTH"
                     /coded_by="NM_013264.5:11..1462"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44766.1"
                     /db_xref="GeneID:29118"
                     /db_xref="HGNC:HGNC:18698"
                     /db_xref="MIM:607663"
ORIGIN      
        1 masllwggda gaaeserlns hfsnlsqprk nlwgikstav rnidgsinni neddeedvvd
       61 laansllnkl ihqslvessh rvevlqkdps splysvktfe elrlkeellk giyamgfnrp
      121 skiqemalpm mlahppqnli aqsqsgtgkt aafvlamlsr vnalelfpqc lclaptyela
      181 lqtgrvveqm gkfcvdvqvm yairgnripr gtditkqiii gtpgtvldwc fklklidltk
      241 irvfvldead vmidtqgfsd hsiriqralp secqmllfsa tfedsvwhfa eriipdpnvi
      301 klrkeeltln nirqyyvlce hrkdkyqalc niygsitigq aiifcqtrrn akwltvemiq
      361 dghqvsllsg eltveqrasi iqrfrdgkek vlittnvcar gidvkqvtiv vnfdlpvkqg
      421 eepdyetylh rigrtgrfgk kglafnmiev delpslmkiq dhfnssikql naedmdeiek
      481 idy
//
LOCUS       NP_872313                452 aa            linear   PRI 27-APR-2025
DEFINITION  keratin, type II cytoskeletal 80 isoform K80 [Homo sapiens].
ACCESSION   NP_872313
VERSION     NP_872313.2
DBSOURCE    REFSEQ: accession NM_182507.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Yun,W.J., Li,J., Yin,N.C., Zhang,C.Y., Cui,Z.G., Zhang,L. and
            Zheng,H.C.
  TITLE     The facilitating effects of KRT80 on chemoresistance, lipogenesis,
            and invasion of esophageal cancer
  JOURNAL   Cancer Biol Ther 25 (1), 2302162 (2024)
   PUBMED   38241178
  REMARK    GeneRIF: The facilitating effects of KRT80 on chemoresistance,
            lipogenesis, and invasion of esophageal cancer.
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Gao,X., Wang,G., Zhang,M., Zhang,X., Zhang,S. and Long,H.
  TITLE     LINC01485 contributes to colorectal cancer progression by targeting
            miR-383-5p/KRT80 axis
  JOURNAL   Environ Toxicol 39 (1), 398-408 (2024)
   PUBMED   37782686
  REMARK    GeneRIF: LINC01485 contributes to colorectal cancer progression by
            targeting miR-383-5p/KRT80 axis.
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Shi,K.H., Xue,H., Zhao,E.H., Xiao,L.J., Sun,H.Z. and Zheng,H.C.
  TITLE     KRT80 expression works as a biomarker and a target for
            differentiation in gastric cancer
  JOURNAL   Histol Histopathol 39 (1), 117-130 (2024)
   PUBMED   37129345
  REMARK    GeneRIF: KRT80 expression works as a biomarker and a target for
            differentiation in gastric cancer.
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Wei,X.Y., Zhao,J., Tong,H.B., Cheng,S.J., He,N. and Song,F.X.
  TITLE     Characters of KRT80 and its roles in neoplasms diseases
  JOURNAL   Cancer Med 12 (13), 13991-14003 (2023)
   PUBMED   37211956
  REMARK    GeneRIF: Characters of KRT80 and its roles in neoplasms diseases.
            Review article
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Zhang,F., Wang,G., Yan,W. and Jiang,H.
  TITLE     MiR-4268 suppresses gastric cancer genesis through inhibiting
            keratin 80
  JOURNAL   Cell Cycle 21 (19), 2051-2064 (2022)
   PUBMED   35748914
  REMARK    GeneRIF: MiR-4268 suppresses gastric cancer genesis through
            inhibiting keratin 80.
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Bray,D.J., Walsh,T.R., Noro,M.G. and Notman,R.
  TITLE     Complete Structure of an Epithelial Keratin Dimer: Implications for
            Intermediate Filament Assembly
  JOURNAL   PLoS One 10 (7), e0132706 (2015)
   PUBMED   26181054
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Liu,Y., Cao,L., Li,Z., Zhou,D., Liu,W., Shen,Q., Wu,Y., Zhang,D.,
            Hu,X., Wang,T., Ye,J., Weng,X., Zhang,H., Zhang,D., Zhang,Z.,
            Liu,F., He,L. and Shi,Y.
  TITLE     A genome-wide association study identifies a locus on TERT for mean
            telomere length in Han Chinese
  JOURNAL   PLoS One 9 (1), e85043 (2014)
   PUBMED   24465473
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Langbein,L., Eckhart,L., Rogers,M.A., Praetzel-Wunder,S. and
            Schweizer,J.
  TITLE     Against the rules: human keratin K80: two functional alternative
            splice variants, K80 and K80.1, with special cellular localization
            in a wide range of epithelia
  JOURNAL   J Biol Chem 285 (47), 36909-36921 (2010)
   PUBMED   20843789
  REMARK    GeneRIF: Alternative splice variants, K80 and K80.1 distribute
            differently in epithelia of hair and skin.
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Schweizer,J., Bowden,P.E., Coulombe,P.A., Langbein,L., Lane,E.B.,
            Magin,T.M., Maltais,L., Omary,M.B., Parry,D.A., Rogers,M.A. and
            Wright,M.W.
  TITLE     New consensus nomenclature for mammalian keratins
  JOURNAL   J Cell Biol 174 (2), 169-174 (2006)
   PUBMED   16831889
REFERENCE   10 (residues 1 to 452)
  AUTHORS   Rogers,M.A., Edler,L., Winter,H., Langbein,L., Beckmann,I. and
            Schweizer,J.
  TITLE     Characterization of new members of the human type II keratin gene
            family and a general evaluation of the keratin gene domain on
            chromosome 12q13.13
  JOURNAL   J Invest Dermatol 124 (3), 536-544 (2005)
   PUBMED   15737194
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021066.37, BC065180.1 and
            AJ717743.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 10, 2007 this sequence version replaced NP_872313.1.
            
            Summary: Keratins are intermediate filament proteins responsible
            for the structural integrity of epithelial cells and are subdivided
            into epithelial keratins and hair keratins. This gene's expression
            profile shows that it encodes a type II epithelial keratin,
            although structurally the encoded protein is more like a type II
            hair keratin. This protein is involved in cell differentiation,
            localizing near desmosomal plaques in earlier stages of
            differentiation but then dispersing throughout the cytoplasm in
            terminally differentiating cells. The type II keratins are
            clustered in a region of chromosome 12q13. Two transcript variants
            encoding two different fully functional isoforms have been found
            for this gene.[provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (K80, also known as a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047308.1, AJ717743.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147596 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394815.3/ ENSP00000378292.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..452
                     /product="keratin, type II cytoskeletal 80 isoform K80"
                     /note="keratin, type II cytoskeletal 80; type II keratin;
                     keratin b20; K80; CK-80; cytokeratin-80; type-II keratin
                     Kb20; keratin 80, type II"
                     /calculated_mol_wt=50394
     Region          1..82
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KB66.2)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6KB66.2)"
     Region          82..393
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          82..118
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KB66.2)"
     Region          119..135
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KB66.2)"
     Region          136..227
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KB66.2)"
     Region          228..251
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KB66.2)"
     Region          252..390
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KB66.2)"
     Site            334
                     /site_type="other"
                     /note="Stutter; propagated from UniProtKB/Swiss-Prot
                     (Q6KB66.2)"
     Region          391..452
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KB66.2)"
     Site            396
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6KB66.2)"
     Region          412..434
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KB66.2)"
     CDS             1..452
                     /gene="KRT80"
                     /gene_synonym="KB20"
                     /coded_by="NM_182507.3:113..1471"
                     /note="isoform K80 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8821.2"
                     /db_xref="GeneID:144501"
                     /db_xref="HGNC:HGNC:27056"
                     /db_xref="MIM:611161"
ORIGIN      
        1 macrscvvgf sslsscevtp vgsprpgtsg wdscrapgpg fssrsltgcw sagtiskvtv
       61 npgllvpldv kldpavqqlk nqekeemkal ndkfasligk vqaleqrnql letrwsflqg
      121 qdsaifdlgh lyeeyqgrlq eelrkvsqer gqleanllqv lekveefrir yedeiskrtd
      181 meftfvqlkk dldaeclhrt eletklksle sfvelmktiy eqelkdlaaq vkdvsvtvgm
      241 dsrchidlsg iveevkaqyd avaarsleea eaysrsqlee qaarsaeygs slqssrseia
      301 dlnvriqklr sqilsvkshc lkleenikta eeqgelafqd aktklaqlea alqqakqdma
      361 rqlrkyqelm nvklaldiei atyrklvege egrmdspsat vvsavqsrck taasrsglsk
      421 apsrkkkgsk gpvikitems ekyfsqesev se
//
LOCUS       NP_001348950             843 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 8 [Mus musculus].
ACCESSION   NP_001348950
VERSION     NP_001348950.1
DBSOURCE    REFSEQ: accession NM_001362021.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 843)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 843)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 843)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 843)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 843)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 843)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 843)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 843)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            Transcript Variant: This variant (31), as well as variant 30,
            encodes isoform 4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164131
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..843
                     /product="cAMP-regulated phosphoprotein 21 isoform 8"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=92408
     Region          162..223
                     /region_name="R3H_encore_like"
                     /note="R3H domain of encore-like and DIP1-like proteins.
                     Drosophila encore is involved in the germline exit after
                     four mitotic divisions, by facilitating
                     SCF-ubiquitin-proteasome-dependent proteolysis. Maize
                     DBF1-interactor protein 1 (DIP1) containing an R3H...;
                     cd02642"
                     /db_xref="CDD:100071"
     Site            order(195,199)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100071"
     Region          244..299
                     /region_name="SUZ"
                     /note="SUZ domain; pfam12752"
                     /db_xref="CDD:463689"
     Region          589..>818
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..843
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362021.1:474..3005"
                     /note="isoform 8 is encoded by transcript variant 31"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqesih lqlssfpslq eedksrkdds erekekdknr
      121 eklserpkir mlskdcsqey tdstgidlhg flintlknns rdrmillkme qemidfiads
      181 nnhykkfpqm ssyqrmlvhr vaayfgldhn vdqtgksvii nktsstripe qrfcehlkde
      241 kseesqkrfi lkrdnssidk ednqqnrmhp frddrrsksi eereeeyqrv rerifahdsv
      301 csqeslfldn srlqedmhic netykkrqlf rahrdssgrt sgsrqssset elrwpdhqra
      361 wsstdsdssn rnlkptmtkt asfggitvlt rgdstsstrs agklsktgse ssssagssgs
      421 lsrthpqsta ltssvaagsp gcmaysengm ggqvppssts yillplesat gippgsilln
      481 phtgqpfvnp dgtpaiynpp gsqqtlrgtv ggqpqqppqq qpspqpqqqv qasqpqmagp
      541 lvtqsvqslq pssqsvqypa vsfppqhllp msptqhfplr eelaaqfsql smsrqssgdt
      601 peppsgtvyp asllpqtaqp qsyvitsagq qlstggfsds gppisqqvlq appspqgfvq
      661 qpppaqmsvy yypsgqypts tsqqyrplas vqysaqrsqq ipqttqqagy qpvlsgqqgf
      721 qgmmgvqqsa hsqgvmssqq gapvhgvmvs yptmssyqvp mtqgsqavpq qtyqppimlp
      781 sqagqgslpa tgmpvycnvt ppnpqnnlrl mgphcpsstv pvmsascrtn cgnvsnagwq
      841 vkf
//
LOCUS       NP_001349658             907 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 62 isoform 2 [Mus musculus].
ACCESSION   NP_001349658 XP_006533266
VERSION     NP_001349658.1
DBSOURCE    REFSEQ: accession NM_001362729.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Choi,M.Y., Romer,A.I., Hu,M., Lepourcelet,M., Mechoor,A.,
            Yesilaltay,A., Krieger,M., Gray,P.A. and Shivdasani,R.A.
  TITLE     A dynamic expression survey identifies transcription factors
            relevant in mouse digestive tract development
  JOURNAL   Development 133 (20), 4119-4129 (2006)
   PUBMED   16971476
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Hunt,C.R., Parsian,A.J. and Kozak,C.A.
  TITLE     Genetic mapping of mouse heat shock protein genes Hsc4a to
            chromosome 11 and Hsc74 to chromosome 18 and two Hsc74 pseudogenes
            to chromosomes X and 8
  JOURNAL   Genomics 56 (3), 358-360 (1999)
   PUBMED   10087208
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Agata,Y., Matsuda,E. and Shimizu,A.
  TITLE     Rapid and efficient cloning of cDNAs encoding Kruppel-like zinc
            finger proteins by degenerate PCR
  JOURNAL   Gene 213 (1-2), 55-64 (1998)
   PUBMED   9630514
REFERENCE   5  (residues 1 to 907)
  AUTHORS   Polimeni,M., Giorgi,S., De Gregorio,L., Dragani,T.A., Molinaro,M.,
            Cossu,G. and Bouche,M.
  TITLE     Differentiation dependent expression in muscle cells of ZT3, a
            novel zinc finger factor differentially expressed in embryonic and
            adult tissues
  JOURNAL   Mech Dev 54 (1), 107-117 (1996)
   PUBMED   8808410
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Danciger,M., Brady,J., Adamson,M.C., Farber,D.B., Piatigorsky,J.
            and Kozak,C.A.
  TITLE     Chromosomal localization of the genes for five zinc finger proteins
            expressed in mouse lens
  JOURNAL   Genomics 28 (1), 39-43 (1995)
   PUBMED   7590745
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606829.13 and BE635021.1.
            
            On Apr 26, 2018 this sequence version replaced XP_006533266.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: CK639846.1, SRR11927932.3249264.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN01164131, SAMN01164134 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 29.23 cM"
     Protein         1..907
                     /product="zinc finger protein 62 isoform 2"
                     /note="ZT3"
                     /calculated_mol_wt=103856
     Region          120..535
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          126..146
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          154..174
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          182..202
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..230
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(215,217,219,221..222,225..226,229,243,245,249..250,
                     253..254,257,271,273,275,277..278,281..282,285)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          238..258
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          266..286
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          294..314
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          322..342
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(327,329,331,333..334,337..338,341,355,357,361..362,
                     365..366,369,383,385,387,389..390,393..394,397)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          350..370
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <372..451
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          378..398
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          406..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          430..843
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          434..454
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(439,441,443,445..446,449..450,453,467,469,473..474,
                     477..478,481,495,497,499,501..502,505..506,509)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          462..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          490..510
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          602..622
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(607,609,611,613..614,617..618,621,635,637,641..642,
                     645..646,649,663,665,667,669..670,673..674,677)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          630..650
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          658..678
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          686..706
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(691,693,695,697..698,701..702,705,719,721,725..726,
                     729..730,733,747,749,751,753..754,757..758,761)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          714..734
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          742..762
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          770..790
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          798..817
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          825..845
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..907
                     /gene="Zfp62"
                     /coded_by="NM_001362729.1:499..3222"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS24601.1"
                     /db_xref="GeneID:22720"
                     /db_xref="MGI:MGI:99662"
ORIGIN      
        1 medeesskkn endsnadsqc psvgffhkdh mqksktgdtc dlfpkwkilk egkssiremi
       61 dthtnaanik leqddetsek sfypstntmh qtiptepnct kqgehtenin gnvhpahiad
      121 kklhkcdecg ksfkynsrlv qhkimhtgek ryecddcrgt frsssslrvh krihtgekpy
      181 kcdecgkaym sysslinhks thsgeknckc decgksfnys svldqhkrih tgekpyecge
      241 cgkafrnssg lrvhkrihtg ekpyecdtcg ktfsnssglr vhkrihtgek pyecdecgka
      301 fitcrtllnh ksihfgdkpy kcdeceksfn ysslliqhkv ihtgekpyec decgkafrns
      361 sglivhkrih tgekpykcdi cgkafsyssg lavhksihpg kkaheckdcg ksfsynslll
      421 qhktihtger pyvcdvcgkt frnnsglkvh rrlhtgekpy kcdvcgkayi srsslknhkg
      481 ihmgekpykc syceksfnys saleqhkrih trekpfgcde cgkafrnnsg lkvhkrihtg
      541 erpykceecg kayislssli nhksvhpgek pfkcdeceka fityrtllnh kkihlgekpy
      601 kcdvceksfn ytsllsqhkr vhtrekpfec drcekvfrnn sslkvhkrih tgekpyecdi
      661 cgkayishss linhksthpg ktsytcdecg kaffssrtli shkrvhlgek pfkcvecgks
      721 fsyssllsqh krihtgekpy vcdwcgkafr nssgltvhkr ihtgekpygc decekayish
      781 sslinhksvh rgkqpyncec gksfnyrsvl dqhkrihtgk kpyrcndcgk afnirsnltk
      841 hkrihtgees lnmanmeshs gtfqkmiyye ggnsldgtrm qmpvweaeha ksqrnqieek
      901 lyeynnf
//
LOCUS       NP_689556                384 aa            linear   PRI 27-APR-2025
DEFINITION  spermatogenesis-associated protein 32 [Homo sapiens].
ACCESSION   NP_689556
VERSION     NP_689556.2
DBSOURCE    REFSEQ: accession NM_152343.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Casabonne,D., Reina,O., Benavente,Y., Becker,N., Maynadie,M.,
            Foretova,L., Cocco,P., Gonzalez-Neira,A., Nieters,A., Boffetta,P.,
            Middeldorp,J.M. and de Sanjose,S.
  TITLE     Single nucleotide polymorphisms of matrix metalloproteinase 9
            (MMP9) and tumor protein 73 (TP73) interact with Epstein-Barr virus
            in chronic lymphocytic leukemia: results from the European
            case-control study EpiLymph
  JOURNAL   Haematologica 96 (2), 323-327 (2011)
   PUBMED   21048031
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Lee,K.F., Tam,Y.T., Zuo,Y., Cheong,A.W., Pang,R.T., Lee,N.P.,
            Shum,C.K., Tam,P.C., Cheung,A.N., Yang,Z.M., Yeung,W.S. and
            Luk,J.M.
  TITLE     Characterization of an acrosome protein VAD1.2/AEP2 which is
            differentially expressed in spermatogenesis
  JOURNAL   Mol Hum Reprod 14 (8), 465-474 (2008)
   PUBMED   18621766
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP369808.1, BP370574.1 and BC028124.1.
            
            On Jun 22, 2007 this sequence version replaced NP_689556.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028124.1, AK058143.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2144333 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331780.5/ ENSP00000331532.4
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..384
                     /product="spermatogenesis-associated protein 32"
                     /note="testis-expressed sequence 34 protein; testis
                     expressed 34; acrosome expressed 2; CTD-2020K17.4;
                     testis-expressed protein 34"
                     /calculated_mol_wt=42194
     Region          23..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LK8.3)"
     Region          138..384
                     /region_name="VAD1-2"
                     /note="Vitamin A-deficiency (VAD) rat model signalling;
                     pfam15310"
                     /db_xref="CDD:464635"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q66H17; propagated from
                     UniProtKB/Swiss-Prot (Q96LK8.3)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q66H17; propagated from
                     UniProtKB/Swiss-Prot (Q96LK8.3)"
     Region          211..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LK8.3)"
     Region          284..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LK8.3)"
     Region          340..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LK8.3)"
     CDS             1..384
                     /gene="SPATA32"
                     /gene_synonym="AEP2; C17orf46; TEX34; VAD1.2"
                     /coded_by="NM_152343.3:79..1233"
                     /db_xref="CCDS:CCDS32669.1"
                     /db_xref="GeneID:124783"
                     /db_xref="HGNC:HGNC:26349"
ORIGIN      
        1 mgvtgahgfp ccgkgsveva emrddlsqhq iqeeqelead mleqkpqlqv dldldpdpdp
       61 dpeleigqvp alleselypa lkleaeldte ansneesdfe epmqlvckie svhsnmglpt
      121 pqtfrpwsln sncrsfteen hvsachhsis aqtskhlfwa nkliqasehs lqrainmqln
      181 ngsagqpirs plreaiptna lcseeqlqip dahsapptts sqapspllss dlpppidlte
      241 litfasslam asssrmdlps lehmmkappq ealepstepl lttveerepe nhaetlpekp
      301 rearaplksw sqedknfaqs yfdfskpgik ratikgqiql lqppatspll qgskedsvpp
      361 gkekenpllv kihfklsapt ipek
//
LOCUS       NP_114402                375 aa            linear   PRI 27-APR-2025
DEFINITION  protein NDRG3 isoform a [Homo sapiens].
ACCESSION   NP_114402
VERSION     NP_114402.1
DBSOURCE    REFSEQ: accession NM_032013.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Wang,X., Rong,S., Sun,Y., Yin,B., Yang,X., Lu,X., Sun,H., Yan,Y.,
            Sun,G., Liang,Y., Wang,P., Xie,S. and Li,Y.
  TITLE     NDRG3 regulates imatinib resistance by promoting beta-catenin
            accumulation in the nucleus in chronic myelogenous leukemia
  JOURNAL   Oncol Rep 50 (2) (2023)
   PUBMED   37350410
  REMARK    GeneRIF: NDRG3 regulates imatinib resistance by promoting
            beta-catenin accumulation in the nucleus in chronic myelogenous
            leukemia.
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Xu,Y., Kusuyama,J., Osana,S., Matsuhashi,S., Li,L., Takada,H.,
            Inada,H. and Nagatomi,R.
  TITLE     Lactate promotes neuronal differentiation of SH-SY5Y cells by
            lactate-responsive gene sets through NDRG3-dependent and
            -independent manners
  JOURNAL   J Biol Chem 299 (6), 104802 (2023)
   PUBMED   37172727
  REMARK    GeneRIF: Lactate promotes neuronal differentiation of SH-SY5Y cells
            by lactate-responsive gene sets through NDRG3-dependent and
            -independent manners.
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Liu,Y., Xia,J., Zhou,Y. and Shao,S.
  TITLE     High expression of NDRG3 correlates with poor prognosis in gastric
            cancer patients
  JOURNAL   Rev Esp Enferm Dig 113 (7), 524-528 (2021)
   PUBMED   33562989
  REMARK    GeneRIF: High expression of NDRG3 correlates with poor prognosis in
            gastric cancer patients.
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Ma,W., Zhao,X., Xue,N., Gao,Y. and Xu,Q.
  TITLE     The LINC01410/miR-122-5p/NDRG3 axis is involved in the
            proliferation and migration of osteosarcoma cells
  JOURNAL   IUBMB Life 73 (4), 705-717 (2021)
   PUBMED   33583123
  REMARK    GeneRIF: The LINC01410/miR-122-5p/NDRG3 axis is involved in the
            proliferation and migration of osteosarcoma cells.
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Kim,K.R., Kim,K.A., Park,J.S., Jang,J.Y., Choi,Y., Lee,H.H.,
            Lee,D.C., Park,K.C., Yeom,Y.I., Kim,H.J. and Han,B.W.
  TITLE     Structural and Biophysical Analyses of Human N-Myc
            Downstream-Regulated Gene 3 (NDRG3) Protein
  JOURNAL   Biomolecules 10 (1), 90 (2020)
   PUBMED   31935861
  REMARK    GeneRIF: Structural and Biophysical Analyses of Human N-Myc
            Downstream-Regulated Gene 3 (NDRG3) Protein.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Qu,X., Zhai,Y., Wei,H., Zhang,C., Xing,G., Yu,Y. and He,F.
  TITLE     Characterization and expression of three novel
            differentiation-related genes belong to the human NDRG gene family
  JOURNAL   Mol Cell Biochem 229 (1-2), 35-44 (2002)
   PUBMED   11936845
  REMARK    GeneRIF: Cloning and expression of the gene; highly expressed in
            brain and testis
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Zhao,W., Tang,R., Huang,Y., Wang,W., Zhou,Z., Gu,S., Dai,J.,
            Ying,K., Xie,Y. and Mao,Y.
  TITLE     Cloning and expression pattern of the human NDRG3 gene
  JOURNAL   Biochim Biophys Acta 1519 (1-2), 134-138 (2001)
   PUBMED   11406283
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Zhou,R.H., Kokame,K., Tsukamoto,Y., Yutani,C., Kato,H. and
            Miyata,T.
  TITLE     Characterization of the human NDRG gene family: a newly identified
            member, NDRG4, is specifically expressed in brain and heart
  JOURNAL   Genomics 73 (1), 86-97 (2001)
   PUBMED   11352569
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Kalaydjieva,L., Gresham,D., Gooding,R., Heather,L., Baas,F., de
            Jonge,R., Blechschmidt,K., Angelicheva,D., Chandler,D., Worsley,P.,
            Rosenthal,A., King,R.H. and Thomas,P.K.
  TITLE     N-myc downstream-regulated gene 1 is mutated in hereditary motor
            and sensory neuropathy-Lom
  JOURNAL   Am J Hum Genet 67 (1), 47-58 (2000)
   PUBMED   10831399
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL132768.15, AB044943.1, AF308609.1 and AA903471.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.265734.1,
                                           SRR1803617.275290.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000349004.6/ ENSP00000345292.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.23"
     Protein         1..375
                     /product="protein NDRG3 isoform a"
                     /note="protein NDRG3; N-myc downstream-regulated gene 3
                     protein"
                     /calculated_mol_wt=41278
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Region          32..317
                     /region_name="Ndr"
                     /note="Ndr family; pfam03096"
                     /db_xref="CDD:397285"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Region          326..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYF9; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UGV2.2)"
     CDS             1..375
                     /gene="NDRG3"
                     /coded_by="NM_032013.4:95..1222"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13285.1"
                     /db_xref="GeneID:57446"
                     /db_xref="HGNC:HGNC:14462"
                     /db_xref="MIM:605273"
ORIGIN      
        1 mdelqdvqlt eikpllndkn gtrnfqdfdc qehdietthg vvhvtirglp kgnrpvilty
       61 hdiglnhksc fnaffnfedm qeitqhfavc hvdapgqqeg apsfptgyqy ptmdelaeml
      121 ppvlthlslk siigigvgag ayilsrfaln hpelveglvl invdpcakgw idwaasklsg
      181 lttnvvdiil ahhfgqeelq anldliqtyr mhiaqdinqd nlqlflnsyn grrdleierp
      241 ilgqndnksk tlkcstllvv gdnspaveav vecnsrlnpi nttllkmadc gglpqvvqpg
      301 klteafkyfl qgmgyipsas mtrlarsrth stssslgsge spfsrsvtsn qsdgtqesce
      361 spdvldrhqt mevsc
//
LOCUS       NP_001926                766 aa            linear   PRI 27-APR-2025
DEFINITION  dipeptidyl peptidase 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001926
VERSION     NP_001926.2
DBSOURCE    REFSEQ: accession NM_001935.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Wesley,U.V. and Dempsey,R.J.
  TITLE     Neuro-molecular perspectives on long COVID-19 impacted
            cerebrovascular diseases - a role for dipeptidyl peptidase IV
  JOURNAL   Exp Neurol 380, 114890 (2024)
   PUBMED   39038507
  REMARK    GeneRIF: Neuro-molecular perspectives on long COVID-19 impacted
            cerebrovascular diseases - a role for dipeptidyl peptidase IV.
            Review article
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Shi,J., Hu,S., Wei,H., Zhang,L., Lan,Y., Guan,J., Zhao,K., Gao,F.,
            He,W. and Li,Z.
  TITLE     Dipeptidyl peptidase 4 interacts with porcine coronavirus PHEV
            spikes and mediates host range expansion
  JOURNAL   J Virol 98 (7), e0075324 (2024)
   PUBMED   38829136
  REMARK    GeneRIF: Dipeptidyl peptidase 4 interacts with porcine coronavirus
            PHEV spikes and mediates host range expansion.
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Hu,X., Jiang,C., Gu,Y. and Xue,X.
  TITLE     Exploring the conformational dynamics and key amino acids in the
            CD26-caveolin-1 interaction and potential therapeutic interventions
  JOURNAL   Medicine (Baltimore) 103 (22), e38367 (2024)
   PUBMED   39259075
  REMARK    GeneRIF: Exploring the conformational dynamics and key amino acids
            in the CD26-caveolin-1 interaction and potential therapeutic
            interventions.
REFERENCE   4  (residues 1 to 766)
  AUTHORS   Gnoth,K., Bar,J.W., Rosche,F., Rahfeld,J.U. and Demuth,H.U.
  TITLE     Contribution of amino acids in the active site of dipeptidyl
            peptidase 4 to the catalytic action of the enzyme
  JOURNAL   PLoS One 19 (4), e0289239 (2024)
   PUBMED   38625918
  REMARK    GeneRIF: Contribution of amino acids in the active site of
            dipeptidyl peptidase 4 to the catalytic action of the enzyme.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 766)
  AUTHORS   Iacobellis,G.
  TITLE     COVID-19 and diabetes: Can DPP4 inhibition play a role?
  JOURNAL   Diabetes Res Clin Pract 162, 108125 (2020)
   PUBMED   32224164
REFERENCE   6  (residues 1 to 766)
  AUTHORS   Vankadari,N. and Wilce,J.A.
  TITLE     Emerging WuHan (COVID-19) coronavirus: glycan shield and structure
            prediction of spike glycoprotein and its interaction with human
            CD26
  JOURNAL   Emerg Microbes Infect 9 (1), 601-604 (2020)
   PUBMED   32178593
  REMARK    GeneRIF: highlights the key finding that the S1 domain of COVID-19
            spike glycoprotein potentially interacts with the human CD26
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 766)
  AUTHORS   Imai,K., Maeda,M., Fujiwara,H., Kariya,M., Takakura,K., Kanzaki,H.
            and Mori,T.
  TITLE     Dipeptidyl peptidase IV as a differentiation marker of the human
            endometrial glandular cells
  JOURNAL   Hum Reprod 7 (9), 1189-1194 (1992)
   PUBMED   1362202
REFERENCE   8  (residues 1 to 766)
  AUTHORS   Misumi,Y., Hayashi,Y., Arakawa,F. and Ikehara,Y.
  TITLE     Molecular cloning and sequence analysis of human dipeptidyl
            peptidase IV, a serine proteinase on the cell surface
  JOURNAL   Biochim Biophys Acta 1131 (3), 333-336 (1992)
   PUBMED   1352704
REFERENCE   9  (residues 1 to 766)
  AUTHORS   Tanaka,T., Camerini,D., Seed,B., Torimoto,Y., Dang,N.H.,
            Kameoka,J., Dahlberg,H.N., Schlossman,S.F. and Morimoto,C.
  TITLE     Cloning and functional expression of the T cell activation antigen
            CD26
  JOURNAL   J Immunol 149 (2), 481-486 (1992)
   PUBMED   1352530
  REMARK    Erratum:[J Immunol. 1993 Mar 1;150(5):2090. PMID: 8094732]
REFERENCE   10 (residues 1 to 766)
  AUTHORS   Darmoul,D., Lacasa,M., Baricault,L., Marguet,D., Sapin,C.,
            Trotot,P., Barbat,A. and Trugnan,G.
  TITLE     Dipeptidyl peptidase IV (CD 26) gene expression in enterocyte-like
            colon cancer cell lines HT-29 and Caco-2. Cloning of the complete
            human coding sequence and changes of dipeptidyl peptidase IV mRNA
            levels during cell differentiation
  JOURNAL   J Biol Chem 267 (7), 4824-4833 (1992)
   PUBMED   1347043
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC065265.1.
            
            On Feb 19, 2002 this sequence version replaced NP_001926.1.
            
            Summary: The DPP4 gene encodes dipeptidyl peptidase 4, which is
            identical to adenosine deaminase complexing protein-2, and to the
            T-cell activation antigen CD26. It is an intrinsic type II
            transmembrane glycoprotein and a serine exopeptidase that cleaves
            X-proline dipeptides from the N-terminus of polypeptides.
            Dipeptidyl peptidase 4 is highly involved in glucose and insulin
            metabolism, as well as in immune regulation. This protein was shown
            to be a functional receptor for Middle East respiratory syndrome
            coronavirus (MERS-CoV), and protein modeling suggests that it may
            play a similar role with SARS-CoV-2, the virus responsible for
            COVID-19. [provided by RefSeq, Apr 2020].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065265.1, X60708.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in SARS-CoV-2 infection
            MANE Ensembl match     :: ENST00000360534.8/ ENSP00000353731.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.2"
     Protein         1..766
                     /product="dipeptidyl peptidase 4 isoform 1"
                     /EC_number="3.4.14.5"
                     /note="dipeptidylpeptidase IV (CD26, adenosine deaminase
                     complexing protein 2); T-cell activation antigen CD26;
                     dipeptidylpeptidase 4; ADCP-2; DPP IV; dipeptidyl
                     peptidase IV; Gly-Pro naphthylamidase;
                     Xaa-Pro-dipeptidylaminopeptidase; Post-proline dipeptidyl
                     aminopeptidase IV"
                     /calculated_mol_wt=88148
     Site            7..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P27487.2)"
     Region          38..58
                     /region_name="DPPIV_rep"
                     /note="Dipeptidyl peptidase IV (DPP IV) low complexity
                     region; pfam18811"
                     /db_xref="CDD:465875"
     mat_peptide     39..766
                     /product="Dipeptidyl peptidase 4 soluble form.
                     /id=PRO_0000027214"
                     /note="propagated from UniProtKB/Swiss-Prot (P27487.2)"
                     /calculated_mol_wt=84377
     Site            85
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12483204,
                     ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826,
                     ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475,
                     ECO:0007744|PDB:4L72; propagated from UniProtKB/Swiss-Prot
                     (P27487.2)"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475,
                     ECO:0007744|PDB:4L72; propagated from UniProtKB/Swiss-Prot
                     (P27487.2)"
     Region          108..478
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Site            150
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12483204,
                     ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475,
                     ECO:0007744|PDB:4L72; propagated from UniProtKB/Swiss-Prot
                     (P27487.2)"
     Site            219
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12483204,
                     ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603,
                     ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72;
                     propagated from UniProtKB/Swiss-Prot (P27487.2)"
     Site            229
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12483204,
                     ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826,
                     ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475,
                     ECO:0007744|PDB:4L72; propagated from UniProtKB/Swiss-Prot
                     (P27487.2)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12483204,
                     ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826,
                     ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72;
                     propagated from UniProtKB/Swiss-Prot (P27487.2)"
     Site            321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12483204,
                     ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475,
                     ECO:0007744|PDB:4L72; propagated from UniProtKB/Swiss-Prot
                     (P27487.2)"
     Site            520
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12483204,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475,
                     ECO:0007744|PDB:4L72; propagated from UniProtKB/Swiss-Prot
                     (P27487.2)"
     Region          559..763
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     Site            685
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P27487.2)"
     CDS             1..766
                     /gene="DPP4"
                     /gene_synonym="ADABP; ADCP2; CD26; DPPIV; TP103"
                     /coded_by="NM_001935.4:235..2535"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2216.1"
                     /db_xref="GeneID:1803"
                     /db_xref="HGNC:HGNC:3009"
                     /db_xref="MIM:102720"
ORIGIN      
        1 mktpwkvllg llgaaalvti itvpvvllnk gtddatadsr ktytltdylk ntyrlklysl
       61 rwisdheyly kqennilvfn aeygnssvfl enstfdefgh sindysispd gqfilleyny
      121 vkqwrhsyta sydiydlnkr qliteeripn ntqwvtwspv ghklayvwnn diyvkiepnl
      181 psyritwtgk ediiyngitd wvyeeevfsa ysalwwspng tflayaqfnd tevplieysf
      241 ysdeslqypk tvrvpypkag avnptvkffv vntdslssvt natsiqitap asmligdhyl
      301 cdvtwatqer islqwlrriq nysvmdicdy dessgrwncl varqhiemst tgwvgrfrps
      361 ephftldgns fykiisneeg yrhicyfqid kkdctfitkg twevigieal tsdylyyisn
      421 eykgmpggrn lykiqlsdyt kvtclsceln percqyysvs fskeakyyql rcsgpglply
      481 tlhssvndkg lrvlednsal dkmlqnvqmp skkldfiiln etkfwyqmil pphfdkskky
      541 pllldvyagp csqkadtvfr lnwatylast eniivasfdg rgsgyqgdki mhainrrlgt
      601 fevedqieaa rqfskmgfvd nkriaiwgws yggyvtsmvl gsgsgvfkcg iavapvsrwe
      661 yydsvytery mglptpednl dhyrnstvms raenfkqvey llihgtaddn vhfqqsaqis
      721 kalvdvgvdf qamwytdedh giasstahqh iythmshfik qcfslp
//
LOCUS       NP_002889                407 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding motif, single-stranded-interacting protein 2 isoform 1
            [Homo sapiens].
ACCESSION   NP_002889
VERSION     NP_002889.1
DBSOURCE    REFSEQ: accession NM_002898.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Sun,X., Hu,Y., Wu,J., Shi,L., Zhu,L., Xi,P.W., Wei,J.F. and Ding,Q.
  TITLE     RBMS2 inhibits the proliferation by stabilizing P21 mRNA in breast
            cancer
  JOURNAL   J Exp Clin Cancer Res 37 (1), 298 (2018)
   PUBMED   30514345
  REMARK    GeneRIF: RBMS2 acts as a tumor suppressor in breast cancer and
            positively regulated the expression of P21 by stabilizing its mRNA.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Dastani,Z., Hivert,M.F., Timpson,N., Perry,J.R., Yuan,X.,
            Scott,R.A., Henneman,P., Heid,I.M., Kizer,J.R., Lyytikainen,L.P.,
            Fuchsberger,C., Tanaka,T., Morris,A.P., Small,K., Isaacs,A.,
            Beekman,M., Coassin,S., Lohman,K., Qi,L., Kanoni,S., Pankow,J.S.,
            Uh,H.W., Wu,Y., Bidulescu,A., Rasmussen-Torvik,L.J.,
            Greenwood,C.M., Ladouceur,M., Grimsby,J., Manning,A.K., Liu,C.T.,
            Kooner,J., Mooser,V.E., Vollenweider,P., Kapur,K.A., Chambers,J.,
            Wareham,N.J., Langenberg,C., Frants,R., Willems-Vandijk,K.,
            Oostra,B.A., Willems,S.M., Lamina,C., Winkler,T.W., Psaty,B.M.,
            Tracy,R.P., Brody,J., Chen,I., Viikari,J., Kahonen,M.,
            Pramstaller,P.P., Evans,D.M., St Pourcain,B., Sattar,N., Wood,A.R.,
            Bandinelli,S., Carlson,O.D., Egan,J.M., Bohringer,S., van
            Heemst,D., Kedenko,L., Kristiansson,K., Nuotio,M.L., Loo,B.M.,
            Harris,T., Garcia,M., Kanaya,A., Haun,M., Klopp,N., Wichmann,H.E.,
            Deloukas,P., Katsareli,E., Couper,D.J., Duncan,B.B.,
            Kloppenburg,M., Adair,L.S., Borja,J.B., Wilson,J.G., Musani,S.,
            Guo,X., Johnson,T., Semple,R., Teslovich,T.M., Allison,M.A.,
            Redline,S., Buxbaum,S.G., Mohlke,K.L., Meulenbelt,I.,
            Ballantyne,C.M., Dedoussis,G.V., Hu,F.B., Liu,Y., Paulweber,B.,
            Spector,T.D., Slagboom,P.E., Ferrucci,L., Jula,A., Perola,M.,
            Raitakari,O., Florez,J.C., Salomaa,V., Eriksson,J.G.,
            Frayling,T.M., Hicks,A.A., Lehtimaki,T., Smith,G.D.,
            Siscovick,D.S., Kronenberg,F., van Duijn,C., Loos,R.J.,
            Waterworth,D.M., Meigs,J.B., Dupuis,J., Richards,J.B., Voight,B.F.,
            Scott,L.J., Steinthorsdottir,V., Dina,C., Welch,R.P., Zeggini,E.,
            Huth,C., Aulchenko,Y.S., Thorleifsson,G., McCulloch,L.J.,
            Ferreira,T., Grallert,H., Amin,N., Wu,G., Willer,C.J.,
            Raychaudhuri,S., McCarroll,S.A., Hofmann,O.M., Segre,A.V., van
            Hoek,M., Navarro,P., Ardlie,K., Balkau,B., Benediktsson,R.,
            Bennett,A.J., Blagieva,R., Boerwinkle,E., Bonnycastle,L.L.,
            Bostrom,K.B., Bravenboer,B., Bumpstead,S., Burtt,N.P.,
            Charpentier,G., Chines,P.S., Cornelis,M., Crawford,G., Doney,A.S.,
            Elliott,K.S., Elliott,A.L., Erdos,M.R., Fox,C.S., Franklin,C.S.,
            Ganser,M., Gieger,C., Grarup,N., Green,T., Griffin,S., Groves,C.J.,
            Guiducci,C., Hadjadj,S., Hassanali,N., Herder,C., Isomaa,B.,
            Jackson,A.U., Johnson,P.R., Jorgensen,T., Kao,W.H., Kong,A.,
            Kraft,P., Kuusisto,J., Lauritzen,T., Li,M., Lieverse,A.,
            Lindgren,C.M., Lyssenko,V., Marre,M., Meitinger,T., Midthjell,K.,
            Morken,M.A., Narisu,N., Nilsson,P., Owen,K.R., Payne,F.,
            Petersen,A.K., Platou,C., Proenca,C., Prokopenko,I., Rathmann,W.,
            Rayner,N.W., Robertson,N.R., Rocheleau,G., Roden,M., Sampson,M.J.,
            Saxena,R., Shields,B.M., Shrader,P., Sigurdsson,G., Sparso,T.,
            Strassburger,K., Stringham,H.M., Sun,Q., Swift,A.J., Thorand,B.,
            Tichet,J., Tuomi,T., van Dam,R.M., van Haeften,T.W., van Herpt,T.,
            van Vliet-Ostaptchouk,J.V., Walters,G.B., Weedon,M.N., Wijmenga,C.,
            Witteman,J., Bergman,R.N., Cauchi,S., Collins,F.S., Gloyn,A.L.,
            Gyllensten,U., Hansen,T., Hide,W.A., Hitman,G.A., Hofman,A.,
            Hunter,D.J., Hveem,K., Laakso,M., Morris,A.D., Palmer,C.N.,
            Rudan,I., Sijbrands,E., Stein,L.D., Tuomilehto,J., Uitterlinden,A.,
            Walker,M., Watanabe,R.M., Abecasis,G.R., Boehm,B.O., Campbell,H.,
            Daly,M.J., Hattersley,A.T., Pedersen,O., Barroso,I., Groop,L.,
            Sladek,R., Thorsteinsdottir,U., Wilson,J.F., Illig,T., Froguel,P.,
            van Duijn,C.M., Stefansson,K., Altshuler,D., Boehnke,M.,
            McCarthy,M.I., Soranzo,N., Wheeler,E., Glazer,N.L.,
            Bouatia-Naji,N., Magi,R., Randall,J., Elliott,P., Rybin,D.,
            Dehghan,A., Hottenga,J.J., Song,K., Goel,A., Lajunen,T., Doney,A.,
            Cavalcanti-Proenca,C., Kumari,M., Timpson,N.J., Zabena,C.,
            Ingelsson,E., An,P., O'Connell,J., Luan,J., Elliott,A.,
            McCarroll,S.A., Roccasecca,R.M., Pattou,F., Sethupathy,P.,
            Ariyurek,Y., Barter,P., Beilby,J.P., Ben-Shlomo,Y., Bergmann,S.,
            Bochud,M., Bonnefond,A., Borch-Johnsen,K., Bottcher,Y., Brunner,E.,
            Bumpstead,S.J., Chen,Y.D., Chines,P., Clarke,R., Coin,L.J.,
            Cooper,M.N., Crisponi,L., Day,I.N., de Geus,E.J., Delplanque,J.,
            Fedson,A.C., Fischer-Rosinsky,A., Forouhi,N.G., Franzosi,M.G.,
            Galan,P., Goodarzi,M.O., Graessler,J., Grundy,S., Gwilliam,R.,
            Hallmans,G., Hammond,N., Han,X., Hartikainen,A.L., Hayward,C.,
            Heath,S.C., Hercberg,S., Hillman,D.R., Hingorani,A.D., Hui,J.,
            Hung,J., Kaakinen,M., Kaprio,J., Kesaniemi,Y.A., Kivimaki,M.,
            Knight,B., Koskinen,S., Kovacs,P., Kyvik,K.O., Lathrop,G.M.,
            Lawlor,D.A., Le Bacquer,O., Lecoeur,C., Li,Y., Mahley,R.,
            Mangino,M., Martinez-Larrad,M.T., McAteer,J.B., McPherson,R.,
            Meisinger,C., Melzer,D., Meyre,D., Mitchell,B.D., Mukherjee,S.,
            Naitza,S., Neville,M.J., Orru,M., Pakyz,R., Paolisso,G.,
            Pattaro,C., Pearson,D., Peden,J.F., Pedersen,N.L., Pfeiffer,A.F.,
            Pichler,I., Polasek,O., Posthuma,D., Potter,S.C., Pouta,A.,
            Province,M.A., Rayner,N.W., Rice,K., Ripatti,S., Rivadeneira,F.,
            Rolandsson,O., Sandbaek,A., Sandhu,M., Sanna,S., Sayer,A.A.,
            Scheet,P., Seedorf,U., Sharp,S.J., Shields,B., Sigurethsson,G.,
            Sijbrands,E.J., Silveira,A., Simpson,L., Singleton,A., Smith,N.L.,
            Sovio,U., Swift,A., Syddall,H., Syvanen,A.C., Tonjes,A.,
            Uitterlinden,A.G., van Dijk,K.W., Varma,D., Visvikis-Siest,S.,
            Vitart,V., Vogelzangs,N., Waeber,G., Wagner,P.J., Walley,A.,
            Ward,K.L., Watkins,H., Wild,S.H., Willemsen,G., Witteman,J.C.,
            Yarnell,J.W., Zelenika,D., Zethelius,B., Zhai,G., Zhao,J.H.,
            Zillikens,M.C., Borecki,I.B., Meneton,P., Magnusson,P.K.,
            Nathan,D.M., Williams,G.H., Silander,K., Bornstein,S.R.,
            Schwarz,P., Spranger,J., Karpe,F., Shuldiner,A.R., Cooper,C.,
            Serrano-Rios,M., Lind,L., Palmer,L.J., Hu,F.B. 1st, Franks,P.W.,
            Ebrahim,S., Marmot,M., Kao,W.H., Pramstaller,P.P., Wright,A.F.,
            Stumvoll,M., Hamsten,A., Buchanan,T.A., Valle,T.T., Rotter,J.I.,
            Penninx,B.W., Boomsma,D.I., Cao,A., Scuteri,A., Schlessinger,D.,
            Uda,M., Ruokonen,A., Jarvelin,M.R., Peltonen,L., Mooser,V.,
            Sladek,R., Musunuru,K., Smith,A.V., Edmondson,A.C., Stylianou,I.M.,
            Koseki,M., Pirruccello,J.P., Chasman,D.I., Johansen,C.T.,
            Fouchier,S.W., Peloso,G.M., Barbalic,M., Ricketts,S.L., Bis,J.C.,
            Feitosa,M.F., Orho-Melander,M., Melander,O., Li,X., Li,M.,
            Cho,Y.S., Go,M.J., Kim,Y.J., Lee,J.Y., Park,T., Kim,K., Sim,X.,
            Ong,R.T., Croteau-Chonka,D.C., Lange,L.A., Smith,J.D., Ziegler,A.,
            Zhang,W., Zee,R.Y., Whitfield,J.B., Thompson,J.R., Surakka,I.,
            Spector,T.D., Smit,J.H., Sinisalo,J., Scott,J., Saharinen,J.,
            Sabatti,C., Rose,L.M., Roberts,R., Rieder,M., Parker,A.N., Pare,G.,
            O'Donnell,C.J., Nieminen,M.S., Nickerson,D.A., Montgomery,G.W.,
            McArdle,W., Masson,D., Martin,N.G., Marroni,F., Lucas,G., Luben,R.,
            Lokki,M.L., Lettre,G., Launer,L.J., Lakatta,E.G., Laaksonen,R.,
            Kyvik,K.O., Konig,I.R., Khaw,K.T., Kaplan,L.M., Johansson,A.,
            Janssens,A.C., Igl,W., Hovingh,G.K., Hengstenberg,C.,
            Havulinna,A.S., Hastie,N.D., Harris,T.B., Haritunians,T.,
            Hall,A.S., Groop,L.C., Gonzalez,E., Freimer,N.B., Erdmann,J.,
            Ejebe,K.G., Doring,A., Dominiczak,A.F., Demissie,S., Deloukas,P.,
            de Faire,U., Crawford,G., Chen,Y.D., Caulfield,M.J.,
            Boekholdt,S.M., Assimes,T.L., Quertermous,T., Seielstad,M.,
            Wong,T.Y., Tai,E.S., Feranil,A.B., Kuzawa,C.W., Taylor,H.A. Jr.,
            Gabriel,S.B., Holm,H., Gudnason,V., Krauss,R.M., Ordovas,J.M.,
            Munroe,P.B., Kooner,J.S., Tall,A.R., Hegele,R.A., Kastelein,J.J.,
            Schadt,E.E., Strachan,D.P., Reilly,M.P., Samani,N.J., Schunkert,H.,
            Cupples,L.A., Sandhu,M.S., Ridker,P.M., Rader,D.J. and
            Kathiresan,S.
  CONSRTM   DIAGRAM+ Consortium; MAGIC Consortium; GLGC Investigators; MuTHER
            Consortium; DIAGRAM Consortium; GIANT Consortium; Global B Pgen
            Consortium; Procardis Consortium; MAGIC investigators; GLGC
            Consortium
  TITLE     Novel loci for adiponectin levels and their influence on type 2
            diabetes and metabolic traits: a multi-ethnic meta-analysis of
            45,891 individuals
  JOURNAL   PLoS Genet 8 (3), e1002607 (2012)
   PUBMED   22479202
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Silva,J.M., Perez,D.S., Pritchett,J.R., Halling,M.L., Tang,H. and
            Smith,D.I.
  TITLE     Identification of long stress-induced non-coding transcripts that
            have altered expression in cancer
  JOURNAL   Genomics 95 (6), 355-362 (2010)
   PUBMED   20214974
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Kanaoka,Y. and Nojima,H.
  TITLE     SCR: novel human suppressors of cdc2/cdc13 mutants of
            Schizosaccharomyces pombe harbour motifs for RNA binding proteins
  JOURNAL   Nucleic Acids Res 22 (13), 2687-2693 (1994)
   PUBMED   8041632
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Skerka,C., Timmann,C., Horstmann,R.D. and Zipfel,P.F.
  TITLE     Two additional human serum proteins structurally related to
            complement factor H. Evidence for a family of factor H-related
            genes
  JOURNAL   J Immunol 148 (10), 3313-3318 (1992)
   PUBMED   1533657
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC097104.18, DC382164.1,
            BC027863.1, AC090681.13 and CF890834.1.
            
            Summary: The protein encoded by this gene is a member of a small
            family of proteins which bind single stranded DNA/RNA. These
            proteins are characterized by the presence of two sets of
            ribonucleoprotein consensus sequence (RNP-CS) that contain
            conserved motifs, RNP1 and RNP2, originally described in RNA
            binding proteins, and required for DNA binding. The RBMS proteins
            have been implicated in such diverse functions as DNA replication,
            gene transcription, cell cycle progression and apoptosis. This
            protein was isolated by phenotypic complementation of cdc2 and
            cdc13 mutants of yeast and is thought to suppress cdc2 and cdc13
            mutants through the induction of translation of cdc2. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC027863.1, SRR1803611.80591.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262031.10/ ENSP00000262031.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..407
                     /product="RNA-binding motif, single-stranded-interacting
                     protein 2 isoform 1"
                     /note="suppressor of CDC2 with RNA-binding motif 3"
                     /calculated_mol_wt=43828
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q15434.1)"
     Region          29..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15434.1)"
     Region          51..134
                     /region_name="RRM1_MSSP2"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     single-stranded DNA-binding protein MSSP-2; cd12471"
                     /db_xref="CDD:409901"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15434.1)"
     Region          135..220
                     /region_name="RRM2_MSSP2"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     single-stranded DNA-binding protein MSSP-2; cd12474"
                     /db_xref="CDD:409904"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15434.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15434.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15434.1)"
     CDS             1..407
                     /gene="RBMS2"
                     /gene_synonym="SCR3"
                     /coded_by="NM_002898.4:205..1428"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8923.1"
                     /db_xref="GeneID:5939"
                     /db_xref="HGNC:HGNC:9909"
                     /db_xref="MIM:602387"
ORIGIN      
        1 mllsvtsrpg istfgynrnn kkpyvslaqq mappspsnst pnsssgsngn dqlsktnlyi
       61 rglqpgttdq dlvklcqpyg kivstkaild kttnkckgyg fvdfdspsaa qkavtalkas
      121 gvqaqmakqq eqdptnlyis nlplsmdeqe legmlkpfgq vistrilrdt sgtsrgvgfa
      181 rmestekcea iithfngkyi ktppgvpaps dpllckfadg gpkkrqnqgk fvqngrawpr
      241 nadmgvmalt ydpttalqng fypapynitp nrmlaqsals pylsspvssy qrvtqtsplq
      301 vpnpswmhhh sylmqpsgsv ltpgmdhpis lqpasmmgpl tqqlghlsls stgtymptaa
      361 amqgayisqy tpvpsssvsv eessgqqnqv avdapsehgv ysfqfnk
//
LOCUS       NP_001117                456 aa            linear   PRI 27-APR-2025
DEFINITION  adenylosuccinate synthetase isozyme 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001117
VERSION     NP_001117.2
DBSOURCE    REFSEQ: accession NM_001126.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Baresova,V., Krijt,M., Skopova,V., Souckova,O., Kmoch,S. and
            Zikanova,M.
  TITLE     CRISPR-Cas9 induced mutations along de novo purine synthesis in
            HeLa cells result in accumulation of individual enzyme substrates
            and affect purinosome formation
  JOURNAL   Mol Genet Metab 119 (3), 270-277 (2016)
   PUBMED   27590927
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Chen,K., Ma,H., Li,L., Zang,R., Wang,C., Song,F., Shi,T., Yu,D.,
            Yang,M., Xue,W., Dai,J., Li,S., Zheng,H., Wu,C., Zhang,Y., Wu,X.,
            Li,D., Xue,F., Li,H., Jiang,Z., Liu,J., Liu,Y., Li,P., Tan,W.,
            Han,J., Jie,J., Hao,Q., Hu,Z., Lin,D., Ma,D., Jia,W., Shen,H. and
            Wei,Q.
  TITLE     Genome-wide association study identifies new susceptibility loci
            for epithelial ovarian cancer in Han Chinese women
  JOURNAL   Nat Commun 5, 4682 (2014)
   PUBMED   25134534
  REMARK    Erratum:[Nat Commun. 2014;5:5828]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Stepinski,J., Pawelczyk,T., Bizon,D. and Angielski,S.
  TITLE     Purine nucleotide cycle in rat renal cortex and medulla under
            conditions that mimic normal and low oxygen supply
  JOURNAL   Kidney Int 50 (4), 1195-1201 (1996)
   PUBMED   8887278
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Powell,S.M., Zalkin,H. and Dixon,J.E.
  TITLE     Cloning and characterization of the cDNA encoding human
            adenylosuccinate synthetase
  JOURNAL   FEBS Lett 303 (1), 4-10 (1992)
   PUBMED   1592113
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Zalkin,H. and Dixon,J.E.
  TITLE     De novo purine nucleotide biosynthesis
  JOURNAL   Prog Nucleic Acid Res Mol Biol 42, 259-287 (1992)
   PUBMED   1574589
  REMARK    Review article
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Lai,L.W., Hart,I.M. and Patterson,D.
  TITLE     A gene correcting the defect in the CHO mutant Ade -H, deficient in
            a branch point enzyme (adenylosuccinate synthetase) of de novo
            purine biosynthesis, is located on the long arm of chromosome 1
  JOURNAL   Genomics 9 (2), 322-328 (1991)
   PUBMED   2004783
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Ogawa,H., Shiraki,H., Matsuda,Y. and Nakagawa,H.
  TITLE     Interaction of adenylosuccinate synthetase with F-actin
  JOURNAL   Eur J Biochem 85 (2), 331-337 (1978)
   PUBMED   648524
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Van der Weyden,M.B. and Kelly,W.N.
  TITLE     Human adenylosuccinate synthetase. Partial purification, kinetic
            and regulatory properties of the enzyme from placenta
  JOURNAL   J Biol Chem 249 (22), 7282-7289 (1974)
   PUBMED   4436310
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012356.1 and AL645465.15.
            
            On Sep 11, 2003 this sequence version replaced NP_001117.1.
            
            Summary: This gene encodes the enzyme adenylosuccinate synthetase
            which catalyzes the first committed step in the conversion of
            inosine monophosphate to adenosine monophosphate. A pseudogene of
            this gene is found on chromosome 17.[provided by RefSeq, Nov 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012356.1, GQ900992.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366535.4/ ENSP00000355493.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..456
                     /product="adenylosuccinate synthetase isozyme 2 isoform 1"
                     /EC_number="6.3.4.4"
                     /note="adenylosuccinate synthetase, acidic isozyme;
                     IMP--aspartate ligase 2; adenylosuccinate synthetase
                     (Ade(-)H-complementing); L-type adenylosuccinate
                     synthetase; adenylosuccinate synthetase, liver isozyme;
                     AMPSase 2; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=49966
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30520.3)"
     Region          32..453
                     /region_name="Adenylsucc_synt"
                     /note="Adenylosuccinate synthetase; pfam00709"
                     /db_xref="CDD:459912"
     CDS             1..456
                     /gene="ADSS2"
                     /gene_synonym="ADEH; ADSS; ADSS 2"
                     /coded_by="NM_001126.5:93..1463"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1624.1"
                     /db_xref="GeneID:159"
                     /db_xref="HGNC:HGNC:292"
                     /db_xref="MIM:103060"
ORIGIN      
        1 mafaetypaa sslpngdcgr prarpggnrv tvvlgaqwgd egkgkvvdll aqdadivcrc
       61 qggnnaghtv vvdsveydfh llpsgiinpn vtafigngvv ihlpglfeea eknvqkgkgl
      121 egwekrliis drahivfdfh qaadgiqeqq rqeqagknlg ttkkgigpvy sskaarsglr
      181 mcdlvsdfdg fserfkvlan qyksiyptle idiegelqkl kgymekikpm vrdgvyflye
      241 alhgppkkil veganaalld idfgtypfvt ssnctvggvc tglgmppqnv gevygvvkay
      301 ttrvgigafp teqdneigel lqtrgrefgv ttgrkrrcgw ldlvllkyah mingftalal
      361 tkldildmft eikvgvaykl dgeiiphipa nqevlnkvev qyktlpgwnt disnarafke
      421 lpvnaqnyvr fiedelqipv kwigvgksre smiqlf
//
LOCUS       NP_001355936             160 aa            linear   PRI 27-APR-2025
DEFINITION  AP-1 complex subunit sigma-2 isoform 4 [Homo sapiens].
ACCESSION   NP_001355936
VERSION     NP_001355936.1
DBSOURCE    REFSEQ: accession NM_001369007.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Noojarern,S., Tim-Aroon,T., Anurat,K., Phetthong,T.,
            Khongkraparn,A. and Wattanasirichaigoon,D.
  TITLE     A novel AP1S2 variant causing leaky splicing in X-linked
            intellectual disability: Further delineation and intrafamilial
            variability
  JOURNAL   Am J Med Genet A 194 (9), e63639 (2024)
   PUBMED   38682877
  REMARK    GeneRIF: A novel AP1S2 variant causing leaky splicing in X-linked
            intellectual disability: Further delineation and intrafamilial
            variability.
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Gu,Y., Zhang,X., Li,Y., Shi,J., Cui,H., Ren,Y., Liu,S., Qiao,Y.,
            Cheng,Y. and Liu,Y.
  TITLE     MiR-204-5p-targeted AP1S2 is necessary for papillary thyroid
            carcinoma
  JOURNAL   Mol Cell Endocrinol 574, 111993 (2023)
   PUBMED   37328093
  REMARK    GeneRIF: MiR-204-5p-targeted AP1S2 is necessary for papillary
            thyroid carcinoma.
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Luan,W., Ding,Y., Ma,S., Ruan,H., Wang,J. and Lu,F.
  TITLE     Long noncoding RNA LINC00518 acts as a competing endogenous RNA to
            promote the metastasis of malignant melanoma via miR-204-5p/AP1S2
            axis
  JOURNAL   Cell Death Dis 10 (11), 855 (2019)
   PUBMED   31712557
  REMARK    GeneRIF: Long noncoding RNA LINC00518 acts as a competing
            endogenous RNA to promote the metastasis of malignant melanoma via
            miR-204-5p/AP1S2 axis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 160)
  AUTHORS   Kirchhausen,T.
  TITLE     Clathrin
  JOURNAL   Annu Rev Biochem 69, 699-727 (2000)
   PUBMED   10966473
  REMARK    Review article
REFERENCE   7  (residues 1 to 160)
  AUTHORS   Carpenter,N.J., Brown,W.T., Qu,Y. and Keenan,K.L.
  TITLE     Regional localization of a nonspecific X-linked mental retardation
            gene (MRX59) to Xp21.2-p22.2
  JOURNAL   Am J Med Genet 85 (3), 266-270 (1999)
   PUBMED   10398241
REFERENCE   8  (residues 1 to 160)
  AUTHORS   Takatsu,H., Sakurai,M., Shin,H.W., Murakami,K. and Nakayama,K.
  TITLE     Identification and characterization of novel clathrin
            adaptor-related proteins
  JOURNAL   J Biol Chem 273 (38), 24693-24700 (1998)
   PUBMED   9733768
REFERENCE   9  (residues 1 to 160)
  AUTHORS   Mulley,J.C., Kerr,B., Stevenson,R. and Lubs,H.
  TITLE     Nomenclature guidelines for X-linked mental retardation
  JOURNAL   Am J Med Genet 43 (1-2), 383-391 (1992)
   PUBMED   1605216
  REMARK    Review article
REFERENCE   10 (residues 1 to 160)
  AUTHORS   Kirchhausen,T., Davis,A.C., Frucht,S., Greco,B.O., Payne,G.S. and
            Tubb,B.
  TITLE     AP17 and AP19, the mammalian small chains of the
            clathrin-associated protein complexes show homology to Yap17p,
            their putative homolog in yeast
  JOURNAL   J Biol Chem 266 (17), 11153-11157 (1991)
   PUBMED   2040623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK299921.1, AF251295.1 and
            AC004106.1.
            
            Summary: Adaptor protein complex 1 is found at the cytoplasmic face
            of coated vesicles located at the Golgi complex, where it mediates
            both the recruitment of clathrin to the membrane and the
            recognition of sorting signals within the cytosolic tails of
            transmembrane receptors. This complex is a heterotetramer composed
            of two large, one medium, and one small adaptin subunit. The
            protein encoded by this gene serves as the small subunit of this
            complex and is a member of the adaptin protein family. Transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1343788.1,
                                           SRR11853560.29788.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..160
                     /product="AP-1 complex subunit sigma-2 isoform 4"
                     /note="clathrin adaptor complex AP1 sigma 1B subunit;
                     clathrin assembly protein complex 1 sigma-1B small chain;
                     AP-1 complex subunit sigma-2; sigma1B-adaptin;
                     adaptor-related protein complex 1 subunit sigma-1B;
                     adaptor related protein complex 1 sigma 2 subunit; adaptor
                     protein complex AP-1 sigma-1B subunit; golgi adaptor
                     HA1/AP1 adaptin sigma-1B subunit; adapter-related protein
                     complex 1 sigma-1B subunit"
                     /calculated_mol_wt=19006
     Region          2..144
                     /region_name="AP1_sigma"
                     /note="AP-1 complex subunit sigma; cd14831"
                     /db_xref="CDD:341435"
     Site            order(8..9,14,61..64,87..88,91,96..100)
                     /site_type="other"
                     /note="dileucine motif interface [polypeptide binding]"
                     /db_xref="CDD:341435"
     Site            order(13..16,18..19,44..48,74..78,80..82,85,96,103..106,
                     110..111,114..115,118..125,127..129,136..138,140..141,144)
                     /site_type="other"
                     /note="AP-1 gamma interface [polypeptide binding]"
                     /db_xref="CDD:341435"
     Site            order(25,29,33,36,50..53)
                     /site_type="other"
                     /note="AP-1 mu interface [polypeptide binding]"
                     /db_xref="CDD:341435"
     CDS             1..160
                     /gene="AP1S2"
                     /gene_synonym="DC22; MRX59; MRXS21; MRXS5; MRXSF; PGS;
                     SIGMA1B"
                     /coded_by="NM_001369007.1:127..609"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS94560.1"
                     /db_xref="GeneID:8905"
                     /db_xref="HGNC:HGNC:560"
                     /db_xref="MIM:300629"
ORIGIN      
        1 mqfmllfsrq gklrlqkwyv plsdkekkki trelvqtvla rkpkmcsfle wrdlkivykr
       61 yaslyfccai edqdnelitl eiihryvell dkyfgsvcel diifnfekay fildefllgg
      121 evqetskknv lkaieqadll qektetmyhs ksfigfkkay
//
LOCUS       NP_001081609             128 aa            linear   VRT 27-APR-2025
DEFINITION  variant histone H2A.Zl1 [Xenopus laevis].
ACCESSION   NP_001081609 NP_001081610
VERSION     NP_001081609.1
DBSOURCE    REFSEQ: accession NM_001088140.2
KEYWORDS    RefSeq.
SOURCE      Xenopus laevis (African clawed frog)
  ORGANISM  Xenopus laevis
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae;
            Xenopus; Xenopus.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Klein,S.L., Strausberg,R.L., Wagner,L., Pontius,J., Clifton,S.W.
            and Richardson,P.
  TITLE     Genetic and genomic tools for Xenopus research: The NIH Xenopus
            initiative
  JOURNAL   Dev Dyn 225 (4), 384-391 (2002)
   PUBMED   12454917
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Iouzalen,N., Moreau,J. and Mechali,M.
  TITLE     H2A.ZI, a new variant histone expressed during Xenopus early
            development exhibits several distinct features from the core
            histone H2A
  JOURNAL   Nucleic Acids Res 24 (20), 3947-3952 (1996)
   PUBMED   8918796
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC128510.1.
            
            On Jul 25, 2007 this sequence version replaced NP_001081610.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DC128510.1, DC105551.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00012418, SAMD00012419
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Xenopus laevis"
                     /db_xref="taxon:8355"
                     /chromosome="1S"
                     /map="1S"
     Protein         1..128
                     /product="variant histone H2A.Zl1"
                     /calculated_mol_wt=13355
     Region          6..121
                     /region_name="PLN00154"
                     /note="histone H2A; Provisional"
                     /db_xref="CDD:177756"
     CDS             1..128
                     /gene="h2az1.S"
                     /gene_synonym="H2A.z; H2A.Z1; h2afz; H2Az"
                     /coded_by="NM_001088140.2:133..519"
                     /db_xref="GeneID:397949"
                     /db_xref="Xenbase:XB-GENE-17342536"
ORIGIN      
        1 maggkagkdt gkakatsitr ssraglqfpv grihrllknr ttshgrvggt aavytaaile
       61 yltaevlela gnaskdlkvk risprhlqla irgdeeldal ikatiagggv iphihkslig
      121 kkgqqktv
//
LOCUS       NP_001356234              35 aa            linear   ROD 27-APR-2025
DEFINITION  sarcoplasmic/endoplasmic reticulum calcium ATPase regulator DWORF
            isoform 1 [Mus musculus].
ACCESSION   NP_001356234
VERSION     NP_001356234.1
DBSOURCE    REFSEQ: accession NM_001369305.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 35)
  AUTHORS   Stege,N.M., Oliveira Nunes Teixeira,V., Zijlstra,S.N.,
            Feringa,A.M., de Boer,R.A. and Sillje,H.H.W.
  TITLE     Deletion of DWORF does not affect cardiac function in aging and in
            PLN-R14del cardiomyopathy
  JOURNAL   Am J Physiol Heart Circ Physiol 326 (3), H870-H876 (2024)
   PUBMED   38334971
  REMARK    GeneRIF: Deletion of DWORF does not affect cardiac function in
            aging and in PLN-R14del cardiomyopathy.
REFERENCE   2  (residues 1 to 35)
  AUTHORS   Makarewich,C.A., Munir,A.Z., Schiattarella,G.G., Bezprozvannaya,S.,
            Raguimova,O.N., Cho,E.E., Vidal,A.H., Robia,S.L., Bassel-Duby,R.
            and Olson,E.N.
  TITLE     The DWORF micropeptide enhances contractility and prevents heart
            failure in a mouse model of dilated cardiomyopathy
  JOURNAL   Elife 7, e38319 (2018)
   PUBMED   30299255
  REMARK    GeneRIF: Here the show that DWORF has a higher apparent binding
            affinity for SERCA than PLN and that DWORF overexpression mitigates
            the contractile dysfunction associated with PLN overexpression,
            substantiating its role as a potent activator of SERCA.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 35)
  AUTHORS   Nelson,B.R., Makarewich,C.A., Anderson,D.M., Winders,B.R.,
            Troupes,C.D., Wu,F., Reese,A.L., McAnally,J.R., Chen,X.,
            Kavalali,E.T., Cannon,S.C., Houser,S.R., Bassel-Duby,R. and
            Olson,E.N.
  TITLE     A peptide encoded by a transcript annotated as long noncoding RNA
            enhances SERCA activity in muscle
  JOURNAL   Science 351 (6270), 271-275 (2016)
   PUBMED   26816378
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC121840.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR2680377.918634.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164132 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..35
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3"
     Protein         1..35
                     /product="sarcoplasmic/endoplasmic reticulum calcium
                     ATPase regulator DWORF isoform 1"
                     /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase
                     regulator DWORF; SERCA regulator DWORF"
                     /calculated_mol_wt=3755
     Region          1..35
                     /region_name="DWORF"
                     /note="DWarf Open Reading Frame (DWORF); cd20247"
                     /db_xref="CDD:380779"
     CDS             1..35
                     /gene="Strit1"
                     /gene_synonym="DWORF; Gm34302"
                     /coded_by="NM_001369305.1:80..187"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:102637511"
                     /db_xref="MGI:MGI:5593461"
ORIGIN      
        1 maekaestsp hlivpilllv gwivgciivi yivff
//
LOCUS       NP_116265                538 aa            linear   PRI 27-APR-2025
DEFINITION  LIM domain-containing protein ajuba isoform 1 [Homo sapiens].
ACCESSION   NP_116265
VERSION     NP_116265.1
DBSOURCE    REFSEQ: accession NM_032876.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Xu,B., Li,Q., Zhang,J. and Chen,F.
  TITLE     LIM domain-containing protein Ajuba inhibits chemotherapy-induced
            apoptosis by negatively regulating p53 stability in colorectal
            cancer cells
  JOURNAL   Mol Oncol 17 (8), 1678-1691 (2023)
   PUBMED   36931700
  REMARK    GeneRIF: LIM domain-containing protein Ajuba inhibits
            chemotherapy-induced apoptosis by negatively regulating p53
            stability in colorectal cancer cells.
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Li,X., Zhao,G., Mi,X., Xu,T., Li,X. and Liu,B.
  TITLE     Ajuba Overexpression Promotes Breast Cancer Chemoresistance and
            Glucose Uptake through TAZ-GLUT3/Survivin Pathway
  JOURNAL   Biomed Res Int 2022, 3321409 (2022)
   PUBMED   35178446
  REMARK    GeneRIF: Ajuba Overexpression Promotes Breast Cancer
            Chemoresistance and Glucose Uptake through TAZ-GLUT3/Survivin
            Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Ponia,S.S., Robertson,S.J., McNally,K.L., Subramanian,G.,
            Sturdevant,G.L., Lewis,M., Jessop,F., Kendall,C., Gallegos,D.,
            Hay,A., Schwartz,C., Rosenke,R., Saturday,G., Bosio,C.M.,
            Martens,C. and Best,S.M.
  TITLE     Mitophagy antagonism by ZIKV reveals Ajuba as a regulator of PINK1
            signaling, PKR-dependent inflammation, and viral invasion of
            tissues
  JOURNAL   Cell Rep 37 (4), 109888 (2021)
   PUBMED   34706234
  REMARK    GeneRIF: Mitophagy antagonism by ZIKV reveals Ajuba as a regulator
            of PINK1 signaling, PKR-dependent inflammation, and viral invasion
            of tissues.
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Hirota,T., Kunitoku,N., Sasayama,T., Marumoto,T., Zhang,D.,
            Nitta,M., Hatakeyama,K. and Saya,H.
  TITLE     Aurora-A and an interacting activator, the LIM protein Ajuba, are
            required for mitotic commitment in human cells
  JOURNAL   Cell 114 (5), 585-598 (2003)
   PUBMED   13678582
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Marie,H., Pratt,S.J., Betson,M., Epple,H., Kittler,J.T., Meek,L.,
            Moss,S.J., Troyanovsky,S., Attwell,D., Longmore,G.D. and Braga,V.M.
  TITLE     The LIM protein Ajuba is recruited to cadherin-dependent cell
            junctions through an association with alpha-catenin
  JOURNAL   J Biol Chem 278 (2), 1220-1228 (2003)
   PUBMED   12417594
  REMARK    GeneRIF: Ajuba contributes to the bridging of the cadherin adhesive
            complexes to the actin cytoskeleton and as such contribute to the
            formation or strengthening of cadherin-mediated cell-cell adhesion.
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Marie,H., Billups,D., Bedford,F.K., Dumoulin,A., Goyal,R.K.,
            Longmore,G.D., Moss,S.J. and Attwell,D.
  TITLE     The amino terminus of the glial glutamate transporter GLT-1
            interacts with the LIM protein Ajuba
  JOURNAL   Mol Cell Neurosci 19 (2), 152-164 (2002)
   PUBMED   11860269
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Kanungo,J., Pratt,S.J., Marie,H. and Longmore,G.D.
  TITLE     Ajuba, a cytosolic LIM protein, shuttles into the nucleus and
            affects embryonal cell proliferation and fate decisions
  JOURNAL   Mol Biol Cell 11 (10), 3299-3313 (2000)
   PUBMED   11029037
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Goyal,R.K., Lin,P., Kanungo,J., Payne,A.S., Muslin,A.J. and
            Longmore,G.D.
  TITLE     Ajuba, a novel LIM protein, interacts with Grb2, augments
            mitogen-activated protein kinase activity in fibroblasts, and
            promotes meiotic maturation of Xenopus oocytes in a Grb2- and
            Ras-dependent manner
  JOURNAL   Mol Cell Biol 19 (6), 4379-4389 (1999)
   PUBMED   10330178
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL132780.5.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034968.2, SRR18074969.3459817.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262713.7/ ENSP00000262713.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..538
                     /product="LIM domain-containing protein ajuba isoform 1"
                     /note="jub, ajuba homolog; LIM domain-containing protein
                     ajuba"
                     /calculated_mol_wt=56803
     Region          1..335
                     /region_name="PreLIM"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96IF1.1)"
     Region          1..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96IF1.1)"
     Region          <18..>103
                     /region_name="PHA03418"
                     /note="hypothetical E4 protein; Provisional"
                     /db_xref="CDD:177646"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96IF1.1)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96IF1.1)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96IF1.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96IF1.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96IF1.1)"
     Region          280..288
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96IF1.1)"
     Region          291..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96IF1.1)"
     Region          338..391
                     /region_name="LIM1_Ajuba_like"
                     /note="The first LIM domain of Ajuba-like proteins;
                     cd09352"
                     /db_xref="CDD:188738"
     Site            order(338,341,360,363,366,369,387,390)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188738"
     Region          403..455
                     /region_name="LIM2_Ajuba_like"
                     /note="The second LIM domain of Ajuba-like proteins;
                     cd09355"
                     /db_xref="CDD:188741"
     Site            order(403,406,423,426,429,432,451,454)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188741"
     Region          463..524
                     /region_name="LIM3_Ajuba_like"
                     /note="The third LIM domain of Ajuba-like proteins;
                     cd09438"
                     /db_xref="CDD:188822"
     Site            order(463,466,490,493,496,499,520,523)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188822"
     CDS             1..538
                     /gene="AJUBA"
                     /gene_synonym="JUB"
                     /coded_by="NM_032876.6:286..1902"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9581.1"
                     /db_xref="GeneID:84962"
                     /db_xref="HGNC:HGNC:20250"
                     /db_xref="MIM:609066"
ORIGIN      
        1 merlgekasr llekfgrrkg essrsgsdgt pgpgkgrlsg lggprksgpr gatggpgdep
       61 lepareqgsl daernqrgsf eapryegsfp agppptralp lpqslppdfr leptapalsp
      121 rssfasssas daskpssprg sllldgagag gaggsrpcsn rtsgismgyd qrhgsplpag
      181 pclfgpplag apagyspggv psaypelhaa ldrlyaqrpa gfgcqesrhs yppalgspga
      241 lagagvgaag plerrgaqpg rhsvtgygdc avgaryqdel tallrltvgt ggreagarge
      301 psgiepsgle eppgpfvpea ararmrepea redyfgtcik cnkgiygqsn acqaldslyh
      361 tqcfvccscg rtlrckafys vngsvyceed ylfsgfqeaa ekccvcghli lekilqamgk
      421 syhpgcfrci vcnkcldgip ftvdfsnqvy cvtdyhknya pkcaacgqpi lpsegcediv
      481 rvismdrdyh fecyhcedcr mqlsdeegcc cfpldghllc hgchmqrlna rqppanyi
//
LOCUS       NP_001098101             809 aa            linear   PRI 27-APR-2025
DEFINITION  3',5'-cyclic-AMP phosphodiesterase 4D isoform PDE4D4 [Homo
            sapiens].
ACCESSION   NP_001098101
VERSION     NP_001098101.1
DBSOURCE    REFSEQ: accession NM_001104631.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Nummela,P., Zafar,S., Veikkolainen,E., Ukkola,I., Cinella,V.,
            Ayo,A., Asghar,M.Y., Valimaki,N., Tornquist,K., Karhu,A.,
            Laakkonen,P., Aaltonen,L.A. and Ristimaki,A.
  TITLE     GNAS mutation inhibits growth and induces phosphodiesterase 4D
            expression in colorectal cancer cell lines
  JOURNAL   Int J Cancer 154 (11), 1987-1998 (2024)
   PUBMED   38319157
  REMARK    GeneRIF: GNAS mutation inhibits growth and induces
            phosphodiesterase 4D expression in colorectal cancer cell lines.
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Mydlarova Blascakova,M., Hricova,K., Maslejova,K., Majherova,M.,
            Vaskova,H., Poracova,J., Bernatova,R., Konecna,M. and Sedlak,V.
  TITLE     Association of the PDE4D gene variant with selected markers in
            individuals with ischaemic heart disease: a pilot study
  JOURNAL   Cent Eur J Public Health 31 (Suppl 1), S75-S81 (2023)
   PUBMED   38272484
  REMARK    GeneRIF: Association of the PDE4D gene variant with selected
            markers in individuals with ischaemic heart disease: a pilot study.
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Rosand,J., Bayley,N., Rost,N. and de Bakker,P.I.
  TITLE     Many hypotheses but no replication for the association between
            PDE4D and stroke
  JOURNAL   Nat Genet 38 (10), 1091-2 (2006)
   PUBMED   17006457
REFERENCE   4  (residues 1 to 809)
  AUTHORS   Gretarsdottir,S., Thorleifsson,G., Reynisdottir,S.T., Manolescu,A.,
            Jonsdottir,S., Jonsdottir,T., Gudmundsdottir,T., Bjarnadottir,S.M.,
            Einarsson,O.B., Gudjonsdottir,H.M., Hawkins,M., Gudmundsson,G.,
            Gudmundsdottir,H., Andrason,H., Gudmundsdottir,A.S.,
            Sigurdardottir,M., Chou,T.T., Nahmias,J., Goss,S.,
            Sveinbjornsdottir,S., Valdimarsson,E.M., Jakobsson,F.,
            Agnarsson,U., Gudnason,V., Thorgeirsson,G., Fingerle,J., Gurney,M.,
            Gudbjartsson,D., Frigge,M.L., Kong,A., Stefansson,K. and
            Gulcher,J.R.
  TITLE     The gene encoding phosphodiesterase 4D confers risk of ischemic
            stroke
  JOURNAL   Nat Genet 35 (2), 131-138 (2003)
   PUBMED   14517540
  REMARK    GeneRIF: fine mapping of locus and testing for association with
            stroke
            Erratum:[Nat Genet. 2005 May;37(5):555]
REFERENCE   5  (residues 1 to 809)
  AUTHORS   Dominiczak,A.F. and McBride,M.W.
  TITLE     Genetics of common polygenic stroke
  JOURNAL   Nat Genet 35 (2), 116-117 (2003)
   PUBMED   14517535
REFERENCE   6  (residues 1 to 809)
  AUTHORS   Le Jeune,I.R., Shepherd,M., Van Heeke,G., Houslay,M.D. and
            Hall,I.P.
  TITLE     Cyclic AMP-dependent transcriptional up-regulation of
            phosphodiesterase 4D5 in human airway smooth muscle cells.
            Identification and characterization of a novel PDE4D5 promoter
  JOURNAL   J Biol Chem 277 (39), 35980-35989 (2002)
   PUBMED   12121997
  REMARK    GeneRIF: PDE4D5 is upregulated in tracheal smooth muscle cells
            because of a CRE-containing, isoform-specific promoter
REFERENCE   7  (residues 1 to 809)
  AUTHORS   Nemoz,G., Zhang,R., Sette,C. and Conti,M.
  TITLE     Identification of cyclic AMP-phosphodiesterase variants from the
            PDE4D gene expressed in human peripheral mononuclear cells
  JOURNAL   FEBS Lett 384 (1), 97-102 (1996)
   PUBMED   8797812
REFERENCE   8  (residues 1 to 809)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
REFERENCE   9  (residues 1 to 809)
  AUTHORS   Milatovich,A., Bolger,G., Michaeli,T. and Francke,U.
  TITLE     Chromosome localizations of genes for five cAMP-specific
            phosphodiesterases in man and mouse
  JOURNAL   Somat Cell Mol Genet 20 (2), 75-86 (1994)
   PUBMED   8009369
REFERENCE   10 (residues 1 to 809)
  AUTHORS   Swinnen,J.V., Joseph,D.R. and Conti,M.
  TITLE     The mRNA encoding a high-affinity cAMP phosphodiesterase is
            regulated by hormones and cAMP
  JOURNAL   Proc Natl Acad Sci U S A 86 (21), 8197-8201 (1989)
   PUBMED   2554303
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027322.4, L20969.1,
            AC092343.3 and BF197530.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes one of four mammalian counterparts to
            the fruit fly 'dunce' gene. The encoded protein has
            3',5'-cyclic-AMP phosphodiesterase activity and degrades cAMP,
            which acts as a signal transduction molecule in multiple cell
            types. This gene uses different promoters to generate multiple
            alternatively spliced transcript variants that encode functional
            proteins.[provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (PDE4D4, also known as isoform 1).
            
            Sequence Note: The sequence L20969.1 is from a chimeric clone. Only
            the region representing PDE4D was propagated into this RefSeq
            record. This RefSeq record was created from transcript and genomic
            sequence data to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005449.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340635.11/ ENSP00000345502.6
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q11.2-q12.1"
     Protein         1..809
                     /product="3',5'-cyclic-AMP phosphodiesterase 4D isoform
                     PDE4D4"
                     /EC_number="3.1.4.53"
                     /note="phosphodiesterase 4D, cAMP-specific
                     (phosphodiesterase E3 dunce homolog, Drosophila);
                     cAMP-specific 3',5'-cyclic phosphodiesterase 4D;
                     cAMP-specific phosphodiesterase PDE4D6; testicular tissue
                     protein Li 136; 3',5'-cyclic-AMP phosphodiesterase 4D"
                     /calculated_mol_wt=90984
     Region          1..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08499.2)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15131123; propagated from
                     UniProtKB/Swiss-Prot (Q08499.2)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q08499.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q08499.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14270; propagated from
                     UniProtKB/Swiss-Prot (Q08499.2)"
     Region          223..339
                     /region_name="PDE4_UCR"
                     /note="Phosphodiesterase 4 upstream conserved regions
                     (UCR); pfam18100"
                     /db_xref="CDD:465648"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08499.2)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08499.2)"
     Region          343..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08499.2)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08499.2)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08499.2)"
     Region          461..701
                     /region_name="PDEase_I"
                     /note="3'5'-cyclic nucleotide phosphodiesterase;
                     pfam00233"
                     /db_xref="CDD:459723"
     Region          710..729
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08499.2)"
     Region          739..809
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08499.2)"
     CDS             1..809
                     /gene="PDE4D"
                     /gene_synonym="ACRDYS2; DPDE3; HSPDE4D; PDE43; PDE4DN2;
                     STRK1"
                     /coded_by="NM_001104631.2:105..2534"
                     /note="isoform PDE4D4 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47213.1"
                     /db_xref="GeneID:5144"
                     /db_xref="HGNC:HGNC:8783"
                     /db_xref="MIM:600129"
ORIGIN      
        1 meaegssapa ragsgegsds aggatlkapk hlwrheqhhq yplrqpqfrl lhphhhlppp
       61 pppspqpqpq cplqpppppp lpppppppga argryassga tgrvrhrgys dterylycra
      121 mdrtsyavet ghrpglkksr mswpssfqgl rrfdvdngts agrspldpmt spgsglilqa
      181 nfvhsqrres flyrsdsdyd lspksmsrns siasdihgdd livtpfaqvl aslrtvrnnf
      241 aaltnlqdra pskrspmcnq psinkatite eayqklaset leeldwcldq letlqtrhsv
      301 semasnkfkr mlnrelthls emsrsgnqvs efisntfldk qheveipspt qkekekkkrp
      361 msqisgvkkl mhsssltnss iprfgvkteq edvlakeled vnkwglhvfr iaelsgnrpl
      421 tvimhtifqe rdllktfkip vdtlitylmt ledhyhadva yhnnihaadv vqsthvllst
      481 paleavftdl eilaaifasa ihdvdhpgvs nqflintnse lalmyndssv lenhhlavgf
      541 kllqeencdi fqnltkkqrq slrkmvidiv latdmskhmn lladlktmve tkkvtssgvl
      601 lldnysdriq vlqnmvhcad lsnptkplql yrqwtdrime effrqgdrer ergmeispmc
      661 dkhnasveks qvgfidyivh plwetwadlv hpdaqdildt lednrewyqs tipqspspap
      721 ddpeegrqgq tekfqfeltl eedgesdtek dsgsqveedt scsdsktlct qdsesteipl
      781 deqveeeavg eeeesqpeac viddrspdt
//
LOCUS       NP_001353346            1292 aa            linear   PRI 27-APR-2025
DEFINITION  histone-lysine N-methyltransferase SETDB1 isoform 4 [Homo sapiens].
ACCESSION   NP_001353346 XP_016858442
VERSION     NP_001353346.1
DBSOURCE    REFSEQ: accession NM_001366417.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1292)
  AUTHORS   Xia,K., Hui,Y., Zhang,L., Qiu,Q., Zhong,J., Chen,H., Liu,X.,
            Wang,L. and Chen,Z.
  TITLE     SETDB1 targeting SESN2 regulates mitochondrial damage and oxidative
            stress in renal ischemia-reperfusion injury
  JOURNAL   BMC Biol 22 (1), 246 (2024)
   PUBMED   39443993
  REMARK    GeneRIF: SETDB1 targeting SESN2 regulates mitochondrial damage and
            oxidative stress in renal ischemia-reperfusion injury.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1292)
  AUTHORS   Chang,Y.H., Yamamoto,K., Fujino,T., Wang,T.W., Sugimoto,E.,
            Zhang,W., Yabushita,T., Suzaki,K., Pietsch,E.C., Weir,B.A.,
            Crescenzo,R., Cowley,G.S., Attar,R., Philippar,U., Wunderlich,M.,
            Mizukawa,B., Zheng,Y., Enomoto,Y., Imai,Y., Kitamura,T. and
            Goyama,S.
  TITLE     SETDB1 suppresses NK cell-mediated immunosurveillance in acute
            myeloid leukemia with granulo-monocytic differentiation
  JOURNAL   Cell Rep 43 (8), 114536 (2024)
   PUBMED   39096901
REFERENCE   3  (residues 1 to 1292)
  AUTHORS   Kang,Y.K., Eom,J., Min,B. and Park,J.S.
  TITLE     SETDB1 deletion causes DNA demethylation and upregulation of
            multiple zinc-finger genes
  JOURNAL   Mol Biol Rep 51 (1), 778 (2024)
   PUBMED   38904842
  REMARK    GeneRIF: SETDB1 deletion causes DNA demethylation and upregulation
            of multiple zinc-finger genes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1292)
  AUTHORS   Yang,W., Wei,Y., Wang,T., Xu,Y., Jin,X., Qian,H., Yang,S. and He,S.
  TITLE     Cytoplasmic localization of SETDB1-induced Warburg effect via
            c-MYC-LDHA axis enhances migration and invasion in breast carcinoma
  JOURNAL   Int J Mol Med 53 (4) (2024)
   PUBMED   38426579
  REMARK    GeneRIF: Cytoplasmic localization of SETDB1-induced Warburg effect
            via c-MYC-LDHA axis enhances migration and invasion in breast
            carcinoma.
REFERENCE   5  (residues 1 to 1292)
  AUTHORS   Hao,Y., Bai,X.Y., Huo,F. and Chen,X.B.
  TITLE     [Downregulation of SETDB1 suppresses epithelial mesenchymal
            transition and invasion and metastasis in oral cancer via SOX7
            methylation]
  JOURNAL   Shanghai Kou Qiang Yi Xue 33 (1), 30-35 (2024)
   PUBMED   38583021
  REMARK    GeneRIF: [Downregulation of SETDB1 suppresses epithelial
            mesenchymal transition and invasion and metastasis in oral cancer
            via SOX7 methylation].
REFERENCE   6  (residues 1 to 1292)
  AUTHORS   Ayyanathan,K., Lechner,M.S., Bell,P., Maul,G.G., Schultz,D.C.,
            Yamada,Y., Tanaka,K., Torigoe,K. and Rauscher,F.J. 3rd.
  TITLE     Regulated recruitment of HP1 to a euchromatic gene induces
            mitotically heritable, epigenetic gene silencing: a mammalian cell
            culture model of gene variegation
  JOURNAL   Genes Dev 17 (15), 1855-1869 (2003)
   PUBMED   12869583
REFERENCE   7  (residues 1 to 1292)
  AUTHORS   Yang,L., Mei,Q., Zielinska-Kwiatkowska,A., Matsui,Y.,
            Blackburn,M.L., Benedetti,D., Krumm,A.A., Taborsky,G.J. Jr. and
            Chansky,H.A.
  TITLE     An ERG (ets-related gene)-associated histone methyltransferase
            interacts with histone deacetylases 1/2 and transcription
            co-repressors mSin3A/B
  JOURNAL   Biochem J 369 (Pt 3), 651-657 (2003)
   PUBMED   12398767
REFERENCE   8  (residues 1 to 1292)
  AUTHORS   Schultz,D.C., Ayyanathan,K., Negorev,D., Maul,G.G. and
            Rauscher,F.J. 3rd.
  TITLE     SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific
            methyltransferase that contributes to HP1-mediated silencing of
            euchromatic genes by KRAB zinc-finger proteins
  JOURNAL   Genes Dev 16 (8), 919-932 (2002)
   PUBMED   11959841
  REMARK    GeneRIF: Contributes to HP1-mediated silencing of euchromatic genes
            by KRAB zinc-finger proteins; KAP-1, SETDB1, H3-MeK9, and HP1 are
            enriched at promoter sequences of a euchromatic gene silenced by
            the KRAB-KAP-1 repression system
REFERENCE   9  (residues 1 to 1292)
  AUTHORS   Yang,L., Xia,L., Wu,D.Y., Wang,H., Chansky,H.A., Schubach,W.H.,
            Hickstein,D.D. and Zhang,Y.
  TITLE     Molecular cloning of ESET, a novel histone H3-specific
            methyltransferase that interacts with ERG transcription factor
  JOURNAL   Oncogene 21 (1), 148-152 (2002)
   PUBMED   11791185
REFERENCE   10 (residues 1 to 1292)
  AUTHORS   Harte,P.J., Wu,W., Carrasquillo,M.M. and Matera,A.G.
  TITLE     Assignment of a novel bifurcated SET domain gene, SETDB1, to human
            chromosome band 1q21 by in situ hybridization and radiation hybrids
  JOURNAL   Cytogenet Cell Genet 84 (1-2), 83-86 (1999)
   PUBMED   10343109
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590133.32.
            
            On Oct 4, 2018 this sequence version replaced XP_016858442.1.
            
            Summary: This gene encodes a histone methyltransferase which
            regulates histone methylation, gene silencing, and transcriptional
            repression. This gene has been identified as a target for treatment
            in Huntington Disease, given that gene silencing and transcription
            dysfunction likely play a role in the disease pathogenesis.
            Alternatively spliced transcript variants of this gene have been
            described.[provided by RefSeq, Jun 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.358138.1,
                                           SRR14038194.3952566.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..1292
                     /product="histone-lysine N-methyltransferase SETDB1
                     isoform 4"
                     /EC_number="2.1.1.366"
                     /note="ERG-associated protein with a SET domain, ESET;
                     histone-lysine N-methyltransferase, H3lysine-9 specific 4;
                     lysine N-methyltransferase 1E; histone-lysine
                     N-methyltransferase SETDB1; histone H3-K9
                     methyltransferase 4; tudor domain containing 21; SET
                     domain bifurcated 1"
                     /calculated_mol_wt=143128
     Region          108..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15047.1)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88974; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88974; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88974; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Region          193..250
                     /region_name="DUF5604"
                     /note="Domain of unknown function (DUF5604); pfam18300"
                     /db_xref="CDD:408109"
     Region          260..341
                     /region_name="Tudor_SETDB1_rpt1"
                     /note="first Tudor domain found in SET domain bifurcated 1
                     (SETDB1) and similar proteins; cd20382"
                     /db_xref="CDD:410453"
     Site            order(296,299..302)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410453"
     Region          348..401
                     /region_name="Tudor_SETDB1_rpt2"
                     /note="second Tudor domain found in SET domain bifurcated
                     1 (SETDB1) and similar proteins; cd21181"
                     /db_xref="CDD:410548"
     Site            order(357,360,386..389,392..394)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410548"
     Region          598..673
                     /region_name="MBD"
                     /note="Methyl-CpG binding domain; smart00391"
                     /db_xref="CDD:128673"
     Site            order(612,614,616,623,625,634,637,641)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238689"
     Region          675..>876
                     /region_name="SET_SETDB1"
                     /note="SET domain (including pre-SET and post-SET domains)
                     found in SET domain bifurcated 1 (SETDB1) and similar
                     proteins; cd10517"
                     /db_xref="CDD:380915"
     Region          869..1161
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15047.1)"
     Site            1026
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Site            1067
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Site            1171
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Site            1179
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Region          <1203..1292
                     /region_name="SET"
                     /note="SET (Su(var)3-9, Enhancer-of-zeste, Trithorax)
                     domain superfamily; cl40432"
                     /db_xref="CDD:394802"
     Site            order(1220..1225,1233..1235,1264..1267)
                     /site_type="active"
                     /db_xref="CDD:380915"
     CDS             1..1292
                     /gene="SETDB1"
                     /gene_synonym="ESET; H3-K9-HMTase4; KG1T; KMT1E; TDRD21"
                     /coded_by="NM_001366417.1:98..3976"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS91050.1"
                     /db_xref="GeneID:9869"
                     /db_xref="HGNC:HGNC:10761"
                     /db_xref="MIM:604396"
ORIGIN      
        1 msslpgcigl daatatvese eiaelqqavv eelgismeel rhfideelek mdcvqqrkkq
       61 laeletwviq kesevahvdq lfddasravt nceslvkdfy sklglqyrds ssedessrpt
      121 eiieipdedd dvlsidsgda gsrtpkdqkl reamaalrks aqdvqkfmda vnkksssqdl
      181 hkgtlsqmsg elskdgdliv smrilgkkrt ktwhkgtlia iqtvgpgkky kvkfdnkgks
      241 llsgnhiayd yhppadklyv gsrvvakykd gnqvwlyagi vaetpnvknk lrfliffddg
      301 yasyvtqsel ypicrplkkt wediediscr dfieeyvtay pnrpmvllks gqlikteweg
      361 twwksrveev dgslvrilfl ddkrcewiyr gstrlepmfs mktssasale kkqgqlrtrp
      421 nmgavrskgp vvqytqdltg tgtqfkpvep pqptappapp fppapplspq agdseslesq
      481 laqsrkqvak kstsfrpgsv gsghssptsp alsenvsggk pginqtyrsp lgstasapap
      541 salpappapp vfhgmlerap aepsyrapme klfylphvcs ytclsrvrpm rneqyrgknp
      601 llvpllydfr rmtarrrvnr kmgfhviykt pcglclrtmq eierylfetg cdflflemfc
      661 ldpyvlvdrk fqpykpfyyi lditygkedv plscvneidt tpppqvaysk eripgkgvfi
      721 ntgpeflvgc dckdgcrdks kcachqltiq atactpggqi npnsgyqykr leeclptgvy
      781 ecnkrckcdp nmctnrlvqh glqvrlqlfk tqnkgwgirc lddiakgsfv ciyagkiltd
      841 dfadkeglem gdeyfanldh iesvenfkeg yesdapcssd ssgvdlkdqe dgnsgtedpe
      901 esnddssddn fckdedfsts svwrsyatrr qtrgqkengl settskdshp pdlgpphipv
      961 ppsipvggcn ppsseetpkn kvaswlscns vseggfadsd shssfktneg gegraggsrm
     1021 eaekastsgl gikdegdikq akkedtddrn kmsvvtessr nygynpspvk peglrrppsk
     1081 tsmhqsrrlm asaqsnpddv ltlssstese gesgtsrkpt agqtsatavd sddiqtissg
     1141 segddfedkk nmtgpmkrqv avkstrgfal ksthgiaiks tnmasvdkge sapvrkntrq
     1201 fydgeescyi idaklegnlg rylnhscspn lfvqnvfvdt hdlrfpwvaf faskriragt
     1261 eltwdynyev gsvegkellc ccgaiecrgr ll
//
LOCUS       NP_001357387             616 aa            linear   PRI 27-APR-2025
DEFINITION  protein phosphatase EYA4 isoform g [Homo sapiens].
ACCESSION   NP_001357387 XP_005266910
VERSION     NP_001357387.1
DBSOURCE    REFSEQ: accession NM_001370458.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   de la Pena Avalos,B., Tropee,R., Duijf,P.H.G. and Dray,E.
  TITLE     EYA4 promotes breast cancer progression and metastasis through its
            role in replication stress avoidance
  JOURNAL   Mol Cancer 22 (1), 158 (2023)
   PUBMED   37777742
  REMARK    GeneRIF: EYA4 promotes breast cancer progression and metastasis
            through its role in replication stress avoidance.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Li,C., Liu,Z., Xu,G., Wu,S., Peng,Y., Wu,R., Zhao,S., Liao,X. and
            Lin,R.
  TITLE     Aberrant DNA methylation and expression of EYA4 in gastric cardia
            intestinal metaplasia
  JOURNAL   Saudi J Gastroenterol 28 (6), 456-465 (2022)
   PUBMED   36453428
  REMARK    GeneRIF: Aberrant DNA methylation and expression of EYA4 in gastric
            cardia intestinal metaplasia.
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Zhang,W., Song,J., Tong,B., Ma,M., Guo,L., Yuan,Y. and Yang,J.
  TITLE     Identification of a novel CNV at the EYA4 gene in a Chinese family
            with autosomal dominant nonsyndromic hearing loss
  JOURNAL   BMC Med Genomics 15 (1), 113 (2022)
   PUBMED   35578334
  REMARK    GeneRIF: Identification of a novel CNV at the EYA4 gene in a
            Chinese family with autosomal dominant nonsyndromic hearing loss.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Ishino,T., Ogawa,Y., Sonoyama,T., Taruya,T., Kono,T., Hamamoto,T.,
            Ueda,T., Takeno,S., Moteki,H., Nishio,S.Y., Usami,S.I., Nagano,Y.,
            Yoshimura,A., Yoshikawa,K., Kato,M., Ichimoto,M. and Watanabe,R.
  TITLE     Identification of a Novel Copy Number Variation of EYA4 Causing
            Autosomal Dominant Non-syndromic Hearing Loss
  JOURNAL   Otol Neurotol 42 (7), e866-e874 (2021)
   PUBMED   33859130
  REMARK    GeneRIF: Identification of a Novel Copy Number Variation of EYA4
            Causing Autosomal Dominant Non-syndromic Hearing Loss.
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Wayne,S., Robertson,N.G., DeClau,F., Chen,N., Verhoeven,K.,
            Prasad,S., Tranebjarg,L., Morton,C.C., Ryan,A.F., Van Camp,G. and
            Smith,R.J.
  TITLE     Mutations in the transcriptional activator EYA4 cause late-onset
            deafness at the DFNA10 locus
  JOURNAL   Hum Mol Genet 10 (3), 195-200 (2001)
   PUBMED   11159937
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Schonberger,J., Levy,H., Grunig,E., Sangwatanaroj,S., Fatkin,D.,
            MacRae,C., Stacker,H., Halpin,C., Eavey,R., Philbin,E.F., Katus,H.,
            Seidman,J.G. and Seidman,C.E.
  TITLE     Dilated cardiomyopathy and sensorineural hearing loss: a heritable
            syndrome that maps to 6q23-24
  JOURNAL   Circulation 101 (15), 1812-1818 (2000)
   PUBMED   10769282
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Borsani,G., DeGrandi,A., Ballabio,A., Bulfone,A., Bernard,L.,
            Banfi,S., Gattuso,C., Mariani,M., Dixon,M., Donnai,D., Metcalfe,K.,
            Winter,R., Robertson,M., Axton,R., Brown,A., van Heyningen,V. and
            Hanson,I.
  TITLE     EYA4, a novel vertebrate gene related to Drosophila eyes absent
  JOURNAL   Hum Mol Genet 8 (1), 11-23 (1999)
   PUBMED   9887327
REFERENCE   8  (residues 1 to 616)
  AUTHORS   O'Neill,M.E., Marietta,J., Nishimura,D., Wayne,S., Van Camp,G., Van
            Laer,L., Negrini,C., Wilcox,E.R., Chen,A., Fukushima,K., Ni,L.,
            Sheffield,V.C. and Smith,R.J.
  TITLE     A gene for autosomal dominant late-onset progressive non-syndromic
            hearing loss, DFNA10, maps to chromosome 6
  JOURNAL   Hum Mol Genet 5 (6), 853-856 (1996)
   PUBMED   8776603
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121959.15, AL024497.5 and
            AL450270.7.
            
            On May 8, 2019 this sequence version replaced XP_005266910.1.
            
            Summary: This gene encodes a member of the eyes absent (EYA) family
            of proteins. The encoded protein may act as a transcriptional
            activator through its protein phosphatase activity, and it may be
            important for eye development, and for continued function of the
            mature organ of Corti. Mutations in this gene are associated with
            postlingual, progressive, autosomal dominant hearing loss at the
            deafness, autosomal dominant non-syndromic sensorineural 10 locus.
            The encoded protein is also a putative oncogene that mediates DNA
            repair, apoptosis, and innate immunity following DNA damage,
            cellular damage, and viral attack. Defects in this gene are also
            associated with dilated cardiomyopathy 1J. Alternative splicing
            results in multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Jul 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2144335,
                              SAMEA2145240 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.2"
     Protein         1..616
                     /product="protein phosphatase EYA4 isoform g"
                     /EC_number="3.1.3.48"
                     /note="eyes absent homolog 4; dJ78N10.1 (eyes absent);
                     eyes absent-like protein 4; protein phosphatase EYA4"
                     /calculated_mol_wt=66846
     Region          12..>328
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     Region          345..616
                     /region_name="HAD_Eya"
                     /note="protein tyrosine phosphatase domain of the nuclear
                     transcription factor of Eyes absent (Eya) and related
                     phosphatase domains; cd02601"
                     /db_xref="CDD:319789"
     Site            order(347,574,576,592,594..597,603,606,609..610,613..616)
                     /site_type="other"
                     /note="SIX1 interface [polypeptide binding]"
                     /db_xref="CDD:319789"
     Site            order(352..356,446..447,555,579..580,584..585)
                     /site_type="active"
                     /db_xref="CDD:319789"
     CDS             1..616
                     /gene="EYA4"
                     /gene_synonym="CMD1J; DFNA10"
                     /coded_by="NM_001370458.1:459..2309"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS94004.1"
                     /db_xref="GeneID:2070"
                     /db_xref="HGNC:HGNC:3522"
                     /db_xref="MIM:603550"
ORIGIN      
        1 medsqdlneq svkktctesd vsqsqnsrsm emqdlaspht lvgggdtpgs skleksnlss
       61 tsvttngtgv sllavktepl nssettattg dgaldtftgs vitssgyspr sahqyspqly
      121 pskpyphils tpaaqtmsay agqtqysgmq qpavytaysq tgqpyslpty dlgvmlpaik
      181 tesglsqtqs plqsgclsys pgfstpqpgq tpysyqmpgs sfapsstiya nnsvsnstnf
      241 sgsqqdypsy tafgqnqyaq yysastygay mtsnntadgt psststyqlq eslpgltnqp
      301 gefdtmqsps tpikdldert crssgsksrg rgrknnpspp pdsdlervfv wdldetiivf
      361 hslltgsyaq kygkdppmav tlglrmeemi fnladthlff ndleecdqvh iddvssddng
      421 qdlstysfat dgfhaaassa nlclptgvrg gvdwmrklaf ryrrvkelyn tyknnvggll
      481 gpakrdawlq lraeiegltd swltnalksl siistrsnci nvlvtttqli palakvllys
      541 lggafpieni ysatkigkes cferivsrfg tnityvvigd grdeehaanq hnmpfwriss
      601 hsdllalhqa leleyl
//
LOCUS       NP_001351859            1839 aa            linear   PRI 27-APR-2025
DEFINITION  proteasome adapter and scaffold protein ECM29 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001351859 XP_005251908
VERSION     NP_001351859.1
DBSOURCE    REFSEQ: accession NM_001364930.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1839)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 1839)
  AUTHORS   Wang,X., Chemmama,I.E., Yu,C., Huszagh,A., Xu,Y., Viner,R.,
            Block,S.A., Cimermancic,P., Rychnovsky,S.D., Ye,Y., Sali,A. and
            Huang,L.
  TITLE     The proteasome-interacting Ecm29 protein disassembles the 26S
            proteasome in response to oxidative stress
  JOURNAL   J Biol Chem 292 (39), 16310-16320 (2017)
   PUBMED   28821611
  REMARK    GeneRIF: Data suggest that the adapter protein ECM29 is the main
            proteasome-interacting protein responsible for oxidative
            stress-induced proteasome disassembly/remodeling; ECM29 appears to
            intrude on interaction between the 20S core particle and 19S
            regulatory particle in 26S proteasome, disrupting proteasome
            structure in response to oxidative stress.
REFERENCE   3  (residues 1 to 1839)
  AUTHORS   Haratake,K., Sato,A., Tsuruta,F. and Chiba,T.
  TITLE     KIAA0368-deficiency affects disassembly of 26S proteasome under
            oxidative stress condition
  JOURNAL   J Biochem 159 (6), 609-618 (2016)
   PUBMED   26802743
  REMARK    GeneRIF: Ecm29 is involved in the dissociation process of 26S
            proteasome, providing clue to analyse the mechanism of proteasomal
            degradation under various stress condition.
REFERENCE   4  (residues 1 to 1839)
  AUTHORS   Gorbea,C., Rechsteiner,M., Vallejo,J.G. and Bowles,N.E.
  TITLE     Depletion of the 26S proteasome adaptor Ecm29 increases Toll-like
            receptor 3 signaling
  JOURNAL   Sci Signal 6 (295), ra86 (2013)
   PUBMED   24084648
  REMARK    GeneRIF: The absence of Ecm29 enhanced TLR3 signaling, which was
            characterized by the increased abundance of the adaptor protein and
            E3 ubiquitin ligase tumor necrosis factor receptor-associated
            factor 3
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1839)
  AUTHORS   Gorbea,C., Pratt,G., Ustrell,V., Bell,R., Sahasrabudhe,S.,
            Hughes,R.E. and Rechsteiner,M.
  TITLE     A protein interaction network for Ecm29 links the 26 S proteasome
            to molecular motors and endosomal components
  JOURNAL   J Biol Chem 285 (41), 31616-31633 (2010)
   PUBMED   20682791
  REMARK    GeneRIF: Ecm29 serves as an adaptor for coupling 26 S proteasomes
            to specific cellular compartments.
REFERENCE   6  (residues 1 to 1839)
  AUTHORS   Gorbea,C., Goellner,G.M., Teter,K., Holmes,R.K. and Rechsteiner,M.
  TITLE     Characterization of mammalian Ecm29, a 26 S proteasome-associated
            protein that localizes to the nucleus and membrane vesicles
  JOURNAL   J Biol Chem 279 (52), 54849-54861 (2004)
   PUBMED   15496406
  REMARK    GeneRIF: Ecm29 protein serves to couple the 26 S proteasome to
            secretory compartments engaged in quality control and to other
            sites of enhanced proteolysis
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL159168.15 and AL354661.14.
            
            On Jul 17, 2018 this sequence version replaced XP_005251908.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.22682.1,
                                           SRR1803617.228883.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1839
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..1839
                     /product="proteasome adapter and scaffold protein ECM29
                     isoform 3"
                     /note="homolog of yeast Ecm29; ECM29 homolog, proteasome
                     accessory protein; proteasome-associated protein ECM29
                     homolog; ecm29 proteasome adapter and scaffold; proteasome
                     adapter and scaffold protein ECM29"
                     /calculated_mol_wt=203864
     Region          10..516
                     /region_name="Ecm29"
                     /note="Proteasome stabilizer; pfam13001"
                     /db_xref="CDD:463769"
     Region          390..422
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          434..460
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          469..500
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          509..535
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1078..1101
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(1093..1094,1097,1100..1101,1134,1137,1140..1141,
                     1146,1174..1175,1178,1181..1182,1185,1216..1217,1220,
                     1223..1224,1266..1267,1270,1273..1274)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          1113..1146
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1135..1220
                     /region_name="HEAT"
                     /note="HEAT repeat; cl46509"
                     /db_xref="CDD:480849"
     Region          1156..1186
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1195..1224
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1245..1275
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1392..1421
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..1839
                     /gene="ECPAS"
                     /gene_synonym="ECM29; KIAA0368"
                     /coded_by="NM_001364930.1:142..5661"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS94456.1"
                     /db_xref="GeneID:23392"
                     /db_xref="HGNC:HGNC:29020"
                     /db_xref="MIM:616694"
ORIGIN      
        1 myhidcrdql ervflrlgha etdeqlqnii skflppvllk lsstqegvrk kvmellvhln
       61 kriksrpkiq lpvetllvqy qdpaavsfvt nftiiyvkmg yprlpvekqc elaptlltam
      121 egkpqpqqds lmhlliptlf hmkypvessk saspfnlaek pktvqllldf mldvllmpyg
      181 yvlnesqsrq nsssaqgsss nsgggsgipq pppgmsfyaa krvigdnpwt peqleqcklg
      241 ivkfieaeqv peleavlhlv iassdtrhsv ataadlelks kqslidwnnp aiinkmykvy
      301 lgdiplktke gavlkpelkr dpvstrvklk ivphllrsrq aaetfpaniq vvydglfgtn
      361 tnsklrtlsl qfvhhicitc peikikplgp mllngltkli neykedpkll smaysavgkl
      421 ssrmphlftk dialvqqlfe alckeepetr laiqealsmm vgaystlega qrtlmealva
      481 sylikpevqv rqvavkfast vfpsdhipsr yllllaagdp reevhgeaqr vlrclpgrnr
      541 kestseqmps fpemvyyiqe kashrmktpv kymtgttvlp fnpaafgeiv lylrmclahs
      601 agvvptsqsl admqdhapai gryirtlmss gqmapsssnk sgetnpvqiy igllqqllag
      661 vgglpvmycl leavsvypek latkfvdkte wikslmnnsk eemrelaalf ysvvvstvsg
      721 nelksmieql ikttkdnhsp eiqhgsllal gftvgrylak kkmrmseqqd lernadtlpd
      781 qeeliqsate tigsfldsts pllaiaacta lgeigrngpl pipsegsgft klhlveslls
      841 ripssketnk mkeraiqtlg yfpvgdgdfp hqklllqglm dsveakqiel qftigeaits
      901 aaigtssvaa rdawqmteee ytppagakvn dvvpwvldvi lnkhiispnp hvrqaaciwl
      961 lslvrklsth kevkshlkei qsafvsvlse ndelsqdvas kglglvyelg neqdqqelvs
     1021 tlvetlmtgk rvkhevsget vvfqggalgk tpdgqglsty kelcslasdl sqpdlvykfm
     1081 nlanhhamwn srkgaafgfn viatrageql apflpqlvpr lyryqfdpnl girqamtsiw
     1141 nalvtdksmv dkylkeilqd lvknltsnmw rvressclal ndllrgrpld diidklpeiw
     1201 etlfrvqddi kesvrkaael alktlskvcv kmcdpakgaa gqrtiaallp clldkgmmst
     1261 vtevralsin tlvkisksag amlkphapkl ipalleslsv lepqvlnyls lrateqekaa
     1321 mdsarlsaak sspmmetinm clqyldvsvl gelvprlcel irsgvglgtk ggcasvivsl
     1381 ttqcpqdltp ysgklmsall sgltdrnsvi qkscafamgh lvrtsrdsst ekllqklngw
     1441 ymekeepiyk tscaltihai gryspdvlkn hakevlplaf lgmheiadee ksekeecnlw
     1501 tevwqenvpg sfggirlylq elititqkal qsqswkmkaq gaiamasiak qtsslvppyl
     1561 gmiltallqg lagrtwagke ellkaiacvv tacsaeleks vpnqpstnei lqavlkecsk
     1621 envkykivai scaadilkat kedrfqefsn iviplikkns lessgvrttk neeenekeke
     1681 lqleyllgaf eslgkawprn aetqrcyrqe lcklmcerlk lstwkvqlgv lqsmnaffqg
     1741 lmlleeehad pealaeille tcksitysle nktyssvrte alsvielllk kleeskqwec
     1801 ltsecrvlli eslatmepds rpelqekaal lkktlenle
//
LOCUS       NP_001353381             378 aa            linear   PRI 27-APR-2025
DEFINITION  rab GTPase-activating protein 1-like isoform M [Homo sapiens].
ACCESSION   NP_001353381
VERSION     NP_001353381.1
DBSOURCE    REFSEQ: accession NM_001366452.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Anttila,V., Winsvold,B.S., Gormley,P., Kurth,T., Bettella,F.,
            McMahon,G., Kallela,M., Malik,R., de Vries,B., Terwindt,G.,
            Medland,S.E., Todt,U., McArdle,W.L., Quaye,L., Koiranen,M.,
            Ikram,M.A., Lehtimaki,T., Stam,A.H., Ligthart,L., Wedenoja,J.,
            Dunham,I., Neale,B.M., Palta,P., Hamalainen,E., Schurks,M.,
            Rose,L.M., Buring,J.E., Ridker,P.M., Steinberg,S., Stefansson,H.,
            Jakobsson,F., Lawlor,D.A., Evans,D.M., Ring,S.M., Farkkila,M.,
            Artto,V., Kaunisto,M.A., Freilinger,T., Schoenen,J., Frants,R.R.,
            Pelzer,N., Weller,C.M., Zielman,R., Heath,A.C., Madden,P.A.F.,
            Montgomery,G.W., Martin,N.G., Borck,G., Gobel,H., Heinze,A.,
            Heinze-Kuhn,K., Williams,F.M.K., Hartikainen,A.L., Pouta,A., van
            den Ende,J., Uitterlinden,A.G., Hofman,A., Amin,N., Hottenga,J.J.,
            Vink,J.M., Heikkila,K., Alexander,M., Muller-Myhsok,B.,
            Schreiber,S., Meitinger,T., Wichmann,H.E., Aromaa,A.,
            Eriksson,J.G., Traynor,B., Trabzuni,D., Rossin,E., Lage,K.,
            Jacobs,S.B.R., Gibbs,J.R., Birney,E., Kaprio,J., Penninx,B.W.,
            Boomsma,D.I., van Duijn,C., Raitakari,O., Jarvelin,M.R.,
            Zwart,J.A., Cherkas,L., Strachan,D.P., Kubisch,C., Ferrari,M.D.,
            van den Maagdenberg,A.M.J.M., Dichgans,M., Wessman,M., Smith,G.D.,
            Stefansson,K., Daly,M.J., Nyholt,D.R., Chasman,D. and Palotie,A.
  CONSRTM   North American Brain Expression Consortium; UK Brain Expression
            Consortium
  TITLE     Genome-wide meta-analysis identifies new susceptibility loci for
            migraine
  JOURNAL   Nat Genet 45 (8), 912-917 (2013)
   PUBMED   23793025
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Kim,J.H., Jung,S.H., Bae,J.S., Lee,H.S., Yim,S.H., Park,S.Y.,
            Bang,S.Y., Hu,H.J., Shin,H.D., Bae,S.C. and Chung,Y.J.
  TITLE     Deletion variants of RABGAP1L, 10q21.3, and C4 are associated with
            the risk of systemic lupus erythematosus in Korean women
  JOURNAL   Arthritis Rheum 65 (4), 1055-1063 (2013)
   PUBMED   23335107
  REMARK    GeneRIF: Deletion variants of RABGAP1L were found to be
            significantly associated with SLE in Korean women.
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 378)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   8  (residues 1 to 378)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 378)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB088774.1, AB019491.1 and Z99127.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB019491.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1"
     Protein         1..378
                     /product="rab GTPase-activating protein 1-like isoform M"
                     /note="TBC1 domain family, member 18; expressed in
                     hematopoietic cells, heart, liver (HLL); rab
                     GTPase-activating protein 1-like"
                     /calculated_mol_wt=43757
     Region          <1..71
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; pfam00566"
                     /db_xref="CDD:459855"
     Region          <121..>345
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..378
                     /gene="RABGAP1L"
                     /gene_synonym="HHL; TBC1D18"
                     /coded_by="NM_001366452.1:123..1259"
                     /note="isoform M is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS91113.1"
                     /db_xref="GeneID:9910"
                     /db_xref="HGNC:HGNC:24663"
                     /db_xref="MIM:609238"
ORIGIN      
        1 mkeqlpdlhs hfsdlnleah myasqwfltl ftakfplcmv fhiidlllce glniifhval
       61 allktskedl lqadfegalk ffrvqlpkry raeenarrlm eqacnikvpt kklkkyekey
      121 qtmresqlqq edpmdrykre nrrlqeasmr leqenddlah elvtskialr ndldqaedka
      181 dvlnkelllt kqrlveteee krkqeeetaq lkevfrkqle kaeyeikktt aiiaeykqic
      241 sqlstrlekq qaaskeelev vkgkmmackh csdifskega lklaatgred qgietddekd
      301 slkkqlreme lelaqtklql veakckiqel ehqrgalmne iqaaknswfs ktlnsiktat
      361 gtqplqpapv tqppkest
//
LOCUS       NP_001345459             636 aa            linear   PRI 27-APR-2025
DEFINITION  molybdenum cofactor biosynthesis protein 1 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001345459 XP_011512934
VERSION     NP_001345459.1
DBSOURCE    REFSEQ: accession NM_001358530.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Liu,H., Yu,X., He,S. and Li,S.
  TITLE     New Neuroimaging Findings in Patients with Molybdenum Cofactor
            Deficiency Type A: A Case Report and Literature Review
  JOURNAL   Curr Med Imaging 20, 1-7 (2024)
   PUBMED   38389347
  REMARK    GeneRIF: New Neuroimaging Findings in Patients with Molybdenum
            Cofactor Deficiency Type A: A Case Report and Literature Review.
            Review article
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Mayr,S.J., Roper,J. and Schwarz,G.
  TITLE     Alternative splicing of the bicistronic gene molybdenum cofactor
            synthesis 1 (MOCS1) uncovers a novel mitochondrial protein
            maturation mechanism
  JOURNAL   J Biol Chem 295 (10), 3029-3039 (2020)
   PUBMED   31996372
  REMARK    GeneRIF: Alternative splicing of the bicistronic gene molybdenum
            cofactor synthesis 1 (MOCS1) uncovers a novel mitochondrial protein
            maturation mechanism.
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Grings,M., Seminotti,B., Karunanidhi,A., Ghaloul-Gonzalez,L.,
            Mohsen,A.W., Wipf,P., Palmfeldt,J., Vockley,J. and Leipnitz,G.
  TITLE     ETHE1 and MOCS1 deficiencies: Disruption of mitochondrial
            bioenergetics, dynamics, redox homeostasis and endoplasmic
            reticulum-mitochondria crosstalk in patient fibroblasts
  JOURNAL   Sci Rep 9 (1), 12651 (2019)
   PUBMED   31477743
  REMARK    GeneRIF: ETHE1 and MOCS1 deficiencies: Disruption of mitochondrial
            bioenergetics, dynamics, redox homeostasis and endoplasmic
            reticulum-mitochondria crosstalk in patient fibroblasts.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 636)
  AUTHORS   Reiss,J. and Hahnewald,R.
  TITLE     Molybdenum cofactor deficiency: Mutations in GPHN, MOCS1, and MOCS2
  JOURNAL   Hum Mutat 32 (1), 10-18 (2011)
   PUBMED   21031595
  REMARK    Review article
REFERENCE   6  (residues 1 to 636)
  AUTHORS   Reiss,J., Christensen,E., Kurlemann,G., Zabot,M.T. and Dorche,C.
  TITLE     Genomic structure and mutational spectrum of the bicistronic MOCS1
            gene defective in molybdenum cofactor deficiency type A
  JOURNAL   Hum Genet 103 (6), 639-644 (1998)
   PUBMED   9921896
REFERENCE   7  (residues 1 to 636)
  AUTHORS   Feng,G., Tintrup,H., Kirsch,J., Nichol,M.C., Kuhse,J., Betz,H. and
            Sanes,J.R.
  TITLE     Dual requirement for gephyrin in glycine receptor clustering and
            molybdoenzyme activity
  JOURNAL   Science 282 (5392), 1321-1324 (1998)
   PUBMED   9812897
REFERENCE   8  (residues 1 to 636)
  AUTHORS   Reiss,J., Cohen,N., Dorche,C., Mandel,H., Mendel,R.R.,
            Stallmeyer,B., Zabot,M.T. and Dierks,T.
  TITLE     Mutations in a polycistronic nuclear gene associated with
            molybdenum cofactor deficiency
  JOURNAL   Nat Genet 20 (1), 51-53 (1998)
   PUBMED   9731530
REFERENCE   9  (residues 1 to 636)
  AUTHORS   Shalata,A., Mandel,H., Reiss,J., Szargel,R., Cohen-Akenine,A.,
            Dorche,C., Zabot,M.T., Van Gennip,A., Abeling,N., Berant,M. and
            Cohen,N.
  TITLE     Localization of a gene for molybdenum cofactor deficiency, on the
            short arm of chromosome 6, by homozygosity mapping
  JOURNAL   Am J Hum Genet 63 (1), 148-154 (1998)
   PUBMED   9634514
REFERENCE   10 (residues 1 to 636)
  AUTHORS   Misko,A., Mahtani,K., Abbott,J., Schwarz,G. and Atwal,P.
  TITLE     Molybdenum Cofactor Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34870926
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FO393411.1 and CA944911.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 1, 2017 this sequence version replaced XP_011512934.1.
            
            Summary: Molybdenum cofactor biosynthesis is a conserved pathway
            leading to the biological activation of molybdenum. The protein
            encoded by this gene is involved in this pathway. This gene was
            originally thought to produce a bicistronic mRNA with the potential
            to produce two proteins (MOCS1A and MOCS1B) from adjacent open
            reading frames. However, only the first open reading frame (MOCS1A)
            has been found to encode a protein from the putative bicistronic
            mRNA, whereas additional splice variants are likely to produce a
            fusion between the two open reading frames. This gene is defective
            in patients with molybdenum cofactor deficiency, type A. A related
            pseudogene has been identified on chromosome 16. [provided by
            RefSeq, Nov 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.178749.1,
                                           SRR1803616.250766.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152474 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340692.10/ ENSP00000344794.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..636
                     /product="molybdenum cofactor biosynthesis protein 1
                     isoform 7"
                     /EC_number="4.1.99.22"
                     /EC_number="4.6.1.17"
                     /note="molybdenum cofactor biosynthesis protein 1;
                     molybdenum cofactor biosynthesis protein A; MOCS1A enzyme;
                     cell migration-inducing gene 11 protein; molybdenum
                     cofactor synthesis-step 1 protein A-B"
                     /calculated_mol_wt=69974
     Region          1..383
                     /region_name="Molybdenum cofactor biosynthesis protein A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZB8.3)"
     Region          19..383
                     /region_name="PLN02951"
                     /note="Molybderin biosynthesis protein CNX2"
                     /db_xref="CDD:215513"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZB8.3)"
     Site            198
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NZB8.3)"
     Region          414..636
                     /region_name="Molybdenum cofactor biosynthesis protein C"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZB8.3)"
     Region          456..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZB8.3)"
     Region          479..631
                     /region_name="MoaC"
                     /note="Molybdenum cofactor biosynthesis enzyme MoaC
                     [Coenzyme transport and metabolism]; COG0315"
                     /db_xref="CDD:440084"
     Site            528
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKZ7; propagated from
                     UniProtKB/Swiss-Prot (Q9NZB8.3)"
     CDS             1..636
                     /gene="MOCS1"
                     /gene_synonym="MIG11; MOCOD; MOCS1A; MOCS1B"
                     /coded_by="NM_001358530.2:46..1956"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS87394.1"
                     /db_xref="GeneID:4337"
                     /db_xref="HGNC:HGNC:7190"
                     /db_xref="MIM:603707"
ORIGIN      
        1 maarplsrml rrllrssars cssgapvtqp cpgesaraas eevsrrrqfl rehaapfsaf
       61 ltdsfgrqhs ylrisltekc nlrcqycmpe egvpltpkan lltteeiltl arlfvkegid
      121 kirltggepl irpdvvdiva qlqrleglrt igvttnginl arllpqlqka glsainisld
      181 tlvpakfefi vrrkgfhkvm egihkaielg ynpvkvncvv mrglnedell dfaalteglp
      241 ldvrfieymp fdgnkwnfkk mvsykemldt vrqqwpelek vpeeesstak afkipgfqgq
      301 isfitsmseh fcgtcnrlri tadgnlkvcl fgnsevslrd hlragaseqe llriigaavg
      361 rkkrqhagmf sisqmknrpm ilielflmfp nsppanpsif swdplhvqgl rprmsfssqv
      421 atlwkgcrvp qtpplaqqrl gsgsfqrhyt sradsdansk clspgswasa apsgpqltse
      481 qlthvdsegr aamvdvgrkp dtervavasa vvllgpvafk lvqqnqlkkg dalvvaqlag
      541 vqaakvtsql iplchhvals hiqvqlelds trhavkiqas crargptgve mealtsaava
      601 altlydmcka vsrdivleei klisktggqr gdfhra
//
LOCUS       NP_001354771             256 aa            linear   PRI 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 2 [Homo sapiens].
ACCESSION   NP_001354771
VERSION     NP_001354771.1
DBSOURCE    REFSEQ: accession NM_001367842.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Lu,J., Li,H., Zhang,H., Lin,Z., Xu,C., Xu,X., Hu,L., Luan,Z.,
            Lou,Y. and Tang,S.
  TITLE     The distal arthrogryposis-linked p.R63C variant promotes the
            stability and nuclear accumulation of TNNT3
  JOURNAL   J Clin Lab Anal 35 (12), e24089 (2021)
   PUBMED   34766372
  REMARK    GeneRIF: The distal arthrogryposis-linked p.R63C variant promotes
            the stability and nuclear accumulation of TNNT3.
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Nunez Lopez,Y.O., Messi,M.L., Pratley,R.E., Zhang,T. and Delbono,O.
  TITLE     Troponin T3 associates with DNA consensus sequence that overlaps
            with p53 binding motifs
  JOURNAL   Exp Gerontol 108, 35-40 (2018)
   PUBMED   29596868
  REMARK    GeneRIF: The TnT3 appears to contribute to age-related sarcopenia
            and possibly other age-related deficiencies such as muscle insulin
            resistance and beta cell dysfunction by interacting with
            TnT3-binding sequences in the promoter area of p53-related genes,
            among others, and consequently modulating the transcriptional
            regulation of these target genes.
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Wei,B. and Jin,J.P.
  TITLE     TNNT1, TNNT2, and TNNT3: Isoform genes, regulation, and
            structure-function relationships
  JOURNAL   Gene 582 (1), 1-13 (2016)
   PUBMED   26774798
  REMARK    GeneRIF: Three homologous genes have evolved in vertebrates to
            encode three muscle type-specific TnT isoforms: TNNT1 for slow
            skeletal muscle TnT, TNNT2 for cardiac muscle TnT, and TNNT3 for
            fast skeletal muscle TnT.
            Review article
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Vorster,A.A., Beighton,P. and Ramesar,R.S.
  TITLE     Digitotalar dysmorphism: Molecular elucidation
  JOURNAL   S Afr Med J 106 (3), 253-255 (2016)
   PUBMED   26915936
  REMARK    GeneRIF: The presence of the p.(Arg63His) missense mutation at
            position 63 of TNNT3 was confirmed through direct cycle sequencing
            of genomic DNA in six affected South African family members for
            whom DNA had been archived.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Lindstrom,S., Thompson,D.J., Paterson,A.D., Li,J., Gierach,G.L.,
            Scott,C., Stone,J., Douglas,J.A., dos-Santos-Silva,I.,
            Fernandez-Navarro,P., Verghase,J., Smith,P., Brown,J., Luben,R.,
            Wareham,N.J., Loos,R.J., Heit,J.A., Pankratz,V.S., Norman,A.,
            Goode,E.L., Cunningham,J.M., deAndrade,M., Vierkant,R.A., Czene,K.,
            Fasching,P.A., Baglietto,L., Southey,M.C., Giles,G.G., Shah,K.P.,
            Chan,H.P., Helvie,M.A., Beck,A.H., Knoblauch,N.W., Hazra,A.,
            Hunter,D.J., Kraft,P., Pollan,M., Figueroa,J.D., Couch,F.J.,
            Hopper,J.L., Hall,P., Easton,D.F., Boyd,N.F., Vachon,C.M. and
            Tamimi,R.M.
  TITLE     Genome-wide association study identifies multiple loci associated
            with both mammographic density and breast cancer risk
  JOURNAL   Nat Commun 5, 5303 (2014)
   PUBMED   25342443
  REMARK    Erratum:[Nat Commun. 2015 Sep 09;6:8358. doi: 10.1038/ncomms9358.
            PMID: 26349435]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Stefancsik,R., Randall,J.D., Mao,C. and Sarkar,S.
  TITLE     Structure and sequence of the human fast skeletal troponin T
            (TNNT3) gene: insight into the evolution of the gene and the origin
            of the developmentally regulated isoforms
  JOURNAL   Comp Funct Genomics 4 (6), 609-625 (2003)
   PUBMED   18629027
  REMARK    Erratum:[Comp Funct Genomics. 2004;5(2):205]
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Briggs,M.M., Maready,M., Schmidt,J.M. and Schachat,F.
  TITLE     Identification of a fetal exon in the human fast troponin T gene
  JOURNAL   FEBS Lett 350 (1), 37-40 (1994)
   PUBMED   8062920
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Wu,Q.L., Jha,P.K., Raychowdhury,M.K., Du,Y., Leavis,P.C. and
            Sarkar,S.
  TITLE     Isolation and characterization of human fast skeletal beta troponin
            T cDNA: comparative sequence analysis of isoforms and insight into
            the evolution of members of a multigene family
  JOURNAL   DNA Cell Biol 13 (3), 217-233 (1994)
   PUBMED   8172653
REFERENCE   10 (residues 1 to 256)
  AUTHORS   Chong,P.C. and Hodges,R.S.
  TITLE     Photochemical cross-linking between rabbit skeletal troponin
            subunits. Troponin I-troponin T interactions
  JOURNAL   J Biol Chem 257 (19), 11667-11672 (1982)
   PUBMED   7118902
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC171727.1 and AC051649.21.
            
            Summary: The binding of Ca(2+) to the trimeric troponin complex
            initiates the process of muscle contraction. Increased Ca(2+)
            concentrations produce a conformational change in the troponin
            complex that is transmitted to tropomyosin dimers situated along
            actin filaments. The altered conformation permits increased
            interaction between a myosin head and an actin filament which,
            ultimately, produces a muscle contraction. The troponin complex has
            protein subunits C, I, and T. Subunit C binds Ca(2+) and subunit I
            binds to actin and inhibits actin-myosin interaction. Subunit T
            binds the troponin complex to the tropomyosin complex and is also
            required for Ca(2+)-mediated activation of actomyosin ATPase
            activity. There are 3 different troponin T genes that encode
            tissue-specific isoforms of subunit T for fast skeletal-, slow
            skeletal-, and cardiac-muscle. This gene encodes fast skeletal
            troponin T protein; also known as troponin T type 3. Alternative
            splicing results in multiple transcript variants encoding
            additional distinct troponin T type 3 isoforms. A developmentally
            regulated switch between fetal/neonatal and adult troponin T type 3
            isoforms occurs. Additional splice variants have been described but
            their biological validity has not been established. Mutations in
            this gene may cause distal arthrogryposis multiplex congenita type
            2B (DA2B). [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (7), as well as variant 2, encodes
            isoform 2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.284410.1,
                                           ERR279830.7826.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..256
                     /product="troponin T, fast skeletal muscle isoform 2"
                     /note="troponin T, fast skeletal muscle; troponin T type 3
                     (skeletal, fast)"
                     /calculated_mol_wt=30218
     Region          60..196
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..256
                     /gene="TNNT3"
                     /gene_synonym="beta-TnTF; DA2B2; TNTF"
                     /coded_by="NM_001367842.1:45..815"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS41594.1"
                     /db_xref="GeneID:7140"
                     /db_xref="HGNC:HGNC:11950"
                     /db_xref="MIM:600692"
ORIGIN      
        1 msdeeveqve eqyeeeeeaq eeaaevheev hepeekprpk ltapkipege kvdfddiqkk
       61 rqnkdlmelq alidshfear kkeeeelval keriekrrae raeqqrirae kererqnrla
      121 eekarreeed akrraeddlk kkkalssmga nyssylakad qkrgkkqtar emkkkilaer
      181 rkplnidhlg edklrdkake lwetlhqlei dkfefgeklk rqkydittlr sridqaqkhs
      241 kkagtpakgk vggrwk
//
LOCUS       NP_542778                542 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 280A [Homo sapiens].
ACCESSION   NP_542778
VERSION     NP_542778.2
DBSOURCE    REFSEQ: accession NM_080740.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   He,L., Wang,X., Chen,P., Du,C. and Li,J.
  TITLE     Knockdown of ZNF280A inhibits cell proliferation and promotes cell
            apoptosis of bladder cancer
  JOURNAL   Histol Histopathol 39 (3), 367-379 (2024)
   PUBMED   37345848
  REMARK    GeneRIF: Knockdown of ZNF280A inhibits cell proliferation and
            promotes cell apoptosis of bladder cancer.
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Liu,H., Qin,Y., Zhou,N., Ma,D. and Wang,Y.
  TITLE     ZNF280A promotes lung adenocarcinoma development by regulating the
            expression of EIF3C
  JOURNAL   Cell Death Dis 12 (1), 39 (2021)
   PUBMED   33414445
  REMARK    GeneRIF: ZNF280A promotes lung adenocarcinoma development by
            regulating the expression of EIF3C.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Kawasaki,K., Minoshima,S., Nakato,E., Shibuya,K., Shintani,A.,
            Schmeits,J.L., Wang,J. and Shimizu,N.
  TITLE     One-megabase sequence analysis of the human immunoglobulin lambda
            gene locus
  JOURNAL   Genome Res 7 (3), 250-261 (1997)
   PUBMED   9074928
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP283207.1, AC246793.1 and
            BC053901.1.
            
            On Apr 24, 2014 this sequence version replaced NP_542778.1.
            
            Summary: This gene encodes a zinc finger protein. The encoded
            protein contains 4 C2H2-type zinc fingers, which are commonly found
            in transcription factors. A variety of functions may be performed
            by this type of zinc finger protein, including the binding of DNA
            or RNA. [provided by RefSeq, Apr 2014].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053901.1, AK093108.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302097.3/ ENSP00000302855.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.22"
     Protein         1..542
                     /product="zinc finger protein 280A"
                     /note="zinc finger protein 280; zinc finger protein 636;
                     suppressor of hairy wing homolog 1"
                     /calculated_mol_wt=60453
     Region          47..217
                     /region_name="DUF4195"
                     /note="Domain of unknown function (DUF4195); pfam13836"
                     /db_xref="CDD:463993"
     Region          66..185
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59817.4)"
     Region          336..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          499..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59817.4)"
     CDS             1..542
                     /gene="ZNF280A"
                     /gene_synonym="3'OY11.1; SUHW1; ZNF280; ZNF636"
                     /coded_by="NM_080740.5:254..1882"
                     /db_xref="CCDS:CCDS13800.1"
                     /db_xref="GeneID:129025"
                     /db_xref="HGNC:HGNC:18597"
ORIGIN      
        1 mgdiflckkv espkknlres kqreeddedp dliyvgvehv hrdaevlfvg misnskpvvs
       61 nilnrvtpgs nsrrkkghfr qypahvsqpa nhvtsmakai mpvslsegrs tdspvtmkss
      121 sepgykmssp qvvspsssds lppgtqclvg amvsgggrne sspdskrlst sdinsrdskr
      181 vklrdgipgv pslavvpsdm sstistntps qgicnssnhv qngvtfpwpd angkahfnlt
      241 dperasesal amtdisslas qnktfdpkke npivllsdfy ygqhkgdgqp eqkthttfkc
      301 lscvkvlkni kfmnhmkhhl efekqrndsw edhttcqhch rqfptpfqlq chidsvhiam
      361 gpsavckice lsfetdqvll qhmkdhhkpg empyvcqvch yrssvfadve thfrtchent
      421 knllclfclk lfktaipymn hcwrhsrrrv lqcskcrlqf ltlkeeiehk tkdhqtfkkp
      481 eqlqglpset kviiqtsvqp gssgmasviv sntdpqsspv ktkkktamnt rdsrlpcskd
      541 ss
//
LOCUS       NP_113553                811 aa            linear   ROD 27-APR-2025
DEFINITION  phosphoinositide 3-kinase adapter protein 1 [Mus musculus].
ACCESSION   NP_113553
VERSION     NP_113553.1
DBSOURCE    REFSEQ: accession NM_031376.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Irizarry-Caro,R.A., McDaniel,M.M., Overcast,G.R., Jain,V.G.,
            Troutman,T.D. and Pasare,C.
  TITLE     TLR signaling adapter BCAP regulates inflammatory to reparatory
            macrophage transition by promoting histone lactylation
  JOURNAL   Proc Natl Acad Sci U S A 117 (48), 30628-30638 (2020)
   PUBMED   33199625
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Miao,Y., Jiang,M., Qi,L., Yang,D., Xiao,W. and Fang,F.
  TITLE     BCAP Regulates Dendritic Cell Maturation Through the
            Dual-Regulation of NF-kappaB and PI3K/AKT Signaling During
            Infection
  JOURNAL   Front Immunol 11, 250 (2020)
   PUBMED   32133012
  REMARK    GeneRIF: BCAP Regulates Dendritic Cell Maturation Through the
            Dual-Regulation of NF-kappaB and PI3K/AKT Signaling During
            Infection.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 811)
  AUTHORS   Carpentier,S.J., Ni,M., Duggan,J.M., James,R.G., Cookson,B.T. and
            Hamerman,J.A.
  TITLE     The signaling adaptor BCAP inhibits NLRP3 and NLRC4 inflammasome
            activation in macrophages through interactions with Flightless-1
  JOURNAL   Sci Signal 12 (581) (2019)
   PUBMED   31088976
  REMARK    GeneRIF: B-cell phosphoinositide 3-kinase adapter protein 1 (BCAP)
            delayed the recruitment and activation of pro-caspase-1 within the
            NLRP3/ASC preinflammasome through its association with
            Flightless-1, suggesting BCAP is a multifunctional signaling
            adaptor that inhibits key pathogen-sensing pathways in macrophages.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 811)
  AUTHORS   Chu,T., Ni,M., Chen,C., Akilesh,S. and Hamerman,J.A.
  TITLE     Cutting Edge: BCAP Promotes Lupus-like Disease and TLR-Mediated
            Type I IFN Induction in Plasmacytoid Dendritic Cells
  JOURNAL   J Immunol 202 (9), 2529-2534 (2019)
   PUBMED   30936294
  REMARK    GeneRIF: a novel role for BCAP in promoting TLR-induced IFN-alpha
            production in pDC and in systemic lupus erythematosus pathogenesis.
REFERENCE   6  (residues 1 to 811)
  AUTHORS   Papin,J. and Subramaniam,S.
  TITLE     Bioinformatics and cellular signaling
  JOURNAL   Curr Opin Biotechnol 15 (1), 78-81 (2004)
   PUBMED   15102471
  REMARK    Review article
REFERENCE   7  (residues 1 to 811)
  AUTHORS   Yamazaki,T. and Kurosaki,T.
  TITLE     Contribution of BCAP to maintenance of mature B cells through c-Rel
  JOURNAL   Nat Immunol 4 (8), 780-786 (2003)
   PUBMED   12833156
REFERENCE   8  (residues 1 to 811)
  AUTHORS   Yamazaki,T. and Kurosaki,T.
  TITLE     [Immunoregulatory role for BCAP in B cell development and function]
  JOURNAL   Tanpakushitsu Kakusan Koso 47 (16 Suppl), 2242-2247 (2002)
   PUBMED   12518443
  REMARK    GeneRIF: plays an immunoregulatory role in B cell development and
            function--review
            Review article
REFERENCE   9  (residues 1 to 811)
  AUTHORS   Yamazaki,T., Takeda,K., Gotoh,K., Takeshima,H., Akira,S. and
            Kurosaki,T.
  TITLE     Essential immunoregulatory role for BCAP in B cell development and
            function
  JOURNAL   J Exp Med 195 (5), 535-545 (2002)
   PUBMED   11877477
REFERENCE   10 (residues 1 to 811)
  AUTHORS   Okada,T., Maeda,A., Iwamatsu,A., Gotoh,K. and Kurosaki,T.
  TITLE     BCAP: the tyrosine kinase substrate that connects B cell receptor
            to phosphoinositide 3-kinase activation
  JOURNAL   Immunity 13 (6), 817-827 (2000)
   PUBMED   11163197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC112271.4 and AC133099.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK171021.1, AK154326.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 34.61 cM"
     Protein         1..811
                     /product="phosphoinositide 3-kinase adapter protein 1"
                     /note="B-cell adapter for phosphoinositide 3-kinase;
                     B-cell phosphoinositide 3-kinase adapter protein 1; B cell
                     phosphoinositide 3-kinase adaptor"
                     /calculated_mol_wt=90798
     Region          10..145
                     /region_name="Necessary and sufficient to mediate
                     inhibition of NF-kappa-B downstream of activated TLRs, may
                     mediate interaction with MYD88 and TIRAP.
                     /evidence=ECO:0000269|PubMed:22187460"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Region          11..142
                     /region_name="TIR_3"
                     /note="Toll/interleukin-1 receptor domain; pfam18567"
                     /db_xref="CDD:436583"
     Region          146..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Region          181..319
                     /region_name="DBB"
                     /note="Dof, BCAP, and BANK (DBB) motif; pfam14545"
                     /db_xref="CDD:464205"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:11163197,
                     ECO:0000269|PubMed:18025150; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SYK.
                     /evidence=ECO:0000305|PubMed:11163197,
                     ECO:0000305|PubMed:18025150, ECO:0000305|PubMed:20728433;
                     propagated from UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SYK.
                     /evidence=ECO:0000305|PubMed:11163197,
                     ECO:0000305|PubMed:18025150, ECO:0000305|PubMed:20728433;
                     propagated from UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SYK.
                     /evidence=ECO:0000305|PubMed:11163197,
                     ECO:0000305|PubMed:18025150, ECO:0000305|PubMed:20728433;
                     propagated from UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000250|UniProtKB:Q6ZUJ8; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Region          525..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000250|UniProtKB:Q6ZUJ8; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000250|UniProtKB:Q6ZUJ8; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000250|UniProtKB:Q6ZUJ8; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZUJ8; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000250|UniProtKB:Q6ZUJ8; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Region          702..811
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQ32.1)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZUJ8; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ32.1)"
     CDS             1..811
                     /gene="Pik3ap1"
                     /gene_synonym="1810044J04Rik; BCAP"
                     /coded_by="NM_031376.4:134..2569"
                     /db_xref="CCDS:CCDS37987.1"
                     /db_xref="GeneID:83490"
                     /db_xref="MGI:MGI:1933177"
ORIGIN      
        1 maasgwgrgc dilifyspda eewcqylqdl fvscrqvrsq ktqtyrlvpd asfsaqdlwv
       61 frdarcvlvl lsaglvgcfg qpgllpmlqr achppqrvvr llcgvqpgde dfqaffpdwa
      121 hwqemtcdde petylaavrk aisedsgcds vtdtepeder elpfskqtnl ppeispgnlm
      181 vvqpdrircg aettvyiivr ckldekvste aefspedsps irvegtlene ytvsvkapdl
      241 ssgnvslkvy sgdlvvcett vsyytdmeei gnllssaanp vefmcqafki vpyntetldk
      301 llteslknni pasglhlfgi nqleeddmmt nqrdeelptl lhfaakyglk nltallltcp
      361 galqaysvan khghypntia ekhgfrdlrq fideyvetvd mlkthikeel mqgeeaddvy
      421 esmahlstdl lmkcslnpgc ddelyesmaa fapaatedly vemlqasagn pvsgesfsrp
      481 tkdsmirkfl egnsvkpasw ereqhhpyge elyhivdede tfsvdlanrp pvpvprpeas
      541 apgpppppdn epyiskvfae ksqerlgnfy vssesirkep lvrpwrdrpp ssiydpfagm
      601 ktpgqrqlit lqeqvklgiv nvdeavlhfk ewqlnqkkrs esfrfqqenl krlresitrr
      661 rkekpksgkh tdleitvpir hsqhlpekve fgvyesgprk svlpartelr rgdwktdsms
      721 stasstsnrs strsllsvss gmegdnedne ipeitrsrgp gptqvdgapv vtgtpvgtle
      781 rpprvppraa sqrpltresf hppppvpprg r
//
LOCUS       NP_660328                364 aa            linear   PRI 27-APR-2025
DEFINITION  homeobox protein Nkx-2.3 [Homo sapiens].
ACCESSION   NP_660328
VERSION     NP_660328.2
DBSOURCE    REFSEQ: accession NM_145285.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Gabris,F., Kajtar,B., Kellermayer,Z. and Balogh,P.
  TITLE     Quantitative Analysis of NKX2-3 Expression in Human Colon: An
            Immunohistochemical Study
  JOURNAL   J Histochem Cytochem 72 (1), 11-23 (2024)
   PUBMED   38063211
  REMARK    GeneRIF: Quantitative Analysis of NKX2-3 Expression in Human Colon:
            An Immunohistochemical Study.
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Hu,M., Chen,N., Chen,M., Chen,F., Lu,Y., Xu,Y., Yang,L., Zeng,H.,
            Shen,M., Chen,X., Chen,S., Wang,F., Wang,S. and Wang,J.
  TITLE     Transcription factor Nkx2-3 maintains the self-renewal of
            hematopoietic stem cells by regulating mitophagy
  JOURNAL   Leukemia 37 (6), 1361-1374 (2023)
   PUBMED   37095209
  REMARK    GeneRIF: Transcription factor Nkx2-3 maintains the self-renewal of
            hematopoietic stem cells by regulating mitophagy.
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Nagel,S., Pommerenke,C., Meyer,C. and MacLeod,R.A.F.
  TITLE     NKL Homeobox Genes NKX2-3 and NKX2-4 Deregulate
            Megakaryocytic-Erythroid Cell Differentiation in AML
  JOURNAL   Int J Mol Sci 22 (21), 11434 (2021)
   PUBMED   34768865
  REMARK    GeneRIF: NKL Homeobox Genes NKX2-3 and NKX2-4 Deregulate
            Megakaryocytic-Erythroid Cell Differentiation in AML.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Liu,C., Wu,W., Xu,M., Mi,J., Xu,L. and Wang,R.
  TITLE     Development and Validation of an Autophagy-Related Signature for
            Head and Neck Squamous Cell Carcinoma
  JOURNAL   Biomed Res Int 2021, 1028158 (2021)
   PUBMED   34423028
  REMARK    GeneRIF: Development and Validation of an Autophagy-Related
            Signature for Head and Neck Squamous Cell Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Burlet,B., Ramla,S., Fournier,C., Abrey-Recalde,M.J., Sauter,C.,
            Chretien,M.L., Rossi,C., Duffourd,Y., Ragot,S., Buriller,C.,
            Tournier,B., Chapusot,C., Nadal,N., Racine,J., Guy,J., Bailly,F.,
            Martin,L., Casasnovas,O., Bastie,J.N., Caillot,D., Albuisson,J.,
            Broccardo,C., Thieblemont,C., Delva,L., Maynadie,M., Aucagne,R. and
            Callanan,M.B.
  TITLE     Identification of novel, clonally stable, somatic mutations
            targeting transcription factors PAX5 and NKX2-3, the epigenetic
            regulator LRIF1, and BRAF in a case of atypical B-cell chronic
            lymphocytic leukemia harboring a t(14;18)(q32;q21)
  JOURNAL   Cold Spring Harb Mol Case Stud 7 (1), a005934 (2021)
   PUBMED   33608382
  REMARK    GeneRIF: Identification of novel, clonally stable, somatic
            mutations targeting transcription factors PAX5 and NKX2-3, the
            epigenetic regulator LRIF1, and BRAF in a case of atypical B-cell
            chronic lymphocytic leukemia harboring a t(14;18)(q32;q21).
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Parkes,M., Barrett,J.C., Prescott,N.J., Tremelling,M.,
            Anderson,C.A., Fisher,S.A., Roberts,R.G., Nimmo,E.R.,
            Cummings,F.R., Soars,D., Drummond,H., Lees,C.W., Khawaja,S.A.,
            Bagnall,R., Burke,D.A., Todhunter,C.E., Ahmad,T., Onnie,C.M.,
            McArdle,W., Strachan,D., Bethel,G., Bryan,C., Lewis,C.M.,
            Deloukas,P., Forbes,A., Sanderson,J., Jewell,D.P., Satsangi,J.,
            Mansfield,J.C., Cardon,L. and Mathew,C.G.
  CONSRTM   Wellcome Trust Case Control Consortium
  TITLE     Sequence variants in the autophagy gene IRGM and multiple other
            replicating loci contribute to Crohn's disease susceptibility
  JOURNAL   Nat Genet 39 (7), 830-832 (2007)
   PUBMED   17554261
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 364)
  CONSRTM   Wellcome Trust Case Control Consortium
  TITLE     Genome-wide association study of 14,000 cases of seven common
            diseases and 3,000 shared controls
  JOURNAL   Nature 447 (7145), 661-678 (2007)
   PUBMED   17554300
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Biben,C., Wang,C.C. and Harvey,R.P.
  TITLE     NK-2 class homeobox genes and pharyngeal/oral patterning: Nkx2-3 is
            required for salivary gland and tooth morphogenesis
  JOURNAL   Int J Dev Biol 46 (4), 415-422 (2002)
   PUBMED   12141427
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Phiel,C.J., Gabbeta,V., Parsons,L.M., Rothblat,D., Harvey,R.P. and
            McHugh,K.M.
  TITLE     Differential binding of an SRF/NK-2/MEF2 transcription factor
            complex in normal versus neoplastic smooth muscle tissues
  JOURNAL   J Biol Chem 276 (37), 34637-34650 (2001)
   PUBMED   11457859
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Harvey,R.P.
  TITLE     NK-2 homeobox genes and heart development
  JOURNAL   Dev Biol 178 (2), 203-216 (1996)
   PUBMED   8812123
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI764885.1, BC025788.1 and
            AL353719.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 9, 2007 this sequence version replaced NP_660328.1.
            
            Summary: This gene encodes a homeodomain-containing transcription
            factor. The encoded protein is a member of the NKX family of
            homeodomain transcription factors. Studies of similar proteins in
            mouse and rat have indicated a potential role in cellular
            differentiation.[provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA935495.1, AK300856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344586.9/ ENSP00000342828.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..364
                     /product="homeobox protein Nkx-2.3"
                     /note="homeobox protein NK-2 homolog C; NK2 transcription
                     factor related, locus 3"
                     /calculated_mol_wt=38275
     Region          132..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAU0.2)"
     Region          149..205
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..364
                     /gene="NKX2-3"
                     /gene_synonym="CSX3; NK2.3; NKX2.3; NKX2C; NKX4-3"
                     /coded_by="NM_145285.3:191..1285"
                     /db_xref="CCDS:CCDS41558.1"
                     /db_xref="GeneID:159296"
                     /db_xref="HGNC:HGNC:7836"
                     /db_xref="MIM:606727"
ORIGIN      
        1 mmlpspvtst pfsvkdilnl eqqhqhfhga hlqadlehhf hsapcmlaaa egtqfsdgge
       61 edeedegekl sylnslaaad ghgdsglcpq gyvhtvlrds csepkeheee pevvrdrsqk
      121 scqlkkslet agdckaaees erpkprsrrk prvlfsqaqv felerrfkqq rylsapereh
      181 lasslkltst qvkiwfqnrr ykckrqrqdk slelgahapp ppprrvavpv lvrdgkpcvt
      241 psaqaygapy svgasaysyn sfpaygygns aaaaaaaaaa aaaaaaysss ygcaypaggg
      301 gggggtsaat tamqpacsaa gggpfvnvsn lggfgsggsa qplhqgtaag aacaqgtlqg
      361 iraw
//
LOCUS       NP_001229410             165 aa            linear   PRI 27-APR-2025
DEFINITION  probable RNA-binding protein EIF1AD [Homo sapiens].
ACCESSION   NP_001229410
VERSION     NP_001229410.1
DBSOURCE    REFSEQ: accession NM_001242481.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Yu,J. and Marintchev,A.
  TITLE     Comparative sequence and structure analysis of eIF1A and eIF1AD
  JOURNAL   BMC Struct Biol 18 (1), 11 (2018)
   PUBMED   30180896
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Smirnova,E.V., Rakitina,T.V., Bogatova,O.V., Ivanova,D.L.,
            Vorobyeva,E.E., Lipkin,A.V., Kostanyan,I.A. and Lipkin,V.M.
  TITLE     Novel protein haponin regulates cellular response to oxidative
            stress
  JOURNAL   Dokl Biochem Biophys 440, 225-227 (2011)
   PUBMED   22095125
  REMARK    GeneRIF: Novel protein haponin regulates cellular response to
            oxidative stress.
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   8  (residues 1 to 165)
  AUTHORS   Vonarshenko,A.V., Radchenko,V.V., Gapon,M.V., Rodionov,I.L.,
            Babichenko,I.I., Kakuev,D.L., Artamonov,I.D., Garkovenko,A.V.,
            D'iachkova,L.G., Lipkin,V.M. and Kostanian,I.A.
  TITLE     [Identification and expression of haponin, a new protein from HL-60
            cells]
  JOURNAL   Bioorg Khim 33 (6), 653-656 (2007)
   PUBMED   18173130
REFERENCE   9  (residues 1 to 165)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP328412.1, BE791453.1, AI831454.1, BE669813.1 and AP006287.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.178571.1,
                                           SRR1660803.45698.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152719, SAMEA2153031
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000533544.6/ ENSP00000434056.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..165
                     /product="probable RNA-binding protein EIF1AD"
                     /note="eukaryotic translation initiation factor 1A
                     domain-containing protein"
                     /calculated_mol_wt=18922
     Region          6..12
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Region          25..102
                     /region_name="S1_eIF1AD_like"
                     /note="eukaryotic translation initiation factor 1A domain
                     containing protein (eIF1AD)-like, S1-like RNA-binding
                     domain. eIF1AD is also known as MGC11102 protein. Little
                     is known about the function of eIF1AD. S1-like RNA-binding
                     domains are found in a wide...; cd05792"
                     /db_xref="CDD:240218"
     Site            order(33..34,38,52..55,58,63)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:240218"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Region          56..65
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Region          112..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3THJ3; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKI6; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3THJ3; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKI6; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     CDS             1..165
                     /gene="EIF1AD"
                     /gene_synonym="haponin; OBELIX"
                     /coded_by="NM_001242481.2:365..862"
                     /db_xref="CCDS:CCDS8124.1"
                     /db_xref="GeneID:84285"
                     /db_xref="HGNC:HGNC:28147"
                     /db_xref="MIM:618473"
ORIGIN      
        1 msqatkrkhv vkevlgehiv psdqqqivrv lrtpgnnlhe vetaqgqrfl vsmpskyrkn
       61 iwikrgdfli vdpieegekv kaeisfvlck dhvrslqkeg fwpeafseva ekhnnrnrqt
      121 qpelpaepql sgeesssedd sdlfvntnrr qyheseeese eeeaa
//
LOCUS       NP_001258578             172 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 138 isoform 4 [Homo sapiens].
ACCESSION   NP_001258578
VERSION     NP_001258578.1
DBSOURCE    REFSEQ: accession NM_001271649.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073349.11.
            
            Transcript Variant: This variant (4) lacks an alternate coding
            exon, and initiates translation at a downstream in-frame start
            codon, compared to variant 1. The encoded isoform (4) has a shorter
            N-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.27426.1,
                                           SRR3476690.156363.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..172
                     /product="zinc finger protein 138 isoform 4"
                     /note="zinc finger protein 138 (clone pHZ-32)"
                     /calculated_mol_wt=20100
     Region          22..42
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          50..70
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(55,57,59,61..62,65..66,69,83,85,89..90,93..94,97,
                     111,113,115,117..118,121..122,125)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <72..155
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          78..98
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          106..126
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          134..151
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..172
                     /gene="ZNF138"
                     /gene_synonym="pHZ-32"
                     /coded_by="NM_001271649.2:378..896"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:7697"
                     /db_xref="HGNC:HGNC:12922"
                     /db_xref="MIM:604080"
ORIGIN      
        1 mhkfsnsnrh kirhtenkhf rckecdkslc mlsrltqhkk ihtrenfykc eecgktfnws
       61 tnlskpkkih tgekpykcev cgkafhqssi ltkhkiirtg ekpykcahcg kafkqsshlt
      121 rhkiihteek pykceqcgkv fkqsptltkh qiiytgeepy kceecgkafn ls
//
LOCUS       NP_689757                757 aa            linear   PRI 27-APR-2025
DEFINITION  probable tRNA (uracil-O(2)-)-methyltransferase isoform 2 [Homo
            sapiens].
ACCESSION   NP_689757
VERSION     NP_689757.2
DBSOURCE    REFSEQ: accession NM_152544.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Wade,R., Di Bernardo,M.C., Richards,S., Rossi,D.,
            Crowther-Swanepoel,D., Gaidano,G., Oscier,D.G., Catovsky,D. and
            Houlston,R.S.
  TITLE     Association between single nucleotide polymorphism-genotype and
            outcome of patients with chronic lymphocytic leukemia in a
            randomized chemotherapy trial
  JOURNAL   Haematologica 96 (10), 1496-1503 (2011)
   PUBMED   21659360
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Leschziner,G.D., Coffey,A.J., Andrew,T., Gregorio,S.P.,
            Dias-Neto,E., Calafato,M., Bentley,D.R., Kinton,L., Sander,J.W. and
            Johnson,M.R.
  TITLE     Q8IYL2 is a candidate gene for the familial epilepsy syndrome of
            Partial Epilepsy with Pericentral Spikes (PEPS)
  JOURNAL   Epilepsy Res 96 (1-2), 109-115 (2011)
   PUBMED   21658913
  REMARK    GeneRIF: This study postulated that Q8IYL2 is a causative gene for
            PEPS , after exhaustive resequencing and bioinformatic analysis.
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Knizewski,L. and Ginalski,K.
  TITLE     DUF1613 is a novel family of eucaryotic AdoMet-dependent
            methyltransferases
  JOURNAL   Cell Cycle 5 (14), 1580-1582 (2006)
   PUBMED   16861910
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104825.4, CB991944.1,
            AC105345.3 and CA450523.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 11, 2010 this sequence version replaced NP_689757.1.
            
            Summary: The protein encoded by this gene is a putative tRNA
            methyltransferase found in the cytoplasm. Defects in this gene may
            be a cause of partial epilepsy with pericentral spikes (PEPS), but
            that has not been proven definitively. [provided by RefSeq, May
            2012].
            
            Transcript Variant: This variant (2) encodes the longer isoform
            (2).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.73682.1,
                                           SRR1660803.74235.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389737.5/ ENSP00000374387.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.1"
     Protein         1..757
                     /product="probable tRNA (uracil-O(2)-)-methyltransferase
                     isoform 2"
                     /EC_number="2.1.1.211"
                     /note="probable tRNA (uracil-O(2)-)-methyltransferase;
                     methyltransferase-like protein 19; methyltransferase like
                     19"
                     /calculated_mol_wt=84498
     Region          55..93
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL2.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL2.2)"
     Region          108..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL2.2)"
     Region          296..407
                     /region_name="AdoMet_MTase"
                     /note="Predicted AdoMet-dependent methyltransferase;
                     pfam07757"
                     /db_xref="CDD:462255"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL2.2)"
     CDS             1..757
                     /gene="TRMT44"
                     /gene_synonym="C4orf23; METTL19; TRM44"
                     /coded_by="NM_152544.3:47..2320"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3402.2"
                     /db_xref="GeneID:152992"
                     /db_xref="HGNC:HGNC:26653"
                     /db_xref="MIM:614309"
ORIGIN      
        1 maevgrtgis ypgallpqgf waavevwler pqvankrlcg arlearwsaa lpcaeargpg
       61 tsagseqker gpgpgqgspg ggpgprslsg peqgtaccel eeaqgqcqqe eaqreaasvp
      121 lrdsghpgha egregdfpaa dldslwedfs qslargnsel lafltssgag sqpeaqreld
      181 vvlrtvipkt sphcplttpr reivvqdvln gtitflplee ddegnlkvkm snvyqiqlsh
      241 skeewfisvl ifcperwhsd givypkptwl geellaklak wsvenkksdf kstlslisim
      301 kyskayqelk ekykemvkvw pevtdpekfv yedvaiaayl lilweeerae rrltarqsfv
      361 dlgcgngllv hilsseghpg rgidvrrrki wdmygpqtql eedaitpndk tlfpdvdwli
      421 gnhsdeltpw ipviaarssy ncrffvlpcc ffdfigrysr rqskktqyre yldfikevgf
      481 tcgfhvdedc lripstkrvc lvgksrtyps sreasvdekr tqyiksrrgc pvsppgwels
      541 psprwvaags aghcdgqqal darvgcvtra waaehgagpq aegpwlpgfh prekaervrn
      601 caalprdfid qvvlqvanll lggkqlntrs srngslktwn ggeslslaev aneldtetlr
      661 rlkrecgglq tllrnshqvf qvvngrvhir dwreetlwkt kqpeakqrll seacktrlcw
      721 ffmhhpdgca lstdccpfah gpaelrpprt tprkkis
//
LOCUS       NP_001001436             154 aa            linear   PRI 27-APR-2025
DEFINITION  UPF0547 protein C16orf87 isoform 1 [Homo sapiens].
ACCESSION   NP_001001436
VERSION     NP_001001436.1
DBSOURCE    REFSEQ: accession NM_001001436.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Joshi,P., Greco,T.M., Guise,A.J., Luo,Y., Yu,F., Nesvizhskii,A.I.
            and Cristea,I.M.
  TITLE     The functional interactome landscape of the human histone
            deacetylase family
  JOURNAL   Mol Syst Biol 9, 672 (2013)
   PUBMED   23752268
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007225.2, BC056676.1 and BX647945.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.300646.1,
                                           SRR1660805.58567.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMN03267769
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000285697.9/ ENSP00000285697.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q11.2"
     Protein         1..154
                     /product="UPF0547 protein C16orf87 isoform 1"
                     /note="UPF0547 protein C16orf87"
                     /calculated_mol_wt=17668
     Region          14..38
                     /region_name="UPF0547"
                     /note="Uncharacterized protein family UPF0547; pfam10571"
                     /db_xref="CDD:402278"
     Region          43..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PH81.1)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6PH81.1)"
     CDS             1..154
                     /gene="C16orf87"
                     /coded_by="NM_001001436.4:32..496"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10724.1"
                     /db_xref="GeneID:388272"
                     /db_xref="HGNC:HGNC:33754"
ORIGIN      
        1 msatrakkvk matkscpecd qqvpvacksc pcgyifisrk llnakhseks ppstenkhea
       61 krrrtervrr ekinstvnkd lenrkrsrsn shsdhirrgr grpksasakk heeerekqek
      121 eidiyanlsd ekafvfsval aeinrkiinq rlil
//
LOCUS       NP_001026               4967 aa            linear   PRI 27-APR-2025
DEFINITION  ryanodine receptor 2 [Homo sapiens].
ACCESSION   NP_001026
VERSION     NP_001026.2
DBSOURCE    REFSEQ: accession NM_001035.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4967)
  AUTHORS   Fernandez-Morales,J.C., Toth,N., Bayram,P., Rienzo,T. and Morad,M.
  TITLE     Loss-of-function W4645R mutation in the RyR2-caffeine binding site:
            implications for synchrony and arrhythmogenesis
  JOURNAL   Cell Calcium 123, 102925 (2024)
   PUBMED   38908063
  REMARK    GeneRIF: Loss-of-function W4645R mutation in the RyR2-caffeine
            binding site: implications for synchrony and arrhythmogenesis.
            Erratum:[Cell Calcium. 2024 Dec;124:102960. doi:
            10.1016/j.ceca.2024.102960. PMID: 39432975]
REFERENCE   2  (residues 1 to 4967)
  AUTHORS   Hsu,C.H., Hong,S.F., Lo,Y.S., Ho,H.Y., Lin,C.C., Chuang,Y.C.,
            Hsieh,M.J. and Chou,M.C.
  TITLE     The Role of Ryanodine Receptor 2 Polymorphisms in Oral Squamous
            Cell Carcinoma Susceptibility and Clinicopathological Features
  JOURNAL   Int J Mol Sci 25 (19), 10328 (2024)
   PUBMED   39408657
  REMARK    GeneRIF: The Role of Ryanodine Receptor 2 Polymorphisms in Oral
            Squamous Cell Carcinoma Susceptibility and Clinicopathological
            Features.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 4967)
  AUTHORS   Ben-Haim,Y., Bird,M., Johnson,D., Mohiddin,S., Favaloro,L., Dyrberg
            Andersen,J., Sheppard,M.N., Pittman,A., Futema,M. and Behr,E.R.
  TITLE     RYR2 Variant and Sudden Death in Patients With Dilated
            Cardiomyopathy
  JOURNAL   J Am Coll Cardiol 83 (11), 1105-1107 (2024)
   PUBMED   38479959
  REMARK    GeneRIF: RYR2 Variant and Sudden Death in Patients With Dilated
            Cardiomyopathy.
REFERENCE   4  (residues 1 to 4967)
  AUTHORS   Hasegawa,H., Tamura,S., Nakajima,T., Kawabata-Iwakawa,R.,
            Kobari,T., Matsumoto,N., Sano,Y., Nishiyama,M., Kurabayashi,M.,
            Kaneko,Y., Nakatani,Y. and Ishii,H.
  TITLE     Diverse Phenotypic Manifestations in a Family with a Novel RYR2
            E4107A Variant
  JOURNAL   Int Heart J 65 (3), 580-585 (2024)
   PUBMED   38825499
  REMARK    GeneRIF: Diverse Phenotypic Manifestations in a Family with a Novel
            RYR2 E4107A Variant.
REFERENCE   5  (residues 1 to 4967)
  AUTHORS   Meyers,M.B., Pickel,V.M., Sheu,S.S., Sharma,V.K., Scotto,K.W. and
            Fishman,G.I.
  TITLE     Association of sorcin with the cardiac ryanodine receptor
  JOURNAL   J Biol Chem 270 (44), 26411-26418 (1995)
   PUBMED   7592856
REFERENCE   6  (residues 1 to 4967)
  AUTHORS   Otsu,K., Fujii,J., Periasamy,M., Difilippantonio,M., Uppender,M.,
            Ward,D.C. and MacLennan,D.H.
  TITLE     Chromosome mapping of five human cardiac and skeletal muscle
            sarcoplasmic reticulum protein genes
  JOURNAL   Genomics 17 (2), 507-509 (1993)
   PUBMED   8406504
REFERENCE   7  (residues 1 to 4967)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   8  (residues 1 to 4967)
  AUTHORS   Napolitano,C., Mazzanti,A., Bloise,R. and Priori,S.G.
  TITLE     Catecholaminergic Polymorphic Ventricular Tachycardia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301466
REFERENCE   9  (residues 1 to 4967)
  AUTHORS   McNally,E., MacLeod,H. and Dellefave-Castillo,L.
  TITLE     Arrhythmogenic Right Ventricular Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301310
REFERENCE   10 (residues 1 to 4967)
  AUTHORS   Otsu,K., Willard,H.F., Khanna,V.K., Zorzato,F., Green,N.M. and
            MacLennan,D.H.
  TITLE     Molecular cloning of cDNA encoding the Ca2+ release channel
            (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic
            reticulum
  JOURNAL   J Biol Chem 265 (23), 13472-13483 (1990)
   PUBMED   2380170
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391809.21, X98330.1,
            AL442065.11, AL365332.9, AL359924.13 and AI218003.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 18, 2006 this sequence version replaced NP_001026.1.
            
            Summary: This gene encodes a ryanodine receptor found in cardiac
            muscle sarcoplasmic reticulum. The encoded protein is one of the
            components of a calcium channel, composed of a tetramer of the
            ryanodine receptor proteins and a tetramer of FK506 binding protein
            1B proteins, that supplies calcium to cardiac muscle. Mutations in
            this gene are associated with stress-induced polymorphic
            ventricular tachycardia and arrhythmogenic right ventricular
            dysplasia. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X98330.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366574.7/ ENSP00000355533.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4967
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..4967
                     /product="ryanodine receptor 2"
                     /note="cardiac muscle ryanodine receptor-calcium release
                     channel; cardiac-type ryanodine receptor; islet-type
                     ryanodine receptor; kidney-type ryanodine receptor; type 2
                     ryanodine receptor; ryanodine receptor 2 (cardiac)"
                     /calculated_mol_wt=564439
     Region          13..222
                     /region_name="Ins145_P3_rec"
                     /note="Inositol 1,4,5-trisphosphate/ryanodine receptor;
                     pfam08709"
                     /db_xref="CDD:462572"
     Region          230..413
                     /region_name="beta-trefoil_MIR_RyR2"
                     /note="MIR domain, beta-trefoil fold, found in ryanodine
                     receptor 2 (RyR2) and similar proteins; cd23291"
                     /db_xref="CDD:467762"
     Site            order(240..241,348,399)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:467762"
     Region          455..648
                     /region_name="RYDR_ITPR"
                     /note="RIH domain; pfam01365"
                     /db_xref="CDD:460175"
     Region          654..805
                     /region_name="SPRY1_RyR"
                     /note="SPRY domain 1 (SPRY1) of ryanodine receptor (RyR);
                     cd12877"
                     /db_xref="CDD:240457"
     Region          853..2925
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Region          862..951
                     /region_name="RyR"
                     /note="RyR domain; pfam02026"
                     /db_xref="CDD:460419"
     Region          976..1065
                     /region_name="RyR"
                     /note="RyR domain; pfam02026"
                     /db_xref="CDD:460419"
     Region          1086..1218
                     /region_name="SPRY2_RyR"
                     /note="SPRY domain 2 (SPRY2) of ryanodine receptor (RyR);
                     cd12878"
                     /db_xref="CDD:240458"
     Site            1341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q401; propagated from
                     UniProtKB/Swiss-Prot (Q92736.3)"
     Region          1412..1558
                     /region_name="SPRY3_RyR"
                     /note="SPRY domain 3 (SPRY3) of ryanodine receptor (RyR);
                     cd12879"
                     /db_xref="CDD:293937"
     Region          1856..1891
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Site            1869
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B0LPN4; propagated from
                     UniProtKB/Swiss-Prot (Q92736.3)"
     Site            2031
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:E9Q401; propagated from
                     UniProtKB/Swiss-Prot (Q92736.3)"
     Region          2125..2336
                     /region_name="RYDR_ITPR"
                     /note="RIH domain; pfam01365"
                     /db_xref="CDD:460175"
     Region          2354..2379
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Site            2369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q401; propagated from
                     UniProtKB/Swiss-Prot (Q92736.3)"
     Site            2697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B0LPN4; propagated from
                     UniProtKB/Swiss-Prot (Q92736.3)"
     Region          2701..2790
                     /region_name="RyR"
                     /note="RyR domain; pfam02026"
                     /db_xref="CDD:460419"
     Site            2797
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q401; propagated from
                     UniProtKB/Swiss-Prot (Q92736.3)"
     Site            2808
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2D and PKA.
                     /evidence=ECO:0000269|PubMed:10830164,
                     ECO:0000269|PubMed:20056922; propagated from
                     UniProtKB/Swiss-Prot (Q92736.3)"
     Site            2811
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q401; propagated from
                     UniProtKB/Swiss-Prot (Q92736.3)"
     Site            2814
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2D.
                     /evidence=ECO:0000269|PubMed:20056922; propagated from
                     UniProtKB/Swiss-Prot (Q92736.3)"
     Region          2821..2904
                     /region_name="RyR"
                     /note="RyR domain; pfam02026"
                     /db_xref="CDD:460419"
     Site            2947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q401; propagated from
                     UniProtKB/Swiss-Prot (Q92736.3)"
     Region          3581..3610
                     /region_name="Interaction with CALM.
                     /evidence=ECO:0000269|PubMed:18650434"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Region          3831..3948
                     /region_name="RIH_assoc"
                     /note="RyR and IP3R Homology associated; pfam08454"
                     /db_xref="CDD:462482"
     Region          4032..4087
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Region          4210..4229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Site            4282..4302
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Region          4333..4599
                     /region_name="RR_TM4-6"
                     /note="Ryanodine Receptor TM 4-6; pfam06459"
                     /db_xref="CDD:461918"
     Region          4415..4467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Site            4504..4524
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Site            4580..4600
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Region          <4718..4878
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            4730..4750
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Site            4769..4789
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     Site            4850..4870
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92736.3)"
     CDS             1..4967
                     /gene="RYR2"
                     /gene_synonym="ARVC2; ARVD2; RyR; RYR-2; VACRDS; VTSIP"
                     /coded_by="NM_001035.3:339..15242"
                     /db_xref="CCDS:CCDS55691.1"
                     /db_xref="GeneID:6262"
                     /db_xref="HGNC:HGNC:10484"
                     /db_xref="MIM:180902"
ORIGIN      
        1 madggegede iqflrtddev vlqctatihk eqqklclaae gfgnrlcfle stsnsknvpp
       61 dlsictfvle qslsvralqe mlantvekse gqvdvekwkf mmktaqgggh rtllyghail
      121 lrhsysgmyl cclstsrsst dklafdvglq edttgeacww tihpaskqrs egekvrvgdd
      181 lilvsvsser ylhlsygngs lhvdaafqqt lwsvapissg seaaqgylig gdvlrllhgh
      241 mdecltvpsg ehgeeqrrtv hyeggavsvh arslwrletl rvawsgshir wgqpfrlrhv
      301 ttgkylslme dknlllmdke kadvkstaft frsskekldv gvrkevdgmg tseikygdsv
      361 cyiqhvdtgl wltyqsvdvk svrmgsiqrk aimhheghmd dgislsrsqh eesrtarvir
      421 stvflfnrfi rgldalskka kastvdlpie svslslqdli gyfhppdehl ehedkqnrlr
      481 alknrqnlfq eegminlvle cidrlhvyss aahfadvagr eageswksil nslyellaal
      541 irgnrkncaq fsgsldwlis rlerleassg ilevlhcvlv espealniik eghiksiisl
      601 ldkhgrnhkv ldvlcslcvc hgvavrsnqh licdnllpgr dlllqtrlvn hvssmrpnif
      661 lgvsegsaqy kkwyyelmvd htepfvtaea thlrvgwast egyspypggg eewggngvgd
      721 dlfsygfdgl hlwsgciart vsspnqhllr tddvisccld lsapsisfri ngqpvqgmfe
      781 nfnidglffp vvsfsagikv rfllggrhge fkflpppgya pcyeavlpke klkvehsrey
      841 kqertytrdl lgptvsltqa aftpipvdts qivlpphler ireklaenih elwvmnkiel
      901 gwqygpvrdd nkrqhpclve fsklpeqern ynlqmsletl ktllalgchv gisdehaedk
      961 vkkmklpkny qltsgykpap mdlsfikltp sqeamvdkla enahnvward rirqgwtygi
     1021 qqdvknrrnp rlvpytlldd rtkksnkdsl reavrtllgy gynleapdqd haaraevcsg
     1081 tgerfrifra ektyavkagr wyfefetvta gdmrvgwsrp gcqpdqelgs derafafdgf
     1141 kaqrwhqgne hygrswqagd vvgcmvdmne htmmftlnge illddsgsel afkdfdvgdg
     1201 fipvcslgva qvgrmnfgkd vstlkyftic glqegyepfa vntnrditmw lskrlpqflq
     1261 vpsnhehiev tridgtidss pclkvtqksf gsqnsntdim fyrlsmpiec aevfsktvag
     1321 glpgaglfgp kndledydad sdfevlmkta hghlvpdrvd kdkeatkpef nnhkdyaqek
     1381 psrlkqrfll rrtkpdysts hsarltedvl addrddydfl mqtstyyysv rifpgqepan
     1441 vwvgwitsdf hqydtgfdld rvrtvtvtlg dekgkvhesi krsncymvca gesmspgqgr
     1501 nnngleigcv vdaasglltf iangkelsty yqvepstklf pavfaqatsp nvfqfelgri
     1561 knvmplsagl fksehknpvp qcpprlhvqf lshvlwsrmp nqflkvdvsr iserqgwlvq
     1621 cldplqfmsl hipeenrsvd ilelteqeel lkfhyhtlrl ysavcalgnh rvahalcshv
     1681 depqllyaie nkympgllra gyydllidih lssyatarlm mnneyivpmt eetksitlfp
     1741 denkkhglpg iglstslrpr mqfsspsfvs isnecyqysp efpldilksk tiqmlteavk
     1801 egslhardpv ggtteflfvp liklfytlli mgifhnedlk hilqliepsv fkeaatpeee
     1861 sdtlekelsv ddaklqgage eeakggkrpk egllqmklpe pvklqmclll qylcdcqvrh
     1921 rieaivafsd dfvaklqdnq rfrynevmqa lnmsaaltar ktkefrsppq eqinmllnfk
     1981 ddksecpcpe eirdqlldfh edlmthcgie ldedgsldgn sdltirgrll slvekvtylk
     2041 kkqaekpves dskksstlqq lisetmvrwa qesviedpel vramfvllhr qydgigglvr
     2101 alpktyting vsvedtinll aslgqirsll svrmgkeeek lmirglgdim nnkvfyqhpn
     2161 lmralgmhet vmevmvnvlg ggeskeitfp kmvanccrfl cyfcrisrqn qkamfdhlsy
     2221 llenssvgla spamrgstpl dvaaasvmdn nelalalrep dlekvvryla gcglqscqml
     2281 vskgypdigw npvegeryld flrfavfcng esveenanvv vrllirrpec fgpalrgegg
     2341 ngllaameea ikiaedpsrd gpspnsgssk tldteeeedd tihmgnaimt fysalidllg
     2401 rcapemhlih agkgeairir silrsliplg dlvgvisiaf qmptiakdgn vvepdmsagf
     2461 cpdhkaamvl fldrvygiev qdfllhllev gflpdlraaa sldtaalsat dmalalnryl
     2521 ctavlplltr caplfagteh haslidsllh tvyrlskgcs ltkaqrdsie vcllsicgql
     2581 rpsmmqhllr rlvfdvplln ehakmplkll tnhyercwky yclpggwgnf gaaseeelhl
     2641 srklfwgifd alsqkkyeqe lfklalpcls avagalppdy mesnyvsmme kqssmdsegn
     2701 fnpqpvdtsn itipekleyf inkyaehshd kwsmdklang wiygeiysds skvqplmkpy
     2761 kllsekekei yrwpikeslk tmlawgwrie rtregdsmal ynrtrrisqt sqvsvdaahg
     2821 yspraidmsn vtlsrdlham aemmaenyhn iwakkkkmel eskgggnhpl lvpydtltak
     2881 ekakdrekaq dilkflqing yavsrgfkdl eldtpsiekr faysflqqli ryvdeahqyi
     2941 lefdggsrgk gehfpyeqei kffakvvlpl idqyfknhrl yflsaasrpl csgghasnke
     3001 kemvtslfck lgvlvrhris lfgndatsiv nclhilgqtl dartvmktgl esvksalraf
     3061 ldnaaedlek tmenlkqgqf thtrnqpkgv tqiinyttva llpmlsslfe higqhqfged
     3121 liledvqvsc yriltslyal gtsksiyver qrsalgecla afagafpvaf lethldkhni
     3181 ysiyntkssr eraalslptn vedvcpnips leklmeeive laesgirytq mphvmevilp
     3241 mlcsymsrww ehgpennper aemcctalns ehmntllgni lkiiynnlgi degawmkrla
     3301 vfsqpiinkv kpqllkthfl plmeklkkka atvvseedhl kaeargdmse aellildeft
     3361 tlardlyafy pllirfvdyn rakwlkepnp eaeelfrmva evfiywsksh nfkreeqnfv
     3421 vqneinnmsf litdtkskms kaavsdqerk kmkrkgdrys mqtslivaal krllpiglni
     3481 capgdqelia laknrfslkd tedevrdiir snihlqgkle dpairwqmal ykdlpnrtdd
     3541 tsdpektver vldianvlfh leqkskrvgr rhyclvehpq rskkavwhkl lskqrkravv
     3601 acfrmaplyn lprhravnlf lqgyekswie teehyfedkl iedlakpgae ppeedegtkr
     3661 vdplhqlill fsrtaltekc kleedflyma yadimaksch deedddgeee vksfeekeme
     3721 kqkllyqqar lhdrgaaemv lqtisaskge tgpmvaatlk lgiailnggn stvqqkmldy
     3781 lkekkdvgff qslaglmqsc svldlnafer qnkaeglgmv teegsgekvl qddeftcdlf
     3841 rflqllcegh nsdfqnylrt qtgnnttvni iistvdyllr vqesisdfyw yysgkdvide
     3901 qgqrnfskai qvakqvfntl teyiqgpctg nqqslahsrl wdavvgflhv fahmqmklsq
     3961 dssqiellke lmdlqkdmvv mllsmlegnv vngtigkqmv dmlvessnnv emilkffdmf
     4021 lklkdltssd tfkeydpdgk gviskrdfhk ameshkhytq setefllsca etdenetldy
     4081 eefvkrfhep akdigfnvav lltnlsehmp ndtrlqtfle laesvlnyfq pflgrieimg
     4141 sakriervyf eisessrtqw ekpqvkeskr qfifdvvneg gekekmelfv nfcedtifem
     4201 qlaaqisesd lnersankee sekerpeeqg prmaffsilt vrsalfalry niltlmrmls
     4261 lkslkkqmkk vkkmtvkdmv taffssywsi fmtllhfvas vfrgffriic slllggslve
     4321 gakkikvael lanmpdptqd evrgdgeege rkpleaalps edltdlkelt eesdllsdif
     4381 gldlkreggq ykliphnpna glsdlmsnpv pmpevqekfq eqkakeeeke ekeetksepe
     4441 kaegedgeke ekakedkgkq klrqlhthry gepevpesaf wkkiiayqqk llnyfarnfy
     4501 nmrmlalfva fainfillfy kvstssvveg kelptrssse nakvtsldss shriiavhyv
     4561 leessgymep tlrilailht visffciigy yclkvplvif krekevarkl efdglyiteq
     4621 pseddikgqw drlvintqsf pnnywdkfvk rkvmdkygef ygrdrisell gmdkaaldfs
     4681 darekkkpkk dsslsavlns idvkyqmwkl gvvftdnsfl ylawymtmsv lghynnfffa
     4741 ahlldiamgf ktlrtilssv thngkqlvlt vgllavvvyl ytvvafnffr kfynksedgd
     4801 tpdmkcddml tcymfhmyvg vragggigde iedpagdeye iyriifditf fffvivilla
     4861 iiqgliidaf gelrdqqeqv kedmetkcfi cgigndyfdt vphgfethtl qehnlanylf
     4921 flmylinkde tehtgqesyv wkmyqercwe ffpagdcfrk qyedqln
//
LOCUS       NP_002038                739 aa            linear   PRI 27-APR-2025
DEFINITION  glycine--tRNA ligase isoform 1 precursor [Homo sapiens].
ACCESSION   NP_002038
VERSION     NP_002038.2
DBSOURCE    REFSEQ: accession NM_002047.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Liu,W., Wei,C., He,Q., Chen,Z., Zhuang,W., Guo,Y. and Xue,X.
  TITLE     Multiple omics integrative analysis identifies GARS1 as a novel
            prognostic and immunological biomarker: from pan-cancer to bladder
            cancer
  JOURNAL   Sci Rep 14 (1), 19025 (2024)
   PUBMED   39152248
  REMARK    GeneRIF: Multiple omics integrative analysis identifies GARS1 as a
            novel prognostic and immunological biomarker: from pan-cancer to
            bladder cancer.
            Erratum:[Sci Rep. 2024 Oct 24;14(1):25244. doi:
            10.1038/s41598-024-76904-x. PMID: 39448730]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Zheng,Y.X., Chen,X.B., Xu,F., Cui,Y.Z., Wang,Z.Y., Zhou,Y.,
            Fu,N.C., Yang,X.Y., Chen,X.Y., Zheng,M. and Man,X.Y.
  TITLE     Glycyl-tRNA Synthetase Induces Psoriasis-Like Skin by Facilitating
            Skin Inflammation and Vascular Endothelial Cell Angiogenesis
  JOURNAL   J Invest Dermatol 144 (4), 774-785 (2024)
   PUBMED   37827278
  REMARK    GeneRIF: Glycyl-tRNA Synthetase Induces Psoriasis-Like Skin by
            Facilitating Skin Inflammation and Vascular Endothelial Cell
            Angiogenesis.
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Khosh Kish,E., Gamallat,Y., Choudhry,M., Ghosh,S., Seyedi,S. and
            Bismar,T.A.
  TITLE     Glycyl-tRNA Synthetase (GARS) Expression Is Associated with
            Prostate Cancer Progression and Its Inhibition Decreases Migration,
            and Invasion In Vitro
  JOURNAL   Int J Mol Sci 24 (5), 4260 (2023)
   PUBMED   36901698
  REMARK    GeneRIF: Glycyl-tRNA Synthetase (GARS) Expression Is Associated
            with Prostate Cancer Progression and Its Inhibition Decreases
            Migration, and Invasion In Vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 739)
  AUTHORS   Alexandrova,J., Paulus,C., Rudinger-Thirion,J., Jossinet,F. and
            Frugier,M.
  TITLE     Elaborate uORF/IRES features control expression and localization of
            human glycyl-tRNA synthetase
  JOURNAL   RNA Biol 12 (12), 1301-1313 (2015)
   PUBMED   26327585
  REMARK    GeneRIF: one of the mRNAs isoforms tightly controls expression and
            localization of human GARS.
REFERENCE   5  (residues 1 to 739)
  AUTHORS   Hipps,D., Shiba,K., Henderson,B. and Schimmel,P.
  TITLE     Operational RNA code for amino acids: species-specific
            aminoacylation of minihelices switched by a single nucleotide
  JOURNAL   Proc Natl Acad Sci U S A 92 (12), 5550-5552 (1995)
   PUBMED   7539919
REFERENCE   6  (residues 1 to 739)
  AUTHORS   Williams,J., Osvath,S., Khong,T.F., Pearse,M. and Power,D.
  TITLE     Cloning, sequencing and bacterial expression of human glycine tRNA
            synthetase
  JOURNAL   Nucleic Acids Res 23 (8), 1307-1310 (1995)
   PUBMED   7753621
REFERENCE   7  (residues 1 to 739)
  AUTHORS   Ge,Q., Trieu,E.P. and Targoff,I.N.
  TITLE     Primary structure and functional expression of human Glycyl-tRNA
            synthetase, an autoantigen in myositis
  JOURNAL   J Biol Chem 269 (46), 28790-28797 (1994)
   PUBMED   7961834
REFERENCE   8  (residues 1 to 739)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   9  (residues 1 to 739)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   10 (residues 1 to 739)
  AUTHORS   Markovitz,R., Ghosh,R., Lotze,T. and Potocki,L.
  TITLE     GARS1-Associated Axonal Neuropathy
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301420
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005154.1, DA386636.1,
            BC007755.2 and AA464978.1.
            
            On Oct 27, 2006 this sequence version replaced NP_002038.1.
            
            Summary: This gene encodes glycyl-tRNA synthetase, one of the
            aminoacyl-tRNA synthetases that charge tRNAs with their cognate
            amino acids. The encoded enzyme is an (alpha)2 dimer which belongs
            to the class II family of tRNA synthetases. It has been shown to be
            a target of autoantibodies in the human autoimmune diseases,
            polymyositis or dermatomyositis. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.394868.1, AK074524.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389266.8/ ENSP00000373918.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..739
                     /product="glycine--tRNA ligase isoform 1 precursor"
                     /EC_number="6.1.1.14"
                     /note="Charcot-Marie-Tooth neuropathy, neuronal type, D;
                     Charcot-Marie-Tooth neuropathy 2D; AP-4-A synthetase;
                     diadenosine tetraphosphate synthetase; glycine--tRNA
                     ligase; ap4A synthetase"
                     /calculated_mol_wt=79186
     transit_peptide 1..36
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P41250.3)"
                     /calculated_mol_wt=3998
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P41250.3)"
     mat_peptide     37..739
                     /product="Glycine--tRNA ligase. /evidence=ECO:0000255.
                     /id=PRO_0000072998"
                     /note="propagated from UniProtKB/Swiss-Prot (P41250.3)"
                     /calculated_mol_wt=79186
     Region          61..724
                     /region_name="PLN02734"
                     /note="glycyl-tRNA synthetase"
                     /db_xref="CDD:178335"
     Site            204
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41250.3)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9CZD3; propagated from
                     UniProtKB/Swiss-Prot (P41250.3)"
     Site            501
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41250.3)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CZD3; propagated from
                     UniProtKB/Swiss-Prot (P41250.3)"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P41250.3)"
     CDS             1..739
                     /gene="GARS1"
                     /gene_synonym="CMT2D; DSMAV; GARS; GlyRS; HMN5; HMN5A;
                     HMND5; SMAD1; SMAJI"
                     /coded_by="NM_002047.4:45..2264"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS43564.1"
                     /db_xref="GeneID:2617"
                     /db_xref="HGNC:HGNC:4162"
                     /db_xref="MIM:600287"
ORIGIN      
        1 mpsprpvllr garaalllll pprllarpsl llrrslsaas cppislpaaa srssmdgaga
       61 eevlaplrla vrqqgdlvrk lkedkapqvd vdkavaelka rkrvleakel alqpkddivd
      121 rakmedtlkr rffydqafai yggvsglydf gpvgcalknn iiqtwrqhfi qeeqileidc
      181 tmltpepvlk tsghvdkfad fmvkdvknge cfradhllka hlqklmsdkk csvekkseme
      241 svlaqldnyg qqeladlfvn ynvkspitgn dlsppvsfnl mfktfigpgg nmpgylrpet
      301 aqgiflnfkr llefnqgklp faaaqignsf rneisprsgl irvreftmae iehfvdpsek
      361 dhpkfqnvad lhlylysaka qvsgqsarkm rlgdaveqgv inntvlgyfi griylyltkv
      421 gispdklrfr qhmenemahy acdcwdaesk tsygwieivg cadrscydls charatkvpl
      481 vaekplkepk tvnvvqfeps kgaigkaykk daklvmeyla icdecyitem emllnekgef
      541 tietegktfq ltkdminvkr fqktlyveev vpnviepsfg lgrimytvfe htfhvregde
      601 qrtffsfpav vapfkcsvlp lsqnqefmpf vkelsealtr hgvshkvdds sgsigrryar
      661 tdeigvafgv tidfdtvnkt phtatlrdrd smrqiraeis elpsivqdla ngnitwadve
      721 aryplfegqe tgkketiee
//
LOCUS       NP_057479                362 aa            linear   PRI 27-APR-2025
DEFINITION  very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 isoform 1
            [Homo sapiens].
ACCESSION   NP_057479 XP_945631
VERSION     NP_057479.2
DBSOURCE    REFSEQ: accession NM_016395.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Li,Q., Jiang,L., Wang,Y., Liu,X., Wang,B., Shan,Z., Wang,Y.H.,
            Wang,Y., Chen,H. and Li,C.
  TITLE     HACD3 Prevents PB1 from Autophagic Degradation to Facilitate the
            Replication of Influenza A Virus
  JOURNAL   Viruses 16 (5), 702 (2024)
   PUBMED   38793585
  REMARK    GeneRIF: HACD3 Prevents PB1 from Autophagic Degradation to
            Facilitate the Replication of Influenza A Virus.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Huang,Z.J., Li,Y.J., Yang,J., Huang,L., Zhao,Q., Lu,Y.F., Hu,Y.,
            Zhang,W.X., Liang,J.Z., Pan,J., Pan,Y.L., He,Q.Y. and Wang,Y.
  TITLE     PTPLAD1 Regulates PHB-Raf Interaction to Orchestrate
            Epithelial-Mesenchymal and Mitofusion-Fission Transitions in
            Colorectal Cancer
  JOURNAL   Int J Biol Sci 20 (6), 2202-2218 (2024)
   PUBMED   38617530
  REMARK    GeneRIF: PTPLAD1 Regulates PHB-Raf Interaction to Orchestrate
            Epithelial-Mesenchymal and Mitofusion-Fission Transitions in
            Colorectal Cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Matos,A.M., Pinto,F.R., Barros,P., Amaral,M.D., Pepperkok,R. and
            Matos,P.
  TITLE     Inhibition of calpain 1 restores plasma membrane stability to
            pharmacologically rescued Phe508del-CFTR variant
  JOURNAL   J Biol Chem 294 (36), 13396-13410 (2019)
   PUBMED   31324722
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Taguwa,S., Okamoto,T., Abe,T., Mori,Y., Suzuki,T., Moriishi,K. and
            Matsuura,Y.
  TITLE     Human butyrate-induced transcript 1 interacts with hepatitis C
            virus NS5A and regulates viral replication
  JOURNAL   J Virol 82 (6), 2631-2641 (2008)
   PUBMED   18160438
  REMARK    GeneRIF: results suggest that hB-ind1 plays a crucial role in HCV
            RNA replication and the propagation of JFH1 virus through
            interaction with viral and host proteins
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Sabbah,M., Saucier,C. and Redeuilh,G.
  TITLE     Human B-ind1 gene promoter: cloning and regulation by histone
            deacetylase inhibitors
  JOURNAL   Gene 374, 128-133 (2006)
   PUBMED   16516406
  REMARK    GeneRIF: The structure of the B-IND1 gene promoter region was
            determined.
REFERENCE   8  (residues 1 to 362)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   9  (residues 1 to 362)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 362)
  AUTHORS   Courilleau,D., Chastre,E., Sabbah,M., Redeuilh,G., Atfi,A. and
            Mester,J.
  TITLE     B-ind1, a novel mediator of Rac1 signaling cloned from sodium
            butyrate-treated fibroblasts
  JOURNAL   J Biol Chem 275 (23), 17344-17348 (2000)
   PUBMED   10747961
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011846.16 and AC027220.10.
            
            On Nov 1, 2006 this sequence version replaced NP_057479.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.177699.1, AK074898.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261875.10/ ENSP00000261875.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..362
                     /product="very-long-chain (3R)-3-hydroxyacyl-CoA
                     dehydratase 3 isoform 1"
                     /EC_number="4.2.1.134"
                     /note="butyrate-induced transcript 1; protein tyrosine
                     phosphatase-like protein PTPLAD1; butyrate-induced protein
                     1; protein-tyrosine phosphatase-like A domain-containing
                     protein 1; very-long-chain
                     (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase 3;
                     very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3;
                     protein tyrosine phosphatase-like A domain containing 1"
                     /calculated_mol_wt=43029
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9P035.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P035.2)"
     Region          8..115
                     /region_name="p23_hB-ind1_like"
                     /note="p23_like domain found in human (h) butyrate-induced
                     transcript 1 (B-ind1) and similar proteins. hB-ind1
                     participates in signaling by the small GTPase Rac1. It
                     binds to Rac1 and enhances different Rac1 effects
                     including activation of nuclear factor (NF)...; cd06465"
                     /db_xref="CDD:107222"
     Site            order(14,26..27,72,77,91,102,104..105,107..108,110)
                     /site_type="active"
                     /note="Hsp90 binding site [active]"
                     /db_xref="CDD:107222"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P035.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P035.2)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P035.2)"
     Site            186..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P035.2)"
     Region          195..355
                     /region_name="PTPLA"
                     /note="Protein tyrosine phosphatase-like protein, PTPLA;
                     pfam04387"
                     /db_xref="CDD:461286"
     Site            218..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P035.2)"
     Site            242..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P035.2)"
     Site            280..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P035.2)"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P035.2)"
     CDS             1..362
                     /gene="HACD3"
                     /gene_synonym="B-IND1; BIND1; HSPC121; PTPLAD1"
                     /coded_by="NM_016395.4:170..1258"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45282.1"
                     /db_xref="GeneID:51495"
                     /db_xref="HGNC:HGNC:24175"
                     /db_xref="MIM:615940"
ORIGIN      
        1 menqvltphv ywaqrhrely lrvelsdvqn paisitenvl hfkaqghgak gdnvyefhle
       61 fldlvkpepv ykltqrqvni tvqkkvsqww erltkqekrp lflapdfdrw ldesdaemel
      121 rakeeerlnk lrlesegspe tltnlrkgyl fmynlvqflg fswifvnltv rfcilgkesf
      181 ydtfhtvadm myfcqmlavv etinaaigvt tspvlpsliq llgrnfilfi ifgtmeemqn
      241 kavvffvfyl wsaieifrys fymltcidmd wkvltwlryt lwiplyplgc laeavsviqs
      301 ipifnetgrf sftlpypvki kvrfsfflqi ylimiflgly infrhlykqr rrrygqkkkk
      361 ih
//
LOCUS       NP_060813                552 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein kinase RIO2 isoform 1 [Homo sapiens].
ACCESSION   NP_060813
VERSION     NP_060813.2
DBSOURCE    REFSEQ: accession NM_018343.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Matsuzaki,Y., Naito,Y., Miura,N., Mori,T., Watabe,Y., Yoshimoto,S.,
            Shibahara,T., Takano,M. and Honda,K.
  TITLE     RIOK2 Contributes to Cell Growth and Protein Synthesis in Human
            Oral Squamous Cell Carcinoma
  JOURNAL   Curr Oncol 30 (1), 381-391 (2022)
   PUBMED   36661680
  REMARK    GeneRIF: RIOK2 Contributes to Cell Growth and Protein Synthesis in
            Human Oral Squamous Cell Carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Ghosh,S., Raundhal,M., Myers,S.A., Carr,S.A., Chen,X., Petsko,G.A.
            and Glimcher,L.H.
  TITLE     Identification of RIOK2 as a master regulator of human blood cell
            development
  JOURNAL   Nat Immunol 23 (1), 109-121 (2022)
   PUBMED   34937919
  REMARK    GeneRIF: Identification of RIOK2 as a master regulator of human
            blood cell development.
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Cerezo,E.L., Houles,T., Lie,O., Sarthou,M.K., Audoynaud,C.,
            Lavoie,G., Halladjian,M., Cantaloube,S., Froment,C.,
            Burlet-Schiltz,O., Henry,Y., Roux,P.P., Henras,A.K. and Romeo,Y.
  TITLE     RIOK2 phosphorylation by RSK promotes synthesis of the human small
            ribosomal subunit
  JOURNAL   PLoS Genet 17 (6), e1009583 (2021)
   PUBMED   34125833
  REMARK    GeneRIF: RIOK2 phosphorylation by RSK promotes synthesis of the
            human small ribosomal subunit.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Gao,S., Sha,Z., Zhou,J., Wu,Y., Song,Y., Li,C., Liu,X., Zhang,T.
            and Yu,R.
  TITLE     BYSL contributes to tumor growth by cooperating with the mTORC2
            complex in gliomas
  JOURNAL   Cancer Biol Med 18 (1), 88-104 (2021)
   PUBMED   33628587
  REMARK    GeneRIF: BYSL contributes to tumor growth by cooperating with the
            mTORC2 complex in gliomas.
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Song,Y., Li,C., Jin,L., Xing,J., Sha,Z., Zhang,T., Ji,D., Yu,R. and
            Gao,S.
  TITLE     RIOK2 is negatively regulated by miR-4744 and promotes glioma cell
            migration/invasion through epithelial-mesenchymal transition
  JOURNAL   J Cell Mol Med 24 (8), 4494-4509 (2020)
   PUBMED   32125767
  REMARK    GeneRIF: RIOK2 is negatively regulated by miR-4744 and promotes
            glioma cell migration/invasion through epithelial-mesenchymal
            transition.
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Read,R.D., Fenton,T.R., Gomez,G.G., Wykosky,J., Vandenberg,S.R.,
            Babic,I., Iwanami,A., Yang,H., Cavenee,W.K., Mischel,P.S.,
            Furnari,F.B. and Thomas,J.B.
  TITLE     A kinome-wide RNAi screen in Drosophila Glia reveals that the RIO
            kinases mediate cell proliferation and survival through TORC2-Akt
            signaling in glioblastoma
  JOURNAL   PLoS Genet 9 (2), e1003253 (2013)
   PUBMED   23459592
  REMARK    GeneRIF: reduced expression of RIOK1 or RIOK2 disrupted Akt
            signaling and caused cell cycle exit, apoptosis, and
            chemosensitivity in glioblastoma cells
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Liu,T., Deng,M., Li,J., Tong,X., Wei,Q. and Ye,X.
  TITLE     Phosphorylation of right open reading frame 2 (Rio2) protein kinase
            by polo-like kinase 1 regulates mitotic progression
  JOURNAL   J Biol Chem 286 (42), 36352-36360 (2011)
   PUBMED   21880710
  REMARK    GeneRIF: Plk1-mediated phosphorylation of Rio2 regulates
            metaphase-anaphase transition during mitotic progression.
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Johnson,M.P., Roten,L.T., Dyer,T.D., East,C.E., Forsmo,S.,
            Blangero,J., Brennecke,S.P., Austgulen,R. and Moses,E.K.
  TITLE     The ERAP2 gene is associated with preeclampsia in Australian and
            Norwegian populations
  JOURNAL   Hum Genet 126 (5), 655-666 (2009)
   PUBMED   19578876
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Zemp,I., Wild,T., O'Donohue,M.F., Wandrey,F., Widmann,B.,
            Gleizes,P.E. and Kutay,U.
  TITLE     Distinct cytoplasmic maturation steps of 40S ribosomal subunit
            precursors require hRio2
  JOURNAL   J Cell Biol 185 (7), 1167-1180 (2009)
   PUBMED   19564402
  REMARK    GeneRIF: Results show that the protein kinase human Rio2 (hRio2) is
            part of a late 40S preribosomal particle in human cells.
REFERENCE   10 (residues 1 to 552)
  AUTHORS   LaRonde-LeBlanc,N. and Wlodawer,A.
  TITLE     A family portrait of the RIO kinases
  JOURNAL   J Biol Chem 280 (45), 37297-37300 (2005)
   PUBMED   16183636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB240299.1, AK002021.1, AC008865.3 and CA415109.1.
            
            On May 1, 2009 this sequence version replaced NP_060813.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.70800.1,
                                           SRR1803611.277357.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283109.8/ ENSP00000283109.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q15"
     Protein         1..552
                     /product="serine/threonine-protein kinase RIO2 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase RIO2"
                     /calculated_mol_wt=63152
     Region          9..91
                     /region_name="Rio2_N"
                     /note="Rio2, N-terminal; pfam09202"
                     /db_xref="CDD:462715"
     Region          94..276
                     /region_name="RIO2_C"
                     /note="C-terminal catalytic domain of the atypical protein
                     serine kinase, RIO2 kinase; cd05144"
                     /db_xref="CDD:270695"
     Site            order(101,106..107,109,121,123,176,188..191,195,232..233,
                     245..246)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270695"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21880710,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21880710,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Region          399..408
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000269|PubMed:19564402"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q9BVS4.2)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21880710; propagated from
                     UniProtKB/Swiss-Prot (Q9BVS4.2)"
     CDS             1..552
                     /gene="RIOK2"
                     /gene_synonym="RIO2"
                     /coded_by="NM_018343.3:57..1715"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4089.1"
                     /db_xref="GeneID:55781"
                     /db_xref="HGNC:HGNC:18999"
                     /db_xref="MIM:617754"
ORIGIN      
        1 mgkvnvaklr ymsrddfrvl tavemgmknh eivpgslias iaslkhggcn kvlrelvkhk
       61 liawertktv qgyrltnagy dylalktlss rqvvesvgnq mgvgkesdiy ivaneegqqf
      121 alklhrlgrt sfrnlknkrd yhkhrhnvsw lylsrlsamk efaymkalye rkfpvpkpid
      181 ynrhavvmel ingyplcqih hvedpasvyd eamelivkla nhglihgdfn efnlildesd
      241 hitmidfpqm vstshpnaew yfdrdvkcik dffmkrfsye selfptfkdi rredtldvev
      301 sasgytkemq addellhplg pddknietke gsefsfsdge vaekaevygs eneserncle
      361 esegcycrss gdpeqikeds lseesadars femtefnqal eeikgqvven nsvtefseek
      421 nrtenynrqd gqrvqggvpa gsdeyedecp hlialsslnr efrpfrdeen vgamnqyrtr
      481 tlsitssgsa vscstippel vkqkvkrqlt kqqksavrrr lqkgeanift kqrrenmqni
      541 kssleaasfw ge
//
LOCUS       NP_066284                278 aa            linear   PRI 27-APR-2025
DEFINITION  dehydrogenase/reductase SDR family member 4 isoform 1 [Homo
            sapiens].
ACCESSION   NP_066284
VERSION     NP_066284.2
DBSOURCE    REFSEQ: accession NM_021004.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Zhou,Y., Li,K., Zou,X., Hua,Z., Wang,H., Bian,W., Wang,H., Chen,F.
            and Dai,T.
  TITLE     LncRNA DHRS4-AS1 ameliorates hepatocellular carcinoma by
            suppressing proliferation and promoting apoptosis via
            miR-522-3p/SOCS5 axis
  JOURNAL   Bioengineered 12 (2), 10862-10877 (2021)
   PUBMED   34666613
  REMARK    GeneRIF: LncRNA DHRS4-AS1 ameliorates hepatocellular carcinoma by
            suppressing proliferation and promoting apoptosis via
            miR-522-3p/SOCS5 axis.
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Su,Z., Liu,G., Song,X., Liang,B., Chang,X. and Huang,D.
  TITLE     CpG island evolution in the mammalian DHRS4 gene cluster and its
            role in the regulation of gene transcription
  JOURNAL   Genet Mol Res 15 (2) (2016)
   PUBMED   27323117
  REMARK    GeneRIF: An analysis of the relationship between the promoter
            characteristics and RNA expression of the DHRS4 gene cluster
            indicated that the development of CpG islands, in addition to the
            promoter sequence, during mammalian evolution could modulate the
            dose compensatory regulation of the copy number-varied DHRS4 gene
            cluster
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Yang,Y., Su,Z., Song,X., Liang,B., Zeng,F., Chang,X. and Huang,D.
  TITLE     Enhancer RNA-driven looping enhances the transcription of the long
            noncoding RNA DHRS4-AS1, a controller of the DHRS4 gene cluster
  JOURNAL   Sci Rep 6, 20961 (2016)
   PUBMED   26864944
  REMARK    GeneRIF: AS1eRNA-driven DNA looping and activating histone
            modifications promote the expression of DHRS4-AS1 to economically
            control the DHRS4 gene cluster.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Yan,Y., Song,X., Liu,G., Su,Z., Du,Y., Sui,X., Chang,X. and
            Huang,D.
  TITLE     Human NRDRB1, an alternatively spliced isoform of NADP(H)-dependent
            retinol dehydrogenase/reductase enhanced enzymatic activity of
            benzil
  JOURNAL   Cell Physiol Biochem 30 (6), 1371-1382 (2012)
   PUBMED   23128527
  REMARK    GeneRIF: NRDRB1, an alternatively spliced isoform of NRDR in vivo
            functions better than NRDR as a dicarbonyl reductase for
            xenobiotics containing reactive carbonyls.
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Matsunaga,T., Endo,S., Maeda,S., Ishikura,S., Tajima,K., Tanaka,N.,
            Nakamura,K.T., Imamura,Y. and Hara,A.
  TITLE     Characterization of human DHRS4: an inducible short-chain
            dehydrogenase/reductase enzyme with 3beta-hydroxysteroid
            dehydrogenase activity
  JOURNAL   Arch Biochem Biophys 477 (2), 339-347 (2008)
   PUBMED   18571493
  REMARK    GeneRIF: Results suggest a novel mechanism of cold inactivation and
            role of the inducible human DHRS4 in 3beta-hydroxysteroid synthesis
            and xenobiotic carbonyl metabolism
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Song,X.H., Liang,B., Liu,G.F., Li,R., Xie,J.P., Du,K. and
            Huang,D.Y.
  TITLE     Expression of a novel alternatively spliced variant of
            NADP(H)-dependent retinol dehydrogenase/reductase with deletion of
            exon 3 in cervical squamous carcinoma
  JOURNAL   Int J Cancer 120 (8), 1618-1626 (2007)
   PUBMED   17230527
  REMARK    GeneRIF: Alternatively spliced variant of NADP(H)-dependent retinol
            dehydrogenase/reductase with deletion of exon 3 is associated with
            cervical squamous carcinoma
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Du,J., Huang,D.Y., Liu,G.F., Wang,G.L., Xu,X.L., Wang,B. and Zhu,L.
  TITLE     CDNA cloning of a short isoform of human liver NADP (H) -dependent
            retinol dehydrogenase/reductase and analysis of its characteristics
  JOURNAL   Yi Chuan Xue Bao 31 (7), 661-667 (2004)
   PUBMED   15473316
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Fransen,M., Van Veldhoven,P.P. and Subramani,S.
  TITLE     Identification of peroxisomal proteins by using M13 phage protein
            VI phage display: molecular evidence that mammalian peroxisomes
            contain a 2,4-dienoyl-CoA reductase
  JOURNAL   Biochem J 340 (Pt 2) (Pt 2), 561-568 (1999)
   PUBMED   10333503
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU529016.1, BC003019.1, BQ030242.1 and CA438339.1.
            
            On Jul 9, 2003 this sequence version replaced NP_066284.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF044127.1, AY358638.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313250.10/ ENSP00000326219.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..278
                     /product="dehydrogenase/reductase SDR family member 4
                     isoform 1"
                     /EC_number="1.1.1.184"
                     /note="peroxisomal short-chain alcohol dehydrogenase;
                     short chain dehydrogenase/reductase family 25C, member 1;
                     short chain dehydrogenase/reductase family 25C member 2;
                     NADPH-dependent retinol dehydrogenase/reductase;
                     NADPH-dependent carbonyl reductase;
                     dehydrogenase/reductase (SDR family) member 4 like 2A;
                     short-chain dehydrogenase/reductase family member 4;
                     NADPH-dependent carbonyl reductase/NADP-retinol
                     dehydrogenase"
                     /calculated_mol_wt=29406
     Region          23..278
                     /region_name="CR_SDR_c"
                     /note="Porcine peroxisomal carbonyl reductase like,
                     classical (c) SDR; cd08936"
                     /db_xref="CDD:187641"
     Site            order(39..44,63..65,68,88..90,116..118,167..169,182,186,
                     212..215,217..220)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187641"
     Site            order(51,124..128,131,134..135,139,143,146..147,149..150,
                     172..173,175,180,183..184,187..188,190..192,194..196,199,
                     204,214,239..243,247,250..251,254,259,261..264,266..273,
                     275..278)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187641"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB2; propagated from
                     UniProtKB/Swiss-Prot (Q9BTZ2.3)"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LB2; propagated from
                     UniProtKB/Swiss-Prot (Q9BTZ2.3)"
     Site            order(124..128,131,134..135,139,142..143,146..147,
                     149..150,153,175,177..178,180,183..184,187..188,191..192,
                     194..196,198..199)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187641"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BTZ2.3)"
     Site            order(141,169,182,186)
                     /site_type="active"
                     /db_xref="CDD:187641"
     Site            176
                     /site_type="other"
                     /note="Responsible for the stereoselective reduction of
                     3-ketosteroids into 3beta-hydroxysteroids and benzil into
                     R-benzoin. /evidence=ECO:0000269|PubMed:19056333;
                     propagated from UniProtKB/Swiss-Prot (Q9BTZ2.3)"
     Site            179
                     /site_type="other"
                     /note="Responsible for the stereoselective reduction of
                     3-ketosteroids into 3beta-hydroxysteroids and benzil into
                     R-benzoin. /evidence=ECO:0000269|PubMed:19056333;
                     propagated from UniProtKB/Swiss-Prot (Q9BTZ2.3)"
     Site            216
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB2; propagated from
                     UniProtKB/Swiss-Prot (Q9BTZ2.3)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99LB2; propagated from
                     UniProtKB/Swiss-Prot (Q9BTZ2.3)"
     Region          276..278
                     /region_name="Peroxisomal targeting signal.
                     /evidence=ECO:0000250|UniProtKB:Q8WNV7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTZ2.3)"
     CDS             1..278
                     /gene="DHRS4"
                     /gene_synonym="CR; NRDR; PHCR; PSCD; SCAD-SRL; SDR-SRL;
                     SDR25C1; SDR25C2"
                     /coded_by="NM_021004.4:20..856"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9605.1"
                     /db_xref="GeneID:10901"
                     /db_xref="HGNC:HGNC:16985"
                     /db_xref="MIM:611596"
ORIGIN      
        1 mhkagllglc arawnsvrma ssgmtrrdpl ankvalvtas tdgigfaiar rlaqdgahvv
       61 vssrkqqnvd qavatlqgeg lsvtgtvchv gkaedrerlv atavklhggi dilvsnaavn
      121 pffgsimdvt eevwdktldi nvkapalmtk avvpemekrg ggsvvivssi aafspspgfs
      181 pynvsktall gltktlaiel aprnirvncl apgliktsfs rmlwmdkeke esmketlrir
      241 rlgepedcag ivsflcseda syitgetvvv gggtpsrl
//
LOCUS       NP_001355997             921 aa            linear   ROD 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 4 [Mus
            musculus].
ACCESSION   NP_001355997
VERSION     NP_001355997.1
DBSOURCE    REFSEQ: accession NM_001369068.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Thoren,L.A., Norgaard,G.A., Weischenfeldt,J., Waage,J.,
            Jakobsen,J.S., Damgaard,I., Bergstrom,F.C., Blom,A.M., Borup,R.,
            Bisgaard,H.C. and Porse,B.T.
  TITLE     UPF2 is a critical regulator of liver development, function and
            regeneration
  JOURNAL   PLoS One 5 (7), e11650 (2010)
   PUBMED   20657840
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Combes,A.N., Lesieur,E., Harley,V.R., Sinclair,A.H., Little,M.H.,
            Wilhelm,D. and Koopman,P.
  TITLE     Three-dimensional visualization of testis cord morphogenesis, a
            novel tubulogenic mechanism in development
  JOURNAL   Dev Dyn 238 (5), 1033-1041 (2009)
   PUBMED   19334288
REFERENCE   3  (residues 1 to 921)
  AUTHORS   Hoffman,B.G., Zavaglia,B., Witzsche,J., Ruiz de Algara,T.,
            Beach,M., Hoodless,P.A., Jones,S.J., Marra,M.A. and Helgason,C.D.
  TITLE     Identification of transcripts with enriched expression in the
            developing and adult pancreas
  JOURNAL   Genome Biol 9 (6), R99 (2008)
   PUBMED   18554416
REFERENCE   4  (residues 1 to 921)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   5  (residues 1 to 921)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 921)
  AUTHORS   Cobellis,G., Nicolaus,G., Iovino,M., Romito,A., Marra,E.,
            Barbarisi,M., Sardiello,M., Di Giorgio,F.P., Iovino,N., Zollo,M.,
            Ballabio,A. and Cortese,R.
  TITLE     Tagging genes with cassette-exchange sites
  JOURNAL   Nucleic Acids Res 33 (4), e44 (2005)
   PUBMED   15741177
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 921)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 921)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 921)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
REFERENCE   10 (residues 1 to 921)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL627185.10 and AL627078.10.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 67.34 cM"
     Protein         1..921
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 4"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein;
                     plenty-of-prolines-101"
                     /calculated_mol_wt=103959
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          622..>819
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..921
                     /gene="Srrm1"
                     /gene_synonym="POP101; Srm160"
                     /coded_by="NM_001369068.1:30..2795"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:51796"
                     /db_xref="MGI:MGI:1858303"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkeks pelpepsvrm kdssvqeats
      241 tsdilkapkp epvpepkeps peknskkeke ktrprsrsrs ksrsrtrsrs pshtrprrrh
      301 rsrsrsyspr rrpsprrrps prrrtpprrm pppprhrrsr spgrrrrrss aslsgsssss
      361 sssrsrsppk kppkrtsspp rktrrlspsa spprrrhrps spatpppktr hsptpqqsnr
      421 trksrvsvsp grtsgkvtkh kgtekresps papkprkvel sesedkgskm aaadsvqqrr
      481 qyrrqnqqss sdsgssstse derpkrshvk ngevgrrrrh spsrsaspsp rkrqketspr
      541 mqmgkrwqsp vtksrrrrsp sppparrrrs pspapppppp pppprrrrsp tppprrrtps
      601 ppprrrspsp rrysppiqrr yspspppkrr taspppppkr raspspppkr rvshspppkq
      661 rsptvtkrrs pslsskhrkg sspgrstrea rspqpnkrhs psprprapqt sspppvrrga
      721 saspqgrqsp spstrpirrv srtpepkkik kaaspspqsv rrvsssrsvs gspepaakkp
      781 pappspvqsq spstnwspav pakkaksptp slsparnsdq egggkkkkkk kdkkhkkdkk
      841 hkkhkkhkke kavtiatpat aapaavsaat ttsaqeepaa apeprketes eaeddnlddl
      901 erhlrekalr smrkaqvspq s
//
LOCUS       NP_001347741             860 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor E2F8 [Mus musculus].
ACCESSION   NP_001347741 XP_006540616
VERSION     NP_001347741.1
DBSOURCE    REFSEQ: accession NM_001360812.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Dou,D., Bi,M., Li,X., Zhang,N., Xu,M., Guo,A., Li,F. and Zhu,W.
  TITLE     ADP Ribosylation Factor 6 Relieves Airway Inflammation and
            Remodeling by Inhibiting Ovalbumin Induced-Epithelial Mesenchymal
            Transition in Experimental Asthma, Possibly by Regulating of E2F
            Transcription Factor 8
  JOURNAL   Immunol Invest 52 (6), 717-734 (2023)
   PUBMED   37326141
  REMARK    GeneRIF: ADP Ribosylation Factor 6 Relieves Airway Inflammation and
            Remodeling by Inhibiting Ovalbumin Induced-Epithelial Mesenchymal
            Transition in Experimental Asthma, Possibly by Regulating of E2F
            Transcription Factor 8.
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Moreno,E., Matondo,A.B., Bongiovanni,L., van de Lest,C.H.A.,
            Molenaar,M.R., Toussaint,M.J.M., van Essen,S.C., Houweling,M.,
            Helms,J.B., Westendorp,B. and de Bruin,A.
  TITLE     Inhibition of polyploidization in Pten-deficient livers reduces
            steatosis
  JOURNAL   Liver Int 42 (11), 2442-2452 (2022)
   PUBMED   35924448
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Park,S.A., Lim,Y.J., Ku,W.L., Zhang,D., Cui,K., Tang,L.Y., Chia,C.,
            Zanvit,P., Chen,Z., Jin,W., Wang,D., Xu,J., Liu,O., Wang,F.,
            Cain,A., Guo,N., Nakatsukasa,H., Wu,C., Zhang,Y.E., Zhao,K. and
            Chen,W.
  TITLE     Opposing functions of circadian protein DBP and atypical E2F family
            E2F8 in anti-tumor Th9 cell differentiation
  JOURNAL   Nat Commun 13 (1), 6069 (2022)
   PUBMED   36241625
  REMARK    GeneRIF: Opposing functions of circadian protein DBP and atypical
            E2F family E2F8 in anti-tumor Th9 cell differentiation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Wenzel,P.L., Wu,L., de Bruin,A., Chong,J.L., Chen,W.Y., Dureska,G.,
            Sites,E., Pan,T., Sharma,A., Huang,K., Ridgway,R., Mosaliganti,K.,
            Sharp,R., Machiraju,R., Saltz,J., Yamamoto,H., Cross,J.C.,
            Robinson,M.L. and Leone,G.
  TITLE     Rb is critical in a mammalian tissue stem cell population
  JOURNAL   Genes Dev 21 (1), 85-97 (2007)
   PUBMED   17210791
REFERENCE   6  (residues 1 to 860)
  AUTHORS   Stefan,M., Claiborn,K.C., Stasiek,E., Chai,J.H., Ohta,T.,
            Longnecker,R., Greally,J.M. and Nicholls,R.D.
  TITLE     Genetic mapping of putative Chrna7 and Luzp2 neuronal
            transcriptional enhancers due to impact of a transgene-insertion
            and 6.8 Mb deletion in a mouse model of Prader-Willi and Angelman
            syndromes
  JOURNAL   BMC Genomics 6, 157 (2005)
   PUBMED   16280085
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 860)
  AUTHORS   Christensen,J., Cloos,P., Toftegaard,U., Klinkenberg,D.,
            Bracken,A.P., Trinh,E., Heeran,M., Di Stefano,L. and Helin,K.
  TITLE     Characterization of E2F8, a novel E2F-like cell-cycle regulated
            repressor of E2F-activated transcription
  JOURNAL   Nucleic Acids Res 33 (17), 5458-5470 (2005)
   PUBMED   16179649
  REMARK    GeneRIF: E2F8 may have an important role in repressing the
            expression of E2F-target genes in the S-phase of the cell cycle.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 860)
  AUTHORS   Logan,N., Graham,A., Zhao,X., Fisher,R., Maiti,B., Leone,G. and La
            Thangue,N.B.
  TITLE     E2F-8: an E2F family member with a similar organization of
            DNA-binding domains to E2F-7
  JOURNAL   Oncogene 24 (31), 5000-5004 (2005)
   PUBMED   15897886
REFERENCE   9  (residues 1 to 860)
  AUTHORS   Maiti,B., Li,J., de Bruin,A., Gordon,F., Timmers,C., Opavsky,R.,
            Patil,K., Tuttle,J., Cleghorn,W. and Leone,G.
  TITLE     Cloning and characterization of mouse E2F8, a novel mammalian E2F
            family member capable of blocking cellular proliferation
  JOURNAL   J Biol Chem 280 (18), 18211-18220 (2005)
   PUBMED   15722552
  REMARK    GeneRIF: Overexpression of E2F8 significantly slows down the
            proliferation of primary mouse embryonic fibroblasts.
REFERENCE   10 (residues 1 to 860)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC124977.8, BC086675.1 and BX528987.1.
            
            On Feb 15, 2018 this sequence version replaced XP_006540616.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY957576.1, SRR11927935.3216089.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134, SAMN01164135
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 31.11 cM"
     Protein         1..860
                     /product="transcription factor E2F8"
                     /note="E2f family member 8"
                     /calculated_mol_wt=93145
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58FA4.1)"
     Region          38..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58FA4.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q58FA4.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A0AVK6; propagated from
                     UniProtKB/Swiss-Prot (Q58FA4.1)"
     Region          114..182
                     /region_name="E2F_TDP"
                     /note="E2F/DP family winged-helix DNA-binding domain;
                     pfam02319"
                     /db_xref="CDD:460530"
     Region          262..347
                     /region_name="E2F_TDP"
                     /note="E2F/DP family winged-helix DNA-binding domain;
                     pfam02319"
                     /db_xref="CDD:460530"
     Region          407..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58FA4.1)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A0AVK6; propagated from
                     UniProtKB/Swiss-Prot (Q58FA4.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A0AVK6; propagated from
                     UniProtKB/Swiss-Prot (Q58FA4.1)"
     Region          <497..830
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          532..616
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58FA4.1)"
     Region          745..803
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58FA4.1)"
     CDS             1..860
                     /gene="E2f8"
                     /gene_synonym="4432406C08Rik"
                     /coded_by="NM_001360812.1:299..2881"
                     /db_xref="CCDS:CCDS39967.1"
                     /db_xref="GeneID:108961"
                     /db_xref="MGI:MGI:1922038"
ORIGIN      
        1 menqkenlfs ephkrglmks plhpsskanm vlaeiqpdlg plttptkpke vsqgepwtpt
       61 anlkmlisav speirsrdqk rglsdnrsal peardclheh lsgdefeksq psrkekslgl
      121 lchkflaryp kypnpavnnd icldevaeel nverrriydi vnvleslhmv srlaknrytw
      181 hgrhnltktl gtlksvgeen kyaeqimmik rkeyeqefdf ikscgiedhv ikshtgqngh
      241 sdmcfvelpg vefraasvns rkdkslrvms qkfvmlflvs tpqivsleia akiligedhv
      301 edldkskykt kirrlydian vlssldlikk vhvteergrk pafkwtgpei spnnsgsspi
      361 mplpasleae qsakencakn lfstrgkpsf trhpsliklv ksiendrrki ssapsspvks
      421 nkaessqnsp pvpnkmaqla aickmqleeq sseprkkvkv nlarsghykp lapldptvnt
      481 elelltpsli qplgvvplip splssavpvi lpqapsgpsy aiylqpaqaq mltpppglsp
      541 tvcptqpsna tgskdptdap aektatdaat tgslqpaper hgakhrsket tgdrgtkrmi
      601 taedsgpssv kkpkedlkal envptptplf psgylipltq csslgpdsvl sntensgtps
      661 pnhriygspi agvipvasse ltavnfppfh vtplklmvsp tsmaavpvgn spalnsghpa
      721 paqnpssaiv nftlqhlgli spgvqmsasp gpgagtvpvs prveadnlss rqrratnhds
      781 pvlgqsqlng qpvagtgaqq pvpvtpkgsq lvaenffrtp ggptkptssp ytdfdgankt
      841 sfgtlfvpqr klevstedih
//
LOCUS       NP_001351612             248 aa            linear   PRI 27-APR-2025
DEFINITION  tropomyosin alpha-3 chain isoform Tpm3.5cy [Homo sapiens].
ACCESSION   NP_001351612
VERSION     NP_001351612.1
DBSOURCE    REFSEQ: accession NM_001364683.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Takeuchi,K., Soda,M., Togashi,Y., Suzuki,R., Sakata,S., Hatano,S.,
            Asaka,R., Hamanaka,W., Ninomiya,H., Uehara,H., Lim Choi,Y.,
            Satoh,Y., Okumura,S., Nakagawa,K., Mano,H. and Ishikawa,Y.
  TITLE     RET, ROS1 and ALK fusions in lung cancer
  JOURNAL   Nat Med 18 (3), 378-381 (2012)
   PUBMED   22327623
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Gunning,P.W., Schevzov,G., Kee,A.J. and Hardeman,E.C.
  TITLE     Tropomyosin isoforms: divining rods for actin cytoskeleton function
  JOURNAL   Trends Cell Biol 15 (6), 333-341 (2005)
   PUBMED   15953552
  REMARK    Review article
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Lin,J.L., Geng,X., Bhattacharya,S.D., Yu,J.R., Reiter,R.S.,
            Sastri,B., Glazier,K.D., Mirza,Z.K., Wang,K.K., Amenta,P.S.,
            Das,K.M. and Lin,J.J.
  TITLE     Isolation and sequencing of a novel tropomyosin isoform
            preferentially associated with colon cancer
  JOURNAL   Gastroenterology 123 (1), 152-162 (2002)
   PUBMED   12105844
  REMARK    GeneRIF: cloned and sequenced a novel nonmuscle tropomyosin (hTM)
            isoform, TC22, which is strongly associated with colonic neoplasia
            and carcinoma
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Lamant,L., Dastugue,N., Pulford,K., Delsol,G. and Mariame,B.
  TITLE     A new fusion gene TPM3-ALK in anaplastic large cell lymphoma
            created by a (1;2)(q25;p23) translocation
  JOURNAL   Blood 93 (9), 3088-3095 (1999)
   PUBMED   10216106
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Laing,N.G., Wilton,S.D., Akkari,P.A., Dorosz,S., Boundy,K.,
            Kneebone,C., Blumbergs,P., White,S., Watkins,H., Love,D.R. et al.
  TITLE     A mutation in the alpha tropomyosin gene TPM3 associated with
            autosomal dominant nemaline myopathy
  JOURNAL   Nat Genet 9 (1), 75-79 (1995)
   PUBMED   7704029
  REMARK    Erratum:[Nat Genet. 1995 Jun;10(2):249. doi: 10.1038/ng0695-249.
            PMID: 7663526]
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Wilton,S.D., Eyre,H., Akkari,P.A., Watkins,H.C., MacRae,C.,
            Laing,N.G. and Callen,D.C.
  TITLE     Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by
            fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 122-124 (1995)
   PUBMED   7956350
REFERENCE   8  (residues 1 to 248)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
REFERENCE   9  (residues 1 to 248)
  AUTHORS   DeChene,E.T., Kang,P.B. and Beggs,A.H.
  TITLE     Congenital Fiber-Type Disproportion - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301436
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Clayton,L., Reinach,F.C., Chumbley,G.M. and MacLeod,A.R.
  TITLE     Organization of the hTMnm gene. Implications for the evolution of
            muscle and non-muscle tropomyosins
  JOURNAL   J Mol Biol 201 (3), 507-515 (1988)
   PUBMED   3418707
REFERENCE   11 (residues 1 to 248)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C. and Talbot,K.
  TITLE     The mRNA and RNA-copy pseudogenes encoding TM30nm, a human
            cytoskeletal tropomyosin
  JOURNAL   Nucleic Acids Res 14 (21), 8413-8426 (1986)
   PUBMED   3024106
REFERENCE   12 (residues 1 to 248)
  AUTHORS   Martin-Zanca,D., Hughes,S.H. and Barbacid,M.
  TITLE     A human oncogene formed by the fusion of truncated tropomyosin and
            protein tyrosine kinase sequences
  JOURNAL   Nature 319 (6056), 743-748 (1986)
   PUBMED   2869410
REFERENCE   13 (residues 1 to 248)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590431.11.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins. Tropomyosins are dimers of coiled-coil
            proteins that provide stability to actin filaments and regulate
            access of other actin-binding proteins. Mutations in this gene
            result in autosomal dominant nemaline myopathy and other muscle
            disorders. This locus is involved in translocations with other
            loci, including anaplastic lymphoma receptor tyrosine kinase (ALK)
            and neurotrophic tyrosine kinase receptor type 1 (NTRK1), which
            result in the formation of fusion proteins that act as oncogenes.
            There are numerous pseudogenes for this gene on different
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.242840.1,
                                           SRR1163658.418535.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..248
                     /product="tropomyosin alpha-3 chain isoform Tpm3.5cy"
                     /note="heat-stable cytoskeletal protein 30 kDa;
                     cytoskeletal tropomyosin TM30; tropomyosin alpha-3 chain;
                     tropomyosin gamma; tropomyosin-5; alpha-tropomyosin, slow
                     skeletal; epididymis secretory sperm binding protein Li
                     82p; epididymis luminal protein 189; tropomyosin 3 nu"
                     /calculated_mol_wt=28791
     Region          12..246
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..248
                     /gene="TPM3"
                     /gene_synonym="CAPM1; CFTD; CMYO4A; CMYO4B; CMYP4A;
                     CMYP4B; HEL-189; HEL-S-82p; hscp30; NEM1; OK/SW-cl.5;
                     TM-5; TM3; TM30; TM30nm; TM5; TPM3nu; TPMsk3; TRK"
                     /coded_by="NM_001364683.1:100..846"
                     /note="isoform Tpm3.5cy is encoded by transcript variant
                     17"
                     /db_xref="GeneID:7170"
                     /db_xref="HGNC:HGNC:12012"
                     /db_xref="MIM:191030"
ORIGIN      
        1 magittieav krkiqvlqqq addaeeraer lqrevegerr areqaeaeva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkvienralk deekmelqei qlkeakhiae
      121 eadrkyeeva rklviiegdl erteeraela esrcremdeq irlmdqnlkc lsaaeekysq
      181 kedkyeeeik iltdklkeae traefaersv aklektiddl edelyaqklk ykaiseeldh
      241 alndmtsi
//
LOCUS       NP_001357322             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357322
VERSION     NP_001357322.1
DBSOURCE    REFSEQ: accession NM_001370393.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1407845.1,
                                           SRR7346977.1456637.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370393.1:1500..3149"
                     /note="isoform 1 is encoded by transcript variant 22"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_001356494             534 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 69 homolog B [Homo sapiens].
ACCESSION   NP_001356494 XP_005271194
VERSION     NP_001356494.1
DBSOURCE    REFSEQ: accession NM_001369565.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Oleksiewicz,U., Machnik,M., Sobocinska,J., Molenda,S.,
            Olechnowicz,A., Florczak,A., Mierzejewska,J., Adamczak,D.,
            Smolibowski,M., Kaczmarek,M. and Mackiewicz,A.
  TITLE     ZNF643/ZFP69B Exerts Oncogenic Properties and Associates with Cell
            Adhesion and Immune Processes
  JOURNAL   Int J Mol Sci 24 (22), 16380 (2023)
   PUBMED   38003570
  REMARK    GeneRIF: ZNF643/ZFP69B Exerts Oncogenic Properties and Associates
            with Cell Adhesion and Immune Processes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Serebrenik,Y.V., Hellerschmied,D., Toure,M., Lopez-Giraldez,F.,
            Brookner,D. and Crews,C.M.
  TITLE     Targeted protein unfolding uncovers a Golgi-specific
            transcriptional stress response
  JOURNAL   Mol Biol Cell 29 (11), 1284-1298 (2018)
   PUBMED   29851555
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031985.10.
            
            On Apr 11, 2019 this sequence version replaced XP_005271194.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.16325.1,
                                           SRR1660807.118045.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..534
                     /product="zinc finger protein 69 homolog B"
                     /note="novel zinc finger protein; zinc finger protein 643;
                     zinc finger protein ZFP69B"
                     /calculated_mol_wt=61350
     Region          <2..40
                     /region_name="SCAN"
                     /note="SCAN domain; pfam02023"
                     /db_xref="CDD:460417"
     Region          74..133
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <221..429
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          257..273
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          281..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(281,284,297,301)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          309..329
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(309,312,325,329)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(314,316,318,320..321,324..325,328,342,344,348..349,
                     352..353,356,370,372,374,376..377,380..381,384)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          337..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          365..385
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          393..413
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(393,396,409,413)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          421..441
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(421,424,437,441)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          433..458
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          449..469
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(449,452,465,469)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(454,456,458,460..461,464..465,468,482,484,488..489,
                     492..493,496,510,512,514,516..517,520..521,524)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          461..486
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          477..497
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          489..514
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          505..525
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..534
                     /gene="ZFP69B"
                     /gene_synonym="ZKSCAN23B; ZNF643; ZSCAN54B"
                     /coded_by="NM_001369565.1:419..2023"
                     /db_xref="CCDS:CCDS452.2"
                     /db_xref="GeneID:65243"
                     /db_xref="HGNC:HGNC:28053"
ORIGIN      
        1 mlqqllitlp teastwvklr hpkaaterva lwedvtkmfk aeallsqdad etqgeslesr
       61 vtlgsltaes qelltfkdvs vdftqeewgq lapahrnlyr evmlenygnl vsvgcqlskp
      121 gvisqlekge epwlmerdis gvpssdlksk tktkesalqn disweelhcg lmmerftkgs
      181 smystlgris kcnklesqqe nqrmgkgqip lmckktftqe rgqesnrfek rinvksevmp
      241 gpiglprkrd rkydtpgkrs rynidlvnhs rsytkmktfe cnicekifkq lihltehmri
      301 htgekpfrck ecgkafsqss sliphqriht gekpyeckec gktfrhpssl tqhvrihtge
      361 kpyecrvcek afsqsigliq hlrthvrekp ftckdcgkaf fqirhlrqhe iihtgvkpyi
      421 cnvcsktfsh styltqhqrt htgerpykck ecgkafsqri hlsihqrvht gvkpyecshc
      481 gkafrhdssf akhqrihtge kpydcnecgk afscssslir hckthlrntf snvv
//
LOCUS       NP_001354972             170 aa            linear   ROD 27-APR-2025
DEFINITION  phospholipid hydroperoxide glutathione peroxidase isoform C [Rattus
            norvegicus].
ACCESSION   NP_001354972
VERSION     NP_001354972.1
DBSOURCE    REFSEQ: accession NM_001368043.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Chen,B., Fan,P., Song,X. and Duan,M.
  TITLE     The role and possible mechanism of the ferroptosis-related
            SLC7A11/GSH/GPX4 pathway in myocardial ischemia-reperfusion injury
  JOURNAL   BMC Cardiovasc Disord 24 (1), 531 (2024)
   PUBMED   39354361
  REMARK    GeneRIF: The role and possible mechanism of the ferroptosis-related
            SLC7A11/GSH/GPX4 pathway in myocardial ischemia-reperfusion injury.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Liu,D., Ren,L. and Liu,J.
  TITLE     METTL14 promotes chondrocyte ferroptosis in osteoarthritis via m6A
            modification of GPX4
  JOURNAL   Int J Rheum Dis 27 (8), e15297 (2024)
   PUBMED   39175261
  REMARK    GeneRIF: METTL14 promotes chondrocyte ferroptosis in osteoarthritis
            via m6A modification of GPX4.
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Chen,D., Tang,Q., Song,W. and He,Y.
  TITLE     Platelet-derived exosomes alleviate tendon stem/progenitor cell
            senescence and ferroptosis by regulating AMPK/Nrf2/GPX4 signaling
            and improve tendon-bone junction regeneration in rats
  JOURNAL   J Orthop Surg Res 19 (1), 382 (2024)
   PUBMED   38943181
  REMARK    GeneRIF: Platelet-derived exosomes alleviate tendon stem/progenitor
            cell senescence and ferroptosis by regulating AMPK/Nrf2/GPX4
            signaling and improve tendon-bone junction regeneration in rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Pfeifer,H., Conrad,M., Roethlein,D., Kyriakopoulos,A.,
            Brielmeier,M., Bornkamm,G.W. and Behne,D.
  TITLE     Identification of a specific sperm nuclei selenoenzyme necessary
            for protamine thiol cross-linking during sperm maturation
  JOURNAL   FASEB J 15 (7), 1236-1238 (2001)
   PUBMED   11344099
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Ursini,F., Heim,S., Kiess,M., Maiorino,M., Roveri,A., Wissing,J.
            and Flohe,L.
  TITLE     Dual function of the selenoprotein PHGPx during sperm maturation
  JOURNAL   Science 285 (5432), 1393-1396 (1999)
   PUBMED   10464096
  REMARK    GeneRIF: Rat Gpx4 is a moonlighting protein that functions both as
            a peroxidase, as well as a structural protein.
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Arai,M., Imai,H., Koumura,T., Yoshida,M., Emoto,K., Umeda,M.,
            Chiba,N. and Nakagawa,Y.
  TITLE     Mitochondrial phospholipid hydroperoxide glutathione peroxidase
            plays a major role in preventing oxidative injury to cells
  JOURNAL   J Biol Chem 274 (8), 4924-4933 (1999)
   PUBMED   9988735
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Pushpa-Rekha,T.R., Burdsall,A.L., Oleksa,L.M., Chisolm,G.M. and
            Driscoll,D.M.
  TITLE     Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning
            and identification of multiple transcription and translation start
            sites
  JOURNAL   J Biol Chem 270 (45), 26993-26999 (1995)
   PUBMED   7592947
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Imai,H., Sumi,D., Hanamoto,A., Arai,M. and Sugiyama,A.
  TITLE     Molecular cloning and functional expression of a cDNA for rat
            phospholipid hydroperoxide glutathione peroxidase: 3'-untranslated
            region of the gene is necessary for functional expression
  JOURNAL   J Biochem 118 (5), 1061-1067 (1995)
   PUBMED   8749327
REFERENCE   9  (residues 1 to 170)
  AUTHORS   Roveri,A., Casasco,A., Maiorino,M., Dalan,P., Calligaro,A. and
            Ursini,F.
  TITLE     Phospholipid hydroperoxide glutathione peroxidase of rat testis.
            Gonadotropin dependence and immunocytochemical identification
  JOURNAL   J Biol Chem 267 (9), 6142-6146 (1992)
   PUBMED   1556123
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Thomas,J.P., Geiger,P.G., Maiorino,M., Ursini,F. and Girotti,A.W.
  TITLE     Enzymatic reduction of phospholipid and cholesterol hydroperoxides
            in artificial bilayers and lipoproteins
  JOURNAL   Biochim Biophys Acta 1045 (3), 252-260 (1990)
   PUBMED   2386798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000007.1.
            
            Summary: The protein encoded by this gene belongs to the
            glutathione peroxidase family, members of which catalyze the
            reduction of hydrogen peroxide, organic hydroperoxides and lipid
            hydroperoxides, and thereby protect cells against oxidative damage.
            Several isozymes of this gene family exist in vertebrates, which
            vary in cellular location and substrate specificity. This isozyme
            has a high preference for lipid hydroperoxides and protects cells
            against membrane lipid peroxidation and cell death. It is also
            required for normal sperm development; thus, it has been identified
            as a 'moonlighting' protein because of its ability to serve dual
            functions as a peroxidase, as well as a structural protein in
            mature spermatozoa. Disruption of this gene in mouse spermatocytes
            is associated with male infertility. This isozyme is also a
            selenoprotein, containing the rare amino acid selenocysteine (Sec)
            at its active site. Sec is encoded by the UGA codon, which normally
            signals translation termination. The 3' UTRs of selenoprotein mRNAs
            contain a conserved stem-loop structure, designated the Sec
            insertion sequence (SECIS) element, that is necessary for the
            recognition of UGA as a Sec codon, rather than as a stop signal.
            Transcript variants resulting from alternative splicing or use of
            alternate promoters have been described to encode isoforms with
            different subcellular localization. Pseudogenes of this locus have
            been identified on chromosomes 1, 10 and 14. [provided by RefSeq,
            Jan 2019].
            
            Transcript Variant: This variant (3) uses an alternate promoter,
            which results in translation initiation from an in-frame downstream
            AUG start codon compared to variant 1. The encoded isoform (C, also
            known as the S-form) has a shorter N-terminus compared to isoform A
            and is localized in the cytoplasm (PMIDs:7592947, 9988735).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ221899.1, FQ234630.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 9988735
            multifunctional gene product(s)    :: PMID: 10464096
            protein contains selenocysteine    :: PMID: 8749327
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..170
                     /product="phospholipid hydroperoxide glutathione
                     peroxidase isoform C"
                     /EC_number="1.11.1.9"
                     /EC_number="1.11.1.12"
                     /note="phospholipid hydroperoxide glutathione peroxidase,
                     nuclear; phospholipid hydroperoxide glutathione
                     peroxidase, mitochondrial"
                     /calculated_mol_wt=19359
     Region          13..166
                     /region_name="GSH_Peroxidase"
                     /note="Glutathione (GSH) peroxidase family; tetrameric
                     selenoenzymes that catalyze the reduction of a variety of
                     hydroperoxides including lipid peroxidases, using GSH as a
                     specific electron donor substrate. GSH peroxidase contains
                     one selenocysteine residue per...; cd00340"
                     /db_xref="CDD:238207"
     Site            order(46,81,136)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238207"
     Site            46
                     /site_type="other"
                     /note="Selenocysteine"
     Site            order(80,83,85,88,91,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238207"
     CDS             1..170
                     /gene="Gpx4"
                     /gene_synonym="gpx-4; Gshpx-4; Phgpx; snGpx"
                     /coded_by="NM_001368043.1:56..568"
                     /note="UGA stop codon recoded as selenocysteine; isoform C
                     is encoded by transcript variant 3"
                     /db_xref="GeneID:29328"
                     /db_xref="RGD:69226"
ORIGIN      
        1 mcasrddwrc arsmhefaak didghmvcld kyrgcvcivt nvasqugktd vnytqlvdlh
       61 aryaecglri lafpcnqfgr qepgsnqeik efaagynvrf dmyskicvng ddahplwkwm
      121 kvqpkgrgml gnaikwnftk flidkngcvv krygpmeepq viekdlpcyl
//
LOCUS       NP_031509                196 aa            linear   ROD 27-APR-2025
DEFINITION  rho-related GTP-binding protein RhoB [Mus musculus].
ACCESSION   NP_031509
VERSION     NP_031509.1
DBSOURCE    REFSEQ: accession NM_007483.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Englert,M., Aurbach,K., Becker,I.C., Gerber,A., Heib,T.,
            Wackerbarth,L.M., Kusch,C., Mott,K., Araujo,G.H.M., Baig,A.A.,
            Dutting,S., Knaus,U.G., Stigloher,C., Schulze,H., Nieswandt,B.,
            Pleines,I. and Nagy,Z.
  TITLE     Impaired microtubule dynamics contribute to microthrombocytopenia
            in RhoB-deficient mice
  JOURNAL   Blood Adv 6 (17), 5184-5197 (2022)
   PUBMED   35819450
  REMARK    GeneRIF: Impaired microtubule dynamics contribute to
            microthrombocytopenia in RhoB-deficient mice.
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Zhang,D., Wang,Y., Zeng,S., Zhang,M., Zhang,X., Wang,Y., Zhang,Z.,
            Wang,X. and Hu,X.
  TITLE     Integrated Analysis of Prognostic Genes Associated With
            Ischemia-Reperfusion Injury in Renal Transplantation
  JOURNAL   Front Immunol 12, 747020 (2021)
   PUBMED   34557203
  REMARK    GeneRIF: Integrated Analysis of Prognostic Genes Associated With
            Ischemia-Reperfusion Injury in Renal Transplantation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Miao,C., Yu,M., Pei,G., Ma,Z., Zhang,L., Yang,J., Lv,J.,
            Zhang,Z.S., Keller,E.T., Yao,Z. and Wang,Q.
  TITLE     An infection-induced RhoB-Beclin 1-Hsp90 complex enhances clearance
            of uropathogenic Escherichia coli
  JOURNAL   Nat Commun 12 (1), 2587 (2021)
   PUBMED   33972537
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Lv,T., Kong,L., Jiang,L., Wu,H., Wen,T., Shi,Y. and Yang,J.
  TITLE     Dicer1 facilitates liver regeneration in a manner dependent on the
            inhibitory effect of miR-21 on Pten and Rhob expression
  JOURNAL   Life Sci 232, 116656 (2019)
   PUBMED   31306658
  REMARK    GeneRIF: identified the promotion effect of Dicer1 on liver
            regeneration by increasing miR-21 expression, which inhibits the
            expression of two negative cell proliferation regulators, Pten and
            Rhob
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Reid,T., Furuyashiki,T., Ishizaki,T., Watanabe,G., Watanabe,N.,
            Fujisawa,K., Morii,N., Madaule,P. and Narumiya,S.
  TITLE     Rhotekin, a new putative target for Rho bearing homology to a
            serine/threonine kinase, PKN, and rhophilin in the rho-binding
            domain
  JOURNAL   J Biol Chem 271 (23), 13556-13560 (1996)
   PUBMED   8662891
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Madaule,P., Furuyashiki,T., Reid,T., Ishizaki,T., Watanabe,G.,
            Morii,N. and Narumiya,S.
  TITLE     A novel partner for the GTP-bound forms of rho and rac
  JOURNAL   FEBS Lett 377 (2), 243-248 (1995)
   PUBMED   8543060
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Fritz,G., Kaina,B. and Aktories,K.
  TITLE     The ras-related small GTP-binding protein RhoB is immediate-early
            inducible by DNA damaging treatments
  JOURNAL   J Biol Chem 270 (42), 25172-25177 (1995)
   PUBMED   7559652
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Hall,A.
  TITLE     Small GTP-binding proteins and the regulation of the actin
            cytoskeleton
  JOURNAL   Annu Rev Cell Biol 10, 31-54 (1994)
   PUBMED   7888179
  REMARK    Review article
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Adamson,P., Marshall,C.J., Hall,A. and Tilbrook,P.A.
  TITLE     Post-translational modifications of p21rho proteins
  JOURNAL   J Biol Chem 267 (28), 20033-20038 (1992)
   PUBMED   1400319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK164518.1 and BC023334.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 3.88 cM"
     Protein         1..196
                     /product="rho-related GTP-binding protein RhoB"
                     /note="ras homolog gene family, member AB; aplysia
                     ras-related homolog B; ras homolog B; ras homolog gene
                     family, member B"
                     /calculated_mol_wt=21992
     mat_peptide     1..193
                     /product="Rho-related GTP-binding protein RhoB.
                     /id=PRO_0000030419"
                     /note="propagated from UniProtKB/Swiss-Prot (P62746.1)"
                     /calculated_mol_wt=21783
     Region          5..179
                     /region_name="RhoA_like"
                     /note="Ras homology family A (RhoA)-like includes RhoA,
                     RhoB and RhoC; cd01870"
                     /db_xref="CDD:206662"
     Site            order(5,34,37..38,41,43,45,54,58..59,61..63,66,68,72)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206662"
     Site            order(15..20,34..35,37,59..60,118,120,161..162)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206662"
     Site            order(23,25..29,42..43,45..47,52..54,163..164,168..169,
                     172)
                     /site_type="active"
                     /note="PKN/PRK1 effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(34,36,38..39,63..66,69,72,94)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Region          34..42
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P62746.1)"
     Site            34..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206662"
     Site            order(37..38,61,66,68..69,71..72,75,105..106,108)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206662"
     Site            order(39,65..69,72,97,101,105)
                     /site_type="active"
                     /note="Mdia effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(39..40,65..66,68..69,72)
                     /site_type="other"
                     /note="Rho kinase (ROCK) effector interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206662"
     Site            62..79
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206662"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206662"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18034455; propagated from
                     UniProtKB/Swiss-Prot (P62746.1)"
     Site            160..162
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206662"
     Site            193
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P62746.1)"
     CDS             1..196
                     /gene="Rhob"
                     /gene_synonym="Arh6; Arhb"
                     /coded_by="NM_007483.3:378..968"
                     /db_xref="CCDS:CCDS25799.1"
                     /db_xref="GeneID:11852"
                     /db_xref="MGI:MGI:107949"
ORIGIN      
        1 maairkklvv vgdgacgktc llivfskdef pevyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvi lmcfsvdspd slenipekwv pevkhfcpnv piilvankkd
      121 lrsdehvrte larmkqepvr tddgramavr iqaydylecs aktkegvrev fetatraalq
      181 krygsqngci ncckvl
//
LOCUS       NP_001353497             835 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001353497
VERSION     NP_001353497.1
DBSOURCE    REFSEQ: accession NM_001366568.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.55303.1,
                                           SRR1803616.98051.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..835
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 6"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=94173
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <537..>671
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..835
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366568.1:2344..4851"
                     /note="isoform 6 is encoded by transcript variant 8"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels eseedkggkm aaadsvqqrr qyrrqnqqss sdsgssssse
      421 derpkrshvk ngevgrrrrh spsrsaspsp rkrqketspr mqmgkrwqsp vtksgrrrrs
      481 psppptrrrr spspappprr rrtptppprr rtpsppprrr spsprryspp iqrryspspp
      541 pkrrtasppp ppkrraspsp ppkrrvshsp ppkqrsspvt krrspslssk hrkgsspsrs
      601 trearspqpn krhspsprpr apqtsssppp vrrgassspq rrqspspstr pirrvsrtpe
      661 pkkikkaasp spqsvrrvss srsvsgspep aakkppapps pvqsqspstn wspavpvkka
      721 ksptpspspp rnsdqegggk kkkkkkdkkh kkdkkhkkhk khkkekavaa aaaaavtpaa
      781 iaaatttlaq eepvaapepk keteseaedn lddlekhlre kalrsmrkaq vspqs
//
LOCUS       NP_001352976             321 aa            linear   PRI 27-APR-2025
DEFINITION  protein ABHD18 isoform 13 [Homo sapiens].
ACCESSION   NP_001352976
VERSION     NP_001352976.1
DBSOURCE    REFSEQ: accession NM_001366047.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099340.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.74003.1, BC128142.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.2"
     Protein         1..321
                     /product="protein ABHD18 isoform 13"
                     /note="abhydrolase domain-containing protein 18;
                     alpha/beta hydrolase domain-containing protein 18; protein
                     ABHD18"
                     /calculated_mol_wt=35836
     Region          <1..321
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
     CDS             1..321
                     /gene="ABHD18"
                     /gene_synonym="C4orf29"
                     /coded_by="NM_001366047.1:499..1464"
                     /note="isoform 13 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS93632.1"
                     /db_xref="GeneID:80167"
                     /db_xref="HGNC:HGNC:26111"
ORIGIN      
        1 marpmikear maslllenpy ygcrkpkdqv rsslknvsdl fvmggalvle saallhwler
       61 egygplgmtg ismgghmasl avsnwpkpmp lipclswsta sgvfttgvls ksinwrelek
      121 qyytqtvyee eiihmleycg tdsfkmgqef vkhftssadk ltnlnlvsrt lnldisnqvv
      181 sqkpadchns sktsvsatse glllqdtskm krfnqtlstn ksgytsrnpq syhllskeqs
      241 rnslrkesli fmkgvmdect hvanfsvpvd psliivvqak edayiprtgv rslqeiwpgc
      301 eirylegghi saylfkqglf r
//
LOCUS       NP_742034                341 aa            linear   PRI 27-APR-2025
DEFINITION  retinol dehydrogenase 10 [Homo sapiens].
ACCESSION   NP_742034
VERSION     NP_742034.1
DBSOURCE    REFSEQ: accession NM_172037.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Zhao,Z., Song,Z., Wang,Z., Zhang,F., Ding,Z., Zhao,Z., Liu,L. and
            Fan,T.
  TITLE     Retinol dehydrogenase 10 promotes epithelial-mesenchymal transition
            in spinal cord gliomas via PI3K/AKT pathway
  JOURNAL   Int J Immunopathol Pharmacol 38, 3946320241276336 (2024)
   PUBMED   39180753
  REMARK    GeneRIF: Retinol dehydrogenase 10 promotes epithelial-mesenchymal
            transition in spinal cord gliomas via PI3K/AKT pathway.
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Murakami,A., Amano,T., Yoshino,F., Kita,H., Moritani,S.,
            Murakami,T. and Chano,T.
  TITLE     Retinol dehydrogenase 10 contributes to cancer stemness and
            intracellular carbohydrate storage in ovarian clear cell carcinomas
  JOURNAL   Cancer Biomark 34 (4), 673-679 (2022)
   PUBMED   35634847
  REMARK    GeneRIF: Retinol dehydrogenase 10 contributes to cancer stemness
            and intracellular carbohydrate storage in ovarian clear cell
            carcinomas.
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Klyuyeva,A.V., Belyaeva,O.V., Goggans,K.R., Krezel,W., Popov,K.M.
            and Kedishvili,N.Y.
  TITLE     Changes in retinoid metabolism and signaling associated with
            metabolic remodeling during fasting and in type I diabetes
  JOURNAL   J Biol Chem 296, 100323 (2021)
   PUBMED   33485967
  REMARK    GeneRIF: Changes in retinoid metabolism and signaling associated
            with metabolic remodeling during fasting and in type I diabetes.
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Guan,F., Kang,Z., Wang,L., Wang,K., Mao,B.B., Peng,W.C.,
            Zhang,B.L., Lin,Z.Y., Zhang,J.T. and Hu,Z.Q.
  TITLE     Retinol dehydrogenase 10 promotes metastasis of glioma cells via
            the transforming growth factor-beta/SMAD signaling pathway
  JOURNAL   Chin Med J (Engl) 132 (20), 2430-2437 (2019)
   PUBMED   31613821
  REMARK    GeneRIF: RDH10 regulated the migration and invasion of glioma cells
            via the TGF-beta/SMAD signaling pathway.
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Belyaeva,O.V., Johnson,M.P. and Kedishvili,N.Y.
  TITLE     Kinetic analysis of human enzyme RDH10 defines the characteristics
            of a physiologically relevant retinol dehydrogenase
  JOURNAL   J Biol Chem 283 (29), 20299-20308 (2008)
   PUBMED   18502750
  REMARK    GeneRIF: dual physiological role for RDH10: in the biosynthesis of
            11-cis-retinaldehyde for vision as well as the biosynthesis of
            all-trans-retinoic acid for differentiation and development
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Rossi,E., Picozzi,P., Bodega,B., Lavazza,C., Carlo-Stella,C.,
            Marozzi,A. and Ginelli,E.
  TITLE     Forced expression of RDH10 gene retards growth of HepG2 cells
  JOURNAL   Cancer Biol Ther 6 (2), 238-244 (2007)
   PUBMED   17218779
  REMARK    GeneRIF: Forced over-expression of the RDH10 gene causes growth
            arrest of HepG2 cells and could be a possible curative strategy for
            hepatocellular carcinoma.
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Picozzi,P., Marozzi,A., Fornasari,D., Benfante,R., Barisani,D.,
            Meneveri,R. and Ginelli,E.
  TITLE     Genomic organization and transcription of the human retinol
            dehydrogenase 10 (RDH10) gene
  JOURNAL   FEBS Lett 554 (1-2), 59-66 (2003)
   PUBMED   14596915
  REMARK    GeneRIF: organization of the gene includes a unique transcriptional
            start site, a coding region with six translated exons and a 3' UTR
            containing at least two used polyadenylation sites.
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Wu,B.X., Chen,Y., Chen,Y., Fan,J., Rohrer,B., Crouch,R.K. and
            Ma,J.X.
  TITLE     Cloning and characterization of a novel all-trans retinol
            short-chain dehydrogenase/reductase from the RPE
  JOURNAL   Invest Ophthalmol Vis Sci 43 (11), 3365-3372 (2002)
   PUBMED   12407145
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD110145.1, AF456765.1,
            BC067131.1, AC111149.4, BM472905.1, BM804062.1 and BM979260.1.
            
            Summary: This gene encodes a retinol dehydrogenase, which converts
            all-trans-retinol to all-trans-retinal, with preference for NADP as
            a cofactor. Studies in mice suggest that this protein is essential
            for synthesis of embryonic retinoic acid and is required for limb,
            craniofacial, and organ development. [provided by RefSeq, Dec
            2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC067131.1, SRR1660805.173060.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000240285.10/ ENSP00000240285.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..341
                     /product="retinol dehydrogenase 10"
                     /EC_number="1.1.1.300"
                     /note="short chain dehydrogenase/reductase family 16C
                     member 4; retinol dehydrogenase 10 (all-trans)"
                     /calculated_mol_wt=37957
     Site            3..23
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZV5.1)"
     Region          38..307
                     /region_name="17beta-HSDXI-like_SDR_c"
                     /note="human 17-beta-hydroxysteroid dehydrogenase XI-like,
                     classical (c) SDRs; cd05339"
                     /db_xref="CDD:187598"
     Site            order(43,45..48,67..69,117..119,145..147,168,195..197,210,
                     214,243..246,248..249)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187598"
     Site            order(122,126,158..159,162..163,166,170..171,174..175,178,
                     207..209,211..212,215..216,219..220,222..224,226..227,
                     249..251,295..296,299,303)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187598"
     Site            order(169,197,210,214)
                     /site_type="active"
                     /db_xref="CDD:187598"
     Site            order(178,181,224,227,233)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187598"
     CDS             1..341
                     /gene="RDH10"
                     /gene_synonym="SDR16C4"
                     /coded_by="NM_172037.5:689..1714"
                     /db_xref="CCDS:CCDS6213.1"
                     /db_xref="GeneID:157506"
                     /db_xref="HGNC:HGNC:19975"
                     /db_xref="MIM:607599"
ORIGIN      
        1 mnivveffvv tfkvlwafvl aaarwlvrpk eksvagqvcl itgagsglgr lfalefarrr
       61 allvlwdint qsneetagmv rhiyrdleaa daaalqagng eeeilphcnl qvftytcdvg
      121 krenvyltae rvrkevgevs vlvnnagvvs ghhllecpde liertmmvnc hahfwttkaf
      181 lptmleinhg hivtvasslg lfstagvedy caskfgvvgf heslshelka aekdgikttl
      241 vcpylvdtgm frgcrirkei epflpplkpd ycvkqamkai ltdqpmictp rlmyivtfmk
      301 silpfeavvc myrflgadkc mypfiaqrkq atnnneakng i
//
LOCUS       NP_000181                361 aa            linear   PRI 27-APR-2025
DEFINITION  porphobilinogen deaminase isoform 1 [Homo sapiens].
ACCESSION   NP_000181
VERSION     NP_000181.2
DBSOURCE    REFSEQ: accession NM_000190.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   M,K., M,R., J,B., A,B.I., K,I.P., R,W., E,O., A,Z.K., R,S. and R,P.
  TITLE     Neurodevelopmental disorder in a patient with HMBS and SCN3A
            variants-A possibly blended phenotype further delineating autosomal
            recessive HMBS related disease
  JOURNAL   Am J Med Genet A 194 (8), e63617 (2024)
   PUBMED   38568055
  REMARK    GeneRIF: Neurodevelopmental disorder in a patient with HMBS and
            SCN3A variants-A possibly blended phenotype further delineating
            autosomal recessive HMBS related disease.
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Hu,Y., Li,W., Kang,N., Ma,L., Teng,Q., Mo,G., Wu,J., Wang,X., Bi,R.
            and Zhang,S.
  TITLE     Identification and molecular analysis of 17 novel variants of
            hydroxymethylbilane synthase in Chinese patients with acute
            intermittent porphyria
  JOURNAL   Clin Genet 101 (1), 116-121 (2022)
   PUBMED   34523126
  REMARK    GeneRIF: Identification and molecular analysis of 17 novel variants
            of hydroxymethylbilane synthase in Chinese patients with acute
            intermittent porphyria.
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Zhang,Y., Xiao,H., Xiong,Q., Wu,C. and Li,P.
  TITLE     Two Novel Hydroxymethylbilane Synthase Splicing Mutations
            Predispose to Acute Intermittent Porphyria
  JOURNAL   Int J Mol Sci 22 (20), 11008 (2021)
   PUBMED   34681668
  REMARK    GeneRIF: Two Novel Hydroxymethylbilane Synthase Splicing Mutations
            Predispose to Acute Intermittent Porphyria.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Stutterd,C.A., Kidd,A., Florkowski,C., Janus,E., Fanjul,M.,
            Raizis,A., Wu,T.Y., Archer,J., Leventer,R.J., Amor,D.J., Lukic,V.,
            Bahlo,M., Gow,P., Lockhart,P.J., van der Knaap,M.S. and
            Delatycki,M.B.
  TITLE     Expanding the clinical and radiological phenotypes of
            leukoencephalopathy due to biallelic HMBS mutations
  JOURNAL   Am J Med Genet A 185 (10), 2941-2950 (2021)
   PUBMED   34089223
  REMARK    GeneRIF: Expanding the clinical and radiological phenotypes of
            leukoencephalopathy due to biallelic HMBS mutations.
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Jerico,D., Luis,E.O., Cusso,L., Fernandez-Seara,M.A., Morales,X.,
            Cordoba,K.M., Benito,M., Sampedro,A., Larriva,M., Ramirez,M.J., de
            Salamanca,R.E., Ortiz-de-Solorzano,C., Alegre,M., Prieto,J.,
            Lanciego,J.L., D'Avola,D., Gonzalez-Aseguinolaza,G., Pastor,M.A.,
            Desco,M. and Fontanellas,A.
  TITLE     Brain ventricular enlargement in human and murine acute
            intermittent porphyria
  JOURNAL   Hum Mol Genet 29 (19), 3211-3223 (2020)
   PUBMED   32916704
  REMARK    GeneRIF: Brain ventricular enlargement in human and murine acute
            intermittent porphyria.
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Sardh,E. and Barbaro,M.
  TITLE     Acute Intermittent Porphyria
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301372
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Gu,X.F., de Rooij,F., Voortman,G., Te Velde,K., Nordmann,Y. and
            Grandchamp,B.
  TITLE     High frequency of mutations in exon 10 of the porphobilinogen
            deaminase gene in patients with a CRIM-positive subtype of acute
            intermittent porphyria
  JOURNAL   Am J Hum Genet 51 (3), 660-665 (1992)
   PUBMED   1496994
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Mgone,C.S., Lanyon,W.G., Moore,M.R. and Connor,J.M.
  TITLE     Detection of seven point mutations in the porphobilinogen deaminase
            gene in patients with acute intermittent porphyria, by direct
            sequencing of in vitro amplified cDNA
  JOURNAL   Hum Genet 90 (1-2), 12-16 (1992)
   PUBMED   1427766
REFERENCE   9  (residues 1 to 361)
  AUTHORS   Kauppinen,R., Peltonen,L., Pihlaja,H. and Mustajoki,P.
  TITLE     CRIM-positive mutations of acute intermittent porphyria in Finland
  JOURNAL   Hum Mutat 1 (5), 392-396 (1992)
   PUBMED   1301948
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Delfau,M.H., Picat,C., De Rooij,F., Voortman,G., Deybach,J.C.,
            Nordmann,Y. and Grandchamp,B.
  TITLE     Molecular heterogeneity of acute intermittent porphyria:
            identification of four additional mutations resulting in the
            CRIM-negative subtype of the disease
  JOURNAL   Am J Hum Genet 49 (2), 421-428 (1991)
   PUBMED   1714233
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB128006.1, BC019323.1 and
            AW139390.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 15, 2002 this sequence version replaced NP_000181.1.
            
            Summary: This gene encodes a member of the hydroxymethylbilane
            synthase superfamily. The encoded protein is the third enzyme of
            the heme biosynthetic pathway and catalyzes the head to tail
            condensation of four porphobilinogen molecules into the linear
            hydroxymethylbilane. Mutations in this gene are associated with the
            autosomal dominant disease acute intermittent porphyria.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290275.1, SRR1163655.660423.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000652429.1/ ENSP00000498786.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..361
                     /product="porphobilinogen deaminase isoform 1"
                     /EC_number="2.5.1.61"
                     /note="porphyria, acute; Chester type;
                     pre-uroporphyrinogen synthase; uroporphyrinogen I
                     synthase; uroporphyrinogen I synthetase; porphobilinogen
                     deaminase"
                     /calculated_mol_wt=39199
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P08397.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08397.2)"
     Region          20..299
                     /region_name="PBP2_HuPBGD_like"
                     /note="Human porphobilinogen deaminase possess type 2
                     periplasmic binding protein fold; cd13645"
                     /db_xref="CDD:270363"
     Site            order(26,30,77,98..99,145..147,149..150,166..170,173,214,
                     261)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270363"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08397.2)"
     Site            74
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P22907; propagated from
                     UniProtKB/Swiss-Prot (P08397.2)"
     Site            order(116,194,203,205,271..272)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270363"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08397.2)"
     CDS             1..361
                     /gene="HMBS"
                     /gene_synonym="ENCEP; LENCEP; PBG-D; PBGD; PORC; UPS"
                     /coded_by="NM_000190.4:154..1239"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8409.1"
                     /db_xref="GeneID:3145"
                     /db_xref="HGNC:HGNC:4982"
                     /db_xref="MIM:609806"
ORIGIN      
        1 msgngnaaat aeenspkmrv irvgtrksql ariqtdsvva tlkasypglq feiiamsttg
       61 dkildtalsk igekslftke lehaleknev dlvvhslkdl ptvlppgfti gaickrenph
      121 davvfhpkfv gktletlpek svvgtsslrr aaqlqrkfph lefrsirgnl ntrlrkldeq
      181 qefsaiilat aglqrmgwhn rvgqilhpee cmyavgqgal gvevrakdqd ildlvgvlhd
      241 petllrciae raflrhlegg csvpvavhta mkdgqlyltg gvwsldgsds iqetmqatih
      301 vpaqhedgpe ddpqlvgita rniprgpqla aqnlgislan lllskgakni ldvarqlnda
      361 h
//
LOCUS       NP_002901                427 aa            linear   PRI 27-APR-2025
DEFINITION  N-acylglucosamine 2-epimerase [Homo sapiens].
ACCESSION   NP_002901
VERSION     NP_002901.2
DBSOURCE    REFSEQ: accession NM_002910.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Wong,E.H., So,H.C., Li,M., Wang,Q., Butler,A.W., Paul,B., Wu,H.M.,
            Hui,T.C., Choi,S.C., So,M.T., Garcia-Barcelo,M.M., McAlonan,G.M.,
            Chen,E.Y., Cheung,E.F., Chan,R.C., Purcell,S.M., Cherny,S.S.,
            Chen,R.R., Li,T. and Sham,P.C.
  TITLE     Common variants on Xq28 conferring risk of schizophrenia in Han
            Chinese
  JOURNAL   Schizophr Bull 40 (4), 777-786 (2014)
   PUBMED   24043878
  REMARK    GeneRIF: rs2269372 in RENBP was associated with risk of
            schizophrenia in a Han Chinese population.
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Dong,Y., Ding,Y., Cun,Y. and Xiao,C.
  TITLE     Association of renin binding protein (RnBP) gene polymorphisms with
            essential hypertension in the Hani minority of southwestern China
  JOURNAL   J Genet Genomics 40 (8), 433-436 (2013)
   PUBMED   23969252
  REMARK    GeneRIF: several SNPs and haplotypes of the RnBP gene are
            associated with either increased or decreased risk of developing
            essential hypertension.
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Bergfeld,A.K., Pearce,O.M., Diaz,S.L., Pham,T. and Varki,A.
  TITLE     Metabolism of vertebrate amino sugars with N-glycolyl groups:
            elucidating the intracellular fate of the non-human sialic acid
            N-glycolylneuraminic acid
  JOURNAL   J Biol Chem 287 (34), 28865-28881 (2012)
   PUBMED   22692205
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Faranda,S., Frattini,A. and Vezzoni,P.
  TITLE     The human genes encoding renin-binding protein and host cell factor
            are closely linked in Xq28 and transcribed in the same direction
  JOURNAL   Gene 155 (2), 237-239 (1995)
   PUBMED   7721097
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Takahashi,S., Inoue,H. and Miyake,Y.
  TITLE     The human gene for renin-binding protein
  JOURNAL   J Biol Chem 267 (18), 13007-13013 (1992)
   PUBMED   1618798
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Inoue,H., Takahashi,S., Fukui,K. and Miyake,Y.
  TITLE     Genetic and molecular properties of human and rat renin-binding
            proteins with reference to the function of the leucine zipper motif
  JOURNAL   J Biochem 110 (4), 493-500 (1991)
   PUBMED   1723410
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Takahashi,S., Miura,R. and Miyake,Y.
  TITLE     A study on renin binding protein (RnBP) in the human kidney
  JOURNAL   J Biochem 97 (2), 671-677 (1985)
   PUBMED   3924907
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Murakami,K., Hirose,S., Chino,S., Ueno,N. and Miyazaki,H.
  TITLE     Properties of renin-binding protein
  JOURNAL   Clin Exp Hypertens A 4 (11-12), 2073-2081 (1982)
   PUBMED   6756682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK298125.1, D10232.1 and
            BC015558.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 19, 2008 this sequence version replaced NP_002901.1.
            
            Summary: The gene product inhibits renin activity by forming a
            dimer with renin, a complex known as high molecular weight renin.
            The encoded protein contains a leucine zipper domain, which is
            essential for its dimerization with renin. The gene product can
            catalyze the interconversion of N-acetylglucosamine to
            N-acetylmannosamine, indicating that it is a GlcNAc 2-epimerase.
            Transcript variants utilizing alternative promoters have been
            described in the literature. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no quality transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and PMID:1618798.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015558.2, SRR1163657.3013.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393700.8/ ENSP00000377303.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..427
                     /product="N-acylglucosamine 2-epimerase"
                     /EC_number="5.1.3.8"
                     /note="GlcNAc 2-epimerase; N-acetyl-D-glucosamine
                     2-epimerase; AGE"
                     /calculated_mol_wt=48700
     Region          14..407
                     /region_name="AGE"
                     /note="AGE domain; N-acyl-D-glucosamine 2-epimerase
                     domain; Responsible for intermediate epimerization during
                     biosynthesis of N-acetylneuraminic acid. Catalytic
                     mechanism is believed to be via nucleotide elimination and
                     readdition and is ATP modulated. AGE is...; cd00249"
                     /db_xref="CDD:238153"
     Site            order(23,30,79,95,402,406)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238153"
     Site            order(66,70,73,132,136,139,190,193..194,197,258,261,
                     264..265,323..324,328,387,391..392,395)
                     /site_type="active"
                     /note="putative active cleft [active]"
                     /db_xref="CDD:238153"
     Region          195..216
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P51606.4)"
     Site            390
                     /site_type="other"
                     /note="Important for enzyme activity.
                     /evidence=ECO:0000269|PubMed:10502668; propagated from
                     UniProtKB/Swiss-Prot (P51606.4)"
     CDS             1..427
                     /gene="RENBP"
                     /gene_synonym="RBP; RNBP"
                     /coded_by="NM_002910.6:34..1317"
                     /db_xref="CCDS:CCDS14738.2"
                     /db_xref="GeneID:5973"
                     /db_xref="HGNC:HGNC:9959"
                     /db_xref="MIM:312420"
ORIGIN      
        1 mskglparqd mekeretlqa wkervgqeld rvvafwmehs hdqehggfft clgregrvyd
       61 dlkyvwlqgr qvwmycrlyr tferfrhaql ldaakaggef llryarvapp gkkcafvltr
      121 dgrpvkvqrt ifsecfytma mnelwratge vryqteavem mdqivhwvqe dasglgrpql
      181 qgapaaepma vpmmllnlve qlgeadeela gkyaelgdwc arrilqhvqr dgqavlenvs
      241 eggkelpgcl grqqnpghtl eagwfllrhc irkgdpelra hvidkflllp fhsgwdpdhg
      301 glfyfqdadn fcptqlewam klwwphseam iaflmgysds gdpvllrlfy qvaeytfrqf
      361 rdpeygewfg ylsregkval sikggpfkgc fhvprclamc eemlgallsr papapspapt
      421 pacrgae
//
LOCUS       NP_036389                514 aa            linear   PRI 27-APR-2025
DEFINITION  HMG box-containing protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_036389
VERSION     NP_036389.2
DBSOURCE    REFSEQ: accession NM_012257.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Zhou,Y., Zhang,T., Wang,S., Yang,R., Jiao,Z., Lu,K., Li,H.,
            Jiang,W. and Zhang,X.
  TITLE     Targeting of HBP1/TIMP3 axis as a novel strategy against breast
            cancer
  JOURNAL   Pharmacol Res 194, 106846 (2023)
   PUBMED   37414199
  REMARK    GeneRIF: Targeting of HBP1/TIMP3 axis as a novel strategy against
            breast cancer.
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Yao,J., Luo,Y., Zeng,C., He,H. and Zhang,X.
  TITLE     UHRF1 regulates the transcriptional repressor HBP1 through MIF in T
            acute lymphoblastic leukemia
  JOURNAL   Oncol Rep 46 (1) (2021)
   PUBMED   34013373
  REMARK    GeneRIF: UHRF1 regulates the transcriptional repressor HBP1 through
            MIF in T acute lymphoblastic leukemia.
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Chan,C.Y., Chang,C.M., Chen,Y.H., Sheu,J.J., Lin,T.Y. and
            Huang,C.Y.
  TITLE     Regulatory role of transcription factor HBP1 in anticancer efficacy
            of EGFR inhibitor erlotinib in HNSCC
  JOURNAL   Head Neck 42 (10), 2958-2967 (2020)
   PUBMED   32677158
  REMARK    GeneRIF: Regulatory role of transcription factor HBP1 in anticancer
            efficacy of EGFR inhibitor erlotinib in HNSCC.
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Liu,W., Li,W.C., Pan,X.F., Sha,H., Gong,W.Q. and Yan,M.
  TITLE     HBP1 deficiency protects against stress-induced premature
            senescence of nucleus pulposus
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (17), 8685-8693 (2020)
   PUBMED   32964956
  REMARK    GeneRIF: HBP1 deficiency protects against stress-induced premature
            senescence of nucleus pulposus.
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Li,K., Zhou,Z., Li,J. and Xiang,R.
  TITLE     miR-146b Functions as an Oncogene in Oral Squamous Cell Carcinoma
            by Targeting HBP1
  JOURNAL   Technol Cancer Res Treat 19, 1533033820959404 (2020)
   PUBMED   33327874
  REMARK    GeneRIF: miR-146b Functions as an Oncogene in Oral Squamous Cell
            Carcinoma by Targeting HBP1.
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Shih,H.H., Xiu,M., Berasi,S.P., Sampson,E.M., Leiter,A.,
            Paulson,K.E. and Yee,A.S.
  TITLE     HMG box transcriptional repressor HBP1 maintains a proliferation
            barrier in differentiated liver tissue
  JOURNAL   Mol Cell Biol 21 (17), 5723-5732 (2001)
   PUBMED   11486012
  REMARK    GeneRIF: HBP1 regulates the cell cycle in liver regeneration and
            provides evidence for a role in tissue maintenance.
            Erratum:[Mol Cell Biol 2001 Nov;21(21):7535]
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Lemercier,C., Duncliffe,K., Boibessot,I., Zhang,H., Verdel,A.,
            Angelov,D. and Khochbin,S.
  TITLE     Involvement of retinoblastoma protein and HBP1 in histone H1(0)
            gene expression
  JOURNAL   Mol Cell Biol 20 (18), 6627-6637 (2000)
   PUBMED   10958660
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Zhuma,T., Tyrrell,R., Sekkali,B., Skavdis,G., Saveliev,A.,
            Tolaini,M., Roderick,K., Norton,T., Smerdon,S., Sedgwick,S.,
            Festenstein,R. and Kioussis,D.
  TITLE     Human HMG box transcription factor HBP1: a role in hCD2 LCR
            function
  JOURNAL   EMBO J 18 (22), 6396-6406 (1999)
   PUBMED   10562551
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Lavender,P., Vandel,L., Bannister,A.J. and Kouzarides,T.
  TITLE     The HMG-box transcription factor HBP1 is targeted by the pocket
            proteins and E1A
  JOURNAL   Oncogene 14 (22), 2721-2728 (1997)
   PUBMED   9178770
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Tevosian,S.G., Shih,H.H., Mendelson,K.G., Sheppard,K.A.,
            Paulson,K.E. and Yee,A.S.
  TITLE     HBP1: a HMG box transcriptional repressor that is targeted by the
            retinoblastoma family
  JOURNAL   Genes Dev 11 (3), 383-396 (1997)
   PUBMED   9030690
  REMARK    GeneRIF: HBP1 was isolated as a cell cycle inhibitor and HMG-box
            transcriptional repressor.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004492.1, BC017069.1 and AF182038.1.
            
            On Jun 10, 2002 this sequence version replaced NP_036389.1.
            
            Transcript Variant: This variant (2) contains an alternate 5' exon
            and uses a downstream start codon, compared to variant 1. Isoform 2
            has a shorter N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.145089.1,
                                           SRR1803613.189398.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222574.9/ ENSP00000222574.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..514
                     /product="HMG box-containing protein 1 isoform 2"
                     /note="HMG box-containing protein 1; high mobility group
                     box transcription factor 1"
                     /calculated_mol_wt=57514
     Region          150..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60381.2)"
     Region          214..340
                     /region_name="AXH"
                     /note="domain in Ataxins and HMG containing proteins;
                     smart00536"
                     /db_xref="CDD:197779"
     Region          435..503
                     /region_name="HMG-box_HBP1"
                     /note="high mobility group (HMG)-box found in HMG
                     box-containing protein 1 (HBP1) and similar proteins;
                     cd21988"
                     /db_xref="CDD:438804"
     Site            order(435..436,438..442,445..446,453,465..466,469,
                     472..473,480,484,487,491,494)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438804"
     CDS             1..514
                     /gene="HBP1"
                     /coded_by="NM_012257.4:199..1743"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5741.1"
                     /db_xref="GeneID:26959"
                     /db_xref="HGNC:HGNC:23200"
                     /db_xref="MIM:616714"
ORIGIN      
        1 mvwevktnqm pnavqklllv mdkrasgmnd slellqcnen lpsspgynsc dehmelddlp
       61 elqavqsdpt qsgmyqlssd vshqeyprss wnqntsdipe ttyrenevdw ltelaniats
      121 pqsplmqcsf ynrsspvhii atskslhsya rpppvssssk sepafphhhw keetpvrher
      181 ansesesgif cmsslsdddd lgwcnswpst vwhcflkgtr lcfhkgsnke wqdvedfara
      241 egcdneedlq mgihkgygsd glkllshees vsfgesvlkl tfdpgtvedg lltveckldh
      301 pfyvknkgws sfypsltvvq hgipccevhi gdvclppghp dainfddsgv fdtfksydft
      361 pmdssavyvl ssmarqrras lscggpggqd farsgfsknc gspgssqlss nslyakavkn
      421 hssgtvsats pnkckrpmna fmlfakkyrv eytqmypgkd nraisvilgd rwkkmkneer
      481 rmytleakal aeeqkrlnpd cwkrkrtnsg sqqh
//
LOCUS       NP_000023                587 aa            linear   PRI 27-APR-2025
DEFINITION  5-aminolevulinate synthase, erythroid-specific, mitochondrial
            isoform a precursor [Homo sapiens].
ACCESSION   NP_000023
VERSION     NP_000023.2
DBSOURCE    REFSEQ: accession NM_000032.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Zhao,Y., Zhu,L., Shi,D., Gao,J. and Fan,M.
  TITLE     Key Genes FECH and ALAS2 under Acute High-Altitude Exposure: A Gene
            Expression and Network Analysis Based on Expression Profile Data
  JOURNAL   Genes (Basel) 15 (8), 1075 (2024)
   PUBMED   39202434
  REMARK    GeneRIF: Key Genes FECH and ALAS2 under Acute High-Altitude
            Exposure: A Gene Expression and Network Analysis Based on
            Expression Profile Data.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Ono,K., Fujiwara,T., Saito,K., Nishizawa,H., Takahashi,N.,
            Suzuki,C., Ochi,T., Kato,H., Ishii,Y., Onodera,K., Ichikawa,S.,
            Fukuhara,N., Onishi,Y., Yokoyama,H., Yamada,R., Nakamura,Y.,
            Igarashi,K. and Harigae,H.
  TITLE     Congenital sideroblastic anemia model due to ALAS2 mutation is
            susceptible to ferroptosis
  JOURNAL   Sci Rep 12 (1), 9024 (2022)
   PUBMED   35637209
  REMARK    GeneRIF: Congenital sideroblastic anemia model due to ALAS2
            mutation is susceptible to ferroptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 587)
  AUTHORS   de Gennes,C., Lamoril,J., Borgel,A., Boi,C., Yao,R., Boileau,C. and
            Tchernitchko,D.
  TITLE     Severe iron overload in a woman with homeostatic iron regulator
            (HFE) and a novel 5'-aminolevulinate synthase 2 (ALAS2) mutations:
            interactions of multiple genetic determinants
  JOURNAL   Br J Haematol 196 (2), e17-e20 (2022)
   PUBMED   34490613
  REMARK    GeneRIF: Severe iron overload in a woman with homeostatic iron
            regulator (HFE) and a novel 5'-aminolevulinate synthase 2 (ALAS2)
            mutations: interactions of multiple genetic determinants.
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Oakley,J.H., Campagna,D.R., Sun,L., Rockowitz,S., Sliz,P.,
            Boudreaux,J., Woods,G. and Fleming,M.D.
  TITLE     A synonymous coding variant that alters ALAS2 splicing and causes
            X-linked sideroblastic anemia
  JOURNAL   Pediatr Blood Cancer 69 (1), e29309 (2022)
   PUBMED   34411431
  REMARK    GeneRIF: A synonymous coding variant that alters ALAS2 splicing and
            causes X-linked sideroblastic anemia.
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 587)
  AUTHORS   Balwani,M. and Desnick,R.
  CONSRTM   Porphyrias Consortium of the NIH-Sponsored Rare Diseases Clinical
            Research Network
  TITLE     X-Linked Protoporphyria
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23409301
REFERENCE   7  (residues 1 to 587)
  AUTHORS   Cotter,P.D., Baumann,M. and Bishop,D.F.
  TITLE     Enzymatic defect in 'X-linked' sideroblastic anemia: molecular
            evidence for erythroid delta-aminolevulinate synthase deficiency
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 4028-4032 (1992)
   PUBMED   1570328
REFERENCE   8  (residues 1 to 587)
  AUTHORS   Cotter,P.D., Willard,H.F., Gorski,J.L. and Bishop,D.F.
  TITLE     Assignment of human erythroid delta-aminolevulinate synthase
            (ALAS2) to a distal subregion of band Xp11.21 by PCR analysis of
            somatic cell hybrids containing X; autosome translocations
  JOURNAL   Genomics 13 (1), 211-212 (1992)
   PUBMED   1577484
REFERENCE   9  (residues 1 to 587)
  AUTHORS   Gardner,L.C., Smith,S.J. and Cox,T.M.
  TITLE     Biosynthesis of delta-aminolevulinic acid and the regulation of
            heme formation by immature erythroid cells in man
  JOURNAL   J Biol Chem 266 (32), 22010-22018 (1991)
   PUBMED   1939222
REFERENCE   10 (residues 1 to 587)
  AUTHORS   Cox,T.C., Bawden,M.J., Martin,A. and May,B.K.
  TITLE     Human erythroid 5-aminolevulinate synthase: promoter analysis and
            identification of an iron-responsive element in the mRNA
  JOURNAL   EMBO J 10 (7), 1891-1902 (1991)
   PUBMED   2050125
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313118.1 and BQ182291.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 23, 2005 this sequence version replaced NP_000023.1.
            
            Summary: The product of this gene specifies an erythroid-specific
            mitochondrially located enzyme. The encoded protein catalyzes the
            first step in the heme biosynthetic pathway. Defects in this gene
            cause X-linked pyridoxine-responsive sideroblastic anemia.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X60364.1, SRR3476690.828307.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000650242.1/
                                                  ENSP00000497236.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.21"
     Protein         1..587
                     /product="5-aminolevulinate synthase, erythroid-specific,
                     mitochondrial isoform a precursor"
                     /EC_number="2.3.1.37"
                     /note="delta-ALA synthetase; 5-aminolevulinate synthase,
                     erythroid-specific, mitochondrial; delta-ALA synthase 2;
                     5-aminolevulinic acid synthase 2; delta-aminolevulinate
                     synthase 2; aminolevulinate, delta-, synthase 2;
                     erythroid-specific delta-aminolevulinate synthase"
                     /calculated_mol_wt=59508
     transit_peptide 1..49
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:14643893; propagated from
                     UniProtKB/Swiss-Prot (P22557.2)"
                     /calculated_mol_wt=5143
     Region          5..100
                     /region_name="Preseq_ALAS"
                     /note="5-aminolevulinate synthase presequence; pfam09029"
                     /db_xref="CDD:462658"
     mat_peptide     50..587
                     /product="5-aminolevulinate synthase, erythroid-specific,
                     mitochondrial. /id=PRO_0000001223"
                     /note="propagated from UniProtKB/Swiss-Prot (P22557.2)"
                     /calculated_mol_wt=59508
     Region          143..548
                     /region_name="5aminolev_synth"
                     /note="5-aminolevulinic acid synthase; TIGR01821"
                     /db_xref="CDD:273820"
     Site            order(197,257..259,285,328,332..333,357,359..360,388,391,
                     517)
                     /site_type="active"
                     /note="substrate-cofactor binding pocket [active]"
                     /db_xref="CDD:99747"
     Site            order(257..259,285,328,332,357,359..360,388,391)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99747"
     Site            391
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99747"
     CDS             1..587
                     /gene="ALAS2"
                     /gene_synonym="ALAS-E; ALASE; ANH1; ASB; SIDBA1; XLDPP;
                     XLEPP; XLSA"
                     /coded_by="NM_000032.5:52..1815"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS14366.1"
                     /db_xref="GeneID:212"
                     /db_xref="HGNC:HGNC:397"
                     /db_xref="MIM:301300"
ORIGIN      
        1 mvtaamllqc cpvlargpts llgkvvkthq flfgigrcpi latqgpncsq ihlkatkagg
       61 dspswakghc pfmlselqdg kskivqkaap evqedvkafk tdlpsslvsv slrkpfsgpq
      121 eqeqisgkvt hliqnnmpgn yvfsydqffr dkimekkqdh tyrvfktvnr wadaypfaqh
      181 fseasvaskd vsvwcsndyl gmsrhpqvlq atqetlqrhg agaggtrnis gtskfhvele
      241 qelaelhqkd sallfsscfv andstlftla kilpgceiys dagnhasmiq girnsgaakf
      301 vfrhndpdhl kklleksnpk ipkivafetv hsmdgaicpl eelcdvshqy galtfvdevh
      361 avglygsrga gigerdgimh kidiisgtlg kafgcvggyi astrdlvdmv rsyaagfift
      421 tslppmvlsg alesvrllkg eegqalrrah qrnvkhmrql lmdrglpvip cpshiipirv
      481 gnaalnsklc dlllskhgiy vqainyptvp rgeellrlap sphhspqmme dfveklllaw
      541 tavglplqdv svaacnfcrr pvhfelmsew ersyfgnmgp qyvttya
//
LOCUS       NP_005708                151 aa            linear   PRI 27-APR-2025
DEFINITION  actin-related protein 2/3 complex subunit 5 isoform 1 [Homo
            sapiens].
ACCESSION   NP_005708
VERSION     NP_005708.1
DBSOURCE    REFSEQ: accession NM_005717.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Gao,Y., Hou,J., Fei,X., Ren,L., Lu,R., Liu,P., Liu,S., Zhu,C.,
            Wang,X. and Pan,Y.
  TITLE     TAGLN2 targeted control of ARPC5-mediated activation of the MEK/ERK
            signaling pathway influences the proliferation, invasion, and
            metastasis of pancreatic cancer cells
  JOURNAL   Cell Signal 120, 111227 (2024)
   PUBMED   38744388
  REMARK    GeneRIF: TAGLN2 targeted control of ARPC5-mediated activation of
            the MEK/ERK signaling pathway influences the proliferation,
            invasion, and metastasis of pancreatic cancer cells.
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Ming,Y., Luo,C., Ji,B. and Cheng,J.
  TITLE     ARPC5 acts as a potential prognostic biomarker that is associated
            with cell proliferation, migration and immune infiltrate in gliomas
  JOURNAL   BMC Cancer 23 (1), 937 (2023)
   PUBMED   37789267
  REMARK    GeneRIF: ARPC5 acts as a potential prognostic biomarker that is
            associated with cell proliferation, migration and immune infiltrate
            in gliomas.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Sindram,E., Caballero-Oteyza,A., Kogata,N., Chor Mei Huang,S.,
            Alizadeh,Z., Gamez-Diaz,L., Fazlollhi,M.R., Peng,X., Grimbacher,B.,
            Way,M. and Proietti,M.
  TITLE     ARPC5 deficiency leads to severe early-onset systemic inflammation
            and mortality
  JOURNAL   Dis Model Mech 16 (7) (2023)
   PUBMED   37382373
  REMARK    GeneRIF: ARPC5 deficiency leads to severe early-onset systemic
            inflammation and mortality.
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Nunes-Santos,C.J., Kuehn,H., Boast,B., Hwang,S., Kuhns,D.B.,
            Stoddard,J., Niemela,J.E., Fink,D.L., Pittaluga,S., Abu-Asab,M.,
            Davies,J.S., Barr,V.A., Kawai,T., Delmonte,O.M., Bosticardo,M.,
            Garofalo,M., Carneiro-Sampaio,M., Somech,R., Gharagozlou,M.,
            Parvaneh,N., Samelson,L.E., Fleisher,T.A., Puel,A.,
            Notarangelo,L.D., Boisson,B., Casanova,J.L., Derfalvi,B. and
            Rosenzweig,S.D.
  TITLE     Inherited ARPC5 mutations cause an actinopathy impairing cell
            motility and disrupting cytokine signaling
  JOURNAL   Nat Commun 14 (1), 3708 (2023)
   PUBMED   37349293
  REMARK    GeneRIF: Inherited ARPC5 mutations cause an actinopathy impairing
            cell motility and disrupting cytokine signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Sadhu,L., Tsopoulidis,N., Hasanuzzaman,M., Laketa,V., Way,M. and
            Fackler,O.T.
  TITLE     ARPC5 isoforms and their regulation by calcium-calmodulin-N-WASP
            drive distinct Arp2/3-dependent actin remodeling events in CD4 T
            cells
  JOURNAL   Elife 12, e82450 (2023)
   PUBMED   37162507
  REMARK    GeneRIF: ARPC5 isoforms and their regulation by
            calcium-calmodulin-N-WASP drive distinct Arp2/3-dependent actin
            remodeling events in CD4 T cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 151)
  AUTHORS   Robinson,R.C., Turbedsky,K., Kaiser,D.A., Marchand,J.B.,
            Higgs,H.N., Choe,S. and Pollard,T.D.
  TITLE     Crystal structure of Arp2/3 complex
  JOURNAL   Science 294 (5547), 1679-1684 (2001)
   PUBMED   11721045
REFERENCE   7  (residues 1 to 151)
  AUTHORS   Gournier,H., Goley,E.D., Niederstrasser,H., Trinh,T. and Welch,M.D.
  TITLE     Reconstitution of human Arp2/3 complex reveals critical roles of
            individual subunits in complex structure and activity
  JOURNAL   Mol Cell 8 (5), 1041-1052 (2001)
   PUBMED   11741539
REFERENCE   8  (residues 1 to 151)
  AUTHORS   Zhao,X., Yang,Z., Qian,M. and Zhu,X.
  TITLE     Interactions among subunits of human Arp2/3 complex: p20-Arc as the
            hub
  JOURNAL   Biochem Biophys Res Commun 280 (2), 513-517 (2001)
   PUBMED   11162547
REFERENCE   9  (residues 1 to 151)
  AUTHORS   Machesky,L.M., Reeves,E., Wientjes,F., Mattheyse,F.J., Grogan,A.,
            Totty,N.F., Burlingame,A.L., Hsuan,J.J. and Segal,A.W.
  TITLE     Mammalian actin-related protein 2/3 complex localizes to regions of
            lamellipodial protrusion and is composed of evolutionarily
            conserved proteins
  JOURNAL   Biochem J 328 (Pt 1) (Pt 1), 105-112 (1997)
   PUBMED   9359840
REFERENCE   10 (residues 1 to 151)
  AUTHORS   Welch,M.D., DePace,A.H., Verma,S., Iwamatsu,A. and Mitchison,T.J.
  TITLE     The human Arp2/3 complex is composed of evolutionarily conserved
            subunits and is localized to cellular regions of dynamic actin
            filament assembly
  JOURNAL   J Cell Biol 138 (2), 375-384 (1997)
   PUBMED   9230079
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN291383.1, AL137800.12,
            AF006088.1 and AI148784.1.
            
            Summary: This gene encodes one of seven subunits of the human
            Arp2/3 protein complex. The Arp2/3 protein complex has been
            implicated in the control of actin polymerization in cells and has
            been conserved through evolution. The exact role of the protein
            encoded by this gene, the p16 subunit, has yet to be determined.
            Alternatively spliced transcript variants encoding different
            isoforms have been observed for this gene. [provided by RefSeq, Jul
            2012].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the shorter protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF006088.1, AK129598.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359856.11/ ENSP00000352918.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.3"
     Protein         1..151
                     /product="actin-related protein 2/3 complex subunit 5
                     isoform 1"
                     /note="Arp2/3 protein complex subunit p16; arp2/3 complex
                     16 kDa subunit; actin related protein 2/3 complex, subunit
                     5, 16kDa"
                     /calculated_mol_wt=16189
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O15511.3)"
     Region          10..149
                     /region_name="P16-Arc"
                     /note="ARP2/3 complex 16 kDa subunit (p16-Arc); pfam04699"
                     /db_xref="CDD:461399"
     Region          21..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15511.3)"
     CDS             1..151
                     /gene="ARPC5"
                     /gene_synonym="ARC16; dJ127C7.3; IMD113; p16-Arc"
                     /coded_by="NM_005717.4:125..580"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1357.1"
                     /db_xref="GeneID:10092"
                     /db_xref="HGNC:HGNC:708"
                     /db_xref="MIM:604227"
ORIGIN      
        1 mskntvssar frkvdvdeyd enkfvdeedg gdgqagpdeg evdsclrqgn mtaalqaalk
       61 nppintksqa vkdragsivl kvlisfkand iekavqsldk ngvdllmkyi ykgfespsdn
      121 ssamllqwhe kalaaggvgs ivrvltarkt v
//
LOCUS       NP_443131               1008 aa            linear   PRI 27-APR-2025
DEFINITION  G protein-regulated inducer of neurite outgrowth 1 [Homo sapiens].
ACCESSION   NP_443131
VERSION     NP_443131.2
DBSOURCE    REFSEQ: accession NM_052899.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Zhou,Q., Li,D., Zheng,H., He,Z., Qian,F., Wu,X., Yin,Z., Bao,P.T.
            and Jin,M.
  TITLE     A novel lncRNA-miRNA-mRNA competing endogenous RNA regulatory
            network in lung adenocarcinoma and kidney renal papillary cell
            carcinoma
  JOURNAL   Thorac Cancer 12 (19), 2526-2536 (2021)
   PUBMED   34453499
  REMARK    GeneRIF: A novel lncRNA-miRNA-mRNA competing endogenous RNA
            regulatory network in lung adenocarcinoma and kidney renal
            papillary cell carcinoma.
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Nordman,J.C., Phillips,W.S., Kodama,N., Clark,S.G., Del Negro,C.A.
            and Kabbani,N.
  TITLE     Axon targeting of the alpha 7 nicotinic receptor in developing
            hippocampal neurons by Gprin1 regulates growth
  JOURNAL   J Neurochem 129 (4), 649-662 (2014)
   PUBMED   24350810
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   4  (residues 1 to 1008)
  AUTHORS   Iida,N. and Kozasa,T.
  TITLE     Identification and biochemical analysis of GRIN1 and GRIN2
  JOURNAL   Methods Enzymol 390, 475-483 (2004)
   PUBMED   15488195
REFERENCE   5  (residues 1 to 1008)
  AUTHORS   Chen,L.T., Gilman,A.G. and Kozasa,T.
  TITLE     A candidate target for G protein action in brain
  JOURNAL   J Biol Chem 274 (38), 26931-26938 (1999)
   PUBMED   10480904
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091934.2.
            
            On Aug 22, 2006 this sequence version replaced NP_443131.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052950.1, SRR1163655.661507.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303991.5/ ENSP00000305839.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..1008
                     /product="G protein-regulated inducer of neurite outgrowth
                     1"
                     /calculated_mol_wt=102269
     Region          1..859
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UNH4; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Region          <466..738
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            615
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            737
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UNH4; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Region          873..1005
                     /region_name="GRIN_C"
                     /note="G protein-regulated inducer of neurite outgrowth
                     C-terminus; pfam15235"
                     /db_xref="CDD:464577"
     Site            877
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UNH4; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            895
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UNH4; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Region          899..1008
                     /region_name="Interaction with GNAO1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UNH4; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Region          943..986
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     Site            993
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2K8.2)"
     CDS             1..1008
                     /gene="GPRIN1"
                     /gene_synonym="GRIN1"
                     /coded_by="NM_052899.3:202..3228"
                     /db_xref="CCDS:CCDS4405.1"
                     /db_xref="GeneID:114787"
                     /db_xref="HGNC:HGNC:24835"
                     /db_xref="MIM:611239"
ORIGIN      
        1 mdtaedpawl qllqkdsspp gprptaffcp qdgslgagss amrdycpsqq kaspapprht
       61 pdqspgmesr hrspsgageg ascsdgprgs lacpsptcfs pqespsketl eahgasisgt
      121 peattsgkpe pvssvktepk ssddrnpmfl ekmdfksskq adstsigked pgssrkadpm
      181 ftgkaepeil gkgdpvapgr mdpmtvrked lgslgkvdpl cssktytvsp rkedpgslrk
      241 vdpvssdkvd pvfprkeepr ysgkehpvss ekvaptsaek vdlvlsgkrd pgpsgkadpm
      301 plesmdsast gktepgllgk lipgssgkng pvssgtgapg slgrldptcl gmadpasvgn
      361 vetvpatked srflgkmdpa ssgegrpvsg htdttasakt dltslknvdp mssgkvdpvs
      421 lgkmdpmcsg kpellspgqa ervsvgkagt vspgkedpvs srredpisag srktssekvn
      481 pessgktnpv ssgpgdprsl gtagppsavk aepatggkgd plssekaglv asgkaaptas
      541 gkaeplavgk edpvskgkad agpsgqgdsv sigkvvstpg ktvpvpsgkv dpvslgkaea
      601 ipegkvgslp lekgspvttt kadprasgka qpqsggkaet klpgqegaaa pgeagavclk
      661 ketpqasekv dpgscrkaep lasgkgepvs lgkadsapsr ktespslgkv vplslektkp
      721 ssssrqldrk algsarspeg argsegrvep kaepvsstea sslgqkdlea agaerspcpe
      781 aaapppgprt rdnftkapsw easappppre dagtqagaqa cvsvavspms pqdgaggsaf
      841 sfqaapraps ppsrrdaglq vslgaaetrs vatgpmtpqa aappafpevr vrpgsalaaa
      901 vappepaepv rdvswdekgm twevygaame vevlgmaiqk hlerqieehg rqgapapppa
      961 aragpgrsgs vrtappdgaa krppglfral lqsvrrprcc sragptae
//
LOCUS       NP_000246                750 aa            linear   PRI 27-APR-2025
DEFINITION  methylmalonyl-CoA mutase, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_000246
VERSION     NP_000246.2
DBSOURCE    REFSEQ: accession NM_000255.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Guo,Y., Zhu,X., Song,L., Wang,Y., Gao,J., Yuan,E., Yu,H., Fang,Y.,
            Shi,Q., Zhao,D. and Zhang,L.
  TITLE     Genetic analysis of isolated methylmalonic acidemia in Henan,
            China: c.1663G>A variant of MMUT prevalent in the Henan population
  JOURNAL   Clin Chim Acta 553, 117729 (2024)
   PUBMED   38128819
  REMARK    GeneRIF: Genetic analysis of isolated methylmalonic acidemia in
            Henan, China: c.1663G>A variant of MMUT prevalent in the Henan
            population.
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Ramon,C., Traversi,F., Burer,C., Froese,D.S. and Stelling,J.
  TITLE     Cellular and computational models reveal environmental and
            metabolic interactions in MMUT-type methylmalonic aciduria
  JOURNAL   J Inherit Metab Dis 46 (3), 421-435 (2023)
   PUBMED   36371683
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Yu,Y., Shuai,R., Liang,L., Qiu,W., Shen,L., Wu,S., Wei,H., Chen,Y.,
            Yang,C., Xu,P., Chen,X., Zou,H., Feng,J., Niu,T., Hu,H., Ye,J.,
            Zhang,H., Lu,D., Gong,Z., Zhan,X., Ji,W., Gu,X. and Han,L.
  TITLE     Different mutations in the MMUT gene are associated with the effect
            of vitamin B12 in a cohort of 266 Chinese patients with mut-type
            methylmalonic acidemia: A retrospective study
  JOURNAL   Mol Genet Genomic Med 9 (11), e1822 (2021)
   PUBMED   34668645
  REMARK    GeneRIF: Different mutations in the MMUT gene are associated with
            the effect of vitamin B12 in a cohort of 266 Chinese patients with
            mut-type methylmalonic acidemia: A retrospective study.
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Manoli,I., Sloan,J.L. and Venditti,C.P.
  TITLE     Isolated Methylmalonic Acidemia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301409
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Crane,A.M., Martin,L.S., Valle,D. and Ledley,F.D.
  TITLE     Phenotype of disease in three patients with identical mutations in
            methylmalonyl CoA mutase
  JOURNAL   Hum Genet 89 (3), 259-264 (1992)
   PUBMED   1351030
REFERENCE   8  (residues 1 to 750)
  AUTHORS   Crane,A.M., Jansen,R., Andrews,E.R. and Ledley,F.D.
  TITLE     Cloning and expression of a mutant methylmalonyl coenzyme A mutase
            with altered cobalamin affinity that causes mut- methylmalonic
            aciduria
  JOURNAL   J Clin Invest 89 (2), 385-391 (1992)
   PUBMED   1346616
REFERENCE   9  (residues 1 to 750)
  AUTHORS   Raff,M.L., Crane,A.M., Jansen,R., Ledley,F.D. and Rosenblatt,D.S.
  TITLE     Genetic characterization of a MUT locus mutation discriminating
            heterogeneity in mut0 and mut- methylmalonic aciduria by
            interallelic complementation
  JOURNAL   J Clin Invest 87 (1), 203-207 (1991)
   PUBMED   1670635
REFERENCE   10 (residues 1 to 750)
  AUTHORS   Frenkel,E.P. and Kitchens,R.L.
  TITLE     Intracellular localization of hepatic propionyl-CoA carboxylase and
            methylmalonyl-CoA mutase in humans and normal and vitamin B12
            deficient rats
  JOURNAL   Br J Haematol 31 (4), 501-513 (1975)
   PUBMED   24458
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292568.1, AK312611.1 and
            AL590668.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 17, 2007 this sequence version replaced NP_000246.1.
            
            Summary: This gene encodes the mitochondrial enzyme methylmalonyl
            Coenzyme A mutase. In humans, the product of this gene is a vitamin
            B12-dependent enzyme which catalyzes the isomerization of
            methylmalonyl-CoA to succinyl-CoA, while in other species this
            enzyme may have different functions. Mutations in this gene may
            lead to various types of methylmalonic aciduria. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: MF170186.1, MF170185.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000274813.4/
                                                  ENSP00000274813.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.3"
     Protein         1..750
                     /product="methylmalonyl-CoA mutase, mitochondrial
                     precursor"
                     /EC_number="5.4.99.2"
                     /note="methylmalonyl Coenzyme A mutase; mutant
                     methylmalonyl CoA mutase; methylmalonyl-CoA mutase,
                     mitochondrial; methylmalonyl-CoA isomerase;
                     methylmalonyl-CoA mutase variant c.613_615delGAA;
                     methylmalonyl-CoA mutase c.*192delA; methylmalonyl-CoA
                     mutase variant c.322C>T; methylmalonyl-CoA mutase variant
                     c.636G>A; methylmalonyl-CoA mutase variant c.643G>A;
                     methylmalonyl-CoA mutase variant c.1495G>A;
                     methylmalonyl-CoA mutase variant c.2011A>G;
                     methylmalonyl-CoA mutase variant c.2150G>T;
                     methylmalonyl-CoA mutase c.*51C>G"
                     /calculated_mol_wt=79341
     transit_peptide 1..32
                     /calculated_mol_wt=3812
     mat_peptide     33..750
                     /product="methylmalonyl-CoA mutase, mitochondrial"
                     /calculated_mol_wt=79341
     Region          41..744
                     /region_name="PRK09426"
                     /note="methylmalonyl-CoA mutase; Reviewed"
                     /db_xref="CDD:236508"
     Site            89
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P16332; propagated from
                     UniProtKB/Swiss-Prot (P22033.4)"
     Site            212
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P16332; propagated from
                     UniProtKB/Swiss-Prot (P22033.4)"
     Site            335
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P16332; propagated from
                     UniProtKB/Swiss-Prot (P22033.4)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22033.4)"
     Site            602
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P16332; propagated from
                     UniProtKB/Swiss-Prot (P22033.4)"
     CDS             1..750
                     /gene="MMUT"
                     /gene_synonym="MCM; MUT"
                     /coded_by="NM_000255.4:191..2443"
                     /db_xref="CCDS:CCDS4924.1"
                     /db_xref="GeneID:4594"
                     /db_xref="HGNC:HGNC:7526"
                     /db_xref="MIM:609058"
ORIGIN      
        1 mlraknqlfl lsphylrqvk essgsrliqq rllhqqqplh pewaalakkq lkgknpedli
       61 whtpegisik plyskrdtmd lpeelpgvkp ftrgpyptmy tfrpwtirqy agfstveesn
      121 kfykdnikag qqglsvafdl athrgydsdn prvrgdvgma gvaidtvedt kilfdgiple
      181 kmsvsmtmng avipvlanfi vtgeeqgvpk ekltgtiqnd ilkefmvrnt yifppepsmk
      241 iiadifeyta khmpkfnsis isgyhmqeag adailelayt ladgleysrt glqagltide
      301 faprlsffwg igmnfymeia kmragrrlwa hliekmfqpk nskslllrah cqtsgwslte
      361 qdpynnivrt aieamaavfg gtqslhtnsf dealglptvk sariarntqi iiqeesgipk
      421 vadpwggsym mecltndvyd aalklineie emggmakava egipklriee caarrqarid
      481 sgsevivgvn kyqlekedav evlaidntsv rnrqieklkk ikssrdqala erclaaltec
      541 aasgdgnila lavdasrarc tvgeitdalk kvfgehkand rmvsgayrqe fgeskeitsa
      601 ikrvhkfmer egrrprllva kmgqdghdrg akviatgfad lgfdvdigpl fqtprevaqq
      661 avdadvhavg istlaaghkt lvpelikeln slgrpdilvm cggvippqdy eflfevgvsn
      721 vfgpgtripk aavqvlddie kclekkqqsv
//
LOCUS       NP_064448                327 aa            linear   PRI 27-APR-2025
DEFINITION  barH-like 1 homeobox protein [Homo sapiens].
ACCESSION   NP_064448
VERSION     NP_064448.1
DBSOURCE    REFSEQ: accession NM_020064.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Gu,Y., Chen,G. and Ning,X.
  TITLE     Homeobox Protein BarH-like 1 Promotes Gastric Cancer Progression by
            Activating Coiled-Coil Domain-Containing Protein 178
  JOURNAL   Dig Dis Sci 69 (4), 1182-1199 (2024)
   PUBMED   38358459
  REMARK    GeneRIF: Homeobox Protein BarH-like 1 Promotes Gastric Cancer
            Progression by Activating Coiled-Coil Domain-Containing Protein
            178.
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Barh,D., Garcia-Solano,M.E., Tiwari,S., Bhattacharya,A., Jain,N.,
            Torres-Moreno,D., Ferri,B., Silva,A., Azevedo,V., Ghosh,P.,
            Blum,K., Conesa-Zamora,P. and Perry,G.
  TITLE     BARHL1 Is Downregulated in Alzheimer's Disease and May Regulate
            Cognitive Functions through ESR1 and Multiple Pathways
  JOURNAL   Genes (Basel) 8 (10), 245 (2017)
   PUBMED   28956815
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Poschl,J., Lorenz,A., Hartmann,W., von Bueren,A.O., Kool,M., Li,S.,
            Peraud,A., Tonn,J.C., Herms,J., Xiang,M., Rutkowski,S.,
            Kretzschmar,H.A. and Schuller,U.
  TITLE     Expression of BARHL1 in medulloblastoma is associated with
            prolonged survival in mice and humans
  JOURNAL   Oncogene 30 (47), 4721-4730 (2011)
   PUBMED   21602885
  REMARK    GeneRIF: expression of Barhl1 decelerates tumor growth both in
            human and in murine medulloblastomas.
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Bulfone,A., Menguzzato,E., Broccoli,V., Marchitiello,A.,
            Gattuso,C., Mariani,M., Consalez,G.G., Martinez,S., Ballabio,A. and
            Banfi,S.
  TITLE     Barhl1, a gene belonging to a new subfamily of mammalian homeobox
            genes, is expressed in migrating neurons of the CNS
  JOURNAL   Hum Mol Genet 9 (9), 1443-1452 (2000)
   PUBMED   10814725
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK054797.1 and AF325688.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK054797.1, AF325688.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263610.7/ ENSP00000263610.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..327
                     /product="barH-like 1 homeobox protein"
                     /calculated_mol_wt=34943
     Region          1..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZE3.1)"
     Region          112..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZE3.1)"
     Region          179..235
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          305..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZE3.1)"
     CDS             1..327
                     /gene="BARHL1"
                     /coded_by="NM_020064.4:193..1176"
                     /db_xref="CCDS:CCDS6950.1"
                     /db_xref="GeneID:56751"
                     /db_xref="HGNC:HGNC:953"
                     /db_xref="MIM:605211"
ORIGIN      
        1 megsngfgid silshragsp alpkgdpllg dcrsplelsp rsesssdcss paspgrdcle
       61 tgtprpggas gpgldshlqp gqlsapaqsr tvtssflird iladckplaa capysssgqp
      121 aapepggrla akaaedfrdk ldksgsnass dseykvkeeg dreisssrds ppvrlkkprk
      181 artaftdhql aqlersferq kylsvqdrme laaslnltdt qvktwyqnrr tkwkrqtavg
      241 lellaeagny salqrmfpsp yfypqslvsn ldpgaalyly rgpsapppal qrplvprili
      301 hglqgasepp pplpplagvl praaqpr
//
LOCUS       NP_057173                364 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 589 [Homo sapiens].
ACCESSION   NP_057173
VERSION     NP_057173.2
DBSOURCE    REFSEQ: accession NM_016089.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Burton,E.M., Akinyemi,I.A., Frey,T.R., Xu,H., Li,X., Su,L.J.,
            Zhi,J., McIntosh,M.T. and Bhaduri-McIntosh,S.
  TITLE     A heterochromatin inducing protein differentially recognizes self
            versus foreign genomes
  JOURNAL   PLoS Pathog 17 (3), e1009447 (2021)
   PUBMED   33730092
  REMARK    GeneRIF: A heterochromatin inducing protein differentially
            recognizes self versus foreign genomes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Venturini,L., Stadler,M., Manukjan,G., Scherr,M.,
            Schlegelberger,B., Steinemann,D. and Ganser,A.
  TITLE     The stem cell zinc finger 1 (SZF1)/ZNF589 protein has a
            human-specific evolutionary nucleotide DNA change and acts as a
            regulator of cell viability in the hematopoietic system
  JOURNAL   Exp Hematol 44 (4), 257-268 (2016)
   PUBMED   26738774
  REMARK    GeneRIF: The stem cell zinc finger 1 (SZF1)/ZNF589 protein has a
            human-specific evolutionary nucleotide DNA change and acts as a
            regulator of cell viability in the hematopoietic system
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Wang,W., Cai,J., Wu,Y., Hu,L., Chen,Z., Hu,J., Chen,Z., Li,W.,
            Guo,M. and Huang,Z.
  TITLE     Novel activity of KRAB domain that functions to reinforce nuclear
            localization of KRAB-containing zinc finger proteins by interacting
            with KAP1
  JOURNAL   Cell Mol Life Sci 70 (20), 3947-3958 (2013)
   PUBMED   23665872
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Peng,H., Zheng,L., Lee,W.H., Rux,J.J. and Rauscher,F.J. 3rd.
  TITLE     A common DNA-binding site for SZF1 and the BRCA1-associated zinc
            finger protein, ZBRK1
  JOURNAL   Cancer Res 62 (13), 3773-3781 (2002)
   PUBMED   12097288
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Liu,C., Levenstein,M., Chen,J., Tsifrina,E., Yonescu,R.,
            Griffin,C., Civin,C.I. and Small,D.
  TITLE     SZF1: a novel KRAB-zinc finger gene expressed in CD34+
            stem/progenitor cells
  JOURNAL   Exp Hematol 27 (2), 313-325 (1999)
   PUBMED   10029171
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104190.3 and AY258146.1.
            
            On Jun 1, 2007 this sequence version replaced NP_057173.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY258146.1, SRR1660803.111045.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354698.8/ ENSP00000346729.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..364
                     /product="zinc finger protein 589"
                     /note="KRAB-zinc finger protein SZF1-1; stem cell zinc
                     finger protein 1"
                     /calculated_mol_wt=41058
     Region          34..74
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          103..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UQ0.1)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q86UQ0.1)"
     Region          223..>311
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          249..270
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          250..270
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(255,257,259,261..262,265..266,269,283,285,289..290,
                     293..294,297,311,313,315,317..318,321..322,325)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          278..298
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          302..>364
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          306..326
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          334..354
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..364
                     /gene="ZNF589"
                     /gene_synonym="SZF1"
                     /coded_by="NM_016089.3:69..1163"
                     /db_xref="CCDS:CCDS43085.1"
                     /db_xref="GeneID:51385"
                     /db_xref="HGNC:HGNC:16747"
                     /db_xref="MIM:616702"
ORIGIN      
        1 mwapreqllg wtaealpakd sawpweekpr ylgpvtfedv avlfteaewk rlsleqrnly
       61 kevmlenlrn lvslaeskpe vhtcpscpla fgsqqflsqd elhnhpipgf hagnqlhpgn
      121 pcpedqpqsq hpsdknhrga eaedqrvegg vrplfwstne rgalvgfssl fqrppisswg
      181 gnrileiqls paqnasseev driskraetp gfgavtfgec alafnqksnl frqkavtaek
      241 ssdkrqsqvc recgrgfsrk sqliihqrth tgekpyvcge cgrgfivesv lrnhlsthsg
      301 ekpyvcshcg rgfsckpyli rhqrthtrek sfmctvcgrg frekselikh qrihtgdkpy
      361 vcrd
//
LOCUS       NP_055139                382 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-methylacyl-CoA racemase isoform 1 [Homo sapiens].
ACCESSION   NP_055139
VERSION     NP_055139.4
DBSOURCE    REFSEQ: accession NM_014324.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Rotterova,P., Alaghehbandan,R., Skopal,J., Rogala,J.,
            Slisarenko,M., Strakova Peterikova,A., Michalova,K., Montiel,D.P.,
            Farcas,M., Ulamec,M., Stransky,P. Jr., Fiala,O., Pitra,T., Hora,M.,
            Michal,M., Pivovarcikova,K. and Hes,O.
  TITLE     Alpha-methyl CoA racemase (AMACR) reactivity across the spectrum of
            clear cell renal cell neoplasms
  JOURNAL   Ann Diagn Pathol 71, 152297 (2024)
   PUBMED   38579443
  REMARK    GeneRIF: Alpha-methyl CoA racemase (AMACR) reactivity across the
            spectrum of clear cell renal cell neoplasms.
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Lerner,G., Tang,H., Singh,K., Golestani,R., St Claire,S.,
            Humphrey,P.A., Lannin,D., Janostiak,R. and Harigopal,M.
  TITLE     AMACR Expression is a Potential Diagnostic Marker in Apocrine
            Lesions of Breast, and is Associated with High Histologic Grade and
            Lymph Node Metastases in Some Invasive Apocrine Breast Cancers
  JOURNAL   Clin Breast Cancer 23 (2), 199-210 (2023)
   PUBMED   36577560
  REMARK    GeneRIF: AMACR Expression is a Potential Diagnostic Marker in
            Apocrine Lesions of Breast, and is Associated with High Histologic
            Grade and Lymph Node Metastases in Some Invasive Apocrine Breast
            Cancers.
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Chen,W., Wu,W., Zhao,J., Yu,C., Liu,W., Jiang,A. and Zhang,J.
  TITLE     Molecular cloning and preliminary analysis of the human
            alpha-methylacyl-CoA racemase promoter
  JOURNAL   Mol Biol Rep 36 (3), 423-430 (2009)
   PUBMED   18080842
  REMARK    GeneRIF: promoter function of AMACR is independent of androgen
            receptor-mediated signaling
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Mubiru,J.N., Shen-Ong,G.L., Valente,A.J. and Troyer,D.A.
  TITLE     Alternative spliced variants of the alpha-methylacyl-CoA racemase
            gene and their expression in prostate cancer
  JOURNAL   Gene 327 (1), 89-98 (2004)
   PUBMED   14960364
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Rubin,M.A., Zhou,M., Dhanasekaran,S.M., Varambally,S.,
            Barrette,T.R., Sanda,M.G., Pienta,K.J., Ghosh,D. and
            Chinnaiyan,A.M.
  TITLE     alpha-Methylacyl coenzyme A racemase as a tissue biomarker for
            prostate cancer
  JOURNAL   JAMA 287 (13), 1662-1670 (2002)
   PUBMED   11926890
  REMARK    GeneRIF: AMACR was shown to be overexpressed in prostate cancer
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Ferdinandusse,S., Denis,S., IJlst,L., Dacremont,G., Waterham,H.R.
            and Wanders,R.J.
  TITLE     Subcellular localization and physiological role of
            alpha-methylacyl-CoA racemase
  JOURNAL   J Lipid Res 41 (11), 1890-1896 (2000)
   PUBMED   11060359
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Amery,L., Fransen,M., De Nys,K., Mannaerts,G.P. and Van
            Veldhoven,P.P.
  TITLE     Mitochondrial and peroxisomal targeting of 2-methylacyl-CoA
            racemase in humans
  JOURNAL   J Lipid Res 41 (11), 1752-1759 (2000)
   PUBMED   11060344
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Ferdinandusse,S., Denis,S., Clayton,P.T., Graham,A., Rees,J.E.,
            Allen,J.T., McLean,B.N., Brown,A.Y., Vreken,P., Waterham,H.R. and
            Wanders,R.J.
  TITLE     Mutations in the gene encoding peroxisomal alpha-methylacyl-CoA
            racemase cause adult-onset sensory motor neuropathy
  JOURNAL   Nat Genet 24 (2), 188-191 (2000)
   PUBMED   10655068
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Schmitz,W., Albers,C., Fingerhut,R. and Conzelmann,E.
  TITLE     Purification and characterization of an alpha-methylacyl-CoA
            racemase from human liver
  JOURNAL   Eur J Biochem 231 (3), 815-822 (1995)
   PUBMED   7649182
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139783.3 and AA969512.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 25, 2004 this sequence version replaced NP_055139.3.
            
            Summary: This gene encodes a racemase. The encoded enzyme
            interconverts pristanoyl-CoA and C27-bile acylCoAs between their
            (R)- and (S)-stereoisomers. The conversion to the (S)-stereoisomers
            is necessary for degradation of these substrates by peroxisomal
            beta-oxidation. Encoded proteins from this locus localize to both
            mitochondria and peroxisomes. Mutations in this gene may be
            associated with adult-onset sensorimotor neuropathy, pigmentary
            retinopathy, and adrenomyeloneuropathy due to defects in bile acid
            synthesis. Alternatively spliced transcript variants have been
            described. Read-through transcription also exists between this gene
            and the upstream neighboring C1QTNF3 (C1q and tumor necrosis factor
            related protein 3) gene. [provided by RefSeq, Mar 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform 1, also referred to as AMACR IA.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.198374.1,
                                           SRR1803616.183681.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 11060344; reported by
                                                  MitoCarta
            MANE Ensembl match                 :: ENST00000335606.11/
                                                  ENSP00000334424.6
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..382
                     /product="alpha-methylacyl-CoA racemase isoform 1"
                     /EC_number="5.1.99.4"
                     /note="2-methylacyl-CoA racemase"
                     /calculated_mol_wt=42256
     Region          1..373
                     /region_name="CaiB"
                     /note="Crotonobetainyl-CoA:carnitine CoA-transferase CaiB
                     and related acyl-CoA transferases [Lipid transport and
                     metabolism]; COG1804"
                     /db_xref="CDD:441409"
     Site            58
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O09174; propagated from
                     UniProtKB/Swiss-Prot (Q9UHK6.2)"
     Site            87
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O09174; propagated from
                     UniProtKB/Swiss-Prot (Q9UHK6.2)"
     Region          380..382
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000269|PubMed:11060344"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHK6.2)"
     CDS             1..382
                     /gene="AMACR"
                     /gene_synonym="AMACRD; CBAS4; P504S; RACE; RM"
                     /coded_by="NM_014324.6:32..1180"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3902.1"
                     /db_xref="GeneID:23600"
                     /db_xref="HGNC:HGNC:451"
                     /db_xref="MIM:604489"
ORIGIN      
        1 malqgisvve lsglapgpfc amvladfgar vvrvdrpgsr ydvsrlgrgk rslvldlkqp
       61 rgaavlrrlc krsdvllepf rrgvmeklql gpeilqrenp rliyarlsgf gqsgsfcrla
      121 ghdinylals gvlskigrsg enpyaplnll adfaggglmc algiimalfd rtrtgkgqvi
      181 danmvegtay lssflwktqk lslweaprgq nmldggapfy ttyrtadgef mavgaiepqf
      241 yellikglgl ksdelpnqms mddwpemkkk fadvfaektk aewcqifdgt dacvtpvltf
      301 eevvhhdhnk ergsfitsee qdvsprpapl llntpaipsf krdpfigeht eeileefgfs
      361 reeiyqlnsd kiiesnkvka sl
//
LOCUS       NP_000110                721 aa            linear   PRI 27-APR-2025
DEFINITION  protein 4.2 isoform 1 [Homo sapiens].
ACCESSION   NP_000110
VERSION     NP_000110.2
DBSOURCE    REFSEQ: accession NM_000119.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Vallese,F., Kim,K., Yen,L.Y., Johnston,J.D., Noble,A.J., Cali,T.
            and Clarke,O.B.
  TITLE     Architecture of the human erythrocyte ankyrin-1 complex
  JOURNAL   Nat Struct Mol Biol 29 (7), 706-718 (2022)
   PUBMED   35835865
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Bustos,S.P. and Reithmeier,R.A.
  TITLE     Protein 4.2 interaction with hereditary spherocytosis mutants of
            the cytoplasmic domain of human anion exchanger 1
  JOURNAL   Biochem J 433 (2), 313-322 (2011)
   PUBMED   21039340
  REMARK    GeneRIF: study shows that cytoplasmic hereditary spherocytosis
            mutants cause impaired binding of protein 4.2 to AE1, leaving
            protein 4.2 susceptible to loss during erythrocyte development
REFERENCE   4  (residues 1 to 721)
  AUTHORS   Korsgren,C., Peters,L.L. and Lux,S.E.
  TITLE     Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid
            alpha-spectrin in a calcium- and calmodulin-dependent manner
  JOURNAL   J Biol Chem 285 (7), 4757-4770 (2010)
   PUBMED   20007969
  REMARK    GeneRIF: Data suggest that one or both of proteins 4.1 and 4.2
            cause a portion of band 3 to localize near the spectrin-actin
            junctions and provide another point of attachment between the
            membrane skeleton and the lipid bilayer.
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Satchwell,T.J., Shoemark,D.K., Sessions,R.B. and Toye,A.M.
  TITLE     Protein 4.2: a complex linker
  JOURNAL   Blood Cells Mol Dis 42 (3), 201-210 (2009)
   PUBMED   19269200
  REMARK    GeneRIF: Current understanding of protein 4.2, its known
            interactions & implications of protein 4.2 deficiency are reviewed.
            A new speculative 'open' homology structure for the the active,
            membrane associated form is proposed. Review.
            Review article
REFERENCE   6  (residues 1 to 721)
  AUTHORS   Kalfa,T.A. and Begtrup,A.H.
  TITLE     EPB42-Related Hereditary Spherocytosis
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24624460
REFERENCE   7  (residues 1 to 721)
  AUTHORS   White,R.A., Peters,L.L., Adkison,L.R., Korsgren,C., Cohen,C.M. and
            Lux,S.E.
  TITLE     The murine pallid mutation is a platelet storage pool disease
            associated with the protein 4.2 (pallidin) gene
  JOURNAL   Nat Genet 2 (1), 80-83 (1992)
   PUBMED   1284644
REFERENCE   8  (residues 1 to 721)
  AUTHORS   Sung,L.A., Chien,S., Fan,Y.S., Lin,C.C., Lambert,K., Zhu,L.,
            Lam,J.S. and Chang,L.S.
  TITLE     Human erythrocyte protein 4.2: isoform expression, differential
            splicing, and chromosomal assignment
  JOURNAL   Blood 79 (10), 2763-2770 (1992)
   PUBMED   1350227
REFERENCE   9  (residues 1 to 721)
  AUTHORS   Bouhassira,E.E., Schwartz,R.S., Yawata,Y., Ata,K., Kanzaki,A.,
            Qiu,J.J., Nagel,R.L. and Rybicki,A.C.
  TITLE     An alanine-to-threonine substitution in protein 4.2 cDNA is
            associated with a Japanese form of hereditary hemolytic anemia
            (protein 4.2NIPPON)
  JOURNAL   Blood 79 (7), 1846-1854 (1992)
   PUBMED   1558976
REFERENCE   10 (residues 1 to 721)
  AUTHORS   Risinger,M.A., Dotimas,E.M. and Cohen,C.M.
  TITLE     Human erythrocyte protein 4.2, a high copy number membrane protein,
            is N-myristylated
  JOURNAL   J Biol Chem 267 (8), 5680-5685 (1992)
   PUBMED   1544941
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Karyn Megy. The reference sequence was derived
            from DW451374.1, M60298.1, BC096093.4 and BU741892.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 31, 2008 this sequence version replaced NP_000110.1.
            
            Summary: Erythrocyte membrane protein band 4.2 is an ATP-binding
            protein which may regulate the association of protein 3 with
            ankyrin. It probably has a role in erythrocyte shape and mechanical
            property regulation. Mutations in the EPB42 gene are associated
            with recessive spherocytic elliptocytosis and recessively
            transmitted hereditary hemolytic anemia. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M30647.1, M60298.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2142680 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.2"
     Protein         1..721
                     /product="protein 4.2 isoform 1"
                     /note="erythrocyte surface protein band 4.2; P4.2;
                     erythrocyte protein 4.2"
                     /calculated_mol_wt=79797
     Region          38..154
                     /region_name="Transglut_N"
                     /note="Transglutaminase family; pfam00868"
                     /db_xref="CDD:459971"
     Region          291..382
                     /region_name="TGc"
                     /note="Transglutaminase/protease-like homologues;
                     smart00460"
                     /db_xref="CDD:214673"
     Region          505..610
                     /region_name="Transglut_C"
                     /note="Transglutaminase family, C-terminal ig like domain;
                     pfam00927"
                     /db_xref="CDD:460002"
     Region          618..716
                     /region_name="Transglut_C"
                     /note="Transglutaminase family, C-terminal ig like domain;
                     pfam00927"
                     /db_xref="CDD:460002"
     CDS             1..721
                     /gene="EPB42"
                     /gene_synonym="PA; SPH5"
                     /coded_by="NM_000119.3:194..2359"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10093.1"
                     /db_xref="GeneID:2038"
                     /db_xref="HGNC:HGNC:3381"
                     /db_xref="MIM:177070"
ORIGIN      
        1 mgqgepsqrs tglaglyaap aaspvfikgs gmdalgiksc dfqaarnnee hhtkalssrr
       61 lfvrrgqpft iilyfrapvr aflpalkkva ltaqtgeqps kinrtqatfp isslgdrkww
      121 savveerdaq swtisvttpa davighysll lqvsgrkqll lgqftllfnp wnredavflk
      181 neaqrmeyll nqngliylgt adciqaeswd fgqfegdvid lslrllskdk qvekwsqpvh
      241 varvlgallh flkeqrvlpt pqtqatqega llnkrrgsvp ilrqwltgrg rpvydgqawv
      301 laavactvlr clgiparvvt tfasaqgtgg rllideyyne eglqngegqr griwifqtst
      361 ecwmtrpalp qgydgwqilh psapngggvl gscdlvpvra vkegtlgltp avsdlfaain
      421 ascvvwkcce dgtleltdsn tkyvgnnist kgvgsdrced itqnykypeg slqekevler
      481 vekekmerek dngirppsle tasplylllk apsslplrgd aqisvtlvnh seqekavqla
      541 igvqavhyng vlaaklwrkk lhltlsanle kiitiglffs nfernppent flrltamath
      601 sesnlscfaq ediaicrphl aikmpekaeq yqpltasvsl qnsldapmed cvisilgrgl
      661 ihrersyrfr svwpentmca kfqftpthvg lqrltvevdc nmfqnltnyk svtvvapels
      721 a
//
LOCUS       NP_078822                726 aa            linear   PRI 27-APR-2025
DEFINITION  ORC ubiquitin ligase 1 [Homo sapiens].
ACCESSION   NP_078822
VERSION     NP_078822.3
DBSOURCE    REFSEQ: accession NM_024546.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Li,X.D., Zhong,Q.L., Luo,D.J., Liang,Q.F., Qiu,J.Q., Du,Q.H.,
            Xiao,L., Zhou,Y.H., Long,Y.B., Liu,W.Q. and Li,J.
  TITLE     RNF219 Promotes Nasopharyngeal Carcinoma Progression by Activating
            the NF-kappaB Pathway
  JOURNAL   Mol Biotechnol 65 (8), 1318-1326 (2023)
   PUBMED   36512252
  REMARK    GeneRIF: RNF219 Promotes Nasopharyngeal Carcinoma Progression by
            Activating the NF-kappaB Pathway.
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Poetz,F., Corbo,J., Levdansky,Y., Spiegelhalter,A., Lindner,D.,
            Magg,V., Lebedeva,S., Schweiggert,J., Schott,J., Valkov,E. and
            Stoecklin,G.
  TITLE     RNF219 attenuates global mRNA decay through inhibition of CCR4-NOT
            complex-mediated deadenylation
  JOURNAL   Nat Commun 12 (1), 7175 (2021)
   PUBMED   34887419
  REMARK    GeneRIF: RNF219 attenuates global mRNA decay through inhibition of
            CCR4-NOT complex-mediated deadenylation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Fu,G.H., Chen,W., Li,H.M., Wang,Y.F., Liu,L. and Qian,Q.J.
  TITLE     A potential association of RNF219-AS1 with ADHD: Evidence from
            categorical analysis of clinical phenotypes and from quantitative
            exploration of executive function and white matter microstructure
            endophenotypes
  JOURNAL   CNS Neurosci Ther 27 (5), 603-616 (2021)
   PUBMED   33644999
  REMARK    GeneRIF: A potential association of RNF219-AS1 with ADHD: Evidence
            from categorical analysis of clinical phenotypes and from
            quantitative exploration of executive function and white matter
            microstructure endophenotypes.
REFERENCE   4  (residues 1 to 726)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 726)
  AUTHORS   Coulombe,P., Nassar,J., Peiffer,I., Stanojcic,S., Sterkers,Y.,
            Delamarre,A., Bocquet,S. and Mechali,M.
  TITLE     The ORC ubiquitin ligase OBI1 promotes DNA replication origin
            firing
  JOURNAL   Nat Commun 10 (1), 2426 (2019)
   PUBMED   31160578
  REMARK    GeneRIF: RNF219 silencing result in defective replication origin
            firing, as shown by reduced CDC45/MCM2-7/GINS complex formation,
            without affecting pre-replicative complex establishment. RNF219
            catalyses the multi-mono-ubiquitylation of a subset of
            chromatin-bound ORC3 and ORC5 during S-phase.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 726)
  AUTHORS   Dichgans,M., Malik,R., Konig,I.R., Rosand,J., Clarke,R.,
            Gretarsdottir,S., Thorleifsson,G., Mitchell,B.D., Assimes,T.L.,
            Levi,C., O'Donnell,C.J., Fornage,M., Thorsteinsdottir,U.,
            Psaty,B.M., Hengstenberg,C., Seshadri,S., Erdmann,J., Bis,J.C.,
            Peters,A., Boncoraglio,G.B., Marz,W., Meschia,J.F., Kathiresan,S.,
            Ikram,M.A., McPherson,R., Stefansson,K., Sudlow,C., Reilly,M.P.,
            Thompson,J.R., Sharma,P., Hopewell,J.C., Chambers,J.C., Watkins,H.,
            Rothwell,P.M., Roberts,R., Markus,H.S., Samani,N.J., Farrall,M. and
            Schunkert,H.
  CONSRTM   METASTROKE Consortium; CARDIoGRAM Consortium; C4D Consortium;
            International Stroke Genetics Consortium
  TITLE     Shared genetic susceptibility to ischemic stroke and coronary
            artery disease: a genome-wide analysis of common variants
  JOURNAL   Stroke 45 (1), 24-36 (2014)
   PUBMED   24262325
  REMARK    Review article
REFERENCE   7  (residues 1 to 726)
  AUTHORS   Barber,M.J., Mangravite,L.M., Hyde,C.L., Chasman,D.I., Smith,J.D.,
            McCarty,C.A., Li,X., Wilke,R.A., Rieder,M.J., Williams,P.T.,
            Ridker,P.M., Chatterjee,A., Rotter,J.I., Nickerson,D.A.,
            Stephens,M. and Krauss,R.M.
  TITLE     Genome-wide association of lipid-lowering response to statins in
            combined study populations
  JOURNAL   PLoS One 5 (3), e9763 (2010)
   PUBMED   20339536
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 726)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 726)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC028586.1, BI550796.1, AK023511.1 and BM674566.1.
            
            On Feb 24, 2006 this sequence version replaced NP_078822.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.252175.1,
                                           SRR1803613.258641.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282003.7/ ENSP00000282003.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q31.1"
     Protein         1..726
                     /product="ORC ubiquitin ligase 1"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 219"
                     /calculated_mol_wt=80986
     Region          15..59
                     /region_name="RING-HC_RNF219"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 219 (RNF219) and similar proteins; cd16562"
                     /db_xref="CDD:438224"
     Region          <90..>267
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Region          276..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Region          436..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2Y0; propagated from
                     UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2Y0; propagated from
                     UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Region          570..602
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2Y0; propagated from
                     UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Region          687..726
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5W0B1.1)"
     Site            721
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5W0B1.1)"
     CDS             1..726
                     /gene="OBI1"
                     /gene_synonym="C13orf7; RNF219"
                     /coded_by="NM_024546.4:36..2216"
                     /db_xref="CCDS:CCDS31997.1"
                     /db_xref="GeneID:79596"
                     /db_xref="HGNC:HGNC:20308"
                     /db_xref="MIM:615906"
ORIGIN      
        1 maqtvqnvtl sltlpitchi clgkvrqpvi cinnhvfcsi cidlwlknns qcpacrvpit
       61 penpckeiig gtsesepmls htvrkhlrkt rlellhkeye deidclqkev eelksknlsl
      121 esqiktildp ltlvqgnqne dkhlvtdnps kinpetvaew kkklrtanei yekvkddvdk
      181 lkeankklkl engglvrenl rlkaevdnrs pqkfgrfava alqskveqye retnrlkkal
      241 ersdkyieel esqvaqlkns seekeamnsi cqtalsadgk gskgseedvv sknqgdsark
      301 qpgsstssss hlakpsssrl cdtssarqes tskadlncsk nkdlyqeqve vmldvtdtsm
      361 dtylerewgn kpsdcvpykd eelydlpapc tplslsclql stpenressv vqaggskkhs
      421 nhlrklvfdd fcdssnvsnk dsseddisrs enekksecfs spktgfwdcc stsyaqnldf
      481 essegntian svgeisskls eksglclskr lnsirsfemn rtrtsseasm daayldkise
      541 ldsmmsesdn skspcnngfk sldldglsks sqgsefleep dkleekteln lskgsltndq
      601 lengsewkpt sffllspsdq emnedfslhs sscpvtneik ppsclfqtef sqgillsssh
      661 rlfedqrfgs slfkmssemh slhnhlqspw stsfvpekrn knvnqstkrk iqsslssasp
      721 skatks
//
LOCUS       NP_689892                437 aa            linear   PRI 27-APR-2025
DEFINITION  sodium/bile acid cotransporter 4 [Homo sapiens].
ACCESSION   NP_689892
VERSION     NP_689892.1
DBSOURCE    REFSEQ: accession NM_152679.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Schmidt,S., Moncada,M., Burger,S. and Geyer,J.
  TITLE     Expression, sorting and transport studies for the orphan carrier
            SLC10A4 in neuronal and non-neuronal cell lines and in Xenopus
            laevis oocytes
  JOURNAL   BMC Neurosci 16, 35 (2015)
   PUBMED   26084360
  REMARK    GeneRIF: SLC10A4 failed to show transport activity for a series of
            neurotransmitters and neuromodulators, indicating that SLC10A4 does
            not seem to represent a typical neurotransmitter transporter such
            as DAT, SERT, CHT1 or VMAT2
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Abe,T., Kanemitu,Y., Nakasone,M., Kawahata,I., Yamakuni,T.,
            Nakajima,A., Suzuki,N., Nishikawa,M., Hishinuma,T. and Tomioka,Y.
  TITLE     SLC10A4 is a protease-activated transporter that transports bile
            acids
  JOURNAL   J Biochem 154 (1), 93-101 (2013)
   PUBMED   23589386
  REMARK    GeneRIF: The extracellular N-terminus of SLC10A4 was predicted to
            be relatively longer at the amino acid level than those of SLC10A1,
            SLC10A2 and SLC10A6. We examined the relationship between the
            N-terminus and transport activity of SLC10A4.
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Popova,S.N. and Alafuzoff,I.
  TITLE     Distribution of SLC10A4, a synaptic vesicle protein in the human
            brain, and the association of this protein with Alzheimer's
            disease-related neuronal degeneration
  JOURNAL   J Alzheimers Dis 37 (3), 603-610 (2013)
   PUBMED   23948907
  REMARK    GeneRIF: Depletion of SLC10A4 is observed in the brain with
            increased severity of Alzheimer's disease-related neuronal
            degeneration.
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Jostins,L., Ripke,S., Weersma,R.K., Duerr,R.H., McGovern,D.P.,
            Hui,K.Y., Lee,J.C., Schumm,L.P., Sharma,Y., Anderson,C.A.,
            Essers,J., Mitrovic,M., Ning,K., Cleynen,I., Theatre,E.,
            Spain,S.L., Raychaudhuri,S., Goyette,P., Wei,Z., Abraham,C.,
            Achkar,J.P., Ahmad,T., Amininejad,L., Ananthakrishnan,A.N.,
            Andersen,V., Andrews,J.M., Baidoo,L., Balschun,T., Bampton,P.A.,
            Bitton,A., Boucher,G., Brand,S., Buning,C., Cohain,A., Cichon,S.,
            D'Amato,M., De Jong,D., Devaney,K.L., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Ferguson,L.R., Franchimont,D., Fransen,K.,
            Gearry,R., Georges,M., Gieger,C., Glas,J., Haritunians,T., Hart,A.,
            Hawkey,C., Hedl,M., Hu,X., Karlsen,T.H., Kupcinskas,L.,
            Kugathasan,S., Latiano,A., Laukens,D., Lawrance,I.C., Lees,C.W.,
            Louis,E., Mahy,G., Mansfield,J., Morgan,A.R., Mowat,C., Newman,W.,
            Palmieri,O., Ponsioen,C.Y., Potocnik,U., Prescott,N.J.,
            Regueiro,M., Rotter,J.I., Russell,R.K., Sanderson,J.D., Sans,M.,
            Satsangi,J., Schreiber,S., Simms,L.A., Sventoraityte,J.,
            Targan,S.R., Taylor,K.D., Tremelling,M., Verspaget,H.W., De Vos,M.,
            Wijmenga,C., Wilson,D.C., Winkelmann,J., Xavier,R.J., Zeissig,S.,
            Zhang,B., Zhang,C.K., Zhao,H., Silverberg,M.S., Annese,V.,
            Hakonarson,H., Brant,S.R., Radford-Smith,G., Mathew,C.G.,
            Rioux,J.D., Schadt,E.E., Daly,M.J., Franke,A., Parkes,M.,
            Vermeire,S., Barrett,J.C. and Cho,J.H.
  CONSRTM   International IBD Genetics Consortium (IIBDGC)
  TITLE     Host-microbe interactions have shaped the genetic architecture of
            inflammatory bowel disease
  JOURNAL   Nature 491 (7422), 119-124 (2012)
   PUBMED   23128233
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Splinter,P.L., Lazaridis,K.N., Dawson,P.A. and LaRusso,N.F.
  TITLE     Cloning and expression of SLC10A4, a putative organic anion
            transport protein
  JOURNAL   World J Gastroenterol 12 (42), 6797-6805 (2006)
   PUBMED   17106928
  REMARK    GeneRIF: Northern analysis revealed that SLC10A4 mRNA is
            ubiquitously expressed in human tissues with the highest levels of
            mRNA expression in brain, placenta, and liver.
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Geyer,J., Wilke,T. and Petzinger,E.
  TITLE     The solute carrier family SLC10: more than a family of bile acid
            transporters regarding function and phylogenetic relationships
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 372 (6), 413-431 (2006)
   PUBMED   16541252
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK126542.1, BC019066.2, AA776274.1, AI421729.1 and AC096952.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK126542.1, BC019066.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000273861.5/ ENSP00000273861.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p11"
     Protein         1..437
                     /product="sodium/bile acid cotransporter 4"
                     /note="bile acid transporter SLC10A4; solute carrier
                     family 10 (sodium/bile acid cotransporter family), member
                     4; Na(+)/bile acid cotransporter 4"
                     /calculated_mol_wt=46373
     Site            6
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            24
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96EP9.2)"
     Region          37..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            87..88
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin; propagated from
                     UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            104..124
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EP9.2)"
     Region          113..385
                     /region_name="SBF"
                     /note="Sodium Bile acid symporter family; cl19217"
                     /db_xref="CDD:450274"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            198..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            234..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            268..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            292..312
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EP9.2)"
     Site            361..381
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EP9.2)"
     CDS             1..437
                     /gene="SLC10A4"
                     /gene_synonym="P4"
                     /coded_by="NM_152679.4:220..1533"
                     /db_xref="CCDS:CCDS3482.1"
                     /db_xref="GeneID:201780"
                     /db_xref="HGNC:HGNC:22980"
                     /db_xref="MIM:618563"
ORIGIN      
        1 mdgndnvtll fapllrdnyt lapnasslgp gtdlalapas sagpgpglsl gpgpsfgfsp
       61 gptptpeptt sglaggaash gpspfprpwa phalpfwdtp lnhglnvfvg aalcitmlgl
      121 gctvdvnhfg ahvrrpvgal laalcqfgll pllafllala fkldevaava vllcgccpgg
      181 nlsnlmsllv dgdmnlsiim tisstllalv lmplclwiys wawintpivq llplgtvtlt
      241 lcstlipigl gvfirykysr vadyivkvsl wsllvtlvvl fimtgtmlgp ellasipaav
      301 yviaifmpla gyasgyglat lfhlppnckr tvcletgsqn vqlctailkl afppqfigsm
      361 ymfpllyalf qsaeagifvl iykmygseml hkrdpldede dtdisykklk eeemadtsyg
      421 tvkaeniimm etaqtsl
//
LOCUS       NP_001355930             288 aa            linear   PRI 27-APR-2025
DEFINITION  aprataxin isoform h [Homo sapiens].
ACCESSION   NP_001355930 XP_024303348
VERSION     NP_001355930.1
DBSOURCE    REFSEQ: accession NM_001369001.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_024303348.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.179317.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..288
                     /product="aprataxin isoform h"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=32994
     Region          3..>44
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Region          110..211
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(204,206,208..210)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            206
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          229..288
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..288
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001369001.1:103..969"
                     /note="isoform h is encoded by transcript variant 22"
                     /db_xref="CCDS:CCDS75827.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqefeeea knpglethrk
       61 rkrsgnsdsi erdaaqeaea gtglepgsns gqcsvplkkg kdapikkesl ghwsqglkis
      121 mqdpkmqvyk deqvvvikdk ypkaryhwlv lpwtsisslk avarehlell khmhtvgekv
      181 ivdfagsskl rfrlgyhaip smshvhlhvi sqdfdspclk nkkhwnsfnt eyflesqavi
      241 emvqeagrvt vrdgmpellk lplrchecqq llpsipqlke hlrkhwtq
//
LOCUS       NP_001354750             316 aa            linear   PRI 27-APR-2025
DEFINITION  aldo-keto reductase family 1 member B15 isoform b [Homo sapiens].
ACCESSION   NP_001354750 XP_011514543
VERSION     NP_001354750.1
DBSOURCE    REFSEQ: accession NM_001367821.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Gimenez-Dejoz,J., Kolar,M.H., Ruiz,F.X., Crespo,I.,
            Cousido-Siah,A., Podjarny,A., Barski,O.A., Fanfrlik,J., Pares,X.,
            Farres,J. and Porte,S.
  TITLE     Substrate Specificity, Inhibitor Selectivity and Structure-Function
            Relationships of Aldo-Keto Reductase 1B15: A Novel Human
            Retinaldehyde Reductase
  JOURNAL   PLoS One 10 (7), e0134506 (2015)
   PUBMED   26222439
  REMARK    GeneRIF: Amino acid substitutions clustered in loops A and C result
            in a smaller more hydrophobic and more rigid active site in AKR1B15
            compared with the AKR1B10 pocket, consistent with distinct
            substrate specificity and narrower inhibitor selectivity for
            AKR1B15.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Weber,S., Salabei,J.K., Moller,G., Kremmer,E., Bhatnagar,A.,
            Adamski,J. and Barski,O.A.
  TITLE     Aldo-keto Reductase 1B15 (AKR1B15): a mitochondrial human aldo-keto
            reductase with activity toward steroids and 3-keto-acyl-CoA
            conjugates
  JOURNAL   J Biol Chem 290 (10), 6531-6545 (2015)
   PUBMED   25577493
  REMARK    GeneRIF: AKR1B15.2 localizes to the cytosol and displays no
            enzymatic activity with the substrates tested.
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Jagoe,W.N., Howe,K., O'Brien,S.C. and Carroll,J.
  TITLE     Identification of a role for a mouse sperm surface aldo-keto
            reductase (AKR1B7) and its human analogue in the detoxification of
            the reactive aldehyde, acrolein
  JOURNAL   Andrologia 45 (5), 326-331 (2013)
   PUBMED   22970857
  REMARK    GeneRIF: human sperm possess an aldo-keto reductase on their
            membrane surface and are thus enzymatically protected against
            reactive aldehyde species both in the male and female reproductive
            tract
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Calvo,S.E., Compton,A.G., Hershman,S.G., Lim,S.C., Lieber,D.S.,
            Tucker,E.J., Laskowski,A., Garone,C., Liu,S., Jaffe,D.B.,
            Christodoulou,J., Fletcher,J.M., Bruno,D.L., Goldblatt,J.,
            Dimauro,S., Thorburn,D.R. and Mootha,V.K.
  TITLE     Molecular diagnosis of infantile mitochondrial disease with
            targeted next-generation sequencing
  JOURNAL   Sci Transl Med 4 (118), 118ra10 (2012)
   PUBMED   22277967
  REMARK    GeneRIF: Strong candidate gene for mitochondrial disease, based on
            recessive mutations detected in infantile patients
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Salabei,J.K., Li,X.P., Petrash,J.M., Bhatnagar,A. and Barski,O.A.
  TITLE     Functional expression of novel human and murine AKR1B genes
  JOURNAL   Chem Biol Interact 191 (1-3), 177-184 (2011)
   PUBMED   21276782
  REMARK    GeneRIF: AKR1B15 and Akr1b16 genes are expressed as functional
            proteins in human and murine tissues
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC078847.2.
            
            On Dec 19, 2018 this sequence version replaced XP_011514543.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2162568,
                              SAMEA2162946 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..316
                     /product="aldo-keto reductase family 1 member B15 isoform
                     b"
                     /EC_number="1.1.1.64"
                     /EC_number="1.1.1.300"
                     /EC_number="1.1.1.216"
                     /EC_number="1.1.1.54"
                     /note="putative aldo-keto reductase family 1 member B15;
                     estradiol 17-beta-dehydrogenase AKR1B15; farnesol
                     dehydrogenase; testosterone 17beta-dehydrogenase"
                     /calculated_mol_wt=36406
     Region          10..316
                     /region_name="AKR_AKR1B1-19"
                     /note="AKR1B family of aldo-keto reductase (AKR); cd19107"
                     /db_xref="CDD:381333"
     Site            order(19..22,44,48..49,78,80,111..112,114,116,123,
                     160..161,184,210..217,220,229,246,261..266,269,272..273,
                     299..301,304,310..311)
                     /site_type="active"
                     /db_xref="CDD:381333"
     Site            order(44,49,78,111)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381333"
     Site            78
                     /site_type="other"
                     /note="Lowers pKa of active site Tyr.
                     /evidence=ECO:0000250|UniProtKB:P14550; propagated from
                     UniProtKB/Swiss-Prot (C9JRZ8.2)"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O60218; propagated from
                     UniProtKB/Swiss-Prot (C9JRZ8.2)"
     Site            263
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O60218; propagated from
                     UniProtKB/Swiss-Prot (C9JRZ8.2)"
     CDS             1..316
                     /gene="AKR1B15"
                     /gene_synonym="AK1R1B7; AKR1B10L; AKR1R1B7"
                     /coded_by="NM_001367821.1:1024..1974"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS94205.1"
                     /db_xref="GeneID:441282"
                     /db_xref="HGNC:HGNC:37281"
                     /db_xref="MIM:616336"
ORIGIN      
        1 matfvelstk akmpivglgt wrsllgkvke avkvaidaey rhidcayfye nqhevgeaiq
       61 ekiqekavmr edlfivskvw ptfferplvr kafektlkdl klsyldvyli hwpqgfktgd
      121 dffpkddkgn misgkgtfld aweameelvd eglvkalgvs nfnhfqierl lnkpglkykp
      181 vtnqvechpy ltqekliqyc hskgitvtay splgspdrpw akpedpslle dpkikeiaak
      241 hkkttaqvli rfhiqrnvtv ipksmtpahi veniqvfdfk lsdeematil sfnrnwrafd
      301 fkefshledf pfdaey
//
LOCUS       NP_000796                101 aa            linear   PRI 27-APR-2025
DEFINITION  gastrin preproprotein [Homo sapiens].
ACCESSION   NP_000796
VERSION     NP_000796.1
DBSOURCE    REFSEQ: accession NM_000805.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Varga,A.J., Nemeth,I.B., Kemeny,L., Varga,J., Tiszlavicz,L.,
            Kumar,D., Dodd,S., Simpson,A.W.M., Buknicz,T., Beynon,R.,
            Simpson,D., Krenacs,T., Dockray,G.J. and Varro,A.
  TITLE     Elevated Serum Gastrin Is Associated with Melanoma Progression:
            Putative Role in Increased Migration and Invasion of Melanoma Cells
  JOURNAL   Int J Mol Sci 24 (23), 16851 (2023)
   PUBMED   38069171
  REMARK    GeneRIF: Elevated Serum Gastrin Is Associated with Melanoma
            Progression: Putative Role in Increased Migration and Invasion of
            Melanoma Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Iwanaga,T.
  TITLE     Anatomical basis of gastrin- and CCK-secreting cells and their
            functions. A review
  JOURNAL   Biomed Res 44 (3), 81-95 (2023)
   PUBMED   37258205
  REMARK    GeneRIF: Anatomical basis of gastrin- and CCK-secreting cells and
            their functions. A review.
            Review article
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Hua,C. and Yu,D.
  TITLE     Correlation Study between Levels of Gastrin, Serum IGF-1, and GHBP
            and Growth and Development in Children with Short Stature Based on
            Big Data Analysis
  JOURNAL   Dis Markers 2022, 4614099 (2022)
   PUBMED   36061351
  REMARK    GeneRIF: Correlation Study between Levels of Gastrin, Serum IGF-1,
            and GHBP and Growth and Development in Children with Short Stature
            Based on Big Data Analysis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Asfuroglu Kalkan,E., Kalkan,C., Gumussoy,M., Gucbey,O. and
            Soykan,I.
  TITLE     Prevalence and predictors of colonoscopic findings in patients with
            autoimmune gastritis
  JOURNAL   J Investig Med 70 (1), 73-78 (2022)
   PUBMED   34341100
  REMARK    GeneRIF: Prevalence and predictors of colonoscopic findings in
            patients with autoimmune gastritis.
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Galvin,S.G., Larraufie,P., Kay,R.G., Pitt,H., Bernard,E.,
            McGavigan,A.K., Brant,H., Hood,J., Sheldrake,L., Conder,S.,
            Atherton-Kemp,D., Lu,V.B., O'Flaherty,E.A.A., Roberts,G.P.,
            Ammala,C., Jermutus,L., Baker,D., Gribble,F.M. and Reimann,F.
  TITLE     Peptidomics of enteroendocrine cells and characterisation of
            potential effects of a novel preprogastrin derived-peptide on
            glucose tolerance in lean mice
  JOURNAL   Peptides 140, 170532 (2021)
   PUBMED   33744371
  REMARK    GeneRIF: Peptidomics of enteroendocrine cells and characterisation
            of potential effects of a novel preprogastrin derived-peptide on
            glucose tolerance in lean mice.
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Pauwels,S., Najdovski,T., Dimaline,R., Lee,C.M. and
            Deschodt-Lanckman,M.
  TITLE     Degradation of human gastrin and CCK by endopeptidase 24.11:
            differential behaviour of the sulphated and unsulphated peptides
  JOURNAL   Biochim Biophys Acta 996 (1-2), 82-88 (1989)
   PUBMED   2736261
REFERENCE   7  (residues 1 to 101)
  AUTHORS   Higashimoto,Y., Himeno,S., Shinomura,Y., Nagao,K., Tamura,T. and
            Tarui,S.
  TITLE     Purification and structural determination of urinary NH2-terminal
            big gastrin fragments
  JOURNAL   Biochem Biophys Res Commun 160 (3), 1364-1370 (1989)
   PUBMED   2730647
REFERENCE   8  (residues 1 to 101)
  AUTHORS   Lund,T., Geurts van Kessel,A.H., Haun,S. and Dixon,J.E.
  TITLE     The genes for human gastrin and cholecystokinin are located on
            different chromosomes
  JOURNAL   Hum Genet 73 (1), 77-80 (1986)
   PUBMED   3011648
REFERENCE   9  (residues 1 to 101)
  AUTHORS   Polosatov,M.V., Klimov,P.K., Masevich,C.G., Samartsev,M.A. and
            Wunsch,E.
  TITLE     Interaction of synthetic human big gastrin with blood proteins of
            man and animals
  JOURNAL   Acta Hepatogastroenterol (Stuttg) 26 (2), 154-159 (1979)
   PUBMED   463490
REFERENCE   10 (residues 1 to 101)
  AUTHORS   Fritsch,W.P., Hausamen,T.U. and Scholten,T.
  TITLE     [Gastrointestinal hormones. I. Hormones of the gastrin group]
  JOURNAL   Z Gastroenterol 15 (4), 264-276 (1977)
   PUBMED   871064
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC130686.15 and AC109319.17.
            
            Summary: Gastrin is a hormone whose main function is to stimulate
            secretion of hydrochloric acid by the gastric mucosa, which results
            in gastrin formation inhibition. This hormone also acts as a
            mitogenic factor for gastrointestinal epithelial cells. Gastrin has
            two biologically active peptide forms, G34 and G17. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM768289.1, BM768748.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329402.4/ ENSP00000331358.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..101
                     /product="gastrin preproprotein"
                     /note="preprogastrin"
                     /calculated_mol_wt=9082
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2330
     mat_peptide     22..92
                     /product="Gastrin-71. /id=PRO_0000010633"
                     /note="propagated from UniProtKB/Swiss-Prot (P01350.1)"
                     /calculated_mol_wt=8067
     Region          22..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01350.1)"
     Site            40..41
                     /site_type="cleavage"
                     /note="Cleavage; propagated from UniProtKB/Swiss-Prot
                     (P01350.1)"
     mat_peptide     41..92
                     /product="Gastrin-52. /id=PRO_0000010634"
                     /note="propagated from UniProtKB/Swiss-Prot (P01350.1)"
                     /calculated_mol_wt=6019
     Site            58..59
                     /site_type="cleavage"
                     /note="Cleavage; propagated from UniProtKB/Swiss-Prot
                     (P01350.1)"
     mat_peptide     59..92
                     /product="Big gastrin. /id=PRO_0000010635"
                     /note="propagated from UniProtKB/Swiss-Prot (P01350.1)"
                     /calculated_mol_wt=3867
     Site            59
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid, in form big gastrin.
                     /evidence=ECO:0000269|PubMed:2730647; propagated from
                     UniProtKB/Swiss-Prot (P01350.1)"
     Site            75..76
                     /site_type="cleavage"
                     /note="Cleavage; propagated from UniProtKB/Swiss-Prot
                     (P01350.1)"
     mat_peptide     76..92
                     /product="Gastrin. /id=PRO_0000010636"
                     /note="propagated from UniProtKB/Swiss-Prot (P01350.1)"
                     /calculated_mol_wt=2116
     Site            76
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid, in form gastrin.
                     /evidence=ECO:0000269|PubMed:5921183; propagated from
                     UniProtKB/Swiss-Prot (P01350.1)"
     mat_peptide     79..92
                     /product="Gastrin-14. /id=PRO_0000010637"
                     /note="propagated from UniProtKB/Swiss-Prot (P01350.1)"
                     /calculated_mol_wt=1834
     mat_peptide     87..92
                     /product="Gastrin-6. /id=PRO_0000010638"
                     /note="propagated from UniProtKB/Swiss-Prot (P01350.1)"
                     /calculated_mol_wt=818
     Site            87
                     /site_type="sulfatation"
                     /note="Sulfotyrosine, partial.
                     /evidence=ECO:0000269|PubMed:11052986,
                     ECO:0000269|PubMed:7530658; propagated from
                     UniProtKB/Swiss-Prot (P01350.1)"
     Region          88..101
                     /region_name="GASTRIN"
                     /note="gastrin / cholecystokinin / caerulein family;
                     smart00029"
                     /db_xref="CDD:214476"
     Site            92
                     /site_type="amidation"
                     /note="Phenylalanine amide.
                     /evidence=ECO:0000269|PubMed:5921183; propagated from
                     UniProtKB/Swiss-Prot (P01350.1)"
     Site            95..96
                     /site_type="cleavage"
                     /note="Cleavage; propagated from UniProtKB/Swiss-Prot
                     (P01350.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:3223964; propagated from
                     UniProtKB/Swiss-Prot (P01350.1)"
     CDS             1..101
                     /gene="GAST"
                     /gene_synonym="GAS"
                     /coded_by="NM_000805.5:63..368"
                     /db_xref="CCDS:CCDS11404.1"
                     /db_xref="GeneID:2520"
                     /db_xref="HGNC:HGNC:4164"
                     /db_xref="MIM:137250"
ORIGIN      
        1 mqrlcvyvli falalaafse aswkprsqqp daplgtganr dlelpwleqq gpashhrrql
       61 gpqgpphlva dpskkqgpwl eeeeeaygwm dfgrrsaede n
//
LOCUS       NP_001349655             914 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 62 isoform 1 [Mus musculus].
ACCESSION   NP_001349655 XP_006533261
VERSION     NP_001349655.1
DBSOURCE    REFSEQ: accession NM_001362726.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Choi,M.Y., Romer,A.I., Hu,M., Lepourcelet,M., Mechoor,A.,
            Yesilaltay,A., Krieger,M., Gray,P.A. and Shivdasani,R.A.
  TITLE     A dynamic expression survey identifies transcription factors
            relevant in mouse digestive tract development
  JOURNAL   Development 133 (20), 4119-4129 (2006)
   PUBMED   16971476
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Hunt,C.R., Parsian,A.J. and Kozak,C.A.
  TITLE     Genetic mapping of mouse heat shock protein genes Hsc4a to
            chromosome 11 and Hsc74 to chromosome 18 and two Hsc74 pseudogenes
            to chromosomes X and 8
  JOURNAL   Genomics 56 (3), 358-360 (1999)
   PUBMED   10087208
REFERENCE   4  (residues 1 to 914)
  AUTHORS   Agata,Y., Matsuda,E. and Shimizu,A.
  TITLE     Rapid and efficient cloning of cDNAs encoding Kruppel-like zinc
            finger proteins by degenerate PCR
  JOURNAL   Gene 213 (1-2), 55-64 (1998)
   PUBMED   9630514
REFERENCE   5  (residues 1 to 914)
  AUTHORS   Polimeni,M., Giorgi,S., De Gregorio,L., Dragani,T.A., Molinaro,M.,
            Cossu,G. and Bouche,M.
  TITLE     Differentiation dependent expression in muscle cells of ZT3, a
            novel zinc finger factor differentially expressed in embryonic and
            adult tissues
  JOURNAL   Mech Dev 54 (1), 107-117 (1996)
   PUBMED   8808410
REFERENCE   6  (residues 1 to 914)
  AUTHORS   Danciger,M., Brady,J., Adamson,M.C., Farber,D.B., Piatigorsky,J.
            and Kozak,C.A.
  TITLE     Chromosomal localization of the genes for five zinc finger proteins
            expressed in mouse lens
  JOURNAL   Genomics 28 (1), 39-43 (1995)
   PUBMED   7590745
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606829.13 and BE635021.1.
            
            On Apr 26, 2018 this sequence version replaced XP_006533261.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR3363660.2665059.1,
                                           SRR9219382.130201.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 29.23 cM"
     Protein         1..914
                     /product="zinc finger protein 62 isoform 1"
                     /note="ZT3"
                     /calculated_mol_wt=104681
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8C827.1)"
     Region          80..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8C827.1)"
     Region          127..542
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          133..153
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          161..181
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          189..209
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(222,224,226,228..229,232..233,236,250,252,256..257,
                     260..261,264,278,280,282,284..285,288..289,292)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..321
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          329..349
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(334,336,338,340..341,344..345,348,362,364,368..369,
                     372..373,376,390,392,394,396..397,400..401,404)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <379..458
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          385..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          437..850
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(446,448,450,452..453,456..457,460,474,476,480..481,
                     484..485,488,502,504,506,508..509,512..513,516)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          525..545
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          553..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          581..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          609..629
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(614,616,618,620..621,624..625,628,642,644,648..649,
                     652..653,656,670,672,674,676..677,680..681,684)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          637..657
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          665..685
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          693..713
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(698,700,702,704..705,708..709,712,726,728,732..733,
                     736..737,740,754,756,758,760..761,764..765,768)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          721..741
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          749..769
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          777..797
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          805..824
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          832..852
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8C827.1)"
     CDS             1..914
                     /gene="Zfp62"
                     /coded_by="NM_001362726.1:247..2991"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:22720"
                     /db_xref="MGI:MGI:99662"
ORIGIN      
        1 msylkttmed eesskknend snadsqcpsv gffhkdhmqk sktgdtcdlf pkwkilkegk
       61 ssiremidth tnaanikleq ddetseksfy pstntmhqti ptepnctkqg ehteningnv
      121 hpahiadkkl hkcdecgksf kynsrlvqhk imhtgekrye cddcrgtfrs ssslrvhkri
      181 htgekpykcd ecgkaymsys slinhksths geknckcdec gksfnyssvl dqhkrihtge
      241 kpyecgecgk afrnssglrv hkrihtgekp yecdtcgktf snssglrvhk rihtgekpye
      301 cdecgkafit crtllnhksi hfgdkpykcd eceksfnyss lliqhkviht gekpyecdec
      361 gkafrnssgl ivhkrihtge kpykcdicgk afsyssglav hksihpgkka heckdcgksf
      421 synslllqhk tihtgerpyv cdvcgktfrn nsglkvhrrl htgekpykcd vcgkayisrs
      481 slknhkgihm gekpykcsyc eksfnyssal eqhkrihtre kpfgcdecgk afrnnsglkv
      541 hkrihtgerp ykceecgkay islsslinhk svhpgekpfk cdecekafit yrtllnhkki
      601 hlgekpykcd vceksfnyts llsqhkrvht rekpfecdrc ekvfrnnssl kvhkrihtge
      661 kpyecdicgk ayishsslin hksthpgkts ytcdecgkaf fssrtlishk rvhlgekpfk
      721 cvecgksfsy ssllsqhkri htgekpyvcd wcgkafrnss gltvhkriht gekpygcdec
      781 ekayishssl inhksvhrgk qpyncecgks fnyrsvldqh krihtgkkpy rcndcgkafn
      841 irsnltkhkr ihtgeeslnm anmeshsgtf qkmiyyeggn sldgtrmqmp vweaehaksq
      901 rnqieeklye ynnf
//
LOCUS       NP_004691                695 aa            linear   PRI 27-APR-2025
DEFINITION  potassium voltage-gated channel subfamily KQT member 4 isoform a
            [Homo sapiens].
ACCESSION   NP_004691 XP_001132376
VERSION     NP_004691.2
DBSOURCE    REFSEQ: accession NM_004700.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Ren,L., Wu,J., Kuang,Y., Chen,K., Jiang,M., Zhuo,Z., Cao,Z. and
            Huang,S.
  TITLE     A novel variant c.902C>A (p. A301D) in KCNQ4 associated with
            non-syndromic deafness 2A in a Chinese family
  JOURNAL   Mol Genet Genomic Med 12 (7), e2446 (2024)
   PUBMED   38980994
  REMARK    GeneRIF: A novel variant c.902C>A (p. A301D) in KCNQ4 associated
            with non-syndromic deafness 2A in a Chinese family.
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Zhang,X., Shi,T., Li,J., Wu,X., Wu,K., Li,D., Wang,D., Guan,J. and
            Wang,H.
  TITLE     Natural History of KCNQ4 p.G285S Related Hearing Loss, Construction
            of iPSC and Mouse Model
  JOURNAL   Laryngoscope 134 (5), 2356-2363 (2024)
   PUBMED   37962101
  REMARK    GeneRIF: Natural History of KCNQ4 p.G285S Related Hearing Loss,
            Construction of iPSC and Mouse Model.
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Zhao,Q., Li,M. and Zhang,Y.
  TITLE     Comprehensive pan-cancer analysis of potassium voltage-gated
            channel Q4 (KCNQ4) gene across multiple human malignant tumors
  JOURNAL   Sci Rep 13 (1), 18608 (2023)
   PUBMED   37903775
  REMARK    GeneRIF: Comprehensive pan-cancer analysis of potassium
            voltage-gated channel Q4 (KCNQ4) gene across multiple human
            malignant tumors.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Oh,K.S., Roh,J.W., Joo,S.Y., Ryu,K., Kim,J.A., Kim,S.J., Jang,S.H.,
            Koh,Y.I., Kim,D.H., Kim,H.Y., Choi,M., Jung,J., Namkung,W.,
            Nam,J.H., Choi,J.Y. and Gee,H.Y.
  TITLE     Overlooked KCNQ4 variants augment the risk of hearing loss
  JOURNAL   Exp Mol Med 55 (4), 844-859 (2023)
   PUBMED   37009795
  REMARK    GeneRIF: Overlooked KCNQ4 variants augment the risk of hearing
            loss.
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Selyanko,A.A., Hadley,J.K., Wood,I.C., Abogadie,F.C., Jentsch,T.J.
            and Brown,D.A.
  TITLE     Inhibition of KCNQ1-4 potassium channels expressed in mammalian
            cells via M1 muscarinic acetylcholine receptors
  JOURNAL   J Physiol 522 Pt 3 (Pt 3), 349-355 (2000)
   PUBMED   10713961
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Coucke,P.J., Van Hauwe,P., Kelley,P.M., Kunst,H., Schatteman,I.,
            Van Velzen,D., Meyers,J., Ensink,R.J., Verstreken,M., Declau,F.,
            Marres,H., Kastury,K., Bhasin,S., McGuirt,W.T., Smith,R.J.,
            Cremers,C.W., Van de Heyning,P., Willems,P.J., Smith,S.D. and Van
            Camp,G.
  TITLE     Mutations in the KCNQ4 gene are responsible for autosomal dominant
            deafness in four DFNA2 families
  JOURNAL   Hum Mol Genet 8 (7), 1321-1328 (1999)
   PUBMED   10369879
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Kubisch,C., Schroeder,B.C., Friedrich,T., Lutjohann,B.,
            El-Amraoui,A., Marlin,S., Petit,C. and Jentsch,T.J.
  TITLE     KCNQ4, a novel potassium channel expressed in sensory outer hair
            cells, is mutated in dominant deafness
  JOURNAL   Cell 96 (3), 437-446 (1999)
   PUBMED   10025409
REFERENCE   8  (residues 1 to 695)
  AUTHORS   Talebizadeh,Z., Kelley,P.M., Askew,J.W., Beisel,K.W. and Smith,S.D.
  TITLE     Novel mutation in the KCNQ4 gene in a large kindred with dominant
            progressive hearing loss
  JOURNAL   Hum Mutat 14 (6), 493-501 (1999)
   PUBMED   10571947
REFERENCE   9  (residues 1 to 695)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Smith,R.J.H. and Hildebrand,M.
  TITLE     DFNA2 Nonsyndromic Hearing Loss
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301388
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC119677.2, AF105202.1,
            DA782056.1, AK074957.1 and CA411644.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Sep 20, 2006 this sequence version replaced
            XP_001132376.1, NP_004691.1.
            
            Summary: The protein encoded by this gene forms a potassium channel
            that is thought to play a critical role in the regulation of
            neuronal excitability, particularly in sensory cells of the
            cochlea. The current generated by this channel is inhibited by M1
            muscarinic acetylcholine receptors and activated by retigabine, a
            novel anti-convulsant drug. The encoded protein can form a
            homomultimeric potassium channel or possibly a heteromultimeric
            channel in association with the protein encoded by the KCNQ3 gene.
            Defects in this gene are a cause of nonsyndromic sensorineural
            deafness type 2 (DFNA2), an autosomal dominant form of progressive
            hearing loss. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer and predominant isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3812009.1,
                                           SRR18074969.1414036.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147975, SAMEA2151887
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000347132.10/ ENSP00000262916.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..695
                     /product="potassium voltage-gated channel subfamily KQT
                     member 4 isoform a"
                     /note="potassium channel KQT-like 4; potassium
                     voltage-gated channel subfamily KQT member 4; potassium
                     channel subunit alpha KvLQT4; potassium voltage-gated
                     channel, KQT-like subfamily, member 4; potassium channel,
                     voltage gated KQT-like subfamily Q, member 4"
                     /calculated_mol_wt=76970
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Site            97..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Region          98..330
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            130..152
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Site            169..191
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Site            203..223
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Site            236..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Site            294..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Region          342..351
                     /region_name="Interaction with CALM.
                     /evidence=ECO:0000269|PubMed:29429937"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Region          400..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Region          464..647
                     /region_name="KCNQ_channel"
                     /note="KCNQ voltage-gated potassium channel; pfam03520"
                     /db_xref="CDD:460954"
     Region          496..515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Region          535..549
                     /region_name="Interaction with CALM.
                     /evidence=ECO:0000250|UniProtKB:P51787"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Region          546..650
                     /region_name="C-terminal assembly domain
                     (tetramerization). /evidence=ECO:0000269|PubMed:17329207"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     Region          587..606
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56696.2)"
     CDS             1..695
                     /gene="KCNQ4"
                     /gene_synonym="DFNA2; DFNA2A; KV7.4"
                     /coded_by="NM_004700.4:308..2395"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS456.1"
                     /db_xref="GeneID:9132"
                     /db_xref="HGNC:HGNC:6298"
                     /db_xref="MIM:603537"
ORIGIN      
        1 maeapprrlg lgpppgdapr aelvaltavq seqgeagggg sprrlgllgs plppgaplpg
       61 pgsgsgsacg qrssaahkry rrlqnwvynv lerprgwafv yhvfifllvf sclvlsvlst
      121 iqehqelane cllilefvmi vvfgleyivr vwsagcccry rgwqgrfrfa rkpfcvidfi
      181 vfvasvavia agtqgnifat salrsmrflq ilrmvrmdrr ggtwkllgsv vyahskelit
      241 awyigflvli fasflvylae kdansdfssy adslwwgtit lttigygdkt phtwlgrvla
      301 agfallgisf falpagilgs gfalkvqeqh rqkhfekrrm paanliqaaw rlystdmsra
      361 yltatwyyyd silpsfrela llfehvqrar ngglrplevr rapvpdgaps ryppvatchr
      421 pgstsfcpge ssrmgikdri rmgssqrrtg pskqhlappt mptspsseqv geatsptkvq
      481 kswsfndrtr fraslrlkpr tsaedapsee vaeeksyqce ltvddimpav ktvirsiril
      541 kflvakrkfk etlrpydvkd vieqysaghl dmlgrikslq trvdqivgrg pgdrkarekg
      601 dkgpsdaevv deismmgrvv kvekqvqsie hkldlllgfy srclrsgtsa slgavqvplf
      661 dpditsdyhs pvdhedisvs aqtlsisrsv stnmd
//
LOCUS       NP_001348996             158 aa            linear   ROD 27-APR-2025
DEFINITION  EKC/KEOPS complex subunit Tprkb isoform b [Mus musculus].
ACCESSION   NP_001348996
VERSION     NP_001348996.1
DBSOURCE    REFSEQ: accession NM_001362067.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Iwata,S., Sasaki,T., Nagahara,M. and Iwamoto,T.
  TITLE     An efficient i-GONAD method for creating and maintaining lethal
            mutant mice using an inversion balancer identified from the
            C3H/HeJJcl strain
  JOURNAL   G3 (Bethesda) 11 (8) (2021)
   PUBMED   34849815
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Braun,D.A., Rao,J., Mollet,G., Schapiro,D., Daugeron,M.C., Tan,W.,
            Gribouval,O., Boyer,O., Revy,P., Jobst-Schwan,T., Schmidt,J.M.,
            Lawson,J.A., Schanze,D., Ashraf,S., Ullmann,J.F.P.,
            Hoogstraten,C.A., Boddaert,N., Collinet,B., Martin,G., Liger,D.,
            Lovric,S., Furlano,M., Guerrera,I.C., Sanchez-Ferras,O., Hu,J.F.,
            Boschat,A.C., Sanquer,S., Menten,B., Vergult,S., De Rocker,N.,
            Airik,M., Hermle,T., Shril,S., Widmeier,E., Gee,H.Y., Choi,W.I.,
            Sadowski,C.E., Pabst,W.L., Warejko,J.K., Daga,A., Basta,T.,
            Matejas,V., Scharmann,K., Kienast,S.D., Behnam,B., Beeson,B.,
            Begtrup,A., Bruce,M., Ch'ng,G.S., Lin,S.P., Chang,J.H., Chen,C.H.,
            Cho,M.T., Gaffney,P.M., Gipson,P.E., Hsu,C.H., Kari,J.A., Ke,Y.Y.,
            Kiraly-Borri,C., Lai,W.M., Lemyre,E., Littlejohn,R.O., Masri,A.,
            Moghtaderi,M., Nakamura,K., Ozaltin,F., Praet,M., Prasad,C.,
            Prytula,A., Roeder,E.R., Rump,P., Schnur,R.E., Shiihara,T.,
            Sinha,M.D., Soliman,N.A., Soulami,K., Sweetser,D.A., Tsai,W.H.,
            Tsai,J.D., Topaloglu,R., Vester,U., Viskochil,D.H.,
            Vatanavicharn,N., Waxler,J.L., Wierenga,K.J., Wolf,M.T.F.,
            Wong,S.N., Leidel,S.A., Truglio,G., Dedon,P.C., Poduri,A., Mane,S.,
            Lifton,R.P., Bouchard,M., Kannu,P., Chitayat,D., Magen,D.,
            Callewaert,B., van Tilbeurgh,H., Zenker,M., Antignac,C. and
            Hildebrandt,F.
  TITLE     Mutations in KEOPS-complex genes cause nephrotic syndrome with
            primary microcephaly
  JOURNAL   Nat Genet 49 (10), 1529-1538 (2017)
   PUBMED   28805828
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Quina,L.A., Wang,S., Ng,L. and Turner,E.E.
  TITLE     Brn3a and Nurr1 mediate a gene regulatory pathway for habenula
            development
  JOURNAL   J Neurosci 29 (45), 14309-14322 (2009)
   PUBMED   19906978
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Daigo,Y., Takayama,I., Ward,S.M., Sanders,K.M. and Fujino,M.A.
  TITLE     Isolation of novel mouse genes that were differentially expressed
            in W/W(V) mouse fundus
  JOURNAL   J Gastroenterol 39 (3), 238-241 (2004)
   PUBMED   15065000
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Miyoshi,A., Kito,K., Aramoto,T., Abe,Y., Kobayashi,N. and Ueda,N.
  TITLE     Identification of CGI-121, a novel PRPK (p53-related protein
            kinase)-binding protein
  JOURNAL   Biochem Biophys Res Commun 303 (2), 399-405 (2003)
   PUBMED   12659830
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158679.8, CO424671.1 and BC027413.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR and in
            the 3' UTR and coding sequence compared to variant 3. The resulting
            isoform (b) has a shorter and distinct C-terminus compared to
            isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CO424671.1, AI317221.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849379
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 37.53 cM"
     Protein         1..158
                     /product="EKC/KEOPS complex subunit Tprkb isoform b"
                     /note="TP53RK-binding protein; Prpk (p53-related protein
                     kinase)-binding protein; EKC/KEOPS complex subunit Tprkb;
                     PRPK-binding protein"
                     /calculated_mol_wt=17549
     Region          20..148
                     /region_name="CGI-121"
                     /note="Kinase binding protein CGI-121; pfam08617"
                     /db_xref="CDD:462537"
     CDS             1..158
                     /gene="Tprkb"
                     /gene_synonym="0610033G21Rik; 1810034M08Rik; Cgi-121;
                     DRWMS1; mDRWMS1"
                     /coded_by="NM_001362067.1:184..660"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS90081.1"
                     /db_xref="GeneID:69786"
                     /db_xref="MGI:MGI:1917036"
ORIGIN      
        1 mqlsqqldlf pecrvtlllf kdvknagdlr kkamegsidg slinpnvivd pfqilvaank
       61 avhlhrlgkm ktrtlsteii fnlspnnnis ealkkfgise tntsvlivyi edgskqvpqe
      121 hlvsqvegqq vpleslpeit rlsevkkvcp ahfeefsr
//
LOCUS       NP_612468                293 aa            linear   PRI 27-APR-2025
DEFINITION  dehydrodolichyl diphosphate synthase complex subunit NUS1 [Homo
            sapiens].
ACCESSION   NP_612468
VERSION     NP_612468.1
DBSOURCE    REFSEQ: accession NM_138459.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Shen,N.X., Qu,X.C., Yu,J., Fan,C.X., Min,F.L., Li,L.Y., Zhang,M.R.,
            Li,B.M., Wang,J., He,N., Liao,W.P., Shi,Y.W. and Li,W.B.
  TITLE     NUS1 Variants Cause Lennox-Gastaut Syndrome Related to Unfolded
            Protein Reaction Activation
  JOURNAL   Mol Neurobiol 61 (11), 8518-8530 (2024)
   PUBMED   38520610
  REMARK    GeneRIF: NUS1 Variants Cause Lennox-Gastaut Syndrome Related to
            Unfolded Protein Reaction Activation.
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Ji,C., Zhao,J., Zhang,J. and Wang,K.
  TITLE     Novel NUS1 variant in a Chinese patient with progressive myoclonus
            epilepsy: a case report and systematic review
  JOURNAL   Neurol Sci 44 (10), 3495-3498 (2023)
   PUBMED   37249665
  REMARK    GeneRIF: Novel NUS1 variant in a Chinese patient with progressive
            myoclonus epilepsy: a case report and systematic review.
            Review article
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Liu,C., Li,S., Zhang,X., Jin,C., Zhao,B., Li,L., Miao,Q.R., Jin,Y.
            and Fan,Z.
  TITLE     Nogo-B receptor increases glycolysis and the paclitaxel resistance
            of estrogen receptor-positive breast cancer via the
            HIF-1alpha-dependent pathway
  JOURNAL   Cancer Gene Ther 30 (5), 647-658 (2023)
   PUBMED   36241702
  REMARK    GeneRIF: Nogo-B receptor increases glycolysis and the paclitaxel
            resistance of estrogen receptor-positive breast cancer via the
            HIF-1alpha-dependent pathway.
            Erratum:[Cancer Gene Ther. 2023 May;30(5):766. doi:
            10.1038/s41417-022-00553-3. PMID: 36376422]
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Jiang,L., Mei,J.P., Zhao,Y.W., Zhang,R., Pan,H.X., Yang,Y.,
            Sun,Q.Y., Xu,Q., Yan,X.X., Tan,J.Q., Li,J.C., Tang,B.S. and
            Guo,J.F.
  TITLE     Low-frequency and rare coding variants of NUS1 contribute to
            susceptibility and phenotype of Parkinson's disease
  JOURNAL   Neurobiol Aging 110, 106-112 (2022)
   PUBMED   34635350
  REMARK    GeneRIF: Low-frequency and rare coding variants of NUS1 contribute
            to susceptibility and phenotype of Parkinson's disease.
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Zhang,T., Zhao,L., Wang,S., Liu,J., Chang,Y., Ma,L., Feng,J. and
            Niu,Y.
  TITLE     Common Variants in NUS1 and GP2 Genes Contributed to the Risk of
            Gestational Diabetes Mellitus
  JOURNAL   Front Endocrinol (Lausanne) 12, 685524 (2021)
   PUBMED   34326813
  REMARK    GeneRIF: Common Variants in NUS1 and GP2 Genes Contributed to the
            Risk of Gestational Diabetes Mellitus.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Harrison,K.D., Park,E.J., Gao,N., Kuo,A., Rush,J.S., Waechter,C.J.,
            Lehrman,M.A. and Sessa,W.C.
  TITLE     Nogo-B receptor is necessary for cellular dolichol biosynthesis and
            protein N-glycosylation
  JOURNAL   EMBO J 30 (12), 2490-2500 (2011)
   PUBMED   21572394
  REMARK    GeneRIF: Nogo-B receptor (NgBR) is an essential component of the
            dolichol monophosophate (Dol-P) biosynthetic machinery. Loss of
            NgBR results in a robust deficit in cis-isoprenyltransferase
            (IPTase) activity and Dol-P production.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Harrison,K.D., Miao,R.Q., Fernandez-Hernando,C., Suarez,Y.,
            Davalos,A. and Sessa,W.C.
  TITLE     Nogo-B receptor stabilizes Niemann-Pick type C2 protein and
            regulates intracellular cholesterol trafficking
  JOURNAL   Cell Metab 10 (3), 208-218 (2009)
   PUBMED   19723497
  REMARK    GeneRIF: The Nogo-B receptor localizes primarily to the endoplasmic
            reticulum and regulates the stability of nascent Niemann-Pick type
            C2 protein.
REFERENCE   8  (residues 1 to 293)
  AUTHORS   Wojcik,S., Engel,W.K., Yan,R., McFerrin,J. and Askanas,V.
  TITLE     NOGO is increased and binds to BACE1 in sporadic inclusion-body
            myositis and in A beta PP-overexpressing cultured human muscle
            fibers
  JOURNAL   Acta Neuropathol 114 (5), 517-526 (2007)
   PUBMED   17764014
  REMARK    GeneRIF: In s-IBM muscle the Nogo-B increase may represent an
            attempt by muscle fiber to decrease A beta production. However, the
            increase of Nogo-B seems insufficient because A beta continues to
            accumulate and the disease progresses.
REFERENCE   9  (residues 1 to 293)
  AUTHORS   Miao,R.Q., Gao,Y., Harrison,K.D., Prendergast,J., Acevedo,L.M.,
            Yu,J., Hu,F., Strittmatter,S.M. and Sessa,W.C.
  TITLE     Identification of a receptor necessary for Nogo-B stimulated
            chemotaxis and morphogenesis of endothelial cells
  JOURNAL   Proc Natl Acad Sci U S A 103 (29), 10997-11002 (2006)
   PUBMED   16835300
  REMARK    GeneRIF: identify a previously uncharacterized Nogo-B receptor
            specific for the amino terminus of Nogo-B
REFERENCE   10 (residues 1 to 293)
  AUTHORS   Josephson,A., Trifunovski,A., Widmer,H.R., Widenfalk,J., Olson,L.
            and Spenger,C.
  TITLE     Nogo-receptor gene activity: cellular localization and
            developmental regulation of mRNA in mice and humans
  JOURNAL   J Comp Neurol 453 (3), 292-304 (2002)
   PUBMED   12378589
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590303.9 and Z98172.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a type I single transmembrane domain
            receptor, which is a subunit of cis-prenyltransferase, and serves
            as a specific receptor for the neural and cardiovascular regulator
            Nogo-B. The encoded protein is essential for dolichol synthesis and
            protein glycosylation. This gene is highly expressed in non-small
            cell lung carcinomas as well as estrogen receptor-alpha positive
            breast cancer cells where it promotes epithelial mesenchymal
            transition. This gene is associated with the poor prognosis of
            human hepatocellular carcinoma patients. Naturally occurring
            mutations in this gene cause a congenital disorder of glycosylation
            and are associated with epilepsy. A knockout of the orthologous
            gene in mice causes embryonic lethality before day 6.5. Pseudogenes
            of this gene have been defined on chromosomes 13 and X. [provided
            by RefSeq, May 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.163431.1,
                                           SRR1660807.136054.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368494.4/ ENSP00000357480.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.1"
     Protein         1..293
                     /product="dehydrodolichyl diphosphate synthase complex
                     subunit NUS1"
                     /EC_number="2.5.1.87"
                     /note="Nogo-B receptor; transport and golgi organization
                     14 homolog; di-trans,poly-cis-decaprenylcistransferase;
                     dehydrodolichyl diphosphate syntase complex subunit NUS1;
                     nuclear undecaprenyl pyrophosphate synthase 1 homolog;
                     cis-prenyltransferase subunit NgBR"
                     /calculated_mol_wt=33093
     Site            1..23
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96E22.1)"
     Site            35..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96E22.1)"
     Site            117..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96E22.1)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21572394; propagated from
                     UniProtKB/Swiss-Prot (Q96E22.1)"
     Region          <196..293
                     /region_name="UppS"
                     /note="Undecaprenyl pyrophosphate synthase [Lipid
                     transport and metabolism]; COG0020"
                     /db_xref="CDD:439791"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21572394; propagated from
                     UniProtKB/Swiss-Prot (Q96E22.1)"
     Region          290..292
                     /region_name="RXG motif, crucial for prenyltransferase
                     activity. /evidence=ECO:0000269|PubMed:32817466,
                     ECO:0000305|PubMed:28842490"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96E22.1)"
     CDS             1..293
                     /gene="NUS1"
                     /gene_synonym="C6orf68; CDG1AA; MGC:7199; MRD55; NgBR;
                     TANGO14"
                     /coded_by="NM_138459.5:203..1084"
                     /db_xref="CCDS:CCDS5118.1"
                     /db_xref="GeneID:116150"
                     /db_xref="HGNC:HGNC:21042"
                     /db_xref="MIM:610463"
ORIGIN      
        1 mtglyelvwr vlhallclhr tltswlrvrf gtwnwiwrrc craasaavla plgftlrkpp
       61 avgrnrrhhr hprggsclaa ahhrmrwrad grsleklpvh mglviteveq epsfsdiasl
      121 vvwcmavgis yisvydhqgi fkrnnsrlmd eilkqqqell gldcskyspe fansndkddq
      181 vlnchlavkv lspedgkadi vraaqdfcql vaqkqkrptd ldvdtlasll ssngcpdpdl
      241 vlkfgpvdst lgflpwhirl teivslpshl nisyedffsa lrqyaaceqr lgk
//
LOCUS       NP_776823                193 aa            linear   MAM 27-APR-2025
DEFINITION  neurocalcin-delta [Bos taurus].
ACCESSION   NP_776823 XP_005215666 XP_872665
VERSION     NP_776823.1
DBSOURCE    REFSEQ: accession NM_174398.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Haynes,L.P., Fitzgerald,D.J., Wareing,B., O'Callaghan,D.W.,
            Morgan,A. and Burgoyne,R.D.
  TITLE     Analysis of the interacting partners of the neuronal
            calcium-binding proteins L-CaBP1, hippocalcin, NCS-1 and
            neurocalcin delta
  JOURNAL   Proteomics 6 (6), 1822-1832 (2006)
   PUBMED   16470652
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Harhay,G.P., Sonstegard,T.S., Keele,J.W., Heaton,M.P.,
            Clawson,M.L., Snelling,W.M., Wiedmann,R.T., Van Tassell,C.P. and
            Smith,T.P.
  TITLE     Characterization of 954 bovine full-CDS cDNA sequences
  JOURNAL   BMC Genomics 6, 166 (2005)
   PUBMED   16305752
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Krishnan,A., Venkataraman,V., Fik-Rymarkiewicz,E., Duda,T. and
            Sharma,R.K.
  TITLE     Structural, biochemical, and functional characterization of the
            calcium sensor neurocalcin delta in the inner retinal neurons and
            its linkage with the rod outer segment membrane guanylate cyclase
            transduction system
  JOURNAL   Biochemistry 43 (10), 2708-2723 (2004)
   PUBMED   15005606
  REMARK    GeneRIF: Neurocalcin delta modulates the Ca2+-modulated membrane
            guanylate cyclase transduction system in the neurons of the retinal
            inner plexiform layer.
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Smith,T.P., Grosse,W.M., Freking,B.A., Roberts,A.J., Stone,R.T.,
            Casas,E., Wray,J.E., White,J., Cho,J., Fahrenkrug,S.C.,
            Bennett,G.L., Heaton,M.P., Laegreid,W.W., Rohrer,G.A.,
            Chitko-McKown,C.G., Pertea,G., Holt,I., Karamycheva,S., Liang,F.,
            Quackenbush,J. and Keele,J.W.
  TITLE     Sequence evaluation of four pooled-tissue normalized bovine cDNA
            libraries and construction of a gene index for cattle
  JOURNAL   Genome Res 11 (4), 626-630 (2001)
   PUBMED   11282978
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Vijay-Kumar,S. and Kumar,V.D.
  TITLE     Crystal structure of recombinant bovine neurocalcin
  JOURNAL   Nat Struct Biol 6 (1), 80-88 (1999)
   PUBMED   9886296
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Kumar,V.D., Hidaka,H., Okazaki,K. and Vijay-Kumar,S.
  TITLE     Crystallization and preliminary X-ray crystallographic studies of
            recombinant bovine neurocalcin delta
  JOURNAL   Proteins 25 (2), 261-264 (1996)
   PUBMED   8811741
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Ladant,D.
  TITLE     Calcium and membrane binding properties of bovine neurocalcin delta
            expressed in Escherichia coli
  JOURNAL   J Biol Chem 270 (7), 3179-3185 (1995)
   PUBMED   7852401
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Hidaka,H. and Okazaki,K.
  TITLE     Neurocalcin family: a novel calcium-binding protein abundant in
            bovine central nervous system
  JOURNAL   Neurosci Res 16 (2), 73-77 (1993)
   PUBMED   8387172
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Okazaki,K., Watanabe,M., Ando,Y., Hagiwara,M., Terasawa,M. and
            Hidaka,H.
  TITLE     Full sequence of neurocalcin, a novel calcium-binding protein
            abundant in central nervous system
  JOURNAL   Biochem Biophys Res Commun 185 (1), 147-153 (1992)
   PUBMED   1599450
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000014.1, EH147775.1, EH153129.1, DT899793.1, DV826731.1,
            EH144443.1 and EH200876.1.
            
            On or before Jan 18, 2018 this sequence version replaced
            XP_005215666.1, XP_872665.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5571258.1102.1,
                                           SRR5571262.22025.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02361203, SAMN03145413
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="14"
                     /map="14"
                     /breed="Hereford"
     Protein         1..193
                     /product="neurocalcin-delta"
                     /calculated_mol_wt=22114
     Region          21..175
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..193
                     /gene="NCALD"
                     /coded_by="NM_174398.3:125..706"
                     /db_xref="BGD:BT25495"
                     /db_xref="GeneID:281940"
                     /db_xref="VGNC:VGNC:31897"
ORIGIN      
        1 mgkqnsklrp evmqdllest dfteheiqew ykgflrdcps ghlsmeefkk iygnffpygd
       61 askfaehvfr tfdangdgti dfrefiials vtsrgkleqk lkwafsmydl dgngyiskae
      121 mleivqaiyk mvssvmkmpe destpekrte kifrqmdtnr dgklsleefi rgaksdpsiv
      181 rllqcdpssa gqf
//
LOCUS       NP_001353127             374 aa            linear   PRI 27-APR-2025
DEFINITION  serpin B8 isoform a [Homo sapiens].
ACCESSION   NP_001353127 XP_024306961
VERSION     NP_001353127.1
DBSOURCE    REFSEQ: accession NM_001366198.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Petersen,M., Lotke,R., Hopfensperger,K., Victoria,S., Haussmann,I.,
            Burster,T., Baldauf,H.M. and Sauter,D.
  TITLE     Inhibition of Infectious HIV-1 Production by Rerouting the Cellular
            Furin Inhibitor Serpin B8
  JOURNAL   J Virol 97 (6), e0029423 (2023)
   PUBMED   37272794
  REMARK    GeneRIF: Inhibition of Infectious HIV-1 Production by Rerouting the
            Cellular Furin Inhibitor Serpin B8.
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Ni,L., Li,P., Li,M., Huang,S. and Dang,N.
  TITLE     SERPINB8 and furin regulate ITGAX expression and affect the
            proliferation and invasion of melanoma cells
  JOURNAL   Exp Dermatol 32 (1), 24-29 (2023)
   PUBMED   36134483
  REMARK    GeneRIF: SERPINB8 and furin regulate ITGAX expression and affect
            the proliferation and invasion of melanoma cells.
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Glavey,S.V., Naba,A., Manier,S., Clauser,K., Tahri,S., Park,J.,
            Reagan,M.R., Moschetta,M., Mishima,Y., Gambella,M., Rocci,A.,
            Sacco,A., O'Dwyer,M.E., Asara,J.M., Palumbo,A., Roccaro,A.M.,
            Hynes,R.O. and Ghobrial,I.M.
  TITLE     Proteomic characterization of human multiple myeloma bone marrow
            extracellular matrix
  JOURNAL   Leukemia 31 (11), 2426-2434 (2017)
   PUBMED   28344315
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Dahlen,J.R., Foster,D.C. and Kisiel,W.
  TITLE     Expression, purification, and inhibitory properties of human
            proteinase inhibitor
  JOURNAL   Biochemistry 36 (48), 14874-14882 (1997)
   PUBMED   9402754
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Bartuski,A.J., Kamachi,Y., Schick,C., Overhauser,J. and
            Silverman,G.A.
  TITLE     Cytoplasmic antiproteinase 2 (PI8) and bomapin (PI10) map to the
            serpin cluster at 18q21.3
  JOURNAL   Genomics 43 (3), 321-328 (1997)
   PUBMED   9268635
REFERENCE   8  (residues 1 to 374)
  AUTHORS   Hubberstey,A., Yu,G., Loewith,R., Lakusta,C. and Young,D.
  TITLE     Mammalian CAP interacts with CAP, CAP2, and actin
  JOURNAL   J Cell Biochem 61 (3), 459-466 (1996)
   PUBMED   8761950
REFERENCE   9  (residues 1 to 374)
  AUTHORS   Sprecher,C.A., Morgenstern,K.A., Mathewes,S., Dahlen,J.R.,
            Schrader,S.K., Foster,D.C. and Kisiel,W.
  TITLE     Molecular cloning, expression, and partial characterization of two
            novel members of the ovalbumin family of serine proteinase
            inhibitors
  JOURNAL   J Biol Chem 270 (50), 29854-29861 (1995)
   PUBMED   8530382
REFERENCE   10 (residues 1 to 374)
  AUTHORS   Huber,R. and Carrell,R.W.
  TITLE     Implications of the three-dimensional structure of alpha
            1-antitrypsin for structure and function of serpins
  JOURNAL   Biochemistry 28 (23), 8951-8966 (1989)
   PUBMED   2690952
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009802.13.
            
            On Sep 26, 2018 this sequence version replaced XP_024306961.1.
            
            Summary: The protein encoded by this gene is a member of the
            ov-serpin family of serine protease inhibitors. The encoded protein
            is produced by platelets and can bind to and inhibit the function
            of furin, a serine protease involved in platelet functions. In
            addition, this protein has been found to enhance the mechanical
            stability of cell-cell adhesion in the skin, and defects in this
            gene have been associated with an autosomal-recessive form of
            exfoliative ichthyosis. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (10) differs in the 5' UTR
            compared to variant 2. Variants 1, 2 and 10 encode the same isoform
            (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138509.9098.1,
                                           SRR5189658.114137.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q22.1"
     Protein         1..374
                     /product="serpin B8 isoform a"
                     /note="protease inhibitor 8 (ovalbumin type); serine (or
                     cysteine) proteinase inhibitor, clade B (ovalbumin),
                     member 8; cytoplasmic antiproteinase 2; serpin B8;
                     peptidase inhibitor 8; serpin peptidase inhibitor, clade B
                     (ovalbumin), member 8"
                     /calculated_mol_wt=42636
     Region          1..374
                     /region_name="serpinB8_CAP-2"
                     /note="serpin family B member 8, cytoplasmic
                     antiproteinase 2; cd19567"
                     /db_xref="CDD:381033"
     Site            322..352
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381033"
     Site            339..340
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P50452.2)"
     CDS             1..374
                     /gene="SERPINB8"
                     /gene_synonym="C18orf53; CAP2; PI-8; PI8; PSS5"
                     /coded_by="NM_001366198.1:179..1303"
                     /note="isoform a is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS11991.1"
                     /db_xref="GeneID:5271"
                     /db_xref="HGNC:HGNC:8952"
                     /db_xref="MIM:601697"
ORIGIN      
        1 mddlceangt faislfkilg eednsrnvff spmsissala mvfmgakgst aaqmsqalcl
       61 ykdgdihrgf qsllsevnrt gtqyllrtan rlfgektcdf lpdfkeycqk fyqaeleels
      121 faedteecrk hindwvaekt egkisevlda gtvdpltklv lvnaiyfkgk wneqfdrkyt
      181 rgmlfktnee kktvqmmfke akfkmgyade vhtqvlelpy veeelsmvil lpddntdlav
      241 vekaltyekf kawtnseklt kskvqvflpr lkleesydle pflrrlgmid afdeakadfs
      301 gmsteknvpl skvahkcfve vneegteaaa atavvrnsrc srmeprfcad hpflffirhh
      361 ktncilfcgr fssp
//
LOCUS       NP_004290                753 aa            linear   PRI 27-APR-2025
DEFINITION  iron-sulfur clusters transporter ABCB7, mitochondrial isoform 1
            [Homo sapiens].
ACCESSION   NP_004290
VERSION     NP_004290.2
DBSOURCE    REFSEQ: accession NM_004299.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Feng,S., Jia,J., Lv,G. and Wang,Y.
  TITLE     Knockdown of ABCB7 inhibits esophageal cancer progression by
            inhibiting the TGF-beta/Smad signaling
  JOURNAL   Arch Biochem Biophys 742, 109620 (2023)
   PUBMED   37142077
  REMARK    GeneRIF: Knockdown of ABCB7 inhibits esophageal cancer progression
            by inhibiting the TGF-beta/Smad signaling.
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Clough,C.A., Pangallo,J., Sarchi,M., Ilagan,J.O., North,K.,
            Bergantinos,R., Stolla,M.C., Naru,J., Nugent,P., Kim,E.,
            Stirewalt,D.L., Subramaniam,A.R., Abdel-Wahab,O., Abkowitz,J.L.,
            Bradley,R.K. and Doulatov,S.
  TITLE     Coordinated missplicing of TMEM14C and ABCB7 causes ring
            sideroblast formation in SF3B1-mutant myelodysplastic syndrome
  JOURNAL   Blood 139 (13), 2038-2049 (2022)
   PUBMED   34861039
  REMARK    GeneRIF: Coordinated missplicing of TMEM14C and ABCB7 causes ring
            sideroblast formation in SF3B1-mutant myelodysplastic syndrome.
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Nie,Z., Yan,Q., Shen,Y. and Yang,X.
  TITLE     Expression, purification and microscopic characterization of human
            ATP-binding cassette sub-family B member 7 protein
  JOURNAL   Protein Expr Purif 183, 105860 (2021)
   PUBMED   33689857
  REMARK    GeneRIF: Expression, purification and microscopic characterization
            of human ATP-binding cassette sub-family B member 7 protein.
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Pearson,S.A. and Cowan,J.A.
  TITLE     Evolution of the human mitochondrial ABCB7 [2Fe-2S](GS)4 cluster
            exporter and the molecular mechanism of an E433K disease-causing
            mutation
  JOURNAL   Arch Biochem Biophys 697, 108661 (2021)
   PUBMED   33157103
  REMARK    GeneRIF: Evolution of the human mitochondrial ABCB7 [2Fe-2S](GS)4
            cluster exporter and the molecular mechanism of an E433K
            disease-causing mutation.
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Csere,P., Lill,R. and Kispal,G.
  TITLE     Identification of a human mitochondrial ABC transporter, the
            functional orthologue of yeast Atm1p
  JOURNAL   FEBS Lett 441 (2), 266-270 (1998)
   PUBMED   9883897
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Shimada,Y., Okuno,S., Kawai,A., Shinomiya,H., Saito,A., Suzuki,M.,
            Omori,Y., Nishino,N., Kanemoto,N., Fujiwara,T., Horie,M. and
            Takahashi,E.
  TITLE     Cloning and chromosomal mapping of a novel ABC transporter gene
            (hABC7), a candidate for X-linked sideroblastic anemia with
            spinocerebellar ataxia
  JOURNAL   J Hum Genet 43 (2), 115-122 (1998)
   PUBMED   9621516
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Savary,S., Allikmets,R., Denizot,F., Luciani,M.F., Mattei,M.G.,
            Dean,M. and Chimini,G.
  TITLE     Isolation and chromosomal mapping of a novel ATP-binding cassette
            transporter conserved in mouse and human
  JOURNAL   Genomics 41 (2), 275-278 (1997)
   PUBMED   9143506
REFERENCE   9  (residues 1 to 753)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
REFERENCE   10 (residues 1 to 753)
  AUTHORS   Bekri,S., D'Hooghe,M. and Vermeersch,P.
  TITLE     X-Linked Sideroblastic Anemia and Ataxia - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK001418.1, AL359545.12 and
            AA403157.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 9, 2004 this sequence version replaced NP_004290.1.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intra-cellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White). This protein is a member of the MDR/TAP subfamily. Members
            of the MDR/TAP subfamily are involved in multidrug resistance as
            well as antigen presentation. This gene encodes a half-transporter
            involved in the transport of heme from the mitochondria to the
            cytosol. With iron/sulfur cluster precursors as its substrates,
            this protein may play a role in metal homeostasis. Mutations in
            this gene have been associated with mitochondrial iron accumulation
            and isodicentric (X)(q13) and sideroblastic anemia. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.578813.1,
                                           SRR14038191.4378710.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.3"
     Protein         1..753
                     /product="iron-sulfur clusters transporter ABCB7,
                     mitochondrial isoform 1"
                     /note="ATP-binding cassette sub-family B member 7,
                     mitochondrial; ABC transporter 7 protein; ATP-binding
                     cassette transporter 7; ATP-binding cassette, sub-family B
                     (MDR/TAP), member 7; iron-sulfur clusters transporter
                     ABCB7, mitochondrial"
                     /calculated_mol_wt=80243
     transit_peptide 1..22
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O75027.2)"
                     /calculated_mol_wt=2545
     Region          126..712
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
     Site            142..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     Site            217
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75027.2)"
     Site            252
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75027.2)"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     Site            292..312
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q704E8; propagated from
                     UniProtKB/Swiss-Prot (O75027.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q704E8; propagated from
                     UniProtKB/Swiss-Prot (O75027.2)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q704E8; propagated from
                     UniProtKB/Swiss-Prot (O75027.2)"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     CDS             1..753
                     /gene="ABCB7"
                     /gene_synonym="ABC7; ASAT; Atm1p; EST140535"
                     /coded_by="NM_004299.6:12..2273"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14428.1"
                     /db_xref="GeneID:22"
                     /db_xref="HGNC:HGNC:48"
                     /db_xref="MIM:300135"
ORIGIN      
        1 mallamhswr waaaaaafek rrhsailirp lvsvsgsgpq wrphqlgalg tarayqqipe
       61 slksitwqrl gkgnsgqfld aakalqvwpl iekrtcwhgh aggglhtdpk eglkdvdtrk
      121 iikamlsyvw pkdrpdlrar vaislgflgg akamnivvpf mfkyavdsln qmsgnmlnls
      181 dapntvatma tavligygvs ragaaffnev rnavfgkvaq nsirriaknv flhlhnldlg
      241 fhlsrqtgal skaidrgtrg isfvlsalvf nllpimfevm lvsgvlyykc gaqfalvtlg
      301 tlgtytaftv avtrwrtrfr iemnkadnda gnaaidslln yetvkyfnne ryeaqrydgf
      361 lktyetaslk ststlamlnf gqsaifsvgl taimvlasqg ivagtltvgd lvmvngllfq
      421 lslplnflgt vyretrqali dmntlftllk vdtqikdkvm asplqitpqt atvafdnvhf
      481 eyiegqkvls gisfevpagk kvaivggsgs gkstivrllf rfyepqkgsi ylagqniqdv
      541 sleslrravg vvpqdavlfh ntiyynllyg nisaspeevy avaklaglhd ailrmphgyd
      601 tqvgerglkl sggekqrvai arailkdppv ilydeatssl dsiteetilg amkdvvkhrt
      661 sifiahrlst vvdadeiivl dqgkvaergt hhgllanphs iysemwhtqs srvqnhdnpk
      721 weakkenisk eeerkklqee ivnsvkgcgn csc
//
LOCUS       NP_001346472            1735 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase MRCK alpha isoform 6 [Mus
            musculus].
ACCESSION   NP_001346472 XP_017175616
VERSION     NP_001346472.1
DBSOURCE    REFSEQ: accession NM_001359543.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1735)
  AUTHORS   Bourdais,A., Dehapiot,B. and Halet,G.
  TITLE     MRCK activates mouse oocyte myosin II for spindle rotation and male
            pronucleus centration
  JOURNAL   J Cell Biol 222 (11) (2023)
   PUBMED   37651121
  REMARK    GeneRIF: MRCK activates mouse oocyte myosin II for spindle rotation
            and male pronucleus centration.
REFERENCE   2  (residues 1 to 1735)
  AUTHORS   Richard,C., Viret,S., Cantero Aguilar,L., Lefevre,C., Leduc,M.,
            Faouzi,E.H., Azar,N., Lavazec,C., Mayeux,P. and Verdier,F.
  TITLE     Myotonic dystrophy kinase-related CDC42-binding kinase alpha, a new
            transferrin receptor type 2-binding partner, is a regulator of
            erythropoiesis
  JOURNAL   Am J Hematol 96 (4), 480-492 (2021)
   PUBMED   33476437
  REMARK    GeneRIF: Myotonic dystrophy kinase-related CDC42-binding kinase
            alpha, a new transferrin receptor type 2-binding partner, is a
            regulator of erythropoiesis.
REFERENCE   3  (residues 1 to 1735)
  AUTHORS   Nakano,Y., Wiechert,S. and Banfi,B.
  TITLE     Overlapping Activities of Two Neuronal Splicing Factors Switch the
            GABA Effect from Excitatory to Inhibitory by Regulating REST
  JOURNAL   Cell Rep 27 (3), 860-871 (2019)
   PUBMED   30995482
REFERENCE   4  (residues 1 to 1735)
  AUTHORS   Dobrowolski,S.F., Lyons-Weiler,J., Spridik,K., Vockley,J.,
            Skvorak,K. and Biery,A.
  TITLE     DNA methylation in the pathophysiology of hyperphenylalaninemia in
            the PAH(enu2) mouse model of phenylketonuria
  JOURNAL   Mol Genet Metab 119 (1-2), 1-7 (2016)
   PUBMED   26822703
REFERENCE   5  (residues 1 to 1735)
  AUTHORS   Lee,I.C.J., Leung,T. and Tan,I.
  TITLE     Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related
            Cdc42-binding kinase (MRCK) regulation of LIMK1 protein in
            lamellipodial F-actin dynamics
  JOURNAL   J Biol Chem 289 (39), 26989-27003 (2014)
   PUBMED   25107909
REFERENCE   6  (residues 1 to 1735)
  AUTHORS   Osipovich,A.B., Long,Q., Manduchi,E., Gangula,R., Hipkens,S.B.,
            Schneider,J., Okubo,T., Stoeckert,C.J. Jr., Takada,S. and
            Magnuson,M.A.
  TITLE     Insm1 promotes endocrine cell differentiation by modulating the
            expression of a network of genes that includes Neurog3 and Ripply3
  JOURNAL   Development 141 (15), 2939-2949 (2014)
   PUBMED   25053427
REFERENCE   7  (residues 1 to 1735)
  AUTHORS   Gomes,E.R., Jani,S. and Gundersen,G.G.
  TITLE     Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow
            establishes MTOC polarization in migrating cells
  JOURNAL   Cell 121 (3), 451-463 (2005)
   PUBMED   15882626
REFERENCE   8  (residues 1 to 1735)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125380.4 and AC132436.3.
            
            On Jan 13, 2018 this sequence version replaced XP_017175616.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660813.239198.1,
                                           SRR1660821.46787.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1735
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 84.01 cM"
     Protein         1..1735
                     /product="serine/threonine-protein kinase MRCK alpha
                     isoform 6"
                     /EC_number="2.7.11.1"
                     /note="myotonic dystrophy kinase-related CDC-42-binding
                     kinase-alpha; serine/threonine-protein kinase MRCK alpha"
                     /calculated_mol_wt=197076
     Region          4..412
                     /region_name="STKc_MRCK_alpha"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     DMPK-related cell division control protein 42 binding
                     kinase (MRCK) alpha; cd05623"
                     /db_xref="CDD:270773"
     Site            order(6..7,10..11,14..15,26,28,30..31,34..35,38,47,52..53,
                     56,59,63,69..73,76,96,101,114,142,394,397..398,400,
                     407..410)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270773"
     Site            order(83..87,91,104,106,138,154..155,157,161,163,201,203,
                     205..206,208,218..219,222,237..242,274,280,283)
                     /site_type="active"
                     /db_xref="CDD:270773"
     Site            order(83..87,91,104,106,138,155..157,161,201,203,205..206,
                     208,218..219)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270773"
     Site            order(87,161,163,201,203,205,222,237..242,274,280,283)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270773"
     Site            218..242
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270773"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            399..404
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270773"
     Region          <438..824
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            478..479
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3 in vitro.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Region          529..608
                     /region_name="KELK"
                     /note="KELK-motif containing domain of MRCK Ser/Thr
                     protein kinase; pfam15796"
                     /db_xref="CDD:464876"
     Region          881..941
                     /region_name="DMPK_coil"
                     /note="DMPK coiled coil domain like; pfam08826"
                     /db_xref="CDD:117396"
     Region          1014..1073
                     /region_name="C1_MRCKalpha"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in myotonic dystrophy kinase-related Cdc42-binding
                     kinase alpha (MRCK alpha) and similar proteins; cd20864"
                     /db_xref="CDD:410414"
     Site            order(1021..1027,1035..1039,1042)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410414"
     Region          1075..1209
                     /region_name="PH_MRCK"
                     /note="MRCK (myotonic dystrophy-related Cdc42-binding
                     kinase) pleckstrin homology (PH) domain; cd01243"
                     /db_xref="CDD:269949"
     Region          1240..1498
                     /region_name="CNH"
                     /note="CNH domain; pfam00780"
                     /db_xref="CDD:459938"
     Site            1548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Region          1595..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1654
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1724
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     CDS             1..1735
                     /gene="Cdc42bpa"
                     /gene_synonym="A930014J19Rik; DMPK-like"
                     /coded_by="NM_001359543.1:351..5558"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:226751"
                     /db_xref="MGI:MGI:2441841"
ORIGIN      
        1 msgevrlrql eqfildgpaq tngqcfsvet lldiliclyd ecnnsplrre knileylewa
       61 kpftskvkqm rlhredfeil kvigrgafge vavvklknad kvfamkilnk wemlkraeta
      121 cfreerdvlv ngdskwittl hyafqddnnl ylvmdyyvgg dlltllskfe drlpeemarf
      181 ylaemviaid svhqlhyvhr dikpdnilmd mnghirladf gsclklmedg tvqssvavgt
      241 pdyispeilq amedgkgryg pecdwwslgv cmyemlyget pfyaeslvet ygkimnhker
      301 fqfpaqvtdv senakdlirr licsrehrlg qngiedfkkh pffsgidwdn irnceapyip
      361 evssptdtsn fdvdddclkn setmppptht afsghhlpfv gftytsscvl sdrsclrvta
      421 gptsldldvs vqrtldnnla teayerrikr leqekleltr klqestqtvq alqystvdgp
      481 ltaskdleik slkeeieklr kqvaevnhle qqleeansvr relddafrqi kasekqiktl
      541 qqereelnke lvqaserlkn qskelkdahc qrklamqefm einerltelh tqkqklarhv
      601 rdkeeevdlv mqkaeslrqe lrraerakke levhtealia easkdkklre qsehyskqle
      661 neleglkqkq isyspgicsi ehqqeitklk tdlekksify eeeiskregi haseiknlkk
      721 elhdsegqql alnkeilvlk dklektrres qsereefene fkqqyerekv llteenkklt
      781 seldkltsly eslslrnqhl eeevkdladk kesvahweaq iteiiqwvsd ekdargylqa
      841 laskmteele alrnsslgtr atdmpwkmrr fakldmsarl elqsaldaei rakqaiqeel
      901 nkvkasnilt ecklkdsekk nlellseieq likdteelrs ekgiehqdsq hsflaflntp
      961 tdaldqfeds lsssssslid flddiadcap lpahtptlrk kgcpastgfp pkrkthqffv
     1021 ksftaptkch qctslmvgli rqgcscevcg fschitcvnk aptvcpvppe qtkgplgidp
     1081 qkgvgtayeg hvripkpagv kkgwqralav vcdfklflyd iaegkasqpt svisqvidmr
     1141 deefsvssvl asdvihasrk dipcifrvta sqlsapsnkc silmladsen erskwvgvls
     1201 elhkilkknk frdrsvyvpk eaydstlpli kttqaaaiid herialgnee glfvvhvtkd
     1261 eivrvgdnkk ihqielipsd qlvavisgrn rhvrlfpmsa ldgretdfyk laetkgcqti
     1321 aagkvrhgal sclcvamkrq vlcyelfqsk trhrkfkeiq vpcnvqwmai fsehlcvgfq
     1381 sgflryplng eggpcnmlhs ndhtlsfish qpmdalcave isnkeyllcf nsigiytdcq
     1441 grrsrqqelm wpanpssccy napylsvyse navdifdvns mewiqtlplk kvrplntegs
     1501 lnllgletir liyfknkmae gdelvvpets dnsrkqmvrn innkrrysfr vpeeermqqr
     1561 remlrdpemr nklisnptnf nhiahmgpgd giqilkdlpm nprpqesrtv fsgsvsipsi
     1621 tksrpepgrs msassglsar ssaqngsalk refsggsynt krqpmpspse gslssggmdq
     1681 gsdapardyd gedsdsprhs tasnssnlss ppspispqkt kslslestdr gswdp
//
LOCUS       NP_001356020             360 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001356020 XP_011538144
VERSION     NP_001356020.1
DBSOURCE    REFSEQ: accession NM_001369091.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            On Mar 18, 2019 this sequence version replaced XP_011538144.1.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.124506.1,
                                           SRR1803611.175034.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..360
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 6"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=40919
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..321
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..360
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369091.1:209..1291"
                     /note="isoform 6 is encoded by transcript variant 12"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilks fallprleyn daisahcnlc lpgssdspas asqvagitvv
//
LOCUS       NP_689996                521 aa            linear   PRI 27-APR-2025
DEFINITION  D-2-hydroxyglutarate dehydrogenase, mitochondrial isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_689996 XP_001130341 XP_001130367
VERSION     NP_689996.4
DBSOURCE    REFSEQ: accession NM_152783.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Hayashi,C., Takagi,K., Sato,A., Yamaguchi,M., Minemura,H., Miki,Y.,
            Harada-Shoji,N., Miyashita,M., Sasano,H. and Suzuki,T.
  TITLE     D-2-hydroxyglutarate dehydrogenase in breast carcinoma as a potent
            prognostic marker associated with proliferation
  JOURNAL   Histol Histopathol 36 (10), 1053-1062 (2021)
   PUBMED   34296423
  REMARK    GeneRIF: D-2-hydroxyglutarate dehydrogenase in breast carcinoma as
            a potent prognostic marker associated with proliferation.
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Yang,J., Zhu,H., Zhang,T. and Ding,J.
  TITLE     Structure, substrate specificity, and catalytic mechanism of human
            D-2-HGDH and insights into pathogenicity of disease-associated
            mutations
  JOURNAL   Cell Discov 7 (1), 3 (2021)
   PUBMED   33431826
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Eckel-Passow,J.E., Drucker,K.L., Kollmeyer,T.M., Kosel,M.L.,
            Decker,P.A., Molinaro,A.M., Rice,T., Praska,C.E., Clark,L.,
            Caron,A., Abyzov,A., Batzler,A., Song,J.S., Pekmezci,M.,
            Hansen,H.M., McCoy,L.S., Bracci,P.M., Wiemels,J., Wiencke,J.K.,
            Francis,S., Burns,T.C., Giannini,C., Lachance,D.H., Wrensch,M. and
            Jenkins,R.B.
  TITLE     Adult diffuse glioma GWAS by molecular subtype identifies variants
            in D2HGDH and FAM20C
  JOURNAL   Neuro Oncol 22 (11), 1602-1613 (2020)
   PUBMED   32386320
  REMARK    GeneRIF: Adult diffuse glioma GWAS by molecular subtype identifies
            variants in D2HGDH and FAM20C.
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Qiu,Z., Lin,A.P., Jiang,S., Elkashef,S.M., Myers,J., Srikantan,S.,
            Sasi,B., Cao,J.Z., Godley,L.A., Rakheja,D., Lyu,Y., Zheng,S.,
            Madesh,M., Shiio,Y., Dahia,P.L.M. and Aguiar,R.C.T.
  TITLE     MYC Regulation of D2HGDH and L2HGDH Influences the Epigenome and
            Epitranscriptome
  JOURNAL   Cell Chem Biol 27 (5), 538-550 (2020)
   PUBMED   32101699
  REMARK    GeneRIF: MYC Regulation of D2HGDH and L2HGDH Influences the
            Epigenome and Epitranscriptome.
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Struys,E.A., Korman,S.H., Salomons,G.S., Darmin,P.S., Achouri,Y.,
            van Schaftingen,E., Verhoeven,N.M. and Jakobs,C.
  TITLE     Mutations in phenotypically mild D-2-hydroxyglutaric aciduria
  JOURNAL   Ann Neurol 58 (4), 626-630 (2005)
   PUBMED   16037974
  REMARK    GeneRIF: Two novel pathogenic mutations in D-2-hydroxyglutarate
            dehydrogenase gene in patient with a mild presentation and
            asymptomatic siblings with D-2-hydroxyglutaric aciduria with a
            splice error (IVS4-2A-->G) and a missense mutation
            (c.1315A-->G;p.Asn439Asp).
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Struys,E.A., Salomons,G.S., Achouri,Y., Van Schaftingen,E.,
            Grosso,S., Craigen,W.J., Verhoeven,N.M. and Jakobs,C.
  TITLE     Mutations in the D-2-hydroxyglutarate dehydrogenase gene cause
            D-2-hydroxyglutaric aciduria
  JOURNAL   Am J Hum Genet 76 (2), 358-360 (2005)
   PUBMED   15609246
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Achouri,Y., Noel,G., Vertommen,D., Rider,M.H., Veiga-Da-Cunha,M.
            and Van Schaftingen,E.
  TITLE     Identification of a dehydrogenase acting on D-2-hydroxyglutarate
  JOURNAL   Biochem J 381 (Pt 1), 35-42 (2004)
   PUBMED   15070399
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Gibson,K.M., Craigen,W., Herman,G.E. and Jakobs,C.
  TITLE     D-2-hydroxyglutaric aciduria in a newborn with neurological
            abnormalities: a new neurometabolic disorder?
  JOURNAL   J Inherit Metab Dis 16 (3), 497-500 (1993)
   PUBMED   7609436
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK304764.1, AK304773.1, BC036604.2, BC071598.1 and BC031817.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Dec 28, 2006 this sequence version replaced
            XP_001130341.1, XP_001130367.1, NP_689996.3.
            
            Summary: This gene encodes D-2hydroxyglutarate dehydrogenase, a
            mitochondrial enzyme belonging to the FAD-binding
            oxidoreductase/transferase type 4 family. This enzyme, which is
            most active in liver and kidney but also active in heart and brain,
            converts D-2-hydroxyglutarate to 2-ketoglutarate. Mutations in this
            gene are present in D-2-hydroxyglutaric aciduria, a rare recessive
            neurometabolic disorder causing developmental delay, epilepsy,
            hypotonia, and dysmorphic features. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.621863.1,
                                           SRR3476690.1161830.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000321264.9/
                                                  ENSP00000315351.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..521
                     /product="D-2-hydroxyglutarate dehydrogenase,
                     mitochondrial isoform 1 precursor"
                     /EC_number="1.1.99.39"
                     /note="D-2-hydroxyglutarate dehydrogenase, mitochondrial"
                     /calculated_mol_wt=54827
     transit_peptide 1..13
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q8N465.3)"
                     /calculated_mol_wt=1607
     mat_peptide     14..521
                     /product="D-2-hydroxyglutarate dehydrogenase,
                     mitochondrial. /id=PRO_0000231674"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N465.3)"
                     /calculated_mol_wt=54827
     Region          62..518
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     CDS             1..521
                     /gene="D2HGDH"
                     /gene_synonym="D2HGD"
                     /coded_by="NM_152783.5:159..1724"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS33426.1"
                     /db_xref="GeneID:728294"
                     /db_xref="HGNC:HGNC:28358"
                     /db_xref="MIM:609186"
ORIGIN      
        1 mlprrplawp awllrgapga agswgrpvgp larrgccsap gtpevpltre rypvrrlpfs
       61 tvskqdlaaf erivpggvvt dpealqapnv dwlrtlrgcs kvllrprtse evshilrhch
      121 ernlavnpqg gntgmvggsv pvfdeiilst armnrvlsfh svsgilvcqa gcvleelsry
      181 veerdfimpl dlgakgschi ggnvatnagg lrflrygslh gtvlglevvl adgtvldclt
      241 slrkdntgyd lkqlfigseg tlgiittvsi lcppkpravn vaflgcpgfa evlqtfstck
      301 gmlgeilsaf efmdavcmql vgrhlhlasp vqespfyvli etsgsnaghd aeklghfleh
      361 algsglvtdg tmatdqrkvk mlwalrerit ealsrdgyvy kydlslpver lydivtdlra
      421 rlgphakhvv gyghlgdgnl hlnvtaeafs psllaaleph vyewtagqqg svsaehgvgf
      481 rkrdvlgysk ppgalqlmqq lkalldpkgi lnpyktlpsq a
//
LOCUS       NP_542194               1661 aa            linear   PRI 27-APR-2025
DEFINITION  microtubule cross-linking factor 2 isoform 1 [Homo sapiens].
ACCESSION   NP_542194
VERSION     NP_542194.2
DBSOURCE    REFSEQ: accession NM_080627.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1661)
  AUTHORS   Li,J., Yang,F., Wang,Z., Zheng,S., Zhang,S., Wang,C., He,B.,
            Wang,J.B. and Wang,H.
  TITLE     METTL16-mediated N6-methyladenosine modification of Soga1 enables
            proper chromosome segregation and chromosomal stability in
            colorectal cancer
  JOURNAL   Cell Prolif 57 (5), e13590 (2024)
   PUBMED   38084791
  REMARK    GeneRIF: METTL16-mediated N6-methyladenosine modification of Soga1
            enables proper chromosome segregation and chromosomal stability in
            colorectal cancer.
REFERENCE   2  (residues 1 to 1661)
  AUTHORS   Matsuoka,R., Miki,M., Mizuno,S., Ito,Y., Yamada,C. and Suzuki,A.
  TITLE     MTCL2 promotes asymmetric microtubule organization by crosslinking
            microtubules on the Golgi membrane
  JOURNAL   J Cell Sci 135 (11) (2022)
   PUBMED   35543016
REFERENCE   3  (residues 1 to 1661)
  AUTHORS   Ferreira,L.T., Logarinho,E., Macedo,J.C., Maia,A.R.R. and Maiato,H.
  TITLE     SOGA1 and SOGA2/MTCL1 are CLASP-interacting proteins required for
            faithful chromosome segregation in human cells
  JOURNAL   Chromosome Res 29 (2), 159-173 (2021)
   PUBMED   33587225
  REMARK    GeneRIF: SOGA1 and SOGA2/MTCL1 are CLASP-interacting proteins
            required for faithful chromosome segregation in human cells.
REFERENCE   4  (residues 1 to 1661)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1661)
  AUTHORS   Habieb,A., Matboli,M., El-Tayeb,H. and El-Asmar,F.
  TITLE     Potential role of lncRNA-TSIX, miR-548-a-3p, and SOGA1 mRNA in the
            diagnosis of hepatocellular carcinoma
  JOURNAL   Mol Biol Rep 46 (4), 4581-4590 (2019)
   PUBMED   31004302
  REMARK    GeneRIF: Authors selected an HCC-specific RNA-based biomarker panel
            that depended on the integration of suppressor of glucose
            autophagy-associated (SOGA1) gene expression with the chosen panel
            of epigenetic regulators of this gene [long non-coding RNA
            antisense for X-inactive-specific transcript (lncRNA-TSIX) and
            microRNA-548-a-3p (miR-548-a-3p)].
            Erratum:[Mol Biol Rep. 2019 Aug;46(4):4591. doi:
            10.1007/s11033-019-04838-z. PMID: 31049832]
REFERENCE   6  (residues 1 to 1661)
  AUTHORS   Kruse,R., Krantz,J., Barker,N., Coletta,R.L., Rafikov,R., Luo,M.,
            Hojlund,K., Mandarino,L.J. and Langlais,P.R.
  TITLE     Characterization of the CLASP2 Protein Interaction Network
            Identifies SOGA1 as a Microtubule-Associated Protein
  JOURNAL   Mol Cell Proteomics 16 (10), 1718-1735 (2017)
   PUBMED   28550165
REFERENCE   7  (residues 1 to 1661)
  AUTHORS   Cowherd,R.B., Asmar,M.M., Alderman,J.M., Alderman,E.A.,
            Garland,A.L., Busby,W.H., Bodnar,W.M., Rusyn,I., Medoff,B.D.,
            Tisch,R., Mayer-Davis,E., Swenberg,J.A., Zeisel,S.H. and Combs,T.P.
  TITLE     Adiponectin lowers glucose production by increasing SOGA
  JOURNAL   Am J Pathol 177 (4), 1936-1945 (2010)
   PUBMED   20813965
  REMARK    Erratum:[Am J Pathol. 2011 Mar;178(3):1406. Cowerd, Rachael B
            [corrected to Cowherd, Rachael B]]
REFERENCE   8  (residues 1 to 1661)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 1661)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL079335.29, AL391602.6, AL132768.15 and BQ027014.1.
            
            On Sep 9, 2009 this sequence version replaced NP_542194.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000237536.9/ ENSP00000237536.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1661
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.23"
     Protein         1..1661
                     /product="microtubule cross-linking factor 2 isoform 1"
                     /note="suppressor of glucose by autophagy; microtubule
                     cross-linking factor 2; suppressor of glucose, autophagy
                     associated 1; suppressor of glucose from autophagy; SOGA
                     family member 1; suppressor of glucose,
                     autophagy-associated protein 1; protein SOGA1"
                     /calculated_mol_wt=183728
     Region          1..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94964.3)"
     Region          <33..>179
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          211..240
                     /region_name="Required for association with Golgi
                     apparatus membrane.
                     /evidence=ECO:0000250|UniProtKB:E1U8D0"
                     /note="propagated from UniProtKB/Swiss-Prot (O94964.3)"
     Region          253..>550
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          353..373
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94964.3)"
     Region          380..474
                     /region_name="SOGA"
                     /note="Protein SOGA; pfam11365"
                     /db_xref="CDD:463264"
     Region          508..597
                     /region_name="SOGA"
                     /note="Protein SOGA; pfam11365"
                     /db_xref="CDD:463264"
     Site            926..927
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250|UniProtKB:E1U8D0;
                     propagated from UniProtKB/Swiss-Prot (O94964.3)"
     Region          <1002..>1119
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
     Region          1069..1207
                     /region_name="DUF4482"
                     /note="Domain of unknown function (DUF4482); pfam14818"
                     /db_xref="CDD:464333"
     Site            1169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O94964.3)"
     Region          1196..1221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94964.3)"
     Site            1255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94964.3)"
     Region          1432..1456
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94964.3)"
     Region          1538..1563
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94964.3)"
     Region          1636..1661
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94964.3)"
     CDS             1..1661
                     /gene="MTCL2"
                     /gene_synonym="C20orf117; KIAA0889; SOGA; SOGA1"
                     /coded_by="NM_080627.4:195..5180"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54459.1"
                     /db_xref="GeneID:140710"
                     /db_xref="HGNC:HGNC:16111"
                     /db_xref="MIM:620225"
ORIGIN      
        1 meapaaeppv rgcgpqpapa papaperkks hrapsparpk dvagwslakg rrgpgpgsav
       61 acsaafssrp dkkgravapg argagvrvag vrtgvrakgr prsgagprpp ppppsltdss
      121 sevsdcasee arllglelal ssdaesaagg pagvrtgqpa qpapsaqqpp rppaspdeps
      181 vaassvgssr lplsaslafs dlteemldcg psglvrelee lrsendylkd eieelraeml
      241 emrdvymeed vyqlqelrqq ldqasktcri lqyrlrkaer rslraaqtgq vdgelirgle
      301 qdvkvskdis mrlhkelevv ekkrarleee neelrqrlie telakqvlqt elerprehsl
      361 kkrgtrslgk adkktlvqed sadlkcqlhf akeesalmck kltklakend smkeellkyr
      421 slygdldsal saeeladaph sretelkvhl klveeeanll srriveleve nrglraemdd
      481 mkdhgggcgg pearlafsal gggecgesla elrrhlqfve eeaellrrss aeledqnkll
      541 lnelakfrse heldvalsed scsvlsepsq eelaaaklqi gelsgkvkkl qyenrvllsn
      601 lqrcdlascq strpmletda eagdsaqcvp aplgethesh avrlcrarea evlpglreqa
      661 alvskaidvl vadangftag lrlcldneca dfrlheapdn segprdtkli hailvrlsvl
      721 qqelnaftrk adavlgcsvk eqqesfsslp plgsqglske illakdlgsd fqppdfrdlp
      781 eweprireaf rtgdldskpd psrsfrpyra edndsyasei kelqlvlaea hdslrglqeq
      841 lsqerqlrke eadnfnqkmv qlkedqqral lrrefelqsl slqrrleqkf wsqeknmlvq
      901 esqqfkhnfl llfmklrwfl krwrqgkvlp segddflevn smkelyllme eeeinaqhsd
      961 nkactgdswt qntpneyikt ladmkvtlke lcwllrderr gltelqqqfa kakatweter
     1021 aelkghtsqm elktgkgage ragpdwkaal qrereeqqhl laesysavme ltrqlqiser
     1081 nwsqeklqlv erlqgekqqv eqqvkelqnr lsqlqkaadp wvlkhselek qdnswketrs
     1141 ekihdkeavs evelggnglk rtksvssmse feslldcspy laggdargkk lpnnpafgfv
     1201 ssepgdpekd tkekpglssr dcnhlgalac qdppgrqmqr sytapdktgi rvyysppvar
     1261 rlgvpvvhdk egkiiiepgf lfttakpkes aeadglaess ygrwlcnfsr qrldggsags
     1321 psaagpgfpa alhdfemsgn msddmkeitn cvrqamrsgs lerkvkstss qtvglasvgt
     1381 qtirtvsvgl qtdpprsslh gkawsprsss lvsvrskqis ssldkvhsri erpccspkyg
     1441 spklqrrsvs kldsskdrsl wnlhqgkqng sawarstttr dspvlrnind glsslfsvve
     1501 hsgstesvwk lgmsetrakp eppkygivqe ffrnvcgrap sptssageeg tkkpeplspa
     1561 syhqpegvar ilnkkaaklg sseevrltml pqvgkdgvlr dgdgavvlpn edavcdcstq
     1621 sltscfarss rsairhspsk crlhpsessw ggeeralpps e
//
LOCUS       NP_060427                632 aa            linear   PRI 27-APR-2025
DEFINITION  epsin-3 [Homo sapiens].
ACCESSION   NP_060427
VERSION     NP_060427.2
DBSOURCE    REFSEQ: accession NM_017957.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Li,Y., Zhang,P., Tang,G., Zhong,J., Wang,Z. and Zhu,B.
  TITLE     Lowering expression of Epsin-3 inhibits migration and invasion of
            lung adenocarcinoma cells by inhibiting the epithelial-mesenchymal
            transition
  JOURNAL   Sci Rep 14 (1), 17069 (2024)
   PUBMED   39048677
  REMARK    GeneRIF: Lowering expression of Epsin-3 inhibits migration and
            invasion of lung adenocarcinoma cells by inhibiting the
            epithelial-mesenchymal transition.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Ahmed,H., Paterson,I., Aziz,S.A., Cremona,O., Robinson,M.,
            Carrozzo,M. and Valentine,R.A.
  TITLE     Expression of Epsin3 and its interaction with Notch signalling in
            oral epithelial dysplasia and oral squamous cell carcinoma
  JOURNAL   J Oral Pathol Med 52 (8), 710-717 (2023)
   PUBMED   37339783
  REMARK    GeneRIF: Expression of Epsin3 and its interaction with Notch
            signalling in oral epithelial dysplasia and oral squamous cell
            carcinoma.
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Meng,J., Zhang,C., Zhu,N., Zhang,C., Liu,M., Han,Z. and Li,Y.
  TITLE     EPN3 plays oncogenic role in non-small cell lung cancer by
            activating the JAK1/2-STAT3 pathway
  JOURNAL   Environ Toxicol 38 (8), 1968-1979 (2023)
   PUBMED   37186036
  REMARK    GeneRIF: EPN3 plays oncogenic role in non-small cell lung cancer by
            activating the JAK1/2-STAT3 pathway.
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Wang,Y., Song,W., Kan,P., Huang,C., Ma,Z., Wu,Q., Yao,X. and
            Zhang,B.
  TITLE     Overexpression of Epsin 3 enhances migration and invasion of glioma
            cells by inducing epithelial-mesenchymal transition
  JOURNAL   Oncol Rep 40 (5), 3049-3059 (2018)
   PUBMED   30226603
  REMARK    GeneRIF: These results suggested that EPN3 enhances the migration
            and invasion of glioblastoma cells by activating the transcription
            factors Slug, Twist and ZEB1, but not Snail 1 or ZEB2, to induce
            EMT in glioma cells; EPN3 involvement in the Notch and
            WNT/betacatenin signaling pathways may contribute to this process.
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Hellwig,B., Madjar,K., Edlund,K., Marchan,R., Cadenas,C.,
            Heimes,A.S., Almstedt,K., Lebrecht,A., Sicking,I., Battista,M.J.,
            Micke,P., Schmidt,M., Hengstler,J.G. and Rahnenfuhrer,J.
  TITLE     Epsin Family Member 3 and Ribosome-Related Genes Are Associated
            with Late Metastasis in Estrogen Receptor-Positive Breast Cancer
            and Long-Term Survival in Non-Small Cell Lung Cancer Using a
            Genome-Wide Identification and Validation Strategy
  JOURNAL   PLoS One 11 (12), e0167585 (2016)
   PUBMED   27926932
  REMARK    GeneRIF: High expression of epsin (EPN3) was associated with
            increased risk of late metastasis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 632)
  AUTHORS   Coon,B.G., Burgner,J., Camonis,J.H. and Aguilar,R.C.
  TITLE     The epsin family of endocytic adaptors promotes fibrosarcoma
            migration and invasion
  JOURNAL   J Biol Chem 285 (43), 33073-33081 (2010)
   PUBMED   20709745
REFERENCE   7  (residues 1 to 632)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 632)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   9  (residues 1 to 632)
  AUTHORS   Spradling,K.D., McDaniel,A.E., Lohi,J. and Pilcher,B.K.
  TITLE     Epsin 3 is a novel extracellular matrix-induced transcript specific
            to wounded epithelia
  JOURNAL   J Biol Chem 276 (31), 29257-29267 (2001)
   PUBMED   11359770
REFERENCE   10 (residues 1 to 632)
  AUTHORS   Spradling,K.D., Burke,T.J., Lohi,J. and Pilcher,B.K.
  TITLE     Cloning and initial characterization of human epsin 3, a novel
            matrix-induced keratinocyte specific transcript
  JOURNAL   J Invest Dermatol 115 (2), 332 (2000)
   PUBMED   10951261
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC388544.1, AK000785.1, DA392550.1, AF324241.1, BM981734.1,
            BU539570.1 and CA944655.1.
            
            On Sep 20, 2007 this sequence version replaced NP_060427.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000785.1, AK292977.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268933.8/ ENSP00000268933.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..632
                     /product="epsin-3"
                     /note="EPS-15-interacting protein 3"
                     /calculated_mol_wt=68091
     Region          19..142
                     /region_name="ENTH_Epsin"
                     /note="Epsin N-Terminal Homology (ENTH) domain of Epsin
                     family; cd16990"
                     /db_xref="CDD:340787"
     Site            order(25,29..30,63,69,73)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:340787"
     Region          172..214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H201.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91W69; propagated from
                     UniProtKB/Swiss-Prot (Q9H201.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91W69; propagated from
                     UniProtKB/Swiss-Prot (Q9H201.1)"
     Region          209..228
                     /region_name="UIM"
                     /note="Ubiquitin-interacting motif; smart00726"
                     /db_xref="CDD:197845"
     Region          236..255
                     /region_name="UIM"
                     /note="Ubiquitin-interacting motif; smart00726"
                     /db_xref="CDD:197845"
     Region          257..296
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H201.1)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91W69; propagated from
                     UniProtKB/Swiss-Prot (Q9H201.1)"
     Region          321..406
                     /region_name="5 X 3 AA repeats of [DE]-P-W"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H201.1)"
     Region          326..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H201.1)"
     Region          <347..630
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          524..631
                     /region_name="3 X 3 AA repeats of N-P-F"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H201.1)"
     Region          525..560
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H201.1)"
     Region          604..632
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H201.1)"
     CDS             1..632
                     /gene="EPN3"
                     /coded_by="NM_017957.3:388..2286"
                     /db_xref="CCDS:CCDS11570.1"
                     /db_xref="GeneID:55040"
                     /db_xref="HGNC:HGNC:18235"
                     /db_xref="MIM:607264"
ORIGIN      
        1 mttsalrrqv knivhnysea eikvreatsn dpwgppsslm seiadltfnt vaftevmgml
       61 wrrlndsgkn wrhvykaltl ldyllktgse rvahqcrenl ytiqtlkdfq yidrdgkdqg
      121 vnvrekvkqv mallkdeerl rqerthalkt kermalegig igsgqlgfsr rygedysrsr
      181 gspssynsss ssprytsdle qarpqtsgee elqlqlalam sreeaekpvp pashrdedlq
      241 lqlalrlsrq ehekevrswq gdgspmanga gavvhhqrdr epereerkee eklktsqssi
      301 ldladifvpa lappsthcsa dpwdipgfrp nteasgsswg psadpwspip sgtvlsrsqp
      361 wdltpmlsss epwgrtpvlp agppttdpwa lnsphhklps tgadpwgasl etsdtpggas
      421 tfdpfakppe stetkegleq alpsgkpssp veldlfgdps psskqngtke pdaldlgilg
      481 ealtqpskea racrtpesfl gpsasslvnl dslvkapqva ktrnpfltgl sapsptnpfg
      541 agepgrptln qmrtgspalg laggpvgapl gsmtysaslp lplssvpagl tlpasvsvfp
      601 qagafapqpl lptpssagpr ppppqtgtnp fl
//
LOCUS       NP_078924                319 aa            linear   PRI 27-APR-2025
DEFINITION  2-oxoglutarate and iron-dependent oxygenase domain-containing
            protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_078924 XP_946504
VERSION     NP_078924.1
DBSOURCE    REFSEQ: accession NM_024648.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK025875.1 and AC132938.9.
            
            On Mar 4, 2006 this sequence version replaced XP_946504.1.
            
            Transcript Variant: This variant (1) encodes isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK025875.1, SRR1163655.604250.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313056.10/ ENSP00000320116.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..319
                     /product="2-oxoglutarate and iron-dependent oxygenase
                     domain-containing protein 3 isoform 1"
                     /note="PKHD domain-containing transmembrane protein
                     C17orf101; 2-oxoglutarate and iron-dependent oxygenase
                     domain-containing protein 3"
                     /calculated_mol_wt=35515
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PK18.2)"
     Site            43..65
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PK18.2)"
     Region          162..305
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     Site            215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PK18.2)"
     CDS             1..319
                     /gene="OGFOD3"
                     /gene_synonym="C17orf101"
                     /coded_by="NM_024648.3:102..1061"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11811.1"
                     /db_xref="GeneID:79701"
                     /db_xref="HGNC:HGNC:26174"
ORIGIN      
        1 mapqrraatk apegngaaer rnrsstkkdr aprevqrlwq rpwlrtaglg agfvltalll
       61 wsslgaddgv aevlarrgev vagrfievpc sedydshrrf egctprkcgr gvtdvvitre
      121 eaerirsvae kglslggsdg gasildlhsg alsvgkhfvn lyryfgdkiq nifseedfrl
      181 yrevrqkvql tiaeafgisa sslhltkptf fsrinstear tahdeywhah vdkvtygsfd
      241 ytsllylsny ledfgggrfm fmeeganktv epragrvsff tsgsenlhrv ekvhwgtrya
      301 itiafscnpd hgiedpafp
//
LOCUS       NP_115879                100 aa            linear   PRI 27-APR-2025
DEFINITION  EKC/KEOPS complex subunit GON7 [Homo sapiens].
ACCESSION   NP_115879
VERSION     NP_115879.2
DBSOURCE    REFSEQ: accession NM_032490.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Arrondel,C., Missoury,S., Snoek,R., Patat,J., Menara,G.,
            Collinet,B., Liger,D., Durand,D., Gribouval,O., Boyer,O.,
            Buscara,L., Martin,G., Machuca,E., Nevo,F., Lescop,E., Braun,D.A.,
            Boschat,A.C., Sanquer,S., Guerrera,I.C., Revy,P., Parisot,M.,
            Masson,C., Boddaert,N., Charbit,M., Decramer,S., Novo,R.,
            Macher,M.A., Ranchin,B., Bacchetta,J., Laurent,A.,
            Collardeau-Frachon,S., van Eerde,A.M., Hildebrandt,F., Magen,D.,
            Antignac,C., van Tilbeurgh,H. and Mollet,G.
  TITLE     Defects in t6A tRNA modification due to GON7 and YRDC mutations
            lead to Galloway-Mowat syndrome
  JOURNAL   Nat Commun 10 (1), 3967 (2019)
   PUBMED   31481669
  REMARK    GeneRIF: Mutations in GON7, encoding the fifth KEOPS subunit, lead
            to a milder form of Galloway-Mowat syndrome (GAMOS), an autosomal
            recessive disease characterized by early-onset steroid-resistant
            nephrotic syndrome and microcephaly. The structure and cellular
            characterization of GON7 suggest its involvement in the cellular
            stability and quaternary arrangement of the KEOPS complex.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Wan,L.C., Maisonneuve,P., Szilard,R.K., Lambert,J.P., Ng,T.F.,
            Manczyk,N., Huang,H., Laister,R., Caudy,A.A., Gingras,A.C.,
            Durocher,D. and Sicheri,F.
  TITLE     Proteomic analysis of the human KEOPS complex identifies C14ORF142
            as a core subunit homologous to yeast Gon7
  JOURNAL   Nucleic Acids Res 45 (2), 805-817 (2017)
   PUBMED   27903914
REFERENCE   5  (residues 1 to 100)
  AUTHORS   Costessi,A., Mahrour,N., Sharma,V., Stunnenberg,R., Stoel,M.A.,
            Tijchon,E., Conaway,J.W., Conaway,R.C. and Stunnenberg,H.G.
  TITLE     The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin
            ligases by the human tumour antigen PRAME
  JOURNAL   PLoS One 7 (8), e42822 (2012)
   PUBMED   22912744
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC021733.2 and AL110118.7.
            
            On Jul 7, 2006 this sequence version replaced NP_115879.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065216.1, BG503923.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306954.5/ ENSP00000306320.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..100
                     /product="EKC/KEOPS complex subunit GON7"
                     /note="uncharacterized protein C14orf142; GON7, KEOPS
                     complex subunit homolog"
                     /calculated_mol_wt=10728
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BXV9.2)"
     Region          3..98
                     /region_name="DUF4611"
                     /note="Domain of unknown function (DUF4611); pfam15387"
                     /db_xref="CDD:464694"
     Region          61..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXV9.2)"
     CDS             1..100
                     /gene="GON7"
                     /gene_synonym="C14orf142; PNAS-127"
                     /coded_by="NM_032490.5:29..331"
                     /db_xref="CCDS:CCDS41981.1"
                     /db_xref="GeneID:84520"
                     /db_xref="HGNC:HGNC:20356"
                     /db_xref="MIM:617436"
ORIGIN      
        1 mellgeyvgq egkpqklrvs ceapgdgdpf qgllsgvaqm kdmvtelfdp lvqgevqhrv
       61 aaapdedldg ddeddaeden nidnrtnfdg psakrpktps
//
LOCUS       NP_001350358             624 aa            linear   ROD 27-APR-2025
DEFINITION  lysine--tRNA ligase isoform 1 [Mus musculus].
ACCESSION   NP_001350358 XP_017168520
VERSION     NP_001350358.1
DBSOURCE    REFSEQ: accession NM_001363429.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Yu,L., Chen,Z., Zhou,X., Teng,F., Bai,Q.R., Li,L., Li,Y., Liu,Y.,
            Zeng,Q., Wang,Y., Wang,M., Xu,Y., Tang,X. and Wang,X.
  TITLE     KARS Mutations Impair Brain Myelination by Inducing Oligodendrocyte
            Deficiency: One Potential Mechanism and Improvement by Melatonin
  JOURNAL   J Pineal Res 76 (5), e12998 (2024)
   PUBMED   39087379
  REMARK    GeneRIF: KARS Mutations Impair Brain Myelination by Inducing
            Oligodendrocyte Deficiency: One Potential Mechanism and Improvement
            by Melatonin.
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Sleigh,J.N., Mech,A.M., Aktar,T., Zhang,Y. and Schiavo,G.
  TITLE     Altered Sensory Neuron Development in CMT2D Mice Is Site-Specific
            and Linked to Increased GlyRS Levels
  JOURNAL   Front Cell Neurosci 14, 232 (2020)
   PUBMED   32848623
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Jiang,D., Burger,C.A., Casasent,A.K., Albrecht,N.E., Li,F. and
            Samuel,M.A.
  TITLE     Spatiotemporal gene expression patterns reveal molecular
            relatedness between retinal laminae
  JOURNAL   J Comp Neurol 528 (5), 729-755 (2020)
   PUBMED   31609468
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Lim,H.X., Jung,H.J., Lee,A., Park,S.H., Han,B.W., Cho,D. and
            Kim,T.S.
  TITLE     Lysyl-Transfer RNA Synthetase Induces the Maturation of Dendritic
            Cells through MAPK and NF-kappaB Pathways, Strongly Contributing to
            Enhanced Th1 Cell Responses
  JOURNAL   J Immunol 201 (9), 2832-2841 (2018)
   PUBMED   30275047
  REMARK    GeneRIF: these results indicated that KRS effectively induced the
            maturation and activation of dendritic cells
REFERENCE   6  (residues 1 to 624)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
REFERENCE   7  (residues 1 to 624)
  AUTHORS   Carninci,P., Waki,K., Shiraki,T., Konno,H., Shibata,K., Itoh,M.,
            Aizawa,K., Arakawa,T., Ishii,Y., Sasaki,D., Bono,H., Kondo,S.,
            Sugahara,Y., Saito,R., Osato,N., Fukuda,S., Sato,K., Watahiki,A.,
            Hirozane-Kishikawa,T., Nakamura,M., Shibata,Y., Yasunishi,A.,
            Kikuchi,N., Yoshiki,A., Kusakabe,M., Gustincich,S., Beisel,K.,
            Pavan,W., Aidinis,V., Nakagawara,A., Held,W.A., Iwata,H., Kono,T.,
            Nakauchi,H., Lyons,P., Wells,C., Hume,D.A., Fagiolini,M.,
            Hensch,T.K., Brinkmeier,M., Camper,S., Hirota,J., Mombaerts,P.,
            Muramatsu,M., Okazaki,Y., Kawai,J. and Hayashizaki,Y.
  TITLE     Targeting a complex transcriptome: the construction of the mouse
            full-length cDNA encyclopedia
  JOURNAL   Genome Res 13 (6B), 1273-1289 (2003)
   PUBMED   12819125
REFERENCE   8  (residues 1 to 624)
  AUTHORS   Kim,J.Y., Kang,Y.S., Lee,J.W., Kim,H.J., Ahn,Y.H., Park,H., Ko,Y.G.
            and Kim,S.
  TITLE     p38 is essential for the assembly and stability of macromolecular
            tRNA synthetase complex: implications for its physiological
            significance
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 7912-7916 (2002)
   PUBMED   12060739
REFERENCE   9  (residues 1 to 624)
  AUTHORS   Maas,S., Kim,Y.G. and Rich,A.
  TITLE     Genomic clustering of tRNA-specific adenosine deaminase ADAT1 and
            two tRNA synthetases
  JOURNAL   Mamm Genome 12 (5), 387-393 (2001)
   PUBMED   11331948
REFERENCE   10 (residues 1 to 624)
  AUTHORS   Ko,M.S., Threat,T.A., Wang,X., Horton,J.H., Cui,Y., Wang,X.,
            Pryor,E., Paris,J., Wells-Smith,J., Kitchen,J.R., Rowe,L.B.,
            Eppig,J., Satoh,T., Brant,L., Fujiwara,H., Yotsumoto,S. and
            Nakashima,H.
  TITLE     Genome-wide mapping of unselected transcripts from extraembryonic
            tissue of 7.5-day mouse embryos reveals enrichment in the t-complex
            and under-representation on the X chromosome
  JOURNAL   Hum Mol Genet 7 (12), 1967-1978 (1998)
   PUBMED   9811942
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114648.25.
            
            On May 18, 2018 this sequence version replaced XP_017168520.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 4. Variants 1, 3, 4, and 5 all encode the same isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.124354.1,
                                           SRR1660813.10380.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164139, SAMN01164143
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 58.27 cM"
     Protein         1..624
                     /product="lysine--tRNA ligase isoform 1"
                     /EC_number="6.1.1.6"
                     /note="lysine--tRNA ligase"
                     /calculated_mol_wt=71160
     Region          42..604
                     /region_name="PLN02502"
                     /note="lysyl-tRNA synthetase"
                     /db_xref="CDD:215278"
     Site            296..300
                     /site_type="other"
                     /note="motif 1"
                     /db_xref="CDD:238398"
     Site            order(328,350,352,358,362,514,521,524,528,580)
                     /site_type="active"
                     /db_xref="CDD:238398"
     Site            349..352
                     /site_type="other"
                     /note="motif 2"
                     /db_xref="CDD:238398"
     Site            577..580
                     /site_type="other"
                     /note="motif 3"
                     /db_xref="CDD:238398"
     CDS             1..624
                     /gene="Kars1"
                     /gene_synonym="D8Ertd698e; D8Wsu108e; Kars; LysRS;
                     mKIAA0070"
                     /coded_by="NM_001363429.1:239..2113"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS52677.1"
                     /db_xref="GeneID:85305"
                     /db_xref="MGI:MGI:1934754"
ORIGIN      
        1 mlmqaavrlv rgalrqtswa ewgqrelrlg hlapfttlhk dqplsdrrse lkrrlkaekk
       61 laekeakqke lsekqlnqta sapnhtadng vgaeeetldp nqyykirsqa vqqlkvtged
      121 pyphkfhvdi sltqfiqeys hlqpgdhltd vtlkvagrih akrasggkli fydlrgegvk
      181 lqvmansrny kseeefvhin nklrrgdiig vegnpgktkk gelsiipqei tllspclhml
      241 phlhfglkdk etryrqryld lilndfvrqk fivrskiity irsfldelgf leietpmmni
      301 ipggavakpf ityhneldmn lymriapely hkmlvvggid rvyeigrqfr negidlthnp
      361 efttcefyma yadyhdlmei tekmlsgmvk sitgsykity hpdgpegqay evdftppfrr
      421 ismveeleka lgvklpetsl feteetrkil ddicvakave cppprttarl ldklvgefle
      481 vtcisptfic dhpqimspla kwhrskeglt erfelfvmkk eicnayteln dpvrqrqlfe
      541 eqakakaagd deamfidenf ctaleyglpp tagwgmgidr ltmfltdsnn ikevllfpam
      601 kpedkketaa ttetpestea spsv
//
LOCUS       NP_059135                854 aa            linear   PRI 27-APR-2025
DEFINITION  gamma-secretase-activating protein isoform a [Homo sapiens].
ACCESSION   NP_059135 XP_374625 XP_379881 XP_499340 XP_499452
VERSION     NP_059135.2
DBSOURCE    REFSEQ: accession NM_017439.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Xu,P., Chang,J.C., Zhou,X., Wang,W., Bamkole,M., Wong,E.,
            Bettayeb,K., Jiang,L.L., Huang,T., Luo,W., Xu,H., Nairn,A.C.,
            Flajolet,M., Ip,N.Y., Li,Y.M. and Greengard,P.
  TITLE     GSAP regulates lipid homeostasis and mitochondrial function
            associated with Alzheimer's disease
  JOURNAL   J Exp Med 218 (8) (2021)
   PUBMED   34156424
  REMARK    GeneRIF: GSAP regulates lipid homeostasis and mitochondrial
            function associated with Alzheimer's disease.
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Perez,S.E., Nadeem,M., Malek-Ahmadi,M.H., He,B. and Mufson,E.J.
  TITLE     Frontal Cortex and Hippocampal gamma-Secretase Activating Protein
            Levels in Prodromal Alzheimer Disease
  JOURNAL   Neurodegener Dis 17 (6), 235-241 (2017)
   PUBMED   28743126
  REMARK    GeneRIF: These data demonstrate that GSAP proteins are
            differentially dysregulated in severe Alzheimer Disease, but only
            the full-length form was associated with cognitive test scores in
            Alzheimer Disease.
REFERENCE   3  (residues 1 to 854)
  AUTHORS   Chu,J., Li,J.G., Hoffman,N.E., Stough,A.M., Madesh,M. and
            Pratico,D.
  TITLE     Regulation of gamma-secretase activating protein by the
            5Lipoxygenase: in vitro and in vivo evidence
  JOURNAL   Sci Rep 5, 11086 (2015)
   PUBMED   26076991
  REMARK    GeneRIF: GSAP cleavage via caspase-3 is regulated and depend upon
            the availability of 5-Lipoxygenase in Alzheimer's disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 854)
  AUTHORS   Zhu,M., Tao,Y., He,Q., Gao,H., Song,F., Sun,Y.M., Li,H.L., Wu,Z.Y.
            and Saffen,D.
  TITLE     Common GSAP promoter variant contributes to Alzheimer's disease
            liability
  JOURNAL   Neurobiol Aging 35 (11), 2656 (2014)
   PUBMED   25037285
  REMARK    GeneRIF: Its promoter variant contributes to Alzheimer's disease
            liability.
REFERENCE   5  (residues 1 to 854)
  AUTHORS   Hussain,I., Fabregue,J., Anderes,L., Ousson,S., Borlat,F.,
            Eligert,V., Berger,S., Dimitrov,M., Alattia,J.R., Fraering,P.C. and
            Beher,D.
  TITLE     The role of gamma-secretase activating protein (GSAP) and imatinib
            in the regulation of gamma-secretase activity and amyloid-beta
            generation
  JOURNAL   J Biol Chem 288 (4), 2521-2531 (2013)
   PUBMED   23209290
  REMARK    GeneRIF: gamma-secretase activating protein (GSAP) and imatinib
            have roles in the regulation of gamma-secretase activity and
            amyloid-beta generation
REFERENCE   6  (residues 1 to 854)
  AUTHORS   Deatherage,C.L., Hadziselimovic,A. and Sanders,C.R.
  TITLE     Purification and characterization of the human gamma-secretase
            activating protein
  JOURNAL   Biochemistry 51 (25), 5153-5159 (2012)
   PUBMED   22681044
  REMARK    GeneRIF: Protocols for recombinant bacterial expression and
            purification of potentially important protein GSAP are not
            successful in generating soluble forms of GSAP that contain
            well-ordered and homogeneous tertiary structure.
REFERENCE   7  (residues 1 to 854)
  AUTHORS   Satoh,J., Tabunoki,H., Ishida,T., Saito,Y. and Arima,K.
  TITLE     Immunohistochemical characterization of gamma-secretase activating
            protein expression in Alzheimer's disease brains
  JOURNAL   Neuropathol Appl Neurobiol 38 (2), 132-141 (2012)
   PUBMED   21718343
  REMARK    GeneRIF: Aberrant regulation of gamma-secretase activating protein
            expression plays a key role in acceleration of gamma-cleavage of
            beta-secretase-cleaved C-terminal fragment of amyloid precursor
            protein and accumulation of Abeta in AD brains
REFERENCE   8  (residues 1 to 854)
  AUTHORS   He,G., Luo,W., Li,P., Remmers,C., Netzer,W.J., Hendrick,J.,
            Bettayeb,K., Flajolet,M., Gorelick,F., Wennogle,L.P. and
            Greengard,P.
  TITLE     Gamma-secretase activating protein is a therapeutic target for
            Alzheimer's disease
  JOURNAL   Nature 467 (7311), 95-98 (2010)
   PUBMED   20811458
  REMARK    GeneRIF: A gamma-secretase activating protein (GSAP) that
            selectively increases amyloid-beta production via interactions with
            both gamma-secretase and its substrate, the amyloid precursor
            protein carboxy-terminal fragment.
REFERENCE   9  (residues 1 to 854)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC110797.1, DB498013.1 and BM842423.1.
            
            On Jun 6, 2007 this sequence version replaced NP_059135.1.
            
            Summary: Accumulation of neurotoxic amyloid-beta is a major
            hallmark of Alzheimer disease (AD; MIM 104300). Formation of
            amyloid-beta is catalyzed by gamma-secretase (see PSEN1; MIM
            104311), a protease with numerous substrates. PION, or GSAP,
            selectively increases amyloid-beta production through a mechanism
            involving its interaction with both gamma-secretase and its
            substrate, the amyloid-beta precursor protein (APP; MIM 104760)
            C-terminal fragment (APP-CTF) (He et al., 2010 [PubMed
            20811458]).[supplied by OMIM, Nov 2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110797.1, SRR1803614.70689.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257626.12/ ENSP00000257626.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..854
                     /product="gamma-secretase-activating protein isoform a"
                     /note="protein pigeon homolog"
                     /calculated_mol_wt=97671
     Region          3..497
                     /region_name="GSAP"
                     /note="gamma-secretase-activating protein and similar
                     proteins; cd23105"
                     /db_xref="CDD:438516"
     Region          642..749
                     /region_name="GSAP-16"
                     /note="gamma-Secretase-activating protein C-term;
                     pfam14959"
                     /db_xref="CDD:464405"
     CDS             1..854
                     /gene="GSAP"
                     /gene_synonym="PION"
                     /coded_by="NM_017439.4:29..2593"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34672.2"
                     /db_xref="GeneID:54103"
                     /db_xref="HGNC:HGNC:28042"
                     /db_xref="MIM:613552"
ORIGIN      
        1 malrlvadfd lgkdvlpwlr aqravseasg agsggadvle ndyeslhvln verngniiyt
       61 ykddkgnvvf glydcqtrqn ellytfekdl qvfscsvnse rtllaaslvq stkegkrnel
      121 qpgskcltll veihpvnnvk vlkavdsyiw vqflyphies hplpenhlll iseekyieqf
      181 rihvaqedgn rvviknsghl prdriaedfv waqwdmseqr lyyidlkksr silkciqfya
      241 desynlmfev pldislsnsg fklvnfgcdy hqyrdkfskh ltlcvftnht gslcvcyspk
      301 caswgqitys vfyihkghsk tfttslenvg shmtkgitfl nldyyvavyl pghffhllnv
      361 qhpdlichnl fltgnnemid mlphcplqsl sgslvldccs gklyrallsq ssllqllqnt
      421 cldcekmaal hcalycgqga qfleaqiiqw isenvsachs fdliqefiia ssywsvyset
      481 snmdkllphs svltwnteip gitlvtedia lplmkvlsfk gyweklnsnl eyvkyakphf
      541 hynnsvvrre whnliseekt gkrrsaayvr nildnavkvi snlearnlgp rltpllqeed
      601 shqrllmglm vselkdhflr hlqgvekkki eqmvldyisk lldlichive tnwrkhnlhs
      661 wvlhfnsrgs aaefavfhim trileatnsl flplppgfht lhtilgvqcl plhnllhcid
      721 sgvlllteta virlmkdldn tekneklkfs iivrlpplig qkicrlwdhp mssniisrnh
      781 vtrllqnykk qprnsminks sfsveflpln yfieiltdie ssnqalypfe ghdnvdaefv
      841 eeaalkhtam llgl
//
LOCUS       NP_056013               1261 aa            linear   PRI 27-APR-2025
DEFINITION  protein cordon-bleu isoform b [Homo sapiens].
ACCESSION   NP_056013
VERSION     NP_056013.2
DBSOURCE    REFSEQ: accession NM_015198.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1261)
  AUTHORS   Abdul Majeed,S., Dunzendorfer,H., Weiner,J., Heiker,J.T., Kiess,W.,
            Korner,A. and Landgraf,K.
  TITLE     COBL, MKX and MYOC Are Potential Regulators of Brown Adipose Tissue
            Development Associated with Obesity-Related Metabolic Dysfunction
            in Children
  JOURNAL   Int J Mol Sci 24 (4), 3085 (2023)
   PUBMED   36834493
  REMARK    GeneRIF: COBL, MKX and MYOC Are Potential Regulators of Brown
            Adipose Tissue Development Associated with Obesity-Related
            Metabolic Dysfunction in Children.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1261)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1261)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1261)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1261)
  AUTHORS   Husson,C., Renault,L., Didry,D., Pantaloni,D. and Carlier,M.F.
  TITLE     Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin
            filament assembly
  JOURNAL   Mol Cell 43 (3), 464-477 (2011)
   PUBMED   21816349
  REMARK    GeneRIF: Cordon-Bleu works as a dynamizer of actin assembly by
            combining many properties of profilin with weak filament nucleating
            and powerful filament severing activities and sequestration of
            ADP-actin, which generate oscillatory polymerization kinetics.
REFERENCE   7  (residues 1 to 1261)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1261)
  AUTHORS   de Krom,M., Staal,W.G., Ophoff,R.A., Hendriks,J., Buitelaar,J.,
            Franke,B., de Jonge,M.V., Bolton,P., Collier,D., Curran,S., van
            Engeland,H. and van Ree,J.M.
  TITLE     A common variant in DRD3 receptor is associated with autism
            spectrum disorder
  JOURNAL   Biol Psychiatry 65 (7), 625-630 (2009)
   PUBMED   19058789
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1261)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
REFERENCE   10 (residues 1 to 1261)
  AUTHORS   Gasca,S., Hill,D.P., Klingensmith,J. and Rossant,J.
  TITLE     Characterization of a gene trap insertion into a novel gene,
            cordon-bleu, expressed in axial structures of the gastrulating
            mouse embryo
  JOURNAL   Dev Genet 17 (2), 141-154 (1995)
   PUBMED   7586755
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC111496.1, AB014533.1,
            DA245843.1, BC045771.1 and AC004414.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 11, 2003 this sequence version replaced NP_056013.1.
            
            Summary: This gene encodes a protein that contains WH2 domains
            (WASP, Wiskott-Aldrich syndrome protein, homology domain-2) that
            interact with actin. The encoded actin regulator protein is
            required for growth and assembly of brush border microvilli that
            play a role in maintaining intestinal homeostasis. A similar
            protein in mouse functions in midbrain neural tube closure. A
            pseudogene of this gene is located on chromosome X. [provided by
            RefSeq, Oct 2016].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, and uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1. The
            encoded isoform (b) is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150263.1, AB014533.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265136.12/ ENSP00000265136.7
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.1"
     Protein         1..1261
                     /product="protein cordon-bleu isoform b"
                     /note="protein cordon-bleu"
                     /calculated_mol_wt=135486
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5NBX1; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          152..230
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZUI5; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZUI5; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          259..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          298..303
                     /region_name="KKRRAP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZUI5; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          331..336
                     /region_name="KKRRAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5NBX1; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          500..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          580..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Region          658..699
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Region          779..843
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            815
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Region          907..1104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            962
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          1099..1131
                     /region_name="WH2_Wa_Cobl"
                     /note="first Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wa) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21799"
                     /db_xref="CDD:409197"
     Site            order(1110,1112..1114,1116..1118,1120,1124,1126..1130)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409197"
     Region          1120..1145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Region          1126..1129
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409197"
     Region          1145..1188
                     /region_name="WH2_Wb_Cobl"
                     /note="second Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wb) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21800"
                     /db_xref="CDD:409198"
     Site            order(1145,1147..1160,1166..1169,1171,1173..1174,
                     1176..1177,1180,1184..1188)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409198"
     Region          1166..1169
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409198"
     Site            1192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          1196..1232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            1227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          1233..1258
                     /region_name="WH2_Wc_Cobl"
                     /note="third Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wc) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21801"
                     /db_xref="CDD:409199"
     Site            order(1237..1238,1240..1242,1244..1246,1254..1257)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409199"
     Region          1254..1257
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409199"
     CDS             1..1261
                     /gene="COBL"
                     /coded_by="NM_015198.5:177..3962"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS34637.1"
                     /db_xref="GeneID:23242"
                     /db_xref="HGNC:HGNC:22199"
                     /db_xref="MIM:610317"
ORIGIN      
        1 mdaprasaak pptgrkmkar appppgkaat lhvhsdqkpp hdgalgsqqn lvrmkealra
       61 stmdvtvvlp sglekrsvln gshammdllv elclqnhlnp shhaleirss etqqplsfkp
      121 ntligtlnvh tvflkekvpe ekvkpgppkv peksvrlvvn ylrtqkavvr vspevplqni
      181 lpvicakcev spehvvllrd niageelels kslnelgike lyawdnrret frksslgnde
      241 tdkekkkflg ffkvnkrsns kgclttpnsp smhsrsltlg pslslgsisg vsvksemkkr
      301 rappppgsgp pvqdkasekv slgsqidlqk kkrrapappp pqppppspli pnrtedkeen
      361 rkstmvslpl gsgshcspdg apqvlseaee tvsvgscfas edttedsgvm sspsdivsld
      421 sqqdsmkykd kwatdqedcs dqdlagtpdl gpqksplwek ngsenshlrt ekavtasnde
      481 edlliagefr ktlaeldedl eemedsyetd tssltssihg asnhcpqdam iphgdtdaip
      541 vtfigevsdd pvdsglfsnr nnnagsfdse gvasrrdsla plqaehsqph ekareevpal
      601 hpashdvgkg irvalsnisk dgnlmetapr vtsfasnlht dnlnakvkdk vygcadgert
      661 qatervnsqp vnekdsndkn aalaptswhq rgqnpgksyr lkhglttyki ippksemrcy
      721 drdvslstga ikidelgnlv sphatgirii slsssvpeae sqpigkvref wrcnsvekhl
      781 grpsessarg ppstpvptqt qnpesrlqad pkpispqqks ahhegrnplg egrnqpptmg
      841 mghvrvpaah ttevtflkpq rrtssqyvas aiakrigapk vhadvvrphg yaekgyagka
      901 pvlaappvtv kddrtssphs etqgwkdgaq wpcvtppnnh gedlavgapp rgevigphrk
      961 lstqdrpaai hrsscfslvq ssqrdrvsvg qscgfsgkqs tssqeassas eprrapdgtd
     1021 pppphtsdtq acsrelvngs vrapghgeps hppggsgtes hillereekp svfstdgnet
     1081 dsiwppsifg pkkkfkpvvq rpvpkdtslh salmeaihsa ggkdrlrkta ehtgegrpak
     1141 lsyteaeger sallaairgh sgtcslrkva ssaseelqsf rdaalsaqgs esplledlgl
     1201 lsppaipppp pppsqalsap rtasrfstgt lsntadarqa lmdairsgtg aarlrkvpll
     1261 v
//
LOCUS       NP_061882                274 aa            linear   PRI 27-APR-2025
DEFINITION  toll-interacting protein isoform 1 [Homo sapiens].
ACCESSION   NP_061882
VERSION     NP_061882.2
DBSOURCE    REFSEQ: accession NM_019009.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Nouri,H.R., Schaunaman,N., Kraft,M., Li,L., Numata,M. and Chu,H.W.
  TITLE     Tollip deficiency exaggerates airway type 2 inflammation in mice
            exposed to allergen and influenza A virus: role of the ATP/IL-33
            signaling axis
  JOURNAL   Front Immunol 14, 1304758 (2023)
   PUBMED   38124753
  REMARK    GeneRIF: Tollip deficiency exaggerates airway type 2 inflammation
            in mice exposed to allergen and influenza A virus: role of the
            ATP/IL-33 signaling axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Demir,A.B., Baris,E., Kaner,U.B., Alotaibi,H., Atabey,N. and Koc,A.
  TITLE     Toll-interacting protein may affect doxorubicin resistance in
            hepatocellular carcinoma cell lines
  JOURNAL   Mol Biol Rep 50 (10), 8551-8563 (2023)
   PUBMED   37644370
  REMARK    GeneRIF: Toll-interacting protein may affect doxorubicin resistance
            in hepatocellular carcinoma cell lines.
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Kowalewski,A., Jaworski,D., Borowczak,J., Maniewski,M.,
            Szczerbowski,K., Antosik,P., Durslewicz,J., Smolinska,M.,
            Ligmanowska,J., Grzanka,D. and Szylberg,L.
  TITLE     TOLLIP Protein Expression Predicts Unfavorable Outcome in Renal
            Cell Carcinoma
  JOURNAL   Int J Mol Sci 23 (23), 14702 (2022)
   PUBMED   36499030
  REMARK    GeneRIF: TOLLIP Protein Expression Predicts Unfavorable Outcome in
            Renal Cell Carcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Venkatasubramanian,S., Pryor,R., Plumlee,C., Cohen,S.B.,
            Simmons,J.D., Warr,A.J., Graustein,A.D., Saha,A., Hawn,T.R.,
            Urdahl,K.B. and Shah,J.A.
  TITLE     TOLLIP Optimizes Dendritic Cell Maturation to Lipopolysaccharide
            and Mycobacterium tuberculosis
  JOURNAL   J Immunol 209 (3), 435-445 (2022)
   PUBMED   35803695
  REMARK    GeneRIF: TOLLIP Optimizes Dendritic Cell Maturation to
            Lipopolysaccharide and Mycobacterium tuberculosis.
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Jensen,L.E. and Whitehead,A.S.
  TITLE     IRAK1b, a novel alternative splice variant of interleukin-1
            receptor-associated kinase (IRAK), mediates interleukin-1 signaling
            and has prolonged stability
  JOURNAL   J Biol Chem 276 (31), 29037-29044 (2001)
   PUBMED   11397809
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Burns,K., Clatworthy,J., Martin,L., Martinon,F., Plumpton,C.,
            Maschera,B., Lewis,A., Ray,K., Tschopp,J. and Volpe,F.
  TITLE     Tollip, a new component of the IL-1RI pathway, links IRAK to the
            IL-1 receptor
  JOURNAL   Nat Cell Biol 2 (6), 346-351 (2000)
   PUBMED   10854325
REFERENCE   8  (residues 1 to 274)
  AUTHORS   Volpe,F., Clatworthy,J., Kaptein,A., Maschera,B., Griffin,A.M. and
            Ray,K.
  TITLE     The IL1 receptor accessory protein is responsible for the
            recruitment of the interleukin-1 receptor associated kinase to the
            IL1/IL1 receptor I complex
  JOURNAL   FEBS Lett 419 (1), 41-44 (1997)
   PUBMED   9426216
REFERENCE   9  (residues 1 to 274)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   10 (residues 1 to 274)
  AUTHORS   Nilsen,K.H.
  TITLE     Malignant lymphoma and rheumatic symptoms
  JOURNAL   N Z Med J 83 (563), 320-322 (1976)
   PUBMED   1085432
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB039994.1, AL136835.1 and
            AA861717.1.
            
            On Jun 10, 2002 this sequence version replaced NP_061882.1.
            
            Summary: This gene encodes a ubiquitin-binding protein that
            interacts with several Toll-like receptor (TLR) signaling cascade
            components. The encoded protein regulates inflammatory signaling
            and is involved in interleukin-1 receptor trafficking and in the
            turnover of IL1R-associated kinase. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.450488.1,
                                           SRR1660805.26131.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317204.11/ ENSP00000314733.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..274
                     /product="toll-interacting protein isoform 1"
                     /note="Toll-interacting protein; adapter protein"
                     /calculated_mol_wt=30151
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H0E2.1)"
     Region          52..172
                     /region_name="C2_Tollip"
                     /note="C2 domain present in Toll-interacting protein
                     (Tollip); cd04016"
                     /db_xref="CDD:175983"
     Site            order(74,121,123,129)
                     /site_type="other"
                     /note="putative Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175983"
     Region          133..136
                     /region_name="AIM1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0E2.1)"
     Region          151..154
                     /region_name="AIM2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0E2.1)"
     Region          230..270
                     /region_name="CUE_TOLIP"
                     /note="CUE domain found in the C-terminal of
                     toll-interacting protein (Tollip) and similar proteins;
                     cd14363"
                     /db_xref="CDD:270546"
     CDS             1..274
                     /gene="TOLLIP"
                     /gene_synonym="IL-1RAcPIP"
                     /coded_by="NM_019009.4:135..959"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7723.1"
                     /db_xref="GeneID:54472"
                     /db_xref="HGNC:HGNC:16476"
                     /db_xref="MIM:606277"
ORIGIN      
        1 mattvstqrg pvyigelpqd flritptqqq rqvqldaqaa qqlqyggavg tvgrlnitvv
       61 qaklaknygm trmdpycrlr lgyavyetpt ahngaknprw nkvihctvpp gvdsfyleif
      121 derafsmddr iawthitipe slrqgkvedk wyslsgrqgd dkegminlvm syallpaamv
      181 mppqpvvlmp tvyqqgvgyv pitgmpavcs pgmvpvalpp aavnaqprcs eedlkaiqdm
      241 fpnmdqevir svleaqrgnk daainsllqm geep
//
LOCUS       NP_060229               1027 aa            linear   PRI 27-APR-2025
DEFINITION  INO80 complex subunit D [Homo sapiens].
ACCESSION   NP_060229
VERSION     NP_060229.3
DBSOURCE    REFSEQ: accession NM_017759.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Chang,C.C., Liu,T.Y., Lee,Y.T., Chen,Y.C., Yeh,K.T., Lee,C.C.,
            Chen,Y.L., Lin,P.C., Chang,Y.S., Chan,W.L., Liu,T.C. and Chang,J.G.
  TITLE     Genome-wide analysis of lncRNAs in 3'-untranslated regions:
            CR933609 acts as a decoy to protect the INO80D gene
  JOURNAL   Int J Oncol 53 (1), 417-433 (2018)
   PUBMED   29750421
  REMARK    GeneRIF: expression levels of CR933609 and INO80D were decreased in
            CR933609-knockdown NSCLC cells, but only expression levels of
            INO80D decreased in INO80D knockdown cells. It was shown that there
            are independent promoters in CR933609 and INO80D
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Zhang,S., Zhou,B., Wang,L., Li,P., Bennett,B.D., Snyder,R.,
            Garantziotis,S., Fargo,D.C., Cox,A.D., Chen,L. and Hu,G.
  TITLE     INO80 is required for oncogenic transcription and tumor growth in
            non-small cell lung cancer
  JOURNAL   Oncogene 36 (10), 1430-1439 (2017)
   PUBMED   27641337
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Cao,L., Ding,J., Dong,L., Zhao,J., Su,J., Wang,L., Sui,Y., Zhao,T.,
            Wang,F., Jin,J. and Cai,Y.
  TITLE     Negative Regulation of p21Waf1/Cip1 by Human INO80 Chromatin
            Remodeling Complex Is Implicated in Cell Cycle Phase G2/M Arrest
            and Abnormal Chromosome Stability
  JOURNAL   PLoS One 10 (9), e0137411 (2015)
   PUBMED   26340092
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1027)
  AUTHORS   Shameer,K., Klee,E.W., Dalenberg,A.K. and Kullo,I.J.
  TITLE     Whole exome sequencing implicates an INO80D mutation in a syndrome
            of aortic hypoplasia, premature atherosclerosis, and arterial
            stiffness
  JOURNAL   Circ Cardiovasc Genet 7 (5), 607-614 (2014)
   PUBMED   25122053
  REMARK    GeneRIF: INO80D is a subunit of the human INO80 chromatin
            remodeling complex; its Ser818Cys mutation has a role in
            accelerated arterial aging
REFERENCE   5  (residues 1 to 1027)
  AUTHORS   Vassileva,I., Yanakieva,I., Peycheva,M., Gospodinov,A. and
            Anachkova,B.
  TITLE     The mammalian INO80 chromatin remodeling complex is required for
            replication stress recovery
  JOURNAL   Nucleic Acids Res 42 (14), 9074-9086 (2014)
   PUBMED   25016522
REFERENCE   6  (residues 1 to 1027)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   7  (residues 1 to 1027)
  AUTHORS   Cotsapas,C., Speliotes,E.K., Hatoum,I.J., Greenawalt,D.M.,
            Dobrin,R., Lum,P.Y., Suver,C., Chudin,E., Kemp,D., Reitman,M.,
            Voight,B.F., Neale,B.M., Schadt,E.E., Hirschhorn,J.N., Kaplan,L.M.
            and Daly,M.J.
  CONSRTM   GIANT Consortium
  TITLE     Common body mass index-associated variants confer risk of extreme
            obesity
  JOURNAL   Hum Mol Genet 18 (18), 3502-3507 (2009)
   PUBMED   19553259
  REMARK    Erratum:[Hum Mol Genet. 2010 Sep 15;19(18):3690-1]
REFERENCE   8  (residues 1 to 1027)
  AUTHORS   Jin,J., Cai,Y., Yao,T., Gottschalk,A.J., Florens,L., Swanson,S.K.,
            Gutierrez,J.L., Coleman,M.K., Workman,J.L., Mushegian,A.,
            Washburn,M.P., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian chromatin remodeling complex with similarities to the
            yeast INO80 complex
  JOURNAL   J Biol Chem 280 (50), 41207-41212 (2005)
   PUBMED   16230350
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK096585.1, DB233201.1, AC007679.4, BC004193.2, AK000316.1 and
            CR746991.1.
            
            On Jun 2, 2007 this sequence version replaced NP_060229.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.216272.1,
                                           SRR1803613.231593.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000403263.6/ ENSP00000384198.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..1027
                     /product="INO80 complex subunit D"
                     /calculated_mol_wt=113071
     Region          18..79
                     /region_name="zf-C3Hc3H"
                     /note="Potential DNA-binding domain; pfam13891"
                     /db_xref="CDD:464023"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53TQ3.3)"
     Region          193..278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TQ3.3)"
     Region          <211..>290
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          447..511
                     /region_name="zf-C3Hc3H"
                     /note="Potential DNA-binding domain; pfam13891"
                     /db_xref="CDD:464023"
     Region          519..574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TQ3.3)"
     Region          813..850
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TQ3.3)"
     Region          <914..>1025
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          914..969
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TQ3.3)"
     Region          982..1027
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TQ3.3)"
     CDS             1..1027
                     /gene="INO80D"
                     /coded_by="NM_017759.5:398..3481"
                     /db_xref="CCDS:CCDS46500.1"
                     /db_xref="GeneID:54891"
                     /db_xref="HGNC:HGNC:25997"
                     /db_xref="MIM:619207"
ORIGIN      
        1 myegkhihfs evdnkplcsy spklckqrrl ngyafcirhv ledktapfkq ceyvakynsq
       61 rctnpipkse drrycnshlq vlgfipkker kkkndpidev kvrhqmdtma fsltvptlal
      121 kmpngldgms lsppgarvpl hyleteledp fafneedddl kkgatvrkkl qsklaqnrqr
      181 qreteilkvr qehfspppap sqqqppqqhs hlsplstslk ppappqgsvc kspqpqntsl
      241 pmqgvaptth tiaqarqlsh krplpllpss raptvdpprt drilmkataf sphfscisrl
      301 qrlvklctqk hqldtdlfph lgldwseesg eepedseqas pyqvawsire tlryqrhasd
      361 dddaesrssr vtqlctyfqq kykhlcrler aesrqkkcrh tfrkallqaa skepectgql
      421 iqelrraacs rtsisrtklr evepaacsgt vkgeqcanka lpftrhcfqh illnhsqqlf
      481 ssctakfadg qqcsvpvfdi thqtplceeh akkmdnflrg dnsrkvqhqq qrkprkktkp
      541 paltkkhkkk rrrgprrpqk pippavpqgn lsmpasvslp veashirsps tpelsadelp
      601 ddianeitdi phdlelnqed fsdvlprlpd dlqdfdffeg kngdllptte eaeeleralq
      661 avtsleclst igvlaqsdgv pvqelsdrgi gvfstgtgas giqslsrevn tdlgellngr
      721 ivhdnfssle ldenllrsat lsnpptplag qiqgqfsapa nvgltsatli sqsalgeraf
      781 pgqfhglhdg shasqrphpa qllskaddli tsrqqyssdh shssphgshy dsehvpspys
      841 dhitsphtts ysgdnmaatf saempimaqh llptqlevpl ggvvnprthw gnlpvnlgdp
      901 spfsnllgad ghllstslst ppttsnsett qpafatvtps sssvlpglpq tsfsgmgpsa
      961 elmastspkq qlpqfsaafg hqlsshsgip kdlqpshssi apptgftvtg atatstnnas
     1021 spfpspn
//
LOCUS       NP_057439                455 aa            linear   PRI 27-APR-2025
DEFINITION  probable ATP-dependent RNA helicase DDX47 isoform 1 [Homo sapiens].
ACCESSION   NP_057439
VERSION     NP_057439.2
DBSOURCE    REFSEQ: accession NM_016355.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Zhu,Y., Cai,W., Zheng,Y., Zhang,W., Wang,B. and Kang,Y.
  TITLE     BIOINFORMATICS APPLICATIONS UNDER CONDITION CONTROL: HIGH
            DIAGNOSTIC VALUE OF DDX47 IN REAL MEDICAL SETTINGS
  JOURNAL   Shock 61 (1), 97-104 (2024)
   PUBMED   37553903
  REMARK    GeneRIF: BIOINFORMATICS APPLICATIONS UNDER CONDITION CONTROL: HIGH
            DIAGNOSTIC VALUE OF DDX47 IN REAL MEDICAL SETTINGS.
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Marchena-Cruz,E., Camino,L.P., Bhandari,J., Silva,S.,
            Marqueta-Gracia,J.J., Amdeen,S.A., Guillen-Mendoza,C.,
            Garcia-Rubio,M.L., Calderon-Montano,J.M., Xue,X., Luna,R. and
            Aguilera,A.
  TITLE     DDX47, MeCP2, and other functionally heterogeneous factors protect
            cells from harmful R loops
  JOURNAL   Cell Rep 42 (3), 112148 (2023)
   PUBMED   36827184
  REMARK    GeneRIF: DDX47, MeCP2, and other functionally heterogeneous factors
            protect cells from harmful R loops.
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Regard,J.B., Scheek,S., Borbiev,T., Lanahan,A.A., Schneider,A.,
            Demetriades,A.M., Hiemisch,H., Barnes,C.A., Verin,A.D. and
            Worley,P.F.
  TITLE     Verge: a novel vascular early response gene
  JOURNAL   J Neurosci 24 (16), 4092-4103 (2004)
   PUBMED   15102925
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Doorbar,J., Elston,R.C., Napthine,S., Raj,K., Medcalf,E.,
            Jackson,D., Coleman,N., Griffin,H.M., Masterson,P., Stacey,S.,
            Mengistu,Y. and Dunlop,J.
  TITLE     The E1E4 protein of human papillomavirus type 16 associates with a
            putative RNA helicase through sequences in its C terminus
  JOURNAL   J Virol 74 (21), 10081-10095 (2000)
   PUBMED   11024137
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136666.1 and BC009379.2.
            
            On Apr 15, 2002 this sequence version replaced NP_057439.1.
            
            Summary: This gene encodes a member of the DEAD box protein family.
            DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure, such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. The protein encoded by this gene can
            shuttle between the nucleus and the cytoplasm, and has an
            RNA-independent ATPase activity. Two alternatively spliced
            transcript variants encoding distinct isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136666.1, SRR5189661.115172.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358007.7/ ENSP00000350698.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.1"
     Protein         1..455
                     /product="probable ATP-dependent RNA helicase DDX47
                     isoform 1"
                     /EC_number="3.6.4.13"
                     /note="E4-DEAD box protein; probable ATP-dependent RNA
                     helicase DDX47; DEAD box polypeptide 47; DEAD box protein
                     47; DEAD (Asp-Glu-Ala-Asp) box polypeptide 47"
                     /calculated_mol_wt=50516
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0S4.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9H0S4.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H0S4.1)"
     Region          23..453
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          24..52
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0S4.1)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H0S4.1)"
     Region          174..177
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0S4.1)"
     Region          413..455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0S4.1)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H0S4.1)"
     CDS             1..455
                     /gene="DDX47"
                     /gene_synonym="E4-DBP; HQ0256; MSTP162; RRP3"
                     /coded_by="NM_016355.4:23..1390"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8655.1"
                     /db_xref="GeneID:51202"
                     /db_xref="HGNC:HGNC:18682"
                     /db_xref="MIM:615428"
ORIGIN      
        1 maapeehdsp teasqpivee eetktfkdlg vtdvlceacd qlgwtkptki qieaiplalq
       61 grdiiglaet gsgktgafal pilnalletp qrlfalvltp trelafqise qfealgssig
      121 vqsavivggi dsmsqslala kkphiiiatp grlidhlent kgfnlralky lvmdeadril
      181 nmdfetevdk ilkviprdrk tflfsatmtk kvqklqraal knpvkcavss kyqtveklqq
      241 yyifipskfk dtylvyilne lagnsfmifc stcnntqrta lllrnlgfta iplhgqmsqs
      301 krlgslnkfk akarsillat dvasrgldip hvdvvvnfdi pthskdyihr vgrtaragrs
      361 gkaitfvtqy dvelfqrieh ligkklpgfp tqddevmmlt ervaeaqrfa rmelrehgek
      421 kkrsredagd nddtegaigv rnkvaggkmk krkgr
//
LOCUS       NP_057570                247 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 69 [Homo sapiens].
ACCESSION   NP_057570 XP_005270976
VERSION     NP_057570.2
DBSOURCE    REFSEQ: accession NM_016486.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA451438.1 and BC013608.1.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_005270976.1, NP_057570.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.198381.1,
                                           SRR5189661.133351.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372025.5/ ENSP00000361095.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..247
                     /product="transmembrane protein 69"
                     /calculated_mol_wt=27420
     Region          93..231
                     /region_name="DUF3429"
                     /note="Protein of unknown function (DUF3429); pfam11911"
                     /db_xref="CDD:463393"
     Site            97..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWH9.1)"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWH9.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWH9.1)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWH9.1)"
     Site            216..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWH9.1)"
     CDS             1..247
                     /gene="TMEM69"
                     /gene_synonym="C1orf154"
                     /coded_by="NM_016486.4:191..934"
                     /db_xref="CCDS:CCDS41325.1"
                     /db_xref="GeneID:51249"
                     /db_xref="HGNC:HGNC:28035"
ORIGIN      
        1 mlrfiqkfsq asskilkysf pvglrtsrtd ilslkmslqq nfspcprpwl sssfpaymsk
       61 tqcyhtspcs fkkqqkqall arpsstityl tdspkpalcv tlaglipfva pplvmlmtkt
      121 yipilaftqm aygasflsfl ggirwgfalp egspakpdyl nlassaaplf fswfaflise
      181 rlseaivtvi mgmgvafhle lfllphypnw fkalrivvtl latfsfiitl vvkssfpekg
      241 hkrpgqv
//
LOCUS       NP_001179147             533 aa            linear   MAM 27-APR-2025
DEFINITION  dnaJ homolog subfamily C member 21 [Bos taurus].
ACCESSION   NP_001179147 XP_586236
VERSION     NP_001179147.1
DBSOURCE    REFSEQ: accession NM_001192218.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            NKLS02000020.1.
            
            On Jul 17, 2010 this sequence version replaced XP_586236.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5571254.4628.1, SRR5571263.8080.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA6648753,
                                           SAMEA6648754 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="20"
                     /map="20"
                     /breed="Hereford"
     Protein         1..533
                     /product="dnaJ homolog subfamily C member 21"
                     /note="DnaJ (Hsp40) homolog, subfamily C, member 21"
                     /calculated_mol_wt=61586
     Region          2..>66
                     /region_name="PRK10767"
                     /note="chaperone protein DnaJ; Provisional"
                     /db_xref="CDD:236757"
     Region          4..>267
                     /region_name="ZUO1"
                     /note="Ribosome-associated chaperone zuotin [Translation,
                     ribosomal structure and biogenesis / Posttranslational
                     modification, protein turnover, chaperones]; COG5269"
                     /db_xref="CDD:227594"
     Region          278..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0II91.2)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5F1R6; propagated from
                     UniProtKB/Swiss-Prot (Q0II91.2)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5F1R6; propagated from
                     UniProtKB/Swiss-Prot (Q0II91.2)"
     Region          314..339
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          316..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          327..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0II91.2)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5F1R6; propagated from
                     UniProtKB/Swiss-Prot (Q0II91.2)"
     Region          503..533
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0II91.2)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5F1R6; propagated from
                     UniProtKB/Swiss-Prot (Q0II91.2)"
     CDS             1..533
                     /gene="DNAJC21"
                     /coded_by="NM_001192218.3:161..1762"
                     /db_xref="BGD:BT21515"
                     /db_xref="GeneID:509302"
ORIGIN      
        1 mkchyealgv rrdaseeelk kayrklalkw hpdknldnaa eaaeqfkliq aaydvlsdpq
       61 erawydnhre allkggldge yqddsldllh yftvtcysgy gddekgfytv yrnvfemiak
      121 eelesaleed medfptfgds qsdydtvvhp fyaywqsfct qknfawkeey dtrqasnrwe
      181 kramekenkk irdkarkekn elvrqlvafi rkrdrrvqah rklveeqnae karkaeamrr
      241 qqklkqakla eqyreqswma vadlekelre meaqyekqfg dgsgedeaed qelrdgqdgk
      301 dsdeaedael ydglycpacd ksfktekamr nhekskkhre mvallkqqle eeeanfsgpq
      361 tdenslnans eeemedapkq klsrkqkkkk qkpaqnyddn fnengigegv kidpedtnln
      421 qnsakeseds lqenvgvtet velcddpkte aksvskpkgk kakdtkksvr vpaepqtmsd
      481 vliscttchs efpsrnklfd hlkatghara pssstslnsv tnsrnkkekr knr
//
LOCUS       NP_001356843             366 aa            linear   PRI 27-APR-2025
DEFINITION  endophilin-B2 isoform d [Homo sapiens].
ACCESSION   NP_001356843
VERSION     NP_001356843.1
DBSOURCE    REFSEQ: accession NM_001369914.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Serfass,J.M., Takahashi,Y., Zhou,Z., Kawasawa,Y.I., Liu,Y.,
            Tsotakos,N., Young,M.M., Tang,Z., Yang,L., Atkinson,J.M.,
            Chroneos,Z.C. and Wang,H.G.
  TITLE     Endophilin B2 facilitates endosome maturation in response to growth
            factor stimulation, autophagy induction, and influenza A virus
            infection
  JOURNAL   J Biol Chem 292 (24), 10097-10111 (2017)
   PUBMED   28455444
  REMARK    GeneRIF: Data (including data from studies in knockout mice)
            suggest that SH3GLB2 regulates trafficking of endocytic vesicles
            and autophagosomes to late endosomes or lysosomes; despite having
            an intracellular localization and tissue distribution similar to
            endophilin B1, endophilin B2 is dispensable for mitochondrial
            apoptosis.
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Fasso,M., Waitz,R., Hou,Y., Rim,T., Greenberg,N.M., Shastri,N.,
            Fong,L. and Allison,J.P.
  TITLE     SPAS-1 (stimulator of prostatic adenocarcinoma-specific T
            cells)/SH3GLB2: A prostate tumor antigen identified by CTLA-4
            blockade
  JOURNAL   Proc Natl Acad Sci U S A 105 (9), 3509-3514 (2008)
   PUBMED   18303116
  REMARK    GeneRIF: identified a nonmutated HLA-A2-binding epitope in the
            human ortholog SH3GLB2, which primed T cells from healthy HLA-A2(+)
            individuals
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Liang,Z.D., Lippman,S.M., Wu,T.T., Lotan,R. and Xu,X.C.
  TITLE     RRIG1 mediates effects of retinoic acid receptor beta2 on tumor
            cell growth and gene expression through binding to and inhibition
            of RhoA
  JOURNAL   Cancer Res 66 (14), 7111-7118 (2006)
   PUBMED   16849557
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Li,J., Hawkins,I.C., Harvey,C.D., Jennings,J.L., Link,A.J. and
            Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 and its interacting
            proteins
  JOURNAL   Mol Cell Biol 23 (21), 7437-7447 (2003)
   PUBMED   14559993
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Pierrat,B., Simonen,M., Cueto,M., Mestan,J., Ferrigno,P. and
            Heim,J.
  TITLE     SH3GLB, a new endophilin-related protein family featuring an SH3
            domain
  JOURNAL   Genomics 71 (2), 222-234 (2001)
   PUBMED   11161816
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL592211.27.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.748879.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..366
                     /product="endophilin-B2 isoform d"
                     /note="SH3-containing protein SH3GLB2; SH3-domain
                     GRB2-like endophilin B2; endophilin-B2; SH3
                     domain-containing GRB2-like protein B2; retinoid
                     receptor-induced gene 1"
                     /calculated_mol_wt=41173
     Region          21..282
                     /region_name="BAR_Endophilin_B2"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of
                     Endophilin-B2; cd07617"
                     /db_xref="CDD:153301"
     Site            order(45,48..49,53,55..56,59..60,62..63,90..91,93..94,
                     97..98,100..101,104,118,121..122,244,247..248,250,254,
                     257..258,260..261,264..265,268..269,271..272,275..276,
                     278..279)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153301"
     Site            order(71,153,157,160,165..166,217,220,226)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153301"
     CDS             1..366
                     /gene="SH3GLB2"
                     /gene_synonym="PP6569; PP9455; RRIG1"
                     /coded_by="NM_001369914.1:178..1278"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:56904"
                     /db_xref="HGNC:HGNC:10834"
                     /db_xref="MIM:609288"
ORIGIN      
        1 mdfnmkklas dagifftrav qfteekfgqa ekteldahfe nllaradstk nwtekilrqt
       61 evllqpnpsa rveeflyekl drkvpsrvtn gellaqymad aaselgpttp ygktlikvae
      121 aekqlgaaer dfihtasisf ltplrnfleg dwktiskerr llqnrrldld ackarlkkak
      181 aaeakatceg dtvpdfqetr prnyilsasa salwndevdk aeqelrvaqt efdrqaevtr
      241 lllegissth vnhlrclhef vksqttyyaq cyrhmldlqk qlgssslsta clawtltgsl
      301 areatrrars lsptwncsar qvppspphsg lgrrgwaqpc hltcllvtql frvgrihpil
      361 slplvt
//
LOCUS       NP_062543                449 aa            linear   PRI 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein H2 [Homo sapiens].
ACCESSION   NP_062543
VERSION     NP_062543.1
DBSOURCE    REFSEQ: accession NM_019597.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Chen,X., Yang,H.T., Zhang,B., Phillips,J.W., Cheng,D., Rigo,F.,
            Witte,O.N., Xing,Y. and Black,D.L.
  TITLE     The RNA-binding proteins hnRNP H and F regulate splicing of a
            MYC-dependent HRAS exon in prostate cancer cells
  JOURNAL   Proc Natl Acad Sci U S A 120 (28), e2220190120 (2023)
   PUBMED   37399401
  REMARK    GeneRIF: The RNA-binding proteins hnRNP H and F regulate splicing
            of a MYC-dependent HRAS exon in prostate cancer cells.
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Gonzalez,J.N., Goldman,S., Carter,M.T. and Bain,J.M.
  TITLE     Rett-like Phenotypes in HNRNPH2-Related Neurodevelopmental Disorder
  JOURNAL   Genes (Basel) 14 (6), 1154 (2023)
   PUBMED   37372334
  REMARK    GeneRIF: Rett-like Phenotypes in HNRNPH2-Related Neurodevelopmental
            Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Kreienkamp,H.J., Wagner,M., Weigand,H., McConkie-Rossell,A.,
            McDonald,M., Keren,B., Mignot,C., Gauthier,J., Soucy,J.F.,
            Michaud,J.L., Dumas,M., Smith,R., Lobel,U., Hempel,M., Kubisch,C.,
            Denecke,J., Campeau,P.M., Bain,J.M. and Lessel,D.
  TITLE     Variant-specific effects define the phenotypic spectrum of
            HNRNPH2-associated neurodevelopmental disorders in males
  JOURNAL   Hum Genet 141 (2), 257-272 (2022)
   PUBMED   34907471
  REMARK    GeneRIF: Variant-specific effects define the phenotypic spectrum of
            HNRNPH2-associated neurodevelopmental disorders in males.
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Diez,J., Rajendrarao,S., Baajour,S.A., Sripadhan,P., Spicer,T.P.,
            Scampavia,L.D. and Minond,D.
  TITLE     Development and Pilot Screen of Novel High Content Assay for Down
            Regulators of Expression of Heterogenous Nuclear Ribonuclear
            Protein H2
  JOURNAL   Cell Physiol Biochem 55 (3), 265-276 (2021)
   PUBMED   34014051
  REMARK    GeneRIF: Development and Pilot Screen of Novel High Content Assay
            for Down Regulators of Expression of Heterogenous Nuclear
            Ribonuclear Protein H2.
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Honore,B., Rasmussen,H.H., Vorum,H., Dejgaard,K., Liu,X.,
            Gromov,P., Madsen,P., Gesser,B., Tommerup,N. and Celis,J.E.
  TITLE     Heterogeneous nuclear ribonucleoproteins H, H', and F are members
            of a ubiquitously expressed subfamily of related but distinct
            proteins encoded by genes mapping to different chromosomes
  JOURNAL   J Biol Chem 270 (48), 28780-28789 (1995)
   PUBMED   7499401
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Vorechovsky,I., Vetrie,D., Holland,J., Bentley,D.R., Thomas,K.,
            Zhou,J.N., Notarangelo,L.D., Plebani,A., Fontan,G., Ochs,H.D. et
            al.
  TITLE     Isolation of cosmid and cDNA clones in the region surrounding the
            BTK gene at Xq21.3-q22
  JOURNAL   Genomics 21 (3), 517-524 (1994)
   PUBMED   7959728
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Tsukada,S., Saffran,D.C., Rawlings,D.J., Parolini,O., Allen,R.C.,
            Klisak,I., Sparkes,R.S., Kubagawa,H., Mohandas,T., Quan,S. et al.
  TITLE     Deficient expression of a B cell cytoplasmic tyrosine kinase in
            human X-linked agammaglobulinemia
  JOURNAL   Cell 72 (2), 279-290 (1993)
   PUBMED   8425221
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Vetrie,D., Vorechovsky,I., Sideras,P., Holland,J., Davies,A.,
            Flinter,F., Hammarstrom,L., Kinnon,C., Levinsky,R., Bobrow,M. et
            al.
  TITLE     The gene involved in X-linked agammaglobulinaemia is a member of
            the src family of protein-tyrosine kinases
  JOURNAL   Nature 361 (6409), 226-233 (1993)
   PUBMED   8380905
  REMARK    Erratum:[Nature 1993 Jul 22;364(6435):362]
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Madhok,S. and Bain,J.
  TITLE     HNRNPH2-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108116
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA686966.1, U01923.1,
            AL035422.12 and AA758785.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to the subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has three
            repeats of quasi-RRM domains that binds to RNAs. It is very similar
            to the family member HNRPH1. This gene is thought to be involved in
            Fabray disease and X-linked agammaglobulinemia phenotype.
            Alternative splicing results in multiple transcript variants
            encoding the same protein. Read-through transcription between this
            locus and the ribosomal protein L36a gene has been observed.
            [provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.2736.1,
                                           SRR3476690.550271.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316594.6/ ENSP00000361927.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..449
                     /product="heterogeneous nuclear ribonucleoprotein H2"
                     /note="heterogeneous nuclear ribonucleoprotein H-prime;
                     FTP-3; hnRNP H'; hnRNP H2; heterogeneous nuclear
                     ribonucleoprotein H2 (H'); epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=49133
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P55795.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in Heterogeneous nuclear
                     ribonucleoprotein H2, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (P55795.1)"
     Region          10..88
                     /region_name="RRM1_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12729"
                     /db_xref="CDD:410128"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (P55795.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (P55795.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (P55795.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70333; propagated from
                     UniProtKB/Swiss-Prot (P55795.1)"
     Region          103..192
                     /region_name="RRM2_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12731"
                     /db_xref="CDD:410130"
     Site            233
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P31943;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P55795.1)"
     Region          234..433
                     /region_name="2 X 16 AA Gly-rich approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P55795.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (P55795.1)"
     Region          257..290
                     /region_name="zf-RNPHF"
                     /note="RNPHF zinc finger; pfam08080"
                     /db_xref="CDD:429823"
     Region          289..364
                     /region_name="RRM3_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 3 (RRM3) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12734"
                     /db_xref="CDD:410133"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P55795.1)"
     Region          354..392
                     /region_name="2 X 19 AA perfect repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P55795.1)"
     CDS             1..449
                     /gene="HNRNPH2"
                     /gene_synonym="FTP3; hnRNPH'; HNRPH'; HNRPH2; MRXSB;
                     NRPH2"
                     /coded_by="NM_019597.5:152..1501"
                     /db_xref="CCDS:CCDS14485.1"
                     /db_xref="GeneID:3188"
                     /db_xref="HGNC:HGNC:5042"
                     /db_xref="MIM:300610"
ORIGIN      
        1 mmlstegreg fvvkvrglpw scsadevmrf fsdckiqngt sgirfiytre grpsgeafve
       61 leseeevkla lkkdretmgh ryvevfksns vemdwvlkht gpnspdtand gfvrlrglpf
      121 gcskeeivqf fsgleivpng mtlpvdfqgr stgeafvqfa sqeiaekalk khkerighry
      181 ieifkssrae vrthydpprk lmamqrpgpy drpgagrgyn sigrgagfer mrrgaygggy
      241 ggyddyggyn dgygfgsdrf grdlnycfsg msdhrygdgg ssfqsttghc vhmrglpyra
      301 tendiynffs plnpmrvhie igpdgrvtge advefathed avaamakdka nmqhryvelf
      361 lnstagtsgg aydhsyvelf lnstagasgg aygsqmmggm glsnqssygg pasqqlsggy
      421 gggyggqssm sgydqvlqen ssdyqsnla
//
LOCUS       NP_001350114            3507 aa            linear   PRI 27-APR-2025
DEFINITION  CUB and sushi domain-containing protein 3 isoform 4 [Homo sapiens].
ACCESSION   NP_001350114 XP_016868500
VERSION     NP_001350114.1
DBSOURCE    REFSEQ: accession NM_001363185.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3507)
  AUTHORS   Wang,H., St Julien,K.R., Stevenson,D.K., Hoffmann,T.J., Witte,J.S.,
            Lazzeroni,L.C., Krasnow,M.A., Quaintance,C.C., Oehlert,J.W.,
            Jelliffe-Pawlowski,L.L., Gould,J.B., Shaw,G.M. and O'Brodovich,H.M.
  TITLE     A genome-wide association study (GWAS) for bronchopulmonary
            dysplasia
  JOURNAL   Pediatrics 132 (2), 290-297 (2013)
   PUBMED   23897914
REFERENCE   2  (residues 1 to 3507)
  AUTHORS   Divaris,K., Monda,K.L., North,K.E., Olshan,A.F., Lange,E.M.,
            Moss,K., Barros,S.P., Beck,J.D. and Offenbacher,S.
  TITLE     Genome-wide association study of periodontal pathogen colonization
  JOURNAL   J Dent Res 91 (7 Suppl), 21S-28S (2012)
   PUBMED   22699663
REFERENCE   3  (residues 1 to 3507)
  AUTHORS   Service,S.K., Verweij,K.J., Lahti,J., Congdon,E., Ekelund,J.,
            Hintsanen,M., Raikkonen,K., Lehtimaki,T., Kahonen,M., Widen,E.,
            Taanila,A., Veijola,J., Heath,A.C., Madden,P.A., Montgomery,G.W.,
            Sabatti,C., Jarvelin,M.R., Palotie,A., Raitakari,O., Viikari,J.,
            Martin,N.G., Eriksson,J.G., Keltikangas-Jarvinen,L., Wray,N.R. and
            Freimer,N.B.
  TITLE     A genome-wide meta-analysis of association studies of Cloninger's
            Temperament Scales
  JOURNAL   Transl Psychiatry 2 (5), e116 (2012)
   PUBMED   22832960
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3507)
  AUTHORS   Gylfe,A.E., Sirkia,J., Ahlsten,M., Jarvinen,H., Mecklin,J.P.,
            Karhu,A. and Aaltonen,L.A.
  TITLE     Somatic mutations and germline sequence variants in patients with
            familial colorectal cancer
  JOURNAL   Int J Cancer 127 (12), 2974-2980 (2010)
   PUBMED   21351276
  REMARK    GeneRIF: Nonsynonymous variants of CSMD3 is associated with
            familial colorectal cancer.
REFERENCE   5  (residues 1 to 3507)
  AUTHORS   Beuten,J., Gelfond,J.A., Martinez-Fierro,M.L., Weldon,K.S.,
            Crandall,A.C., Rojas-Martinez,A., Thompson,I.M. and Leach,R.J.
  TITLE     Association of chromosome 8q variants with prostate cancer risk in
            Caucasian and Hispanic men
  JOURNAL   Carcinogenesis 30 (8), 1372-1379 (2009)
   PUBMED   19528667
  REMARK    GeneRIF: Single-nucleotide polymorphisms in CSMD3 is associated
            with prostate cancer risk in hispanic men.
REFERENCE   6  (residues 1 to 3507)
  AUTHORS   Floris,C., Rassu,S., Boccone,L., Gasperini,D., Cao,A. and
            Crisponi,L.
  TITLE     Two patients with balanced translocations and autistic disorder:
            CSMD3 as a candidate gene for autism found in their common 8q23
            breakpoint area
  JOURNAL   Eur J Hum Genet 16 (6), 696-704 (2008)
   PUBMED   18270536
  REMARK    GeneRIF: Breakpoints on chromosomes 8 in both patients do not
            interrupt any known gene but both map in a region containing the
            CSMD3 gene, which thereby can be considered as a candidate for
            autistic spectrum disorders
REFERENCE   7  (residues 1 to 3507)
  AUTHORS   Riedl,S., Giedion,A., Schweitzer,K., Mullner-Eidenbock,A.,
            Grill,F., Frisch,H. and Ludecke,H.J.
  TITLE     Pronounced short stature in a girl with tricho-rhino-phalangeal
            syndrome II (TRPS II, Langer-Giedion syndrome) and growth hormone
            deficiency
  JOURNAL   Am J Med Genet A 131 (2), 200-203 (2004)
   PUBMED   15523607
  REMARK    GeneRIF: CSMD3 is deleted in a subject with combined
            tricho-rhino-phalangeal syndrome II with mental retardation and
            growth hormone deficiency.
REFERENCE   8  (residues 1 to 3507)
  AUTHORS   Shimizu,A., Asakawa,S., Sasaki,T., Yamazaki,S., Yamagata,H.,
            Kudoh,J., Minoshima,S., Kondo,I. and Shimizu,N.
  TITLE     A novel giant gene CSMD3 encoding a protein with CUB and sushi
            multiple domains: a candidate gene for benign adult familial
            myoclonic epilepsy on human chromosome 8q23.3-q24.1
  JOURNAL   Biochem Biophys Res Commun 309 (1), 143-154 (2003)
   PUBMED   12943675
  REMARK    GeneRIF: CSMD3 encodes a protein with CUB and sushi multiple
            domains and is a candidate gene for benign adult familial myoclonic
            epilepsy on human chromosome 8q23.3-q24.1
REFERENCE   9  (residues 1 to 3507)
  AUTHORS   Lau,W.L. and Scholnick,S.B.
  TITLE     Identification of two new members of the CSMD gene family
  JOURNAL   Genomics 82 (3), 412-415 (2003)
   PUBMED   12906867
  REMARK    GeneRIF: CSMD3 protein domain structure and the sequence of the
            cytoplasmic tail are highly conserved between mammals and fish.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB114604.1, AY210419.1, AB114605.1 and AB067481.2.
            
            On May 11, 2018 this sequence version replaced XP_016868500.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1968540, SAMEA1968968
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..3507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q23.3"
     Protein         1..3507
                     /product="CUB and sushi domain-containing protein 3
                     isoform 4"
                     /note="CUB and sushi domain-containing protein 3; CUB and
                     sushi multiple domains protein 3"
                     /calculated_mol_wt=384138
     Region          65..171
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(73,75,77,104,109,143,167,169,171)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          178..236
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(188,205)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          257..344
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Region          356..414
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(366,383)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          418..526
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(426,428,430,458,463,499,523,525)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          534..588
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(544,561)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          591..698
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(601,603,630,635,669,693,695,697..698)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          704..761
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(714,731)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          765..872
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(773,775,777,804,809,843,867,869,871..872)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          880..933
                     /region_name="CCP"
                     /note="Domain abundant in complement control proteins;
                     SUSHI repeat; short complement-like repeat (SCR);
                     smart00032"
                     /db_xref="CDD:214478"
     Site            order(890,907)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          937..1045
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(945,947,949,976,981,1014,1041,1043,1045)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          1052..1108
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(1062,1079)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          1111..1218
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(1119,1121,1123,1150,1155,1189,1213,1215,1217..1218)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          1224..1281
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(1234,1252)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          1284..1392
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(1293,1295,1297,1324,1329,1363,1387,1389,1391..1392)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          1398..1455
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(1408,1425)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          1458..1565
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(1466,1468,1470,1497,1502,1536,1560,1562,1564..1565)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          <1567..1764
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          1739..1846
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(1749,1751,1778,1783,1817,1841,1843,1845..1846)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          1852..1907
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(1862,1879)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          1911..2018
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(1919,1921,1923,1950,1955,1989,2013,2015,2017..2018)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          2024..2080
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(2034,2051)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          2083..2189
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(2091,2093,2095,2122,2127,2161,2184,2186,2188..2189)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          2195..2253
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(2205,2224)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          2260..2366
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(2266,2268,2270,2297,2302,2337,2361,2363,2365..2366)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          2369..2428
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(2379,2397)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          2427..2671
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          2556..2791
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          2728..2968
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          2968..3207
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          3211..3267
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(3221,3239)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     CDS             1..3507
                     /gene="CSMD3"
                     /coded_by="NM_001363185.1:86..10609"
                     /note="isoform 4 is encoded by transcript variant d"
                     /db_xref="GeneID:114788"
                     /db_xref="HGNC:HGNC:19291"
                     /db_xref="MIM:608399"
ORIGIN      
        1 mkgirkgesr akeskpwepg krrcakcgrl dfilmkkmgi ksgftfwnlv flltvscvkg
       61 fiytcggtlk glngtiespg fpygypngan ctwviiaeer nriqivfqsf aleeeydyls
      121 lydghphptn frtrltgfhl pppvtstksv fslrltsdfa vsahgfkvyy eelqssscgn
      181 pgvppkgvly gtrfdvgdki ryscvtgyil dghpqltcia nsvntaswdf pvpicraeda
      241 cggtmrgssg iisspsfpne yhnnadctwt ivaepgdtis liftdfqmee kydyleiegs
      301 epptiwlsgm nipppiisnk nwlrlhfvtd snhryrgfsa pyqvneggik tasnlcpdpg
      361 epengkrigs dfslgstvqf scdedyvlqg aksitcqria evfaawsdhr pvckvktcgs
      421 nlqgpsgtft spnfpfqyds naqcvwvita vntnkviqin feefdleigy dtltigdgge
      481 vgdprtvlqv ltgsfvpdli vsmssqmwlh lqtdesvgsv gfkvnykeie kescgdpgtp
      541 lygiregdgf snrdvlrfec qfgfeligek sivcqennqw sanipicifp clsnftapmg
      601 tvlspdypeg ygnnlnciwt iisdpgsrih lsfndfdles qfdflavkdg dspespilgt
      661 ftgaevpshl tsnshilrle fqadhsmsgr gfnityntfg hnecpdpgip inarrfgdnf
      721 qlgssisvic eegfiktqgt etitcilmdg kvmwsglipk cgapcgghfs apsgvilspg
      781 wpgyykdsln cewvieaepg hsikitferf qtelnydvle vhdgpnllsp llgsyngtqv
      841 pqflfsssnf iyllfttdns rsnngfkihy esvtvntysc ldpgipvhgr ryghdfsigs
      901 tvsfscdsgy rlsheepllc eknhwwshpl ptcdalcggd vrgpsgtils pgypefypns
      961 lnctwtvdvt hgkgvqfnfh tfhledhhdy llitengsft qplarltgsd lpptinagly
     1021 gnfraqlrfi sdfsisyegf nitfseynle pcedpgipqy gsrigfnfgi gdtltfscss
     1081 gyrlegtsei iclgggrrvw saplprcvae cgasatnneg illspnypln yennheciys
     1141 iqvqagkgin isartfhlaq gdvlkiydgk dktthllgaf tgasmrgltl sstsnqlwle
     1201 fnsdtegtde gfqlvytsfe lshcedpgip qfgykisdqg hfagstiiyg cnpgytlhgs
     1261 sllkcmtger rawdyplpsc iaecggrfkg essgrilspg ypfpydnnlr cmwmievdpg
     1321 nivslqflaf dteashdilr vwdgppendm llkeisgsli pegihstlni vtiqfdtdfy
     1381 isksgfaiqf sssvatacrd pgvpmngtrn gdgrepgdtv vfqcdpgyel qgeeritciq
     1441 venryfwqps ppvciapcgg nltgssgfil spnfphpyph srdcdwtitv nadyvislaf
     1501 isfsiepnyd flyiydgpds nspligsfqd sklperiess sntmhlafrs dgsvsytgfh
     1561 leykaklres cfdpgnimng trlgmdyklg stvtyycdag yvlqgystlt cimgddgrpg
     1621 wnralpscha pcgsrstgse gtvlspnypk nysvghncvy siavpkefav prtsstqcss
     1681 vpeprfgrri gnefavgssv lfdcnpgyil hgsiaircet vpnslaqwnd slptcivpcg
     1741 giltkrkgti lspgypepyd nnlncvwkit vpegagiqvq vvsfatehnw dsldfydggd
     1801 nnaprlgsys gttiphllns tsnnlylnfq sdisvsaagf hleytaigld scpepqtpss
     1861 gikigdrymv gdvvsfqcdq gyslqghshi tcmpgpvrrw nypipiclaq cggamsdfsg
     1921 vilspgfpgn ypssldctwt inlpigfgvh lqfvnfstet ihdylevrsg ssetstvigr
     1981 lsgpqipssl fstthetsly fhsdysqnkq gfhivyqayq lqscpdprpf rngfvigndf
     2041 tvgqtisfec fpgytligns altclhgvsr nwnhplprce alcggnitam ngtiyspgyp
     2101 deypnfqdcf wlvrvppgng iyinftvlqt epiydfitvw dgpdqnspqi gqfsgntale
     2161 svystsnqil ikfhsdftts gffvlsyhay qlrvcqpppp vpnaeilted defeigdiir
     2221 yqclpgftlv gnailtcrlg erlqmdgapp vcqvlcpane lrldstgvil spgypdsypn
     2281 lqmcawsisv ekgynitmfv effqtekefd vlqvydgpni qspvlislsg dyssafnits
     2341 nghevflqws adhgnnkkgf riryiafycs tpespphgyi isqtggqlns vvrwacdrgf
     2401 rlvgkssavc rkssygyhaw dapvpacqai scgipkaptn ggilttdylv gtrvtyfcnd
     2461 gyrlsskelt tavcqsdgtw snhnktprcv vvtcpsinsf ilehgrwriv ngshyeyktk
     2521 vvfscdpgyh glgpasiecl pngtwswrne rpycqiiscg elptppngnk igtqtsygst
     2581 aiftcdlgfm lvgsavrecl ssglwseset rclaghcgip elivngqvig enygyrdtvv
     2641 yqcnpgfrli gssvricqqd hnwsgqlpsc vpvscghpgs piygrtsgng fnfndvvtfs
     2701 cnigylmqgp tkaqcqanrq wshpppmckv vncsdpgipa nskreskieh gnftygtvvf
     2761 ydcnpgyflf gssvlicqpn gqwdkplpec imidcghpgv ppnavlsgek ytfgstvhys
     2821 ctgkrsllgq ssrtcqlngh wsgsqphcsg datgtcgdpg tpghgsrqes nfrtkstvry
     2881 acdtgyilhg seertclang swtgrqpeck avqcgnpgtt angkvfridg ttfsssviys
     2941 cmegyilsgp svrqctangt wsgtlpncti iscgdpgipa nglrygddyv vgqnvsymcq
     3001 pgytmelngs rirtctingt wsgvmptcra vtcptppqis ngrlegtnfd wgfsisyics
     3061 pgyelsfpav ltcvgngtws gevpqclpkf cgdpgipaqg kregksfiyq sevsfscnfp
     3121 filvgsstri cqadgtwsgs sphcieptqt scenpgvprh gsqnntfgfq vgsvvqfhck
     3181 kghllqgstt rtclpdltws giqpeciphs ckqpetpaha nvvgmdlpsh gytliytcqp
     3241 gfflaggteh rvcrsdntwt gkvpiceags kilvkdprpa lgtpspklsv pddvfaqnyi
     3301 wkgsynfkgr kqpmtltvts fnastgrvna tlsnsnmell lsgvyksqea rlmlriylik
     3361 vpahasvkkm keenwamdgf vsaepdgaty vfqgfiqgkd ygqfglqrlg lnmsegsnss
     3421 nqphgtnsss vaiailvpff alifagfgfy lykqrtapkt qytgcsvhen nngqaafenp
     3481 mydtnaksve gkavrfdpnl ntvctmv
//
LOCUS       NP_077011                554 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 426 isoform 1 [Homo sapiens].
ACCESSION   NP_077011 XP_005260132
VERSION     NP_077011.1
DBSOURCE    REFSEQ: accession NM_024106.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Blandin,G., Marchand,S., Charton,K., Daniele,N., Gicquel,E.,
            Boucheteil,J.B., Bentaib,A., Barrault,L., Stockholm,D., Bartoli,M.
            and Richard,I.
  TITLE     A human skeletal muscle interactome centered on proteins involved
            in muscular dystrophies: LGMD interactome
  JOURNAL   Skelet Muscle 3 (1), 3 (2013)
   PUBMED   23414517
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Yang,Z., Wen,H.J., Minhas,V. and Wood,C.
  TITLE     The zinc finger DNA-binding domain of K-RBP plays an important role
            in regulating Kaposi's sarcoma-associated herpesvirus RTA-mediated
            gene expression
  JOURNAL   Virology 391 (2), 221-231 (2009)
   PUBMED   19592062
  REMARK    GeneRIF: These findings suggest that the DNA-binding activity of
            K-RBP plays an important role in repressing viral promoter
            activity.
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Yang,Z., Yan,Z. and Wood,C.
  TITLE     Kaposi's sarcoma-associated herpesvirus transactivator RTA promotes
            degradation of the repressors to regulate viral lytic replication
  JOURNAL   J Virol 82 (7), 3590-3603 (2008)
   PUBMED   18216089
  REMARK    GeneRIF: It was found that herpesvirus 8 RTA can induce K-RBP
            degradation through the ubiquitin-proteasome pathway and that two
            regions in RTA are responsible.
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Yang,Z. and Wood,C.
  TITLE     The transcriptional repressor K-RBP modulates RTA-mediated
            transactivation and lytic replication of Kaposi's
            sarcoma-associated herpesvirus
  JOURNAL   J Virol 81 (12), 6294-6306 (2007)
   PUBMED   17409159
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Wang,S., Liu,S., Wu,M.H., Geng,Y. and Wood,C.
  TITLE     Identification of a cellular protein that interacts and synergizes
            with the RTA (ORF50) protein of Kaposi's sarcoma-associated
            herpesvirus in transcriptional activation
  JOURNAL   J Virol 75 (24), 11961-11973 (2001)
   PUBMED   11711586
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP245135.1, BC001791.1 and
            AC008567.5.
            
            On Aug 31, 2013 this sequence version replaced XP_005260132.1.
            
            Summary: Kaposi's sarcoma-associated herpesvirus (KSHV) can be
            reactivated from latency by the viral protein RTA. The protein
            encoded by this gene is a zinc finger transcriptional repressor
            that interacts with RTA to modulate RTA-mediated reactivation of
            KSHV. While the encoded protein can repress KSHV reactivation, RTA
            can induce degradation of this protein through the
            ubiquitin-proteasome pathway to overcome the repression. Several
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.183926.1, BC001791.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253115.7/ ENSP00000253115.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..554
                     /product="zinc finger protein 426 isoform 1"
                     /note="KSHV RTA binding protein; CTC-543D15.7"
                     /calculated_mol_wt=62975
     Region          42..98
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          148..168
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          176..214
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          224..246
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(287,289,291,293..294,297..298,301,315,317,321..322,
                     325..326,329,343,345,347,349..350,353..354,357)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          294..319
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <334..486
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          422..442
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          450..470
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(455,457,459,461..462,465..466,469,483,485,489..490,
                     493..494,497,511,513,515,517..518,521..522,525)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          478..498
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          490..515
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          506..526
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..543
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          534..554
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..554
                     /gene="ZNF426"
                     /gene_synonym="K-RBP"
                     /coded_by="NM_024106.3:283..1947"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12215.1"
                     /db_xref="GeneID:79088"
                     /db_xref="HGNC:HGNC:20725"
ORIGIN      
        1 maaadlshgh ylsgdpvclh eektpagriv adcltdcyqd svtfddvavd ftqeewtlld
       61 stqrslysdv mlenyknlat vggqiikpsl iswleqeesr tvqggvlqgw emrletqwsi
      121 lqqdflrgqt sigiqlegkh ngrelcdceq cgevfsehsc lkthvrtqst gnthdcnqyg
      181 kdfltlcekt stgeklsefn qsekifsltp nivyqrtstq eksfecshcg ksfinesylq
      241 ahmrthngek lyewrnygpg fidstslsvl ietlnakkpy kckecgkgyr ypaylsihmr
      301 thtgekpyec kecgkafnys nsfqihgrth tgekpyvcke cgkaftqysg lsmhvrshsg
      361 dkpyeckecg ksfltssrli qhirthtgek pfvcvecgka favssnlsgh lrthteekac
      421 eckicgkvfg ypsclnnhmr thsaqkpytc kecgkafnys thlkihmrih tgekpyeckq
      481 cgkafshsss fqiherthtg ekpyeckecg kaftcsssfr ihekthteek pykcqqcgka
      541 yshprslrrh eqih
//
LOCUS       NP_001001173            1288 aa            linear   MAM 27-APR-2025
DEFINITION  5-oxoprolinase [Bos taurus].
ACCESSION   NP_001001173 XP_005215194 XP_594260
VERSION     NP_001001173.2
DBSOURCE    REFSEQ: accession NM_001001173.2
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 1288)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   2  (residues 1 to 1288)
  AUTHORS   Watanabe,T., Abe,K., Ishikawa,H. and Iijima,Y.
  TITLE     Bovine 5-oxo-L-prolinase: simple assay method, purification, cDNA
            cloning, and detection of mRNA in the coronary artery
  JOURNAL   Biol Pharm Bull 27 (3), 288-294 (2004)
   PUBMED   14993790
  REMARK    GeneRIF: amino acid sequence determined
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000014.1, EV743436.1 and AW461711.1.
            
            On or before Jan 19, 2018 this sequence version replaced
            XP_005215194.1, NP_001001173.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6764281.29680.1,
                                           SRR6764281.30795.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA6648753, SAMEA6648754
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1288
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="14"
                     /map="14"
                     /breed="Hereford"
     Protein         1..1288
                     /product="5-oxoprolinase"
                     /EC_number="3.5.2.9"
                     /note="5-oxo-L-prolinase; pyroglutamase"
                     /calculated_mol_wt=137224
     Region          1..1258
                     /region_name="PLN02666"
                     /note="5-oxoprolinase"
                     /db_xref="CDD:215358"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O14841; propagated from
                     UniProtKB/Swiss-Prot (Q75WB5.2)"
     Region          1249..1269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75WB5.2)"
     Site            1265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97608; propagated from
                     UniProtKB/Swiss-Prot (Q75WB5.2)"
     CDS             1..1288
                     /gene="OPLAH"
                     /gene_synonym="5-OPase"
                     /coded_by="NM_001001173.2:65..3931"
                     /db_xref="BGD:BT11542"
                     /db_xref="GeneID:408006"
                     /db_xref="VGNC:VGNC:53869"
ORIGIN      
        1 mggpegrfhf aidrggtftd vfaqcpgghv rvlkllsedp anyvdapteg irrileqegg
       61 vllprdrpld tsriasirmg ttvatnalle rqgervallv trgfrdllhv gtqaradlfd
      121 lavpmpetly eevlevderv vlyrgepgag tpvkgctgdl levqqpvdlg glrgklegll
      181 srgirslavv lmhsytwaqh eqqvgalare lgfthvslss eampmvrivp rghtacaday
      241 ltptiqryvq gfrrgfqgql kdvqvlfmrs dgglapmdsf sgsravlsgp aggvvgysat
      301 tyrveggqpv igfdmggtst dvsryagefe hvfeastagv tlqapqldin tvaagggsrl
      361 ffrsglfvvg pesagahpgp acyrkggpvt vtdanlvlgr llpasfpcif gpgedqplsp
      421 easrkaleav atevnsfltn gpcpasplsl eevamgfvrv aneamcrpir altqarghdp
      481 sahvlacfgg aggqhacaia ralgmdtvhi hrhsgllsal glaladvvhe aqepcslpya
      541 petfaqldqr lgrleeqcve alraqgfprs qistesflhl ryqgtdcalm vsahqhpasa
      601 rspragdfga afverymref gfiiperpvv vddvrvrgtg ssslrledvp kahsgpprvd
      661 kmtqcyfegg yqetpvyllg elgcghklqg pcliidsnst ilvepgcqae vtetgdiris
      721 vgaetasvvg tqldpihlsi fshrfmsiae qmgrilqrta istnikerld fscalfgpdg
      781 glvsnaphip vhlgamqetv qfqiqqlgad lhpgdvllsn hpsaggshlp dltvitpvfw
      841 pgqtrpvfyv asrghhadig gitpgsmpph stslqqegav flsfklvhgg vfqeeavtea
      901 lrapgkipgc sgtrnlhdnl sdlraqvaan qkgiqlvgel igqygldvvq aymghiqana
      961 elavrdmlra fgtarqargl plevsaedhm ddgspirlrv qinmsqgsav fdfsgsgpev
     1021 fgnlnaprai tlsaliyclr clvgrdipln qgclapvrvv ipkgsildps pdaavvggnv
     1081 ltsqrvvdvi lgafgacaas qgcmnnvtlg nahmgyyetv aggagagpgw hgrsgvhshm
     1141 tntritdpei lesrypvilr rfelrlgsgg rgrfrggdgi irellfreea llsvlterra
     1201 fqpyglmgge pgarglnlli rkdgrtvnlg gktsvpvypg dvfclhtpgg ggygdpedpa
     1261 plpgsplqpl afpergsvye yrraqeav
//
LOCUS       NP_000980                115 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein eL30 [Homo sapiens].
ACCESSION   NP_000980
VERSION     NP_000980.1
DBSOURCE    REFSEQ: accession NM_000989.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Lee,J.H., Han,J.H., Kim,H., Park,S.M., Joe,E.H. and Jou,I.
  TITLE     Parkinson's disease-associated LRRK2-G2019S mutant acts through
            regulation of SERCA activity to control ER stress in astrocytes
  JOURNAL   Acta Neuropathol Commun 7 (1), 68 (2019)
   PUBMED   31046837
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Behrmann,E., Loerke,J., Budkevich,T.V., Yamamoto,K., Schmidt,A.,
            Penczek,P.A., Vos,M.R., Burger,J., Mielke,T., Scheerer,P. and
            Spahn,C.M.
  TITLE     Structural snapshots of actively translating human ribosomes
  JOURNAL   Cell 161 (4), 845-857 (2015)
   PUBMED   25957688
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Khatter,H., Myasnikov,A.G., Natchiar,S.K. and Klaholz,B.P.
  TITLE     Structure of the human 80S ribosome
  JOURNAL   Nature 520 (7549), 640-645 (2015)
   PUBMED   25901680
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Martin,I., Kim,J.W., Lee,B.D., Kang,H.C., Xu,J.C., Jia,H.,
            Stankowski,J., Kim,M.S., Zhong,J., Kumar,M., Andrabi,S.A.,
            Xiong,Y., Dickson,D.W., Wszolek,Z.K., Pandey,A., Dawson,T.M. and
            Dawson,V.L.
  TITLE     Ribosomal protein s15 phosphorylation mediates LRRK2
            neurodegeneration in Parkinson's disease
  JOURNAL   Cell 157 (2), 472-485 (2014)
   PUBMED   24725412
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 115)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 115)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 115)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 115)
  AUTHORS   Feo,S., Davies,B. and Fried,M.
  TITLE     The mapping of seven intron-containing ribosomal protein genes
            shows they are unlinked in the human genome
  JOURNAL   Genomics 13 (1), 201-207 (1992)
   PUBMED   1577483
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BM785413.1 and BC095426.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L30E family of ribosomal proteins. It is located in the
            cytoplasm. This gene is co-transcribed with the U72 small nucleolar
            RNA gene, which is located in its fourth intron. As is typical for
            genes encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV761808.1, BE439872.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287038.8/ ENSP00000287038.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.2"
     Protein         1..115
                     /product="large ribosomal subunit protein eL30"
                     /note="60S ribosomal protein L30"
                     /calculated_mol_wt=12653
     Region          2..107
                     /region_name="PTZ00106"
                     /note="60S ribosomal protein L30; Provisional"
                     /db_xref="CDD:185450"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62888.2)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62888.2)"
     Site            26
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62888.2)"
     CDS             1..115
                     /gene="RPL30"
                     /gene_synonym="eL30; L30"
                     /coded_by="NM_000989.4:71..418"
                     /db_xref="CCDS:CCDS34928.1"
                     /db_xref="GeneID:6156"
                     /db_xref="HGNC:HGNC:10333"
                     /db_xref="MIM:180467"
ORIGIN      
        1 mvaakktkks lesinsrlql vmksgkyvlg ykqtlkmirq gkaklvilan ncpalrksei
       61 eyyamlaktg vhhysgnnie lgtacgkyyr vctlaiidpg dsdiirsmpe qtgek
//
LOCUS       NP_001350291             602 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 3B
            isoform 6 [Mus musculus].
ACCESSION   NP_001350291
VERSION     NP_001350291.1
DBSOURCE    REFSEQ: accession NM_001363362.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Chang,W.H., Choi,S.H., Moon,B.S., Cai,M., Lyu,J., Bai,J., Gao,F.,
            Hajjali,I., Zhao,Z., Campbell,D.B., Weiner,L.P. and Lu,W.
  TITLE     Smek1/2 is a nuclear chaperone and cofactor for cleaved Wnt
            receptor Ryk, regulating cortical neurogenesis
  JOURNAL   Proc Natl Acad Sci U S A 114 (50), E10717-E10725 (2017)
   PUBMED   29180410
  REMARK    GeneRIF: Smek1 and Smek2 (Smek1/2) are key factors in the Ryk
            signaling pathway
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Moon,B.S., Yun,H.M., Chang,W.H., Steele,B.H., Cai,M., Choi,S.H. and
            Lu,W.
  TITLE     Smek promotes corticogenesis through regulating Mbd3's stability
            and Mbd3/NuRD complex recruitment to genes associated with
            neurogenesis
  JOURNAL   PLoS Biol 15 (5), e2001220 (2017)
   PUBMED   28467410
  REMARK    GeneRIF: Smek/Mbd3 interaction regulates neuronal gene expression
            and neuronal differentiation during cortical development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Lee,D.H., Acharya,S.S., Kwon,M., Drane,P., Guan,Y., Adelmant,G.,
            Kalev,P., Shah,J., Pellman,D., Marto,J.A. and Chowdhury,D.
  TITLE     Dephosphorylation enables the recruitment of 53BP1 to double-strand
            DNA breaks
  JOURNAL   Mol Cell 54 (3), 512-525 (2014)
   PUBMED   24703952
REFERENCE   5  (residues 1 to 602)
  AUTHORS   Krol,A.J., Roellig,D., Dequeant,M.L., Tassy,O., Glynn,E.,
            Hattem,G., Mushegian,A., Oates,A.C. and Pourquie,O.
  TITLE     Evolutionary plasticity of segmentation clock networks
  JOURNAL   Development 138 (13), 2783-2792 (2011)
   PUBMED   21652651
REFERENCE   6  (residues 1 to 602)
  AUTHORS   Lyu,J., Jho,E.H. and Lu,W.
  TITLE     Smek promotes histone deacetylation to suppress transcription of
            Wnt target gene brachyury in pluripotent embryonic stem cells
  JOURNAL   Cell Res 21 (6), 911-921 (2011)
   PUBMED   21423269
  REMARK    GeneRIF: the Smek-containing protein phosphatase 4 complex
            represses transcription of Wnt-responsive development-related genes
            through histone deacetylation, and that this complex is essential
            for embryonic stem cell pluripotency maintenance
REFERENCE   7  (residues 1 to 602)
  AUTHORS   Thiagarajan,R.D., Georgas,K.M., Rumballe,B.A., Lesieur,E.,
            Chiu,H.S., Taylor,D., Tang,D.T., Grimmond,S.M. and Little,M.H.
  TITLE     Identification of anchor genes during kidney development defines
            ontological relationships, molecular subcompartments and regulatory
            pathways
  JOURNAL   PLoS One 6 (2), e17286 (2011)
   PUBMED   21386911
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 602)
  AUTHORS   Yoon,Y.S., Lee,M.W., Ryu,D., Kim,J.H., Ma,H., Seo,W.Y., Kim,Y.N.,
            Kim,S.S., Lee,C.H., Hunter,T., Choi,C.S., Montminy,M.R. and
            Koo,S.H.
  TITLE     Suppressor of MEK null (SMEK)/protein phosphatase 4 catalytic
            subunit (PP4C) is a key regulator of hepatic gluconeogenesis
  JOURNAL   Proc Natl Acad Sci U S A 107 (41), 17704-17709 (2010)
   PUBMED   20876121
REFERENCE   9  (residues 1 to 602)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
REFERENCE   10 (residues 1 to 602)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX000351.17 and BX294116.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK165940.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 16.46 cM"
     Protein         1..602
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 3B isoform 6"
                     /note="serine/threonine-protein phosphatase 4 regulatory
                     subunit 3B; SMEK homolog 2, suppressor of mek1"
                     /calculated_mol_wt=69376
     Region          7..>65
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          168..359
                     /region_name="PP4R3"
                     /note="Phosphatase 4 regulatory subunit 3; pfam04802"
                     /db_xref="CDD:461435"
     CDS             1..602
                     /gene="Ppp4r3b"
                     /gene_synonym="mKIAA1387; Smek2"
                     /coded_by="NM_001363362.1:331..2139"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:104570"
                     /db_xref="MGI:MGI:2144474"
ORIGIN      
        1 msdtrrrvkv ytlnedrqwd drgtghvsst yveelkgmsl lvraesdgsl lleskinpnt
       61 ayqkqqdtli vwseaenydl alsfqekagc deiwekicqv qgkdpsvevt qdlideseee
      121 rfeempetsh lidlpacels kleeiadlvt svlsspirre klalaleneg yikkllqlfq
      181 acenlenteg lhhlyeiirg ilflnkatlf evmfsdecim dvvgcleydp alaqpkrhre
      241 fltktakfke vipitdselr qkihqtyrvq yiqdiilptp svfeenflst ltsfiffnkv
      301 eivsmlqede kflsevfaql tdeatdddkr relvnffkef cafsqtlqpq nrdaffktla
      361 klgilpalei vmgmddlqvr saatdifsyl vefspsmvre fvmqeaqqsd ddvllinvvi
      421 eqmicdtdpe lggavqlmgl lrtlidpenm lattnkteks eflnffynhc mhvltapllt
      481 ntsedkcekd nyqtaqllal ilelltfcve hhtyhiknyi mnkdllrrvl vlmnskhtfl
      541 alcalrfmrr iiglkdefyn ryitkgnlfe pvinalldng trynllnsav ielfefirvv
      601 sl
//
LOCUS       NP_001349673             197 aa            linear   ROD 27-APR-2025
DEFINITION  serine racemase isoform 4 [Mus musculus].
ACCESSION   NP_001349673
VERSION     NP_001349673.1
DBSOURCE    REFSEQ: accession NM_001362744.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Wang,Y., Xu,D., Zhao,Y., Zhu,H., Xiu,X., Jiang,H., Liu,Y., Shan,G.
            and Wu,S.
  TITLE     Age- and Sex-Specific Regulation of Serine Racemase in the Retina
            of an Alzheimer's Disease Mouse
  JOURNAL   Invest Ophthalmol Vis Sci 66 (1), 36 (2025)
   PUBMED   39813057
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Barragan,E.V., Anisimova,M., Vijayakumar,V., Coblentz,A.,
            Park,D.K., Salaka,R.J., Nisan,A.F.K., Petshow,S., Dore,K., Zito,K.
            and Gray,J.A.
  TITLE     d-Serine Inhibits Non-ionotropic NMDA Receptor Signaling
  JOURNAL   J Neurosci 44 (32), e0140242024 (2024)
   PUBMED   38942470
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Radzishevsky,I., Odeh,M., Bodner,O., Zubedat,S., Shaulov,L.,
            Litvak,M., Esaki,K., Yoshikawa,T., Agranovich,B., Li,W.H.,
            Radzishevsky,A., Gottlieb,E., Avital,A. and Wolosker,H.
  TITLE     Impairment of serine transport across the blood-brain barrier by
            deletion of Slc38a5 causes developmental delay and motor
            dysfunction
  JOURNAL   Proc Natl Acad Sci U S A 120 (42), e2302780120 (2023)
   PUBMED   37812701
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Ni,X., Inoue,R., Wu,Y., Yoshida,T., Yaku,K., Nakagawa,T., Saito,T.,
            Saido,T.C., Takao,K. and Mori,H.
  TITLE     Regional contributions of D-serine to Alzheimer's disease pathology
            in male AppNL-G-F/NL-G-F mice
  JOURNAL   Front Aging Neurosci 15, 1211067 (2023)
   PUBMED   37455930
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 197)
  AUTHORS   Cook,S.P., Galve-Roperh,I., Martinez del Pozo,A. and
            Rodriguez-Crespo,I.
  TITLE     Direct calcium binding results in activation of brain serine
            racemase
  JOURNAL   J Biol Chem 277 (31), 27782-27792 (2002)
   PUBMED   12021263
  REMARK    GeneRIF: Direct calcium binding results in activation in brain
REFERENCE   7  (residues 1 to 197)
  AUTHORS   Panizzutti,R., De Miranda,J., Ribeiro,C.S., Engelender,S. and
            Wolosker,H.
  TITLE     A new strategy to decrease N-methyl-D-aspartate (NMDA) receptor
            coactivation: inhibition of D-serine synthesis by converting serine
            racemase into an eliminase
  JOURNAL   Proc Natl Acad Sci U S A 98 (9), 5294-5299 (2001)
   PUBMED   11309496
REFERENCE   8  (residues 1 to 197)
  AUTHORS   De Miranda,J., Santoro,A., Engelender,S. and Wolosker,H.
  TITLE     Human serine racemase: moleular cloning, genomic organization and
            functional analysis
  JOURNAL   Gene 256 (1-2), 183-188 (2000)
   PUBMED   11054547
REFERENCE   9  (residues 1 to 197)
  AUTHORS   Wolosker,H., Blackshaw,S. and Snyder,S.H.
  TITLE     Serine racemase: a glial enzyme synthesizing D-serine to regulate
            glutamate-N-methyl-D-aspartate neurotransmission
  JOURNAL   Proc Natl Acad Sci U S A 96 (23), 13409-13414 (1999)
   PUBMED   10557334
REFERENCE   10 (residues 1 to 197)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL604066.9 and AK079343.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK079343.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 45.76 cM"
     Protein         1..197
                     /product="serine racemase isoform 4"
                     /EC_number="4.3.1.17"
                     /EC_number="5.1.1.18"
                     /EC_number="4.3.1.18"
                     /note="D-serine dehydratase; L-serine dehydratase;
                     D-serine ammonia-lyase; L-serine ammonia-lyase"
                     /calculated_mol_wt=20741
     Region          <1..180
                     /region_name="Trp-synth-beta_II"
                     /note="Tryptophan synthase beta superfamily (fold type
                     II); this family of pyridoxal phosphate (PLP)-dependent
                     enzymes catalyzes beta-replacement and beta-elimination
                     reactions. This CD corresponds to
                     aminocyclopropane-1-carboxylate deaminase (ACCD),
                     tryptophan...; cl00342"
                     /db_xref="CDD:444852"
     CDS             1..197
                     /gene="Srr"
                     /gene_synonym="M100034; Rgsc34; Srs"
                     /coded_by="NM_001362744.1:393..986"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:27364"
                     /db_xref="MGI:MGI:1351636"
ORIGIN      
        1 mqetegilvh pnqepaviag qgtialevln qvplvdalvv pvggggmvag iaitikalkp
       61 svkvyaaeps naddcyqskl kgeltpnlhp petiadgvks siglntwpii rdlvddvftv
      121 tedeikyatq lvwgrmklli eptagvalaa vlsqhfqtvs pevknvcivl sggnvdltsl
      181 nwvgqaerpa pyqtvsv
//
LOCUS       NP_001353189             110 aa            linear   PRI 27-APR-2025
DEFINITION  protein archease isoform 5 [Homo sapiens].
ACCESSION   NP_001353189 XP_011539637
VERSION     NP_001353189.1
DBSOURCE    REFSEQ: accession NM_001366260.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Mason,C.C., Khorashad,J.S., Tantravahi,S.K., Kelley,T.W.,
            Zabriskie,M.S., Yan,D., Pomicter,A.D., Reynolds,K.R., Eiring,A.M.,
            Kronenberg,Z., Sherman,R.L., Tyner,J.W., Dalley,B.K., Dao,K.H.,
            Yandell,M., Druker,B.J., Gotlib,J., O'Hare,T. and Deininger,M.W.
  TITLE     Age-related mutations and chronic myelomonocytic leukemia
  JOURNAL   Leukemia 30 (4), 906-913 (2016)
   PUBMED   26648538
  REMARK    GeneRIF: ARCH mutation is associated with chronic myelomonocytic
            leukemia.
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Jurkin,J., Henkel,T., Nielsen,A.F., Minnich,M., Popow,J.,
            Kaufmann,T., Heindl,K., Hoffmann,T., Busslinger,M. and Martinez,J.
  TITLE     The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA
            and controls antibody secretion in plasma cells
  JOURNAL   EMBO J 33 (24), 2922-2936 (2014)
   PUBMED   25378478
  REMARK    GeneRIF: RTCB, the catalytic subunit of the tRNA ligase complex,
            and its co-factor archease mediate XBP1 mRNA splicing both in vitro
            and in vivo.
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Popow,J., Jurkin,J., Schleiffer,A. and Martinez,J.
  TITLE     Analysis of orthologous groups reveals archease and DDX1 as tRNA
            splicing factors
  JOURNAL   Nature 511 (7507), 104-107 (2014)
   PUBMED   24870230
  REMARK    GeneRIF: archease (also called ZBTB8OS), a protein of unknown
            function, is required for full activity of the human tRNA ligase
            complex and, in cooperation with DDX1, facilitates the formation of
            an RTCB-guanylate intermediate central to mammalian RNA ligation
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Popow,J., Englert,M., Weitzer,S., Schleiffer,A., Mierzwa,B.,
            Mechtler,K., Trowitzsch,S., Will,C.L., Luhrmann,R., Soll,D. and
            Martinez,J.
  TITLE     HSPC117 is the essential subunit of a human tRNA splicing ligase
            complex
  JOURNAL   Science 331 (6018), 760-764 (2011)
   PUBMED   21311021
REFERENCE   7  (residues 1 to 110)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 110)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2 and AL033529.25.
            
            On Sep 27, 2018 this sequence version replaced XP_011539637.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138528.213349.1,
                                           ERR3218373.114973.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..110
                     /product="protein archease isoform 5"
                     /note="protein archease; archease-like protein; archease
                     (ARCH); zinc finger and BTB domain-containing opposite
                     strand protein 8"
                     /calculated_mol_wt=12646
     Region          1..110
                     /region_name="Archease"
                     /note="Archease protein family (MTH1598/TM1083);
                     pfam01951"
                     /db_xref="CDD:426527"
     CDS             1..110
                     /gene="ZBTB8OS"
                     /gene_synonym="ARCH; ARCH2"
                     /coded_by="NM_001366260.1:617..949"
                     /note="isoform 5 is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS76134.1"
                     /db_xref="GeneID:339487"
                     /db_xref="HGNC:HGNC:24094"
                     /db_xref="MIM:615891"
ORIGIN      
        1 mamfgymtdt gtveplqtve vetqgddlqs llfhfldewl ykfsadeffi prevkvlsid
       61 qrnfklrsig wgeefslskh pqgtevkait ysamqvynee npevfviidi
//
LOCUS       NP_000311                244 aa            linear   PRI 27-APR-2025
DEFINITION  dihydropteridine reductase isoform 1 [Homo sapiens].
ACCESSION   NP_000311
VERSION     NP_000311.2
DBSOURCE    REFSEQ: accession NM_000320.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Girish,A., Sutar,S., Murthy,T.P.K., Premanand,S.A., Garg,V.,
            Patil,L., Shreyas,S., Shukla,R., Yadav,A.K. and Singh,T.R.
  TITLE     Comprehensive bioinformatics analysis of structural and functional
            consequences of deleterious missense mutations in the human QDPR
            gene
  JOURNAL   J Biomol Struct Dyn 42 (11), 5485-5501 (2024)
   PUBMED   37382215
  REMARK    GeneRIF: Comprehensive bioinformatics analysis of structural and
            functional consequences of deleterious missense mutations in the
            human QDPR gene.
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Liu,J., He,X., Deng,S., Zhao,S., Zhang,S., Chen,Z., Xue,C.,
            Zeng,L., Zhao,H., Zhou,Y., Bai,R., Xu,Z., Liu,S., Zhou,Q., Li,M.,
            Zhang,J., Huang,X., Chen,R., Wang,L., Lin,D. and Zheng,J.
  TITLE     QDPR deficiency drives immune suppression in pancreatic cancer
  JOURNAL   Cell Metab 36 (5), 984-999 (2024)
   PUBMED   38642552
  REMARK    GeneRIF: QDPR deficiency drives immune suppression in pancreatic
            cancer.
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Chandrashekaran,S., Karthikeyan,S., Balakrishnan,A., Nair,S.,
            Satheesh Kumar,M.K., Vattathara,J.J. and Menon,K.N.
  TITLE     Expression and Purification of Quinine Dihydro Pteridine Reductase
            from astrocytes and its significance in the astrocyte pathology
  JOURNAL   Int J Biol Macromol 110, 567-572 (2018)
   PUBMED   29355631
  REMARK    GeneRIF: show for the first time statistically significant up
            regulation of iNOS in QDPR overexpressing astrocytes. Increased
            expression of iNOS associated with astrocyte pathology seen in many
            neurodegenerative disorders may have implications in autoimmune
            neurodegenerative disorders.
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Si,Q., Sun,S. and Gu,Y.
  TITLE     A278C mutation of dihydropteridine reductase decreases autophagy
            via mTOR signaling
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 49 (8), 706-712 (2017)
   PUBMED   28633336
  REMARK    GeneRIF: Mutation of dihydropteridine reductase (QDPR) inhibited
            the regulation of TOR serine-threonine kinases (mTOR), suggesting
            that QDPR is a positive regulator of autophagy via suppressing mTOR
            signaling.
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Howells,D.W., Forrest,S.M., Dahl,H.H. and Cotton,R.G.
  TITLE     Insertion of an extra codon for threonine is a cause of
            dihydropteridine reductase deficiency
  JOURNAL   Am J Hum Genet 47 (2), 279-285 (1990)
   PUBMED   2116088
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Sumi,S., Ishikawa,T., Ito,Y., Oishi,H., Asai,K. and Wada,Y.
  TITLE     Probable assignment of the dihydropteridine reductase gene to
            4p15.31
  JOURNAL   Tohoku J Exp Med 160 (1), 93-94 (1990)
   PUBMED   2330583
REFERENCE   8  (residues 1 to 244)
  AUTHORS   Lockyer,J., Cook,R.G., Milstien,S., Kaufman,S., Woo,S.L. and
            Ledley,F.D.
  TITLE     Structure and expression of human dihydropteridine reductase
  JOURNAL   Proc Natl Acad Sci U S A 84 (10), 3329-3333 (1987)
   PUBMED   3033643
REFERENCE   9  (residues 1 to 244)
  AUTHORS   Dahl,H.H., Hutchison,W., McAdam,W., Wake,S., Morgan,F.J. and
            Cotton,R.G.
  TITLE     Human dihydropteridine reductase: characterisation of a cDNA clone
            and its use in analysis of patients with dihydropteridine reductase
            deficiency
  JOURNAL   Nucleic Acids Res 15 (5), 1921-1932 (1987)
   PUBMED   3031582
REFERENCE   10 (residues 1 to 244)
  AUTHORS   Kaufman,S., Holtzman,N.A., Milstien,S., Butler,L.J. and Krumholz,A.
  TITLE     Phenylketonuria due to a deficiency of dihydropteridine reductase
  JOURNAL   N Engl J Med 293 (16), 785-790 (1975)
   PUBMED   1160969
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM762805.1, BC000576.2,
            AC093600.3 and AW104747.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 8, 2008 this sequence version replaced NP_000311.1.
            
            Summary: This gene encodes the enzyme dihydropteridine reductase,
            which catalyzes the NADH-mediated reduction of quinonoid
            dihydrobiopterin.  This enzyme is an essential component of the
            pterin-dependent aromatic amino acid hydroxylating systems.
            Mutations in this gene resulting in QDPR deficiency include
            aberrant splicing, amino acid substitutions, insertions, or
            premature terminations.  Dihydropteridine reductase deficiency
            presents as atypical phenylketonuria due to insufficient production
            of biopterin, a cofactor for phenylalanine hydroxylase. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.736743.1,
                                           SRR3476690.840895.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146411 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281243.10/ ENSP00000281243.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.32"
     Protein         1..244
                     /product="dihydropteridine reductase isoform 1"
                     /EC_number="1.5.1.34"
                     /note="6,7-dihydropteridine reductase; testis secretory
                     sperm-binding protein Li 236P; short chain
                     dehydrogenase/reductase family 33C member 1"
                     /calculated_mol_wt=25658
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.11,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P09417.2)"
     Region          10..232
                     /region_name="DHPR_SDR_c_like"
                     /note="dihydropteridine reductase (DHPR), classical (c)
                     SDRs; cd05334"
                     /db_xref="CDD:187595"
     Site            order(16..17,19..22,41,54,63,86..89,110,114,135..136,150,
                     154,182..185,187,190)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187595"
     Site            order(64,94..97,100..102,104..105,116,120,123,140,
                     142..145,148,151..152,156,159..160,162..164,166..170)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187595"
     Site            order(150,154)
                     /site_type="active"
                     /db_xref="CDD:187595"
     CDS             1..244
                     /gene="QDPR"
                     /gene_synonym="DHPR; HDHPR; PKU2; SDR33C1"
                     /coded_by="NM_000320.3:37..771"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3421.1"
                     /db_xref="GeneID:5860"
                     /db_xref="HGNC:HGNC:9752"
                     /db_xref="MIM:612676"
ORIGIN      
        1 maaaaaagea rrvlvyggrg algsrcvqaf rarnwwvasv dvveneeasa siivkmtdsf
       61 teqadqvtae vgkllgeekv dailcvaggw aggnaksksl fkncdlmwkq siwtstissh
      121 latkhlkegg lltlagakaa ldgtpgmigy gmakgavhql cqslagknsg mppgaaaiav
      181 lpvtldtpmn rksmpeadfs swtpleflve tfhdwitgkn rpssgsliqv vttegrtelt
      241 payf
//
LOCUS       NP_001965                886 aa            linear   PRI 27-APR-2025
DEFINITION  adhesion G protein-coupled receptor E1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001965
VERSION     NP_001965.3
DBSOURCE    REFSEQ: accession NM_001974.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 886)
  AUTHORS   Akter,R., Park,R., Lee,S.K., Han,E.J., Park,K.S., Park,J. and
            Cho,M.Y.
  TITLE     Upregulation of EMR1 (ADGRE1) by Tumor-Associated Macrophages
            Promotes Colon Cancer Progression by Activating the JAK2/STAT1,3
            Signaling Pathway in Tumor Cells
  JOURNAL   Int J Mol Sci 25 (8), 4388 (2024)
   PUBMED   38673975
  REMARK    GeneRIF: Upregulation of EMR1 (ADGRE1) by Tumor-Associated
            Macrophages Promotes Colon Cancer Progression by Activating the
            JAK2/STAT1,3 Signaling Pathway in Tumor Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 886)
  AUTHORS   Ali,H., Olsson,L., Lindmark,G., Hammarstrom,M.L., Hammarstrom,S.
            and Sitohy,B.
  TITLE     The myeloid cell biomarker EMR1 is ectopically expressed in colon
            cancer
  JOURNAL   Tumour Biol 43 (1), 209-223 (2021)
   PUBMED   34486997
  REMARK    GeneRIF: The myeloid cell biomarker EMR1 is ectopically expressed
            in colon cancer.
REFERENCE   3  (residues 1 to 886)
  AUTHORS   Wang,Y. and Tatakis,D.N.
  TITLE     Human gingiva transcriptome during wound healing
  JOURNAL   J Clin Periodontol 44 (4), 394-402 (2017)
   PUBMED   28005267
  REMARK    GeneRIF: EMR1 expression is significantly upregulated in human
            masticatory mucosa during wound healing
REFERENCE   4  (residues 1 to 886)
  AUTHORS   Hamann,J., Aust,G., Arac,D., Engel,F.B., Formstone,C.,
            Fredriksson,R., Hall,R.A., Harty,B.L., Kirchhoff,C., Knapp,B.,
            Krishnan,A., Liebscher,I., Lin,H.H., Martinelli,D.C., Monk,K.R.,
            Peeters,M.C., Piao,X., Promel,S., Schoneberg,T., Schwartz,T.W.,
            Singer,K., Stacey,M., Ushkaryov,Y.A., Vallon,M., Wolfrum,U.,
            Wright,M.W., Xu,L., Langenhan,T. and Schioth,H.B.
  TITLE     International Union of Basic and Clinical Pharmacology. XCIV.
            Adhesion G protein-coupled receptors
  JOURNAL   Pharmacol Rev 67 (2), 338-367 (2015)
   PUBMED   25713288
  REMARK    Review article
REFERENCE   5  (residues 1 to 886)
  AUTHORS   Divaris,K., Monda,K.L., North,K.E., Olshan,A.F., Reynolds,L.M.,
            Hsueh,W.C., Lange,E.M., Moss,K., Barros,S.P., Weyant,R.J., Liu,Y.,
            Newman,A.B., Beck,J.D. and Offenbacher,S.
  TITLE     Exploring the genetic basis of chronic periodontitis: a genome-wide
            association study
  JOURNAL   Hum Mol Genet 22 (11), 2312-2324 (2013)
   PUBMED   23459936
REFERENCE   6  (residues 1 to 886)
  AUTHORS   Lin,H.H., Stacey,M., Hamann,J., Gordon,S. and McKnight,A.J.
  TITLE     Human EMR2, a novel EGF-TM7 molecule on chromosome 19p13.1, is
            closely related to CD97
  JOURNAL   Genomics 67 (2), 188-200 (2000)
   PUBMED   10903844
REFERENCE   7  (residues 1 to 886)
  AUTHORS   Carver,E.A., Hamann,J., Olsen,A.S. and Stubbs,L.
  TITLE     Physical mapping of EMR1 and CD97 in human Chromosome 19 and
            assignment of Cd97 to mouse Chromosome 8 suggest an ancient genomic
            duplication
  JOURNAL   Mamm Genome 10 (10), 1039-1040 (1999)
   PUBMED   10501980
REFERENCE   8  (residues 1 to 886)
  AUTHORS   McKnight,A.J. and Gordon,S.
  TITLE     The EGF-TM7 family: unusual structures at the leukocyte surface
  JOURNAL   J Leukoc Biol 63 (3), 271-280 (1998)
   PUBMED   9500513
  REMARK    Review article
REFERENCE   9  (residues 1 to 886)
  AUTHORS   McKnight,A.J., Macfarlane,A.J., Seldin,M.F. and Gordon,S.
  TITLE     Chromosome mapping of the Emr1 gene
  JOURNAL   Mamm Genome 8 (12), 946 (1997)
   PUBMED   9383301
REFERENCE   10 (residues 1 to 886)
  AUTHORS   Baud,V., Chissoe,S.L., Viegas-Pequignot,E., Diriong,S.,
            N'Guyen,V.C., Roe,B.A. and Lipinski,M.
  TITLE     EMR1, an unusual member in the family of hormone receptors with
            seven transmembrane segments
  JOURNAL   Genomics 26 (2), 334-344 (1995)
   PUBMED   7601460
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA465986.1, BC059395.1,
            X81479.1 and AK297003.1.
            
            On Jan 13, 2004 this sequence version replaced NP_001965.2.
            
            Summary: This gene encodes a protein that has a domain resembling
            seven transmembrane G protein-coupled hormone receptors (7TM
            receptors) at its C-terminus. The N-terminus of the encoded protein
            has six EGF-like modules, separated from the transmembrane segments
            by a serine/threonine-rich domain, a feature reminiscent of
            mucin-like, single-span, integral membrane glycoproteins with
            adhesive properties. Multiple alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2012].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X81479.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312053.9/ ENSP00000311545.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..886
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3-p13.2"
     Protein         1..886
                     /product="adhesion G protein-coupled receptor E1 isoform 1
                     precursor"
                     /note="egf-like module containing, mucin-like, hormone
                     receptor-like sequence 1; EGF-like module-containing
                     mucin-like hormone receptor-like 1; EMR1 hormone receptor;
                     EGF-like module receptor 1; egf-like module containing,
                     mucin-like, hormone receptor-like 1"
                     /calculated_mol_wt=95315
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2387
     mat_peptide     21..886
                     /product="Adhesion G protein-coupled receptor E1.
                     /id=PRO_0000012873"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14246.3)"
                     /calculated_mol_wt=95315
     Region          33..62
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          80..114
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(80,83,99)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Region          132..171
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(132,135,150)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Region          172..205
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(172,175,190)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            189
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Region          221..>250
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(221,224,237)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Site            258
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Region          268..301
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(268,271,287)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            312
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Site            366
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Site            375
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Site            448
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14246.3)"
     Region          546..595
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Region          550..597
                     /region_name="GPS.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14246.3)"
     Region          599..861
                     /region_name="7tmB2_EMR"
                     /note="epidermal growth factor-like module-containing
                     mucin-like hormone receptors, member of the class B2
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15439"
                     /db_xref="CDD:320555"
     Site            600..627
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14246.3)"
     Region          601..626
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320555"
     Site            order(606,610,652,655..656,659,666,673,750..751,753,755,
                     811,814,826,830)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320555"
     Region          635..657
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320555"
     Site            635..656
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14246.3)"
     Region          666..693
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320555"
     Site            667..690
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14246.3)"
     Site            710..731
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14246.3)"
     Region          710..730
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320555"
     Region          747..770
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320555"
     Site            748..776
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14246.3)"
     Region          794..819
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320555"
     Site            795..814
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14246.3)"
     Region          823..848
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320555"
     Site            830..852
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14246.3)"
     Region          862..886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14246.3)"
     CDS             1..886
                     /gene="ADGRE1"
                     /gene_synonym="EMR1; TM7LN3"
                     /coded_by="NM_001974.5:31..2691"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12175.1"
                     /db_xref="GeneID:2015"
                     /db_xref="HGNC:HGNC:3336"
                     /db_xref="MIM:600493"
ORIGIN      
        1 mrgfnlllfw gccvmhsweg hirptrkpnt kgnncrdstl cpayatctnt vdsyycackq
       61 gflssngqnh fkdpgvrckd idecsqspqp cgpnsscknl sgrykcscld gfssptgndw
      121 vpgkpgnfsc tdinecltss vcpehsdcvn smgsyscscq vgfisrnstc edvdecadpr
      181 acpehatcnn tvgnyscfcn pgfesssghl sfqglkasce didectemcp instctntpg
      241 syfctchpgf apsngqlnft dqgvecrdid ecrqdpstcg pnsictnalg syscgciagf
      301 hpnpegsqkd gnfscqrvlf kckedvipdn kqiqqcqegt avkpayvsfc aqinnifsvl
      361 dkvcenkttv vslknttesf vpvlkqistw tkftkeetss latvflesve smtlasfwkp
      421 sanitpavrt eyldieskvi nkecseenvt ldlvakgdkm kigcstiees estettgvaf
      481 vsfvgmesvl nerffkdhqa plttseiklk mnsrvvggim tgekkdgfsd piiytleniq
      541 pkqkferpic vswstdvkgg rwtsfgcvil easetytics cnqmanlavi masgeltmdf
      601 slyiishvgi iislvclvla iatfllcrsi rnhntylhlh lcvclllakt lflagihktd
      661 nkmgcaiiag flhylflacf fwmlveavil flmvrnlkvv nyfssrnikm lhicafgygl
      721 pmlvvvisas vqpqgygmhn rcwlntetgf iwsflgpvct vivinslllt wtlwilrqrl
      781 ssvnaevstl kdtrlltfka faqlfilgcs wvlgifqigp vagvmaylft iinslqgafi
      841 flihcllngq vreeykrwit gktkpssqsq tsrillssmp sasktg
//
LOCUS       NP_078804                415 aa            linear   PRI 27-APR-2025
DEFINITION  NF-kappa-B-activating protein [Homo sapiens].
ACCESSION   NP_078804
VERSION     NP_078804.2
DBSOURCE    REFSEQ: accession NM_024528.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Xu,X., Gao,C., Ye,F., Peng,A., Xu,J., Jin,K., Zhang,J., Ye,Y.,
            Yang,Y., Zhang,X., Shen,S. and Jin,F.
  TITLE     From phenotype to mechanism: Prenatal spectrum of NKAP
            mutation-related disorder and its pathogenesis inducing congenital
            heart disease
  JOURNAL   J Cell Mol Med 28 (8), e18305 (2024)
   PUBMED   38647244
  REMARK    GeneRIF: From phenotype to mechanism: Prenatal spectrum of NKAP
            mutation-related disorder and its pathogenesis inducing congenital
            heart disease.
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Sun,S., Gao,T., Pang,B., Su,X., Guo,C., Zhang,R. and Pang,Q.
  TITLE     RNA binding protein NKAP protects glioblastoma cells from
            ferroptosis by promoting SLC7A11 mRNA splicing in an m6A-dependent
            manner
  JOURNAL   Cell Death Dis 13 (1), 73 (2022)
   PUBMED   35064112
  REMARK    GeneRIF: RNA binding protein NKAP protects glioblastoma cells from
            ferroptosis by promoting SLC7A11 mRNA splicing in an
            m(6)A-dependent manner.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Liu,J., Chen,S.J., Hsu,S.W., Zhang,J., Li,J.M., Yang,D.C., Gu,S.,
            Pinkerton,K.E. and Chen,C.H.
  TITLE     MARCKS cooperates with NKAP to activate NF-kB signaling in
            smoke-related lung cancer
  JOURNAL   Theranostics 11 (9), 4122-4136 (2021)
   PUBMED   33754052
  REMARK    GeneRIF: MARCKS cooperates with NKAP to activate NF-kB signaling in
            smoke-related lung cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Hsu,F.C., Pajerowski,A.G., Nelson-Holte,M., Sundsbak,R. and
            Shapiro,V.S.
  TITLE     NKAP is required for T cell maturation and acquisition of
            functional competency
  JOURNAL   J Exp Med 208 (6), 1291-1304 (2011)
   PUBMED   21624937
  REMARK    GeneRIF: NKAP is required for T cell maturation and the acquisition
            of functional competency
REFERENCE   8  (residues 1 to 415)
  AUTHORS   D'Addabbo,A., Latiano,A., Palmieri,O., Creanza,M.T., Maglietta,R.,
            Annese,V. and Ancona,N.
  TITLE     Association of genetic profiles to Crohn's disease by linear
            combinations of single nucleotide polymorphisms
  JOURNAL   Artif Intell Med 46 (2), 131-138 (2009)
   PUBMED   18804983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Pajerowski,A.G., Nguyen,C., Aghajanian,H., Shapiro,M.J. and
            Shapiro,V.S.
  TITLE     NKAP is a transcriptional repressor of notch signaling and is
            required for T cell development
  JOURNAL   Immunity 30 (5), 696-707 (2009)
   PUBMED   19409814
  REMARK    GeneRIF: NKAP functions as a transcriptional repressor, acting on
            Notch target genes, and is required for alphabeta T cell
            development.
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Chen,D., Li,Z., Yang,Q., Zhang,J., Zhai,Z. and Shu,H.B.
  TITLE     Identification of a nuclear protein that promotes NF-kappaB
            activation
  JOURNAL   Biochem Biophys Res Commun 310 (3), 720-724 (2003)
   PUBMED   14550261
  REMARK    GeneRIF: NKAP is a novel nuclear regulator of TNF- and IL-1-induced
            NF-kappaB activation
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY388958.1, BC015354.1 and
            AC002477.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 21, 2008 this sequence version replaced NP_078804.1.
            
            Summary: This gene encodes a protein that is involved in the
            activation of the ubiquitous transcription factor NF-kappaB. This
            protein is associated with the the histone deacetylase HDAC3 and
            with the Notch corepressor complex, and it thereby acts as a
            transcriptional repressor of Notch target genes. It is also
            required for alphabeta T cell development. A related pseudogene has
            been identified on chromosome X, while a related and intronless
            retrocopy, which has an intact CDS and may be functional, is
            located on chromosome 6. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY388958.1, AK026279.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371410.5/ ENSP00000360464.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq24"
     Protein         1..415
                     /product="NF-kappa-B-activating protein"
                     /note="NF-kappaB activating protein"
                     /calculated_mol_wt=47007
     Region          1..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Site            112
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Region          120..>176
                     /region_name="NKAP"
                     /note="NF-kappa-B-activating protein; pfam15692"
                     /db_xref="CDD:464805"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Region          179..272
                     /region_name="Necessary for interaction with CIR1.
                     /evidence=ECO:0000269|PubMed:19409814"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Region          273..415
                     /region_name="Necessary for interaction with HDAC3 and
                     transcriptional repression.
                     /evidence=ECO:0000269|PubMed:19409814"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5F7.1)"
     Region          306..405
                     /region_name="Nkap_C"
                     /note="NF-kappa-B-activating protein C-terminal domain;
                     pfam06047"
                     /db_xref="CDD:461812"
     CDS             1..415
                     /gene="NKAP"
                     /gene_synonym="MRXSHD"
                     /coded_by="NM_024528.4:147..1394"
                     /db_xref="CCDS:CCDS14592.1"
                     /db_xref="GeneID:79576"
                     /db_xref="HGNC:HGNC:29873"
                     /db_xref="MIM:300766"
ORIGIN      
        1 mapvsgsrsp dreasgsggr rrssskspkp sksarsprgr rsrshscsrs gdrnglthql
       61 gglsqgsrnq syrsrsrsrs rerpsaprgi pfasasssvy ygsysrpygs dkpwpslldk
      121 ereeslrqkr lsererigel gapevwglsp knpepdsdeh tpvedeepkk sttsastsee
      181 ekkkkssrsk erskkrrkkk sskrkhkkys edsdsdsdse tdssdednkr rakkakkkek
      241 kkkhrskkyk kkrskksrke ssdssskesq eeflenpwkd rtkaeepsdl igpeapktlt
      301 sqddkplnyg hallpgegaa maeyvkagkr iprrgeiglt seeiasfecs gyvmsgsrhr
      361 rmeavrlrke nqiysadekr alasfnqeer rkrenkilas fremvyrktk gkddk
//
LOCUS       NP_620138                615 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 653 [Homo sapiens].
ACCESSION   NP_620138
VERSION     NP_620138.2
DBSOURCE    REFSEQ: accession NM_138783.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Borud,B., Mellgren,G., Lund,J. and Bakke,M.
  TITLE     Cloning and characterization of a novel zinc finger protein that
            modulates the transcriptional activity of nuclear receptors
  JOURNAL   Mol Endocrinol 17 (11), 2303-2319 (2003)
   PUBMED   12920234
  REMARK    GeneRIF: novel zinc-finger protein that influences gene activation
            through interaction with the functionally important activation
            function-2 domain of nuclear receptors
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK131037.1, BC014187.2 and CB241280.1.
            
            On Feb 24, 2010 this sequence version replaced NP_620138.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY072704.1, BC016816.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000293771.10/ ENSP00000293771.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..615
                     /product="zinc finger protein 653"
                     /note="zinc finger protein Zip67; 67 kDa zinc finger
                     protein"
                     /calculated_mol_wt=67104
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CK0.1)"
     Region          95..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CK0.1)"
     Region          107..118
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CK0.1)"
     Region          176..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CK0.1)"
     Region          401..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CK0.1)"
     Region          445..451
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CK0.1)"
     Region          <486..614
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          503..522
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(507,509,511,513..514,517..518,521,535,537,541..542,
                     545..546,549,563,565,567,569..570,573..574,577)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          514..539
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          530..550
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          558..578
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          588..609
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..615
                     /gene="ZNF653"
                     /gene_synonym="E430039K05Rik; ZIP67"
                     /coded_by="NM_138783.4:54..1901"
                     /db_xref="CCDS:CCDS12261.1"
                     /db_xref="GeneID:115950"
                     /db_xref="HGNC:HGNC:25196"
                     /db_xref="MIM:611371"
ORIGIN      
        1 maeralepea eaeaeagagg eaaaeegaag rkargrprlt esdrarrrle srkkydvrrv
       61 ylgeahgpwv dlrrrsgwsd aklaaylisl ergqrsgrhg kpweqvpkkp krkkrrrrnv
      121 nclknvviwy edhkhrcpye phlaeldptf glyttavwqc eaghryfqdl hsplkplsds
      181 dpdsdkvgng lvagssdsss sgsasdsees pegqpvkaaa aaaaatptsp vgssglitqe
      241 gvhipfdvhh veslaeqgtp lcsnpagngp ealetvvcvp vpvqvgagps alfenvpqea
      301 lgevvascpm pgmvpgsqvi iiagpgydal taegihlnma agsgvpgsgl geevpcamme
      361 gvaaytqtep egsqpstmda tavagietkk ekedlcllkk eekeepvape lattvpesae
      421 peaeadgeel dgsdmsaiiy eipkepekrr rskrsrvmda dgllemfhcp yegcsqvyva
      481 lssfqnhvnl vhrkgktkvc phpgcgkkfy lsnhlrrhmi ihsgvreftc etcgksfkrk
      541 nhlevhrrth tgetplqcei cgyqcrqras lnwhmkkhta evqynftcdr cgkrfeklds
      601 vkfhtlkshp dhkpt
//
LOCUS       NP_056060               1134 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat and SAM domain-containing protein 1A [Homo sapiens].
ACCESSION   NP_056060 XP_166478
VERSION     NP_056060.2
DBSOURCE    REFSEQ: accession NM_015245.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Lee,J., Lee,H., Lee,H., Shin,M., Shin,M.G., Seo,J., Lee,E.J.,
            Park,S.A. and Park,S.
  TITLE     ANKS1A regulates LDL receptor-related protein 1 (LRP1)-mediated
            cerebrovascular clearance in brain endothelial cells
  JOURNAL   Nat Commun 14 (1), 8463 (2023)
   PUBMED   38123547
  REMARK    GeneRIF: ANKS1A regulates LDL receptor-related protein 1
            (LRP1)-mediated cerebrovascular clearance in brain endothelial
            cells.
            Erratum:[Nat Commun. 2024 Apr 9;15(1):3062. doi:
            10.1038/s41467-024-47249-w. PMID: 38594263]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 1134)
  AUTHORS   Zholudeva,A.O., Lomakina,M.E., Orlova,E.A., Wang,Y., Fokin,A.I.,
            Polesskaya,A., Gautreau,A.M. and Alexandrova,A.Y.
  TITLE     The Role of the Adapter Protein Anks1a in the Regulation of Breast
            Cancer Cell Motility
  JOURNAL   Biochemistry (Mosc) 87 (12), 1651-1661 (2022)
   PUBMED   36717454
  REMARK    GeneRIF: The Role of the Adapter Protein Anks1a in the Regulation
            of Breast Cancer Cell Motility.
REFERENCE   4  (residues 1 to 1134)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   5  (residues 1 to 1134)
  AUTHORS   Fantino,M., Paquette,M., Bernard,S. and Baass,A.
  TITLE     ANKS1A genotype predicts cardiovascular events in patients with
            familial hypercholesterolemia
  JOURNAL   J Clin Lipidol 15 (4), 602-607 (2021)
   PUBMED   34130940
  REMARK    GeneRIF: ANKS1A genotype predicts cardiovascular events in patients
            with familial hypercholesterolemia.
REFERENCE   6  (residues 1 to 1134)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   7  (residues 1 to 1134)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 1134)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 1134)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   10 (residues 1 to 1134)
  AUTHORS   Pandey,A., Blagoev,B., Kratchmarova,I., Fernandez,M., Nielsen,M.,
            Kristiansen,T.Z., Ohara,O., Podtelejnikov,A.V., Roche,S.,
            Lodish,H.F. and Mann,M.
  TITLE     Cloning of a novel phosphotyrosine binding domain containing
            molecule, Odin, involved in signaling by receptor tyrosine kinases
  JOURNAL   Oncogene 21 (52), 8029-8036 (2002)
   PUBMED   12439753
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL033520.16, BC022396.1, D86982.1, AL138721.16 and BF592042.1.
            
            On Apr 4, 2007 this sequence version replaced NP_056060.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D86982.1, BC132832.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360359.5/ ENSP00000353518.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..1134
                     /product="ankyrin repeat and SAM domain-containing protein
                     1A"
                     /note="ankyrin repeat and SAM domain containing 1; Odin"
                     /calculated_mol_wt=122977
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0000269|PubMed:12439753; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Region          7..77
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          33..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Region          72..285
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          79..108
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Region          80..110
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(81,85..86,89..91,93..94,98,101,110,112,114,118..119,
                     122..124,126..127,131,134,146,148,150,154..155,158..160,
                     162..163,167,170,179)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          112..146
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          112..141
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Region          148..179
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          148..177
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Region          181..212
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          181..210
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Region          214..244
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          214..243
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Region          246..275
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Region          247..277
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          305..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Region          375..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Region          469..498
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Region          569..650
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P59672; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Site            663
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P59672; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Site            677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Region          697..763
                     /region_name="SAM_AIDA1AB-like_repeat1"
                     /note="SAM domain of AIDA1AB-like proteins, repeat 1;
                     cd09499"
                     /db_xref="CDD:188898"
     Site            order(719..722,724,726..727,730..731,733..734,737,
                     740..741)
                     /site_type="other"
                     /note="intramolecular dimer interface ML [polypeptide
                     binding]"
                     /db_xref="CDD:188898"
     Region          768..832
                     /region_name="SAM_AIDA1AB-like_repeat2"
                     /note="SAM domain of AIDA1AB-like proteins, repeat 2;
                     cd09500"
                     /db_xref="CDD:188899"
     Site            order(818..821,823..824)
                     /site_type="other"
                     /note="intramolecular dimer interface EH [polypeptide
                     binding]"
                     /db_xref="CDD:188899"
     Region          856..896
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92625.4)"
     Region          926..1071
                     /region_name="PTB_Anks"
                     /note="Ankyrin repeat and sterile alpha motif (SAM)
                     domain-containing (Anks) protein family
                     Phosphotyrosine-binding (PTB) domain; cd01274"
                     /db_xref="CDD:269972"
     Site            order(945,1020,1040)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269972"
     Site            order(1009..1014,1027,1051,1055)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269972"
     Region          1079..1134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92625.4)"
     CDS             1..1134
                     /gene="ANKS1A"
                     /gene_synonym="ANKS1"
                     /coded_by="NM_015245.3:149..3553"
                     /db_xref="CCDS:CCDS4798.1"
                     /db_xref="GeneID:23294"
                     /db_xref="HGNC:HGNC:20961"
                     /db_xref="MIM:608994"
ORIGIN      
        1 mgkeqellea artghlpave kllsgkrlss gfgggggggs ggggggsggg ggglgssshp
       61 lssllsmwrg pnvncvdstg ytplhhaaln ghkdvvevll rndaltnvad skgcyplhla
      121 awkgdaqivr llihqgpsht rvneqnndne talhcaaqyg htevvkvlle eltdptmrnn
      181 kfetpldlaa lygrlevvkm llnahpnlls cntkkhtplh laarnghkav vqvlldagmd
      241 snyqtemgsa lheaalfgkt dvvqillaag tdvnikdnhg ltaldtvrel psqksqqiaa
      301 liedhmtgkr stkevdktpp pqpplissmd sisqksqgdv ekavteliid fdanaeeegp
      361 yealynaisc hsldsmasgr ssdqdstnke aeaagvkpag vrprerpppp akpppdeeee
      421 dhidkkyfpl tasevlsmrp rihgsaaree dehpyelllt aetkkvvlvd gktkdhrrss
      481 ssrsqdsaeg qdgqvpeqfs gllhgsspvc evgqdpfqll ctagqshpdg spqqgachka
      541 smqleetgvh apgasqpsal dqskrvgylt glpttnsrsh petlthtasp hpggaeegdr
      601 sgarsrappt skpkaelkls rslsksdsdl ltcsptedat mgsrseslsn csigkkrlek
      661 spsfasewde iekimssige gidfsqerqk isglrtleqs vgewlesigl qqyeskllln
      721 gfddvhflgs nvmeeqdlrd igisdpqhrr kllqaarslp kvkalgydgn sppsvpswld
      781 slglqdyvhs flssgyssid tvknlwelel vnvlkvqllg hrkriiasla drpyeeppqk
      841 pprfsqlrcq dllsqtsspl sqndsctgrs adlllppgdt grrrhdslhd paapsraerf
      901 riqeehreak ltlrppslaa pyapvqswqh qpeklifesc gyeanylgsm likdlrgtes
      961 tqdacakmrk stehmkkipt iilsitykgv kfidasnknv iaeheirnis caaqdpedlc
     1021 tfayitkdlq tshhychvfs tvdvnltyei iltlgqafev ayqlalqaqk sratgasaae
     1081 mietksskpv pkprvgvrks aleppdmdqd aqshasvswv vdpkpdskrs lstn
//
LOCUS       NP_060555               1041 aa            linear   PRI 27-APR-2025
DEFINITION  importin-9 [Homo sapiens].
ACCESSION   NP_060555
VERSION     NP_060555.2
DBSOURCE    REFSEQ: accession NM_018085.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   de Almeida,M., Hinterndorfer,M., Brunner,H., Grishkovskaya,I.,
            Singh,K., Schleiffer,A., Jude,J., Deswal,S., Kalis,R., Vunjak,M.,
            Lendl,T., Imre,R., Roitinger,E., Neumann,T., Kandolf,S.,
            Schutzbier,M., Mechtler,K., Versteeg,G.A., Haselbach,D. and
            Zuber,J.
  TITLE     AKIRIN2 controls the nuclear import of proteasomes in vertebrates
  JOURNAL   Nature 599 (7885), 491-496 (2021)
   PUBMED   34711951
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Padavannil,A., Sarkar,P., Kim,S.J., Cagatay,T., Jiou,J.,
            Brautigam,C.A., Tomchick,D.R., Sali,A., D'Arcy,S. and Chook,Y.M.
  TITLE     Importin-9 wraps around the H2A-H2B core to act as nuclear importer
            and histone chaperone
  JOURNAL   Elife 8, e43630 (2019)
   PUBMED   30855230
  REMARK    GeneRIF: Like many histone chaperones, which prevent inappropriate
            non-nucleosomal interactions, Importin-9 also sequesters H2A-H2B
            from DNA. Importin-9 appears to act as a storage chaperone for
            H2A-H2B while escorting it to the nucleus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Izdebska,M., Grzanka,D., Gagat,M., Halas-Wisniewska,M. and
            Grzanka,A.
  TITLE     Downregulation of importin-9 protects MCF-7 cells against apoptosis
            induced by the combination of garlic-derived alliin and paclitaxel
  JOURNAL   Oncol Rep 35 (5), 3084-3093 (2016)
   PUBMED   26934847
  REMARK    GeneRIF: CFL1 itself does not translocate actin into the cell
            nucleus but this transport requires the functional expression of
            IPO9.
REFERENCE   4  (residues 1 to 1041)
  AUTHORS   Matsumiya,T., Xing,F., Ebina,M., Hayakari,R., Imaizumi,T.,
            Yoshida,H., Kikuchi,H., Topham,M.K., Satoh,K. and Stafforini,D.M.
  TITLE     Novel role for molecular transporter importin 9 in
            posttranscriptional regulation of IFN-epsilon expression
  JOURNAL   J Immunol 191 (4), 1907-1915 (2013)
   PUBMED   23851686
  REMARK    GeneRIF: IPO9 associates with 2 stable stem-loop structures of the
            IFN-epsilon 5'UTR. IPO9 overexpression decreased, and IPO9
            silencing increased basal IFN-epsilon expression.
REFERENCE   5  (residues 1 to 1041)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 1041)
  AUTHORS   Koch,H.B., Zhang,R., Verdoodt,B., Bailey,A., Zhang,C.D., Yates,J.R.
            3rd, Menssen,A. and Hermeking,H.
  TITLE     Large-scale identification of c-MYC-associated proteins using a
            combined TAP/MudPIT approach
  JOURNAL   Cell Cycle 6 (2), 205-217 (2007)
   PUBMED   17314511
REFERENCE   7  (residues 1 to 1041)
  AUTHORS   King,F.W. and Shtivelman,E.
  TITLE     Inhibition of nuclear import by the proapoptotic protein CC3
  JOURNAL   Mol Cell Biol 24 (16), 7091-7101 (2004)
   PUBMED   15282309
REFERENCE   8  (residues 1 to 1041)
  AUTHORS   Lubert,E.J. and Sarge,K.D.
  TITLE     Interaction between protein phosphatase 2A and members of the
            importin beta superfamily
  JOURNAL   Biochem Biophys Res Commun 303 (3), 908-913 (2003)
   PUBMED   12670497
  REMARK    GeneRIF: specific interaction between a member of the importin
            beta/karyopherin beta superfamily, importin 9, and the A subunit of
            PP2A (PR65)
REFERENCE   9  (residues 1 to 1041)
  AUTHORS   Jakel,S., Mingot,J.M., Schwarzmaier,P., Hartmann,E. and Gorlich,D.
  TITLE     Importins fulfil a dual function as nuclear import receptors and
            cytoplasmic chaperones for exposed basic domains
  JOURNAL   EMBO J 21 (3), 377-386 (2002)
   PUBMED   11823430
REFERENCE   10 (residues 1 to 1041)
  AUTHORS   Muhlhausser,P., Muller,E.C., Otto,A. and Kutay,U.
  TITLE     Multiple pathways contribute to nuclear import of core histones
  JOURNAL   EMBO Rep 2 (8), 690-696 (2001)
   PUBMED   11493596
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL645504.10, DB232332.1, DA861528.1, AF410465.1 and AL513217.11.
            
            On Jun 10, 2002 this sequence version replaced NP_060555.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.156909.1,
                                           SRR1803613.200236.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361565.9/ ENSP00000354742.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..1041
                     /product="importin-9"
                     /note="ranBP9; ran-binding protein 9"
                     /calculated_mol_wt=115832
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q96P70.3)"
     Region          34..812
                     /region_name="CSE1"
                     /note="CAS/CSE protein involved in chromosome segregation
                     [Cell division and chromosome partitioning]; COG5657"
                     /db_xref="CDD:227944"
     Region          936..967
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P70.3)"
     CDS             1..1041
                     /gene="IPO9"
                     /gene_synonym="Imp9"
                     /coded_by="NM_018085.5:54..3179"
                     /db_xref="CCDS:CCDS1415.1"
                     /db_xref="GeneID:55705"
                     /db_xref="HGNC:HGNC:19425"
                     /db_xref="MIM:620893"
ORIGIN      
        1 maaaaaagaa sglpgpvaqg lkealvdtlt gilspvqevr aaaeeqikvl evteefgvhl
       61 aeltvdpqga lairqlasvi lkqyvethwc aqsekfrppe tterakivir ellpnglres
      121 iskvrssvay avsaiahwdw peawpqlfnl lmemlvsgdl navhgamrvl teftrevtdt
      181 qmplvapvil pemykiftma evygirtrsr aveifttcah micnmeelek gaakvlifpv
      241 vqqfteafvq alqipdgpts dsgfkmevlk avtalvknfp khmvssmqqi lpivwntlte
      301 saafyvrtev nyteevedpv dsdgevlgfe nlvfsifefv hallenskfk stvkkalpel
      361 iyyiilymqi teeqikvwta npqqfveded ddtfsytvri aaqdlllava tdfqnesaaa
      421 laaaatrhlq eaeqtknsgt ehwwkiheac mlalgsvkai itdsvkngri hfdmhgfltn
      481 viladlnlsv spfllgralw aasrftvams peliqqflqa tvsglhetqp psvrisavra
      541 iwgycdqlkv sesthvlqpf lpsildglih laaqfssevl nlvmetlciv ctvdpeftas
      601 meskicpfti aiflkysndp vvaslaqdif kelsqieacq gpmqmrlipt lvsimqapad
      661 kipaglcata idilttvvrn tkpplsqlli cqafpavaqc tlhtddnatm qnggeclray
      721 vsvtleqvaq whdeqghngl wyvmqvvsql ldprtsefta afvgrlvstl iskagrelge
      781 nldqilrail skmqqaetls vmqslimvfa hlvhtqlepl leflcslpgp tgkpalefvm
      841 aewtsrqhlf ygqyegkvss valckllqhg inaddkrlqd irvkgeeiys mdegirtrsk
      901 saknperwtn ipllvkilkl iinelsnvme anaarqatpa ewsqddsndm wedqeeeeee
      961 eedglagqll sdilatskye edyyeddeed dpdalkdply qidlqayltd flcqfaqqpc
     1021 yimfsghlnd nerrvlqtig i
//
LOCUS       NP_005206               1447 aa            linear   PRI 27-APR-2025
DEFINITION  netrin receptor DCC [Homo sapiens].
ACCESSION   NP_005206
VERSION     NP_005206.2
DBSOURCE    REFSEQ: accession NM_005215.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1447)
  AUTHORS   Badary,D.M., Elsaied,H., Abdel-Fadeil,M.R., Ali,M.K., Abou-Taleb,H.
            and Iraqy,H.M.
  TITLE     Possible Role of Netrin-1/Deleted in Colorectal Cancer/Vascular
            Endothelial Growth Factor Signaling Pathway in the Pathogenesis of
            Placenta Accreta Spectrum: A Case-control Study
  JOURNAL   Int J Gynecol Pathol 43 (6), 565-572 (2024)
   PUBMED   38289148
  REMARK    GeneRIF: Possible Role of Netrin-1/Deleted in Colorectal
            Cancer/Vascular Endothelial Growth Factor Signaling Pathway in the
            Pathogenesis of Placenta Accreta Spectrum: A Case-control Study.
REFERENCE   2  (residues 1 to 1447)
  AUTHORS   Marquez-Gonzalez,R.M., Saucedo-Sarinana,A.M., de Jesus
            Tovar-Jacome,C., Barros-Nunez,P., Gallegos-Arreola,M.P.,
            Orozco-Gutierrez,M.H., Mariscal-Ramirez,I., Pineda-Razo,T.D.,
            Alcaraz-Wong,A.A., Marin-Contreras,M.E. and Rosales-Reynoso,M.A.
  TITLE     NME1 and DCC variants are associated with susceptibility and tumor
            characteristics in Mexican patients with colorectal cancer
  JOURNAL   J Egypt Natl Canc Inst 36 (1), 10 (2024)
   PUBMED   38556604
  REMARK    GeneRIF: NME1 and DCC variants are associated with susceptibility
            and tumor characteristics in Mexican patients with colorectal
            cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1447)
  AUTHORS   Serwer,T., Wahid,M., Imtiaz,F. and Memon,A.S.
  TITLE     Identification of specific codon 201 mutation of the DCC Gene in
            the colonoscopic specimen of colorectal cancer
  JOURNAL   J Pak Med Assoc 74 (2), 287-293 (2024)
   PUBMED   38419228
  REMARK    GeneRIF: Identification of specific codon 201 mutation of the DCC
            Gene in the colonoscopic specimen of colorectal cancer.
REFERENCE   4  (residues 1 to 1447)
  AUTHORS   Li,W., Lee,J., Vikis,H.G., Lee,S.H., Liu,G., Aurandt,J., Shen,T.L.,
            Fearon,E.R., Guan,J.L., Han,M., Rao,Y., Hong,K. and Guan,K.L.
  TITLE     Activation of FAK and Src are receptor-proximal events required for
            netrin signaling
  JOURNAL   Nat Neurosci 7 (11), 1213-1221 (2004)
   PUBMED   15494734
REFERENCE   5  (residues 1 to 1447)
  AUTHORS   Keino-Masu,K., Masu,M., Hinck,L., Leonardo,E.D., Chan,S.S.,
            Culotti,J.G. and Tessier-Lavigne,M.
  TITLE     Deleted in Colorectal Cancer (DCC) encodes a netrin receptor
  JOURNAL   Cell 87 (2), 175-185 (1996)
   PUBMED   8861902
REFERENCE   6  (residues 1 to 1447)
  AUTHORS   Cho,K.R., Oliner,J.D., Simons,J.W., Hedrick,L., Fearon,E.R.,
            Preisinger,A.C., Hedge,P., Silverman,G.A. and Vogelstein,B.
  TITLE     The DCC gene: structural analysis and mutations in colorectal
            carcinomas
  JOURNAL   Genomics 19 (3), 525-531 (1994)
   PUBMED   8188295
REFERENCE   7  (residues 1 to 1447)
  AUTHORS   Fearon,E.R., Ekstrand,B.C., Hu,G., Pierceall,W.E., Reale,M.A. and
            Bigner,S.H.
  TITLE     Studies of the deleted in colorectal cancer gene in normal and
            neoplastic tissues
  JOURNAL   Cold Spring Harb Symp Quant Biol 59, 637-643 (1994)
   PUBMED   7587124
REFERENCE   8  (residues 1 to 1447)
  AUTHORS   Meneret,A., Trouillard,O., Dunoyer,M., Depienne,C. and Roze,E.
  TITLE     Congenital Mirror Movements
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25763452
REFERENCE   9  (residues 1 to 1447)
  AUTHORS   Nigro,J.M., Cho,K.R., Fearon,E.R., Kern,S.E., Ruppert,J.M.,
            Oliner,J.D., Kinzler,K.W. and Vogelstein,B.
  TITLE     Scrambled exons
  JOURNAL   Cell 64 (3), 607-613 (1991)
   PUBMED   1991322
REFERENCE   10 (residues 1 to 1447)
  AUTHORS   Fearon,E.R., Cho,K.R., Nigro,J.M., Kern,S.E., Simons,J.W.,
            Ruppert,J.M., Hamilton,S.R., Preisinger,A.C., Thomas,G.,
            Kinzler,K.W. et al.
  TITLE     Identification of a chromosome 18q gene that is altered in
            colorectal cancers
  JOURNAL   Science 247 (4938), 49-56 (1990)
   PUBMED   2294591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011155.13, X76132.1,
            BC036524.1 and AC103949.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 18, 2006 this sequence version replaced NP_005206.1.
            
            Summary: This gene encodes a netrin 1 receptor. The transmembrane
            protein is a member of the immunoglobulin superfamily of cell
            adhesion molecules, and mediates axon guidance of neuronal growth
            cones towards sources of netrin 1 ligand. The cytoplasmic tail
            interacts with the tyrosine kinases Src and focal adhesion kinase
            (FAK, also known as PTK2) to mediate axon attraction. The protein
            partially localizes to lipid rafts, and induces apoptosis in the
            absence of ligand. The protein functions as a tumor suppressor, and
            is frequently mutated or downregulated in colorectal cancer and
            esophageal carcinoma. [provided by RefSeq, Oct 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X76132.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267772, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000442544.7/ ENSP00000389140.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..1447
                     /product="netrin receptor DCC"
                     /note="colorectal cancer suppressor; tumor suppressor
                     protein DCC; immunoglobulin superfamily DCC subclass
                     member 1; deleted in colorectal carcinoma; putative
                     colorectal tumor suppressor"
                     /calculated_mol_wt=158326
     Region          39..136
                     /region_name="IgI_1_Neogenin_like"
                     /note="First immunoglobulin (Ig)-like domain in neogenin,
                     and similar domains; member of the I-set of Ig superfamily
                     (IgSF) domains; cd05722"
                     /db_xref="CDD:409387"
     Region          39..42
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409387"
     Region          45..51
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409387"
     Region          55..65
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409387"
     Region          70..76
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409387"
     Region          78..81
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409387"
     Region          88..93
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409387"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Region          95..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409387"
     Region          113..120
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409387"
     Region          125..136
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409387"
     Region          139..216
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          241..327
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          257..261
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409562"
     Region          270..274
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409562"
     Region          293..297
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409562"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Region          307..312
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409562"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Region          322..325
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409562"
     Region          334..417
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          348..352
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409388"
     Region          361..365
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409388"
     Region          383..387
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409388"
     Region          397..402
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409388"
     Region          410..413
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409388"
     Region          429..521
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(429,494,509)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          <478..901
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            478
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Site            order(510..511,513..514)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            628
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Site            702
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Region          946..1041
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(1030..1031,1033..1034)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            1098..1122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     Region          1126..1152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     Region          1148..1445
                     /region_name="Neogenin_C"
                     /note="Neogenin C-terminus; pfam06583"
                     /db_xref="CDD:461954"
     Region          1165..1222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q63155; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Site            1187
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q63155; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Site            1267
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q63155; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Region          1288..1330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     Region          1394..1419
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     Region          1432..1439
                     /region_name="Interaction with MYO10.
                     /evidence=ECO:0000269|PubMed:21642953"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     CDS             1..1447
                     /gene="DCC"
                     /gene_synonym="CRC18; CRCR1; HGPPS2; IGDCC1; MRMV1;
                     NTN1R1"
                     /coded_by="NM_005215.4:592..4935"
                     /db_xref="CCDS:CCDS11952.1"
                     /db_xref="GeneID:1630"
                     /db_xref="HGNC:HGNC:2701"
                     /db_xref="MIM:120470"
ORIGIN      
        1 menslrcvwv pklafvlfga slfsahlqvt gfqikaftal rflsepsdav tmrggnvlld
       61 csaesdrgvp vikwkkdgih lalgmderkq qlsngslliq nilhsrhhkp deglyqceas
      121 lgdsgsiisr takvavagpl rflsqtesvt afmgdtvllk cevigepmpt ihwqknqqdl
      181 tpipgdsrvv vlpsgalqis rlqpgdigiy rcsarnpass rtgneaevri lsdpglhrql
      241 yflqrpsnvv aiegkdavle ccvsgyppps ftwlrgeevi qlrskkysll ggsnllisnv
      301 tdddsgmytc vvtyknenis asaeltvlvp pwflnhpsnl yayesmdief ectvsgkpvp
      361 tvnwmkngdv vipsdyfqiv ggsnlrilgv vksdegfyqc vaeneagnaq tsaqlivpkp
      421 aipsssvlps aprdvvpvlv ssrfvrlswr ppaeakgniq tftvffsreg dnreralntt
      481 qpgslqltvg nlkpeamytf rvvaynewgp gessqpikva tqpelqvpgp venlqavsts
      541 ptsilitwep payangpvqg yrlfctevst gkeqnievdg lsykleglkk fteyslrfla
      601 ynrygpgvst dditvvtlsd vpsappqnvs levvnsrsik vswlpppsgt qngfitgyki
      661 rhrkttrrge metlepnnlw ylftglekgs qysfqvsamt vngtgppsnw ytaetpendl
      721 desqvpdqps slhvrpqtnc iimswtppln pnivvrgyii gygvgspyae tvrvdskqry
      781 ysierlesss hyvislkafn nagegvplye sattrsitdp tdpvdyypll ddfptsvpdl
      841 stpmlppvgv qavalthdav rvswadnsvp knqktsevrl ytvrwrtsfs asakyksedt
      901 tslsytatgl kpntmyefsv mvtknrrsst wsmtahatty eaaptsapkd ltvitregkp
      961 ravivswqpp leangkitay ilfytldkni piddwimeti sgdrlthqim dlnldtmyyf
     1021 riqarnskgv gplsdpilfr tlkvehpdkm andqgrhgdg gywpvdtnli drstlneppi
     1081 gqmhpphgsv tpqknsnllv iivvtvgvit vlvvvivavi ctrrssaqqr kkrathsagk
     1141 rkgsqkdlrp pdlwihheem emkniekpsg tdpagrdspi qscqdltpvs hsqsetqlgs
     1201 kstshsgqdt eeagssmstl erslaarrap raklmipmda qsnnpavvsa ipvptlesaq
     1261 ypgilpsptc gyphpqftlr pvpfptlsvd rgfgagrsqs vsegpttqqp pmlppsqpeh
     1321 ssseeapsrt iptacvrpth plrsfanpll pppmsaiepk vpytpllsqp gptlpkthvk
     1381 taslglagka rspllpvsvp tapevseesh kptedsanvy eqddlseqma sleglmkqln
     1441 aitgsaf
//
LOCUS       NP_001356345             297 aa            linear   PRI 27-APR-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 2 [Homo sapiens].
ACCESSION   NP_001356345
VERSION     NP_001356345.1
DBSOURCE    REFSEQ: accession NM_001369416.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
            Review article
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Du,P., Li,G., Wu,L. and Huang,M.
  TITLE     Perspectives of ERCC1 in early-stage and advanced cervical cancer:
            From experiments to clinical applications
  JOURNAL   Front Immunol 13, 1065379 (2023)
   PUBMED   36713431
  REMARK    GeneRIF: Perspectives of ERCC1 in early-stage and advanced cervical
            cancer: From experiments to clinical applications.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 297)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 297)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 297)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 297)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139353.3 and AC092309.3.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2605344.1,
                                           SRR18074968.810513.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..297
                     /product="DNA excision repair protein ERCC-1 isoform 2"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=32431
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P07992.1)"
     Region          17..23
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          220..297
                     /region_name="HhH2, dimerization with ERCC4/XPF.
                     /evidence=ECO:0000269|PubMed:16338413"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Region          <251..293
                     /region_name="MUS81"
                     /note="ERCC4-type crossover junction endonuclease
                     [Replication, recombination and repair]; COG1948"
                     /db_xref="CDD:441551"
     CDS             1..297
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369416.1:155..1048"
                     /note="isoform 2 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS12662.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrvteclt
      241 tvksvnktds qtllttfgsl eqliaasred lalcpglgpq karrlfdvlh epflkvp
//
LOCUS       NP_001781                473 aa            linear   PRI 27-APR-2025
DEFINITION  M-phase inducer phosphatase 3 isoform a [Homo sapiens].
ACCESSION   NP_001781
VERSION     NP_001781.2
DBSOURCE    REFSEQ: accession NM_001790.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Li,Y.F., Zheng,F.Y., Miao,X.Y., Liu,H.L., Zhang,Y.Y., Chao,N.X. and
            Mo,F.R.
  TITLE     Cell division cyclin 25C knockdown inhibits hepatocellular
            carcinoma development by inducing endoplasmic reticulum stress
  JOURNAL   World J Gastroenterol 30 (19), 2564-2574 (2024)
   PUBMED   38817663
  REMARK    GeneRIF: Cell division cyclin 25C knockdown inhibits hepatocellular
            carcinoma development by inducing endoplasmic reticulum stress.
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Zhai,M., Miao,J., Zhang,R., Liu,R., Li,F., Shen,Y., Wang,T., Xu,X.,
            Gao,G., Hu,J., He,A. and Bai,J.
  TITLE     KIF22 promotes multiple myeloma progression by regulating the
            CDC25C/CDK1/cyclinB1 pathway
  JOURNAL   J Cancer Res Clin Oncol 150 (5), 239 (2024)
   PUBMED   38713252
  REMARK    GeneRIF: KIF22 promotes multiple myeloma progression by regulating
            the CDC25C/CDK1/cyclinB1 pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Xu,N., Ren,Y., Bao,Y., Shen,X., Kang,J., Wang,N., Wang,Z., Han,X.,
            Li,Z., Zuo,J., Wei,G.H., Wang,Z., Zong,W.X., Liu,W., Xie,G. and
            Wang,Y.
  TITLE     PUF60 promotes cell cycle and lung cancer progression by regulating
            alternative splicing of CDC25C
  JOURNAL   Cell Rep 42 (9), 113041 (2023)
   PUBMED   37682709
  REMARK    GeneRIF: PUF60 promotes cell cycle and lung cancer progression by
            regulating alternative splicing of CDC25C.
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 473)
  AUTHORS   Bureik,M., Rief,N., Drescher,R., Jungbluth,A., Montenarh,M. and
            Wagner,P.
  TITLE     An additional transcript of the cdc25C gene from A431 cells encodes
            a functional protein
  JOURNAL   Int J Oncol 17 (6), 1251-1258 (2000)
   PUBMED   11078813
REFERENCE   6  (residues 1 to 473)
  AUTHORS   Wegener,S., Hampe,W., Herrmann,D. and Schaller,H.C.
  TITLE     Alternative splicing in the regulatory region of the human
            phosphatases CDC25A and CDC25C
  JOURNAL   Eur J Cell Biol 79 (11), 810-815 (2000)
   PUBMED   11139144
REFERENCE   7  (residues 1 to 473)
  AUTHORS   Sartor,H., Ehlert,F., Grzeschik,K.H., Muller,R. and Adolph,S.
  TITLE     Assignment of two human cell cycle genes, CDC25C and CCNB1, to 5q31
            and 5q12, respectively
  JOURNAL   Genomics 13 (3), 911-912 (1992)
   PUBMED   1386342
REFERENCE   8  (residues 1 to 473)
  AUTHORS   Galaktionov,K. and Beach,D.
  TITLE     Specific activation of cdc25 tyrosine phosphatases by B-type
            cyclins: evidence for multiple roles of mitotic cyclins
  JOURNAL   Cell 67 (6), 1181-1194 (1991)
   PUBMED   1836978
REFERENCE   9  (residues 1 to 473)
  AUTHORS   Strausfeld,U., Labbe,J.C., Fesquet,D., Cavadore,J.C., Picard,A.,
            Sadhu,K., Russell,P. and Doree,M.
  TITLE     Dephosphorylation and activation of a p34cdc2/cyclin B complex in
            vitro by human CDC25 protein
  JOURNAL   Nature 351 (6323), 242-245 (1991)
   PUBMED   1828290
REFERENCE   10 (residues 1 to 473)
  AUTHORS   Gould,K.L., Moreno,S., Tonks,N.K. and Nurse,P.
  TITLE     Complementation of the mitotic activator, p80cdc25, by a human
            protein-tyrosine phosphatase
  JOURNAL   Science 250 (4987), 1573-1576 (1990)
   PUBMED   1703321
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104116.3, M34065.1,
            DB040755.1 and AW512559.1.
            
            On Feb 9, 2007 this sequence version replaced NP_001781.1.
            
            Summary: This gene encodes a conserved protein that plays a key
            role in the regulation of cell division. The encoded protein
            directs dephosphorylation of cyclin B-bound CDC2 and triggers entry
            into mitosis. It also suppresses p53-induced growth arrest.
            Multiple alternatively spliced transcript variants of this gene
            have been described. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) encodes isoform a. Variants 1
            and 3 encode the same protein (isoform a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M34065.1, SRR1163657.23.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267752 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323760.11/ ENSP00000321656.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.2"
     Protein         1..473
                     /product="M-phase inducer phosphatase 3 isoform a"
                     /EC_number="3.1.3.48"
                     /note="dual specificity phosphatase CDC25C; mitosis
                     inducer CDC25; phosphotyrosine phosphatase; protein
                     phosphatase 1, regulatory subunit 60; CDC25 homolog C;
                     M-phase inducer phosphatase 3"
                     /calculated_mol_wt=53234
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30307.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:8119945,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000305;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P30307.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:8119945,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P30307.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000305|PubMed:8119945; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12595692; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:12595692; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Region          132..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30307.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8119945,
                     ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:14968113; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:14968113; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Region          <207..447
                     /region_name="MIH1"
                     /note="Mitotic inducer, protein phosphatase [Cell division
                     and chromosome partitioning]; COG5105"
                     /db_xref="CDD:227436"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000305|PubMed:8119945; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CHEK1, CHEK2, BRSK1, MAPK14 AND
                     MARK3. /evidence=ECO:0000269|PubMed:11333986,
                     ECO:0000269|PubMed:15150265, ECO:0000269|PubMed:15629715,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     Region          302..421
                     /region_name="Cdc25"
                     /note="Cdc25 phosphatases are members of the Rhodanese
                     Homology Domain superfamily. They activate the cell
                     division kinases throughout the cell cycle progression.
                     Cdc25 phosphatases dephosphorylate phosphotyrosine and
                     phosphothreonine residues, in order to...; cd01530"
                     /db_xref="CDD:238788"
     Region          334..379
                     /region_name="HIV-1 Vpr binding site"
                     /note="propagated from UniProtKB/Swiss-Prot (P30307.2)"
     Site            377..383
                     /site_type="active"
                     /note="oxyanion binding site [active]"
                     /db_xref="CDD:238788"
     Site            377
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238788"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P30307.2)"
     CDS             1..473
                     /gene="CDC25C"
                     /gene_synonym="CDC25; PPP1R60"
                     /coded_by="NM_001790.5:249..1670"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4202.1"
                     /db_xref="GeneID:995"
                     /db_xref="HGNC:HGNC:1727"
                     /db_xref="MIM:157680"
ORIGIN      
        1 mstelfsstr eegssgsgps frsnqrkmln lllerdtsft vcpdvprtpv gkflgdsanl
       61 silsggtpkr cldlsnlssg eitatqltts adldetghld ssglqevhla gmnhdqhlmk
      121 cspaqllcst pngldrghrk rdamcsssan kendngnlvd semkylgspi ttvpkldknp
      181 nlgedqaeei sdelmefslk dqeakvsrsg lyrspsmpen lnrprlkqve kfkdntipdk
      241 vkkkyfsgqg klrkglclkk tvslcditit qmleedsnqg hligdfskvc alptvsgkhq
      301 dlkyvnpetv aallsgkfqg liekfyvidc rypyeylggh iqgalnlysq eelfnfflkk
      361 pivpldtqkr iiivfhcefs sergprmcrc lreedrslnq ypalyypely ilkggyrdff
      421 peymelcepq sycpmhhqdh ktellrcrsq skvqegerql reqiallvkd msp
//
LOCUS       NP_008889                682 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 16 isoform 1 [Homo sapiens].
ACCESSION   NP_008889
VERSION     NP_008889.2
DBSOURCE    REFSEQ: accession NM_006958.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Zhang,H., Song,Y., Du,Z., Li,X., Zhang,J., Chen,S., Chen,F., Li,T.
            and Zhan,Q.
  TITLE     Exome sequencing identifies new somatic alterations and mutation
            patterns of tongue squamous cell carcinoma in a Chinese population
  JOURNAL   J Pathol 251 (4), 353-364 (2020)
   PUBMED   32432340
  REMARK    GeneRIF: Exome sequencing identifies new somatic alterations and
            mutation patterns of tongue squamous cell carcinoma in a Chinese
            population.
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Ahn,S.W., Ahn,A.R., Ha,S.H., Hussein,U.K., Do Yang,J., Kim,K.M.,
            Park,H.S., Park,S.H., Yu,H.C. and Jang,K.Y.
  TITLE     Expression of FAM83H and ZNF16 are associated with shorter survival
            of patients with gallbladder carcinoma
  JOURNAL   Diagn Pathol 15 (1), 63 (2020)
   PUBMED   32460791
  REMARK    GeneRIF: Expression of FAM83H and ZNF16 are associated with shorter
            survival of patients with gallbladder carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Chen,J., Li,X.B., Su,R., Song,L., Wang,F. and Zhang,J.W.
  TITLE     ZNF16 (HZF1) promotes erythropoiesis and megakaryocytopoiesis via
            regulation of the c-KIT gene
  JOURNAL   Biochem J 458 (1), 171-183 (2014)
   PUBMED   24180487
  REMARK    GeneRIF: study demonstrate that ZNF16 plays an important role in
            erythropoiesis and megakaryocytopoiesis via its regulation of the
            c-Kit/c-Raf/MEK/ERK/c-Jun/HEY1/GATA1 cascade
REFERENCE   5  (residues 1 to 682)
  AUTHORS   Li,X.B., Chen,J., Deng,M.J., Wang,F., Du,Z.W. and Zhang,J.W.
  TITLE     Zinc finger protein HZF1 promotes K562 cell proliferation by
            interacting with and inhibiting INCA1
  JOURNAL   Mol Med Rep 4 (6), 1131-1137 (2011)
   PUBMED   21874239
REFERENCE   6  (residues 1 to 682)
  AUTHORS   Lorenz,P., Dietmann,S., Wilhelm,T., Koczan,D., Autran,S., Gad,S.,
            Wen,G., Ding,G., Li,Y., Rousseau-Merck,M.F. and Thiesen,H.J.
  TITLE     The ancient mammalian KRAB zinc finger gene cluster on human
            chromosome 8q24.3 illustrates principles of C2H2 zinc finger
            evolution associated with unique expression profiles in human
            tissues
  JOURNAL   BMC Genomics 11, 206 (2010)
   PUBMED   20346131
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 682)
  AUTHORS   Deng,M.J., Li,X.B., Peng,H. and Zhang,J.W.
  TITLE     Identification of the trans-activation domain and the nuclear
            location signals of human zinc finger protein HZF1 (ZNF16)
  JOURNAL   Mol Biotechnol 44 (2), 83-89 (2010)
   PUBMED   19763908
REFERENCE   8  (residues 1 to 682)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 682)
  AUTHORS   Peng,H., Du,Z.W. and Zhang,J.W.
  TITLE     Identification and characterization of a novel zinc finger protein
            (HZF1) gene and its function in erythroid and megakaryocytic
            differentiation of K562 cells
  JOURNAL   Leukemia 20 (6), 1109-1116 (2006)
   PUBMED   16628192
REFERENCE   10 (residues 1 to 682)
  AUTHORS   Rousseau-Merck,M.F., Duro,D., Berger,R. and Thiesen,H.J.
  TITLE     Chromosomal localization of two KOX zinc finger genes on chromosome
            bands 7q21-q22
  JOURNAL   Ann Genet 38 (2), 81-84 (1995)
   PUBMED   7486829
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK127625.1 and AF244088.1.
            
            On Oct 30, 2003 this sequence version replaced NP_008889.1.
            
            Summary: The protein encoded by this gene contains multiple tandem
            zinc finger motifs. The encoded protein is involved in the
            differentiation of erythroid and megakaryocytic cells. This gene is
            located in a cluster of related genes on chromosome 8 encoding zinc
            finger proteins. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2012].
            
            Transcript Variant: This variant (1) lacks an alternate exon in the
            5' UTR and encodes the same protein, as compared to transcript
            variant 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.463278.1, AK127625.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146, SAMEA2467148
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394909.7/ ENSP00000378369.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..682
                     /product="zinc finger protein 16 isoform 1"
                     /note="zinc finger protein KOX9; zinc finger protein
                     Kruppel type 9"
                     /calculated_mol_wt=76341
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17020.3)"
     Region          62..210
                     /region_name="Necessary for transcription activation"
                     /note="propagated from UniProtKB/Swiss-Prot (P17020.3)"
     Region          <160..369
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          187..203
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          211..231
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          239..259
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          267..287
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          268..393
                     /region_name="Required for nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (P17020.3)"
     Region          295..315
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          303..675
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          323..343
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(328,330,332,334..335,338..339,342,356,358,362..363,
                     366..367,370,384,386,388,390..391,394..395,398)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          341..373
                     /region_name="Required for nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (P17020.3)"
     Region          351..371
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          379..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          407..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          463..483
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          473..503
                     /region_name="Required for nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (P17020.3)"
     Site            487
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P17020.3)"
     Region          491..511
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(496,498,500,502..503,506..507,510,524,526,530..531,
                     534..535,538,552,554,556,558..559,562..563,566)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          519..539
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          547..567
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          575..595
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(580,582,584,586..587,590..591,594,608,610,614..615,
                     618..619,622,636,638,640,642..643,646..647,650)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          603..623
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          631..651
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          659..679
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..682
                     /gene="ZNF16"
                     /gene_synonym="HZF1; KOX9"
                     /coded_by="NM_006958.3:94..2142"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6437.1"
                     /db_xref="GeneID:7564"
                     /db_xref="HGNC:HGNC:12947"
                     /db_xref="MIM:601262"
ORIGIN      
        1 mpslrtrree aemelsvpgp spwtpaaqar vrdapavthp gsaacgtpcc sdteleaicp
       61 hyqqpdcdtr tedkeflhke dihedlesqa eisenyagdv sqvpelgdlc ddvserdwgv
      121 pegrrlpqsl sqegdftpaa mgllrgplge kdldcngfds rfslspnlma cqeipteerp
      181 hpydmggqsf qhsvdltghe gvptaespli cnecgktfqg npdliqrqiv htgeasfmcd
      241 dcgktfsqns vlknrhrshm sekayqcsec gkafrghsdf srhqshhsse rpymcnecgk
      301 afsqnsslkk hqkshmsekp yecnecgkaf rrssnliqhq rihsgekpyv csecgkafrr
      361 ssnlikhhrt htgekpfecg ecgkafsqsa hlrkhqrvht gekpyecndc gkpfsrvsnl
      421 ikhhrvhtge kpykcsdcgk afsqsssliq hrrihtgekp hvcnvcgkaf syssvlrkhq
      481 iihtgekpyr csvcgkafsh ssaliqhqgv htgdkpyach ecgktfgrss nlilhqrvht
      541 gekpyectec gktfsqsstl iqhqrihngl kphecnqcgk afnrssnlih hqkvhtgekp
      601 ytcvecgkgf sqsshliqhq iihtgerpyk csecgkafsq rsvliqhqri htgvkpydca
      661 acgkafsqrs klikhqliht re
//
LOCUS       NP_001347403             265 aa            linear   ROD 27-APR-2025
DEFINITION  8-oxo-dGDP phosphatase NUDT18 isoform 2 [Mus musculus].
ACCESSION   NP_001347403 XP_006518855
VERSION     NP_001347403.1
DBSOURCE    REFSEQ: accession NM_001360474.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Tamplin,O.J., Cox,B.J. and Rossant,J.
  TITLE     Integrated microarray and ChIP analysis identifies multiple Foxa2
            dependent target genes in the notochord
  JOURNAL   Dev Biol 360 (2), 415-425 (2011)
   PUBMED   22008794
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC122268.5, AK157937.1 and AK089446.1.
            
            On Feb 6, 2018 this sequence version replaced XP_006518855.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036718.1, BI663618.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849384
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 36.32 cM"
     Protein         1..265
                     /product="8-oxo-dGDP phosphatase NUDT18 isoform 2"
                     /EC_number="3.6.1.58"
                     /note="mutT homolog 3; 2-hydroxy-dADP phosphatase;
                     7,8-dihydro-8-oxoguanine phosphatase; 8-oxo-dGDP
                     phosphatase NUDT18; nudix (nucleoside diphosphate linked
                     moiety X)-type motif 18"
                     /calculated_mol_wt=29479
     Region          1..115
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     CDS             1..265
                     /gene="Nudt18"
                     /coded_by="NM_001360474.1:422..1219"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS88705.1"
                     /db_xref="GeneID:213484"
                     /db_xref="MGI:MGI:2385853"
ORIGIN      
        1 miqeakrecr gtwylpagrm epgetiveam qrevkeeagl lcepvtllsv eergaswirf
       61 vflarptggv lktskdadse slqagwyprv slptplrahd vlhlvelgak fcqqamhpli
      121 lpqelpcsvv cqrlvttftt vqsvwvlvgt vgtphlpita cgftpmeqrg gikvailrll
      181 qecltlhsla vetkgllglq hlgrdhvdgv clnvlvtvaf rnpgiqdepp kirgenyfww
      241 kvleedlqkl llyrlqessv iplsr
//
LOCUS       NP_001356877             521 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 12 [Homo
            sapiens].
ACCESSION   NP_001356877
VERSION     NP_001356877.1
DBSOURCE    REFSEQ: accession NM_001369948.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.198516.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..521
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 12"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=59181
     Region          233..272
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..521
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369948.1:945..2510"
                     /note="isoform 12 is encoded by transcript variant 31"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mpllelkdiv lylcdtcttl wafldifpla cqtfqkhdfc yrlasfyeaa ipemesaikk
       61 rrledskllg dlwqrlshsr kklmeifhii lnqicllpil esscdniqgf ieeflqifss
      121 llqekrflrd ydalfpvaed isllqqassv ldetrtayil qavesawegv drrkatdakd
      181 psvieepnge pngvtvtaea vsqasshpen seeeecmgaa aavgpamcgv eldslisqvk
      241 dllpdlgegf ilacleyyhy dpeqvinnil eerlaptlsq ldrnldremk pdptplltsr
      301 hnvfqndefd vfsrdsvdls rvhkgkstrk eentrsllnd kravaaqrqr yeqysvvvee
      361 vplqpgeslp yhsvyyedey ddtydgnqvg andadsddel isrrpftipq vlrtkvpreg
      421 qeeddddeed dadeeapkpd hfvqdpavlr ekaearrmaf lakkgyrhds stavagsprg
      481 hgqsrettqe rrkkeankat ranhnrrtma drkrskgmip s
//
LOCUS       NP_057064                171 aa            linear   PRI 27-APR-2025
DEFINITION  neuronal vesicle trafficking-associated protein 2 [Homo sapiens].
ACCESSION   NP_057064
VERSION     NP_057064.1
DBSOURCE    REFSEQ: accession NM_015980.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Chander,P., Kennedy,M.J., Winckler,B. and Weick,J.P.
  TITLE     Neuron-Specific Gene 2 (NSG2) Encodes an AMPA Receptor Interacting
            Protein That Modulates Excitatory Neurotransmission
  JOURNAL   eNeuro 6 (1) (2019)
   PUBMED   30680309
  REMARK    GeneRIF: found in discrete punctae restricted to the
            somatodendritic arbors of developing mouse and human neurons, and a
            significant proportion of NSG2 punctae colocalize with postsynaptic
            HOMER1 and surface-expressed AMPA-type glutamate receptors (AMPARs)
            at excitatory synapses.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 171)
  AUTHORS   Muthusamy,N., Chen,Y.J., Yin,D.M., Mei,L. and Bergson,C.
  TITLE     Complementary roles of the neuron-enriched endosomal proteins
            NEEP21 and calcyon in neuronal vesicle trafficking
  JOURNAL   J Neurochem 132 (1), 20-31 (2015)
   PUBMED   25376768
  REMARK    Review article
REFERENCE   6  (residues 1 to 171)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   7  (residues 1 to 171)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 171)
  AUTHORS   Fu,G.K., Wang,J.T., Yang,J., Au-Young,J. and Stuve,L.L.
  TITLE     Circular rapid amplification of cDNA ends for high-throughput
            extension cloning of partial genes
  JOURNAL   Genomics 84 (1), 205-210 (2004)
   PUBMED   15203218
REFERENCE   9  (residues 1 to 171)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   10 (residues 1 to 171)
  AUTHORS   Saberan-Djoneidi,D., Marey-Semper,I., Picart,R., Studler,J.M.,
            Tougard,C., Glowinski,J. and Levi-Strauss,M.
  TITLE     A 19-kDa protein belonging to a new family is expressed in the
            Golgi apparatus of neural cells
  JOURNAL   J Biol Chem 270 (4), 1888-1893 (1995)
   PUBMED   7829526
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC366641.1, BC002619.2, CD627354.1 and EL950772.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.717650.1,
                                           SRR3476690.104183.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303177.8/ ENSP00000307722.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..171
                     /product="neuronal vesicle trafficking-associated protein
                     2"
                     /note="hypothalamus golgi apparatus expressed 19 kDa
                     protein; calcyon family member 3; neuron-specific protein
                     family member 2; p19 protein; protein p19"
                     /calculated_mol_wt=18954
     Region          1..162
                     /region_name="Calcyon"
                     /note="D1 dopamine receptor-interacting protein (calcyon);
                     pfam06387"
                     /db_xref="CDD:461892"
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y328.1)"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y328.1)"
     CDS             1..171
                     /gene="NSG2"
                     /gene_synonym="CALY3; HMP19"
                     /coded_by="NM_015980.5:161..676"
                     /db_xref="CCDS:CCDS4391.1"
                     /db_xref="GeneID:51617"
                     /db_xref="HGNC:HGNC:24955"
                     /db_xref="MIM:616752"
ORIGIN      
        1 mvklnsnpse kgtkppsved gfqtvplitp levnhlqlpa pekvivktrt eyqpeqknkg
       61 kfrvpkiaef tvtilvslal aflacivflv vykaftydhs cpegfvykhk rcipaslday
      121 yssqdpnsrs rfytvishys vakqstarai gpwlsaaavi hepkppktqg h
//
LOCUS       NP_665825                637 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-17 receptor E isoform 1 precursor [Mus musculus].
ACCESSION   NP_665825
VERSION     NP_665825.2
DBSOURCE    REFSEQ: accession NM_145826.6
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Wang,J., Wang,X., Wang,M., Wang,J., Wu,Y. and Qi,X.
  TITLE     Clinical significance of Interleukin 17 receptor E in diabetic
            nephropathy
  JOURNAL   Int Immunopharmacol 120, 110324 (2023)
   PUBMED   37235960
  REMARK    GeneRIF: Clinical significance of Interleukin 17 receptor E in
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Lin,X., Gaudino,S.J., Jang,K.K., Bahadur,T., Singh,A., Banerjee,A.,
            Beaupre,M., Chu,T., Wong,H.T., Kim,C.K., Kempen,C., Axelrad,J.,
            Huang,H., Khalid,S., Shah,V., Eskiocak,O., Parks,O.B., Berisha,A.,
            McAleer,J.P., Good,M., Hoshino,M., Blumberg,R., Bialkowska,A.B.,
            Gaffen,S.L., Kolls,J.K., Yang,V.W., Beyaz,S., Cadwell,K. and
            Kumar,P.
  TITLE     IL-17RA-signaling in Lgr5+ intestinal stem cells induces expression
            of transcription factor ATOH1 to promote secretory cell lineage
            commitment
  JOURNAL   Immunity 55 (2), 237-253 (2022)
   PUBMED   35081371
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Wang,J., Gong,J., Yang,Q., Wang,L., Jian,Y. and Wang,P.
  TITLE     Interleukin-17 Receptor E and C-C Motif Chemokine Receptor 10
            Identify Heterogeneous T Helper 17 Subsets in a Mouse Dry Eye
            Disease Model
  JOURNAL   Am J Pathol 192 (2), 332-343 (2022)
   PUBMED   35144761
  REMARK    GeneRIF: Interleukin-17 Receptor E and C-C Motif Chemokine Receptor
            10 Identify Heterogeneous T Helper 17 Subsets in a Mouse Dry Eye
            Disease Model.
REFERENCE   4  (residues 1 to 637)
  AUTHORS   Hansakon,A., Jeerawattanawart,S., Pattanapanyasat,K. and
            Angkasekwinai,P.
  TITLE     IL-25 Receptor Signaling Modulates Host Defense against
            Cryptococcus neoformans Infection
  JOURNAL   J Immunol 205 (3), 674-685 (2020)
   PUBMED   32561567
  REMARK    GeneRIF: IL-25 Receptor Signaling Modulates Host Defense against
            Cryptococcus neoformans Infection.
REFERENCE   5  (residues 1 to 637)
  AUTHORS   Vella,G., Lunding,L., Ritzmann,F., Honecker,A., Herr,C.,
            Wegmann,M., Bals,R. and Beisswenger,C.
  TITLE     The IL-17 receptor IL-17RE mediates polyIC-induced exacerbation of
            experimental allergic asthma
  JOURNAL   Respir Res 21 (1), 176 (2020)
   PUBMED   32641167
  REMARK    GeneRIF: The IL-17 receptor IL-17RE mediates polyIC-induced
            exacerbation of experimental allergic asthma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 637)
  AUTHORS   Chang,S.H., Reynolds,J.M., Pappu,B.P., Chen,G., Martinez,G.J. and
            Dong,C.
  TITLE     Interleukin-17C promotes Th17 cell responses and autoimmune disease
            via interleukin-17 receptor E
  JOURNAL   Immunity 35 (4), 611-621 (2011)
   PUBMED   21982598
  REMARK    GeneRIF: IL-17C-IL-17RE induced the expression of a nuclear IkappaB
            family member, IkappaBzeta, in Th17 cells to potentiate the Th17
            cell response
REFERENCE   7  (residues 1 to 637)
  AUTHORS   Ramirez-Carrozzi,V., Sambandam,A., Luis,E., Lin,Z., Jeet,S.,
            Lesch,J., Hackney,J., Kim,J., Zhou,M., Lai,J., Modrusan,Z., Sai,T.,
            Lee,W., Xu,M., Caplazi,P., Diehl,L., de Voss,J., Balazs,M.,
            Gonzalez,L. Jr., Singh,H., Ouyang,W. and Pappu,R.
  TITLE     IL-17C regulates the innate immune function of epithelial cells in
            an autocrine manner
  JOURNAL   Nat Immunol 12 (12), 1159-1166 (2011)
   PUBMED   21993848
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 637)
  AUTHORS   Swaidani,S., Bulek,K., Kang,Z., Liu,C., Lu,Y., Yin,W., Aronica,M.
            and Li,X.
  TITLE     The critical role of epithelial-derived Act1 in IL-17- and
            IL-25-mediated pulmonary inflammation
  JOURNAL   J Immunol 182 (3), 1631-1640 (2009)
   PUBMED   19155512
REFERENCE   9  (residues 1 to 637)
  AUTHORS   Li,T.S., Li,X.N., Chang,Z.J., Fu,X.Y. and Liu,L.
  TITLE     Identification and functional characterization of a novel
            interleukin 17 receptor: a possible mitogenic activation through
            ras/mitogen-activated protein kinase signaling pathway
  JOURNAL   Cell Signal 18 (8), 1287-1298 (2006)
   PUBMED   16310341
REFERENCE   10 (residues 1 to 637)
  AUTHORS   Maezawa,Y., Nakajima,H., Suzuki,K., Tamachi,T., Ikeda,K., Inoue,J.,
            Saito,Y. and Iwamoto,I.
  TITLE     Involvement of TNF receptor-associated factor 6 in IL-25 receptor
            signaling
  JOURNAL   J Immunol 176 (2), 1013-1018 (2006)
   PUBMED   16393988
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC153910.6.
            
            On Jun 10, 2003 this sequence version replaced NP_665825.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK046302.1, AK046713.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 52.76 cM"
     Protein         1..637
                     /product="interleukin-17 receptor E isoform 1 precursor"
                     /note="IL-17 receptor E"
                     /calculated_mol_wt=68532
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BH06.1)"
                     /calculated_mol_wt=2319
     mat_peptide     24..637
                     /product="Interleukin-17 receptor E. /id=PRO_0000309468"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH06.1)"
                     /calculated_mol_wt=68532
     Region          56..408
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Region          87..134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH06.1)"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BH06.1)"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BH06.1)"
     Site            415..435
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH06.1)"
     Region          448..575
                     /region_name="SEFIR"
                     /note="SEFIR domain; pfam08357"
                     /db_xref="CDD:254756"
     CDS             1..637
                     /gene="Il17re"
                     /gene_synonym="IL-17RE; Il25r"
                     /coded_by="NM_145826.6:125..2038"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS20420.1"
                     /db_xref="GeneID:57890"
                     /db_xref="MGI:MGI:1889371"
ORIGIN      
        1 mgsprlaall lslpllligl avsarvacpc lrswtshcll ayrvdkrfag lqwgwfpllv
       61 rksksppkfe dywrhrtpas fqrkllgsps lseeshrisi pssaishrgq rtkraqpsaa
      121 egrehlpeag sqkcggpefs fdllpevqav rvtipagpka svrlcyqwal ecedlsspfd
      181 tqkivsgght vdlpyefllp cmcieasylq edtvrrkkcp fqswpeaygs dfwqsirftd
      241 ysqhnqmvma ltlrcplkle aslcwrqdpl tpcetlpnat aqesegwyil envdlhpqlc
      301 fkfsfenssh vecphqsgsl pswtvsmdtq aqqltlhfss rtyatfsaaw sdpglgpdtp
      361 mppvysisqt qgsvpvtldl iipflrqenc ilvwrsdvhf awkhvlcpdv shrhlgllil
      421 allaltalvg vvlvllgrrl lpgsgrtrpv lllhaadsea qrrlvgalae llrtalgggr
      481 dvivdlwegt hvarigplpw lwaarervar eqgtvlllwn cagpstacsg dpqaaslrtl
      541 lcaaprplll ayfsrlcakg diprplralp ryrllrdlpr llraldaqpa tlasswshlg
      601 akrclknrle qchlleleaa kddyqgstns pcgfscl
//
LOCUS       NP_113637                920 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger MIZ domain-containing protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_113637 XP_371897 XP_374430
VERSION     NP_113637.3
DBSOURCE    REFSEQ: accession NM_031449.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Gan,X., Feng,Y., Liu,Y., Lin,X., Yu,X., Rong,X. and Han,Q.
  TITLE     Identification of zinc finger MIZ-type containing 2 as an
            oncoprotein enhancing NAD-dependent protein deacetylase sirtuin-1
            deacetylase activity to regulate Wnt and Hippo pathways in
            non-small-cell lung cancer
  JOURNAL   Cell Mol Biol Lett 29 (1), 122 (2024)
   PUBMED   39266996
  REMARK    GeneRIF: Identification of zinc finger MIZ-type containing 2 as an
            oncoprotein enhancing NAD-dependent protein deacetylase sirtuin-1
            deacetylase activity to regulate Wnt and Hippo pathways in
            non-small-cell lung cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Zhu,Y., Gu,L., Lin,X., Cui,K., Liu,C., Lu,B., Zhou,F., Zhao,Q.,
            Shen,H. and Li,Y.
  TITLE     LINC00265 promotes colorectal tumorigenesis via ZMIZ2 and
            USP7-mediated stabilization of beta-catenin
  JOURNAL   Cell Death Differ 27 (4), 1316-1327 (2020)
   PUBMED   31527801
  REMARK    GeneRIF: LINC00265 promotes colorectal tumorigenesis via ZMIZ2 and
            USP7-mediated stabilization of beta-catenin.
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   7  (residues 1 to 920)
  AUTHORS   Peng,Y., Lee,J., Zhu,C. and Sun,Z.
  TITLE     A novel role for protein inhibitor of activated STAT (PIAS)
            proteins in modulating the activity of Zimp7, a novel PIAS-like
            protein, in androgen receptor-mediated transcription
  JOURNAL   J Biol Chem 285 (15), 11465-11475 (2010)
   PUBMED   20159969
  REMARK    GeneRIF: there is an interaction between Zimp7 and PIAS proteins
            with higher preference for PIAS3, in androgen receptor-mediated
            transcription
REFERENCE   8  (residues 1 to 920)
  AUTHORS   Li,X., Thyssen,G., Beliakoff,J. and Sun,Z.
  TITLE     The novel PIAS-like protein hZimp10 enhances Smad transcriptional
            activity
  JOURNAL   J Biol Chem 281 (33), 23748-23756 (2006)
   PUBMED   16777850
REFERENCE   9  (residues 1 to 920)
  AUTHORS   Huang,C.Y., Beliakoff,J., Li,X., Lee,J., Li,X., Sharma,M., Lim,B.
            and Sun,Z.
  TITLE     hZimp7, a novel PIAS-like protein, enhances androgen
            receptor-mediated transcription and interacts with SWI/SNF-like BAF
            complexes
  JOURNAL   Mol Endocrinol 19 (12), 2915-2929 (2005)
   PUBMED   16051670
  REMARK    GeneRIF: hZimp7 modulates androgen receptor and/or other nuclear
            receptor-mediated transcription, possibly through alteration of
            chromatin structure by SWI/SNF-like BAF complexes.
REFERENCE   10 (residues 1 to 920)
  AUTHORS   Ueki,N., Oda,T., Kondo,M., Yano,K., Noguchi,T. and Muramatsu,M.
  TITLE     Selection system for genes encoding nuclear-targeted proteins
  JOURNAL   Nat Biotechnol 16 (13), 1338-1342 (1998)
   PUBMED   9853615
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004859.3, AK090415.1, AY426594.1, BI115680.1, AK128359.1 and
            CD367243.1.
            
            On or before Oct 25, 2004 this sequence version replaced
            XP_374430.1, XP_371897.1, NP_113637.2.
            
            Summary: ZMIZ2 and ZMIZ1 (MIM 607159) are members of a PIAS (see
            MIM 603566)-like family of proteins that interact with nuclear
            hormone receptors. ZMIZ2 interacts with androgen receptor (AR; MIM
            313700) and enhances AR-mediated transcription (Huang et al., 2005
            [PubMed 16051670]).[supplied by OMIM, May 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and it encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK090415.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309315.9/ ENSP00000311778.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..920
                     /product="zinc finger MIZ domain-containing protein 2
                     isoform 1"
                     /note="zinc finger MIZ domain-containing protein 2;
                     PIAS-like protein Zimp7"
                     /calculated_mol_wt=96406
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NF64.2)"
     Region          54..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NF64.2)"
     Site            111
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8CIE2; propagated from
                     UniProtKB/Swiss-Prot (Q8NF64.2)"
     Region          <181..297
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Region          <197..428
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          243..265
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NF64.2)"
     Site            245
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8NF64.2)"
     Site            262
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8NF64.2)"
     Region          286..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NF64.2)"
     Region          435..506
                     /region_name="Interaction with AR.
                     /evidence=ECO:0000269|PubMed:16051670"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NF64.2)"
     Region          595..657
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(600,603,616,618,623,626,639,642)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438111"
     Region          803..920
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NF64.2)"
     CDS             1..920
                     /gene="ZMIZ2"
                     /gene_synonym="hZIMP7; NET27; TRAFIP20; ZIMP7"
                     /coded_by="NM_031449.4:208..2970"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43576.1"
                     /db_xref="GeneID:83637"
                     /db_xref="HGNC:HGNC:22229"
                     /db_xref="MIM:611196"
ORIGIN      
        1 mnsmnpmkpa lppaphgdgs fayesvpwqq satqpagsls vvttvwgvgn atqsqvlgnp
       61 mgpagspsgs smmpgvaggs saltspqclg qqafaeggan kgyvqqgvys rggypgapgf
      121 ttgyaggpgg lglpshaarp stdftqaaaa aavaaaaata tatatatvaa lqekqsqels
      181 qygamgagqs fnsqflqhgg prgpsvpagm nptgiggvmg psglsplamn ptraagmtpl
      241 yagqrlpqhg ypgppqaqpl prqgvkrtys evypgqqylq ggqyapstaq fapspgqppa
      301 pspsypghrl plqqgmtqsl svpgptglhy kpteqfngqg asfnggsvsy sqpglsgptr
      361 sipgypsspl pgnptppmtp sssvpymspn qevkspflpd lkpnlnslhs spsgsgpcde
      421 lrltfpvrdg vvlepfrlqh nlavsnhvfq lrdsvyktli mrpdlelqfk cyhhedrqmn
      481 tnwpasvqvs vnatpltier gdnktshkpl ylkhvcqpgr ntiqitvtac ccshlfvlql
      541 vhrpsvrsvl qgllkkrllp aehcitkikr nfssgtipgt pgpngedgve qtaikvslkc
      601 pitfrriqlp arghdcrhiq cfdlesylql ncergtwrcp vcnktalleg levdqymlgi
      661 liyiqnsdye eitidptcsw kpvpvkpdmh ikeepdgpal krcrtvspah vlmpsvmemi
      721 aalgpgaapf aplqppsvpa psdypgqgss flgpgtfpes fppttpstpt laeftpgppp
      781 isyqsdipss lltsekstac lpsqmapagh ldpthnpgtp glhtsnlgap pgpqlhhsnp
      841 ppasrqslgq aslgptgela fspatgvmgp psmsgageap epaldllpel tnpdellsyl
      901 gppdlptnnn ddllslfenn
//
LOCUS       NP_067421                140 aa            linear   ROD 27-APR-2025
DEFINITION  ergosterol biosynthetic protein 28 homolog isoform 1 [Mus
            musculus].
ACCESSION   NP_067421
VERSION     NP_067421.1
DBSOURCE    REFSEQ: accession NM_021446.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Easterday,M.C., Dougherty,J.D., Jackson,R.L., Ou,J., Nakano,I.,
            Paucar,A.A., Roobini,B., Dianati,M., Irvin,D.K., Weissman,I.L.,
            Terskikh,A.V., Geschwind,D.H. and Kornblum,H.I.
  TITLE     Neural progenitor genes. Germinal zone expression and analysis of
            genetic overlap in stem cell populations
  JOURNAL   Dev Biol 264 (2), 309-322 (2003)
   PUBMED   14651920
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Nelson,P.S., Pritchard,C., Abbott,D. and Clegg,N.
  TITLE     The human (PEDB) and mouse (mPEDB) Prostate Expression Databases
  JOURNAL   Nucleic Acids Res 30 (1), 218-220 (2002)
   PUBMED   11752298
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Ottolenghi,C., Daizadeh,I., Ju,A., Kossida,S., Renault,G.,
            Jacquet,M., Fellous,A., Gilbert,W. and Veitia,R.
  TITLE     The genomic structure of c14orf1 is conserved across eukarya
  JOURNAL   Mamm Genome 11 (9), 786-788 (2000)
   PUBMED   10967139
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138303.4, AK004480.1 and AI844820.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004591.1, AK004480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 39.81 cM"
     Protein         1..140
                     /product="ergosterol biosynthetic protein 28 homolog
                     isoform 1"
                     /note="probable ergosterol biosynthetic protein 28;
                     c14orf1-like protein; ergosterol biosynthetic protein 28
                     homolog"
                     /calculated_mol_wt=15675
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERY9.1)"
     Region          8..119
                     /region_name="Erg28"
                     /note="Erg28 like protein; pfam03694"
                     /db_xref="CDD:461015"
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERY9.1)"
     Site            79..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERY9.1)"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERY9.1)"
     CDS             1..140
                     /gene="Erg28"
                     /gene_synonym="0610007P14Rik; 1190004E09Rik; ORF11"
                     /coded_by="NM_021446.3:452..874"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS26063.1"
                     /db_xref="GeneID:58520"
                     /db_xref="MGI:MGI:1915571"
ORIGIN      
        1 msrflnvlrs wlvmvsiiam gntlqsfrdh tflyeklytg kpnlvnglqa rtfgiwtlls
       61 svirclcaid ihnktlyhit lwtfllalgh flselfvfgt aaptvgvlap lmvasfsilg
      121 mlvglrylea epvsrqkkrn
//
LOCUS       NP_598838                983 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein 26 isoform 4 [Mus musculus].
ACCESSION   NP_598838
VERSION     NP_598838.3
DBSOURCE    REFSEQ: accession NM_134077.5
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Kogo,H., Kowa-Sugiyama,H., Yamada,K., Bolor,H., Tsutsumi,M.,
            Ohye,T., Inagaki,H., Taniguchi,M., Toda,T. and Kurahashi,H.
  TITLE     Screening of genes involved in chromosome segregation during
            meiosis I: toward the identification of genes responsible for
            infertility in humans
  JOURNAL   J Hum Genet 55 (5), 293-299 (2010)
   PUBMED   20339383
REFERENCE   4  (residues 1 to 983)
  AUTHORS   Guo,G., Huss,M., Tong,G.Q., Wang,C., Li Sun,L., Clarke,N.D. and
            Robson,P.
  TITLE     Resolution of cell fate decisions revealed by single-cell gene
            expression analysis from zygote to blastocyst
  JOURNAL   Dev Cell 18 (4), 675-685 (2010)
   PUBMED   20412781
REFERENCE   5  (residues 1 to 983)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   6  (residues 1 to 983)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 983)
  AUTHORS   Peterson,K.A., King,B.L., Hagge-Greenberg,A., Roix,J.J., Bult,C.J.
            and O'Brien,T.P.
  TITLE     Functional and comparative genomic analysis of the piebald deletion
            region of mouse chromosome 14
  JOURNAL   Genomics 80 (2), 172-184 (2002)
   PUBMED   12160731
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113125.8 and AC146601.3.
            
            On Jan 20, 2007 this sequence version replaced NP_598838.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC049360.1, SRR17784644.1112742.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 55.36 cM"
     Protein         1..983
                     /product="RNA-binding protein 26 isoform 4"
                     /note="RNA-binding protein 26; cutaneous T-cell lymphoma
                     tumor antigen se70-2; protein expressed in male leptotene
                     and zygotene spermatocytes 393"
                     /calculated_mol_wt=110883
     Region          11..76
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <294..314
                     /region_name="ZnF_C3H1"
                     /note="zinc finger; smart00356"
                     /db_xref="CDD:214632"
     Region          531..606
                     /region_name="RRM1_RBM26"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     RNA-binding protein 26 (RBM26); cd12516"
                     /db_xref="CDD:409938"
     Region          <654..>808
                     /region_name="HEC1"
                     /note="Chromosome segregation protein NDC80, interacts
                     with SMC proteins [Cell cycle control, cell division,
                     chromosome partitioning]; COG5185"
                     /db_xref="CDD:444066"
     Region          862..933
                     /region_name="RRM2_RBM26_like"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     RNA-binding protein 26 (RBM26) and similar proteins;
                     cd12258"
                     /db_xref="CDD:409703"
     CDS             1..983
                     /gene="Rbm26"
                     /gene_synonym="1700009P03Rik; C230097K14Rik; MLZ-393;
                     Pro1777; Se70-2"
                     /coded_by="NM_134077.5:463..3414"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS37003.1"
                     /db_xref="GeneID:74213"
                     /db_xref="MGI:MGI:1921463"
ORIGIN      
        1 mvskmiienf ealkswlskt lepicdadps alakyvlalv kkdksekelk alcidqldvf
       61 lqketqifve klfdavntks ylpppeqpss gslkvdflqh qekdikkeel tkeeerekkf
      121 srrlnhsppq sssryrdnrs rderkkddrs rkrdydrnpp rrdsyrdryn rrrgrsrsys
      181 rsrsrswske rlrdrdrdrs rtrsrsrtrs rerdlvkpky dldrtdplen nytpvssvsn
      241 issghypvpt lsstitviap thhgnnttes wsefhedqvd hnsyvrppmp kkrcrdydek
      301 gfcmrgdmcp fdhgsdpvvv edvnlpgmlp fpaqppvveg ppppglpppp piltpppvnl
      361 rppvpppgpl ppslppvtgp ppplpplqps gmdappnsat ssvptvvttg ihhqpppapp
      421 slftadtydt dgynpeapsi tntsrpmyrh rvhaqrpnli gltsgdmdlp prekppnkss
      481 mrivvdsesr krtigsgepg vstkktwfdk pnfnrtnspg fqkkvqfgne ntklelrkvp
      541 pelnniskln ehfsrfgtlv nlqvayngdp egaliqfaty eeakkaisst eavlnnrfik
      601 vywhregttq qlqttspkvi qplvqqpilp vvkqsvkerl gpvpsattep aeaqsatsel
      661 pqvlststgl tktvynpaal kaaqktlsvs tpavdnneaq kkkqealklq qdvrkrkqei
      721 lekhietqkm liskleknkt mksedkaeim ktleiltkni tklkdevkst spgrclpksi
      781 ktktqmqkel ldteldlykk mqageevtel rrkytelqle aakrgilssg rgrgihtrgr
      841 gtahgrgrgr grgrgvpgha vvdhrprale isaftesdre dllphfaqyg eiedcqidda
      901 slhaiitfkt raeaeaaaih garfkgqdlk lawnkpianm savdteeaep deeefqeesl
      961 vddsllqddd eeeednesrs wrr
//
LOCUS       NP_003770                393 aa            linear   PRI 27-APR-2025
DEFINITION  beta-1,4-galactosyltransferase 3 [Homo sapiens].
ACCESSION   NP_003770
VERSION     NP_003770.1
DBSOURCE    REFSEQ: accession NM_003779.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Bi,C., Shan,J., Li,M., Zhang,Q., Li,C., Tong,J. and Huang,Q.
  TITLE     Long noncoding RNA differentiation antagonizing nonprotein coding
            RNA promotes the proliferation, invasion and migration of
            neuroblastoma cells via targeting beta-1, 4-galactosyltransferase
            III by sponging miR-338-3p
  JOURNAL   Neuroreport 32 (12), 965-974 (2021)
   PUBMED   34050113
  REMARK    GeneRIF: Long noncoding RNA differentiation antagonizing nonprotein
            coding RNA promotes the proliferation, invasion and migration of
            neuroblastoma cells via targeting beta-1, 4-galactosyltransferase
            III by sponging miR-338-3p.
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Wu,T., Li,Y. and Chen,B.
  TITLE     B4GALT3 promotes cell proliferation and invasion in glioblastoma
  JOURNAL   Neurol Res 42 (6), 463-470 (2020)
   PUBMED   32202233
  REMARK    GeneRIF: B4GALT3 promotes cell proliferation and invasion in
            glioblastoma.
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Tange,R., Tomatsu,T. and Sato,T.
  TITLE     Transcription of human beta4-galactosyltransferase 3 is regulated
            by differential DNA binding of Sp1/Sp3 in SH-SY5Y human
            neuroblastoma and A549 human lung cancer cell lines
  JOURNAL   Glycobiology 29 (3), 211-221 (2019)
   PUBMED   30561605
  REMARK    GeneRIF: These findings suggest that the transcription of the
            b4GalT3 gene is regulated by differential DNA binding of Sp3 and
            Sp1 in neuroblastoma and lung cancer. The increased expression of
            b4GalT3 in neuroblastoma may be ascribed to the enhanced expression
            of Sp3, which is observed for various cancers.
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Liu,H., Chen,D., Bi,J., Han,J., Yang,M., Dong,W., Lin,T. and
            Huang,J.
  TITLE     Circular RNA circUBXN7 represses cell growth and invasion by
            sponging miR-1247-3p to enhance B4GALT3 expression in bladder
            cancer
  JOURNAL   Aging (Albany NY) 10 (10), 2606-2623 (2018)
   PUBMED   30312173
  REMARK    GeneRIF: In bladder tumor cells circUBXN7 serves as a competitive
            endogenous RNA of miR-1247-3p to elevate B4GALT3 expression,
            consequently inhibiting cell viability and invasion.
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Fang,T., Lv,H., Lv,G., Li,T., Wang,C., Han,Q., Yu,L., Su,B.,
            Guo,L., Huang,S., Cao,D., Tang,L., Tang,S., Wu,M., Yang,W. and
            Wang,H.
  TITLE     Tumor-derived exosomal miR-1247-3p induces cancer-associated
            fibroblast activation to foster lung metastasis of liver cancer
  JOURNAL   Nat Commun 9 (1), 191 (2018)
   PUBMED   29335551
  REMARK    GeneRIF: High-metastatic hepatocellular carcinoma cells secrete
            exosomal miR-1247-3p that directly targets B4GALT3, leading to
            activation of beta1-integrin-NF-kappaappaB metastatic signaling in
            fibroblasts resulting in lung cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Davidsson,J., Andersson,A., Paulsson,K., Heidenblad,M.,
            Isaksson,M., Borg,A., Heldrup,J., Behrendtz,M., Panagopoulos,I.,
            Fioretos,T. and Johansson,B.
  TITLE     Tiling resolution array comparative genomic hybridization,
            expression and methylation analyses of dup(1q) in Burkitt lymphomas
            and pediatric high hyperdiploid acute lymphoblastic leukemias
            reveal clustered near-centromeric breakpoints and overexpression of
            genes in 1q22-32.3
  JOURNAL   Hum Mol Genet 16 (18), 2215-2225 (2007)
   PUBMED   17613536
  REMARK    GeneRIF: B4GALT3, DAP3, RGS16, TMEM183A and UCK2--were
            significantly overexpressed in dup(1q)-positive ALLs compared with
            high hyperdiploid ALLs without dup(1q).
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Guo,S., Sato,T., Shirane,K. and Furukawa,K.
  TITLE     Galactosylation of N-linked oligosaccharides by human
            beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed
            in Sf-9 cells
  JOURNAL   Glycobiology 11 (10), 813-820 (2001)
   PUBMED   11588157
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Amado,M., Almeida,R., Schwientek,T. and Clausen,H.
  TITLE     Identification and characterization of large galactosyltransferase
            gene families: galactosyltransferases for all functions
  JOURNAL   Biochim Biophys Acta 1473 (1), 35-53 (1999)
   PUBMED   10580128
  REMARK    Review article
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Lo,N.W., Shaper,J.H., Pevsner,J. and Shaper,N.L.
  TITLE     The expanding beta 4-galactosyltransferase gene family: messages
            from the databanks
  JOURNAL   Glycobiology 8 (5), 517-526 (1998)
   PUBMED   9597550
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Almeida,R., Amado,M., David,L., Levery,S.B., Holmes,E.H., Merkx,G.,
            van Kessel,A.G., Rygaard,E., Hassan,H., Bennett,E. and Clausen,H.
  TITLE     A family of human beta4-galactosyltransferases. Cloning and
            expression of two novel UDP-galactose:beta-n-acetylglucosamine
            beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3
  JOURNAL   J Biol Chem 272 (51), 31979-31991 (1997)
   PUBMED   9405390
  REMARK    Erratum:[J Biol Chem 1998 Jul 17;273(29):18674]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC339671.1, AK291455.1 and
            BC006099.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is one of seven beta-1,4-galactosyltransferase
            (beta4GalT) genes. They encode type II membrane-bound glycoproteins
            that appear to have exclusive specificity for the donor substrate
            UDP-galactose; all transfer galactose in a beta1,4 linkage to
            similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a
            distinct function in the biosynthesis of different glycoconjugates
            and saccharide structures. As type II membrane proteins, they have
            an N-terminal hydrophobic signal sequence that directs the protein
            to the Golgi apparatus and which then remains uncleaved to function
            as a transmembrane anchor. By sequence similarity, the beta4GalTs
            form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and
            beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. This gene
            encodes an enzyme that may be mainly involved in the synthesis of
            the first N-acetyllactosamine unit of poly-N-acetyllactosamine
            chains. Multiple alternatively spliced transcript variants encoding
            the same protein have been found for this gene. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (2) lacks an internal segment in
            the 5' UTR, and encodes the same protein, as compared to variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.181823.1,
                                           SRR3476690.701043.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319769.10/ ENSP00000320965.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..393
                     /product="beta-1,4-galactosyltransferase 3"
                     /EC_number="2.4.1.90"
                     /EC_number="2.4.1.38"
                     /EC_number="2.4.1.275"
                     /note="beta-N-acetylglucosaminyl-glycolipid
                     beta-1,4-galactosyltransferase 3; b4Gal-T3;
                     beta-1,4-GalTase 3; epididymis secretory sperm binding
                     protein; nal synthase; N-acetyllactosamine synthase;
                     UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3;
                     UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 3; UDP-Gal:betaGlcNAc beta
                     1,4- galactosyltransferase, polypeptide 3;
                     beta-N-acetylglucosaminylglycopeptide
                     beta-1,4-galactosyltransferase; neolactotriaosylceramide
                     beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=43797
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60512.2)"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     Region          122..341
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(130,132,134,169,195..197)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     Site            order(195,197,291)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     Region          339..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60512.2)"
     Site            385
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     CDS             1..393
                     /gene="B4GALT3"
                     /gene_synonym="beta4Gal-T3"
                     /coded_by="NM_003779.4:246..1427"
                     /db_xref="CCDS:CCDS1222.1"
                     /db_xref="GeneID:8703"
                     /db_xref="HGNC:HGNC:926"
                     /db_xref="MIM:604014"
ORIGIN      
        1 mlrrllerpc tlallvgsql avmmylslgg frslsalfgr dqgptfdysh prdvysnlsh
       61 lpgapggppa pqglpycper spllvgpvsv sfspvpslae ivernprvep ggryrpagce
      121 prsrtaiivp hrarehhlrl llyhlhpflq rqqlaygiyv ihqagngtfn rakllnvgvr
      181 ealrdeewdc lflhdvdllp endhnlyvcd prgprhvava mnkfgyslpy pqyfggvsal
      241 tpdqylkmng fpneywgwgg edddiatrvr lagmkisrpp tsvghykmvk hrgdkgneen
      301 phrfdllvrt qnswtqdgmn sltyqllare lgplytnita digtdprgpr apsgpryppg
      361 ssqafrqeml qrrpparpgp lstanhtalr gsh
//
LOCUS       NP_689813                562 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 579 [Homo sapiens].
ACCESSION   NP_689813
VERSION     NP_689813.2
DBSOURCE    REFSEQ: accession NM_152600.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Schlag,K., Steinhilber,D., Karas,M. and Sorg,B.L.
  TITLE     Analysis of proximal ALOX5 promoter binding proteins by
            quantitative proteomics
  JOURNAL   FEBS J 287 (20), 4481-4499 (2020)
   PUBMED   32096311
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Teumer,A., Holtfreter,B., Volker,U., Petersmann,A., Nauck,M.,
            Biffar,R., Volzke,H., Kroemer,H.K., Meisel,P., Homuth,G. and
            Kocher,T.
  TITLE     Genome-wide association study of chronic periodontitis in a general
            German population
  JOURNAL   J Clin Periodontol 40 (11), 977-985 (2013)
   PUBMED   24024966
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 562)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008735.9, CN340494.1, CX781546.1, AK092772.1 and AW003562.1.
            
            On Jul 26, 2006 this sequence version replaced NP_689813.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK092772.1, SRR1163655.402716.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325421.7/ ENSP00000320188.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..562
                     /product="zinc finger protein 579"
                     /calculated_mol_wt=60378
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAF0.2)"
     Region          45..>105
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          46..66
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(51,53,55,57..58,61..62,65,79,81,85..86,89..90,93,
                     107,109,111,113..114,117..118)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          72..94
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          74..94
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            92
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8NAF0.2)"
     Region          102..119
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          139..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAF0.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NAF0.2)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8NAF0.2)"
     Region          232..254
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(237,239,241,243..244,247..248,253,277,279,283..284,
                     287..288,291,305,307,309,311..312,315..316,319)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          272..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..320
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          327..379
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAF0.2)"
     Region          386..406
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(391,393,395,397..398,401..402,405,419,421,425..426,
                     429..430,433,448,450,452,454..455,458..459,462)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          414..434
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          443..463
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          477..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAF0.2)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NAF0.2)"
     CDS             1..562
                     /gene="ZNF579"
                     /coded_by="NM_152600.3:57..1745"
                     /db_xref="CCDS:CCDS12927.1"
                     /db_xref="GeneID:163033"
                     /db_xref="HGNC:HGNC:26646"
ORIGIN      
        1 mdpqppppaq gspphrgrgr grgrgrgrgr grgrggagap raplpcptcg rlfrfpyyls
       61 rhrlshsglr phacplcpka frrpahlsrh lrghgpqppl rcaacprtfp epaqlrrhla
      121 qehaggevel aiervaketa epswgpqdeg seppttaaag ateeeavaaw petwpageps
      181 tlaaptsaae preseseeae agaaelrael alaagrqeek qvllqadwtl lclrcreafa
      241 tkgelkahpc lrpegeqege ggppprpkrh qcsiclkafa rpwslsrhrl vhstdrpfvc
      301 pdcglafrla sylrqhrrvh gplsllaplp aagkkddkas garnsakgpe ggegaecgga
      361 seggegqngg daaparppag eprfwcpecg kgfrrrahlr qhgvthsgar pfqcvrcqre
      421 fkrladlarh aqvhaggpap hpcprcprrf sraysllrhq rchraelera aalqalqaqa
      481 ptsppppppp lkaeqeeegl plplanikee ppspgtppqs ppappvflsa scfdsqdhsa
      541 femeeeevds kahlrglggl as
//
LOCUS       NP_032038                316 aa            linear   ROD 27-APR-2025
DEFINITION  aldose reductase-related protein 2 [Mus musculus].
ACCESSION   NP_032038
VERSION     NP_032038.1
DBSOURCE    REFSEQ: accession NM_008012.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Deng,Q., Yao,Y., Yang,J., Khoshaba,R., Shen,Y., Wang,X. and Cao,D.
  TITLE     AKR1B8 deficiency drives severe DSS-induced acute colitis through
            invasion of luminal bacteria and activation of innate immunity
  JOURNAL   Front Immunol 13, 1042549 (2022)
   PUBMED   36518763
  REMARK    GeneRIF: AKR1B8 deficiency drives severe DSS-induced acute colitis
            through invasion of luminal bacteria and activation of innate
            immunity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Rajak,S., Gupta,P., Anjum,B., Raza,S., Tewari,A., Ghosh,S.,
            Tripathi,M., Singh,B.K. and Sinha,R.A.
  TITLE     Role of AKR1B10 and AKR1B8 in the pathogenesis of non-alcoholic
            steatohepatitis (NASH) in mouse
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1868 (4), 166319 (2022)
   PUBMED   34954342
  REMARK    GeneRIF: Role of AKR1B10 and AKR1B8 in the pathogenesis of
            non-alcoholic steatohepatitis (NASH) in mouse.
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Cajigas,I., Chakraborty,A., Lynam,M., Swyter,K.R., Bastidas,M.,
            Collens,L., Luo,H., Ay,F. and Kohtz,J.D.
  TITLE     Sox2-Evf2 lncRNA-mediated mechanisms of chromosome topological
            control in developing forebrain
  JOURNAL   Development 148 (6) (2021)
   PUBMED   33593819
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Wang,X., Khoshaba,R., Shen,Y., Cao,Y., Lin,M., Zhu,Y., Cao,Z.,
            Liao,D.F. and Cao,D.
  TITLE     Impaired Barrier Function and Immunity in the Colon of Aldo-Keto
            Reductase 1B8 Deficient Mice
  JOURNAL   Front Cell Dev Biol 9, 632805 (2021)
   PUBMED   33644071
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Ho,H.T., Jenkins,N.A., Copeland,N.G., Gilbert,D.J., Winkles,J.A.,
            Louie,H.W., Lee,F.K., Chung,S.S. and Chung,S.K.
  TITLE     Comparisons of genomic structures and chromosomal locations of the
            mouse aldose reductase and aldose reductase-like genes
  JOURNAL   Eur J Biochem 259 (3), 726-730 (1999)
   PUBMED   10092857
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Lau,E.T., Cao,D., Lin,C., Chung,S.K. and Chung,S.S.
  TITLE     Tissue-specific expression of two aldose reductase-like genes in
            mice: abundant expression of mouse vas deferens protein and
            fibroblast growth factor-regulated protein in the adrenal gland
  JOURNAL   Biochem J 312 (Pt 2) (Pt 2), 609-615 (1995)
   PUBMED   8526877
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Fabre,S., Darne,C., Veyssiere,G. and Jean,C.
  TITLE     Characterization of the promoter of the gene for a mouse vas
            deferens protein related to the aldo-keto reductase superfamily:
            effect of steroid hormones and phorbol esters
  JOURNAL   J Steroid Biochem Mol Biol 55 (3-4), 315-325 (1995)
   PUBMED   8541228
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Wilson,D.K., Nakano,T., Petrash,J.M. and Quiocho,F.A.
  TITLE     1.7 A structure of FR-1, a fibroblast growth factor-induced member
            of the aldo-keto reductase family, complexed with coenzyme and
            inhibitor
  JOURNAL   Biochemistry 34 (44), 14323-14330 (1995)
   PUBMED   7578036
REFERENCE   10 (residues 1 to 316)
  AUTHORS   Donohue,P.J., Alberts,G.F., Hampton,B.S. and Winkles,J.A.
  TITLE     A delayed-early gene activated by fibroblast growth factor-1
            encodes a protein related to aldose reductase
  JOURNAL   J Biol Chem 269 (11), 8604-8609 (1994)
   PUBMED   7510692
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC115767.14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U04204.1, BC005789.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 14.91 cM"
     Protein         1..316
                     /product="aldose reductase-related protein 2"
                     /EC_number="1.1.1.21"
                     /note="AR; protein FR-1; aldehyde reductase; fibroblast
                     growth factor-regulated protein"
                     /calculated_mol_wt=35989
     Region          10..316
                     /region_name="AKR_AKR1B1-19"
                     /note="AKR1B family of aldo-keto reductase (AKR); cd19107"
                     /db_xref="CDD:381333"
     Site            order(19..22,44,48..49,78,80,111..112,114,116,123,
                     160..161,184,210..217,220,229,246,261..266,269,272..273,
                     299..301,304,310..311)
                     /site_type="active"
                     /db_xref="CDD:381333"
     Site            order(44,49,78,111)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381333"
     Site            78
                     /site_type="other"
                     /note="Lowers pKa of active site Tyr.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P45377.2)"
     CDS             1..316
                     /gene="Akr1b8"
                     /gene_synonym="Fgfrp; Fgrp; FR-1"
                     /coded_by="NM_008012.2:86..1036"
                     /db_xref="CCDS:CCDS19991.1"
                     /db_xref="GeneID:14187"
                     /db_xref="MGI:MGI:107673"
ORIGIN      
        1 matfvelstk akmpivglgt wksppnqvke avkaaidagy rhidcayayc nenevgeaiq
       61 ekikekavqr edlfivsklw ptcfekkllk eafqktltdl kldyldlyli hwpqglqpgk
      121 elfpkddqgr iltskttfle awegmeelvd qglvkalgvs nfnhfqierl lnkpglkhkp
      181 vtnqvechpy ltqekliqyc hskgisvtay splgspdrps akpedpslle dpkikeiaak
      241 hektsaqvli rfhiqrnvvv ipksvtpsri qeniqvfdfq lsdeematil sfnrnwracl
      301 lpetvnmeey pydaey
//
LOCUS       NP_116176                797 aa            linear   PRI 27-APR-2025
DEFINITION  adhesion G-protein coupled receptor G7 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_116176
VERSION     NP_116176.2
DBSOURCE    REFSEQ: accession NM_032787.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Zackova,S., Pavova,M., Trylcova,J., Chalupova,J., Priss,A.,
            Luksan,O. and Weber,J.
  TITLE     Upregulation of mRNA Expression of ADGRD1/GPR133 and ADGRG7/GPR128
            in SARS-CoV-2-Infected Lung Adenocarcinoma Calu-3 Cells
  JOURNAL   Cells 13 (10), 791 (2024)
   PUBMED   38786015
  REMARK    GeneRIF: Upregulation of mRNA Expression of ADGRD1/GPR133 and
            ADGRG7/GPR128 in SARS-CoV-2-Infected Lung Adenocarcinoma Calu-3
            Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Hamann,J., Aust,G., Arac,D., Engel,F.B., Formstone,C.,
            Fredriksson,R., Hall,R.A., Harty,B.L., Kirchhoff,C., Knapp,B.,
            Krishnan,A., Liebscher,I., Lin,H.H., Martinelli,D.C., Monk,K.R.,
            Peeters,M.C., Piao,X., Promel,S., Schoneberg,T., Schwartz,T.W.,
            Singer,K., Stacey,M., Ushkaryov,Y.A., Vallon,M., Wolfrum,U.,
            Wright,M.W., Xu,L., Langenhan,T. and Schioth,H.B.
  TITLE     International Union of Basic and Clinical Pharmacology. XCIV.
            Adhesion G protein-coupled receptors
  JOURNAL   Pharmacol Rev 67 (2), 338-367 (2015)
   PUBMED   25713288
  REMARK    Review article
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Chase,A., Ernst,T., Fiebig,A., Collins,A., Grand,F., Erben,P.,
            Reiter,A., Schreiber,S. and Cross,N.C.
  TITLE     TFG, a target of chromosome translocations in lymphoma and soft
            tissue tumors, fuses to GPR128 in healthy individuals
  JOURNAL   Haematologica 95 (1), 20-26 (2010)
   PUBMED   19797732
  REMARK    GeneRIF: An expressed in-frame TRK-fused gene-G-protein-coupled
            receptor GPR128 is identified in healthy individuals and in
            patients with myeloproliferative neoplasms.
REFERENCE   6  (residues 1 to 797)
  AUTHORS   Bjarnadottir,T.K., Fredriksson,R., Hoglund,P.J., Gloriam,D.E.,
            Lagerstrom,M.C. and Schioth,H.B.
  TITLE     The human and mouse repertoire of the adhesion family of
            G-protein-coupled receptors
  JOURNAL   Genomics 84 (1), 23-33 (2004)
   PUBMED   15203201
REFERENCE   7  (residues 1 to 797)
  AUTHORS   Fredriksson,R., Gloriam,D.E., Hoglund,P.J., Lagerstrom,M.C. and
            Schioth,H.B.
  TITLE     There exist at least 30 human G-protein-coupled receptors with long
            Ser/Thr-rich N-termini
  JOURNAL   Biochem Biophys Res Commun 301 (3), 725-734 (2003)
   PUBMED   12565841
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK027360.1, AC069223.15 and AK172769.1.
            
            On Jun 4, 2009 this sequence version replaced NP_116176.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027360.1, BC113451.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000273352.8/ ENSP00000273352.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q12.2"
     Protein         1..797
                     /product="adhesion G-protein coupled receptor G7 isoform 1
                     precursor"
                     /note="G-protein coupled receptor 128"
                     /calculated_mol_wt=86198
     sig_peptide     1..26
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
                     /calculated_mol_wt=2729
     mat_peptide     27..797
                     /product="Adhesion G-protein coupled receptor G7.
                     /id=PRO_0000012903"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K78.2)"
                     /calculated_mol_wt=86198
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
     Site            159
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
     Site            261
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
     Site            312
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
     Site            316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
     Region          381..421
                     /region_name="GPS"
                     /note="GPCR proteolysis site, GPS, motif; pfam01825"
                     /db_xref="CDD:460350"
     Region          383..428
                     /region_name="GPS.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K78.2)"
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
     Site            413
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K78.2)"
     Region          431..737
                     /region_name="7tmB2_GPR128"
                     /note="orphan adhesion receptor GPR128, member of the
                     class B2 family of seven-transmembrane G protein-coupled
                     receptors; cd15257"
                     /db_xref="CDD:320385"
     Region          433..458
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320385"
     Site            order(438,442,485,488..489,492,527,534,624..625,627,629,
                     684,687,702,706)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320385"
     Site            439..459
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K78.2)"
     Region          468..490
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320385"
     Site            469..489
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K78.2)"
     Region          527..554
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320385"
     Site            529..549
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K78.2)"
     Site            566..586
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K78.2)"
     Region          567..587
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320385"
     Region          621..651
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320385"
     Site            624..644
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K78.2)"
     Region          665..692
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320385"
     Site            670..690
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K78.2)"
     Region          699..724
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320385"
     Site            699..719
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K78.2)"
     CDS             1..797
                     /gene="ADGRG7"
                     /gene_synonym="GPR128"
                     /coded_by="NM_032787.3:257..2650"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2938.1"
                     /db_xref="GeneID:84873"
                     /db_xref="HGNC:HGNC:19241"
                     /db_xref="MIM:612307"
ORIGIN      
        1 mascrawnlr vlvavvcgll tgiilglgiw riviriqrgk stsssstpte fcrnggtwen
       61 grcicteewk glrctianfc enstymgftf aripvgrygp slqtcgkdtp nagnpmavrl
      121 cslslygeie lqkvtigncn enletlekqv kdvtaplnni ssevqiltsd ankltaenit
      181 satrvvgqif ntsrnaspea kkvaivtvsq lldasedafq rvaatandda lttlieqmet
      241 yslslgnqsv vepniaiqsa nfssenavgp snvrfsvqkg assslvssst fihtnvdgln
      301 pdaqtelqvl lnmtknytkt cgfvvyqndk lfqsktftak sdfsqkiiss ktdeneqdqs
      361 asvdmvfspk ynqkefqlys yacvywnlsa kdwdtygcqk dkgtdgflrc rcnhttnfav
      421 lmtfkkdyqy pksldilsnv gcalsvtgla ltvifqivtr kvrktsvtwv lvnlcismli
      481 fnllfvfgie nsnknlqtsd gdinnidfdn ndiprtdtin ipnpmctaia allhyfllvt
      541 ftwnalsaaq lyyllirtmk plprhfilfi sligwgvpai vvaitvgviy sqngnnpqwe
      601 ldyrqekicw laipepngvi kspllwsfiv pvtiilisnv vmfitisikv lwknnqnlts
      661 tkkvssmkki vstlsvavvf gitwilaylm lvnddsiriv fsyifclfnt tqglqifily
      721 tvrtkvfqse askvlmllss igrrkslpsv trprlrvkmy nflrslptlh erfrlletsp
      781 steeitlses dnakesi
//
LOCUS       NP_001351637            1196 aa            linear   PRI 27-APR-2025
DEFINITION  uncharacterized protein SPEM3 isoform 1 [Homo sapiens].
ACCESSION   NP_001351637 XP_011522098 XP_024308361
VERSION     NP_001351637.1
DBSOURCE    REFSEQ: accession NM_001364708.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113189.11 and HY033016.1.
            
            On or before Jun 30, 2018 this sequence version replaced
            XP_024308361.1, XP_011522098.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000636696.4/ ENSP00000490274.1
            RefSeq Select criteria    :: based on manual assertion, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..1196
                     /product="uncharacterized protein SPEM3 isoform 1"
                     /calculated_mol_wt=128519
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUW6.1)"
     Region          150..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUW6.1)"
     Region          <217..>687
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          <255..438
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          367..402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUW6.1)"
     Region          669..762
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUW6.1)"
     Region          775..806
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUW6.1)"
     Region          826..877
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUW6.1)"
     Region          960..1009
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUW6.1)"
     Region          1168..1196
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUW6.1)"
     CDS             1..1196
                     /gene="SPEM3"
                     /coded_by="NM_001364708.1:47..3637"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS92248.1"
                     /db_xref="GeneID:107983988"
                     /db_xref="HGNC:HGNC:53651"
ORIGIN      
        1 mgerayhgaq vcsgtnprkc qdlgdsilll lgsfillnvw invvtllwkh lksslrilfr
       61 hffpkdkqps gshpicicss vdpknlcskv ssrvhprpgf llrrvnhlds wipdtndekv
      121 sacccvppkc ghagvpresa rglykagmmg ggeapqvtas kaqasllsrp etssqfpkms
      181 kldtgpchlp qesktktpdc apaeapaqaq vhspthtpvc tpthpwtrst dhtavhtpah
      241 swthskartp egthsqaqdt saqaqahtsa ptpaqtpahi qahtpaptpa kasahtkaht
      301 saqaqthspp htpeythsqa hspehtsahs paqapmpvpa hpqahapeyt sahapayipd
      361 hshlvrssvp vptsapappg tlapattpvl aptpapvpas apspapalvm altttpvpdp
      421 vpattpapii tpipstppaf shdlstghvv ydarrekqnf fhmsspqnpe ysrkdlatlf
      481 rpqegqdlvs sgiseqtkqc sgdsaklpag silgylelrn mewknsddak dkfpqtktsp
      541 ycsfhpcsse kntdsqapfy pkflaysrdt acaktcfhsa ttaqssvctl pppftlslpl
      601 vpprsfvppq ptnhqrpstl iqtptvlpts kspqsiltsq fpipslfati sqpliqpqcp
      661 echeslgltq dsglqrtpgp skdsrvprnl dlaqnpdlyk npgltqdpgl henpglapnq
      721 glhefpglpq dsylcqnpsp sqdfglhkns gitqdshpqk ntgltqeagi lrspcltqsp
      781 glhkktpftq tsdlqrssgf tqdsgiyrnl epnqetviyk nqdlsqatdh qknlgsskds
      841 gghkntgnvq dpgvcstagl tedsgsqkgp yvpqdsevnk ssgviqesfl hkspglvqts
      901 glpkcsgltq nsgdyknpgl iqdcgghkvk gltqdsnlps ltqatkverr fslpqdvgvy
      961 rssehsqdsn lhkcpginqd pgphkdpalv qdsglpkisg ltqesgpyks sclipdpsly
     1021 knpspalgsd fvqllsllqt pkstlslmks svpekaaqke daqrhvlwar vqlnenscps
     1081 kaqvvsndlq tfsevpvlie lqssswrags qhgayrpvdt vpsgyqnyrq msmpthinwk
     1141 shcpgpgtqa ghvvfdarqr rlavgkdkce alsprrlhqe apsnsgkpsr sgdirm
//
LOCUS       NP_945314               1386 aa            linear   PRI 27-APR-2025
DEFINITION  putative ATP-dependent RNA helicase DHX57 isoform 1 [Homo sapiens].
ACCESSION   NP_945314
VERSION     NP_945314.1
DBSOURCE    REFSEQ: accession NM_198963.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1386)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 1386)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 1386)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 1386)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB211450.1, BC131534.1, AC018693.8 and AF070590.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC131534.1, ERR3218374.640107.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000457308.6/ ENSP00000405111.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.1"
     Protein         1..1386
                     /product="putative ATP-dependent RNA helicase DHX57
                     isoform 1"
                     /EC_number="3.6.4.13"
                     /note="DEAH-box RNA/DNA helicase AAM73547; putative
                     ATP-dependent RNA helicase DHX57; DEAH box protein 57;
                     DEAH (Asp-Glu-Ala-Asp/His) box polypeptide 57; DEAH-box
                     helicase 57"
                     /calculated_mol_wt=155474
     Region          1..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P158.2)"
     Region          120..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P158.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P158.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P158.2)"
     Region          181..218
                     /region_name="UBA_DHX57"
                     /note="UBA domain found in putative ATP-dependent RNA
                     helicase DHX57 and similar proteins; cd14317"
                     /db_xref="CDD:270502"
     Region          242..425
                     /region_name="RWD_DHX57"
                     /note="RWD domain of DEAH box protein 57 (DHX57) and
                     related proteins; cd23825"
                     /db_xref="CDD:467661"
     Region          305..323
                     /region_name="zf_CCCH_4"
                     /note="Zinc finger domain; pfam18345"
                     /db_xref="CDD:465719"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P158.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P158.2)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P158.2)"
     Region          543..>1170
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
     Region          668..671
                     /region_name="DEVH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P158.2)"
     Region          1213..1310
                     /region_name="OB_NTP_bind"
                     /note="Oligonucleotide/oligosaccharide-binding (OB)-fold;
                     pfam07717"
                     /db_xref="CDD:400182"
     CDS             1..1386
                     /gene="DHX57"
                     /gene_synonym="DDX57"
                     /coded_by="NM_198963.3:155..4315"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1800.1"
                     /db_xref="GeneID:90957"
                     /db_xref="HGNC:HGNC:20086"
ORIGIN      
        1 msssvrrkgk pgkgggkgss rggrggrsha skshgsgggg gggggggggn rkassriwdd
       61 gddfcifses rrpsrpsnsn iskgesrpkw kpkakvplqt lhmtsenqek vkallrdlqe
      121 qdadagserg lsgeeeddep dccnderywp agqepslvpd ldpleyagla svepyvpeft
      181 vspfavqkls rygfntercq avlrmcdgdv gaslehlltq cfsetfgerm kiseavnqis
      241 ldecmeqrqe eafalksicg ekfieriqnr vwtigleley ltsrfrkskp kestknvqen
      301 sleickfylk gnckfgskcr fkhevppnqi vgriersvdd shlnaiedas flyeleirfs
      361 kdhkypyqap lvafystnen lplacrlhis eflydkaltf aetsepvvys litlleeese
      421 ivklltnthh kysdppvnfl pvpsrtrinn pachktvipn nsfvsnqipe vekasesees
      481 deddgpapvi venesyvnlk kkiskrydwq aksvhaengk ickqfrmkqa srqfqsilqe
      541 rqslpaweer etilnllrkh qvvvisgmtg cgkttqipqf ilddslngpp ekvaniictq
      601 prrisaisva ervakeraer vgltvgyqir lesvkssatr llycttgvll rrlegdtalq
      661 gvshiivdev herteesdfl llvlkdivsq rpglqvilms atlnaelfsd yfnscpviti
      721 pgrtfpvdqf fledaiavtr yvlqdgspym rsmkqiskek lkarrnrtaf eeveedlrls
      781 lhlqdqdsvk davpdqqldf kqllarykgv sksviktmsi mdfekvnlel ieallewivd
      841 gkhsyppgai lvflpglaei kmlyeqlqsn slfnnrrsnr cvihplhssl sseeqqavfv
      901 kppagvtkii istniaetsi tiddvvyvid sgkmkekryd askgmesled tfvsqanalq
      961 rkgragrvas gvcfhlftsh hynhqllkqq lpeiqrvple qlclrikile mfsahnlqsv
     1021 fsrlieppht dslraskirl rdlgaltpde rltplgyhla slpvdvrigk lmlfgsifrc
     1081 ldpaltiaas lafkspfvsp wdkkeeanqk klefafansd ylallqaykg wqlstkegvr
     1141 asynycrqnf lsgrvlqema slkrqftell sdigfaregl rareiekraq ggdgvldatg
     1201 eeansnaenp klisamlcaa lypnvvqvks pegkfqktst gavrmqpksa elkfvtkndg
     1261 yvhihpssvn yqvrhfdspy llyhekikts rvfirdcsmv svyplvlfgg gqvnvqlqrg
     1321 efvvslddgw irfvaashqv aelvkelrce ldqllqdkik npsidlctcp rgsriistiv
     1381 klvttq
//
LOCUS       NP_808565               1034 aa            linear   ROD 27-APR-2025
DEFINITION  N-acetyl-beta-glucosaminyl-glycoprotein
            4-beta-N-acetylgalactosaminyltransferase 1 [Mus musculus].
ACCESSION   NP_808565 XP_355977
VERSION     NP_808565.2
DBSOURCE    REFSEQ: accession NM_177897.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Rutledge,E.A., Benazet,J.D. and McMahon,A.P.
  TITLE     Cellular heterogeneity in the ureteric progenitor niche and
            distinct profiles of branching morphogenesis in organ development
  JOURNAL   Development 144 (17), 3177-3188 (2017)
   PUBMED   28705898
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Fiete,D., Beranek,M. and Baenziger,J.U.
  TITLE     Peptide-specific transfer of N-acetylgalactosamine to O-linked
            glycans by the glycosyltransferases beta1,4-N-acetylgalactosaminyl
            transferase 3 (beta4GalNAc-T3) and beta4GalNAc-T4
  JOURNAL   J Biol Chem 287 (34), 29204-29212 (2012)
   PUBMED   22722940
  REMARK    GeneRIF: Peptide-specific transfer of N-acetylgalactosamine to
            O-linked glycans by the glycosyltransferases
            beta1,4-N-acetylgalactosaminyl transferase 3 (beta4GalNAc-T3) and
            beta4GalNAc-T4.
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Fiete,D., Beranek,M. and Baenziger,J.U.
  TITLE     Molecular basis for protein-specific transfer of
            N-acetylgalactosamine to N-linked glycans by the
            glycosyltransferases beta1,4-N-acetylgalactosaminyl transferase 3
            (beta4GalNAc-T3) and beta4GalNAc-T4
  JOURNAL   J Biol Chem 287 (34), 29194-29203 (2012)
   PUBMED   22722937
  REMARK    GeneRIF: Molecular basis for protein-specific transfer of
            N-acetylgalactosamine to N-linked glycans by the
            glycosyltransferases beta1,4-N-acetylgalactosaminyl transferase 3
            (beta4GalNAc-T3) and beta4GalNAc-T4.
REFERENCE   4  (residues 1 to 1034)
  AUTHORS   Gotoh,M., Sato,T., Kiyohara,K., Kameyama,A., Kikuchi,N., Kwon,Y.D.,
            Ishizuka,Y., Iwai,T., Nakanishi,H. and Narimatsu,H.
  TITLE     Molecular cloning and characterization of
            beta1,4-N-acetylgalactosaminyltransferases IV synthesizing
            N,N'-diacetyllactosediamine
  JOURNAL   FEBS Lett 562 (1-3), 134-140 (2004)
   PUBMED   15044014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC109272.20.
            
            On or before Feb 4, 2005 this sequence version replaced
            XP_355977.2, NP_808565.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB114827.1, SRR11927937.3511107.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 86.32 cM"
     Protein         1..1034
                     /product="N-acetyl-beta-glucosaminyl-glycoprotein
                     4-beta-N-acetylgalactosaminyltransferase 1"
                     /EC_number="2.4.1.244"
                     /note="beta
                     1,4-N-acetylgalactosaminyltransferase-transferase 4;
                     beta4GalNAc-T4; beta-1,4-N-acetylgalactosaminyltransferase
                     IV; beta1,4-N-acetylgalactosaminyltransferase IV"
                     /calculated_mol_wt=117243
     Site            13..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q766D5.1)"
     Region          51..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q766D5.1)"
     Site            106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q766D5.1)"
     Region          133..278
                     /region_name="PA14"
                     /note="PA14 domain; cl08459"
                     /db_xref="CDD:471833"
     Region          450..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q766D5.1)"
     Region          <490..606
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     Region          556..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q766D5.1)"
     Site            611
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q766D5.1)"
     Region          626..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q766D5.1)"
     Region          <706..1015
                     /region_name="CHGN"
                     /note="Chondroitin N-acetylgalactosaminyltransferase;
                     pfam05679"
                     /db_xref="CDD:461712"
     Region          782..801
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q766D5.1)"
     CDS             1..1034
                     /gene="B4galnt4"
                     /gene_synonym="beta4GalNAcT4; Gm1095; NGalNAc-T1"
                     /coded_by="NM_177897.4:297..3401"
                     /db_xref="CCDS:CCDS21998.1"
                     /db_xref="GeneID:330671"
                     /db_xref="MGI:MGI:2652891"
ORIGIN      
        1 mpwfpvkkvr kqmkllllll lltcaawlty vhrslvrpgr alrqrlgygr dgekltgvtd
       61 srgvrvpsst qrsedssesh eeeqapegrg pnmlfpggpr kppplnlthq tppwreefkg
      121 qvnlhvfedw cggavghlrr nlhfplfpht rttvtklavs pkwknyglri fgfihpardg
      181 diqfsvasdd nsefwlslde spaaaqlvaf vgktgsewta pgeftkfssq vskprrlmas
      241 rryyfellhk qddkgsdhve vgwraflpgl kfeiidsahi slytdesslk mdhvahvpqs
      301 pashiggfpp qgepsadmlh pdprdtfflt prmeplslen vlepcayapt yilkdfpiar
      361 yqglqfvyls fiypndhtrl thmetdnkcf yresplyler fgfykymkmd keegeedeee
      421 evqrraflfl npddfldeed eqdlldslep tdasvqqshr tptpaastgt tasptpptts
      481 pldeqtlrhs ralnwaprpl plflgrappp rtvekspskv yvtrvrpgqr aspralrdsp
      541 wppfpgvflr pkplprvqlr vpphpprtqg yrtsgpkvte lkppvraqts qggregqlhg
      601 qglmvptvdl nssvetqpvt sflslsqvsr pqlpgegeeg eedgapgdea tsedseeeee
      661 paagrplgrw redainwqrt fsvgamdfel lrsdwndlrc nvsgnlqlpe aeavdvvaqy
      721 merlnakhgg rfsllrivnv ekrrdsargs rfllelelqe rggsrqrlse yvflrlpgar
      781 vgdedgespe pppaasihpd srpelcrplh lawrqdvmvh fivpvknqar wvvqfladmt
      841 alhvhtgdsy fniilvdfes edmdveralr aaqlpryqyl krtgnfersa glqtgvdave
      901 dpssivflcd lhihfppnil dsirkhcveg klafapvvmr lgcgsspwdp hgywevngfg
      961 lfgiyksdfd rvggmnteef rdqwggedwe lldrvlqagl everlrlrhf yhhyhskrgm
     1021 watrsrkgar aqrs
//
LOCUS       NP_001346983             102 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim10 B
            isoform c [Mus musculus].
ACCESSION   NP_001346983
VERSION     NP_001346983.1
DBSOURCE    REFSEQ: accession NM_001360054.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Kitamura,H., Nakagawa,T., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of FLJ
            genes: the complete nucleotide sequences of 110 mouse
            FLJ-homologous cDnas identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (2), 127-135 (2004)
   PUBMED   15449545
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Bauer,M.F., Rothbauer,U., Muhlenbein,N., Smith,R.J., Gerbitz,K.,
            Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     The mitochondrial TIM22 preprotein translocase is highly conserved
            throughout the eukaryotic kingdom
  JOURNAL   FEBS Lett 464 (1-2), 41-47 (1999)
   PUBMED   10611480
REFERENCE   6  (residues 1 to 102)
  AUTHORS   Jin,H., Kendall,E., Freeman,T.C., Roberts,R.G. and Vetrie,D.L.
  TITLE     The human family of Deafness/Dystonia peptide (DDP) related
            mitochondrial import proteins
  JOURNAL   Genomics 61 (3), 259-267 (1999)
   PUBMED   10552927
REFERENCE   7  (residues 1 to 102)
  AUTHORS   Hadjiargyrou,M., Halsey,M.F., Ahrens,W., Rightmire,E.P.,
            McLeod,K.J. and Rubin,C.T.
  TITLE     Cloning of a novel cDNA expressed during the early stages of
            fracture healing
  JOURNAL   Biochem Biophys Res Commun 249 (3), 879-884 (1998)
   PUBMED   9731230
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125227.6 and AV583975.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV583975.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 55.93 cM"
     Protein         1..102
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim10 B isoform c"
                     /note="small zinc finger-like protein; fractured callus 1;
                     mitochondrial import inner membrane translocase subunit
                     Tim9 B; Fracture Callus 1; fractured callus expressed
                     transcript 1; mitochondrial import inner membrane
                     translocase subunit Tim10 B"
                     /calculated_mol_wt=11470
     CDS             1..102
                     /gene="Timm10b"
                     /gene_synonym="Fxc1; Tim10b; Tim9b"
                     /coded_by="NM_001360054.1:149..457"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS90304.1"
                     /db_xref="GeneID:14356"
                     /db_xref="MGI:MGI:1315196"
ORIGIN      
        1 meqqqqqlrn rcvpslhhra ldaeevetvr pactavlgns silttaswpl tctscppwss
       61 aasrttrlpr prqvflqnrp etrhqaasrp wplerscqke ll
//
LOCUS       NP_001158177             546 aa            linear   ROD 27-APR-2025
DEFINITION  APC membrane recruitment protein 2 isoform 2 [Mus musculus].
ACCESSION   NP_001158177
VERSION     NP_001158177.2
DBSOURCE    REFSEQ: accession NM_001164705.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Pfister,A.S., Hadjihannas,M.V., Rohrig,W., Schambony,A. and
            Behrens,J.
  TITLE     Amer2 protein interacts with EB1 protein and adenomatous polyposis
            coli (APC) and controls microtubule stability and cell migration
  JOURNAL   J Biol Chem 287 (42), 35333-35340 (2012)
   PUBMED   22898821
  REMARK    GeneRIF: the Amer2-EB1-APC complex regulates cell migration by
            altering microtubule stability.
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Comai,G., Boutet,A., Neirijnck,Y. and Schedl,A.
  TITLE     Expression patterns of the Wtx/Amer gene family during mouse
            embryonic development
  JOURNAL   Dev Dyn 239 (6), 1867-1878 (2010)
   PUBMED   20503382
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC166113.3.
            
            On Feb 15, 2019 this sequence version replaced NP_001158177.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC056350.1, AK011185.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 31.62 cM"
     Protein         1..546
                     /product="APC membrane recruitment protein 2 isoform 2"
                     /note="protein FAM123A; APC membrane recruitment protein
                     2; family with sequence similarity 123, member A"
                     /calculated_mol_wt=57223
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Region          94..465
                     /region_name="WTX"
                     /note="WTX protein; pfam09422"
                     /db_xref="CDD:462794"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     CDS             1..546
                     /gene="Amer2"
                     /gene_synonym="2600011E07Rik; Fam123a"
                     /coded_by="NM_001164705.2:556..2196"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS88682.1"
                     /db_xref="GeneID:72125"
                     /db_xref="MGI:MGI:1919375"
ORIGIN      
        1 metgrsrggg aavserggga ragvcgrqeq agalaadmds hcecaaetpa aeppsgkink
       61 aafklfkkrk sggtmpsifg vknkgdgkss gptgmvrsrt hdglaevlvl egskkeeppg
      121 gsdhsgarpi pgppkpsgpg lgslasssva kshsffsllk kngrsetgkg dhaeaskagg
      181 kqkrglkgif ssmrwhrrdk rgkeeeekav raagpgnlvl pgsltaslec vkeeppraar
      241 rpdspgqdas rhaagcgdii adpeeeagps cdkhvpgpgk pvlskknasv vayqgggeem
      301 aspdqvddty lpefwdmlsq tedqgqgtqe gaakaatasd iklapetssd trcgeaakdm
      361 ssvkrrrlhr ipiesqqkee pkhpekehqe gvpnsdegyw dsttpgpeee sisnsssskk
      421 vviprdsdsg dalcdlyvep easpatlpat edppclsrlk pvspgtitcp lrtpgsllkd
      481 skipisikhl snlpsshpvv hqqparsevp rtkipvskvl vrrvsnrgla gttiraaach
      541 dsakkl
//
LOCUS       NP_001346878             266 aa            linear   ROD 27-APR-2025
DEFINITION  sesquipedalian-1 [Mus musculus].
ACCESSION   NP_001346878
VERSION     NP_001346878.1
DBSOURCE    REFSEQ: accession NM_001359949.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Swan,L.E., Tomasini,L., Pirruccello,M., Lunardi,J. and De
            Camilli,P.
  TITLE     Two closely related endocytic proteins that share a common
            OCRL-binding motif with APPL1
  JOURNAL   Proc Natl Acad Sci U S A 107 (8), 3511-3516 (2010)
   PUBMED   20133602
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113302.13.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All three variants encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5286961.27270.1, BF122882.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 62.01 cM"
     Protein         1..266
                     /product="sesquipedalian-1"
                     /note="27 kDa inositol polyphosphate phosphatase
                     interacting protein A; family with sequence similarity
                     109, member A"
                     /calculated_mol_wt=29087
     Region          11..130
                     /region_name="PH_Ses"
                     /note="Sesquipedalian family Pleckstrin homology (PH)
                     domain; cd13288"
                     /db_xref="CDD:270105"
     Region          165..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH49.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N4B1; propagated from
                     UniProtKB/Swiss-Prot (Q8BH49.1)"
     Region          191..203
                     /region_name="F&H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH49.1)"
     CDS             1..266
                     /gene="Pheta1"
                     /gene_synonym="A230106M15Rik; Fam109a; IPIP27A; Ses1"
                     /coded_by="NM_001359949.1:337..1137"
                     /db_xref="CCDS:CCDS19642.1"
                     /db_xref="GeneID:231717"
                     /db_xref="MGI:MGI:2442708"
ORIGIN      
        1 mklnerslaf yatcdapvdn agflykrggr gtgshrrwfv lrgnilfyfe aegsreplgv
       61 illegctvel vdareefafa vrfaggrsrp yvlaadsqaa legwvkalsr asfhylrlvv
      121 releqqlaam regspanalp anpspvltqr pkengwvvws tlpeqpsvap qrppplpprr
      181 rasaangpla sfaqlharyg levqalrdqw rggqaglasl evpwhpgsae tqtqdqpalr
      241 ghsgckvlhv frsvewpvcn pgsqgt
//
LOCUS       NP_001158232             381 aa            linear   PRI 27-APR-2025
DEFINITION  cAMP-dependent protein kinase type I-beta regulatory subunit [Homo
            sapiens].
ACCESSION   NP_001158232
VERSION     NP_001158232.1
DBSOURCE    REFSEQ: accession NM_001164760.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Feng,Z.H., Zheng,L., Yao,T., Tao,S.Y., Wei,X.A., Zheng,Z.Y.,
            Zheng,B.J., Zhang,X.Y., Huang,B., Liu,J.H., Chen,Y.L., Shan,Z.,
            Yuan,P.T., Wang,C.G., Chen,J., Shen,S.Y. and Zhao,F.D.
  TITLE     EIF4A3-induced circular RNA PRKAR1B promotes osteosarcoma
            progression by miR-361-3p-mediated induction of FZD4 expression
  JOURNAL   Cell Death Dis 12 (11), 1025 (2021)
   PUBMED   34716310
  REMARK    GeneRIF: EIF4A3-induced circular RNA PRKAR1B promotes osteosarcoma
            progression by miR-361-3p-mediated induction of FZD4 expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Marbach,F., Stoyanov,G., Erger,F., Stratakis,C.A., Settas,N.,
            London,E., Rosenfeld,J.A., Torti,E., Haldeman-Englert,C.,
            Sklirou,E., Kessler,E., Ceulemans,S., Nelson,S.F.,
            Martinez-Agosto,J.A., Palmer,C.G.S., Signer,R.H., Andrews,M.V.,
            Grange,D.K., Willaert,R., Person,R., Telegrafi,A., Sievers,A.,
            Laugsch,M., Theiss,S., Cheng,Y., Lichtarge,O., Katsonis,P.,
            Stocco,A. and Schaaf,C.P.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     Variants in PRKAR1B cause a neurodevelopmental disorder with autism
            spectrum disorder, apraxia, and insensitivity to pain
  JOURNAL   Genet Med 23 (8), 1465-1473 (2021)
   PUBMED   33833410
  REMARK    GeneRIF: Variants in PRKAR1B cause a neurodevelopmental disorder
            with autism spectrum disorder, apraxia, and insensitivity to pain.
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Drougat,L., Settas,N., Ronchi,C.L., Bathon,K., Calebiro,D.,
            Maria,A.G., Haydar,S., Voutetakis,A., London,E., Faucz,F.R. and
            Stratakis,C.A.
  TITLE     Genomic and sequence variants of protein kinase A regulatory
            subunit type 1beta (PRKAR1B) in patients with adrenocortical
            disease and Cushing syndrome
  JOURNAL   Genet Med 23 (1), 174-182 (2021)
   PUBMED   32895490
  REMARK    GeneRIF: Genomic and sequence variants of protein kinase A
            regulatory subunit type 1beta (PRKAR1B) in patients with
            adrenocortical disease and Cushing syndrome.
            Erratum:[Genet Med. 2021 Jan;23(1):239. doi:
            10.1038/s41436-020-01018-4. PMID: 33082560]
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Solberg,R., Sistonen,P., Traskelin,A.L., Berube,D., Simard,J.,
            Krajci,P., Jahnsen,T. and de la Chapelle,A.
  TITLE     Mapping of the regulatory subunits RI beta and RII beta of
            cAMP-dependent protein kinase genes on human chromosome 7
  JOURNAL   Genomics 14 (1), 63-69 (1992)
   PUBMED   1358799
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Solberg,R., Tasken,K., Keiserud,A. and Jahnsen,T.
  TITLE     Molecular cloning, cDNA structure and tissue-specific expression of
            the human regulatory subunit RI beta of cAMP-dependent protein
            kinases
  JOURNAL   Biochem Biophys Res Commun 176 (1), 166-172 (1991)
   PUBMED   1708242
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Hofmann,B., Nishanian,P., Baldwin,R.L., Insixiengmay,P., Nel,A. and
            Fahey,J.L.
  TITLE     HIV inhibits the early steps of lymphocyte activation, including
            initiation of inositol phospholipid metabolism
  JOURNAL   J Immunol 145 (11), 3699-3705 (1990)
   PUBMED   1978848
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Taylor,S.S., Buechler,J.A. and Yonemoto,W.
  TITLE     cAMP-dependent protein kinase: framework for a diverse family of
            regulatory enzymes
  JOURNAL   Annu Rev Biochem 59, 971-1005 (1990)
   PUBMED   2165385
  REMARK    Review article
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Scambler,P., Oyen,O., Wainwright,B., Farrall,M., Law,H.Y.,
            Estivill,X., Sandberg,M., Williamson,R. and Jahnsen,T.
  TITLE     Exclusion of catalytic and regulatory subunits of cAMP-dependent
            protein kinase as candidate genes for the defect causing cystic
            fibrosis
  JOURNAL   Am J Hum Genet 41 (5), 925-932 (1987)
   PUBMED   3479018
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CT003793.1, BC036828.1 and
            AC147651.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a regulatory subunit
            of cyclic AMP-dependent protein kinase A (PKA), which is involved
            in the signaling pathway of the second messenger cAMP. Two
            regulatory and two catalytic subunits form the PKA holoenzyme,
            disbands after cAMP binding. The holoenzyme is involved in many
            cellular events, including ion transport, metabolism, and
            transcription. Several transcript variants encoding the same
            protein have been found for this gene. [provided by RefSeq, Aug
            2015].
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. All of the variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.449535.1,
                                           SRR1660805.67190.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000537384.6/ ENSP00000440449.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..381
                     /product="cAMP-dependent protein kinase type I-beta
                     regulatory subunit"
                     /EC_number="2.7.11.1"
                     /note="protein kinase, cAMP-dependent, regulatory subunit
                     type I beta; protein kinase, cAMP-dependent, regulatory,
                     type I, beta"
                     /calculated_mol_wt=42942
     Region          2..136
                     /region_name="Dimerization and phosphorylation"
                     /note="propagated from UniProtKB/Swiss-Prot (P31321.4)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P31321.4)"
     Region          11..64
                     /region_name="DD_RIbeta_PKA"
                     /note="dimerization/docking (D/D) domain of the Type I
                     beta Regulatory subunit of cAMP-dependent protein kinase;
                     cd12102"
                     /db_xref="CDD:438523"
     Site            order(15,18..19,28..29,31..32,35..36)
                     /site_type="other"
                     /note="putative AKAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:438523"
     Site            order(17..18,21,25,27,30..31,35,38..39,42..48,50..51,
                     54..55,57..58,61..62)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:438523"
     Region          67..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31321.4)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P31321.4)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31321.4)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P12849; propagated from
                     UniProtKB/Swiss-Prot (P31321.4)"
     Region          96..100
                     /region_name="Pseudophosphorylation motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P31321.4)"
     Site            97
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P12849; propagated from
                     UniProtKB/Swiss-Prot (P31321.4)"
     Region          137..246
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(201..202,211..213)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(233..235,239..241)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          255..370
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(325..326,335..337)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(357..359,363..365)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     CDS             1..381
                     /gene="PRKAR1B"
                     /gene_synonym="MASNS; PRKAR1"
                     /coded_by="NM_001164760.2:95..1240"
                     /db_xref="CCDS:CCDS34579.1"
                     /db_xref="GeneID:5575"
                     /db_xref="HGNC:HGNC:9390"
                     /db_xref="MIM:176911"
ORIGIN      
        1 masppacpse edeslkgcel yvqlhgiqqv lkdcivhlci skperpmkfl rehfekleke
       61 enrqilarqk snsqsdshde evsptppnpv vkarrrrggv saevyteeda vsyvrkvipk
      121 dyktmtalak aisknvlfah lddnersdif damfpvthia getviqqgne gdnfyvvdqg
      181 evdvyvngew vtniseggsf gelaliygtp raatvkaktd lklwgidrds yrrilmgstl
      241 rkrkmyeefl skvsilesle kwerltvada lepvqfedge kivvqgepgd dfyiitegta
      301 svlqrrspne eyvevgrlgp sdyfgeiall lnrpraatvv argplkcvkl drprfervlg
      361 pcseilkrni qrynsfislt v
//
LOCUS       NP_620152                300 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 54 isoform 1 [Homo
            sapiens].
ACCESSION   NP_620152
VERSION     NP_620152.1
DBSOURCE    REFSEQ: accession NM_138797.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Gustafsson,M.O., Mohammad,D.K., Ylosmaki,E., Choi,H., Shrestha,S.,
            Wang,Q., Nore,B.F., Saksela,K. and Smith,C.I.
  TITLE     ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from
            a Human Src-Homology 3 (SH3) domain library
  JOURNAL   PLoS One 12 (4), e0174909 (2017)
   PUBMED   28369144
  REMARK    GeneRIF: the results show that the interaction between BTK and
            ANKRD54 is highly selective, since it was also identified in a
            screen using human SH3-domainome. A novel finding is that BTK not
            only binds to ANKRD54, but stands out as the preferred interactor,
            being highly dominant over all other human SH3-domains.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Gustafsson,M.O., Hussain,A., Mohammad,D.K., Mohamed,A.J.,
            Nguyen,V., Metalnikov,P., Colwill,K., Pawson,T., Smith,C.I. and
            Nore,B.F.
  TITLE     Regulation of nucleocytoplasmic shuttling of Bruton's tyrosine
            kinase (Btk) through a novel SH3-dependent interaction with ankyrin
            repeat domain 54 (ANKRD54)
  JOURNAL   Mol Cell Biol 32 (13), 2440-2453 (2012)
   PUBMED   22527282
  REMARK    GeneRIF: Liar is the first protein identified that specifically
            influences the nucleocytoplasmic shuttling of Btk and Txk and
            belongs to a rare group of known proteins carrying out this
            activity in a Crm1-dependent manner.
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY007929.1, BC066909.1 and BC014641.1.
            
            Transcript Variant: This variant (1) represents the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014641.1, SRR1163658.175952.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215941.9/ ENSP00000215941.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..300
                     /product="ankyrin repeat domain-containing protein 54
                     isoform 1"
                     /note="ankyrin repeat domain-containing protein 54;
                     lyn-interacting ankyrin repeat protein"
                     /calculated_mol_wt=32374
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Region          99..117
                     /region_name="Nuclear localization signal (NLS).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Region          109..138
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Region          <114..>236
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(119..121,123..124,128,131,140,142,144,148..149,
                     152..154,156..157,161,164,173,175,177,181..182,185..187,
                     189..190,194,197,206)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          141..241
                     /region_name="LYN-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Region          142..173
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          175..206
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          208..244
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Region          283..293
                     /region_name="Nuclear export signal (NES).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     CDS             1..300
                     /gene="ANKRD54"
                     /gene_synonym="LIAR"
                     /coded_by="NM_138797.4:97..999"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13959.1"
                     /db_xref="GeneID:129138"
                     /db_xref="HGNC:HGNC:25185"
                     /db_xref="MIM:613383"
ORIGIN      
        1 maaaagdadd eprsghssse gecavapepl tdaeglfsfa dfgsalgggg aglsgrasgg
       61 aqsplrylhv lwqqdaeprd elrckipagr lrraarphrr lgptgkevha lkrlrdsana
      121 ndvetvqqll edgadpcaad dkgrtalhfa scngndqivq llldhgadpn qrdglgntpl
      181 hlaactnhvp vittllrgga rvdaldragr tplhlakskl nilqeghaqc leavrlevkq
      241 iihmlreyle rlgqheqrer lddlctrlqm tstkeqvdev tdllasftsl slqmqsmekr
//
LOCUS       NP_036243                338 aa            linear   PRI 27-APR-2025
DEFINITION  activator of 90 kDa heat shock protein ATPase homolog 1 isoform 1
            [Homo sapiens].
ACCESSION   NP_036243
VERSION     NP_036243.1
DBSOURCE    REFSEQ: accession NM_012111.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Hussein,S.K., Bhat,R., Overduin,M. and LaPointe,P.
  TITLE     Recruitment of Ahsa1 to Hsp90 is regulated by a conserved peptide
            that inhibits ATPase stimulation
  JOURNAL   EMBO Rep 25 (8), 3532-3546 (2024)
   PUBMED   38937628
  REMARK    GeneRIF: Recruitment of Ahsa1 to Hsp90 is regulated by a conserved
            peptide that inhibits ATPase stimulation.
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Tang,J., Hu,H., Zhou,C. and Zhang,N.
  TITLE     Human Aha1's N-terminal extension confers it holdase activity in
            vitro
  JOURNAL   Protein Sci 32 (9), e4735 (2023)
   PUBMED   37486705
  REMARK    GeneRIF: Human Aha1's N-terminal extension confers it holdase
            activity in vitro.
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Biebl,M.M. and Buchner,J.
  TITLE     p23 and Aha1: Distinct Functions Promote Client Maturation
  JOURNAL   Subcell Biochem 101, 159-187 (2023)
   PUBMED   36520307
  REMARK    GeneRIF: p23 and Aha1: Distinct Functions Promote Client
            Maturation.
            Review article
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Li,W. and Liu,J.
  TITLE     The Prognostic and Immunotherapeutic Significance of AHSA1 in
            Pan-Cancer, and Its Relationship With the Proliferation and
            Metastasis of Hepatocellular Carcinoma
  JOURNAL   Front Immunol 13, 845585 (2022)
   PUBMED   35757728
  REMARK    GeneRIF: The Prognostic and Immunotherapeutic Significance of AHSA1
            in Pan-Cancer, and Its Relationship With the Proliferation and
            Metastasis of Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Wang,X., Venable,J., LaPointe,P., Hutt,D.M., Koulov,A.V.,
            Coppinger,J., Gurkan,C., Kellner,W., Matteson,J., Plutner,H.,
            Riordan,J.R., Kelly,J.W., Yates,J.R. 3rd and Balch,W.E.
  TITLE     Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in
            cystic fibrosis
  JOURNAL   Cell 127 (4), 803-815 (2006)
   PUBMED   17110338
  REMARK    GeneRIF: Hsp90 cochaperones modulate Hsp90-dependent stability of
            CFTR protein folding in the endoplasmic reticulum
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Swick,L. and Kapatos,G.
  TITLE     A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein
            interactions
  JOURNAL   J Neurochem 97 (5), 1447-1455 (2006)
   PUBMED   16696853
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Lotz,G.P., Lin,H., Harst,A. and Obermann,W.M.
  TITLE     Aha1 binds to the middle domain of Hsp90, contributes to client
            protein activation, and stimulates the ATPase activity of the
            molecular chaperone
  JOURNAL   J Biol Chem 278 (19), 17228-17235 (2003)
   PUBMED   12604615
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Panaretou,B., Siligardi,G., Meyer,P., Maloney,A., Sullivan,J.K.,
            Singh,S., Millson,S.H., Clarke,P.A., Naaby-Hansen,S., Stein,R.,
            Cramer,R., Mollapour,M., Workman,P., Piper,P.W., Pearl,L.H. and
            Prodromou,C.
  TITLE     Activation of the ATPase activity of hsp90 by the stress-regulated
            cochaperone aha1
  JOURNAL   Mol Cell 10 (6), 1307-1318 (2002)
   PUBMED   12504007
  REMARK    GeneRIF: stimulates the inherent ATPase activity of Hsp90
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Sevier,C.S. and Machamer,C.E.
  TITLE     p38: A novel protein that associates with the vesicular stomatitis
            virus glycoprotein
  JOURNAL   Biochem Biophys Res Commun 287 (2), 574-582 (2001)
   PUBMED   11554768
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000321.2 and AF161440.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ243310.1, SRR1163657.47594.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216479.8/ ENSP00000216479.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..338
                     /product="activator of 90 kDa heat shock protein ATPase
                     homolog 1 isoform 1"
                     /note="activator of 90 kDa heat shock protein ATPase
                     homolog 1; AHA1, activator of heat shock 90kDa protein
                     ATPase homolog 1"
                     /calculated_mol_wt=38143
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95433.1)"
     Region          29..158
                     /region_name="Aha1_N"
                     /note="Activator of Hsp90 ATPase, N-terminal; smart01000"
                     /db_xref="CDD:214964"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O95433.1)"
     Region          208..333
                     /region_name="SRPBCC_Aha1"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of the Hsp90 co-chaperone Aha1 and related proteins;
                     cd08892"
                     /db_xref="CDD:176901"
     Site            order(209,211,213,222..224,226..227,232,240,248,250,252,
                     254,256,258..259,261,264,270,272..273,286..287,289,291,
                     301,303,305,307,311..319,322..324,327)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176901"
     Site            212
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95433.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL.
                     /evidence=ECO:0000305|PubMed:29127155; propagated from
                     UniProtKB/Swiss-Prot (O95433.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95433.1)"
     Site            order(261,273,286,296..297)
                     /site_type="other"
                     /note="putative Hsp90 binding residues [polypeptide
                     binding]"
                     /db_xref="CDD:176901"
     CDS             1..338
                     /gene="AHSA1"
                     /gene_synonym="AHA1; C14orf3; hAha1; p38"
                     /coded_by="NM_012111.3:98..1114"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9863.1"
                     /db_xref="GeneID:10598"
                     /db_xref="HGNC:HGNC:1189"
                     /db_xref="MIM:608466"
ORIGIN      
        1 makwgegdpr wiveeradat nvnnwhwter dasnwstdkl ktlflavqvq neegkcevte
       61 vskldgeasi nnrkgkliff yewsvklnwt gtsksgvqyk ghveipnlsd ensvdeveis
      121 vslakdepdt nlvalmkeeg vkllreamgi yistlkteft qgmilptmng esvdpvgqpa
      181 lkteerkakp apsktqarpv gvkiptckit lketfltspe elyrvfttqe lvqafthapa
      241 tleadrggkf hmvdgnvsge ftdlvpekhi vmkwrfkswp eghfatitlt fidkngetel
      301 cmegrgipap eeertrqgwq ryyfegikqt fgygarlf
//
LOCUS       NP_055467                963 aa            linear   PRI 27-APR-2025
DEFINITION  importin-13 [Homo sapiens].
ACCESSION   NP_055467 XP_003403768
VERSION     NP_055467.3
DBSOURCE    REFSEQ: accession NM_014652.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Gajewska,K.A., Jans,D.A. and Wagstaff,K.M.
  TITLE     The Nuclear Transporter Importin 13 Can Regulate Stress-Induced
            Cell Death through the Clusterin/KU70 Axis
  JOURNAL   Cells 12 (2), 279 (2023)
   PUBMED   36672214
  REMARK    GeneRIF: The Nuclear Transporter Importin 13 Can Regulate
            Stress-Induced Cell Death through the Clusterin/KU70 Axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Gajewska,K.A., Lescesen,H., Ramialison,M., Wagstaff,K.M. and
            Jans,D.A.
  TITLE     Nuclear transporter Importin-13 plays a key role in the oxidative
            stress transcriptional response
  JOURNAL   Nat Commun 12 (1), 5904 (2021)
   PUBMED   34625540
  REMARK    GeneRIF: Nuclear transporter Importin-13 plays a key role in the
            oxidative stress transcriptional response.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Zohud,B.A., Guo,P., Zohud,B.A., Li,F., Hao,J.J., Shan,X., Yu,W.,
            Guo,W., Qin,Y. and Cai,X.
  TITLE     Importin 13 promotes NSCLC progression by mediating RFPL3 nuclear
            translocation and hTERT expression upregulation
  JOURNAL   Cell Death Dis 11 (10), 879 (2020)
   PUBMED   33082305
  REMARK    GeneRIF: Importin 13 promotes NSCLC progression by mediating RFPL3
            nuclear translocation and hTERT expression upregulation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 963)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 963)
  AUTHORS   Kahle,J., Baake,M., Doenecke,D. and Albig,W.
  TITLE     Subunits of the heterotrimeric transcription factor NF-Y are
            imported into the nucleus by distinct pathways involving importin
            beta and importin 13
  JOURNAL   Mol Cell Biol 25 (13), 5339-5354 (2005)
   PUBMED   15964792
REFERENCE   7  (residues 1 to 963)
  AUTHORS   Ploski,J.E., Shamsher,M.K. and Radu,A.
  TITLE     Paired-type homeodomain transcription factors are imported into the
            nucleus by karyopherin 13
  JOURNAL   Mol Cell Biol 24 (11), 4824-4834 (2004)
   PUBMED   15143176
REFERENCE   8  (residues 1 to 963)
  AUTHORS   Weis,K.
  TITLE     Regulating access to the genome: nucleocytoplasmic transport
            throughout the cell cycle
  JOURNAL   Cell 112 (4), 441-451 (2003)
   PUBMED   12600309
  REMARK    Review article
REFERENCE   9  (residues 1 to 963)
  AUTHORS   Mingot,J.M., Kostka,S., Kraft,R., Hartmann,E. and Gorlich,D.
  TITLE     Importin 13: a novel mediator of nuclear import and export
  JOURNAL   EMBO J 20 (14), 3685-3694 (2001)
   PUBMED   11447110
REFERENCE   10 (residues 1 to 963)
  AUTHORS   Zhang,C., Sweezey,N.B., Gagnon,S., Muskat,B., Koehler,D., Post,M.
            and Kaplan,F.
  TITLE     A novel karyopherin-beta homolog is developmentally and hormonally
            regulated in fetal lung
  JOURNAL   Am J Respir Cell Mol Biol 22 (4), 451-459 (2000)
   PUBMED   10745026
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB018267.1, AL357079.24 and
            BX116797.1.
            
            On or before Aug 3, 2011 this sequence version replaced
            XP_003403768.1, NP_055467.2.
            
            Summary: This gene encodes a member of the importin-beta family of
            nuclear transport proteins. The encoded protein mediates the import
            of specific cargo proteins from the cytoplasm to the nucleus and is
            dependent on the Ras-related nuclear protein-GTPase system. The
            encoded protein is also involved in nuclear export of the
            eukaryotic translation initiation factor 1A.[provided by RefSeq,
            Mar 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB018267.1, SRR1803615.249357.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372343.8/ ENSP00000361418.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..963
                     /product="importin-13"
                     /note="karyopherin 13; Ran binding protein 13; late
                     gestation lung 2; ran-binding protein 13"
                     /calculated_mol_wt=108065
     Region          24..54
                     /region_name="HEAT 1.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          45..109
                     /region_name="IBN_N"
                     /note="Importin-beta N-terminal domain; smart00913"
                     /db_xref="CDD:197981"
     Region          56..88
                     /region_name="HEAT 2.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          95..135
                     /region_name="HEAT 3.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          116..263
                     /region_name="Xpo1"
                     /note="Exportin 1-like protein; pfam08389"
                     /db_xref="CDD:462459"
     Region          142..179
                     /region_name="HEAT 4.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          194..231
                     /region_name="HEAT 5.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          236..268
                     /region_name="HEAT 6.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          276..325
                     /region_name="HEAT 7.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          330..372
                     /region_name="HEAT 8.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          375..438
                     /region_name="HEAT 9.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          402..441
                     /region_name="Importin_rep"
                     /note="Importin 13 repeat; pfam18773"
                     /db_xref="CDD:436727"
     Region          440..476
                     /region_name="HEAT 10.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          487..522
                     /region_name="HEAT 11.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          524..558
                     /region_name="HEAT 12.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          562..600
                     /region_name="HEAT 13.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          584..627
                     /region_name="Importin_rep_2"
                     /note="Importin 13 repeat; pfam18786"
                     /db_xref="CDD:408557"
     Region          603..648
                     /region_name="HEAT 14.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          631..669
                     /region_name="Importin_rep_2"
                     /note="Importin 13 repeat; pfam18786"
                     /db_xref="CDD:408557"
     Region          676..716
                     /region_name="HEAT 15.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          720..754
                     /region_name="HEAT 16.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          761..803
                     /region_name="HEAT 17.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          815..845
                     /region_name="HEAT 18.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          826..900
                     /region_name="Importin_rep_3"
                     /note="Importin 13 repeat; pfam18806"
                     /db_xref="CDD:465873"
     Region          860..893
                     /region_name="HEAT 19.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     Region          897..931
                     /region_name="HEAT 20.
                     /evidence=ECO:0000269|PubMed:20122403"
                     /note="propagated from UniProtKB/Swiss-Prot (O94829.3)"
     CDS             1..963
                     /gene="IPO13"
                     /gene_synonym="IMP13; KAP13; LGL2; RANBP13"
                     /coded_by="NM_014652.4:652..3543"
                     /db_xref="CCDS:CCDS503.1"
                     /db_xref="GeneID:9670"
                     /db_xref="HGNC:HGNC:16853"
                     /db_xref="MIM:610411"
ORIGIN      
        1 merreeqpga agagaapald ftvenvekal hqlyydpnie nknlaqkwlm qaqvspqawh
       61 fswqllqpdk vpeiqyfgas alhikisryw sdiptdqyes lkaqlftqit rfasgskivl
      121 trlcvalasl alsmmpdawp cavadmvrlf qaedspvdgq grclallell tvlpeefqts
      181 rlpqyrkglv rtslavecga vfplleqllq qpsspscvrq kvlkcfsswv qlevplqdce
      241 aliqaafaal qdselfdssv eaivnaisqp daqryvntll kliplvlglq eqlrqavqng
      301 dmetshgicr iavalgenhs ralldqvehw qsflalvnmi mfctgipghy pvnettsslt
      361 ltfwytlqdd ilsfeaekqa vyqqvyrpvy fqlvdvllhk aqfpsdeeyg fwssdekeqf
      421 riyrvdisdt lmyvyemlga ellsnlydkl grlltsseep yswqhteall ygfqsiaeti
      481 dvnysdvvpg ligliprisi snvqladtvm ftigalsewl adhpvminsv lplvlhalgn
      541 pelsvssvst lkkicrecky dlppyaaniv avsqdvlmkq ihktsqcmwl mqalgfllsa
      601 lqveeilknl hslispyiqq leklaeeipn psnklaivhi lgllsnlftt ldishheddh
      661 egpelrklpv pqgpnpvvvv lqqvfqliqk vlskwlndaq vveavcaife ksvktllddf
      721 apmvpqlcem lgrmystipq asaldltrql vhifahepah fppiealfll vtsvtltlfq
      781 qgprdhpdiv dsfmqllaqa lkrkpdlflc erldvkavfq cavlalkfpe aptvkascgf
      841 ftellprcge vesvgkvvqe dgrmlliavl eaiggqasrs lmdcfadilf alnkhcfsll
      901 smwikealqp pgfpsarlsp eqkdtfsqqi lrervnkrrv kemvkeftll crglhgtdyt
      961 ady
//
LOCUS       NP_054906                173 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 208 isoform 1 [Homo sapiens].
ACCESSION   NP_054906
VERSION     NP_054906.2
DBSOURCE    REFSEQ: accession NM_014187.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Yang,J. and Song,T.
  TITLE     Exploring the Role and Prognostic Value of TMEM208 in Head and Neck
            Squamous Cell Carcinoma
  JOURNAL   Asian Pac J Cancer Prev 25 (3), 909-919 (2024)
   PUBMED   38546073
  REMARK    GeneRIF: Exploring the Role and Prognostic Value of TMEM208 in Head
            and Neck Squamous Cell Carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Dutta,D., Kanca,O., Shridharan,R.V., Marcogliese,P.C., Steger,B.,
            Morimoto,M., Frost,F.G., Macnamara,E., Wangler,M.F., Yamamoto,S.,
            Jenny,A., Adams,D., Malicdan,M.C. and Bellen,H.J.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     Loss of the endoplasmic reticulum protein Tmem208 affects cell
            polarity, development, and viability
  JOURNAL   Proc Natl Acad Sci U S A 121 (9), e2322582121 (2024)
   PUBMED   38381787
  REMARK    GeneRIF: Loss of the endoplasmic reticulum protein Tmem208 affects
            cell polarity, development, and viability.
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Yang,J., Hirata,T., Liu,Y.S., Guo,X.Y., Gao,X.D., Kinoshita,T. and
            Fujita,M.
  TITLE     Human SND2 mediates ER targeting of GPI-anchored proteins with low
            hydrophobic GPI attachment signals
  JOURNAL   FEBS Lett 595 (11), 1542-1558 (2021)
   PUBMED   33838053
  REMARK    GeneRIF: Human SND2 mediates ER targeting of GPI-anchored proteins
            with low hydrophobic GPI attachment signals.
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Lei,P., Xiao,Y., Li,P., Xie,P., Wang,H., Huang,S., Song,P. and
            Zhao,Y.
  TITLE     hSnd2/TMEM208 is an HIF-1alpha-targeted gene and contains a WH2
            motif
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 52 (3), 328-331 (2020)
   PUBMED   32002553
  REMARK    GeneRIF: hSnd2/TMEM208 is an HIF-1alpha-targeted gene and contains
            a WH2 motif.
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Hassdenteufel,S., Sicking,M., Schorr,S., Aviram,N.,
            Fecher-Trost,C., Schuldiner,M., Jung,M., Zimmermann,R. and Lang,S.
  TITLE     hSnd2 protein represents an alternative targeting factor to the
            endoplasmic reticulum in human cells
  JOURNAL   FEBS Lett 591 (20), 3211-3224 (2017)
   PUBMED   28862756
  REMARK    GeneRIF: Snd2 protein represents an alternative targeting factor to
            the endoplasmic reticulum in human cells.
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Zhao,Y., Hu,J., Miao,G., Qu,L., Wang,Z., Li,G., Lv,P., Ma,D. and
            Chen,Y.
  TITLE     Transmembrane protein 208: a novel ER-localized protein that
            regulates autophagy and ER stress
  JOURNAL   PLoS One 8 (5), e64228 (2013)
   PUBMED   23691174
  REMARK    GeneRIF: novel ER-located protein regulates both ER stress and
            autophagy
            Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI838179.1 and BC003080.2.
            
            On Nov 23, 2006 this sequence version replaced NP_054906.1.
            
            Summary: This gene encodes a highly conserved protein which is
            localized in the endoplasmic reticulum (ER). The protein is linked
            to autophagy and ER stress. Knockdown of this gene increased
            autophagy and triggered ER stress. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.31429.1,
                                           SRR5189655.218246.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304800.14/ ENSP00000305892.9
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..173
                     /product="transmembrane protein 208 isoform 1"
                     /note="SRP-independent targeting 2 homolog"
                     /calculated_mol_wt=19511
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:25732826,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BTX3.1)"
     Region          8..156
                     /region_name="TMEM208_SND2"
                     /note="SRP-independent targeting protein 2/TMEM208;
                     pfam05620"
                     /db_xref="CDD:428546"
     Site            25..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX3.1)"
     Site            51..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX3.1)"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX3.1)"
     Region          152..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX3.1)"
     CDS             1..173
                     /gene="TMEM208"
                     /gene_synonym="hSND2; HSPC171; SND2"
                     /coded_by="NM_014187.4:90..611"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45511.1"
                     /db_xref="GeneID:29100"
                     /db_xref="HGNC:HGNC:25015"
                     /db_xref="MIM:620781"
ORIGIN      
        1 mapkgkvgtr gkkqifeenr etlkfylrii lganaiyclv tlvffyssas fwawlalgfs
       61 lavygasyhs mssmaraafs edgalmdggm dlnmeqgmae hlkdvillta ivqvlscfsl
      121 yvwsfwllap gralyllwvn vlgpwftads gtpapehnek rqrrqerrqm krl
//
LOCUS       NP_057559                311 aa            linear   PRI 27-APR-2025
DEFINITION  JNK1/MAPK8-associated membrane protein isoform 1 [Homo sapiens].
ACCESSION   NP_057559
VERSION     NP_057559.2
DBSOURCE    REFSEQ: accession NM_016475.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Cubero,F.J., Zhao,G., Nevzorova,Y.A., Hatting,M., Al Masaoudi,M.,
            Verdier,J., Peng,J., Schaefer,F.M., Hermanns,N., Boekschoten,M.V.,
            Grouls,C., Gassler,N., Kiessling,F., Muller,M., Davis,R.J.,
            Liedtke,C. and Trautwein,C.
  TITLE     Haematopoietic cell-derived Jnk1 is crucial for chronic
            inflammation and carcinogenesis in an experimental model of liver
            injury
  JOURNAL   J Hepatol 62 (1), 140-149 (2015)
   PUBMED   25173965
  REMARK    GeneRIF: synergistic function of Jnk1 in haematopoietic cells and
            hepatocytes might be relevant for the development of chronic liver
            injury
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Roy,S.J., Glazkova,I., Frechette,L., Iorio-Morin,C., Binda,C.,
            Petrin,D., Trieu,P., Robitaille,M., Angers,S., Hebert,T.E. and
            Parent,J.L.
  TITLE     Novel, gel-free proteomics approach identifies RNF5 and JAMP as
            modulators of GPCR stability
  JOURNAL   Mol Endocrinol 27 (8), 1245-1266 (2013)
   PUBMED   23798571
  REMARK    GeneRIF: Expression of DP, a receptor largely retained in the ER,
            promoted proteasome recruitment by JAMP.
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Tcherpakov,M., Delaunay,A., Toth,J., Kadoya,T., Petroski,M.D. and
            Ronai,Z.A.
  TITLE     Regulation of endoplasmic reticulum-associated degradation by
            RNF5-dependent ubiquitination of JNK-associated membrane protein
            (JAMP)
  JOURNAL   J Biol Chem 284 (18), 12099-12109 (2009)
   PUBMED   19269966
  REMARK    GeneRIF: RNF5 associates with JAMP in the ER membrane. This
            association results in Ubc13-dependent RNF5-mediated noncanonical
            ubiquitination of JAMP.
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Tcherpakov,M., Broday,L., Delaunay,A., Kadoya,T., Khurana,A.,
            Erdjument-Bromage,H., Tempst,P., Qiu,X.B., DeMartino,G.N. and
            Ronai,Z.
  TITLE     JAMP optimizes ERAD to protect cells from unfolded proteins
  JOURNAL   Mol Biol Cell 19 (11), 5019-5028 (2008)
   PUBMED   18784250
  REMARK    GeneRIF: JAMP is an important component for coordinated clearance
            of misfolded proteins from the endoplasmic reticulum.
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Kadoya,T., Khurana,A., Tcherpakov,M., Bromberg,K.D., Didier,C.,
            Broday,L., Asahara,T., Bhoumik,A. and Ronai,Z.
  TITLE     JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein,
            regulates duration of JNK activity
  JOURNAL   Mol Cell Biol 25 (19), 8619-8630 (2005)
   PUBMED   16166642
  REMARK    GeneRIF: Identification and functional characterization of the
            mouse Jamp ortholog.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC381037.1, AL136696.1, BX161501.1, AL121694.4 and HY340214.1.
            
            On Jun 10, 2002 this sequence version replaced NP_057559.1.
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.125270.1,
                                           SRR1803616.15433.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000616435.5/ ENSP00000479775.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.1"
     Protein         1..311
                     /product="JNK1/MAPK8-associated membrane protein isoform
                     1"
                     /note="JNK-associated membrane protein; Jun N-terminal
                     kinase 1-associated membrane protein; medulloblastoma
                     antigen MU-MB-50.4"
                     /calculated_mol_wt=35108
     Region          9..300
                     /region_name="JAMP"
                     /note="JNK1/MAPK8-associated membrane protein; pfam05571"
                     /db_xref="CDD:398936"
     Site            22
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9P055.4)"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P055.4)"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P055.4)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P055.4)"
     Site            189..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P055.4)"
     Site            211..231
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P055.4)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P055.4)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P055.4)"
     CDS             1..311
                     /gene="JKAMP"
                     /gene_synonym="C14orf100; C24orf100; CDA06; HSPC213;
                     HSPC327; JAMP"
                     /coded_by="NM_016475.5:74..1009"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45116.1"
                     /db_xref="GeneID:51528"
                     /db_xref="HGNC:HGNC:20184"
                     /db_xref="MIM:611176"
ORIGIN      
        1 mavdiqpacl glycgktllf kngsteiyge cgvcprgqrt naqkycqpct espelydwly
       61 lgfmamlplv lhwffiewys gkksssalfq hitalfecsm aaiitllvsd pvgvlyirsc
      121 rvlmlsdwyt mlynpspdyv ttvhctheav yplytivfiy yafclvlmml lrpllvkkia
      181 cglgksdrfk siyaalyffp iltvlqavgg gllyyafpyi ilvlslvtla vymsaseien
      241 cydllvrkkr livlfshwll haygiisisr vdkleqdlpl lalvptpalf ylftakftep
      301 srilsegang h
//
LOCUS       NP_005253                205 aa            linear   PRI 27-APR-2025
DEFINITION  FAD-linked sulfhydryl oxidase ALR [Homo sapiens].
ACCESSION   NP_005253
VERSION     NP_005253.3
DBSOURCE    REFSEQ: accession NM_005262.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Feng,S., Zhao,J., Yang,T. and Li,L.
  TITLE     TMPRSS11D/ALR-mediated ER stress regulates the function of
            myeloid-derived suppressor cells in the cervical cancer
            microenvironment
  JOURNAL   Int Immunopharmacol 124 (Pt A), 110869 (2023)
   PUBMED   37666068
  REMARK    GeneRIF: TMPRSS11D/ALR-mediated ER stress regulates the function of
            myeloid-derived suppressor cells in the cervical cancer
            microenvironment.
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Guo,L., Dou,Y., Xiang,Y., Luo,L., Xu,X., Wang,Q., Zhang,Y. and
            Liang,T.
  TITLE     Systematic analysis of cancer-specific synthetic lethal
            interactions provides insight into personalized anticancer therapy
  JOURNAL   FEBS J 290 (6), 1531-1548 (2023)
   PUBMED   36181326
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Klyosova,E.Y., Shkurat,E.A., Azarova,Y.E. and Polonikov,A.V.
  TITLE     Polymorphism rs1046495 of the GFER Gene as a New Genetic Marker of
            Preposition to Type 2 Diabetes Mellitus
  JOURNAL   Bull Exp Biol Med 172 (5), 587-591 (2022)
   PUBMED   35352250
  REMARK    GeneRIF: Polymorphism rs1046495 of the GFER Gene as a New Genetic
            Marker of Preposition to Type 2 Diabetes Mellitus.
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Lisowsky,T., Weinstat-Saslow,D.L., Barton,N., Reeders,S.T. and
            Schneider,M.C.
  TITLE     A new human gene located in the PKD1 region of chromosome 16 is a
            functional homologue to ERV1 of yeast
  JOURNAL   Genomics 29 (3), 690-697 (1995)
   PUBMED   8575761
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Francavilla,A., Hagiya,M., Porter,K.A., Polimeno,L., Ihara,I. and
            Starzl,T.E.
  TITLE     Augmenter of liver regeneration: its place in the universe of
            hepatic growth factors
  JOURNAL   Hepatology 20 (3), 747-757 (1994)
   PUBMED   8076931
  REMARK    Review article
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Lisowsky,T.
  TITLE     Dual function of a new nuclear gene for oxidative phosphorylation
            and vegetative growth in yeast
  JOURNAL   Mol Gen Genet 232 (1), 58-64 (1992)
   PUBMED   1552903
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Renan,M.J. and Reeves,B.R.
  TITLE     Chromosomal localization of human endogenous retroviral element
            ERV1 to 18q22----q23 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 44 (2-3), 167-170 (1987)
   PUBMED   3568764
REFERENCE   10 (residues 1 to 205)
  AUTHORS   O'Brien,S.J., Bonner,T.I., Cohen,M., O'Connell,C. and Nash,W.G.
  TITLE     Mapping of an endogenous retroviral sequence to human chromosome 18
  JOURNAL   Nature 303 (5912), 74-77 (1983)
   PUBMED   6843662
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG705583.1, AF306863.1 and
            BC002429.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 13, 2004 this sequence version replaced NP_005253.2.
            
            Summary: The hepatotrophic factor designated augmenter of liver
            regeneration (ALR) is thought to be one of the factors responsible
            for the extraordinary regenerative capacity of mammalian liver. It
            has also been called hepatic regenerative stimulation substance
            (HSS). The gene resides on chromosome 16 in the interval containing
            the locus for polycystic kidney disease (PKD1). The putative gene
            product is 42% similar to the scERV1 protein of yeast. The yeast
            scERV1 gene had been found to be essential for oxidative
            phosphorylation, the maintenance of mitochondrial genomes, and the
            cell division cycle. The human gene is both the structural and
            functional homolog of the yeast scERV1 gene. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC002429.1, SRR3476690.738756.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248114.7/ ENSP00000248114.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..205
                     /product="FAD-linked sulfhydryl oxidase ALR"
                     /EC_number="1.8.3.2"
                     /note="hepatic regenerative stimulation substance; ERV1
                     homolog; erv1-like growth factor; hepatopoietin protein"
                     /calculated_mol_wt=23318
     Region          1..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55789.2)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P55789.2)"
     Region          <86..201
                     /region_name="Evr1_Alr"
                     /note="Erv1 / Alr family; cl02107"
                     /db_xref="CDD:470469"
     CDS             1..205
                     /gene="GFER"
                     /gene_synonym="ALR; ERV1; HERV1; HPO; HPO1; HPO2; HSS;
                     MMCHD; MPMCD"
                     /coded_by="NM_005262.3:27..644"
                     /db_xref="CCDS:CCDS32368.1"
                     /db_xref="GeneID:2671"
                     /db_xref="HGNC:HGNC:4236"
                     /db_xref="MIM:600924"
ORIGIN      
        1 maapgergrf hggnlfflpg garsemmddl atdargrgag rrdaaasast paqaptsdsp
       61 vaedasrrrp cracvdfktw mrtqqkrdtk fredcppdre elgrhswavl htlaayypdl
      121 ptpeqqqdma qfihlfskfy pceecaedlr krlcrnhpdt rtracftqwl chlhnevnrk
      181 lgkpdfdcsk vderwrdgwk dgscd
//
LOCUS       NP_082602                860 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 618 isoform b [Mus musculus].
ACCESSION   NP_082602 XP_001473246 XP_915675
VERSION     NP_082602.1
DBSOURCE    REFSEQ: accession NM_028326.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Lee,D.J., Kim,H.Y., Lee,S.J. and Jung,H.S.
  TITLE     Spatiotemporal Changes in Transcriptome of Odontogenic and
            Non-odontogenic Regions in the Dental Arch of Mus musculus
  JOURNAL   Front Cell Dev Biol 9, 723326 (2021)
   PUBMED   34722506
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Quina,L.A., Wang,S., Ng,L. and Turner,E.E.
  TITLE     Brn3a and Nurr1 mediate a gene regulatory pathway for habenula
            development
  JOURNAL   J Neurosci 29 (45), 14309-14322 (2009)
   PUBMED   19906978
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Georgas,K., Rumballe,B., Valerius,M.T., Chiu,H.S.,
            Thiagarajan,R.D., Lesieur,E., Aronow,B.J., Brunskill,E.W.,
            Combes,A.N., Tang,D., Taylor,D., Grimmond,S.M., Potter,S.S.,
            McMahon,A.P. and Little,M.H.
  TITLE     Analysis of early nephron patterning reveals a role for distal RV
            proliferation in fusion to the ureteric tip via a cap
            mesenchyme-derived connecting segment
  JOURNAL   Dev Biol 332 (2), 273-286 (2009)
   PUBMED   19501082
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Long,J.E., Cobos,I., Potter,G.B. and Rubenstein,J.L.
  TITLE     Dlx1&2 and Mash1 transcription factors control MGE and CGE
            patterning and differentiation through parallel and overlapping
            pathways
  JOURNAL   Cereb Cortex 19 Suppl 1 (Suppl 1), i96-i106 (2009)
   PUBMED   19386638
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Kumar,S., Tomooka,Y. and Noda,M.
  TITLE     Identification of a set of genes with developmentally
            down-regulated expression in the mouse brain
  JOURNAL   Biochem Biophys Res Commun 185 (3), 1155-1161 (1992)
   PUBMED   1378265
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL691431.20 and AL691496.13.
            
            On or before Jul 2, 2009 this sequence version replaced
            XP_915675.3, XP_001473246.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN00849374, SAMN00849375
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 33.82 cM"
     Protein         1..860
                     /product="zinc finger protein 618 isoform b"
                     /note="neural precursor cell expressed, developmentally
                     down-regulated gene 10"
                     /calculated_mol_wt=95335
     Region          116..136
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          157..177
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..860
                     /gene="Zfp618"
                     /gene_synonym="2810031P15Rik; 2810040O04Rik; bM257P7.1;
                     D430033D05Rik; Nedd10; Znf618"
                     /coded_by="NM_028326.2:108..2690"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS51203.1"
                     /db_xref="GeneID:72701"
                     /db_xref="MGI:MGI:1919950"
ORIGIN      
        1 msqpdgaaap qvdgasapgr ksavnrerlk rsqksskveg pepvpaeasl saeqgtmtev
       61 kvktevpddy iqeviwqgea keekaggkds tgdvpaeicv viggvrnqqt lgsyecgicg
      121 kkykyyncfq thvrahrdte atsgegvsqs nnfrytcdic gkkykyyscf qehrdlhavd
      181 vfsvegapen radpfdqgvv atdevkeepp epfqkigpms spvsasyprc emrmceqrkt
      241 gnytcefcgk qykyytpyqe hvalhapikn tfsrrveska qnhfeetnss sqnssepytc
      301 gacgiqfqfy snllehmqsh aadnennits nqsrsppaav eekwkpqaqr nsanntttsg
      361 ltpnsvipek erqniaerll rvmcadlgal svvsgkeflk laqtlvdsga rygafsvtei
      421 lgnfntlalk hlprmynqvk vkvtcalgsn aclgigvtch sqsvgpdscy iltayqaegn
      481 hiksyvlgvk gadirdsgdl vhhwvqnvls efvmseirtv yvtdcrvsts afskagmclr
      541 csacalnsvv qsvlskrtlq arsmheviel lnvcedlags tglaketfgs leetspppcw
      601 nsvtdslllv heryeqicef ysrakkmnli qslnkhllsn laailtpvkq avielsnesq
      661 ptlqlvlpty vrleklftak andagtvskl chlflealke nfkvhpahkv amildpqqkl
      721 rpvppyqhee iiskvcelin evkeswaeea dfepaakkar satgehpaaq eedrlgknev
      781 ydylqeplfq atpdlfqyws cvtqkhtkla klafwllavp avgarsgcvn mceqallikr
      841 rrllspedmn klmflksnml
//
LOCUS       NP_001348929              88 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 1 [Mus musculus].
ACCESSION   NP_001348929
VERSION     NP_001348929.1
DBSOURCE    REFSEQ: accession NM_001362000.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 88)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 88)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 88)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 88)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7.
            
            Transcript Variant: This variant (10), as well as variants 1, 8, 9,
            and 11-19, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.121165.1,
                                           SRR1660819.182870.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..88
                     /product="cAMP-regulated phosphoprotein 21 isoform 1"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=9408
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q7M2N1; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10854908,
                     ECO:0000269|PubMed:15499021; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     CDS             1..88
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362000.1:745..1011"
                     /note="isoform 1 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS40786.1"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqtl
//
LOCUS       NP_056480                546 aa            linear   PRI 27-APR-2025
DEFINITION  aladin isoform 1 [Homo sapiens].
ACCESSION   NP_056480
VERSION     NP_056480.1
DBSOURCE    REFSEQ: accession NM_015665.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Smits,D.J., Dekker,J., Douben,H., Schot,R., Magee,H., Bakhtiari,S.,
            Koehler,K., Huebner,A., Schuelke,M., Darvish,H., Vosoogh,S.,
            Tafakhori,A., Jameie,M., Taghiabadi,E., Wilson,Y., Shah,M., van
            Slegtenhorst,M.A., Medici-van den Herik,E.G., van Ham,T.J.,
            Kruer,M.C. and Mancini,G.M.S.
  TITLE     Biallelic NDC1 variants that interfere with ALADIN binding are
            associated with neuropathy and triple A-like syndrome
  JOURNAL   HGG Adv 5 (4), 100327 (2024)
   PUBMED   39003500
  REMARK    GeneRIF: Biallelic NDC1 variants that interfere with ALADIN binding
            are associated with neuropathy and triple A-like syndrome.
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Jayant,S.S., Gupta,R., Agrawal,K., Das,L., Dutta,P. and Bhansali,A.
  TITLE     Triple A (Allgrove) syndrome due to AAAS gene mutation with a rare
            association of amyotrophy
  JOURNAL   Hormones (Athens) 20 (1), 197-205 (2021)
   PUBMED   32700293
  REMARK    GeneRIF: Triple A (Allgrove) syndrome due to AAAS gene mutation
            with a rare association of amyotrophy.
            Review article
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Koehler,K., Hackmann,K., Landgraf,D., Schubert,T., Shakiba,M.,
            Kariminejad,A. and Huebner,A.
  TITLE     Homozygous deletion of the entire AAAS gene in a triple A syndrome
            patient
  JOURNAL   Eur J Med Genet 62 (7), 103665 (2019)
   PUBMED   31071487
  REMARK    GeneRIF: A homozygous deletion of the entire AAAS gene was
            identified in a patient with triple A syndrome.
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Leveille,E., Gonorazky,H.D., Rioux,M.F., Hazrati,L.N., Ruskey,J.A.,
            Carnevale,A., Spiegelman,D., Dionne-Laporte,A., Rouleau,G.A.,
            Yoon,G. and Gan-Or,Z.
  TITLE     Triple A syndrome presenting as complicated hereditary spastic
            paraplegia
  JOURNAL   Mol Genet Genomic Med 6 (6), 1134-1139 (2018)
   PUBMED   30381913
  REMARK    GeneRIF: AAAS mutations were identified in two families with
            hereditary spastic paraplegia.
REFERENCE   5  (residues 1 to 546)
  AUTHORS   Singh,K., Puri,R.D., Bhai,P., Arya,A.D., Chawla,G., Saxena,R. and
            Verma,I.C.
  TITLE     Clinical heterogeneity and molecular profile of triple A syndrome:
            a study of seven cases
  JOURNAL   J Pediatr Endocrinol Metab 31 (7), 799-807 (2018)
   PUBMED   29874194
  REMARK    GeneRIF: Mutation in AAAS gene is associated with triple A
            syndrome.
REFERENCE   6  (residues 1 to 546)
  AUTHORS   Sandrini,F., Farmakidis,C., Kirschner,L.S., Wu,S.M.,
            Tullio-Pelet,A., Lyonnet,S., Metzger,D.L., Bourdony,C.J.,
            Tiosano,D., Chan,W.Y. and Stratakis,C.A.
  TITLE     Spectrum of mutations of the AAAS gene in Allgrove syndrome: lack
            of mutations in six kindreds with isolated resistance to
            corticotropin
  JOURNAL   J Clin Endocrinol Metab 86 (11), 5433-5437 (2001)
   PUBMED   11701718
REFERENCE   7  (residues 1 to 546)
  AUTHORS   Handschug,K., Sperling,S., Yoon,S.J., Hennig,S., Clark,A.J. and
            Huebner,A.
  TITLE     Triple A syndrome is caused by mutations in AAAS, a new WD-repeat
            protein gene
  JOURNAL   Hum Mol Genet 10 (3), 283-290 (2001)
   PUBMED   11159947
REFERENCE   8  (residues 1 to 546)
  AUTHORS   Tullio-Pelet,A., Salomon,R., Hadj-Rabia,S., Mugnier,C., de
            Laet,M.H., Chaouachi,B., Bakiri,F., Brottier,P., Cattolico,L.,
            Penet,C., Begeot,M., Naville,D., Nicolino,M., Chaussain,J.L.,
            Weissenbach,J., Munnich,A. and Lyonnet,S.
  TITLE     Mutant WD-repeat protein in triple-A syndrome
  JOURNAL   Nat Genet 26 (3), 332-335 (2000)
   PUBMED   11062474
REFERENCE   9  (residues 1 to 546)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   10 (residues 1 to 546)
  AUTHORS   Weber,A., Wienker,T.F., Jung,M., Easton,D., Dean,H.J.,
            Heinrichs,C., Reis,A. and Clark,A.J.
  TITLE     Linkage of the gene for the triple A syndrome to chromosome 12q13
            near the type II keratin gene cluster
  JOURNAL   Hum Mol Genet 5 (12), 2061-2066 (1996)
   PUBMED   8968764
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC393722.1 and AJ289857.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            WD-repeat family of regulatory proteins and may be involved in
            normal development of the peripheral and central nervous system.
            The encoded protein is part of the nuclear pore complex and is
            anchored there by NDC1. Defects in this gene are a cause of
            achalasia-addisonianism-alacrima syndrome (AAAS), also called
            triple-A syndrome or Allgrove syndrome. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF226048.1, BC000659.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000209873.9/ ENSP00000209873.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..546
                     /product="aladin isoform 1"
                     /note="Allgrove, triple-A; achalasia, adrenocortical
                     insufficiency, alacrimia"
                     /calculated_mol_wt=59443
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylcysteine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Region          142..180
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Region          157..193
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <158..>344
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          183..222
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Region          197..243
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          234..274
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Region          247..283
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          280..316
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Region          291..328
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          324..380
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Region          356..390
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          386..433
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Region          442..482
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Region          500..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58742; propagated from
                     UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58742; propagated from
                     UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NRG9.1)"
     Region          544..546
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRG9.1)"
     CDS             1..546
                     /gene="AAAS"
                     /gene_synonym="AAA; AAASb; ADRACALA; ADRACALIN; ALADIN;
                     GL003"
                     /coded_by="NM_015665.6:146..1786"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8856.1"
                     /db_xref="GeneID:8086"
                     /db_xref="HGNC:HGNC:13666"
                     /db_xref="MIM:605378"
ORIGIN      
        1 mcslglfppp pprgqvtlye hnnelvtgss yespppdfrg qwinlpvlql tkdplktpgr
       61 ldhgtrtafi hhreqvwkrc iniwrdvglf gvlneianse eevfewvkta sgwalalcrw
      121 asslhgslfp hlslrsedli aefaqvtnws scclrvfawh phtnkfaval lddsvrvyna
      181 sstivpslkh rlqrnvasla wkplsasvla vacqsciliw tldptslstr pssgcaqvls
      241 hpghtpvtsl awapsggrll saspvdaair vwdvstetcv plpwfrgggv tnllwspdgs
      301 kilattpsav frvweaqmwt cerwptlsgr cqtgcwspdg srllftvlge pliyslsfpe
      361 rcgegkgcvg gaksativad lsettiqtpd geerlggeah smvwdpsger lavlmkgkpr
      421 vqdgkpvill frtrnspvfe llpcgiiqge pgaqpqlitf hpsfnkgall svgwstgria
      481 hiplyfvnaq fprfspvlgr aqeppagggg sihdlplfte tsptsapwdp lpgpppvlph
      541 sphshl
//
LOCUS       NP_001009909             346 aa            linear   PRI 27-APR-2025
DEFINITION  leucine zipper protein 2 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001009909 XP_370616
VERSION     NP_001009909.2
DBSOURCE    REFSEQ: accession NM_001009909.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Li,Y., Deng,G., Qi,Y., Zhang,H., Jiang,H., Geng,R., Ye,Z., Liu,B.
            and Chen,Q.
  TITLE     Downregulation of LUZP2 Is Correlated with Poor Prognosis of
            Low-Grade Glioma
  JOURNAL   Biomed Res Int 2020, 9716720 (2020)
   PUBMED   32695826
  REMARK    GeneRIF: Downregulation of LUZP2 Is Correlated with Poor Prognosis
            of Low-Grade Glioma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Cummings,A.C., Jiang,L., Velez Edwards,D.R., McCauley,J.L.,
            Laux,R., McFarland,L.L., Fuzzell,D., Knebusch,C., Caywood,L.,
            Reinhart-Mercer,L., Nations,L., Gilbert,J.R., Konidari,I.,
            Tramontana,M., Cuccaro,M.L., Scott,W.K., Pericak-Vance,M.A. and
            Haines,J.L.
  TITLE     Genome-wide association and linkage study in the Amish detects a
            novel candidate late-onset Alzheimer disease gene
  JOURNAL   Ann Hum Genet 76 (5), 342-351 (2012)
   PUBMED   22881374
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Loo,S.K., Shtir,C., Doyle,A.E., Mick,E., McGough,J.J.,
            McCracken,J., Biederman,J., Smalley,S.L., Cantor,R.M., Faraone,S.V.
            and Nelson,S.F.
  TITLE     Genome-wide association study of intelligence: additive effects of
            novel brain expressed genes
  JOURNAL   J Am Acad Child Adolesc Psychiatry 51 (4), 432-440 (2012)
   PUBMED   22449649
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Benyamin,B., McRae,A.F., Zhu,G., Gordon,S., Henders,A.K.,
            Palotie,A., Peltonen,L., Martin,N.G., Montgomery,G.W.,
            Whitfield,J.B. and Visscher,P.M.
  TITLE     Variants in TF and HFE explain approximately 40% of genetic
            variation in serum-transferrin levels
  JOURNAL   Am J Hum Genet 84 (1), 60-65 (2009)
   PUBMED   19084217
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 346)
  AUTHORS   Wu,M., Michaud,E.J. and Johnson,D.K.
  TITLE     Cloning, functional study and comparative mapping of Luzp2 to mouse
            chromosome 7 and human chromosome 11p13-11p14
  JOURNAL   Mamm Genome 14 (5), 323-334 (2003)
   PUBMED   12856284
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA706662.1, BC132829.1,
            AC087373.4, AK126974.1 and AL832641.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 21, 2005 this sequence version replaced NP_001009909.1.
            
            Summary: This gene encodes a leucine zipper protein. This protein
            is deleted in some patients with Wilms tumor-Aniridia-Genitourinary
            anomalies-mental Retardation (WAGR) syndrome. Alternate splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.216111.1, AL832641.3
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336930.11/ ENSP00000336817.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p14.3"
     Protein         1..346
                     /product="leucine zipper protein 2 isoform 1 precursor"
                     /calculated_mol_wt=36865
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86TE4.2)"
                     /calculated_mol_wt=2111
     mat_peptide     20..346
                     /product="Leucine zipper protein 2. /id=PRO_0000315274"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TE4.2)"
                     /calculated_mol_wt=36865
     Region          <25..>208
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86TE4.2)"
     Region          164..192
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TE4.2)"
     Region          221..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TE4.2)"
     Region          248..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TE4.2)"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86TE4.2)"
     Site            302
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86TE4.2)"
     CDS             1..346
                     /gene="LUZP2"
                     /gene_synonym="KFSP2566; PRO6246"
                     /coded_by="NM_001009909.4:192..1232"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS31446.1"
                     /db_xref="GeneID:338645"
                     /db_xref="HGNC:HGNC:23206"
                     /db_xref="MIM:608178"
ORIGIN      
        1 mkfspahyll pllpalvlst rqdyeelekq lkevfkerst ilrqltktsr eldgikvnlq
       61 slkndeqsak tdvqkllelg qkqreemksl qealqnqlke tsekaekhqa tinflkteve
      121 rkskmirdlq nenkslknkl lsgnklcgih aeeskkiqaq lkelrygkkd llfkaqqltd
      181 leqklavakn elekaaldre sqmkamketv qlcltsvfrd qpppplslit snptrmllpp
      241 rniasklpda aakskpqqsa sgnnessqve stkegnpstt acdsqdegrp csmkhkespp
      301 snataetepi pqklqmppcs ecevkkapek pltsfegmaa reekil
//
LOCUS       NP_542391                300 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger CCCH-type antiviral protein 1-like [Homo sapiens].
ACCESSION   NP_542391
VERSION     NP_542391.2
DBSOURCE    REFSEQ: accession NM_080660.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Fang,W., Wei,Y., Kang,Y. and Landweber,L.F.
  TITLE     Detection of a common chimeric transcript between human chromosomes
            7 and 16
  JOURNAL   Biol Direct 7, 49 (2012)
   PUBMED   23273016
  REMARK    GeneRIF: Study reports the discovery of a chimeric RNA between
            ZC3HAV1L and CHMP1A in human, located on chromosome 7 and 16,
            respectively. The fusion occurs at an exon-exon boundary, and was
            detected both computationally and experimentally from different
            cells or tissue types.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC083868.3 and BC008842.2.
            
            On Sep 28, 2009 this sequence version replaced NP_542391.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008842.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147920 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000275766.2/ ENSP00000275766.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..300
                     /product="zinc finger CCCH-type antiviral protein 1-like"
                     /note="zinc finger CCCH-type, antiviral 1-like; zinc
                     finger CCCH-type containing, antiviral 1 like"
                     /calculated_mol_wt=32831
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.3,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96H79.2)"
     Region          5..60
                     /region_name="HTH_53"
                     /note="Zap helix turn helix N-terminal domain; pfam18606"
                     /db_xref="CDD:465819"
     Region          252..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96H79.2)"
     CDS             1..300
                     /gene="ZC3HAV1L"
                     /gene_synonym="C7orf39"
                     /coded_by="NM_080660.4:26..928"
                     /db_xref="CCDS:CCDS5850.1"
                     /db_xref="GeneID:92092"
                     /db_xref="HGNC:HGNC:22423"
ORIGIN      
        1 maeptvcsfl tkvlcahggr mflkdlrghv elsearlrdv lqragperfl lqevetqegl
       61 gdaeaeaaag avggggtsaw rvvavssvrl caryqrgecq acdqlhfcrr hmlgkcpnrd
      121 cwstctlshd ihtpvnmqvl kshglfglne nqlrilllqn dpcllpevcl lynkgealyg
      181 ycnlkdkcnk fhvcksfvkg ecklqtckrs hqlihaaslk llqdqglnip svvnfqiist
      241 ykhmklhkml entdnsspst ehsqglekqg vhaagaaeag plasvpaqsa kkpcpvscek
//
LOCUS       NP_766281                576 aa            linear   ROD 27-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 12 [Mus musculus].
ACCESSION   NP_766281
VERSION     NP_766281.1
DBSOURCE    REFSEQ: accession NM_172693.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Airik,M., Schuler,M., McCourt,B., Weiss,A.C., Herdman,N.,
            Ludtke,T.H., Widmeier,E., Stolz,D.B., Nejak-Bowen,K.N.,
            Yimlamai,D., Wu,Y.L., Kispert,A., Airik,R. and Hildebrandt,F.
  TITLE     Loss of Anks6 leads to YAP deficiency and liver abnormalities
  JOURNAL   Hum Mol Genet 29 (18), 3064-3080 (2020)
   PUBMED   32886109
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Peluso,G., Tian,E., Abusleme,L., Munemasa,T., Mukaibo,T. and Ten
            Hagen,K.G.
  TITLE     Loss of the disease-associated glycosyltransferase Galnt3 alters
            Muc10 glycosylation and the composition of the oral microbiome
  JOURNAL   J Biol Chem 295 (5), 1411-1425 (2020)
   PUBMED   31882545
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Tian,E., Wang,S., Zhang,L., Zhang,Y., Malicdan,M.C., Mao,Y.,
            Christoffersen,C., Tabak,L.A., Schjoldager,K.T. and Ten Hagen,K.G.
  TITLE     Galnt11 regulates kidney function by glycosylating the endocytosis
            receptor megalin to modulate ligand binding
  JOURNAL   Proc Natl Acad Sci U S A 116 (50), 25196-25202 (2019)
   PUBMED   31740596
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Tian,E., Stevens,S.R., Guan,Y., Springer,D.A., Anderson,S.A.,
            Starost,M.F., Patel,V., Ten Hagen,K.G. and Tabak,L.A.
  TITLE     Galnt1 is required for normal heart valve development and cardiac
            function
  JOURNAL   PLoS One 10 (1), e0115861 (2015)
   PUBMED   25615642
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Yoshida,C.A., Kawane,T., Moriishi,T., Purushothaman,A.,
            Miyazaki,T., Komori,H., Mori,M., Qin,X., Hashimoto,A., Sugahara,K.,
            Yamana,K., Takada,K. and Komori,T.
  TITLE     Overexpression of Galnt3 in chondrocytes resulted in dwarfism due
            to the increase of mucin-type O-glycans and reduction of
            glycosaminoglycans
  JOURNAL   J Biol Chem 289 (38), 26584-26596 (2014)
   PUBMED   25107907
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Tian,E., Hoffman,M.P. and Ten Hagen,K.G.
  TITLE     O-glycosylation modulates integrin and FGF signalling by
            influencing the secretion of basement membrane components
  JOURNAL   Nat Commun 3, 869 (2012)
   PUBMED   22643896
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK043977.1, AK033638.1 and CK627557.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK156751.1, AK033638.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 25.96 cM"
     Protein         1..576
                     /product="polypeptide N-acetylgalactosaminyltransferase
                     12"
                     /EC_number="2.4.1.41"
                     /note="polypeptide GalNAc transferase 12; protein-UDP
                     acetylgalactosaminyltransferase 12; UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase 12;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 12"
                     /calculated_mol_wt=66410
     Site            20..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGT9.1)"
     Region          38..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGT9.1)"
     Region          130..239
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGT9.1)"
     Region          134..428
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(138..140,142,171,200,203,207,223..225,307..308,
                     330..331,333,358,361,366)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(223,225,358)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          299..361
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGT9.1)"
     Region          438..574
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cl49609"
                     /db_xref="CDD:483949"
     Site            order(455..457,470,472,480..481)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(503..504,512,514,523..524)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(544..546,557,559,566..567)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     CDS             1..576
                     /gene="Galnt12"
                     /gene_synonym="9130206E10; A630062B03Rik; galNAc-T12;
                     mpp-GalNAc-T12; pp-GaNTase; pp-GaNTase 12"
                     /coded_by="NM_172693.4:51..1781"
                     /db_xref="CCDS:CCDS18158.1"
                     /db_xref="GeneID:230145"
                     /db_xref="MGI:MGI:2444664"
ORIGIN      
        1 mwgravrrrc prglrrgrea llallalagl gallrarsrs gtvdpgpprt plpgrhepvl
       61 prpplpadal gahgeavrlq lqgeelrlqe esvkqhqini ylsdrislhr rlperwnplc
      121 revkydydnl pktsvviafy neawstllrt vysvletspd illeevilvd dysdrehlke
      181 rlanelsqlp kvrlirasrr eglvrarllg asaargevlt fldchceche gwlepllqri
      241 hekesavvcp vidvidwntf eylgnsgepq iggfdwrlvf twhvvpqrer qsmrspidvi
      301 rsptmagglf avskryfdyl gsydtgmevw ggenlefsfr iwqcggtlet hpcshvghvf
      361 pkqapysrsk alansvraae vwmdefkely yhrnpqarle pfgdvterkk lraklqckdf
      421 kwfldtvype lhvpedrpgf fgmlqnrglr gycldynppn enhveghqvl lylchgmgqn
      481 qffeyttrke iryntrqpea citvedgkdt lvmdlcretv penqefilqe dgtlvhkhsr
      541 kcveatekvl dngfapylrd ctnsdnqrwf fkerms
//
LOCUS       NP_001135441             740 aa            linear   PRI 27-APR-2025
DEFINITION  death domain-associated protein 6 isoform a [Homo sapiens].
ACCESSION   NP_001135441
VERSION     NP_001135441.1
DBSOURCE    REFSEQ: accession NM_001141969.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Yasunaga,Y., Tanaka,M., Arita,J., Hasegawa,K. and Ushiku,T.
  TITLE     Loss of ATRX and DAXX in pancreatic neuroendocrine tumors:
            Association with recurrence risk, cellular phenotype, and
            heterogeneity
  JOURNAL   Hum Pathol 150, 51-57 (2024)
   PUBMED   38909708
  REMARK    GeneRIF: Loss of ATRX and DAXX in pancreatic neuroendocrine tumors:
            Association with recurrence risk, cellular phenotype, and
            heterogeneity.
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Pinto,L.M., Pailas,A., Bondarchenko,M., Sharma,A.B., Neumann,K.,
            Rizzo,A.J., Jeanty,C., Nicot,N., Racca,C., Graham,M.K.,
            Naughton,C., Liu,Y., Chen,C.L., Meakin,P.J., Gilbert,N.,
            Britton,S., Meeker,A.K., Heaphy,C.M., Larminat,F. and Van Dyck,E.
  TITLE     DAXX promotes centromeric stability independently of ATRX by
            preventing the accumulation of R-loop-induced DNA double-stranded
            breaks
  JOURNAL   Nucleic Acids Res 52 (3), 1136-1155 (2024)
   PUBMED   38038252
  REMARK    GeneRIF: DAXX promotes centromeric stability independently of ATRX
            by preventing the accumulation of R-loop-induced DNA
            double-stranded breaks.
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Ding,S., Wang,H., Liao,Y., Chen,R., Hu,Y., Wu,H., Shen,H. and
            Tang,S.
  TITLE     HPV16 E7 protein antagonizes TNF-alpha-induced apoptosis of
            cervical cancer cells via Daxx/JNK pathway
  JOURNAL   Microb Pathog 185, 106423 (2023)
   PUBMED   37871853
  REMARK    GeneRIF: HPV16 E7 protein antagonizes TNF-alpha-induced apoptosis
            of cervical cancer cells via Daxx/JNK pathway.
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Ali Naeem,H., Nazar Ibraheim,W. and Abdullah Alomar,S.A.
  TITLE     The Impact of Human Mammary Tumor Virus (HMTV) on the Expression of
            Epidermal Growth Factor Receptor (EGFR) and Death-Domain Associated
            Protein (DAXX) in Breast Carcinoma Tissues
  JOURNAL   Arch Razi Inst 78 (2), 689-699 (2023)
   PUBMED   37396746
  REMARK    GeneRIF: The Impact of Human Mammary Tumor Virus (HMTV) on the
            Expression of Epidermal Growth Factor Receptor (EGFR) and
            Death-Domain Associated Protein (DAXX) in Breast Carcinoma Tissues.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Carraro,M., Hendriks,I.A., Hammond,C.M., Solis-Mezarino,V.,
            Volker-Albert,M., Elsborg,J.D., Weisser,M.B., Spanos,C.,
            Montoya,G., Rappsilber,J., Imhof,A., Nielsen,M.L. and Groth,A.
  TITLE     DAXX adds a de novo H3.3K9me3 deposition pathway to the histone
            chaperone network
  JOURNAL   Mol Cell 83 (7), 1075-1092 (2023)
   PUBMED   36868228
  REMARK    GeneRIF: DAXX adds a de novo H3.3K9me3 deposition pathway to the
            histone chaperone network.
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Chang,H.Y., Nishitoh,H., Yang,X., Ichijo,H. and Baltimore,D.
  TITLE     Activation of apoptosis signal-regulating kinase 1 (ASK1) by the
            adapter protein Daxx
  JOURNAL   Science 281 (5384), 1860-1863 (1998)
   PUBMED   9743501
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Pluta,A.F., Earnshaw,W.C. and Goldberg,I.G.
  TITLE     Interphase-specific association of intrinsic centromere protein
            CENP-C with HDaxx, a death domain-binding protein implicated in
            Fas-mediated cell death
  JOURNAL   J Cell Sci 111 (Pt 14), 2029-2041 (1998)
   PUBMED   9645950
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Herberg,J.A., Beck,S. and Trowsdale,J.
  TITLE     TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form
            a dense cluster at the centromeric end of the MHC
  JOURNAL   J Mol Biol 277 (4), 839-857 (1998)
   PUBMED   9545376
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Kiriakidou,M., Driscoll,D.A., Lopez-Guisa,J.M. and Strauss,J.F.
            3rd.
  TITLE     Cloning and expression of primate Daxx cDNAs and mapping of the
            human gene to chromosome 6p21.3 in the MHC region
  JOURNAL   DNA Cell Biol 16 (11), 1289-1298 (1997)
   PUBMED   9407001
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Yang,X., Khosravi-Far,R., Chang,H.Y. and Baltimore,D.
  TITLE     Daxx, a novel Fas-binding protein that activates JNK and apoptosis
  JOURNAL   Cell 89 (7), 1067-1076 (1997)
   PUBMED   9215629
  REMARK    GeneRIF: A partial human cDNA clone was identified by its
            interaction with murine Fas in a yeast two-hybrid screening. The
            human clone was then used to clone the murine Daxx, which was
            further characterized.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC359186.1, BC073776.1,
            AK223404.1 and BM997178.1.
            
            Summary: This gene encodes a multifunctional protein that resides
            in multiple locations in the nucleus and in the cytoplasm. It
            interacts with a wide variety of proteins, such as apoptosis
            antigen Fas, centromere protein C, and transcription factor
            erythroblastosis virus E26 oncogene homolog 1. In the nucleus, the
            encoded protein functions as a potent transcription repressor that
            binds to sumoylated transcription factors. Its repression can be
            relieved by the sequestration of this protein into promyelocytic
            leukemia nuclear bodies or nucleoli. This protein also associates
            with centromeres in G2 phase. In the cytoplasm, the encoded protein
            may function to regulate apoptosis. The subcellular localization
            and function of this protein are modulated by post-translational
            modifications, including sumoylation, phosphorylation and
            polyubiquitination. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript but encodes the shorter isoform (a). Variants 1 and 2
            encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223404.1, SRR1803614.195016.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374542.10/ ENSP00000363668.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..740
                     /product="death domain-associated protein 6 isoform a"
                     /note="death-associated protein 6; Fas-binding protein;
                     CENP-C binding protein; ETS1-associated protein 1; death
                     domain-associated protein 6; fas death domain-associated
                     protein"
                     /calculated_mol_wt=81242
     Region          1..160
                     /region_name="Necessary for interaction with USP7 and
                     ATRX"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          56..144
                     /region_name="Daxx"
                     /note="Daxx N-terminal Rassf1C-interacting domain;
                     pfam03344"
                     /db_xref="CDD:460889"
     Site            order(81,83..84,87..88,91,121..122,124..125,127..128,
                     131..132,135,140)
                     /site_type="other"
                     /note="Rassf1C interface [polypeptide binding]"
                     /db_xref="CDD:240522"
     Region          147..185
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          183..417
                     /region_name="Interaction with histone H3.3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          183..387
                     /region_name="DAXX_histone_binding"
                     /note="Histone binding domain of the death-domain
                     associated protein (DAXX); cd13150"
                     /db_xref="CDD:240523"
     Site            order(195..196,199,202..203,205..211,215..218,220..223,
                     225..226,229,232..233,236,249..251,283..287,290,317,
                     321..322,325,328,331..332,335..336,338..340,342,369,
                     372..373,376..377,379..380,383..384,387)
                     /site_type="other"
                     /note="Histone H3.3 interface [polypeptide binding]"
                     /db_xref="CDD:240523"
     Site            order(209,283,285,288,329,332..333,336,341,348..351,354,
                     357,361,364,368,371..372,375..376,379,383)
                     /site_type="other"
                     /note="Histone H4 interface [polypeptide binding]"
                     /db_xref="CDD:240523"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          347..570
                     /region_name="Necessary for interaction with USP7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          384..724
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          391..395
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O35613; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VIB2; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          501..625
                     /region_name="Interaction with MAP3K5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            512
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VIB2; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VIB2; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          626..740
                     /region_name="Interaction with SPOP.
                     /evidence=ECO:0000269|PubMed:15240113"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          627..634
                     /region_name="(Microbial infection) Interaction with
                     Puumala hantavirus nucleoprotein.
                     /evidence=ECO:0000269|PubMed:11907324"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          628..634
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          658..663
                     /region_name="(Microbial infection) Interaction with
                     Puumala hantavirus nucleoprotein.
                     /evidence=ECO:0000269|PubMed:11907324"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12968034,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Region          733..740
                     /region_name="Sumo interaction motif (SIM)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            737
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q9UER7.2)"
     CDS             1..740
                     /gene="DAXX"
                     /gene_synonym="BING2; DAP6; EAP1; SMIM40"
                     /coded_by="NM_001141969.2:151..2373"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4776.1"
                     /db_xref="GeneID:1616"
                     /db_xref="HGNC:HGNC:2681"
                     /db_xref="MIM:603186"
ORIGIN      
        1 matansiivl ddddedeaaa qpgpshplpn aaspgaeaps ssephgargs sssggkkcyk
       61 leneklfeef lelckmqtad hpevvpflyn rqqrahslfl asaefcnils rvlsrarsrp
      121 aklyvyinel ctvlkahsak kklnlapaat tsnepsgnnp pthlsldptn aentasqspr
      181 trgsrrqiqr leqllalyva eirrlqekel dlselddpds aylqearlkr klirlfgrlc
      241 elkdcssltg rvieqripyr gtrypevnrr ierlinkpgp dtfpdygdvl ravekaaarh
      301 slglprqqlq lmaqdafrdv girlqerrhl dliynfgchl tddyrpgvdp alsdpvlarr
      361 lrenrslams rldeviskya mlqdkseege rkkrrarlqg tsshsadtpe asldsgegps
      421 gmasqgcpsa sraetddedd eesdeeeeee eeeeeeeatd seeeedleqm qegqeddeee
      481 deeeeaaagk dgdkspmssl qisneknlep gkqisrssge qqnkgrivsp sllseeplap
      541 ssidaesnge qpeeltleee spvsqlfele iealpldtps svetdisssr kqseepfttv
      601 lengagmvss tsfnggvsph nwgdsgppck ksrkekkqtg sgplgnsyve rqrsvhekng
      661 kkictlpspp splaslapva dsstrvdsps hglvtsslci psparlsqtp hsqpprpgtc
      721 ktsvatqcdp eeiivlsdsd
//
LOCUS       NP_149417                356 aa            linear   PRI 27-APR-2025
DEFINITION  G patch domain and ankyrin repeat-containing protein 1 [Homo
            sapiens].
ACCESSION   NP_149417
VERSION     NP_149417.1
DBSOURCE    REFSEQ: accession NM_033177.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Harney,S.M., Vilarino-Guell,C., Adamopoulos,I.E., Sims,A.M.,
            Lawrence,R.W., Cardon,L.R., Newton,J.L., Meisel,C., Pointon,J.J.,
            Darke,C., Athanasou,N., Wordsworth,B.P. and Brown,M.A.
  TITLE     Fine mapping of the MHC Class III region demonstrates association
            of AIF1 and rheumatoid arthritis
  JOURNAL   Rheumatology (Oxford) 47 (12), 1761-1767 (2008)
   PUBMED   18835879
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Xie,T., Rowen,L., Aguado,B., Ahearn,M.E., Madan,A., Qin,S.,
            Campbell,R.D. and Hood,L.
  TITLE     Analysis of the gene-dense major histocompatibility complex class
            III region and its comparison to mouse
  JOURNAL   Genome Res 13 (12), 2621-2636 (2003)
   PUBMED   14656967
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Spies,T., Blanck,G., Bresnahan,M., Sands,J. and Strominger,J.L.
  TITLE     A new cluster of genes within the human major histocompatibility
            complex
  JOURNAL   Science 243 (4888), 214-217 (1989)
   PUBMED   2911734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC018875.2, AK123707.1 and
            AL662899.5.
            
            Summary: This gene is located in a cluster of HLA-B-associated
            transcripts, which is included in the human major
            histocompatability complex III region. This gene encodes a protein
            which is thought to play a role in immunity. Multiple alternatively
            spliced variants, encoding the same protein, have been identified.
            [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, 4, and 5 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.127969.1, BC008783.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375896.9/ ENSP00000365060.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..356
                     /product="G patch domain and ankyrin repeat-containing
                     protein 1"
                     /note="G patch domain containing 10; protein BAT4; G patch
                     domain and ankyrin repeats-containing protein 1; protein
                     G5; HLA-B-associated transcript 4; g patch
                     domain-containing protein 10; ankyrin repeat
                     domain-containing protein 59"
                     /calculated_mol_wt=39183
     Region          1..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95872.1)"
     Region          <111..198
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          111..141
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O95872.1)"
     Site            order(113..115,117..118,122,125,140,142,144,148..149,
                     152..154,156..157,161,164,174,176,178,182..183,186..188,
                     190..191,195)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          142..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          142..172
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O95872.1)"
     Region          256..299
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     CDS             1..356
                     /gene="GPANK1"
                     /gene_synonym="ANKRD59; BAT4; D6S54E; G5; GPATCH10"
                     /coded_by="NM_033177.4:257..1327"
                     /db_xref="CCDS:CCDS4711.1"
                     /db_xref="GeneID:7918"
                     /db_xref="HGNC:HGNC:13920"
                     /db_xref="MIM:142610"
ORIGIN      
        1 msrpllitft patdpsdlwk dgqqqpqpek pestldgaaa rafyealigd essapdsqrs
       61 qteparerkr kkrrimkapa aeavaegasg rhgqgrslea edkmthrilr aaqegdlpel
      121 rrllepheag gaggninard afwwtplmca aragqgaavs yllgrgaawv gvcelsgrda
      181 aqlaeeagfp evarmvresh getrspenrs ptpslqycen cdthfqdsnh rtstahllsl
      241 sqgpqppnlp lgvpisspgf klllrggwep gmglgprgeg ranpiptvlk rdqeglgyrs
      301 apqprvthfp awdtravagr erpprvatls wreerrreek drawerdlrt ymnlef
//
LOCUS       NP_444512                132 aa            linear   PRI 27-APR-2025
DEFINITION  SH2 domain-containing protein 1B [Homo sapiens].
ACCESSION   NP_444512
VERSION     NP_444512.2
DBSOURCE    REFSEQ: accession NM_053282.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Taha,M., Nezerwa,E. and Nam,H.J.
  TITLE     The X-ray Crystallographic Structure of Human EAT2 (SH2D1B)
  JOURNAL   Protein Pept Lett 23 (10), 862-866 (2016)
   PUBMED   27586300
  REMARK    GeneRIF: When compared with SAP, the other single SH2 domain
            protein in human, EAT2 shows similar binding energies to
            unphosphorylated ligands. This is inconsistent to the previous data
            showing low affinity of EAT2 toward unphosphorylated peptides
            compared to SAP which shows high affinity
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Arking,D.E., Pulit,S.L., Crotti,L., van der Harst,P., Munroe,P.B.,
            Koopmann,T.T., Sotoodehnia,N., Rossin,E.J., Morley,M., Wang,X.,
            Johnson,A.D., Lundby,A., Gudbjartsson,D.F., Noseworthy,P.A.,
            Eijgelsheim,M., Bradford,Y., Tarasov,K.V., Dorr,M.,
            Muller-Nurasyid,M., Lahtinen,A.M., Nolte,I.M., Smith,A.V.,
            Bis,J.C., Isaacs,A., Newhouse,S.J., Evans,D.S., Post,W.S.,
            Waggott,D., Lyytikainen,L.P., Hicks,A.A., Eisele,L., Ellinghaus,D.,
            Hayward,C., Navarro,P., Ulivi,S., Tanaka,T., Tester,D.J.,
            Chatel,S., Gustafsson,S., Kumari,M., Morris,R.W., Naluai,A.T.,
            Padmanabhan,S., Kluttig,A., Strohmer,B., Panayiotou,A.G.,
            Torres,M., Knoflach,M., Hubacek,J.A., Slowikowski,K.,
            Raychaudhuri,S., Kumar,R.D., Harris,T.B., Launer,L.J.,
            Shuldiner,A.R., Alonso,A., Bader,J.S., Ehret,G., Huang,H.,
            Kao,W.H., Strait,J.B., Macfarlane,P.W., Brown,M., Caulfield,M.J.,
            Samani,N.J., Kronenberg,F., Willeit,J., Smith,J.G., Greiser,K.H.,
            Meyer Zu Schwabedissen,H., Werdan,K., Carella,M., Zelante,L.,
            Heckbert,S.R., Psaty,B.M., Rotter,J.I., Kolcic,I., Polasek,O.,
            Wright,A.F., Griffin,M., Daly,M.J., Arnar,D.O., Holm,H.,
            Thorsteinsdottir,U., Denny,J.C., Roden,D.M., Zuvich,R.L.,
            Emilsson,V., Plump,A.S., Larson,M.G., O'Donnell,C.J., Yin,X.,
            Bobbo,M., D'Adamo,A.P., Iorio,A., Sinagra,G., Carracedo,A.,
            Cummings,S.R., Nalls,M.A., Jula,A., Kontula,K.K., Marjamaa,A.,
            Oikarinen,L., Perola,M., Porthan,K., Erbel,R., Hoffmann,P.,
            Jockel,K.H., Kalsch,H., Nothen,M.M., den Hoed,M., Loos,R.J.,
            Thelle,D.S., Gieger,C., Meitinger,T., Perz,S., Peters,A.,
            Prucha,H., Sinner,M.F., Waldenberger,M., de Boer,R.A., Franke,L.,
            van der Vleuten,P.A., Beckmann,B.M., Martens,E., Bardai,A.,
            Hofman,N., Wilde,A.A., Behr,E.R., Dalageorgou,C., Giudicessi,J.R.,
            Medeiros-Domingo,A., Barc,J., Kyndt,F., Probst,V., Ghidoni,A.,
            Insolia,R., Hamilton,R.M., Scherer,S.W., Brandimarto,J.,
            Margulies,K., Moravec,C.E., del Greco,M. F, Fuchsberger,C.,
            O'Connell,J.R., Lee,W.K., Watt,G.C., Campbell,H., Wild,S.H., El
            Mokhtari,N.E., Frey,N., Asselbergs,F.W., Mateo Leach,I., Navis,G.,
            van den Berg,M.P., van Veldhuisen,D.J., Kellis,M., Krijthe,B.P.,
            Franco,O.H., Hofman,A., Kors,J.A., Uitterlinden,A.G.,
            Witteman,J.C., Kedenko,L., Lamina,C., Oostra,B.A., Abecasis,G.R.,
            Lakatta,E.G., Mulas,A., Orru,M., Schlessinger,D., Uda,M.,
            Markus,M.R., Volker,U., Snieder,H., Spector,T.D., Arnlov,J.,
            Lind,L., Sundstrom,J., Syvanen,A.C., Kivimaki,M., Kahonen,M.,
            Mononen,N., Raitakari,O.T., Viikari,J.S., Adamkova,V., Kiechl,S.,
            Brion,M., Nicolaides,A.N., Paulweber,B., Haerting,J.,
            Dominiczak,A.F., Nyberg,F., Whincup,P.H., Hingorani,A.D.,
            Schott,J.J., Bezzina,C.R., Ingelsson,E., Ferrucci,L., Gasparini,P.,
            Wilson,J.F., Rudan,I., Franke,A., Muhleisen,T.W., Pramstaller,P.P.,
            Lehtimaki,T.J., Paterson,A.D., Parsa,A., Liu,Y., van Duijn,C.M.,
            Siscovick,D.S., Gudnason,V., Jamshidi,Y., Salomaa,V., Felix,S.B.,
            Sanna,S., Ritchie,M.D., Stricker,B.H., Stefansson,K., Boyer,L.A.,
            Cappola,T.P., Olsen,J.V., Lage,K., Schwartz,P.J., Kaab,S.,
            Chakravarti,A., Ackerman,M.J., Pfeufer,A., de Bakker,P.I. and
            Newton-Cheh,C.
  CONSRTM   CARe Consortium; COGENT Consortium; DCCT/EDIC; eMERGE Consortium;
            HRGEN Consortium
  TITLE     Genetic association study of QT interval highlights role for
            calcium signaling pathways in myocardial repolarization
  JOURNAL   Nat Genet 46 (8), 826-836 (2014)
   PUBMED   24952745
REFERENCE   6  (residues 1 to 132)
  AUTHORS   Veillette,A. and Latour,S.
  TITLE     The SLAM family of immune-cell receptors
  JOURNAL   Curr Opin Immunol 15 (3), 277-285 (2003)
   PUBMED   12787752
  REMARK    Review article
REFERENCE   7  (residues 1 to 132)
  AUTHORS   Tangye,S.G., van de Weerdt,B.C., Avery,D.T. and Hodgkin,P.D.
  TITLE     CD84 is up-regulated on a major population of human memory B cells
            and recruits the SH2 domain containing proteins SAP and EAT-2
  JOURNAL   Eur J Immunol 32 (6), 1640-1649 (2002)
   PUBMED   12115647
REFERENCE   8  (residues 1 to 132)
  AUTHORS   Morra,M., Lu,J., Poy,F., Martin,M., Sayos,J., Calpe,S., Gullo,C.,
            Howie,D., Rietdijk,S., Thompson,A., Coyle,A.J., Denny,C.,
            Yaffe,M.B., Engel,P., Eck,M.J. and Terhorst,C.
  TITLE     Structural basis for the interaction of the free SH2 domain EAT-2
            with SLAM receptors in hematopoietic cells
  JOURNAL   EMBO J 20 (21), 5840-5852 (2001)
   PUBMED   11689425
REFERENCE   9  (residues 1 to 132)
  AUTHORS   Morra,M., Howie,D., Grande,M.S., Sayos,J., Wang,N., Wu,C., Engel,P.
            and Terhorst,C.
  TITLE     X-linked lymphoproliferative disease: a progressive
            immunodeficiency
  JOURNAL   Annu Rev Immunol 19, 657-682 (2001)
   PUBMED   11244050
  REMARK    Review article
REFERENCE   10 (residues 1 to 132)
  AUTHORS   Thompson,A.D., Braun,B.S., Arvand,A., Stewart,S.D., May,W.A.,
            Chen,E., Korenberg,J. and Denny,C.
  TITLE     EAT-2 is a novel SH2 domain containing protein that is up regulated
            by Ewing's sarcoma EWS/FLI1 fusion gene
  JOURNAL   Oncogene 13 (12), 2649-2658 (1996)
   PUBMED   9000139
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL512785.7.
            
            On Oct 29, 2004 this sequence version replaced NP_444512.1.
            
            Summary: By binding phosphotyrosines through its free SRC (MIM
            190090) homology-2 (SH2) domain, EAT2 regulates signal transduction
            through receptors expressed on the surface of antigen-presenting
            cells (Morra et al., 2001 [PubMed 11689425]).[supplied by OMIM, Mar
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF484964.1, AK097162.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367929.3/ ENSP00000356906.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..132
                     /product="SH2 domain-containing protein 1B"
                     /note="SH2 domain-containing molecule EAT2; EAT-2;
                     EWS/FLI1-activated transcript 2"
                     /calculated_mol_wt=15166
     Region          1..103
                     /region_name="SH2_SAP1"
                     /note="Src homology 2 (SH2) domain found in
                     SLAM-associated protein (SAP)1; cd10342"
                     /db_xref="CDD:198205"
     Site            order(12,31,54)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198205"
     Site            order(52..53,65..66,71,90..92)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198205"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:24687958; propagated from
                     UniProtKB/Swiss-Prot (O14796.2)"
     CDS             1..132
                     /gene="SH2D1B"
                     /gene_synonym="EAT2"
                     /coded_by="NM_053282.5:121..519"
                     /db_xref="CCDS:CCDS30928.1"
                     /db_xref="GeneID:117157"
                     /db_xref="HGNC:HGNC:30416"
                     /db_xref="MIM:608510"
ORIGIN      
        1 mdlpyyhgrl tkqdcetlll kegvdgnfll rdsesipgvl clcvsfkniv ytyrifrekh
       61 gyyriqtaeg spkqvfpslk eliskfekpn qgmvvhllkp ikrtspslrw rglkleletf
      121 vnsnsdyvdv lp
//
LOCUS       NP_001349833             268 aa            linear   ROD 27-APR-2025
DEFINITION  protein artemis isoform 7 [Mus musculus].
ACCESSION   NP_001349833
VERSION     NP_001349833.1
DBSOURCE    REFSEQ: accession NM_001362904.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Collins,P.L., Purman,C., Porter,S.I., Nganga,V., Saini,A.,
            Hayer,K.E., Gurewitz,G.L., Sleckman,B.P., Bednarski,J.J.,
            Bassing,C.H. and Oltz,E.M.
  TITLE     DNA double-strand breaks induce H2Ax phosphorylation domains in a
            contact-dependent manner
  JOURNAL   Nat Commun 11 (1), 3158 (2020)
   PUBMED   32572033
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Liu,X., Wang,X.S., Lee,B.J., Wu-Baer,F.K., Lin,X., Shao,Z.,
            Estes,V.M., Gautier,J., Baer,R. and Zha,S.
  TITLE     CtIP is essential for early B cell proliferation and development in
            mice
  JOURNAL   J Exp Med 216 (7), 1648-1663 (2019)
   PUBMED   31097467
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Spehalski,E., Capper,K.M., Smith,C.J., Morgan,M.J., Dinkelmann,M.,
            Buis,J., Sekiguchi,J.M. and Ferguson,D.O.
  TITLE     MRE11 Promotes Tumorigenesis by Facilitating Resistance to
            Oncogene-Induced Replication Stress
  JOURNAL   Cancer Res 77 (19), 5327-5338 (2017)
   PUBMED   28819025
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Jiang,W., Crowe,J.L., Liu,X., Nakajima,S., Wang,Y., Li,C.,
            Lee,B.J., Dubois,R.L., Liu,C., Yu,X., Lan,L. and Zha,S.
  TITLE     Differential phosphorylation of DNA-PKcs regulates the interplay
            between end-processing and end-ligation during nonhomologous
            end-joining
  JOURNAL   Mol Cell 58 (1), 172-185 (2015)
   PUBMED   25818648
  REMARK    GeneRIF: ATM phosphorylates DNA-PKcs to recruit Artemis and promote
            end-processing.
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Desai,A. and Gerson,S.
  TITLE     Exo1 independent DNA mismatch repair involves multiple compensatory
            nucleases
  JOURNAL   DNA Repair (Amst) 21, 55-64 (2014)
   PUBMED   25037770
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Yan,Y., Akhter,S., Zhang,X. and Legerski,R.
  TITLE     The multifunctional SNM1 gene family: not just nucleases
  JOURNAL   Future Oncol 6 (6), 1015-1029 (2010)
   PUBMED   20528238
  REMARK    Review article
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Mills,K.D., Ferguson,D.O. and Alt,F.W.
  TITLE     The role of DNA breaks in genomic instability and tumorigenesis
  JOURNAL   Immunol Rev 194, 77-95 (2003)
   PUBMED   12846809
  REMARK    Review article
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Rooney,S., Alt,F.W., Lombard,D., Whitlow,S., Eckersdorff,M.,
            Fleming,J., Fugmann,S., Ferguson,D.O., Schatz,D.G. and Sekiguchi,J.
  TITLE     Defective DNA repair and increased genomic instability in
            Artemis-deficient murine cells
  JOURNAL   J Exp Med 197 (5), 553-565 (2003)
   PUBMED   12615897
  REMARK    GeneRIF: Data show that Artemis appears to be required for a subset
            of nonhomologous DNA end joining reactions that require end
            processing [Artemis].
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Rooney,S., Sekiguchi,J., Zhu,C., Cheng,H.L., Manis,J., Whitlow,S.,
            DeVido,J., Foy,D., Chaudhuri,J., Lombard,D. and Alt,F.W.
  TITLE     Leaky Scid phenotype associated with defective V(D)J coding end
            processing in Artemis-deficient mice
  JOURNAL   Mol Cell 10 (6), 1379-1390 (2002)
   PUBMED   12504013
  REMARK    GeneRIF: deficient mice have a phenotype similar to that of
            DNA-PKcs-deficient mice-including severe combined immunodeficiency
            associated with defects in opening and joining V(D)J coding hairpin
            ends and increased cellular ionizing radiation sensitivity
            (artemis)
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL732620.14 and AK038788.1.
            
            Summary: This gene encodes a member of the SNM1 family of nucleases
            and is involved in V(D)J recombination and DNA repair. This protein
            has single-strand-specific 5'-3' exonuclease activity; it also
            exhibits endonuclease activity on 5' and 3' overhangs and hairpins.
            The protein also functions in the regulation of the cell cycle in
            response to DNA damage. Homozygous knockout mice for this gene
            exhibit severe combined immunodeficiency with sensitivity to
            ionizing radiation. Mutations in this gene in humans can cause
            Athabascan-type severe combined immunodeficiency (SCIDA) and Omenn
            syndrome. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Nov
            2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK038788.1, SRR7345562.2306779.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            multifunctional gene product(s) :: PMID: 20528238
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 1.93 cM"
     Protein         1..268
                     /product="protein artemis isoform 7"
                     /note="protein artemis; SNM1-like protein; DNA cross-link
                     repair 1C protein; DNA cross-link repair 1A, PSO2 homolog;
                     DNA cross-link repair 1C, PSO2 homolog"
                     /calculated_mol_wt=30742
     Region          1..171
                     /region_name="artemis-SNM1C-like_MBL-fold"
                     /note="artemis-SNM1C and related proteins; MBL-fold
                     metallo-hydrolase domain; cd16297"
                     /db_xref="CDD:293855"
     Site            order(33,35,37..38,115..116,136,166)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293855"
     CDS             1..268
                     /gene="Dclre1c"
                     /gene_synonym="9930121L06Rik; Art; Snm1l"
                     /coded_by="NM_001362904.1:88..894"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:227525"
                     /db_xref="MGI:MGI:2441769"
ORIGIN      
        1 mssfqgqmae yptisidrfd renlkarayf lshchkdhmk glrapslkrr lecslkvfly
       61 cspvtkelll tspkyrfwen riitieietp tqislvdeas gekeevvvtl lpaghcpgsv
      121 mflfqgsngt vlytgdfrla kgeasrmell hsggrvkdiq svyldttfcd prfyqipsre
      181 qclrgilelv rswvtrsphh vvwlnckaay gyeylftnls eelgvqvhvd kldmfknmpd
      241 ilhhlttdrn tqihacrhpk vlgkhprd
//
LOCUS       NP_001352522             816 aa            linear   PRI 27-APR-2025
DEFINITION  neuroligin-4, Y-linked isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001352522 XP_016885526
VERSION     NP_001352522.1
DBSOURCE    REFSEQ: accession NM_001365593.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Nguyen,T.A., Wu,K., Pandey,S., Lehr,A.W., Li,Y., Bemben,M.A.,
            Badger,J.D. 2nd, Lauzon,J.L., Wang,T., Zaghloul,K.A., Thurm,A.,
            Jain,M., Lu,W. and Roche,K.W.
  TITLE     A Cluster of Autism-Associated Variants on X-Linked NLGN4X
            Functionally Resemble NLGN4Y
  JOURNAL   Neuron 106 (5), 759-768 (2020)
   PUBMED   32243781
  REMARK    GeneRIF: A Cluster of Autism-Associated Variants on X-Linked NLGN4X
            Functionally Resemble NLGN4Y.
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Bogaert,A.F., Skorska,M.N., Wang,C., Gabrie,J., MacNeil,A.J.,
            Hoffarth,M.R., VanderLaan,D.P., Zucker,K.J. and Blanchard,R.
  TITLE     Male homosexuality and maternal immune responsivity to the Y-linked
            protein NLGN4Y
  JOURNAL   Proc Natl Acad Sci U S A 115 (2), 302-306 (2018)
   PUBMED   29229842
  REMARK    GeneRIF: Results suggest an association between a maternal immune
            response to neuroligin 4 Y-linked (NLGN4Y) and subsequent sexual
            orientation in male offspring.
            Erratum:[Proc Natl Acad Sci U S A. 2022 Aug 23;119(34):e2212767119.
            doi: 10.1073/pnas.2212767119. PMID: 35981140]
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Gong,Y., Wang,L., Chippada-Venkata,U., Dai,X., Oh,W.K. and Zhu,J.
  TITLE     Constructing Bayesian networks by integrating gene expression and
            copy number data identifies NLGN4Y as a novel regulator of prostate
            cancer progression
  JOURNAL   Oncotarget 7 (42), 68688-68707 (2016)
   PUBMED   27626693
  REMARK    GeneRIF: Results suggest that NLGN4Y is an important negative
            regulator in prostate cancer progression.
REFERENCE   4  (residues 1 to 816)
  AUTHORS   Ross,J.L., Tartaglia,N., Merry,D.E., Dalva,M. and Zinn,A.R.
  TITLE     Behavioral phenotypes in males with XYY and possible role of
            increased NLGN4Y expression in autism features
  JOURNAL   Genes Brain Behav 14 (2), 137-144 (2015)
   PUBMED   25558953
  REMARK    GeneRIF: Expression of NLGN4Y, a gene that may be involved in
            synaptic function, is increased in boys with XYY
REFERENCE   5  (residues 1 to 816)
  AUTHORS   Dinamarca,M.C., Weinstein,D., Monasterio,O. and Inestrosa,N.C.
  TITLE     The synaptic protein neuroligin-1 interacts with the amyloid
            beta-peptide. Is there a role in Alzheimer's disease?
  JOURNAL   Biochemistry 50 (38), 8127-8137 (2011)
   PUBMED   21838267
REFERENCE   6  (residues 1 to 816)
  AUTHORS   Yamakawa,H., Oyama,S., Mitsuhashi,H., Sasagawa,N., Uchino,S.,
            Kohsaka,S. and Ishiura,S.
  TITLE     Neuroligins 3 and 4X interact with syntrophin-gamma2, and the
            interactions are affected by autism-related mutations
  JOURNAL   Biochem Biophys Res Commun 355 (1), 41-46 (2007)
   PUBMED   17292328
REFERENCE   7  (residues 1 to 816)
  AUTHORS   Ylisaukko-oja,T., Rehnstrom,K., Auranen,M., Vanhala,R., Alen,R.,
            Kempas,E., Ellonen,P., Turunen,J.A., Makkonen,I., Riikonen,R.,
            Nieminen-von Wendt,T., von Wendt,L., Peltonen,L. and Jarvela,I.
  TITLE     Analysis of four neuroligin genes as candidates for autism
  JOURNAL   Eur J Hum Genet 13 (12), 1285-1292 (2005)
   PUBMED   16077734
  REMARK    GeneRIF: Neuroligin mutations most probably represent rare causes
            of autism; it is unlikely that the allelic variants in any of these
            genes would be major risk factors for autism.
REFERENCE   8  (residues 1 to 816)
  AUTHORS   Skaletsky,H., Kuroda-Kawaguchi,T., Minx,P.J., Cordum,H.S.,
            Hillier,L., Brown,L.G., Repping,S., Pyntikova,T., Ali,J., Bieri,T.,
            Chinwalla,A., Delehaunty,A., Delehaunty,K., Du,H., Fewell,G.,
            Fulton,L., Fulton,R., Graves,T., Hou,S.F., Latrielle,P.,
            Leonard,S., Mardis,E., Maupin,R., McPherson,J., Miner,T., Nash,W.,
            Nguyen,C., Ozersky,P., Pepin,K., Rock,S., Rohlfing,T., Scott,K.,
            Schultz,B., Strong,C., Tin-Wollam,A., Yang,S.P., Waterston,R.H.,
            Wilson,R.K., Rozen,S. and Page,D.C.
  TITLE     The male-specific region of the human Y chromosome is a mosaic of
            discrete sequence classes
  JOURNAL   Nature 423 (6942), 825-837 (2003)
   PUBMED   12815422
REFERENCE   9  (residues 1 to 816)
  AUTHORS   Jamain,S., Quach,H., Betancur,C., Rastam,M., Colineaux,C.,
            Gillberg,I.C., Soderstrom,H., Giros,B., Leboyer,M., Gillberg,C. and
            Bourgeron,T.
  CONSRTM   Paris Autism Research International Sibpair Study
  TITLE     Mutations of the X-linked genes encoding neuroligins NLGN3 and
            NLGN4 are associated with autism
  JOURNAL   Nat Genet 34 (1), 27-29 (2003)
   PUBMED   12669065
REFERENCE   10 (residues 1 to 816)
  AUTHORS   Cantallops,I. and Cline,H.T.
  TITLE     Synapse formation: if it looks like a duck and quacks like a duck
            ...
  JOURNAL   Curr Biol 10 (17), R620-R623 (2000)
   PUBMED   10996085
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010726.4, AC010979.3,
            AC010879.2 and AC011903.4.
            
            On Sep 5, 2018 this sequence version replaced XP_016885526.1.
            
            Summary: This gene encodes a type I membrane protein that belongs
            to the family of neuroligins, which are cell adhesion molecules
            present at the postsynaptic side of the synapse, and may be
            essential for the formation of functional synapses. Alternatively
            spliced transcript variants have been found for this gene.[provided
            by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.124723.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153427, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..816
                     /product="neuroligin-4, Y-linked isoform 1 precursor"
                     /note="alternative HNL4Y"
                     /calculated_mol_wt=87194
     sig_peptide     1..43
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ3.1)"
                     /calculated_mol_wt=4845
     mat_peptide     44..816
                     /product="Neuroligin-4, Y-linked. /id=PRO_0000008649"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ3.1)"
                     /calculated_mol_wt=87194
     Region          44..590
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     Site            order(174..176,253..255,258,399,405..406,444,490,493)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(254,375,489)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Region          359..364
                     /region_name="Interaction with NRXN1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     Site            511
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     Region          636..659
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     Site            677..697
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     Site            712
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62889; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     CDS             1..816
                     /gene="NLGN4Y"
                     /gene_synonym="HNL4Y"
                     /coded_by="NM_001365593.1:141..2591"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 12"
                     /db_xref="CCDS:CCDS14788.1"
                     /db_xref="GeneID:22829"
                     /db_xref="HGNC:HGNC:15529"
                     /db_xref="MIM:400028"
ORIGIN      
        1 mlrpqgllwl pllftsvcvm lnsnvllwit alaikftlid sqaqypvvnt nygkiqglrt
       61 plpseilgpv eqylgvpyas pptgerrfqp pespsswtgi rnatqfsavc pqhlderfll
      121 hdmlpiwftt sldtlmtyvq dqnedclyln iyvpmeddih eqnskkpvmv yihggsymeg
      181 tgnmidgsil asygnvivit inyrlgilgf lstgdqaakg nyglldqiqa lrwieenvga
      241 fggdpkrvti fgsgagascv slltlshyse glfqkaiiqs gtalsswavn yqpakytril
      301 adkvgcnmld ttdmveclkn knykeliqqt itpatyhiaf gpvidgdvip ddpqilmeqg
      361 eflnydimlg vnqgeglkfv dgivdnedgv tpndfdfsvs nfvdnlygyp egkdtlreti
      421 kfmytdwadk enpetrrktl valftdhqwv apavatadlh aqygsptyfy afyhhcqsem
      481 kpswadsahg devpyvfgip migptelfsc nfskndvmls avvmtywtnf aktgdpnqpv
      541 pqdtkfihtk pnrfeevaws kynpkdqlyl higlkprvrd hyratkvafw lelvphlhnl
      601 neifqyvstt tkvpppdmts fpygtrrspa kiwpttkrpa itpannpkhs kdphktgped
      661 ttvlietkrd ystelsvtia vgasllflni lafaalyykk dkrrhethrh pspqrnttnd
      721 ithiqneeim slqmkqlehd heceslqahd tlrltcppdy tltlrrspdd ipfmtpntit
      781 mipntlmgmq plhtfktfsg gqnstnlphg hsttrv
//
LOCUS       NP_055496               1143 aa            linear   PRI 27-APR-2025
DEFINITION  probable ATP-dependent RNA helicase DHX34 [Homo sapiens].
ACCESSION   NP_055496
VERSION     NP_055496.2
DBSOURCE    REFSEQ: accession NM_014681.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Hug,N., Aitken,S., Longman,D., Raab,M., Armes,H., Mann,A.R.,
            Rio-Machin,A., Fitzgibbon,J., Rouault-Pierre,K. and Caceres,J.F.
  TITLE     A dual role for the RNA helicase DHX34 in NMD and pre-mRNA splicing
            and its function in hematopoietic differentiation
  JOURNAL   RNA 28 (9), 1224-1238 (2022)
   PUBMED   35768279
  REMARK    GeneRIF: A dual role for the RNA helicase DHX34 in NMD and pre-mRNA
            splicing and its function in hematopoietic differentiation.
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Lopez-Perrote,A., Hug,N., Gonzalez-Corpas,A., Rodriguez,C.F.,
            Serna,M., Garcia-Martin,C., Boskovic,J., Fernandez-Leiro,R.,
            Caceres,J.F. and Llorca,O.
  TITLE     Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated
            mRNA decay factor DHX34, as evidenced by Cryo-EM
  JOURNAL   Elife 9, e63042 (2020)
   PUBMED   33205750
  REMARK    GeneRIF: Regulation of RUVBL1-RUVBL2 AAA-ATPases by the
            nonsense-mediated mRNA decay factor DHX34, as evidenced by Cryo-EM.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1143)
  AUTHORS   Paine,I., Posey,J.E., Grochowski,C.M., Jhangiani,S.N.,
            Rosenheck,S., Kleyner,R., Marmorale,T., Yoon,M., Wang,K.,
            Robison,R., Cappuccio,G., Pinelli,M., Magli,A., Coban Akdemir,Z.,
            Hui,J., Yeung,W.L., Wong,B.K.Y., Ortega,L., Bekheirnia,M.R.,
            Bierhals,T., Hempel,M., Johannsen,J., Santer,R., Aktas,D.,
            Alikasifoglu,M., Bozdogan,S., Aydin,H., Karaca,E., Bayram,Y.,
            Ityel,H., Dorschner,M., White,J.J., Wilichowski,E., Wortmann,S.B.,
            Casella,E.B., Kitajima,J.P., Kok,F., Monteiro,F., Muzny,D.M.,
            Bamshad,M., Gibbs,R.A., Sutton,V.R., Van Esch,H.,
            Brunetti-Pierri,N., Hildebrandt,F., Brautbar,A., Van den
            Veyver,I.B., Glass,I., Lessel,D., Lyon,G.J. and Lupski,J.R.
  CONSRTM   University of Washington Center for Mendelian Genomics,
            Baylor-Hopkins Center for Mendelian Genomics, Telethon Undiagnosed
            Diseases Program
  TITLE     Paralog Studies Augment Gene Discovery: DDX and DHX Genes
  JOURNAL   Am J Hum Genet 105 (2), 302-316 (2019)
   PUBMED   31256877
  REMARK    GeneRIF: Missense mutation in DHX34 gene is associated with
            neurodevelopmental disorder.
REFERENCE   5  (residues 1 to 1143)
  AUTHORS   Melero,R., Hug,N., Lopez-Perrote,A., Yamashita,A., Caceres,J.F. and
            Llorca,O.
  TITLE     The RNA helicase DHX34 functions as a scaffold for SMG1-mediated
            UPF1 phosphorylation
  JOURNAL   Nat Commun 7, 10585 (2016)
   PUBMED   26841701
  REMARK    GeneRIF: DHX34 activates nonsense-mediated mRNA decay by
            functioning as a scaffold for SMG1-mediated UPF1 phosphorylation
            via complex formation with SMG1 and UPF1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1143)
  AUTHORS   Hug,N. and Caceres,J.F.
  TITLE     The RNA helicase DHX34 activates NMD by promoting a transition from
            the surveillance to the decay-inducing complex
  JOURNAL   Cell Rep 8 (6), 1845-1856 (2014)
   PUBMED   25220460
  REMARK    GeneRIF: DHX34 promotes mRNP remodeling and triggers the conversion
            from the SURF complex to the DECID complex resulting in NMD
            activation.
REFERENCE   7  (residues 1 to 1143)
  AUTHORS   Longman,D., Hug,N., Keith,M., Anastasaki,C., Patton,E.E., Grimes,G.
            and Caceres,J.F.
  TITLE     DHX34 and NBAS form part of an autoregulatory NMD circuit that
            regulates endogenous RNA targets in human cells, zebrafish and
            Caenorhabditis elegans
  JOURNAL   Nucleic Acids Res 41 (17), 8319-8331 (2013)
   PUBMED   23828042
  REMARK    GeneRIF: DHX34 and NBAS act in concert with core nonsense-mediated
            mRNA decay factors to co-regulate a large number of endogenous RNA
            targets.
REFERENCE   8  (residues 1 to 1143)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   9  (residues 1 to 1143)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 1143)
  AUTHORS   Smith,J.S., Tachibana,I., Pohl,U., Lee,H.K., Thanarajasingam,U.,
            Portier,B.P., Ueki,K., Ramaswamy,S., Billings,S.J.,
            Mohrenweiser,H.W., Louis,D.N. and Jenkins,R.B.
  TITLE     A transcript map of the chromosome 19q-arm glioma tumor suppressor
            region
  JOURNAL   Genomics 64 (1), 44-50 (2000)
   PUBMED   10708517
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI826597.1, CN307402.1,
            DR762320.1, CF125648.1, AK297692.1 and BU732557.1.
            
            On Nov 4, 2003 this sequence version replaced NP_055496.1.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this DEAD box
            protein family are believed to be involved in embryogenesis,
            spermatogenesis, and cellular growth and division. This gene
            encodes a member of this family. It is mapped to the glioma 19q
            tumor suppressor region and is a tumor suppressor candidate gene.
            [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.129868.1,
                                           SRR1803613.168126.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000328771.9/ ENSP00000331907.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..1143
                     /product="probable ATP-dependent RNA helicase DHX34"
                     /EC_number="3.6.4.13"
                     /note="DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 34;
                     probable ATP-dependent helicase DHX34; DEAH box protein
                     34; DEAH (Asp-Glu-Ala-His) box polypeptide 34; DEAH-box
                     helicase 34"
                     /calculated_mol_wt=127989
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14147.2)"
     Region          75..94
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14147.2)"
     Region          160..>624
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
     Region          279..282
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14147.2)"
     Region          701..955
                     /region_name="Negatively regulates interaction with UPF1.
                     /evidence=ECO:0000269|PubMed:26841701"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14147.2)"
     Region          724..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14147.2)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14147.2)"
     Site            750
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14147.2)"
     Region          800..911
                     /region_name="OB_NTP_bind"
                     /note="Oligonucleotide/oligosaccharide-binding (OB)-fold;
                     pfam07717"
                     /db_xref="CDD:400182"
     Region          810..1143
                     /region_name="Required for phosphorylation of UPF1. Not
                     required for interaction with UPF1.
                     /evidence=ECO:0000269|PubMed:26841701"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14147.2)"
     Region          957..1143
                     /region_name="Required for the interaction with SMG1 and
                     subsequent phosphorylation of UPF1.
                     /evidence=ECO:0000269|PubMed:26841701"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14147.2)"
     CDS             1..1143
                     /gene="DHX34"
                     /gene_synonym="DDX34; HRH1"
                     /coded_by="NM_014681.6:316..3747"
                     /db_xref="CCDS:CCDS12700.1"
                     /db_xref="GeneID:9704"
                     /db_xref="HGNC:HGNC:16719"
                     /db_xref="MIM:615475"
ORIGIN      
        1 mppprtregr drrdhhraps eeealekwdw ncpetrrlle daffreedyi rqgseecqkf
       61 wtfferlqrf qnlktsrkee kdpgqpkhsi paladlprty dpryrinlsv lgpatrgsqg
      121 lgrhlpaerv aefrrallhy ldfgqkqafg rlaklqrera alpiaqygnr ilqtlkehqv
      181 vvvagdtgcg kstqvpqyll aagfshvact qprriacisl akrvgfesls qygsqvgyqi
      241 rfestrsaat kivfltvgll lrqiqrepsl pqyevlivde vherhlhndf llgvlqrllp
      301 trpdlkvilm satinislfs syfsnapvvq vpgrlfpitv vyqpqeaept tsksekldpr
      361 pflrvlesid hkyppeergd llvflsgmae isavleaaqt yashtqrwvv lplhsalsva
      421 dqdkvfdvap pgvrkcilst niaetsvtid girfvvdsgk vkemsydpqa klqrlqefwi
      481 sqasaeqrkg ragrtgpgvc frlyaesdyd afapypvpei rrvaldslvl qmksmsvgdp
      541 rtfpfieppp pasletaily lrdqgaldss ealtpigsll aqlpvdvvig kmlilgsmfs
      601 lvepvltiaa alsvqspftr saqsspecaa arrplesdqg dpftlfnvfn awvqvksers
      661 rnsrkwcrrr gieehrlyem anlrrqfkel ledhgllaga qaaqvgdsys rlqqrrerra
      721 lhqlkrqhee gagrrrkvlr lqeeqdggss dedragpapp gasdgvdiqd vkfklrhdla
      781 qlqaaassaq dlsreqlall klvlgrglyp qlavpdafns srkdsdqifh tqakqgavlh
      841 ptcvfagspe vlhaqeleas ncdgsrddkd kmsskhqlls fvslletnkp ylvncvripa
      901 lqslllfsrs ldtngdcsrl vadgwlelql adsesairll aaslrlrarw esaldrqlah
      961 qaqqqleeee edtpvspkev atlskellqf taskipyslr rltglevqnm yvgpqtipat
     1021 phlpglfgss tlsphptkgg yavtdfltyn cltndtdlys dclrtfwtcp hcglhapltp
     1081 leriahentc pqapqdgppg aeeaaletlq ktsvlqrpyh ceacgkdflf tptevlrhrk
     1141 qhv
//
LOCUS       NP_001350673             469 aa            linear   PRI 27-APR-2025
DEFINITION  macrophage scavenger receptor types I and II isoform 4 [Homo
            sapiens].
ACCESSION   NP_001350673 XP_024302928
VERSION     NP_001350673.1
DBSOURCE    REFSEQ: accession NM_001363744.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Saadh,M.J., Pallathadka,H., Abed,H.S., Menon,S.V., Sivaprasad,G.V.,
            Hjazi,A., Rizaev,J., Suri,S., Jawad,M.A. and Husseen,B.
  TITLE     Detailed role of SR-A1 and SR-E3 in tumor biology, progression, and
            therapy
  JOURNAL   Cell Biochem Biophys 82 (3), 1735-1750 (2024)
   PUBMED   38884861
  REMARK    GeneRIF: Detailed role of SR-A1 and SR-E3 in tumor biology,
            progression, and therapy.
            Review article
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Onyishi,C.U., Desanti,G.E., Wilkinson,A.L., Lara-Reyna,S.,
            Frickel,E.M., Fejer,G., Christophe,O.D., Bryant,C.E.,
            Mukhopadhyay,S., Gordon,S. and May,R.C.
  TITLE     Toll-like receptor 4 and macrophage scavenger receptor 1 crosstalk
            regulates phagocytosis of a fungal pathogen
  JOURNAL   Nat Commun 14 (1), 4895 (2023)
   PUBMED   37580395
  REMARK    GeneRIF: Toll-like receptor 4 and macrophage scavenger receptor 1
            crosstalk regulates phagocytosis of a fungal pathogen.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 469)
  AUTHORS   AbdElneam,A.I., Al-Dhubaibi,M.S., Bahaj,S.S. and Mohammed,G.F.
  TITLE     Role of macrophage scavenger receptor 1 in the progression of
            dyslipidemia in acne vulgaris patients
  JOURNAL   Skin Res Technol 29 (8), e13424 (2023)
   PUBMED   37632192
  REMARK    GeneRIF: Role of macrophage scavenger receptor 1 in the progression
            of dyslipidemia in acne vulgaris patients.
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Cheng,W., Shu,M., Kuang,L., Bai,X., Jia,X., Zhao,Y., Lu,Y., Zhu,L.,
            Wang,L., Zhu,Y., Shu,Y., Song,Y. and Jin,S.
  TITLE     Scavenger receptor a mediates glycated LDL transcytosis across
            endothelial cells to promote atherosclerosis
  JOURNAL   Int J Biol Macromol 235, 123836 (2023)
   PUBMED   36849072
  REMARK    GeneRIF: Scavenger receptor a mediates glycated LDL transcytosis
            across endothelial cells to promote atherosclerosis.
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Sheng,W., Ji,G. and Zhang,L.
  TITLE     Role of macrophage scavenger receptor MSR1 in the progression of
            non-alcoholic steatohepatitis
  JOURNAL   Front Immunol 13, 1050984 (2022)
   PUBMED   36591228
  REMARK    GeneRIF: Role of macrophage scavenger receptor MSR1 in the
            progression of non-alcoholic steatohepatitis.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 469)
  AUTHORS   Resnick,D., Chatterton,J.E., Schwartz,K., Slayter,H. and Krieger,M.
  TITLE     Structures of class A macrophage scavenger receptors. Electron
            microscopic study of flexible, multidomain, fibrous proteins and
            determination of the disulfide bond pattern of the scavenger
            receptor cysteine-rich domain
  JOURNAL   J Biol Chem 271 (43), 26924-26930 (1996)
   PUBMED   8900177
REFERENCE   7  (residues 1 to 469)
  AUTHORS   Ashkenas,J., Penman,M., Vasile,E., Acton,S., Freeman,M. and
            Krieger,M.
  TITLE     Structures and high and low affinity ligand binding properties of
            murine type I and type II macrophage scavenger receptors
  JOURNAL   J Lipid Res 34 (6), 983-1000 (1993)
   PUBMED   8394868
REFERENCE   8  (residues 1 to 469)
  AUTHORS   Emi,M., Asaoka,H., Matsumoto,A., Itakura,H., Kurihara,Y., Wada,Y.,
            Kanamori,H., Yazaki,Y., Takahashi,E., Lepert,M. et al.
  TITLE     Structure, organization, and chromosomal mapping of the human
            macrophage scavenger receptor gene
  JOURNAL   J Biol Chem 268 (3), 2120-2125 (1993)
   PUBMED   8093617
REFERENCE   9  (residues 1 to 469)
  AUTHORS   Naito,M., Suzuki,H., Mori,T., Matsumoto,A., Kodama,T. and
            Takahashi,K.
  TITLE     Coexpression of type I and type II human macrophage scavenger
            receptors in macrophages of various organs and foam cells in
            atherosclerotic lesions
  JOURNAL   Am J Pathol 141 (3), 591-599 (1992)
   PUBMED   1519666
REFERENCE   10 (residues 1 to 469)
  AUTHORS   Matsumoto,A., Naito,M., Itakura,H., Ikemoto,S., Asaoka,H.,
            Hayakawa,I., Kanamori,H., Aburatani,H., Takaku,F., Suzuki,H. et al.
  TITLE     Human macrophage scavenger receptors: primary structure,
            expression, and localization in atherosclerotic lesions
  JOURNAL   Proc Natl Acad Sci U S A 87 (23), 9133-9137 (1990)
   PUBMED   2251254
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK293217.1, BC063878.1 and
            AC023396.4.
            
            On May 30, 2018 this sequence version replaced XP_024302928.1.
            
            Summary: This gene encodes the class A macrophage scavenger
            receptors, which include three different types (1, 2, 3) generated
            by alternative splicing of this gene. These receptors or isoforms
            are macrophage-specific trimeric integral membrane glycoproteins
            and have been implicated in many macrophage-associated
            physiological and pathological processes including atherosclerosis,
            Alzheimer's disease, and host defense. The isoforms type 1 and type
            2 are functional receptors and are able to mediate the endocytosis
            of modified low density lipoproteins (LDLs). The isoform type 3
            does not internalize modified LDL (acetyl-LDL) despite having the
            domain shown to mediate this function in the types 1 and 2
            isoforms. It has an altered intracellular processing and is trapped
            within the endoplasmic reticulum, making it unable to perform
            endocytosis. The isoform type 3 can inhibit the function of
            isoforms type 1 and type 2 when co-expressed, indicating a dominant
            negative effect and suggesting a mechanism for regulation of
            scavenger receptor activity in macrophages. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293217.1, SRR1803617.132555.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467147 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..469
                     /product="macrophage scavenger receptor types I and II
                     isoform 4"
                     /note="macrophage scavenger receptor type III; macrophage
                     acetylated LDL receptor I and II; macrophage scavenger
                     receptor types I and II; scavenger receptor class A member
                     1"
                     /calculated_mol_wt=51595
     Region          139..187
                     /region_name="Macscav_rec"
                     /note="Macrophage scavenger receptor; pfam03523"
                     /db_xref="CDD:460956"
     Region          218..>376
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          298..352
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          368..468
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     CDS             1..469
                     /gene="MSR1"
                     /gene_synonym="CD204; phSR1; phSR2; SCARA1; SR-A; SR-AI;
                     SR-AII; SR-AIII; SRA"
                     /coded_by="NM_001363744.1:65..1474"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS87581.1"
                     /db_xref="GeneID:4481"
                     /db_xref="HGNC:HGNC:7376"
                     /db_xref="MIM:153622"
ORIGIN      
        1 mcylsaiisi sllnkkpsme qwdhfhnqqe dtdscsesvk fdarsmtall ppnpknspsl
       61 qeklksfkaa lialyllvfa vlipligiva aqllkwetkn csvsstnand itqsltgkgn
      121 dseeemrfqe vfmehmsnme kriqhildme anlmdtehfq nfsmttdqrf ndillqlstl
      181 fssvqghgna ideiskslis lnttlldlql nienlngkiq entfkqqeei skleervynv
      241 saeimamkee qvhleqeikg evkvlnnitn dlrlkdwehs qtlrnitliq gppgppgekg
      301 drgptgesgp rgfpgpigpp glkgdrgaig fpgsrglpgy agrpgnsgpk gqkgekgsgn
      361 tltpftkvrl vggsgphegr veilhsgqwg ticddrwevr vgqvvcrslg ypgvqavhka
      421 ahfgqgtgpi wlnevfcfgr essieeckir qwgtracshs edagvtctl
//
LOCUS       NP_036551                210 aa            linear   PRI 27-APR-2025
DEFINITION  regulator of G-protein signaling 17 [Homo sapiens].
ACCESSION   NP_036551
VERSION     NP_036551.3
DBSOURCE    REFSEQ: accession NM_012419.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Ren,J., Fang,C., Liu,Y. and Xie,P.
  TITLE     Hsa_circ_0000285-Mediated miR-599/RGS17 Axis Participates in the
            Pathogenesis of Abdominal Aortic Aneurysm by Regulating the
            Functions of Vascular Smooth Muscle Cells
  JOURNAL   Ann Clin Lab Sci 53 (2), 238-247 (2023)
   PUBMED   37094862
  REMARK    GeneRIF: Hsa_circ_0000285-Mediated miR-599/RGS17 Axis Participates
            in the Pathogenesis of Abdominal Aortic Aneurysm by Regulating the
            Functions of Vascular Smooth Muscle Cells.
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Wang,S.L., Dong,X.W., Zhao,F. and Li,C.X.
  TITLE     MiR-203 inhibits cell proliferation, invasion, and migration of
            ovarian cancer through regulating RGS17
  JOURNAL   J Biol Regul Homeost Agents 35 (3), 1109-1115 (2021)
   PUBMED   34002599
  REMARK    GeneRIF: MiR-203 inhibits cell proliferation, invasion, and
            migration of ovarian cancer through regulating RGS17.
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Hu,P., Zhou,G., Zhang,X., Song,G., Zhan,L. and Cao,Y.
  TITLE     Long non-coding RNA Linc00483 accelerated tumorigenesis of cervical
            cancer by regulating miR-508-3p/RGS17 axis
  JOURNAL   Life Sci 234, 116789 (2019)
   PUBMED   31454494
  REMARK    GeneRIF: Knock-down of Long non-coding RNA Linc00483 inhibited the
            development of cervical cancer by regulating miR-508-3p/RGS17 axis.
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Larminie,C., Murdock,P., Walhin,J.P., Duckworth,M., Blumer,K.J.,
            Scheideler,M.A. and Garnier,M.
  TITLE     Selective expression of regulators of G-protein signaling (RGS) in
            the human central nervous system
  JOURNAL   Brain Res Mol Brain Res 122 (1), 24-34 (2004)
   PUBMED   14992813
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Fischer,T., De Vries,L., Meerloo,T. and Farquhar,M.G.
  TITLE     Promotion of G alpha i3 subunit down-regulation by GIPN, a putative
            E3 ubiquitin ligase that interacts with RGS-GAIP
  JOURNAL   Proc Natl Acad Sci U S A 100 (14), 8270-8275 (2003)
   PUBMED   12826607
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Sierra,D.A., Gilbert,D.J., Householder,D., Grishin,N.V., Yu,K.,
            Ukidwe,P., Barker,S.A., He,W., Wensel,T.G., Otero,G., Brown,G.,
            Copeland,N.G., Jenkins,N.A. and Wilkie,T.M.
  TITLE     Evolution of the regulators of G-protein signaling multigene family
            in mouse and human
  JOURNAL   Genomics 79 (2), 177-185 (2002)
   PUBMED   11829488
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Jordan,J.D., Carey,K.D., Stork,P.J. and Iyengar,R.
  TITLE     Modulation of rap activity by direct interaction of Galpha(o) with
            Rap1 GTPase-activating protein
  JOURNAL   J Biol Chem 274 (31), 21507-21510 (1999)
   PUBMED   10419452
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356963.17, AF202257.3,
            BC013117.1, AA902430.1, CK902282.1 and AL080276.9.
            
            On Jun 10, 2002 this sequence version replaced NP_036551.2.
            
            Summary: This gene encodes a member of the regulator of G-protein
            signaling family. This protein contains a conserved, 120 amino acid
            motif called the RGS domain and a cysteine-rich region. The protein
            attenuates the signaling activity of G-proteins by binding to
            activated, GTP-bound G alpha subunits and acting as a GTPase
            activating protein (GAP), increasing the rate of conversion of the
            GTP to GDP. This hydrolysis allows the G alpha subunits to bind G
            beta/gamma subunit heterodimers, forming inactive G-protein
            heterotrimers, thereby terminating the signal. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013117.1, AF202257.3 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000206262.2/ ENSP00000206262.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.2"
     Protein         1..210
                     /product="regulator of G-protein signaling 17"
                     /calculated_mol_wt=24228
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGC6.2)"
     Region          41..197
                     /region_name="RGS"
                     /note="Regulator of G protein signaling (RGS) domain
                     superfamily; cl02565"
                     /db_xref="CDD:470619"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZB0; propagated from
                     UniProtKB/Swiss-Prot (Q9UGC6.2)"
     CDS             1..210
                     /gene="RGS17"
                     /gene_synonym="hRGS17; RGS-17; RGSZ2"
                     /coded_by="NM_012419.5:185..817"
                     /db_xref="CCDS:CCDS5244.1"
                     /db_xref="GeneID:26575"
                     /db_xref="HGNC:HGNC:14088"
                     /db_xref="MIM:607191"
ORIGIN      
        1 mrkrqqsqne gtpavsqapg nqrpnntccf cwccccscsc ltvrneerge nagrpthttk
       61 mesiqvleec qnptaeevls wsqnfdkmmk apagrnlfre flrteyseen llfwlacedl
      121 kkeqnkkvie ekarmiyedy isilspkevs ldsrvrevin rnlldpnphm yedaqlqiyt
      181 lmhrdsfprf lnsqiyksfv estagssses
//
LOCUS       NP_005468               1203 aa            linear   PRI 27-APR-2025
DEFINITION  potassium/sodium hyperpolarization-activated cyclic
            nucleotide-gated channel 4 [Homo sapiens].
ACCESSION   NP_005468
VERSION     NP_005468.1
DBSOURCE    REFSEQ: accession NM_005477.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1203)
  AUTHORS   Fraile,A., Cebrian,J., Thuissard-Vasallo,I., Perez-Martin,S.,
            Casado,R., Gil-Fournier,B., Alonso-Martin,J., Tamargo,J.,
            Caballero,R., Delpon,E. and Cosio,F.G.
  TITLE     Coexistent HCN4 and GATA5 Rare Variants and Atrial Fibrillation in
            a Large Spanish Family
  JOURNAL   Can J Cardiol 40 (7), 1270-1280 (2024)
   PUBMED   38432398
  REMARK    GeneRIF: Coexistent HCN4 and GATA5 Rare Variants and Atrial
            Fibrillation in a Large Spanish Family.
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Camara-Checa,A., Perin,F., Rubio-Alarcon,M., Dago,M.,
            Crespo-Garcia,T., Rapun,J., Marin,M., Cebrian,J., Gomez,R.,
            Bermudez-Jimenez,F., Monserrat,L., Tamargo,J., Caballero,R.,
            Jimenez-Jaimez,J. and Delpon,E.
  TITLE     A gain-of-function HCN4 mutant in the HCN domain is responsible for
            inappropriate sinus tachycardia in a Spanish family
  JOURNAL   Proc Natl Acad Sci U S A 120 (49), e2305135120 (2023)
   PUBMED   38032931
  REMARK    GeneRIF: A gain-of-function HCN4 mutant in the HCN domain is
            responsible for inappropriate sinus tachycardia in a Spanish
            family.
REFERENCE   3  (residues 1 to 1203)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1203)
  AUTHORS   Wang,H., Wu,T., Huang,Z., Huang,J., Geng,Z., Cui,B., Yan,Y.,
            Zhang,Y. and Wang,Y.
  TITLE     Channel HCN4 mutation R666Q associated with sporadic arrhythmia
            decreases channel electrophysiological function and increases
            protein degradation
  JOURNAL   J Biol Chem 298 (11), 102599 (2022)
   PUBMED   36244448
  REMARK    GeneRIF: Channel HCN4 mutation R666Q associated with sporadic
            arrhythmia decreases channel electrophysiological function and
            increases protein degradation.
REFERENCE   5  (residues 1 to 1203)
  AUTHORS   Qu,J., Altomare,C., Bucchi,A., DiFrancesco,D. and Robinson,R.B.
  TITLE     Functional comparison of HCN isoforms expressed in ventricular and
            HEK 293 cells
  JOURNAL   Pflugers Arch 444 (5), 597-601 (2002)
   PUBMED   12194012
  REMARK    GeneRIF: HCN4 activates substantially slower than HCN2 and with a
            half-maximum activation voltage approximately equal 10 mV less
            negative, both isoforms activate more positively in myocytes
            suggesting cell-type specificity
REFERENCE   6  (residues 1 to 1203)
  AUTHORS   Stevens,D.R., Seifert,R., Bufe,B., Muller,F., Kremmer,E., Gauss,R.,
            Meyerhof,W., Kaupp,U.B. and Lindemann,B.
  TITLE     Hyperpolarization-activated channels HCN1 and HCN4 mediate
            responses to sour stimuli
  JOURNAL   Nature 413 (6856), 631-635 (2001)
   PUBMED   11675786
  REMARK    GeneRIF: The rat HCN1 and HCN4 were shown to mediate responses to
            sour stimuli, suggesting a potential new function for the related
            human proteins.
REFERENCE   7  (residues 1 to 1203)
  AUTHORS   Seifert,R., Scholten,A., Gauss,R., Mincheva,A., Lichter,P. and
            Kaupp,U.B.
  TITLE     Molecular characterization of a slowly gating human
            hyperpolarization-activated channel predominantly expressed in
            thalamus, heart, and testis
  JOURNAL   Proc Natl Acad Sci U S A 96 (16), 9391-9396 (1999)
   PUBMED   10430953
REFERENCE   8  (residues 1 to 1203)
  AUTHORS   Ludwig,A., Zong,X., Stieber,J., Hullin,R., Hofmann,F. and Biel,M.
  TITLE     Two pacemaker channels from human heart with profoundly different
            activation kinetics
  JOURNAL   EMBO J 18 (9), 2323-2329 (1999)
   PUBMED   10228147
REFERENCE   9  (residues 1 to 1203)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   10 (residues 1 to 1203)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ238850.1, AJ132429.1,
            AC068397.6, BP291686.1 and BM979827.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the
            hyperpolarization-activated cyclic nucleotide-gated potassium
            channels. The encoded protein shows slow kinetics of activation and
            inactivation, and is necessary for the cardiac pacemaking process.
            This channel may also mediate responses to sour stimuli. Mutations
            in this gene have been linked to sick sinus syndrome 2, also known
            as atrial fibrillation with bradyarrhythmia or familial sinus
            bradycardia. Two pseudogenes have been identified on chromosome 15.
            [provided by RefSeq, Oct 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ132429.1, AJ238850.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261917.4/ ENSP00000261917.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..1203
                     /product="potassium/sodium hyperpolarization-activated
                     cyclic nucleotide-gated channel 4"
                     /note="hyperpolarization activated cyclic nucleotide-gated
                     cation channel 4"
                     /calculated_mol_wt=128911
     Region          1..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKA7; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Region          209..260
                     /region_name="Involved in subunit assembly.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Region          218..260
                     /region_name="Ion_trans_N"
                     /note="Ion transport protein N-terminal; pfam08412"
                     /db_xref="CDD:400630"
     Region          253..>740
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Site            264..286
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Site            294..314
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Site            337..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Site            379..399
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Site            414..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Site            458
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Site            492..517
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Region          595..703
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(659..660,669..671)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(691..693,697..699)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          <766..1044
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          836..856
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Region          870..897
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Region          918..1203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Region          <928..1200
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70507; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     Site            1108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70507; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q4.1)"
     CDS             1..1203
                     /gene="HCN4"
                     /gene_synonym="BRGDA8; EIG18; SSS2"
                     /coded_by="NM_005477.3:689..4300"
                     /db_xref="CCDS:CCDS10248.1"
                     /db_xref="GeneID:10021"
                     /db_xref="HGNC:HGNC:16882"
                     /db_xref="MIM:605206"
ORIGIN      
        1 mdklppsmrk rlyslpqqvg akawimdeee daeeegaggr qdpsrrsirl rplpspspsa
       61 aaggtesrss algaadsegp argagksstn gdcrrfrgsl aslgsrgggs ggtgsgsshg
      121 hlhdsaeerr liaegdaspg edrtppglaa eperpgasaq paasppppqq ppqpasasce
      181 qpsvdtaikv eggaaagdqi lpeaevrlgq agfmqrqfga mlqpgvnkfs lrmfgsqkav
      241 ereqervksa gfwiihpysd frfywdltml llmvgnliii pvgitffkde nttpwivfnv
      301 vsdtfflidl vlnfrtgivv ednteiildp qrikmkylks wfmvdfissi pvdyiflive
      361 tridsevykt aralrivrft kilsllrllr lsrliryihq weeifhmtyd lasavvrivn
      421 ligmmlllch wdgclqflvp mlqdfpddcw vsinnmvnns wgkqysyalf kamshmlcig
      481 ygrqapvgms dvwltmlsmi vgatcyamfi ghataliqsl dssrrqyqek ykqveqymsf
      541 hklppdtrqr ihdyyehryq gkmfdeesil gelseplree iinfncrklv asmplfanad
      601 pnfvtsmltk lrfevfqpgd yiiregtigk kmyfiqhgvv svltkgnket kladgsyfge
      661 iclltrgrrt asvradtycr lyslsvdnfn evleeypmmr rafetvaldr ldrigkknsi
      721 llhkvqhdln sgvfnyqene iiqqivqhdr emahcahrvq aaasatptpt pviwtpliqa
      781 plqaaaatts vaialthhpr lpaaifrppp gsglgnlgag qtprhlkrlq slipsalgsa
      841 spasspsqvd tpssssfhiq qlagfsapag lspllpssss spppgacgsp saptpsagva
      901 attiagfghf hkalggslss sdsplltplq pgarspqaaq pspappgarg glglpehflp
      961 pppssrspss spgqlgqppg elslglatgp lstpetpprq peppslvaga sggaspvgft
     1021 prgglsppgh spgpprtfps apprasgshg slllppassp pppqvpqrrg tppltpgrlt
     1081 qdlklisasq palpqdgaqt lrrasphssg esmaafplfp ragggsggsg ssgglgppgr
     1141 pygaipgqhv tlprktssgs lppplslfga ratssggppl tagpqrepga rpepvrsklp
     1201 snl
//
LOCUS       NP_060715               1010 aa            linear   PRI 27-APR-2025
DEFINITION  2-oxoglutarate dehydrogenase-like, mitochondrial isoform a [Homo
            sapiens].
ACCESSION   NP_060715
VERSION     NP_060715.2
DBSOURCE    REFSEQ: accession NM_018245.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Lin,S.J., Vona,B., Lau,T., Huang,K., Zaki,M.S., Aldeen,H.S.,
            Karimiani,E.G., Rocca,C., Noureldeen,M.M., Saad,A.K., Petree,C.,
            Bartolomaeus,T., Abou Jamra,R., Zifarelli,G., Gotkhindikar,A.,
            Wentzensen,I.M., Liao,M., Cork,E.E., Varshney,P., Hashemi,N.,
            Mohammadi,M.H., Rad,A., Neira,J., Toosi,M.B., Knopp,C., Kurth,I.,
            Challman,T.D., Smith,R., Abdalla,A., Haaf,T., Suri,M., Joshi,M.,
            Chung,W.K., Moreno-De-Luca,A., Houlden,H., Maroofian,R. and
            Varshney,G.K.
  TITLE     Evaluating the association of biallelic OGDHL variants with
            significant phenotypic heterogeneity
  JOURNAL   Genome Med 15 (1), 102 (2023)
   PUBMED   38031187
  REMARK    GeneRIF: Evaluating the association of biallelic OGDHL variants
            with significant phenotypic heterogeneity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Dai,W., Li,Y., Sun,W., Ji,M., Bao,R., Chen,J., Xu,S., Dai,Y.,
            Chen,Y., Liu,W., Ge,C., Sun,W., Mo,W., Guo,C. and Xu,X.
  TITLE     Silencing of OGDHL promotes liver cancer metastasis by enhancing
            hypoxia inducible factor 1 alpha protein stability
  JOURNAL   Cancer Sci 114 (4), 1309-1323 (2023)
   PUBMED   36000493
  REMARK    GeneRIF: Silencing of OGDHL promotes liver cancer metastasis by
            enhancing hypoxia inducible factor 1 alpha protein stability.
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 1010)
  AUTHORS   Yap,Z.Y., Efthymiou,S., Seiffert,S., Vargas Parra,K., Lee,S.,
            Nasca,A., Maroofian,R., Schrauwen,I., Pendziwiat,M., Jung,S.,
            Bhoj,E., Striano,P., Mankad,K., Vona,B., Cuddapah,S., Wagner,A.,
            Alvi,J.R., Davoudi-Dehaghani,E., Fallah,M.S., Gannavarapu,S.,
            Lamperti,C., Legati,A., Murtaza,B.N., Nadeem,M.S., Rehman,M.U.,
            Saeidi,K., Salpietro,V., von Spiczak,S., Sandoval,A., Zeinali,S.,
            Zeviani,M., Reich,A., Jang,C., Helbig,I., Barakat,T.S., Ghezzi,D.,
            Leal,S.M., Weber,Y., Houlden,H. and Yoon,W.H.
  CONSRTM   SYNaPS Study Group; University of Washington Center for Mendelian
            Genomics
  TITLE     Bi-allelic variants in OGDHL cause a neurodevelopmental spectrum
            disease featuring epilepsy, hearing loss, visual impairment, and
            ataxia
  JOURNAL   Am J Hum Genet 108 (12), 2368-2384 (2021)
   PUBMED   34800363
  REMARK    GeneRIF: Bi-allelic variants in OGDHL cause a neurodevelopmental
            spectrum disease featuring epilepsy, hearing loss, visual
            impairment, and ataxia.
REFERENCE   5  (residues 1 to 1010)
  AUTHORS   Mao,M., Huang,R.Z., Zheng,J., Liang,H.Q., Huang,W.H., Liu,J. and
            Li,J.H.
  TITLE     OGDHL closely associates with tumor microenvironment and can serve
            as a prognostic biomarker for papillary thyroid cancer
  JOURNAL   Cancer Med 10 (2), 728-736 (2021)
   PUBMED   33405394
  REMARK    GeneRIF: OGDHL closely associates with tumor microenvironment and
            can serve as a prognostic biomarker for papillary thyroid cancer.
REFERENCE   6  (residues 1 to 1010)
  AUTHORS   Khalaj-Kondori,M., Hosseinnejad,M., Hosseinzadeh,A., Behroz
            Sharif,S. and Hashemzadeh,S.
  TITLE     Aberrant hypermethylation of OGDHL gene promoter in sporadic
            colorectal cancer
  JOURNAL   Curr Probl Cancer 44 (1), 100471 (2020)
   PUBMED   30904169
  REMARK    GeneRIF: Aberrant hypermethylation of OGDHL gene promoter in
            sporadic colorectal cancer.
REFERENCE   7  (residues 1 to 1010)
  AUTHORS   Sen,T., Sen,N., Noordhuis,M.G., Ravi,R., Wu,T.C., Ha,P.K.,
            Sidransky,D. and Hoque,M.O.
  TITLE     OGDHL is a modifier of AKT-dependent signaling and NF-kappaB
            function
  JOURNAL   PLoS One 7 (11), e48770 (2012)
   PUBMED   23152800
  REMARK    GeneRIF: inactivation of OGDHL can contribute to cervical
            tumorigenesis via activation of the AKT signaling pathway and thus
            support it as an important anti-proliferative gene in cervical
            cancer.
REFERENCE   8  (residues 1 to 1010)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of gene polymorphisms with chronic kidney disease in
            Japanese individuals
  JOURNAL   Int J Mol Med 24 (4), 539-547 (2009)
   PUBMED   19724895
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1010)
  AUTHORS   Bunik,V., Kaehne,T., Degtyarev,D., Shcherbakova,T. and Reiser,G.
  TITLE     Novel isoenzyme of 2-oxoglutarate dehydrogenase is identified in
            brain, but not in heart
  JOURNAL   FEBS J 275 (20), 4990-5006 (2008)
   PUBMED   18783430
REFERENCE   10 (residues 1 to 1010)
  AUTHORS   Bunik,V.I. and Degtyarev,D.
  TITLE     Structure-function relationships in the 2-oxo acid dehydrogenase
            family: substrate-specific signatures and functional predictions
            for the 2-oxoglutarate dehydrogenase-like proteins
  JOURNAL   Proteins 71 (2), 874-890 (2008)
   PUBMED   18004749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA238469.1, BC026320.1,
            DA411851.1, AB033116.3 and BQ549806.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 24, 2009 this sequence version replaced NP_060715.1.
            
            Summary: The protein encoded by this gene is similar to
            oxoglutarate dehydrogenase (OGDH) of the OGDH complex, which
            degrades glucose and glutamate. This gene encodes several isoforms,
            including some that appear to localize to mitochondria. The encoded
            protein down-regulates the AKT signaling cascade and can suppress
            the growth of cervical cancer cells. [provided by RefSeq, Dec
            2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1 and 4 both encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001713.1, SRR1803616.263597.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000374103.9/
                                                  ENSP00000363216.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.23"
     Protein         1..1010
                     /product="2-oxoglutarate dehydrogenase-like, mitochondrial
                     isoform a"
                     /EC_number="1.2.4.2"
                     /note="2-oxoglutarate dehydrogenase-like, mitochondrial;
                     oxoglutarate dehydrogenase like; OGDC-E1-like;
                     alpha-ketoglutarate dehydrogenase-like; 2-oxoglutarate
                     dehydrogenase complex component E1-like"
                     /calculated_mol_wt=106444
     transit_peptide 1..73
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9ULD0.3)"
                     /calculated_mol_wt=8056
     Region          51..1002
                     /region_name="SucA"
                     /note="2-oxoglutarate dehydrogenase complex, dehydrogenase
                     (E1) component, and related enzymes [Energy production and
                     conversion]; COG0567"
                     /db_xref="CDD:440333"
     mat_peptide     74..1010
                     /product="2-oxoglutarate dehydrogenase-like,
                     mitochondrial. /id=PRO_0000310983"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULD0.3)"
                     /calculated_mol_wt=106444
     Region          81..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULD0.3)"
     CDS             1..1010
                     /gene="OGDHL"
                     /gene_synonym="YOBELN"
                     /coded_by="NM_018245.3:87..3119"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7234.1"
                     /db_xref="GeneID:55753"
                     /db_xref="HGNC:HGNC:25590"
                     /db_xref="MIM:617513"
ORIGIN      
        1 msqlrllpsr lgvqaarlla ahdvpvfgwr srssgppatf psskggggss ymeemyfawl
       61 enpqsvhksw dsffreasee afsgsaqprp psvvhesrsa vssrtktskl vedhlavqsl
      121 irayqirghh vaqldplgil dadldsfvps dlittidkla fydlqeadld kefqlptttf
      181 iggsentlsl reiirrlent ycqhiglefm findveqcqw irqkfetpgv mqfsseekrt
      241 llarlvrsmr fedflarkws sekrfglegc evmipalkti idkssemgie nvilgmphrg
      301 rlnvlanvir kdleqifcqf dpkleaadeg sgdvkyhlgm yherinrvtn rnitlslvan
      361 pshleavdpv vqgktkaeqf yrgdaqgkkv msilvhgdaa fagqgvvyet fhlsdlpsyt
      421 tngtvhvvvn nqigfttdpr marsspyptd varvvnapif hvnaddpeav iyvcsvaaew
      481 rntfnkdvvv dlvcyrrrgh nemdepmftq plmykqihrq vpvlkkyadk liaegtvtlq
      541 efeeeiakyd riceeaygrs kdkkilhikh wldspwpgff nvdgepksmt cpatgipedm
      601 lthigsvass vpledfkiht glsrilrgra dmtknrtvdw alaeymafgs llkegihvrl
      661 sgqdvergtf shrhhvlhdq evdrrtcvpm nhlwpdqapy tvcnsslsey gvlgfelgya
      721 maspnalvlw eaqfgdfhnt aqciidqfis tgqakwvrhn givlllphgm egmgpehssa
      781 rperflqmsn ddsdaypaft kdfevsqlyd cnwivvncst panyfhvlrr qillpfrkpl
      841 iiftpksllr hpeakssfdq mvsgtsfqrv ipedgaaara peqvqrlifc tgkvyydlvk
      901 erssqdleek vaitrleqis pfpfdlikqe aekypgaela wcqeehknmg yydyisprfm
      961 tilrrarpiw yvgrdpaaap atgnrnthlv slkkfldtaf nlqafegktf
//
LOCUS       NP_001349779             411 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-N-acetylgalactosaminidase precursor [Homo sapiens].
ACCESSION   NP_001349779 XP_005261673
VERSION     NP_001349779.1
DBSOURCE    REFSEQ: accession NM_001362850.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Yilmaz,S. and Oner,P.
  TITLE     Could low alpha-N-acetylgalactosaminidase plasma concentration
            cause schizophrenia?
  JOURNAL   World J Biol Psychiatry 24 (1), 70-77 (2023)
   PUBMED   35521802
  REMARK    GeneRIF: Could low alpha-N-acetylgalactosaminidase plasma
            concentration cause schizophrenia?
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Jafari,M., Rahimi,N., Jami,M.S., Hashemzadeh Chaleshtori,M.,
            Elahian,F. and Mirzaei,S.A.
  TITLE     Silencing of alpha-N-acetylgalactosaminidase in the gastric cancer
            cells amplified cell death and attenuated migration, while the
            multidrug resistance remained unchanged
  JOURNAL   Cell Biol Int 46 (2), 255-264 (2022)
   PUBMED   34816536
  REMARK    GeneRIF: Silencing of alpha-N-acetylgalactosaminidase in the
            gastric cancer cells amplified cell death and attenuated migration,
            while the multidrug resistance remained unchanged.
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Li,Y., Ma,C., Li,W., Yang,Y., Li,X., Liu,J., Wang,J., Li,S.,
            Liu,Y., Li,K., Li,J., Huang,D., Chen,R., Lv,L., Li,M. and Luo,X.J.
  TITLE     A missense variant in NDUFA6 confers schizophrenia risk by
            affecting YY1 binding and NAGA expression
  JOURNAL   Mol Psychiatry 26 (11), 6896-6911 (2021)
   PUBMED   33931730
  REMARK    GeneRIF: A missense variant in NDUFA6 confers schizophrenia risk by
            affecting YY1 binding and NAGA expression.
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Mohamed,F.E., Al Sorkhy,M., Ghattas,M.A., Al-Zaabi,N.,
            Al-Shamsi,A., Almansoori,T.M., Al-Gazali,L., Al-Dirbashi,O.Y.,
            Al-Jasmi,F. and Ali,B.R.
  TITLE     A Novel Homozygous Missense Variant in the NAGA Gene with Extreme
            Intrafamilial Phenotypic Heterogeneity
  JOURNAL   J Mol Neurosci 70 (1), 45-55 (2020)
   PUBMED   31468281
  REMARK    GeneRIF: A Novel Homozygous Missense Variant in the NAGA Gene with
            Extreme Intrafamilial Phenotypic Heterogeneity.
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Meshach Paul,D. and Rajasekaran,R.
  TITLE     Exploration of Structural and Functional Variations Owing to Point
            Mutations in alpha-NAGA
  JOURNAL   Interdiscip Sci 10 (1), 81-92 (2018)
   PUBMED   27138754
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Wang,A.M. and Desnick,R.J.
  TITLE     Structural organization and complete sequence of the human
            alpha-N-acetylgalactosaminidase gene: homology with the
            alpha-galactosidase A gene provides evidence for evolution from a
            common ancestral gene
  JOURNAL   Genomics 10 (1), 133-142 (1991)
   PUBMED   1646157
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Wang,A.M., Bishop,D.F. and Desnick,R.J.
  TITLE     Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide
            sequence, and expression of a full-length cDNA. Homology with human
            alpha-galactosidase A suggests evolution from a common ancestral
            gene
  JOURNAL   J Biol Chem 265 (35), 21859-21866 (1990)
   PUBMED   2174888
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Warner,T.G., Louie,A. and Potier,M.
  TITLE     Photolabeling of the alpha-neuraminidase/beta-galactosidase complex
            from human placenta with a photoreactive neuraminidase inhibitor
  JOURNAL   Biochem Biophys Res Commun 173 (1), 13-19 (1990)
   PUBMED   2256909
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Wang,A.M., Schindler,D. and Desnick,R.
  TITLE     Schindler disease: the molecular lesion in the
            alpha-N-acetylgalactosaminidase gene that causes an infantile
            neuroaxonal dystrophy
  JOURNAL   J Clin Invest 86 (5), 1752-1756 (1990)
   PUBMED   2243144
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Cantz,M. and Ulrich-Bott,B.
  TITLE     Disorders of glycoprotein degradation
  JOURNAL   J Inherit Metab Dis 13 (4), 523-537 (1990)
   PUBMED   2122119
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z99716.4.
            
            On May 1, 2018 this sequence version replaced XP_005261673.1.
            
            Summary: NAGA encodes the lysosomal enzyme
            alpha-N-acetylgalactosaminidase, which cleaves
            alpha-N-acetylgalactosaminyl moieties from glycoconjugates.
            Mutations in NAGA have been identified as the cause of  Schindler
            disease types I and II (type II also known as Kanzaki disease).
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1-3 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.900920.1,
                                           SRR11853561.20062.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..411
                     /product="alpha-N-acetylgalactosaminidase precursor"
                     /EC_number="3.2.1.49"
                     /note="Acetylgalactosaminidase, alpha-N-
                     (alpha-galactosidase B); N-acetylgalactosaminidase,
                     alpha-"
                     /calculated_mol_wt=44703
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1879
     mat_peptide     18..411
                     /product="Alpha-N-acetylgalactosaminidase.
                     /id=PRO_0000001018"
                     /note="propagated from UniProtKB/Swiss-Prot (P17050.2)"
                     /calculated_mol_wt=44703
     Region          25..308
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(33,78..79,119,154,156,188,213,217)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19683538; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19683538; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Site            201
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Region          311..394
                     /region_name="Melibiase_2_C"
                     /note="Alpha galactosidase A C-terminal beta sandwich
                     domain; pfam17450"
                     /db_xref="CDD:407508"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Site            359
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Site            385
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19683538; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     CDS             1..411
                     /gene="NAGA"
                     /gene_synonym="D22S674; GALB"
                     /coded_by="NM_001362850.1:150..1385"
                     /db_xref="CCDS:CCDS14030.1"
                     /db_xref="GeneID:4668"
                     /db_xref="HGNC:HGNC:7631"
                     /db_xref="MIM:104170"
ORIGIN      
        1 mllktvlllg hvaqvlmldn gllqtppmgw lawerfrcni ncdedpknci seqlfmemad
       61 rmaqdgwrdm gytylniddc wiggrdasgr lmpdpkrfph gipfladyvh slglklgiya
      121 dmgnftcmgy pgttldkvvq daqtfaewkv dmlkldgcfs tpeeraqgyp kmaaalnatg
      181 rpiafscswp ayegglpprv nyslladicn lwrnyddiqd swwsvlsiln wfvehqdilq
      241 pvagpghwnd pdmllignfg lsleqsraqm alwtvlaapl lmstdlrtis aqnmdilqnp
      301 lmikinqdpl giqgrrihke kslievymrp lsnkasalvf fscrtdmpyr yhsslgqlnf
      361 tgsviyeaqd vysgdiisgl rdetnftvii npsgvvmwyl ypiknlemsq q
//
LOCUS       NP_001350411             337 aa            linear   PRI 27-APR-2025
DEFINITION  B-cell receptor-associated protein 29 isoform c [Homo sapiens].
ACCESSION   NP_001350411 XP_016867925
VERSION     NP_001350411.1
DBSOURCE    REFSEQ: accession NM_001363482.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Tang,Y., Qin,F., Liu,A. and Li,H.
  TITLE     Recurrent fusion RNA DUS4L-BCAP29 in non-cancer human tissues and
            cells
  JOURNAL   Oncotarget 8 (19), 31415-31423 (2017)
   PUBMED   28415823
  REMARK    GeneRIF: we believe that in contrast to traditional gene fusions,
            DUS4L-BCAP29 cannot be used as a cancer biomarker. Instead, it is a
            fusion transcript that exists in normal physiology and that its
            pro-growth effect is not unique to cancer cells.
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Foster,L.J., Zeemann,P.A., Li,C., Mann,M., Jensen,O.N. and
            Kassem,M.
  TITLE     Differential expression profiling of membrane proteins by
            quantitative proteomics in a human mesenchymal stem cell line
            undergoing osteoblast differentiation
  JOURNAL   Stem Cells 23 (9), 1367-1377 (2005)
   PUBMED   16210410
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Schamel,W.W., Kuppig,S., Becker,B., Gimborn,K., Hauri,H.P. and
            Reth,M.
  TITLE     A high-molecular-weight complex of membrane proteins BAP29/BAP31 is
            involved in the retention of membrane-bound IgD in the endoplasmic
            reticulum
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 9861-9866 (2003)
   PUBMED   12886015
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Kim,K.M., Adachi,T., Nielsen,P.J., Terashima,M., Lamers,M.C.,
            Kohler,G. and Reth,M.
  TITLE     Two new proteins preferentially associated with membrane
            immunoglobulin D
  JOURNAL   EMBO J 13 (16), 3793-3800 (1994)
   PUBMED   8070407
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004839.1 and AC078937.1.
            
            On May 19, 2018 this sequence version replaced XP_016867925.1.
            
            Transcript Variant: This variant (4), as well as variant 8, encodes
            isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.258892.1,
                                           SRR1803611.15929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..337
                     /product="B-cell receptor-associated protein 29 isoform c"
                     /note="BCR-associated protein 29"
                     /calculated_mol_wt=38971
     Region          1..129
                     /region_name="Bap31"
                     /note="Bap31/Bap29 transmembrane region; pfam05529"
                     /db_xref="CDD:461673"
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHQ4.2)"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHQ4.2)"
     Site            104..124
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHQ4.2)"
     Region          <128..>271
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          185..>230
                     /region_name="Bap31_Bap29_C"
                     /note="Bap31/Bap29 cytoplasmic coiled-coil domain;
                     pfam18035"
                     /db_xref="CDD:465623"
     Region          198..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHQ4.2)"
     CDS             1..337
                     /gene="BCAP29"
                     /gene_synonym="B29; BAP29"
                     /coded_by="NM_001363482.1:71..1084"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:55973"
                     /db_xref="HGNC:HGNC:24131"
                     /db_xref="MIM:619612"
ORIGIN      
        1 mtlqwaavat flyaeiglil ifclpfippq rwqkifsfnv wgkiatfwnk afltiiilli
       61 vlfldavrev rkyssvhtie ksstsrpday ehtqmklfrs qrnlyisgfs lffwlvlrrl
      121 vtlitqlake lsnkgvlktq aentnkaakk fmeeneklkr ilkshgkdee cvleaenkkl
      181 vedqeklkte lrktsdalsk aqndvmemkm qserlskeyd qllkehselq kqreilphrr
      241 gestvtteae igvmepqqrn adshqkleea knrffprass srsmalqipi klildflasr
      301 tmginllfqa ikfviicycc hskliqehag qicngln
//
LOCUS       NP_060661                531 aa            linear   PRI 27-APR-2025
DEFINITION  RCC1 and BTB domain-containing protein 1 isoform a [Homo sapiens].
ACCESSION   NP_060661
VERSION     NP_060661.3
DBSOURCE    REFSEQ: accession NM_018191.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Wiphakphongpakorn,P., Juengsomjit,R., Poomsawat,S., Meesakul,O.,
            Bhattarai,B.P., Klongnoi,B., Buajeeb,W. and Khovidhunkit,S.P.
  TITLE     Expression of CLLD7 and CHC1L Proteins in Oral Epithelial Dysplasia
            in a Group of Thai Patients
  JOURNAL   Asian Pac J Cancer Prev 25 (4), 1257-1264 (2024)
   PUBMED   38679985
  REMARK    GeneRIF: Expression of CLLD7 and CHC1L Proteins in Oral Epithelial
            Dysplasia in a Group of Thai Patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Catomeris,A.J., Ballios,B.G., Sangermano,R., Wagner,N.E.,
            Comander,J.I., Pierce,E.A., Place,E.M., Bujakowska,K.M. and
            Huckfeldt,R.M.
  TITLE     Novel RCBTB1 variants causing later-onset non-syndromic retinal
            dystrophy with macular chorioretinal atrophy
  JOURNAL   Ophthalmic Genet 43 (3), 332-339 (2022)
   PUBMED   35057699
  REMARK    GeneRIF: Novel RCBTB1 variants causing later-onset non-syndromic
            retinal dystrophy with macular chorioretinal atrophy.
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Huang,Z., Zhang,D., Thompson,J.A., Jamuar,S.S., Roshandel,D.,
            Jennings,L., Mellough,C., Charng,J., Chen,S.C., McLaren,T.L.,
            Lamey,T.M., Chelva,E., De Roach,J.N., Chan,C.M., McLenachan,S. and
            Chen,F.K.
  TITLE     Deep clinical phenotyping and gene expression analysis in a patient
            with RCBTB1-associated retinopathy
  JOURNAL   Ophthalmic Genet 42 (3), 266-275 (2021)
   PUBMED   33624564
  REMARK    GeneRIF: Deep clinical phenotyping and gene expression analysis in
            a patient with RCBTB1-associated retinopathy.
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Yang,J., Xiao,X., Sun,W., Li,S., Jia,X. and Zhang,Q.
  TITLE     Variants in RCBTB1 are Associated with Autosomal Recessive
            Retinitis Pigmentosa but Not Autosomal Dominant FEVR
  JOURNAL   Curr Eye Res 46 (6), 839-844 (2021)
   PUBMED   33104391
  REMARK    GeneRIF: Variants in RCBTB1 are Associated with Autosomal Recessive
            Retinitis Pigmentosa but Not Autosomal Dominant FEVR.
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Guo,D.F., Tardif,V., Ghelima,K., Chan,J.S., Ingelfinger,J.R.,
            Chen,X. and Chenier,I.
  TITLE     A novel angiotensin II type 1 receptor-associated protein induces
            cellular hypertrophy in rat vascular smooth muscle and renal
            proximal tubular cells
  JOURNAL   J Biol Chem 279 (20), 21109-21120 (2004)
   PUBMED   14985364
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Solomou,E.E., Sfikakis,P.P., Kotsi,P., Papaioannou,M., Karali,V.,
            Vervessou,E., Hoffbrand,A.V. and Panayiotidis,P.
  TITLE     13q deletion in chronic lymphocytic leukemia: characterization of
            E4.5, a novel chromosome condensation regulator-like guanine
            nucleotide exchange factor
  JOURNAL   Leuk Lymphoma 44 (9), 1579-1585 (2003)
   PUBMED   14565662
  REMARK    GeneRIF: E4.5 gene, which maps at chromosome band 13q14.3, encodes
            for a 4 kb mRNA expressed in various tissues and has an open
            reading frame of 531 amino acids. It has a potential role in the
            pathogenesis of chronic lymphocytic leukemia [E4.5]
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Mabuchi,H., Fujii,H., Calin,G., Alder,H., Negrini,M., Rassenti,L.,
            Kipps,T.J., Bullrich,F. and Croce,C.M.
  TITLE     Cloning and characterization of CLLD6, CLLD7, and CLLD8, novel
            candidate genes for leukemogenesis at chromosome 13q14, a region
            commonly deleted in B-cell chronic lymphocytic leukemia
  JOURNAL   Cancer Res 61 (7), 2870-2877 (2001)
   PUBMED   11306461
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK096654.1, AF334406.1,
            AL833821.1, AK090807.1 and AI079751.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 7, 2005 this sequence version replaced NP_060661.2.
            
            Summary: This gene encodes a protein with an N-terminal RCC1 domain
            and a C-terminal BTB (broad complex, tramtrack and bric-a-brac)
            domain. In rat, over-expression of this gene in vascular smooth
            muscle cells induced cellular hypertrophy. In rat, the C-terminus
            of RCBTB1 interacts with the angiotensin II receptor-1A. In humans,
            this gene maps to a region of chromosome 13q that is frequently
            deleted in B-cell chronic lymphocytic leukemia and other lymphoid
            malignancies. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1-5 all encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF334406.1, SRR1660803.193337.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378302.7/ ENSP00000367552.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..531
                     /product="RCC1 and BTB domain-containing protein 1 isoform
                     a"
                     /note="GDP/GTP exchange factor (GEF)-like protein; chronic
                     lymphocytic leukemia deletion region gene 7 protein;
                     regulator of chromosome condensation and BTB
                     domain-containing protein 1; CLL deletion region gene 7
                     protein; regulator of chromosome condensation (RCC1) and
                     BTB (POZ) domain containing protein 1"
                     /calculated_mol_wt=58121
     Region          13..311
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          40..91
                     /region_name="RCC1 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDN9.1)"
     Region          93..145
                     /region_name="RCC1 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDN9.1)"
     Region          147..198
                     /region_name="RCC1 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDN9.1)"
     Region          199..250
                     /region_name="RCC1 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDN9.1)"
     Region          252..302
                     /region_name="RCC1 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDN9.1)"
     Region          304..356
                     /region_name="RCC1 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDN9.1)"
     Region          350..466
                     /region_name="BTB_POZ_RCBTB1_CLLD7"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in RCC1 and BTB
                     domain-containing protein 1 (RCBTB1); cd18353"
                     /db_xref="CDD:349662"
     Region          466..531
                     /region_name="BACK_RCBTB1"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     RCC1 and BTB domain-containing protein 1 (RCBTB1);
                     cd18528"
                     /db_xref="CDD:350603"
     CDS             1..531
                     /gene="RCBTB1"
                     /gene_synonym="CLLD7; CLLL7; GLP; RDEOA"
                     /coded_by="NM_018191.4:237..1832"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9418.1"
                     /db_xref="GeneID:55213"
                     /db_xref="HGNC:HGNC:18243"
                     /db_xref="MIM:607867"
ORIGIN      
        1 mvdvgkwpif tllspqeias irkacvfgts asealyvtdn devfvfglny snclgtgdnq
       61 stlvpkkleg lcgkkiksls ygsgphvlls tedgvvyawg hngysqlgng ttnqgiapvq
      121 vctnllikqv vevacgshhs malaadgevf awgynncgqv gsgstanqpt prkvtnclhi
      181 krvvgiacgq tssmavldng evygwgyngn gqlglgnngn qltpvrvaal hsvcvnqivc
      241 gyahtlaltd egllyawgan tygqlgtgnk nnllspahim vekervveia achsahtsaa
      301 ktqgghvymw gqcrgqsvil phlthfsctd dvfacfatpa vswrllsveh edfltvaesl
      361 kkefdspeta dlkfridgky ihvhkavlki rcehfrsmfq sywnedmkev ieidqfsypv
      421 yraflqylyt dtvdlppeda iglldlatsy cenrlkklcq hiikrgitve nafslfsaav
      481 rydaedleef cfkfcinhlt evtqtaafwq mdgpllkefi akaskcgafk n
//
LOCUS       NP_001334312             100 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane emp24 domain-containing protein 5 isoform 2 precursor
            [Mus musculus].
ACCESSION   NP_001334312 XP_011247880
VERSION     NP_001334312.1
DBSOURCE    REFSEQ: accession NM_001347383.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Nagae,M., Liebschner,D., Yamada,Y., Morita-Matsumoto,K.,
            Matsugaki,N., Senda,T., Fujita,M., Kinoshita,T. and Yamaguchi,Y.
  TITLE     Crystallographic analysis of murine p24gamma2 Golgi dynamics domain
  JOURNAL   Proteins 85 (4), 764-770 (2017)
   PUBMED   28066915
  REMARK    GeneRIF: Crystallographic analysis of murine p24gamma2 Golgi
            dynamics domain has been reported.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC159996.7.
            
            On Nov 24, 2016 this sequence version replaced XP_011247880.1.
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (2)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK014065.1, BY713066.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849383
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 52.49 cM"
     Protein         1..100
                     /product="transmembrane emp24 domain-containing protein 5
                     isoform 2 precursor"
                     /note="transmembrane emp24 domain-containing protein 5;
                     p24 family protein gamma-2; transmembrane emp24 protein
                     transport domain containing 5"
                     /calculated_mol_wt=8237
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2779
     Region          35..>100
                     /region_name="EMP24_GP25L"
                     /note="emp24/gp25L/p24 family/GOLD; pfam01105"
                     /db_xref="CDD:426051"
     CDS             1..100
                     /gene="Tmed5"
                     /gene_synonym="3110020O18Rik; 4432412D15Rik; p24gamma2"
                     /coded_by="NM_001347383.2:197..499"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS84924.1"
                     /db_xref="GeneID:73130"
                     /db_xref="MGI:MGI:1921586"
ORIGIN      
        1 mggrmwlpfp vlllsalpaa llrgaagftp sldsdftftl pagrkecfyq pmplkaslei
       61 eyqvldggel didfhltspe grtlvfeqrk sdgvhtisit
//
LOCUS       NP_003144                847 aa            linear   PRI 27-APR-2025
DEFINITION  signal transducer and activator of transcription 6 isoform 1 [Homo
            sapiens].
ACCESSION   NP_003144
VERSION     NP_003144.3
DBSOURCE    REFSEQ: accession NM_003153.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Eschbacher,K.L., Tran,Q.T., Moskalev,E.A., Jenkins,S., Fritchie,K.,
            Stoehr,R., Caron,A., Link,M.J., Brown,P.D., Guajardo,A., Brat,D.J.,
            Wu,A., Santagata,S., Louis,D.N., Brastianos,P.K., Kaplan,A.B.,
            Alexander,B., Rossi,S., Ferrarese,F., Raleigh,D.R., Nguyen,M.P.,
            Gross,J., Velazquez Vega,J., Rodriguez,F., Perry,A.,
            Martinez-Lage,M., Orr,B.A., Haller,F. and Giannini,C.
  TITLE     NAB2::STAT6 fusions and genome-wide DNA methylation profiling:
            Predictors of patient outcomes in meningeal solitary fibrous tumors
  JOURNAL   Brain Pathol 34 (6), e13256 (2024)
   PUBMED   38523251
  REMARK    GeneRIF: NAB2::STAT6 fusions and genome-wide DNA methylation
            profiling: Predictors of patient outcomes in meningeal solitary
            fibrous tumors.
REFERENCE   2  (residues 1 to 847)
  AUTHORS   de Juan,A., Tabtim-On,D., Coillard,A., Becher,B., Goudot,C. and
            Segura,E.
  TITLE     The aryl hydrocarbon receptor shapes monocyte transcriptional
            responses to interleukin-4 by prolonging STAT6 binding to promoters
  JOURNAL   Sci Signal 17 (858), eadn6324 (2024)
   PUBMED   39405377
  REMARK    GeneRIF: The aryl hydrocarbon receptor shapes monocyte
            transcriptional responses to interleukin-4 by prolonging STAT6
            binding to promoters.
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Deng,C., Huo,M., Chu,H., Zhuang,X., Deng,G., Li,W., Wei,H.,
            Zeng,L., He,Y., Liu,H., Li,J., Zhang,C. and Chen,H.
  TITLE     Exosome circATP8A1 induces macrophage M2 polarization by regulating
            the miR-1-3p/STAT6 axis to promote gastric cancer progression
  JOURNAL   Mol Cancer 23 (1), 49 (2024)
   PUBMED   38459596
  REMARK    GeneRIF: Exosome circATP8A1 induces macrophage M2 polarization by
            regulating the miR-1-3p/STAT6 axis to promote gastric cancer
            progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Benoit,A., Abraham,M.J., Li,S., Kim,J., Estrada-Tejedor,R.,
            Bakadlag,R., Subramaniam,N., Makhani,K., Guilbert,C., Tu,R.,
            Salaciak,M., Klein,K.O., Coyle,K.M., Hilton,L.K., Santiago,R.,
            Dmitrienko,S., Assouline,S., Morin,R.D., Del Rincon,S.V.,
            Johnson,N.A. and Mann,K.K.
  TITLE     STAT6 mutations enriched at diffuse large B-cell lymphoma relapse
            reshape the tumor microenvironment
  JOURNAL   Int J Hematol 119 (3), 275-290 (2024)
   PUBMED   38285120
  REMARK    GeneRIF: STAT6 mutations enriched at diffuse large B-cell lymphoma
            relapse reshape the tumor microenvironment.
REFERENCE   5  (residues 1 to 847)
  AUTHORS   Tolomeo,M. and Cascio,A.
  TITLE     STAT4 and STAT6, their role in cellular and humoral immunity and in
            diverse human diseases
  JOURNAL   Int Rev Immunol 43 (6), 394-418 (2024)
   PUBMED   39188021
  REMARK    GeneRIF: STAT4 and STAT6, their role in cellular and humoral
            immunity and in diverse human diseases.
            Review article
REFERENCE   6  (residues 1 to 847)
  AUTHORS   Shimoda,K., van Deursen,J., Sangster,M.Y., Sarawar,S.R.,
            Carson,R.T., Tripp,R.A., Chu,C., Quelle,F.W., Nosaka,T.,
            Vignali,D.A., Doherty,P.C., Grosveld,G., Paul,W.E. and Ihle,J.N.
  TITLE     Lack of IL-4-induced Th2 response and IgE class switching in mice
            with disrupted Stat6 gene
  JOURNAL   Nature 380 (6575), 630-633 (1996)
   PUBMED   8602264
REFERENCE   7  (residues 1 to 847)
  AUTHORS   Takeda,K., Tanaka,T., Shi,W., Matsumoto,M., Minami,M.,
            Kashiwamura,S., Nakanishi,K., Yoshida,N., Kishimoto,T. and Akira,S.
  TITLE     Essential role of Stat6 in IL-4 signalling
  JOURNAL   Nature 380 (6575), 627-630 (1996)
   PUBMED   8602263
REFERENCE   8  (residues 1 to 847)
  AUTHORS   Quelle,F.W., Shimoda,K., Thierfelder,W., Fischer,C., Kim,A.,
            Ruben,S.M., Cleveland,J.L., Pierce,J.H., Keegan,A.D., Nelms,K. et
            al.
  TITLE     Cloning of murine Stat6 and human Stat6, Stat proteins that are
            tyrosine phosphorylated in responses to IL-4 and IL-3 but are not
            required for mitogenesis
  JOURNAL   Mol Cell Biol 15 (6), 3336-3343 (1995)
   PUBMED   7760829
REFERENCE   9  (residues 1 to 847)
  AUTHORS   Hou,J., Schindler,U., Henzel,W.J., Ho,T.C., Brasseur,M. and
            McKnight,S.L.
  TITLE     An interleukin-4-induced transcription factor: IL-4 Stat
  JOURNAL   Science 265 (5179), 1701-1706 (1994)
   PUBMED   8085155
REFERENCE   10 (residues 1 to 847)
  AUTHORS   Kotanides,H. and Reich,N.C.
  TITLE     Requirement of tyrosine phosphorylation for rapid activation of a
            DNA binding factor by IL-4
  JOURNAL   Science 262 (5137), 1265-1267 (1993)
   PUBMED   7694370
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC005823.2, AC023237.34 and
            AI082533.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 1, 2002 this sequence version replaced NP_003144.2.
            
            Summary: The protein encoded by this gene is a member of the STAT
            family of transcription factors. In response to cytokines and
            growth factors, STAT family members are phosphorylated by the
            receptor associated kinases, and then form homo- or heterodimers
            that translocate to the cell nucleus where they act as
            transcription activators. This protein plays a central role in
            exerting IL4 mediated biological responses. It is found to induce
            the expression of BCL2L1/BCL-X(L), which is responsible for the
            anti-apoptotic activity of IL4. Knockout studies in mice suggested
            the roles of this gene in differentiation of T helper 2 (Th2)
            cells, expression of cell surface markers, and class switch of
            immunoglobulins. Alternative splicing results in multiple
            transcript variants.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' UTR compared to variant 1. Variants 1, 2 and 3 encode the
            same protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC075852.1, U16031.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300134.8/ ENSP00000300134.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..847
                     /product="signal transducer and activator of transcription
                     6 isoform 1"
                     /note="STAT, interleukin4-induced; transcription factor
                     IL-4 STAT; signal transducer and activator of
                     transcription 6, interleukin-4 induced"
                     /calculated_mol_wt=94004
     Region          2..115
                     /region_name="STAT_int"
                     /note="STAT protein, protein interaction domain;
                     smart00964"
                     /db_xref="CDD:214942"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P42226.1)"
     Region          105..276
                     /region_name="STAT6_CCD"
                     /note="Coiled-coil domain of Signal Transducer and
                     Activator of Transcription 6 (STAT6); cd16856"
                     /db_xref="CDD:341081"
     Region          273..432
                     /region_name="STAT6_DBD"
                     /note="DNA-binding domain of Signal Transducer and
                     Activator of Transcription 6 (STAT6); cd16850"
                     /db_xref="CDD:341088"
     Site            order(284,287..288,367,370,373..374,378..379,414..415,418)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:341088"
     Region          517..646
                     /region_name="SH2_STAT6"
                     /note="Src homology 2 (SH2) domain found in signal
                     transducer and activator of transcription (STAT) 6
                     proteins; cd10377"
                     /db_xref="CDD:198240"
     Site            order(544,562,588,590)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198240"
     Site            order(589,605)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198240"
     Site            order(599..600,646)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:198240"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK.
                     /evidence=ECO:0000269|PubMed:27796300; propagated from
                     UniProtKB/Swiss-Prot (P42226.1)"
     Region          655..847
                     /region_name="STAT6_C"
                     /note="STAT6 C-terminal; pfam14596"
                     /db_xref="CDD:291272"
     Region          802..806
                     /region_name="LXXLL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P42226.1)"
     Region          809..847
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42226.1)"
     CDS             1..847
                     /gene="STAT6"
                     /gene_synonym="D12S1644; HIES6; IL-4-STAT; STAT6B; STAT6C"
                     /coded_by="NM_003153.5:256..2799"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8931.1"
                     /db_xref="GeneID:6778"
                     /db_xref="HGNC:HGNC:11368"
                     /db_xref="MIM:601512"
ORIGIN      
        1 mslwglvskm ppekvqrlyv dfpqhlrhll gdwlesqpwe flvgsdafcc nlasallsdt
       61 vqhlqasvge qgegstilqh istlesiyqr dplklvatfr qilqgekkav meqfrhlpmp
      121 fhwkqeelkf ktglrrlqhr vgeihllrea lqkgaeagqv slhslietpa ngtgpseala
      181 mllqettgel eaakalvlkr iqiwkrqqql agngapfees laplqerces lvdiysqlqq
      241 evgaaggele pktrasltgr ldevlrtlvt scflvekqpp qvlktqtkfq agvrfllglr
      301 flgapakppl vradmvtekq arelsvpqgp gagaestgei inntvplens ipgnccsalf
      361 knlllkkikr cerkgtesvt eekcavlfsa sftlgpgklp iqlqalslpl vvivhgnqdn
      421 nakatilwdn afsemdrvpf vvaervpwek mcetlnlkfm aevgtnrgll pehflflaqk
      481 ifndnslsme afqhrsvsws qfnkeillgr gftfwqwfdg vldltkrclr sywsdrliig
      541 fiskqyvtsl llnepdgtfl lrfsdseigg itiahvirgq dgspqieniq pfsakdlsir
      601 slgdrirdla qlknlypkkp kdeafrshyk peqmgkdgrg yvpatikmtv erdqplptpe
      661 lqmptmvpsy dlgmapdssm smqlgpdmvp qvypphshsi ppyqglspee svnvlsafqe
      721 phlqmppslg qmslpfdqph pqgllpcqpq ehavsspdpl lcsdvtmved sclsqpvtaf
      781 pqgtwigedi fppllppteq dltklllegq gesgggslga qpllqpshyg qsgismshmd
      841 lranpsw
//
LOCUS       NP_001349650             448 aa            linear   ROD 27-APR-2025
DEFINITION  BUB3-interacting and GLEBS motif-containing protein ZNF207 isoform
            5 [Mus musculus].
ACCESSION   NP_001349650 XP_017169998
VERSION     NP_001349650.1
DBSOURCE    REFSEQ: accession NM_001362721.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Malla,S., Prasad Bhattarai,D., Groza,P., Melguizo-Sanchis,D.,
            Atanasoai,I., Martinez-Gamero,C., Roman,A.C., Zhu,D., Lee,D.F.,
            Kutter,C. and Aguilo,F.
  TITLE     ZFP207 sustains pluripotency by coordinating OCT4 stability,
            alternative splicing and RNA export
  JOURNAL   EMBO Rep 23 (3), e53191 (2022)
   PUBMED   35037361
  REMARK    GeneRIF: ZFP207 sustains pluripotency by coordinating OCT4
            stability, alternative splicing and RNA export.
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Zhang,J., Liu,W., Li,G., Xu,C., Nie,X., Qin,D., Wang,Q., Lu,X.,
            Liu,J. and Li,L.
  TITLE     BCAS2 is involved in alternative splicing and mouse oocyte
            development
  JOURNAL   FASEB J 36 (2), e22128 (2022)
   PUBMED   34972250
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Wang,A., Wang,J., Tian,K., Huo,D., Ye,H., Li,S., Zhao,C., Zhang,B.,
            Zheng,Y., Xu,L., Hua,X., Wang,K., Wu,Q.F., Wu,X., Zeng,T., Liu,Y.
            and Zhou,Y.
  TITLE     An epigenetic circuit controls neurogenic programs during neocortex
            development
  JOURNAL   Development 148 (22) (2021)
   PUBMED   35020876
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Tamplin,O.J., Kinzel,D., Cox,B.J., Bell,C.E., Rossant,J. and
            Lickert,H.
  TITLE     Microarray analysis of Foxa2 mutant mouse embryos reveals novel
            gene expression and inductive roles for the gastrula organizer and
            its derivatives
  JOURNAL   BMC Genomics 9, 511 (2008)
   PUBMED   18973680
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Misawa,K., Nosaka,T., Morita,S., Kaneko,A., Nakahata,T., Asano,S.
            and Kitamura,T.
  TITLE     A method to identify cDNAs based on localization of green
            fluorescent protein fusion products
  JOURNAL   Proc Natl Acad Sci U S A 97 (7), 3062-3066 (2000)
   PUBMED   10716735
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Taguchi,E., Muramatsu,H., Fan,Q.W., Kurosawa,N., Sobue,G. and
            Muramatsu,T.
  TITLE     Zep: A novel zinc finger protein containing a large proline-rich
            domain
  JOURNAL   J Biochem 124 (6), 1220-1228 (1998)
   PUBMED   9832628
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591146.21 and DV661373.1.
            
            On Apr 26, 2018 this sequence version replaced XP_017169998.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3509630.1,
                                           SRR1660817.53620.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 47.83 cM"
     Protein         1..448
                     /product="BUB3-interacting and GLEBS motif-containing
                     protein ZNF207 isoform 5"
                     /note="49 kDa zinc finger protein; BUB3-interacting and
                     GLEBS motif-containing protein ZNF207"
                     /calculated_mol_wt=47718
     Region          10..90
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          13..34
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          13..32
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(18,24,31,33,36,43)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          37..58
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          37..58
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <390..425
                     /region_name="SMN"
                     /note="Survival motor neuron protein (SMN); pfam06003"
                     /db_xref="CDD:428716"
     CDS             1..448
                     /gene="Zfp207"
                     /gene_synonym="8430401D15Rik; BuGZ; Zep; Znf207"
                     /coded_by="NM_001362721.1:177..1523"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:22680"
                     /db_xref="MGI:MGI:1340045"
ORIGIN      
        1 mgrkkkkqlk pwcwycnrdf ddekiliqhq kakhfkchic hkklytgpgl aihcmqvhke
       61 tidavpnaip grtdieleiy gmegipekdm derrrlleqk tqesqkkkqq ddsdeyddde
      121 saastsfqpq pvqpqqgyip pmaqpglppv pgapgmppgi pplmpgvppl mpgmppvmpg
      181 mppgmmpmgg mmppgpgipp lmpgmppgmp ppvprpgipp mtqaqavsap gilnrppapt
      241 aavpapqppv tkplfpsagq aqaavqgpvg tdfkplnstp aattteppkp tfpaytqsta
      301 sttsttnsta akpaasitsk patltttsat sklihpdedi sleerraqlp kyqrnlprpg
      361 qtpignppvg piggmmppqp glpqqqamrp pmpphgqygg hhqgmpgylp gamppygqgp
      421 pmvppyqggp prppmgmrpp vmsqggry
//
LOCUS       NP_006074                557 aa            linear   PRI 27-APR-2025
DEFINITION  protein Red [Homo sapiens].
ACCESSION   NP_006074 NP_004502
VERSION     NP_006074.2
DBSOURCE    REFSEQ: accession NM_006083.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 557)
  AUTHORS   von Elsner,L., Chai,G., Schneeberger,P.E., Harms,F.L., Casar,C.,
            Qi,M., Alawi,M., Abdel-Salam,G.M.H., Zaki,M.S., Arndt,F., Yang,X.,
            Stanley,V., Hempel,M., Gleeson,J.G. and Kutsche,K.
  TITLE     Biallelic FRA10AC1 variants cause a neurodevelopmental disorder
            with growth retardation
  JOURNAL   Brain 145 (4), 1551-1563 (2022)
   PUBMED   34694367
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Gao,C., Han,Y., Bai,L., Wang,Y. and Xue,F.
  TITLE     IK: A novel cell mitosis regulator that contributes to
            carcinogenesis
  JOURNAL   Cell Biochem Funct 39 (7), 854-859 (2021)
   PUBMED   34250629
  REMARK    GeneRIF: IK: A novel cell mitosis regulator that contributes to
            carcinogenesis.
            Review article
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Willers,J., Haffner,A., Zepter,K., Storz,M., Urosevic,M., Burg,G.
            and Dummer,R.
  TITLE     The interferon inhibiting cytokine IK is overexpressed in cutaneous
            T cell lymphoma derived tumor cells that fail to upregulate major
            histocompatibility complex class II upon interferon-gamma
            stimulation
  JOURNAL   J Invest Dermatol 116 (6), 874-879 (2001)
   PUBMED   11407974
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Assier,E., Bouzinba-Segard,H., Stolzenberg,M.C., Stephens,R.,
            Bardos,J., Freemont,P., Charron,D., Trowsdale,J. and Rich,T.
  TITLE     Isolation, sequencing and expression of RED, a novel human gene
            encoding an acidic-basic dipeptide repeat
  JOURNAL   Gene 230 (2), 145-154 (1999)
   PUBMED   10216252
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Cao,L.X., Le Bousse-Kerdiles,M.C., Clay,D., Oshevski,S., Jasmin,C.
            and Krief,P.
  TITLE     Implication of a new molecule IK in CD34+ hematopoietic progenitor
            cell proliferation and differentiation
  JOURNAL   Blood 89 (10), 3615-3623 (1997)
   PUBMED   9160666
REFERENCE   10 (residues 1 to 557)
  AUTHORS   Krief,P., Augery-Bourget,Y., Plaisance,S., Merck,M.F., Assier,E.,
            Tanchou,V., Billard,M., Boucheix,C., Jasmin,C. and Azzarone,B.
  TITLE     A new cytokine (IK) down-regulating HLA class II: monoclonal
            antibodies, cloning and chromosome localization
  JOURNAL   Oncogene 9 (12), 3449-3456 (1994)
   PUBMED   7970704
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF182645.1, BC071964.1 and
            BC013005.2.
            
            On Feb 16, 2007 this sequence version replaced NP_006074.1.
            
            Summary: The protein encoded by this gene was identified by its RED
            repeat, a stretch of repeated arginine, glutamic acid and aspartic
            acid residues. The protein localizes to discrete dots within the
            nucleus, excluding the nucleolus. Its function is unknown. This
            gene maps to chromosome 5; however, a pseudogene may exist on
            chromosome 2. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.680642.1,
                                           SRR3476690.957447.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000417647.7/ ENSP00000396301.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..557
                     /product="protein Red"
                     /note="RD element; prer protein; IK factor; IK cytokine,
                     down-regulator of HLA II; chondrosarcoma-associated
                     protein 2; cytokine IK"
                     /calculated_mol_wt=65471
     Region          1..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13123.3)"
     Region          84..295
                     /region_name="RED_N"
                     /note="RED-like protein N-terminal region; pfam07808"
                     /db_xref="CDD:462273"
     Site            98
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1M8; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Region          181..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13123.3)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Region          294..403
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13123.3)"
     Region          342..375
                     /region_name="17 X 2 AA tandem repeats of R-[ED]"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13123.3)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Region          445..549
                     /region_name="RED_C"
                     /note="RED-like protein C-terminal region; pfam07807"
                     /db_xref="CDD:462272"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     CDS             1..557
                     /gene="IK"
                     /gene_synonym="CSA2; RED; RER"
                     /coded_by="NM_006083.4:81..1754"
                     /db_xref="CCDS:CCDS47280.1"
                     /db_xref="GeneID:3550"
                     /db_xref="HGNC:HGNC:5958"
                     /db_xref="MIM:600549"
ORIGIN      
        1 mperdsepfs nplapdghdv ddphsfhqsk ltnedfrkll mtpraaptsa ppsksrhhem
       61 preynededp aarrrkkksy yaklrqqeie rerelaekyr drakerrdgv nkdyeeteli
      121 sttanyravg ptaeadksaa ekrrqliqes kflggdmeht hlvkgldfal lqkvraeias
      181 kekeeeelme kpqketkkde dpenkiefkt rlgrnvyrml fkskayerne lflpgrmayv
      241 vdlddeyadt dipttlirsk adcptmeaqt tlttndivis kltqilsylr qgtrnkklkk
      301 kdkgkleekk ppeadmnife digdyvpstt ktprdkerer yrererdrer drdrdrerer
      361 erdrererer drereeekkr hsyfekpkvd depmdvdkgp gstkeliksi nekfagsagw
      421 egteslkkpe dkkqlgdffg msnsyaecyp atmddmavds deevdyskmd qgnkkgplgr
      481 wdfdtqeeys eymnnkealp kaafqygikm segrktrrfk etndkaeldr qwkkisaiie
      541 krkkmeadgv evkrpky
//
LOCUS       NP_001139806            1562 aa            linear   PRI 27-APR-2025
DEFINITION  NAC-alpha domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_001139806 XP_001126176 XP_001133202 XP_001717233 XP_002342744
            XP_002344315 XP_002346024 XP_002346914 XP_166571
VERSION     NP_001139806.1
DBSOURCE    REFSEQ: accession NM_001146334.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1562)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC013416.4, EG328798.1, AB002361.1, BM728120.1 and BM680676.1.
            
            On or before Aug 27, 2009 this sequence version replaced
            XP_002342744.1, XP_002344315.1, XP_002346024.1, XP_002346914.1,
            XP_166571.5, XP_001126176.2, XP_001133202.2, XP_001717233.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000490531.3/ ENSP00000420477.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..1562
                     /product="NAC-alpha domain-containing protein 1"
                     /EC_number="5.3.99.3"
                     /calculated_mol_wt=160971
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15069.3)"
     Region          56..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15069.3)"
     Region          131..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15069.3)"
     Region          249..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15069.3)"
     Region          327..365
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15069.3)"
     Region          381..458
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15069.3)"
     Region          503..941
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15069.3)"
     Region          <575..1032
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          897..>1186
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          953..1423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15069.3)"
     Site            1068
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O15069.3)"
     Region          <1079..1295
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Site            1354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SWP3; propagated from
                     UniProtKB/Swiss-Prot (O15069.3)"
     Region          1425..1472
                     /region_name="NAC_NACA"
                     /note="nascent polypeptide-associated complex (NAC), alpha
                     subunit; cd22054"
                     /db_xref="CDD:409233"
     Site            order(1429,1431..1441,1452,1459..1467,1472)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409233"
     Region          1519..1562
                     /region_name="UBA_NACAD"
                     /note="UBA-like domain found in nascent
                     polypeptide-associated complex subunit alpha
                     domain-containing protein 1 (NACAD); cd14416"
                     /db_xref="CDD:270599"
     CDS             1..1562
                     /gene="NACAD"
                     /coded_by="NM_001146334.2:76..4764"
                     /db_xref="CCDS:CCDS47582.1"
                     /db_xref="GeneID:23148"
                     /db_xref="HGNC:HGNC:22196"
                     /db_xref="MIM:619419"
ORIGIN      
        1 mpgeaarael llpeadrpgp rtdlscdaaa attilggdrr epcaltpgps hlaltflpsk
       61 pgarpqpega swdagpggap sawadpgegg pspmllpegl ssqalsteap lpatlepriv
      121 mgeetcqall spraartalr dqegghaspd pppelcsqgd lsvpspppdp dsfftppstp
      181 tkttyallpa cgphgdards eaelrdelld sppaspsgsy itadgdswas spscslslla
      241 paegldfpsg wglspqgsmv derelhpagt peppssessl sadsssswgq eghffdldfl
      301 andpmipaal lpfqgslifq veavevtpls peeeeeeava dpdpggdlag egeedstsas
      361 flqslsdlsi tegmdeafaf rddtsaassd sdsasyaead derlysgeph aqatllqdsv
      421 qkteeesggg akglqaqdgt vswaveaapq tsdrgaylsq rqelisevte eglalgqest
      481 atvtphtlqv apglqvevat rvtpqageee tdstagqesa amampqpsqe giseilgqes
      541 vtaeklptpq eetsltlcpd spqnlkeegg ldlpsgrkpv aaativprqa kedltlpqds
      601 amtpplplqd tdlssapkpv aaativsqqa eegltlpqds vmtpplplqd telssapkpv
      661 aaatlvsqqa eegltlpqds amtpplplqd tdlssapkpv aaatlvsqqa eegltlpqds
      721 amtpplplqd tdlssapkpv aaatlvsqqa eegltlpqds amtpplplqd tdlssapkpv
      781 aaativsqqa eegltlpqds amtpplplqd tdlssapkpv aaativsqqa eegltlpqds
      841 amtpplplqd tdlssapkpv aaatpvsqqa eegltlpqds amtpplplqd tdlssapkpv
      901 aaatpvsqqa eegltlpqds amtaplplqd tgptsgpepl avatpqtlqa eagcapgtep
      961 vatmaqqevg ealgprpape eknaalptvp epaaldqvqq ddpqpaaeag tpwaaqedad
     1021 stlgmealsl pepasgagee iaealsrpgr eaclearaht gdgakpdspq ketlevenqq
     1081 egglkplaqe hgprsalgga revpdappaa cpevsqarll spareergls gkstpeptlp
     1141 savateasld scpessvgav ssldrgcpda paptsaptsq qpepvlglgs veqphevpsv
     1201 lgtpllqppe nlakgqpstp vdrplgpdps apgtlagaal ppleppapcl cqdpqedsve
     1261 deeppgslgl pppqagvqpa aaavsgttqp lgtgprvsls phspllspkv asmdakdlal
     1321 qilppcqvpp psgpqspagp qglsapeqqe dedsleedsp ralgsgqhsd shgessaeld
     1381 eqdilapqtv qcpaqapagg seetiakakq srsekkarka msklglrqiq gvtritiqks
     1441 knilfviakp dvfkspasdt yvvfgeakie dlsqqvhkaa aekfkvpsep salvpesapr
     1501 prvrleckee eeeeeeevde aglelrdiel vmaqanvsra kavralrdnh sdivnaimel
     1561 tm
//
LOCUS       NP_075392                525 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein SOWAHC [Homo sapiens].
ACCESSION   NP_075392
VERSION     NP_075392.2
DBSOURCE    REFSEQ: accession NM_023016.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Zhu,Q., Wang,J., Zhang,Q., Wang,F., Fang,L., Song,B., Xie,C. and
            Liu,J.
  TITLE     Methylation-driven genes PMPCAP1, SOWAHC and ZNF454 as potential
            prognostic biomarkers in lung squamous cell carcinoma
  JOURNAL   Mol Med Rep 21 (3), 1285-1295 (2020)
   PUBMED   32016477
  REMARK    GeneRIF: Methylationdriven genes PMPCAP1, SOWAHC and ZNF454 as
            potential prognostic biomarkers in lung squamous cell carcinoma.
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Maeso,I., Irimia,M., Tena,J.J., Gonzalez-Perez,E., Tran,D.,
            Ravi,V., Venkatesh,B., Campuzano,S., Gomez-Skarmeta,J.L. and
            Garcia-Fernandez,J.
  TITLE     An ancient genomic regulatory block conserved across bilaterians
            and its dismantling in tetrapods by retrogene replacement
  JOURNAL   Genome Res 22 (4), 642-655 (2012)
   PUBMED   22234889
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC066772.1, AC011753.6, AK023346.1 and AK025523.1.
            
            On Oct 23, 2004 this sequence version replaced NP_075392.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK025523.1, BC066772.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356454.5/ ENSP00000365830.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..525
                     /product="ankyrin repeat domain-containing protein SOWAHC"
                     /note="ankyrin repeat domain-containing protein 57;
                     ankyrin repeat domain 57; protein sosondowah homolog C"
                     /calculated_mol_wt=55541
     Region          <5..203
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          84..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53LP3.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0J6; propagated from
                     UniProtKB/Swiss-Prot (Q53LP3.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53LP3.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q53LP3.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q53LP3.1)"
     Region          301..330
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53LP3.1)"
     Region          <302..393
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          302..338
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          340..372
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          340..370
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53LP3.1)"
     Region          434..525
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53LP3.1)"
     CDS             1..525
                     /gene="SOWAHC"
                     /gene_synonym="ANKRD57; C2orf26"
                     /coded_by="NM_023016.4:127..1704"
                     /db_xref="CCDS:CCDS33270.1"
                     /db_xref="GeneID:65124"
                     /db_xref="HGNC:HGNC:26149"
ORIGIN      
        1 megpaewgpe aalgpeavlr flaerggral haelvqhfrg alggepeqra rarahfkelv
       61 navatvrvdp adgakyvhlk krfcegpsep sgdppriqvt aepeapdgpa gpeardrlpd
      121 aaapeslpgq grelgegepp apahwpplsa garrknsrrd vqplprtpap gpsedlelpp
      181 hgceeadrgs slvgataqrp arqnlrdlvm gsspqlkrsv cpggsspgss sgggrgrggg
      241 dsdsasvass saeeessggg svtldpleha wmlsasdgkw dsleglltce pgllvkrdfi
      301 tgftclhwaa khgrqellam lvnfankhql pvnidartsg gytalhlaam hghvevvkll
      361 vgaydadvdi rdysgkkasq ylsrsiaeei knlvgaldeg dgesaagsgg grwrlskvlp
      421 shlityklsh aledggdhhh hhhsaegwvg gkakdpgrka sgsssgrikp rlnkirfrtq
      481 ivhttpsfrd peqplegrge egvgeerpvk ghspftlrpk snvfg
//
LOCUS       NP_001357270             215 aa            linear   PRI 27-APR-2025
DEFINITION  high mobility group protein B1 isoform 1 [Homo sapiens].
ACCESSION   NP_001357270 XP_024305110
VERSION     NP_001357270.1
DBSOURCE    REFSEQ: accession NM_001370341.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wang,S., Cheng,T., Chen,X., Zeng,C., Qin,W. and Xu,Y.
  TITLE     IFN-gamma induces acute graft-versus-host disease by promoting
            HMGB1-mediated nuclear-to-cytoplasm translocation and autophagic
            degradation of p53
  JOURNAL   Clin Sci (Lond) 138 (20), 1287-1304 (2024)
   PUBMED   39312196
  REMARK    GeneRIF: IFN-gamma induces acute graft-versus-host disease by
            promoting HMGB1-mediated nuclear-to-cytoplasm translocation and
            autophagic degradation of p53.
REFERENCE   2  (residues 1 to 215)
  AUTHORS   De Luca,G., Goette,N.P., Lev,P.R., Baroni Pietto,M.C., Marin
            Oyarzun,C.P., Castro Rios,M.A., Moiraghi,B., Sackmann,F.,
            Kamiya,L.J., Verri,V., Caula,V., Fernandez,V., Vicente,A., Pose
            Cabarcos,J., Caruso,V., Camacho,M.F., Larripa,I.B., Khoury,M.,
            Marta,R.F., Glembotsky,A.C. and Heller,P.G.
  TITLE     Elevated levels of damage-associated molecular patterns HMGB1 and
            S100A8/A9 coupled with toll-like receptor-triggered monocyte
            activation are associated with inflammation in patients with
            myelofibrosis
  JOURNAL   Front Immunol 15, 1365015 (2024)
   PUBMED   39391311
  REMARK    GeneRIF: Elevated levels of damage-associated molecular patterns
            HMGB1 and S100A8/A9 coupled with toll-like receptor-triggered
            monocyte activation are associated with inflammation in patients
            with myelofibrosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Ozbay Kurt,F.G., Cicortas,B.A., Balzasch,B.M., De la Torre,C.,
            Ast,V., Tavukcuoglu,E., Ak,C., Wohlfeil,S.A., Cerwenka,A.,
            Utikal,J. and Umansky,V.
  TITLE     S100A9 and HMGB1 orchestrate MDSC-mediated immunosuppression in
            melanoma through TLR4 signaling
  JOURNAL   J Immunother Cancer 12 (9), e009552 (2024)
   PUBMED   39266214
  REMARK    GeneRIF: S100A9 and HMGB1 orchestrate MDSC-mediated
            immunosuppression in melanoma through TLR4 signaling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Gao,P., Wu,Y. and Yan,Z.
  TITLE     LncRNA ILF3-AS1 mediates oxidative stress and inflammation through
            miR-504-3p/HMGB1 axis in a cellular model of temporal lobe epilepsy
  JOURNAL   Brain Behav 14 (8), e3615 (2024)
   PUBMED   39135276
  REMARK    GeneRIF: LncRNA ILF3-AS1 mediates oxidative stress and inflammation
            through miR-504-3p/HMGB1 axis in a cellular model of temporal lobe
            epilepsy.
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Ferrari,S., Finelli,P., Rocchi,M. and Bianchi,M.E.
  TITLE     The active gene that encodes human high mobility group 1 protein
            (HMG1) contains introns and maps to chromosome 13
  JOURNAL   Genomics 35 (2), 367-371 (1996)
   PUBMED   8661151
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Ge,H. and Roeder,R.G.
  TITLE     The high mobility group protein HMG1 can reversibly inhibit class
            II gene transcription by interaction with the TATA-binding protein
  JOURNAL   J Biol Chem 269 (25), 17136-17140 (1994)
   PUBMED   8006019
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Paull,T.T., Haykinson,M.J. and Johnson,R.C.
  TITLE     The nonspecific DNA-binding and -bending proteins HMG1 and HMG2
            promote the assembly of complex nucleoprotein structures
  JOURNAL   Genes Dev 7 (8), 1521-1534 (1993)
   PUBMED   8339930
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Parkkinen,J. and Rauvala,H.
  TITLE     Interactions of plasminogen and tissue plasminogen activator (t-PA)
            with amphoterin. Enhancement of t-PA-catalyzed plasminogen
            activation by amphoterin
  JOURNAL   J Biol Chem 266 (25), 16730-16735 (1991)
   PUBMED   1909331
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Wen,L., Huang,J.K., Johnson,B.H. and Reeck,G.R.
  TITLE     A human placental cDNA clone that encodes nonhistone chromosomal
            protein HMG-1
  JOURNAL   Nucleic Acids Res 17 (3), 1197-1214 (1989)
   PUBMED   2922262
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Bernues,J., Espel,E. and Querol,E.
  TITLE     Identification of the core-histone-binding domains of HMG1 and HMG2
  JOURNAL   Biochim Biophys Acta 866 (4), 242-251 (1986)
   PUBMED   3697355
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353648.27.
            
            On May 7, 2019 this sequence version replaced XP_024305110.1.
            
            Summary: This gene encodes a protein that belongs to the High
            Mobility Group-box superfamily. The encoded non-histone, nuclear
            DNA-binding protein regulates transcription, and is involved in
            organization of DNA. This protein plays a role in several cellular
            processes, including inflammation, cell differentiation and tumor
            cell migration. Multiple pseudogenes of this gene have been
            identified. Alternative splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Sep
            2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1080622.1,
                                           SRR14038191.3021020.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146411, SAMEA2155974
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.3"
     Protein         1..215
                     /product="high mobility group protein B1 isoform 1"
                     /note="Sulfoglucuronyl carbohydrate binding protein;
                     Amphoterin; high-mobility group (nonhistone chromosomal)
                     protein 1; high mobility group protein B1"
                     /calculated_mol_wt=24763
     Region          1..97
                     /region_name="Sufficient for interaction with HAVCR2.
                     /evidence=ECO:0000250|UniProtKB:P63158"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          3..15
                     /region_name="LPS binding (delipidated).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          8..76
                     /region_name="HMG-box_HMGB_rpt1"
                     /note="first high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21978"
                     /db_xref="CDD:438794"
     Site            order(8..10,13,16..17,19..21,25,28,35..36,38..39,41..43,
                     45..46,50)
                     /site_type="other"
                     /note="p53 binding site [polypeptide binding]"
                     /db_xref="CDD:438794"
     Site            order(8,10..11,13..17,20..21,36,38..39,41..43,46,49)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438794"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            10..11
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin:thrombomodulin.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            12
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          27..43
                     /region_name="Nuclear localization signal (NLS) 1.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            67..68
                     /site_type="cleavage"
                     /note="Cleavage, by CASP1.
                     /evidence=ECO:0000269|PubMed:24474694; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          76..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          80..96
                     /region_name="LPS binding (Lipid A).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          89..108
                     /region_name="Cytokine-stimulating activity.
                     /evidence=ECO:0000269|PubMed:12765338"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            90
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          93..163
                     /region_name="HMG-box_HMGB_rpt2"
                     /note="second high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21979"
                     /db_xref="CDD:438795"
     Site            order(94..100,102..104,106..107,110,122..123,125..127,130,
                     133,152,155..156,159,162..163)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438795"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            141
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          150..183
                     /region_name="Binding to AGER/RAGE.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          161..215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            172
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            177
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          178..184
                     /region_name="Nuclear localization signal (NLS) 2.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            182
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            183
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            184
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            185
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     CDS             1..215
                     /gene="HMGB1"
                     /gene_synonym="HMG-1; HMG1; HMG3; SBP-1"
                     /coded_by="NM_001370341.1:183..830"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS9335.1"
                     /db_xref="GeneID:3146"
                     /db_xref="HGNC:HGNC:4983"
                     /db_xref="MIM:163905"
ORIGIN      
        1 mgkgdpkkpr gkmssyaffv qtcreehkkk hpdasvnfse fskkcserwk tmsakekgkf
       61 edmakadkar yeremktyip pkgetkkkfk dpnapkrpps afflfcseyr pkikgehpgl
      121 sigdvakklg emwnntaadd kqpyekkaak lkekyekdia ayrakgkpda akkgvvkaek
      181 skkkkeeeed eedeedeeee edeededeee dddde
//
LOCUS       NP_037417                731 aa            linear   PRI 27-APR-2025
DEFINITION  nucleolar GTP-binding protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_037417
VERSION     NP_037417.1
DBSOURCE    REFSEQ: accession NM_013285.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Nakamura,K., Reid,B.M., Chen,A., Chen,Z., Goode,E.L., Permuth,J.B.,
            Teer,J.K., Tyrer,J., Yu,X., Kanetsky,P.A., Pharoah,P.D.,
            Gayther,S.A., Sellers,T.A., Lawrenson,K. and Karreth,F.A.
  TITLE     Functional analysis of the 1p34.3 risk locus implicates GNL2 in
            high-grade serous ovarian cancer
  JOURNAL   Am J Hum Genet 109 (1), 116-135 (2022)
   PUBMED   34965383
  REMARK    GeneRIF: Functional analysis of the 1p34.3 risk locus implicates
            GNL2 in high-grade serous ovarian cancer.
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Dong,Y., Cai,Q., Fu,L., Liu,H., Ma,M. and Wu,X.
  TITLE     Study of the G Protein Nucleolar 2 Value in Liver Hepatocellular
            Carcinoma Treatment and Prognosis
  JOURNAL   Biomed Res Int 2021, 4873678 (2021)
   PUBMED   34337013
  REMARK    GeneRIF: Study of the G Protein Nucleolar 2 Value in Liver
            Hepatocellular Carcinoma Treatment and Prognosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Datta,D., Anbarasu,K., Rajabather,S., Priya,R.S., Desai,P. and
            Mahalingam,S.
  TITLE     Nucleolar GTP-binding Protein-1 (NGP-1) Promotes G1 to S Phase
            Transition by Activating Cyclin-dependent Kinase Inhibitor p21
            Cip1/Waf1
  JOURNAL   J Biol Chem 290 (35), 21536-21552 (2015)
   PUBMED   26203195
  REMARK    GeneRIF: NGP-1 promotes cell cycle progression through the
            activation of the p53/p21(Cip-1/Waf1) pathway.
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Casadio,A., Longman,D., Hug,N., Delavaine,L., Vallejos Baier,R.,
            Alonso,C.R. and Caceres,J.F.
  TITLE     Identification and characterization of novel factors that act in
            the nonsense-mediated mRNA decay pathway in nematodes, flies and
            mammals
  JOURNAL   EMBO Rep 16 (1), 71-78 (2015)
   PUBMED   25452588
  REMARK    GeneRIF: GNL2 and SEC13 are required for nonsense-mediated mRNA
            decay pathway in human cells.
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Matsuo,Y., Granneman,S., Thoms,M., Manikas,R.G., Tollervey,D. and
            Hurt,E.
  TITLE     Coupled GTPase and remodelling ATPase activities form a checkpoint
            for ribosome export
  JOURNAL   Nature 505 (7481), 112-116 (2014)
   PUBMED   24240281
REFERENCE   6  (residues 1 to 731)
  AUTHORS   Cheng,C.Y., Schache,M., Ikram,M.K., Young,T.L., Guggenheim,J.A.,
            Vitart,V., MacGregor,S., Verhoeven,V.J., Barathi,V.A., Liao,J.,
            Hysi,P.G., Bailey-Wilson,J.E., St Pourcain,B., Kemp,J.P.,
            McMahon,G., Timpson,N.J., Evans,D.M., Montgomery,G.W., Mishra,A.,
            Wang,Y.X., Wang,J.J., Rochtchina,E., Polasek,O., Wright,A.F.,
            Amin,N., van Leeuwen,E.M., Wilson,J.F., Pennell,C.E., van
            Duijn,C.M., de Jong,P.T., Vingerling,J.R., Zhou,X., Chen,P., Li,R.,
            Tay,W.T., Zheng,Y., Chew,M., Burdon,K.P., Craig,J.E., Iyengar,S.K.,
            Igo,R.P. Jr., Lass,J.H. Jr., Chew,E.Y., Haller,T., Mihailov,E.,
            Metspalu,A., Wedenoja,J., Simpson,C.L., Wojciechowski,R., Hohn,R.,
            Mirshahi,A., Zeller,T., Pfeiffer,N., Lackner,K.J., Bettecken,T.,
            Meitinger,T., Oexle,K., Pirastu,M., Portas,L., Nag,A.,
            Williams,K.M., Yonova-Doing,E., Klein,R., Klein,B.E.,
            Hosseini,S.M., Paterson,A.D., Makela,K.M., Lehtimaki,T.,
            Kahonen,M., Raitakari,O., Yoshimura,N., Matsuda,F., Chen,L.J.,
            Pang,C.P., Yip,S.P., Yap,M.K., Meguro,A., Mizuki,N., Inoko,H.,
            Foster,P.J., Zhao,J.H., Vithana,E., Tai,E.S., Fan,Q., Xu,L.,
            Campbell,H., Fleck,B., Rudan,I., Aung,T., Hofman,A.,
            Uitterlinden,A.G., Bencic,G., Khor,C.C., Forward,H., Parssinen,O.,
            Mitchell,P., Rivadeneira,F., Hewitt,A.W., Williams,C., Oostra,B.A.,
            Teo,Y.Y., Hammond,C.J., Stambolian,D., Mackey,D.A., Klaver,C.C.,
            Wong,T.Y., Saw,S.M. and Baird,P.N.
  CONSRTM   Consortium for Refractive Error and Myopia; Fuchs' Genetics
            Multi-Center Study Group; Wellcome Trust Case Control Consortium 2;
            Diabetes Control and Complications Trial/Epidemiology of Diabetes
            Interventions, and Complications Research Group
  TITLE     Nine loci for ocular axial length identified through genome-wide
            association studies, including shared loci with refractive error
  JOURNAL   Am J Hum Genet 93 (2), 264-277 (2013)
   PUBMED   24144296
REFERENCE   7  (residues 1 to 731)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 731)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 731)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 731)
  AUTHORS   Racevskis,J., Dill,A., Stockert,R. and Fineberg,S.A.
  TITLE     Cloning of a novel nucleolar guanosine 5'-triphosphate binding
            protein autoantigen from a breast tumor
  JOURNAL   Cell Growth Differ 7 (2), 271-280 (1996)
   PUBMED   8822211
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB452094.1, BC009250.2 and AA766044.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.126743.1,
                                           SRR3476690.1153684.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373062.8/ ENSP00000362153.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..731
                     /product="nucleolar GTP-binding protein 2 isoform 1"
                     /note="nucleolar GTPase; guanine nucleotide binding
                     protein-like 2 (nucleolar); nucleolar G-protein gene 1;
                     nucleolar GTP-binding protein 2; novel nucleolar guanosine
                     5'-triphosphate binding protein autoantigen; autoantigen
                     NGP-1; nucleostemin-2"
                     /calculated_mol_wt=83524
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13823.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13823.1)"
     Region          43..174
                     /region_name="NGP1NT"
                     /note="NGP1NT (NUC091) domain; pfam08153"
                     /db_xref="CDD:462379"
     Region          209..365
                     /region_name="NGP_1"
                     /note="A novel nucleolar GTP-binding protein, circularly
                     permuted subfamily of the Ras GTPases; cd01858"
                     /db_xref="CDD:206751"
     Site            order(255..256,258..259,284..286,319..325,364)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206751"
     Site            255..258
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206751"
     Site            284..286
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206751"
     Site            317..324
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206751"
     Site            342..349
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206751"
     Site            345
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206751"
     Site            361..364
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206751"
     Site            363..365
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206751"
     Region          481..502
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13823.1)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99LH1; propagated from
                     UniProtKB/Swiss-Prot (Q13823.1)"
     Region          555..594
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13823.1)"
     Region          630..731
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13823.1)"
     CDS             1..731
                     /gene="GNL2"
                     /gene_synonym="HUMAUANTIG; Ngp-1; NGP1; Nog2; Nug2"
                     /coded_by="NM_013285.3:116..2311"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS421.1"
                     /db_xref="GeneID:29889"
                     /db_xref="HGNC:HGNC:29925"
                     /db_xref="MIM:609365"
ORIGIN      
        1 mvkpkykgrs tinpskastn pdrvqgaggq nmrdratirr lnmyrqkerr nsrgkiikpl
       61 qyqstvasgt varvepnikw fgntrvikqs slqkfqeemd tvmkdpykvv mkqsklpmsl
      121 lhdrirphnl kvhildtesf ettfgpksqr krpnlfasdm qslienaems tesydqgkdr
      181 dlvtedtgvr neaqeeiykk gqskriwgel ykvidssdvv vqvldardpm gtrsphiety
      241 lkkekpwkhl ifvlnkcdlv ptwatkrwva vlsqdyptla fhasltnpfg kgafiqllrq
      301 fgklhtdkkq isvgfigypn vgkssvintl rskkvcnvap iagetkvwqy itlmrrifli
      361 dcpgvvypse dsetdivlkg vvqvekiksp edhigavler akpeyiskty kidswenaed
      421 fleklafrtg kllkggepdl qtvgkmvlnd wqrgripffv kppnaeplva pqllpsssle
      481 vvpeaaqnnp geevtetage gsesiikeet eenshcdant emqqiltrvr qnfgkinvvp
      541 qfsgddlvpv evsdleeele sfsdeeeeeq eqqrddaees ssepeeenvg ndtkavikal
      601 dekiakyqkf ldkakakkfs avriskglse kifakpeeqr ktleedvddr apskkgkkrk
      661 aqreeeqehs nkapraltsk errravrqqr pkkvgvryye thnvknrnrn kkktndsegq
      721 khkrkkfrqk q
//
LOCUS       NP_113680                359 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding protein 4B isoform 1 [Homo sapiens].
ACCESSION   NP_113680
VERSION     NP_113680.1
DBSOURCE    REFSEQ: accession NM_031492.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Weimann,M., Grossmann,A., Woodsmith,J., Ozkan,Z., Birth,P.,
            Meierhofer,D., Benlasfer,N., Valovka,T., Timmermann,B.,
            Wanker,E.E., Sauer,S. and Stelzl,U.
  TITLE     A Y2H-seq approach defines the human protein methyltransferase
            interactome
  JOURNAL   Nat Methods 10 (4), 339-342 (2013)
   PUBMED   23455924
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Pfuhl,T., Mamiani,A., Durr,M., Welter,S., Stieber,J., Ankara,J.,
            Liss,M., Dobner,T., Schmitt,A., Falkai,P., Kremmer,E., Jung,V.,
            Barth,S. and Grasser,F.A.
  TITLE     The LARK/RBM4a protein is highly expressed in cerebellum as
            compared to cerebrum
  JOURNAL   Neurosci Lett 444 (1), 11-15 (2008)
   PUBMED   18708123
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Guo,D., Ling,J., Wang,M.H., She,J.X., Gu,J. and Wang,C.Y.
  TITLE     Physical interaction and functional coupling between ACDP4 and the
            intracellular ion chaperone COX11, an implication of the role of
            ACDP4 in essential metal ion transport and homeostasis
  JOURNAL   Mol Pain 1, 15 (2005)
   PUBMED   15840172
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Lai,M.C., Kuo,H.W., Chang,W.C. and Tarn,W.Y.
  TITLE     A novel splicing regulator shares a nuclear import pathway with SR
            proteins
  JOURNAL   EMBO J 22 (6), 1359-1369 (2003)
   PUBMED   12628928
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ428264.1 and BC004951.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.250994.1,
                                           SRR1803616.20599.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310046.9/ ENSP00000310471.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..359
                     /product="RNA-binding protein 4B isoform 1"
                     /note="zinc finger CCHC-type and RNA binding motif 3B;
                     RNA-binding protein 4B; RNA-binding motif protein 30"
                     /calculated_mol_wt=40019
     Region          2..68
                     /region_name="RRM1_RBM4"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     RNA-binding protein 4 (RBM4); cd12606"
                     /db_xref="CDD:410018"
     Region          78..144
                     /region_name="RRM2_RBM4"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     RNA-binding protein 4 (RBM4); cd12607"
                     /db_xref="CDD:410019"
     Region          <145..>181
                     /region_name="PTZ00368"
                     /note="universal minicircle sequence binding protein
                     (UMSBP); Provisional"
                     /db_xref="CDD:173561"
     Region          161..176
                     /region_name="ZnF_C2HC"
                     /note="zinc finger; smart00343"
                     /db_xref="CDD:197667"
     Region          196..359
                     /region_name="Interaction with TNPO3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ04.1)"
     CDS             1..359
                     /gene="RBM4B"
                     /gene_synonym="RBM30; RBM4L; ZCCHC15; ZCCHC21B; ZCRB3B"
                     /coded_by="NM_031492.4:137..1216"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8149.1"
                     /db_xref="GeneID:83759"
                     /db_xref="HGNC:HGNC:28842"
                     /db_xref="MIM:621045"
ORIGIN      
        1 mvklfignlp reateqeirs lfeqygkvle cdiiknygfv hiedktaaed airnlhhykl
       61 hgvninveas knkskastkl hvgnisptct nqelrakfee ygpviecdiv kdyafvhmer
      121 aedaveairg ldntefqgkr mhvqlstsrl rtapgmgdqs gcyrcgkegh wskecpvdrt
      181 grvadfteqy neqygavrtp ytmgygesmy yndaygaldy ykryrvrsye avaaaaaasa
      241 ynyaeqtmsh lpqvqsttvt shlnstsvdp ydrhllpnsg aaatsaamaa aaattssyyg
      301 rdrsplrraa amlptvgegy gygpeselsq asaatrnsly dmaryereqy vdrarysaf
//
LOCUS       NP_001346957             380 aa            linear   ROD 27-APR-2025
DEFINITION  dematin isoform 3 [Mus musculus].
ACCESSION   NP_001346957 XP_006518603
VERSION     NP_001346957.1
DBSOURCE    REFSEQ: accession NM_001360028.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Huang,S., Reed,C., Ilsley,M., Magor,G., Tallack,M., Landsberg,M.,
            Mitchell,H., Gillinder,K. and Perkins,A.
  TITLE     Mutations in linker-2 of KLF1 impair expression of membrane
            transporters and cytoskeletal proteins causing hemolysis
  JOURNAL   Nat Commun 15 (1), 7019 (2024)
   PUBMED   39147774
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Fritz,D.I., Ding,Y., Merrill-Skoloff,G., Flaumenhaft,R., Hanada,T.
            and Chishti,A.H.
  TITLE     Dematin Regulates Calcium Mobilization, Thrombosis, and Early Akt
            Activation in Platelets
  JOURNAL   Mol Cell Biol 43 (6), 283-299 (2023)
   PUBMED   37216480
  REMARK    GeneRIF: Dematin Regulates Calcium Mobilization, Thrombosis, and
            Early Akt Activation in Platelets.
REFERENCE   3  (residues 1 to 380)
  AUTHORS   O'Neil,S.D., Racz,B., Brown,W.E., Gao,Y., Soderblom,E.J., Yasuda,R.
            and Soderling,S.H.
  TITLE     Action potential-coupled Rho GTPase signaling drives presynaptic
            plasticity
  JOURNAL   Elife 10, e63756 (2021)
   PUBMED   34269176
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Huang,Y.S., Delgadillo,L.F., Cyr,K.H., Kingsley,P.D., An,X.,
            McGrath,K.E., Mohandas,N., Conboy,J.G., Waugh,R.E., Wan,J. and
            Palis,J.
  TITLE     Circulating primitive erythroblasts establish a functional, protein
            4.1R-dependent cytoskeletal network prior to enucleating
  JOURNAL   Sci Rep 7 (1), 5164 (2017)
   PUBMED   28701737
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Lu,Y., Hanada,T., Fujiwara,Y., Nwankwo,J.O., Wieschhaus,A.J.,
            Hartwig,J., Huang,S., Han,J. and Chishti,A.H.
  TITLE     Gene disruption of dematin causes precipitous loss of erythrocyte
            membrane stability and severe hemolytic anemia
  JOURNAL   Blood 128 (1), 93-103 (2016)
   PUBMED   27073223
  REMARK    GeneRIF: results demonstrate that dematin plays a critical role in
            maintaining the fundamental properties of the membrane cytoskeleton
            complex.
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Strehl,S., Glatt,K., Liu,Q.M., Glatt,H. and Lalande,M.
  TITLE     Characterization of two novel protocadherins (PCDH8 and PCDH9)
            localized on human chromosome 13 and mouse chromosome 14
  JOURNAL   Genomics 53 (1), 81-89 (1998)
   PUBMED   9787079
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Cornwall,G.A. and Hsia,N.
  TITLE     ADAM7, a member of the ADAM (a disintegrin and metalloprotease)
            gene family is specifically expressed in the mouse anterior
            pituitary and epididymis
  JOURNAL   Endocrinology 138 (10), 4262-4272 (1997)
   PUBMED   9322939
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Malgaretti,N., Pozzoli,O., Bosetti,A., Corradi,A., Ciarmatori,S.,
            Panigada,M., Bianchi,M.E., Martinez,S. and Consalez,G.G.
  TITLE     Mmot1, a new helix-loop-helix transcription factor gene displaying
            a sharp expression boundary in the embryonic mouse brain
  JOURNAL   J Biol Chem 272 (28), 17632-17639 (1997)
   PUBMED   9211912
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Peters,L.L., Eicher,E.M., Azim,A.C. and Chishti,A.H.
  TITLE     The gene encoding the erythrocyte membrane skeleton protein dematin
            (Epb4.9) maps to mouse chromosome 14
  JOURNAL   Genomics 26 (3), 634-635 (1995)
   PUBMED   7607697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY270342.1, CX243464.1, AK158744.1, AK165204.1, BY601680.1 and
            AI413696.1.
            
            On Jan 26, 2018 this sequence version replaced XP_006518603.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660817.170442.1,
                                           SRR1660817.192820.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 36.32 cM"
     Protein         1..380
                     /product="dematin isoform 3"
                     /note="erythrocyte membrane protein band 4.9; erythrocyte
                     protein band 4.9"
                     /calculated_mol_wt=42940
     Region          7..330
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          345..380
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..380
                     /gene="Dmtn"
                     /gene_synonym="dematin; Epb4.9; Epb49"
                     /coded_by="NM_001360028.1:281..1423"
                     /note="isoform 3 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS88707.1"
                     /db_xref="GeneID:13829"
                     /db_xref="MGI:MGI:99670"
ORIGIN      
        1 merlqkakmd nqvlgykdla aipkdkaild ierpdlmiye phftyslleh velprsrecs
       61 lspkstsppp spevwaesrt lgiisqastp rttgtprtsl phfhhpettr pdsniykkpp
      121 iykqresvgg spqskhlied liiesskfpa aqppdpnqpa kietdywpcp pslavvetew
      181 rkrkasrkga eeeeeeeddd seeeikaire rqkeelskvt snlgkmilke emekslpirr
      241 ktrslpdrtp fhtslhsgts kssslpsygr ttlsrlqste fspsgseags pglqngegqr
      301 grmdrgnslp cvleqkiypy emlvvtnkgr tklppgvdrm rlerhlsaed fsrvfamspe
      361 efgklalwkr nelkkkaslf
//
LOCUS       NP_775819                421 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 584 isoform 1 [Homo sapiens].
ACCESSION   NP_775819
VERSION     NP_775819.1
DBSOURCE    REFSEQ: accession NM_173548.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Khakpour,G., Noruzinia,M., Izadi,P., Karami,F., Ahmadvand,M.,
            Heshmat,R., Amoli,M.M. and Tavakkoly-Bazzaz,J.
  TITLE     Methylomics of breast cancer: Seeking epimarkers in peripheral
            blood of young subjects
  JOURNAL   Tumour Biol 39 (3), 1010428317695040 (2017)
   PUBMED   28349825
  REMARK    GeneRIF: total of 1799 differentially methylated regions were
            identified including SLC6A3, Rab40C, ZNF584, and FOXD3 whose
            significant methylation differences were confirmed in breast cancer
            patients through quantitative real-time polymerase chain
            reaction.Methylation of those aforementioned genes in white blood
            cells of our young patients may highlight their potential as early
            epimarkers
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012313.7, DC350090.1, BC033149.1 and AK290068.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033149.1, SRR3476690.1112192.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306910.9/ ENSP00000306756.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..421
                     /product="zinc finger protein 584 isoform 1"
                     /calculated_mol_wt=48141
     Region          17..77
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          120..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVC4.1)"
     Region          161..181
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <189..374
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          216..236
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(221,223,225,227..228,231..232,235,249,251,255..256,
                     259..260,263,277,279,281,283..284,287..288,291)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          244..264
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          272..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          356..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..404
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          384..404
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          402..421
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVC4.1)"
     CDS             1..421
                     /gene="ZNF584"
                     /coded_by="NM_173548.3:500..1765"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12979.1"
                     /db_xref="GeneID:201514"
                     /db_xref="HGNC:HGNC:27318"
ORIGIN      
        1 mageaeaqld pslqglvmfe dvtvyfsree wgllnvtqkg lyrdvmlenf alvsslglap
       61 srspvftqle ddeqswvpsw vdvtpvsrae arrgfgldgl crvederahp ehlksyrviq
      121 hqdthsegkp rrhtehgaaf ppgsscgqqq evhvaeklfk csdcgkvflk afalldhlit
      181 hseerpfrcp tgrsafkksa hinprkihtg etahvcnecg kafsypsklr khqkvhtgik
      241 pfkcsdcgkt fnrkdalvlh qrihtgerpy ecskcgktfs vlstlirhrk vhigerpyec
      301 tecgkffkyn nsfilhqrvh tgerpfeckq cgkgyvtrsg lyqhwkvhtg erpyecslcg
      361 ktfttrsyrn rhqqfhteer syectecgka fkhsstllqh kkvhtperrq edrahgkvvs
      421 c
//
LOCUS       NP_001544                282 aa            linear   PRI 27-APR-2025
DEFINITION  insulin-like growth factor-binding protein 7 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001544
VERSION     NP_001544.1
DBSOURCE    REFSEQ: accession NM_001553.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   He,R., Feng,B., Zhang,Y., Li,Y., Wang,D. and Yu,L.
  TITLE     IGFBP7 promotes endothelial cell repair in the recovery phase of
            acute lung injury
  JOURNAL   Clin Sci (Lond) 138 (13), 797-815 (2024)
   PUBMED   38840498
  REMARK    GeneRIF: IGFBP7 promotes endothelial cell repair in the recovery
            phase of acute lung injury.
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Xu,Y., Sun,Y., Zhu,Y. and Song,G.
  TITLE     Structural insight into CD93 recognition by IGFBP7
  JOURNAL   Structure 32 (3), 282-291 (2024)
   PUBMED   38218180
  REMARK    GeneRIF: Structural insight into CD93 recognition by IGFBP7.
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Wang,Y., Bo,J., Zhao,Z., Han,Y., Zhang,Q. and Liu,L.
  TITLE     Depletion of Igfbp7 alleviates zebrafish NAFLD progression through
            inhibiting hepatic ferroptosis
  JOURNAL   Life Sci 332, 122086 (2023)
   PUBMED   37714372
  REMARK    GeneRIF: Depletion of Igfbp7 alleviates zebrafish NAFLD progression
            through inhibiting hepatic ferroptosis.
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Liu,F., Yu,T., Liu,J., Yang,Q., Wu,J., Ren,J. and Zhu,N.
  TITLE     IGFBP-7 secreted by adipose-derived stem cells inhibits keloid
            formation via the BRAF/MEK/ERK signaling pathway
  JOURNAL   J Dermatol Sci 111 (1), 10-19 (2023)
   PUBMED   37316358
  REMARK    GeneRIF: IGFBP-7 secreted by adipose-derived stem cells inhibits
            keloid formation via the BRAF/MEK/ERK signaling pathway.
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Liu,C.T., Wu,F.C., Zhuang,Y.X., Huang,X.Y., Li,X.H., Qu,Q.Q.,
            Peng,Y.H., Xu,Y.W., Chen,S.L. and Huang,X.C.
  TITLE     The diagnostic value of serum insulin-like growth factor binding
            protein 7 in gastric cancer
  JOURNAL   PeerJ 11, e15419 (2023)
   PUBMED   37304887
  REMARK    GeneRIF: The diagnostic value of serum insulin-like growth factor
            binding protein 7 in gastric cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Oh,Y., Nagalla,S.R., Yamanaka,Y., Kim,H.S., Wilson,E. and
            Rosenfeld,R.G.
  TITLE     Synthesis and characterization of insulin-like growth
            factor-binding protein (IGFBP)-7. Recombinant human mac25 protein
            specifically binds IGF-I and -II
  JOURNAL   J Biol Chem 271 (48), 30322-30325 (1996)
   PUBMED   8939990
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Swisshelm,K., Ryan,K., Tsuchiya,K. and Sager,R.
  TITLE     Enhanced expression of an insulin growth factor-like binding
            protein (mac25) in senescent human mammary epithelial cells and
            induced expression with retinoic acid
  JOURNAL   Proc Natl Acad Sci U S A 92 (10), 4472-4476 (1995)
   PUBMED   7538673
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Yamauchi,T., Umeda,F., Masakado,M., Isaji,M., Mizushima,S. and
            Nawata,H.
  TITLE     Purification and molecular cloning of prostacyclin-stimulating
            factor from serum-free conditioned medium of human diploid
            fibroblast cells
  JOURNAL   Biochem J 303 (Pt 2) (Pt 2), 591-598 (1994)
   PUBMED   7980422
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Akaogi,K., Okabe,Y., Funahashi,K., Yoshitake,Y., Nishikawa,K.,
            Yasumitsu,H., Umeda,M. and Miyazaki,K.
  TITLE     Cell adhesion activity of a 30-kDa major secreted protein from
            human bladder carcinoma cells
  JOURNAL   Biochem Biophys Res Commun 198 (3), 1046-1053 (1994)
   PUBMED   8117260
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Murphy,M., Pykett,M.J., Harnish,P., Zang,K.D. and George,D.L.
  TITLE     Identification and characterization of genes differentially
            expressed in meningiomas
  JOURNAL   Cell Growth Differ 4 (9), 715-722 (1993)
   PUBMED   7694637
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC066339.1, AI761388.1 and
            AC069307.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the insulin-like growth
            factor (IGF)-binding protein (IGFBP) family. IGFBPs bind IGFs with
            high affinity, and regulate IGF availability in body fluids and
            tissues and modulate IGF binding to its receptors. This protein
            binds IGF-I and IGF-II with relatively low affinity, and belongs to
            a subfamily of low-affinity IGFBPs. It also stimulates prostacyclin
            production and cell adhesion. Alternatively spliced transcript
            variants encoding different isoforms have been described for this
            gene, and one variant has been associated with retinal arterial
            macroaneurysm (PMID:21835307). [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC066339.1, S75725.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295666.6/ ENSP00000295666.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..282
                     /product="insulin-like growth factor-binding protein 7
                     isoform 1 precursor"
                     /note="angiomodulin; IGFBP-rP1; IGF-binding protein 7;
                     PGI2-stimulating factor; tumor-derived adhesion factor;
                     prostacyclin-stimulating factor"
                     /calculated_mol_wt=26443
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2705
     mat_peptide     27..282
                     /product="Insulin-like growth factor-binding protein 7.
                     /id=PRO_0000014392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16270.1)"
                     /calculated_mol_wt=26443
     Region          30..>90
                     /region_name="IGFBP"
                     /note="Insulin-like growth factor binding protein;
                     cl02472"
                     /db_xref="CDD:470586"
     Region          111..156
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Region          160..265
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:8939990; propagated from
                     UniProtKB/Swiss-Prot (Q16270.1)"
     Region          177..181
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409405"
     Region          190..194
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409405"
     Region          227..235
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409405"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (Q16270.1)"
     Region          245..250
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409405"
     Region          258..261
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409405"
     CDS             1..282
                     /gene="IGFBP7"
                     /gene_synonym="AGM; FSTL2; IBP-7; IGFBP-7; IGFBP-7v;
                     IGFBPRP1; MAC25; PSF; RAMSVPS; TAF"
                     /coded_by="NM_001553.3:35..883"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3512.1"
                     /db_xref="GeneID:3490"
                     /db_xref="HGNC:HGNC:5476"
                     /db_xref="MIM:602867"
ORIGIN      
        1 merpslrall lgaaglllll lplssssssd tcgpcepasc pplpplgcll getrdacgcc
       61 pmcargegep cggggagrgy capgmecvks rkrrkgkaga aaggpgvsgv cvcksrypvc
      121 gsdgttypsg cqlraasqra esrgekaitq vskgtceqgp sivtppkdiw nvtgaqvyls
      181 cevigiptpv liwnkvkrgh ygvqrtellp gdrdnlaiqt rggpekhevt gwvlvsplsk
      241 edageyecha snsqgqasas akitvvdalh eipvkkgega el
//
LOCUS       NP_004631                428 aa            linear   PRI 27-APR-2025
DEFINITION  spliceosome RNA helicase DDX39B [Homo sapiens].
ACCESSION   NP_004631
VERSION     NP_004631.1
DBSOURCE    REFSEQ: accession NM_004640.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Banerjee,S., Nagasawa,C.K., Widen,S.G. and Garcia-Blanco,M.A.
  TITLE     Parsing the roles of DExD-box proteins DDX39A and DDX39B in
            alternative RNA splicing
  JOURNAL   Nucleic Acids Res 52 (14), 8534-8551 (2024)
   PUBMED   38801080
  REMARK    GeneRIF: Parsing the roles of DExD-box proteins DDX39A and DDX39B
            in alternative RNA splicing.
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Fujita,K.I., Yamazaki,T., Mayeda,A. and Masuda,S.
  TITLE     Terminal regions of UAP56 and URH49 are required for their distinct
            complex formation functioning to an essential role in mRNA
            processing and export
  JOURNAL   Biochem Biophys Res Commun 703, 149682 (2024)
   PUBMED   38377942
  REMARK    GeneRIF: Terminal regions of UAP56 and URH49 are required for their
            distinct complex formation functioning to an essential role in mRNA
            processing and export.
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Fujita,K.I., Ito,M., Irie,M., Harada,K., Fujiwara,N., Ikeda,Y.,
            Yoshioka,H., Yamazaki,T., Kojima,M., Mikami,B., Mayeda,A. and
            Masuda,S.
  TITLE     Structural differences between the closely related RNA helicases,
            UAP56 and URH49, fashion distinct functional apo-complexes
  JOURNAL   Nat Commun 15 (1), 455 (2024)
   PUBMED   38225262
  REMARK    GeneRIF: Structural differences between the closely related RNA
            helicases, UAP56 and URH49, fashion distinct functional
            apo-complexes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Shen,H.
  TITLE     UAP56- a key player with surprisingly diverse roles in pre-mRNA
            splicing and nuclear export
  JOURNAL   BMB Rep 42 (4), 185-188 (2009)
   PUBMED   19403039
  REMARK    GeneRIF: This report summarizes recent evidence for the role of
            UAP56 in pre-mRNA splicing and nuclear export.
            Review article
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Zhao,R., Shen,J., Green,M.R., MacMorris,M. and Blumenthal,T.
  TITLE     Crystal structure of UAP56, a DExD/H-box protein involved in
            pre-mRNA splicing and mRNA export
  JOURNAL   Structure 12 (8), 1373-1381 (2004)
   PUBMED   15296731
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Allcock,R.J., Price,P., Gaudieri,S., Leelayuwat,C., Witt,C.S. and
            Dawkins,R.L.
  TITLE     Characterisation of the human central MHC gene, BAT1: genomic
            structure and expression
  JOURNAL   Exp Clin Immunogenet 16 (2), 98-106 (1999)
   PUBMED   10343160
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Fleckner,J., Zhang,M., Valcarcel,J. and Green,M.R.
  TITLE     U2AF65 recruits a novel human DEAD box protein required for the U2
            snRNP-branchpoint interaction
  JOURNAL   Genes Dev 11 (14), 1864-1872 (1997)
   PUBMED   9242493
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Peelman,L.J., Chardon,P., Nunes,M., Renard,C., Geffrotin,C.,
            Vaiman,M., Van Zeveren,A., Coppieters,W., van de Weghe,A.,
            Bouquet,Y. et al.
  TITLE     The BAT1 gene in the MHC encodes an evolutionarily conserved
            putative nuclear RNA helicase of the DEAD family
  JOURNAL   Genomics 26 (2), 210-218 (1995)
   PUBMED   7601445
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Spies,T., Blanck,G., Bresnahan,M., Sands,J. and Strominger,J.L.
  TITLE     A new cluster of genes within the human major histocompatibility
            complex
  JOURNAL   Science 243 (4888), 214-217 (1989)
   PUBMED   2911734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA272922.1, Z37166.1 and
            BM993499.1.
            
            Summary: This gene encodes a member of the DEAD box family of
            RNA-dependent ATPases that mediate ATP hydrolysis during pre-mRNA
            splicing. The encoded protein is an essential splicing factor
            required for association of U2 small nuclear ribonucleoprotein with
            pre-mRNA, and it also plays an important role in mRNA export from
            the nucleus to the cytoplasm. This gene belongs to a cluster of
            genes localized in the vicinity of the genes encoding tumor
            necrosis factor alpha and tumor necrosis factor beta. These genes
            are all within the human major histocompatibility complex class III
            region. Mutations in this gene may be associated with rheumatoid
            arthritis. Alternative splicing results in multiple transcript
            variants. Related pseudogenes have been identified on both
            chromosomes 6 and 11. Read-through transcription also occurs
            between this gene and the upstream ATP6V1G2 (ATPase, H+
            transporting, lysosomal 13kDa, V1 subunit G2) gene. [provided by
            RefSeq, Feb 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222912.1, SRR5189661.39354.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396172.6/ ENSP00000379475.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..428
                     /product="spliceosome RNA helicase DDX39B"
                     /EC_number="3.6.4.13"
                     /note="nuclear RNA helicase (DEAD family); ATP-dependent
                     RNA helicase p47; DEAD-box helicase 39B; 56 kDa
                     U2AF65-associated protein; spliceosome RNA helicase BAT1;
                     DEAD (Asp-Glu-Ala-Asp) box polypeptide 39B;
                     HLA-B-associated transcript 1 protein"
                     /calculated_mol_wt=48860
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13838.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q13838.1)"
     Site            36
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13838.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13838.1)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13838.1)"
     Region          44..251
                     /region_name="DEADc_DDX39"
                     /note="DEAD-box helicase domain of DEAD box protein 39;
                     cd17950"
                     /db_xref="CDD:350708"
     Region          45..73
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13838.1)"
     Site            order(47,65,67..69,72,91..97,196..197)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350708"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13838.1)"
     Region          196..199
                     /region_name="DECD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13838.1)"
     Region          262..391
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(350,352,377,380..381)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     CDS             1..428
                     /gene="DDX39B"
                     /gene_synonym="BAT1; D6S81E; UAP56"
                     /coded_by="NM_004640.7:187..1473"
                     /db_xref="CCDS:CCDS4697.1"
                     /db_xref="GeneID:7919"
                     /db_xref="HGNC:HGNC:13917"
                     /db_xref="MIM:142560"
ORIGIN      
        1 maendvdnel ldyeddevet aaggdgaeap akkdvkgsyv sihssgfrdf llkpellrai
       61 vdcgfehpse vqhecipqai lgmdvlcqak sgmgktavfv latlqqlepv tgqvsvlvmc
      121 htrelafqis keyerfskym pnvkvavffg glsikkdeev lkkncphivv gtpgrilala
      181 rnkslnlkhi khfildecdk mleqldmrrd vqeifrmtph ekqvmmfsat lskeirpvcr
      241 kfmqdpmeif vddetkltlh glqqyyvklk dneknrklfd lldvlefnqv vifvksvqrc
      301 ialaqllveq nfpaiaihrg mpqeerlsry qqfkdfqrri lvatnlfgrg mdiervniaf
      361 nydmpedsdt ylhrvaragr fgtkglaitf vsdendakil ndvqdrfevn iselpdeidi
      421 ssyieqtr
//
LOCUS       NP_064575                406 aa            linear   PRI 27-APR-2025
DEFINITION  olfactomedin-like protein 3 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_064575
VERSION     NP_064575.1
DBSOURCE    REFSEQ: accession NM_020190.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Toedebusch,R.G., Lucchesi,C.A., Debebe,E.T., Wittenburg,L.A.,
            Chen,X. and Toedebusch,C.M.
  TITLE     Microglia-Derived Olfactomedin-like 3 Promotes Pro-Tumorigenic
            Microglial Function and Malignant Features of Glioma Cells
  JOURNAL   Int J Mol Sci 22 (23), 13052 (2021)
   PUBMED   34884869
  REMARK    GeneRIF: Microglia-Derived Olfactomedin-like 3 Promotes
            Pro-Tumorigenic Microglial Function and Malignant Features of
            Glioma Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Mei,H., Zha,Z., Wang,W., Xie,Y., Huang,Y., Li,W., Wei,D., Zhang,X.,
            Qu,J. and Liu,J.
  TITLE     Surfaceome CRISPR screen identifies OLFML3 as a
            rhinovirus-inducible IFN antagonist
  JOURNAL   Genome Biol 22 (1), 297 (2021)
   PUBMED   34686207
  REMARK    GeneRIF: Surfaceome CRISPR screen identifies OLFML3 as a
            rhinovirus-inducible IFN antagonist.
            Erratum:[Genome Biol. 2021 Nov 15;22(1):314. doi:
            10.1186/s13059-021-02534-5. PMID: 34782001]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Chen,P., Hsu,W.H., Chang,A., Tan,Z., Lan,Z., Zhou,A., Spring,D.J.,
            Lang,F.F., Wang,Y.A. and DePinho,R.A.
  TITLE     Circadian Regulator CLOCK Recruits Immune-Suppressive Microglia
            into the GBM Tumor Microenvironment
  JOURNAL   Cancer Discov 10 (3), 371-381 (2020)
   PUBMED   31919052
  REMARK    GeneRIF: Circadian Regulator CLOCK Recruits Immune-Suppressive
            Microglia into the GBM Tumor Microenvironment.
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Dunn,L.L., de Valence,S., Tille,J.C., Hammel,P., Walpoth,B.H.,
            Stocker,R., Imhof,B.A. and Miljkovic-Licina,M.
  TITLE     Biodegradable and plasma-treated electrospun scaffolds coated with
            recombinant Olfactomedin-like 3 for accelerating wound healing and
            tissue regeneration
  JOURNAL   Wound Repair Regen 24 (6), 1030-1035 (2016)
   PUBMED   27684720
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Anholt,R.R.
  TITLE     Olfactomedin proteins: central players in development and disease
  JOURNAL   Front Cell Dev Biol 2, 6 (2014)
   PUBMED   25364714
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Rodriguez-Sanchez,I.P., Garza-Rodriguez,M.L., Mohamed-Noriega,K.,
            Voruganti,V.S., Tejero,M.E., Delgado-Enciso,I., Perez-Ibave,D.C.,
            Schlabritz-Loutsevitch,N.E., Mohamed-Noriega,J.,
            Martinez-Fierro,M.L., Resendez-Perez,D., Cole,S.A.,
            Cavazos-Adame,H., Comuzzie,A.G., Mohamed-Hamsho,J. and
            Barrera-Saldana,H.A.
  TITLE     Olfactomedin-like 3 (OLFML3) gene expression in baboon and human
            ocular tissues: cornea, lens, uvea, and retina
  JOURNAL   J Med Primatol 42 (3), 105-111 (2013)
   PUBMED   23398349
  REMARK    GeneRIF: This paper reports OLFML3 expression in human and baboon
            eye. The full coding DNA sequence has 1221 bp, from which an open
            reading frame of 406 amino acid was obtained.
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Miljkovic-Licina,M., Hammel,P., Garrido-Urbani,S., Lee,B.P.,
            Meguenani,M., Chaabane,C., Bochaton-Piallat,M.L. and Imhof,B.A.
  TITLE     Targeting olfactomedin-like 3 inhibits tumor growth by impairing
            angiogenesis and pericyte coverage
  JOURNAL   Mol Cancer Ther 11 (12), 2588-2599 (2012)
   PUBMED   23002094
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Fautsch,M.P., Vrabel,A.M. and Johnson,D.H.
  TITLE     The identification of myocilin-associated proteins in the human
            trabecular meshwork
  JOURNAL   Exp Eye Res 82 (6), 1046-1052 (2006)
   PUBMED   16289162
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Zeng,L.C., Han,Z.G. and Ma,W.J.
  TITLE     Elucidation of subfamily segregation and intramolecular coevolution
            of the olfactomedin-like proteins by comprehensive phylogenetic
            analysis and gene expression pattern assessment
  JOURNAL   FEBS Lett 579 (25), 5443-5453 (2005)
   PUBMED   16212957
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Zeng,L.C., Liu,F., Zhang,X., Zhu,Z.D., Wang,Z.Q., Han,Z.G. and
            Ma,W.J.
  TITLE     hOLF44, a secreted glycoprotein with distinct expression pattern,
            belongs to an uncharacterized olfactomedin-like subfamily newly
            identified by phylogenetic analysis
  JOURNAL   FEBS Lett 571 (1-3), 74-80 (2004)
   PUBMED   15280020
  REMARK    GeneRIF: may have matrix-related function involved in human
            placental and embryonic development, or play a similar role in
            other physiological processes
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY464015.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the olfactomedin-like gene
            family which also includes genes encoding noelin, tiarin, myocilin,
            amassin, optimedin, photomedin, and latrophilin. The encoded
            protein is a secreted extracellular matrix glycoprotein with a
            C-terminal olfactomedin domain that facilitates protein-protein
            interactions, cell adhesion, and intercellular interactions. It
            serves as both a scaffold protein that recruits bone morphogenetic
            protein 1 to its substrate chordin, and as a vascular tissue
            remodeler with pro-angiogenic properties. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Feb
            2017].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF201945.1, AY464015.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000320334.5/ ENSP00000322273.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..406
                     /product="olfactomedin-like protein 3 isoform 1 precursor"
                     /note="olfactomedin-like protein 3; olfactomedin, 44-kd"
                     /calculated_mol_wt=43801
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2228
     mat_peptide     22..406
                     /product="Olfactomedin-like protein 3. /id=PRO_0000020092"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRN5.1)"
                     /calculated_mol_wt=43801
     Region          <31..>100
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          139..399
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; pfam02191"
                     /db_xref="CDD:460482"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRN5.1)"
     Site            248
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRN5.1)"
     CDS             1..406
                     /gene="OLFML3"
                     /gene_synonym="HNOEL-iso; OLF44"
                     /coded_by="NM_020190.5:44..1264"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS870.1"
                     /db_xref="GeneID:56944"
                     /db_xref="HGNC:HGNC:24956"
                     /db_xref="MIM:610088"
ORIGIN      
        1 mgpstpllil fllswsgplq gqqhhlveym errlaaleer laqcqdqssr haaelrdfkn
       61 kmlpllevae kerealrtea dtisgrvdrl erevdyletq npalpcvefd ekvtggpgtk
      121 gkgrrnekyd mvtdcgytis qvrsmkilkr fggpaglwtk dplgqtekiy vldgtqndta
      181 fvfprlrdft lamaarkasr vrvpfpwvgt gqlvyggfly farrppgrpg gggementlq
      241 likfhlanrt vvdssvfpae glippyglta dtyidlaade eglwavyatr eddrhlclak
      301 ldpqtldteq qwdtpcpren aeaafvicgt lyvvyntrpa srariqcsfd asgtltpera
      361 alpyfprryg ahaslrynpr erqlyawddg yqivyklemr kkeeev
//
LOCUS       NP_001349112             528 aa            linear   ROD 27-APR-2025
DEFINITION  phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR14 isoform
            3 [Mus musculus].
ACCESSION   NP_001349112 XP_006506888
VERSION     NP_001349112.1
DBSOURCE    REFSEQ: accession NM_001362183.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Feng,Q., Li,X., Liu,R., Liu,G., He,Y. and Li,T.
  TITLE     Overexpression of MTMR14 induced learning and memory impairments in
            2-month-old C57 mice
  JOURNAL   Neurosci Lett 825, 137700 (2024)
   PUBMED   38401642
  REMARK    GeneRIF: Overexpression of MTMR14 induced learning and memory
            impairments in 2-month-old C57 mice.
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Kong,L.Y., Liang,C., Li,P.C., Zhang,Y.W., Feng,S.D., Zhang,D.H.,
            Yao,R., Yang,L.L., Hao,Z.Y., Zhang,H., Tian,X.X., Guo,C.R.,
            Du,B.B., Dong,J.Z. and Zhang,Y.Z.
  TITLE     Myotubularin-Related Protein14 Prevents Neointima Formation and
            Vascular Smooth Muscle Cell Proliferation by Inhibiting Polo-Like
            Kinase1
  JOURNAL   J Am Heart Assoc 11 (21), e026174 (2022)
   PUBMED   36314496
  REMARK    GeneRIF: Myotubularin-Related Protein14 Prevents Neointima
            Formation and Vascular Smooth Muscle Cell Proliferation by
            Inhibiting Polo-Like Kinase1.
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Pan,Q., Liu,Y., Wang,G., Wen,Z. and Wang,Y.
  TITLE     MTMR14 protects against cerebral stroke through suppressing
            PTEN-regulated autophagy
  JOURNAL   Biochem Biophys Res Commun 529 (4), 1045-1052 (2020)
   PUBMED   32819563
  REMARK    GeneRIF: MTMR14 protects against cerebral stroke through
            suppressing PTEN-regulated autophagy.
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Li,S., Zhang,M. and Zhang,B.
  TITLE     MTMR14 protects against hepatic ischemia-reperfusion injury through
            interacting with AKT signaling in vivo and in vitro
  JOURNAL   Biomed Pharmacother 129, 110455 (2020)
   PUBMED   32768948
  REMARK    GeneRIF: MTMR14 protects against hepatic ischemia-reperfusion
            injury through interacting with AKT signaling in vivo and in vitro.
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Romero-Suarez,S., Shen,J., Brotto,L., Hall,T., Mo,C.,
            Valdivia,H.H., Andresen,J., Wacker,M., Nosek,T.M., Qu,C.K. and
            Brotto,M.
  TITLE     Muscle-specific inositide phosphatase (MIP/MTMR14) is reduced with
            age and its loss accelerates skeletal muscle aging process by
            altering calcium homeostasis
  JOURNAL   Aging (Albany NY) 2 (8), 504-513 (2010)
   PUBMED   20817957
  REMARK    GeneRIF: a knockout mice were more susceptible to exercise-induced
            muscle damage, a trademark of muscle functional changes in older
            subjects
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Sansom,S.N., Griffiths,D.S., Faedo,A., Kleinjan,D.J., Ruan,Y.,
            Smith,J., van Heyningen,V., Rubenstein,J.L. and Livesey,F.J.
  TITLE     The level of the transcription factor Pax6 is essential for
            controlling the balance between neural stem cell self-renewal and
            neurogenesis
  JOURNAL   PLoS Genet 5 (6), e1000511 (2009)
   PUBMED   19521500
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Shen,J., Yu,W.M., Brotto,M., Scherman,J.A., Guo,C., Stoddard,C.,
            Nosek,T.M., Valdivia,H.H. and Qu,C.K.
  TITLE     Deficiency of MIP/MTMR14 phosphatase induces a muscle disorder by
            disrupting Ca(2+) homeostasis
  JOURNAL   Nat Cell Biol 11 (6), 769-776 (2009)
   PUBMED   19465920
  REMARK    GeneRIF: Data report that mice deficient in the newly identified
            phosphatidylinositol phosphate phosphatase MIP/MTMR14
            (muscle-specific inositol phosphatase) show muscle weakness and
            fatigue.
REFERENCE   9  (residues 1 to 528)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   10 (residues 1 to 528)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC153592.3 and AC155287.6.
            
            On Apr 6, 2018 this sequence version replaced XP_006506888.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3) is
            shorter at the N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.4734645.1,
                                           SRR1660811.253274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 52.74 cM"
     Protein         1..528
                     /product="phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR14 isoform 3"
                     /EC_number="3.1.3.95"
                     /note="mJumpy; phosphatidylinositol-3-phosphate
                     phosphatase; phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR14"
                     /calculated_mol_wt=59078
     Region          7..123
                     /region_name="PH-GRAM_MTMR14"
                     /note="Myotubularian (MTM) related 14 protein (MTMR14)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13213"
                     /db_xref="CDD:275400"
     Region          <173..266
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     CDS             1..528
                     /gene="Mtmr14"
                     /gene_synonym="1110061O04Rik"
                     /coded_by="NM_001362183.1:335..1921"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:97287"
                     /db_xref="MGI:MGI:1916075"
ORIGIN      
        1 marcrgrfvc pvilfkgkhi crsatlagwg elygrsgyny lfsggaddtw astedvteed
       61 fvlrsgdthl fdkvrgydik llqylsvkyi cdlmvenkkv kfgmnvtsse kvdkaqryan
      121 ftllsipypg ceffkeykdr dymaeglifn wkqdyvdapl nipnfltqsl nidwsqyqsw
      181 dlvqqtqnyl klllfimnrd ddsgllvhci sgwdrtplfi sllrlslwad glihtslkpa
      241 eilyltvayd wflfghmlvd rlskgeeiff fcfnflkhit seefclktqr rkslptrdag
      301 ftvedicmlr hkdrgsttsl gsdfslvleh spgavgsfsy etvelapaga ptqaawrksh
      361 ssspqsmlws rpqpseerlp shhglteaks ssssssnhsd nffrmgsspl evpkprsvdh
      421 plpgsslstd fgswqlvsgc gsiqdrpvlh tdsslpfsfq delpnscllt alsdretrlq
      481 evrsaflaay sstvglraat pspsgaiggl leqfargvgl rgtststl
//
LOCUS       NP_061897               2071 aa            linear   PRI 27-APR-2025
DEFINITION  HEAT repeat-containing protein 5B [Homo sapiens].
ACCESSION   NP_061897 XP_042685
VERSION     NP_061897.1
DBSOURCE    REFSEQ: accession NM_019024.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2071)
  AUTHORS   Marmorale,L.J., Jin,H., Reidy,T.G., Palomino-Alonso,B.,
            Zysnarski,C.J., Jordan-Javed,F., Lahiri,S. and Duncan,M.C.
  TITLE     Fast-evolving cofactors regulate the role of HEATR5 complexes in
            intra-Golgi trafficking
  JOURNAL   J Cell Biol 223 (3) (2024)
   PUBMED   38240799
  REMARK    GeneRIF: Fast-evolving cofactors regulate the role of HEATR5
            complexes in intra-Golgi trafficking.
REFERENCE   2  (residues 1 to 2071)
  AUTHORS   Ghosh,S.G., Breuss,M.W., Schlachetzki,Z., Chai,G., Ross,D.,
            Stanley,V., Sonmez,F.M., Topaloglu,H., Zaki,M.S., Hosny,H., Gad,S.
            and Gleeson,J.G.
  TITLE     Biallelic hypomorphic mutations in HEATR5B, encoding HEAT
            repeat-containing protein 5B, in a neurological syndrome with
            pontocerebellar hypoplasia
  JOURNAL   Eur J Hum Genet 29 (6), 957-964 (2021)
   PUBMED   33824466
  REMARK    GeneRIF: Biallelic hypomorphic mutations in HEATR5B, encoding HEAT
            repeat-containing protein 5B, in a neurological syndrome with
            pontocerebellar hypoplasia.
REFERENCE   3  (residues 1 to 2071)
  AUTHORS   Zysnarski,C.J., Lahiri,S., Javed,F.T., Martinez-Marquez,J.Y.,
            Trowbridge,J.W. and Duncan,M.C.
  TITLE     Adaptor protein complex-1 (AP-1) is recruited by the HEATR5 protein
            Laa1 and its co-factor Laa2 in yeast
  JOURNAL   J Biol Chem 294 (4), 1410-1419 (2019)
   PUBMED   30523155
REFERENCE   4  (residues 1 to 2071)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2071)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 2071)
  AUTHORS   Luke,M.M., O'Meara,E.S., Rowland,C.M., Shiffman,D., Bare,L.A.,
            Arellano,A.R., Longstreth,W.T. Jr., Lumley,T., Rice,K., Tracy,R.P.,
            Devlin,J.J. and Psaty,B.M.
  TITLE     Gene variants associated with ischemic stroke: the cardiovascular
            health study
  JOURNAL   Stroke 40 (2), 363-368 (2009)
   PUBMED   19023099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 2071)
  AUTHORS   Shiffman,D., O'Meara,E.S., Bare,L.A., Rowland,C.M., Louie,J.Z.,
            Arellano,A.R., Lumley,T., Rice,K., Iakoubova,O., Luke,M.M.,
            Young,B.A., Malloy,M.J., Kane,J.P., Ellis,S.G., Tracy,R.P.,
            Devlin,J.J. and Psaty,B.M.
  TITLE     Association of gene variants with incident myocardial infarction in
            the Cardiovascular Health Study
  JOURNAL   Arterioscler Thromb Vasc Biol 28 (1), 173-179 (2008)
   PUBMED   17975119
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 2071)
  AUTHORS   Hirst,J., Borner,G.H., Harbour,M. and Robinson,M.S.
  TITLE     The aftiphilin/p200/gamma-synergin complex
  JOURNAL   Mol Biol Cell 16 (5), 2554-2565 (2005)
   PUBMED   15758025
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007899.3, AV759566.1, AK096637.1, AB037835.1, BX538008.1,
            CA432330.1 and AC007404.4.
            
            On Nov 22, 2004 this sequence version replaced XP_042685.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.200923.1,
                                           SRR1660809.37106.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000233099.6/ ENSP00000233099.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2071
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.2"
     Protein         1..2071
                     /product="HEAT repeat-containing protein 5B"
                     /calculated_mol_wt=224172
     Region          97..121
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(113..114,117,120..121,154..155,158,161..162,165,
                     195..196,199,202..203,206,236..237,240,243..244)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          137..165
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          177..207
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          218..244
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(831..832,835,838..839,842,870..871,874,877..878,881,
                     909..910,917,920..921,953..954,957,960..961)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          848..885
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D3.2)"
     Region          852..882
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          891..921
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          932..962
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1062..1099
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D3.2)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9P2D3.2)"
     Region          1288..1493
                     /region_name="Laa1_Sip1_HTR5"
                     /note="Laa1/Sip1/HEATR5 HEAT repeat region; pfam20210"
                     /db_xref="CDD:466361"
     Region          1290..1327
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D3.2)"
     Site            1563
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2D3.2)"
     Site            1564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2D3.2)"
     Site            1737
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2D3.2)"
     CDS             1..2071
                     /gene="HEATR5B"
                     /gene_synonym="p200; p200a"
                     /coded_by="NM_019024.3:127..6342"
                     /db_xref="CCDS:CCDS33181.1"
                     /db_xref="GeneID:54497"
                     /db_xref="HGNC:HGNC:29273"
                     /db_xref="MIM:619627"
ORIGIN      
        1 melahsllln eealaqitea krpvfifewl rfldkvlvaa nktdvkekqk klveqltgli
       61 ssspgpptrk llaknlaaly sigdtftvfq tldkcndiir nkddtaaylp tklaavacvg
      121 afyekmgrml gsafpetvnn llkslksaes qgrseilmsl qkvlsglgga aasshrdiyk
      181 narslltdrs mavrcavakc llelqneavf mwtaelenia tlcfkalens nygvrvavsk
      241 llgtvmatal mpkqatvmrq nvkratfdev lelmatgflr ggsgflksgg emlkvggsvn
      301 revrvgvtqa yvvfvttlgg qwlersfatf lshvldlvsh pratqthvea vysrrcvsfi
      361 lratvgsllg ekaqiaaake icqaigkqmk aveavvndts genksgaadi aasqhvmvca
      421 lqelgslvqs lnataspliq easiglleiv tsvllhpsma arlaaawclr cvavalpfql
      481 tpfldrcaer lnnlktspea vsgysfamaa llggvhqcpl giphakgkmv vsiaedllrt
      541 aaqnsrlslq rtqagwlllg almtlgpsvv ryhlpkmlll wrnvfprslk eleaekargd
      601 sftwqvtleg ragalcamrs fvahcpellt edvirklmtp iecamtmmsh ipsvmkahga
      661 hlkasaamvr lrlydilall ppktyegsfn allrelvaef tltdnsantt tsllrslchy
      721 ddsvllgswl qetdhksied qlqpnsasgs galehdpssi ylripageav pgplplgvsv
      781 idasvalfgv vfphvsykhr lqmldhfaec vkqakgvrqq avqlniftav lsalkglaen
      841 kstlgpeevr ksaltlvmgp ldnpnpilrc aagealgrma qvvgeatfia rmaqysfdkl
      901 ksardvvsrt ghslalgclh ryvggigsgq hlktsvsill alaqdgtspe vqtwslhsla
      961 livdssgpmy rgyveptlsl vltllltvpp shtevhqclg rclgaiittv gpelqgngat
     1021 tstirssclv gcaitqdhsd slvqaaaisc lqqlhmfapr hvnlsslvps lcvhlcsshl
     1081 llrraavacl rqlaqreaae vceyamslak ntgdkesssa nvspfapgvs srtdihcrhq
     1141 gvnitetgle gllfgmldre tdrklcsdih dtlghmlssl aveklshwlm lckdvlaass
     1201 dmstatllss gkdeeaekkd emdddtmftt lgeedkskpf vaprwatrvf aadclcriin
     1261 lcenadqahf dlalarsakl rnptndllvl hlsdlirmaf maatdhsnql rmaglqaled
     1321 iikkfasvpe pefpghvile qyqanvgaal rpafsqdtps diiakacqvc stwigsgvvs
     1381 dlndlrrvhn llvssldkvq agkgsssqly resattmekl avlkawaevy vvamnikkea
     1441 eskpkraikn tddddddcgt idelppdsli tlvqpelptl srlwlaalkd yalltlpaef
     1501 ssqlppdgga fytpetidta rlhyrnswap ilhavalwln stgftcsest eaaaisglqk
     1561 rstsvnlnqa sgavgsaksl peinkdrmhl ilgvsiqflc sprpeepieh vtaclqalht
     1621 lldspyarvh iaedqligve llsvlhrlll twnpssvqll vtgvvqqivr aaqdylqekr
     1681 ntlneddmek eactvlgegg dsgglipgks lvfatmellm filvrhmphl stkvsdspsh
     1741 iatktrlsee sarlvaatvt ilsdlpslcs pagcmtilpt ilfliarilk dtaiksadnq
     1801 vpppvsaalq giksivtlsm akteagvqkq wtalirstla cileysqped svptpdevsm
     1861 ltaialflws asneiigvqs lqngcmnrfk nalnscdpwv qakcyqllls vfqhsnrals
     1921 tpyihslapi vveklkaver nrpasniell avqegikvle tlvalgeeqn rvqllallvp
     1981 tlisyllden sfasassask dlhefalqnl mhigplypha fktvmgaape lkvrletavr
     2041 asqaskakaa arqpapaihs aptiklktsf f
//
LOCUS       NP_113648                332 aa            linear   PRI 27-APR-2025
DEFINITION  potassium channel subfamily K member 17 isoform 1 [Homo sapiens].
ACCESSION   NP_113648 NP_149085
VERSION     NP_113648.2
DBSOURCE    REFSEQ: accession NM_031460.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Neelsen,L.C., Riel,E.B., Rinne,S., Schmid,F.R., Jurs,B.C.,
            Bedoya,M., Langer,J.P., Eymsh,B., Kiper,A.K., Cordeiro,S.,
            Decher,N., Baukrowitz,T. and Schewe,M.
  TITLE     Ion occupancy of the selectivity filter controls opening of a
            cytoplasmic gate in the K2P channel TALK-2
  JOURNAL   Nat Commun 15 (1), 7545 (2024)
   PUBMED   39215031
  REMARK    GeneRIF: Ion occupancy of the selectivity filter controls opening
            of a cytoplasmic gate in the K2P channel TALK-2.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Khoubza,L., Gilbert,N., Kim,E.J., Chatelain,F.C., Feliciangeli,S.,
            Abelanet,S., Kang,D., Lesage,F. and Bichet,D.
  TITLE     Alkaline-sensitive two-pore domain potassium channels form
            functional heteromers in pancreatic beta-cells
  JOURNAL   J Biol Chem 298 (10), 102447 (2022)
   PUBMED   36063992
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Chai,S., Wan,X., Ramirez-Navarro,A., Tesar,P.J., Kaufman,E.S.,
            Ficker,E., George,A.L. Jr. and Deschenes,I.
  TITLE     Physiological genomics identifies genetic modifiers of long QT
            syndrome type 2 severity
  JOURNAL   J Clin Invest 128 (3), 1043-1056 (2018)
   PUBMED   29431731
  REMARK    GeneRIF: 2 novel gene variants in REM2 and KCNK17 that provide a
            physiologically plausible explanation for variable expressivity in
            a large subset of patients in a multigenerational long QT syndrome
            type 2 family
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Suzuki,Y., Tsutsumi,K., Miyamoto,T., Yamamura,H. and Imaizumi,Y.
  TITLE     Heterodimerization of two pore domain K+ channel TASK1 and TALK2 in
            living heterologous expression systems
  JOURNAL   PLoS One 12 (10), e0186252 (2017)
   PUBMED   29016681
  REMARK    GeneRIF: The results suggested that heterodimerization of TASK1 and
            TALK2 provides cells with the ability to make multiple responses to
            a variety of physiological and pharmacological stimuli.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Schewe,M., Nematian-Ardestani,E., Sun,H., Musinszki,M.,
            Cordeiro,S., Bucci,G., de Groot,B.L., Tucker,S.J., Rapedius,M. and
            Baukrowitz,T.
  TITLE     A Non-canonical Voltage-Sensing Mechanism Controls Gating in K2P
            K(+) Channels
  JOURNAL   Cell 164 (5), 937-949 (2016)
   PUBMED   26919430
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Gierten,J., Ficker,E., Bloehs,R., Schlomer,K., Kathofer,S.,
            Scholz,E., Zitron,E., Kiesecker,C., Bauer,A., Becker,R.,
            Katus,H.A., Karle,C.A. and Thomas,D.
  TITLE     Regulation of two-pore-domain (K2P) potassium leak channels by the
            tyrosine kinase inhibitor genistein
  JOURNAL   Br J Pharmacol 154 (8), 1680-1690 (2008)
   PUBMED   18516069
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Goldstein,S.A., Bayliss,D.A., Kim,D., Lesage,F., Plant,L.D. and
            Rajan,S.
  TITLE     International Union of Pharmacology. LV. Nomenclature and molecular
            relationships of two-P potassium channels
  JOURNAL   Pharmacol Rev 57 (4), 527-540 (2005)
   PUBMED   16382106
  REMARK    Review article
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Girard,C., Duprat,F., Terrenoire,C., Tinel,N., Fosset,M., Romey,G.,
            Lazdunski,M. and Lesage,F.
  TITLE     Genomic and functional characteristics of novel human pancreatic 2P
            domain K(+) channels
  JOURNAL   Biochem Biophys Res Commun 282 (1), 249-256 (2001)
   PUBMED   11263999
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Decher,N., Maier,M., Dittrich,W., Gassenhuber,J., Bruggemann,A.,
            Busch,A.E. and Steinmeyer,K.
  TITLE     Characterization of TASK-4, a novel member of the pH-sensitive,
            two-pore domain potassium channel family
  JOURNAL   FEBS Lett 492 (1-2), 84-89 (2001)
   PUBMED   11248242
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP317866.1, AF358910.1 and
            BC025726.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Nov 20, 2001 this sequence version replaced
            NP_149085.1, NP_113648.1.
            
            Summary: The protein encoded by this gene belongs to the family of
            potassium channel proteins containing two pore-forming P domains.
            This channel is an open rectifier which primarily passes outward
            current under physiological K+ concentrations. This gene is
            activated at alkaline pH. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025726.1, AY358853.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373231.9/ ENSP00000362328.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..332
                     /product="potassium channel subfamily K member 17 isoform
                     1"
                     /note="2P domain potassium channel Talk-2; TWIK-related
                     alkaline pH-activated K(+) channel 2; TWIK-related
                     acid-sensitive K(+) channel 4; acid-sensitive potassium
                     channel protein TASK-4; potassium channel, two pore domain
                     subfamily K, member 17; TWIK-related acid-sensitive K+ 4"
                     /calculated_mol_wt=36764
     Site            21..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96T54.1)"
     Site            65
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96T54.1)"
     Region          81..157
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96T54.1)"
     Region          116..121
                     /region_name="Selectivity filter 1.
                     /evidence=ECO:0000250|UniProtKB:P57789"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96T54.1)"
     Site            128..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96T54.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96T54.1)"
     Region          <206..268
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          221..226
                     /region_name="Selectivity filter 2.
                     /evidence=ECO:0000250|UniProtKB:P57789"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96T54.1)"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96T54.1)"
     Region          287..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96T54.1)"
     CDS             1..332
                     /gene="KCNK17"
                     /gene_synonym="K2p17.1; TALK-2; TALK2; TASK-4; TASK4"
                     /coded_by="NM_031460.4:100..1098"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4842.1"
                     /db_xref="GeneID:89822"
                     /db_xref="HGNC:HGNC:14465"
                     /db_xref="MIM:607370"
ORIGIN      
        1 myrpraraap egrvrgcavp stvllllayl aylalgtgvf wtlegraaqd ssrsfqrdkw
       61 ellqnftcld rpaldslird vvqaykngas llsnttsmgr welvgsfffs vstittigyg
      121 nlspntmaar lfciffalvg iplnlvvlnr lghlmqqgvn hwasrlggtw qdpdkarwla
      181 gsgallsgll lflllppllf shmegwsyte gfyfafitls tvgfgdyvig mnpsqryplw
      241 yknmvslwil fgmawlalii klilsqletp grvcscchhs skedfksqsw rqgpdrepes
      301 hspqqgcype gpmgiiqhle psahaagcgk ds
//
LOCUS       NP_060464                314 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 248 [Homo sapiens].
ACCESSION   NP_060464
VERSION     NP_060464.1
DBSOURCE    REFSEQ: accession NM_017994.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Lu,Y., Vitart,V., Burdon,K.P., Khor,C.C., Bykhovskaya,Y.,
            Mirshahi,A., Hewitt,A.W., Koehn,D., Hysi,P.G., Ramdas,W.D.,
            Zeller,T., Vithana,E.N., Cornes,B.K., Tay,W.T., Tai,E.S.,
            Cheng,C.Y., Liu,J., Foo,J.N., Saw,S.M., Thorleifsson,G.,
            Stefansson,K., Dimasi,D.P., Mills,R.A., Mountain,J., Ang,W.,
            Hoehn,R., Verhoeven,V.J., Grus,F., Wolfs,R., Castagne,R.,
            Lackner,K.J., Springelkamp,H., Yang,J., Jonasson,F., Leung,D.Y.,
            Chen,L.J., Tham,C.C., Rudan,I., Vatavuk,Z., Hayward,C., Gibson,J.,
            Cree,A.J., MacLeod,A., Ennis,S., Polasek,O., Campbell,H.,
            Wilson,J.F., Viswanathan,A.C., Fleck,B., Li,X., Siscovick,D.,
            Taylor,K.D., Rotter,J.I., Yazar,S., Ulmer,M., Li,J., Yaspan,B.L.,
            Ozel,A.B., Richards,J.E., Moroi,S.E., Haines,J.L., Kang,J.H.,
            Pasquale,L.R., Allingham,R.R., Ashley-Koch,A., Mitchell,P.,
            Wang,J.J., Wright,A.F., Pennell,C., Spector,T.D., Young,T.L.,
            Klaver,C.C., Martin,N.G., Montgomery,G.W., Anderson,M.G., Aung,T.,
            Willoughby,C.E., Wiggs,J.L., Pang,C.P., Thorsteinsdottir,U.,
            Lotery,A.J., Hammond,C.J., van Duijn,C.M., Hauser,M.A.,
            Rabinowitz,Y.S., Pfeiffer,N., Mackey,D.A., Craig,J.E., Macgregor,S.
            and Wong,T.Y.
  CONSRTM   NEIGHBOR Consortium
  TITLE     Genome-wide association analyses identify multiple loci associated
            with central corneal thickness and keratoconus
  JOURNAL   Nat Genet 45 (2), 155-163 (2013)
   PUBMED   23291589
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK222774.1, BC012562.1 and AC079920.6.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.73632.1,
                                           SRR1660807.11846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341567.8/ ENSP00000340668.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..314
                     /product="transmembrane protein 248"
                     /note="UPF0458 protein C7orf42"
                     /calculated_mol_wt=34921
     Region          10..257
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     Site            21..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWD8.1)"
     Region          78..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWD8.1)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWD8.1)"
     Site            236..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWD8.1)"
     Site            270..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWD8.1)"
     CDS             1..314
                     /gene="TMEM248"
                     /gene_synonym="C7orf42"
                     /coded_by="NM_017994.5:256..1200"
                     /db_xref="CCDS:CCDS5536.1"
                     /db_xref="GeneID:55069"
                     /db_xref="HGNC:HGNC:25476"
ORIGIN      
        1 mfsinplenl kvyissrppl vvfmisvsam aiafltlgyf fkikeikspe maedwntfll
       61 rfndldlcvs enetlkhltn dtttpestmt sgqarastqs pqaledsgpv nisvsitltl
      121 dplkpfggys rnvthlysti lghqiglsgr eaheeinitf tlptawssdd calhghceqv
      181 vftacmtlta spgvfpvtvq pphcvpdtys natlwykift tardantkya qdynpfwcyk
      241 gaigkvyhal npkltvivpd ddrslinlhl mhtsyflfvm vitmfcyavi kgrpsklrqs
      301 npefcpekva laea
//
LOCUS       NP_003559                345 aa            linear   PRI 27-APR-2025
DEFINITION  annexin A9 [Homo sapiens].
ACCESSION   NP_003559
VERSION     NP_003559.2
DBSOURCE    REFSEQ: accession NM_003568.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Gao,H., Xia,M. and Ruan,H.
  TITLE     Knockdown of sulfotransferase 2B1 suppresses cell migration,
            invasion and promotes apoptosis in ovarian carcinoma cells via
            targeting annexin A9
  JOURNAL   J Obstet Gynaecol Res 50 (8), 1334-1344 (2024)
   PUBMED   38777329
  REMARK    GeneRIF: Knockdown of sulfotransferase 2B1 suppresses cell
            migration, invasion and promotes apoptosis in ovarian carcinoma
            cells via targeting annexin A9.
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Zhou,X., Zhao,J., Yan,T., Ye,D., Wang,Y., Zhou,B., Liu,D., Wang,X.,
            Zheng,W., Zheng,B., Qian,F., Li,Y., Li,D. and Fang,L.
  TITLE     ANXA9 facilitates S100A4 and promotes breast cancer progression
            through modulating STAT3 pathway
  JOURNAL   Cell Death Dis 15 (4), 260 (2024)
   PUBMED   38609357
  REMARK    GeneRIF: ANXA9 facilitates S100A4 and promotes breast cancer
            progression through modulating STAT3 pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Kou,X., Ding,H., Li,L. and Chao,H.
  TITLE     Hsa-miR-105-1 Regulates Cisplatin-Resistance in Ovarian Carcinoma
            Cells by Targeting ANXA9
  JOURNAL   Anal Cell Pathol (Amst) 2021, 6662486 (2021)
   PUBMED   33680718
  REMARK    GeneRIF: Hsa-miR-105-1 Regulates Cisplatin-Resistance in Ovarian
            Carcinoma Cells by Targeting ANXA9.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Zhou,Y., Qiu,C., Wang,T., Tao,L., Zhang,Z. and Yao,J.
  TITLE     High Expression of Annexin A9 Promotes Cell Proliferation and
            Migration in Gastric Cancer via the TGF-beta Signaling Pathway
  JOURNAL   J Environ Pathol Toxicol Oncol 40 (3), 87-94 (2021)
   PUBMED   34587407
  REMARK    GeneRIF: High Expression of Annexin A9 Promotes Cell Proliferation
            and Migration in Gastric Cancer via the TGF-beta Signaling Pathway.
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Goebeler,V., Ruhe,D., Gerke,V. and Rescher,U.
  TITLE     Atypical properties displayed by annexin A9, a novel member of the
            annexin family of Ca(2+) and lipid binding proteins
  JOURNAL   FEBS Lett 546 (2-3), 359-364 (2003)
   PUBMED   12832069
  REMARK    GeneRIF: examination of atypical properties
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Nguyen,V.T., Ndoye,A. and Grando,S.A.
  TITLE     Pemphigus vulgaris antibody identifies pemphaxin. A novel
            keratinocyte annexin-like molecule binding acetylcholine
  JOURNAL   J Biol Chem 275 (38), 29466-29476 (2000)
   PUBMED   10899159
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Morgan,R.O., Bell,D.W., Testa,J.R. and Fernandez,M.P.
  TITLE     Human annexin 31 genetic mapping and origin
  JOURNAL   Gene 227 (1), 33-38 (1999)
   PUBMED   9931420
REFERENCE   9  (residues 1 to 345)
  AUTHORS   Morgan,R.O. and Fernandez,M.P.
  TITLE     Expression profile and structural divergence of novel human annexin
            31
  JOURNAL   FEBS Lett 434 (3), 300-304 (1998)
   PUBMED   9742942
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Benz,J. and Hofmann,A.
  TITLE     Annexins: from structure to function
  JOURNAL   Biol Chem 378 (3-4), 177-183 (1997)
   PUBMED   9165068
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BJ993162.1, BC005830.2 and AJ009985.1.
            
            On Apr 26, 2007 this sequence version replaced NP_003559.1.
            
            Summary: The annexins are a family of calcium-dependent
            phospholipid-binding proteins. Members of the annexin family
            contain 4 internal repeat domains, each of which includes a type II
            calcium-binding site. The calcium-binding sites are required for
            annexins to aggregate and cooperatively bind anionic phospholipids
            and extracellular matrix proteins. This gene encodes a divergent
            member of the annexin protein family in which all four homologous
            type II calcium-binding sites in the conserved tetrad core contain
            amino acid substitutions that ablate their function. However,
            structural analysis suggests that the conserved putative ion
            channel formed by the tetrad core is intact. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ009985.1, BC005830.2 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368947.9/ ENSP00000357943.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..345
                     /product="annexin A9"
                     /note="annexin 31; annexin XXXI; annexin-9; pemphaxin"
                     /calculated_mol_wt=38233
     Region          41..112
                     /region_name="Annexin 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (O76027.3)"
     Region          46..110
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          113..184
                     /region_name="Annexin 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (O76027.3)"
     Region          117..182
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          197..266
                     /region_name="Annexin 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (O76027.3)"
     Region          201..264
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          270..341
                     /region_name="Annexin 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (O76027.3)"
     Region          274..339
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     CDS             1..345
                     /gene="ANXA9"
                     /gene_synonym="ANX31"
                     /coded_by="NM_003568.3:202..1239"
                     /db_xref="CCDS:CCDS975.2"
                     /db_xref="GeneID:8416"
                     /db_xref="HGNC:HGNC:547"
                     /db_xref="MIM:603319"
ORIGIN      
        1 msvtggkmap sltqeilshl glasktaawg tlgtlrtfln fsvdkdaqrl lraitgqgvd
       61 rsaivdvltn rsreqrqlis rnfqertqqd lmkslqaals gnlerivmal lqptaqfdaq
      121 elrtalkasd savdvaieil atrtppqlqe clavykhnfq veavdditse tsgilqdlll
      181 alakggrdsy sgiidynlae qdvqalqrae gpsreetwvp vftqrnpehl irvfdqyqrs
      241 tgqeleeavq nrfhgdaqva llglasvikn tplyfadklh qalqetepny qvlirilisr
      301 cetdllsira efrkkfgksl ysslqdavkg dcqsallalc raedm
//
LOCUS       NP_004705                629 aa            linear   PRI 27-APR-2025
DEFINITION  dual specificity tyrosine-phosphorylation-regulated kinase 1B
            isoform p69 [Homo sapiens].
ACCESSION   NP_004705
VERSION     NP_004705.1
DBSOURCE    REFSEQ: accession NM_004714.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Folon,L., Baron,M., Scherrer,V., Toussaint,B., Vaillant,E.,
            Loiselle,H., Dechaume,A., De Pooter,F., Boutry,R., Boissel,M.,
            Diallo,A., Ning,L., Balkau,B., Charpentier,G., Franc,S., Marre,M.,
            Derhourhi,M., Froguel,P. and Bonnefond,A.
  TITLE     Pathogenic, Total Loss-of-Function DYRK1B Variants Cause Monogenic
            Obesity Associated With Type 2 Diabetes
  JOURNAL   Diabetes Care 47 (3), 444-451 (2024)
   PUBMED   38170957
  REMARK    GeneRIF: Pathogenic, Total Loss-of-Function DYRK1B Variants Cause
            Monogenic Obesity Associated With Type 2 Diabetes.
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Beckers,C., Vasilikos,L., Sanchez Fernandez,A., Moor,L. and
            Pruschy,M.
  TITLE     Targeting the survival kinase DYRK1B: A novel approach to overcome
            radiotherapy-related treatment resistance
  JOURNAL   Radiother Oncol 190, 110039 (2024)
   PUBMED   38040123
  REMARK    GeneRIF: Targeting the survival kinase DYRK1B: A novel approach to
            overcome radiotherapy-related treatment resistance.
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 629)
  AUTHORS   Armanmehr,A., Jafari Khamirani,H., Zoghi,S. and Dianatpour,M.
  TITLE     Analysis of DYRK1B, PPARG, and CEBPB Expression Patterns in
            Adipose-Derived Stem Cells from Patients Carrying DYRK1B R102C and
            Healthy Individuals During Adipogenesis
  JOURNAL   Metab Syndr Relat Disord 20 (10), 576-583 (2022)
   PUBMED   36318489
  REMARK    GeneRIF: Analysis of DYRK1B, PPARG, and CEBPB Expression Patterns
            in Adipose-Derived Stem Cells from Patients Carrying DYRK1B R102C
            and Healthy Individuals During Adipogenesis.
REFERENCE   5  (residues 1 to 629)
  AUTHORS   Leder,S., Czajkowska,H., Maenz,B., De Graaf,K., Barthel,A.,
            Joost,H.G. and Becker,W.
  TITLE     Alternative splicing variants of dual specificity tyrosine
            phosphorylated and regulated kinase 1B exhibit distinct patterns of
            expression and functional properties
  JOURNAL   Biochem J 372 (Pt 3), 881-888 (2003)
   PUBMED   12633499
REFERENCE   6  (residues 1 to 629)
  AUTHORS   Lim,S., Zou,Y. and Friedman,E.
  TITLE     The transcriptional activator Mirk/Dyrk1B is sequestered by
            p38alpha/beta MAP kinase
  JOURNAL   J Biol Chem 277 (51), 49438-49445 (2002)
   PUBMED   12384504
  REMARK    GeneRIF: p38 MAP Kinase suppresses the function of Mirk as a
            transcriptional activator only when cells are proliferating
REFERENCE   7  (residues 1 to 629)
  AUTHORS   Lim,S., Jin,K. and Friedman,E.
  TITLE     Mirk protein kinase is activated by MKK3 and functions as a
            transcriptional activator of HNF1alpha
  JOURNAL   J Biol Chem 277 (28), 25040-25046 (2002)
   PUBMED   11980910
  REMARK    GeneRIF: activation by MKK2 and role as transcriptional activator
            of HNF1alpha
            Erratum:[J Biol Chem. 2004 Feb 6;279(6):5047]
REFERENCE   8  (residues 1 to 629)
  AUTHORS   Lee,K., Deng,X. and Friedman,E.
  TITLE     Mirk protein kinase is a mitogen-activated protein kinase substrate
            that mediates survival of colon cancer cells
  JOURNAL   Cancer Res 60 (13), 3631-3637 (2000)
   PUBMED   10910078
REFERENCE   9  (residues 1 to 629)
  AUTHORS   Leder,S., Weber,Y., Altafaj,X., Estivill,X., Joost,H.G. and
            Becker,W.
  TITLE     Cloning and characterization of DYRK1B, a novel member of the DYRK
            family of protein kinases
  JOURNAL   Biochem Biophys Res Commun 254 (2), 474-479 (1999)
   PUBMED   9918863
REFERENCE   10 (residues 1 to 629)
  AUTHORS   Becker,W., Weber,Y., Wetzel,K., Eirmbter,K., Tejedor,F.J. and
            Joost,H.G.
  TITLE     Sequence characteristics, subcellular localization, and substrate
            specificity of DYRK-related kinases, a novel family of dual
            specificity protein kinases
  JOURNAL   J Biol Chem 273 (40), 25893-25902 (1998)
   PUBMED   9748265
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y17999.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of a family of
            nuclear-localized protein kinases. The encoded protein participates
            in the regulation of the cell cycle. Expression of this gene may be
            altered in tumor cells, and mutations in this gene were found to
            cause abdominal obesity-metabolic syndrome 3. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jun
            2014].
            
            Transcript Variant: This variant (1, also known as 'a') represents
            the longest transcript and encodes the longest isoform (p69, also
            known as isoform a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018751.1, Y17999.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323039.10/ ENSP00000312789.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..629
                     /product="dual specificity
                     tyrosine-phosphorylation-regulated kinase 1B isoform p69"
                     /EC_number="2.7.12.1"
                     /note="minibrain-related kinase; mirk protein kinase; dual
                     specificity tyrosine-(Y)-phosphorylation regulated kinase
                     1B"
                     /calculated_mol_wt=69067
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13627; propagated from
                     UniProtKB/Swiss-Prot (Q9Y463.1)"
     Region          67..89
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y463.1)"
     Region          69..86
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y463.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13627; propagated from
                     UniProtKB/Swiss-Prot (Q9Y463.1)"
     Region          97..436
                     /region_name="PKc_DYRK1"
                     /note="Catalytic domain of the protein kinase,
                     Dual-specificity tYrosine-phosphorylated and -Regulated
                     Kinase 1; cd14226"
                     /db_xref="CDD:271128"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13627; propagated from
                     UniProtKB/Swiss-Prot (Q9Y463.1)"
     Site            order(117..121,125,138,140,154,174,190..193,196,198..199,
                     239,241,243..244,246,259,262,271,273..276,278,315)
                     /site_type="active"
                     /db_xref="CDD:271128"
     Site            order(117..121,125,138,140,174,190..193,196,239,241,
                     243..244,246,259)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271128"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13627; propagated from
                     UniProtKB/Swiss-Prot (Q9Y463.1)"
     Site            order(154,198,239,241,262,271,273..276,278,315)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271128"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q63470; propagated from
                     UniProtKB/Swiss-Prot (Q9Y463.1)"
     Site            258..278
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271128"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13627; propagated from
                     UniProtKB/Swiss-Prot (Q9Y463.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:10910078; propagated from
                     UniProtKB/Swiss-Prot (Q9Y463.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:10910078; propagated from
                     UniProtKB/Swiss-Prot (Q9Y463.1)"
     Region          380..399
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y463.1)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13627; propagated from
                     UniProtKB/Swiss-Prot (Q9Y463.1)"
     Region          436..629
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y463.1)"
     Region          480..520
                     /region_name="Interaction with RANBP9.
                     /evidence=ECO:0000269|PubMed:14500717"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y463.1)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13627; propagated from
                     UniProtKB/Swiss-Prot (Q9Y463.1)"
     CDS             1..629
                     /gene="DYRK1B"
                     /gene_synonym="AOMS3; MIRK"
                     /coded_by="NM_004714.3:242..2131"
                     /note="isoform p69 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12543.1"
                     /db_xref="GeneID:9149"
                     /db_xref="HGNC:HGNC:3092"
                     /db_xref="MIM:604556"
ORIGIN      
        1 mavppghgpf sgfpgpqeht qvlpdvrllp rrlplafrda tsaplrklsv dliktykhin
       61 evyyakkkrr aqqappqdss nkkekkvlnh gydddnhdyi vrsgerwler yeidsligkg
      121 sfgqvvkayd hqtqelvaik iiknkkafln qaqielrlle lmnqhdtemk yyivhlkrhf
      181 mfrnhlclvf ellsynlydl lrnthfrgvs lnltrklaqq lctallflat pelsiihcdl
      241 kpenillcnp krsaikivdf gsscqlgqri yqyiqsrfyr spevllgtpy dlaidmwslg
      301 cilvemhtge plfsgsnevd qmnrivevlg ippaamldqa pkarkyferl pgggwtlrrt
      361 kelrkdyqgp gtrrlqevlg vqtggpggrr agepghspad ylrfqdlvlr mleyepaari
      421 splgalqhgf frrtadeatn tgpagssast spapldtcps sstassisss ggssgsssdn
      481 rtyrysnryc ggpgppitdc emnspqvpps qplrpwaggd vphkthqapa sasslpgtga
      541 qlppqprylg rppsptsppp pelmdvslvg gpadcspphp apapqhpaas alrtrmtggr
      601 pplpppddpa tlgphlglrg vpqstaass
//
LOCUS       NP_006545                263 aa            linear   PRI 27-APR-2025
DEFINITION  metaxin-2 isoform 1 [Homo sapiens].
ACCESSION   NP_006545
VERSION     NP_006545.1
DBSOURCE    REFSEQ: accession NM_006554.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Li,T., Bao,Y., Xia,Y., Meng,H., Zhou,C., Huang,L., Wang,X.,
            Lai,E.Y., Jiang,P. and Mao,J.
  TITLE     Loss of MTX2 causes mitochondrial dysfunction, podocyte injury,
            nephrotic proteinuria and glomerulopathy in mice and patients
  JOURNAL   Int J Biol Sci 20 (3), 937-952 (2024)
   PUBMED   38250156
  REMARK    GeneRIF: Loss of MTX2 causes mitochondrial dysfunction, podocyte
            injury, nephrotic proteinuria and glomerulopathy in mice and
            patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Elouej,S., Harhouri,K., Le Mao,M., Baujat,G., Nampoothiri,S.,
            Kayserili,H., Menabawy,N.A., Selim,L., Paneque,A.L., Kubisch,C.,
            Lessel,D., Rubinsztajn,R., Charar,C., Bartoli,C., Airault,C.,
            Deleuze,J.F., Rotig,A., Bauer,P., Pereira,C., Loh,A.,
            Escande-Beillard,N., Muchir,A., Martino,L., Gruenbaum,Y., Lee,S.H.,
            Manivet,P., Lenaers,G., Reversade,B., Levy,N. and De
            Sandre-Giovannoli,A.
  TITLE     Loss of MTX2 causes mandibuloacral dysplasia and links
            mitochondrial dysfunction to altered nuclear morphology
  JOURNAL   Nat Commun 11 (1), 4589 (2020)
   PUBMED   32917887
  REMARK    GeneRIF: Loss of MTX2 causes mandibuloacral dysplasia and links
            mitochondrial dysfunction to altered nuclear morphology.
            Erratum:[Nat Commun. 2020 Oct 19;11(1):5349. doi:
            10.1038/s41467-020-19290-y. PMID: 33077719]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Anderson,A.J., Jackson,T.D., Stroud,D.A. and Stojanovski,D.
  TITLE     Mitochondria-hubs for regulating cellular biochemistry: emerging
            concepts and networks
  JOURNAL   Open Biol 9 (8), 190126 (2019)
   PUBMED   31387448
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Guarani,V., McNeill,E.M., Paulo,J.A., Huttlin,E.L., Frohlich,F.,
            Gygi,S.P., Van Vactor,D. and Harper,J.W.
  TITLE     QIL1 is a novel mitochondrial protein required for MICOS complex
            stability and cristae morphology
  JOURNAL   Elife 4, e06265 (2015)
   PUBMED   25997101
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Xie,J., Marusich,M.F., Souda,P., Whitelegge,J. and Capaldi,R.A.
  TITLE     The mitochondrial inner membrane protein mitofilin exists as a
            complex with SAM50, metaxins 1 and 2, coiled-coil-helix
            coiled-coil-helix domain-containing protein 3 and 6 and DnaJC11
  JOURNAL   FEBS Lett 581 (18), 3545-3549 (2007)
   PUBMED   17624330
  REMARK    GeneRIF: mitofilin helps regulate mitochondrial morphology and at
            least four of the associated proteins (metaxins 1 and 2, SAM50 and
            CHCHD3) have been implicated in protein import
REFERENCE   9  (residues 1 to 263)
  AUTHORS   Kozjak-Pavlovic,V., Ross,K., Benlasfer,N., Kimmig,S., Karlas,A. and
            Rudel,T.
  TITLE     Conserved roles of Sam50 and metaxins in VDAC biogenesis
  JOURNAL   EMBO Rep 8 (6), 576-582 (2007)
   PUBMED   17510655
  REMARK    GeneRIF: The pathway of Voltage-dependent anion-selective channel
            biogenesis in human mitochondria involves the TOM complex, Sam50
            and metaxins, and that it is evolutionarily conserved.
REFERENCE   10 (residues 1 to 263)
  AUTHORS   Armstrong,L.C., Saenz,A.J. and Bornstein,P.
  TITLE     Metaxin 1 interacts with metaxin 2, a novel related protein
            associated with the mammalian mitochondrial outer membrane
  JOURNAL   J Cell Biochem 74 (1), 11-22 (1999)
   PUBMED   10381257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC067831.1 and AI991560.1.
            
            Summary: The protein encoded by this gene is highly similar to the
            metaxin 2 protein from mouse, which has been shown to interact with
            the mitochondrial membrane protein metaxin 1. Because of this
            similarity, it is thought that the encoded protein is peripherally
            associated with the cytosolic face of the outer mitochondrial
            membrane, and that it is involved in the import of proteins into
            the mitochondrion. Alternative splicing results in multiple
            transcript variants. A related pseudogene has been identified on
            chromosome 7. [provided by RefSeq, Jun 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.364517.1,
                                           SRR5189652.151700.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000249442.11/
                                                  ENSP00000249442.6
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..263
                     /product="metaxin-2 isoform 1"
                     /note="mitochondrial outer membrane import complex protein
                     2"
                     /calculated_mol_wt=29632
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (O75431.1)"
     Region          22..95
                     /region_name="GST_N_Metaxin2"
                     /note="GST_N family, Metaxin subfamily, Metaxin 2; a
                     metaxin 1 binding protein identified through a yeast
                     two-hybrid system using metaxin 1 as the bait. Metaxin 2
                     shares sequence similarity with metaxin 1 but does not
                     contain a C-terminal mitochondrial outer...; cd03079"
                     /db_xref="CDD:239377"
     Site            order(40,42..43,45..46,49..50,86,89..90)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239377"
     Site            order(40,71..73,84..85)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239377"
     Site            order(71,83..84,86..87,90)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239377"
     Region          125..250
                     /region_name="GST_C_Metaxin2"
                     /note="C-terminal, alpha helical domain of Metaxin 2;
                     cd03211"
                     /db_xref="CDD:198320"
     Site            order(130,137,210,213..214,217,221)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198320"
     CDS             1..263
                     /gene="MTX2"
                     /gene_synonym="MDPS; metaxin-2"
                     /coded_by="NM_006554.5:189..980"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2272.1"
                     /db_xref="GeneID:10651"
                     /db_xref="HGNC:HGNC:7506"
                     /db_xref="MIM:608555"
ORIGIN      
        1 mslvaeafvs qiaaaepwpe natlyqqlkg eqillsdnaa slavqaflqm cnlpikvvcr
       61 anaeymspsg kvpfihvgnq vvselgpivq fvkakghsls dgleevqkae mkaymelvnn
      121 mlltaelylq wcdeatvgei tharygspyp wplnhilayq kqwevkrkmk aigwgkktld
      181 qvledvdqcc qalsqrlgtq pyffnkqpte ldalvfghly tilttqltnd elsekvknys
      241 nllafcrrie qhyfedrgkg rls
//
LOCUS       NP_055988               1168 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 1 isoform 1 [Homo sapiens].
ACCESSION   NP_055988 XP_376314
VERSION     NP_055988.2
DBSOURCE    REFSEQ: accession NM_015173.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1168)
  AUTHORS   Wang,Q., Rong,P., Zhang,W., Yang,X., Chen,L., Cao,Y., Liu,M.,
            Feng,W., Ouyang,Q., Chen,Q., Li,H., Liang,H., Meng,F., Wang,H.Y.
            and Chen,S.
  TITLE     TBC1D1 is an energy-responsive polarization regulator of
            macrophages via governing ROS production in obesity
  JOURNAL   Sci China Life Sci 67 (9), 1899-1914 (2024)
   PUBMED   38902450
  REMARK    GeneRIF: TBC1D1 is an energy-responsive polarization regulator of
            macrophages via governing ROS production in obesity.
REFERENCE   2  (residues 1 to 1168)
  AUTHORS   Song,D., Yang,Q., Li,L., Wei,Y., Zhang,C., Du,H., Ren,G. and Li,H.
  TITLE     Novel prognostic biomarker TBC1D1 is associated with immunotherapy
            resistance in gliomas
  JOURNAL   Front Immunol 15, 1372113 (2024)
   PUBMED   38529286
  REMARK    GeneRIF: Novel prognostic biomarker TBC1D1 is associated with
            immunotherapy resistance in gliomas.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1168)
  AUTHORS   Cai,J., Jiang,Y., Chen,P., Liang,J., Zhang,Y., Yuan,R., Fan,H.,
            Zhong,Y., Cai,J., Cheng,S. and Zhang,Y.
  TITLE     TBC1D1 represses glioma progression by altering the integrity of
            the cytoskeleton
  JOURNAL   Aging (Albany NY) 16 (1), 431-444 (2024)
   PUBMED   38189823
  REMARK    GeneRIF: TBC1D1 represses glioma progression by altering the
            integrity of the cytoskeleton.
REFERENCE   4  (residues 1 to 1168)
  AUTHORS   Miklosz,A., Lukaszuk,B., Supruniuk,E., Grubczak,K., Moniuszko,M.,
            Choromanska,B., Mysliwiec,P. and Chabowski,A.
  TITLE     Does TBC1D4 (AS160) or TBC1D1 Deficiency Affect the Expression of
            Fatty Acid Handling Proteins in the Adipocytes Differentiated from
            Human Adipose-Derived Mesenchymal Stem Cells (ADMSCs) Obtained from
            Subcutaneous and Visceral Fat Depots?
  JOURNAL   Cells 10 (6), 1515 (2021)
   PUBMED   34208471
  REMARK    GeneRIF: Does TBC1D4 (AS160) or TBC1D1 Deficiency Affect the
            Expression of Fatty Acid Handling Proteins in the Adipocytes
            Differentiated from Human Adipose-Derived Mesenchymal Stem Cells
            (ADMSCs) Obtained from Subcutaneous and Visceral Fat Depots?
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1168)
  AUTHORS   Hook,S.C., Chadt,A., Heesom,K.J., Kishida,S., Al-Hasani,H.,
            Tavare,J.M. and Thomas,E.C.
  TITLE     TBC1D1 interacting proteins, VPS13A and VPS13C, regulate GLUT4
            homeostasis in C2C12 myotubes
  JOURNAL   Sci Rep 10 (1), 17953 (2020)
   PUBMED   33087848
  REMARK    GeneRIF: TBC1D1 interacting proteins, VPS13A and VPS13C, regulate
            GLUT4 homeostasis in C2C12 myotubes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1168)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   7  (residues 1 to 1168)
  AUTHORS   Roach,W.G., Chavez,J.A., Miinea,C.P. and Lienhard,G.E.
  TITLE     Substrate specificity and effect on GLUT4 translocation of the Rab
            GTPase-activating protein Tbc1d1
  JOURNAL   Biochem J 403 (2), 353-358 (2007)
   PUBMED   17274760
  REMARK    GeneRIF: form of Tbc1d1 also inhibited GLUT4 translocation and that
            this effect also required a functional GAP domain
REFERENCE   8  (residues 1 to 1168)
  AUTHORS   Stone,S., Abkevich,V., Russell,D.L., Riley,R., Timms,K., Tran,T.,
            Trem,D., Frank,D., Jammulapati,S., Neff,C.D., Iliev,D., Gress,R.,
            He,G., Frech,G.C., Adams,T.D., Skolnick,M.H., Lanchbury,J.S.,
            Gutin,A., Hunt,S.C. and Shattuck,D.
  TITLE     TBC1D1 is a candidate for a severe obesity gene and evidence for a
            gene/gene interaction in obesity predisposition
  JOURNAL   Hum Mol Genet 15 (18), 2709-2720 (2006)
   PUBMED   16893906
  REMARK    GeneRIF: coding variant R125W affects obesity susceptibility,
            delimits the location of an obesity gene at 4q34-35 and identifies
            a gene/gene interaction that influences the risk for obesity
            predisposition
REFERENCE   9  (residues 1 to 1168)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   10 (residues 1 to 1168)
  AUTHORS   White,R.A., Pasztor,L.M., Richardson,P.M. and Zon,L.I.
  TITLE     The gene encoding TBC1D1 with homology to the tre-2/USP6 oncogene,
            BUB2, and cdc16 maps to mouse chromosome 5 and human chromosome 4
  JOURNAL   Cytogenet Cell Genet 89 (3-4), 272-275 (2000)
   PUBMED   10965142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB036208.1, BC050321.1, AB449881.1, BC014529.2 and AK074954.1.
            
            On or before Feb 20, 2005 this sequence version replaced
            XP_376314.1, NP_055988.1.
            
            Summary: TBC1D1 is the founding member of a family of proteins
            sharing a 180- to 200-amino acid TBC domain presumed to have a role
            in regulating cell growth and differentiation. These proteins share
            significant homology with TRE2 (USP6; MIM 604334), yeast Bub2, and
            CDC16 (MIM 603461) (White et al., 2000 [PubMed 10965142]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050321.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1168
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..1168
                     /product="TBC1 domain family member 1 isoform 1"
                     /note="TBC1 (tre-2/USP6, BUB2, cdc16) domain family,
                     member 1"
                     /calculated_mol_wt=132953
     Region          21..150
                     /region_name="PTB"
                     /note="Phosphotyrosine-binding (PTB) PH-like fold;
                     cd00934"
                     /db_xref="CDD:269911"
     Site            order(24,112,133)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269911"
     Site            order(93..96,105..106,119,144,148)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269911"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          164..371
                     /region_name="PTB_TBC1D1_like"
                     /note="TBC1 domain family member 1 and related proteins
                     Phosphotyrosine-binding (PTB) domain; cd01269"
                     /db_xref="CDD:269967"
     Site            order(176,330,353)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269967"
     Region          203..238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:24879834; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            order(319..324,337,364,368)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269967"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          532..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          564..587
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24879834; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          628..658
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          678..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          690..745
                     /region_name="DUF3350"
                     /note="Domain of unknown function (DUF3350); pfam11830"
                     /db_xref="CDD:463365"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          797..1014
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            941
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            952
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          1094..1156
                     /region_name="ZapB"
                     /note="Cell division protein ZapB, interacts with FtsZ
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG3074"
                     /db_xref="CDD:442308"
     Site            1131
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          1145..1168
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TI0.2)"
     CDS             1..1168
                     /gene="TBC1D1"
                     /gene_synonym="TBC; TBC1"
                     /coded_by="NM_015173.4:359..3865"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33972.1"
                     /db_xref="GeneID:23216"
                     /db_xref="HGNC:HGNC:11578"
                     /db_xref="MIM:609850"
ORIGIN      
        1 mepitftark hllsnevsvd fglqlvgslp vhslttmpml pwvvaevrrl srqstrkepv
       61 tkqvrlcvsp sglrcepepg rsqqwdpliy ssifeckpqr vhklihnshd psyfaclike
      121 davhrqsicy vfkaddqtkv peiissirqa gkiarqeelh cpsefddtfs kkfevlfcgr
      181 vtvahkkapp alideciekf nhvsgsrgse sprpnpphaa ptgsqepvrr pmrksfsqpg
      241 lrslafrkel qdgglrssgf fssfeesdie nhlisghniv qptdieenrt mlftigqsev
      301 ylispdtkki aleknfkeis fcsqgirhvd hfgficress ggggfhfvcy vfqctnealv
      361 deimmtlkqa ftvaavqqta kapaqlcegc plqslhklce riegmnsskt klelqkhltt
      421 ltnqeqatif eevqklrprn eqreneliis flrclyeekq kehihigemk qtsqmaaeni
      481 gselppsatr frldmlknka krsltesles ilsrgnkarg lqehsisvdl dsslsstlsn
      541 tskepsvcek ealpisessf kllgssedls sdseshlpee paplspqqaf rrrantlshf
      601 piecqeppqp argspgvsqr klmryhsvst etpherkdfe skanhlgdsg gtpvktrrhs
      661 wrqqiflrva tpqkacdsss ryedyselge lpprsplepv cedgpfgppp eekkrtsrel
      721 relwqkailq qilllrmeke nqklqasend llnkrlkldy eeitpclkev ttvwekmlst
      781 pgrskikfdm ekmhsavgqg vprhhrgeiw kflaeqfhlk hqfpskqqpk dvpykellkq
      841 ltsqqhaili dlgrtfpthp yfsaqlgagq lslynilkay slldqevgyc qglsfvagil
      901 llhmseeeaf kmlkflmfdm glrkqyrpdm iilqiqmyql srllhdyhrd lynhleehei
      961 gpslyaapwf ltmfasqfpl gfvarvfdmi flqgtevifk valsllgshk plilqhenle
     1021 tivdfikstl pnlglvqmek tinqvfemdi akqlqayeve yhvlqeelid ssplsdnqrm
     1081 dklektnssl rkqnldlleq lqvangriqs leatieklls sesklkqaml tlelersall
     1141 qtveelrrrs aepsdrepec tqpeptgd
//
LOCUS       NP_112571                977 aa            linear   PRI 27-APR-2025
DEFINITION  Fc receptor-like protein 5 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_112571 XP_001133405 XP_001134256
VERSION     NP_112571.2
DBSOURCE    REFSEQ: accession NM_031281.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Reyes,R.A., Clarke,K., Gonzales,S.J., Cantwell,A.M., Garza,R.,
            Catano,G., Tragus,R.E., Patterson,T.F., Bol,S. and Bunnik,E.M.
  TITLE     SARS-CoV-2 spike-specific memory B cells express higher levels of
            T-bet and FcRL5 after non-severe COVID-19 as compared to severe
            disease
  JOURNAL   PLoS One 16 (12), e0261656 (2021)
   PUBMED   34936684
  REMARK    GeneRIF: SARS-CoV-2 spike-specific memory B cells express higher
            levels of T-bet and FcRL5 after non-severe COVID-19 as compared to
            severe disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Li,H., Dement-Brown,J., Liao,P.J., Mazo,I., Mills,F., Kraus,Z.,
            Fitzsimmons,S. and Tolnay,M.
  TITLE     Fc receptor-like 4 and 5 define human atypical memory B cells
  JOURNAL   Int Immunol 32 (12), 755-770 (2020)
   PUBMED   32805738
  REMARK    GeneRIF: Fc receptor-like 4 and 5 define human atypical memory B
            cells.
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Liu,H.W., Wei,D.X., He,D.W., Deng,J.Z., Zhu,J.J., Xu,K., Hu,D.,
            Li,J., Hu,W.H., Wang,Y., Xiao,S.H. and Fu,L.G.
  TITLE     The rs6427384 and rs6692977 Single Nucleotide Polymorphisms of the
            Fc Receptor-Like 5 (FCRL5) Gene and the Risk of Ankylosing
            Spondylitis: A Case Control Study in a Single Center in China
  JOURNAL   Med Sci Monit 26, e920956 (2020)
   PUBMED   32892204
  REMARK    GeneRIF: The rs6427384 and rs6692977 Single Nucleotide
            Polymorphisms of the Fc Receptor-Like 5 (FCRL5) Gene and the Risk
            of Ankylosing Spondylitis: A Case Control Study in a Single Center
            in China.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 977)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 977)
  AUTHORS   Gu,Z., Shen,Y., Tang,X.Y., Ke,X., Yao,H.B., Hong,S.L. and Kang,H.Y.
  TITLE     Genetic risk of FCRL3 and FCRL5 polymorphisms in children with
            asthma and allergic rhinitis in a Chinese Han population
  JOURNAL   Int J Pediatr Otorhinolaryngol 120, 58-63 (2019)
   PUBMED   30771554
  REMARK    GeneRIF: This study identified novel Single nucleotide polymorphism
            in FCRL3 and FCRL5 significantly associated with the risk for
            asthma with comorbid allergic rhinitis in the Chinese population
REFERENCE   6  (residues 1 to 977)
  AUTHORS   Miller,I., Hatzivassiliou,G., Cattoretti,G., Mendelsohn,C. and
            Dalla-Favera,R.
  TITLE     IRTAs: a new family of immunoglobulinlike receptors differentially
            expressed in B cells
  JOURNAL   Blood 99 (8), 2662-2669 (2002)
   PUBMED   11929751
  REMARK    GeneRIF: Characterization and comparison of the structure and
            B-cell expression pattern of the entire family of IRTA genes, which
            includes 5 members contiguously located on chromosome.
REFERENCE   7  (residues 1 to 977)
  AUTHORS   Davis,R.S., Wang,Y.H., Kubagawa,H. and Cooper,M.D.
  TITLE     Identification of a family of Fc receptor homologs with
            preferential B cell expression
  JOURNAL   Proc Natl Acad Sci U S A 98 (17), 9772-9777 (2001)
   PUBMED   11493702
REFERENCE   8  (residues 1 to 977)
  AUTHORS   Nakayama,Y., Weissman,S.M. and Bothwell,A.L.
  TITLE     BXMAS1 identifies a cluster of homologous genes differentially
            expressed in B cells
  JOURNAL   Biochem Biophys Res Commun 285 (3), 830-837 (2001)
   PUBMED   11453668
REFERENCE   9  (residues 1 to 977)
  AUTHORS   Hatzivassiliou,G., Miller,I., Takizawa,J., Palanisamy,N., Rao,P.H.,
            Iida,S., Tagawa,S., Taniwaki,M., Russo,J., Neri,A., Cattoretti,G.,
            Clynes,R., Mendelsohn,C., Chaganti,R.S. and Dalla-Favera,R.
  TITLE     IRTA1 and IRTA2, novel immunoglobulin superfamily receptors
            expressed in B cells and involved in chromosome 1q21 abnormalities
            in B cell malignancy
  JOURNAL   Immunity 14 (3), 277-289 (2001)
   PUBMED   11290337
REFERENCE   10 (residues 1 to 977)
  AUTHORS   Nakayama,Y., Iwamoto,Y., Maher,S.E., Tanaka,Y. and Bothwell,A.L.
  TITLE     Altered gene expression upon BCR cross-linking in Burkitt's
            lymphoma B cell line
  JOURNAL   Biochem Biophys Res Commun 277 (1), 124-127 (2000)
   PUBMED   11027651
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF369794.2, BC101067.1,
            AL353899.22 and BE676280.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 27, 2007 this sequence version replaced NP_112571.1.
            
            Summary: This gene encodes a member of the immunoglobulin receptor
            superfamily and the Fc-receptor like family. This gene and several
            other Fc receptor-like gene members are clustered on the long arm
            of chromosome 1. The encoded protein is a single-pass type I
            membrane protein and contains 8 immunoglobulin-like C2-type
            domains. This gene is implicated in B cell development and
            lymphomagenesis. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Sep
            2010].
            
            Transcript Variant: This variant (1) encodes the dominant isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF369794.2, AF343664.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361835.8/ ENSP00000354691.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.1"
     Protein         1..977
                     /product="Fc receptor-like protein 5 isoform 1 precursor"
                     /note="immunoglobulin superfamily receptor translocation
                     associated 2 (IRTA2); fcR-like protein 5; fc receptor
                     homolog 5; immune receptor translocation-associated
                     protein 2"
                     /calculated_mol_wt=104832
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1624
     mat_peptide     16..977
                     /product="Fc receptor-like protein 5 isoform 1"
                     /calculated_mol_wt=104832
     Region          23..100
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          40..44
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          54..58
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          71..74
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          82..87
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          93..96
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          105..185
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          119..123
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          133..136
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          149..153
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          163..168
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          178..181
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          287..373
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Region          380..466
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Site            383
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RD9.3)"
     Region          473..545
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          565..638
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          658..731
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          754..835
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Site            852..872
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RD9.3)"
     Region          879..898
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RD9.3)"
     Region          897..902
                     /region_name="ITIM motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RD9.3)"
     Region          910..915
                     /region_name="ITIM motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RD9.3)"
     Region          922..927
                     /region_name="ITIM motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RD9.3)"
     Region          952..957
                     /region_name="ITIM motif 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RD9.3)"
     CDS             1..977
                     /gene="FCRL5"
                     /gene_synonym="BXMAS1; CD307; CD307e; FCRH5; IRTA2;
                     PRO820"
                     /coded_by="NM_031281.3:154..3087"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1165.1"
                     /db_xref="GeneID:83416"
                     /db_xref="HGNC:HGNC:18508"
                     /db_xref="MIM:605877"
ORIGIN      
        1 mllwvillvl apvsgqfart prpiiflqpp wttvfqgerv tltckgfrfy spqktkwyhr
       61 ylgkeilret pdnilevqes geyrcqaqgs plsspvhldf ssaslilqap lsvfegdsvv
      121 lrcrakaevt lnntiykndn vlaflnkrtd fhiphaclkd ngayrctgyk esccpvssnt
      181 vkiqvqepft rpvlrassfq pisgnpvtlt cetqlslers dvplrfrffr ddqtlglgws
      241 lspnfqitam wskdsgfywc kaatmpysvi sdsprswiqv qipashpvlt lspekalnfe
      301 gtkvtlhcet qedslrtlyr fyhegvplrh ksvrcergas isfslttens gnyyctadng
      361 lgakpskavs lsvtvpvshp vlnlsspedl ifegakvtlh ceaqrgslpi lyqfhhegaa
      421 lerrsansag gvaisfslta ehsgnyycta dngfgpqrsk avslsvtvpv shpvltlssa
      481 ealtfegatv tlhcevqrgs pqilyqfyhe dmplwssstp svgrvsfsfs lteghsgnyy
      541 ctadngfgpq rsevvslfvt vpvsrpiltl rvpraqavvg dllelhceap rgsppilywf
      601 yhedvtlgss sapsggeasf nlsltaehsg nysceanngl vaqhsdtisl svivpvsrpi
      661 ltfrapraqa vvgdllelhc ealrgsspil ywfyhedvtl gkisapsggg asfnlsltte
      721 hsgiyscead ngleaqrsem vtlkvavpvs rpvltlrapg thaavgdlle lhcealrgsp
      781 lilyrffhed vtlgnrssps ggaslnlslt aehsgnysce adnglgaqrs etvtlyitgl
      841 tanrsgpfat gvaggllsia glaagallly cwlsrkagrk pasdparsps dsdsqeptyh
      901 nvpaweelqp vytnanprge nvvysevrii qekkkhavas dprhlrnkgs piiysevkva
      961 stpvsgslfl assaphr
//
LOCUS       NP_001349114             412 aa            linear   ROD 27-APR-2025
DEFINITION  phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR14 isoform
            4 [Mus musculus].
ACCESSION   NP_001349114
VERSION     NP_001349114.1
DBSOURCE    REFSEQ: accession NM_001362185.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Feng,Q., Li,X., Liu,R., Liu,G., He,Y. and Li,T.
  TITLE     Overexpression of MTMR14 induced learning and memory impairments in
            2-month-old C57 mice
  JOURNAL   Neurosci Lett 825, 137700 (2024)
   PUBMED   38401642
  REMARK    GeneRIF: Overexpression of MTMR14 induced learning and memory
            impairments in 2-month-old C57 mice.
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Kong,L.Y., Liang,C., Li,P.C., Zhang,Y.W., Feng,S.D., Zhang,D.H.,
            Yao,R., Yang,L.L., Hao,Z.Y., Zhang,H., Tian,X.X., Guo,C.R.,
            Du,B.B., Dong,J.Z. and Zhang,Y.Z.
  TITLE     Myotubularin-Related Protein14 Prevents Neointima Formation and
            Vascular Smooth Muscle Cell Proliferation by Inhibiting Polo-Like
            Kinase1
  JOURNAL   J Am Heart Assoc 11 (21), e026174 (2022)
   PUBMED   36314496
  REMARK    GeneRIF: Myotubularin-Related Protein14 Prevents Neointima
            Formation and Vascular Smooth Muscle Cell Proliferation by
            Inhibiting Polo-Like Kinase1.
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Pan,Q., Liu,Y., Wang,G., Wen,Z. and Wang,Y.
  TITLE     MTMR14 protects against cerebral stroke through suppressing
            PTEN-regulated autophagy
  JOURNAL   Biochem Biophys Res Commun 529 (4), 1045-1052 (2020)
   PUBMED   32819563
  REMARK    GeneRIF: MTMR14 protects against cerebral stroke through
            suppressing PTEN-regulated autophagy.
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Li,S., Zhang,M. and Zhang,B.
  TITLE     MTMR14 protects against hepatic ischemia-reperfusion injury through
            interacting with AKT signaling in vivo and in vitro
  JOURNAL   Biomed Pharmacother 129, 110455 (2020)
   PUBMED   32768948
  REMARK    GeneRIF: MTMR14 protects against hepatic ischemia-reperfusion
            injury through interacting with AKT signaling in vivo and in vitro.
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Romero-Suarez,S., Shen,J., Brotto,L., Hall,T., Mo,C.,
            Valdivia,H.H., Andresen,J., Wacker,M., Nosek,T.M., Qu,C.K. and
            Brotto,M.
  TITLE     Muscle-specific inositide phosphatase (MIP/MTMR14) is reduced with
            age and its loss accelerates skeletal muscle aging process by
            altering calcium homeostasis
  JOURNAL   Aging (Albany NY) 2 (8), 504-513 (2010)
   PUBMED   20817957
  REMARK    GeneRIF: a knockout mice were more susceptible to exercise-induced
            muscle damage, a trademark of muscle functional changes in older
            subjects
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Sansom,S.N., Griffiths,D.S., Faedo,A., Kleinjan,D.J., Ruan,Y.,
            Smith,J., van Heyningen,V., Rubenstein,J.L. and Livesey,F.J.
  TITLE     The level of the transcription factor Pax6 is essential for
            controlling the balance between neural stem cell self-renewal and
            neurogenesis
  JOURNAL   PLoS Genet 5 (6), e1000511 (2009)
   PUBMED   19521500
REFERENCE   8  (residues 1 to 412)
  AUTHORS   Shen,J., Yu,W.M., Brotto,M., Scherman,J.A., Guo,C., Stoddard,C.,
            Nosek,T.M., Valdivia,H.H. and Qu,C.K.
  TITLE     Deficiency of MIP/MTMR14 phosphatase induces a muscle disorder by
            disrupting Ca(2+) homeostasis
  JOURNAL   Nat Cell Biol 11 (6), 769-776 (2009)
   PUBMED   19465920
  REMARK    GeneRIF: Data report that mice deficient in the newly identified
            phosphatidylinositol phosphate phosphatase MIP/MTMR14
            (muscle-specific inositol phosphatase) show muscle weakness and
            fatigue.
REFERENCE   9  (residues 1 to 412)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   10 (residues 1 to 412)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC153592.3 and AC155287.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.11934.1,
                                           SRR7345562.2908513.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 52.74 cM"
     Protein         1..412
                     /product="phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR14 isoform 4"
                     /EC_number="3.1.3.95"
                     /note="mJumpy; phosphatidylinositol-3-phosphate
                     phosphatase; phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR14"
                     /calculated_mol_wt=46271
     Region          <38..59
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          <109..202
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     CDS             1..412
                     /gene="Mtmr14"
                     /gene_synonym="1110061O04Rik"
                     /coded_by="NM_001362185.1:432..1670"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:97287"
                     /db_xref="MGI:MGI:1916075"
ORIGIN      
        1 mdardttiys qgeqmipgqv qkmsqkrtlf fgvvtrtfli svtssekvdk aqryanftll
       61 sipypgceff keykdrdyma eglifnwkqd yvdaplnipn fltqslnidw sqyqswdlvq
      121 qtqnylklll fimnrdddsg llvhcisgwd rtplfisllr lslwadglih tslkpaeily
      181 ltvaydwflf ghmlvdrlsk geeifffcfn flkhitseef clktqrrksl ptrdagftve
      241 dicmlrhkdr gsttslgsdf slvlehspga vgsfsyetve lapagaptqa awrkshsssp
      301 qsmlwsrpqp seerlpshhg lteaksssss ssnhsdnffr mgssplevpk prltalsdre
      361 trlqevrsaf laaysstvgl raatpspsga igglleqfar gvglrgtsts tl
//
LOCUS       NP_060739                179 aa            linear   PRI 27-APR-2025
DEFINITION  acireductone dioxygenase isoform 1 [Homo sapiens].
ACCESSION   NP_060739
VERSION     NP_060739.2
DBSOURCE    REFSEQ: accession NM_018269.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Bae,D.H., Lane,D.J.R., Siafakas,A.R., Sutak,R., Paluncic,J.,
            Huang,M.L.H., Jansson,P.J., Rahmanto,Y.S. and Richardson,D.R.
  TITLE     Acireductone dioxygenase 1 (ADI1) is regulated by cellular iron by
            a mechanism involving the iron chaperone, PCBP1, with PCBP2 acting
            as a potential co-chaperone
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1866 (10), 165844 (2020)
   PUBMED   32480040
  REMARK    GeneRIF: Acireductone dioxygenase 1 (ADI1) is regulated by cellular
            iron by a mechanism involving the iron chaperone, PCBP1, with PCBP2
            acting as a potential co-chaperone.
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Qiang,L., Cao,H., Chen,J., Weller,S.G., Krueger,E.W., Zhang,L.,
            Razidlo,G.L. and McNiven,M.A.
  TITLE     Pancreatic tumor cell metastasis is restricted by MT1-MMP binding
            protein MTCBP-1
  JOURNAL   J Cell Biol 218 (1), 317-332 (2019)
   PUBMED   30487181
  REMARK    GeneRIF: Pancreatic tumor cell metastasis is restricted by MT1-MMP
            binding protein MTCBP-1.
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Su,L., Yang,K., Li,S., Liu,C., Han,J., Zhang,Y. and Xu,G.
  TITLE     Enolase-phosphatase 1 as a novel potential malignant glioma
            indicator promotes cell proliferation and migration
  JOURNAL   Oncol Rep 40 (4), 2233-2241 (2018)
   PUBMED   30066900
  REMARK    GeneRIF: High ADI1 expression is associated with malignant glioma.
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Deshpande,A.R., Pochapsky,T.C., Petsko,G.A. and Ringe,D.
  TITLE     Dual chemistry catalyzed by human acireductone dioxygenase
  JOURNAL   Protein Eng Des Sel 30 (3), 197-204 (2017)
   PUBMED   28062648
  REMARK    GeneRIF: The thermal stability of the HsARD isozymes is a function
            of the metal ion identity, with Ni2+-bound HsARD being the most
            stable followed by Co2+ and Fe2+, and Mn2+-bound HsARD being the
            least stable.
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Gotoh,I., Uekita,T. and Seiki,M.
  TITLE     Regulated nucleo-cytoplasmic shuttling of human aci-reductone
            dioxygenase (hADI1) and its potential role in mRNA processing
  JOURNAL   Genes Cells 12 (1), 105-117 (2007)
   PUBMED   17212658
  REMARK    GeneRIF: nucleo-cytoplasmic transport of hADI1 is regulated by a
            non-canonical nuclear export signal (NES) located in the N-terminal
            region of hADI1.
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Hirano,W., Gotoh,I., Uekita,T. and Seiki,M.
  TITLE     Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding
            protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase
            (ARD) in the methionine salvage pathway
  JOURNAL   Genes Cells 10 (6), 565-574 (2005)
   PUBMED   15938715
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Uekita,T., Gotoh,I., Kinoshita,T., Itoh,Y., Sato,H., Shiomi,T.,
            Okada,Y. and Seiki,M.
  TITLE     Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding
            protein-1 is a new member of the Cupin superfamily. A possible
            multifunctional protein acting as an invasion suppressor
            down-regulated in tumors
  JOURNAL   J Biol Chem 279 (13), 12734-12743 (2004)
   PUBMED   14718544
  REMARK    GeneRIF: MTCBP-1 is a new member of the Cupin superfamily with a
            role as an invasion suppressor down-regulated in tumors
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Yeh,C.T., Lai,H.Y., Chen,T.C., Chu,C.M. and Liaw,Y.F.
  TITLE     Identification of a hepatic factor capable of supporting hepatitis
            C virus replication in a nonpermissive cell line
  JOURNAL   J Virol 75 (22), 11017-11024 (2001)
   PUBMED   11602742
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB129674.1, BC001467.2,
            AB073609.1 and AC114810.4.
            
            On Mar 29, 2008 this sequence version replaced NP_060739.1.
            
            Summary: This gene encodes an enzyme that belongs to the
            aci-reductone dioxygenase family of metal-binding enzymes, which
            are involved in methionine salvage. This enzyme may regulate mRNA
            processing in the nucleus, and may carry out different functions
            depending on its localization. Related pseudogenes have been
            defined on chromosomes 8 and 20. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.151555.1,
                                           SRR1803614.65319.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155590, SAMEA2162328
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327435.11/ ENSP00000333666.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.3"
     Protein         1..179
                     /product="acireductone dioxygenase isoform 1"
                     /EC_number="1.13.11.54"
                     /EC_number="1.13.11.53"
                     /note="submergence induced protein 2; membrane-type 1
                     matrix metalloproteinase cytoplasmic tail binding
                     protein-1; MT1-MMP cytoplasmic tail-binding protein-1;
                     acireductone dioxygenase (Ni(2+)-requiring);
                     submergence-induced protein-like factor; acireductone
                     dioxygenase (Fe(2+)-requiring)"
                     /calculated_mol_wt=21367
     Region          7..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BV57.1)"
     Region          28..157
                     /region_name="cupin_ARD"
                     /note="acireductone dioxygenase (ARD), cupin domain;
                     cd02232"
                     /db_xref="CDD:380360"
     Site            order(84,88,90,94,96,133)
                     /site_type="active"
                     /db_xref="CDD:380360"
     CDS             1..179
                     /gene="ADI1"
                     /gene_synonym="APL1; ARD; ARD'; Fe-ARD; HMFT1638; MTCBP1;
                     mtnD; Ni-ARD; SIPL"
                     /coded_by="NM_018269.4:45..584"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1653.1"
                     /db_xref="GeneID:55256"
                     /db_xref="HGNC:HGNC:30576"
                     /db_xref="MIM:613400"
ORIGIN      
        1 mvqawymdda pgdprqphrp dpgrpvgleq lrrlgvlywk ldadkyendp elekirrern
       61 yswmdiitic kdklpnyeek ikmfyeehlh lddeiryild gsgyfdvrdk edqwirifme
      121 kgdmvtlpag iyhrftvdek nytkamrlfv gepvwtaynr padhfeargq yvkflaqta
//
LOCUS       NP_001350280             964 aa            linear   PRI 27-APR-2025
DEFINITION  cortactin-binding protein 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001350280 XP_005250692
VERSION     NP_001350280.1
DBSOURCE    REFSEQ: accession NM_001363351.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 964)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 964)
  AUTHORS   Shih,P.Y., Lee,S.P., Chen,Y.K. and Hsueh,Y.P.
  TITLE     Cortactin-binding protein 2 increases microtubule stability and
            regulates dendritic arborization
  JOURNAL   J Cell Sci 127 (Pt 16), 3521-3534 (2014)
   PUBMED   24928895
  REMARK    GeneRIF: Cttnbp2 increases microtubule stability and regulates
            dendritic arborization.
REFERENCE   3  (residues 1 to 964)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   4  (residues 1 to 964)
  AUTHORS   Zink,D., Amaral,M.D., Englmann,A., Lang,S., Clarke,L.A.,
            Rudolph,C., Alt,F., Luther,K., Braz,C., Sadoni,N., Rosenecker,J.
            and Schindelhauer,D.
  TITLE     Transcription-dependent spatial arrangements of CFTR and adjacent
            genes in human cell nuclei
  JOURNAL   J Cell Biol 166 (6), 815-825 (2004)
   PUBMED   15364959
  REMARK    GeneRIF: CORTBP2 (CTTNBP2) has a transcription-dependent spatial
            arrangement.
REFERENCE   5  (residues 1 to 964)
  AUTHORS   Cheung,J., Petek,E., Nakabayashi,K., Tsui,L.C., Vincent,J.B. and
            Scherer,S.W.
  TITLE     Identification of the human cortactin-binding protein-2 gene from
            the autism candidate region at 7q31
  JOURNAL   Genomics 78 (1-2), 7-11 (2001)
   PUBMED   11707066
REFERENCE   6  (residues 1 to 964)
  AUTHORS   Ohoka,Y. and Takai,Y.
  TITLE     Isolation and characterization of cortactin isoforms and a novel
            cortactin-binding protein, CBP90
  JOURNAL   Genes Cells 3 (9), 603-612 (1998)
   PUBMED   9813110
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN255418.1, AF377960.1,
            AC004240.1 and BC019644.1.
            
            On May 17, 2018 this sequence version replaced XP_005250692.1.
            
            Summary: This gene encodes a protein with six ankyrin repeats and
            several proline-rich regions. A similar gene in rat interacts with
            a central regulator of the actin cytoskeleton. [provided by RefSeq,
            Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.269520.1,
                                           SRR1660807.181825.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..964
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.31"
     Protein         1..964
                     /product="cortactin-binding protein 2 isoform 3"
                     /note="CORTBP2, C7orf8"
                     /calculated_mol_wt=106034
     Region          13..271
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          13..42
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          44..75
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(77,79,83..84,87..89,91..92,96,99,108,110,112,
                     116..117,120..122,124..125,129,132,141,143,145,149..150,
                     153..155,157..158,162,165)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          77..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          110..141
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..964
                     /gene="CTTNBP2"
                     /gene_synonym="C7orf8; CORTBP2; Orf4"
                     /coded_by="NM_001363351.1:1961..4855"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:83992"
                     /db_xref="HGNC:HGNC:15679"
                     /db_xref="MIM:609772"
ORIGIN      
        1 msggpaplag rptllqqaaa qgnvtllsml lneegldiny scedghsaly saaknghtdc
       61 vrlllsaeaq vnaadkngft plcaaaaqgh fecvellisy daninhaadg gqtplylack
      121 ngnkecikll leagtnrsvk ttdgwtpvha avdtgnvdsl kllmyhripa hgnsfneees
      181 essvfdldgg eespegiskp vvpadlinha nregwtaahi aaskgfkncl eilcrhggle
      241 perrdkcnrt vhdvatddck hllenlnalk iplrisvgei epsnygsddl ecenticaln
      301 irkqtswddf skavsqaltn hfqaissdgw wsledvtcnn ttdsniglsa rsirsitlgn
      361 vpwsvgqsfa qspwdfmrkn kaehitvlls gpqegclssv tyasmiplqm mqnylrlveq
      421 yhnvifhgpe gslqdyivhq lalclkhrqm aagfsceivr aevdagfske qlldlfissa
      481 clipvkqsps kkkiiiilen leksslsell rdflaplenr stespctfqk gnglsecyyf
      541 hencflmgti akaclqgsdl lvqqhfrwvq lrwdgepmqg llqrflrrkv vnkfkgqaps
      601 pcdpvckivd walsvwrqln sclarlgtpe allgpkyfls cpvvpghaqv tvkwmsklwn
      661 gviaprvqea ilsrasvkrq pgfgqttakr hpsqgqqavv kaalsillnk avlhgcplpr
      721 aeldqhtadf kggsfplsiv ssyntcnkkk gesgawrkvn tsprrksgrf slptwnkpdl
      781 stegmknkti sqlncnrnas lskqkslend lsltlnldqr lslgsddead lvkelqsmcs
      841 sksesdiski adsrddlrmf dssgnnpvls atinnlrmpv sqkevsplss hqttecsnsk
      901 sktelgvsrv ksflpvprsk vtqcsqntkr sssssntrqi einnnskevn wnlhknehle
      961 kpnk
//
LOCUS       NP_859078                190 aa            linear   PRI 27-APR-2025
DEFINITION  spermatogenesis-associated protein 12 [Homo sapiens].
ACCESSION   NP_859078
VERSION     NP_859078.1
DBSOURCE    REFSEQ: accession NM_181727.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Zhang,Y., Yang,L., Lin,Y., Rong,Z., Liu,X. and Li,D.
  TITLE     SPATA12 and its possible role in DNA damage induced by
            ultraviolet-C
  JOURNAL   PLoS One 8 (10), e78201 (2013)
   PUBMED   24205157
  REMARK    GeneRIF: SPATA12 could be induced under UV-C stress.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Li,D., Lin,Y., Liu,Z., Zhang,Y., Rong,Z. and Liu,X.
  TITLE     Transcriptional regulation of human novel gene SPATA12 promoter by
            AP-1 and HSF
  JOURNAL   Gene 511 (1), 18-25 (2012)
   PUBMED   22981541
  REMARK    GeneRIF: AP-1 is founded to be a potential transcriptional
            activator of SPATA12. The promoter activity of SPATA12 was
            drastically declined after AP-1 binding site mutation or deletion.
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Dan,L., Lifang,Y. and Guangxiu,L.
  TITLE     Expression and possible functions of a novel gene SPATA12 in human
            testis
  JOURNAL   J Androl 28 (4), 502-512 (2007)
   PUBMED   17251597
  REMARK    GeneRIF: putative function of SPATA12 is to maintain the cell in a
            differentiated state and/or to suppress cell proliferation in the
            human testis.
REFERENCE   6  (residues 1 to 190)
  AUTHORS   Li,D. and Lu,G.X.
  TITLE     Identification and expression of a novel human testis-specific gene
            by digital differential display
  JOURNAL   Chin Med J (Engl) 117 (12), 1791-1796 (2004)
   PUBMED   15603706
  REMARK    GeneRIF: Didital differential display can be confirmed by SPATA12
            as a novel computational biology-based approach for identification
            of the testis-specific expression of genes.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY221117.1.
            
            Summary: This gene is expressed primarily in testis and may play a
            role in testicular development and spermatogenesis. The encoded
            protein may be upregulated in response to ultraviolet-C radiation.
            [provided by RefSeq, Dec 2015].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY221117.1, SRR5189667.65815.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334325.2/ ENSP00000335392.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     Protein         1..190
                     /product="spermatogenesis-associated protein 12"
                     /note="spermatogenesis-related protein 5; testicular
                     tissue protein Li 184"
                     /calculated_mol_wt=20287
     CDS             1..190
                     /gene="SPATA12"
                     /gene_synonym="SRG5"
                     /coded_by="NM_181727.2:453..1025"
                     /db_xref="CCDS:CCDS2879.1"
                     /db_xref="GeneID:353324"
                     /db_xref="HGNC:HGNC:23221"
                     /db_xref="MIM:609869"
ORIGIN      
        1 msssaltcgs tleksgdtwe mkaldssrlv pwpprglgss tqhpnkphca lascqgpgvl
       61 pgaasalpel tfqgdvcqse tcqrylqaai sldiavsqin llgrpssppa lliqqgsceq
      121 vihnstpqfl gmedgdnert tgwlwrlced idaepsstgc srsnqltfte gcfvrslstv
      181 ysnthihthl
//
LOCUS       NP_055552                326 aa            linear   PRI 27-APR-2025
DEFINITION  ras association domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_055552
VERSION     NP_055552.1
DBSOURCE    REFSEQ: accession NM_014737.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Aykanli,E., Arisan,S., Arisan,E.D. and Yavuzsan,A.H.
  TITLE     Diagnostic Value of GSTP1, RASSF1, AND RASSF2 Methylation in Serum
            of Prostate Cancer Patients
  JOURNAL   Urol J 21 (3), 182-188 (2024)
   PUBMED   38493315
  REMARK    GeneRIF: Diagnostic Value of GSTP1, RASSF1, AND RASSF2 Methylation
            in Serum of Prostate Cancer Patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Liu,Z., Feng,G., Chen,Y., Fan,J., Liang,Z., Bi,J. and Dai,X.
  TITLE     Hyperhomocysteinemia may aggravate abdominal aortic aneurysm
            formation by up-regulating RASSF2
  JOURNAL   Gene 898, 148036 (2024)
   PUBMED   38036076
  REMARK    GeneRIF: Hyperhomocysteinemia may aggravate abdominal aortic
            aneurysm formation by up-regulating RASSF2.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Dhanaraman,T., Singh,S., Killoran,R.C., Singh,A., Xu,X.,
            Shifman,J.M. and Smith,M.J.
  TITLE     RASSF effectors couple diverse RAS subfamily GTPases to the Hippo
            pathway
  JOURNAL   Sci Signal 13 (653) (2020)
   PUBMED   33051258
  REMARK    GeneRIF: RASSF effectors couple diverse RAS subfamily GTPases to
            the Hippo pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Hesson,L.B., Wilson,R., Morton,D., Adams,C., Walker,M., Maher,E.R.
            and Latif,F.
  TITLE     CpG island promoter hypermethylation of a novel Ras-effector gene
            RASSF2A is an early event in colon carcinogenesis and correlates
            inversely with K-ras mutations
  JOURNAL   Oncogene 24 (24), 3987-3994 (2005)
   PUBMED   15806169
  REMARK    GeneRIF: In colonic neoplsms epigenetic (RASSF2A) and genetic
            (K-ras) changes are mutually exclusive and provide alternative
            pathways for affecting Ras signalling.
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Fujita,H., Fukuhara,S., Sakurai,A., Yamagishi,A., Kamioka,Y.,
            Nakaoka,Y., Masuda,M. and Mochizuki,N.
  TITLE     Local activation of Rap1 contributes to directional vascular
            endothelial cell migration accompanied by extension of microtubules
            on which RAPL, a Rap1-associating molecule, localizes
  JOURNAL   J Biol Chem 280 (6), 5022-5031 (2005)
   PUBMED   15569673
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Vos,M.D., Ellis,C.A., Elam,C., Ulku,A.S., Taylor,B.J. and
            Clark,G.J.
  TITLE     RASSF2 is a novel K-Ras-specific effector and potential tumor
            suppressor
  JOURNAL   J Biol Chem 278 (30), 28045-28051 (2003)
   PUBMED   12732644
  REMARK    GeneRIF: RASSF2 is a new member of the RASSF1 family of Ras
            effectors/tumor suppressors that exhibits a specificity for
            interacting with K-Ras
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Comincini,S., Castiglioni,B.M., Foti,G.M., Del Vecchio,I. and
            Ferretti,L.
  TITLE     Isolation and molecular characterization of rasfadin, a novel gene
            in the vicinity of the bovine prion gene
  JOURNAL   Mamm Genome 12 (2), 150-156 (2001)
   PUBMED   11210185
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D79990.1, DA333367.1 and
            AL133354.14.
            
            Summary: This gene encodes a protein that contains a Ras
            association domain. Similar to its cattle and sheep counterparts,
            this gene is located near the prion gene. Two alternatively spliced
            transcripts encoding the same isoform have been reported. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY154470.1, SRR1803613.260208.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379400.8/ ENSP00000368710.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..326
                     /product="ras association domain-containing protein 2"
                     /note="Ras association (RalGDS/AF-6) domain family 2; Ras
                     association (RalGDS/AF-6) domain family member 2;
                     centromere protein 34"
                     /calculated_mol_wt=37659
     Region          111..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50749.1)"
     Region          177..263
                     /region_name="RA_RASSF2"
                     /note="Ras-associating (RA) domain found in
                     Ras-association domain-containing protein 2 (RASSF2);
                     cd17221"
                     /db_xref="CDD:340741"
     Region          274..319
                     /region_name="SARAH_RASSF2"
                     /note="C-terminal SARAH domain found in Ras-association
                     domain-containing protein 2 (RASSF2); cd21893"
                     /db_xref="CDD:439187"
     Site            order(275..276,278,280,283,287,290..291,293..294,297..298,
                     301..302,304..305,308..309,312,315..316)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:439187"
     CDS             1..326
                     /gene="RASSF2"
                     /gene_synonym="CENP-34; RASFADIN"
                     /coded_by="NM_014737.3:160..1140"
                     /db_xref="CCDS:CCDS13083.1"
                     /db_xref="GeneID:9770"
                     /db_xref="HGNC:HGNC:9883"
                     /db_xref="MIM:609492"
ORIGIN      
        1 mdyshqtslv pcgqdkyisk nelllhlkty nlyyegqnlq lrhreeedef ivegllnisw
       61 glrrpirlqm qddnerirpp psssswhsgc nlgaqgttlk pltvpkvqis evdappegdq
      121 mpsstdsrgl kplqedtpql mrtrsdvgvr rrgnvrtpsd qrrirrhrfs inghfynhkt
      181 svftpaygsv tnvrinstmt tpqvlkllln kfkiensaee falyvvhtsg ekqklkatdy
      241 pliarilqgp ceqiskvflm ekdqveevty dvaqyikfem pvlksfiqkl qeeedrevkk
      301 lmrkytvlrl mirqrleeia etpati
//
LOCUS       NP_077269                543 aa            linear   PRI 27-APR-2025
DEFINITION  reticulophagy regulator 2 isoform 1 [Homo sapiens].
ACCESSION   NP_077269
VERSION     NP_077269.3
DBSOURCE    REFSEQ: accession NM_024293.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Toyoda,Y., Cattin,C.J., Stewart,M.P., Poser,I., Theis,M.,
            Kurzchalia,T.V., Buchholz,F., Hyman,A.A. and Muller,D.J.
  TITLE     Genome-scale single-cell mechanical phenotyping reveals
            disease-related genes involved in mitotic rounding
  JOURNAL   Nat Commun 8 (1), 1266 (2017)
   PUBMED   29097687
  REMARK    GeneRIF: Depleting the endoplasmic reticulum-localized protein
            FAM134A impairs mitotic progression by affecting metaphase plate
            alignment and pressure generation by delocalizing cortical myosin
            II.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Khaminets,A., Heinrich,T., Mari,M., Grumati,P., Huebner,A.K.,
            Akutsu,M., Liebmann,L., Stolz,A., Nietzsche,S., Koch,N., Mauthe,M.,
            Katona,I., Qualmann,B., Weis,J., Reggiori,F., Kurth,I., Hubner,C.A.
            and Dikic,I.
  TITLE     Regulation of endoplasmic reticulum turnover by selective autophagy
  JOURNAL   Nature 522 (7556), 354-358 (2015)
   PUBMED   26040720
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Vinayagam,A., Stelzl,U., Foulle,R., Plassmann,S., Zenkner,M.,
            Timm,J., Assmus,H.E., Andrade-Navarro,M.A. and Wanker,E.E.
  TITLE     A directed protein interaction network for investigating
            intracellular signal transduction
  JOURNAL   Sci Signal 4 (189), rs8 (2011)
   PUBMED   21900206
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Zhang,J., Liu,G., Meng,Y., Lin,H. and Lu,Y.
  TITLE     MAG-2 promotes invasion, mobility and adherence capability of lung
            cancer cells by MMP-2, CD44 and intracellular calcium in vitro
  JOURNAL   Oncol Rep 21 (3), 697-706 (2009)
   PUBMED   19212629
  REMARK    GeneRIF: MAG-2 may be a novel causal gene for lung cancer invasion
            and metastasis.
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG723788.1, BG700888.1, BC141851.1, AL136758.2, AC068946.4 and
            BU615764.1.
            
            On May 7, 2008 this sequence version replaced NP_077269.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.10067.1, AK074983.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000430297.7/ ENSP00000395249.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..543
                     /product="reticulophagy regulator 2 isoform 1"
                     /note="protein FAM134A; metastasis associated gene-2;
                     family with sequence similarity 134 member A;
                     reticulophagy regulator 2"
                     /calculated_mol_wt=57699
     Site            12..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC44.3)"
     Region          51..249
                     /region_name="RETR2_RHD"
                     /note="N-terminal reticulon-homology domain of
                     Reticulophagy regulator 2; cd22561"
                     /db_xref="CDD:411700"
     Site            100..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            204..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC44.3)"
     Region          254..287
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6NS82; propagated from
                     UniProtKB/Swiss-Prot (Q8NC44.3)"
     Region          336..394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NS82; propagated from
                     UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NC44.3)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8NC44.3)"
     Region          411..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC44.3)"
     Region          490..495
                     /region_name="LIR motif.
                     /evidence=ECO:0000305|PubMed:26040720"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC44.3)"
     Region          504..543
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC44.3)"
     CDS             1..543
                     /gene="RETREG2"
                     /gene_synonym="C2orf17; FAM134A; MAG-2"
                     /coded_by="NM_024293.6:79..1710"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2434.1"
                     /db_xref="GeneID:79137"
                     /db_xref="HGNC:HGNC:28450"
ORIGIN      
        1 masgggggnt gagggpgmgl slglglglsl gmseatseae eeaataeavg rlattlwlrl
       61 rgweavlaaa qrllvwekpl hslvtaaaln glfwllssss lrpffllsvs llayflldlw
      121 qprflpdvsa sspeephsds egagsgarph llsvpelcry laeswltfqi hlqellqykr
      181 qnpaqfcvrv csgcavlavl ghyvpgimis yivllsillw plvvyheliq rmytrlepll
      241 mqldysmkae analhhkhdk rkrqgknapp ggdeplaete seseaelagf spvvdvkkta
      301 lalaitdsel sdeeasiles ggfsvsratt pqltdvsedl dqqslpsepe etlsrdlgeg
      361 eegelapped llgrpqalsr qaldseeeee dvaaketllr lssplhfvnt hfngagsppd
      421 gvkcspggpv etlspetvsg gltalpgtls pplclvgsdp apspsilppv pqdspqplpa
      481 peeeealtte dfelldqgel eqlnaelgle petppkppda pplgpdihsl vqsdqeaqav
      541 aep
//
LOCUS       NP_055587                598 aa            linear   PRI 27-APR-2025
DEFINITION  CBP80/20-dependent translation initiation factor isoform 1 [Homo
            sapiens].
ACCESSION   NP_055587 XP_375538
VERSION     NP_055587.1
DBSOURCE    REFSEQ: accession NM_014772.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Park,Y., Park,J., Hwang,H.J., Kim,L., Jeong,K., Song,H.K.,
            Rufener,S.C., Muhlemann,O. and Kim,Y.K.
  TITLE     Translation mediated by the nuclear cap-binding complex is confined
            to the perinuclear region via a CTIF-DDX19B interaction
  JOURNAL   Nucleic Acids Res 49 (14), 8261-8276 (2021)
   PUBMED   34232997
  REMARK    GeneRIF: Translation mediated by the nuclear cap-binding complex is
            confined to the perinuclear region via a CTIF-DDX19B interaction.
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Garcia-de-Gracia,F., Gaete-Argel,A., Riquelme-Barrios,S.,
            Pereira-Montecinos,C., Rojas-Araya,B., Aguilera,P.,
            Oyarzun-Arrau,A., Rojas-Fuentes,C., Acevedo,M.L., Chnaiderman,J.,
            Valiente-Echeverria,F., Toro-Ascuy,D. and Soto-Rifo,R.
  TITLE     CBP80/20-dependent translation initiation factor (CTIF) inhibits
            HIV-1 Gag synthesis by targeting the function of the viral protein
            Rev
  JOURNAL   RNA Biol 18 (5), 745-758 (2021)
   PUBMED   33103564
  REMARK    GeneRIF: CBP80/20-dependent translation initiation factor (CTIF)
            inhibits HIV-1 Gag synthesis by targeting the function of the viral
            protein Rev.
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Krastev,D.B., Pettitt,S.J., Campbell,J., Song,F., Tanos,B.E.,
            Stoynov,S.S., Ashworth,A. and Lord,C.J.
  TITLE     Coupling bimolecular PARylation biosensors with genetic screens to
            identify PARylation targets
  JOURNAL   Nat Commun 9 (1), 2016 (2018)
   PUBMED   29789535
  REMARK    GeneRIF: CTIF was identified as a novel PARylation target of the
            TNKS2 in the centrosomal region of cells, which plays a role in the
            distribution of the centrosomal satellites.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 598)
  AUTHORS   Ong,B.A., Li,J., McDonough,J.M., Wei,Z., Kim,C., Chiavacci,R.,
            Mentch,F., Caboot,J.B., Spergel,J., Allen,J.L., Sleiman,P.M. and
            Hakonarson,H.
  TITLE     Gene network analysis in a pediatric cohort identifies novel lung
            function genes
  JOURNAL   PLoS One 8 (9), e72899 (2013)
   PUBMED   24023788
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 598)
  AUTHORS   Anttila,V., Winsvold,B.S., Gormley,P., Kurth,T., Bettella,F.,
            McMahon,G., Kallela,M., Malik,R., de Vries,B., Terwindt,G.,
            Medland,S.E., Todt,U., McArdle,W.L., Quaye,L., Koiranen,M.,
            Ikram,M.A., Lehtimaki,T., Stam,A.H., Ligthart,L., Wedenoja,J.,
            Dunham,I., Neale,B.M., Palta,P., Hamalainen,E., Schurks,M.,
            Rose,L.M., Buring,J.E., Ridker,P.M., Steinberg,S., Stefansson,H.,
            Jakobsson,F., Lawlor,D.A., Evans,D.M., Ring,S.M., Farkkila,M.,
            Artto,V., Kaunisto,M.A., Freilinger,T., Schoenen,J., Frants,R.R.,
            Pelzer,N., Weller,C.M., Zielman,R., Heath,A.C., Madden,P.A.F.,
            Montgomery,G.W., Martin,N.G., Borck,G., Gobel,H., Heinze,A.,
            Heinze-Kuhn,K., Williams,F.M.K., Hartikainen,A.L., Pouta,A., van
            den Ende,J., Uitterlinden,A.G., Hofman,A., Amin,N., Hottenga,J.J.,
            Vink,J.M., Heikkila,K., Alexander,M., Muller-Myhsok,B.,
            Schreiber,S., Meitinger,T., Wichmann,H.E., Aromaa,A.,
            Eriksson,J.G., Traynor,B., Trabzuni,D., Rossin,E., Lage,K.,
            Jacobs,S.B.R., Gibbs,J.R., Birney,E., Kaprio,J., Penninx,B.W.,
            Boomsma,D.I., van Duijn,C., Raitakari,O., Jarvelin,M.R.,
            Zwart,J.A., Cherkas,L., Strachan,D.P., Kubisch,C., Ferrari,M.D.,
            van den Maagdenberg,A.M.J.M., Dichgans,M., Wessman,M., Smith,G.D.,
            Stefansson,K., Daly,M.J., Nyholt,D.R., Chasman,D. and Palotie,A.
  CONSRTM   North American Brain Expression Consortium; UK Brain Expression
            Consortium
  TITLE     Genome-wide meta-analysis identifies new susceptibility loci for
            migraine
  JOURNAL   Nat Genet 45 (8), 912-917 (2013)
   PUBMED   23793025
REFERENCE   8  (residues 1 to 598)
  AUTHORS   Lauc,G., Huffman,J.E., Pucic,M., Zgaga,L., Adamczyk,B., Muzinic,A.,
            Novokmet,M., Polasek,O., Gornik,O., Kristic,J., Keser,T.,
            Vitart,V., Scheijen,B., Uh,H.W., Molokhia,M., Patrick,A.L.,
            McKeigue,P., Kolcic,I., Lukic,I.K., Swann,O., van Leeuwen,F.N.,
            Ruhaak,L.R., Houwing-Duistermaat,J.J., Slagboom,P.E., Beekman,M.,
            de Craen,A.J., Deelder,A.M., Zeng,Q., Wang,W., Hastie,N.D.,
            Gyllensten,U., Wilson,J.F., Wuhrer,M., Wright,A.F., Rudd,P.M.,
            Hayward,C., Aulchenko,Y., Campbell,H. and Rudan,I.
  TITLE     Loci associated with N-glycosylation of human immunoglobulin G show
            pleiotropy with autoimmune diseases and haematological cancers
  JOURNAL   PLoS Genet 9 (1), e1003225 (2013)
   PUBMED   23382691
REFERENCE   9  (residues 1 to 598)
  AUTHORS   Choe,J., Cho,H., Chi,S.G. and Kim,Y.K.
  TITLE     Ago2/miRISC-mediated inhibition of CBP80/20-dependent translation
            and thereby abrogation of nonsense-mediated mRNA decay require the
            cap-associating activity of Ago2
  JOURNAL   FEBS Lett 585 (17), 2682-2687 (2011)
   PUBMED   21840310
  REMARK    GeneRIF: Study reveals that Ago2, but not Ago2F2V2, inhibits the
            binding of CBP80/20 to cap structure.
REFERENCE   10 (residues 1 to 598)
  AUTHORS   Kim,K.M., Cho,H., Choi,K., Kim,J., Kim,B.W., Ko,Y.G., Jang,S.K. and
            Kim,Y.K.
  TITLE     A new MIF4G domain-containing protein, CTIF, directs nuclear
            cap-binding protein CBP80/20-dependent translation
  JOURNAL   Genes Dev 23 (17), 2033-2045 (2009)
   PUBMED   19648179
  REMARK    GeneRIF: a new MIF4G domain-containing protein, CTIF that interacts
            directly with CBP80 and is part of the CBP80/20-dependent
            translation initiation complex [CBP80/20-dependent translation
            initiation factor, CTIF]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC048380.12, AB007887.1, AK095970.1, BC042146.1 and BU688371.1.
            
            On Mar 8, 2004 this sequence version replaced XP_375538.1.
            
            Summary: CTIF is a component of the CBP80 (NCBP1; MIM 600469)/CBP20
            (NCBP2; MIM 605133) translation initiation complex that binds
            cotranscriptionally to the cap end of nascent mRNA. The CBP80/CBP20
            complex is involved in a simultaneous editing and translation step
            that recognizes premature termination codons (PTCs) in mRNAs and
            directs PTC-containing mRNAs toward nonsense-mediated decay (NMD).
            On mRNAs without PTCs, the CBP80/CBP20 complex is replaced with
            cytoplasmic mRNA cap-binding proteins, including EIF4G (MIM
            600495), and steady-state translation of the mRNAs resumes in the
            cytoplasm (Kim et al., 2009 [PubMed 19648179]).[supplied by OMIM,
            Dec 2009].
            
            Transcript Variant: This variant (1) represents the more
            predominant transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB007887.1, SRR7346977.2419178.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256413.8/ ENSP00000256413.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..598
                     /product="CBP80/20-dependent translation initiation factor
                     isoform 1"
                     /note="CBP80/20-dependent translation initiation factor"
                     /calculated_mol_wt=67456
     Region          1..305
                     /region_name="Interaction with NCBP1/CBP80.
                     /evidence=ECO:0000269|PubMed:19648179"
                     /note="propagated from UniProtKB/Swiss-Prot (O43310.1)"
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43310.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O43310.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43310.1)"
     Region          43..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43310.1)"
     Region          180..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43310.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43310.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43310.1)"
     Region          376..577
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     CDS             1..598
                     /gene="CTIF"
                     /gene_synonym="Gm672; KIAA0427"
                     /coded_by="NM_014772.3:311..2107"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11935.1"
                     /db_xref="GeneID:9811"
                     /db_xref="HGNC:HGNC:23925"
                     /db_xref="MIM:613178"
ORIGIN      
        1 menssaasas seagssrsqe ieelerfids yvleyqvqgl ladktegdge sertqshisq
       61 wtadcsepld sscsfsrgra ppqqngskdn sldmlgtdiw aantfdsfsg atwdlqpekl
      121 dftqfhrkvr htpkqplphi dregcgkgkl edgdginlnd iekvlpawqg yhpmphevei
      181 ahtkklfrrr rndrrrqqrp pggnkpqqhg dhqpgsakhn rdhqksyqgg saphpsgrpt
      241 hhgysqnrrw hhgnmkhppg dkgeagahrn aketmtienp kledtagdtg hssleaprsp
      301 dtlapvaser lppqqsggpe vetkrkdsil perigerpki tllqsskdrl rrrlkekdev
      361 avetttpqqn kmdklieiln smrnnssdvd tklttfmeea qnstnseeml geivrtiyqk
      421 avsdrsfaft aaklcdkmal fmvegtkfrs lllnmlqkdf tvreelqqqd verwlgfitf
      481 lcevfgtmrs stgepfrvlv cpiytclrel lqsqdvkeda vlccsmelqs tgrlleeqlp
      541 emmtellasa rdkmlcpses mltrslllev ielhanswnp ltppitqyyn rtiqklta
//
LOCUS       NP_004834                636 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-27 receptor subunit alpha precursor [Homo sapiens].
ACCESSION   NP_004834
VERSION     NP_004834.1
DBSOURCE    REFSEQ: accession NM_004843.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Martin,E., Winter,S., Garcin,C., Tanita,K., Hoshino,A., Lenoir,C.,
            Fournier,B., Migaud,M., Boutboul,D., Simonin,M., Fernandes,A.,
            Bastard,P., Le Voyer,T., Roupie,A.L., Ben Ahmed,Y.,
            Leruez-Ville,M., Burgard,M., Rao,G., Ma,C.S., Masson,C.,
            Soudais,C., Picard,C., Bustamante,J., Tangye,S.G., Cheikh,N.,
            Seppanen,M., Puel,A., Daly,M., Casanova,J.L., Neven,B., Fischer,A.
            and Latour,S.
  TITLE     Role of IL-27 in Epstein-Barr virus infection revealed by IL-27RA
            deficiency
  JOURNAL   Nature 628 (8008), 620-629 (2024)
   PUBMED   38509369
  REMARK    GeneRIF: Role of IL-27 in Epstein-Barr virus infection revealed by
            IL-27RA deficiency.
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Brownlie,R.J., Kennedy,R., Wilson,E.B., Milanovic,M., Taylor,C.F.,
            Wang,D., Davies,J.R., Owston,H., Adams,E.J., Stephenson,S.,
            Caeser,R., Gewurz,B.E., Giannoudis,P.V., Scuoppo,C., McGonagle,D.,
            Hodson,D.J., Tooze,R.M., Doody,G.M., Cook,G., Westhead,D.R. and
            Klein,U.
  TITLE     Cytokine receptor IL27RA is an NF-kappaB-responsive gene involved
            in CD38 upregulation in multiple myeloma
  JOURNAL   Blood Adv 7 (15), 3874-3890 (2023)
   PUBMED   36867577
  REMARK    GeneRIF: Cytokine receptor IL27RA is an NF-kappaB-responsive gene
            involved in CD38 upregulation in multiple myeloma.
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Jin,Y., Fyfe,P.K., Gardner,S., Wilmes,S., Bubeck,D. and Moraga,I.
  TITLE     Structural insights into the assembly and activation of the IL-27
            signaling complex
  JOURNAL   EMBO Rep 23 (10), e55450 (2022)
   PUBMED   35920255
  REMARK    GeneRIF: Structural insights into the assembly and activation of
            the IL-27 signaling complex.
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Aghayev,T., Mazitova,A.M., Fang,J.R., Peshkova,I.O., Rausch,M.,
            Hung,M., White,K.F., Masia,R., Titerina,E.K., Fatkhullina,A.R.,
            Cousineau,I., Turcotte,S., Zhigarev,D., Marchenko,A.,
            Khoziainova,S., Makhov,P., Tan,Y.F., Kossenkov,A.V., Wiest,D.L.,
            Stagg,J., Wang,X.W., Campbell,K.S., Dzutsev,A.K., Trinchieri,G.,
            Hill,J.A., Grivennikov,S.I. and Koltsova,E.K.
  TITLE     IL27 Signaling Serves as an Immunologic Checkpoint for Innate
            Cytotoxic Cells to Promote Hepatocellular Carcinoma
  JOURNAL   Cancer Discov 12 (8), 1960-1983 (2022)
   PUBMED   35723626
  REMARK    GeneRIF: IL27 Signaling Serves as an Immunologic Checkpoint for
            Innate Cytotoxic Cells to Promote Hepatocellular Carcinoma.
REFERENCE   5  (residues 1 to 636)
  AUTHORS   Wu,M., Xia,X., Hu,J., Fowlkes,N.W. and Li,S.
  TITLE     WSX1 act as a tumor suppressor in hepatocellular carcinoma by
            downregulating neoplastic PD-L1 expression
  JOURNAL   Nat Commun 12 (1), 3500 (2021)
   PUBMED   34108491
  REMARK    GeneRIF: WSX1 act as a tumor suppressor in hepatocellular carcinoma
            by downregulating neoplastic PD-L1 expression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 636)
  AUTHORS   Pflanz,S., Hibbert,L., Mattson,J., Rosales,R., Vaisberg,E.,
            Bazan,J.F., Phillips,J.H., McClanahan,T.K., de Waal Malefyt,R. and
            Kastelein,R.A.
  TITLE     WSX-1 and glycoprotein 130 constitute a signal-transducing receptor
            for IL-27
  JOURNAL   J Immunol 172 (4), 2225-2231 (2004)
   PUBMED   14764690
  REMARK    GeneRIF: WSX-1 together with the cytokine receptor gp130
            constitutes a functional signal-transducing receptor for IL-27.
REFERENCE   7  (residues 1 to 636)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 636)
  AUTHORS   Takeda,A., Hamano,S., Yamanaka,A., Hanada,T., Ishibashi,T.,
            Mak,T.W., Yoshimura,A. and Yoshida,H.
  TITLE     Cutting edge: role of IL-27/WSX-1 signaling for induction of T-bet
            through activation of STAT1 during initial Th1 commitment
  JOURNAL   J Immunol 170 (10), 4886-4890 (2003)
   PUBMED   12734330
  REMARK    GeneRIF: WSX-1 is essential for transcriptional activation of STAT1
            and for augmenting the induction of T-bet expression during
            initiation of Th1 cell differentiation.
REFERENCE   9  (residues 1 to 636)
  AUTHORS   Pflanz,S., Timans,J.C., Cheung,J., Rosales,R., Kanzler,H.,
            Gilbert,J., Hibbert,L., Churakova,T., Travis,M., Vaisberg,E.,
            Blumenschein,W.M., Mattson,J.D., Wagner,J.L., To,W., Zurawski,S.,
            McClanahan,T.K., Gorman,D.M., Bazan,J.F., de Waal Malefyt,R.,
            Rennick,D. and Kastelein,R.A.
  TITLE     IL-27, a heterodimeric cytokine composed of EBI3 and p28 protein,
            induces proliferation of naive CD4+ T cells
  JOURNAL   Immunity 16 (6), 779-790 (2002)
   PUBMED   12121660
REFERENCE   10 (residues 1 to 636)
  AUTHORS   Sprecher,C.A., Grant,F.J., Baumgartner,J.W., Presnell,S.R.,
            Schrader,S.K., Yamagiwa,T., Whitmore,T.E., O'Hara,P.J. and
            Foster,D.F.
  TITLE     Cloning and characterization of a novel class I cytokine receptor
  JOURNAL   Biochem Biophys Res Commun 246 (1), 82-90 (1998)
   PUBMED   9600072
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF053004.1, AF106912.1 and
            AC022098.9.
            
            Summary: In mice, CD4+ helper T-cells differentiate into type 1
            (Th1) cells, which are critical for cell-mediated immunity,
            predominantly under the influence of IL12. Also, IL4 influences
            their differentiation into type 2 (Th2) cells, which are critical
            for most antibody responses. Mice deficient in these cytokines,
            their receptors, or associated transcription factors have impaired,
            but are not absent of, Th1 or Th2 immune responses. This gene
            encodes a protein which is similar to the mouse T-cell cytokine
            receptor Tccr at the amino acid level, and is predicted to be a
            glycosylated transmembrane protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF106912.1, AY358876.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263379.4/ ENSP00000263379.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..636
                     /product="interleukin-27 receptor subunit alpha precursor"
                     /note="T-cell cytokine receptor type 1; class I cytokine
                     receptor; interleukin 27 receptor, alpha; IL-27R-alpha;
                     IL-27R subunit alpha; cytokine receptor-like 1; IL-27
                     receptor subunit alpha; type I T-cell cytokine receptor;
                     cytokine receptor WSX-1"
                     /calculated_mol_wt=65704
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3788
     mat_peptide     33..636
                     /product="Interleukin-27 receptor subunit alpha.
                     /id=PRO_0000010876"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWB1.2)"
                     /calculated_mol_wt=65704
     Site            51
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWB1.2)"
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWB1.2)"
     Region          128..228
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(128,198,211)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          217..221
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWB1.2)"
     Site            order(217..218,220..221)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            302
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWB1.2)"
     Site            311
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWB1.2)"
     Region          321..394
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            374
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWB1.2)"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWB1.2)"
     Site            467
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWB1.2)"
     Site            517..537
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWB1.2)"
     Region          554..562
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWB1.2)"
     Region          587..636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWB1.2)"
     CDS             1..636
                     /gene="IL27RA"
                     /gene_synonym="CRL1; IL-27RA; IL27R; TCCR; WSX1; zcytor1"
                     /coded_by="NM_004843.4:112..2022"
                     /db_xref="CCDS:CCDS12303.1"
                     /db_xref="GeneID:9466"
                     /db_xref="HGNC:HGNC:17290"
                     /db_xref="MIM:605350"
ORIGIN      
        1 mrggrgapfw lwplpklall pllwvlfqrt rpqgsagplq cygvgplgdl ncsweplgdl
       61 gapselhlqs qkyrsnktqt vavaagrswv aipreqltms dkllvwgtka gqplwppvfv
      121 nletqmkpna prlgpdvdfs eddpleatvh wapptwpshk vlicqfhyrr cqeaawtlle
      181 pelktipltp veiqdlelat gykvygrcrm ekeedlwgew spilsfqtpp sapkdvwvsg
      241 nlcgtpggee plllwkapgp cvqvsykvwf wvggrelspe gitcccslip sgaewarvsa
      301 vnatsweplt nlslvcldsa saprsvavss iagstellvt wqpgpgeple hvvdwardgd
      361 pleklnwvrl ppgnlsallp gnftvgvpyr itvtavsasg lasassvwgf reelaplvgp
      421 tlwrlqdapp gtpaiawgev prhqlrghlt hytlcaqsgt spsvcmnvsg ntqsvtlpdl
      481 pwgpcelwvt astiagqgpp gpilrlhlpd ntlrwkvlpg ilflwglfll gcglslatsg
      541 rcyhlrhkvl prwvwekvpd pansssgqph meqvpeaqpl gdlpilevee mepppvmess
      601 qpaqatapld sgyekhflpt peelgllgpp rpqvla
//
LOCUS       NP_004950                461 aa            linear   PRI 27-APR-2025
DEFINITION  steroidogenic factor 1 [Homo sapiens].
ACCESSION   NP_004950
VERSION     NP_004950.2
DBSOURCE    REFSEQ: accession NM_004959.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Wen,F., Ding,Y., Wang,M., Du,J., Zhang,S. and Kee,K.
  TITLE     FOXL2 and NR5A1 induce human fibroblasts into steroidogenic ovarian
            granulosa-like cells
  JOURNAL   Cell Prolif 57 (5), e13589 (2024)
   PUBMED   38192172
  REMARK    GeneRIF: FOXL2 and NR5A1 induce human fibroblasts into
            steroidogenic ovarian granulosa-like cells.
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Houzelstein,D., Eozenou,C., Lagos,C.F., Elzaiat,M.,
            Bignon-Topalovic,J., Gonzalez,I., Laville,V., Schlick,L.,
            Wankanit,S., Madon,P., Kirtane,J., Athalye,A., Buonocore,F.,
            Bigou,S., Conway,G.S., Bohl,D., Achermann,J.C., Bashamboo,A. and
            McElreavey,K.
  TITLE     A conserved NR5A1-responsive enhancer regulates SRY in
            testis-determination
  JOURNAL   Nat Commun 15 (1), 2796 (2024)
   PUBMED   38555298
  REMARK    GeneRIF: A conserved NR5A1-responsive enhancer regulates SRY in
            testis-determination.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Dottermusch,M., Ryba,A., Ricklefs,F.L., Flitsch,J., Schmid,S.,
            Glatzel,M., Saeger,W., Neumann,J.E. and Schuller,U.
  TITLE     Pituitary neuroendocrine tumors with PIT1/SF1 co-expression show
            distinct clinicopathological and molecular features
  JOURNAL   Acta Neuropathol 147 (1), 16 (2024)
   PUBMED   38228887
  REMARK    GeneRIF: Pituitary neuroendocrine tumors with PIT1/SF1
            co-expression show distinct clinicopathological and molecular
            features.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Sadovsky,Y., Crawford,P.A., Woodson,K.G., Polish,J.A.,
            Clements,M.A., Tourtellotte,L.M., Simburger,K. and Milbrandt,J.
  TITLE     Mice deficient in the orphan receptor steroidogenic factor 1 lack
            adrenal glands and gonads but express P450 side-chain-cleavage
            enzyme in the placenta and have normal embryonic serum levels of
            corticosteroids
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 10939-10943 (1995)
   PUBMED   7479914
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Sasano,H., Shizawa,S., Suzuki,T., Takayama,K., Fukaya,T.,
            Morohashi,K. and Nagura,H.
  TITLE     Ad4BP in the human adrenal cortex and its disorders
  JOURNAL   J Clin Endocrinol Metab 80 (8), 2378-2380 (1995)
   PUBMED   7629233
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Taketo,M., Parker,K.L., Howard,T.A., Tsukiyama,T., Wong,M.,
            Niwa,O., Morton,C.C., Miron,P.M. and Seldin,M.F.
  TITLE     Homologs of Drosophila Fushi-Tarazu factor 1 map to mouse
            chromosome 2 and human chromosome 9q33
  JOURNAL   Genomics 25 (2), 565-567 (1995)
   PUBMED   7789992
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Shen,W.H., Moore,C.C., Ikeda,Y., Parker,K.L. and Ingraham,H.A.
  TITLE     Nuclear receptor steroidogenic factor 1 regulates the mullerian
            inhibiting substance gene: a link to the sex determination cascade
  JOURNAL   Cell 77 (5), 651-661 (1994)
   PUBMED   8205615
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Mohnach,L., Fechner,P.Y. and Keegan,C.E.
  TITLE     Nonsyndromic Disorders of Testicular Development Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301714
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Delot,E.C. and Vilain,E.J.
  TITLE     Nonsyndromic 46,XX Testicular Disorders/Differences of Sex
            Development
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301589
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC032501.1, U76388.1 and
            AK090858.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 8, 2002 this sequence version replaced NP_004950.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            activator involved in sex determination. The encoded protein binds
            DNA as a monomer. Defects in this gene are a cause of XY sex
            reversal with or without adrenal failure as well as adrenocortical
            insufficiency without ovarian defect. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032501.1, SRR14038192.1997746.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267761, SAMN03267762
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373588.9/ ENSP00000362690.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..461
                     /product="steroidogenic factor 1"
                     /note="fushi tarazu factor homolog 1; adrenal 4 binding
                     protein; steroid hormone receptor Ad4BP; steroidogenic
                     factor-1; steroidogenic factor 1 nuclear receptor; nuclear
                     receptor AdBP4; STF-1"
                     /calculated_mol_wt=51505
     Region          13..105
                     /region_name="NR_DBD_Lrh-1_like"
                     /note="The DNA-binding domain of Lrh-1 like nuclear
                     receptor family like is composed of two C4-type zinc
                     fingers; cd07167"
                     /db_xref="CDD:143541"
     Site            order(13,16,30,33,49,55,65,68)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143541"
     Site            order(23..25,31..32,34,36,38..39,42,62..63,69,82..84,
                     87..93,99)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143541"
     Site            34
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000305|PubMed:11479297; propagated from
                     UniProtKB/Swiss-Prot (Q13285.2)"
     Site            38
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000305|PubMed:11479297; propagated from
                     UniProtKB/Swiss-Prot (Q13285.2)"
     Site            72
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000305|PubMed:11479297; propagated from
                     UniProtKB/Swiss-Prot (Q13285.2)"
     Region          119..157
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13285.2)"
     Region          <137..216
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK7.
                     /evidence=ECO:0000269|PubMed:10230405,
                     ECO:0000269|PubMed:17901130, ECO:0000269|PubMed:19015234;
                     propagated from UniProtKB/Swiss-Prot (Q13285.2)"
     Region          223..459
                     /region_name="NR_LBD_SF-1"
                     /note="The ligand binding domain of nuclear receptor
                     steroidogenic factor 1, a member of nuclear receptor
                     superfamily; cd07070"
                     /db_xref="CDD:132755"
     Region          230..461
                     /region_name="Important for dimerization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13285.2)"
     Site            order(262,265,303,306..307,310,323,325,331,335..336,
                     339..341,344,351,430,433,436..437,440)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132755"
     Site            order(294..295,451,454..455)
                     /site_type="active"
                     /note="corepressor recognition site [active]"
                     /db_xref="CDD:132755"
     CDS             1..461
                     /gene="NR5A1"
                     /gene_synonym="AD4BP; ELP; FTZ1; FTZF1; hSF-1; POF7; SF-1;
                     SF1; SPGF8; SRXX4; SRXY3"
                     /coded_by="NM_004959.5:167..1552"
                     /db_xref="CCDS:CCDS6856.1"
                     /db_xref="GeneID:2516"
                     /db_xref="HGNC:HGNC:7983"
                     /db_xref="MIM:184757"
ORIGIN      
        1 mdysydedld elcpvcgdkv sgyhyglltc esckgffkrt vqnnkhytct esqsckidkt
       61 qrkrcpfcrf qkcltvgmrl eavradrmrg grnkfgpmyk rdralkqqkk aqirangfkl
      121 etgppmgvpp ppppapdyvl ppslhgpepk glaagppagp lgdfgapalp mavpgahgpl
      181 agylypafpg raikseypep yasppqpglp ygypepfsgg pnvpelilql lqlepdedqv
      241 rarilgclqe ptksrpdqpa afgllcrmad qtfisivdwa rrcmvfkele vadqmtllqn
      301 cwsellvfdh iyrqvqhgke gsillvtgqe velttvatqa gsllhslvlr aqelvlqlla
      361 lqldrqefvc lkfiilfsld lkflnnhilv kdaqekanaa lldytlchyp hcgdkfqqll
      421 lclvevrals mqakeylyhk hlgnemprnn lliemlqakq t
//
LOCUS       NP_002051                333 aa            linear   PRI 27-APR-2025
DEFINITION  gap junction alpha-4 protein [Homo sapiens].
ACCESSION   NP_002051
VERSION     NP_002051.2
DBSOURCE    REFSEQ: accession NM_002060.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Pithova,P., Cichrova,M., Kvapil,M., Hubacek,J.A., Dlouha,D. and
            Pitha,J.
  TITLE     Determinants of vascular impairment in type 1 diabetes-impact of
            sex and connexin 37 gene polymorphism: A cross-sectional study
  JOURNAL   Cardiovasc Diabetol 23 (1), 309 (2024)
   PUBMED   39175027
  REMARK    GeneRIF: Determinants of vascular impairment in type 1
            diabetes-impact of sex and connexin 37 gene polymorphism: A
            cross-sectional study.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Huo,R., Yang,Y., Xu,H., Zhao,S., Song,D., Weng,J., Ma,R., Sun,Y.,
            Wang,J., Jiao,Y., Zhang,J., He,Q., Wu,R., Wang,S., Zhao,J.Z.,
            Zhang,J., Wang,J. and Cao,Y.
  TITLE     Somatic GJA4 mutation in intracranial extra-axial cavernous
            hemangiomas
  JOURNAL   Stroke Vasc Neurol 8 (6), 453-462 (2023)
   PUBMED   37072338
  REMARK    GeneRIF: Somatic GJA4 mutation in intracranial extra-axial
            cavernous hemangiomas.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Acharya,B.R., Fang,J.S., Jeffery,E.D., Chavkin,N.W., Genet,G.,
            Vasavada,H., Nelson,E.A., Sheynkman,G.M., Humphries,M.J. and
            Hirschi,K.K.
  TITLE     Connexin 37 sequestering of activated-ERK in the cytoplasm promotes
            p27-mediated endothelial cell cycle arrest
  JOURNAL   Life Sci Alliance 6 (8), e202201685 (2023)
   PUBMED   37197981
  REMARK    GeneRIF: Connexin 37 sequestering of activated-ERK in the cytoplasm
            promotes p27-mediated endothelial cell cycle arrest.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hongo,H., Miyawaki,S., Teranishi,Y., Mitsui,J., Katoh,H.,
            Komura,D., Tsubota,K., Matsukawa,T., Watanabe,M., Kurita,M.,
            Yoshimura,J., Dofuku,S., Ohara,K., Ishigami,D., Okano,A., Kato,M.,
            Hakuno,F., Takahashi,A., Kunita,A., Ishiura,H., Shin,M.,
            Nakatomi,H., Nagao,T., Goto,H., Takahashi,S.I., Ushiku,T.,
            Ishikawa,S., Okazaki,M., Morishita,S., Tsuji,S. and Saito,N.
  TITLE     Somatic GJA4 gain-of-function mutation in orbital cavernous venous
            malformations
  JOURNAL   Angiogenesis 26 (1), 37-52 (2023)
   PUBMED   35902510
  REMARK    GeneRIF: Somatic GJA4 gain-of-function mutation in orbital
            cavernous venous malformations.
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Chen,K.H., Huang,H.Y., Chen,T.C., Liu,Y.J., Lin,I.C., Ng,K.F.,
            Chuang,H.C. and Huang,S.C.
  TITLE     A clinicopathological reappraisal of orbital vascular malformations
            and distinctive GJA4 mutation in cavernous venous malformations
  JOURNAL   Hum Pathol 130, 79-87 (2022)
   PUBMED   36209871
  REMARK    GeneRIF: A clinicopathological reappraisal of orbital vascular
            malformations and distinctive GJA4 mutation in cavernous venous
            malformations.
            Review article
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Reed,K.E., Westphale,E.M., Larson,D.M., Wang,H.Z., Veenstra,R.D.
            and Beyer,E.C.
  TITLE     Molecular cloning and functional expression of human connexin37, an
            endothelial cell gap junction protein
  JOURNAL   J Clin Invest 91 (3), 997-1004 (1993)
   PUBMED   7680674
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Haefliger,J.A., Bruzzone,R., Jenkins,N.A., Gilbert,D.J.,
            Copeland,N.G. and Paul,D.L.
  TITLE     Four novel members of the connexin family of gap junction proteins.
            Molecular cloning, expression, and chromosome mapping
  JOURNAL   J Biol Chem 267 (3), 2057-2064 (1992)
   PUBMED   1370487
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Willecke,K., Jungbluth,S., Dahl,E., Hennemann,H., Heynkes,R. and
            Grzeschik,K.H.
  TITLE     Six genes of the human connexin gene family coding for gap
            junctional proteins are assigned to four different human
            chromosomes
  JOURNAL   Eur J Cell Biol 53 (2), 275-280 (1990)
   PUBMED   1964417
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Beyer,E.C., Paul,D.L. and Goodenough,D.A.
  TITLE     Connexin family of gap junction proteins
  JOURNAL   J Membr Biol 116 (3), 187-194 (1990)
   PUBMED   2167375
  REMARK    Review article
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Risek,B., Guthrie,S., Kumar,N. and Gilula,N.B.
  TITLE     Modulation of gap junction transcript and protein expression during
            pregnancy in the rat
  JOURNAL   J Cell Biol 110 (2), 269-282 (1990)
   PUBMED   1688855
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU103361.1, BC072389.1 and
            BC027889.1.
            
            On Apr 22, 2005 this sequence version replaced NP_002051.1.
            
            Summary: This gene encodes a member of the connexin gene family.
            The encoded protein is a component of gap junctions, which are
            composed of arrays of intercellular channels that provide a route
            for the diffusion of low molecular weight materials from cell to
            cell. Mutations in this gene have been associated with
            atherosclerosis and a higher risk of myocardial infarction.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.63189.1,
                                           SRR3476690.817105.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342280.5/ ENSP00000343676.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..333
                     /product="gap junction alpha-4 protein"
                     /note="connexin-37; gap junction protein, alpha 4, 37kDa"
                     /calculated_mol_wt=37283
     Region          3..220
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            21..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35212.3)"
     Site            77..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35212.3)"
     Site            149..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35212.3)"
     Site            208..230
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35212.3)"
     Region          292..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35212.3)"
     CDS             1..333
                     /gene="GJA4"
                     /gene_synonym="CX37"
                     /coded_by="NM_002060.3:88..1089"
                     /db_xref="CCDS:CCDS30669.1"
                     /db_xref="GeneID:2701"
                     /db_xref="HGNC:HGNC:4278"
                     /db_xref="MIM:121012"
ORIGIN      
        1 mgdwgflekl ldqvqehstv vgkiwltvlf ifrililgla gesvwgdeqs dfecntaqpg
       61 ctnvcydqaf pishirywvl qflfvstptl vylghviyls rreerlrqke gelralpakd
      121 pqveralaav erqmakisva edgrlrirga lmgtyvasvl cksvleagfl ygqwrlygwt
      181 mepvfvcqra pcpylvdcfv srptektifi ifmlvvglis lvlnllelvh llcrclsrgm
      241 rarqgqdapp tqgtssdpyt dqvffylpvg qgpssppcpt ynglssseqn wanltteerl
      301 assrpplfld pppqngqkpp srpsssaskk qyv
//
LOCUS       NP_078934               1081 aa            linear   PRI 27-APR-2025
DEFINITION  importin-4 [Homo sapiens].
ACCESSION   NP_078934
VERSION     NP_078934.3
DBSOURCE    REFSEQ: accession NM_024658.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Guo,Y., Tao,T., Wu,T., Hou,J. and Lin,W.
  TITLE     Nucleoporin Nup98 is an essential factor for ipo4 dependent protein
            import
  JOURNAL   J Cell Biochem 125 (7), e30573 (2024)
   PUBMED   38780165
  REMARK    GeneRIF: Nucleoporin Nup98 is an essential factor for ipo4
            dependent protein import.
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Zhou,Y., Liu,F., Xu,Q., Yang,B., Li,X., Jiang,S., Hu,L., Zhang,X.,
            Zhu,L., Li,Q., Zhu,X., Shao,H., Dai,M., Shen,Y., Ni,B., Wang,S.,
            Zhang,Z. and Teng,Y.
  TITLE     Inhibiting Importin 4-mediated nuclear import of CEBPD enhances
            chemosensitivity by repression of PRKDC-driven DNA damage repair in
            cervical cancer
  JOURNAL   Oncogene 39 (34), 5633-5648 (2020)
   PUBMED   32661323
  REMARK    GeneRIF: Inhibiting Importin 4-mediated nuclear import of CEBPD
            enhances chemosensitivity by repression of PRKDC-driven DNA damage
            repair in cervical cancer.
REFERENCE   4  (residues 1 to 1081)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1081)
  AUTHORS   Xu,X., Zhang,X., Xing,H., Liu,Z., Jia,J., Jin,C. and Zhang,Y.
  TITLE     Importin-4 functions as a driving force in human primary gastric
            cancer
  JOURNAL   J Cell Biochem 120 (8), 12638-12646 (2019)
   PUBMED   30861176
  REMARK    GeneRIF: Importin-4 functions as a driving force in human primary
            gastric cancer.
REFERENCE   6  (residues 1 to 1081)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   7  (residues 1 to 1081)
  AUTHORS   Miyauchi,Y., Michigami,T., Sakaguchi,N., Sekimoto,T., Yoneda,Y.,
            Pike,J.W., Yamagata,M. and Ozono,K.
  TITLE     Importin 4 is responsible for ligand-independent nuclear
            translocation of vitamin D receptor
  JOURNAL   J Biol Chem 280 (49), 40901-40908 (2005)
   PUBMED   16207705
  REMARK    GeneRIF: demonstrated that vitamin D receptor (VDR) has two nuclear
            import systems: ligand-dependent & ligand-independent pathways, &
            that importin 4 fulfills the ligand-independent nuclear transport
            through the interaction with the amino terminus of VDR
REFERENCE   8  (residues 1 to 1081)
  AUTHORS   Tagami,H., Ray-Gallet,D., Almouzni,G. and Nakatani,Y.
  TITLE     Histone H3.1 and H3.3 complexes mediate nucleosome assembly
            pathways dependent or independent of DNA synthesis
  JOURNAL   Cell 116 (1), 51-61 (2004)
   PUBMED   14718166
REFERENCE   9  (residues 1 to 1081)
  AUTHORS   Lischka,P., Sorg,G., Kann,M., Winkler,M. and Stamminger,T.
  TITLE     A nonconventional nuclear localization signal within the UL84
            protein of human cytomegalovirus mediates nuclear import via the
            importin alpha/beta pathway
  JOURNAL   J Virol 77 (6), 3734-3748 (2003)
   PUBMED   12610148
REFERENCE   10 (residues 1 to 1081)
  AUTHORS   Jakel,S., Mingot,J.M., Schwarzmaier,P., Hartmann,E. and Gorlich,D.
  TITLE     Importins fulfil a dual function as nuclear import receptors and
            cytoplasmic chaperones for exposed basic domains
  JOURNAL   EMBO J 21 (3), 377-386 (2002)
   PUBMED   11823430
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK056527.1, BC003690.1 and AK094897.1.
            
            On Apr 9, 2005 this sequence version replaced NP_078934.2.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110804.1, AK057277.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354464.11/ ENSP00000346453.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..1081
                     /product="importin-4"
                     /note="imp4b; ranBP4; importin-4b; ran-binding protein 4"
                     /calculated_mol_wt=118585
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8TEX9.2)"
     Region          24..90
                     /region_name="IBN_N"
                     /note="Importin-beta N-terminal domain; smart00913"
                     /db_xref="CDD:197981"
     Region          348..385
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEX9.2)"
     Region          353..381
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          <357..>620
                     /region_name="KAP95"
                     /note="Karyopherin (importin) beta [Intracellular
                     trafficking and secretion]; COG5215"
                     /db_xref="CDD:227540"
     Site            order(370..371,374,377..378,381,412..413,416,419..420,423,
                     456..457,460,463..464,498..499,502,505..506)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          390..427
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEX9.2)"
     Region          394..424
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          431..471
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEX9.2)"
     Region          435..464
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          475..513
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEX9.2)"
     Region          477..507
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          519..551
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          895..932
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEX9.2)"
     Region          936..974
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEX9.2)"
     CDS             1..1081
                     /gene="IPO4"
                     /gene_synonym="Imp4"
                     /coded_by="NM_024658.4:30..3275"
                     /db_xref="CCDS:CCDS9616.1"
                     /db_xref="GeneID:79711"
                     /db_xref="HGNC:HGNC:19426"
ORIGIN      
        1 mesagleqll relllpdter irrateqlqi vlrapaalpa lcdllasaad pqirqfaavl
       61 trrrlntrwr rlaaeqresl ksliltalqr etehcvslsl aqlsatifrk egleawpqll
      121 qllqhsthsp hsperemgll llsvvvtsrp eafqphhrel lrllnetlge vgspgllfys
      181 lrtlttmapy lstedvplar mlvpklimam qtlipideak acealealde llesevpvit
      241 pylsevltfc levarnvalg nairirilcc ltflvkvksk allknrllpp llhtlfpiva
      301 aepppgqldp edqdseeeel eielmgetpk hfavqvvdml alhlppeklc pqlmpmleea
      361 lrsespyqrk agllvlavls dgagdhirqr llppllqivc kgledpsqvv rnaalfalgq
      421 fsenlqphis sysrevmpll laylksvplg hthhlakacy alenfvenlg pkvqpylpel
      481 mecmlqllrn pssprakela vsalgaiata aqasllpyfp aimehlrefl ltgredlqpv
      541 qiqsletlgv laravgepmr plaeeccqlg lglcdqvddp dlrrctyslf aalsglmgeg
      601 laphleqitt lmllslrste givpqydgss sfllfddesd geeeeelmde dveeeddsei
      661 sgysvenaff dekedtcaav geisvntsva flpymesvfe evfkllecph lnvrkaahea
      721 lgqfccalhk acqscpsepn taalqaalar vvpsymqavn rererqvvma vlealtgvlr
      781 scgtltlkpp grlaelcgvl kavlqrktac qdtdeeeeee dddqaeydam llehageaip
      841 alaaaaggds fapffagflp llvcktkqgc tvaeksfavg tlaetiqglg aasaqfvsrl
      901 lpvllstaqe adpevrsnai fgmgvlaehg ghpaqehfpk llgllfplla rerhdrvrdn
      961 icgalarllm asptrkpepq vlaallhalp lkedleewvt igrlfsflyq sspdqvidva
     1021 pellricsli ladnkippdt kaallllltf lakqhtdsfq aalgslpvdk aqelqavlgl
     1081 s
//
LOCUS       NP_001351421             186 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity mitogen-activated protein kinase kinase 5 isoform
            2 [Mus musculus].
ACCESSION   NP_001351421
VERSION     NP_001351421.1
DBSOURCE    REFSEQ: accession NM_001364492.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Tsitsikov,E.N., Phan,K.P., Liu,Y., Tsytsykova,A.V., Kinter,M.,
            Selland,L., Garman,L., Griffin,C. and Dunn,I.F.
  TITLE     TRAF7 is an essential regulator of blood vessel integrity during
            mouse embryonic and neonatal development
  JOURNAL   iScience 26 (8), 107474 (2023)
   PUBMED   37583551
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Huang,Y., Wang,P., Morales,R., Luo,Q. and Ma,J.
  TITLE     Map2k5-Deficient Mice Manifest Phenotypes and Pathological Changes
            of Dopamine Deficiency in the Central Nervous System
  JOURNAL   Front Aging Neurosci 13, 651638 (2021)
   PUBMED   34168549
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Luiz,J.P.M., Toller-Kawahisa,J.E., Viacava,P.R., Nascimento,D.C.,
            Pereira,P.T., Saraiva,A.L., Prado,D.S., LeBert,M., Giurisato,E.,
            Tournier,C., Cunha,T.M., Cunha,F.Q., Quesniaux,V., Ryffel,B. and
            Alves-Filho,J.C.
  TITLE     MEK5/ERK5 signaling mediates IL-4-induced M2 macrophage
            differentiation through regulation of c-Myc expression
  JOURNAL   J Leukoc Biol 108 (4), 1215-1223 (2020)
   PUBMED   32745297
  REMARK    GeneRIF: MEK5/ERK5 signaling mediates IL-4-induced M2 macrophage
            differentiation through regulation of c-Myc expression.
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Sanchez-Fdez,A., Ortiz-Ruiz,M.J., Re-Louhau,M.F., Ramos,I.,
            Blanco-Munez,O., Ludena,D., Abad,M., Sanchez-Martin,M.,
            Pandiella,A. and Esparis-Ogando,A.
  TITLE     MEK5 promotes lung adenocarcinoma
  JOURNAL   Eur Respir J 53 (2), 1801327 (2019)
   PUBMED   30442718
  REMARK    GeneRIF: MEK5 promotes lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Nakamura,K. and Johnson,G.L.
  TITLE     PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain
            for activation of the ERK5 pathway
  JOURNAL   J Biol Chem 278 (39), 36989-36992 (2003)
   PUBMED   12912994
  REMARK    GeneRIF: PB1 domain mediates the association of MEKK2 and MEKK3
            with MEK5 and that the respective PB1 domains of these kinases are
            critical for regulation of the ERK5 pathway.
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Lamark,T., Perander,M., Outzen,H., Kristiansen,K., Overvatn,A.,
            Michaelsen,E., Bjorkoy,G. and Johansen,T.
  TITLE     Interaction codes within the family of mammalian Phox and Bem1p
            domain-containing proteins
  JOURNAL   J Biol Chem 278 (36), 34568-34581 (2003)
   PUBMED   12813044
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Nicol,R.L., Frey,N., Pearson,G., Cobb,M., Richardson,J. and
            Olson,E.N.
  TITLE     Activated MEK5 induces serial assembly of sarcomeres and eccentric
            cardiac hypertrophy
  JOURNAL   EMBO J 20 (11), 2757-2767 (2001)
   PUBMED   11387209
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Kamakura,S., Moriguchi,T. and Nishida,E.
  TITLE     Activation of the protein kinase ERK5/BMK1 by receptor tyrosine
            kinases. Identification and characterization of a signaling pathway
            to the nucleus
  JOURNAL   J Biol Chem 274 (37), 26563-26571 (1999)
   PUBMED   10473620
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC124753.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013697.1, SRR13422601.2267923.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 33.96 cM"
     Protein         1..186
                     /product="dual specificity mitogen-activated protein
                     kinase kinase 5 isoform 2"
                     /EC_number="2.7.12.2"
                     /note="dual specificity mitogen-activated protein kinase
                     kinase 5; MAP kinase kinase 5; MAPK/ERK kinase 5"
                     /calculated_mol_wt=20606
     Region          17..107
                     /region_name="PB1_Map2k5"
                     /note="PB1 domain is essential part of the
                     mitogen-activated protein kinase kinase 5 (Map2k5, alias
                     MEK5) one of the key member of the signaling kinases
                     cascade which involved in angiogenesis and early
                     cardiovascular development. The PB1 domain of Map2k5...;
                     cd06395"
                     /db_xref="CDD:99717"
     Region          18..25
                     /region_name="Interaction with MAPK7.
                     /evidence=ECO:0000269|PubMed:16507987"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVS7.1)"
     Site            order(64,66,68,77)
                     /site_type="other"
                     /note="PB1 interaction surface [polypeptide binding]"
                     /db_xref="CDD:99717"
     Region          64..68
                     /region_name="Interaction with MAP3K2/MAP3K3.
                     /evidence=ECO:0000269|PubMed:12813044,
                     ECO:0000269|PubMed:16507987"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVS7.1)"
     Region          116..144
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVS7.1)"
     Region          117..131
                     /region_name="Interaction with MAPK7.
                     /evidence=ECO:0000269|PubMed:16507987"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVS7.1)"
     Region          164..>186
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..186
                     /gene="Map2k5"
                     /gene_synonym="Mapkk5; MEK5; Prkmk5"
                     /coded_by="NM_001364492.1:646..1206"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:23938"
                     /db_xref="MGI:MGI:1346345"
ORIGIN      
        1 mlwlalgpfc amenqvlvir ikipnsgavd wtvhsgpqll frdvldvigq vlpeatttaf
       61 eyededgdri tvrsdeemka mlsyyystvm eqqvngqlie plqifprack ppgernihgl
      121 kvntragpsq htspvvsdsl psnslkkssa elrkilangq mneqdiryrd tlghgnggtv
      181 ykllhi
//
LOCUS       NP_006433                205 aa            linear   PRI 27-APR-2025
DEFINITION  dr1-associated corepressor [Homo sapiens].
ACCESSION   NP_006433
VERSION     NP_006433.2
DBSOURCE    REFSEQ: accession NM_006442.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Castano,E., Gross,P., Wang,Z., Roeder,R.G. and Oelgeschlager,T.
  TITLE     The C-terminal domain-phosphorylated IIO form of RNA polymerase II
            is associated with the transcription repressor NC2 (Dr1/DRAP1) and
            is required for transcription activation in human nuclear extracts
  JOURNAL   Proc Natl Acad Sci U S A 97 (13), 7184-7189 (2000)
   PUBMED   10852970
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Ikeda,K., Halle,J.P., Stelzer,G., Meisterernst,M. and Kawakami,K.
  TITLE     Involvement of negative cofactor NC2 in active repression by zinc
            finger-homeodomain transcription factor AREB6
  JOURNAL   Mol Cell Biol 18 (1), 10-18 (1998)
   PUBMED   9418848
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Yeung,K., Kim,S. and Reinberg,D.
  TITLE     Functional dissection of a human Dr1-DRAP1 repressor complex
  JOURNAL   Mol Cell Biol 17 (1), 36-45 (1997)
   PUBMED   8972183
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Goppelt,A., Stelzer,G., Lottspeich,F. and Meisterernst,M.
  TITLE     A mechanism for repression of class II gene transcription through
            specific binding of NC2 to TBP-promoter complexes via heterodimeric
            histone fold domains
  JOURNAL   EMBO J 15 (12), 3105-3116 (1996)
   PUBMED   8670811
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Mermelstein,F., Yeung,K., Cao,J., Inostroza,J.A.,
            Erdjument-Bromage,H., Eagelson,K., Landsman,D., Levitt,P.,
            Tempst,P. and Reinberg,D.
  TITLE     Requirement of a corepressor for Dr1-mediated repression of
            transcription
  JOURNAL   Genes Dev 10 (8), 1033-1048 (1996)
   PUBMED   8608938
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG036132.1, BC010025.2 and
            BQ773919.1.
            
            On Jan 30, 2002 this sequence version replaced NP_006433.1.
            
            Summary: Transcriptional repression is a general mechanism for
            regulating transcriptional initiation in organisms ranging from
            yeast to humans.  Accurate initiation of transcription from
            eukaryotic protein-encoding genes requires the assembly of a large
            multiprotein complex consisting of RNA polymerase II and general
            transcription factors such as TFIIA, TFIIB, and TFIID. DR1 is a
            repressor that interacts with the TATA-binding protein (TBP) of
            TFIID and prevents the formation of an active transcription complex
            by precluding the entry of TFIIA and/or TFIIB into the
            preinitiation complex. The protein encoded by this gene is a
            corepressor of transcription that interacts with DR1 to enhance
            DR1-mediated repression. The interaction between this corepressor
            and DR1 is required for corepressor function and appears to
            stabilize the TBP-DR1-DNA complex. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.428529.1,
                                           SRR1163658.289450.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312515.7/ ENSP00000307850.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..205
                     /product="dr1-associated corepressor"
                     /note="negative cofactor 2 alpha; negative co-factor
                     2-alpha"
                     /calculated_mol_wt=22219
     Region          9..83
                     /region_name="HFD_DRAP1"
                     /note="histone-fold domain found in Dr1-associated protein
                     1 (DRAP1) and similar proteins; cd22906"
                     /db_xref="CDD:467031"
     Site            order(10,12..13,16,19..21,23..24,26..27,29..31,34,36..37,
                     40..42,44..47,50..51,54,64..67,70..71,74)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467031"
     Site            order(15,18..19,29)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:467031"
     Site            order(22,24,26..29)
                     /site_type="other"
                     /note="TBP binding site [polypeptide binding]"
                     /db_xref="CDD:467031"
     Region          91..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14919.3)"
     CDS             1..205
                     /gene="DRAP1"
                     /gene_synonym="NC2-alpha"
                     /coded_by="NM_006442.4:77..694"
                     /db_xref="CCDS:CCDS8123.1"
                     /db_xref="GeneID:10589"
                     /db_xref="HGNC:HGNC:3019"
                     /db_xref="MIM:602289"
ORIGIN      
        1 mpskkkkyna rfpparikki mqtdeeigkv aaavpviisr alelflesll kkacqvtqsr
       61 naktmttshl kqcieleqqf dflkdlvasv pdmqgdgedn hmdgdkgarr grkpgsggrk
      121 nggmgtkskd kklsgtdseq edesedtdtd geeetsqppp qashpsahfq spptpflpfa
      181 stlplppapp gpsapdeede edyds
//
LOCUS       NP_057332               1901 aa            linear   PRI 27-APR-2025
DEFINITION  A-kinase anchor protein 11 [Homo sapiens].
ACCESSION   NP_057332
VERSION     NP_057332.1
DBSOURCE    REFSEQ: accession NM_016248.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1901)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1901)
  AUTHORS   Palmer,D.S., Howrigan,D.P., Chapman,S.B., Adolfsson,R., Bass,N.,
            Blackwood,D., Boks,M.P.M., Chen,C.Y., Churchhouse,C., Corvin,A.P.,
            Craddock,N., Curtis,D., Di Florio,A., Dickerson,F., Freimer,N.B.,
            Goes,F.S., Jia,X., Jones,I., Jones,L., Jonsson,L., Kahn,R.S.,
            Landen,M., Locke,A.E., McIntosh,A.M., McQuillin,A., Morris,D.W.,
            O'Donovan,M.C., Ophoff,R.A., Owen,M.J., Pedersen,N.L., Posthuma,D.,
            Reif,A., Risch,N., Schaefer,C., Scott,L., Singh,T., Smoller,J.W.,
            Solomonson,M., Clair,D.S., Stahl,E.A., Vreeker,A., Walters,J.T.R.,
            Wang,W., Watts,N.A., Yolken,R., Zandi,P.P. and Neale,B.M.
  TITLE     Exome sequencing in bipolar disorder identifies AKAP11 as a risk
            gene shared with schizophrenia
  JOURNAL   Nat Genet 54 (5), 541-547 (2022)
   PUBMED   35410376
  REMARK    GeneRIF: Exome sequencing in bipolar disorder identifies AKAP11 as
            a risk gene shared with schizophrenia.
REFERENCE   3  (residues 1 to 1901)
  AUTHORS   Deng,Z., Li,X., Blanca Ramirez,M., Purtell,K., Choi,I., Lu,J.H.,
            Yu,Q. and Yue,Z.
  TITLE     Selective autophagy of AKAP11 activates cAMP/PKA to fuel
            mitochondrial metabolism and tumor cell growth
  JOURNAL   Proc Natl Acad Sci U S A 118 (14) (2021)
   PUBMED   33785595
  REMARK    GeneRIF: Selective autophagy of AKAP11 activates cAMP/PKA to fuel
            mitochondrial metabolism and tumor cell growth.
REFERENCE   4  (residues 1 to 1901)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 1901)
  AUTHORS   Correa-Rodriguez,M., Schmidt Rio-Valle,J. and Rueda-Medina,B.
  TITLE     AKAP11 gene polymorphism is associated with bone mass measured by
            quantitative ultrasound in young adults
  JOURNAL   Int J Med Sci 15 (10), 999-1004 (2018)
   PUBMED   30013441
  REMARK    GeneRIF: AKAP11 gene (rs9533090) influences QUS trait in a
            population of Caucasian young adults. The rs9533090 SNP may be
            considered a factor affecting peak bone mass acquisition.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1901)
  AUTHORS   Schillace,R.V., Voltz,J.W., Sim,A.T., Shenolikar,S. and Scott,J.D.
  TITLE     Multiple interactions within the AKAP220 signaling complex
            contribute to protein phosphatase 1 regulation
  JOURNAL   J Biol Chem 276 (15), 12128-12134 (2001)
   PUBMED   11152471
REFERENCE   7  (residues 1 to 1901)
  AUTHORS   Reinton,N., Collas,P., Haugen,T.B., Skalhegg,B.S., Hansson,V.,
            Jahnsen,T. and Tasken,K.
  TITLE     Localization of a novel human A-kinase-anchoring protein, hAKAP220,
            during spermatogenesis
  JOURNAL   Dev Biol 223 (1), 194-204 (2000)
   PUBMED   10864471
REFERENCE   8  (residues 1 to 1901)
  AUTHORS   Schillace,R.V. and Scott,J.D.
  TITLE     Association of the type 1 protein phosphatase PP1 with the A-kinase
            anchoring protein AKAP220
  JOURNAL   Curr Biol 9 (6), 321-324 (1999)
   PUBMED   10209101
REFERENCE   9  (residues 1 to 1901)
  AUTHORS   Lester,L.B. and Scott,J.D.
  TITLE     Anchoring and scaffold proteins for kinases and phosphatases
  JOURNAL   Recent Prog Horm Res 52, 409-29 (1997)
   PUBMED   9238861
  REMARK    Review article
REFERENCE   10 (residues 1 to 1901)
  AUTHORS   Lester,L.B., Coghlan,V.M., Nauert,B. and Scott,J.D.
  TITLE     Cloning and characterization of a novel A-kinase anchoring protein.
            AKAP 220, association with testicular peroxisomes
  JOURNAL   J Biol Chem 271 (16), 9460-9465 (1996)
   PUBMED   8621616
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136527.9, AF176555.1,
            DA780016.1, BE694434.1 and BE670178.1.
            
            Summary: The A-kinase anchor proteins (AKAPs) are a group of
            structurally diverse proteins, which have the common function of
            binding to the regulatory subunit of protein kinase A (PKA) and
            confining the holoenzyme to discrete locations within the cell.
            This gene encodes a member of the AKAP family. The encoded protein
            is expressed at high levels throughout spermatogenesis and in
            mature sperm. It binds the RI and RII subunits of PKA in testis. It
            may serve a function in cell cycle control of both somatic cells
            and germ cells in addition to its putative role in spermatogenesis
            and sperm function. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF176555.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000025301.4/ ENSP00000025301.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1901
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.11"
     Protein         1..1901
                     /product="A-kinase anchor protein 11"
                     /note="A-kinase anchoring protein, 220kDa; A kinase (PRKA)
                     anchor protein 11; protein kinase A anchoring protein 11;
                     a kinase anchor protein 220 kDa; A-kinase anchor protein
                     220 kDa; protein phosphatase 1, regulatory subunit 44"
                     /calculated_mol_wt=210382
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Region          407..443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Region          843..864
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Region          971..993
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Region          1131..1153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            1171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            1176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62924; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62924; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            1242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            1337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            1485
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Site            1580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Region          1650..1663
                     /region_name="PKA-RII subunit binding domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Region          1708..1805
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA4.1)"
     Region          <1804..1900
                     /region_name="AKAP_110"
                     /note="A-kinase anchor protein 110 kDa (AKAP 110);
                     cl14906"
                     /db_xref="CDD:449376"
     CDS             1..1901
                     /gene="AKAP11"
                     /gene_synonym="AKAP-11; AKAP220; PPP1R44; PRKA11"
                     /coded_by="NM_016248.4:177..5882"
                     /db_xref="CCDS:CCDS9383.1"
                     /db_xref="GeneID:11215"
                     /db_xref="HGNC:HGNC:369"
                     /db_xref="MIM:604696"
ORIGIN      
        1 matfrnnhmk tkasvrksfs edvfqsvksl lqsqkelcsv taedclqqde hanltevtfl
       61 gfneetdaah iqdlaavsle lpdilnslhf cslneneiic mkninkpldi ssdplnqshp
      121 sgmlcvmrvs ptsprlridf ifsllskyat girytldtfl hqkhqlettd eddddtnqsv
      181 ssieddfvta fehleeeets kpyndgmnit vlrsqcdaas qtvtghhlet hdlkilissg
      241 qqkslakpst ssvnvlghke lpsvktsvtt sisepwtqrs fyrssnasdk dsdlqktffs
      301 sspayssese csspspvifl deegyqkslk aklelpkipv mkddiedsds evseffdsfd
      361 qfdeleqtle tclfnkdpvi gkssqrkghk hgkscmnpqk fkfdrpalpa nvrkptprkp
      421 espygnlcda pdsprpvkas redsglfspi rssafsplgg ctpaecfcqt diggdrihen
      481 hdsvyytyed yaksiscevl gsvlrthhtn tlsninsikh genktvtfkh gnldqknksk
      541 nkslmikdsi qkfaadlvek sfgsafkdlq kgvssctnal yhlaikltss vlqmafdelr
      601 rqrafslker aisglanflv sealsnalkd lqyvkkqift ntvarfaadl aeelvfegim
      661 evcqfsypqt paspqcgsfd fedkvvklya kdlsesviqe afielsqvdv tfttkaavsv
      721 stdnikyvsa esvvpstqav tfspsfhnqa imvtkpvqey kkeytvqqal fctsgivtsi
      781 pvplagsall pyhisstacq akahlssdds nsngdsaqvh iatknreeka aclrniclps
      841 ehnpgnqndf kptnddiemq sssklpndpa iisnfsaavv htivnetles mtslevtkmv
      901 dertdyltks lkektppfsh cdqavlqcse assnkdmfad rlsksiikhs idksksvipn
      961 idknavykes lpvsgeesql tpekspkfpd sqnqlthcsl saakdcvpec kvsmvhgssl
     1021 etlpscpavt gqksdlkesa kdqplkkhnl nstslealsf gqenpfphsh tfsstaltcv
     1081 dglhvedkqk vrdrnvipdt ppstplvpsr assewdikkl tkklkgelak efapatppst
     1141 phnssvgsls eneqntieke efmlklmrsl seevessesg elpevdvkse hsgkkvqfae
     1201 alathilsla temaashldn kiiqepkvkn pclnvqsqrs vsptflnpsd enlktlcnfa
     1261 gdlaaevite aekiakvrnc mlfkqkknsc yadgdedykv eekldieavv hprevdpfil
     1321 slppsscmsg lmykypsces vtdeyaghli qilkqeggns elimdqyanr layrsvksgl
     1381 qeaakttkvq cnsrmfpvps sqvktnkell mfsnkehhqe adkkrqskrn egyfcknqtc
     1441 ertldpyrne vsqlysfsts lvhsitkdak eeltaslvgl pksltdsclf eksgyeedne
     1501 chvtpelpks lqpssqnhrf yhstgslngy gcgdnvvqav eqyakkvvdd tleltlgstv
     1561 frvsettksa drvtyaekls pltgqacryc dlkelhnctg nssqhffrqg slasskpasn
     1621 pkfssryqks rifhlsvpqi hvnldkkavl aekivaeaie kaerelssts laadsgigqe
     1681 gasfaeslat etmtaavtnv ghavssskei edfqstesvs sqqmnlsigd dstgswsnls
     1741 fedehqdess sfhhlsesng nssswsslgl egdlyednls fptsdsdgpd dkdeehedev
     1801 eglgqdgktl litnidmepc tvdpqlriil qwliaseaev aelyfhdsan kefmllskql
     1861 qekgwkvgdl lqavlqyyev mekasseerc kslfdwllen a
//
LOCUS       NP_001273465             341 aa            linear   PRI 27-APR-2025
DEFINITION  cell cycle checkpoint control protein RAD9B isoform e [Homo
            sapiens].
ACCESSION   NP_001273465 XP_005253907
VERSION     NP_001273465.1
DBSOURCE    REFSEQ: accession NM_001286536.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Barroso-Chinea,P., Salas-Hernandez,J., Cruz-Muros,I.,
            Lopez-Fernandez,J., Freire,R. and Afonso-Oramas,D.
  TITLE     Expression of RAD9B in the mesostriatal system of rats and humans:
            Overexpression in a 6-OHDA rat model of Parkinson's disease
  JOURNAL   Ann Anat 250, 152135 (2023)
   PUBMED   37460044
  REMARK    GeneRIF: Expression of RAD9B in the mesostriatal system of rats and
            humans: Overexpression in a 6-OHDA rat model of Parkinson's
            disease.
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Cao,X., Tian,T., Steele,J.W., Cabrera,R.M., Aguiar-Pulido,V.,
            Wadhwa,S., Bhavani,N., Bi,P., Gargurevich,N.H., Hoffman,E.N.,
            Cai,C.Q., Marini,N.J., Yang,W., Shaw,G.M., Ross,M.E., Finnell,R.H.
            and Lei,Y.
  TITLE     Loss of RAD9B impairs early neural development and contributes to
            the risk for human spina bifida
  JOURNAL   Hum Mutat 41 (4), 786-799 (2020)
   PUBMED   31898828
  REMARK    GeneRIF: Loss of RAD9B impairs early neural development and
            contributes to the risk for human spina bifida.
            Erratum:[Hum Mutat. 2021 Apr;42(4):487. doi: 10.1002/humu.24175.
            PMID: 33856736]
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Lyndaker,A.M., Vasileva,A., Wolgemuth,D.J., Weiss,R.S. and
            Lieberman,H.B.
  TITLE     Clamping down on mammalian meiosis
  JOURNAL   Cell Cycle 12 (19), 3135-3145 (2013)
   PUBMED   24013428
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Perez-Castro,A.J. and Freire,R.
  TITLE     Rad9B responds to nucleolar stress through ATR and JNK signalling,
            and delays the G1-S transition
  JOURNAL   J Cell Sci 125 (Pt 5), 1152-1164 (2012)
   PUBMED   22399810
  REMARK    GeneRIF: Rad9B responds to nucleolar stress after the activation of
            JNK-dependent stress signalling and ATR-dependent DNA damage
            response pathways, and actively accumulates within nucleoli, where
            it does not cause a transcription block.
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Lieberman,H.B.
  TITLE     Rad9, an evolutionarily conserved gene with multiple functions for
            preserving genomic integrity
  JOURNAL   J Cell Biochem 97 (4), 690-697 (2006)
   PUBMED   16365875
  REMARK    GeneRIF: The encoded mammalian proteins participate in promoting
            resistance to DNA damage, cell cycle checkpoint control, DNA
            repair, and apoptosis.
            Review article
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dufault,V.M., Oestreich,A.J., Vroman,B.T. and Karnitz,L.M.
  TITLE     Identification and characterization of RAD9B, a paralog of the RAD9
            checkpoint gene
  JOURNAL   Genomics 82 (6), 644-651 (2003)
   PUBMED   14611806
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Hopkins,K.M., Wang,X., Berlin,A., Hang,H., Thaker,H.M. and
            Lieberman,H.B.
  TITLE     Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint
            control genes in normal and cancerous testicular tissue
  JOURNAL   Cancer Res 63 (17), 5291-5298 (2003)
   PUBMED   14500360
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Zou,L. and Elledge,S.J.
  TITLE     Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
  JOURNAL   Science 300 (5625), 1542-1548 (2003)
   PUBMED   12791985
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002350.1.
            
            On Nov 8, 2013 this sequence version replaced XP_005253907.1.
            
            Transcript Variant: This variant (7) lacks three alternate exons,
            which results in a frameshift, compared to variant 1. The encoded
            isoform (e) has a distinct C-terminus and is shorter than isoform
            a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302512.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..341
                     /product="cell cycle checkpoint control protein RAD9B
                     isoform e"
                     /EC_number="3.1.11.2"
                     /note="DNA repair exonuclease rad9 homolog B; cell cycle
                     checkpoint control protein RAD9B; RAD9 homolog B"
                     /calculated_mol_wt=37932
     Region          17..207
                     /region_name="Rad9"
                     /note="pfam04139"
                     /db_xref="CDD:427739"
     CDS             1..341
                     /gene="RAD9B"
                     /coded_by="NM_001286536.2:8..1033"
                     /note="isoform e is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS66469.1"
                     /db_xref="GeneID:144715"
                     /db_xref="HGNC:HGNC:21700"
                     /db_xref="MIM:608368"
ORIGIN      
        1 maamlkcvms gsqvkvfgka vqalsrisde fwldpskkgl alrcvnssrs aygcvlfspv
       61 ffqhyqwsal vkmseneldt tlhlkcklgm ksilpifrcl nslerniekc riftrsdkck
      121 vviqffyrhd lsnavhsemf vgsdefdffq igmdteitfc fkelkgiltf seathapisi
      181 yfdfpgkpla lsiddmlvea nfilatlade qsrasspqsl clsqkrkrsd liekkagknv
      241 tgqalecisk kaaprrlypk etltnisale ncgspamkrv dgdvsevses svsnteevpg
      301 slclrkcaag knlmevmpni svlsdieqyp plprqpefgv e
//
LOCUS       NP_001013642             473 aa            linear   PRI 27-APR-2025
DEFINITION  dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol
            alpha-1,2-glucosyltransferase isoform 1 [Homo sapiens].
ACCESSION   NP_001013642 XP_047770
VERSION     NP_001013642.2
DBSOURCE    REFSEQ: accession NM_001013620.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Zhou,W., Ye,D., Tester,D.J., Bains,S., Giudicessi,J.R.,
            Haglund-Turnquist,C.M., Orland,K.M., January,C.T., Eckhardt,L.L.,
            Maginot,K.R. and Ackerman,M.J.
  TITLE     Elucidation of ALG10B as a Novel Long-QT Syndrome-Susceptibility
            Gene
  JOURNAL   Circ Genom Precis Med 16 (2), e003726 (2023)
   PUBMED   37071726
  REMARK    GeneRIF: Elucidation of ALG10B as a Novel Long-QT
            Syndrome-Susceptibility Gene.
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Probst,F.J., Corrigan,R.R., Del Gaudio,D., Salinger,A.P.,
            Lorenzo,I., Gao,S.S., Chiu,I., Xia,A., Oghalai,J.S. and
            Justice,M.J.
  TITLE     A point mutation in the gene for asparagine-linked glycosylation
            10B (Alg10b) causes nonsyndromic hearing impairment in mice (Mus
            musculus)
  JOURNAL   PLoS One 8 (11), e80408 (2013)
   PUBMED   24303013
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Hayashi,K., Fujino,N., Ino,H., Uchiyama,K., Sakata,K., Konno,T.,
            Masuta,E., Funada,A., Sakamoto,Y., Tsubokawa,T., Hodatsu,A.,
            Yasuda,T., Kanaya,H., Kim,M.Y., Kupershmidt,S., Higashida,H. and
            Yamagishi,M.
  TITLE     A KCR1 variant implicated in susceptibility to the long QT syndrome
  JOURNAL   J Mol Cell Cardiol 50 (1), 50-57 (2011)
   PUBMED   20950623
  REMARK    GeneRIF: Findings suggest that KCR1 genetic variations that
            diminish the ability of KCR1 to protect KCNH2 from inhibition by
            commonly used therapeutic agents constitute a risk factor for the
            aLQTS.
REFERENCE   5  (residues 1 to 473)
  AUTHORS   Daly,A.K., Donaldson,P.T., Bhatnagar,P., Shen,Y., Pe'er,I.,
            Floratos,A., Daly,M.J., Goldstein,D.B., John,S., Nelson,M.R.,
            Graham,J., Park,B.K., Dillon,J.F., Bernal,W., Cordell,H.J.,
            Pirmohamed,M., Aithal,G.P. and Day,C.P.
  CONSRTM   DILIGEN Study; International SAE Consortium
  TITLE     HLA-B*5701 genotype is a major determinant of drug-induced liver
            injury due to flucloxacillin
  JOURNAL   Nat Genet 41 (7), 816-819 (2009)
   PUBMED   19483685
REFERENCE   6  (residues 1 to 473)
  AUTHORS   Nakajima,T., Hayashi,K., Viswanathan,P.C., Kim,M.Y., Anghelescu,M.,
            Barksdale,K.A., Shuai,W., Balser,J.R. and Kupershmidt,S.
  TITLE     HERG is protected from pharmacological block by
            alpha-1,2-glucosyltransferase function
  JOURNAL   J Biol Chem 282 (8), 5506-5513 (2007)
   PUBMED   17189275
REFERENCE   7  (residues 1 to 473)
  AUTHORS   Petersen,C.I., McFarland,T.R., Stepanovic,S.Z., Yang,P.,
            Reiner,D.J., Hayashi,K., George,A.L., Roden,D.M., Thomas,J.H. and
            Balser,J.R.
  TITLE     In vivo identification of genes that modify ether-a-go-go-related
            gene activity in Caenorhabditis elegans may also affect human
            cardiac arrhythmia
  JOURNAL   Proc Natl Acad Sci U S A 101 (32), 11773-11778 (2004)
   PUBMED   15280551
REFERENCE   8  (residues 1 to 473)
  AUTHORS   Kupershmidt,S., Yang,I.C., Hayashi,K., Wei,J., Chanthaphaychith,S.,
            Petersen,C.I., Johns,D.C., George,A.L. Jr., Roden,D.M. and
            Balser,J.R.
  TITLE     The IKr drug response is modulated by KCR1 in transfected cardiac
            and noncardiac cell lines
  JOURNAL   FASEB J 17 (15), 2263-2265 (2003)
   PUBMED   14525949
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC117372.2.
            
            On Nov 23, 2018 this sequence version replaced NP_001013642.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.398127.1,
                                           SRR1163657.499250.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308742.9/ ENSP00000310120.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..473
                     /product="dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol
                     alpha-1,2-glucosyltransferase isoform 1"
                     /EC_number="2.4.1.256"
                     /note="modifier of the HERG potassium channel; putative
                     alpha-1,2-glucosyltransferase ALG10-B; asparagine-linked
                     glycosylation 10 homolog B (yeast,
                     alpha-1,2-glucosyltransferase); potassium channel
                     regulator 1; alpha-2-glucosyltransferase ALG10-B;
                     asparagine-linked glycosylation protein 10 homolog B;
                     alpha-1,2-glucosyltransferase ALG10-A; putative
                     Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol
                     alpha-1,2-glucosyltransferase; asparagine-linked
                     glycosylation 10, alpha-1,2-glucosyltransferase homolog B;
                     dolichyl-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-dolichol
                     alpha-1,2- glucosyltransferase; ALG10B,
                     alpha-1,2-glucosyltransferase;
                     dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol
                     alpha-1,2-glucosyltransferase"
                     /calculated_mol_wt=55317
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Region          32..427
                     /region_name="DIE2_ALG10"
                     /note="DIE2/ALG10 family; pfam04922"
                     /db_xref="CDD:461481"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Site            127..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Site            151..171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Site            176..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Site            284..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Site            366..386
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Site            393..413
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     Site            437..457
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I7T1.2)"
     CDS             1..473
                     /gene="ALG10B"
                     /gene_synonym="ALG10; KCR1"
                     /coded_by="NM_001013620.4:121..1542"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31772.1"
                     /db_xref="GeneID:144245"
                     /db_xref="HGNC:HGNC:31088"
                     /db_xref="MIM:603313"
ORIGIN      
        1 maqlegycfs aalsctflvs cllfsafsra lrepymdeif hlpqaqryce ghfslsqwdp
       61 mittlpglyl vsvgvvkpai wifawsehvv csigmlrfvn llfsvgnfyl lyllfhkvqp
      121 rnkaassiqr vlstltlavf ptlyffnfly yteagsmfft lfaylmclyg nhktsaflgf
      181 cgfmfrqtni iwavfcagnv iaqklteawk telqkkedrl ppikgpfaef rkilqfllay
      241 smsfknlsml fcltwpyill gflfcafvvv nggivigdrs sheaclhfpq lfyffsftlf
      301 fsfphllsps kiktflslvw khgilflvvt lvsvflvwkf tyahkyllad nrhytfyvwk
      361 rvfqryailk yllvpayifa gwsiadslks kpifwnlmff iclfivivpq kllefryfil
      421 pyviyrlnit lpptsrlvce lscyaivnfi tfyiflnktf qwpnsqdiqr fmw
//
LOCUS       NP_113655                959 aa            linear   PRI 27-APR-2025
DEFINITION  anion exchange protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_113655
VERSION     NP_113655.2
DBSOURCE    REFSEQ: accession NM_031467.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Pena-Munzenmayer,G., George,A.T., Shull,G.E., Melvin,J.E. and
            Catalan,M.A.
  TITLE     Ae4 (Slc4a9) is an electroneutral monovalent cation-dependent
            Cl-/HCO3- exchanger
  JOURNAL   J Gen Physiol 147 (5), 423-436 (2016)
   PUBMED   27114614
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Parker,M.D., Ourmozdi,E.P. and Tanner,M.J.
  TITLE     Human BTR1, a new bicarbonate transporter superfamily member and
            human AE4 from kidney
  JOURNAL   Biochem Biophys Res Commun 282 (5), 1103-1109 (2001)
   PUBMED   11302728
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Lipovich,L., Lynch,E.D., Lee,M.K. and King,M.C.
  TITLE     A novel sodium bicarbonate cotransporter-like gene in an ancient
            duplicated region: SLC4A9 at 5q31
  JOURNAL   Genome Biol 2 (4), RESEARCH0011 (2001)
   PUBMED   11305939
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008438.6, AF332961.1,
            AB032762.1 and CB046220.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 5, 2007 this sequence version replaced NP_113655.1.
            
            Summary: The protein encoded by this gene is a membrane protein
            involved in anion exchange. Expression of this gene is mostly
            limited to the kidney. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, May 2012].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction at the 5' end of an exon compared to variant 1. The
            resulting isoform (2) lacks an alternate internal segment compared
            to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB032762.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159080 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000506757.7/ ENSP00000424424.1
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..959
                     /product="anion exchange protein 4 isoform 2"
                     /note="anion exchange protein 4; anion exchanger 4; sodium
                     bicarbonate cotransporter 5; solute carrier family 4,
                     sodium bicarbonate cotransporter, member 9"
                     /calculated_mol_wt=105571
     Region          57..914
                     /region_name="Band_3_cyto"
                     /note="Band 3 cytoplasmic domain; cl26877"
                     /db_xref="CDD:452680"
     CDS             1..959
                     /gene="SLC4A9"
                     /gene_synonym="AE4"
                     /coded_by="NM_031467.3:44..2923"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47278.1"
                     /db_xref="GeneID:83697"
                     /db_xref="HGNC:HGNC:11035"
                     /db_xref="MIM:610207"
ORIGIN      
        1 memklpgqeg feassaprni psgeldsnpd pgtgpspdgp sdteskelgv pkdpllfiql
       61 nellgwpqal ewretgrwvl feeklevaag rwsaphvptl alpslqklrs llaeglvlld
      121 cpaqsllelv eqvtrvesls pelrgqlqal llqrpqhynq ttgtrpcwgs thprkasdne
      181 eaplreqcqn plrqklppga eagtvlagel gflaqplgaf vrlrnpvvlg sltevslpsr
      241 ffclllgpcm lgkgyhemgr aaavllsdpq fqwsvrrasn lhdllaalda fleevtvlpp
      301 grwdptarip ppkclpsqhk rlpsqqreir gpavprltsa edrhrhgpha hspelqrtgr
      361 lfggliqdvr rkvpwypsdf ldalhlqcfs avlyiylatv tnaitfggll gdatdgaqgv
      421 lesflgtava gaafclmagq pltilsstgp vlvferllfs fsrdysldyl pfrlwvgiwv
      481 atfclvlvat easvlvryft rfteegfcal islifiydav gkmlnlthty piqkpgssay
      541 gclcqypgpg gnesqwirtr pkdrddivsm dlglinasll pppectrqgg hprgpgchtv
      601 pdiaffslll fltsfffama lkcvktsrff psvvrkglsd fssvlaillg cgldaflgla
      661 tpklmvpref kptlpgrgwl vspfganpww wsvaaalpal llsilifmdq qitavilnrm
      721 eyrlqkgagf hldlfcvavl mlltsalglp wyvsatvisl ahmdslrres racapgerpn
      781 flgireqrlt glvvfiltga siflapvlkf ipmpvlygif lymgvaalss iqftnrvkll
      841 lmpakhqpdl lllrhvpltr vhlftaiqla clgllwiiks tpaaiifplm llglvgvrka
      901 lervfspqel lwldelmpee ersipekgle pehsfsgsds edselmyqpk apeinisvn
//
LOCUS       NP_780577                503 aa            linear   ROD 27-APR-2025
DEFINITION  uncharacterized protein SPEM2 [Mus musculus].
ACCESSION   NP_780577
VERSION     NP_780577.1
DBSOURCE    REFSEQ: accession NM_175368.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Li,C., Shen,C., Xiong,W., Ge,H., Shen,Y., Chi,J., Zhang,H.,
            Tang,L., Lu,S., Wang,J., Fei,J. and Wang,Z.
  TITLE     Spem2, a novel testis-enriched gene, is required for spermiogenesis
            and fertilization in mice
  JOURNAL   Cell Mol Life Sci 81 (1), 108 (2024)
   PUBMED   38421455
  REMARK    GeneRIF: Spem2, a novel testis-enriched gene, is required for
            spermiogenesis and fertilization in mice.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL603707.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK077090.1, BC137961.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 42.89 cM"
     Protein         1..503
                     /product="uncharacterized protein SPEM2"
                     /note="uncharacterized protein C17orf74 homolog"
                     /calculated_mol_wt=56803
     Region          1..261
                     /region_name="Spem1"
                     /note="Spermatid maturation protein 1; pfam15670"
                     /db_xref="CDD:464793"
     Site            26..46
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8C5U4.1)"
     Region          155..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8C5U4.1)"
     Region          311..381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8C5U4.1)"
     Region          436..456
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8C5U4.1)"
     Region          472..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8C5U4.1)"
     CDS             1..503
                     /gene="Spem2"
                     /gene_synonym="4933402P03Rik"
                     /coded_by="NM_175368.2:67..1578"
                     /db_xref="CCDS:CCDS24912.1"
                     /db_xref="GeneID:108803"
                     /db_xref="MGI:MGI:1918293"
ORIGIN      
        1 menqlwqntl rcceqyqesp qdaenilfll lgliilvnis invatamwqg lqnaidkmif
       61 wmnqktevvq vtecppkepq panvqdvhih cildpvqvkm aqptqcssss shyfckrsnd
      121 rrsrrrygyq qgnlqihqss qqqgclshqq rlrnrplsrg yppfrkqpqg hkmsqmrpmp
      181 ffdmedrdsl peghscphak qprrgwgslc kpvrlasnvg lwgrqggila slplpslyls
      241 pelrrlpkrv eakselrlqg fgphysqsri wgtveaeqwa sspppprrll pnpswvtvgy
      301 ssfpsgghip ydardqwrrg tegcepppaf vprnprevqg yrdhnsqahr qnfsshthsq
      361 pnhsppqsmg hvgyssresh evrrrapdwi evfpsrhplt tstsltalge asyqrappas
      421 sglmiphssq rlaevqisdp tpppttfvpl srnpggnaty qvydslelkr qvqenrgras
      481 slpppstsas rpslhrsrtg kln
//
LOCUS       NP_775858                523 aa            linear   PRI 27-APR-2025
DEFINITION  REST corepressor 2 isoform 1 [Homo sapiens].
ACCESSION   NP_775858
VERSION     NP_775858.2
DBSOURCE    REFSEQ: accession NM_173587.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Rivera,C., Verbel-Vergara,D., Arancibia,D., Lappala,A.,
            Gonzalez,M., Guzman,F., Merello,G., Lee,J.T. and Andres,M.E.
  TITLE     Revealing RCOR2 as a regulatory component of nuclear speckles
  JOURNAL   Epigenetics Chromatin 14 (1), 51 (2021)
   PUBMED   34819154
  REMARK    GeneRIF: Revealing RCOR2 as a regulatory component of nuclear
            speckles.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Hiramatsu,H., Kobayashi,K., Kobayashi,K., Haraguchi,T., Ino,Y.,
            Todo,T. and Iba,H.
  TITLE     The role of the SWI/SNF chromatin remodeling complex in maintaining
            the stemness of glioma initiating cells
  JOURNAL   Sci Rep 7 (1), 889 (2017)
   PUBMED   28420882
  REMARK    Erratum:[Sci Rep. 2018 Oct 25;8(1):16079. doi:
            10.1038/s41598-018-31444-z. PMID: 30356171]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Monaghan,C.E., Nechiporuk,T., Jeng,S., McWeeney,S.K., Wang,J.,
            Rosenfeld,M.G. and Mandel,G.
  TITLE     REST corepressors RCOR1 and RCOR2 and the repressor INSM1 regulate
            the proliferation-differentiation balance in the developing brain
  JOURNAL   Proc Natl Acad Sci U S A 114 (3), E406-E415 (2017)
   PUBMED   28049845
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Suva,M.L., Rheinbay,E., Gillespie,S.M., Patel,A.P., Wakimoto,H.,
            Rabkin,S.D., Riggi,N., Chi,A.S., Cahill,D.P., Nahed,B.V.,
            Curry,W.T., Martuza,R.L., Rivera,M.N., Rossetti,N., Kasif,S.,
            Beik,S., Kadri,S., Tirosh,I., Wortman,I., Shalek,A.K.,
            Rozenblatt-Rosen,O., Regev,A., Louis,D.N. and Bernstein,B.E.
  TITLE     Reconstructing and reprogramming the tumor-propagating potential of
            glioblastoma stem-like cells
  JOURNAL   Cell 157 (3), 580-594 (2014)
   PUBMED   24726434
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Yang,P., Wang,Y., Chen,J., Li,H., Kang,L., Zhang,Y., Chen,S.,
            Zhu,B. and Gao,S.
  TITLE     RCOR2 is a subunit of the LSD1 complex that regulates ESC property
            and substitutes for SOX2 in reprogramming somatic cells to
            pluripotency
  JOURNAL   Stem Cells 29 (5), 791-801 (2011)
   PUBMED   21433225
  REMARK    GeneRIF: Ectopic expression of Rcor2 in both mouse and human
            somatic cells effectively substituted the requirement for exogenous
            Sox2 expression in somatic cell reprogramming.
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003780.3 and BC023587.2.
            
            On Nov 24, 2009 this sequence version replaced NP_775858.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC023587.2, AB593132.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301459.5/ ENSP00000301459.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..523
                     /product="REST corepressor 2 isoform 1"
                     /calculated_mol_wt=57881
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Region          46..98
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Region          134..178
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cl21498"
                     /db_xref="CDD:473887"
     Site            order(135,164..165,167..168,170..172,174..176)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          185..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5FWT8; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Region          331..374
                     /region_name="Myb_DNA-binding"
                     /note="Myb-like DNA-binding domain; pfam00249"
                     /db_xref="CDD:459731"
     Region          387..523
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Region          <466..520
                     /region_name="Gag_MA"
                     /note="Matrix protein (MA), p15; pfam01140"
                     /db_xref="CDD:426076"
     Site            479
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8C796; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     CDS             1..523
                     /gene="RCOR2"
                     /coded_by="NM_173587.4:709..2280"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8052.1"
                     /db_xref="GeneID:283248"
                     /db_xref="HGNC:HGNC:27455"
                     /db_xref="MIM:616019"
ORIGIN      
        1 mpsvmekpsa gsgilsrsra ktvpnggqph seddsseeeh shdsmirvgt nyqavipeck
       61 pesparysnk elkgmlvwsp nhcvsdakld kyiamakekh gynieqalgm llwhkhdvek
      121 sladlanftp fpdewtvedk vlfeqafgfh gkcfqriqqm lpdklipslv kyyyswkktr
      181 srtsvmdrqa rrlggrkdke dsdeleegrg gvsegepdpa dpkreplpsr plnarpgpgk
      241 kevqvsqyrh hplrtrrrpp kgmylspegl tavsgspdla nltlrgldsq lislkrqvqs
      301 mkqtnsslrq aleggidplr ppeantkfns rwttdeqlla vqairrygkd fgaiaevign
      361 ktltqvktff vsyrrrfnle evlqeweaeq dgapgapvpm eearrgaplp apaleeddev
      421 qitsvstsvp rsvppapppp ppptslsqpp pllrpplpta ptllrqpppl qqgrflqprl
      481 apnqppppli rpalaaprhs arpgpqpppt ligtpleppa psl
//
LOCUS       NP_001354908            1783 aa            linear   PRI 27-APR-2025
DEFINITION  doublecortin domain-containing protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001354908 XP_024304242
VERSION     NP_001354908.1
DBSOURCE    REFSEQ: accession NM_001367979.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1783)
  AUTHORS   Okada,Y., Sim,X., Go,M.J., Wu,J.Y., Gu,D., Takeuchi,F.,
            Takahashi,A., Maeda,S., Tsunoda,T., Chen,P., Lim,S.C., Wong,T.Y.,
            Liu,J., Young,T.L., Aung,T., Seielstad,M., Teo,Y.Y., Kim,Y.J.,
            Lee,J.Y., Han,B.G., Kang,D., Chen,C.H., Tsai,F.J., Chang,L.C.,
            Fann,S.J., Mei,H., Rao,D.C., Hixson,J.E., Chen,S., Katsuya,T.,
            Isono,M., Ogihara,T., Chambers,J.C., Zhang,W., Kooner,J.S.,
            Albrecht,E., Yamamoto,K., Kubo,M., Nakamura,Y., Kamatani,N.,
            Kato,N., He,J., Chen,Y.T., Cho,Y.S., Tai,E.S. and Tanaka,T.
  CONSRTM   KidneyGen Consortium; CKDGen Consortium; GUGC consortium
  TITLE     Meta-analysis identifies multiple loci associated with kidney
            function-related traits in east Asian populations
  JOURNAL   Nat Genet 44 (8), 904-909 (2012)
   PUBMED   22797727
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1783)
  AUTHORS   Estrada,K., Styrkarsdottir,U., Evangelou,E., Hsu,Y.H., Duncan,E.L.,
            Ntzani,E.E., Oei,L., Albagha,O.M., Amin,N., Kemp,J.P., Koller,D.L.,
            Li,G., Liu,C.T., Minster,R.L., Moayyeri,A., Vandenput,L.,
            Willner,D., Xiao,S.M., Yerges-Armstrong,L.M., Zheng,H.F.,
            Alonso,N., Eriksson,J., Kammerer,C.M., Kaptoge,S.K., Leo,P.J.,
            Thorleifsson,G., Wilson,S.G., Wilson,J.F., Aalto,V., Alen,M.,
            Aragaki,A.K., Aspelund,T., Center,J.R., Dailiana,Z., Duggan,D.J.,
            Garcia,M., Garcia-Giralt,N., Giroux,S., Hallmans,G., Hocking,L.J.,
            Husted,L.B., Jameson,K.A., Khusainova,R., Kim,G.S., Kooperberg,C.,
            Koromila,T., Kruk,M., Laaksonen,M., Lacroix,A.Z., Lee,S.H.,
            Leung,P.C., Lewis,J.R., Masi,L., Mencej-Bedrac,S., Nguyen,T.V.,
            Nogues,X., Patel,M.S., Prezelj,J., Rose,L.M., Scollen,S.,
            Siggeirsdottir,K., Smith,A.V., Svensson,O., Trompet,S., Trummer,O.,
            van Schoor,N.M., Woo,J., Zhu,K., Balcells,S., Brandi,M.L.,
            Buckley,B.M., Cheng,S., Christiansen,C., Cooper,C., Dedoussis,G.,
            Ford,I., Frost,M., Goltzman,D., Gonzalez-Macias,J., Kahonen,M.,
            Karlsson,M., Khusnutdinova,E., Koh,J.M., Kollia,P., Langdahl,B.L.,
            Leslie,W.D., Lips,P., Ljunggren,O., Lorenc,R.S., Marc,J.,
            Mellstrom,D., Obermayer-Pietsch,B., Olmos,J.M.,
            Pettersson-Kymmer,U., Reid,D.M., Riancho,J.A., Ridker,P.M.,
            Rousseau,F., Slagboom,P.E., Tang,N.L., Urreizti,R., Van Hul,W.,
            Viikari,J., Zarrabeitia,M.T., Aulchenko,Y.S.,
            Castano-Betancourt,M., Grundberg,E., Herrera,L., Ingvarsson,T.,
            Johannsdottir,H., Kwan,T., Li,R., Luben,R., Medina-Gomez,C.,
            Palsson,S.T., Reppe,S., Rotter,J.I., Sigurdsson,G., van Meurs,J.B.,
            Verlaan,D., Williams,F.M., Wood,A.R., Zhou,Y., Gautvik,K.M.,
            Pastinen,T., Raychaudhuri,S., Cauley,J.A., Chasman,D.I.,
            Clark,G.R., Cummings,S.R., Danoy,P., Dennison,E.M., Eastell,R.,
            Eisman,J.A., Gudnason,V., Hofman,A., Jackson,R.D., Jones,G.,
            Jukema,J.W., Khaw,K.T., Lehtimaki,T., Liu,Y., Lorentzon,M.,
            McCloskey,E., Mitchell,B.D., Nandakumar,K., Nicholson,G.C.,
            Oostra,B.A., Peacock,M., Pols,H.A., Prince,R.L., Raitakari,O.,
            Reid,I.R., Robbins,J., Sambrook,P.N., Sham,P.C., Shuldiner,A.R.,
            Tylavsky,F.A., van Duijn,C.M., Wareham,N.J., Cupples,L.A.,
            Econs,M.J., Evans,D.M., Harris,T.B., Kung,A.W., Psaty,B.M.,
            Reeve,J., Spector,T.D., Streeten,E.A., Zillikens,M.C.,
            Thorsteinsdottir,U., Ohlsson,C., Karasik,D., Richards,J.B.,
            Brown,M.A., Stefansson,K., Uitterlinden,A.G., Ralston,S.H.,
            Ioannidis,J.P., Kiel,D.P. and Rivadeneira,F.
  TITLE     Genome-wide meta-analysis identifies 56 bone mineral density loci
            and reveals 14 loci associated with risk of fracture
  JOURNAL   Nat Genet 44 (5), 491-501 (2012)
   PUBMED   22504420
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1783)
  AUTHORS   Kaplan,A. and Reiner,O.
  TITLE     Linking cytoplasmic dynein and transport of Rab8 vesicles to the
            midbody during cytokinesis by the doublecortin domain-containing 5
            protein
  JOURNAL   J Cell Sci 124 (Pt 23), 3989-4000 (2011)
   PUBMED   22159412
  REMARK    GeneRIF: DCDC5 colocalizes with Rab8 and links it to dynein during
            cytokinesis. DCDC5 knockdown increased apoptosis and the number of
            multinucleated cells.
REFERENCE   4  (residues 1 to 1783)
  AUTHORS   Cheng,F., Song,W., Kang,Y., Yu,S. and Yuan,H.
  TITLE     A 556 kb deletion in the downstream region of the PAX6 gene causes
            familial aniridia and other eye anomalies in a Chinese family
  JOURNAL   Mol Vis 17, 448-455 (2011)
   PUBMED   21321669
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1783)
  AUTHORS   Dijkmans,T.F., van Hooijdonk,L.W., Fitzsimons,C.P. and
            Vreugdenhil,E.
  TITLE     The doublecortin gene family and disorders of neuronal structure
  JOURNAL   Cent Nerv Syst Agents Med Chem 10 (1), 32-46 (2010)
   PUBMED   20236041
  REMARK    Review article
REFERENCE   6  (residues 1 to 1783)
  AUTHORS   Reiner,O., Coquelle,F.M., Peter,B., Levy,T., Kaplan,A., Sapir,T.,
            Orr,I., Barkai,N., Eichele,G. and Bergmann,S.
  TITLE     The evolving doublecortin (DCX) superfamily
  JOURNAL   BMC Genomics 7, 188 (2006)
   PUBMED   16869982
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1783)
  AUTHORS   Zeng,L., Gu,S., Li,Y., Zhao,E., Xu,J., Ye,X., Wu,Q., Wang,L.,
            Xie,Y. and Mao,Y.
  TITLE     Identification of a novel human doublecortin-domain-containing gene
            (DCDC1) expressed mainly in testis
  JOURNAL   J Hum Genet 48 (7), 393-396 (2003)
   PUBMED   12820024
  REMARK    GeneRIF: DCDC1 was mapped to 11p13; mainly expressed in adult
            testis; and its expression in fetal brain was much higher than in
            adult brain
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL137804.7, AL162614.25,
            AL133376.6, AL137160.7 and AL135932.7.
            
            On Jan 4, 2019 this sequence version replaced XP_024304242.1.
            
            Summary: This gene encodes a member of the doublecortin family. The
            protein encoded by this gene is a hydrophilic, intracellular
            protein. It contains a single doublecortin domain and is unable to
            bind microtubules and to regulate microtubule polymerization. This
            gene is mainly expressed in adult testis. It does not have a mouse
            homolog. [provided by RefSeq, Sep 2010].
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1783
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p14.1-p13"
     Protein         1..1783
                     /product="doublecortin domain-containing protein 1 isoform
                     4"
                     /note="doublecortin domain-containing protein 1;
                     doublecortin domain-containing protein 5; doublecortin
                     domain-containing 5 protein"
                     /calculated_mol_wt=200461
     Region          93..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (M0R2J8.1)"
     Region          174..245
                     /region_name="DCX_DCDC1"
                     /note="Doublecortin-like domain found in doublecortin
                     domain-containing protein 1 (DCDC1); cd17155"
                     /db_xref="CDD:340675"
     Region          295..380
                     /region_name="DCX2_DCDC5"
                     /note="Doublecortin-like domain 2 found in doublecortin
                     domain-containing protein 5 (DCDC5); cd17157"
                     /db_xref="CDD:340677"
     Site            order(328,344)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340677"
     Region          <547..580
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          <730..>774
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cl49609"
                     /db_xref="CDD:483949"
     Region          860..880
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (M0R2J8.1)"
     Region          936..1013
                     /region_name="DCX1_DCDC5"
                     /note="Doublecortin-like domain 1 found in doublecortin
                     domain-containing protein 5 (DCDC5); cd17156"
                     /db_xref="CDD:340676"
     Site            order(950,964,986,996)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340676"
     Region          1032..1267
                     /region_name="beta-trefoil_Ricin_DCDC1"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in doublecortin domain-containing protein 1 (DCDC1)
                     and similar proteins; cd23427"
                     /db_xref="CDD:467305"
     Site            order(1049..1052,1061,1063,1066,1164..1165)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467305"
     Site            order(1185..1188,1198,1200,1203,1208..1209)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467305"
     Site            order(1231..1234,1247,1249,1252,1260..1261)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467305"
     Region          1412..1549
                     /region_name="DCX3_DCDC5"
                     /note="Doublecortin-like domain 3 found in doublecortin
                     domain-containing protein 5 (DCDC5); cd17158"
                     /db_xref="CDD:340678"
     Region          1667..1739
                     /region_name="DCX4_DCDC5"
                     /note="Doublecortin-like domain 4 found in doublecortin
                     domain-containing protein 5 (DCDC5); cd17159"
                     /db_xref="CDD:340679"
     Site            order(1699,1725)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340679"
     CDS             1..1783
                     /gene="DCDC1"
                     /gene_synonym="DCDC5"
                     /coded_by="NM_001367979.1:168..5519"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS91454.1"
                     /db_xref="GeneID:341019"
                     /db_xref="HGNC:HGNC:20625"
                     /db_xref="MIM:608062"
ORIGIN      
        1 maktgaedhr ealsqsslsl lteamevlqq sspegtldgn tvnpiykyil ndlprefmss
       61 qakavikttd dylqsqfgpn rlvhsaavse gsglqdcsth qtasdhshde isdldsyksn
      121 sknnscsisa skrnrpvsap vgqlrvaefs slkfqsarnw qklsqrhklq prvikvtayk
      181 ngsrtvfarv tvptitllle ecteklnlnm aarrvfladg kealepedip headvyvstg
      241 epflnpfkki kdhlllikkv twtmnglmlp tdikrrktkp vlsirmkklt ertsvrilff
      301 kngmgqdghe itvgketmkk vldtctirmn lnlparyfyd lygrkiedis kvpllekclq
      361 nsitplrgll wvskgegfsp sgakmyiqgv llalyqrlks akkyykqlnl vmneqkekit
      421 ekvilsmtak ehhkeqeevs rlidelqtai ksnighlckl gpqlqaeqeq fssyvyqhik
      481 slpantlvpg glqlkvfeng kntgeisvgi skkdlgsdsp iqtdhmmerl llkihqrlqg
      541 ssinppglny ssmrlfdeng qeiknplslk neqkiwvsyg rayrsplnla lgltfdrvsa
      601 fargdimvay ktfldpnavl lpgcgnwevc egfpinfnct sqqipdqfek vdlenhflqn
      661 kvdpnivlha svsigkwsfs gseassrsqi apsilwpvas vwlitktgmi lsraitqgcl
      721 aighpirvka aegtslegyk lilqkrhsgd dsqkwvfgtd gciyskaypq fvltyleeln
      781 aqvdvtqtey hihhgawtta hqehgrnlae evlqesasnl glkqlpepsd thlmpegsle
      841 etgeltvalv rkleekhpka saqrwaikhe gtskpgqwkh srvenplwnk ltymwpvlps
      901 gqlneefdwp iqgllvpssp pmkkpicktt epyapvrlrv lqngeknknr svtilgpdis
      961 pgrktqctei lnlpsaarrl ynekgkeifa lkdlqrdelv yvscgelwin pdlsiaqqkk
     1021 qiflrnlesd iakiqifcst hkiealvlev qsdivsgskl avhkpvaifg eekqvtepee
     1081 kqmqedpltt enasseilds hvrahlrmka chtlpryawq etshdfdedd slpkktekgl
     1141 fenvepqkkh scspkhsklh khchqqfeyr dgqiishaap qlvlgvqgpn lrsgmevvlv
     1201 ekksdgshqr wihqedsrtf hlvsnpdlvl avsmtktrne vcgypvivqk ykpynngaan
     1261 qkwhymknik alvafhstal dkeitsanya gvctssvike enidqpgycy lspdgkrktm
     1321 lclacgqsmr tekglkqllp gvpflcisgt ktqkpflqgp fkvisvaevd lscdkaektl
     1381 syyqarllsl rmktctqaas hsgmaathqk avkiiaykng dgyrngkliv agtfpmllte
     1441 cteqlglara askvytkdgt piftlrdlvl waldesflqr dsekqkqdaa pvgkeqiive
     1501 knprmkvknr lfaksvtsds ldgidksllt lilrnpiaiw vscgepflpp nalqkaekle
     1561 kqnwlkkdri ladldtmrhk mrqlkgrrva acqpatmvpt kspvqpvvve ggwteqtqqe
     1621 iklmelirht eahlseiqem eskinfpiat kriavkpsnl ykqpntkrvw iylnggrped
     1681 gtyawgktis ellqdcssrl kmthparaly tpsgepiqsw ddierdmvic vsmghgfktp
     1741 kelkqlmeir anyarirrqq gpqatdivvs pstkllslah lhn
//
LOCUS       NP_689534                273 aa            linear   PRI 27-APR-2025
DEFINITION  endoplasmic reticulum resident protein 27 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_689534
VERSION     NP_689534.1
DBSOURCE    REFSEQ: accession NM_152321.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Kober,F.X., Koelmel,W., Kuper,J., Drechsler,J., Mais,C.,
            Hermanns,H.M. and Schindelin,H.
  TITLE     The crystal structure of the protein-disulfide isomerase family
            member ERp27 provides insights into its substrate binding
            capabilities
  JOURNAL   J Biol Chem 288 (3), 2029-2039 (2013)
   PUBMED   23192347
  REMARK    GeneRIF: ERp27 is able to distinguish between folded and unfolded
            substrates, only interacting with the latter and presenting them to
            for catalysis.
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Galligan,J.J. and Petersen,D.R.
  TITLE     The human protein disulfide isomerase gene family
  JOURNAL   Hum Genomics 6 (1), 6 (2012)
   PUBMED   23245351
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Verweij,M.C., Koppers-Lalic,D., Loch,S., Klauschies,F., de la
            Salle,H., Quinten,E., Lehner,P.J., Mulder,A., Knittler,M.R.,
            Tampe,R., Koch,J., Ressing,M.E. and Wiertz,E.J.
  TITLE     The varicellovirus UL49.5 protein blocks the transporter associated
            with antigen processing (TAP) by inhibiting essential
            conformational transitions in the 6+6 transmembrane TAP core
            complex
  JOURNAL   J Immunol 181 (7), 4894-4907 (2008)
   PUBMED   18802093
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Alanen,H.I., Williamson,R.A., Howard,M.J., Hatahet,F.S., Salo,K.E.,
            Kauppila,A., Kellokumpu,S. and Ruddock,L.W.
  TITLE     ERp27, a new non-catalytic endoplasmic reticulum-located human
            protein disulfide isomerase family member, interacts with ERp57
  JOURNAL   J Biol Chem 281 (44), 33727-33738 (2006)
   PUBMED   16940051
  REMARK    GeneRIF: ERp27 is bound by ERp57 both in vitro and in vivo by a
            similar mechanism by which ERp57 binds calreticulin
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK056677.1, AY358536.1, BQ574479.1 and AA772096.1.
            
            Summary: This gene encodes a noncatalytic member of the protein
            disulfide isomerase (PDI) family of endoplasmic reticulum (ER)
            proteins. The canonical protein has an N-terminal signal sequence,
            two thioredoxin (TRX)-like domains and a C-terminal ER-retention
            sequence. Alternative splicing results in multiple transcript
            variants encoding distinct isoforms; some of which lack domains
            present in the canonical protein. [provided by RefSeq, Dec 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056677.1, AY358536.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153347 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000266397.7/ ENSP00000266397.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.3"
     Protein         1..273
                     /product="endoplasmic reticulum resident protein 27
                     isoform 1 precursor"
                     /note="endoplasmic reticulum protein 27 kDa; protein
                     disulfide isomerase family A, member 8; endoplasmic
                     reticulum resident protein 27; ER protein 27; inactive
                     protein disulfide-isomerase 27"
                     /calculated_mol_wt=27753
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2745
     mat_peptide     26..273
                     /product="Endoplasmic reticulum resident protein 27.
                     /id=PRO_0000281118"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN0.1)"
                     /calculated_mol_wt=27753
     Region          64..250
                     /region_name="Thioredoxin_6"
                     /note="Thioredoxin-like domain; pfam13848"
                     /db_xref="CDD:463999"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q96DN0.1)"
     Region          230..233
                     /region_name="PDIA3-binding site.
                     /evidence=ECO:0000269|PubMed:16940051"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN0.1)"
     Region          270..273
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000305|PubMed:16940051"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN0.1)"
     CDS             1..273
                     /gene="ERP27"
                     /gene_synonym="C12orf46; PDIA8"
                     /coded_by="NM_152321.4:30..851"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8670.1"
                     /db_xref="GeneID:121506"
                     /db_xref="HGNC:HGNC:26495"
                     /db_xref="MIM:610642"
ORIGIN      
        1 meaapsrfmf llflltcela aevaaeveks sdgpgaaqep twltdvpaam efiaatevav
       61 igffqdleip avpilhsmvq kfpgvsfgis tdsevlthyn itgnticlfr lvdneqlnle
      121 dediesidat klsrfieins lhmvteynpv tviglfnsvi qihlllimnk aspeyeenmh
      181 ryqkaaklfq gkilfilvds gmkengkvis ffklkesqlp alaiyqtldd ewdtlptaev
      241 svehvqnfcd gflsgkllke nresegktpk vel
//
LOCUS       NP_859062                395 aa            linear   PRI 27-APR-2025
DEFINITION  protein TAMALIN isoform 1 [Homo sapiens].
ACCESSION   NP_859062
VERSION     NP_859062.1
DBSOURCE    REFSEQ: accession NM_181711.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Pandey,S., Ramsakha,N., Sharma,R., Gulia,R., Ojha,P., Lu,W. and
            Bhattacharyya,S.
  TITLE     The post-synaptic scaffolding protein tamalin regulates
            ligand-mediated trafficking of metabotropic glutamate receptors
  JOURNAL   J Biol Chem 295 (25), 8575-8588 (2020)
   PUBMED   32376687
  REMARK    GeneRIF: The post-synaptic scaffolding protein tamalin regulates
            ligand-mediated trafficking of metabotropic glutamate receptors.
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Matosin,N., Fernandez-Enright,F., Lum,J.S., Andrews,J.L., Engel,M.,
            Huang,X.F. and Newell,K.A.
  TITLE     Metabotropic glutamate receptor 5, and its trafficking molecules
            Norbin and Tamalin, are increased in the CA1 hippocampal region of
            subjects with schizophrenia
  JOURNAL   Schizophr Res 166 (1-3), 212-218 (2015)
   PUBMED   26048293
  REMARK    GeneRIF: Schizophrenia subjects compared to controls showed a
            marked increase in CA1 hippocampal Norbin, and Tamalin proteins
            (47% and 34% respectively), which are endogenous regulators of
            mGluR5 signalling and trafficking
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Fransen,E., Bonneux,S., Corneveaux,J.J., Schrauwen,I., Di
            Berardino,F., White,C.H., Ohmen,J.D., Van de Heyning,P.,
            Ambrosetti,U., Huentelman,M.J., Van Camp,G. and Friedman,R.A.
  TITLE     Genome-wide association analysis demonstrates the highly polygenic
            character of age-related hearing impairment
  JOURNAL   Eur J Hum Genet 23 (1), 110-115 (2015)
   PUBMED   24939585
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Heinrich,F., Nanda,H., Goh,H.Z., Bachert,C., Losche,M. and
            Linstedt,A.D.
  TITLE     Myristoylation restricts orientation of the GRASP domain on
            membranes and promotes membrane tethering
  JOURNAL   J Biol Chem 289 (14), 9683-9691 (2014)
   PUBMED   24505136
  REMARK    GeneRIF: myristoylated GRASP promoted tethering and exhibited a
            unique membrane complex. Thus, myristoylation restricts the
            membrane orientation of the GRASP domain favoring interactions in
            trans for membrane tethering.
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Attar,M.A. and Santy,L.C.
  TITLE     The scaffolding protein GRASP/Tamalin directly binds to Dock180 as
            well as to cytohesins facilitating GTPase crosstalk in epithelial
            cell migration
  JOURNAL   BMC Cell Biol 14, 9 (2013)
   PUBMED   23441967
  REMARK    GeneRIF: GRASP bridges the guanine nucleotide exchange factors
            (GEFs) that activate Arf and Rac, thereby promoting Arf-to-Rac
            signaling By binding to both cytohesin 2/ARNO and Dock180.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Sugi,T., Oyama,T., Muto,T., Nakanishi,S., Morikawa,K. and
            Jingami,H.
  TITLE     Crystal structures of autoinhibitory PDZ domain of Tamalin:
            implications for metabotropic glutamate receptor trafficking
            regulation
  JOURNAL   EMBO J 26 (8), 2192-2205 (2007)
   PUBMED   17396155
  REMARK    GeneRIF: The crystal structures of the autoinhibitory PDZ domain of
            Tamalin has implications for the regulation of metabotropic
            glutamate receptor trafficking.
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Kitano,J., Yamazaki,Y., Kimura,K., Masukado,T., Nakajima,Y. and
            Nakanishi,S.
  TITLE     Tamalin is a scaffold protein that interacts with multiple neuronal
            proteins in distinct modes of protein-protein association
  JOURNAL   J Biol Chem 278 (17), 14762-14768 (2003)
   PUBMED   12586822
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Kitano,J., Kimura,K., Yamazaki,Y., Soda,T., Shigemoto,R.,
            Nakajima,Y. and Nakanishi,S.
  TITLE     Tamalin, a PDZ domain-containing protein, links a protein complex
            formation of group 1 metabotropic glutamate receptors and the
            guanine nucleotide exchange factor cytohesins
  JOURNAL   J Neurosci 22 (4), 1280-1289 (2002)
   PUBMED   11850456
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Nevrivy,D.J., Peterson,V.J., Avram,D., Ishmael,J.E., Hansen,S.G.,
            Dowell,P., Hruby,D.E., Dawson,M.I. and Leid,M.
  TITLE     Interaction of GRASP, a protein encoded by a novel retinoic
            acid-induced gene, with members of the cytohesin family of guanine
            nucleotide exchange factors
  JOURNAL   J Biol Chem 275 (22), 16827-16836 (2000)
   PUBMED   10828067
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Dominguez,O., Ashhab,Y., Sabater,L., Belloso,E., Caro,P. and
            Pujol-Borrell,R.
  TITLE     Cloning of ARE-containing genes by AU-motif-directed display
  JOURNAL   Genomics 54 (2), 278-286 (1998)
   PUBMED   9828130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY052304.1, BC053666.1 and
            BC052967.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that functions as a molecular
            scaffold, linking receptors, including group 1 metabotropic
            glutamate receptors, to neuronal proteins. The encoded protein
            contains conserved domains, including a leucine zipper sequence,
            PDZ domain and a C-terminal PDZ-binding motif. Alternately spliced
            transcript variants have been observed for this gene.[provided by
            RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279868.3230.1, BC053666.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000293662.9/ ENSP00000293662.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..395
                     /product="protein TAMALIN isoform 1"
                     /note="general receptor for phosphoinositides 1 associated
                     scaffold protein; GRP1 (general receptor for
                     phosphoinositides 1)-associated scaffold protein; protein
                     TAMALIN"
                     /calculated_mol_wt=42492
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJA9; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R4T5; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Region          97..187
                     /region_name="PDZ_tamalin_CYTIP-like"
                     /note="PDZ domain of tamalin, cytohesin-1-interacting
                     protein (CYTIP), and related domains; cd06713"
                     /db_xref="CDD:467197"
     Site            order(111..117,136,139,168,172,175..176)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467197"
     Region          181..258
                     /region_name="Interaction with PSCD3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Site            270
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJA9; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Region          293..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJA9; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     CDS             1..395
                     /gene="TAMALIN"
                     /gene_synonym="GRASP"
                     /coded_by="NM_181711.4:75..1262"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8817.1"
                     /db_xref="GeneID:160622"
                     /db_xref="HGNC:HGNC:18707"
                     /db_xref="MIM:612027"
ORIGIN      
        1 mtlrrlrklq qkeeaaatpd paartpdsev apaapvptpg ppaaaatpgp padelyaale
       61 dyhpaelyra lavsggtlpr rkgsgfrwkn lsqspeqqrk vltlekednq tfgfeiqtyg
      121 lhhreeqrve mvtfvcrvhe sspaqlaglt pgdtiasvng lnvegirhre ivdiikasgn
      181 vlrletlygt sirkaelear lqylkqtlye kwgeyrslmv qeqrlvhglv vkdpsiydtl
      241 esvrsclyga gllpgslpfg pllavpgrpr ggarrargda ddavyhtcff gdseppalpp
      301 pppparafgp gpaetpavgp gpgpraalsr sasvrcagpg ggggggapga lwteareqal
      361 cgpglrktky rsfrrrllkf ipglnrslee eesql
//
LOCUS       NP_060283                359 aa            linear   PRI 27-APR-2025
DEFINITION  Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase [Homo
            sapiens].
ACCESSION   NP_060283
VERSION     NP_060283.3
DBSOURCE    REFSEQ: accession NM_017813.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Chen,Q.W., Cai,Q.Q., Yang,Y., Dong,S., Liu,Y.Y., Chen,Z.Y.,
            Kang,C.L., Qi,B., Dong,Y.W., Wu,W., Zhuang,L.P., Shen,Y.H.,
            Meng,Z.Q. and Wu,X.Z.
  TITLE     LncRNA BC promotes lung adenocarcinoma progression by modulating
            IMPAD1 alternative splicing
  JOURNAL   Clin Transl Med 13 (1), e1129 (2023)
   PUBMED   36650118
  REMARK    GeneRIF: LncRNA BC promotes lung adenocarcinoma progression by
            modulating IMPAD1 alternative splicing.
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Yang,Y.F., Wang,Y.Y., Hsiao,M., Lo,S., Chang,Y.C., Jan,Y.H.,
            Lai,T.C., Lee,Y.C., Hsieh,Y.C. and Yuan,S.F.
  TITLE     IMPAD1 functions as mitochondrial electron transport inhibitor that
            prevents ROS production and promotes lung cancer metastasis through
            the AMPK-Notch1-HEY1 pathway
  JOURNAL   Cancer Lett 485, 27-37 (2020)
   PUBMED   32417395
  REMARK    GeneRIF: IMPAD1 functions as mitochondrial electron transport
            inhibitor that prevents ROS production and promotes lung cancer
            metastasis through the AMPK-Notch1-HEY1 pathway.
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Wu,Z.L., Robey,M.T., Tatge,T., Lin,C., Leymarie,N., Zou,Y. and
            Zaia,J.
  TITLE     Detecting O-GlcNAc using in vitro sulfation
  JOURNAL   Glycobiology 24 (8), 740-747 (2014)
   PUBMED   24799377
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Nizon,M., Alanay,Y., Tuysuz,B., Kiper,P.O., Genevieve,D.,
            Sillence,D., Huber,C., Munnich,A. and Cormier-Daire,V.
  TITLE     IMPAD1 mutations in two Catel-Manzke like patients
  JOURNAL   Am J Med Genet A 158A (9), 2183-2187 (2012)
   PUBMED   22887726
  REMARK    GeneRIF: concluded that IMPAD1 should be screened for patients with
            Catel-Manzke and additional features
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Prather,B., Ethen,C.M., Machacek,M. and Wu,Z.L.
  TITLE     Golgi-resident PAP-specific 3'-phosphatase-coupled sulfotransferase
            assays
  JOURNAL   Anal Biochem 423 (1), 86-92 (2012)
   PUBMED   22289690
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Vissers,L.E., Lausch,E., Unger,S., Campos-Xavier,A.B., Gilissen,C.,
            Rossi,A., Del Rosario,M., Venselaar,H., Knoll,U., Nampoothiri,S.,
            Nair,M., Spranger,J., Brunner,H.G., Bonafe,L., Veltman,J.A.,
            Zabel,B. and Superti-Furga,A.
  TITLE     Chondrodysplasia and abnormal joint development associated with
            mutations in IMPAD1, encoding the Golgi-resident nucleotide
            phosphatase, gPAPP
  JOURNAL   Am J Hum Genet 88 (5), 608-615 (2011)
   PUBMED   21549340
  REMARK    GeneRIF: Affected individuals carried homozygous missense mutations
            in IMPAD1, the gene coding for gPAPP, a Golgi-resident nucleotide
            phosphatase that hydrolyzes phosphoadenosine phosphate (PAP), the
            byproduct of sulfotransferase reactions, to AMP.
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Frederick,J.P., Tafari,A.T., Wu,S.M., Megosh,L.C., Chiou,S.T.,
            Irving,R.P. and York,J.D.
  TITLE     A role for a lithium-inhibited Golgi nucleotidase in skeletal
            development and sulfation
  JOURNAL   Proc Natl Acad Sci U S A 105 (33), 11605-11612 (2008)
   PUBMED   18695242
REFERENCE   9  (residues 1 to 359)
  AUTHORS   Zhang,H., Li,X.J., Martin,D.B. and Aebersold,R.
  TITLE     Identification and quantification of N-linked glycoproteins using
            hydrazide chemistry, stable isotope labeling and mass spectrometry
  JOURNAL   Nat Biotechnol 21 (6), 660-666 (2003)
   PUBMED   12754519
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI601447.1, BC017797.1,
            AC032027.7 and AI095394.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 20, 2007 this sequence version replaced NP_060283.2.
            
            Summary: This gene encodes a member of the inositol monophosphatase
            family. The encoded protein is localized to the Golgi apparatus and
            catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to
            adenosine monophosphate (AMP). Mutations in this gene are a cause
            of GRAPP type chondrodysplasia with joint dislocations, and a
            pseudogene of this gene is located on the long arm of chromosome 1.
            [provided by RefSeq, Dec 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.550838.1,
                                           SRR14038192.3307311.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262644.9/ ENSP00000262644.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..359
                     /product="Golgi-resident adenosine 3',5'-bisphosphate
                     3'-phosphatase"
                     /EC_number="3.1.3.7"
                     /note="myo-inositol monophosphatase A3; IMPase 3;
                     inositol-1(or 4)-monophosphatase 3; inositol
                     monophosphatase domain-containing protein 1;
                     golgi-resident PAP phosphatase; Golgi 3-prime
                     phosphoadenosine 5-prime phosphate 3-prime phosphatase;
                     inositol monophosphatase domain containing 1;
                     golgi-resident nucleotide phosphatase; phosphoadenosine
                     phosphate 3'-nucleotidase"
                     /calculated_mol_wt=38550
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:25732826; propagated from
                     UniProtKB/Swiss-Prot (Q9NX62.1)"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX62.1)"
     Region          66..349
                     /region_name="IPPase"
                     /note="Inositol polyphosphate-1-phosphatase, a member of
                     the Mg++ dependent family of inositol monophosphatase-like
                     domains, hydrolyzes the 1' position phosphate from
                     inositol 1,3,4-trisphosphate and inositol
                     1,4-bisphosphate. Members in this group may also...;
                     cd01640"
                     /db_xref="CDD:238818"
     Region          86..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX62.1)"
     Site            order(110,133..134,174..179,181,244,266..269,272,290,292,
                     295..296,299..300)
                     /site_type="active"
                     /db_xref="CDD:238818"
     Site            259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:18695242; propagated from
                     UniProtKB/Swiss-Prot (Q9NX62.1)"
     CDS             1..359
                     /gene="BPNT2"
                     /gene_synonym="GPAPP; IMP 3; IMP-3; IMPA3; IMPAD1"
                     /coded_by="NM_017813.5:283..1362"
                     /db_xref="CCDS:CCDS6169.1"
                     /db_xref="GeneID:54928"
                     /db_xref="HGNC:HGNC:26019"
                     /db_xref="MIM:614010"
ORIGIN      
        1 mapmgirlsp lgvavfcllg lgvlyhlysg flagrfslfg lggepgggaa gpaaaadggt
       61 vdlremlavs vlaavrggde vrrvresnvl hekskgktre gaedkmtsgd vlsnrkmfyl
      121 lktafpsvqi nteehvdaad qevilwdhki pedilkevtt pkevpaesvt vwidpldatq
      181 eytedlrkyv ttmvcvavng kpmlgvihkp fseytawamv dggsnvkars synektpriv
      241 vsrshsgmvk qvalqtfgnq ttiipaggag ykvlalldvp dksqekadly ihvtyikkwd
      301 icagnailka lgghmttlsg eeisytgsdg ieggllasir mnhqalvrkl pdlektghk
//
LOCUS       NP_001357268             158 aa            linear   PRI 27-APR-2025
DEFINITION  high mobility group protein B1 isoform 2 [Homo sapiens].
ACCESSION   NP_001357268 XP_024305111
VERSION     NP_001357268.1
DBSOURCE    REFSEQ: accession NM_001370339.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Wang,S., Cheng,T., Chen,X., Zeng,C., Qin,W. and Xu,Y.
  TITLE     IFN-gamma induces acute graft-versus-host disease by promoting
            HMGB1-mediated nuclear-to-cytoplasm translocation and autophagic
            degradation of p53
  JOURNAL   Clin Sci (Lond) 138 (20), 1287-1304 (2024)
   PUBMED   39312196
  REMARK    GeneRIF: IFN-gamma induces acute graft-versus-host disease by
            promoting HMGB1-mediated nuclear-to-cytoplasm translocation and
            autophagic degradation of p53.
REFERENCE   2  (residues 1 to 158)
  AUTHORS   De Luca,G., Goette,N.P., Lev,P.R., Baroni Pietto,M.C., Marin
            Oyarzun,C.P., Castro Rios,M.A., Moiraghi,B., Sackmann,F.,
            Kamiya,L.J., Verri,V., Caula,V., Fernandez,V., Vicente,A., Pose
            Cabarcos,J., Caruso,V., Camacho,M.F., Larripa,I.B., Khoury,M.,
            Marta,R.F., Glembotsky,A.C. and Heller,P.G.
  TITLE     Elevated levels of damage-associated molecular patterns HMGB1 and
            S100A8/A9 coupled with toll-like receptor-triggered monocyte
            activation are associated with inflammation in patients with
            myelofibrosis
  JOURNAL   Front Immunol 15, 1365015 (2024)
   PUBMED   39391311
  REMARK    GeneRIF: Elevated levels of damage-associated molecular patterns
            HMGB1 and S100A8/A9 coupled with toll-like receptor-triggered
            monocyte activation are associated with inflammation in patients
            with myelofibrosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Ozbay Kurt,F.G., Cicortas,B.A., Balzasch,B.M., De la Torre,C.,
            Ast,V., Tavukcuoglu,E., Ak,C., Wohlfeil,S.A., Cerwenka,A.,
            Utikal,J. and Umansky,V.
  TITLE     S100A9 and HMGB1 orchestrate MDSC-mediated immunosuppression in
            melanoma through TLR4 signaling
  JOURNAL   J Immunother Cancer 12 (9), e009552 (2024)
   PUBMED   39266214
  REMARK    GeneRIF: S100A9 and HMGB1 orchestrate MDSC-mediated
            immunosuppression in melanoma through TLR4 signaling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Gao,P., Wu,Y. and Yan,Z.
  TITLE     LncRNA ILF3-AS1 mediates oxidative stress and inflammation through
            miR-504-3p/HMGB1 axis in a cellular model of temporal lobe epilepsy
  JOURNAL   Brain Behav 14 (8), e3615 (2024)
   PUBMED   39135276
  REMARK    GeneRIF: LncRNA ILF3-AS1 mediates oxidative stress and inflammation
            through miR-504-3p/HMGB1 axis in a cellular model of temporal lobe
            epilepsy.
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Ferrari,S., Finelli,P., Rocchi,M. and Bianchi,M.E.
  TITLE     The active gene that encodes human high mobility group 1 protein
            (HMG1) contains introns and maps to chromosome 13
  JOURNAL   Genomics 35 (2), 367-371 (1996)
   PUBMED   8661151
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Ge,H. and Roeder,R.G.
  TITLE     The high mobility group protein HMG1 can reversibly inhibit class
            II gene transcription by interaction with the TATA-binding protein
  JOURNAL   J Biol Chem 269 (25), 17136-17140 (1994)
   PUBMED   8006019
REFERENCE   7  (residues 1 to 158)
  AUTHORS   Paull,T.T., Haykinson,M.J. and Johnson,R.C.
  TITLE     The nonspecific DNA-binding and -bending proteins HMG1 and HMG2
            promote the assembly of complex nucleoprotein structures
  JOURNAL   Genes Dev 7 (8), 1521-1534 (1993)
   PUBMED   8339930
REFERENCE   8  (residues 1 to 158)
  AUTHORS   Parkkinen,J. and Rauvala,H.
  TITLE     Interactions of plasminogen and tissue plasminogen activator (t-PA)
            with amphoterin. Enhancement of t-PA-catalyzed plasminogen
            activation by amphoterin
  JOURNAL   J Biol Chem 266 (25), 16730-16735 (1991)
   PUBMED   1909331
REFERENCE   9  (residues 1 to 158)
  AUTHORS   Wen,L., Huang,J.K., Johnson,B.H. and Reeck,G.R.
  TITLE     A human placental cDNA clone that encodes nonhistone chromosomal
            protein HMG-1
  JOURNAL   Nucleic Acids Res 17 (3), 1197-1214 (1989)
   PUBMED   2922262
REFERENCE   10 (residues 1 to 158)
  AUTHORS   Bernues,J., Espel,E. and Querol,E.
  TITLE     Identification of the core-histone-binding domains of HMG1 and HMG2
  JOURNAL   Biochim Biophys Acta 866 (4), 242-251 (1986)
   PUBMED   3697355
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353648.27.
            
            On May 7, 2019 this sequence version replaced XP_024305111.1.
            
            Summary: This gene encodes a protein that belongs to the High
            Mobility Group-box superfamily. The encoded non-histone, nuclear
            DNA-binding protein regulates transcription, and is involved in
            organization of DNA. This protein plays a role in several cellular
            processes, including inflammation, cell differentiation and tumor
            cell migration. Multiple pseudogenes of this gene have been
            identified. Alternative splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Sep
            2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.225312.1,
                                           SRR14038191.2124332.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146411, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.3"
     Protein         1..158
                     /product="high mobility group protein B1 isoform 2"
                     /note="Sulfoglucuronyl carbohydrate binding protein;
                     Amphoterin; high-mobility group (nonhistone chromosomal)
                     protein 1; high mobility group protein B1"
                     /calculated_mol_wt=18180
     Region          1..97
                     /region_name="Sufficient for interaction with HAVCR2.
                     /evidence=ECO:0000250|UniProtKB:P63158"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          3..15
                     /region_name="LPS binding (delipidated).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          8..76
                     /region_name="HMG-box_HMGB_rpt1"
                     /note="first high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21978"
                     /db_xref="CDD:438794"
     Site            order(8..10,13,16..17,19..21,25,28,35..36,38..39,41..43,
                     45..46,50)
                     /site_type="other"
                     /note="p53 binding site [polypeptide binding]"
                     /db_xref="CDD:438794"
     Site            order(8,10..11,13..17,20..21,36,38..39,41..43,46,49)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438794"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            10..11
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin:thrombomodulin.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            12
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          27..43
                     /region_name="Nuclear localization signal (NLS) 1.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            67..68
                     /site_type="cleavage"
                     /note="Cleavage, by CASP1.
                     /evidence=ECO:0000269|PubMed:24474694; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          76..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          80..96
                     /region_name="LPS binding (Lipid A).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          89..108
                     /region_name="Cytokine-stimulating activity.
                     /evidence=ECO:0000269|PubMed:12765338"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            90
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          93..157
                     /region_name="HMG-box_HMGB_rpt2"
                     /note="second high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21979"
                     /db_xref="CDD:438795"
     Site            order(94..100,102..104,106..107,110,122..123,125..127,130,
                     133,152,155..156)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438795"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            141
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     CDS             1..158
                     /gene="HMGB1"
                     /gene_synonym="HMG-1; HMG1; HMG3; SBP-1"
                     /coded_by="NM_001370339.1:156..632"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS86347.1"
                     /db_xref="GeneID:3146"
                     /db_xref="HGNC:HGNC:4983"
                     /db_xref="MIM:163905"
ORIGIN      
        1 mgkgdpkkpr gkmssyaffv qtcreehkkk hpdasvnfse fskkcserwk tmsakekgkf
       61 edmakadkar yeremktyip pkgetkkkfk dpnapkrpps afflfcseyr pkikgehpgl
      121 sigdvakklg emwnntaadd kqpyekkaak lkekyekf
//
LOCUS       NP_001032               1827 aa            linear   PRI 27-APR-2025
DEFINITION  sucrase-isomaltase, intestinal [Homo sapiens].
ACCESSION   NP_001032
VERSION     NP_001032.2
DBSOURCE    REFSEQ: accession NM_001041.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1827)
  AUTHORS   Iryanci,F.I., Guven,B. and Cakir,M.
  TITLE     Congenital Sucrase-Isomaltase Deficiency: Same Mutation with
            Different Clinical Presentations
  JOURNAL   Turk J Gastroenterol 35 (4), 343-349 (2024)
   PUBMED   39128102
  REMARK    GeneRIF: Congenital Sucrase-Isomaltase Deficiency: Same Mutation
            with Different Clinical Presentations.
REFERENCE   2  (residues 1 to 1827)
  AUTHORS   Zamfir-Taranu,A., Loscher,B.S., Husein,D.M., Hoter,A.,
            Garcia-Etxebarria,K., Etxeberria,U., Gayoso,L., Mayr,G.,
            Nilholm,C., Gustafsson,R.J., Ozaydin,O., Zheng,T.,
            Esteban-Blanco,C., Bozzarelli,I., Bonfiglio,F., Rizk,S., Franke,A.,
            Bujanda,L., Naim,H.Y., Ohlsson,B. and D'Amato,M.
  TITLE     Sucrase-isomaltase genotype and response to a starch-reduced and
            sucrose-reduced diet in IBS-D patients
  JOURNAL   Gut 73 (4), 706-708 (2024)
   PUBMED   36878682
  REMARK    GeneRIF: Sucrase-isomaltase genotype and response to a
            starch-reduced and sucrose-reduced diet in IBS-D patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1827)
  AUTHORS   Tannous,S., Stellbrinck,T., Hoter,A. and Naim,H.Y.
  TITLE     Interaction between the alpha-glucosidases, sucrase-isomaltase and
            maltase-glucoamylase, in human intestinal brush border membranes
            and its potential impact on disaccharide digestion
  JOURNAL   Front Mol Biosci 10, 1160860 (2023)
   PUBMED   36968271
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1827)
  AUTHORS   Taskin,D.G., Civan,H.A., Sari,E.E., Altuntas,C., Ersoy,M.,
            Tuncel,T., Onay,H. and Selimoglu,A.
  TITLE     Prevalence of congenital sucrase-isomaltase deficiency in Turkey
            may be much higher than the estimates
  JOURNAL   J Genet 102 (2023)
   PUBMED   37349966
  REMARK    GeneRIF: Prevalence of congenital sucrase-isomaltase deficiency in
            Turkey may be much higher than the estimates.
REFERENCE   5  (residues 1 to 1827)
  AUTHORS   Hoter,A. and Naim,H.Y.
  TITLE     The glucose-regulated protein GRP94 interacts avidly in the
            endoplasmic reticulum with sucrase-isomaltase isoforms that are
            associated with congenital sucrase-isomaltase deficiency
  JOURNAL   Int J Biol Macromol 186, 237-243 (2021)
   PUBMED   34242650
  REMARK    GeneRIF: The glucose-regulated protein GRP94 interacts avidly in
            the endoplasmic reticulum with sucrase-isomaltase isoforms that are
            associated with congenital sucrase-isomaltase deficiency.
REFERENCE   6  (residues 1 to 1827)
  AUTHORS   Chantret,I., Lacasa,M., Chevalier,G., Ruf,J., Islam,I., Mantei,N.,
            Edwards,Y., Swallow,D. and Rousset,M.
  TITLE     Sequence of the complete cDNA and the 5' structure of the human
            sucrase-isomaltase gene. Possible homology with a yeast
            glucoamylase
  JOURNAL   Biochem J 285 (Pt 3) (Pt 3), 915-923 (1992)
   PUBMED   1353958
REFERENCE   7  (residues 1 to 1827)
  AUTHORS   Wu,G.D., Wang,W. and Traber,P.G.
  TITLE     Isolation and characterization of the human sucrase-isomaltase gene
            and demonstration of intestine-specific transcriptional elements
  JOURNAL   J Biol Chem 267 (11), 7863-7870 (1992)
   PUBMED   1560017
REFERENCE   8  (residues 1 to 1827)
  AUTHORS   Fransen,J.A., Hauri,H.P., Ginsel,L.A. and Naim,H.Y.
  TITLE     Naturally occurring mutations in intestinal sucrase-isomaltase
            provide evidence for the existence of an intracellular sorting
            signal in the isomaltase subunit
  JOURNAL   J Cell Biol 115 (1), 45-57 (1991)
   PUBMED   1717481
  REMARK    Erratum:[J Cell Biol 1991 Dec;115(5):following 1473]
REFERENCE   9  (residues 1 to 1827)
  AUTHORS   Gorvel,J.P., Ferrero,A., Chambraud,L., Rigal,A., Bonicel,J. and
            Maroux,S.
  TITLE     Expression of sucrase-isomaltase and dipeptidylpeptidase IV in
            human small intestine and colon
  JOURNAL   Gastroenterology 101 (3), 618-625 (1991)
   PUBMED   1677636
REFERENCE   10 (residues 1 to 1827)
  AUTHORS   Green,F., Edwards,Y., Hauri,H.P., Povey,S., Ho,M.W., Pinto,M. and
            Swallow,D.
  TITLE     Isolation of a cDNA probe for a human jejunal brush-border
            hydrolase, sucrase-isomaltase, and assignment of the gene locus to
            chromosome 3
  JOURNAL   Gene 57 (1), 101-110 (1987)
   PUBMED   2962903
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC140119.3, DA919374.1,
            BC132860.1, AC092695.8 and BG187733.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 19, 2007 this sequence version replaced NP_001032.1.
            
            Summary: This gene encodes a sucrase-isomaltase enzyme that is
            expressed in the intestinal brush border. The encoded protein is
            synthesized as a precursor protein that is cleaved by pancreatic
            proteases into two enzymatic subunits sucrase and isomaltase. These
            two subunits heterodimerize to form the sucrose-isomaltase complex.
            This complex is essential for the digestion of dietary
            carbohydrates including starch, sucrose and isomaltose. Mutations
            in this gene are the cause of congenital sucrase-isomaltase
            deficiency.[provided by RefSeq, Apr 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X63597.1, BC132834.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264382.8/ ENSP00000264382.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1827
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.1"
     Protein         1..1827
                     /product="sucrase-isomaltase, intestinal"
                     /EC_number="3.2.1.10"
                     /EC_number="3.2.1.48"
                     /note="oligosaccharide alpha-1,6-glucosidase;
                     alpha-glucosidase; Oligo-1,6-glucosidase;
                     Alpha-methylglucosidase"
                     /calculated_mol_wt=209323
     mat_peptide     2..1007
                     /product="isomaltase"
                     /calculated_mol_wt=114207
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:8521865; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            13..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14410.6)"
     Region          40..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14410.6)"
     Region          63..108
                     /region_name="Trefoil"
                     /note="Trefoil (P-type) domain; pfam00088"
                     /db_xref="CDD:459666"
     Site            order(81,104..105)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:238059"
     Site            order(96,104)
                     /site_type="active"
                     /note="putative binding specificity loop [active]"
                     /db_xref="CDD:238059"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20356844; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Region          110..1007
                     /region_name="Isomaltase"
                     /note="propagated from UniProtKB/Swiss-Prot (P14410.6)"
     Region          125..235
                     /region_name="NtCtMGAM_N"
                     /note="N-terminal barrel of NtMGAM and CtMGAM,
                     maltase-glucoamylase; pfam16863"
                     /db_xref="CDD:465286"
     Region          227..333
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            237
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P14410.6)"
     Site            239
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P14410.6)"
     Site            264
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          343..707
                     /region_name="GH31_MGAM_SI_GAA"
                     /note="maltase-glucoamylase, sucrase-isomaltase, lysosomal
                     acid alpha-glucosidase; cd06602"
                     /db_xref="CDD:269888"
     Site            order(360,388..389,425,468,503,505..506,588,601,604,637,
                     662)
                     /site_type="active"
                     /db_xref="CDD:269888"
     Site            391
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P14410.6)"
     Site            400
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P14410.6)"
     Site            437
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            455
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20356844; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            667
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P14410.6)"
     Site            763
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P14410.6)"
     Site            765
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P14410.6)"
     Site            823
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            855
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20356844; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            904
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20356844; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            926
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Region          935..980
                     /region_name="PD"
                     /note="P or trefoil or TFF domain; smart00018"
                     /db_xref="CDD:197472"
     Site            order(946,972..973)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:238059"
     Site            order(963,972)
                     /site_type="active"
                     /note="putative binding specificity loop [active]"
                     /db_xref="CDD:238059"
     Region          994..1108
                     /region_name="NtCtMGAM_N"
                     /note="N-terminal barrel of NtMGAM and CtMGAM,
                     maltase-glucoamylase; pfam16863"
                     /db_xref="CDD:465286"
     mat_peptide     1008..1827
                     /product="sucrase"
                     /calculated_mol_wt=95134
     Region          1008..1827
                     /region_name="Sucrase"
                     /note="propagated from UniProtKB/Swiss-Prot (P14410.6)"
     Region          1100..1214
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            1137
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          1195..1691
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Site            1235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            1303
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            1340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            1354
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            1403
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            1535
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            1572
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            1675
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            1748
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            1763
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     Site            1815
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14410.6)"
     CDS             1..1827
                     /gene="SI"
                     /coded_by="NM_001041.4:65..5548"
                     /db_xref="CCDS:CCDS3196.1"
                     /db_xref="GeneID:6476"
                     /db_xref="HGNC:HGNC:10856"
                     /db_xref="MIM:609845"
ORIGIN      
        1 markkfsgle islivlfviv tiiaialivv latktpavde isdststpat trvttnpsds
       61 gkcpnvlndp vnvrincipe qfptegicaq rgccwrpwnd slipwcffvd nhgynvqdmt
      121 ttsigveakl nripsptlfg ndinsvlftt qnqtpnrfrf kitdpnnrry evphqyvkef
      181 tgptvsdtly dvkvaqnpfs iqvirksngk tlfdtsigpl vysdqylqis trlpsdyiyg
      241 igeqvhkrfr hdlswktwpi ftrdqlpgdn nnnlyghqtf fmciedtsgk sfgvflmnsn
      301 ameifiqptp ivtyrvtggi ldfyillgdt peqvvqqyqq lvglpampay wnlgfqlsrw
      361 nyksldvvke vvrrnreagi pfdtqvtdid ymedkkdfty dqvafnglpq fvqdlhdhgq
      421 kyviildpai sigrrangtt yatyergntq hvwinesdgs tpiigevwpg ltvypdftnp
      481 ncidwwanec sifhqevqyd glwidmnevs sfiqgstkgc nvnklnyppf tpdildklmy
      541 skticmdavq nwgkqydvhs lygysmaiat eqavqkvfpn krsfiltrst fagsgrhaah
      601 wlgdntaswe qmewsitgml efslfgiplv gadicgfvae tteelcrrwm qlgafypfsr
      661 nhnsdgyehq dpaffgqnsl lvkssrqylt irytllpfly tlfykahvfg etvarpvlhe
      721 fyedtnswie dteflwgpal litpvlkqga dtvsayipda iwydyesgak rpwrkqrvdm
      781 ylpadkiglh lrggyiipiq epdvtttasr knplglival genntakgdf fwddgetkdt
      841 iqngnyilyt fsvsnntldi vcthssyqeg ttlafqtvki lgltdsvtev rvaennqpmn
      901 ahsnftydas nqvlliadlk lnlgrnfsvq wnqifsener fncypdadla teqkctqrgc
      961 vwrtgsslsk apecyfprqd nsysvnsary ssmgitadlq lntanarikl psdpistlrv
     1021 evkyhkndml qfkiydpqkk ryevpvplni pttpistyed rlydveiken pfgiqirrrs
     1081 sgrviwdswl pgfafndqfi qistrlpsey iygfgeveht afkrdlnwnt wgmftrdqpp
     1141 gyklnsygfh pyymaleeeg nahgvfllns namdvtfqpt paltyrtvgg ildfymflgp
     1201 tpevatkqyh evighpvmpa ywalgfqlcr ygyantsevr elydamvaan ipydvqytdi
     1261 dymerqldft igeafqdlpq fvdkirgegm ryiiildpai sgnetktypa fergqqndvf
     1321 vkwpntndic wakvwpdlpn itidktlted eavnasrahv afpdffrtst aewwareivd
     1381 fynekmkfdg lwidmnepss fvngtttnqc rndelnyppy fpeltkrtdg lhfrticmea
     1441 eqilsdgtsv lhydvhnlyg wsqmkpthda lqkttgkrgi visrstypts grwgghwlgd
     1501 nyarwdnmdk siigmmefsl fgmsytgadi cgffnnseyh lctrwmqlga fypysrnhni
     1561 antrrqdpas wnetfaemsr nilnirytll pyfytqmhei hanggtvirp llheffdekp
     1621 twdifkqflw gpafmvtpvl epyvqtvnay vpnarwfdyh tgkdigvrgq fqtfnasydt
     1681 inlhvrgghi lpcqepaqnt fysrqkhmkl ivaaddnqma qgslfwddge sidtyerdly
     1741 lsvqfnlnqt tltstilkrg yinksetrlg slhvwgkgtt pvnavtltyn gnknslpfne
     1801 dttnmilrid ltthnvtlee pieinws
//
LOCUS       NP_031368                423 aa            linear   PRI 27-APR-2025
DEFINITION  nucleoporin NUP42 isoform 2 [Homo sapiens].
ACCESSION   NP_031368
VERSION     NP_031368.1
DBSOURCE    REFSEQ: accession NM_007342.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Schwartz,T.U.
  TITLE     The Structure Inventory of the Nuclear Pore Complex
  JOURNAL   J Mol Biol 428 (10 Pt A), 1986-2000 (2016)
   PUBMED   27016207
  REMARK    Review article
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Bui,K.H., von Appen,A., DiGuilio,A.L., Ori,A., Sparks,L.,
            Mackmull,M.T., Bock,T., Hagen,W., Andres-Pons,A., Glavy,J.S. and
            Beck,M.
  TITLE     Integrated structural analysis of the human nuclear pore complex
            scaffold
  JOURNAL   Cell 155 (6), 1233-1243 (2013)
   PUBMED   24315095
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Waldmann,I., Spillner,C. and Kehlenbach,R.H.
  TITLE     The nucleoporin-like protein NLP1 (hCG1) promotes CRM1-dependent
            nuclear protein export
  JOURNAL   J Cell Sci 125 (Pt 1), 144-154 (2012)
   PUBMED   22250199
  REMARK    GeneRIF: NLP1 functions as an accessory factor in CRM1-dependent
            nuclear protein export
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Farjot,G., Sergeant,A. and Mikaelian,I.
  TITLE     A new nucleoporin-like protein interacts with both HIV-1 Rev
            nuclear export signal and CRM-1
  JOURNAL   J Biol Chem 274 (24), 17309-17317 (1999)
   PUBMED   10358091
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Katahira,J., Strasser,K., Podtelejnikov,A., Mann,M., Jung,J.U. and
            Hurt,E.
  TITLE     The Mex67p-mediated nuclear mRNA export pathway is conserved from
            yeast to human
  JOURNAL   EMBO J 18 (9), 2593-2609 (1999)
   PUBMED   10228171
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Fouchier,R.A., Meyer,B.E., Simon,J.H., Fischer,U., Albright,A.V.,
            Gonzalez-Scarano,F. and Malim,M.H.
  TITLE     Interaction of the human immunodeficiency virus type 1 Vpr protein
            with the nuclear pore complex
  JOURNAL   J Virol 72 (7), 6004-6013 (1998)
   PUBMED   9621063
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Van Laer,L., Van Camp,G., van Zuijlen,D., Green,E.D.,
            Verstreken,M., Schatteman,I., Van de Heyning,P., Balemans,W.,
            Coucke,P., Greinwald,J.H., Smith,R.J., Huizing,E. and Willems,P.
  TITLE     Refined mapping of a gene for autosomal dominant progressive
            sensorineural hearing loss (DFNA5) to a 2-cM region, and exclusion
            of a candidate gene that is expressed in the cochlea
  JOURNAL   Eur J Hum Genet 5 (6), 397-405 (1997)
   PUBMED   9450185
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U97198.1 and AI352214.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1174588.1,
                                           SRR3476690.183434.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258742.10/ ENSP00000258742.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.3"
     Protein         1..423
                     /product="nucleoporin NUP42 isoform 2"
                     /note="nucleoporin-like protein 1; H_RG271G13.9;
                     nucleoporin-like protein 2; NUP42 homolog; nucleoporin
                     hCG1; nucleoporin like 2; nucleoporin NUP42"
                     /calculated_mol_wt=44741
     Region          4..22
                     /region_name="zf_CCCH_4"
                     /note="Zinc finger domain; pfam18345"
                     /db_xref="CDD:465719"
     Region          14..15
                     /region_name="FG 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          24..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          94..170
                     /region_name="Interaction with HIV-1 Vpr"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15504.1)"
     Region          <202..389
                     /region_name="PPE"
                     /note="PPE-repeat protein [Function unknown]; COG5651"
                     /db_xref="CDD:444372"
     Region          218..219
                     /region_name="FG 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          220..221
                     /region_name="FG 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          265..266
                     /region_name="FG 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          271..272
                     /region_name="FG 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          288..289
                     /region_name="FG 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          290..291
                     /region_name="FG 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          311..312
                     /region_name="FG 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          336..337
                     /region_name="FG 10"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          345..346
                     /region_name="FG 11"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          364..365
                     /region_name="FG 12"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     Region          365..423
                     /region_name="Interaction with GLE1.
                     /evidence=ECO:0000269|PubMed:16000379"
                     /note="propagated from UniProtKB/Swiss-Prot (O15504.1)"
     CDS             1..423
                     /gene="NUP42"
                     /gene_synonym="CG1; hCG1; NLP-1; NLP1; NLP_1; NUPL2; UIP1"
                     /coded_by="NM_007342.3:39..1310"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5379.1"
                     /db_xref="GeneID:11097"
                     /db_xref="HGNC:HGNC:17010"
                     /db_xref="MIM:619998"
ORIGIN      
        1 maicqfflqg rcrfgdrcwn ehpgargagg grqqpqqqps gnnrrgwntt sqrysnviqp
       61 ssfskstpwg gsrdqekpyf ssfdsgastn rkegfglsen pfaslspdeq kdekkllegi
      121 vkdmevwess gqwmfsvysp vkkkpnisgf tdispeelrl eyhnfltsnn lqsylnsvqr
      181 linqwrnrvn elkslnistk vallsdvkdg vnqaapafgf gssqaatfms pgfpvnnsss
      241 dnaqnfsfkt nsgfaaassg spagfgsspa fgaaastssg istsapafgf gkpevtsaas
      301 fsfkspaass fgspgfsglp aslatgpvra pvapafgggs svagfgspgs hshtafskps
      361 sdtfgnssis tslsasssii atdnvlftpr dkltveeleq fqskkftlgk iplkppplel
      421 lnv
//
LOCUS       NP_001349333             504 aa            linear   ROD 27-APR-2025
DEFINITION  UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2 [Mus
            musculus].
ACCESSION   NP_001349333
VERSION     NP_001349333.1
DBSOURCE    REFSEQ: accession NM_001362404.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Yoshida-Moriguchi,T., Willer,T., Anderson,M.E., Venzke,D.,
            Whyte,T., Muntoni,F., Lee,H., Nelson,S.F., Yu,L. and Campbell,K.P.
  TITLE     SGK196 is a glycosylation-specific O-mannose kinase required for
            dystroglycan function
  JOURNAL   Science 341 (6148), 896-899 (2013)
   PUBMED   23929950
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Hiruma,T., Togayachi,A., Okamura,K., Sato,T., Kikuchi,N.,
            Kwon,Y.D., Nakamura,A., Fujimura,K., Gotoh,M., Tachibana,K.,
            Ishizuka,Y., Noce,T., Nakanishi,H. and Narimatsu,H.
  TITLE     A novel human beta1,3-N-acetylgalactosaminyltransferase that
            synthesizes a unique carbohydrate structure, GalNAcbeta1-3GlcNAc
  JOURNAL   J Biol Chem 279 (14), 14087-14095 (2004)
   PUBMED   14724282
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK151677.1 and CT009546.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK151677.1, AK153362.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849378, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 5.29 cM"
     Protein         1..504
                     /product="UDP-GalNAc:beta-1,
                     3-N-acetylgalactosaminyltransferase 2"
                     /EC_number="2.4.1.313"
                     /note="beta-1,3-GalNAc-T2;
                     beta-1,3-N-acetylgalactosaminyltransferase II"
                     /calculated_mol_wt=57088
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG28.1)"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BG28.1)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BG28.1)"
     Region          <330..459
                     /region_name="Galactosyl_T"
                     /note="Galactosyltransferase; cl21608"
                     /db_xref="CDD:473923"
     CDS             1..504
                     /gene="B3galnt2"
                     /gene_synonym="A930105D20Rik; D230016N13Rik"
                     /coded_by="NM_001362404.1:132..1646"
                     /db_xref="CCDS:CCDS26246.1"
                     /db_xref="GeneID:97884"
                     /db_xref="MGI:MGI:2145517"
ORIGIN      
        1 mrnwlvllcp cvlgaalhlw hlwlrsppdp hntgpsaadq salfphwkfs hydvvvgvls
       61 arnnhelrnv irntwlknll hhptlsqrvl vkfiigargc evpvedredp yscrllnitn
      121 pvlnqeieaf sfpedasssr lsedrvvsvs frvlypivit slgvfydasd vgfqrnitvk
      181 lyqteqeeal fiarfsppsc gvqvnklwyk pveqfilpes fegtivwesq dlhglvsrnl
      241 hrvtvndggg vlrvlaageg alphefmegv egvaggfiyt vqegdallrs lysrpqrlad
      301 hiqdlqveda llqeessvhd divfvdvvdt yrnvpaklln fyrwtvests fdlllktddd
      361 cyidleavfn riaqknldgp nfwwgnfrln wavdrtgkwq eleypspayp afacgsgyvi
      421 skdivdwlag nsrrlktyqg edvsmgiwma aigpkrhqds lwlcektcet gmlsspqysp
      481 eelsklwelk elcgdpcqce akvr
//
LOCUS       NP_660355                441 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 485 isoform a [Homo sapiens].
ACCESSION   NP_660355
VERSION     NP_660355.2
DBSOURCE    REFSEQ: accession NM_145312.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK074679.1 and BC014161.2.
            
            On Aug 29, 2008 this sequence version replaced NP_660355.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 all encode the same isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: CA394799.1, AK074679.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361807.8/ ENSP00000354694.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.21"
     Protein         1..441
                     /product="zinc finger protein 485 isoform a"
                     /note="Zinc finger protein 93 (Zinc finger protein HTF34)"
                     /calculated_mol_wt=50149
     Region          11..71
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <124..361
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          132..152
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          160..180
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          188..208
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          216..236
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          244..264
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(249,251,253,255..256,259..260,263,277,279,283..284,
                     287..288,291,305,307,309,311..312,315..316,319)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          272..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          356..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(361,363,365,367..368,371..372,375,389,391,395..396,
                     399..400,403,417,419,421,423..424,427..428,431)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          372..393
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          384..404
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          397..419
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          410..432
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          412..432
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..441
                     /gene="ZNF485"
                     /coded_by="NM_145312.4:164..1489"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7205.2"
                     /db_xref="GeneID:220992"
                     /db_xref="HGNC:HGNC:23440"
ORIGIN      
        1 mapraqiqgp ltfgdvavaf triewrhlda aqralyrdvm lenygnlvsv gllsskpkli
       61 tqleqgaepw tevreapsgt havedywfet kmsalkqsts easvlgertk svmmekgldw
      121 egrsstekny kckecgkvfk ynssfishqr nhtsekphkc kecgiafmns ssllnhhkvh
      181 agkqpyrcie cgkflkkhst finhqrihsr ekphkciecg ktfrknsill shqrihtgqk
      241 pykcndcgka faqnaaltrh erihsgekpf kcnkcgrafr dnstvlehqk ihtgekpyqc
      301 necgkafrks stlishqrmh tgekpyhcsk cgksfrysss faghqkthsg nkpyqcrdcg
      361 kaftksstlt ghqrihtgek pyhckkcgka frhssglveh qrlhtgekpy kcnecgkafp
      421 rssalkqhkk ihnkeramkc s
//
LOCUS       NP_071896                800 aa            linear   PRI 27-APR-2025
DEFINITION  nucleolar complex protein 3 homolog [Homo sapiens].
ACCESSION   NP_071896
VERSION     NP_071896.8
DBSOURCE    REFSEQ: accession NM_022451.11
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Jin,H., Kwak,S.H., Yoon,J.W., Lee,S., Park,K.S., Won,S. and
            Cho,N.H.
  TITLE     Genome-Wide Association Study on Longitudinal Change in Fasting
            Plasma Glucose in Korean Population
  JOURNAL   Diabetes Metab J 47 (2), 255-266 (2023)
   PUBMED   36653889
  REMARK    GeneRIF: Genome-Wide Association Study on Longitudinal Change in
            Fasting Plasma Glucose in Korean Population.
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Cheung,M.H., Amin,A., Wu,R., Qin,Y., Zou,L., Yu,Z. and Liang,C.
  TITLE     Human NOC3 is essential for DNA replication licensing in human
            cells
  JOURNAL   Cell Cycle 18 (5), 605-620 (2019)
   PUBMED   30741601
  REMARK    GeneRIF: Knockdown of human NOC3 in HeLa cells abrogates the
            chromatin association of other pre-RC proteins including hCDC6 and
            hMCM, leading to DNA replication defects and eventual apoptosis in
            an abortive S-phase. Human NOC3 physically interacts with multiple
            human pre-replicative complex (pre-RC) proteins and associates with
            known replication origins throughout the cell cycle.
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Duan,X., Li,X., Lou,H., Geng,T., Jin,T., Liang,P., Li,S., Long,Y.
            and Chen,C.
  TITLE     Genetic association of PLCE1, C11orf92-C11orf93, and NOC3L with
            colorectal cancer risk in the Han population
  JOURNAL   Tumour Biol 35 (3), 1813-1817 (2014)
   PUBMED   24146276
  REMARK    GeneRIF: We found PLCE1, C11orf92-C11orf93, and NOC3L associated
            with colorectal cancer susceptibility
REFERENCE   4  (residues 1 to 800)
  AUTHORS   Yuan,L.J., Jin,T.B., Yin,J.K., Du,X.L., Wang,Q., Dong,R.,
            Wang,S.Z., Cui,Y., Chen,C. and Lu,J.G.
  TITLE     Polymorphisms of tumor-related genes IL-10, PSCA, MTRR and NOC3L
            are associated with the risk of gastric cancer in the Chinese Han
            population
  JOURNAL   Cancer Epidemiol 36 (6), e366-e372 (2012)
   PUBMED   22796266
  REMARK    GeneRIF: Results indicate the importance of four gastric cancer
            susceptibility polymorphisms of IL-10, NOC3L, PSCA and MTRR in the
            Chinese Han population.
REFERENCE   5  (residues 1 to 800)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 800)
  AUTHORS   Abnet,C.C., Freedman,N.D., Hu,N., Wang,Z., Yu,K., Shu,X.O.,
            Yuan,J.M., Zheng,W., Dawsey,S.M., Dong,L.M., Lee,M.P., Ding,T.,
            Qiao,Y.L., Gao,Y.T., Koh,W.P., Xiang,Y.B., Tang,Z.Z., Fan,J.H.,
            Wang,C., Wheeler,W., Gail,M.H., Yeager,M., Yuenger,J.,
            Hutchinson,A., Jacobs,K.B., Giffen,C.A., Burdett,L., Fraumeni,J.F.
            Jr., Tucker,M.A., Chow,W.H., Goldstein,A.M., Chanock,S.J. and
            Taylor,P.R.
  TITLE     A shared susceptibility locus in PLCE1 at 10q23 for gastric
            adenocarcinoma and esophageal squamous cell carcinoma
  JOURNAL   Nat Genet 42 (9), 764-767 (2010)
   PUBMED   20729852
REFERENCE   7  (residues 1 to 800)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   8  (residues 1 to 800)
  AUTHORS   Johmura,Y., Osada,S., Nishizuka,M. and Imagawa,M.
  TITLE     FAD24, a regulator of adipogenesis, is required for the regulation
            of DNA replication in cell proliferation
  JOURNAL   Biol Pharm Bull 31 (6), 1092-1095 (2008)
   PUBMED   18520036
REFERENCE   9  (residues 1 to 800)
  AUTHORS   Tominaga,K., Johmura,Y., Nishizuka,M. and Imagawa,M.
  TITLE     Fad24, a mammalian homolog of Noc3p, is a positive regulator in
            adipocyte differentiation
  JOURNAL   J Cell Sci 117 (Pt 25), 6217-6226 (2004)
   PUBMED   15564382
  REMARK    GeneRIF: Fad24, a mammalian homolog of Noc3p, is a positive
            regulator in adipocyte differentiation.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX505710.1, AK091246.1, BC049850.1 and AI632144.1.
            
            On May 16, 2002 this sequence version replaced NP_071896.7.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC049850.1, AK091246.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371361.3/ ENSP00000360412.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.33"
     Protein         1..800
                     /product="nucleolar complex protein 3 homolog"
                     /note="NOC3 protein homolog; factor for adipocyte
                     differentiation 24; nucleolar complex-associated protein
                     3-like protein; nucleolar complex associated 3 homolog;
                     NOC3L DNA replication regulator"
                     /calculated_mol_wt=92417
     Region          27..93
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WTT2.1)"
     Region          113..711
                     /region_name="NOC3"
                     /note="Protein involved in the nuclear export of
                     pre-ribosomes [Translation, ribosomal structure and
                     biogenesis / Intracellular trafficking and secretion];
                     COG5117"
                     /db_xref="CDD:227447"
     Region          160..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WTT2.1)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WTT2.1)"
     CDS             1..800
                     /gene="NOC3L"
                     /gene_synonym="AD24; C10orf117; FAD24"
                     /coded_by="NM_022451.11:102..2504"
                     /db_xref="CCDS:CCDS7433.1"
                     /db_xref="GeneID:64318"
                     /db_xref="HGNC:HGNC:24034"
                     /db_xref="MIM:610769"
ORIGIN      
        1 mkarrnkkqi psfrklikts kvklenklkn kqfkqqstlk kyrkeqrklr qavkdavskk
       61 piplenpkek rpgkrieree eeeeealpld mmdeddlqlm kdlgqrvsfl trdlsssepv
      121 hakkrkheri idkyekiprt lqtapekeli hllpikdksg iipqtrekpv tdsnkdeedq
      181 eeereleeei iedpiqelti eehlierkkk lqekkmhiaa lasailsdpe nnikklkelr
      241 smlmeqdpdv avtvrklviv slmelfkdit psykirplte aekstktrke tqklrefeeg
      301 lvsqykfyle nleqmvkdwk qrklkksnvv slkaykglae vavkslcell valphfnfhn
      361 niivlivplm ndmsklisem cceavkklfk qdklgqaslg vikvisgfvk grnyevrpem
      421 lktflclrik evevkkdted inkpkkfmtf kekrkslsrm qrkwkkaeek lerelreaea
      481 sestekklkl htetlnivfv tyfrilkkaq rspllpavle glakfahlin veffddllvv
      541 lhtliesgdl syqeslhcvq tafhilsgqg dvlnidplkf ythlyktlfk lhagatnegv
      601 eivlqcldvm ltkrrkqvsq qralafikrl ctlalhvlpn ssigilattr ilmhtfpktd
      661 llldsesqgs gvflpeldep eycnaqntal welhalrrhy hpivqrfaah liagapsegs
      721 galkpelsrr satelfeays maemtfnppv essnpkikgk flqgdsflne dlnqlikrys
      781 sevatespld ftkylktslh
//
LOCUS       NP_116213                555 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 87B isoform 1 precursor [Homo sapiens].
ACCESSION   NP_116213
VERSION     NP_116213.1
DBSOURCE    REFSEQ: accession NM_032824.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Hoel,C.M., Zhang,L. and Brohawn,S.G.
  TITLE     Structure of the GOLD-domain seven-transmembrane helix protein
            family member TMEM87A
  JOURNAL   Elife 11, e81704 (2022)
   PUBMED   36373655
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Yu,H.C., Coughlin,C.R., Geiger,E.A., Salvador,B.J., Elias,E.R.,
            Cavanaugh,J.L., Chatfield,K.C., Miyamoto,S.D. and Shaikh,T.H.
  TITLE     Discovery of a potentially deleterious variant in TMEM87B in a
            patient with a hemizygous 2q13 microdeletion suggests a recessive
            condition characterized by congenital heart disease and restrictive
            cardiomyopathy
  JOURNAL   Cold Spring Harb Mol Case Stud 2 (3), a000844 (2016)
   PUBMED   27148590
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Riley,K.N., Catalano,L.M., Bernat,J.A., Adams,S.D., Martin,D.M.,
            Lalani,S.R., Patel,A., Burnside,R.D., Innis,J.W. and Rudd,M.K.
  TITLE     Recurrent deletions and duplications of chromosome 2q11.2 and 2q13
            are associated with variable outcomes
  JOURNAL   Am J Med Genet A 167A (11), 2664-2673 (2015)
   PUBMED   26227573
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Hirata,T., Fujita,M., Nakamura,S., Gotoh,K., Motooka,D.,
            Murakami,Y., Maeda,Y. and Kinoshita,T.
  TITLE     Post-Golgi anterograde transport requires GARP-dependent
            endosome-to-TGN retrograde transport
  JOURNAL   Mol Biol Cell 26 (17), 3071-3084 (2015)
   PUBMED   26157166
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Hladilkova,E., Baroy,T., Fannemel,M., Vallova,V., Misceo,D.,
            Bryn,V., Slamova,I., Prasilova,S., Kuglik,P. and Frengen,E.
  TITLE     A recurrent deletion on chromosome 2q13 is associated with
            developmental delay and mild facial dysmorphisms
  JOURNAL   Mol Cytogenet 8, 57 (2015)
   PUBMED   26236398
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Russell,M.W., Raeker,M.O., Geisler,S.B., Thomas,P.E., Simmons,T.A.,
            Bernat,J.A., Thorsson,T. and Innis,J.W.
  TITLE     Functional analysis of candidate genes in 2q13 deletion syndrome
            implicates FBLN7 and TMEM87B deficiency in congenital heart defects
            and FBLN7 in craniofacial malformations
  JOURNAL   Hum Mol Genet 23 (16), 4272-4284 (2014)
   PUBMED   24694933
  REMARK    GeneRIF: Heterozygous loss of FBLN7 and TMEM87B account for some of
            the clinical features, including cardiac defects and craniofacial
            abnormalities associated with 2q13 deletion syndrome.
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Li,S., Liu,P., Xi,L., Jiang,X., Wu,M., Deng,D., Wei,J., Zhu,T.,
            Zhou,L., Wang,S., Xu,G., Meng,L., Zhou,J. and Ma,D.
  TITLE     Expression of TMEM87B interacting with the human papillomavirus
            type 18 E6 oncogene in the Hela cDNA library by a yeast two-hybrid
            system
  JOURNAL   Oncol Rep 20 (2), 421-427 (2008)
   PUBMED   18636207
REFERENCE   8  (residues 1 to 555)
  AUTHORS   Johnson,J.M., Castle,J., Garrett-Engele,P., Kan,Z., Loerch,P.M.,
            Armour,C.D., Santos,R., Schadt,E.E., Stoughton,R. and
            Shoemaker,D.D.
  TITLE     Genome-wide survey of human alternative pre-mRNA splicing with exon
            junction microarrays
  JOURNAL   Science 302 (5653), 2141-2144 (2003)
   PUBMED   14684825
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA550235.1, AK027587.1,
            AK074243.1, AC092645.2 and AI806006.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that may interact with human
            papillomavirus type 18 E6 oncogene. The protein is also likely to
            be involved in endosome-to-trans-Golgi network retrograde
            transport. The gene is expressed in adult and fetal tissues,
            including brain and heart. This gene is a component of the 2q13
            deletion syndrome. Mutations in this gene may be associated with
            congenital heart defects. [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.263269.1,
                                           SRR1660807.261290.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283206.9/ ENSP00000283206.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..555
                     /product="transmembrane protein 87B isoform 1 precursor"
                     /calculated_mol_wt=58948
     sig_peptide     1..42
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4607
     mat_peptide     43..555
                     /product="Transmembrane protein 87B. /id=PRO_0000291753"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K49.1)"
                     /calculated_mol_wt=58948
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K49.1)"
     Region          174..458
                     /region_name="Lung_7-TM_R"
                     /note="Lung seven transmembrane receptor; pfam06814"
                     /db_xref="CDD:369089"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            248..268
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            300..320
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            397..417
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            430..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96K49.1)"
     Site            534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96K49.1)"
     CDS             1..555
                     /gene="TMEM87B"
                     /coded_by="NM_032824.3:324..1991"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS33275.1"
                     /db_xref="GeneID:84910"
                     /db_xref="HGNC:HGNC:25913"
                     /db_xref="MIM:617203"
ORIGIN      
        1 mvaacrsvag llprrrrcfp arapllrval cllcwtpaav ravpelglwl etvndksgpl
       61 ifrktmfnst diklsvksfh csgpvkftiv whlkyhtchn ehsnleelfq khklsvdedf
      121 chylkndncw ttknenldcn sdsqvfpsln nkelinirnv snqersmdvv artqkdgfhi
      181 fivsiktent daswnlnvsl smigphgyis asdwplmify mvmcivyily gilwltwsac
      241 ywkdilriqf wiaaviflgm lekavfysey qnisntglst qgllifaeli saikrtlarl
      301 lviivslgyg ivkprlgtvm hrviglglly lifaavegvm rviggsnhla vvlddiilav
      361 idsifvwfif islaqtmktl rlrkntvkfs lyrhfkntli favlasivfm gwttktfria
      421 kcqsdwmerw vddafwsflf slilivimfl wrpsannqry afmpliddsd deieefmvts
      481 enltegiklr asksvsngta kpatsenfde dlkwveenip ssftdvalpv lvdsdeeimt
      541 rsemaekmfs sekim
//
LOCUS       NP_055888               1781 aa            linear   PRI 27-APR-2025
DEFINITION  signal-induced proliferation-associated 1-like protein 3 [Homo
            sapiens].
ACCESSION   NP_055888 XP_032278
VERSION     NP_055888.1
DBSOURCE    REFSEQ: accession NM_015073.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1781)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   2  (residues 1 to 1781)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1781)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1781)
  AUTHORS   Zhang,R., Lai,L., Dong,X., He,J., You,D., Chen,C., Lin,L., Zhu,Y.,
            Huang,H., Shen,S., Wei,L., Chen,X., Guo,Y., Liu,L., Su,L.,
            Shafer,A., Moran,S., Fleischer,T., Bjaanaes,M.M., Karlsson,A.,
            Planck,M., Staaf,J., Helland,A., Esteller,M., Wei,Y., Chen,F. and
            Christiani,D.C.
  TITLE     SIPA1L3 methylation modifies the benefit of smoking cessation on
            lung adenocarcinoma survival: an epigenomic-smoking interaction
            analysis
  JOURNAL   Mol Oncol 13 (5), 1235-1248 (2019)
   PUBMED   30924596
  REMARK    GeneRIF: smoking cessation benefited survival of LUAD patients with
            low methylation at cg02268510SIPA 1L3 . The results have
            implications for not only smoking cessation after diagnosis, but
            also possible methylation-specific drug targeting.
REFERENCE   5  (residues 1 to 1781)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 1781)
  AUTHORS   Evers,C., Paramasivam,N., Hinderhofer,K., Fischer,C., Granzow,M.,
            Schmidt-Bacher,A., Eils,R., Steinbeisser,H., Schlesner,M. and
            Moog,U.
  TITLE     SIPA1L3 identified by linkage analysis and whole-exome sequencing
            as a novel gene for autosomal recessive congenital cataract
  JOURNAL   Eur J Hum Genet 23 (12), 1627-1633 (2015)
   PUBMED   25804400
  REMARK    GeneRIF: Whole-exome sequencing identified a homozygous nonsense
            variant in SIPA1L3 in two sisters with congenital cataract.
REFERENCE   7  (residues 1 to 1781)
  AUTHORS   Greenlees,R., Mihelec,M., Yousoof,S., Speidel,D., Wu,S.K.,
            Rinkwitz,S., Prokudin,I., Perveen,R., Cheng,A., Ma,A., Nash,B.,
            Gillespie,R., Loebel,D.A., Clayton-Smith,J., Lloyd,I.C.,
            Grigg,J.R., Tam,P.P., Yap,A.S., Becker,T.S., Black,G.C., Semina,E.
            and Jamieson,R.V.
  TITLE     Mutations in SIPA1L3 cause eye defects through disruption of cell
            polarity and cytoskeleton organization
  JOURNAL   Hum Mol Genet 24 (20), 5789-5804 (2015)
   PUBMED   26231217
  REMARK    GeneRIF: Abnormalities of SIPA1L3 contribute to lens and eye
            defects, and we identify a critical role for SIPA1L3 in epithelial
            cell morphogenesis, polarity, adhesion and cytoskeletal
            organization.
REFERENCE   8  (residues 1 to 1781)
  AUTHORS   Spilker,C. and Kreutz,M.R.
  TITLE     RapGAPs in brain: multipurpose players in neuronal Rap signalling
  JOURNAL   Eur J Neurosci 32 (1), 1-9 (2010)
   PUBMED   20576033
  REMARK    Review article
REFERENCE   9  (residues 1 to 1781)
  AUTHORS   Benzinger,A., Muster,N., Koch,H.B., Yates,J.R. 3rd and Hermeking,H.
  TITLE     Targeted proteomic analysis of 14-3-3 sigma, a p53 effector
            commonly silenced in cancer
  JOURNAL   Mol Cell Proteomics 4 (6), 785-795 (2005)
   PUBMED   15778465
REFERENCE   10 (residues 1 to 1781)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016582.9, BM193478.1,
            BC150620.1, AC011465.4, AC011479.7 and AI560928.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 27, 2005 this sequence version replaced XP_032278.5.
            
            Summary: This gene belongs to the signal induced proliferation
            associated 1 family of genes, which encode GTPase-activating
            proteins specific for the GTP-binding protein Rap1. Rap1 has been
            implicated in regulation of cell adhesion, cell polarity, and
            organization of the cytoskeleton. Like other members of the family,
            the protein encoded by this gene contains RapGAP and PDZ domains.
            In addition, this protein contains a C-terminal leucine zipper
            domain. This gene is proposed to function in epithelial cell
            morphogenesis and establishment or maintenance of polarity.
            Consistently, expression of the protein in cell culture showed
            localization to cell-cell borders in apical regions, and
            downregulation of the gene in 3D Caco2 cell culture resulted in
            abnormal cell polarity and morphogenesis. Allelic variants of this
            gene have been associated with congenital cataracts in humans.
            [provided by RefSeq, Feb 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150620.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222345.11/ ENSP00000222345.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1781
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.13-q13.2"
     Protein         1..1781
                     /product="signal-induced proliferation-associated 1-like
                     protein 3"
                     /note="SIPA1-like protein 3; SPA-1-like protein 3;
                     spine-associated RapGAP 3"
                     /calculated_mol_wt=194480
     Region          45..166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60292.3)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G3X9J0; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G3X9J0; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Region          239..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60292.3)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Region          641..821
                     /region_name="Rap_GAP"
                     /note="Rap/ran-GAP; pfam02145"
                     /db_xref="CDD:460463"
     Region          966..1038
                     /region_name="PDZ_SIPA1-like"
                     /note="PDZ domain of signal-induced
                     proliferation-associated protein 1 (SIPA1), and related
                     domains; cd06745"
                     /db_xref="CDD:467227"
     Site            order(976..982,988,991,1020,1024,1027..1028)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467227"
     Region          1046..1112
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60292.3)"
     Region          <1064..1490
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1124..1221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60292.3)"
     Region          1236..1565
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60292.3)"
     Site            1364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Site            1387
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:G3X9J0; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Site            1448
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Region          1477..1726
                     /region_name="SPAR_C"
                     /note="C-terminal domain of SPAR protein; pfam11881"
                     /db_xref="CDD:463383"
     Site            1544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Site            1547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G3X9J0; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Region          1583..1636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60292.3)"
     Site            1619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G3X9J0; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Site            1622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G3X9J0; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Site            1677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G3X9J0; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Region          1685..1712
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60292.3)"
     Site            1699
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     Site            1703
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:G3X9J0; propagated from
                     UniProtKB/Swiss-Prot (O60292.3)"
     CDS             1..1781
                     /gene="SIPA1L3"
                     /gene_synonym="CTRCT45; SPAL3; SPAR3"
                     /coded_by="NM_015073.3:530..5875"
                     /db_xref="CCDS:CCDS33007.1"
                     /db_xref="GeneID:23094"
                     /db_xref="HGNC:HGNC:23801"
                     /db_xref="MIM:616655"
ORIGIN      
        1 mttyraipsd gvdlaascga rvgdvlpgph tgdyaplgfw aqngsmsqpl gespatatat
       61 atattrpspt tpampkmgvr arvadwppkr ealrehsnps psqdtdgtka tkmahsmrsi
      121 qngqpptstp assgskafhr lsrrrskdve fqdgwprspg raflplrhrs sseitlsecd
      181 aedageprga rhtgalplfr eygstssidv qgmpeqsffd ilnefrseqp dargcqalte
      241 llradpgphl mgggggakgd shngqpakds llplqptkek ekarkkparg lgggdtvdss
      301 ifrklrsskp egeagrspge adegrsppea srpwvcqksf ahfdvqsmlf dlneaaanrv
      361 svsqrrnttt gasaasaasa masltasrah slggldpaft stedlncken leqdlgddns
      421 ndlllscphf rneiggecer nvsfsrasvg spssgeghla epalsayrtn asisvlevpk
      481 eqqrtqsrpr qysiehvdlg aryyqdyfvg kehanyfgvd eklgpvavsi krekledhke
      541 hgpqyqyrii frtrelitlr gsiledatpt atkhgtgrgl plkdaleyvi pelnihclrl
      601 alntpkvteq llkldeqglc rkhkvgilyc kagqsseeem ynneeagpaf eeflsligek
      661 vclkgftkya aqldvktdst gthslytmyq dyeimfhvst llpytpnnrq qllrkrhign
      721 divtiifqep galpftpkni rshfqhvfii vrvhnpctdn vcysmavtrs kdappfgppi
      781 psgttfrksd vfrdfllakv inaenaahks dkfhtmatrt rqeylkdlae ncvsntpids
      841 tgkfnlislt skkkektkar agaeqhsaga iawrvvaqdy aqgveidcil gisnefvvll
      901 dlrtkevvfn cycgdvigwt pdsstlkify grgdhiflqa tegsvedire ivqrlkvmts
      961 gwetvdmtlr rnglgqlgfh vkydgtvaev edygfawqag lrqgsrlvei ckvavvtlth
     1021 dqmidllrts vtvkvviipp fedgtprrgw petydmntse pkteqesitp ggrppyrsna
     1081 pwqwsgpash nslpaskwat pttpghaqsl srplkqtpiv pfresqplhs krpvsfpetp
     1141 ytvspagadr vppyrqpsgs fstpgsatyv rykpsperyt aaphpllsld phfshdgtss
     1201 gdsssgglts qestmerqkp eplwhvpaqa rlsaiagssg nkhpsrqdaa gkdspnrhsk
     1261 gepqysshss sntlssnass shsddrwfdp ldplepeqdp lskggssdsg idttlytssp
     1321 scmslakapr pakphkppgs mglcgggrea agrshhadrr revspapava gqskgyrpkl
     1381 yssgsstptg laggsrdppr qpsdmgsrvg ypaqvyktas aetprpsqla qpspfqlsas
     1441 vpksffskqp vrnkhptgwk rteeppprpl pfsdpkkqvd tntknvfgqp rlraslrdlr
     1501 sprknyksti eddlkkliim dnlgpeqerd tgqspqkglq rtlsdeslcs grrepsfasp
     1561 aglepglpsd vlftstcafp sstlparrqh qhphppvgpg atpaagsgfp ekkstisase
     1621 lsladgrdrp lrrldpglmp lpdtaaglew sslvnaakay evqravslfs lndpalspdi
     1681 ppahspvhsh lslergpptp rttptmseep pldltgkvyq levmlkqlht dlqkekqdkv
     1741 vlqsevaslr qnnqrlqees qaaseqlrkf aeifcrekke l
//
LOCUS       NP_001355553            2434 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-binding cassette sub-family A member 2 isoform 2 [Mus
            musculus].
ACCESSION   NP_001355553 XP_006497675
VERSION     NP_001355553.1
DBSOURCE    REFSEQ: accession NM_001368624.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 2434)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 2434)
  AUTHORS   Davis,W. Jr.
  TITLE     The ATP-Binding Cassette Transporter-2 (ABCA2) Overexpression
            Modulates Sphingosine Levels and Transcription of the Amyloid
            Precursor Protein (APP) Gene
  JOURNAL   Curr Alzheimer Res 12 (9), 847-859 (2015)
   PUBMED   26510981
  REMARK    GeneRIF: Study suggests that ABCA2 modulation of sphingolipid
            metabolism activates a signaling pathway that regulates amyloid
            precursor protein transcription
REFERENCE   3  (residues 1 to 2434)
  AUTHORS   Thompson,C.L., Ng,L., Menon,V., Martinez,S., Lee,C.K.,
            Glattfelder,K., Sunkin,S.M., Henry,A., Lau,C., Dang,C.,
            Garcia-Lopez,R., Martinez-Ferre,A., Pombero,A., Rubenstein,J.L.R.,
            Wakeman,W.B., Hohmann,J., Dee,N., Sodt,A.J., Young,R., Smith,K.,
            Nguyen,T.N., Kidney,J., Kuan,L., Jeromin,A., Kaykas,A., Miller,J.,
            Page,D., Orta,G., Bernard,A., Riley,Z., Smith,S., Wohnoutka,P.,
            Hawrylycz,M.J., Puelles,L. and Jones,A.R.
  TITLE     A high-resolution spatiotemporal atlas of gene expression of the
            developing mouse brain
  JOURNAL   Neuron 83 (2), 309-323 (2014)
   PUBMED   24952961
REFERENCE   4  (residues 1 to 2434)
  AUTHORS   Haller,J.F., Cavallaro,P., Hernandez,N.J., Dolat,L., Soscia,S.J.,
            Welti,R., Grabowski,G.A., Fitzgerald,M.L. and Freeman,M.W.
  TITLE     Endogenous beta-glucocerebrosidase activity in Abca12/epidermis
            elevates ceramide levels after topical lipid application but does
            not restore barrier function
  JOURNAL   J Lipid Res 55 (3), 493-503 (2014)
   PUBMED   24293640
REFERENCE   5  (residues 1 to 2434)
  AUTHORS   Davis,W. Jr.
  TITLE     The ATP-binding cassette transporter-2 (ABCA2) regulates
            esterification of plasma membrane cholesterol by modulation of
            sphingolipid metabolism
  JOURNAL   Biochim Biophys Acta 1841 (1), 168-179 (2014)
   PUBMED   24201375
  REMARK    GeneRIF: control of ABCA2 expression level may be a key locus of
            regulation for esterification of plasma membrane-derived
            cholesterol through modulation of sphingolipid metabolism.
REFERENCE   6  (residues 1 to 2434)
  AUTHORS   Kasahara,M., Hayashi,M., Tanaka,K., Inoko,H., Sugaya,K., Ikemura,T.
            and Ishibashi,T.
  TITLE     Chromosomal localization of the proteasome Z subunit gene reveals
            an ancient chromosomal duplication involving the major
            histocompatibility complex
  JOURNAL   Proc Natl Acad Sci U S A 93 (17), 9096-9101 (1996)
   PUBMED   8799160
REFERENCE   7  (residues 1 to 2434)
  AUTHORS   Allikmets,R., Gerrard,B., Glavac,D., Ravnik-Glavac,M.,
            Jenkins,N.A., Gilbert,D.J., Copeland,N.G., Modi,W. and Dean,M.
  TITLE     Characterization and mapping of three new mammalian ATP-binding
            transporter genes from an EST database
  JOURNAL   Mamm Genome 6 (2), 114-117 (1995)
   PUBMED   7766993
REFERENCE   8  (residues 1 to 2434)
  AUTHORS   Pilz,A., Woodward,K., Povey,S. and Abbott,C.
  TITLE     Comparative mapping of 50 human chromosome 9 loci in the laboratory
            mouse
  JOURNAL   Genomics 25 (1), 139-149 (1995)
   PUBMED   7774911
REFERENCE   9  (residues 1 to 2434)
  AUTHORS   Luciani,M.F., Denizot,F., Savary,S., Mattei,M.G. and Chimini,G.
  TITLE     Cloning of two novel ABC transporters mapping on human chromosome 9
  JOURNAL   Genomics 21 (1), 150-159 (1994)
   PUBMED   8088782
REFERENCE   10 (residues 1 to 2434)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: from microorganisms to man
  JOURNAL   Annu Rev Cell Biol 8, 67-113 (1992)
   PUBMED   1282354
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CJ126415.1, AK169438.1, AL732557.4 and CJ263864.1.
            
            On Feb 12, 2019 this sequence version replaced XP_006497675.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849374,
                              SAMN00849375 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2434
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 17.25 cM"
     Protein         1..2434
                     /product="ATP-binding cassette sub-family A member 2
                     isoform 2"
                     /note="ATP-binding cassette transporter 2; ATP-binding
                     cassette 2; ATP-binding cassette, sub-family A (ABC1),
                     member 2"
                     /calculated_mol_wt=270510
     Region          1..2368
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     CDS             1..2434
                     /gene="Abca2"
                     /gene_synonym="Abc2; D2H0S1474E; mKIAA1062"
                     /coded_by="NM_001368624.1:172..7476"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:11305"
                     /db_xref="MGI:MGI:99606"
ORIGIN      
        1 mgflhqlqll lwknvtlkrr spwvlafeif iplvlffill glrqkkptis vkevsfytaa
       61 pltsagilpv mqslcpdgqr defgflqyan stvtqllerl hrvveegnlf dpvrpslgse
      121 lealrqrlea lssgpgtwes hsarpavssf sldsvardqr elwrflmqnl slpnstaqal
      181 laarvdpsev yrllfgplpd ldgklgflrk qepwsrlgsn pllqmeelll apalleqltc
      241 apgsgelgri ltmpeghqvd lqgyrdavcs gqataraqrf sdlaaelrnq ldtakiaqql
      301 gfdvpngsdp qpqapspqsl pallgdllda qkllqdvdvl salalllpqg acagqasapq
      361 asslnglans tgigansgsn ttveegtqsp vspaspdtlq gqcsafvqlw aglqpilcgn
      421 nrtiepealr rgnmsslgft skeqrnlgll vhlmtsnpki lyapvgsead rvilkanetf
      481 afvgnvthya qvwlnistei rsfleqgrlq qhlqwlqqyv adlqlhpeam nlsleelppa
      541 lrqdfslpng tallqqldti dnaacgwiqf mskvsvdifk gfpdeesivn ytlnqayqdn
      601 vtvfasvifq trkdgslpph vhykirqnss ftektneirr aywrpgpntg grfyflygfv
      661 wiqdmmerai intfvghdvv epgnyvqmfp ypcytrddfl fviehmmplc mviswvysva
      721 mtiqhivaek ehrlkevmkt mglnnavhwv awfitgfvql sisvtaltai lkygqvlmhs
      781 hvliiwlfla vyavatimfc flvsvlyska klasacggii yflsyvpymy vaireevahd
      841 kitafekcia slmsttafgl gskyfalyev agvgiqwhtf sqspvegddf nlllavtmlm
      901 vdtvvygvlt wyieavhpgm yglprpwyfp lqksywlgsg rteawewswp wahtprlsvm
      961 eedqacames rhfeetrgme eepthlplvv cvdkltkvyk ndkkmalnkl slnlyenqvv
     1021 sflghngagk tttmsiltgl fpptsgsati yghdirtemd eirknlgmcp qhnvlfdrlt
     1081 veehlwfysr lksmaqeeir ketdkmiedl elsnkrhslv qtlsggmkrk lsvaiafvgg
     1141 sraiildept agvdpyarra iwdlilkykp grtillsthh mdeadllgdr iaiishgklk
     1201 ccgsplflkg aygdgyrltl vkqpaepgts qepglassps gcprlsscse pqvsqfirkh
     1261 vassllvsdt stelsyilps eavkkgafer lfqqlehsld alhlssfglm dttleevflk
     1321 vseedqslen seadvkesrk dvlpgaeglt avggqagnla rcselaqsqa slqsassvgs
     1381 argeegtgys dgygdyrplf dnlqdpdnvs lqeaemeala qvgqgsrkle gwwlkmrqfh
     1441 gllvkrfhca rrnskalcsq illpaffvcv amtvalsvpe igdlpplvls psqyhnytqp
     1501 rgnfipyane erqeyrlrls pdaspqqlvs tfrlpsgvga tcvlkspang slgpmlnlss
     1561 gesrllaarf fdsmclesft qglplsnfvp pppspapsds pvspdedslq awnmslppta
     1621 gpetwtsaps lprlvhepvr ctcsaqgtgf scpssvgghp pqmrvvtgdi ltditghnvs
     1681 eyllftsdrf rlhrygaitf gnvqksipas fgarvppmvr kiavrrvaqv lynnkgyhsm
     1741 ptylnslnna ilranlpksk gnpaaygitv tnhpmnktsa slsldyllqg tdvviaifii
     1801 vamsfvpasf vvflvaekst kakhlqfvsg cnpviywlan yvwdmlnylv patccviilf
     1861 vfdlpaytsp tnfpavlslf llygwsitpi mypasfwfev pssayvfliv inlfigitat
     1921 vatfllqlfe hdkdlkvvns ylkscflifp nynlghglme mayneyiney yakigqfdkm
     1981 kspfewdivt rglvamtveg fvgffltimc qynflrqpqr lpvstkpved dvdvaserqr
     2041 vlrgdadndm vkienltkvy ksrkigrila vdrlclgvrp gecfgllgvn gagktstfkm
     2101 ltgdesttgg eafvnghsvl kdllqvqqsl gycpqfdalf deltarehlq lytrlrgipw
     2161 kdeaqvvkwa lekleltkya dkpagtysgg nkrklstaia ligypafifl depttgmdpk
     2221 arrflwnlil dliktgrsvv ltshsmeece alctrlaimv ngrlrclgsi qhlknrfgdg
     2281 ymitvrtkss qnvkdvvrff nrnfpeamlk erhhtkvqyq lksehislaq vfskmeqvvg
     2341 vlgiedysvs qttldnvfvn fakkqsdnve qqeaepsslp splgllsllr prpaptelra
     2401 lvadepedld tedeglisfe eeraqlsfnt dtlc
//
LOCUS       NP_060312                146 aa            linear   PRI 27-APR-2025
DEFINITION  heme transporter HRG1 [Homo sapiens].
ACCESSION   NP_060312
VERSION     NP_060312.2
DBSOURCE    REFSEQ: accession NM_017842.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Fogarty,F.M., O'Keeffe,J., Zhadanov,A., Papkovsky,D., Ayllon,V. and
            O'Connor,R.
  TITLE     HRG-1 enhances cancer cell invasive potential and couples glucose
            metabolism to cytosolic/extracellular pH gradient regulation by the
            vacuolar-H(+) ATPase
  JOURNAL   Oncogene 33 (38), 4653-4663 (2014)
   PUBMED   24141772
  REMARK    GeneRIF: HRG-1 may represent a novel target for selectively
            disrupting V-ATPase activity and the metastatic potential of cancer
            cells.
REFERENCE   3  (residues 1 to 146)
  AUTHORS   White,C., Yuan,X., Schmidt,P.J., Bresciani,E., Samuel,T.K.,
            Campagna,D., Hall,C., Bishop,K., Calicchio,M.L., Lapierre,A.,
            Ward,D.M., Liu,P., Fleming,M.D. and Hamza,I.
  TITLE     HRG1 is essential for heme transport from the phagolysosome of
            macrophages during erythrophagocytosis
  JOURNAL   Cell Metab 17 (2), 261-270 (2013)
   PUBMED   23395172
  REMARK    GeneRIF: These results reveal HRG1 as the long-sought heme
            transporter for heme-iron recycling in macrophages and suggest that
            genetic variations in HRG1 could be modifiers of human iron
            metabolism.
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Kottgen,A., Albrecht,E., Teumer,A., Vitart,V., Krumsiek,J.,
            Hundertmark,C., Pistis,G., Ruggiero,D., O'Seaghdha,C.M., Haller,T.,
            Yang,Q., Tanaka,T., Johnson,A.D., Kutalik,Z., Smith,A.V., Shi,J.,
            Struchalin,M., Middelberg,R.P., Brown,M.J., Gaffo,A.L., Pirastu,N.,
            Li,G., Hayward,C., Zemunik,T., Huffman,J., Yengo,L., Zhao,J.H.,
            Demirkan,A., Feitosa,M.F., Liu,X., Malerba,G., Lopez,L.M., van der
            Harst,P., Li,X., Kleber,M.E., Hicks,A.A., Nolte,I.M., Johansson,A.,
            Murgia,F., Wild,S.H., Bakker,S.J., Peden,J.F., Dehghan,A.,
            Steri,M., Tenesa,A., Lagou,V., Salo,P., Mangino,M., Rose,L.M.,
            Lehtimaki,T., Woodward,O.M., Okada,Y., Tin,A., Muller,C.,
            Oldmeadow,C., Putku,M., Czamara,D., Kraft,P., Frogheri,L.,
            Thun,G.A., Grotevendt,A., Gislason,G.K., Harris,T.B., Launer,L.J.,
            McArdle,P., Shuldiner,A.R., Boerwinkle,E., Coresh,J., Schmidt,H.,
            Schallert,M., Martin,N.G., Montgomery,G.W., Kubo,M., Nakamura,Y.,
            Tanaka,T., Munroe,P.B., Samani,N.J., Jacobs,D.R. Jr., Liu,K.,
            D'Adamo,P., Ulivi,S., Rotter,J.I., Psaty,B.M., Vollenweider,P.,
            Waeber,G., Campbell,S., Devuyst,O., Navarro,P., Kolcic,I.,
            Hastie,N., Balkau,B., Froguel,P., Esko,T., Salumets,A., Khaw,K.T.,
            Langenberg,C., Wareham,N.J., Isaacs,A., Kraja,A., Zhang,Q.,
            Wild,P.S., Scott,R.J., Holliday,E.G., Org,E., Viigimaa,M.,
            Bandinelli,S., Metter,J.E., Lupo,A., Trabetti,E., Sorice,R.,
            Doring,A., Lattka,E., Strauch,K., Theis,F., Waldenberger,M.,
            Wichmann,H.E., Davies,G., Gow,A.J., Bruinenberg,M., Stolk,R.P.,
            Kooner,J.S., Zhang,W., Winkelmann,B.R., Boehm,B.O., Lucae,S.,
            Penninx,B.W., Smit,J.H., Curhan,G., Mudgal,P., Plenge,R.M.,
            Portas,L., Persico,I., Kirin,M., Wilson,J.F., Mateo Leach,I., van
            Gilst,W.H., Goel,A., Ongen,H., Hofman,A., Rivadeneira,F.,
            Uitterlinden,A.G., Imboden,M., von Eckardstein,A., Cucca,F.,
            Nagaraja,R., Piras,M.G., Nauck,M., Schurmann,C., Budde,K.,
            Ernst,F., Farrington,S.M., Theodoratou,E., Prokopenko,I.,
            Stumvoll,M., Jula,A., Perola,M., Salomaa,V., Shin,S.Y.,
            Spector,T.D., Sala,C., Ridker,P.M., Kahonen,M., Viikari,J.,
            Hengstenberg,C., Nelson,C.P., Meschia,J.F., Nalls,M.A., Sharma,P.,
            Singleton,A.B., Kamatani,N., Zeller,T., Burnier,M., Attia,J.,
            Laan,M., Klopp,N., Hillege,H.L., Kloiber,S., Choi,H., Pirastu,M.,
            Tore,S., Probst-Hensch,N.M., Volzke,H., Gudnason,V., Parsa,A.,
            Schmidt,R., Whitfield,J.B., Fornage,M., Gasparini,P.,
            Siscovick,D.S., Polasek,O., Campbell,H., Rudan,I., Bouatia-Naji,N.,
            Metspalu,A., Loos,R.J., van Duijn,C.M., Borecki,I.B., Ferrucci,L.,
            Gambaro,G., Deary,I.J., Wolffenbuttel,B.H., Chambers,J.C., Marz,W.,
            Pramstaller,P.P., Snieder,H., Gyllensten,U., Wright,A.F., Navis,G.,
            Watkins,H., Witteman,J.C., Sanna,S., Schipf,S., Dunlop,M.G.,
            Tonjes,A., Ripatti,S., Soranzo,N., Toniolo,D., Chasman,D.I.,
            Raitakari,O., Kao,W.H., Ciullo,M., Fox,C.S., Caulfield,M.,
            Bochud,M. and Gieger,C.
  CONSRTM   LifeLines Cohort Study; CARDIoGRAM Consortium; DIAGRAM Consortium;
            ICBP Consortium; MAGIC Consortium
  TITLE     Genome-wide association analyses identify 18 new loci associated
            with serum urate concentrations
  JOURNAL   Nat Genet 45 (2), 145-154 (2013)
   PUBMED   23263486
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Yuan,X., Protchenko,O., Philpott,C.C. and Hamza,I.
  TITLE     Topologically conserved residues direct heme transport in
            HRG-1-related proteins
  JOURNAL   J Biol Chem 287 (7), 4914-4924 (2012)
   PUBMED   22174408
  REMARK    GeneRIF: a model in which heme is translocated across membranes
            facilitated by conserved amino acids positioned on the exoplasmic,
            cytoplasmic, and transmembrane regions of HRG-1-related proteins.
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 146)
  AUTHORS   O'Callaghan,K.M., Ayllon,V., O'Keeffe,J., Wang,Y., Cox,O.T.,
            Loughran,G., Forgac,M. and O'Connor,R.
  TITLE     Heme-binding protein HRG-1 is induced by insulin-like growth factor
            I and associates with the vacuolar H+-ATPase to control endosomal
            pH and receptor trafficking
  JOURNAL   J Biol Chem 285 (1), 381-391 (2010)
   PUBMED   19875448
  REMARK    GeneRIF: HRG-1 regulates V-ATPase activity, which is essential for
            endosomal acidification, heme binding, and receptor trafficking in
            mammalian cells.
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Rajagopal,A., Rao,A.U., Amigo,J., Tian,M., Upadhyay,S.K., Hall,C.,
            Uhm,S., Mathew,M.K., Fleming,M.D., Paw,B.H., Krause,M. and Hamza,I.
  TITLE     Haem homeostasis is regulated by the conserved and concerted
            functions of HRG-1 proteins
  JOURNAL   Nature 453 (7198), 1127-1131 (2008)
   PUBMED   18418376
  REMARK    GeneRIF: Human and worm proteins localize together, and bind and
            transport haem, thus establishing an evolutionarily conserved
            function for HRG-1.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC026344.1 and AC004466.1.
            
            On Oct 21, 2008 this sequence version replaced NP_060312.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026344.1, SRR1803613.204957.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000442218.3/ ENSP00000415998.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..146
                     /product="heme transporter HRG1"
                     /note="heme-responsive gene 1 protein homolog; solute
                     carrier family 48 (heme transporter), member 1"
                     /calculated_mol_wt=16288
     Site            12..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1K1.1)"
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1K1.1)"
     Region          72..122
                     /region_name="HRG"
                     /note="Haem-transporter, endosomal/lysosomal,
                     haem-responsive gene; pfam16954"
                     /db_xref="CDD:465321"
     Site            74..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1K1.1)"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1K1.1)"
     Region          142..143
                     /region_name="Di-leucine motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1K1.1)"
     CDS             1..146
                     /gene="SLC48A1"
                     /gene_synonym="hHRG-1; HRG; HRG-1; HRG1"
                     /coded_by="NM_017842.3:68..508"
                     /db_xref="CCDS:CCDS8755.2"
                     /db_xref="GeneID:55652"
                     /db_xref="HGNC:HGNC:26035"
                     /db_xref="MIM:612187"
ORIGIN      
        1 mapsrlqlgl raaysgissv agfsiflvwt vvyrqpgtaa mgglagvlal wvlvthvmym
       61 qdywrtwlkg lrgfffvgvl fsavsiaafc tflvlaitrh qsltdptsyy lssvwsfisf
      121 kwafllslya hryradfadi silsdf
//
LOCUS       NP_002460                242 aa            linear   PRI 27-APR-2025
DEFINITION  myogenic factor 6 [Homo sapiens].
ACCESSION   NP_002460
VERSION     NP_002460.1
DBSOURCE    REFSEQ: accession NM_002469.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Arons,E., Zhou,H., Sokolsky,M., Gorelik,D., Potocka,K., Davies,S.,
            Fykes,E., Still,K., Edelman,D.C., Wang,Y., Meltzer,P.S.,
            Raffeld,M., Wiestner,A., Xi,L., Wang,H.W., Stetler-Stevenson,M.,
            Yuan,C. and Kreitman,R.J.
  TITLE     Expression of the muscle-associated gene MYF6 in hairy cell
            leukemia
  JOURNAL   PLoS One 15 (2), e0227586 (2020)
   PUBMED   32040482
  REMARK    GeneRIF: Hypomethylation status of MYF6 supported expression in
            Hairy cell leukemia more than Hairy cell leukemia variant.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Yerges,L.M., Klei,L., Cauley,J.A., Roeder,K., Kammerer,C.M.,
            Moffett,S.P., Ensrud,K.E., Nestlerode,C.S., Marshall,L.M.,
            Hoffman,A.R., Lewis,C., Lang,T.F., Barrett-Connor,E., Ferrell,R.E.,
            Orwoll,E.S. and Zmuda,J.M.
  CONSRTM   MrOS Research Group
  TITLE     High-density association study of 383 candidate genes for
            volumetric BMD at the femoral neck and lumbar spine among older men
  JOURNAL   J Bone Miner Res 24 (12), 2039-2049 (2009)
   PUBMED   19453261
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Kwon,H.S., Lee,D.K., Lee,J.J., Edenberg,H.J., Ahn,Y.H. and Hur,M.W.
  TITLE     Posttranscriptional regulation of human ADH5/FDH and Myf6 gene
            expression by upstream AUG codons
  JOURNAL   Arch Biochem Biophys 386 (2), 163-171 (2001)
   PUBMED   11368338
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Kong,Y., Flick,M.J., Kudla,A.J. and Konieczny,S.F.
  TITLE     Muscle LIM protein promotes myogenesis by enhancing the activity of
            MyoD
  JOURNAL   Mol Cell Biol 17 (8), 4750-4760 (1997)
   PUBMED   9234731
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Cupelli,L., Renault,B., Leblanc-Straceski,J., Banks,A., Ward,D.,
            Kucherlapati,R.S. and Krauter,K.
  TITLE     Assignment of the human myogenic factors 5 and 6 (MYF5, MYF6) gene
            cluster to 12q21 by in situ hybridization and physical mapping of
            the locus between D12S350 and D12S106
  JOURNAL   Cytogenet Cell Genet 72 (2-3), 250-251 (1996)
   PUBMED   8978788
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Braun,T. and Arnold,H.H.
  TITLE     The four human muscle regulatory helix-loop-helix proteins
            Myf3-Myf6 exhibit similar hetero-dimerization and DNA binding
            properties
  JOURNAL   Nucleic Acids Res 19 (20), 5645-5651 (1991)
   PUBMED   1945842
REFERENCE   10 (residues 1 to 242)
  AUTHORS   Braun,T., Bober,E., Winter,B., Rosenthal,N. and Arnold,H.H.
  TITLE     Myf-6, a new member of the human gene family of myogenic
            determination factors: evidence for a gene cluster on chromosome 12
  JOURNAL   EMBO J 9 (3), 821-831 (1990)
   PUBMED   2311584
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA899591.1, BC017834.1 and
            AA176491.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a probable basic
            helix-loop-helix (bHLH) DNA binding protein involved in muscle
            differentiation. The encoded protein likely acts as a heterodimer
            with another bHLH protein. Defects in this gene are a cause of
            autosomal dominant centronuclear myopathy (ADCNM). [provided by
            RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313287.1, BC017834.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158800, SAMEA2162946
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000228641.4/ ENSP00000228641.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.31"
     Protein         1..242
                     /product="myogenic factor 6"
                     /note="muscle-specific regulatory factor 4; class C basic
                     helix-loop-helix protein 4; myogenic factor 6 (herculin)"
                     /calculated_mol_wt=26821
     Region          3..98
                     /region_name="Basic"
                     /note="Myogenic Basic domain; cl11603"
                     /db_xref="CDD:472231"
     Region          31..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23409.1)"
     Region          93..156
                     /region_name="bHLH_TS_MRF4_Myf6"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     muscle-specific regulatory factor 4 (MRF4) and similar
                     proteins; cd18934"
                     /db_xref="CDD:381504"
     Site            order(94..95,99,101..103,105,110,127..130)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381504"
     Site            order(108..109,112..113,115..116,131,134,138,140..141,145,
                     147..148)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381504"
     CDS             1..242
                     /gene="MYF6"
                     /gene_synonym="bHLHc4; CNM3; MRF4; myf-6"
                     /coded_by="NM_002469.3:87..815"
                     /db_xref="CCDS:CCDS9019.1"
                     /db_xref="GeneID:4618"
                     /db_xref="HGNC:HGNC:7566"
                     /db_xref="MIM:159991"
ORIGIN      
        1 mmmdlfetgs yffyldgenv tlqplevaeg splypgsdgt lspcqdqmpp eagsdssgee
       61 hvlappglqp phcpgqcliw acktckrksa ptdrrkaatl rerrrlkkin eafealkrrt
      121 vanpnqrlpk veilrsaisy ierlqdllhr ldqqekmqel gvdpfsyrpk qenlegadfl
      181 rtcssqwpsv sdhsrglvit akeggasids sassslrcls sivdsissee rklpcveevv
      241 ek
//
LOCUS       NP_001355336            1151 aa            linear   ROD 27-APR-2025
DEFINITION  cation channel sperm-associated protein subunit gamma 1 isoform 2
            precursor [Mus musculus].
ACCESSION   NP_001355336
VERSION     NP_001355336.1
DBSOURCE    REFSEQ: accession NM_001368407.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1151)
  AUTHORS   Chung,J.J., Navarro,B., Krapivinsky,G., Krapivinsky,L. and
            Clapham,D.E.
  TITLE     A novel gene required for male fertility and functional CATSPER
            channel formation in spermatozoa
  JOURNAL   Nat Commun 2, 153 (2011)
   PUBMED   21224844
REFERENCE   2  (residues 1 to 1151)
  AUTHORS   Wang,H., Liu,J., Cho,K.H. and Ren,D.
  TITLE     A novel, single, transmembrane protein CATSPERG is associated with
            CATSPER1 channel protein
  JOURNAL   Biol Reprod 81 (3), 539-544 (2009)
   PUBMED   19516020
  REMARK    GeneRIF: CATSPERG is predicted to be a single
            transmembrane-spanning protein with a large extracellular domain
            and a short intracellular tail.
REFERENCE   3  (residues 1 to 1151)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC164564.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1151
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 16.94 cM"
     Protein         1..1151
                     /product="cation channel sperm-associated protein subunit
                     gamma 1 isoform 2 precursor"
                     /note="cation channel sperm-associated protein subunit
                     gamma 1; cation channel, sperm-associated, gamma 1;
                     catsper channel auxiliary subunit gamma 1"
                     /calculated_mol_wt=127937
     sig_peptide     1..38
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4433
     Region          7..973
                     /region_name="CATSPERG"
                     /note="Cation channel sperm-associated protein subunit
                     gamma; pfam15064"
                     /db_xref="CDD:464479"
     mat_peptide     39..1151
                     /product="Cation channel sperm-associated protein subunit
                     gamma 1. /id=PRO_0000416886"
                     /note="propagated from UniProtKB/Swiss-Prot (E9Q355.1)"
                     /calculated_mol_wt=127937
     Site            356
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (E9Q355.1)"
     Site            1064..1084
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9Q355.1)"
     Region          1113..1151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9Q355.1)"
     CDS             1..1151
                     /gene="Catsperg1"
                     /gene_synonym="A230107C01Rik; Catsperg"
                     /coded_by="NM_001368407.1:12..3467"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS90197.1"
                     /db_xref="GeneID:320225"
                     /db_xref="MGI:MGI:2443617"
ORIGIN      
        1 mvsrpamspv spvwprkpnl wafwvlrlvl llslkswaed tlqhctwllv lnkfekvglh
       61 lskdrfqdhe pidtvakvfq kltdspidps enylsfpyyl qinfscpgqn seelarkghl
      121 mgmkpmvrin ymysvnfyrw emenlqilme aapmrstgyc paeamcilnw ytpmpfkngs
      181 vvssvdiytn gigpfipkkr fyvnmngflk rdasgkslfa igyeslvlks shfrlsksrp
      241 lwytvnhapv filggfydek ailfsdsnfq dyvllelsid scwvgsfycp ilgfsatihd
      301 aiatestlfi rqnqlvyyft gtystlfdks hgssrwvrvl psecikrlcp vyfsgngsey
      361 vlalttgkne gyihigtitd glvsfemvpd gwsvceklpg kncsidwaty itdernllll
      421 vkidsgqfyl vnfntefktl nilykipefi peakeldflv lldtvtytnt pmtpkglffn
      481 tlnnmlyiwg nfilqsynre efifladfpk estikymvns fkgqmavvte neeiwyfleg
      541 gydvyqvvps qgwrtylklq kmqksplyst neslvslfyq denlfqlvyl fdvgkerlvk
      601 rllpvgtlme ynlpkpftvv nqgnykmitf tntcpfkaih avdvpkkqha srtesyvalp
      661 plvseslgfh nnntlavyqg lvyyllwlhs kydkpyadpv hdptwrwwqh ktkdkdyffy
      721 lfsnrlaaeg iyinmnayqk lynmsgdygi pdlffldkgn wftftvvlls hqdtftssds
      781 qgptinvdkk lslslvladp eclsvtatre fllnrntllt kikvidkkrc seqgmvgrni
      841 kktsmlikvl gapgnciqrt ylgdhiqgir lvpifigcpp gkrlafdvsy tikhseeink
      901 hyfdcvikda empcflfrdl fqpfflvqdl vtgdsgsflg syvlkvvggg rtlntirdyt
      961 eeeifrynsp ldttnsliwk tkverttedk kfyimshesp gvewlclens pcydiipqsi
     1021 yppefffkll vsnrgvdnst ycdykltfiv hihglplssk rssfivmvst sffialvvfy
     1081 ilfclvwphi vkawvsfrwk ihnmmapety ssssssggft lhshssegsf egpsrpgtke
     1141 dnvqakrakv a
//
LOCUS       NP_001106678             115 aa            linear   PRI 27-APR-2025
DEFINITION  thiosulfate:glutathione sulfurtransferase isoform 1 [Homo sapiens].
ACCESSION   NP_001106678 NP_001119784 XP_001722303 XP_001725777 XP_001725778
VERSION     NP_001106678.1
DBSOURCE    REFSEQ: accession NM_001113207.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Libiad,M., Motl,N., Akey,D.L., Sakamoto,N., Fearon,E.R., Smith,J.L.
            and Banerjee,R.
  TITLE     Thiosulfate sulfurtransferase-like domain-containing 1 protein
            interacts with thioredoxin
  JOURNAL   J Biol Chem 293 (8), 2675-2686 (2018)
   PUBMED   29348167
  REMARK    GeneRIF: Data suggest that TSTD1 can utilize thioredoxin as an
            acceptor in the presence of thioredoxin reductase and NADPH.
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Schlittler,M., Goiny,M., Agudelo,L.Z., Venckunas,T., Brazaitis,M.,
            Skurvydas,A., Kamandulis,S., Ruas,J.L., Erhardt,S., Westerblad,H.
            and Andersson,D.C.
  TITLE     Endurance exercise increases skeletal muscle kynurenine
            aminotransferases and plasma kynurenic acid in humans
  JOURNAL   Am J Physiol Cell Physiol 310 (10), C836-C840 (2016)
   PUBMED   27030575
  REMARK    GeneRIF: Endurance exercise caused an increase in plasma KYNA
            within the first hour after exercise. In contrast, a bout of
            high-intensity eccentric exercise did not lead to increased plasma
            KYNA concentration. Our results show that regular endurance
            exercise causes adaptations in kynurenine metabolism which can have
            implications for exercise recommendations for patients with
            depressive disorder.
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Melideo,S.L., Jackson,M.R. and Jorns,M.S.
  TITLE     Biosynthesis of a central intermediate in hydrogen sulfide
            metabolism by a novel human sulfurtransferase and its yeast
            ortholog
  JOURNAL   Biochemistry 53 (28), 4739-4753 (2014)
   PUBMED   24981631
  REMARK    GeneRIF: Biosynthesis of a central intermediate in hydrogen sulfide
            metabolism by a novel human sulfurtransferase and its yeast
            ortholog.
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Rejdak,R., Rummelt,C., Zrenner,E., Grieb,P., Rejdak,K., Okuno,E.,
            Thaler,S., Nowomiejska,K., Kruse,F., Turski,W. and Junemann,A.G.
  TITLE     Presence of L-kynurenine aminotransferase III in retinal ganglion
            cells and corpora amylacea in the human retina and optic nerve
  JOURNAL   Folia Neuropathol 49 (2), 132-137 (2011)
   PUBMED   21845542
  REMARK    GeneRIF: The presence of kynurenine aminotransferase III in Corpora
            amylacea in the human retina and optic nerve indicates that this
            enzyme may be relevant in mechanisms of neurodegeneration leading
            to Corpora amylaceaformation.
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Wenzel,K., Felix,S.B., Flachmeier,C., Heere,P., Schulze,W.,
            Grunewald,I., Pankow,H., Hewelt,A., Scherneck,S., Bauer,D. and
            Hoehe,M.R.
  TITLE     Identification and characterization of KAT, a novel gene
            preferentially expressed in several human cancer cell lines
  JOURNAL   Biol Chem 384 (5), 763-775 (2003)
   PUBMED   12817473
REFERENCE   7  (residues 1 to 115)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
REFERENCE   8  (residues 1 to 115)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 115)
  AUTHORS   Gupta,S.K., Pillarisetti,K. and Ohlstein,E.H.
  TITLE     Platelet agonist F11 receptor is a member of the immunoglobulin
            superfamily and identical with junctional adhesion molecule (JAM):
            regulation of expression in human endothelial cells and macrophages
  JOURNAL   IUBMB Life 50 (1), 51-56 (2000)
   PUBMED   11087121
REFERENCE   10 (residues 1 to 115)
  AUTHORS   Ozaki,H., Ishii,K., Horiuchi,H., Arai,H., Kawamoto,T., Okawa,K.,
            Iwamatsu,A. and Kita,T.
  TITLE     Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes
            redistribution of junctional adhesion molecule in human endothelial
            cells
  JOURNAL   J Immunol 163 (2), 553-557 (1999)
   PUBMED   10395639
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD675389.1.
            
            On Mar 12, 2009 this sequence version replaced NP_001119784.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.486518.1, CB994352.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence (PMID:
                                                12665801)
            MANE Ensembl match               :: ENST00000423014.3/
                                                ENSP00000388293.2
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..115
                     /product="thiosulfate:glutathione sulfurtransferase
                     isoform 1"
                     /EC_number="2.8.1.3"
                     /note="putative thiosulfate sulfurtransferase KAT;
                     thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 1; thiosulfate sulfurtransferase
                     (rhodanese)-like domain containing 1;
                     thiosulfate:glutathione sulfurtransferase"
                     /calculated_mol_wt=12399
     Region          7..112
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Site            79
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238089"
     CDS             1..115
                     /gene="TSTD1"
                     /gene_synonym="KAT; TST"
                     /coded_by="NM_001113207.2:76..423"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53400.1"
                     /db_xref="GeneID:100131187"
                     /db_xref="HGNC:HGNC:35410"
                     /db_xref="MIM:616041"
ORIGIN      
        1 magaptvslp elrsllasgr arlfdvrsre eaaagtipga lnipvseles alqmepaafq
       61 alysaekpkl edehlvffcq mgkrglqatq larslgytga rnyagayrew lekes
//
LOCUS       NP_001348961             822 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 12 [Mus musculus].
ACCESSION   NP_001348961 XP_017169136
VERSION     NP_001348961.1
DBSOURCE    REFSEQ: accession NM_001362032.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 822)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 822)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 822)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            On Mar 31, 2018 this sequence version replaced XP_017169136.1.
            
            Transcript Variant: This variant (41), as well as variants 40, 42,
            and 43, encodes isoform 12.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164131
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..822
                     /product="cAMP-regulated phosphoprotein 21 isoform 12"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=89758
     Region          162..223
                     /region_name="R3H_encore_like"
                     /note="R3H domain of encore-like and DIP1-like proteins.
                     Drosophila encore is involved in the germline exit after
                     four mitotic divisions, by facilitating
                     SCF-ubiquitin-proteasome-dependent proteolysis. Maize
                     DBF1-interactor protein 1 (DIP1) containing an R3H...;
                     cd02642"
                     /db_xref="CDD:100071"
     Site            order(195,199)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100071"
     Region          244..298
                     /region_name="SUZ"
                     /note="SUZ domain; pfam12752"
                     /db_xref="CDD:463689"
     Region          568..>797
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..822
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362032.1:434..2902"
                     /note="isoform 12 is encoded by transcript variant 42"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqesih lqlssfpslq eedksrkdds erekekdknr
      121 eklserpkir mlskdcsqey tdstgidlhg flintlknns rdrmillkme qemidfiads
      181 nnhykkfpqm ssyqrmlvhr vaayfgldhn vdqtgksvii nktsstripe qrfcehlkde
      241 kseesqkrfi lkrdnssidk ednqnrmhpf rddrrsksie ereeeyqrvr erifahdsvc
      301 sqeslfldnr ahrdssgrts gsrqsssete lrwpdhqraw sstdsdssnr nlkptmtkta
      361 sfggitvltr gdstsstrsa gklsktgses sssagssgsl srthpqstal tssvaagspg
      421 cmaysengmg gqvppsstsy illplesatg ippgsillnp htgqpfvnpd gtpaiynppg
      481 sqqtlrgtvg gqpqqppqqq pspqpqqqvq asqpqmagpl vtqsvqslqp ssqsvqypav
      541 sfppqhllpm sptqhfplre elaaqfsqls msrqssgdtp eppsgtvypa sllpqtaqpq
      601 syvitsagqq lstggfsdsg ppisqqvlqa ppspqgfvqq pppaqmsvyy ypsgqyptst
      661 sqqyrplasv qysaqrsqqi pqttqqagyq pvlsgqqgfq gmmgvqqsah sqgvmssqqg
      721 apvhgvmvsy ptmssyqvpm tqgsqavpqq tyqppimlps qagqgslpat gmpvycnvtp
      781 pnpqnnlrlm gphcpsstvp vmsascrtnc gnvsnagwqv kf
//
LOCUS       NP_796338                908 aa            linear   ROD 27-APR-2025
DEFINITION  SH3 and PX domain-containing protein 2B [Mus musculus].
ACCESSION   NP_796338
VERSION     NP_796338.2
DBSOURCE    REFSEQ: accession NM_177364.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 908)
  AUTHORS   Mehes,E., Barath,M., Gulyas,M., Bugyik,E., Geiszt,M., Szoor,A.,
            Lanyi,A. and Czirok,A.
  TITLE     Enhanced endothelial motility and multicellular sprouting is
            mediated by the scaffold protein TKS4
  JOURNAL   Sci Rep 9 (1), 14363 (2019)
   PUBMED   31591456
  REMARK    GeneRIF: Enhanced endothelial motility and multicellular sprouting
            is mediated by the scaffold protein TKS4.
            Erratum:[Sci Rep. 2020 Jul 20;10(1):12293. doi:
            10.1038/s41598-020-68536-8. PMID: 32686692]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 908)
  AUTHORS   Vas,V., Hahner,T., Kudlik,G., Ernszt,D., Kvell,K., Kuti,D.,
            Kovacs,K.J., Tovari,J., Trexler,M., Mero,B.L., Szeder,B.,
            Koprivanacz,K. and Buday,L.
  TITLE     Analysis of Tks4 Knockout Mice Suggests a Role for Tks4 in Adipose
            Tissue Homeostasis in the Context of Beigeing
  JOURNAL   Cells 8 (8), 831 (2019)
   PUBMED   31387265
  REMARK    GeneRIF: Beigeing process was more robust in the WAT of Tks4-KO
            mice compared to the wild-type animals.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 908)
  AUTHORS   Daniel,S., Meyer,K.J., Clark,A.F., Anderson,M.G. and McDowell,C.M.
  TITLE     Effect of ocular hypertension on the pattern of retinal ganglion
            cell subtype loss in a mouse model of early-onset glaucoma
  JOURNAL   Exp Eye Res 185, 107703 (2019)
   PUBMED   31211954
REFERENCE   4  (residues 1 to 908)
  AUTHORS   Vas,V., Kovacs,T., Kormendi,S., Brody,A., Kudlik,G., Szeder,B.,
            Mezo,D., Kallai,D., Koprivanacz,K., Mero,B.L., Dulk,M., Tovari,J.,
            Vajdovich,P., Senel,S.N., Ozcan,I., Helyes,Z., Dobo-Nagy,C. and
            Buday,L.
  TITLE     Significance of the Tks4 scaffold protein in bone tissue
            homeostasis
  JOURNAL   Sci Rep 9 (1), 5781 (2019)
   PUBMED   30962481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 908)
  AUTHORS   Iizuka,S., Abdullah,C., Buschman,M.D., Diaz,B. and Courtneidge,S.A.
  TITLE     The role of Tks adaptor proteins in invadopodia formation, growth
            and metastasis of melanoma
  JOURNAL   Oncotarget 7 (48), 78473-78486 (2016)
   PUBMED   27802184
  REMARK    GeneRIF: Suggest the importance of Tks adaptor proteins in melanoma
            growth and metastasis in vivo is likely via functional invadopodia
            formation.
REFERENCE   6  (residues 1 to 908)
  AUTHORS   Iqbal,Z., Cejudo-Martin,P., de Brouwer,A., van der Zwaag,B.,
            Ruiz-Lozano,P., Scimia,M.C., Lindsey,J.D., Weinreb,R., Albrecht,B.,
            Megarbane,A., Alanay,Y., Ben-Neriah,Z., Amenduni,M., Artuso,R.,
            Veltman,J.A., van Beusekom,E., Oudakker,A., Millan,J.L.,
            Hennekam,R., Hamel,B., Courtneidge,S.A. and van Bokhoven,H.
  TITLE     Disruption of the podosome adaptor protein TKS4 (SH3PXD2B) causes
            the skeletal dysplasia, eye, and cardiac abnormalities of Frank-Ter
            Haar Syndrome
  JOURNAL   Am J Hum Genet 86 (2), 254-261 (2010)
   PUBMED   20137777
  REMARK    GeneRIF: These findings establish a role for TKS4 in Frank-Ter Haar
            syndrome and embryonic development.
REFERENCE   7  (residues 1 to 908)
  AUTHORS   Mao,M., Thedens,D.R., Chang,B., Harris,B.S., Zheng,Q.Y.,
            Johnson,K.R., Donahue,L.R. and Anderson,M.G.
  TITLE     The podosomal-adaptor protein SH3PXD2B is essential for normal
            postnatal development
  JOURNAL   Mamm Genome 20 (8), 462-475 (2009)
   PUBMED   19669234
  REMARK    GeneRIF: SH3PXD2B is a podosomal-adaptor protein required for
            postnatal growth and development.
REFERENCE   8  (residues 1 to 908)
  AUTHORS   Hishida,T., Nishizuka,M., Osada,S. and Imagawa,M.
  TITLE     The role of C/EBPdelta in the early stages of adipogenesis
  JOURNAL   Biochimie 91 (5), 654-657 (2009)
   PUBMED   19233245
  REMARK    GeneRIF: Silencing of C/EBPdelta impaired the expression of factor
            for adipocyte differentiation (fad) 49, which is up-regulated and
            plays a crucial role early in adipogenesis.
REFERENCE   9  (residues 1 to 908)
  AUTHORS   Buschman,M.D., Bromann,P.A., Cejudo-Martin,P., Wen,F., Pass,I. and
            Courtneidge,S.A.
  TITLE     The novel adaptor protein Tks4 (SH3PXD2B) is required for
            functional podosome formation
  JOURNAL   Mol Biol Cell 20 (5), 1302-1311 (2009)
   PUBMED   19144821
  REMARK    GeneRIF: Tks4 has a role in the formation and function of
            podosomes.
REFERENCE   10 (residues 1 to 908)
  AUTHORS   Hishida,T., Eguchi,T., Osada,S., Nishizuka,M. and Imagawa,M.
  TITLE     A novel gene, fad49, plays a crucial role in the immediate early
            stage of adipocyte differentiation via involvement in mitotic
            clonal expansion
  JOURNAL   FEBS J 275 (22), 5576-5588 (2008)
   PUBMED   18959745
  REMARK    GeneRIF: Induction of the fad49 gene was observed in adipocyte
            differentiable 3T3-L1 cells, but not in non-adipogenic NIH-3T3
            cells.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY197208.1, AK089330.1 and AL662780.20.
            
            On May 6, 2005 this sequence version replaced NP_796338.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK171384.1, AK154898.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 18.89 cM"
     Protein         1..908
                     /product="SH3 and PX domain-containing protein 2B"
                     /note="tyrosine kinase substrate with four SH3 domains;
                     factor for adipocyte differentiation 49"
                     /calculated_mol_wt=101386
     Region          7..125
                     /region_name="PX_FISH"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Five SH protein; cd06888"
                     /db_xref="CDD:132798"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:19144821; propagated from
                     UniProtKB/Swiss-Prot (A2AAY5.1)"
     Site            order(44..46,78..79,94)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132798"
     Region          155..209
                     /region_name="SH3_Tks4_1"
                     /note="First Src homology 3 domain of Tyrosine kinase
                     substrate with four SH3 domains; cd12075"
                     /db_xref="CDD:213008"
     Site            order(161,163,169..170,187..189,200,202,204..205)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213008"
     Region          224..277
                     /region_name="SH3_Tks4_2"
                     /note="Second Src homology 3 domain of Tyrosine kinase
                     substrate with four SH3 domains; cd12076"
                     /db_xref="CDD:213009"
     Site            order(230,232,238..239,256..258,269,271,273..274)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213009"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A1X283; propagated from
                     UniProtKB/Swiss-Prot (A2AAY5.1)"
     Region          280..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2AAY5.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A1X283; propagated from
                     UniProtKB/Swiss-Prot (A2AAY5.1)"
     Region          315..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2AAY5.1)"
     Region          372..424
                     /region_name="SH3_Tks4_3"
                     /note="Third Src homology 3 domain of Tyrosine kinase
                     substrate with four SH3 domains; cd12078"
                     /db_xref="CDD:213011"
     Site            order(377,379,385..386,403..405,416,418,420..421)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213011"
     Region          455..832
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2AAY5.1)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (A2AAY5.1)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (A2AAY5.1)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (A2AAY5.1)"
     Site            840
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319; propagated from
                     UniProtKB/Swiss-Prot (A2AAY5.1)"
     Region          851..906
                     /region_name="SH3_Tks4_4"
                     /note="Fourth (C-terminal) Src homology 3 domain of
                     Tyrosine kinase substrate with four SH3 domains; cd12018"
                     /db_xref="CDD:212951"
     Site            order(856,858,863..864,881..883,898,900,902..903)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212951"
     CDS             1..908
                     /gene="Sh3pxd2b"
                     /gene_synonym="fad49; G431001E03Rik; Tks4; TSK4"
                     /coded_by="NM_177364.4:55..2781"
                     /db_xref="CCDS:CCDS24526.1"
                     /db_xref="GeneID:268396"
                     /db_xref="MGI:MGI:2442062"
ORIGIN      
        1 mpprrsivev kvldvqkrrv pnkhyvyiir vtwssgatea iyrryskffd lqmqmldkfp
       61 meggqkdpkq riipflpgki lfrrshirdv avkrlipide yckaliqlpp yisqcdevlq
      121 ffetrpedln ppkeehigkk ksgndptsvd pmvleqyvvv adyqkqesse islsvgqvvd
      181 iieknesgww fvstaeeqgw vpatclegqd gvqdefslqp eeeekytviy pytardqdem
      241 nlergavvev vqknlegwwk iryqgkegwa pasylkknsg eplppklgps spahsgaldl
      301 dgvsrhqnam grekellnnq rdgrfegrlv pdgdvkqrsp kmrqrppprr dmtiprglnl
      361 pkppippqve eeyytiaefq ttipdgisfq aglkveviek slsgwwyiqm edkegwapat
      421 fidkykktss asrpnflapl phemtqlrlg daaatenntg peavgpsrpl peaphgavds
      481 gmlwskdwkg gkeaprkass dlsastgyee isdptqeekp slpprkesii kseeellere
      541 rqkmeplrgs spkppgmilp mipakhapla rdsrkpepkl dkskfplrnd mglecghkvl
      601 akevkkpnlr pisrskaels eekvdptsqn lfmksrpqvr pkptpspkte paqsedhvdi
      661 ynlrsklrpa ksqekalldg eshhaagshd talsrsflpg egpghgqdrs grqdglspke
      721 tpcrapprpa kttdpgpknv pvpvqeatlq qrpvvpprrp pppkktsssp lscrplpevr
      781 gaqreesrva paagrallvp pkakpflsns svgqddmrgk gglgprvtgk vgetrekaas
      841 flnadgpkds lyvavanfeg dedtssfqeg tvfevrekns sgwwfcqvls gapswegwip
      901 snylrkkp
//
LOCUS       NP_003913               4861 aa            linear   PRI 27-APR-2025
DEFINITION  probable E3 ubiquitin-protein ligase HERC1 [Homo sapiens].
ACCESSION   NP_003913
VERSION     NP_003913.3
DBSOURCE    REFSEQ: accession NM_003922.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4861)
  AUTHORS   Jankovic,M., Poon,W.W.L., Gonzales-Losada,C., Vazquez,G.G.,
            Sharif-Askari,B., Ding,Y., Craplet-Desombre,C., Ilie,A., Shi,J.,
            Wang,Y., Jayavelu,A.K., Orthwein,A. and Mercier,F.E.
  TITLE     The E3 ubiquitin ligase Herc1 modulates the response to nucleoside
            analogs in acute myeloid leukemia
  JOURNAL   Blood Adv 8 (20), 5315-5329 (2024)
   PUBMED   39093953
  REMARK    GeneRIF: The E3 ubiquitin ligase Herc1 modulates the response to
            nucleoside analogs in acute myeloid leukemia.
REFERENCE   2  (residues 1 to 4861)
  AUTHORS   Cui,Y., Wu,X., Jin,J., Man,W., Li,J., Li,X., Li,Y., Yao,H.,
            Zhong,R., Chen,S., Wu,J., Zhu,T., Lin,Y., Xu,J. and Wang,Y.
  TITLE     CircHERC1 promotes non-small cell lung cancer cell progression by
            sequestering FOXO1 in the cytoplasm and regulating the
            miR-142-3p-HMGB1 axis
  JOURNAL   Mol Cancer 22 (1), 179 (2023)
   PUBMED   37932766
  REMARK    GeneRIF: CircHERC1 promotes non-small cell lung cancer cell
            progression by sequestering FOXO1 in the cytoplasm and regulating
            the miR-142-3p-HMGB1 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 4861)
  AUTHORS   Lalonde,R. and Strazielle,C.
  TITLE     The Herc1 gene in neurobiology
  JOURNAL   Gene 814, 146144 (2022)
   PUBMED   34990797
  REMARK    GeneRIF: The Herc1 gene in neurobiology.
            Review article
REFERENCE   4  (residues 1 to 4861)
  AUTHORS   Zavodszky,E., Peak-Chew,S.Y., Juszkiewicz,S., Narvaez,A.J. and
            Hegde,R.S.
  TITLE     Identification of a quality-control factor that monitors failures
            during proteasome assembly
  JOURNAL   Science 373 (6558), 998-1004 (2021)
   PUBMED   34446601
  REMARK    GeneRIF: Identification of a quality-control factor that monitors
            failures during proteasome assembly.
REFERENCE   5  (residues 1 to 4861)
  AUTHORS   Garcia-Gonzalo,F.R., Munoz,P., Gonzalez,E., Casaroli-Marano,R.P.,
            Vilaro,S., Bartrons,R., Ventura,F. and Rosa,J.L.
  TITLE     The giant protein HERC1 is recruited to aluminum fluoride-induced
            actin-rich surface protrusions in HeLa cells
  JOURNAL   FEBS Lett 559 (1-3), 77-83 (2004)
   PUBMED   14960311
  REMARK    GeneRIF: HERC1 overexpression does not stimulate protrusion
            formation in the absence of AlF(4)(-), in conditions where ARNO
            does, indicating that HERC1 is not acting as an ARF6-GEF, but
            instead its recruitment takes place downstream of ARF6 activation
REFERENCE   6  (residues 1 to 4861)
  AUTHORS   Garcia-Gonzalo,F.R., Cruz,C., Munoz,P., Mazurek,S., Eigenbrodt,E.,
            Ventura,F., Bartrons,R. and Rosa,J.L.
  TITLE     Interaction between HERC1 and M2-type pyruvate kinase
  JOURNAL   FEBS Lett 539 (1-3), 78-84 (2003)
   PUBMED   12650930
  REMARK    GeneRIF: physical interaction between the HECT domain of HERC1, a
            giant protein involved in intracellular membrane traffic, and the
            M2 isoform of glycolytic enzyme pyruvate kinase (M2-PK)
REFERENCE   7  (residues 1 to 4861)
  AUTHORS   Ji,Y., Walkowicz,M.J., Buiting,K., Johnson,D.K., Tarvin,R.E.,
            Rinchik,E.M., Horsthemke,B., Stubbs,L. and Nicholls,R.D.
  TITLE     The ancestral gene for transcribed, low-copy repeats in the
            Prader-Willi/Angelman region encodes a large protein implicated in
            protein trafficking, which is deficient in mice with neuromuscular
            and spermiogenic abnormalities
  JOURNAL   Hum Mol Genet 8 (3), 533-542 (1999)
   PUBMED   9949213
REFERENCE   8  (residues 1 to 4861)
  AUTHORS   Cruz,C., Paladugu,A., Ventura,F., Bartrons,R., Aldaz,C.M. and
            Rosa,J.L.
  TITLE     Assignment of the human P532 gene (HERC1) to chromosome 15q22 by
            fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 86 (1), 68-69 (1999)
   PUBMED   10516438
REFERENCE   9  (residues 1 to 4861)
  AUTHORS   Rosa,J.L. and Barbacid,M.
  TITLE     A giant protein that stimulates guanine nucleotide exchange on ARF1
            and Rab proteins forms a cytosolic ternary complex with clathrin
            and Hsp70
  JOURNAL   Oncogene 15 (1), 1-6 (1997)
   PUBMED   9233772
REFERENCE   10 (residues 1 to 4861)
  AUTHORS   Rosa,J.L., Casaroli-Marano,R.P., Buckler,A.J., Vilaro,S. and
            Barbacid,M.
  TITLE     p619, a giant protein related to the chromosome condensation
            regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and
            Rab proteins
  JOURNAL   EMBO J 15 (16), 4262-4273 (1996)
   PUBMED   8861955
  REMARK    Erratum:[EMBO J 1996 Oct 15;15(20):5738]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB117652.1, U50078.1,
            BQ216911.1 and AK226162.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 23, 2007 this sequence version replaced NP_003913.2.
            
            Summary: This gen encodes a member of the HERC protein family. This
            protein stimulates guanine nucleotide exchange on ARF1 and Rab
            proteins. This protein may be involved in membrane transport
            processes. [provided by RefSeq, Mar 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U50078.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000443617.7/ ENSP00000390158.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..4861
                     /product="probable E3 ubiquitin-protein ligase HERC1"
                     /EC_number="2.3.2.26"
                     /note="guanine nucleotide exchange factor p532; HECT
                     domain and RCC1-like domain-containing protein 1; hect
                     (homologous to the E6-AP (UBE3A) carboxyl terminus) domain
                     and RCC1 (CHC1)-like domain (RLD) 1; HECT-type E3
                     ubiquitin transferase HERC1"
                     /calculated_mol_wt=532100
     Region          125..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          371..420
                     /region_name="RCC1 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          374..703
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          421..475
                     /region_name="RCC1 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          476..528
                     /region_name="RCC1 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          529..578
                     /region_name="RCC1 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          580..631
                     /region_name="RCC1 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          633..682
                     /region_name="RCC1 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          683..735
                     /region_name="RCC1 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          683..733
                     /region_name="RCC1"
                     /note="Regulator of chromosome condensation (RCC1) repeat;
                     pfam00415"
                     /db_xref="CDD:395335"
     Region          1322..1341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Site            1342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Region          1348..1379
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          1397..1432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Site            1406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Site            1428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Site            1491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Region          1503..1529
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Site            1512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Site            1517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Site            1521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Region          1864..1886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          2032..2189
                     /region_name="SPRY_HERC1"
                     /note="SPRY domain in HERC1; cd12881"
                     /db_xref="CDD:293939"
     Region          2257..2286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          2406..2497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Site            2422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Region          2617..2675
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          2692..2752
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Site            2701
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Site            2706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Site            2710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Site            2720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Site            2723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     Region          2753..2796
                     /region_name="UBA_HERC1"
                     /note="UBA domain found in probable E3 ubiquitin-protein
                     ligase HERC1 and similar proteins; cd14401"
                     /db_xref="CDD:270584"
     Region          2798..2876
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          3236..3255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          <3387..3778
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          3426..3465
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          3432..3475
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3484..3522
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          3489..3524
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3524..3572
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          3529..3576
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3580..3619
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          3585..3620
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3624..3663
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          3629..3665
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3667..3713
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          3672..3703
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3745..3784
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          3750..3786
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3996..4044
                     /region_name="RCC1 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          3999..4335
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          4046..4099
                     /region_name="RCC1 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          4101..4151
                     /region_name="RCC1 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          4153..4203
                     /region_name="RCC1 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          4205..4256
                     /region_name="RCC1 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          4258..4308
                     /region_name="RCC1 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          4310..4360
                     /region_name="RCC1 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15751.2)"
     Region          4473..4841
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4478,4519,4530,4597,4775,4805..4806,4809..4813,4833,
                     4840)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4625,4628..4629,4631..4632,4635,4643,4645,
                     4649..4650,4652,4661,4666,4683,4687)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4857
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15751.2)"
     CDS             1..4861
                     /gene="HERC1"
                     /gene_synonym="MDFPMR; p532; p619"
                     /coded_by="NM_003922.4:149..14734"
                     /db_xref="CCDS:CCDS45277.1"
                     /db_xref="GeneID:8925"
                     /db_xref="HGNC:HGNC:4867"
                     /db_xref="MIM:605109"
ORIGIN      
        1 matmippvkl kwlehlnssw itedsesiat regvavlysk lvsnkevvpl pqqvlclkgp
       61 qlpdferesl ssdeqdhyld allssqlala kmvcsdspfa galrkrllvl qrvfyalsnk
      121 yhdkgkvkqq qhspesssgs advhsvserp rsstdaliem gvrtglsllf allrqswmmp
      181 vsgpglslcn dvihtaievv sslpplslan eskippmgld clsqvttflk gvtipnsgad
      241 tlgrrlasel llglaaqrgs lryllewiem algasavvht mekgkllssq egmisfdcfm
      301 tilmqmrrsl gssadrsqwr eptrtsdglc slyeaalclf eevcrmasdy srtcaspdsi
      361 qtgdapivse tcevyvwgsn sshqlvegtq ekilqpklap sfsdaqtiea gqyctfvist
      421 dgsvracgkg sygrlglgds nnqstlkklt fephrsikkv ssskgsdght lafttegevf
      481 swgdgdygkl ghgnsstqky pkliqgplqg kvvvcvsagy rhsaavtedg elytwgegdf
      541 grlghgdsns rniptlvkdi snvgevscgs shtialskdg rtvwsfgggd ngklghgdtn
      601 rvykpkviea lqgmfirkvc agsqsslalt stgqvyawgc gaclgcgsse atalrpklie
      661 elaatrivdv sigdshclal shdnevyawg nnsmgqcgqg nstgpitkpk kvsgldgiai
      721 qqisagtshs lawtalprdr qvvawhrpyc vdleestfsh lrsflerycd kinseipplp
      781 fpssrehhsf lklclkllsn hlalalaggv atsilgrqag plrnllfrlm dstvpdeiqe
      841 vvietlsvga tmllpplrer mellhsllpq gpdrweslsk gqrmqldiil tslqdhthva
      901 sllgysspsd aadlssvctg ygnlsdqpyg tqschpdthl aeilmktllr nlgfytdqaf
      961 geleknsdkf llgtsssens qpahlhellc slqkqllafc hinnisenss svallhkhlq
     1021 lllphatdiy srsanllkes pwngsvgekl rdviyvsaag smlcqivnsl lllpvsvarp
     1081 llsylldllp pldclnrllp aadlledqel qwplhggpel idpaglplpq paqswvwlvd
     1141 lertiallig rclggmlqgs pvspeeqdta ywmktplfsd gvemdtpqld kcmsclleva
     1201 lsgneeqkpf dyklrpeiav yvdlalgcsk eparslwism qdyavskdwd satlsnesll
     1261 dtvsrfvlaa llkhtnllsq acgesryqpg khlsevyrcv ykvrsrllac knleliqtrs
     1321 ssrdrwisen qdsadvdpqe hsftrtidee aemeeqaerd reeghpeped eeeerehevm
     1381 tagkifqcfl sarevarsrd rdrmnsgags garaddpppq sqqerrvstd lpegqdvyta
     1441 acnsvihrca llilgvspvi delqkrreeg qlqqpstsas eggglmtrse sltaesrlvh
     1501 tspnyrliks rsesdlsqpe sdeegyalsg rrnvdldlaa shrkrgpmhs qleslsdswa
     1561 rlkhsrdwlc nssysfesdf dltkslgvht lienvvsfvs gdvgnapgfk epeesmstsp
     1621 qasiiameqq qlraelrlea lhqilvllsg meekgsisla gsrlssgfqs stlltsvrlq
     1681 flagcfglgt vghtggkges grlhhyqdgi raakrniqie iqvavhkiyq qlsatleral
     1741 qankhhieaq qrlllvtvfa lsvhyqpvdv slaistglln vlsqlcgtdt mlgqplqllp
     1801 ktgvsqlsta lkvastrllq ilaittgtya dklspkvvqs lldllcsqlk nllsqtgvlh
     1861 masfgegeqe dgeeeekkvd ssgetekkdf raalrkqhaa elhlgdflvf lrrvvsskai
     1921 qskmaspkwt evllniasqk cssgiplvgn lrtrllalhv leavlpaces gveddqmaqi
     1981 verlfsllsd cmwetpiaqa khaiqikeke qeiklqkqge leeedenlpi qevsfdpeka
     2041 qcclvengqi lthgsggkgy glastgvtsg cyqwkfyivk enrgnegtcv gvsrwpvhdf
     2101 nhrttsdmwl yraysgnlyh ngeqtltlss ftqgdfitcv ldmeartisf gkngeepkla
     2161 fedvdaaely pcvmfyssnp gekvkicdmq mrgtprdllp gdpicspvaa vlaeatiqli
     2221 rilhrtdrwt ycinkkmmer lhkikicike sgqklkksrs vqsreenemr eekeskeeek
     2281 gkhtrhglad lselqlrtlc ievwpvlavi ggvdaglrvg grcvhkqtgr hatllgvvke
     2341 gstsakvqwd eaeitisfpt fwspsdtply nlepceplpf dvarfrglta svlldltylt
     2401 gvhedmgkqs tkrhekkhrh eseekgdveq kpesesaldm rtgltsddvk sqsttsskse
     2461 neiasfsldp tlpsvesqhq itegkrknhe hmsknhdvaq seiravqlsy lylgamksls
     2521 allgcskyae lllipkvlae nghnsdcass pvvhedvemr aalqflmrhm vkravmrspi
     2581 kralgladle raqamiyklv vhglledqfg gkikqeidqq aeesdpaqqa qtpvttspsa
     2641 ssttsfmsss ledtttattp vtdtetvpas espgvmplsl lrqmfssypt ttvlptrraq
     2701 tppisslpts psdevgrrqs ltspdsqsar panrtalsdp ssrlstsppp paiavpllem
     2761 gfslrqiaka meatgargea daqnitvlam wmiehpghed eeepqsgsta dsrpgaavlg
     2821 sggksndpcy lqspgdipsa daaemeegfs espdnldhte naasgsgpsa rgrsavtrrh
     2881 kfdlaartll araaglyrsv qahrnqsrre gislqqdpga lydfnldeel eidlddeame
     2941 amfgqdltsd ndilgmwipe vldwptwhvc esedreevvv celcecsvvs fnqhmkrnhp
     3001 gcgrsanrqg yrsngsyvdg wfggecgsgn pyyllcgtcr ekylamktks kstsserykg
     3061 qapdligkqd svyeedwdml dvdedekltg eeefellagp lglndrrivp epvqfpdsdp
     3121 lgasvamvta tnsmeetlmq igchgsveks ssgritlgeq aaalanphdr vvalrrvtaa
     3181 aqvllartmv mralsllsvs gsscslaagl eslgltdirt lvrlmclaaa graglstsps
     3241 amastsersr gghskankpi sclaylstav gclasnapsa akllvqlctq nlisaatgvn
     3301 lttvddsiqr kflpsflrgi aeenklvtsp nfvvtqalva lladkgaklr pnydksevek
     3361 kgplelanal aacclssrls sqhrqwaaqq lvrtlaahdr dnqttlqtla dmggdlrkcs
     3421 fikleahqnr vmtcvwcnkk gllatsgndg tirvwnvtkk qyslqqtcvf nrlegdaees
     3481 lgspsdpsfs pvswsisgky lagalekmvn iwqvnggkgl vdiqphwvsa lawpeegpat
     3541 awsgespell lvgrmdgslg lievvdvstm hrrelehcyr kdvsvtciaw fsedrpfavg
     3601 yfdgklllgt keplekggiv lidahkdtli smkwdptghi lmtcakedsv klwgsisgcw
     3661 cclhslchps ivngiawcrl pgkgsklqll matgcqsglv cvwripqdtt qtnvtsaegw
     3721 weqesncqdg yrkssgakcv yqlrghitpv rtvafssdgl alvsgglggl mniwslrdgs
     3781 vlqtvvigsg aiqttvwipe vgvaacsnrs kdvlvvncta ewaaanhvla tcrtalkqqg
     3841 vlglnmapcm raflerlpmm lqeqyayekp hvvcgdqlvh spymqclasl avglhldqll
     3901 cnppvpphhq nclpdpaswn pnewawlecf sttikaaeal tngaqfpesf tvpdlepvpe
     3961 delvflmdns kwingmdeqi mswatsrped whlggkcdvy lwgagrhgql aeagrnvmvp
     4021 aaapsfsqaq qvicgqnctf viqangtvla cgegsygrlg qgnsddlhvl tvisalqgfv
     4081 vtqlvtscgs dghsmaltes gevfswgdgd ygklghgnsd rqrrprqiea lqgeevvqms
     4141 cgfkhsavvt sdgklftfgn gdygrlglgn tsnkklperv talegyqigq vacglnhtla
     4201 vsadgsmvwa fgdgdygklg lgnstakssp qkidvlcgig ikkvacgtqf svaltkdghv
     4261 ytfgqdrlig lpegrarnhn rpqqipvlag viiedvavga ehtlalasng dvyawgsnse
     4321 gqlglghtnh vreptlvtgl qgknvrqisa grchsaawta ppvpprapgv svplqlglpd
     4381 tvppqygalr evsihtvrar lrllyhfsdl mysswrllnl spnnqnstsh ynagtwgivq
     4441 gqlrpllapr vytlpmvrsi gktmvqgkny gpqitvkris trgrkckpif vqiarqvvkl
     4501 nasdlrlpsr awkvklvgeg addaggvfdd titemcqele tgivdllips pnataevgyn
     4561 rdrflfnpsa cldehlmqfk flgilmgvai rtkkpldlhl aplvwkqlcc vpltledlee
     4621 vdllyvqtln silhiedsgi teesfhemip ldsfvgqsad gkmvpiipgg nsipltfsnr
     4681 keyveraiey rlhemdrqva avregmswiv pvpllsllta kqleqmvcgm peisvevlkk
     4741 vvryrevdeq hqlvqwfwht leefsneerv lfmrfvsgrs rlpantadis qrfqimkvdr
     4801 pydslptsqt cffqlrlppy ssqlvmaerl ryainncrsi dmdnymlsrn vdnaegsdtd
     4861 y
//
LOCUS       NP_055363                351 aa            linear   PRI 27-APR-2025
DEFINITION  tropomodulin-2 isoform a [Homo sapiens].
ACCESSION   NP_055363
VERSION     NP_055363.1
DBSOURCE    REFSEQ: accession NM_014548.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Zhao,M.L., Wang,J.X., Bian,X.K., Zhang,J., Han,Y.W., Xu,S.X.,
            Lee,S.C. and Zhao,J.Z.
  TITLE     Hexavalent chromium causes centrosome amplification by inhibiting
            the binding between TMOD2 and NPM2
  JOURNAL   Toxicol Lett 380, 12-22 (2023)
   PUBMED   36963620
  REMARK    GeneRIF: Hexavalent chromium causes centrosome amplification by
            inhibiting the binding between TMOD2 and NPM2.
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Pawlak,G., McGarvey,T.W., Nguyen,T.B., Tomaszewski,J.E.,
            Puthiyaveettil,R., Malkowicz,S.B. and Helfman,D.M.
  TITLE     Alterations in tropomyosin isoform expression in human transitional
            cell carcinoma of the urinary bladder
  JOURNAL   Int J Cancer 110 (3), 368-373 (2004)
   PUBMED   15095301
  REMARK    GeneRIF: levels of TM1, TM2 and TM3 are reduced in human
            transitional cell carcinoma cells, but significantly upregulated by
            inhibition of the mitogen-activated protein kinase-signaling
            pathway
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Cox,P.R. and Zoghbi,H.Y.
  TITLE     Sequencing, expression analysis, and mapping of three unique human
            tropomodulin genes and their mouse orthologs
  JOURNAL   Genomics 63 (1), 97-107 (2000)
   PUBMED   10662549
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA808222.1, BC064961.1 and
            AC090971.3.
            
            Summary: This gene encodes a neuronal-specific member of the
            tropomodulin family of actin-regulatory proteins. The encoded
            protein caps the pointed end of actin filaments preventing both
            elongation and depolymerization. The capping activity of this
            protein is dependent on its association with tropomyosin.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Dec 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.54106.1,
                                           SRR1660805.107963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000249700.9/ ENSP00000249700.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.2"
     Protein         1..351
                     /product="tropomodulin-2 isoform a"
                     /note="neuronal tropomodulin; tropomodulin 2 (neuronal)"
                     /calculated_mol_wt=39464
     Region          5..146
                     /region_name="Tropomodulin"
                     /note="pfam03250"
                     /db_xref="CDD:460862"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70566; propagated from
                     UniProtKB/Swiss-Prot (Q9NZR1.1)"
     Region          <209..338
                     /region_name="RNA1"
                     /note="Ran GTPase-activating protein (RanGAP) involved in
                     mRNA processing and transport [Translation, ribosomal
                     structure and biogenesis]; COG5238"
                     /db_xref="CDD:444072"
     CDS             1..351
                     /gene="TMOD2"
                     /gene_synonym="N-TMOD; NTMOD"
                     /coded_by="NM_014548.4:186..1241"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10144.1"
                     /db_xref="GeneID:29767"
                     /db_xref="HGNC:HGNC:11872"
                     /db_xref="MIM:602928"
ORIGIN      
        1 malpfqkele kyknidedel lgklseeelk qlenvlddld pesamlpagf rqkdqtqkaa
       61 tgpfdrehll mylekealeq kdredfvpft gekkgrvfip kekpietrke ekvtldpele
      121 ealasasdte lydlaavlgv hnllnnpkfd eetannkggk gpvrnvvkge kvkpvfeepp
      181 nptnveislq qmkandpslq evnlnnikni piptlrefak aletnthvkk fslaatrsnd
      241 pvaiafadml kvnktltsln iesnfitgtg ilalvealke ndtlteikid nqrqqlgtav
      301 emeiaqmlee nsrilkfgyq ftkqgprtrv aaaitknndl vrkkrveadr r
//
LOCUS       NP_000818                906 aa            linear   PRI 27-APR-2025
DEFINITION  glutamate receptor 1 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_000818
VERSION     NP_000818.2
DBSOURCE    REFSEQ: accession NM_000827.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 906)
  AUTHORS   Lai,S.K., Wu,K.L.K., Ma,C.W., Ng,K.P., Hu,X.Q., Tam,K.W.,
            Yung,W.H., Wang,Y.T., Wong,T.P., Shum,D.K. and Chan,Y.S.
  TITLE     Timely insertion of AMPA receptor in developing vestibular circuits
            is required for manifestation of righting reflexes and effective
            navigation
  JOURNAL   Prog Neurobiol 221, 102402 (2023)
   PUBMED   36608782
  REMARK    GeneRIF: Timely insertion of AMPA receptor in developing vestibular
            circuits is required for manifestation of righting reflexes and
            effective navigation.
REFERENCE   2  (residues 1 to 906)
  AUTHORS   Ismail,V., Zachariassen,L.G., Godwin,A., Sahakian,M., Ellard,S.,
            Stals,K.L., Baple,E., Brown,K.T., Foulds,N., Wheway,G.,
            Parker,M.O., Lyngby,S.M., Pedersen,M.G., Desir,J., Bayat,A.,
            Musgaard,M., Guille,M., Kristensen,A.S. and Baralle,D.
  TITLE     Identification and functional evaluation of GRIA1 missense and
            truncation variants in individuals with ID: An emerging
            neurodevelopmental syndrome
  JOURNAL   Am J Hum Genet 109 (7), 1217-1241 (2022)
   PUBMED   35675825
  REMARK    GeneRIF: Identification and functional evaluation of GRIA1 missense
            and truncation variants in individuals with ID: An emerging
            neurodevelopmental syndrome.
REFERENCE   3  (residues 1 to 906)
  AUTHORS   Zhao,M., Dong,J., Liao,Y., Lu,G., Pan,W., Zhou,H., Zuo,X. and
            Shan,B.
  TITLE     MicroRNA miR-18a-3p promotes osteoporosis and possibly contributes
            to spinal fracture by inhibiting the glutamate AMPA receptor
            subunit 1 gene (GRIA1)
  JOURNAL   Bioengineered 13 (1), 370-382 (2022)
   PUBMED   34937502
  REMARK    GeneRIF: MicroRNA miR-18a-3p promotes osteoporosis and possibly
            contributes to spinal fracture by inhibiting the glutamate AMPA
            receptor subunit 1 gene (GRIA1).
REFERENCE   4  (residues 1 to 906)
  AUTHORS   Ge,Y. and Wang,Y.T.
  TITLE     GluA1-homomeric AMPA receptor in synaptic plasticity and
            neurological diseases
  JOURNAL   Neuropharmacology 197, 108708 (2021)
   PUBMED   34274350
  REMARK    GeneRIF: GluA1-homomeric AMPA receptor in synaptic plasticity and
            neurological diseases.
            Review article
REFERENCE   5  (residues 1 to 906)
  AUTHORS   Melo,H.M., de Carvalho,C.R., Hoeller,A.A., Marques,J.L.B.,
            Linhares,M.N., Lopes,M.W., Fialho,G.L., Wolf,P., Lin,K.,
            Bortolotto,Z.A., Henley,J.M., D'Avila,A., Leal,R.B. and Walz,R.
  TITLE     AMPAr GluA1 Phosphorylation at Serine 845 in Limbic System Is
            Associated with Cardiac Autonomic Tone
  JOURNAL   Mol Neurobiol 58 (4), 1859-1870 (2021)
   PUBMED   33404979
  REMARK    GeneRIF: AMPAr GluA1 Phosphorylation at Serine 845 in Limbic System
            Is Associated with Cardiac Autonomic Tone.
REFERENCE   6  (residues 1 to 906)
  AUTHORS   Yakel,J.L., Vissavajjhala,P., Derkach,V.A., Brickey,D.A. and
            Soderling,T.R.
  TITLE     Identification of a Ca2+/calmodulin-dependent protein kinase II
            regulatory phosphorylation site in non-N-methyl-D-aspartate
            glutamate receptors
  JOURNAL   Proc Natl Acad Sci U S A 92 (5), 1376-1380 (1995)
   PUBMED   7877986
REFERENCE   7  (residues 1 to 906)
  AUTHORS   McNamara,J.O., Eubanks,J.H., McPherson,J.D., Wasmuth,J.J.,
            Evans,G.A. and Heinemann,S.F.
  TITLE     Chromosomal localization of human glutamate receptor genes
  JOURNAL   J Neurosci 12 (7), 2555-2562 (1992)
   PUBMED   1319477
REFERENCE   8  (residues 1 to 906)
  AUTHORS   Sun,W., Ferrer-Montiel,A.V., Schinder,A.F., McPherson,J.P.,
            Evans,G.A. and Montal,M.
  TITLE     Molecular cloning, chromosomal mapping, and functional expression
            of human brain glutamate receptors
  JOURNAL   Proc Natl Acad Sci U S A 89 (4), 1443-1447 (1992)
   PUBMED   1311100
REFERENCE   9  (residues 1 to 906)
  AUTHORS   Potier,M.C., Spillantini,M.G. and Carter,N.P.
  TITLE     The human glutamate receptor cDNA GluR1: cloning, sequencing,
            expression and localization to chromosome 5
  JOURNAL   DNA Seq 2 (4), 211-218 (1992)
   PUBMED   1320959
REFERENCE   10 (residues 1 to 906)
  AUTHORS   Puckett,C., Gomez,C.M., Korenberg,J.R., Tung,H., Meier,T.J.,
            Chen,X.N. and Hood,L.
  TITLE     Molecular cloning and chromosomal localization of one of the human
            glutamate receptor genes
  JOURNAL   Proc Natl Acad Sci U S A 88 (17), 7557-7561 (1991)
   PUBMED   1652753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC335107.1, AK310189.1,
            M81886.1, X58633.1, AB209094.1 and AL120214.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 6, 2008 this sequence version replaced NP_000818.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. These receptors
            are heteromeric protein complexes with multiple subunits, each
            possessing transmembrane regions, and all arranged to form a
            ligand-gated ion channel. The classification of glutamate receptors
            is based on their activation by different pharmacologic agonists.
            This gene belongs to a family of
            alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA)
            receptors. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.221732.1,
                                           SRR1803616.21965.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000285900.10/ ENSP00000285900.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..906
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.2"
     Protein         1..906
                     /product="glutamate receptor 1 isoform 1 precursor"
                     /note="AMPA 1; gluR-1; gluR-A; gluR-K1; AMPA-selective
                     glutamate receptor 1; AMPA receptor subunit GluA1;
                     glutamate receptor, ionotropic, AMPA 1"
                     /calculated_mol_wt=99579
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1945
     mat_peptide     19..906
                     /product="glutamate receptor 1 isoform 1"
                     /calculated_mol_wt=99579
     Region          26..392
                     /region_name="PBP1_iGluR_AMPA_GluR1"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the GluR1 subunit of the
                     AMPA receptor; cd06390"
                     /db_xref="CDD:380613"
     Site            63
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42261.2)"
     Site            order(66..68,71..73,95..96,99..100,103..105,120,149,151,
                     155,159,162..163,171,173..174,176,179,187,190..191,317,
                     319..330,332,335,339)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380613"
     Site            order(66..68,71..72,75,100,103,149,159,162..163,166..167,
                     174,176,191,322..324,326,328)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380613"
     Site            249
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42261.2)"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42261.2)"
     Site            363
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42261.2)"
     Site            401
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42261.2)"
     Region          406..787
                     /region_name="PBP2_iGluR_AMPA_GluR1"
                     /note="The ligand-binding domain of the AMPA
                     (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic
                     acid) subtype GluR1 of ionotropic glutamate receptors, a
                     member of the type 2 periplasmic binding fold protein
                     superfamily; cd13729"
                     /db_xref="CDD:270447"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42261.2)"
     Site            order(433,445,449,496..497,500,505..508,743,761..762,
                     765..770,772,775)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270447"
     Site            order(464,492..494,499,664,667..669,718..719,722,746)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270447"
     Site            order(507..511,765,768,773..774,777)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:270447"
     Site            537..557
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42261.2)"
     Site            610..630
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42261.2)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19490; propagated from
                     UniProtKB/Swiss-Prot (P42261.2)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19490; propagated from
                     UniProtKB/Swiss-Prot (P42261.2)"
     Site            806..826
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42261.2)"
     Site            849
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19490; propagated from
                     UniProtKB/Swiss-Prot (P42261.2)"
     Region          861..880
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42261.2)"
     Site            863
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19490; propagated from
                     UniProtKB/Swiss-Prot (P42261.2)"
     Region          903..906
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P42261.2)"
     CDS             1..906
                     /gene="GRIA1"
                     /gene_synonym="GluA1; GLUH1; GLUR1; GLURA; HBGR1; MRD67;
                     MRT76"
                     /coded_by="NM_000827.4:220..2940"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4322.1"
                     /db_xref="GeneID:2890"
                     /db_xref="HGNC:HGNC:4571"
                     /db_xref="MIM:138248"
ORIGIN      
        1 mqhifaffct gflgavvgan fpnniqiggl fpnqqsqeha afrfalsqlt eppkllpqid
       61 ivnisdsfem tyrfcsqfsk gvyaifgfye rrtvnmltsf cgalhvcfit psfpvdtsnq
      121 fvlqlrpelq dalisiidhy kwqkfvyiyd adrglsvlqk vldtaaeknw qvtavniltt
      181 teegyrmlfq dlekkkerlv vvdceserln ailgqiikle kngigyhyil anlgfmdidl
      241 nkfkesganv tgfqlvnytd tipakimqqw knsdardhtr vdwkrpkyts altydgvkvm
      301 aeafqslrrq ridisrrgna gdclanpavp wgqgidiqra lqqvrfeglt gnvqfnekgr
      361 rtnytlhvie mkhdgirkig ywneddkfvp aatdaqaggd nssvqnrtyi vttiledpyv
      421 mlkknanqfe gndryegycv elaaeiakhv gysyrleivs dgkygardpd tkawngmvge
      481 lvygradvav apltitlvre evidfskpfm slgisimikk pqkskpgvfs fldplayeiw
      541 mcivfayigv svvlflvsrf spyewhseef eegrdqttsd qsnefgifns lwfslgafmq
      601 qgcdisprsl sgrivggvww fftliiissy tanlaafltv ermvspiesa edlakqteia
      661 ygtleagstk effrrskiav fekmwtymks aepsvfvrtt eegmirvrks kgkyaylles
      721 tmneyieqrk pcdtmkvggn ldskgygiat pkgsalrnpv nlavlklneq glldklknkw
      781 wydkgecgsg ggdskdktsa lslsnvagvf yiligglgla mlvaliefcy ksrseskrmk
      841 gfclipqqsi neairtstlp rnsgagassg gsgengrvvs hdfpksmqsi pcmshssgmp
      901 lgatgl
//
LOCUS       NP_001165694             268 aa            linear   PRI 27-APR-2025
DEFINITION  MOB kinase activator 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001165694
VERSION     NP_001165694.1
DBSOURCE    REFSEQ: accession NM_001172223.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Jiang,K., Yao,G., Hu,L., Yan,Y., Liu,J., Shi,J., Chang,Y.,
            Zhang,Y., Liang,D., Shen,D., Zhang,G., Meng,S. and Piao,H.
  TITLE     MOB2 suppresses GBM cell migration and invasion via regulation of
            FAK/Akt and cAMP/PKA signaling
  JOURNAL   Cell Death Dis 11 (4), 230 (2020)
   PUBMED   32286266
  REMARK    GeneRIF: MOB2 suppresses GBM cell migration and invasion via
            regulation of FAK/Akt and cAMP/PKA signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Gomez,V., Gundogdu,R., Gomez,M., Hoa,L., Panchal,N., O'Driscoll,M.
            and Hergovich,A.
  TITLE     Regulation of DNA damage responses and cell cycle progression by
            hMOB2
  JOURNAL   Cell Signal 27 (2), 326-339 (2015)
   PUBMED   25460043
  REMARK    GeneRIF: hMOB2 interacts with RAD50, facilitating the recruitment
            of the MRE11-RAD50-NBS1 (MRN) DNA damage sensor complex and
            activated ATM to DNA damaged chromatin.
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Hauri,S., Wepf,A., van Drogen,A., Varjosalo,M., Tapon,N.,
            Aebersold,R. and Gstaiger,M.
  TITLE     Interaction proteome of human Hippo signaling: modular control of
            the co-activator YAP1
  JOURNAL   Mol Syst Biol 9, 713 (2013)
   PUBMED   24366813
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Leng,J.J., Tan,H.M., Chen,K., Shen,W.G. and Tan,J.W.
  TITLE     Growth-inhibitory effects of MOB2 on human hepatic carcinoma cell
            line SMMC-7721
  JOURNAL   World J Gastroenterol 18 (48), 7285-7289 (2012)
   PUBMED   23326134
  REMARK    GeneRIF: MOB2 overexpression induces apoptosis and inhibits the
            growth of human hepatic cancer cells
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Kohler,R.S., Schmitz,D., Cornils,H., Hemmings,B.A. and Hergovich,A.
  TITLE     Differential NDR/LATS interactions with the human MOB family reveal
            a negative role for human MOB2 in the regulation of human NDR
            kinases
  JOURNAL   Mol Cell Biol 30 (18), 4507-4520 (2010)
   PUBMED   20624913
  REMARK    GeneRIF: Data indicate that human MOB2 is a negative regulator of
            human NDR kinases in biochemical and biological settings.
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Devroe,E., Erdjument-Bromage,H., Tempst,P. and Silver,P.A.
  TITLE     Human Mob proteins regulate the NDR1 and NDR2 serine-threonine
            kinases
  JOURNAL   J Biol Chem 279 (23), 24444-24451 (2004)
   PUBMED   15067004
  REMARK    GeneRIF: Binds to and stimulates the kinase activity of the related
            human serine-threonine kinases NDR1 and NDR2.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091196.6, DC413532.1, AK296658.1, BC047291.1 and AW874617.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.852508.1, ERR279857.515.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329957.7/ ENSP00000328694.6
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..268
                     /product="MOB kinase activator 2 isoform 1"
                     /note="Mps one binder kinase activator-like 2; MOB2 Mps
                     One Binder homolog"
                     /calculated_mol_wt=30043
     Region          63..231
                     /region_name="Mob1_phocein"
                     /note="Mob1/phocein family; pfam03637"
                     /db_xref="CDD:461000"
     CDS             1..268
                     /gene="MOB2"
                     /gene_synonym="HCCA2"
                     /coded_by="NM_001172223.3:224..1030"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53591.1"
                     /db_xref="GeneID:81532"
                     /db_xref="HGNC:HGNC:24904"
                     /db_xref="MIM:611969"
ORIGIN      
        1 mlgdhcslpe dqarpgqslq sglcckmvlq avskvlrksk akpngkkpaa eerkaylepe
       61 htkaritdfq fkelvvlpre idlnewlasn tttffhhinl qystisefct getcqtmavc
      121 ntqyywyder gkkvkctapq yvdfvmssvq klvtdedvfp tkygrefpss feslvrkicr
      181 hlfhvlahiy wahfketlal elhghlntly vhfilfaref nlldpketai mddltevlcs
      241 gaggvhsggs gdgagsggpg aqnhvker
//
LOCUS       NP_005660                189 aa            linear   PRI 27-APR-2025
DEFINITION  receptor expression-enhancing protein 5 [Homo sapiens].
ACCESSION   NP_005660
VERSION     NP_005660.4
DBSOURCE    REFSEQ: accession NM_005669.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Li,J., Gui,Q., Liang,F.-X., Sall,J., Zhang,Q., Duan,Y.,
            Dhabaria,A., Askenazi,M., Ueberheide,B., Stapleford,K.A. and
            Pagano,M.
  TITLE     The REEP5/TRAM1 complex binds SARS-CoV-2 NSP3 and promotes virus
            replication
  JOURNAL   J Virol 97 (10), e0050723 (2023)
   PUBMED   37768083
  REMARK    GeneRIF: The REEP5/TRAM1 complex binds SARS-CoV-2 NSP3 and promotes
            virus replication.
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Lee,S.H., Hadipour-Lakmehsari,S., Murthy,H.R., Gibb,N., Miyake,T.,
            Teng,A.C.T., Cosme,J., Yu,J.C., Moon,M., Lim,S., Wong,V., Liu,P.,
            Billia,F., Fernandez-Gonzalez,R., Stagljar,I., Sharma,P.,
            Kislinger,T., Scott,I.C. and Gramolini,A.O.
  TITLE     REEP5 depletion causes sarco-endoplasmic reticulum vacuolization
            and cardiac functional defects
  JOURNAL   Nat Commun 11 (1), 965 (2020)
   PUBMED   32075961
  REMARK    GeneRIF: The sarco-endoplasmic reticulum (SR/ER) plays an important
            role in the development and progression of many heart diseases.
            Receptor accessory protein 5 (REEP5), a cardiac enriched,
            sarco-endoplasmic reticulum (SR/ER) membrane protein,is centrally
            involved in regulating SR/ER organization and cellular stress
            responses in cardiac myocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Prieschl,E.E., Pendl,G.G., Harrer,N.E. and Baumruker,T.
  TITLE     The murine homolog of TB2/DP1, a gene of the familial adenomatous
            polyposis (FAP) locus
  JOURNAL   Gene 169 (2), 215-218 (1996)
   PUBMED   8647449
REFERENCE   7  (residues 1 to 189)
  AUTHORS   Spirio,L., Joslyn,G., Nelson,L., Leppert,M. and White,R.
  TITLE     A CA repeat 30-70 KB downstream from the adenomatous polyposis coli
            (APC) gene
  JOURNAL   Nucleic Acids Res 19 (22), 6348 (1991)
   PUBMED   1659692
  REMARK    Erratum:[Nucleic Acids Res. 1992 Feb 11;20(3):642. doi:
            10.1093/nar/20.3.642-a. PMID: 1312235]
REFERENCE   8  (residues 1 to 189)
  AUTHORS   Joslyn,G., Carlson,M., Thliveris,A., Albertsen,H., Gelbert,L.,
            Samowitz,W., Groden,J., Stevens,J., Spirio,L., Robertson,M. et al.
  TITLE     Identification of deletion mutations and three new genes at the
            familial polyposis locus
  JOURNAL   Cell 66 (3), 601-613 (1991)
   PUBMED   1678319
REFERENCE   9  (residues 1 to 189)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 189)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA807043.1, BC000232.1 and AC008575.7.
            
            On Sep 30, 2006 this sequence version replaced NP_005660.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.41716.1,
                                           SRR1803612.60533.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145774, SAMEA2467144
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379638.9/ ENSP00000368959.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..189
                     /product="receptor expression-enhancing protein 5"
                     /note="polyposis locus protein 1; deleted in polyposis 1;
                     polyposis coli region hypothetical protein DP1"
                     /calculated_mol_wt=21362
     Site            35..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00765.3)"
     Site            54..74
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00765.3)"
     Region          67..144
                     /region_name="TB2_DP1_HVA22"
                     /note="TB2/DP1, HVA22 family; pfam03134"
                     /db_xref="CDD:460820"
     Site            85..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00765.3)"
     Site            106..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00765.3)"
     Region          114..185
                     /region_name="Required for dimerization and maintaining
                     endoplasmic reticulum morphology.
                     /evidence=ECO:0000269|PubMed:32075961"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00765.3)"
     CDS             1..189
                     /gene="REEP5"
                     /gene_synonym="C5orf18; D5S346; DP1; POB16; TB2; Yip2e;
                     YOP1"
                     /coded_by="NM_005669.5:38..607"
                     /db_xref="CCDS:CCDS4109.2"
                     /db_xref="GeneID:7905"
                     /db_xref="HGNC:HGNC:30077"
                     /db_xref="MIM:125265"
ORIGIN      
        1 msaamrerfd rflhekncmt dllakleakt gvnrsfialg viglvalylv fgygasllcn
       61 ligfgypayi sikaiespnk eddtqwltyw vvygvfsiae ffsdiflswf pfyymlkcgf
      121 llwcmapsps ngaellykri irpfflkhes qmdsvvkdlk dkaketadai tkeakkatvn
      181 llgeekkst
//
LOCUS       NP_003642                372 aa            linear   PRI 27-APR-2025
DEFINITION  Y-box-binding protein 3 isoform a [Homo sapiens].
ACCESSION   NP_003642
VERSION     NP_003642.3
DBSOURCE    REFSEQ: accession NM_003651.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Awad,S., Skipper,W., Vostrejs,W., Ozorowski,K., Min,K., Pfuhler,L.,
            Mehta,D. and Cooke,A.
  TITLE     The YBX3 RNA-binding protein posttranscriptionally controls SLC1A5
            mRNA in proliferating and differentiating skeletal muscle cells
  JOURNAL   J Biol Chem 300 (2), 105602 (2024)
   PUBMED   38159852
  REMARK    GeneRIF: The YBX3 RNA-binding protein posttranscriptionally
            controls SLC1A5 mRNA in proliferating and differentiating skeletal
            muscle cells.
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Peng,W., Zeng,C., Xu,J., Zhao,H., Zhu,Q., Xu,H., Chen,H., Huang,H.,
            Zhou,Y. and Zhao,C.
  TITLE     Regulation of epithelial cell differentiation by the Ubiquitous
            expressed transcript isoform 1 in ulcerative colitis
  JOURNAL   J Gastroenterol Hepatol 38 (11), 2006-2017 (2023)
   PUBMED   37608570
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Xie,J., Zhang,H., Wang,K., Ni,J., Ma,X., Khoury,C.J., Prifti,V.,
            Hoard,B., Cerenzia,E.G., Yin,L., Zhang,H., Wang,R., Zhuo,D., Mao,W.
            and Peng,B.
  TITLE     M6A-mediated-upregulation of lncRNA BLACAT3 promotes bladder cancer
            angiogenesis and hematogenous metastasis through YBX3 nuclear
            shuttling and enhancing NCF2 transcription
  JOURNAL   Oncogene 42 (40), 2956-2970 (2023)
   PUBMED   37612524
  REMARK    GeneRIF: M6A-mediated-upregulation of lncRNA BLACAT3 promotes
            bladder cancer angiogenesis and hematogenous metastasis through
            YBX3 nuclear shuttling and enhancing NCF2 transcription.
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Wang,C., You,Z., He,Y. and Chen,X.
  TITLE     Identification of RNA-binding protein YBX3 as an oncogene in clear
            cell renal cell carcinoma
  JOURNAL   Funct Integr Genomics 23 (3), 225 (2023)
   PUBMED   37418046
  REMARK    GeneRIF: Identification of RNA-binding protein YBX3 as an oncogene
            in clear cell renal cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Hayashi,J., Kajino,K., Umeda,T., Takano,S., Arakawa,Y., Kudo,M. and
            Hino,O.
  TITLE     Somatic mutation and SNP in the promoter of dbpA and human
            hepatocarcinogenesis
  JOURNAL   Int J Oncol 21 (4), 847-850 (2002)
   PUBMED   12239625
  REMARK    GeneRIF: human dbpA has a role in accelerating hepatocarcinogenesis
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Argyrokastritis,A., Kontaraki,J., Kamakari,S., Pasparaki,A. and
            Moschonas,N.K.
  TITLE     Assignment of a human cold shock domain protein A intronless
            pseudogene (CSDAP1) to human chromosome 16 band p11.2 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 84 (1-2), 53-54 (1999)
   PUBMED   10343102
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Lloberas,J., Soler,C. and Celada,A.
  TITLE     Repression mechanisms of the I-A beta gene of the major
            histocompatibility complex
  JOURNAL   Immunobiology 198 (1-3), 249-263 (1997)
   PUBMED   9442396
  REMARK    Review article
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Coles,L.S., Diamond,P., Occhiodoro,F., Vadas,M.A. and Shannon,M.F.
  TITLE     Cold shock domain proteins repress transcription from the GM-CSF
            promoter
  JOURNAL   Nucleic Acids Res 24 (12), 2311-2317 (1996)
   PUBMED   8710501
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Kudo,S., Mattei,M.G. and Fukuda,M.
  TITLE     Characterization of the gene for dbpA, a family member of the
            nucleic-acid-binding proteins containing a cold-shock domain
  JOURNAL   Eur J Biochem 231 (1), 72-82 (1995)
   PUBMED   7628487
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Sakura,H., Maekawa,T., Imamoto,F., Yasuda,K. and Ishii,S.
  TITLE     Two human genes isolated by a novel method encode DNA-binding
            proteins containing a common region of homology
  JOURNAL   Gene 73 (2), 499-507 (1988)
   PUBMED   2977358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC021049.12.
            
            On Mar 6, 2009 this sequence version replaced NP_003642.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021926.1, SRR1163657.295287.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000228251.9/ ENSP00000228251.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..372
                     /product="Y-box-binding protein 3 isoform a"
                     /note="cold-shock domain containing A1; DNA-binding
                     protein A; single-strand DNA-binding protein NF-GMB;
                     ZO-1-associated nucleic acid-binding protein; cold-shock
                     domain protein A; cold shock domain-containing protein A"
                     /calculated_mol_wt=39959
     Region          1..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16989.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Region          91..160
                     /region_name="CSD"
                     /note="'Cold-shock' DNA-binding domain; pfam00313"
                     /db_xref="CDD:278729"
     Site            order(97,106,117,150)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:239905"
     Site            order(103..109,116..119)
                     /site_type="active"
                     /note="RNA-binding motif [active]"
                     /db_xref="CDD:239905"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Region          181..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16989.4)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P16989.4)"
     Site            251
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Site            326
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62764; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62764; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62764; propagated from
                     UniProtKB/Swiss-Prot (P16989.4)"
     CDS             1..372
                     /gene="YBX3"
                     /gene_synonym="CSDA; CSDA1; DBPA; ZONAB"
                     /coded_by="NM_003651.5:213..1331"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8630.1"
                     /db_xref="GeneID:8531"
                     /db_xref="HGNC:HGNC:2428"
                     /db_xref="MIM:603437"
ORIGIN      
        1 mseageattt ttttlpqapt eaaaaapqdp apkspvgsga pqaaapapaa hvagnpggda
       61 apaatgtaaa aslataagse daekkvlatk vlgtvkwfnv rngygfinrn dtkedvfvhq
      121 taikknnprk ylrsvgdget vefdvvegek gaeaanvtgp dgvpvegsry aadrrryrrg
      181 yygrrrgppr nyageeeeeg sgssegfdpp atdrqfsgar nqlrrpqyrp qyrqrrfppy
      241 hvgqtfdrrs rvlphpnriq ageigemkdg vpegaqlqgp vhrnptyrpr yrsrgpprpr
      301 papavgeaed kenqqatsgp nqpsvrrgyr rpynyrrrpr ppnapsqdgk eakageapte
      361 npapptqqss ae
//
LOCUS       NP_079359                508 aa            linear   PRI 27-APR-2025
DEFINITION  enhancer of mRNA-decapping protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_079359
VERSION     NP_079359.2
DBSOURCE    REFSEQ: accession NM_025083.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Rudolph,C., Sigruener,A., Hartmann,A., Orso,E., Bals-Pratsch,M.,
            Gronwald,W., Seifert,B., Kalbitzer,H.R., Verdorfer,I.,
            Luetjens,C.M., Ortmann,O., Bornstein,S.R. and Schmitz,G.
  TITLE     ApoA-I-binding protein (AI-BP) and its homologues hYjeF_N2 and
            hYjeF_N3 comprise the YjeF_N domain protein family in humans with a
            role in spermiogenesis and oogenesis
  JOURNAL   Horm Metab Res 39 (5), 322-335 (2007)
   PUBMED   17533573
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Fenger-Gron,M., Fillman,C., Norrild,B. and Lykke-Andersen,J.
  TITLE     Multiple processing body factors and the ARE binding protein TTP
            activate mRNA decapping
  JOURNAL   Mol Cell 20 (6), 905-915 (2005)
   PUBMED   16364915
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Benzinger,A., Muster,N., Koch,H.B., Yates,J.R. 3rd and Hermeking,H.
  TITLE     Targeted proteomic analysis of 14-3-3 sigma, a p53 effector
            commonly silenced in cancer
  JOURNAL   Mol Cell Proteomics 4 (6), 785-795 (2005)
   PUBMED   15778465
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Albrecht,M. and Lengauer,T.
  TITLE     Novel Sm-like proteins with long C-terminal tails and associated
            methyltransferases
  JOURNAL   FEBS Lett 569 (1-3), 18-26 (2004)
   PUBMED   15225602
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091230.23 and BC011534.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_079359.1.
            
            Summary: This gene encodes a protein that is important in mRNA
            degradation. The encoded protein is a component of a decapping
            complex that promotes efficient removal of the monomethylguanosine
            (m7G) cap from mRNAs, as part of the 5' to 3' mRNA decay pathway.
            Mutations in this gene have been identified in human patients with
            an autosomal recessive form of intellectual disability. [provided
            by RefSeq, May 2017].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1-4 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011534.1, SRR1803614.246983.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315127.9/ ENSP00000320503.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..508
                     /product="enhancer of mRNA-decapping protein 3 isoform 1"
                     /note="LSM16 homolog (EDC3, S. cerevisiae); enhancer of
                     mRNA-decapping protein 3; yjeF domain-containing protein
                     1; yjeF N-terminal domain-containing protein 2; yjeF
                     domain containing; enhancer of mRNA decapping 3 homolog"
                     /calculated_mol_wt=55947
     Region          1..79
                     /region_name="Required for P-body targeting and
                     interaction with DCP1A. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          2..66
                     /region_name="LSm16_N"
                     /note="Like-Sm protein 16, N-terminal domain; cd01737"
                     /db_xref="CDD:212484"
     Site            order(2,5,28,33,56,59..64)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:212484"
     Site            order(10..15,19..30,33..36)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212484"
     Site            order(29,55)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212484"
     Site            51..62
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212484"
     Region          95..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          102..194
                     /region_name="Edc3_linker"
                     /note="Linker region of enhancer of mRNA-decapping protein
                     3; pfam16598"
                     /db_xref="CDD:465188"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96F86.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96F86.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96F86.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          191..296
                     /region_name="Required for interaction with DDX6.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          198..301
                     /region_name="FDF"
                     /note="FDF domain; pfam09532"
                     /db_xref="CDD:430668"
     Region          302..455
                     /region_name="YjeF_N"
                     /note="YjeF-related protein N-terminus; pfam03853"
                     /db_xref="CDD:427546"
     CDS             1..508
                     /gene="EDC3"
                     /gene_synonym="hYjeF_N2-15q23; LSM16; MRT50; YJDC; YJEFN2"
                     /coded_by="NM_025083.5:164..1690"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS10267.1"
                     /db_xref="GeneID:80153"
                     /db_xref="HGNC:HGNC:26114"
                     /db_xref="MIM:609842"
ORIGIN      
        1 matdwlgsiv sincgdslgv yqgrvsavdq vsqtisltrp fhngvkclvp evtfragdit
       61 elkileipgp gdnqhfgdlh qtelgpsgag cqvginqngt gkfvkkpass ssapqnipkr
      121 tdvksqdvav spqqqqcsks yvdrhmesls qsksfrrrhn swssssrhpn qatpkksglk
      181 ngqmknkdde cfgddieeip dtdfdfegnl alfdkaavfe eidtyerrsg trsrgipner
      241 ptryrhdeni lesepivyrr iivphnvske fctdsglvvp sisyelhkkl lsvaekhglt
      301 lerrlemtgv casqmaltll ggpnrlnpkn vhqrptvall cgphvkgaqg iscgrhlanh
      361 dvqvilflpn fvkmlesitn elslfsktqg qqvsslkdlp tspvdlvinc ldcpenvflr
      421 dqpwykaava wanqnrapvl sidppvheve qgidakwsla lglplplgeh agriylcdig
      481 ipqqvfqevg inyhspfgck fviplhsa
//
LOCUS       NP_001116131             442 aa            linear   PRI 27-APR-2025
DEFINITION  endothelin receptor type B isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001116131
VERSION     NP_001116131.1
DBSOURCE    REFSEQ: accession NM_001122659.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Tani,K., Maki-Yonekura,S., Kanno,R., Negami,T., Hamaguchi,T.,
            Hall,M., Mizoguchi,A., Humbel,B.M., Terada,T., Yonekura,K. and
            Doi,T.
  TITLE     Structure of endothelin ETB receptor-Gi complex in a conformation
            stabilized by unique NPxxL motif
  JOURNAL   Commun Biol 7 (1), 1303 (2024)
   PUBMED   39414992
  REMARK    GeneRIF: Structure of endothelin ETB receptor-Gi complex in a
            conformation stabilized by unique NPxxL motif.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Ham,D., Shihoya,W., Nureki,O., Inoue,A. and Chung,K.Y.
  TITLE     Molecular mechanism of the endothelin receptor type B interactions
            with Gs, Gi, and Gq
  JOURNAL   Structure 32 (10), 1632-1639 (2024)
   PUBMED   39043181
  REMARK    GeneRIF: Molecular mechanism of the endothelin receptor type B
            interactions with Gs, Gi, and Gq.
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Wang,C.H., Tsuji,T., Wu,L.H., Yang,C.Y., Huang,T.L., Sato,M.,
            Shamsi,F. and Tseng,Y.H.
  TITLE     Endothelin 3/EDNRB signaling induces thermogenic differentiation of
            white adipose tissue
  JOURNAL   Nat Commun 15 (1), 7215 (2024)
   PUBMED   39174539
  REMARK    GeneRIF: Endothelin 3/EDNRB signaling induces thermogenic
            differentiation of white adipose tissue.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Medstrand,P., Landry,J.R. and Mager,D.L.
  TITLE     Long terminal repeats are used as alternative promoters for the
            endothelin B receptor and apolipoprotein C-I genes in humans
  JOURNAL   J Biol Chem 276 (3), 1896-1903 (2001)
   PUBMED   11054415
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Puffenberger,E.G., Hosoda,K., Washington,S.S., Nakao,K., deWit,D.,
            Yanagisawa,M. and Chakravart,A.
  TITLE     A missense mutation of the endothelin-B receptor gene in multigenic
            Hirschsprung's disease
  JOURNAL   Cell 79 (7), 1257-1266 (1994)
   PUBMED   8001158
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Arai,H., Nakao,K., Hosoda,K., Ogawa,Y., Nakagawa,O., Komatsu,Y. and
            Imura,H.
  TITLE     [Molecular cloning of human endothelin receptors and their
            expression in vascular endothelial cells and smooth muscle cells]
  JOURNAL   Jpn Circ J 56 Suppl 5, 1303-1307 (1992)
   PUBMED   1291713
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Haendler,B., Hechler,U. and Schleuning,W.D.
  TITLE     Molecular cloning of human endothelin (ET) receptors ETA and ETB
  JOURNAL   J Cardiovasc Pharmacol 20 Suppl 12, S1-S4 (1992)
   PUBMED   1282938
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Cyr,C., Huebner,K., Druck,T. and Kris,R.
  TITLE     Cloning and chromosomal localization of a human endothelin ETA
            receptor
  JOURNAL   Biochem Biophys Res Commun 181 (1), 184-190 (1991)
   PUBMED   1659806
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Nakamuta,M., Takayanagi,R., Sakai,Y., Sakamoto,S., Hagiwara,H.,
            Mizuno,T., Saito,Y., Hirose,S., Yamamoto,M. and Nawata,H.
  TITLE     Cloning and sequence analysis of a cDNA encoding human
            non-selective type of endothelin receptor
  JOURNAL   Biochem Biophys Res Commun 177 (1), 34-39 (1991)
   PUBMED   1710450
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139002.18.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a G protein-coupled
            receptor which activates a phosphatidylinositol-calcium second
            messenger system. Its ligand, endothelin, consists of a family of
            three potent vasoactive peptides: ET1, ET2, and ET3. Studies
            suggest that the multigenic disorder, Hirschsprung disease type 2,
            is due to mutations in the endothelin receptor type B gene.
            Alternative splicing and the use of alternative promoters results
            in multiple transcript variants. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1 and 3 both encode isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.243839.1,
                                           SRR1660803.99844.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA2142348 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000646607.2/ ENSP00000493527.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q22.3"
     Protein         1..442
                     /product="endothelin receptor type B isoform 1 precursor"
                     /note="endothelin receptor non-selective type;
                     Hirschsprung disease 2; endothelin receptor subtype B1"
                     /calculated_mol_wt=46953
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2709
     mat_peptide     27..442
                     /product="Endothelin receptor type B. /id=PRO_0000012729"
                     /note="propagated from UniProtKB/Swiss-Prot (P24530.1)"
                     /calculated_mol_wt=46953
     Site            59
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P24530.1)"
     Region          69..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24530.1)"
     Region          102..397
                     /region_name="7tmA_ET-BR"
                     /note="endothelin B receptor, member of the class A family
                     of seven-transmembrane G protein-coupled receptors;
                     cd15976"
                     /db_xref="CDD:320642"
     Site            102..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P24530.1)"
     Region          103..129
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320642"
     Region          136..162
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320642"
     Site            138..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P24530.1)"
     Site            order(158,161..162,174..179,181..182,185,230,232..236,270,
                     273..275,277..279,281..282,336,339..340,342..343,346,
                     364..365,367..369,372,375..376)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320642"
     Region          174..204
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320642"
     Site            176..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P24530.1)"
     Region          216..236
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320642"
     Site            219..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P24530.1)"
     Region          270..295
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320642"
     Site            272..296
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P24530.1)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P24530.1)"
     Region          316..346
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320642"
     Site            325..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P24530.1)"
     Site            363..389
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P24530.1)"
     Region          365..390
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320642"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P24530.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P24530.1)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P24530.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P24530.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P24530.1)"
     CDS             1..442
                     /gene="EDNRB"
                     /gene_synonym="ABCDS; ET-B; ET-BR; ETB; ETB1; ETBR; ETRB;
                     HSCR; HSCR2; WS4A"
                     /coded_by="NM_001122659.3:259..1587"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS9461.1"
                     /db_xref="GeneID:1910"
                     /db_xref="HGNC:HGNC:3180"
                     /db_xref="MIM:131244"
ORIGIN      
        1 mqpppslcgr alvalvlacg lsriwgeerg fppdratpll qtaeimtppt ktlwpkgsna
       61 slarslapae vpkgdrtags pprtispppc qgpieiketf kyintvvscl vfvlgiigns
      121 tllriiyknk cmrngpnili aslalgdllh ividipinvy kllaedwpfg aemcklvpfi
      181 qkasvgitvl slcalsidry ravaswsrik gigvpkwtav eivliwvvsv vlavpeaigf
      241 diitmdykgs ylricllhpv qktafmqfyk takdwwlfsf yfclplaita ffytlmtcem
      301 lrkksgmqia lndhlkqrre vaktvfclvl vfalcwlplh lsrilkltly nqndpnrcel
      361 lsfllvldyi ginmaslnsc inpialylvs krfkncfksc lccwcqsfee kqsleekqsc
      421 lkfkandhgy dnfrssnkys ss
//
LOCUS       NP_653285                535 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 480 isoform 1 [Homo sapiens].
ACCESSION   NP_653285
VERSION     NP_653285.2
DBSOURCE    REFSEQ: accession NM_144684.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Jouan,L., Girard,S.L., Dobrzeniecka,S., Ambalavanan,A., Krebs,M.O.,
            Joober,R., Gauthier,J., Dion,P.A. and Rouleau,G.A.
  TITLE     Investigation of rare variants in LRP1, KPNA1, ALS2CL and ZNF480
            genes in schizophrenia patients reflects genetic heterogeneity of
            the disease
  JOURNAL   Behav Brain Funct 9, 9 (2013)
   PUBMED   23425335
  REMARK    GeneRIF: This supports the notion that de novo mutations in ZNF480
            are extremely rare in schizophrenia
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Yi,Z., Li,Y., Ma,W., Li,D., Zhu,C., Luo,J., Wang,Y., Huang,X.,
            Yuan,W., Liu,M. and Wu,X.
  TITLE     A novel KRAB zinc-finger protein, ZNF480, expresses in human heart
            and activates transcriptional activities of AP-1 and SRE
  JOURNAL   Biochem Biophys Res Commun 320 (2), 409-415 (2004)
   PUBMED   15219843
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA501214.1, AK303271.1, AY512662.1, AK096442.1, AL832560.1 and
            AC010320.10.
            
            On Mar 5, 2009 this sequence version replaced NP_653285.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018783.1, SRR1803612.48997.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000595962.6/ ENSP00000471754.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..535
                     /product="zinc finger protein 480 isoform 1"
                     /calculated_mol_wt=61577
     Region          27..87
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <158..501
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          205..225
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          233..253
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(238,240,242,244..245,248..249,252,266,268,272..273,
                     276..277,280,294,296,298,300..301,304..305,308)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          261..281
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          289..309
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          317..336
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          345..365
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(350,352,354,356..357,360..361,364,378,380,384..385,
                     388..389,392,406,408,410,412..413,416..417,420)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          373..393
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          401..421
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          429..449
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          457..477
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(462,464,466,468..469,472..473,476,490,492,496..497,
                     500..501,504,518,520,522,524..525,528..529,532)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          485..505
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..522
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          513..533
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..535
                     /gene="ZNF480"
                     /coded_by="NM_144684.4:75..1682"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12850.2"
                     /db_xref="GeneID:147657"
                     /db_xref="HGNC:HGNC:23305"
                     /db_xref="MIM:613910"
ORIGIN      
        1 mlcdekaqkr rkrkakesgm alpqghltfr dvaiefsqae wkcldpaqra lykdvmleny
       61 rnlvslgisl pdlninsmle qrrepwsges evkiaknsdg recikgvntg ssyalgsnae
      121 dkpikkqlgv sfhlhlsele lfpderving cnqvenfinh sssvsclqem sssvktpifn
      181 rndfddssfl pqeqkvhlre kpyecnehsk vfrvsssltk hqvihtvekp ykcnscgkvf
      241 srnshlaehc rihtgekpyk cnvcgkvfsy nsnfarhqri htrekpyecn ecgkvfsnns
      301 ylarhqriha eekpykcnec gkgfshkssl anhwriytge kpykcdecgk afyriallvr
      361 hqkihtgekp ykcnecgkvf iqnshlaqhw rihtgekpyk cnecgkvfnq lsnlarhrri
      421 htgekpykcn ecgkafseys glsahlviht gekpykcsec gkafrhklsl tnhqrihtge
      481 rpykcnecgk vfnriahlar hrkihtgekp ykcnecgkaf srisylaqhw tihmg
//
LOCUS       NP_004594                288 aa            linear   PRI 27-APR-2025
DEFINITION  syntaxin-1A isoform 1 [Homo sapiens].
ACCESSION   NP_004594
VERSION     NP_004594.1
DBSOURCE    REFSEQ: accession NM_004603.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Habib,C.A., El-Sebai,A.A., Fouad,M.M., El-Mohamdy,M.A., Abdel
            Ghani,A.M. and Bawady,S.A.
  TITLE     Assessment of Stx-1A gene polymorphism (rs1569061) in relation to
            the development of multiple sclerosis in Egyptian patients
  JOURNAL   Egypt J Immunol 31 (2), 18-27 (2024)
   PUBMED   38615201
  REMARK    GeneRIF: Assessment of Stx-1A gene polymorphism (rs1569061) in
            relation to the development of multiple sclerosis in Egyptian
            patients.
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Iadarola,M.J., Sapio,M.R., Loydpierson,A.J., Mervis,C.B.,
            Fehrenbacher,J.C., Vasko,M.R., Maric,D., Eisenberg,D.P., Nash,T.A.,
            Kippenhan,J.S., Garvey,M.H., Mannes,A.J., Gregory,M.D. and
            Berman,K.F.
  TITLE     Syntaxin1A overexpression and pain insensitivity in individuals
            with 7q11.23 duplication syndrome
  JOURNAL   JCI Insight 9 (4), e176147 (2024)
   PUBMED   38261410
  REMARK    GeneRIF: Syntaxin1A overexpression and pain insensitivity in
            individuals with 7q11.23 duplication syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Luppe,J., Sticht,H., Lecoquierre,F., Goldenberg,A., Gorman,K.M.,
            Molloy,B., Agolini,E., Novelli,A., Briuglia,S., Kuismin,O.,
            Marcelis,C., Vitobello,A., Denomme-Pichon,A.S., Julia,S.,
            Lemke,J.R., Abou Jamra,R. and Platzer,K.
  TITLE     Heterozygous and homozygous variants in STX1A cause a
            neurodevelopmental disorder with or without epilepsy
  JOURNAL   Eur J Hum Genet 31 (3), 345-352 (2023)
   PUBMED   36564538
  REMARK    GeneRIF: Heterozygous and homozygous variants in STX1A cause a
            neurodevelopmental disorder with or without epilepsy.
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Turkevi-Nagy,S., Bathori,A., Bocz,J., Krenacs,L., Cserni,G. and
            Kovari,B.
  TITLE     Syntaxin-1 and Insulinoma-Associated Protein 1 Expression in Breast
            Neoplasms with Neuroendocrine Features
  JOURNAL   Pathol Oncol Res 27, 1610039 (2021)
   PUBMED   34764822
  REMARK    GeneRIF: Syntaxin-1 and Insulinoma-Associated Protein 1 Expression
            in Breast Neoplasms with Neuroendocrine Features.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Agliardi,C., Meloni,M., Guerini,F.R., Zanzottera,M., Bolognesi,E.,
            Baglio,F. and Clerici,M.
  TITLE     Oligomeric alpha-Syn and SNARE complex proteins in peripheral
            extracellular vesicles of neural origin are biomarkers for
            Parkinson's disease
  JOURNAL   Neurobiol Dis 148, 105185 (2021)
   PUBMED   33217562
  REMARK    GeneRIF: Oligomeric alpha-Syn and SNARE complex proteins in
            peripheral extracellular vesicles of neural origin are biomarkers
            for Parkinson's disease.
REFERENCE   6  (residues 1 to 288)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Hanson,P.I., Otto,H., Barton,N. and Jahn,R.
  TITLE     The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce
            a conformational change in syntaxin
  JOURNAL   J Biol Chem 270 (28), 16955-16961 (1995)
   PUBMED   7622514
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Zhang,R., Maksymowych,A.B. and Simpson,L.L.
  TITLE     Cloning and sequence analysis of a cDNA encoding human syntaxin 1A,
            a polypeptide essential for exocytosis
  JOURNAL   Gene 159 (2), 293-294 (1995)
   PUBMED   7622072
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Bennett,M.K., Calakos,N. and Scheller,R.H.
  TITLE     Syntaxin: a synaptic protein implicated in docking of synaptic
            vesicles at presynaptic active zones
  JOURNAL   Science 257 (5067), 255-259 (1992)
   PUBMED   1321498
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Wilson,D.W., Whiteheart,S.W., Wiedmann,M., Brunner,M. and
            Rothman,J.E.
  TITLE     A multisubunit particle implicated in membrane fusion
  JOURNAL   J Cell Biol 117 (3), 531-538 (1992)
   PUBMED   1315316
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA159446.1, BC064644.1 and
            BC003011.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the syntaxin superfamily.
            Syntaxins are nervous system-specific proteins implicated in the
            docking of synaptic vesicles with the presynaptic plasma membrane.
            Syntaxins possess a single C-terminal transmembrane domain, a SNARE
            [Soluble NSF (N-ethylmaleimide-sensitive fusion protein)-Attachment
            protein REceptor] domain (known as H3), and an N-terminal
            regulatory domain (Habc). Syntaxins bind synaptotagmin in a
            calcium-dependent fashion and interact with voltage dependent
            calcium and potassium channels via the C-terminal H3 domain. This
            gene product is a key molecule in ion channel regulation and
            synaptic exocytosis. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.[provided
            by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064644.1, D37932.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222812.8/ ENSP00000222812.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..288
                     /product="syntaxin-1A isoform 1"
                     /note="neuron-specific antigen HPC-1; syntaxin 1A (brain)"
                     /calculated_mol_wt=32892
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15822905; propagated from
                     UniProtKB/Swiss-Prot (Q16623.1)"
     Region          30..181
                     /region_name="SynN"
                     /note="Syntaxin N-terminus domain; syntaxins are nervous
                     system-specific proteins implicated in the docking of
                     synaptic vesicles with the presynaptic plasma membrane;
                     they are a family of receptors for intracellular transport
                     vesicles; each target membrane may...; cd00179"
                     /db_xref="CDD:238105"
     Site            order(30,34,41,114..115,118..119,122,125..126,132,135,166)
                     /site_type="active"
                     /note="nSec1 interaction sites [active]"
                     /db_xref="CDD:238105"
     Site            order(61,72,75..76,83,87,90,97,120,125,128,134,141..142,
                     145..146,148..149,152,178)
                     /site_type="active"
                     /note="interdomain interaction site [active]"
                     /db_xref="CDD:238105"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35526; propagated from
                     UniProtKB/Swiss-Prot (Q16623.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P32851; propagated from
                     UniProtKB/Swiss-Prot (Q16623.1)"
     Site            order(158..168,177..181)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238105"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DAPK1.
                     /evidence=ECO:0000269|PubMed:12730201; propagated from
                     UniProtKB/Swiss-Prot (Q16623.1)"
     Region          191..259
                     /region_name="SNARE_syntaxin1"
                     /note="SNARE motif of syntaxin 1; cd15880"
                     /db_xref="CDD:277233"
     Site            order(196,198..199,201..206,208..210,212..213,215..217,
                     219..220,222..224,226..227,229..234,236..241,243..248,
                     250..252)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277233"
     Site            order(213,216..217,220..221,223..225,228..234,236..238,
                     240..245)
                     /site_type="other"
                     /note="Munc18 interface [polypeptide binding]"
                     /db_xref="CDD:277233"
     Site            226
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277233"
     Site            266..286
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16623.1)"
     CDS             1..288
                     /gene="STX1A"
                     /gene_synonym="HPC-1; P35-1; STX1; SYN1A"
                     /coded_by="NM_004603.4:39..905"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34655.1"
                     /db_xref="GeneID:6804"
                     /db_xref="HGNC:HGNC:11433"
                     /db_xref="MIM:186590"
ORIGIN      
        1 mkdrtqelrt akdsdddddv avtvdrdrfm deffeqveei rgfidkiaen veevkrkhsa
       61 ilaspnpdek tkeeleelms dikktankvr sklksieqsi eqeeglnrss adlrirktqh
      121 stlsrkfvev mseynatqsd yrerckgriq rqleitgrtt tseeledmle sgnpaifasg
      181 iimdssiskq alseietrhs eiiklensir elhdmfmdma mlvesqgemi drieynveha
      241 vdyveravsd tkkavkyqsk arrkkimiii ccvilgivia stvggifa
//
LOCUS       NP_064615                473 aa            linear   PRI 27-APR-2025
DEFINITION  suppressor of SWI4 1 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_064615
VERSION     NP_064615.3
DBSOURCE    REFSEQ: accession NM_020230.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Chen,X., Zhang,Q., Yang,Z., Yu,H., Qu,Y., Tan,R., Gao,Y., He,Y. and
            Li,L.
  TITLE     An SNP reducing SNORD105 and PPAN expression decreases the risk of
            hepatocellular carcinoma in a Chinese population
  JOURNAL   J Clin Lab Anal 35 (12), e24095 (2021)
   PUBMED   34741342
  REMARK    GeneRIF: An SNP reducing SNORD105 and PPAN expression decreases the
            risk of hepatocellular carcinoma in a Chinese population.
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Dannheisig,D.P., Beck,E., Calzia,E., Walther,P., Behrends,C. and
            Pfister,A.S.
  TITLE     Loss of Peter Pan (PPAN) Affects Mitochondrial Homeostasis and
            Autophagic Flux
  JOURNAL   Cells 8 (8), 894 (2019)
   PUBMED   31416196
  REMARK    GeneRIF: The study uncovers that PPAN knockdown is linked to
            mitochondrial damage and stimulates autophagy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Keil,M., Meyer,M.T., Dannheisig,D.P., Maerz,L.D., Philipp,M. and
            Pfister,A.S.
  TITLE     Loss of Peter Pan protein is associated with cell cycle defects and
            apoptotic events
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1866 (5), 882-895 (2019)
   PUBMED   30716409
  REMARK    GeneRIF: data underline the notion that the PPAN-mediated,
            p53-independent nucleolar stress response has multiple facets.
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Pfister,A.S., Keil,M. and Kuhl,M.
  TITLE     The Wnt Target Protein Peter Pan Defines a Novel p53-independent
            Nucleolar Stress-Response Pathway
  JOURNAL   J Biol Chem 290 (17), 10905-10918 (2015)
   PUBMED   25759387
  REMARK    GeneRIF: a novel nucleolar stress-response pathway involving PPAN,
            NPM, and BAX to guarantee cell survival in a p53-independent
            manner.
            Erratum:[J Biol Chem. 2023 Jan;299(1):102808. doi:
            10.1016/j.jbc.2022.102808. PMID: 36566638]
REFERENCE   5  (residues 1 to 473)
  AUTHORS   Han,F., Faraco,J., Dong,X.S., Ollila,H.M., Lin,L., Li,J., An,P.,
            Wang,S., Jiang,K.W., Gao,Z.C., Zhao,L., Yan,H., Liu,Y.N., Li,Q.H.,
            Zhang,X.Z., Hu,Y., Wang,J.Y., Lu,Y.H., Lu,C.J., Zhou,W.,
            Hallmayer,J., Huang,Y.S., Strohl,K.P., Pollmacher,T. and Mignot,E.
  TITLE     Genome wide analysis of narcolepsy in China implicates novel immune
            loci and reveals changes in association prior to versus after the
            2009 H1N1 influenza pandemic
  JOURNAL   PLoS Genet 9 (10), e1003880 (2013)
   PUBMED   24204295
REFERENCE   6  (residues 1 to 473)
  AUTHORS   Communi,D., Suarez-Huerta,N., Dussossoy,D., Savi,P. and
            Boeynaems,J.M.
  TITLE     Cotranscription and intergenic splicing of human P2Y11 and SSF1
            genes
  JOURNAL   J Biol Chem 276 (19), 16561-16566 (2001)
   PUBMED   11278528
REFERENCE   7  (residues 1 to 473)
  AUTHORS   Suarez-Huerta,N., Boeynaems,J.M. and Communi,D.
  TITLE     Cloning, genomic organization, and tissue distribution of human
            Ssf-1
  JOURNAL   Biochem Biophys Res Commun 275 (1), 37-42 (2000)
   PUBMED   10944437
REFERENCE   8  (residues 1 to 473)
  AUTHORS   Welch,P.J., Marcusson,E.G., Li,Q.X., Beger,C., Kruger,M., Zhou,C.,
            Leavitt,M., Wong-Staal,F. and Barber,J.R.
  TITLE     Identification and validation of a gene involved in
            anchorage-independent cell growth control using a library of
            randomized hairpin ribozymes
  JOURNAL   Genomics 66 (3), 274-283 (2000)
   PUBMED   10873382
REFERENCE   9  (residues 1 to 473)
  AUTHORS   Migeon,J.C., Garfinkel,M.S. and Edgar,B.A.
  TITLE     Cloning and characterization of peter pan, a novel Drosophila gene
            required for larval growth
  JOURNAL   Mol Biol Cell 10 (6), 1733-1744 (1999)
   PUBMED   10359593
  REMARK    GeneRIF: The functional analysis of the Drosophila homolog. [LH]
REFERENCE   10 (residues 1 to 473)
  AUTHORS   Communi,D., Govaerts,C., Parmentier,M. and Boeynaems,J.M.
  TITLE     Cloning of a human purinergic P2Y receptor coupled to phospholipase
            C and adenylyl cyclase
  JOURNAL   J Biol Chem 272 (51), 31969-31973 (1997)
   PUBMED   9405388
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC033202.1 and AC020931.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 14, 2004 this sequence version replaced NP_064615.2.
            
            Summary: The protein encoded by this gene is an evolutionarily
            conserved protein similar to yeast SSF1 as well as to the gene
            product of the Drosophila gene peter pan (ppan). SSF1 is known to
            be involved in the second step of mRNA splicing. Both SSF1 and ppan
            are essential for cell growth and proliferation. Exogenous
            expression of this gene was reported to reduce the
            anchorage-independent growth of some tumor cells. Read-through
            transcription of this gene with P2RY11/P2Y(11), an adjacent
            downstream gene that encodes an ATP receptor, has been found. These
            read-through transcripts are ubiquitously present and up-regulated
            during granulocyte differentiation. [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.163791.1,
                                           SRR1660805.148204.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253107.12/ ENSP00000253107.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..473
                     /product="suppressor of SWI4 1 homolog isoform 1"
                     /note="suppressor of sterile four 1; homolog of S.
                     cerevisiae SSF1; suppressor of SWI4 1 homolog; second-step
                     splicing factor 1; brix domain-containing protein 3"
                     /calculated_mol_wt=53063
     Region          32..201
                     /region_name="Brix"
                     /note="The Brix domain is found in a number of eukaryotic
                     proteins; smart00879"
                     /db_xref="CDD:214879"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YU8; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ55.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YU8; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ55.1)"
     Region          <270..341
                     /region_name="Brix"
                     /note="The Brix domain is found in a number of eukaryotic
                     proteins; cl00935"
                     /db_xref="CDD:469999"
     Region          323..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ55.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YU8; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ55.1)"
     Site            438
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q91YU8; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ55.1)"
     CDS             1..473
                     /gene="PPAN"
                     /gene_synonym="BXDC3; SSF; SSF-1; SSF1; SSF2"
                     /coded_by="NM_020230.7:34..1455"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12225.1"
                     /db_xref="GeneID:56342"
                     /db_xref="HGNC:HGNC:9227"
                     /db_xref="MIM:607793"
ORIGIN      
        1 mgqsgrsrhq kraraqaqlr nleayaanph sfvftrgctg rnirqlsldv rrvmepltas
       61 rlqvrkknsl kdcvavagpl gvthflilsk tetnvyfklm rlpggptltf qvkkyslvrd
      121 vvsslrrhrm heqqfahppl lvlnsfgphg mhvklmatmf qnlfpsinvh kvnlntikrc
      181 llidynpdsq eldfrhysik vvpvgasrgm kkllqekfpn msrlqdisel latgaglses
      241 eaepdgdhni telpqavagr gnmraqqsav rlteigprmt lqlikvqegv gegkvmfhsf
      301 vskteeelqa ileakekklr lkaqrqaqqa qnvqrkqeqr eahrkksleg mkkarvggsd
      361 eeasgipsrt aslelgeddd eqedddieyf cqavgeapse dlfpeakqkr lakspgrkrk
      421 rwemdrgrgr lcdqkfpktk dksqgaqarr gprgasrdgg rgrgrgrpgk rva
//
LOCUS       NP_001150               1338 aa            linear   PRI 27-APR-2025
DEFINITION  aldehyde oxidase [Homo sapiens].
ACCESSION   NP_001150
VERSION     NP_001150.3
DBSOURCE    REFSEQ: accession NM_001159.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1338)
  AUTHORS   Sun,S. and Iwata,T.
  TITLE     Role of AOX1 on RXR signaling regulates osteoblastogenesis in
            hPDLMSCs
  JOURNAL   Sci Rep 14 (1), 16767 (2024)
   PUBMED   39034354
  REMARK    GeneRIF: Role of AOX1 on RXR signaling regulates osteoblastogenesis
            in hPDLMSCs.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1338)
  AUTHORS   Yuan,Z., Yi,G., Ma,R., Wang,Z., Hu,J., Zhao,W. and Hu,Y.
  TITLE     Aldehyde oxidase 1 promotes gallbladder carcinogenesis through
            ROS-mediated activation of the Wnt/beta-catenin pathway
  JOURNAL   Cell Signal 116, 111042 (2024)
   PUBMED   38199597
  REMARK    GeneRIF: Aldehyde oxidase 1 promotes gallbladder carcinogenesis
            through ROS-mediated activation of the Wnt/beta-catenin pathway.
REFERENCE   3  (residues 1 to 1338)
  AUTHORS   Hammid,A., Fallon,J.K., Vellonen,K.S., Lassila,T., Reinisalo,M.,
            Urtti,A., Gonzalez,F., Tolonen,A., Smith,P.C. and Honkakoski,P.
  TITLE     Aldehyde oxidase 1 activity and protein expression in human,
            rabbit, and pig ocular tissues
  JOURNAL   Eur J Pharm Sci 191, 106603 (2023)
   PUBMED   37827455
  REMARK    GeneRIF: Aldehyde oxidase 1 activity and protein expression in
            human, rabbit, and pig ocular tissues.
REFERENCE   4  (residues 1 to 1338)
  AUTHORS   Wu,J., Wei,Y., Li,T., Lin,L., Yang,Z. and Ye,L.
  TITLE     DNA Methylation-Mediated Lowly Expressed AOX1 Promotes Cell
            Migration and Invasion of Prostate Cancer
  JOURNAL   Urol Int 107 (5), 517-525 (2023)
   PUBMED   35354150
  REMARK    GeneRIF: DNA Methylation-Mediated Lowly Expressed AOX1 Promotes
            Cell Migration and Invasion of Prostate Cancer.
REFERENCE   5  (residues 1 to 1338)
  AUTHORS   Zhang,W., Chai,W., Zhu,Z. and Li,X.
  TITLE     Aldehyde oxidase 1 promoted the occurrence and development of
            colorectal cancer by up-regulation of expression of CD133
  JOURNAL   Int Immunopharmacol 85, 106618 (2020)
   PUBMED   32470878
  REMARK    GeneRIF: Aldehyde oxidase 1 promoted the occurrence and development
            of colorectal cancer by up-regulation of expression of CD133.
REFERENCE   6  (residues 1 to 1338)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   7  (residues 1 to 1338)
  AUTHORS   Ichida,K., Matsumura,T., Sakuma,R., Hosoya,T. and Nishino,T.
  TITLE     Mutation of human molybdenum cofactor sulfurase gene is responsible
            for classical xanthinuria type II
  JOURNAL   Biochem Biophys Res Commun 282 (5), 1194-1200 (2001)
   PUBMED   11302742
REFERENCE   8  (residues 1 to 1338)
  AUTHORS   Berger,R., Mezey,E., Clancy,K.P., Harta,G., Wright,R.M.,
            Repine,J.E., Brown,R.H., Brownstein,M. and Patterson,D.
  TITLE     Analysis of aldehyde oxidase and xanthine dehydrogenase/oxidase as
            possible candidate genes for autosomal recessive familial
            amyotrophic lateral sclerosis
  JOURNAL   Somat Cell Mol Genet 21 (2), 121-131 (1995)
   PUBMED   7570184
REFERENCE   9  (residues 1 to 1338)
  AUTHORS   Rodrigues,A.D.
  TITLE     Comparison of levels of aldehyde oxidase with cytochrome P450
            activities in human liver in vitro
  JOURNAL   Biochem Pharmacol 48 (1), 197-200 (1994)
   PUBMED   8043023
REFERENCE   10 (residues 1 to 1338)
  AUTHORS   Wright,R.M., Vaitaitis,G.M., Wilson,C.M., Repine,T.B., Terada,L.S.
            and Repine,J.E.
  TITLE     cDNA cloning, characterization, and tissue-specific expression of
            human xanthine dehydrogenase/xanthine oxidase
  JOURNAL   Proc Natl Acad Sci U S A 90 (22), 10690-10694 (1993)
   PUBMED   8248161
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC080164.6 and AC007163.3.
            
            On Aug 3, 2005 this sequence version replaced NP_001150.2.
            
            Summary: Aldehyde oxidase produces hydrogen peroxide and, under
            certain conditions, can catalyze the formation of superoxide.
            Aldehyde oxidase is a candidate gene for amyotrophic lateral
            sclerosis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L11005.1, SRR1660803.14342.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374700.7/ ENSP00000363832.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..1338
                     /product="aldehyde oxidase"
                     /EC_number="1.2.3.1"
                     /note="azaheterocycle hydroxylase"
                     /calculated_mol_wt=147788
     Region          5..1338
                     /region_name="mam_aldehyde_ox"
                     /note="aldehyde oxidase; TIGR02969"
                     /db_xref="CDD:132014"
     Site            1068
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06278.2)"
     CDS             1..1338
                     /gene="AOX1"
                     /gene_synonym="AO; AOH1"
                     /coded_by="NM_001159.4:96..4112"
                     /db_xref="CCDS:CCDS33360.1"
                     /db_xref="GeneID:316"
                     /db_xref="HGNC:HGNC:553"
                     /db_xref="MIM:602841"
ORIGIN      
        1 mdrasellfy vngrkviekn vdpetmllpy lrkklrltgt kygcggggcg actvmisryn
       61 pitkrirhhp anaclipics lygaavttve gigsthtrih pvqeriakch gtqcgfctpg
      121 mvmsiytllr nhpeptldql tdalggnlcr ctgyrpiida cktfcktsgc cqskengvcc
      181 ldqginglpe feegsktspk lfaeeeflpl dptqelifpp elmimaekqs qrtrvfgser
      241 mmwfspvtlk ellefkfkyp qapvimgnts vgpevkfkgv fhpviispdr ieelsvvnha
      301 yngltlgagl slaqvkdila dvvqklpeek tqmyhallkh lgtlagsqir nmaslgghii
      361 srhpdsdlnp ilavgnctln llskegkrqi plneqflskc pnadlkpqei lvsvnipysr
      421 kwefvsafrq aqrqenalai vnsgmrvffg egdgiirelc isyggvgpat icaknscqkl
      481 igrhwneqml diacrlilne vsllgsapgg kvefkrtlii sflfkfylev sqilkkmdpv
      541 hypsladkye saledlhskh hcstlkyqni gpkqhpedpi ghpimhlsgv khatgeaiyc
      601 ddmplvdqel fltfvtssra hakivsidls ealsmpgvvd imtaehlsdv nsfcffteae
      661 kflatdkvfc vgqlvcavla dsevqakraa krvkivyqdl epliltiees iqhnssfkpe
      721 rkleygnvde afkvvdqile geihmggqeh fymetqsmlv vpkgedqemd vyvstqfpky
      781 iqdivastlk lpankvmchv rrvggafggk vlktgiiaav tafaankhgr avrcvlerge
      841 dmlitggrhp ylgkykagfm ndgrilaldm ehysnagasl deslfviemg llkmdnaykf
      901 pnlrcrgwac rtnlpsntaf rgfgfpqaal itesciteva akcglspekv riinmykeid
      961 qtpykqeina knliqcwrec mamssyslrk vavekfnaen ywkkkglamv plkfpvglgs
     1021 raagqaaalv hiyldgsvlv thggiemgqg vhtkmiqvvs relrmpmsnv hlrgtstetv
     1081 pnanisggsv vadlnglavk dacqtllkrl epiisknpkg twkdwaqtaf desinlsavg
     1141 yfrgyesdmn wekgegqpfe yfvygaacse veidcltgdh knirtdivmd vgcsinpaid
     1201 igqiegafiq gmglytieel nyspqgilht rgpdqykipa icdmptelhi allppsqnsn
     1261 tlysskglge sgvflgcsvf faihdavsaa rqerglhgpl tlnspltpek irmacedkft
     1321 kmiprdepgs yvpwnvpi
//
LOCUS       NP_665823                620 aa            linear   ROD 27-APR-2025
DEFINITION  ran-binding protein 10 [Mus musculus].
ACCESSION   NP_665823
VERSION     NP_665823.3
DBSOURCE    REFSEQ: accession NM_145824.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   3  (residues 1 to 620)
  AUTHORS   Meyer,I., Kunert,S., Schwiebert,S., Hagedorn,I., Italiano,J.E. Jr.,
            Dutting,S., Nieswandt,B., Bachmann,S. and Schulze,H.
  TITLE     Altered microtubule equilibrium and impaired thrombus stability in
            mice lacking RanBP10
  JOURNAL   Blood 120 (17), 3594-3602 (2012)
   PUBMED   22936655
  REMARK    GeneRIF: RanBP10 inhibits premature microtubule polymerization of
            beta1-tubulin and plays a pivotal role in thrombus stabilization.
REFERENCE   4  (residues 1 to 620)
  AUTHORS   Hosono,K., Noda,S., Shimizu,A., Nakanishi,N., Ohtsubo,M.,
            Shimizu,N. and Minoshima,S.
  TITLE     YPEL5 protein of the YPEL gene family is involved in the cell cycle
            progression by interacting with two distinct proteins RanBPM and
            RanBP10
  JOURNAL   Genomics 96 (2), 102-111 (2010)
   PUBMED   20580816
REFERENCE   5  (residues 1 to 620)
  AUTHORS   Kunert,S., Meyer,I., Fleischhauer,S., Wannack,M., Fiedler,J.,
            Shivdasani,R.A. and Schulze,H.
  TITLE     The microtubule modulator RanBP10 plays a critical role in
            regulation of platelet discoid shape and degranulation
  JOURNAL   Blood 114 (27), 5532-5540 (2009)
   PUBMED   19801445
  REMARK    GeneRIF: Data suggest that RanBP10 plays an essential role in
            hemostasis and in maintaining microtubule dynamics with respect to
            both platelet shape and function.
REFERENCE   6  (residues 1 to 620)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   7  (residues 1 to 620)
  AUTHORS   Wang,D., Li,Z., Schoen,S.R., Messing,E.M. and Wu,G.
  TITLE     A novel MET-interacting protein shares high sequence similarity
            with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling
  JOURNAL   Biochem Biophys Res Commun 313 (2), 320-326 (2004)
   PUBMED   14684163
REFERENCE   8  (residues 1 to 620)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 620)
  AUTHORS   Wang,D., Li,Z., Messing,E.M. and Wu,G.
  TITLE     Activation of Ras/Erk pathway by a novel MET-interacting protein
            RanBPM
  JOURNAL   J Biol Chem 277 (39), 36216-36222 (2002)
   PUBMED   12147692
REFERENCE   10 (residues 1 to 620)
  AUTHORS   Hemberger,M., Himmelbauer,H., Ruschmann,J., Zeitz,C. and Fundele,R.
  TITLE     cDNA subtraction cloning reveals novel genes whose temporal and
            spatial expression indicates association with trophoblast invasion
  JOURNAL   Dev Biol 222 (1), 158-169 (2000)
   PUBMED   10885754
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC152826.2.
            
            On Mar 5, 2019 this sequence version replaced NP_665823.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC024698.1, AY337314.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164140, SAMN01164143
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 53.04 cM"
     Protein         1..620
                     /product="ran-binding protein 10"
                     /calculated_mol_wt=67058
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6VN19.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q6VN20; propagated from
                     UniProtKB/Swiss-Prot (Q6VN19.2)"
     Region          77..219
                     /region_name="SPRY_RanBP9_10"
                     /note="SPRY domain in Ran binding proteins 9 and 10;
                     cd12909"
                     /db_xref="CDD:293966"
     Region          257..284
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          291..>345
                     /region_name="CTLH"
                     /note="CTLH/CRA C-terminal to LisH motif domain;
                     pfam10607"
                     /db_xref="CDD:402305"
     Region          347..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6VN19.2)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6VN20; propagated from
                     UniProtKB/Swiss-Prot (Q6VN19.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6VN19.2)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6VN19.2)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6VN19.2)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6VN19.2)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6VN20; propagated from
                     UniProtKB/Swiss-Prot (Q6VN19.2)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6VN19.2)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6VN19.2)"
     Region          507..604
                     /region_name="CRA"
                     /note="CT11-RanBPM; smart00757"
                     /db_xref="CDD:214806"
     CDS             1..620
                     /gene="Ranbp10"
                     /gene_synonym="4432417N03Rik"
                     /coded_by="NM_145824.5:25..1887"
                     /db_xref="CCDS:CCDS22613.1"
                     /db_xref="GeneID:74334"
                     /db_xref="MGI:MGI:1921584"
ORIGIN      
        1 maaatadpga gnpqagdssg gdsggglpsp geqelsrrlq rlypavnqhe tplprswspk
       61 dkynyiglsq gnlrvhykgh gknhkdaasv rathpipaac giyyfevkiv skgrdgymgi
      121 glsaqgvnmn rlpgwdkhsy gyhgddghsf cssgtgqpyg ptfttgdvig ccvnlingtc
      181 fytknghslg iaftdlpanl yptvglqtpg eivdanfgqq pflfdiedym rewrakvqgt
      241 vhgfpisarl gewqavlqnm vssylvhhgy cstatafarm tetpiqeeqa siknrqkiqk
      301 lvlegrvgea iettqrfypg llehnpnllf mlkcrqfvem vngtdsevrs lssrspksqd
      361 sypgspslsp rhgpssshih ntgadspscs ngvastknkq nhskypapss ssssssssss
      421 sspssvnyse snstdstksq phsstsnqet sdsememeae hypngvlesv strivngayk
      481 hddlqtdess mddghprrql cggnqaater iilfgrelqa lseqlgreyg knlahtemlq
      541 dafsllaysd pwscpvghql dpiqrepvca alnsailesq nlpkqpplml algqaseclr
      601 lmaraglgsc sfarvddylh
//
LOCUS       NP_001146                673 aa            linear   PRI 27-APR-2025
DEFINITION  annexin A6 isoform 1 [Homo sapiens].
ACCESSION   NP_001146
VERSION     NP_001146.2
DBSOURCE    REFSEQ: accession NM_001155.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Yang,Y., Huang,L., Zhang,N., Deng,Y.N., Cao,X., Liang,Y., Hou,H.,
            Luo,Y., Yang,Y., Li,Q. and Liang,S.
  TITLE     SUMOylation of annexin A6 retards cell migration and tumor growth
            by suppressing RHOU/AKT1-involved EMT in hepatocellular carcinoma
  JOURNAL   Cell Commun Signal 22 (1), 206 (2024)
   PUBMED   38566133
  REMARK    GeneRIF: SUMOylation of annexin A6 retards cell migration and tumor
            growth by suppressing RHOU/AKT1-involved EMT in hepatocellular
            carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Wang,Y., Yang,Z., Wang,R., Zheng,Y., Han,Z., Fan,J., Yan,F., Liu,P.
            and Luo,Y.
  TITLE     Annexin A6 mitigates neurological deficit in ischemia/reperfusion
            injury by promoting synaptic plasticity
  JOURNAL   CNS Neurosci Ther 30 (2), e14639 (2024)
   PUBMED   38380783
  REMARK    GeneRIF: Annexin A6 mitigates neurological deficit in
            ischemia/reperfusion injury by promoting synaptic plasticity.
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Huang,B. and Yang,K.
  TITLE     Comprehensive analysis the diagnosis, malignant progression and
            immune infiltrate of ANXA6 in prostate cancer
  JOURNAL   Genes Genomics 45 (9), 1197-1209 (2023)
   PUBMED   37311953
  REMARK    GeneRIF: Comprehensive analysis the diagnosis, malignant
            progression and immune infiltrate of ANXA6 in prostate cancer.
            Erratum:[Genes Genomics. 2023 Jul 13. doi:
            10.1007/s13258-023-01425-2. PMID: 37450236]
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Gounou,C., Bouvet,F., Liet,B., Prouzet-Mauleon,V., d'Agata,L.,
            Harte,E., Argoul,F., Siegfried,G., Iggo,R., Khatib,A.M. and
            Bouter,A.
  TITLE     Annexin-A5 and annexin-A6 silencing prevents metastasis of breast
            cancer cells in zebrafish
  JOURNAL   Biol Cell 115 (6), e202200110 (2023)
   PUBMED   36958013
  REMARK    GeneRIF: Annexin-A5 and annexin-A6 silencing prevents metastasis of
            breast cancer cells in zebrafish.
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Williams,J.K., Ngo,J.M., Lehman,I.M. and Schekman,R.
  TITLE     Annexin A6 mediates calcium-dependent exosome secretion during
            plasma membrane repair
  JOURNAL   Elife 12, e86556 (2023)
   PUBMED   37204294
  REMARK    GeneRIF: Annexin A6 mediates calcium-dependent exosome secretion
            during plasma membrane repair.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Moss,S.E., Jacob,S.M., Davies,A.A. and Crumpton,M.J.
  TITLE     A growth-dependent post-translational modification of annexin VI
  JOURNAL   Biochim Biophys Acta 1160 (1), 120-126 (1992)
   PUBMED   1420329
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Barel,M., Gauffre,A., Lyamani,F., Fiandino,A., Hermann,J. and
            Frade,R.
  TITLE     Intracellular interaction of EBV/C3d receptor (CR2) with p68, a
            calcium-binding protein present in normal but not in transformed B
            lymphocytes
  JOURNAL   J Immunol 147 (4), 1286-1291 (1991)
   PUBMED   1831222
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Blackwood,R.A. and Ernst,J.D.
  TITLE     Characterization of Ca2(+)-dependent phospholipid binding, vesicle
            aggregation and membrane fusion by annexins
  JOURNAL   Biochem J 266 (1), 195-200 (1990)
   PUBMED   2138016
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Yoshizaki,H., Mizoguchi,T., Arai,K., Shiratsuchi,M., Shidara,Y. and
            Maki,M.
  TITLE     Structure and properties of calphobindin II, an anticoagulant
            protein from human placenta
  JOURNAL   J Biochem 107 (1), 43-50 (1990)
   PUBMED   2139657
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Iwasaki,A., Suda,M., Watanabe,M., Nakao,H., Hattori,Y., Nagoya,T.,
            Saino,Y., Shidara,Y. and Maki,M.
  TITLE     Structure and expression of cDNA for calphobindin II, a human
            placental coagulation inhibitor
  JOURNAL   J Biochem 106 (1), 43-49 (1989)
   PUBMED   2528541
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC411634.1, BC017046.1,
            AI566871.1 and AC008641.7.
            
            On Aug 3, 2005 this sequence version replaced NP_001146.1.
            
            Summary: Annexin VI belongs to a family of calcium-dependent
            membrane and phospholipid binding proteins. Several members of the
            annexin family have been implicated in membrane-related events
            along exocytotic and endocytotic pathways. The annexin VI gene is
            approximately 60 kbp long and contains 26 exons. It encodes a
            protein of about 68 kDa that consists of eight 68-amino acid
            repeats separated by linking sequences of variable lengths. It is
            highly similar to human annexins I and II sequences, each of which
            contain four such repeats. Annexin VI has been implicated in
            mediating the endosome aggregation and vesicle fusion in secreting
            epithelia during exocytosis. Alternatively spliced transcript
            variants have been described. [provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.179629.1, HM005611.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354546.10/ ENSP00000346550.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..673
                     /product="annexin A6 isoform 1"
                     /note="annexin VI (p68); calcium-binding protein p68;
                     calphobindin II; calelectrin; annexin-6; lipocortin VI;
                     chromobindin-20; 67 kDa calelectrin; testis secretory
                     sperm-binding protein Li 198a"
                     /calculated_mol_wt=75742
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Region          20..91
                     /region_name="Annexin 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P08133.3)"
     Region          24..89
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Site            63
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Site            68
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Site            75
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Site            81
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Region          92..163
                     /region_name="Annexin 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P08133.3)"
     Region          97..161
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          175..247
                     /region_name="Annexin 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P08133.3)"
     Region          179..245
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P14824; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Region          251..322
                     /region_name="Annexin 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P08133.3)"
     Region          255..320
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            306
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Region          363..434
                     /region_name="Annexin 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P08133.3)"
     Region          368..432
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            370
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Site            418
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48037; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Region          435..506
                     /region_name="Annexin 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P08133.3)"
     Region          439..504
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            483
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Region          521..595
                     /region_name="Annexin 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P08133.3)"
     Region          527..593
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     Region          599..670
                     /region_name="Annexin 8.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P08133.3)"
     Region          603..668
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            620
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08133.3)"
     CDS             1..673
                     /gene="ANXA6"
                     /gene_synonym="ANX6; CBP68; CPB-II; p68; p70"
                     /coded_by="NM_001155.5:126..2147"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47315.1"
                     /db_xref="GeneID:309"
                     /db_xref="HGNC:HGNC:544"
                     /db_xref="MIM:114070"
ORIGIN      
        1 makpaqgaky rgsihdfpgf dpnqdaealy tamkgfgsdk eaildiitsr snrqrqevcq
       61 sykslygkdl iadlkyeltg kferlivglm rppaycdake ikdaisgigt dekclieila
      121 srtneqmhql vaaykdayer dleadiigdt sghfqkmlvv llqgtreedd vvsedlvqqd
      181 vqdlyeagel kwgtdeaqfi yilgnrskqh lrlvfdeylk ttgkpieasi rgelsgdfek
      241 lmlavvkcir stpeyfaerl fkamkglgtr dntlirimvs rseldmldir eifrtkyeks
      301 lysmikndts geykktllkl sggdddaagq ffpeaaqvay qmwelsavar velkgtvrpa
      361 ndfnpdadak alrkamkglg tdedtiidii thrsnvqrqq irqtfkshfg rdlmtdlkse
      421 isgdlarlil glmmppahyd akqlkkameg agtdekalie ilatrtnaei raineayked
      481 yhksledals sdtsghfrri lislatghre eggenldqar edaqvaaeil eiadtpsgdk
      541 tsletrfmti lctrsyphlr rvfqefikmt nydvehtikk emsgdvrdaf vaivqsvknk
      601 plffadklyk smkgagtdek tltrimvsrs eidllnirre fiekydkslh qaiegdtsgd
      661 flkallalcg ged
//
LOCUS       NP_004279                359 aa            linear   PRI 27-APR-2025
DEFINITION  cytohesin-interacting protein [Homo sapiens].
ACCESSION   NP_004279
VERSION     NP_004279.3
DBSOURCE    REFSEQ: accession NM_004288.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Tompkins,N., MacKenzie,B., Ward,C., Salgado,D., Leidal,A.,
            McCormick,C. and Pohajdak,B.
  TITLE     Cytohesin-associated scaffolding protein (CASP) is involved in
            migration and IFN-gamma secretion in natural killer cells
  JOURNAL   Biochem Biophys Res Commun 451 (2), 165-170 (2014)
   PUBMED   25058460
  REMARK    GeneRIF: CASP has a direct role in the secretion of IFN-gamma, and
            NK cell motility and ability to kill tumor cells. CASP polarizes to
            the leading edge of migrating NK cells, and to the immunological
            synapse when engaged with tumor cells.
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Boehm,T., Hofer,S., Winklehner,P., Kellersch,B., Geiger,C.,
            Trockenbacher,A., Neyer,S., Fiegl,H., Ebner,S., Ivarsson,L.,
            Schneider,R., Kremmer,E., Heufler,C. and Kolanus,W.
  TITLE     Attenuation of cell adhesion in lymphocytes is regulated by CYTIP,
            a protein which mediates signal complex sequestration
  JOURNAL   EMBO J 22 (5), 1014-1024 (2003)
   PUBMED   12606567
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Mansour,M., Lee,S.Y. and Pohajdak,B.
  TITLE     The N-terminal coiled coil domain of the cytohesin/ARNO family of
            guanine nucleotide exchange factors interacts with the scaffolding
            protein CASP
  JOURNAL   J Biol Chem 277 (35), 32302-32309 (2002)
   PUBMED   12052827
  REMARK    GeneRIF: observations suggest that CASP is a scaffolding protein
            that facilitates the function of at least one member of the
            cytohesin/ARNO family in response to specific cellular stimuli
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Tang,P., Cheng,T.P., Agnello,D., Wu,C.Y., Hissong,B.D.,
            Watford,W.T., Ahn,H.J., Galon,J., Moss,J., Vaughan,M., O'Shea,J.J.
            and Gadina,M.
  TITLE     Cybr, a cytokine-inducible protein that binds cytohesin-1 and
            regulates its activity
  JOURNAL   Proc Natl Acad Sci U S A 99 (5), 2625-2629 (2002)
   PUBMED   11867758
REFERENCE   9  (residues 1 to 359)
  AUTHORS   Kim,H.S.
  TITLE     Assignment of the human B3-1 gene (PSCDBP) to chromosome 2 band
            q11.2 by radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 84 (1-2), 95 (1999)
   PUBMED   10343115
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Dixon,B., Sahely,B., Liu,L. and Pohajdak,B.
  TITLE     Cloning a cDNA from human NK/T cells which codes for an unusual
            leucine zipper containing protein
  JOURNAL   Biochim Biophys Acta 1216 (2), 321-324 (1993)
   PUBMED   8241278
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB219691.1, BC036449.2 and
            AC019201.6.
            
            On Jun 2, 2004 this sequence version replaced NP_004279.2.
            
            Summary: The protein encoded by this gene contains 2 leucine zipper
            domains and a putative C-terminal nuclear targeting signal, but
            does not have any hydrophobic regions. This protein is expressed
            weakly in resting NK and T cells. The encoded protein modulates the
            activation of ARF genes by CYTH1. This protein interacts with CYTH1
            and SNX27 proteins and may act to sequester CYTH1 protein in the
            cytoplasm.[provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036449.2, SRR1803613.251262.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264192.8/ ENSP00000264192.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.1"
     Protein         1..359
                     /product="cytohesin-interacting protein"
                     /note="cytohesin binding protein HE; cytohesin binder and
                     regulator; cbp HE; cytohesin-associated scaffolding
                     protein; pleckstrin homology Sec7 and coiled-coil
                     domains-binding protein"
                     /calculated_mol_wt=39879
     Region          74..163
                     /region_name="PDZ_tamalin_CYTIP-like"
                     /note="PDZ domain of tamalin, cytohesin-1-interacting
                     protein (CYTIP), and related domains; cd06713"
                     /db_xref="CDD:467197"
     Site            order(87..93,112,115,144,148,151..152)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467197"
     Region          166..188
                     /region_name="Interaction with CYTH1"
                     /note="propagated from UniProtKB/Swiss-Prot (O60759.2)"
     CDS             1..359
                     /gene="CYTIP"
                     /gene_synonym="B3-1; CASP; CYBR; CYTHIP; HE; PSCDBP"
                     /coded_by="NM_004288.5:70..1149"
                     /db_xref="CCDS:CCDS2204.1"
                     /db_xref="GeneID:9595"
                     /db_xref="HGNC:HGNC:9506"
                     /db_xref="MIM:604448"
ORIGIN      
        1 mslqrllqhs sngnladfca gpayssystl tgsltmddnr riqmladtva tlprgrkqla
       61 ltrssslsdf swsqrklvtv ekqdnetfgf eiqsyrpqnq nacssemftl ickiqedspa
      121 hcaglqagdv laningvste gftykqvvdl irssgnllti etlngtmilk rteleaklqv
      181 lkqtlkqkwv eyrslqlqeh rllhgdaanc pslenmdlde lslfgplpgp gpalvdrnrl
      241 ssessckswl ssmtmdsedg yqtcvsedss rgafsrqtst ddecfipkeg ddflrrsssr
      301 rnrsisntss gsmsplwegn lssmfgtlpr ksrkgsvrkq llkfipglhr aveeeesrf
//
LOCUS       NP_919445                428 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF128 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_919445
VERSION     NP_919445.1
DBSOURCE    REFSEQ: accession NM_194463.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ray,P., Jaiswal,S., Ferrer-Torres,D., Wang,Z., Nancarrow,D.,
            Curtin,M., Martinho,M.S., Lacy,S.M., Kasturirangan,S., Thomas,D.,
            Spence,J.R., Truttmann,M.C., Lagisetty,K.H., Lawrence,T.S.,
            Wang,T.D., Beer,D.G. and Ray,D.
  TITLE     GRAIL1 Stabilizes Misfolded Mutant p53 through a Ubiquitin
            Ligase-Independent, Chaperone Regulatory Function
  JOURNAL   Mol Cancer Res 22 (11), 996-1010 (2024)
   PUBMED   39018356
  REMARK    GeneRIF: GRAIL1 Stabilizes Misfolded Mutant p53 through a Ubiquitin
            Ligase-Independent, Chaperone Regulatory Function.
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Huang,S., Zhao,J., Yu,H. and Chen,G.
  TITLE     Mechanism of tumor-derived extracellular vesicles in prostatic
            cancer progression through the circFMN2/KLF2/RNF128 axis
  JOURNAL   Apoptosis 28 (9-10), 1372-1389 (2023)
   PUBMED   37452271
  REMARK    GeneRIF: Mechanism of tumor-derived extracellular vesicles in
            prostatic cancer progression through the circFMN2/KLF2/RNF128 axis.
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Fujimoto,S., Kyuichi,K., Kaede,Y., Chihiro,Y., Emi,I., Ryo,I.,
            Reiji,H., Toshiki,Y. and Yokomise,H.
  TITLE     RNF128 expression in lung adenocarcinoma is a favorable prognostic
            factor associated with decreased tumor-associated macrophages
  JOURNAL   Thorac Cancer 14 (17), 1581-1588 (2023)
   PUBMED   37186218
  REMARK    GeneRIF: RNF128 expression in lung adenocarcinoma is a favorable
            prognostic factor associated with decreased tumor-associated
            macrophages.
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Zhuang,Y., Liu,P.F., Zhan,Y., Kong,D.L., Tian,F. and Zhao,P.
  TITLE     RING finger protein 128 (RNF128) regulates malignant biological
            behaviors of colorectal cancer cells via PI3K/AKT signaling pathway
  JOURNAL   Cell Biol Int 46 (10), 1604-1611 (2022)
   PUBMED   35723244
  REMARK    GeneRIF: RING finger protein 128 (RNF128) regulates malignant
            biological behaviors of colorectal cancer cells via PI3K/AKT
            signaling pathway.
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Ray,P., Nancarrow,D.J., Ferrer-Torres,D., Wang,Z., San Martinho,M.,
            Hinton,T., Wu,J.H., Wu,A., Turgeon,D.K., Hammer,M.A., Dame,M.K.,
            Lawrence,T.S., O'Brien,P.J., Spence,J.R., Beer,D.G. and Ray,D.
  TITLE     UBCH5 Family Members Differentially Impact Stabilization of Mutant
            p53 via RNF128 Iso1 During Barrett's Progression to Esophageal
            Adenocarcinoma
  JOURNAL   Cell Mol Gastroenterol Hepatol 13 (1), 129-149 (2022)
   PUBMED   34416429
  REMARK    GeneRIF: UBCH5 Family Members Differentially Impact Stabilization
            of Mutant p53 via RNF128 Iso1 During Barrett's Progression to
            Esophageal Adenocarcinoma.
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Kostianovsky,A.M., Maier,L.M., Baecher-Allan,C., Anderson,A.C. and
            Anderson,D.E.
  TITLE     Up-regulation of gene related to anergy in lymphocytes is
            associated with Notch-mediated human T cell suppression
  JOURNAL   J Immunol 178 (10), 6158-6163 (2007)
   PUBMED   17475842
  REMARK    GeneRIF: Inhibition of T cell activation is not due to apoptosis or
            disruption of proximal T- cell receptor signaling, but is
            associated with up-regulation of GRAIL in CD4+ T cells, with modest
            effects on other E3 ubiquitin ligases.
REFERENCE   7  (residues 1 to 428)
  AUTHORS   MacKenzie,D.A., Schartner,J., Lin,J., Timmel,A., Jennens-Clough,M.,
            Fathman,C.G. and Seroogy,C.M.
  TITLE     GRAIL is up-regulated in CD4+ CD25+ T regulatory cells and is
            sufficient for conversion of T cells to a regulatory phenotype
  JOURNAL   J Biol Chem 282 (13), 9696-9702 (2007)
   PUBMED   17259178
  REMARK    GeneRIF: Forced expression of GRAIL in a T cell line from a T-cell
            receptor transgenic mouse is sufficient for conversion of these
            cells to a regulatory phenotype.
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Ross,M.T., Grafham,D.V., Coffey,A.J., Scherer,S., McLay,K.,
            Muzny,D., Platzer,M., Howell,G.R., Burrows,C., Bird,C.P.,
            Frankish,A., Lovell,F.L., Howe,K.L., Ashurst,J.L., Fulton,R.S.,
            Sudbrak,R., Wen,G., Jones,M.C., Hurles,M.E., Andrews,T.D.,
            Scott,C.E., Searle,S., Ramser,J., Whittaker,A., Deadman,R.,
            Carter,N.P., Hunt,S.E., Chen,R., Cree,A., Gunaratne,P., Havlak,P.,
            Hodgson,A., Metzker,M.L., Richards,S., Scott,G., Steffen,D.,
            Sodergren,E., Wheeler,D.A., Worley,K.C., Ainscough,R.,
            Ambrose,K.D., Ansari-Lari,M.A., Aradhya,S., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Ballabio,A., Banerjee,R., Barker,G.E.,
            Barlow,K.F., Barrett,I.P., Bates,K.N., Beare,D.M., Beasley,H.,
            Beasley,O., Beck,A., Bethel,G., Blechschmidt,K., Brady,N.,
            Bray-Allen,S., Bridgeman,A.M., Brown,A.J., Brown,M.J., Bonnin,D.,
            Bruford,E.A., Buhay,C., Burch,P., Burford,D., Burgess,J.,
            Burrill,W., Burton,J., Bye,J.M., Carder,C., Carrel,L., Chako,J.,
            Chapman,J.C., Chavez,D., Chen,E., Chen,G., Chen,Y., Chen,Z.,
            Chinault,C., Ciccodicola,A., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S., Clerc-Blankenburg,K., Clifford,K., Cobley,V., Cole,C.G.,
            Conquer,J.S., Corby,N., Connor,R.E., David,R., Davies,J., Davis,C.,
            Davis,J., Delgado,O., Deshazo,D., Dhami,P., Ding,Y., Dinh,H.,
            Dodsworth,S., Draper,H., Dugan-Rocha,S., Dunham,A., Dunn,M.,
            Durbin,K.J., Dutta,I., Eades,T., Ellwood,M., Emery-Cohen,A.,
            Errington,H., Evans,K.L., Faulkner,L., Francis,F., Frankland,J.,
            Fraser,A.E., Galgoczy,P., Gilbert,J., Gill,R., Glockner,G.,
            Gregory,S.G., Gribble,S., Griffiths,C., Grocock,R., Gu,Y.,
            Gwilliam,R., Hamilton,C., Hart,E.A., Hawes,A., Heath,P.D.,
            Heitmann,K., Hennig,S., Hernandez,J., Hinzmann,B., Ho,S., Hoffs,M.,
            Howden,P.J., Huckle,E.J., Hume,J., Hunt,P.J., Hunt,A.R.,
            Isherwood,J., Jacob,L., Johnson,D., Jones,S., de Jong,P.J.,
            Joseph,S.S., Keenan,S., Kelly,S., Kershaw,J.K., Khan,Z.,
            Kioschis,P., Klages,S., Knights,A.J., Kosiura,A., Kovar-Smith,C.,
            Laird,G.K., Langford,C., Lawlor,S., Leversha,M., Lewis,L., Liu,W.,
            Lloyd,C., Lloyd,D.M., Loulseged,H., Loveland,J.E., Lovell,J.D.,
            Lozado,R., Lu,J., Lyne,R., Ma,J., Maheshwari,M., Matthews,L.H.,
            McDowall,J., McLaren,S., McMurray,A., Meidl,P., Meitinger,T.,
            Milne,S., Miner,G., Mistry,S.L., Morgan,M., Morris,S., Muller,I.,
            Mullikin,J.C., Nguyen,N., Nordsiek,G., Nyakatura,G., O'Dell,C.N.,
            Okwuonu,G., Palmer,S., Pandian,R., Parker,D., Parrish,J.,
            Pasternak,S., Patel,D., Pearce,A.V., Pearson,D.M., Pelan,S.E.,
            Perez,L., Porter,K.M., Ramsey,Y., Reichwald,K., Rhodes,S.,
            Ridler,K.A., Schlessinger,D., Schueler,M.G., Sehra,H.K.,
            Shaw-Smith,C., Shen,H., Sheridan,E.M., Shownkeen,R., Skuce,C.D.,
            Smith,M.L., Sotheran,E.C., Steingruber,H.E., Steward,C.A.,
            Storey,R., Swann,R.M., Swarbreck,D., Tabor,P.E., Taudien,S.,
            Taylor,T., Teague,B., Thomas,K., Thorpe,A., Timms,K., Tracey,A.,
            Trevanion,S., Tromans,A.C., d'Urso,M., Verduzco,D., Villasana,D.,
            Waldron,L., Wall,M., Wang,Q., Warren,J., Warry,G.L., Wei,X.,
            West,A., Whitehead,S.L., Whiteley,M.N., Wilkinson,J.E.,
            Willey,D.L., Williams,G., Williams,L., Williamson,A.,
            Williamson,H., Wilming,L., Woodmansey,R.L., Wray,P.W., Yen,J.,
            Zhang,J., Zhou,J., Zoghbi,H., Zorilla,S., Buck,D., Reinhardt,R.,
            Poustka,A., Rosenthal,A., Lehrach,H., Meindl,A., Minx,P.J.,
            Hillier,L.W., Willard,H.F., Wilson,R.K., Waterston,R.H., Rice,C.M.,
            Vaudin,M., Coulson,A., Nelson,D.L., Weinstock,G., Sulston,J.E.,
            Durbin,R., Hubbard,T., Gibbs,R.A., Beck,S., Rogers,J. and
            Bentley,D.R.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Soares,L., Seroogy,C., Skrenta,H., Anandasabapathy,N., Lovelace,P.,
            Chung,C.D., Engleman,E. and Fathman,C.G.
  TITLE     Two isoforms of otubain 1 regulate T cell anergy via GRAIL
  JOURNAL   Nat Immunol 5 (1), 45-54 (2004)
   PUBMED   14661020
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Anandasabapathy,N., Ford,G.S., Bloom,D., Holness,C., Paragas,V.,
            Seroogy,C., Skrenta,H., Hollenhorst,M., Fathman,C.G. and Soares,L.
  TITLE     GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene
            transcription is expressed in anergic CD4+ T cells
  JOURNAL   Immunity 18 (4), 535-547 (2003)
   PUBMED   12705856
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK074264.1, BI600046.1 and
            BC012931.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein that localizes to the endocytic pathway. This protein
            contains a RING zinc-finger motif and has been shown to possess E3
            ubiquitin ligase activity. Expression of this gene in retrovirally
            transduced T cell hybridoma significantly inhibits
            activation-induced IL2 and IL4 cytokine production. Induced
            expression of this gene was observed in anergic CD4(+) T cells,
            which suggested a role in the induction of anergic phenotype.
            Alternatively spliced transcript variants encoding distinct
            isoforms have been reported. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.179438.1, AK074264.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000255499.3/ ENSP00000255499.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.3"
     Protein         1..428
                     /product="E3 ubiquitin-protein ligase RNF128 isoform 1
                     precursor"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF128; gene related to
                     anergy in lymphocytes protein; RING-type E3 ubiquitin
                     transferase RNF128; ring finger protein 128, E3 ubiquitin
                     protein ligase"
                     /calculated_mol_wt=42764
     sig_peptide     1..38
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3775
     Region          48..193
                     /region_name="PA_GRAIL_like"
                     /note="PA _GRAIL_like: Protease-associated (PA) domain
                     GRAIL-like. This group includes PA domain containing E3
                     (ubiquitin ligases) similar to human GRAIL (gene related
                     to anergy in lymphocytes) protein. Proteins in this group
                     contain a C3H2C3 RING finger. E3...; cd02122"
                     /db_xref="CDD:239037"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TEB7.1)"
     Site            59
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TEB7.1)"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|Ref.12; propagated from
                     UniProtKB/Swiss-Prot (Q8TEB7.1)"
     Site            154..156
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:239037"
     Site            208..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEB7.1)"
     Region          275..323
                     /region_name="RING-H2_RNF128-like"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 128 (RNF128) and similar proteins; cd16802"
                     /db_xref="CDD:438454"
     Region          346..428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEB7.1)"
     CDS             1..428
                     /gene="RNF128"
                     /gene_synonym="GRAIL"
                     /coded_by="NM_194463.2:214..1500"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS14521.1"
                     /db_xref="GeneID:79589"
                     /db_xref="HGNC:HGNC:21153"
                     /db_xref="MIM:300439"
ORIGIN      
        1 mgpppgagvs crggcgfsrl lawcfllals pqapgsrgae avwtaylnvs wrvphtgvnr
       61 tvwelseegv ygqdsplepv agvlvppdgp galnacnpht nftvptvwgs tvqvswlali
      121 qrgggctfad kihlayerga sgavifnfpg trnevipmsh pgavdivaim ignlkgtkil
      181 qsiqrgiqvt mvievgkkhg pwvnhysiff vsvsffiita atvgyfifys arrlrnaraq
      241 srkqrqlkad akkaigrlql rtlkqgdkei gpdgdscavc ielykpndlv riltcnhifh
      301 ktcvdpwlle hrtcpmckcd ilkalgievd vedgsvslqv pvsneisnsa ssheednrse
      361 tassgyasvq gtdeppleeh vqstneslql vnheansvav dviphvdnpt feedetpnqe
      421 tavreiks
//
LOCUS       NP_689764                339 aa            linear   PRI 27-APR-2025
DEFINITION  U11/U12 small nuclear ribonucleoprotein 48 kDa protein [Homo
            sapiens].
ACCESSION   NP_689764
VERSION     NP_689764.3
DBSOURCE    REFSEQ: accession NM_152551.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Tidow,H., Andreeva,A., Rutherford,T.J. and Fersht,A.R.
  TITLE     Solution structure of the U11-48K CHHC zinc-finger domain that
            specifically binds the 5' splice site of U12-type introns
  JOURNAL   Structure 17 (2), 294-302 (2009)
   PUBMED   19217400
  REMARK    GeneRIF: A model in which the U11-48K Zn finger stabilizes U11-5'
            splice site base pairing and thus plays an important role during
            the minor spliceosome assembly.
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Turunen,J.J., Will,C.L., Grote,M., Luhrmann,R. and Frilander,M.J.
  TITLE     The U11-48K protein contacts the 5' splice site of U12-type introns
            and the U11-59K protein
  JOURNAL   Mol Cell Biol 28 (10), 3548-3560 (2008)
   PUBMED   18347052
  REMARK    GeneRIF: RNA interference-induced knockdown of 48K led to reduced
            cell growth and the inhibition of U12-type splicing, as well as the
            activation of cryptic, U2-type splice sites, suggesting that 48K
            plays a critical role in U12-type intron recognition.
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031058.1, AL832462.1, BC062458.1 and AL390026.1.
            
            On Jul 26, 2005 this sequence version replaced NP_689764.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.24205.1,
                                           SRR1803616.153226.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342415.6/ ENSP00000339834.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
     Protein         1..339
                     /product="U11/U12 small nuclear ribonucleoprotein 48 kDa
                     protein"
                     /note="U11/U12 snRNP 48K; small nuclear ribonucleoprotein
                     48kDa (U11/U12); U11/U12-48K; U11/U12 snRNP 48 kDa
                     protein; small nuclear ribonucleoprotein, U11/U12 48KDa
                     subunit; U11-48K"
                     /calculated_mol_wt=39834
     Region          57..79
                     /region_name="zf-U11-48K"
                     /note="U11-48K-like CHHC zinc finger; pfam05253"
                     /db_xref="CDD:461603"
     Region          255..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IEG0.2)"
     CDS             1..339
                     /gene="SNRNP48"
                     /gene_synonym="C6orf151; dJ336K20B.1; dJ512B11.2"
                     /coded_by="NM_152551.4:61..1080"
                     /db_xref="CCDS:CCDS4502.1"
                     /db_xref="GeneID:154007"
                     /db_xref="HGNC:HGNC:21368"
ORIGIN      
        1 megepppvee rrrlqeelne fvesgcrtle evtaslgwdl dsldpgeeea aedevvicpy
       61 dsnhhmpkss lakhmascrl rkmgytkeee demynpeffy envkipsitl nkdsqfqiik
      121 qartavgkds dcynqriyss lpvevplnhk rfvcdltqad rlalydfvve etkkkrsdsq
      181 iiendsdlfv dlaakinqdn srkspksyle ilaevrdykr rrqsyraknv hitkksytev
      241 irdvinvhme elsnhwqeeq ekaeddaekn eerrsasvds rqsggsylda ecsrhrrdrs
      301 rsphkrkrnk dkdkncesrr rkerdgerhh shkrrkqki
//
LOCUS       NP_001240312             204 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein eL15 isoform 1 [Homo sapiens].
ACCESSION   NP_001240312
VERSION     NP_001240312.1
DBSOURCE    REFSEQ: accession NM_001253383.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Wang,G., Qin,M., Zhang,B., Yan,Y., Yang,F., Chen,Q., Liu,Y.,
            Qiao,F. and Ni,Y.
  TITLE     Decreased expression of RPL15 and RPL18 exacerbated the
            calcification of valve interstitial cells during aortic valve
            calcification
  JOURNAL   Cell Biol Int 47 (10), 1749-1759 (2023)
   PUBMED   37431269
  REMARK    GeneRIF: Decreased expression of RPL15 and RPL18 exacerbated the
            calcification of valve interstitial cells during aortic valve
            calcification.
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Xu,C., He,X.Y., Ren,X.H., Han,D. and Cheng,S.X.
  TITLE     Detection of mRNAs of Ribosomal Protein L15 and E-Cadherin in
            Living Circulating Tumor Cells at Single Cell Resolution To Study
            Tumor Heterogeneity
  JOURNAL   Anal Chem 94 (30), 10610-10616 (2022)
   PUBMED   35856393
  REMARK    GeneRIF: Detection of mRNAs of Ribosomal Protein L15 and E-Cadherin
            in Living Circulating Tumor Cells at Single Cell Resolution To
            Study Tumor Heterogeneity.
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Wang,Q., Yang,C., Zhou,J., Wang,X., Wu,M. and Liu,Z.
  TITLE     Cloning and characterization of full-length human ribosomal protein
            L15 cDNA which was overexpressed in esophageal cancer
  JOURNAL   Gene 263 (1-2), 205-209 (2001)
   PUBMED   11223259
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Sieff,C.
  TITLE     Diamond-Blackfan Anemia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC351786.1, DA205054.1 and
            AC124914.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of four RNA species and approximately
            80 structurally distinct proteins. This gene encodes a member of
            the L15E family of ribosomal proteins and a component of the 60S
            subunit. This gene shares sequence similarity with the yeast
            ribosomal protein YL10 gene. Elevated expression of this gene has
            been observed in esophageal tumors and gastric cancer tissues, and
            deletion of this gene has been observed in a Diamond-Blackfan
            anemia (DBA) patient. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. Variants 1-5 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.243527.1,
                                           SRR1660809.125562.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.2"
     Protein         1..204
                     /product="large ribosomal subunit protein eL15 isoform 1"
                     /note="60S ribosomal protein L15; large ribosomal subunit
                     protein eL15"
                     /calculated_mol_wt=24015
     Region          2..191
                     /region_name="Ribosomal_L15e"
                     /note="Ribosomal L15; pfam00827"
                     /db_xref="CDD:459950"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61314; propagated from
                     UniProtKB/Swiss-Prot (P61313.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P61313.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P61313.2)"
     Region          165..186
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61313.2)"
     CDS             1..204
                     /gene="RPL15"
                     /gene_synonym="DBA12; EC45; eL15; L15; RPL10; RPLY10;
                     RPYL10"
                     /coded_by="NM_001253383.3:119..733"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS2640.1"
                     /db_xref="GeneID:6138"
                     /db_xref="HGNC:HGNC:10306"
                     /db_xref="MIM:604174"
ORIGIN      
        1 mgaykyiqel wrkkqsdvmr fllrvrcwqy rqlsalhrap rptrpdkarr lgykakqgyv
       61 iyrirvrrgg rkrpvpkgat ygkpvhhgvn qlkfarslqs vaeeragrhc galrvlnsyw
      121 vgedstykff evilidpfhk airrnpdtqw itkpvhkhre mrgltsagrk srglgkghkf
      181 hhtiggsrra awrrrntlql hryr
//
LOCUS       NP_001352156             358 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-dependent glucokinase isoform 6 precursor [Homo sapiens].
ACCESSION   NP_001352156 XP_011520404
VERSION     NP_001352156.1
DBSOURCE    REFSEQ: accession NM_001365227.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Herrera-Morande,A., Vallejos-Baccelliere,G., Cea,P.A., Zamora,R.A.,
            Cid,D., Maturana,P., Gonzalez-Ordenes,F., Castro-Fernandez,V. and
            Guixe,V.
  TITLE     Kinetic characterization and phylogenetic analysis of human
            ADP-dependent glucokinase reveal new insights into its regulatory
            properties
  JOURNAL   Arch Biochem Biophys 741, 109602 (2023)
   PUBMED   37084804
  REMARK    GeneRIF: Kinetic characterization and phylogenetic analysis of
            human ADP-dependent glucokinase reveal new insights into its
            regulatory properties.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Tandon,A., Birkenhagen,J., Nagalla,D., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase as a novel onco-target for haematological
            malignancies
  JOURNAL   Sci Rep 10 (1), 13584 (2020)
   PUBMED   32788680
  REMARK    GeneRIF: ADP-dependent glucokinase as a novel onco-target for
            haematological malignancies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Jiang,H.Y. and Wang,Z.J.
  TITLE     ADPGK-AS1 promotes the progression of colorectal cancer via
            sponging miR-525 to upregulate FUT1
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2380-2386 (2020)
   PUBMED   32196589
  REMARK    GeneRIF: ADPGK-AS1 promotes the progression of colorectal cancer
            via sponging miR-525 to upregulate FUT1.
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Imle,R., Wang,B.T., Stutzenberger,N., Birkenhagen,J., Tandon,A.,
            Carl,M., Himmelreich,N., Thiel,C., Grone,H.J., Poschet,G.,
            Volkers,M., Gulow,K., Schroder,A., Carillo,S., Mittermayr,S.,
            Bones,J., Kaminski,M.M., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing
  JOURNAL   Sci Rep 9 (1), 14248 (2019)
   PUBMED   31582762
  REMARK    GeneRIF: ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Richter,J.P., Goroncy,A.K., Ronimus,R.S. and Sutherland-Smith,A.J.
  TITLE     The Structural and Functional Characterization of Mammalian
            ADP-dependent Glucokinase
  JOURNAL   J Biol Chem 291 (8), 3694-3704 (2016)
   PUBMED   26555263
  REMARK    GeneRIF: ADPGK is substrate inhibited by high glucose concentration
            and shows high specificity for glucose, with no activity for other
            sugars, as determined by NMR spectroscopy, including 2-deoxyglucose
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Cuesta-Munoz,A.L., Tuomi,T., Cobo-Vuilleumier,N., Koskela,H.,
            Odili,S., Stride,A., Buettger,C., Otonkoski,T., Froguel,P.,
            Grimsby,J., Garcia-Gimeno,M. and Matschinsky,F.M.
  TITLE     Clinical heterogeneity in monogenic diabetes caused by mutations in
            the glucokinase gene (GCK-MODY)
  JOURNAL   Diabetes Care 33 (2), 290-292 (2010)
   PUBMED   19903754
  REMARK    GeneRIF: Glucose and insulin response to oral glucose is higher in
            GCK(261) carriers, indicating clinical heterogeneity in GCK
            maturity diabetes carriers.
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Codner,E., Rocha,A., Deng,L., Martinez-Aguayo,A., Godoy,C.,
            Mericq,V. and Chung,W.K.
  TITLE     Mild fasting hyperglycemia in children: high rate of glucokinase
            mutations and some risk of developing type 1 diabetes mellitus
  JOURNAL   Pediatr Diabetes 10 (6), 382-388 (2009)
   PUBMED   19309449
  REMARK    GeneRIF: The presence of mild persistent hyperglycemia in any
            patient without autoantibodies should lead to genetic analysis of
            glucokinase, particularly if there is a positive family history.
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Ronimus,R.S. and Morgan,H.W.
  TITLE     Cloning and biochemical characterization of a novel mouse
            ADP-dependent glucokinase
  JOURNAL   Biochem Biophys Res Commun 315 (3), 652-658 (2004)
   PUBMED   14975750
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009712.22 and BI906568.1.
            
            On Aug 9, 2018 this sequence version replaced XP_011520404.1.
            
            Summary: ADPGK (EC 2.7.1.147) catalyzes the ADP-dependent
            phosphorylation of glucose to glucose-6-phosphate and may play a
            role in glycolysis, possibly during ischemic conditions (Ronimus
            and Morgan, 2004 [PubMed 14975750]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.16980.1, BI906568.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..358
                     /product="ADP-dependent glucokinase isoform 6 precursor"
                     /EC_number="2.7.1.147"
                     /note="ATP-dependent glucokinase; rbBP-35"
                     /calculated_mol_wt=36657
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1854
     Region          60..353
                     /region_name="ribokinase_pfkB_like"
                     /note="ribokinase/pfkB superfamily: Kinases that accept a
                     wide variety of substrates, including carbohydrates and
                     aromatic small molecules, all are phosphorylated at a
                     hydroxyl group. The superfamily includes ribokinase,
                     fructokinase, ketohexokinase; cl00192"
                     /db_xref="CDD:469648"
     Site            order(162,339,342)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238177"
     Site            order(186,243,337,340..341,344)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238177"
     CDS             1..358
                     /gene="ADPGK"
                     /gene_synonym="2610017G09Rik; ADP-GK"
                     /coded_by="NM_001365227.1:68..1144"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:83440"
                     /db_xref="HGNC:HGNC:25250"
                     /db_xref="MIM:611861"
ORIGIN      
        1 malwrgsaya gflalavgcv fllepelpgs alrslwsslc lgpapappgp vspegrlaaa
       61 wdalivrpvr rwrrvavgvn acvdvvlsgv kllqalglsp gngkdhsilh srndleeafi
      121 hfmgkgaaae rffsdketfh diaqvasefp gaqhyvggna aligqkfaan sdlkqvfpav
      181 tslglneqel lfltqsasgp hsslsswngv pdvgmvsdil fwilkehgrs ksrasdltri
      241 hfhtlvyhil atvdghwanq laavaagarv agtqacatet idtsrvslra pqefmtshse
      301 agsrivlnpn kpvvewhreg isfhftpvlv ckdpirtvgl gdaisaeglf ysevhphy
//
LOCUS       NP_005915                304 aa            linear   PRI 27-APR-2025
DEFINITION  homeobox protein MOX-2 [Homo sapiens].
ACCESSION   NP_005915
VERSION     NP_005915.2
DBSOURCE    REFSEQ: accession NM_005924.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Schonrock,A., Heinzelmann,E., Steffl,B., Demirdizen,E.,
            Narayanan,A., Krunic,D., Bahr,M., Park,J.W., Schmidt,C.,
            Ozduman,K., Pamir,M.N., Wick,W., Bestvater,F., Weichenhan,D.,
            Plass,C., Taranda,J., Mall,M. and Turcan,S.
  TITLE     MEOX2 homeobox gene promotes growth of malignant gliomas
  JOURNAL   Neuro Oncol 24 (11), 1911-1924 (2022)
   PUBMED   35468210
  REMARK    GeneRIF: MEOX2 homeobox gene promotes growth of malignant gliomas.
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Wang,H., Tang,Y., Wang,M., Zhao,J., Ding,C., Yang,X., Han,P. and
            Liu,P.
  TITLE     Low expression of MEOX2 is associated with poor survival in
            patients with breast cancer
  JOURNAL   Biomark Med 16 (16), 1161-1170 (2022)
   PUBMED   36625258
  REMARK    GeneRIF: Low expression of MEOX2 is associated with poor survival
            in patients with breast cancer.
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Wang,J., Chen,Y., Wang,Q., Xu,H., Wu,C., Jiang,Q., Wu,G., Zhou,H.,
            Xiao,Z., Chen,Y., Zhang,T. and Lan,Q.
  TITLE     MEOX2-mediated regulation of Cathepsin S promotes cell
            proliferation and motility in glioma
  JOURNAL   Cell Death Dis 13 (4), 360 (2022)
   PUBMED   35436995
  REMARK    GeneRIF: MEOX2-mediated regulation of Cathepsin S promotes cell
            proliferation and motility in glioma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Cai,Y., Liu,Y., Sun,Y. and Ren,Y.
  TITLE     Mesenchyme homeobox 2 has a cancer-inhibiting function in breast
            carcinoma via affection of the PI3K/AKT/mTOR and ERK1/2 pathways
  JOURNAL   Biochem Biophys Res Commun 593, 20-27 (2022)
   PUBMED   35051778
  REMARK    GeneRIF: Mesenchyme homeobox 2 has a cancer-inhibiting function in
            breast carcinoma via affection of the PI3K/AKT/mTOR and ERK1/2
            pathways.
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Yu,R., Zhang,J., Zhuo,Y., Hong,X., Ye,J., Tang,S. and Zhang,Y.
  TITLE     Identification of Diagnostic Signatures and Immune Cell
            Infiltration Characteristics in Rheumatoid Arthritis by Integrating
            Bioinformatic Analysis and Machine-Learning Strategies
  JOURNAL   Front Immunol 12, 724934 (2021)
   PUBMED   34691030
  REMARK    GeneRIF: Identification of Diagnostic Signatures and Immune Cell
            Infiltration Characteristics in Rheumatoid Arthritis by Integrating
            Bioinformatic Analysis and Machine-Learning Strategies.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Quinn,L.M., Latham,S.E. and Kalionis,B.
  TITLE     The homeobox genes MSX2 and MOX2 are candidates for regulating
            epithelial-mesenchymal cell interactions in the human placenta
  JOURNAL   Placenta 21 Suppl A, S50-S54 (2000)
   PUBMED   10831122
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Quinn,L.M., Johnson,B.V., Nicholl,J., Sutherland,G.R. and
            Kalionis,B.
  TITLE     Isolation and identification of homeobox genes from the human
            placenta including a novel member of the Distal-less family, DLX4
  JOURNAL   Gene 187 (1), 55-61 (1997)
   PUBMED   9073066
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Grigoriou,M., Kastrinaki,M.C., Modi,W.S., Theodorakis,K.,
            Mankoo,B., Pachnis,V. and Karagogeos,D.
  TITLE     Isolation of the human MOX2 homeobox gene and localization to
            chromosome 7p22.1-p21.3
  JOURNAL   Genomics 26 (3), 550-555 (1995)
   PUBMED   7607679
REFERENCE   9  (residues 1 to 304)
  AUTHORS   LePage,D.F., Altomare,D.A., Testa,J.R. and Walsh,K.
  TITLE     Molecular cloning and localization of the human GAX gene to 7p21
  JOURNAL   Genomics 24 (3), 535-540 (1994)
   PUBMED   7713505
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Reardon,W., McManus,S.P., Summers,D. and Winter,R.M.
  TITLE     Cytogenetic evidence that the Saethre-Chotzen gene maps to 7p21.2
  JOURNAL   Am J Med Genet 47 (5), 633-636 (1993)
   PUBMED   8266988
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA586635.1, BC017021.1 and
            BQ025060.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 30, 2005 this sequence version replaced NP_005915.1.
            
            Summary: This gene encodes a member of a subfamily of
            non-clustered, diverged, antennapedia-like homeobox-containing
            genes. The encoded protein may play a role in the regulation of
            vertebrate limb myogenesis. Mutations in the related mouse protein
            may be associated with craniofacial and/or skeletal abnormalities,
            in addition to neurovascular dysfunction observed in Alzheimer's
            disease. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017021.1, X82629.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162568, SAMEA2467143
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262041.6/ ENSP00000262041.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.2"
     Protein         1..304
                     /product="homeobox protein MOX-2"
                     /note="growth arrest-specific homeobox"
                     /calculated_mol_wt=33463
     Region          63..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50222.2)"
     Region          160..284
                     /region_name="COG5576"
                     /note="Homeodomain-containing transcription factor
                     [Transcription]"
                     /db_xref="CDD:227863"
     Region          188..244
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..304
                     /gene="MEOX2"
                     /gene_synonym="GAX; MOX2"
                     /coded_by="NM_005924.5:282..1196"
                     /db_xref="CCDS:CCDS34605.1"
                     /db_xref="GeneID:4223"
                     /db_xref="HGNC:HGNC:7014"
                     /db_xref="MIM:600535"
ORIGIN      
        1 mehplfgclr sphataqglh pfsqsslalh grsdhmsype lstsssscii agypneegmf
       61 asqhhrghhh hhhhhhhhhh qqqqhqalqt nwhlpqmssp psaarhslcl qpdsggppel
      121 gssppvlcsn ssslgsstpt gaacapgdyg rqalspaeae krsggkrksd ssdsqegnyk
      181 sevnskprke rtaftkeqir eleaefahhn yltrlrryei avnldlterq vkvwfqnrrm
      241 kwkrvkggqq gaaarekelv nvkkgtllps elsgigaatl qqtgdsiane dshdsdhsse
      301 hahl
//
LOCUS       NP_001349037             706 aa            linear   ROD 27-APR-2025
DEFINITION  integrator complex subunit 13 isoform 4 [Mus musculus].
ACCESSION   NP_001349037 XP_006507172
VERSION     NP_001349037.1
DBSOURCE    REFSEQ: accession NM_001362108.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Jodoin,J.N., Sitaram,P., Albrecht,T.R., May,S.B., Shboul,M.,
            Lee,E., Reversade,B., Wagner,E.J. and Lee,L.A.
  TITLE     Nuclear-localized Asunder regulates cytoplasmic dynein localization
            via its role in the integrator complex
  JOURNAL   Mol Biol Cell 24 (18), 2954-2965 (2013)
   PUBMED   23904267
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Jodoin,J.N., Shboul,M., Sitaram,P., Zein-Sabatto,H., Reversade,B.,
            Lee,E. and Lee,L.A.
  TITLE     Human Asunder promotes dynein recruitment and centrosomal tethering
            to the nucleus at mitotic entry
  JOURNAL   Mol Biol Cell 23 (24), 4713-4724 (2012)
   PUBMED   23097494
REFERENCE   4  (residues 1 to 706)
  AUTHORS   Mu,X., Zhao,S., Pershad,R., Hsieh,T.F., Scarpa,A., Wang,S.W.,
            White,R.A., Beremand,P.D., Thomas,T.L., Gan,L. and Klein,W.H.
  TITLE     Gene expression in the developing mouse retina by EST sequencing
            and microarray analysis
  JOURNAL   Nucleic Acids Res 29 (24), 4983-4993 (2001)
   PUBMED   11812828
REFERENCE   5  (residues 1 to 706)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC124128.11.
            
            On Apr 6, 2018 this sequence version replaced XP_006507172.1.
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon and compared to variant 1. The resulting isoform (4) has the
            same N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.629539.1,
                                           SRR7345562.180846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164142, SAMN01164143
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 77.7 cM"
     Protein         1..706
                     /product="integrator complex subunit 13 isoform 4"
                     /note="cell cycle regulator Mat89Bb homolog; protein
                     asunder homolog; asunder, spermatogenesis regulator;
                     likely orthologue of H. sapiens chromosome 12 open reading
                     frame 11 (C12orf11); spermatogenesis associated 30;
                     spermatogenesis-associated protein 30"
                     /calculated_mol_wt=79873
     Region          4..692
                     /region_name="Mat89Bb"
                     /note="Cell cycle and development regulator Mat89Bb;
                     pfam10221"
                     /db_xref="CDD:463006"
     CDS             1..706
                     /gene="Ints13"
                     /gene_synonym="4933424B01Rik; Asun; Spata30"
                     /coded_by="NM_001362108.1:547..2667"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:71177"
                     /db_xref="MGI:MGI:1918427"
ORIGIN      
        1 mkifseshkt vfvvdhcpym aescrqhvef dmlvknrtqg iiplapisks lwtcsvessm
       61 eycrimydif pfkklvnfiv sdsgahvlns wtqedqnlqe lmaalatvgp pnpradpecc
      121 silhglvaav etlckiteyq heartllmen aervgnrgri icitnaksds hvrmledcvq
      181 etihehnkla ansdhlmqiq kcelvlihty pvgedslvsd rpkkelspvl tsevhsvrag
      241 rhlatklnvl vqqhfdlast titnipmkee qhantsanyd vellhhkdah vdflrsgdsh
      301 sgsssregpf ketvtlkwct prtnsielhy ctgayrispv dvnsrpsscl tnfllngrsv
      361 lleqprksgs kvishmlssh ggeiflhvls ssrsiledpp sisegcggrv tdyritdfge
      421 fmrenrltpf ldprykidas leiplerakd qlekhtrywp miisqttifn mqavvplagv
      481 ivkeslteed vlncqktiyn lvdmerkndp lpvstvgtrg kgpkrdeqyr imwneletlv
      541 rahisnsekh qrvleclmac rskppeeeer kkrgrkredr edkseqagke hgtekarpda
      601 drlkgilerg keelaeaevi kdspdspepp nkkplvetde tphmekskgp vsllslwsnr
      661 intansrkhq efagrlnsvn nraelyqhlk eengmetten gkasrq
//
LOCUS       NP_001357324             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357324
VERSION     NP_001357324.1
DBSOURCE    REFSEQ: accession NM_001370395.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1754117.1,
                                           SRR7346977.2198266.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370395.1:1504..3153"
                     /note="isoform 1 is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_060357                160 aa            linear   PRI 27-APR-2025
DEFINITION  CXXC motif containing zinc binding protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_060357
VERSION     NP_060357.1
DBSOURCE    REFSEQ: accession NM_017887.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   A Rahaman,S.N., Mat Yusop,J., Mohamed-Hussein,Z.A., Aizat,W.M.,
            Ho,K.L., Teh,A.H., Waterman,J., Tan,B.K., Tan,H.L., Li,A.Y.,
            Chen,E.S. and Ng,C.L.
  TITLE     Crystal structure and functional analysis of human C1ORF123
  JOURNAL   PeerJ 6, e5377 (2018)
   PUBMED   30280012
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Furukawa,Y., Lim,C., Tosha,T., Yoshida,K., Hagai,T., Akiyama,S.,
            Watanabe,S., Nakagome,K. and Shiro,Y.
  TITLE     Identification of a novel zinc-binding protein, C1orf123, as an
            interactor with a heavy metal-associated domain
  JOURNAL   PLoS One 13 (9), e0204355 (2018)
   PUBMED   30260988
  REMARK    GeneRIF: Study performed yeast two-hybrid screening of the human
            proteome and found an uncharacterized protein encoded as open
            reading frame 123 in chromosome 1 (C1orf123) that can interact
            specifically with the heavy metal-associated domain of a copper
            chaperone for superoxide dismutase.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Rahaman,S.N., Mat Yusop,J., Mohamed-Hussein,Z.A., Ho,K.L.,
            Teh,A.H., Waterman,J. and Ng,C.L.
  TITLE     Cloning, expression, purification, crystallization and X-ray
            crystallographic analysis of recombinant human C1ORF123 protein
  JOURNAL   Acta Crystallogr F Struct Biol Commun 72 (Pt 3), 207-213 (2016)
   PUBMED   26919524
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Mate,S.E., Brown,K.J. and Hoffman,E.P.
  TITLE     Integrated genomics and proteomics of the Torpedo californica
            electric organ: concordance with the mammalian neuromuscular
            junction
  JOURNAL   Skelet Muscle 1 (1), 20 (2011)
   PUBMED   21798097
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA305789.1, BC010908.1 and AK000587.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.85583.1,
                                           SRR5189661.184283.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294360.5/ ENSP00000294360.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..160
                     /product="CXXC motif containing zinc binding protein
                     isoform 1"
                     /note="UPF0587 protein C1orf123"
                     /calculated_mol_wt=17917
     Region          6..157
                     /region_name="CXXC_Zn-b_euk"
                     /note="CXXC motif containing zinc binding protein,
                     eukaryotic; pfam05907"
                     /db_xref="CDD:461777"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NWV4.1)"
     CDS             1..160
                     /gene="CZIB"
                     /gene_synonym="C1orf123"
                     /coded_by="NM_017887.3:60..542"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS576.1"
                     /db_xref="GeneID:54987"
                     /db_xref="HGNC:HGNC:26059"
ORIGIN      
        1 mgkialqlka tlenitnlrp vgedfrwylk mkcgncgeis dkwqyirlmd svalkggrgs
       61 asmvqkcklc arensieils stikpynaed nenfktivef ecrglepvdf qpqagfaaeg
      121 vesgtafsdi nlqekdwtdy dekaqesvgi yevthqfvkc
//
LOCUS       NP_079500                589 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 46 [Homo sapiens].
ACCESSION   NP_079500
VERSION     NP_079500.2
DBSOURCE    REFSEQ: accession NM_025224.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Wen,Y.C., Liu,C.L., Yeh,H.L., Chen,W.H., Jiang,K.C., Tram,V.T.N.,
            Hsiao,M., Huang,J., Chen,W.Y. and Liu,Y.N.
  TITLE     PCK1 regulates neuroendocrine differentiation in a positive
            feedback loop of LIF/ZBTB46 signalling in castration-resistant
            prostate cancer
  JOURNAL   Br J Cancer 126 (5), 778-790 (2022)
   PUBMED   34815524
  REMARK    GeneRIF: PCK1 regulates neuroendocrine differentiation in a
            positive feedback loop of LIF/ZBTB46 signalling in
            castration-resistant prostate cancer.
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Carrera,C., Carcel-Marquez,J., Cullell,N., Torres-Aguila,N.,
            Muino,E., Castillo,J., Sobrino,T., Campos,F., Rodriguez-Castro,E.,
            Llucia-Carol,L., Millan,M., Munoz-Narbona,L., Lopez-Cancio,E.,
            Bustamante,A., Ribo,M., Alvarez-Sabin,J., Jimenez-Conde,J.,
            Roquer,J., Giralt-Steinhauer,E., Soriano-Tarraga,C.,
            Mola-Caminal,M., Vives-Bauza,C., Navarro,R.D., Tur,S., Obach,V.,
            Arenillas,J.F., Segura,T., Serrano-Heras,G., Marti-Fabregas,J.,
            Delgado-Mederos,R., Freijo-Guerrero,M.M., Moniche,F., Cabezas,J.A.,
            Castellanos,M., Gallego-Fabrega,C., Gonzalez-Sanchez,J.,
            Krupinsky,J., Strbian,D., Tatlisumak,T., Thijs,V., Lemmens,R.,
            Slowik,A., Pera,J., Kittner,S., Cole,J., Heitsch,L., Ibanez,L.,
            Cruchaga,C., Lee,J.M., Montaner,J. and Fernandez-Cadenas,I.
  TITLE     Single nucleotide variations in ZBTB46 are associated with
            post-thrombolytic parenchymal haematoma
  JOURNAL   Brain 144 (8), 2416-2426 (2021)
   PUBMED   33723576
  REMARK    GeneRIF: Single nucleotide variations in ZBTB46 are associated with
            post-thrombolytic parenchymal haematoma.
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Chen,W.Y., Wen,Y.C., Lin,S.R., Yeh,H.L., Jiang,K.C., Chen,W.H.,
            Lin,Y.S., Zhang,Q., Liew,P.L., Hsiao,M., Huang,J. and Liu,Y.N.
  TITLE     Nerve growth factor interacts with CHRM4 and promotes
            neuroendocrine differentiation of prostate cancer and castration
            resistance
  JOURNAL   Commun Biol 4 (1), 22 (2021)
   PUBMED   33398073
  REMARK    GeneRIF: Nerve growth factor interacts with CHRM4 and promotes
            neuroendocrine differentiation of prostate cancer and castration
            resistance.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Wang,Y., Sun,H.Y., Kumar,S., Puerta,M.D.M., Jo,H. and Rezvan,A.
  TITLE     ZBTB46 is a shear-sensitive transcription factor inhibiting
            endothelial cell proliferation via gene expression regulation of
            cell cycle proteins
  JOURNAL   Lab Invest 99 (3), 305-318 (2019)
   PUBMED   29884909
  REMARK    GeneRIF: In vitro results using endothelial cells (ECs) showed that
            cell confluence and laminar shear stress, both known physiological
            conditions promoting EC quiescence, led to upregulation of ZBTB46
            expression.
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Chen,W.Y., Zeng,T., Wen,Y.C., Yeh,H.L., Jiang,K.C., Chen,W.H.,
            Zhang,Q., Huang,J. and Liu,Y.N.
  TITLE     Androgen deprivation-induced ZBTB46-PTGS1 signaling promotes
            neuroendocrine differentiation of prostate cancer
  JOURNAL   Cancer Lett 440-441, 35-46 (2019)
   PUBMED   30312731
  REMARK    GeneRIF: ZBTB46 is inversely correlated with SPDEF and is increased
            in higher tumor grades and small-cell NE prostate cancer (SCNC)
            patients, which are positively associated with PTGS1. Findings
            suggest that the induction of ZBTB46 results in increased PTGS1
            expression, which is associated with NEPC progression and linked to
            the dysregulation of the AR-SPDEF pathway.
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Sawcer,S., Hellenthal,G., Pirinen,M., Spencer,C.C.,
            Patsopoulos,N.A., Moutsianas,L., Dilthey,A., Su,Z., Freeman,C.,
            Hunt,S.E., Edkins,S., Gray,E., Booth,D.R., Potter,S.C., Goris,A.,
            Band,G., Oturai,A.B., Strange,A., Saarela,J., Bellenguez,C.,
            Fontaine,B., Gillman,M., Hemmer,B., Gwilliam,R., Zipp,F.,
            Jayakumar,A., Martin,R., Leslie,S., Hawkins,S., Giannoulatou,E.,
            D'alfonso,S., Blackburn,H., Martinelli Boneschi,F., Liddle,J.,
            Harbo,H.F., Perez,M.L., Spurkland,A., Waller,M.J., Mycko,M.P.,
            Ricketts,M., Comabella,M., Hammond,N., Kockum,I., McCann,O.T.,
            Ban,M., Whittaker,P., Kemppinen,A., Weston,P., Hawkins,C.,
            Widaa,S., Zajicek,J., Dronov,S., Robertson,N., Bumpstead,S.J.,
            Barcellos,L.F., Ravindrarajah,R., Abraham,R., Alfredsson,L.,
            Ardlie,K., Aubin,C., Baker,A., Baker,K., Baranzini,S.E.,
            Bergamaschi,L., Bergamaschi,R., Bernstein,A., Berthele,A.,
            Boggild,M., Bradfield,J.P., Brassat,D., Broadley,S.A., Buck,D.,
            Butzkueven,H., Capra,R., Carroll,W.M., Cavalla,P., Celius,E.G.,
            Cepok,S., Chiavacci,R., Clerget-Darpoux,F., Clysters,K., Comi,G.,
            Cossburn,M., Cournu-Rebeix,I., Cox,M.B., Cozen,W., Cree,B.A.,
            Cross,A.H., Cusi,D., Daly,M.J., Davis,E., de Bakker,P.I.,
            Debouverie,M., D'hooghe,M.B., Dixon,K., Dobosi,R., Dubois,B.,
            Ellinghaus,D., Elovaara,I., Esposito,F., Fontenille,C., Foote,S.,
            Franke,A., Galimberti,D., Ghezzi,A., Glessner,J., Gomez,R.,
            Gout,O., Graham,C., Grant,S.F., Guerini,F.R., Hakonarson,H.,
            Hall,P., Hamsten,A., Hartung,H.P., Heard,R.N., Heath,S., Hobart,J.,
            Hoshi,M., Infante-Duarte,C., Ingram,G., Ingram,W., Islam,T.,
            Jagodic,M., Kabesch,M., Kermode,A.G., Kilpatrick,T.J., Kim,C.,
            Klopp,N., Koivisto,K., Larsson,M., Lathrop,M., Lechner-Scott,J.S.,
            Leone,M.A., Leppa,V., Liljedahl,U., Bomfim,I.L., Lincoln,R.R.,
            Link,J., Liu,J., Lorentzen,A.R., Lupoli,S., Macciardi,F., Mack,T.,
            Marriott,M., Martinelli,V., Mason,D., McCauley,J.L., Mentch,F.,
            Mero,I.L., Mihalova,T., Montalban,X., Mottershead,J., Myhr,K.M.,
            Naldi,P., Ollier,W., Page,A., Palotie,A., Pelletier,J., Piccio,L.,
            Pickersgill,T., Piehl,F., Pobywajlo,S., Quach,H.L., Ramsay,P.P.,
            Reunanen,M., Reynolds,R., Rioux,J.D., Rodegher,M., Roesner,S.,
            Rubio,J.P., Ruckert,I.M., Salvetti,M., Salvi,E., Santaniello,A.,
            Schaefer,C.A., Schreiber,S., Schulze,C., Scott,R.J., Sellebjerg,F.,
            Selmaj,K.W., Sexton,D., Shen,L., Simms-Acuna,B., Skidmore,S.,
            Sleiman,P.M., Smestad,C., Sorensen,P.S., Sondergaard,H.B.,
            Stankovich,J., Strange,R.C., Sulonen,A.M., Sundqvist,E.,
            Syvanen,A.C., Taddeo,F., Taylor,B., Blackwell,J.M., Tienari,P.,
            Bramon,E., Tourbah,A., Brown,M.A., Tronczynska,E., Casas,J.P.,
            Tubridy,N., Corvin,A., Vickery,J., Jankowski,J., Villoslada,P.,
            Markus,H.S., Wang,K., Mathew,C.G., Wason,J., Palmer,C.N.,
            Wichmann,H.E., Plomin,R., Willoughby,E., Rautanen,A.,
            Winkelmann,J., Wittig,M., Trembath,R.C., Yaouanq,J.,
            Viswanathan,A.C., Zhang,H., Wood,N.W., Zuvich,R., Deloukas,P.,
            Langford,C., Duncanson,A., Oksenberg,J.R., Pericak-Vance,M.A.,
            Haines,J.L., Olsson,T., Hillert,J., Ivinson,A.J., De Jager,P.L.,
            Peltonen,L., Stewart,G.J., Hafler,D.A., Hauser,S.L., McVean,G.,
            Donnelly,P. and Compston,A.
  CONSRTM   International Multiple Sclerosis Genetics Consortium; Wellcome
            Trust Case Control Consortium 2
  TITLE     Genetic risk and a primary role for cell-mediated immune mechanisms
            in multiple sclerosis
  JOURNAL   Nature 476 (7359), 214-219 (2011)
   PUBMED   21833088
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 589)
  AUTHORS   Anderson,C.A., Boucher,G., Lees,C.W., Franke,A., D'Amato,M.,
            Taylor,K.D., Lee,J.C., Goyette,P., Imielinski,M., Latiano,A.,
            Lagace,C., Scott,R., Amininejad,L., Bumpstead,S., Baidoo,L.,
            Baldassano,R.N., Barclay,M., Bayless,T.M., Brand,S., Buning,C.,
            Colombel,J.F., Denson,L.A., De Vos,M., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Fehrmann,R.S., Floyd,J.A., Florin,T.,
            Franchimont,D., Franke,L., Georges,M., Glas,J., Glazer,N.L.,
            Guthery,S.L., Haritunians,T., Hayward,N.K., Hugot,J.P., Jobin,G.,
            Laukens,D., Lawrance,I., Lemann,M., Levine,A., Libioulle,C.,
            Louis,E., McGovern,D.P., Milla,M., Montgomery,G.W., Morley,K.I.,
            Mowat,C., Ng,A., Newman,W., Ophoff,R.A., Papi,L., Palmieri,O.,
            Peyrin-Biroulet,L., Panes,J., Phillips,A., Prescott,N.J.,
            Proctor,D.D., Roberts,R., Russell,R., Rutgeerts,P., Sanderson,J.,
            Sans,M., Schumm,P., Seibold,F., Sharma,Y., Simms,L.A.,
            Seielstad,M., Steinhart,A.H., Targan,S.R., van den Berg,L.H.,
            Vatn,M., Verspaget,H., Walters,T., Wijmenga,C., Wilson,D.C.,
            Westra,H.J., Xavier,R.J., Zhao,Z.Z., Ponsioen,C.Y., Andersen,V.,
            Torkvist,L., Gazouli,M., Anagnou,N.P., Karlsen,T.H., Kupcinskas,L.,
            Sventoraityte,J., Mansfield,J.C., Kugathasan,S., Silverberg,M.S.,
            Halfvarson,J., Rotter,J.I., Mathew,C.G., Griffiths,A.M., Gearry,R.,
            Ahmad,T., Brant,S.R., Chamaillard,M., Satsangi,J., Cho,J.H.,
            Schreiber,S., Daly,M.J., Barrett,J.C., Parkes,M., Annese,V.,
            Hakonarson,H., Radford-Smith,G., Duerr,R.H., Vermeire,S.,
            Weersma,R.K. and Rioux,J.D.
  TITLE     Meta-analysis identifies 29 additional ulcerative colitis risk
            loci, increasing the number of confirmed associations to 47
  JOURNAL   Nat Genet 43 (3), 246-252 (2011)
   PUBMED   21297633
  REMARK    Erratum:[Nat Genet. 2011 Sep;43(9):919]
REFERENCE   9  (residues 1 to 589)
  AUTHORS   Kutsenko,A.S., Gizatullin,R.Z., Al-Amin,A.N., Wang,F., Kvasha,S.M.,
            Podowski,R.M., Matushkin,Y.G., Gyanchandani,A., Muravenko,O.V.,
            Levitsky,V.G., Kolchanov,N.A., Protopopov,A.I., Kashuba,V.I.,
            Kisselev,L.L., Wasserman,W., Wahlestedt,C. and Zabarovsky,E.R.
  TITLE     NotI flanking sequences: a tool for gene discovery and verification
            of the human genome
  JOURNAL   Nucleic Acids Res 30 (14), 3163-3170 (2002)
   PUBMED   12136098
REFERENCE   10 (residues 1 to 589)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL121845.20.
            
            On May 21, 2011 this sequence version replaced NP_079500.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131482.1, SRR14038197.1676647.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..589
                     /product="zinc finger and BTB domain-containing protein
                     46"
                     /note="zinc finger protein 340; BTB (POZ) domain
                     containing 4; BTB/POZ domain-containing protein 4; BTB-ZF
                     protein expressed in effector lymphocytes"
                     /calculated_mol_wt=63953
     Region          10..134
                     /region_name="BTB_POZ_ZBTB46"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 46 (ZBTB46); cd18230"
                     /db_xref="CDD:349539"
     Region          173..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UZ6.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UZ6.2)"
     Region          <361..>486
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          418..442
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          420..440
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(425,427,429..430,435..436,439,453,455,459..460,
                     463..464,467,481,483,485,487..488,492..493,497)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          433..457
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          448..468
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(448,451,464,468)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          476..498
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          512..589
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UZ6.2)"
     CDS             1..589
                     /gene="ZBTB46"
                     /gene_synonym="BTBD4; BZEL; dJ583P15.7; dJ583P15.8; RINZF;
                     ZNF340"
                     /coded_by="NM_025224.4:202..1971"
                     /db_xref="CCDS:CCDS13538.1"
                     /db_xref="GeneID:140685"
                     /db_xref="HGNC:HGNC:16094"
                     /db_xref="MIM:614639"
ORIGIN      
        1 mnnrkedmei tshyrhllre lneqrqhgvl cdvcvvvegk vfkahknvll gssryfktly
       61 cqvqktseqa tvthldivta qgfkaiidfm ysahlaltsr nvievmsaas flqmtdivqa
      121 chdfikaald isiksdasde laefeigass ssstealisa vmagrsispw larrtspans
      181 sgdsaiasch dggssygked qepkadgpdd vssqplwpgd vgygplrike eqvspsqygg
      241 selpsakdga vqnsfseqsa gdawqptgrr knrknketvr hitqqvedds rasspvpsfl
      301 ptsgwpfssr dsnadlsvte asssdsrger aelyaqveeg llggeasylg ppltpekdda
      361 lhqatavanl raalmsknsl lslkadvlgd dgsllfeylp rgahslslne ftvirkkfkc
      421 pycsfsamhq cilkrhmrsh tgerpypcei cgkkftrreh mkrhtlvhsk dkkyvckvcs
      481 rvfmsaasvg irhgsrrhgv ctdcagrgma gpldhggggg egspealfpg dgpyledped
      541 prgeaeelge ddeglapeda lladdkdeed sprprsppgg pdkdfawls
//
LOCUS       NP_001351931             667 aa            linear   PRI 27-APR-2025
DEFINITION  transcription initiation factor TFIID subunit 6 isoform delta [Homo
            sapiens].
ACCESSION   NP_001351931 XP_016868057
VERSION     NP_001351931.1
DBSOURCE    REFSEQ: accession NM_001365002.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Tuc,E., Bengur,F.B., Aykut,A., Sahin,O. and Alanay,Y.
  TITLE     The third family with TAF6-related phenotype: Alazami-Yuan syndrome
  JOURNAL   Clin Genet 97 (5), 795-796 (2020)
   PUBMED   32030742
  REMARK    GeneRIF: The third family with TAF6-related phenotype: Alazami-Yuan
            syndrome.
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Delannoy,A., Wilhelm,E., Eilebrecht,S., Alvarado-Cuevas,E.M.,
            Benecke,A.G. and Bell,B.
  TITLE     BIM and NOXA are mitochondrial effectors of TAF6delta-driven
            apoptosis
  JOURNAL   Cell Death Dis 9 (2), 70 (2018)
   PUBMED   29358700
  REMARK    GeneRIF: BIM and NOXA contribute to TAF6delta-dependent cell death.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Gupta,K., Watson,A.A., Baptista,T., Scheer,E., Chambers,A.L.,
            Koehler,C., Zou,J., Obong-Ebong,I., Kandiah,E., Temblador,A.,
            Round,A., Forest,E., Man,P., Bieniossek,C., Laue,E.D., Lemke,E.A.,
            Rappsilber,J., Robinson,C.V., Devys,D., Tora,L. and Berger,I.
  TITLE     Architecture of TAF11/TAF13/TBP complex suggests novel regulation
            properties of general transcription factor TFIID
  JOURNAL   Elife 6, e30395 (2017)
   PUBMED   29111974
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Bell,B., Scheer,E. and Tora,L.
  TITLE     Identification of hTAF(II)80 delta links apoptotic signaling
            pathways to transcription factor TFIID function
  JOURNAL   Mol Cell 8 (3), 591-600 (2001)
   PUBMED   11583621
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Hisatake,K., Ohta,T., Takada,R., Guermah,M., Horikoshi,M.,
            Nakatani,Y. and Roeder,R.G.
  TITLE     Evolutionary conservation of human
            TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and
            interactions of TAFII80 with other TAFs and with general
            transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 92 (18), 8195-8199 (1995)
   PUBMED   7667268
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Weinzierl,R.O., Ruppert,S., Dynlacht,B.D., Tanese,N. and Tjian,R.
  TITLE     Cloning and expression of Drosophila TAFII60 and human TAFII70
            reveal conserved interactions with other subunits of TFIID
  JOURNAL   EMBO J 12 (13), 5303-5309 (1993)
   PUBMED   8262073
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 667)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
REFERENCE   10 (residues 1 to 667)
  AUTHORS   Mathe,G., Schwarzenberg,L., Halle-Pannenko,O. and Simmler,M.C.
  TITLE     Discussion paper: experimental and clinical immunopharmacology data
            applicable to cancer immunotherapy
  JOURNAL   Ann N Y Acad Sci 277 (00), 467-484 (1976)
   PUBMED   826207
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073842.5.
            
            On Jul 20, 2018 this sequence version replaced XP_016868057.1.
            
            Summary: Initiation of transcription by RNA polymerase II requires
            the activities of more than 70 polypeptides. The protein that
            coordinates these activities is transcription factor IID (TFIID),
            which binds to the core promoter to position the polymerase
            properly, serves as the scaffold for assembly of the remainder of
            the transcription complex, and acts as a channel for regulatory
            signals. TFIID is composed of the TATA-binding protein (TBP) and a
            group of evolutionarily conserved proteins known as TBP-associated
            factors or TAFs. TAFs may participate in basal transcription, serve
            as coactivators, function in promoter recognition or modify general
            transcription factors (GTFs) to facilitate complex assembly and
            transcription initiation. This gene encodes one of the smaller
            subunits of TFIID that binds weakly to TBP but strongly to TAF1,
            the largest subunit of TFIID. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jun 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.69717.1,
                                           SRR1660803.23167.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..667
                     /product="transcription initiation factor TFIID subunit 6
                     isoform delta"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, E, 70/85kD; transcription initiation
                     factor TFIID subunit 6; RNA polymerase II TBP-associated
                     factor subunit E; transcription initiation factor TFIID 70
                     kDa subunit; TAF6 RNA polymerase II, TATA box binding
                     protein (TBP)-associated factor, 80kDa"
                     /calculated_mol_wt=71349
     Region          12..67
                     /region_name="HFD_TAF6"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 6 (TAF6) and similar
                     proteins; cd22931"
                     /db_xref="CDD:467055"
     Site            order(38,42,46..47,49..54,62..63,66)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467055"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          132..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Region          204..420
                     /region_name="TAF6C"
                     /note="C-terminal domain of TATA Binding Protein (TBP)
                     Associated Factor 6 (TAF6); cd08050"
                     /db_xref="CDD:381749"
     Site            order(208..210,212..213,216,227..228,231,235,238..239,245)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:381749"
     Region          208..239
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          246..281
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          291..334
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          341..373
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          375..419
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          514..564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Site            514
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          601..667
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62311; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     CDS             1..667
                     /gene="TAF6"
                     /gene_synonym="ALYUS; MGC:8964; TAF(II)70; TAF(II)80;
                     TAF2E; TAFII-70; TAFII-80; TAFII70; TAFII80; TAFII85"
                     /coded_by="NM_001365002.1:539..2542"
                     /note="isoform delta is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS94153.1"
                     /db_xref="GeneID:6878"
                     /db_xref="HGNC:HGNC:11540"
                     /db_xref="MIM:602955"
ORIGIN      
        1 maeekklkls ntvlpsesmk vvaesmgiaq iqeetcqllt dedalkfmhm gkrqklttsd
       61 idyalklknv eplygfhaqe fipfrfasgg grelyfyeek evdlsdiint plprvpldvc
      121 lkahwlsieg cqpaipenpp papkeqqkae ateplksakp gqeedgplkg kgqgattadg
      181 kgkekkappl legaplrlkp rsihelsveq qlyykeitea cvgsceakra ealqsiatdp
      241 glyqmlprfs tfisegvrvn vvqnnlalli ylmrmvkalm dnptlyleky vhelipavmt
      301 civsrqlclr pdvdnhwalr dfaarlvaqi ckhfstttnn iqsritktft kswvdektpw
      361 ttrygsiagl aelghdvikt lilprlqqeg erirsvldgp vlsnidriga dhvqslllkh
      421 capvlaklrp ppdnqdayra efgslgpllc sqvvkaraqa alqaqqvnrt tltitqprpt
      481 ltlsqapqpg prtpgllkvp gsialpvqtl vsaraaappq psppptkfiv msssssapst
      541 qqvlslstsa pgsgstttsp vtttvpsvqp ivklvstatt appstapsgp gsvqkyivvs
      601 lpptgegkgg ptshpspvpp passpsplsg salcggkqea gdspppapgt pkangsqpns
      661 gspqpap
//
LOCUS       NP_001171172             186 aa            linear   PRI 27-APR-2025
DEFINITION  intraflagellar transport protein 27 homolog isoform 1 [Homo
            sapiens].
ACCESSION   NP_001171172
VERSION     NP_001171172.1
DBSOURCE    REFSEQ: accession NM_001177701.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Zhou,Z., Qiu,H., Castro-Araya,R.F., Takei,R., Nakayama,K. and
            Katoh,Y.
  TITLE     Impaired cooperation between IFT74/BBS22-IFT81 and
            IFT25-IFT27/BBS19 causes Bardet-Biedl syndrome
  JOURNAL   Hum Mol Genet 31 (10), 1681-1693 (2022)
   PUBMED   34888642
  REMARK    GeneRIF: Impaired cooperation between IFT74/BBS22-IFT81 and
            IFT25-IFT27/BBS19 causes Bardet-Biedl syndrome.
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Liew,G.M., Ye,F., Nager,A.R., Murphy,J.P., Lee,J.S., Aguiar,M.,
            Breslow,D.K., Gygi,S.P. and Nachury,M.V.
  TITLE     The intraflagellar transport protein IFT27 promotes BBSome exit
            from cilia through the GTPase ARL6/BBS3
  JOURNAL   Dev Cell 31 (3), 265-278 (2014)
   PUBMED   25443296
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Aldahmesh,M.A., Li,Y., Alhashem,A., Anazi,S., Alkuraya,H.,
            Hashem,M., Awaji,A.A., Sogaty,S., Alkharashi,A., Alzahrani,S., Al
            Hazzaa,S.A., Xiong,Y., Kong,S., Sun,Z. and Alkuraya,F.S.
  TITLE     IFT27, encoding a small GTPase component of IFT particles, is
            mutated in a consanguineous family with Bardet-Biedl syndrome
  JOURNAL   Hum Mol Genet 23 (12), 3307-3315 (2014)
   PUBMED   24488770
  REMARK    GeneRIF: Study coupled human genetics with functional validation in
            zebrafish and identified IFT27 as a novel BBS gene (BBS19).
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Diekmann,Y., Seixas,E., Gouw,M., Tavares-Cadete,F., Seabra,M.C. and
            Pereira-Leal,J.B.
  TITLE     Thousands of rab GTPases for the cell biologist
  JOURNAL   PLoS Comput Biol 7 (10), e1002217 (2011)
   PUBMED   22022256
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Qin,H., Wang,Z., Diener,D. and Rosenbaum,J.
  TITLE     Intraflagellar transport protein 27 is a small G protein involved
            in cell-cycle control
  JOURNAL   Curr Biol 17 (3), 193-202 (2007)
   PUBMED   17276912
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB457924.1 and BC000566.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a GTP-binding protein that is a core
            component of the intraflagellar transport complex B.
            Characterization of the similar Chlamydomonas protein indicates a
            function in cell cycle control. Alternative splicing of this gene
            results in multiple transcript variants. [provided by RefSeq, Jan
            2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Both variants 1 and
            5 encode isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000566.2, SRR1163655.290013.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000433985.7/ ENSP00000393541.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..186
                     /product="intraflagellar transport protein 27 homolog
                     isoform 1"
                     /EC_number="3.6.5.2"
                     /note="RAB, member of RAS oncogene family-like 4;
                     intraflagellar transport protein 27 homolog; rab-like
                     protein 4"
                     /calculated_mol_wt=20349
     Region          6..172
                     /region_name="RabL4"
                     /note="Rab GTPase-like family 4 (Rab-like4); cd04101"
                     /db_xref="CDD:206688"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206688"
     Site            order(14..20,30,38..39,67,123..124,126,153..155)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206688"
     Site            order(30,37..46)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206688"
     Site            39
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206688"
     Site            order(40,42..44,61,63,70..71,74,78,80..83)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206688"
     Site            order(40,43,63..64)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206688"
     Site            order(43..48,59)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206688"
     Site            64..67
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206688"
     Site            order(67,70..72,74..82)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206688"
     Site            123..126
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206688"
     Site            153..155
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206688"
     CDS             1..186
                     /gene="IFT27"
                     /gene_synonym="BBS19; CFAP156; FAP156; RABL4; RAYL"
                     /coded_by="NM_001177701.3:413..973"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54523.1"
                     /db_xref="GeneID:11020"
                     /db_xref="HGNC:HGNC:18626"
                     /db_xref="MIM:615870"
ORIGIN      
        1 mvklaakcil agdpavgkta laqifrsdga hfqksytltt gmdlvvktvp vpdtgdsvel
       61 fifdsagkel fsemldklwe spnvlclvyd vtneesfnnc skwlekarsq apgislpgvl
      121 vgnktdlagr ravdsaeara walgqglecf etsvkemenf eapfhclakq fhqlyrekve
      181 vfrala
//
LOCUS       NP_006460                642 aa            linear   PRI 27-APR-2025
DEFINITION  influenza virus NS1A-binding protein [Homo sapiens].
ACCESSION   NP_006460
VERSION     NP_006460.2
DBSOURCE    REFSEQ: accession NM_006469.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Waldran,M.J., Wegman,A.D., Bahr,L.E., Roy,N.H., Currier,J.R. and
            Waickman,A.T.
  TITLE     Soluble NS1 Antagonizes IgG- and IgA- Mediated Monocytic
            Phagocytosis of DENV Infected Cells
  JOURNAL   J Infect Dis 228 (1), 70-79 (2023)
   PUBMED   37103221
  REMARK    GeneRIF: Soluble NS1 Antagonizes IgG- and IgA- Mediated Monocytic
            Phagocytosis of DENV Infected Cells.
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Zhang,K., Shang,G., Padavannil,A., Wang,J., Sakthivel,R., Chen,X.,
            Kim,M., Thompson,M.G., Garcia-Sastre,A., Lynch,K.W., Chen,Z.J.,
            Chook,Y.M. and Fontoura,B.M.A.
  TITLE     Structural-functional interactions of NS1-BP protein with the
            splicing and mRNA export machineries for viral and host gene
            expression
  JOURNAL   Proc Natl Acad Sci U S A 115 (52), E12218-E12227 (2018)
   PUBMED   30538201
  REMARK    GeneRIF: The central BACK domain of NS1-BP interacts directly with
            splicing factors such as hnRNP K and PTBP1 and with the viral NS1
            protein.
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Thompson,M.G., Munoz-Moreno,R., Bhat,P., Roytenberg,R.,
            Lindberg,J., Gazzara,M.R., Mallory,M.J., Zhang,K.,
            Garcia-Sastre,A., Fontoura,B.M.A. and Lynch,K.W.
  TITLE     Co-regulatory activity of hnRNP K and NS1-BP in influenza and human
            mRNA splicing
  JOURNAL   Nat Commun 9 (1), 2407 (2018)
   PUBMED   29921878
  REMARK    GeneRIF: Data show that heterogeneous nuclear ribonucleoprotein K
            (hnRNP K) and influenza virus NS1A binding protein (NS1-BP)
            regulate host splicing events and that viral infection causes
            mis-splicing of some of these transcripts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Wang,Y., Cheng,J., Xie,D., Ding,X., Hou,H., Chen,X., Er,P.,
            Zhang,F., Zhao,L., Yuan,Z., Pang,Q., Wang,P. and Qian,D.
  TITLE     NS1-binding protein radiosensitizes esophageal squamous cell
            carcinoma by transcriptionally suppressing c-Myc
  JOURNAL   Cancer Commun (Lond) 38 (1), 33 (2018)
   PUBMED   29871674
  REMARK    GeneRIF: In esophageal squamous cell carcinoma (ESCC) tissues,
            c-Myc expression was inversely correlated with NS1-binding protein
            (NS1-BP) levels, and was associated with a shorter disease-specific
            survival (DSS).
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Guo,L. and Liu,Y.
  TITLE     Crystal structure of the Kelch domain of human NS1-binding protein
            at 1.98 A resolution
  JOURNAL   Acta Crystallogr F Struct Biol Commun 74 (Pt 3), 174-178 (2018)
   PUBMED   29497022
  REMARK    GeneRIF: Comparison of the Kelch-domain structures of NS1-BP and
            its homologues showed that the Gly-Gly pair in beta-strand B and
            the hydrophobic Trp residue in beta-strand D are highly conserved,
            while the B-C loops in blades 2 and 6 are variable
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Naukkarinen,J., Surakka,I., Pietilainen,K.H., Rissanen,A.,
            Salomaa,V., Ripatti,S., Yki-Jarvinen,H., van Duijn,C.M.,
            Wichmann,H.E., Kaprio,J., Taskinen,M.R. and Peltonen,L.
  CONSRTM   ENGAGE Consortium
  TITLE     Use of genome-wide expression data to mine the 'Gray Zone' of GWA
            studies leads to novel candidate obesity genes
  JOURNAL   PLoS Genet 6 (6), e1000976 (2010)
   PUBMED   20532202
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 642)
  AUTHORS   Perconti,G., Ferro,A., Amato,F., Rubino,P., Randazzo,D., Wolff,T.,
            Feo,S. and Giallongo,A.
  TITLE     The kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is
            involved in c-Myc gene transcriptional control
  JOURNAL   Biochim Biophys Acta 1773 (12), 1774-1785 (2007)
   PUBMED   17996313
  REMARK    GeneRIF: These findings further support the distinct roles of
            alpha-enolase and its MBP-1 variant in maintaining cell
            homeostasis. Moreover, these data suggest a novel function for
            NS1-BP in the control of cell proliferation.
REFERENCE   8  (residues 1 to 642)
  AUTHORS   Dunham,E.E., Stevens,E.A., Glover,E. and Bradfield,C.A.
  TITLE     The aryl hydrocarbon receptor signaling pathway is modified through
            interactions with a Kelch protein
  JOURNAL   Mol Pharmacol 70 (1), 8-15 (2006)
   PUBMED   16582008
REFERENCE   9  (residues 1 to 642)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
REFERENCE   10 (residues 1 to 642)
  AUTHORS   Wolff,T., O'Neill,R.E. and Palese,P.
  TITLE     NS1-Binding protein (NS1-BP): a novel human protein that interacts
            with the influenza A virus nonstructural NS1 protein is relocalized
            in the nuclei of infected cells
  JOURNAL   J Virol 72 (9), 7170-7180 (1998)
   PUBMED   9696811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB020657.1, AK000931.1, AL137640.1 and AF205218.1.
            
            On Nov 2, 2002 this sequence version replaced NP_006460.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ012449.1, AF205218.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367498.8/ ENSP00000356468.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.3"
     Protein         1..642
                     /product="influenza virus NS1A-binding protein"
                     /note="NS1-binding protein; NCX downstream gene 1; aryl
                     hydrocarbon receptor-associated 3; aryl hydrocarbon
                     receptor-associated protein 3; kelch-like family member
                     39; kelch-like protein 39"
                     /calculated_mol_wt=71599
     Region          14..137
                     /region_name="BTB_POZ_NS1BP"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Influenza virus
                     NS1A-binding protein (NS1-BP); cd18306"
                     /db_xref="CDD:349615"
     Region          129..225
                     /region_name="BACK_NS1BP_IVNS1ABP"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     influenza virus NS1A-binding protein (NS1-BP); cd18502"
                     /db_xref="CDD:350577"
     Region          164..368
                     /region_name="Sufficient for AHR interaction and
                     signaling"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Region          257..281
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Region          349..627
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          358..401
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          384..421
                     /region_name="Kelch 1.
                     /evidence=ECO:0000303|PubMed:30538201,
                     ECO:0007744|PDB:6N3H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Region          409..451
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          432..469
                     /region_name="Kelch 2.
                     /evidence=ECO:0000303|PubMed:30538201,
                     ECO:0007744|PDB:6N3H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Region          453..498
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          481..518
                     /region_name="Kelch 3.
                     /evidence=ECO:0000303|PubMed:30538201,
                     ECO:0007744|PDB:6N3H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Region          502..545
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          527..565
                     /region_name="Kelch 4.
                     /evidence=ECO:0000303|PubMed:30538201,
                     ECO:0007744|PDB:6N3H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Region          549..593
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          575..612
                     /region_name="Kelch 5.
                     /evidence=ECO:0000303|PubMed:30538201,
                     ECO:0007744|PDB:6N3H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     Region          596..635
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          622..642
                     /region_name="Kelch 6.
                     /evidence=ECO:0000303|PubMed:30538201,
                     ECO:0007744|PDB:6N3H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6Y0.3)"
     CDS             1..642
                     /gene="IVNS1ABP"
                     /gene_synonym="ARA3; FLARA3; HSPC068; IMD70; KLHL39; ND1;
                     NS-1; NS1-BP; NS1BP"
                     /coded_by="NM_006469.5:538..2466"
                     /db_xref="CCDS:CCDS1368.1"
                     /db_xref="GeneID:10625"
                     /db_xref="HGNC:HGNC:16951"
                     /db_xref="MIM:609209"
ORIGIN      
        1 mipngylmfe denfiessva klnalrksgq fcdvrlqvcg hemlahravl accspylfei
       61 fnsdsdphgi shvkfddlnp eavevllnya ytaqlkadke lvkdvysaak klkmdrvkqv
      121 cgdyllsrmd vtscisyrnf ascmgdsrll nkvdayiqeh llqiseeeef lklprlklev
      181 mlednvclps ngklytkvin wvqrsiweng dsleelmeev qtlyysadhk lldgnlldgq
      241 aevfgsdddh iqfvqkkppr enghkqisss stgclsspna tvqspkhewk ivasektsnn
      301 tylclavldg ifcviflhgr nspqssptst pklskslsfe mqqdeliekp mspmqyarsg
      361 lgtaemngkl iaaggynree clrtvecynp htdhwsflap mrtprarfqm avlmgqlyvv
      421 ggsnghsddl scgemydsni ddwipvpelr tnrcnagvca lngklyivgg sdpygqkglk
      481 ncdvfdpvtk lwtscaplni rrhqsavcel ggylyiigga eswnclntve rynpenntwt
      541 liapmnvarr gagvavlngk lfvcggfdgs haiscvemyd ptrnewkmmg nmtsprsnag
      601 iatvgntiya vggfdgnefl ntvevynles newspytkif qf
//
LOCUS       NP_001352634             313 aa            linear   PRI 27-APR-2025
DEFINITION  NF-kappa-B inhibitor delta isoform 4 [Homo sapiens].
ACCESSION   NP_001352634 XP_024307511
VERSION     NP_001352634.1
DBSOURCE    REFSEQ: accession NM_001365705.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Presa,M., Racine,J.J., Dwyer,J.R., Lamont,D.J., Ratiu,J.J.,
            Sarsani,V.K., Chen,Y.G., Geurts,A., Schmitz,I., Stearns,T.,
            Allocco,J., Chapman,H.D. and Serreze,D.V.
  TITLE     A Hypermorphic Nfkbid Allele Contributes to Impaired Thymic
            Deletion of Autoreactive Diabetogenic CD8+ T Cells in NOD Mice
  JOURNAL   J Immunol 201 (7), 1907-1917 (2018)
   PUBMED   30127089
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Tao,Z., Fusco,A., Huang,D.B., Gupta,K., Young Kim,D., Ware,C.F.,
            Van Duyne,G.D. and Ghosh,G.
  TITLE     p100/IkappaBdelta sequesters and inhibits NF-kappaB through
            kappaBsome formation
  JOURNAL   Proc Natl Acad Sci U S A 111 (45), 15946-15951 (2014)
   PUBMED   25349408
  REMARK    GeneRIF: The unique ability of p100/IkappaBdelta to stably interact
            with all NF-kappaB subunits by forming kappaBsomes demonstrates its
            importance in sequestering NF-kappaB subunits and releasing them as
            dictated by specific stimuli for developmental programs.
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Ivanov,I.P., Firth,A.E., Michel,A.M., Atkins,J.F. and Baranov,P.V.
  TITLE     Identification of evolutionarily conserved non-AUG-initiated
            N-terminal extensions in human coding sequences
  JOURNAL   Nucleic Acids Res 39 (10), 4220-4234 (2011)
   PUBMED   21266472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AD000864.1.
            
            On Sep 13, 2018 this sequence version replaced XP_024307511.1.
            
            Transcript Variant: This variant (4) encodes the longest isoform
            (4), formerly known as isoform 1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803615.98045.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..313
                     /product="NF-kappa-B inhibitor delta isoform 4"
                     /note="NF-kappa-B inhibitor delta; T-cell activation
                     NFKB-like protein; ikB-delta; ikappaBdelta;
                     I-kappa-B-delta; nuclear factor of kappa light polypeptide
                     gene enhancer in B-cells inhibitor, delta"
                     /calculated_mol_wt=33350
     Region          32..303
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(48,50,54..55,58..60,66..67,71,75,82,84,86,90..91,
                     94..96,98..99,103,106,115,117,119,123..124,127..129,
                     131..132,136,139,150)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          48..83
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI38.1)"
     Region          48..82
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          84..115
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          84..113
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI38.1)"
     Region          117..150
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          117..146
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI38.1)"
     Site            order(152,154,158..159,182..184,186..187,191,194,203,206,
                     208,212..213,216..218,220..221,225,228,242,243,245,
                     249..250,253..254,259,261..262,266,269,278)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          152..203
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          152..201
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI38.1)"
     Region          206..242
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          206..236
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI38.1)"
     Region          243..278
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          243..276
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI38.1)"
     CDS             1..313
                     /gene="NFKBID"
                     /gene_synonym="IkappaBNS; IkBNS; TA-NFKBH"
                     /coded_by="NM_001365705.1:385..1326"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS42552.1"
                     /db_xref="GeneID:84807"
                     /db_xref="HGNC:HGNC:15671"
                     /db_xref="MIM:618887"
ORIGIN      
        1 meagpwrvsa ppsgppqfpa vvpgpsleva rahmlalgpq qllaqdeegd tllhlfaarg
       61 lrwaayaaae vlqvyrrldi rehkgktpll vaaaanqpli vedllnlgae pnaadhqgrs
      121 vlhvaatygl pgvllavlns gvqvdleard fegltplhta ilalnvamrp sdlcprvlst
      181 qardrldcvh mllqmganht sqeiksnktv lhlavqaanp tlvqlllelp rgdlrtfvnm
      241 kahgntalhm aaalppgpaq eaivrhllaa gadptlrnle neqpvhllrp gpgpeglrql
      301 lkrsrvappg lss
//
LOCUS       NP_001356044             897 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 618 isoform e [Mus musculus].
ACCESSION   NP_001356044
VERSION     NP_001356044.1
DBSOURCE    REFSEQ: accession NM_001369115.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 897)
  AUTHORS   Lee,D.J., Kim,H.Y., Lee,S.J. and Jung,H.S.
  TITLE     Spatiotemporal Changes in Transcriptome of Odontogenic and
            Non-odontogenic Regions in the Dental Arch of Mus musculus
  JOURNAL   Front Cell Dev Biol 9, 723326 (2021)
   PUBMED   34722506
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 897)
  AUTHORS   Quina,L.A., Wang,S., Ng,L. and Turner,E.E.
  TITLE     Brn3a and Nurr1 mediate a gene regulatory pathway for habenula
            development
  JOURNAL   J Neurosci 29 (45), 14309-14322 (2009)
   PUBMED   19906978
REFERENCE   3  (residues 1 to 897)
  AUTHORS   Georgas,K., Rumballe,B., Valerius,M.T., Chiu,H.S.,
            Thiagarajan,R.D., Lesieur,E., Aronow,B.J., Brunskill,E.W.,
            Combes,A.N., Tang,D., Taylor,D., Grimmond,S.M., Potter,S.S.,
            McMahon,A.P. and Little,M.H.
  TITLE     Analysis of early nephron patterning reveals a role for distal RV
            proliferation in fusion to the ureteric tip via a cap
            mesenchyme-derived connecting segment
  JOURNAL   Dev Biol 332 (2), 273-286 (2009)
   PUBMED   19501082
REFERENCE   4  (residues 1 to 897)
  AUTHORS   Long,J.E., Cobos,I., Potter,G.B. and Rubenstein,J.L.
  TITLE     Dlx1&2 and Mash1 transcription factors control MGE and CGE
            patterning and differentiation through parallel and overlapping
            pathways
  JOURNAL   Cereb Cortex 19 Suppl 1 (Suppl 1), i96-i106 (2009)
   PUBMED   19386638
REFERENCE   5  (residues 1 to 897)
  AUTHORS   Kumar,S., Tomooka,Y. and Noda,M.
  TITLE     Identification of a set of genes with developmentally
            down-regulated expression in the mouse brain
  JOURNAL   Biochem Biophys Res Commun 185 (3), 1155-1161 (1992)
   PUBMED   1378265
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL691431.20 and AL691496.13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660811.132710.1,
                                           SRR1660815.126183.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..897
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 33.82 cM"
     Protein         1..897
                     /product="zinc finger protein 618 isoform e"
                     /note="neural precursor cell expressed, developmentally
                     down-regulated gene 10"
                     /calculated_mol_wt=99036
     Region          92..112
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          133..153
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..897
                     /gene="Zfp618"
                     /gene_synonym="2810031P15Rik; 2810040O04Rik; bM257P7.1;
                     D430033D05Rik; Nedd10; Znf618"
                     /coded_by="NM_001369115.1:1105..3798"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:72701"
                     /db_xref="MGI:MGI:1919950"
ORIGIN      
        1 mtevkvktev pddyiqeviw qgeakeekag gkdstgdvpa eicvviggvr nqqtldgkap
       61 egsphggsvr srysgtwifd qalkyasgsy ecgicgkkyk yyncfqthvr ahrdteatsg
      121 egvsqsnnfr ytcdicgkky kyyscfqehr dlhavdvfsv egapenradp fdqgvvatde
      181 vkeeppepfq kigpktgnyt cefcgkqyky ytpyqehval hapistapgw eppedpdtgs
      241 ecshpevtps prfvaaktqs nqsgkkapas vvrctsllhr tppatqtqtf rapnsgspas
      301 kaaaaentfs rrveskaqnh feetnsssqn ssepytcgac giqfqfysnl lehmqshaad
      361 nennitsnqs rsppaaveek wkpqaqrnsa nntttsgltp nsvipekerq niaerllrvm
      421 cadlgalsvv sgkeflklaq tlvdsgaryg afsvteilgn fntlalkhlp rmynqvkvkv
      481 tcalgsnacl gigvtchsqs vgpdscyilt ayqaegnhik syvlgvkgad irdsgdlvhh
      541 wvqnvlsefv mseirtvyvt dcrvstsafs kagmclrcsa calnsvvqsv lskrtlqars
      601 mheviellnv cedlagstgl aketfgslee tspppcwnsv tdslllvher yeqicefysr
      661 akkmnliqsl nkhllsnlaa iltpvkqavi elsnesqptl qlvlptyvrl eklftakand
      721 agtvsklchl flealkenfk vhpahkvami ldpqqklrpv ppyqheeiis kvcelinevk
      781 eswaeeadfe paakkarsat gehpaaqeed rlgknevydy lqeplfqatp dlfqywscvt
      841 qkhtklakla fwllavpavg arsgcvnmce qallikrrrl lspedmnklm flksnml
//
LOCUS       NP_003668                198 aa            linear   PRI 27-APR-2025
DEFINITION  density-regulated protein [Homo sapiens].
ACCESSION   NP_003668
VERSION     NP_003668.2
DBSOURCE    REFSEQ: accession NM_003677.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Grove,D.J., Russell,P.J. and Kearse,M.G.
  TITLE     To initiate or not to initiate: A critical assessment of eIF2A,
            eIF2D, and MCT-1.DENR to deliver initiator tRNA to ribosomes
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1833 (2024)
   PUBMED   38433101
  REMARK    GeneRIF: To initiate or not to initiate: A critical assessment of
            eIF2A, eIF2D, and MCT-1.DENR to deliver initiator tRNA to
            ribosomes.
            Review article
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Clemm von Hohenberg,K., Muller,S., Schleich,S., Meister,M.,
            Bohlen,J., Hofmann,T.G. and Teleman,A.A.
  TITLE     Cyclin B/CDK1 and Cyclin A/CDK2 phosphorylate DENR to promote
            mitotic protein translation and faithful cell division
  JOURNAL   Nat Commun 13 (1), 668 (2022)
   PUBMED   35115540
  REMARK    GeneRIF: Cyclin B/CDK1 and Cyclin A/CDK2 phosphorylate DENR to
            promote mitotic protein translation and faithful cell division.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Petrozziello,T., Bordt,E.A., Mills,A.N., Kim,S.E., Sapp,E.,
            Devlin,B.A., Obeng-Marnu,A.A., Farhan,S.M.K., Amaral,A.C.,
            Dujardin,S., Dooley,P.M., Henstridge,C., Oakley,D.H., Neueder,A.,
            Hyman,B.T., Spires-Jones,T.L., Bilbo,S.D., Vakili,K.,
            Cudkowicz,M.E., Berry,J.D., DiFiglia,M., Silva,M.C., Haggarty,S.J.
            and Sadri-Vakili,G.
  TITLE     Targeting Tau Mitigates Mitochondrial Fragmentation and Oxidative
            Stress in Amyotrophic Lateral Sclerosis
  JOURNAL   Mol Neurobiol 59 (1), 683-702 (2022)
   PUBMED   34757590
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Bohlen,J., Harbrecht,L., Blanco,S., Clemm von Hohenberg,K.,
            Fenzl,K., Kramer,G., Bukau,B. and Teleman,A.A.
  TITLE     DENR promotes translation reinitiation via ribosome recycling to
            drive expression of oncogenes including ATF4
  JOURNAL   Nat Commun 11 (1), 4676 (2020)
   PUBMED   32938922
  REMARK    GeneRIF: DENR promotes translation reinitiation via ribosome
            recycling to drive expression of oncogenes including ATF4.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Nakamura,N., Kimura,Y., Tokuda,M., Honda,S. and Hirose,S.
  TITLE     MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to
            change mitochondrial morphology
  JOURNAL   EMBO Rep 7 (10), 1019-1022 (2006)
   PUBMED   16936636
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Yonashiro,R., Ishido,S., Kyo,S., Fukuda,T., Goto,E., Matsuki,Y.,
            Ohmura-Hoshino,M., Sada,K., Hotta,H., Yamamura,H., Inatome,R. and
            Yanagi,S.
  TITLE     A novel mitochondrial ubiquitin ligase plays a critical role in
            mitochondrial dynamics
  JOURNAL   EMBO J 25 (15), 3618-3626 (2006)
   PUBMED   16874301
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Oh,J.J., Grosshans,D.R., Wong,S.G. and Slamon,D.J.
  TITLE     Identification of differentially expressed genes associated with
            HER-2/neu overexpression in human breast cancer cells
  JOURNAL   Nucleic Acids Res 27 (20), 4008-4017 (1999)
   PUBMED   10497265
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Deyo,J.E., Chiao,P.J. and Tainsky,M.A.
  TITLE     drp, a novel protein expressed at high cell density but not during
            growth arrest
  JOURNAL   DNA Cell Biol 17 (5), 437-447 (1998)
   PUBMED   9628587
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP872988.1, AB014731.1,
            CB043904.1, AF103800.1, CN300034.1 and AI093455.1.
            
            On Jan 5, 2003 this sequence version replaced NP_003668.1.
            
            Summary: This gene encodes a protein whose expression was found to
            increase in cultured cells at high density but not during growth
            arrest. This gene was also shown to have increased expression in
            cells overexpressing HER-2/neu proto-oncogene. The protein contains
            an SUI1 domain. In budding yeast, SUI1 is a translation initiation
            factor that along with eIF-2 and the initiator tRNA-Met, directs
            the ribosome to the proper translation start site. Proteins similar
            to SUI have been found in mammals, insects, and plants. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.261324.1,
                                           SRR1660807.117039.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280557.11/ ENSP00000280557.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..198
                     /product="density-regulated protein"
                     /note="smooth muscle cell associated protein-3"
                     /calculated_mol_wt=21961
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (O43583.2)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43583.2)"
     Region          28..193
                     /region_name="DRP1"
                     /note="density-regulated protein DRP1; TIGR01159"
                     /db_xref="CDD:273472"
     Region          72..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43583.2)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43583.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43583.2)"
     Site            order(122,125..126,128,146,149..151,153..155,157,167,170)
                     /site_type="other"
                     /note="putative rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:211320"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQJ6; propagated from
                     UniProtKB/Swiss-Prot (O43583.2)"
     CDS             1..198
                     /gene="DENR"
                     /gene_synonym="DRP; DRP1; SMAP-3"
                     /coded_by="NM_003677.5:137..733"
                     /db_xref="CCDS:CCDS45003.1"
                     /db_xref="GeneID:8562"
                     /db_xref="HGNC:HGNC:2769"
                     /db_xref="MIM:604550"
ORIGIN      
        1 maadisessg adckgdprns akldadyplr vlycgvcslp teyceympdv akcrqwlekn
       61 fpnefakltv enspkqeagi segqgtagee eekkkqkrgg rgqikqkkkt vpqkvtiaki
      121 prakkkyvtr vcglatfeid lkeaqrffaq kfscgasvtg edeiiiqgdf tddiidviqe
      181 kwpevdddsi edlgevkk
//
LOCUS       NP_001356417             394 aa            linear   PRI 27-APR-2025
DEFINITION  hexosaminidase D isoform 4 [Homo sapiens].
ACCESSION   NP_001356417 XP_016879974
VERSION     NP_001356417.1
DBSOURCE    REFSEQ: accession NM_001369488.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Alteen,M.G., Oehler,V., Nemcovicova,I., Wilson,I.B., Vocadlo,D.J.
            and Gloster,T.M.
  TITLE     Mechanism of Human Nucleocytoplasmic Hexosaminidase D
  JOURNAL   Biochemistry 55 (19), 2735-2747 (2016)
   PUBMED   27149221
  REMARK    GeneRIF: The catalytically important residues are Asp148 and
            Glu149, with Glu149 serving as the general acid/base residue and
            Asp148 as the polarizing residue. HexD is inhibited by
            Gal-NAG-thiazoline (Ki = 420 nM).
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Pasztoi,M., Sodar,B., Misjak,P., Paloczi,K., Kittel,A., Toth,K.,
            Wellinger,K., Geher,P., Nagy,G., Lakatos,T., Falus,A. and
            Buzas,E.I.
  TITLE     The recently identified hexosaminidase D enzyme substantially
            contributes to the elevated hexosaminidase activity in rheumatoid
            arthritis
  JOURNAL   Immunol Lett 149 (1-2), 71-76 (2013)
   PUBMED   23099419
  REMARK    GeneRIF: the expression and disease relevance of the HEXDC gene in
            humans demonstrate the expression of this novel enzyme within the
            joints, and suggests that its activity may significantly contribute
            to the overall local exoglycosidase activity.
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Barrera-Chimal,J. and Bobadilla,N.A.
  TITLE     Are recently reported biomarkers helpful for early and accurate
            diagnosis of acute kidney injury?
  JOURNAL   Biomarkers 17 (5), 385-393 (2012)
   PUBMED   22515481
  REMARK    GeneRIF: Studies indicate the most studied biomarkers for acute
            kidney injury are neutrophil gelatinase-associated lipocalin-2,
            kidney injury molecule-1, IL-18, cystatin C,
            N-acetyl-beta-D-glucosaminidase, liver fatty-acid binding protein,
            and heat shock protein 72.
            Review article
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Lisowska-Myjak,B., Krych,A., Kolodziejczyk,A., Pachecka,J. and
            Gaciong,Z.
  TITLE     Urinary proteins, N-acetyl-beta-D-glucosaminidase activity and
            estimated glomerular filtration rate in hypertensive patients with
            normoalbuminuria and microalbuminuria
  JOURNAL   Nephrology (Carlton) 16 (4), 403-409 (2011)
   PUBMED   21265931
  REMARK    GeneRIF: In normoalbuminuric/microalbuminuric patients with
            essential hypertension renal impairment measured by e-GFR is
            related to the increased urinary NAG activity and
            albumin/creatinine ratio rather than elevated concentrations of
            individual proteins.
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Ren,L., Ji,J., Fang,Y., Jiang,S.H., Lin,Y.M., Bo,J., Qian,J.Y.,
            Xu,X.H. and Ding,X.Q.
  TITLE     Assessment of urinary N-acetyl-beta-glucosaminidase as an early
            marker of contrast-induced nephropathy
  JOURNAL   J Int Med Res 39 (2), 647-653 (2011)
   PUBMED   21672370
  REMARK    GeneRIF: The results suggest that, following coronary angiography
            and/or percutaneous coronary intervention, contrast-induced
            nephropathy (CIN) occurs to a certain degree and that NAG may be a
            useful early CIN marker.
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Gutternigg,M., Rendic,D., Voglauer,R., Iskratsch,T. and Wilson,I.B.
  TITLE     Mammalian cells contain a second nucleocytoplasmic hexosaminidase
  JOURNAL   Biochem J 419 (1), 83-90 (2009)
   PUBMED   19040401
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132938.9.
            
            On Apr 10, 2019 this sequence version replaced XP_016879974.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.849871.1,
                                           SRR3476690.1051700.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..394
                     /product="hexosaminidase D isoform 4"
                     /EC_number="3.2.1.52"
                     /note="beta-hexosaminidase D; beta-N-acetylhexosaminidase;
                     N-acetyl-beta-galactosaminidase; hexosaminidase
                     domain-containing protein; hexosaminidase (glycosyl
                     hydrolase family 20, catalytic domain) containing;
                     hexosaminidase D, cytosolic"
                     /calculated_mol_wt=43317
     Region          <1..231
                     /region_name="GH20_hexosaminidase"
                     /note="Beta-N-acetylhexosaminidases of glycosyl hydrolase
                     family 20 (GH20) catalyze the removal of beta-1,4-linked
                     N-acetyl-D-hexosamine residues from the non-reducing ends
                     of N-acetyl-beta-D-hexosaminides including
                     N-acetylglucosides and N-acetylgalactosides; cl02948"
                     /db_xref="CDD:445966"
     CDS             1..394
                     /gene="HEXD"
                     /gene_synonym="HEXDC"
                     /coded_by="NM_001369488.1:612..1796"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:284004"
                     /db_xref="HGNC:HGNC:26307"
                     /db_xref="MIM:616864"
ORIGIN      
        1 mefvlkhtaf ahlrevgsfp ctlnpheaes lalvgamidq vlelhpgaqr lhigcdevyy
       61 lgegeasrrw lqqeqnstgk lclshmrava sgvkarrpsv tplvwddmlr dlpedqlaas
      121 gvpqlvepvl wdytadldvh gkvllmqkyr rcgfpqlwaa safkgatgps qavppvehhl
      181 rnhvqwlqva gsgptdslqg iiltgwqryd hysvlcellp agvpslaacl qlllrggfde
      241 dvkakvenll gisslektdp vregagsfpg snilalvtqv slhlrssvda llegnryvtg
      301 wfspyhrqrk lihpvmvqhi qpaalsllaq wstlvqelea alqlafypda veewleenvh
      361 pslqrlqall qdlsevsapp lpptspgrdv aqdp
//
LOCUS       NP_064543                235 aa            linear   PRI 27-APR-2025
DEFINITION  exosome complex component RRP46 [Homo sapiens].
ACCESSION   NP_064543
VERSION     NP_064543.3
DBSOURCE    REFSEQ: accession NM_020158.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Calame,D.G., Herman,I., Fatih,J.M., Du,H., Akay,G., Jhangiani,S.N.,
            Coban-Akdemir,Z., Milewicz,D.M., Gibbs,R.A., Posey,J.E., Marafi,D.,
            Hunter,J.V., Fan,Y., Lupski,J.R. and Miyake,C.Y.
  TITLE     Risk of sudden cardiac death in EXOSC5-related disease
  JOURNAL   Am J Med Genet A 185 (8), 2532-2540 (2021)
   PUBMED   34089229
  REMARK    GeneRIF: Risk of sudden cardiac death in EXOSC5-related disease.
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Slavotinek,A., Misceo,D., Htun,S., Mathisen,L., Frengen,E.,
            Foreman,M., Hurtig,J.E., Enyenihi,L., Sterrett,M.C., Leung,S.W.,
            Schneidman-Duhovny,D., Estrada-Veras,J., Duncan,J.L., Haaxma,C.A.,
            Kamsteeg,E.J., Xia,V., Beleford,D., Si,Y., Douglas,G.,
            Treidene,H.E., van Hoof,A., Fasken,M.B. and Corbett,A.H.
  TITLE     Biallelic variants in the RNA exosome gene EXOSC5 are associated
            with developmental delays, short stature, cerebellar hypoplasia and
            motor weakness
  JOURNAL   Hum Mol Genet 29 (13), 2218-2239 (2020)
   PUBMED   32504085
  REMARK    GeneRIF: Biallelic variants in the RNA exosome gene EXOSC5 are
            associated with developmental delays, short stature, cerebellar
            hypoplasia and motor weakness.
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Raijmakers,R., Noordman,Y.E., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Protein-protein interactions of hCsl4p with other human exosome
            subunits
  JOURNAL   J Mol Biol 315 (4), 809-818 (2002)
   PUBMED   11812149
  REMARK    GeneRIF: association of hCsl4p with the exosome is mediated by
            protein-protein interactions with hRrp42p and hRrp46p
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Mukherjee,D., Gao,M., O'Connor,J.P., Raijmakers,R., Pruijn,G.,
            Lutz,C.S. and Wilusz,J.
  TITLE     The mammalian exosome mediates the efficient degradation of mRNAs
            that contain AU-rich elements
  JOURNAL   EMBO J 21 (1-2), 165-174 (2002)
   PUBMED   11782436
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Allmang,C., Petfalski,E., Podtelejnikov,A., Mann,M., Tollervey,D.
            and Mitchell,P.
  TITLE     The yeast exosome and human PM-Scl are related complexes of 3' -->
            5' exonucleases
  JOURNAL   Genes Dev 13 (16), 2148-2158 (1999)
   PUBMED   10465791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011462.4 and AF281134.1.
            
            On May 14, 2004 this sequence version replaced NP_064543.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF285785.1, SRR5189658.209245.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221233.9/ ENSP00000221233.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..235
                     /product="exosome complex component RRP46"
                     /note="exosome component Rrp46; exosome complex
                     exonuclease RRP46; ribosomal RNA-processing protein 46;
                     chronic myelogenous leukemia tumor antigen 28"
                     /calculated_mol_wt=25118
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQT4.1)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQT4.1)"
     Region          28..225
                     /region_name="RNase_PH_RRP46"
                     /note="RRP46 subunit of eukaryotic exosome; cd11372"
                     /db_xref="CDD:206777"
     Site            order(36,38..39,41..42,61..63,111,113,145,147..149,151,
                     188,225)
                     /site_type="other"
                     /note="Rrp40 interface [polypeptide binding]"
                     /db_xref="CDD:206777"
     Site            order(40,42,57,59..61,77,79,84,93,96,100,114,119,124,
                     142..144,192..203,206,210)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:206777"
     CDS             1..235
                     /gene="EXOSC5"
                     /gene_synonym="CABAC; hRrp46p; p12B; RRP41B; RRP46;
                     Rrp46p"
                     /coded_by="NM_020158.4:32..739"
                     /db_xref="CCDS:CCDS12580.1"
                     /db_xref="GeneID:56915"
                     /db_xref="HGNC:HGNC:24662"
                     /db_xref="MIM:606492"
ORIGIN      
        1 meeethtdak iraengtgss prgpgcslrh faceqnllsr pdgsasflqg dtsvlagvyg
       61 paevkvskei fnkatlevil rpkiglpgva eksrerlirn tceavvlgtl hprtsitvvl
      121 qvvsdagsll acclnaacma lvdagvpmra lfcgvacald sdgtlvldpt skqekearav
      181 ltfaldsver kllmsstkgl ysdtelqqcl aaaqaasqhv frfyreslqr rysks
//
LOCUS       NP_001357019             261 aa            linear   PRI 27-APR-2025
DEFINITION  gap junction beta-6 protein [Homo sapiens].
ACCESSION   NP_001357019
VERSION     NP_001357019.1
DBSOURCE    REFSEQ: accession NM_001370090.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   O'Shaughnessy,E.M., Duffy,W., Garcia-Vega,L., Hussey,K.,
            Burden,A.D., Zamiri,M. and Martin,P.E.
  TITLE     Dysregulation of Connexin Expression Plays a Pivotal Role in
            Psoriasis
  JOURNAL   Int J Mol Sci 22 (11), 6060 (2021)
   PUBMED   34199748
  REMARK    GeneRIF: Dysregulation of Connexin Expression Plays a Pivotal Role
            in Psoriasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Buonfiglio,P., Bruque,C.D., Luce,L., Giliberto,F., Lotersztein,V.,
            Menazzi,S., Paoli,B., Elgoyhen,A.B. and Dalamon,V.
  TITLE     GJB2 and GJB6 Genetic Variant Curation in an Argentinean
            Non-Syndromic Hearing-Impaired Cohort
  JOURNAL   Genes (Basel) 11 (10), 1233 (2020)
   PUBMED   33096615
  REMARK    GeneRIF: GJB2 and GJB6 Genetic Variant Curation in an Argentinean
            Non-Syndromic Hearing-Impaired Cohort.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Zhan,Y., Luo,S., Pi,Z. and Zhang,G.
  TITLE     A recurrent mutation of GJB6 in a big Chinese family with Hidrotic
            ectodermal dysplasia
  JOURNAL   Hereditas 157 (1), 34 (2020)
   PUBMED   32843087
  REMARK    GeneRIF: A recurrent mutation of GJB6 in a big Chinese family with
            Hidrotic ectodermal dysplasia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Eggena,M., Targan,S.R., Iwanczyk,L., Vidrich,A., Gordon,L.K. and
            Braun,J.
  TITLE     Phage display cloning and characterization of an immunogenetic
            marker (perinuclear anti-neutrophil cytoplasmic antibody) in
            ulcerative colitis
  JOURNAL   J Immunol 156 (10), 4005-4011 (1996)
   PUBMED   8621942
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Kibar,Z., Der Kaloustian,V.M., Brais,B., Hani,V., Fraser,F.C. and
            Rouleau,G.A.
  TITLE     The gene responsible for Clouston hidrotic ectodermal dysplasia
            maps to the pericentromeric region of chromosome 13q
  JOURNAL   Hum Mol Genet 5 (4), 543-547 (1996)
   PUBMED   8845850
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Stoppini,M., Bellotti,V., Negri,A., Merlini,G., Garver,F. and
            Ferri,G.
  TITLE     Characterization of the two unique human anti-flavin monoclonal
            immunoglobulins
  JOURNAL   Eur J Biochem 228 (3), 886-893 (1995)
   PUBMED   7737190
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Smith,R.J.H. and Ranum,P.T.
  TITLE     Nonsyndromic Hearing Loss and Deafness, DFNA3 - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301708
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Smith,R.J.H., Azaiez,H. and Booth,K.
  TITLE     GJB2-Related Autosomal Recessive Nonsyndromic Hearing Loss
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301449
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Mellerio,J. and Greenblatt,D.
  TITLE     Hidrotic Ectodermal Dysplasia 2
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301379
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355984.11.
            
            Summary: Gap junctions allow the transport of ions and metabolites
            between the cytoplasm of adjacent cells. They are formed by two
            hemichannels, made up of six connexin proteins assembled in groups.
            Each connexin protein has four transmembrane segments, two
            extracellular loops, a cytoplasmic loop formed between the two
            inner transmembrane segments, and the N- and C-terminus both being
            in the cytoplasm. The specificity of the gap junction is determined
            by which connexin proteins comprise the hemichannel. In the past,
            connexin protein names were based on their molecular weight,
            however the new nomenclature uses sequential numbers based on which
            form (alpha or beta) of the gap junction is present. This gene
            encodes one of the connexin proteins. Mutations in this gene have
            been found in some forms of deafness and in some families with
            hidrotic ectodermal dysplasia. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.183949.1, AY789476.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147596 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..261
                     /product="gap junction beta-6 protein"
                     /note="ectodermal dysplasia 2, hidrotic (Clouston
                     syndrome); connexin 30; gap junction protein, beta 6,
                     30kDa"
                     /calculated_mol_wt=30256
     Region          2..215
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            23..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     Site            76..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     Site            132..154
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     Site            193..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     CDS             1..261
                     /gene="GJB6"
                     /gene_synonym="CX30; DFNA3; DFNA3B; DFNB1B; ECTD2; ED2;
                     EDH; HED; HED2"
                     /coded_by="NM_001370090.1:552..1337"
                     /db_xref="CCDS:CCDS9291.1"
                     /db_xref="GeneID:10804"
                     /db_xref="HGNC:HGNC:4288"
                     /db_xref="MIM:604418"
ORIGIN      
        1 mdwgtlhtfi ggvnkhstsi gkvwitvifi frvmilvvaa qevwgdeqed fvcntlqpgc
       61 knvcydhffp vshirlwalq lifvstpall vamhvayyrh ettrkfrrge krndfkdied
      121 ikkqkvrieg slwwtytssi ffriifeaaf myvfyflyng yhlpwvlkcg idpcpnlvdc
      181 fisrptektv ftifmisasv icmllnvael cylllkvcfr rskraqtqkn hpnhalkesk
      241 qnemnelisd sgqnaitgfp s
//
LOCUS       NP_067066                 81 aa            linear   PRI 27-APR-2025
DEFINITION  costars family protein ABRACL [Homo sapiens].
ACCESSION   NP_067066 XP_371848 XP_946232
VERSION     NP_067066.1
DBSOURCE    REFSEQ: accession NM_021243.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Li,J. and Chen,H.
  TITLE     Actin-binding Rho activating C-terminal like (ABRACL)
            transcriptionally regulated by MYB proto-oncogene like 2 (MYBL2)
            promotes the proliferation, invasion, migration and
            epithelial-mesenchymal transition of breast cancer cells
  JOURNAL   Bioengineered 13 (4), 9019-9031 (2022)
   PUBMED   35341461
  REMARK    GeneRIF: Actin-binding Rho activating C-terminal like (ABRACL)
            transcriptionally regulated by MYB proto-oncogene like 2 (MYBL2)
            promotes the proliferation, invasion, migration and
            epithelial-mesenchymal transition of breast cancer cells.
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Fan,S., Chen,P. and Li,S.
  TITLE     miR-145-5p Inhibits the Proliferation, Migration, and Invasion of
            Esophageal Carcinoma Cells by Targeting ABRACL
  JOURNAL   Biomed Res Int 2021, 6692544 (2021)
   PUBMED   33728339
  REMARK    GeneRIF: miR-145-5p Inhibits the Proliferation, Migration, and
            Invasion of Esophageal Carcinoma Cells by Targeting ABRACL.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Hsiao,B.Y., Chen,C.H., Chi,H.Y., Yen,P.R., Yu,Y.Z., Lin,C.H.,
            Pang,T.L., Lin,W.C., Li,M.L., Yeh,Y.C., Chou,T.Y. and Chen,M.Y.
  TITLE     Human Costars Family Protein ABRACL Modulates Actin Dynamics and
            Cell Migration and Associates with Tumorigenic Growth
  JOURNAL   Int J Mol Sci 22 (4), 2037 (2021)
   PUBMED   33670794
  REMARK    GeneRIF: Human Costars Family Protein ABRACL Modulates Actin
            Dynamics and Cell Migration and Associates with Tumorigenic Growth.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Lin,J., Zhou,T. and Wang,J.
  TITLE     Solution structure of the human HSPC280 protein
  JOURNAL   Protein Sci 20 (1), 216-223 (2011)
   PUBMED   21082705
  REMARK    GeneRIF: Solution structure of the human HSPC280 protein
            Erratum:[Protein Sci. 2011 Sep;20(9):1644]
REFERENCE   5  (residues 1 to 81)
  AUTHORS   Pang,T.L., Chen,F.C., Weng,Y.L., Liao,H.C., Yi,Y.H., Ho,C.L.,
            Lin,C.H. and Chen,M.Y.
  TITLE     Costars, a Dictyostelium protein similar to the C-terminal domain
            of STARS, regulates the actin cytoskeleton and motility
  JOURNAL   J Cell Sci 123 (Pt 21), 3745-3755 (2010)
   PUBMED   20940261
REFERENCE   6  (residues 1 to 81)
  AUTHORS   Molina,H., Bunkenborg,J., Reddy,G.H., Muthusamy,B., Scheel,P.J. and
            Pandey,A.
  TITLE     A proteomic analysis of human hemodialysis fluid
  JOURNAL   Mol Cell Proteomics 4 (5), 637-650 (2005)
   PUBMED   15723814
REFERENCE   7  (residues 1 to 81)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG563686.1 and AF116682.1.
            
            On or before Jul 26, 2007 this sequence version replaced
            XP_371848.5, XP_946232.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.36065.1,
                                           SRR1163658.170877.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367660.4/ ENSP00000356632.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.1"
     Protein         1..81
                     /product="costars family protein ABRACL"
                     /note="ABRA C-terminal-like protein"
                     /calculated_mol_wt=8925
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9P1F3.1)"
     Region          2..79
                     /region_name="Costars"
                     /note="pfam14705"
                     /db_xref="CDD:464274"
     CDS             1..81
                     /gene="ABRACL"
                     /gene_synonym="C6orf115; Costars; HSPC280; PRO2013"
                     /coded_by="NM_021243.3:138..383"
                     /db_xref="CCDS:CCDS43509.1"
                     /db_xref="GeneID:58527"
                     /db_xref="HGNC:HGNC:21230"
ORIGIN      
        1 mnvdhevnll veeihrlgsk nadgklsvkf gvlfrddkca nlfealvgtl kaakrrkivt
       61 ypgelllqgv hddvdiillq d
//
LOCUS       NP_001357320             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357320
VERSION     NP_001357320.1
DBSOURCE    REFSEQ: accession NM_001370391.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.54696.1,
                                           SRR1803614.254584.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370391.1:1609..3258"
                     /note="isoform 1 is encoded by transcript variant 20"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_851320                440 aa            linear   PRI 27-APR-2025
DEFINITION  integral membrane protein GPR180 precursor [Homo sapiens].
ACCESSION   NP_851320
VERSION     NP_851320.1
DBSOURCE    REFSEQ: accession NM_180989.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Yoshida,K., Yokota,K., Watanabe,K., Tsuda,H., Matsumoto,A.,
            Mizukami,H. and Iwamoto,S.
  TITLE     Lack of GPR180 ameliorates hepatic lipid depot via downregulation
            of mTORC1 signaling
  JOURNAL   Sci Rep 13 (1), 1843 (2023)
   PUBMED   36726016
  REMARK    GeneRIF: Lack of GPR180 ameliorates hepatic lipid depot via
            downregulation of mTORC1 signaling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Balazova,L., Balaz,M., Horvath,C., Horvath,A., Moser,C.,
            Kovanicova,Z., Ghosh,A., Ghoshdastider,U., Efthymiou,V.,
            Kiehlmann,E., Sun,W., Dong,H., Ding,L., Amri,E.Z., Nuutila,P.,
            Virtanen,K.A., Niemi,T., Ukropcova,B., Ukropec,J., Pelczar,P.,
            Lamla,T., Hamilton,B., Neubauer,H. and Wolfrum,C.
  TITLE     GPR180 is a component of TGFbeta signalling that promotes
            thermogenic adipocyte function and mediates the metabolic effects
            of the adipocyte-secreted factor CTHRC1
  JOURNAL   Nat Commun 12 (1), 7144 (2021)
   PUBMED   34880217
  REMARK    GeneRIF: GPR180 is a component of TGFbeta signalling that promotes
            thermogenic adipocyte function and mediates the metabolic effects
            of the adipocyte-secreted factor CTHRC1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Pozza,E., Verdin,H., Deconinck,H., Dheedene,A., Menten,B., De
            Baere,E. and Balikova,I.
  TITLE     Microcoria due to first duplication of 13q32.1 including the GPR180
            gene and maternal mosaicism
  JOURNAL   Eur J Med Genet 63 (5), 103918 (2020)
   PUBMED   32200002
  REMARK    GeneRIF: Microcoria due to first duplication of 13q32.1 including
            the GPR180 gene and maternal mosaicism.
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Fares-Taie,L., Gerber,S., Tawara,A., Ramirez-Miranda,A.,
            Douet,J.Y., Verdin,H., Guilloux,A., Zenteno,J.C., Kondo,H.,
            Moisset,H., Passet,B., Yamamoto,K., Iwai,M., Tanaka,T.,
            Nakamura,Y., Kimura,W., Bole-Feysot,C., Vilotte,M., Odent,S.,
            Vilotte,J.L., Munnich,A., Regnier,A., Chassaing,N., De Baere,E.,
            Raymond-Letron,I., Kaplan,J., Calvas,P., Roche,O. and Rozet,J.M.
  TITLE     Submicroscopic deletions at 13q32.1 cause congenital microcoria
  JOURNAL   Am J Hum Genet 96 (4), 631-639 (2015)
   PUBMED   25772937
  REMARK    GeneRIF: A null GPR180 mutation segregates over two generations
            with iridocorneal angle dysgenesis, consistent with the view that
            deletions of this gene are the cause of MCOR.
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Tsukada,S., Iwai,M., Nishiu,J., Itoh,M., Tomoike,H., Horiuchi,M.,
            Nakamura,Y. and Tanaka,T.
  TITLE     Inhibition of experimental intimal thickening in mice lacking a
            novel G-protein-coupled receptor
  JOURNAL   Circulation 107 (2), 313-319 (2003)
   PUBMED   12538434
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Iida,A., Tanaka,T. and Nakamura,Y.
  TITLE     High-density SNP map of human ITR, a gene associated with vascular
            remodeling
  JOURNAL   J Hum Genet 48 (4), 170-172 (2003)
   PUBMED   12730718
  REMARK    GeneRIF: 22 SNPs were isolated from the ITR locus by systematically
            screening genomic DNA from 48 healthy Japanese individuals
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD110068.1, BC052243.1,
            DB150630.1, AL359708.8 and AL049452.1.
            
            Summary: This gene encodes a protein that is a member of the G
            protein-coupled receptor superfamily. This protein is produced
            predominantly in vascular smooth muscle cells and may play an
            important role in the regulation of vascular remodeling. [provided
            by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.224667.1,
                                           SRR1660805.140334.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376958.5/ ENSP00000366157.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q32.1"
     Protein         1..440
                     /product="integral membrane protein GPR180 precursor"
                     /note="intimal thickness-related receptor; integral
                     membrane protein GPR180"
                     /calculated_mol_wt=47066
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2348
     mat_peptide     23..440
                     /product="integral membrane protein GPR180"
                     /calculated_mol_wt=47066
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86V85.1)"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86V85.1)"
     Region          141..405
                     /region_name="GpcrRhopsn4"
                     /note="Rhodopsin-like GPCR transmembrane domain;
                     pfam10192"
                     /db_xref="CDD:462989"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86V85.1)"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86V85.1)"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86V85.1)"
     Site            284..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86V85.1)"
     Site            321..341
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86V85.1)"
     Site            360..380
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86V85.1)"
     Site            389..409
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86V85.1)"
     CDS             1..440
                     /gene="GPR180"
                     /gene_synonym="ITR"
                     /coded_by="NM_180989.6:72..1394"
                     /db_xref="CCDS:CCDS9472.1"
                     /db_xref="GeneID:160897"
                     /db_xref="HGNC:HGNC:28899"
                     /db_xref="MIM:607787"
ORIGIN      
        1 mgglrllava ltccwwpqgs qgktlrgsfs staaqdaqgq righfefhgd hallcvrinn
       61 iavavgkeak lylfqaqewl klqqsshgys cseklskaql tmtmnqtehn ltvsqipspq
      121 twhvfyadky tcqddkensq vedipfemvl lnpdaegnpf dhfsagesgl hefffllvlv
      181 yfviaciyaq slwqaikkgg pmhmilkvlt talllqagsa lanyihfssy skdgigvpfm
      241 gslaeffdia sqiqmlylll slcmgwtivr mkksqsrplq wdstpastgi avfivmtqsv
      301 lllweqfedi shhsyhshhn lagillivlr iclalslgcg lyqiitvers tlkrefyitf
      361 akgcilwflc hpvlacisvi fsdyqrdkvi tigvilcqsv smvilyrlfl shslywevss
      421 lssvtlplti ssghksrphf
//
LOCUS       NP_001159743            1277 aa            linear   PRI 27-APR-2025
DEFINITION  spermatogenesis-associated protein 13 isoform 1 [Homo sapiens].
ACCESSION   NP_001159743
VERSION     NP_001159743.1
DBSOURCE    REFSEQ: accession NM_001166271.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1277)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   2  (residues 1 to 1277)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1277)
  AUTHORS   Waseem,N.H., Low,S., Shah,A.Z., Avisetti,D., Ostergaard,P.,
            Simpson,M., Niemiec,K.A., Martin-Martin,B., Aldehlawi,H., Usman,S.,
            Lee,P.S., Khawaja,A.P., Ruddle,J.B., Shah,A., Sackey,E., Day,A.,
            Jiang,Y., Swinfield,G., Viswanathan,A., Alfano,G., Chakarova,C.,
            Cordell,H.J., Garway-Heath,D.F., Khaw,P.T., Bhattacharya,S.S.,
            Waseem,A. and Foster,P.J.
  TITLE     Mutations in SPATA13/ASEF2 cause primary angle closure glaucoma
  JOURNAL   PLoS Genet 16 (4), e1008721 (2020)
   PUBMED   32339198
  REMARK    GeneRIF: Mutations in SPATA13 cause primary angle closure glaucoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1277)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 1277)
  AUTHORS   Evans,J.C., Hines,K.M., Forsythe,J.G., Erdogan,B., Shi,M., Hill,S.,
            Rose,K.L., McLean,J.A. and Webb,D.J.
  TITLE     Phosphorylation of serine 106 in Asef2 regulates cell migration and
            adhesion turnover
  JOURNAL   J Proteome Res 13 (7), 3303-3313 (2014)
   PUBMED   24874604
  REMARK    GeneRIF: Phosphorylation of S106 modulates Asef2 guanine nucleotide
            exchange factor activity and Asef2-mediated cell migration and
            adhesion turnover.
REFERENCE   6  (residues 1 to 1277)
  AUTHORS   Bristow,J.M., Sellers,M.H., Majumdar,D., Anderson,B., Hu,L. and
            Webb,D.J.
  TITLE     The Rho-family GEF Asef2 activates Rac to modulate adhesion and
            actin dynamics and thereby regulate cell migration
  JOURNAL   J Cell Sci 122 (Pt 24), 4535-4546 (2009)
   PUBMED   19934221
  REMARK    GeneRIF: Asef2 activates Rac1 to modulate adhesion and actin
            dynamics and thereby regulate cell migration.
REFERENCE   7  (residues 1 to 1277)
  AUTHORS   Sagara,M., Kawasaki,Y., Iemura,S.I., Natsume,T., Takai,Y. and
            Akiyama,T.
  TITLE     Asef2 and Neurabin2 cooperatively regulate actin cytoskeletal
            organization and are involved in HGF-induced cell migration
  JOURNAL   Oncogene 28 (10), 1357-1365 (2009)
   PUBMED   19151759
  REMARK    GeneRIF: Asef2, Neurabin2 and APC cooperatively regulate actin
            cytoskeletal organization and are required for HGF-induced cell
            migration.
REFERENCE   8  (residues 1 to 1277)
  AUTHORS   Lasky-Su,J., Neale,B.M., Franke,B., Anney,R.J., Zhou,K.,
            Maller,J.B., Vasquez,A.A., Chen,W., Asherson,P., Buitelaar,J.,
            Banaschewski,T., Ebstein,R., Gill,M., Miranda,A., Mulas,F.,
            Oades,R.D., Roeyers,H., Rothenberger,A., Sergeant,J.,
            Sonuga-Barke,E., Steinhausen,H.C., Taylor,E., Daly,M., Laird,N.,
            Lange,C. and Faraone,S.V.
  TITLE     Genome-wide association scan of quantitative traits for attention
            deficit hyperactivity disorder identifies novel associations and
            confirms candidate gene associations
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 147B (8), 1345-1354 (2008)
   PUBMED   18821565
REFERENCE   9  (residues 1 to 1277)
  AUTHORS   Kawasaki,Y., Sagara,M., Shibata,Y., Shirouzu,M., Yokoyama,S. and
            Akiyama,T.
  TITLE     Identification and characterization of Asef2, a guanine-nucleotide
            exchange factor specific for Rac1 and Cdc42
  JOURNAL   Oncogene 26 (55), 7620-7267 (2007)
   PUBMED   17599059
  REMARK    GeneRIF: These results suggest that similar to Asef, Asef2 plays an
            important role in cell migration, and that Asef2 activated by
            truncated mutant APC is required for aberrant migration of
            colorectal tumor cells.
REFERENCE   10 (residues 1 to 1277)
  AUTHORS   Hamann,M.J., Lubking,C.M., Luchini,D.N. and Billadeau,D.D.
  TITLE     Asef2 functions as a Cdc42 exchange factor and is stimulated by the
            release of an autoinhibitory module from a concealed C-terminal
            activation element
  JOURNAL   Mol Cell Biol 27 (4), 1380-1393 (2007)
   PUBMED   17145773
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP201334.1, AK092754.1, AL359736.19, DB221004.1 and AK055770.1.
            
            Transcript Variant: This variant (1) encodes isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BX648244.1, SRR1803614.140528.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968540, SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000382108.8/ ENSP00000371542.3
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.12"
     Protein         1..1277
                     /product="spermatogenesis-associated protein 13 isoform 1"
                     /note="spermatogenesis-associated protein 13; adenomatous
                     polyposis coli stimulated exchange factor 2;
                     APC-stimulated guanine nucleotide exchange factor 2"
                     /calculated_mol_wt=141305
     Region          759..830
                     /region_name="SH3_ASEF"
                     /note="Src homology 3 domain of APC-Stimulated guanine
                     nucleotide Exchange Factor; cd11973"
                     /db_xref="CDD:212906"
     Site            order(759..768,770..771,803,806..807,820,830)
                     /site_type="other"
                     /note="APC binding site [polypeptide binding]"
                     /db_xref="CDD:212906"
     Site            order(778..780,785..786,788,816,824,827,829..830)
                     /site_type="other"
                     /note="DH-PH interface [polypeptide binding]"
                     /db_xref="CDD:212906"
     Site            order(781,783,786,790,808..809,822,824..825)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212906"
     Region          869..1048
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; smart00325"
                     /db_xref="CDD:214619"
     Site            order(872,876,971,998..999,1002..1003,1005..1006,
                     1009..1010,1013..1014,1017,1043,1047)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          1053..1191
                     /region_name="PH_Collybistin_ASEF"
                     /note="Collybistin/APC-stimulated guanine nucleotide
                     exchange factor pleckstrin homology (PH) domain; cd01224"
                     /db_xref="CDD:269931"
     CDS             1..1277
                     /gene="SPATA13"
                     /gene_synonym="ARHGEF29; ASEF2"
                     /coded_by="NM_001166271.3:325..4158"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53857.1"
                     /db_xref="GeneID:221178"
                     /db_xref="HGNC:HGNC:23222"
                     /db_xref="MIM:613324"
ORIGIN      
        1 mtqaavrpwa pclenmttap nglgpgpaap cagsdlkdak mvtslacgng vcgcspggdt
       61 dtqeaklspa klvrlfstsr krtgahperp hsmvlvgnss twntlasfrk mgsfkklkss
      121 vlkgiqsreg snacskgeas ehglgksipn gavpgaqasr gsplapgpac galrpaewgt
      181 ldgsdledtd dafqrsthrs rslrrayglg riclldapqn hatptiatgq vpavceilvr
      241 dpennsmgyr rskstdnlaf lkkssfkrks tsnladlrta hdarvpqrtl sssstdsqkl
      301 gsgrtkrwrs pirakdfdrv fklvsnvtea awrresprsg apspgeaslr lqahsrlhdd
      361 ysrrvsrste qdsrrggavm hgttatctva pgfgsatskg phldadtavf pletksswav
      421 esdssctcss lpspivqdvl skdscdpnag sqltfdpeqp ptplrpttpk pqspqspqsp
      481 gagsaschsn hsalsansee segraeepaq repgpvslqd pleathgdeg skdllvnigv
      541 aagpeekeke evvpdgpwrr sssqdeerte aqrtpkrrwg sgrrprprpf sdygqlasrs
      601 lsipedsvaa dpqkedrvde dpqasmtsas pedqnapvgc pkgarrrrpi sviggvslyg
      661 tnqteeldnl ltqpasrppm pahqvppyka vsarfrpftf sqstpigldr vgrrrqmras
      721 nvssdggtep salvddngse edfsyedlcq asprylqpgg eqlainelis dgnvvcaeal
      781 wdhvtmddqe lgfkagdviq vleasnkdww wgrsedkeaw fpasfvrlrv nqeelsenss
      841 stpseeqdee asqsrhrhce nkqqmrtnvi reimdtervy ikhlrdiceg yirqcrkhtg
      901 mftvaqlati fgniediykf qrkflkdlek qynkeephls eigscflqnq egfaiyseyc
      961 nnhpgaclel anlmkqgkyr hffeacrllq qmidiaidgf lltpvqkick yplqlaellk
     1021 yttqehgdys nikaayeamk nvaclinerk rklesidkia rwqvsivgwe gldildrsse
     1081 lihsgeltki tkqgksqqrt fflfdhqlvs ckkdllrrdm lyykgrldmd emelvdlgdg
     1141 rdkdcnlsvk nafklvsrtt devylfcakk qedkarwlqa caderrrvqe dkemgmeise
     1201 nqkklamlna qkaghgkskg ynrcpvapph qglhpihqrh itmptsvpqq qvfglaepkr
     1261 ksslfwhtfn rltpfrk
//
LOCUS       NP_008879                471 aa            linear   PRI 27-APR-2025
DEFINITION  heat shock 70 kDa protein 13 precursor [Homo sapiens].
ACCESSION   NP_008879
VERSION     NP_008879.3
DBSOURCE    REFSEQ: accession NM_006948.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Espinoza,M.F., Nguyen,K.K., Sycks,M.M., Lyu,Z., Quanrud,G.M.,
            Montoya,M.R. and Genereux,J.C.
  TITLE     Heat shock protein Hspa13 regulates endoplasmic reticulum and
            cytosolic proteostasis through modulation of protein translocation
  JOURNAL   J Biol Chem 298 (12), 102597 (2022)
   PUBMED   36244454
  REMARK    GeneRIF: Heat shock protein Hspa13 regulates endoplasmic reticulum
            and cytosolic proteostasis through modulation of protein
            translocation.
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Bakhos-Douaihy,D., Seaayfan,E., Demaretz,S., Komhoff,M. and
            Laghmani,K.
  TITLE     Differential Effects of STCH and Stress-Inducible Hsp70 on the
            Stability and Maturation of NKCC2
  JOURNAL   Int J Mol Sci 22 (4), 2207 (2021)
   PUBMED   33672238
  REMARK    GeneRIF: Differential Effects of STCH and Stress-Inducible Hsp70 on
            the Stability and Maturation of NKCC2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 471)
  AUTHORS   He,Y., Xu,R., Zhai,B., Fang,Y., Hou,C., Xing,C., Xiao,H., Chen,G.,
            Wang,X., Ma,N., Han,G. and Wang,R.
  TITLE     Hspa13 Promotes Plasma Cell Production and Antibody Secretion
  JOURNAL   Front Immunol 11, 913 (2020)
   PUBMED   32547538
  REMARK    GeneRIF: Hspa13 Promotes Plasma Cell Production and Antibody
            Secretion.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Chouchane,L., Danguir,J., Beji,C., Bouassida,K., Camoin,L.,
            Sfar,H., Gabbouj,S. and Strosberg,A.D.
  TITLE     Genetic variation in the stress protein hsp70-2 gene is highly
            associated with obesity
  JOURNAL   Int J Obes Relat Metab Disord 25 (4), 462-466 (2001)
   PUBMED   11319647
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Kaye,F.J., Modi,S., Ivanovska,I., Koonin,E.V., Thress,K., Kubo,A.,
            Kornbluth,S. and Rose,M.D.
  TITLE     A family of ubiquitin-like proteins binds the ATPase domain of
            Hsp70-like Stch
  JOURNAL   FEBS Lett 467 (2-3), 348-355 (2000)
   PUBMED   10675567
REFERENCE   9  (residues 1 to 471)
  AUTHORS   Brodsky,G., Otterson,G.A., Parry,B.B., Hart,I., Patterson,D. and
            Kaye,F.J.
  TITLE     Localization of STCH to human chromosome 21q11.1
  JOURNAL   Genomics 30 (3), 627-628 (1995)
   PUBMED   8825657
REFERENCE   10 (residues 1 to 471)
  AUTHORS   Otterson,G.A., Flynn,G.C., Kratzke,R.A., Coxon,A., Johnston,P.G.
            and Kaye,F.J.
  TITLE     Stch encodes the 'ATPase core' of a microsomal stress 70 protein
  JOURNAL   EMBO J 13 (5), 1216-1225 (1994)
   PUBMED   8131751
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI548162.1, U04735.1,
            BC036370.2, CA392315.1, AA018751.1, CF141775.1, BE467288.1,
            AI912654.1 and AA767266.1.
            
            On Jun 18, 2004 this sequence version replaced NP_008879.2.
            
            Summary: The protein encoded by this gene is a member of the heat
            shock protein 70 family and is found associated with microsomes.
            Members of this protein family play a role in the processing of
            cytosolic and secretory proteins, as well as in the removal of
            denatured or incorrectly-folded proteins. The encoded protein
            contains an ATPase domain and has been shown to associate with a
            ubiquitin-like protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036370.2, HM005612.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000285667.4/ ENSP00000285667.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q11.2"
     Protein         1..471
                     /product="heat shock 70 kDa protein 13 precursor"
                     /note="stress 70 protein chaperone, microsome-associated,
                     60kDa; microsomal stress 70 protein ATPase core; heat
                     shock 70 kDa protein 13; stress-70 protein chaperone
                     microsome-associated 60 kDa protein; heat shock protein
                     70kDa family, member 13; testis secretory sperm-binding
                     protein Li 199a; heat shock protein family A member 13"
                     /calculated_mol_wt=51797
     Region          10..452
                     /region_name="ASKHA_NBD_HSP70_HSPA13"
                     /note="nucleotide-binding domain (NBD) of heat shock 70
                     kDa protein 13 (HSPA13) and similar proteins; cd10237"
                     /db_xref="CDD:466835"
     mat_peptide     23..471
                     /product="heat shock 70 kDa protein 13"
                     /calculated_mol_wt=49638
     Region          315..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48723.1)"
     CDS             1..471
                     /gene="HSPA13"
                     /gene_synonym="STCH"
                     /coded_by="NM_006948.5:28..1443"
                     /db_xref="CCDS:CCDS13567.1"
                     /db_xref="GeneID:6782"
                     /db_xref="HGNC:HGNC:11375"
                     /db_xref="MIM:601100"
ORIGIN      
        1 maremtilgs avltlllagy laqqylplpt pkvigidlgt tycsvgvffp gtgkvkvipd
       61 enghisipsm vsftdndvyv gyesvelads npqntiydak rfigkiftae eleaeigryp
      121 fkvlnkngmv efsvtsneti tvspeyvgsr lllklkemae aylgmpvana visvpaefdl
      181 kqrnstieaa nlaglkilrv ineptaaama yglhkadvfh vlvidlgggt ldvsllnkqg
      241 gmfltramsg nnklggqdfn qrllqylykq iyqtygfvps rkeeihrlrq avemvklnlt
      301 lhqsaqlsvl ltveeqdrke phssdtelpk dklssaddhr vnsgfgrgls dkksgesqvl
      361 feteisrklf dtlnedlfqk ilvpiqqvlk eghlekteid evvlvggstr iprirqviqe
      421 ffgkdpntsv dpdlavvtgv aiqagidggs wplqvsalei pnkhlqktnf n
//
LOCUS       NP_001351332             580 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger CCCH domain-containing protein 14 isoform h [Mus
            musculus].
ACCESSION   NP_001351332 XP_006516394
VERSION     NP_001351332.1
DBSOURCE    REFSEQ: accession NM_001364403.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Li,Q., Yang,G., Ren,B., Liu,X., Tang,L.Q., Shi,Q., Shan,G. and
            Wang,X.
  TITLE     ZC3H14 facilitates backsplicing by binding to exon-intron boundary
            and 3' UTR
  JOURNAL   Mol Cell 84 (22), 4314-4333 (2024)
   PUBMED   39461343
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Corgiat,E.B., List,S.M., Rounds,J.C., Corbett,A.H. and Moberg,K.H.
  TITLE     The RNA-binding protein Nab2 regulates the proteome of the
            developing Drosophila brain
  JOURNAL   J Biol Chem 297 (1), 100877 (2021)
   PUBMED   34139237
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Wheeler,J.M., McMillan,P., Strovas,T.J., Liachko,N.F.,
            Amlie-Wolf,A., Kow,R.L., Klein,R.L., Szot,P., Robinson,L.,
            Guthrie,C., Saxton,A., Kanaan,N.M., Raskind,M., Peskind,E.,
            Trojanowski,J.Q., Lee,V.M.Y., Wang,L.S., Keene,C.D., Bird,T.,
            Schellenberg,G.D. and Kraemer,B.
  TITLE     Activity of the poly(A) binding protein MSUT2 determines
            susceptibility to pathological tau in the mammalian brain
  JOURNAL   Sci Transl Med 11 (523) (2019)
   PUBMED   31852801
REFERENCE   5  (residues 1 to 580)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 580)
  AUTHORS   Rha,J., Jones,S.K., Fidler,J., Banerjee,A., Leung,S.W.,
            Morris,K.J., Wong,J.C., Inglis,G.A.S., Shapiro,L., Deng,Q.,
            Cutler,A.A., Hanif,A.M., Pardue,M.T., Schaffer,A., Seyfried,N.T.,
            Moberg,K.H., Bassell,G.J., Escayg,A., Garcia,P.S. and Corbett,A.H.
  TITLE     The RNA-binding protein, ZC3H14, is required for proper poly(A)
            tail length control, expression of synaptic proteins, and brain
            function in mice
  JOURNAL   Hum Mol Genet 26 (19), 3663-3681 (2017)
   PUBMED   28666327
  REMARK    GeneRIF: Among the proteins increased in the hippocampi of
            Zc3h14Deltaex13/Deltaex13 mice compared to control are key synaptic
            proteins including CaMK2a. This newly generated mouse serves as a
            tool to study the function of ZC3H14 in vivo.
REFERENCE   7  (residues 1 to 580)
  AUTHORS   Watanabe,K., Takebayashi,H., Bepari,A.K., Esumi,S., Yanagawa,Y. and
            Tamamaki,N.
  TITLE     Dpy19l1, a multi-transmembrane protein, regulates the radial
            migration of glutamatergic neurons in the developing cerebral
            cortex
  JOURNAL   Development 138 (22), 4979-4990 (2011)
   PUBMED   22028030
  REMARK    Erratum:[Development. 2012 Mar;139(6):1225]
REFERENCE   8  (residues 1 to 580)
  AUTHORS   Pak,C., Garshasbi,M., Kahrizi,K., Gross,C., Apponi,L.H., Noto,J.J.,
            Kelly,S.M., Leung,S.W., Tzschach,A., Behjati,F., Abedini,S.S.,
            Mohseni,M., Jensen,L.R., Hu,H., Huang,B., Stahley,S.N., Liu,G.,
            Williams,K.R., Burdick,S., Feng,Y., Sanyal,S., Bassell,G.J.,
            Ropers,H.H., Najmabadi,H., Corbett,A.H., Moberg,K.H. and Kuss,A.W.
  TITLE     Mutation of the conserved polyadenosine RNA binding protein,
            ZC3H14/dNab2, impairs neural function in Drosophila and humans
  JOURNAL   Proc Natl Acad Sci U S A 108 (30), 12390-12395 (2011)
   PUBMED   21734151
REFERENCE   9  (residues 1 to 580)
  AUTHORS   Leung,S.W., Apponi,L.H., Cornejo,O.E., Kitchen,C.M.,
            Valentini,S.R., Pavlath,G.K., Dunham,C.M. and Corbett,A.H.
  TITLE     Splice variants of the human ZC3H14 gene generate multiple isoforms
            of a zinc finger polyadenosine RNA binding protein
  JOURNAL   Gene 439 (1-2), 71-78 (2009)
   PUBMED   19303045
REFERENCE   10 (residues 1 to 580)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC159193.2.
            
            On Jun 15, 2018 this sequence version replaced XP_006516394.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.518838.1,
                                           SRR7974084.29104.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 49.88 cM"
     Protein         1..580
                     /product="zinc finger CCCH domain-containing protein 14
                     isoform h"
                     /note="zinc finger CCCH domain-containing protein 14"
                     /calculated_mol_wt=64999
     Region          446..463
                     /region_name="zf-CCCH_2"
                     /note="RNA-binding, Nab2-type zinc finger; pfam14608"
                     /db_xref="CDD:464217"
     Region          466..484
                     /region_name="zf-CCCH_2"
                     /note="RNA-binding, Nab2-type zinc finger; pfam14608"
                     /db_xref="CDD:464217"
     Region          525..542
                     /region_name="zf-CCCH_2"
                     /note="RNA-binding, Nab2-type zinc finger; pfam14608"
                     /db_xref="CDD:464217"
     CDS             1..580
                     /gene="Zc3h14"
                     /gene_synonym="1010001P15Rik; 1700016A15Rik;
                     2700069A02Rik"
                     /coded_by="NM_001364403.1:506..2248"
                     /note="isoform h is encoded by transcript variant 9"
                     /db_xref="GeneID:75553"
                     /db_xref="MGI:MGI:1919824"
ORIGIN      
        1 mstvkplrep apsedvidik pepddlided lnfvqenpls qkkptvtlty gssrpsieiy
       61 rppasrnadt gthlnrlqlh pqqssahaak qldvqssqvs eagrlceppv lssvedtysp
      121 ffrnnldkms iedenfrkrk lpvvssvvkv krfshdgeee eededygtri gslsssvsvp
      181 akperrpslp pskqanknli lkaiseaqes vtkttnysav pqkqtlpvap rtrtsqeell
      241 aemvqgqnra prisppvkee eakgdntgks qgtqqrqlls rlqidpvmve tmemsqdyyd
      301 mesmvhadtr sfilkkpkls eeivvtpnqd sgmktadalr vlsghlmqtr dlvqpdkpas
      361 pkfivtldgv psppgymsdq eeemcfegmk pvnqtsasnk glrgllhpqq lhllsrqled
      421 pdgsfsnaem tdlsvaqkpe kllerckywp ackngdecvy hhpispckaf pnckfaekcl
      481 fvhpnckydt kctkadcpft hmsrrasilt pkpvsspaps sngqlcryfp ackkmecpfy
      541 hpkhcrfntq ctrpdctfyh ptitvpprha lkwirpqsse
//
LOCUS       NP_543154                325 aa            linear   PRI 27-APR-2025
DEFINITION  intelectin-2 precursor [Homo sapiens].
ACCESSION   NP_543154
VERSION     NP_543154.1
DBSOURCE    REFSEQ: accession NM_080878.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Nonnecke,E.B., Castillo,P.A., Johansson,M.E.V., Hollox,E.J.,
            Shen,B., Lonnerdal,B. and Bevins,C.L.
  TITLE     Human intelectin-2 (ITLN2) is selectively expressed by secretory
            Paneth cells
  JOURNAL   FASEB J 36 (3), e22200 (2022)
   PUBMED   35182405
  REMARK    GeneRIF: Human intelectin-2 (ITLN2) is selectively expressed by
            secretory Paneth cells.
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Yan,J., Xu,L., Zhang,Y., Zhang,C., Zhang,C., Zhao,F. and Feng,L.
  TITLE     Comparative genomic and phylogenetic analyses of the intelectin
            gene family: implications for their origin and evolution
  JOURNAL   Dev Comp Immunol 41 (2), 189-199 (2013)
   PUBMED   23643964
  REMARK    GeneRIF: Studies indicate that ITLN1 and ITLN2 intelectins are
            positioned on a single chromosome 1, suggesting mammalian
            intelectins have been independently expanded by partial gene
            duplication.
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Jablonski,K.A., McAteer,J.B., de Bakker,P.I., Franks,P.W.,
            Pollin,T.I., Hanson,R.L., Saxena,R., Fowler,S., Shuldiner,A.R.,
            Knowler,W.C., Altshuler,D. and Florez,J.C.
  CONSRTM   Diabetes Prevention Program Research Group
  TITLE     Common variants in 40 genes assessed for diabetes incidence and
            response to metformin and lifestyle intervention in the diabetes
            prevention program
  JOURNAL   Diabetes 59 (10), 2672-2681 (2010)
   PUBMED   20682687
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 325)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 325)
  AUTHORS   Lee,J.K., Schnee,J., Pang,M., Wolfert,M., Baum,L.G., Moremen,K.W.
            and Pierce,M.
  TITLE     Human homologs of the Xenopus oocyte cortical granule lectin XL35
  JOURNAL   Glycobiology 11 (1), 65-73 (2001)
   PUBMED   11181563
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591806.16, AY358905.1 and AL354714.22.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358905.1, AY065973.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368029.4/ ENSP00000357008.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..325
                     /product="intelectin-2 precursor"
                     /note="endothelial lectin HL-2"
                     /calculated_mol_wt=33342
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2888
     mat_peptide     27..325
                     /product="Intelectin-2. /id=PRO_0000009149"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWU7.1)"
                     /calculated_mol_wt=33342
     Region          52..94
                     /region_name="GGGWT_bact"
                     /note="fibrinogen-like bacterial YCDxxxxGGGW domain;
                     NF040941"
                     /db_xref="CDD:468872"
     CDS             1..325
                     /gene="ITLN2"
                     /gene_synonym="HL-2; HL2"
                     /coded_by="NM_080878.3:69..1046"
                     /note="PRO7179"
                     /db_xref="CCDS:CCDS1212.1"
                     /db_xref="GeneID:142683"
                     /db_xref="HGNC:HGNC:20599"
                     /db_xref="MIM:609874"
ORIGIN      
        1 mlsmlrtmtr lcfllffsva tsgcsaaaas slemlsrefe tcafsfsslp rsckeikerc
       61 hsagdglyfl rtkngvvyqt fcdmtsgggg wtlvasvhen dmrgkctvgd rwssqqgnka
      121 dypegdgnwa nyntfgsaea atsddyknpg yydiqakdlg iwhvpnkspm qhwrnsallr
      181 yrtntgflqr lghnlfgiyq kypvkyrsgk cwndngpaip vvydfgdakk tasyyspygq
      241 refvagfvqf rvfnneraan alcagikvtg cntehhcigg ggffpqgkpr qcgdfsafdw
      301 dgygthvkss csreiteaav llfyr
//
LOCUS       NP_001258567             287 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 138 isoform 5 [Homo sapiens].
ACCESSION   NP_001258567
VERSION     NP_001258567.2
DBSOURCE    REFSEQ: accession NM_001271638.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073349.11.
            
            On Dec 8, 2018 this sequence version replaced NP_001258567.1.
            
            Transcript Variant: This variant (6) includes an alternate exon,
            and initiates translation at a downstream in-frame start codon,
            compared to variant 1. The encoded isoform (5) has a shorter
            N-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC141847.1, DB461597.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..287
                     /product="zinc finger protein 138 isoform 5"
                     /note="zinc finger protein 138 (clone pHZ-32)"
                     /calculated_mol_wt=33555
     Region          2..>40
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          109..129
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          137..157
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          165..185
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(170,172,174,176..177,180..181,184,198,200,204..205,
                     208..209,212,226,228,230,232..233,236..237,240)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <187..270
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          193..213
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          221..241
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          249..266
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..287
                     /gene="ZNF138"
                     /gene_synonym="pHZ-32"
                     /coded_by="NM_001271638.2:249..1112"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS64661.1"
                     /db_xref="GeneID:7697"
                     /db_xref="HGNC:HGNC:12922"
                     /db_xref="MIM:604080"
ORIGIN      
        1 mdvaiefsle ewqcldtaqr nvyrhvmlen yrnlvflalc srfaqdlwle qnikdsfqkv
       61 tlsrygkygh knlqlrkgck svdeckghqg gfnglnqclk ittskifqcn kyvkvmhkfs
      121 nsnrhkirht enkhfrckec dkslcmlsrl tqhkkihtre nfykceecgk tfnwstnlsk
      181 pkkihtgekp ykcevcgkaf hqssiltkhk iirtgekpyk cahcgkafkq sshltrhkii
      241 hteekpykce qcgkvfkqsp tltkhqiiyt geepykceec gkafnls
//
LOCUS       NP_001353141             871 aa            linear   PRI 27-APR-2025
DEFINITION  disks large homolog 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001353141 XP_016861305
VERSION     NP_001353141.1
DBSOURCE    REFSEQ: accession NM_001366212.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Veljacic Viskovic,D., Lozic,M., Vukoja,M., Soljic,V., Vukojevic,K.,
            Glavina Durdov,M., Filipovic,N. and Lozic,B.
  TITLE     Spatio-Temporal Expression Pattern of CAKUT Candidate Genes DLG1
            and KIF12 during Human Kidney Development
  JOURNAL   Biomolecules 13 (2), 340 (2023)
   PUBMED   36830709
  REMARK    GeneRIF: Spatio-Temporal Expression Pattern of CAKUT Candidate
            Genes DLG1 and KIF12 during Human Kidney Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 871)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861305.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.22313.1,
                                           SRR11853565.21617.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..871
                     /product="disks large homolog 1 isoform 8"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=96945
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          680..858
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..871
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366212.1:624..3239"
                     /note="isoform 8 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS93452.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt snasdsessy
      661 rgqeeyvlsy epvnqqevny trpviilgpm kdrinddlis efpdkfgscv phttrpkrdy
      721 evdgrdyhfv tsreqmekdi qehkfieagq ynnhlygtsv qsvrevaekg khcildvsgn
      781 aikrlqiaql ypisifikpk smenimemnk rlteeqarkt feramkleqe ftehftaivq
      841 gdtlediynq vkqiieeqsg syiwvpakek l
//
LOCUS       NP_612409                860 aa            linear   PRI 27-APR-2025
DEFINITION  nucleolar MIF4G domain-containing protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_612409 XP_049384 XP_374590
VERSION     NP_612409.1
DBSOURCE    REFSEQ: accession NM_138400.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Solomon-Zemler,R., Pozniak,Y., Geiger,T. and Werner,H.
  TITLE     Identification of nucleolar protein NOM1 as a novel nuclear
            IGF1R-interacting protein
  JOURNAL   Mol Genet Metab 126 (3), 259-265 (2019)
   PUBMED   30639046
  REMARK    GeneRIF: Results are consistent with a physiologically-relevant
            interplay between the nuclear IGF1 signaling pathway and nucleolar
            protein NOM1.
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Alexandrov,A., Colognori,D. and Steitz,J.A.
  TITLE     Human eIF4AIII interacts with an eIF4G-like partner, NOM1,
            revealing an evolutionarily conserved function outside the exon
            junction complex
  JOURNAL   Genes Dev 25 (10), 1078-1090 (2011)
   PUBMED   21576267
  REMARK    GeneRIF: demonstrate direct physical interactions between yeast
            Sgd1p and Fal1p, and between their human orthologs (NOM1 and
            eIF4AIII) in vitro and in vivo, identifying human NOM1 as a missing
            eIF4G-like interacting partner of eIF4AIII
REFERENCE   6  (residues 1 to 860)
  AUTHORS   Gunawardena,S.R., Ruis,B.L., Meyer,J.A., Kapoor,M. and Conklin,K.F.
  TITLE     NOM1 targets protein phosphatase I to the nucleolus
  JOURNAL   J Biol Chem 283 (1), 398-404 (2008)
   PUBMED   17965019
  REMARK    GeneRIF: Data demonstrate that NOM1 can target PP1 to the nucleolus
            and show NOM1 nucleolar localization sequence are required for this
            targeting activity and conclude that NOM1 is a PP1 nucleolar
            targeting subunit, the first identified in eukaryotic cells.
REFERENCE   7  (residues 1 to 860)
  AUTHORS   Simmons,H.M., Ruis,B.L., Kapoor,M., Hudacek,A.W. and Conklin,K.F.
  TITLE     Identification of NOM1, a nucleolar, eIF4A binding protein encoded
            within the chromosome 7q36 breakpoint region targeted in cases of
            pediatric acute myeloid leukemia
  JOURNAL   Gene 347 (1), 137-145 (2005)
   PUBMED   15715967
REFERENCE   8  (residues 1 to 860)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   9  (residues 1 to 860)
  AUTHORS   Heus,H.C., Hing,A., van Baren,M.J., Joosse,M., Breedveld,G.J.,
            Wang,J.C., Burgess,A., Donnis-Keller,H., Berglund,C., Zguricas,J.,
            Scherer,S.W., Rommens,J.M., Oostra,B.A. and Heutink,P.
  TITLE     A physical and transcriptional map of the preaxial polydactyly
            locus on chromosome 7q36
  JOURNAL   Genomics 57 (3), 342-351 (1999)
   PUBMED   10329000
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006357.5 and AY576779.1.
            
            On or before Mar 14, 2005 this sequence version replaced
            XP_049384.9, XP_374590.3.
            
            Summary: Proteins that contain MIF4G (middle of eIF4G (MIM 600495))
            and/or MA3 domains, such as NOM1, function in protein translation.
            These domains include binding sites for members of the EIF4A family
            of ATP-dependent DEAD box RNA helicases (see EIF4A1; MIM 602641)
            (Simmons et al., 2005 [PubMed 15715967]).[supplied by OMIM, Mar
            2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY576779.1, SRR1803612.115891.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000275820.4/ ENSP00000275820.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.3"
     Protein         1..860
                     /product="nucleolar MIF4G domain-containing protein 1
                     isoform 1"
                     /note="nucleolar MIF4G domain-containing protein 1;
                     protein phosphatase 1, regulatory subunit 113; SGD1
                     homolog"
                     /calculated_mol_wt=96127
     Region          1..269
                     /region_name="Necessary for nucleolar localization and for
                     targeting PPP1CA to the nucleolus"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5C9Z4.1)"
     Region          1..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5C9Z4.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5C9Z4.1)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5C9Z4.1)"
     Region          191..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5C9Z4.1)"
     Region          226..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5C9Z4.1)"
     Region          307..310
                     /region_name="Required for efficient binding to PPP1CA and
                     for targeting PPP1CA to the nucleolus"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5C9Z4.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q5C9Z4.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q5C9Z4.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q5C9Z4.1)"
     Region          363..559
                     /region_name="MIF4G"
                     /note="Middle domain of eukaryotic initiation factor 4G
                     (eIF4G); smart00543"
                     /db_xref="CDD:214713"
     Region          364..559
                     /region_name="MIF4G domain"
     Region          655..761
                     /region_name="MA3"
                     /note="MA3 domain; cl02653"
                     /db_xref="CDD:413424"
     Region          655..739
                     /region_name="MA3 domain"
     CDS             1..860
                     /gene="NOM1"
                     /gene_synonym="C7orf3; PPP1R113; SGD1"
                     /coded_by="NM_138400.2:27..2609"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34787.1"
                     /db_xref="GeneID:64434"
                     /db_xref="HGNC:HGNC:13244"
                     /db_xref="MIM:611269"
ORIGIN      
        1 maasrsagea gpggsqgrvv rmkrrggrgp rrgpagggek alkrlklave efvhatsege
       61 apggcegrga pvsfrpggrk srkelrkekr hlrkarrlqr tagpeqgpgl ggrsgaeeas
      121 ghrqdteera rpapsrdpsp prkprpsrvk akataatakt rpsaaataaa rkrallaane
      181 eedreirkle rclglnkrkk kdgsssvpls fardgldyil galesgknsg lydssgeeee
      241 dagqtlpesd lesdsqdese eeeegdveke kkaqeaeaqs edddedteee qgeekekgaq
      301 ekrrgkrvrf aedeeksens sedgditdks lcgsgekyip phvrqaeetv dfkkkeeler
      361 lkkhvkglln rlsepnmasi sgqleelyma hsrkdmndtl tsalmgacvt asampsrlmm
      421 ehvllvsilh htvgievgah fleavvrkfd aiykygsegk ecdnlftvia hlynfhvvqs
      481 llifdilkkl igtftekdie lillmlknvg fslrkddals lkeliteaqt kasgagsefq
      541 dqtrirfmle tmlalknndm rkipgydpep veklrklqra lvrnagsgse tqlrvswdsv
      601 lsaeqtgrww ivgsawsgap midnshhthl qkqlvgtvss kilelarkqr mntdirrnif
      661 ctimtsedfl dafekllklg lkdqqereii hvlmdcclqe ktynpfyafl askfceyerr
      721 fqmtfqfsiw dkfrdlenlp atnfsnlvhl vahllktksl slsilkvvef seldkprvrf
      781 lrkvlsillm etevedlsli ftrvsdnpkl gvlreglklf ishfllknaq ahrsadeanv
      841 lrekadlatk clqgkaslrm
//
LOCUS       NP_001347136             566 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 30 isoform a [Mus musculus].
ACCESSION   NP_001347136 XP_017177623
VERSION     NP_001347136.1
DBSOURCE    REFSEQ: accession NM_001360207.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Laudermilk,L.T., Tovar,A., Homstad,A.K., Thomas,J.M.,
            McFadden,K.M., Tune,M.K., Cowley,D.O., Mock,J.R., Ideraabdullah,F.
            and Kelada,S.N.P.
  TITLE     Baseline and innate immune response characterization of a Zfp30
            knockout mouse strain
  JOURNAL   Mamm Genome 31 (7-8), 205-214 (2020)
   PUBMED   32860515
  REMARK    GeneRIF: Baseline and innate immune response characterization of a
            Zfp30 knockout mouse strain.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Chen,W., Schwalie,P.C., Pankevich,E.V., Gubelmann,C., Raghav,S.K.,
            Dainese,R., Cassano,M., Imbeault,M., Jang,S.M., Russeil,J.,
            Delessa,T., Duc,J., Trono,D., Wolfrum,C. and Deplancke,B.
  TITLE     ZFP30 promotes adipogenesis through the KAP1-mediated activation of
            a retrotransposon-derived Pparg2 enhancer
  JOURNAL   Nat Commun 10 (1), 1809 (2019)
   PUBMED   31000713
  REMARK    GeneRIF: Using murine and human in vitro and in vivo models, study
            demonstrated that ZFP30 promotes adipogenesis by directly targeting
            and activating a retrotransposon-derived Pparg2 enhancer. Through
            mechanistic studies, study further show that ZFP30 recruits the
            co-regulator KAP1, which acts as a ZFP30 co-activator in this
            adipogenic context.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Laudermilk,L.T., Thomas,J.M. and Kelada,S.N.
  TITLE     Differential Regulation of Zfp30 Expression in Murine Airway
            Epithelia Through Altered Binding of ZFP148 to rs51434084
  JOURNAL   G3 (Bethesda) 8 (2), 687-693 (2018)
   PUBMED   29242385
  REMARK    GeneRIF: Data indicate zinc finger protein 148 (ZFP148) as a
            transcription factor that differentially binds to the zinc finger
            protein 30 protein (Zfp30) promoter region harboring rs51434084.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Rutledge,H., Aylor,D.L., Carpenter,D.E., Peck,B.C., Chines,P.,
            Ostrowski,L.E., Chesler,E.J., Churchill,G.A., de Villena,F.P. and
            Kelada,S.N.
  TITLE     Genetic regulation of Zfp30, CXCL1, and neutrophilic inflammation
            in murine lung
  JOURNAL   Genetics 198 (2), 735-745 (2014)
   PUBMED   25114278
  REMARK    GeneRIF: Zfp30 is expressed in airway epithelia in the normal mouse
            lung and Zfp30 expression in vitro affects CXCL1 responses to an
            immune stimulus.
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Denny,P. and Ashworth,A.
  TITLE     Zfp30, a KRAB domain containing zinc finger protein gene, maps to
            mouse chromosome 7
  JOURNAL   Mamm Genome 5 (10), 643-645 (1994)
   PUBMED   7849402
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Ashworth,A. and Denny,P.
  TITLE     Zinc finger protein genes in the mouse genome
  JOURNAL   Mamm Genome 1 (3), 196-200 (1991)
   PUBMED   1797234
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC156934.1.
            
            On Jan 30, 2018 this sequence version replaced XP_017177623.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.281813.1,
                                           SRR7652917.682223.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 17.26 cM"
     Protein         1..566
                     /product="zinc finger protein 30 isoform a"
                     /calculated_mol_wt=66130
     Region          39..100
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          196..556
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          207..227
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          235..255
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          263..283
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(268,270,272,274..275,278..279,282,296,298,302..303,
                     306..307,310,324,326,328,330..331,334..335,338)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          291..311
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          319..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          347..367
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          375..395
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(380,382,384,386..387,390..391,394,408,410,414..415,
                     418..419,422,436,438,440,442..443,446..447,450)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          403..423
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          431..451
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          459..479
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          487..507
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(492,494,496,498..499,502..503,506,520,522,526..527,
                     530..531,534,548,550,552,554..555,558..559,562)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          515..535
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          543..563
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..566
                     /gene="Zfp30"
                     /gene_synonym="2610306P15Rik; Zfp-30"
                     /coded_by="NM_001360207.1:956..2656"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:22693"
                     /db_xref="MGI:MGI:99178"
ORIGIN      
        1 maapspssss lcerlhqdmi leeeqasscd sgimahstvm frdvavgfsq eeweclsaye
       61 rdlyrdvmle nyshlvslag csiskpdvit lleqgkepwm ivraekrrws rdlesryssn
      121 gllpekntye inlspweimg riqrrgpeds llgkdfeyki yeeqenshrv yfrhviktts
      181 gkrpryrkrt pvslyqktpn gekpyecgec gkafkvrqql tfhqrihtge kpyeckecgk
      241 afrqcahlsr hqrihasdkl yeckkcakif tcssdlrghq rshvgekpyd ckecgkafrv
      301 rgqlmlhqri htgekpyact ecgksfrqva hltrhqrlns gssrheckec graflcstgl
      361 rlhhklhtge kpydckecgk afrvrqqltl herihtgekp fdckecgktf srgyhltlhq
      421 rihtgekpye ckecrkffrr yselishqgi higekpydck ecgkafrlfs qltqhqsihf
      481 gekpykcmec ektfrllsql tqhqsihtge kpydckecgk afrlhssliq hqrihsgekp
      541 ykcteckkaf rqhshltyhq rihknl
//
LOCUS       NP_004252                165 aa            linear   PRI 27-APR-2025
DEFINITION  selenoprotein F isoform 1 precursor [Homo sapiens].
ACCESSION   NP_004252
VERSION     NP_004252.2
DBSOURCE    REFSEQ: accession NM_004261.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Flowers,B., Bochnacka,O., Poles,A., Diamond,A.M. and Kastrati,I.
  TITLE     Distinct Roles of SELENOF in Different Human Cancers
  JOURNAL   Biomolecules 13 (3), 486 (2023)
   PUBMED   36979420
  REMARK    GeneRIF: Distinct Roles of SELENOF in Different Human Cancers.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Bera,S. and Diamond,A.M.
  TITLE     Role of SELENBP1 and SELENOF in prostate cancer bioenergetics
  JOURNAL   Arch Biochem Biophys 732, 109451 (2022)
   PUBMED   36334799
  REMARK    GeneRIF: Role of SELENBP1 and SELENOF in prostate cancer
            bioenergetics.
            Review article
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Zhao,Z., Mousa,R. and Metanis,N.
  TITLE     One-Pot Chemical Protein Synthesis Utilizing Fmoc-Masked
            Selenazolidine to Address the Redox Functionality of Human
            Selenoprotein F
  JOURNAL   Chemistry 28 (16), e202200279 (2022)
   PUBMED   35112407
  REMARK    GeneRIF: One-Pot Chemical Protein Synthesis Utilizing Fmoc-Masked
            Selenazolidine to Address the Redox Functionality of Human
            Selenoprotein F.
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Zigrossi,A., Hong,L.K., Ekyalongo,R.C., Cruz-Alvarez,C.,
            Gornick,E., Diamond,A.M. and Kastrati,I.
  TITLE     SELENOF is a new tumor suppressor in breast cancer
  JOURNAL   Oncogene 41 (9), 1263-1268 (2022)
   PUBMED   35082382
  REMARK    GeneRIF: SELENOF is a new tumor suppressor in breast cancer.
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Wu,H.J., Lin,C., Zha,Y.Y., Yang,J.G., Zhang,M.C., Zhang,X.Y.,
            Liang,X., Fu,M. and Wu,M.
  TITLE     [Redox reactions of Sep15 and its relationship with tumor
            development]
  JOURNAL   Ai Zheng 22 (2), 119-122 (2003)
   PUBMED   12600282
  REMARK    GeneRIF: Studies in mouse show that Sep15 may have redox function.
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Kumaraswamy,E., Korotkov,K.V., Diamond,A.M., Gladyshev,V.N. and
            Hatfield,D.L.
  TITLE     Genetic and functional analysis of mammalian Sep15 selenoprotein
  JOURNAL   Methods Enzymol 347, 187-197 (2002)
   PUBMED   11898406
  REMARK    GeneRIF: Genetic and functional analysis of mammalian Sep15
            selenoprotein.
REFERENCE   8  (residues 1 to 165)
  AUTHORS   Korotkov,K.V., Kumaraswamy,E., Zhou,Y., Hatfield,D.L. and
            Gladyshev,V.N.
  TITLE     Association between the 15-kDa selenoprotein and
            UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic
            reticulum of mammalian cells
  JOURNAL   J Biol Chem 276 (18), 15330-15336 (2001)
   PUBMED   11278576
REFERENCE   9  (residues 1 to 165)
  AUTHORS   Kumaraswamy,E., Malykh,A., Korotkov,K.V., Kozyavkin,S., Hu,Y.,
            Kwon,S.Y., Moustafa,M.E., Carlson,B.A., Berry,M.J., Lee,B.J.,
            Hatfield,D.L., Diamond,A.M. and Gladyshev,V.N.
  TITLE     Structure-expression relationships of the 15-kDa selenoprotein
            gene. Possible role of the protein in cancer etiology
  JOURNAL   J Biol Chem 275 (45), 35540-35547 (2000)
   PUBMED   10945981
REFERENCE   10 (residues 1 to 165)
  AUTHORS   Gladyshev,V.N., Jeang,K.T., Wootton,J.C. and Hatfield,D.L.
  TITLE     A new human selenium-containing protein. Purification,
            characterization, and cDNA sequence
  JOURNAL   J Biol Chem 273 (15), 8910-8915 (1998)
   PUBMED   9535873
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU941543.1, BC016359.1 and
            AK225640.1.
            
            On Feb 23, 2004 this sequence version replaced NP_004252.1.
            
            Summary: The protein encoded by this gene belongs to the
            SEP15/selenoprotein M family. The exact function of this protein is
            not known; however, it has been found to associate with
            UDP-glucose:glycoprotein glucosyltransferase (UGTR), an endoplasmic
            reticulum(ER)-resident protein, which is involved in the quality
            control of protein folding. The association with UGTR retains this
            protein in the ER, where it may play a role in protein folding. It
            has also been suggested to have a role in cancer etiology. This
            protein is a selenoprotein, containing the rare amino acid
            selenocysteine (Sec). Sec is encoded by the UGA codon, which
            normally signals translation termination. The 3' UTRs of
            selenoprotein mRNAs contain a conserved stem-loop structure,
            designated the Sec insertion sequence (SECIS) element, that is
            necessary for the recognition of UGA as a Sec codon, rather than as
            a stop signal. Alternatively spliced transcript variants have been
            found for this gene. [provided by RefSeq, Nov 2016].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.84236.1,
                                           SRR3476690.1166565.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match              :: ENST00000331835.10/
                                               ENSP00000328729.6
            protein contains selenocysteine :: PMID: 9535873, 10945981
            RefSeq Select criteria          :: based on conservation,
                                               expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.3"
     Protein         1..165
                     /product="selenoprotein F isoform 1 precursor"
                     /note="15 kDa selenoprotein"
                     /calculated_mol_wt=15081
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3029
     Region          88..163
                     /region_name="Sep15_SelM"
                     /note="Sep15/SelM redox domain; pfam08806"
                     /db_xref="CDD:462607"
     Site            96
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..165
                     /gene="SELENOF"
                     /gene_synonym="SEP15"
                     /coded_by="NM_004261.5:16..513"
                     /note="UGA stop codon recoded as selenocysteine; isoform 1
                     precursor is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS76178.1"
                     /db_xref="GeneID:9403"
                     /db_xref="HGNC:HGNC:17705"
                     /db_xref="MIM:606254"
ORIGIN      
        1 mvamaagpsg clvpafglrl llatvlqavs afgaefssea crelgfssnl lcsscdllgq
       61 fnllqldpdc rgccqeeaqf etkklyagai levcguklgr fpqvqafvrs dkpklfrglq
      121 ikyvrgsdpv lkllddngni aeelsilkwn tdsveeflse kleri
//
LOCUS       NP_003950               1068 aa            linear   PRI 27-APR-2025
DEFINITION  huntingtin-interacting protein 1-related protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_003950 XP_290592
VERSION     NP_003950.1
DBSOURCE    REFSEQ: accession NM_003959.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Zhu,S., Xu,H., Chen,R., Shen,Q., Yang,D., Peng,H., Tong,J. and
            Fu,Q.
  TITLE     DNA methylation and miR-92a-3p-mediated repression of HIP1R
            promotes pancreatic cancer progression by activating the PI3K/AKT
            pathway
  JOURNAL   J Cell Mol Med 27 (6), 788-802 (2023)
   PUBMED   36811277
  REMARK    GeneRIF: DNA methylation and miR-92a-3p-mediated repression of
            HIP1R promotes pancreatic cancer progression by activating the
            PI3K/AKT pathway.
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Yang,N., Liang,Y., Yang,P. and Jiang,L.
  TITLE     Flurbiprofen inhibits cell proliferation in thyroid cancer through
            interrupting HIP1R-induced endocytosis of PTEN
  JOURNAL   Eur J Med Res 27 (1), 29 (2022)
   PUBMED   35209947
  REMARK    GeneRIF: Flurbiprofen inhibits cell proliferation in thyroid cancer
            through interrupting HIP1R-induced endocytosis of PTEN.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Zhu,J., Wang,X., Guan,H., Xiao,Q., Wu,Z., Shi,J., Zhang,F., Gao,P.,
            Song,Y. and Wang,Z.
  TITLE     HIP1R acts as a tumor suppressor in gastric cancer by promoting
            cancer cell apoptosis and inhibiting migration and invasion through
            modulating Akt
  JOURNAL   J Clin Lab Anal 34 (9), e23425 (2020)
   PUBMED   32548851
  REMARK    GeneRIF: HIP1R acts as a tumor suppressor in gastric cancer by
            promoting cancer cell apoptosis and inhibiting migration and
            invasion through modulating Akt.
REFERENCE   4  (residues 1 to 1068)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1068)
  AUTHORS   Biancospino,M., Buel,G.R., Nino,C.A., Maspero,E., Scotto di
            Perrotolo,R., Raimondi,A., Redlingshofer,L., Weber,J.,
            Brodsky,F.M., Walters,K.J. and Polo,S.
  TITLE     Clathrin light chain A drives selective myosin VI recruitment to
            clathrin-coated pits under membrane tension
  JOURNAL   Nat Commun 10 (1), 4974 (2019)
   PUBMED   31672988
  REMARK    GeneRIF: There is coordinated action of myosin VI and CLCa at the
            apical surface where these proteins are essential for fission of
            clathrin-coated pits. Myosin VI and Huntingtin-interacting protein
            1-related protein (Hip1R) are mutually exclusive interactors with
            CLCa, and suggest a model for the sequential function of myosin VI
            and Hip1R in actin-mediated clathrin-coated vesicle budding.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1068)
  AUTHORS   Okano,A., Usuda,N., Furihata,K., Nakayama,K., Bao Tian,Q.,
            Okamoto,T. and Suzuki,T.
  TITLE     Huntingtin-interacting protein-1-related protein of rat (rHIP1R) is
            localized in the postsynaptic regions
  JOURNAL   Brain Res 967 (1-2), 210-225 (2003)
   PUBMED   12650982
REFERENCE   7  (residues 1 to 1068)
  AUTHORS   Legendre-Guillemin,V., Metzler,M., Charbonneau,M., Gan,L.,
            Chopra,V., Philie,J., Hayden,M.R. and McPherson,P.S.
  TITLE     HIP1 and HIP12 display differential binding to F-actin, AP2, and
            clathrin. Identification of a novel interaction with clathrin light
            chain
  JOURNAL   J Biol Chem 277 (22), 19897-19904 (2002)
   PUBMED   11889126
  REMARK    GeneRIF: HIP1 and HIP12 display differential binding to F-actin,
            AP2, and clathrin. Identification of a novel interaction with
            clathrin light chain. (HIP12)
REFERENCE   8  (residues 1 to 1068)
  AUTHORS   Chopra,V.S., Metzler,M., Rasper,D.M., Engqvist-Goldstein,A.E.,
            Singaraja,R., Gan,L., Fichter,K.M., McCutcheon,K., Drubin,D.,
            Nicholson,D.W. and Hayden,M.R.
  TITLE     HIP12 is a non-proapoptotic member of a gene family including HIP1,
            an interacting protein with huntingtin
  JOURNAL   Mamm Genome 11 (11), 1006-1015 (2000)
   PUBMED   11063258
REFERENCE   9  (residues 1 to 1068)
  AUTHORS   Seki,N., Muramatsu,M., Sugano,S., Suzuki,Y., Nakagawara,A.,
            Ohhira,M., Hayashi,A., Hori,T. and Saito,T.
  TITLE     Cloning, expression analysis, and chromosomal localization of
            HIP1R, an isolog of huntingtin interacting protein (HIP1)
  JOURNAL   J Hum Genet 43 (4), 268-271 (1998)
   PUBMED   9852681
REFERENCE   10 (residues 1 to 1068)
  AUTHORS   Puigvert,A.
  TITLE     Caliceal urodynamics
  JOURNAL   Urol Int 30 (4), 282-296 (1975)
   PUBMED   1189126
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN999807.1, AB014555.1, DA779723.1 and AC027290.31.
            
            On Aug 30, 2004 this sequence version replaced XP_290592.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.221395.1, AB014555.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253083.9/ ENSP00000253083.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..1068
                     /product="huntingtin-interacting protein 1-related protein
                     isoform 1"
                     /note="huntingtin interacting protein 12;
                     huntingtin-interacting protein 1-related protein; HIP-12;
                     HIP1-related protein"
                     /calculated_mol_wt=119258
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O75146.2)"
     Region          30..299
                     /region_name="ANTH"
                     /note="ANTH domain; pfam07651"
                     /db_xref="CDD:400137"
     Site            order(37,47,49..50)
                     /site_type="other"
                     /note="PtdIns(4,5)P2-binding site [chemical binding]"
                     /db_xref="CDD:340811"
     Region          <354..>811
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          424..443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75146.2)"
     Region          461..559
                     /region_name="HIP1_clath_bdg"
                     /note="Clathrin-binding domain of Huntingtin-interacting
                     protein 1; pfam16515"
                     /db_xref="CDD:465154"
     Region          529..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75146.2)"
     Region          582..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75146.2)"
     Region          814..1012
                     /region_name="ILWEQ"
                     /note="I/LWEQ domain; smart00307"
                     /db_xref="CDD:214607"
     Region          867..924
                     /region_name="Important for actin binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O75146.2)"
     Region          1016..1060
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75146.2)"
     Site            1017
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75146.2)"
     CDS             1..1068
                     /gene="HIP1R"
                     /gene_synonym="HIP12; HIP3; ILWEQ"
                     /coded_by="NM_003959.3:95..3301"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31922.1"
                     /db_xref="GeneID:9026"
                     /db_xref="HGNC:HGNC:18415"
                     /db_xref="MIM:605613"
ORIGIN      
        1 mnsiknvpar vlsrrpghsl eaereqfdkt qaisiskain tqeapvkekh arriilgthh
       61 ekgaftfwsy aiglplpsss ilswkfchvl hkvlrdghpn vlhdcqryrs nireigdlwg
      121 hlhdrygqlv nvytkllltk isfhlkhpqf paglevtdev lekaagtdvn nifqltvemf
      181 dymdcelkls esvfrqlnta iavsqmssgq crlapliqvi qdcshlyhyt vkllfklhsc
      241 lpadtlqghr drfheqfhsl rnffrrasdm lyfkrliqip rlpegppnfl rasalaehik
      301 pvvvipeeap edeepenlie istgppagep vvvadlfdqt fgppngsvkd drdlqieslk
      361 revemlrsel ekikleaqry iaqlksqvna legeleeqrk qkqkalvdne qlrhelaqlr
      421 aaqlegersq glreeaerka satearynkl kekhselvhv haellrknad takqltvtqq
      481 sqeevarvke qlafqveqvk reselkleek sdqleklkre leakagelar aqealshteq
      541 skselssrld tlsaekdals gavrqreadl laaqslvret eaalsreqqr ssqeqgelqg
      601 rlaeresqeq glrqrlldeq favlrgaaae aagilqdavs klddplhlrc tsspdylvsr
      661 aqealdavst leeghaqylt sladasalva altrfshlaa dtiinggats hlaptdpadr
      721 lidtcrecga ralelmgqlq dqqalrhmqa slvrtplqgi lqlgqelkpk sldvrqeelg
      781 avvdkemaat saaiedavrr iedmmnqarh assgvklevn erilnsctdl mkairllvtt
      841 stslqkeive sgrgaatqqe fyaknsrwte glisaskavg wgatqlveaa dkvvlhtgky
      901 eelivcshei aastaqlvaa skvkankhsp hlsrlqecsr tvneraanvv astksgqeqi
      961 edrdtmdfsg lsliklkkqe metqvrvlel ektleaermr lgelrkqhyv lagasgspge
     1021 evairpstap rsvttkkppl aqkpsvaprq dhqldkkdgi ypaqlvny
//
LOCUS       NP_853553                410 aa            linear   PRI 27-APR-2025
DEFINITION  lipid droplet-regulating VLDL assembly factor AUP1 [Homo sapiens].
ACCESSION   NP_853553
VERSION     NP_853553.1
DBSOURCE    REFSEQ: accession NM_181575.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Zhu,Y., Yang,W., Wang,X. and Chen,M.
  TITLE     AUP1 transcriptionally activated by KDM5B reprograms lipid
            metabolism to promote the malignant progression of cervical cancer
  JOURNAL   Int J Oncol 65 (5) (2024)
   PUBMED   39329209
  REMARK    GeneRIF: AUP1 transcriptionally activated by KDM5B reprograms lipid
            metabolism to promote the malignant progression of cervical cancer.
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Frachon,N., Demaretz,S., Seaayfan,E., Chelbi,L., Bakhos-Douaihy,D.
            and Laghmani,K.
  TITLE     AUP1 Regulates the Endoplasmic Reticulum-Associated Degradation and
            Polyubiquitination of NKCC2
  JOURNAL   Cells 13 (5), 389 (2024)
   PUBMED   38474353
  REMARK    GeneRIF: AUP1 Regulates the Endoplasmic Reticulum-Associated
            Degradation and Polyubiquitination of NKCC2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Chen,C., Zhao,W., Lu,X., Ma,Y., Zhang,P., Wang,Z., Cui,Z. and
            Xia,Q.
  TITLE     AUP1 regulates lipid metabolism and induces lipid accumulation to
            accelerate the progression of renal clear cell carcinoma
  JOURNAL   Cancer Sci 113 (8), 2600-2615 (2022)
   PUBMED   35633317
  REMARK    GeneRIF: AUP1 regulates lipid metabolism and induces lipid
            accumulation to accelerate the progression of renal clear cell
            carcinoma.
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Lohmann,D., Spandl,J., Stevanovic,A., Schoene,M.,
            Philippou-Massier,J. and Thiele,C.
  TITLE     Monoubiquitination of ancient ubiquitous protein 1 promotes lipid
            droplet clustering
  JOURNAL   PLoS One 8 (9), e72453 (2013)
   PUBMED   24039768
  REMARK    GeneRIF: Monoubiquitinated AUP1 on the lipid droplet surface
            specifically induces clustering.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Christianson,J.C., Olzmann,J.A., Shaler,T.A., Sowa,M.E.,
            Bennett,E.J., Richter,C.M., Tyler,R.E., Greenblatt,E.J.,
            Harper,J.W. and Kopito,R.R.
  TITLE     Defining human ERAD networks through an integrative mapping
            strategy
  JOURNAL   Nat Cell Biol 14 (1), 93-105 (2011)
   PUBMED   22119785
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Klemm,E.J., Spooner,E. and Ploegh,H.L.
  TITLE     Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet
            accumulation and endoplasmic reticulum (ER) protein quality control
  JOURNAL   J Biol Chem 286 (43), 37602-37614 (2011)
   PUBMED   21857022
  REMARK    GeneRIF: Dual role of ancient ubiquitous protein 1 (AUP1) in lipid
            droplet accumulation and endoplasmic reticulum (ER) protein quality
            control.
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Spandl,J., Lohmann,D., Kuerschner,L., Moessinger,C. and Thiele,C.
  TITLE     Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and
            binds the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding
            region
  JOURNAL   J Biol Chem 286 (7), 5599-5606 (2011)
   PUBMED   21127063
  REMARK    GeneRIF: The presence of the AUP1-Ube2g2 complex at LDs provides a
            direct molecular link between LDs and the cellular ubiquitination
            machinery.
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Kato,A., Kawamata,N., Tamayose,K., Egashira,M., Miura,R.,
            Fujimura,T., Murayama,K. and Oshimi,K.
  TITLE     Ancient ubiquitous protein 1 binds to the conserved
            membrane-proximal sequence of the cytoplasmic tail of the integrin
            alpha subunits that plays a crucial role in the inside-out
            signaling of alpha IIbbeta 3
  JOURNAL   J Biol Chem 277 (32), 28934-28941 (2002)
   PUBMED   12042322
  REMARK    GeneRIF: binding of Aup1 plays a crucial role in the
            alpha(IIb)beta(3) inside-out signaling
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Jang,W., Weber,J.S., Bashir,R., Bushby,K. and Meisler,M.H.
  TITLE     Aup1, a novel gene on mouse chromosome 6 and human chromosome 2p13
  JOURNAL   Genomics 36 (2), 366-368 (1996)
   PUBMED   8812468
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY078082.1, AF165515.1 and
            AI580873.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded this gene is involved in several
            pathways including quality control of misfolded proteins in the
            endoplasmic reticulum and lipid droplet accumulation. Lipid
            droplets are organelles in the cytoplasm that store neutral lipids
            such as cholesterol esters and trigylycerides to prevent the
            overabundance of free cholesterol and fatty acids in cells, but
            also to act as storage for other metabolic processes, such as
            membrane biogenesis. Reduced expression of this gene results in
            reduced lipid droplet clustering, a function that is dependent on
            ubiquitination of the protein. This protein contains multiple
            domains including a hydrophobic N-terminal domain, an
            acetyltranferase domain, a ubiquitin-binding CUE domain, and a
            UBE2B2-binding domain (G2BR). Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Nov 2014].
            
            Transcript Variant: This variant (2) represents the shortest
            transcript and encodes the functional protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.559767.1,
                                           SRR1163655.500782.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377526.4/ ENSP00000366748.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..410
                     /product="lipid droplet-regulating VLDL assembly factor
                     AUP1"
                     /note="ancient ubiquitous protein 1"
                     /calculated_mol_wt=45656
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9Y679.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y679.2)"
     Region          66..264
                     /region_name="LPLAT"
                     /note="Lysophospholipid acyltransferases (LPLATs) of
                     glycerophospholipid biosynthesis; cl17185"
                     /db_xref="CDD:473073"
     Site            order(96,99,101,124,125..126,163..165)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153244"
     Region          255..295
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y679.2)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y679.2)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9Y679.2)"
     Region          296..340
                     /region_name="CUE_AUP1"
                     /note="CUE domain found in ancient ubiquitous protein 1
                     (AUP1) and similar proteins; cd14420"
                     /db_xref="CDD:270603"
     Region          350..369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y679.2)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9Y679.2)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9Y679.2)"
     CDS             1..410
                     /gene="AUP1"
                     /coded_by="NM_181575.5:78..1310"
                     /db_xref="CCDS:CCDS42702.1"
                     /db_xref="GeneID:550"
                     /db_xref="HGNC:HGNC:891"
                     /db_xref="MIM:602434"
ORIGIN      
        1 melpsgpgpe rlfdshrlpg dcflllvlll yapvgfcllv lrlflgihvf lvscalpdsv
       61 lrrfvvrtmc avlglvarqe dsglrdhsvr vlisnhvtpf dhnivnlltt cstpllnspp
      121 sfvcwsrgfm emngrgelve slkrfcastr lpptplllfp eeeatngreg llrfsswpfs
      181 iqdvvqpltl qvqrplvsvt vsdaswvsel lwslfvpftv yqvrwlrpvh rqlgeaneef
      241 alrvqqlvak elgqtgtrlt padkaehmkr qrhprlrpqs aqssfppspg pspdvqlatl
      301 aqrvkevlph vplgviqrdl aktgcvdlti tnllegavaf mpeditkgtq slptasaskf
      361 pssgpvtpqp taltfakssw arqeslqerk qalyeyarrr fterraqead
//
LOCUS       NP_219489                373 aa            linear   PRI 27-APR-2025
DEFINITION  sorting nexin-21 isoform a [Homo sapiens].
ACCESSION   NP_219489
VERSION     NP_219489.1
DBSOURCE    REFSEQ: accession NM_033421.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Danson,C.M., Pearson,N., Heesom,K.J. and Cullen,P.J.
  TITLE     Sorting nexin-21 is a scaffold for the endosomal recruitment of
            huntingtin
  JOURNAL   J Cell Sci 131 (17) (2018)
   PUBMED   30072438
  REMARK    GeneRIF: The N-terminal extension of SNX21 interacts with
            huntingtin and recruit Htt to an endosomal population.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Zeng,W., Yuan,W., Wang,Y., Jiao,W., Zhu,Y., Huang,C., Li,D., Li,Y.,
            Zhu,C., Wu,X. and Liu,M.
  TITLE     Expression of a novel member of sorting nexin gene family, SNX-L,
            in human liver development
  JOURNAL   Biochem Biophys Res Commun 299 (4), 542-548 (2002)
   PUBMED   12459172
  REMARK    GeneRIF: Data suggest that human sorting nexin-L (SNX-L) may be a
            regulatory gene involved in receptor protein degradation during
            embryonic liver development.
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Xu,Y., Seet,L.F., Hanson,B. and Hong,W.
  TITLE     The Phox homology (PX) domain, a new player in phosphoinositide
            signalling
  JOURNAL   Biochem J 360 (Pt 3), 513-530 (2001)
   PUBMED   11736640
  REMARK    Review article
REFERENCE   8  (residues 1 to 373)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL008726.3 and KF456922.1.
            
            Summary: This gene encodes a member of the sorting nexin family.
            Members of this family contain a phox (PX) domain, which is a
            phosphoinositide binding domain, and are involved in intracellular
            trafficking. This protein does not contain a coiled coil region,
            like some family members. The specific function of this protein has
            not been determined. Multiple transcript variants encoding distinct
            isoforms have been identified for this gene. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.519417.1, AF523834.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000491381.6/ ENSP00000418593.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..373
                     /product="sorting nexin-21 isoform a"
                     /note="sorting nexin L; sorting nexin-21"
                     /calculated_mol_wt=41234
     Region          1..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969T3.1)"
     Region          131..242
                     /region_name="PX_SNX21"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 21; cd07301"
                     /db_xref="CDD:132834"
     Region          164..>353
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(171..173,197..198,212)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132834"
     Site            order(244..245,248..249,251,283,287..288,291..292,
                     294..295,327,330..331,334..335,338)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          244..268
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          281..312
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          326..353
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..373
                     /gene="SNX21"
                     /gene_synonym="C20orf161; dJ337O18.4; PP3993; SNX-L; SNXL"
                     /coded_by="NM_033421.4:122..1243"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13377.1"
                     /db_xref="GeneID:90203"
                     /db_xref="HGNC:HGNC:16154"
                     /db_xref="MIM:619200"
ORIGIN      
        1 mhrgtqegam asrllhrlrh alagdgpgea aaspeaeqfp esseleddda eglssrlsgt
       61 lsftsaedde ddededdeea gpdqlplgdg tsgedaersp ppdgqwgsql larqlqdfwk
      121 ksrntlapqr llfevtsanv vkdppskyvl ytlavigpgp pdcqpaqisr rysdferlhr
      181 nlqrqfrgpm aaisfprkrl rrnftaetia rrsrafeqfl ghlqavpelr hapdlqdffv
      241 lpelrraqsl tctglyreal alwanawqlq aqlgtpsgpd rplltlagla vchqeledpg
      301 earaccekal qllgdkslhp llapfleahv rlswrlgldk rqsearlqal qeagltptpp
      361 pslkellike vld
//
LOCUS       NP_001356737             327 aa            linear   PRI 27-APR-2025
DEFINITION  hematopoietic SH2 domain-containing protein isoform 5 [Homo
            sapiens].
ACCESSION   NP_001356737
VERSION     NP_001356737.1
DBSOURCE    REFSEQ: accession NM_001369808.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Wang,J. and Xiong,Y.
  TITLE     HSH2D contributes to methotrexate resistance in human T-cell acute
            lymphoblastic leukaemia
  JOURNAL   Oncol Rep 44 (5), 2121-2129 (2020)
   PUBMED   33000278
  REMARK    GeneRIF: HSH2D contributes to methotrexate resistance in human
            Tcell acute lymphoblastic leukaemia.
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Huang,J., Burston,J.J., Li,L., Ashraf,S., Mapp,P.I., Bennett,A.J.,
            Ravipati,S., Pousinis,P., Barrett,D.A., Scammell,B.E. and
            Chapman,V.
  TITLE     Targeting the D Series Resolvin Receptor System for the Treatment
            of Osteoarthritis Pain
  JOURNAL   Arthritis Rheumatol 69 (5), 996-1008 (2017)
   PUBMED   27860453
  REMARK    GeneRIF: Both ALX and ChemR23 were present in human synovium and
            medial tibial plateau bone obtained following total knee
            replacement surgery for osteoarthritis.
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Petri,M.H., Thul,S., Ovchinnikova,O. and Back,M.
  TITLE     Differential regulation of monocytic expression of leukotriene and
            lipoxin receptors
  JOURNAL   Prostaglandins Other Lipid Mediat 121 (Pt A), 138-143 (2015)
   PUBMED   26248046
  REMARK    GeneRIF: pro-inflammatory stimuli lead to FPR2/ALX expression while
            LXA4 induces an anti-inflammatory response
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Shapiro,M.J., Chen,Y.Y. and Shapiro,V.S.
  TITLE     The carboxyl-terminal segment of the adaptor protein ALX directs
            its nuclear export during T cell activation
  JOURNAL   J Biol Chem 280 (46), 38242-38246 (2005)
   PUBMED   16169852
  REMARK    GeneRIF: ALX exerts its effect on IL-2 up-regulation in the
            cytoplasm and responds to TCR and CD28 signaling
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Shapiro,M.J., Powell,P., Ndubuizu,A., Nzerem,C. and Shapiro,V.S.
  TITLE     The ALX Src homology 2 domain is both necessary and sufficient to
            inhibit T cell receptor/CD28-mediated up-regulation of RE/AP
  JOURNAL   J Biol Chem 279 (39), 40647-40652 (2004)
   PUBMED   15284240
  REMARK    GeneRIF: the ALX SH2 domain plays a critical role in ALX function
            downstream of CD28
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Greene,T.A., Powell,P., Nzerem,C., Shapiro,M.J. and Shapiro,V.S.
  TITLE     Cloning and characterization of ALX, an adaptor downstream of CD28
  JOURNAL   J Biol Chem 278 (46), 45128-45134 (2003)
   PUBMED   12960172
  REMARK    GeneRIF: ALX is an adaptor involved in T cell activation and
            interleukin-2 (IL-2) promoter activation
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Oda,T., Muramatsu,M.A., Isogai,T., Masuho,Y., Asano,S. and
            Yamashita,T.
  TITLE     HSH2: a novel SH2 domain-containing adapter protein involved in
            tyrosine kinase signaling in hematopoietic cells
  JOURNAL   Biochem Biophys Res Commun 288 (5), 1078-1086 (2001)
   PUBMED   11700021
  REMARK    GeneRIF: involved in tyrosine kinase signaling in hematopoietic
            cells
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008894.9, DA672492.1, KF495722.1 and AC020911.9.
            
            Summary: T-cell activation requires 2 signals: recognition of
            antigen by the T-cell receptor (see TCR; MIM 186880) and a
            costimulatory signal provided primarily by CD28 (MIM 186760) in
            naive T cells. HSH2 is a target of both of these signaling pathways
            (Greene et al., 2003 [PubMed 12960172]).[supplied by OMIM, Mar
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA672492.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..327
                     /product="hematopoietic SH2 domain-containing protein
                     isoform 5"
                     /note="adaptor in lymphocytes of unknown function X;
                     hematopoietic SH2 domain-containing protein"
                     /calculated_mol_wt=36048
     Region          18..102
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(55,83)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198173"
     CDS             1..327
                     /gene="HSH2D"
                     /gene_synonym="ALX; HSH2"
                     /coded_by="NM_001369808.1:118..1101"
                     /note="isoform 5 is encoded by transcript variant 7"
                     /db_xref="GeneID:84941"
                     /db_xref="HGNC:HGNC:24920"
                     /db_xref="MIM:608349"
ORIGIN      
        1 mteagklplp lpprldwdae nllesqplgs flirvshshv gytlsykaqs scchfmvkll
       61 ddgtfmipge kvahtsldal vtfhqqkpie prrelltqpc rqkdpanvdy edlflysnav
      121 aeeaacpvsa peeaspkpvl chqskerkps aemnrittke atsscppksp lgetrqklwr
      181 slkmlpergq rvrqqlkshl atvnlsslld vrrstvisgp gtgkgsqdhs gdptsgdrgy
      241 tdpcvatslk spsqpqapkd rkvptrkaer svscievtpg drswhqmvvr alssqeskpe
      301 hqglaepend qlpeeyqqpp pfapgyc
//
LOCUS       NP_001346955             405 aa            linear   ROD 27-APR-2025
DEFINITION  dematin isoform 1 [Mus musculus].
ACCESSION   NP_001346955 XP_017171327
VERSION     NP_001346955.1
DBSOURCE    REFSEQ: accession NM_001360026.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Huang,S., Reed,C., Ilsley,M., Magor,G., Tallack,M., Landsberg,M.,
            Mitchell,H., Gillinder,K. and Perkins,A.
  TITLE     Mutations in linker-2 of KLF1 impair expression of membrane
            transporters and cytoskeletal proteins causing hemolysis
  JOURNAL   Nat Commun 15 (1), 7019 (2024)
   PUBMED   39147774
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Fritz,D.I., Ding,Y., Merrill-Skoloff,G., Flaumenhaft,R., Hanada,T.
            and Chishti,A.H.
  TITLE     Dematin Regulates Calcium Mobilization, Thrombosis, and Early Akt
            Activation in Platelets
  JOURNAL   Mol Cell Biol 43 (6), 283-299 (2023)
   PUBMED   37216480
  REMARK    GeneRIF: Dematin Regulates Calcium Mobilization, Thrombosis, and
            Early Akt Activation in Platelets.
REFERENCE   3  (residues 1 to 405)
  AUTHORS   O'Neil,S.D., Racz,B., Brown,W.E., Gao,Y., Soderblom,E.J., Yasuda,R.
            and Soderling,S.H.
  TITLE     Action potential-coupled Rho GTPase signaling drives presynaptic
            plasticity
  JOURNAL   Elife 10, e63756 (2021)
   PUBMED   34269176
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Huang,Y.S., Delgadillo,L.F., Cyr,K.H., Kingsley,P.D., An,X.,
            McGrath,K.E., Mohandas,N., Conboy,J.G., Waugh,R.E., Wan,J. and
            Palis,J.
  TITLE     Circulating primitive erythroblasts establish a functional, protein
            4.1R-dependent cytoskeletal network prior to enucleating
  JOURNAL   Sci Rep 7 (1), 5164 (2017)
   PUBMED   28701737
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Lu,Y., Hanada,T., Fujiwara,Y., Nwankwo,J.O., Wieschhaus,A.J.,
            Hartwig,J., Huang,S., Han,J. and Chishti,A.H.
  TITLE     Gene disruption of dematin causes precipitous loss of erythrocyte
            membrane stability and severe hemolytic anemia
  JOURNAL   Blood 128 (1), 93-103 (2016)
   PUBMED   27073223
  REMARK    GeneRIF: results demonstrate that dematin plays a critical role in
            maintaining the fundamental properties of the membrane cytoskeleton
            complex.
REFERENCE   6  (residues 1 to 405)
  AUTHORS   Strehl,S., Glatt,K., Liu,Q.M., Glatt,H. and Lalande,M.
  TITLE     Characterization of two novel protocadherins (PCDH8 and PCDH9)
            localized on human chromosome 13 and mouse chromosome 14
  JOURNAL   Genomics 53 (1), 81-89 (1998)
   PUBMED   9787079
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Cornwall,G.A. and Hsia,N.
  TITLE     ADAM7, a member of the ADAM (a disintegrin and metalloprotease)
            gene family is specifically expressed in the mouse anterior
            pituitary and epididymis
  JOURNAL   Endocrinology 138 (10), 4262-4272 (1997)
   PUBMED   9322939
REFERENCE   8  (residues 1 to 405)
  AUTHORS   Malgaretti,N., Pozzoli,O., Bosetti,A., Corradi,A., Ciarmatori,S.,
            Panigada,M., Bianchi,M.E., Martinez,S. and Consalez,G.G.
  TITLE     Mmot1, a new helix-loop-helix transcription factor gene displaying
            a sharp expression boundary in the embryonic mouse brain
  JOURNAL   J Biol Chem 272 (28), 17632-17639 (1997)
   PUBMED   9211912
REFERENCE   9  (residues 1 to 405)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
REFERENCE   10 (residues 1 to 405)
  AUTHORS   Peters,L.L., Eicher,E.M., Azim,A.C. and Chishti,A.H.
  TITLE     The gene encoding the erythrocyte membrane skeleton protein dematin
            (Epb4.9) maps to mouse chromosome 14
  JOURNAL   Genomics 26 (3), 634-635 (1995)
   PUBMED   7607697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY270342.1, BB873101.1, BY278973.1, CJ070069.1, AK162866.1,
            AK165204.1, BY601680.1 and AI413696.1.
            
            On Jan 25, 2018 this sequence version replaced XP_017171327.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660817.208289.1,
                                           SRR1660821.189315.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 36.32 cM"
     Protein         1..405
                     /product="dematin isoform 1"
                     /note="erythrocyte membrane protein band 4.9; erythrocyte
                     protein band 4.9"
                     /calculated_mol_wt=45337
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV69.1)"
     Region          8..355
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Region          81..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Region          108..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Region          224..308
                     /region_name="Interaction with RASGRF2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087,
                     ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Region          370..405
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     CDS             1..405
                     /gene="Dmtn"
                     /gene_synonym="dematin; Epb4.9; Epb49"
                     /coded_by="NM_001360026.1:411..1628"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS88708.1"
                     /db_xref="GeneID:13829"
                     /db_xref="MGI:MGI:99670"
ORIGIN      
        1 merlqkqplt spgsvsssrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srecslspks tspppspevw aesrtlgiis qastprttgt
      121 prtslphfhh pettrpdsni ykkppiykqr esvggspqsk hliedliies skfpaaqppd
      181 pnqpakietd ywpcppslav vetewrkrka srkgaeeeee eedddseeei kairerqkee
      241 lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl hsgtsksssl psygrttlsr
      301 lqstefspsg seagspglqn gegqrgrmdr gnslpcvleq kiypyemlvv tnkgrtklpp
      361 gvdrmrlerh lsaedfsrvf amspeefgkl alwkrnelkk kaslf
//
LOCUS       NP_116070                452 aa            linear   PRI 27-APR-2025
DEFINITION  tripartite motif-containing protein 51 [Homo sapiens].
ACCESSION   NP_116070
VERSION     NP_116070.2
DBSOURCE    REFSEQ: accession NM_032681.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Han,K., Lou,D.I. and Sawyer,S.L.
  TITLE     Identification of a genomic reservoir for new TRIM genes in primate
            genomes
  JOURNAL   PLoS Genet 7 (12), e1002388 (2011)
   PUBMED   22144910
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC036111.7, DV080293.1 and BC005014.1.
            
            On Oct 21, 2008 this sequence version replaced NP_116070.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1968968, SAMEA2145743
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000449290.6/ ENSP00000395086.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..452
                     /product="tripartite motif-containing protein 51"
                     /note="SPRY domain-containing protein 5; SPRY domain
                     containing 5"
                     /calculated_mol_wt=52154
     Region          9..67
                     /region_name="RING-HC_TRIM43-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51,
                     TRIM64 and similar proteins; cd16603"
                     /db_xref="CDD:438265"
     Region          87..>129
                     /region_name="Bbox2_TRIM43-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51,
                     TRIM64, TRIM77 and similar proteins; cd19783"
                     /db_xref="CDD:380841"
     Region          285..448
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     CDS             1..452
                     /gene="TRIM51"
                     /gene_synonym="SPRYD5; TRIM51A"
                     /coded_by="NM_032681.4:93..1451"
                     /db_xref="GeneID:84767"
                     /db_xref="HGNC:HGNC:19023"
ORIGIN      
        1 mnsgilqvfq raltcpicmn yfldpvtidc ghsfcrpcly lnwqdtavla qcseckkttr
       61 qrnlntdicl knmafiarka slrqflssee qicgmhretk kmfcevdksl lclpcsnsqe
      121 hrnhihcpie waaeerreel lkkmqslwek acenlrnlnm ettrtrcwkd yvslrieair
      181 aeyqkmpafl heeeqhhler lrkegedifq qlneskarme hsrellrgmy edlkqmchka
      241 dvellqafgd ilhryeslll qvsepvnpel sagpitglld slsgfrvdft lqperanshi
      301 flcgdlrsmn vgcdpqddpd itgksecflv wgaqaftsgk yywevhmgds wnwafgvcnn
      361 ywkekrqndk idgeeglfll gcvkedthcs lfttsplvvq yvprptstvg lfldcegrtv
      421 sfvdvdqssl iytipncsfs pplrpifccs hf
//
LOCUS       NP_065749                477 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane and coiled-coil domain protein 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_065749
VERSION     NP_065749.3
DBSOURCE    REFSEQ: accession NM_020698.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Wang,Y.H., Chan,Y.T., Hung,T.H., Hung,J.T., Kuo,M.W., Wang,S.H.,
            Huang,Y., Lin,Y.J., Chen,S.C., Yu,J.C., Wu,J.C., Yu,J. and Yu,A.L.
  TITLE     Transmembrane and coiled-coil domain family 3 (TMCC3) regulates
            breast cancer stem cell and AKT activation
  JOURNAL   Oncogene 40 (16), 2858-2871 (2021)
   PUBMED   33742122
  REMARK    GeneRIF: Transmembrane and coiled-coil domain family 3 (TMCC3)
            regulates breast cancer stem cell and AKT activation.
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Wisesa,S., Yamamoto,Y. and Sakisaka,T.
  TITLE     TMCC3 localizes at the three-way junctions for the proper tubular
            network of the endoplasmic reticulum
  JOURNAL   Biochem J 476 (21), 3241-3260 (2019)
   PUBMED   31696206
  REMARK    GeneRIF: A TMCC3 mutant lacking the N-terminal coiled-coil domain
            abolished localization to tubular network of the endoplasmic
            reticulum, suggesting that TMCC3 localized independently of binding
            to atlastins.
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 477)
  AUTHORS   Sohn,W.J., Kim,J.Y., Kim,D., Park,J.A., Lee,Y. and Kwon,H.J.
  TITLE     Expression and characterization of transmembrane and coiled-coil
            domain family 3
  JOURNAL   BMB Rep 49 (11), 629-634 (2016)
   PUBMED   27697108
  REMARK    GeneRIF: TMCC3 proteins are localized in endoplasmic reticulum
            through transmembrane domains and polymerized with other TMCC3
            protein an 1-3-3 proteins.
REFERENCE   7  (residues 1 to 477)
  AUTHORS   Zhang,C., Kho,Y.S., Wang,Z., Chiang,Y.T., Ng,G.K., Shaw,P.C.,
            Wang,Y. and Qi,R.Z.
  TITLE     Transmembrane and coiled-coil domain family 1 is a novel protein of
            the endoplasmic reticulum
  JOURNAL   PLoS One 9 (1), e85206 (2014)
   PUBMED   24454821
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 477)
  AUTHORS   Davis,O.S., Butcher,L.M., Docherty,S.J., Meaburn,E.L., Curtis,C.J.,
            Simpson,M.A., Schalkwyk,L.C. and Plomin,R.
  TITLE     A three-stage genome-wide association study of general cognitive
            ability: hunting the small effects
  JOURNAL   Behav Genet 40 (6), 759-767 (2010)
   PUBMED   20306291
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026672.44.
            
            On Nov 23, 2018 this sequence version replaced NP_065749.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.221159.1,
                                           SRR1660805.4038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261226.9/ ENSP00000261226.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q22"
     Protein         1..477
                     /product="transmembrane and coiled-coil domain protein 3
                     isoform 1"
                     /note="transmembrane and coiled-coil domains 3;
                     transmembrane and coiled-coil domains protein 3;
                     transmembrane and coiled-coil domain protein 3"
                     /calculated_mol_wt=53654
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R310; propagated from
                     UniProtKB/Swiss-Prot (Q9ULS5.3)"
     Region          64..463
                     /region_name="Tmemb_cc2"
                     /note="Predicted transmembrane and coiled-coil 2 protein;
                     pfam10267"
                     /db_xref="CDD:463036"
     Region          168..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULS5.3)"
     Region          249..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULS5.3)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R310; propagated from
                     UniProtKB/Swiss-Prot (Q9ULS5.3)"
     Site            417..437
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULS5.3)"
     Site            450..470
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULS5.3)"
     CDS             1..477
                     /gene="TMCC3"
                     /coded_by="NM_020698.4:128..1561"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31877.1"
                     /db_xref="GeneID:57458"
                     /db_xref="HGNC:HGNC:29199"
                     /db_xref="MIM:617459"
ORIGIN      
        1 mpgsdtaltv drtysypgrh hrcksrverh dmntlslpln irrggsdtnl nfdvpdgild
       61 fhkvkltads lkqkilkvte qikieqtsrd gnvaeylklv nnadkqqagr ikqvfekknq
      121 ksahsiaqlq kkleqyhrkl reieqngasr sskdiskdhl kdihrslkda hvksrtaphc
      181 messksgmpg vsltppvfvf nksrefanli rnkfgsadni ahlknsleef rpeasarayg
      241 gsativnkpk ygsddecssg tsgsadsngn qsfgaggast ldsqgklavi leelreikdt
      301 qaqlaediea lkvqfkreyg fisqtlqeer yryerledql hdltdlhqhe tanlkqelas
      361 ieekvayqay ersrdiqeal escqtriskl elhqqeqqal qtdtvnakvl lgrcinvila
      421 fmtvilvcvs tiakfvspmm ksrchilgtf favtllaifc knwdhilcai ermiipr
//
LOCUS       NP_005940                 61 aa            linear   PRI 27-APR-2025
DEFINITION  metallothionein-1F isoform 1 [Homo sapiens].
ACCESSION   NP_005940
VERSION     NP_005940.1
DBSOURCE    REFSEQ: accession NM_005949.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Ogasawara,Y., Takeda,Y., Takayama,H., Nishimoto,S., Ichikawa,K.,
            Ueki,M., Suzuki,T. and Ishii,K.
  TITLE     Significance of the rapid increase in GSH levels in the protective
            response to cadmium exposure through phosphorylated Nrf2 signaling
            in Jurkat T-cells
  JOURNAL   Free Radic Biol Med 69, 58-66 (2014)
   PUBMED   24440467
  REMARK    GeneRIF: we found that metallothionein expression induced by Cd
            occurred much later, with the expression seen at least 12h or more
            after the Nrf2-dependent immediate responses were almost completed.
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Miranda Viana Ade,C., Ribeiro,D.C., Florencio,T.N., Santos,V.T.,
            Sousa,A.A. and Aguiar,M.C.
  TITLE     Immunohistochemical expression of metallothionein in pleomorphic
            adenoma of minor salivary glands: a role in the control of
            apoptosis?
  JOURNAL   Acta Histochem 115 (6), 564-568 (2013)
   PUBMED   23332881
  REMARK    GeneRIF: Metallothionein may have a role in the control of
            apoptosis in pleomorphic adenoma.
REFERENCE   3  (residues 1 to 61)
  AUTHORS   Lind,P.A., Zhu,G., Montgomery,G.W., Madden,P.A., Heath,A.C.,
            Martin,N.G. and Slutske,W.S.
  TITLE     Genome-wide association study of a quantitative disordered gambling
            trait
  JOURNAL   Addict Biol 18 (3), 511-522 (2013)
   PUBMED   22780124
REFERENCE   4  (residues 1 to 61)
  AUTHORS   Miao,X., Wang,Y., Sun,J., Sun,W., Tan,Y., Cai,L., Zheng,Y., Su,G.,
            Liu,Q. and Wang,Y.
  TITLE     Zinc protects against diabetes-induced pathogenic changes in the
            aorta: roles of metallothionein and nuclear factor
            (erythroid-derived 2)-like 2
  JOURNAL   Cardiovasc Diabetol 12, 54 (2013)
   PUBMED   23536959
  REMARK    GeneRIF: Aortic protection in diabetes by zinc supplementation is
            associated with upregulation of both metallothionein and Nrf2
            expression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 61)
  AUTHORS   Werynska,B., Pula,B., Muszczynska-Bernhard,B., Gomulkiewicz,A.,
            Piotrowska,A., Prus,R., Podhorska-Okolow,M., Jankowska,R. and
            Dziegiel,P.
  TITLE     Metallothionein 1F and 2A overexpression predicts poor outcome of
            non-small cell lung cancer patients
  JOURNAL   Exp Mol Pathol 94 (1), 301-308 (2013)
   PUBMED   23064051
  REMARK    GeneRIF: findings show 5 MT isoforms were overexpressed in
            non-small cell lung cancer and overexpression of MT-1F and MT-2A
            predicted poor outcome; both isoforms may be involved in
            progression of this cancer type; upregulated MT-1F expression
            associated with larger primary tumor size and higher grade of
            malignanacy
REFERENCE   6  (residues 1 to 61)
  AUTHORS   West,A.K., Stallings,R., Hildebrand,C.E., Chiu,R., Karin,M. and
            Richards,R.I.
  TITLE     Human metallothionein genes: structure of the functional locus at
            16q13
  JOURNAL   Genomics 8 (3), 513-518 (1990)
   PUBMED   2286373
REFERENCE   7  (residues 1 to 61)
  AUTHORS   Foster,R., Jahroudi,N., Varshney,U. and Gedamu,L.
  TITLE     Structure and expression of the human metallothionein-IG gene.
            Differential promoter activity of two linked metallothionein-I
            genes in response to heavy metals
  JOURNAL   J Biol Chem 263 (23), 11528-11535 (1988)
   PUBMED   3403543
REFERENCE   8  (residues 1 to 61)
  AUTHORS   Gedamu,L., Varshney,U., Jahroudi,N., Foster,R. and Shworak,N.W.
  TITLE     Structure and expression of the human metallothionein genes
  JOURNAL   Experientia Suppl 52, 361-372 (1987)
   PUBMED   2444457
REFERENCE   9  (residues 1 to 61)
  AUTHORS   Varshney,U., Jahroudi,N., Foster,R. and Gedamu,L.
  TITLE     Structure, organization, and regulation of human metallothionein IF
            gene: differential and cell-type-specific expression in response to
            heavy metals and glucocorticoids
  JOURNAL   Mol Cell Biol 6 (1), 26-37 (1986)
   PUBMED   3023827
REFERENCE   10 (residues 1 to 61)
  AUTHORS   Schmidt,C.J., Jubier,M.F. and Hamer,D.H.
  TITLE     Structure and expression of two human metallothionein-I isoform
            genes and a related pseudogene
  JOURNAL   J Biol Chem 260 (12), 7731-7737 (1985)
   PUBMED   2581970
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC029453.1 and BQ939879.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript but encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AI814448.1, CA418635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334350.7/ ENSP00000334872.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..61
                     /product="metallothionein-1F isoform 1"
                     /note="metallothionein 1F (functional); MT-1F; MT-IF;
                     metallothionein-IF"
                     /calculated_mol_wt=5955
     Region          1..29
                     /region_name="Beta"
                     /note="propagated from UniProtKB/Swiss-Prot (P04733.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.5;
                     propagated from UniProtKB/Swiss-Prot (P04733.1)"
     Region          4..60
                     /region_name="Metallothio"
                     /note="Metallothionein; pfam00131"
                     /db_xref="CDD:395080"
     Region          30..61
                     /region_name="Alpha"
                     /note="propagated from UniProtKB/Swiss-Prot (P04733.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02795; propagated from
                     UniProtKB/Swiss-Prot (P04733.1)"
     CDS             1..61
                     /gene="MT1F"
                     /gene_synonym="MT1"
                     /coded_by="NM_005949.4:101..286"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32456.1"
                     /db_xref="GeneID:4494"
                     /db_xref="HGNC:HGNC:7398"
                     /db_xref="MIM:156352"
ORIGIN      
        1 mdpncscaag vsctcagsck ckeckctsck ksccsccpvg cskcaqgcvc kgasekcscc
       61 d
//
LOCUS       NP_004421                387 aa            linear   PRI 27-APR-2025
DEFINITION  early growth response protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_004421 XP_944327
VERSION     NP_004421.2
DBSOURCE    REFSEQ: accession NM_004430.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ge,Y., Liu,H., Huang,W., Zhu,H., Zong,D. and He,X.
  TITLE     Immunoinhibitory effects of hypoxia-driven reprogramming of EGR1hi
            and EGR3 positive B cells in the nasopharyngeal carcinoma
            microenvironment
  JOURNAL   Oral Oncol 158, 106999 (2024)
   PUBMED   39197193
  REMARK    GeneRIF: Immunoinhibitory effects of hypoxia-driven reprogramming
            of EGR1[hi] and EGR3 positive B cells in the nasopharyngeal
            carcinoma microenvironment.
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Abudukeyimu,Z., Luo,J., Liu,F., Ma,Y., Li,J., Wang,J. and Li,X.
  TITLE     Early growth response factor 3 may regulate coronary
            atherosclerosis through the NF-kappaB signaling pathway and VEGF
            expression
  JOURNAL   Am J Med Sci 368 (5), 476-484 (2024)
   PUBMED   38992750
  REMARK    GeneRIF: Early growth response factor 3 may regulate coronary
            atherosclerosis through the NF-kappaB signaling pathway and VEGF
            expression.
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Chen,C.H., Chen,Y., Li,Y.N., Zhang,H., Huang,X., Li,Y.Y., Li,Z.Y.,
            Han,J.X., Wu,X.Y., Liu,H.J. and Sun,T.
  TITLE     EGR3 Inhibits Tumor Progression by Inducing Schwann Cell-Like
            Differentiation
  JOURNAL   Adv Sci (Weinh) 11 (34), e2400066 (2024)
   PUBMED   38973154
  REMARK    GeneRIF: EGR3 Inhibits Tumor Progression by Inducing Schwann
            Cell-Like Differentiation.
REFERENCE   4  (residues 1 to 387)
  AUTHORS   da Silva,A.R., Gunawan,F., Boezio,G.L.M., Faure,E., Theron,A.,
            Avierinos,J.F., Lim,S., Jha,S.G., Ramadass,R., Guenther,S.,
            Looso,M., Zaffran,S., Juan,T. and Stainier,D.Y.R.
  TITLE     egr3 is a mechanosensitive transcription factor gene required for
            cardiac valve morphogenesis
  JOURNAL   Sci Adv 10 (20), eadl0633 (2024)
   PUBMED   38748804
  REMARK    GeneRIF: egr3 is a mechanosensitive transcription factor gene
            required for cardiac valve morphogenesis.
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Peng,L., Sun,X., Yi,X., Wang,Z. and Chen,K.
  TITLE     EGR3 reduces podocyte inflammatory damage in obesity related
            glomerulopathy by inhibiting the PRMT1/p-STAT3 pathway
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 49 (3), 349-358 (2024)
   PUBMED   38970508
  REMARK    GeneRIF: EGR3 reduces podocyte inflammatory damage in obesity
            related glomerulopathy by inhibiting the PRMT1/p-STAT3 pathway.
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Yang,Y., Dong,B., Mittelstadt,P.R., Xiao,H. and Ashwell,J.D.
  TITLE     HIV Tat binds Egr proteins and enhances Egr-dependent
            transactivation of the Fas ligand promoter
  JOURNAL   J Biol Chem 277 (22), 19482-19487 (2002)
   PUBMED   11909874
  REMARK    GeneRIF: HIV Tat binds Egr proteins and enhances Egr-dependent
            transactivation of the Fas ligand promoter
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Tourtellotte,W.G. and Milbrandt,J.
  TITLE     Sensory ataxia and muscle spindle agenesis in mice lacking the
            transcription factor Egr3
  JOURNAL   Nat Genet 20 (1), 87-91 (1998)
   PUBMED   9731539
REFERENCE   8  (residues 1 to 387)
  AUTHORS   Morris,M.E., Viswanathan,N., Kuhlman,S., Davis,F.C. and Weitz,C.J.
  TITLE     A screen for genes induced in the suprachiasmatic nucleus by light
  JOURNAL   Science 279 (5356), 1544-1547 (1998)
   PUBMED   9488654
REFERENCE   9  (residues 1 to 387)
  AUTHORS   Mages,H.W., Stamminger,T., Rilke,O., Bravo,R. and Kroczek,R.A.
  TITLE     Expression of PILOT, a putative transcription factor, requires two
            signals and is cyclosporin A sensitive in T cells
  JOURNAL   Int Immunol 5 (1), 63-70 (1993)
   PUBMED   8443122
REFERENCE   10 (residues 1 to 387)
  AUTHORS   Patwardhan,S., Gashler,A., Siegel,M.G., Chang,L.C., Joseph,L.J.,
            Shows,T.B., Le Beau,M.M. and Sukhatme,V.P.
  TITLE     EGR3, a novel member of the Egr family of genes encoding
            immediate-early transcription factors
  JOURNAL   Oncogene 6 (6), 917-928 (1991)
   PUBMED   1906159
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105046.10, S40832.1, X63741.1
            and N66802.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_944327.1, NP_004421.1.
            
            Summary: This gene encodes a transcriptional regulator that belongs
            to the EGR family of C2H2-type zinc-finger proteins. It is an
            immediate-early growth response gene which is induced by mitogenic
            stimulation. The protein encoded by this gene participates in the
            transcriptional regulation of genes in controling biological
            rhythm. It may also play a role in a wide variety of processes
            including muscle development, lymphocyte development, endothelial
            cell growth and migration, and neuronal development. Alternative
            splicing results in multiple transcript variants encoding distinct
            isoforms.[provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: S40832.1, X63741.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317216.3/ ENSP00000318057.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..387
                     /product="early growth response protein 3 isoform 1"
                     /note="zinc finger protein pilot; early growth response
                     protein 3"
                     /calculated_mol_wt=42482
     Region          87..173
                     /region_name="DUF3446"
                     /note="Early growth response N-terminal domain; pfam11928"
                     /db_xref="CDD:463400"
     Region          241..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06889.1)"
     Region          275..299
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          277..299
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(284,286,288,290..291,294..295,298,312,314,318..319,
                     322..323,326,340,342,344,346..347,350..351,354)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          291..316
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          307..327
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          319..344
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          335..355
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          348..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06889.1)"
     CDS             1..387
                     /gene="EGR3"
                     /gene_synonym="EGR-3; PILOT"
                     /coded_by="NM_004430.3:537..1700"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6033.1"
                     /db_xref="GeneID:1960"
                     /db_xref="HGNC:HGNC:3240"
                     /db_xref="MIM:602419"
ORIGIN      
        1 mtgklaeklp vtmssllnql pdnlypeeip salnlfsgss dsvvhynqma tenvmdiglt
       61 nekpnpelsy sgsfqpapgn ktvtylgkfa fdspsnwcqd niislmsagi lgvppasgal
      121 stqtstasmv qppqgdveam ypalppysnc gdlysepvsf hdpqgnpgla yspqdyqsak
      181 paldsnlfpm ipdynlyhhp ndmgsipehk pfqgmdpirv npppitplet ikafkdkqih
      241 pgfgslpqpp ltlkpirprk ypnrpsktpl herphacpae gcdrrfsrsd eltrhlriht
      301 ghkpfqcric mrsfsrsdhl tthirthtge kpfacefcgr kfarsderkr hakihlkqke
      361 kkaekggaps assappvsla pvvttca
//
LOCUS       NP_003789                734 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-catulin isoform a [Homo sapiens].
ACCESSION   NP_003789
VERSION     NP_003789.1
DBSOURCE    REFSEQ: accession NM_003798.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Wu,D., Zhu,J., Yang,F., Li,R., Liu,L., Liu,D., Liu,C., Qu,X.,
            Liu,H., Ji,M., Qin,X., Hua,L. and Xiang,Y.
  TITLE     CTNNAL1 deficiency suppresses CFTR expression in HDM-induced asthma
            mouse model through ROCK1-CAL signaling pathway
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (10), 1618-1629 (2023)
   PUBMED   37715489
  REMARK    GeneRIF: CTNNAL1 deficiency suppresses CFTR expression in
            HDM-induced asthma mouse model through ROCK1-CAL signaling pathway.
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Tung,C.H., Huang,M.F., Liang,C.H., Wu,Y.Y., Wu,J.E., Hsu,C.L.,
            Chen,Y.L. and Hong,T.M.
  TITLE     alpha-Catulin promotes cancer stemness by antagonizing
            WWP1-mediated KLF5 degradation in lung cancer
  JOURNAL   Theranostics 12 (3), 1173-1186 (2022)
   PUBMED   35154481
  REMARK    GeneRIF: alpha-Catulin promotes cancer stemness by antagonizing
            WWP1-mediated KLF5 degradation in lung cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 734)
  AUTHORS   Wang,Y., Jiang,Q., Cai,H., Xu,Z., Wu,W., Gu,B., Li,L. and Cai,W.
  TITLE     Genetic variants in RET, ARHGEF3 and CTNNAL1, and relevant
            interaction networks, contribute to the risk of Hirschsprung
            disease
  JOURNAL   Aging (Albany NY) 12 (5), 4379-4393 (2020)
   PUBMED   32139661
  REMARK    GeneRIF: Genetic variants in RET, ARHGEF3 and CTNNAL1, and relevant
            interaction networks, contribute to the risk of Hirschsprung
            disease.
REFERENCE   6  (residues 1 to 734)
  AUTHORS   Surpili,M.J., Delben,T.M. and Kobarg,J.
  TITLE     Identification of proteins that interact with the central
            coiled-coil region of the human protein kinase NEK1
  JOURNAL   Biochemistry 42 (51), 15369-15376 (2003)
   PUBMED   14690447
REFERENCE   7  (residues 1 to 734)
  AUTHORS   Shieh,Y.S., Chang,L.C., Chiu,K.C., Wu,C.W. and Lee,H.S.
  TITLE     Cadherin and catenin expression in mucoepidermoid carcinoma:
            correlation with histopathologic grade, clinical stage, and patient
            outcome
  JOURNAL   J Oral Pathol Med 32 (5), 297-304 (2003)
   PUBMED   12694354
  REMARK    GeneRIF: Abnormal expression of alpha-catenin was seen in
            mucoepidermoid carcinoma.
REFERENCE   8  (residues 1 to 734)
  AUTHORS   Park,B., Nguyen,N.T., Dutt,P., Merdek,K.D., Bashar,M.,
            Sterpetti,P., Tosolini,A., Testa,J.R. and Toksoz,D.
  TITLE     Association of Lbc Rho guanine nucleotide exchange factor with
            alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports
            serum response factor activation
  JOURNAL   J Biol Chem 277 (47), 45361-45370 (2002)
   PUBMED   12270917
  REMARK    GeneRIF: Results show that alpha-catulin co-expression leads to
            increased Lbc-induced serum response factor activation and may
            modulate Rho pathway signaling in vivo by providing a scaffold for
            the Lbc Rho guanine nucleotide exchange factor.
REFERENCE   9  (residues 1 to 734)
  AUTHORS   Janssens,B., Staes,K. and van Roy,F.
  TITLE     Human alpha-catulin, a novel alpha-catenin-like molecule with
            conserved genomic structure, but deviating alternative splicing
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 341-347 (1999)
   PUBMED   10542337
REFERENCE   10 (residues 1 to 734)
  AUTHORS   Zhang,J.S., Nelson,M., Wang,L., Liu,W., Qian,C.P., Shridhar,V.,
            Urrutia,R. and Smith,D.I.
  TITLE     Identification and chromosomal localization of CTNNAL1, a novel
            protein homologous to alpha-catenin
  JOURNAL   Genomics 54 (1), 149-154 (1998)
   PUBMED   9806841
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK022926.1 and AF030233.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript but encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022926.1, AK223230.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325551.9/ ENSP00000320434.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..734
                     /product="alpha-catulin isoform a"
                     /note="alpha-catulin; alpha2-catulin; catenin alpha-like
                     protein 1; alpha-catenin-related protein; catenin
                     (cadherin-associated protein), alpha-like 1"
                     /calculated_mol_wt=81766
     Region          31..675
                     /region_name="Vinculin"
                     /note="Vinculin family; pfam01044"
                     /db_xref="CDD:460040"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88327; propagated from
                     UniProtKB/Swiss-Prot (Q9UBT7.2)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBT7.2)"
     CDS             1..734
                     /gene="CTNNAL1"
                     /gene_synonym="ACRP; alpha-CATU; CLLP"
                     /coded_by="NM_003798.4:58..2262"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6775.1"
                     /db_xref="GeneID:8727"
                     /db_xref="HGNC:HGNC:2512"
                     /db_xref="MIM:604785"
ORIGIN      
        1 maaspgpagv ggagavygsg ssgfaldsgl eiktrsveqt llplvsqitt linhkdntkk
       61 sdktlqaiqr vgqavnlavg rfvkvgeaia nenwdlkeei niacieakqa getiaaltdi
      121 tnlnhlesdg qitiftdktg vikaarllls svtkvlllad rvvikqiits rnkvlatmer
      181 lekvnsfqef vqifsqfgne mvefahlsgd rqndlkdekk kakmaaarav lekctmmllt
      241 asktclrhpn cesahknkeg vfdrmkvald kvieivtdck pngetdissi siftgikefk
      301 mniealrenl yfqskenlsv tlevilerme dftdsaytsh ehrerilels tqarmelqql
      361 isvwiqaqsk ktksiaeele lsilkishsl nelkkelhst atqlaadllk yhadhvvlka
      421 lkltgvegnl ealaeyackl seqkeqlvet crllrhisgt epleitciha eetfqvtgqq
      481 iisaaetltl hpsskiaken ldvfceawes qisdmstllr eindvfegrr gekygylslp
      541 kpmknnanlk slkpdkpdse eqakiaklgl klglltsdad ceiekwedqe neivqygrnm
      601 ssmayslylf trgegplkts qdlihqlevf aaeglkltss vqafskqlkd ddklmlllei
      661 nkliplchql qtvtktslqn kvflkvdkci tktrsmmall vqllslcykl lkklqmenng
      721 wvsvtnkdtm dskt
//
LOCUS       NP_001349774             548 aa            linear   ROD 27-APR-2025
DEFINITION  diacylglycerol kinase epsilon isoform 2 [Mus musculus].
ACCESSION   NP_001349774
VERSION     NP_001349774.1
DBSOURCE    REFSEQ: accession NM_001362845.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Traczyk,G., Hromada-Judycka,A., Swiatkowska,A., Wisniewska,J.,
            Ciesielska,A. and Kwiatkowska,K.
  TITLE     Diacylglycerol kinase-epsilon is S-palmitoylated on cysteine in the
            cytoplasmic end of its N-terminal transmembrane fragment
  JOURNAL   J Lipid Res 65 (1), 100480 (2024)
   PUBMED   38008259
  REMARK    GeneRIF: Diacylglycerol kinase-epsilon is S-palmitoylated on
            cysteine in the cytoplasmic end of its N-terminal transmembrane
            fragment.
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Nakano,T., Suzuki,A. and Goto,K.
  TITLE     Ablation of diacylglycerol kinase epsilon promotes whitening of
            brown adipose tissue under high fat diet feeding
  JOURNAL   Adv Biol Regul 91, 100994 (2024)
   PUBMED   37875386
  REMARK    GeneRIF: Ablation of diacylglycerol kinase epsilon promotes
            whitening of brown adipose tissue under high fat diet feeding.
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Wang,Z., Zhou,Z., Zhang,Y., Zuo,F., Du,J., Wang,M., Hu,M., Sun,Y.,
            Wang,X., Liu,M., Zhang,Y., Tang,W. and Yi,F.
  TITLE     Diacylglycerol kinase epsilon protects against renal
            ischemia/reperfusion injury in mice through Kruppel-like factor
            15/klotho pathway
  JOURNAL   Ren Fail 44 (1), 902-913 (2022)
   PUBMED   35616094
  REMARK    GeneRIF: Diacylglycerol kinase epsilon protects against renal
            ischemia/reperfusion injury in mice through Kruppel-like factor
            15/klotho pathway.
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Traczyk,G., Swiatkowska,A., Hromada-Judycka,A., Janikiewicz,J. and
            Kwiatkowska,K.
  TITLE     An intact zinc finger motif of the C1B domain is critical for
            stability and activity of diacylglycerol kinase-epsilon
  JOURNAL   Int J Biochem Cell Biol 152, 106295 (2022)
   PUBMED   36113832
  REMARK    GeneRIF: An intact zinc finger motif of the C1B domain is critical
            for stability and activity of diacylglycerol kinase-epsilon.
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Crotty,T., Cai,J., Sakane,F., Taketomi,A., Prescott,S.M. and
            Topham,M.K.
  TITLE     Diacylglycerol kinase delta regulates protein kinase C and
            epidermal growth factor receptor signaling
  JOURNAL   Proc Natl Acad Sci U S A 103 (42), 15485-15490 (2006)
   PUBMED   17021016
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Desai,J., Shannon,M.E., Johnson,M.D., Ruff,D.W., Hughes,L.A.,
            Kerley,M.K., Carpenter,D.A., Johnson,D.K., Rinchik,E.M. and
            Culiat,C.T.
  TITLE     Nell1-deficient mice have reduced expression of extracellular
            matrix proteins causing cranial and vertebral defects
  JOURNAL   Hum Mol Genet 15 (8), 1329-1341 (2006)
   PUBMED   16537572
REFERENCE   8  (residues 1 to 548)
  AUTHORS   Lukiw,W.J., Cui,J.G., Musto,A.E., Musto,B.C. and Bazan,N.G.
  TITLE     Epileptogenesis in diacylglycerol kinase epsilon deficiency
            up-regulates COX-2 and tyrosine hydroxylase in hippocampus
  JOURNAL   Biochem Biophys Res Commun 338 (1), 77-81 (2005)
   PUBMED   16137646
  REMARK    GeneRIF: A regulatory role is suggested for DGK epsilon, COX-2, and
            catecholamine signaling during kindling epileptogenesis.
REFERENCE   9  (residues 1 to 548)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 548)
  AUTHORS   Rodriguez de Turco,E.B., Tang,W., Topham,M.K., Sakane,F.,
            Marcheselli,V.L., Chen,C., Taketomi,A., Prescott,S.M. and
            Bazan,N.G.
  TITLE     Diacylglycerol kinase epsilon regulates seizure susceptibility and
            long-term potentiation through arachidonoyl- inositol lipid
            signaling
  JOURNAL   Proc Natl Acad Sci U S A 98 (8), 4740-4745 (2001)
   PUBMED   11287665
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL646096.8.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.11324.1,
                                           SRR17253011.3559188.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 54.34 cM"
     Protein         1..548
                     /product="diacylglycerol kinase epsilon isoform 2"
                     /EC_number="2.7.1.107"
                     /note="DAG kinase epsilon; diglyceride kinase epsilon"
                     /calculated_mol_wt=61715
     Region          55..108
                     /region_name="C1_DGKepsilon_typeIII_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in type III diacylglycerol kinase, DAG
                     kinase epsilon, and similar proteins; cd20801"
                     /db_xref="CDD:410351"
     Site            order(58,72,75,85,88,93,96,106)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:410351"
     Region          122..186
                     /region_name="C1_DGKepsilon_typeIII_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in type III diacylglycerol kinase, DAG
                     kinase epsilon, and similar proteins; cd20853"
                     /db_xref="CDD:410403"
     Region          218..346
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          366..505
                     /region_name="DAGK_acc"
                     /note="Diacylglycerol kinase accessory domain; cl02440"
                     /db_xref="CDD:470579"
     CDS             1..548
                     /gene="Dgke"
                     /gene_synonym="DAGK6; DGK; DGK-epsilon"
                     /coded_by="NM_001362845.1:364..2010"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:56077"
                     /db_xref="MGI:MGI:1889276"
ORIGIN      
        1 megdqrsgpp aqsllpdghl vlwtlcsvll pvfitlwcsl qrsrrqlhrr difrkskhcw
       61 rdtdlfshpt yccvcaqhil qgafcdccgl rvdegclkkv dkrfpckeim lkndkaadam
      121 phhwirgnvp lcsycvfcrq qcgsqpklcd yrciwcqktv hdecmrgslr sekcdfgefr
      181 nliippsylt sinqmrkdkn tnyeglaskf gkqwtpliil ansrsgtnmg egllgefkil
      241 lnpvqvfdvt ktppikalql ctllpyysvr vlvcggdgtv gwvldaidem kikgqekyip
      301 evavlplgtg ndlsntlgwg tgyageipva qvlrnvmead gikldrwkvq vtnkgyynlr
      361 kpkeftmnny fsvgpdalma lnfhahreka pslfssriln kavylfygtk dclvqeckdl
      421 nkkieleldg ervelpnleg iivlnigywg ggcrlwegmg detyplarhd dglleivgvy
      481 gsfhcaqiql tlkcsmmpmq vdgepwaqgp ctvtithkth almlyfsgeq sdddisspsd
      541 hedvkeae
//
LOCUS       NP_036244                747 aa            linear   PRI 27-APR-2025
DEFINITION  targeting protein for Xklp2 [Homo sapiens].
ACCESSION   NP_036244
VERSION     NP_036244.2
DBSOURCE    REFSEQ: accession NM_012112.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Yu,J., Wang,W., Jiang,Z. and Liu,H.
  TITLE     TPX2 upregulates MMP13 to promote the progression of
            lipopolysaccharide-induced osteoarthritis
  JOURNAL   PeerJ 12, e17032 (2024)
   PUBMED   38770093
  REMARK    GeneRIF: TPX2 upregulates MMP13 to promote the progression of
            lipopolysaccharide-induced osteoarthritis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Wang,L., Zhang,H., Li,Y. and Li,L.
  TITLE     TPX2 influences the regulation of macrophage polarization via the
            NF-kappaB pathway in lung adenocarcinoma
  JOURNAL   Life Sci 340, 122437 (2024)
   PUBMED   38266813
  REMARK    GeneRIF: TPX2 influences the regulation of macrophage polarization
            via the NF-kappaB pathway in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Zhu,M., Wang,X., Zhang,Q., Xie,C., Wang,T., Shen,K., Zhang,L. and
            Zhou,X.
  TITLE     Integrative analysis confirms TPX2 as a novel biomarker for
            clinical implication, tumor microenvironment, and immunotherapy
            response across human solid tumors
  JOURNAL   Aging (Albany NY) 16 (3), 2563-2590 (2024)
   PUBMED   38315450
  REMARK    GeneRIF: Integrative analysis confirms TPX2 as a novel biomarker
            for clinical implication, tumor microenvironment, and immunotherapy
            response across human solid tumors.
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Liu,N., Jiang,Y., Chen,S., Pan,F., Tang,Y. and Tan,X.
  TITLE     miRNA-27b-3p/TPX2 Axis Regulates Clear Cell Renal Cell Carcinoma
            Cell Proliferation, Invasion and Migration
  JOURNAL   Crit Rev Eukaryot Gene Expr 34 (1), 27-39 (2024)
   PUBMED   37824390
  REMARK    GeneRIF: miRNA-27b-3p/TPX2 Axis Regulates Clear Cell Renal Cell
            Carcinoma Cell Proliferation, Invasion and Migration.
REFERENCE   5  (residues 1 to 747)
  AUTHORS   Qi,X., Liu,Y., Peng,Y., Fu,Y., Fu,Y., Yin,L. and Li,X.
  TITLE     UHRF1 promotes spindle assembly and chromosome congression by
            catalyzing EG5 polyubiquitination
  JOURNAL   J Cell Biol 222 (11) (2023)
   PUBMED   37728657
REFERENCE   6  (residues 1 to 747)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   7  (residues 1 to 747)
  AUTHORS   Wittmann,T., Wilm,M., Karsenti,E. and Vernos,I.
  TITLE     TPX2, A novel xenopus MAP involved in spindle pole organization
  JOURNAL   J Cell Biol 149 (7), 1405-1418 (2000)
   PUBMED   10871281
REFERENCE   8  (residues 1 to 747)
  AUTHORS   Manda,R., Kohno,T., Matsuno,Y., Takenoshita,S., Kuwano,H. and
            Yokota,J.
  TITLE     Identification of genes (SPON2 and C20orf2) differentially
            expressed between cancerous and noncancerous lung cells by mRNA
            differential display
  JOURNAL   Genomics 61 (1), 5-14 (1999)
   PUBMED   10512675
REFERENCE   9  (residues 1 to 747)
  AUTHORS   Zhang,Y., Heidebrecht,H., Rott,A., Schlegelberger,B. and
            Parwaresch,R.
  TITLE     Assignment of human proliferation associated p100 gene (C20orf1) to
            human chromosome band 20q11.2 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 84 (3-4), 182-183 (1999)
   PUBMED   10393424
REFERENCE   10 (residues 1 to 747)
  AUTHORS   Heidebrecht,H.J., Buck,F., Steinmann,J., Sprenger,R., Wacker,H.H.
            and Parwaresch,R.
  TITLE     p100: a novel proliferation-associated nuclear protein specifically
            restricted to cell cycle phases S, G2, and M
  JOURNAL   Blood 90 (1), 226-233 (1997)
   PUBMED   9207457
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB960160.1, AF098158.2 and BC020207.1.
            
            On Apr 10, 2002 this sequence version replaced NP_036244.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.191620.1,
                                           SRR1803615.244086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300403.11/ ENSP00000300403.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..747
                     /product="targeting protein for Xklp2"
                     /note="preferentially expressed in colorectal cancer;
                     differentially expressed in lung cells; hepatocellular
                     carcinoma-associated antigen 519; restricted expression
                     proliferation associated protein 100; protein fls353;
                     differentially expressed in cancerous and non-cancerous
                     lung cells 2; TPX2, microtubule-associated, homolog;
                     hepatocellular carcinoma-associated antigen 90; TPX2,
                     microtubule-associated protein homolog; differentially
                     expressed in cancerous and noncancerous lung cells 2"
                     /calculated_mol_wt=85522
     Region          1..68
                     /region_name="Aurora-A_bind"
                     /note="Aurora-A binding; pfam09041"
                     /db_xref="CDD:430383"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Region          110..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:A2APB8; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Region          156..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            305
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Region          367..489
                     /region_name="TPX2_importin"
                     /note="Cell cycle regulated microtubule associated
                     protein; pfam12214"
                     /db_xref="CDD:463495"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            375
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:A2APB8; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW0.2)"
     Region          660..732
                     /region_name="TPX2"
                     /note="Targeting protein for Xklp2 (TPX2) domain;
                     pfam06886"
                     /db_xref="CDD:462029"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULW0.2)"
     CDS             1..747
                     /gene="TPX2"
                     /gene_synonym="C20orf1; C20orf2; DIL-2; DIL2; FLS353;
                     GD:C20orf1; HCA519; HCTP4; p100; REPP86"
                     /coded_by="NM_012112.5:510..2753"
                     /db_xref="CCDS:CCDS13190.1"
                     /db_xref="GeneID:22974"
                     /db_xref="HGNC:HGNC:1249"
                     /db_xref="MIM:605917"
ORIGIN      
        1 msqvkssysy dapsdfinfs slddegdtqn idswfeekan lenkllgkng tgglfqgktp
       61 lrkanlqqai vtplkpvdnt yykeaekenl veqsipsnac ssleveaais rktpaqpqrr
      121 slrlsaqkdl eqkekhhvkm kakrcatpvi ideilpskkm kvsnnkkkpe eegsahqdta
      181 eknasspeka kgrhtvpcmp pakqkflkst eeqeleksmk mqqevvemrk kneefkklal
      241 agigqpvkks vsqvtksvdf hfrtderikq hpknqeeyke vnftselrkh pssparvtkg
      301 ctivkpfnls qgkkrtfdet vstyvplaqq vedfhkrtpn ryhlrskkdd inllpskssv
      361 tkicrdpqtp vlqtkhrara vtckstaele aeeleklqqy kfkareldpr ileggpilpk
      421 kppvkpptep igfdleiekr iqereskkkt edehfefhsr pcptkiledv vgvpekkvlp
      481 itvpkspafa lknrirmptk edeeedepvv ikaqpvphyg vpfkpqipea rtveicpfsf
      541 dsrdkerqlq kekkikelqk gevpkfkalp lphfdtinlp ekkvknvtqi epfcletdrr
      601 galkaqtwkh qleeelrqqk eaacfkarpn tvisqepfvp kkekksvaeg lsgslvqepf
      661 qlatekrake rqelekrmae veaqkaqqle earlqeeeqk keelarlrre lvhkanpirk
      721 yqgleikssd qpltvpvspk fstrfhc
//
LOCUS       NP_005857                223 aa            linear   PRI 27-APR-2025
DEFINITION  sigma non-opioid intracellular receptor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_005857
VERSION     NP_005857.1
DBSOURCE    REFSEQ: accession NM_005866.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Kong,M., Chen,Z., Lin,Z., Yin,P. and Zhao,Q.
  TITLE     SIGMAR1 targets AMPK/ULK1 pathway to inhibit SH-SY5Y cell apoptosis
            by regulating endoplasmic reticulum stress and autophagy
  JOURNAL   Funct Integr Genomics 24 (4), 134 (2024)
   PUBMED   39107544
  REMARK    GeneRIF: SIGMAR1 targets AMPK/ULK1 pathway to inhibit SH-SY5Y cell
            apoptosis by regulating endoplasmic reticulum stress and autophagy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   D'Atri,I., Martin,E.R., Yang,L., Sears,E., Baple,E., Crosby,A.H.,
            Chilton,J.K. and Oguro-Ando,A.
  TITLE     Unraveling the CLCC1 interactome: Impact of the Asp25Glu variant
            and its interaction with SigmaR1 at the Mitochondrial-Associated ER
            Membrane (MAM)
  JOURNAL   Neurosci Lett 830, 137778 (2024)
   PUBMED   38621504
  REMARK    GeneRIF: Unraveling the CLCC1 interactome: Impact of the Asp25Glu
            variant and its interaction with SigmaR1 at the
            Mitochondrial-Associated ER Membrane (MAM).
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Hosszu,A., Toth,A.R., Lakat,T., Stepanova,G., Antal,Z.,
            Wagner,L.J., Szabo,A.J. and Fekete,A.
  TITLE     The Sigma-1 Receptor Is a Novel Target for Improving Cold
            Preservation in Rodent Kidney Transplants
  JOURNAL   Int J Mol Sci 24 (14), 11630 (2023)
   PUBMED   37511389
  REMARK    GeneRIF: The Sigma-1 Receptor Is a Novel Target for Improving Cold
            Preservation in Rodent Kidney Transplants.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Zhao,F., Yang,T., Zhou,L., Li,R., Liu,J., Zhao,J. and Jia,R.
  TITLE     Sig1R activates extracellular matrix-induced bladder cancer cell
            proliferation and angiogenesis by combing beta-integrin
  JOURNAL   Aging (Albany NY) 15 (10), 4182-4201 (2023)
   PUBMED   37199665
  REMARK    GeneRIF: Sig1R activates extracellular matrix-induced bladder
            cancer cell proliferation and angiogenesis by combing
            beta-integrin.
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Couly,S., Yasui,Y. and Su,T.P.
  TITLE     SIGMAR1 Confers Innate Resilience against Neurodegeneration
  JOURNAL   Int J Mol Sci 24 (9), 7767 (2023)
   PUBMED   37175473
  REMARK    GeneRIF: SIGMAR1 Confers Innate Resilience against
            Neurodegeneration.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Dussossoy,D., Carayon,P., Belugou,S., Feraut,D., Bord,A.,
            Goubet,C., Roque,C., Vidal,H., Combes,T., Loison,G. and Casellas,P.
  TITLE     Colocalization of sterol isomerase and sigma(1) receptor at
            endoplasmic reticulum and nuclear envelope level
  JOURNAL   Eur J Biochem 263 (2), 377-386 (1999)
   PUBMED   10406945
REFERENCE   7  (residues 1 to 223)
  AUTHORS   Ganapathy,M.E., Prasad,P.D., Huang,W., Seth,P., Leibach,F.H. and
            Ganapathy,V.
  TITLE     Molecular and ligand-binding characterization of the sigma-receptor
            in the Jurkat human T lymphocyte cell line
  JOURNAL   J Pharmacol Exp Ther 289 (1), 251-260 (1999)
   PUBMED   10087012
REFERENCE   8  (residues 1 to 223)
  AUTHORS   Prasad,P.D., Li,H.W., Fei,Y.J., Ganapathy,M.E., Fujita,T.,
            Plumley,L.H., Yang-Feng,T.L., Leibach,F.H. and Ganapathy,V.
  TITLE     Exon-intron structure, analysis of promoter region, and chromosomal
            localization of the human type 1 sigma receptor gene
  JOURNAL   J Neurochem 70 (2), 443-451 (1998)
   PUBMED   9453537
REFERENCE   9  (residues 1 to 223)
  AUTHORS   Jbilo,O., Vidal,H., Paul,R., De Nys,N., Bensaid,M., Silve,S.,
            Carayon,P., Davi,D., Galiegue,S., Bourrie,B., Guillemot,J.C.,
            Ferrara,P., Loison,G., Maffrand,J.P., Le Fur,G. and Casellas,P.
  TITLE     Purification and characterization of the human SR 31747A-binding
            protein. A nuclear membrane protein related to yeast sterol
            isomerase
  JOURNAL   J Biol Chem 272 (43), 27107-27115 (1997)
   PUBMED   9341151
REFERENCE   10 (residues 1 to 223)
  AUTHORS   Kekuda,R., Prasad,P.D., Fei,Y.J., Leibach,F.H. and Ganapathy,V.
  TITLE     Cloning and functional expression of the human type 1 sigma
            receptor (hSigmaR1)
  JOURNAL   Biochem Biophys Res Commun 229 (2), 553-558 (1996)
   PUBMED   8954936
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK130502.1, AL450283.16 and
            BC007839.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a receptor protein that interacts with a
            variety of psychotomimetic drugs, including cocaine and
            amphetamines. The receptor is believed to play an important role in
            the cellular functions of various tissues associated with the
            endocrine, immune, and nervous systems. As indicated by its
            previous name, opioid receptor sigma 1 (OPRS1), the product of this
            gene was erroneously thought to function as an opioid receptor; it
            is now thought to be a non-opioid receptor. Mutations in this gene
            has been associated with juvenile amyotrophic lateral sclerosis 16.
            Alternative splicing of this gene results in transcript variants
            encoding distinct isoforms. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK130502.1, SRR3476690.394732.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000277010.9/ ENSP00000277010.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..223
                     /product="sigma non-opioid intracellular receptor 1
                     isoform 1"
                     /note="SR31747 binding protein 1; sigma 1-type opioid
                     receptor; aging-associated gene 8 protein"
                     /calculated_mol_wt=24997
     Region          2..8
                     /region_name="Targeting to endoplasmic
                     reticulum-associated lipid droplets.
                     /evidence=ECO:0000250|UniProtKB:O55242"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99720.1)"
     Site            10..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99720.1)"
     Region          25..214
                     /region_name="ERG2_Sigma1R"
                     /note="ERG2 and Sigma1 receptor like protein; pfam04622"
                     /db_xref="CDD:461372"
     Region          99..106
                     /region_name="Important for ligand-binding.
                     /evidence=ECO:0000250|UniProtKB:Q60492"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99720.1)"
     Site            126
                     /site_type="other"
                     /note="Important for ligand binding.
                     /evidence=ECO:0000269|PubMed:11476895; propagated from
                     UniProtKB/Swiss-Prot (Q99720.1)"
     Site            172
                     /site_type="other"
                     /note="Important for ligand binding.
                     /evidence=ECO:0000269|PubMed:11476895; propagated from
                     UniProtKB/Swiss-Prot (Q99720.1)"
     Region          177..223
                     /region_name="C-terminal hydrophobic region.
                     /evidence=ECO:0000269|PubMed:27042935"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99720.1)"
     CDS             1..223
                     /gene="SIGMAR1"
                     /gene_synonym="ALS16; DSMA2; HMNR2; hSigmaR1; OPRS1;
                     SIG-1R; sigma1R; SR-BP; SR-BP1; SRBP"
                     /coded_by="NM_005866.4:91..762"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6562.1"
                     /db_xref="GeneID:10280"
                     /db_xref="HGNC:HGNC:8157"
                     /db_xref="MIM:601978"
ORIGIN      
        1 mqwavgrrwa waalllavaa vltqvvwlwl gtqsfvfqre eiaqlarqya gldhelafsr
       61 livelrrlhp ghvlpdeelq wvfvnaggwm gamcllhasl seyvllfgta lgsrghsgry
      121 waeisdtiis gtfhqwregt tksevfypge tvvhgpgeat avewgpntwm veygrgvips
      181 tlafaladtv fstqdfltlf ytlrsyargl rlelttylfg qdp
//
LOCUS       NP_001355111             386 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein with KRAB and SCAN domains 3 isoform b [Mus
            musculus].
ACCESSION   NP_001355111 XP_006516854
VERSION     NP_001355111.1
DBSOURCE    REFSEQ: accession NM_001368182.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Zhang,T., Zhu,S. and Huang,G.W.
  TITLE     ALKBH5 suppresses autophagic flux via N6-methyladenosine
            demethylation of ZKSCAN3 mRNA in acute pancreatitis
  JOURNAL   World J Gastroenterol 30 (12), 1764-1776 (2024)
   PUBMED   38617741
  REMARK    GeneRIF: ALKBH5 suppresses autophagic flux via N6-methyladenosine
            demethylation of ZKSCAN3 mRNA in acute pancreatitis.
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Ouyang,X., Bakshi,S., Benavides,G.A., Sun,Z., Hernandez-Moreno,G.,
            Collins,H.E., Kane,M.S., Litovsky,S., Young,M.E., Chatham,J.C.,
            Darley-Usmar,V., Wende,A.R. and Zhang,J.
  TITLE     Cardiomyocyte ZKSCAN3 regulates remodeling following
            pressure-overload
  JOURNAL   Physiol Rep 11 (9), e15686 (2023)
   PUBMED   37144628
  REMARK    GeneRIF: Cardiomyocyte ZKSCAN3 regulates remodeling following
            pressure-overload.
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Li,X.M., Wen,J.H., Feng,Z.S., Wu,Y.S., Li,D.Y., Liang,S., Wu,D.,
            Wu,H.L., Li,S.M., Ye,Z.N., Yang,C., Sun,L., Tang,J.X. and Liu,H.F.
  TITLE     Effect of Lacking ZKSCAN3 on Autophagy, Lysosomal Biogenesis and
            Senescence
  JOURNAL   Int J Mol Sci 24 (9), 7786 (2023)
   PUBMED   37175493
  REMARK    GeneRIF: Effect of Lacking ZKSCAN3 on Autophagy, Lysosomal
            Biogenesis and Senescence.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Liu,Z., Li,X., Li,X., Li,Z., Chen,H., Gong,S., Zhang,M., Zhang,Y.,
            Li,Z., Yang,L. and Liu,H.
  TITLE     The kidney-expressed transcription factor ZKSCAN3 is dispensable
            for autophagy transcriptional regulation and AKI progression in
            mouse
  JOURNAL   Mutat Res 825, 111790 (2022)
   PUBMED   35841832
  REMARK    GeneRIF: The kidney-expressed transcription factor ZKSCAN3 is
            dispensable for autophagy transcriptional regulation and AKI
            progression in mouse.
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Wu,X., Ren,Y., Wen,Y., Lu,S., Li,H., Yu,H., Li,W. and Zou,F.
  TITLE     Deacetylation of ZKSCAN3 by SIRT1 induces autophagy and protects
            SN4741 cells against MPP+-induced oxidative stress
  JOURNAL   Free Radic Biol Med 181, 82-97 (2022)
   PUBMED   35124181
  REMARK    GeneRIF: Deacetylation of ZKSCAN3 by SIRT1 induces autophagy and
            protects SN4741 cells against MPP(+)-induced oxidative stress.
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Georgas,K., Rumballe,B., Valerius,M.T., Chiu,H.S.,
            Thiagarajan,R.D., Lesieur,E., Aronow,B.J., Brunskill,E.W.,
            Combes,A.N., Tang,D., Taylor,D., Grimmond,S.M., Potter,S.S.,
            McMahon,A.P. and Little,M.H.
  TITLE     Analysis of early nephron patterning reveals a role for distal RV
            proliferation in fusion to the ureteric tip via a cap
            mesenchyme-derived connecting segment
  JOURNAL   Dev Biol 332 (2), 273-286 (2009)
   PUBMED   19501082
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Yang,L., Zhang,L., Wu,Q. and Boyd,D.D.
  TITLE     Unbiased screening for transcriptional targets of ZKSCAN3
            identifies integrin beta 4 and vascular endothelial growth factor
            as downstream targets
  JOURNAL   J Biol Chem 283 (50), 35295-35304 (2008)
   PUBMED   18940803
  REMARK    GeneRIF: ZKSCAN3 regulates the expression of several genes favoring
            tumor progression including integrin beta 4 and VEGF
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Honer,C., Chen,P., Toth,M.J. and Schumacher,C.
  TITLE     Identification of SCAN dimerization domains in four gene families
  JOURNAL   Biochim Biophys Acta 1517 (3), 441-448 (2001)
   PUBMED   11342224
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Agata,Y., Matsuda,E. and Shimizu,A.
  TITLE     Rapid and efficient cloning of cDNAs encoding Kruppel-like zinc
            finger proteins by degenerate PCR
  JOURNAL   Gene 213 (1-2), 55-64 (1998)
   PUBMED   9630514
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX001068.7, CK627138.1, AK028902.1 and AI132359.1.
            
            On Jan 19, 2019 this sequence version replaced XP_006516854.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.43428.1, CK627138.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN01164134
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 7.78 cM"
     Protein         1..386
                     /product="zinc finger protein with KRAB and SCAN domains 3
                     isoform b"
                     /note="zinc finger protein 307; zinc finger protein 306;
                     SCAN-KRAB-zinc finger gene 1; zinc finger protein with
                     KRAB and SCAN domains 3; SCAN-KRAB-zinc finger protein;
                     zinc finger protein 47 homolog"
                     /calculated_mol_wt=43531
     Region          46..100
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          146..168
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          148..168
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          161..183
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          174..196
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          176..196
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <200..347
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          204..224
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(209,211,213,215..216,219..220,223,237,239,243..244,
                     247..248,251,265,267,269,271..272,275..276,279)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          232..252
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          260..280
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          314..334
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          340..362
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          342..362
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..386
                     /gene="Zkscan3"
                     /gene_synonym="2810435N07Rik; mszf35; Skz1; Zf47; Zfp-47;
                     Zfp306; Zfp307"
                     /coded_by="NM_001368182.1:169..1329"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS88419.1"
                     /db_xref="GeneID:72739"
                     /db_xref="MGI:MGI:1919989"
ORIGIN      
        1 mepvepllkq eslgslpsev rvthvghcge dgvtatrlts elqgllkmed vapvlsprwt
       61 eqdssqmnly kdgmqehsgs lvsldqdmqt kvrdlpraee yrdqkpeqtv cflgedtvpi
      121 ptgaeaseqe gklqaaqksa tgtrrfycre cgksfaqssg lskhkrihtg lkpyeceecg
      181 kafigssali ihqrvhtgek pyeceecgka fshssdlikh qrthtgekpy ecddcgktft
      241 qscsllehhr ihtgekpyqc nmcpkafrrs shllrhqrth tgdkdffvpe pywesqsrve
      301 shwenietpv syqcndcers fsritslieh qkvhtgekpf ecqtcgkgft rpsyliqhqr
      361 rhtgkktsvt vtpavhsevg vqlsln
//
LOCUS       NP_005012                875 aa            linear   PRI 27-APR-2025
DEFINITION  ectonucleotide pyrophosphatase/phosphodiesterase family member 3
            [Homo sapiens].
ACCESSION   NP_005012
VERSION     NP_005012.2
DBSOURCE    REFSEQ: accession NM_005021.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Qin,Y., Li,Y., Hao,Y., Li,Y. and Kang,S.
  TITLE     Hypomethylation of the ENPP3 promoter region contributes to the
            occurrence and development of ovarian endometriosis via the
            AKT/mTOR/4EBP1 signaling pathway
  JOURNAL   Biomol Biomed 24 (4), 848-856 (2023)
   PUBMED   38149831
  REMARK    GeneRIF: Hypomethylation of the ENPP3 promoter region contributes
            to the occurrence and development of ovarian endometriosis via the
            AKT/mTOR/4EBP1 signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Sadovnik,I., Ivanov,D., Smiljkovic,D., Stefanzl,G.,
            Degenfeld-Schonburg,L., Herndlhofer,S., Eisenwort,G.,
            Hauswirth,A.W., Sliwa,T., Keil,F., Sperr,W.R. and Valent,P.
  TITLE     Identification of CD203c as a New Basophil-Specific Flow-Marker in
            Ph+ Chronic Myeloid Leukemia
  JOURNAL   Cells 12 (1), 3 (2022)
   PUBMED   36611797
  REMARK    GeneRIF: Identification of CD203c as a New Basophil-Specific
            Flow-Marker in Ph[+] Chronic Myeloid Leukemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 875)
  AUTHORS   Qi,Z., Xue,Q., Wang,H., Cao,B., Su,Y., Xing,Q. and Yang,J.J.
  TITLE     Serum CD203c+ Extracellular Vesicle Serves as a Novel Diagnostic
            and Prognostic Biomarker for Succinylated Gelatin Induced
            Perioperative Hypersensitive Reaction
  JOURNAL   Front Immunol 12, 732209 (2021)
   PUBMED   34650557
  REMARK    GeneRIF: Serum CD203c+ Extracellular Vesicle Serves as a Novel
            Diagnostic and Prognostic Biomarker for Succinylated Gelatin
            Induced Perioperative Hypersensitive Reaction.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 875)
  AUTHORS   Imamura,S., Washio,K., Mizuno,M., Oda,Y., Fukunaga,A. and
            Nishigori,C.
  TITLE     Activated steady status and distinctive FcepsilonRI-mediated
            responsiveness in basophils of atopic dermatitis
  JOURNAL   Allergol Int 70 (3), 327-334 (2021)
   PUBMED   33674191
  REMARK    GeneRIF: Activated steady status and distinctive
            FcepsilonRI-mediated responsiveness in basophils of atopic
            dermatitis.
REFERENCE   5  (residues 1 to 875)
  AUTHORS   Heneberg,P., Riegerova,K., Rihova,A., Simcikova,D. and Kucera,P.
  TITLE     Updates on the surface antigens of basophils: CD16 on basophils of
            patients with respiratory or insect venom allergy and the rejection
            of CD203c and CD63 externalization decoupling by
            bisindolylmaleimides
  JOURNAL   Clin Exp Allergy 49 (1), 54-67 (2019)
   PUBMED   30288810
  REMARK    GeneRIF: Updates on the surface antigens of basophils: CD16 on
            basophils of patients with respiratory or insect venom allergy and
            the rejection of CD203c and CD63 externalization decoupling by
            bisindolylmaleimides.
REFERENCE   6  (residues 1 to 875)
  AUTHORS   Vollmayer,P., Clair,T., Goding,J.W., Sano,K., Servos,J. and
            Zimmermann,H.
  TITLE     Hydrolysis of diadenosine polyphosphates by nucleotide
            pyrophosphatases/phosphodiesterases
  JOURNAL   Eur J Biochem 270 (14), 2971-2978 (2003)
   PUBMED   12846830
REFERENCE   7  (residues 1 to 875)
  AUTHORS   Buhring,H.J., Seiffert,M., Giesert,C., Marxer,A., Kanz,L.,
            Valent,P. and Sano,K.
  TITLE     The basophil activation marker defined by antibody 97A6 is
            identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3
  JOURNAL   Blood 97 (10), 3303-3305 (2001)
   PUBMED   11342463
REFERENCE   8  (residues 1 to 875)
  AUTHORS   Andoh,K., Piao,J.H., Terashima,K., Nakamura,H. and Sano,K.
  TITLE     Genomic structure and promoter analysis of the
            ecto-phosphodiesterase I gene (PDNP3) expressed in glial cells
  JOURNAL   Biochim Biophys Acta 1446 (3), 213-224 (1999)
   PUBMED   10524196
REFERENCE   9  (residues 1 to 875)
  AUTHORS   Johnson,K., Vaingankar,S., Chen,Y., Moffa,A., Goldring,M.B.,
            Sano,K., Jin-Hua,P., Sali,A., Goding,J. and Terkeltaub,R.
  TITLE     Differential mechanisms of inorganic pyrophosphate production by
            plasma cell membrane glycoprotein-1 and B10 in chondrocytes
  JOURNAL   Arthritis Rheum 42 (9), 1986-1997 (1999)
   PUBMED   10513816
REFERENCE   10 (residues 1 to 875)
  AUTHORS   Jin-Hua,P., Goding,J.W., Nakamura,H. and Sano,K.
  TITLE     Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3),
            a new member of the human phosphodiesterase I genes
  JOURNAL   Genomics 45 (2), 412-415 (1997)
   PUBMED   9344668
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY106781.1, AL121575.24,
            EF560735.1 and AK024899.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 4, 2006 this sequence version replaced NP_005012.1.
            
            Summary: The protein encoded by this gene belongs to a series of
            ectoenzymes that are involved in hydrolysis of extracellular
            nucleotides. These ectoenzymes possess ATPase and ATP
            pyrophosphatase activities and are type II transmembrane proteins.
            Expression of the related rat mRNA has been found in a subset of
            immature glial cells and in the alimentary tract. The corresponding
            rat protein has been detected in the pancreas, small intestine,
            colon, and liver. The human mRNA is expressed in glioma cells,
            prostate, and uterus. Expression of the human protein has been
            detected in uterus, basophils, and mast cells. Two transcript
            variants, one protein coding and the other non-protein coding, have
            been found for this gene. [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) represents the longer,
            protein-coding transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK024899.1, AK292903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357639.8/ ENSP00000350265.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.2"
     Protein         1..875
                     /product="ectonucleotide pyrophosphatase/phosphodiesterase
                     family member 3"
                     /EC_number="3.1.4.1"
                     /EC_number="3.6.1.9"
                     /note="phosphodiesterase-I beta; gp130RB13-6;
                     phosphodiesterase I/nucleotide pyrophosphatase 3;
                     dJ914N13.3 (phosphodiesterase I/nucleotide pyrophosphatase
                     3); NPPase; dJ1005H11.3 (phosphodiesterase I/nucleotide
                     pyrophosphatase 3); nucleotide diphosphatase; alkaline
                     phosphodiesterase I; dinucleoside polyphosphatase"
                     /calculated_mol_wt=99994
     Site            12..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14638.2)"
     Region          51..93
                     /region_name="SO"
                     /note="Somatomedin B -like domains; smart00201"
                     /db_xref="CDD:197571"
     Region          78..80
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O14638.2)"
     Region          94..137
                     /region_name="SO"
                     /note="Somatomedin B -like domains; smart00201"
                     /db_xref="CDD:197571"
     Region          159..525
                     /region_name="Enpp"
                     /note="Ectonucleotide pyrophosphatase/phosphodiesterase,
                     also called autotaxin; cd16018"
                     /db_xref="CDD:293742"
     Region          160..545
                     /region_name="Phosphodiesterase.
                     /evidence=ECO:0000305|PubMed:29717535"
                     /note="propagated from UniProtKB/Swiss-Prot (O14638.2)"
     Site            order(167,204..205,226,325,329,372..373,483)
                     /site_type="active"
                     /db_xref="CDD:293742"
     Site            order(167,204..205,226,325,329,373,483)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293742"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            279
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            290
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            426
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            508..510
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293742"
     Site            533
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Region          582..875
                     /region_name="Nuclease.
                     /evidence=ECO:0000305|PubMed:29717535"
                     /note="propagated from UniProtKB/Swiss-Prot (O14638.2)"
     Site            582
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C01; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            594
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C01; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Region          627..857
                     /region_name="NUC"
                     /note="DNA/RNA non-specific endonuclease; smart00477"
                     /db_xref="CDD:214683"
     Site            687
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:29717535; propagated from
                     UniProtKB/Swiss-Prot (O14638.2)"
     Site            order(689..690,692,729,733)
                     /site_type="active"
                     /db_xref="CDD:238043"
     Site            order(689..690,733)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238043"
     Site            699
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     Site            789
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29717535,
                     ECO:0007744|PDB:6C02; propagated from UniProtKB/Swiss-Prot
                     (O14638.2)"
     CDS             1..875
                     /gene="ENPP3"
                     /gene_synonym="B10; CD203c; NPP3; PD-IBETA; PDNP3"
                     /coded_by="NM_005021.5:84..2711"
                     /db_xref="CCDS:CCDS5148.1"
                     /db_xref="GeneID:5169"
                     /db_xref="HGNC:HGNC:3358"
                     /db_xref="MIM:602182"
ORIGIN      
        1 mestltlate qpvkkntlkk ykiacivlla llvimslglg lglglrklek qgscrkkcfd
       61 asfrglencr cdvackdrgd ccwdfedtcv estriwmcnk frcgetrlea slcscsddcl
      121 qrkdccadyk svcqgetswl eencdtaqqs qcpegfdlpp vilfsmdgfr aeylytwdtl
      181 mpninklktc gihskymram yptktfpnhy tivtglypes hgiidnnmyd vnlnknfsls
      241 skeqnnpaww hgqpmwltam yqglkaatyf wpgsevaing sfpsiympyn gsvpfeeris
      301 tllkwldlpk aerprfytmy feepdssgha ggpvsarvik alqvvdhafg mlmeglkqrn
      361 lhncvniill adhgmdqtyc nkmeymtdyf prinffymye gpaprirahn iphdffsfns
      421 eeivrnlscr kpdqhfkpyl tpdlpkrlhy aknvridkvh lfvdqqwlav rsksntncgg
      481 gnhgynnefr smeaiflahg psfkekteve pfenievynl mcdllriqpa pnngthgsln
      541 hllkvpfyep shaeevskfs vcgfanplpt esldcfcphl qnstqleqvn qmlnltqeei
      601 tatvkvnlpf grprvlqknv dhcllyhrey vsgfgkamrm pmwssytvpq lgdtsplppt
      661 vpdclradvr vppsesqkcs fyladknith gflyppasnr tsdsqydali tsnlvpmyee
      721 frkmwdyfhs vllikhater ngvnvvsgpi fdynydghfd apdeitkhla ntdvpipthy
      781 fvvltscknk shtpencpgw ldvlpfiiph rptnvescpe gkpealwvee rftahiarvr
      841 dvelltgldf yqdkvqpvse ilqlktylpt fetti
//
LOCUS       NP_081131                266 aa            linear   ROD 27-APR-2025
DEFINITION  protein ARV1 [Mus musculus].
ACCESSION   NP_081131
VERSION     NP_081131.1
DBSOURCE    REFSEQ: accession NM_026855.5
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Gallo-Ebert,C., Francisco,J., Liu,H.Y., Draper,R., Modi,K.,
            Hayward,M.D., Jones,B.K., Buiakova,O., McDonough,V. and
            Nickels,J.T. Jr.
  TITLE     Mice lacking ARV1 have reduced signs of metabolic syndrome and
            non-alcoholic fatty liver disease
  JOURNAL   J Biol Chem 293 (16), 5956-5974 (2018)
   PUBMED   29491146
  REMARK    GeneRIF: Arv1-/- animals fed a high-fat diet were resistant to
            diet-induced obesity, had lower blood cholesterol and triglyceride
            levels, and retained glucose tolerance and insulin sensitivity.
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Palmer,E.E., Jarrett,K.E., Sachdev,R.K., Al Zahrani,F.,
            Hashem,M.O., Ibrahim,N., Sampaio,H., Kandula,T., Macintosh,R.,
            Gupta,R., Conlon,D.M., Billheimer,J.T., Rader,D.J., Funato,K.,
            Walkey,C.J., Lee,C.S., Loo,C., Brammah,S., Elakis,G., Zhu,Y.,
            Buckley,M., Kirk,E.P., Bye,A., Alkuraya,F.S., Roscioli,T. and
            Lagor,W.R.
  TITLE     Neuronal deficiency of ARV1 causes an autosomal recessive epileptic
            encephalopathy
  JOURNAL   Hum Mol Genet 25 (14), 3042-3054 (2016)
   PUBMED   27270415
  REMARK    GeneRIF: In contrast to wild type human ARV1, neither variant
            expressed detectable levels of protein in mammalian cells. Mice
            with a neuronal deletion of Arv1 recapitulated the human phenotype,
            exhibiting seizures and a severe survival defect in adulthood. Our
            data support ARV1 deficiency as a cause of autosomal recessive
            epileptic encephalopathy
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Lagor,W.R., Tong,F., Jarrett,K.E., Lin,W., Conlon,D.M., Smith,M.,
            Wang,M.Y., Yenilmez,B.O., McCoy,M.G., Fields,D.W., O'Neill,S.M.,
            Gupta,R., Kumaravel,A., Redon,V., Ahima,R.S., Sturley,S.L.,
            Billheimer,J.T. and Rader,D.J.
  TITLE     Deletion of murine Arv1 results in a lean phenotype with increased
            energy expenditure
  JOURNAL   Nutr Diabetes 5 (10), e181 (2015)
   PUBMED   26479315
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Ruggles,K.V., Garbarino,J., Liu,Y., Moon,J., Schneider,K.,
            Henneberry,A., Billheimer,J., Millar,J.S., Marchadier,D.,
            Valasek,M.A., Joblin-Mills,A., Gulati,S., Munkacsi,A.B., Repa,J.J.,
            Rader,D. and Sturley,S.L.
  TITLE     A functional, genome-wide evaluation of liposensitive yeast
            identifies the 'ARE2 required for viability' (ARV1) gene product as
            a major component of eukaryotic fatty acid resistance
  JOURNAL   J Biol Chem 289 (7), 4417-4431 (2014)
   PUBMED   24273168
  REMARK    GeneRIF: These results implicate ARV1 as a protective factor in
            lipotoxic diseases due to modulation of fatty acid metabolism.
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Tong,F., Billheimer,J., Shechtman,C.F., Liu,Y., Crooke,R.,
            Graham,M., Cohen,D.E., Sturley,S.L. and Rader,D.J.
  TITLE     Decreased expression of ARV1 results in cholesterol retention in
            the endoplasmic reticulum and abnormal bile acid metabolism
  JOURNAL   J Biol Chem 285 (44), 33632-33641 (2010)
   PUBMED   20663892
  REMARK    GeneRIF: Arv1p has a role in sterol movement from the ER and in the
            ensuing regulation of hepatic cholesterol and bile acid metabolism
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC151736.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK004398.1, BC119376.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 72.81 cM"
     Protein         1..266
                     /product="protein ARV1"
                     /calculated_mol_wt=30404
     Region          28..217
                     /region_name="Arv1"
                     /note="Arv1-like family; pfam04161"
                     /db_xref="CDD:461202"
     Site            139..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D0U9.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D0U9.1)"
     Site            228..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D0U9.1)"
     CDS             1..266
                     /gene="Arv1"
                     /gene_synonym="1110067L22Rik"
                     /coded_by="NM_026855.5:19..819"
                     /db_xref="CCDS:CCDS22774.1"
                     /db_xref="GeneID:68865"
                     /db_xref="MGI:MGI:1916115"
ORIGIN      
        1 mgtggrrgtr sgkgtegaaa tsssclyrci ecnreaqely rdyshgvlki tickscqkpv
       61 dkyieydpvi ilinailckt qayrhilfnt kinihgklcm fcllceaylr wwqlqdssqs
      121 papddvirya kewdfyrmfv iasfeqaafl tgifaflwvq qpmtakrapd fvlllkalll
      181 ssygklllip aviwehdytp lclrlikvfv ltsnfqavrv tlntnrrlsl lvvlsgllle
      241 sivvfffqrm ewdvssdcal yksqdf
//
LOCUS       NP_005128                550 aa            linear   PRI 27-APR-2025
DEFINITION  integral membrane protein DGCR2/IDD isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_005128
VERSION     NP_005128.1
DBSOURCE    REFSEQ: accession NM_005137.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Belangero,S.I., Ota,V.K., Gadelha,A., Berberian,A.A.,
            Assuncao-Leme,I.B., Noto,C., Christofolini,D.M., Bellucco,F.T.,
            Santoro,M.L., Mazzotti,D.R., Zugman,A., Melaragno,M.I.,
            Smith,M.A.C., Pellegrino,R., Hakonarson,H., Cordeiro,Q.,
            Moretti,P.N., Bressan,R.A., Mari,J.J. and Jackowski,A.P.
  TITLE     DGCR2 influences cortical thickness through a mechanism independent
            of schizophrenia pathogenesis
  JOURNAL   Psychiatry Res 274, 391-394 (2019)
   PUBMED   30901624
  REMARK    GeneRIF: While no association between DGCR2 polymorphisms and
            schizophrenia was found, the missense variant rs2072123 was
            associated to left rostral anterior cingulate thickness, showing
            that DGCR2 seems not to be associated directly with the
            schizophrenia but might be influencing the brain morphology. We
            also showed a DGCR2 downregulation in schizophrenia patients when
            compared to controls and first episode of psychosis.
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Swaminathan,S., Huentelman,M.J., Corneveaux,J.J., Myers,A.J.,
            Faber,K.M., Foroud,T., Mayeux,R., Shen,L., Kim,S., Turk,M.,
            Hardy,J., Reiman,E.M. and Saykin,A.J.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative  and  NIA-LOAD/NCRAD
            Family Study Group
  TITLE     Analysis of copy number variation in Alzheimer's disease in a
            cohort of clinically characterized and neuropathologically verified
            individuals
  JOURNAL   PLoS One 7 (12), e50640 (2012)
   PUBMED   23227193
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Gong,W., Emanuel,B.S., Collins,J., Kim,D.H., Wang,Z., Chen,F.,
            Zhang,G., Roe,B. and Budarf,M.L.
  TITLE     A transcription map of the DiGeorge and velo-cardio-facial syndrome
            minimal critical region on 22q11
  JOURNAL   Hum Mol Genet 5 (6), 789-800 (1996)
   PUBMED   8776594
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Kajiwara,K., Nagasawa,H., Shimizu-Nishikawa,K., Ookura,T.,
            Kimura,M. and Sugaya,E.
  TITLE     Cloning of SEZ-12 encoding seizure-related and membrane-bound
            adhesion protein
  JOURNAL   Biochem Biophys Res Commun 222 (1), 144-148 (1996)
   PUBMED   8630060
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Wadey,R., Daw,S., Taylor,C., Atif,U., Kamath,S., Halford,S.,
            O'Donnell,H., Wilson,D., Goodship,J., Burn,J. et al.
  TITLE     Isolation of a gene encoding an integral membrane protein from the
            vicinity of a balanced translocation breakpoint associated with
            DiGeorge syndrome
  JOURNAL   Hum Mol Genet 4 (6), 1027-1033 (1995)
   PUBMED   7655455
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Demczuk,S., Aledo,R., Zucman,J., Delattre,O., Desmaze,C.,
            Dauphinot,L., Jalbert,P., Rouleau,G.A., Thomas,G. and Aurias,A.
  TITLE     Cloning of a balanced translocation breakpoint in the DiGeorge
            syndrome critical region and isolation of a novel potential
            adhesion receptor gene in its vicinity
  JOURNAL   Hum Mol Genet 4 (4), 551-558 (1995)
   PUBMED   7633403
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Augusseau,S., Jouk,S., Jalbert,P. and Prieur,M.
  TITLE     DiGeorge syndrome and 22q11 rearrangements
  JOURNAL   Hum Genet 74 (2), 206 (1986)
   PUBMED   3770751
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA494775.1, D79985.1 and
            BC040500.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Deletions of the 22q11.2 have been associated with a wide
            range of developmental defects (notably DiGeorge syndrome,
            velocardiofacial syndrome, conotruncal anomaly face syndrome and
            isolated conotruncal cardiac defects) classified under the acronym
            CATCH 22. The DGCR2 gene encodes a novel putative adhesion receptor
            protein, which could play a role in neural crest cells migration, a
            process which has been proposed to be altered in DiGeorge syndrome.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040500.1, SRR1803611.76350.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263196.12/ ENSP00000263196.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..550
                     /product="integral membrane protein DGCR2/IDD isoform 1
                     precursor"
                     /note="integral membrane protein DGCR2/IDD; integral
                     membrane protein deleted in DiGeorge syndrome; DiGeorge
                     syndrome critical region protein 2"
                     /calculated_mol_wt=58354
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2475
     Region          30..66
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(35,45,56..57)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(49,52,56,62..63)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            59..63
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          69..92
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98153.1)"
     Region          115..267
                     /region_name="CLECT_DGCR2_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in DGCR2, an integral membrane protein deleted in DiGeorge
                     Syndrome (DGS); cd03599"
                     /db_xref="CDD:153069"
     Site            149
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98153.1)"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98153.1)"
     Site            order(231,235,237,251,253..256,259..261)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153069"
     Region          271..329
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Site            350..368
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98153.1)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P98153.1)"
     Region          <428..537
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          500..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98153.1)"
     CDS             1..550
                     /gene="DGCR2"
                     /gene_synonym="DGS-C; IDD; LAN; SEZ-12"
                     /coded_by="NM_005137.3:207..1859"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS33598.1"
                     /db_xref="GeneID:9993"
                     /db_xref="HGNC:HGNC:2845"
                     /db_xref="MIM:600594"
ORIGIN      
        1 mvpkadsgaf lllfllvltv teplrpelrc npgqfacrsg tiqciplpwq cdgwatcede
       61 sdeancpevt gevrphhgke avdprqgrar ggdpshfhav nvaqpvrfss flgkcptgwh
      121 hyegtascyr vylsgenywd aaqtcqrlng slatfstdqe lrfvlaqewd qpersfgwkd
      181 qrklwvgyqy vitgrnrsle grwevafkgs sevflppdpi fasamsendn vfcaqlqcfh
      241 fptlrhhdlh swhaescyek ssflckrsqt cvdikdnvvd egfyftpkgd dpclsctchg
      301 gepemcvaal cerpqgcqqy rkdpkecckf mcldpdgnsl fdsmasgmrl vvscissfli
      361 lslllfmvhr lrqrrrerie sliganlhhf nlgrripgfd ygpdgfgtgl tplhlsddge
      421 ggtfhfhdpp ppytaykypd igqpddpppp yeasihpdsv fydpadddaf epvevslpap
      481 gdggsegall rrleqplpta gasladleds adsssallvp pdpaqsgstp aaealpgggr
      541 hsrsslntvv
//
LOCUS       NP_001092007            1342 aa            linear   PRI 27-APR-2025
DEFINITION  patatin-like phospholipase domain-containing protein 7 isoform a
            [Homo sapiens].
ACCESSION   NP_001092007
VERSION     NP_001092007.2
DBSOURCE    REFSEQ: accession NM_001098537.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1342)
  AUTHORS   Bai,Y., Luo,K. and Xie,W.
  TITLE     The phospholipase PNPLA7 functions as a positive indicator in human
            colorectal and gastric cancers
  JOURNAL   Medicine (Baltimore) 102 (42), e35279 (2023)
   PUBMED   37861523
  REMARK    GeneRIF: The phospholipase PNPLA7 functions as a positive indicator
            in human colorectal and gastric cancers.
REFERENCE   2  (residues 1 to 1342)
  AUTHORS   Harada,S., Taketomi,Y., Aiba,T., Kawaguchi,M., Hirabayashi,T.,
            Uranbileg,B., Kurano,M., Yatomi,Y. and Murakami,M.
  TITLE     The Lysophospholipase PNPLA7 Controls Hepatic Choline and
            Methionine Metabolism
  JOURNAL   Biomolecules 13 (3), 471 (2023)
   PUBMED   36979406
  REMARK    GeneRIF: The Lysophospholipase PNPLA7 Controls Hepatic Choline and
            Methionine Metabolism.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1342)
  AUTHORS   Zhao,Z., Heier,C., Pang,H., Wang,Y., Huang,F. and Chang,P.
  TITLE     The Patatin-Like Phospholipase Domain Containing Protein 7
            Regulates Macrophage Classical Activation through SIRT1/NF-kappaB
            and p38 MAPK Pathways
  JOURNAL   Int J Mol Sci 23 (23), 14983 (2022)
   PUBMED   36499308
  REMARK    GeneRIF: The Patatin-Like Phospholipase Domain Containing Protein 7
            Regulates Macrophage Classical Activation through SIRT1/NF-kappaB
            and p38 MAPK Pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1342)
  AUTHORS   Wang,X., Guo,M., Wang,Q., Wang,Q., Zuo,S., Zhang,X., Tong,H.,
            Chen,J., Wang,H., Chen,X., Guo,J., Su,X., Liang,H., Zhou,H. and
            Li,J.Z.
  TITLE     The Patatin-Like Phospholipase Domain Containing Protein 7
            Facilitates VLDL Secretion by Modulating ApoE Stability
  JOURNAL   Hepatology 72 (5), 1569-1585 (2020)
   PUBMED   32103509
  REMARK    GeneRIF: The Patatin-Like Phospholipase Domain Containing Protein 7
            Facilitates VLDL Secretion by Modulating ApoE Stability.
REFERENCE   5  (residues 1 to 1342)
  AUTHORS   Heier,C., Kien,B., Huang,F., Eichmann,T.O., Xie,H., Zechner,R. and
            Chang,P.A.
  TITLE     The phospholipase PNPLA7 functions as a lysophosphatidylcholine
            hydrolase and interacts with lipid droplets through its catalytic
            domain
  JOURNAL   J Biol Chem 292 (46), 19087-19098 (2017)
   PUBMED   28887301
  REMARK    GeneRIF: PNPLA7 acts as an endoplasmic reticulum -anchored
            lysophosphatidylcholine hydrolase that is composed of specific
            functional domains mediating catalytic activity, subcellular
            positioning, and interactions with cellular organelles.
REFERENCE   6  (residues 1 to 1342)
  AUTHORS   Su,Y., Kong,G.L., Su,Y.L., Zhou,Y., Lv,L.F., Wang,Q., Huang,B.P.,
            Zheng,R.Z., Li,Q.Z., Yuan,H.J. and Zhao,Z.G.
  TITLE     Correlation analysis of the PNPLA7 gene polymorphism and
            susceptibility to menstrual disorder
  JOURNAL   Genet Mol Res 14 (1), 1733-1740 (2015)
   PUBMED   25867316
  REMARK    GeneRIF: We explored Single Nucleotide Polymorphism in the PNPLA7
            gene on chromosome 9 and investigated their correlation with the
            susceptibility to menstrual disorder.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1342)
  AUTHORS   Kienesberger,P.C., Oberer,M., Lass,A. and Zechner,R.
  TITLE     Mammalian patatin domain containing proteins: a family with diverse
            lipolytic activities involved in multiple biological functions
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S63-S68 (2009)
   PUBMED   19029121
  REMARK    Review article
REFERENCE   8  (residues 1 to 1342)
  AUTHORS   Wilson,P.A., Gardner,S.D., Lambie,N.M., Commans,S.A. and
            Crowther,D.J.
  TITLE     Characterization of the human patatin-like phospholipase family
  JOURNAL   J Lipid Res 47 (9), 1940-1949 (2006)
   PUBMED   16799181
REFERENCE   9  (residues 1 to 1342)
  AUTHORS   Winrow,C.J., Hemming,M.L., Allen,D.M., Quistad,G.B., Casida,J.E.
            and Barlow,C.
  TITLE     Loss of neuropathy target esterase in mice links organophosphate
            exposure to hyperactivity
  JOURNAL   Nat Genet 33 (4), 477-485 (2003)
   PUBMED   12640454
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA963194.1, AK126267.1, AK125060.1, AL365502.57 and AL832944.1.
            
            On Apr 19, 2014 this sequence version replaced NP_001092007.1.
            
            Summary: Human patatin-like phospholipases, such as PNPLA7, have
            been implicated in regulation of adipocyte differentiation and have
            been induced by metabolic stimuli (Wilson et al., 2006 [PubMed
            16799181]).[supplied by OMIM, Jun 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.130318.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000406427.6/ ENSP00000384610.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..1342
                     /product="patatin-like phospholipase domain-containing
                     protein 7 isoform a"
                     /EC_number="3.1.1.5"
                     /note="patatin-like phospholipase domain-containing
                     protein 7; patatin like phospholipase domain containing 7"
                     /calculated_mol_wt=148301
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZV29.4)"
     Region          170..291
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(239..240,255,257..258)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(278..280,284..286)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          345..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZV29.4)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6ZV29.4)"
     Region          395..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZV29.4)"
     Region          484..592
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(554..555,564..566)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Region          607..715
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(670..671,680..682)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Region          684..970
                     /region_name="Involved in the binding to lipid droplets.
                     /evidence=ECO:0000250|UniProtKB:A2AJ88"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZV29.4)"
     Site            order(702..704,708..710)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          936..1241
                     /region_name="Pat_PNPLA6_PNPLA7"
                     /note="Patatin-like phospholipase domain containing
                     protein 6 and protein 7; cd07225"
                     /db_xref="CDD:132864"
     Region          957..962
                     /region_name="GXGXXG.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01161"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZV29.4)"
     Site            order(958..959,961,986,1106)
                     /site_type="active"
                     /db_xref="CDD:132864"
     Region          984..988
                     /region_name="GXSXG.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01161"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZV29.4)"
     Site            984..988
                     /site_type="other"
                     /note="nucleophile elbow"
                     /db_xref="CDD:132864"
     Region          1106..1108
                     /region_name="DGA/G.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01161"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZV29.4)"
     Site            1283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AJ88; propagated from
                     UniProtKB/Swiss-Prot (Q6ZV29.4)"
     Site            1287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5BK26; propagated from
                     UniProtKB/Swiss-Prot (Q6ZV29.4)"
     Region          1296..1342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZV29.4)"
     CDS             1..1342
                     /gene="PNPLA7"
                     /gene_synonym="C9orf111; NTE-R1; NTEL1"
                     /coded_by="NM_001098537.3:206..4234"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS48070.1"
                     /db_xref="GeneID:375775"
                     /db_xref="HGNC:HGNC:24768"
                     /db_xref="MIM:612122"
ORIGIN      
        1 meeekddspq adfclgtalh swglwfteeg spstmltgia vgallalalv gvlilfmfrr
       61 lrqfrqaqpt pqyrfrkrdk vmfygrkimr kvttlpntlv entalprqra rkrtkvlsla
      121 krilrfkkey palqpkeppp slleadltef dvknshlpse vlymlknvrv lghfekplfl
      181 elckhivfvq lqegehvfqp repdpsicvv qdgrlevciq dtdgtevvvk evlagdsvhs
      241 llsildiitg haapyktvsv raaipstilr lpaaafhgvf ekypetlvrv vqiimvrlqr
      301 vtflalhnyl glttelfnae sqaiplvsva svaagkakkq vfygeeerlk kpprlqescd
      361 sdhgggrpaa agpllkrshs vpapsirkqi leelekpgag dpdpsapqgg pgsatsdlgm
      421 acdrarvflh sdehpgssva sksrksvmva eipstvsqhs eshtdetlas rksdaifraa
      481 kkdlltlmkl edsslldgrv allhvpagtv vsrqgdqdas ilfvvsgllh vyqrkigsqe
      541 dtclfltrpg emvgqlavlt gepliftvka nrdcsflsis kahfyeimrk qptvvlgvah
      601 tvvkrmssfv rqidfaldwv eveagraiyr qgdksdctyi mlsgrlrsvi rkddgkkrla
      661 geygrgdlvg vvetlthqar attvhavrds elaklpagal tsikrrypqv vtrlihllge
      721 kilgslqqgp vtghqlglpt egskwdlgnp avnlstvavm pvseevplta falelehals
      781 aigptlllts dnikrrlgsa aldsvheyrl sswlgqqedt hrivlyqadg tltpwtqrcv
      841 rqadcilivg lgdqeptvge lermlestav raqkqlillh reegpapart vewlnmrswc
      901 sghlhlccpr rvfsrrslpk lvemykhvfq rppdrhsdfs rlarvltgna ialvlgggga
      961 rgcaqvgvlk alaecgipvd mvggtsigaf vgalyseern ysqmrirakq waegmtslmk
     1021 aaldltypit smfsgagfns sifsvfkdqq iedlwipyfa ittditasam rvhtdgslww
     1081 yvrasmslsg ympplcdpkd ghllmdggyi nnlpadvars mgakvviaid vgsrdetdlt
     1141 nygdalsgww llwkrwnpla tkvkvlnmae iqtrlayvcc vrqlevvkss dyceylrppi
     1201 dsystldfgk fneicevgyq hgrtvfdiwg rsgvlekmlr dqqgpskkpa savltcpnas
     1261 ftdlaeivsr iepakpamvd desdyqteye eelldvprda yadfqstsaq qgsdledess
     1321 lrhrhpslaf pklsegssdq dg
//
LOCUS       NP_000156                382 aa            linear   PRI 27-APR-2025
DEFINITION  gap junction alpha-1 protein [Homo sapiens].
ACCESSION   NP_000156
VERSION     NP_000156.1
DBSOURCE    REFSEQ: accession NM_000165.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Irwin,R.M., Thomas,M.A., Fahey,M.J., Mayan,M.D., Smyth,J.W. and
            Delco,M.L.
  TITLE     Connexin 43 regulates intercellular mitochondrial transfer from
            human mesenchymal stromal cells to chondrocytes
  JOURNAL   Stem Cell Res Ther 15 (1), 359 (2024)
   PUBMED   39390589
  REMARK    GeneRIF: Connexin 43 regulates intercellular mitochondrial transfer
            from human mesenchymal stromal cells to chondrocytes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Chen,J.C., Yeh,K.T., Lin,Y.M. and Cheng,Y.W.
  TITLE     Mutations of the Cx43 Gene in Non-Small Cell Lung Cancer:
            Association with Aberrant Localization of Cx43 Protein Expression
            and Tumor Progression
  JOURNAL   Medicina (Kaunas) 60 (10), 1641 (2024)
   PUBMED   39459427
  REMARK    GeneRIF: Mutations of the Cx43 Gene in Non-Small Cell Lung Cancer:
            Association with Aberrant Localization of Cx43 Protein Expression
            and Tumor Progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Fu,Y., Sun,X., He,Q., Gu,Z., Jia,X. and Zhuang,Z.
  TITLE     Connexin 43 controls metastatic behavior in triple negative breast
            cancer through TGFbeta1-Smad3-intergin alphaV signaling axis Based
            on optical image diagnosis
  JOURNAL   SLAS Technol 29 (5), 100190 (2024)
   PUBMED   39299505
  REMARK    GeneRIF: Connexin 43 controls metastatic behavior in triple
            negative breast cancer through TGFbeta1-Smad3-intergin alphaV
            signaling axis Based on optical image diagnosis.
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Luse,M.A., Dunaway,L.S., Nyshadham,S., Carvalho,A., Sedovy,M.W.,
            Ruddiman,C.A., Tessema,R., Hirschi,K., Johnstone,S.R. and
            Isakson,B.E.
  TITLE     Endothelial-adipocyte Cx43 Mediated Gap Junctions Can Regulate
            Adiposity
  JOURNAL   Function (Oxf) 5 (5) (2024)
   PUBMED   38984993
  REMARK    GeneRIF: Endothelial-adipocyte Cx43 Mediated Gap Junctions Can
            Regulate Adiposity.
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Della Morte,E., Giannasi,C., Valenza,A., Cadelano,F., Aldegheri,A.,
            Zagra,L., Niada,S. and Brini,A.T.
  TITLE     Connexin 43 Modulation in Human Chondrocytes, Osteoblasts and
            Cartilage Explants: Implications for Inflammatory Joint Disorders
  JOURNAL   Int J Mol Sci 25 (15), 8547 (2024)
   PUBMED   39126115
  REMARK    GeneRIF: Connexin 43 Modulation in Human Chondrocytes, Osteoblasts
            and Cartilage Explants: Implications for Inflammatory Joint
            Disorders.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Britz-Cunningham,S.H., Shah,M.M., Zuppan,C.W. and Fletcher,W.H.
  TITLE     Mutations of the Connexin43 gap-junction gene in patients with
            heart malformations and defects of laterality
  JOURNAL   N Engl J Med 332 (20), 1323-1329 (1995)
   PUBMED   7715640
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Fishman,G.I., Moreno,A.P., Spray,D.C. and Leinwand,L.A.
  TITLE     Functional analysis of human cardiac gap junction channel mutants
  JOURNAL   Proc Natl Acad Sci U S A 88 (9), 3525-3529 (1991)
   PUBMED   1850831
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Fishman,G.I., Eddy,R.L., Shows,T.B., Rosenthal,L. and Leinwand,L.A.
  TITLE     The human connexin gene family of gap junction proteins: distinct
            chromosomal locations but similar structures
  JOURNAL   Genomics 10 (1), 250-256 (1991)
   PUBMED   1646158
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Fishman,G.I., Spray,D.C. and Leinwand,L.A.
  TITLE     Molecular characterization and functional expression of the human
            cardiac gap junction channel
  JOURNAL   J Cell Biol 111 (2), 589-598 (1990)
   PUBMED   1696265
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP226987.1, BC026329.1,
            AL139098.15 and AW664595.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the connexin gene family. The
            encoded protein is a component of gap junctions, which are composed
            of arrays of intercellular channels that provide a route for the
            diffusion of low molecular weight materials from cell to cell. The
            encoded protein is the major protein of gap junctions in the heart
            that are thought to have a crucial role in the synchronized
            contraction of the heart and in embryonic development. A related
            intronless pseudogene has been mapped to chromosome 5. Mutations in
            this gene have been associated with oculodentodigital dysplasia,
            autosomal recessive craniometaphyseal dysplasia and heart
            malformations. [provided by RefSeq, May 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.188866.1,
                                           SRR1660803.132563.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282561.4/ ENSP00000282561.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31"
     Protein         1..382
                     /product="gap junction alpha-1 protein"
                     /note="gap junction 43 kDa heart protein; connexin-43; gap
                     junction protein, alpha 1, 43kDa"
                     /calculated_mol_wt=42877
     Region          3..233
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08050; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            24..44
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P17302.2)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P17302.2)"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P17302.2)"
     Site            208..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P17302.2)"
     Region          244..382
                     /region_name="Interaction with NOV.
                     /evidence=ECO:0000250|UniProtKB:P08050"
                     /note="propagated from UniProtKB/Swiss-Prot (P17302.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P23242; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15605363,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14702389,
                     ECO:0000269|PubMed:15605363; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Region          264..382
                     /region_name="Interaction with UBQLN4.
                     /evidence=ECO:0000250|UniProtKB:P23242"
                     /note="propagated from UniProtKB/Swiss-Prot (P17302.2)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P23242; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Region          283..361
                     /region_name="Connexin43"
                     /note="Gap junction alpha-1 protein (Cx43); pfam03508"
                     /db_xref="CDD:460950"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23242; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Region          317..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17302.2)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:12270943; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P23242; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:12270943; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:12270943; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23242; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCG and PKC/PRKCD.
                     /evidence=ECO:0000250|UniProtKB:P23242; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23242; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08050; propagated from
                     UniProtKB/Swiss-Prot (P17302.2)"
     CDS             1..382
                     /gene="GJA1"
                     /gene_synonym="AVSD3; CMDR; CX43; EKVP; EKVP3; GJAL;
                     HLHS1; HSS; ODDD; PPKCA"
                     /coded_by="NM_000165.5:204..1352"
                     /db_xref="CCDS:CCDS5123.1"
                     /db_xref="GeneID:2697"
                     /db_xref="HGNC:HGNC:4274"
                     /db_xref="MIM:121014"
ORIGIN      
        1 mgdwsalgkl ldkvqaysta ggkvwlsvlf ifrilllgta vesawgdeqs afrcntqqpg
       61 cenvcydksf pishvrfwvl qiifvsvptl lylahvfyvm rkeeklnkke eelkvaqtdg
      121 vnvdmhlkqi eikkfkygie ehgkvkmrgg llrtyiisil fksifevafl liqwyiygfs
      181 lsavytckrd pcphqvdcfl srptektifi ifmlvvslvs lalniielfy vffkgvkdrv
      241 kgksdpyhat sgalspakdc gsqkyayfng cssptaplsp msppgyklvt gdrnnsscrn
      301 ynkqaseqnw anysaeqnrm gqagstisns haqpfdfpdd nqnskklaag helqplaivd
      361 qrpssrassr assrprpddl ei
//
LOCUS       NP_001357444             225 aa            linear   PRI 27-APR-2025
DEFINITION  phosphoserine phosphatase [Homo sapiens].
ACCESSION   NP_001357444
VERSION     NP_001357444.1
DBSOURCE    REFSEQ: accession NM_001370515.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Rawat,V., Malvi,P., Della Manna,D., Yang,E.S., Bugide,S., Zhang,X.,
            Gupta,R. and Wajapeyee,N.
  TITLE     PSPH promotes melanoma growth and metastasis by metabolic
            deregulation-mediated transcriptional activation of NR4A1
  JOURNAL   Oncogene 40 (13), 2448-2462 (2021)
   PUBMED   33674745
  REMARK    GeneRIF: PSPH promotes melanoma growth and metastasis by metabolic
            deregulation-mediated transcriptional activation of NR4A1.
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Park,S.M., Seo,E.H., Bae,D.H., Kim,S.S., Kim,J., Lin,W., Kim,K.H.,
            Park,J.B., Kim,Y.S., Yin,J. and Kim,S.Y.
  TITLE     Phosphoserine Phosphatase Promotes Lung Cancer Progression through
            the Dephosphorylation of IRS-1 and a Noncanonical
            L-Serine-Independent Pathway
  JOURNAL   Mol Cells 42 (8), 604-616 (2019)
   PUBMED   31446747
  REMARK    GeneRIF: a specific interaction between PSPH and IRS1 and the
            dephosphorylation of phospho-IRS-1 by PSPH in lung cancer cells,
            was identified.
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Haufroid,M., Mirgaux,M., Leherte,L. and Wouters,J.
  TITLE     Crystal structures and snapshots along the reaction pathway of
            human phosphoserine phosphatase
  JOURNAL   Acta Crystallogr D Struct Biol 75 (Pt 6), 592-604 (2019)
   PUBMED   31205021
  REMARK    GeneRIF: three new high-resolution crystal structures of hPSP
            (1.5-2.0 A) in complexes with phosphoserine and with serine, which
            are the substrate and the product of the reaction, respectively,
            and in complex with a noncleavable substrate analogue (homocysteic
            acid) are presented.
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Liao,L., Ge,M., Zhan,Q., Huang,R., Ji,X., Liang,X. and Zhou,X.
  TITLE     PSPH Mediates the Metastasis and Proliferation of Non-small Cell
            Lung Cancer through MAPK Signaling Pathways
  JOURNAL   Int J Biol Sci 15 (1), 183-194 (2019)
   PUBMED   30662358
  REMARK    GeneRIF: The results suggest that PSPH may act as a putative
            oncogene and a potential therapeutic target in NSCLC.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 225)
  AUTHORS   van der Crabben,S.N. and de Koning,T.J.
  TITLE     Serine Deficiency Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37347880
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Veeranna and Shetty,K.T.
  TITLE     Phosphoserine phosphatase of human brain: partial purification,
            characterization, regional distribution, and effect of certain
            modulators including psychoactive drugs
  JOURNAL   Neurochem Res 15 (12), 1203-1210 (1990)
   PUBMED   1965857
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Minelli,A., Piantanida,M., Maserati,E., Campagnoli,E., Pasquali,F.
            and Danesino,C.
  TITLE     Gene dosage effect in acquired monosomy 7: distinct behaviour of
            beta-glucuronidase and phosphoserine phosphatase
  JOURNAL   Genes Chromosomes Cancer 1 (3), 216-220 (1990)
   PUBMED   1964582
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Novelli,G. and Dallapiccola,B.
  TITLE     Gene dosage studies regionally assign the phosphoserine phosphatase
            gene to 7p15.1 or 2
  JOURNAL   Ann Genet 31 (3), 195-196 (1988)
   PUBMED   2851960
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Moro-Furlani,A.M., Turner,V.S. and Hopkinson,D.A.
  TITLE     Genetical and biochemical studies on human phosphoserine
            phosphatase
  JOURNAL   Ann Hum Genet 43 (4), 323-333 (1980)
   PUBMED   6249179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092579.3.
            
            Summary: The protein encoded by this gene belongs to a subfamily of
            the phosphotransferases. This encoded enzyme is responsible for the
            third and last step in L-serine formation. It catalyzes
            magnesium-dependent hydrolysis of L-phosphoserine and is also
            involved in an exchange reaction between L-serine and
            L-phosphoserine. Deficiency of this protein is thought to be linked
            to Williams syndrome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.192192.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2159912
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p11.2"
     Protein         1..225
                     /product="phosphoserine phosphatase"
                     /EC_number="3.1.3.3"
                     /note="L-3-phosphoserine phosphatase; O-phosphoserine
                     phosphohydrolase; PSPase"
                     /calculated_mol_wt=24877
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P78330.2)"
     Region          15..216
                     /region_name="HAD_PSP_eu"
                     /note="phosphoserine phosphatase eukaryotic-like, similar
                     to human phosphoserine phosphatase; cd04309"
                     /db_xref="CDD:319801"
     Site            order(20..24,29,109..110,158,178..179,182..183)
                     /site_type="active"
                     /db_xref="CDD:319801"
     CDS             1..225
                     /gene="PSPH"
                     /gene_synonym="PSP; PSPHD"
                     /coded_by="NM_001370515.1:900..1577"
                     /db_xref="CCDS:CCDS5522.1"
                     /db_xref="GeneID:5723"
                     /db_xref="HGNC:HGNC:9577"
                     /db_xref="MIM:172480"
ORIGIN      
        1 mvshselrkl fysadavcfd vdstvireeg idelakicgv edavsemtrr amggavpfka
       61 alterlaliq psreqvqrli aeqpphltpg irelvsrlqe rnvqvflisg gfrsivehva
      121 sklnipatnv fanrlkfyfn geyagfdetq ptaesggkgk vikllkekfh fkkiimigdg
      181 atdmeacppa dafigfggnv irqqvkdnak wyitdfvell gelee
//
LOCUS       NP_112572                515 aa            linear   PRI 27-APR-2025
DEFINITION  Fc receptor-like protein 4 precursor [Homo sapiens].
ACCESSION   NP_112572
VERSION     NP_112572.1
DBSOURCE    REFSEQ: accession NM_031282.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Carlsen,E.D., Bhavsar,S., Cook,J.R. and Swerdlow,S.H.
  TITLE     IRTA1 positivity helps identify a MALT-lymphoma-like subset of
            primary cutaneous marginal zone lymphomas, largely but not
            exclusively defined by IgM expression
  JOURNAL   J Cutan Pathol 49 (1), 55-60 (2022)
   PUBMED   34309899
  REMARK    GeneRIF: IRTA1 positivity helps identify a MALT-lymphoma-like
            subset of primary cutaneous marginal zone lymphomas, largely but
            not exclusively defined by IgM expression.
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Du,W., Han,M., Zhu,X., Xiao,F., Huang,E., Che,N., Tang,X., Zou,H.,
            Jiang,Q. and Lu,L.
  TITLE     The Multiple Roles of B Cells in the Pathogenesis of Sjogren's
            Syndrome
  JOURNAL   Front Immunol 12, 684999 (2021)
   PUBMED   34168653
  REMARK    GeneRIF: The Multiple Roles of B Cells in the Pathogenesis of
            Sjogren's Syndrome.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Li,H., Dement-Brown,J., Liao,P.J., Mazo,I., Mills,F., Kraus,Z.,
            Fitzsimmons,S. and Tolnay,M.
  TITLE     Fc receptor-like 4 and 5 define human atypical memory B cells
  JOURNAL   Int Immunol 32 (12), 755-770 (2020)
   PUBMED   32805738
  REMARK    GeneRIF: Fc receptor-like 4 and 5 define human atypical memory B
            cells.
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Falini,B., Tiacci,E., Pucciarini,A., Bigerna,B., Kurth,J.,
            Hatzivassiliou,G., Droetto,S., Galletti,B.V., Gambacorta,M.,
            Orazi,A., Pasqualucci,L., Miller,I., Kuppers,R., Dalla-Favera,R.
            and Cattoretti,G.
  TITLE     Expression of the IRTA1 receptor identifies intraepithelial and
            subepithelial marginal zone B cells of the mucosa-associated
            lymphoid tissue (MALT)
  JOURNAL   Blood 102 (10), 3684-3692 (2003)
   PUBMED   12881317
  REMARK    GeneRIF: role of IRTA1 in the immune function of B cells within
            epithelia
REFERENCE   6  (residues 1 to 515)
  AUTHORS   Lestou,V.S., Ludkovski,O., Connors,J.M., Gascoyne,R.D., Lam,W.L.
            and Horsman,D.E.
  TITLE     Characterization of the recurrent translocation
            t(1;1)(p36.3;q21.1-2) in non-Hodgkin lymphoma by multicolor banding
            and fluorescence in situ hybridization analysis
  JOURNAL   Genes Chromosomes Cancer 36 (4), 375-381 (2003)
   PUBMED   12619161
REFERENCE   7  (residues 1 to 515)
  AUTHORS   Guselnikov,S.V., Ershova,S.A., Mechetina,L.V., Najakshin,A.M.,
            Volkova,O.Y., Alabyev,B.Y. and Taranin,A.V.
  TITLE     A family of highly diverse human and mouse genes structurally links
            leukocyte FcR, gp42 and PECAM-1
  JOURNAL   Immunogenetics 54 (2), 87-95 (2002)
   PUBMED   12037601
REFERENCE   8  (residues 1 to 515)
  AUTHORS   Miller,I., Hatzivassiliou,G., Cattoretti,G., Mendelsohn,C. and
            Dalla-Favera,R.
  TITLE     IRTAs: a new family of immunoglobulinlike receptors differentially
            expressed in B cells
  JOURNAL   Blood 99 (8), 2662-2669 (2002)
   PUBMED   11929751
  REMARK    GeneRIF: Characterization and comparison of the structure and
            B-cell expression pattern of the entire family of IRTA genes, which
            includes 5 members contiguously located on chromosome.
REFERENCE   9  (residues 1 to 515)
  AUTHORS   Davis,R.S., Wang,Y.H., Kubagawa,H. and Cooper,M.D.
  TITLE     Identification of a family of Fc receptor homologs with
            preferential B cell expression
  JOURNAL   Proc Natl Acad Sci U S A 98 (17), 9772-9777 (2001)
   PUBMED   11493702
REFERENCE   10 (residues 1 to 515)
  AUTHORS   Hatzivassiliou,G., Miller,I., Takizawa,J., Palanisamy,N., Rao,P.H.,
            Iida,S., Tagawa,S., Taniwaki,M., Russo,J., Neri,A., Cattoretti,G.,
            Clynes,R., Mendelsohn,C., Chaganti,R.S. and Dalla-Favera,R.
  TITLE     IRTA1 and IRTA2, novel immunoglobulin superfamily receptors
            expressed in B cells and involved in chromosome 1q21 abnormalities
            in B cell malignancy
  JOURNAL   Immunity 14 (3), 277-289 (2001)
   PUBMED   11290337
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135929.5, AF343659.1 and
            AF343661.1.
            
            Summary: This gene encodes a member of the immunoglobulin receptor
            superfamily and is one of several Fc receptor-like glycoproteins
            clustered on the long arm of chromosome 1. The encoded protein has
            four extracellular C2-type immunoglobulin domains, a transmembrane
            domain and a cytoplasmic domain that contains three immune-receptor
            tyrosine-based inhibitory motifs. This protein may play a role in
            the function of memory B-cells in the epithelia. Aberrations in the
            chromosomal region encoding this gene are associated with
            non-Hodgkin lymphoma and multiple myeloma. [provided by RefSeq, Apr
            2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF343661.1, AF343660.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000271532.2/ ENSP00000271532.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.1"
     Protein         1..515
                     /product="Fc receptor-like protein 4 precursor"
                     /note="immunoglobulin superfamily receptor translocation
                     associated 1; immunoglobulin superfamily Fc receptor,
                     gp42; fc receptor-like protein 4; hIFGP2; fcR-like protein
                     4; IFGP family protein 2; fc receptor homolog 4; immune
                     receptor translocation-associated protein 1"
                     /calculated_mol_wt=55293
     sig_peptide     1..19
                     /calculated_mol_wt=1949
     Site            17..18
                     /site_type="other"
                     /note="Breakpoint for insertion to form FCRL4-IGHA1 fusion
                     protein; propagated from UniProtKB/Swiss-Prot (Q96PJ5.1)"
     mat_peptide     20..515
                     /product="Fc receptor-like protein 4"
                     /calculated_mol_wt=55293
     Region          23..100
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          40..44
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          54..58
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          70..74
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          82..87
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          93..96
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          105..170
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          119..123
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          133..137
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          150..154
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          164..169
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          193..281
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Region          295..377
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          306..310
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          320..324
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          342..346
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          356..361
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            374
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PJ5.1)"
     Site            388..408
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PJ5.1)"
     Region          449..454
                     /region_name="ITIM motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PJ5.1)"
     Region          461..466
                     /region_name="ITIM motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PJ5.1)"
     Region          491..496
                     /region_name="ITIM motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PJ5.1)"
     Region          494..515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PJ5.1)"
     CDS             1..515
                     /gene="FCRL4"
                     /gene_synonym="CD307d; FCRH4; IGFP2; IRTA1"
                     /coded_by="NM_031282.3:142..1689"
                     /db_xref="CCDS:CCDS1166.1"
                     /db_xref="GeneID:83417"
                     /db_xref="HGNC:HGNC:18507"
                     /db_xref="MIM:605876"
ORIGIN      
        1 mllwasllaf apvcgqsaaa hkpvisvhpp wttffkgerv tltcngfqfy atekttwyhr
       61 hywgekltlt pgntlevres glyrcqargs prsnpvrllf ssdslilqap ysvfegdtlv
      121 lrchrrrkek ltavkytwng nilsisnksw dllipqassn nngnyrcigy gdendvfrsn
      181 fkiikiqelf phpelkatds qptegnsvnl scetqlpper sdtplhfnff rdgevilsdw
      241 stypelqlpt vwrensgsyw cgaetvrgni hkhspslqih vqripvsgvl letqpsggqa
      301 vegemlvlvc svaegtgdtt fswhredmqe slgrktqrsl raelelpair qshaggyyct
      361 adnsygpvqs mvlnvtvret pgnrdglvaa gatggllsal llavallfhc wrrrksgvgf
      421 lgdetrlppa pgpgesshsi cpaqvelqsl yvdvhpkkgd lvyseiqttq lgeeeeants
      481 rtlledkdvs vvysevktqh pdnsagkiss kdees
//
LOCUS       NP_203537                422 aa            linear   ROD 27-APR-2025
DEFINITION  keratin, type I cytoskeletal 23 [Mus musculus].
ACCESSION   NP_203537 XP_909209
VERSION     NP_203537.1
DBSOURCE    REFSEQ: accession NM_033373.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Xie,Z., Ma,X.H., Bai,Q.F., Tang,J., Sun,J.H., Jiang,F., Guo,W.,
            Wang,C.M., Yang,R., Wen,Y.C., Wang,F.Y., Chen,Y.X., Zhang,H.,
            He,D.Z., Kelley,M.W., Yang,S. and Zhang,W.J.
  TITLE     ZBTB20 is essential for cochlear maturation and hearing in mice
  JOURNAL   Proc Natl Acad Sci U S A 120 (24), e2220867120 (2023)
   PUBMED   37279265
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Saito,K., Michon,F., Yamada,A., Inuzuka,H., Yamaguchi,S.,
            Fukumoto,E., Yoshizaki,K., Nakamura,T., Arakaki,M., Chiba,Y.,
            Ishikawa,M., Okano,H., Thesleff,I. and Fukumoto,S.
  TITLE     Sox21 Regulates Anapc10 Expression and Determines the Fate of
            Ectodermal Organ
  JOURNAL   iScience 23 (7), 101329 (2020)
   PUBMED   32674056
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Kim,D., Brocker,C.N., Takahashi,S., Yagai,T., Kim,T., Xie,G.,
            Wang,H., Qu,A. and Gonzalez,F.J.
  TITLE     Keratin 23 Is a Peroxisome Proliferator-Activated Receptor
            Alpha-Dependent, MYC-Amplified Oncogene That Promotes Hepatocyte
            Proliferation
  JOURNAL   Hepatology 70 (1), 154-167 (2019)
   PUBMED   30697791
  REMARK    GeneRIF: PPARA and MYC bind to sites within the Krt23 promoter
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Pehrson,J.R., Changolkar,L.N., Costanzi,C. and Leu,N.A.
  TITLE     Mice without macroH2A histone variants
  JOURNAL   Mol Cell Biol 34 (24), 4523-4533 (2014)
   PUBMED   25312643
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Gerber,S.D., Amann,R., Wyder,S. and Trueb,B.
  TITLE     Comparison of the gene expression profiles from normal and Fgfrl1
            deficient mouse kidneys reveals downstream targets of Fgfrl1
            signaling
  JOURNAL   PLoS One 7 (3), e33457 (2012)
   PUBMED   22432025
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Schweizer,J., Bowden,P.E., Coulombe,P.A., Langbein,L., Lane,E.B.,
            Magin,T.M., Maltais,L., Omary,M.B., Parry,D.A., Rogers,M.A. and
            Wright,M.W.
  TITLE     New consensus nomenclature for mammalian keratins
  JOURNAL   J Cell Biol 174 (2), 169-174 (2006)
   PUBMED   16831889
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Zhang,J.S., Wang,L., Huang,H., Nelson,M. and Smith,D.I.
  TITLE     Keratin 23 (K23), a novel acidic keratin, is highly induced by
            histone deacetylase inhibitors during differentiation of pancreatic
            cancer cells
  JOURNAL   Genes Chromosomes Cancer 30 (2), 123-135 (2001)
   PUBMED   11135429
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK036901.1 and AF102849.1.
            
            On Dec 7, 2005 this sequence version replaced XP_909209.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF102849.1, AK036954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN01164134
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 62.92 cM"
     Protein         1..422
                     /product="keratin, type I cytoskeletal 23"
                     /note="keratin complex 1, acidic, gene 23; cytokeratin-23;
                     type I intermediate filament cytokeratin"
                     /calculated_mol_wt=47896
     Region          1..71
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PS0.1)"
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PS0.1)"
     Region          71..377
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          72..107
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PS0.1)"
     Region          108..125
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PS0.1)"
     Region          126..217
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PS0.1)"
     Region          218..240
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PS0.1)"
     Region          241..378
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PS0.1)"
     Region          379..422
                     /region_name="Rod-like helical tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PS0.1)"
     CDS             1..422
                     /gene="Krt23"
                     /gene_synonym="CK23; Haik1; K23; Krt1-23"
                     /coded_by="NM_033373.2:57..1325"
                     /db_xref="CCDS:CCDS25382.1"
                     /db_xref="GeneID:94179"
                     /db_xref="MGI:MGI:2148866"
ORIGIN      
        1 mnsshsfnqt ysasvhslgs trgrqgschr apsvhggagg vrislsfttp gclppggswg
       61 sgrsspllgg ngkatmqnln drlatylekv raleeanskl etrilrwhqe repshrkdys
      121 qyeenisrlq eqivdgkman ahivvlidna rmavddfnlk fenehslkkd leieveglrk
      181 tlddltivtt dleqevegmr kelilmkkrh eqemeenhlp sdfkvsvkvd ttpgedlikv
      241 ledmrqeyel iikkkhqeld twfreqsaam aqevaspapv qgnqsdihel rrtfqaleid
      301 lqaqhsrkta lenmltetra ryscrlqdmq qiishyeeel iqlrqdlerq nnehkvllgi
      361 kthlekeiat yrrllegdte gtmdgsesrl kgseastika itqesvngri vlsqvneiqk
      421 hi
//
LOCUS       NP_061815                348 aa            linear   PRI 27-APR-2025
DEFINITION  homeobox protein HMX1 isoform 1 [Homo sapiens].
ACCESSION   NP_061815 XP_001133154
VERSION     NP_061815.2
DBSOURCE    REFSEQ: accession NM_018942.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Si,N., Meng,X., Lu,X., Liu,Z., Qi,Z., Wang,L., Li,C., Yang,M.,
            Zhang,Y., Wang,C., Guo,P., Zhu,L., Liu,L., Li,Z., Zhang,Z., Cai,Z.,
            Pan,B., Jiang,H. and Zhang,X.
  TITLE     Duplications involving the long range HMX1 enhancer are associated
            with human isolated bilateral concha-type microtia
  JOURNAL   J Transl Med 18 (1), 244 (2020)
   PUBMED   32552830
  REMARK    GeneRIF: Duplications involving the long range HMX1 enhancer are
            associated with human isolated bilateral concha-type microtia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Abdel-Salam,G.M.H., Abdel-Hamid,M.S., Mehrez,M.I., Kamal,A.M.,
            Taher,M.B. and Afifi,H.H.
  TITLE     Further delineation of the oculoauricular syndrome phenotype: A new
            family with a novel truncating HMX1 mutation
  JOURNAL   Ophthalmic Genet 39 (2), 215-220 (2018)
   PUBMED   29140751
  REMARK    GeneRIF: Mutation analysis revealed a novel homozygous nonsense
            mutation c.487G>T in the second exon of the HMX1 that predicted to
            introduce a premature stop codon at position 163 (p.E163*).
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Vaclavik,V., Schorderet,D.F., Borruat,F.X. and Munier,F.L.
  TITLE     Retinal dystrophy in the oculo-auricular syndrome due to HMX1
            mutation
  JOURNAL   Ophthalmic Genet 32 (2), 114-117 (2011)
   PUBMED   21417677
  REMARK    GeneRIF: The retinal degeneration in the recessively inherited
            oculo-auricular syndrome is a progressive rod-cone dystrophy.
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Schorderet,D.F., Nichini,O., Boisset,G., Polok,B., Tiab,L.,
            Mayeur,H., Raji,B., de la Houssaye,G., Abitbol,M.M. and Munier,F.L.
  TITLE     Mutation in the human homeobox gene NKX5-3 causes an
            oculo-auricular syndrome
  JOURNAL   Am J Hum Genet 82 (5), 1178-1184 (2008)
   PUBMED   18423520
  REMARK    GeneRIF: Linkage analysis and mutation screening revealed in the
            first exon of the NKX5-3 gene a homozygous 26 nucleotide deletion,
            generating a truncating protein that lacked the complete
            homeodomain.
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Amendt,B.A., Sutherland,L.B. and Russo,A.F.
  TITLE     Transcriptional antagonism between Hmx1 and Nkx2.5 for a shared
            DNA-binding site
  JOURNAL   J Biol Chem 274 (17), 11635-11642 (1999)
   PUBMED   10206974
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Stadler,H.S., Murray,J.C., Leysens,N.J., Goodfellow,P.J. and
            Solursh,M.
  TITLE     Phylogenetic conservation and physical mapping of members of the H6
            homeobox gene family
  JOURNAL   Mamm Genome 6 (6), 383-388 (1995)
   PUBMED   7647458
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Stadler,H.S., Padanilam,B.J., Buetow,K., Murray,J.C. and Solursh,M.
  TITLE     Identification and genetic mapping of a homeobox gene to the 4p16.1
            region of human chromosome 4
  JOURNAL   Proc Natl Acad Sci U S A 89 (23), 11579-11583 (1992)
   PUBMED   1360670
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC116612.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 27, 2006 this sequence version replaced NP_061815.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the H6 family of homeobox proteins. This protein can bind a
            5'-CAAG-3' core DNA sequence, and it is involved in the development
            of craniofacial structures. Mutations in this gene cause
            oculoauricular syndrome, a disorder of the eye and external ear.
            [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longer variant
            and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M99587.1, ERR3218380.250109.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000400677.5/ ENSP00000383516.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.1"
     Protein         1..348
                     /product="homeobox protein HMX1 isoform 1"
                     /note="homeobox protein HMX1; H6 homeodomain protein;
                     homeobox protein H6; NK5 homeobox 3"
                     /calculated_mol_wt=36024
     Region          29..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP08.2)"
     Region          206..260
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          263..273
                     /region_name="HMX family specific domain 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP08.2)"
     Region          276..289
                     /region_name="HMX family specific domain 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP08.2)"
     CDS             1..348
                     /gene="HMX1"
                     /gene_synonym="H6; NKX5-3"
                     /coded_by="NM_018942.3:226..1272"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47018.1"
                     /db_xref="GeneID:3166"
                     /db_xref="HGNC:HGNC:5017"
                     /db_xref="MIM:142992"
ORIGIN      
        1 mpdeltepgr atparassfl ienllaaeak gagratqgdg sredeeeddd dpededaeqa
       61 rrrrlqrrrq llagtgpgge ararallgpg alglgprppp gpgppfalgc ggaarwypra
      121 hggyggglsp dtsdrdspet geemgraega wprgpgpgav qreaaelaar gpaagteeas
      181 elaevpaaag etrggvgvgg grkkktrtvf srsqvfqles tfdlkrylss aeraglaasl
      241 qltetqvkiw fqnrrnkwkr qlaaeleaas lsppgaqrlv rvpvlyhesp paaaaagppa
      301 tlpfplapaa pappppllgf sgalayplaa fpaaasvpfl raqmpglv
//
LOCUS       NP_001239343             106 aa            linear   ROD 27-APR-2025
DEFINITION  RPA-interacting protein isoform 4 [Mus musculus].
ACCESSION   NP_001239343
VERSION     NP_001239343.1
DBSOURCE    REFSEQ: accession NM_001252414.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Kim,K., Lee,E.J., Lee,S.H., Seo,T., Jang,I.S., Park,J. and Lee,J.H.
  TITLE     Species-specific variation of RPA-interacting protein (RIP) splice
            isoforms
  JOURNAL   BMB Rep 42 (1), 22-27 (2009)
   PUBMED   19192389
  REMARK    GeneRIF: The alternative splicing of RIPalpha in the Drosophila,
            Xenopus, and mouse system, was examined.
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Park,J., Seo,T., Kim,H. and Choe,J.
  TITLE     Sumoylation of the novel protein hRIP{beta} is involved in
            replication protein A deposition in PML nuclear bodies
  JOURNAL   Mol Cell Biol 25 (18), 8202-8214 (2005)
   PUBMED   16135809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL596136.5, CB588111.1, DQ810271.1, BC047996.1 and BY576068.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG962238.1, AA231070.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 43.21 cM"
     Protein         1..106
                     /product="RPA-interacting protein isoform 4"
                     /note="RPA interacting protein epsilon; RPA interacting
                     protein delta 2"
                     /calculated_mol_wt=11990
     Region          8..47
                     /region_name="RPA_interact_N"
                     /note="Replication protein A interacting N-terminal;
                     pfam14766"
                     /db_xref="CDD:464304"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UA6; propagated from
                     UniProtKB/Swiss-Prot (Q9CWY9.1)"
     CDS             1..106
                     /gene="Rpain"
                     /gene_synonym="2400006N03Rik; Rip"
                     /coded_by="NM_001252414.2:309..629"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS56792.1"
                     /db_xref="GeneID:69723"
                     /db_xref="MGI:MGI:1916973"
ORIGIN      
        1 maessgsphr llykqvgsph wketfrqgcl ermrnsrhrl lnkyrqaags tpgtasdrll
       61 vqevmeeewa slqsvencpe allqlelpld lavlqdieqe lcnedl
//
LOCUS       NP_031386                216 aa            linear   PRI 27-APR-2025
DEFINITION  NKG2-D type II integral membrane protein [Homo sapiens].
ACCESSION   NP_031386
VERSION     NP_031386.2
DBSOURCE    REFSEQ: accession NM_007360.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Hartmann,J.A., Cardoso,M.R., Talarico,M.C.R., Kenney,D.J.,
            Leone,M.R., Reese,D.C., Turcinovic,J., O'Connell,A.K., Gertje,H.P.,
            Marino,C., Ojeda,P.E., De Paula,E.V., Orsi,F.A., Velloso,L.A.,
            Cafiero,T.R., Connor,J.H., Ploss,A., Hoelzemer,A., Carrington,M.,
            Barczak,A.K., Crossland,N.A., Douam,F., Boucau,J. and
            Garcia-Beltran,W.F.
  TITLE     Evasion of NKG2D-mediated cytotoxic immunity by sarbecoviruses
  JOURNAL   Cell 187 (10), 2393-2410 (2024)
   PUBMED   38653235
  REMARK    GeneRIF: Evasion of NKG2D-mediated cytotoxic immunity by
            sarbecoviruses.
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Ma,Y., Ping,D., Huang,K., Tao,Y., Peng,Y., Sun,X. and Liu,C.
  TITLE     Lower NKG2D expression in hepatic natural killer cells predicts
            poorer prognosis for chronic hepatitis B patients with cirrhosis
  JOURNAL   Hum Immunol 85 (3), 110775 (2024)
   PUBMED   38493049
  REMARK    GeneRIF: Lower NKG2D expression in hepatic natural killer cells
            predicts poorer prognosis for chronic hepatitis B patients with
            cirrhosis.
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Fernandez-Soto,D., Garcia-Jimenez,A.F., Casasnovas,J.M.,
            Vales-Gomez,M. and Reyburn,H.T.
  TITLE     Elevated levels of cell-free NKG2D-ligands modulate NKG2D surface
            expression and compromise NK cell function in severe COVID-19
            disease
  JOURNAL   Front Immunol 15, 1273942 (2024)
   PUBMED   38410511
  REMARK    GeneRIF: Elevated levels of cell-free NKG2D-ligands modulate NKG2D
            surface expression and compromise NK cell function in severe
            COVID-19 disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Raulet,D.H.
  TITLE     Roles of the NKG2D immunoreceptor and its ligands
  JOURNAL   Nat Rev Immunol 3 (10), 781-790 (2003)
   PUBMED   14523385
  REMARK    GeneRIF: NKG2D signalling enhances innate and adaptive immune
            responses (review)
            Review article
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Wu,J., Song,Y., Bakker,A.B., Bauer,S., Spies,T., Lanier,L.L. and
            Phillips,J.H.
  TITLE     An activating immunoreceptor complex formed by NKG2D and DAP10
  JOURNAL   Science 285 (5428), 730-732 (1999)
   PUBMED   10426994
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Bauer,S., Groh,V., Wu,J., Steinle,A., Phillips,J.H., Lanier,L.L.
            and Spies,T.
  TITLE     Activation of NK cells and T cells by NKG2D, a receptor for
            stress-inducible MICA
  JOURNAL   Science 285 (5428), 727-729 (1999)
   PUBMED   10426993
REFERENCE   7  (residues 1 to 216)
  AUTHORS   Glienke,J., Sobanov,Y., Brostjan,C., Steffens,C., Nguyen,C.,
            Lehrach,H., Hofer,E. and Francis,F.
  TITLE     The genomic organization of NKG2C, E, F, and D receptor genes in
            the human natural killer gene complex
  JOURNAL   Immunogenetics 48 (3), 163-173 (1998)
   PUBMED   9683661
REFERENCE   8  (residues 1 to 216)
  AUTHORS   Plougastel,B. and Trowsdale,J.
  TITLE     Sequence analysis of a 62-kb region overlapping the human KLRC
            cluster of genes
  JOURNAL   Genomics 49 (2), 193-199 (1998)
   PUBMED   9598306
REFERENCE   9  (residues 1 to 216)
  AUTHORS   Plougastel,B. and Trowsdale,J.
  TITLE     Cloning of NKG2-F, a new member of the NKG2 family of human natural
            killer cell receptor genes
  JOURNAL   Eur J Immunol 27 (11), 2835-2839 (1997)
   PUBMED   9394807
REFERENCE   10 (residues 1 to 216)
  AUTHORS   Houchins,J.P., Yabe,T., McSherry,C. and Bach,F.H.
  TITLE     DNA sequence analysis of NKG2, a family of related cDNA clones
            encoding type II integral membrane proteins on human natural killer
            cells
  JOURNAL   J Exp Med 173 (4), 1017-1020 (1991)
   PUBMED   2007850
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA933271.1, AK292059.1,
            AC022075.29 and CB241686.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 1, 2008 this sequence version replaced NP_031386.1.
            
            Summary: Natural killer (NK) cells are lymphocytes that can mediate
            lysis of certain tumor cells and virus-infected cells without
            previous activation. They can also regulate specific humoral and
            cell-mediated immunity. NK cells preferentially express several
            calcium-dependent (C-type) lectins, which have been implicated in
            the regulation of NK cell function. The NKG2 gene family is located
            within the NK complex, a region that contains several C-type lectin
            genes preferentially expressed in NK cells. This gene encodes a
            member of the NKG2 family. The encoded transmembrane protein is
            characterized by a type II membrane orientation (has an
            extracellular C terminus) and the presence of a C-type lectin
            domain. It binds to a diverse family of ligands that include MHC
            class I chain-related A and B proteins and UL-16 binding proteins,
            where ligand-receptor interactions can result in the activation of
            NK and T cells. The surface expression of these ligands is
            important for the recognition of stressed cells by the immune
            system, and thus this protein and its ligands are therapeutic
            targets for the treatment of immune diseases and cancers.
            Read-through transcription exists between this gene and the
            upstream KLRC4 (killer cell lectin-like receptor subfamily C,
            member 4) family member in the same cluster. [provided by RefSeq,
            Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC039836.1, AK292059.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000240618.11/ ENSP00000240618.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..216
                     /product="NKG2-D type II integral membrane protein"
                     /note="NK cell receptor D; NKG2-D-activating NK receptor;
                     killer cell lectin-like receptor subfamily K, member 1"
                     /calculated_mol_wt=25173
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26718.2)"
     Region          99..213
                     /region_name="CLECT_NK_receptors_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in natural killer cell receptors (NKRs); cd03593"
                     /db_xref="CDD:153063"
     Site            131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26718.2)"
     Site            order(152,179,197,199..200)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153063"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26718.2)"
     Site            202
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26718.2)"
     CDS             1..216
                     /gene="KLRK1"
                     /gene_synonym="CD314; D12S2489E; KLR; NKG2-D; NKG2D"
                     /coded_by="NM_007360.4:165..815"
                     /db_xref="GeneID:22914"
                     /db_xref="HGNC:HGNC:18788"
                     /db_xref="MIM:611817"
ORIGIN      
        1 mgwirgrrsr hswemsefhn ynldlkksdf strwqkqrcp vvkskcrena spfffccfia
       61 vamgirfiim vtiwsavfln slfnqevqip ltesycgpcp knwicyknnc yqffdesknw
      121 yesqascmsq nasllkvysk edqdllklvk syhwmglvhi ptngswqwed gsilspnllt
      181 iiemqkgdca lyassfkgyi encstpntyi cmqrtv
//
LOCUS       NP_002153                547 aa            linear   PRI 27-APR-2025
DEFINITION  intercellular adhesion molecule 3 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_002153
VERSION     NP_002153.2
DBSOURCE    REFSEQ: accession NM_002162.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Li,L., Yang,C., Aruna, Zhou,Q., Jiang,X., Du,W., Liu,C., Lv,P.,
            Wang,X., Fan,G., Zhao,S., Zhang,X., Jin,A. and Shen,W.
  TITLE     Functional evaluation of various ICAM3 transcript variants in
            diffuse large B-Cell lymphoma
  JOURNAL   Leuk Lymphoma 63 (12), 2869-2878 (2022)
   PUBMED   35849332
  REMARK    GeneRIF: Functional evaluation of various ICAM3 transcript variants
            in diffuse large B-Cell lymphoma.
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Zicheng,H., Xiao,Y., Rongzhong,H., Yongyong,L., Haitao,R. and
            Tingting,S.
  TITLE     Association of Circulating ICAM3 Concentrations with Severity and
            Short-term Outcomes of Acute Ischemic Stroke
  JOURNAL   Neurotox Res 39 (4), 1293-1299 (2021)
   PUBMED   33999358
  REMARK    GeneRIF: Association of Circulating ICAM3 Concentrations with
            Severity and Short-term Outcomes of Acute Ischemic Stroke.
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Pletsch-Borba,L., Grafetstatter,M., Husing,A., Johnson,T., Gonzalez
            Maldonado,S., Gross,M.L., Kloss,M., Hoffmeister,M., Bugert,P.,
            Kaaks,R. and Kuhn,T.
  TITLE     Vascular injury biomarkers and stroke risk: A population-based
            study
  JOURNAL   Neurology 94 (22), e2337-e2345 (2020)
   PUBMED   32371447
  REMARK    GeneRIF: Vascular injury biomarkers and stroke risk: A
            population-based study.
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 547)
  AUTHORS   Sokolovskaya,A., Korneeva,E., Zaichenko,D., Virus,E., Kolesov,D.,
            Moskovtsev,A. and Kubatiev,A.
  TITLE     Changes in the Surface Expression of Intercellular Adhesion
            Molecule 3, the Induction of Apoptosis, and the Inhibition of
            Cell-Cycle Progression of Human Multidrug-Resistant Jurkat/A4 Cells
            Exposed to a Random Positioning Machine
  JOURNAL   Int J Mol Sci 21 (3), 855 (2020)
   PUBMED   32013031
  REMARK    GeneRIF: Changes in the Surface Expression of Intercellular
            Adhesion Molecule 3, the Induction of Apoptosis, and the Inhibition
            of Cell-Cycle Progression of Human Multidrug-Resistant Jurkat/A4
            Cells Exposed to a Random Positioning Machine.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 547)
  AUTHORS   Pino-Otin,M.R., Juan,M., de la Fuente,M.A., Vinas,O.,
            Martinez-Caceres,E., Fernandez,M.D., Miralles,A., Vilella,R.,
            Yague,J., Vives,J. et al.
  TITLE     CD50 (intercellular adhesion molecule-3) is expressed at higher
            levels on memory than on naive human T cells but induces a similar
            calcium mobilization on both subsets
  JOURNAL   Tissue Antigens 46 (1), 32-44 (1995)
   PUBMED   7482494
REFERENCE   7  (residues 1 to 547)
  AUTHORS   Simmons,D.L.
  TITLE     The role of ICAM expression in immunity and disease
  JOURNAL   Cancer Surv 24, 141-155 (1995)
   PUBMED   7553659
  REMARK    Review article
REFERENCE   8  (residues 1 to 547)
  AUTHORS   Marazuela,M., Postigo,A.A., Acevedo,A., Diaz-Gonzalez,F.,
            Sanchez-Madrid,F. and de Landazuri,M.O.
  TITLE     Adhesion molecules from the LFA-1/ICAM-1,3 and VLA-4/VCAM-1
            pathways on T lymphocytes and vascular endothelium in Graves' and
            Hashimoto's thyroid glands
  JOURNAL   Eur J Immunol 24 (10), 2483-2490 (1994)
   PUBMED   7523142
REFERENCE   9  (residues 1 to 547)
  AUTHORS   Vazeux,R., Hoffman,P.A., Tomita,J.K., Dickinson,E.S., Jasman,R.L.,
            St John,T. and Gallatin,W.M.
  TITLE     Cloning and characterization of a new intercellular adhesion
            molecule ICAM-R
  JOURNAL   Nature 360 (6403), 485-488 (1992)
   PUBMED   1448174
REFERENCE   10 (residues 1 to 547)
  AUTHORS   Fawcett,J., Holness,C.L., Needham,L.A., Turley,H., Gatter,K.C.,
            Mason,D.Y. and Simmons,D.L.
  TITLE     Molecular cloning of ICAM-3, a third ligand for LFA-1,
            constitutively expressed on resting leukocytes
  JOURNAL   Nature 360 (6403), 481-484 (1992)
   PUBMED   1448173
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CR982084.1, AC114271.2,
            AK226023.1 and BC040123.1.
            
            On Feb 8, 2008 this sequence version replaced NP_002153.1.
            
            Summary: The protein encoded by this gene is a member of the
            intercellular adhesion molecule (ICAM) family. All ICAM proteins
            are type I transmembrane glycoproteins, contain 2-9
            immunoglobulin-like C2-type domains, and bind to the leukocyte
            adhesion LFA-1 protein. This protein is constitutively and
            abundantly expressed by all leucocytes and may be the most
            important ligand for LFA-1 in the initiation of the immune
            response. It functions not only as an adhesion molecule, but also
            as a potent signalling molecule. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.92873.1,
                                           SRR1163658.455224.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000160262.10/ ENSP00000160262.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..547
                     /product="intercellular adhesion molecule 3 isoform 1
                     precursor"
                     /note="ICAM-3"
                     /calculated_mol_wt=56412
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3147
     mat_peptide     30..547
                     /product="Intercellular adhesion molecule 3.
                     /id=PRO_0000014794"
                     /note="propagated from UniProtKB/Swiss-Prot (P32942.2)"
                     /calculated_mol_wt=56412
     Region          30..114
                     /region_name="IgI_N_ICAM-3"
                     /note="N-terminal immunoglobulin domain of the
                     intercellular adhesion molecules ICAM-3 (Cluster of
                     Differentiation 50 or CD50); member of the I-set of IgSF
                     domains; cd20997"
                     /db_xref="CDD:409589"
     Region          34..37
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409589"
     Region          40..43
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409589"
     Region          48..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409589"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15728350; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Region          61..66
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409589"
     Region          68..69
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409589"
     Region          71..77
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409589"
     Region          80..85
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409589"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Region          91..99
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409589"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Region          103..113
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409589"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15728350; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Region          117..211
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Region          135..139
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          151..155
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          173..177
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          187..192
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973;
                     propagated from UniProtKB/Swiss-Prot (P32942.2)"
     Region          207..210
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Region          317..396
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Site            320
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Site            363
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973;
                     propagated from UniProtKB/Swiss-Prot (P32942.2)"
     Site            389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Region          420..469
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          420..423
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          432..436
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            453
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Site            457
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32942.2)"
     Region          459..464
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            486..510
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32942.2)"
     CDS             1..547
                     /gene="ICAM3"
                     /gene_synonym="CD50; CDW50; ICAM-R"
                     /coded_by="NM_002162.5:11..1654"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12235.1"
                     /db_xref="GeneID:3385"
                     /db_xref="HGNC:HGNC:5346"
                     /db_xref="MIM:146631"
ORIGIN      
        1 matmvpsvlw pracwtllvc clltpgvqgq efllrvepqn pvlsaggslf vncstdcpss
       61 ekialetsls kelvasgmgw aafnlsnvtg nsrilcsvyc ngsqitgssn itvyrlperv
      121 elaplppwqp vgqnftlrcq vedgsprtsl tvvllrweee lsrqpaveep aevtatvlas
      181 rddhgapfsc rteldmqpqg lglfvntsap rqlrtfvlpv tpprlvaprf levetswpvd
      241 ctldglfpas eaqvylalgd qmlnatvmnh gdtltatata taradqegar eivcnvtlgg
      301 errearenlt vfsflgpivn lseptahegs tvtvscmaga rvqvtldgvp aaapgqpaql
      361 qlnatesddg rsffcsatle vdgeflhrns svqlrvlygp kidratcpqh lkwkdktrhv
      421 lqcqargnpy pelrclkegs srevpvgipf fvnvthngty qcqasssrgk ytlvvvmdie
      481 agsshfvpvf vavlltlgvv tivlalmyvf rehqrsgsyh vreestylpl tsmqpteamg
      541 eepsrae
//
LOCUS       NP_056982                584 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 7A [Homo sapiens].
ACCESSION   NP_056982
VERSION     NP_056982.1
DBSOURCE    REFSEQ: accession NM_015898.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Kambe,G., Kobayashi,M., Ishikita,H., Koyasu,S., Hammond,E.M. and
            Harada,H.
  TITLE     ZBTB7A forms a heterodimer with ZBTB2 and inhibits ZBTB2
            homodimerization required for full activation of HIF-1
  JOURNAL   Biochem Biophys Res Commun 733, 150604 (2024)
   PUBMED   39197198
  REMARK    GeneRIF: ZBTB7A forms a heterodimer with ZBTB2 and inhibits ZBTB2
            homodimerization required for full activation of HIF-1.
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Wang,Y., Zeng,H., Li,L., Liu,J., Lin,J., Bie,Y., Wang,S., Cheng,X.,
            Nashun,B., Yao,Y., Hu,X. and Zhao,Y.
  TITLE     Pokemon inhibits Bim transcription to promote the proliferation,
            anti-anoikis, invasion, histological grade, and dukes stage of
            colorectal neoplasms
  JOURNAL   J Cancer Res Clin Oncol 150 (8), 380 (2024)
   PUBMED   39095579
  REMARK    GeneRIF: Pokemon inhibits Bim transcription to promote the
            proliferation, anti-anoikis, invasion, histological grade, and
            dukes stage of colorectal neoplasms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Athanasopoulou,K., Chondrou,V., Xiropotamos,P., Psarias,G.,
            Vasilopoulos,Y., Georgakilas,G.K. and Sgourou,A.
  TITLE     Transcriptional repression of lncRNA and miRNA subsets mediated by
            LRF during erythropoiesis
  JOURNAL   J Mol Med (Berl) 101 (9), 1097-1112 (2023)
   PUBMED   37486375
  REMARK    GeneRIF: Transcriptional repression of lncRNA and miRNA subsets
            mediated by LRF during erythropoiesis.
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Chang,H., Sun,W., Zhao,Y., Sun,T. and Zhao,Z.
  TITLE     Targeting Pokemon is a novel strategy to suppress cancer
            aggressiveness of non-small cell lung cancer: Identification of
            Pokemon as ideal target for developing anti-NSCLC drugs
  JOURNAL   Arch Biochem Biophys 742, 109637 (2023)
   PUBMED   37182800
  REMARK    GeneRIF: Targeting Pokemon is a novel strategy to suppress cancer
            aggressiveness of non-small cell lung cancer: Identification of
            Pokemon as ideal target for developing anti-NSCLC drugs.
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Bae,S.Y., Bergom,H.E., Day,A., Greene,J.T., Sychev,Z.E., Larson,G.,
            Corey,E., Plymate,S.R., Freedman,T.S., Hwang,J.H. and Drake,J.M.
  TITLE     ZBTB7A as a novel vulnerability in neuroendocrine prostate cancer
  JOURNAL   Front Endocrinol (Lausanne) 14, 1093332 (2023)
   PUBMED   37065756
  REMARK    GeneRIF: ZBTB7A as a novel vulnerability in neuroendocrine prostate
            cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Pessler,F. and Hernandez,N.
  TITLE     Flexible DNA binding of the BTB/POZ-domain protein FBI-1
  JOURNAL   J Biol Chem 278 (31), 29327-29335 (2003)
   PUBMED   12750370
  REMARK    GeneRIF: found that FBI-1 binds to inverted sequence repeats
            downstream of the HIV-1 transcription start site
REFERENCE   7  (residues 1 to 584)
  AUTHORS   Lee,D.K., Suh,D., Edenberg,H.J. and Hur,M.W.
  TITLE     POZ domain transcription factor, FBI-1, represses transcription of
            ADH5/FDH by interacting with the zinc finger and interfering with
            DNA binding activity of Sp1
  JOURNAL   J Biol Chem 277 (30), 26761-26768 (2002)
   PUBMED   12004059
  REMARK    GeneRIF: POZ domain of FBI1 represses transcription of ADH5.
REFERENCE   8  (residues 1 to 584)
  AUTHORS   Pendergrast,P.S., Wang,C., Hernandez,N. and Huang,S.
  TITLE     FBI-1 can stimulate HIV-1 Tat activity and is targeted to a novel
            subnuclear domain that includes the Tat-P-TEFb-containing nuclear
            speckles
  JOURNAL   Mol Biol Cell 13 (3), 915-929 (2002)
   PUBMED   11907272
  REMARK    GeneRIF: Results suggest that FBI-1 is a cellular factor that
            preferentially associates with active chromatin and that can
            specifically stimulate Tat-activated HIV-1 transcription.
REFERENCE   9  (residues 1 to 584)
  AUTHORS   Morrison,D.J., Pendergrast,P.S., Stavropoulos,P., Colmenares,S.U.,
            Kobayashi,R. and Hernandez,N.
  TITLE     FBI-1, a factor that binds to the HIV-1 inducer of short
            transcripts (IST), is a POZ domain protein
  JOURNAL   Nucleic Acids Res 27 (5), 1251-1262 (1999)
   PUBMED   9973611
REFERENCE   10 (residues 1 to 584)
  AUTHORS   Davies,J.M., Hawe,N., Kabarowski,J., Huang,Q.H., Zhu,J.,
            Brand,N.J., Leprince,D., Dhordain,P., Cook,M., Morriss-Kay,G. and
            Zelent,A.
  TITLE     Novel BTB/POZ domain zinc-finger protein, LRF, is a potential
            target of the LAZ-3/BCL-6 oncogene
  JOURNAL   Oncogene 18 (2), 365-375 (1999)
   PUBMED   9927193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC016586.9 and BC084568.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.474873.1, AF000561.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322357.9/ ENSP00000323670.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..584
                     /product="zinc finger and BTB domain-containing protein
                     7A"
                     /note="zinc finger and BTB domain containing 7A, HIV-1
                     inducer of short transcripts binding protein; lymphoma
                     related factor; HIV-1 1st-binding protein 1;
                     TTF-I-interacting peptide 21; factor binding IST protein
                     1; leukemia/lymphoma-related factor; POK erythroid myeloid
                     ontogenic factor; pokemon 1; POZ and Krueppel erythroid
                     myeloid ontogenic factor; factor that binds to inducer of
                     short transcripts protein 1; zinc finger protein 857A"
                     /calculated_mol_wt=61308
     Region          9..128
                     /region_name="BTB_POZ_ZBTB7A"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 7A (ZBTB7A); cd18326"
                     /db_xref="CDD:349635"
     Site            order(9..13,16..18,20..21,24,27,33,48,50,53..54,63..64,
                     91..92,95..100,118,122)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349635"
     Region          220..313
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95365.1)"
     Region          277..584
                     /region_name="Mediates interaction with KHDRBS1.
                     /evidence=ECO:0000269|PubMed:24514149"
                     /note="propagated from UniProtKB/Swiss-Prot (O95365.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95365.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O95365.1)"
     Region          349..584
                     /region_name="Mediates interaction with RELA.
                     /evidence=ECO:0000250|UniProtKB:O88939"
                     /note="propagated from UniProtKB/Swiss-Prot (O95365.1)"
     Region          377..584
                     /region_name="Mediates interaction with SMAD4.
                     /evidence=ECO:0000269|PubMed:25514493"
                     /note="propagated from UniProtKB/Swiss-Prot (O95365.1)"
     Region          384..404
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          399..421
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          412..432
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(417,419,421,423..424,427..428,431,445,447,451..452,
                     455..456,459,473,475,477,479..480,483..484)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          425..449
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          440..460
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          452..477
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          468..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          486..584
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95365.1)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O95365.1)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O95365.1)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O95365.1)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95365.1)"
     CDS             1..584
                     /gene="ZBTB7A"
                     /gene_synonym="FBI-1; FBI1; LRF; MNDLFH; pokemon; TIP21;
                     ZBTB7; ZNF857A"
                     /coded_by="NM_015898.4:234..1988"
                     /db_xref="CCDS:CCDS12119.1"
                     /db_xref="GeneID:51341"
                     /db_xref="HGNC:HGNC:18078"
                     /db_xref="MIM:605878"
ORIGIN      
        1 maggvdgpig ipfpdhssdi lsglneqrtq gllcdvvilv egrefpthrs vlaacsqyfk
       61 klftsgavvd qqnvyeidfv saealtalmd faytatltvs tanvgdilsa arlleipavs
      121 hvcadlldrq ilaadagada gqldlvdqid qrnllrakey leffqsnpmn slppaaaaaa
      181 asfpwsafga sdddldatke avaaavaava agdcngldfy gpgppaerpp tgdgdegdsn
      241 pglwperded aptgglfppp vappaatqng hygrggeeea aslseaapep gdspgflsga
      301 aegedgdgpd vdglaastll qqmmssvgra gaaagdsdee sraddkgvmd yylkyfsgah
      361 dgdvypawsq kvekkiraka fqkcpicekv iqgagklprh irthtgekpy ecnickvrft
      421 rqdklkvhmr khtgekpylc qqcgaafahn ydlknhmrvh tglrpyqcds ccktfvrsdh
      481 lhrhlkkdgc ngvpsrrgrk prvrggapdp spgatatpga paqpsspdar rngqekhfkd
      541 edededvasp dglgrlnvag aggggdsggg pgaatdgnft agla
//
LOCUS       NP_001347225             687 aa            linear   PLN 27-APR-2025
DEFINITION  sulfite reductase [ferredoxin], chloroplastic [Glycine max].
ACCESSION   NP_001347225 XP_003537728
VERSION     NP_001347225.1
DBSOURCE    REFSEQ: accession NM_001360296.1
KEYWORDS    RefSeq.
SOURCE      Glycine max (soybean)
  ORGANISM  Glycine max
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
            Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50
            kb inversion clade; NPAAA clade; indigoferoid/millettioid clade;
            Phaseoleae; Glycine; Glycine subgen. Soja.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Chi-Ham,C.L., Keaton,M.A., Cannon,G.C. and Heinhorst,S.
  TITLE     The DNA-compacting protein DCP68 from soybean chloroplasts is
            ferredoxin:sulfite reductase and co-localizes with the organellar
            nucleoid
  JOURNAL   Plant Mol Biol 49 (6), 621-631 (2002)
   PUBMED   12081370
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Cannon,G.C., Ward,L.N., Case,C.I. and Heinhorst,S.
  TITLE     The 68 kDa DNA compacting nucleoid protein from soybean
            chloroplasts inhibits DNA synthesis in vitro
  JOURNAL   Plant Mol Biol 39 (4), 835-845 (1999)
   PUBMED   10350096
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FG988540.1, AY017473.1, CK768707.1 and CX548422.1.
            
            On Jan 31, 2018 this sequence version replaced XP_003537728.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN09064557,
                              SAMN09064558 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Glycine max"
                     /cultivar="Williams 82"
                     /db_xref="taxon:3847"
                     /chromosome="11"
                     /map="11"
     Protein         1..687
                     /product="sulfite reductase [ferredoxin], chloroplastic"
                     /EC_number="1.8.7.1"
                     /note="Nucleoid DNA-compacting protein of 68 kDa"
                     /calculated_mol_wt=71632
     transit_peptide 1..54
                     /note="Chloroplast. /evidence=ECO:0000269|PubMed:12081370;
                     propagated from UniProtKB/Swiss-Prot (Q9AWB2.1)"
                     /calculated_mol_wt=5650
     Region          23..638
                     /region_name="PLN00178"
                     /note="sulfite reductase"
                     /db_xref="CDD:177773"
     CDS             1..687
                     /gene="SIR"
                     /gene_synonym="DCP68; GmSIR"
                     /coded_by="NM_001360296.1:106..2169"
                     /db_xref="GeneID:547693"
ORIGIN      
        1 mttsfgpatt saplkdhkvq ipsfhglrss sasalprnal slpsstrsls liravstpaq
       61 setatvkrsk veifkeqsnf iryplnedil tdapniseaa tqlikfhgsy qqynreergs
      121 rsysfmirtk npcgkvsnql yltmddladq fgigtlrltt rqtfqlhgvl kkdlktvmgt
      181 iirnmgstlg acgdlnrnvl apaaplarkd ylfaqqtaen iaallapqsg fyydiwvdge
      241 kiltseppev vqarndnshg tnfpdspepi ygtqflprkf kiavtvptdn svdiltndig
      301 vvvvtdddge pqgfniyvgg gmgrthrlet tfprlaepig yvpkedilya vkaivvtqre
      361 ngrrddrkys rlkylisswg iekfrsvveq yygkkfepfr alpewefksy lgwheqgdgk
      421 lfyglhvdng riggnmkktl reviekynln vritpnqnii ltdvraawkr pitttlaqag
      481 llqprfvdpl nitamacpaf plcplaitea ergipnilkr irdvfdkvgl kysesvvvri
      541 tgcpngcarp ymaelglvgd gpnsyqiwlg gnhkqtslar sfmdrvkild lekvleplfy
      601 ywkqkrqske sfgdftnrmg feklkeyiek wegpvvapsr hnlklfadke tyesmdalak
      661 lqnktahqla mevirnyvas nqngkge
//
LOCUS       NP_001355695             248 aa            linear   ROD 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 45 isoform 2 [Mus
            musculus].
ACCESSION   NP_001355695
VERSION     NP_001355695.1
DBSOURCE    REFSEQ: accession NM_001368766.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138640.7.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.26782.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 69.75 cM"
     Protein         1..248
                     /product="ankyrin repeat domain-containing protein 45
                     isoform 2"
                     /note="ankyrin repeat domain-containing protein 45"
                     /calculated_mol_wt=27603
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810N6.1)"
     Region          <62..207
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          75..104
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810N6.1)"
     Region          76..106
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(77,81..82,85..87,89..90,94,97,106,108,110,114..115,
                     118..120,122..123,127,130,139,141,143,147..148,151..153,
                     155..156,160)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          108..139
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          108..137
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810N6.1)"
     Region          <185..239
                     /region_name="PTZ00009"
                     /note="heat shock 70 kDa protein; Provisional"
                     /db_xref="CDD:240227"
     CDS             1..248
                     /gene="Ankrd45"
                     /gene_synonym="4933409K03Rik"
                     /coded_by="NM_001368766.1:106..852"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS87902.1"
                     /db_xref="GeneID:73844"
                     /db_xref="MGI:MGI:1921094"
ORIGIN      
        1 mepeetlese ssekslfssq qeyeesqeae etgaenpllq ptltgdvegl qkifedpehp
       61 hhehavqlll eedivgrnll yaacmagksd vikalakygv nlneatargy tllhcaaawg
      121 rletlkalve ldvdiealnf rgekardvaa rysqvecvnf ldwadarlil kkiitkssli
      181 itdpekgpgk lfkedkstil nacrlknewl eshpeasise ifeqkqqled ivspilakms
      241 tprhfaas
//
LOCUS       NP_620416                533 aa            linear   PRI 27-APR-2025
DEFINITION  neuropilin and tolloid-like protein 1 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_620416
VERSION     NP_620416.2
DBSOURCE    REFSEQ: accession NM_138966.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Xu,Y., Wang,W., Chen,J., Mao,H., Liu,Y., Gu,S., Liu,Q., Xi,Q. and
            Shi,W.
  TITLE     High neuropilin and tolloid-like 1 expression associated with
            metastasis and poor survival in epithelial ovarian cancer via
            regulation of actin cytoskeleton
  JOURNAL   J Cell Mol Med 24 (16), 9114-9124 (2020)
   PUBMED   32638511
  REMARK    GeneRIF: High neuropilin and tolloid-like 1 expression associated
            with metastasis and poor survival in epithelial ovarian cancer via
            regulation of actin cytoskeleton.
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Orav,E., Atanasova,T., Shintyapina,A., Kesaf,S., Kokko,M.,
            Partanen,J., Taira,T. and Lauri,S.E.
  TITLE     NETO1 Guides Development of Glutamatergic Connectivity in the
            Hippocampus by Regulating Axonal Kainate Receptors
  JOURNAL   eNeuro 4 (3) (2017)
   PUBMED   28680963
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Sheng,N., Shi,Y.S. and Nicoll,R.A.
  TITLE     Amino-terminal domains of kainate receptors determine the
            differential dependence on Neto auxiliary subunits for trafficking
  JOURNAL   Proc Natl Acad Sci U S A 114 (5), 1159-1164 (2017)
   PUBMED   28100490
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Li,B., Rex,E., Wang,H., Qian,Y., Ogden,A.M., Bleakman,D. and
            Johnson,K.W.
  TITLE     Pharmacological Modulation of GluK1 and GluK2 by NETO1, NETO2, and
            PSD95
  JOURNAL   Assay Drug Dev Technol 14 (2), 131-143 (2016)
   PUBMED   26991362
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Fisher,J.L.
  TITLE     The auxiliary subunits Neto1 and Neto2 have distinct,
            subunit-dependent effects at recombinant GluK1- and
            GluK2-containing kainate receptors
  JOURNAL   Neuropharmacology 99, 471-480 (2015)
   PUBMED   26277340
  REMARK    GeneRIF: Results suggested that the extracellular N-terminal region
            including the two CUB domains was largely responsible for the
            distinct regulatory effects of Neto1 and Neto2 on the
            desensitization properties of GluK1 homomeric receptors
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Tang,M., Pelkey,K.A., Ng,D., Ivakine,E., McBain,C.J., Salter,M.W.
            and McInnes,R.R.
  TITLE     Neto1 is an auxiliary subunit of native synaptic kainate receptors
  JOURNAL   J Neurosci 31 (27), 10009-10018 (2011)
   PUBMED   21734292
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Straub,C., Hunt,D.L., Yamasaki,M., Kim,K.S., Watanabe,M.,
            Castillo,P.E. and Tomita,S.
  TITLE     Distinct functions of kainate receptors in the brain are determined
            by the auxiliary subunit Neto1
  JOURNAL   Nat Neurosci 14 (7), 866-873 (2011)
   PUBMED   21623363
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 533)
  AUTHORS   O'Donnell,L., Soileau,B., Heard,P., Carter,E., Sebold,C.,
            Gelfond,J., Hale,D.E. and Cody,J.D.
  TITLE     Genetic determinants of autism in individuals with deletions of 18q
  JOURNAL   Hum Genet 128 (2), 155-164 (2010)
   PUBMED   20499253
REFERENCE   9  (residues 1 to 533)
  AUTHORS   Ng,D., Pitcher,G.M., Szilard,R.K., Sertie,A., Kanisek,M.,
            Clapcote,S.J., Lipina,T., Kalia,L.V., Joo,D., McKerlie,C.,
            Cortez,M., Roder,J.C., Salter,M.W. and McInnes,R.R.
  TITLE     Neto1 is a novel CUB-domain NMDA receptor-interacting protein
            required for synaptic plasticity and learning
  JOURNAL   PLoS Biol 7 (2), e41 (2009)
   PUBMED   19243221
  REMARK    GeneRIF: Mouse neto1 plays a critical role in spatial learning and
            memory through the regulation of NMDAR subunit abundance at
            synapses.
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Stohr,H., Berger,C., Frohlich,S. and Weber,B.H.
  TITLE     A novel gene encoding a putative transmembrane protein with two
            extracellular CUB domains and a low-density lipoprotein class A
            module: isolation of alternatively spliced isoforms in retina and
            brain
  JOURNAL   Gene 286 (2), 223-231 (2002)
   PUBMED   11943477
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091138.6 and AC023301.5.
            
            On Nov 23, 2018 this sequence version replaced NP_620416.1.
            
            Summary: This gene encodes a transmembrane protein containing two
            extracellular CUB domains followed by a low-density lipoprotein
            class A (LDLa) domain. This protein is thought to play a critical
            role in spatial learning and memory by regulating the function of
            synaptic N-methyl-D-aspartic acid receptor complexes in the
            hippocampus. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Aug 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.156901.1, AF448838.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327305.11/ ENSP00000313088.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q22.3"
     Protein         1..533
                     /product="neuropilin and tolloid-like protein 1 isoform 3
                     precursor"
                     /note="neuropilin and tolloid-like protein 1;
                     brain-specific transmembrane protein containing 2 CUB and
                     1 LDL-receptor class A domains protein 1; neuropilin (NRP)
                     and tolloid (TLL)-like 1"
                     /calculated_mol_wt=57872
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2338
     mat_peptide     23..533
                     /product="Neuropilin and tolloid-like protein 1.
                     /id=PRO_0000021799"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDF5.2)"
                     /calculated_mol_wt=57872
     Region          51..154
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(52,54,81,86,125,149,151,153..154)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          <200..286
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Region          292..326
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(297,305,316..317)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            306
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDF5.2)"
     Site            order(309,312,316,322..323)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            319..323
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDF5.2)"
     Site            345..365
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDF5.2)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8R4I7; propagated from
                     UniProtKB/Swiss-Prot (Q8TDF5.2)"
     Region          531..533
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDF5.2)"
     CDS             1..533
                     /gene="NETO1"
                     /gene_synonym="BCTL1; BTCL1"
                     /coded_by="NM_138966.5:697..2298"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS12000.1"
                     /db_xref="GeneID:81832"
                     /db_xref="HGNC:HGNC:13823"
                     /db_xref="MIM:607973"
ORIGIN      
        1 mihgrsvlhi vasliilhls gatkkgtekq ttsetqksvq cgtwtkhaeg giftspnyps
       61 kyppdreciy iieaaprqci elyfdekysi epsweckfdh ievrdgpfgf spiigrfcgq
      121 qnppvikssg rflwikffad gelesmgfsa rynftpdpdf kdlgalkplp acefemggse
      181 givesiqimk egkataseav dckwyirapp rskiylrfld yemqnsneck rnfvavydgs
      241 ssvedlkakf cstvandvml rtglgvirmw adegsrnsrf qmlftsfqep pcegntffch
      301 snmcinntlv cnglqncvyp wdenhckekr ktslldqltn tsgtvigvts civiiliiis
      361 vivqikqprk kyvqrksdfd qtvfqevfep phyelctlrg tgatadfadv addfenyhkl
      421 rrssskcihd hhcgsqlsst kgsrsnlstr dasiltempt qpgkplippm nrrnilvmkh
      481 sysqdaadac dideieevpt tshrlsrhdk avqrfcligs lskheseynt trv
//
LOCUS       NP_078975                268 aa            linear   PRI 27-APR-2025
DEFINITION  AN1-type zinc finger protein 1 isoform a [Homo sapiens].
ACCESSION   NP_078975
VERSION     NP_078975.2
DBSOURCE    REFSEQ: accession NM_024699.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Lai,C.H., Ko,K.T., Fan,P.J., Yu,T.A., Chang,C.F., Draczkowski,P.
            and Hsu,S.D.
  TITLE     Structural insight into the ZFAND1-p97 interaction involved in
            stress granule clearance
  JOURNAL   J Biol Chem 300 (5), 107230 (2024)
   PUBMED   38537699
  REMARK    GeneRIF: Structural insight into the ZFAND1-p97 interaction
            involved in stress granule clearance.
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Turakhiya,A., Meyer,S.R., Marincola,G., Bohm,S., Vanselow,J.T.,
            Schlosser,A., Hofmann,K. and Buchberger,A.
  TITLE     ZFAND1 Recruits p97 and the 26S Proteasome to Promote the Clearance
            of Arsenite-Induced Stress Granules
  JOURNAL   Mol Cell 70 (5), 906-919 (2018)
   PUBMED   29804830
  REMARK    GeneRIF: By recruiting the 26S proteasome and the
            ubiquitin-selective ATPase p97 to arsenite-induced stress granules,
            ZFAND1 ensures their timely clearance and prevents their
            aberration.
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Sa-Moura,B., Funakoshi,M., Tomko,R.J. Jr., Dohmen,R.J., Wu,Z.,
            Peng,J. and Hochstrasser,M.
  TITLE     A conserved protein with AN1 zinc finger and ubiquitin-like domains
            modulates Cdc48 (p97) function in the ubiquitin-proteasome pathway
  JOURNAL   J Biol Chem 288 (47), 33682-33696 (2013)
   PUBMED   24121501
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Pharoah,P.D., Tsai,Y.Y., Ramus,S.J., Phelan,C.M., Goode,E.L.,
            Lawrenson,K., Buckley,M., Fridley,B.L., Tyrer,J.P., Shen,H.,
            Weber,R., Karevan,R., Larson,M.C., Song,H., Tessier,D.C., Bacot,F.,
            Vincent,D., Cunningham,J.M., Dennis,J., Dicks,E., Aben,K.K.,
            Anton-Culver,H., Antonenkova,N., Armasu,S.M., Baglietto,L.,
            Bandera,E.V., Beckmann,M.W., Birrer,M.J., Bloom,G., Bogdanova,N.,
            Brenton,J.D., Brinton,L.A., Brooks-Wilson,A., Brown,R., Butzow,R.,
            Campbell,I., Carney,M.E., Carvalho,R.S., Chang-Claude,J.,
            Chen,Y.A., Chen,Z., Chow,W.H., Cicek,M.S., Coetzee,G., Cook,L.S.,
            Cramer,D.W., Cybulski,C., Dansonka-Mieszkowska,A., Despierre,E.,
            Doherty,J.A., Dork,T., du Bois,A., Durst,M., Eccles,D., Edwards,R.,
            Ekici,A.B., Fasching,P.A., Fenstermacher,D., Flanagan,J., Gao,Y.T.,
            Garcia-Closas,M., Gentry-Maharaj,A., Giles,G., Gjyshi,A., Gore,M.,
            Gronwald,J., Guo,Q., Halle,M.K., Harter,P., Hein,A., Heitz,F.,
            Hillemanns,P., Hoatlin,M., Hogdall,E., Hogdall,C.K., Hosono,S.,
            Jakubowska,A., Jensen,A., Kalli,K.R., Karlan,B.Y., Kelemen,L.E.,
            Kiemeney,L.A., Kjaer,S.K., Konecny,G.E., Krakstad,C.,
            Kupryjanczyk,J., Lambrechts,D., Lambrechts,S., Le,N.D., Lee,N.,
            Lee,J., Leminen,A., Lim,B.K., Lissowska,J., Lubinski,J.,
            Lundvall,L., Lurie,G., Massuger,L.F., Matsuo,K., McGuire,V.,
            McLaughlin,J.R., Menon,U., Modugno,F., Moysich,K.B., Nakanishi,T.,
            Narod,S.A., Ness,R.B., Nevanlinna,H., Nickels,S., Noushmehr,H.,
            Odunsi,K., Olson,S., Orlow,I., Paul,J., Pejovic,T., Pelttari,L.M.,
            Permuth-Wey,J., Pike,M.C., Poole,E.M., Qu,X., Risch,H.A.,
            Rodriguez-Rodriguez,L., Rossing,M.A., Rudolph,A., Runnebaum,I.,
            Rzepecka,I.K., Salvesen,H.B., Schwaab,I., Severi,G., Shen,H.,
            Shridhar,V., Shu,X.O., Sieh,W., Southey,M.C., Spellman,P.,
            Tajima,K., Teo,S.H., Terry,K.L., Thompson,P.J., Timorek,A.,
            Tworoger,S.S., van Altena,A.M., van den Berg,D., Vergote,I.,
            Vierkant,R.A., Vitonis,A.F., Wang-Gohrke,S., Wentzensen,N.,
            Whittemore,A.S., Wik,E., Winterhoff,B., Woo,Y.L., Wu,A.H.,
            Yang,H.P., Zheng,W., Ziogas,A., Zulkifli,F., Goodman,M.T., Hall,P.,
            Easton,D.F., Pearce,C.L., Berchuck,A., Chenevix-Trench,G.,
            Iversen,E., Monteiro,A.N., Gayther,S.A., Schildkraut,J.M. and
            Sellers,T.A.
  CONSRTM   Australian Cancer Study; Australian Ovarian Cancer Study Group
  TITLE     GWAS meta-analysis and replication identifies three new
            susceptibility loci for ovarian cancer
  JOURNAL   Nat Genet 45 (4), 362-370 (2013)
   PUBMED   23535730
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ427843.1, BC022251.2, AC132219.3 and BU678501.1.
            
            On Jan 1, 2010 this sequence version replaced NP_078975.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.63941.1,
                                           SRR1803614.277179.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000220669.10/ ENSP00000220669.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.13"
     Protein         1..268
                     /product="AN1-type zinc finger protein 1 isoform a"
                     /EC_number="3.1.3.25"
                     /note="AN1-type zinc finger protein 1; zinc finger
                     AN1-type-containing protein 1; zinc finger, AN1-type
                     domain 1"
                     /calculated_mol_wt=30656
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:37316325; propagated from
                     UniProtKB/Swiss-Prot (Q8TCF1.1)"
     Region          10..46
                     /region_name="zf-AN1"
                     /note="AN1-like Zinc finger; pfam01428"
                     /db_xref="CDD:460208"
     Region          64..100
                     /region_name="zf-AN1"
                     /note="AN1-like Zinc finger; pfam01428"
                     /db_xref="CDD:460208"
     Region          160..260
                     /region_name="ubiquitin-like.
                     /evidence=ECO:0000303|PubMed:29804830"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCF1.1)"
     CDS             1..268
                     /gene="ZFAND1"
                     /coded_by="NM_024699.3:20..826"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6232.1"
                     /db_xref="GeneID:79752"
                     /db_xref="HGNC:HGNC:25858"
ORIGIN      
        1 maeldigqhc qvehcrqrdf lpfvcddcsg ifclehrsre shgcpevtvi nerlktdqht
       61 sypcsfkdca erelvavicp yceknfclrh rhqsdhecek leipkprmaa tqklvkdiid
      121 sktgetaskr wkgaknseta akvalmklkm hadgdkslpq teriyfqvfl pkgskekskp
      181 mffchrwsig kaidfaasla rlkndnnkft akklrlchit sgealpldht letwiakedc
      241 plynggniil eylndeeqfc knvesyle
//
LOCUS       NP_055938               1034 aa            linear   PRI 27-APR-2025
DEFINITION  FERM domain-containing protein 4B [Homo sapiens].
ACCESSION   NP_055938 XP_001134464 XP_114303
VERSION     NP_055938.2
DBSOURCE    REFSEQ: accession NM_015123.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Pieragostino,D., Agnifili,L., Fasanella,V., D'Aguanno,S.,
            Mastropasqua,R., Di Ilio,C., Sacchetta,P., Urbani,A. and Del
            Boccio,P.
  TITLE     Shotgun proteomics reveals specific modulated protein patterns in
            tears of patients with primary open angle glaucoma naive to therapy
  JOURNAL   Mol Biosyst 9 (6), 1108-1116 (2013)
   PUBMED   23580065
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Matkovich,S.J., Van Booven,D.J., Cappola,T.P. and Dorn,G.W. 2nd.
  TITLE     Association of an intronic, but not any exonic, FRMD4B sequence
            variant and heart failure
  JOURNAL   Clin Transl Sci 3 (4), 134-139 (2010)
   PUBMED   20718813
  REMARK    GeneRIF: association between the intronic rs6787362 FRMD4B SNP and
            ischemic cardiomyopathy in a European-derived population, but not
            FRMD4B variants as susceptibility factors in common heart failure
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 1034)
  AUTHORS   Dubois,P.C., Trynka,G., Franke,L., Hunt,K.A., Romanos,J.,
            Curtotti,A., Zhernakova,A., Heap,G.A., Adany,R., Aromaa,A.,
            Bardella,M.T., van den Berg,L.H., Bockett,N.A., de la Concha,E.G.,
            Dema,B., Fehrmann,R.S., Fernandez-Arquero,M., Fiatal,S.,
            Grandone,E., Green,P.M., Groen,H.J., Gwilliam,R., Houwen,R.H.,
            Hunt,S.E., Kaukinen,K., Kelleher,D., Korponay-Szabo,I., Kurppa,K.,
            MacMathuna,P., Maki,M., Mazzilli,M.C., McCann,O.T., Mearin,M.L.,
            Mein,C.A., Mirza,M.M., Mistry,V., Mora,B., Morley,K.I.,
            Mulder,C.J., Murray,J.A., Nunez,C., Oosterom,E., Ophoff,R.A.,
            Polanco,I., Peltonen,L., Platteel,M., Rybak,A., Salomaa,V.,
            Schweizer,J.J., Sperandeo,M.P., Tack,G.J., Turner,G., Veldink,J.H.,
            Verbeek,W.H., Weersma,R.K., Wolters,V.M., Urcelay,E., Cukrowska,B.,
            Greco,L., Neuhausen,S.L., McManus,R., Barisani,D., Deloukas,P.,
            Barrett,J.C., Saavalainen,P., Wijmenga,C. and van Heel,D.A.
  TITLE     Multiple common variants for celiac disease influencing immune gene
            expression
  JOURNAL   Nat Genet 42 (4), 295-302 (2010)
   PUBMED   20190752
  REMARK    Erratum:[Nat Genet.2010 May;42(5):465]
REFERENCE   5  (residues 1 to 1034)
  AUTHORS   Cappola,T.P., Li,M., He,J., Ky,B., Gilmore,J., Qu,L., Keating,B.,
            Reilly,M., Kim,C.E., Glessner,J., Frackelton,E., Hakonarson,H.,
            Syed,F., Hindes,A., Matkovich,S.J., Cresci,S. and Dorn,G.W. 2nd.
  TITLE     Common variants in HSPB7 and FRMD4B associated with advanced heart
            failure
  JOURNAL   Circ Cardiovasc Genet 3 (2), 147-154 (2010)
   PUBMED   20124441
  REMARK    GeneRIF: SNP is located in a 3' intronic region of the FRMD4B gene.
            FRMD4B as novel susceptibility loci for advanced heart failure.
REFERENCE   6  (residues 1 to 1034)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1034)
  AUTHORS   Kiel,D.P., Demissie,S., Dupuis,J., Lunetta,K.L., Murabito,J.M. and
            Karasik,D.
  TITLE     Genome-wide association with bone mass and geometry in the
            Framingham Heart Study
  JOURNAL   BMC Med Genet 8 Suppl 1 (Suppl 1), S14 (2007)
   PUBMED   17903296
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1034)
  AUTHORS   Klarlund,J.K., Holik,J., Chawla,A., Park,J.G., Buxton,J. and
            Czech,M.P.
  TITLE     Signaling complexes of the FERM domain-containing protein GRSP1
            bound to ARF exchange factor GRP1
  JOURNAL   J Biol Chem 276 (43), 40065-40070 (2001)
   PUBMED   11445584
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135851.1 and AC112221.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_055938.1.
            
            Summary: This gene encodes a GRP1-binding protein which contains a
            FERM protein interaction domain as well as two coiled coil domains.
            This protein may play a role as a scaffolding protein. [provided by
            RefSeq, Mar 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.108962.1,
                                           SRR1803612.254213.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398540.8/ ENSP00000381549.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.1"
     Protein         1..1034
                     /product="FERM domain-containing protein 4B"
                     /note="GRP1-binding protein GRSP1"
                     /calculated_mol_wt=117916
     Region          57..145
                     /region_name="FERM_F1_FRMD4B"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in FERM domain-containing
                     protein 4B (FRMD4B); cd17200"
                     /db_xref="CDD:340720"
     Region          75..260
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          256..366
                     /region_name="FERM_C_FRMD4A_FRMD4B"
                     /note="FERM domain C-lobe of FERM domain-containing
                     protein 4A and 4B (FRMD4A and 4B); cd13191"
                     /db_xref="CDD:270012"
     Site            order(264,281,283,292)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270012"
     Site            order(296,301..304,347,351,354..355)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270012"
     Site            347..358
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270012"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q920B0; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     Region          395..529
                     /region_name="CUPID"
                     /note="Cytohesin Ubiquitin Protein Inducing Domain;
                     pfam11819"
                     /db_xref="CDD:463360"
     Region          542..971
                     /region_name="Necessary for adherens junction and tight
                     junction localization.
                     /evidence=ECO:0000250|UniProtKB:Q920B0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     Region          576..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     Region          635..698
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q920B0; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     Region          712..735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     Region          752..786
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     Region          905..925
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     Region          1004..1034
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2L6.4)"
     CDS             1..1034
                     /gene="FRMD4B"
                     /gene_synonym="6030440G05Rik; GRSP1"
                     /coded_by="NM_015123.3:100..3204"
                     /db_xref="CCDS:CCDS46863.1"
                     /db_xref="GeneID:23150"
                     /db_xref="HGNC:HGNC:24886"
                     /db_xref="MIM:617467"
ORIGIN      
        1 masvfmcgve dllfsgsrfv wnltvstlrr wyterlrach qvlrtwcglq dvyqmtegrh
       61 cqvhllddrr lellvqpkll arelldlvas hfnlkekeyf gitfiddtgq qnwlqldhrv
      121 ldhdlpkkpg ptilhfavrf yiesisflkd kttvelffln akacvhkgqi evesetifkl
      181 aafilqeakg dytsdenark dlktlpafpt ktlqehpsla ycedrviehy lkikgltrgq
      241 avvqymkive alptygvhyy avkdkqglpw wlgisykgig qydiqdkvkp rklfqwkqle
      301 nlyfrekkfa vevhdprris vsrrtfgqsg lfvqtwyans sliksiwvma isqhqfyldr
      361 kqskakipsa rsldeiamdl tetgtqrask lvtletksqf imasngslis sgsqdsevse
      421 eqkrekilel kkkekllqek llkkveelkk iclreaeltg kmpkeyplni gekppqvrrr
      481 vgtafklddn llpseedpal qelesnfliq qklveaakkl anepdlcktv kkkrkqdytd
      541 amkklqeien aineyrircg kkpsqkatvl pediipsess slsdtttydd psdaftfpgq
      601 rsssvphspr ilppkslgie rihfrkssin eqfvdtrqsr emlsthsspy ktlerrpqgg
      661 rsmpttpvlt rnayssshle pesssqhcrq rsgslesqsh llsemdsdkp ffslsksqrs
      721 ssteilddgs sytsqsstey ycvtpvtgpy yttqtldtrt rgrrrskkqn vstsnsgsmp
      781 nlaqkdslrn gvysksqepp sssyyiagyt pyaecdfyys ggyvyendte gqysvnpsyr
      841 ssahygyerq rdysrsfhed evdrvphnpy atlrlprkaa aksehitkni hkalvaehlr
      901 gwyqrasgqk dqghspqtsf dsdrgsqrcl gfaglqvpcs pssrassyss vsstnasgnw
      961 rtqltiglsd yetpahssyt scygnvynpl pspsrqytei sqldgtdgnq lednlesseq
     1021 rlfwhedskp gtlv
//
LOCUS       NP_005619                541 aa            linear   PRI 27-APR-2025
DEFINITION  neutral amino acid transporter B(0) isoform 1 [Homo sapiens].
ACCESSION   NP_005619
VERSION     NP_005619.1
DBSOURCE    REFSEQ: accession NM_005628.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Borowska,A.M., Chiariello,M.G., Garaeva,A.A., Rheinberger,J.,
            Marrink,S.J., Paulino,C. and Slotboom,D.J.
  TITLE     Structural basis of the obligatory exchange mode of human neutral
            amino acid transporter ASCT2
  JOURNAL   Nat Commun 15 (1), 6570 (2024)
   PUBMED   39095408
  REMARK    GeneRIF: Structural basis of the obligatory exchange mode of human
            neutral amino acid transporter ASCT2.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Yang,R., Zhang,S., Wang,L., Chen,Y., Chen,X., Xia,J., Ren,X.,
            Cheng,B. and Chen,X.
  TITLE     Radiation-induced exosomes promote oral squamous cell carcinoma
            progression via enhancing SLC1A5-glutamine metabolism
  JOURNAL   J Oral Pathol Med 53 (7), 458-467 (2024)
   PUBMED   38802300
  REMARK    GeneRIF: Radiation-induced exosomes promote oral squamous cell
            carcinoma progression via enhancing SLC1A5-glutamine metabolism.
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Zhang,G., Yu,J. and Wan,Y.
  TITLE     USP48 deubiquitination stabilizes SLC1A5 to inhibit retinal pigment
            epithelium cell inflammation, oxidative stress and ferroptosis in
            the progression of diabetic retinopathy
  JOURNAL   J Bioenerg Biomembr 56 (3), 311-321 (2024)
   PUBMED   38427128
  REMARK    GeneRIF: USP48 deubiquitination stabilizes SLC1A5 to inhibit
            retinal pigment epithelium cell inflammation, oxidative stress and
            ferroptosis in the progression of diabetic retinopathy.
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Zhang,Z., Liu,W., Huang,T., Li,J., Hu,H., Xu,X. and Fan,Z.
  TITLE     CircCPA4 induces ASCT2 expression to promote tumor property of
            non-small cell lung cancer cells in a miR-145-5p-dependent manner
  JOURNAL   Thorac Cancer 15 (10), 764-777 (2024)
   PUBMED   38400818
  REMARK    GeneRIF: CircCPA4 induces ASCT2 expression to promote tumor
            property of non-small cell lung cancer cells in a
            miR-145-5p-dependent manner.
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Awad,S., Skipper,W., Vostrejs,W., Ozorowski,K., Min,K., Pfuhler,L.,
            Mehta,D. and Cooke,A.
  TITLE     The YBX3 RNA-binding protein posttranscriptionally controls SLC1A5
            mRNA in proliferating and differentiating skeletal muscle cells
  JOURNAL   J Biol Chem 300 (2), 105602 (2024)
   PUBMED   38159852
  REMARK    GeneRIF: The YBX3 RNA-binding protein posttranscriptionally
            controls SLC1A5 mRNA in proliferating and differentiating skeletal
            muscle cells.
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Tailor,C.S., Marin,M., Nouri,A., Kavanaugh,M.P. and Kabat,D.
  TITLE     Truncated forms of the dual function human ASCT2 neutral amino acid
            transporter/retroviral receptor are translationally initiated at
            multiple alternative CUG and GUG codons
  JOURNAL   J Biol Chem 276 (29), 27221-27230 (2001)
   PUBMED   11350958
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Broer,A., Wagner,C., Lang,F. and Broer,S.
  TITLE     Neutral amino acid transporter ASCT2 displays substrate-induced Na+
            exchange and a substrate-gated anion conductance
  JOURNAL   Biochem J 346 Pt 3 (Pt 3), 705-710 (2000)
   PUBMED   10698697
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Tailor,C.S., Nouri,A., Zhao,Y., Takeuchi,Y. and Kabat,D.
  TITLE     A sodium-dependent neutral-amino-acid transporter mediates
            infections of feline and baboon endogenous retroviruses and simian
            type D retroviruses
  JOURNAL   J Virol 73 (5), 4470-4474 (1999)
   PUBMED   10196349
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Rasko,J.E., Battini,J.L., Gottschalk,R.J., Mazo,I. and Miller,A.D.
  TITLE     The RD114/simian type D retrovirus receptor is a neutral amino acid
            transporter
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 2129-2134 (1999)
   PUBMED   10051606
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Kekuda,R., Prasad,P.D., Fei,Y.J., Torres-Zamorano,V., Sinha,S.,
            Yang-Feng,T.L., Leibach,F.H. and Ganapathy,V.
  TITLE     Cloning of the sodium-dependent, broad-scope, neutral amino acid
            transporter Bo from a human placental choriocarcinoma cell line
  JOURNAL   J Biol Chem 271 (31), 18657-18661 (1996)
   PUBMED   8702519
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008622.6, U53347.1, AB209738.1 and AK301661.1.
            
            Summary: The SLC1A5 gene encodes a sodium-dependent neutral amino
            acid transporter that can act as a receptor for RD114/type D
            retrovirus (Larriba et al., 2001 [PubMed 11781704]).[supplied by
            OMIM, Jan 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF105423.1, AK292690.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000542575.6/ ENSP00000444408.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..541
                     /product="neutral amino acid transporter B(0) isoform 1"
                     /note="baboon M7 virus receptor; RD114 virus receptor;
                     neutral amino acid transporter B; neutral amino acid
                     transporter B(0); ATB(0); RD114/simian type D retrovirus
                     receptor; sodium-dependent neutral amino acid transporter
                     type 2; solute carrier family 1 (neutral amino acid
                     transporter), member 5; Alanine/serine/cysteine
                     transporter 2; ASC amino acid transporter-2"
                     /calculated_mol_wt=56467
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q15758.2)"
     Site            52..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15758.2)"
     Site            95..116
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15758.2)"
     Region          106..479
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     Site            131..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15758.2)"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15758.2)"
     Site            212
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q15758.2)"
     Site            225..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15758.2)"
     Site            258..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15758.2)"
     Site            307..328
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15758.2)"
     Site            374..400
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15758.2)"
     Site            461..482
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15758.2)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15758.2)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15758.2)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15758.2)"
     Region          511..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15758.2)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15758.2)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15758.2)"
     CDS             1..541
                     /gene="SLC1A5"
                     /gene_synonym="AAAT; ASCT2; ATBO; M7V1; M7VS1; R16; RDRC"
                     /coded_by="NM_005628.3:630..2255"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12692.1"
                     /db_xref="GeneID:6510"
                     /db_xref="HGNC:HGNC:10943"
                     /db_xref="MIM:109190"
ORIGIN      
        1 mvadpprdsk glaaaeptan gglalasied qgaaaggycg srdqvrrclr anllvlltvv
       61 avvagvalgl gvsgaggala lgperlsafv fpgelllrll rmiilplvvc sliggaasld
      121 pgalgrlgaw allfflvttl lasalgvgla lalqpgaasa ainasvgaag saenapskev
      181 ldsfldlarn ifpsnlvsaa frsysttyee rnitgtrvkv pvgqevegmn ilglvvfaiv
      241 fgvalrklgp egellirffn sfneatmvlv swimwyapvg imflvagkiv emedvgllfa
      301 rlgkyilccl lghaihgllv lpliyflftr knpyrflwgi vtplatafgt ssssatlplm
      361 mkcveenngv akhisrfilp igatvnmdga alfqcvaavf iaqlsqqsld fvkiitilvt
      421 atassvgaag ipaggvltla iileavnlpv dhislilavd wlvdrsctvl nvegdalgag
      481 llqnyvdrte srstepeliq vkselpldpl pvpteegnpl lkhyrgpagd atvasekesv
      541 m
//
LOCUS       NP_003949                485 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF8 isoform 1 [Homo sapiens].
ACCESSION   NP_003949
VERSION     NP_003949.1
DBSOURCE    REFSEQ: accession NM_003958.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Sun,Q., Sui,Y., Li,S., Zhou,R., Fu,Z., Luo,J. and Zhao,W.
  TITLE     RNF8-mediated multi-ubiquitination of MCM7: Linking disassembly of
            the CMG helicase with DNA damage response in human cells
  JOURNAL   Life Sci 353, 122912 (2024)
   PUBMED   39004272
  REMARK    GeneRIF: RNF8-mediated multi-ubiquitination of MCM7: Linking
            disassembly of the CMG helicase with DNA damage response in human
            cells.
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Kuang,J., Duan,T., Gao,C., Liu,C., Chen,S., Zhu,L.Y., Min,L.,
            Lu,C., Wang,W. and Zhu,L.
  TITLE     RNF8 depletion attenuates hepatocellular carcinoma progression by
            inhibiting epithelial-mesenchymal transition and enhancing drug
            sensitivity
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (4), 661-671 (2023)
   PUBMED   37154586
  REMARK    GeneRIF: RNF8 depletion attenuates hepatocellular carcinoma
            progression by inhibiting epithelial-mesenchymal transition and
            enhancing drug sensitivity.
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Zhou,T., Wang,S., Song,X., Liu,W., Dong,F., Huo,Y., Zou,R.,
            Wang,C., Zhang,S., Liu,W., Sun,G., Lin,L., Zeng,K., Dong,X.,
            Guo,Q., Yi,F., Wang,Z., Li,X., Jiang,B., Cao,L. and Zhao,Y.
  TITLE     RNF8 up-regulates AR/ARV7 action to contribute to advanced prostate
            cancer progression
  JOURNAL   Cell Death Dis 13 (4), 352 (2022)
   PUBMED   35428760
  REMARK    GeneRIF: RNF8 up-regulates AR/ARV7 action to contribute to advanced
            prostate cancer progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Lu,X., Xu,M., Zhu,Q., Zhang,J., Liu,G., Bao,Y., Gu,L., Tian,Y.,
            Wen,H. and Zhu,W.G.
  TITLE     RNF8-ubiquitinated KMT5A is required for RNF168-induced H2A
            ubiquitination in response to DNA damage
  JOURNAL   FASEB J 35 (4), e21326 (2021)
   PUBMED   33710666
  REMARK    GeneRIF: RNF8-ubiquitinated KMT5A is required for RNF168-induced
            H2A ubiquitination in response to DNA damage.
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   7  (residues 1 to 485)
  AUTHORS   Takano,Y., Adachi,S., Okuno,M., Muto,Y., Yoshioka,T.,
            Matsushima-Nishiwaki,R., Tsurumi,H., Ito,K., Friedman,S.L.,
            Moriwaki,H., Kojima,S. and Okano,Y.
  TITLE     The RING finger protein, RNF8, interacts with retinoid X receptor
            alpha and enhances its transcription-stimulating activity
  JOURNAL   J Biol Chem 279 (18), 18926-18934 (2004)
   PUBMED   14981089
  REMARK    GeneRIF: results suggest a novel function of RNF8 as a regulator of
            RXR alpha-mediated transcriptional activity through interaction
            between their respective N-terminal regions
REFERENCE   8  (residues 1 to 485)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 485)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
REFERENCE   10 (residues 1 to 485)
  AUTHORS   Seki,N., Hattori,A., Sugano,S., Suzuki,Y., Nakagawara,A.,
            Ohhira,M., Muramatsu,M., Hori,T. and Saito,T.
  TITLE     Isolation, tissue expression, and chromosomal assignment of a novel
            human gene which encodes a protein with RING finger motif
  JOURNAL   J Hum Genet 43 (4), 272-274 (1998)
   PUBMED   9852682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA064222.1, AB014546.1 and
            BE327572.1.
            
            Summary: The protein encoded by this gene contains a RING finger
            motif and an FHA domain. This protein has been shown to interact
            with several class II ubiquitin-conjugating enzymes (E2), including
            UBE2E1/UBCH6, UBE2E2, and UBE2E3, and may act as an ubiquitin
            ligase (E3) in the ubiquitination of certain nuclear proteins. This
            protein is also known to play a role in the DNA damage response and
            depletion of this protein causes cell growth inhibition and cell
            cycle arrest. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Feb 2012].
            
            Transcript Variant: This variant (1) represents the most abundant
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.211118.1, AB014546.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373479.9/ ENSP00000362578.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..485
                     /product="E3 ubiquitin-protein ligase RNF8 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="C3HC4-type zinc finger protein; ring finger protein
                     (C3HC4 type) 8; E3 ubiquitin-protein ligase RNF8;
                     UBC13/UEV-interacting ring finger protein; ring finger
                     protein 8, E3 ubiquitin protein ligase; RING-type E3
                     ubiquitin transferase RNF8"
                     /calculated_mol_wt=55387
     Region          18..126
                     /region_name="FHA_RNF8"
                     /note="forkhead associated (FHA) domain found in RING
                     finger protein 8 (RNF8) and similar proteins; cd22663"
                     /db_xref="CDD:438715"
     Site            order(42,55,57..61,82..83,110)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438715"
     Region          68..72
                     /region_name="Required for interaction with PIWIL1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03067"
                     /note="propagated from UniProtKB/Swiss-Prot (O76064.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O76064.1)"
     Region          181..220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O76064.1)"
     Region          <233..>402
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
     Region          400..463
                     /region_name="RING-HC_RNF8"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 8 (RNF8) and similar proteins; cd16535"
                     /db_xref="CDD:438197"
     Site            order(400..401,415..416,419..421,448..453,455..456,
                     459..460,463)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:438197"
     Site            order(402,404..408,429..430,433..434,438,441)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438197"
     CDS             1..485
                     /gene="RNF8"
                     /gene_synonym="hRNF8"
                     /coded_by="NM_003958.4:183..1640"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4834.1"
                     /db_xref="GeneID:9025"
                     /db_xref="HGNC:HGNC:10071"
                     /db_xref="MIM:611685"
ORIGIN      
        1 mgepgffvtg draggrswcl rrvgmsagwl lledgcevtv grgfgvtyql vskicplmis
       61 rnhcvlkqnp egqwtimdnk slngvwlnra rleplrvysi hqgdyiqlgv plenkenaey
      121 eyevteedwe tiypclspkn dqmieknkel rtkrkfslde lagpgaegps nlkskinkvs
      181 cesgqpvksq gkgevastps dnldpkltal epskttgapi ypgfpkvtev hheqkasnss
      241 asqrslqmfk vtmsrilrlk iqmqekheav mnvkkqtqkg nskkvvqmeq elqdlqsqlc
      301 aeqaqqqarv eqlektfqee eqhlqgleia qgekdlkqql aqalqehwal meelnrskkd
      361 feaiiqaknk eleqtkeeke kmqaqkeevl shmndvlene lqciicseyf ieavtlncah
      421 sfcsycinew mkrkiecpic rkdiksktys lvldncinkm vnnlssevke rrivlirerk
      481 akrlf
//
LOCUS       NP_997276                125 aa            linear   PRI 27-APR-2025
DEFINITION  insulin growth factor-like family member 3 precursor [Homo
            sapiens].
ACCESSION   NP_997276
VERSION     NP_997276.1
DBSOURCE    REFSEQ: accession NM_207393.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Wang,Y. and Tatakis,D.N.
  TITLE     Human gingiva transcriptome during wound healing
  JOURNAL   J Clin Periodontol 44 (4), 394-402 (2017)
   PUBMED   28005267
  REMARK    GeneRIF: IGFL3 expression is significantly downregulated in human
            masticatory mucosa during wound healing
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Lobito,A.A., Ramani,S.R., Tom,I., Bazan,J.F., Luis,E.,
            Fairbrother,W.J., Ouyang,W. and Gonzalez,L.C.
  TITLE     Murine insulin growth factor-like (IGFL) and human IGFL1 proteins
            are induced in inflammatory skin conditions and bind to a novel
            tumor necrosis factor receptor family member, IGFLR1
  JOURNAL   J Biol Chem 286 (21), 18969-18981 (2011)
   PUBMED   21454693
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Emtage,P., Vatta,P., Arterburn,M., Muller,M.W., Park,E., Boyle,B.,
            Hazell,S., Polizotto,R., Funk,W.D. and Tang,Y.T.
  TITLE     IGFL: A secreted family with conserved cysteine residues and
            similarities to the IGF superfamily
  JOURNAL   Genomics 88 (4), 513-520 (2006)
   PUBMED   16890402
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007785.1 and AY358434.1.
            
            Summary: IGFL3 belongs to the insulin-like growth factor (IGF; see
            MIM 147440) family of signaling molecules that play critical roles
            in cellular energy metabolism and in growth and development,
            especially prenatal growth (Emtage et al., 2006 [PubMed
            16890402]).[supplied by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358434.1, AY672113.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147596 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341415.3/ ENSP00000344860.2
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..125
                     /product="insulin growth factor-like family member 3
                     precursor"
                     /note="insulin growth factor-like family member 3;
                     RPRC483"
                     /calculated_mol_wt=11461
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2755
     mat_peptide     25..125
                     /product="Insulin growth factor-like family member 3.
                     /id=PRO_0000044634"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXB1.1)"
                     /calculated_mol_wt=11461
     Region          33..115
                     /region_name="IGFL"
                     /note="Insulin growth factor-like family; pfam14653"
                     /db_xref="CDD:464239"
     CDS             1..125
                     /gene="IGFL3"
                     /gene_synonym="UNQ483"
                     /coded_by="NM_207393.2:40..417"
                     /db_xref="CCDS:CCDS33058.1"
                     /db_xref="GeneID:388555"
                     /db_xref="HGNC:HGNC:32930"
                     /db_xref="MIM:610546"
ORIGIN      
        1 mrprccilal vcwitvfllq cskgttdapv gsglwlcqpt prcgnkiynp seqccyddai
       61 lslketrrcg stctfwpcfe lccpesfgpq qkflvklrvl gmksqchlsp isrsctrnrr
      121 hvlyp
//
LOCUS       NP_001347981            1304 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 532 isoform 1 [Mus musculus].
ACCESSION   NP_001347981 XP_006526107
VERSION     NP_001347981.1
DBSOURCE    REFSEQ: accession NM_001361052.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1304)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1304)
  AUTHORS   Liang,G.H., Luo,Y.N., Wei,R.Z., Yin,J.Y., Qin,Z.L., Lu,L.L. and
            Ma,W.H.
  TITLE     CircZNF532 knockdown protects retinal pigment epithelial cells
            against high glucose-induced apoptosis and pyroptosis by regulating
            the miR-20b-5p/STAT3 axis
  JOURNAL   J Diabetes Investig 13 (5), 781-795 (2022)
   PUBMED   34839589
  REMARK    GeneRIF: CircZNF532 knockdown protects retinal pigment epithelial
            cells against high glucose-induced apoptosis and pyroptosis by
            regulating the miR-20b-5p/STAT3 axis.
REFERENCE   3  (residues 1 to 1304)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1304)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
REFERENCE   5  (residues 1 to 1304)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132307.5 and AC124578.4.
            
            On Feb 27, 2018 this sequence version replaced XP_006526107.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.65913.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849385, SAMN00849389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1304
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 38.91 cM"
     Protein         1..1304
                     /product="zinc finger protein 532 isoform 1"
                     /calculated_mol_wt=141250
     Region          <136..371
                     /region_name="PTZ00108"
                     /note="DNA topoisomerase 2-like protein; Provisional"
                     /db_xref="CDD:240271"
     Region          753..772
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          781..816
                     /region_name="zf-RING_7"
                     /note="C4-type zinc ribbon domain; pfam02591"
                     /db_xref="CDD:426857"
     Region          782..802
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(787,789,791,793..794,797..798,801,816,820..821,
                     824..825,831,846,848,850,852..853,856..857)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          810..832
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          841..858
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          869..890
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          904..924
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1024..1044
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1029,1031,1033,1035..1036,1039..1040,1043,1059,1061,
                     1065..1066,1069..1070,1073,1092,1094,1096,1098..1099,
                     1102..1103)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1054..1075
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1084..1104
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1179..1199
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1184,1186,1188,1190..1191,1194..1195,1198,1213,1215,
                     1219..1220,1223..1224,1228,1274,1276,1278,1280..1281,
                     1284..1285,1288)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1204..1230
                     /region_name="zf-C2H2_11"
                     /note="zinc-finger C2H2-type; pfam16622"
                     /db_xref="CDD:465205"
     Region          1208..1229
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1268..1289
                     /region_name="zf-C2H2_6"
                     /note="C2H2-type zinc finger; pfam13912"
                     /db_xref="CDD:433576"
     Region          1269..1289
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1304
                     /gene="Zfp532"
                     /gene_synonym="C530030I18Rik; mKIAA1629; Znf532"
                     /coded_by="NM_001361052.1:112..4026"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS89265.1"
                     /db_xref="GeneID:328977"
                     /db_xref="MGI:MGI:3036282"
ORIGIN      
        1 mtmgdmktpd fddllaafdi pdmvdpkaai esghddhesh ikqnahvddd shtpsssdvg
       61 vsvivknvrn idssegvekd ghnptgnglh ngfltassld sygkdgaksl kgdtpasevt
      121 lkdpafsqfs pissaeefed dekievddpp dkeearagfr snvltgsapq qdfdklkalg
      181 genssktgvs tsghtdknkv kreaesnsit lsvyepfkvr kaedklkens ekmlesrvld
      241 gkpsseksds giaaaasskt kpssklssci aaiaalsakk aasdsckepv ansreasplp
      301 kevndspkaa dkspesqnli dgtkkaslkp sdsprsvsse nsskgspssp vgstpaipkv
      361 riktiktssg eikrtvtrvl pevdldsgkk pseqaasvma svtsllsssa satvlssppr
      421 aplqtamvts avssaeltpk qvtikpvata flpvsavkta gsqvinlkla nnttvkatvi
      481 saasvqsass aiikaanaiq qqtvvvpass lanaklvpkt vhlanlnllp qgaqatselr
      541 qvltkpqqqi kqaiinaaas qppkkvsrvq vvsslqssvv eafnkvlssv npvpvytpnl
      601 sppanagitl pmrgykclec gdafaleksl sqhydrrsvr ievtcnhctk nlvfynkcsl
      661 lsharghkek gvvmqcshli lkpvpadqmi vppssntaas tlqssvgaat htvpkvqpgi
      721 agavisapas tpmspampld edpsklcrhs lkclecnevf qdepslathf qhaadtsgqk
      781 tctvcqmllp nqcsyashqr ihqhkspytc pecgaicrsv hfqnhitknc lhytrrvgfr
      841 cvhcnvvysd vaalkshiqg shcevfykcp icpmafksap sthshaytqh pgvkigepki
      901 iykcsmcdtv ftlqtllyrh fdqhtdnqkv svfkcpdcsl lyaqkqlmmd hiksmhgtlk
      961 siegppnlgi nlplsvkpat qnsanhsred aksvngkekl ekkspspakk stepkkmasl
     1021 gwtcwecdrl ftqrdvylsh mrkehgkqmk khpcrqcdks fssshslcrh nrikhkgirk
     1081 vyacshcpds rrtftkrlml erhiqlmhgi kdpdvkelsd dagdvtndee eeaeikedak
     1141 vpspkrklee pvlefrpprg aitqplkklk invfkvhkca vcgfttenll qfhehipqhr
     1201 sdgsshqcre cglcytshgs larhlfivhk lkepqpvskq ngagedsqqe nkpspedeaa
     1261 egaasdrkck vcaktfetea alnthmrthg mafikskrms saek
//
LOCUS       NP_001334009             100 aa            linear   ROD 27-APR-2025
DEFINITION  neuronal vesicle trafficking-associated protein 2 isoform 2 [Mus
            musculus].
ACCESSION   NP_001334009
VERSION     NP_001334009.1
DBSOURCE    REFSEQ: accession NM_001347080.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Zimmerman,A.J., Serrano-Rodriguez,A., Sun,M., Wilson,S.J.,
            Linsenbardt,D.N., Brigman,J.L. and Weick,J.P.
  TITLE     Knockout of AMPA receptor binding protein Neuron-specific gene 2
            (NSG2) enhances associative learning and cognitive flexibility
  JOURNAL   Mol Brain 17 (1), 95 (2024)
   PUBMED   39695712
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Chander,P., Kennedy,M.J., Winckler,B. and Weick,J.P.
  TITLE     Neuron-Specific Gene 2 (NSG2) Encodes an AMPA Receptor Interacting
            Protein That Modulates Excitatory Neurotransmission
  JOURNAL   eNeuro 6 (1) (2019)
   PUBMED   30680309
  REMARK    GeneRIF: NSG2 is found in discrete punctae restricted to the
            somatodendritic arbors of developing mouse and human neurons, and a
            significant proportion of NSG2 punctae colocalize with postsynaptic
            HOMER1 and surface-expressed AMPA-type glutamate receptors (AMPARs)
            at excitatory synapses.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 100)
  AUTHORS   Timmermans,S. and Libert,C.
  TITLE     Overview of inactivating mutations in the protein-coding genome of
            the mouse reference strain C57BL/6J
  JOURNAL   JCI Insight 3 (13), 121758 (2018)
   PUBMED   29997285
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 100)
  AUTHORS   Kawaguchi,A., Ikawa,T., Kasukawa,T., Ueda,H.R., Kurimoto,K.,
            Saitou,M. and Matsuzaki,F.
  TITLE     Single-cell gene profiling defines differential progenitor
            subclasses in mammalian neurogenesis
  JOURNAL   Development 135 (18), 3113-3124 (2008)
   PUBMED   18725516
REFERENCE   7  (residues 1 to 100)
  AUTHORS   Heanue,T.A. and Pachnis,V.
  TITLE     Expression profiling the developing mammalian enteric nervous
            system identifies marker and candidate Hirschsprung disease genes
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 6919-6924 (2006)
   PUBMED   16632597
REFERENCE   8  (residues 1 to 100)
  AUTHORS   Abramova,N., Charniga,C., Goderie,S.K. and Temple,S.
  TITLE     Stage-specific changes in gene expression in acutely isolated mouse
            CNS progenitor cells
  JOURNAL   Dev Biol 283 (2), 269-281 (2005)
   PUBMED   15890332
REFERENCE   9  (residues 1 to 100)
  AUTHORS   Saberan-Djoneidi,D., Marey-Semper,I., Picart,R., Studler,J.M.,
            Tougard,C., Glowinski,J. and Levi-Strauss,M.
  TITLE     A 19-kDa protein belonging to a new family is expressed in the
            Golgi apparatus of neural cells
  JOURNAL   J Biol Chem 270 (4), 1888-1893 (1995)
   PUBMED   7829526
REFERENCE   10 (residues 1 to 100)
  AUTHORS   Diriong,S., Saberan-Djoneidi,D., Levi-Strauss,M., Bernheim,A. and
            Nguyen,V.C.
  TITLE     Assignment of the human 8.5 H gene to chromosome 5, region 5q35
  JOURNAL   Hum Genet 93 (6), 703-706 (1994)
   PUBMED   8005598
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN176718.1 and AK041338.1.
            
            Transcript Variant: This variant (4) contains an alternate 3'
            terminal exon, resulting in novel 3' coding region and 3' UTR,
            compared to variant 1. It encodes isoform 2, which is shorter and
            has a distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849375,
                              SAMN00849382 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 18.72 cM"
     Protein         1..100
                     /product="neuronal vesicle trafficking-associated protein
                     2 isoform 2"
                     /note="neuron-specific protein family member 2; protein
                     8.5; protein p19; neuronal vesicle trafficking-associated
                     protein 2"
                     /calculated_mol_wt=11156
     Region          1..>74
                     /region_name="Calcyon"
                     /note="D1 dopamine receptor-interacting protein (calcyon);
                     pfam06387"
                     /db_xref="CDD:461892"
     CDS             1..100
                     /gene="Nsg2"
                     /gene_synonym="P19"
                     /coded_by="NM_001347080.1:200..502"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS88140.1"
                     /db_xref="GeneID:18197"
                     /db_xref="MGI:MGI:1202070"
ORIGIN      
        1 mvklnsnpge kgakppsved gfqtvplitp levnhlqlaa pekvivktrt eyqpeqrnkg
       61 kfrvpkiaef tvalpklpap afnglqiwyq qhrqkivysp
//
LOCUS       NP_078891                854 aa            linear   PRI 27-APR-2025
DEFINITION  protein mono-ADP-ribosyltransferase PARP8 isoform 1 [Homo sapiens].
ACCESSION   NP_078891 XP_943922 XP_948977 XP_948982 XP_948984
VERSION     NP_078891.2
DBSOURCE    REFSEQ: accession NM_024615.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Vyas,S., Matic,I., Uchima,L., Rood,J., Zaja,R., Hay,R.T., Ahel,I.
            and Chang,P.
  TITLE     Family-wide analysis of poly(ADP-ribose) polymerase activity
  JOURNAL   Nat Commun 5, 4426 (2014)
   PUBMED   25043379
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Viding,E., Price,T.S., Jaffee,S.R., Trzaskowski,M., Davis,O.S.,
            Meaburn,E.L., Haworth,C.M. and Plomin,R.
  TITLE     Genetics of callous-unemotional behavior in children
  JOURNAL   PLoS One 8 (7), e65789 (2013)
   PUBMED   23874384
  REMARK    Erratum:[PLoS One. 2013;8(7). doi:
            10.1371/annotation/0b16418f-ceb5-41b2-be2a-a20f0c56f9a6]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 854)
  AUTHORS   Fan,Q., Barathi,V.A., Cheng,C.Y., Zhou,X., Meguro,A., Nakata,I.,
            Khor,C.C., Goh,L.K., Li,Y.J., Lim,W., Ho,C.E., Hawthorne,F.,
            Zheng,Y., Chua,D., Inoko,H., Yamashiro,K., Ohno-Matsui,K.,
            Matsuo,K., Matsuda,F., Vithana,E., Seielstad,M., Mizuki,N.,
            Beuerman,R.W., Tai,E.S., Yoshimura,N., Aung,T., Young,T.L.,
            Wong,T.Y., Teo,Y.Y. and Saw,S.M.
  TITLE     Genetic variants on chromosome 1q41 influence ocular axial length
            and high myopia
  JOURNAL   PLoS Genet 8 (6), e1002753 (2012)
   PUBMED   22685421
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC112187.2, DC417471.1, DC429180.1, AL834477.1 and AC022441.5.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_948977.1, XP_948982.1, XP_948984.1, XP_943922.1, NP_078891.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.193309.1,
                                           SRR1803617.263938.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281631.10/ ENSP00000281631.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q11.1"
     Protein         1..854
                     /product="protein mono-ADP-ribosyltransferase PARP8
                     isoform 1"
                     /EC_number="2.4.2.30"
                     /note="ADP-ribosyltransferase diphtheria toxin-like 16;
                     protein mono-ADP-ribosyltransferase PARP8"
                     /calculated_mol_wt=95740
     Region          113..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3A8.1)"
     Region          291..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3A8.1)"
     Region          <482..581
                     /region_name="ADP_ribosyl"
                     /note="ADP_ribosylating enzymes catalyze the transfer of
                     ADP_ribose from NAD+ to substrates. Bacterial toxins are
                     cytoplasmic and catalyze the transfer of a single
                     ADP_ribose unit to eukaryotic elongation factor 2, halting
                     protein synthesis and killing the cell; cd01341"
                     /db_xref="CDD:238651"
     Region          694..818
                     /region_name="ADP_ribosyl"
                     /note="ADP_ribosylating enzymes catalyze the transfer of
                     ADP_ribose from NAD+ to substrates. Bacterial toxins are
                     cytoplasmic and catalyze the transfer of a single
                     ADP_ribose unit to eukaryotic elongation factor 2, halting
                     protein synthesis and killing the cell; cd01341"
                     /db_xref="CDD:238651"
     Site            order(696..700,703,707,711..713,715,731..733,743,804)
                     /site_type="other"
                     /note="nad+ binding pocket [chemical binding]"
                     /db_xref="CDD:238651"
     Region          750..777
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3A8.1)"
     CDS             1..854
                     /gene="PARP8"
                     /gene_synonym="ARTD16; pART16"
                     /coded_by="NM_024615.4:460..3024"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3954.1"
                     /db_xref="GeneID:79668"
                     /db_xref="HGNC:HGNC:26124"
ORIGIN      
        1 mgmcsrqeri qkdidvviqk sraekdclfa dfrysdstft ftyvggprsv sysvhvsedy
       61 pdntyvssse ndedvlvtte pipvifhria telrktndin cclsiksklq kengeesrqn
      121 stveedsegd ndseefyygg qvnydgelhk hpqleadlsa vreiygphav slreygaidd
      181 vdidlhidvs fldeeiavaw evirtepiiv rlhcsltqyl ngpvptvdvf qistkerfgl
      241 ghqlkkimqt fvtqqwkqsk eksnclhnkk lsekkvkspl hlfstlrrsp sypppgcgks
      301 ksklkseqdg iskthkllrr tcsstvktdd vcvtkshrtf grslssdpra eqamtaiksh
      361 kllnrpcpaa vkseecltlk shrlltrscs gdprcehntn lkphkllsrs yssnlrmeel
      421 yglknhklls ksyssapkss ktelfkepna egrrlsltsg ligiltpsss sssqlapnga
      481 kcipvrdrgf lvqtiefaeq ripvlneycv vcdephvfqn gpmlrptvce relcvfafqt
      541 lgvmneaade iatgaqvvdl lvsmcrsale sprkvvifep ypsvvdpndp qmlafnprkk
      601 nydrvmkald sitsiremtq apyleikkqm dkqdplahpl lqwvissnrs hivklpvnrq
      661 lkfmhtphqf lllssppake snfraakklf gstfafhgsh ienwhsilrn glvvasntrl
      721 qlhgamygsg iylspmssis fgysgmnkkq kvsakdepas sskssntsqs qkkgqqsqfl
      781 qsrnlkcial cevitssdlh khgeiwvvpn tdhvctrfff vyedgqvgda nintqeggih
      841 keilrvignq tatg
//
LOCUS       NP_001350776             365 aa            linear   PRI 27-APR-2025
DEFINITION  lactosylceramide alpha-2,3-sialyltransferase isoform 6 [Homo
            sapiens].
ACCESSION   NP_001350776 XP_005264687
VERSION     NP_001350776.1
DBSOURCE    REFSEQ: accession NM_001363847.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Dookwah,M., Wagner,S.K., Ishihara,M., Yu,S.H., Ulrichs,H.,
            Kulik,M.J., Zeltner,N., Dalton,S., Strauss,K.A., Aoki,K., Steet,R.
            and Tiemeyer,M.
  TITLE     Neural-specific alterations in glycosphingolipid biosynthesis and
            cell signaling associated with two human ganglioside GM3 synthase
            deficiency variants
  JOURNAL   Hum Mol Genet 32 (24), 3323-3341 (2023)
   PUBMED   37676252
  REMARK    GeneRIF: Neural-specific alterations in glycosphingolipid
            biosynthesis and cell signaling associated with two human
            ganglioside GM3 synthase deficiency variants.
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Watanabe,S., Lei,M., Nakagawa,E., Takeshita,E., Inamori,K.I.,
            Shishido,F., Sasaki,M., Mitsuhashi,S., Matsumoto,N., Kimura,Y.,
            Iwasaki,M., Takahashi,Y., Mizusawa,H., Migita,O., Ohno,I. and
            Inokuchi,J.I.
  TITLE     Neurological insights on two siblings with GM3 synthase deficiency
            due to novel compound heterozygous ST3GAL5 variants
  JOURNAL   Brain Dev 45 (5), 270-277 (2023)
   PUBMED   36690566
  REMARK    GeneRIF: Neurological insights on two siblings with GM3 synthase
            deficiency due to novel compound heterozygous ST3GAL5 variants.
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Liu,J., Li,M., Wu,J., Qi,Q., Li,Y., Wang,S., Liang,S., Zhang,Y.,
            Zhu,Z., Huang,R., Yan,J. and Zhu,R.
  TITLE     Identification of ST3GAL5 as a prognostic biomarker correlating
            with CD8+ T cell exhaustion in clear cell renal cell carcinoma
  JOURNAL   Front Immunol 13, 979605 (2022)
   PUBMED   36172374
  REMARK    GeneRIF: Identification of ST3GAL5 as a prognostic biomarker
            correlating with CD8(+) T cell exhaustion in clear cell renal cell
            carcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Indellicato,R., Parini,R., Domenighini,R., Malagolini,N.,
            Iascone,M., Gasperini,S., Masera,N., dall'Olio,F. and Trinchera,M.
  TITLE     Total loss of GM3 synthase activity by a normally processed enzyme
            in a novel variant and in all ST3GAL5 variants reported to cause a
            distinct congenital disorder of glycosylation
  JOURNAL   Glycobiology 29 (3), 229-241 (2019)
   PUBMED   30576498
  REMARK    GeneRIF: HEK-293T clones permanently expressing HaloTag-ST3GAL5
            carrying each of the five variants were assessed by quantitative
            PCR, flow cytometry, western blotting and confocal microscopy.
            Compared with the very mild phenotype of st3gal5 KO mouse models,
            the results suggest that unknown mechanisms, in addition to the
            lack of a-b-c-series gangliosides, contribute to the syndrome.
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Gordon-Lipkin,E., Cohen,J.S., Srivastava,S., Soares,B.P., Levey,E.
            and Fatemi,A.
  TITLE     ST3GAL5-Related Disorders: A Deficiency in Ganglioside Metabolism
            and a Genetic Cause of Intellectual Disability and Choreoathetosis
  JOURNAL   J Child Neurol 33 (13), 825-831 (2018)
   PUBMED   30185102
  REMARK    GeneRIF: GM3 synthase deficiency is a neurodevelopmental disorder
            with consistent features of profound intellectual disability,
            choreoathetosis, and deafness.
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Allende,M.L., Li,J., Darling,D.S., Worth,C.A. and Young,W.W. Jr.
  TITLE     Evidence supporting a late Golgi location for lactosylceramide to
            ganglioside GM3 conversion
  JOURNAL   Glycobiology 10 (10), 1025-1032 (2000)
   PUBMED   11030748
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Kapitonov,D., Bieberich,E. and Yu,R.K.
  TITLE     Combinatorial PCR approach to homology-based cloning: cloning and
            expression of mouse and human GM3-synthase
  JOURNAL   Glycoconj J 16 (7), 337-350 (1999)
   PUBMED   10619706
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Fukumoto,S., Miyazaki,H., Goto,G., Urano,T., Furukawa,K. and
            Furukawa,K.
  TITLE     Expression cloning of mouse cDNA of CMP-NeuAc:Lactosylceramide
            alpha2,3-sialyltransferase, an enzyme that initiates the synthesis
            of gangliosides
  JOURNAL   J Biol Chem 274 (14), 9271-9276 (1999)
   PUBMED   10092602
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Ishii,A., Ohta,M., Watanabe,Y., Matsuda,K., Ishiyama,K., Sakoe,K.,
            Nakamura,M., Inokuchi,J., Sanai,Y. and Saito,M.
  TITLE     Expression cloning and functional characterization of human cDNA
            for ganglioside GM3 synthase
  JOURNAL   J Biol Chem 273 (48), 31652-31655 (1998)
   PUBMED   9822625
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Cruz,V., Xin,B. and Wang,H.
  TITLE     GM3 Synthase Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37471511
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105053.3.
            
            On Jun 3, 2018 this sequence version replaced XP_005264687.1.
            
            Summary: Ganglioside GM3 is known to participate in the induction
            of cell differentiation, modulation of cell proliferation,
            maintenance of fibroblast morphology, signal transduction, and
            integrin-mediated cell adhesion. The protein encoded by this gene
            is a type II membrane protein which catalyzes the formation of GM3
            using lactosylceramide as the substrate. The encoded protein is a
            member of glycosyltransferase family 29 and may be localized to the
            Golgi apparatus. Mutation in this gene has been associated with
            Amish infantile epilepsy syndrome. Transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.511.1,
                                           SRR3476690.326876.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..365
                     /product="lactosylceramide alpha-2,3-sialyltransferase
                     isoform 6"
                     /EC_number="2.4.3.9"
                     /note="sialyltransferase 9 (CMP-NeuAc:lactosylceramide
                     alpha-2,3-sialyltransferase; GM3 synthase); alpha
                     2,3-sialyltransferase V; ganglioside GM3 synthase; ST3
                     beta-galactoside alpha-23-sialyltransferase 5"
                     /calculated_mol_wt=41331
     Region          191..348
                     /region_name="GT29"
                     /note="glycosyltransferase family 29; cl45931"
                     /db_xref="CDD:480271"
     Site            order(199..201,222..223,244,287..289,307..308,318..320,
                     336)
                     /site_type="active"
                     /db_xref="CDD:467690"
     CDS             1..365
                     /gene="ST3GAL5"
                     /gene_synonym="SATI; SIAT9; SIATGM3S; SPDRS; ST3Gal V;
                     ST3GalV"
                     /coded_by="NM_001363847.1:130..1227"
                     /note="isoform 6 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS86857.1"
                     /db_xref="GeneID:8869"
                     /db_xref="HGNC:HGNC:10872"
                     /db_xref="MIM:604402"
ORIGIN      
        1 mrtkaagcae rrplqprtea aaapagramp seytyvklrs dcsrpslqwy traqskmrrp
       61 slllkdilkc tllvfgvwil yilklnytte ecdmkkmhyv dpdhvkraqk yaqqvlqkec
      121 rpkfaktsma llfehrysvd llpfvqkapk dseaeskydp pfgfrkfssk vqtllellpe
      181 hdlpehlkak tcrrcvvigs ggilhglelg htlnqfdvvi rlnsapvegy sehvgnktti
      241 rmtypegapl sdleyysndl fvavlfksvd fnwlqamvkk etlnvptigv iavvlathlc
      301 devslagfgy dlnqprtplh yfdsqcmaam nfqtmhnvtt etkfllklvk egvvkdlsgg
      361 idref
//
LOCUS       NP_002906                356 aa            linear   PRI 27-APR-2025
DEFINITION  replication factor C subunit 3 isoform 1 [Homo sapiens].
ACCESSION   NP_002906
VERSION     NP_002906.1
DBSOURCE    REFSEQ: accession NM_002915.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Guo,Z. and Guo,L.
  TITLE     Abnormal activation of RFC3, A YAP1/TEAD downstream target,
            promotes gastric cancer progression
  JOURNAL   Int J Clin Oncol 29 (4), 442-455 (2024)
   PUBMED   38383698
  REMARK    GeneRIF: Abnormal activation of RFC3, A YAP1/TEAD downstream
            target, promotes gastric cancer progression.
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Avs,K.R., Pandi,C., Kannan,B., Pandi,A., Jayaseelan,V.P. and
            Arumugam,P.
  TITLE     RFC3 serves as a novel prognostic biomarker and target for head and
            neck squamous cell carcinoma
  JOURNAL   Clin Oral Investig 27 (11), 6961-6969 (2023)
   PUBMED   37861747
  REMARK    GeneRIF: RFC3 serves as a novel prognostic biomarker and target for
            head and neck squamous cell carcinoma.
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Ren,K., Zhu,Y., Sun,H., Li,S., Duan,X., Li,S., Li,Y., Li,B. and
            Chen,L.
  TITLE     IRF2 inhibits ZIKV replication by promoting FAM111A expression to
            enhance the host restriction effect of RFC3
  JOURNAL   Virol J 18 (1), 256 (2021)
   PUBMED   34930359
  REMARK    GeneRIF: IRF2 inhibits ZIKV replication by promoting FAM111A
            expression to enhance the host restriction effect of RFC3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Uhlmann,F., Cai,J., Gibbs,E., O'Donnell,M. and Hurwitz,J.
  TITLE     Deletion analysis of the large subunit p140 in human replication
            factor C reveals regions required for complex formation and
            replication activities
  JOURNAL   J Biol Chem 272 (15), 10058-10064 (1997)
   PUBMED   9092549
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Wood,R.D. and Shivji,M.K.
  TITLE     Which DNA polymerases are used for DNA-repair in eukaryotes?
  JOURNAL   Carcinogenesis 18 (4), 605-610 (1997)
   PUBMED   9111189
  REMARK    Review article
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Uhlmann,F., Cai,J., Flores-Rozas,H., Dean,F.B., Finkelstein,J.,
            O'Donnell,M. and Hurwitz,J.
  TITLE     In vitro reconstitution of human replication factor C from its five
            subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (13), 6521-6526 (1996)
   PUBMED   8692848
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Okumura,K., Nogami,M., Taguchi,H., Dean,F.B., Chen,M., Pan,Z.Q.,
            Hurwitz,J., Shiratori,A., Murakami,Y., Ozawa,K. et al.
  TITLE     Assignment of the 36.5-kDa (RFC5), 37-kDa (RFC4), 38-kDa (RFC3),
            and 40-kDa (RFC2) subunit genes of human replication factor C to
            chromosome bands 12q24.2-q24.3, 3q27, 13q12.3-q13, and 7q11.23
  JOURNAL   Genomics 25 (1), 274-278 (1995)
   PUBMED   7774928
REFERENCE   10 (residues 1 to 356)
  AUTHORS   O'Donnell,M., Onrust,R., Dean,F.B., Chen,M. and Hurwitz,J.
  TITLE     Homology in accessory proteins of replicative polymerases--E. coli
            to humans
  JOURNAL   Nucleic Acids Res 21 (1), 1-3 (1993)
   PUBMED   8441605
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC000149.2 and AA447424.1.
            
            Summary: The elongation of primed DNA templates by DNA polymerase
            delta and DNA polymerase epsilon requires the accessory proteins
            proliferating cell nuclear antigen (PCNA) and replication factor C
            (RFC). RFC, also named activator 1, is a protein complex consisting
            of five distinct subunits of 140, 40, 38, 37, and 36 kDa. This gene
            encodes the 38 kDa subunit. This subunit is essential for the
            interaction between the 140 kDa subunit and the core complex that
            consists of the 36, 37, and 40 kDa subunits. Alternatively spliced
            transcript variants encoding distinct isoforms have been described.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.123849.1,
                                           SRR1803615.175648.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380071.8/ ENSP00000369411.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q13.2"
     Protein         1..356
                     /product="replication factor C subunit 3 isoform 1"
                     /note="RFC, 38 kD subunit; A1 38 kDa subunit; RF-C 38 kDa
                     subunit; activator 1 subunit 3; activator 1 38 kDa
                     subunit; replication factor C 38 kDa subunit; replication
                     factor C (activator 1) 3, 38kDa"
                     /calculated_mol_wt=40425
     Region          3..339
                     /region_name="PRK12402"
                     /note="replication factor C small subunit 2; Reviewed"
                     /db_xref="CDD:237090"
     Site            20
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P40938.2)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (P40938.2)"
     CDS             1..356
                     /gene="RFC3"
                     /gene_synonym="RFC38"
                     /coded_by="NM_002915.4:31..1101"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9352.1"
                     /db_xref="GeneID:5983"
                     /db_xref="HGNC:HGNC:9971"
                     /db_xref="MIM:600405"
ORIGIN      
        1 mslwvdkyrp cslgrldyhk eqaaqlrnlv qcgdfphllv ygpsgagkkt rimcilrely
       61 gvgveklrie hqtittpskk kieistiasn yhlevnpsda gnsdrvviqe mlktvaqsqq
      121 letnsqrdfk vvlltevdkl tkdaqhalrr tmekymstcr lilccnstsk vippirsrcl
      181 avrvpapsie dichvlstvc kkeglnlpsq lahrlaeksc rnlrkallmc eacrvqqypf
      241 tadqeipetd wevylretan aivsqqtpqr llevrgrlye llthcippei imkgllsell
      301 hncdgqlkge vaqmaayyeh rlqlgskaiy hleafvakfm alykkfmedg legmmf
//
LOCUS       NP_001350234             178 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear distribution protein nudE-like 1 isoform 3 [Mus musculus].
ACCESSION   NP_001350234
VERSION     NP_001350234.1
DBSOURCE    REFSEQ: accession NM_001363305.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Das,B.K., Gogoi,J., Kannan,A., Gao,L., Xing,W., Mohan,S. and
            Zhao,H.
  TITLE     The Cytoplasmic Dynein Associated Protein NDE1 Regulates
            Osteoclastogenesis by Modulating M-CSF and RANKL Signaling Pathways
  JOURNAL   Cells 11 (1), 13 (2021)
   PUBMED   35011575
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Amberg,N. and Hippenmeyer,S.
  TITLE     Genetic mosaic dissection of candidate genes in mice using mosaic
            analysis with double markers
  JOURNAL   STAR Protoc 2 (4), 100939 (2021)
   PUBMED   34825212
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kim,Y.B., Hlavaty,D., Maycock,J. and Lechler,T.
  TITLE     Roles for Ndel1 in keratin organization and desmosome function
  JOURNAL   Mol Biol Cell 32 (20), ar2 (2021)
   PUBMED   34319758
  REMARK    GeneRIF: Roles for Ndel1 in keratin organization and desmosome
            function.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Gavrilovici,C., Jiang,Y., Kiroski,I., Sterley,T.L., Vandal,M.,
            Bains,J., Park,S.K., Rho,J.M., Teskey,G.C. and Nguyen,M.D.
  TITLE     Behavioral Deficits in Mice with Postnatal Disruption of Ndel1 in
            Forebrain Excitatory Neurons: Implications for Epilepsy and
            Neuropsychiatric Disorders
  JOURNAL   Cereb Cortex Commun 2 (1), tgaa096 (2021)
   PUBMED   33615226
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Ozeki,Y., Tomoda,T., Kleiderlein,J., Kamiya,A., Bord,L., Fujii,K.,
            Okawa,M., Yamada,N., Hatten,M.E., Snyder,S.H., Ross,C.A. and
            Sawa,A.
  TITLE     Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents
            binding to NudE-like (NUDEL) and inhibits neurite outgrowth
  JOURNAL   Proc Natl Acad Sci U S A 100 (1), 289-294 (2003)
   PUBMED   12506198
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13969]
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Ko,J., Humbert,S., Bronson,R.T., Takahashi,S., Kulkarni,A.B., Li,E.
            and Tsai,L.H.
  TITLE     p35 and p39 are essential for cyclin-dependent kinase 5 function
            during neurodevelopment
  JOURNAL   J Neurosci 21 (17), 6758-6771 (2001)
   PUBMED   11517264
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Sweeney,K.J., Prokscha,A. and Eichele,G.
  TITLE     NudE-L, a novel Lis1-interacting protein, belongs to a family of
            vertebrate coiled-coil proteins
  JOURNAL   Mech Dev 101 (1-2), 21-33 (2001)
   PUBMED   11231056
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Niethammer,M., Smith,D.S., Ayala,R., Peng,J., Ko,J., Lee,M.S.,
            Morabito,M. and Tsai,L.H.
  TITLE     NUDEL is a novel Cdk5 substrate that associates with LIS1 and
            cytoplasmic dynein
  JOURNAL   Neuron 28 (3), 697-711 (2000)
   PUBMED   11163260
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Sasaki,S., Shionoya,A., Ishida,M., Gambello,M.J., Yingling,J.,
            Wynshaw-Boris,A. and Hirotsune,S.
  TITLE     A LIS1/NUDEL/cytoplasmic dynein heavy chain complex in the
            developing and adult nervous system
  JOURNAL   Neuron 28 (3), 681-696 (2000)
   PUBMED   11163259
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL603662.11.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.227774.1,
                                           SRR17253014.5336141.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 42.09 cM"
     Protein         1..178
                     /product="nuclear distribution protein nudE-like 1 isoform
                     3"
                     /note="nuclear distribution protein nudE-like 1; protein
                     Nudel; nuclear disribution gene E like; nuclear
                     distribution gene E-like homolog 1"
                     /calculated_mol_wt=18562
     Region          <6..142
                     /region_name="NUDE_C"
                     /note="NUDE protein, C-terminal conserved region;
                     pfam04880"
                     /db_xref="CDD:461464"
     CDS             1..178
                     /gene="Ndel1"
                     /gene_synonym="2600006O07Rik; MITAP1; mNudE-L; mNudel;
                     NUDEL"
                     /coded_by="NM_001363305.1:571..1107"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:83431"
                     /db_xref="MGI:MGI:1932915"
ORIGIN      
        1 mmtwseqkdl rqelavrerq qevtrksaps sptldcekmd savqaslslp atpvgkgten
       61 sfpspkaipn gfgtspltps arisalnivg dllrkvgale sklaacrnfa kdqasrksyv
      121 pgsvncgvmn sngpecprsg ratffhkgav ngfdpapppp glgssrpssa pgmlplsv
//
LOCUS       NP_001350150             276 aa            linear   ROD 27-APR-2025
DEFINITION  gasdermin-A2 isoform 2 [Mus musculus].
ACCESSION   NP_001350150
VERSION     NP_001350150.1
DBSOURCE    REFSEQ: accession NM_001363221.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Fattinger,S.A., Maurer,L., Geiser,P., Bernard,E.M., Enz,U.,
            Ganguillet,S., Gul,E., Kroon,S., Demarco,B., Mack,V., Furter,M.,
            Barthel,M., Pelczar,P., Shao,F., Broz,P., Sellin,M.E. and
            Hardt,W.D.
  TITLE     Gasdermin D is the only Gasdermin that provides protection against
            acute Salmonella gut infection in mice
  JOURNAL   Proc Natl Acad Sci U S A 120 (48), e2315503120 (2023)
   PUBMED   37988464
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Tamura,M., Tanaka,S., Fujii,T., Aoki,A., Komiyama,H., Ezawa,K.,
            Sumiyama,K., Sagai,T. and Shiroishi,T.
  TITLE     Members of a novel gene family, Gsdm, are expressed exclusively in
            the epithelium of the skin and gastrointestinal tract in a highly
            tissue-specific manner
  JOURNAL   Genomics 89 (5), 618-629 (2007)
   PUBMED   17350798
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Runkel,F., Marquardt,A., Stoeger,C., Kochmann,E., Simon,D.,
            Kohnke,B., Korthaus,D., Wattler,F., Fuchs,H., Hrabe de Angelis,M.,
            Stumm,G., Nehls,M., Wattler,S., Franz,T. and Augustin,M.
  TITLE     The dominant alopecia phenotypes Bareskin, Rex-denuded, and Reduced
            Coat 2 are caused by mutations in gasdermin 3
  JOURNAL   Genomics 84 (5), 824-835 (2004)
   PUBMED   15475261
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Evolutionary recombination hotspot around GSDML-GSDM locus is
            closely linked to the oncogenomic recombination hotspot around the
            PPP1R1B-ERBB2-GRB7 amplicon
  JOURNAL   Int J Oncol 24 (4), 757-763 (2004)
   PUBMED   15010812
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591125.20 and AK008613.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK008613.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN00849376,
                                           SAMN00849377 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 62.28 cM"
     Protein         1..276
                     /product="gasdermin-A2 isoform 2"
                     /note="gasdermin-2; gasderminA-2"
                     /calculated_mol_wt=30755
     Region          <19..66
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Region          85..249
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..276
                     /gene="Gsdma2"
                     /gene_synonym="2200001G21Rik; 2210006M16Rik;
                     2210009F20Rik; 2210411P14Rik; Gsdm2; GsdmA-2; Gsdml2"
                     /coded_by="NM_001363221.1:290..1120"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS88246.1"
                     /db_xref="GeneID:76758"
                     /db_xref="MGI:MGI:1921490"
ORIGIN      
        1 mcapttlswm cwsraappqg svnhkeavti pkgcvlayrv rqliiygkde wgipyictdn
       61 mptfnplcvl qrqgstvqmi sgemhedfkt lkkevqqetq eveklspvgr sslltslshl
      121 lgkkkelqdl eqmlegaldk ghevtlealp kdvlllkdam dailyflgal telseeqlki
      181 lvkslenkvl pvqlklvesi leqnflqdke dvfplrpdll sslgeedqil tealvglsgl
      241 evqrsgpqyt wnpdtchnlc alyaglsllh llsrds
//
LOCUS       NP_008937                227 aa            linear   PRI 27-APR-2025
DEFINITION  cleavage and polyadenylation specificity factor subunit 5 [Homo
            sapiens].
ACCESSION   NP_008937
VERSION     NP_008937.1
DBSOURCE    REFSEQ: accession NM_007006.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Liu,W., Pang,Y., Yu,X., Lu,D., Yang,Y., Meng,F., Xu,C., Yuan,L. and
            Nan,Y.
  TITLE     Pan-cancer analysis of NUDT21 and its effect on the proliferation
            of human head and neck squamous cell carcinoma
  JOURNAL   Aging (Albany NY) 16 (4), 3363-3385 (2024)
   PUBMED   38349866
  REMARK    GeneRIF: Pan-cancer analysis of NUDT21 and its effect on the
            proliferation of human head and neck squamous cell carcinoma.
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Liu,M., Chen,X., Gu,Z., He,H., Chen,M., Kuai,L., Jia,Z., Li,Y.,
            Chen,Y., Hong,M. and Xiao,F.
  TITLE     Predictive Value of CFIm25 Expression in Peripheral Blood Monocytes
            for Coronary Atherosclerosis
  JOURNAL   Int J Med Sci 21 (3), 562-570 (2024)
   PUBMED   38322593
  REMARK    GeneRIF: Predictive Value of CFIm25 Expression in Peripheral Blood
            Monocytes for Coronary Atherosclerosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Huang,X.D., Chen,Y.W., Tian,L., Du,L., Cheng,X.C., Lu,Y.X.,
            Lin,D.D. and Xiao,F.J.
  TITLE     NUDT21 interacts with NDUFS2 to activate the PI3K/AKT pathway and
            promotes pancreatic cancer pathogenesis
  JOURNAL   J Cancer Res Clin Oncol 150 (1), 8 (2024)
   PUBMED   38195952
  REMARK    GeneRIF: NUDT21 interacts with NDUFS2 to activate the PI3K/AKT
            pathway and promotes pancreatic cancer pathogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Zhang,N., Liu,X., Huang,L., Zeng,J., Ma,C., Han,L., Li,W., Yu,J.
            and Yang,M.
  TITLE     LINC00921 reduces lung cancer radiosensitivity by destabilizing
            NUDT21 and driving aberrant MED23 alternative polyadenylation
  JOURNAL   Cell Rep 42 (12), 113479 (2023)
   PUBMED   37999979
  REMARK    GeneRIF: LINC00921 reduces lung cancer radiosensitivity by
            destabilizing NUDT21 and driving aberrant MED23 alternative
            polyadenylation.
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Kim,H. and Lee,Y.
  TITLE     Interaction of poly(A) polymerase with the 25-kDa subunit of
            cleavage factor I
  JOURNAL   Biochem Biophys Res Commun 289 (2), 513-518 (2001)
   PUBMED   11716503
REFERENCE   7  (residues 1 to 227)
  AUTHORS   de Vries,H., Ruegsegger,U., Hubner,W., Friedlein,A., Langen,H. and
            Keller,W.
  TITLE     Human pre-mRNA cleavage factor II(m) contains homologs of yeast
            proteins and bridges two other cleavage factors
  JOURNAL   EMBO J 19 (21), 5895-5904 (2000)
   PUBMED   11060040
REFERENCE   8  (residues 1 to 227)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Ruegsegger,U., Blank,D. and Keller,W.
  TITLE     Human pre-mRNA cleavage factor Im is related to spliceosomal SR
            proteins and can be reconstituted in vitro from recombinant
            subunits
  JOURNAL   Mol Cell 1 (2), 243-253 (1998)
   PUBMED   9659921
REFERENCE   10 (residues 1 to 227)
  AUTHORS   Ruegsegger,U., Beyer,K. and Keller,W.
  TITLE     Purification and characterization of human cleavage factor Im
            involved in the 3' end processing of messenger RNA precursors
  JOURNAL   J Biol Chem 271 (11), 6107-6113 (1996)
   PUBMED   8626397
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL535307.3, BC001403.2 and
            AC092140.4.
            
            Summary: The protein encoded by this gene is one subunit of a
            cleavage factor required for 3' RNA cleavage and polyadenylation
            processing. The interaction of the protein with the RNA is one of
            the earliest steps in the assembly of the 3' end processing complex
            and facilitates the recruitment of other processing factors. This
            gene encodes the 25kD subunit of the protein complex, which is
            composed of four polypeptides. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX537360.1, SRR1660803.7601.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300291.10/ ENSP00000300291.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..227
                     /product="cleavage and polyadenylation specificity factor
                     subunit 5"
                     /note="pre-mRNA cleavage factor Im (25kD); cleavage and
                     polyadenylation specific factor 5, 25 kD subunit; cleavage
                     factor Im complex 25 kDa subunit; cleavage and
                     polyadenylation specific factor 5, 25 kDa; pre-mRNA
                     cleavage factor Im, 25kD subunit; nudix motif 21; CPSF 25
                     kDa subunit; pre-mRNA cleavage factor Im 25 kDa subunit;
                     nucleoside diphosphate-linked moiety X motif 21; cleavage
                     and polyadenylation specificity factor 25 kDa subunit;
                     nudix (nucleoside diphosphate linked moiety X)-type motif
                     21; pre-mRNA cleavage factor Im 68 kDa subunit"
                     /calculated_mol_wt=26096
     Region          2..147
                     /region_name="Necessary for RNA-binding.
                     /evidence=ECO:0000269|PubMed:15169763"
                     /note="propagated from UniProtKB/Swiss-Prot (O43809.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.6;
                     propagated from UniProtKB/Swiss-Prot (O43809.1)"
     Site            15
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O43809.1)"
     Site            23
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:17172643,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O43809.1)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O43809.1)"
     Region          39..221
                     /region_name="NUDIX_Cfim25_Nudt21"
                     /note="25 kDa subunit of cleavage factor Im; cd18871"
                     /db_xref="CDD:467583"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (O43809.1)"
     Site            55
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:20479262,
                     ECO:0000312|PDB:3MDG, ECO:0000312|PDB:3MDI; propagated
                     from UniProtKB/Swiss-Prot (O43809.1)"
     Site            56
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O43809.1)"
     Site            63
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:20479262,
                     ECO:0000312|PDB:3MDG, ECO:0000312|PDB:3MDI; propagated
                     from UniProtKB/Swiss-Prot (O43809.1)"
     Region          81..160
                     /region_name="Necessary for interactions with PAPOLA and
                     PABPN1. /evidence=ECO:0000269|PubMed:15169763"
                     /note="propagated from UniProtKB/Swiss-Prot (O43809.1)"
     Region          102..104
                     /region_name="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:20479262,
                     ECO:0000269|PubMed:21295486, ECO:0000312|PDB:3MDG,
                     ECO:0000312|PDB:3MDI, ECO:0000312|PDB:3Q2T"
                     /note="propagated from UniProtKB/Swiss-Prot (O43809.1)"
     Region          109..130
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (O43809.1)"
     CDS             1..227
                     /gene="NUDT21"
                     /gene_synonym="CFIM25; CPSF5"
                     /coded_by="NM_007006.3:131..814"
                     /db_xref="CCDS:CCDS10760.1"
                     /db_xref="GeneID:11051"
                     /db_xref="HGNC:HGNC:13870"
                     /db_xref="MIM:604978"
ORIGIN      
        1 msvvppnrsq tgwprgvtqf gnkyiqqtkp ltlertinly pltnytfgtk eplyekdssv
       61 aarfqrmree fdkigmrrtv egvlivhehr lphvlllqlg ttffklpgge lnpgedeveg
      121 lkrlmteilg rqdgvlqdwv iddcignwwr pnfeppqypy ipahitkpke hkklflvqlq
      181 ekalfavpkn yklvaaplfe lydnapgygp iisslpqlls rfnfiyn
//
LOCUS       NP_001017922             475 aa            linear   PRI 27-APR-2025
DEFINITION  erythroid membrane-associated protein precursor [Homo sapiens].
ACCESSION   NP_001017922
VERSION     NP_001017922.1
DBSOURCE    REFSEQ: accession NM_001017922.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Li,J., Liu,X.G., Ge,R.L., Yin,Y.P., Liu,Y.D., Lu,W.P., Huang,M.,
            He,X.Y., Wang,J., Cai,G., Sun,S.H. and Yuan,J.H.
  TITLE     The ligation between ERMAP, galectin-9 and dectin-2 promotes
            Kupffer cell phagocytosis and antitumor immunity
  JOURNAL   Nat Immunol 24 (11), 1813-1824 (2023)
   PUBMED   37813965
  REMARK    GeneRIF: The ligation between ERMAP, galectin-9 and dectin-2
            promotes Kupffer cell phagocytosis and antitumor immunity.
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Su,M., Lin,Y., Cui,C., Tian,X. and Lai,L.
  TITLE     ERMAP is a B7 family-related molecule that negatively regulates T
            cell and macrophage responses
  JOURNAL   Cell Mol Immunol 18 (8), 1920-1933 (2021)
   PUBMED   32620788
  REMARK    GeneRIF: ERMAP is a B7 family-related molecule that negatively
            regulates T cell and macrophage responses.
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Belsito,A., Costa,D., Fiorito,C., De Iorio,G., Casamassimi,A.,
            Perrotta,S. and Napoli,C.
  TITLE     Erythrocyte genotyping for transfusion-dependent patients at the
            Azienda Universitaria Policlinico of Naples
  JOURNAL   Transfus Apher Sci 52 (1), 72-77 (2015)
   PUBMED   25582271
  REMARK    GeneRIF: Through molecular genotyping we also identified
            polymorphisms in RhCE, Kell, Duffy, Colton, Lutheran and Scianna
            loci in donors and patients.
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Reid,M.E., Hue-Roye,K., Velliquette,R.W., Larimore,K.,
            Moscarelli,S., Ohswaldt,N. and Lomas-Francis,C.
  TITLE     SC*994C>T causes the Sc(null) phenotype in Pacific Islanders and
            successful transfusion of Sc3+ blood to a patient with anti-Sc3
  JOURNAL   Immunohematology 29 (2), 69-72 (2013)
   PUBMED   24094239
  REMARK    GeneRIF: the five known probands with the SC*994C>T silencing
            nucleotide change were from the Pacific Islands.
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Wagner,F.F., Poole,J. and Flegel,W.A.
  TITLE     Scianna antigens including Rd are expressed by ERMAP
  JOURNAL   Blood 101 (2), 752-757 (2003)
   PUBMED   12393480
  REMARK    GeneRIF: DNA sequencing demonstrates Scianna antigens including Rd
            are expressed by ERMAP.
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Su,Y.Y., Gordon,C.T., Ye,T.Z., Perkins,A.C. and Chui,D.H.
  TITLE     Human ERMAP: an erythroid adhesion/receptor transmembrane protein
  JOURNAL   Blood Cells Mol Dis 27 (5), 938-949 (2001)
   PUBMED   11783959
  REMARK    GeneRIF: A human cDNA and gene encoding for human ERMAP is cloned
            and characterized. The protein is sequenced and its expression
            analyzed.
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Xu,H., Foltz,L., Sha,Y., Madlansacay,M.R., Cain,C., Lindemann,G.,
            Vargas,J., Nagy,D., Harriman,B., Mahoney,W. and Schueler,P.A.
  TITLE     Cloning and characterization of human erythroid membrane-associated
            protein, human ERMAP
  JOURNAL   Genomics 76 (1-3), 2-4 (2001)
   PUBMED   11549310
  REMARK    GeneRIF: ERMAP, a unique member of the B30.2 domain protein family,
            is expressed in erythroid cells in fetal liver, adult bone marrow,
            reticulocytes and in circulating erythroblasts in 8-12-week fetal
            cord blood.
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Lewis,M., Kaita,H., Philipps,S., Giblett,E.R., Anderson,J.E.,
            McAlpine,P.J. and Nickel,B.
  TITLE     The position of the Radin blood group locus in relation to other
            chromosome l loci
  JOURNAL   Ann Hum Genet 44 (2), 179-184 (1980)
   PUBMED   6459052
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Lewis,M. and Kaita,H.
  TITLE     Genetic linkage between the Radin and Rh blood group loci
  JOURNAL   Vox Sang 37 (5), 286-289 (1979)
   PUBMED   118583
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX507568.1, AY049028.1,
            AL512353.16 and AF311285.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a cell surface
            transmembrane protein that may act as an erythroid cell receptor,
            possibly as a mediator of cell adhesion. Polymorphisms in this gene
            are responsible for the Scianna/Radin blood group system. Two
            transcript variants encoding the same protein have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the longer transcript.
            Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record represents the ERMAP*001.1.1
            allele.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314436.1, SRR1803616.246050.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372517.8/ ENSP00000361595.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..475
                     /product="erythroid membrane-associated protein precursor"
                     /note="erythroid membrane-associated protein; Radin blood
                     group (Rd); Scianna blood group (Sc); radin blood group
                     antigen; scianna blood group antigen"
                     /calculated_mol_wt=49574
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3049
     mat_peptide     30..475
                     /product="erythroid membrane-associated protein"
                     /calculated_mol_wt=49574
     Region          39..144
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          46..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409031"
     Region          62..66
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409031"
     Region          109..113
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409031"
     Region          123..128
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409031"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PL5.1)"
     Region          136..139
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409031"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PL5.1)"
     Region          230..412
                     /region_name="SPRY_PRY_TRIM20"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     20 (TRIM20), also known as pyrin; cd15813"
                     /db_xref="CDD:293985"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLN5; propagated from
                     UniProtKB/Swiss-Prot (Q96PL5.1)"
     CDS             1..475
                     /gene="ERMAP"
                     /gene_synonym="BTN5; PRO2801; RD; SC"
                     /coded_by="NM_001017922.2:254..1681"
                     /db_xref="CCDS:CCDS475.1"
                     /db_xref="GeneID:114625"
                     /db_xref="HGNC:HGNC:15743"
                     /db_xref="MIM:609017"
ORIGIN      
        1 memassagsw lsgcliplvf lrlsvhvsgh agdagkfhva llggtaellc plslwpgtvp
       61 kevrwlrspf pqrsqavhif rdgkdqdedl mpeykgrtvl vrdaqegsvt lqildvrled
      121 qgsyrcliqv gnlskedtvi lqvaapsvgs lspsavalav ilpvlvllim vclcliwkqr
      181 rakekllyeh vtevdnllsd hakekgklhk avkklrselk lkraaansgw rrarlhfvav
      241 tldpdtahpk lilsedqrcv rlgdrrqpvp dnpqrfdfvv silgseyftt gchywevyvg
      301 dktkwilgvc sesvsrkgkv taspanghwl lrqsrgneye altspqtsfr lkepprcvgi
      361 fldyeagvis fynvtnkshi ftfthnfsgp lrpffepclh dggkntaplv icselhksee
      421 sivprpegkg hangdvslkv nssllppkap elkdiilslp pdlgpalqel kapsf
//
LOCUS       NP_699166                348 aa            linear   PRI 27-APR-2025
DEFINITION  STE20-related kinase adapter protein alpha isoform 3 [Homo
            sapiens].
ACCESSION   NP_699166
VERSION     NP_699166.2
DBSOURCE    REFSEQ: accession NM_153335.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Smith,R.H.B., Khan,Z.M., Ung,P.M., Scopton,A.P., Silber,L.,
            Mack,S.M., Real,A.M., Schlessinger,A. and Dar,A.C.
  TITLE     Type II Binders Targeting the 'GLR-Out' Conformation of the
            Pseudokinase STRADalpha
  JOURNAL   Biochemistry 60 (4), 289-302 (2021)
   PUBMED   33440120
  REMARK    GeneRIF: Type II Binders Targeting the ''GLR-Out'' Conformation of
            the Pseudokinase STRADalpha.
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Alsaif,H.S., Khashab,H.Y.E.L. and Alkuraya,F.S.
  TITLE     Two further cases of polyhydramnios, megalencephaly, and
            symptomatic epilepsy syndrome, caused by a truncating variant in
            STRADA
  JOURNAL   Am J Med Genet A 185 (2), 604-607 (2021)
   PUBMED   33247513
  REMARK    GeneRIF: Two further cases of polyhydramnios, megalencephaly, and
            symptomatic epilepsy syndrome, caused by a truncating variant in
            STRADA.
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Milburn,C.C., Boudeau,J., Deak,M., Alessi,D.R. and van Aalten,D.M.
  TITLE     Crystal structure of MO25 alpha in complex with the C terminus of
            the pseudo kinase STE20-related adaptor
  JOURNAL   Nat Struct Mol Biol 11 (2), 193-200 (2004)
   PUBMED   14730349
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Boudeau,J., Baas,A.F., Deak,M., Morrice,N.A., Kieloch,A.,
            Schutkowski,M., Prescott,A.R., Clevers,H.C. and Alessi,D.R.
  TITLE     MO25alpha/beta interact with STRADalpha/beta enhancing their
            ability to bind, activate and localize LKB1 in the cytoplasm
  JOURNAL   EMBO J 22 (19), 5102-5114 (2003)
   PUBMED   14517248
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Baas,A.F., Boudeau,J., Sapkota,G.P., Smit,L., Medema,R.,
            Morrice,N.A., Alessi,D.R. and Clevers,H.C.
  TITLE     Activation of the tumour suppressor kinase LKB1 by the STE20-like
            pseudokinase STRAD
  JOURNAL   EMBO J 22 (12), 3062-3072 (2003)
   PUBMED   12805220
  REMARK    GeneRIF: Identification and characterization of an LKB1-specific
            adaptor protein and substrate, STRAD. Results imply that STRAD
            plays a key role in regulating the tumor suppressor activities of
            LKB1.
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Scanlan,M.J., Gout,I., Gordon,C.M., Williamson,B., Stockert,E.,
            Gure,A.O., Jager,D., Chen,Y.T., Mackay,A., O'Hare,M.J. and Old,L.J.
  TITLE     Humoral immunity to human breast cancer: antigen definition and
            quantitative analysis of mRNA expression
  JOURNAL   Cancer Immun 1, 4 (2001)
   PUBMED   12747765
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA049174.1, AY290821.2 and
            BQ682133.1.
            
            On Jun 19, 2003 this sequence version replaced NP_699166.1.
            
            Summary: The protein encoded by this gene contains a STE20-like
            kinase domain, but lacks several residues that are critical for
            catalytic activity, so it is termed a 'pseudokinase'. The protein
            forms a heterotrimeric complex with serine/threonine kinase 11
            (STK11, also known as LKB1) and the scaffolding protein calcium
            binding protein 39 (CAB39, also known as MO25). The protein
            activates STK11 leading to the phosphorylation of both proteins and
            excluding STK11 from the nucleus. The protein is necessary for
            STK11-induced G1 cell cycle arrest. A mutation in this gene has
            been shown to result in polyhydramnios, megalencephaly, and
            symptomatic epilepsy (PMSE) syndrome. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            Additional transcript variants have been described but their
            full-length nature is not known. [provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY290821.2, AK075005.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..348
                     /product="STE20-related kinase adapter protein alpha
                     isoform 3"
                     /note="STE20-like pseudokinase; STE20-related kinase
                     adapter protein alpha; protein kinase LYK5; serologically
                     defined breast cancer antigen NY-BR-96; STE20-related
                     kinase adaptor alpha"
                     /calculated_mol_wt=38466
     Region          33..330
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(38..41,46,48,61,63,94,110..113,158,162..163,165,
                     175..176)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..348
                     /gene="STRADA"
                     /gene_synonym="LYK5; NY-BR-96; PMSE; Stlk; STRAD; STRAD
                     alpha"
                     /coded_by="NM_153335.6:291..1337"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS11642.1"
                     /db_xref="GeneID:92335"
                     /db_xref="HGNC:HGNC:30172"
                     /db_xref="MIM:608626"
ORIGIN      
        1 msfltndass esiasfskqe vmssflpegg cyelltvigk gfedlmtvnl arykptgeyv
       61 tvrrinleac snemvtflqg elhvsklfnh pnivpyratf iadnelwvvt sfmaygsakd
      121 licthfmdgm nelaiayilq gvlkaldyih hmgyvhrsvk ashilisvdg kvylsglrsn
      181 lsmishgqrq rvvhdfpkys vkvlpwlspe vlqqnlqgyd aksdiysvgi tacelanghv
      241 pfkdmpatqm lleklngtvp clldtstipa eeltmspsrs vansglsdsl ttstprpsng
      301 dspshpyhrt fsphfhhfve qclqrnpdar ypcwpgpglr esrgcsgg
//
LOCUS       NP_573574                304 aa            linear   PRI 27-APR-2025
DEFINITION  GS homeobox 2 [Homo sapiens].
ACCESSION   NP_573574
VERSION     NP_573574.2
DBSOURCE    REFSEQ: accession NM_133267.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Zhuang,L., Yao,Y., Peng,L., Cui,F., Chen,C., Zhang,Y., Sun,L.,
            Yu,Q. and Lin,K.
  TITLE     Silencing GS Homeobox 2 Alleviates Gemcitabine Resistance in
            Pancreatic Cancer Cells by Activating SHH/GLI1 Signaling Pathway
  JOURNAL   Dig Dis Sci 67 (8), 3773-3782 (2022)
   PUBMED   34623580
  REMARK    GeneRIF: Silencing GS Homeobox 2 Alleviates Gemcitabine Resistance
            in Pancreatic Cancer Cells by Activating SHH/GLI1 Signaling
            Pathway.
REFERENCE   2  (residues 1 to 304)
  AUTHORS   De Mori,R., Severino,M., Mancardi,M.M., Anello,D., Tardivo,S.,
            Biagini,T., Capra,V., Casella,A., Cereda,C., Copeland,B.R.,
            Gagliardi,S., Gamucci,A., Ginevrino,M., Illi,B., Lorefice,E.,
            Musaev,D., Stanley,V., Micalizzi,A., Gleeson,J.G., Mazza,T.,
            Rossi,A. and Valente,E.M.
  TITLE     Agenesis of the putamen and globus pallidus caused by recessive
            mutations in the homeobox gene GSX2
  JOURNAL   Brain 142 (10), 2965-2978 (2019)
   PUBMED   31412107
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Zeng,W.J., Yang,Y.L., Liu,Z.Z., Wen,Z.P., Chen,Y.H., Hu,X.L.,
            Cheng,Q., Xiao,J., Zhao,J. and Chen,X.P.
  TITLE     Integrative Analysis of DNA Methylation and Gene Expression
            Identify a Three-Gene Signature for Predicting Prognosis in
            Lower-Grade Gliomas
  JOURNAL   Cell Physiol Biochem 47 (1), 428-439 (2018)
   PUBMED   29794476
  REMARK    GeneRIF: This study identified and validated a three-gene (EMP3,
            GSX2 and EMILIN3) prognostic signature in Lower-Grade Gliomas.
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Faedo,A., Laporta,A., Segnali,A., Galimberti,M., Besusso,D.,
            Cesana,E., Belloli,S., Moresco,R.M., Tropiano,M., Fuca,E., Wild,S.,
            Bosio,A., Vercelli,A.E., Biella,G. and Cattaneo,E.
  TITLE     Differentiation of human telencephalic progenitor cells into MSNs
            by inducible expression of Gsx2 and Ebf1
  JOURNAL   Proc Natl Acad Sci U S A 114 (7), E1234-E1242 (2017)
   PUBMED   28137879
  REMARK    GeneRIF: Data show that GS Homeobox 2 (Gsx2) and Early B-cell
            factor 1 (Ebf1) combined overexpression in human embryonic stem
            (hES) cells achieves high yields of medium spiny neurons (MSNs).
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Waclaw,R.R., Wang,B., Pei,Z., Ehrman,L.A. and Campbell,K.
  TITLE     Distinct temporal requirements for the homeobox gene Gsx2 in
            specifying striatal and olfactory bulb neuronal fates
  JOURNAL   Neuron 63 (4), 451-465 (2009)
   PUBMED   19709628
  REMARK    GeneRIF: Gsx2 specifies striatal projection neuron and olfactory
            bulb interneuron identity at distinct time points during
            neurogenesis in transgenic mice.
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Dauwerse,J.G., De Die-Smulders,C.E., Bakker,E., Breuning,M.H. and
            Peters,D.J.
  TITLE     Heterozygous truncating mutation in the human homeobox gene GSH2
            has no discernable phenotypic effect
  JOURNAL   J Med Genet 39 (9), 686-688 (2002)
   PUBMED   12205114
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Cools,J., Mentens,N., Odero,M.D., Peeters,P., Wlodarska,I.,
            Delforge,M., Hagemeijer,A. and Marynen,P.
  TITLE     Evidence for position effects as a variant ETV6-mediated
            leukemogenic mechanism in myeloid leukemias with a
            t(4;12)(q11-q12;p13) or t(5;12)(q31;p13)
  JOURNAL   Blood 99 (5), 1776-1784 (2002)
   PUBMED   11861295
  REMARK    GeneRIF: ectopically expressed in myeloid leukemic cells with
            t(4;12)(q11-q12;p13), suggesting that expression of GSH2 was
            deregulated by the translocation, indicating a variant leukemogenic
            mechanism for translocations involving the 5' end of ETV6
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC110298.5.
            
            On Nov 23, 2018 this sequence version replaced NP_573574.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB028838.1, BC075090.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326902.7/ ENSP00000319118.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..304
                     /product="GS homeobox 2"
                     /note="homeobox protein GSH-2; genetic-screened homeobox
                     2"
                     /calculated_mol_wt=31900
     Region          116..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZM3.2)"
     Region          203..259
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          283..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZM3.2)"
     CDS             1..304
                     /gene="GSX2"
                     /gene_synonym="DMJDS2; GSH2"
                     /coded_by="NM_133267.3:183..1097"
                     /db_xref="CCDS:CCDS3494.1"
                     /db_xref="GeneID:170825"
                     /db_xref="HGNC:HGNC:24959"
                     /db_xref="MIM:616253"
ORIGIN      
        1 msrsfyvdsl iikdtsrpap slpephpgpd ffiplgmppp lvmsvsgpgc psrksgafcv
       61 cplcvtshlh ssrgsvgags ggagagvtga ggsgvagaag alpllkgqfs sapgdaqfcp
      121 rvnhahhhhh ppqhhhhhhq pqqpgsaaaa aaaaaaaaaa aalghpqhha pvctattynv
      181 adprrfhclt mggsdasqvp ngkrmrtaft stqllelere fssnmylsrl rrieiatyln
      241 lsekqvkiwf qnrrvkhkke gkgtqrnsha gckcvgsqvh yarsededsl spasanddke
      301 ispl
//
LOCUS       NP_001356112            1260 aa            linear   ROD 27-APR-2025
DEFINITION  ral GTPase-activating protein subunit beta isoform d [Mus
            musculus].
ACCESSION   NP_001356112
VERSION     NP_001356112.1
DBSOURCE    REFSEQ: accession NM_001369183.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1260)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1260)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1260)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1260)
  AUTHORS   Skorobogatko,Y., Dragan,M., Cordon,C., Reilly,S.M., Hung,C.W.,
            Xia,W., Zhao,P., Wallace,M., Lackey,D.E., Chen,X.W., Osborn,O.,
            Bogner-Strauss,J.G., Theodorescu,D., Metallo,C.M., Olefsky,J.M. and
            Saltiel,A.R.
  TITLE     RalA controls glucose homeostasis by regulating glucose uptake in
            brown fat
  JOURNAL   Proc Natl Acad Sci U S A 115 (30), 7819-7824 (2018)
   PUBMED   29915037
REFERENCE   5  (residues 1 to 1260)
  AUTHORS   Chen,X.W., Leto,D., Xiong,T., Yu,G., Cheng,A., Decker,S. and
            Saltiel,A.R.
  TITLE     A Ral GAP complex links PI 3-kinase/Akt signaling to RalA
            activation in insulin action
  JOURNAL   Mol Biol Cell 22 (1), 141-152 (2011)
   PUBMED   21148297
  REMARK    GeneRIF: study reports the identification and characterization of a
            Ral GAP complex (RG1 (KIAA1219), RGC2) that mediates the activation
            of RalA downstream of the PI 3-kinase/Akt pathway
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL844513.8 and AL663091.13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN00849374, SAMN00849375
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1260
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 78.72 cM"
     Protein         1..1260
                     /product="ral GTPase-activating protein subunit beta
                     isoform d"
                     /note="ral GTPase-activating protein beta subunit; ral
                     GTPase-activating protein subunit beta"
                     /calculated_mol_wt=139804
     CDS             1..1260
                     /gene="Ralgapb"
                     /gene_synonym="B230339M05Rik; p170"
                     /coded_by="NM_001369183.1:896..4678"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:228850"
                     /db_xref="MGI:MGI:2444531"
ORIGIN      
        1 mtygpsfppf kvpdedanli ppemdnecia qtwfrflhml snpvdlsnpa visstpkfqe
       61 qflnvsgmpq elsqypclkh lpqifframr gisclvdafl gisrprsdsa pptpvnrlsm
      121 pqsaavnttp phnrrhravt vnkatmktst vttahtskvq hqasstspls spnqtssepr
      181 plpaprrpkv nsilnlfgsw lfdaafvhck lhnginrdns mtasfiqill sykssiatqa
      241 smefrrkgsq mstdtmvsnp vfdasefpdn yeagraeacg tlcrifcskk tgeeilpayl
      301 srfymlliqg lqindyvchp vlasvilnsp plfccdlkgi dvvvpyfisa letilpdrel
      361 skfksyvnpt elrrssinil lsllplphhf gtvrsevvle gkfsnddsss ydkpitflsl
      421 klrlvnilig alqtetdpnn tqmilgamln ivqdsallea igcqmemggg ennlkshsrt
      481 nsgissasgg stepttpdse rpaqallrdy gstalntdsa agllirsihl vtqrlnsqwr
      541 qdmsislaal ellsglakvk vmvdsgdrkr aissvcsyiv yqcsrpaplh srdlhsmiva
      601 afqclcvwlt ehpdmldekd clkevleive lgisgskskn seqevkykgd kepnpasmrv
      661 kdaaeatltc imqllgafps psgpaspcsl vnettlikys rlptinkhsf ryfvldnsvi
      721 lamleqplgn eqndffpsvt vlvrgmsgrl awaqqlcllp rgakanqklf vpeprpvpkn
      781 dvgfkysvkh rpfpeevdki pfvkadlsip dlheivteel eerheklrsg maqqiayemh
      841 leqqsegelq krsfpdpvtd ckppppaqef qtarlflshf gflslealke pansrlpphl
      901 ialdstipgf fddigyldll pcrpfdtvfi fymkpgqktn qeilknvess rnvqphflef
      961 llslgwsvdv gkhpgwtghv stswsinscd dgegsepdei tssedvgasi fngqkkvlyy
     1021 adalteiafv vpspvesltd slesnisdqd sdsnmdlmpg ilkqppltle lvpnhtdsln
     1081 ssqrlspssr mkklpqgrpv pplgpetrvs vvwveryddi enfplsdlmt eistgvetta
     1141 nsstslrstt lekevpvifi hplntglfri kiqgatgkfn mviplvdgmi vsrralgflv
     1201 rqtvinicrr krlesdsysp phvrrkqkit divnkyrnkq lepefytalf qevglkncss
//
LOCUS       NP_444499                366 aa            linear   ROD 27-APR-2025
DEFINITION  DNA repair protein RAD51 homolog 3 isoform 2 [Mus musculus].
ACCESSION   NP_444499
VERSION     NP_444499.1
DBSOURCE    REFSEQ: accession NM_053269.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Tomaszowski,K.H., Roy,S., Guerrero,C., Shukla,P., Keshvani,C.,
            Chen,Y., Ott,M., Wu,X., Zhang,J., DiNardo,C.D., Schindler,D. and
            Schlacher,K.
  TITLE     Hypomorphic Brca2 and Rad51c double mutant mice display Fanconi
            anemia, cancer and polygenic replication stress
  JOURNAL   Nat Commun 14 (1), 1333 (2023)
   PUBMED   36906610
  REMARK    GeneRIF: Hypomorphic Brca2 and Rad51c double mutant mice display
            Fanconi anemia, cancer and polygenic replication stress.
            Erratum:[Nat Commun. 2024 Mar 12;15(1):2214. doi:
            10.1038/s41467-024-46561-9. PMID: 38472265]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Rojas,E., Martinez-Pacheco,M., Rodriguez-Sastre,M.A.,
            Ramos-Espinosa,P. and Valverde,M.
  TITLE     Post-transcriptional regulation of Rad51c by miR-222 contributes
            cellular transformation
  JOURNAL   PLoS One 15 (1), e0221681 (2020)
   PUBMED   31923208
  REMARK    GeneRIF: we demonstrate that miR-222 up-regulation, directly
            regulates Rad51c expression negatively, and impairs homologous
            recombination of double-strand break DNA repair during the
            initiation stage of cell transformation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Tumiati,M., Munne,P.M., Edgren,H., Eldfors,S., Hemmes,A. and
            Kuznetsov,S.G.
  TITLE     Rad51c- and Trp53-double-mutant mouse model reveals common features
            of homologous recombination-deficient breast cancers
  JOURNAL   Oncogene 35 (35), 4601-4610 (2016)
   PUBMED   26820992
  REMARK    GeneRIF: Similar to other BC models, Rad51c/p53 double-mutant mouse
            mammary tumors also reveal a propensity for genomic instability,
            but lack the focal amplification of the Met locus or distinct
            mutational signatures reported for other HR genes
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Tumiati,M., Hemmes,A., Uusivirta,S., Koopal,S., Kankainen,M.,
            Lehtonen,E. and Kuznetsov,S.G.
  TITLE     Loss of Rad51c accelerates tumourigenesis in sebaceous glands of
            Trp53-mutant mice
  JOURNAL   J Pathol 235 (1), 136-146 (2015)
   PUBMED   25270124
  REMARK    GeneRIF: a critical synergy between Rad51c and Trp53 in tumour
            progression and provide a predictable in vivo model system for
            studying mechanisms of Rad51c-mediated carcinogenesis
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Badie,S., Escandell,J.M., Bouwman,P., Carlos,A.R., Thanasoula,M.,
            Gallardo,M.M., Suram,A., Jaco,I., Benitez,J., Herbig,U.,
            Blasco,M.A., Jonkers,J. and Tarsounas,M.
  TITLE     BRCA2 acts as a RAD51 loader to facilitate telomere replication and
            capping
  JOURNAL   Nat Struct Mol Biol 17 (12), 1461-1469 (2010)
   PUBMED   21076401
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Kuznetsov,S.G., Haines,D.C., Martin,B.K. and Sharan,S.K.
  TITLE     Loss of Rad51c leads to embryonic lethality and modulation of
            Trp53-dependent tumorigenesis in mice
  JOURNAL   Cancer Res 69 (3), 863-872 (2009)
   PUBMED   19155299
  REMARK    GeneRIF: Rad51c mutation in DH-cis mice promoted the development of
            tumors of specialized sebaceous glands and suppressed tumors
            characteristic of Trp53 mutation. In addition, DH-cis females
            developed tumors significantly earlier than any other group.
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Kuznetsov,S., Pellegrini,M., Shuda,K., Fernandez-Capetillo,O.,
            Liu,Y., Martin,B.K., Burkett,S., Southon,E., Pati,D.,
            Tessarollo,L., West,S.C., Donovan,P.J., Nussenzweig,A. and
            Sharan,S.K.
  TITLE     RAD51C deficiency in mice results in early prophase I arrest in
            males and sister chromatid separation at metaphase II in females
  JOURNAL   J Cell Biol 176 (5), 581-592 (2007)
   PUBMED   17312021
  REMARK    GeneRIF: RAD51C has a late role in meiotic recombination.
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Liu,Y., Tarsounas,M., O'regan,P. and West,S.C.
  TITLE     Role of RAD51C and XRCC3 in genetic recombination and DNA repair
  JOURNAL   J Biol Chem 282 (3), 1973-1979 (2007)
   PUBMED   17114795
  REMARK    GeneRIF: the RAD51C-XRCC3-associated Holliday junction resolvase
            complex associates with crossovers and may play an essential role
            in the resolution of recombination intermediates prior to
            chromosome segregation
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Godthelp,B.C., Wiegant,W.W., van Duijn-Goedhart,A., Scharer,O.D.,
            van Buul,P.P., Kanaar,R. and Zdzienicka,M.Z.
  TITLE     Mammalian Rad51C contributes to DNA cross-link resistance, sister
            chromatid cohesion and genomic stability
  JOURNAL   Nucleic Acids Res 30 (10), 2172-2182 (2002)
   PUBMED   12000837
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Leasure,C.S., Chandler,J., Gilbert,D.J., Householder,D.B.,
            Stephens,R., Copeland,N.G., Jenkins,N.A. and Sharan,S.K.
  TITLE     Sequence, chromosomal location and expression analysis of the
            murine homologue of human RAD51L2/RAD51C
  JOURNAL   Gene 271 (1), 59-67 (2001)
   PUBMED   11410366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL669902.8, BY720217.1, BC090648.1 and AL596130.13.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090648.1, SRR1660819.148112.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164143 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 52.08 cM"
     Protein         1..366
                     /product="DNA repair protein RAD51 homolog 3 isoform 2"
                     /note="DNA repair protein RAD51 homolog 3; RAD51-like
                     protein 2; RAD51 homolog C"
                     /calculated_mol_wt=40544
     Region          1..117
                     /region_name="Required for Holliday junction resolution
                     activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924H5.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43502; propagated from
                     UniProtKB/Swiss-Prot (Q924H5.1)"
     Region          70..127
                     /region_name="Interaction with RAD51B, RAD51D and XRCC3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924H5.1)"
     Region          109..321
                     /region_name="Rad51C"
                     /note="RAD51C recombinase; cd19492"
                     /db_xref="CDD:410900"
     Site            order(119..124,152,233,276,308)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:410900"
     Region          343..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924H5.1)"
     Region          356..360
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924H5.1)"
     CDS             1..366
                     /gene="Rad51c"
                     /gene_synonym="R51H3; Rad51l2"
                     /coded_by="NM_053269.4:86..1186"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS25212.1"
                     /db_xref="GeneID:114714"
                     /db_xref="MGI:MGI:2150020"
ORIGIN      
        1 mqrelvgypl spavrgklva agfqtaedvl evkpselske vgiskeeale tlqilrrecl
       61 tnkprcagts vanekctale lleqehtqgf iitfcsaldn ilgggiplmk ttevcgvpgv
      121 gktqlcmqla vdvqipecfg gvageavfid tegsfmvdrv vslataciqh lhliagthte
      181 eehqkalkdf tlenilshiy yfrchdytel laqvyllpdf lsdhpkvqlv iidgiafpfr
      241 hdledlslrt rllnglaqqm islannhrla viltnqmttk idknqallvp algeswghaa
      301 tirlifhweq kqrfatlyks psqkestipf qitpqgfrda vvtaassqte sslnfrkrsr
      361 epeeec
//
LOCUS       NP_001257437             790 aa            linear   PRI 27-APR-2025
DEFINITION  tumor necrosis factor alpha-induced protein 3 [Homo sapiens].
ACCESSION   NP_001257437
VERSION     NP_001257437.1
DBSOURCE    REFSEQ: accession NM_001270508.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Wang,C., Huang,C., Li,Y., Bai,J., Zhao,K., Fang,Z. and Chen,J.
  TITLE     Hepatitis B surface antigen impairs TLR4 signaling by upregulating
            A20 expression in monocytes
  JOURNAL   Microbiol Spectr 12 (10), e0090924 (2024)
   PUBMED   39248482
  REMARK    GeneRIF: Hepatitis B surface antigen impairs TLR4 signaling by
            upregulating A20 expression in monocytes.
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Ning,F., Wang,H., Liang,Z. and Lan,J.
  TITLE     TNFAIP3 Overexpression Inhibits Diffuse Large B-Cell Lymphoma
            Progression by Promoting Autophagy through TLR4/MyD88/NF-kappaB
            Signaling Pathway
  JOURNAL   Discov Med 36 (187), 1627-1640 (2024)
   PUBMED   39190378
  REMARK    GeneRIF: TNFAIP3 Overexpression Inhibits Diffuse Large B-Cell
            Lymphoma Progression by Promoting Autophagy through
            TLR4/MyD88/NF-kappaB Signaling Pathway.
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Kommer,A., Meineck,M., Classen,P. and Weinmann-Menke,J.
  TITLE     A20 in Kidney Transplantation and Autoimmunity
  JOURNAL   Int J Mol Sci 25 (12), 6628 (2024)
   PUBMED   38928333
  REMARK    GeneRIF: A20 in Kidney Transplantation and Autoimmunity.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 790)
  AUTHORS   Ha,N.T., Trang,D.T., Nhat,P.V., Huong,P.T., Giang,N.H., Mao,C.V.,
            Binh,V.D., Vuong,N.B. and Xuan,N.T.
  TITLE     A20 promoted the phagocytosis of lymphoma cells by dendritic cells
            from activated B-cell-like non-Hodgkin lymphoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 1-9 (2024)
   PUBMED   38814241
  REMARK    GeneRIF: A20 promoted the phagocytosis of lymphoma cells by
            dendritic cells from activated B-cell-like non-Hodgkin lymphoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Hua,X., Hongbing,R., Juan,X., Jizan,L. and Beibei,Y.
  TITLE     Dysregulation of TNF-induced protein 3 and CCAAT/enhancer-binding
            protein beta in alveolar macrophages: Implications for systemic
            sclerosis-associated interstitial lung disease
  JOURNAL   Int J Rheum Dis 27 (5), e15174 (2024)
   PUBMED   38720423
  REMARK    GeneRIF: Dysregulation of TNF-induced protein 3 and
            CCAAT/enhancer-binding protein beta in alveolar macrophages:
            Implications for systemic sclerosis-associated interstitial lung
            disease.
REFERENCE   6  (residues 1 to 790)
  AUTHORS   Cooper,J.T., Stroka,D.M., Brostjan,C., Palmetshofer,A., Bach,F.H.
            and Ferran,C.
  TITLE     A20 blocks endothelial cell activation through a
            NF-kappaB-dependent mechanism
  JOURNAL   J Biol Chem 271 (30), 18068-18073 (1996)
   PUBMED   8663499
REFERENCE   7  (residues 1 to 790)
  AUTHORS   Song,H.Y., Rothe,M. and Goeddel,D.V.
  TITLE     The tumor necrosis factor-inducible zinc finger protein A20
            interacts with TRAF1/TRAF2 and inhibits NF-kappaB activation
  JOURNAL   Proc Natl Acad Sci U S A 93 (13), 6721-6725 (1996)
   PUBMED   8692885
REFERENCE   8  (residues 1 to 790)
  AUTHORS   Deuitch,N.T., Schwartz,D.M. and Aksentijevich,I.
  TITLE     Haploinsufficiency of A20
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   39715316
REFERENCE   9  (residues 1 to 790)
  AUTHORS   Opipari,A.W. Jr., Boguski,M.S. and Dixit,V.M.
  TITLE     The A20 cDNA induced by tumor necrosis factor alpha encodes a novel
            type of zinc finger protein
  JOURNAL   J Biol Chem 265 (25), 14705-14708 (1990)
   PUBMED   2118515
REFERENCE   10 (residues 1 to 790)
  AUTHORS   Dixit,V.M., Green,S., Sarma,V., Holzman,L.B., Wolf,F.W.,
            O'Rourke,K., Ward,P.A., Prochownik,E.V. and Marks,R.M.
  TITLE     Tumor necrosis factor-alpha induction of novel gene products in
            human endothelial cells including a macrophage-specific chemotaxin
  JOURNAL   J Biol Chem 265 (5), 2973-2978 (1990)
   PUBMED   2406243
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY009939.1, M59465.1 and
            CB528739.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene was identified as a gene whose expression is
            rapidly induced by the tumor necrosis factor (TNF). The protein
            encoded by this gene is a zinc finger protein and ubiqitin-editing
            enzyme, and has been shown to inhibit NF-kappa B activation as well
            as TNF-mediated apoptosis. The encoded protein, which has both
            ubiquitin ligase and deubiquitinase activities, is involved in the
            cytokine-mediated immune and inflammatory responses. Several
            transcript variants encoding the same protein have been found for
            this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All three variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.119981.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000612899.5/ ENSP00000481570.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.3"
     Protein         1..790
                     /product="tumor necrosis factor alpha-induced protein 3"
                     /EC_number="3.4.19.12"
                     /note="tumor necrosis factor inducible protein A20; zinc
                     finger protein A20; OTU domain-containing protein 7C;
                     putative DNA-binding protein A20; tumor necrosis factor,
                     alpha induced protein 3"
                     /calculated_mol_wt=89483
     mat_peptide     2..439
                     /product="A20p50. /id=PRO_0000418127"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
                     /calculated_mol_wt=50896
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P21580.1)"
     Region          41..261
                     /region_name="OTU_TNFAIP3"
                     /note="OTU (ovarian tumor) domain of tumor necrosis factor
                     alpha induced protein 3; cd22766"
                     /db_xref="CDD:438603"
     Region          58..300
                     /region_name="TRAF-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Site            order(98..99,101..103,149..151,155..156,158..159,167,171,
                     174,190..192,214..215,217..219,223..225,227,252,255..257)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438603"
     Region          157..159
                     /region_name="Interaction with ubiquitin.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Region          190..192
                     /region_name="Interaction with ubiquitin.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Region          224..227
                     /region_name="Interaction with ubiquitin.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Region          357..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Region          369..775
                     /region_name="Interaction with TNIP1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Region          384..409
                     /region_name="ZnF_A20"
                     /note="A20-like zinc fingers; smart00259"
                     /db_xref="CDD:128555"
     Region          386..453
                     /region_name="Interaction with RIPK1.
                     /evidence=ECO:0000269|PubMed:19131965"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Region          415..434
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Site            439..440
                     /site_type="cleavage"
                     /note="Cleavage, by MALT1; propagated from
                     UniProtKB/Swiss-Prot (P21580.1)"
     mat_peptide     440..790
                     /product="A20p37. /id=PRO_0000418128"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
                     /calculated_mol_wt=38606
     Region          447..468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P21580.1)"
     Region          475..500
                     /region_name="ZnF_A20"
                     /note="A20-like zinc fingers; smart00259"
                     /db_xref="CDD:128555"
     Region          550..583
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P21580.1)"
     Region          604..629
                     /region_name="ZnF_A20"
                     /note="A20-like zinc fingers; smart00259"
                     /db_xref="CDD:128555"
     Region          605..655
                     /region_name="Required for proteasomal degradation of
                     UBE2N and UBE2D3, TRAF6 deubiquitination, and TAX1BP1
                     interaction with UBE2N. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Region          606..790
                     /region_name="Sufficient for inhibitory activity of
                     TNF-induced NF-kappa-B activity. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P21580.1)"
     Region          654..679
                     /region_name="ZnF_A20"
                     /note="A20-like zinc fingers; smart00259"
                     /db_xref="CDD:128555"
     Region          689..712
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Region          697..790
                     /region_name="Required for lysosomal localization and for
                     TRAF2 lysosomal degradation"
                     /note="propagated from UniProtKB/Swiss-Prot (P21580.1)"
     Region          713..738
                     /region_name="ZnF_A20"
                     /note="A20-like zinc fingers; smart00259"
                     /db_xref="CDD:128555"
     Region          759..784
                     /region_name="ZnF_A20"
                     /note="A20-like zinc fingers; smart00259"
                     /db_xref="CDD:128555"
     CDS             1..790
                     /gene="TNFAIP3"
                     /gene_synonym="A20; AIFBL1; AISBL; OTUD7C; TNFA1P2"
                     /coded_by="NM_001270508.2:300..2672"
                     /db_xref="CCDS:CCDS5187.1"
                     /db_xref="GeneID:7128"
                     /db_xref="HGNC:HGNC:11896"
                     /db_xref="MIM:191163"
ORIGIN      
        1 maeqvlpqal ylsnmrkavk irertpedif kptngiihhf ktmhrytlem frtcqfcpqf
       61 reiihkalid rniqatlesq kklnwcrevr klvalktngd gnclmhatsq ymwgvqdtdl
      121 vlrkalfstl ketdtrnfkf rwqleslksq efvetglcyd trnwndewdn likmastdtp
      181 marsglqyns leeihifvlc nilrrpiivi sdkmlrsles gsnfaplkvg giylplhwpa
      241 qecyrypivl gydshhfvpl vtlkdsgpei ravplvnrdr grfedlkvhf ltdpenemke
      301 kllkeylmvi eipvqgwdhg tthlinaakl deanlpkein lvddyfelvq heykkwqens
      361 eqgrreghaq npmepsvpql slmdvkcetp ncpffmsvnt qplchecser rqknqnklpk
      421 lnskpgpegl pgmalgasrg eayeplawnp eestggphsa pptapspflf settamkcrs
      481 pgcpftlnvq hngfcerchn arqlhashap dhtrhldpgk cqaclqdvtr tfngicstcf
      541 krttaeasss lstslppsch qrsksdpsrl vrspsphsch ragndapagc lsqaartpgd
      601 rtgtskcrka gcvyfgtpen kgfctlcfie yrenkhfaaa sgkvsptasr fqntipclgr
      661 ecgtlgstmf egycqkcfie aqnqrfheak rteeqlrssq rrdvprttqs tsrpkcaras
      721 cknilacrse elcmecqhpn qrmgpgahrg epapedppkq rcrapacdhf gnakcngycn
      781 ecfqfkqmyg
//
LOCUS       NP_001001433             325 aa            linear   PRI 27-APR-2025
DEFINITION  syntaxin-16 isoform a [Homo sapiens].
ACCESSION   NP_001001433
VERSION     NP_001001433.1
DBSOURCE    REFSEQ: accession NM_001001433.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Odom,J., Bacino,C.A., Karaviti,L.P., Bi,W. and Hoyos-Martinez,A.
  TITLE     Intrafamilial phenotypic heterogeneity in siblings with
            pseudohypoparathyroidism 1B due to maternal STX16 deletion
  JOURNAL   J Pediatr Endocrinol Metab 37 (1), 84-89 (2023)
   PUBMED   38095637
  REMARK    GeneRIF: Intrafamilial phenotypic heterogeneity in siblings with
            pseudohypoparathyroidism 1B due to maternal STX16 deletion.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Kiuchi,Z., Reyes,M., Hanna,P., Sharma,A., DeClue,T., Olney,R.C.,
            Tebben,P. and Juppner,H.
  TITLE     Progression of PTH Resistance in Autosomal Dominant
            Pseudohypoparathyroidism Type Ib Due to Maternal STX16 Deletions
  JOURNAL   J Clin Endocrinol Metab 107 (2), e681-e687 (2022)
   PUBMED   34477200
  REMARK    GeneRIF: Progression of PTH Resistance in Autosomal Dominant
            Pseudohypoparathyroidism Type Ib Due to Maternal STX16 Deletions.
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Chen,Y., Gan,B.Q. and Tang,B.L.
  TITLE     Syntaxin 16: unraveling cellular physiology through a ubiquitous
            SNARE molecule
  JOURNAL   J Cell Physiol 225 (2), 326-332 (2010)
   PUBMED   20589833
  REMARK    Review article
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Chua,C.E. and Tang,B.L.
  TITLE     Syntaxin 16 is enriched in neuronal dendrites and may have a role
            in neurite outgrowth
  JOURNAL   Mol Membr Biol 25 (1), 35-45 (2008)
   PUBMED   17852734
  REMARK    GeneRIF: Syntaxin 16 may thus play a role in neurite outgrowth and
            perhaps other specific dendritic anterograde/retrograde traffic.
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Dulubova,I., Yamaguchi,T., Gao,Y., Min,S.W., Huryeva,I.,
            Sudhof,T.C. and Rizo,J.
  TITLE     How Tlg2p/syntaxin 16 'snares' Vps45
  JOURNAL   EMBO J 21 (14), 3620-3631 (2002)
   PUBMED   12110575
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Mallard,F., Tang,B.L., Galli,T., Tenza,D., Saint-Pol,A., Yue,X.,
            Antony,C., Hong,W., Goud,B. and Johannes,L.
  TITLE     Early/recycling endosomes-to-TGN transport involves two SNARE
            complexes and a Rab6 isoform
  JOURNAL   J Cell Biol 156 (4), 653-664 (2002)
   PUBMED   11839770
REFERENCE   8  (residues 1 to 325)
  AUTHORS   Simonsen,A., Bremnes,B., Ronning,E., Aasland,R. and Stenmark,H.
  TITLE     Syntaxin-16, a putative Golgi t-SNARE
  JOURNAL   Eur J Cell Biol 75 (3), 223-231 (1998)
   PUBMED   9587053
REFERENCE   9  (residues 1 to 325)
  AUTHORS   Tang,B.L., Low,D.Y., Lee,S.S., Tan,A.E. and Hong,W.
  TITLE     Molecular cloning and localization of human syntaxin 16, a member
            of the syntaxin family of SNARE proteins
  JOURNAL   Biochem Biophys Res Commun 242 (3), 673-679 (1998)
   PUBMED   9464276
REFERENCE   10 (residues 1 to 325)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL050327.6, AL139349.37 and
            KF456959.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that is a member of the
            syntaxin or t-SNARE (target-SNAP receptor) family. These proteins
            are found on cell membranes and serve as the targets for V-SNARES
            (vesicle-SNAP receptors) permitting specific synaptic vesicle
            docking and fusion. A microdeletion in the region of chromosome 20
            where this gene is located has been associated with
            pseudohypoparathyroidism type Ib. Multiple transcript variants have
            been found for this gene. Read-through transcription also exists
            between this gene and the neighboring downstream
            aminopeptidase-like 1 (NPEPL1) gene. [provided by RefSeq, Mar
            2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a, also referred to as
            isoform B).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.213711.1,
                                           SRR1803617.15616.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371141.8/ ENSP00000360183.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..325
                     /product="syntaxin-16 isoform a"
                     /calculated_mol_wt=36900
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BVI5; propagated from
                     UniProtKB/Swiss-Prot (O14662.3)"
     Region          75..301
                     /region_name="COG5325"
                     /note="t-SNARE complex subunit, syntaxin [Intracellular
                     trafficking and secretion]"
                     /db_xref="CDD:227635"
     Region          233..291
                     /region_name="SNARE_syntaxin16"
                     /note="SNARE motif of syntaxin 16; cd15845"
                     /db_xref="CDD:277198"
     Site            order(234,236..237,239..244,246..248,250..251,253..255,
                     257..258,260..262,264..265,267..272,274..279,281..286,
                     288..290)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277198"
     Site            264
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277198"
     Site            302..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14662.3)"
     CDS             1..325
                     /gene="STX16"
                     /gene_synonym="SYN-16; SYN16"
                     /coded_by="NM_001001433.3:725..1702"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13468.1"
                     /db_xref="GeneID:8675"
                     /db_xref="HGNC:HGNC:11431"
                     /db_xref="MIM:603666"
ORIGIN      
        1 matrrltdaf lllrnnsiqn rqllaeqvss hitssplhsr siaaeldela ddrmalvsgi
       61 sldpeaaigv tkrpppkwvd gvdeiqydvg rikqkmkela slhdkhlnrp tlddsseeeh
      121 aieittqeit qlfhrcqrav qalpsrarac seqegrllgn vvaslaqalq elstsfrhaq
      181 sgylkrmknr eersqhffdt svplmddgdd ntlyhrgfte dqlvlveqnt lmveererei
      241 rqivqsisdl neifrdlgam iveqgtvldr idynveqsci ktedglkqlh kaeqyqkknr
      301 kmlvililfv iiivlivvlv gvksr
//
LOCUS       NP_038562                732 aa            linear   ROD 27-APR-2025
DEFINITION  prolyl 3-hydroxylase 3 precursor [Mus musculus].
ACCESSION   NP_038562 XP_990096 XP_990127 XP_990160
VERSION     NP_038562.2
DBSOURCE    REFSEQ: accession NM_013534.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Ishikawa,Y., Taga,Y., Zientek,K., Mizuno,N., Salo,A.M.,
            Semenova,O., Tufa,S.F., Keene,D.R., Holden,P., Mizuno,K.,
            Gould,D.B., Myllyharju,J. and Bachinger,H.P.
  TITLE     Type I and type V procollagen triple helix uses different subsets
            of the molecular ensemble for lysine posttranslational
            modifications in the rER
  JOURNAL   J Biol Chem 296, 100453 (2021)
   PUBMED   33631195
  REMARK    GeneRIF: Type I and type V procollagen triple helix uses different
            subsets of the molecular ensemble for lysine posttranslational
            modifications in the rER.
REFERENCE   3  (residues 1 to 732)
  AUTHORS   Hudson,D.M., Weis,M., Rai,J., Joeng,K.S., Dimori,M., Lee,B.H.,
            Morello,R. and Eyre,D.R.
  TITLE     P3h3-null and Sc65-null Mice Phenocopy the Collagen Lysine
            Under-hydroxylation and Cross-linking Abnormality of Ehlers-Danlos
            Syndrome Type VIA
  JOURNAL   J Biol Chem 292 (9), 3877-3887 (2017)
   PUBMED   28115524
  REMARK    GeneRIF: both P3h3- and Sc65-null mice displayed a similar pattern
            of severe under-hydroxylation of lysines, particularly at
            cross-linking sites in type I collagen from bone, skin, dentin,
            cornea, and aorta, revealing a complex evolution and interplay
            between the proteins forming the machinery of collagen prolyl
            3-hydroxylation and lysyl hydroxylation in the ER
REFERENCE   4  (residues 1 to 732)
  AUTHORS   Heard,M.E., Besio,R., Weis,M., Rai,J., Hudson,D.M., Dimori,M.,
            Zimmerman,S.M., Kamykowski,J.A., Hogue,W.R., Swain,F.L.,
            Burdine,M.S., Mackintosh,S.G., Tackett,A.J., Suva,L.J., Eyre,D.R.
            and Morello,R.
  TITLE     Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum
            Complex Regulating Collagen Lysyl Hydroxylation
  JOURNAL   PLoS Genet 12 (4), e1006002 (2016)
   PUBMED   27119146
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 732)
  AUTHORS   Vranka,J., Stadler,H.S. and Bachinger,H.P.
  TITLE     Expression of prolyl 3-hydroxylase genes in embryonic and adult
            mouse tissues
  JOURNAL   Cell Struct Funct 34 (2), 97-104 (2009)
   PUBMED   19652424
  REMARK    GeneRIF: This report characterizes expression of the P3H1, P3H2 and
            P3H3 genes in embryonic and adult mice.
REFERENCE   6  (residues 1 to 732)
  AUTHORS   Capellini,T.D., Dunn,M.P., Passamaneck,Y.J., Selleri,L. and Di
            Gregorio,A.
  TITLE     Conservation of notochord gene expression across chordates:
            insights from the Leprecan gene family
  JOURNAL   Genesis 46 (11), 683-696 (2008)
   PUBMED   18798549
  REMARK    GeneRIF: Study found that all 3 mouse Leprecan genes Lepre1,
            leprel1 and leprel2 are expressed in the notochord; additionally,
            they are expressed in dorsal root ganglia, limb buds, branchial
            arches, and developing kidneys.
REFERENCE   7  (residues 1 to 732)
  AUTHORS   Vranka,J.A., Sakai,L.Y. and Bachinger,H.P.
  TITLE     Prolyl 3-hydroxylase 1, enzyme characterization and identification
            of a novel family of enzymes
  JOURNAL   J Biol Chem 279 (22), 23615-23621 (2004)
   PUBMED   15044469
REFERENCE   8  (residues 1 to 732)
  AUTHORS   Jarnum,S., Kjellman,C., Darabi,A., Nilsson,I., Edvardsen,K. and
            Aman,P.
  TITLE     LEPREL1, a novel ER and Golgi resident member of the Leprecan
            family
  JOURNAL   Biochem Biophys Res Commun 317 (2), 342-351 (2004)
   PUBMED   15063763
REFERENCE   9  (residues 1 to 732)
  AUTHORS   Ansari-Lari,M.A., Oeltjen,J.C., Schwartz,S., Zhang,Z., Muzny,D.M.,
            Lu,J., Gorrell,J.H., Chinault,A.C., Belmont,J.W., Miller,W. and
            Gibbs,R.A.
  TITLE     Comparative sequence analysis of a gene-rich cluster at human
            chromosome 12p13 and its syntenic region in mouse chromosome 6
  JOURNAL   Genome Res 8 (1), 29-40 (1998)
   PUBMED   9445485
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC142254.4.
            
            On or before May 4, 2006 this sequence version replaced
            XP_990160.1, XP_990127.1, XP_990096.1, NP_038562.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ441086.1, BC003726.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 59.17 cM"
     Protein         1..732
                     /product="prolyl 3-hydroxylase 3 precursor"
                     /EC_number="1.14.11.7"
                     /note="gene rich cluster, B; protein B; leprecan-like
                     protein 2"
                     /calculated_mol_wt=79593
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2126
     Region          15..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CG70.1)"
     mat_peptide     20..732
                     /product="Prolyl 3-hydroxylase 3. /id=PRO_0000240361"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CG70.1)"
                     /calculated_mol_wt=79593
     Region          39..72
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CG70.1)"
     Region          152..185
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CG70.1)"
     Region          214..247
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CG70.1)"
     Region          312..345
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CG70.1)"
     Site            327
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CG70.1)"
     Site            458
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CG70.1)"
     Region          470..670
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     Region          676..732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CG70.1)"
     Region          729..732
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU10138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CG70.1)"
     CDS             1..732
                     /gene="P3h3"
                     /gene_synonym="Grcb; Leprel2"
                     /coded_by="NM_013534.5:31..2229"
                     /db_xref="CCDS:CCDS20533.1"
                     /db_xref="GeneID:14789"
                     /db_xref="MGI:MGI:1315208"
ORIGIN      
        1 mlrllrllll lllpppgspe ppeppglaql spgsppqapd llyadglray sagawapava
       61 llrealrsra algrarqecg ascaaepgaa lpsqllgaph pvsgpgvwep lllratlrra
      121 ecltqcavrr lgpggaarlr vgsalrdafr rrepynylqr ayyqlkkldl aasaahtffv
      181 anpthlqmre dmakyrrmsa irpqsfrdlv tplywaaydt glelleqrea alalpqleea
      241 lqgslahmes craacegpee hqgaeeegeg sqgglyeaia ghwirvlqcr qhcvadtatr
      301 pgrsfpvqdf llsqlrrlhe ayaqvgnmsq amenvlsvll fypedeaakk alnqyqtqlg
      361 eprpdlgpre diqrfilrsl gekrqlyyam ehlgtsfkdp dswtpealip kalrerlred
      421 qekkpwdhqp pqqkplahwk dallmegvtl tqdaqqlngs eravldgllt saecgvllql
      481 akdaaqagar sgyrgrrsph spherfeglt vlkaaqlara gtvgrpgakl llevservrt
      541 ltqayfsper plhlsfthlv crsaiegeqe qrmdlshpvh adncvldpdt gecwreppay
      601 tyrdysglly lnddfkggdl fftqpnaltv taqvrprcgr lvafssggen phgvwavtrg
      661 rrcalalwht wapehseqew teakellqee eeeeeeedil srdpspepps hklqrvqeka
      721 gkprrvrvre el
//
LOCUS       NP_849190                128 aa            linear   PRI 27-APR-2025
DEFINITION  organic solute transporter subunit beta [Homo sapiens].
ACCESSION   NP_849190
VERSION     NP_849190.2
DBSOURCE    REFSEQ: accession NM_178859.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Chan,J.W., Neo,C.W.Y., Ghosh,S., Choi,H., Lim,S.C., Tai,E.S. and
            Teo,A.K.K.
  TITLE     HNF1A binds and regulates the expression of SLC51B to facilitate
            the uptake of estrone sulfate in human renal proximal tubule
            epithelial cells
  JOURNAL   Cell Death Dis 14 (5), 302 (2023)
   PUBMED   37137894
  REMARK    GeneRIF: HNF1A binds and regulates the expression of SLC51B to
            facilitate the uptake of estrone sulfate in human renal proximal
            tubule epithelial cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Zhou,Y., Ye,C., Lou,Y., Liu,J., Ye,S., Chen,L., Lei,J., Guo,S.,
            Zeng,S. and Yu,L.
  TITLE     Epigenetic Mechanisms Underlying Organic Solute Transporter beta
            Repression in Colorectal Cancer
  JOURNAL   Mol Pharmacol 97 (4), 259-266 (2020)
   PUBMED   32005758
  REMARK    GeneRIF: Study found lower organic solute transporter beta
            (OSTbeta) expression in colon cancer tissues compared with adjacent
            normal tissues and revealed the epigenetic mechanisms of it and
            proved that p300 controls OSTbeta expression through modulating
            H3K27Ac state at OSTbeta promoter region and hence causes low
            expression of OSTbeta in colorectal cancer.
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Xu,S., Soroka,C.J., Sun,A.Q., Backos,D.S., Mennone,A., Suchy,F.J.
            and Boyer,J.L.
  TITLE     A Novel Di-Leucine Motif at the N-Terminus of Human Organic Solute
            Transporter Beta Is Essential for Protein Association and Membrane
            Localization
  JOURNAL   PLoS One 11 (6), e0158269 (2016)
   PUBMED   27351185
  REMARK    GeneRIF: Dileucine motif in the extracellular N-terminal region is
            essential for OSTB plasma membrane targeting.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Schaffner,C.A., Mwinyi,J., Gai,Z., Thasler,W.E., Eloranta,J.J. and
            Kullak-Ublick,G.A.
  TITLE     The organic solute transporters alpha and beta are induced by
            hypoxia in human hepatocytes
  JOURNAL   Liver Int 35 (4), 1152-1161 (2015)
   PUBMED   24703425
  REMARK    GeneRIF: Hepatic OSTalpha-OSTbeta expression is induced by hypoxia.
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Landrier,J.F., Eloranta,J.J., Vavricka,S.R. and Kullak-Ublick,G.A.
  TITLE     The nuclear receptor for bile acids, FXR, transactivates human
            organic solute transporter-alpha and -beta genes
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 290 (3), G476-G485 (2006)
   PUBMED   16269519
  REMARK    GeneRIF: OSTalpha/OSTbeta expression is induced by bile acids
            through ligand-dependent transactivation of both OST genes by the
            nuclear bile acid receptor/farnesoid X receptor (FXR).
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Lee,H., Zhang,Y., Lee,F.Y., Nelson,S.F., Gonzalez,F.J. and
            Edwards,P.A.
  TITLE     FXR regulates organic solute transporters alpha and beta in the
            adrenal gland, kidney, and intestine
  JOURNAL   J Lipid Res 47 (1), 201-214 (2006)
   PUBMED   16251721
  REMARK    GeneRIF: overexpression of human OSTalpha and OSTbeta facilitated
            the uptake of conjugated chenodeoxycholate and the activation of
            FXR target genes
REFERENCE   8  (residues 1 to 128)
  AUTHORS   Ballatori,N., Christian,W.V., Lee,J.Y., Dawson,P.A., Soroka,C.J.,
            Boyer,J.L., Madejczyk,M.S. and Li,N.
  TITLE     OSTalpha-OSTbeta: a major basolateral bile acid and steroid
            transporter in human intestinal, renal, and biliary epithelia
  JOURNAL   Hepatology 42 (6), 1270-1279 (2005)
   PUBMED   16317684
  REMARK    GeneRIF: the selective localization of OSTalpha and OSTbeta to the
            basolateral plasma membrane of epithelial cells responsible for
            bile acid and sterol reabsorption.
REFERENCE   9  (residues 1 to 128)
  AUTHORS   Dawson,P.A., Hubbert,M., Haywood,J., Craddock,A.L., Zerangue,N.,
            Christian,W.V. and Ballatori,N.
  TITLE     The heteromeric organic solute transporter alpha-beta,
            Ostalpha-Ostbeta, is an ileal basolateral bile acid transporter
  JOURNAL   J Biol Chem 280 (8), 6960-6968 (2005)
   PUBMED   15563450
REFERENCE   10 (residues 1 to 128)
  AUTHORS   Seward,D.J., Koh,A.S., Boyer,J.L. and Ballatori,N.
  TITLE     Functional complementation between a novel mammalian polygenic
            transport complex and an evolutionarily ancient organic solute
            transporter, OSTalpha-OSTbeta
  JOURNAL   J Biol Chem 278 (30), 27473-27482 (2003)
   PUBMED   12719432
  REMARK    GeneRIF: OSTbeta has roles in biological transport and is widely
            expressed in human tissues
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AI793107.1, AK129601.1 and AC013553.14.
            
            On Nov 25, 2009 this sequence version replaced NP_849190.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK129601.1, ERR279837.11029.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334287.3/ ENSP00000335292.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..128
                     /product="organic solute transporter subunit beta"
                     /note="OST-beta; organic solute transporter beta subunit;
                     solute carrier family 51 beta subunit; solute carrier
                     family 51 subunit beta; SLC51A1 binding protein"
                     /calculated_mol_wt=14215
     Region          3..122
                     /region_name="OSTbeta"
                     /note="Organic solute transporter subunit beta protein;
                     pfam15048"
                     /db_xref="CDD:405697"
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW2.2)"
     CDS             1..128
                     /gene="SLC51B"
                     /gene_synonym="OSTB; OSTBETA; PBAM2; SLC51A1BP"
                     /coded_by="NM_178859.4:305..691"
                     /db_xref="CCDS:CCDS10199.1"
                     /db_xref="GeneID:123264"
                     /db_xref="HGNC:HGNC:29956"
                     /db_xref="MIM:612085"
ORIGIN      
        1 mehsegapgd pagtvvpqel leemlwffrv edaspwnhsi lalaavvvii smvllgrsiq
       61 asrkekmqpp eketpevlhl deakdhnsln nlretllsek pnlaqvelel kerdvlsvfl
      121 pdvpetes
//
LOCUS       NP_001129162             267 aa            linear   PRI 27-APR-2025
DEFINITION  proenkephalin-A preproprotein [Homo sapiens].
ACCESSION   NP_001129162
VERSION     NP_001129162.1
DBSOURCE    REFSEQ: accession NM_001135690.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Bullen,A.L., Katz,R., Poursadrolah,S., Short,S.A.P., Long,D.L.,
            Cheung,K.L., Sharma,S., Al-Rousan,T., Fregoso,A., Schulte,J.,
            Gutierrez,O.M., Shlipak,M.G., Cushman,M., Ix,J.H. and Rifkin,D.E.
  TITLE     Plasma proenkephalin A and incident chronic kidney disease and
            albuminuria in the REasons for Geographic And Racial Differences in
            Stroke (REGARDS) cohort
  JOURNAL   BMC Nephrol 25 (1), 16 (2024)
   PUBMED   38200454
  REMARK    GeneRIF: Plasma proenkephalin A and incident chronic kidney disease
            and albuminuria in the REasons for Geographic And Racial
            Differences in Stroke (REGARDS) cohort.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Lin,L.C., Chuan,M.H., Liu,J.H., Liao,H.W., Ng,L.L., Magnusson,M.,
            Jujic,A., Pan,H.C., Wu,V.C. and Forni,L.G.
  TITLE     Proenkephalin as a biomarker correlates with acute kidney injury: a
            systematic review with meta-analysis and trial sequential analysis
  JOURNAL   Crit Care 27 (1), 481 (2023)
   PUBMED   38057904
  REMARK    GeneRIF: Proenkephalin as a biomarker correlates with acute kidney
            injury: a systematic review with meta-analysis and trial sequential
            analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Zhang,H.P., Yu,Z.L., Wu,B.B. and Sun,F.R.
  TITLE     PENK inhibits osteosarcoma cell migration by activating the
            PI3K/Akt signaling pathway
  JOURNAL   J Orthop Surg Res 15 (1), 162 (2020)
   PUBMED   32334633
  REMARK    GeneRIF: PENK inhibits osteosarcoma cell migration by activating
            the PI3K/Akt signaling pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Gruber,P., Fluri,F., Schweizer,J., Luft,A., Muller,B.,
            Christ-Crain,M. and Katan,M.
  TITLE     Proenkephalin A Adds No Incremental Prognostic Value After Acute
            Ischemic Stroke
  JOURNAL   Clin Appl Thromb Hemost 26, 1076029619895318 (2020)
   PUBMED   31973568
  REMARK    GeneRIF: PENK-A was neither independently associated with
            functional outcome (OR: 1.29, 95% CI: 0.16-10.35) nor mortality
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Liu,F., Housley,P.R. and Wilson,S.P.
  TITLE     Initial processing of human proenkephalin in bovine chromaffin
            cells
  JOURNAL   J Neurochem 67 (4), 1457-1462 (1996)
   PUBMED   8858927
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Lindberg,I. and Shaw,E.
  TITLE     Posttranslational processing of proenkephalin in SK-N-MC cells:
            evidence for phosphorylation
  JOURNAL   J Neurochem 58 (2), 448-453 (1992)
   PUBMED   1729392
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Litt,M., Buroker,N.E., Kondoleon,S., Douglass,J., Liston,D.,
            Sheehy,R. and Magenis,R.E.
  TITLE     Chromosomal localization of the human proenkephalin and
            prodynorphin genes
  JOURNAL   Am J Hum Genet 42 (2), 327-334 (1988)
   PUBMED   2893547
REFERENCE   8  (residues 1 to 267)
  AUTHORS   Legon,S., Glover,D.M., Hughes,J., Lowry,P.J., Rigby,P.W. and
            Watson,C.J.
  TITLE     The structure and expression of the preproenkephalin gene
  JOURNAL   Nucleic Acids Res 10 (24), 7905-7918 (1982)
   PUBMED   6761648
REFERENCE   9  (residues 1 to 267)
  AUTHORS   Noda,M., Teranishi,Y., Takahashi,H., Toyosato,M., Notake,M.,
            Nakanishi,S. and Numa,S.
  TITLE     Isolation and structural organization of the human preproenkephalin
            gene
  JOURNAL   Nature 297 (5865), 431-434 (1982)
   PUBMED   6281660
REFERENCE   10 (residues 1 to 267)
  AUTHORS   Comb,M., Seeburg,P.H., Adelman,J., Eiden,L. and Herbert,E.
  TITLE     Primary structure of the human Met- and Leu-enkephalin precursor
            and its mRNA
  JOURNAL   Nature 295 (5851), 663-666 (1982)
   PUBMED   7057924
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314908.1 and BI496610.1.
            
            Summary: This gene encodes a preproprotein that is proteolytically
            processed to generate multiple protein products. These products
            include the pentapeptide opioids Met-enkephalin and Leu-enkephalin,
            which are stored in synaptic vesicles, then released into the
            synapse where they bind to mu- and delta-opioid receptors to
            modulate the perception of pain. Other non-opioid cleavage products
            may function in distinct biological activities. [provided by
            RefSeq, Jul 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.173079.1,
                                           SRR1660805.88477.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000451791.7/ ENSP00000400894.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..267
                     /product="proenkephalin-A preproprotein"
                     /note="preproenkephalin; enkephalin A; proenkephalin-A;
                     peptide F"
                     /calculated_mol_wt=28175
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=2630
     mat_peptide     25..97
                     /product="Synenkephalin. /id=PRO_0000008242"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=8198
     Region          25..70
                     /region_name="Opiods_neuropep"
                     /note="Vertebrate endogenous opioids neuropeptide;
                     pfam01160"
                     /db_xref="CDD:426090"
     mat_peptide     100..104
                     /product="Met-enkephalin.
                     /evidence=ECO:0000269|PubMed:656131. /id=PRO_0000008243"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=574
     mat_peptide     107..111
                     /product="Met-enkephalin.
                     /evidence=ECO:0000269|PubMed:656131. /id=PRO_0000008244"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=574
     Site            111..112
                     /site_type="cleavage"
                     /note="Cleavage, by CTSL.
                     /evidence=ECO:0000250|UniProtKB:P01211; propagated from
                     UniProtKB/Swiss-Prot (P01210.1)"
     Site            112..113
                     /site_type="cleavage"
                     /note="Cleavage, by CTSL.
                     /evidence=ECO:0000250|UniProtKB:P01211; propagated from
                     UniProtKB/Swiss-Prot (P01210.1)"
     mat_peptide     114..133
                     /product="PENK(114-133).
                     /evidence=ECO:0000250|UniProtKB:P04094.
                     /id=PRO_0000377691"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=2267
     Site            133..134
                     /site_type="cleavage"
                     /note="Cleavage, by CTSL.
                     /evidence=ECO:0000250|UniProtKB:P01211; propagated from
                     UniProtKB/Swiss-Prot (P01210.1)"
     mat_peptide     136..140
                     /product="Met-enkephalin. /id=PRO_0000008246"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=574
     mat_peptide     143..183
                     /product="PENK(143-183).
                     /evidence=ECO:0000250|UniProtKB:P04094.
                     /id=PRO_0000377692"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=4587
     Region          163..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
     mat_peptide     186..193
                     /product="Met-enkephalin-Arg-Gly-Leu.
                     /evidence=ECO:0000269|PubMed:2982830. /id=PRO_0000008248"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=900
     mat_peptide     210..214
                     /product="Met-enkephalin. /id=PRO_0000008250"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=574
     Site            214..215
                     /site_type="cleavage"
                     /note="Cleavage, by CTSL.
                     /evidence=ECO:0000250|UniProtKB:P01211; propagated from
                     UniProtKB/Swiss-Prot (P01210.1)"
     Site            215..216
                     /site_type="cleavage"
                     /note="Cleavage, by CTSL.
                     /evidence=ECO:0000250|UniProtKB:P01211; propagated from
                     UniProtKB/Swiss-Prot (P01210.1)"
     Site            218..219
                     /site_type="cleavage"
                     /note="Cleavage, by CTSL.
                     /evidence=ECO:0000250|UniProtKB:P01211; propagated from
                     UniProtKB/Swiss-Prot (P01210.1)"
     mat_peptide     230..234
                     /product="Leu-enkephalin. /id=PRO_0000008252"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=556
     mat_peptide     237..258
                     /product="PENK(237-258).
                     /evidence=ECO:0000250|UniProtKB:P04094.
                     /id=PRO_0000377693"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=2474
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04094; propagated from
                     UniProtKB/Swiss-Prot (P01210.1)"
     mat_peptide     261..267
                     /product="Met-enkephalin-Arg-Phe.
                     /evidence=ECO:0000250|UniProtKB:P04094.
                     /id=PRO_0000008254"
                     /note="propagated from UniProtKB/Swiss-Prot (P01210.1)"
                     /calculated_mol_wt=877
     CDS             1..267
                     /gene="PENK"
                     /gene_synonym="PE; PENK-A"
                     /coded_by="NM_001135690.3:133..936"
                     /db_xref="CCDS:CCDS6168.1"
                     /db_xref="GeneID:5179"
                     /db_xref="HGNC:HGNC:8831"
                     /db_xref="MIM:131330"
ORIGIN      
        1 marfltlctw llllgpglla tvraecsqdc atcsyrlvrp adinflacvm ecegklpslk
       61 iwetckellq lskpelpqdg tstlrenskp eeshllakry ggfmkryggf mkkmdelypm
      121 epeeeangse ilakryggfm kkdaeeddsl anssdllkel letgdnrers hhqdgsdnee
      181 evskryggfm rglkrspqle deakelqkry ggfmrrvgrp ewwmdyqkry ggflkrfaea
      241 lpsdeegesy skevpemekr yggfmrf
//
LOCUS       NP_115919                807 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 594 [Homo sapiens].
ACCESSION   NP_115919 XP_290737 XP_945729
VERSION     NP_115919.1
DBSOURCE    REFSEQ: accession NM_032530.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA448705.1, BX472376.1, AB058774.2, AK131271.1, AC087500.16 and
            AC012146.25.
            
            On or before Jul 5, 2007 this sequence version replaced
            XP_290737.6, XP_945729.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.125900.1,
                                           SRR1660805.31344.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000575779.2/ ENSP00000461032.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..807
                     /product="zinc finger protein 594"
                     /note="zinc finger protein HZF18"
                     /calculated_mol_wt=93776
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JF6.3)"
     Region          96..518
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          105..121
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          129..149
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(134,136,138,140..141,144..145,148,162,164,168..169,
                     172..173,176,190,192,194,196..197,200..201,204)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          157..177
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          185..205
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          213..233
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          241..261
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(246,248,250,252..253,256..257,260,274,276,280..281,
                     284..285,288,302,304,306,308..309,312..313,316)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          269..289
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          297..317
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          325..345
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          351..370
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          378..398
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          402..791
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          406..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          434..454
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(439,441,443,445..446,449..450,453,467,469,473..474,
                     477..478,481,495,497,499,501..502,505..506,509)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          462..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          490..510
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          570..590
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          598..618
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(603,605,607,609..610,613..614,617,631,633,637..638,
                     641..642,645,659,661,663,665..666,669..670,673)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          626..646
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          654..674
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          682..702
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          710..730
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          736..755
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          763..783
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     CDS             1..807
                     /gene="ZNF594"
                     /coded_by="NM_032530.2:142..2565"
                     /db_xref="CCDS:CCDS42241.1"
                     /db_xref="GeneID:84622"
                     /db_xref="HGNC:HGNC:29392"
ORIGIN      
        1 mkewkskmei seekksaraa seklqrqitq ecelvetsns edrllkhwvs plkdamrhlp
       61 sqesgiremh iipqkaivge ighgcnegek ilsagesshr yevsgqnfkq ksgltehqki
      121 hninktyeck ecektfnrss nliihqriht gnkpyvcnec gkdsnqssnl iihqrihtgk
      181 kpyichecgk dfnqssnlvr hkqihsggnp yeckecgkaf kgssnlvlhq rihsrgkpyl
      241 cnkcgkafsq stdliihhri htgekpyecy dcgqmfsqss hlvphqriht gekplkcnec
      301 ekafrqhshl tehqrlhsge kpyechrcgk tfsgrtaflk hqrlhageki eecektfskd
      361 eelreeqrih qeekaywcnq cgrnfqgtsd lirhqvthtg ekpyeckecg ktfnqssdll
      421 rhhrihsgek pcvcskcgks frgssdlirh hrvhtgekpy ecsecgkafs qrshlvthqk
      481 ihtgekpyqc tecgkafrrr slliqhrrih sgekpyecke cgklfiwrta flkhqslhtg
      541 eklecektfs qdeelrgeqk ihqeakaywc nqcgrafqgs sdlirhqvth trekpyecke
      601 cgktfnqssd llrhhrihsg ekpyvcnkcg ksfrgssdli khhrihtgek pyecsecgka
      661 fsqrshlath qkihtgekpy qcsecgnafr rrslliqhrr lhsgekpyec kecgklfmwh
      721 taflkhqrlh agekleecek tfskdeelrk eqrthqekkv ywcnqcsrtf qgssdlirhq
      781 vthtrekpye ckecgktqse lrpsets
//
LOCUS       NP_620129                268 aa            linear   PRI 27-APR-2025
DEFINITION  R3H domain-containing protein 4 [Homo sapiens].
ACCESSION   NP_620129
VERSION     NP_620129.2
DBSOURCE    REFSEQ: accession NM_138774.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005379.1 and BC012775.2.
            
            On Jul 30, 2003 this sequence version replaced NP_620129.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012775.2, SRR3476690.1065571.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361574.10/ ENSP00000355385.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..268
                     /product="R3H domain-containing protein 4"
                     /note="R3H domain-containing protein C19orf22"
                     /calculated_mol_wt=30219
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96D70.3)"
     Region          46..182
                     /region_name="R3H-assoc"
                     /note="R3H-associated N-terminal domain; pfam13902"
                     /db_xref="CDD:464031"
     Region          142..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96D70.3)"
     Region          188..247
                     /region_name="R3H"
                     /note="R3H domain; pfam01424"
                     /db_xref="CDD:460206"
     CDS             1..268
                     /gene="R3HDM4"
                     /gene_synonym="C19orf22"
                     /coded_by="NM_138774.4:63..869"
                     /db_xref="CCDS:CCDS12048.1"
                     /db_xref="GeneID:91300"
                     /db_xref="HGNC:HGNC:28270"
ORIGIN      
        1 mvalenpecg peaaegtpgg rrllplpscl palassqvkr lsasrrkqhf inqavrnsdl
       61 vpkakgrksl qrlentqyll tlletdgglp gledgdlapp aspgifaeac nnatyvevwn
      121 dfmnrsgeeq ervlrylede grskarrrgp grgedrrred paytprecfq risrrlravl
      181 krsripmetl etweerllrf fsvspqavyt amldnsferl llhavcqymd lisasadleg
      241 krqmkvsnrh ldflppglll sayleqhs
//
LOCUS       NP_001092108             708 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF169 [Homo sapiens].
ACCESSION   NP_001092108 XP_495886 XP_945281
VERSION     NP_001092108.1
DBSOURCE    REFSEQ: accession NM_001098638.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Roewenstrunk,J., Di Vona,C., Chen,J., Borras,E., Dong,C., Arato,K.,
            Sabido,E., Huen,M.S.Y. and de la Luna,S.
  TITLE     A comprehensive proteomics-based interaction screen that links
            DYRK1A to RNF169 and to the DNA damage response
  JOURNAL   Sci Rep 9 (1), 6014 (2019)
   PUBMED   30979931
  REMARK    GeneRIF: A comprehensive proteomics-based interaction screen that
            links DYRK1A to RNF169 and to the DNA damage response.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 708)
  AUTHORS   An,L., Dong,C., Li,J., Chen,J., Yuan,J., Huang,J., Chan,K.M.,
            Yu,C.H. and Huen,M.S.Y.
  TITLE     RNF169 limits 53BP1 deposition at DSBs to stimulate single-strand
            annealing repair
  JOURNAL   Proc Natl Acad Sci U S A 115 (35), E8286-E8295 (2018)
   PUBMED   30104380
  REMARK    GeneRIF: results highlight the interplay of RNF169 with 53BP1 in
            fine-tuning choice of DSB repair pathways.
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Hu,Q., Botuyan,M.V., Cui,G., Zhao,D. and Mer,G.
  TITLE     Mechanisms of Ubiquitin-Nucleosome Recognition and Regulation of
            53BP1 Chromatin Recruitment by RNF168/169 and RAD18
  JOURNAL   Mol Cell 66 (4), 473-487 (2017)
   PUBMED   28506460
  REMARK    GeneRIF: Ubiquitin ligases RNF168, RNF169, and RAD18 specifically
            bind histone H2A Lys13/15-ubiquitylated nucleosomes. 53BP1
            chromatin recruitment may be activated by RNF168 and blocked by
            RNF169 and RAD18.
REFERENCE   5  (residues 1 to 708)
  AUTHORS   Kitevski-LeBlanc,J., Fradet-Turcotte,A., Kukic,P., Wilson,M.D.,
            Portella,G., Yuwen,T., Panier,S., Duan,S., Canny,M.D., van
            Ingen,H., Arrowsmith,C.H., Rubinstein,J.L., Vendruscolo,M.,
            Durocher,D. and Kay,L.E.
  TITLE     The RNF168 paralog RNF169 defines a new class of ubiquitylated
            histone reader involved in the response to DNA damage
  JOURNAL   Elife 6, e23872 (2017)
   PUBMED   28406400
  REMARK    GeneRIF: The authors establish that RNF169 binds to ubiquitylated
            histone H2A-Lys13/Lys15 in a manner that involves its canonical
            ubiquitin-binding helix and a pair of arginine-rich motifs that
            interact with the nucleosome acidic patch.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 708)
  AUTHORS   Poulsen,M., Lukas,C., Lukas,J., Bekker-Jensen,S. and Mailand,N.
  TITLE     Human RNF169 is a negative regulator of the ubiquitin-dependent
            response to DNA double-strand breaks
  JOURNAL   J Cell Biol 197 (2), 189-199 (2012)
   PUBMED   22492721
  REMARK    GeneRIF: results show that RNF169 functions in a noncanonical
            fashion to harness RNF168-mediated protein recruitment to
            DSB-containing chromatin, thereby contributing to regulation of DSB
            repair pathway utilization.
REFERENCE   7  (residues 1 to 708)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 708)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   9  (residues 1 to 708)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 708)
  AUTHORS   Ohara,O., Nagase,T., Mitsui,G., Kohga,H., Kikuno,R., Hiraoka,S.,
            Takahashi,Y., Kitajima,S., Saga,Y. and Koseki,H.
  TITLE     Characterization of size-fractionated cDNA libraries generated by
            the in vitro recombination-assisted method
  JOURNAL   DNA Res 9 (2), 47-57 (2002)
   PUBMED   12056414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP000560.4, AB082522.1 and BU735906.1.
            
            On or before Jun 26, 2007 this sequence version replaced
            XP_495886.1, XP_945281.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB082522.1, DRR138518.431516.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299563.5/ ENSP00000299563.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..708
                     /product="E3 ubiquitin-protein ligase RNF169"
                     /EC_number="2.3.2.27"
                     /note="RING-type E3 ubiquitin transferase RNF169"
                     /calculated_mol_wt=77064
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Region          65..117
                     /region_name="RING-HC_RNF169"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 169 (RNF169) and similar proteins; cd16551"
                     /db_xref="CDD:438213"
     Region          96..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Region          170..238
                     /region_name="UDM1_RNF169"
                     /note="UDM1 (ubiquitin-dependent DSB recruitment module 1)
                     domain found in RING finger protein 169; cd22264"
                     /db_xref="CDD:409017"
     Site            order(177..178,181,183..184,186..187,193..194,197,
                     200..201,203..205,207..208,211,215)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:409017"
     Region          195..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Region          205..213
                     /region_name="UMI motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:30773093,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:30773093,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Region          491..555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            644
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Region          655..708
                     /region_name="MIU_RNF169_C"
                     /note="C-terminal motif interacting with ubiquitin domain
                     found in RING finger protein 169; cd21951"
                     /db_xref="CDD:409265"
     Region          665..682
                     /region_name="MIU motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            order(666,668..670,672..674,676..677,679..681,697..700)
                     /site_type="other"
                     /note="histone/ubiquitin binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409265"
     Region          689..701
                     /region_name="LR motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCN4.2)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NCN4.2)"
     CDS             1..708
                     /gene="RNF169"
                     /coded_by="NM_001098638.2:33..2159"
                     /db_xref="CCDS:CCDS41691.1"
                     /db_xref="GeneID:254225"
                     /db_xref="HGNC:HGNC:26961"
                     /db_xref="MIM:618650"
ORIGIN      
        1 maaagpstra ssaaaaaals rrgrrgrcde taaaktgapg pasgpsllvl sppllqpplp
       61 prpeesgcag cleppgeaaa lpcghslcrg caqraadaag pgcprcrarg pgwarrrard
      121 dgqadsevlg ecarrsqper crprrdggaa aagprpeqep raapaepdfi frapiklskp
      181 gelreeyesl rklreeklqe ekpsedqihk llpedtetgk rkmdeqkkrd eplvlktnle
      241 rcparlsdse neepsrgqmt qthrsafvsk nnsyslafla gklnskvers qscsdtaqer
      301 aksrvravpg nkakvttmtp asnpiigvll stqnnrcvsa pdltiekrlp fsslsslasl
      361 hkpersvspe sndsiseeln hfkpivcspc tppkrlpdgr vlspliikst prnlnrslqk
      421 qtsyeaspri lkkweqifqe rqikktlska tltslapemg eellgsegih sskekplvav
      481 ntrlsggqvl seytgptsad ldhfpsvsqt kaeqdsdnks steipletcc sselkgggsg
      541 tslereqfeg lgstpdakld ktcisramki ttvnsvlpqn svlggvlktk qqlktlnhfd
      601 ltngvlvesl seeplpslrr grkrhcktkh leqngslkkl rqtsgevgla ptdpvlreme
      661 qklqqeeedr qlalqlqrmf dnerrtvsrr kgsvdqyllr ssnmagak
//
LOCUS       NP_064709                312 aa            linear   PRI 27-APR-2025
DEFINITION  anamorsin isoform 1 [Homo sapiens].
ACCESSION   NP_064709
VERSION     NP_064709.2
DBSOURCE    REFSEQ: accession NM_020313.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Yuan,H., Zhong,M., Liu,J., Tang,S., Zhu,H., Wei,Q., Pu,B. and Li,Y.
  TITLE     Downregulation of CIAPIN1 regulates the proliferation, migration
            and glycolysis of breast cancer cells via inhibition of STAT3
            pathway
  JOURNAL   Sci Rep 14 (1), 20794 (2024)
   PUBMED   39242716
  REMARK    GeneRIF: Downregulation of CIAPIN1 regulates the proliferation,
            migration and glycolysis of breast cancer cells via inhibition of
            STAT3 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Wang,J., Zhou,Y., Ma,L., Cao,S., Gao,W., Xiong,Q., Wang,K. and
            Yang,L.
  TITLE     CIAPIN1 Targeted NHE1 and ERK1/2 to Suppress NSCLC Cells'
            Metastasis and Predicted Good Prognosis in NSCLC Patients Receiving
            Pulmonectomy
  JOURNAL   Oxid Med Cell Longev 2019, 1970818 (2019)
   PUBMED   31093311
  REMARK    GeneRIF: NHE1 (Na+/H+ exchanger 1) expression and ERK1/2
            phosphorylation decreased along with CIAPIN1 upregulation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Hao,Z., Li,X., Qiao,T. and Fan,D.
  TITLE     Successful expression and purification of human CIAPIN1 in
            baculovirus-insect cell system and application of this system to
            investigation of its potential methyltransferase activity
  JOURNAL   Int J Biol Macromol 42 (1), 27-32 (2008)
   PUBMED   17935775
  REMARK    GeneRIF: CIAPIN1 might be a DNA or RNA methyltransferase.
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Hao,Z., Li,X., Qiao,T., Du,R., Zhang,G. and Fan,D.
  TITLE     Subcellular localization of CIAPIN1
  JOURNAL   J Histochem Cytochem 54 (12), 1437-1444 (2006)
   PUBMED   16957168
  REMARK    GeneRIF: CIAPIN1 was localized in both the cytoplasm and the
            nucleus and was accumulated in the nucleolus. Bioinformatic
            prediction disclosed a putative nuclear localization signal and a
            putative nuclear export signal within human CIAPIN1.
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Hao,Z., Li,X., Qiao,T., Du,R., Hong,L. and Fan,D.
  TITLE     CIAPIN1 confers multidrug resistance by upregulating the expression
            of MDR-1 and MRP-1 in gastric cancer cells
  JOURNAL   Cancer Biol Ther 5 (3), 261-266 (2006)
   PUBMED   16410721
  REMARK    GeneRIF: it is concluded that CIAPIN1 confers multidrug resistance
            in gastric cancer cells, likely by upregulating MDR-1 and MRP-1
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Shibayama,H., Takai,E., Matsumura,I., Kouno,M., Morii,E.,
            Kitamura,Y., Takeda,J. and Kanakura,Y.
  TITLE     Identification of a cytokine-induced antiapoptotic molecule
            anamorsin essential for definitive hematopoiesis
  JOURNAL   J Exp Med 199 (4), 581-592 (2004)
   PUBMED   14970183
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC024196.2, BC067303.1 and AF248964.1.
            
            On Mar 9, 2006 this sequence version replaced NP_064709.1.
            
            Summary: CIAPIN1 is a cytokine-induced inhibitor of apoptosis with
            no relation to apoptosis regulatory molecules of the BCL2 (MIM
            151430) or CASP (see MIM 147678) families. Expression of CIAPIN1 is
            dependent on growth factor stimulation (Shibayama et al., 2004
            [PubMed 14970183]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1163755.1, AF248964.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394391.9/ ENSP00000377914.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q21"
     Protein         1..312
                     /product="anamorsin isoform 1"
                     /note="predicted protein of HQ0915; fe-S cluster assembly
                     protein DRE2 homolog"
                     /calculated_mol_wt=33451
     Region          3..95
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
     Region          6..172
                     /region_name="N-terminal SAM-like domain.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6FI81.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6FI81.2)"
     Region          173..224
                     /region_name="Linker.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6FI81.2)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6FI81.2)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6FI81.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6FI81.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6FI81.2)"
     Region          237..251
                     /region_name="Fe-S binding site A.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6FI81.2)"
     Region          240..304
                     /region_name="CIAPIN1"
                     /note="Cytokine-induced anti-apoptosis inhibitor 1, Fe-S
                     biogenesis; pfam05093"
                     /db_xref="CDD:398662"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8WTY4; propagated from
                     UniProtKB/Swiss-Prot (Q6FI81.2)"
     Region          274..288
                     /region_name="Fe-S binding site B.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6FI81.2)"
     Region          274..277
                     /region_name="Cx2C motif 1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6FI81.2)"
     Region          285..288
                     /region_name="Cx2C motif 2.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6FI81.2)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6FI81.2)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6FI81.2)"
     CDS             1..312
                     /gene="CIAPIN1"
                     /gene_synonym="Anamorsin; CIAE2; DRE2; PRO0915"
                     /coded_by="NM_020313.4:100..1038"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10781.2"
                     /db_xref="GeneID:57019"
                     /db_xref="HGNC:HGNC:28050"
                     /db_xref="MIM:608943"
ORIGIN      
        1 madfgisagq fvavvwdkss pvealkglvd klqaltgneg rvsvenikql lqsahkessf
       61 diilsglvpg sttlhsaeil aeiarilrpg gclflkepve tavdnnskvk tasklcsalt
      121 lsglvevkel qrepltpeev qsvrehlghe sdnllfvqit gkkpnfevgs srqlklsitk
      181 ksspsvkpav dpaaaklwtl sandmeddsm dlidsdelld pedlkkpdpa slraascgeg
      241 kkrkacknct cglaeeleke ksreqmssqp ksacgncylg dafrcascpy lgmpafkpge
      301 kvllsdsnlh da
//
LOCUS       NP_001170855             999 aa            linear   PRI 27-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 2 isoform F
            [Homo sapiens].
ACCESSION   NP_001170855
VERSION     NP_001170855.1
DBSOURCE    REFSEQ: accession NM_001177384.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Zhao,G., Zhao,Z., Xia,M., Xiao,L., Zhu,B., Wang,H., Li,X. and Di,J.
  TITLE     CPEB2 inhibit cell proliferation through upregulating p21 mRNA
            stability in glioma
  JOURNAL   Sci Rep 13 (1), 23103 (2023)
   PUBMED   38158431
  REMARK    GeneRIF: CPEB2 inhibit cell proliferation through upregulating p21
            mRNA stability in glioma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Zeng,P., Wang,F., Long,X., Cao,Y., Wen,F., Li,J. and Luo,Z.
  TITLE     CPEB2 enhances cell growth and angiogenesis by upregulating ARPC5
            mRNA stability in multiple myeloma
  JOURNAL   J Orthop Surg Res 18 (1), 384 (2023)
   PUBMED   37231521
  REMARK    GeneRIF: CPEB2 enhances cell growth and angiogenesis by
            upregulating ARPC5 mRNA stability in multiple myeloma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Zhang,M., Yang,C., Ruan,X., Liu,X., Wang,D., Liu,L., Shao,L.,
            Wang,P., Dong,W. and Xue,Y.
  TITLE     CPEB2 m6A methylation regulates blood-tumor barrier permeability by
            regulating splicing factor SRSF5 stability
  JOURNAL   Commun Biol 5 (1), 908 (2022)
   PUBMED   36064747
  REMARK    GeneRIF: CPEB2 m6A methylation regulates blood-tumor barrier
            permeability by regulating splicing factor SRSF5 stability.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 999)
  AUTHORS   Di,J., Zhao,G., Wang,H., Wu,Y., Zhao,Z., Zhu,B., Zhang,Y.,
            Zheng,J., Liu,Y. and Hu,Y.
  TITLE     A p53/CPEB2 negative feedback loop regulates renal cancer cell
            proliferation and migration
  JOURNAL   J Genet Genomics 48 (7), 606-617 (2021)
   PUBMED   34362680
  REMARK    GeneRIF: A p53/CPEB2 negative feedback loop regulates renal cancer
            cell proliferation and migration.
REFERENCE   5  (residues 1 to 999)
  AUTHORS   Pascual,R., Martin,J., Salvador,F., Reina,O., Chanes,V.,
            Millanes-Romero,A., Suner,C., Fernandez-Miranda,G., Bartomeu,A.,
            Huang,Y.S., Gomis,R.R. and Mendez,R.
  TITLE     The RNA binding protein CPEB2 regulates hormone sensing in mammary
            gland development and luminal breast cancer
  JOURNAL   Sci Adv 6 (20), eaax3868 (2020)
   PUBMED   32440535
  REMARK    GeneRIF: The RNA binding protein CPEB2 regulates hormone sensing in
            mammary gland development and luminal breast cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 999)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 999)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 999)
  AUTHORS   Peng,S.C., Lai,Y.T., Huang,H.Y., Huang,H.D. and Huang,Y.S.
  TITLE     A novel role of CPEB3 in regulating EGFR gene transcription via
            association with Stat5b in neurons
  JOURNAL   Nucleic Acids Res 38 (21), 7446-7457 (2010)
   PUBMED   20639532
REFERENCE   9  (residues 1 to 999)
  AUTHORS   Hagele,S., Kuhn,U., Boning,M. and Katschinski,D.M.
  TITLE     Cytoplasmic polyadenylation-element-binding protein (CPEB)1 and 2
            bind to the HIF-1alpha mRNA 3'-UTR and modulate HIF-1alpha protein
            expression
  JOURNAL   Biochem J 417 (1), 235-246 (2009)
   PUBMED   18752464
REFERENCE   10 (residues 1 to 999)
  AUTHORS   Kurihara,Y., Tokuriki,M., Myojin,R., Hori,T., Kuroiwa,A.,
            Matsuda,Y., Sakurai,T., Kimura,M., Hecht,N.B. and Uesugi,S.
  TITLE     CPEB2, a novel putative translational regulator in mouse haploid
            germ cells
  JOURNAL   Biol Reprod 69 (1), 261-268 (2003)
   PUBMED   12672660
  REMARK    GeneRIF: Functional studies of the mouse homolog
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105289.4, BC105925.1 and
            AC098829.3.
            
            Summary: The protein encoded by this gene is highly similar to
            cytoplasmic polyadenylation element binding protein (CPEB), an
            mRNA-binding protein that regulates cytoplasmic polyadenylation of
            mRNA as a trans factor in oogenesis and spermatogenesis. Studies of
            the similar gene in mice suggested a possible role of this protein
            in transcriptionally inactive haploid spermatids. Alternatively
            spliced transcript variants encoding distinct isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (F) lacks two alternate in-frame
            exons and uses an alternate in-frame splice site in the central
            coding region, compared to variant D. The resulting isoform (F)
            differs at two internal regions, compared to isoform D.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The genomic coordinates used for
            the transcript record were based on alignments. The 5' CDS is
            inferred based on comparison of the mouse and human orthologs.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105925.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.32"
     Protein         1..999
                     /product="cytoplasmic polyadenylation element-binding
                     protein 2 isoform F"
                     /note="CPE-binding protein 2"
                     /calculated_mol_wt=105838
     Region          742..833
                     /region_name="RRM1_CPEB2_like"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein CPEB-2, CPEB-3,
                     CPEB-4 and similar protiens; cd12724"
                     /db_xref="CDD:410123"
     Region          850..930
                     /region_name="RRM2_CPEB2_like"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein CPEB-2, CPEB-3,
                     CPEB-4 and similar protiens; cd12726"
                     /db_xref="CDD:410125"
     Region          925..986
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..999
                     /gene="CPEB2"
                     /gene_synonym="CPE-BP2; CPEB-2; hCPEB-2"
                     /coded_by="NM_001177384.2:194..3193"
                     /note="isoform F is encoded by transcript variant F"
                     /db_xref="CCDS:CCDS93480.1"
                     /db_xref="GeneID:132864"
                     /db_xref="HGNC:HGNC:21745"
                     /db_xref="MIM:610605"
ORIGIN      
        1 mrdfgfgvlq taplrssspg plfcgeaygp yavgsvnplp satpfgplsp pplpvtgfle
       61 aaspfsvplg ggagspaaaa sssspflahq qtmqdelllg ltqqparpls gaaateklpd
      121 hhpgggtiag vthllpsqdf kpslhhpsss sassccccrt sspqdfskrq qqqlssqkrk
      181 efspphlphp pdskpppppp plhcpgrfsp ppppagpllq paqlaqrqqq qppqqfsllh
      241 qqhlspqdfa prqrpadlpp lpqlppsppa aprrrhggag sprktpaage gsaaespnag
      301 lasstpvnpa pgsmespnhp llnspsnllp ggalgagafs slqspdlphp gggggggggg
      361 ppgggggggs asppplpgfg tpwsvqtasp ppqpqqpppt qpqqqppppq qppqpqpqpp
      421 gssattpggg sggslsampp pspdsengfy pglpssmnpa ffpsfspvsp hgctglsvpt
      481 sggggggfgg pfsatavppp pppamnipqq qppppaapqq pqsrrspvsp qlqqqhqaaa
      541 aaflqqrnsy nhhqpllkqs pwsnhqssgw gtgsmswgam hgrdhrrtgn mgipgtmnqi
      601 splkkpfsgn viappkftrs tpsltpkswi ednvfrtdnn sntllplqvr mdrsrmydsl
      661 nmhslensli dimraehdpl kgrlsyphpg tdnllmlngr sslfpiddgl lddghsdqvg
      721 vlnsptcysa hqngerierf srkvfvgglp pdidedeita sfrrfgplvv dwphkaesks
      781 yfppkgyafl lfqeessvqa lidacieedg klylcvsspt ikdkpvqirp wnlsdsdfvm
      841 dgsqpldprk tifvggvprp lravelamim drlyggvcya gidtdpelky pkgagrvafs
      901 nqqsyiaais arfvqlqhgd idkrvevkpy vlddqmcdec qgarcggkfa pffcanvtcl
      961 qyycefcwan ihsragrefh kplvkegadr prqihfrwn
//
LOCUS       NP_877433                313 aa            linear   PRI 27-APR-2025
DEFINITION  speedy protein A isoform 1 [Homo sapiens].
ACCESSION   NP_877433 XP_351428
VERSION     NP_877433.2
DBSOURCE    REFSEQ: accession NM_182756.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Chen,Y., Wang,Y., Chen,J., Zuo,W., Fan,Y., Huang,S., Liu,Y.,
            Chen,G., Li,Q., Li,J., Wu,J., Bian,Q., Huang,C. and Lei,M.
  TITLE     The SUN1-SPDYA interaction plays an essential role in meiosis
            prophase I
  JOURNAL   Nat Commun 12 (1), 3176 (2021)
   PUBMED   34039995
  REMARK    GeneRIF: The SUN1-SPDYA interaction plays an essential role in
            meiosis prophase I.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kaya,Y., Kucukvardar,S. and Yildiz,A.
  TITLE     Speedy/RINGO protein interacts with ERK/MAPK and PI3K/AKT pathways
            in SH-SY5Y neuroblastoma cells
  JOURNAL   Mol Cell Biochem 473 (1-2), 133-141 (2020)
   PUBMED   32602013
  REMARK    GeneRIF: Speedy/RINGO protein interacts with ERK/MAPK and PI3K/AKT
            pathways in SH-SY5Y neuroblastoma cells.
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Arziman,S., Tanriverdi,O., Kucukvardar,S., Citil,N. and Yildiz,A.
  TITLE     Salicylidene acylhydrazides attenuate survival of SH-SY5Y
            neuroblastoma cells through affecting mitotic regulator
            Speedy/RINGO and ERK/MAPK-PI3K/AKT signaling
  JOURNAL   Med Oncol 37 (8), 65 (2020)
   PUBMED   32691165
  REMARK    GeneRIF: Salicylidene acylhydrazides attenuate survival of SH-SY5Y
            neuroblastoma cells through affecting mitotic regulator
            Speedy/RINGO and ERK/MAPK-PI3K/AKT signaling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Fifield,B.A., Qemo,I., Kirou,E., Cardiff,R.D. and Porter,L.A.
  TITLE     The atypical cyclin-like protein Spy1 overrides p53-mediated tumour
            suppression and promotes susceptibility to breast tumourigenesis
  JOURNAL   Breast Cancer Res 21 (1), 140 (2019)
   PUBMED   31829284
  REMARK    GeneRIF: This mouse model demonstrates for the first time that
            degradation of the cyclin-like protein Spy1 is an essential
            component of p53-mediated tumour suppression. Targeting cyclin-like
            protein activity may therefore represent a mechanism of
            re-sensitizing cells to important cell cycle checkpoints in a
            therapeutic setting.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Gastwirt,R.F., Slavin,D.A., McAndrew,C.W. and Donoghue,D.J.
  TITLE     Spy1 expression prevents normal cellular responses to DNA damage:
            inhibition of apoptosis and checkpoint activation
  JOURNAL   J Biol Chem 281 (46), 35425-35435 (2006)
   PUBMED   16951407
  REMARK    GeneRIF: This study reports that Spy1 expression allows cells to
            evade checkpoints and apoptosis and suggest that Spy1 regulation of
            CDK2 is important for the response to DNA damage.
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Cheng,A., Xiong,W., Ferrell,J.E. Jr. and Solomon,M.J.
  TITLE     Identification and comparative analysis of multiple mammalian
            Speedy/Ringo proteins
  JOURNAL   Cell Cycle 4 (1), 155-165 (2005)
   PUBMED   15611625
REFERENCE   8  (residues 1 to 313)
  AUTHORS   Porter,L.A., Kong-Beltran,M. and Donoghue,D.J.
  TITLE     Spy1 interacts with p27Kip1 to allow G1/S progression
  JOURNAL   Mol Biol Cell 14 (9), 3664-3674 (2003)
   PUBMED   12972555
REFERENCE   9  (residues 1 to 313)
  AUTHORS   Barnes,E.A., Porter,L.A., Lenormand,J.L., Dellinger,R.W. and
            Donoghue,D.J.
  TITLE     Human Spy1 promotes survival of mammalian cells following DNA
            damage
  JOURNAL   Cancer Res 63 (13), 3701-3707 (2003)
   PUBMED   12839962
  REMARK    GeneRIF: This protein mediates protection of mammalian cells
            against DNA damage.
REFERENCE   10 (residues 1 to 313)
  AUTHORS   Porter,L.A., Dellinger,R.W., Tynan,J.A., Barnes,E.A., Kong,M.,
            Lenormand,J.L. and Donoghue,D.J.
  TITLE     Human Speedy: a novel cell cycle regulator that enhances
            proliferation through activation of Cdk2
  JOURNAL   J Cell Biol 157 (3), 357-366 (2002)
   PUBMED   11980914
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC093005.1, BC047224.1 and AY820304.1.
            
            On Mar 4, 2005 this sequence version replaced NP_877433.1.
            
            Transcript Variant: This variant (1) lacks a segment in the 5' UTR,
            compared to variant 3. Variants 1 and 3 both encode the longer
            protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.122914.1, BC047224.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334056.10/ ENSP00000335628.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.2"
     Protein         1..313
                     /product="speedy protein A isoform 1"
                     /note="speedy protein A; RINGO A; speedy-1; hSpy/Ringo A;
                     rapid inducer of G2/M progression in oocytes A; speedy
                     homolog A; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=36332
     Region          68..200
                     /region_name="Speedy/Ringo box, Required for CDK-binding.
                     /evidence=ECO:0000269|PubMed:28666995"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5MJ70.2)"
     Region          69..199
                     /region_name="Spy1"
                     /note="Cell cycle regulatory protein; pfam11357"
                     /db_xref="CDD:463263"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5IBH7; propagated from
                     UniProtKB/Swiss-Prot (Q5MJ70.2)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5IBH7; propagated from
                     UniProtKB/Swiss-Prot (Q5MJ70.2)"
     Region          278..313
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5MJ70.2)"
     CDS             1..313
                     /gene="SPDYA"
                     /gene_synonym="RINGO3; RINGOA; SPDY1; SPY1"
                     /coded_by="NM_182756.4:207..1148"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1767.2"
                     /db_xref="GeneID:245711"
                     /db_xref="HGNC:HGNC:30613"
                     /db_xref="MIM:614029"
ORIGIN      
        1 mrhnqmccet pptvtvyvks gsnrshqpkk pitlkrpick dnwqafeknt hnnnkskrpk
       61 gpclviqrqd mtaffklfdd dliqdflwmd ccckiadkyl lamtfvyfkr akftisehtr
      121 inffialyla ntveedeeet kyeifpwalg knwrklfpnf lklrdqlwdr idyraivsrr
      181 cceevmaiap thyiwqrers vhhsgavrny nrdevqlprg psatpvdcsl cgkkrryvrl
      241 glssssslss htagvtekhs qdsynslsmd iigdpsqayt gsevvndhqs nkgkktnflk
      301 kdksmewftg see
//
LOCUS       NP_004741                422 aa            linear   PRI 27-APR-2025
DEFINITION  cytokine receptor-like factor 1 precursor [Homo sapiens].
ACCESSION   NP_004741
VERSION     NP_004741.1
DBSOURCE    REFSEQ: accession NM_004750.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Lu,Z., Wang,D., Sun,Y. and Dai,Y.
  TITLE     ENO1 regulates IL-1beta-induced chondrocyte inflammation, apoptosis
            and matrix degradation possibly through the potential binding to
            CRLF1
  JOURNAL   Tissue Cell 90, 102504 (2024)
   PUBMED   39116531
  REMARK    GeneRIF: ENO1 regulates IL-1beta-induced chondrocyte inflammation,
            apoptosis and matrix degradation possibly through the potential
            binding to CRLF1.
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Xiang,C., Chen,L., Zhu,S., Chen,Y., Huang,H., Yang,C., Chi,Y.,
            Wang,Y., Lei,Y. and Cai,X.
  TITLE     CRLF1 bridges AKT and mTORC2 through SIN1 to inhibit pyroptosis and
            enhance chemo-resistance in ovarian cancer
  JOURNAL   Cell Death Dis 15 (9), 662 (2024)
   PUBMED   39256356
  REMARK    GeneRIF: CRLF1 bridges AKT and mTORC2 through SIN1 to inhibit
            pyroptosis and enhance chemo-resistance in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Yu,B., Cao,Y., Li,S., Bai,R., Zhou,G., Fu,Q., Liang,L., Gu,W.,
            Zhang,L. and Chen,M.
  TITLE     Identification and validation of CRLF1 and NRG1 as immune-related
            signatures in hypertrophic scar
  JOURNAL   Genomics 116 (2), 110797 (2024)
   PUBMED   38262564
  REMARK    GeneRIF: Identification and validation of CRLF1 and NRG1 as
            immune-related signatures in hypertrophic scar.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Guo,J., Ye,W., Wu,X., Huang,H., Li,B., Ren,Z. and Yang,Z.
  TITLE     Long non-coding RNA MIR22HG suppresses the chondrogenic
            differentiation of human adipose-derived stem cells by interacting
            with CTCF to upregulate CRLF1
  JOURNAL   Funct Integr Genomics 23 (4), 329 (2023)
   PUBMED   37910254
  REMARK    GeneRIF: Long non-coding RNA MIR22HG suppresses the chondrogenic
            differentiation of human adipose-derived stem cells by interacting
            with CTCF to upregulate CRLF1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 422)
  AUTHORS   A,R., Chandran,S., Ghatak,A.R., Thomas,N. and Danda,S.
  TITLE     Novel Mutations in CRLF1: Case Reports with Crisponi Syndrome
  JOURNAL   Indian J Pediatr 89 (11), 1148-1150 (2022)
   PUBMED   35984556
  REMARK    GeneRIF: Novel Mutations in CRLF1: Case Reports with Crisponi
            Syndrome.
            Review article
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Knappskog,P.M., Majewski,J., Livneh,A., Nilsen,P.T., Bringsli,J.S.,
            Ott,J. and Boman,H.
  TITLE     Cold-induced sweating syndrome is caused by mutations in the CRLF1
            gene
  JOURNAL   Am J Hum Genet 72 (2), 375-383 (2003)
   PUBMED   12509788
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Elson,G.C., Lelievre,E., Guillet,C., Chevalier,S., Plun-Favreau,H.,
            Froger,J., Suard,I., de Coignac,A.B., Delneste,Y., Bonnefoy,J.Y.,
            Gauchat,J.F. and Gascan,H.
  TITLE     CLF associates with CLC to form a functional heteromeric ligand for
            the CNTF receptor complex
  JOURNAL   Nat Neurosci 3 (9), 867-872 (2000)
   PUBMED   10966616
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Elson,G.C., Graber,P., Losberger,C., Herren,S., Gretener,D.,
            Menoud,L.N., Wells,T.N., Kosco-Vilbois,M.H. and Gauchat,J.F.
  TITLE     Cytokine-like factor-1, a novel soluble protein, shares homology
            with members of the cytokine type I receptor family
  JOURNAL   J Immunol 161 (3), 1371-1379 (1998)
   PUBMED   9686600
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Hahn,A.F. and Knappskog,P.M.
  TITLE     Cold-Induced Sweating Syndrome Including Crisponi Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21370513
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF073515.1 and AY358291.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the cytokine type I receptor
            family. The protein forms a secreted complex with
            cardiotrophin-like cytokine factor 1 and acts on cells expressing
            ciliary neurotrophic factor receptors. The complex can promote
            survival of neuronal cells. Mutations in this gene result in
            Crisponi syndrome and cold-induced sweating syndrome. [provided by
            RefSeq, Oct 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF073515.1, AY358291.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392386.8/ ENSP00000376188.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..422
                     /product="cytokine receptor-like factor 1 precursor"
                     /note="cytokine type 1 receptor CRLP-1; class I cytokine
                     receptor; cytokine-like factor 1"
                     /calculated_mol_wt=42588
     sig_peptide     1..37
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3732
     mat_peptide     38..422
                     /product="cytokine receptor-like factor 1"
                     /calculated_mol_wt=42588
     Region          41..>104
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75462.1)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75462.1)"
     Region          133..228
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            order(135,203,218)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75462.1)"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75462.1)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JM58; propagated from
                     UniProtKB/Swiss-Prot (O75462.1)"
     Region          236..338
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75462.1)"
     Region          327..331
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O75462.1)"
     Site            order(327..328,330..331)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          332..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75462.1)"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75462.1)"
     Region          399..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75462.1)"
     CDS             1..422
                     /gene="CRLF1"
                     /gene_synonym="CISS; CISS1; CLF; CLF-1; NR6; zcytor5"
                     /coded_by="NM_004750.5:144..1412"
                     /db_xref="CCDS:CCDS32962.1"
                     /db_xref="GeneID:9244"
                     /db_xref="HGNC:HGNC:2364"
                     /db_xref="MIM:604237"
ORIGIN      
        1 mpagrrgpaa qsarrpppll plllllcvlg apragsgaht avispqdptl ligssllatc
       61 svhgdppgat aeglywtlng rrlppelsrv lnastlalal anlngsrqrs gdnlvchard
      121 gsilagscly vglppekpvn iscwsknmkd ltcrwtpgah getflhtnys lkyklrwygq
      181 dntceeyhtv gphschipkd lalftpyeiw veatnrlgsa rsdvltldil dvvttdpppd
      241 vhvsrvggle dqlsvrwvsp palkdflfqa kyqiryrved svdwkvvddv snqtscrlag
      301 lkpgtvyfvq vrcnpfgiyg skkagiwsew shptaastpr serpgpggga ceprggepss
      361 gpvrrelkqf lgwlkkhayc snlsfrlydq wrawmqkshk trnqdegilp sgrrgtargp
      421 ar
//
LOCUS       NP_001355732             822 aa            linear   ROD 27-APR-2025
DEFINITION  band 4.1-like protein 1 isoform i [Mus musculus].
ACCESSION   NP_001355732
VERSION     NP_001355732.1
DBSOURCE    REFSEQ: accession NM_001368803.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Wang,D., Zhang,L., Hu,A., Wang,Y., Liu,Y., Yang,J., Du,N., An,X.,
            Wu,C. and Liu,C.
  TITLE     Loss of 4.1N in epithelial ovarian cancer results in EMT and
            matrix-detached cell death resistance
  JOURNAL   Protein Cell 12 (2), 107-127 (2021)
   PUBMED   32448967
  REMARK    GeneRIF: Loss of 4.1N in epithelial ovarian cancer results in EMT
            and matrix-detached cell death resistance.
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Wang,H., Parra,M., Conboy,J.G., Hillyer,C.D., Mohandas,N. and An,X.
  TITLE     Selective effects of protein 4.1N deficiency on neuroendocrine and
            reproductive systems
  JOURNAL   Sci Rep 10 (1), 16947 (2020)
   PUBMED   33046791
  REMARK    GeneRIF: Selective effects of protein 4.1N deficiency on
            neuroendocrine and reproductive systems.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Zhang,X., Chen,M.H., Wu,X., Kodani,A., Fan,J., Doan,R., Ozawa,M.,
            Ma,J., Yoshida,N., Reiter,J.F., Black,D.L., Kharchenko,P.V.,
            Sharp,P.A. and Walsh,C.A.
  TITLE     Cell-Type-Specific Alternative Splicing Governs Cell Fate in the
            Developing Cerebral Cortex
  JOURNAL   Cell 166 (5), 1147-1162 (2016)
   PUBMED   27565344
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Fukatsu,K., Bannai,H., Zhang,S., Nakamura,H., Inoue,T. and
            Mikoshiba,K.
  TITLE     Lateral diffusion of inositol 1,4,5-trisphosphate receptor type 1
            is regulated by actin filaments and 4.1N in neuronal dendrites
  JOURNAL   J Biol Chem 279 (47), 48976-48982 (2004)
   PUBMED   15364918
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Zhang,S., Mizutani,A., Hisatsune,C., Higo,T., Bannai,H.,
            Nakayama,T., Hattori,M. and Mikoshiba,K.
  TITLE     Protein 4.1N is required for translocation of inositol
            1,4,5-trisphosphate receptor type 1 to the basolateral membrane
            domain in polarized Madin-Darby canine kidney cells
  JOURNAL   J Biol Chem 278 (6), 4048-4056 (2003)
   PUBMED   12444087
REFERENCE   8  (residues 1 to 822)
  AUTHORS   Walensky,L.D., Blackshaw,S., Liao,D., Watkins,C.C., Weier,H.U.,
            Parra,M., Huganir,R.L., Conboy,J.G., Mohandas,N. and Snyder,S.H.
  TITLE     A novel neuron-enriched homolog of the erythrocyte membrane
            cytoskeletal protein 4.1
  JOURNAL   J Neurosci 19 (15), 6457-6467 (1999)
   PUBMED   10414974
REFERENCE   9  (residues 1 to 822)
  AUTHORS   Peters,L.L., Weier,H.U., Walensky,L.D., Snyder,S.H., Parra,M.,
            Mohandas,N. and Conboy,J.G.
  TITLE     Four paralogous protein 4.1 genes map to distinct chromosomes in
            mouse and human
  JOURNAL   Genomics 54 (2), 348-350 (1998)
   PUBMED   9828140
REFERENCE   10 (residues 1 to 822)
  AUTHORS   Takeuchi,K., Kawashima,A., Nagafuchi,A. and Tsukita,S.
  TITLE     Structural diversity of band 4.1 superfamily members
  JOURNAL   J Cell Sci 107 (Pt 7), 1921-1928 (1994)
   PUBMED   7983158
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL928935.14 and AL929153.11.
            
            Transcript Variant: This variant (11), as well as variant 12,
            encodes isoform i.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.1577158.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134, SAMN01164136
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 77.39 cM"
     Protein         1..822
                     /product="band 4.1-like protein 1 isoform i"
                     /note="band 4.1-like protein 1; neuronal protein 4.1;
                     erythrocyte protein band 4.1 like 1"
                     /calculated_mol_wt=92412
     Region          1..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          99..288
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          283..376
                     /region_name="FERM_C_4_1_family"
                     /note="FERM domain C-lobe of Protein 4.1 family; cd13184"
                     /db_xref="CDD:270005"
     Site            order(292,309,311,317)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270005"
     Site            order(321,326..329,364,368,371..372)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18034455; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            364..375
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          381..482
                     /region_name="Hydrophilic"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          385..428
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     Region          <396..>599
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          428..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTP0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          483..541
                     /region_name="Spectrin--actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          493..>524
                     /region_name="SAB"
                     /note="SAB domain; pfam04382"
                     /db_xref="CDD:461285"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          514..594
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            550
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16452087,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          657..696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            665
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            721
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          <756..808
                     /region_name="4_1_CTD"
                     /note="4.1 protein C-terminal domain (CTD); pfam05902"
                     /db_xref="CDD:461774"
     CDS             1..822
                     /gene="Epb41l1"
                     /gene_synonym="4.1N; Epb4.1l1; mKIAA0338; NBL1"
                     /coded_by="NM_001368803.1:327..2795"
                     /note="isoform i is encoded by transcript variant 11"
                     /db_xref="GeneID:13821"
                     /db_xref="MGI:MGI:103010"
ORIGIN      
        1 mttetgpdse vkkaqeetpq qpeaaaavtt pvtpaghshp etnsnekhlt qqdtrpaeqs
       61 ldmddkdyse adglserttp skaqkspqki akkfksaicr vtlldaseye cevekhgrgq
      121 vlfdlvcehl nllekdyfgl tycdadsqkn wldpskeikk qirsspwnfa ftvkfyppdp
      181 aqlteditry ylclqlradi itgrlpcsfv thallgsyav qaelgdydae ehvgnyvsel
      241 rfapnqtrel eerimelhkt yrgmtpgeae ihflenakkl smygvdlhha kdsegidiml
      301 gvcanglliy rdrlrinrfa wpkilkisyk rsnfyikirp geyeqfesti gfklpnhrsa
      361 krlwkvcieh htffrlvspe pppkgflvmg skfrysgrtq aqtrqasali drpapffers
      421 sskrytmsrs ldgaefsrpa svsenhdagp dgdkreddae sggrrseaee gevrtptkik
      481 elkpeqettp rhkqefldkp edvllkhqas inelkrtlke pnsklihrdr dwdrerrlps
      541 spaspspkgt pekaseragl regseekvkp prprapesdt gdedqdqerd avflkdnhla
      601 ierkcssitv sstssleaev dftvigdyhg gafedfsrsl peldrdksds eteglvfard
      661 lkgpssqede sggledspdr gacstpempq fesvkaetmt vsslairkki epeamlqsrv
      721 saadstqvdg gtpmvkdfmt tppcitteti sttmtvkggf setriekrii itgdedvdqd
      781 qalalaikea klqhpdmlvt kavvyretdp speerdkkpq es
//
LOCUS       NP_057049                144 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 [Homo
            sapiens].
ACCESSION   NP_057049
VERSION     NP_057049.5
DBSOURCE    REFSEQ: accession NM_015965.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Wang,B., Yang,Y., Ye,J., Han,X., Yang,L., Huang,Y. and Chao,L.
  TITLE     GRIM-19 deficiency promotes macrophage polarization to the M1
            phenotype partly through glycolysis in unexplained recurrent
            spontaneous abortiondagger
  JOURNAL   Biol Reprod 110 (4), 739-749 (2024)
   PUBMED   38206868
  REMARK    GeneRIF: GRIM-19 deficiency promotes macrophage polarization to the
            M1 phenotype partly through glycolysis in unexplained recurrent
            spontaneous abortiondagger.
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Yang,L., Yang,Y., Han,X., Huang,C., Wang,Y., Jiang,D. and Chao,L.
  TITLE     GRIM19 deficiency aggravates metabolic disorder and ovarian
            dysfunction in PCOS
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (4), 167063 (2024)
   PUBMED   38360073
  REMARK    GeneRIF: GRIM19 deficiency aggravates metabolic disorder and
            ovarian dysfunction in PCOS.
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Zeng,X., Yang,M., Ye,T., Feng,J., Xu,X., Yang,H., Wang,X., Bao,L.,
            Li,R., Xue,B., Zang,J. and Huang,Y.
  TITLE     Mitochondrial GRIM-19 loss in parietal cells promotes spasmolytic
            polypeptide-expressing metaplasia through NLR family pyrin
            domain-containing 3 (NLRP3)-mediated IL-33 activation via a
            reactive oxygen species (ROS) -NRF2- Heme
            oxygenase-1(HO-1)-NF-small ka, CyrillicB axis
  JOURNAL   Free Radic Biol Med 202, 46-61 (2023)
   PUBMED   36990300
  REMARK    GeneRIF: Mitochondrial GRIM-19 loss in parietal cells promotes
            spasmolytic polypeptide-expressing metaplasia through NLR family
            pyrin domain-containing 3 (NLRP3)-mediated IL-33 activation via a
            reactive oxygen species (ROS) -NRF2- Heme
            oxygenase-1(HO-1)-NF-small ka, CyrillicB axis.
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Lu,H. and Cao,X.
  TITLE     GRIM-19 is essential for maintenance of mitochondrial membrane
            potential
  JOURNAL   Mol Biol Cell 19 (5), 1893-1902 (2008)
   PUBMED   18287540
  REMARK    GeneRIF: GRIM-19 is required for electron transfer activity of
            complex I, and disruption of mitochondrial transmembrane potential
            by GRIM-19 mutants enhances the cells' sensitivity to apoptotic
            stimuli.
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Yeo,W.M., Isegawa,Y. and Chow,V.T.
  TITLE     The U95 protein of human herpesvirus 6B interacts with human
            GRIM-19: silencing of U95 expression reduces viral load and
            abrogates loss of mitochondrial membrane potential
  JOURNAL   J Virol 82 (2), 1011-1020 (2008)
   PUBMED   17928352
  REMARK    GeneRIF: results indicate that the high affinity between U95 early
            viral protein and GRIM-19 may be closely linked to the detrimental
            effect of HHV-6B infection on mitochondria.
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Kalakonda,S., Nallar,S.C., Lindner,D.J., Hu,J., Reddy,S.P. and
            Kalvakolanu,D.V.
  TITLE     Tumor-suppressive activity of the cell death activator GRIM-19 on a
            constitutively active signal transducer and activator of
            transcription 3
  JOURNAL   Cancer Res 67 (13), 6212-6220 (2007)
   PUBMED   17616678
  REMARK    GeneRIF: GRIM-19 suppresses constitutive STAT3-induced cellular
            transformation in vitro and in vivo by down-regulating the
            expression of a number of cellular genes involved in cell
            proliferation and apoptosis
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Angell,J.E., Lindner,D.J., Shapiro,P.S., Hofmann,E.R. and
            Kalvakolanu,D.V.
  TITLE     Identification of GRIM-19, a novel cell death-regulatory gene
            induced by the interferon-beta and retinoic acid combination, using
            a genetic approach
  JOURNAL   J Biol Chem 275 (43), 33416-33426 (2000)
   PUBMED   10924506
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Chidambaram,N.V., Angell,J.E., Ling,W., Hofmann,E.R. and
            Kalvakolanu,D.V.
  TITLE     Chromosomal localization of human GRIM-19, a novel IFN-beta and
            retinoic acid-activated regulator of cell death
  JOURNAL   J Interferon Cytokine Res 20 (7), 661-665 (2000)
   PUBMED   10926209
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC009189.2 and BG705222.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 8, 2009 this sequence version replaced NP_057049.4.
            
            Summary: This gene encodes a subunit of the mitochondrial membrane
            respiratory chain NADH dehydrogenase (Complex I), which functions
            in the transfer of electrons from NADH to the respiratory chain.
            The protein is required for complex I assembly and electron
            transfer activity. The protein binds the signal transducers and
            activators of transcription 3 (STAT3) transcription factor, and can
            function as a tumor suppressor. The human protein purified from
            mitochondria migrates at approximately 16 kDa. Transcripts
            originating from an upstream promoter and capable of expressing a
            protein with a longer N-terminus have been found, but their
            biological validity has not been determined. [provided by RefSeq,
            Oct 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF261134.1, SRR5189667.105639.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 12611891, 17928352;
                                                  reported by MitoCarta
            MANE Ensembl match                 :: ENST00000507754.9/
                                                  ENSP00000423673.1
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..144
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 13"
                     /EC_number="7.1.1.2"
                     /note="complex I B16.6 subunit; cell death-regulatory
                     protein GRIM19; CI-B16.6; complex I-B16.6; cell death
                     regulatory protein GRIM-19; NADH-ubiquinone oxidoreductase
                     B16.6 subunit; gene associated with retinoic and
                     IFN-induced mortality 19 protein; gene associated with
                     retinoic and interferon-induced mortality 19 protein; NADH
                     dehydrogenase (ubiquinone) 1 alpha subcomplex, 13"
                     /calculated_mol_wt=16567
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q95KV7; propagated from
                     UniProtKB/Swiss-Prot (Q9P0J0.3)"
     Region          5..128
                     /region_name="GRIM-19"
                     /note="GRIM-19 protein; pfam06212"
                     /db_xref="CDD:461852"
     Site            30..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0J0.3)"
     Region          102..144
                     /region_name="Important for inducing cell death"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0J0.3)"
     CDS             1..144
                     /gene="NDUFA13"
                     /gene_synonym="B16.6; CDA016; CGI-39; GRIM-19; GRIM19;
                     MC1DN28"
                     /coded_by="NM_015965.7:15..449"
                     /db_xref="CCDS:CCDS12404.2"
                     /db_xref="GeneID:51079"
                     /db_xref="HGNC:HGNC:17194"
                     /db_xref="MIM:609435"
ORIGIN      
        1 maaskvkqdm pppggygpid ykrnlprrgl sgysmlaigi gtliyghwsi mkwnrerrrl
       61 qiedfearia llpllqaetd rrtlqmlren leeeaiimkd vpdwkvgesv fhttrwvppl
      121 igelyglrtt eealhashgf mwyt
//
LOCUS       NP_067076                518 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM39 isoform 1 [Homo sapiens].
ACCESSION   NP_067076
VERSION     NP_067076.2
DBSOURCE    REFSEQ: accession NM_021253.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ogura,T., Azuma,K., Takeiwa,T., Sato,J., Kinowaki,K., Ikeda,K.,
            Kawabata,H. and Inoue,S.
  TITLE     TRIM39 is a poor prognostic factor for patients with estrogen
            receptor-positive breast cancer and promotes cell cycle progression
  JOURNAL   Pathol Int 72 (2), 96-106 (2022)
   PUBMED   35174936
  REMARK    GeneRIF: TRIM39 is a poor prognostic factor for patients with
            estrogen receptor-positive breast cancer and promotes cell cycle
            progression.
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Hu,J., Ding,X., Tian,S., Chu,Y., Liu,Z., Li,Y., Li,X., Wang,G.,
            Wang,L. and Wang,Z.
  TITLE     TRIM39 deficiency inhibits tumor progression and autophagic flux in
            colorectal cancer via suppressing the activity of Rab7
  JOURNAL   Cell Death Dis 12 (4), 391 (2021)
   PUBMED   33846303
  REMARK    GeneRIF: TRIM39 deficiency inhibits tumor progression and
            autophagic flux in colorectal cancer via suppressing the activity
            of Rab7.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Ning,L., Ko,J.M., Yu,V.Z., Ng,H.Y., Chan,C.K., Tao,L., Lam,S.Y.,
            Leong,M.M., Ngan,R.K., Kwong,D.L., Lee,A.W., Ng,W.T., Cheng,A.,
            Tung,S., Lee,V.H., Lam,K.O., Kwan,C.K., Li,W.S., Yau,S., Bei,J.X.
            and Lung,M.L.
  TITLE     Nasopharyngeal carcinoma MHC region deep sequencing identifies HLA
            and novel non-HLA TRIM31 and TRIM39 loci
  JOURNAL   Commun Biol 3 (1), 759 (2020)
   PUBMED   33311639
  REMARK    GeneRIF: Nasopharyngeal carcinoma MHC region deep sequencing
            identifies HLA and novel non-HLA TRIM31 and TRIM39 loci.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 518)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 518)
  AUTHORS   Roberts,J.D. Jr., Chiche,J.D., Kolpa,E.M., Bloch,D.B. and
            Bloch,K.D.
  TITLE     cGMP-dependent protein kinase I interacts with TRIM39R, a novel
            Rpp21 domain-containing TRIM protein
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 293 (4), L903-L912 (2007)
   PUBMED   17601797
REFERENCE   7  (residues 1 to 518)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   8  (residues 1 to 518)
  AUTHORS   Tao,W.A., Wollscheid,B., O'Brien,R., Eng,J.K., Li,X.J.,
            Bodenmiller,B., Watts,J.D., Hood,L. and Aebersold,R.
  TITLE     Quantitative phosphoproteome analysis using a dendrimer conjugation
            chemistry and tandem mass spectrometry
  JOURNAL   Nat Methods 2 (8), 591-598 (2005)
   PUBMED   16094384
REFERENCE   9  (residues 1 to 518)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   10 (residues 1 to 518)
  AUTHORS   Orimo,A., Yamagishi,T., Tominaga,N., Yamauchi,Y., Hishinuma,T.,
            Okada,K., Suzuki,M., Sato,M., Nogi,Y., Suzuki,H., Inoue,S.,
            Yoshimura,K., Shimizu,Y. and Muramatsu,M.
  TITLE     Molecular cloning of testis-abundant finger Protein/Ring finger
            protein 23 (RNF23), a novel RING-B box-coiled coil-B30.2 protein on
            the class I region of the human MHC
  JOURNAL   Biochem Biophys Res Commun 276 (1), 45-51 (2000)
   PUBMED   11006080
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662795.5.
            
            On Nov 27, 2002 this sequence version replaced NP_067076.1.
            
            Summary: The protein encoded by this gene is a member of the
            tripartite motif (TRIM) family. The TRIM motif includes three
            zinc-binding domains, a RING, a B-box type 1 and a B-box type 2,
            and a coiled-coil region. The function of this protein has not been
            identified. This gene lies within the major histocompatibility
            complex class I region on chromosome 6. Alternate splicing results
            in two transcript variants encoding different isoforms. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2584317.1, AK292512.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..518
                     /product="E3 ubiquitin-protein ligase TRIM39 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 23; testis-abundant finger
                     protein; tripartite motif-containing protein 39; E3
                     ubiquitin-protein ligase TRIM39; RING-type E3 ubiquitin
                     transferase TRIM39"
                     /calculated_mol_wt=59560
     Region          22..82
                     /region_name="RING-HC_TRIM7-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins, TRIM7, TRIM11 and TRIM27, and
                     similar proteins; cd16594"
                     /db_xref="CDD:438256"
     Region          103..146
                     /region_name="Bbox2_TRIM39-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins TRIM39, TRIM58 and similar
                     proteins; cd19780"
                     /db_xref="CDD:380838"
     Region          149..>268
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          268..337
                     /region_name="Interaction with CDKN1A.
                     /evidence=ECO:0000269|PubMed:23213251"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCM9.2)"
     Region          335..513
                     /region_name="SPRY_PRY_TRIM39"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     39 (TRIM39) and TRIM39-like; cd13745"
                     /db_xref="CDD:293979"
     Region          389..518
                     /region_name="Interaction with CDKN1A.
                     /evidence=ECO:0000269|PubMed:23213251"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCM9.2)"
     CDS             1..518
                     /gene="TRIM39"
                     /gene_synonym="RNF23; TFP; TRIM39B"
                     /coded_by="NM_021253.4:688..2244"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34377.1"
                     /db_xref="GeneID:56658"
                     /db_xref="HGNC:HGNC:10065"
                     /db_xref="MIM:605700"
ORIGIN      
        1 maetslleag asaastaaal enlqveascs vcleylkepv iiecghnfck acitrwwedl
       61 erdfpcpvcr ktsryrslrp nrqlgsmvei akqlqavkrk irdeslcpqh healslfcye
      121 dqeavclica ishthrahtv vplddatqey keklqkclep leqklqeitr cksseekkpg
      181 elkrlvesrr qqilrefeel hrrldeeqqv llsrleeeeq dilqrlrena ahlgdkrrdl
      241 ahlaaevegk clqsgfemlk dvkstlekni prkfggslst icprdhkall glvkeinrce
      301 kvktmevtsv sieleknfsn fprqyfalrk ilkqliadvt ldpetahpnl vlsedrksvk
      361 fvetrlrdlp dtprrftfyp cvlategfts grhywevevg dkthwavgvc rdsvsrkgel
      421 tplpetgywr vrlwngdkya atttpftplh ikvkpkrvgi fldyeagtls fynvtdrshi
      481 ytftdtftek lwplfypgir agrknaaplt irpptdwe
//
LOCUS       NP_004764                155 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger HIT domain-containing protein 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_004764
VERSION     NP_004764.1
DBSOURCE    REFSEQ: accession NM_004773.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Brakta,S., Du,Q., Chorich,L.P., Hawkins,Z.A., Sullivan,M.E.,
            Ko,E.K., Kim,H.G., Knight,J., Taylor,H.S., Friez,M., Phillips,J.A.
            3rd and Layman,L.C.
  TITLE     Heterozygous ZNHIT3 variants within the 17q12 recurrent deletion
            region are associated with Mayer-Rokitansky-Kuster Hauser (MRKH)
            syndrome
  JOURNAL   Mol Cell Endocrinol 589, 112237 (2024)
   PUBMED   38599276
  REMARK    GeneRIF: Heterozygous ZNHIT3 variants within the 17q12 recurrent
            deletion region are associated with Mayer-Rokitansky-Kuster Hauser
            (MRKH) syndrome.
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 155)
  AUTHORS   Anttonen,A.K., Laari,A., Kousi,M., Yang,Y.J., Jaaskelainen,T.,
            Somer,M., Siintola,E., Jakkula,E., Muona,M., Tegelberg,S.,
            Lonnqvist,T., Pihko,H., Valanne,L., Paetau,A., Lun,M.P.,
            Hastbacka,J., Kopra,O., Joensuu,T., Katsanis,N., Lehtinen,M.K.,
            Palvimo,J.J. and Lehesjoki,A.E.
  TITLE     ZNHIT3 is defective in PEHO syndrome, a severe encephalopathy with
            cerebellar granule neuron loss
  JOURNAL   Brain 140 (5), 1267-1279 (2017)
   PUBMED   28335020
  REMARK    GeneRIF: results suggest that loss-of-function missense mutation of
            znhit3 underlies PEHO syndrome.
REFERENCE   6  (residues 1 to 155)
  AUTHORS   Rothe,B., Saliou,J.M., Quinternet,M., Back,R., Tiotiu,D.,
            Jacquemin,C., Loegler,C., Schlotter,F., Pena,V., Eckert,K.,
            Morera,S., Dorsselaer,A.V., Branlant,C., Massenet,S.,
            Sanglier-Cianferani,S., Manival,X. and Charpentier,B.
  TITLE     Protein Hit1, a novel box C/D snoRNP assembly factor, controls
            cellular concentration of the scaffolding protein Rsa1 by direct
            interaction
  JOURNAL   Nucleic Acids Res 42 (16), 10731-10747 (2014)
   PUBMED   25170085
REFERENCE   7  (residues 1 to 155)
  AUTHORS   Koppen,A., Houtman,R., Pijnenburg,D., Jeninga,E.H., Ruijtenbeek,R.
            and Kalkhoven,E.
  TITLE     Nuclear receptor-coregulator interaction profiling identifies TRIP3
            as a novel peroxisome proliferator-activated receptor gamma
            cofactor
  JOURNAL   Mol Cell Proteomics 8 (10), 2212-2226 (2009)
   PUBMED   19596656
  REMARK    GeneRIF: Results identify TRIP3 as a novel regulator of
            PPARgamma-mediated adipocyte differentiation.
REFERENCE   8  (residues 1 to 155)
  AUTHORS   Zhang,J.B., Li,X.H., Ning,F. and Guo,X.S.
  TITLE     [Relationship between expression of GYPC and TRIP3 genes and
            prognosis of acute lymphoblastic leukemia in children]
  JOURNAL   Zhongguo Dang Dai Er Ke Za Zhi 11 (1), 29-32 (2009)
   PUBMED   19149918
  REMARK    GeneRIF: A high GYPC gene expression is associated with an
            unfavorable outcome, in contrast, a high TRIP3 gene expression is
            associated with a favorable outcome in childhood ALL.
REFERENCE   9  (residues 1 to 155)
  AUTHORS   Iwahashi,H., Yamagata,K., Yoshiuchi,I., Terasaki,J., Yang,Q.,
            Fukui,K., Ihara,A., Zhu,Q., Asakura,T., Cao,Y., Imagawa,A.,
            Namba,M., Hanafusa,T., Miyagawa,J. and Matsuzawa,Y.
  TITLE     Thyroid hormone receptor interacting protein 3 (trip3) is a novel
            coactivator of hepatocyte nuclear factor-4alpha
  JOURNAL   Diabetes 51 (4), 910-914 (2002)
   PUBMED   11916906
REFERENCE   10 (residues 1 to 155)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF400652.1 and BQ009986.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.5078.1,
                                           SRR5189667.11595.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000617429.5/ ENSP00000484687.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..155
                     /product="zinc finger HIT domain-containing protein 3
                     isoform 1"
                     /note="thyroid receptor interacting protein 3; thyroid
                     hormone receptor interactor 3; zinc finger, HIT domain
                     containing 3; zinc finger, HIT type 3; zinc finger HIT
                     domain-containing protein 3; TRIP-3; HNF-4a coactivator;
                     TR-interacting protein 3"
                     /calculated_mol_wt=17476
     Region          10..44
                     /region_name="zf-HIT_ZNHIT2-3"
                     /note="zinc finger HIT (zf-HIT) found in zinc finger HIT
                     domain-containing protein 2 (ZNHIT2), 3 (ZNHIT3) and
                     similar proteins; cd23024"
                     /db_xref="CDD:467796"
     Site            order(11,14,22,25,30,34,38,42)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:467796"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15649.2)"
     CDS             1..155
                     /gene="ZNHIT3"
                     /gene_synonym="Hit1; PEHO; TRIP3"
                     /coded_by="NM_004773.4:20..487"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11312.1"
                     /db_xref="GeneID:9326"
                     /db_xref="HGNC:HGNC:12309"
                     /db_xref="MIM:604500"
ORIGIN      
        1 maslkcstvv cviclekpky rcpacrvpyc svvcfrkhke qcnpetrpve kkirsalptk
       61 tvkpvenkdd ddsiadflns deeedrvslq nlknlgesat lrslllnphl rqlmvnldqg
      121 edkaklmray mqeplfvefa dcclgiveps qnees
//
LOCUS       NP_031383                738 aa            linear   PRI 27-APR-2025
DEFINITION  conserved oligomeric Golgi complex subunit 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_031383
VERSION     NP_031383.1
DBSOURCE    REFSEQ: accession NM_007357.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Bailey Blackburn,J., Pokrovskaya,I., Fisher,P., Ungar,D. and
            Lupashin,V.V.
  TITLE     COG Complex Complexities: Detailed Characterization of a Complete
            Set of HEK293T Cells Lacking Individual COG Subunits
  JOURNAL   Front Cell Dev Biol 4, 23 (2016)
   PUBMED   27066481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Kodera,H., Ando,N., Yuasa,I., Wada,Y., Tsurusaki,Y., Nakashima,M.,
            Miyake,N., Saitoh,S., Matsumoto,N. and Saitsu,H.
  TITLE     Mutations in COG2 encoding a subunit of the conserved oligomeric
            golgi complex cause a congenital disorder of glycosylation
  JOURNAL   Clin Genet 87 (5), 455-460 (2015)
   PUBMED   24784932
  REMARK    GeneRIF: Our data strongly suggest that these compound heterozygous
            mutations in COG2 are causative of CDG.
REFERENCE   6  (residues 1 to 738)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     The binary interacting network of the conserved oligomeric Golgi
            tethering complex
  JOURNAL   J Biol Chem 279 (23), 24640-24648 (2004)
   PUBMED   15047703
REFERENCE   7  (residues 1 to 738)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   8  (residues 1 to 738)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   9  (residues 1 to 738)
  AUTHORS   Podos,S.D., Reddy,P., Ashkenas,J. and Krieger,M.
  TITLE     LDLC encodes a brefeldin A-sensitive, peripheral Golgi protein
            required for normal Golgi function
  JOURNAL   J Cell Biol 127 (3), 679-691 (1994)
   PUBMED   7962052
REFERENCE   10 (residues 1 to 738)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC349417.1, AL158214.33,
            DB449302.1, AK312678.1 and BC051906.1.
            
            Summary: This gene encodes a subunit of the conserved oligomeric
            Golgi complex that is required for maintaining normal structure and
            activity of the Golgi complex. The encoded protein specifically
            interacts with the USO1 vesicle docking protein and may be
            necessary for normal Golgi ribbon formation and trafficking of
            Golgi enzymes. Mutations of this gene are associated with abnormal
            glycosylation within the Golgi apparatus. Alternative splicing
            results in multiple transcript variants.[provided by RefSeq, Feb
            2009].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014960.1, SRR1803611.38136.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366669.9/ ENSP00000355629.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.2"
     Protein         1..738
                     /product="conserved oligomeric Golgi complex subunit 2
                     isoform 1"
                     /note="brefeldin A-sensitive, peripheral Golgi protein;
                     conserved oligomeric Golgi complex protein 2; low density
                     lipoprotein receptor defect C complementing; conserved
                     oligomeric Golgi complex subunit 2; COG complex subunit 2;
                     low density lipoprotein receptor defect C-complementing
                     protein"
                     /calculated_mol_wt=83077
     Region          15..147
                     /region_name="COG2"
                     /note="COG (conserved oligomeric Golgi) complex component,
                     COG2; pfam06148"
                     /db_xref="CDD:399271"
     Region          474..504
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14746.1)"
     Region          573..699
                     /region_name="COG2_C"
                     /note="COG complex component, COG2, C-terminal; pfam12022"
                     /db_xref="CDD:463434"
     Region          668..687
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14746.1)"
     CDS             1..738
                     /gene="COG2"
                     /gene_synonym="CDG2Q; LDLC"
                     /coded_by="NM_007357.3:127..2343"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1584.1"
                     /db_xref="GeneID:22796"
                     /db_xref="HGNC:HGNC:6546"
                     /db_xref="MIM:606974"
ORIGIN      
        1 meksrmnlpk gpdtlcfdkd efmkedfdvd hfvsdcrkrv qleelrddle lyykllktam
       61 velinkdyad fvnlstnlvg mdkalnqlsv plgqlreevl slrssvsegi ravdermskq
      121 edirkkkmcv lrliqvirsv ekiekilnsq ssketsalea ssplltgqil eriatefnql
      181 qfhavqskgm plldkvrpri agitamlqqs legllleglq tsdvdiirhc lrtyatidkt
      241 rdaealvgqv lvkpyidevi ieqfveshpn glqvmynkll efvphhcrll revtggaiss
      301 ekgntvpgyd flvnsvwpqi vqgleeklps lfnpgnpdaf hekytismdf vrrlerqcgs
      361 qasvkrlrah payhsfnkkw nlpvyfqirf reiagsleaa ltdvledapa espycllash
      421 rtwsslrrcw sdemflpllv hrlwrltlqi larysvfvne lslrpisnes pkeikkplvt
      481 gskepsitqg ntedqgsgps etkpvvsisr tqlvyvvadl dklqeqlpel leiikpklem
      541 igfknfssis aaledsqssf sacvpslssk iiqdlsdscf gflksalevp rlyrrtnkev
      601 pttassyvds alkplfqlqs ghkdklkqai iqqwlegtls esthkyyetv sdvlnsvkkm
      661 eeslkrlkqa rkttpanpvg psggmsdddk irlqlaldve ylgeqiqklg lqasdiksfs
      721 alaelvaaak dqataeqp
//
LOCUS       NP_001311025             466 aa            linear   PRI 27-APR-2025
DEFINITION  cytokine-like nuclear factor N-PAC isoform 3 [Homo sapiens].
ACCESSION   NP_001311025
VERSION     NP_001311025.2
DBSOURCE    REFSEQ: accession NM_001324096.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Gonzalez-Teran,B., Pittman,M., Felix,F., Thomas,R.,
            Richmond-Buccola,D., Huttenhain,R., Choudhary,K., Moroni,E.,
            Costa,M.W., Huang,Y., Padmanabhan,A., Alexanian,M., Lee,C.Y.,
            Maven,B.E.J., Samse-Knapp,K., Morton,S.U., McGregor,M.,
            Gifford,C.A., Seidman,J.G., Seidman,C.E., Gelb,B.D., Colombo,G.,
            Conklin,B.R., Black,B.L., Bruneau,B.G., Krogan,N.J., Pollard,K.S.
            and Srivastava,D.
  TITLE     Transcription factor protein interactomes reveal genetic
            determinants in heart disease
  JOURNAL   Cell 185 (5), 794-814 (2022)
   PUBMED   35182466
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Hu,Z., Long,T., Ma,Y., Zhu,J., Gao,L., Zhong,Y., Wang,X., Wang,X.
            and Li,Z.
  TITLE     Downregulation of GLYR1 contributes to microsatellite instability
            colorectal cancer by targeting p21 via the p38MAPK and PI3K/AKT
            pathways
  JOURNAL   J Exp Clin Cancer Res 39 (1), 76 (2020)
   PUBMED   32370786
  REMARK    GeneRIF: Downregulation of GLYR1 contributes to microsatellite
            instability colorectal cancer by targeting p21 via the p38MAPK and
            PI3K/AKT pathways.
            Erratum:[J Exp Clin Cancer Res. 2020 Jul 6;39(1):125. doi:
            10.1186/s13046-020-01635-6. PMID: 32624003]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 466)
  AUTHORS   Fei,J., Ishii,H., Hoeksema,M.A., Meitinger,F., Kassavetis,G.A.,
            Glass,C.K., Ren,B. and Kadonaga,J.T.
  TITLE     NDF, a nucleosome-destabilizing factor that facilitates
            transcription through nucleosomes
  JOURNAL   Genes Dev 32 (9-10), 682-694 (2018)
   PUBMED   29759984
REFERENCE   7  (residues 1 to 466)
  AUTHORS   Fang,R., Chen,F., Dong,Z., Hu,D., Barbera,A.J., Clark,E.A.,
            Fang,J., Yang,Y., Mei,P., Rutenberg,M., Li,Z., Zhang,Y., Xu,Y.,
            Yang,H., Wang,P., Simon,M.D., Zhou,Q., Li,J., Marynick,M.P., Li,X.,
            Lu,H., Kaiser,U.B., Kingston,R.E., Xu,Y. and Shi,Y.G.
  TITLE     LSD2/KDM1B and its cofactor NPAC/GLYR1 endow a structural and
            molecular model for regulation of H3K4 demethylation
  JOURNAL   Mol Cell 49 (3), 558-570 (2013)
   PUBMED   23260659
REFERENCE   8  (residues 1 to 466)
  AUTHORS   Vermeulen,M., Eberl,H.C., Matarese,F., Marks,H., Denissov,S.,
            Butter,F., Lee,K.K., Olsen,J.V., Hyman,A.A., Stunnenberg,H.G. and
            Mann,M.
  TITLE     Quantitative interaction proteomics and genome-wide profiling of
            epigenetic histone marks and their readers
  JOURNAL   Cell 142 (6), 967-980 (2010)
   PUBMED   20850016
REFERENCE   9  (residues 1 to 466)
  AUTHORS   Fu,J., Yang,Z., Wei,J., Han,J. and Gu,J.
  TITLE     Nuclear protein NP60 regulates p38 MAPK activity
  JOURNAL   J Cell Sci 119 (Pt 1), 115-123 (2006)
   PUBMED   16352664
REFERENCE   10 (residues 1 to 466)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020663.1 and KF456151.1.
            
            On May 9, 2019 this sequence version replaced NP_001311025.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..466
                     /product="cytokine-like nuclear factor N-PAC isoform 3"
                     /note="nuclear protein 60 kDa; nuclear protein 60kDa;
                     cytokine-like nuclear factor n-pac; putative
                     oxidoreductase GLYR1; nuclear protein NP60; nuclear
                     protein of 60 kDa; 3-hydroxyisobutyrate dehydrogenase-like
                     protein; nucleosome-destabilizing factor"
                     /calculated_mol_wt=50649
     Region          6..90
                     /region_name="PWWP_GLYR1"
                     /note="PWWP domain found in glyoxylate reductase 1 (GLYR1)
                     and similar proteins; cd05836"
                     /db_xref="CDD:438961"
     Site            order(19,22,46)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438961"
     Site            20..23
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438961"
     Region          187..464
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
     CDS             1..466
                     /gene="GLYR1"
                     /gene_synonym="BM045; HIBDL; hNDF; N-PAC; NP60; NPAC"
                     /coded_by="NM_001324096.2:24..1424"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84656"
                     /db_xref="HGNC:HGNC:24434"
                     /db_xref="MIM:610660"
ORIGIN      
        1 maavslrlgd lvwgklgryp pwpgkivnpp kdlkkprgkk cffvkffgte dhawikveql
       61 kpyhahkeem ikinkgkrfq qavdaveefl rrakgkdqdl tipesstvkg mmagpmaafk
      121 wqptasepvk dadphfhhfl lsqtekpavc yqaitkklki ceeetgstsi qaadstavng
      181 sitptdkkig flglglmgsg ivsnllkmgh tvtvwnrtae kegarlgrtp aevvstcdit
      241 facvsdpkaa kdlvlgpsgv lqgirpgkcy vdmstvdadt vtelaqvivs rggrfleapv
      301 sgnqqlsndg mlvilaagdr glyedcsscf qamgktsffl gevgnaakmm livnmvqgsf
      361 matiaegltl aqvtgqsqqt lldilnqgql asifldqkcq nilqgnfkpd fylkyiqkdl
      421 rlaialgdav nhptpmaaaa nevykrakal dqsdndmsav yrayih
//
LOCUS       NP_003411                527 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 35 [Homo sapiens].
ACCESSION   NP_003411
VERSION     NP_003411.3
DBSOURCE    REFSEQ: accession NM_003420.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Zhou,H., Liu,L.H., Zhang,H., Lei,Z. and Lan,Z.J.
  TITLE     Expression of zinc finger protein 105 in the testis and its role in
            male fertility
  JOURNAL   Mol Reprod Dev 77 (6), 511-520 (2010)
   PUBMED   20186958
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 527)
  AUTHORS   Calabro,V., Pengue,G., Bartoli,P.C., Pagliuca,A., Featherstone,T.
            and Lania,L.
  TITLE     Positional cloning of cDNAs from the human chromosome 3p21-22
            region identifies a clustered organization of zinc-finger genes
  JOURNAL   Hum Genet 95 (1), 18-21 (1995)
   PUBMED   7814019
REFERENCE   7  (residues 1 to 527)
  AUTHORS   Pengue,G., Cannada-Bartoli,P. and Lania,L.
  TITLE     The ZNF35 human zinc finger gene encodes a sequence-specific
            DNA-binding protein
  JOURNAL   FEBS Lett 321 (2-3), 233-236 (1993)
   PUBMED   8477855
REFERENCE   8  (residues 1 to 527)
  AUTHORS   Lanfrancone,L., Pengue,G., Pandolfi,P.P., Salcini,A.E.,
            Giacomucci,A., Longo,L., Donti,E., De Luca,P., La Mantia,G.,
            Pelicci,P.G. et al.
  TITLE     Structural and functional organization of the HF.10 human zinc
            finger gene (ZNF35) located on chromosome 3p21-p22
  JOURNAL   Genomics 12 (4), 720-728 (1992)
   PUBMED   1572646
REFERENCE   9  (residues 1 to 527)
  AUTHORS   Donti,E., Lanfrancone,L., Huebner,K., Pascucci,A., Venti,G.,
            Pengue,G., Grignani,F., Croce,C.M., Lania,L. and Pelicci,P.G.
  TITLE     Localization of the human HF.10 finger gene on a chromosome region
            (3p21-22) frequently deleted in human cancers
  JOURNAL   Hum Genet 84 (5), 391-395 (1990)
   PUBMED   2108922
REFERENCE   10 (residues 1 to 527)
  AUTHORS   Pannuti,A., Lanfrancone,L., Pascucci,A., Pelicci,P.G., La Mantia,G.
            and Lania,L.
  TITLE     Isolation of cDNAs encoding finger proteins and measurement of the
            corresponding mRNA levels during myeloid terminal differentiation
  JOURNAL   Nucleic Acids Res 16 (10), 4227-4237 (1988)
   PUBMED   3380682
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099669.2, BP237260.1, BC013597.1 and BC015892.1.
            
            On Jun 29, 2006 this sequence version replaced NP_003411.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.210570.1,
                                           SRR1803611.117490.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396056.7/ ENSP00000379368.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..527
                     /product="zinc finger protein 35"
                     /note="zinc finger protein 35 (clone HF.10); zinc finger
                     protein HF.10"
                     /calculated_mol_wt=58958
     Region          9..221
                     /region_name="Globular domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P13682.4)"
     Region          16..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13682.4)"
     Region          <214..369
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          224..244
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(229,231,233,235..236,239..240,243,257,259,263..264,
                     267..268,271,285,287,289,291..292,295..296,299)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          252..272
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          280..300
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          308..328
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          336..356
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(341,343,345,347..348,351..352,355,369,371,375..376,
                     379..380,383,397,399,401,403..404,407..408,411)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          364..384
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          372..>449
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          392..412
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          420..440
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          448..468
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(453,455,457,459..460,463..464,467,481,483,487..488,
                     491..492,495,509,511,513,515..516,519..520,523)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          460..485
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          474..496
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          476..496
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          488..513
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          504..524
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..527
                     /gene="ZNF35"
                     /gene_synonym="HF.10; HF10; Zfp105"
                     /coded_by="NM_003420.4:231..1814"
                     /db_xref="CCDS:CCDS2718.2"
                     /db_xref="GeneID:7584"
                     /db_xref="HGNC:HGNC:13099"
                     /db_xref="MIM:194533"
ORIGIN      
        1 mtaelreama lapwgpvkvk keeeeeenfp gqassqqvhs enikvwapvq glqtgldgse
       61 eeekgqnisw dmavvlkatq eapaastlgs yslpgtlaks eilethgtmn flgaetknlq
      121 llvpkteice eaekpliise riqkadpqgp elgeacekgn mlkrqrikre kkdfrqvivn
      181 dchlpesfke eenqkckksg gkyslnsgav knpktqlgqk pftcsvcgkg fsqsanlvvh
      241 qrihtgekpf echecgkafi qsanlvvhqr ihtgqkpyvc skcgkaftqs snltvhqkih
      301 slektfkcne cekafsyssq larhqkvhit ekcyecnecg ktftrssnli vhqrihtgek
      361 pfacndcgka ftqsanlivh qrshtgekpy eckecgkafs cfshlivhqr ihtaekpydc
      421 secgkafsql sclivhqrih sgdlpyvcne cgkaftcssy llihqrihng ekpytcnecg
      481 kafrqrsslt vhqrthtgek pyecekcgaa fisnshlmrh hrthlve
//
LOCUS       NP_689538                289 aa            linear   PRI 27-APR-2025
DEFINITION  testis-expressed protein 26 isoform a [Homo sapiens].
ACCESSION   NP_689538
VERSION     NP_689538.1
DBSOURCE    REFSEQ: accession NM_152325.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353680.8 and BC030277.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.226642.1,
                                           SRR5189667.347037.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380473.8/ ENSP00000369840.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.3"
     Protein         1..289
                     /product="testis-expressed protein 26 isoform a"
                     /note="testis-expressed sequence 26 protein;
                     testis-expressed protein 26"
                     /calculated_mol_wt=33464
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6G2.1)"
     Region          30..42
                     /region_name="Mn 1. /evidence=ECO:0000305|PubMed:38538594"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6G2.1)"
     Region          69..83
                     /region_name="Mn 2. /evidence=ECO:0000305|PubMed:38538594"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6G2.1)"
     Region          144..157
                     /region_name="Mn 3. /evidence=ECO:0000305|PubMed:38538594"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6G2.1)"
     Region          179..193
                     /region_name="Mn 4. /evidence=ECO:0000305|PubMed:38538594"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6G2.1)"
     Region          233..247
                     /region_name="Mn 5. /evidence=ECO:0000305|PubMed:38538594"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6G2.1)"
     CDS             1..289
                     /gene="TEX26"
                     /gene_synonym="C13orf26"
                     /coded_by="NM_152325.3:61..930"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9339.1"
                     /db_xref="GeneID:122046"
                     /db_xref="HGNC:HGNC:28622"
ORIGIN      
        1 meqpgprapd pslchhnlqp tddpnwdsya ttmrtaftpk tgavpalirq ngirrlgyty
       61 slsdpilnqt qysdeytwks hskedlikte tsrgikshks hlnediflwt lphcqqtgtl
      121 knclpwkipa smkevnkals nqfisltkrd fvdrskaqki kksshlslew kkllpqppdt
      181 efrrnyqipa kipelqdfsf kygcysslpv asqglvpsvl hsylrnqeht kkqttyqsdy
      241 dktypdflml lnsftssqvk eylqslsykd rqiidrfirt hcdtnkkkk
//
LOCUS       NP_056131               1090 aa            linear   PRI 27-APR-2025
DEFINITION  apoptosis-stimulating of p53 protein 1 [Homo sapiens].
ACCESSION   NP_056131
VERSION     NP_056131.2
DBSOURCE    REFSEQ: accession NM_015316.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Patel,K.D., Barasiya,Y.V., Patel,J.B. and Patel,P.S.
  TITLE     Apoptosis stimulating protein of p53 (ASPP) 1 and ASPP2 m-RNA
            expression in oral cancer
  JOURNAL   Arch Oral Biol 119, 104920 (2020)
   PUBMED   32987288
  REMARK    GeneRIF: Apoptosis stimulating protein of p53 (ASPP) 1 and ASPP2
            m-RNA expression in oral cancer.
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Liu,D., Ertay,A., Hill,C., Zhou,Y., Li,J., Zou,Y., Qiu,H., Yuan,X.,
            Ewing,R.M., Lu,X., Xiong,H. and Wang,Y.
  TITLE     ASPP1 deficiency promotes epithelial-mesenchymal transition,
            invasion and metastasis in colorectal cancer
  JOURNAL   Cell Death Dis 11 (4), 224 (2020)
   PUBMED   32269211
  REMARK    GeneRIF: ASPP1 deficiency promotes epithelial-mesenchymal
            transition, invasion and metastasis in colorectal cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1090)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1090)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1090)
  AUTHORS   Fogal,V., Kartasheva,N.N., Trigiante,G., Llanos,S., Yap,D.,
            Vousden,K.H. and Lu,X.
  TITLE     ASPP1 and ASPP2 are new transcriptional targets of E2F
  JOURNAL   Cell Death Differ 12 (4), 369-376 (2005)
   PUBMED   15731768
  REMARK    GeneRIF: target of E2F transcription factor
REFERENCE   7  (residues 1 to 1090)
  AUTHORS   Liu,Z.J., Lu,X., Zhang,Y., Zhong,S., Gu,S.Z., Zhang,X.B., Yang,X.
            and Xin,H.M.
  TITLE     Downregulated mRNA expression of ASPP and the hypermethylation of
            the 5'-untranslated region in cancer cell lines retaining wild-type
            p53
  JOURNAL   FEBS Lett 579 (7), 1587-1590 (2005)
   PUBMED   15757645
  REMARK    GeneRIF: ASPP1 CpG island aberrant methylation could be one
            molecular and genetic alteration in wild-type p53 tumours.
REFERENCE   8  (residues 1 to 1090)
  AUTHORS   Bergamaschi,D., Samuels,Y., Jin,B., Duraisingham,S., Crook,T. and
            Lu,X.
  TITLE     ASPP1 and ASPP2: common activators of p53 family members
  JOURNAL   Mol Cell Biol 24 (3), 1341-1350 (2004)
   PUBMED   14729977
REFERENCE   9  (residues 1 to 1090)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
REFERENCE   10 (residues 1 to 1090)
  AUTHORS   Samuels-Lev,Y., O'Connor,D.J., Bergamaschi,D., Trigiante,G.,
            Hsieh,J.K., Zhong,S., Campargue,I., Naumovski,L., Crook,T. and
            Lu,X.
  TITLE     ASPP proteins specifically stimulate the apoptotic function of p53
  JOURNAL   Mol Cell 8 (4), 781-794 (2001)
   PUBMED   11684014
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB461586.2, BC035446.1,
            AJ318887.2, AW295594.1 and AL049840.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 5, 2007 this sequence version replaced NP_056131.1.
            
            Summary: This gene encodes a member of the ASPP
            (apoptosis-stimulating protein of p53) family of p53 interacting
            proteins. The protein contains four ankyrin repeats and an SH3
            domain involved in protein-protein interactions. ASPP proteins are
            required for the induction of apoptosis by p53-family proteins.
            They promote DNA binding and transactivation of p53-family proteins
            on the promoters of proapoptotic genes. Expression of this gene is
            regulated by the E2F transcription factor. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035446.1, AJ318887.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000202556.14/ ENSP00000202556.9
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..1090
                     /product="apoptosis-stimulating of p53 protein 1"
                     /note="apoptosis-stimulating protein of p53, 1; protein
                     phosphatase 1, regulatory (inhibitor) subunit 13B"
                     /calculated_mol_wt=119435
     Region          2..86
                     /region_name="RA_ASPP1"
                     /note="Ras-associating (RA) domain found in
                     apoptosis-stimulating protein of p53 protein 1 (ASPP1);
                     cd17224"
                     /db_xref="CDD:340744"
     Region          82..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Region          <158..>331
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Region          376..723
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Region          <445..863
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            554
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q62415; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Region          738..803
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Region          809..828
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Region          834..881
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Region          892..978
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          892..918
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(893..894,897..899,901..902,906,909,918,920,922,
                     926..927,930..932,934..935,939,942,951,953,955,959..960,
                     963..965,967..968,972,975)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          920..952
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Region          920..951
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          953..985
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ4.3)"
     Region          953..982
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1022..1078
                     /region_name="SH3_ASPP1"
                     /note="Src Homology 3 domain of Apoptosis Stimulating of
                     p53 protein 1; cd11954"
                     /db_xref="CDD:212887"
     Site            order(1030,1033..1034,1036..1037,1055..1056,1058..1059,
                     1070,1072,1074)
                     /site_type="other"
                     /note="p53 binding site [polypeptide binding]"
                     /db_xref="CDD:212887"
     CDS             1..1090
                     /gene="PPP1R13B"
                     /gene_synonym="ASPP1; p53BP2-like; p85"
                     /coded_by="NM_015316.3:269..3541"
                     /db_xref="CCDS:CCDS41997.1"
                     /db_xref="GeneID:23368"
                     /db_xref="HGNC:HGNC:14950"
                     /db_xref="MIM:606455"
ORIGIN      
        1 mmpmiltvfl snneqiltev pitpettcrd vvefckepge gschlaevwr gnerpipfdh
       61 mmyehlqkwg prreevkffl rhedsptens eqggrqtqeq rtqrnvinvp gekrtengvg
      121 nprveltlse lqdmaarqqq qienqqqmlv akeqrlhflk qqerrqqqsi seneklqklk
      181 erveaqenkl kkiramrgqv dyskimngnl saeierfsam fqekkqevqt ailrvdqlsq
      241 qledlkkgkl ngfqsyngkl tgpaavelkr lyqelqirnq lnqeqnsklq qqkellnkrn
      301 mevammdkri selrerlygk kiqlnrvngt sspqsplsts grvaavgpyi qvpsagsfpv
      361 lgdpikpqsl siasnaahgr sksandgnwp tlkqnssssv kpvqvagadw kdpsvegsvk
      421 qgtvssqpvp fsalgptekp gieigkvppp ipgvgkqlpp sygtypsptp lgpgstssle
      481 rrkegslprp saglpsrqrp tllpatgstp qpgssqqiqq risvppspty ppagppafpa
      541 gdskpelplt vairpfladk gsrpqsprkg pqtvnsssiy smylqqatpp knyqpaahsa
      601 lnksvkavyg kpvlpsgsts psplpflhgs lstgtpqpqp psestekepe qdgpaapadg
      661 stveslprpl sptkltpivh splryqsdad lealrrklan aprplkkrss itepegpggp
      721 niqkllyqrf ntlaggmegt pfyqpspsqd fmgtladvdn gntnangnle elppaqptap
      781 lpaepapssd andnelpspe peelicpqtt hqtaepaedn nnnvatvptt eqipspvaea
      841 pspgeeqvpp aplppashpp atstnkrtnl kkpnsertgh glrvrfnpla llldaslege
      901 fdlvqriiye vedpskpnde gitplhnavc aghhhivkfl ldfgvnvnaa dsdgwtplhc
      961 aascnsvhlc kqlvesgaai fastisdiet aadkceemee gyiqcsqfly gvqeklgvmn
     1021 kgvayalwdy eaqnsdelsf hegdaltilr rkdeseteww warlgdregy vpknllglyp
     1081 rikprqrtla
//
LOCUS       NP_001349897              85 aa            linear   ROD 27-APR-2025
DEFINITION  7-methylguanosine phosphate-specific 5'-nucleotidase isoform 5 [Mus
            musculus].
ACCESSION   NP_001349897
VERSION     NP_001349897.1
DBSOURCE    REFSEQ: accession NM_001362968.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590968.8 and AK166393.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK166393.1, BY735095.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 63.47 cM"
     Protein         1..85
                     /product="7-methylguanosine phosphate-specific
                     5'-nucleotidase isoform 5"
                     /EC_number="3.1.3.5"
                     /EC_number="3.1.3.91"
                     /note="cytosolic 5'-nucleotidase III-like protein;
                     cN-III-like protein; 5'-nucleotidase, cytosolic III-like;
                     cytosolic 5'-nucleotidase 3B; 7-methylguanosine
                     phosphate-specific 5'-nucleotidase; 7-methylguanosine
                     nucleotidase; N(7)-methylguanylate 5'-phosphatase"
                     /calculated_mol_wt=9301
     Region          17..>76
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     CDS             1..85
                     /gene="Nt5c3b"
                     /gene_synonym="2610037D24Rik; C330027I04Rik; Nt5c3l"
                     /coded_by="NM_001362968.1:44..301"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:68106"
                     /db_xref="MGI:MGI:1915356"
ORIGIN      
        1 maeevsslmk atvlmrqpgr vqeivgalrr gggdrlqvis dfdmtlsrfa yngqrcpssh
       61 nildnskiis edcrkecget cnprg
//
LOCUS       NP_001323               1225 aa            linear   PRI 27-APR-2025
DEFINITION  catenin delta-2 isoform 1 [Homo sapiens].
ACCESSION   NP_001323
VERSION     NP_001323.1
DBSOURCE    REFSEQ: accession NM_001332.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1225)
  AUTHORS   Assendorp,N., Fossati,M., Libe-Philippot,B., Christopoulou,E.,
            Depp,M., Rapone,R., Dingli,F., Loew,D., Vanderhaeghen,P. and
            Charrier,C.
  TITLE     CTNND2 moderates the pace of synaptic maturation and links human
            evolution to synaptic neoteny
  JOURNAL   Cell Rep 43 (10), 114797 (2024)
   PUBMED   39352808
  REMARK    GeneRIF: CTNND2 moderates the pace of synaptic maturation and links
            human evolution to synaptic neoteny.
REFERENCE   2  (residues 1 to 1225)
  AUTHORS   Pauly,M., Krumbiegel,M., Trumpp,S., Braig,S., Rupprecht,T.,
            Kraus,C., Uebe,S., Reis,A. and Vasileiou,G.
  TITLE     Severe manifestation of Rauch-Azzarello syndrome associated with
            biallelic deletion of CTNND2
  JOURNAL   Clin Genet 106 (2), 180-186 (2024)
   PUBMED   38604781
  REMARK    GeneRIF: Severe manifestation of Rauch-Azzarello syndrome
            associated with biallelic deletion of CTNND2.
REFERENCE   3  (residues 1 to 1225)
  AUTHORS   Li,M., Nopparat,J., Aguilar,B.J., Chen,Y.H., Zhang,J., Du,J.,
            Ai,X., Luo,Y., Jiang,Y., Boykin,C. and Lu,Q.
  TITLE     Intratumor delta-catenin heterogeneity driven by genomic
            rearrangement dictates growth factor dependent prostate cancer
            progression
  JOURNAL   Oncogene 39 (22), 4358-4374 (2020)
   PUBMED   32313227
  REMARK    GeneRIF: Intratumor delta-catenin heterogeneity driven by genomic
            rearrangement dictates growth factor dependent prostate cancer
            progression.
REFERENCE   4  (residues 1 to 1225)
  AUTHORS   Miller,D.E., Squire,A. and Bennett,J.T.
  TITLE     A child with autism, behavioral issues, and dysmorphic features
            found to have a tandem duplication within CTNND2 by mate-pair
            sequencing
  JOURNAL   Am J Med Genet A 182 (3), 543-547 (2020)
   PUBMED   31814264
  REMARK    GeneRIF: A child with autism, behavioral issues, and dysmorphic
            features found to have a tandem duplication within CTNND2 by
            mate-pair sequencing.
REFERENCE   5  (residues 1 to 1225)
  AUTHORS   Liang,Y., Feng,Y., Wu,W., Chang,C., Chen,D., Chen,S. and Zhen,G.
  TITLE     microRNA-218-5p plays a protective role in eosinophilic airway
            inflammation via targeting delta-catenin, a novel catenin in asthma
  JOURNAL   Clin Exp Allergy 50 (1), 29-40 (2020)
   PUBMED   31520422
  REMARK    GeneRIF: microRNA-218-5p plays a protective role in eosinophilic
            airway inflammation via targeting delta-catenin, a novel catenin in
            asthma.
REFERENCE   6  (residues 1 to 1225)
  AUTHORS   Lu,Q., Paredes,M., Medina,M., Zhou,J., Cavallo,R., Peifer,M.,
            Orecchio,L. and Kosik,K.S.
  TITLE     delta-catenin, an adhesive junction-associated protein which
            promotes cell scattering
  JOURNAL   J Cell Biol 144 (3), 519-532 (1999)
   PUBMED   9971746
REFERENCE   7  (residues 1 to 1225)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 1225)
  AUTHORS   Paffenholz,R. and Franke,W.W.
  TITLE     Identification and localization of a neurally expressed member of
            the plakoglobin/armadillo multigene family
  JOURNAL   Differentiation 61 (5), 293-304 (1997)
   PUBMED   9342840
REFERENCE   9  (residues 1 to 1225)
  AUTHORS   Zhou,J., Liyanage,U., Medina,M., Ho,C., Simmons,A.D., Lovett,M. and
            Kosik,K.S.
  TITLE     Presenilin 1 interaction in the brain with a novel member of the
            Armadillo family
  JOURNAL   Neuroreport 8 (8), 2085-2090 (1997)
   PUBMED   9223106
REFERENCE   10 (residues 1 to 1225)
  AUTHORS   Simmons,A.D., Overhauser,J. and Lovett,M.
  TITLE     Isolation of cDNAs from the Cri-du-chat critical region by direct
            screening of a chromosome 5-specific cDNA library
  JOURNAL   Genome Res 7 (2), 118-127 (1997)
   PUBMED   9049630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127460.2, DC341093.1,
            AB013805.1, U52351.1, U96136.1 and AC010626.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an adhesive junction associated protein
            of the armadillo/beta-catenin superfamily and is implicated in
            brain and eye development and cancer formation. The protein encoded
            by this gene promotes the disruption of E-cadherin based adherens
            junction to favor cell spreading upon stimulation by hepatocyte
            growth factor. This gene is overexpressed in prostate
            adenocarcinomas and is associated with decreased expression of
            tumor suppressor E-cadherin in this tissue. This gene resides in a
            region of the short arm of chromosome 5 that is deleted in Cri du
            Chat syndrome. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Dec
            2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U96136.1, AB013805.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304623.13/ ENSP00000307134.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..1225
                     /product="catenin delta-2 isoform 1"
                     /note="catenin (cadherin-associated protein), delta 2
                     (neural plakophilin-related arm-repeat protein); T-cell
                     delta-catenin; neurojungin"
                     /calculated_mol_wt=132526
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          87..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          134..242
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          163..>534
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            209
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          256..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            264
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            282
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            296
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          394..438
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          432..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          514..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          540..579
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          550..>723
                     /region_name="PLN03200"
                     /note="cellulose synthase-interactive protein;
                     Provisional"
                     /db_xref="CDD:215629"
     Region          552..577
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(568,572,576,610,614,618,655,659,663)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          581..621
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          582..621
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          585..621
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          625..666
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          626..666
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          629..664
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          671..722
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          682..724
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          728..773
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          834..875
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          835..875
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          838..875
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          882..921
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          885..920
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          885..919
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          926..972
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          974..1018
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          975..1018
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Region          978..1013
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          1042..1077
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     Site            1076
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35927; propagated from
                     UniProtKB/Swiss-Prot (Q9UQB3.3)"
     CDS             1..1225
                     /gene="CTNND2"
                     /gene_synonym="GT24; NPRAP"
                     /coded_by="NM_001332.4:594..4271"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3881.1"
                     /db_xref="GeneID:1501"
                     /db_xref="HGNC:HGNC:2516"
                     /db_xref="MIM:604275"
ORIGIN      
        1 mfarkppgaa plgampvpdq pssasektss lspglntsng dgsetettsa ilasvkeqel
       61 qferltrele aerqivasql ercklgsetg smssmssaee qfqwqsqdgq kdiedelttg
      121 lelvdscirs lqesgildpq dystgerpsl lsqsalqlns kpegsfqypa syhsnqtlal
      181 gettpsqlpa rgtqaratgq sfsqgttsra ghlagpepap pppppprepf apslgsafhl
      241 pdappaaaaa alyyssstlp apprggspla apqggsptkl qrggsapega tyaaprgssp
      301 kqspsrlaks ystsspiniv vssaglspir vtspptvqst issspihqls stigtyatls
      361 ptkrlvhase qyskhsqely atatlqrpgs laagsrasys sqhghlgpel ralqspehhi
      421 dpiyedrvyq kppmrslsqs qgdplppaht gtyrtstaps spgvdsvplq rtgsqhgpqn
      481 aaaatfqras yaagpasnya dpyrqlqycp svespysksg palppegtla rspsidsiqk
      541 dprefgwrdp elpeviqmlq hqfpsvqsna aaylqhlcfg dnkikaeirr qggiqllvdl
      601 ldhrmtevhr sacgalrnlv ygkanddnki alkncggipa lvrllrkttd leirelvtgv
      661 lwnlsscdal kmpiiqdala vltnaviiph sgwensplqd drkiqlhssq vlrnatgclr
      721 nvssageear rrmrecdglt dallyviqsa lgsseidskt vencvcilrn lsyrlaaets
      781 qgqhmgtdel dgllcgeang kdaessgcwg kkkkkkksqd qwdgvgplpd caeppkgiqm
      841 lwhpsivkpy ltllsecsnp dtlegaagal qnlaagswkw svyiraavrk ekglpilvel
      901 lridndrvvc avatalrnma ldvrnkelig kyamrdlvhr lpggnnsnnt askamsddtv
      961 tavcctlhev itknmenaka lrdaggiekl vgiskskgdk hspkvvkaas qvlnsmwqyr
     1021 dlrslykkdg wsqyhfvass stierdrqrp ysssrtpsis pvrvspnnrs asapasprem
     1081 islkerktdy ectgsnatyh gakgehtsrk damtaqntgi stlyrnsyga paedikhnqv
     1141 saqpvpqeps rkdyetyqpf qnstrnydes ffedqvhhrp paseytmhlg lkstgnyvdf
     1201 ysaarpysel nyetshypas pdswv
//
LOCUS       NP_001265724             375 aa            linear   PRI 27-APR-2025
DEFINITION  neuropeptide Y receptor type 4-2 [Homo sapiens].
ACCESSION   NP_001265724 XP_003846542 XP_003846799 XP_011537416
VERSION     NP_001265724.1
DBSOURCE    REFSEQ: accession NM_001278795.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Yan,H., Yang,J., Marasco,J., Yamaguchi,K., Brenner,S., Collins,F.
            and Karbon,W.
  TITLE     Cloning and functional expression of cDNAs encoding human and rat
            pancreatic polypeptide receptors
  JOURNAL   Proc Natl Acad Sci U S A 93 (10), 4661-4665 (1996)
   PUBMED   8643460
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Lundell,I., Blomqvist,A.G., Berglund,M.M., Schober,D.A.,
            Johnson,D., Statnick,M.A., Gadski,R.A., Gehlert,D.R. and
            Larhammar,D.
  TITLE     Cloning of a human receptor of the NPY receptor family with high
            affinity for pancreatic polypeptide and peptide YY
  JOURNAL   J Biol Chem 270 (49), 29123-29128 (1995)
   PUBMED   7493937
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Bard,J.A., Walker,M.W., Branchek,T.A. and Weinshank,R.L.
  TITLE     Cloning and functional expression of a human Y4 subtype receptor
            for pancreatic polypeptide, neuropeptide Y, and peptide YY
  JOURNAL   J Biol Chem 270 (45), 26762-26765 (1995)
   PUBMED   7592911
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245041.3.
            
            On or before May 2, 2019 this sequence version replaced
            XP_011537416.1, XP_003846542.1, XP_003846799.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.39685.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.22"
     Protein         1..375
                     /product="neuropeptide Y receptor type 4-2"
                     /note="neuropeptide Y receptor Y42; Neuropeptide Y
                     receptor type 4; Pancreatic polypeptide receptor 1"
                     /calculated_mol_wt=42064
     Site            2
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0DQD5.1)"
     Site            19
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0DQD5.1)"
     Site            29
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0DQD5.1)"
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DQD5.1)"
     Region          42..333
                     /region_name="7tmA_NPY4R"
                     /note="neuropeptide Y receptor type 4, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15397"
                     /db_xref="CDD:320519"
     Region          43..69
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320519"
     Region          76..101
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320519"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DQD5.1)"
     Site            order(98,101..102,114..119,121..122,125,168,170..174,211,
                     214..216,218..220,222..223,278,281..282,284..285,288,
                     300..301,303..305,308,311..312)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320519"
     Region          114..144
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320519"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DQD5.1)"
     Region          155..176
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320519"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DQD5.1)"
     Site            187
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0DQD5.1)"
     Region          211..240
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320519"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DQD5.1)"
     Region          258..288
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320519"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DQD5.1)"
     Region          301..326
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320519"
     Site            302..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DQD5.1)"
     CDS             1..375
                     /gene="NPY4R2"
                     /gene_synonym="CH17-360D5.1; NPY4-R; NPY4R; PP1; PPYR1"
                     /coded_by="NM_001278795.2:336..1463"
                     /db_xref="CCDS:CCDS81459.1"
                     /db_xref="GeneID:100996758"
                     /db_xref="HGNC:HGNC:52383"
ORIGIN      
        1 mntshllall lpkspqgenr skplgtpynf sehcqdsvdv mvfivtsysi etvvgvlgnl
       61 clmcvtvrqk ekanvtnlli anlafsdflm cllcqpltav ytimdywifg etlckmsafi
      121 qcmsvtvsil slvlvalerh qliinptgwk psisqaylgi vliwviacvl slpflansil
      181 envfhknhsk alefladkvv cteswplahh rtiyttflll fqyclplgfi lvcyariyrr
      241 lqrqgrvfhk gtyslraghm kqvnvvlvvm vvafavlwlp lhvfnsledw hheaipichg
      301 nliflvchll amastcvnpf iygflntnfk keikalvltc qqsapleese hlplstvhte
      361 vskgslrlsg rsnpi
//
LOCUS       NP_002430               1137 aa            linear   PRI 27-APR-2025
DEFINITION  DNA mismatch repair protein Msh3 [Homo sapiens].
ACCESSION   NP_002430
VERSION     NP_002430.3
DBSOURCE    REFSEQ: accession NM_002439.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Singh,S., Singh,N., Gupta,P.S.S., Panda,S.K., Dhamija,I.,
            Nathiya,D., Kumar,S. and Sharma,S.
  TITLE     Assessing the impact of MSH3 and MSH6 polymorphisms on lung cancer
            risk in North Indian patients undergoing platinum chemotherapy
            through molecular dynamics simulation
  JOURNAL   Sci Rep 14 (1), 16164 (2024)
   PUBMED   39003369
  REMARK    GeneRIF: Assessing the impact of MSH3 and MSH6 polymorphisms on
            lung cancer risk in North Indian patients undergoing platinum
            chemotherapy through molecular dynamics simulation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Rashid,M., Rashid,R., Gadewal,N., Carethers,J.M., Koi,M., Brim,H.
            and Ashktorab,H.
  TITLE     High-throughput sequencing and in-silico analysis confirm
            pathogenicity of novel MSH3 variants in African American colorectal
            cancer
  JOURNAL   Neoplasia 49, 100970 (2024)
   PUBMED   38281411
  REMARK    GeneRIF: High-throughput sequencing and in-silico analysis confirm
            pathogenicity of novel MSH3 variants in African American colorectal
            cancer.
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wang,X., Qu,Y., Xing,R., Zhou,J., Liu,Y., Zhang,H., Zhu,J., Ma,J.,
            Cui,X., Song,T., Xing,S., Ji,G., Liu,P., Sun,W., Fu,S. and Meng,X.
  TITLE     Novel insights into the ecDNA formation mechanism involving MSH3 in
            methotrexate-resistant human colorectal cancer cells
  JOURNAL   Int J Oncol 63 (6) (2023)
   PUBMED   37888748
  REMARK    GeneRIF: Novel insights into the ecDNA formation mechanism
            involving MSH3 in methotrexate-resistant human colorectal cancer
            cells.
REFERENCE   4  (residues 1 to 1137)
  AUTHORS   Villy,M.C., Masliah-Planchon,J., Schnitzler,A., Delhomelle,H.,
            Buecher,B., Filser,M., Merchadou,K., Golmard,L., Melaabi,S.,
            Vacher,S., Blanluet,M., Suybeng,V., Corsini,C., Dhooge,M.,
            Hamzaoui,N., Farelly,S., Ait Omar,A., Benamouzig,R., Caumette,V.,
            Bahuau,M., Cucherousset,J., Allory,Y., Stoppa-Lyonnet,D., Bieche,I.
            and Colas,C.
  TITLE     MSH3: a confirmed predisposing gene for adenomatous polyposis
  JOURNAL   J Med Genet 60 (12), 1198-1205 (2023)
   PUBMED   37402566
  REMARK    GeneRIF: MSH3: a confirmed predisposing gene for adenomatous
            polyposis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1137)
  AUTHORS   Oh,J.M., Kang,Y., Park,J., Sung,Y., Kim,D., Seo,Y., Lee,E.A.,
            Ra,J.S., Amarsanaa,E., Park,Y.U., Lee,S.Y., Hwang,J.M., Kim,H.,
            Scharer,O., Cho,S.W., Lee,C., Takata,K.I., Lee,J.Y. and Myung,K.
  TITLE     MSH2-MSH3 promotes DNA end resection during homologous
            recombination and blocks polymerase theta-mediated end-joining
            through interaction with SMARCAD1 and EXO1
  JOURNAL   Nucleic Acids Res 51 (11), 5584-5602 (2023)
   PUBMED   37140056
  REMARK    GeneRIF: MSH2-MSH3 promotes DNA end resection during homologous
            recombination and blocks polymerase theta-mediated end-joining
            through interaction with SMARCAD1 and EXO1.
REFERENCE   6  (residues 1 to 1137)
  AUTHORS   Risinger,J.I., Umar,A., Boyd,J., Berchuck,A., Kunkel,T.A. and
            Barrett,J.C.
  TITLE     Mutation of MSH3 in endometrial cancer and evidence for its
            functional role in heteroduplex repair
  JOURNAL   Nat Genet 14 (1), 102-105 (1996)
   PUBMED   8782829
REFERENCE   7  (residues 1 to 1137)
  AUTHORS   Watanabe,A., Ikejima,M., Suzuki,N. and Shimada,T.
  TITLE     Genomic organization and expression of the human MSH3 gene
  JOURNAL   Genomics 31 (3), 311-318 (1996)
   PUBMED   8838312
REFERENCE   8  (residues 1 to 1137)
  AUTHORS   Shinya,E. and Shimada,T.
  TITLE     Identification of two initiator elements in the bidirectional
            promoter of the human dihydrofolate reductase and mismatch repair
            protein 1 genes
  JOURNAL   Nucleic Acids Res 22 (11), 2143-2149 (1994)
   PUBMED   8029024
REFERENCE   9  (residues 1 to 1137)
  AUTHORS   Fujii,H. and Shimada,T.
  TITLE     Isolation and characterization of cDNA clones derived from the
            divergently transcribed gene in the region upstream from the human
            dihydrofolate reductase gene
  JOURNAL   J Biol Chem 264 (17), 10057-10064 (1989)
   PUBMED   2722860
REFERENCE   10 (residues 1 to 1137)
  AUTHORS   Chen,M.J., Shimada,T., Moulton,A.D., Cline,A., Humphries,R.K.,
            Maizel,J. and Nienhuis,A.W.
  TITLE     The functional human dihydrofolate reductase gene
  JOURNAL   J Biol Chem 259 (6), 3933-3943 (1984)
   PUBMED   6323448
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC130434.1, J04810.1,
            AC022493.12, U61981.1 and AA601983.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 28, 2010 this sequence version replaced NP_002430.2.
            
            Summary: The protein encoded by this gene forms a heterodimer with
            MSH2 to form MutS beta, part of the post-replicative DNA mismatch
            repair system. MutS beta initiates mismatch repair by binding to a
            mismatch and then forming a complex with MutL alpha heterodimer.
            This gene contains a polymorphic 9 bp tandem repeat sequence in the
            first exon. The repeat is present 6 times in the reference genome
            sequence and 3-7 repeats have been reported. Defects in this gene
            are a cause of susceptibility to endometrial cancer. [provided by
            RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U61981.1, SRR1803615.35610.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265081.7/ ENSP00000265081.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..1137
                     /product="DNA mismatch repair protein Msh3"
                     /note="mismatch repair protein 1; divergent upstream
                     protein; hMSH3; epididymis secretory sperm binding
                     protein"
                     /calculated_mol_wt=127281
     Region          31..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20585.4)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20585.4)"
     Region          75..297
                     /region_name="Interaction with EXO1.
                     /evidence=ECO:0000269|PubMed:11427529"
                     /note="propagated from UniProtKB/Swiss-Prot (P20585.4)"
     Region          201..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20585.4)"
     Region          225..1094
                     /region_name="MutS"
                     /note="DNA mismatch repair ATPase MutS [Replication,
                     recombination and repair]; COG0249"
                     /db_xref="CDD:440019"
     Site            1099
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P20585.4)"
     CDS             1..1137
                     /gene="MSH3"
                     /gene_synonym="DUP; FAP4; MRP1"
                     /coded_by="NM_002439.5:77..3490"
                     /db_xref="CCDS:CCDS34195.1"
                     /db_xref="GeneID:4437"
                     /db_xref="HGNC:HGNC:7326"
                     /db_xref="MIM:600887"
ORIGIN      
        1 msrrkpasgg laasssapar qavlsrffqs tgslkstsss tgaadqvdpg aaaaaaaaaa
       61 aappappapa fppqlpphia teidrrkkrp lendgpvkkk vkkvqqkegg sdlgmsgnse
      121 pkkclrtrnv sksleklkef ccdsalpqsr vqteslqerf avlpkctdfd disllhakna
      181 vssedskrqi nqkdttlfdl sqfgssntsh enlqktasks ankrsksiyt plelqyiemk
      241 qqhkdavlcv ecgykyrffg edaeiaarel niychldhnf mtasipthrl fvhvrrlvak
      301 gykvgvvkqt etaalkaigd nrsslfsrkl talytkstli gedvnplikl ddavnvdeim
      361 tdtstsyllc isenkenvrd kkkgnifigi vgvqpatgev vfdsfqdsas rseletrmss
      421 lqpvelllps alseqteali hratsvsvqd drirvermdn iyfeyshafq avtefyakdt
      481 vdikgsqiis givnlekpvi cslaaiikyl kefnlekmls kpenfkqlss kmefmtingt
      541 tlrnleilqn qtdmktkgsl lwvldhtkts fgrrklkkwv tqpllklrei narldavsev
      601 lhsessvfgq ienhlrklpd ierglcsiyh kkcstqeffl ivktlyhlks efqaiipavn
      661 shiqsdllrt vileipells pvehylkiln eqaakvgdkt elfkdlsdfp likkrkdeiq
      721 gvideirmhl qeirkilknp saqyvtvsgq efmieiknsa vsciptdwvk vgstkavsrf
      781 hspfivenyr hlnqlreqlv ldcsaewldf lekfsehyhs lckavhhlat vdcifslakv
      841 akqgdycrpt vqeerkivik ngrhpvidvl lgeqdqyvpn ntdlsedser vmiitgpnmg
      901 gkssyikqva litimaqigs yvpaeeatig ivdgiftrmg aadniykgqs tfmeeltdta
      961 eiirkatsqs lvildelgrg tsthdgiaia yatleyfird vksltlfvth yppvcelekn
     1021 yshqvgnyhm gflvsedesk ldpgaaeqvp dfvtflyqit rgiaarsygl nvakladvpg
     1081 eilkkaahks keleglintk rkrlkyfakl wtmhnaqdlq kwteefnmee tqtsllh
//
LOCUS       NP_060952               1129 aa            linear   PRI 27-APR-2025
DEFINITION  arf-GAP with SH3 domain, ANK repeat and PH domain-containing
            protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_060952
VERSION     NP_060952.2
DBSOURCE    REFSEQ: accession NM_018482.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Zhang,Y., Bai,H., Zhang,W., Gao,J., Gao,C., Deng,T., Liu,X.,
            Sun,X., Liu,Y., Wang,N. and Wu,Y.
  TITLE     miR-212/132 attenuates OVA-induced airway inflammation by
            inhibiting mast cells activation through MRGPRX2 and ASAP1
  JOURNAL   Exp Cell Res 433 (2), 113828 (2023)
   PUBMED   37875175
  REMARK    GeneRIF: miR-212/132 attenuates OVA-induced airway inflammation by
            inhibiting mast cells activation through MRGPRX2 and ASAP1.
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Park,H., Son,H., Cha,H., Song,K., Bang,S., Jee,S., Kim,H.,
            Myung,J., Shin,S.J., Cha,C., Chung,M.S. and Paik,S.
  TITLE     ASAP1 Expression in Invasive Breast Cancer and Its Prognostic Role
  JOURNAL   Int J Mol Sci 24 (18), 14355 (2023)
   PUBMED   37762658
  REMARK    GeneRIF: ASAP1 Expression in Invasive Breast Cancer and Its
            Prognostic Role.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Barbagallo,C., Stella,M., Di Mauro,S., Scamporrino,A.,
            Filippello,A., Scionti,F., Di Martino,M.T., Purrello,M., Ragusa,M.,
            Purrello,F. and Piro,S.
  TITLE     An Uncharacterised lncRNA Coded by the ASAP1 Locus Is Downregulated
            in Serum of Type 2 Diabetes Mellitus Patients
  JOURNAL   Int J Mol Sci 24 (17), 13485 (2023)
   PUBMED   37686290
  REMARK    GeneRIF: An Uncharacterised lncRNA Coded by the ASAP1 Locus Is
            Downregulated in Serum of Type 2 Diabetes Mellitus Patients.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1129)
  AUTHORS   Xie,W., Han,Z., Zuo,Z., Xin,D., Chen,H., Huang,J., Zhu,S., Lou,H.,
            Yu,Z., Chen,C., Chen,S., Hu,Y., Huang,J., Zhang,F., Ni,Z., Shen,X.,
            Xue,X. and Lin,K.
  TITLE     ASAP1 activates the IQGAP1/CDC42 pathway to promote tumor
            progression and chemotherapy resistance in gastric cancer
  JOURNAL   Cell Death Dis 14 (2), 124 (2023)
   PUBMED   36792578
  REMARK    GeneRIF: ASAP1 activates the IQGAP1/CDC42 pathway to promote tumor
            progression and chemotherapy resistance in gastric cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1129)
  AUTHORS   Cui,X., Yuan,T., Ning,P., Han,J., Liu,Y., Feng,J., Lian,F., Hao,M.,
            Dong,L., Hao,J., Xing,L. and Wu,C.
  TITLE     Polymorphisms in the ASAP1 and SP110 Genes and Its Association with
            the Susceptibility to Pulmonary Tuberculosis in a Mongolian
            Population
  JOURNAL   J Immunol Res 2022, 2713869 (2022)
   PUBMED   36249417
  REMARK    GeneRIF: Polymorphisms in the ASAP1 and SP110 Genes and Its
            Association with the Susceptibility to Pulmonary Tuberculosis in a
            Mongolian Population.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1129)
  AUTHORS   Oshiro,T., Koyama,S., Sugiyama,S., Kondo,A., Onodera,Y.,
            Asahara,T., Sabe,H. and Kikuchi,A.
  TITLE     Interaction of POB1, a downstream molecule of small G protein Ral,
            with PAG2, a paxillin-binding protein, is involved in cell
            migration
  JOURNAL   J Biol Chem 277 (41), 38618-38626 (2002)
   PUBMED   12149250
  REMARK    GeneRIF: These results suggest that POB1 interacts with PAG2
            through its proline-rich motif, thereby regulating cell migration
            (PAG2).
REFERENCE   7  (residues 1 to 1129)
  AUTHORS   Scott,M.P., Zappacosta,F., Kim,E.Y., Annan,R.S. and Miller,W.T.
  TITLE     Identification of novel SH3 domain ligands for the Src family
            kinase Hck. Wiskott-Aldrich syndrome protein (WASP),
            WASP-interacting protein (WIP), and ELMO1
  JOURNAL   J Biol Chem 277 (31), 28238-28246 (2002)
   PUBMED   12029088
REFERENCE   8  (residues 1 to 1129)
  AUTHORS   Liu,Y., Loijens,J.C., Martin,K.H., Karginov,A.V. and Parsons,J.T.
  TITLE     The association of ASAP1, an ADP ribosylation factor-GTPase
            activating protein, with focal adhesion kinase contributes to the
            process of focal adhesion assembly
  JOURNAL   Mol Biol Cell 13 (6), 2147-2156 (2002)
   PUBMED   12058076
REFERENCE   9  (residues 1 to 1129)
  AUTHORS   Furman,C., Short,S.M., Subramanian,R.R., Zetter,B.R. and
            Roberts,T.M.
  TITLE     DEF-1/ASAP1 is a GTPase-activating protein (GAP) for ARF1 that
            enhances cell motility through a GAP-dependent mechanism
  JOURNAL   J Biol Chem 277 (10), 7962-7969 (2002)
   PUBMED   11773070
  REMARK    GeneRIF: DEF-1 alters cell motility through the deactivation of
            ARF1. In contrast, the inhibition of cell spreading by DEF-1 was
            not dependent on GAP activity, indicating that spreading and
            motility are altered by DEF-1 through different pathways.
REFERENCE   10 (residues 1 to 1129)
  AUTHORS   Brown,M.T., Andrade,J., Radhakrishna,H., Donaldson,J.G.,
            Cooper,J.A. and Randazzo,P.A.
  TITLE     ASAP1, a phospholipid-dependent arf GTPase-activating protein that
            associates with and is phosphorylated by Src
  JOURNAL   Mol Cell Biol 18 (12), 7038-7051 (1998)
   PUBMED   9819391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP005856.2, DA319233.1,
            BC137135.1, AB033075.1 and AI494058.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 2, 2004 this sequence version replaced NP_060952.1.
            
            Summary: This gene encodes an ADP-ribosylation factor (ARF)
            GTPase-activating protein. The GTPase-activating activity is
            stimulated by phosphatidylinositol 4,5-biphosphate (PIP2), and is
            greater towards ARF1 and ARF5, and lesser for ARF6. This gene maybe
            involved in regulation of membrane trafficking and cytoskeleton
            remodeling. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR3218372.153065.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000518721.6/ ENSP00000429900.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21-q24.22"
     Protein         1..1129
                     /product="arf-GAP with SH3 domain, ANK repeat and PH
                     domain-containing protein 1 isoform 1"
                     /note="centaurin, beta 4; arf-GAP with SH3 domain, ANK
                     repeat and PH domain-containing protein 1; DEF-1;
                     PIP2-dependent ARF1 GAP; ARF GTPase-activating protein 1;
                     development and differentiation-enhancing factor 1;
                     ADP-ribosylation factor-directed GTPase-activating protein
                     1; 130 kDa phosphatidylinositol 4,5-biphosphate-dependent
                     ARF1 GTPase-activating protein; 130 kDa
                     phosphatidylinositol 4,5-bisphosphate-dependent ARF1
                     GTPase-activating protein"
                     /calculated_mol_wt=125367
     Region          54..268
                     /region_name="BAR_ASAP1"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with
                     SH3 domain, ANK repeat and PH domain containing protein 1;
                     cd07641"
                     /db_xref="CDD:153325"
     Site            order(63,66..67,71,73..74,77..78,80..81,91..92,94..95,
                     98..99,101..102,105,121,124..125,226,229..230,232,234,
                     237..238,240..241,247..248,251..252,254..255,258..259,
                     261..262)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153325"
     Region          316..422
                     /region_name="PH_ASAP"
                     /note="ArfGAP with SH3 domain, ankyrin repeat and PH
                     domain Pleckstrin homology (PH) domain; cd13251"
                     /db_xref="CDD:270071"
     Region          437..558
                     /region_name="ArfGap_ASAP1"
                     /note="ArfGAP domain of ASAP1 (ArfGAP with SH3 domain, ANK
                     repeat and PH domain-containing protein 1); cd08848"
                     /db_xref="CDD:350073"
     Site            order(440..441,444,467..469,490,498..502,504..506,
                     508..510,514..515,518..519,550,553..554)
                     /site_type="other"
                     /note="putative ANK repeat binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350073"
     Site            order(454,457,474,477,539)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350073"
     Site            order(454,457,474,477,482)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350073"
     Site            order(479,482..483)
                     /site_type="other"
                     /note="putative GTP binding site [chemical binding]"
                     /db_xref="CDD:350073"
     Region          <582..693
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          600..632
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Region          601..634
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(602,606..607,610..612,617..618,622,625,634,636,638,
                     642..643,646..648,650..651,655,658,667,669,671,675..676,
                     679..681,683..684,688)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          636..667
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          636..665
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Region          713..760
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            717
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Region          <724..1060
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q1AAU6; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Region          776..1062
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            839
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            843
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            1008
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            1027
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            1041
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            1048
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWY8; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Region          1071..1127
                     /region_name="SH3_ASAP1"
                     /note="Src homology 3 domain of ArfGAP with SH3 domain,
                     ankyrin repeat and PH domain containing protein 1;
                     cd11965"
                     /db_xref="CDD:212898"
     Site            order(1076,1078,1081,1085,1103..1104,1120,1122..1123)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212898"
     Site            1128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWY8; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     CDS             1..1129
                     /gene="ASAP1"
                     /gene_synonym="AMAP1; CENTB4; DDEF1; PAG2; PAP; ZG14P"
                     /coded_by="NM_018482.4:243..3632"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6362.1"
                     /db_xref="GeneID:50807"
                     /db_xref="HGNC:HGNC:2720"
                     /db_xref="MIM:605953"
ORIGIN      
        1 mrssasrlss fssrdslwnr mpdqisvsef iaettedyns pttssfttrl hncrntvtll
       61 eealdqdrta lqkvkksvka iynsgqdhvq neenyaqvld kfgsnflsrd npdlgtafvk
      121 fstltkelst llknllqgls hnviftldsl lkgdlkgvkg dlkkpfdkaw kdyetkftki
      181 ekekrehakq hgmirteitg aeiaeemeke rrlfqlqmce ylikvneikt kkgvdllqnl
      241 ikyyhaqcnf fqdglktadk lkqyieklaa dlynikqtqd eekkqltalr dliksslqld
      301 qkedsqsrqg gysmhqlqgn keygsekkgy llkksdgirk vwqrrkcsvk ngiltishat
      361 snrqpaklnl ltcqvkpnae dkksfdlish nrtyhfqaed eqdyvawisv ltnskeealt
      421 mafrgeqsag ensledltka iiedvqrlpg ndiccdcgss eptwlstnlg iltciecsgi
      481 hremgvhisr iqsleldklg tselllaknv gnnsfndime anlpspspkp tpssdmtvrk
      541 eyitakyvdh rfsrktcsts saklnellea iksrdllali qvyaegvelm epllepgqel
      601 getalhlavr tadqtslhlv dflvqncgnl dkqtalgntv lhycsmyskp eclklllrsk
      661 ptvdivnqag etaldiakrl katqcedlls qaksgkfnph vhveyewnlr qeeidesddd
      721 lddkpspikk ersprpqsfc hsssispqdk lalpgfstpr dkqrlsygaf tnqifvstst
      781 dsptspttea pplpprnagk gptgppstlp lstqtssgss tlskkrpppp ppghkrtlsd
      841 ppsplphgpp nkgavpwgnd ggpssssktt nkfeglsqqs stssaktalg prvlpklpqk
      901 valrktdhls ldkatippei fqkssqlael pqkpppgdlp pkptelapkp qigdlppkpg
      961 elppkpqlgd lppkpqlsdl ppkpqmkdlp pkpqlgdlla ksqtgdvspk aqqpsevtlk
     1021 shpldlspnv qsrdaiqkqa sedsndltpt lpetpvplpr kintgknkvr rvktiydcqa
     1081 dnddeltfie geviivtgee dqewwighie gqperkgvfp vsfvhilsd
//
LOCUS       NP_001352513             836 aa            linear   PRI 27-APR-2025
DEFINITION  neuroligin-4, Y-linked isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001352513 XP_011529726
VERSION     NP_001352513.1
DBSOURCE    REFSEQ: accession NM_001365584.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Nguyen,T.A., Wu,K., Pandey,S., Lehr,A.W., Li,Y., Bemben,M.A.,
            Badger,J.D. 2nd, Lauzon,J.L., Wang,T., Zaghloul,K.A., Thurm,A.,
            Jain,M., Lu,W. and Roche,K.W.
  TITLE     A Cluster of Autism-Associated Variants on X-Linked NLGN4X
            Functionally Resemble NLGN4Y
  JOURNAL   Neuron 106 (5), 759-768 (2020)
   PUBMED   32243781
  REMARK    GeneRIF: A Cluster of Autism-Associated Variants on X-Linked NLGN4X
            Functionally Resemble NLGN4Y.
REFERENCE   2  (residues 1 to 836)
  AUTHORS   Bogaert,A.F., Skorska,M.N., Wang,C., Gabrie,J., MacNeil,A.J.,
            Hoffarth,M.R., VanderLaan,D.P., Zucker,K.J. and Blanchard,R.
  TITLE     Male homosexuality and maternal immune responsivity to the Y-linked
            protein NLGN4Y
  JOURNAL   Proc Natl Acad Sci U S A 115 (2), 302-306 (2018)
   PUBMED   29229842
  REMARK    GeneRIF: Results suggest an association between a maternal immune
            response to neuroligin 4 Y-linked (NLGN4Y) and subsequent sexual
            orientation in male offspring.
            Erratum:[Proc Natl Acad Sci U S A. 2022 Aug 23;119(34):e2212767119.
            doi: 10.1073/pnas.2212767119. PMID: 35981140]
REFERENCE   3  (residues 1 to 836)
  AUTHORS   Gong,Y., Wang,L., Chippada-Venkata,U., Dai,X., Oh,W.K. and Zhu,J.
  TITLE     Constructing Bayesian networks by integrating gene expression and
            copy number data identifies NLGN4Y as a novel regulator of prostate
            cancer progression
  JOURNAL   Oncotarget 7 (42), 68688-68707 (2016)
   PUBMED   27626693
  REMARK    GeneRIF: Results suggest that NLGN4Y is an important negative
            regulator in prostate cancer progression.
REFERENCE   4  (residues 1 to 836)
  AUTHORS   Ross,J.L., Tartaglia,N., Merry,D.E., Dalva,M. and Zinn,A.R.
  TITLE     Behavioral phenotypes in males with XYY and possible role of
            increased NLGN4Y expression in autism features
  JOURNAL   Genes Brain Behav 14 (2), 137-144 (2015)
   PUBMED   25558953
  REMARK    GeneRIF: Expression of NLGN4Y, a gene that may be involved in
            synaptic function, is increased in boys with XYY
REFERENCE   5  (residues 1 to 836)
  AUTHORS   Dinamarca,M.C., Weinstein,D., Monasterio,O. and Inestrosa,N.C.
  TITLE     The synaptic protein neuroligin-1 interacts with the amyloid
            beta-peptide. Is there a role in Alzheimer's disease?
  JOURNAL   Biochemistry 50 (38), 8127-8137 (2011)
   PUBMED   21838267
REFERENCE   6  (residues 1 to 836)
  AUTHORS   Yamakawa,H., Oyama,S., Mitsuhashi,H., Sasagawa,N., Uchino,S.,
            Kohsaka,S. and Ishiura,S.
  TITLE     Neuroligins 3 and 4X interact with syntrophin-gamma2, and the
            interactions are affected by autism-related mutations
  JOURNAL   Biochem Biophys Res Commun 355 (1), 41-46 (2007)
   PUBMED   17292328
REFERENCE   7  (residues 1 to 836)
  AUTHORS   Ylisaukko-oja,T., Rehnstrom,K., Auranen,M., Vanhala,R., Alen,R.,
            Kempas,E., Ellonen,P., Turunen,J.A., Makkonen,I., Riikonen,R.,
            Nieminen-von Wendt,T., von Wendt,L., Peltonen,L. and Jarvela,I.
  TITLE     Analysis of four neuroligin genes as candidates for autism
  JOURNAL   Eur J Hum Genet 13 (12), 1285-1292 (2005)
   PUBMED   16077734
  REMARK    GeneRIF: Neuroligin mutations most probably represent rare causes
            of autism; it is unlikely that the allelic variants in any of these
            genes would be major risk factors for autism.
REFERENCE   8  (residues 1 to 836)
  AUTHORS   Skaletsky,H., Kuroda-Kawaguchi,T., Minx,P.J., Cordum,H.S.,
            Hillier,L., Brown,L.G., Repping,S., Pyntikova,T., Ali,J., Bieri,T.,
            Chinwalla,A., Delehaunty,A., Delehaunty,K., Du,H., Fewell,G.,
            Fulton,L., Fulton,R., Graves,T., Hou,S.F., Latrielle,P.,
            Leonard,S., Mardis,E., Maupin,R., McPherson,J., Miner,T., Nash,W.,
            Nguyen,C., Ozersky,P., Pepin,K., Rock,S., Rohlfing,T., Scott,K.,
            Schultz,B., Strong,C., Tin-Wollam,A., Yang,S.P., Waterston,R.H.,
            Wilson,R.K., Rozen,S. and Page,D.C.
  TITLE     The male-specific region of the human Y chromosome is a mosaic of
            discrete sequence classes
  JOURNAL   Nature 423 (6942), 825-837 (2003)
   PUBMED   12815422
REFERENCE   9  (residues 1 to 836)
  AUTHORS   Jamain,S., Quach,H., Betancur,C., Rastam,M., Colineaux,C.,
            Gillberg,I.C., Soderstrom,H., Giros,B., Leboyer,M., Gillberg,C. and
            Bourgeron,T.
  CONSRTM   Paris Autism Research International Sibpair Study
  TITLE     Mutations of the X-linked genes encoding neuroligins NLGN3 and
            NLGN4 are associated with autism
  JOURNAL   Nat Genet 34 (1), 27-29 (2003)
   PUBMED   12669065
REFERENCE   10 (residues 1 to 836)
  AUTHORS   Cantallops,I. and Cline,H.T.
  TITLE     Synapse formation: if it looks like a duck and quacks like a duck
            ...
  JOURNAL   Curr Biol 10 (17), R620-R623 (2000)
   PUBMED   10996085
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010726.4, AC010979.3,
            AC010879.2 and AC011903.4.
            
            On Sep 5, 2018 this sequence version replaced XP_011529726.1.
            
            Summary: This gene encodes a type I membrane protein that belongs
            to the family of neuroligins, which are cell adhesion molecules
            present at the postsynaptic side of the synapse, and may be
            essential for the formation of functional synapses. Alternatively
            spliced transcript variants have been found for this gene.[provided
            by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.123071.1,
                                           SRR1803616.224540.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147975, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..836
                     /product="neuroligin-4, Y-linked isoform 4 precursor"
                     /note="alternative HNL4Y"
                     /calculated_mol_wt=89576
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4646
     Region          44..610
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            order(194..196,273..275,278,419,425..426,464,510,513)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(274,395,509)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     CDS             1..836
                     /gene="NLGN4Y"
                     /gene_synonym="HNL4Y"
                     /coded_by="NM_001365584.1:520..3030"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 6"
                     /db_xref="CCDS:CCDS94714.1"
                     /db_xref="GeneID:22829"
                     /db_xref="HGNC:HGNC:15529"
                     /db_xref="MIM:400028"
ORIGIN      
        1 mlrpqgllwl pllftsvcvm lnsnvllwit alaikftlid sqaqypvvnt nygkiqglrt
       61 plpseilgpv eqylgvpyas pptgerrfqp pespsswtgi rnatqfsavc pqhlderfll
      121 hdmlpiwftt sldtlmtyvq dqnedclyln iyvpmedgtn ikrnaddits ndhgedkdih
      181 eqnskkpvmv yihggsymeg tgnmidgsil asygnvivit inyrlgilgf lstgdqaakg
      241 nyglldqiqa lrwieenvga fggdpkrvti fgsgagascv slltlshyse glfqkaiiqs
      301 gtalsswavn yqpakytril adkvgcnmld ttdmveclkn knykeliqqt itpatyhiaf
      361 gpvidgdvip ddpqilmeqg eflnydimlg vnqgeglkfv dgivdnedgv tpndfdfsvs
      421 nfvdnlygyp egkdtlreti kfmytdwadk enpetrrktl valftdhqwv apavatadlh
      481 aqygsptyfy afyhhcqsem kpswadsahg devpyvfgip migptelfsc nfskndvmls
      541 avvmtywtnf aktgdpnqpv pqdtkfihtk pnrfeevaws kynpkdqlyl higlkprvrd
      601 hyratkvafw lelvphlhnl neifqyvstt tkvpppdmts fpygtrrspa kiwpttkrpa
      661 itpannpkhs kdphktgped ttvlietkrd ystelsvtia vgasllflni lafaalyykk
      721 dkrrhethrh pspqrnttnd ithiqneeim slqmkqlehd heceslqahd tlrltcppdy
      781 tltlrrspdd ipfmtpntit mipntlmgmq plhtfktfsg gqnstnlphg hsttrv
//
LOCUS       NP_001347501             683 aa            linear   ROD 27-APR-2025
DEFINITION  synaptic vesicle glycoprotein 2B [Mus musculus].
ACCESSION   NP_001347501 XP_006541123
VERSION     NP_001347501.1
DBSOURCE    REFSEQ: accession NM_001360572.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Paulussen,I., Beckert,H., Musial,T.F., Gschossmann,L.J., Wolf,J.,
            Schmitt,M., Clasadonte,J., Mairet-Coello,G., Wolff,C., Schoch,S.
            and Dietrich,D.
  TITLE     SV2B defines a subpopulation of synaptic vesicles
  JOURNAL   J Mol Cell Biol 15 (9) (2024)
   PUBMED   37682518
  REMARK    GeneRIF: SV2B defines a subpopulation of synaptic vesicles.
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Bolz,S., Kaempf,N., Puchkov,D., Krauss,M., Russo,G., Soykan,T.,
            Schmied,C., Lehmann,M., Muller,R., Schultz,C., Perrais,D.,
            Maritzen,T. and Haucke,V.
  TITLE     Synaptotagmin 1-triggered lipid signaling facilitates coupling of
            exo- and endocytosis
  JOURNAL   Neuron 111 (23), 3765-3774 (2023)
   PUBMED   37738980
  REMARK    Erratum:[Neuron. 2023 Dec 6;111(23):3900. doi:
            10.1016/j.neuron.2023.11.003. PMID: 38061332]
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Vana,N.S., van Loo,K.M.J., van Waardenberg,A.J., Tiessen,M.,
            Cases-Cunillera,S., Sun,W., Quatraccioni,A., Schoch,S. and
            Dietrich,D.
  TITLE     Early cortical oligodendrocyte precursor cells are
            transcriptionally distinct and lack synaptic connections
  JOURNAL   Glia 71 (9), 2210-2233 (2023)
   PUBMED   37226895
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Lopez-Tello,J. and Sferruzzi-Perri,A.N.
  TITLE     Characterization of placental endocrine function and fetal brain
            development in a mouse model of small for gestational age
  JOURNAL   Front Endocrinol (Lausanne) 14, 1116770 (2023)
   PUBMED   36843585
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Noakes,P.G., Chin,D., Kim,S.S., Liang,S. and Phillips,W.D.
  TITLE     Expression and localisation of dynamin and syntaxin during neural
            development and neuromuscular synapse formation
  JOURNAL   J Comp Neurol 410 (4), 531-540 (1999)
   PUBMED   10398046
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Serpinskaya,A.S., Feng,G., Sanes,J.R. and Craig,A.M.
  TITLE     Synapse formation by hippocampal neurons from agrin-deficient mice
  JOURNAL   Dev Biol 205 (1), 65-78 (1999)
   PUBMED   9882498
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Rich,K.A., Zhan,Y. and Blanks,J.C.
  TITLE     Migration and synaptogenesis of cone photoreceptors in the
            developing mouse retina
  JOURNAL   J Comp Neurol 388 (1), 47-63 (1997)
   PUBMED   9364238
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Gautam,M., Noakes,P.G., Moscoso,L., Rupp,F., Scheller,R.H.,
            Merlie,J.P. and Sanes,J.R.
  TITLE     Defective neuromuscular synaptogenesis in agrin-deficient mutant
            mice
  JOURNAL   Cell 85 (4), 525-535 (1996)
   PUBMED   8653788
REFERENCE   10 (residues 1 to 683)
  AUTHORS   Ahnert-Hilger,G., Kutay,U., Chahoud,I., Rapoport,T. and
            Wiedenmann,B.
  TITLE     Synaptobrevin is essential for secretion but not for the
            development of synaptic processes
  JOURNAL   Eur J Cell Biol 70 (1), 1-11 (1996)
   PUBMED   8738414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC127355.4, AC116898.11 and AC113471.9.
            
            On Feb 7, 2018 this sequence version replaced XP_006541123.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 3. All seven variants encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR9219382.114749.1,
                                           SRR1660811.244439.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 43.62 cM"
     Protein         1..683
                     /product="synaptic vesicle glycoprotein 2B"
                     /note="synaptic vesicle protein 2B; synaptic vesicle
                     glycoprotein 2 b"
                     /calculated_mol_wt=77327
     Region          1..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Region          8..683
                     /region_name="synapt_SV2"
                     /note="synaptic vesicle protein SV2; TIGR01299"
                     /db_xref="CDD:130366"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            111..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            183..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            206..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            391..411
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18034455; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            441
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            491
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            516
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            536..556
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            566..586
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            593..613
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            627..649
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            654..672
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     CDS             1..683
                     /gene="Sv2b"
                     /gene_synonym="A830038F04Rik; mKIAA0735"
                     /coded_by="NM_001360572.1:599..2650"
                     /db_xref="CCDS:CCDS21368.1"
                     /db_xref="GeneID:64176"
                     /db_xref="MGI:MGI:1927338"
ORIGIN      
        1 mddyryrdny egyapsdgyy rsneqnqeed aqsdvteghd eedeiyegey qgiphpddvk
       61 skqtkmapsr adglggqadl maermedeee lahqyetiid ecghgrfqwt lffvlglalm
      121 adgveifvvs falpsaekdm clssskkgml glivylgmma gafilgglad klgrkkvlsm
      181 slainasfas lssfvqgyga flfcrlisgi giggslpivf ayfseflsre krgehlswlg
      241 ifwmtggiya samawsiiph ygwgfsmgtn yhfhswrvfv ivcalpatvs mvalkfmpes
      301 prfllemgkh deawmilkqv hdtnmrakgt pekvftvshi ktpkqmdefi eiqsstgtwy
      361 qrwlvrfmti fkqvwdnaly cvmgpyrmnt lilavvwftm alsyygltvw fpdmiryfqd
      421 eeykskmkvf fgehvhgati nftmenqihq hgklvndkfi kmyfkhvlfe dtffdkcyfe
      481 dvtstdtyfk nctiesttfy ntdlykhkfi ncrfinstfl eqkegchmdf eedndfliyl
      541 vsflgslsvl pgniisallm drigrlkmig gsmlisavcc fflffgnses amigwqclfc
      601 gtsiaawnal dvitvelypt nqratafgil nglckfgail gntifasfvg itkvvpilla
      661 aaslvgggli alrlpetreq vlm
//
LOCUS       NP_076036                358 aa            linear   ROD 27-APR-2025
DEFINITION  INO80 complex subunit B [Mus musculus].
ACCESSION   NP_076036
VERSION     NP_076036.2
DBSOURCE    REFSEQ: accession NM_023547.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Yang,G., Xin,Q., Feng,I., Wu,D. and Dean,J.
  TITLE     Germ cell-specific eIF4E1b regulates maternal mRNA translation to
            ensure zygotic genome activation
  JOURNAL   Genes Dev 37 (9-10), 418-431 (2023)
   PUBMED   37257918
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Min,J.N., Tian,Y., Xiao,Y., Wu,L., Li,L. and Chang,S.
  TITLE     The mINO80 chromatin remodeling complex is required for efficient
            telomere replication and maintenance of genome stability
  JOURNAL   Cell Res 23 (12), 1396-1413 (2013)
   PUBMED   23979016
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Miyako,K., Cobb,L.J., Francis,M., Huang,A., Peng,B., Pintar,J.E.,
            Ariga,H. and Cohen,P.
  TITLE     PAPA-1 Is a nuclear binding partner of IGFBP-2 and modulates its
            growth-promoting actions
  JOURNAL   Mol Endocrinol 23 (2), 169-175 (2009)
   PUBMED   19095771
  REMARK    GeneRIF: Results suggest that the growth-promoting role of IGFBP-2
            in prostate cancer is inhibited by its intracellular interaction
            with PAPA-1.
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Maita,H., Kitaura,H., Ariga,H. and Iguchi-Ariga,S.M.
  TITLE     CIR, a corepressor of CBF1, binds to PAP-1 and effects alternative
            splicing
  JOURNAL   Exp Cell Res 303 (2), 375-387 (2005)
   PUBMED   15652350
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Kuroda,T.S., Maita,H., Tabata,T., Taira,T., Kitaura,H., Ariga,H.
            and Iguchi-Ariga,S.M.
  TITLE     A novel nucleolar protein, PAPA-1, induces growth arrest as a
            result of cell cycle arrest at the G1 phase
  JOURNAL   Gene 340 (1), 83-98 (2004)
   PUBMED   15556297
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104324.21.
            
            On Feb 16, 2019 this sequence version replaced NP_076036.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC058788.1, AK010946.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164139, SAMN01164140
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 35.94 cM"
     Protein         1..358
                     /product="INO80 complex subunit B"
                     /note="high mobility group AT-hook 1-like 4; PAP-1 binding
                     protein; PAPA-1; PAP-1-associated protein 1; zinc finger
                     HIT domain-containing protein 4; zinc finger, HIT type 4"
                     /calculated_mol_wt=38710
     Region          211..289
                     /region_name="PAPA-1"
                     /note="PAPA-1-like conserved region; pfam04795"
                     /db_xref="CDD:461431"
     Region          309..341
                     /region_name="zf-HIT_IN80B"
                     /note="zinc finger HIT (zf-HIT) found in INO80 complex
                     subunit B (INO80B) and similar proteins; cd23021"
                     /db_xref="CDD:467793"
     Site            order(316,332,336)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:467793"
     Site            order(320..326,332..334,337..338)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467793"
     CDS             1..358
                     /gene="Ino80b"
                     /gene_synonym="2510009I23Rik; HMG1YL4; Hmga1l4; Papa1;
                     Znhit4"
                     /coded_by="NM_023547.2:52..1128"
                     /db_xref="CCDS:CCDS39530.1"
                     /db_xref="GeneID:70020"
                     /db_xref="MGI:MGI:1917270"
ORIGIN      
        1 msklwrrgst sgameapepg etlelslaga hghgvhkkkh kkhkkkhkkk hhqeeeagpt
       61 lqtpakpqlk lkiklggqvl gtksvptftv ipegprspsp lmvvdneeep megvpleqyr
      121 awldedsnls psplrdlpgd legqeeeeeq rwldalekge lddngdlkke inerlltarq
      181 rallqkarsq psptlplpvg ggcpapalte emllkreera rkrrlqaarr aeehknqtie
      241 rltktaapsg rggrgaarge rrggraaapa papmvrycsg aqgstlsfpp gvptptavaq
      301 rpapsgpapr csvpgcphpr ryacsrtgqa lcslqcyrin lqlrlggpeg pgspllat
//
LOCUS       NP_005699                555 aa            linear   PRI 27-APR-2025
DEFINITION  glypican-6 precursor [Homo sapiens].
ACCESSION   NP_005699
VERSION     NP_005699.1
DBSOURCE    REFSEQ: accession NM_005708.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Crenshaw,M.M., Meyers,M.L., Brown,K., Slegesky,V., Duis,J.,
            Elias,E.R., Saenz,M., Shi,W., Filmus,J. and Meeks,N.J.L.
  TITLE     Five siblings expand the spectrum of GPC6-related skeletal
            dysplasia
  JOURNAL   Am J Med Genet A 191 (10), 2571-2577 (2023)
   PUBMED   37353964
  REMARK    GeneRIF: Five siblings expand the spectrum of GPC6-related skeletal
            dysplasia.
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Wang,F., Li,Y., Li,Z., Zou,Z., Lu,Y., Xu,C., Zhao,Z., Wang,H.,
            Wang,Y., Guo,S., Jin,L., Wang,J., Li,Q., Jiang,G., Xia,F., Shen,B.
            and Wu,J.
  TITLE     Prognostic value of GPC5 polymorphism rs2352028 and clinical
            characteristics in Chinese lung cancer patients
  JOURNAL   Future Oncol 18 (28), 3165-3177 (2022)
   PUBMED   36165234
  REMARK    GeneRIF: Prognostic value of GPC5 polymorphism rs2352028 and
            clinical characteristics in Chinese lung cancer patients.
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Lehmkuhl,E.M., Loganathan,S., Alsop,E., Blythe,A.D., Kovalik,T.,
            Mortimore,N.P., Barrameda,D., Kueth,C., Eck,R.J., Siddegowda,B.B.,
            Joardar,A., Ball,H., Macias,M.E., Bowser,R., Van Keuren-Jensen,K.
            and Zarnescu,D.C.
  TITLE     TDP-43 proteinopathy alters the ribosome association of multiple
            mRNAs including the glypican Dally-like protein (Dlp)/GPC6
  JOURNAL   Acta Neuropathol Commun 9 (1), 52 (2021)
   PUBMED   33762006
  REMARK    GeneRIF: TDP-43 proteinopathy alters the ribosome association of
            multiple mRNAs including the glypican Dally-like protein
            (Dlp)/GPC6.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Levy,D., Larson,M.G., Benjamin,E.J., Newton-Cheh,C., Wang,T.J.,
            Hwang,S.J., Vasan,R.S. and Mitchell,G.F.
  TITLE     Framingham Heart Study 100K Project: genome-wide associations for
            blood pressure and arterial stiffness
  JOURNAL   BMC Med Genet 8 Suppl 1 (Suppl 1), S3 (2007)
   PUBMED   17903302
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 555)
  AUTHORS   Veugelers,M., De Cat,B., Ceulemans,H., Bruystens,A.M., Coomans,C.,
            Durr,J., Vermeesch,J., Marynen,P. and David,G.
  TITLE     Glypican-6, a new member of the glypican family of cell surface
            heparan sulfate proteoglycans
  JOURNAL   J Biol Chem 274 (38), 26968-26977 (1999)
   PUBMED   10480909
REFERENCE   9  (residues 1 to 555)
  AUTHORS   Paine-Saunders,S., Viviano,B.L. and Saunders,S.
  TITLE     GPC6, a novel member of the glypican gene family, encodes a product
            structurally related to GPC4 and is colocalized with GPC5 on human
            chromosome 13
  JOURNAL   Genomics 57 (3), 455-458 (1999)
   PUBMED   10329016
REFERENCE   10 (residues 1 to 555)
  AUTHORS   Watanabe,K., Yamada,H. and Yamaguchi,Y.
  TITLE     K-glypican: a novel GPI-anchored heparan sulfate proteoglycan that
            is highly expressed in developing brain and kidney
  JOURNAL   J Cell Biol 130 (5), 1207-1218 (1995)
   PUBMED   7657705
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354811.13, DA267422.1,
            AF111178.2, AY358462.1, AK290144.1, BX640888.1, AL137144.14 and
            BQ009005.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The glypicans comprise a family of
            glycosylphosphatidylinositol-anchored heparan sulfate
            proteoglycans, and they have been implicated in the control of cell
            growth and cell division. The glypican encoded by this gene is a
            putative cell surface coreceptor for growth factors, extracellular
            matrix proteins, proteases and anti-proteases. Mutations in this
            gene are associated with omodysplasia 1. [provided by RefSeq, Nov
            2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no quality transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.111997.1,
                                           SRR1803613.235929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377047.9/ ENSP00000366246.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q31.3-q32.1"
     Protein         1..555
                     /product="glypican-6 precursor"
                     /note="glypican proteoglycan 6"
                     /calculated_mol_wt=60451
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2303
     Region          22..548
                     /region_name="Glypican"
                     /note="pfam01153"
                     /db_xref="CDD:460084"
     mat_peptide     24..529
                     /product="Glypican-6. /id=PRO_0000012323"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y625.1)"
                     /calculated_mol_wt=57586
     Region          348..376
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y625.1)"
     Region          480..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y625.1)"
     CDS             1..555
                     /gene="GPC6"
                     /gene_synonym="OMIMD1"
                     /coded_by="NM_005708.5:651..2318"
                     /db_xref="CCDS:CCDS9469.1"
                     /db_xref="GeneID:10082"
                     /db_xref="HGNC:HGNC:4454"
                     /db_xref="MIM:604404"
ORIGIN      
        1 mpswigavil pllglllslp agadvkarsc gevrqaygak gfsladipyq eiagehlric
       61 pqeytcctte medklsqqsk lefenlveet shfvrttfvs rhkkfdeffr ellenaeksl
      121 ndmfvrtygm lymqnsevfq dlftelkryy tggnvnleem lndfwarlle rmfqlinpqy
      181 hfsedylecv skytdqlkpf gdvprklkiq vtrafiaart fvqgltvgre vanrvskvsp
      241 tpgciralmk mlycpycrgl ptvrpcnnyc lnvmkgclan qadldtewnl fidamllvae
      301 rlegpfnies vmdpidvkis eaimnmqens mqvsakvfqg cgqpkpapal rsarsapenf
      361 ntrfrpynpe erpttaagts ldrlvtdike klklskkvws alpytickde svtagtsnee
      421 ecwnghskar ylpeimndgl tnqinnpevd vditrpdtfi rqqimalrvm tnklknayng
      481 ndvnfqdtsd essgsgsgsg cmddvcptef efvtteapav dpdrrevdss aaqrghslls
      541 wsltcivlal qrlcr
//
LOCUS       NP_006542                 90 aa            linear   PRI 27-APR-2025
DEFINITION  secretoglobin family 1D member 2 precursor [Homo sapiens].
ACCESSION   NP_006542
VERSION     NP_006542.1
DBSOURCE    REFSEQ: accession NM_006551.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Strausz,S., Abner,E., Blacker,G., Galloway,S., Hansen,P., Feng,Q.,
            Lee,B.T., Jones,S.E., Haapaniemi,H., Raak,S., Nahass,G.R.,
            Sanders,E., Soodla,P., Vosa,U., Esko,T., Sinnott-Armstrong,N.,
            Weissman,I.L., Daly,M., Aivelo,T., Tal,M.C. and Ollila,H.M.
  CONSRTM   FinnGen; Estonian Genome Centre; Estonian Biobank Research Team
  TITLE     SCGB1D2 inhibits growth of Borrelia burgdorferi and affects
            susceptibility to Lyme disease
  JOURNAL   Nat Commun 15 (1), 2041 (2024)
   PUBMED   38503741
  REMARK    GeneRIF: SCGB1D2 inhibits growth of Borrelia burgdorferi and
            affects susceptibility to Lyme disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Taniuchi,K., Okabayashi,T., Sakaguchi,M. and Iwata,J.
  TITLE     [Measurement of PODXL and SCGB1D2 for detecting intraductal
            papillary mucinous neoplasm]
  JOURNAL   Nihon Shokakibyo Gakkai Zasshi 118 (3), 235-244 (2021)
   PUBMED   33692257
  REMARK    GeneRIF: [Measurement of PODXL and SCGB1D2 for detecting
            intraductal papillary mucinous neoplasm].
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Fischer,K., von Brunneck,A.C., Hornung,D., Denkert,C., Ufer,C.,
            Schiebel,H., Kuhn,H. and Borchert,A.
  TITLE     Differential expression of secretoglobins in normal ovary and in
            ovarian carcinoma--overexpression of mammaglobin-1 is linked to
            tumor progression
  JOURNAL   Arch Biochem Biophys 547, 27-36 (2014)
   PUBMED   24603286
  REMARK    GeneRIF: The data indicate that MGB1, MGB2 and LIPB mRNAs are
            expressed at low levels in human tissues but basal expression is
            upregulated in ovarian cancer.
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Bignotti,E., Tassi,R.A., Calza,S., Ravaggi,A., Rossi,E.,
            Donzelli,C., Todeschini,P., Romani,C., Bandiera,E., Zanotti,L.,
            Carnazza,M., Quadraro,F., Tognon,G., Sartori,E., Pecorelli,S.,
            Roque,D.M. and Santin,A.D.
  TITLE     Secretoglobin expression in ovarian carcinoma: lipophilin B gene
            upregulation as an independent marker of better prognosis
  JOURNAL   J Transl Med 11, 162 (2013)
   PUBMED   23819652
  REMARK    GeneRIF: lipophilin B gene overexpression correlates with a less
            aggressive tumor phenotype and represents a novel ovarian carcinoma
            prognostic factor
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 90)
  AUTHORS   Jackson,B.C., Thompson,D.C., Wright,M.W., McAndrews,M., Bernard,A.,
            Nebert,D.W. and Vasiliou,V.
  TITLE     Update of the human secretoglobin (SCGB) gene superfamily and an
            example of 'evolutionary bloom' of androgen-binding protein genes
            within the mouse Scgb gene superfamily
  JOURNAL   Hum Genomics 5 (6), 691-702 (2011)
   PUBMED   22155607
  REMARK    Review article
REFERENCE   6  (residues 1 to 90)
  AUTHORS   Sjodin,A., Guo,D., Lund-Johansen,M., Krossnes,B.K., Lilleng,P.,
            Henriksson,R. and Hedman,H.
  TITLE     Secretoglobins in the human pituitary: high expression of
            lipophilin B and its down-regulation in pituitary adenomas
  JOURNAL   Acta Neuropathol 109 (4), 381-386 (2005)
   PUBMED   15668787
  REMARK    GeneRIF: The present report demonstrates, for the first time,
            lipophilin B expression in the pituitary and its apparent
            down-regulation in pituitary adenomas.
REFERENCE   7  (residues 1 to 90)
  AUTHORS   Carter,D., Dillon,D.C., Reynolds,L.D., Retter,M.W., Fanger,G.,
            Molesh,D.A., Sleath,P.R., McNeill,P.D., Vedvick,T.S., Reed,S.G.,
            Persing,D.H. and Houghton,R.L.
  TITLE     Serum antibodies to lipophilin B detected in late stage breast
            cancer patients
  JOURNAL   Clin Cancer Res 9 (2), 749-754 (2003)
   PUBMED   12576445
  REMARK    GeneRIF: Serum antibodies to this protein are detected in late
            stage breast cancer patients.
REFERENCE   8  (residues 1 to 90)
  AUTHORS   Carter,D., Douglass,J.F., Cornellison,C.D., Retter,M.W.,
            Johnson,J.C., Bennington,A.A., Fleming,T.P., Reed,S.G.,
            Houghton,R.L., Diamond,D.L. and Vedvick,T.S.
  TITLE     Purification and characterization of the mammaglobin/lipophilin B
            complex, a promising diagnostic marker for breast cancer
  JOURNAL   Biochemistry 41 (21), 6714-6722 (2002)
   PUBMED   12022875
REFERENCE   9  (residues 1 to 90)
  AUTHORS   Zhao,C., Nguyen,T., Yusifov,T., Glasgow,B.J. and Lehrer,R.I.
  TITLE     Lipophilins: human peptides homologous to rat prostatein
  JOURNAL   Biochem Biophys Res Commun 256 (1), 147-155 (1999)
   PUBMED   10066439
REFERENCE   10 (residues 1 to 90)
  AUTHORS   Lehrer,R.I., Xu,G., Abduragimov,A., Dinh,N.N., Qu,X.D., Martin,D.
            and Glasgow,B.J.
  TITLE     Lipophilin, a novel heterodimeric protein of human tears
  JOURNAL   FEBS Lett 432 (3), 163-167 (1998)
   PUBMED   9720917
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003306.2, AL708956.1 and
            AJ224172.1.
            
            Summary: The protein encoded by this gene is a member of the
            lipophilin subfamily, part of the uteroglobin superfamily, and is
            an ortholog of prostatein, the major secretory glycoprotein of the
            rat ventral prostate gland. Lipophilin gene products are widely
            expressed in normal tissues, especially in endocrine-responsive
            organs. Assuming that human lipophilins are the functional
            counterparts of prostatein, they may be transcriptionally regulated
            by steroid hormones, with the ability to bind androgens, other
            steroids and possibly bind and concentrate estramustine, a
            chemotherapeutic agent widely used for prostate cancer. Although
            the gene has been reported to be on chromosome 10, this sequence
            appears to be from a cluster of genes on chromosome 11 that
            includes mammaglobin 2. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL708956.1, BP314377.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000244926.4/ ENSP00000244926.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..90
                     /product="secretoglobin family 1D member 2 precursor"
                     /note="prostatein-like lipophilin B; lipophilin-B"
                     /calculated_mol_wt=7672
     Region          1..87
                     /region_name="Uteroglobin"
                     /note="Uteroglobin family; pfam01099"
                     /db_xref="CDD:460063"
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2271
     mat_peptide     22..90
                     /product="secretoglobin family 1D member 2"
                     /calculated_mol_wt=7672
     Site            order(26..27,30,42,46,49,54..59,61..62,65,73,75..77,
                     79..80,83)
                     /site_type="other"
                     /note="Dimer interface [polypeptide binding]"
                     /db_xref="CDD:238346"
     Site            order(27,34,42,59,62,77,80..81)
                     /site_type="other"
                     /note="Hydrophobic pocket - steroid binding site [chemical
                     binding]"
                     /db_xref="CDD:238346"
     CDS             1..90
                     /gene="SCGB1D2"
                     /gene_synonym="LIPB; LPHB; LPNB"
                     /coded_by="NM_006551.4:70..342"
                     /db_xref="CCDS:CCDS8017.1"
                     /db_xref="GeneID:10647"
                     /db_xref="HGNC:HGNC:18396"
                     /db_xref="MIM:615061"
ORIGIN      
        1 mklsvclllv tlalccyqan aefcpalvse lldfffisep lfklslakfd appeavaakl
       61 gvkrctdqms lqkrsliaev lvkilkkcsv
//
LOCUS       NP_001356317             386 aa            linear   PRI 27-APR-2025
DEFINITION  nucleosome assembly protein 1-like 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001356317
VERSION     NP_001356317.1
DBSOURCE    REFSEQ: accession NM_001369388.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Tan,L., Cheng,W., Liu,F., Wang,D.O., Wu,L., Cao,N. and Wang,J.
  TITLE     Positive natural selection of N6-methyladenosine on the RNAs of
            processed pseudogenes
  JOURNAL   Genome Biol 22 (1), 180 (2021)
   PUBMED   34120636
  REMARK    GeneRIF: Positive natural selection of N6-methyladenosine on the
            RNAs of processed pseudogenes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Mizuhashi,S., Fukushima,S., Ishibashi,T., Kuriyama,H., Kimura,T.,
            Kanemaru,H., Kajihara,I., Makino,K., Miyashita,A., Aoi,J., Kita,K.
            and Ihn,H.
  TITLE     Nucleosome assembly protein 1-like 4, a new therapeutic target for
            proliferation and invasion of melanoma cells
  JOURNAL   J Dermatol Sci 102 (1), 16-24 (2021)
   PUBMED   33583643
  REMARK    GeneRIF: Nucleosome assembly protein 1-like 4, a new therapeutic
            target for proliferation and invasion of melanoma cells.
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Tanaka,T., Hozumi,Y., Martelli,A.M., Iino,M. and Goto,K.
  TITLE     Nucleosome assembly proteins NAP1L1 and NAP1L4 modulate p53
            acetylation to regulate cell fate
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1866 (12), 118560 (2019)
   PUBMED   31634504
  REMARK    GeneRIF: The NAP1L4 regulates cell fate by controlling the
            expression of p53-responsive proarrest and proapoptotic genes
            through selective modulation of p53 acetylation at specific sites
            during normal homeostasis and in stress-induced responses.
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Tanaka,T., Hozumi,Y., Iino,M. and Goto,K.
  TITLE     NAP1L1 regulates NF-kappaB signaling pathway acting on
            anti-apoptotic Mcl-1 gene expression
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1864 (10), 1759-1768 (2017)
   PUBMED   28687276
  REMARK    GeneRIF: knockdown of NAP1L1 suppresses IkappaBalpha degradation
            and nuclear transport of p65 subunit after treatment with TNF-a
            stimulation, leading to attenuation of the NF-kappaB
            transcriptional activity, whereas NAP1L4 knockdown remains
            silent.results of this study suggest that NAP1L1 downregulation
            renders the cell vulnerable to apoptotic cell death through
            attenuation of NF-kappaB transcriptional activity on the
            anti-apop...
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Ruiz,M.T., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2 is part of multi-protein complexes in HeLa cells
  JOURNAL   J Cell Biochem 93 (2), 398-408 (2004)
   PUBMED   15368365
  REMARK    GeneRIF: NAP-2 is in complex(es) with other proteins, which are
            distinct from histones
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Shikama,N., Chan,H.M., Krstic-Demonacos,M., Smith,L., Lee,C.W.,
            Cairns,W. and La Thangue,N.B.
  TITLE     Functional interaction between nucleosome assembly proteins and
            p300/CREB-binding protein family coactivators
  JOURNAL   Mol Cell Biol 20 (23), 8933-8943 (2000)
   PUBMED   11073993
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Pelletier,J., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2: histone chaperone function and phosphorylation state through
            the cell cycle
  JOURNAL   J Mol Biol 298 (2), 225-238 (2000)
   PUBMED   10764593
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Munroe,D., Prawitt,D., Chu,L.L., Bric,E., Kim,J.,
            Reid,L.H., Davies,C., Nakagama,H., Loebbert,R., Winterpacht,A.,
            Petruzzi,M.J., Higgins,M.J., Nowak,N., Evans,G., Shows,T.,
            Weissman,B.E., Zabel,B., Housman,D.E. and Pelletier,J.
  TITLE     Functional characterization of human nucleosome assembly protein-2
            (NAP1L4) suggests a role as a histone chaperone
  JOURNAL   Genomics 44 (3), 253-265 (1997)
   PUBMED   9325046
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Hu,R.J., Lee,M.P., Johnson,L.A. and Feinberg,A.P.
  TITLE     A novel human homologue of yeast nucleosome assembly protein, 65 kb
            centromeric to the p57KIP2 gene, is biallelically expressed in
            fetal and adult tissues
  JOURNAL   Hum Mol Genet 5 (11), 1743-1748 (1996)
   PUBMED   8923002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC131971.9.
            
            Summary: This gene encodes a member of the nucleosome assembly
            protein (NAP) family which can interact with both core and linker
            histones. It can shuttle between the cytoplasm and nucleus,
            suggesting a role as a histone chaperone. This gene is one of
            several located near the imprinted gene domain of 11p15.5, an
            important tumor-suppressor gene region. Alterations in this region
            have been associated with the Beckwith-Wiedemann syndrome, Wilms
            tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung,
            ovarian, and breast cancer. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.96460.1,
                                           DRR138514.90366.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..386
                     /product="nucleosome assembly protein 1-like 4 isoform 2"
                     /note="nucleosome assembly protein 2; nucleosome assembly
                     protein 1-like 4b; NAP-2"
                     /calculated_mol_wt=43948
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          65..338
                     /region_name="NAP"
                     /note="Nucleosome assembly protein (NAP); pfam00956"
                     /db_xref="CDD:460010"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P28656; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          116..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          265..271
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     CDS             1..386
                     /gene="NAP1L4"
                     /gene_synonym="hNAP2; NAP1L4b; NAP2; NAP2L"
                     /coded_by="NM_001369388.1:356..1516"
                     /note="isoform 2 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS91410.1"
                     /db_xref="GeneID:4676"
                     /db_xref="HGNC:HGNC:7640"
                     /db_xref="MIM:601651"
ORIGIN      
        1 madhsfsdgv psdsveaakn asntekltdq vmqnprvlaa lqerldnvph tpssyietlp
       61 kavkrrinal kqlqvrcahi eakfyeevhd lerkyaalyq plfdkrrefi tgdveptdae
      121 sewhseneee eklagdmksk vvvtekaaat aeepdpkgip efwftifrnv dmlselvqey
      181 depilkhlqd ikvkfsdpgq pmsfvlefhf epndyftnsv ltktykmkse pdkadpfsfe
      241 gpeivdcdgc tidwkkgknv tvktikkkqk hkgrgtvrti tkqvpnesff nffnplkasg
      301 dgesldedse ftlasdfeig hffrerivpr avlyftgeai edddnfeege egeeeelegd
      361 eegededdae inpkkepsqp aeckqq
//
LOCUS       NP_001275576             409 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 286A isoform 5 [Homo sapiens].
ACCESSION   NP_001275576
VERSION     NP_001275576.1
DBSOURCE    REFSEQ: accession NM_001288647.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Murakami,T., Sun,Z.S., Lee,C.C. and Lupski,J.R.
  TITLE     Isolation of novel genes from the CMT1A duplication/HNPP deletion
            critical region in 17p11.2-p12
  JOURNAL   Genomics 39 (1), 99-103 (1997)
   PUBMED   9027492
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005324.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2145245 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..409
                     /product="zinc finger protein 286A isoform 5"
                     /note="zinc finger protein ZNF286"
                     /calculated_mol_wt=47341
     Region          <110..245
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          133..153
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          161..181
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          188..208
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          216..236
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <240..395
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          244..264
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          272..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(277,279,281,283..284,287..288,291,305,307,311..312,
                     315..316,319,333,335,337,339..340,343..344,347)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          356..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          384..404
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..409
                     /gene="ZNF286A"
                     /gene_synonym="ZNF286"
                     /coded_by="NM_001288647.2:502..1731"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:57335"
                     /db_xref="HGNC:HGNC:13501"
ORIGIN      
        1 metrpqskds tsvqdfskae sckvaiidrl trnsvydsnl eaalecenwl enqqgnqerh
       61 lremfthmns lseetdhkhd vywksfnqks vlitedrvpk gsyafhtlek slkqksnlmk
      121 kqrtykekkp hkcndcgelf tyhsvlirhq rvhtgekpyt cnecgksfsh ranltkhqrt
      181 htrilfecse ckktftesss lathqrihvg erpyecnecg kgfnrsthlv qhqlihtgvk
      241 pyecnecdka fihssalikh qrthtgekpy kcqecgkafs hcssltkhqr vhtgekpyec
      301 secgktfsqs thlvqhqrih tgekpyecne cgktfsrssn fakhqrihig kkpykcsecg
      361 kafihssali qhqrthtgek pfrcnecgks fkcssslirh qrvhteeqp
//
LOCUS       NP_003115                261 aa            linear   PRI 27-APR-2025
DEFINITION  sepiapterin reductase [Homo sapiens].
ACCESSION   NP_003115
VERSION     NP_003115.1
DBSOURCE    REFSEQ: accession NM_003124.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Himmelreich,N., Blau,N. and Thony,B.
  TITLE     Molecular and metabolic bases of tetrahydrobiopterin (BH4)
            deficiencies
  JOURNAL   Mol Genet Metab 133 (2), 123-136 (2021)
   PUBMED   33903016
  REMARK    GeneRIF: Molecular and metabolic bases of tetrahydrobiopterin (BH4)
            deficiencies.
            Review article
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Zahra,C., Tabone,C., Camilleri,G., Felice,A.E., Farrugia,R. and
            Bezzina Wettinger,S.
  TITLE     Genetic causes of Parkinson's disease in the Maltese: a study of
            selected mutations in LRRK2, MTHFR, QDPR and SPR
  JOURNAL   BMC Med Genet 17 (1), 65 (2016)
   PUBMED   27613114
  REMARK    GeneRIF: The allele frequencies for the SPR c.596-2A > G (0.7%)
            polymorphism is not a major cause of Parkinson's disease in the
            Maltese.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Yco,L.P., Geerts,D., Mocz,G., Koster,J. and Bachmann,A.S.
  TITLE     Effect of sulfasalazine on human neuroblastoma: analysis of
            sepiapterin reductase (SPR) as a new therapeutic target
  JOURNAL   BMC Cancer 15, 477 (2015)
   PUBMED   26093909
  REMARK    GeneRIF: We earlier presented evidence for a physical interaction
            between ODC and SPR and we showed that RNAi-mediated knockdown of
            SPR expression significantly reduced native ODC enzyme activity and
            impeded Neuroblastoma cell proliferation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Thony,B., Heizmann,C.W. and Mattei,M.G.
  TITLE     Human GTP-cyclohydrolase I gene and sepiapterin reductase gene map
            to region 14q21-q22 and 2p14-p12, respectively, by in situ
            hybridization
  JOURNAL   Genomics 26 (1), 168-170 (1995)
   PUBMED   7782081
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Friedman,J.
  TITLE     Sepiapterin Reductase Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26131547
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Maier,J., Schott,K., Werner,T., Bacher,A. and Ziegler,I.
  TITLE     Northern blot analysis of sepiapterin reductase mRNA in mammalian
            cell lines and tissues
  JOURNAL   Adv Exp Med Biol 338, 195-198 (1993)
   PUBMED   8304109
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Ichinose,H., Katoh,S., Sueoka,T., Titani,K., Fujita,K. and
            Nagatsu,T.
  TITLE     Cloning and sequencing of cDNA encoding human sepiapterin
            reductase--an enzyme involved in tetrahydrobiopterin biosynthesis
  JOURNAL   Biochem Biophys Res Commun 179 (1), 183-189 (1991)
   PUBMED   1883349
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Takikawa,S., Curtius,H.C., Redweik,U., Leimbacher,W. and Ghisla,S.
  TITLE     Biosynthesis of tetrahydrobiopterin. Purification and
            characterization of 6-pyruvoyl-tetrahydropterin synthase from human
            liver
  JOURNAL   Eur J Biochem 161 (2), 295-302 (1986)
   PUBMED   3536512
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092630.3, BC017310.2 and
            BF434649.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an aldo-keto reductase that catalyzes
            the NADPH-dependent reduction of pteridine derivatives and is
            important in the biosynthesis of tetrahydrobiopterin (BH4).
            Mutations in this gene result in DOPA-responsive dystonia due to
            sepiaterin reductase deficiency. A pseudogene has been identified
            on chromosome 1. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.467140.1, AK222942.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000234454.6/ ENSP00000234454.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.2"
     Protein         1..261
                     /product="sepiapterin reductase"
                     /EC_number="1.1.1.153"
                     /note="short chain dehydrogenase/reductase family 38C,
                     member 1; sepiapterin reductase
                     (7,8-dihydrobiopterin:NADP+ oxidoreductase); Sepiapterin
                     reductase (L-erythro-7,8-dihydrobiopterin forming)"
                     /calculated_mol_wt=27917
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P18297; propagated from
                     UniProtKB/Swiss-Prot (P35270.1)"
     Region          8..260
                     /region_name="sepiapter_red"
                     /note="sepiapterin reductase; TIGR01500"
                     /db_xref="CDD:273660"
     Site            order(14..19,41..43,68..70,100..102,126,155..157,170,174,
                     198..201,203..206)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187625"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P18297; propagated from
                     UniProtKB/Swiss-Prot (P35270.1)"
     Site            order(77,117..118,120..121,124..125,128..129,132..133,136,
                     159..161,168..169,171..172,176,179..180,183..184,186..188)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187625"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35270.1)"
     Site            order(127,157,170,174)
                     /site_type="active"
                     /db_xref="CDD:187625"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2, in vitro.
                     /evidence=ECO:0000269|PubMed:11825621; propagated from
                     UniProtKB/Swiss-Prot (P35270.1)"
     CDS             1..261
                     /gene="SPR"
                     /gene_synonym="SDR38C1"
                     /coded_by="NM_003124.5:26..811"
                     /db_xref="CCDS:CCDS1920.1"
                     /db_xref="GeneID:6697"
                     /db_xref="HGNC:HGNC:11257"
                     /db_xref="MIM:182125"
ORIGIN      
        1 megglgravc lltgasrgfg rtlapllasl lspgsvlvls arndealrql eaelgaersg
       61 lrvvrvpadl gaeaglqqll galrelprpk glqrlllinn agslgdvskg fvdlsdstqv
      121 nnywalnlts mlcltssvlk afpdspglnr tvvnisslca lqpfkgwaly cagkaardml
      181 fqvlaleepn vrvlnyapgp ldtdmqqlar etsvdpdmrk glqelkakgk lvdckvsaqk
      241 llsllekdef ksgahvdfyd k
//
LOCUS       NP_001346954             405 aa            linear   ROD 27-APR-2025
DEFINITION  dematin isoform 1 [Mus musculus].
ACCESSION   NP_001346954 XP_006518594
VERSION     NP_001346954.1
DBSOURCE    REFSEQ: accession NM_001360025.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Huang,S., Reed,C., Ilsley,M., Magor,G., Tallack,M., Landsberg,M.,
            Mitchell,H., Gillinder,K. and Perkins,A.
  TITLE     Mutations in linker-2 of KLF1 impair expression of membrane
            transporters and cytoskeletal proteins causing hemolysis
  JOURNAL   Nat Commun 15 (1), 7019 (2024)
   PUBMED   39147774
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Fritz,D.I., Ding,Y., Merrill-Skoloff,G., Flaumenhaft,R., Hanada,T.
            and Chishti,A.H.
  TITLE     Dematin Regulates Calcium Mobilization, Thrombosis, and Early Akt
            Activation in Platelets
  JOURNAL   Mol Cell Biol 43 (6), 283-299 (2023)
   PUBMED   37216480
  REMARK    GeneRIF: Dematin Regulates Calcium Mobilization, Thrombosis, and
            Early Akt Activation in Platelets.
REFERENCE   3  (residues 1 to 405)
  AUTHORS   O'Neil,S.D., Racz,B., Brown,W.E., Gao,Y., Soderblom,E.J., Yasuda,R.
            and Soderling,S.H.
  TITLE     Action potential-coupled Rho GTPase signaling drives presynaptic
            plasticity
  JOURNAL   Elife 10, e63756 (2021)
   PUBMED   34269176
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Huang,Y.S., Delgadillo,L.F., Cyr,K.H., Kingsley,P.D., An,X.,
            McGrath,K.E., Mohandas,N., Conboy,J.G., Waugh,R.E., Wan,J. and
            Palis,J.
  TITLE     Circulating primitive erythroblasts establish a functional, protein
            4.1R-dependent cytoskeletal network prior to enucleating
  JOURNAL   Sci Rep 7 (1), 5164 (2017)
   PUBMED   28701737
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Lu,Y., Hanada,T., Fujiwara,Y., Nwankwo,J.O., Wieschhaus,A.J.,
            Hartwig,J., Huang,S., Han,J. and Chishti,A.H.
  TITLE     Gene disruption of dematin causes precipitous loss of erythrocyte
            membrane stability and severe hemolytic anemia
  JOURNAL   Blood 128 (1), 93-103 (2016)
   PUBMED   27073223
  REMARK    GeneRIF: results demonstrate that dematin plays a critical role in
            maintaining the fundamental properties of the membrane cytoskeleton
            complex.
REFERENCE   6  (residues 1 to 405)
  AUTHORS   Strehl,S., Glatt,K., Liu,Q.M., Glatt,H. and Lalande,M.
  TITLE     Characterization of two novel protocadherins (PCDH8 and PCDH9)
            localized on human chromosome 13 and mouse chromosome 14
  JOURNAL   Genomics 53 (1), 81-89 (1998)
   PUBMED   9787079
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Cornwall,G.A. and Hsia,N.
  TITLE     ADAM7, a member of the ADAM (a disintegrin and metalloprotease)
            gene family is specifically expressed in the mouse anterior
            pituitary and epididymis
  JOURNAL   Endocrinology 138 (10), 4262-4272 (1997)
   PUBMED   9322939
REFERENCE   8  (residues 1 to 405)
  AUTHORS   Malgaretti,N., Pozzoli,O., Bosetti,A., Corradi,A., Ciarmatori,S.,
            Panigada,M., Bianchi,M.E., Martinez,S. and Consalez,G.G.
  TITLE     Mmot1, a new helix-loop-helix transcription factor gene displaying
            a sharp expression boundary in the embryonic mouse brain
  JOURNAL   J Biol Chem 272 (28), 17632-17639 (1997)
   PUBMED   9211912
REFERENCE   9  (residues 1 to 405)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
REFERENCE   10 (residues 1 to 405)
  AUTHORS   Peters,L.L., Eicher,E.M., Azim,A.C. and Chishti,A.H.
  TITLE     The gene encoding the erythrocyte membrane skeleton protein dematin
            (Epb4.9) maps to mouse chromosome 14
  JOURNAL   Genomics 26 (3), 634-635 (1995)
   PUBMED   7607697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY282941.1, BY259253.1, CJ070069.1, AK162866.1, AK165204.1,
            BY601680.1 and AI413696.1.
            
            On Jan 25, 2018 this sequence version replaced XP_006518594.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF155547.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN01164131 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 36.32 cM"
     Protein         1..405
                     /product="dematin isoform 1"
                     /note="erythrocyte membrane protein band 4.9; erythrocyte
                     protein band 4.9"
                     /calculated_mol_wt=45337
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV69.1)"
     Region          8..355
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Region          81..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Region          108..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Region          224..308
                     /region_name="Interaction with RASGRF2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087,
                     ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Region          370..405
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:Q08495; propagated from
                     UniProtKB/Swiss-Prot (Q9WV69.1)"
     CDS             1..405
                     /gene="Dmtn"
                     /gene_synonym="dematin; Epb4.9; Epb49"
                     /coded_by="NM_001360025.1:382..1599"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS88708.1"
                     /db_xref="GeneID:13829"
                     /db_xref="MGI:MGI:99670"
ORIGIN      
        1 merlqkqplt spgsvsssrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srecslspks tspppspevw aesrtlgiis qastprttgt
      121 prtslphfhh pettrpdsni ykkppiykqr esvggspqsk hliedliies skfpaaqppd
      181 pnqpakietd ywpcppslav vetewrkrka srkgaeeeee eedddseeei kairerqkee
      241 lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl hsgtsksssl psygrttlsr
      301 lqstefspsg seagspglqn gegqrgrmdr gnslpcvleq kiypyemlvv tnkgrtklpp
      361 gvdrmrlerh lsaedfsrvf amspeefgkl alwkrnelkk kaslf
//
LOCUS       NP_035031               1076 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear factor of activated T-cells, cytoplasmic 3 isoform 1 [Mus
            musculus].
ACCESSION   NP_035031 XP_134391
VERSION     NP_035031.2
DBSOURCE    REFSEQ: accession NM_010901.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Bulow,S., Ederer,K.U., Holzinger,J.M., Zeller,L., Werner,M.,
            Toelge,M., Pfab,C., Hirsch,S., Gopferich,F., Hiergeist,A.,
            Berberich-Siebelt,F. and Gessner,A.
  TITLE     Bactericidal/permeability-increasing protein instructs dendritic
            cells to elicit Th22 cell response
  JOURNAL   Cell Rep 43 (3), 113929 (2024)
   PUBMED   38457343
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Pal,D., Dutta,S., Iyer,D.P., Shriram,D., Bhaduri,U. and Rao,M.R.S.
  TITLE     Identification of PAX6 and NFAT4 as the Transcriptional Regulators
            of the Long Noncoding RNA Mrhl in Neuronal Progenitors
  JOURNAL   Mol Cell Biol 42 (11), e0003622 (2022)
   PUBMED   36317923
  REMARK    GeneRIF: Identification of PAX6 and NFAT4 as the Transcriptional
            Regulators of the Long Noncoding RNA Mrhl in Neuronal Progenitors.
REFERENCE   4  (residues 1 to 1076)
  AUTHORS   Peuker,K., Strigli,A., Tauriello,D.V.F., Hendricks,A., von
            Schonfels,W., Burmeister,G., Brosch,M., Herrmann,A., Kruger,S.,
            Nitsche,J., Juznic,L., Geissler,M.M., Hiergeist,A., Gessner,A.,
            Wirbel,J., Ponnudurai,R.P., Tunger,A., Wehner,R., Stange,D.E.,
            Weitz,J., Aust,D.E., Baretton,G.B., Schmitz,M., Rocken,C.,
            Hampe,J., Hinz,S., Zeller,G., Chavakis,T., Schafmayer,C., Batlle,E.
            and Zeissig,S.
  TITLE     Microbiota-dependent activation of the myeloid calcineurin-NFAT
            pathway inhibits B7H3- and B7H4-dependent anti-tumor immunity in
            colorectal cancer
  JOURNAL   Immunity 55 (4), 701-717 (2022)
   PUBMED   35364006
REFERENCE   5  (residues 1 to 1076)
  AUTHORS   Liu,X., Guo,J.W., Lin,X.C., Tuo,Y.H., Peng,W.L., He,S.Y., Li,Z.Q.,
            Ye,Y.C., Yu,J., Zhang,F.R., Ma,M.M., Shang,J.Y., Lv,X.F.,
            Zhou,A.D., Ouyang,Y., Wang,C., Pang,R.P., Sun,J.X., Ou,J.S.,
            Zhou,J.G. and Liang,S.J.
  TITLE     Macrophage NFATc3 prevents foam cell formation and atherosclerosis:
            evidence and mechanisms
  JOURNAL   Eur Heart J 42 (47), 4847-4861 (2021)
   PUBMED   34570211
  REMARK    GeneRIF: Macrophage NFATc3 prevents foam cell formation and
            atherosclerosis: evidence and mechanisms.
REFERENCE   6  (residues 1 to 1076)
  AUTHORS   Pan,S., Koyano-Nakagawa,N., Tsuruta,L., Amasaki,Y., Yokota,T.,
            Mori,S., Arai,N. and Arai,K.
  TITLE     Molecular cloning and functional characterization of murine cDNA
            encoding transcription factor NFATc
  JOURNAL   Biochem Biophys Res Commun 240 (2), 314-323 (1997)
   PUBMED   9388475
REFERENCE   7  (residues 1 to 1076)
  AUTHORS   Liu,J., Koyano-Nakagawa,N., Amasaki,Y., Saito-Ohara,F., Ikeuchi,T.,
            Imai,S., Takano,T., Arai,N., Yokota,T. and Arai,K.
  TITLE     Calcineurin-dependent nuclear translocation of a murine
            transcription factor NFATx: molecular cloning and functional
            characterization
  JOURNAL   Mol Biol Cell 8 (1), 157-170 (1997)
   PUBMED   9017603
REFERENCE   8  (residues 1 to 1076)
  AUTHORS   Ho,S.N., Thomas,D.J., Timmerman,L.A., Li,X., Francke,U. and
            Crabtree,G.R.
  TITLE     NFATc3, a lymphoid-specific NFATc family member that is
            calcium-regulated and exhibits distinct DNA binding specificity
  JOURNAL   J Biol Chem 270 (34), 19898-19907 (1995)
   PUBMED   7650004
REFERENCE   9  (residues 1 to 1076)
  AUTHORS   Lin,X., Nelson,P.J., Frankfort,B., Tombler,E., Johnson,R. and
            Gelman,I.H.
  TITLE     Isolation and characterization of a novel mitogenic regulatory
            gene, 322, which is transcriptionally suppressed in cells
            transformed by src and ras
  JOURNAL   Mol Cell Biol 15 (5), 2754-2762 (1995)
   PUBMED   7739556
REFERENCE   10 (residues 1 to 1076)
  AUTHORS   Masuda,E.S., Naito,Y., Tokumitsu,H., Campbell,D., Saito,F.,
            Hannum,C., Arai,K. and Arai,N.
  TITLE     NFATx, a novel member of the nuclear factor of activated T cells
            family that is expressed predominantly in the thymus
  JOURNAL   Mol Cell Biol 15 (5), 2697-2706 (1995)
   PUBMED   7739550
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC133499.3 and AC133195.4.
            
            On Aug 25, 2006 this sequence version replaced NP_035031.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK134054.1, BC120901.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 53.08 cM"
     Protein         1..1076
                     /product="nuclear factor of activated T-cells, cytoplasmic
                     3 isoform 1"
                     /note="NF-AT4; NF-ATc3; T-cell transcription factor NFAT4;
                     nuclear factor of activated T-cells, cytoplasmic 3"
                     /calculated_mol_wt=115406
     Region          422..595
                     /region_name="RHD-n_NFAT"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor of activated T-cells (NFAT)
                     proteins; cd07881"
                     /db_xref="CDD:143641"
     Site            order(445,448,450..451,453..455,502,543,545..546,560..561,
                     563,594)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143641"
     Region          600..700
                     /region_name="IPT_NFAT"
                     /note="IPT domain of the NFAT family of transcription
                     factors. NFAT transcription complexes are a target of
                     calcineurin, a calcium dependent phosphatase, and activate
                     genes mainly involved in cell-cell-interaction; cd01178"
                     /db_xref="CDD:238583"
     Site            order(624,688)
                     /site_type="DNA binding"
                     /note="DNA binding sites [nucleotide binding]"
                     /db_xref="CDD:238583"
     CDS             1..1076
                     /gene="Nfatc3"
                     /gene_synonym="D8Ertd281e; NFAT4; NFATx"
                     /coded_by="NM_010901.3:302..3532"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS22628.1"
                     /db_xref="GeneID:18021"
                     /db_xref="MGI:MGI:103296"
ORIGIN      
        1 mttancgahd eldfklvfge dgapapvsqv srpadlepdd casiyifnvd pppstlnssl
       61 glphhgllqs hssvlspsfq lqgyknyegt gdiseskysp lggpkpfecp siqitsispn
      121 chqgtdahed dlhindpere ylerpsrdhl ylplepsyre sslspspass issrswfsda
      181 ssceslshiy ddvdselnea aarftlgspl tspggspggc pgeeswhqqy gsghslsprq
      241 spchsprssi tdenwlsprp asgpssrpts pcgkrrhssa evcyagslsp hhspvpspgh
      301 sprgsvtedt wltapvhtgs glspapfpfq ycvetdiplk trktsedqaa ilpgkleics
      361 ddqgnlspsr etsvddglgs qyplkkdssg dqflsvpspf twskpkpght pifrtsslpp
      421 ldwplpthfg qcelkievqp kthhrahyet egsrgavkas tgghpvvkll gysekpinlq
      481 mfigtaddry lrphafyqvh ritgktvata sqeiiiastk vleipllpen nmsasidcag
      541 ilklrnsdie lrkgetdigr kntrvrlvfr vhipqpsgkv lslqiasipv ecsqrsaqel
      601 phiekysins csvngghemi vtgsnflpes kiiflekgqd grphweaegk iirekcqgah
      661 ivlevppyhn pavtsavqvh fylcngkrkk sqsqrftytp vlmkqeqred tdlpsvpslp
      721 vphsaqaqrp ssetghphdr amsapgsllc qvqpaytsmv asthlpqlqc rdegagkeqh
      781 iatssvmhqp fqvtptspig ssyqsiqtsm yngptclpvn passqefdpv lfqqdaalss
      841 lvnlgcqpls pipfhssnsd atghllahsp hsvqtpphlq smgyhcsnag qtalsspvad
      901 qitgqpsshl qpitycpshp gsataaspaa shplasspis gpsspqlqpm pyqspssgta
      961 sspspttrmh sgqhstqaqs tgqgglsvps slvchslcdp asfppggatv sikpepedqe
     1021 pnfatiglqd itlddvneii grdmsqisvs qatevmrdtp lpgpaspdlm tshsaq
//
LOCUS       NP_542452                566 aa            linear   PRI 27-APR-2025
DEFINITION  osteoclast stimulatory transmembrane protein [Homo sapiens].
ACCESSION   NP_542452 XP_001722590 XP_496476 XP_943526
VERSION     NP_542452.1
DBSOURCE    REFSEQ: accession NM_080721.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Wang,Z.L., Liu,Y., Zhou,Y.L., Li,J.L., Sun,Q.Y., Wu,L.X., Wen,L.,
            Lai,Y.Y., Liu,Y.R., Chang,Y.J., Shi,H.X., Liu,K.Y., Huang,X.J.,
            Lu,J. and Ruan,G.R.
  TITLE     Osteoclast stimulatory transmembrane protein (OC-STAMP) is a
            promising molecular prognostic indicator for multiple myeloma
  JOURNAL   Eur J Haematol 105 (2), 185-195 (2020)
   PUBMED   32282962
  REMARK    GeneRIF: Osteoclast stimulatory transmembrane protein (OC-STAMP) is
            a promising molecular prognostic indicator for multiple myeloma.
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Yuan,H., He,J., Zhang,G., Zhang,D., Kong,X. and Chen,F.
  TITLE     Osteoclast stimulatory transmembrane protein induces a phenotypic
            switch in macrophage polarization suppressing an M1
            pro-inflammatory state
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 49 (10), 935-944 (2017)
   PUBMED   28981605
  REMARK    GeneRIF: Results indicte that oc-stamp may play an important role
            in macrophage polarization and inhibit the M1 pro-inflammatory
            state.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Yang,M., Birnbaum,M.J., MacKay,C.A., Mason-Savas,A., Thompson,B.
            and Odgren,P.R.
  TITLE     Osteoclast stimulatory transmembrane protein (OC-STAMP), a novel
            protein induced by RANKL that promotes osteoclast differentiation
  JOURNAL   J Cell Physiol 215 (2), 497-505 (2008)
   PUBMED   18064667
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034424.9.
            
            On or before Mar 26, 2009 this sequence version replaced
            XP_943526.1, XP_001722590.1, XP_496476.2.
            
            Summary: The protein encoded by this gene is orthologous to the
            mouse osteoclast stimulatory transmembrane protein (OCSTAMP), which
            is a membrane-anchored cell surface receptor that promotes
            nucleation of osteoclasts. The mouse protein is also involved in
            bone resorption and osteoclast differentiation. [provided by
            RefSeq, Feb 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1233594.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2148874 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000279028.3/ ENSP00000279028.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..566
                     /product="osteoclast stimulatory transmembrane protein"
                     /note="transmembrane protein C20orf123"
                     /calculated_mol_wt=61449
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR26.2)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR26.2)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR26.2)"
     Site            228..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR26.2)"
     Region          254..446
                     /region_name="DC_STAMP"
                     /note="DC-STAMP-like protein; pfam07782"
                     /db_xref="CDD:462265"
     Site            305..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR26.2)"
     Site            399..419
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR26.2)"
     CDS             1..566
                     /gene="OCSTAMP"
                     /gene_synonym="C20orf123; dJ257E24.3; OC-STAMP"
                     /coded_by="NM_080721.3:95..1795"
                     /db_xref="CCDS:CCDS54468.1"
                     /db_xref="GeneID:128506"
                     /db_xref="HGNC:HGNC:16116"
                     /db_xref="MIM:620432"
ORIGIN      
        1 mpghpgaaeq lvktgwrswh lgfwkalapl qaawdafsqp vpascgqllt qlllcaslaa
       61 aaaglvyhwl aslllyppgp samvatvcgl lvflslglvp pvrclfalsv ptlgmeqgrr
      121 lllsystatl aiavvpnvla nvgaagqvlr cvtegslesl lntthqlhaa sralgptgqa
      181 gsrgltfeaq dngsafylhm lrvtqqvled fsgleslara aalgtqrvvt glfmlgllve
      241 sawylhcylt dlrfdniyat qqltqrlaqa qathllappp twllqaaqlr lsqeellscl
      301 lrlgllalll vatavavatd hvafllaqat vdwaqklptv pitltvkydv aytvlgfipf
      361 lfnqlapesp flsvhssyqw elrltsarcp llparrpraa aplaagalql lagstvllea
      421 yarrlrhaia asfftaqear rvrhlharlq rrhdrhqgqq lplgdpscvp tprpackppa
      481 widyrldalr tessegegke lwscrdlscn lgpvpppcvt lgkslhlsep rflhlhndsi
      541 ftidvtyfpr rdvvrmegnt ghdrpg
//
LOCUS       NP_001356329             206 aa            linear   PRI 27-APR-2025
DEFINITION  ras-related protein Ral-B [Homo sapiens].
ACCESSION   NP_001356329
VERSION     NP_001356329.1
DBSOURCE    REFSEQ: accession NM_001369400.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Yoshimachi,S., Shirakawa,R., Cao,M., Trinh,D.A., Gao,P., Sakata,N.,
            Miyazaki,K., Goto,K., Miura,T., Ariake,K., Maeda,S., Masuda,K.,
            Ishida,M., Ohtsuka,H., Unno,M. and Horiuchi,H.
  TITLE     Ral GTPase-activating protein regulates the malignancy of
            pancreatic ductal adenocarcinoma
  JOURNAL   Cancer Sci 112 (8), 3064-3073 (2021)
   PUBMED   34009715
  REMARK    GeneRIF: Ral GTPase-activating protein regulates the malignancy of
            pancreatic ductal adenocarcinoma.
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Wang,Y., Zheng,Y., Chen,Q., Dai,Y. and Li,T.
  TITLE     MicroRNA-139 inhibits pancreatic-cancer carcinogenesis by
            suppressing RalB via the Ral/RAC/PI3K pathway
  JOURNAL   Arch Biochem Biophys 704, 108719 (2021)
   PUBMED   33290747
  REMARK    GeneRIF: MicroRNA-139 inhibits pancreatic-cancer carcinogenesis by
            suppressing RalB via the Ral/RAC/PI3K pathway.
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Naszai,M., Bellec,K., Yu,Y., Roman-Fernandez,A., Sandilands,E.,
            Johansson,J., Campbell,A.D., Norman,J.C., Sansom,O.J., Bryant,D.M.
            and Cordero,J.B.
  TITLE     RAL GTPases mediate EGFR-driven intestinal stem cell proliferation
            and tumourigenesis
  JOURNAL   Elife 10, e63807 (2021)
   PUBMED   34096503
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Khawaja,H., Campbell,A., Roberts,J.Z., Javadi,A., O'Reilly,P.,
            McArt,D., Allen,W.L., Majkut,J., Rehm,M., Bardelli,A., Di
            Nicolantonio,F., Scott,C.J., Kennedy,R., Vitale,N., Harrison,T.,
            Sansom,O.J., Longley,D.B., Evergren,E. and Van Schaeybroeck,S.
  TITLE     RALB GTPase: a critical regulator of DR5 expression and TRAIL
            sensitivity in KRAS mutant colorectal cancer
  JOURNAL   Cell Death Dis 11 (10), 930 (2020)
   PUBMED   33122623
  REMARK    GeneRIF: RALB GTPase: a critical regulator of DR5 expression and
            TRAIL sensitivity in KRAS mutant colorectal cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Joneson,T. and Bar-Sagi,D.
  TITLE     Ras effectors and their role in mitogenesis and oncogenesis
  JOURNAL   J Mol Med (Berl) 75 (8), 587-593 (1997)
   PUBMED   9297626
  REMARK    Review article
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Jilkina,O. and Bhullar,R.P.
  TITLE     Generation of antibodies specific for the RalA and RalB GTP-binding
            proteins and determination of their concentration and distribution
            in human platelets
  JOURNAL   Biochim Biophys Acta 1314 (1-2), 157-166 (1996)
   PUBMED   8972729
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Jullien-Flores,V., Dorseuil,O., Romero,F., Letourneur,F.,
            Saragosti,S., Berger,R., Tavitian,A., Gacon,G. and Camonis,J.H.
  TITLE     Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with
            CDC42/Rac GTPase-activating protein activity
  JOURNAL   J Biol Chem 270 (38), 22473-22477 (1995)
   PUBMED   7673236
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Hsieh,C.L., Swaroop,A. and Francke,U.
  TITLE     Chromosomal localization and cDNA sequence of human ralB, a GTP
            binding protein
  JOURNAL   Somat Cell Mol Genet 16 (4), 407-410 (1990)
   PUBMED   2120779
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Chardin,P. and Tavitian,A.
  TITLE     Coding sequences of human ralA and ralB cDNAs
  JOURNAL   Nucleic Acids Res 17 (11), 4380 (1989)
   PUBMED   2662142
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012363.6.
            
            Summary: This gene encodes a GTP-binding protein that belongs to
            the small GTPase superfamily and Ras family of proteins.
            GTP-binding proteins mediate the transmembrane signaling initiated
            by the occupancy of certain cell surface receptors. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.2"
     Protein         1..206
                     /product="ras-related protein Ral-B"
                     /EC_number="3.6.5.2"
                     /note="RAS-like protein B; v-ral simian leukemia viral
                     oncogene homolog B (ras related; GTP binding protein); ras
                     related GTP binding protein B; RALB Ras like
                     proto-oncogene B"
                     /calculated_mol_wt=23277
     Region          15..178
                     /region_name="RalA_RalB"
                     /note="Ral (Ras-like) family containing highly homologous
                     RalA and RalB; cd04139"
                     /db_xref="CDD:206710"
     Site            21..28
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206710"
     Site            order(22..23,70..72,74..75,79,82,97,99,102..103,106..107,
                     110)
                     /site_type="active"
                     /note="GDI interaction site [active]"
                     /db_xref="CDD:206710"
     Site            order(23..29,39..40,46,71,128..129,131,158..159)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206710"
     Site            order(28..29,43,45,51..52,65..66,68,70..71,160)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206710"
     Site            order(36,38,47..52,56,60..61,161..164,166)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:206710"
     Region          43..51
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11234.1)"
     Site            44..51
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206710"
     Site            46
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206710"
     Site            68..71
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206710"
     Site            70..88
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206710"
     Site            128..131
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206710"
     Site            order(140..141,144,148,156)
                     /site_type="active"
                     /note="alternate GDI interaction site [active]"
                     /db_xref="CDD:206710"
     Site            158..160
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206710"
     Region          180..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11234.1)"
     Site            203
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P11234.1)"
     CDS             1..206
                     /gene="RALB"
                     /coded_by="NM_001369400.1:180..800"
                     /db_xref="CCDS:CCDS2131.1"
                     /db_xref="GeneID:5899"
                     /db_xref="HGNC:HGNC:9840"
                     /db_xref="MIM:179551"
ORIGIN      
        1 maankskgqs slalhkvimv gsggvgksal tlqfmydefv edyeptkads yrkkvvldge
       61 evqidildta gqedyaaird nyfrsgegfl lvfsitehes ftataefreq ilrvkaeedk
      121 ipllvvgnks dleerrqvpv eearskaeew gvqyvetsak tranvdkvff dlmreirtkk
      181 msenkdkngk kssknkksfk erccll
//
LOCUS       NP_938080                603 aa            linear   PRI 27-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 10 [Homo sapiens].
ACCESSION   NP_938080
VERSION     NP_938080.1
DBSOURCE    REFSEQ: accession NM_198321.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Zhao,F.Y., Zhang,Q., Wang,J.M., Jiang,J.Y., Huyan,L.Y., Liu,B.Q.,
            Yan,J., Li,C. and Wang,H.Q.
  TITLE     BAG3 epigenetically regulates GALNT10 expression via WDR5 and
            facilitates the stem cell-like properties of platin-resistant
            ovarian cancer cells
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1868 (9), 119077 (2021)
   PUBMED   34111434
  REMARK    GeneRIF: BAG3 epigenetically regulates GALNT10 expression via WDR5
            and facilitates the stem cell-like properties of platin-resistant
            ovarian cancer cells.
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Liu,Z., Pan,L., Yan,X. and Duan,X.
  TITLE     The long noncoding RNA DLGAP1-AS2 facilitates cholangiocarcinoma
            progression via miR-505 and GALNT10
  JOURNAL   FEBS Open Bio 11 (2), 413-422 (2021)
   PUBMED   33301605
  REMARK    GeneRIF: The long noncoding RNA DLGAP1-AS2 facilitates
            cholangiocarcinoma progression via miR-505 and GALNT10.
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Xu,G., Wu,Y.L., Li,N., Xu,R., Zhang,J.B., Ming,H. and Zhang,Y.
  TITLE     GALNT10 promotes the proliferation and metastatic ability of
            gastric cancer and reduces 5-fluorouracil sensitivity by activating
            HOXD13
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (22), 11610-11619 (2020)
   PUBMED   33275228
  REMARK    GeneRIF: GALNT10 promotes the proliferation and metastatic ability
            of gastric cancer and reduces 5-fluorouracil sensitivity by
            activating HOXD13.
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Zhang,G., Lu,J., Yang,M., Wang,Y., Liu,H. and Xu,C.
  TITLE     Elevated GALNT10 expression identifies immunosuppressive
            microenvironment and dismal prognosis of patients with high grade
            serous ovarian cancer
  JOURNAL   Cancer Immunol Immunother 69 (2), 175-187 (2020)
   PUBMED   31853576
  REMARK    GeneRIF: high GALNT10 expression confers with immunosuppressive
            microenvironment to promote tumor progression and predicts poor
            clinical outcomes in HGSC patients.
REFERENCE   5  (residues 1 to 603)
  AUTHORS   Liu,L., Xiong,Y., Xi,W., Wang,J., Qu,Y., Lin,Z., Chen,X., Yao,J.,
            Xu,J. and Guo,J.
  TITLE     Prognostic role of N-Acetylgalactosaminyltransferase 10 in
            metastatic renal cell carcinoma
  JOURNAL   Oncotarget 8 (9), 14995-15003 (2017)
   PUBMED   28122358
  REMARK    GeneRIF: identified that GALNT10 was an independent prognostic
            factor for overall survival
REFERENCE   6  (residues 1 to 603)
  AUTHORS   Monda,K.L., Chen,G.K., Taylor,K.C., Palmer,C., Edwards,T.L.,
            Lange,L.A., Ng,M.C., Adeyemo,A.A., Allison,M.A., Bielak,L.F.,
            Chen,G., Graff,M., Irvin,M.R., Rhie,S.K., Li,G., Liu,Y., Liu,Y.,
            Lu,Y., Nalls,M.A., Sun,Y.V., Wojczynski,M.K., Yanek,L.R.,
            Aldrich,M.C., Ademola,A., Amos,C.I., Bandera,E.V., Bock,C.H.,
            Britton,A., Broeckel,U., Cai,Q., Caporaso,N.E., Carlson,C.S.,
            Carpten,J., Casey,G., Chen,W.M., Chen,F., Chen,Y.D., Chiang,C.W.,
            Coetzee,G.A., Demerath,E., Deming-Halverson,S.L., Driver,R.W.,
            Dubbert,P., Feitosa,M.F., Feng,Y., Freedman,B.I., Gillanders,E.M.,
            Gottesman,O., Guo,X., Haritunians,T., Harris,T., Harris,C.C.,
            Hennis,A.J., Hernandez,D.G., McNeill,L.H., Howard,T.D.,
            Howard,B.V., Howard,V.J., Johnson,K.C., Kang,S.J., Keating,B.J.,
            Kolb,S., Kuller,L.H., Kutlar,A., Langefeld,C.D., Lettre,G.,
            Lohman,K., Lotay,V., Lyon,H., Manson,J.E., Maixner,W., Meng,Y.A.,
            Monroe,K.R., Morhason-Bello,I., Murphy,A.B., Mychaleckyj,J.C.,
            Nadukuru,R., Nathanson,K.L., Nayak,U., N'diaye,A., Nemesure,B.,
            Wu,S.Y., Leske,M.C., Neslund-Dudas,C., Neuhouser,M., Nyante,S.,
            Ochs-Balcom,H., Ogunniyi,A., Ogundiran,T.O., Ojengbede,O.,
            Olopade,O.I., Palmer,J.R., Ruiz-Narvaez,E.A., Palmer,N.D.,
            Press,M.F., Rampersaud,E., Rasmussen-Torvik,L.J.,
            Rodriguez-Gil,J.L., Salako,B., Schadt,E.E., Schwartz,A.G.,
            Shriner,D.A., Siscovick,D., Smith,S.B., Wassertheil-Smoller,S.,
            Speliotes,E.K., Spitz,M.R., Sucheston,L., Taylor,H., Tayo,B.O.,
            Tucker,M.A., Van Den Berg,D.J., Edwards,D.R., Wang,Z.,
            Wiencke,J.K., Winkler,T.W., Witte,J.S., Wrensch,M., Wu,X.,
            Yang,J.J., Levin,A.M., Young,T.R., Zakai,N.A., Cushman,M.,
            Zanetti,K.A., Zhao,J.H., Zhao,W., Zheng,Y., Zhou,J., Ziegler,R.G.,
            Zmuda,J.M., Fernandes,J.K., Gilkeson,G.S., Kamen,D.L., Hunt,K.J.,
            Spruill,I.J., Ambrosone,C.B., Ambs,S., Arnett,D.K., Atwood,L.,
            Becker,D.M., Berndt,S.I., Bernstein,L., Blot,W.J., Borecki,I.B.,
            Bottinger,E.P., Bowden,D.W., Burke,G., Chanock,S.J., Cooper,R.S.,
            Ding,J., Duggan,D., Evans,M.K., Fox,C., Garvey,W.T.,
            Bradfield,J.P., Hakonarson,H., Grant,S.F., Hsing,A., Chu,L.,
            Hu,J.J., Huo,D., Ingles,S.A., John,E.M., Jordan,J.M.,
            Kabagambe,E.K., Kardia,S.L., Kittles,R.A., Goodman,P.J.,
            Klein,E.A., Kolonel,L.N., Le Marchand,L., Liu,S., McKnight,B.,
            Millikan,R.C., Mosley,T.H., Padhukasahasram,B., Williams,L.K.,
            Patel,S.R., Peters,U., Pettaway,C.A., Peyser,P.A., Psaty,B.M.,
            Redline,S., Rotimi,C.N., Rybicki,B.A., Sale,M.M., Schreiner,P.J.,
            Signorello,L.B., Singleton,A.B., Stanford,J.L., Strom,S.S.,
            Thun,M.J., Vitolins,M., Zheng,W., Moore,J.H., Williams,S.M.,
            Ketkar,S., Zhu,X., Zonderman,A.B., Kooperberg,C.,
            Papanicolaou,G.J., Henderson,B.E., Reiner,A.P., Hirschhorn,J.N.,
            Loos,R.J., North,K.E. and Haiman,C.A.
  CONSRTM   NABEC Consortium; UKBEC Consortium; BioBank Japan Project; AGEN
            Consortium
  TITLE     A meta-analysis identifies new loci associated with body mass index
            in individuals of African ancestry
  JOURNAL   Nat Genet 45 (6), 690-696 (2013)
   PUBMED   23583978
REFERENCE   7  (residues 1 to 603)
  AUTHORS   Ng,M.C., Hester,J.M., Wing,M.R., Li,J., Xu,J., Hicks,P.J.,
            Roh,B.H., Lu,L., Divers,J., Langefeld,C.D., Freedman,B.I.,
            Palmer,N.D. and Bowden,D.W.
  TITLE     Genome-wide association of BMI in African Americans
  JOURNAL   Obesity (Silver Spring) 20 (3), 622-627 (2012)
   PUBMED   21701570
REFERENCE   8  (residues 1 to 603)
  AUTHORS   Perrine,C.L., Ganguli,A., Wu,P., Bertozzi,C.R., Fritz,T.A.,
            Raman,J., Tabak,L.A. and Gerken,T.A.
  TITLE     Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc
            T10), involved in mucin-type O-glycosylation, has a unique
            GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in
            ppGalNAc T1 or T2
  JOURNAL   J Biol Chem 284 (30), 20387-20397 (2009)
   PUBMED   19460755
  REMARK    GeneRIF: GalNAc T10 has a large and pronounced glycopeptide
            preference for Ser/Thr-O-GalNAc only at the +1 position from the
            acceptor site, whereas T1 and T2 have significantly reduced and
            variable preferences for Ser/Thr-O-GalNAc.
REFERENCE   9  (residues 1 to 603)
  AUTHORS   Raman,J., Fritz,T.A., Gerken,T.A., Jamison,O., Live,D., Liu,M. and
            Tabak,L.A.
  TITLE     The catalytic and lectin domains of UDP-GalNAc:polypeptide
            alpha-N-Acetylgalactosaminyltransferase function in concert to
            direct glycosylation site selection
  JOURNAL   J Biol Chem 283 (34), 22942-22951 (2008)
   PUBMED   18562306
  REMARK    GeneRIF: sequence recognition by the catalytic domain differs
            between hT2 and hT10 in that hT10 requires a pre-existing GalNAc
            residue while hT2 does not
REFERENCE   10 (residues 1 to 603)
  AUTHORS   Cheng,L., Tachibana,K., Zhang,Y., Guo,Jm., Kahori Tachibana,K.,
            Kameyama,A., Wang,H., Hiruma,T., Iwasaki,H., Togayachi,A., Kudo,T.
            and Narimatsu,H.
  TITLE     Characterization of a novel human UDP-GalNAc transferase,
            pp-GalNAc-T10
  JOURNAL   FEBS Lett 531 (2), 115-121 (2002)
   PUBMED   12417297
  REMARK    GeneRIF: Molecular cloning and characterization of pp-GalNAc-T10 as
            a UDP-GalNAc transferase.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010295.7, BC050333.1,
            AJ505950.1, AC008625.5 and BQ549377.1.
            
            Summary: This gene encodes a member of the GalNAc polypeptide
            N-acetylgalactosaminyltransferases. These enzymes catalyze the
            first step in the synthesis of mucin-type oligosaccharides. These
            proteins transfer GalNAc from UDP-GalNAc to either serine or
            threonine residues of polypeptide acceptors. The protein encoded by
            this locus may have increased catalytic activity toward
            glycosylated peptides compared to activity toward non-glycosylated
            peptides.[provided by RefSeq, Apr 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127135.1, AB078145.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297107.11/ ENSP00000297107.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.2"
     Protein         1..603
                     /product="polypeptide N-acetylgalactosaminyltransferase
                     10"
                     /EC_number="2.4.1.41"
                     /note="GalNAc transferase 10; UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase 10;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 10 (GalNAc-T10)"
                     /calculated_mol_wt=68861
     Site            12..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SR1.2)"
     Region          38..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SR1.2)"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16650853; propagated from
                     UniProtKB/Swiss-Prot (Q86SR1.2)"
     Region          144..253
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SR1.2)"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16650853; propagated from
                     UniProtKB/Swiss-Prot (Q86SR1.2)"
     Region          148..443
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(152..154,156,185,214,217,221,237..239,319..320,
                     342..343,345,370,373,378)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(237,239,370)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          311..373
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SR1.2)"
     Region          373..384
                     /region_name="Flexible loop"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SR1.2)"
     Region          454..603
                     /region_name="beta-trefoil_Ricin_GALNT10"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide N-acetylgalactosaminyltransferase 10
                     (GALNT10) and similar proteins; cd23476"
                     /db_xref="CDD:467354"
     Site            order(456,593,595..596)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467354"
     Site            order(525,536,539,543..544)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467354"
     Site            593
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16650853; propagated from
                     UniProtKB/Swiss-Prot (Q86SR1.2)"
     CDS             1..603
                     /gene="GALNT10"
                     /gene_synonym="GALNACT10; PPGALNACT10; PPGANTASE10"
                     /coded_by="NM_198321.4:135..1946"
                     /db_xref="CCDS:CCDS4325.1"
                     /db_xref="GeneID:55568"
                     /db_xref="HGNC:HGNC:19873"
                     /db_xref="MIM:608043"
ORIGIN      
        1 mrrkekrllq avalvlaalv llpnvglwal yrerqpdgtp ggsgaavapa agqgshsrqk
       61 ktfflgdgqk lkdwhdkeai rrdaqrvgng eqgrpypmtd aervdqayre ngfniyvsdk
      121 islnrslpdi rhpncnskry letlpntsii ipfhnegwss llrtvhsvln rsppelvaei
      181 vlvddfsdre hlkkpledym alfpsvrilr tkkreglirt rmlgasvatg dvitfldshc
      241 eanvnwlppl ldriarnrkt ivcpmidvid hddfryetqa gdamrgafdw emyykripip
      301 pelqkadpsd pfespvmagg lfavdrkwfw elggydpgle iwggeqyeis fkvwmcggrm
      361 edipcsrvgh iyrkyvpykv pagvslarnl krvaevwmde yaeyiyqrrp eyrhlsagdv
      421 avqkklrssl ncksfkwfmt kiawdlpkfy ppveppaaaw geirnvgtgl cadtkhgalg
      481 splrlegcvr grgeaawnnm qvftftwred irpgdpqhtk kfcfdaisht spvtlydchs
      541 mkgnqlwkyr kdktlyhpvs gscmdcsesd hrifmntcnp ssltqqwlfe htnstvlekf
      601 nrn
//
LOCUS       NP_001356855             704 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001356855 XP_016884490
VERSION     NP_001356855.1
DBSOURCE    REFSEQ: accession NM_001369926.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 704)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 704)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 704)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 704)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 704)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 704)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            On Apr 24, 2019 this sequence version replaced XP_016884490.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.22946.1,
                                           SRR1660809.208381.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..704
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 6"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=79905
     Region          416..455
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..704
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369926.1:177..2291"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mpalpldqlq ithkdpktgk lrtspalvif detlqkclds ylryvprkfd egvasapevv
       61 dmqkrlhrsv fltflrmsth keskdhfisp safgeilynn flfdipkild lcvlfgkgns
      121 pllqkmigni ftqqpsyysd ldetlptilq vfsnilqhcg lqgdganttp qkleergrlt
      181 psdmpllelk divlylcdtc ttlwafldif placqtfqkh dfcyrlasfy eaaipemesa
      241 ikkrrledsk llgdlwqrls hsrkklmeif hiilnqicll pilesscdni qgfieeflqi
      301 fssllqekrf lrdydalfpv aedisllqqa ssvldetrta yilqavesaw egvdrrkatd
      361 akdpsvieep ngepngvtvt aeavsqassh penseeeecm gaaaavgpam cgveldslis
      421 qvkdllpdlg egfilacley yhydpeqvin nileerlapt lsqldrnldr emkpdptpll
      481 tsrhnvfqnd efdvfsrdsv dlsrvhkgks trkeentrsl lndkravaaq rqryeqysvv
      541 veevplqpge slpyhsvyye deyddtydgn qvgandadsd delisrrpft ipqvlrtkvp
      601 regqeedddd eeddadeeap kpdhfvqdpa vlrekaearr maflakkgyr hdsstavags
      661 prghgqsret tqerrkkean katranhnrr tmadrkrskg mips
//
LOCUS       NP_443183                329 aa            linear   PRI 27-APR-2025
DEFINITION  deoxynucleotidyltransferase terminal-interacting protein 1 [Homo
            sapiens].
ACCESSION   NP_443183
VERSION     NP_443183.1
DBSOURCE    REFSEQ: accession NM_052951.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Ding,S., Gao,Y., Lv,D., Tao,Y., Liu,S., Chen,C., Huang,Z.,
            Zheng,S., Hu,Y., Chow,L.K., Wei,Y., Feng,P., Dai,W., Wang,X. and
            Xia,Y.
  TITLE     DNTTIP1 promotes nasopharyngeal carcinoma metastasis via recruiting
            HDAC1 to DUSP2 promoter and activating ERK signaling pathway
  JOURNAL   EBioMedicine 81, 104100 (2022)
   PUBMED   35689852
  REMARK    GeneRIF: DNTTIP1 promotes nasopharyngeal carcinoma metastasis via
            recruiting HDAC1 to DUSP2 promoter and activating ERK signaling
            pathway.
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Liu,Q., Xiong,J., Xu,D., Hao,N., Zhang,Y., Sang,Y., Wang,Z.,
            Zheng,X., Min,J., Diao,H., Raphael,J., Maleki Vareki,S.,
            Koropatnick,J. and Min,W.
  TITLE     TdIF1-LSD1 Axis Regulates Epithelial-Mesenchymal Transition and
            Metastasis via Histone Demethylation of E-Cadherin Promoter in Lung
            Cancer
  JOURNAL   Int J Mol Sci 23 (1), 250 (2021)
   PUBMED   35008676
  REMARK    GeneRIF: TdIF1-LSD1 Axis Regulates Epithelial-Mesenchymal
            Transition and Metastasis via Histone Demethylation of E-Cadherin
            Promoter in Lung Cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Sawai,Y., Kasamatsu,A., Nakashima,D., Fushimi,K., Kasama,H.,
            Iyoda,M., Kouzu,Y., Shiiba,M., Tanzawa,H. and Uzawa,K.
  TITLE     Critical role of deoxynucleotidyl transferase terminal interacting
            protein 1 in oral cancer
  JOURNAL   Lab Invest 98 (8), 980-988 (2018)
   PUBMED   29855544
  REMARK    GeneRIF: Overexpressed deoxynucleotidyltransferase terminal
            interacting protein 1 (DNTTIP1) was observed in oral squamous cell
            carcinomas (OSCCs) in vitro and in vivo and was correlated
            positively with tumoral growth.
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Kubota,T., Maezawa,S., Koiwai,K., Hayano,T. and Koiwai,O.
  TITLE     Identification of functional domains in TdIF1 and its inhibitory
            mechanism for TdT activity
  JOURNAL   Genes Cells 12 (8), 941-959 (2007)
   PUBMED   17663723
  REMARK    GeneRIF: The TdT binding, DNA binding and dimerization regions, and
            nuclear localization signal (NLS) in TdIF1, were identified.
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Fujisaki,S., Sato,A., Toyomoto,T., Hayano,T., Sugai,M., Kubota,T.
            and Koiwai,O.
  TITLE     Direct binding of TReP-132 with TdT results in reduction of TdT
            activity
  JOURNAL   Genes Cells 11 (1), 47-57 (2006)
   PUBMED   16371131
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Tomarev,S.I., Wistow,G., Raymond,V., Dubois,S. and Malyukova,I.
  TITLE     Gene expression profile of the human trabecular meshwork: NEIBank
            sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 44 (6), 2588-2596 (2003)
   PUBMED   12766061
REFERENCE   9  (residues 1 to 329)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 329)
  AUTHORS   Yamashita,N., Shimazaki,N., Ibe,S., Kaneko,R., Tanabe,A.,
            Toyomoto,T., Fujita,K., Hasegawa,T., Toji,S., Tamai,K., Yamamoto,H.
            and Koiwai,O.
  TITLE     Terminal deoxynucleotidyltransferase directly interacts with a
            novel nuclear protein that is homologous to p65
  JOURNAL   Genes Cells 6 (7), 641-652 (2001)
   PUBMED   11473582
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG720866.1 and AB035676.1.
            
            Summary: DNTTIP1 binds DNA and enhances the activity of terminal
            deoxynucleotidyltransferase (TDT, or DNTT; MIM 187410), a DNA
            polymerase that catalyzes the polymerization of DNA in the absence
            of a DNA template (Yamashita et al., 2001 [PubMed
            11473582]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1064637.1, AB035676.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372622.8/ ENSP00000361705.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..329
                     /product="deoxynucleotidyltransferase terminal-interacting
                     protein 1"
                     /note="TdT binding protein; tdT-interacting factor 1;
                     terminal deoxynucleotidyltransferase-interacting factor 1"
                     /calculated_mol_wt=36882
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H147.2)"
     Region          56..147
                     /region_name="Important for dimerization.
                     /evidence=ECO:0000269|PubMed:25653165"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H147.2)"
     Region          65..132
                     /region_name="DNTTIP1_dimer"
                     /note="DNTTIP1 dimerization domain; pfam18192"
                     /db_xref="CDD:408020"
     Region          147..178
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H147.2)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H147.2)"
     Region          164..170
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H147.2)"
     Region          197..316
                     /region_name="Important for DNA and nucleosome binding.
                     /evidence=ECO:0000269|PubMed:25653165"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H147.2)"
     CDS             1..329
                     /gene="DNTTIP1"
                     /gene_synonym="C20orf167; dJ447F3.4; Tdif1"
                     /coded_by="NM_052951.3:52..1041"
                     /db_xref="CCDS:CCDS13369.1"
                     /db_xref="GeneID:116092"
                     /db_xref="HGNC:HGNC:16160"
                     /db_xref="MIM:611388"
ORIGIN      
        1 mgatgdaeqp rgpsgaergg lelgdagaag qlvltnpwni mikhrqvqrr grrsqmttsf
       61 tdpaismdll ravlqpsine eiqtvfnkym kffqkaalnv rdnvgeevda eqliqeacrs
      121 cleqakllfs dgekviprlt helpgikrgr qaeeecahrg splpkkrkgr ppghilssdr
      181 aaagmvwkpk scepirregp kwdparlnes ttfvlgsran kalgmggtrg riyikhphlf
      241 kyaadpqdkh wlaeqhhmra tggkmaylli eedirdlaas ddyrgcldlk leelksfvlp
      301 swmvekmrky metlrteneh raveappqt
//
LOCUS       NP_001297997              77 aa            linear   ROD 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
            isoform 2 [Mus musculus].
ACCESSION   NP_001297997 XP_006505224
VERSION     NP_001297997.1
DBSOURCE    REFSEQ: accession NM_001311068.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Vercellino,I. and Sazanov,L.A.
  TITLE     SCAF1 drives the compositional diversity of mammalian respirasomes
  JOURNAL   Nat Struct Mol Biol 31 (7), 1061-1071 (2024)
   PUBMED   38575788
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Nie,H., Yu,X., He,H., Zhou,L., Li,Q., Song,C., Wang,D., Ren,T.,
            Chen,Z., Huang,H., Dai,X. and Zhou,Y.
  TITLE     Hepatocyte miR-33a mediates mitochondrial dysfunction and
            hepatosteatosis by suppressing NDUFA5
  JOURNAL   J Cell Mol Med 22 (12), 6285-6293 (2018)
   PUBMED   30324697
  REMARK    GeneRIF: Through bioinformatics prediction, we found miR-33a
            directly targeted on the 3'-UTR of NDUFA5. Dual-luciferase reporter
            analysis further confirmed the direct suppression of miR-33a on
            NDUFA5 expression
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Yavari,A., Stocker,C.J., Ghaffari,S., Wargent,E.T., Steeples,V.,
            Czibik,G., Pinter,K., Bellahcene,M., Woods,A., Martinez de
            Morentin,P.B., Cansell,C., Lam,B.Y., Chuster,A., Petkevicius,K.,
            Nguyen-Tu,M.S., Martinez-Sanchez,A., Pullen,T.J., Oliver,P.L.,
            Stockenhuber,A., Nguyen,C., Lazdam,M., O'Dowd,J.F., Harikumar,P.,
            Toth,M., Beall,C., Kyriakou,T., Parnis,J., Sarma,D., Katritsis,G.,
            Wortmann,D.D., Harper,A.R., Brown,L.A., Willows,R., Gandra,S.,
            Poncio,V., de Oliveira Figueiredo,M.J., Qi,N.R., Peirson,S.N.,
            McCrimmon,R.J., Gereben,B., Tretter,L., Fekete,C., Redwood,C.,
            Yeo,G.S., Heisler,L.K., Rutter,G.A., Smith,M.A., Withers,D.J.,
            Carling,D., Sternick,E.B., Arch,J.R., Cawthorne,M.A., Watkins,H.
            and Ashrafian,H.
  TITLE     Chronic Activation of gamma2 AMPK Induces Obesity and Reduces beta
            Cell Function
  JOURNAL   Cell Metab 23 (5), 821-836 (2016)
   PUBMED   27133129
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Dai,N., Zhao,L., Wrighting,D., Kramer,D., Majithia,A., Wang,Y.,
            Cracan,V., Borges-Rivera,D., Mootha,V.K., Nahrendorf,M.,
            Thorburn,D.R., Minichiello,L., Altshuler,D. and Avruch,J.
  TITLE     IGF2BP2/IMP2-Deficient mice resist obesity through enhanced
            translation of Ucp1 mRNA and Other mRNAs encoding mitochondrial
            proteins
  JOURNAL   Cell Metab 21 (4), 609-621 (2015)
   PUBMED   25863250
REFERENCE   6  (residues 1 to 77)
  AUTHORS   Peralta,S., Torraco,A., Wenz,T., Garcia,S., Diaz,F. and Moraes,C.T.
  TITLE     Partial complex I deficiency due to the CNS conditional ablation of
            Ndufa5 results in a mild chronic encephalopathy but no increase in
            oxidative damage
  JOURNAL   Hum Mol Genet 23 (6), 1399-1412 (2014)
   PUBMED   24154540
  REMARK    GeneRIF: At the age of 11 months, mice with a central nervous
            system knockout of Ndufa5 (Ndufa5 CNS-KO) showed lethargy and loss
            of motor skills. In these mice cortices, the levels of NDUFA5
            protein were reduced to 25% of controls. Fully assembled complex I
            (CI) levels were also greatly reduced in cortex and CI activity in
            homogenates was reduced to 60% of controls.
REFERENCE   7  (residues 1 to 77)
  AUTHORS   Wirtz,S. and Schuelke,M.
  TITLE     Region-specific expression of mitochondrial complex I genes during
            murine brain development
  JOURNAL   PLoS One 6 (4), e18897 (2011)
   PUBMED   21556144
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 77)
  AUTHORS   Shimada,T., Moriuchi,R., Mori,T., Yamada,K., Ishimaru,T. and
            Katamine,S.
  TITLE     Identification of NADH dehydrogenase 1 alpha subcomplex 5 capable
            to transform murine fibroblasts and overexpressed in human cervical
            carcinoma cell lines
  JOURNAL   Biochem Biophys Res Commun 339 (3), 852-857 (2006)
   PUBMED   16329995
  REMARK    GeneRIF: The real-time RT-PCR analysis revealed that the
            expressions of the NDUFA5 mRNA, but not the ZNF9 mRNA level, were
            significantly up-regulated in all the tested cell lines derived
            from HPV-positive cervical cancer, HeLa, SW576, and CaSKi.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC153635.4, BY253904.1, BY247454.1 and W66892.1.
            
            On Jul 22, 2015 this sequence version replaced XP_006505224.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the coding region, compared to variant 1. It encodes
            isoform 2, which lacks an internal segment and is shorter, compared
            to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU563501.1, BU563424.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 11.28 cM"
     Protein         1..77
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 5 isoform 2"
                     /EC_number="7.1.1.2"
                     /EC_number="1.6.99.3"
                     /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
                     subunit 5; complex I-13kD-B; complex I subunit B13;
                     NADH-ubiquinone oxidoreductase 13 kDa-B subunit; NADH
                     dehydrogenase (ubiquinone) 1 alpha subcomplex, 5"
                     /calculated_mol_wt=8554
     CDS             1..77
                     /gene="Ndufa5"
                     /gene_synonym="2900002J19Rik; CI-13kD-B"
                     /coded_by="NM_001311068.2:145..378"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS80494.1"
                     /db_xref="GeneID:68202"
                     /db_xref="MGI:MGI:1915452"
ORIGIN      
        1 magllkkttg lvglavcdtp heepdvkkle allqggevee vilqaekels larkmlkwkp
       61 weplveeppa nqwkwpi
//
LOCUS       NP_995313                 80 aa            linear   PRI 27-APR-2025
DEFINITION  serine protease inhibitor Kazal-type 6 precursor [Homo sapiens].
ACCESSION   NP_995313
VERSION     NP_995313.2
DBSOURCE    REFSEQ: accession NM_205841.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Wang,D., Li,C., Chiu,M.C., Yu,Y., Liu,X., Zhao,X., Huang,J.,
            Cheng,Z., Yuan,S., Poon,V., Cai,J.P., Chu,H., Chan,J.F., To,K.K.,
            Yuen,K.Y. and Zhou,J.
  TITLE     SPINK6 inhibits human airway serine proteases and restricts
            influenza virus activation
  JOURNAL   EMBO Mol Med 14 (1), e14485 (2022)
   PUBMED   34826211
  REMARK    GeneRIF: SPINK6 inhibits human airway serine proteases and
            restricts influenza virus activation.
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Kim,H.J., Shim,J.H., Park,J.H., Shin,H.T., Shim,J.S., Jang,K.T.,
            Park,W.Y., Lee,K.H., Kwon,E.J., Jang,H.S., Yang,H., Lee,J.H.,
            Yang,J.M. and Lee,D.
  TITLE     Single-cell RNA sequencing of human nail unit defines RSPO4
            onychofibroblasts and SPINK6 nail epithelium
  JOURNAL   Commun Biol 4 (1), 692 (2021)
   PUBMED   34099859
  REMARK    GeneRIF: Single-cell RNA sequencing of human nail unit defines
            RSPO4 onychofibroblasts and SPINK6 nail epithelium.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Ge,K., Huang,J., Wang,W., Gu,M., Dai,X., Xu,Y., Wu,H., Li,G.,
            Lu,H., Zhong,J. and Huang,Q.
  TITLE     Serine protease inhibitor kazal-type 6 inhibits tumorigenesis of
            human hepatocellular carcinoma cells via its extracellular action
  JOURNAL   Oncotarget 8 (4), 5965-5975 (2017)
   PUBMED   27999203
  REMARK    GeneRIF: Study showed that the expression of SPINK6 is specifically
            suppressed in liver tumor tissues. The suppression could be even
            detected in the early stage tumors. As SPINK6 is a secretory
            protein, the extracellular protein level may be decreased because
            of tumor development. These results support that SPINK6 is an
            important tumor suppressor in liver.
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Zheng,L.S., Yang,J.P., Cao,Y., Peng,L.X., Sun,R., Xie,P.,
            Wang,M.Y., Meng,D.F., Luo,D.H., Zou,X., Chen,M.Y., Mai,H.Q.,
            Guo,L., Guo,X., Shao,J.Y., Huang,B.J., Zhang,W. and Qian,C.N.
  TITLE     SPINK6 Promotes Metastasis of Nasopharyngeal Carcinoma via Binding
            and Activation of Epithelial Growth Factor Receptor
  JOURNAL   Cancer Res 77 (2), 579-589 (2017)
   PUBMED   27671677
  REMARK    GeneRIF: our results identified a novel EGFR-activating mechanism
            in which SPINK6 has a critical role in promoting nasopharyngeal
            carcinoma metastasis
REFERENCE   5  (residues 1 to 80)
  AUTHORS   Plaza,K., Kalinska,M., Bochenska,O., Meyer-Hoffert,U., Wu,Z.,
            Fischer,J., Falkowski,K., Sasiadek,L., Bielecka,E., Potempa,B.,
            Kozik,A., Potempa,J. and Kantyka,T.
  TITLE     Gingipains of Porphyromonas gingivalis Affect the Stability and
            Function of Serine Protease Inhibitor of Kazal-type 6 (SPINK6), a
            Tissue Inhibitor of Human Kallikreins
  JOURNAL   J Biol Chem 291 (36), 18753-18764 (2016)
   PUBMED   27354280
  REMARK    GeneRIF: a significant fraction of SPINK6-sensitive proteases in
            healthy saliva and confirmed the ability of gingipains to
            inactivate SPINK6 under ex vivo conditions
REFERENCE   6  (residues 1 to 80)
  AUTHORS   Meyer-Hoffert,U., Wu,Z., Kantyka,T., Fischer,J., Latendorf,T.,
            Hansmann,B., Bartels,J., He,Y., Glaser,R. and Schroder,J.M.
  TITLE     Isolation of SPINK6 in human skin: selective inhibitor of
            kallikrein-related peptidases
  JOURNAL   J Biol Chem 285 (42), 32174-32181 (2010)
   PUBMED   20667819
  REMARK    GeneRIF: Data suggest that SPINK6 plays a role in modulating the
            activity of kallikreins in human skin.
REFERENCE   7  (residues 1 to 80)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   8  (residues 1 to 80)
  AUTHORS   Puente,X.S. and Lopez-Otin,C.
  TITLE     A genomic analysis of rat proteases and protease inhibitors
  JOURNAL   Genome Res 14 (4), 609-622 (2004)
   PUBMED   15060002
REFERENCE   9  (residues 1 to 80)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 80)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from GQ504704.1 and AY358716.1.
            
            On Jun 29, 2005 this sequence version replaced NP_995313.1.
            
            Summary: The protein encoded by this gene is a Kazal-type serine
            protease inhibitor that acts on kallikrein-related peptidases in
            the skin. Two transcript variants the same protein have been found
            for this gene. [provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032003.1, BG191133.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325630.3/ ENSP00000324870.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..80
                     /product="serine protease inhibitor Kazal-type 6
                     precursor"
                     /note="protease inhibitor H; serine protease inhibitor
                     Kazal-type 6; acrosin inhibitor; kallikrein inhibitor"
                     /calculated_mol_wt=6064
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2539
     mat_peptide     24..80
                     /product="serine protease inhibitor Kazal-type 6"
                     /calculated_mol_wt=6064
     Site            24
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000250|UniProtKB:P01001; propagated from
                     UniProtKB/Swiss-Prot (Q6UWN8.1)"
     Region          36..80
                     /region_name="Kazal_1"
                     /note="Kazal-type serine protease inhibitor domain;
                     pfam00050"
                     /db_xref="CDD:395004"
     Site            42..43
                     /site_type="other"
                     /note="Reactive bond.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00798; propagated
                     from UniProtKB/Swiss-Prot (Q6UWN8.1)"
     CDS             1..80
                     /gene="SPINK6"
                     /gene_synonym="BUSI2; UNQ844"
                     /coded_by="NM_205841.4:56..298"
                     /db_xref="CCDS:CCDS34268.1"
                     /db_xref="GeneID:404203"
                     /db_xref="HGNC:HGNC:29486"
                     /db_xref="MIM:615868"
ORIGIN      
        1 mklsgmflll slalfcfltg vfsqggqvdc gefqdpkvyc tresnphcgs dgqtygnkca
       61 fckaivksgg kislkhpgkc
//
LOCUS       NP_619579                166 aa            linear   PRI 27-APR-2025
DEFINITION  cofilin-2 isoform 1 [Homo sapiens].
ACCESSION   NP_619579
VERSION     NP_619579.1
DBSOURCE    REFSEQ: accession NM_138638.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Robaszkiewicz,K., Wrobel,J. and Moraczewska,J.
  TITLE     Troponin and a Myopathy-Linked Mutation in TPM3 Inhibit
            Cofilin-2-Induced Thin Filament Depolymerization
  JOURNAL   Int J Mol Sci 24 (22), 16457 (2023)
   PUBMED   38003645
  REMARK    GeneRIF: Troponin and a Myopathy-Linked Mutation in TPM3 Inhibit
            Cofilin-2-Induced Thin Filament Depolymerization.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Kraus,J., Russell,R.W., Kudryashova,E., Xu,C., Katyal,N.,
            Perilla,J.R., Kudryashov,D.S. and Polenova,T.
  TITLE     Magic angle spinning NMR structure of human cofilin-2 assembled on
            actin filaments reveals isoform-specific conformation and binding
            mode
  JOURNAL   Nat Commun 13 (1), 2114 (2022)
   PUBMED   35440100
  REMARK    GeneRIF: Magic angle spinning NMR structure of human cofilin-2
            assembled on actin filaments reveals isoform-specific conformation
            and binding mode.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Zhang,L., Zhang,W., Zuo,Z., Tang,J., Song,Y., Cao,F., Yu,X., Liu,S.
            and Cai,X.
  TITLE     Circ_0008673 regulates breast cancer malignancy by miR-153-3p/CFL2
            axis
  JOURNAL   Arch Gynecol Obstet 305 (1), 223-232 (2022)
   PUBMED   34324029
  REMARK    GeneRIF: Circ_0008673 regulates breast cancer malignancy by
            miR-153-3p/CFL2 axis.
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Bamburg,J.R., McGough,A. and Ono,S.
  TITLE     Putting a new twist on actin: ADF/cofilins modulate actin dynamics
  JOURNAL   Trends Cell Biol 9 (9), 364-370 (1999)
   PUBMED   10461190
  REMARK    Review article
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Yang,N., Higuchi,O., Ohashi,K., Nagata,K., Wada,A., Kangawa,K.,
            Nishida,E. and Mizuno,K.
  TITLE     Cofilin phosphorylation by LIM-kinase 1 and its role in
            Rac-mediated actin reorganization
  JOURNAL   Nature 393 (6687), 809-812 (1998)
   PUBMED   9655398
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Nebl,G., Meuer,S.C. and Samstag,Y.
  TITLE     Dephosphorylation of serine 3 regulates nuclear translocation of
            cofilin
  JOURNAL   J Biol Chem 271 (42), 26276-26280 (1996)
   PUBMED   8824278
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Gillett,G.T., Fox,M.F., Rowe,P.S., Casimir,C.M. and Povey,S.
  TITLE     Mapping of human non-muscle type cofilin (CFL1) to chromosome 11q13
            and muscle-type cofilin (CFL2) to chromosome 14
  JOURNAL   Ann Hum Genet 60 (3), 201-211 (1996)
   PUBMED   8800436
REFERENCE   10 (residues 1 to 166)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC022364.1, AL355885.4 and
            DB378917.1.
            
            Summary: This gene encodes an intracellular protein that is
            involved in the regulation of actin-filament dynamics. This protein
            is a major component of intranuclear and cytoplasmic actin rods. It
            can bind G- and F-actin in a 1:1 ratio of cofilin to actin, and it
            reversibly controls actin polymerization and depolymerization in a
            pH-dependent manner. Mutations in this gene cause nemaline myopathy
            type 7, a form of congenital myopathy. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Jul 2009].
            
            Transcript Variant: This variant (2) encodes the longer isoform
            (1). Both variants 1 and 2 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.372399.1,
                                           SRR14038191.3614043.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298159.11/ ENSP00000298159.6
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..166
                     /product="cofilin-2 isoform 1"
                     /note="nemaline myopathy type 7; cofilin 2 (muscle)"
                     /calculated_mol_wt=18606
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:37316325; propagated from
                     UniProtKB/Swiss-Prot (Q9Y281.1)"
     Region          2..55
                     /region_name="Interaction with CSRP3.
                     /evidence=ECO:0000269|PubMed:19752190"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y281.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:37316325, ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9Y281.1)"
     Region          3..153
                     /region_name="ADF_cofilin_like"
                     /note="Cofilin, Destrin, and related actin depolymerizing
                     factors; cd11286"
                     /db_xref="CDD:200442"
     Site            3..4
                     /site_type="other"
                     /note="putative G-actin interface [polypeptide binding]"
                     /db_xref="CDD:200442"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9Y281.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P45591; propagated from
                     UniProtKB/Swiss-Prot (Q9Y281.1)"
     Region          30..34
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y281.1)"
     Region          55..105
                     /region_name="Interaction with CSRP3.
                     /evidence=ECO:0000269|PubMed:19752190"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y281.1)"
     Site            order(96,98,112,139,142)
                     /site_type="other"
                     /note="putative F-actin interface [polypeptide binding]"
                     /db_xref="CDD:200442"
     CDS             1..166
                     /gene="CFL2"
                     /gene_synonym="NEM7"
                     /coded_by="NM_138638.5:54..554"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9649.1"
                     /db_xref="GeneID:1073"
                     /db_xref="HGNC:HGNC:1875"
                     /db_xref="MIM:601443"
ORIGIN      
        1 masgvtvnde vikvfndmkv rksstqeeik krkkavlfcl sddkrqiive eakqilvgdi
       61 gdtvedpyts fvkllplndc ryalydatye tkeskkedlv fifwapesap lkskmiyass
      121 kdaikkkftg ikhewqvngl ddikdrstlg eklggnvvvs legkpl
//
LOCUS       NP_005484                729 aa            linear   PRI 27-APR-2025
DEFINITION  ran-binding protein 9 [Homo sapiens].
ACCESSION   NP_005484
VERSION     NP_005484.2
DBSOURCE    REFSEQ: accession NM_005493.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Deng,T., Xie,L., Xiaofang,C., Zhang,Z., Xiao,Y., Peng,Y., Yin,L.,
            Fu,Y. and Li,X.
  TITLE     ATM-Mediated translocation of RanBPM regulates DNA damage response
            by stabilizing p21 in non-small cell lung cancer cells
  JOURNAL   Cell Oncol (Dordr) 47 (1), 245-258 (2024)
   PUBMED   37676377
  REMARK    GeneRIF: ATM-Mediated translocation of RanBPM regulates DNA damage
            response by stabilizing p21 in non-small cell lung cancer cells.
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Tessari,A., Parbhoo,K., Pawlikowski,M., Fassan,M., Rulli,E.,
            Foray,C., Fabbri,A., Embrione,V., Ganzinelli,M., Capece,M.,
            Campbell,M.J., Broggini,M., La Perle,K., Farina,G., Cole,S.,
            Marabese,M., Hernandez,M., Amann,J.M., Pruneri,G., Carbone,D.P.,
            Garassino,M.C., Croce,C.M., Palmieri,D. and Coppola,V.
  TITLE     RANBP9 affects cancer cells response to genotoxic stress and its
            overexpression is associated with worse response to platinum in
            NSCLC patients
  JOURNAL   Oncogene 37 (50), 6463-6476 (2018)
   PUBMED   30076413
  REMARK    GeneRIF: the present study provides preclinical and clinical data
            indicating that lower RANBP9 protein levels might be used, after
            perspective validation, as a biomarker predictive of response of
            non-small cell lung cancer to platinum based compounds
REFERENCE   5  (residues 1 to 729)
  AUTHORS   Lampert,F., Stafa,D., Goga,A., Soste,M.V., Gilberto,S., Olieric,N.,
            Picotti,P., Stoffel,M. and Peter,M.
  TITLE     The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell
            proliferation and targets the transcription factor Hbp1 for
            degradation
  JOURNAL   Elife 7, e35528 (2018)
   PUBMED   29911972
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 729)
  AUTHORS   Ideguchi,H., Ueda,A., Tanaka,M., Yang,J., Tsuji,T., Ohno,S.,
            Hagiwara,E., Aoki,A. and Ishigatsubo,Y.
  TITLE     Structural and functional characterization of the USP11
            deubiquitinating enzyme, which interacts with the RanGTP-associated
            protein RanBPM
  JOURNAL   Biochem J 367 (Pt 1), 87-95 (2002)
   PUBMED   12084015
  REMARK    GeneRIF: RanBPM is the enzymic substrate for USP11 and is
            deubiquitinated specifically
REFERENCE   7  (residues 1 to 729)
  AUTHORS   Caballero,O.L., Resto,V., Patturajan,M., Meerzaman,D., Guo,M.Z.,
            Engles,J., Yochem,R., Ratovitski,E., Sidransky,D. and Jen,J.
  TITLE     Interaction and colocalization of PGP9.5 with JAB1 and p27(Kip1)
  JOURNAL   Oncogene 21 (19), 3003-3010 (2002)
   PUBMED   12082530
REFERENCE   8  (residues 1 to 729)
  AUTHORS   Nishitani,H., Hirose,E., Uchimura,Y., Nakamura,M., Umeda,M.,
            Nishii,K., Mori,N. and Nishimoto,T.
  TITLE     Full-sized RanBPM cDNA encodes a protein possessing a long stretch
            of proline and glutamine within the N-terminal region, comprising a
            large protein complex
  JOURNAL   Gene 272 (1-2), 25-33 (2001)
   PUBMED   11470507
REFERENCE   9  (residues 1 to 729)
  AUTHORS   Nishimoto,T.
  TITLE     A new role of ran GTPase
  JOURNAL   Biochem Biophys Res Commun 262 (3), 571-574 (1999)
   PUBMED   10471364
  REMARK    Review article
REFERENCE   10 (residues 1 to 729)
  AUTHORS   Nakamura,M., Masuda,H., Horii,J., Kuma,Ki., Yokoyama,N., Ohba,T.,
            Nishitani,H., Miyata,T., Tanaka,M. and Nishimoto,T.
  TITLE     When overexpressed, a novel centrosomal protein, RanBPM, causes
            ectopic microtubule nucleation similar to gamma-tubulin
  JOURNAL   J Cell Biol 143 (4), 1041-1052 (1998)
   PUBMED   9817760
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z93020.1, AB055311.1,
            BC052781.1 and AF306510.1.
            
            On Dec 12, 2003 this sequence version replaced NP_005484.1.
            
            Summary: This gene encodes a protein that binds RAN, a small GTP
            binding protein belonging to the RAS superfamily that is essential
            for the translocation of RNA and proteins through the nuclear pore
            complex. The protein encoded by this gene has also been shown to
            interact with several other proteins, including met proto-oncogene,
            homeodomain interacting protein kinase 2, androgen receptor, and
            cyclin-dependent kinase 11. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF306510.1, BC052781.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000011619.6/ ENSP00000011619.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p23"
     Protein         1..729
                     /product="ran-binding protein 9"
                     /note="novel centrosomal protein RanBPM; ran binding
                     protein, centrosomal; Ran Binding Protein in the
                     Microtubule organizing center; ran-binding protein M"
                     /calculated_mol_wt=77717
     Region          1..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S59.1)"
     Region          189..331
                     /region_name="SPRY_RanBP9_10"
                     /note="SPRY domain in Ran binding proteins 9 and 10;
                     cd12909"
                     /db_xref="CDD:293966"
     Region          364..397
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          401..407
                     /region_name="Interaction with CALB1.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S59.1)"
     Region          403..>457
                     /region_name="CTLH"
                     /note="CTLH/CRA C-terminal to LisH motif domain;
                     pfam10607"
                     /db_xref="CDD:402305"
     Site            405
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96S59.1)"
     Region          461..489
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S59.1)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P69566; propagated from
                     UniProtKB/Swiss-Prot (Q96S59.1)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96S59.1)"
     Region          615..729
                     /region_name="Interaction with FMR1.
                     /evidence=ECO:0000269|PubMed:15381419"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S59.1)"
     Region          616..708
                     /region_name="CRA"
                     /note="CT11-RanBPM; smart00757"
                     /db_xref="CDD:214806"
     CDS             1..729
                     /gene="RANBP9"
                     /gene_synonym="BPM-L; BPM90; RanBP7; RANBPM"
                     /coded_by="NM_005493.3:331..2520"
                     /db_xref="CCDS:CCDS4529.1"
                     /db_xref="GeneID:10048"
                     /db_xref="HGNC:HGNC:13727"
                     /db_xref="MIM:603854"
ORIGIN      
        1 msgqpppppp qqqqqqqqls ppppaalapv sgvvlpappa vsagsspags pgggaggegl
       61 gaaaaalllh pppppppata appppppppp ppasaaapas gppappglaa gpgpaggapt
      121 palvagssaa apfphgdsal neqekelqrr lkrlypavde qetplprsws pkdkfsyigl
      181 sqnnlrvhyk ghgktpkdaa svrathpipa acgiyyfevk ivskgrdgym giglsaqgvn
      241 mnrlpgwdkh sygyhgddgh sfcssgtgqp ygptfttgdv igccvnlinn tcfytknghs
      301 lgiaftdlpp nlyptvglqt pgevvdanfg qhpfvfdied ymrewrtkiq aqidrfpigd
      361 regewqtmiq kmvssylvhh gycataeafa rstdqtvlee lasiknrqri qklvlagrmg
      421 eaiettqqly psllernpnl lftlkvrqfi emvngtdsev rclggrspks qdsypvsprp
      481 fsspsmspsh gmnihnlasg kgstahfsgf escsngvisn kahqsychsn khqssnlnvp
      541 elnsinmsrs qqvnnftsnd vdmetdhysn gvgetssngf lngsskhdhe medcdtemev
      601 dssqlrrqlc ggsqaaierm ihfgrelqam seqlrrdcgk ntankkmlkd afsllaysdp
      661 wnspvgnqld piqrepvcsa lnsailethn lpkqpplala mgqatqclgl marsgigsca
      721 fatvedylh
//
LOCUS       NP_006351                374 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 3 subunit M isoform 1
            [Homo sapiens].
ACCESSION   NP_006351
VERSION     NP_006351.2
DBSOURCE    REFSEQ: accession NM_006360.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Lee,A.S., Kranzusch,P.J. and Cate,J.H.
  TITLE     eIF3 targets cell-proliferation messenger RNAs for translational
            activation or repression
  JOURNAL   Nature 522 (7554), 111-114 (2015)
   PUBMED   25849773
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Hinnebusch,A.G.
  TITLE     eIF3: a versatile scaffold for translation initiation complexes
  JOURNAL   Trends Biochem Sci 31 (10), 553-562 (2006)
   PUBMED   16920360
  REMARK    Review article
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   8  (residues 1 to 374)
  AUTHORS   Perez-Romero,P. and Fuller,A.O.
  TITLE     The C terminus of the B5 receptor for herpes simplex virus contains
            a functional region important for infection
  JOURNAL   J Virol 79 (12), 7431-7437 (2005)
   PUBMED   15919899
  REMARK    GeneRIF: Concluded that the C terminus of B5 contains a functional
            region that is important for the B5 receptor to mediate events in
            HSV entry.
REFERENCE   9  (residues 1 to 374)
  AUTHORS   Perez,A., Li,Q.X., Perez-Romero,P., Delassus,G., Lopez,S.R.,
            Sutter,S., McLaren,N. and Fuller,A.O.
  TITLE     A new class of receptor for herpes simplex virus has heptad repeat
            motifs that are common to membrane fusion proteins
  JOURNAL   J Virol 79 (12), 7419-7430 (2005)
   PUBMED   15919898
  REMARK    GeneRIF: Cloned a previously uncharacterized human gene, designated
            hfl-B5, and showed that it encodes a type II cell surface membrane
            protein that can serve as a receptor for entry of HSV.
REFERENCE   10 (residues 1 to 374)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB479224.1, BC019103.2, AK304378.1, BE935691.1, CK002866.1 and
            AL078477.5.
            
            On Oct 1, 2002 this sequence version replaced NP_006351.1.
            
            Summary: This gene encodes a protein that is part of the
            eurkaryotic translation initiation factor 3 complete (eIF-3)
            required for protein synthesis. Elevated levels of the encoded
            protein are present in cancer cell lines. Inactivation of the
            encoded protein has been shown to interfere with translation of
            herpes virus mRNAs by preventing the association of mRNAs with the
            ribosomes. A pseudogene of this gene is located on the X
            chromosome. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.234014.1,
                                           SRR1803611.13609.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000531120.6/ ENSP00000436049.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..374
                     /product="eukaryotic translation initiation factor 3
                     subunit M isoform 1"
                     /EC_number="3.6.5.3"
                     /note="dendritic cell protein; PCI domain containing 1
                     (herpesvirus entry mediator); fetal lung protein B5; B5
                     receptor; PCI domain-containing protein 1; transport and
                     golgi organization 7 homolog"
                     /calculated_mol_wt=42372
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03012,
                     ECO:0000269|PubMed:17322308, ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7L2H7.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L2H7.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L2H7.1)"
     Site            254
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7L2H7.1)"
     Region          269..357
                     /region_name="PINT"
                     /note="motif in proteasome subunits, Int-6, Nip-1 and
                     TRIP-15; smart00088"
                     /db_xref="CDD:214509"
     Region          344..374
                     /region_name="Interaction with HSV-1 and HSV-2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L2H7.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L2H7.1)"
     CDS             1..374
                     /gene="EIF3M"
                     /gene_synonym="B5; GA17; hfl-B5; PCID1; TANGO7"
                     /coded_by="NM_006360.6:58..1182"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7880.1"
                     /db_xref="GeneID:10480"
                     /db_xref="HGNC:HGNC:24460"
                     /db_xref="MIM:609641"
ORIGIN      
        1 msvpafidis eedqaaelra ylkskgaeis eensegglhv dlaqiieacd vclkeddkdv
       61 esvmnsvvsl llilepdkqe alieslcekl vkfregerps lrlqllsnlf hgmdkntpvr
      121 ytvycslikv aascgaiqyi pteldqvrkw isdwnlttek khtllrllye alvdckksda
      181 askvmvellg sytednasqa rvdahrcivr alkdpnaflf dhlltlkpvk flegelihdl
      241 ltifvsakla syvkfyqnnk dfidslgllh eqnmakmrll tfmgmavenk eisfdtmqqe
      301 lqigaddvea fvidavrtkm vyckidqtqr kvvvshsthr tfgkqqwqql ydtlnawkqn
      361 lnkvknslls lsdt
//
LOCUS       NP_001357438             225 aa            linear   PRI 27-APR-2025
DEFINITION  phosphoserine phosphatase [Homo sapiens].
ACCESSION   NP_001357438
VERSION     NP_001357438.1
DBSOURCE    REFSEQ: accession NM_001370509.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Rawat,V., Malvi,P., Della Manna,D., Yang,E.S., Bugide,S., Zhang,X.,
            Gupta,R. and Wajapeyee,N.
  TITLE     PSPH promotes melanoma growth and metastasis by metabolic
            deregulation-mediated transcriptional activation of NR4A1
  JOURNAL   Oncogene 40 (13), 2448-2462 (2021)
   PUBMED   33674745
  REMARK    GeneRIF: PSPH promotes melanoma growth and metastasis by metabolic
            deregulation-mediated transcriptional activation of NR4A1.
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Park,S.M., Seo,E.H., Bae,D.H., Kim,S.S., Kim,J., Lin,W., Kim,K.H.,
            Park,J.B., Kim,Y.S., Yin,J. and Kim,S.Y.
  TITLE     Phosphoserine Phosphatase Promotes Lung Cancer Progression through
            the Dephosphorylation of IRS-1 and a Noncanonical
            L-Serine-Independent Pathway
  JOURNAL   Mol Cells 42 (8), 604-616 (2019)
   PUBMED   31446747
  REMARK    GeneRIF: a specific interaction between PSPH and IRS1 and the
            dephosphorylation of phospho-IRS-1 by PSPH in lung cancer cells,
            was identified.
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Haufroid,M., Mirgaux,M., Leherte,L. and Wouters,J.
  TITLE     Crystal structures and snapshots along the reaction pathway of
            human phosphoserine phosphatase
  JOURNAL   Acta Crystallogr D Struct Biol 75 (Pt 6), 592-604 (2019)
   PUBMED   31205021
  REMARK    GeneRIF: three new high-resolution crystal structures of hPSP
            (1.5-2.0 A) in complexes with phosphoserine and with serine, which
            are the substrate and the product of the reaction, respectively,
            and in complex with a noncleavable substrate analogue (homocysteic
            acid) are presented.
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Liao,L., Ge,M., Zhan,Q., Huang,R., Ji,X., Liang,X. and Zhou,X.
  TITLE     PSPH Mediates the Metastasis and Proliferation of Non-small Cell
            Lung Cancer through MAPK Signaling Pathways
  JOURNAL   Int J Biol Sci 15 (1), 183-194 (2019)
   PUBMED   30662358
  REMARK    GeneRIF: The results suggest that PSPH may act as a putative
            oncogene and a potential therapeutic target in NSCLC.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 225)
  AUTHORS   van der Crabben,S.N. and de Koning,T.J.
  TITLE     Serine Deficiency Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37347880
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Veeranna and Shetty,K.T.
  TITLE     Phosphoserine phosphatase of human brain: partial purification,
            characterization, regional distribution, and effect of certain
            modulators including psychoactive drugs
  JOURNAL   Neurochem Res 15 (12), 1203-1210 (1990)
   PUBMED   1965857
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Minelli,A., Piantanida,M., Maserati,E., Campagnoli,E., Pasquali,F.
            and Danesino,C.
  TITLE     Gene dosage effect in acquired monosomy 7: distinct behaviour of
            beta-glucuronidase and phosphoserine phosphatase
  JOURNAL   Genes Chromosomes Cancer 1 (3), 216-220 (1990)
   PUBMED   1964582
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Novelli,G. and Dallapiccola,B.
  TITLE     Gene dosage studies regionally assign the phosphoserine phosphatase
            gene to 7p15.1 or 2
  JOURNAL   Ann Genet 31 (3), 195-196 (1988)
   PUBMED   2851960
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Moro-Furlani,A.M., Turner,V.S. and Hopkinson,D.A.
  TITLE     Genetical and biochemical studies on human phosphoserine
            phosphatase
  JOURNAL   Ann Hum Genet 43 (4), 323-333 (1980)
   PUBMED   6249179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092579.3.
            
            Summary: The protein encoded by this gene belongs to a subfamily of
            the phosphotransferases. This encoded enzyme is responsible for the
            third and last step in L-serine formation. It catalyzes
            magnesium-dependent hydrolysis of L-phosphoserine and is also
            involved in an exchange reaction between L-serine and
            L-phosphoserine. Deficiency of this protein is thought to be linked
            to Williams syndrome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.442558.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p11.2"
     Protein         1..225
                     /product="phosphoserine phosphatase"
                     /EC_number="3.1.3.3"
                     /note="L-3-phosphoserine phosphatase; O-phosphoserine
                     phosphohydrolase; PSPase"
                     /calculated_mol_wt=24877
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P78330.2)"
     Region          15..216
                     /region_name="HAD_PSP_eu"
                     /note="phosphoserine phosphatase eukaryotic-like, similar
                     to human phosphoserine phosphatase; cd04309"
                     /db_xref="CDD:319801"
     Site            order(20..24,29,109..110,158,178..179,182..183)
                     /site_type="active"
                     /db_xref="CDD:319801"
     CDS             1..225
                     /gene="PSPH"
                     /gene_synonym="PSP; PSPHD"
                     /coded_by="NM_001370509.1:437..1114"
                     /db_xref="CCDS:CCDS5522.1"
                     /db_xref="GeneID:5723"
                     /db_xref="HGNC:HGNC:9577"
                     /db_xref="MIM:172480"
ORIGIN      
        1 mvshselrkl fysadavcfd vdstvireeg idelakicgv edavsemtrr amggavpfka
       61 alterlaliq psreqvqrli aeqpphltpg irelvsrlqe rnvqvflisg gfrsivehva
      121 sklnipatnv fanrlkfyfn geyagfdetq ptaesggkgk vikllkekfh fkkiimigdg
      181 atdmeacppa dafigfggnv irqqvkdnak wyitdfvell gelee
//
LOCUS       NP_056509                831 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 777 [Homo sapiens].
ACCESSION   NP_056509
VERSION     NP_056509.2
DBSOURCE    REFSEQ: accession NM_015694.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 831)
  AUTHORS   Al Chiblak,M., Steinbeck,F., Thiesen,H.J. and Lorenz,P.
  TITLE     DUF3669, a 'domain of unknown function' within ZNF746 and ZNF777,
            oligomerizes and contributes to transcriptional repression
  JOURNAL   BMC Mol Cell Biol 20 (1), 60 (2019)
   PUBMED   31856708
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 831)
  AUTHORS   Yuki,R., Aoyama,K., Kubota,S., Yamaguchi,N., Kubota,S.,
            Hasegawa,H., Morii,M., Huang,X., Liu,K., Williams,R., Fukuda,M.N.
            and Yamaguchi,N.
  TITLE     Overexpression of zinc-finger protein 777 (ZNF777) inhibits
            proliferation at low cell density through down-regulation of
            FAM129A
  JOURNAL   J Cell Biochem 116 (6), 954-968 (2015)
   PUBMED   25560148
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073314.4, DR763452.1, BX444270.2, AB033111.1 and BC023985.2.
            
            On Dec 7, 2006 this sequence version replaced NP_056509.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247930.5/ ENSP00000247930.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..831
                     /product="zinc finger protein 777"
                     /calculated_mol_wt=93631
     Region          1..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Region          <7..>165
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Region          285..343
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          339..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Region          398..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Region          488..545
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Region          546..568
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          548..568
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          576..596
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          600..634
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Site            623
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULD5.3)"
     Region          638..658
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <640..826
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          669..686
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          696..716
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(701,703,705,707..708,711..712,715,729,731,735..736,
                     739..740,743,757,759,761,763..764,767..768,771)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          724..744
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          752..772
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          780..800
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          808..828
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..831
                     /gene="ZNF777"
                     /coded_by="NM_015694.3:264..2759"
                     /db_xref="CCDS:CCDS43675.1"
                     /db_xref="GeneID:27153"
                     /db_xref="HGNC:HGNC:22213"
                     /db_xref="MIM:619298"
ORIGIN      
        1 menqrsspls fpsvpqeetl rqapaglpre tlfqsrvlpp keipslspti prqgslpqts
       61 sapkqetsgr mphvlqkgps llcsaaseqe tslqgplasq egtqypppaa aeqevsllsh
      121 sphhqeapvh speapekdpl tlsptvpetd mdpllqspvs qkdtpfqiss avqkeqplpt
      181 aeitrlavwa avqaverkle aqamrlltle grtgtnekki adcektavef anhleskwvv
      241 lgtllqeygl lqrrlenmen llknrnfwil rlppgsngev pkvpvtfddv avhfseqewg
      301 nlsewqkely knvmrgnyes lvsmdyaisk pdlmsqmerg erptmqeqed seegetptdp
      361 saahdgivik ievqtndegs esletpeplm gqveehgfqd selgdpcgeq pdldmqepen
      421 tleestegss efselkqmlv qqrnctegiv ikteeqdeee eeeeedelpq hlqslgqlsg
      481 ryeasmyqtp lpgemspege esppplqlgn pavkrlapsv hgerhlsenr gassqqqrnr
      541 rgerpftcme cgksfrlkin liihqrnhik egpyecaece isfrhkqqlt lhqrihrvrg
      601 gcvspergpt fnpkhalkpr pkspssgsgg ggpkpykcpe cdssfshkss ltkhqithtg
      661 erpytcpeck ksfrlhislv ihqrvhagkh evsficslcg ksfsrpshll rhqrthtger
      721 pfkcpeceks fsekskltnh crvhsrerph acpecgksfi rkhhllehrr ihtgerpyhc
      781 aecgkrftqk hhllehqrah tgerpypcth cakcfrykqs lkyhlrthtg e
//
LOCUS       NP_001357465             715 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RFWD3 isoform 2 [Homo sapiens].
ACCESSION   NP_001357465 XP_016878881
VERSION     NP_001357465.1
DBSOURCE    REFSEQ: accession NM_001370536.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Moore,C.E., Yalcindag,S.E., Czeladko,H., Ravindranathan,R.,
            Wijesekara Hanthi,Y., Levy,J.C., Sannino,V., Schindler,D.,
            Ciccia,A., Costanzo,V. and Elia,A.E.H.
  TITLE     RFWD3 promotes ZRANB3 recruitment to regulate the remodeling of
            stalled replication forks
  JOURNAL   J Cell Biol 222 (5) (2023)
   PUBMED   37036693
  REMARK    GeneRIF: RFWD3 promotes ZRANB3 recruitment to regulate the
            remodeling of stalled replication forks.
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Zhu,Y., Peng,X., Wang,X., Ying,P., Wang,H., Li,B., Li,Y., Zhang,M.,
            Cai,Y., Lu,Z., Niu,S., Yang,N., Zhong,R., Tian,J., Chang,J. and
            Miao,X.
  TITLE     Systematic analysis on expression quantitative trait loci
            identifies a novel regulatory variant in ring finger and WD repeat
            domain 3 associated with prognosis of pancreatic cancer
  JOURNAL   Chin Med J (Engl) 135 (11), 1348-1357 (2022)
   PUBMED   35830250
  REMARK    GeneRIF: Systematic analysis on expression quantitative trait loci
            identifies a novel regulatory variant in ring finger and WD repeat
            domain 3 associated with prognosis of pancreatic cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Gallina,I., Hendriks,I.A., Hoffmann,S., Larsen,N.B., Johansen,J.,
            Colding-Christensen,C.S., Schubert,L., Selles-Baiget,S., Fabian,Z.,
            Kuhbacher,U., Gao,A.O., Raschle,M., Rasmussen,S., Nielsen,M.L.,
            Mailand,N. and Duxin,J.P.
  TITLE     The ubiquitin ligase RFWD3 is required for translesion DNA
            synthesis
  JOURNAL   Mol Cell 81 (3), 442-458 (2021)
   PUBMED   33321094
  REMARK    GeneRIF: The ubiquitin ligase RFWD3 is required for translesion DNA
            synthesis.
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Hsu,R.Y.C., Giri,S., Wang,Y., Lin,Y.C., Liu,D., Wopat,S.,
            Chakraborty,A., Prasanth,K.V. and Prasanth,S.G.
  TITLE     The E3 ligase RFWD3 stabilizes ORC in a p53-dependent manner
  JOURNAL   Cell Cycle 19 (21), 2927-2938 (2020)
   PUBMED   33044890
  REMARK    GeneRIF: The E3 ligase RFWD3 stabilizes ORC in a p53-dependent
            manner.
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Jia,J., Yang,Y., Yan,T., Chen,T. and Lu,G.
  TITLE     Down-regulation of RFWD3 inhibits cancer cells proliferation and
            migration in gastric carcinoma
  JOURNAL   Gen Physiol Biophys 39 (4), 363-371 (2020)
   PUBMED   32902405
  REMARK    GeneRIF: Down-regulation of RFWD3 inhibits cancer cells
            proliferation and migration in gastric carcinoma.
REFERENCE   6  (residues 1 to 715)
  AUTHORS   Dastani,Z., Pajukanta,P., Marcil,M., Rudzicz,N., Ruel,I.,
            Bailey,S.D., Lee,J.C., Lemire,M., Faith,J., Platko,J., Rioux,J.,
            Hudson,T.J., Gaudet,D., Engert,J.C. and Genest,J.
  TITLE     Fine mapping and association studies of a high-density lipoprotein
            cholesterol linkage region on chromosome 16 in French-Canadian
            subjects
  JOURNAL   Eur J Hum Genet 18 (3), 342-347 (2010)
   PUBMED   19844255
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 715)
  AUTHORS   Markson,G., Kiel,C., Hyde,R., Brown,S., Charalabous,P., Bremm,A.,
            Semple,J., Woodsmith,J., Duley,S., Salehi-Ashtiani,K., Vidal,M.,
            Komander,D., Serrano,L., Lehner,P. and Sanderson,C.M.
  TITLE     Analysis of the human E2 ubiquitin conjugating enzyme protein
            interaction network
  JOURNAL   Genome Res 19 (10), 1905-1911 (2009)
   PUBMED   19549727
REFERENCE   8  (residues 1 to 715)
  AUTHORS   van Wijk,S.J., de Vries,S.J., Kemmeren,P., Huang,A., Boelens,R.,
            Bonvin,A.M. and Timmers,H.T.
  TITLE     A comprehensive framework of E2-RING E3 interactions of the human
            ubiquitin-proteasome system
  JOURNAL   Mol Syst Biol 5, 295 (2009)
   PUBMED   19690564
  REMARK    Erratum:[Mol Syst Biol. 2009;5:317]
REFERENCE   9  (residues 1 to 715)
  AUTHORS   Tsuritani,K., Irie,T., Yamashita,R., Sakakibara,Y., Wakaguri,H.,
            Kanai,A., Mizushima-Sugano,J., Sugano,S., Nakai,K. and Suzuki,Y.
  TITLE     Distinct class of putative 'non-conserved' promoters in humans:
            comparative studies of alternative promoters of human and mouse
            genes
  JOURNAL   Genome Res 17 (7), 1005-1014 (2007)
   PUBMED   17567985
REFERENCE   10 (residues 1 to 715)
  AUTHORS   Mehta,P.A. and Ebens,C.
  TITLE     Fanconi Anemia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC109599.4.
            
            On May 9, 2019 this sequence version replaced XP_016878881.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.31049.1,
                                           SRR1803613.79167.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..715
                     /product="E3 ubiquitin-protein ligase RFWD3 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="RING finger and WD repeat domain-containing protein
                     3; E3 ubiquitin-protein ligase RFWD3; RING finger protein
                     201; RING-type E3 ubiquitin transferase RFWD3"
                     /calculated_mol_wt=78458
     Region          283..343
                     /region_name="mRING-C3HGC3_RFWD3"
                     /note="Modified RING finger, C3HGC3-type, found in RING
                     finger and WD repeat domain-containing protein 3 (RFWD3)
                     and similar proteins; cd16450"
                     /db_xref="CDD:438114"
     CDS             1..715
                     /gene="RFWD3"
                     /gene_synonym="FANCW; RNF201"
                     /coded_by="NM_001370536.1:95..2242"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:55159"
                     /db_xref="HGNC:HGNC:25539"
                     /db_xref="MIM:614151"
ORIGIN      
        1 maheameydv qvqlnhaeqq papagmassq ggpallqpvp advvssqgvp silqpapaev
       61 issqatppll qpapqlsvdl tevevlgedt veninprtse qhrqgsdgnh tipasslhsm
      121 tnfisglqrl hgmleflrps ssnhsvgpmr trrrvsasrr araggsqrtd sarlraplda
      181 yfqvsrtqpd lpattydset rnpvseelqv ssssdsdsds saeyggvvdq aeesgavile
      241 eqlagvsaeq evtcidggkt lpkqpspqks epllpsasmd eeegdtctic leqwtnagdh
      301 rlsalrcghl fgyrcistwl kgqvrkcpqc nkkarhsdiv vlyartlral dtseqermks
      361 sllkeqmlrk qaelesaqcr lqlqvltdkc trlqrrvqdl qkltshqsqn lqqprgsqaw
      421 vlscspssqg qhkhkyhfqk tftvsqagnc rimaycdals clvisqpspq asflpgfgvk
      481 mlstanmkss qyipmhgkqi rglafssylr glllsasldn tikltrcplv slsympraas
      541 aafpyggvla gtledasfwe qkmdfshwph vlplepggci dfqtenssrh clvtyrpdkn
      601 httirsvlme msyrlddtgn picscqpvht ffggptckll tknaifqspe ndgnilvctg
      661 deaansallw daasgsllqd lqtdqpvldi cpfevnrnsy latltekmvh iykwe
//
LOCUS       NP_001348964             808 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 13 [Mus musculus].
ACCESSION   NP_001348964
VERSION     NP_001348964.1
DBSOURCE    REFSEQ: accession NM_001362035.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 808)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 808)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 808)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 808)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 808)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 808)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 808)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            Transcript Variant: This variant (45), as well as variant 44,
            encodes isoform 13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164131
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..808
                     /product="cAMP-regulated phosphoprotein 21 isoform 13"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=87922
     Region          162..223
                     /region_name="R3H_encore_like"
                     /note="R3H domain of encore-like and DIP1-like proteins.
                     Drosophila encore is involved in the germline exit after
                     four mitotic divisions, by facilitating
                     SCF-ubiquitin-proteasome-dependent proteolysis. Maize
                     DBF1-interactor protein 1 (DIP1) containing an R3H...;
                     cd02642"
                     /db_xref="CDD:100071"
     Site            order(195,199)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100071"
     Region          554..>783
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..808
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362035.1:474..2900"
                     /note="isoform 13 is encoded by transcript variant 45"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqesih lqlssfpslq eedksrkdds erekekdknr
      121 eklserpkir mlskdcsqey tdstgidlhg flintlknns rdrmillkme qemidfiads
      181 nnhykkfpqm ssyqrmlvhr vaayfgldhn vdqtgksvii nktsstripe qrfcehlkde
      241 kseesqkrfi lkrdnssidk ednqsvcsqe slfldnrlqe dmhicnetyk krqlfrahrd
      301 ssgrtsgsrq sssetelrwp dhqrawsstd sdssnrnlkp tmtktasfgg itvltrgdst
      361 sstrsagkls ktgsessssa gssgslsrth pqstaltssv aagspgcmay sengmggqvp
      421 psstsyillp lesatgippg sillnphtgq pfvnpdgtpa iynppgsqqt lrgtvggqpq
      481 qppqqqpspq pqqqvqasqp qmagplvtqs vqslqpssqs vqypavsfpp qhllpmsptq
      541 hfplreelaa qfsqlsmsrq ssgdtpepps gtvypasllp qtaqpqsyvi tsagqqlstg
      601 gfsdsgppis qqvlqappsp qgfvqqpppa qmsvyyypsg qyptstsqqy rplasvqysa
      661 qrsqqipqtt qqagyqpvls gqqgfqgmmg vqqsahsqgv mssqqgapvh gvmvsyptms
      721 syqvpmtqgs qavpqqtyqp pimlpsqagq gslpatgmpv ycnvtppnpq nnlrlmgphc
      781 psstvpvmsa scrtncgnvs nagwqvkf
//
LOCUS       NP_848597                347 aa            linear   PRI 27-APR-2025
DEFINITION  probable E3 ubiquitin-protein ligase DTX3 isoform a [Homo sapiens].
ACCESSION   NP_848597
VERSION     NP_848597.1
DBSOURCE    REFSEQ: accession NM_178502.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Scalia,P., Merali,C., Barrero,C., Suma,A., Carnevale,V., Merali,S.
            and Williams,S.J.
  TITLE     Novel Isoform DTX3c Associates with UBE2N-UBA1 and Cdc48/p97 as
            Part of the EphB4 Degradation Complex Regulated by the Autocrine
            IGF-II/IRA Signal in Malignant Mesothelioma
  JOURNAL   Int J Mol Sci 24 (8), 7380 (2023)
   PUBMED   37108544
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Hu,W., Hu,Y., Pei,Y., Li,R., Xu,F., Chi,X., Mi,J., Bergquist,J.,
            Lu,L., Zhang,L. and Yang,C.
  TITLE     Silencing DTX3L Inhibits the Progression of Cervical Carcinoma by
            Regulating PI3K/AKT/mTOR Signaling Pathway
  JOURNAL   Int J Mol Sci 24 (1), 861 (2023)
   PUBMED   36614304
  REMARK    GeneRIF: Silencing DTX3L Inhibits the Progression of Cervical
            Carcinoma by Regulating PI3K/AKT/mTOR Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Valla,M., Opdahl,S., Ytterhus,B. and Bofin,A.M.
  TITLE     DTX3 copy number increase in breast cancer: a study of associations
            to molecular subtype, proliferation and prognosis
  JOURNAL   Breast Cancer Res Treat 187 (1), 57-67 (2021)
   PUBMED   33616774
  REMARK    GeneRIF: DTX3 copy number increase in breast cancer: a study of
            associations to molecular subtype, proliferation and prognosis.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Markson,G., Kiel,C., Hyde,R., Brown,S., Charalabous,P., Bremm,A.,
            Semple,J., Woodsmith,J., Duley,S., Salehi-Ashtiani,K., Vidal,M.,
            Komander,D., Serrano,L., Lehner,P. and Sanderson,C.M.
  TITLE     Analysis of the human E2 ubiquitin conjugating enzyme protein
            interaction network
  JOURNAL   Genome Res 19 (10), 1905-1911 (2009)
   PUBMED   19549727
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Chastagner,P., Israel,A. and Brou,C.
  TITLE     Itch/AIP4 mediates Deltex degradation through the formation of
            K29-linked polyubiquitin chains
  JOURNAL   EMBO Rep 7 (11), 1147-1153 (2006)
   PUBMED   17028573
  REMARK    GeneRIF: We show here that both molecules (Deltex (DTX) and AIP4)
            interact and partially colocalize to endocytic vesicles, and that
            AIP4 targets DTX for lysosomal degradation.
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Takeyama,K., Aguiar,R.C., Gu,L., He,C., Freeman,G.J., Kutok,J.L.,
            Aster,J.C. and Shipp,M.A.
  TITLE     The BAL-binding protein BBAP and related Deltex family members
            exhibit ubiquitin-protein isopeptide ligase activity
  JOURNAL   J Biol Chem 278 (24), 21930-21937 (2003)
   PUBMED   12670957
  REMARK    GeneRIF: It is reported that BBAP and the human family of DTX
            proteins (DTX1, DTX2, and DTX3) function as E3 ligases based on
            their capacity for self-ubiquitination.
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Kishi,N., Tang,Z., Maeda,Y., Hirai,A., Mo,R., Ito,M., Suzuki,S.,
            Nakao,K., Kinoshita,T., Kadesch,T., Hui,C., Artavanis-Tsakonas,S.,
            Okano,H. and Matsuno,K.
  TITLE     Murine homologs of deltex define a novel gene family involved in
            vertebrate Notch signaling and neurogenesis
  JOURNAL   Int J Dev Neurosci 19 (1), 21-35 (2001)
   PUBMED   11226752
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Matsuno,K., Diederich,R.J., Go,M.J., Blaumueller,C.M. and
            Artavanis-Tsakonas,S.
  TITLE     Deltex acts as a positive regulator of Notch signaling through
            interactions with the Notch ankyrin repeats
  JOURNAL   Development 121 (8), 2633-2644 (1995)
   PUBMED   7671825
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK092085.1 and AK094385.1.
            
            Summary: DTX3 functions as an E3 ubiquitin ligase (Takeyama et al.,
            2003 [PubMed 12670957]).[supplied by OMIM, Nov 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the shorter isoform (a). Both variants 1 and
            2 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.445099.1, AK092085.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337737.8/ ENSP00000338050.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..347
                     /product="probable E3 ubiquitin-protein ligase DTX3
                     isoform a"
                     /EC_number="2.3.2.27"
                     /note="protein deltex-3; RING finger protein 154; probable
                     E3 ubiquitin-protein ligase DTX3; deltex 3, E3 ubiquitin
                     ligase; deltex homolog 3; RING-type E3 ubiquitin
                     transferase DTX3"
                     /calculated_mol_wt=37857
     Region          113..157
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9I9.2)"
     Region          161..214
                     /region_name="RING-HC_DTX3"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Deltex3 (DTX3) and similar
                     proteins; cd16711"
                     /db_xref="CDD:438371"
     Region          210..344
                     /region_name="DTC"
                     /note="Deltex C-terminal domain; pfam18102"
                     /db_xref="CDD:465650"
     Site            order(220..224,226,239,241,243..245,264..266,268,302,
                     315..316,324)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:193607"
     CDS             1..347
                     /gene="DTX3"
                     /gene_synonym="deltex3; RNF154"
                     /coded_by="NM_178502.4:335..1378"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41800.1"
                     /db_xref="GeneID:196403"
                     /db_xref="HGNC:HGNC:24457"
                     /db_xref="MIM:613142"
ORIGIN      
        1 msfvlsrmaa cggtcknkvt vskpvwdfls ketparlarl reehrvsili dgetsdiyvl
       61 qlspqgpppa ppnglylark alkgllkeae kelkkaqrqg elmgclalgg ggehpemhra
      121 gppplraapl lppgarglpp pppplppplp prlreeaeeq estcpiclge iqnaktlekc
      181 rhsfcegcit ralqvkkacp mcgrfygqlv gnqpqngrml vskdatlllp syekygtivi
      241 qyvfppgvqg aehpnpgvry pgttrvaylp dcpegnkvlt lfrkafdqrl tftigtsmtt
      301 grpnvitwnd ihhktsctgg pqlfgypdpt yltrvqeelr akgitdd
//
LOCUS       NP_001123468             491 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 222 isoform 1 [Homo sapiens].
ACCESSION   NP_001123468
VERSION     NP_001123468.1
DBSOURCE    REFSEQ: accession NM_001129996.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Shannon,M., Hamilton,A.T., Gordon,L., Branscomb,E. and Stubbs,L.
  TITLE     Differential expansion of zinc-finger transcription factor loci in
            homologous human and mouse gene clusters
  JOURNAL   Genome Res 13 (6A), 1097-1110 (2003)
   PUBMED   12743021
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Constantinou-Deltas,C.D., Gilbert,J., Bartlett,R.J.,
            Herbstreith,M., Roses,A.D. and Lee,J.E.
  TITLE     The identification and characterization of KRAB-domain-containing
            zinc finger proteins
  JOURNAL   Genomics 12 (3), 581-589 (1992)
   PUBMED   1559709
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB185422.1 and BC030261.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and it encodes the longer protein (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.136505.1,
                                           SRR1803614.114954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000391960.4/ ENSP00000375822.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..491
                     /product="zinc finger protein 222 isoform 1"
                     /calculated_mol_wt=56974
     Region          17..76
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          160..179
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..207
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(192,194,196,198..199,202..203,206,220,222,226..227,
                     230..231,234,248,250,252,254..255,258..259,262)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          210..>260
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          212..240
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          215..235
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(220,226,233,239,242,249)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          243..263
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          243..260
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          <265..404
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          271..291
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          331..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          355..375
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(360,362,364,366..367,370..371,374,388,390,394..395,
                     398..399,402,416,418,420,422..423,426..427,430)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <377..445
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          383..403
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          411..431
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..459
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..491
                     /gene="ZNF222"
                     /coded_by="NM_001129996.2:59..1534"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46098.1"
                     /db_xref="GeneID:7673"
                     /db_xref="HGNC:HGNC:13015"
                     /db_xref="MIM:617357"
ORIGIN      
        1 midsgekkpg rraeeavtfk dvavifteee lglldpaqrk lyrdvmlenf rnllsvghqp
       61 fhgdtfhflr eekfwvmgtt sqregnlggk iqtemetvpe agtheefsck qiweqiasdl
      121 trsqdttisn sqlfeqddnp sqikarlstv htrekpfqge nckqffsdvs ffdlpqqlys
      181 gekshtcdec gksfcyisal hihqrvhmgv kcykcdvcgk efsqssrlqt hqrvhtgekp
      241 fkceqcgkgf rcrsalkvhc klhmrekpyn cekcgkafmh nfqlqkhhri htgekpfkce
      301 icgksfclrs slnrhcmvht aeklykseky grgfidrldl hkhqmihmgq kpynckecgk
      361 sfkwssyllv hqrvhtgekp ykceecgkgy isksgldfhh rthtgersyn cdncgksfrh
      421 assilnhkkl hcqrkplkce dcgkrlvcrs yckdqqrdhs genpskcedc gkrykrrlnl
      481 diilslflnd i
//
LOCUS       NP_115688                244 aa            linear   PRI 27-APR-2025
DEFINITION  protein YIPF4 [Homo sapiens].
ACCESSION   NP_115688
VERSION     NP_115688.1
DBSOURCE    REFSEQ: accession NM_032312.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Kranjc,T., Dempsey,E., Cagney,G., Nakamura,N., Shields,D.C. and
            Simpson,J.C.
  TITLE     Functional characterisation of the YIPF protein family in mammalian
            cells
  JOURNAL   Histochem Cell Biol 147 (4), 439-451 (2017)
   PUBMED   27999994
  REMARK    GeneRIF: The significance of YIPF4 protein for the maintenance of
            the morphology of the Golgi was tested by RNA interference,
            revealing a number of specific morphological changes to this
            organelle on their depletion.
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Muller,M., Wasson,C.W., Bhatia,R., Boxall,S., Millan,D., Goh,G.Y.,
            Haas,J., Stonehouse,N.J. and Macdonald,A.
  TITLE     YIP1 family member 4 (YIPF4) is a novel cellular binding partner of
            the papillomavirus E5 proteins
  JOURNAL   Sci Rep 5, 12523 (2015)
   PUBMED   26235900
  REMARK    GeneRIF: YIPF4 is a binding partner of the papillomavirus E5
            proteins.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Tanimoto,K., Suzuki,K., Jokitalo,E., Sakai,N., Sakaguchi,T.,
            Tamura,D., Fujii,G., Aoki,K., Takada,S., Ishida,R., Tanabe,M.,
            Itoh,H., Yoneda,Y., Sohda,M., Misumi,Y. and Nakamura,N.
  TITLE     Characterization of YIPF3 and YIPF4, cis-Golgi Localizing Yip
            domain family proteins
  JOURNAL   Cell Struct Funct 36 (2), 171-185 (2011)
   PUBMED   21757827
  REMARK    GeneRIF: YIPF4 was detected as a single mobility form consistent
            with its predicted molecular weight, three different mobility forms
            of YIPF3 were detected by western blotting.
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Ohira,M., Morohashi,A., Nakamura,Y., Isogai,E., Furuya,K.,
            Hamano,S., Machida,T., Aoyama,M., Fukumura,M., Miyazaki,K.,
            Suzuki,Y., Sugano,S., Hirato,J. and Nakagawara,A.
  TITLE     Neuroblastoma oligo-capping cDNA project: toward the understanding
            of the genesis and biology of neuroblastoma
  JOURNAL   Cancer Lett 197 (1-2), 63-68 (2003)
   PUBMED   12880961
  REMARK    Review article
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP207600.1, BC004875.2, AL121653.2, BU608699.1 and AL133245.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.168893.1,
                                           SRR1660807.155128.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000238831.9/ ENSP00000238831.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.3"
     Protein         1..244
                     /product="protein YIPF4"
                     /note="putative protein product of Nbla11189; YIP1 family
                     member 4"
                     /calculated_mol_wt=26952
     Region          <74..237
                     /region_name="YIP1"
                     /note="Rab GTPase interacting factor, Golgi membrane
                     protein [Intracellular trafficking and secretion];
                     cl46908"
                     /db_xref="CDD:481248"
     Site            114..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSR8.1)"
     Site            139..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSR8.1)"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSR8.1)"
     Site            196..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSR8.1)"
     Site            224..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSR8.1)"
     CDS             1..244
                     /gene="YIPF4"
                     /gene_synonym="FinGER4; Nbla11189; YIPFalpha2"
                     /coded_by="NM_032312.4:253..987"
                     /db_xref="CCDS:CCDS1781.1"
                     /db_xref="GeneID:84272"
                     /db_xref="HGNC:HGNC:28145"
                     /db_xref="MIM:617534"
ORIGIN      
        1 mqppgpppay aptngdftfv ssadaedlsg siaspdvkln lggdfikest attflrqrgy
       61 gwlleveddd pednkpllee ldidlkdiyy kircvlmpmp slgfnrqvvr dnpdfwgpla
      121 vvlffsmisl ygqfrvvswi itiwifgslt ifllarvlgg evaygqvlgv igysllpliv
      181 iapvllvvgs fevvstlikl fgvfwaaysa asllvgeefk tkkplliypi fllyiyflsl
      241 ytgv
//
LOCUS       NP_892021                582 aa            linear   PRI 27-APR-2025
DEFINITION  DBIRD complex subunit ZNF326 isoform 1 [Homo sapiens].
ACCESSION   NP_892021
VERSION     NP_892021.1
DBSOURCE    REFSEQ: accession NM_182976.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Xu,Y., Qin,Y., Cui,J.X. and Xu,J.
  TITLE     MicroRNA-136-5p regulates gemcitabine resistance in pancreatic
            cancer via down-regulating ZNF32
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (20), 10472-10482 (2020)
   PUBMED   33155203
  REMARK    GeneRIF: MicroRNA-136-5p regulates gemcitabine resistance in
            pancreatic cancer via down-regulating ZNF32.
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Deng,C., Zhang,B., Zhang,Y., Xu,X., Xiong,D., Chen,X. and Wu,J.
  TITLE     A long non-coding RNA OLBC15 promotes triple-negative breast cancer
            progression via enhancing ZNF326 degradation
  JOURNAL   J Clin Lab Anal 34 (8), e23304 (2020)
   PUBMED   32329931
  REMARK    GeneRIF: A long non-coding RNA OLBC15 promotes triple-negative
            breast cancer progression via enhancing ZNF326 degradation.
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Wang,M., Han,Q., Su,Z. and Yu,X.
  TITLE     Transcription Factor ZNF326 Upregulates the Expression of ERCC1 and
            HDAC7 and its Clinicopathologic Significance in Glioma
  JOURNAL   Lab Med 51 (4), 377-384 (2020)
   PUBMED   31930344
  REMARK    GeneRIF: Transcription Factor ZNF326 Upregulates the Expression of
            ERCC1 and HDAC7 and its Clinicopathologic Significance in Glioma.
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Yu,X., Wang,M., Wu,J., Han,Q. and Zhang,X.
  TITLE     ZNF326 promotes malignant phenotype of glioma by up-regulating
            HDAC7 expression and activating Wnt pathway
  JOURNAL   J Exp Clin Cancer Res 38 (1), 40 (2019)
   PUBMED   30691485
  REMARK    GeneRIF: High ZNF326 expression is associated with glioma.
            Erratum:[J Exp Clin Cancer Res. 2020 Jan 16;39(1):14. doi:
            10.1186/s13046-020-1526-z. PMID: 31941535]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 582)
  AUTHORS   Close,P., East,P., Dirac-Svejstrup,A.B., Hartmann,H., Heron,M.,
            Maslen,S., Chariot,A., Soding,J., Skehel,M. and Svejstrup,J.Q.
  TITLE     DBIRD complex integrates alternative mRNA splicing with RNA
            polymerase II transcript elongation
  JOURNAL   Nature 484 (7394), 386-389 (2012)
   PUBMED   22446626
  REMARK    GeneRIF: data indicate that the DBIRD complex (consisting of DBC1
            and ZNF326) acts at the interface between mRNP particles and
            RNAPII, integrating transcript elongation with the regulation of
            alternative splicing
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 582)
  AUTHORS   Liou,Y.J., Chen,C.H., Cheng,C.Y., Chen,S.Y., Chen,T.J., Yu,Y.W.,
            Nian,F.S., Tsai,S.J. and Hong,C.J.
  TITLE     Convergent evidence from mouse and human studies suggests the
            involvement of zinc finger protein 326 gene in antidepressant
            treatment response
  JOURNAL   PLoS One 7 (5), e32984 (2012)
   PUBMED   22666313
  REMARK    GeneRIF: involvement of the Zfp326 and ZNF326 genes in
            antidepressant treatment response
REFERENCE   9  (residues 1 to 582)
  AUTHORS   Stein,J.L., Hua,X., Morra,J.H., Lee,S., Hibar,D.P., Ho,A.J.,
            Leow,A.D., Toga,A.W., Sul,J.H., Kang,H.M., Eskin,E., Saykin,A.J.,
            Shen,L., Foroud,T., Pankratz,N., Huentelman,M.J., Craig,D.W.,
            Gerber,J.D., Allen,A.N., Corneveaux,J.J., Stephan,D.A., Webster,J.,
            DeChairo,B.M., Potkin,S.G., Jack,C.R. Jr., Weiner,M.W. and
            Thompson,P.M.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     Genome-wide analysis reveals novel genes influencing temporal lobe
            structure with relevance to neurodegeneration in Alzheimer's
            disease
  JOURNAL   Neuroimage 51 (2), 542-554 (2010)
   PUBMED   20197096
REFERENCE   10 (residues 1 to 582)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN299618.1, BC090866.2, AK303707.1, AL161797.10 and BU676987.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.120816.1,
                                           SRR1803613.166355.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340281.9/ ENSP00000340796.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.2"
     Protein         1..582
                     /product="DBIRD complex subunit ZNF326 isoform 1"
                     /note="ZNF-protein interacting with nuclear mRNPs and
                     DBC1; DBIRD complex subunit ZNF326; zinc finger protein
                     interacting with mRNPs and DBC1"
                     /calculated_mol_wt=65523
     Region          1..124
                     /region_name="Mediates transcriptional activation.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Region          154..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            173
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            235
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Region          238..260
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Region          243..302
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            247
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     Region          337..472
                     /region_name="AKAP95"
                     /note="A-kinase anchoring protein 95 (AKAP95); pfam04988"
                     /db_xref="CDD:461509"
     Region          472..582
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKZ1.2)"
     CDS             1..582
                     /gene="ZNF326"
                     /gene_synonym="dJ871E2.1; ZAN75; Zfp326; ZIRD"
                     /coded_by="NM_182976.4:149..1897"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS727.1"
                     /db_xref="GeneID:284695"
                     /db_xref="HGNC:HGNC:14104"
                     /db_xref="MIM:614601"
ORIGIN      
        1 mdfeddyths acrntyqgfn gmdrdygpgs yggmdrdygh gsyggqrsmd sylnqsygmd
       61 nhsgggggsr fgpyesydsr sslggrdlyr sgygfnepeq srfggsyggr fessyrnsld
      121 sfggrnqggs sweapysrsk lrpgfmedrg renyssyssf ssphmkpapv gsrgrgtpay
      181 pestfgsrny dafggpstgr grgrghmgdf gsihrpgivv dyqnkstnvt vaaargikrk
      241 mmqpfnkpsg tfikkpklak pmekislsks ptktdpknee eekrriearr ekqrrrrekn
      301 sekygdgyrm aftcsfckfr tfeekdielh lessshqetl dhiqkqtkfd kvvmeflhec
      361 mvnkfkktsi rkqqtnnqte vvkiiekdvm egvtvddhmm kvetvhcsac svyipalhss
      421 vqqhlkspdh ikgkqaykeq ikresvltat silnnpivka ryerfvkgen pfeiqdhsqd
      481 qqiegdeede ekidepieee ededeeeeae evgeveevee veevreggie gegniqgvge
      541 ggevgvvgev egvgeveeve eleeetakee padfpveqpe en
//
LOCUS       NP_940867               1582 aa            linear   PRI 27-APR-2025
DEFINITION  nik-related protein kinase [Homo sapiens].
ACCESSION   NP_940867 XP_114703
VERSION     NP_940867.2
DBSOURCE    REFSEQ: accession NM_198465.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1582)
  AUTHORS   He,W., Tian,Z., Dong,B., Cao,Y., Hu,W., Wu,P., Yu,L., Zhang,X. and
            Guo,S.
  TITLE     Identification and functional activity of Nik related kinase (NRK)
            in benign hyperplastic prostate
  JOURNAL   J Transl Med 22 (1), 255 (2024)
   PUBMED   38459501
  REMARK    GeneRIF: Identification and functional activity of Nik related
            kinase (NRK) in benign hyperplastic prostate.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1582)
  AUTHORS   Wei,T., Song,J., Liang,K., Li,L., Mo,X., Huang,Z., Chen,G., Mao,N.
            and Yang,J.
  TITLE     Identification of a novel therapeutic candidate, NRK, in primary
            cancer-associated fibroblasts of lung adenocarcinoma
            microenvironment
  JOURNAL   J Cancer Res Clin Oncol 147 (4), 1049-1064 (2021)
   PUBMED   33387038
  REMARK    GeneRIF: Identification of a novel therapeutic candidate, NRK, in
            primary cancer-associated fibroblasts of lung adenocarcinoma
            microenvironment.
REFERENCE   3  (residues 1 to 1582)
  AUTHORS   Naito,S., Fukushima,T., Endo,A., Denda,K. and Komada,M.
  TITLE     Nik-related kinase is targeted for proteasomal degradation by the
            chaperone-dependent ubiquitin ligase CHIP
  JOURNAL   FEBS Lett 594 (11), 1778-1786 (2020)
   PUBMED   32162334
  REMARK    GeneRIF: Nik-related kinase is targeted for proteasomal degradation
            by the chaperone-dependent ubiquitin ligase CHIP.
REFERENCE   4  (residues 1 to 1582)
  AUTHORS   Yanagawa,T., Denda,K., Inatani,T., Fukushima,T., Tanaka,T.,
            Kumaki,N., Inagaki,Y. and Komada,M.
  TITLE     Deficiency of X-Linked Protein Kinase Nrk during Pregnancy Triggers
            Breast Tumor in Mice
  JOURNAL   Am J Pathol 186 (10), 2751-2760 (2016)
   PUBMED   27634343
  REMARK    GeneRIF: The results suggest that Nrk suppresses the excessive
            proliferation of mammary epithelial cells during pregnancy, and the
            impairment of this regulatory system leads to frequent occurrence
            of breast tumor in Nrk mutant mice.
REFERENCE   5  (residues 1 to 1582)
  AUTHORS   Ross,M.T., Grafham,D.V., Coffey,A.J., Scherer,S., McLay,K.,
            Muzny,D., Platzer,M., Howell,G.R., Burrows,C., Bird,C.P.,
            Frankish,A., Lovell,F.L., Howe,K.L., Ashurst,J.L., Fulton,R.S.,
            Sudbrak,R., Wen,G., Jones,M.C., Hurles,M.E., Andrews,T.D.,
            Scott,C.E., Searle,S., Ramser,J., Whittaker,A., Deadman,R.,
            Carter,N.P., Hunt,S.E., Chen,R., Cree,A., Gunaratne,P., Havlak,P.,
            Hodgson,A., Metzker,M.L., Richards,S., Scott,G., Steffen,D.,
            Sodergren,E., Wheeler,D.A., Worley,K.C., Ainscough,R.,
            Ambrose,K.D., Ansari-Lari,M.A., Aradhya,S., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Ballabio,A., Banerjee,R., Barker,G.E.,
            Barlow,K.F., Barrett,I.P., Bates,K.N., Beare,D.M., Beasley,H.,
            Beasley,O., Beck,A., Bethel,G., Blechschmidt,K., Brady,N.,
            Bray-Allen,S., Bridgeman,A.M., Brown,A.J., Brown,M.J., Bonnin,D.,
            Bruford,E.A., Buhay,C., Burch,P., Burford,D., Burgess,J.,
            Burrill,W., Burton,J., Bye,J.M., Carder,C., Carrel,L., Chako,J.,
            Chapman,J.C., Chavez,D., Chen,E., Chen,G., Chen,Y., Chen,Z.,
            Chinault,C., Ciccodicola,A., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S., Clerc-Blankenburg,K., Clifford,K., Cobley,V., Cole,C.G.,
            Conquer,J.S., Corby,N., Connor,R.E., David,R., Davies,J., Davis,C.,
            Davis,J., Delgado,O., Deshazo,D., Dhami,P., Ding,Y., Dinh,H.,
            Dodsworth,S., Draper,H., Dugan-Rocha,S., Dunham,A., Dunn,M.,
            Durbin,K.J., Dutta,I., Eades,T., Ellwood,M., Emery-Cohen,A.,
            Errington,H., Evans,K.L., Faulkner,L., Francis,F., Frankland,J.,
            Fraser,A.E., Galgoczy,P., Gilbert,J., Gill,R., Glockner,G.,
            Gregory,S.G., Gribble,S., Griffiths,C., Grocock,R., Gu,Y.,
            Gwilliam,R., Hamilton,C., Hart,E.A., Hawes,A., Heath,P.D.,
            Heitmann,K., Hennig,S., Hernandez,J., Hinzmann,B., Ho,S., Hoffs,M.,
            Howden,P.J., Huckle,E.J., Hume,J., Hunt,P.J., Hunt,A.R.,
            Isherwood,J., Jacob,L., Johnson,D., Jones,S., de Jong,P.J.,
            Joseph,S.S., Keenan,S., Kelly,S., Kershaw,J.K., Khan,Z.,
            Kioschis,P., Klages,S., Knights,A.J., Kosiura,A., Kovar-Smith,C.,
            Laird,G.K., Langford,C., Lawlor,S., Leversha,M., Lewis,L., Liu,W.,
            Lloyd,C., Lloyd,D.M., Loulseged,H., Loveland,J.E., Lovell,J.D.,
            Lozado,R., Lu,J., Lyne,R., Ma,J., Maheshwari,M., Matthews,L.H.,
            McDowall,J., McLaren,S., McMurray,A., Meidl,P., Meitinger,T.,
            Milne,S., Miner,G., Mistry,S.L., Morgan,M., Morris,S., Muller,I.,
            Mullikin,J.C., Nguyen,N., Nordsiek,G., Nyakatura,G., O'Dell,C.N.,
            Okwuonu,G., Palmer,S., Pandian,R., Parker,D., Parrish,J.,
            Pasternak,S., Patel,D., Pearce,A.V., Pearson,D.M., Pelan,S.E.,
            Perez,L., Porter,K.M., Ramsey,Y., Reichwald,K., Rhodes,S.,
            Ridler,K.A., Schlessinger,D., Schueler,M.G., Sehra,H.K.,
            Shaw-Smith,C., Shen,H., Sheridan,E.M., Shownkeen,R., Skuce,C.D.,
            Smith,M.L., Sotheran,E.C., Steingruber,H.E., Steward,C.A.,
            Storey,R., Swann,R.M., Swarbreck,D., Tabor,P.E., Taudien,S.,
            Taylor,T., Teague,B., Thomas,K., Thorpe,A., Timms,K., Tracey,A.,
            Trevanion,S., Tromans,A.C., d'Urso,M., Verduzco,D., Villasana,D.,
            Waldron,L., Wall,M., Wang,Q., Warren,J., Warry,G.L., Wei,X.,
            West,A., Whitehead,S.L., Whiteley,M.N., Wilkinson,J.E.,
            Willey,D.L., Williams,G., Williams,L., Williamson,A.,
            Williamson,H., Wilming,L., Woodmansey,R.L., Wray,P.W., Yen,J.,
            Zhang,J., Zhou,J., Zoghbi,H., Zorilla,S., Buck,D., Reinhardt,R.,
            Poustka,A., Rosenthal,A., Lehrach,H., Meindl,A., Minx,P.J.,
            Hillier,L.W., Willard,H.F., Wilson,R.K., Waterston,R.H., Rice,C.M.,
            Vaudin,M., Coulson,A., Nelson,D.L., Weinstock,G., Sulston,J.E.,
            Durbin,R., Hubbard,T., Gibbs,R.A., Beck,S., Rogers,J. and
            Bentley,D.R.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
REFERENCE   6  (residues 1 to 1582)
  AUTHORS   Nakano,K., Kanai-Azuma,M., Kanai,Y., Moriyama,K., Yazaki,K.,
            Hayashi,Y. and Kitamura,N.
  TITLE     Cofilin phosphorylation and actin polymerization by NRK/NESK, a
            member of the germinal center kinase family
  JOURNAL   Exp Cell Res 287 (2), 219-227 (2003)
   PUBMED   12837278
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z70274.1, BX538345.1, Z69734.2,
            KF459287.1, Z68339.2 and Z83850.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 2, 2006 this sequence version replaced NP_940867.1.
            
            Summary: The mouse ortholog of this gene encodes a protein kinase
            required for JNK activation. The encoded protein may be involved in
            the induction of actin polymerization in late
            embryogenesis.[provided by RefSeq, Jun 2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX538345.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000243300.14/ ENSP00000434830.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1582
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.3"
     Protein         1..1582
                     /product="nik-related protein kinase"
                     /EC_number="2.7.11.1"
                     /calculated_mol_wt=178349
     Region          18..313
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(31..34,37,39,52,54,107,129..132,177,181..182,184,
                     194..195)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          <386..>537
                     /region_name="PRK10927"
                     /note="cell division protein FtsN"
                     /db_xref="CDD:236797"
     Region          492..579
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z2Y5.2)"
     Region          783..859
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z2Y5.2)"
     Site            852
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2Y5.2)"
     Site            855
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2Y5.2)"
     Region          926..1156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z2Y5.2)"
     Site            1027
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2Y5.2)"
     Site            1031
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2Y5.2)"
     Site            1034
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q7Z2Y5.2)"
     Region          1218..1548
                     /region_name="CNH"
                     /note="CNH domain; cl02434"
                     /db_xref="CDD:470577"
     CDS             1..1582
                     /gene="NRK"
                     /gene_synonym="NESK"
                     /coded_by="NM_198465.4:308..5056"
                     /db_xref="CCDS:CCDS65305.1"
                     /db_xref="GeneID:203447"
                     /db_xref="HGNC:HGNC:25391"
                     /db_xref="MIM:300791"
ORIGIN      
        1 magpggwrdr evtdlghlpd ptgifsldkt iglgtygriy lglhektgaf tavkvmnark
       61 tplpeigrrv rvnkyqksvg wrysdeeedl rtelnllrky sfhknivsfy gaffklsppg
      121 qrhqlwmvme lcaagsvtdv vrmtsnqslk edwiayicre ilqglahlha hrvihrdikg
      181 qnvllthnae vklvdfgvsa qvsrtngrrn sfigtpywma pevidcdedp rrsydyrsdv
      241 wsvgitaiem aegapplcnl qplealfvil resaptvkss gwsrkfhnfm ekctiknflf
      301 rptsanmlqh pfvrdikner hvvesltrhl tgiikkrqkk gipliferee aikeqytvrr
      361 frgpscthel lrlptssrcr plrvlhgeps qprwlpdree pqvqalqqlq gaarvfmplq
      421 aldsapkplk gqaqapqrlq gaarvfmplq aqvkakaskp lqmqikappr lrraarvlmp
      481 lqaqvraprl lqvqsqvskk qqaqtqtsep qdldqvpeef qgqdqvpeqq rqgqapeqqq
      541 rhnqvpeqel eqnqapeqpe vqeqaaepaq aeteaeepes lrvnaqvflp llsqdhhvll
      601 plhldtqvli pvegqtegsp qaqawtlepp qaigsvqali eglsrdllra pnsnnskplg
      661 plqtlmenls snrfysqpeq arekkskvst lrqalakrls pkrfrakssw rpeklelsdl
      721 earrqrrqrr wedifnqhee elrqvdkdke dessdndevf hsiqaevqie plkpyisnpk
      781 kievqersps vpnnqdhahh vkfsssvpqr slleqaqkpi dirqrssqnr qnwlaasess
      841 seeespvtgr rsqssppyst idqkllvdih vpdgfkvgki sppvyltnew vgynalseif
      901 rndwltpapv iqppeedgdy velydasadt dgddddesnd tfedtydhan gnddldnqvd
      961 qandvckdhd ddnnkfvddv nnnyyeapsc prasygrdgs ckqdgydgsr gkeeayrgyg
     1021 shtanrshgg saasednaai gdqeehaani gserrgsegd ggkgvvrtse esgalglnge
     1081 encsetdgpg lkrpasqdfe ylqeepgggn easnaidsga apsapdhesd nkdisesstq
     1141 sdfsanhssp skgsgmsada nfasailyag fvevpeespk qpsevnvnpl yvspackkpl
     1201 ihmyekefts eiccgslwgv nlllgtrsnl ylmdrsgkad itklirrrpf rqiqvlepln
     1261 llitisghkn rlrvyhltwl rnkilnndpe skrrqeemlk teeackaidk ltgcehfsvl
     1321 qheettyiai alkssihlya wapksfdest aikvcidqsa dsegdymsyq ayirilakiq
     1381 aadpvnrfkr pdellhllkl kvfptldhkp vtvdlaigse krlkiffssa dgyhlidaes
     1441 evmsdvtlpk npleiiipqn iiilpdclgi gmmltfnaea lsveaneqlf kkilemwkdi
     1501 pssiafectq rttgwgqkai evrslqsrvl eselkrrsik klrflctrgd klfftstlrn
     1561 hhsrvyfmtl gkleelqsny dv
//
LOCUS       NP_444483                440 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger MYND domain-containing protein 10 isoform 1 [Mus
            musculus].
ACCESSION   NP_444483 XP_981515
VERSION     NP_444483.2
DBSOURCE    REFSEQ: accession NM_053253.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Mali,G.R., Yeyati,P.L., Mizuno,S., Dodd,D.O., Tennant,P.A.,
            Keighren,M.A., Zur Lage,P., Shoemark,A., Garcia-Munoz,A.,
            Shimada,A., Takeda,H., Edlich,F., Takahashi,S., von Kreigsheim,A.,
            Jarman,A.P. and Mill,P.
  TITLE     ZMYND10 functions in a chaperone relay during axonemal dynein
            assembly
  JOURNAL   Elife 7, e34389 (2018)
   PUBMED   29916806
  REMARK    GeneRIF: ZMYND10 is a novel co-chaperone that confers specificity
            for the FKBP8-HSP90 chaperone complex towards axonemal dynein
            clients required for cilia motility.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Cho,K.J., Noh,S.H., Han,S.M., Choi,W.I., Kim,H.Y., Yu,S., Lee,J.S.,
            Rim,J.H., Lee,M.G., Hildebrandt,F. and Gee,H.Y.
  TITLE     ZMYND10 stabilizes intermediate chain proteins in the cytoplasmic
            pre-assembly of dynein arms
  JOURNAL   PLoS Genet 14 (3), e1007316 (2018)
   PUBMED   29601588
  REMARK    GeneRIF: results demonstrated that ZMYND10 regulated the early
            stage of DA cytoplasmic pre-assembly by stabilizing DNAI1
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Shi,B., Xue,J., Zhou,J., Kasowitz,S.D., Zhang,Y., Liang,G.,
            Guan,Y., Shi,Q., Liu,M., Sha,J., Huang,X. and Wang,P.J.
  TITLE     MORC2B is essential for meiotic progression and fertility
  JOURNAL   PLoS Genet 14 (1), e1007175 (2018)
   PUBMED   29329290
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Moore,D.J., Onoufriadis,A., Shoemark,A., Simpson,M.A., zur
            Lage,P.I., de Castro,S.C., Bartoloni,L., Gallone,G., Petridi,S.,
            Woollard,W.J., Antony,D., Schmidts,M., Didonna,T.,
            Makrythanasis,P., Bevillard,J., Mongan,N.P., Djakow,J., Pals,G.,
            Lucas,J.S., Marthin,J.K., Nielsen,K.G., Santoni,F., Guipponi,M.,
            Hogg,C., Antonarakis,S.E., Emes,R.D., Chung,E.M., Greene,N.D.,
            Blouin,J.L., Jarman,A.P. and Mitchison,H.M.
  TITLE     Mutations in ZMYND10, a gene essential for proper axonemal assembly
            of inner and outer dynein arms in humans and flies, cause primary
            ciliary dyskinesia
  JOURNAL   Am J Hum Genet 93 (2), 346-356 (2013)
   PUBMED   23891471
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Agathanggelou,A., Dallol,A., Zochbauer-Muller,S., Morrissey,C.,
            Honorio,S., Hesson,L., Martinsson,T., Fong,K.M., Kuo,M.J.,
            Yuen,P.W., Maher,E.R., Minna,J.D. and Latif,F.
  TITLE     Epigenetic inactivation of the candidate 3p21.3 suppressor gene BLU
            in human cancers
  JOURNAL   Oncogene 22 (10), 1580-1588 (2003)
   PUBMED   12629521
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Lerman,M.I. and Minna,J.D.
  TITLE     The 630-kb lung cancer homozygous deletion region on human
            chromosome 3p21.3: identification and evaluation of the resident
            candidate tumor suppressor genes. The International Lung Cancer
            Chromosome 3p21.3 Tumor Suppressor Gene Consortium
  JOURNAL   Cancer Res 60 (21), 6116-6133 (2000)
   PUBMED   11085536
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY284492.1, BC052357.1 and AL672219.7.
            
            On or before May 4, 2006 this sequence version replaced
            XP_981515.1, NP_444483.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052357.1, AK132332.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 58.12 cM"
     Protein         1..440
                     /product="zinc finger MYND domain-containing protein 10
                     isoform 1"
                     /note="zinc finger MYND domain-containing protein 10;
                     protein BLu"
                     /calculated_mol_wt=50516
     Region          394..430
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..440
                     /gene="Zmynd10"
                     /gene_synonym="Blu"
                     /coded_by="NM_053253.4:154..1476"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS23493.1"
                     /db_xref="GeneID:114602"
                     /db_xref="MGI:MGI:2387863"
ORIGIN      
        1 mgdlelllpg eaevlvrglr sfqlremgse gwnkqhesle klnmqailda tisqaepiqe
       61 llinhgkipt lveeliavem wkqkvfpvlc rledfkpqnt fpiymvvhhe asiinlletv
      121 ffhkevcesa ddkvldlvdy chrklillva rkgggdlsee eqfqdstpmq elqkqaemme
      181 feislkalsv lryitdcvds lslstlnrml rthnlpcllv ellehspwsr rvggklqhfe
      241 sgrwqtvaps eqqklnkldg qvwialynll lspeararyc ltsfakgqll klqafltdtl
      301 ldqlpnladl kgflahlsla etqppkkdlv leqipeiwdr lerenkgkwq aiakhqlqhv
      361 fslsekdlrq qaqrwaetyr ldvleavape rprcgycnae askrcsrcqn vwyccrecqv
      421 khwekhgktc vlaaqgdrak
//
LOCUS       NP_001346966             324 aa            linear   ROD 27-APR-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Mus musculus].
ACCESSION   NP_001346966 XP_011243867
VERSION     NP_001346966.1
DBSOURCE    REFSEQ: accession NM_001360037.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Park,C.S., Guan,J., Rhee,P., Gonzalez,F., Lee,H.S., Park,J.H.,
            Coscoy,L., Robey,E.A., Shastri,N. and Sadegh-Nasseri,S.
  TITLE     Fam49b dampens TCR signal strength to regulate survival of
            positively selected thymocytes and peripheral T cells
  JOURNAL   Elife 13, e76940 (2024)
   PUBMED   39158947
  REMARK    GeneRIF: Fam49b dampens TCR signal strength to regulate survival of
            positively selected thymocytes and peripheral T cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Sisario,D., Spindler,M., Ermer,K.J., Grutz,N., Nicolai,L.,
            Gaertner,F., Machesky,L.M. and Bender,M.
  TITLE     Differential Role of the RAC1-Binding Proteins FAM49b (CYRI-B) and
            CYFIP1 in Platelets
  JOURNAL   Cells 13 (4), 299 (2024)
   PUBMED   38391912
  REMARK    GeneRIF: Differential Role of the RAC1-Binding Proteins FAM49b
            (CYRI-B) and CYFIP1 in Platelets.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Huang,Z., Pu,J., Luo,Y., Fan,J., Li,K., Peng,D., Zong,K., Zhou,B.,
            Guan,X. and Zhou,F.
  TITLE     FAM49B, restrained by miR-22, relieved hepatic ischemia/reperfusion
            injury by inhibiting TRAF6/IKK signaling pathway in a
            Rac1-dependent manner
  JOURNAL   Mol Immunol 143, 135-146 (2022)
   PUBMED   35131594
  REMARK    GeneRIF: FAM49B, restrained by miR-22, relieved hepatic
            ischemia/reperfusion injury by inhibiting TRAF6/IKK signaling
            pathway in a Rac1-dependent manner.
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Uslu,V.V., Petretich,M., Ruf,S., Langenfeld,K., Fonseca,N.A.,
            Marioni,J.C. and Spitz,F.
  TITLE     Long-range enhancers regulating Myc expression are required for
            normal facial morphogenesis
  JOURNAL   Nat Genet 46 (7), 753-758 (2014)
   PUBMED   24859337
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Nagarajan,N.A., Gonzalez,F. and Shastri,N.
  TITLE     Nonclassical MHC class Ib-restricted cytotoxic T cells monitor
            antigen processing in the endoplasmic reticulum
  JOURNAL   Nat Immunol 13 (6), 579-586 (2012)
   PUBMED   22522492
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Ishikawa,H., Thompson,J., Yates,J.R. 3rd and Marshall,W.F.
  TITLE     Proteomic analysis of mammalian primary cilia
  JOURNAL   Curr Biol 22 (5), 414-419 (2012)
   PUBMED   22326026
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Lo,J.C., Jamsai,D., O'Connor,A.E., Borg,C., Clark,B.J.,
            Whisstock,J.C., Field,M.C., Adams,V., Ishikawa,T., Aitken,R.J.,
            Whittle,B., Goodnow,C.C., Ormandy,C.J. and O'Bryan,M.K.
  TITLE     RAB-like 2 has an essential role in male fertility, sperm
            intra-flagellar transport, and tail assembly
  JOURNAL   PLoS Genet 8 (10), e1002969 (2012)
   PUBMED   23055941
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC156573.3 and AC140673.4.
            
            On Jan 26, 2018 this sequence version replaced XP_011243867.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1. 2, 3, and 4 encode the same protein.z.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR10662774.889660.1,
                                           SRR10662773.496531.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164134
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 28.16 cM"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; family with sequence similarity 49,
                     member B"
                     /calculated_mol_wt=36645
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="Cyrib"
                     /gene_synonym="0910001A06Rik; Fam49b"
                     /coded_by="NM_001360037.1:316..1290"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS27505.1"
                     /db_xref="GeneID:223601"
                     /db_xref="MGI:MGI:1923520"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqir smlq
//
LOCUS       NP_149017                519 aa            linear   PRI 27-APR-2025
DEFINITION  BBSome complex member BBS4 isoform 1 [Homo sapiens].
ACCESSION   NP_149017
VERSION     NP_149017.2
DBSOURCE    REFSEQ: accession NM_033028.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Zacchia,M., Blanco,F.D.V., Trepiccione,F., Blasio,G., Torella,A.,
            Melluso,A., Capolongo,G., Pollastro,R.M., Piluso,G., Di Iorio,V.,
            Simonelli,F., Viggiano,D., Perna,A., Nigro,V. and Capasso,G.
  TITLE     Nephroplex: a kidney-focused NGS panel highlights the challenges of
            PKD1 sequencing and identifies a founder BBS4 mutation
  JOURNAL   J Nephrol 34 (6), 1855-1874 (2021)
   PUBMED   33964006
  REMARK    GeneRIF: Nephroplex: a kidney-focused NGS panel highlights the
            challenges of PKD1 sequencing and identifies a founder BBS4
            mutation.
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Benardais,K., Delfino,G., Samama,B., Devys,D., Antal,M.C.,
            Ghandour,M.S. and Boehm,N.
  TITLE     BBS4 protein has basal body/ciliary localization in sensory organs
            but extra-ciliary localization in oligodendrocytes during human
            development
  JOURNAL   Cell Tissue Res 385 (1), 37-48 (2021)
   PUBMED   33860840
  REMARK    GeneRIF: BBS4 protein has basal body/ciliary localization in
            sensory organs but extra-ciliary localization in oligodendrocytes
            during human development.
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Riise,R., Tornqvist,K., Wright,A.F., Mykytyn,K. and Sheffield,V.C.
  TITLE     The phenotype in Norwegian patients with Bardet-Biedl syndrome with
            mutations in the BBS4 gene
  JOURNAL   Arch Ophthalmol 120 (10), 1364-1367 (2002)
   PUBMED   12365916
  REMARK    GeneRIF: The phenotype of patients with BBS4 mutations consists of
            severe retinitis pigmentosa, variable obesity, brachydactyly with
            variable polydactyly, small or missing teeth, genital hypoplasia,
            and cardiovascular disease.
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Katsanis,N., Eichers,E.R., Ansley,S.J., Lewis,R.A., Kayserili,H.,
            Hoskins,B.E., Scambler,P.J., Beales,P.L. and Lupski,J.R.
  TITLE     BBS4 is a minor contributor to Bardet-Biedl syndrome and may also
            participate in triallelic inheritance
  JOURNAL   Am J Hum Genet 71 (1), 22-29 (2002)
   PUBMED   12016587
  REMARK    GeneRIF: BBS4 is a minor contributor to Bardet-Biedl syndrome and
            may also participate in triallelic inheritance. Evaluated the
            spectrum of mutations in the recently identified BBS4 gene with a
            combination of haplotype analysis and mutation screening.
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Mykytyn,K., Braun,T., Carmi,R., Haider,N.B., Searby,C.C.,
            Shastri,M., Beck,G., Wright,A.F., Iannaccone,A., Elbedour,K.,
            Riise,R., Baldi,A., Raas-Rothschild,A., Gorman,S.W., Duhl,D.M.,
            Jacobson,S.G., Casavant,T., Stone,E.M. and Sheffield,V.C.
  TITLE     Identification of the gene that, when mutated, causes the human
            obesity syndrome BBS4
  JOURNAL   Nat Genet 28 (2), 188-191 (2001)
   PUBMED   11381270
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Bruford,E.A., Riise,R., Teague,P.W., Porter,K., Thomson,K.L.,
            Moore,A.T., Jay,M., Warburg,M., Schinzel,A., Tommerup,N.,
            Tornqvist,K., Rosenberg,T., Patton,M., Mansfield,D.C. and
            Wright,A.F.
  TITLE     Linkage mapping in 29 Bardet-Biedl syndrome families confirms loci
            in chromosomal regions 11q13, 15q22.3-q23, and 16q21
  JOURNAL   Genomics 41 (1), 93-99 (1997)
   PUBMED   9126487
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Carmi,R., Rokhlina,T., Kwitek-Black,A.E., Elbedour,K.,
            Nishimura,D., Stone,E.M. and Sheffield,V.C.
  TITLE     Use of a DNA pooling strategy to identify a human obesity syndrome
            locus on chromosome 15
  JOURNAL   Hum Mol Genet 4 (1), 9-13 (1995)
   PUBMED   7711739
REFERENCE   9  (residues 1 to 519)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009712.22.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 29, 2002 this sequence version replaced NP_149017.1.
            
            Summary: This gene is a member of the Bardet-Biedl syndrome (BBS)
            gene family. Bardet-Biedl syndrome is an autosomal recessive
            disorder characterized by severe pigmentary retinopathy, obesity,
            polydactyly, renal malformation and cognitive disability. The
            proteins encoded by BBS gene family members are structurally
            diverse. The similar phenotypes exhibited by mutations in BBS gene
            family members are likely due to the protein's shared roles in
            cilia formation and function. Many BBS proteins localize to the
            basal bodies, ciliary axonemes, and pericentriolar regions of
            cells. BBS proteins may also be involved in intracellular
            trafficking via microtubule-related transport. The protein encoded
            by this gene has sequence similarity to O-linked
            N-acetylglucosamine (O-GlcNAc) transferases in plants and
            archaebacteria and in human forms a multi-protein 'BBSome' complex
            with seven other BBS proteins. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF359281.1, SRR1660807.196134.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268057.9/ ENSP00000268057.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..519
                     /product="BBSome complex member BBS4 isoform 1"
                     /note="bardet-Biedl syndrome 4 protein; BBSome complex
                     member BBS4"
                     /calculated_mol_wt=58151
     Region          1..66
                     /region_name="Required for localization to centrosomes"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RK4.2)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RK4.2)"
     Region          36..61
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          67..100
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RK4.2)"
     Region          68..95
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          71..332
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          101..337
                     /region_name="Interaction with PCM1.
                     /evidence=ECO:0000269|PubMed:15107855"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RK4.2)"
     Region          101..129
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(102,105..106,109..110,112,136,139..140,143..144,
                     146..147,172..173,176..177,180)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          134..164
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          169..196
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..229
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          236..264
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          250..>446
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          270..298
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(271,274..275,278..279,281,305,308..309,312..313,
                     315..316,339,342..343,346..347,350)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          303..333
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          338..519
                     /region_name="Required for localization to centrosomes"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RK4.2)"
     Region          338..365
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          372..397
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          440..519
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RK4.2)"
     CDS             1..519
                     /gene="BBS4"
                     /coded_by="NM_033028.5:22..1581"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10246.1"
                     /db_xref="GeneID:585"
                     /db_xref="HGNC:HGNC:969"
                     /db_xref="MIM:600374"
ORIGIN      
        1 maeervatrt qfpvstesqk prqkkapefp ilekqnwlih lhyirkdyea ckavikeqlq
       61 etqglceyai yvqalifrle gniqeslelf qtcavlspqs adnlkqvars lfllgkhkaa
      121 ievyneaakl nqkdweishn lgvcyiylkq fnkaqdqlhn alnlnrhdlt yimlgkihll
      181 egdldkaiev ykkavefspe ntellttlgl lylqlgiyqk afehlgnalt ydptnykail
      241 aagsmmqthg dfdvaltkyr vvacavpesp plwnnigmcf fgkkkyvaai sclkranyla
      301 pfdwkilynl glvhltmqqy asafhflsaa infqpkmgel ymllavaltn ledienakra
      361 yaeavhldkc nplvnlnyav llynqgekkn alaqyqemek kvsllkdnss lefdsemvem
      421 aqklgaalqv gealvwtkpv kdpkskhqtt stskpasfqq plgsnqalgq amssaaayrt
      481 lpsgaggtsq ftkppslple pepavesspt etseqirek
//
LOCUS       NP_660291                195 aa            linear   PRI 27-APR-2025
DEFINITION  sperm acrosome-associated protein 7 precursor [Homo sapiens].
ACCESSION   NP_660291
VERSION     NP_660291.2
DBSOURCE    REFSEQ: accession NM_145248.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Korfanty,J., Toma,A., Wojtas,A., Rusin,A., Vydra,N. and Widlak,W.
  TITLE     Identification of a new mouse sperm acrosome-associated protein
  JOURNAL   Reproduction 143 (6), 749-757 (2012)
   PUBMED   22495889
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC016750.2, AL160033.21 and AI219896.1.
            
            On Aug 21, 2010 this sequence version replaced NP_660291.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX379456.2, AK130866.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283550.8/ ENSP00000283550.3
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..195
                     /product="sperm acrosome-associated protein 7 precursor"
                     /note="protein SPACA7; sperm acrosome-associated protein
                     7"
                     /calculated_mol_wt=18824
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96KW9.2)"
                     /calculated_mol_wt=2660
     Region          19..125
                     /region_name="SPACA7"
                     /note="Sperm acrosome-associated protein 7; pfam15307"
                     /db_xref="CDD:434617"
     mat_peptide     25..195
                     /product="Sperm acrosome-associated protein 7.
                     /id=PRO_0000274330"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KW9.2)"
                     /calculated_mol_wt=18824
     Site            62
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96KW9.2)"
     Region          64..89
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KW9.2)"
     Region          119..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KW9.2)"
     Site            159
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96KW9.2)"
     CDS             1..195
                     /gene="SPACA7"
                     /gene_synonym="C13orf28"
                     /coded_by="NM_145248.5:32..619"
                     /db_xref="CCDS:CCDS9524.1"
                     /db_xref="GeneID:122258"
                     /db_xref="HGNC:HGNC:29575"
ORIGIN      
        1 mavsqgdgtl cfvlllccwq etelrprtvi pgspteipfs skqedmsell deilvqeild
       61 lnkttpsemp stastlstpl hagidenyqa ggsenyhell enlqfspgie vkisndeana
      121 nanlhgdpse nyrgpqvspg seksvsskek nskntqyenl sildqilqni grssgnifhk
      181 eqqrtsaqrr sqgsq
//
LOCUS       NP_001132466             273 aa            linear   PLN 27-APR-2025
DEFINITION  SKA complex subunit 1 homolog [Zea mays].
ACCESSION   NP_001132466
VERSION     NP_001132466.1
DBSOURCE    REFSEQ: accession NM_001138994.2
KEYWORDS    RefSeq.
SOURCE      Zea mays
  ORGANISM  Zea mays
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD
            clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
            Zea.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Soderlund,C., Descour,A., Kudrna,D., Bomhoff,M., Boyd,L.,
            Currie,J., Angelova,A., Collura,K., Wissotski,M., Ashley,E.,
            Morrow,D., Fernandes,J., Walbot,V. and Yu,Y.
  TITLE     Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs
  JOURNAL   PLoS Genet 5 (11), e1000740 (2009)
   PUBMED   19936069
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Gardiner,J., Schroeder,S., Polacco,M.L., Sanchez-Villeda,H.,
            Fang,Z., Morgante,M., Landewe,T., Fengler,K., Useche,F.,
            Hanafey,M., Tingey,S., Chou,H., Wing,R., Soderlund,C. and Coe,E.H.
            Jr.
  TITLE     Anchoring 9,371 maize expressed sequence tagged unigenes to the
            bacterial artificial chromosome contig map by two-dimensional
            overgo hybridization
  JOURNAL   Plant Physiol 134 (4), 1317-1326 (2004)
   PUBMED   15020742
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EU969508.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU969508.1, SRR3147028.12376.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00780084, SAMN00780136
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Zea mays"
                     /db_xref="taxon:4577"
                     /chromosome="7"
                     /map="7"
     Protein         1..273
                     /product="SKA complex subunit 1 homolog"
                     /note="pco142961(571); spindle and kinetochore-associated
                     protein 1-like protein"
                     /calculated_mol_wt=30244
     Region          23..263
                     /region_name="SKA1"
                     /note="Spindle and kinetochore-associated protein 1;
                     pfam07160"
                     /db_xref="CDD:462107"
     CDS             1..273
                     /gene="LOC100193922"
                     /gene_synonym="GRMZM2G050126; pco142961"
                     /coded_by="NM_001138994.2:109..930"
                     /db_xref="GeneID:100193922"
ORIGIN      
        1 mevddgsrat ppldavaaaf ksqvmelqdl vlarsmfpat alpdlanvda lvtamesqve
       61 tisrrlqeel daipkakklv qrslkeeekl qhmlanlpsg mrkndfanqh eqsssrmlph
      121 fnssfteane celkikdepv aaprkgrapa prwyisteel dslssymrgr ltlekvniai
      181 nevasyadan ahlvtcpkkk lsedtwekal elrdiaasga vkgnhfflea dikgpglkld
      241 ntgkailtvl rhlgrfhevr ighhrvfils kqa
//
LOCUS       NP_940978               2045 aa            linear   PRI 27-APR-2025
DEFINITION  agrin isoform 2 precursor [Homo sapiens].
ACCESSION   NP_940978 XP_372195
VERSION     NP_940978.2
DBSOURCE    REFSEQ: accession NM_198576.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2045)
  AUTHORS   Kamiya,K., Tachiki,T., Sato,Y., Kouda,K., Kajita,E., Tamaki,J.,
            Kagamimori,S. and Iki,M.
  TITLE     Association between the 110-kDa C-terminal agrin fragment and
            skeletal muscle decline among community-dwelling older women
  JOURNAL   J Cachexia Sarcopenia Muscle 14 (5), 2253-2263 (2023)
   PUBMED   37562951
  REMARK    GeneRIF: Association between the 110-kDa C-terminal agrin fragment
            and skeletal muscle decline among community-dwelling older women.
REFERENCE   2  (residues 1 to 2045)
  AUTHORS   Lv,R., Duan,L., Gao,J., Si,J., Feng,C., Hu,J. and Zheng,X.
  TITLE     Bioinformatics-based analysis of the roles of basement
            membrane-related gene AGRN in systemic lupus erythematosus and
            pan-cancer development
  JOURNAL   Front Immunol 14, 1231611 (2023)
   PUBMED   37841281
  REMARK    GeneRIF: Bioinformatics-based analysis of the roles of basement
            membrane-related gene AGRN in systemic lupus erythematosus and
            pan-cancer development.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2045)
  AUTHORS   Uyen Dao,T.M., Barbeau,S., Messeant,J., Della-Gaspera,B.,
            Bouceba,T., Semprez,F., Legay,C. and Dobbertin,A.
  TITLE     The collagen ColQ binds to LRP4 and regulates the activation of the
            Muscle-Specific Kinase-LRP4 receptor complex by agrin at the
            neuromuscular junction
  JOURNAL   J Biol Chem 299 (8), 104962 (2023)
   PUBMED   37356721
  REMARK    GeneRIF: The collagen ColQ binds to LRP4 and regulates the
            activation of the Muscle-Specific Kinase-LRP4 receptor complex by
            agrin at the neuromuscular junction.
REFERENCE   4  (residues 1 to 2045)
  AUTHORS   Zhang,H., Liang,J., Lu,T., Li,M., Shan,G., Bi,G., Zhao,M., Jin,X.,
            Wang,Q., Chen,Z. and Zhan,C.
  TITLE     AGRN promotes lung adenocarcinoma progression by activating Notch
            signaling pathway and acts as a therapeutic target
  JOURNAL   Pharmacol Res 194, 106819 (2023)
   PUBMED   37321467
  REMARK    GeneRIF: AGRN promotes lung adenocarcinoma progression by
            activating Notch signaling pathway and acts as a therapeutic
            target.
REFERENCE   5  (residues 1 to 2045)
  AUTHORS   Pratt,J., Whitton,L., Ryan,A., Juliusdottir,T., Dolan,J.,
            Conroy,J., Narici,M., De Vito,G. and Boreham,C.
  TITLE     Genes encoding agrin (AGRN) and neurotrypsin (PRSS12) are
            associated with muscle mass, strength and plasma C-terminal agrin
            fragment concentration
  JOURNAL   Geroscience 45 (3), 1289-1302 (2023)
   PUBMED   36609795
  REMARK    GeneRIF: Genes encoding agrin (AGRN) and neurotrypsin (PRSS12) are
            associated with muscle mass, strength and plasma C-terminal agrin
            fragment concentration.
REFERENCE   6  (residues 1 to 2045)
  AUTHORS   Denzer,A.J., Brandenberger,R., Gesemann,M., Chiquet,M. and
            Ruegg,M.A.
  TITLE     Agrin binds to the nerve-muscle basal lamina via laminin
  JOURNAL   J Cell Biol 137 (3), 671-683 (1997)
   PUBMED   9151673
REFERENCE   7  (residues 1 to 2045)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
REFERENCE   8  (residues 1 to 2045)
  AUTHORS   Rupp,F., Ozcelik,T., Linial,M., Peterson,K., Francke,U. and
            Scheller,R.
  TITLE     Structure and chromosomal localization of the mammalian agrin gene
  JOURNAL   J Neurosci 12 (9), 3535-3544 (1992)
   PUBMED   1326608
REFERENCE   9  (residues 1 to 2045)
  AUTHORS   Campanelli,J.T., Hoch,W., Rupp,F., Kreiner,T. and Scheller,R.H.
  TITLE     Agrin mediates cell contact-induced acetylcholine receptor
            clustering
  JOURNAL   Cell 67 (5), 909-916 (1991)
   PUBMED   1659950
REFERENCE   10 (residues 1 to 2045)
  AUTHORS   Rupp,F., Payan,D.G., Magill-Solc,C., Cowan,D.M. and Scheller,R.H.
  TITLE     Structure and expression of a rat agrin
  JOURNAL   Neuron 6 (5), 811-823 (1991)
   PUBMED   1851019
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645608.30, AB191264.1,
            CN314674.1, CN314678.1, AW119098.1, BC007649.1 and CK000983.1.
            
            On or before Nov 15, 2004 this sequence version replaced
            XP_372195.1, NP_940978.1.
            
            Summary: This gene encodes one of several proteins that are
            critical in the development of the neuromuscular junction (NMJ), as
            identified in mouse knock-out studies. The encoded protein contains
            several laminin G, Kazal type serine protease inhibitor, and
            epidermal growth factor domains. Additional post-translational
            modifications occur to add glycosaminoglycans and disulfide bonds.
            In one family with congenital myasthenic syndrome affecting
            limb-girdle muscles, a mutation in this gene was found. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (2) lacks alternate in-frame exons
            in the 3' coding region, compared to variant 1. The encoded isoform
            (2) is shorter, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB191264.1, AF016903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379370.7/ ENSP00000368678.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2045
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..2045
                     /product="agrin isoform 2 precursor"
                     /note="agrin proteoglycan"
                     /calculated_mol_wt=212045
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2820
     mat_peptide     30..1102
                     /product="Agrin N-terminal 110 kDa subunit.
                     /evidence=ECO:0000250. /id=PRO_0000421613"
                     /note="propagated from UniProtKB/Swiss-Prot (O00468.6)"
                     /calculated_mol_wt=111896
     Region          31..146
                     /region_name="NtA"
                     /note="Agrin NtA domain; pfam03146"
                     /db_xref="CDD:460825"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Region          196..242
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Site            250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Region          272..317
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Region          349..389
                     /region_name="KAZAL_FS"
                     /note="Kazal type serine protease inhibitors and
                     follistatin-like domains. Kazal inhibitors inhibit serine
                     proteases, such as, trypsin, chyomotrypsin, avian
                     ovomucoids, and elastases. The inhibitory domain has one
                     reactive site peptide bond, which serves the...; cl00097"
                     /db_xref="CDD:412159"
     Region          421..461
                     /region_name="KAZAL_FS"
                     /note="Kazal type serine protease inhibitors and
                     follistatin-like domains. Kazal inhibitors inhibit serine
                     proteases, such as, trypsin, chyomotrypsin, avian
                     ovomucoids, and elastases. The inhibitory domain has one
                     reactive site peptide bond, which serves the...; cd00104"
                     /db_xref="CDD:238052"
     Region          489..534
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Region          554..599
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Region          619..664
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Site            674
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2ASQ1; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Site            676
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2ASQ1; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Region          704..750
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Site            777
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Region          793..835
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(793,795,805,812,814,823)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          847..>883
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(847,849,859,866,868,877)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          922..969
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Site            932
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Region          995..1096
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00468.6)"
     Site            1102..1103
                     /site_type="cleavage"
                     /note="Cleavage, alpha site, by neurotrypsin.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Region          1130..1254
                     /region_name="SEA"
                     /note="Domain found in sea urchin sperm protein,
                     enterokinase, agrin; smart00200"
                     /db_xref="CDD:214554"
     Site            1250
                     /site_type="other"
                     /note="Alternative splice site to produce 'x' isoforms.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Region          1277..1334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00468.6)"
     Region          1333..1363
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          1400..1531
                     /region_name="Laminin_G_1"
                     /note="Laminin G domain; pfam00054"
                     /db_xref="CDD:395008"
     Region          1555..1585
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1668..1799
                     /region_name="Laminin_G_1"
                     /note="Laminin G domain; pfam00054"
                     /db_xref="CDD:395008"
     Site            1751
                     /site_type="other"
                     /note="Alternative splice site to produce 'y' isoforms.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Region          1821..1853
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            1831
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) serine.
                     /evidence=ECO:0000250|UniProtKB:P25304; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Site            1858
                     /site_type="other"
                     /note="Critical for cleavage by neurotrypsin.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Site            1859..1860
                     /site_type="cleavage"
                     /note="Cleavage, beta site, by neurotrypsin.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O00468.6)"
     Region          1898..2028
                     /region_name="Laminin_G_1"
                     /note="Laminin G domain; pfam00054"
                     /db_xref="CDD:395008"
     CDS             1..2045
                     /gene="AGRN"
                     /gene_synonym="AGRIN; CMS8; CMSPPD"
                     /coded_by="NM_198576.4:54..6191"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS30551.1"
                     /db_xref="GeneID:375790"
                     /db_xref="HGNC:HGNC:329"
                     /db_xref="MIM:103320"
ORIGIN      
        1 magrshpgpl rpllpllvva acvlpgaggt cperalerre eeanvvltgt veeilnvdpv
       61 qhtysckvrv wrylkgkdlv areslldggn kvvisgfgdp licdnqvstg dtriffvnpa
      121 ppylwpahkn elmlnsslmr itlrnleeve fcvedkpgth ftpvpptppd acrgmlcgfg
      181 avcepnaegp grascvckks pcpsvvapvc gsdastysne celqraqcsq qrrirllsrg
      241 pcgsrdpcsn vtcsfgstca rsadgltasc lcpatcrgap egtvcgsdga dypgecqllr
      301 racarqenvf kkfdgpcdpc qgalpdpsrs crvnprtrrp emllrpescp arqapvcgdd
      361 gvtyendcvm grsgaargll lqkvrsgqcq grdqcpepcr fnavclsrrg rprcscdrvt
      421 cdgayrpvca qdgrtydsdc wrqqaecrqq raipskhqgp cdqapspclg vqcafgatca
      481 vkngqaacec lqacsslydp vcgsdgvtyg saceleatac tlgreiqvar kgpcdrcgqc
      541 rfgalceaet grcvcpsecv alaqpvcgsd ghtypsecml hvhacthqis lhvasagpce
      601 tcgdavcafg avcsagqcvc prcehpppgp vcgsdgvtyg sacelreaac lqqtqieear
      661 agpceqaecg sggsgsgedg dceqelcrqr ggiwdedsed gpcvcdfscq svpgspvcgs
      721 dgvtystece lkkarcesqr glyvaaqgac rgptfaplpp vaplhcaqtp ygccqdnita
      781 argvglagcp sacqcnphgs yggtcdpatg qcscrpgvgg lrcdrcepgf wnfrgivtdg
      841 rsgctpcscd pqgavrddce qmtglcsckp gvagpkcgqc pdgralgpag ceadasapat
      901 caemrcefga rcveesgsah cvcpmltcpe anatkvcgsd gvtygnecql ktiacrqglq
      961 isiqslgpcq eavapsthpt sasvtvttpg lllsqalpap pgalplapss tahsqttppp
     1021 ssrprttasv prttvwpvlt vpptapspap slvasafges gstdgssdee lsgdqeasgg
     1081 gsgglepleg ssvatpgppv erascynsal gccsdgktps ldaegsncpa tkvfqgvlel
     1141 egvegqelfy tpemadpkse lfgetarsie stlddlfrns dvkkdfrsvr lrdlgpgksv
     1201 raivdvhfdp ttafrapdva rallrqiqvs rrrslgvrrp lqehvrfmdf dwfpafitga
     1261 tsgaiaagat arattasrlp ssavtpraph pshtsqpvak ttaapttrrp pttapsrvpg
     1321 rrppapqqpp kpcdsqpcfh ggtcqdwalg ggftcscpag rggavcekvl gapvpafegr
     1381 sflafptlra yhtlrlalef ralepqglll yngnargkdf lalalldgrv qlrfdtgsgp
     1441 avltsavpve pgqwhrlels rhwrrgtlsv dgetpvlges psgtdglnld tdlfvggvpe
     1501 dqaavalert fvgaglrgci rlldvnnqrl elgigpgaat rgsgvgecgd hpclpnpchg
     1561 gapcqnleag rfhcqcppgr vgptcadeks pcqpnpchga apcrvlpegg aqcecplgre
     1621 gtfcqtasgq dgsgpfladf ngfshlelrg lhtfardlge kmalevvfla rgpsglllyn
     1681 gqktdgkgdf vslalrdrrl efrydlgkga avirsrepvt lgawtrvsle rngrkgalrv
     1741 gdgprvlges pvphtvlnlk eplyvggapd fsklaraaav ssgfdgaiql vslggrqllt
     1801 pehvlrqvdv tsfaghpctr asghpclnga scvpreaayv clcpggfsgp hcekglveks
     1861 agdvdtlafd grtfveylna vtesekalqs nhfelslrte atqglvlwsg kateradyva
     1921 laivdghlql synlgsqpvv lrstvpvntn rwlrvvahre qregslqvgn eapvtgsspl
     1981 gatqldtdga lwlgglpelp vgpalpkayg tgfvgclrdv vvgrhplhll edavtkpelr
     2041 pcptp
//
LOCUS       NP_038656                753 aa            linear   ROD 27-APR-2025
DEFINITION  neuroendocrine convertase 1 precursor [Mus musculus].
ACCESSION   NP_038656
VERSION     NP_038656.1
DBSOURCE    REFSEQ: accession NM_013628.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Moeller,J. and Meier,D.T.
  TITLE     Ablation of PC1/3 in POMC-Expressing Tissues but Not in Immune
            Cells Induces Sepsis Hypersensitivity
  JOURNAL   J Endocr Soc 8 (11), bvae171 (2024)
   PUBMED   39435302
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Lu,C., Zhang,J., Wang,B., Gao,Q., Ma,K., Pei,S., Li,J. and Cui,S.
  TITLE     Casein kinase 1alpha is required to maintain murine hypothalamic
            pro-opiomelanocortin expression
  JOURNAL   iScience 26 (5), 106670 (2023)
   PUBMED   37168577
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Ni,Z., Wang,Y., Shi,C., Zhang,X., Gong,H. and Dong,Y.
  TITLE     Islet MC4R Regulates PC1/3 to Improve Insulin Secretion in T2DM
            Mice via the cAMP and beta-arrestin-1 Pathways
  JOURNAL   Appl Biochem Biotechnol 194 (12), 6164-6178 (2022)
   PUBMED   35900711
  REMARK    GeneRIF: Islet MC4R Regulates PC1/3 to Improve Insulin Secretion in
            T2DM Mice via the cAMP and beta-arrestin-1 Pathways.
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Meier,D.T., Rachid,L., Wiedemann,S.J., Traub,S., Trimigliozzi,K.,
            Stawiski,M., Sauteur,L., Winter,D.V., Le Foll,C., Bregere,C.,
            Guzman,R., Odermatt,A., Boni-Schnetzler,M. and Donath,M.Y.
  TITLE     Prohormone convertase 1/3 deficiency causes obesity due to impaired
            proinsulin processing
  JOURNAL   Nat Commun 13 (1), 4761 (2022)
   PUBMED   35963866
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Steiner,D.F., Smeekens,S.P., Ohagi,S. and Chan,S.J.
  TITLE     The new enzymology of precursor processing endoproteases
  JOURNAL   J Biol Chem 267 (33), 23435-23438 (1992)
   PUBMED   1429684
  REMARK    Review article
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Copeland,N.G., Gilbert,D.J., Chretien,M., Seidah,N.G. and
            Jenkins,N.A.
  TITLE     Regional localization of three convertases, PC1 (Nec-1), PC2
            (Nec-2), and furin (Fur), on mouse chromosomes
  JOURNAL   Genomics 13 (4), 1356-1358 (1992)
   PUBMED   1354647
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Seidah,N.G., Mattei,M.G., Gaspar,L., Benjannet,S., Mbikay,M. and
            Chretien,M.
  TITLE     Chromosomal assignments of the genes for neuroendocrine convertase
            PC1 (NEC1) to human 5q15-21, neuroendocrine convertase PC2 (NEC2)
            to human 20p11.1-11.2, and furin (mouse 7[D1-E2] region)
  JOURNAL   Genomics 11 (1), 103-107 (1991)
   PUBMED   1765368
REFERENCE   9  (residues 1 to 753)
  AUTHORS   Korner,J., Chun,J., Harter,D. and Axel,R.
  TITLE     Isolation and functional expression of a mammalian prohormone
            processing enzyme, murine prohormone convertase 1
  JOURNAL   Proc Natl Acad Sci U S A 88 (15), 6834-6838 (1991)
   PUBMED   1862107
REFERENCE   10 (residues 1 to 753)
  AUTHORS   Nakayama,K., Hosaka,M., Hatsuzawa,K. and Murakami,K.
  TITLE     Cloning and functional expression of a novel endoprotease involved
            in prohormone processing at dibasic sites
  JOURNAL   J Biochem 109 (6), 803-806 (1991)
   PUBMED   1657897
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158543.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M69196.1, X57088.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 40.63 cM"
     Protein         1..753
                     /product="neuroendocrine convertase 1 precursor"
                     /EC_number="3.4.21.93"
                     /note="neuroendocrine convertase 1; furin homolog;
                     prohormone convertase 1; propeptide-processing protease;
                     prohormone convertase 1/3"
                     /calculated_mol_wt=81081
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P63239.1)"
                     /calculated_mol_wt=3112
     Region          34..110
                     /region_name="S8_pro-domain"
                     /note="Peptidase S8 pro-domain; pfam16470"
                     /db_xref="CDD:465126"
     mat_peptide     111..753
                     /product="Neuroendocrine convertase 1. /id=PRO_0000027060"
                     /note="propagated from UniProtKB/Swiss-Prot (P63239.1)"
                     /calculated_mol_wt=71407
     Region          121..415
                     /region_name="Peptidases_S8_Protein_convertases_Kexins_Fur
                     in-lik"
                     /note="Peptidase S8 family domain in Protein convertases;
                     cd04059"
                     /db_xref="CDD:173789"
     Site            order(123,176,222)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173789"
     Site            order(167..168,205,208,250,268,278,309,320,382)
                     /site_type="active"
                     /db_xref="CDD:173789"
     Site            order(167,208,382)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173789"
     Site            order(315,345)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173789"
     Site            order(323,325,328,330)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:173789"
     Site            401
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P63239.1)"
     Region          504..591
                     /region_name="P_proprotein"
                     /note="Proprotein convertase P-domain; pfam01483"
                     /db_xref="CDD:460225"
     Region          633..663
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63239.1)"
     Site            645
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P63239.1)"
     Region          713..751
                     /region_name="Proho_convert"
                     /note="Prohormone convertase enzyme; pfam12177"
                     /db_xref="CDD:463483"
     CDS             1..753
                     /gene="Pcsk1"
                     /gene_synonym="Nec-1; Nec1; PC1; PC3; Phpp-1; SPC3"
                     /coded_by="NM_013628.3:206..2467"
                     /db_xref="CCDS:CCDS26649.1"
                     /db_xref="GeneID:18548"
                     /db_xref="MGI:MGI:97511"
ORIGIN      
        1 meqrgwtlqc tafaffcvwc alnsvkakrq fvnewaaeip ggqeaasaia eelgydllgq
       61 igslenhylf khkshprrsr rsalhitkrl sdddrvtwae qqyekerskr svqkdsaldl
      121 fndpmwnqqw ylqdtrmtaa lpkldlhvip vwekgitgkg vvitvlddgl ewnhtdiyan
      181 ydpeasydfn dndhdpfpry dltnenkhgt rcageiamqa nnhkcgvgva ynskvggirm
      241 ldgivtdaie assigfnpgh vdiysaswgp nddgktvegp grlaqkafey gvkqgrqgkg
      301 sifvwasgng grqgdncdcd gytdsiytis issasqqgls pwyaekcsst latsyssgdy
      361 tdqritsadl hndctethtg tsasaplaag ifalaleanp nltwrdmqhl vvwtseydpl
      421 asnpgwkkng aglmvnsrfg fgllnakalv dladprtwrn vpekkecvvk dnnfepralk
      481 angeviveip tracegqena ikslehvqfe atieysrrgd lhvtltsavg tstvllaere
      541 rdtspngfkn wdfmsvhtwg enpvgtwtlk itdmsgrmqn egrivnwkli lhgtssqpeh
      601 mkqprvytsy ntvqndrrgv ekmvnvvekr ptqkslngnl lvpknssssn vegrrdeqvq
      661 gtpskamlrl lqsafsknal skqspkksps aklsipyesf yealeklnkp sklegsedsl
      721 ysdyvdvfyn tkpykhrddr llqalmdiln een
//
LOCUS       NP_001137324             498 aa            linear   PRI 27-APR-2025
DEFINITION  trichoplein keratin filament-binding protein [Homo sapiens].
ACCESSION   NP_001137324
VERSION     NP_001137324.1
DBSOURCE    REFSEQ: accession NM_001143852.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Andersen,J.S., Vijayakumaran,A., Godbehere,C., Lorentzen,E.,
            Mennella,V. and Schou,K.B.
  TITLE     Uncovering structural themes across cilia microtubule inner
            proteins with implications for human cilia function
  JOURNAL   Nat Commun 15 (1), 2687 (2024)
   PUBMED   38538594
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 498)
  AUTHORS   Buraschi,S., Neill,T. and Iozzo,R.V.
  TITLE     Decorin is a devouring proteoglycan: Remodeling of intracellular
            catabolism via autophagy and mitophagy
  JOURNAL   Matrix Biol 75-76, 260-270 (2019)
   PUBMED   29080840
  REMARK    GeneRIF: Soluble matrix-derived cues being transduced downstream of
            receptor engagement converge upon a newly-discovered nexus of
            autophagic machinery consisting of Peg3 for endothelial cell
            autophagy and mitostatin for tumor cell mitophagy.
            Review article
REFERENCE   6  (residues 1 to 498)
  AUTHORS   Tokumasu,F., Fairhurst,R.M., Ostera,G.R., Brittain,N.J., Hwang,J.,
            Wellems,T.E. and Dvorak,J.A.
  TITLE     Band 3 modifications in Plasmodium falciparum-infected AA and CC
            erythrocytes assayed by autocorrelation analysis using quantum dots
  JOURNAL   J Cell Sci 118 (Pt 5), 1091-1098 (2005)
   PUBMED   15731014
REFERENCE   7  (residues 1 to 498)
  AUTHORS   Nishizawa,M., Izawa,I., Inoko,A., Hayashi,Y., Nagata,K.,
            Yokoyama,T., Usukura,J. and Inagaki,M.
  TITLE     Identification of trichoplein, a novel keratin filament-binding
            protein
  JOURNAL   J Cell Sci 118 (Pt 5), 1081-1090 (2005)
   PUBMED   15731013
  REMARK    GeneRIF: trichoplein is a keratin 8/18-binding protein that may be
            involved in the organization of the apical network of keratin
            filaments and desmosomes in simple epithelial cells
REFERENCE   8  (residues 1 to 498)
  AUTHORS   Panzegrau,B., Gordon,L. and Goudy,G.H.
  TITLE     Outpatient therapeutic 131I for thyroid cancer
  JOURNAL   J Nucl Med Technol 33 (1), 28-30 (2005)
   PUBMED   15731017
REFERENCE   9  (residues 1 to 498)
  AUTHORS   Katanick,S.L.
  CONSRTM   Intersocietal Commission for the Accrediation of Nuclear Medicine
            Laboratories
  TITLE     Fundamentals of ICANL accreditation
  JOURNAL   J Nucl Med Technol 33 (1), 19-23 (2005)
   PUBMED   15731016
REFERENCE   10 (residues 1 to 498)
  AUTHORS   Seibert,J.A. and Boone,J.M.
  TITLE     X-ray imaging physics for nuclear medicine technologists. Part 2:
            X-ray interactions and image formation
  JOURNAL   J Nucl Med Technol 33 (1), 3-18 (2005)
   PUBMED   15731015
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK092736.1, BC004285.1, AY007230.1 and AK000079.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.96755.1,
                                           SRR1803613.151273.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000405876.9/ ENSP00000384520.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..498
                     /product="trichoplein keratin filament-binding protein"
                     /note="mitostatin; tumor suppressor protein; mitochondrial
                     protein with oncostatic activity"
                     /calculated_mol_wt=60941
     Region          73..498
                     /region_name="Interaction with keratin proteins.
                     /evidence=ECO:0000269|PubMed:15731013"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT92.1)"
     Region          146..483
                     /region_name="TPH"
                     /note="Trichohyalin-plectin-homology domain; pfam13868"
                     /db_xref="CDD:464007"
     Region          167..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT92.1)"
     Region          259..425
                     /region_name="Trichohyalin/plectin homology domain.
                     /evidence=ECO:0000269|PubMed:15731013"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT92.1)"
     Region          447..498
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT92.1)"
     CDS             1..498
                     /gene="TCHP"
                     /gene_synonym="TpMs"
                     /coded_by="NM_001143852.2:154..1650"
                     /db_xref="CCDS:CCDS9137.1"
                     /db_xref="GeneID:84260"
                     /db_xref="HGNC:HGNC:28135"
                     /db_xref="MIM:612654"
ORIGIN      
        1 malptlpsyw csqqrlnqql arqreqearl rqqweqnsry frmsdicssk qaewssktsy
       61 qrsmhayqre kmkeekrrsl earreklrql mqeeqdllar eleelrlsmn lqerrireqh
      121 gklksakeeq rkliaeqlly ehwkknnpkl remeldlhqk hvvnswemqk eekkqqeata
      181 eqenkryene yerarreale rmkaeeerrq ledklqaeal lqqmeelklk eveatklkke
      241 qenllkqrwe lerleeerkq meafrqkael grflrhqyna qlsrrtqqiq eeleadrril
      301 qallekedes qrlhlarreq vmadvawmkq aieeqlqler areaelqmll reeakemwek
      361 reaewarers ardrlmsevl tgrqqqiqek ieqnrraqee slkhreqlir nleevrelar
      421 rekeeseklk sarkqeleaq vaerrlqawe adqqeeeeee earrveqlsd allqqeaetm
      481 aeqgyrpkpy ghpkiawn
//
LOCUS       NP_001354925             106 aa            linear   PRI 27-APR-2025
DEFINITION  ninjurin-2 isoform 3 [Homo sapiens].
ACCESSION   NP_001354925
VERSION     NP_001354925.1
DBSOURCE    REFSEQ: accession NM_001367996.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Sahoo,B., Mou,Z., Liu,W., Dubyak,G. and Dai,X.
  TITLE     How NINJ1 mediates plasma membrane rupture and why NINJ2 cannot
  JOURNAL   Cell 188 (2), 292-302 (2025)
   PUBMED   39667936
REFERENCE   2  (residues 1 to 106)
  AUTHORS   David,L., Borges,J.P., Hollingsworth,L.R., Volchuk,A., Jansen,I.,
            Garlick,E., Steinberg,B.E. and Wu,H.
  TITLE     NINJ1 mediates plasma membrane rupture by cutting and releasing
            membrane disks
  JOURNAL   Cell 187 (9), 2224-2235 (2024)
   PUBMED   38614101
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Khorrami,M., Saneipour,M., Moridnia,A., Shaygannejad,V.,
            Sadeghi,E., Kassani,A., Sarmadi,A. and Mirmosayyeb,O.
  TITLE     Interdependency of NINJ2 gene expression and polymorphism with
            susceptibility and response to interferon beta in patients with
            multiple sclerosis
  JOURNAL   Int J Neurosci 134 (4), 347-352 (2024)
   PUBMED   35912872
  REMARK    GeneRIF: Interdependency of NINJ2 gene expression and polymorphism
            with susceptibility and response to interferon beta in patients
            with multiple sclerosis.
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Yan,Y., Du,X., Dou,X., Li,J., Zhang,W., Yang,S., Meng,W. and
            Tian,G.
  TITLE     Effects of Ninjurin 2 polymorphisms on susceptibility to coronary
            heart disease
  JOURNAL   Cell Cycle 23 (3), 328-337 (2024)
   PUBMED   38512812
  REMARK    GeneRIF: Effects of Ninjurin 2 polymorphisms on susceptibility to
            coronary heart disease.
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Sorosina,M., Peroni,S., Mascia,E., Santoro,S., Osiceanu,A.M.,
            Ferre,L., Clarelli,F., Giordano,A., Cannizzaro,M., Martinelli
            Boneschi,F., Filippi,M. and Esposito,F.
  TITLE     Involvement of NINJ2 Protein in Inflammation and Blood-Brain
            Barrier Transmigration of Monocytes in Multiple Sclerosis
  JOURNAL   Genes (Basel) 13 (11), 1946 (2022)
   PUBMED   36360183
  REMARK    GeneRIF: Involvement of NINJ2 Protein in Inflammation and
            Blood-Brain Barrier Transmigration of Monocytes in Multiple
            Sclerosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Chen,K., Xiao,Z.S., Hou,S.Q., Zhao,R.T., Liu,Y.F., Dou,H.D.,
            Li,G.P., Tao,X.M., Li,F., Zhou,W.Y. and Qiu,C.C.
  TITLE     [Strong association between the NINJ2 gene polymorphism and the
            susceptibility of stroke in Chinese Han population in Fangshan
            district]
  JOURNAL   Beijing Da Xue Xue Bao Yi Xue Ban 42 (5), 498-502 (2010)
   PUBMED   20957003
  REMARK    GeneRIF: There is a significant association between rs11833579 site
            polymorphism of the NINJ2 gene and risk for stroke in Han Chinese.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 106)
  CONSRTM   International Stroke Genetics Consortium; Wellcome Trust
            Case-Control Consortium 2
  TITLE     Failure to validate association between 12p13 variants and ischemic
            stroke
  JOURNAL   N Engl J Med 362 (16), 1547-1550 (2010)
   PUBMED   20410525
  REMARK    GeneRIF: Meta-analysis of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 106)
  AUTHORS   Ikram,M.A., Seshadri,S., Bis,J.C., Fornage,M., DeStefano,A.L.,
            Aulchenko,Y.S., Debette,S., Lumley,T., Folsom,A.R., van den
            Herik,E.G., Bos,M.J., Beiser,A., Cushman,M., Launer,L.J.,
            Shahar,E., Struchalin,M., Du,Y., Glazer,N.L., Rosamond,W.D.,
            Rivadeneira,F., Kelly-Hayes,M., Lopez,O.L., Coresh,J., Hofman,A.,
            DeCarli,C., Heckbert,S.R., Koudstaal,P.J., Yang,Q., Smith,N.L.,
            Kase,C.S., Rice,K., Haritunians,T., Roks,G., de Kort,P.L.,
            Taylor,K.D., de Lau,L.M., Oostra,B.A., Uitterlinden,A.G.,
            Rotter,J.I., Boerwinkle,E., Psaty,B.M., Mosley,T.H., van
            Duijn,C.M., Breteler,M.M., Longstreth,W.T. Jr. and Wolf,P.A.
  TITLE     Genomewide association studies of stroke
  JOURNAL   N Engl J Med 360 (17), 1718-1728 (2009)
   PUBMED   19369658
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 106)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   10 (residues 1 to 106)
  AUTHORS   Araki,T. and Milbrandt,J.
  TITLE     Ninjurin2, a novel homophilic adhesion molecule, is expressed in
            mature sensory and enteric neurons and promotes neurite outgrowth
  JOURNAL   J Neurosci 20 (1), 187-195 (2000)
   PUBMED   10627596
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC021054.28 and AC006205.9.
            
            Summary: The protein encoded by this gene belongs to the ninjurin
            (for nerve injury induced) family. It is a cell surface adhesion
            protein that is upregulated in Schwann cells surrounding the distal
            segment of injured nerve, and promotes neurite outgrowth, thus may
            have a role in nerve regeneration after nerve injury. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (4), as well as variant 3, encodes
            isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.31461.1,
                                           SRR1163658.158812.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..106
                     /product="ninjurin-2 isoform 3"
                     /note="nerve injury-induced protein 2"
                     /calculated_mol_wt=11596
     Region          1..89
                     /region_name="Ninjurin"
                     /note="pfam04923"
                     /db_xref="CDD:461482"
     CDS             1..106
                     /gene="NINJ2"
                     /coded_by="NM_001367996.1:333..653"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS76499.1"
                     /db_xref="GeneID:4815"
                     /db_xref="HGNC:HGNC:7825"
                     /db_xref="MIM:607297"
ORIGIN      
        1 mldvalfmsn amrlkavleq gpsshyyttl vtlislslll qvvigvllvv iarlnlneve
       61 kqwrlnqlnn aatilvfftv vinvfitafg ahktgflaar asrnpl
//
LOCUS       NP_001354874             780 aa            linear   PRI 27-APR-2025
DEFINITION  rho GTPase-activating protein 42 isoform 2 [Homo sapiens].
ACCESSION   NP_001354874 XP_011540919
VERSION     NP_001354874.1
DBSOURCE    REFSEQ: accession NM_001367945.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Li,Q., Dibus,M., Casey,A., Yee,C.S.K., Vargas,S.O., Luo,S.,
            Rosen,S.M., Madden,J.A., Genetti,C.A., Brabek,J., Brownstein,C.A.,
            Kazerounian,S., Raby,B.A., Schmitz-Abe,K., Kennedy,J.C.,
            Fishman,M.P., Mullen,M.P., Taylor,J.M., Rosel,D. and Agrawal,P.B.
  TITLE     A homozygous stop-gain variant in ARHGAP42 is associated with
            childhood interstitial lung disease, systemic hypertension, and
            immunological findings
  JOURNAL   PLoS Genet 17 (7), e1009639 (2021)
   PUBMED   34232960
  REMARK    GeneRIF: A homozygous stop-gain variant in ARHGAP42 is associated
            with childhood interstitial lung disease, systemic hypertension,
            and immunological findings.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Lei,Y., Ludorf,K.L., Yu,X., Benjamin,R.H., Gu,X., Lin,Y.,
            Finnell,R.H., Mitchell,L.E., Musfee,F.I., Malik,S., Canfield,M.A.,
            Morrison,A.C., Hobbs,C.A., Van Zutphen,A.R., Fisher,S. and
            Agopian,A.J.
  TITLE     Maternal Hypertension-Related Genotypes and Congenital Heart
            Defects
  JOURNAL   Am J Hypertens 34 (1), 82-91 (2021)
   PUBMED   32710738
  REMARK    GeneRIF: Maternal Hypertension-Related Genotypes and Congenital
            Heart Defects.
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Bai,X., Mangum,K., Kakoki,M., Smithies,O., Mack,C.P. and
            Taylor,J.M.
  TITLE     GRAF3 serves as a blood volume-sensitive rheostat to control smooth
            muscle contractility and blood pressure
  JOURNAL   Small GTPases 11 (3), 194-203 (2020)
   PUBMED   29099324
  REMARK    GeneRIF: GRAF3 serves as a blood volume-sensitive rheostat to
            control smooth muscle contractility and blood pressure.
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Mangum,K.D., Freeman,E.J., Magin,J.C., Taylor,J.M. and Mack,C.P.
  TITLE     Transcriptional and posttranscriptional regulation of the
            SMC-selective blood pressure-associated gene, ARHGAP42
  JOURNAL   Am J Physiol Heart Circ Physiol 318 (2), H413-H424 (2020)
   PUBMED   31886719
  REMARK    GeneRIF: ARHGAP42 expression was inhibited by micro-RNA 505
            (miR505) which interacted with the ARHGAP42 3'-untranslated region
            (UTR) to facilitate its degradation and by AK124326, a long
            noncoding RNA that overlaps with the ARHGAP42 transcription start
            site on the opposite DNA strand
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Fjorder,A.S., Rasmussen,M.B., Mehrjouy,M.M., Nazaryan-Petersen,L.,
            Hansen,C., Bak,M., Grarup,N., Norremolle,A., Larsen,L.A.,
            Vestergaard,H., Hansen,T., Tommerup,N. and Bache,I.
  TITLE     Haploinsufficiency of ARHGAP42 is associated with hypertension
  JOURNAL   Eur J Hum Genet 27 (8), 1296-1303 (2019)
   PUBMED   30903111
  REMARK    GeneRIF: A decreased expression level of Rho GTPase-activating
            protein 42 gene (ARHGAP42) mRNA in the blood was found in the
            translocation carriers relative to controls.
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Tanikawa,C., Okada,Y., Takahashi,A., Oda,K., Kamatani,N., Kubo,M.,
            Nakamura,Y. and Matsuda,K.
  TITLE     Genome wide association study of age at menarche in the Japanese
            population
  JOURNAL   PLoS One 8 (5), e63821 (2013)
   PUBMED   23667675
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Bai,X., Lenhart,K.C., Bird,K.E., Suen,A.A., Rojas,M., Kakoki,M.,
            Li,F., Smithies,O., Mack,C.P. and Taylor,J.M.
  TITLE     The smooth muscle-selective RhoGAP GRAF3 is a critical regulator of
            vascular tone and hypertension
  JOURNAL   Nat Commun 4, 2910 (2013)
   PUBMED   24335996
  REMARK    GeneRIF: The smooth muscle-selective GRAF3 is a critical regulator
            of vascular tone and hypertension.
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Ehret,G.B., Munroe,P.B., Rice,K.M., Bochud,M., Johnson,A.D.,
            Chasman,D.I., Smith,A.V., Tobin,M.D., Verwoert,G.C., Hwang,S.J.,
            Pihur,V., Vollenweider,P., O'Reilly,P.F., Amin,N.,
            Bragg-Gresham,J.L., Teumer,A., Glazer,N.L., Launer,L., Zhao,J.H.,
            Aulchenko,Y., Heath,S., Sober,S., Parsa,A., Luan,J., Arora,P.,
            Dehghan,A., Zhang,F., Lucas,G., Hicks,A.A., Jackson,A.U.,
            Peden,J.F., Tanaka,T., Wild,S.H., Rudan,I., Igl,W., Milaneschi,Y.,
            Parker,A.N., Fava,C., Chambers,J.C., Fox,E.R., Kumari,M., Go,M.J.,
            van der Harst,P., Kao,W.H., Sjogren,M., Vinay,D.G., Alexander,M.,
            Tabara,Y., Shaw-Hawkins,S., Whincup,P.H., Liu,Y., Shi,G.,
            Kuusisto,J., Tayo,B., Seielstad,M., Sim,X., Nguyen,K.D.,
            Lehtimaki,T., Matullo,G., Wu,Y., Gaunt,T.R., Onland-Moret,N.C.,
            Cooper,M.N., Platou,C.G., Org,E., Hardy,R., Dahgam,S., Palmen,J.,
            Vitart,V., Braund,P.S., Kuznetsova,T., Uiterwaal,C.S., Adeyemo,A.,
            Palmas,W., Campbell,H., Ludwig,B., Tomaszewski,M., Tzoulaki,I.,
            Palmer,N.D., Aspelund,T., Garcia,M., Chang,Y.P., O'Connell,J.R.,
            Steinle,N.I., Grobbee,D.E., Arking,D.E., Kardia,S.L.,
            Morrison,A.C., Hernandez,D., Najjar,S., McArdle,W.L., Hadley,D.,
            Brown,M.J., Connell,J.M., Hingorani,A.D., Day,I.N., Lawlor,D.A.,
            Beilby,J.P., Lawrence,R.W., Clarke,R., Hopewell,J.C., Ongen,H.,
            Dreisbach,A.W., Li,Y., Young,J.H., Bis,J.C., Kahonen,M.,
            Viikari,J., Adair,L.S., Lee,N.R., Chen,M.H., Olden,M., Pattaro,C.,
            Bolton,J.A., Kottgen,A., Bergmann,S., Mooser,V., Chaturvedi,N.,
            Frayling,T.M., Islam,M., Jafar,T.H., Erdmann,J., Kulkarni,S.R.,
            Bornstein,S.R., Grassler,J., Groop,L., Voight,B.F., Kettunen,J.,
            Howard,P., Taylor,A., Guarrera,S., Ricceri,F., Emilsson,V.,
            Plump,A., Barroso,I., Khaw,K.T., Weder,A.B., Hunt,S.C., Sun,Y.V.,
            Bergman,R.N., Collins,F.S., Bonnycastle,L.L., Scott,L.J.,
            Stringham,H.M., Peltonen,L., Perola,M., Vartiainen,E., Brand,S.M.,
            Staessen,J.A., Wang,T.J., Burton,P.R., Soler Artigas,M., Dong,Y.,
            Snieder,H., Wang,X., Zhu,H., Lohman,K.K., Rudock,M.E.,
            Heckbert,S.R., Smith,N.L., Wiggins,K.L., Doumatey,A., Shriner,D.,
            Veldre,G., Viigimaa,M., Kinra,S., Prabhakaran,D., Tripathy,V.,
            Langefeld,C.D., Rosengren,A., Thelle,D.S., Corsi,A.M.,
            Singleton,A., Forrester,T., Hilton,G., McKenzie,C.A., Salako,T.,
            Iwai,N., Kita,Y., Ogihara,T., Ohkubo,T., Okamura,T., Ueshima,H.,
            Umemura,S., Eyheramendy,S., Meitinger,T., Wichmann,H.E., Cho,Y.S.,
            Kim,H.L., Lee,J.Y., Scott,J., Sehmi,J.S., Zhang,W., Hedblad,B.,
            Nilsson,P., Smith,G.D., Wong,A., Narisu,N., Stancakova,A.,
            Raffel,L.J., Yao,J., Kathiresan,S., O'Donnell,C.J., Schwartz,S.M.,
            Ikram,M.A., Longstreth,W.T. Jr., Mosley,T.H., Seshadri,S.,
            Shrine,N.R., Wain,L.V., Morken,M.A., Swift,A.J., Laitinen,J.,
            Prokopenko,I., Zitting,P., Cooper,J.A., Humphries,S.E., Danesh,J.,
            Rasheed,A., Goel,A., Hamsten,A., Watkins,H., Bakker,S.J., van
            Gilst,W.H., Janipalli,C.S., Mani,K.R., Yajnik,C.S., Hofman,A.,
            Mattace-Raso,F.U., Oostra,B.A., Demirkan,A., Isaacs,A.,
            Rivadeneira,F., Lakatta,E.G., Orru,M., Scuteri,A., Ala-Korpela,M.,
            Kangas,A.J., Lyytikainen,L.P., Soininen,P., Tukiainen,T., Wurtz,P.,
            Ong,R.T., Dorr,M., Kroemer,H.K., Volker,U., Volzke,H., Galan,P.,
            Hercberg,S., Lathrop,M., Zelenika,D., Deloukas,P., Mangino,M.,
            Spector,T.D., Zhai,G., Meschia,J.F., Nalls,M.A., Sharma,P.,
            Terzic,J., Kumar,M.V., Denniff,M., Zukowska-Szczechowska,E.,
            Wagenknecht,L.E., Fowkes,F.G., Charchar,F.J., Schwarz,P.E.,
            Hayward,C., Guo,X., Rotimi,C., Bots,M.L., Brand,E., Samani,N.J.,
            Polasek,O., Talmud,P.J., Nyberg,F., Kuh,D., Laan,M., Hveem,K.,
            Palmer,L.J., van der Schouw,Y.T., Casas,J.P., Mohlke,K.L.,
            Vineis,P., Raitakari,O., Ganesh,S.K., Wong,T.Y., Tai,E.S.,
            Cooper,R.S., Laakso,M., Rao,D.C., Harris,T.B., Morris,R.W.,
            Dominiczak,A.F., Kivimaki,M., Marmot,M.G., Miki,T., Saleheen,D.,
            Chandak,G.R., Coresh,J., Navis,G., Salomaa,V., Han,B.G., Zhu,X.,
            Kooner,J.S., Melander,O., Ridker,P.M., Bandinelli,S.,
            Gyllensten,U.B., Wright,A.F., Wilson,J.F., Ferrucci,L., Farrall,M.,
            Tuomilehto,J., Pramstaller,P.P., Elosua,R., Soranzo,N.,
            Sijbrands,E.J., Altshuler,D., Loos,R.J., Shuldiner,A.R., Gieger,C.,
            Meneton,P., Uitterlinden,A.G., Wareham,N.J., Gudnason,V.,
            Rotter,J.I., Rettig,R., Uda,M., Strachan,D.P., Witteman,J.C.,
            Hartikainen,A.L., Beckmann,J.S., Boerwinkle,E., Vasan,R.S.,
            Boehnke,M., Larson,M.G., Jarvelin,M.R., Psaty,B.M., Abecasis,G.R.,
            Chakravarti,A., Elliott,P., van Duijn,C.M., Newton-Cheh,C.,
            Levy,D., Caulfield,M.J. and Johnson,T.
  CONSRTM   International Consortium for Blood Pressure Genome-Wide Association
            Studies; CARDIoGRAM consortium; CKDGen Consortium; KidneyGen
            Consortium; EchoGen consortium; CHARGE-HF consortium
  TITLE     Genetic variants in novel pathways influence blood pressure and
            cardiovascular disease risk
  JOURNAL   Nature 478 (7367), 103-109 (2011)
   PUBMED   21909115
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Wain,L.V., Verwoert,G.C., O'Reilly,P.F., Shi,G., Johnson,T.,
            Johnson,A.D., Bochud,M., Rice,K.M., Henneman,P., Smith,A.V.,
            Ehret,G.B., Amin,N., Larson,M.G., Mooser,V., Hadley,D., Dorr,M.,
            Bis,J.C., Aspelund,T., Esko,T., Janssens,A.C., Zhao,J.H., Heath,S.,
            Laan,M., Fu,J., Pistis,G., Luan,J., Arora,P., Lucas,G., Pirastu,N.,
            Pichler,I., Jackson,A.U., Webster,R.J., Zhang,F., Peden,J.F.,
            Schmidt,H., Tanaka,T., Campbell,H., Igl,W., Milaneschi,Y.,
            Hottenga,J.J., Vitart,V., Chasman,D.I., Trompet,S.,
            Bragg-Gresham,J.L., Alizadeh,B.Z., Chambers,J.C., Guo,X.,
            Lehtimaki,T., Kuhnel,B., Lopez,L.M., Polasek,O., Boban,M.,
            Nelson,C.P., Morrison,A.C., Pihur,V., Ganesh,S.K., Hofman,A.,
            Kundu,S., Mattace-Raso,F.U., Rivadeneira,F., Sijbrands,E.J.,
            Uitterlinden,A.G., Hwang,S.J., Vasan,R.S., Wang,T.J., Bergmann,S.,
            Vollenweider,P., Waeber,G., Laitinen,J., Pouta,A., Zitting,P.,
            McArdle,W.L., Kroemer,H.K., Volker,U., Volzke,H., Glazer,N.L.,
            Taylor,K.D., Harris,T.B., Alavere,H., Haller,T., Keis,A.,
            Tammesoo,M.L., Aulchenko,Y., Barroso,I., Khaw,K.T., Galan,P.,
            Hercberg,S., Lathrop,M., Eyheramendy,S., Org,E., Sober,S., Lu,X.,
            Nolte,I.M., Penninx,B.W., Corre,T., Masciullo,C., Sala,C.,
            Groop,L., Voight,B.F., Melander,O., O'Donnell,C.J., Salomaa,V.,
            d'Adamo,A.P., Fabretto,A., Faletra,F., Ulivi,S., Del Greco,F.,
            Facheris,M., Collins,F.S., Bergman,R.N., Beilby,J.P., Hung,J.,
            Musk,A.W., Mangino,M., Shin,S.Y., Soranzo,N., Watkins,H., Goel,A.,
            Hamsten,A., Gider,P., Loitfelder,M., Zeginigg,M., Hernandez,D.,
            Najjar,S.S., Navarro,P., Wild,S.H., Corsi,A.M., Singleton,A., de
            Geus,E.J., Willemsen,G., Parker,A.N., Rose,L.M., Buckley,B.,
            Stott,D., Orru,M., Uda,M., van der Klauw,M.M., Zhang,W., Li,X.,
            Scott,J., Chen,Y.D., Burke,G.L., Kahonen,M., Viikari,J., Doring,A.,
            Meitinger,T., Davies,G., Starr,J.M., Emilsson,V., Plump,A.,
            Lindeman,J.H., Hoen,P.A., Konig,I.R., Felix,J.F., Clarke,R.,
            Hopewell,J.C., Ongen,H., Breteler,M., Debette,S., Destefano,A.L.,
            Fornage,M., Mitchell,G.F., Smith,N.L., Holm,H., Stefansson,K.,
            Thorleifsson,G., Thorsteinsdottir,U., Samani,N.J., Preuss,M.,
            Rudan,I., Hayward,C., Deary,I.J., Wichmann,H.E., Raitakari,O.T.,
            Palmas,W., Kooner,J.S., Stolk,R.P., Jukema,J.W., Wright,A.F.,
            Boomsma,D.I., Bandinelli,S., Gyllensten,U.B., Wilson,J.F.,
            Ferrucci,L., Schmidt,R., Farrall,M., Spector,T.D., Palmer,L.J.,
            Tuomilehto,J., Pfeufer,A., Gasparini,P., Siscovick,D.,
            Altshuler,D., Loos,R.J., Toniolo,D., Snieder,H., Gieger,C.,
            Meneton,P., Wareham,N.J., Oostra,B.A., Metspalu,A., Launer,L.,
            Rettig,R., Strachan,D.P., Beckmann,J.S., Witteman,J.C., Erdmann,J.,
            van Dijk,K.W., Boerwinkle,E., Boehnke,M., Ridker,P.M.,
            Jarvelin,M.R., Chakravarti,A., Abecasis,G.R., Gudnason,V.,
            Newton-Cheh,C., Levy,D., Munroe,P.B., Psaty,B.M., Caulfield,M.J.,
            Rao,D.C., Tobin,M.D., Elliott,P. and van Duijn,C.M.
  CONSRTM   LifeLines Cohort Study; EchoGen consortium; AortaGen Consortium;
            CHARGE Consortium Heart Failure Working Group; KidneyGen
            consortium; CKDGen consortium; Cardiogenics consortium; CardioGram
  TITLE     Genome-wide association study identifies six new loci influencing
            pulse pressure and mean arterial pressure
  JOURNAL   Nat Genet 43 (10), 1005-1011 (2011)
   PUBMED   21909110
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Eberth,A., Lundmark,R., Gremer,L., Dvorsky,R., Koessmeier,K.T.,
            McMahon,H.T. and Ahmadian,M.R.
  TITLE     A BAR domain-mediated autoinhibitory mechanism for RhoGAPs of the
            GRAF family
  JOURNAL   Biochem J 417 (1), 371-377 (2009)
   PUBMED   18954304
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001351.5, AC015600.8 and
            AP000872.5.
            
            On Jan 1, 2019 this sequence version replaced XP_011540919.1.
            
            Summary: This gene encodes a Rho GTPase-activating protein
            (RhoGAP), and member of the GRAF or BAR-PH family of proteins.
            Expression of this gene is enriched in vascular smooth muscle cells
            and the encoded protein inhibits RhoA activity to regulate vascular
            tone and control blood pressure. A mutation in the first intron of
            this gene modulates its expression and is associated with reduced
            blood pressure in human patients with borderline hypertension.
            [provided by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1660809.159280.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.1"
     Protein         1..780
                     /product="rho GTPase-activating protein 42 isoform 2"
                     /note="rho GTPase-activating protein 42; rho-type
                     GTPase-activating protein 42; transmembrane protein 133"
                     /calculated_mol_wt=87589
     Region          <11..131
                     /region_name="BAR"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain, a
                     dimerization module that binds membranes and detects
                     membrane curvature; cl12013"
                     /db_xref="CDD:472257"
     Region          173..282
                     /region_name="BAR-PH_GRAF_family"
                     /note="GTPase Regulator Associated with Focal adhesion and
                     related proteins Pleckstrin homology (PH) domain; cd01249"
                     /db_xref="CDD:269953"
     Region          275..473
                     /region_name="RhoGAP_Graf"
                     /note="GTPase-activator protein (GAP) domain for Rho-like
                     GTPases found in GRAF (GTPase regulator associated with
                     focal adhesion kinase); Graf is a multi-domain protein,
                     containing SH3 and PH domains, that binds focal adhesion
                     kinase and influences cytoskeletal...; cd04374"
                     /db_xref="CDD:239839"
     Site            order(323,364,368,437,440..441,464)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239839"
     Site            323
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239839"
     Region          726..780
                     /region_name="SH3_GRAF3"
                     /note="Src Homology 3 domain of GTPase Regulator
                     Associated with Focal adhesion kinase 3; cd12066"
                     /db_xref="CDD:212999"
     Site            order(731,733,736,740,759..760,773,775..776)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212999"
     CDS             1..780
                     /gene="ARHGAP42"
                     /gene_synonym="AD031; GRAF3; TMEM133"
                     /coded_by="NM_001367945.1:974..3316"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:143872"
                     /db_xref="HGNC:HGNC:26545"
                     /db_xref="MIM:615936"
ORIGIN      
        1 mawlncdelp iqnandvlia plekfrkeqi gaakdgkkkf dkesekyysi lekhlnlsak
       61 kkeshlqead tqidrehqnf yeasleyvfk iqevqekkkf efvepllsfl qglftfyheg
      121 yelaqefapy kqqlqfnlqn trnnfestrq everlmqrmk sanqdyrpps qwtmegylyv
      181 qekrplgftw ikhyctydkg sktftmsvse mkssgkmngl vtsspemfkl kscirrktds
      241 idkrfcfdie vverhgiitl qafseanrkl wleamdgkep iytlpaiisk keemylneag
      301 fnfvrkciqa vetrgitilg lyriggvnsk vqklmnttfs pksppdidid ielwdnktit
      361 sglknylrcl aeplmtyklh kdfiiavksd dqnyrveavh alvhklpekn remldilikh
      421 lvkvslhsqq nlmtvsnlgv ifgptlmraq eetvaammni kfqnivveil iehyekifht
      481 apdpsiplpq pqsrsgsrrt raiclstgsr kprgrytpcl aepdsdsyss spdstpmgsi
      541 eslsshsseq nsttksascq preksggipw iatpsssngq kslglwttsp esssredatk
      601 tdaesdcqsv asvtspgdvs ppidlvkkep yglsglkras asslrsisaa egnksysgsi
      661 qsltsvgske tpkaspnpdl ppkmcrrlrl dtassngyqr pgsvvaakaq lfenvgspkp
      721 vssgrqakam ysckaehshe lsfpqgaifs nvypsvepgw lkatyegktg lvpenyvvfl
//
LOCUS       NP_004996                179 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 isoform
            1 [Homo sapiens].
ACCESSION   NP_004996
VERSION     NP_004996.1
DBSOURCE    REFSEQ: accession NM_005005.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Ye,Z. and Connor,J.R.
  TITLE     cDNA cloning by amplification of circularized first strand cDNAs
            reveals non-IRE-regulated iron-responsive mRNAs
  JOURNAL   Biochem Biophys Res Commun 275 (1), 223-227 (2000)
   PUBMED   10944468
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Lin,X., Wells,D.E., Kimberling,W.J. and Kumar,S.
  TITLE     Human NDUFB9 gene: genomic organization and a possible candidate
            gene associated with deafness disorder mapped to chromosome 8q13
  JOURNAL   Hum Hered 49 (2), 75-80 (1999)
   PUBMED   10077726
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Emahazion,T., Beskow,A., Gyllensten,U. and Brookes,A.J.
  TITLE     Intron based radiation hybrid mapping of 15 complex I genes of the
            human electron transport chain
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 115-119 (1998)
   PUBMED   9763677
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Gu,J.Z., Lin,X. and Wells,D.E.
  TITLE     The human B22 subunit of the NADH-ubiquinone oxidoreductase maps to
            the region of chromosome 8 involved in branchio-oto-renal syndrome
  JOURNAL   Genomics 35 (1), 6-10 (1996)
   PUBMED   8661098
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AI907018.1 and AF261090.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a subunit of the
            mitochondrial oxidative phosphorylation complex I (nicotinamide
            adenine dinucleotide: ubiquinone oxidoreductase). Complex I is
            localized to the inner mitochondrial membrane and functions to
            dehydrogenate nicotinamide adenine dinucleotide and to shuttle
            electrons to coenzyme Q. Complex I deficiency is the most common
            defect found in oxidative phosphorylation disorders and results in
            a range of conditions, including lethal neonatal disease,
            hypertrophic cardiomyopathy, liver disease, and adult-onset
            neurodegenerative disorders. Pseudogenes of this gene are found on
            chromosomes five, seven and eight. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.78573.1,
                                           SRR5189661.147724.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000276689.8/
                                                  ENSP00000276689.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..179
                     /product="NADH dehydrogenase [ubiquinone] 1 beta
                     subcomplex subunit 9 isoform 1"
                     /note="complex I B22 subunit; LYR motif-containing protein
                     3; NADH-ubiquinone oxidoreductase B22 subunit; NADH
                     dehydrogenase (ubiquinone) 1 beta subcomplex, 9, 22kDa"
                     /calculated_mol_wt=21700
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6M9.3)"
     Region          12..88
                     /region_name="Complex1_LYR_NDUFB9_LYRM3"
                     /note="LYR (leucine-tyrosine-arginine) motif found in NADH
                     dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
                     (NDUFB9) and similar proteins; cd20263"
                     /db_xref="CDD:380758"
     Site            order(12..13,16,23,26,47..48,51..52,60,63,67,71,74)
                     /site_type="other"
                     /note="phosphopantetheine binding site [chemical binding]"
                     /db_xref="CDD:380758"
     Site            order(14,17..18,20..22,24..25,29..30,34..36,38..40,42,
                     45..46,65,68..70,72..80,82..86,88)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:380758"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6M9.3)"
     Region          136..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6M9.3)"
     CDS             1..179
                     /gene="NDUFB9"
                     /gene_synonym="B22; CI-B22; LYRM3; MC1DN24; UQOR22"
                     /coded_by="NM_005005.3:65..604"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6352.1"
                     /db_xref="GeneID:4715"
                     /db_xref="HGNC:HGNC:7704"
                     /db_xref="MIM:601445"
ORIGIN      
        1 maflasgpyl thqqkvlrly kralrhlesw cvqrdkyryf aclmrarfee hknekdmaka
       61 tqllkeaeee fwyrqhpqpy ifpdspggts yerydcykvp ewclddwhps ekamypdyfa
      121 kreqwkklrr eswerevkql qeetppggpl tealpparke gdlpplwwyi vtrprerpm
//
LOCUS       NP_001356307             375 aa            linear   PRI 27-APR-2025
DEFINITION  nucleosome assembly protein 1-like 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001356307
VERSION     NP_001356307.1
DBSOURCE    REFSEQ: accession NM_001369378.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Tan,L., Cheng,W., Liu,F., Wang,D.O., Wu,L., Cao,N. and Wang,J.
  TITLE     Positive natural selection of N6-methyladenosine on the RNAs of
            processed pseudogenes
  JOURNAL   Genome Biol 22 (1), 180 (2021)
   PUBMED   34120636
  REMARK    GeneRIF: Positive natural selection of N6-methyladenosine on the
            RNAs of processed pseudogenes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Mizuhashi,S., Fukushima,S., Ishibashi,T., Kuriyama,H., Kimura,T.,
            Kanemaru,H., Kajihara,I., Makino,K., Miyashita,A., Aoi,J., Kita,K.
            and Ihn,H.
  TITLE     Nucleosome assembly protein 1-like 4, a new therapeutic target for
            proliferation and invasion of melanoma cells
  JOURNAL   J Dermatol Sci 102 (1), 16-24 (2021)
   PUBMED   33583643
  REMARK    GeneRIF: Nucleosome assembly protein 1-like 4, a new therapeutic
            target for proliferation and invasion of melanoma cells.
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Tanaka,T., Hozumi,Y., Martelli,A.M., Iino,M. and Goto,K.
  TITLE     Nucleosome assembly proteins NAP1L1 and NAP1L4 modulate p53
            acetylation to regulate cell fate
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1866 (12), 118560 (2019)
   PUBMED   31634504
  REMARK    GeneRIF: The NAP1L4 regulates cell fate by controlling the
            expression of p53-responsive proarrest and proapoptotic genes
            through selective modulation of p53 acetylation at specific sites
            during normal homeostasis and in stress-induced responses.
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Tanaka,T., Hozumi,Y., Iino,M. and Goto,K.
  TITLE     NAP1L1 regulates NF-kappaB signaling pathway acting on
            anti-apoptotic Mcl-1 gene expression
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1864 (10), 1759-1768 (2017)
   PUBMED   28687276
  REMARK    GeneRIF: knockdown of NAP1L1 suppresses IkappaBalpha degradation
            and nuclear transport of p65 subunit after treatment with TNF-a
            stimulation, leading to attenuation of the NF-kappaB
            transcriptional activity, whereas NAP1L4 knockdown remains
            silent.results of this study suggest that NAP1L1 downregulation
            renders the cell vulnerable to apoptotic cell death through
            attenuation of NF-kappaB transcriptional activity on the
            anti-apop...
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Rodriguez,P., Ruiz,M.T., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2 is part of multi-protein complexes in HeLa cells
  JOURNAL   J Cell Biochem 93 (2), 398-408 (2004)
   PUBMED   15368365
  REMARK    GeneRIF: NAP-2 is in complex(es) with other proteins, which are
            distinct from histones
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Shikama,N., Chan,H.M., Krstic-Demonacos,M., Smith,L., Lee,C.W.,
            Cairns,W. and La Thangue,N.B.
  TITLE     Functional interaction between nucleosome assembly proteins and
            p300/CREB-binding protein family coactivators
  JOURNAL   Mol Cell Biol 20 (23), 8933-8943 (2000)
   PUBMED   11073993
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Rodriguez,P., Pelletier,J., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2: histone chaperone function and phosphorylation state through
            the cell cycle
  JOURNAL   J Mol Biol 298 (2), 225-238 (2000)
   PUBMED   10764593
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Rodriguez,P., Munroe,D., Prawitt,D., Chu,L.L., Bric,E., Kim,J.,
            Reid,L.H., Davies,C., Nakagama,H., Loebbert,R., Winterpacht,A.,
            Petruzzi,M.J., Higgins,M.J., Nowak,N., Evans,G., Shows,T.,
            Weissman,B.E., Zabel,B., Housman,D.E. and Pelletier,J.
  TITLE     Functional characterization of human nucleosome assembly protein-2
            (NAP1L4) suggests a role as a histone chaperone
  JOURNAL   Genomics 44 (3), 253-265 (1997)
   PUBMED   9325046
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Hu,R.J., Lee,M.P., Johnson,L.A. and Feinberg,A.P.
  TITLE     A novel human homologue of yeast nucleosome assembly protein, 65 kb
            centromeric to the p57KIP2 gene, is biallelically expressed in
            fetal and adult tissues
  JOURNAL   Hum Mol Genet 5 (11), 1743-1748 (1996)
   PUBMED   8923002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC131971.9.
            
            Summary: This gene encodes a member of the nucleosome assembly
            protein (NAP) family which can interact with both core and linker
            histones. It can shuttle between the cytoplasm and nucleus,
            suggesting a role as a histone chaperone. This gene is one of
            several located near the imprinted gene domain of 11p15.5, an
            important tumor-suppressor gene region. Alterations in this region
            have been associated with the Beckwith-Wiedemann syndrome, Wilms
            tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung,
            ovarian, and breast cancer. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.213809.1,
                                           SRR1803612.131216.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..375
                     /product="nucleosome assembly protein 1-like 4 isoform 1"
                     /note="nucleosome assembly protein 2; nucleosome assembly
                     protein 1-like 4b; NAP-2"
                     /calculated_mol_wt=42692
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          65..338
                     /region_name="NAP"
                     /note="Nucleosome assembly protein (NAP); pfam00956"
                     /db_xref="CDD:460010"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P28656; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          116..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          265..271
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          339..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     CDS             1..375
                     /gene="NAP1L4"
                     /gene_synonym="hNAP2; NAP1L4b; NAP2; NAP2L"
                     /coded_by="NM_001369378.1:332..1459"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS41599.1"
                     /db_xref="GeneID:4676"
                     /db_xref="HGNC:HGNC:7640"
                     /db_xref="MIM:601651"
ORIGIN      
        1 madhsfsdgv psdsveaakn asntekltdq vmqnprvlaa lqerldnvph tpssyietlp
       61 kavkrrinal kqlqvrcahi eakfyeevhd lerkyaalyq plfdkrrefi tgdveptdae
      121 sewhseneee eklagdmksk vvvtekaaat aeepdpkgip efwftifrnv dmlselvqey
      181 depilkhlqd ikvkfsdpgq pmsfvlefhf epndyftnsv ltktykmkse pdkadpfsfe
      241 gpeivdcdgc tidwkkgknv tvktikkkqk hkgrgtvrti tkqvpnesff nffnplkasg
      301 dgesldedse ftlasdfeig hffrerivpr avlyftgeai edddnfeege egeeeelegd
      361 eegededdae inpkv
//
LOCUS       NP_001351886             387 aa            linear   ROD 27-APR-2025
DEFINITION  5-hydroxytryptamine receptor 4 isoform 3 [Mus musculus].
ACCESSION   NP_001351886
VERSION     NP_001351886.1
DBSOURCE    REFSEQ: accession NM_001364957.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Hu,S., Kou,Y., Liu,X., Rong,W., Han,H. and Zhang,G.
  TITLE     Activation of the 5-hydroxytryptamine 4 receptor ameliorates tight
            junction barrier dysfunction in the colon of type 1 diabetic mice
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (12), 1874-1883 (2023)
   PUBMED   37766457
  REMARK    GeneRIF: Activation of the 5-hydroxytryptamine 4 receptor
            ameliorates tight junction barrier dysfunction in the colon of type
            1 diabetic mice.
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Karayol,R., Medrihan,L., Warner-Schmidt,J.L., Fait,B.W., Rao,M.N.,
            Holzner,E.B., Greengard,P., Heintz,N. and Schmidt,E.F.
  TITLE     Serotonin receptor 4 in the hippocampus modulates mood and anxiety
  JOURNAL   Mol Psychiatry 26 (6), 2334-2349 (2021)
   PUBMED   33441982
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Bhattarai,Y., Jie,S., Linden,D.R., Ghatak,S., Mars,R.A.T.,
            Williams,B.B., Pu,M., Sonnenburg,J.L., Fischbach,M.A., Farrugia,G.,
            Sha,L. and Kashyap,P.C.
  TITLE     Bacterially Derived Tryptamine Increases Mucus Release by
            Activating a Host Receptor in a Mouse Model of Inflammatory Bowel
            Disease
  JOURNAL   iScience 23 (12), 101798 (2020)
   PUBMED   33299969
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Okumura,M., Hamada,A., Ohsaka,F., Tsuruta,T., Hira,T. and
            Sonoyama,K.
  TITLE     Expression of serotonin receptor HTR4 in glucagon-like
            peptide-1-positive enteroendocrine cells of the murine intestine
  JOURNAL   Pflugers Arch 472 (10), 1521-1532 (2020)
   PUBMED   32870377
  REMARK    GeneRIF: Expression of serotonin receptor HTR4 in glucagon-like
            peptide-1-positive enteroendocrine cells of the murine intestine.
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Kobayashi,K., Mikahara,Y., Murata,Y., Morita,D., Matsuura,S.,
            Segi-Nishida,E. and Suzuki,H.
  TITLE     Predominant Role of Serotonin at the Hippocampal Mossy Fiber
            Synapse with Redundant Monoaminergic Modulation
  JOURNAL   iScience 23 (4), 101025 (2020)
   PUBMED   32283526
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Claeysen,S., Sebben,M., Becamel,C., Bockaert,J. and Dumuis,A.
  TITLE     Novel brain-specific 5-HT4 receptor splice variants show marked
            constitutive activity: role of the C-terminal intracellular domain
  JOURNAL   Mol Pharmacol 55 (5), 910-920 (1999)
   PUBMED   10220570
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Claeysen,S., Faye,P., Sebben,M., Taviaux,S., Bockaert,J. and
            Dumuis,A.
  TITLE     5-HT4 receptors: cloning and expression of new splice variants
  JOURNAL   Ann N Y Acad Sci 861, 49-56 (1998)
   PUBMED   9928238
  REMARK    Review article
REFERENCE   8  (residues 1 to 387)
  AUTHORS   Claeysen,S., Sebben,M., Journot,L., Bockaert,J. and Dumuis,A.
  TITLE     Cloning, expression and pharmacology of the mouse 5-HT(4L) receptor
  JOURNAL   FEBS Lett 398 (1), 19-25 (1996)
   PUBMED   8946946
REFERENCE   9  (residues 1 to 387)
  AUTHORS   Ullmer,C., Schmuck,K., Kalkman,H.O. and Lubbert,H.
  TITLE     Expression of serotonin receptor mRNAs in blood vessels
  JOURNAL   FEBS Lett 370 (3), 215-221 (1995)
   PUBMED   7656980
REFERENCE   10 (residues 1 to 387)
  AUTHORS   Gerald,C., Adham,N., Kao,H.T., Olsen,M.A., Laz,T.M.,
            Schechter,L.E., Bard,J.A., Vaysse,P.J., Hartig,P.R., Branchek,T.A.
            et al.
  TITLE     The 5-HT4 receptor: molecular cloning and pharmacological
            characterization of two splice variants
  JOURNAL   EMBO J 14 (12), 2806-2815 (1995)
   PUBMED   7796807
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC152454.5 and AC131714.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y09587.1, SRR7652917.1059245.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 35.1 cM"
     Protein         1..387
                     /product="5-hydroxytryptamine receptor 4 isoform 3"
                     /note="5-hydroxytryptamine receptor 4"
                     /calculated_mol_wt=44031
     Region          20..323
                     /region_name="7tmA_5-HT4"
                     /note="serotonin receptor subtype 4, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15056"
                     /db_xref="CDD:320184"
     Region          21..47
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320184"
     Region          55..81
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320184"
     Region          93..123
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320184"
     Site            order(96,100..101,104..105,186,193,196..197,200,272,
                     275..276,279,294,298,302)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320184"
     Region          136..159
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320184"
     Region          189..218
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320184"
     Region          252..282
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320184"
     Region          291..316
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320184"
     CDS             1..387
                     /gene="Htr4"
                     /gene_synonym="5-HT-4; 5-HT4; 5-HT<4L>; 5HTR4"
                     /coded_by="NM_001364957.1:48..1211"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS89257.1"
                     /db_xref="GeneID:15562"
                     /db_xref="MGI:MGI:109246"
ORIGIN      
        1 mdkldanvss negfrsvekv vlltflavvi lmailgnllv mvavcrdrql rkiktnyfiv
       61 slafadllvs vlvmpfgaie lvqdiwayge mfclvrtsld vllttasifh lccisldryy
      121 aiccqplvyr nkmtplrial mlggcwvlpm fisflpimqg wnnigivdvi ekrkfshnsn
      181 stwcvfmvnk pyaitcsvva fyipfllmvl ayyriyvtak ehaqqiqmlq ragatsesrp
      241 qpadqhsthr mrtetkaakt lcvimgcfcf cwapffvtni vdpfidytvp eqvwtaflwl
      301 gyinsglnpf lyaflnksfr rafliilccd derykrppil gqtvpcsttt ingsthvlry
      361 tvlhsghhqe leklpihndp eslescf
//
LOCUS       NP_689576                615 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat and LEM domain-containing protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_689576
VERSION     NP_689576.6
DBSOURCE    REFSEQ: accession NM_152363.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Freeman,A.D.J., Declais,A.C., Wilson,T.J. and Lilley,D.M.J.
  TITLE     Biochemical and mechanistic analysis of the cleavage of branched
            DNA by human ANKLE1
  JOURNAL   Nucleic Acids Res 51 (11), 5743-5754 (2023)
   PUBMED   37216589
  REMARK    GeneRIF: Biochemical and mechanistic analysis of the cleavage of
            branched DNA by human ANKLE1.
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Kaspers,M.S., Pogenberg,V., Pett,C., Ernst,S., Ecker,F.,
            Ochtrop,P., Groll,M., Hedberg,C. and Itzen,A.
  TITLE     Dephosphocholination by Legionella effector Lem3 functions through
            remodelling of the switch II region of Rab1b
  JOURNAL   Nat Commun 14 (1), 2245 (2023)
   PUBMED   37076474
  REMARK    GeneRIF: Dephosphocholination by Legionella effector Lem3 functions
            through remodelling of the switch II region of Rab1b.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Jiang,H., Kong,N., Liu,Z., West,S.C. and Chan,Y.W.
  TITLE     Human Endonuclease ANKLE1 Localizes at the Midbody and Processes
            Chromatin Bridges to Prevent DNA Damage and cGAS-STING Activation
  JOURNAL   Adv Sci (Weinh) 10 (12), e2204388 (2023)
   PUBMED   36825683
  REMARK    GeneRIF: Human Endonuclease ANKLE1 Localizes at the Midbody and
            Processes Chromatin Bridges to Prevent DNA Damage and cGAS-STING
            Activation.
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Martini,R., Chen,Y., Jenkins,B.D., Elhussin,I.A., Cheng,E.,
            Hoda,S.A., Ginter,P.S., Hanover,J., Zeidan,R.B., Oppong,J.K.,
            Adjei,E.K., Jibril,A., Chitale,D., Bensenhaver,J.M., Awuah,B.,
            Bekele,M., Abebe,E., Kyei,I., Aitpillah,F.S., Adinku,M.O.,
            Ankomah,K., Osei-Bonsu,E.B., Nathansan,S.D., Jackson,L., Jiagge,E.,
            Petersen,L.F., Proctor,E., Nikolinakos,P., Gyan,K.K., Yates,C.,
            Kittles,R., Newman,L.A. and Davis,M.B.
  TITLE     Investigation of triple-negative breast cancer risk alleles in an
            International African-enriched cohort
  JOURNAL   Sci Rep 11 (1), 9247 (2021)
   PUBMED   33927264
  REMARK    GeneRIF: Investigation of triple-negative breast cancer risk
            alleles in an International African-enriched cohort.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Song,J., Freeman,A.D.J., Knebel,A., Gartner,A. and Lilley,D.M.J.
  TITLE     Human ANKLE1 Is a Nuclease Specific for Branched DNA
  JOURNAL   J Mol Biol 432 (21), 5825-5834 (2020)
   PUBMED   32866453
  REMARK    GeneRIF: Human ANKLE1 Is a Nuclease Specific for Branched DNA.
REFERENCE   6  (residues 1 to 615)
  AUTHORS   Brachner,A., Braun,J., Ghodgaonkar,M., Castor,D., Zlopasa,L.,
            Ehrlich,V., Jiricny,J., Gotzmann,J., Knasmuller,S. and Foisner,R.
  TITLE     The endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA
            cleavage in vivo
  JOURNAL   J Cell Sci 125 (Pt 4), 1048-1057 (2012)
   PUBMED   22399800
  REMARK    GeneRIF: Ankle1 is conserved in metazoans and contains a unique
            C-terminal GIY-YIG motif that confers endonuclease activity in
            vitro and in vivo
REFERENCE   7  (residues 1 to 615)
  AUTHORS   Bolton,K.L., Tyrer,J., Song,H., Ramus,S.J., Notaridou,M., Jones,C.,
            Sher,T., Gentry-Maharaj,A., Wozniak,E., Tsai,Y.Y., Weidhaas,J.,
            Paik,D., Van Den Berg,D.J., Stram,D.O., Pearce,C.L., Wu,A.H.,
            Brewster,W., Anton-Culver,H., Ziogas,A., Narod,S.A., Levine,D.A.,
            Kaye,S.B., Brown,R., Paul,J., Flanagan,J., Sieh,W., McGuire,V.,
            Whittemore,A.S., Campbell,I., Gore,M.E., Lissowska,J., Yang,H.P.,
            Medrek,K., Gronwald,J., Lubinski,J., Jakubowska,A., Le,N.D.,
            Cook,L.S., Kelemen,L.E., Brooks-Wilson,A., Massuger,L.F.,
            Kiemeney,L.A., Aben,K.K., van Altena,A.M., Houlston,R.,
            Tomlinson,I., Palmieri,R.T., Moorman,P.G., Schildkraut,J.,
            Iversen,E.S., Phelan,C., Vierkant,R.A., Cunningham,J.M.,
            Goode,E.L., Fridley,B.L., Kruger-Kjaer,S., Blaeker,J., Hogdall,E.,
            Hogdall,C., Gross,J., Karlan,B.Y., Ness,R.B., Edwards,R.P.,
            Odunsi,K., Moyisch,K.B., Baker,J.A., Modugno,F., Heikkinenen,T.,
            Butzow,R., Nevanlinna,H., Leminen,A., Bogdanova,N., Antonenkova,N.,
            Doerk,T., Hillemanns,P., Durst,M., Runnebaum,I., Thompson,P.J.,
            Carney,M.E., Goodman,M.T., Lurie,G., Wang-Gohrke,S., Hein,R.,
            Chang-Claude,J., Rossing,M.A., Cushing-Haugen,K.L., Doherty,J.,
            Chen,C., Rafnar,T., Besenbacher,S., Sulem,P., Stefansson,K.,
            Birrer,M.J., Terry,K.L., Hernandez,D., Cramer,D.W., Vergote,I.,
            Amant,F., Lambrechts,D., Despierre,E., Fasching,P.A.,
            Beckmann,M.W., Thiel,F.C., Ekici,A.B., Chen,X., Johnatty,S.E.,
            Webb,P.M., Beesley,J., Chanock,S., Garcia-Closas,M., Sellers,T.,
            Easton,D.F., Berchuck,A., Chenevix-Trench,G., Pharoah,P.D. and
            Gayther,S.A.
  CONSRTM   Australian Ovarian Cancer Study Group; Australian Cancer Study
            (Ovarian Cancer); Ovarian Cancer Association Consortium
  TITLE     Common variants at 19p13 are associated with susceptibility to
            ovarian cancer
  JOURNAL   Nat Genet 42 (10), 880-884 (2010)
   PUBMED   20852633
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
            Erratum:[Nat Genet. 2016 Jan;48(1):101. doi: 10.1038/ng0116-101b.
            Brook-Wilson, Angela [corrected to Brooks-Wilson, Angela]. PMID:
            26711112]
REFERENCE   8  (residues 1 to 615)
  AUTHORS   Antoniou,A.C., Wang,X., Fredericksen,Z.S., McGuffog,L., Tarrell,R.,
            Sinilnikova,O.M., Healey,S., Morrison,J., Kartsonaki,C.,
            Lesnick,T., Ghoussaini,M., Barrowdale,D., Peock,S., Cook,M.,
            Oliver,C., Frost,D., Eccles,D., Evans,D.G., Eeles,R., Izatt,L.,
            Chu,C., Douglas,F., Paterson,J., Stoppa-Lyonnet,D., Houdayer,C.,
            Mazoyer,S., Giraud,S., Lasset,C., Remenieras,A., Caron,O.,
            Hardouin,A., Berthet,P., Hogervorst,F.B., Rookus,M.A., Jager,A.,
            van den Ouweland,A., Hoogerbrugge,N., van der Luijt,R.B.,
            Meijers-Heijboer,H., Gomez Garcia,E.B., Devilee,P., Vreeswijk,M.P.,
            Lubinski,J., Jakubowska,A., Gronwald,J., Huzarski,T., Byrski,T.,
            Gorski,B., Cybulski,C., Spurdle,A.B., Holland,H., Goldgar,D.E.,
            John,E.M., Hopper,J.L., Southey,M., Buys,S.S., Daly,M.B.,
            Terry,M.B., Schmutzler,R.K., Wappenschmidt,B., Engel,C., Meindl,A.,
            Preisler-Adams,S., Arnold,N., Niederacher,D., Sutter,C.,
            Domchek,S.M., Nathanson,K.L., Rebbeck,T., Blum,J.L., Piedmonte,M.,
            Rodriguez,G.C., Wakeley,K., Boggess,J.F., Basil,J., Blank,S.V.,
            Friedman,E., Kaufman,B., Laitman,Y., Milgrom,R., Andrulis,I.L.,
            Glendon,G., Ozcelik,H., Kirchhoff,T., Vijai,J., Gaudet,M.M.,
            Altshuler,D., Guiducci,C., Loman,N., Harbst,K., Rantala,J.,
            Ehrencrona,H., Gerdes,A.M., Thomassen,M., Sunde,L., Peterlongo,P.,
            Manoukian,S., Bonanni,B., Viel,A., Radice,P., Caldes,T., de la
            Hoya,M., Singer,C.F., Fink-Retter,A., Greene,M.H., Mai,P.L.,
            Loud,J.T., Guidugli,L., Lindor,N.M., Hansen,T.V., Nielsen,F.C.,
            Blanco,I., Lazaro,C., Garber,J., Ramus,S.J., Gayther,S.A.,
            Phelan,C., Narod,S., Szabo,C.I., Benitez,J., Osorio,A.,
            Nevanlinna,H., Heikkinen,T., Caligo,M.A., Beattie,M.S., Hamann,U.,
            Godwin,A.K., Montagna,M., Casella,C., Neuhausen,S.L., Karlan,B.Y.,
            Tung,N., Toland,A.E., Weitzel,J., Olopade,O., Simard,J., Soucy,P.,
            Rubinstein,W.S., Arason,A., Rennert,G., Martin,N.G.,
            Montgomery,G.W., Chang-Claude,J., Flesch-Janys,D., Brauch,H.,
            Severi,G., Baglietto,L., Cox,A., Cross,S.S., Miron,P., Gerty,S.M.,
            Tapper,W., Yannoukakos,D., Fountzilas,G., Fasching,P.A.,
            Beckmann,M.W., Dos Santos Silva,I., Peto,J., Lambrechts,D.,
            Paridaens,R., Rudiger,T., Forsti,A., Winqvist,R., Pylkas,K.,
            Diasio,R.B., Lee,A.M., Eckel-Passow,J., Vachon,C., Blows,F.,
            Driver,K., Dunning,A., Pharoah,P.P., Offit,K., Pankratz,V.S.,
            Hakonarson,H., Chenevix-Trench,G., Easton,D.F. and Couch,F.J.
  CONSRTM   EMBRACE; GEMO Study Collaborators; HEBON; kConFab; SWE-BRCA; MOD
            SQUAD; GENICA
  TITLE     A locus on 19p13 modifies risk of breast cancer in BRCA1 mutation
            carriers and is associated with hormone receptor-negative breast
            cancer in the general population
  JOURNAL   Nat Genet 42 (10), 885-892 (2010)
   PUBMED   20852631
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-gene interaction. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 615)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 615)
  AUTHORS   Lee,K.K. and Wilson,K.L.
  TITLE     All in the family: evidence for four new LEM-domain proteins Lem2
            (NET-25), Lem3, Lem4 and Lem5 in the human genome
  JOURNAL   Symp Soc Exp Biol (56), 329-339 (2004)
   PUBMED   15565891
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK303628.1, AK096688.1 and AC010463.6.
            
            On Nov 9, 2018 this sequence version replaced NP_689576.5.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.280551.1,
                                           SRR1163657.66042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2154529
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000404085.7/ ENSP00000384008.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..615
                     /product="ankyrin repeat and LEM domain-containing protein
                     1 isoform 1"
                     /note="LEM domain containing 6; ankyrin repeat and LEM
                     domain-containing protein 1; LEM-domain containing 3;
                     ankyrin repeat domain-containing protein 41"
                     /calculated_mol_wt=66759
     Region          <22..>128
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          39..71
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAG6.2)"
     Region          75..106
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          75..104
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAG6.2)"
     Region          108..137
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAG6.2)"
     Region          138..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAG6.2)"
     Region          271..280
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000269|PubMed:27245214"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAG6.2)"
     Region          283..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAG6.2)"
     Region          361..398
                     /region_name="LEM_ANKL1"
                     /note="LEM (Lap2/Emerin/Man1) domain found in ankyrin
                     repeat and LEM domain-containing protein 1 (ANKL1);
                     cd12943"
                     /db_xref="CDD:240590"
     Site            order(363..364,376..381,383..384,387..388,390..391)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:240590"
     Region          450..565
                     /region_name="GIY-YIG_COG3680_Meta"
                     /note="GIY-YIG domain of hypothetical proteins from
                     Metazoa; cd10454"
                     /db_xref="CDD:198401"
     Site            order(451..453,486..488)
                     /site_type="other"
                     /note="GIY-YIG motif/motif A"
                     /db_xref="CDD:198401"
     Site            order(453,486,488..489,494,498,551,565)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:198401"
     Site            551
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:198401"
     Region          579..586
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:27245214"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAG6.2)"
     CDS             1..615
                     /gene="ANKLE1"
                     /gene_synonym="ANKRD41; LEM3; LEMD6"
                     /coded_by="NM_152363.6:21..1868"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12354.4"
                     /db_xref="GeneID:126549"
                     /db_xref="HGNC:HGNC:26812"
                     /db_xref="MIM:619348"
ORIGIN      
        1 mcsearlarr lrdalreeep waveellrcg adpnlvledg aaavhlaaga rhprglrclg
       61 allrqggdpn arsvealtpl hvaaawgcrr glelllsqga dpalrdqdgl rpldlalqqg
      121 hlecarvlqd ldtrtrtrtr igaetqepep apgtpglsgp tdetldsial qkqpcrgdnr
      181 digleadpgp pslpvpletv dkhgssaspp ghwdyssdas fvtavevsga edpasdtppw
      241 agslpptrqg llhvvhanqr vprsqgteae lnarlqaltl tppnaagfqs spssmplldr
      301 spahspprtp tpgasdchcl wehqtsidsd matlwltede asstggrepv gpcrhlpvst
      361 vsdlellkgl ralgenphpi tpftrqlyhq qleeaqiapg pefsghslel aaalrtgcip
      421 dvqadedala qqfeqpdpar rwregvvkss ftyllldpre tqdlparafs ltpaerlqtf
      481 iraifyvgkg trarpyvhlw ealghhgrsr kqphqacpkv rqildiwasg cgvvslhcfq
      541 hvvaveaytr eacivealgi qtltnqkqgh cygvvagwpp arrrrlgvhl lhrallvfla
      601 egerqlhpqd iqarg
//
LOCUS       NP_057649                 87 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome c oxidase assembly factor 4 homolog, mitochondrial [Homo
            sapiens].
ACCESSION   NP_057649
VERSION     NP_057649.2
DBSOURCE    REFSEQ: accession NM_016565.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Fischer,M., Horn,S., Belkacemi,A., Kojer,K., Petrungaro,C.,
            Habich,M., Ali,M., Kuttner,V., Bien,M., Kauff,F., Dengjel,J.,
            Herrmann,J.M. and Riemer,J.
  TITLE     Protein import and oxidative folding in the mitochondrial
            intermembrane space of intact mammalian cells
  JOURNAL   Mol Biol Cell 24 (14), 2160-2170 (2013)
   PUBMED   23676665
REFERENCE   4  (residues 1 to 87)
  AUTHORS   Bestwick,M., Jeong,M.Y., Khalimonchuk,O., Kim,H. and Winge,D.R.
  TITLE     Analysis of Leigh syndrome mutations in the yeast SURF1 homolog
            reveals a new member of the cytochrome oxidase assembly factor
            family
  JOURNAL   Mol Cell Biol 30 (18), 4480-4491 (2010)
   PUBMED   20624914
REFERENCE   5  (residues 1 to 87)
  AUTHORS   Charpentier,A.H., Bednarek,A.K., Daniel,R.L., Hawkins,K.A.,
            Laflin,K.J., Gaddis,S., MacLeod,M.C. and Aldaz,C.M.
  TITLE     Effects of estrogen on global gene expression: identification of
            novel targets of estrogen action
  JOURNAL   Cancer Res 60 (21), 5977-5983 (2000)
   PUBMED   11085516
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP002770.3 and AK000434.1.
            
            On Apr 5, 2004 this sequence version replaced NP_057649.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.464421.1,
                                           SRR5189667.154486.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355693.5/ ENSP00000347919.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..87
                     /product="cytochrome c oxidase assembly factor 4 homolog,
                     mitochondrial"
                     /note="coiled-coil-helix-coiled-coil-helix
                     domain-containing protein 8; E2-induced gene 2 protein;
                     coiled-coil-helix-coiled-coil-helix domain containing 8"
                     /calculated_mol_wt=10003
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ1.2)"
     Region          34..44
                     /region_name="Cx9C motif 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ1.2)"
     Region          54..64
                     /region_name="Cx9C motif 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ1.2)"
     Region          68..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ1.2)"
     CDS             1..87
                     /gene="COA4"
                     /gene_synonym="CHCHD8; CMC3; E2IG2"
                     /coded_by="NM_016565.3:107..370"
                     /db_xref="CCDS:CCDS8225.1"
                     /db_xref="GeneID:51287"
                     /db_xref="HGNC:HGNC:24604"
                     /db_xref="MIM:608016"
ORIGIN      
        1 mstsvpqght wtqrvkkdde eedpldqlis rsgcaashfa vqecmaqhqd wrqcqpqvqa
       61 fkdcmseqqa rrqeelqrrq eqagahh
//
LOCUS       NP_001349111             596 aa            linear   ROD 27-APR-2025
DEFINITION  phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR14 isoform
            2 [Mus musculus].
ACCESSION   NP_001349111 XP_006506886
VERSION     NP_001349111.1
DBSOURCE    REFSEQ: accession NM_001362182.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Feng,Q., Li,X., Liu,R., Liu,G., He,Y. and Li,T.
  TITLE     Overexpression of MTMR14 induced learning and memory impairments in
            2-month-old C57 mice
  JOURNAL   Neurosci Lett 825, 137700 (2024)
   PUBMED   38401642
  REMARK    GeneRIF: Overexpression of MTMR14 induced learning and memory
            impairments in 2-month-old C57 mice.
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Kong,L.Y., Liang,C., Li,P.C., Zhang,Y.W., Feng,S.D., Zhang,D.H.,
            Yao,R., Yang,L.L., Hao,Z.Y., Zhang,H., Tian,X.X., Guo,C.R.,
            Du,B.B., Dong,J.Z. and Zhang,Y.Z.
  TITLE     Myotubularin-Related Protein14 Prevents Neointima Formation and
            Vascular Smooth Muscle Cell Proliferation by Inhibiting Polo-Like
            Kinase1
  JOURNAL   J Am Heart Assoc 11 (21), e026174 (2022)
   PUBMED   36314496
  REMARK    GeneRIF: Myotubularin-Related Protein14 Prevents Neointima
            Formation and Vascular Smooth Muscle Cell Proliferation by
            Inhibiting Polo-Like Kinase1.
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Pan,Q., Liu,Y., Wang,G., Wen,Z. and Wang,Y.
  TITLE     MTMR14 protects against cerebral stroke through suppressing
            PTEN-regulated autophagy
  JOURNAL   Biochem Biophys Res Commun 529 (4), 1045-1052 (2020)
   PUBMED   32819563
  REMARK    GeneRIF: MTMR14 protects against cerebral stroke through
            suppressing PTEN-regulated autophagy.
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Li,S., Zhang,M. and Zhang,B.
  TITLE     MTMR14 protects against hepatic ischemia-reperfusion injury through
            interacting with AKT signaling in vivo and in vitro
  JOURNAL   Biomed Pharmacother 129, 110455 (2020)
   PUBMED   32768948
  REMARK    GeneRIF: MTMR14 protects against hepatic ischemia-reperfusion
            injury through interacting with AKT signaling in vivo and in vitro.
REFERENCE   6  (residues 1 to 596)
  AUTHORS   Romero-Suarez,S., Shen,J., Brotto,L., Hall,T., Mo,C.,
            Valdivia,H.H., Andresen,J., Wacker,M., Nosek,T.M., Qu,C.K. and
            Brotto,M.
  TITLE     Muscle-specific inositide phosphatase (MIP/MTMR14) is reduced with
            age and its loss accelerates skeletal muscle aging process by
            altering calcium homeostasis
  JOURNAL   Aging (Albany NY) 2 (8), 504-513 (2010)
   PUBMED   20817957
  REMARK    GeneRIF: a knockout mice were more susceptible to exercise-induced
            muscle damage, a trademark of muscle functional changes in older
            subjects
REFERENCE   7  (residues 1 to 596)
  AUTHORS   Sansom,S.N., Griffiths,D.S., Faedo,A., Kleinjan,D.J., Ruan,Y.,
            Smith,J., van Heyningen,V., Rubenstein,J.L. and Livesey,F.J.
  TITLE     The level of the transcription factor Pax6 is essential for
            controlling the balance between neural stem cell self-renewal and
            neurogenesis
  JOURNAL   PLoS Genet 5 (6), e1000511 (2009)
   PUBMED   19521500
REFERENCE   8  (residues 1 to 596)
  AUTHORS   Shen,J., Yu,W.M., Brotto,M., Scherman,J.A., Guo,C., Stoddard,C.,
            Nosek,T.M., Valdivia,H.H. and Qu,C.K.
  TITLE     Deficiency of MIP/MTMR14 phosphatase induces a muscle disorder by
            disrupting Ca(2+) homeostasis
  JOURNAL   Nat Cell Biol 11 (6), 769-776 (2009)
   PUBMED   19465920
  REMARK    GeneRIF: Data report that mice deficient in the newly identified
            phosphatidylinositol phosphate phosphatase MIP/MTMR14
            (muscle-specific inositol phosphatase) show muscle weakness and
            fatigue.
REFERENCE   9  (residues 1 to 596)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   10 (residues 1 to 596)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC153592.3 and AC155287.6.
            
            On Apr 6, 2018 this sequence version replaced XP_006506886.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' end compared to variant 1. The resulting isoform (2)
            has the same N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.2146653.1,
                                           SRR1660811.208422.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 52.74 cM"
     Protein         1..596
                     /product="phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR14 isoform 2"
                     /EC_number="3.1.3.95"
                     /note="mJumpy; phosphatidylinositol-3-phosphate
                     phosphatase; phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR14"
                     /calculated_mol_wt=66768
     Region          127..243
                     /region_name="PH-GRAM_MTMR14"
                     /note="Myotubularian (MTM) related 14 protein (MTMR14)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13213"
                     /db_xref="CDD:275400"
     Region          <293..386
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     CDS             1..596
                     /gene="Mtmr14"
                     /gene_synonym="1110061O04Rik"
                     /coded_by="NM_001362182.1:124..1914"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:97287"
                     /db_xref="MGI:MGI:1916075"
ORIGIN      
        1 magaraaaaa sagstassgs pppqepglwe lleefsrtqy rakdsggksg skveriekrc
       61 lelfgrdycf svipnvngdi cghyprhivf leyessekek dtfqstvqvn klqdlihrsk
      121 marcrgrfvc pvilfkgkhi crsatlagwg elygrsgyny lfsggaddtw astedvteed
      181 fvlrsgdthl fdkvrgydik llqylsvkyi cdlmvenkkv kfgmnvtsse kvdkaqryan
      241 ftllsipypg ceffkeykdr dymaeglifn wkqdyvdapl nipnfltqsl nidwsqyqsw
      301 dlvqqtqnyl klllfimnrd ddsgllvhci sgwdrtplfi sllrlslwad glihtslkpa
      361 eilyltvayd wflfghmlvd rlskgeeiff fcfnflkhit seefclktqr rkslptrdag
      421 ftvedicmlr hkdrgsttsl gsdfslvleh spgavgsfsy etvelapaga ptqaawrksh
      481 ssspqsmlws rpqpseerlp shhglteaks ssssssnhsd nffrmgsspl evpkprltal
      541 sdretrlqev rsaflaayss tvglraatps psgaigglle qfargvglrg tststl
//
LOCUS       NP_001034881             115 aa            linear   PRI 27-APR-2025
DEFINITION  histidine-rich carboxyl terminus protein 1 [Homo sapiens].
ACCESSION   NP_001034881 XP_935023
VERSION     NP_001034881.1
DBSOURCE    REFSEQ: accession NM_001039792.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Hou,F., Shi,D.B., Guo,X.Y., Zhao,R.N., Zhang,H., Ma,R.R., He,J.Y.
            and Gao,P.
  TITLE     HRCT1, negatively regulated by miR-124-3p, promotes tumor
            metastasis and the growth of gastric cancer by activating the
            ERBB2-MAPK pathway
  JOURNAL   Gastric Cancer 26 (2), 250-263 (2023)
   PUBMED   36602696
  REMARK    GeneRIF: HRCT1, negatively regulated by miR-124-3p, promotes tumor
            metastasis and the growth of gastric cancer by activating the
            ERBB2-MAPK pathway.
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY358408.1.
            
            On Mar 17, 2006 this sequence version replaced XP_935023.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AY358408.1, ERR279842.1349.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354323.3/ ENSP00000346283.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..115
                     /product="histidine-rich carboxyl terminus protein 1"
                     /calculated_mol_wt=13052
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXD1.1)"
     Region          30..>87
                     /region_name="HRCT1"
                     /note="Histidine-rich carboxyl terminus protein 1;
                     pfam15758"
                     /db_xref="CDD:434913"
     Region          86..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXD1.1)"
     CDS             1..115
                     /gene="HRCT1"
                     /gene_synonym="LGLL338; PRO537; UNQ338"
                     /coded_by="NM_001039792.2:87..434"
                     /db_xref="CCDS:CCDS35012.1"
                     /db_xref="GeneID:646962"
                     /db_xref="HGNC:HGNC:33872"
ORIGIN      
        1 mlgllgstal vgwitgaava vlllllllat clfhgrqdcd vernrtaagg nrvrraqpwp
       61 frrrghlgif hhhrhpghvs hvpnvglhhh hhprhtphhl hhhhhphrhh prhar
//
LOCUS       NP_795344                447 aa            linear   PRI 27-APR-2025
DEFINITION  gastrin/cholecystokinin type B receptor isoform 1 [Homo sapiens].
ACCESSION   NP_795344 NP_000722
VERSION     NP_795344.1
DBSOURCE    REFSEQ: accession NM_176875.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Harikumar,K.G., Zhao,P., Cary,B.P., Xu,X., Desai,A.J., Dong,M.,
            Mobbs,J.I., Toufaily,C., Furness,S.G.B., Christopoulos,A.,
            Belousoff,M.J., Wootten,D., Sexton,P.M. and Miller,L.J.
  TITLE     Cholesterol-dependent dynamic changes in the conformation of the
            type 1 cholecystokinin receptor affect ligand binding and G protein
            coupling
  JOURNAL   PLoS Biol 22 (7), e3002673 (2024)
   PUBMED   39083706
  REMARK    GeneRIF: Cholesterol-dependent dynamic changes in the conformation
            of the type 1 cholecystokinin receptor affect ligand binding and G
            protein coupling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Lvovs,A., Matrov,D., Kurrikoff,T., Veidebaum,T. and Harro,J.
  TITLE     Cholecystokinin B receptor gene polymorphism (rs2941026) is
            associated with anxious personality and suicidal thoughts in a
            longitudinal study
  JOURNAL   Acta Neuropsychiatr 34 (4), 201-211 (2022)
   PUBMED   34924075
  REMARK    GeneRIF: Cholecystokinin B receptor gene polymorphism (rs2941026)
            is associated with anxious personality and suicidal thoughts in a
            longitudinal study.
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Sato,Y., Ban,S., Katayama,Y. and Mitsui,T.
  TITLE     Unique membranous gastrin receptor expression of parietal cells and
            its distribution pattern in the gastric oxyntic mucosa and fundic
            gland polyps
  JOURNAL   Hum Pathol 125, 23-34 (2022)
   PUBMED   35430166
  REMARK    GeneRIF: Unique membranous gastrin receptor expression of parietal
            cells and its distribution pattern in the gastric oxyntic mucosa
            and fundic gland polyps.
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Meng,L.L., Wang,J.L., Xu,S.P., Zu,L.D., Yan,Z.W., Zhang,J.B.,
            Han,Y.Q. and Fu,G.H.
  TITLE     Low serum gastrin associated with ER+ breast cancer development via
            inactivation of CCKBR/ERK/P65 signaling
  JOURNAL   BMC Cancer 18 (1), 824 (2018)
   PUBMED   30115027
  REMARK    GeneRIF: We concluded that low serum gastrin is related to
            increased risk of ER(+) BC development. The results also
            established that CCKBR/ERK/P65 signaling function is generally
            tumor suppressive in ER(+) BC, indicating therapies should focus on
            restoring, not inhibiting, CCKBR/ERK/P65 pathway activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Smith,J.P. and Solomon,T.E.
  TITLE     Cholecystokinin and pancreatic cancer: the chicken or the egg?
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 306 (2), G91-G101 (2014)
   PUBMED   24177032
  REMARK    Review article
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Miyake,A.
  TITLE     A truncated isoform of human CCK-B/gastrin receptor generated by
            alternative usage of a novel exon
  JOURNAL   Biochem Biophys Res Commun 208 (1), 230-237 (1995)
   PUBMED   7887934
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Ito,M., Iwata,N., Taniguchi,T., Murayama,T., Chihara,K. and
            Matsui,T.
  TITLE     Functional characterization of two cholecystokinin-B/gastrin
            receptor isoforms: a preferential splice donor site in the human
            receptor gene
  JOURNAL   Cell Growth Differ 5 (10), 1127-1135 (1994)
   PUBMED   7848914
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Herget,T., Sethi,T., Wu,S.V., Walsh,J.H. and Rozengurt,E.
  TITLE     Cholecystokinin stimulates Ca2+ mobilization and clonal growth in
            small cell lung cancer through CCKA and CCKB/gastrin receptors
  JOURNAL   Ann N Y Acad Sci 713, 283-297 (1994)
   PUBMED   8185170
  REMARK    Review article
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Lee,Y.M., Beinborn,M., McBride,E.W., Lu,M., Kolakowski,L.F. Jr. and
            Kopin,A.S.
  TITLE     The human brain cholecystokinin-B/gastrin receptor. Cloning and
            characterization
  JOURNAL   J Biol Chem 268 (11), 8164-8169 (1993)
   PUBMED   7681836
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Pisegna,J.R., de Weerth,A., Huppi,K. and Wank,S.A.
  TITLE     Molecular cloning of the human brain and gastric cholecystokinin
            receptor: structure, functional expression and chromosomal
            localization
  JOURNAL   Biochem Biophys Res Commun 189 (1), 296-303 (1992)
   PUBMED   1280419
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022762.8 and AC068733.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 31, 2003 this sequence version replaced NP_000722.2.
            
            Summary: This gene encodes a G-protein coupled receptor for gastrin
            and cholecystokinin (CCK), regulatory peptides of the brain and
            gastrointestinal tract. This protein is a type B gastrin receptor,
            which has a high affinity for both sulfated and nonsulfated CCK
            analogs and is found principally in the central nervous system and
            the gastrointestinal tract. Alternative splicing results in
            multiple transcript variants. A misspliced transcript variant
            including an intron has been observed in cells from colorectal and
            pancreatic tumors. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.274990.1,
                                           SRR3476690.982740.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334619.7/ ENSP00000335544.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..447
                     /product="gastrin/cholecystokinin type B receptor isoform
                     1"
                     /note="gastrin receptor; CCK2 receptor; CCK-B receptor;
                     cholecystokinin-2 receptor; cholecystokinin type 2
                     receptor"
                     /calculated_mol_wt=48288
     Site            7
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32239.1)"
     Site            30
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32239.1)"
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32239.1)"
     Region          55..401
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          57..81
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320645"
     Site            58..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32239.1)"
     Site            88..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32239.1)"
     Region          90..112
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320645"
     Region          128..150
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320645"
     Site            132..150
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32239.1)"
     Site            171..189
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32239.1)"
     Region          173..189
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320645"
     Region          216..239
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320645"
     Site            220..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32239.1)"
     Region          258..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32239.1)"
     Region          332..354
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320645"
     Site            334..355
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32239.1)"
     Region          369..394
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320645"
     Site            374..394
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32239.1)"
     CDS             1..447
                     /gene="CCKBR"
                     /gene_synonym="CCK-2R; CCK-B; CCK2R; GASR"
                     /coded_by="NM_176875.4:92..1435"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7761.1"
                     /db_xref="GeneID:887"
                     /db_xref="HGNC:HGNC:1571"
                     /db_xref="MIM:118445"
ORIGIN      
        1 mellklnrsv qgtgpgpgas lcrpgaplln sssvgnlsce pprirgagtr elelairitl
       61 yaviflmsvg gnmliivvlg lsrrlrtvtn afllslavsd lllavacmpf tllpnlmgtf
      121 ifgtvickav sylmgvsvsv stlslvaial erysaicrpl qarvwqtrsh aarvivatwl
      181 lsgllmvpyp vytvvqpvgp rvlqcvhrwp sarvrqtwsv llllllffip gvvmavaygl
      241 isrelylglr fdgdsdsdsq srvrnqgglp gavhqngrcr petgavgeds dgcyvqlprs
      301 rpaleltalt apgpgsgsrp tqakllakkr vvrmllvivv lfflcwlpvy santwrafdg
      361 pgahralsga pisfihllsy asacvnplvy cfmhrrfrqa cletcarccp rpprarpral
      421 pdedpptpsi aslsrlsytt istlgpg
//
LOCUS       NP_064539                242 aa            linear   PRI 27-APR-2025
DEFINITION  endoplasmic reticulum membrane protein complex subunit 7 precursor
            [Homo sapiens].
ACCESSION   NP_064539
VERSION     NP_064539.1
DBSOURCE    REFSEQ: accession NM_020154.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Pleiner,T., Tomaleri,G.P., Januszyk,K., Inglis,A.J., Hazu,M. and
            Voorhees,R.M.
  TITLE     Structural basis for membrane insertion by the human ER membrane
            protein complex
  JOURNAL   Science 369 (6502), 433-436 (2020)
   PUBMED   32439656
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Bagchi,P., Torres,M., Qi,L. and Tsai,B.
  TITLE     Selective EMC subunits act as molecular tethers of intracellular
            organelles exploited during viral entry
  JOURNAL   Nat Commun 11 (1), 1127 (2020)
   PUBMED   32111841
  REMARK    GeneRIF: ER membrane protein complex subunit 4 (EMC4) and EMC7
            support SV40 infection by promoting from the late endosome (LE) to
            the endoplasmic reticulum (ER) targeting of the virus. They do this
            by engaging LE-associated Rab7, to stabilize contact between the LE
            and ER. These EMC subunits also bind to the ER-resident fusion
            machinery component syntaxin18, which is required for SV40-arrival
            to the ER.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Petko,J., Thileepan,M., Sargen,M., Canfield,V. and Levenson,R.
  TITLE     Alternative splicing of the Wnt trafficking protein, Wntless and
            its effects on protein-protein interactions
  JOURNAL   BMC Mol Cell Biol 20 (1), 22 (2019)
   PUBMED   31286866
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Christianson,J.C., Olzmann,J.A., Shaler,T.A., Sowa,M.E.,
            Bennett,E.J., Richter,C.M., Tyler,R.E., Greenblatt,E.J.,
            Harper,J.W. and Kopito,R.R.
  TITLE     Defining human ERAD networks through an integrative mapping
            strategy
  JOURNAL   Nat Cell Biol 14 (1), 93-105 (2011)
   PUBMED   22119785
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Domal-Kwiatkowska,D., Glanowska,G., Smolik,S., Wilczewski,P.,
            Mazurek,U., Nowalany-Kozielska,E., Fudal,M. and Wodniecki,J.
  TITLE     [Familial hypertrophic cardiomyopathy--a case report]
  JOURNAL   Kardiol Pol 64 (11), 1287-1291 (2006)
   PUBMED   17165166
  REMARK    GeneRIF: Candidate modifier gene on the phenotypic expression of
            hypertrophy in patients with hyperthophic cardiomyopathy.
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 242)
  AUTHORS   O'Brien,K.P., Tapia-Paez,I., Stahle-Backdahl,M., Kedra,D. and
            Dumanski,J.P.
  TITLE     Characterization of five novel human genes in the 11q13-q22 region
  JOURNAL   Biochem Biophys Res Commun 273 (1), 90-94 (2000)
   PUBMED   10873569
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079203.9, AJ245874.1, BC012456.1 and AC069045.11.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358445.1, SRR5189655.179690.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256545.9/ ENSP00000256545.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..242
                     /product="endoplasmic reticulum membrane protein complex
                     subunit 7 precursor"
                     /note="chromosome 15 hypothetical ATG/GTP binding protein;
                     UPF0480 protein C15orf24; endoplasmic reticulum membrane
                     protein complex subunit 7"
                     /calculated_mol_wt=24027
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2462
     mat_peptide     24..242
                     /product="Endoplasmic reticulum membrane protein complex
                     subunit 7. /id=PRO_0000240860"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPA0.1)"
                     /calculated_mol_wt=24027
     Region          57..168
                     /region_name="EMC7_beta-sandw"
                     /note="ER membrane protein complex subunit 7,
                     beta-sandwich domain; pfam09430"
                     /db_xref="CDD:430607"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPA0.1)"
     Region          217..242
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPA0.1)"
     CDS             1..242
                     /gene="EMC7"
                     /gene_synonym="C11orf3; C15orf24; HT022; ORF1-FL1"
                     /coded_by="NM_020154.3:24..752"
                     /db_xref="CCDS:CCDS10032.1"
                     /db_xref="GeneID:56851"
                     /db_xref="HGNC:HGNC:24301"
                     /db_xref="MIM:620631"
ORIGIN      
        1 maaalwgffp vllllllsgd vqssevpgaa aegsggsgvg igdrfkiegr avvpgvkpqd
       61 wisaarvlvd geehvgflkt dgsfvvhdip sgsyvvevvs payrfdpvrv ditskgkmra
      121 ryvnyiktse vvrlpyplqm kssgppsyfi kreswgwtdf lmnpmvmmmv lpllifvllp
      181 kvvntsdpdm rremeqsmnm lnsnhelpdv sefmtrlfss kssgksssgs sktgksgagk
      241 rr
//
LOCUS       NP_001353133             871 aa            linear   PRI 27-APR-2025
DEFINITION  disks large homolog 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001353133 XP_016861306
VERSION     NP_001353133.1
DBSOURCE    REFSEQ: accession NM_001366204.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Veljacic Viskovic,D., Lozic,M., Vukoja,M., Soljic,V., Vukojevic,K.,
            Glavina Durdov,M., Filipovic,N. and Lozic,B.
  TITLE     Spatio-Temporal Expression Pattern of CAKUT Candidate Genes DLG1
            and KIF12 during Human Kidney Development
  JOURNAL   Biomolecules 13 (2), 340 (2023)
   PUBMED   36830709
  REMARK    GeneRIF: Spatio-Temporal Expression Pattern of CAKUT Candidate
            Genes DLG1 and KIF12 during Human Kidney Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 871)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861306.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.75522.1,
                                           SRR1803613.6201.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..871
                     /product="disks large homolog 1 isoform 8"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=96945
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          680..858
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..871
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366204.1:109..2724"
                     /note="isoform 8 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS93452.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt snasdsessy
      661 rgqeeyvlsy epvnqqevny trpviilgpm kdrinddlis efpdkfgscv phttrpkrdy
      721 evdgrdyhfv tsreqmekdi qehkfieagq ynnhlygtsv qsvrevaekg khcildvsgn
      781 aikrlqiaql ypisifikpk smenimemnk rlteeqarkt feramkleqe ftehftaivq
      841 gdtlediynq vkqiieeqsg syiwvpakek l
//
LOCUS       NP_663695                 97 aa            linear   PRI 27-APR-2025
DEFINITION  sperm protein associated with the nucleus on the X chromosome A
            [Homo sapiens].
ACCESSION   NP_663695 XP_001128442
VERSION     NP_663695.1
DBSOURCE    REFSEQ: accession NM_145662.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Li,J., Bo,H., Zhu,F., Li,Q., Chen,T., Lei,S. and Fan,L.
  TITLE     Hypomethylated SPANXA1/A2 promotes the metastasis of head and neck
            squamous cell carcinoma
  JOURNAL   Med Oncol 37 (12), 112 (2020)
   PUBMED   33175201
  REMARK    GeneRIF: Hypomethylated SPANXA1/A2 promotes the metastasis of head
            and neck squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 97)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Hansen,S., Eichler,E.E., Fullerton,S.M. and Carrell,D.
  TITLE     SPANX gene variation in fertile and infertile males
  JOURNAL   Syst Biol Reprod Med 55, 18-26 (2010)
   PUBMED   20073942
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Westbrook,V.A., Schoppee,P.D., Vanage,G.R., Klotz,K.L.,
            Diekman,A.B., Flickinger,C.J., Coppola,M.A. and Herr,J.C.
  TITLE     Hominoid-specific SPANXA/D genes demonstrate differential
            expression in individuals and protein localization to a distinct
            nuclear envelope domain during spermatid morphogenesis
  JOURNAL   Mol Hum Reprod 12 (11), 703-716 (2006)
   PUBMED   17012309
REFERENCE   6  (residues 1 to 97)
  AUTHORS   Kouprina,N., Mullokandov,M., Rogozin,I.B., Collins,N.K.,
            Solomon,G., Otstot,J., Risinger,J.I., Koonin,E.V., Barrett,J.C. and
            Larionov,V.
  TITLE     The SPANX gene family of cancer/testis-specific antigens: rapid
            evolution and amplification in African great apes and hominids
  JOURNAL   Proc Natl Acad Sci U S A 101 (9), 3077-3082 (2004)
   PUBMED   14973187
REFERENCE   7  (residues 1 to 97)
  AUTHORS   Westbrook,V.A., Schoppee,P.D., Diekman,A.B., Klotz,K.L.,
            Allietta,M., Hogan,K.T., Slingluff,C.L., Patterson,J.W.,
            Frierson,H.F., Irvin,W.P. Jr., Flickinger,C.J., Coppola,M.A. and
            Herr,J.C.
  TITLE     Genomic organization, incidence, and localization of the SPAN-x
            family of cancer-testis antigens in melanoma tumors and cell lines
  JOURNAL   Clin Cancer Res 10 (1 Pt 1), 101-112 (2004)
   PUBMED   14734458
REFERENCE   8  (residues 1 to 97)
  AUTHORS   Zendman,A.J., Zschocke,J., van Kraats,A.A., de Wit,N.J.,
            Kurpisz,M., Weidle,U.H., Ruiter,D.J., Weiss,E.H. and van
            Muijen,G.N.
  TITLE     The human SPANX multigene family: genomic organization, alignment
            and expression in male germ cells and tumor cell lines
  JOURNAL   Gene 309 (2), 125-133 (2003)
   PUBMED   12758128
REFERENCE   9  (residues 1 to 97)
  AUTHORS   Westbrook,V.A., Diekman,A.B., Naaby-Hansen,S., Coonrod,S.A.,
            Klotz,K.L., Thomas,T.S., Norton,E.J., Flickinger,C.J. and Herr,J.C.
  TITLE     Differential nuclear localization of the cancer/testis-associated
            protein, SPAN-X/CTp11, in transfected cells and in 50% of human
            spermatozoa
  JOURNAL   Biol Reprod 64 (1), 345-358 (2001)
   PUBMED   11133693
REFERENCE   10 (residues 1 to 97)
  AUTHORS   Westbrook,V.A., Diekman,A.B., Klotz,K.L., Khole,V.V., von
            Kap-Herr,C., Golden,W.L., Eddy,R.L., Shows,T.B., Stoler,M.H.,
            Lee,C.Y., Flickinger,C.J. and Herr,J.C.
  TITLE     Spermatid-specific expression of the novel X-linked gene product
            SPAN-X localized to the nucleus of human spermatozoa
  JOURNAL   Biol Reprod 63 (2), 469-481 (2000)
   PUBMED   10906052
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB110020.1.
            
            On Dec 2, 2006 this sequence version replaced XP_001128442.1.
            
            Summary: Temporally regulated transcription and translation of
            several testis-specific genes is required to initiate the series of
            molecular and morphological changes in the male germ cell lineage
            necessary for the formation of mature spermatozoa. This gene is a
            member of the SPANX family of cancer/testis-associated genes, which
            are located in a cluster on chromosome X. The SPANX genes encode
            differentially expressed testis-specific proteins that localize to
            various subcellular compartments. This particular gene maps to
            chromosome X in a head-to-head orientation with SPANX family member
            A1 and appears to be a duplication of that locus. The protein
            encoded by this gene targets to the nucleus where it associates
            with nuclear vacuoles and the redundant nuclear envelope. Based on
            its association with these poorly characterized regions of the
            sperm nucleus, this protein provides a biochemical marker to study
            unique structures in spermatazoa while attempting to further define
            its role in spermatogenesis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB113891.1, CB122914.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370518.4/ ENSP00000359549.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq27.2"
     Protein         1..97
                     /product="sperm protein associated with the nucleus on the
                     X chromosome A"
                     /note="sperm protein associated with the nucleus, X
                     chromosome, family member A2; nuclear-associated protein
                     SPAN-Xa; SPANX family member A; cancer/testis antigen
                     11.1; Sperm protein associated with the nucleus on the X
                     chromosome C; Cancer/testis antigen 11.3;
                     Cancer/testis-associated protein CTp11; Nuclear-associated
                     protein SPAN-Xc"
                     /calculated_mol_wt=10907
     Region          1..81
                     /region_name="SPAN-X"
                     /note="Sperm protein associated with nucleus, mapped to X
                     chromosome; pfam07458"
                     /db_xref="CDD:400025"
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NS26.1)"
     Region          37..45
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NS26.1)"
     CDS             1..97
                     /gene="SPANXA2"
                     /gene_synonym="CT11.1; CT11.3; SPANX; SPANX-A; SPANX-C;
                     SPANXA; SPANXC"
                     /coded_by="NM_145662.4:61..354"
                     /db_xref="CCDS:CCDS44007.1"
                     /db_xref="GeneID:728712"
                     /db_xref="HGNC:HGNC:14328"
                     /db_xref="MIM:300493"
ORIGIN      
        1 mdkqssaggv krsvpcdsne anemmpetpt gdsdpqpapk kmktsessti lvvryrrnfk
       61 rtspeellnd harenrinpl qmeeeefmei mveipak
//
LOCUS       NP_001350919             478 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit alpha
            isoform 2 [Homo sapiens].
ACCESSION   NP_001350919
VERSION     NP_001350919.1
DBSOURCE    REFSEQ: accession NM_001363990.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Lin,J., Xia,H., Yu,J., Wang,Y., Wang,H., Xie,D., Cheng,C., Lu,L.,
            Bian,T., Wu,Y. and Liu,Q.
  TITLE     circADAMTS6 via stabilizing CAMK2A is involved in smoking-induced
            emphysema through driving M2 macrophage polarization
  JOURNAL   Environ Int 190, 108832 (2024)
   PUBMED   38936066
  REMARK    GeneRIF: circADAMTS6 via stabilizing CAMK2A is involved in
            smoking-induced emphysema through driving M2 macrophage
            polarization.
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Zhang,Y., Xia,M., Zhao,T., Zhang,Q., Li,R. and Yang,L.
  TITLE     Camk2a suppresses denervated muscle atrophy by maintaining the Ca2+
            homeostasis in muscle cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (11), 25-29 (2023)
   PUBMED   38015546
  REMARK    GeneRIF: Camk2a suppresses denervated muscle atrophy by maintaining
            the Ca2+ homeostasis in muscle cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Alphonse,N., Wanford,J.J., Voak,A.A., Gay,J., Venkhaya,S.,
            Burroughs,O., Mathew,S., Lee,T., Evans,S.L., Zhao,W., Frowde,K.,
            Alrehaili,A., Dickenson,R.E., Munk,M., Panina,S., Mahmood,I.F.,
            Llorian,M., Stanifer,M.L., Boulant,S., Berchtold,M.W.,
            Bergeron,J.R.C., Wack,A., Lesser,C.F. and Odendall,C.
  TITLE     A family of conserved bacterial virulence factors dampens
            interferon responses by blocking calcium signaling
  JOURNAL   Cell 185 (13), 2354-2369 (2022)
   PUBMED   35568036
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Zheng,J., Zhang,Y.W. and Pan,Z.F.
  TITLE     [Dysregulation of MAD2L1/CAMK2A/PTTG1 Gene Cluster Maintains the
            Stemness Characteristics of Uterine Corpus Endometrial Carcinoma]
  JOURNAL   Zhongguo Yi Xue Ke Xue Yuan Xue Bao 43 (5), 685-695 (2021)
   PUBMED   34728029
  REMARK    GeneRIF: [Dysregulation of MAD2L1/CAMK2A/PTTG1 Gene Cluster
            Maintains the Stemness Characteristics of Uterine Corpus
            Endometrial Carcinoma].
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Bredt,D.S., Ferris,C.D. and Snyder,S.H.
  TITLE     Nitric oxide synthase regulatory sites. Phosphorylation by cyclic
            AMP-dependent protein kinase, protein kinase C, and
            calcium/calmodulin protein kinase; identification of flavin and
            calmodulin binding sites
  JOURNAL   J Biol Chem 267 (16), 10976-10981 (1992)
   PUBMED   1375933
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Omary,M.B., Baxter,G.T., Chou,C.F., Riopel,C.L., Lin,W.Y. and
            Strulovici,B.
  TITLE     PKC epsilon-related kinase associates with and phosphorylates
            cytokeratin 8 and 18
  JOURNAL   J Cell Biol 117 (3), 583-593 (1992)
   PUBMED   1374067
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Wegner,M., Cao,Z. and Rosenfeld,M.G.
  TITLE     Calcium-regulated phosphorylation within the leucine zipper of
            C/EBP beta
  JOURNAL   Science 256 (5055), 370-373 (1992)
   PUBMED   1314426
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Tokui,T., Yamauchi,T., Yano,T., Nishi,Y., Kusagawa,M., Yatani,R.
            and Inagaki,M.
  TITLE     Ca2(+)-calmodulin-dependent protein kinase II phosphorylates
            various types of non-epithelial intermediate filament proteins
  JOURNAL   Biochem Biophys Res Commun 169 (3), 896-904 (1990)
   PUBMED   2114109
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011372.7.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinases family, and to the Ca(2+)/calmodulin-dependent
            protein kinases subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. This calcium
            calmodulin-dependent protein kinase is composed of four different
            chains: alpha, beta, gamma, and delta. The alpha chain encoded by
            this gene is required for hippocampal long-term potentiation (LTP)
            and spatial learning. In addition to its calcium-calmodulin
            (CaM)-dependent activity, this protein can undergo
            autophosphorylation, resulting in CaM-independent activity. Several
            transcript variants encoding distinct isoforms have been identified
            for this gene. [provided by RefSeq, Jun 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.185252.1,
                                           SRR1660803.209488.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..478
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit alpha isoform 2"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II alpha; CaM-kinase II alpha chain;
                     calcium/calmodulin-dependent protein kinase II alpha-B
                     subunit; CaM kinase II alpha subunit; CaMK-II alpha
                     subunit; calcium/calmodulin-dependent protein kinase type
                     II alpha chain; calcium/calmodulin-dependent protein
                     kinase type II subunit alpha; caMK-II subunit alpha; caM
                     kinase II subunit alpha"
                     /calculated_mol_wt=53957
     Region          11..302
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            order(19..23,27,40,42,73,89..92,96,98,134..135,137,
                     139..140,142,155..156,159,174..178,180)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(19..22,27,40,42,73,89..92,96,139..140,142,155..156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(23,96,98,134..135,137,139,159,174..178,180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(155..165,168..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11275; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P11275; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Region          290..300
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            order(293,295..302)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          310..320
                     /region_name="Interaction with BAALC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Region          314..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Region          346..473
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     CDS             1..478
                     /gene="CAMK2A"
                     /gene_synonym="CAMKA; CaMKIIalpha; CaMKIINalpha; MRD53;
                     MRT63"
                     /coded_by="NM_001363990.1:335..1771"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS43386.1"
                     /db_xref="GeneID:815"
                     /db_xref="HGNC:HGNC:1460"
                     /db_xref="MIM:114078"
ORIGIN      
        1 matitctrft eeyqlfeelg kgafsvvrrc vkvlagqeya akiintkkls ardhqklere
       61 aricrllkhp nivrlhdsis eeghhylifd lvtggelfed ivareyysea dashciqqil
      121 eavlhchqmg vvhrdlkpen lllasklkga avkladfgla ievegeqqaw fgfagtpgyl
      181 spevlrkdpy gkpvdlwacg vilyillvgy ppfwdedqhr lyqqikagay dfpspewdtv
      241 tpeakdlink mltinpskri taaealkhpw ishrstvasc mhrqetvdcl kkfnarrklk
      301 gailttmlat rnfsggksgg nkksdgvkes sestnttied edtkvrkqei ikvteqliea
      361 isngdfesyt kmcdpgmtaf epealgnlve gldfhrfyfe nlwsrnskpv httilnphih
      421 lmgdesacia yiritqylda ggiprtaqse etrvwhrrdg kwqivhfhrs gapsvlph
//
LOCUS       NP_001129690             253 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 51 isoform 1 [Homo sapiens].
ACCESSION   NP_001129690
VERSION     NP_001129690.1
DBSOURCE    REFSEQ: accession NM_001136218.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Christians,A., Poisel,E., Hartmann,C., von Deimling,A. and Pusch,S.
  TITLE     Characterization of the epithelial membrane protein 3 interaction
            network reveals a potential functional link to mitogenic signal
            transduction regulation
  JOURNAL   Int J Cancer 145 (2), 461-473 (2019)
   PUBMED   30614533
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL035405.13 and AL391094.12.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1 through 4 encode the same isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.216846.1,
                                           SRR3476690.685660.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376008.3/ ENSP00000365176.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.21"
     Protein         1..253
                     /product="transmembrane protein 51 isoform 1"
                     /calculated_mol_wt=27628
     Region          7..240
                     /region_name="TMEM51"
                     /note="Transmembrane protein 51; pfam15345"
                     /db_xref="CDD:464663"
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW97.1)"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW97.1)"
     Region          93..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW97.1)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NW97.1)"
     Region          164..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW97.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NW97.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NW97.1)"
     CDS             1..253
                     /gene="TMEM51"
                     /gene_synonym="C1orf72"
                     /coded_by="NM_001136218.2:475..1236"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS154.1"
                     /db_xref="GeneID:55092"
                     /db_xref="HGNC:HGNC:25488"
ORIGIN      
        1 mmaqskangs hyaltaiglg mlvlgvimam wnlvpgfsaa ekptaqgsnk tevgggilks
       61 ktfsvayvlv gagvmlllls iclsirdkrk qrqgedlahv qhptgagpha qeedsqeeee
      121 edeeaasryy vpsyeevmnt nyseargeeq nprlsislps yesltgldet tptstradve
      181 aspgnppdrq nsklakrlkp lkvrriksek lhlkdfrinl pdknvpppsi epltpppqyd
      241 evqekapdtr ppd
//
LOCUS       NP_001068593             951 aa            linear   MAM 27-APR-2025
DEFINITION  AP-2 complex subunit beta [Bos taurus].
ACCESSION   NP_001068593 XP_591504 XP_871962 XP_883909 XP_883942 XP_883971
            XP_883998 XP_884026 XP_884079 XP_884105 XP_884141 XP_884174
            XP_884200 XP_884228 XP_884257 XP_884278
VERSION     NP_001068593.1
DBSOURCE    REFSEQ: accession NM_001075125.2
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Ponnambalam,S., Robinson,M.S., Jackson,A.P., Peiperl,L. and
            Parham,P.
  TITLE     Conservation and diversity in families of coated vesicle adaptins
  JOURNAL   J Biol Chem 265 (9), 4814-4820 (1990)
   PUBMED   1969413
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC123583.1.
            
            On or before Oct 4, 2006 this sequence version replaced
            XP_883909.1, XP_883942.1, XP_883971.1, XP_883998.1, XP_884026.1,
            XP_591504.2, XP_884079.1, XP_884105.1, XP_884141.1, XP_884174.1,
            XP_884200.1, XP_884228.1, XP_884257.1, XP_884278.1, XP_871962.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC123583.1, SRR5721697.5838.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA6648753,
                                           SAMEA6648754 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="19"
                     /map="19"
                     /breed="Hereford"
     Protein         1..951
                     /product="AP-2 complex subunit beta"
                     /note="clathrin-associated / assembly / adaptor protein,
                     large, beta 1; AP-1 complex subunit beta-1; AP105B;
                     beta1-adaptin; beta2-adaptin; beta-adaptin 1; adaptor
                     protein complex AP-2 subunit beta; golgi adaptor HA1/AP1
                     adaptin beta subunit; adaptor protein complex AP-1 subunit
                     beta-1; adapter-related protein complex 2 subunit beta;
                     adaptor-related protein complex 2 subunit beta;
                     adaptor-related protein complex 1 subunit beta-1;
                     adapter-related protein complex 2 beta subunit;
                     adapter-related protein complex 1 subunit beta-1; clathrin
                     assembly protein complex 1 beta large chain; clathrin
                     assembly protein complex 2 beta large chain; plasma
                     membrane adaptor HA2/AP2 adaptin beta subunit;
                     beta-1-adaptin; beta-2-adaptin; adaptor-related protein
                     complex 2, beta 1 subunit"
                     /calculated_mol_wt=105575
     Region          11..534
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          51..75
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(67..68,71,74..75,104..105,108,111..112,139..140,143,
                     146..147,150,178..179,182,185..186,220..221,224,227..228)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          87..114
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          121..151
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          160..186
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          197..228
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q10567; propagated from
                     UniProtKB/Swiss-Prot (Q08DS7.1)"
     Region          392..416
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          428..457
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          464..494
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          505..541
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          731..831
                     /region_name="Alpha_adaptinC2"
                     /note="Adaptin C-terminal domain; smart00809"
                     /db_xref="CDD:197886"
     Region          840..950
                     /region_name="B2-adapt-app_C"
                     /note="Beta2-adaptin appendage, C-terminal sub-domain;
                     smart01020"
                     /db_xref="CDD:198088"
     CDS             1..951
                     /gene="AP2B1"
                     /gene_synonym="CLAPB1"
                     /coded_by="NM_001075125.2:120..2975"
                     /db_xref="BGD:BT11432"
                     /db_xref="GeneID:282183"
                     /db_xref="VGNC:VGNC:55033"
ORIGIN      
        1 mtdskyfttn kkgeifelka elnnekkekr keavkkviaa mtvgkdvssl fpdvvncmqt
       61 dnlelkklvy lylmnyaksq pdmaimavns fvkdcedpnp liralavrtm gcirvdkite
      121 ylceplrkcl kdedpyvrkt aavcvaklhd inaqmvedqg fldslrdlia dsnpmvvana
      181 vaalseises hpnsnlldln pqninkllta lnectewgqi fildclsnyn pkddreaqsi
      241 cervtprlsh ansavvlsav kvlmkflell pkesdyynml lkklapplvt llsgepevqy
      301 valrninliv qkrpeilkqe ikvffvkynd piyvklekld imirlasqan iaqvlaelke
      361 yatevdvdfv rkavraigrc aikveqsaer cvstlldliq tkvnyvvqea ivvirdifrk
      421 ypnkyesiia tlcenldsld epdaraamiw ivgeyaerid nadellesfl egfhdestqv
      481 qltlltaivk lflkkpsetq elvqqvlsla tqdsdnpdlr drgyiywrll stdpvtakev
      541 vlsekplise etdlieptll delichigsl asvyhkppna fvegshgihr khlpihhgst
      601 dagdspvgtt tatnleqpqv ipsqgdllgd llnldlgppv nvpqvssmqm gavdllgggl
      661 dsllgsdlgg giggspavgq sfipssvpat fapsptpavv ssglndlfel stgigmapgg
      721 yvapkavwlp avkakgleis gtfthrqghi ymemnftnka lqhmtdfaiq fnknsfgvip
      781 stplaihtpl mpnqsidvsl plntlgpvmk meplnnlqva vknnidvfyf scliplnvlf
      841 vedgkmerqv flatwkdipn enelqfqike chlnadtvss klqnnnvyti akrnvegqdm
      901 lyqslkltng iwilaelriq pgnpnytlsl kcrapevsqy iyqvydsilk n
//
LOCUS       NP_113649                500 aa            linear   PRI 27-APR-2025
DEFINITION  cysteine-rich secretory protein LCCL domain-containing 1 isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_113649
VERSION     NP_113649.1
DBSOURCE    REFSEQ: accession NM_031461.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Khadjeh,S., Hindmarsh,V., Weber,F., Cyganek,L., Vidal,R.O.,
            Torkieh,S., Streckfuss-Bomeke,K., Lbik,D., Tiburcy,M.,
            Mohamed,B.A., Bonn,S., Toischer,K. and Hasenfuss,G.
  TITLE     CRISPLD1: a novel conserved target in the transition to human heart
            failure
  JOURNAL   Basic Res Cardiol 115 (3), 27 (2020)
   PUBMED   32146539
  REMARK    GeneRIF: CRISPLD1: a novel conserved target in the transition to
            human heart failure; findings provide new pathophysiological data
            on Ca(2+) regulation in the transition to failure and novel
            candidate genes with promising potential for therapeutic
            interventions
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Chiquet,B.T., Henry,R., Burt,A., Mulliken,J.B., Stal,S.,
            Blanton,S.H. and Hecht,J.T.
  TITLE     Nonsyndromic cleft lip and palate: CRISPLD genes and the folate
            gene pathway connection
  JOURNAL   Birth Defects Res A Clin Mol Teratol 91 (1), 44-49 (2011)
   PUBMED   21254358
  REMARK    GeneRIF: These novel findings suggest that CRISPLD1 plays a role in
            Nonsyndromic cleft lip and palate (NSCLP) through the interaction
            with CRISPLD2 and folate pathway genes.
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP357192.1, BC020514.1, AC100782.2 and BU790187.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL834301.1, SRR1660805.247975.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262207.9/ ENSP00000262207.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.13"
     Protein         1..500
                     /product="cysteine-rich secretory protein LCCL
                     domain-containing 1 isoform 1 precursor"
                     /note="CocoaCrisp; trypsin inhibitor Hl; cysteine-rich
                     secretory protein 10; LCCL domain-containing cysteine-rich
                     secretory protein 1"
                     /calculated_mol_wt=54242
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H336.1)"
                     /calculated_mol_wt=2665
     mat_peptide     24..500
                     /product="Cysteine-rich secretory protein LCCL
                     domain-containing 1. /id=PRO_0000248146"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H336.1)"
                     /calculated_mol_wt=54242
     Region          62..207
                     /region_name="CAP_CRISPLD1"
                     /note="CAP (cysteine-rich secretory proteins, antigen 5,
                     and pathogenesis-related 1 proteins) domain of
                     cysteine-rich secretory protein LCCL domain-containing 1;
                     cd18813"
                     /db_xref="CDD:349407"
     Region          254..281
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H336.1)"
     Region          291..375
                     /region_name="LCCL"
                     /note="LCCL domain; smart00603"
                     /db_xref="CDD:128866"
     Region          394..491
                     /region_name="LCCL"
                     /note="LCCL domain; pfam03815"
                     /db_xref="CDD:427521"
     CDS             1..500
                     /gene="CRISPLD1"
                     /gene_synonym="CRISP-10; CRISP10; LCRISP1"
                     /coded_by="NM_031461.6:479..1981"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS6219.1"
                     /db_xref="GeneID:83690"
                     /db_xref="HGNC:HGNC:18206"
ORIGIN      
        1 mkctarewlr vttvlfmara ipamvvpnat llekllekym dedgewwiak qrgkraitdn
       61 dmqsildlhn klrsqvypta snmeymtwdv elersaeswa esclwehgpa sllpsigqnl
      121 gahwgryrpp tfhvqswyde vkdfsypyeh ecnpycpfrc sgpvcthytq vvwatsnrig
      181 cainlchnmn iwgqiwpkav ylvcnyspkg nwwghapykh grpcsacpps fgggcrenlc
      241 ykegsdryyp preeetneie rqqsqvhdth vrtrsddssr nevisaqqms qivscevrlr
      301 dqckgttcnr yecpagclds kakvigsvhy emqssicraa ihygiidndg gwvditrqgr
      361 khyfiksnrn giqtigkyqs ansftvskvt vqavtcettv eqlcpfhkpa shcprvycpr
      421 ncmqanphya rvigtrvysd lssicraavh agvvrnhggy vdvmpvdkrk tyiasfqngi
      481 fseslqnppg gkafrvfavv
//
LOCUS       NP_001004301             617 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 813 [Homo sapiens].
ACCESSION   NP_001004301 XP_064903
VERSION     NP_001004301.2
DBSOURCE    REFSEQ: accession NM_001004301.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC022137.6, DB066632.1, DB235327.1 and AK131422.1.
            
            On Jun 12, 2006 this sequence version replaced NP_001004301.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1512369.1,
                                           SRR1803613.239872.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396403.9/ ENSP00000379684.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..617
                     /product="zinc finger protein 813"
                     /calculated_mol_wt=71590
     Region          7..48
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          241..617
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..321
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(306,308,310,312..313,316..317,320,334,336,340..341,
                     344..345,348,362,364,366,368..369,372..373,376)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          329..349
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(329,332,345,349)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          385..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          525..545
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(530,532,534,536..537,540..541,544,558,560,564..565,
                     568..569,572,586,588,590,592..593,596..597,600)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          553..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(553,556,569,573)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          581..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..617
                     /gene="ZNF813"
                     /coded_by="NM_001004301.4:131..1984"
                     /db_xref="CCDS:CCDS46172.1"
                     /db_xref="GeneID:126017"
                     /db_xref="HGNC:HGNC:33257"
ORIGIN      
        1 malpqglltf rdvaiefsqe ewkcldpaqr tlyrdvmlen yrnlvsldis skcmmkefss
       61 taqgnrevih tgtlqrhesh htgdfrfqei dkdihnlefq wqedernshe apmteikklt
      121 gsadrydqrh agnkpikdql gssfhshlpe lhmfqtqgki gnqveksind assistsqri
      181 scrpkthisn nygnnfrnss lltqkqevhm reksfqcnes gkafnyssll rkhqiihlge
      241 kqykcdvcgk vfnrkrnlvc hrrchtgekp yrcnecgktf sqtysltchr rlhtgekpyk
      301 ceecdkafsf ksnlkrhrri hagekpykcn ecgktfsqts sltchrrlht gekpfkcnec
      361 gktfsrkssl tchhrlhtge kpykcnecgk tfsqeltlkc hrrlhtgekp ykcnecgkvf
      421 nkkanlarhh rlhsgekpyk ctecvktfsr nsalvihkai higekrykcn ecgktfsris
      481 alvihtaiht gekpykcnec gkgfnrkthl achhrlhtge kpykcnecgk vfnrkthlah
      541 hhrlhtgdkp ykcnecgkvf nqkahlarhh rlhtgekpyk cnecgkvfnq kanlarhhrl
      601 htgekpykfn ecgkafn
//
LOCUS       NP_001355665            1029 aa            linear   ROD 27-APR-2025
DEFINITION  protein phosphatase 1 regulatory subunit 12A isoform 1 [Mus
            musculus].
ACCESSION   NP_001355665 XP_006513389
VERSION     NP_001355665.1
DBSOURCE    REFSEQ: accession NM_001368736.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Wang,Y., Jiang,Z.H., Zhou,Y.W., Qiu,T.T., Wang,H., Zhu,M.S.,
            Chen,X. and Zhang,X.N.
  TITLE     Gallbladder dysfunction caused by MYPT1 ablation triggers
            cholestasis-induced hepatic fibrosis in mice
  JOURNAL   Hepatol Commun 8 (7), e0473 (2024)
   PUBMED   38934703
  REMARK    GeneRIF: Gallbladder dysfunction caused by MYPT1 ablation triggers
            cholestasis-induced hepatic fibrosis in mice.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Chen,J., Li,C.G., Yang,L.X., Qian,Y., Zhu,L.W., Liu,P.Y., Cao,X.,
            Wang,Y., Zhu,M.S. and Xu,Y.
  TITLE     MYPT1SMKO Mice Function as a Novel Spontaneous Age- and
            Hypertension-Dependent Animal Model of CSVD
  JOURNAL   Transl Stroke Res 15 (3), 606-619 (2024)
   PUBMED   36843141
  REMARK    GeneRIF: MYPT1[SMKO] Mice Function as a Novel Spontaneous Age- and
            Hypertension-Dependent Animal Model of CSVD.
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Nagaoka,T., Katsuno,T., Fujimura,K., Tsuchida,K. and Kishi,M.
  TITLE     Functional interaction between Vangl2 and N-cadherin regulates
            planar cell polarization of the developing neural tube and cochlear
            sensory epithelium
  JOURNAL   Sci Rep 13 (1), 3905 (2023)
   PUBMED   36890135
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1029)
  AUTHORS   Takahashi,H., Yang,G., Yoneshiro,T., Abe,Y., Ito,R., Yang,C.,
            Nakazono,J., Okamoto-Katsuyama,M., Uchida,A., Arai,M., Jin,H.,
            Choi,H., Tumenjargal,M., Xie,S., Zhang,J., Sagae,H., Zhao,Y.,
            Yamaguchi,R., Nomura,Y., Shimizu,Y., Yamada,K., Yasuda,S.,
            Kimura,H., Tanaka,T., Wada,Y., Kodama,T., Aburatani,H., Zhu,M.S.,
            Inagaki,T., Osborne,T.F., Kawamura,T., Ishihama,Y., Matsumura,Y.
            and Sakai,J.
  TITLE     MYPT1-PP1beta phosphatase negatively regulates both chromatin
            landscape and co-activator recruitment for beige adipogenesis
  JOURNAL   Nat Commun 13 (1), 5715 (2022)
   PUBMED   36175407
  REMARK    GeneRIF: MYPT1-PP1beta phosphatase negatively regulates both
            chromatin landscape and co-activator recruitment for beige
            adipogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1029)
  AUTHORS   Zhao,W., Sun,J., Yao,L.Y., Hang,D., Li,Y.Q., Chen,C.P., Zhou,Y.W.,
            Chen,X., Tao,T., Wei,L.S., Zheng,Y.Y., Ge,X., Li,C.J., Xin,Z.C.,
            Pan,Y., Wang,X.Z., He,W.Q., Zhang,X.N., Yao,B. and Zhu,M.S.
  TITLE     MYPT1 reduction is a pathogenic factor of erectile dysfunction
  JOURNAL   Commun Biol 5 (1), 744 (2022)
   PUBMED   35879418
  REMARK    GeneRIF: MYPT1 reduction is a pathogenic factor of erectile
            dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1029)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
REFERENCE   7  (residues 1 to 1029)
  AUTHORS   Arimura,T., Suematsu,N., Zhou,Y.B., Nishimura,J., Satoh,S.,
            Takeshita,A., Kanaide,H. and Kimura,A.
  TITLE     Identification, characterization, and functional analysis of
            heart-specific myosin light chain phosphatase small subunit
  JOURNAL   J Biol Chem 276 (9), 6073-6082 (2001)
   PUBMED   11067852
REFERENCE   8  (residues 1 to 1029)
  AUTHORS   Machida,H., Ito,M., Okamoto,R., Shiraki,K., Isaka,N.,
            Hartshorne,D.J. and Nakano,T.
  TITLE     Molecular cloning and analysis of the 5'-flanking region of the
            human MYPT1 gene
  JOURNAL   Biochim Biophys Acta 1517 (3), 424-429 (2001)
   PUBMED   11342221
REFERENCE   9  (residues 1 to 1029)
  AUTHORS   Tate,P., Lee,M., Tweedie,S., Skarnes,W.C. and Bickmore,W.A.
  TITLE     Capturing novel mouse genes encoding chromosomal and other nuclear
            proteins
  JOURNAL   J Cell Sci 111 (Pt 17), 2575-2585 (1998)
   PUBMED   9701556
REFERENCE   10 (residues 1 to 1029)
  AUTHORS   Kimura,K., Ito,M., Amano,M., Chihara,K., Fukata,Y., Nakafuku,M.,
            Yamamori,B., Feng,J., Nakano,T., Okawa,K., Iwamatsu,A. and
            Kaibuchi,K.
  TITLE     Regulation of myosin phosphatase by Rho and Rho-associated kinase
            (Rho-kinase)
  JOURNAL   Science 273 (5272), 245-248 (1996)
   PUBMED   8662509
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC139335.3.
            
            On Feb 22, 2019 this sequence version replaced XP_006513389.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849375,
                              SAMN00849380 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 56.33 cM"
     Protein         1..1029
                     /product="protein phosphatase 1 regulatory subunit 12A
                     isoform 1"
                     /note="myosin phosphatase target subunit 1; myosin
                     phosphatase-targeting subunit 1; protein phosphatase 1,
                     regulatory (inhibitor) subunit 12A"
                     /calculated_mol_wt=114866
     Region          35..38
                     /region_name="KVKF motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Region          39..331
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          39..68
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            order(49..51,53..54,58,61,70,72,74,78..79,82..84,86..87,
                     91,94,103,105,107,111..112,115..117,119..120,124,127,136)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Site            67
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Region          72..103
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          72..101
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            100
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Region          105..136
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          105..134
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Region          138..229
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          138..164
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Region          198..227
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            226
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Region          231..262
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          231..260
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Region          290..786
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NUAK1.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NUAK1.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Region          658..712
                     /region_name="IPD_MYPT1"
                     /note="inhibitory phosphorylation domain of myosin
                     phosphatase targeting subunit 1(MYPT1); cd21944"
                     /db_xref="CDD:412019"
     Region          680..863
                     /region_name="Interaction with ROCK2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKG, in vitro.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKG, in vitro.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK1, ROCK2, CDC42BP,
                     ZIPK/DAPK3 and RAF1.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            801
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Region          808..927
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            851
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ROCK2.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            870
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Site            909
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NUAK1.
                     /evidence=ECO:0000250|UniProtKB:O14974; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     Region          930..1029
                     /region_name="PRKG1_interact"
                     /note="cGMP-dependent protein kinase interacting domain;
                     pfam15898"
                     /db_xref="CDD:464927"
     Site            994
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DBR7.2)"
     CDS             1..1029
                     /gene="Ppp1r12a"
                     /gene_synonym="1200015F06Rik; 5730577I22Rik; D10Ertd625e;
                     Mypt1"
                     /coded_by="NM_001368736.1:303..3392"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS88083.1"
                     /db_xref="GeneID:17931"
                     /db_xref="MGI:MGI:1309528"
ORIGIN      
        1 mkmadakqkr neqlkrwigs etdleppvvk rqktkvkfdd gavflaacss gdtdevlkll
       61 hrgadinyan vdgltalhqa ciddnvdmvk flvenganin qpdnegwipl haaascgyld
      121 iaefligqga hvgavnsegd tpldiaeeea meellqnevn rqgvdieaar keeervmlrd
      181 arqwlnsghi sdvrhaksgg talhvaaakg ytevlklliq agydvnikdy dgwtplhaaa
      241 hwgkeeacri lvdnlcdmet vnkvgqtafd vadedilgyl eelqkkqtll hsekrdkksp
      301 liestanmen nqpqkafknk etliiepekn asrieslehe kadeeeegkk desscsseed
      361 eeddseseae tdktkpmasv snahtsstqa apaavtaptl ssnqgtptsp vkkfpisttk
      421 ispkeeerkd espaswrlgl rktgsygala eisaskeaqk ekdtagvmrs assprlsssl
      481 dnkekekdnk gtrlayvtpt iprrlastsd ieekenress slrtsssytr rkweddlkkn
      541 ssinegstyh rscsfgrrqd dliscsvpst tstptvtsaa glqrslpsst staaktppgs
      601 ssagtqssts nrlwaedste kekdsaptav tipvaptvvn aaapstttlt tttagtvsev
      661 rerrrsyltp vrdeesesqr karsrqarqs rrstqgvtlt dlqeaektig rsrstrtreq
      721 eneekekeek ekqdkekqee kkeseasred eykqkysrty detytryrpv stssssapss
      781 sslstlgstl yassqlnrpn slvgitsays rglakenere gekkeeekeg edksqpksir
      841 errrprekrr stgvsfwtqd sdeneqerqs dtedgsskre tqtdsvsryd ssstsssdry
      901 dsllgrsasy syledrkpys srlekddstd fkklyeqila eneklkaqlh dtnmeltdlk
      961 lqlekatqrq erfadrsqle mekrerrale rrisemeeel kmlpdlkadn qrlkdengal
     1021 irvisklsk
//
LOCUS       NP_004751                414 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein kinase 17A [Homo sapiens].
ACCESSION   NP_004751
VERSION     NP_004751.2
DBSOURCE    REFSEQ: accession NM_004760.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Pang,K., Lee,J., Kim,J., Park,J., Park,Y., Hong,E., An,H.,
            Ooshima,A., Son,M., Park,K.S., Cho,J.H., Lee,C., Song,Y.S.,
            Yang,K.M. and Kim,S.J.
  TITLE     Degradation of DRAK1 by CUL3/SPOP E3 Ubiquitin ligase promotes
            tumor growth of paclitaxel-resistant cervical cancer cells
  JOURNAL   Cell Death Dis 13 (2), 169 (2022)
   PUBMED   35194034
  REMARK    GeneRIF: Degradation of DRAK1 by CUL3/SPOP E3 Ubiquitin ligase
            promotes tumor growth of paclitaxel-resistant cervical cancer
            cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Wang,Z., Wang,C., Jiang,B.H., Shi,L., Lin,S., Wang,L., Liu,L.Z.,
            Qiu,J.G., Qin,Y. and Jia,Y.
  TITLE     Predictive significance of STK17A in patients with gastric cancer
            and association with gastric cancer cell proliferation and
            migration
  JOURNAL   Oncol Rep 45 (6) (2021)
   PUBMED   33955523
  REMARK    GeneRIF: Predictive significance of STK17A in patients with gastric
            cancer and association with gastric cancer cell proliferation and
            migration.
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Cho,J., Park,K., Choi,S.M., Lee,J., Lee,C.H., Lee,J.K., Heo,E.Y.,
            Kim,D.K., Lee,Y.J., Park,J.S., Cho,Y.J., Yoon,H.I., Lee,J.H.,
            Lee,C.T., Kim,N., Choi,K.Y., Lee,K.H., Sung,J., Won,S. and Yim,J.J.
  TITLE     Genome-wide association study of non-tuberculous mycobacterial
            pulmonary disease
  JOURNAL   Thorax 76 (2), 169-177 (2021)
   PUBMED   33115937
  REMARK    GeneRIF: Genome-wide association study of non-tuberculous
            mycobacterial pulmonary disease.
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Park,Y., Pang,K., Park,J., Hong,E., Lee,J., Ooshima,A., Kim,H.S.,
            Cho,J.H., Han,Y., Lee,C., Song,Y.S., Park,K.S., Yang,K.M. and
            Kim,S.J.
  TITLE     Destablilization of TRAF6 by DRAK1 Suppresses Tumor Growth and
            Metastasis in Cervical Cancer Cells
  JOURNAL   Cancer Res 80 (12), 2537-2549 (2020)
   PUBMED   32265222
  REMARK    GeneRIF: Destablilization of TRAF6 by DRAK1 Suppresses Tumor Growth
            and Metastasis in Cervical Cancer Cells.
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Wei,W. and Liu,C.
  TITLE     Prognostic and predictive roles of microRNA-411 and its target
            STK17A in evaluating radiotherapy efficacy and their effects on
            cell migration and invasion via the p53 signaling pathway in
            cervical cancer
  JOURNAL   Mol Med Rep 21 (1), 267-281 (2020)
   PUBMED   31746360
  REMARK    GeneRIF: Prognostic and predictive roles of microRNA411 and its
            target STK17A in evaluating radiotherapy efficacy and their effects
            on cell migration and invasion via the p53 signaling pathway in
            cervical cancer.
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Mao,P., Hever,M.P., Niemaszyk,L.M., Haghkerdar,J.M., Yanco,E.G.,
            Desai,D., Beyrouthy,M.J., Kerley-Hamilton,J.S., Freemantle,S.J. and
            Spinella,M.J.
  TITLE     Serine/threonine kinase 17A is a novel p53 target gene and
            modulator of cisplatin toxicity and reactive oxygen species in
            testicular cancer cells
  JOURNAL   J Biol Chem 286 (22), 19381-19391 (2011)
   PUBMED   21489989
  REMARK    GeneRIF: identified STK17A as a novel direct target of p53 and a
            modulator of cisplatin toxicity and reactive oxygen species in
            testicular cancer cells.
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Shimada,M., Miyagawa,T., Kawashima,M., Tanaka,S., Honda,Y.,
            Honda,M. and Tokunaga,K.
  TITLE     An approach based on a genome-wide association study reveals
            candidate loci for narcolepsy
  JOURNAL   Hum Genet 128 (4), 433-441 (2010)
   PUBMED   20677014
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Landa,I., Ruiz-Llorente,S., Montero-Conde,C., Inglada-Perez,L.,
            Schiavi,F., Leskela,S., Pita,G., Milne,R., Maravall,J., Ramos,I.,
            Andia,V., Rodriguez-Poyo,P., Jara-Albarran,A., Meoro,A., del
            Peso,C., Arribas,L., Iglesias,P., Caballero,J., Serrano,J.,
            Pico,A., Pomares,F., Gimenez,G., Lopez-Mondejar,P., Castello,R.,
            Merante-Boschin,I., Pelizzo,M.R., Mauricio,D., Opocher,G.,
            Rodriguez-Antona,C., Gonzalez-Neira,A., Matias-Guiu,X.,
            Santisteban,P. and Robledo,M.
  TITLE     The variant rs1867277 in FOXE1 gene confers thyroid cancer
            susceptibility through the recruitment of USF1/USF2 transcription
            factors
  JOURNAL   PLoS Genet 5 (9), e1000637 (2009)
   PUBMED   19730683
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Sanjo,H., Kawai,T. and Akira,S.
  TITLE     DRAKs, novel serine/threonine kinases related to death-associated
            protein kinase that trigger apoptosis
  JOURNAL   J Biol Chem 273 (44), 29066-29071 (1998)
   PUBMED   9786912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI461892.1, AB011420.1,
            AC005189.2 and AW183478.1.
            
            On Jun 19, 2006 this sequence version replaced NP_004751.1.
            
            Summary: This gene is a member of the DAP kinase-related
            apoptosis-inducing protein kinase family and encodes an
            autophosphorylated nuclear protein with a protein kinase domain.
            The protein has apoptosis-inducing activity. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.25120.1,
                                           SRR1803616.95452.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319357.6/ ENSP00000319192.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..414
                     /product="serine/threonine-protein kinase 17A"
                     /EC_number="2.7.11.1"
                     /note="death-associated protein kinase-related 1;
                     serine/threonine kinase 17a (apoptosis-inducing); DAP
                     kinase-related apoptosis-inducing protein kinase 1"
                     /calculated_mol_wt=46427
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UEE5.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q9UEE5.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UEE5.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UEE5.2)"
     Region          51..321
                     /region_name="STKc_DRAK1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Death-associated protein kinase-Related Apoptosis-inducing
                     protein Kinase 1; cd14197"
                     /db_xref="CDD:271099"
     Site            order(67..71,73,75,88,90,122,138..139,141,145,147,186,188,
                     190..191,193,206..207,210,225..228)
                     /site_type="active"
                     /db_xref="CDD:271099"
     Site            order(67..71,73,75,88,90,122,138..139,141,145,190..191,
                     193,206..207)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271099"
     Site            order(71,145,147,186,188,190,210,225..228)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271099"
     Site            206..228
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271099"
     Region          342..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UEE5.2)"
     CDS             1..414
                     /gene="STK17A"
                     /gene_synonym="DRAK1"
                     /coded_by="NM_004760.3:137..1381"
                     /db_xref="CCDS:CCDS5470.1"
                     /db_xref="GeneID:9263"
                     /db_xref="HGNC:HGNC:11395"
                     /db_xref="MIM:604726"
ORIGIN      
        1 miplekpgsg gsspgatsgs gragrglsgp crpppppqar gllteiravv rtepfqdgys
       61 lcpgrelgrg kfavvrkcik kdsgkefaak fmrkrrkgqd crmeiiheia vlelaqdnpw
      121 vinlhevyet asemilvley aaggeifdqc vadreeafke kdvqrlmrqi legvhflhtr
      181 dvvhldlkpq nilltsespl gdikivdfgl srilknseel reimgtpeyv apeilsydpi
      241 smatdmwsig vltyvmltgi spflgndkqe tflnisqmnl syseeefdvl sesavdfirt
      301 llvkkpedra taeeclkhpw ltqssiqeps frmekaleea nalqeghsvp einsdtdkse
      361 tkesivteel ivvtsytlgq crqsekekme qkaiskrfkf eepllqeipg efiy
//
LOCUS       NP_001352997             160 aa            linear   PRI 27-APR-2025
DEFINITION  cysteine-rich protein 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001352997 XP_024302210
VERSION     NP_001352997.1
DBSOURCE    REFSEQ: accession NM_001366068.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Suzuki,H., Okamoto-Katsuyama,M., Suwa,T., Maeda,R., Tamura,T.A. and
            Yamaguchi,Y.
  TITLE     TLP-mediated global transcriptional repression after double-strand
            DNA breaks slows down DNA repair and induces apoptosis
  JOURNAL   Sci Rep 9 (1), 4868 (2019)
   PUBMED   30890736
  REMARK    GeneRIF: TLP-mediated global transcriptional repression after
            double-strand DNA breaks slows down DNA repair and induces
            apoptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Casrouge,A., Veitia,R., Kirchner,J., Bevan,M.J. and
            Kanellopoulos,J.
  TITLE     The human and mouse orthologous LIM-only proteins respectively
            encoded in chromosome 6 and 17 show a different expression pattern
  JOURNAL   Microbes Infect 6 (12), 1063-1072 (2004)
   PUBMED   15380775
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL583834.6.
            
            On Sep 21, 2018 this sequence version replaced XP_024302210.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.27042.1,
                                           SRR5189655.23639.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..160
                     /product="cysteine-rich protein 3 isoform 2"
                     /note="thymus LIM protein TLP-A; chromosome 6 LIM domain
                     only protein"
                     /calculated_mol_wt=17860
     Region          5..58
                     /region_name="LIM1_TLP"
                     /note="The first LIM domain of thymus LIM protein (TLP);
                     cd09476"
                     /db_xref="CDD:188860"
     Site            order(5,8,26,29,32,35,53,57)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188860"
     Region          80..133
                     /region_name="LIM2_TLP"
                     /note="The second LIM domain of thymus LIM protein (TLP);
                     cd09477"
                     /db_xref="CDD:188861"
     Site            order(80,83,101,104,107,110,128,132)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188861"
     CDS             1..160
                     /gene="CRIP3"
                     /gene_synonym="CRP-3; h6LIMo; TLP; TLP-A"
                     /coded_by="NM_001366068.1:35..517"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:401262"
                     /db_xref="HGNC:HGNC:17751"
ORIGIN      
        1 mswtcprcqq pvffaekvss lgknwhrfcl kcerchsils pgghaehngr pychkpcyga
       61 lfgprgpphm ktftgetslc pgcgepvyfa ekvmslgrnw hrpclrcqrc hktltagsha
      121 ehdgvpychv pcygylfgpk gvnigdvgcy iydpvkikfk
//
LOCUS       NP_001230854             382 aa            linear   PRI 27-APR-2025
DEFINITION  MAP kinase-activated protein kinase 3 [Homo sapiens].
ACCESSION   NP_001230854
VERSION     NP_001230854.1
DBSOURCE    REFSEQ: accession NM_001243925.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Ludwig,S., Engel,K., Hoffmeyer,A., Sithanandam,G., Neufeld,B.,
            Palm,D., Gaestel,M. and Rapp,U.R.
  TITLE     3pK, a novel mitogen-activated protein (MAP) kinase-activated
            protein kinase, is targeted by three MAP kinase pathways
  JOURNAL   Mol Cell Biol 16 (12), 6687-6697 (1996)
   PUBMED   8943323
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Clifton,A.D., Young,P.R. and Cohen,P.
  TITLE     A comparison of the substrate specificity of MAPKAP kinase-2 and
            MAPKAP kinase-3 and their activation by cytokines and cellular
            stress
  JOURNAL   FEBS Lett 392 (3), 209-214 (1996)
   PUBMED   8774846
REFERENCE   7  (residues 1 to 382)
  AUTHORS   McLaughlin,M.M., Kumar,S., McDonnell,P.C., Van Horn,S., Lee,J.C.,
            Livi,G.P. and Young,P.R.
  TITLE     Identification of mitogen-activated protein (MAP) kinase-activated
            protein kinase-3, a novel substrate of CSBP p38 MAP kinase
  JOURNAL   J Biol Chem 271 (14), 8488-8492 (1996)
   PUBMED   8626550
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Sithanandam,G., Latif,F., Duh,F.M., Bernal,R., Smola,U., Li,H.,
            Kuzmin,I., Wixler,V., Geil,L. and Shrestha,S.
  TITLE     3pK, a new mitogen-activated protein kinase-activated protein
            kinase located in the small cell lung cancer tumor suppressor gene
            region
  JOURNAL   Mol Cell Biol 16 (3), 868-876 (1996)
   PUBMED   8622688
  REMARK    Erratum:[Mol Cell Biol 1996 Apr;16(4):1880]
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Ben-Levy,R., Leighton,I.A., Doza,Y.N., Attwood,P., Morrice,N.,
            Marshall,C.J. and Cohen,P.
  TITLE     Identification of novel phosphorylation sites required for
            activation of MAPKAP kinase-2
  JOURNAL   EMBO J 14 (23), 5920-5930 (1995)
   PUBMED   8846784
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Lavoie,J.N., Lambert,H., Hickey,E., Weber,L.A. and Landry,J.
  TITLE     Modulation of cellular thermoresistance and actin filament
            stability accompanies phosphorylation-induced changes in the
            oligomeric structure of heat shock protein 27
  JOURNAL   Mol Cell Biol 15 (1), 505-516 (1995)
   PUBMED   7799959
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM848086.1, U09578.1,
            AC096920.2 and BE301676.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the Ser/Thr protein kinase
            family. This kinase functions as a mitogen-activated protein kinase
            (MAP kinase)- activated protein kinase. MAP kinases are also known
            as extracellular signal-regulated kinases (ERKs), act as an
            integration point for multiple biochemical signals. This kinase was
            shown to be activated by growth inducers and stress stimulation of
            cells. In vitro studies demonstrated that ERK, p38 MAP kinase and
            Jun N-terminal kinase were all able to phosphorylate and activate
            this kinase, which suggested the role of this kinase as an
            integrative element of signaling in both mitogen and stress
            responses. This kinase was reported to interact with, phosphorylate
            and repress the activity of E47, which is a basic helix-loop-helix
            transcription factor known to be involved in the regulation of
            tissue-specific gene expression and cell differentiation. Alternate
            splicing results in multiple transcript variants that encode the
            same protein. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.211140.1,
                                           SRR1660807.98658.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000621469.5/ ENSP00000478922.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..382
                     /product="MAP kinase-activated protein kinase 3"
                     /EC_number="2.7.11.1"
                     /note="MAPKAP kinase 3; chromosome 3p kinase;
                     mitogen-activated protein kinase-activated protein kinase
                     3"
                     /calculated_mol_wt=42856
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Region          39..304
                     /region_name="STKc_MAPKAPK3"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Mitogen-activated protein kinase-activated protein kinase
                     3; cd14172"
                     /db_xref="CDD:271074"
     Site            order(50..55,58,71,73,98,118..121,125,127,165..166,168,
                     170..171,173,186..187,190,203..207,209)
                     /site_type="active"
                     /db_xref="CDD:271074"
     Site            order(50..55,58,71,73,98,118..121,171,173,186..187)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271074"
     Site            order(52..55,57,206..210,214,216,219,240,242..245,
                     259..260,262..263,287..288)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271074"
     Site            order(54,125,127,165..166,168,170,190,203..207,209)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271074"
     Site            order(186..195,197..207)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271074"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q3UMW7; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          307..343
                     /region_name="Autoinhibitory helix. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          335..344
                     /region_name="Nuclear export signal (NES).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          345..369
                     /region_name="p38 MAPK-binding site.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          350..353
                     /region_name="Bipartite nuclear localization signal 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          357..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          364..368
                     /region_name="Bipartite nuclear localization signal 2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     CDS             1..382
                     /gene="MAPKAPK3"
                     /gene_synonym="3PK; MAPKAP-K3; MAPKAP3; MAPKAPK-3; MDPT3;
                     MK-3; MK3"
                     /coded_by="NM_001243925.2:144..1292"
                     /db_xref="CCDS:CCDS2832.1"
                     /db_xref="GeneID:7867"
                     /db_xref="HGNC:HGNC:6888"
                     /db_xref="MIM:602130"
ORIGIN      
        1 mdgetaeeqg gpvpppvapg gpglggapgg rrepkkyavt ddyqlskqvl glgvngkvle
       61 cfhrrtgqkc alkllydspk arqevdhhwq asggphivci ldvyenmhhg krclliimec
      121 meggelfsri qergdqafte reaaeimrdi gtaiqflhsh niahrdvkpe nllytskekd
      181 avlkltdfgf akettqnalq tpcytpyyva pevlgpekyd kscdmwslgv imyillcgfp
      241 pfysntgqai spgmkrrirl gqygfpnpew sevsedakql irlllktdpt erltitqfmn
      301 hpwinqsmvv pqtplhtarv lqedkdhwde vkeemtsala tmrvdydqvk ikdlktsnnr
      361 llnkrrkkqa gsssasqgcn nq
//
LOCUS       NP_808592                395 aa            linear   PRI 27-APR-2025
DEFINITION  acid ceramidase isoform a preproprotein [Homo sapiens].
ACCESSION   NP_808592
VERSION     NP_808592.2
DBSOURCE    REFSEQ: accession NM_177924.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kleynerman,A., Rybova,J., Faber,M.L., McKillop,W.M., Levade,T. and
            Medin,J.A.
  TITLE     Acid Ceramidase Deficiency: Bridging Gaps between Clinical
            Presentation, Mouse Models, and Future Therapeutic Interventions
  JOURNAL   Biomolecules 13 (2), 274 (2023)
   PUBMED   36830643
  REMARK    GeneRIF: Acid Ceramidase Deficiency: Bridging Gaps between Clinical
            Presentation, Mouse Models, and Future Therapeutic Interventions.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Munk,R., Anerillas,C., Rossi,M., Tsitsipatis,D., Martindale,J.L.,
            Herman,A.B., Yang,J.H., Roberts,J.A., Varma,V.R., Pandey,P.R.,
            Thambisetty,M., Gorospe,M. and Abdelmohsen,K.
  TITLE     Acid ceramidase promotes senescent cell survival
  JOURNAL   Aging (Albany NY) 13 (12), 15750-15769 (2021)
   PUBMED   34102611
  REMARK    GeneRIF: Acid ceramidase promotes senescent cell survival.
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Malvi,P., Janostiak,R., Nagarajan,A., Zhang,X. and Wajapeyee,N.
  TITLE     N-acylsphingosine amidohydrolase 1 promotes melanoma growth and
            metastasis by suppressing peroxisome biogenesis-induced ROS
            production
  JOURNAL   Mol Metab 48, 101217 (2021)
   PUBMED   33766731
  REMARK    GeneRIF: N-acylsphingosine amidohydrolase 1 promotes melanoma
            growth and metastasis by suppressing peroxisome biogenesis-induced
            ROS production.
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Clifford,R.E., Govindarajah,N., Bowden,D., Sutton,P., Glenn,M.,
            Darvish-Damavandi,M., Buczacki,S., McDermott,U., Szulc,Z.,
            Ogretmen,B., Parsons,J.L. and Vimalachandran,D.
  TITLE     Targeting Acid Ceramidase to Improve the Radiosensitivity of Rectal
            Cancer
  JOURNAL   Cells 9 (12), 2693 (2020)
   PUBMED   33334013
  REMARK    GeneRIF: Targeting Acid Ceramidase to Improve the Radiosensitivity
            of Rectal Cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Ferlinz,K., Kopal,G., Bernardo,K., Linke,T., Bar,J., Breiden,B.,
            Neumann,U., Lang,F., Schuchman,E.H. and Sandhoff,K.
  TITLE     Human acid ceramidase: processing, glycosylation, and lysosomal
            targeting
  JOURNAL   J Biol Chem 276 (38), 35352-35360 (2001)
   PUBMED   11451951
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Li,C.M., Park,J.H., He,X., Levy,B., Chen,F., Arai,K., Adler,D.A.,
            Disteche,C.M., Koch,J., Sandhoff,K. and Schuchman,E.H.
  TITLE     The human acid ceramidase gene (ASAH): structure, chromosomal
            location, mutation analysis, and expression
  JOURNAL   Genomics 62 (2), 223-231 (1999)
   PUBMED   10610716
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Perry,D.K. and Hannun,Y.A.
  TITLE     The role of ceramide in cell signaling
  JOURNAL   Biochim Biophys Acta 1436 (1-2), 233-243 (1998)
   PUBMED   9838138
  REMARK    Review article
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Koch,J., Gartner,S., Li,C.M., Quintern,L.E., Bernardo,K.,
            Levran,O., Schnabel,D., Desnick,R.J., Schuchman,E.H. and
            Sandhoff,K.
  TITLE     Molecular cloning and characterization of a full-length
            complementary DNA encoding human acid ceramidase. Identification Of
            the first molecular lesion causing Farber disease
  JOURNAL   J Biol Chem 271 (51), 33110-33115 (1996)
   PUBMED   8955159
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Bernardo,K., Hurwitz,R., Zenk,T., Desnick,R.J., Ferlinz,K.,
            Schuchman,E.H. and Sandhoff,K.
  TITLE     Purification, characterization, and biosynthesis of human acid
            ceramidase
  JOURNAL   J Biol Chem 270 (19), 11098-11102 (1995)
   PUBMED   7744740
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Dyment,D.A., Bennett,S.A.L., Medin,J.A. and Levade,T.
  TITLE     ASAH1-Related Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29595935
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA306573.1, DA260852.1,
            AK289481.1, AY305384.1, AK222780.1, BU633536.1, AI241768.1 and
            AC124242.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 22, 2008 this sequence version replaced NP_808592.1.
            
            Summary: This gene encodes a member of the acid ceramidase family
            of proteins. Alternative splicing results in multiple transcript
            variants, at least one of which encodes a preproprotein that is
            proteolytically processed. Processing of this preproprotein
            generates alpha and beta subunits that heterodimerize to form the
            mature lysosomal enzyme, which catalyzes the degradation of
            ceramide into sphingosine and free fatty acid. This enzyme is
            overexpressed in multiple human cancers and may play a role in
            cancer progression. Mutations in this gene are associated with the
            lysosomal storage disorder, Farber lipogranulomatosis, and a
            neuromuscular disorder, spinal muscular atrophy with progressive
            myoclonic epilepsy. [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) differs in the 5' UTR and
            coding sequence compared to variant 2. The resulting isoform (a)
            includes a predicted signal peptide, is shorter and has a distinct
            N-terminus compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.46311.1,
                                           SRR5189664.67191.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154125 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000637790.2/ ENSP00000490272.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..395
                     /product="acid ceramidase isoform a preproprotein"
                     /EC_number="3.5.1.23"
                     /EC_number="3.5.1.109"
                     /note="acylsphingosine deacylase; putative 32 kDa heart
                     protein; acid CDase; N-acylsphingosine amidohydrolase
                     (acid ceramidase) 1; N-acylethanolamine hydrolase ASAH1;
                     glycosylceramide deacylase"
                     /calculated_mol_wt=42675
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2002
     mat_peptide     22..142
                     /product="Acid ceramidase subunit alpha.
                     /evidence=ECO:0000305|PubMed:29692406. /id=PRO_0000002312"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13510.5)"
                     /calculated_mol_wt=13705
     Region          45..108
                     /region_name="NAAA-beta"
                     /note="beta subunit of N-acylethanolamine-hydrolyzing acid
                     amidase; pfam15508"
                     /db_xref="CDD:464754"
     Region          134..379
                     /region_name="Ntn_AC_NAAA"
                     /note="AC_NAAA This conserved domain includes two closely
                     related proteins, acid ceramidase (AC, also known as
                     N-acylsphingosine amidohydrolase), and
                     N-acylethanolamine-hydrolyzing acid amidase (NAAA). AC
                     catalyzes the hydrolysis of ceramide to sphingosine
                     and...; cd01903"
                     /db_xref="CDD:238886"
     mat_peptide     143..395
                     /product="Acid ceramidase subunit beta.
                     /evidence=ECO:0000305|PubMed:29692406. /id=PRO_0000002313"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13510.5)"
                     /calculated_mol_wt=28988
     Site            162
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000269|PubMed:29692406; propagated from
                     UniProtKB/Swiss-Prot (Q13510.5)"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29692406,
                     ECO:0007744|PDB:5U7Z; propagated from UniProtKB/Swiss-Prot
                     (Q13510.5)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13510.5)"
     Site            259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:29692406,
                     ECO:0007744|PDB:5U7Z; propagated from UniProtKB/Swiss-Prot
                     (Q13510.5)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:29692406,
                     ECO:0007744|PDB:5U7Z; propagated from UniProtKB/Swiss-Prot
                     (Q13510.5)"
     Site            320
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000269|PubMed:29692406; propagated from
                     UniProtKB/Swiss-Prot (Q13510.5)"
     Site            333
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000269|PubMed:29692406; propagated from
                     UniProtKB/Swiss-Prot (Q13510.5)"
     Site            342
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29692406,
                     ECO:0007744|PDB:5U7Z; propagated from UniProtKB/Swiss-Prot
                     (Q13510.5)"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13510.5)"
     CDS             1..395
                     /gene="ASAH1"
                     /gene_synonym="AC; ACDase; ASAH; PHP; PHP32; SMAPME"
                     /coded_by="NM_177924.5:50..1237"
                     /note="isoform a preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS6006.1"
                     /db_xref="GeneID:427"
                     /db_xref="HGNC:HGNC:735"
                     /db_xref="MIM:613468"
ORIGIN      
        1 mpgrscvalv llaaavscav aqhappwted crkstyppsg ptyrgavpwy tinldlppyk
       61 rwhelmldka pvlkvivnsl knmintfvps gkimqvvdek lpgllgnfpg pfeeemkgia
      121 avtdiplgei isfnifyelf tictsivaed kkghlihgrn mdfgvflgwn inndtwvite
      181 qlkpltvnld fqrnnktvfk assfagyvgm ltgfkpglfs ltlnerfsin ggylgilewi
      241 lgkkdvmwig fltrtvlens tsyeeaknll tktkilapay filggnqsge gcvitrdrke
      301 sldvyeldak qgrwyvvqtn ydrwkhpffl ddrrtpakmc lnrtsqenis fetmydvlst
      361 kpvlnkltvy ttlidvtkgq fetylrdcpd pcigw
//
LOCUS       NP_064532                257 aa            linear   PRI 27-APR-2025
DEFINITION  THAP domain-containing protein 10 [Homo sapiens].
ACCESSION   NP_064532
VERSION     NP_064532.1
DBSOURCE    REFSEQ: accession NM_020147.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Li,Y., Ning,Q., Shi,J., Chen,Y., Jiang,M., Gao,L., Huang,W.,
            Jing,Y., Huang,S., Liu,A., Hu,Z., Liu,D., Wang,L., Nervi,C.,
            Dai,Y., Zhang,M.Q. and Yu,L.
  TITLE     A novel epigenetic AML1-ETO/THAP10/miR-383 mini-circuitry
            contributes to t(8;21) leukaemogenesis
  JOURNAL   EMBO Mol Med 9 (7), 933-949 (2017)
   PUBMED   28539478
  REMARK    GeneRIF: Altogether, these results revealed an unexpected and
            important epigenetic mini-circuit of AML1-ETO/THAP10/miR-383 in
            t(8;21) acute myeloid leukaemia, in which epigenetic suppression of
            THAP10 predicts a poor clinical outcome and represents a novel
            therapeutic target.
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 257)
  AUTHORS   De Souza Santos,E., De Bessa,S.A., Netto,M.M. and Nagai,M.A.
  TITLE     Silencing of LRRC49 and THAP10 genes by bidirectional promoter
            hypermethylation is a frequent event in breast cancer
  JOURNAL   Int J Oncol 33 (1), 25-31 (2008)
   PUBMED   18575747
  REMARK    GeneRIF: transcripts of LRRC49/THAP10 bidirectional gene pair are
            co-regulated by estrogen and that hypermethylation of the
            bidirectional promoter region simultaneously silences both genes.
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Roussigne,M., Kossida,S., Lavigne,A.C., Clouaire,T., Ecochard,V.,
            Glories,A., Amalric,F. and Girard,J.P.
  TITLE     The THAP domain: a novel protein motif with similarity to the
            DNA-binding domain of P element transposase
  JOURNAL   Trends Biochem Sci 28 (2), 66-69 (2003)
   PUBMED   12575992
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA272000.1, BC027857.1 and
            AC090868.4.
            
            Summary: This gene encodes a member of a family of proteins sharing
            an N-terminal Thanatos-associated domain. The Thanatos-associated
            domain contains a zinc finger signature similar to DNA-binding
            domains. This gene is part of a bidirectional gene pair on the long
            arm of chromosome 15 that is regulated by estrogen and may play a
            role in breast cancer. [provided by RefSeq, Nov 2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072414.1, SRR1660807.211441.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000249861.9/ ENSP00000249861.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q23"
     Protein         1..257
                     /product="THAP domain-containing protein 10"
                     /calculated_mol_wt=28220
     Region          4..90
                     /region_name="THAP"
                     /note="The THAP domain is a putative DNA-binding domain
                     (DBD) and probably also binds a zinc ion; smart00980"
                     /db_xref="CDD:214951"
     Region          154..178
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2Z0.1)"
     CDS             1..257
                     /gene="THAP10"
                     /coded_by="NM_020147.4:162..935"
                     /db_xref="CCDS:CCDS10237.1"
                     /db_xref="GeneID:56906"
                     /db_xref="HGNC:HGNC:23193"
                     /db_xref="MIM:612538"
ORIGIN      
        1 mparcvaahc gnttksgksl frfpkdravr llwdrfvrgc radwyggndr svicsdhfap
       61 acfdvssviq knlrfsqrlr lvagavptlh rvpapapkrg eegdqagrld trgelqaarh
      121 seaapgpvsc trpragkqaa asqitcenel vqtqphadnp sntvtsvpth ceegpvhkst
      181 qislkrprhr svgiqakvka fgkrlcnatt qteelwsrts slfdiyssds etdtdwdiks
      241 eqsdlsymav qvkeetc
//
LOCUS       NP_861522               1098 aa            linear   PRI 27-APR-2025
DEFINITION  beta-alanine-activating enzyme isoform 1 [Homo sapiens].
ACCESSION   NP_861522
VERSION     NP_861522.2
DBSOURCE    REFSEQ: accession NM_181806.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Drozak,J., Veiga-da-Cunha,M., Kadziolka,B. and Van Schaftingen,E.
  TITLE     Vertebrate Acyl CoA synthetase family member 4 (ACSF4-U26) is a
            beta-alanine-activating enzyme homologous to bacterial
            non-ribosomal peptide synthetase
  JOURNAL   FEBS J 281 (6), 1585-1597 (2014)
   PUBMED   24467666
  REMARK    GeneRIF: ACSF4 (U26) is a beta-alanine activating enzyme homologous
            to bacterial nonribosomal peptide synthetase. Experiments using the
            mouse protein suggest this enzyme may be involved in a rare
            intracellular reaction, possibly an infrequent post-translational
            or post-transcriptional modification.
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Watkins,P.A., Maiguel,D., Jia,Z. and Pevsner,J.
  TITLE     Evidence for 26 distinct acyl-coenzyme A synthetase genes in the
            human genome
  JOURNAL   J Lipid Res 48 (12), 2736-2750 (2007)
   PUBMED   17762044
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wang,L., Jil,C., Xu,Y., Xu,J., Dai,J., Wu,Q., Wu,M., Zou,X.,
            Sun,L., Gu,S., Xie,Y. and Mao,Y.
  TITLE     Cloning and characterization of a novel human homolog* of mouse
            U26, a putative PQQ-dependent AAS dehydrogenase
  JOURNAL   Mol Biol Rep 32 (1), 47-53 (2005)
   PUBMED   15865210
  REMARK    GeneRIF: Human 2-aminoadipic 6-semialdehyde dehydrogenase gene was
            cloned; its mRNA is ubiquitously expressed in adult tissues and is
            highly expressed in colon adenocarcinoma (CX-1) and colon
            adenocarcinoma (GI-112) cell lines.
REFERENCE   4  (residues 1 to 1098)
  AUTHORS   Wellenreuther,R., Schupp,I., Poustka,A. and Wiemann,S.
  CONSRTM   German cDNA Consortium
  TITLE     SMART amplification combined with cDNA size fractionation in order
            to obtain large full-length clones
  JOURNAL   BMC Genomics 5 (1), 36 (2004)
   PUBMED   15198809
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1098)
  AUTHORS   Kasahara,T. and Kato,T.
  TITLE     Nutritional biochemistry: A new redox-cofactor vitamin for mammals
  JOURNAL   Nature 422 (6934), 832 (2003)
   PUBMED   12712191
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC306784.1, AY314787.1,
            AK304309.1 and AA743758.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 18, 2004 this sequence version replaced NP_861522.1.
            
            Summary: This gene encodes a member of the non-ribosome peptide
            syntesase (NRPS) enzyme family. The encoded protein contains an
            AMP-binding domain, PP-binding (phosphopantetheine, or pantetheine
            4'phosphate-binding) domain and the Pyrrolo-quinoline quinon (PQQ)
            binding domain. The protein is expressed in several adult tissues.
            [provided by RefSeq, Apr 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY422212.1, AK316296.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000205214.11/ ENSP00000205214.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..1098
                     /product="beta-alanine-activating enzyme isoform 1"
                     /EC_number="6.2.1.-"
                     /note="acyl-CoA synthetase family member 4; 2-aminoadipic
                     6-semialdehyde dehydrogenase; non-ribosomal peptide
                     synthetase 998; non-ribosomal peptide synthetase 1098;
                     beta-alanine-activating enzyme"
                     /calculated_mol_wt=122467
     Region          15..533
                     /region_name="A_NRPS_acs4"
                     /note="acyl-CoA synthetase family member 4; cd17654"
                     /db_xref="CDD:341309"
     Site            order(195,198..203,205..206)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341309"
     Site            order(198..199,319..320,342..347,375,428,439,442,527)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341309"
     Region          552..>608
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q4L235.3)"
     Site            724
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q4L235.3)"
     Region          750..1091
                     /region_name="PQQ_DH_like"
                     /note="PQQ-dependent dehydrogenases and related proteins;
                     cl11493"
                     /db_xref="CDD:472205"
     CDS             1..1098
                     /gene="AASDH"
                     /gene_synonym="ACSF4; LYS2; NRPS1098; NRPS998"
                     /coded_by="NM_181806.4:173..3469"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3504.1"
                     /db_xref="GeneID:132949"
                     /db_xref="HGNC:HGNC:23993"
                     /db_xref="MIM:614365"
ORIGIN      
        1 mtlqelvhka ascymdrvav cfdecnnqlp vyytyktvvn aaselsnfll lhcdfqgire
       61 iglycqpgid lpswilgilq vpaayvpiep dsppslsthf mkkcnlkyil vekkqinkfk
      121 sfhetllnyd tftvehndlv lfrlhwknte vnlmlndgke kyekekiksi ssehvneeka
      181 eehmdlrlkh clayvlhtsg ttgipkivrv phkcivpniq hfrvlfditq edvlflaspl
      241 tfdpsvveif lalssgasll ivptsvkllp sklasvlfsh hrvtvlqatp tllrrfgsql
      301 ikstvlsatt slrvlalgge afpsltvlrs wrgegnktqi fnvygitevs swatiyripe
      361 ktlnstlkce lpvqlgfpll gtvvevrdtn gftiqegsgq vflggrnrvc flddevtvpl
      421 gtmratgdfv tvkdgeiffl grkdsqikrh gkrlnielvq qvaeelqqve scavtwynqe
      481 klilfmvskd asvkeyifke lqkylpshav pdelvlidsl pftshgkidv selnkiylny
      541 inlksenkls gkedlweklq ylwkstlnlp edllrvpdes lflnsggdsl ksirllseie
      601 klvgtsvpgl leiilsssil eiynhilqtv vpdedvtfrk scatkrklsd inqeeasgts
      661 lhqkaimtft chneinafvv lsrgsqilsl nstrfltklg hcssacpsds vsqtniqnlk
      721 glnspvligk skdpscvakv seegkpaigt qkmelhvrwr sdtgkcvdas plvviptfdk
      781 ssttvyigsh shrmkavdfy sgkvkweqil gdriessacv skcgnfivvg cynglvyvlk
      841 snsgekywmf ttedavkssa tmdpttgliy igshdqhaya ldiyrkkcvw kskcggtvfs
      901 spclnliphh lyfatlggll lavnpatgnv iwkhscgkpl fsspqccsqy icigcvdgnl
      961 lcfthfgeqv wqfstsgpif sspctspseq kiffgshdcf iyccnmkghl qwkfettsrv
     1021 yatpfafhny ngsnemllaa astdgkvwil esqsgqlqsv yelpgevfss pvvlesmlii
     1081 gcrdnyvycl dllggnqk
//
LOCUS       NP_001229738             727 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 6 isoform a [Homo
            sapiens].
ACCESSION   NP_001229738
VERSION     NP_001229738.1
DBSOURCE    REFSEQ: accession NM_001242809.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Luan,L., Li,N., Zhang,K., Wang,X. and Pan,H.
  TITLE     Diversin upregulates the proliferative ability of colorectal cancer
            by inducing cell cycle proteins
  JOURNAL   Exp Mol Pathol 129, 104850 (2023)
   PUBMED   36623636
  REMARK    GeneRIF: Diversin upregulates the proliferative ability of
            colorectal cancer by inducing cell cycle proteins.
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Allache,R., Wang,M., De Marco,P., Merello,E., Capra,V. and Kibar,Z.
  TITLE     Genetic studies of ANKRD6 as a molecular switch between Wnt
            signaling pathways in human neural tube defects
  JOURNAL   Birth Defects Res A Clin Mol Teratol 103 (1), 20-26 (2015)
   PUBMED   25200652
  REMARK    GeneRIF: missense mutations in ANKRD6 are associated with neural
            tube defects.
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Jones,C., Qian,D., Kim,S.M., Li,S., Ren,D., Knapp,L., Sprinzak,D.,
            Avraham,K.B., Matsuzaki,F., Chi,F. and Chen,P.
  TITLE     Ankrd6 is a mammalian functional homolog of Drosophila planar cell
            polarity gene diego and regulates coordinated cellular orientation
            in the mouse inner ear
  JOURNAL   Dev Biol 395 (1), 62-72 (2014)
   PUBMED   25218921
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Wang,M., Yu,X., Dong,Q. and Wang,Y.
  TITLE     Diversin is overexpressed in human gliomas and its depletion
            inhibits proliferation and invasion
  JOURNAL   Tumour Biol 35 (8), 7905-7909 (2014)
   PUBMED   24833088
  REMARK    GeneRIF: diversin is overexpressed in human glioma and regulates
            glioma cell proliferation and invasion, possibly through MMP9
REFERENCE   5  (residues 1 to 727)
  AUTHORS   Yu,X., Wang,M., Dong,Q. and Jin,F.
  TITLE     Diversin is overexpressed in breast cancer and accelerates cell
            proliferation and invasion
  JOURNAL   PLoS One 9 (5), e98591 (2014)
   PUBMED   24858714
  REMARK    GeneRIF: study demonstrated that diversin was overexpressed in
            human breast cancers. Diversin could contribute to breast cancer
            cell proliferation and invasion.
            Erratum:[PLoS One. 2014;9(12):e116045]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 727)
  AUTHORS   Li,J., Liu,F., Wang,H., Liu,X., Liu,J., Li,N., Wan,F., Wang,W.,
            Zhang,C., Jin,S., Liu,J., Zhu,P. and Liu,Y.
  TITLE     Systematic mapping and functional analysis of a family of human
            epididymal secretory sperm-located proteins
  JOURNAL   Mol Cell Proteomics 9 (11), 2517-2528 (2010)
   PUBMED   20736409
REFERENCE   7  (residues 1 to 727)
  AUTHORS   Haribaskar,R., Putz,M., Schupp,B., Skouloudaki,K., Bietenbeck,A.,
            Walz,G. and Schafer,T.
  TITLE     The planar cell polarity (PCP) protein Diversin translocates to the
            nucleus to interact with the transcription factor AF9
  JOURNAL   Biochem Biophys Res Commun 387 (1), 212-217 (2009)
   PUBMED   19591803
  REMARK    GeneRIF: Diversin, containing several nuclear localization signals,
            translocates to the nucleus, where it interacts with the
            transcription factor AF9.
REFERENCE   8  (residues 1 to 727)
  AUTHORS   Miyasaka,K.Y., Kida,Y.S., Sato,T., Minami,M. and Ogura,T.
  TITLE     Csrp1 regulates dynamic cell movements of the mesendoderm and
            cardiac mesoderm through interactions with Dishevelled and Diversin
  JOURNAL   Proc Natl Acad Sci U S A 104 (27), 11274-11279 (2007)
   PUBMED   17592114
REFERENCE   9  (residues 1 to 727)
  AUTHORS   Schwarz-Romond,T., Asbrand,C., Bakkers,J., Kuhl,M., Schaeffer,H.J.,
            Huelsken,J., Behrens,J., Hammerschmidt,M. and Birchmeier,W.
  TITLE     The ankyrin repeat protein Diversin recruits Casein kinase Iepsilon
            to the beta-catenin degradation complex and acts in both canonical
            Wnt and Wnt/JNK signaling
  JOURNAL   Genes Dev 16 (16), 2073-2084 (2002)
   PUBMED   12183362
REFERENCE   10 (residues 1 to 727)
  AUTHORS   Tissir,F., Bar,I., Goffinet,A.M. and Lambert De Rouvroit,C.
  TITLE     Expression of the ankyrin repeat domain 6 gene (Ankrd6) during
            mouse brain development
  JOURNAL   Dev Dyn 224 (4), 465-469 (2002)
   PUBMED   12203740
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL138717.6, DN999929.1, AK295731.1 and AL096678.8.
            
            Transcript Variant: This variant (1) and variant 2 encode the same
            longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.11198.1,
                                           SRR1803616.2790.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000339746.9/ ENSP00000345767.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q15"
     Protein         1..727
                     /product="ankyrin repeat domain-containing protein 6
                     isoform a"
                     /note="ankyrin repeat domain-containing protein 6;
                     diversin; diego homolog; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=79840
     Region          9..38
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     Region          14..244
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(41,43,47..48,51..53,55..56,60,63,72,74,76,80..81,
                     84..86,88..89,93,96,105,107,109,113..114,117..119,
                     121..122,126,129,138)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          41..72
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          41..70
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     Region          74..105
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          74..103
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     Region          107..138
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          107..136
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     Region          140..169
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     Region          141..171
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(142,146..147,150..152,154..155,159,162,171,173,175,
                     179..180,183..185,187..188,192,195,204,206,208,212..213,
                     216..218,220..221,225,228,237)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          173..204
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          173..202
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     Region          206..237
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          206..235
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     Region          239..268
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     Region          277..386
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     Region          548..586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     Region          601..657
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G4.3)"
     CDS             1..727
                     /gene="ANKRD6"
                     /coded_by="NM_001242809.2:368..2551"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS56441.1"
                     /db_xref="GeneID:22881"
                     /db_xref="HGNC:HGNC:17280"
                     /db_xref="MIM:610583"
ORIGIN      
        1 msqqdavaal serllvaayk gqtenvvqli nkgarvavtk hgrtplhlaa nkghlpvvqi
       61 llkagcdldv qddgdqtalh ratvvgntei iaalihegca ldrqdkdgnt alheaswhgf
      121 sqsakllika ganvlaknka gntalhlacq nshsqstrvl llagsradlk nnagdtclhv
      181 aarynhlsii rllltafcsv heknqagdta lhvaaalnhk kvakilleag adttivnnag
      241 qtpletaryh nnpevalllt kapqvlrfsr grslrkkrer lkeerraqsv prdevaqskg
      301 svsagdtpss eqavarkeea reeflsaspe prakddrrrk srpkvsafsd ptppadqqpg
      361 hqknlhahnh pkkrnrhrcs spppphefra yqlytlyrgk dgkvmqapin gcrceplink
      421 lenqleatve eikaelgsvq dkmntklgqm enktqhqmrv ldklmverls aerteclnrl
      481 qqhsdtekhe gekrqislvd elktwcmlki qnleqklsgd sracrakstp stcesstgvd
      541 qlvvtagpaa asdssppvvr pkekalnsta tqrlqqelss sdctgsrlrn vkvqtallpm
      601 neaarsdqqa gpcvnrgtqt kksgksgptr hraqqpaass tcgqpppatg seqtgphird
      661 tsqaleltqy ffeavstqme kwyerkieea rsqanqkaqq dkatlkehik sleeelaklr
      721 trvqken
//
LOCUS       NP_689814                641 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 709 [Homo sapiens].
ACCESSION   NP_689814
VERSION     NP_689814.1
DBSOURCE    REFSEQ: accession NM_152601.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX954970.1, DA493682.1, AC008758.7 and BQ027911.1.
            
            Sequence Note: This RefSeq was created from transcript and genomic
            sequence data to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DC351830.1, SRR1803615.87868.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267750, SAMN03267752
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397732.8/ ENSP00000380840.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..641
                     /product="zinc finger protein 709"
                     /calculated_mol_wt=74522
     Region          3..44
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          77..551
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          104..124
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(147,149,151,153..154,157..158,161,175,177,181..182,
                     185..186,189,203,205,207,209..210,213..214,217)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(170,173,186,190)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(282,285,298,302)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(399,401,403,405..406,409..410,413,427,429,433..434,
                     437..438,441,455,457,459,461..462,465..466,469)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          422..442
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(422,425,438,442)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          450..470
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          478..498
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(483,485,487,489..490,493..494,497,511,513,517..518,
                     521..522,525,539,541,543,545..546,549..550,553)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          506..526
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(506,509,522,526)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          534..554
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          548..571
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          562..582
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..599
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          590..610
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          602..627
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          618..638
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..641
                     /gene="ZNF709"
                     /coded_by="NM_152601.4:160..2085"
                     /db_xref="CCDS:CCDS42504.1"
                     /db_xref="GeneID:163051"
                     /db_xref="HGNC:HGNC:20629"
ORIGIN      
        1 mdsvvfedva vnftqeewal lgpsqkklyr dvmqetfvnl asigenweek niedhknqgr
       61 klrshmverl cerkegsqfg etisqtpnpk pnkktftrvk pyecsvcgkd ymchsslnrh
      121 mrshtehrsy eyhkygeksy eckecgkrfs frssfriher thtgekpykc kqcgkafswp
      181 ssfqiherth tgekpyecke cgkafiyhtt frghmrmhtg ekpykckecg ktfshpssfr
      241 nherthsgek pyeckqcgka fryyqtfqih erthtgekpy qckqcgkals cptsfrsher
      301 ihtgekpykc kkcgkafsfp ssfrkherih tgekpydcke cgkafislps yrrhmimhtg
      361 ngpykckecg kafdcpssfq iherthtgek pyeckqcgka fscsssfrmh erthtgekph
      421 eckqcgkafs csssvriher thtgekpyec kqcgkafscs ssfrmherih tgekpyeckq
      481 cgkafsfsss frmherthtg ekpyeckqcg kafscsssfr mherthtgek pyeckqcgka
      541 fscsssirih erthtgekpy eckqcgkafs csssvrmher thtgvkpyec kqcdkafscs
      601 rsfriherth tgekpyacqq cgkafkcsrs frihervhsg e
//
LOCUS       NP_082418                381 aa            linear   ROD 27-APR-2025
DEFINITION  putative methyltransferase NSUN4 isoform a [Mus musculus].
ACCESSION   NP_082418
VERSION     NP_082418.1
DBSOURCE    REFSEQ: accession NM_028142.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Metodiev,M.D., Spahr,H., Loguercio Polosa,P., Meharg,C., Becker,C.,
            Altmueller,J., Habermann,B., Larsson,N.G. and Ruzzenente,B.
  TITLE     NSUN4 is a dual function mitochondrial protein required for both
            methylation of 12S rRNA and coordination of mitoribosomal assembly
  JOURNAL   PLoS Genet 10 (2), e1004110 (2014)
   PUBMED   24516400
  REMARK    GeneRIF: The presented data suggest that NSUN4 has a key role in
            controlling a final step in ribosome biogenesis to ensure that only
            the mature SSU and LSU are assembled.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Chi,L. and Delgado-Olguin,P.
  TITLE     Expression of NOL1/NOP2/sun domain (Nsun) RNA methyltransferase
            family genes in early mouse embryogenesis
  JOURNAL   Gene Expr Patterns 13 (8), 319-327 (2013)
   PUBMED   23816522
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Camara,Y., Asin-Cayuela,J., Park,C.B., Metodiev,M.D., Shi,Y.,
            Ruzzenente,B., Kukat,C., Habermann,B., Wibom,R., Hultenby,K.,
            Franz,T., Erdjument-Bromage,H., Tempst,P., Hallberg,B.M.,
            Gustafsson,C.M. and Larsson,N.G.
  TITLE     MTERF4 regulates translation by targeting the methyltransferase
            NSUN4 to the mammalian mitochondrial ribosome
  JOURNAL   Cell Metab 13 (5), 527-539 (2011)
   PUBMED   21531335
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Jamsai,D., Rijal,S., Bianco,D.M., O'Connor,A.E., Merriner,D.J.,
            Smith,S.J., Gibbs,G.M. and O'Bryan,M.K.
  TITLE     A novel protein, sperm head and tail associated protein (SHTAP),
            interacts with cysteine-rich secretory protein 2 (CRISP2) during
            spermatogenesis in the mouse
  JOURNAL   Biol Cell 102 (2), 93-106 (2009)
   PUBMED   19686095
  REMARK    GeneRIF: expression and localization of SHTAP in testis and sperm
            raise the possibility that the SHTAP-CRISP2 complex has a potential
            role in sperm formation and/or function.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL627105.13.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC024628.1, AK012994.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 53.1 cM"
     Protein         1..381
                     /product="putative methyltransferase NSUN4 isoform a"
                     /note="sperm head and tail associated protein; putative
                     methyltransferase NSUN4; 5-methylcytosine tRNA
                     methyltransferase NSUN4; 5-cytosine tRNA methyltransferase
                     NSUN4"
                     /calculated_mol_wt=39929
     transit_peptide 1..25
                     /note="Mitochondrion.
                     /evidence=ECO:0000250|UniProtKB:Q96CB9; propagated from
                     UniProtKB/Swiss-Prot (Q9CZ57.1)"
                     /calculated_mol_wt=2943
     mat_peptide     26..381
                     /product="5-cytosine rRNA methyltransferase NSUN4.
                     /id=PRO_0000289235"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZ57.1)"
                     /calculated_mol_wt=39929
     Region          152..323
                     /region_name="nop2p"
                     /note="NOL1/NOP2/sun family putative RNA methylase;
                     TIGR00446"
                     /db_xref="CDD:188051"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96CB9; propagated from
                     UniProtKB/Swiss-Prot (Q9CZ57.1)"
     CDS             1..381
                     /gene="Nsun4"
                     /gene_synonym="2310010O12Rik; 2810405F18Rik; Shtap"
                     /coded_by="NM_028142.5:36..1181"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS18502.1"
                     /db_xref="GeneID:72181"
                     /db_xref="MGI:MGI:1919431"
ORIGIN      
        1 maapvlrcvr kllklvdftp vprryrykkk wattepqfta srlalqnfdm tysvqfgdlw
       61 psirvsllse qkygalvnnf aawdsvsakl eqlsakdfvs eaishqklep esglsptpsl
      121 dcspnlrcft fsrgdvsrfp parlgslglm dyylmdaasl lpvlalglqh gdtvldlcaa
      181 pggktlallq tgccrnlaan dlstsrtgrl qkvlhsyvpq diregnqvrv tswdgrkwge
      241 legdtydrvl vdvpcttdrh slheeennif qrsrkkerqm lpmlqvqlla agllatkpgg
      301 hvvystcsls hlqneyvvqg aiellanqyn ikvqvedlsh frklfmdtfc ffpscqvgel
      361 vipnlmvnfg pmyfcklhrl p
//
LOCUS       NP_112188                267 aa            linear   PRI 27-APR-2025
DEFINITION  integral membrane protein 2C isoform 1 [Homo sapiens].
ACCESSION   NP_112188
VERSION     NP_112188.1
DBSOURCE    REFSEQ: accession NM_030926.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Maurya,N.S., Kushwaha,S., Vetukuri,R.R. and Mani,A.
  TITLE     Unlocking the Potential of the CA2, CA7, and ITM2C Gene Signatures
            for the Early Detection of Colorectal Cancer: A Comprehensive
            Analysis of RNA-Seq Data by Utilizing Machine Learning Algorithms
  JOURNAL   Genes (Basel) 14 (10), 1836 (2023)
   PUBMED   37895185
  REMARK    GeneRIF: Unlocking the Potential of the CA2, CA7, and ITM2C Gene
            Signatures for the Early Detection of Colorectal Cancer: A
            Comprehensive Analysis of RNA-Seq Data by Utilizing Machine
            Learning Algorithms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Matsuda,S., Matsuda,Y. and D'Adamio,L.
  TITLE     CD74 interacts with APP and suppresses the production of Abeta
  JOURNAL   Mol Neurodegener 4, 41 (2009)
   PUBMED   19849849
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Wu,H., Liu,G., Li,C. and Zhao,S.
  TITLE     bri3, a novel gene, participates in tumor necrosis
            factor-alpha-induced cell death
  JOURNAL   Biochem Biophys Res Commun 311 (2), 518-524 (2003)
   PUBMED   14592447
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Vidal,R., Calero,M., Revesz,T., Plant,G., Ghiso,J. and Frangione,B.
  TITLE     Sequence, genomic structure and tissue expression of Human BRI3, a
            member of the BRI gene family
  JOURNAL   Gene 266 (1-2), 95-102 (2001)
   PUBMED   11290423
REFERENCE   8  (residues 1 to 267)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 267)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
REFERENCE   10 (residues 1 to 267)
  AUTHORS   Deleersnijder,W., Hong,G., Cortvrindt,R., Poirier,C.,
            Tylzanowski,P., Pittois,K., Van Marck,E. and Merregaert,J.
  TITLE     Isolation of markers for chondro-osteogenic differentiation using
            cDNA library subtraction. Molecular cloning and characterization of
            a gene belonging to a novel multigene family of integral membrane
            proteins
  JOURNAL   J Biol Chem 271 (32), 19475-19482 (1996)
   PUBMED   8702637
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF272043.1 and BC098563.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Both variants 1 and 5 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF271781.1, AF272043.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326427.11/ ENSP00000322730.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..267
                     /product="integral membrane protein 2C isoform 1"
                     /note="BRICHOS domain containing 2C; integral membrane
                     protein 3; cerebral protein 14; transmembrane protein
                     BRI3"
                     /calculated_mol_wt=30093
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5PQL7; propagated from
                     UniProtKB/Swiss-Prot (Q9NQX7.1)"
     Site            55..75
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQX7.1)"
     Region          136..228
                     /region_name="BRICHOS"
                     /note="The BRICHOS domain is found in a variety of
                     proteins implicated in dementia, respiratory distress and
                     cancer; smart01039"
                     /db_xref="CDD:198107"
     Site            169
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:15606899; propagated from
                     UniProtKB/Swiss-Prot (Q9NQX7.1)"
     Site            242..243
                     /site_type="cleavage"
                     /note="Cleavage, by furin; propagated from
                     UniProtKB/Swiss-Prot (Q9NQX7.1)"
     mat_peptide     243..267
                     /product="CT-BRI3. /id=PRO_0000232645"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQX7.1)"
                     /calculated_mol_wt=2735
     CDS             1..267
                     /gene="ITM2C"
                     /gene_synonym="BRI3; BRICD2C; E25; E25C; ITM3"
                     /coded_by="NM_030926.6:85..888"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2479.1"
                     /db_xref="GeneID:81618"
                     /db_xref="HGNC:HGNC:6175"
                     /db_xref="MIM:609554"
ORIGIN      
        1 mvkisfqpav agikgdkadk asasapapas ateilltpar eeqppqhrsk rggsvggvcy
       61 lsmgmvvllm glvfasvyiy ryfflaqlar dnffrcgvly edslssqvrt qmeleedvki
      121 yldenyerin vpvpqfgggd padiihdfqr gltayhdisl dkcyvielnt tivlpprnfw
      181 ellmnvkrgt ylpqtyiiqe emvvtehvsd kealgsfiyh lcngkdtyrl rrratrrrin
      241 krgakncnai rhfentfvve tlicgvv
//
LOCUS       NP_001356001             893 aa            linear   ROD 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 8 [Mus
            musculus].
ACCESSION   NP_001356001 XP_006539093
VERSION     NP_001356001.1
DBSOURCE    REFSEQ: accession NM_001369072.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Thoren,L.A., Norgaard,G.A., Weischenfeldt,J., Waage,J.,
            Jakobsen,J.S., Damgaard,I., Bergstrom,F.C., Blom,A.M., Borup,R.,
            Bisgaard,H.C. and Porse,B.T.
  TITLE     UPF2 is a critical regulator of liver development, function and
            regeneration
  JOURNAL   PLoS One 5 (7), e11650 (2010)
   PUBMED   20657840
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Combes,A.N., Lesieur,E., Harley,V.R., Sinclair,A.H., Little,M.H.,
            Wilhelm,D. and Koopman,P.
  TITLE     Three-dimensional visualization of testis cord morphogenesis, a
            novel tubulogenic mechanism in development
  JOURNAL   Dev Dyn 238 (5), 1033-1041 (2009)
   PUBMED   19334288
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Hoffman,B.G., Zavaglia,B., Witzsche,J., Ruiz de Algara,T.,
            Beach,M., Hoodless,P.A., Jones,S.J., Marra,M.A. and Helgason,C.D.
  TITLE     Identification of transcripts with enriched expression in the
            developing and adult pancreas
  JOURNAL   Genome Biol 9 (6), R99 (2008)
   PUBMED   18554416
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   5  (residues 1 to 893)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 893)
  AUTHORS   Cobellis,G., Nicolaus,G., Iovino,M., Romito,A., Marra,E.,
            Barbarisi,M., Sardiello,M., Di Giorgio,F.P., Iovino,N., Zollo,M.,
            Ballabio,A. and Cortese,R.
  TITLE     Tagging genes with cassette-exchange sites
  JOURNAL   Nucleic Acids Res 33 (4), e44 (2005)
   PUBMED   15741177
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL627185.10 and AL627078.10.
            
            On Mar 17, 2019 this sequence version replaced XP_006539093.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.28186.1,
                                           SRR9219382.30920.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 67.34 cM"
     Protein         1..893
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 8"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein;
                     plenty-of-prolines-101"
                     /calculated_mol_wt=100457
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          594..>791
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..893
                     /gene="Srrm1"
                     /gene_synonym="POP101; Srm160"
                     /coded_by="NM_001369072.1:30..2711"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:51796"
                     /db_xref="MGI:MGI:1858303"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrtksrsp
      181 spapekkeks pelpepsvrm kdssvqeats tsdilkapkp epvpepkeps peknskkeke
      241 ktrprsrsrs ksrsrtrsrs pshtrprrrh rsrsrsyspr rrpsprrrps prrrtpprrm
      301 pppprhrrsr spgrrrrrss aslsgsssss sssrsrsppk kppkrtsspp rktrrlspsa
      361 spprrrhrps spatpppktr hsptpqqsnr trksrvsvsp grtsgkvtkh kgtekresps
      421 papkprkvel seseedkgsk maaadsvqqr rqyrrqnqqs ssdsgsssts ederpkrshv
      481 kngevgrrrr hspsrsasps prkrqketsp rmqmgkrwqs pvtkssrrrr spsppparrr
      541 rspspapppp pppppprrrr sptppprrrt psppprrrsp sprrysppiq rryspspppk
      601 rrtasppppp krraspsppp krrvshsppp kqrsptvtkr rspslsskhr kgsspgrstr
      661 earspqpnkr hspsprprap qtsspppvrr gasaspqgrq spspstrpir rvsrtpepkk
      721 ikkaaspspq svrrvsssrs vsgspepaak kppappspvq sqspstnwsp avpakkaksp
      781 tpslsparns dqegggkkkk kkkdkkhkkd kkhkkhkkhk kekavtiatp ataapaavsa
      841 atttsaqeep aaapeprket eseaeddnld dlerhlreka lrsmrkaqvs pqs
//
LOCUS       NP_083745                201 aa            linear   ROD 27-APR-2025
DEFINITION  homeobox protein goosecoid-2 [Mus musculus].
ACCESSION   NP_083745 XP_001476859 XP_001480663 XP_001480801
VERSION     NP_083745.2
DBSOURCE    REFSEQ: accession NM_029469.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Ruiz-Reig,N., Rakotobe,M., Bethus,I., Le Menn,G., Huditz,H.I.,
            Marie,H., Lamonerie,T. and D'Autreaux,F.
  TITLE     Developmental Requirement of Homeoprotein Otx2 for Specific
            Habenulo-Interpeduncular Subcircuits
  JOURNAL   J Neurosci 39 (6), 1005-1019 (2019)
   PUBMED   30593496
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Thompson,C.L., Ng,L., Menon,V., Martinez,S., Lee,C.K.,
            Glattfelder,K., Sunkin,S.M., Henry,A., Lau,C., Dang,C.,
            Garcia-Lopez,R., Martinez-Ferre,A., Pombero,A., Rubenstein,J.L.R.,
            Wakeman,W.B., Hohmann,J., Dee,N., Sodt,A.J., Young,R., Smith,K.,
            Nguyen,T.N., Kidney,J., Kuan,L., Jeromin,A., Kaykas,A., Miller,J.,
            Page,D., Orta,G., Bernard,A., Riley,Z., Smith,S., Wohnoutka,P.,
            Hawrylycz,M.J., Puelles,L. and Jones,A.R.
  TITLE     A high-resolution spatiotemporal atlas of gene expression of the
            developing mouse brain
  JOURNAL   Neuron 83 (2), 309-323 (2014)
   PUBMED   24952961
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Chung,Y.C., Tsai,Y.J., Shiu,T.Y., Sun,Y.Y., Wang,P.F. and Chen,C.L.
  TITLE     Screening large numbers of expression patterns of transcription
            factors in late stages of the mouse thymus
  JOURNAL   Gene Expr Patterns 11 (1-2), 84-92 (2011)
   PUBMED   20932939
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Funato,H., Sato,M., Sinton,C.M., Gautron,L., Williams,S.C.,
            Skach,A., Elmquist,J.K., Skoultchi,A.I. and Yanagisawa,M.
  TITLE     Loss of Goosecoid-like and DiGeorge syndrome critical region 14 in
            interpeduncular nucleus results in altered regulation of rapid eye
            movement sleep
  JOURNAL   Proc Natl Acad Sci U S A 107 (42), 18155-18160 (2010)
   PUBMED   20921407
  REMARK    GeneRIF: results indicate that the absence of Gscl and Dgcr14 in
            the IP results in altered regulation of REM sleep
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Maynard,T.M., Haskell,G.T., Peters,A.Z., Sikich,L., Lieberman,J.A.
            and LaMantia,A.S.
  TITLE     A comprehensive analysis of 22q11 gene expression in the developing
            and adult brain
  JOURNAL   Proc Natl Acad Sci U S A 100 (24), 14433-14438 (2003)
   PUBMED   14614146
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Puech,A., Saint-Jore,B., Funke,B., Gilbert,D.J., Sirotkin,H.,
            Copeland,N.G., Jenkins,N.A., Kucherlapati,R., Morrow,B. and
            Skoultchi,A.I.
  TITLE     Comparative mapping of the human 22q11 chromosomal region and the
            orthologous region in mice reveals complex changes in gene
            organization
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14608-14613 (1997)
   PUBMED   9405660
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Funke,B., Saint-Jore,B., Puech,A., Sirotkin,H., Edelmann,L.,
            Carlson,C., Raft,S., Pandita,R.K., Kucherlapati,R., Skoultchi,A.
            and Morrow,B.E.
  TITLE     Characterization and mutation analysis of goosecoid-like (GSCL), a
            homeodomain-containing gene that maps to the critical region for
            VCFS/DGS on 22q11
  JOURNAL   Genomics 46 (3), 364-372 (1997)
   PUBMED   9441739
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Botta,A., Lindsay,E.A., Jurecic,V. and Baldini,A.
  TITLE     Comparative mapping of the DiGeorge syndrome region in mouse shows
            inconsistent gene order and differential degree of gene
            conservation
  JOURNAL   Mamm Genome 8 (12), 890-895 (1997)
   PUBMED   9383280
  REMARK    Erratum:[Mamm Genome 1998 Apr;9(4):344]
REFERENCE   9  (residues 1 to 201)
  AUTHORS   Galili,N., Baldwin,H.S., Lund,J., Reeves,R., Gong,W., Wang,Z.,
            Roe,B.A., Emanuel,B.S., Nayak,S., Mickanin,C., Budarf,M.L. and
            Buck,C.A.
  TITLE     A region of mouse chromosome 16 is syntenic to the DiGeorge,
            velocardiofacial syndrome minimal critical region
  JOURNAL   Genome Res 7 (1), 17-26 (1997)
   PUBMED   9037598
  REMARK    Erratum:[Genome Res. 1997 Apr;7(4):399. PMID: 9110179]
REFERENCE   10 (residues 1 to 201)
  AUTHORS   Halford,S., Wadey,R., Roberts,C., Daw,S.C., Whiting,J.A.,
            O'Donnell,H., Dunham,I., Bentley,D., Lindsay,E., Baldini,A. et al.
  TITLE     Isolation of a putative transcriptional regulator from the region
            of 22q11 deleted in DiGeorge syndrome, Shprintzen syndrome and
            familial congenital heart disease
  JOURNAL   Hum Mol Genet 2 (12), 2099-2107 (1993)
   PUBMED   8111380
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC125356.1 and AK016252.1.
            
            On Feb 12, 2019 this sequence version replaced NP_083745.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC132637.1, SRR7345562.1450018.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849376, SAMN01164138
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="16"
                     /map="16 11.1 cM"
     Protein         1..201
                     /product="homeobox protein goosecoid-2"
                     /note="GSC-L"
                     /calculated_mol_wt=21891
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56916.2)"
     Region          95..124
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56916.2)"
     Region          124..180
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          179..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56916.2)"
     CDS             1..201
                     /gene="Gsc2"
                     /gene_synonym="4930568H22Rik; GSC-2; Gscl"
                     /coded_by="NM_029469.2:25..630"
                     /db_xref="CCDS:CCDS49786.2"
                     /db_xref="GeneID:195333"
                     /db_xref="MGI:MGI:892006"
ORIGIN      
        1 matagsaasr rdpgrpcpfs iehilsslpe rrpatrppqp vggrnpaeld epeapvpaap
       61 cacccccnpr aatrgtpets sgpglrlawp lrlapatpsp ltapragspa ltgtsgpgpq
      121 rrtrrhrtif seeqlqalea lfvqnqypdv gtrerlavri rlreervevw fknrrakwrh
      181 qkrasssrll pgtkktpkes c
//
LOCUS       NP_004958                317 aa            linear   PRI 27-APR-2025
DEFINITION  integrin-binding sialoprotein precursor [Homo sapiens].
ACCESSION   NP_004958
VERSION     NP_004958.2
DBSOURCE    REFSEQ: accession NM_004967.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Ma,Y., Chen,B., Zhang,B., Zhang,C., Zhu,Q., Wang,X., Liu,Z. and
            Liu,H.
  TITLE     High expression of integrin-binding sialoprotein (IBSP) is
            associated with poor prognosis of osteosarcoma
  JOURNAL   Aging (Albany NY) 16 (1), 28-42 (2023)
   PUBMED   38006395
  REMARK    GeneRIF: High expression of integrin-binding sialoprotein (IBSP) is
            associated with poor prognosis of osteosarcoma.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Fonseca,J.M., Martins,M.D., Vargas,P.A., Silva,W.G.,
            Normando,A.G.C., Palmier,N.R., Ribeiro,A.C.P., Brandao,T.B.,
            Lopes,M.A., Goes,M.F. and Santos-Silva,A.R.
  TITLE     Preservation of immunoexpression of type I collagen, BSP and BMP4
            in the dentin-pulp complex of head and neck cancer patients after
            radiotherapy
  JOURNAL   Braz Oral Res 36, e012 (2022)
   PUBMED   35081229
  REMARK    GeneRIF: Preservation of immunoexpression of type I collagen, BSP
            and BMP4 in the dentin-pulp complex of head and neck cancer
            patients after radiotherapy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Chen,Y., Qin,Y., Dai,M., Liu,L., Ni,Y., Sun,Q., Li,L., Zhou,Y.,
            Qiu,C. and Jiang,Y.
  TITLE     IBSP, a potential recurrence biomarker, promotes the progression of
            colorectal cancer via Fyn/beta-catenin signaling pathway
  JOURNAL   Cancer Med 10 (12), 4030-4045 (2021)
   PUBMED   33987980
  REMARK    GeneRIF: IBSP, a potential recurrence biomarker, promotes the
            progression of colorectal cancer via Fyn/beta-catenin signaling
            pathway.
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Benz,F., Bogen,A., Praktiknjo,M., Jansen,C., Meyer,C., Wree,A.,
            Demir,M., Loosen,S., Vucur,M., Schierwagen,R., Tacke,F.,
            Trebicka,J. and Roderburg,C.
  TITLE     Serum levels of bone sialoprotein correlate with portal pressure in
            patients with liver cirrhosis
  JOURNAL   PLoS One 15 (4), e0231701 (2020)
   PUBMED   32302330
  REMARK    GeneRIF: Study analyzed circulating bone sialoprotein (BSP) in a
            large cohort of patients with liver cirrhosis. Serum levels of BSP
            were similar in patients with different disease stages and were not
            indicative for prognosis. BSP serum levels did correlate inversely
            with portal pressure. BSP might represent a previously unrecognized
            marker for portal hypertension in patients with liver cirrhosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Maaroufi,A., Khadem-Ansari,M.H., Khalkhali,H.R. and Rasmi,Y.
  TITLE     Serum levels of bone sialoprotein, osteopontin, and
            beta2-microglobulin in stage I of multiple myeloma
  JOURNAL   J Cancer Res Ther 16 (1), 98-101 (2020)
   PUBMED   32362616
  REMARK    GeneRIF: Serum levels of bone sialoprotein, osteopontin, and
            beta2-microglobulin in stage I of multiple myeloma.
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Kim,R.H., Shapiro,H.S., Li,J.J., Wrana,J.L. and Sodek,J.
  TITLE     Characterization of the human bone sialoprotein (BSP) gene and its
            promoter sequence
  JOURNAL   Matrix Biol 14 (1), 31-40 (1994)
   PUBMED   8061918
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Goold,R.D., diSibio,G.L., Xu,H., Lang,D.B., Dadgar,J.,
            Magrane,G.G., Dugaiczyk,A., Smith,K.A., Cox,D.R., Masters,S.B. et
            al.
  TITLE     The development of sequence-tagged sites for human chromosome 4
  JOURNAL   Hum Mol Genet 2 (8), 1271-1288 (1993)
   PUBMED   8401509
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Fisher,L.W., McBride,O.W., Termine,J.D. and Young,M.F.
  TITLE     Human bone sialoprotein. Deduced protein sequence and chromosomal
            localization
  JOURNAL   J Biol Chem 265 (4), 2347-2351 (1990)
   PUBMED   2404984
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Oldberg,A., Franzen,A., Heinegard,D., Pierschbacher,M. and
            Ruoslahti,E.
  TITLE     Identification of a bone sialoprotein receptor in osteosarcoma
            cells
  JOURNAL   J Biol Chem 263 (36), 19433-19436 (1988)
   PUBMED   2461939
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Fisher,L.W., Hawkins,G.R., Tuross,N. and Termine,J.D.
  TITLE     Purification and partial characterization of small proteoglycans I
            and II, bone sialoproteins I and II, and osteonectin from the
            mineral compartment of developing human bone
  JOURNAL   J Biol Chem 262 (20), 9702-9708 (1987)
   PUBMED   3597437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093768.3, AI751848.1,
            J05213.1, DV462680.1, BQ573754.1 and AA452255.1.
            
            On Feb 8, 2008 this sequence version replaced NP_004958.1.
            
            Summary: The protein encoded by this gene is a major structural
            protein of the bone matrix. It constitutes approximately 12% of the
            noncollagenous proteins in human bone and is synthesized by
            skeletal-associated cell types, including hypertrophic
            chondrocytes, osteoblasts, osteocytes, and osteoclasts. The only
            extraskeletal site of its synthesis is the trophoblast. This
            protein binds to calcium and hydroxyapatite via its acidic amino
            acid clusters, and mediates cell attachment through an RGD sequence
            that recognizes the vitronectin receptor. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.193979.1,
                                           SRR1660807.136311.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000226284.7/ ENSP00000226284.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.1"
     Protein         1..317
                     /product="integrin-binding sialoprotein precursor"
                     /note="bone sialoprotein II; bone sialoprotein 2; BSP II;
                     cell-binding sialoprotein"
                     /calculated_mol_wt=33517
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1649
     mat_peptide     17..317
                     /product="integrin-binding sialoprotein"
                     /calculated_mol_wt=33517
     Region          17..314
                     /region_name="BSP_II"
                     /note="Bone sialoprotein II (BSP-II); pfam05432"
                     /db_xref="CDD:461651"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11669636; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Region          58..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21815.4)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            119
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            122
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            182
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            227
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            228
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            229
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            238
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            239
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Region          286..288
                     /region_name="cell-attachment tripeptide"
     Site            313
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000269|PubMed:11669636; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            314
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000269|PubMed:11669636; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     CDS             1..317
                     /gene="IBSP"
                     /gene_synonym="BNSP; BSP; BSP-II; SP-II"
                     /coded_by="NM_004967.4:95..1048"
                     /db_xref="CCDS:CCDS3624.1"
                     /db_xref="GeneID:3381"
                     /db_xref="HGNC:HGNC:5341"
                     /db_xref="MIM:147563"
ORIGIN      
        1 mktalillsi lgmacafsmk nlhrrvkied seengvfkyr pryylykhay fyphlkrfpv
       61 qgssdsseen gddsseeeee eeetsnegen neesnededs eaenttlsat tlgygedatp
      121 gtgytglaai qlpkkagdit nkatkekesd eeeeeeeegn eneeseaevd eneqgingts
      181 tnsteaengn gssggdngee geeesvtgan aedttetgrq gkgtskttts pnggfepttp
      241 pqvyrttspp fgktttveye geyeytgane ydngyeiyes engeprgdny rayedeysyf
      301 kgqgydgydg qnyyhhq
//
LOCUS       NP_694533                592 aa            linear   PRI 27-APR-2025
DEFINITION  signal peptide peptidase-like 2B isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_694533 NP_064557
VERSION     NP_694533.1
DBSOURCE    REFSEQ: accession NM_152988.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Maccioni,R., Travisan,C., Badman,J., Zerial,S., Wagener,A.,
            Andrade-Talavera,Y., Picciau,F., Grassi,C., Chen,G., Lemoine,L.,
            Fisahn,A., Jiang,R., Fluhrer,R., Mentrup,T., Schroder,B.,
            Nilsson,P. and Tambaro,S.
  TITLE     Signal peptide peptidase-like 2b modulates the amyloidogenic
            pathway and exhibits an Abeta-dependent expression in Alzheimer's
            disease
  JOURNAL   Prog Neurobiol 235, 102585 (2024)
   PUBMED   38367747
  REMARK    GeneRIF: Signal peptide peptidase-like 2b modulates the
            amyloidogenic pathway and exhibits an Abeta-dependent expression in
            Alzheimer's disease.
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Mentrup,T., Theodorou,K., Cabrera-Cabrera,F., Helbig,A.O., Happ,K.,
            Gijbels,M., Gradtke,A.C., Rabe,B., Fukumori,A., Steiner,H.,
            Tholey,A., Fluhrer,R., Donners,M. and Schroder,B.
  TITLE     Atherogenic LOX-1 signaling is controlled by SPPL2-mediated
            intramembrane proteolysis
  JOURNAL   J Exp Med 216 (4), 807-830 (2019)
   PUBMED   30819724
  REMARK    GeneRIF: SPPL2a/b negatively regulates LOX-1 signaling and
            atherosclerosis.
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Nalls,M.A., Pankratz,N., Lill,C.M., Do,C.B., Hernandez,D.G.,
            Saad,M., DeStefano,A.L., Kara,E., Bras,J., Sharma,M., Schulte,C.,
            Keller,M.F., Arepalli,S., Letson,C., Edsall,C., Stefansson,H.,
            Liu,X., Pliner,H., Lee,J.H., Cheng,R., Ikram,M.A., Ioannidis,J.P.,
            Hadjigeorgiou,G.M., Bis,J.C., Martinez,M., Perlmutter,J.S.,
            Goate,A., Marder,K., Fiske,B., Sutherland,M., Xiromerisiou,G.,
            Myers,R.H., Clark,L.N., Stefansson,K., Hardy,J.A., Heutink,P.,
            Chen,H., Wood,N.W., Houlden,H., Payami,H., Brice,A., Scott,W.K.,
            Gasser,T., Bertram,L., Eriksson,N., Foroud,T. and Singleton,A.B.
  CONSRTM   International Parkinson's Disease Genomics Consortium (IPDGC);
            Parkinson's Study Group (PSG) Parkinson's Research: The Organized
            GENetics Initiative (PROGENI); 23andMe; GenePD; NeuroGenetics
            Research Consortium (NGRC); Hussman Institute of Human Genomics
            (HIHG); Ashkenazi Jewish Dataset Investigator; Cohorts for Health
            and Aging Research in Genetic Epidemiology (CHARGE); North American
            Brain Expression Consortium (NABEC); United Kingdom Brain
            Expression Consortium (UKBEC); Greek Parkinson's Disease
            Consortium; Alzheimer Genetic Analysis Group
  TITLE     Large-scale meta-analysis of genome-wide association data
            identifies six new risk loci for Parkinson's disease
  JOURNAL   Nat Genet 46 (9), 989-993 (2014)
   PUBMED   25064009
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Zahn,C., Kaup,M., Fluhrer,R. and Fuchs,H.
  TITLE     The transferrin receptor-1 membrane stub undergoes intramembrane
            proteolysis by signal peptide peptidase-like 2b
  JOURNAL   FEBS J 280 (7), 1653-1663 (2013)
   PUBMED   23384347
  REMARK    GeneRIF: TfR1 N-terminal fragment is a substrate for intramembrane
            proteolysis by SPPL2b.
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Friedmann,E., Lemberg,M.K., Weihofen,A., Dev,K.K., Dengler,U.,
            Rovelli,G. and Martoglio,B.
  TITLE     Consensus analysis of signal peptide peptidase and homologous human
            aspartic proteases reveals opposite topology of catalytic domains
            compared with presenilins
  JOURNAL   J Biol Chem 279 (49), 50790-50798 (2004)
   PUBMED   15385547
  REMARK    GeneRIF: SPP, SPPL2a, -2b, -2c, and -3 probably cleave type
            II-oriented substrate peptides as shown by consensus analysis
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Grigorenko,A.P., Moliaka,Y.K., Korovaitseva,G.I. and Rogaev,E.I.
  TITLE     Novel class of polytopic proteins with domains associated with
            putative protease activity
  JOURNAL   Biochemistry (Mosc) 67 (7), 826-835 (2002)
   PUBMED   12139484
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Weihofen,A., Binns,K., Lemberg,M.K., Ashman,K. and Martoglio,B.
  TITLE     Identification of signal peptide peptidase, a presenilin-type
            aspartic protease
  JOURNAL   Science 296 (5576), 2215-2218 (2002)
   PUBMED   12077416
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Petroff,O.A., Novotny,E.J., Ogino,T., Avison,M. and Prichard,J.W.
  TITLE     In vivo measurements of ethanol concentration in rabbit brain by 1H
            magnetic resonance spectroscopy
  JOURNAL   J Neurochem 54 (4), 1188-1195 (1990)
   PUBMED   2313285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC093046.1, AB040965.1 and
            BU733058.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 26, 2006 this sequence version replaced NP_064557.1.
            
            Summary: This gene encodes a member of the GXGD family of aspartic
            proteases. The GXGD proteases are transmembrane proteins with two
            conserved catalytic motifs localized within the membrane-spanning
            regions. This enzyme localizes to endosomes, lysosomes, and the
            plasma membrane. It cleaves the transmembrane domain of tumor
            necrosis factor alpha to release the intracellular domain, which
            triggers cytokine expression in the innate and adaptive immunity
            pathways. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) represents the shorter
            transcript but encodes the longer isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB040965.1, BC093046.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000613503.5/ ENSP00000478298.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..592
                     /product="signal peptide peptidase-like 2B isoform 2
                     precursor"
                     /EC_number="3.4.23.-"
                     /note="SPP-like 2B; intramembrane protease 4;
                     presenilin-like protein 1; presenilin homologous protein
                     4"
                     /calculated_mol_wt=62248
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2414
     Region          44..163
                     /region_name="PA_hSPPL_like"
                     /note="Protease-associated domain containing human signal
                     peptide peptidase-like (hSPPL)-like. This group contains
                     various PA domain-containing proteins similar to hSPPL2a
                     and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is
                     sorted to the late endosomes; cd02129"
                     /db_xref="CDD:239044"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Site            124..126
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:239044"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Site            175..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Region          213..505
                     /region_name="Peptidase_A22B"
                     /note="Signal peptide peptidase; pfam04258"
                     /db_xref="CDD:282158"
     Site            222..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Site            249..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Site            294..314
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Site            320..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Site            349..369
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Site            413..433
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Site            446..466
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Site            471..491
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Region          472..474
                     /region_name="PAL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Region          512..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT7.2)"
     Region          <520..590
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     CDS             1..592
                     /gene="SPPL2B"
                     /gene_synonym="IMP-4; IMP4; PSH4; PSL1"
                     /coded_by="NM_152988.3:27..1805"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS74252.1"
                     /db_xref="GeneID:56928"
                     /db_xref="HGNC:HGNC:30627"
                     /db_xref="MIM:608239"
ORIGIN      
        1 maaavaaala rllaafllla aqvaceygmv hvvsqaggpe gkdycilynp qwahlphdls
       61 kasflqlrnw tasllcsaad lpargfsnqi plvargnctf yekvrlaqgs gargllivsr
      121 erlvppggnk tqydeigipv allsykdmld iftrfgrtvr aalyapkepv ldynmviifi
      181 mavgtvaigg ywagsrdvkk rymkhkrddg pekqedeavd vtpvmtcvfv vmccsmlvll
      241 yyfydllvyv vigifclasa tglysclapc vrrlpfgkcr ipnnslpyfh krpqarmlll
      301 alfcvavsvv wgvfrnedqw awvlqdalgi afclymlkti rlptfkactl lllvlflydi
      361 ffvfitpflt ksgssimvev atgpsdsatr eklpmvlkvp rlnssplalc drpfsllgfg
      421 dilvpgllva ychrfdiqvq ssrvyfvact iaygvgllvt fvalalmqrg qpallylvpc
      481 tlvtscaval wrrelgvfwt gsgfakvlpp spwapapadg pqppkdsatp lspqppseep
      541 atspwpaeqs pksrtseemg agapmrepgs paesegrdqa qpspvtqpga sa
//
LOCUS       NP_001356046             864 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 618 isoform g [Mus musculus].
ACCESSION   NP_001356046
VERSION     NP_001356046.1
DBSOURCE    REFSEQ: accession NM_001369117.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Lee,D.J., Kim,H.Y., Lee,S.J. and Jung,H.S.
  TITLE     Spatiotemporal Changes in Transcriptome of Odontogenic and
            Non-odontogenic Regions in the Dental Arch of Mus musculus
  JOURNAL   Front Cell Dev Biol 9, 723326 (2021)
   PUBMED   34722506
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Quina,L.A., Wang,S., Ng,L. and Turner,E.E.
  TITLE     Brn3a and Nurr1 mediate a gene regulatory pathway for habenula
            development
  JOURNAL   J Neurosci 29 (45), 14309-14322 (2009)
   PUBMED   19906978
REFERENCE   3  (residues 1 to 864)
  AUTHORS   Georgas,K., Rumballe,B., Valerius,M.T., Chiu,H.S.,
            Thiagarajan,R.D., Lesieur,E., Aronow,B.J., Brunskill,E.W.,
            Combes,A.N., Tang,D., Taylor,D., Grimmond,S.M., Potter,S.S.,
            McMahon,A.P. and Little,M.H.
  TITLE     Analysis of early nephron patterning reveals a role for distal RV
            proliferation in fusion to the ureteric tip via a cap
            mesenchyme-derived connecting segment
  JOURNAL   Dev Biol 332 (2), 273-286 (2009)
   PUBMED   19501082
REFERENCE   4  (residues 1 to 864)
  AUTHORS   Long,J.E., Cobos,I., Potter,G.B. and Rubenstein,J.L.
  TITLE     Dlx1&2 and Mash1 transcription factors control MGE and CGE
            patterning and differentiation through parallel and overlapping
            pathways
  JOURNAL   Cereb Cortex 19 Suppl 1 (Suppl 1), i96-i106 (2009)
   PUBMED   19386638
REFERENCE   5  (residues 1 to 864)
  AUTHORS   Kumar,S., Tomooka,Y. and Noda,M.
  TITLE     Identification of a set of genes with developmentally
            down-regulated expression in the mouse brain
  JOURNAL   Biochem Biophys Res Commun 185 (3), 1155-1161 (1992)
   PUBMED   1378265
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL691431.20 and AL691496.13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3315547.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 33.82 cM"
     Protein         1..864
                     /product="zinc finger protein 618 isoform g"
                     /note="neural precursor cell expressed, developmentally
                     down-regulated gene 10"
                     /calculated_mol_wt=95558
     Region          60..80
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          101..121
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..864
                     /gene="Zfp618"
                     /gene_synonym="2810031P15Rik; 2810040O04Rik; bM257P7.1;
                     D430033D05Rik; Nedd10; Znf618"
                     /coded_by="NM_001369117.1:368..2962"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="GeneID:72701"
                     /db_xref="MGI:MGI:1919950"
ORIGIN      
        1 mtevkvktev pddyiqeviw qgeakeekag gkdstgdvpa eicvviggvr nqqtlgsyec
       61 gicgkkykyy ncfqthvrah rdteatsgeg vsqsnnfryt cdicgkkyky yscfqehrdl
      121 havdvfsveg apenradpfd qgvvatdevk eeppepfqki gpktgnytce fcgkqykyyt
      181 pyqehvalha pistapgwep pedpdtgsec shpevtpspr fvaaktqsnq sgkkapasvv
      241 rctsllhrtp patqtqtfra pnsgspaska aaentfsrrv eskaqnhfee tnsssqnsse
      301 pytcgacgiq fqfysnlleh mqshaadnen nitsnqsrsp paaveekwkp qaqrnsannt
      361 ttsgltpnsv ipekerqnia erllrvmcad lgalsvvsgk eflklaqtlv dsgarygafs
      421 vteilgnfnt lalkhlprmy nqvkvkvtca lgsnaclgig vtchsqsvgp dscyiltayq
      481 aegnhiksyv lgvkgadird sgdlvhhwvq nvlsefvmse irtvyvtdcr vstsafskag
      541 mclrcsacal nsvvqsvlsk rtlqarsmhe viellnvced lagstglake tfgsleetsp
      601 ppcwnsvtds lllvheryeq icefysrakk mnliqslnkh llsnlaailt pvkqaviels
      661 nesqptlqlv lptyvrlekl ftakandagt vsklchlfle alkenfkvhp ahkvamildp
      721 qqklrpvppy qheeiiskvc elinevkesw aeeadfepaa kkarsatgeh paaqeedrlg
      781 knevydylqe plfqatpdlf qywscvtqkh tklaklafwl lavpavgars gcvnmceqal
      841 likrrrllsp edmnklmflk snml
//
LOCUS       NP_060177                903 aa            linear   PRI 27-APR-2025
DEFINITION  arf-GAP with SH3 domain, ANK repeat and PH domain-containing
            protein 3 isoform a [Homo sapiens].
ACCESSION   NP_060177
VERSION     NP_060177.2
DBSOURCE    REFSEQ: accession NM_017707.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Song,X., Xu,W., Xu,G., Kong,S., Ding,L., Xiao,J., Cao,X. and
            Wang,F.
  TITLE     ACAP4 interacts with CrkII to promote the recycling of integrin
            beta1
  JOURNAL   Biochem Biophys Res Commun 516 (1), 8-14 (2019)
   PUBMED   31182282
  REMARK    GeneRIF: ACAP4 physically interacts with CrkII. Functional
            characterization showed that the interaction is required for the
            recruitment of ACAP4 to the plasma membrane where ACAP4 functions
            to regulate the recycling of the signal transducer integrin beta1.
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Guo,L., Fu,J., Sun,S., Zhu,M., Zhang,L., Niu,H., Chen,Z., Zhang,Y.,
            Guo,L. and Wang,S.
  TITLE     MicroRNA-143-3p inhibits colorectal cancer metastases by targeting
            ITGA6 and ASAP3
  JOURNAL   Cancer Sci 110 (2), 805-816 (2019)
   PUBMED   30536996
  REMARK    GeneRIF: MiR-143-3p acts as an anti-oncogene by downregulating
            ITGA6/ASAP3 protein expression and could offer new insight into
            potential therapeutic targets for CRC.
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Ismail,S.A., Vetter,I.R., Sot,B. and Wittinghofer,A.
  TITLE     The structure of an Arf-ArfGAP complex reveals a Ca2+ regulatory
            mechanism
  JOURNAL   Cell 141 (5), 812-821 (2010)
   PUBMED   20510928
  REMARK    GeneRIF: The ArfGAP catalytic mechanism and shows a glutamine from
            Arf6 and an arginine fingerASAP3 as the important catalytic
            residues; unexpectedly the structure shows a calcium ion, liganded
            by both proteins in the complex interface.
            Erratum:[Cell. 2010 Dec 23;143(7):1190]
REFERENCE   7  (residues 1 to 903)
  AUTHORS   Brehme,M., Hantschel,O., Colinge,J., Kaupe,I., Planyavsky,M.,
            Kocher,T., Mechtler,K., Bennett,K.L. and Superti-Furga,G.
  TITLE     Charting the molecular network of the drug target Bcr-Abl
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7414-7419 (2009)
   PUBMED   19380743
REFERENCE   8  (residues 1 to 903)
  AUTHORS   Ha,V.L., Bharti,S., Inoue,H., Vass,W.C., Campa,F., Nie,Z., de
            Gramont,A., Ward,Y. and Randazzo,P.A.
  TITLE     ASAP3 is a focal adhesion-associated Arf GAP that functions in cell
            migration and invasion
  JOURNAL   J Biol Chem 283 (22), 14915-14926 (2008)
   PUBMED   18400762
  REMARK    GeneRIF: ASAP3 functions nonredundantly with ASAP1 to control cell
            movement and may have a role in cancer cell invasion.
REFERENCE   9  (residues 1 to 903)
  AUTHORS   Fang,Z., Miao,Y., Ding,X., Deng,H., Liu,S., Wang,F., Zhou,R.,
            Watson,C., Fu,C., Hu,Q., Lillard,J.W. Jr., Powell,M., Chen,Y.,
            Forte,J.G. and Yao,X.
  TITLE     Proteomic identification and functional characterization of a novel
            ARF6 GTPase-activating protein, ACAP4
  JOURNAL   Mol Cell Proteomics 5 (8), 1437-1449 (2006)
   PUBMED   16737952
  REMARK    GeneRIF: ACAP4 is involved in ARF6-mediated cell migration.
            Erratum:[Mol Cell Proteomics. 2006 Sep;5(9):1718]
REFERENCE   10 (residues 1 to 903)
  AUTHORS   Okabe,H., Furukawa,Y., Kato,T., Hasegawa,S., Yamaoka,Y. and
            Nakamura,Y.
  TITLE     Isolation of development and differentiation enhancing factor-like
            1 (DDEFL1) as a drug target for hepatocellular carcinomas
  JOURNAL   Int J Oncol 24 (1), 43-48 (2004)
   PUBMED   14654939
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL021154.1, AB056749.1,
            AL357134.13 and AK000206.1.
            
            On Apr 4, 2002 this sequence version replaced NP_060177.1.
            
            Summary: This gene encodes a member of a subfamily of
            ADP-ribosylation factor(Arf) GTPase-activating proteins that
            contain additional ankyrin repeat and pleckstrin homology domains.
            The Arf GAP domain of this protein catalyzes the hydrolysis of GTP
            bound to Arf proteins. The encoded protein promotes cell
            differentiation and migration and has been implicated in cancer
            cell invasion. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jan 2009].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060786.1, SRR1803614.136563.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336689.8/ ENSP00000338769.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..903
                     /product="arf-GAP with SH3 domain, ANK repeat and PH
                     domain-containing protein 3 isoform a"
                     /note="development and differentiation enhancing
                     factor-like 1; ArfGAP with SH3 domain, ankyrin repeat and
                     PH domain 3 1; centaurin, beta 6; ARF6 GTPase-activating
                     protein; arf-GAP with SH3 domain, ANK repeat and PH
                     domain-containing protein 3; up-regulated in liver cancer
                     1 (UPLC1); protein up-regulated in liver cancer 1"
                     /calculated_mol_wt=99025
     Region          35..243
                     /region_name="BAR_ASAP3"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with
                     SH3 domain, ANK repeat and PH domain containing protein 3;
                     cd07640"
                     /db_xref="CDD:153324"
     Site            order(44,47..48,52,54..55,58..59,61..62,72..73,75..76,
                     79..80,82..83,86,102,105..106,201,204..205,207,209,
                     212..213,215..216,222..223,226..227,229..230,233..234,
                     236..237)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153324"
     Region          294..400
                     /region_name="PH_ASAP"
                     /note="ArfGAP with SH3 domain, ankyrin repeat and PH
                     domain Pleckstrin homology (PH) domain; cd13251"
                     /db_xref="CDD:270071"
     Region          424..546
                     /region_name="ArfGap_ASAP3"
                     /note="ArfGAP domain of ASAP3 (ArfGAP with ANK repeat and
                     PH domain-containing protein 3); cd17900"
                     /db_xref="CDD:350087"
     Site            order(427..428,431,454..456,477,485..489,491..493,
                     495..497,501..502,505..506,538,541..542)
                     /site_type="other"
                     /note="putative ANK repeat binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350087"
     Site            order(441,444,461,464,527)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350087"
     Site            order(441,444,461,464,469)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350087"
     Site            order(466,469..470)
                     /site_type="other"
                     /note="GTP binding site [chemical binding]"
                     /db_xref="CDD:350087"
     Region          551..584
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(552..553,556..558,560..561,565,568,584,586,587,
                     591..592,595..597,602..603,607,610,619,621,623,627..628,
                     631..633,635..636,640,643,652)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          585..617
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY4.1)"
     Region          586..619
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <590..679
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          621..652
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          621..650
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY4.1)"
     Region          720..855
                     /region_name="Metaviral_G"
                     /note="Metaviral_G glycoprotein; pfam09595"
                     /db_xref="CDD:462833"
     Region          740..903
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY4.1)"
     CDS             1..903
                     /gene="ASAP3"
                     /gene_synonym="ACAP4; CENTB6; DDEFL1; UPLC1"
                     /coded_by="NM_017707.4:47..2758"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS235.1"
                     /db_xref="GeneID:55616"
                     /db_xref="HGNC:HGNC:14987"
                     /db_xref="MIM:616594"
ORIGIN      
        1 mpeqfsvaef lavtaedlss pagaaafaak mpryrgaala reeilegdqa ilqrikkavr
       61 aihssglghv eneeqyreav eslgnshlsq nshelstgfl nlavftreva alfknliqnl
      121 nnivsfplds lmkgqlrdgr qdskkqleka wkdyeakmak lekerdrarv tggipgevaq
      181 dmqrerrifq lhmceyllka gesqmkqgpd flqslikffh aqhnffqdgw kaaqslfpfi
      241 eklaasvhal hqaqedelqk ltqlrdslrg tlqlesreeh lsrknsgcgy sihqhqgnkq
      301 fgtekvgfly kksdgirrvw qkrkcgvkyg cltishstin rppvkltllt cqvrpnpeek
      361 kcfdlvthnr tyhfqaedeh eceawvsvlq nskdealssa flgepsagpg swgsaghdge
      421 phdltkllia evksrpgnsq ccdcgaadpt wlstnlgvlt ciqcsgvhre lgvrfsrmqs
      481 ltldllgpse lllalnmgnt sfnevmeaql pshggpkpsa esdmgtrrdy imakyvehrf
      541 arrctpepqr lwtaicnrdl lsvleafang qdfgqplpgp daqapeelvl hlavkvanqa
      601 slplvdfiiq ngghldakaa dgntalhyaa lynqpdclkl llkgralvgt vneagetald
      661 iarkkhhkec eelleqaqag tfafplhvdy swvistepgs dseedeeekr cllklpaqah
      721 wasgrldisn ktyetvaslg aatpqgesed cppplpvkns srtlvqgcar hasgdrsevs
      781 slsseapetp eslgspasss slmsplepgd psqappnsee glreppgtsr psltsgttps
      841 emylpvrfss estrsyrrga rspedgpsar qplprrnvpv gitegdgsrt gslpassvql
      901 lqd
//
LOCUS       NP_001352784             153 aa            linear   PRI 27-APR-2025
DEFINITION  OX-2 membrane glycoprotein isoform c [Homo sapiens].
ACCESSION   NP_001352784 XP_016861948
VERSION     NP_001352784.1
DBSOURCE    REFSEQ: accession NM_001365855.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Wedig,J., Jasani,S., Mukherjee,D., Lathrop,H., Matreja,P., Pfau,T.,
            D'Alesio,L., Guenther,A., Fenn,L., Kaiser,M., Torok,M.A., McGue,J.,
            Sizemore,G.M., Noonan,A.M., Dillhoff,M.E., Blaser,B.W.,
            Frankel,T.L., Culp,S., Hart,P.A., Cruz-Monserrate,Z. and Mace,T.A.
  TITLE     CD200 is overexpressed in the pancreatic tumor microenvironment and
            predictive of overall survival
  JOURNAL   Cancer Immunol Immunother 73 (6), 96 (2024)
   PUBMED   38619621
  REMARK    GeneRIF: CD200 is overexpressed in the pancreatic tumor
            microenvironment and predictive of overall survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Gonzalez-Montes,Y., Osca-Gelis,G., Rodriguez-Romanos,R.,
            Villavicencio,A., Gonzalez-Bartulos,M., Llopis,F., Clapes,V.,
            Oriol,A., Sureda,A., Escoda,L., Sarra,J., Garzo,A., Lloveras,N.,
            Gomez,B., Granada,I. and Gallardo,D.
  TITLE     CD200 genotype is associated with clinical outcome of patients with
            multiple myeloma
  JOURNAL   Front Immunol 15, 1252445 (2024)
   PUBMED   38455039
  REMARK    GeneRIF: CD200 genotype is associated with clinical outcome of
            patients with multiple myeloma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Tang,Y., Liu,W., Kadu,S., Johnson,O., Hasanali,Z.S., Kelly,A.,
            Shestov,A., Pajarillo,R., Greenblatt,E., Holmes,M., Wang,L.P.,
            Shih,N., O'Connor,R.S., Ruella,M., Garfall,A.L., Allman,D.,
            Vogl,D.T., Cohen,A., June,C.H. and Sheppard,N.C.
  TITLE     Exploiting the CD200-CD200R immune checkpoint axis in multiple
            myeloma to enhance CAR T-cell therapy
  JOURNAL   Blood 143 (2), 139-151 (2024)
   PUBMED   37616575
  REMARK    GeneRIF: Exploiting the CD200-CD200R immune checkpoint axis in
            multiple myeloma to enhance CAR T-cell therapy.
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Zhang,M., Qian,X.H., Hu,J., Zhang,Y., Lin,X., Hai,W., Shi,K.,
            Jiang,X., Li,Y., Tang,H.D. and Li,B.
  TITLE     Integrating TSPO PET imaging and transcriptomics to unveil the role
            of neuroinflammation and amyloid-beta deposition in Alzheimer's
            disease
  JOURNAL   Eur J Nucl Med Mol Imaging 51 (2), 455-467 (2024)
   PUBMED   37801139
  REMARK    GeneRIF: Integrating TSPO PET imaging and transcriptomics to unveil
            the role of neuroinflammation and amyloid-beta deposition in
            Alzheimer's disease.
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Moon,S.Y., Han,M., Ryu,G., Shin,S.A., Lee,J.H. and Lee,C.S.
  TITLE     Emerging Immune Checkpoint Molecules on Cancer Cells: CD24 and
            CD200
  JOURNAL   Int J Mol Sci 24 (20), 15072 (2023)
   PUBMED   37894750
  REMARK    GeneRIF: Emerging Immune Checkpoint Molecules on Cancer Cells: CD24
            and CD200.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Chen,Z., Marsden,P.A. and Gorczynski,R.M.
  TITLE     Cloning and characterization of the human CD200 promoter region
  JOURNAL   Mol Immunol 43 (6), 579-587 (2006)
   PUBMED   15955564
  REMARK    GeneRIF: revealed a 169 bp region responsible for constitutive
            expression of CD200; positive regulatory domains were identified in
            the core promoter; and documented evidence for C/EBPbeta as being
            important in transcriptional regulation of CD200
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Preston,S., Wright,G.J., Starr,K., Barclay,A.N. and Brown,M.H.
  TITLE     The leukocyte/neuron cell surface antigen OX2 binds to a ligand on
            macrophages
  JOURNAL   Eur J Immunol 27 (8), 1911-1918 (1997)
   PUBMED   9295026
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Douglas,J., Albertson,D.G., Barclay,A.N., Davis,M. and
            Rabbitts,P.H.
  TITLE     RFLP and mapping of human MOX-1 gene on chromosome 3
  JOURNAL   Nucleic Acids Res 16 (18), 9067 (1988)
   PUBMED   2902568
REFERENCE   9  (residues 1 to 153)
  AUTHORS   McCaughan,G.W., Clark,M.J., Hurst,J., Grosveld,F. and Barclay,A.N.
  TITLE     The gene for MRC OX-2 membrane glycoprotein is localized on human
            chromosome 3
  JOURNAL   Immunogenetics 25 (2), 133-135 (1987)
   PUBMED   3817906
REFERENCE   10 (residues 1 to 153)
  AUTHORS   McCaughan,G.W., Clark,M.J. and Barclay,A.N.
  TITLE     Characterization of the human homolog of the rat MRC OX-2 membrane
            glycoprotein
  JOURNAL   Immunogenetics 25 (5), 329-335 (1987)
   PUBMED   3032785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112487.3.
            
            On Sep 20, 2018 this sequence version replaced XP_016861948.1.
            
            Summary: This gene encodes a type I membrane glycoprotein
            containing two extracellular immunoglobulin domains, a
            transmembrane and a cytoplasmic domain. This gene is expressed by
            various cell types, including B cells, a subset of T cells,
            thymocytes, endothelial cells, and neurons. The encoded protein
            plays an important role in immunosuppression and regulation of
            anti-tumor activity. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.37438.1,
                                           SRR1660805.47985.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.2"
     Protein         1..153
                     /product="OX-2 membrane glycoprotein isoform c"
                     /note="CD200 antigen; antigen identified by monoclonal
                     antibody MRC OX-2; OX-2 membrane glycoprotein"
                     /calculated_mol_wt=16926
     Region          27..104
                     /region_name="ig"
                     /note="Immunoglobulin domain; pfam00047"
                     /db_xref="CDD:395002"
     Region          53..57
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          81..85
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          95..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          110..113
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..153
                     /gene="CD200"
                     /gene_synonym="MOX1; MOX2; MRC; OX-2"
                     /coded_by="NM_001365855.1:461..922"
                     /note="isoform c is encoded by transcript variant 10"
                     /db_xref="GeneID:4345"
                     /db_xref="HGNC:HGNC:7203"
                     /db_xref="MIM:155970"
ORIGIN      
        1 mkgvtcvssi plvlgrsqer paspsmpivs lhykfsedhl nitcsatarp apmvfwkvpr
       61 sgienstvtl shpngttsvt silhikdpkn qvgkevicqv lhlgtvtdfk qtvnkgywfs
      121 vplllsivsl villvlisil lywkrhrnqd rep
//
LOCUS       NP_001337860             234 aa            linear   PRI 27-APR-2025
DEFINITION  sperm-associated microtubule inner protein 5 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001337860 XP_016871242
VERSION     NP_001337860.1
DBSOURCE    REFSEQ: accession NM_001350931.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Leung,M.R., Zeng,J., Wang,X., Roelofs,M.C., Huang,W., Zenezini
            Chiozzi,R., Hevler,J.F., Heck,A.J.R., Dutcher,S.K., Brown,A.,
            Zhang,R. and Zeev-Ben-Mordehai,T.
  TITLE     Structural specializations of the sperm tail
  JOURNAL   Cell 186 (13), 2880-2896 (2023)
   PUBMED   37327785
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB451139.1, BX537582.1, BX117017.1, HY204705.1 and BC021737.2.
            
            On Apr 27, 2017 this sequence version replaced XP_016871242.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.361306.1,
                                           SRR5189667.254483.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000588184.2/ ENSP00000465712.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q25.3"
     Protein         1..234
                     /product="sperm-associated microtubule inner protein 5
                     isoform 2"
                     /note="uncharacterized protein C10orf82; sperm associated
                     microtubule inner protein 5"
                     /calculated_mol_wt=26212
     CDS             1..234
                     /gene="SPMIP5"
                     /gene_synonym="C10orf82"
                     /coded_by="NM_001350931.2:52..756"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS81510.1"
                     /db_xref="GeneID:143379"
                     /db_xref="HGNC:HGNC:28500"
ORIGIN      
        1 mepsktfmrn lpitpgysgf vpflscqgms keddmnhcvk tfqektqryk eqlrelccav
       61 atapklkpvn seetvlqalh qynlqyhpli leckyvkkpl qeppipgwag ylprakvtef
      121 gcgtrytvma kncykdflei terakkahlk pyeeiygvss tktsapspkv lqheellpky
      181 pdfsipdgsc palgrplred pktpltcgca qrpsipcsgk myleplssak yaeg
//
LOCUS       NP_112218                811 aa            linear   PRI 27-APR-2025
DEFINITION  toll-like receptor 10 isoform a precursor [Homo sapiens].
ACCESSION   NP_112218
VERSION     NP_112218.2
DBSOURCE    REFSEQ: accession NM_030956.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Deb,P., Singh,S., Kalyoussef,E., Hess,N.J., Tapping,R.I. and
            Fitzgerald-Bocarsly,P.
  TITLE     TLR10 (CD290) Is a Regulator of Immune Responses in Human
            Plasmacytoid Dendritic Cells
  JOURNAL   J Immunol 213 (5), 577-587 (2024)
   PUBMED   38995177
  REMARK    GeneRIF: TLR10 (CD290) Is a Regulator of Immune Responses in Human
            Plasmacytoid Dendritic Cells.
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Lee,K.M., Baris,D., Zhang,Y., Hosgood,H.D. 3rd, Menashe,I.,
            Yeager,M., Zahm,S.H., Wang,S.S., Purdue,M.P., Chanock,S., Zheng,T.,
            Rothman,N. and Lan,Q.
  TITLE     Common single nucleotide polymorphisms in immunoregulatory genes
            and multiple myeloma risk among women in Connecticut
  JOURNAL   Am J Hematol 85 (8), 560-563 (2010)
   PUBMED   20568250
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Guan,Y., Ranoa,D.R., Jiang,S., Mutha,S.K., Li,X., Baudry,J. and
            Tapping,R.I.
  TITLE     Human TLRs 10 and 1 share common mechanisms of innate immune
            sensing but not signaling
  JOURNAL   J Immunol 184 (9), 5094-5103 (2010)
   PUBMED   20348427
  REMARK    GeneRIF: Analysis of chimeric receptors containing the TLR10
            extracellular recognition domain indicates that human TLR10
            cooperates with TLR2 in sensing of microbes and fungi but possesses
            a signaling function distinct from that of other TLR2 subfamily
            members.
REFERENCE   4  (residues 1 to 811)
  AUTHORS   Georgel,P., Macquin,C. and Bahram,S.
  TITLE     The heterogeneous allelic repertoire of human toll-like receptor
            (TLR) genes
  JOURNAL   PLoS One 4 (11), e7803 (2009)
   PUBMED   19924287
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 811)
  AUTHORS   Nakajima,T., Ohtani,H., Satta,Y., Uno,Y., Akari,H., Ishida,T. and
            Kimura,A.
  TITLE     Natural selection in the TLR-related genes in the course of primate
            evolution
  JOURNAL   Immunogenetics 60 (12), 727-735 (2008)
   PUBMED   18810425
REFERENCE   6  (residues 1 to 811)
  AUTHORS   Nyman,T., Stenmark,P., Flodin,S., Johansson,I., Hammarstrom,M. and
            Nordlund,P.
  TITLE     The crystal structure of the human toll-like receptor 10
            cytoplasmic domain reveals a putative signaling dimer
  JOURNAL   J Biol Chem 283 (18), 11861-11865 (2008)
   PUBMED   18332149
  REMARK    GeneRIF: The TLR10 structure is in good agreement with available
            biochemical data on TLR receptors and is likely to provide a good
            model for the physiological dimer.
REFERENCE   7  (residues 1 to 811)
  AUTHORS   Dasari,P., Nicholson,I.C. and Zola,H.
  TITLE     Toll-like receptors
  JOURNAL   J Biol Regul Homeost Agents 22 (1), 17-26 (2008)
   PUBMED   18394314
  REMARK    Review article
REFERENCE   8  (residues 1 to 811)
  AUTHORS   Lien,E. and Ingalls,R.R.
  TITLE     Toll-like receptors
  JOURNAL   Crit Care Med 30 (1 Suppl), S1-S11 (2002)
   PUBMED   11782555
  REMARK    Review article
REFERENCE   9  (residues 1 to 811)
  AUTHORS   Chuang,T. and Ulevitch,R.J.
  TITLE     Identification of hTLR10: a novel human Toll-like receptor
            preferentially expressed in immune cells
  JOURNAL   Biochim Biophys Acta 1518 (1-2), 157-161 (2001)
   PUBMED   11267672
REFERENCE   10 (residues 1 to 811)
  AUTHORS   Rock,F.L., Hardiman,G., Timans,J.C., Kastelein,R.A. and Bazan,J.F.
  TITLE     A family of human receptors structurally related to Drosophila Toll
  JOURNAL   Proc Natl Acad Sci U S A 95 (2), 588-593 (1998)
   PUBMED   9435236
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA643313.1, DB226380.1,
            AF296673.1, AY358300.1 and AC118137.3.
            
            On Apr 22, 2005 this sequence version replaced NP_112218.1.
            
            Summary: The protein encoded by this gene is a member of the
            Toll-like receptor (TLR) family which plays a fundamental role in
            pathogen recognition and activation of innate immunity. TLRs are
            highly conserved from Drosophila to humans and share structural and
            functional similarities. They recognize pathogen-associated
            molecular patterns (PAMPs) that are expressed on infectious agents,
            and mediate the production of cytokines necessary for the
            development of effective immunity. The various TLRs exhibit
            different patterns of expression. This gene is most highly
            expressed in lymphoid tissues such as spleen, lymph node, thymus,
            and tonsil. Multiple alternatively spliced transcript variants
            which encode different protein isoforms have been found for this
            gene. [provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1-4 encode the same protein (isoform a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1011504.1,
                                           SRR14243140.5243797.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308973.9/ ENSP00000308925.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..811
                     /product="toll-like receptor 10 isoform a precursor"
                     /EC_number="3.2.2.6"
                     /calculated_mol_wt=92352
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2231
     Region          24..46
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          <33..267
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Site            33
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          49..70
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          50..73
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          72..129
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          73..94
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          74..97
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          97..118
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          98..112
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          119..143
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          119..139
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          143..166
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          144..155
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            189
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          296..321
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          325..348
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          <348..>524
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          349..368
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          373..394
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          374..398
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          398..419
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          399..444
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            416
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          422..442
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Site            427
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          444..465
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          445..467
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          467..488
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          468..481
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          489..509
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          491..513
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          522..574
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Site            577..597
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXR5.2)"
     Region          633..775
                     /region_name="TIR"
                     /note="Toll - interleukin 1 - resistance; smart00255"
                     /db_xref="CDD:214587"
     CDS             1..811
                     /gene="TLR10"
                     /gene_synonym="CD290"
                     /coded_by="NM_030956.4:639..3074"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3445.1"
                     /db_xref="GeneID:81793"
                     /db_xref="HGNC:HGNC:15634"
                     /db_xref="MIM:606270"
ORIGIN      
        1 mrlirniyif csivmtaegd apelpeerel mtncsnmslr kvpadltpat ttldlsynll
       61 fqlqssdfhs vsklrvlilc hnriqqldlk tfefnkelry ldlsnnrlks vtwyllaglr
      121 yldlsfndfd tmpiceeagn mshleilgls gakiqksdfq kiahlhlntv flgfrtlphy
      181 eegslpilnt tklhivlpmd tnfwvllrdg iktskilemt nidgksqfvs yemqrnlsle
      241 naktsvllln kvdllwddlf lilqfvwhts vehfqirnvt fggkayldhn sfdysntvmr
      301 tiklehvhfr vfyiqqdkiy llltkmdien ltisnaqmph mlfpnyptkf qylnfannil
      361 tdelfkrtiq lphlktliln gnkletlslv scfanntple hldlsqnllq hkndencswp
      421 etvvnmnlsy nklsdsvfrc lpksiqildl nnnqiqtvpk etihlmalre lniafnfltd
      481 lpgcshfsrl svlniemnfi lspsldfvqs cqevktlnag rnpfrctcel knfiqletys
      541 evmmvgwsds ytceyplnlr gtrlkdvhlh elscntalli vtivvimlvl glavafcclh
      601 fdlpwylrml gqctqtwhrv rkttqeqlkr nvrfhafisy sehdslwvkn elipnleked
      661 gsiliclyes yfdpgksise nivsfieksy ksifvlspnf vqnewchyef yfahhnlfhe
      721 nsdhiilill epipfycipt ryhklkalle kkaylewpkd rrkcglfwan lraainvnvl
      781 atremyelqt ftelneesrg stislmrtdc l
//
LOCUS       NP_064524                245 aa            linear   PRI 27-APR-2025
DEFINITION  dehydrogenase/reductase SDR family member 6 [Homo sapiens].
ACCESSION   NP_064524
VERSION     NP_064524.3
DBSOURCE    REFSEQ: accession NM_020139.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Liu,J.Z., Hu,Y.L., Feng,Y., Jiang,Y., Guo,Y.B., Liu,Y.F., Chen,X.,
            Yang,J.L., Chen,Y.Y., Mao,Q.S. and Xue,W.J.
  TITLE     BDH2 triggers ROS-induced cell death and autophagy by promoting
            Nrf2 ubiquitination in gastric cancer
  JOURNAL   J Exp Clin Cancer Res 39 (1), 123 (2020)
   PUBMED   32605589
  REMARK    GeneRIF: BDH2 triggers ROS-induced cell death and autophagy by
            promoting Nrf2 ubiquitination in gastric cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Yang,W.C., Lin,S.F., Wang,S.C., Tsai,W.C., Wu,C.C. and Wu,S.C.
  TITLE     The Effects of Human BDH2 on the Cell Cycle, Differentiation, and
            Apoptosis and Associations with Leukemia Transformation in
            Myelodysplastic Syndrome
  JOURNAL   Int J Mol Sci 21 (9), 3033 (2020)
   PUBMED   32344823
  REMARK    GeneRIF: The Effects of Human BDH2 on the Cell Cycle,
            Differentiation, and Apoptosis and Associations with Leukemia
            Transformation in Myelodysplastic Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Li,B., Liao,Z., Mo,Y., Zhao,W., Zhou,X., Xiao,X., Cui,W., Feng,G.,
            Zhong,S., Liang,Y., Du,C., Huang,G., Li,P., Xiao,X., Zhou,X.,
            Wang,R. and Zhang,Z.
  TITLE     Inactivation of 3-hydroxybutyrate dehydrogenase type 2 promotes
            proliferation and metastasis of nasopharyngeal carcinoma by iron
            retention
  JOURNAL   Br J Cancer 122 (1), 102-110 (2020)
   PUBMED   31819181
  REMARK    GeneRIF: BDH2 expression is downregulated in nasopharyngeal
            carcinoma. Overexpression of BDH2 in nasopharyngeal carcinoma cells
            decreased the levels of intracellular iron, thereby inhibiting cell
            proliferation. In addition, overexpression of BDH2 reduced invasion
            and migration of nasopharyngeal carcinoma cells by reversing
            epithelial-mesenchymal transition.
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Cui,X.P., Wang,C.X., Wang,Z.Y., Li,J., Tan,Y.W., Gu,S.T. and
            Qin,C.K.
  TITLE     LncRNA TP73-AS1 sponges miR-141-3p to promote the migration and
            invasion of pancreatic cancer cells through the up-regulation of
            BDH2
  JOURNAL   Biosci Rep 39 (3) (2019)
   PUBMED   30643007
  REMARK    GeneRIF: LncRNA TP73 antisense RNA 1T (TP73-AS1) positively
            regulates 3-hydroxybutyrate dehydrogenase type 2 (BDH2) by
            regulating miR-141.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Guo,K., Lukacik,P., Papagrigoriou,E., Meier,M., Lee,W.H.,
            Adamski,J. and Oppermann,U.
  TITLE     Characterization of human DHRS6, an orphan short chain
            dehydrogenase/reductase enzyme: a novel, cytosolic type 2
            R-beta-hydroxybutyrate dehydrogenase
  JOURNAL   J Biol Chem 281 (15), 10291-10297 (2006)
   PUBMED   16380372
  REMARK    GeneRIF: DHRS6 is an orphan short chain dehydrogenase/ reductase
            enzyme
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI544872.1, BC001953.1, BC095414.1, AW136198.1 and AC097485.2.
            
            On Jun 3, 2005 this sequence version replaced NP_064524.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.187435.1,
                                           SRR1803611.224475.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296424.9/ ENSP00000296424.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..245
                     /product="dehydrogenase/reductase SDR family member 6"
                     /EC_number="1.1.1.30"
                     /EC_number="1.1.1.104"
                     /note="oxidoreductase UCPA; short chain
                     dehydrogenase/reductase family 15C member 1;
                     R-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate
                     dehydrogenase, type 2; 4-oxo-L-proline reductase;
                     (R)-beta-hydroxybutyrate dehydrogenase"
                     /calculated_mol_wt=26593
     Region          5..245
                     /region_name="DHRS6_like_SDR_c"
                     /note="human DHRS6-like, classical (c) SDRs; cd05368"
                     /db_xref="CDD:187626"
     Site            order(13,15..18,37..39,57..59,81..83,104,131..132,147,151,
                     177..180,182..184,188)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187626"
     Site            order(62,89..91,93..95,98..99,102,106..107,110,113..114,
                     117..118,121,136,138..140,142..143,145,148..149,152..153,
                     155..157,159..160,162..166,179,207..208,210..212,216,220,
                     223,231..233,235,238..242,245)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187626"
     Site            order(62,89..91,93..95,98..99,102,106..107,110,113..114,
                     117..118,121,136,138,140,142..143,145,148..149,152..153,
                     155..157,159..160,163..165)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187626"
     Site            order(105,133,147,151)
                     /site_type="active"
                     /db_xref="CDD:187626"
     CDS             1..245
                     /gene="BDH2"
                     /gene_synonym="DHRS6; EFA6R; PRO20933; SDR15C1; UCPA-OR;
                     UNQ6308"
                     /coded_by="NM_020139.4:73..810"
                     /db_xref="CCDS:CCDS3663.1"
                     /db_xref="GeneID:56898"
                     /db_xref="HGNC:HGNC:32389"
ORIGIN      
        1 mgrldgkvii ltaaaqgigq aaalafareg akviatdine sklqelekyp giqtrvldvt
       61 kkkqidqfan everldvlfn vagfvhhgtv ldceekdwdf smnlnvrsmy lmikaflpkm
      121 laqksgniin mssvassvkg vvnrcvystt kaavigltks vaadfiqqgi rcncvcpgtv
      181 dtpslqeriq argnpeearn dflkrqktgr fataeeiaml cvylasdesa yvtgnpviid
      241 ggwsl
//
LOCUS       NP_001165696             660 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 540 isoform a [Homo sapiens].
ACCESSION   NP_001165696
VERSION     NP_001165696.1
DBSOURCE    REFSEQ: accession NM_001172225.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Xiang,Z., Yuan,W., Luo,N., Wang,Y., Tan,K., Deng,Y., Zhou,X.,
            Zhu,C., Li,Y., Liu,M., Wu,X. and Li,Y.
  TITLE     A novel human zinc finger protein ZNF540 interacts with MVP and
            inhibits transcriptional activities of the ERK signal pathway
  JOURNAL   Biochem Biophys Res Commun 347 (1), 288-296 (2006)
   PUBMED   16815308
  REMARK    GeneRIF: Taken together, these results suggest that ZNF540 may act
            as a transcriptional repressor in MAPK signaling pathway to mediate
            cellular functions.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC017940.1, AL832315.1 and BE464266.1.
            
            Transcript Variant: This variant (1) encodes isoform a. Both
            variants 1 and 2 encode the same isoform (a), which is longer than
            isoform b.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.269908.1,
                                           SRR1803611.276137.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316433.9/ ENSP00000324598.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..660
                     /product="zinc finger protein 540 isoform a"
                     /note="putative protein product of Nbla10512;
                     CTD-3064H18.6"
                     /calculated_mol_wt=76963
     Region          6..66
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          189..209
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(222,224,226,228..229,232..233,236,250,252,256..257,
                     260..261,264,278,280,282,284..285,288..289,292)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          241..620
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(245,248,261,265)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..321
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          329..349
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(357,360,373,377)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          385..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(390,392,394,396..397,400..401,404,418,420,424..425,
                     428..429,432,446,448,450,452..453,456..457,460)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(413,416,429,433)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          525..545
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          553..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          581..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(586,588,590,592..593,596..597,600,614,616,620..621,
                     624..625,628,642,644,646,648..649,652..653,656)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          609..629
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(609,612,625,629)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          621..646
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          637..657
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..660
                     /gene="ZNF540"
                     /gene_synonym="Nbla10512"
                     /coded_by="NM_001172225.3:293..2275"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:163255"
                     /db_xref="HGNC:HGNC:25331"
                     /db_xref="MIM:613903"
ORIGIN      
        1 mahalvtfrd vaidfsqkew ecldttqrkl yrdvmlenyn nlvslgysgs kpdvitlleq
       61 gkepcvvard vtgrqcpgll srhktkklss ekdiheisls kesiiekskt lrlkgsifrn
      121 ewqnksefeg qqglkersis qkkivskkms tdrkrpsftl nqrihnseks cdshlvqhgk
      181 idsdvkhdck ecgstfnnvy qltlhqkiht geksckcekc gkvfshsyql tlhqrfhtge
      241 kpyecqecgk tftlypqlnr hqkihtgkkp ymckkcdkgf fsrleltqhk rihtgkksye
      301 ckecgkvfql ifyfkeheri htgkkpyeck ecgkafsvcg qltrhqkiht gvkpyeckec
      361 gktfrlsfyl tehrrthagk kpyeckecgk sfnvrgqlnr hktihtgikp fackvcekaf
      421 sysgdlrvhs rihtgekpye ckecgkafml rsvltehqrl htgvkpyeck ecgktfrvrs
      481 qislhkkiht dvkpykcvrc gktfrfgfyl tehqrihtge kpykckecgk afirrgnlke
      541 hlkihsglkp ydckecgksf srrgqftehq kihtgvkpyk ckecgkafsr svdlrihqri
      601 htgekpyeck qcgkafrlns hltehqriht gekpyeckvc rkafrqyshl yqhqkthnvi
//
LOCUS       NP_689416                416 aa            linear   PRI 27-APR-2025
DEFINITION  inositol polyphosphate multikinase [Homo sapiens].
ACCESSION   NP_689416
VERSION     NP_689416.1
DBSOURCE    REFSEQ: accession NM_152230.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Lee,H., Kim,E. and Kim,S.
  TITLE     miRNA-Induced Downregulation of IPMK in Macrophages Mediates
            Lipopolysaccharide-Triggered TLR4 Signaling
  JOURNAL   Biomolecules 13 (2), 332 (2023)
   PUBMED   36830701
  REMARK    GeneRIF: miRNA-Induced Downregulation of IPMK in Macrophages
            Mediates Lipopolysaccharide-Triggered TLR4 Signaling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Dato,S., Crocco,P., De Rango,F., Iannone,F., Maletta,R.,
            Bruni,A.C., Saiardi,A., Rose,G. and Passarino,G.
  TITLE     IP6K3 and IPMK variations in LOAD and longevity: Evidence for a
            multifaceted signaling network at the crossroad between
            neurodegeneration and survival
  JOURNAL   Mech Ageing Dev 195, 111439 (2021)
   PUBMED   33497757
  REMARK    GeneRIF: IP6K3 and IPMK variations in LOAD and longevity: Evidence
            for a multifaceted signaling network at the crossroad between
            neurodegeneration and survival.
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Chen,D., Wang,Z., Zhao,Y.G., Zheng,H., Zhao,H., Liu,N. and Zhang,H.
  TITLE     Inositol Polyphosphate Multikinase Inhibits Liquid-Liquid Phase
            Separation of TFEB to Negatively Regulate Autophagy Activity
  JOURNAL   Dev Cell 55 (5), 588-602 (2020)
   PUBMED   33290695
  REMARK    GeneRIF: Inositol Polyphosphate Multikinase Inhibits Liquid-Liquid
            Phase Separation of TFEB to Negatively Regulate Autophagy Activity.
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Morgan-Lappe,S., Woods,K.W., Li,Q., Anderson,M.G., Schurdak,M.E.,
            Luo,Y., Giranda,V.L., Fesik,S.W. and Leverson,J.D.
  TITLE     RNAi-based screening of the human kinome identifies Akt-cooperating
            kinases: a new approach to designing efficacious multitargeted
            kinase inhibitors
  JOURNAL   Oncogene 25 (9), 1340-1348 (2006)
   PUBMED   16247451
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Chang,S.C. and Majerus,P.W.
  TITLE     Inositol polyphosphate multikinase regulates inositol
            1,4,5,6-tetrakisphosphate
  JOURNAL   Biochem Biophys Res Commun 339 (1), 209-216 (2006)
   PUBMED   16293229
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Mayr,G.W., Windhorst,S. and Hillemeier,K.
  TITLE     Antiproliferative plant and synthetic polyphenolics are specific
            inhibitors of vertebrate inositol-1,4,5-trisphosphate 3-kinases and
            inositol polyphosphate multikinase
  JOURNAL   J Biol Chem 280 (14), 13229-13240 (2005)
   PUBMED   15659385
  REMARK    Erratum:[J Biol Chem. 2007 Nov 30;282(48):35424]
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Nalaskowski,M.M. and Mayr,G.W.
  TITLE     The families of kinases removing the Ca2+ releasing second
            messenger Ins(1,4,5)P3
  JOURNAL   Curr Mol Med 4 (3), 277-290 (2004)
   PUBMED   15101685
  REMARK    Review article
REFERENCE   9  (residues 1 to 416)
  AUTHORS   Chang,S.C., Miller,A.L., Feng,Y., Wente,S.R. and Majerus,P.W.
  TITLE     The human homolog of the rat inositol phosphate multikinase is an
            inositol 1,3,4,6-tetrakisphosphate 5-kinase
  JOURNAL   J Biol Chem 277 (46), 43836-43843 (2002)
   PUBMED   12223481
  REMARK    GeneRIF: the major activity of human InsP(4) 5-kinase is
            phosphorylation at the D-5 position [InsP(4) 5-kinase]
REFERENCE   10 (residues 1 to 416)
  AUTHORS   Nalaskowski,M.M., Deschermeier,C., Fanick,W. and Mayr,G.W.
  TITLE     The human homologue of yeast ArgRIII protein is an inositol
            phosphate multikinase with predominantly nuclear localization
  JOURNAL   Biochem J 366 (Pt 2), 549-556 (2002)
   PUBMED   12027805
  REMARK    GeneRIF: cloning of a full-length 1248-bp cDNA encoding a human
            inositol phosphate multikinase (IPMK); localized predominantly in
            the nucleus when transiently expressed in mammalian cells
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC065709.1 and AC026884.7.
            
            Summary: This gene encodes a member of the inositol phosphokinase
            family. The encoded protein has 3-kinase, 5-kinase and 6-kinase
            activities on phosphorylated inositol substrates. The encoded
            protein plays an important role in the biosynthesis of inositol
            1,3,4,5,6-pentakisphosphate, and has a preferred 5-kinase activity.
            This gene may play a role in nuclear mRNA export. Pseudogenes of
            this gene are located on the long arm of chromosome 13 and the
            short arm of chromosome 19. [provided by RefSeq, Dec 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.200331.1,
                                           SRR1660803.36997.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373935.4/ ENSP00000363046.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.1"
     Protein         1..416
                     /product="inositol polyphosphate multikinase"
                     /EC_number="2.7.1.153"
                     /EC_number="2.7.1.151"
                     /EC_number="2.7.1.140"
                     /note="inositol 1,3,4,6-tetrakisphosphate 5-kinase"
                     /calculated_mol_wt=47091
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFU5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q8NFU5.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q8NFU5.1)"
     Region          127..411
                     /region_name="IPK"
                     /note="Inositol polyphosphate kinase; pfam03770"
                     /db_xref="CDD:397715"
     Region          320..330
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000305|PubMed:12027805"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFU5.1)"
     CDS             1..416
                     /gene="IPMK"
                     /coded_by="NM_152230.5:284..1534"
                     /db_xref="CCDS:CCDS7250.1"
                     /db_xref="GeneID:253430"
                     /db_xref="HGNC:HGNC:20739"
                     /db_xref="MIM:609851"
ORIGIN      
        1 mateppsplr veapgppemr tspaiestpe gtpqpaggrl rflngcvpls hqvaghmygk
       61 dkvgilqhpd gtvlkqlqpp prgprelefy nmvyaadcfd gvllelrkyl pkyygiwspp
      121 tapndlylkl edvthkfnkp cimdvkigqk sydpfassek iqqqvskypl meeigflvlg
      181 mrvyhvhsds yetenqhygr sltketikdg vsrffhngyc lrkdavaasi qkiekilqwf
      241 enqkqlnfya ssllfvyegs sqptttklnd rtlaekflsk gqlsdtevle ynnnfhvlss
      301 tangkiessv gkslskmyar hrkiytkkhh sqtslkvenl eqdngwksms qehlngnvls
      361 qlekvfyhlp tgcqeiaeve vrmidfahvf psntidegyv yglkhlisvl rsildn
//
LOCUS       NP_001357436             225 aa            linear   PRI 27-APR-2025
DEFINITION  phosphoserine phosphatase [Homo sapiens].
ACCESSION   NP_001357436 XP_006715823
VERSION     NP_001357436.1
DBSOURCE    REFSEQ: accession NM_001370507.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Rawat,V., Malvi,P., Della Manna,D., Yang,E.S., Bugide,S., Zhang,X.,
            Gupta,R. and Wajapeyee,N.
  TITLE     PSPH promotes melanoma growth and metastasis by metabolic
            deregulation-mediated transcriptional activation of NR4A1
  JOURNAL   Oncogene 40 (13), 2448-2462 (2021)
   PUBMED   33674745
  REMARK    GeneRIF: PSPH promotes melanoma growth and metastasis by metabolic
            deregulation-mediated transcriptional activation of NR4A1.
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Park,S.M., Seo,E.H., Bae,D.H., Kim,S.S., Kim,J., Lin,W., Kim,K.H.,
            Park,J.B., Kim,Y.S., Yin,J. and Kim,S.Y.
  TITLE     Phosphoserine Phosphatase Promotes Lung Cancer Progression through
            the Dephosphorylation of IRS-1 and a Noncanonical
            L-Serine-Independent Pathway
  JOURNAL   Mol Cells 42 (8), 604-616 (2019)
   PUBMED   31446747
  REMARK    GeneRIF: a specific interaction between PSPH and IRS1 and the
            dephosphorylation of phospho-IRS-1 by PSPH in lung cancer cells,
            was identified.
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Haufroid,M., Mirgaux,M., Leherte,L. and Wouters,J.
  TITLE     Crystal structures and snapshots along the reaction pathway of
            human phosphoserine phosphatase
  JOURNAL   Acta Crystallogr D Struct Biol 75 (Pt 6), 592-604 (2019)
   PUBMED   31205021
  REMARK    GeneRIF: three new high-resolution crystal structures of hPSP
            (1.5-2.0 A) in complexes with phosphoserine and with serine, which
            are the substrate and the product of the reaction, respectively,
            and in complex with a noncleavable substrate analogue (homocysteic
            acid) are presented.
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Liao,L., Ge,M., Zhan,Q., Huang,R., Ji,X., Liang,X. and Zhou,X.
  TITLE     PSPH Mediates the Metastasis and Proliferation of Non-small Cell
            Lung Cancer through MAPK Signaling Pathways
  JOURNAL   Int J Biol Sci 15 (1), 183-194 (2019)
   PUBMED   30662358
  REMARK    GeneRIF: The results suggest that PSPH may act as a putative
            oncogene and a potential therapeutic target in NSCLC.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 225)
  AUTHORS   van der Crabben,S.N. and de Koning,T.J.
  TITLE     Serine Deficiency Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37347880
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Veeranna and Shetty,K.T.
  TITLE     Phosphoserine phosphatase of human brain: partial purification,
            characterization, regional distribution, and effect of certain
            modulators including psychoactive drugs
  JOURNAL   Neurochem Res 15 (12), 1203-1210 (1990)
   PUBMED   1965857
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Minelli,A., Piantanida,M., Maserati,E., Campagnoli,E., Pasquali,F.
            and Danesino,C.
  TITLE     Gene dosage effect in acquired monosomy 7: distinct behaviour of
            beta-glucuronidase and phosphoserine phosphatase
  JOURNAL   Genes Chromosomes Cancer 1 (3), 216-220 (1990)
   PUBMED   1964582
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Novelli,G. and Dallapiccola,B.
  TITLE     Gene dosage studies regionally assign the phosphoserine phosphatase
            gene to 7p15.1 or 2
  JOURNAL   Ann Genet 31 (3), 195-196 (1988)
   PUBMED   2851960
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Moro-Furlani,A.M., Turner,V.S. and Hopkinson,D.A.
  TITLE     Genetical and biochemical studies on human phosphoserine
            phosphatase
  JOURNAL   Ann Hum Genet 43 (4), 323-333 (1980)
   PUBMED   6249179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092579.3.
            
            On May 9, 2019 this sequence version replaced XP_006715823.1.
            
            Summary: The protein encoded by this gene belongs to a subfamily of
            the phosphotransferases. This encoded enzyme is responsible for the
            third and last step in L-serine formation. It catalyzes
            magnesium-dependent hydrolysis of L-phosphoserine and is also
            involved in an exchange reaction between L-serine and
            L-phosphoserine. Deficiency of this protein is thought to be linked
            to Williams syndrome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.130190.1,
                                           SRR1803614.122536.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p11.2"
     Protein         1..225
                     /product="phosphoserine phosphatase"
                     /EC_number="3.1.3.3"
                     /note="L-3-phosphoserine phosphatase; O-phosphoserine
                     phosphohydrolase; PSPase"
                     /calculated_mol_wt=24877
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P78330.2)"
     Region          15..216
                     /region_name="HAD_PSP_eu"
                     /note="phosphoserine phosphatase eukaryotic-like, similar
                     to human phosphoserine phosphatase; cd04309"
                     /db_xref="CDD:319801"
     Site            order(20..24,29,109..110,158,178..179,182..183)
                     /site_type="active"
                     /db_xref="CDD:319801"
     CDS             1..225
                     /gene="PSPH"
                     /gene_synonym="PSP; PSPHD"
                     /coded_by="NM_001370507.1:761..1438"
                     /db_xref="CCDS:CCDS5522.1"
                     /db_xref="GeneID:5723"
                     /db_xref="HGNC:HGNC:9577"
                     /db_xref="MIM:172480"
ORIGIN      
        1 mvshselrkl fysadavcfd vdstvireeg idelakicgv edavsemtrr amggavpfka
       61 alterlaliq psreqvqrli aeqpphltpg irelvsrlqe rnvqvflisg gfrsivehva
      121 sklnipatnv fanrlkfyfn geyagfdetq ptaesggkgk vikllkekfh fkkiimigdg
      181 atdmeacppa dafigfggnv irqqvkdnak wyitdfvell gelee
//
LOCUS       NP_004392                331 aa            linear   PRI 27-APR-2025
DEFINITION  DNA fragmentation factor subunit alpha isoform 1 [Homo sapiens].
ACCESSION   NP_004392
VERSION     NP_004392.1
DBSOURCE    REFSEQ: accession NM_004401.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Banas,T., Pitynski,K., Mikos,M. and Cielecka-Kuszyk,J.
  TITLE     Endometrial Polyps and Benign Endometrial Hyperplasia Have
            Increased Prevalence of DNA Fragmentation Factors 40 and 45 (DFF40
            and DFF45) Together With the Antiapoptotic B-Cell Lymphoma (Bcl-2)
            Protein Compared With Normal Human Endometria
  JOURNAL   Int J Gynecol Pathol 37 (5), 431-440 (2018)
   PUBMED   28914671
  REMARK    GeneRIF: Glandular, menopause-independent DFF40, DFF45, and Bcl-2
            overexpression may play an important role in the pathogenesis of
            endometrial polyps and benign endometrial hyperplasia
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Fawzy,M.S., Toraih,E.A., Ibrahiem,A., Abdeldayem,H., Mohamed,A.O.
            and Abdel-Daim,M.M.
  TITLE     Evaluation of miRNA-196a2 and apoptosis-related target genes:
            ANXA1, DFFA and PDCD4 expression in gastrointestinal cancer
            patients: A pilot study
  JOURNAL   PLoS One 12 (11), e0187310 (2017)
   PUBMED   29091952
  REMARK    GeneRIF: evaluate the relative expression levels of miR-196a2 and
            three of its selected apoptosis-related targets; ANXA1, DFFA and
            PDCD4 in a sample of GI cancer patients
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Morgan,C.W., Diaz,J.E., Zeitlin,S.G., Gray,D.C. and Wells,J.A.
  TITLE     Engineered cellular gene-replacement platform for selective and
            inducible proteolytic profiling
  JOURNAL   Proc Natl Acad Sci U S A 112 (27), 8344-8349 (2015)
   PUBMED   26106156
  REMARK    GeneRIF: Data show that the caspase-activated DNase (CAD) is
            activated when caspases cleave its endogenous inhibitor ICAD,
            resulting in the characteristic DNA laddering of apoptosis.
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Liu,X., Zou,H., Widlak,P., Garrard,W. and Wang,X.
  TITLE     Activation of the apoptotic endonuclease DFF40 (caspase-activated
            DNase or nuclease). Oligomerization and direct interaction with
            histone H1
  JOURNAL   J Biol Chem 274 (20), 13836-13840 (1999)
   PUBMED   10318789
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Inohara,N., Koseki,T., Chen,S., Wu,X. and Nunez,G.
  TITLE     CIDE, a novel family of cell death activators with homology to the
            45 kDa subunit of the DNA fragmentation factor
  JOURNAL   EMBO J 17 (9), 2526-2533 (1998)
   PUBMED   9564035
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Enari,M., Sakahira,H., Yokoyama,H., Okawa,K., Iwamatsu,A. and
            Nagata,S.
  TITLE     A caspase-activated DNase that degrades DNA during apoptosis, and
            its inhibitor ICAD
  JOURNAL   Nature 391 (6662), 43-50 (1998)
   PUBMED   9422506
  REMARK    Erratum:[Nature 1998 May 28;393(6683):396]
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Liu,X., Zou,H., Slaughter,C. and Wang,X.
  TITLE     DFF, a heterodimeric protein that functions downstream of caspase-3
            to trigger DNA fragmentation during apoptosis
  JOURNAL   Cell 89 (2), 175-184 (1997)
   PUBMED   9108473
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Leek,J.P., Carr,I.M., Bell,S.M., Markham,A.F. and Lench,N.J.
  TITLE     Assignment of the DNA fragmentation factor gene (DFFA) to human
            chromosome bands 1p36.3-->p36.2 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 212-213 (1997)
   PUBMED   9605855
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU121791.1, BC007112.1,
            BC000037.2, BC007721.2 and AL354956.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Apoptosis is a cell death process that removes toxic
            and/or useless cells during mammalian development. The apoptotic
            process is accompanied by shrinkage and fragmentation of the cells
            and nuclei and degradation of the chromosomal DNA into nucleosomal
            units. DNA fragmentation factor (DFF) is a heterodimeric protein of
            40-kD (DFFB) and 45-kD (DFFA) subunits. DFFA is the substrate for
            caspase-3 and triggers DNA fragmentation during apoptosis. DFF
            becomes activated when DFFA is cleaved by caspase-3. The cleaved
            fragments of DFFA dissociate from DFFB, the active component of
            DFF. DFFB has been found to trigger both DNA fragmentation and
            chromatin condensation during apoptosis. Two alternatively spliced
            transcript variants encoding distinct isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript but encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.376436.1, BC007721.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377038.8/ ENSP00000366237.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..331
                     /product="DNA fragmentation factor subunit alpha isoform
                     1"
                     /note="DFF45; inhibitor of CAD; DNA fragmentation factor
                     45 kDa subunit; DNA fragmentation factor, 45kDa, alpha
                     polypeptide"
                     /calculated_mol_wt=36391
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O00273.1)"
     Region          18..96
                     /region_name="CIDE_N"
                     /note="CIDE_N domain, found at the N-terminus of the CIDE
                     (cell death-inducing DFF45-like effector) proteins, as
                     well as CAD nuclease (caspase-activated DNase/DNA
                     fragmentation factor, DFF40) and its inhibitor,
                     ICAD(DFF45). These proteins are associated with...;
                     cl02541"
                     /db_xref="CDD:470607"
     Site            order(22,31..32,34..35,45,49,66,68..69,74..75,94,96)
                     /site_type="other"
                     /note="putative heterodimer interaction sites [polypeptide
                     binding]"
                     /db_xref="CDD:119367"
     Region          100..264
                     /region_name="DFF-C"
                     /note="DNA Fragmentation factor 45kDa, C terminal domain;
                     pfam09033"
                     /db_xref="CDD:462661"
     Site            117..118
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3; propagated from
                     UniProtKB/Swiss-Prot (O00273.1)"
     Site            224..225
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3; propagated from
                     UniProtKB/Swiss-Prot (O00273.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00273.1)"
     Region          305..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00273.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00273.1)"
     CDS             1..331
                     /gene="DFFA"
                     /gene_synonym="DFF-45; DFF1; ICAD"
                     /coded_by="NM_004401.3:72..1067"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS118.1"
                     /db_xref="GeneID:1676"
                     /db_xref="HGNC:HGNC:2772"
                     /db_xref="MIM:601882"
ORIGIN      
        1 mevtgdagvp esgeirtlkp cllrrnysre qhgvaascle dlrskacdil aidksltpvt
       61 lvlaedgtiv ddddyflclp sntkfvalas nekwaynnsd ggtawisqes fdvdetdsga
      121 glkwknvarq lkedlssiil lseedlqmlv dapcsdlaqe lrqscatvqr lqhtlqqvld
      181 qreevrqskq llqlylqale kegsllskqe eskaafgeev davdtgisre tssdvalash
      241 iltalrekqa pelslssqdl elvtkedpka lavalnwdik ktetvqeace relalrlqqt
      301 qslhslrsis askasppgdl qnpkrarqdp t
//
LOCUS       NP_001350151             791 aa            linear   ROD 27-APR-2025
DEFINITION  protein SFI1 homolog isoform 2 [Mus musculus].
ACCESSION   NP_001350151 XP_017170332
VERSION     NP_001350151.1
DBSOURCE    REFSEQ: accession NM_001363222.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Alvarez-Dominguez,J.R., Zhang,X. and Hu,W.
  TITLE     Widespread and dynamic translational control of red blood cell
            development
  JOURNAL   Blood 129 (5), 619-629 (2017)
   PUBMED   27899360
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Pezer,Z., Harr,B., Teschke,M., Babiker,H. and Tautz,D.
  TITLE     Divergence patterns of genic copy number variation in natural
            populations of the house mouse (Mus musculus domesticus) reveal
            three conserved genes with major population-specific expansions
  JOURNAL   Genome Res 25 (8), 1114-1124 (2015)
   PUBMED   26149421
  REMARK    GeneRIF: Study showed major differences in gene copy number in
            natural populations. CWC22, SFI1, and HJURP are highly conserved
            genes with the most copy-number variation. They all exhibit
            population-specific expansion patterns, perhaps for local
            adaptations.
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Alvarez-Dominguez,J.R., Hu,W., Yuan,B., Shi,J., Park,S.S.,
            Gromatzky,A.A., van Oudenaarden,A. and Lodish,H.F.
  TITLE     Global discovery of erythroid long noncoding RNAs reveals novel
            regulators of red cell maturation
  JOURNAL   Blood 123 (4), 570-581 (2014)
   PUBMED   24200680
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Harrow,J.L., Steward,C.A., Frankish,A., Gilbert,J.G.,
            Gonzalez,J.M., Loveland,J.E., Mudge,J., Sheppard,D., Thomas,M.,
            Trevanion,S. and Wilming,L.G.
  TITLE     The Vertebrate Genome Annotation browser 10 years on
  JOURNAL   Nucleic Acids Res 42 (Database issue), D771-D779 (2014)
   PUBMED   24316575
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Park,C.S., Rehrauer,H. and Mansuy,I.M.
  TITLE     Genome-wide analysis of H4K5 acetylation associated with fear
            memory in mice
  JOURNAL   BMC Genomics 14, 539 (2013)
   PUBMED   23927422
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 791)
  AUTHORS   Gendrel,A.V., Tang,Y.A., Suzuki,M., Godwin,J., Nesterova,T.B.,
            Greally,J.M., Heard,E. and Brockdorff,N.
  TITLE     Epigenetic functions of smchd1 repress gene clusters on the
            inactive X chromosome and on autosomes
  JOURNAL   Mol Cell Biol 33 (16), 3150-3165 (2013)
   PUBMED   23754746
REFERENCE   7  (residues 1 to 791)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL671968.17 and BX572640.9.
            
            On May 12, 2018 this sequence version replaced XP_017170332.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660813.80695.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 2.19 cM"
     Protein         1..791
                     /product="protein SFI1 homolog isoform 2"
                     /note="protein SFI1 homolog"
                     /calculated_mol_wt=91377
     Region          <93..369
                     /region_name="Sfi1"
                     /note="Sfi1 spindle body protein; pfam08457"
                     /db_xref="CDD:430007"
     CDS             1..791
                     /gene="Sfi1"
                     /coded_by="NM_001363222.1:2233..4608"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:78887"
                     /db_xref="MGI:MGI:1926137"
ORIGIN      
        1 maewvtvlhk cvrvwlryvh krqwqqllra radghfqqra lpaafytwyr gwlwhqqrri
       61 lhtkavrfhr gtlekqvfal wrqkmsqhre nclaermail qaeqqllrrf wfvwhqqaav
      121 cqlerqqqam aiahhhsgll rrafciwkes tqgfriermg raqaahfhsa qllsrawsmw
      181 revyqnrvrs vlrevaarer qhnrqllwwa lhlwrentma rldgakktsq arvhysrtlc
      241 skvlvqwrev tsvqiyyrqk eaaalreark aldrgrlqnw fqhwrfcsqr aaqqrfqlgq
      301 aaqhhhwqll meamarwkah hlgcirkkfl qrqaaqllaq rlsracfcqw rkqlavrkqe
      361 qwgtaralwl wafslqakvw tawlgfvler rrkkarlera mqayqqqllq egatrllrft
      421 agtkafrqql qaqqqvqaah slhcavrhca elwkkkvlgp gktsqppapt tfskrvtfkd
      481 sflsghaaea gdatqetkkl rappsqgvlg slagaagepc hldlnaarss rkqprrpsfl
      541 lerlgsqrsp ewyslgeqql ekppeeesta llggssltrp flpgvlpnvp gpklpptasp
      601 glellppssi mphaaggtar vsakpsipgp qpwgcpslpr dldpqllpgd sistrtepvy
      661 gseatghtel eaelegiqqq lqhyqttkqn lwscqrqans lrrwlelsqe epksedlhle
      721 eqvkteleev rpgqpraspw lsflsaclvp psrpcpqvel qvqqlakele aqrqpvgtci
      781 arvralrral c
//
LOCUS       NP_001348304             133 aa            linear   ROD 27-APR-2025
DEFINITION  adipose-secreted signaling protein isoform 3 [Mus musculus].
ACCESSION   NP_001348304
VERSION     NP_001348304.1
DBSOURCE    REFSEQ: accession NM_001361375.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Chen,Q., Huang,L., Pan,D., Hu,K., Li,R., Friedline,R.H., Kim,J.K.,
            Zhu,L.J., Guertin,D.A. and Wang,Y.X.
  TITLE     A brown fat-enriched adipokine Adissp controls adipose
            thermogenesis and glucose homeostasis
  JOURNAL   Nat Commun 13 (1), 7633 (2022)
   PUBMED   36496438
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY706619.1, CX222938.1, AK006622.1 and AL831736.16.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CX222938.1, SRR7345562.942298.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849376
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 63.28 cM"
     Protein         1..133
                     /product="adipose-secreted signaling protein isoform 3"
                     /note="UPF0687 protein C20orf27 homolog"
                     /calculated_mol_wt=14891
     Region          1..132
                     /region_name="DUF4517"
                     /note="Domain of unknown function (DUF4517); pfam15006"
                     /db_xref="CDD:464438"
     CDS             1..133
                     /gene="Adissp"
                     /gene_synonym="1700037H04Rik"
                     /coded_by="NM_001361375.1:347..748"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:67326"
                     /db_xref="MGI:MGI:1914576"
ORIGIN      
        1 mvtqesdnsf lvkvgflkil hryeitftlp pvrrlskdir etpvhslhlk llsvtptseg
       61 ysikceysah kegvlkeeml lacegdigtc vrvtvqarvm drhhgtpmll dgvkcvgael
      121 eydseqsdwl gfd
//
LOCUS       NP_003428                540 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 136 isoform 1 [Homo sapiens].
ACCESSION   NP_003428 XP_942071
VERSION     NP_003428.1
DBSOURCE    REFSEQ: accession NM_003437.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 540)
  AUTHORS   Liu,C. and Chen,X.
  TITLE     A potential cellular host factor homologous to ZNF-136 can interact
            with truncated nonstructural protein 2 of hepatitis C virus
  JOURNAL   Arch Virol 159 (4), 785-789 (2014)
   PUBMED   24136724
  REMARK    GeneRIF: Through peptide mass fingerprinting, the hepatitis C virus
            NS2-interacting protein was found to be homologous to a repressor
            of transcription, ZNF136.
REFERENCE   6  (residues 1 to 540)
  AUTHORS   Vissing,H., Meyer,W.K., Aagaard,L., Tommerup,N. and Thiesen,H.J.
  TITLE     Repression of transcriptional activity by heterologous KRAB domains
            present in zinc finger proteins
  JOURNAL   FEBS Lett 369 (2-3), 153-157 (1995)
   PUBMED   7649249
REFERENCE   7  (residues 1 to 540)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
REFERENCE   8  (residues 1 to 540)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL537987.3, BC006421.1,
            DB369850.1, BQ574220.1, CN429121.1 and BP420506.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_942071.1.
            
            Summary: This gene encodes a zinc finger protein containing a
            Kruppel-associated box (KRAB) A-box domain at its N-terminus,
            followed by fourteen contiguous C2H2 zinc finger domains and a
            degenerate zinc finger. The KRAB A-box showed weak transcriptional
            repressor activity in a reporter gene assay. Alternative splicing
            results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Dec 2016].
            
            Transcript Variant: This variant (1) encodes the longer/longest*
            isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BJ991067.1, SRR1660805.43816.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000343979.6/ ENSP00000344162.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..540
                     /product="zinc finger protein 136 isoform 1"
                     /calculated_mol_wt=62653
     Region          3..44
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          143..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          157..526
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52737.1)"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(259,261,263,265..266,269..270,273,287,289,293..294,
                     297..298,301,315,317,319,321..322,325..326,329)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          422..442
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(427,429,431,433..434,437..438,441,455,457,461..462,
                     465..466,469,483,485,487,489..490,493..494,497)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          450..470
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          478..498
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          506..526
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..540
                     /gene="ZNF136"
                     /gene_synonym="pHZ-20"
                     /coded_by="NM_003437.5:109..1731"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32916.1"
                     /db_xref="GeneID:7695"
                     /db_xref="HGNC:HGNC:12920"
                     /db_xref="MIM:604078"
ORIGIN      
        1 mdsvafedvd vnftqeewal ldpsqknlyr dvmwetmrnl asigkkwkdq nikdhykhrg
       61 rnlrshmler lyqtkdgsqr ggifsqfanq nlskkipgvk lcesivygev smgqsslnrh
      121 ikdhsghepk eyqeygekpd trnqcwkpfs shhsfrthei ihtgeklydc kecgktffsl
      181 krirrhiith sgytpykckv cgkafdypsr frthershtg ekpyecqecg kaftcitsvr
      241 rhmikhtgdg pykckvcgkp fhslssfqvh erihtgekpf kckqcgkafs csptlriher
      301 thtgekpyec kqcgkafsyl pslrlherih tgekpfvckq cgkafrsast fqiherthtg
      361 ekpyeckecg eafscipsmr rhmikhtgeg pykckvcgkp fhslspfrih erthtgekpy
      421 vckhcgkafv sstsiriher thtgekpyec kqcgkafsyl nsfrthemih tgekpfeckr
      481 cgkafrssss frlherthtg qkpyhckecg kayscrasfq rhmlthaedg ppykcmwesl
//
LOCUS       NP_001352272             254 aa            linear   PRI 27-APR-2025
DEFINITION  trafficking protein particle complex subunit 13 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001352272 XP_016865379
VERSION     NP_001352272.1
DBSOURCE    REFSEQ: accession NM_001365343.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Gupta,R., Somyajit,K., Narita,T., Maskey,E., Stanlie,A., Kremer,M.,
            Typas,D., Lammers,M., Mailand,N., Nussenzweig,A., Lukas,J. and
            Choudhary,C.
  TITLE     DNA Repair Network Analysis Reveals Shieldin as a Key Regulator of
            NHEJ and PARP Inhibitor Sensitivity
  JOURNAL   Cell 173 (4), 972-988 (2018)
   PUBMED   29656893
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Ramirez-Peinado,S., Ignashkova,T.I., van Raam,B.J., Baumann,J.,
            Sennott,E.L., Gendarme,M., Lindemann,R.K., Starnbach,M.N. and
            Reiling,J.H.
  TITLE     TRAPPC13 modulates autophagy and the response to Golgi stress
  JOURNAL   J Cell Sci 130 (14), 2251-2265 (2017)
   PUBMED   28536105
  REMARK    GeneRIF: Results lend support for the existence of a mammalian
            TRAPPIII complex containing TRAPPC13, which is important for
            autophagic flux under certain stress conditions.
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Kim,J.J., Lipatova,Z. and Segev,N.
  TITLE     TRAPP Complexes in Secretion and Autophagy
  JOURNAL   Front Cell Dev Biol 4, 20 (2016)
   PUBMED   27066478
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Bassik,M.C., Kampmann,M., Lebbink,R.J., Wang,S., Hein,M.Y.,
            Poser,I., Weibezahn,J., Horlbeck,M.A., Chen,S., Mann,M.,
            Hyman,A.A., Leproust,E.M., McManus,M.T. and Weissman,J.S.
  TITLE     A systematic mammalian genetic interaction map reveals pathways
            underlying ricin susceptibility
  JOURNAL   Cell 152 (4), 909-922 (2013)
   PUBMED   23394947
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Choi,C., Davey,M., Schluter,C., Pandher,P., Fang,Y., Foster,L.J.
            and Conibear,E.
  TITLE     Organization and assembly of the TRAPPII complex
  JOURNAL   Traffic 12 (6), 715-725 (2011)
   PUBMED   21453443
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008560.6 and DA236226.1.
            
            On Aug 18, 2018 this sequence version replaced XP_016865379.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.17056.1,
                                           SRR1803616.17103.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..254
                     /product="trafficking protein particle complex subunit 13
                     isoform 7"
                     /note="UPF0533 protein C5orf44; Trs65-related;
                     REV7-interacting novel NHEJ regulator 1; trafficking
                     protein particle complex 13"
                     /calculated_mol_wt=28514
     Region          <1..135
                     /region_name="DUF974"
                     /note="Protein of unknown function (DUF974); pfam06159"
                     /db_xref="CDD:461841"
     CDS             1..254
                     /gene="TRAPPC13"
                     /gene_synonym="C5orf44; SHLD3"
                     /coded_by="NM_001365343.1:421..1185"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:80006"
                     /db_xref="HGNC:HGNC:25828"
ORIGIN      
        1 myfrkffkfq vlkpldvktk fynaetdevf leaqiqnmtt spmfmekvsl epsimynvte
       61 lnsvsqagec vstfgsrayl qpmdtrqyly clkpknefae kagiikgvtv igkldivwkt
      121 nlgergrlqt sqlqrmapgy gdvrlsleai pdtvnleepf hitckitncs ertmdlvlem
      181 cntnsihwcg isgrqlgklh pssslclalt llssvqglqs isglrltdtf lkrtyeyddi
      241 aqvcvvssai kves
//
LOCUS       NP_829884               1116 aa            linear   PRI 27-APR-2025
DEFINITION  ELKS/Rab6-interacting/CAST family member 1 isoform epsilon [Homo
            sapiens].
ACCESSION   NP_829884
VERSION     NP_829884.1
DBSOURCE    REFSEQ: accession NM_178040.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Ribolla,L.M., Sala,K., Tonoli,D., Ramella,M., Bracaglia,L.,
            Bonomo,I., Gonnelli,L., Lamarca,A., Brindisi,M., Pierattelli,R.,
            Provenzani,A. and de Curtis,I.
  TITLE     Interfering with the ERC1-LL5beta interaction disrupts plasma
            membrane-Associated platforms and affects tumor cell motility
  JOURNAL   PLoS One 18 (7), e0287670 (2023)
   PUBMED   37437062
  REMARK    GeneRIF: Interfering with the ERC1-LL5beta interaction disrupts
            plasma membrane-Associated platforms and affects tumor cell
            motility.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Liang,M., Jin,G., Xie,X., Zhang,W., Li,K., Niu,F., Yu,C. and Wei,Z.
  TITLE     Oligomerized liprin-alpha promotes phase separation of ELKS for
            compartmentalization of presynaptic active zone proteins
  JOURNAL   Cell Rep 34 (12), 108901 (2021)
   PUBMED   33761347
  REMARK    GeneRIF: Oligomerized liprin-alpha promotes phase separation of
            ELKS for compartmentalization of presynaptic active zone proteins.
            Erratum:[Cell Rep. 2021 Jul 27;36(4):109476. doi:
            10.1016/j.celrep.2021.109476. PMID: 34320361]
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Cong,S., Yao,X., Huang,Z., Risacher,S.L., Nho,K., Saykin,A.J. and
            Shen,L.
  CONSRTM   UK Brain Expression Consortium; Alzheimer's Disease Neuroimaging
            Initiative
  TITLE     Volumetric GWAS of medial temporal lobe structures identifies an
            ERC1 locus using ADNI high-resolution T2-weighted MRI data
  JOURNAL   Neurobiol Aging 95, 81-93 (2020)
   PUBMED   32768867
  REMARK    GeneRIF: Volumetric GWAS of medial temporal lobe structures
            identifies an ERC1 locus using ADNI high-resolution T2-weighted MRI
            data.
REFERENCE   4  (residues 1 to 1116)
  AUTHORS   Ohara-Imaizumi,M., Aoyagi,K. and Ohtsuka,T.
  TITLE     Role of the active zone protein, ELKS, in insulin secretion from
            pancreatic beta-cells
  JOURNAL   Mol Metab 27S (Suppl), S81-S91 (2019)
   PUBMED   31500835
  REMARK    GeneRIF: The ELKS forms a potent insulin secretion complex with
            L-type voltage-dependent Ca(2+) channels on the vascular-facing
            plasma membrane of beta-cells, enabling polarized Ca(2+) influx and
            first-phase insulin secretion from islets.
            Review article
REFERENCE   5  (residues 1 to 1116)
  AUTHORS   Ko,J., Na,M., Kim,S., Lee,J.R. and Kim,E.
  TITLE     Interaction of the ERC family of RIM-binding proteins with the
            liprin-alpha family of multidomain proteins
  JOURNAL   J Biol Chem 278 (43), 42377-42385 (2003)
   PUBMED   12923177
  REMARK    GeneRIF: In vitro results indicate that ERC2/CAST, an active
            zone-specific isoform, interacts with all of the known isoforms of
            liprin-alpha and that liprin-alpha1 associates with both ERC2 and
            ERC1b
REFERENCE   6  (residues 1 to 1116)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 1116)
  AUTHORS   Nakata,T., Yokota,T., Emi,M. and Minami,S.
  TITLE     Differential expression of multiple isoforms of the ELKS mRNAs
            involved in a papillary thyroid carcinoma
  JOURNAL   Genes Chromosomes Cancer 35 (1), 30-37 (2002)
   PUBMED   12203787
  REMARK    GeneRIF: Analysis of the gene structure of four isoforms (ELKS
            beta, ELKS gamma, ELKS delta, and ELKS epsilon) in a case of
            papillary thyroid carcinoma reveal that the isoforms are produced
            by alternative splicing.
REFERENCE   8  (residues 1 to 1116)
  AUTHORS   Monier,S., Jollivet,F., Janoueix-Lerosey,I., Johannes,L. and
            Goud,B.
  TITLE     Characterization of novel Rab6-interacting proteins involved in
            endosome-to-TGN transport
  JOURNAL   Traffic 3 (4), 289-297 (2002)
   PUBMED   11929610
REFERENCE   9  (residues 1 to 1116)
  AUTHORS   Yokota,T., Nakata,T., Minami,S., Inazawa,J. and Emi,M.
  TITLE     Genomic organization and chromosomal mapping of ELKS, a gene
            rearranged in a papillary thyroid carcinoma
  JOURNAL   J Hum Genet 45 (1), 6-11 (2000)
   PUBMED   10697956
REFERENCE   10 (residues 1 to 1116)
  AUTHORS   Nakata,T., Kitamura,Y., Shimizu,K., Tanaka,S., Fujimori,M.,
            Yokoyama,S., Ito,K. and Emi,M.
  TITLE     Fusion of a novel gene, ELKS, to RET due to translocation
            t(10;12)(q11;p13) in a papillary thyroid carcinoma
  JOURNAL   Genes Chromosomes Cancer 25 (2), 97-103 (1999)
   PUBMED   10337992
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR000847.1, AC004803.11,
            AB053471.1, AC004672.1, AC004671.1 and BM984956.1.
            
            Summary: The protein encoded by this gene is a member of a family
            of RIM-binding proteins. RIMs are active zone proteins that
            regulate neurotransmitter release. This gene has been found fused
            to the receptor-type tyrosine kinase gene RET by gene rearrangement
            due to the translocation t(10;12)(q11;p13) in thyroid papillary
            carcinoma. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (epsilon) encodes the longest
            isoform (epsilon).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB053471.1, BC132784.1 [ECO:0000331]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360905.9/ ENSP00000354158.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..1116
                     /product="ELKS/Rab6-interacting/CAST family member 1
                     isoform epsilon"
                     /note="RAB6 interacting protein 2"
                     /calculated_mol_wt=127956
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            10
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MI1; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MI1; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Region          154..982
                     /region_name="Cast"
                     /note="RIM-binding protein of the cytomatrix active zone;
                     pfam10174"
                     /db_xref="CDD:431111"
     Region          590..609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            719..720
                     /site_type="other"
                     /note="Breakpoint for translocation to form ERC1-RET
                     oncogene; propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Region          814..836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            1005
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q811U3; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            1046
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Region          1068..1108
                     /region_name="RBD-FIP"
                     /note="FIP domain; pfam09457"
                     /db_xref="CDD:462805"
     CDS             1..1116
                     /gene="ERC1"
                     /gene_synonym="Cast2; ELKS; ERC-1; RAB6IP2"
                     /coded_by="NM_178040.4:257..3607"
                     /note="isoform epsilon is encoded by transcript variant
                     epsilon"
                     /db_xref="CCDS:CCDS8508.1"
                     /db_xref="GeneID:23085"
                     /db_xref="HGNC:HGNC:17072"
                     /db_xref="MIM:607127"
ORIGIN      
        1 mygsarsvgk vepssqspgr sprlprsprl ghrrtnstgg ssgssvgggs gktlsmeniq
       61 slnaayatsg pmylsdhenv gsetpkstmt lgrsggrlpy gvrmtamgss pniassgvas
      121 dtiafgehhl ppvsmastvp hslrqardnt imdlqtqlke vlrendllrk dvevkeskls
      181 ssmnsiktfw spelkkeral rkdeaskiti wkeqyrvvqe enqhmqmtiq alqdelriqr
      241 dlnqlfqqds ssrtgepcva elteenfqrl haeherqake lfllrktlee melrietqkq
      301 tlnardesik kllemlqskg lsakateedh ertrrlaeae mhvhhlesll eqkekensml
      361 reemhrrfen apdsaktkal qtviemkdsk issmerglrd leeeiqmlks ngalsteere
      421 eemkqmevyr shskfmknkv eqlkeelssk eaqweelkkk aaglqaeigq vkqelsrkdt
      481 ellalqtkle tltnqfsdsk qhievlkesl takeqraail qtevdalrlr leeketmlnk
      541 ktkqiqdmae ekgtqageih dlkdmldvke rkvnvlqkki enlqeqlrdk ekqmsslker
      601 vkslqadttn tdtalttlee alaekertie rlkeqrdrde rekqeeidny kkdlkdlkek
      661 vsllqgdlse keaslldlke hasslassgl kkdsrlktle ialeqkkeec lkmesqlkka
      721 heaalearas pemsdriqhl ereitrykde sskaqaevdr lleilkeven ekndkdkkia
      781 elerqvkdqn kkvanlkhke qvekkksaqm leearrredn lndssqqlqd slrkkddrie
      841 eleealresv qitaeremvl aqeesartna ekqveellma mekvkqeles mkaklsstqq
      901 slaekethlt nlraerrkhl eevlemkqea llaaisekda niallelsss kkktqeevaa
      961 lkrekdrlvq qlkqqtqnrm klmadnyedd hfksshsnqt nhkpspdqii qplleldqnr
     1021 sklklyighl ttlchdrdpl ilrgltppas ynldddqaaw enelqkmtrg qlqdelekge
     1081 rdnaelqefa nailqqiadh cpdileqvvn aleess
//
LOCUS       NP_001155                710 aa            linear   PRI 27-APR-2025
DEFINITION  amyloid beta precursor protein binding family B member 1 isoform a
            [Homo sapiens].
ACCESSION   NP_001155
VERSION     NP_001155.1
DBSOURCE    REFSEQ: accession NM_001164.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Revol,R.S., Koistinen,N.A., Menon,P.K., Chicote-Gonzalez,A.,
            Iverfeldt,K. and Strom,A.L.
  TITLE     Alpha-secretase dependent nuclear localization of the amyloid-beta
            precursor protein-binding protein Fe65 promotes DNA repair
  JOURNAL   Mol Cell Neurosci 127, 103903 (2023)
   PUBMED   37918552
  REMARK    GeneRIF: Alpha-secretase dependent nuclear localization of the
            amyloid-beta precursor protein-binding protein Fe65 promotes DNA
            repair.
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Chau,D.D., Li,W., Chan,W.W.R., Sun,J.K., Zhai,Y., Chow,H.M. and
            Lau,K.F.
  TITLE     Insulin stimulates atypical protein kinase C-mediated
            phosphorylation of the neuronal adaptor FE65 to potentiate neurite
            outgrowth by activating ARF6-Rac1 signaling
  JOURNAL   FASEB J 36 (11), e22594 (2022)
   PUBMED   36250347
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Hu,Q., Hearn,M.G., Jin,L.W., Bressler,S.L. and Martin,G.M.
  TITLE     Alternatively spliced isoforms of FE65 serve as neuron-specific and
            non-neuronal markers
  JOURNAL   J Neurosci Res 58 (5), 632-640 (1999)
   PUBMED   10561691
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Ermekova,K.S., Zambrano,N., Linn,H., Minopoli,G., Gertler,F.,
            Russo,T. and Sudol,M.
  TITLE     The WW domain of neural protein FE65 interacts with proline-rich
            motifs in Mena, the mammalian homolog of Drosophila enabled
  JOURNAL   J Biol Chem 272 (52), 32869-32877 (1997)
   PUBMED   9407065
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Zambrano,N., Buxbaum,J.D., Minopoli,G., Fiore,F., De Candia,P., De
            Renzis,S., Faraonio,R., Sabo,S., Cheetham,J., Sudol,M. and Russo,T.
  TITLE     Interaction of the phosphotyrosine interaction/phosphotyrosine
            binding-related domains of Fe65 with wild-type and mutant
            Alzheimer's beta-amyloid precursor proteins
  JOURNAL   J Biol Chem 272 (10), 6399-6405 (1997)
   PUBMED   9045663
REFERENCE   8  (residues 1 to 710)
  AUTHORS   McLoughlin,D.M. and Miller,C.C.
  TITLE     The intracellular cytoplasmic domain of the Alzheimer's disease
            amyloid precursor protein interacts with phosphotyrosine-binding
            domain proteins in the yeast two-hybrid system
  JOURNAL   FEBS Lett 397 (2-3), 197-200 (1996)
   PUBMED   8955346
REFERENCE   9  (residues 1 to 710)
  AUTHORS   Borg,J.P., Ooi,J., Levy,E. and Margolis,B.
  TITLE     The phosphotyrosine interaction domains of X11 and FE65 bind to
            distinct sites on the YENPTY motif of amyloid precursor protein
  JOURNAL   Mol Cell Biol 16 (11), 6229-6241 (1996)
   PUBMED   8887653
REFERENCE   10 (residues 1 to 710)
  AUTHORS   Bressler,S.L., Gray,M.D., Sopher,B.L., Hu,Q., Hearn,M.G.,
            Pham,D.G., Dinulos,M.B., Fukuchi,K., Sisodia,S.S., Miller,M.A.,
            Disteche,C.M. and Martin,G.M.
  TITLE     cDNA cloning and chromosome mapping of the human Fe65 gene:
            interaction of the conserved cytoplasmic domains of the human
            beta-amyloid precursor protein and its homologues with the mouse
            Fe65 protein
  JOURNAL   Hum Mol Genet 5 (10), 1589-1598 (1996)
   PUBMED   8894693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY145957.1, L77864.1 and
            BC010854.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the Fe65
            protein family. It is an adaptor protein localized in the nucleus.
            It interacts with the Alzheimer's disease amyloid precursor protein
            (APP), transcription factor CP2/LSF/LBP1 and the low-density
            lipoprotein receptor-related protein. APP functions as a cytosolic
            anchoring site that can prevent the gene product's nuclear
            translocation. This encoded protein could play an important role in
            the pathogenesis of Alzheimer's disease. It is thought to regulate
            transcription. Also it is observed to block cell cycle progression
            by downregulating thymidylate synthase expression. Multiple
            alternatively spliced transcript variants encoding different
            isoforms have been described for this gene. [provided by RefSeq,
            Mar 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a, also known as E9).
            This isoform is exclusively expressed in neurons.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.236835.1,
                                           SRR1803612.229885.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000609360.6/ ENSP00000477213.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..710
                     /product="amyloid beta precursor protein binding family B
                     member 1 isoform a"
                     /note="stat-like protein; adaptor protein FE65a2; amyloid
                     beta (A4) precursor protein-binding, family B, member 1
                     (Fe65)"
                     /calculated_mol_wt=77113
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00213.2)"
     Region          131..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00213.2)"
     Site            204
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:33938178; propagated from
                     UniProtKB/Swiss-Prot (O00213.2)"
     Region          255..283
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          276..299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00213.2)"
     Region          340..365
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00213.2)"
     Region          368..507
                     /region_name="PTB1_Fe65"
                     /note="Fe65 N-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01272"
                     /db_xref="CDD:269970"
     Site            order(382,451,470)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269970"
     Site            order(450..455,470,492,496)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269970"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:36250347; propagated from
                     UniProtKB/Swiss-Prot (O00213.2)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXJ1; propagated from
                     UniProtKB/Swiss-Prot (O00213.2)"
     Region          535..660
                     /region_name="PTB2_Fe65"
                     /note="Fe65 C-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01271"
                     /db_xref="CDD:269969"
     Site            order(546,619,638)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269969"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000269|PubMed:15031292,
                     ECO:0000269|PubMed:18922798; propagated from
                     UniProtKB/Swiss-Prot (O00213.2)"
     Site            order(557,559,606..607,609..616,618,626,632,642,644,647,
                     651,654..655,657..658)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269969"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SGK1.
                     /evidence=ECO:0000250|UniProtKB:P46933; propagated from
                     UniProtKB/Swiss-Prot (O00213.2)"
     Site            701
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:33938178; propagated from
                     UniProtKB/Swiss-Prot (O00213.2)"
     CDS             1..710
                     /gene="APBB1"
                     /gene_synonym="FE65; MGC:9072; RIR"
                     /coded_by="NM_001164.5:125..2257"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS66018.1"
                     /db_xref="GeneID:322"
                     /db_xref="HGNC:HGNC:581"
                     /db_xref="MIM:602709"
ORIGIN      
        1 msvpsslsqs ainanshggp alslplplha ahnqllnakl qatavgpkdl rsamgegggp
       61 epgpanakwl kegqnqlrra atahrdqnrn vtltlaeeas qepemaplgp kglihlysel
      121 elsahnaanr glrgpgliis tqeqgpdege ekaageaeee eeddddeeee edlssppglp
      181 eplesveapp rpqaltdgpr ehsksasllf gmrnsaasde dsswatlsqg spsygspedt
      241 dsfwnpnafe tdsdlpagwm rvqdtsgtyy whiptgttqw eppgraspsq gsspqeesql
      301 twtgfahgeg fedgefwkde psdeapmelg lkepeegtlt fpaqslspep lpqeeeklpp
      361 rntnpgikcf avrslgwvem teeelapgrs svavnncirq lsyhknnlhd pmsggwgegk
      421 dlllqledet lklvepqsqa llhaqpiisi rvwgvgrdsg rerdfayvar dkltqmlkch
      481 vfrceapakn iatslheics kimaerrnar clvnglsldh sklvdvpfqv efpapknelv
      541 qkfqvyylgn vpvakpvgvd vingalesvl ssssreqwtp shvsvapatl tilhqqteav
      601 lgecrvrfls flavgrdvht fafimaagpa sfcchmfwce pnaaslseav qaacmlryqk
      661 cldarsqast sclpappaes varrvgwtvr rgvqslwgsl kpkrlgahtp
//
LOCUS       NP_001014305             259 aa            linear   PRI 27-APR-2025
DEFINITION  DCN1-like protein 2 [Homo sapiens].
ACCESSION   NP_001014305
VERSION     NP_001014305.1
DBSOURCE    REFSEQ: accession NM_001014283.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Keuss,M.J., Thomas,Y., Mcarthur,R., Wood,N.T., Knebel,A. and
            Kurz,T.
  TITLE     Characterization of the mammalian family of DCN-type NEDD8 E3
            ligases
  JOURNAL   J Cell Sci 129 (7), 1441-1454 (2016)
   PUBMED   26906416
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Monda,J.K., Scott,D.C., Miller,D.J., Lydeard,J., King,D.,
            Harper,J.W., Bennett,E.J. and Schulman,B.A.
  TITLE     Structural conservation of distinctive N-terminal
            acetylation-dependent interactions across a family of mammalian
            NEDD8 ligation enzymes
  JOURNAL   Structure 21 (1), 42-53 (2013)
   PUBMED   23201271
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Meyer-Schaller,N., Chou,Y.C., Sumara,I., Martin,D.D., Kurz,T.,
            Katheder,N., Hofmann,K., Berthiaume,L.G., Sicheri,F. and Peter,M.
  TITLE     The human Dcn1-like protein DCNL3 promotes Cul3 neddylation at
            membranes
  JOURNAL   Proc Natl Acad Sci U S A 106 (30), 12365-12370 (2009)
   PUBMED   19617556
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Kurz,T., Ozlu,N., Rudolf,F., O'Rourke,S.M., Luke,B., Hofmann,K.,
            Hyman,A.A., Bowerman,B. and Peter,M.
  TITLE     The conserved protein DCN-1/Dcn1p is required for cullin
            neddylation in C. elegans and S. cerevisiae
  JOURNAL   Nature 435 (7046), 1257-1261 (2005)
   PUBMED   15988528
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL442125.13, BM836766.1, AK001566.1 and AK000099.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.79048.1,
                                           SRR1803613.91220.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000478244.6/ ENSP00000417706.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..259
                     /product="DCN1-like protein 2"
                     /note="DCUN1 domain-containing protein 2; defective in
                     cullin neddylation protein 1-like protein 2; DCN1,
                     defective in cullin neddylation 1, domain containing 2"
                     /calculated_mol_wt=30048
     Region          2..48
                     /region_name="UBA_DCNL2"
                     /note="UBA-like domain found in DCN1-like protein 2
                     (DCNL2) and similar proteins; cd14412"
                     /db_xref="CDD:270595"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZJ7; propagated from
                     UniProtKB/Swiss-Prot (Q6PH85.1)"
     Region          136..246
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     CDS             1..259
                     /gene="DCUN1D2"
                     /gene_synonym="C13orf17; DCNL2"
                     /coded_by="NM_001014283.2:43..822"
                     /db_xref="CCDS:CCDS32013.1"
                     /db_xref="GeneID:55208"
                     /db_xref="HGNC:HGNC:20328"
ORIGIN      
        1 mhklkssqkd kvrqfmactq agertaiycl tqnewrldea tdsffqnpds lhresmrnav
       61 dkkklerlyg rykdpqdenk igvdgiqqfc ddlsldpasi svlviawkfr aatqcefsrk
      121 efldgmtelg cdsmeklkal lprleqelkd takfkdfyqf tftfaknpgq kgldlemava
      181 ywklvlsgrf kfldlwntfl mehhkrsipr dtwnllldfg nmiaddmsny deegawpvli
      241 ddfveyarpv vtggkrslf
//
LOCUS       NP_036418                288 aa            linear   PRI 27-APR-2025
DEFINITION  mortality factor 4-like protein 2 [Homo sapiens].
ACCESSION   NP_036418
VERSION     NP_036418.1
DBSOURCE    REFSEQ: accession NM_012286.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Kooblall,K.G., Stokes,V.J., Shariq,O.A., English,K.A.,
            Stevenson,M., Broxholme,J., Wright,B., Lockstone,H.E., Buck,D.,
            Grozinsky-Glasberg,S., Yates,C.J., Thakker,R.V. and Lines,K.E.
  TITLE     miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2
  JOURNAL   Endocr Relat Cancer 29 (10), 557-568 (2022)
   PUBMED   35900839
  REMARK    GeneRIF: miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Zheng,X., Sun,Z., Yu,L., Shi,D., Zhu,M., Yao,H. and Li,L.
  TITLE     Interactome Analysis of the Nucleocapsid Protein of SARS-CoV-2
            Virus
  JOURNAL   Pathogens 10 (9), 1155 (2021)
   PUBMED   34578187
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Zhang,R., Ji,Z., Yao,Y., Zuo,W., Yang,M., Qu,Y., Su,Y., Ma,G. and
            Li,Y.
  TITLE     Identification of hub genes in unstable atherosclerotic plaque by
            conjoint analysis of bioinformatics
  JOURNAL   Life Sci 262, 118517 (2020)
   PUBMED   33011223
  REMARK    GeneRIF: Identification of hub genes in unstable atherosclerotic
            plaque by conjoint analysis of bioinformatics.
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Cai,Y., Jin,J., Tomomori-Sato,C., Sato,S., Sorokina,I.,
            Parmely,T.J., Conaway,R.C. and Conaway,J.W.
  TITLE     Identification of new subunits of the multiprotein mammalian
            TRRAP/TIP60-containing histone acetyltransferase complex
  JOURNAL   J Biol Chem 278 (44), 42733-42736 (2003)
   PUBMED   12963728
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Yochum,G.S. and Ayer,D.E.
  TITLE     Role for the mortality factors MORF4, MRGX, and MRG15 in
            transcriptional repression via associations with Pf1, mSin3A, and
            Transducin-Like Enhancer of Split
  JOURNAL   Mol Cell Biol 22 (22), 7868-7876 (2002)
   PUBMED   12391155
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Sakai,K., Shirakawa,T., Li,Y., Kitagawa,Y. and Hirose,G.
  TITLE     Interaction of a paraneoplastic cerebellar degeneration-associated
            neuronal protein with the nuclear helix-loop-helix leucine zipper
            protein MRG X
  JOURNAL   Mol Cell Neurosci 19 (4), 477-484 (2002)
   PUBMED   11988016
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Bertram,M.J., Berube,N.G., Hang-Swanson,X., Ran,Q., Leung,J.K.,
            Bryce,S., Spurgers,K., Bick,R.J., Baldini,A., Ning,Y., Clark,L.J.,
            Parkinson,E.K., Barrett,J.C., Smith,J.R. and Pereira-Smith,O.M.
  TITLE     Identification of a gene that reverses the immortal phenotype of a
            subset of cells and is a member of a novel family of transcription
            factor-like genes
  JOURNAL   Mol Cell Biol 19 (2), 1479-1485 (1999)
   PUBMED   9891081
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA987770.1, AL049610.9 and BC093013.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.65532.1,
                                           SRR5189655.79087.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000441076.7/ ENSP00000391969.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.2"
     Protein         1..288
                     /product="mortality factor 4-like protein 2"
                     /note="MSL3-2 protein; protein MSL3-2; MORF-related gene X
                     protein; transcription factor-like protein MRGX"
                     /calculated_mol_wt=32177
     Region          1..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15014.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15014.1)"
     Region          102..276
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..288
                     /gene="MORF4L2"
                     /gene_synonym="MORFL2; MRGX"
                     /coded_by="NM_012286.3:337..1203"
                     /db_xref="CCDS:CCDS14512.1"
                     /db_xref="GeneID:9643"
                     /db_xref="HGNC:HGNC:16849"
                     /db_xref="MIM:300409"
ORIGIN      
        1 mssrkqgsqp rgqqsaeeen fkkptrsnmq rskmrgassg kktagpqqkn lepalpgrwg
       61 grsaenppsg svrktrknkq ktpgngdggs tseapqpprk kraradptve seeafknrme
      121 vkvkipeelk pwlvedwdlv trqkqlfqlp akknvdaile eyanckksqg nvdnkeyavn
      181 evvagikeyf nvmlgtqlly kferpqyaei llahpdapms qvygaphllr lfvrigamla
      241 ytpldeksla lllgylhdfl kylaknsasl ftasdykvas aeyhrkal
//
LOCUS       NP_057181                 82 aa            linear   PRI 27-APR-2025
DEFINITION  immediate early response 3-interacting protein 1 [Homo sapiens].
ACCESSION   NP_057181 NP_060992
VERSION     NP_057181.1
DBSOURCE    REFSEQ: accession NM_016097.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Zhong,X., Moresco,J.J., Keller,K., Lazaro,D.R., Ely,C.,
            Moresco,E.M.Y., Beutler,B. and Choi,J.H.
  TITLE     Essential requirement for IER3IP1 in B cell development
  JOURNAL   Proc Natl Acad Sci U S A 120 (46), e2312810120 (2023)
   PUBMED   37934820
  REMARK    GeneRIF: Essential requirement for IER3IP1 in B cell development.
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Esk,C., Lindenhofer,D., Haendeler,S., Wester,R.A., Pflug,F.,
            Schroeder,B., Bagley,J.A., Elling,U., Zuber,J., von Haeseler,A. and
            Knoblich,J.A.
  TITLE     A human tissue screen identifies a regulator of ER secretion as a
            brain-size determinant
  JOURNAL   Science 370 (6519), 935-941 (2020)
   PUBMED   33122427
  REMARK    GeneRIF: A human tissue screen identifies a regulator of ER
            secretion as a brain-size determinant.
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Valenzuela,I., Boronat,S., Martinez-Saez,E., Clemente,M.,
            Sanchez-Montanez,A., Munell,F., Carrascosa,A. and Macaya,A.
  TITLE     Microcephaly with simplified gyral pattern, epilepsy and permanent
            neonatal diabetes syndrome (MEDS). A new patient and review of the
            literature
  JOURNAL   Eur J Med Genet 60 (10), 517-520 (2017)
   PUBMED   28711742
  REMARK    GeneRIF: 233 T > C mutation in the IER3IP1 causes microcephaly with
            simplified gyral pattern, epilepsy and permanent neonatal diabetes
            syndrome.
            Review article
REFERENCE   5  (residues 1 to 82)
  AUTHORS   Poulton,C.J., Schot,R., Kia,S.K., Jones,M., Verheijen,F.W.,
            Venselaar,H., de Wit,M.C., de Graaff,E., Bertoli-Avella,A.M. and
            Mancini,G.M.
  TITLE     Microcephaly with simplified gyration, epilepsy, and infantile
            diabetes linked to inappropriate apoptosis of neural progenitors
  JOURNAL   Am J Hum Genet 89 (2), 265-276 (2011)
   PUBMED   21835305
REFERENCE   6  (residues 1 to 82)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 82)
  AUTHORS   Yiu,W.H., Yeung,T.L., Poon,J.W., Tsui,S.K., Fung,K.P. and Waye,M.M.
  TITLE     Transcriptional regulation of IER3IP1 gene by tumor necrosis
            factor-alpha and Sp family proteins
  JOURNAL   Cell Biochem Funct 28 (1), 31-37 (2010)
   PUBMED   19885854
  REMARK    GeneRIF: IER3IP1 gene expression is regulated by Sp1, Sp3, and the
            TNF-a; induction of the gene in HepG2 liver cancer cell line
REFERENCE   8  (residues 1 to 82)
  AUTHORS   Lei,Y., Zhang,Y. and Wang,Y.Q.
  TITLE     [Effect of IER3IP1 gene expression on the proliferation and
            erythroid differentiation of K562 cells]
  JOURNAL   Zhonghua Xue Ye Xue Za Zhi 30 (6), 409-413 (2009)
   PUBMED   19951536
  REMARK    GeneRIF: Inhibiting the expression of IER3IP1 can inhibit erythroid
            differentiation and elevate the proliferation of K562 cells.
REFERENCE   9  (residues 1 to 82)
  AUTHORS   Wang,W.J., Zhang,Y. and Huang,F.X.
  TITLE     [The expression of IER3IP1 gene in K562 cells treated by matrine
            and its effect on the cell growth]
  JOURNAL   Zhonghua Xue Ye Xue Za Zhi 28 (12), 823-827 (2007)
   PUBMED   18476594
  REMARK    GeneRIF: Matrine can inhibit the growth of K562 cells, and
            transiently increase the expression level of IER3IP1 gene in a
            dose-dependent manner.
REFERENCE   10 (residues 1 to 82)
  AUTHORS   Yiu,W.H., Poon,J.W., Tsui,S.K., Fung,K.P. and Waye,M.M.
  TITLE     Cloning and characterization of a novel endoplasmic reticulum
            localized G-patch domain protein, IER3IP1
  JOURNAL   Gene 337, 37-44 (2004)
   PUBMED   15276200
  REMARK    GeneRIF: IER3IP1 gene was mapped to chromosome 18q12 and showed a
            high expression in heart, skeletal muscle and kidney, a moderate
            expression in liver and brain and a low expression in placenta,
            lung and peripheral blood leukocyte.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM829309.1, AF164798.1,
            AA211693.1 and AC051635.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 17, 2001 this sequence version replaced NP_060992.1.
            
            Summary: This gene encodes a small protein that is localized to the
            endoplasmic reticulum (ER) and may play a role in the ER stress
            response by mediating cell differentiation and apoptosis.
            Transcription of this gene is regulated by tumor necrosis factor
            alpha and specificity protein 1 (Sp1). Mutations in this gene may
            play a role in microcephaly, epilepsy, and diabetes syndrome
            (MEDS), and a pseudogene of this gene is located on the long arm of
            chromosome 12. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027108.1, SRR1803617.7722.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159080, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256433.6/ ENSP00000256433.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..82
                     /product="immediate early response 3-interacting protein
                     1"
                     /calculated_mol_wt=8838
     Site            2..22
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5U9.1)"
     Region          5..82
                     /region_name="Yos1"
                     /note="Yos1-like; pfam08571"
                     /db_xref="CDD:462523"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5U9.1)"
     CDS             1..82
                     /gene="IER3IP1"
                     /gene_synonym="HSPC039; MEDS; PRO2309"
                     /coded_by="NM_016097.5:88..336"
                     /db_xref="CCDS:CCDS11933.1"
                     /db_xref="GeneID:51124"
                     /db_xref="HGNC:HGNC:18550"
                     /db_xref="MIM:609382"
ORIGIN      
        1 maftlysllq aallcvnaia vlheerflkn igwgtdqgig gfgeepgiks qlmnlirsvr
       61 tvmrvpliiv nsiaivllll fg
//
LOCUS       NP_001139140              81 aa            linear   PRI 27-APR-2025
DEFINITION  cortexin-2 [Homo sapiens].
ACCESSION   NP_001139140
VERSION     NP_001139140.1
DBSOURCE    REFSEQ: accession NM_001145668.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Zody,M.C., Garber,M., Sharpe,T., Young,S.K., Rowen,L., O'Neill,K.,
            Whittaker,C.A., Kamal,M., Chang,J.L., Cuomo,C.A., Dewar,K.,
            FitzGerald,M.G., Kodira,C.D., Madan,A., Qin,S., Yang,X., Abbasi,N.,
            Abouelleil,A., Arachchi,H.M., Baradarani,L., Birditt,B., Bloom,S.,
            Bloom,T., Borowsky,M.L., Burke,J., Butler,J., Cook,A.,
            DeArellano,K., DeCaprio,D., Dorris,L. 3rd, Dors,M., Eichler,E.E.,
            Engels,R., Fahey,J., Fleetwood,P., Friedman,C., Gearin,G.,
            Hall,J.L., Hensley,G., Johnson,E., Jones,C., Kamat,A., Kaur,A.,
            Locke,D.P., Madan,A., Munson,G., Jaffe,D.B., Lui,A., Macdonald,P.,
            Mauceli,E., Naylor,J.W., Nesbitt,R., Nicol,R., O'Leary,S.B.,
            Ratcliffe,A., Rounsley,S., She,X., Sneddon,K.M., Stewart,S.,
            Sougnez,C., Stone,S.M., Topham,K., Vincent,D., Wang,S.,
            Zimmer,A.R., Birren,B.W., Hood,L., Lander,E.S. and Nusbaum,C.
  TITLE     Analysis of the DNA sequence and duplication history of human
            chromosome 15
  JOURNAL   Nature 440 (7084), 671-675 (2006)
   PUBMED   16572171
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC066612.7 and BX537772.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX537772.1, SRR1803614.89059.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000417307.3/ ENSP00000406145.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..81
                     /product="cortexin-2"
                     /calculated_mol_wt=8849
     Region          9..81
                     /region_name="Cortexin"
                     /note="Cortexin of kidney; pfam11057"
                     /db_xref="CDD:314086"
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C2S0.1)"
     CDS             1..81
                     /gene="CTXN2"
                     /coded_by="NM_001145668.2:247..492"
                     /db_xref="CCDS:CCDS45254.1"
                     /db_xref="GeneID:399697"
                     /db_xref="HGNC:HGNC:31109"
ORIGIN      
        1 msstycgnss akmsvnevsa fsltleqktg fafvgilcif lglliircfk illdpyssmp
       61 sstwedevee fdkgtfeyal a
//
LOCUS       NP_001346892             396 aa            linear   ROD 27-APR-2025
DEFINITION  N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D isoform
            b [Mus musculus].
ACCESSION   NP_001346892 XP_006535774
VERSION     NP_001346892.1
DBSOURCE    REFSEQ: accession NM_001359963.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Tevosian,M., Todorov,H., Lomazzo,E., Bindila,L., Ueda,N.,
            Bassetti,D., Warm,D., Kirischuk,S., Luhmann,H.J., Gerber,S. and
            Lutz,B.
  TITLE     NAPE-PLD deletion in stress-TRAPed neurons results in an anxiogenic
            phenotype
  JOURNAL   Transl Psychiatry 13 (1), 152 (2023)
   PUBMED   37149657
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Palese,F., Pontis,S., Realini,N. and Piomelli,D.
  TITLE     NAPE-specific phospholipase D regulates LRRK2 association with
            neuronal membranes
  JOURNAL   Adv Pharmacol 90, 217-238 (2021)
   PUBMED   33706934
  REMARK    GeneRIF: NAPE-specific phospholipase D regulates LRRK2 association
            with neuronal membranes.
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Rastelli,M., Van Hul,M., Terrasi,R., Lefort,C., Regnier,M.,
            Beiroa,D., Delzenne,N.M., Everard,A., Nogueiras,R., Luquet,S.,
            Muccioli,G.G. and Cani,P.D.
  TITLE     Intestinal NAPE-PLD contributes to short-term regulation of food
            intake via gut-to-brain axis
  JOURNAL   Am J Physiol Endocrinol Metab 319 (3), E647-E657 (2020)
   PUBMED   32776827
  REMARK    GeneRIF: Intestinal NAPE-PLD contributes to short-term regulation
            of food intake via gut-to-brain axis.
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Aggarwal,G., Zarrow,J.E., Mashhadi,Z., Flynn,C.R., Vinson,P.,
            Weaver,C.D. and Davies,S.S.
  TITLE     Symmetrically substituted dichlorophenes inhibit
            N-acyl-phosphatidylethanolamine phospholipase D
  JOURNAL   J Biol Chem 295 (21), 7289-7300 (2020)
   PUBMED   32284327
  REMARK    GeneRIF: Symmetrically substituted dichlorophenes inhibit
            N-acyl-phosphatidylethanolamine phospholipase D.
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Lefort,C., Roumain,M., Van Hul,M., Rastelli,M., Manco,R.,
            Leclercq,I., Delzenne,N.M., Marzo,V.D., Flamand,N., Luquet,S.,
            Silvestri,C., Muccioli,G.G. and Cani,P.D.
  TITLE     Hepatic NAPE-PLD Is a Key Regulator of Liver Lipid Metabolism
  JOURNAL   Cells 9 (5), 1247 (2020)
   PUBMED   32443626
  REMARK    GeneRIF: Hepatic NAPE-PLD Is a Key Regulator of Liver Lipid
            Metabolism.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Simon,G.M. and Cravatt,B.F.
  TITLE     Endocannabinoid biosynthesis proceeding through
            glycerophospho-N-acyl ethanolamine and a role for
            alpha/beta-hydrolase 4 in this pathway
  JOURNAL   J Biol Chem 281 (36), 26465-26472 (2006)
   PUBMED   16818490
  REMARK    GeneRIF: Results support the existence of an N-acyl
            phosphatidylethanolamine (NAPE)-phospholipase D-independent route
            for N-acyl ethanolamine (NAE) biosynthesis and suggest that Abh4
            plays a role in this pathway by acting as a (lyso)NAPE-selective
            lipase.
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Wang,J., Okamoto,Y., Morishita,J., Tsuboi,K., Miyatake,A. and
            Ueda,N.
  TITLE     Functional analysis of the purified anandamide-generating
            phospholipase D as a member of the metallo-beta-lactamase family
  JOURNAL   J Biol Chem 281 (18), 12325-12335 (2006)
   PUBMED   16527816
REFERENCE   8  (residues 1 to 396)
  AUTHORS   Leung,D., Saghatelian,A., Simon,G.M. and Cravatt,B.F.
  TITLE     Inactivation of N-acyl phosphatidylethanolamine phospholipase D
            reveals multiple mechanisms for the biosynthesis of
            endocannabinoids
  JOURNAL   Biochemistry 45 (15), 4720-4726 (2006)
   PUBMED   16605240
  REMARK    GeneRIF: Inactivation of N-acyl phosphatidylethanolamine
            phospholipase D reveals multiple mechanisms for the biosynthesis of
            endocannabinoids.
REFERENCE   9  (residues 1 to 396)
  AUTHORS   Okamoto,Y., Morishita,J., Wang,J., Schmid,P.C., Krebsbach,R.J.,
            Schmid,H.H. and Ueda,N.
  TITLE     Mammalian cells stably overexpressing
            N-acylphosphatidylethanolamine-hydrolysing phospholipase D exhibit
            significantly decreased levels of N-acylphosphatidylethanolamines
  JOURNAL   Biochem J 389 (Pt 1), 241-247 (2005)
   PUBMED   15760304
  REMARK    GeneRIF: results confirm that overexpressed NAPE-PLD is capable of
            forming NAEs, including anandamide, in living cells
REFERENCE   10 (residues 1 to 396)
  AUTHORS   Okamoto,Y., Morishita,J., Tsuboi,K., Tonai,T. and Ueda,N.
  TITLE     Molecular characterization of a phospholipase D generating
            anandamide and its congeners
  JOURNAL   J Biol Chem 279 (7), 5298-5305 (2004)
   PUBMED   14634025
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125343.2, AK049135.1 and AC161484.4.
            
            On Jan 20, 2018 this sequence version replaced XP_006535774.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2, 3, and
            4 all encode the same isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK141585.1, AK049135.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164141, SAMN01164143
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 9.97 cM"
     Protein         1..396
                     /product="N-acyl-phosphatidylethanolamine-hydrolyzing
                     phospholipase D isoform b"
                     /EC_number="3.1.4.54"
                     /note="Metallo-beta-lactamase domain containing 1;
                     N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase
                     D; NAPE-hydrolyzing phospholipase D"
                     /calculated_mol_wt=45685
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH82.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q6IQ20; propagated from
                     UniProtKB/Swiss-Prot (Q8BH82.1)"
     Region          129..316
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
     Site            order(185,187,189..190,263..264,284,316)
                     /site_type="active"
                     /db_xref="CDD:293792"
     CDS             1..396
                     /gene="Napepld"
                     /gene_synonym="A530089G06; Mbldc1; NAPE-PLD"
                     /coded_by="NM_001359963.1:439..1629"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS19105.1"
                     /db_xref="GeneID:242864"
                     /db_xref="MGI:MGI:2140885"
ORIGIN      
        1 mdeyedsqsp apsyqypket lrkrqnsvqn sggsvssrfs rksfkldyrl eedvtkskkg
       61 kdgrfvnpwp twknisipnv lrwlimeknh sgvpgskeel dkelpvlkpy fvsdpedagv
      121 reaglrvtwl ghatlmvemd elifltdpmf ssraspsqym gpkrfrrppc tiselptida
      181 vlishnhydh ldygsvlaln erfgselrwf vplglldwmq kcgcenviel dwweencvpg
      241 hdkvtfvftp sqhwckrtll ddnkvlwgsw svlgpwsrff fagdtgycpa feeigkrfgp
      301 fdlaaipiga yeprwfmkyq hadpedavri hidlqtkrsv aihwgtfala nehyleppvk
      361 lnealerygl scedffilkh gesrylntdd rafeet
//
LOCUS       NP_001127835            1227 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding protein 20 [Homo sapiens].
ACCESSION   NP_001127835 XP_001716171 XP_291671 XP_944430
VERSION     NP_001127835.2
DBSOURCE    REFSEQ: accession NM_001134363.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1227)
  AUTHORS   Lin,X.
  TITLE     [Research progress on the expression of the RBM20 gene in dilated
            cardiomyopathy]
  JOURNAL   Zhongguo Dang Dai Er Ke Za Zhi 25 (10), 1084-1088 (2023)
   PUBMED   37905768
  REMARK    GeneRIF: [Research progress on the expression of the RBM20 gene in
            dilated cardiomyopathy].
            Review article
REFERENCE   2  (residues 1 to 1227)
  AUTHORS   Cannie,D.E., Protonotarios,A., Bakalakos,A., Syrris,P.,
            Lorenzini,M., De Stavola,B., Bjerregaard,L., Dybro,A.M., Hey,T.M.,
            Hansen,F.G., Navarro Penalver,M., Crespo-Leiro,M.G.,
            Larranaga-Moreira,J.M., de Frutos,F., Johnson,R., Slater,T.A.,
            Monserrat,L., Sengupta,A., Mestroni,L., Taylor,M.R.G., Sinagra,G.,
            Bilinska,Z., Solla-Ruiz,I., Arana Achaga,X., Barriales-Villa,R.,
            Garcia-Pavia,P., Gimeno,J.R., Dal Ferro,M., Merlo,M., Wahbi,K.,
            Fatkin,D., Mogensen,J., Rasmussen,T.B. and Elliott,P.M.
  TITLE     Risks of Ventricular Arrhythmia and Heart Failure in Carriers of
            RBM20 Variants
  JOURNAL   Circ Genom Precis Med 16 (5), 434-441 (2023)
   PUBMED   37593875
  REMARK    GeneRIF: Risks of Ventricular Arrhythmia and Heart Failure in
            Carriers of RBM20 Variants.
REFERENCE   3  (residues 1 to 1227)
  AUTHORS   Yamamoto,T., Sano,R., Miura,A., Imasaka,M., Naito,Y.,
            Nishiguchi,M., Ihara,K., Otani,N., Kominato,Y., Ohmuraya,M.,
            Kuroyanagi,H. and Nishio,H.
  TITLE     I536T variant of RBM20 affects splicing of cardiac structural
            proteins that are causative for developing dilated cardiomyopathy
  JOURNAL   J Mol Med (Berl) 100 (12), 1741-1754 (2022)
   PUBMED   36198914
  REMARK    GeneRIF: I536T variant of RBM20 affects splicing of cardiac
            structural proteins that are causative for developing dilated
            cardiomyopathy.
REFERENCE   4  (residues 1 to 1227)
  AUTHORS   Sun,M., Jin,Y., Zhang,Y., Gregorich,Z.R., Ren,J., Ge,Y. and Guo,W.
  TITLE     SR Protein Kinases Regulate the Splicing of Cardiomyopathy-Relevant
            Genes via Phosphorylation of the RSRSP Stretch in RBM20
  JOURNAL   Genes (Basel) 13 (9), 1526 (2022)
   PUBMED   36140694
  REMARK    GeneRIF: SR Protein Kinases Regulate the Splicing of
            Cardiomyopathy-Relevant Genes via Phosphorylation of the RSRSP
            Stretch in RBM20.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1227)
  AUTHORS   Linke,W.A. and Bucker,S.
  TITLE     King of hearts: a splicing factor rules cardiac proteins
  JOURNAL   Nat Med 18 (5), 660-661 (2012)
   PUBMED   22561820
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1227)
  AUTHORS   Millat,G., Bouvagnet,P., Chevalier,P., Sebbag,L., Dulac,A.,
            Dauphin,C., Jouk,P.S., Delrue,M.A., Thambo,J.B., Le Metayer,P.,
            Seronde,M.F., Faivre,L., Eicher,J.C. and Rousson,R.
  TITLE     Clinical and mutational spectrum in a cohort of 105 unrelated
            patients with dilated cardiomyopathy
  JOURNAL   Eur J Med Genet 54 (6), e570-e575 (2011)
   PUBMED   21846512
REFERENCE   7  (residues 1 to 1227)
  AUTHORS   Li,D., Morales,A., Gonzalez-Quintana,J., Norton,N., Siegfried,J.D.,
            Hofmeyer,M. and Hershberger,R.E.
  TITLE     Identification of novel mutations in RBM20 in patients with dilated
            cardiomyopathy
  JOURNAL   Clin Transl Sci 3 (3), 90-97 (2010)
   PUBMED   20590677
  REMARK    GeneRIF: Dilated cardiomyopathy in patients with RBM20 mutations is
            associated with advanced disease.
REFERENCE   8  (residues 1 to 1227)
  AUTHORS   Macrae,C.A. and McKenna,W.J.
  TITLE     Splicing and dilated cardiomyopathy one gene to rule them all?
  JOURNAL   J Am Coll Cardiol 54 (10), 942-943 (2009)
   PUBMED   19712805
  REMARK    GeneRIF: RBM20 missense mutation is a novel gene underlying one
            form of dilated cardiomyopathy
REFERENCE   9  (residues 1 to 1227)
  AUTHORS   Brauch,K.M., Karst,M.L., Herron,K.J., de Andrade,M., Pellikka,P.A.,
            Rodeheffer,R.J., Michels,V.V. and Olson,T.M.
  TITLE     Mutations in ribonucleic acid binding protein gene cause familial
            dilated cardiomyopathy
  JOURNAL   J Am Coll Cardiol 54 (10), 930-941 (2009)
   PUBMED   19712804
  REMARK    GeneRIF: RBM20 as a dilated cardiomyopathy gene and reveal a
            mutation hotspot in the RS domain. Individuals in each family
            revealed distinct heterozygous missense mutations in exon 9 of
            RBM20, encoding ribonucleic acid (RNA) binding motif protein 20.
REFERENCE   10 (residues 1 to 1227)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359260.20, EU822950.1 and
            KF459660.1.
            
            On Apr 15, 2014 this sequence version replaced NP_001127835.1.
            
            Summary: This gene encodes a protein that binds RNA and regulates
            splicing. Mutations in this gene have been associated with familial
            dilated cardiomyopathy. [provided by RefSeq, Apr 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU822950.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151741, SAMEA2154361
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369519.4/ ENSP00000358532.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q25.2"
     Protein         1..1227
                     /product="RNA-binding protein 20"
                     /note="probable RNA-binding protein 20"
                     /calculated_mol_wt=134128
     Region          1..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T481.4)"
     Region          185..>362
                     /region_name="PTZ00395"
                     /note="Sec24-related protein; Provisional"
                     /db_xref="CDD:185594"
     Region          289..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Region          518..593
                     /region_name="RRM_RBM20"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     RNA-binding protein 20 (RBM20); cd12685"
                     /db_xref="CDD:410086"
     Site            order(521,523..524,549,551,554..556,558,589..593)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410086"
     Region          624..906
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T481.4)"
     Region          628..655
                     /region_name="RS. /evidence=ECO:0000305|PubMed:23886709"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UQS8; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PT37; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PT37; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            679
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Region          <682..941
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            801
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            865
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            891
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PT37; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PT37; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Region          977..1089
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            977
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PT37; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            980
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            1013
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PT37; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            1048
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UQS8; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            1060
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            1080
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            1115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PT37; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            1120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     Region          1159..1193
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          1201..1227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T481.4)"
     Site            1210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35427468; propagated from
                     UniProtKB/Swiss-Prot (Q5T481.4)"
     CDS             1..1227
                     /gene="RBM20"
                     /coded_by="NM_001134363.3:120..3803"
                     /db_xref="CCDS:CCDS44477.1"
                     /db_xref="GeneID:282996"
                     /db_xref="HGNC:HGNC:27424"
                     /db_xref="MIM:613171"
ORIGIN      
        1 mvlaaamsqd adpsgpeqpd rvacsvpgar aspapsgprg mqqpppppqp ppppqaglpq
       61 iiqnaaklld knpfsvsnpn pllpspaslq laqlqaqltl hrlklaqtav tnntaaatvl
      121 nqvlskvams qplfnqlrhp svitgphgha gvpqhaaaip strfpsnaia fsppsqtrgp
      181 gpsmnlpnqp psamvmhpft gvmpqtpgqp avilgigktg papatagfye ygkassgqty
      241 gpetdgqpgf lpssastsgs vtyeghysht gqdgqaafsk dfygpnsqgs hvasgfpaeq
      301 agglksevgp llqgtnsqwe sphgfsgqsk pdltagpmwp pphnqpyely dpeeptsdrt
      361 ppsfggrlnn skqgfigagr rakedqalls vrplqaheln dfhgvaplhl phicsicdkk
      421 vfdlkdwelh vkgklhaqkc lvfsenagir cilgsaegtl caspnstavy npagnedyas
      481 nlgtsyvpip arsftqsspt fplasvgttf aqrkgagrvv hicnlpegsc tendvinlgl
      541 pfgkvtnyil mkstnqafle mayteaaqam vqyyqeksav ingekllirm skrykelqlk
      601 kpgkavaaii qdihsqrerd mfreadrygp erprsrspvs rslsprshtp sftscssshs
      661 ppgpsradwg ngrdswehsp yarreeerdp apwrdngddk rdrmdpwahd rkhhprqldk
      721 aelderpegg rphrekyprs gspnlphsvs syksredgyy rkepkaksdk ylkqqqdapg
      781 rsrrkdearl resrhphpdd sgkedglgpk vtrapegaka kqneknktkr tdrdqegadd
      841 rkentmaene agkeeqegme espqsvgrqe keaefsdpen trtkkeqdwe seseaegesw
      901 yptnmeelvt vdevgeeedf ivepdipele eivpidqkdk icpetclcvt ttldldlaqd
      961 fpkegvkavg ngaaeislks prelpsasts cpsdmdvemp glnldaerkp aesetglsle
     1021 dsdcyekeak gvessdvhpa ptvqqmsspk paeerarqps pfvddcktrg tpedgacegs
     1081 pleekasppi etdlqnqacq evltpensry vemkslevrs peytevelkq plslpswepe
     1141 dvfselsipl gvefvvprtg fycklcglfy tseetakmsh crsavhyrnl qkylsqlaee
     1201 glketegads prpedsgivp rferkkl
//
LOCUS       NP_001157751             356 aa            linear   PRI 27-APR-2025
DEFINITION  glucose-6-phosphate exchanger SLC37A4 isoform 3 [Homo sapiens].
ACCESSION   NP_001157751
VERSION     NP_001157751.1
DBSOURCE    REFSEQ: accession NM_001164279.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Tanigaki,K., Matsumura,R., Sasaki,N., Kato,Y., Tamamori,T.,
            Yamaga,S., Nakamura,E., Sakanaka,A., Kuboniwa,M., Matsusaki,M.,
            Amano,A. and Takeuchi,H.
  TITLE     SLC37A4, gene responsible for glycogen storage disease type 1b,
            regulates gingival epithelial barrier function via JAM1 expression
  JOURNAL   Sci Rep 14 (1), 24797 (2024)
   PUBMED   39433915
  REMARK    GeneRIF: SLC37A4, gene responsible for glycogen storage disease
            type 1b, regulates gingival epithelial barrier function via JAM1
            expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Wang,Z., Zhao,R., Jia,X., Li,X., Ma,L. and Fu,H.
  TITLE     Three novel SLC37A4 variants in glycogen storage disease type 1b
            and a literature review
  JOURNAL   J Int Med Res 51 (12), 3000605231216633 (2023)
   PUBMED   38087503
  REMARK    GeneRIF: Three novel SLC37A4 variants in glycogen storage disease
            type 1b and a literature review.
            Review article
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Ng,B.G., Sosicka,P., Fenaille,F., Harroche,A.,
            Vuillaumier-Barrot,S., Porterfield,M., Xia,Z.J., Wagner,S.,
            Bamshad,M.J., Vergnes-Boiteux,M.C., Cholet,S., Dalton,S., Dell,A.,
            Dupre,T., Fiore,M., Haslam,S.M., Huguenin,Y., Kumagai,T., Kulik,M.,
            McGoogan,K., Michot,C., Nickerson,D.A., Pascreau,T., Borgel,D.,
            Raymond,K., Warad,D., Flanagan-Steet,H., Steet,R., Tiemeyer,M.,
            Seta,N., Bruneel,A. and Freeze,H.H.
  CONSRTM   University of Washington Center for Mendelian Genomics (UW-CMG)
  TITLE     A mutation in SLC37A4 causes a dominantly inherited congenital
            disorder of glycosylation characterized by liver dysfunction
  JOURNAL   Am J Hum Genet 108 (6), 1040-1052 (2021)
   PUBMED   33964207
  REMARK    GeneRIF: A mutation in SLC37A4 causes a dominantly inherited
            congenital disorder of glycosylation characterized by liver
            dysfunction.
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Xu,Q., Tang,H., Duan,L., Zuo,X., Shi,X., Li,Y., Zhao,H. and
            Zhang,H.
  TITLE     A novel SLC37A4 missense mutation in GSD-Ib without hepatomegaly
            causes enhanced leukocytes endoplasmic reticulum stress and
            apoptosis
  JOURNAL   Mol Genet Genomic Med 9 (1), e1568 (2021)
   PUBMED   33280276
  REMARK    GeneRIF: A novel SLC37A4 missense mutation in GSD-Ib without
            hepatomegaly causes enhanced leukocytes endoplasmic reticulum
            stress and apoptosis.
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Veiga-da-Cunha,M., Gerin,I., Chen,Y.T., de Barsy,T., de Lonlay,P.,
            Dionisi-Vici,C., Fenske,C.D., Lee,P.J., Leonard,J.V., Maire,I.,
            McConkie-Rosell,A., Schweitzer,S., Vikkula,M. and Van
            Schaftingen,E.
  TITLE     A gene on chromosome 11q23 coding for a putative glucose-
            6-phosphate translocase is mutated in glycogen-storage disease
            types Ib and Ic
  JOURNAL   Am J Hum Genet 63 (4), 976-983 (1998)
   PUBMED   9758626
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Annabi,B., Hiraiwa,H., Mansfield,B.C., Lei,K.J., Ubagai,T.,
            Polymeropoulos,M.H., Moses,S.W., Parvari,R., Hershkovitz,E.,
            Mandel,H., Fryman,M. and Chou,J.Y.
  TITLE     The gene for glycogen-storage disease type 1b maps to chromosome
            11q23
  JOURNAL   Am J Hum Genet 62 (2), 400-405 (1998)
   PUBMED   9463334
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Ihara,K., Takabayashi,A., Terasaki,K. and Hara,T.
  TITLE     Assignment1 of glucose 6-phosphate translocase (G6PT1) to human
            chromosome band 11q23.3 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 50-51 (1998)
   PUBMED   9925924
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Gerin,I., Veiga-da-Cunha,M., Achouri,Y., Collet,J.F. and Van
            Schaftingen,E.
  TITLE     Sequence of a putative glucose 6-phosphate translocase, mutated in
            glycogen storage disease type Ib
  JOURNAL   FEBS Lett 419 (2-3), 235-238 (1997)
   PUBMED   9428641
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Bali,D.S., El-Gharbawy,A., Austin,S., Pendyal,S. and Kishnani,P.S.
  TITLE     Glycogen Storage Disease Type I
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301489
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Narisawa,K., Igarashi,Y., Otomo,H. and Tada,K.
  TITLE     A new variant of glycogen storage disease type I probably due to a
            defect in the glucose-6-phosphate transport system
  JOURNAL   Biochem Biophys Res Commun 83 (4), 1360-1364 (1978)
   PUBMED   212064
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003392.2 and FP885832.1.
            
            Summary: This gene regulates glucose-6-phosphate transport from the
            cytoplasm to the lumen of the endoplasmic reticulum, in order to
            maintain glucose homeostasis. It also plays a role in ATP-mediated
            calcium sequestration in the lumen of the endoplasmic reticulum.
            Mutations in this gene have been associated with various forms of
            glycogen storage disease. Alternative splicing in this gene results
            in multiple transcript variants.[provided by RefSeq, Aug 2009].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            a downstream translational start codon, compared to variant 1. This
            results in a shorter protein (isoform 3), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300646.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..356
                     /product="glucose-6-phosphate exchanger SLC37A4 isoform 3"
                     /note="glucose-6-phosphate translocase;
                     glucose-6-phosphatase, transport (glucose-6-phosphate)
                     protein 1; glucose-6-phosphatase, transport
                     (phosphate/pyrophosphate) protein 2;
                     glucose-6-phosphatase, transport (glucose) protein 3;
                     microsomal glucose-6-phosphate transporter;
                     glucose-5-phosphate transporter; transformation-related
                     gene 19 protein; solute carrier family 37
                     (glucose-6-phosphate transporter), member 4;
                     glucose-6-phosphate exchanger SLC37A4;
                     glucose-6-phosphatase transporter; sugar-phosphate
                     exchange protein 4"
                     /calculated_mol_wt=38098
     Region          1..344
                     /region_name="MFS_SLC37A4"
                     /note="Solute carrier family 37 member 4 of the Major
                     Facilitator Superfamily of transporters; cd17343"
                     /db_xref="CDD:340901"
     Site            order(41..42,44..46,49,69,72..73,76,160,163..164,167..169,
                     172,200,204,268..269,273,277,293,296..297,300..301,304)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340901"
     CDS             1..356
                     /gene="SLC37A4"
                     /gene_synonym="CDG2W; G6PT; G6PT1; G6PT2; G6PT3; GSD1b;
                     GSD1c; GSD1d; PRO0685; SPX4; TRG-19; TRG19"
                     /coded_by="NM_001164279.2:374..1444"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:2542"
                     /db_xref="HGNC:HGNC:4061"
                     /db_xref="MIM:602671"
ORIGIN      
        1 msarwlfssg lllvglvnif fawsstvpvf aalwflngla qglgwppcgk vlrkwfepsq
       61 fgtwwailst smnlagglgp ilatilaqsy swrstlalsg alcvvvsflc lllihnepad
      121 vglrnldpmp segkkgslke estlqellls pylwvlstgy lvvfgvktcc tdwgqffliq
      181 ekgqsalvgs symsalevgg lvgsiaagyl sdramakagl snygnprhgl llfmmagmtv
      241 smylfrvtvt sdspklwilv lgavfgfssy gpialfgvia nesappnlcg tshaivglma
      301 nvggflaglp fstiakhysw stafwvaevi caastaaffl lrnirtkmgr vskkae
//
LOCUS       NP_006380                999 aa            linear   PRI 27-APR-2025
DEFINITION  hypoxia up-regulated protein 1 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_006380
VERSION     NP_006380.1
DBSOURCE    REFSEQ: accession NM_006389.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Wang,W., Jiang,X., Xia,F., Chen,X., Li,G., Liu,L., Xu,Q., Zhu,M.
            and Chen,C.
  TITLE     HYOU1 promotes cell proliferation, migration, and invasion via the
            PI3K/AKT/FOXO1 feedback loop in bladder cancer
  JOURNAL   Mol Biol Rep 50 (1), 453-464 (2023)
   PUBMED   36348197
  REMARK    GeneRIF: HYOU1 promotes cell proliferation, migration, and invasion
            via the PI3K/AKT/FOXO1 feedback loop in bladder cancer.
            Erratum:[Mol Biol Rep. 2023 Jun;50(6):5527. doi:
            10.1007/s11033-023-08325-4. PMID: 37072656]
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Arab,F., Rezaei,N., Taheri,F., Kouhpeikar,H., Rayzan,E.,
            Mirbeyk,M., Zare-Abdollahi,D. and Ghadami,M.
  TITLE     The Clinical and Molecular Assessment of Iranian Families with
            Severe Congenital Neutropenia, Identification of HYOU1 and SHOC2 as
            Potential Novel Gene Defects
  JOURNAL   Iran J Allergy Asthma Immunol 21 (3), 344-354 (2022)
   PUBMED   35822684
  REMARK    GeneRIF: The Clinical and Molecular Assessment of Iranian Families
            with Severe Congenital Neutropenia, Identification of HYOU1 and
            SHOC2 as Potential Novel Gene Defects.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Liu,J. and Wang,Y.
  TITLE     Long non-coding RNA KCNQ1OT1 facilitates the progression of
            cervical cancer and tumor growth through modulating
            miR-296-5p/HYOU1 axis
  JOURNAL   Bioengineered 12 (1), 8753-8767 (2021)
   PUBMED   34704918
  REMARK    GeneRIF: Long non-coding RNA KCNQ1OT1 facilitates the progression
            of cervical cancer and tumor growth through modulating
            miR-296-5p/HYOU1 axis.
REFERENCE   4  (residues 1 to 999)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 999)
  AUTHORS   Wang,J.M., Jiang,J.Y., Zhang,D.L., Du,X., Wu,T. and Du,Z.X.
  TITLE     HYOU1 facilitates proliferation, invasion and glycolysis of
            papillary thyroid cancer via stabilizing LDHB mRNA
  JOURNAL   J Cell Mol Med 25 (10), 4814-4825 (2021)
   PUBMED   33792181
  REMARK    GeneRIF: HYOU1 facilitates proliferation, invasion and glycolysis
            of papillary thyroid cancer via stabilizing LDHB mRNA.
REFERENCE   6  (residues 1 to 999)
  AUTHORS   Bando,Y., Ogawa,S., Yamauchi,A., Kuwabara,K., Ozawa,K., Hori,O.,
            Yanagi,H., Tamatani,M. and Tohyama,M.
  TITLE     150-kDa oxygen-regulated protein (ORP150) functions as a novel
            molecular chaperone in MDCK cells
  JOURNAL   Am J Physiol Cell Physiol 278 (6), C1172-C1182 (2000)
   PUBMED   10837345
REFERENCE   7  (residues 1 to 999)
  AUTHORS   Ozawa,K., Kuwabara,K., Tamatani,M., Takatsuji,K., Tsukamoto,Y.,
            Kaneda,S., Yanagi,H., Stern,D.M., Eguchi,Y., Tsujimoto,Y., Ogawa,S.
            and Tohyama,M.
  TITLE     150-kDa oxygen-regulated protein (ORP150) suppresses
            hypoxia-induced apoptotic cell death
  JOURNAL   J Biol Chem 274 (10), 6397-6404 (1999)
   PUBMED   10037731
REFERENCE   8  (residues 1 to 999)
  AUTHORS   Tsukamoto,Y., Kuwabara,K., Hirota,S., Kawano,K., Yoshikawa,K.,
            Ozawa,K., Kobayashi,T., Yanagi,H., Stern,D.M., Tohyama,M.,
            Kitamura,Y. and Ogawa,S.
  TITLE     Expression of the 150-kd oxygen-regulated protein in human breast
            cancer
  JOURNAL   Lab Invest 78 (6), 699-706 (1998)
   PUBMED   9645760
REFERENCE   9  (residues 1 to 999)
  AUTHORS   Ikeda,J., Kaneda,S., Kuwabara,K., Ogawa,S., Kobayashi,T.,
            Matsumoto,M., Yura,T. and Yanagi,H.
  TITLE     Cloning and expression of cDNA encoding the human 150 kDa
            oxygen-regulated protein, ORP150
  JOURNAL   Biochem Biophys Res Commun 230 (1), 94-99 (1997)
   PUBMED   9020069
REFERENCE   10 (residues 1 to 999)
  AUTHORS   Tsukamoto,Y., Kuwabara,K., Hirota,S., Ikeda,J., Stern,D.,
            Yanagi,H., Matsumoto,M., Ogawa,S. and Kitamura,Y.
  TITLE     150-kD oxygen-regulated protein is expressed in human
            atherosclerotic plaques and allows mononuclear phagocytes to
            withstand cellular stress on exposure to hypoxia and modified low
            density lipoprotein
  JOURNAL   J Clin Invest 98 (8), 1930-1941 (1996)
   PUBMED   8878445
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY089857.1, DC364982.1,
            U65785.1, AK301514.1, AK127324.1, BC072436.1 and AA580314.1.
            
            Summary: The protein encoded by this gene belongs to the heat shock
            protein 70 family. This gene uses alternative transcription start
            sites. A cis-acting segment found in the 5' UTR is involved in
            stress-dependent induction, resulting in the accumulation of this
            protein in the endoplasmic reticulum (ER) under hypoxic conditions.
            The protein encoded by this gene is thought to play an important
            role in protein folding and secretion in the ER. Since suppression
            of the protein is associated with accelerated apoptosis, it is also
            suggested to have an important cytoprotective role in
            hypoxia-induced cellular perturbation. This protein has been shown
            to be up-regulated in tumors, especially in breast tumors, and thus
            it is associated with tumor invasiveness. This gene also has an
            alternative translation initiation site, resulting in a protein
            that lacks the N-terminal signal peptide. This signal
            peptide-lacking protein, which is only 3 amino acids shorter than
            the mature protein in the ER, is thought to have a housekeeping
            function in the cytosol. In rat, this protein localizes to both the
            ER by a carboxy-terminal peptide sequence and to mitochondria by an
            amino-terminal targeting signal. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U65785.1, SRR1660809.146826.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000617285.5/ ENSP00000480150.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..999
                     /product="hypoxia up-regulated protein 1 isoform 1
                     precursor"
                     /note="oxygen regulated protein (150kD); hypoxia
                     up-regulated protein 1; 150 kDa oxygen-regulated protein;
                     170 kDa glucose-regulated protein; epididymis secretory
                     sperm binding protein; heat shock protein family H member
                     4"
                     /calculated_mol_wt=107660
     sig_peptide     1..32
                     /note="/evidence=ECO:0007744|PubMed:25944712; propagated
                     from UniProtKB/Swiss-Prot (Q9Y4L1.1)"
                     /calculated_mol_wt=3693
     mat_peptide     33..999
                     /product="Hypoxia up-regulated protein 1.
                     /id=PRO_0000013538"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4L1.1)"
                     /calculated_mol_wt=107660
     Region          34..424
                     /region_name="ASKHA_NBD_HSP70_HYOU1"
                     /note="nucleotide-binding domain (NBD) of hypoxia
                     up-regulated protein 1 (HYOU1) and similar proteins;
                     cd10230"
                     /db_xref="CDD:466828"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Site            515
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973;
                     propagated from UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Region          578..694
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Region          <593..694
                     /region_name="LGT"
                     /note="Prolipoprotein diacylglyceryl transferase; cl00478"
                     /db_xref="CDD:469786"
     Site            596
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Site            830
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Site            862
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Site            869
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Site            883
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKR6; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Region          909..999
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Site            922
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Site            931
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     Region          996..999
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4L1.1)"
     CDS             1..999
                     /gene="HYOU1"
                     /gene_synonym="GRP-170; Grp170; HSP12A; IMD59; ORP-150;
                     ORP150"
                     /coded_by="NM_006389.5:194..3193"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8408.1"
                     /db_xref="GeneID:10525"
                     /db_xref="HGNC:HGNC:16931"
                     /db_xref="MIM:601746"
ORIGIN      
        1 madkvrrqrp rrrvcwalva vlladllals dtlavmsvdl gsesmkvaiv kpgvpmeivl
       61 nkesrrktpv ivtlkenerf fgdsaasmai knpkatlryf qhllgkqadn phvalyqarf
      121 peheltfdpq rqtvhfqiss qlqfspeevl gmvlnysrsl aedfaeqpik davitvpvff
      181 nqaerravlq aarmaglkvl qlindntata lsygvfrrkd inttaqnimf ydmgsgstvc
      241 tivtyqmvkt keagmqpqlq irgvgfdrtl gglemelrlr erlaglfneq rkgqrakdvr
      301 enpramakll reanrlktvl sanadhmaqi eglmddvdfk akvtrvefee lcadlfervp
      361 gpvqqalqsa emsldeieqv ilvggatrvp rvqevllkav gkeelgknin adeaaamgav
      421 yqaaalskaf kvkpfvvrda vvypilveft reveeepgih slkhnkrvlf srmgpypqrk
      481 vitfnryshd fnfhinygdl gflgpedlrv fgsqnlttvk lkgvgdsfkk ypdyeskgik
      541 ahfnldesgv lsldrvesvf etlvedsaee estltklgnt isslfgggtt pdakengtdt
      601 vqeeeespae gskdepgeqv elkeeaeapv edgsqppppe pkgdatpege katekengdk
      661 seaqkpseka eagpegvapa pegekkqkpa rkrrmveeig velvvldlpd lpedklaqsv
      721 qklqdltlrd lekqerekaa nsleafifet qdklyqpeyq evsteeqree isgklsaast
      781 wledegvgat tvmlkeklae lrklcqglff rveerkkwpe rlsaldnlln hssmflkgar
      841 lipemdqift evemttlekv inetwawkna tlaeqaklpa tekpvllskd ieakmmaldr
      901 evqyllnkak ftkprprpkd kngtraeppl nasasdqgek vippagqted aepisepekv
      961 etgsepgdte plelggpgae peqkeqstgq krplkndel
//
LOCUS       NP_001258554              81 aa            linear   MAM 27-APR-2025
DEFINITION  alternative prion protein isoform AltPrp [Bos taurus].
ACCESSION   NP_001258554
VERSION     NP_001258554.1
DBSOURCE    REFSEQ: accession NM_001271625.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Pimenta,J.M.B.G.A., Pires,V.M.R., Nolasco,S., Castelo-Branco,P.,
            Marques,C.C., Apolonio,J., Azevedo,R., Fernandes,M.T.,
            Lopes-da-Costa,L., Prates,J. and Pereira,R.M.L.N.
  TITLE     Post-transcriptional silencing of Bos taurus prion family genes and
            its impact on granulosa cell steroidogenesis
  JOURNAL   Biochem Biophys Res Commun 598, 95-99 (2022)
   PUBMED   35151978
  REMARK    GeneRIF: Post-transcriptional silencing of Bos taurus prion family
            genes and its impact on granulosa cell steroidogenesis.
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Ashok,A., Kang,M.H., Wise,A.S., Pattabiraman,P., Johnson,W.M.,
            Lonigro,M., Ravikumar,R., Rhee,D.J. and Singh,N.
  TITLE     Prion protein modulates endothelial to mesenchyme-like transition
            in trabecular meshwork cells: Implications for primary open angle
            glaucoma
  JOURNAL   Sci Rep 9 (1), 13090 (2019)
   PUBMED   31511544
  REMARK    GeneRIF: Prion protein modulates endothelial to mesenchyme-like
            transition in trabecular meshwork cells: Implications for primary
            open angle glaucoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Memon,S., Li,G., Xiong,H., Wang,L., Liu,X.Y., Yuan,M., Deng,W. and
            Xi,D.
  TITLE     Deletion/insertion polymorphisms of the prion protein gene (PRNP)
            in gayal (Bos frontalis)
  JOURNAL   J Genet 97 (5), 1131-1138 (2018)
   PUBMED   30555062
  REMARK    GeneRIF: Deletion/insertion polymorphisms of the PRNP gene is
            associated with bovine spongiformencephalopathy.
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Vrentas,C.E., Greenlee,J.J., Foster,G.H., West,J., Jahnke,M.M.,
            Schmidt,M.T. and Nicholson,E.M.
  TITLE     Effects of a naturally occurring amino acid substitution in bovine
            PrP: a model for inherited prion disease in a natural host species
  JOURNAL   BMC Res Notes 10 (1), 759 (2017)
   PUBMED   29262866
  REMARK    GeneRIF: Data suggest that the E211K prion protein provides the
            opportunity for future analysis of physiological changes over time.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 81)
  AUTHORS   Vazquez-Fernandez,E., Vos,M.R., Afanasyev,P., Cebey,L.,
            Sevillano,A.M., Vidal,E., Rosa,I., Renault,L., Ramos,A.,
            Peters,P.J., Fernandez,J.J., van Heel,M., Young,H.S., Requena,J.R.
            and Wille,H.
  TITLE     The Structural Architecture of an Infectious Mammalian Prion Using
            Electron Cryomicroscopy
  JOURNAL   PLoS Pathog 12 (9), e1005835 (2016)
   PUBMED   27606840
  REMARK    GeneRIF: the data indicate a four-rung beta-solenoid structure as a
            key feature for the architecture of infectious mammalian prions.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 81)
  AUTHORS   Vanderperre,B., Staskevicius,A.B., Tremblay,G., McCoy,M.,
            O'Neill,M.A., Cashman,N.R. and Roucou,X.
  TITLE     An overlapping reading frame in the PRNP gene encodes a novel
            polypeptide distinct from the prion protein
  JOURNAL   FASEB J 25 (7), 2373-2386 (2011)
   PUBMED   21478263
REFERENCE   7  (residues 1 to 81)
  AUTHORS   Prusiner,S.B., Fuzi,M., Scott,M., Serban,D., Serban,H.,
            Taraboulos,A., Gabriel,J.M., Wells,G.A., Wilesmith,J.W., Bradley,R.
            et al.
  TITLE     Immunologic and molecular biologic studies of prion proteins in
            bovine spongiform encephalopathy
  JOURNAL   J Infect Dis 167 (3), 602-613 (1993)
   PUBMED   8440932
REFERENCE   8  (residues 1 to 81)
  AUTHORS   Yoshimoto,J., Iinuma,T., Ishiguro,N., Horiuchi,M., Imamura,M. and
            Shinagawa,M.
  TITLE     Comparative sequence analysis and expression of bovine PrP gene in
            mouse L-929 cells
  JOURNAL   Virus Genes 6 (4), 343-356 (1992)
   PUBMED   1362024
REFERENCE   9  (residues 1 to 81)
  AUTHORS   Goldmann,W., Hunter,N., Martin,T., Dawson,M. and Hope,J.
  TITLE     Different forms of the bovine PrP gene have five or six copies of a
            short, G-C-rich element within the protein-coding exon
  JOURNAL   J Gen Virol 72 (Pt 1), 201-204 (1991)
   PUBMED   1671225
REFERENCE   10 (residues 1 to 81)
  AUTHORS   Hope,J., Reekie,L.J., Hunter,N., Multhaup,G., Beyreuther,K.,
            White,H., Scott,A.C., Stack,M.J., Dawson,M. and Wells,G.A.
  TITLE     Fibrils from brains of cows with new cattle disease contain
            scrapie-associated protein
  JOURNAL   Nature 336 (6197), 390-392 (1988)
   PUBMED   2904126
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000013.1.
            
            Transcript Variant: This variant (3) encodes a shorter protein from
            an overlapping reading frame, compared to variant 1. Alternative
            prion protein (AltPrp) has no similarity to the other protein
            encoded by this gene and localizes to the outer mitochondrial
            membrane.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB001468.1, SRR5571258.4178.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA6648753, SAMEA6648754
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="13"
                     /map="13"
                     /breed="Hereford"
     Protein         1..81
                     /product="alternative prion protein isoform AltPrp"
                     /note="major prion protein; prion protein precursor PrP;
                     prion protein PrP; major scrapie-associated fibril protein
                     1; prion protein (p27-30) (Creutzfeldt-Jakob disease,
                     Gerstmann-Strausler-Scheinker syndrome, fatal familial
                     insomnia); alternative prion protein"
                     /calculated_mol_wt=9632
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F7VJQ2.1)"
     Site            50..66
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (F7VJQ2.1)"
     CDS             1..81
                     /gene="PRNP"
                     /gene_synonym="AltPrP; prn; PrP"
                     /coded_by="NM_001271625.3:281..526"
                     /note="isoform AltPrp is encoded by transcript variant 3"
                     /db_xref="BGD:BT10271"
                     /db_xref="GeneID:281427"
                     /db_xref="VGNC:VGNC:33356"
ORIGIN      
        1 mehwgepipr tgqswrqpls tsgrgwlgsa pwrwlgpasw rwlgpaswrw lgsapwwwlg
       61 tatwwwrlgs rwyprsmeqt q
//
LOCUS       NP_067274                227 aa            linear   ROD 27-APR-2025
DEFINITION  GTP:AMP phosphotransferase AK3, mitochondrial isoform 1 [Mus
            musculus].
ACCESSION   NP_067274
VERSION     NP_067274.1
DBSOURCE    REFSEQ: accession NM_021299.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Noma,T., Fujisawa,K., Yamashiro,Y., Shinohara,M., Nakazawa,A.,
            Gondo,T., Ishihara,T. and Yoshinobu,K.
  TITLE     Structure and expression of human mitochondrial adenylate kinase
            targeted to the mitochondrial matrix
  JOURNAL   Biochem J 358 (Pt 1), 225-232 (2001)
   PUBMED   11485571
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Bonhomme,F., Catalan,J., Britton-Davidian,J., Chapman,V.M.,
            Moriwaki,K., Nevo,E. and Thaler,L.
  TITLE     Biochemical diversity and evolution in the genus Mus
  JOURNAL   Biochem Genet 22 (3-4), 275-303 (1984)
   PUBMED   6375655
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK147060.1 and AW457236.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC058191.1, AK147060.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849382, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 23.61 cM"
     Protein         1..227
                     /product="GTP:AMP phosphotransferase AK3, mitochondrial
                     isoform 1"
                     /EC_number="2.7.4.10"
                     /note="adenylate kinase 3 alpha-like 1; GTP:AMP
                     phosphotransferase AK3, mitochondrial"
                     /calculated_mol_wt=25295
     Region          12..190
                     /region_name="ADK"
                     /note="Adenylate kinase; pfam00406"
                     /db_xref="CDD:395329"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9WTP7.3)"
     Site            34
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9WTP7.3)"
     Region          37..66
                     /region_name="NMP.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03169"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTP7.3)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WTP7.3)"
     Site            64
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9WTP7.3)"
     Site            80
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9WTP7.3)"
     Region          127..164
                     /region_name="LID.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03169"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTP7.3)"
     Site            174
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9WTP7.3)"
     Site            189
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9WTP7.3)"
     Site            203
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9WTP7.3)"
     CDS             1..227
                     /gene="Ak3"
                     /gene_synonym="AK-3; Ak3l; Ak3l1; Akl3l"
                     /coded_by="NM_021299.2:133..816"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS29730.1"
                     /db_xref="GeneID:56248"
                     /db_xref="MGI:MGI:1860835"
ORIGIN      
        1 mgasgrllra vimgapgsgk gtvssritkh felkhlssgd llrqnmlqgt eigvlaktfi
       61 dqgklipddv mtrlalhelk tltqcswlld gfprtlpqae aldkvyqidt vinlnvpfev
      121 ikqrltarwi hpasgrvyni efnppktvgi ddltgepliq reddkpetvi krlkayeaqt
      181 epvlqyyqkk gvletfsgte tnkiwphvys flqtkvpett qkasvtp
//
LOCUS       NP_003078                127 aa            linear   PRI 27-APR-2025
DEFINITION  gamma-synuclein isoform 1 [Homo sapiens].
ACCESSION   NP_003078
VERSION     NP_003078.2
DBSOURCE    REFSEQ: accession NM_003087.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Yang,H.M., Cheng,Y.Z., Hou,T.Z., Fan,J.K., Gu,L., Zhang,J.N. and
            Zhang,H.
  TITLE     Upregulation of Parkinson's disease-associated protein
            alpha-synuclein suppresses tumorigenesis via interaction with
            mGluR5 and gamma-synuclein in liver cancer
  JOURNAL   Arch Biochem Biophys 744, 109698 (2023)
   PUBMED   37487948
  REMARK    GeneRIF: Upregulation of Parkinson's disease-associated protein
            alpha-synuclein suppresses tumorigenesis via interaction with
            mGluR5 and gamma-synuclein in liver cancer.
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Li,J., Li,P., Li,J., Yang,H., Liu,G., Shen,P. and Jiang,G.
  TITLE     Effects of the Methylation Levels for the Breast Cancer Associated
            Genes BCSG1 and BRCA1 on Cellular Proliferation and Migration
  JOURNAL   Genet Test Mol Biomarkers 26 (9), 422-429 (2022)
   PUBMED   36166741
  REMARK    GeneRIF: Effects of the Methylation Levels for the Breast Cancer
            Associated Genes BCSG1 and BRCA1 on Cellular Proliferation and
            Migration.
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Liu,J., Shao,T., Zhang,J., Liu,Q., Hua,H., Zhang,H., Wang,J.,
            Luo,T., Shi,Y.E. and Jiang,Y.
  TITLE     Gamma synuclein promotes cancer metastasis through the
            MKK3/6-p38MAPK cascade
  JOURNAL   Int J Biol Sci 18 (8), 3167-3177 (2022)
   PUBMED   35637967
  REMARK    GeneRIF: Gamma synuclein promotes cancer metastasis through the
            MKK3/6-p38MAPK cascade.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Yang,J., Pan,Y., Peng,L., Zhang,L., Zhao,J., Zheng,Z., Zheng,J.,
            Xu,X. and Zeng,Y.
  TITLE     Upregulation of Synuclein-gamma and Snai1 Contributes to Poor
            Clinical Prognosis in Oral Squamous Cell Carcinoma Patients
  JOURNAL   Biomed Res Int 2022, 6534626 (2022)
   PUBMED   35434126
  REMARK    GeneRIF: Upregulation of Synuclein-gamma and Snai1 Contributes to
            Poor Clinical Prognosis in Oral Squamous Cell Carcinoma Patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Zhang,L., Yang,X., Tian,Y., Yu,Q., Zhou,D., Wu,Z. and Zhao,X.
  TITLE     Noninvasive Detection of Esophageal Cancer by the Combination of
            mSEPT9 and SNCG
  JOURNAL   Genet Test Mol Biomarkers 26 (1), 8-16 (2022)
   PUBMED   35089073
  REMARK    GeneRIF: Noninvasive Detection of Esophageal Cancer by the
            Combination of mSEPT9 and SNCG.
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Lavedan,C., Buchholtz,S., Auburger,G., Albin,R.L.,
            Athanassiadou,A., Blancato,J., Burguera,J.A., Ferrell,R.E.,
            Kostic,V., Leroy,E., Leube,B., Mota-Vieira,L., Papapetropoulos,T.,
            Pericak-Vance,M.A., Pinkus,J., Scott,W.K., Ulm,G., Vasconcelos,J.,
            Vilchez,J.J., Nussbaum,R.L. and Polymeropoulos,M.H.
  TITLE     Absence of mutation in the beta- and gamma-synuclein genes in
            familial autosomal dominant Parkinson's disease
  JOURNAL   DNA Res 5 (6), 401-402 (1998)
   PUBMED   10048491
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Buchman,V.L., Hunter,H.J., Pinon,L.G., Thompson,J., Privalova,E.M.,
            Ninkina,N.N. and Davies,A.M.
  TITLE     Persyn, a member of the synuclein family, has a distinct pattern of
            expression in the developing nervous system
  JOURNAL   J Neurosci 18 (22), 9335-9341 (1998)
   PUBMED   9801372
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Ninkina,N.N., Alimova-Kost,M.V., Paterson,J.W., Delaney,L.,
            Cohen,B.B., Imreh,S., Gnuchev,N.V., Davies,A.M. and Buchman,V.L.
  TITLE     Organization, expression and polymorphism of the human persyn gene
  JOURNAL   Hum Mol Genet 7 (9), 1417-1424 (1998)
   PUBMED   9700196
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Lavedan,C., Leroy,E., Dehejia,A., Buchholtz,S., Dutra,A.,
            Nussbaum,R.L. and Polymeropoulos,M.H.
  TITLE     Identification, localization and characterization of the human
            gamma-synuclein gene
  JOURNAL   Hum Genet 103 (1), 106-112 (1998)
   PUBMED   9737786
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Ji,H., Liu,Y.E., Jia,T., Wang,M., Liu,J., Xiao,G., Joseph,B.K.,
            Rosen,C. and Shi,Y.E.
  TITLE     Identification of a breast cancer-specific gene, BCSG1, by direct
            differential cDNA sequencing
  JOURNAL   Cancer Res 57 (4), 759-764 (1997)
   PUBMED   9044857
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK223367.1 and BC014098.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 17, 2008 this sequence version replaced NP_003078.1.
            
            Summary: This gene encodes a member of the synuclein family of
            proteins which are believed to be involved in the pathogenesis of
            neurodegenerative diseases. Mutations in this gene have also been
            associated with breast tumor development. [provided by RefSeq, Jan
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ221776.1, AF017256.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372017.4/ ENSP00000361087.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.2"
     Protein         1..127
                     /product="gamma-synuclein isoform 1"
                     /note="persyn; synoretin; gamma-synuclein; breast
                     cancer-specific gene 1 protein; synuclein, gamma (breast
                     cancer-specific protein 1); E pound-synuclein; -synuclein"
                     /calculated_mol_wt=13200
     Region          1..112
                     /region_name="Synuclein"
                     /note="pfam01387"
                     /db_xref="CDD:460186"
     Region          20..67
                     /region_name="4 X 11 AA tandem repeats of
                     [EGSA]-K-T-K-[EQ]-[GQ]-V-X(4)"
                     /note="propagated from UniProtKB/Swiss-Prot (O76070.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63544; propagated from
                     UniProtKB/Swiss-Prot (O76070.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63544; propagated from
                     UniProtKB/Swiss-Prot (O76070.2)"
     Region          96..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O76070.2)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by BARK1, CaMK2 and CK2.
                     /evidence=ECO:0000269|PubMed:10852916; propagated from
                     UniProtKB/Swiss-Prot (O76070.2)"
     CDS             1..127
                     /gene="SNCG"
                     /gene_synonym="BCSG1; SR"
                     /coded_by="NM_003087.3:100..483"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7380.1"
                     /db_xref="GeneID:6623"
                     /db_xref="HGNC:HGNC:11141"
                     /db_xref="MIM:602998"
ORIGIN      
        1 mdvfkkgfsi akegvvgave ktkqgvteaa ektkegvmyv gaktkenvvq svtsvaektk
       61 eqanavseav vssvntvatk tveeaeniav tsgvvrkedl rpsapqqege askekeevae
      121 eaqsggd
//
LOCUS       NP_065934               1185 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger SWIM domain-containing protein 5 [Homo sapiens].
ACCESSION   NP_065934 XP_046581 XP_946519
VERSION     NP_065934.1
DBSOURCE    REFSEQ: accession NM_020883.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1185)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL592294.15, CN429257.1, AB040944.1, BC013836.1, BM711793.1 and
            AL359473.22.
            
            On or before Jun 29, 2007 this sequence version replaced
            XP_046581.8, XP_946519.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB040944.1, SRR1803616.54229.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359600.6/ ENSP00000352614.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1185
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..1185
                     /product="zinc finger SWIM domain-containing protein 5"
                     /note="zinc finger, SWIM domain containing 5"
                     /calculated_mol_wt=130503
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P217.2)"
     Region          123..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P217.2)"
     Region          180..>291
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
     CDS             1..1185
                     /gene="ZSWIM5"
                     /coded_by="NM_020883.2:256..3813"
                     /db_xref="CCDS:CCDS41319.1"
                     /db_xref="GeneID:57643"
                     /db_xref="HGNC:HGNC:29299"
                     /db_xref="MIM:620132"
ORIGIN      
        1 madggereel lspspvspak rqcswpspqa hhprgspgaa gggaggvgss clvlgarphl
       61 qpdslldcaa ktvaekwaye rveerferip epvqrrivyw sfprnereic myssfqyrgg
      121 pgagaaggaa gaspaeegpq pppgaaapag sapggvaaga spglgagaga agcggeglpf
      181 rrgirlldsg svenvlqvgf hlsgtvtela tasepavtyk vaisfdrcki tsvtcgcgnk
      241 difycahvva lslyrirkpd qvklrlpise tlfqmnrdql qkfiqylita hhtevlptaq
      301 kladeilssn seinqvngap dptagasidd encwhldeeq vkeqvklfls qggycgsgkq
      361 lnsmfakvre mlrmrdsnga rmltliteqf vadprltlwr qqgtnmtdkc rqlwdelgal
      421 wvciilnphc kleekscwlq qlqkwsdldv cpledgnygh elpnitnalp qsaihspdsl
      481 srprrtvftr aiegrelhwq dshlqriiss dvytapacqr eserllfnsq gqplwlehvp
      541 tacarvdalr shgypkealr ltvaiintlr lqqqrqleiy khqkkellqr gtttitnleg
      601 wvghpldpid clfltlteac rlnddgylem sdmnesrppv yqhvpvaags pnssesylsl
      661 alevalmglg qqrlmpegly aqdkvcrnee qllsqlqelq lddelvqtlq kqcilllegg
      721 pfsglgevih resvpmhtfa kylfsallph dpdlsyklal ramrlpvlen sasagdtshp
      781 hhmvsvvpsr yprwftlghl esqqcelast mltaakgdtl rlrtileaiq khihssslif
      841 klaqdafkia tptdsstdst llnvalelgl qvmrmtlstl nwrrremvrw lvtcatevgv
      901 ralvsilqsw ytlftpteat sivaatavsh ttilrlsldy pqreelasca rtlalqcamk
      961 dpqscalsal tlcekdhiaf eaayqiaida aaggmthsql ftiarymelr gyplrafkla
     1021 slamshlnla ynqdthpain dvlwacalsh slgknelaal iplvvksvhc atvlsdilrr
     1081 ctvtapglag ipgrrssgkl mstdkaplrq lldatinayi ntthsrlthi sprhygefie
     1141 flskaretfl lpqdghlqfa qfidnlkqiy kgkkklmllv rerfg
//
LOCUS       NP_015628               1119 aa            linear   PRI 27-APR-2025
DEFINITION  transient receptor potential cation channel subfamily A member 1
            [Homo sapiens].
ACCESSION   NP_015628
VERSION     NP_015628.2
DBSOURCE    REFSEQ: accession NM_007332.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Matsubara,M., Muraki,Y., Suzuki,H., Hatano,N. and Muraki,K.
  TITLE     Critical amino acid residues regulating TRPA1 Zn2+ response: A
            comparative study across species
  JOURNAL   J Biol Chem 300 (6), 107302 (2024)
   PUBMED   38642892
  REMARK    GeneRIF: Critical amino acid residues regulating TRPA1 Zn[2+]
            response: A comparative study across species.
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Sanchez,J.C., Aleman,A., Henao,J.F., Olaya,J.C. and Ehrlich,B.E.
  TITLE     NCS-1 protein regulates TRPA1 channel through the PI3K pathway in
            breast cancer and neuronal cells
  JOURNAL   J Physiol Biochem 80 (2), 451-463 (2024)
   PUBMED   38564162
  REMARK    GeneRIF: NCS-1 protein regulates TRPA1 channel through the PI3K
            pathway in breast cancer and neuronal cells.
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Xu,F., Jiang,H., Li,X., Pan,J., Li,H., Wang,L., Zhang,P., Chen,J.,
            Qiu,S., Xie,Y., Li,Y., Zhang,D. and Dong,Z.
  TITLE     Discovery of PRDM16-Mediated TRPA1 Induction as the Mechanism for
            Low Tubulo-Interstitial Fibrosis in Diabetic Kidney Disease
  JOURNAL   Adv Sci (Weinh) 11 (7), e2306704 (2024)
   PUBMED   38072665
  REMARK    GeneRIF: Discovery of PRDM16-Mediated TRPA1 Induction as the
            Mechanism for Low Tubulo-Interstitial Fibrosis in Diabetic Kidney
            Disease.
REFERENCE   4  (residues 1 to 1119)
  AUTHORS   Kim,M.S. and Simons,C.T.
  TITLE     The role of TRPA1 and TRPV1 in the perception of astringency
  JOURNAL   Chem Senses 49 (2024)
   PUBMED   39223911
  REMARK    GeneRIF: The role of TRPA1 and TRPV1 in the perception of
            astringency.
REFERENCE   5  (residues 1 to 1119)
  AUTHORS   Vlachova,V., Barvik,I. and Zimova,L.
  TITLE     Human Transient Receptor Potential Ankyrin 1 Channel: Structure,
            Function, and Physiology
  JOURNAL   Subcell Biochem 104, 207-244 (2024)
   PUBMED   38963489
  REMARK    GeneRIF: Human Transient Receptor Potential Ankyrin 1 Channel:
            Structure, Function, and Physiology.
            Review article
REFERENCE   6  (residues 1 to 1119)
  AUTHORS   Stokes,A., Wakano,C., Koblan-Huberson,M., Adra,C.N., Fleig,A. and
            Turner,H.
  TITLE     TRPA1 is a substrate for de-ubiquitination by the tumor suppressor
            CYLD
  JOURNAL   Cell Signal 18 (10), 1584-1594 (2006)
   PUBMED   16500080
  REMARK    GeneRIF: TRPA1 is a novel substrate for the de-ubiquitinating
            activity of CYLD, and this de-ubiquitination has the net effect of
            increasing the cellular pool of TRPA1 proteins.
REFERENCE   7  (residues 1 to 1119)
  AUTHORS   Clapham,D.E., Julius,D., Montell,C. and Schultz,G.
  TITLE     International Union of Pharmacology. XLIX. Nomenclature and
            structure-function relationships of transient receptor potential
            channels
  JOURNAL   Pharmacol Rev 57 (4), 427-450 (2005)
   PUBMED   16382100
  REMARK    Review article
REFERENCE   8  (residues 1 to 1119)
  AUTHORS   Jordt,S.E., Bautista,D.M., Chuang,H.H., McKemy,D.D., Zygmunt,P.M.,
            Hogestatt,E.D., Meng,I.D. and Julius,D.
  TITLE     Mustard oils and cannabinoids excite sensory nerve fibres through
            the TRP channel ANKTM1
  JOURNAL   Nature 427 (6971), 260-265 (2004)
   PUBMED   14712238
  REMARK    GeneRIF: cellular and molecular target for the pungent action of
            mustard oils; support an emerging role for TRP channel ANKTM1 as an
            ionotropic cannabinoid receptor
REFERENCE   9  (residues 1 to 1119)
  AUTHORS   Jaquemar,D., Schenker,T. and Trueb,B.
  TITLE     An ankyrin-like protein with transmembrane domains is specifically
            lost after oncogenic transformation of human fibroblasts
  JOURNAL   J Biol Chem 274 (11), 7325-7333 (1999)
   PUBMED   10066796
REFERENCE   10 (residues 1 to 1119)
  AUTHORS   Schenker,T. and Trueb,B.
  TITLE     Down-regulated proteins of mesenchymal tumor cells
  JOURNAL   Exp Cell Res 239 (1), 161-168 (1998)
   PUBMED   9511734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016057.6 and AC022867.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 24, 2006 this sequence version replaced NP_015628.1.
            
            Summary: The structure of the protein encoded by this gene is
            highly related to both the protein ankyrin and transmembrane
            proteins.  The specific function of this protein has not yet been
            determined; however, studies indicate the function may involve a
            role in signal transduction and growth control. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y10601.1, SRR14038197.2696851.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262209.5/ ENSP00000262209.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..1119
                     /product="transient receptor potential cation channel
                     subfamily A member 1"
                     /note="ankyrin-like with transmembrane domains 1;
                     transformation-sensitive protein p120; wasabi receptor"
                     /calculated_mol_wt=127371
     Region          47..343
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          62..92
                     /region_name="ANK 1. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          67..95
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(97,99,103..104,107..109,111..112,116,119,128,130,
                     132,136..137,140..142,144..145,149,152,162,164,166,
                     170..171,174..176,178..179,183,186)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          97..128
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          97..126
                     /region_name="ANK 2. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          130..162
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          130..160
                     /region_name="ANK 3. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          164..193
                     /region_name="ANK 4. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          164..189
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          197..236
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          197..226
                     /region_name="ANK 5. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          229..519
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          238..267
                     /region_name="ANK 6. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          241..269
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(244..245,248..250,252..253,257,260,269,271,273,
                     277..278,281..283,285..286,290,330,339,341,343,347..348,
                     351..353,355..356,360,363,372)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          271..339
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          271..301
                     /region_name="ANK 7. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          308..337
                     /region_name="ANK 8. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          341..372
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          341..370
                     /region_name="ANK 9. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          374..403
                     /region_name="ANK 10.
                     /evidence=ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Site            394
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline, by EGLN1, transient, in normoxia
                     and hyperoxia. /evidence=ECO:0000269|PubMed:21873995;
                     propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          412..443
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          412..441
                     /region_name="ANK 11. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          445..479
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          445..474
                     /region_name="ANK 12. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Site            order(481,483,487..488,491..493,495..496,500,503,511,513,
                     515,519..520,523..525,527..528,532,535,545,547,549,
                     553..554,557..559,561..562,566,569)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          481..511
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          481..510
                     /region_name="ANK 13. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          486..577
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          513..545
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          513..542
                     /region_name="ANK 14. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          547..576
                     /region_name="ANK 15. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          547..572
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          579..609
                     /region_name="ANK 16. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:25855297"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Site            620
                     /site_type="other"
                     /note="Required for C-621 reactivity.
                     /evidence=ECO:0000269|PubMed:27241698; propagated from
                     UniProtKB/Swiss-Prot (O75762.3)"
     Site            621
                     /site_type="other"
                     /note="Essential for electrophile activation. Sensor for
                     electrophilic agents.
                     /evidence=ECO:0000269|PubMed:31866091,
                     ECO:0000269|PubMed:32641835; propagated from
                     UniProtKB/Swiss-Prot (O75762.3)"
     Site            622
                     /site_type="other"
                     /note="Key residue for activation by the scorpion wasabi
                     receptor toxin. /evidence=ECO:0000269|PubMed:31447178;
                     propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Site            634
                     /site_type="other"
                     /note="Important residue for activation by the scorpion
                     wasabi receptor toxin.
                     /evidence=ECO:0000269|PubMed:31447178; propagated from
                     UniProtKB/Swiss-Prot (O75762.3)"
     Site            646
                     /site_type="other"
                     /note="Important residue for activation by the scorpion
                     wasabi receptor toxin.
                     /evidence=ECO:0000269|PubMed:31447178; propagated from
                     UniProtKB/Swiss-Prot (O75762.3)"
     Site            665
                     /site_type="other"
                     /note="Important for electrophile activation.
                     /evidence=ECO:0000269|PubMed:31866091,
                     ECO:0000269|PubMed:32641835; propagated from
                     UniProtKB/Swiss-Prot (O75762.3)"
     Site            719..739
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Site            747
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75762.3)"
     Site            753
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75762.3)"
     Site            768..793
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Region          <796..972
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            799..823
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Site            830..850
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Site            863..892
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     Site            915
                     /site_type="other"
                     /note="Crucial for calcium permeation.
                     /evidence=ECO:0000250|UniProtKB:Q6RI86; propagated from
                     UniProtKB/Swiss-Prot (O75762.3)"
     Site            934..960
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75762.3)"
     CDS             1..1119
                     /gene="TRPA1"
                     /gene_synonym="ANKTM1; FEPS; FEPS1; p120"
                     /coded_by="NM_007332.3:176..3535"
                     /db_xref="CCDS:CCDS34908.1"
                     /db_xref="GeneID:8989"
                     /db_xref="HGNC:HGNC:497"
                     /db_xref="MIM:604775"
ORIGIN      
        1 mkrslrkmwr pgekkepqgv vyedvpddte dfkeslkvvf egsayglqnf nkqkklkrcd
       61 dmdtfflhya aaegqielme kitrdsslev lhemddygnt plhcaveknq iesvkfllsr
      121 ganpnlrnfn mmaplhiavq gmnnevmkvl lehrtidvnl egengntavi iacttnnsea
      181 lqillkkgak pcksnkwgcf pihqaafsgs kecmeiilrf geehgysrql hinfmnngka
      241 tplhlavqng dlemikmcld ngaqidpvek grctaihfaa tqgateivkl missysgsvd
      301 ivnttdgche tmlhraslfd hheladylis vgadinkids egrsplilat asaswnivnl
      361 llskgaqvdi kdnfgrnflh ltvqqpyglk nlrpefmqmq qikelvmded ndgctplhya
      421 crqggpgsvn nllgfnvsih skskdkkspl hfaasygrin tcqrllqdis dtrllnegdl
      481 hgmtplhlaa knghdkvvql llkkgalfls dhngwtalhh asmggytqtm kvildtnlkc
      541 tdrldedgnt alhfaaregh akavalllsh nadivlnkqq asflhlalhn krkevvltii
      601 rskrwdeclk ifshnspgnk cpitemieyl pecmkvlldf cmlhstedks crdyyieynf
      661 kylqcpleft kktptqdviy epltalnamv qnnriellnh pvckeyllmk wlaygfrahm
      721 mnlgsyclgl ipmtilvvni kpgmafnstg iinetsdhse ildttnsyli ktcmilvfls
      781 sifgyckeag qifqqkrnyf mdisnvlewi iyttgiifvl plfveipahl qwqcgaiavy
      841 fywmnfllyl qrfencgifi vmlevilktl lrstvvfifl llafglsfyi llnlqdpfss
      901 pllsiiqtfs mmlgdinyre sflepylrne lahpvlsfaq lvsftifvpi vlmnlligla
      961 vgdiaevqkh aslkriamqv elhtslekkl plwflrkvdq kstivypnkp rsggmlfhif
     1021 cflfctgeir qeipnadksl emeilkqkyr lkdltfllek qhelikliiq kmeiiseted
     1081 ddshcsfqdr fkkeqmeqrn srwntvlrav kakthhlep
//
LOCUS       NP_001346912             668 aa            linear   ROD 27-APR-2025
DEFINITION  sperm-associated antigen 1 isoform 2 [Mus musculus].
ACCESSION   NP_001346912 XP_017172126
VERSION     NP_001346912.1
DBSOURCE    REFSEQ: accession NM_001359983.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Huang,C., Wu,D., Khan,F.A., Jiao,X., Guan,K. and Huo,L.
  TITLE     The GTPase SPAG-1 orchestrates meiotic program by dictating meiotic
            resumption and cytoskeleton architecture in mouse oocytes
  JOURNAL   Mol Biol Cell 27 (11), 1776-1785 (2016)
   PUBMED   27053660
  REMARK    GeneRIF: Findings broaden our knowledge of SPAG-1, showing that it
            exerts a role in oocyte meiotic execution via its involvement in
            AMPK and MAPK signaling pathways.
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Hayashida,K., Omagari,K., Masuda,J. and Kohno,S.
  TITLE     An integrase of endogenous retrovirus is involved in maternal
            mitochondrial DNA inheritance of the mouse
  JOURNAL   Biochem Biophys Res Commun 366 (1), 206-211 (2008)
   PUBMED   18054325
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Hayashida,K., Omagari,K., Masuda,J., Hazama,H., Kadokawa,Y.,
            Ohba,K. and Kohno,S.
  TITLE     The sperm mitochondria-specific translocator has a key role in
            maternal mitochondrial inheritance
  JOURNAL   Cell Biol Int 29 (6), 472-481 (2005)
   PUBMED   15979907
  REMARK    GeneRIF: The number of PCR positives of sperm mtDNA in two-cell
            embryos was significantly increased following sperm incubation with
            anti-tetratricopeptide repeat-containing protein involved in
            spermatogenesis (tpis).
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Yamashita,H., Avraham,S., Jiang,S., London,R., Van Veldhoven,P.P.,
            Subramani,S., Rogers,R.A. and Avraham,H.
  TITLE     Characterization of human and murine PMP20 peroxisomal proteins
            that exhibit antioxidant activity in vitro
  JOURNAL   J Biol Chem 274 (42), 29897-29904 (1999)
   PUBMED   10514471
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Takaishi,M. and Huh,Nh.
  TITLE     A tetratricopeptide repeat-containing protein gene, tpis, whose
            expression is induced with differentiation of spermatogenic cells
  JOURNAL   Biochem Biophys Res Commun 264 (1), 81-85 (1999)
   PUBMED   10527845
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC121577.3.
            
            On Jan 24, 2018 this sequence version replaced XP_017172126.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1. This
            results in a shorter protein (isoform 2), compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.143845.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 14.46 cM"
     Protein         1..668
                     /product="sperm-associated antigen 1 isoform 2"
                     /note="infertility-related sperm protein Spag-1;
                     TPR-containing protein involved in spermatogenesis"
                     /calculated_mol_wt=73841
     Region          <3..105
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          13..42
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          47..75
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <200..>437
                     /region_name="3a0801s09"
                     /note="mitochondrial precursor proteins import receptor
                     (72 kDa mitochondrial outermembrane protein)
                     (mitochondrial import receptor for the ADP/ATP carrier)
                     (translocase of outermembrane tom70); TIGR00990"
                     /db_xref="CDD:273380"
     Region          200..226
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(201..202,205..206,208,240,243..244,247..248,
                     250..251,274,277..278,281..282,285)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          238..268
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          273..301
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(374,377..378,381..382,384,408,411..412,415..416,
                     418..419,442,445..446,449..450,453)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          374..401
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          386..>562
                     /region_name="PLN03088"
                     /note="SGT1, suppressor of G2 allele of SKP1; Provisional"
                     /db_xref="CDD:215568"
     Region          406..436
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          545..636
                     /region_name="RPAP3_C"
                     /note="Potential Monad-binding region of RPAP3; pfam13877"
                     /db_xref="CDD:464012"
     CDS             1..668
                     /gene="Spag1"
                     /gene_synonym="tpis"
                     /coded_by="NM_001359983.1:1283..3289"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:26942"
                     /db_xref="MGI:MGI:1349387"
ORIGIN      
        1 myytrslsal ptaiaynnra qaeiklqrws saledcekal eldpgnvkal lrrattykhq
       61 nklqeavddl rkvlqvepdn dlakktlsev erdlknsepv selqtkgkrm vieevensgd
      121 eggkgsader edggsdeaam gniqkklmvr rseggrrsrr grtpgpraeq qgglretata
      181 stgdshypee praadnpsgl krrgnelfrg gqfaeaaaqy svaiaqlept gsanadelsi
      241 lysnraacyl kegncrdciq dcnralelhp fsvkpllrra mayetleqyr nayvdyktvl
      301 qidcgiqlas dsanriaril teldgskwre rlppipavpt seplrvwlpa aetpdqdpcp
      361 nncmpsitde kmfqalkeeg nqlvkdknyk daiskynecl kinskacaiy tnralcylkl
      421 gqfeeakldc eqalqidgen vkashrlala qkglencres gvdpsqvlls pdsseaarhl
      481 dtkndtapps kgrerrriqv qevdgssdee perpaeasat sapardgved ggsaepaekl
      541 dvskptnaye fgqvlstisa rkdeeacahl laitapkdlp lllsnklegd tfllliqslk
      601 shlvakdpsl vyehllylsk aerfktmltl inkgqkeqma qlfdglsdtq sdgltaedvq
      661 alrrqyel
//
LOCUS       NP_066979                349 aa            linear   PRI 27-APR-2025
DEFINITION  thioredoxin-related transmembrane protein 4 precursor [Homo
            sapiens].
ACCESSION   NP_066979
VERSION     NP_066979.2
DBSOURCE    REFSEQ: accession NM_021156.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Galligan,J.J. and Petersen,D.R.
  TITLE     The human protein disulfide isomerase gene family
  JOURNAL   Hum Genomics 6 (1), 6 (2012)
   PUBMED   23245351
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Lynes,E.M., Bui,M., Yap,M.C., Benson,M.D., Schneider,B.,
            Ellgaard,L., Berthiaume,L.G. and Simmen,T.
  TITLE     Palmitoylated TMX and calnexin target to the
            mitochondria-associated membrane
  JOURNAL   EMBO J 31 (2), 457-470 (2012)
   PUBMED   22045338
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Sugiura,Y., Araki,K., Iemura,S., Natsume,T., Hoseki,J. and
            Nagata,K.
  TITLE     Novel thioredoxin-related transmembrane protein TMX4 has reductase
            activity
  JOURNAL   J Biol Chem 285 (10), 7135-7142 (2010)
   PUBMED   20056998
  REMARK    GeneRIF: Data identify a novel transmembrane Trx-like protein 4
            (TMX4), in the ER of mammalian cells, and confirm that the Trx-like
            domain has reductase activity in vitro.
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Roth,D., Lynes,E., Riemer,J., Hansen,H.G., Althaus,N., Simmen,T.
            and Ellgaard,L.
  TITLE     A di-arginine motif contributes to the ER localization of the type
            I transmembrane ER oxidoreductase TMX4
  JOURNAL   Biochem J 425 (1), 195-205 (2009)
   PUBMED   19811453
  REMARK    GeneRIF: Data show that features not commonly found in other PDIs
            characterize TMX4 and suggest unique functional properties of the
            protein.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC044777.1, HY011753.1, BC021964.2 and AL021396.8.
            
            On Dec 20, 2003 this sequence version replaced NP_066979.1.
            
            Summary: This gene encodes a member of the disulfide isomerase
            (PDI) family of endoplasmic reticulum (ER) proteins that catalyze
            protein folding and thiol-disulfide interchange reactions. The
            encoded protein has an N-terminal ER-signal sequence, a
            catalytically active thioredoxin domain, one transmembrane domain
            and C-terminal ASP/GLU-rich calcium binding domain. Unlike most
            members of this gene family, it lacks a C-terminal ER-retention
            sequence. The encoded protein has been shown to have reductase
            activity in vitro. [provided by RefSeq, Jan 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.203715.1,
                                           SRR1803617.59751.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000246024.7/ ENSP00000246024.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.3"
     Protein         1..349
                     /product="thioredoxin-related transmembrane protein 4
                     precursor"
                     /note="protein disulfide isomerase family A, member 14;
                     thioredoxin domain containing 13; thioredoxin
                     domain-containing protein 13"
                     /calculated_mol_wt=36758
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H1E5.1)"
                     /calculated_mol_wt=2213
     mat_peptide     24..349
                     /product="Thioredoxin-related transmembrane protein 4.
                     /id=PRO_0000034191"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1E5.1)"
                     /calculated_mol_wt=36758
     Region          37..137
                     /region_name="PDI_a_TMX"
                     /note="PDIa family, TMX subfamily; composed of proteins
                     similar to the TRX-related human transmembrane protein,
                     TMX. TMX is a type I integral membrane protein; the
                     N-terminal redox active TRX domain is present in the
                     endoplasmic reticulum (ER) lumen while the...; cd02994"
                     /db_xref="CDD:239292"
     Site            order(64,67)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239292"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1E5.1)"
     Region          225..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1E5.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H1E5.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H1E5.1)"
     CDS             1..349
                     /gene="TMX4"
                     /gene_synonym="DJ971N18.2; PDIA14; TXNDC13"
                     /coded_by="NM_021156.4:149..1198"
                     /db_xref="CCDS:CCDS13101.1"
                     /db_xref="GeneID:56255"
                     /db_xref="HGNC:HGNC:25237"
                     /db_xref="MIM:616766"
ORIGIN      
        1 maggrcgpql tallaawiaa vaatagpeea alppeqsrvq pmtasnwtlv megewmlkfy
       61 apwcpscqqt dseweafakn geilqisvgk vdviqepgls grffvttlpa ffhakdgifr
      121 ryrgpgifed lqnyilekkw qsvepltgwk spasltmsgm aglfsisgki whlhnyftvt
      181 lgipawcsyv ffviatlvfg lfmglvlvvi secfyvplpr hlserseqnr rseeahraeq
      241 lqdaeeekdd sneeenkdsl vddeeekedl gdedeaeeee eednlaagvd eerseandqg
      301 ppgedgvtre evepeeaeeg iseqpcpadt evvedslrqr ksqhadkgl
//
LOCUS       NP_004575                391 aa            linear   PRI 27-APR-2025
DEFINITION  cell cycle checkpoint control protein RAD9A isoform 1 [Homo
            sapiens].
ACCESSION   NP_004575
VERSION     NP_004575.1
DBSOURCE    REFSEQ: accession NM_004584.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Yang,T., Liu,Y.L., Guo,H.L., Peng,X.F., Zhang,B., Wang,D.,
            Yao,H.F., Zhang,J.F., Wang,X.Y., Chen,P.C. and Xu,D.P.
  TITLE     Unveiling an anoikis-related risk model and the role of RAD9A in
            colon cancer
  JOURNAL   Int Immunopharmacol 140, 112874 (2024)
   PUBMED   39116498
  REMARK    GeneRIF: Unveiling an anoikis-related risk model and the role of
            RAD9A in colon cancer.
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Hara,K., Tatsukawa,K., Nagata,K., Iida,N., Hishiki,A., Ohashi,E.
            and Hashimoto,H.
  TITLE     Structural basis for intra- and intermolecular interactions on RAD9
            subunit of 9-1-1 checkpoint clamp implies functional 9-1-1
            regulation by RHINO
  JOURNAL   J Biol Chem 300 (3), 105751 (2024)
   PUBMED   38354779
  REMARK    GeneRIF: Structural basis for intra- and intermolecular
            interactions on RAD9 subunit of 9-1-1 checkpoint clamp implies
            functional 9-1-1 regulation by RHINO.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Hara,K., Hishiki,A., Hoshino,T., Nagata,K., Iida,N., Sawada,Y.,
            Ohashi,E. and Hashimoto,H.
  TITLE     The 9-1-1 DNA clamp subunit RAD1 forms specific interactions with
            clamp loader RAD17, revealing functional implications for
            binding-protein RHINO
  JOURNAL   J Biol Chem 299 (4), 103061 (2023)
   PUBMED   36841485
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Bessho,T. and Sancar,A.
  TITLE     Human DNA damage checkpoint protein hRAD9 is a 3' to 5' exonuclease
  JOURNAL   J Biol Chem 275 (11), 7451-7454 (2000)
   PUBMED   10713044
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Komatsu,K., Miyashita,T., Hang,H., Hopkins,K.M., Zheng,W.,
            Cuddeback,S., Yamada,M., Lieberman,H.B. and Wang,H.G.
  TITLE     Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and
            promotes apoptosis
  JOURNAL   Nat Cell Biol 2 (1), 1-6 (2000)
   PUBMED   10620799
REFERENCE   8  (residues 1 to 391)
  AUTHORS   St Onge,R.P., Udell,C.M., Casselman,R. and Davey,S.
  TITLE     The human G2 checkpoint control protein hRAD9 is a nuclear
            phosphoprotein that forms complexes with hRAD1 and hHUS1
  JOURNAL   Mol Biol Cell 10 (6), 1985-1995 (1999)
   PUBMED   10359610
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Volkmer,E. and Karnitz,L.M.
  TITLE     Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9
            form a DNA damage-responsive protein complex
  JOURNAL   J Biol Chem 274 (2), 567-570 (1999)
   PUBMED   9872989
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Lieberman,H.B., Hopkins,K.M., Nass,M., Demetrick,D. and Davey,S.
  TITLE     A human homolog of the Schizosaccharomyces pombe rad9+ checkpoint
            control gene
  JOURNAL   Proc Natl Acad Sci U S A 93 (24), 13890-13895 (1996)
   PUBMED   8943031
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC014848.1, U53174.1 and
            AA708970.1.
            
            Summary: This gene product is highly similar to Schizosaccharomyces
            pombe rad9, a cell cycle checkpoint protein required for cell cycle
            arrest and DNA damage repair. This protein possesses 3' to 5'
            exonuclease activity, which may contribute to its role in sensing
            and repairing DNA damage. It forms a checkpoint protein complex
            with RAD1 and HUS1. This complex is recruited by checkpoint protein
            RAD17 to the sites of DNA damage, which is thought to be important
            for triggering the checkpoint-signaling cascade. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U53174.1, BC014848.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307980.7/ ENSP00000311360.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..391
                     /product="cell cycle checkpoint control protein RAD9A
                     isoform 1"
                     /EC_number="3.1.11.2"
                     /note="cell cycle checkpoint control protein RAD9A; hRAD9;
                     DNA repair exonuclease rad9 homolog A; RAD9 homolog A"
                     /calculated_mol_wt=42416
     Region          13..265
                     /region_name="Rad9"
                     /note="pfam04139"
                     /db_xref="CDD:427739"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:11971963; propagated from
                     UniProtKB/Swiss-Prot (Q99638.1)"
     Region          51..91
                     /region_name="Possesses 3'-5' exonuclease activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99638.1)"
     Region          266..391
                     /region_name="Sufficient for interaction with ABL1.
                     /evidence=ECO:0000269|PubMed:11971963"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99638.1)"
     Region          268..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99638.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12709442; propagated from
                     UniProtKB/Swiss-Prot (Q99638.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12709442,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99638.1)"
     Region          319..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99638.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12709442,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99638.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:12709442,
                     ECO:0000269|PubMed:20545769; propagated from
                     UniProtKB/Swiss-Prot (Q99638.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12709442,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99638.1)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12709442,
                     ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q99638.1)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:12709442,
                     ECO:0000269|PubMed:17575048, ECO:0000269|PubMed:20545769,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99638.1)"
     CDS             1..391
                     /gene="RAD9A"
                     /gene_synonym="RAD9"
                     /coded_by="NM_004584.3:60..1235"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8159.1"
                     /db_xref="GeneID:5883"
                     /db_xref="HGNC:HGNC:9827"
                     /db_xref="MIM:603761"
ORIGIN      
        1 mkclvtggnv kvlgkavhsl srigdelyle pledglslrt vnssrsayac flfaplffqq
       61 yqaatpgqdl lrckilmksf lsvfrslaml ektvekccis lngrssrlvv qlhckfgvrk
      121 thnlsfqdce slqavfdpas cphmlrapar vlgeavlpfs palaevtlgi grgrrvilrs
      181 yheeeadsta kamvtemclg eedfqqlqaq egvaitfclk efrgllsfae sanlnlsihf
      241 dapgrpaift ikdslldghf vlatlsdtds hsqdlgsper hqpvpqlqah stphpddfan
      301 ddidsymiam ettignegsr vlpsislspg pqppkspgph seeedeaeps tvpgtpppkk
      361 frslffgsil apvrspqgps pvlaedsege g
//
LOCUS       NP_699174                440 aa            linear   PRI 27-APR-2025
DEFINITION  glycerophosphocholine cholinephosphodiesterase ENPP6 precursor
            [Homo sapiens].
ACCESSION   NP_699174
VERSION     NP_699174.1
DBSOURCE    REFSEQ: accession NM_153343.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Sakagami,H., Aoki,J., Natori,Y., Nishikawa,K., Kakehi,Y., Natori,Y.
            and Arai,H.
  TITLE     Biochemical and molecular characterization of a novel
            choline-specific glycerophosphodiester phosphodiesterase belonging
            to the nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   J Biol Chem 280 (24), 23084-23093 (2005)
   PUBMED   15788404
  REMARK    GeneRIF: NPP6 has a specific role through the hydrolysis of
            polyunsaturated LPC, glycerophosphorylcholine, or
            sphingosylphosphorylcholine in kidney and brain
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079080.5, BC035035.2 and AC107222.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence data to make the sequence
            consistent with the reference genome assembly. The extent of this
            RefSeq transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035035.2, SRR1803616.152303.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2158188
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296741.7/ ENSP00000296741.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q35.1"
     Protein         1..440
                     /product="glycerophosphocholine cholinephosphodiesterase
                     ENPP6 precursor"
                     /EC_number="3.1.4.38"
                     /note="B830047L21Rik; ectonucleotide
                     pyrophosphatase/phosphodiesterase family member 6; NPP-6;
                     E-NPP 6; choline-specific glycerophosphodiester
                     phosphodiesterase; GPC-Cpde; glycerophosphocholine
                     cholinephosphodiesterase ENPP6"
                     /calculated_mol_wt=48137
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2123
     mat_peptide     23..419
                     /product="Glycerophosphocholine cholinephosphodiesterase
                     ENPP6. /id=PRO_0000239361"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWR7.2)"
                     /calculated_mol_wt=45908
     Region          24..397
                     /region_name="Enpp"
                     /note="Ectonucleotide pyrophosphatase/phosphodiesterase,
                     also called autotaxin; cd16018"
                     /db_xref="CDD:293742"
     Site            order(32,70..71,92,193,197,240..241,354)
                     /site_type="active"
                     /db_xref="CDD:293742"
     Site            order(32,70..71,92,193,197,241,354)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293742"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B0BND0; propagated from
                     UniProtKB/Swiss-Prot (Q6UWR7.2)"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q8BGN3; propagated from
                     UniProtKB/Swiss-Prot (Q6UWR7.2)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q8BGN3; propagated from
                     UniProtKB/Swiss-Prot (Q6UWR7.2)"
     Site            341
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q8BGN3; propagated from
                     UniProtKB/Swiss-Prot (Q6UWR7.2)"
     Site            379..381
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293742"
     Site            404
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q8BGN3; propagated from
                     UniProtKB/Swiss-Prot (Q6UWR7.2)"
     CDS             1..440
                     /gene="ENPP6"
                     /gene_synonym="NPP6"
                     /coded_by="NM_153343.4:55..1377"
                     /db_xref="CCDS:CCDS3834.1"
                     /db_xref="GeneID:133121"
                     /db_xref="HGNC:HGNC:23409"
                     /db_xref="MIM:616983"
ORIGIN      
        1 mavklgtlll alalglaqpa sarrkllvfl ldgfrsdyis dealeslpgf keivsrgvkv
       61 dyltpdfpsl sypnyytlmt grhcevhqmi gnymwdpttn ksfdigvnkd slmplwwngs
      121 eplwvtltka krkvymyywp gceveilgvr ptycleyknv ptdinfanav sdaldsfksg
      181 radlaaiyhe ridveghhyg paspqrkdal kavdtvlkym tkwiqerglq drlnviifsd
      241 hgmtdifwmd kvielnkyis lndlqqvkdr gpvvslwpap gkhseiynkl stvehmtvye
      301 keaipsrfyy kkgkfvsplt lvadegwfit enremlpfwm nstgrregwq rgwhgydnel
      361 mdmrgiflaf gpdfksnfra apirsvdvyn vmcnvvgitp lpnngswsrv mcmlkgrast
      421 appvwpshca lalillflla
//
LOCUS       NP_003730                323 aa            linear   PRI 27-APR-2025
DEFINITION  aldo-keto reductase family 1 member C3 isoform 1 [Homo sapiens].
ACCESSION   NP_003730
VERSION     NP_003730.4
DBSOURCE    REFSEQ: accession NM_003739.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Gao,Y., Tao,W., Wang,S., Duan,R. and Zhang,Z.
  TITLE     AKR1C3 silencing inhibits autophagy-dependent glycolysis in thyroid
            cancer cells by inactivating ERK signaling
  JOURNAL   Drug Dev Res 85 (1), e22142 (2024)
   PUBMED   38349266
  REMARK    GeneRIF: AKR1C3 silencing inhibits autophagy-dependent glycolysis
            in thyroid cancer cells by inactivating ERK signaling.
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Himura,R., Kawano,S., Nagata,Y., Kawai,M., Ota,A., Kudo,Y.,
            Yoshino,Y., Fujimoto,N., Miyamoto,H., Endo,S. and Ikari,A.
  TITLE     Inhibition of aldo-keto reductase 1C3 overcomes
            gemcitabine/cisplatin resistance in bladder cancer
  JOURNAL   Chem Biol Interact 388, 110840 (2024)
   PUBMED   38122923
  REMARK    GeneRIF: Inhibition of aldo-keto reductase 1C3 overcomes
            gemcitabine/cisplatin resistance in bladder cancer.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Jeng,K.S., Cheng,P.Y., Lin,Y.H., Liu,P.C., Tseng,P.H., Wang,Y.C.,
            Chang,C.F. and Leu,C.M.
  TITLE     Aldo-keto reductase family member C3 (AKR1C3) promotes
            hepatocellular carcinoma cell growth by producing prostaglandin
            F2alpha
  JOURNAL   Oncol Res 32 (1), 163-174 (2023)
   PUBMED   38188684
  REMARK    GeneRIF: Aldo-keto reductase family member C3 (AKR1C3) promotes
            hepatocellular carcinoma cell growth by producing prostaglandin
            F2alpha.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Lazzarini,R., Tartaglione,M.F., Ciarapica,V., Piva,F.,
            Giulietti,M., Fulgenzi,G., Martelli,M., Ledda,C., Vitale,E.,
            Malavolta,M., Santarelli,L. and Bracci,M.
  TITLE     Keratinocytes Exposed to Blue or Red Light: Proteomic
            Characterization Showed Cytoplasmic Thioredoxin Reductase 1 and
            Aldo-Keto Reductase Family 1 Member C3 Triggered Expression
  JOURNAL   Int J Mol Sci 24 (22), 16189 (2023)
   PUBMED   38003379
  REMARK    GeneRIF: Keratinocytes Exposed to Blue or Red Light: Proteomic
            Characterization Showed Cytoplasmic Thioredoxin Reductase 1 and
            Aldo-Keto Reductase Family 1 Member C3 Triggered Expression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Takano,S., Fukami,T., Ichida,H., Suzuki,K., Nakano,M. and
            Nakajima,M.
  TITLE     In Vitro Evaluation of the Reductase Activities of Human AKR1C3
            Allelic Variants
  JOURNAL   Drug Metab Dispos 51 (9), 1188-1195 (2023)
   PUBMED   37344179
  REMARK    GeneRIF: In Vitro Evaluation of the Reductase Activities of Human
            AKR1C3 Allelic Variants.
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Bennett,M.J., Schlegel,B.P., Jez,J.M., Penning,T.M. and Lewis,M.
  TITLE     Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase
            complexed with NADP+
  JOURNAL   Biochemistry 35 (33), 10702-10711 (1996)
   PUBMED   8718859
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Khanna,M., Qin,K.N., Wang,R.W. and Cheng,K.C.
  TITLE     Substrate specificity, gene structure, and tissue-specific
            distribution of multiple human 3 alpha-hydroxysteroid
            dehydrogenases
  JOURNAL   J Biol Chem 270 (34), 20162-20168 (1995)
   PUBMED   7650035
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Khanna,M., Qin,K.N. and Cheng,K.C.
  TITLE     Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain
            and molecular cloning of multiple cDNAs encoding structurally
            related proteins in humans
  JOURNAL   J Steroid Biochem Mol Biol 53 (1-6), 41-46 (1995)
   PUBMED   7626489
REFERENCE   9  (residues 1 to 323)
  AUTHORS   Khanna,M., Qin,K.N., Klisak,I., Belkin,S., Sparkes,R.S. and
            Cheng,K.C.
  TITLE     Localization of multiple human dihydrodiol dehydrogenase (DDH1 and
            DDH2) and chlordecone reductase (CHDR) genes in chromosome 10 by
            the polymerase chain reaction and fluorescence in situ
            hybridization
  JOURNAL   Genomics 25 (2), 588-590 (1995)
   PUBMED   7789999
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Qin,K.N., New,M.I. and Cheng,K.C.
  TITLE     Molecular cloning of multiple cDNAs encoding human enzymes
            structurally related to 3 alpha-hydroxysteroid dehydrogenase
  JOURNAL   J Steroid Biochem Mol Biol 46 (6), 673-679 (1993)
   PUBMED   8274401
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AV761799.2 and BC019230.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 3, 2002 this sequence version replaced NP_003730.3.
            
            Summary: This gene encodes a member of the aldo/keto reductase
            superfamily, which consists of more than 40 known enzymes and
            proteins. These enzymes catalyze the conversion of aldehydes and
            ketones to their corresponding alcohols by utilizing NADH and/or
            NADPH as cofactors. The enzymes display overlapping but distinct
            substrate specificity. This enzyme catalyzes the reduction of
            prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the
            oxidation of 9alpha,11beta-PGF2 to PGD2. It may play an important
            role in the pathogenesis of allergic diseases such as asthma, and
            may also have a role in controlling cell growth and/or
            differentiation. This gene shares high sequence identity with three
            other gene members and is clustered with those three genes at
            chromosome 10p15-p14. Three transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Dec
            2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes one of the larger isoforms (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001479.2, AB018580.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380554.5/ ENSP00000369927.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p15.1"
     Protein         1..323
                     /product="aldo-keto reductase family 1 member C3 isoform
                     1"
                     /EC_number="1.1.1.62"
                     /EC_number="1.1.1.188"
                     /EC_number="1.1.1.239"
                     /EC_number="1.1.1.64"
                     /EC_number="1.1.1.357"
                     /EC_number="1.1.1.210"
                     /EC_number="1.1.1.53"
                     /note="dihydrodiol dehydrogenase X; type IIb 3-alpha
                     hydroxysteroid dehydrogenase; prostaglandin F synthase;
                     trans-1,2-dihydrobenzene-1,2-diol dehydrogenase;
                     dihydrodiol dehydrogenase 3; 3-alpha hydroxysteroid
                     dehydrogenase, type II; indanol dehydrogenase; 3-alpha-HSD
                     type II, brain; chlordecone reductase homolog HAKRb;
                     testosterone 17-beta-dehydrogenase 5"
                     /calculated_mol_wt=36722
     Region          6..306
                     /region_name="AKR_AKR1C1-35"
                     /note="AKR1C family of aldo-keto reductase (AKR); cd19108"
                     /db_xref="CDD:381334"
     Site            order(22..24,50,54..55,84,86,117..118,120,128..129,
                     166..167,190,216..222,224,227,236,253,268..273,276,
                     279..280,306)
                     /site_type="active"
                     /db_xref="CDD:381334"
     Site            order(50,55,84,117)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381334"
     Site            54
                     /site_type="other"
                     /note="Important for substrate specificity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P42330.4)"
     Site            84
                     /site_type="other"
                     /note="Lowers pKa of active site Tyr.
                     /evidence=ECO:0000250|UniProtKB:P14550; propagated from
                     UniProtKB/Swiss-Prot (P42330.4)"
     Site            227
                     /site_type="other"
                     /note="Involved in ligand recognition and product release.
                     /evidence=ECO:0000269|PubMed:15087468; propagated from
                     UniProtKB/Swiss-Prot (P42330.4)"
     Site            306
                     /site_type="other"
                     /note="Involved in ligand recognition and product release.
                     /evidence=ECO:0000269|PubMed:15087468; propagated from
                     UniProtKB/Swiss-Prot (P42330.4)"
     CDS             1..323
                     /gene="AKR1C3"
                     /gene_synonym="DD3; DDX; HA1753; HAKRB; HAKRe; hluPGFS;
                     HSD17B5; PGFS"
                     /coded_by="NM_003739.6:32..1003"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7063.1"
                     /db_xref="GeneID:8644"
                     /db_xref="HGNC:HGNC:386"
                     /db_xref="MIM:603966"
ORIGIN      
        1 mdskhqcvkl ndghfmpvlg fgtyappevp rskalevtkl aieagfrhid sahlynneeq
       61 vglairskia dgsvkredif ytsklwstfh rpelvrpale nslkkaqldy vdlylihspm
      121 slkpgeelsp tdengkvifd ivdlcttwea mekckdagla ksigvsnfnr rqlemilnkp
      181 glkykpvcnq vechpyfnrs klldfckskd ivlvaysalg sqrdkrwvdp nspvlledpv
      241 lcalakkhkr tpalialryq lqrgvvvlak syneqrirqn vqvfefqlta edmkaidgld
      301 rnlhyfnsds fashpnypys dey
//
LOCUS       NP_001291922             329 aa            linear   PRI 27-APR-2025
DEFINITION  serine dehydratase-like [Homo sapiens].
ACCESSION   NP_001291922 XP_005253887
VERSION     NP_001291922.1
DBSOURCE    REFSEQ: accession NM_001304993.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Yamada,T., Komoto,J., Kasuya,T., Takata,Y., Ogawa,H., Mori,H. and
            Takusagawa,F.
  TITLE     A catalytic mechanism that explains a low catalytic activity of
            serine dehydratase like-1 from human cancer cells: crystal
            structure and site-directed mutagenesis studies
  JOURNAL   Biochim Biophys Acta 1780 (5), 809-818 (2008)
   PUBMED   18342636
  REMARK    GeneRIF: The crystal structure of SDSL has been determined.
            Site-directed mutagenesis studies suggest that having a glycine at
            residue 72 of SDSL is the major reason for the reduction of its
            catalytic activity, in comparison with the liver enzyme (SDS).
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Ogawa,H., Gomi,T., Nishizawa,M., Hayakawa,Y., Endo,S., Hayashi,K.,
            Ochiai,H., Takusagawa,F., Pitot,H.C., Mori,H., Sakurai,H.,
            Koizumi,K., Saiki,I., Oda,H., Fujishita,T., Miwa,T., Maruyama,M.
            and Kobayashi,M.
  TITLE     Enzymatic and biochemical properties of a novel human serine
            dehydratase isoform
  JOURNAL   Biochim Biophys Acta 1764 (5), 961-971 (2006)
   PUBMED   16580895
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010178.40 and BC091479.1.
            
            On Feb 13, 2015 this sequence version replaced XP_005253887.1.
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' UTR, compared to variant 1. Variants 1 and 2 encode the same
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091479.1, SRR5189655.222857.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000403593.9/ ENSP00000385790.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.13"
     Protein         1..329
                     /product="serine dehydratase-like"
                     /EC_number="4.3.1.17"
                     /EC_number="4.3.1.19"
                     /EC_number="5.1.1.3"
                     /note="serine dehydratase related sequence 1; L-serine
                     deaminase; serine dehydratase 2; L-threonine dehydratase;
                     L-serine dehydratase/L-threonine deaminase; glutamate
                     racemase; cancerous serine dehydratase"
                     /calculated_mol_wt=34543
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q96GA7.1)"
     Region          17..326
                     /region_name="Trp-synth-beta_II"
                     /note="Tryptophan synthase beta superfamily (fold type
                     II); this family of pyridoxal phosphate (PLP)-dependent
                     enzymes catalyzes beta-replacement and beta-elimination
                     reactions. This CD corresponds to
                     aminocyclopropane-1-carboxylate deaminase (ACCD),
                     tryptophan...; cl00342"
                     /db_xref="CDD:444852"
     Site            order(47..48,74,174..178,275,309..310)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:107202"
     Site            48
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107202"
     CDS             1..329
                     /gene="SDSL"
                     /gene_synonym="cSDH; SDH 2; SDHL; SDS-RS1; TDH"
                     /coded_by="NM_001304993.2:120..1109"
                     /db_xref="CCDS:CCDS9170.1"
                     /db_xref="GeneID:113675"
                     /db_xref="HGNC:HGNC:30404"
                     /db_xref="MIM:620735"
ORIGIN      
        1 mdgpvaehak qepfhvvtpl leswalsqva gmpvflkcen vqpsgsfkir gighfcqema
       61 kkgcrhlvcs sggnagiaaa yaarklgipa tivlpestsl qvvqrlqgeg aevqltgkvw
      121 deanlraqel akrdgwenvp pfdhpliwkg haslvqelka vlrtppgalv lavgggglla
      181 gvvagllevg wqhvpiiame thgahcfnaa itagklvtlp ditsvakslg aktvaarale
      241 cmqvckihse vvedteavsa vqqlldderm lvepacgaal aaiysgllrr lqaegclpps
      301 ltsvvvivcg gnninsrelq alkthlgqv
//
LOCUS       NP_001357496             761 aa            linear   PRI 27-APR-2025
DEFINITION  semaphorin-4A isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001357496 XP_016857545
VERSION     NP_001357496.1
DBSOURCE    REFSEQ: accession NM_001370567.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Hou,T., Zhang,P., Tian,H., Luo,Y., Li,J., Zhang,K. and Li,Y.
  TITLE     Semaphorin 4A Maintains Trophoblastic Function via Activating the
            STAT3 Pathway
  JOURNAL   Biomolecules 14 (7), 826 (2024)
   PUBMED   39062540
  REMARK    GeneRIF: Semaphorin 4A Maintains Trophoblastic Function via
            Activating the STAT3 Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Naito,Y., Koyama,S., Masuhiro,K., Hirai,T., Uenami,T., Inoue,T.,
            Osa,A., Machiyama,H., Watanabe,G., Sax,N., Villa,J.,
            Kinugasa-Katayama,Y., Nojima,S., Yaga,M., Hosono,Y., Okuzaki,D.,
            Satoh,S., Tsuda,T., Nakanishi,Y., Suga,Y., Morita,T., Fukushima,K.,
            Nishide,M., Shiroyama,T., Miyake,K., Iwahori,K., Hirata,H.,
            Nagatomo,I., Yano,Y., Tamiya,M., Kumagai,T., Takemoto,N.,
            Inohara,H., Yamasaki,S., Yamashita,K., Aoshi,T., Akbay,E.A.,
            Hosen,N., Shintani,Y., Takamatsu,H., Mori,M., Takeda,Y. and
            Kumanogoh,A.
  TITLE     Tumor-derived semaphorin 4A improves PD-1-blocking antibody
            efficacy by enhancing CD8+ T cell cytotoxicity and proliferation
  JOURNAL   Sci Adv 9 (20), eade0718 (2023)
   PUBMED   37205755
  REMARK    GeneRIF: Tumor-derived semaphorin 4A improves PD-1-blocking
            antibody efficacy by enhancing CD8[+] T cell cytotoxicity and
            proliferation.
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Eiza,N., Garty,M., Staun-Ram,E., Miller,A. and Vadasz,Z.
  TITLE     The possible involvement of sema3A and sema4A in the pathogenesis
            of multiple sclerosis
  JOURNAL   Clin Immunol 238, 109017 (2022)
   PUBMED   35460904
  REMARK    GeneRIF: The possible involvement of sema3A and sema4A in the
            pathogenesis of multiple sclerosis.
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Chapoval,S.P., Lee,M., Lemmer,A., Ajayi,O., Qi,X., Neuwald,A.F. and
            Keegan,A.D.
  TITLE     Identifying Function Determining Residues in Neuroimmune Semaphorin
            4A
  JOURNAL   Int J Mol Sci 23 (6), 3024 (2022)
   PUBMED   35328445
  REMARK    GeneRIF: Identifying Function Determining Residues in Neuroimmune
            Semaphorin 4A.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Kumanogoh,A. and Kikutani,H.
  TITLE     Immune semaphorins: a new area of semaphorin research
  JOURNAL   J Cell Sci 116 (Pt 17), 3463-3470 (2003)
   PUBMED   12893810
  REMARK    Review article
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Kikutani,H. and Kumanogoh,A.
  TITLE     Semaphorins in interactions between T cells and antigen-presenting
            cells
  JOURNAL   Nat Rev Immunol 3 (2), 159-167 (2003)
   PUBMED   12563299
  REMARK    Review article
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Kumanogoh,A., Marukawa,S., Suzuki,K., Takegahara,N., Watanabe,C.,
            Ch'ng,E., Ishida,I., Fujimura,H., Sakoda,S., Yoshida,K. and
            Kikutani,H.
  TITLE     Class IV semaphorin Sema4A enhances T-cell activation and interacts
            with Tim-2
  JOURNAL   Nature 419 (6907), 629-633 (2002)
   PUBMED   12374982
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Puschel,A.W., Adams,R.H. and Betz,H.
  TITLE     Murine semaphorin D/collapsin is a member of a diverse gene family
            and creates domains inhibitory for axonal extension
  JOURNAL   Neuron 14 (5), 941-948 (1995)
   PUBMED   7748561
REFERENCE   10 (residues 1 to 761)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            On May 10, 2019 this sequence version replaced XP_016857545.1.
            
            Summary: This gene encodes a member of the semaphorin family of
            soluble and transmembrane proteins. Semaphorins are involved in
            numerous functions, including axon guidance, morphogenesis,
            carcinogenesis, and immunomodulation. The encoded protein is a
            single-pass type I membrane protein containing an
            immunoglobulin-like C2-type domain, a PSI domain and a sema domain.
            It inhibits axonal extension by providing local signals to specify
            territories inaccessible for growing axons. It is an activator of
            T-cell-mediated immunity and suppresses vascular endothelial growth
            factor (VEGF)-mediated endothelial cell migration and proliferation
            in vitro and angiogenesis in vivo. Mutations in this gene are
            associated with retinal degenerative diseases including retinitis
            pigmentosa type 35 (RP35) and cone-rod dystrophy type 10 (CORD10).
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been identified.[provided by RefSeq, Sep
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.62185.1,
                                           SRR1660803.122934.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..761
                     /product="semaphorin-4A isoform 1 precursor"
                     /note="sema B; semaphorin-B; sema domain, immunoglobulin
                     domain (Ig), transmembrane domain (TM) and short
                     cytoplasmic domain, (semaphorin) 4A"
                     /calculated_mol_wt=80167
     sig_peptide     1..32
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
                     /calculated_mol_wt=3425
     mat_peptide     33..761
                     /product="semaphorin-4A isoform 1"
                     /calculated_mol_wt=80167
     Region          55..495
                     /region_name="Sema_4A"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4A (Sema4A); cd11256"
                     /db_xref="CDD:200517"
     Site            order(115..117,178,199,201..202,204,219,222,224,229,252,
                     276..280,282,361..362,386,390,393)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200517"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Site            order(253..254,256,259..261,295,297..299,301,303,326..328,
                     334..335,399,411)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200517"
     Region          496..540
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Site            496
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          566..638
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          576..580
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409456"
     Region          588..592
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409456"
     Region          607..611
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409456"
     Site            607
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          621..626
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409456"
     Site            684..704
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          722..749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S1.2)"
     CDS             1..761
                     /gene="SEMA4A"
                     /gene_synonym="CORD10; RP35; SEMAB; SEMB"
                     /coded_by="NM_001370567.1:32..2317"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS1132.1"
                     /db_xref="GeneID:64218"
                     /db_xref="HGNC:HGNC:10729"
                     /db_xref="MIM:607292"
ORIGIN      
        1 malpalgldp wsllglflfq llqlllpttt aggggqgpmp rvryyagder ralsffhqkg
       61 lqdfdtllls gdgntlyvga reailaldiq dpgvprlknm ipwpasdrkk secafkkksn
      121 etqcfnfirv lvsynvthly tcgtfafspa ctfielqdsy llpisedkvm egkgqspfdp
      181 ahkhtavlvd gmlysgtmnn flgsepilmr tlgsqpvlkt dnflrwlhhd asfvaaipst
      241 qvvyfffeet asefdfferl htsrvarvck ndvggekllq kkwttflkaq llctqpgqlp
      301 fnvirhavll padsptaphi yavftsqwqv ggtrssavca fslldiervf kgkykelnke
      361 tsrwttyrgp etnprpgscs vgpssdkalt fmkdhflmde qvvgtpllvk sgveytrlav
      421 etaqgldghs hlvmylgttt gslhkavvsg dssahlveei qlfpdpepvr nlqlaptqga
      481 vfvgfsggvw rvprancsvy escvdcvlar dphcawdpes rtccllsapn lnswkqdmer
      541 gnpewacasg pmsrslrpqs rpqiikevla vpnsilelpc phlsalasyy wshgpaavpe
      601 asstvyngsl llivqdgvgg lyqcwateng fsypvisywv dsqdqtlald pelagipreh
      661 vkvpltrvsg gaalaaqqsy wphfvtvtvl falvlsgali ilvasplral rargkvqgce
      721 tlrpgekapl sreqhlqspk ecrtsasdvd adnnclgtev a
//
LOCUS       NP_036330                217 aa            linear   PRI 27-APR-2025
DEFINITION  grancalcin isoform b [Homo sapiens].
ACCESSION   NP_036330
VERSION     NP_036330.1
DBSOURCE    REFSEQ: accession NM_012198.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Han,S.H., Korm,S., Han,Y.G., Choi,S.Y., Kim,S.H., Chung,H.J.,
            Park,K., Kim,J.Y., Myung,K., Lee,J.Y., Kim,H. and Kim,D.W.
  TITLE     GCA links TRAF6-ULK1-dependent autophagy activation in resistant
            chronic myeloid leukemia
  JOURNAL   Autophagy 15 (12), 2076-2090 (2019)
   PUBMED   30929559
  REMARK    GeneRIF: GCA activates TRAF6 ubiquitin ligase activity to induce
            Lys63 ubiquitination of ULK1, a crucial regulator of autophagy,
            resulting in its stabilization and activation. It was also
            highlighted the role of GCA-TRAF6-ULK1 autophagy regulatory axis in
            imatinib resistance.
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Lollike,K., Johnsen,A.H., Durussel,I., Borregaard,N. and Cox,J.A.
  TITLE     Biochemical characterization of the penta-EF-hand protein
            grancalcin and identification of L-plastin as a binding partner
  JOURNAL   J Biol Chem 276 (21), 17762-17769 (2001)
   PUBMED   11279160
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Jia,J., Han,Q., Borregaard,N., Lollike,K. and Cygler,M.
  TITLE     Crystal structure of human grancalcin, a member of the
            penta-EF-hand protein family
  JOURNAL   J Mol Biol 300 (5), 1271-1281 (2000)
   PUBMED   10903868
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Maki,M., Narayana,S.V. and Hitomi,K.
  TITLE     A growing family of the Ca2+-binding proteins with five EF-hand
            motifs
  JOURNAL   Biochem J 328 (Pt 2) (Pt 2), 718-720 (1997)
   PUBMED   9441591
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Teahan,C.G., Totty,N.F. and Segal,A.W.
  TITLE     Isolation and characterization of grancalcin, a novel 28 kDa
            EF-hand calcium-binding protein from human neutrophils
  JOURNAL   Biochem J 286 (Pt 2) (Pt 2), 549-554 (1992)
   PUBMED   1530588
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Boyhan,A., Casimir,C.M., French,J.K., Teahan,C.G. and Segal,A.W.
  TITLE     Molecular cloning and characterization of grancalcin, a novel
            EF-hand calcium-binding protein abundant in neutrophils and
            monocytes
  JOURNAL   J Biol Chem 267 (5), 2928-2933 (1992)
   PUBMED   1737748
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010876.2, BC005214.1 and
            M81637.1.
            
            Summary: This gene encodes a calcium-binding protein that is
            abundant in neutrophils and macrophages. In the absence of divalent
            cation, this protein localizes to the cytosolic fraction; with
            magnesium alone, it partitions with the granule fraction; and in
            the presence of magnesium and calcium, it associates with both the
            granule and membrane fractions. Alternative splicing and use of
            alternative promoters results in multiple transcript variants.
            [provided by RefSeq, Aug 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.65667.1,
                                           SRR1660805.219044.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000437150.7/ ENSP00000394842.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.2"
     Protein         1..217
                     /product="grancalcin isoform b"
                     /note="grancalcin, EF-hand calcium-binding protein;
                     grancalcin, penta-EF-hand protein"
                     /calculated_mol_wt=23879
     Region          53..217
                     /region_name="EFh_PEF_grancalcin"
                     /note="Penta-EF hand, calcium binding motifs, found in
                     grancalcin; cd16186"
                     /db_xref="CDD:320061"
     Region          53..81
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320061"
     Site            order(65,72,132,134,136,140,143)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320061"
     Region          93..122
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320061"
     Site            order(95,105,153,159,162,165..169,177,181,184..185,
                     188..189,191..192,201..208,210,212,214..217)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320061"
     Region          123..153
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320061"
     Region          159..186
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320061"
     Region          187..217
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320061"
     CDS             1..217
                     /gene="GCA"
                     /gene_synonym="GCL"
                     /coded_by="NM_012198.5:118..771"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS2218.1"
                     /db_xref="GeneID:25801"
                     /db_xref="HGNC:HGNC:15990"
                     /db_xref="MIM:607030"
ORIGIN      
        1 maypgygggf gnfsiqvpgm qmgqpvpetg pailldgysg paysdtyssa gdsvytyfsa
       61 vagqdgevda eelqrcltqs gingtyspfs letcrimiam ldrdhtgkmg fnafkelwaa
      121 lnawkenfmt vdqdgsgtve hhelrqaigl mgyrlspqtl ttivkryskn griffddyva
      181 ccvklraltd ffrkrdhlqq gsanfiyddf lqgtmai
//
LOCUS       NP_003416                682 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 45 [Homo sapiens].
ACCESSION   NP_003416
VERSION     NP_003416.1
DBSOURCE    REFSEQ: accession NM_003425.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Giri,A.K., Prasad,G., Bandesh,K., Parekatt,V., Mahajan,A.,
            Banerjee,P., Kauser,Y., Chakraborty,S., Rajashekar,D., Sharma,A.,
            Mathur,S.K., Basu,A., McCarthy,M.I., Tandon,N. and Bharadwaj,D.
  CONSRTM   INDICO
  TITLE     Multifaceted genome-wide study identifies novel regulatory loci in
            SLC22A11 and ZNF45 for body mass index in Indians
  JOURNAL   Mol Genet Genomics 295 (4), 1013-1026 (2020)
   PUBMED   32363570
  REMARK    GeneRIF: our study discovered 3 novel population-specific
            functional genetic variants (rs6913677, rs2078267, rs8100011) in 2
            novel (SLC22A11 and ZNF45) and 1 earlier reported gene (BAI3) for
            BMI in Indians. Our study decodes key genomic loci underlying
            obesity phenotype in Indians that may serve as prospective drug
            targets in future
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Davis,O.S., Band,G., Pirinen,M., Haworth,C.M., Meaburn,E.L.,
            Kovas,Y., Harlaar,N., Docherty,S.J., Hanscombe,K.B.,
            Trzaskowski,M., Curtis,C.J., Strange,A., Freeman,C., Bellenguez,C.,
            Su,Z., Pearson,R., Vukcevic,D., Langford,C., Deloukas,P., Hunt,S.,
            Gray,E., Dronov,S., Potter,S.C., Tashakkori-Ghanbaria,A.,
            Edkins,S., Bumpstead,S.J., Blackwell,J.M., Bramon,E., Brown,M.A.,
            Casas,J.P., Corvin,A., Duncanson,A., Jankowski,J.A., Markus,H.S.,
            Mathew,C.G., Palmer,C.N., Rautanen,A., Sawcer,S.J., Trembath,R.C.,
            Viswanathan,A.C., Wood,N.W., Barroso,I., Peltonen,L., Dale,P.S.,
            Petrill,S.A., Schalkwyk,L.S., Craig,I.W., Lewis,C.M., Price,T.S.,
            Donnelly,P., Plomin,R. and Spencer,C.C.
  CONSRTM   Wellcome Trust Case Control Consortium 2
  TITLE     The correlation between reading and mathematics ability at age
            twelve has a substantial genetic component
  JOURNAL   Nat Commun 5, 4204 (2014)
   PUBMED   25003214
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Bonetti,A., Koivisto,K., Pirttila,T., Elovaara,I., Reunanen,M.,
            Laaksonen,M., Ruutiainen,J., Peltonen,L., Rantamaki,T. and
            Tienari,P.J.
  TITLE     A follow-up study of chromosome 19q13 in multiple sclerosis
            susceptibility
  JOURNAL   J Neuroimmunol 208 (1-2), 119-124 (2009)
   PUBMED   19195718
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 682)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   6  (residues 1 to 682)
  AUTHORS   Shannon,M. and Stubbs,L.
  TITLE     Analysis of homologous XRCC1-linked zinc-finger gene families in
            human and mouse: evidence for orthologous genes
  JOURNAL   Genomics 49 (1), 112-121 (1998)
   PUBMED   9570955
REFERENCE   7  (residues 1 to 682)
  AUTHORS   Constantinou Deltas,C., Bashiardes,E., Patsalis,P.C.,
            Hadjimarcou,M., Kroisel,P.M., Ioannou,P.A., Roses,A.D. and Lee,J.E.
  TITLE     Complete coding sequence, exon/intron arrangement and chromosome
            location of ZNF45, a KRAB-domain-containing gene
  JOURNAL   Cytogenet Cell Genet 75 (4), 230-233 (1996)
   PUBMED   9067431
REFERENCE   8  (residues 1 to 682)
  AUTHORS   Constantinou-Deltas,C.D., Gilbert,J., Bartlett,R.J.,
            Herbstreith,M., Roses,A.D. and Lee,J.E.
  TITLE     The identification and characterization of KRAB-domain-containing
            zinc finger proteins
  JOURNAL   Genomics 12 (3), 581-589 (1992)
   PUBMED   1559709
REFERENCE   9  (residues 1 to 682)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006213.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.51680.1, AK127739.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269973.10/ ENSP00000269973.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..682
                     /product="zinc finger protein 45"
                     /note="zinc finger protein 45 (a Kruppel-associated box
                     (KRAB) domain polypeptide); zinc finger protein 13;
                     BRC1744; zinc finger protein KOX5"
                     /calculated_mol_wt=78111
     Region          8..67
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Site            order(148,150..151,154..155,157,171,173,177..178,181..182,
                     185,199,201,203,205..206,209..210,213)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          166..186
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          169..542
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          194..214
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          251..270
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          278..298
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          306..326
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(311,313,315,317..318,321..322,325,339,341,345..346,
                     349..350,353,367,369,371,373..374,377..378,381)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          334..354
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          362..382
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          390..410
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          418..438
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          446..466
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(451,453,455,457..458,461..462,465,479,481,485..486,
                     489..490,493,507,509,511,513..514,517..518,521)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          474..494
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <496..607
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          502..522
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..550
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          558..578
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          586..606
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(591,593,595,597..598,601..602,605,619,621,625..626,
                     629..630,633,647,649,651,653..654,657..658,661)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          598..622
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          614..634
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          626..650
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          642..662
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          662..682
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02386.2)"
     CDS             1..682
                     /gene="ZNF45"
                     /gene_synonym="KOX5; ZNF13"
                     /coded_by="NM_003425.4:1115..3163"
                     /db_xref="CCDS:CCDS12632.1"
                     /db_xref="GeneID:7596"
                     /db_xref="HGNC:HGNC:13111"
                     /db_xref="MIM:194554"
ORIGIN      
        1 mtkskeavtf kdvavvfsee elqlldlaqr klyrdvmlen frnvvsvghq stpdglpqle
       61 reeklwmmkm atqrdnssga knlkemetlq evglrylphe elfcsqiwqq itrelikyqd
      121 svvniqrtgc qlekrddlhy kdegfsnqss hlqvhrvhtg ekpykgehcv ksfswsshlq
      181 inqrahagek pykcekcdna frrfsslqah qrvhsraksy tndasyrsfs qrshlphhqr
      241 vptgenpyky eecgrnvgks shcqaplivh tgekpykcee cgvgfsqrsy lqvhlkvhtg
      301 kkpykceecg ksfswrsrlq aherihtgek pykcnacgks fsysshlnih crihtgekpy
      361 kceecgkgfs vgshlqahqi shtgekpykc eecgkgfcra snlldhqrgh tgekpyqcda
      421 cgkgfsrssd fnihfrvhtg ekpykceecg kgfsqasnll ahqrghtgek pykcgtcgkg
      481 fsrssdlnvh crihtgekpy kcercgkafs qfsslqvhqr vhtgekpyqc aecgkgfsvg
      541 sqlqahqrch tgekpyqcee cgkgfcrasn flahrgvhtg ekpyrcdvcg krfrqrsylq
      601 ahqrvhtger pykceecgkv fswssylqah qrvhtgekpy kceecgkgfs wsssliihqr
      661 vhaddegdkd fpssedshrk tr
//
LOCUS       NP_001353518             901 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 22 [Homo
            sapiens].
ACCESSION   NP_001353518 XP_016855508
VERSION     NP_001353518.1
DBSOURCE    REFSEQ: accession NM_001366589.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 901)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 901)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 901)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 901)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 901)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 901)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 901)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855508.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.132822.1,
                                           SRR1660805.159851.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..901
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 22"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=101890
     Region          1..156
                     /region_name="Necessary for mRNA 3'-end cleavage and
                     cytoplasmic accumulation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          1..151
                     /region_name="Necessary for DNA and RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          <603..>737
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            623
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            625
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            704
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            712
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            737
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            745
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            753
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            774
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            790
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            869
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     CDS             1..901
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366589.1:26..2731"
                     /note="isoform 22 is encoded by transcript variant 29"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkekt pelpepsvkv kepsvqeats
      241 tsdilkvpkp epipepkeps peknskkeke kektrprsrs rsksrsrtrs rspshtrprr
      301 rhrsrsrsys prrrpsprrr psprrrtppr rmpppprhrr srspvrrrrr ssaslsgsss
      361 sssssrsrsp pkkppkrtss pprktrrlsp saspprrrhr psppatpppk trhsptpqqs
      421 nrtrksrvsv spgrtsvtkh kgtekresps papkprkvel sesedkggkm aaadsvqqrr
      481 qyrrqnqqss sdsgssssse derpkrshvk ngevgrrrrh spsrsaspsp rkrqketspr
      541 grrrrspspp ptrrrrspsp appprrrrtp tppprrrtps ppprrrspsp rrysppiqrr
      601 yspspppkrr taspppppkr raspspppkr rvshspppkq rsspvtkrrs pslsskhrkg
      661 sspsrstrea rspqpnkrhs psprprapqt ssspppvrrg assspqrrqs pspstrpirr
      721 vsrtpepkki kkaaspspqs vrrvsssrsv sgspepaakk ppappspvqs qspstnwspa
      781 vpvkkakspt pspspprnsd qegggkkkkk kkdkkhkkdk khkkhkkhkk ekavaaaaaa
      841 avtpaaiaaa tttlaqeepv aapepkkete seaednlddl ekhlrekalr smrkaqvspq
      901 s
//
LOCUS       NP_001346772             193 aa            linear   ROD 27-APR-2025
DEFINITION  neurocalcin-delta [Mus musculus].
ACCESSION   NP_001346772 XP_006520170
VERSION     NP_001346772.1
DBSOURCE    REFSEQ: accession NM_001359843.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Kolesova,H., Hrabalova,P., Bohuslavova,R., Abaffy,P.,
            Fabriciova,V., Sedmera,D. and Pavlinkova,G.
  TITLE     Reprogramming of the developing heart by Hif1a-deficient
            sympathetic system and maternal diabetes exposure
  JOURNAL   Front Endocrinol (Lausanne) 15, 1344074 (2024)
   PUBMED   38505753
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Ahuja,N., Hiltabidle,M.S., Rajasekhar,H., Voss,S., Lu,S.Z.,
            Barlow,H.R., Cowdin,M.A., Daniel,E., Vaddaraju,V., Anandakumar,T.,
            Black,E., Cleaver,O. and Maynard,C.
  TITLE     Endothelial Cyp26b1 restrains murine heart valve growth during
            development
  JOURNAL   Dev Biol 486, 81-95 (2022)
   PUBMED   35364055
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Del Aguila,A., Adam,M., Ullom,K., Shaw,N., Qin,S., Ehrman,J.,
            Nardini,D., Salomone,J., Gebelein,B., Lu,Q.R., Potter,S.S.,
            Waclaw,R., Campbell,K. and Nakafuku,M.
  TITLE     Olig2 defines a subset of neural stem cells that produce specific
            olfactory bulb interneuron subtypes in the subventricular zone of
            adult mice
  JOURNAL   Development 149 (5) (2022)
   PUBMED   35132995
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Upadhyay,A., Hosseinibarkooie,S., Schneider,S., Kaczmarek,A.,
            Torres-Benito,L., Mendoza-Ferreira,N., Overhoff,M., Rombo,R.,
            Grysko,V., Kye,M.J., Kononenko,N.L. and Wirth,B.
  TITLE     Neurocalcin Delta Knockout Impairs Adult Neurogenesis Whereas Half
            Reduction Is Not Pathological
  JOURNAL   Front Mol Neurosci 12, 19 (2019)
   PUBMED   30853885
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Duda,T., Pertzev,A. and Sharma,R.K.
  TITLE     Ca(2+) modulation of ANF-RGC: new signaling paradigm interlocked
            with blood pressure regulation
  JOURNAL   Biochemistry 51 (46), 9394-9405 (2012)
   PUBMED   23088492
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Brouns,M.R., De Castro,S.C., Terwindt-Rouwenhorst,E.A., Massa,V.,
            Hekking,J.W., Hirst,C.S., Savery,D., Munts,C., Partridge,D.,
            Lamers,W., Kohler,E., van Straaten,H.W., Copp,A.J. and Greene,N.D.
  TITLE     Over-expression of Grhl2 causes spina bifida in the Axial defects
            mutant mouse
  JOURNAL   Hum Mol Genet 20 (8), 1536-1546 (2011)
   PUBMED   21262862
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Kotani,T., Murata,Y., Ohnishi,H., Mori,M., Kusakari,S., Saito,Y.,
            Okazawa,H., Bixby,J.L. and Matozaki,T.
  TITLE     Expression of PTPRO in the interneurons of adult mouse olfactory
            bulb
  JOURNAL   J Comp Neurol 518 (2), 119-136 (2010)
   PUBMED   19924828
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Murias,A.R., Weruaga,E., Recio,J.S., Airado,C., Diaz,D. and
            Alonso,J.R.
  TITLE     Distribution of neurocalcin-containing neurons reveals sexual
            dimorphism in the mouse olfactory bulb
  JOURNAL   Chem Senses 32 (7), 673-680 (2007)
   PUBMED   17548529
  REMARK    GeneRIF: According to their distribution in the olfactory bulb,
            neurocalcin-immunoreactive interneurons could reflect a sexually
            dimorphic regulation of specific odorants.
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Germana,A., del Valle,M.E., Laura,R., Ciriaco,E., Vega,J.A. and
            Germana,G.
  TITLE     Effects of neurotrophin-3 gene mutation in the expression of
            neurocalcin
  JOURNAL   Ital J Anat Embryol 110 (2 Suppl 1), 37-47 (2005)
   PUBMED   16101019
  REMARK    GeneRIF: Neurocalcin-containing DRG neurons include all
            proprioceptive, and a subset of mechanoreceptive and
            proprioceptive. Furthermore, NT-3 is involved in the maturation of
            motor end-plates.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC122506.4, AC122263.5 and AC121814.3.
            
            On Jan 13, 2018 this sequence version replaced XP_006520170.1.
            
            Transcript Variant: This variant (9) differs in the 5' UTR compared
            to variant 1. Variants 1 through 11 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660825.155058.1,
                                           SRR1660815.71105.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 14.94 cM"
     Protein         1..193
                     /product="neurocalcin-delta"
                     /calculated_mol_wt=22114
     Region          21..175
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..193
                     /gene="Ncald"
                     /gene_synonym="D030020D09Rik; D15Ertd412e"
                     /coded_by="NM_001359843.1:550..1131"
                     /db_xref="CCDS:CCDS27435.1"
                     /db_xref="GeneID:52589"
                     /db_xref="MGI:MGI:1196326"
ORIGIN      
        1 mgkqnsklrp evmqdllest dfteheiqew ykgflrdcps ghlsmeefkk iygnffpygd
       61 askfaehvfr tfdangdgti dfrefiials vtsrgkleqk lkwafsmydl dgngyiskae
      121 mleivqaiyk mvssvmkmpe destpekrte kifrqmdtnr dgklsleefi rgaksdpsiv
      181 rllqcdpssa gqf
//
LOCUS       NP_631961                592 aa            linear   PRI 27-APR-2025
DEFINITION  TATA-binding protein-associated factor 2N isoform 1 [Homo sapiens].
ACCESSION   NP_631961
VERSION     NP_631961.1
DBSOURCE    REFSEQ: accession NM_139215.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Fu,X.L., He,F.T., Li,M.H., Fu,C.Y. and Chen,J.Z.
  TITLE     circZNF532 promotes endothelial-to-mesenchymal transition in
            diabetic retinopathy by recruiting TAF15 to stabilize PIK3CD
  JOURNAL   Endocr J 71 (7), 675-686 (2024)
   PUBMED   38811189
  REMARK    GeneRIF: circZNF532 promotes endothelial-to-mesenchymal transition
            in diabetic retinopathy by recruiting TAF15 to stabilize PIK3CD.
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Yang,H., He,P., Luo,W., Liu,S. and Yang,Y.
  TITLE     circRNA TATA-box binding protein associated factor 15 acts as an
            oncogene to facilitate bladder cancer progression through targeting
            miR-502-5p/high mobility group box 3
  JOURNAL   Mol Carcinog 63 (4), 629-646 (2024)
   PUBMED   38226841
  REMARK    GeneRIF: circRNA TATA-box binding protein associated factor 15 acts
            as an oncogene to facilitate bladder cancer progression through
            targeting miR-502-5p/high mobility group box 3.
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Couthouis,J., Hart,M.P., Shorter,J., DeJesus-Hernandez,M.,
            Erion,R., Oristano,R., Liu,A.X., Ramos,D., Jethava,N.,
            Hosangadi,D., Epstein,J., Chiang,A., Diaz,Z., Nakaya,T.,
            Ibrahim,F., Kim,H.J., Solski,J.A., Williams,K.L.,
            Mojsilovic-Petrovic,J., Ingre,C., Boylan,K., Graff-Radford,N.R.,
            Dickson,D.W., Clay-Falcone,D., Elman,L., McCluskey,L., Greene,R.,
            Kalb,R.G., Lee,V.M., Trojanowski,J.Q., Ludolph,A., Robberecht,W.,
            Andersen,P.M., Nicholson,G.A., Blair,I.P., King,O.D., Bonini,N.M.,
            Van Deerlin,V., Rademakers,R., Mourelatos,Z. and Gitler,A.D.
  TITLE     A yeast functional screen predicts new candidate ALS disease genes
  JOURNAL   Proc Natl Acad Sci U S A 108 (52), 20881-20890 (2011)
   PUBMED   22065782
  REMARK    GeneRIF: Missense mutations of TAF-15, an RNA-binding protein, were
            found in patients with amyotrophic lateral sclerosis, and gene
            conferred neurodegeneration when expressend in Drosophila.
            Erratum:[Proc Natl Acad Sci U S A. 2023 Jan 3;120(1):e2220845120.
            doi: 10.1073/pnas.2220845120. PMID: 36577079]
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Martini,A., La Starza,R., Janssen,H., Bilhou-Nabera,C.,
            Corveleyn,A., Somers,R., Aventin,A., Foa,R., Hagemeijer,A.,
            Mecucci,C. and Marynen,P.
  TITLE     Recurrent rearrangement of the Ewing's sarcoma gene, EWSR1, or its
            homologue, TAF15, with the transcription factor CIZ/NMP4 in acute
            leukemia
  JOURNAL   Cancer Res 62 (19), 5408-5412 (2002)
   PUBMED   12359745
  REMARK    GeneRIF: The transcription factor gene CIZ/NMP4 is recurrently
            involved in acute leukemia through fusion with either EWSR1 or
            TAF15.
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Panagopoulos,I., Mencinger,M., Dietrich,C.U., Bjerkehagen,B.,
            Saeter,G., Mertens,F., Mandahl,N. and Heim,S.
  TITLE     Fusion of the RBP56 and CHN genes in extraskeletal myxoid
            chondrosarcomas with translocation t(9;17)(q22;q11)
  JOURNAL   Oncogene 18 (52), 7594-7598 (1999)
   PUBMED   10602519
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Morohoshi,F., Ootsuka,Y., Arai,K., Ichikawa,H., Mitani,S.,
            Munakata,N. and Ohki,M.
  TITLE     Genomic structure of the human RBP56/hTAFII68 and FUS/TLS genes
  JOURNAL   Gene 221 (2), 191-198 (1998)
   PUBMED   9795213
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Morohoshi,F., Arai,K., Takahashi,E.I., Tanigami,A. and Ohki,M.
  TITLE     Cloning and mapping of a human RBP56 gene encoding a putative RNA
            binding protein similar to FUS/TLS and EWS proteins
  JOURNAL   Genomics 38 (1), 51-57 (1996)
   PUBMED   8954779
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Parada,C.A., Yoon,J.B. and Roeder,R.G.
  TITLE     A novel LBP-1-mediated restriction of HIV-1 transcription at the
            level of elongation in vitro
  JOURNAL   J Biol Chem 270 (5), 2274-2283 (1995)
   PUBMED   7836461
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Zhou,Q. and Sharp,P.A.
  TITLE     Novel mechanism and factor for regulation by HIV-1 Tat
  JOURNAL   EMBO J 14 (2), 321-328 (1995)
   PUBMED   7835343
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314194.1, BG403710.1,
            BC046099.1 and AI351964.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the TET family of
            RNA-binding proteins. The encoded protein plays a role in RNA
            polymerase II gene transcription as a component of a distinct
            subset of multi-subunit transcription initiation factor TFIID
            complexes. Translocations involving this gene play a role in acute
            leukemia and extraskeletal myxoid chondrosarcoma, and mutations in
            this gene may play a role in amyotrophic lateral sclerosis.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, May
            2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U51334.1, SRR3476690.1086746.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000605844.6/ ENSP00000474096.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..592
                     /product="TATA-binding protein-associated factor 2N
                     isoform 1"
                     /note="TATA box-binding protein-associated factor 2N
                     (RNA-binding protein 56); TATA box binding protein
                     (TBP)-associated factor, RNA polymerase II, N, 68kD
                     (RNA-binding protein 56); RBP56/CSMF fusion;
                     TBP-associated factor 15; TAF15 RNA polymerase II, TATA
                     box binding protein (TBP)-associated factor, 68kDa"
                     /calculated_mol_wt=61699
     Region          1..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92804.1)"
     Region          <2..>124
                     /region_name="ser_rich_anae_1"
                     /note="serine-rich protein; NF033849"
                     /db_xref="CDD:468206"
     Region          136..>315
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Site            206
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:19124016, ECO:0000269|Ref.9;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Region          232..317
                     /region_name="RRM_FUS_TAF15"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     fused in Ewing's sarcoma protein (FUS), TATA-binding
                     protein-associated factor 15 (TAF15) and similar proteins;
                     cd12535"
                     /db_xref="CDD:409951"
     Site            268
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Region          324..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92804.1)"
     Region          354..384
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          358..379
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     Region          373..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92804.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Region          407..575
                     /region_name="21 X approximate tandem repeats of
                     D-R-[S,G](0,3)-G-G-Y-G-G"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92804.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            431
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            459
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            475
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            483
                     /site_type="methylation"
                     /note="Dimethylated arginine. /evidence=ECO:0000269|Ref.9;
                     propagated from UniProtKB/Swiss-Prot (Q92804.1)"
     Site            528
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:19124016; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            535
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:19124016; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            562
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92804.1)"
     Site            570
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:19124016, ECO:0000269|Ref.9;
                     Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:19124016, ECO:0000269|Ref.9;
                     propagated from UniProtKB/Swiss-Prot (Q92804.1)"
     CDS             1..592
                     /gene="TAF15"
                     /gene_synonym="Npl3; RBP56; TAF2N; TAFII68"
                     /coded_by="NM_139215.3:87..1865"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32623.1"
                     /db_xref="GeneID:8148"
                     /db_xref="HGNC:HGNC:11547"
                     /db_xref="MIM:601574"
ORIGIN      
        1 msdsgsygqs ggeqqsysty gnpgsqgygq asqsysgygq ttdssygqny sgyssygqsq
       61 sgysqsyggy enqkqssysq qpynnqgqqq nmessgsqgg rapsydqpdy gqqdsydqqs
      121 gydqhqgsyd eqsnydqqhd sysqnqqsyh sqrenyshht qddrrdvsry gednrgyggs
      181 qgggrgrggy dkdgrgpmtg ssggdrggfk nfgghrdygp rtdadsesdn sdnntifvqg
      241 lgegvstdqv geffkqigii ktnkktgkpm inlytdkdtg kpkgeatvsf ddppsakaai
      301 dwfdgkefhg niikvsfatr rpefmrgggs gggrrgrggy rgrggfqgrg gdpksgdwvc
      361 pnpscgnmnf arrnscnqcn eprpedsrps ggdfrgrgyg gergyrgrgg rggdrggygg
      421 drsgggyggd rssgggysgd rsgggyggdr sgggyggdrg ggyggdrggg yggdrgggyg
      481 gdrggyggdr gggyggdrgg yggdrggygg drggyggdrg gyggdrsrgg yggdrgggsg
      541 yggdrsggyg gdrsgggygg drgggyggdr ggyggkmggr ndyrndqrnr py
//
LOCUS       NP_001352975             279 aa            linear   PRI 27-APR-2025
DEFINITION  protein ABHD18 isoform 14 [Homo sapiens].
ACCESSION   NP_001352975
VERSION     NP_001352975.1
DBSOURCE    REFSEQ: accession NM_001366046.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099340.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.235846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.2"
     Protein         1..279
                     /product="protein ABHD18 isoform 14"
                     /note="abhydrolase domain-containing protein 18;
                     alpha/beta hydrolase domain-containing protein 18; protein
                     ABHD18"
                     /calculated_mol_wt=30998
     Region          <1..279
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
     CDS             1..279
                     /gene="ABHD18"
                     /gene_synonym="C4orf29"
                     /coded_by="NM_001366046.1:688..1527"
                     /note="isoform 14 is encoded by transcript variant 17"
                     /db_xref="GeneID:80167"
                     /db_xref="HGNC:HGNC:26111"
ORIGIN      
        1 mggalvlesa allhwlereg ygplgmtgis mgghmaslav snwpkpmpli pclswstasg
       61 vfttgvlsks inwrelekqy ytqtvyeeei ihmleycgtd sfkmgqefvk hftssadklt
      121 nlnlvsrtln ldisnqvvsq kpadchnssk tsvsatsegl llqdtskmkr fnqtlstnks
      181 gytsrnpqsy hllskeqsrn slrkeslifm kgvmdecthv anfsvpvdps liivvqaked
      241 ayiprtgvrs lqeiwpgcei rylegghisa ylfkqglfr
//
LOCUS       NP_004480                327 aa            linear   PRI 27-APR-2025
DEFINITION  G protein pathway suppressor 2 [Homo sapiens].
ACCESSION   NP_004480 NP_116329
VERSION     NP_004480.1
DBSOURCE    REFSEQ: accession NM_004489.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Zhao,L., Gu,C., Zhang,Y., Yan,J., Qiu,L., Qin,X. and Wang,Y.
  TITLE     Regulation mechanism of GPS2 on PGC-1alpha/Drp1-mediated
            mitochondrial dynamics in inflammation of acute lung injury
  JOURNAL   Int Immunopharmacol 140, 112838 (2024)
   PUBMED   39116501
  REMARK    GeneRIF: Regulation mechanism of GPS2 on PGC-1alpha/Drp1-mediated
            mitochondrial dynamics in inflammation of acute lung injury.
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Lu,Y., Ma,W.B., Ren,G.M., Li,Y.T., Wang,T., Zhan,Y.Q., Xiang,S.S.,
            Chen,H., Gao,H.Y., Zhao,K., Yu,M., Li,C.Y., Yang,X.M. and Yin,R.H.
  TITLE     GPS2 promotes erythroid differentiation in K562 erythroleukemia
            cells primarily via NCOR1
  JOURNAL   Int J Hematol 120 (2), 157-166 (2024)
   PUBMED   38814500
  REMARK    GeneRIF: GPS2 promotes erythroid differentiation in K562
            erythroleukemia cells primarily via NCOR1.
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Si,Y., Zhang,H., Peng,P., Zhu,C., Shen,J., Xiong,Y., Liu,X.,
            Xiang,Y., Li,W., Ren,Y., Wan,F., Zhang,L. and Liu,Y.
  TITLE     G protein pathway suppressor 2 suppresses gastric cancer by
            destabilizing epidermal growth factor receptor
  JOURNAL   Cancer Sci 112 (12), 4867-4882 (2021)
   PUBMED   34609770
  REMARK    GeneRIF: G protein pathway suppressor 2 suppresses gastric cancer
            by destabilizing epidermal growth factor receptor.
            Erratum:[Cancer Sci. 2025 Jan;116(1):279. doi: 10.1111/cas.16391.
            PMID: 39500631]
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Degenhardt,Y.Y. and Silverstein,S.J.
  TITLE     Gps2, a protein partner for human papillomavirus E6 proteins
  JOURNAL   J Virol 75 (1), 151-160 (2001)
   PUBMED   11119584
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Peng,Y.C., Breiding,D.E., Sverdrup,F., Richard,J. and Androphy,E.J.
  TITLE     AMF-1/Gps2 binds p300 and enhances its interaction with
            papillomavirus E2 proteins
  JOURNAL   J Virol 74 (13), 5872-5879 (2000)
   PUBMED   10846067
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Breiding,D.E., Sverdrup,F., Grossel,M.J., Moscufo,N., Boonchai,W.
            and Androphy,E.J.
  TITLE     Functional interaction of a novel cellular protein with the
            papillomavirus E2 transactivation domain
  JOURNAL   Mol Cell Biol 17 (12), 7208-7219 (1997)
   PUBMED   9372953
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Jin,D.Y., Teramoto,H., Giam,C.Z., Chun,R.F., Gutkind,J.S. and
            Jeang,K.T.
  TITLE     A human suppressor of c-Jun N-terminal kinase 1 activation by tumor
            necrosis factor alpha
  JOURNAL   J Biol Chem 272 (41), 25816-25823 (1997)
   PUBMED   9325311
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Spain,B.H., Bowdish,K.S., Pacal,A.R., Staub,S.F., Koo,D.,
            Chang,C.Y., Xie,W. and Colicelli,J.
  TITLE     Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11),
            suppress G-protein- and mitogen-activated protein kinase-mediated
            signal transduction in yeast and mammalian cells
  JOURNAL   Mol Cell Biol 16 (12), 6698-6706 (1996)
   PUBMED   8943324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026954.14 and BC013652.1.
            
            On Oct 6, 2004 this sequence version replaced NP_116329.1.
            
            Summary: This gene encodes a protein involved in G
            protein-mitogen-activated protein kinase (MAPK) signaling cascades.
            When overexpressed in mammalian cells, this gene could potently
            suppress a RAS- and MAPK-mediated signal and interfere with JNK
            activity, suggesting that the function of this gene may be signal
            repression. The encoded protein is an integral subunit of the
            NCOR1-HDAC3 (nuclear receptor corepressor 1-histone deacetylase 3)
            complex, and it was shown that the complex inhibits JNK activation
            through this subunit and thus could potentially provide an
            alternative mechanism for hormone-mediated antagonism of AP1
            (activator protein 1) function. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.68963.1,
                                           SRR1803612.98914.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380728.7/ ENSP00000370104.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..327
                     /product="G protein pathway suppressor 2"
                     /note="GPS-2"
                     /calculated_mol_wt=36558
     Region          5..292
                     /region_name="G_path_suppress"
                     /note="G-protein pathway suppressor; pfam15991"
                     /db_xref="CDD:464961"
     Region          26..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13227.3)"
     Region          61..94
                     /region_name="interaction with SUMO.
                     /evidence=ECO:0000269|PubMed:20159957"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13227.3)"
     Region          177..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13227.3)"
     Region          253..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13227.3)"
     Site            312
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13227.3)"
     Site            323
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:19917673,
                     ECO:0007744|PubMed:24129315; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0000269|PubMed:19917673;
                     propagated from UniProtKB/Swiss-Prot (Q13227.3)"
     CDS             1..327
                     /gene="GPS2"
                     /gene_synonym="AMF-1"
                     /coded_by="NM_004489.5:98..1081"
                     /db_xref="CCDS:CCDS11100.1"
                     /db_xref="GeneID:2874"
                     /db_xref="HGNC:HGNC:4550"
                     /db_xref="MIM:601935"
ORIGIN      
        1 mpallerpkl snamaralhr himmererkr qeeeevdkmm eqkmkeeqer rkkkemeerm
       61 sleetkeqil kleekllalq eekhqlflql kkvlheeekr rrkeqsdltt ltsaayqqsl
      121 tvhtgthlls mqgspgghnr pgtlmaadra kqmfgpqvlt trhyvgsaaa fagtpehgqf
      181 qgspggaygt aqppphygpt qpayspsqql rapsafpavq ylsqpqpqpy avhghfqptq
      241 tgflqpggal slqkqmehan qqtgfsdsss lrpmhpqalh papgllaspq lpvqmqpagk
      301 sgfaatsqpg prlpfiqhsq nprfyhk
//
LOCUS       NP_076986                226 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane gamma-carboxyglutamic acid protein 4 precursor [Homo
            sapiens].
ACCESSION   NP_076986
VERSION     NP_076986.1
DBSOURCE    REFSEQ: accession NM_024081.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Zhang,L., Qin,Y., Wu,G., Wang,J., Cao,J., Wang,Y., Wu,D., Yang,K.,
            Zhao,Z., He,L., Lyu,J., Li,H. and Gu,H.
  TITLE     PRRG4 promotes breast cancer metastasis through the recruitment of
            NEDD4 and downregulation of Robo1
  JOURNAL   Oncogene 39 (49), 7196-7208 (2020)
   PUBMED   33037408
  REMARK    GeneRIF: PRRG4 promotes breast cancer metastasis through the
            recruitment of NEDD4 and downregulation of Robo1.
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Justice,E.D., Barnum,S.J. and Kidd,T.
  TITLE     The WAGR syndrome gene PRRG4 is a functional homologue of the
            commissureless axon guidance gene
  JOURNAL   PLoS Genet 13 (8), e1006865 (2017)
   PUBMED   28859078
  REMARK    GeneRIF: PRRG4 could re-localize hRobo1 from the cell surface,
            suggesting that PRRG4 is a functional homologue of Comm. Comm is
            required for axon guidance and synapse formation in the fly, so
            PRRG4 could contribute to the autistic symptoms of WAGR by
            disturbing either of these processes in the developing human brain.
            Erratum:[PLoS Genet. 2017 Oct 23;13(10):e1007061. doi:
            10.1371/journal.pgen.1007061. PMID: 29059187]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Yamamoto,T., Togawa,M., Shimada,S., Sangu,N., Shimojima,K. and
            Okamoto,N.
  TITLE     Narrowing of the responsible region for severe developmental delay
            and autistic behaviors in WAGR syndrome down to 1.6 Mb including
            PAX6, WT1, and PRRG4
  JOURNAL   Am J Med Genet A 164A (3), 634-638 (2014)
   PUBMED   24357251
  REMARK    GeneRIF: the unique genotype identified in this study suggested
            that haploinsufficiencies of PAX6 or PRRG4 included in this region
            are candidate genes for severe developmental delay and autistic
            features characteristic of WAGR syndrome.
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Yazicioglu,M.N., Monaldini,L., Chu,K., Khazi,F.R., Murphy,S.L.,
            Huang,H., Margaritis,P. and High,K.A.
  TITLE     Cellular localization and characterization of cytosolic binding
            partners for Gla domain-containing proteins PRRG4 and PRRG2
  JOURNAL   J Biol Chem 288 (36), 25908-25914 (2013)
   PUBMED   23873930
  REMARK    GeneRIF: Cellular localization and characterization of cytosolic
            binding partners for Gla domain-containing proteins PRRG4 and
            PRRG2.
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Latourelle,J.C., Pankratz,N., Dumitriu,A., Wilk,J.B., Goldwurm,S.,
            Pezzoli,G., Mariani,C.B., DeStefano,A.L., Halter,C., Gusella,J.F.,
            Nichols,W.C., Myers,R.H. and Foroud,T.
  CONSRTM   PROGENI Investigators, Coordinators and Molecular Genetic
            Laboratories; GenePD Investigators, Coordinators and Molecular
            Genetic Laboratories
  TITLE     Genomewide association study for onset age in Parkinson disease
  JOURNAL   BMC Med Genet 10, 98 (2009)
   PUBMED   19772629
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Kulman,J.D., Harris,J.E., Xie,L. and Davie,E.W.
  TITLE     Identification of two novel transmembrane gamma-carboxyglutamic
            acid proteins expressed broadly in fetal and adult tissues
  JOURNAL   Proc Natl Acad Sci U S A 98 (4), 1370-1375 (2001)
   PUBMED   11171957
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL035400.13, BC010052.2 and BC063393.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063393.1, ERR279828.10324.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257836.4/ ENSP00000257836.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..226
                     /product="transmembrane gamma-carboxyglutamic acid protein
                     4 precursor"
                     /note="transmembrane gamma-carboxyglutamic acid protein 4;
                     proline-rich Gla protein 4; proline rich Gla
                     (G-carboxyglutamic acid) 4 (transmembrane); proline-rich
                     gamma-carboxyglutamic acid protein 4"
                     /calculated_mol_wt=23575
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1846
     Region          33..96
                     /region_name="GLA"
                     /note="Domain containing Gla (gamma-carboxyglutamate)
                     residues; smart00069"
                     /db_xref="CDD:214503"
     mat_peptide     50..226
                     /product="Transmembrane gamma-carboxyglutamic acid protein
                     4. /id=PRO_0000022552"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZD6.1)"
                     /calculated_mol_wt=19908
     Site            72
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00463; propagated
                     from UniProtKB/Swiss-Prot (Q9BZD6.1)"
     Site            114..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZD6.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BZD6.1)"
     Region          186..189
                     /region_name="LPXY motif, mediates binding to WW
                     domain-containing proteins.
                     /evidence=ECO:0000269|PubMed:23873930"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZD6.1)"
     Region          204..207
                     /region_name="PPXY motif, mediates binding to WW
                     domain-containing proteins.
                     /evidence=ECO:0000269|PubMed:23873930"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZD6.1)"
     CDS             1..226
                     /gene="PRRG4"
                     /gene_synonym="PRGP4; TMG4"
                     /coded_by="NM_024081.6:270..950"
                     /db_xref="CCDS:CCDS7881.1"
                     /db_xref="GeneID:79056"
                     /db_xref="HGNC:HGNC:30799"
                     /db_xref="MIM:611690"
ORIGIN      
        1 mftllvllsq lptvtlgfph cargpkaskh ageevftske eanffihrrl lynrfdlelf
       61 tpgnlerecn eelcnyeear eifvdedkti afwqeysakg pttksdgnre kidvmglltg
      121 liaagvflvi fgllgyylci tkcnrlqhpc ssavyergrh tpsiifrrpe eaalsplpps
      181 vedaglpsye qavaltrkhs vsppppypgh tkgfrvfkks mslpsh
//
LOCUS       NP_057616                448 aa            linear   PRI 27-APR-2025
DEFINITION  inositol polyphosphate 5-phosphatase K isoform 1 [Homo sapiens].
ACCESSION   NP_057616
VERSION     NP_057616.2
DBSOURCE    REFSEQ: accession NM_016532.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Moes,B., Li,H., Molina-Ortiz,P., Radermecker,C., Rosu,A., Vande
            Catsyne,C.A., Sayyed,S.A., Fontela,J., Duque,M., Mostafa,A.,
            Azzi,A., Barata,J.T., Merino,R., Xu,C., Desmet,C.J. and
            Schurmans,S.
  TITLE     INPP5K controls the dynamic structure and signaling of wild-type
            and mutated, leukemia-associated IL-7 receptors
  JOURNAL   Blood 141 (14), 1708-1717 (2023)
   PUBMED   36599086
  REMARK    GeneRIF: INPP5K controls the dynamic structure and signaling of
            wild-type and mutated, leukemia-associated IL-7 receptors.
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Sun,J., Harion,R., Naito,T. and Saheki,Y.
  TITLE     INPP5K and Atlastin-1 maintain the nonuniform distribution of
            ER-plasma membrane contacts in neurons
  JOURNAL   Life Sci Alliance 4 (11), e202101092 (2021)
   PUBMED   34556534
  REMARK    GeneRIF: INPP5K and Atlastin-1 maintain the nonuniform distribution
            of ER-plasma membrane contacts in neurons.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Hathazi,D., Cox,D., D'Amico,A., Tasca,G., Charlton,R.,
            Carlier,R.Y., Baumann,J., Kollipara,L., Zahedi,R.P., Feldmann,I.,
            Deleuze,J.F., Torella,A., Cohn,R., Robinson,E., Ricci,F.,
            Jungbluth,H., Fattori,F., Boland,A., O'Connor,E., Horvath,R.,
            Barresi,R., Lochmuller,H., Urtizberea,A., Jacquemont,M.L.,
            Nelson,I., Swan,L., Bonne,G. and Roos,A.
  TITLE     INPP5K and SIL1 associated pathologies with overlapping clinical
            phenotypes converge through dysregulation of PHGDH
  JOURNAL   Brain 144 (8), 2427-2442 (2021)
   PUBMED   33792664
  REMARK    GeneRIF: INPP5K and SIL1 associated pathologies with overlapping
            clinical phenotypes converge through dysregulation of PHGDH.
            Erratum:[Brain. 2024 Aug 1;147(8):e62. doi: 10.1093/brain/awae239.
            PMID: 39023925]
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Schurmans,S., Vande Catsyne,C.A., Desmet,C. and Moes,B.
  TITLE     The phosphoinositide 5-phosphatase INPP5K: From gene structure to
            in vivo functions
  JOURNAL   Adv Biol Regul 79, 100760 (2021)
   PUBMED   33060052
  REMARK    GeneRIF: The phosphoinositide 5-phosphatase INPP5K: From gene
            structure to in vivo functions.
            Review article
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Gurung,R., Tan,A., Ooms,L.M., McGrath,M.J., Huysmans,R.D.,
            Munday,A.D., Prescott,M., Whisstock,J.C. and Mitchell,C.A.
  TITLE     Identification of a novel domain in two mammalian
            inositol-polyphosphate 5-phosphatases that mediates membrane ruffle
            localization. The inositol 5-phosphatase skip localizes to the
            endoplasmic reticulum and translocates to membrane ruffles
            following epidermal growth factor stimulation
  JOURNAL   J Biol Chem 278 (13), 11376-11385 (2003)
   PUBMED   12536145
  REMARK    GeneRIF: identification of novel domain that mediates membrane
            ruffle localization
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Ijuin,T. and Takenawa,T.
  TITLE     SKIP negatively regulates insulin-induced GLUT4 translocation and
            membrane ruffle formation
  JOURNAL   Mol Cell Biol 23 (4), 1209-1220 (2003)
   PUBMED   12556481
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Ijuin,T., Mochizuki,Y., Fukami,K., Funaki,M., Asano,T. and
            Takenawa,T.
  TITLE     Identification and characterization of a novel inositol
            polyphosphate 5-phosphatase
  JOURNAL   J Biol Chem 275 (15), 10870-10875 (2000)
   PUBMED   10753883
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Drayer,A.L., Pesesse,X., De Smedt,F., Communi,D., Moreau,C. and
            Erneux,C.
  TITLE     The family of inositol and phosphatidylinositol polyphosphate
            5-phosphatases
  JOURNAL   Biochem Soc Trans 24 (4), 1001-1005 (1996)
   PUBMED   8968500
  REMARK    Review article
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Mitchell,C.A., Brown,S., Campbell,J.K., Munday,A.D. and Speed,C.J.
  TITLE     Regulation of second messengers by the inositol polyphosphate
            5-phosphatases
  JOURNAL   Biochem Soc Trans 24 (4), 994-1000 (1996)
   PUBMED   8968499
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100748.2, BC004362.1,
            AB036829.1 and BM510617.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 19, 2002 this sequence version replaced NP_057616.1.
            
            Summary: This gene encodes a protein with 5-phosphatase activity
            toward polyphosphate inositol. The protein localizes to the cytosol
            in regions lacking actin stress fibers. It is thought that this
            protein may negatively regulate the actin cytoskeleton.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform of
            this protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB036829.1, SRR3476690.994275.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000421807.7/ ENSP00000413937.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..448
                     /product="inositol polyphosphate 5-phosphatase K isoform
                     1"
                     /EC_number="3.1.3.56"
                     /EC_number="3.1.3.36"
                     /EC_number="3.1.3.86"
                     /note="phosphatidylinositol-4,5-bisphosphate
                     5-phosphatase; phosphatidylinositol-3,4,5-trisphosphate
                     5-phosphatase; skeletal muscle and kidney-enriched
                     inositol phosphatase"
                     /calculated_mol_wt=50959
     Region          14..320
                     /region_name="EEP"
                     /note="Exonuclease-Endonuclease-Phosphatase (EEP) domain
                     superfamily; cl00490"
                     /db_xref="CDD:469791"
     Region          16..318
                     /region_name="Catalytic. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT40.3)"
     Site            order(22,54,149,192,194,269,310..311)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197306"
     Site            order(54,310)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197306"
     Site            order(149,194,311)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197306"
     Region          318..448
                     /region_name="Required for interaction with GPR78 and
                     PAK1. /evidence=ECO:0000269|PubMed:26940976"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT40.3)"
     Region          321..448
                     /region_name="Required for ruffle localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT40.3)"
     Region          331..431
                     /region_name="SKICH"
                     /note="SKICH domain; pfam17751"
                     /db_xref="CDD:465482"
     CDS             1..448
                     /gene="INPP5K"
                     /gene_synonym="MDCCAID; PPS; SKIP"
                     /coded_by="NM_016532.4:114..1460"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11004.1"
                     /db_xref="GeneID:51763"
                     /db_xref="HGNC:HGNC:33882"
                     /db_xref="MIM:607875"
ORIGIN      
        1 mssrklsgpk grrlsihvvt wnvasaappl dlsdllqlnn rnlnldiyvi glqelnsgii
       61 sllsdaafnd swssflmdvl splsfikvsh vrmqgilllv fakyqhlpyi qilstkstpt
      121 glfgywgnkg gvniclklyg yyvsiinchl pphisnnyqr lehfdrilem qncegrdipn
      181 ildhdliiwf gdmnfriedf glhfvresik nrcygglwek dqlsiakkhd pllrefqegr
      241 llfpptykfd rnsndydtse kkrkpawtdr ilwrlkrqpc agpdtpippa shfslslrgy
      301 sshmtygisd hkpvsgtfdl elkplvsapl ivlmpedlwt vendmmvsys stsdfpsspw
      361 dwiglykvgl rdvndyvsya wvgdskvscs dnlnqvyidi snipttedef llcyysnslr
      421 svvgisrpfq ippgslredp lgeaqpqi
//
LOCUS       NP_689841                440 aa            linear   PRI 27-APR-2025
DEFINITION  sorting nexin-31 isoform 1 [Homo sapiens].
ACCESSION   NP_689841
VERSION     NP_689841.3
DBSOURCE    REFSEQ: accession NM_152628.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 440)
  AUTHORS   McNally,K.E., Faulkner,R., Steinberg,F., Gallon,M., Ghai,R.,
            Pim,D., Langton,P., Pearson,N., Danson,C.M., Nagele,H.,
            Morris,L.L., Singla,A., Overlee,B.L., Heesom,K.J., Sessions,R.,
            Banks,L., Collins,B.M., Berger,I., Billadeau,D.D., Burstein,E. and
            Cullen,P.J.
  TITLE     Retriever is a multiprotein complex for retromer-independent
            endosomal cargo recycling
  JOURNAL   Nat Cell Biol 19 (10), 1214-1225 (2017)
   PUBMED   28892079
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Vieira,N., Deng,F.M., Liang,F.X., Liao,Y., Chang,J., Zhou,G.,
            Zheng,W., Simon,J.P., Ding,M., Wu,X.R., Romih,R., Kreibich,G. and
            Sun,T.T.
  TITLE     SNX31: a novel sorting nexin associated with the
            uroplakin-degrading multivesicular bodies in terminally
            differentiated urothelial cells
  JOURNAL   PLoS One 9 (6), e99644 (2014)
   PUBMED   24914955
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Seet,L.F. and Hong,W.
  TITLE     The Phox (PX) domain proteins and membrane traffic
  JOURNAL   Biochim Biophys Acta 1761 (8), 878-896 (2006)
   PUBMED   16782399
  REMARK    Review article
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Kurth,J., Perniok,A., Schmitz,R., Iking-Konert,C., Chiorazzi,N.,
            Thompson,K.M., Winkler,T., Rajewsky,K. and Kuppers,R.
  TITLE     Lack of deleterious somatic mutations in the CD95 gene of
            plasmablasts from systemic lupus erythematosus patients and
            autoantibody-producing cell lines
  JOURNAL   Eur J Immunol 32 (12), 3785-3792 (2002)
   PUBMED   12516573
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001205.3, AK093906.1, CD106024.1 and BQ012274.1.
            
            On Feb 5, 2009 this sequence version replaced NP_689841.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK093906.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311812.7/ ENSP00000312368.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..440
                     /product="sorting nexin-31 isoform 1"
                     /calculated_mol_wt=50671
     Region          4..106
                     /region_name="PX_SNX17_31"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexins 17 and 31; cd06885"
                     /db_xref="CDD:132795"
     Site            order(37..39,61..62,75)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132795"
     Region          112..209
                     /region_name="FERM_F1_SNX31"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 31
                     (SNX31); cd16122"
                     /db_xref="CDD:340539"
     Region          270..384
                     /region_name="FERM-like_C_SNX31"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     31; cd13336"
                     /db_xref="CDD:275415"
     CDS             1..440
                     /gene="SNX31"
                     /coded_by="NM_152628.4:152..1474"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6288.1"
                     /db_xref="GeneID:169166"
                     /db_xref="HGNC:HGNC:28605"
                     /db_xref="MIM:619839"
ORIGIN      
        1 mkmhfcipvs qqrsdalggr yvlysvhldg flfcrvrysq lhgwneqlrr vfgnclppfp
       61 pkyylamtta maderrdqle qylqnvtmdp nvlrsdvfve flklaqlntf diatkkayld
      121 iflpneqsir ieiitsdtae rvlevvshki glcrellgyf glflirfgke gklsvvkkla
      181 dfelpyvslg ssevenckvg lrkwymapsl dsvlmdcrva vdllymqaiq diekgwakpt
      241 qaqrqkleaf qkedsqtkfl elarevrhyg ylqldpctcd ypesgsgavl svgnneiscc
      301 itlpdsqtqd ivfqmsrvkc wqvtflgtll dtdgpqrtln qnlelrfqys edscwqwfvi
      361 ytkqafllss clkkmisekm vklaaentem qievpeqsks kkyhiqqsqq kdyssflsrk
      421 skikiakddc vfgnikeedl
//
LOCUS       NP_699192                436 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein kinase NIM1 [Homo sapiens].
ACCESSION   NP_699192
VERSION     NP_699192.1
DBSOURCE    REFSEQ: accession NM_153361.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Faber,S., Letteboer,S.J.F., Junger,K., Butcher,R., Tammana,T.V.S.,
            van Beersum,S.E.C., Ueffing,M., Collin,R.W.J., Liu,Q., Boldt,K. and
            Roepman,R.
  TITLE     PDE6D Mediates Trafficking of Prenylated Proteins NIM1K and UBL3 to
            Primary Cilia
  JOURNAL   Cells 12 (2), 312 (2023)
   PUBMED   36672247
  REMARK    GeneRIF: PDE6D Mediates Trafficking of Prenylated Proteins NIM1K
            and UBL3 to Primary Cilia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Jaleel,M., McBride,A., Lizcano,J.M., Deak,M., Toth,R., Morrice,N.A.
            and Alessi,D.R.
  TITLE     Identification of the sucrose non-fermenting related kinase SNRK,
            as a novel LKB1 substrate
  JOURNAL   FEBS Lett 579 (6), 1417-1423 (2005)
   PUBMED   15733851
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA778478.1, AC106800.2 and BC036422.2.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036422.2, SRR1803617.62469.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326035.6/ ENSP00000313572.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..436
                     /product="serine/threonine-protein kinase NIM1"
                     /EC_number="2.7.11.1"
                     /calculated_mol_wt=49475
     Region          23..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY84.1)"
     Region          71..325
                     /region_name="STKc_NIM1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     NIM1; cd14075"
                     /db_xref="CDD:270977"
     Site            order(80..84,88,101,103,134,150..153,157,159..160,162,
                     195..196,198,200..201,203,213..214,217,231..235,237,
                     267..270)
                     /site_type="active"
                     /db_xref="CDD:270977"
     Site            order(80..83,88,101,103,134,150..153,157,200..201,203,
                     213..214)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270977"
     Site            order(157,159..160,162,196,198,200,217,231..235,237,
                     267..270)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270977"
     Site            213..235
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270977"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15733851; propagated from
                     UniProtKB/Swiss-Prot (Q8IY84.1)"
     CDS             1..436
                     /gene="NIM1K"
                     /gene_synonym="NIM1"
                     /coded_by="NM_153361.4:882..2192"
                     /db_xref="CCDS:CCDS3943.1"
                     /db_xref="GeneID:167359"
                     /db_xref="HGNC:HGNC:28646"
ORIGIN      
        1 mtavymnggg lvnphyarwd rrdsvesgcq tesskegeeg qprqltpfek ltqdmsqdek
       61 vvreitlgkr igfyrirgei gsgnfsqvkl gihsltkekv aikildktkl dqktqrllsr
      121 eissmeklhh pniirlyevv etlsklhlvm eyagggelfg kistegklse pesklifsqi
      181 vsavkhmhen qiihrdlkae nvfytsntcv kvgdfgfstv skkgemlntf cgsppyaape
      241 lfrdehyigi yvdiwalgvl lyfmvtgtmp fraetvaklk ksilegtysv pphvsepchr
      301 lirgvlqqip terygidcim ndewmqgvpy ptplepfqld pkhlsetstl keeenevkst
      361 lehlgiteeh irnnqgrdar ssitgvyrii lhrvqrkkal esvpvmmlpd pkerdlkkgs
      421 rvyrgirhts kfcsil
//
LOCUS       NP_004943                238 aa            linear   PRI 27-APR-2025
DEFINITION  ephrin-A3 precursor [Homo sapiens].
ACCESSION   NP_004943
VERSION     NP_004943.1
DBSOURCE    REFSEQ: accession NM_004952.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Yiminniyaze,R., Zhang,X., Zhu,N., Wang,J., Li,C., Wumaier,G.,
            Zhou,D., Li,J., Xia,J., Zhang,Y., Dong,L., Zhang,Y. and Li,S.
  TITLE     EphrinA3 is a key regulator of malignant behaviors and a potential
            prognostic factor in lung adenocarcinoma
  JOURNAL   Cancer Med 12 (2), 1630-1642 (2023)
   PUBMED   35770949
  REMARK    GeneRIF: EphrinA3 is a key regulator of malignant behaviors and a
            potential prognostic factor in lung adenocarcinoma.
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Ye,B., Liang,X., Zhao,Y., Cai,X., Wang,Z., Lin,S., Wang,W.,
            Shan,P., Huang,W. and Huang,Z.
  TITLE     Hsa_circ_0007478 aggravates NLRP3 inflammasome activation and lipid
            metabolism imbalance in ox-LDL-stimulated macrophage via
            miR-765/EFNA3 axis
  JOURNAL   Chem Biol Interact 368, 110195 (2022)
   PUBMED   36191606
  REMARK    GeneRIF: Hsa_circ_0007478 aggravates NLRP3 inflammasome activation
            and lipid metabolism imbalance in ox-LDL-stimulated macrophage via
            miR-765/EFNA3 axis.
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Zhuang,Y., Cheng,M., Li,M., Cui,J., Huang,J., Zhang,C., Si,J.,
            Lin,K. and Yu,H.
  TITLE     Small extracellular vesicles derived from hypoxic mesenchymal stem
            cells promote vascularized bone regeneration through the
            miR-210-3p/EFNA3/PI3K pathway
  JOURNAL   Acta Biomater 150, 413-426 (2022)
   PUBMED   35850484
  REMARK    GeneRIF: Small extracellular vesicles derived from hypoxic
            mesenchymal stem cells promote vascularized bone regeneration
            through the miR-210-3p/EFNA3/PI3K pathway.
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Husain,A., Chiu,Y.T., Sze,K.M., Ho,D.W., Tsui,Y.M., Suarez,E.M.S.,
            Zhang,V.X., Chan,L.K., Lee,E., Lee,J.M., Cheung,T.T., Wong,C.C.,
            Chung,C.Y. and Ng,I.O.
  TITLE     Ephrin-A3/EphA2 axis regulates cellular metabolic plasticity to
            enhance cancer stemness in hypoxic hepatocellular carcinoma
  JOURNAL   J Hepatol 77 (2), 383-396 (2022)
   PUBMED   35227773
  REMARK    GeneRIF: Ephrin-A3/EphA2 axis regulates cellular metabolic
            plasticity to enhance cancer stemness in hypoxic hepatocellular
            carcinoma.
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Jiang,B., Yang,K., Tang,C., Chen,R. and Wang,C.
  TITLE     LncRNA LINC01270 aggravates the progression of gastric cancer
            through modulation of miR-326/EFNA3 axis
  JOURNAL   Bioengineered 13 (4), 8994-9005 (2022)
   PUBMED   35345980
  REMARK    GeneRIF: LncRNA LINC01270 aggravates the progression of gastric
            cancer through modulation of miR-326/EFNA3 axis.
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Zhou,R.
  TITLE     The Eph family receptors and ligands
  JOURNAL   Pharmacol Ther 77 (3), 151-181 (1998)
   PUBMED   9576626
  REMARK    Review article
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Flanagan,J.G. and Vanderhaeghen,P.
  TITLE     The ephrins and Eph receptors in neural development
  JOURNAL   Annu Rev Neurosci 21, 309-345 (1998)
   PUBMED   9530499
  REMARK    Review article
REFERENCE   8  (residues 1 to 238)
  AUTHORS   Cerretti,D.P., Lyman,S.D., Kozlosky,C.J., Copeland,N.G.,
            Gilbert,D.J., Jenkins,N.A., Valentine,V., Kirstein,M.N.,
            Shapiro,D.N. and Morris,S.W.
  TITLE     The genes encoding the eph-related receptor tyrosine kinase ligands
            LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4,
            Epl4) are clustered on human chromosome 1 and mouse chromosome 3
  JOURNAL   Genomics 33 (2), 277-282 (1996)
   PUBMED   8660976
REFERENCE   9  (residues 1 to 238)
  AUTHORS   Kozlosky,C.J., Maraskovsky,E., McGrew,J.T., VandenBos,T., Teepe,M.,
            Lyman,S.D., Srinivasan,S., Fletcher,F.A., Gayle,R.B. 3rd,
            Cerretti,D.P. et al.
  TITLE     Ligands for the receptor tyrosine kinases hek and elk: isolation of
            cDNAs encoding a family of proteins
  JOURNAL   Oncogene 10 (2), 299-306 (1995)
   PUBMED   7838529
REFERENCE   10 (residues 1 to 238)
  AUTHORS   Davis,S., Gale,N.W., Aldrich,T.H., Maisonpierre,P.C., Lhotak,V.,
            Pawson,T., Goldfarb,M. and Yancopoulos,G.D.
  TITLE     Ligands for EPH-related receptor tyrosine kinases that require
            membrane attachment or clustering for activity
  JOURNAL   Science 266 (5186), 816-819 (1994)
   PUBMED   7973638
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL691442.32.
            
            Summary: This gene encodes a member of the ephrin (EPH) family. The
            ephrins and EPH-related receptors comprise the largest subfamily of
            receptor protein-tyrosine kinases and have been implicated in
            mediating developmental events, especially in the nervous system
            and in erythropoiesis. Based on their structures and sequence
            relationships, ephrins are divided into the ephrin-A (EFNA) class,
            which are anchored to the membrane by a
            glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB)
            class, which are transmembrane proteins. This gene encodes an EFNA
            class ephrin. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.438053.1,
                                           SRR3476690.820847.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368408.4/ ENSP00000357393.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..238
                     /product="ephrin-A3 precursor"
                     /note="ligand of eph-related kinase 3; eph-related
                     receptor tyrosine kinase ligand 3; EFL-2; LERK-3; EHK1
                     ligand"
                     /calculated_mol_wt=23918
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2450
     Region          31..166
                     /region_name="Ephrin-A_Ectodomain"
                     /note="Ectodomain of Ephrin A; cd10425"
                     /db_xref="CDD:259896"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P52797.1)"
     Site            order(58,105..109,121..122,129..134,136..137)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:259896"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P52797.1)"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P52797.1)"
     CDS             1..238
                     /gene="EFNA3"
                     /gene_synonym="EFL2; Ehk1-L; EPLG3; LERK3"
                     /coded_by="NM_004952.5:106..822"
                     /db_xref="CCDS:CCDS1090.1"
                     /db_xref="GeneID:1944"
                     /db_xref="HGNC:HGNC:3223"
                     /db_xref="MIM:601381"
ORIGIN      
        1 maaaplllll llvpvpllpl laqgpggalg nrhavywnss nqhlrregyt vqvnvndyld
       61 iycphynssg vgpgagpgpg ggaeqyvlym vsrngyrtcn asqgfkrwec nrphaphspi
      121 kfsekfqrys afslgyefha gheyyyistp thnlhwkclr mkvfvccast shsgekpvpt
      181 lpqftmgpnv kinvledfeg enpqvpklek sisgtspkre hlplavgiaf flmtflas
//
LOCUS       NP_005300                496 aa            linear   PRI 27-APR-2025
DEFINITION  alanine aminotransferase 1 [Homo sapiens].
ACCESSION   NP_005300
VERSION     NP_005300.1
DBSOURCE    REFSEQ: accession NM_005309.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Fan,X., Rong,H., Wang,Y., Li,M., Song,W., Su,A. and Yu,T.
  TITLE     The correlation between serum total bile acid and alanine
            aminotransferase of pregnant women and the disorders of neonatal
            hyperbilirubinemia-related amino acid metabolism
  JOURNAL   BMC Pregnancy Childbirth 24 (1), 26 (2024)
   PUBMED   38172739
  REMARK    GeneRIF: The correlation between serum total bile acid and alanine
            aminotransferase of pregnant women and the disorders of neonatal
            hyperbilirubinemia-related amino acid metabolism.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Zhang,C., Xu,Q., Xu,C., Yang,K., Xia,T., Hasi,W., Hao,M. and
            Kuang,H.
  TITLE     Sex Differences in the Association Between AST/ALT and Incidence of
            Type 2 Diabetes in Japanese Patients with Nonalcoholic Fatty Liver
            Disease: A Retrospective Cohort Study
  JOURNAL   Endocr Res 49 (1), 1-11 (2024)
   PUBMED   37752709
  REMARK    GeneRIF: Sex Differences in the Association Between AST/ALT and
            Incidence of Type 2 Diabetes in Japanese Patients with Nonalcoholic
            Fatty Liver Disease: A Retrospective Cohort Study.
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Qin,Y.J., Wang,Z.G., Gong,J.H., Gong,J.P. and Li,J.H.
  TITLE     Role of alanine aminotransferase in the effects of urinary caffeine
            concentration and its primary metabolite concentration on cognitive
            function in older adults: Bayesian Kernel Machine regression
            analysis and mediation analysis
  JOURNAL   Eur Rev Med Pharmacol Sci 28 (2), 721-733 (2024)
   PUBMED   38305614
  REMARK    GeneRIF: Role of alanine aminotransferase in the effects of urinary
            caffeine concentration and its primary metabolite concentration on
            cognitive function in older adults: Bayesian Kernel Machine
            regression analysis and mediation analysis.
REFERENCE   4  (residues 1 to 496)
  AUTHORS   He,S., Yu,C., Kuang,M., Qiu,J., Yang,R., Zhang,S., Sheng,G. and
            Zou,Y.
  TITLE     Alanine aminotransferase to high- density lipoprotein cholesterol
            ratio is positively correlated with the occurrence of diabetes in
            the Chinese population: a population-based cohort study
  JOURNAL   Front Endocrinol (Lausanne) 14, 1266692 (2023)
   PUBMED   38089616
  REMARK    GeneRIF: Alanine aminotransferase to high- density lipoprotein
            cholesterol ratio is positively correlated with the occurrence of
            diabetes in the Chinese population: a population-based cohort
            study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Asgari,S., Molavizadeh,D., Tohidi,M., Momenan,A.A., Azizi,F. and
            Hadaegh,F.
  TITLE     Prevalence and metabolic determinants of abnormal alanine
            aminotransferase: A cross-sectional study of Iranian adults,
            2018-2022
  JOURNAL   J Clin Lab Anal 37 (11-12), e24937 (2023)
   PUBMED   37403787
  REMARK    GeneRIF: Prevalence and metabolic determinants of abnormal alanine
            aminotransferase: A cross-sectional study of Iranian adults,
            2018-2022.
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Ishiguro,M., Takio,K., Suzuki,M., Oyama,R., Matsuzawa,T. and
            Titani,K.
  TITLE     Complete amino acid sequence of human liver cytosolic alanine
            aminotransferase (GPT) determined by a combination of conventional
            and mass spectral methods
  JOURNAL   Biochemistry 30 (43), 10451-10457 (1991)
   PUBMED   1931970
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Rocha,J., Amorim,A., Almeida,V.M., Oliveira,J.P., Leao,M.,
            Tavares,M.C., Pereira,M.S. and Vidal-Pinheiro,L.
  TITLE     Gene dosage evidence for the regional assignment of GPT
            (glutamate-pyruvate transaminase; E.C. 2.6.1.2) locus to
            8q24.2----8qter
  JOURNAL   Hum Genet 80 (3), 299-300 (1988)
   PUBMED   3192219
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Astrin,K.H., Arredondo-Vega,F.X., Desnick,R.J. and Smith,M.
  TITLE     Assignment of the gene for cytosolic alanine aminotransferase
            (AAT1) to human chromosome 8
  JOURNAL   Ann Hum Genet 46 (2), 125-133 (1982)
   PUBMED   7114790
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Olaisen,B.
  TITLE     Genetics of the GPT system. Family, mother/child and association
            studies
  JOURNAL   Clin Genet 7 (3), 245-254 (1975)
   PUBMED   49232
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Chen,S.H. and Giblett,E.R.
  TITLE     Polymorphism of soluble glutamic-pyruvic transaminase: a new
            genetic marker in man
  JOURNAL   Science 173 (3992), 148-149 (1971)
   PUBMED   5581908
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP275218.1, BT006992.1 and
            AI283141.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes cytosolic alanine aminotransaminase 1
            (ALT1); also known as glutamate-pyruvate transaminase 1. This
            enzyme catalyzes the reversible transamination between alanine and
            2-oxoglutarate to generate pyruvate and glutamate and, therefore,
            plays a key role in the intermediary metabolism of glucose and
            amino acids. Serum activity levels of this enzyme are routinely
            used as a biomarker of liver injury caused by drug toxicity,
            infection, alcohol, and steatosis. A related gene on chromosome 16
            encodes a putative mitochondrial alanine
            aminotransaminase.[provided by RefSeq, Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.911110.1,
                                           SRR1660807.79276.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: relevant for disease process
            MANE Ensembl match     :: ENST00000394955.3/ ENSP00000378408.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..496
                     /product="alanine aminotransferase 1"
                     /EC_number="2.6.1.2"
                     /note="glutamic-alanine transaminase 1; glutamic--pyruvic
                     transaminase 1; alanine aminotransferase; glutamate
                     pyruvate transaminase 1; glutamic-pyruvate transaminase
                     (alanine aminotransferase)"
                     /calculated_mol_wt=54506
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:1931970; propagated from
                     UniProtKB/Swiss-Prot (P24298.3)"
     Region          17..496
                     /region_name="PTZ00377"
                     /note="alanine aminotransferase; Provisional"
                     /db_xref="CDD:240391"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P24298.3)"
     CDS             1..496
                     /gene="GPT"
                     /gene_synonym="AAT1; ALT; ALT1; GPT1; SGPT"
                     /coded_by="NM_005309.3:166..1656"
                     /db_xref="CCDS:CCDS6430.1"
                     /db_xref="GeneID:2875"
                     /db_xref="HGNC:HGNC:4552"
                     /db_xref="MIM:138200"
ORIGIN      
        1 masstgdrsq avrhglrakv ltldgmnprv rrveyavrgp ivqraleleq elrqgvkkpf
       61 teviranigd aqamgqrpit flrqvlalcv npdllsspnf pddakkraer ilqacgghsl
      121 gaysvssgiq liredvaryi errdggipad pnnvflstga sdaivtvlkl lvageghtrt
      181 gvlipipqyp lysatlaelg avqvdyylde erawaldvae lhralgqard hcrpralcvi
      241 npgnptgqvq trecieavir fafeerlfll adevyqdnvy aagsqfhsfk kvlmemgppy
      301 agqqelasfh stskgymgec gfrggyvevv nmdaavqqqm lklmsvrlcp pvpgqalldl
      361 vvsppaptdp sfaqfqaekq avlaelaaka klteqvfnea pgiscnpvqg amysfprvql
      421 ppraveraqe lglapdmffc lrlleetgic vvpgsgfgqr egtyhfrmti lppleklrll
      481 leklsrfhak ftleys
//
LOCUS       NP_001355102             151 aa            linear   PRI 27-APR-2025
DEFINITION  D-aspartate oxidase isoform f [Homo sapiens].
ACCESSION   NP_001355102
VERSION     NP_001355102.1
DBSOURCE    REFSEQ: accession NM_001368173.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Rabattoni,V., Motta,Z., Miceli,M., Molla,G., Fissore,A.,
            Adinolfi,S., Pollegioni,L. and Sacchi,S.
  TITLE     On the regulation of human D-aspartate oxidase
  JOURNAL   Protein Sci 32 (11), e4802 (2023)
   PUBMED   37805834
  REMARK    GeneRIF: On the regulation of human D-aspartate oxidase.
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Lombardo,B., Pagani,M., De Rosa,A., Nunziato,M., Migliarini,S.,
            Garofalo,M., Terrile,M., D'Argenio,V., Galbusera,A., Nuzzo,T.,
            Ranieri,A., Vitale,A., Leggiero,E., Di Maio,A., Barsotti,N.,
            Borello,U., Napolitano,F., Mandarino,A., Carotenuto,M.,
            Heresco-Levy,U., Pasqualetti,M., Malatesta,P., Gozzi,A., Errico,F.,
            Salvatore,F., Pastore,L. and Usiello,A.
  TITLE     D-aspartate oxidase gene duplication induces social recognition
            memory deficit in mice and intellectual disabilities in humans
  JOURNAL   Transl Psychiatry 12 (1), 305 (2022)
   PUBMED   35915065
  REMARK    GeneRIF: D-aspartate oxidase gene duplication induces social
            recognition memory deficit in mice and intellectual disabilities in
            humans.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Chen,A.S., Liu,H., Wu,Y., Luo,S., Patz,E.F. Jr., Glass,C., Su,L.,
            Du,M., Christiani,D.C. and Wei,Q.
  TITLE     Genetic variants in DDO and PEX5L in peroxisome-related pathways
            predict non-small cell lung cancer survival
  JOURNAL   Mol Carcinog 61 (7), 619-628 (2022)
   PUBMED   35502931
  REMARK    GeneRIF: Genetic variants in DDO and PEX5L in peroxisome-related
            pathways predict non-small cell lung cancer survival.
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Rabattoni,V., Pollegioni,L., Tedeschi,G., Maffioli,E. and Sacchi,S.
  TITLE     Cellular studies of the two main isoforms of human d-aspartate
            oxidase
  JOURNAL   FEBS J 288 (16), 4939-4954 (2021)
   PUBMED   33650155
  REMARK    GeneRIF: Cellular studies of the two main isoforms of human
            d-aspartate oxidase.
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Molla,G., Chaves-Sanjuan,A., Savinelli,A., Nardini,M. and
            Pollegioni,L.
  TITLE     Structure and kinetic properties of human d-aspartate oxidase, the
            enzyme-controlling d-aspartate levels in brain
  JOURNAL   FASEB J 34 (1), 1182-1197 (2020)
   PUBMED   31914658
  REMARK    GeneRIF: three-dimensional structural analysis contributes insights
            into the structure-function relationships of human DASPO
REFERENCE   6  (residues 1 to 151)
  AUTHORS   Setoyama,C. and Miura,R.
  TITLE     Structural and functional characterization of the human brain
            D-aspartate oxidase
  JOURNAL   J Biochem 121 (4), 798-803 (1997)
   PUBMED   9163533
REFERENCE   7  (residues 1 to 151)
  AUTHORS   Simonic,T., Duga,S., Negri,A., Tedeschi,G., Malcovati,M.,
            Tenchini,M.L. and Ronchi,S.
  TITLE     cDNA cloning and expression of the flavoprotein D-aspartate oxidase
            from bovine kidney cortex
  JOURNAL   Biochem J 322 (Pt 3) (Pt 3), 729-735 (1997)
   PUBMED   9148742
REFERENCE   8  (residues 1 to 151)
  AUTHORS   Nagasaki,H.
  TITLE     Gender-related differences of mouse liver D-aspartate oxidase in
            the activity and response to administration of D-aspartate and
            peroxisome proliferators
  JOURNAL   Int J Biochem 26 (3), 415-423 (1994)
   PUBMED   8187937
REFERENCE   9  (residues 1 to 151)
  AUTHORS   Van Veldhoven,P.P., Brees,C. and Mannaerts,G.P.
  TITLE     D-aspartate oxidase, a peroxisomal enzyme in liver of rat and man
  JOURNAL   Biochim Biophys Acta 1073 (1), 203-208 (1991)
   PUBMED   1991137
REFERENCE   10 (residues 1 to 151)
  AUTHORS   Barker,R.F. and Hopkinson,D.A.
  TITLE     The genetic and biochemical properties of the D-amino acid oxidases
            in human tissues
  JOURNAL   Ann Hum Genet 41 (1), 27-42 (1977)
   PUBMED   21608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL050350.14.
            
            Summary: The protein encoded by this gene is a peroxisomal
            flavoprotein that catalyzes the oxidative deamination of
            D-aspartate and N-methyl D-aspartate. Flavin adenine dinucleotide
            or 6-hydroxyflavin adenine dinucleotide can serve as the cofactor
            in this reaction. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jan
            2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.140721.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..151
                     /product="D-aspartate oxidase isoform f"
                     /EC_number="1.4.3.1"
                     /note="aspartic oxidase; D-aspartate oxidase, DDO"
                     /calculated_mol_wt=16252
     Region          5..>79
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
     CDS             1..151
                     /gene="DDO"
                     /gene_synonym="DASOX; DASPO; DDO-1; DDO-2"
                     /coded_by="NM_001368173.1:114..569"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:8528"
                     /db_xref="HGNC:HGNC:2727"
                     /db_xref="MIM:124450"
ORIGIN      
        1 mdtariavvg agvvglstav cisklvprcs vtiisdkftp dttsdvaagm liphtypdtp
       61 ihtqkqwfre tfnhlfaian saeagdagvh lvsgikgsgg wtltrriedl welhpsfdiv
      121 vncsglgsrq lagdskifpn ifyfflnmkn n
//
LOCUS       NP_073585               1445 aa            linear   PRI 27-APR-2025
DEFINITION  tensin-3 isoform 3 [Homo sapiens].
ACCESSION   NP_073585
VERSION     NP_073585.8
DBSOURCE    REFSEQ: accession NM_022748.12
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1445)
  AUTHORS   Juilland,M., Alouche,N., Ubezzi,I., Gonzalez,M., Rashid,H.O.,
            Scarpellino,L., Erdmann,T., Grau,M., Lenz,G., Luther,S.A. and
            Thome,M.
  TITLE     Identification of Tensin-3 as a MALT1 substrate that controls B
            cell adhesion and lymphoma dissemination
  JOURNAL   Proc Natl Acad Sci U S A 120 (52), e2301155120 (2023)
   PUBMED   38109544
  REMARK    GeneRIF: Identification of Tensin-3 as a MALT1 substrate that
            controls B cell adhesion and lymphoma dissemination.
REFERENCE   2  (residues 1 to 1445)
  AUTHORS   Zhang,S., van de Peppel,J., Koedam,M., van Leeuwen,J.P.T.M. and van
            der Eerden,B.C.J.
  TITLE     Tensin-3 is involved in osteogenic versus adipogenic fate of human
            bone marrow stromal cells
  JOURNAL   Cell Mol Life Sci 80 (9), 277 (2023)
   PUBMED   37668682
  REMARK    GeneRIF: Tensin-3 is involved in osteogenic versus adipogenic fate
            of human bone marrow stromal cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1445)
  AUTHORS   Wu,Y., Zhang,H.Q., Tang,M., Guo,C., Liu,S., Li,J., Wang,Y., Xiao,L.
            and Yang,G.
  TITLE     Abnormal TNS3 gene methylation in patients with congenital
            scoliosis
  JOURNAL   BMC Musculoskelet Disord 23 (1), 797 (2022)
   PUBMED   35987623
  REMARK    GeneRIF: Abnormal TNS3 gene methylation in patients with congenital
            scoliosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1445)
  AUTHORS   Zuidema,A., Atherton,P., Kreft,M., Hoekman,L., Bleijerveld,O.B.,
            Nagaraj,N., Chen,N., Fassler,R. and Sonnenberg,A.
  TITLE     PEAK1 Y635 phosphorylation regulates cell migration through
            association with Tensin3 and integrins
  JOURNAL   J Cell Biol 221 (8) (2022)
   PUBMED   35687021
  REMARK    GeneRIF: PEAK1 Y635 phosphorylation regulates cell migration
            through association with Tensin3 and integrins.
REFERENCE   5  (residues 1 to 1445)
  AUTHORS   Park,G.C., Kim,J.M., Shin,S.C., Cheon,Y.I., Sung,E.S., Lee,M.,
            Lee,J.C. and Lee,B.J.
  TITLE     Tensin Regulates Fundamental Biological Processes by Interacting
            with Integrins of Tonsil-Derived Mesenchymal Stem Cells
  JOURNAL   Cells 11 (15), 2333 (2022)
   PUBMED   35954177
  REMARK    GeneRIF: Tensin Regulates Fundamental Biological Processes by
            Interacting with Integrins of Tonsil-Derived Mesenchymal Stem
            Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1445)
  AUTHORS   Liao,Y.C., Si,L., deVere White,R.W. and Lo,S.H.
  TITLE     The phosphotyrosine-independent interaction of DLC-1 and the SH2
            domain of cten regulates focal adhesion localization and growth
            suppression activity of DLC-1
  JOURNAL   J Cell Biol 176 (1), 43-49 (2007)
   PUBMED   17190795
REFERENCE   7  (residues 1 to 1445)
  AUTHORS   Maeda,I., Takano,T., Yoshida,H., Matsuzuka,F., Amino,N. and
            Miyauchi,A.
  TITLE     Tensin3 is a novel thyroid-specific gene
  JOURNAL   J Mol Endocrinol 36 (1), R1-R8 (2006)
   PUBMED   16461921
  REMARK    Review article
REFERENCE   8  (residues 1 to 1445)
  AUTHORS   Jones,R.B., Gordus,A., Krall,J.A. and MacBeath,G.
  TITLE     A quantitative protein interaction network for the ErbB receptors
            using protein microarrays
  JOURNAL   Nature 439 (7073), 168-174 (2006)
   PUBMED   16273093
REFERENCE   9  (residues 1 to 1445)
  AUTHORS   Cui,Y., Liao,Y.C. and Lo,S.H.
  TITLE     Epidermal growth factor modulates tyrosine phosphorylation of a
            novel tensin family member, tensin3
  JOURNAL   Mol Cancer Res 2 (4), 225-232 (2004)
   PUBMED   15140944
  REMARK    GeneRIF: Tensin3 may function as a platform for the disassembly of
            EGF-related signaling complexes at focal adhesions.
REFERENCE   10 (residues 1 to 1445)
  AUTHORS   Carson-Walter,E.B., Watkins,D.N., Nanda,A., Vogelstein,B.,
            Kinzler,K.W. and St Croix,B.
  TITLE     Cell surface tumor endothelial markers are conserved in mice and
            humans
  JOURNAL   Cancer Res 61 (18), 6649-6655 (2001)
   PUBMED   11559528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK092864.1, AC092000.3, AC073341.10, AF417489.1 and AF378756.1.
            
            On May 14, 2005 this sequence version replaced NP_073585.7.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749644.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311160.14/ ENSP00000312143.9
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.3"
     Protein         1..1445
                     /product="tensin-3 isoform 3"
                     /note="tensin-like SH2 domain containing 1; tumor
                     endothelial marker 6; thyroid specific PTB domain protein;
                     tensin-like SH2 domain-containing protein 1"
                     /calculated_mol_wt=155135
     Region          8..166
                     /region_name="PTP_tensin-3"
                     /note="protein tyrosine phosphatase-like domain of
                     tensin-3; cd14561"
                     /db_xref="CDD:350409"
     Region          173..299
                     /region_name="PTEN_C2"
                     /note="C2 domain of PTEN tumour-suppressor protein;
                     pfam10409"
                     /db_xref="CDD:463081"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:26166433; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Region          358..421
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Region          538..568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSZ5; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Region          618..695
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Region          <624..1058
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSZ5; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSZ5; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Region          717..769
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            811
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Region          859..981
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Region          1076..1127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            1149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Site            1154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Region          1168..1284
                     /region_name="SH2_Tensin_like"
                     /note="Src homology 2 domain found in Tensin-like
                     proteins; cd09927"
                     /db_xref="CDD:198181"
     Site            order(1179,1197,1236,1238)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198181"
     Site            order(1237,1267)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198181"
     Site            1293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     Region          1308..1439
                     /region_name="PTB_tensin"
                     /note="Tensin Phosphotyrosine-binding (PTB) domain;
                     cd01213"
                     /db_xref="CDD:269924"
     Site            order(1314,1398,1419)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269924"
     Site            order(1378..1383,1405,1428,1432)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269924"
     Site            1441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q68CZ2.2)"
     CDS             1..1445
                     /gene="TNS3"
                     /gene_synonym="TEM6; TENS1"
                     /coded_by="NM_022748.12:326..4663"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS5506.2"
                     /db_xref="GeneID:64759"
                     /db_xref="HGNC:HGNC:21616"
                     /db_xref="MIM:606825"
ORIGIN      
        1 meeghgldlt yiteriiavs fpagcseesy lhnlqevtrm lkskhgdnyl vlnlsekryd
       61 ltklnpkimd vgwpelhapp ldkmcticka qeswlnsnlq hvvvihcrgg kgrigvviss
      121 ymhftnvsas adqaldrfam kkfyddkvsa lmqpsqkryv qflsgllsgs vkmnasplfl
      181 hfvilhgtpn fdtggvcrpf lklyqamqpv ytsgiynvgp enpsricivi epaqllkgdv
      241 mvkcyhkkyr satrdvifrl qfhtgavqgy glvfgkedld naskddrfpd ygkvelvfsa
      301 tpekiqgseh lyndhgvivd ynttdplirw dsyenlsadg evlhtqgpvd gslyakvrkk
      361 sssdpgipgg pqaipatnsp dhsdhtlsvs sdsghstasa rtdkteerla pgtrrglsaq
      421 ekaeldqlls gfgledpgss lkemtdarsk ysgtrhvvpa qvhvngdaal kdretdildd
      481 emphhdlhsv dslgtlssse gpqsahlgpf tchkssqnsl lsdgfgsnvg edpqgtlvpd
      541 lglgmdgpye rertfgsrep kqpqpllrkp svsaqmqayg qssystqtwv rqqqmvvahq
      601 ysfapdgear lvsrcpadnp glvqaqprvp ltptrgtssr vavqrgvgsg phppdtqqps
      661 pskafkprfp gdqvvngagp elstgpspgs ptldidqsie qlnrlileld ptfepipthm
      721 nalgsqangs vspdsvgggl rassrlpdtg egpsratgrq gssaeqplgg rlrklslgqy
      781 dndaggqlpf skcawgkagv dyapnlppfp spadvketmt pgypqdldii dgrilsskes
      841 mcstpafpvs petpyvktal rhppfsppep plsspasqhk ggreprscpe tlthavgmse
      901 spigpkstml radasstpsf qqafasscti ssngpgqrre ssssaerqwv esspkpmvsl
      961 lgsgrptgsp lsaefsgtrk dspvlscfpp selqapfhsh elslaeppds lappssqafl
     1021 gfgtapvgsg lppeedlgal lanshgaspt psipltatga adngflshnf ltvapghssh
     1081 hspglqgqgv tlpgqpplpe kkrasegdrs lgsvspsssg fssphsgsti sipfpnvlpd
     1141 fskaseaasp lpdspgdklv ivkfvqdtsk fwykadisre qaiamlkdke pgsfivrdsh
     1201 sfrgayglam kvatpppsvl qlnkkagdla nelvrhflie ctpkgvrlkg csnepyfgsl
     1261 talvcqhsit plalpcklli perdpleeia esspqtaans aaellkqgaa cnvwylnsve
     1321 mesltghqai qkalsitlvq epppvstvvh fkvsaqgitl tdnqrklffr rhypvnsvif
     1381 caldpqdrkw ikdgpsskvf gfvarkqgsa tdnvchlfae hdpeqpasai vnfvskvmig
     1441 spkkv
//
LOCUS       NP_057113                339 aa            linear   PRI 27-APR-2025
DEFINITION  dehydrogenase/reductase SDR family member 7 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_057113
VERSION     NP_057113.1
DBSOURCE    REFSEQ: accession NM_016029.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Rizzotto,A., Tollis,S., Pham,N.T., Zheng,Y., Abad,M.A.,
            Wildenhain,J., Jeyaprakash,A.A., Auer,M., Tyers,M. and
            Schirmer,E.C.
  TITLE     Reduction in Nuclear Size by DHRS7 in Prostate Cancer Cells and by
            Estradiol Propionate in DHRS7-Depleted Cells
  JOURNAL   Cells 13 (1), 57 (2023)
   PUBMED   38201261
  REMARK    GeneRIF: Reduction in Nuclear Size by DHRS7 in Prostate Cancer
            Cells and by Estradiol Propionate in DHRS7-Depleted Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Jiang,K., Yang,Z., Cui,W., Su,K., Ma,J.Z., Payne,T.J. and Li,M.D.
  TITLE     An Exome-Wide Association Study Identifies New Susceptibility Loci
            for Age of Smoking Initiation in African- and European-American
            Populations
  JOURNAL   Nicotine Tob Res 21 (6), 707-713 (2019)
   PUBMED   29216386
  REMARK    GeneRIF: Single nucleotide polymorphism in DHRS7 gene is associated
            with smoking in African americans.
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Zemanova,L., Kirubakaran,P., Pato,I.H., Stambergova,H. and
            Vondrasek,J.
  TITLE     The identification of new substrates of human DHRS7 by molecular
            modeling and in vitro testing
  JOURNAL   Int J Biol Macromol 105 (Pt 1), 171-182 (2017)
   PUBMED   28687384
  REMARK    GeneRIF: identification of new substrates of human DHRS7
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Ramasamy,A., Curjuric,I., Coin,L.J., Kumar,A., McArdle,W.L.,
            Imboden,M., Leynaert,B., Kogevinas,M., Schmid-Grendelmeier,P.,
            Pekkanen,J., Wjst,M., Bircher,A.J., Sovio,U., Rochat,T.,
            Hartikainen,A.L., Balding,D.J., Jarvelin,M.R., Probst-Hensch,N.,
            Strachan,D.P. and Jarvis,D.L.
  TITLE     A genome-wide meta-analysis of genetic variants associated with
            allergic rhinitis and grass sensitization and their interaction
            with birth order
  JOURNAL   J Allergy Clin Immunol 128 (5), 996-1005 (2011)
   PUBMED   22036096
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Haeseleer,F. and Palczewski,K.
  TITLE     Short-chain dehydrogenases/reductases in retina
  JOURNAL   Methods Enzymol 316, 372-383 (2000)
   PUBMED   10800688
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL163853.4.
            
            Summary: This gene encodes a member of the short-chain
            dehydrogenases/reductases (SDR) family, which has over 46,000
            members. Members in this family are enzymes that metabolize many
            different compounds, such as steroid hormones, prostaglandins,
            retinoids, lipids and xenobiotics. [provided by RefSeq, Apr 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.247767.1,
                                           SRR1660803.234503.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153932, SAMEA2155984
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000557185.6/ ENSP00000451882.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.1"
     Protein         1..339
                     /product="dehydrogenase/reductase SDR family member 7
                     isoform 1 precursor"
                     /note="retinal short-chain dehydrogenase/reductase 4;
                     dehydrogenase/reductase (SDR family) member 7; short chain
                     dehydrogenase/reductase family 34C member 1"
                     /calculated_mol_wt=34937
     sig_peptide     1..28
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y394.1)"
                     /calculated_mol_wt=3380
     mat_peptide     29..339
                     /product="Dehydrogenase/reductase SDR family member 7.
                     /id=PRO_0000031968"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y394.1)"
                     /calculated_mol_wt=34937
     Region          48..308
                     /region_name="11beta-HSD1_like_SDR_c"
                     /note="11beta-hydroxysteroid dehydrogenase type 1
                     (11beta-HSD1)-like, classical (c) SDRs; cd05332"
                     /db_xref="CDD:187593"
     Site            order(57..62,81..83,110..112,138..140,142,161,166,
                     188..190,203,207,234..237,239,241..242)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187593"
     Site            order(115,145..149,152,155..156,159..160,163..164,168,171,
                     194..201,204..205,208..209,211..213,215..217,219..220,
                     248..252,287,296..297,299,301..302,304..306,308)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187593"
     Site            order(140,143,190..192,197,200,203,234..236,241..242,
                     245..246)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187593"
     Site            order(162,190,203,207)
                     /site_type="active"
                     /db_xref="CDD:187593"
     CDS             1..339
                     /gene="DHRS7"
                     /gene_synonym="CGI-86; retDSR4; retSDR4; SDR34C1"
                     /coded_by="NM_016029.4:90..1109"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9743.1"
                     /db_xref="GeneID:51635"
                     /db_xref="HGNC:HGNC:21524"
                     /db_xref="MIM:612833"
ORIGIN      
        1 mnwelllwll vlcalllllv qllrflradg dltllwaewq grrpeweltd mvvwvtgass
       61 gigeelayql sklgvslvls arrvhelerv krrclengnl kekdilvlpl dltdtgshea
      121 atkavlqefg ridilvnngg msqrslcmdt sldvyrklie lnylgtvslt kcvlphmier
      181 kqgkivtvns ilgiisvpls igycaskhal rgffnglrte latypgiivs nicpgpvqsn
      241 ivenslagev tktignngdq shkmttsrcv rlmlismand lkevwiseqp fllvtylwqy
      301 mptwawwitn kmgkkrienf ksgvdadssy fkifktkhd
//
LOCUS       NP_001278928             377 aa            linear   PRI 27-APR-2025
DEFINITION  SH2/SH3 adapter protein NCK1 isoform 1 [Homo sapiens].
ACCESSION   NP_001278928 XP_005247555
VERSION     NP_001278928.1
DBSOURCE    REFSEQ: accession NM_001291999.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Deng,S., Zhang,Y., Wang,H., Liang,W., Xie,L., Li,N., Fang,Y.,
            Wang,Y., Liu,J., Chi,H., Sun,Y., Ye,R., Shan,L., Shi,J., Shen,Z.,
            Wang,Y., Wang,S., Brosseau,J.P., Wang,F., Liu,G., Quan,Y. and Xu,J.
  TITLE     ITPRIPL1 binds CD3epsilon to impede T cell activation and enable
            tumor immune evasion
  JOURNAL   Cell 187 (9), 2305-2323 (2024)
   PUBMED   38614099
REFERENCE   3  (residues 1 to 377)
  AUTHORS   He,P., Liu,Z., Qi,J., Shan,J. and Sheng,J.
  TITLE     Long noncoding RNA LINC00885 upregulates NCK1 to promote cell
            viability and migration of triple-negative breast cancer cells
            through sponging miR-654-3p
  JOURNAL   Cancer Biomark 39 (1), 63-78 (2024)
   PUBMED   37694355
  REMARK    GeneRIF: Long noncoding RNA LINC00885 upregulates NCK1 to promote
            cell viability and migration of triple-negative breast cancer cells
            through sponging miR-654-3p.
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Nuiyen,A., Rattanasri,A., Wipa,P., Roytrakul,S.,
            Wangteeraprasert,A., Pongcharoen,S. and Ngoenkam,J.
  TITLE     Lack of Nck1 protein and Nck-CD3 interaction caused the increment
            of lipid content in Jurkat T cells
  JOURNAL   BMC Mol Cell Biol 23 (1), 36 (2022)
   PUBMED   35902806
  REMARK    GeneRIF: Lack of Nck1 protein and Nck-CD3 interaction caused the
            increment of lipid content in Jurkat T cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Rivero-Lezcano,O.M., Marcilla,A., Sameshima,J.H. and Robbins,K.C.
  TITLE     Wiskott-Aldrich syndrome protein physically associates with Nck
            through Src homology 3 domains
  JOURNAL   Mol Cell Biol 15 (10), 5725-5731 (1995)
   PUBMED   7565724
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Rivero-Lezcano,O.M., Sameshima,J.H., Marcilla,A. and Robbins,K.C.
  TITLE     Physical association between Src homology 3 elements and the
            protein product of the c-cbl proto-oncogene
  JOURNAL   J Biol Chem 269 (26), 17363-17366 (1994)
   PUBMED   7517397
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Meisenhelder,J. and Hunter,T.
  TITLE     The SH2/SH3 domain-containing protein Nck is recognized by certain
            anti-phospholipase C-gamma 1 monoclonal antibodies, and its
            phosphorylation on tyrosine is stimulated by platelet-derived
            growth factor and epidermal growth factor treatment
  JOURNAL   Mol Cell Biol 12 (12), 5843-5856 (1992)
   PUBMED   1448108
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Park,D. and Rhee,S.G.
  TITLE     Phosphorylation of Nck in response to a variety of receptors,
            phorbol myristate acetate, and cyclic AMP
  JOURNAL   Mol Cell Biol 12 (12), 5816-5823 (1992)
   PUBMED   1333046
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Lehmann,J.M., Riethmuller,G. and Johnson,J.P.
  TITLE     Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of
            the src homology units SH2 and SH3
  JOURNAL   Nucleic Acids Res 18 (4), 1048 (1990)
   PUBMED   2107526
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA855124.1, BC006403.2 and
            AC011597.27.
            
            On May 15, 2014 this sequence version replaced XP_005247555.1.
            
            Summary: The protein encoded by this gene is one of the signaling
            and transforming proteins containing Src homology 2 and 3 (SH2 and
            SH3) domains. It is located in the cytoplasm and is an adaptor
            protein involved in transducing signals from receptor tyrosine
            kinases to downstream signal recipients such as RAS. Alternatively
            spliced transcript variants encoding different isoforms have been
            found. [provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1 and 3 encode the same protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.254690.1,
                                           SRR1660807.77761.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000481752.6/ ENSP00000417273.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..377
                     /product="SH2/SH3 adapter protein NCK1 isoform 1"
                     /note="NCK tyrosine kinase; non-catalytic region of
                     tyrosine kinase; SH2/SH3 adaptor protein NCK-alpha;
                     melanoma NCK protein; cytoplasmic protein NCK1; NCK
                     adapter protein 1; SH2/SH3 adapter protein NCK-alpha;
                     SH2/SH3 adapter protein NCK1"
                     /calculated_mol_wt=42733
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Region          3..61
                     /region_name="SH3_Nck1_1"
                     /note="First Src Homology 3 domain of Nck1 adaptor
                     protein; cd11900"
                     /db_xref="CDD:212833"
     Site            order(13,16..17,19..20,36..38,50,52..55)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212833"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P16333.1)"
     Region          108..162
                     /region_name="SH3_Nck1_2"
                     /note="Second Src Homology 3 domain of Nck1 adaptor
                     protein; cd11901"
                     /db_xref="CDD:212834"
     Site            order(115,117,120,124,142..143,156,158..159)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212834"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Region          193..249
                     /region_name="SH3_Nck1_3"
                     /note="Third Src Homology 3 domain of Nck1 adaptor
                     protein; cd11904"
                     /db_xref="CDD:212837"
     Site            order(199,201,204,208,228..229,243,245..246)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212837"
     Region          280..376
                     /region_name="SH2_Nck1"
                     /note="Src homology 2 (SH2) domain found in Nck; cd10408"
                     /db_xref="CDD:198271"
     Site            order(289,308,310..312,318,331)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198271"
     Site            order(330,341,344,361..363)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198271"
     CDS             1..377
                     /gene="NCK1"
                     /gene_synonym="NCK; nck-1; NCKalpha"
                     /coded_by="NM_001291999.2:165..1298"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS3092.1"
                     /db_xref="GeneID:4690"
                     /db_xref="HGNC:HGNC:7664"
                     /db_xref="MIM:600508"
ORIGIN      
        1 maeevvvvak fdyvaqqeqe ldikknerlw llddskswwr vrnsmnktgf vpsnyverkn
       61 sarkasivkn lkdtlgigkv krkpsvpdsa spaddsfvdp gerlydlnmp ayvkfnymae
      121 redelslikg tkvivmekcs dgwwrgsyng qvgwfpsnyv teegdsplgd hvgslsekla
      181 avvnnlntgq vlhvvqalyp fsssndeeln fekgdvmdvi ekpendpeww kcrkingmvg
      241 lvpknyvtvm qnnpltsgle psppqcdyir psltgkfagn pwyygkvtrh qaemalnerg
      301 hegdflirds esspndfsvs lkaqgknkhf kvqlketvyc igqrkfstme elvehykkap
      361 iftseqgekl ylvkhls
//
LOCUS       NP_005658                685 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF103 isoform 1 [Homo sapiens].
ACCESSION   NP_005658
VERSION     NP_005658.1
DBSOURCE    REFSEQ: accession NM_005667.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Scheper,J., Oliva,B., Villa-Freixa,J. and Thomson,T.M.
  TITLE     Analysis of electrostatic contributions to the selectivity of
            interactions between RING-finger domains and ubiquitin-conjugating
            enzymes
  JOURNAL   Proteins 74 (1), 92-103 (2009)
   PUBMED   18615712
  REMARK    GeneRIF: Analysis reveals that the main determinants of selectivity
            between ubiquitin ligases RNF103 and E2 ubiquitin-conjugating
            enzymes resides on ring domains, rather than on the E2s.
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Maruyama,Y., Yamada,M., Takahashi,K. and Yamada,M.
  TITLE     Ubiquitin ligase Kf-1 is involved in the endoplasmic
            reticulum-associated degradation pathway
  JOURNAL   Biochem Biophys Res Commun 374 (4), 737-741 (2008)
   PUBMED   18675248
  REMARK    GeneRIF: Kf-1 is an ER ubiquitin ligase involved in the endoplasmic
            reticulum-associated degradation pathway.
REFERENCE   3  (residues 1 to 685)
  AUTHORS   Yang,Y., Lorick,K.L., Jensen,J.P. and Weissman,A.M.
  TITLE     Expression and evaluation of RING finger proteins
  JOURNAL   Methods Enzymol 398, 103-112 (2005)
   PUBMED   16275323
REFERENCE   4  (residues 1 to 685)
  AUTHORS   Nishioka,G., Yamada,M., Kudo,K., Takahashi,K., Kiuchi,Y.,
            Higuchi,T., Momose,K., Kamijima,K. and Yamada,M.
  TITLE     Induction of kf-1 after repeated electroconvulsive treatment and
            chronic antidepressant treatment in rat frontal cortex and
            hippocampus
  JOURNAL   J Neural Transm (Vienna) 110 (3), 277-285 (2003)
   PUBMED   12658376
REFERENCE   5  (residues 1 to 685)
  AUTHORS   Yamada,M., Yamada,M., Yamazaki,S., Takahashi,K., Nishioka,G.,
            Kudo,K., Ozawa,H., Yamada,S., Kiuchi,Y., Kamijima,K., Higuchi,T.
            and Momose,K.
  TITLE     Identification of a novel gene with RING-H2 finger motif induced
            after chronic antidepressant treatment in rat brain
  JOURNAL   Biochem Biophys Res Commun 278 (1), 150-157 (2000)
   PUBMED   11071867
REFERENCE   6  (residues 1 to 685)
  AUTHORS   Lorick,K.L., Jensen,J.P., Fang,S., Ong,A.M., Hatakeyama,S. and
            Weissman,A.M.
  TITLE     RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
            ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11364-11369 (1999)
   PUBMED   10500182
REFERENCE   7  (residues 1 to 685)
  AUTHORS   Yasojima,K., Tsujimura,A., Mizuno,T., Shigeyoshi,Y., Inazawa,J.,
            Kikuno,R., Kuma,K., Ohkubo,K., Hosokawa,Y., Ibata,Y., Abe,T.,
            Miyata,T., Matsubara,K., Nakajima,K. and Hashimoto-Gotoh,T.
  TITLE     Cloning of human and mouse cDNAs encoding novel zinc finger
            proteins expressed in cerebellum and hippocampus
  JOURNAL   Biochem Biophys Res Commun 231 (2), 481-487 (1997)
   PUBMED   9070305
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA816879.1, BC035053.2,
            AW964704.1 and BC110333.1.
            
            Summary: The protein encoded by this gene contains a RING-H2
            finger, a motif known to be involved in protein-protein and
            protein-DNA interactions. This gene is highly expressed in normal
            cerebellum, but not in the cerebral cortex. The expression of the
            rat counterpart in the frontal cortex and hippocampus was shown to
            be induced by elctroconvulsive treatment (ECT) as well as chronic
            antidepressant treatment, suggesting that this gene may be a
            molecular target for ECT and antidepressants. The protein is a
            ubiquitin ligase that functions in the endoplasmic
            reticulum-associated degradation pathway. Alternative splicing of
            this gene results in multiple transcript variants. Read-through
            transcription also exists between this gene and the downstream
            CHMP3 (charged multivesicular body protein 3) gene. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035053.2, D76444.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2467147
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000237455.5/ ENSP00000237455.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..685
                     /product="E3 ubiquitin-protein ligase RNF103 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF103; zinc finger
                     protein expressed in cerebellum; zinc finger protein 103
                     homolog; RING-type E3 ubiquitin transferase RNF103"
                     /calculated_mol_wt=79274
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00237.1)"
     Site            326..346
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00237.1)"
     Site            366..386
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00237.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00237.1)"
     Region          526..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00237.1)"
     Region          615..669
                     /region_name="RING-H2_RNF103"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 103 (RNF103) and similar proteins; cd16473"
                     /db_xref="CDD:438136"
     CDS             1..685
                     /gene="RNF103"
                     /gene_synonym="HKF-1; KF-1; KF1; ZFP-103; ZFP103"
                     /coded_by="NM_005667.4:980..3037"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33237.1"
                     /db_xref="GeneID:7844"
                     /db_xref="HGNC:HGNC:12859"
                     /db_xref="MIM:602507"
ORIGIN      
        1 mwlklfflll yflvlfvlar ffeaivwyet gifatqlvdp valsfkklkt ilecrglgys
       61 glpekkdvre lveksgdlme gelysalkee easesvsstn fsgemhfyel vedtkdgiwl
      121 vqviandrsp lvgkihwekm vkkvsrfgir tgtfncssdp rycrrrgwvr stlimsvpqt
      181 stskgkvmlk eysgrkieve hifkwitaha asriktiyna ehlkeewnks dqywlkiylf
      241 anldqppaff salsikftgr vefifvnven wdnksymtdi giynmpsyil rtpegiyryg
      301 nhtgefislq amdsflrslq pevndlfvls lvlvnlmawm dlfitqgati krfvvlistl
      361 gtynslliis wlpvlgflql pyldsfyeys lkllrysntt tlaswvradw mfysshpalf
      421 lstylghgll idyfekkrrr nnnndevnan nlewlsslwd wytsylfhpi asfqnfpves
      481 dwdedpdlfl erlafpdlwl hpliptdyik nlpmwrfkcl gvqseeemse gsqdtendse
      541 sentdtlsse kevfedkqsv lhnspgtash cdaeacscan kycqtspcer kgrsygsynt
      601 nedmepdwlt wpadmlhcte cvvclenfen gcllmglpcg hvfhqncivm wlaggrhccp
      661 vcrwpsykkk qpyaqhqpls ndvps
//
LOCUS       NP_001349692             529 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein 39 isoform c [Mus musculus].
ACCESSION   NP_001349692 XP_006498895
VERSION     NP_001349692.1
DBSOURCE    REFSEQ: accession NM_001362763.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Zhou,J., Wang,R., Zhang,J., Zhu,L., Liu,W., Lu,S., Chen,P., Li,H.,
            Yin,B., Yuan,J., Qiang,B., Shu,P. and Peng,X.
  TITLE     Conserved expression of ultra-conserved noncoding RNA in mammalian
            nervous system
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1860 (12), 1159-1168 (2017)
   PUBMED   29055695
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Anderson,D.M., Cannavino,J., Li,H., Anderson,K.M., Nelson,B.R.,
            McAnally,J., Bezprozvannaya,S., Liu,Y., Lin,W., Liu,N.,
            Bassel-Duby,R. and Olson,E.N.
  TITLE     Severe muscle wasting and denervation in mice lacking the
            RNA-binding protein ZFP106
  JOURNAL   Proc Natl Acad Sci U S A 113 (31), E4494-E4503 (2016)
   PUBMED   27418600
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Faherty,N., Benson,M., Sharma,E., Lee,A., Howarth,A., Lockstone,H.,
            Ebner,D. and Bhattacharya,S.
  TITLE     Negative autoregulation of BMP dependent transcription by SIN3B
            splicing reveals a role for RBM39
  JOURNAL   Sci Rep 6, 28210 (2016)
   PUBMED   27324164
  REMARK    GeneRIF: this study shows that negative autoregulation of BMP4
            dependent transcription by SIN3B splicing reveals a role for RBM39
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Kang,Y.K., Putluri,N., Maity,S., Tsimelzon,A., Ilkayeva,O., Mo,Q.,
            Lonard,D., Michailidis,G., Sreekumar,A., Newgard,C.B., Wang,M.,
            Tsai,S.Y., Tsai,M.J. and O'Malley,B.W.
  TITLE     CAPER is vital for energy and redox homeostasis by integrating
            glucose-induced mitochondrial functions via ERR-alpha-Gabpa and
            stress-induced adaptive responses via NF-kappaB-cMYC
  JOURNAL   PLoS Genet 11 (4), e1005116 (2015)
   PUBMED   25830341
  REMARK    GeneRIF: CAPER integrates mitochondrial energy metabolism by
            coactivating ERR-alpha-Gabpa and stress-induced adaptive metabolic
            responses via NF- kappaB/c-Myc.
            Erratum:[PLoS Genet. 2015 Jun 15;11(6):e1005316. doi:
            10.1371/journal.pgen.1005316. PMID: 26075908]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Jensen,P., Magdaleno,S., Lehman,K.M., Rice,D.S., Lavallie,E.R.,
            Collins-Racie,L., McCoy,J.M. and Curran,T.
  TITLE     A neurogenomics approach to gene expression analysis in the
            developing brain
  JOURNAL   Brain Res Mol Brain Res 132 (2), 116-127 (2004)
   PUBMED   15582152
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Jung,D.J., Na,S.Y., Na,D.S. and Lee,J.W.
  TITLE     Molecular cloning and characterization of CAPER, a novel
            coactivator of activating protein-1 and estrogen receptors
  JOURNAL   J Biol Chem 277 (2), 1229-1234 (2002)
   PUBMED   11704680
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL929404.19 and BX649640.5.
            
            On Apr 26, 2018 this sequence version replaced XP_006498895.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.1295952.1,
                                           ERR3363658.2019187.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164139, SAMN01164140
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 77.36 cM"
     Protein         1..529
                     /product="RNA-binding protein 39 isoform c"
                     /note="coactivator of activating protein-1 and estrogen
                     receptors; RNA-binding region (RNP1, RRM) containing 2;
                     RNA-binding protein 39; coactivator of AP-1 and ERs;
                     transcription coactivator CAPER; RNA-binding
                     region-containing protein 2; Caper alpha"
                     /calculated_mol_wt=59189
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q14498; propagated from
                     UniProtKB/Swiss-Prot (Q8VH51.2)"
     Region          46..517
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q14498; propagated from
                     UniProtKB/Swiss-Prot (Q8VH51.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14498; propagated from
                     UniProtKB/Swiss-Prot (Q8VH51.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14498; propagated from
                     UniProtKB/Swiss-Prot (Q8VH51.2)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8VH51.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8VH51.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14498; propagated from
                     UniProtKB/Swiss-Prot (Q8VH51.2)"
     Region          290..405
                     /region_name="Interaction with JUN.
                     /evidence=ECO:0000269|PubMed:11704680"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VH51.2)"
     Region          290..354
                     /region_name="Activating domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VH51.2)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8VH51.2)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8VH51.2)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14498; propagated from
                     UniProtKB/Swiss-Prot (Q8VH51.2)"
     Region          354..405
                     /region_name="Interaction with ESR1 and ESR2.
                     /evidence=ECO:0000269|PubMed:11704680"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VH51.2)"
     Region          405..529
                     /region_name="Interaction with NCOA6.
                     /evidence=ECO:0000269|PubMed:11704680"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VH51.2)"
     CDS             1..529
                     /gene="Rbm39"
                     /gene_synonym="1500012C14Rik; 2310040E03Rik;
                     B330012G18Rik; caper; Rnpc2"
                     /coded_by="NM_001362763.1:366..1955"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:170791"
                     /db_xref="MGI:MGI:2157953"
ORIGIN      
        1 maddidieam leapykkden klnsanghee rskkrkksks rsrsherkrs kskerkrsrd
       61 rerkksksre rkrsrskerr rsrsrsrdrr frgryrspys gpkfnsairg kiglphsikl
      121 rrrsrskspf rkdkspvrep idnltpeerd artvfcmqla arirprdlee ffstvgkvrd
      181 vrmisdrnsr rskgiayvef vdvssvplai gltgqrvlgv piivqasqae knraaamann
      241 lqkgsagpmr lyvgslhfni tedmlrgife pfgriesiql mmdsetgrsk gygfitfsds
      301 ecakkaleql ngfelagrpm kvghvtertd assassflds delertgidl gttgrlqlma
      361 rlaegtglqi ppaaqqalqm sgslafgava efsfvidlqt rlsqqteasa laaaasvqpl
      421 atqcfqlsnm fnpqteeevg wdteikddvi eecnkhggvi hiyvdknsaq gnvyvkcpsi
      481 aaaiaavnal hgrwfagkmi taayvplpty hnlfpdsmta tqllvpsrr
//
LOCUS       NP_080671                196 aa            linear   ROD 27-APR-2025
DEFINITION  protein RER1 [Mus musculus].
ACCESSION   NP_080671
VERSION     NP_080671.1
DBSOURCE    REFSEQ: accession NM_026395.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Hara,T., Maejima,I., Akuzawa,T., Hirai,R., Kobayashi,H.,
            Tsukamoto,S., Tsunoda,M., Ono,A., Yamakoshi,S., Oikawa,S. and
            Sato,K.
  TITLE     Rer1-mediated quality control system is required for neural stem
            cell maintenance during cerebral cortex development
  JOURNAL   PLoS Genet 14 (9), e1007647 (2018)
   PUBMED   30260951
  REMARK    GeneRIF: Study in knockout mice and genetically modified human HAP1
            cell line suggests that Rer1 maintains Notch signaling by
            maintaining sufficient expression of the gamma-secretase complex on
            the cell surface and regulating neural stem cell maintenance during
            cerebral cortex development.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Valkova,C., Liebmann,L., Kramer,A., Hubner,C.A. and Kaether,C.
  TITLE     The sorting receptor Rer1 controls Purkinje cell function via
            voltage gated sodium channels
  JOURNAL   Sci Rep 7, 41248 (2017)
   PUBMED   28117367
  REMARK    GeneRIF: Rer1 controls the assembly and transport of Nav1.1 and
            1.6, the principal sodium channels responsible for recurrent
            firing, in Purkinje cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Jurisch-Yaksi,N., Rose,A.J., Lu,H., Raemaekers,T., Munck,S.,
            Baatsen,P., Baert,V., Vermeire,W., Scales,S.J., Verleyen,D.,
            Vandepoel,R., Tylzanowski,P., Yaksi,E., de Ravel,T., Yost,H.J.,
            Froyen,G., Arrington,C.B. and Annaert,W.
  TITLE     Rer1p maintains ciliary length and signaling by regulating
            gamma-secretase activity and Foxj1a levels
  JOURNAL   J Cell Biol 200 (6), 709-720 (2013)
   PUBMED   23479743
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Ulyanova,T., Jiang,Y., Padilla,S., Nakamoto,B. and
            Papayannopoulou,T.
  TITLE     Combinatorial and distinct roles of alpha and alpha integrins in
            stress erythropoiesis in mice
  JOURNAL   Blood 117 (3), 975-985 (2011)
   PUBMED   20956802
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Valkova,C., Albrizio,M., Roder,I.V., Schwake,M., Betto,R.,
            Rudolf,R. and Kaether,C.
  TITLE     Sorting receptor Rer1 controls surface expression of muscle
            acetylcholine receptors by ER retention of unassembled
            alpha-subunits
  JOURNAL   Proc Natl Acad Sci U S A 108 (2), 621-625 (2011)
   PUBMED   21187406
  REMARK    GeneRIF: Rer1 is a functionally important unique factor that
            controls surface expression of muscle acetylcholine receptors by
            localizing unassembled alpha-subunits to the early secretory
            pathway
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY164316.1, AK002550.1 and BM898853.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK002550.1, AK078396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135, SAMN01164137
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 86.17 cM"
     Protein         1..196
                     /product="protein RER1"
                     /note="RER1 retention in endoplasmic reticulum 1 homolog"
                     /calculated_mol_wt=22857
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:O15258; propagated from
                     UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15258; propagated from
                     UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15258; propagated from
                     UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15258; propagated from
                     UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Region          20..185
                     /region_name="Rer1"
                     /note="Rer1 family; pfam03248"
                     /db_xref="CDD:460860"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQU3.1)"
     CDS             1..196
                     /gene="Rer1"
                     /gene_synonym="1110060F11Rik; 5830454N22Rik"
                     /coded_by="NM_026395.2:157..747"
                     /db_xref="CCDS:CCDS19022.1"
                     /db_xref="GeneID:67830"
                     /db_xref="MGI:MGI:1915080"
ORIGIN      
        1 msegdsvgds vhgkpsvvyr ffsrlgqiyq swldkstpyt avrwvvtlgl sfvymirvyl
       61 lqgwyivtya lgiyhlnlfi aflspkvdps lmedsddgps lptkqneefr pfirrlpefk
      121 fwhaatkgil vamictffea fnvpvfwpil vmyfimlfci tmkrqikhmi kyryipfthg
      181 krrykgkedv gktfas
//
LOCUS       NP_001793                454 aa            linear   PRI 27-APR-2025
DEFINITION  cerebellar degeneration-related protein 2 [Homo sapiens].
ACCESSION   NP_001793 XP_071866
VERSION     NP_001793.1
DBSOURCE    REFSEQ: accession NM_001802.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Erikstad,K.I., Herdlevaer,I., Peter,E., Haugen,M., Totland,C. and
            Vedeler,C.
  TITLE     A cerebellar degeneration-related protein 2-like cell-based assay
            for anti-Yo detection in patients with paraneoplastic cerebellar
            degeneration
  JOURNAL   Eur J Neurol 30 (6), 1727-1733 (2023)
   PUBMED   36912432
  REMARK    GeneRIF: A cerebellar degeneration-related protein 2-like
            cell-based assay for anti-Yo detection in patients with
            paraneoplastic cerebellar degeneration.
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Mo,J.S. and Chae,S.C.
  TITLE     MicroRNA 452 regulates ASB8, NOL8, and CDR2 expression in
            colorectal cancer cells
  JOURNAL   Genes Genomics 43 (1), 33-41 (2021)
   PUBMED   33398662
  REMARK    GeneRIF: MicroRNA 452 regulates ASB8, NOL8, and CDR2 expression in
            colorectal cancer cells.
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Fletcher,C.F., Okano,H.J., Gilbert,D.J., Yang,Y., Yang,C.,
            Copeland,N.G., Jenkins,N.A. and Darnell,R.B.
  TITLE     Mouse chromosomal locations of nine genes encoding homologs of
            human paraneoplastic neurologic disorder antigens
  JOURNAL   Genomics 45 (2), 313-319 (1997)
   PUBMED   9344654
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Gress,T., Baldini,A., Rocchi,M., Furneaux,H., Posner,J.B. and
            Siniscalco,M.
  TITLE     In situ mapping of the gene coding for a leucine zipper DNA binding
            protein (CDR62) to 16p12-16p13.1
  JOURNAL   Genomics 13 (4), 1340-1342 (1992)
   PUBMED   1505970
REFERENCE   8  (residues 1 to 454)
  AUTHORS   Sakai,K., Mitchell,D.J., Tsukamoto,T. and Steinman,L.
  TITLE     Isolation of a complementary DNA clone encoding an autoantigen
            recognized by an anti-neuronal cell antibody from a patient with
            paraneoplastic cerebellar degeneration
  JOURNAL   Ann Neurol 30 (5), 738 (1991)
   PUBMED   1763903
  REMARK    Correction to:[Ann Neurol. 1990 Nov;28(5):692-8. doi:
            10.1002/ana.410280515. PMID: 2260856]
REFERENCE   9  (residues 1 to 454)
  AUTHORS   Fathallah-Shaykh,H., Wolf,S., Wong,E., Posner,J.B. and
            Furneaux,H.M.
  TITLE     Cloning of a leucine-zipper protein recognized by the sera of
            patients with antibody-associated paraneoplastic cerebellar
            degeneration
  JOURNAL   Proc Natl Acad Sci U S A 88 (8), 3451-3454 (1991)
   PUBMED   2014264
REFERENCE   10 (residues 1 to 454)
  AUTHORS   Sakai,K., Mitchell,D.J., Tsukamoto,T. and Steinman,L.
  TITLE     Isolation of a complementary DNA clone encoding an autoantigen
            recognized by an anti-neuronal cell antibody from a patient with
            paraneoplastic cerebellar degeneration
  JOURNAL   Ann Neurol 28 (5), 692-698 (1990)
   PUBMED   2260856
  REMARK    Erratum:[Ann Neurol. 1991 Nov;30(5):738. doi:
            10.1002/ana.410300523. PMID: 1763903]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092338.4, CB990819.1, BG386156.1, BG750955.1, BC017503.1,
            M63256.1 and BM714067.1.
            
            On Nov 22, 2004 this sequence version replaced XP_071866.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017503.1, SRR1163658.234190.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268383.7/ ENSP00000268383.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..454
                     /product="cerebellar degeneration-related protein 2"
                     /note="Yo paraneoplastic antigen; major Yo paraneoplastic
                     antigen; paraneoplastic cerebellar degeneration-associated
                     antigen; cerebellar degeneration-related protein 2, 62kDa"
                     /calculated_mol_wt=51724
     Region          <8..>263
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          134..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01850.2)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01850.2)"
     CDS             1..454
                     /gene="CDR2"
                     /gene_synonym="CDR62; Yo"
                     /coded_by="NM_001802.2:311..1675"
                     /db_xref="CCDS:CCDS32404.1"
                     /db_xref="GeneID:1039"
                     /db_xref="HGNC:HGNC:1799"
                     /db_xref="MIM:117340"
ORIGIN      
        1 mlaenlveef emkedepwyd hqdlqqdlql aaelgktlld rnteledsvq qmyttnqeql
       61 qeieyltkqv ellrqmneqh akvyeqldvt areleetnqk lvadskasqq kilsltetie
      121 clqtnidhlq sqveelkssg qgrrspgkcd qekpapsfac lkelydlrqh fvydhvfaek
      181 itslqgqpsp deeenehlkk tvtmlqaqls lerqkrvtme eeyglvlken seleqqlgat
      241 gayraralel eaevaemrqm lqsehpfvng veklvpdsly vpfkepsqsl leemfltvpe
      301 shrkplkrss setilsslag sdivkgheet cirrakavkq rgisllhevd tqysalkvky
      361 eellkkcqee qdslshkavq tsraaakdlt gvnaqsepva sgwelasvnp epvsspttpp
      421 eykalfkeif scikktkqei deqrtkyrsl sshs
//
LOCUS       NP_060047                662 aa            linear   PRI 27-APR-2025
DEFINITION  protein Aster-C isoform 1 [Homo sapiens].
ACCESSION   NP_060047
VERSION     NP_060047.3
DBSOURCE    REFSEQ: accession NM_017577.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079944.17, BC035040.1, AK292846.1 and CV575069.1.
            
            On May 10, 2008 this sequence version replaced NP_060047.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035040.1, SRR1660803.210240.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358160.9/ ENSP00000350881.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.31"
     Protein         1..662
                     /product="protein Aster-C isoform 1"
                     /note="GRAM domain-containing protein 1C; protein Aster-C"
                     /calculated_mol_wt=75904
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYS0.2)"
     Region          80..173
                     /region_name="PH-GRAM_GRAMDC"
                     /note="GRAM domain-containing protein (GRAMDC) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13220"
                     /db_xref="CDD:275406"
     Region          212..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYS0.2)"
     Region          249..284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYS0.2)"
     Region          329..476
                     /region_name="VASt"
                     /note="VAD1 Analog of StAR-related lipid transfer domain;
                     pfam16016"
                     /db_xref="CDD:464975"
     Site            557..577
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYS0.2)"
     CDS             1..662
                     /gene="GRAMD1C"
                     /coded_by="NM_017577.5:123..2111"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33826.1"
                     /db_xref="GeneID:54762"
                     /db_xref="HGNC:HGNC:25252"
                     /db_xref="MIM:620180"
ORIGIN      
        1 megaptvrqv mnegdsslat dlqedveenp sptveennvv vkkqgpnlhn wsgdwsfwis
       61 sstykdrnee yrrqfthlpd terliadyac alqrdillqg rlylsenwlc fysnifrwet
      121 tisialknit fmtkektarl ipnaiqivte sekffftsfg ardrsylsif rlwqnvlldk
      181 sltrqefwql lqqnygtelg lnaeemenls lsiedvqprs pgrsslddsg erdeklsksi
      241 sftsesisrv setesfdgns skgglgkees qnekqtkksl lptlekkltr vpsksldlnk
      301 neylsldkss tsdsvdeenv pekdlhgrlf inrifhisad rmfellftss rfmqkfassr
      361 niidvvstpw taelggdqlr tmtytivlns pltgkctaat ekqtlykesr earfylvdse
      421 vlthdvpyhd yfytvnryci irsskqkcrl rvstdlkyrk qpwglvksli eknswssled
      481 yfkqlesdll ieesvlnqai edpgkltglr rrrrtfnrta etvpklssqh ssgdvglgak
      541 gditgkkkem enynvtlivv msifvlllvl lnvtlflkls kiehaaqsfy rlrlqeeksl
      601 nlasdmvsra etiqknkdqa hrlkgvlrds ivmleqlkss limlqktfdl lnknktgmav
      661 es
//
LOCUS       NP_001357345              81 aa            linear   PRI 27-APR-2025
DEFINITION  cortexin-2 [Homo sapiens].
ACCESSION   NP_001357345 XP_011519855
VERSION     NP_001357345.1
DBSOURCE    REFSEQ: accession NM_001370416.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Zody,M.C., Garber,M., Sharpe,T., Young,S.K., Rowen,L., O'Neill,K.,
            Whittaker,C.A., Kamal,M., Chang,J.L., Cuomo,C.A., Dewar,K.,
            FitzGerald,M.G., Kodira,C.D., Madan,A., Qin,S., Yang,X., Abbasi,N.,
            Abouelleil,A., Arachchi,H.M., Baradarani,L., Birditt,B., Bloom,S.,
            Bloom,T., Borowsky,M.L., Burke,J., Butler,J., Cook,A.,
            DeArellano,K., DeCaprio,D., Dorris,L. 3rd, Dors,M., Eichler,E.E.,
            Engels,R., Fahey,J., Fleetwood,P., Friedman,C., Gearin,G.,
            Hall,J.L., Hensley,G., Johnson,E., Jones,C., Kamat,A., Kaur,A.,
            Locke,D.P., Madan,A., Munson,G., Jaffe,D.B., Lui,A., Macdonald,P.,
            Mauceli,E., Naylor,J.W., Nesbitt,R., Nicol,R., O'Leary,S.B.,
            Ratcliffe,A., Rounsley,S., She,X., Sneddon,K.M., Stewart,S.,
            Sougnez,C., Stone,S.M., Topham,K., Vincent,D., Wang,S.,
            Zimmer,A.R., Birren,B.W., Hood,L., Lander,E.S. and Nusbaum,C.
  TITLE     Analysis of the DNA sequence and duplication history of human
            chromosome 15
  JOURNAL   Nature 440 (7084), 671-675 (2006)
   PUBMED   16572171
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC066612.7.
            
            On May 7, 2019 this sequence version replaced XP_011519855.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.215556.1,
                                           SRR1660803.206848.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..81
                     /product="cortexin-2"
                     /calculated_mol_wt=8849
     Region          9..81
                     /region_name="Cortexin"
                     /note="Cortexin of kidney; pfam11057"
                     /db_xref="CDD:314086"
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C2S0.1)"
     CDS             1..81
                     /gene="CTXN2"
                     /coded_by="NM_001370416.1:465..710"
                     /db_xref="CCDS:CCDS45254.1"
                     /db_xref="GeneID:399697"
                     /db_xref="HGNC:HGNC:31109"
ORIGIN      
        1 msstycgnss akmsvnevsa fsltleqktg fafvgilcif lglliircfk illdpyssmp
       61 sstwedevee fdkgtfeyal a
//
LOCUS       NP_001278388             549 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 3L isoform 2 [Homo sapiens].
ACCESSION   NP_001278388 XP_003960742 XP_006722308
VERSION     NP_001278388.1
DBSOURCE    REFSEQ: accession NM_001291459.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Hodzic,D., Kong,C., Wainszelbaum,M.J., Charron,A.J., Su,X. and
            Stahl,P.D.
  TITLE     TBC1D3, a hominoid oncoprotein, is encoded by a cluster of
            paralogues located on chromosome 17q12
  JOURNAL   Genomics 88 (6), 731-736 (2006)
   PUBMED   16863688
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC243569.3.
            
            On or before Apr 16, 2014 this sequence version replaced
            XP_006722308.1, XP_003960742.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..549
                     /product="TBC1 domain family member 3L isoform 2"
                     /calculated_mol_wt=62056
     Region          99..312
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Region          350..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B9A6J9.1)"
     Region          <356..>468
                     /region_name="PHA03381"
                     /note="tegument protein VP22; Provisional"
                     /db_xref="CDD:177618"
     CDS             1..549
                     /gene="TBC1D3L"
                     /coded_by="NM_001291459.2:113..1762"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74043.1"
                     /db_xref="GeneID:101060376"
                     /db_xref="HGNC:HGNC:51246"
ORIGIN      
        1 mdvvevagsw waqerediim kyekghragl pedkgpkpfr synnnvdhlg ivhetelppl
       61 tareakqirr eisrkskwvd mlgdwekyks srklidrayk gmpmnirgpm wsvllnteem
      121 klknpgryqi mkekgkrsse hiqridrdvs gtlrkhiffr drygtkqrel lhillayeey
      181 npevgycrdl shiaalflly lpeedafwal vqllaserhs lqgfhspngg tvqglqdqqe
      241 hvvatsqpkt mghqdkkdlc gqcsplgcli rilidgislg ltlrlwdvyl vegeqalmpi
      301 triafkvqqk rltktsrcgp warfcnrfvd twardedtvl khlrasmkkl trkqgdlqpp
      361 akpeqgssas rpvpasrggk tlckgdrqap pgpparfprp iwsaspprap rsstpcpgga
      421 vredtypvgt qgvpspalaq ggpqgswrfl qwnsmprlpt dldvegpwfr hydfrqscwv
      481 raisqedqla pcwqaehpae rvrsafaaps tdsdqgtpfr ardeqpcapt sgpclcglhl
      541 essqfppgf
//
LOCUS       NP_001277744             654 aa            linear   ROD 27-APR-2025
DEFINITION  actin-binding LIM protein 1 isoform 5 [Mus musculus].
ACCESSION   NP_001277744 XP_006527108
VERSION     NP_001277744.1
DBSOURCE    REFSEQ: accession NM_001290815.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Chen,X., Liu,Y., Xu,C., Ba,L., Liu,Z., Li,X., Huang,J., Simpson,E.,
            Gao,H., Cao,D., Sheng,W., Qi,H., Ji,H., Sanderson,M., Cai,C.L.,
            Li,X., Yang,L., Na,J., Yamamura,K., Liu,Y., Huang,G., Shou,W. and
            Sun,N.
  TITLE     QKI is a critical pre-mRNA alternative splicing regulator of
            cardiac myofibrillogenesis and contractile function
  JOURNAL   Nat Commun 12 (1), 89 (2021)
   PUBMED   33397958
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Jin,S.H., Kim,H., Gu,D.R., Park,K.H., Lee,Y.R., Choi,Y. and
            Lee,S.H.
  TITLE     Actin-binding LIM protein 1 regulates receptor activator of
            NF-kappaB ligand-mediated osteoclast differentiation and motility
  JOURNAL   BMB Rep 51 (7), 356-361 (2018)
   PUBMED   29921413
  REMARK    GeneRIF: ABLIM1 is associated with the regulation of preosteoclast
            motility via the PI3K/Akt/Rac1 pathway during RANKL-mediated
            osteoclastogenesis.
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Zhang,Q., Huang,R., Ye,Y., Guo,X., Lu,J., Zhu,F., Gong,X.,
            Zhang,Q., Yan,J., Luo,L., Zhuang,S., Chen,Y., Zhao,X., Evans,S.M.,
            Jiang,C., Liang,X. and Sun,Y.
  TITLE     Temporal requirements for ISL1 in sympathetic neuron proliferation,
            differentiation, and diversification
  JOURNAL   Cell Death Dis 9 (2), 247 (2018)
   PUBMED   29445148
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 654)
  AUTHORS   Narahara,H., Sakai,E., Yamaguchi,Y., Narahara,S., Iwatake,M.,
            Okamoto,K., Yoshida,N. and Tsukuba,T.
  TITLE     Actin binding LIM 1 (abLIM1) negatively controls osteoclastogenesis
            by regulating cell migration and fusion
  JOURNAL   J Cell Physiol 234 (1), 486-499 (2018)
   PUBMED   29904924
  REMARK    GeneRIF: abLIM1 regulated the localization of tubulin, migration,
            and fusion in osteoclasts. Thus, these results indicate that abLIM1
            negatively controls osteoclast differentiation by regulating cell
            migration and fusion mediated via actin formation.
REFERENCE   6  (residues 1 to 654)
  AUTHORS   Erkman,L., Yates,P.A., McLaughlin,T., McEvilly,R.J., Whisenhunt,T.,
            O'Connell,S.M., Krones,A.I., Kirby,M.A., Rapaport,D.H.,
            Bermingham,J.R., O'Leary,D.D. and Rosenfeld,M.G.
  TITLE     A POU domain transcription factor-dependent program regulates axon
            pathfinding in the vertebrate visual system
  JOURNAL   Neuron 28 (3), 779-792 (2000)
   PUBMED   11163266
REFERENCE   7  (residues 1 to 654)
  AUTHORS   Suriyapperuma,S.P., Lozovatsky,L., Ciciotte,S.L., Peters,L.L. and
            Gilligan,D.M.
  TITLE     The mouse adducin gene family: alternative splicing and chromosomal
            localization
  JOURNAL   Mamm Genome 11 (1), 16-23 (2000)
   PUBMED   10602987
REFERENCE   8  (residues 1 to 654)
  AUTHORS   Kim,H.J., Noben-Trauth,K. and Morell,R.J.
  TITLE     Tectorin-beta (Tectb) maps to mouse chromosome 19
  JOURNAL   Genomics 53 (3), 419-420 (1998)
   PUBMED   9799617
REFERENCE   9  (residues 1 to 654)
  AUTHORS   Kim,A.C., Peters,L.L., Knoll,J.H., Van Huffel,C., Ciciotte,S.L.,
            Kleyn,P.W. and Chishti,A.H.
  TITLE     Limatin (LIMAB1), an actin-binding LIM protein, maps to mouse
            chromosome 19 and human chromosome 10q25, a region frequently
            deleted in human cancers
  JOURNAL   Genomics 46 (2), 291-293 (1997)
   PUBMED   9417918
REFERENCE   10 (residues 1 to 654)
  AUTHORS   Roof,D.J., Hayes,A., Adamian,M., Chishti,A.H. and Li,T.
  TITLE     Molecular characterization of abLIM, a novel actin-binding and
            double zinc finger protein
  JOURNAL   J Cell Biol 138 (3), 575-588 (1997)
   PUBMED   9245787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC102655.7, AW060969.1, AF404775.1, AC161518.3 and BE994737.1.
            
            On Mar 20, 2014 this sequence version replaced XP_006527108.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and lacks four alternate in-frame
            exons in the 3' coding region, compared to variant 1. It initiates
            translation at an alternate start codon. The encoded isoform (5)
            has a distinct N-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK122196.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 52.09 cM"
     Protein         1..654
                     /product="actin-binding LIM protein 1 isoform 5"
                     /note="actin-binding double zinc finger protein;
                     actin-binding LIM protein family member 1"
                     /calculated_mol_wt=73921
     Region          23..74
                     /region_name="LIM1_abLIM"
                     /note="The first LIM domain of actin binding LIM (abLIM)
                     proteins; cd09327"
                     /db_xref="CDD:188713"
     Site            order(23,26,43,46,49,52,70,73)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188713"
     Region          79..134
                     /region_name="LIM2_abLIM"
                     /note="The second LIM domain on actin binding LIM (abLIM)
                     proteins; cd09328"
                     /db_xref="CDD:188714"
     Site            order(82,85,102,105,108,111,130,133)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188714"
     Region          150..201
                     /region_name="LIM3_abLIM"
                     /note="The third LIM domain of actin binding LIM (abLIM)
                     proteins; cd09329"
                     /db_xref="CDD:188715"
     Site            order(150,153,171,174,177,180,197,200)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188715"
     Region          209..264
                     /region_name="LIM4_abLIM"
                     /note="The fourth LIM domain of actin binding LIM (abLIM)
                     proteins; cd09330"
                     /db_xref="CDD:188716"
     Site            order(209,212,229,232,235,238,257,260)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188716"
     Region          273..604
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          619..654
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..654
                     /gene="Ablim1"
                     /gene_synonym="2210411C18Rik; 2610209L21Rik;
                     4833406P10Rik; 9330196J19Rik; Limab1; mKIAA0059"
                     /coded_by="NM_001290815.2:318..2282"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS70964.1"
                     /db_xref="GeneID:226251"
                     /db_xref="MGI:MGI:1194500"
ORIGIN      
        1 mvkekvahpq dphhssekpv ihchkcgepc kgevlrvqtk hfhikcftck vcgcdlaqgg
       61 ffikngdylc tldyqrmygt rchgcgefve gevvtalgkt yhpncfacti ckrpfppgdr
      121 vtfngrdclc qlcaqpmsss pkeascssnc agcgrdikng qallaldkqw hlgcfkcksc
      181 gkvltgeyis kdgspycekd yqglfgvkce achqfitgkv leagdkhyhp scarcsrcnq
      241 mftegeemyl qgstvwhpdc kqstkteekl rptrtssesi ysrpgssipg spghtiyakv
      301 dneildykdl aaipkvkaiy dierpdlity epfytsgyed kqerqslges prtlsptpsa
      361 egyqdvrdrm ihrstsqgsi nspvysrhsy tpttsrspqh fhrpgnepss grnsplpyrp
      421 dsrpltptya qapkhfhvpd qginiyrkpp iykqhgtdpr rrssgreede eellrrrqlq
      481 eeqlmklnsg lgqlilkeem ekesrerasl asrydsplhs ashapsskts slpgygkngl
      541 hrpvstdfaq ynsygdisgg vrdyqtlpdg hmpavrmdrg vsmpnmlepk ifpyemlmvt
      601 nrgrnkilrd vdrtrlerhl apevfweifg msiqefdklp lwrrndmkkk aklf
//
LOCUS       NP_690848               1626 aa            linear   PRI 27-APR-2025
DEFINITION  collagen alpha-1(XXII) chain precursor [Homo sapiens].
ACCESSION   NP_690848 XP_291257
VERSION     NP_690848.1
DBSOURCE    REFSEQ: accession NM_152888.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1626)
  AUTHORS   Sun,Z., Cieszczyk,P., Lulinska,E., Dzitkowska-Zabielska,M.,
            Johne,M., Huminska-Lisowska,K., Michalowska-Sawczyn,M., Ficek,K.,
            Leonska-Duniec,A., Mastalerz,A., Janczyk,A. and Marek,S.
  TITLE     Are COL22A1 Gene Polymorphisms rs11784270 and rs6577958 Associated
            with Susceptibility to a Non-Contact Anterior Cruciate Ligament
            Injury in Polish Athletes?
  JOURNAL   Int J Environ Res Public Health 20 (1), 515 (2022)
   PUBMED   36612834
  REMARK    GeneRIF: Are COL22A1 Gene Polymorphisms rs11784270 and rs6577958
            Associated with Susceptibility to a Non-Contact Anterior Cruciate
            Ligament Injury in Polish Athletes?
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1626)
  AUTHORS   Miyamoto-Mikami,E., Kumagai,H., Kikuchi,N., Kamiya,N., Miyamoto,N.
            and Fuku,N.
  TITLE     eQTL variants in COL22A1 are associated with muscle injury in
            athletes
  JOURNAL   Physiol Genomics 52 (12), 588-589 (2020)
   PUBMED   33166209
  REMARK    GeneRIF: eQTL variants in COL22A1 are associated with muscle injury
            in athletes.
REFERENCE   3  (residues 1 to 1626)
  AUTHORS   Watanabe,T., Baker Frost,D.A., Mlakar,L., Heywood,J., da
            Silveira,W.A., Hardiman,G. and Feghali-Bostwick,C.
  TITLE     A Human Skin Model Recapitulates Systemic Sclerosis Dermal Fibrosis
            and Identifies COL22A1 as a TGFbeta Early Response Gene that
            Mediates Fibroblast to Myofibroblast Transition
  JOURNAL   Genes (Basel) 10 (2), 75 (2019)
   PUBMED   30678304
  REMARK    GeneRIF: COL22A1 mediates fibroblast to myofibroblast transition in
            systemic sclerosis.  Silencing of COL22A1 significantly reduced
            TGFbeta-induced ACTA2 expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1626)
  AUTHORS   Ton,Q.V., Leino,D., Mowery,S.A., Bredemeier,N.O., Lafontant,P.J.,
            Lubert,A., Gurung,S., Farlow,J.L., Foroud,T.M., Broderick,J. and
            Sumanas,S.
  TITLE     Collagen COL22A1 maintains vascular stability and mutations in
            COL22A1 are potentially associated with intracranial aneurysms
  JOURNAL   Dis Model Mech 11 (12) (2018)
   PUBMED   30541770
  REMARK    GeneRIF: COL22A1 is required to maintain vascular integrity.  These
            data further suggest that mutations in COL22A1 could be one of the
            risk factors for intracranial aneurysms in humans.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1626)
  AUTHORS   Zwolanek,D., Veit,G., Eble,J.A., Gullberg,D., Ruggiero,F.,
            Heino,J., Meier,M., Stetefeld,J. and Koch,M.
  TITLE     Collagen XXII binds to collagen-binding integrins via the novel
            motifs GLQGER and GFKGER
  JOURNAL   Biochem J 459 (1), 217-227 (2014)
   PUBMED   24428702
  REMARK    GeneRIF: Collage XXII interacts with collagen-binding integrins via
            the protein motifs GLQGER and GFKGER.
REFERENCE   6  (residues 1 to 1626)
  AUTHORS   Charvet,B., Guiraud,A., Malbouyres,M., Zwolanek,D., Guillon,E.,
            Bretaud,S., Monnot,C., Schulze,J., Bader,H.L., Allard,B., Koch,M.
            and Ruggiero,F.
  TITLE     Knockdown of col22a1 gene in zebrafish induces a muscular dystrophy
            by disruption of the myotendinous junction
  JOURNAL   Development 140 (22), 4602-4613 (2013)
   PUBMED   24131632
REFERENCE   7  (residues 1 to 1626)
  AUTHORS   Pattaro,C., De Grandi,A., Vitart,V., Hayward,C., Franke,A.,
            Aulchenko,Y.S., Johansson,A., Wild,S.H., Melville,S.A., Isaacs,A.,
            Polasek,O., Ellinghaus,D., Kolcic,I., Nothlings,U., Zgaga,L.,
            Zemunik,T., Gnewuch,C., Schreiber,S., Campbell,S., Hastie,N.,
            Boban,M., Meitinger,T., Oostra,B.A., Riegler,P., Minelli,C.,
            Wright,A.F., Campbell,H., van Duijn,C.M., Gyllensten,U.,
            Wilson,J.F., Krawczak,M., Rudan,I. and Pramstaller,P.P.
  CONSRTM   EUROSPAN consortium
  TITLE     A meta-analysis of genome-wide data from five European isolates
            reveals an association of COL22A1, SYT1, and GABRR2 with serum
            creatinine level
  JOURNAL   BMC Med Genet 11, 41 (2010)
   PUBMED   20222955
  REMARK    GeneRIF: association between serum creatinine level and
            polymorphisms in the collagen type XXII alpha 1 (COL22A1) gene, on
            chromosome 8, and in the synaptotagmin-1 (SYT1) gene, on chromosome
            12
            GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1626)
  AUTHORS   Carter,E.M. and Raggio,C.L.
  TITLE     Genetic and orthopedic aspects of collagen disorders
  JOURNAL   Curr Opin Pediatr 21 (1), 46-54 (2009)
   PUBMED   19253462
  REMARK    Review article
REFERENCE   9  (residues 1 to 1626)
  AUTHORS   Ricard-Blum,S. and Ruggiero,F.
  TITLE     The collagen superfamily: from the extracellular matrix to the cell
            membrane
  JOURNAL   Pathol Biol (Paris) 53 (7), 430-442 (2005)
   PUBMED   16085121
  REMARK    Review article
REFERENCE   10 (residues 1 to 1626)
  AUTHORS   Koch,M., Schulze,J., Hansen,U., Ashwodt,T., Keene,D.R.,
            Brunken,W.J., Burgeson,R.E., Bruckner,P. and Bruckner-Tuderman,L.
  TITLE     A novel marker of tissue junctions, collagen XXII
  JOURNAL   J Biol Chem 279 (21), 22514-22521 (2004)
   PUBMED   15016833
  REMARK    GeneRIF: collagen XXII is the first specific extracellular matrix
            protein present only at tissue junctions
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068476.13, BX094632.1,
            AF406780.1 and BC144535.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 26, 2004 this sequence version replaced XP_291257.2.
            
            Summary: This gene encodes member of the collagen family which is
            thought to contribute to the stabilization of myotendinous
            junctions and strengthen skeletal muscle attachments during
            contractile activity. It belongs to the fibril-associated collagens
            with interrupted triple helix (FACIT) subset of the collagen
            superfamily, which associate with collagen fibers through their
            C-terminal collagenous domains and mediate protein-protein
            interactions through their N-terminal noncollagenous domains. The
            encoded protein is deposited in the basement membrane zone of the
            myotendinous junction which is present only at the tissue junctions
            of muscles, tendons, the heart, articular cartilage, and skin. A
            knockdown of the orthologous zebrafish gene induces a muscular
            dystrophy by disruption of the myotendinous junction. [provided by
            RefSeq, May 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF406780.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303045.11/ ENSP00000303153.6
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1626
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.23-q24.3"
     Protein         1..1626
                     /product="collagen alpha-1(XXII) chain precursor"
                     /note="collagen alpha-1(XXII) chain"
                     /calculated_mol_wt=158461
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2703
     Region          36..219
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Site            order(44,115,151)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
     Region          239..426
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cl22861"
                     /db_xref="CDD:473984"
     Site            375
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFW1.2)"
     Region          <481..>703
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          506..1002
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW1.2)"
     Region          <798..>1097
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1019..1103
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW1.2)"
     Region          1119..1458
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW1.2)"
     Region          <1170..>1386
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1288..>1584
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1491..1609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW1.2)"
     CDS             1..1626
                     /gene="COL22A1"
                     /coded_by="NM_152888.3:496..5376"
                     /db_xref="CCDS:CCDS6376.1"
                     /db_xref="GeneID:169044"
                     /db_xref="HGNC:HGNC:22989"
                     /db_xref="MIM:610026"
ORIGIN      
        1 maglrgnava gllwmlllws ggggcqaqra gcksvhydlv flldtsssvg kedfekvrqw
       61 vanlvdtfev gpdrtrvgvv rysdrpttaf elglfgsqee vkaaarrlay hggntntgda
      121 lryitarsfs phaggrprdr aykqvaillt dgrsqdlvld aaaaahragi rifavgvgea
      181 lkeeleeias epksahvfhv sdfnaidkir gklrrrlcen vlcpsvrveg drfkhtnggt
      241 keitgfdlmd lfsvkeilgk rengaqssyv rmgsfpvvqs tedvfpqglp deyafvttfr
      301 frktsrkedw yiwqvidqys ipqvsirldg enkaveynav gamkdavrvv frgsrvndlf
      361 drdwhkmals iqaqnvslhi dcalvqtlpi eerenidiqg ktvigkrlyd svpidfdlqr
      421 iviycdsrha eletccdips gpcqvtvvte pppppppqrp ptpgseqigf lktincscpa
      481 gekgemgvag pmglpgpkgd igaigpvgap gpkgekgdvg igpfgqgekg ekgslglpgp
      541 pgrdgskgmr gepgelgepg lpgevgmrgp qgppglpgpp grvgapglqg ergekgtrge
      601 kgergldgfp gkpgdtgqqg rpgpsgvagp qgekgdvgpa gppgvpgsvv qqeglkgeqg
      661 apgprghqga pgppgargpi gpegrdgppg lqglrgkkgd mgppgipgll glqgppgppg
      721 vpgppgpggs pglpgeigfp gkpgppgptg ppgkdgpngp pgppgtkgep gergedglpg
      781 kpglrgeige qglagrpgek geaglpgapg fpgvrgekgd qgekgelglp glkgdrgekg
      841 eagpagppgl pgttslftph prmpgeqgpk gekgdpglpg epglqgrpge lgpqgptgpp
      901 gakgqegahg apgaagnpga pghvgapgps gppgsvgapg lrgtpgkdge rgekgaagee
      961 gspgpvgprg dpgapglpgp pgkgkdgepg lrgspglpgp lgtkaacgkv rgsencalgg
     1021 qcvkgdrgap gipgspgsrg dpgigvagpp gpsgppgdkg spgsrglpgf pgpqgpagrd
     1081 gapgnpgerg ppgkpglssl lspgdinlla kdvcndcppg ppglpglpgf kgdkgvpgkp
     1141 gregtegkkg eagppglpgp pgiagpqgsq gergadgevg qkgdqghpgv pgfmgppgnp
     1201 gppgadgiag aagppgiqgs pgkegppgpq gpsglpgipg eegkegrdgk pgppgepgka
     1261 gepglpgpeg argppgfkgh tgdsgapgpr gesgamglpg qeglpgkdgd tgptgpqgpq
     1321 gprgppgkng spgspgepgp sgtpgqkgsk gengspglpg flgprgppge pgekgvpgke
     1381 gvpgkpgepg fkgergdpgi kgdkgppggk gqpgdpgipg hkghtglmgp qglpgengpv
     1441 gppgppgqpg fpglrgesps metlrrliqe elgkqletrl ayllaqmppa ymkssqgrpg
     1501 ppgppgkdgl pgragpmgep grpgqggleg psgpigpkge rgakgdpgap gvglrgemgp
     1561 pgipgqpgep gyakdglpgi pgpqgetgpa ghpglpgppg ppgqcdpsqc ayfaslaarp
     1621 gnvkgp
//
LOCUS       NP_699196                567 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane anterior posterior transformation protein 1 homolog
            [Homo sapiens].
ACCESSION   NP_699196
VERSION     NP_699196.2
DBSOURCE    REFSEQ: accession NM_153365.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Etich,J., Semler,O., Stevenson,N.L., Stephan,A., Besio,R.,
            Garibaldi,N., Reintjes,N., Dafinger,C., Liebau,M.C., Baumann,U.,
            Morgelin,M., Forlino,A., Stephens,D.J., Netzer,C., Zaucke,F. and
            Rehberg,M.
  TITLE     TAPT1-at the crossroads of extracellular matrix and signaling in
            Osteogenesis imperfecta
  JOURNAL   EMBO Mol Med 15 (7), e17528 (2023)
   PUBMED   37292039
  REMARK    GeneRIF: TAPT1-at the crossroads of extracellular matrix and
            signaling in Osteogenesis imperfecta.
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Nabavizadeh,N., Bressin,A., Shboul,M., Moreno Traspas,R.,
            Chia,P.H., Bonnard,C., Szenker-Ravi,E., Saribas,B., Beillard,E.,
            Altunoglu,U., Hojati,Z., Drutman,S., Freier,S., El-Khateeb,M.,
            Fathallah,R., Casanova,J.L., Soror,W., Arafat,A.,
            Escande-Beillard,N., Mayer,A. and Reversade,B.
  TITLE     A progeroid syndrome caused by a deep intronic variant in TAPT1 is
            revealed by RNA/SI-NET sequencing
  JOURNAL   EMBO Mol Med 15 (2), e16478 (2023)
   PUBMED   36652330
  REMARK    GeneRIF: A progeroid syndrome caused by a deep intronic variant in
            TAPT1 is revealed by RNA/SI-NET sequencing.
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Wang,B., Zhao,Q., Gong,X., Wang,C., Bai,Y., Wang,H., Zhou,J. and
            Rong,X.
  TITLE     Transmembrane anterior posterior transformation 1 regulates BMP
            signaling and modulates the protein stability of SMAD1/5
  JOURNAL   J Biol Chem 298 (12), 102684 (2022)
   PUBMED   36370851
  REMARK    GeneRIF: Transmembrane anterior posterior transformation 1
            regulates BMP signaling and modulates the protein stability of
            SMAD1/5.
            Erratum:[J Biol Chem. 2023 Jul;299(7):104957. doi:
            10.1016/j.jbc.2023.104957. PMID: 37393648]
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Symoens,S., Barnes,A.M., Gistelinck,C., Malfait,F., Guillemyn,B.,
            Steyaert,W., Syx,D., D'hondt,S., Biervliet,M., De Backer,J.,
            Witten,E.P., Leikin,S., Makareeva,E., Gillessen-Kaesbach,G.,
            Huysseune,A., Vleminckx,K., Willaert,A., De Paepe,A., Marini,J.C.
            and Coucke,P.J.
  TITLE     Genetic Defects in TAPT1 Disrupt Ciliogenesis and Cause a Complex
            Lethal Osteochondrodysplasia
  JOURNAL   Am J Hum Genet 97 (4), 521-534 (2015)
   PUBMED   26365339
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Argos,M., Tong,L., Pierce,B.L., Rakibuz-Zaman,M., Ahmed,A.,
            Islam,T., Rahman,M., Paul-Brutus,R., Rahaman,R., Roy,S.,
            Jasmine,F., Kibriya,M.G. and Ahsan,H.
  TITLE     Genome-wide association study of smoking behaviours among
            Bangladeshi adults
  JOURNAL   J Med Genet 51 (5), 327-333 (2014)
   PUBMED   24665060
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Howell,G.R., Shindo,M., Murray,S., Gridley,T., Wilson,L.A. and
            Schimenti,J.C.
  TITLE     Mutation of a ubiquitously expressed mouse transmembrane protein
            (Tapt1) causes specific skeletal homeotic transformations
  JOURNAL   Genetics 175 (2), 699-707 (2007)
   PUBMED   17151244
  REMARK    GeneRIF: A perinatal lethal mutation in mouse Tapt1 results in
            homeotic, posterior-to-anterior transformations of the axial
            skeleton.
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Baldwin,B.R., Zhang,C.O. and Keay,S.
  TITLE     Cloning and epitope mapping of a functional partial fusion receptor
            for human cytomegalovirus gH
  JOURNAL   J Gen Virol 81 (Pt 1), 27-35 (2000)
   PUBMED   10640539
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Baldwin,B.R., Kleinberg,M. and Keay,S.
  TITLE     Molecular cloning and expression of receptor peptides that block
            human cytomegalovirus/cell fusion
  JOURNAL   Biochem Biophys Res Commun 219 (2), 668-673 (1996)
   PUBMED   8605045
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC066899.1, AC108063.3 and
            AA811306.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 14, 2007 this sequence version replaced NP_699196.1.
            
            Summary: This gene encodes a highly conserved protein that
            localizes to the centrosome and/or ciliary basal body. Mutations in
            this gene disrupt Golgi morphology and trafficking and normal
            primary cilium formation and these mutations are congenitally
            manifested by severe undermineralization of the intra-uterine
            skeleton. A mutation in the mouse ortholog of this gene results in
            homeotic, posterior-to-anterior transformations of the axial
            skeleton which are similar to the phenotype of mouse homeobox C8
            gene mutants. In mouse, this gene is thought to function downstream
            of homeobox C8 to transduce extracellular patterning information
            during axial skeleton development. [provided by RefSeq, Jan 2017].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK074494.1, SRR1803611.153281.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000405303.7/ ENSP00000385347.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.32"
     Protein         1..567
                     /product="transmembrane anterior posterior transformation
                     protein 1 homolog"
                     /note="cytomegalovirus partial fusion receptor"
                     /calculated_mol_wt=64129
     Region          1..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT6.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT6.1)"
     Site            111..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT6.1)"
     Region          155..459
                     /region_name="DUF747"
                     /note="Eukaryotic membrane protein family; pfam05346"
                     /db_xref="CDD:398815"
     Site            157..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT6.1)"
     Site            236..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT6.1)"
     Site            403..423
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT6.1)"
     Site            432..452
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT6.1)"
     Region          466..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT6.1)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT6.1)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q4VBD2; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT6.1)"
     CDS             1..567
                     /gene="TAPT1"
                     /gene_synonym="CMVFR; OCLSBG"
                     /coded_by="NM_153365.3:15..1718"
                     /db_xref="CCDS:CCDS47030.1"
                     /db_xref="GeneID:202018"
                     /db_xref="HGNC:HGNC:26887"
                     /db_xref="MIM:612758"
ORIGIN      
        1 magvgdaaap gegggggvdg pqrdgrgeae qpggsggqgp ppapqltetl gfyesdrrre
       61 rrrgrtelsl lrflsaeltr gyflehneak yterrervyt clriprelek lmvfgiflcl
      121 daflyvftll plrvflalfr lltlpcyglr drrllqpaqv cdilkgvilv icyfmmhyvd
      181 ysmmyhlirg qsviklyiiy nmlevadrlf ssfgqdilda lywtatepke rkrahigvip
      241 hffmavlyvf lhailimvqa ttlnvafnsh nkslltimms nnfveikgsv fkkfeknnlf
      301 qmsnsdiker ftnyvllliv clrnmeqfsw npdhlwvlfp dvcmviasei avdivkhafi
      361 tkfnditadv yseyraslaf dlvssrqkna ytdysdsvar rmgfiplpla vllirvvtss
      421 ikvqgilsya cvilfyfgli slkvlnsivl lgkscqyvke akmeeklsnp patctpgkps
      481 sksqnkckps qglsteenls asitkqpihq keniipllvt snsdqflttp dgdekditqd
      541 nselkhrssk kdlleidrft icgnrid
//
LOCUS       NP_056169               1749 aa            linear   PRI 27-APR-2025
DEFINITION  nucleoporin NUP188 [Homo sapiens].
ACCESSION   NP_056169 XP_497078
VERSION     NP_056169.1
DBSOURCE    REFSEQ: accession NM_015354.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1749)
  AUTHORS   Muir,A.M., Cohen,J.L., Sheppard,S.E., Guttipatti,P., Lo,T.Y.,
            Weed,N., Doherty,D., DeMarzo,D., Fagerberg,C.R., Kjaersgaard,L.,
            Larsen,M.J., Rump,P., Lohner,K., Hirsch,Y., Zeevi,D.A.,
            Zackai,E.H., Bhoj,E., Song,Y. and Mefford,H.C.
  TITLE     Bi-allelic Loss-of-Function Variants in NUP188 Cause a Recognizable
            Syndrome Characterized by Neurologic, Ocular, and Cardiac
            Abnormalities
  JOURNAL   Am J Hum Genet 106 (5), 623-631 (2020)
   PUBMED   32275884
  REMARK    GeneRIF: results implicate bi-allelic loss-of-function NUP188
            variants in a recessive syndrome characterized by a distinct
            neurologic, ophthalmologic, and facial phenotype
REFERENCE   2  (residues 1 to 1749)
  AUTHORS   Vishnoi,N., Dhanasekeran,K., Chalfant,M., Surovstev,I., Khokha,M.K.
            and Lusk,C.P.
  TITLE     Differential turnover of Nup188 controls its levels at centrosomes
            and role in centriole duplication
  JOURNAL   J Cell Biol 219 (3) (2020)
   PUBMED   32211895
  REMARK    GeneRIF: Differential turnover of Nup188 controls its levels at
            centrosomes and role in centriole duplication.
REFERENCE   3  (residues 1 to 1749)
  AUTHORS   Roczniak-Ferguson,A. and Ferguson,S.M.
  TITLE     Pleiotropic requirements for human TDP-43 in the regulation of cell
            and organelle homeostasis
  JOURNAL   Life Sci Alliance 2 (5), e201900358 (2019)
   PUBMED   31527135
  REMARK    GeneRIF: Results identified Nup188 as a novel TDP-43 target which
            controls the mRNA splicing of Nup188.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1749)
  AUTHORS   Del Viso,F., Huang,F., Myers,J., Chalfant,M., Zhang,Y., Reza,N.,
            Bewersdorf,J., Lusk,C.P. and Khokha,M.K.
  TITLE     Congenital Heart Disease Genetics Uncovers Context-Dependent
            Organization and Function of Nucleoporins at Cilia
  JOURNAL   Dev Cell 38 (5), 478-492 (2016)
   PUBMED   27593162
  REMARK    GeneRIF: we show that knockdown of Nup188 or its binding partner
            Nup93 leads to a loss of cilia during embryonic development while
            leaving NPC function largely intact. Many data, including the
            localization of endogenous Nup188/93 at cilia bases, support their
            direct role at cilia. Super-resolution imaging of Nup188 shows two
            barrel-like structures
REFERENCE   5  (residues 1 to 1749)
  AUTHORS   Schwartz,T.U.
  TITLE     The Structure Inventory of the Nuclear Pore Complex
  JOURNAL   J Mol Biol 428 (10 Pt A), 1986-2000 (2016)
   PUBMED   27016207
  REMARK    Review article
REFERENCE   6  (residues 1 to 1749)
  AUTHORS   Braun,D.A., Sadowski,C.E., Kohl,S., Lovric,S., Astrinidis,S.A.,
            Pabst,W.L., Gee,H.Y., Ashraf,S., Lawson,J.A., Shril,S., Airik,M.,
            Tan,W., Schapiro,D., Rao,J., Choi,W.I., Hermle,T., Kemper,M.J.,
            Pohl,M., Ozaltin,F., Konrad,M., Bogdanovic,R., Buscher,R.,
            Helmchen,U., Serdaroglu,E., Lifton,R.P., Antonin,W. and
            Hildebrandt,F.
  TITLE     Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause
            steroid-resistant nephrotic syndrome
  JOURNAL   Nat Genet 48 (4), 457-465 (2016)
   PUBMED   26878725
REFERENCE   7  (residues 1 to 1749)
  AUTHORS   Bui,K.H., von Appen,A., DiGuilio,A.L., Ori,A., Sparks,L.,
            Mackmull,M.T., Bock,T., Hagen,W., Andres-Pons,A., Glavy,J.S. and
            Beck,M.
  TITLE     Integrated structural analysis of the human nuclear pore complex
            scaffold
  JOURNAL   Cell 155 (6), 1233-1243 (2013)
   PUBMED   24315095
REFERENCE   8  (residues 1 to 1749)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   9  (residues 1 to 1749)
  AUTHORS   Denoeud,F., Kapranov,P., Ucla,C., Frankish,A., Castelo,R.,
            Drenkow,J., Lagarde,J., Alioto,T., Manzano,C., Chrast,J., Dike,S.,
            Wyss,C., Henrichsen,C.N., Holroyd,N., Dickson,M.C., Taylor,R.,
            Hance,Z., Foissac,S., Myers,R.M., Rogers,J., Hubbard,T., Harrow,J.,
            Guigo,R., Gingeras,T.R., Antonarakis,S.E. and Reymond,A.
  TITLE     Prominent use of distal 5' transcription start sites and discovery
            of a large number of additional exons in ENCODE regions
  JOURNAL   Genome Res 17 (6), 746-759 (2007)
   PUBMED   17567994
REFERENCE   10 (residues 1 to 1749)
  AUTHORS   Miller,B.R., Powers,M., Park,M., Fischer,W. and Forbes,D.J.
  TITLE     Identification of a new vertebrate nucleoporin, Nup188, with the
            use of a novel organelle trap assay
  JOURNAL   Mol Biol Cell 11 (10), 3381-3396 (2000)
   PUBMED   11029043
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY094051.1, D79991.1 and
            AA731883.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 30, 2005 this sequence version replaced XP_497078.1.
            
            Summary: The nuclear pore complex (NPC) is found on the nuclear
            envelope and forms a gateway that regulates the flow of proteins
            and RNAs between the cytoplasm and nucleoplasm. The NPC is
            comprised of approximately 30 distinct proteins collectively known
            as nucleoporins. Nucleoporins are pore-complex-specific
            glycoproteins which often have cytoplasmically oriented O-linked
            N-acetylglucosamine residues and numerous repeats of the
            pentapeptide sequence XFXFG. However, the nucleoporin protein
            encoded by this gene does not contain the typical FG repeat
            sequences found in most vertebrate nucleoporins. This nucleoporin
            is thought to form part of the scaffold for the central channel of
            the nuclear pore. [provided by RefSeq, Jan 2013].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.225471.1,
                                           SRR1660809.113796.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372577.2/ ENSP00000361658.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1749
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..1749
                     /product="nucleoporin NUP188"
                     /note="nucleoporin NUP188 homolog; nucleoporin 188kDa"
                     /calculated_mol_wt=195913
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q5SRE5.1)"
     Region          31..941
                     /region_name="Nup188"
                     /note="Nucleoporin subcomplex protein binding to Pom34;
                     pfam10487"
                     /db_xref="CDD:463110"
     Region          1514..1542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SRE5.1)"
     Site            1523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5SRE5.1)"
     Region          1707..1733
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SRE5.1)"
     Site            1709
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5SRE5.1)"
     Site            1712
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5SRE5.1)"
     Site            1717
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5SRE5.1)"
     CDS             1..1749
                     /gene="NUP188"
                     /gene_synonym="hNup188; KIAA0169; SANDSTEF"
                     /coded_by="NM_015354.3:22..5271"
                     /db_xref="CCDS:CCDS35156.1"
                     /db_xref="GeneID:23511"
                     /db_xref="HGNC:HGNC:17859"
                     /db_xref="MIM:615587"
ORIGIN      
        1 maaaaggpcv rssrelwtil lgrsalrels qieaelnkhw rrlleglsyy kppspssaek
       61 vkankdvasp lkelglrisk flgldeeqsv qllqcylqed yrgtrdsvkt vlqderqsqa
      121 lilkiadyyy eertcilrcv lhlltyfqde rhpyrveyad cvdklekelv skyrqqfeel
      181 ykteaptwet hgnlmterqv srwfvqclre qsmlleiifl yyayfemaps dllvltkmfk
      241 eqgfgsrqtn rhlvdetmdp fvdrigyfsa lilvegmdie slhkcalddr relhqfaqdg
      301 licqdmdclm ltfgdiphha pvllawallr htlnpeetss vvrkiggtai qlnvfqyltr
      361 llqslasggn dcttstacmc vygllsfvlt slelhtlgnq qdiidtacev ladpslpelf
      421 wgteptsglg iildsvcgmf phllspllql lralvsgkst akkvysfldk msfynelykh
      481 kphdvished gtlwrrqtpk llyplggqtn lripqgtvgq vmlddraylv rweysysswt
      541 lftceiemll hvvstadviq hcqrvkpiid lvhkvistdl siadcllpit sriymllqrl
      601 ttvisppvdv iascvncltv laarnpakvw tdlrhtgflp fvahpvssls qmisaegmna
      661 ggygnllmns eqpqgeygvt iaflrlittl vkgqlgstqs qglvpcvmfv lkemlpsyhk
      721 wrynshgvre qigclileli hailnlchet dlhsshtpsl qflcicslay teagqtvini
      781 mgigvdtidm vmaaqprsdg aegqgqgqll iktvklafsv tnnvirlkpp snvvspleqa
      841 lsqhgahgnn liavlakyiy hkhdpalprl aiqllkrlat vapmsvyacl gndaaairda
      901 fltrlqskie dmrikvmile fltvavetqp glielflnle vkdgsdgske fslgmwsclh
      961 avlelidsqq qdrywcppll hraaiaflha lwqdrrdsam lvlrtkpkfw enltsplfgt
     1021 lsppsetsep siletcalim kiicleiyyv vkgsldqslk dtlkkfsiek rfaywsgyvk
     1081 slavhvaete gssctslley qmlvsawrml liiatthadi mhltdsvvrr qlfldvldgt
     1141 kalllvpasv nclrlgsmkc tlllillrqw krelgsvdei lgplteileg vlqadqqlme
     1201 ktkakvfsaf itvlqmkemk vsdipqysql vlnvcetlqe evialfdqtr hslalgsate
     1261 dkdsmetddc srsrhrdqrd gvcvlglhla kelcevdedg dswlqvtrrl pilptllttl
     1321 evslrmkqnl hfteatlhll ltlartqqga tavagagitq siclpllsvy qlstngtaqt
     1381 psasrkslda pswpgvyrls mslmeqllkt lrynflpeal dfvgvhqert lqclnavrtv
     1441 qslacleead htvgfilqls nfmkewhfhl pqlmrdiqvn lgylcqacts llhsrkmlqh
     1501 ylqnkngdgl psavaqrvqr ppsaasaaps sskqpaadte aseqqalhtv qygllkilsk
     1561 tlaalrhftp dvcqilldqs ldlaeynflf alsfttptfd sevapsfgtl latvnvalnm
     1621 lgeldkkkep ltqavglstq aegtrtlksl lmftmencfy llisqamryl rdpavhprdk
     1681 qrmkqelsse lstllsslsr yfrrgapssp atgvlpspqg kstslskasp esqepliqlv
     1741 qafvrhmqr
//
LOCUS       NP_005787                127 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear transport factor 2 [Homo sapiens].
ACCESSION   NP_005787
VERSION     NP_005787.1
DBSOURCE    REFSEQ: accession NM_005796.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Vukovic,L.D., Chen,P., Mishra,S., White,K.H., Gigley,J.P. and
            Levy,D.L.
  TITLE     Nuclear Transport Factor 2 (NTF2) suppresses WM983B metastatic
            melanoma by modifying cell migration, metastasis, and gene
            expression
  JOURNAL   Sci Rep 11 (1), 23586 (2021)
   PUBMED   34880267
  REMARK    GeneRIF: Nuclear Transport Factor 2 (NTF2) suppresses WM983B
            metastatic melanoma by modifying cell migration, metastasis, and
            gene expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Shen,Q., Tian,T., Xiong,Q., Ellis Fisher,P.D., Xiong,Y.,
            Melia,T.J., Lusk,C.P. and Lin,C.
  TITLE     DNA-Origami NanoTrap for Studying the Selective Barriers Formed by
            Phenylalanine-Glycine-Rich Nucleoporins
  JOURNAL   J Am Chem Soc 143 (31), 12294-12303 (2021)
   PUBMED   34324340
  REMARK    GeneRIF: DNA-Origami NanoTrap for Studying the Selective Barriers
            Formed by Phenylalanine-Glycine-Rich Nucleoporins.
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Stewart,M., Kent,H.M. and McCoy,A.J.
  TITLE     Structural basis for molecular recognition between nuclear
            transport factor 2 (NTF2) and the GDP-bound form of the Ras-family
            GTPase Ran
  JOURNAL   J Mol Biol 277 (3), 635-646 (1998)
   PUBMED   9533885
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Clarkson,W.D., Corbett,A.H., Paschal,B.M., Kent,H.M., McCoy,A.J.,
            Gerace,L., Silver,P.A. and Stewart,M.
  TITLE     Nuclear protein import is decreased by engineered mutants of
            nuclear transport factor 2 (NTF2) that do not bind GDP-Ran
  JOURNAL   J Mol Biol 272 (5), 716-730 (1997)
   PUBMED   9368653
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Hu,T., Guan,T. and Gerace,L.
  TITLE     Molecular and functional characterization of the p62 complex, an
            assembly of nuclear pore complex glycoproteins
  JOURNAL   J Cell Biol 134 (3), 589-601 (1996)
   PUBMED   8707840
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Bullock,T.L., Clarkson,W.D., Kent,H.M. and Stewart,M.
  TITLE     The 1.6 angstroms resolution crystal structure of nuclear transport
            factor 2 (NTF2)
  JOURNAL   J Mol Biol 260 (3), 422-431 (1996)
   PUBMED   8757804
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Paschal,B.M. and Gerace,L.
  TITLE     Identification of NTF2, a cytosolic factor for nuclear import that
            interacts with nuclear pore complex protein p62
  JOURNAL   J Cell Biol 129 (4), 925-937 (1995)
   PUBMED   7744965
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Grundmann,U., Nerlich,C., Rein,T., Lottspeich,F. and Kupper,H.A.
  TITLE     Isolation of cDNA coding for the placental protein 15 (PP15)
  JOURNAL   Nucleic Acids Res 16 (10), 4721 (1988)
   PUBMED   3380696
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X07315.1 and BX647782.1.
            
            Summary: This gene encodes a cytosolic factor that facilitates
            protein transport into the nucleus. The encoded protein is required
            for nuclear import of the small Ras-like GTPase, Ran which is
            involved in numerous cellular processes. This protein also
            interacts with the nuclear pore complex glycoprotein p62. [provided
            by RefSeq, Apr 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1105906.1,
                                           SRR3476690.653232.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219169.9/ ENSP00000219169.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..127
                     /product="nuclear transport factor 2"
                     /note="placental protein 15"
                     /calculated_mol_wt=14347
     Site            4
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P61970.1)"
     Region          7..122
                     /region_name="NTF2"
                     /note="Nuclear transport factor 2 (NTF2) domain plays an
                     important role in the trafficking of macromolecules, ions
                     and small molecules between the cytoplasm and nucleus.
                     This bi-directional transport of macromolecules across the
                     nuclear envelope requires many...; cd00780"
                     /db_xref="CDD:238403"
     Site            order(34,40,47,72,74..75,84,106,116..118,120,122)
                     /site_type="active"
                     /note="TAP/p15 interaction [active]"
                     /db_xref="CDD:238403"
     Site            order(38,40..41,69..70,72,74..75,82,86..88,92,94..97,100,
                     106,116..118,120..122)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238403"
     Site            order(41..42,59,64,87,89,91..92,94,97,119,121)
                     /site_type="active"
                     /note="RanGDP-NTF2 interaction [active]"
                     /db_xref="CDD:238403"
     CDS             1..127
                     /gene="NUTF2"
                     /gene_synonym="NTF-2; NTF2; PP15"
                     /coded_by="NM_005796.3:83..466"
                     /db_xref="CCDS:CCDS10848.1"
                     /db_xref="GeneID:10204"
                     /db_xref="HGNC:HGNC:13722"
                     /db_xref="MIM:605813"
ORIGIN      
        1 mgdkpiweqi gssfiqhyyq lfdndrtqlg aiyidasclt wegqqfqgka aiveklsslp
       61 fqkiqhsita qdhqptpdsc iismvvgqlk adedpimgfh qmfllknind awvctndmfr
      121 lalhnfg
//
LOCUS       NP_835235                505 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome P450 4Z1 [Homo sapiens].
ACCESSION   NP_835235 XP_947488 XP_951034
VERSION     NP_835235.1
DBSOURCE    REFSEQ: accession NM_178134.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Al-Saraireh,Y.M., Alshammari,F.O.F.O., Satari,A.O., Al-Mahdy,Y.S.,
            Almuhaisen,G.H., Abu-Azzam,O.H., Uwais,A.N., Abufraijeh,S.M.,
            Al-Kharabsheh,A.M., Al-Dalain,S.M., Al-Qtaitat,A., Al-Tarawneh,F.,
            Al Shuneigat,J.M. and Al-Sarayreh,S.A.
  TITLE     Cytochrome 4Z1 Expression Connotes Unfavorable Prognosis in Ovarian
            Cancers
  JOURNAL   Medicina (Kaunas) 58 (9), 1263 (2022)
   PUBMED   36143940
  REMARK    GeneRIF: Cytochrome 4Z1 Expression Connotes Unfavorable Prognosis
            in Ovarian Cancers.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Al-Saraireh,Y.M., Alshammari,F.O.F.O., Youssef,A.M.M.,
            Al-Sarayra,Y.M., Al-Saraireh,R.A., Al-Muhaisen,G.H., Al-Mahdy,Y.S.,
            Al-Kharabsheh,A.M., Abufraijeh,S.M. and Alrawashdeh,H.M.
  TITLE     Cytochrome 4Z1 Expression Is Correlated with Poor Prognosis in
            Patients with Cervical Cancer
  JOURNAL   Curr Oncol 28 (5), 3573-3584 (2021)
   PUBMED   34590601
  REMARK    GeneRIF: Cytochrome 4Z1 Expression Is Correlated with Poor
            Prognosis in Patients with Cervical Cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Al-Saraireh,Y.M., Alshammari,F.O.F.O., Youssef,A.M.M.,
            Al-Sarayreh,S., Almuhaisen,G.H., Alnawaiseh,N., Al Shuneigat,J.M.
            and Alrawashdeh,H.M.
  TITLE     Profiling of CYP4Z1 and CYP1B1 expression in bladder cancers
  JOURNAL   Sci Rep 11 (1), 5581 (2021)
   PUBMED   33692504
  REMARK    GeneRIF: Profiling of CYP4Z1 and CYP1B1 expression in bladder
            cancers.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Liu,J., Machalz,D., Wolber,G., Sorensen,E.J. and Bureik,M.
  TITLE     New Proluciferin Substrates for Human CYP4 Family Enzymes
  JOURNAL   Appl Biochem Biotechnol 193 (1), 218-237 (2021)
   PUBMED   32869209
  REMARK    GeneRIF: New Proluciferin Substrates for Human CYP4 Family Enzymes.
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Du,W., Machalz,D., Yan,Q., Sorensen,E.J., Wolber,G. and Bureik,M.
  TITLE     Importance of asparagine-381 and arginine-487 for substrate
            recognition in CYP4Z1
  JOURNAL   Biochem Pharmacol 174, 113850 (2020)
   PUBMED   32044355
  REMARK    GeneRIF: Importance of asparagine-381 and arginine-487 for
            substrate recognition in CYP4Z1.
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Savas,U., Hsu,M.H., Griffin,K.J., Bell,D.R. and Johnson,E.F.
  TITLE     Conditional regulation of the human CYP4X1 and CYP4Z1 genes
  JOURNAL   Arch Biochem Biophys 436 (2), 377-385 (2005)
   PUBMED   15797250
  REMARK    GeneRIF: PPARalpha has a role in CYP4X1 regulation, and the
            glucocorticoid and progesterone receptors have roles in CYP4Z1 gene
            activation
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Rieger,M.A., Ebner,R., Bell,D.R., Kiessling,A., Rohayem,J.,
            Schmitz,M., Temme,A., Rieber,E.P. and Weigle,B.
  TITLE     Identification of a novel mammary-restricted cytochrome P450,
            CYP4Z1, with overexpression in breast carcinoma
  JOURNAL   Cancer Res 64 (7), 2357-2364 (2004)
   PUBMED   15059886
  REMARK    GeneRIF: Human cytochrome P450 (CYP), termed CYP4Z1,was identified,
            and the cDNA was cloned from a breast carcinoma line .
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Simpson,A.E.
  TITLE     The cytochrome P450 4 (CYP4) family
  JOURNAL   Gen Pharmacol 28 (3), 351-359 (1997)
   PUBMED   9068972
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL450996.2 and AL135960.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_947488.1, XP_951034.1.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This gene is part of a cluster of cytochrome P450 genes on
            chromosome 1p33. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358631.1, AK292175.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144335, SAMEA2158569
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334194.4/ ENSP00000334246.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p33"
     Protein         1..505
                     /product="cytochrome P450 4Z1"
                     /EC_number="1.14.14.1"
                     /EC_number="1.14.14.130"
                     /note="CYPIVZ1; cytochrome P450, family 4, subfamily Z,
                     polypeptide 1; laurate 7-monooxygenase"
                     /calculated_mol_wt=58955
     Site            10..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86W10.1)"
     Region          66..500
                     /region_name="CYP4B-like"
                     /note="cytochrome P450 family 4, subfamily B and similar
                     cytochrome P450s, including subfamilies A, T, X, and Z;
                     cd20678"
                     /db_xref="CDD:410771"
     Site            order(109,114,125..126,133,137,144,311,314..315,318,
                     378..379,382,444..446,450..454,457..458,462)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410771"
     Site            order(126,313..314,318,379,381,383,490)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410771"
     Site            452
                     /site_type="binding"
                     /note="heme binding site"
     CDS             1..505
                     /gene="CYP4Z1"
                     /gene_synonym="CYP4A20"
                     /coded_by="NM_178134.3:261..1778"
                     /db_xref="CCDS:CCDS545.1"
                     /db_xref="GeneID:199974"
                     /db_xref="HGNC:HGNC:20583"
                     /db_xref="MIM:618953"
ORIGIN      
        1 mepswlqelm ahpflllill cmslllfqvi rlyqrrrwmi ralhlfpapp ahwfyghkef
       61 ypvkefevyh klmekypcav plwvgpftmf fsvhdpdyak illkrqdpks avshkilesw
      121 vgrglvtldg skwkkhrqiv kpgfnisilk ifitmmsesv rmmlnkweeh iaqnsrlelf
      181 qhvslmtlds imkcafshqg siqldstlds ylkavfnlsk isnqrmnnfl hhndlvfkfs
      241 sqgqifskfn qelhqftekv iqdrkeslkd klkqdttqkr rwdfldills aksentkdfs
      301 eadlqaevkt fmfaghdtts saiswilycl akypehqqrc rdeirellgd gssitwehls
      361 qmpyttmcik eclrlyapvv nisrlldkpi tfpdgrslpa gitvfiniwa lhhnpyfwed
      421 pqvfnplrfs rensekihpy afipfsaglr ncigqhfaii eckvavaltl lrfklapdhs
      481 rppqpvrqvv lkskngihvf akkvc
//
LOCUS       NP_001356775             308 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 37 isoform c [Homo
            sapiens].
ACCESSION   NP_001356775
VERSION     NP_001356775.1
DBSOURCE    REFSEQ: accession NM_001369846.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136170.14 and KF455104.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK057310.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1"
     Protein         1..308
                     /product="zinc finger and BTB domain-containing protein 37
                     isoform c"
                     /note="zinc finger and BTB domain-containing protein 37"
                     /calculated_mol_wt=33905
     Region          7..129
                     /region_name="BTB_POZ_ZBTB37"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 37 (ZBTB37); cd18222"
                     /db_xref="CDD:349531"
     Region          140..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TC79.1)"
     CDS             1..308
                     /gene="ZBTB37"
                     /gene_synonym="D430004I08Rik; ZNF908"
                     /coded_by="NM_001369846.1:400..1326"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS86033.1"
                     /db_xref="GeneID:84614"
                     /db_xref="HGNC:HGNC:28365"
ORIGIN      
        1 mekggniqle ipdfsnsvls hlnqlrmqgr lcdivvnvqg qafrahkvvl aasspyfrdh
       61 mslnemstvs isviknptvf eqllsfcytg riclqladii syltaasflq mqhiidkctq
      121 ilegihfkin vaeveaelsq trtkhqerpp eshrvtpnln rslsprhntp kgnrrgqvsa
      181 vldirelspp eestspqiie pssdvesrep ilrinragqw yvetgvadrg grsddevrvl
      241 gavhiktenl eewlgpenqp sgedgssaee vtamvidttg hgsvgqenyt lgssgakvar
      301 ptssevdr
//
LOCUS       NP_001697                706 aa            linear   PRI 27-APR-2025
DEFINITION  B-cell lymphoma 6 protein isoform 1 [Homo sapiens].
ACCESSION   NP_001697
VERSION     NP_001697.2
DBSOURCE    REFSEQ: accession NM_001706.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Liongue,C., Almohaisen,F.L.J. and Ward,A.C.
  TITLE     B Cell Lymphoma 6 (BCL6): A Conserved Regulator of Immunity and
            Beyond
  JOURNAL   Int J Mol Sci 25 (20), 10968 (2024)
   PUBMED   39456751
  REMARK    GeneRIF: B Cell Lymphoma 6 (BCL6): A Conserved Regulator of
            Immunity and Beyond.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Gopalakrishnan,V., Roy,U., Srivastava,S., Kariya,K.M., Sharma,S.,
            Javedakar,S.M., Choudhary,B. and Raghavan,S.C.
  TITLE     Delineating the mechanism of fragility at BCL6 breakpoint region
            associated with translocations in diffuse large B cell lymphoma
  JOURNAL   Cell Mol Life Sci 81 (1), 21 (2024)
   PUBMED   38196006
  REMARK    GeneRIF: Delineating the mechanism of fragility at BCL6 breakpoint
            region associated with translocations in diffuse large B cell
            lymphoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 706)
  AUTHORS   Blomme,S., De Paepe,P., Devos,H., Emmerechts,J., Snauwaert,S. and
            Cauwelier,B.
  TITLE     Alternative genetic alterations of MYC, BCL2, and/or BCL6 in
            high-grade B-cell lymphoma (HGBL) and diffuse large B-cell lymphoma
            (DLBCL): Can we identify different prognostic subgroups?
  JOURNAL   Genes Chromosomes Cancer 63 (1), e23211 (2024)
   PUBMED   37897298
  REMARK    GeneRIF: Alternative genetic alterations of MYC, BCL2, and/or BCL6
            in high-grade B-cell lymphoma (HGBL) and diffuse large B-cell
            lymphoma (DLBCL): Can we identify different prognostic subgroups?
REFERENCE   5  (residues 1 to 706)
  AUTHORS   Tacho-Pinot,R., Stamper,C.T., King,J.I., Matei-Rascu,V.,
            Richardson,E., Li,Z., Roberts,L.B., Bassett,J.W., Melo-Gonzalez,F.,
            Fiancette,R., Lin,I.H., Dent,A., Harada,Y., Finlay,C., Mjosberg,J.,
            Withers,D.R. and Hepworth,M.R.
  TITLE     Bcl6 is a subset-defining transcription factor of lymphoid tissue
            inducer-like ILC3
  JOURNAL   Cell Rep 42 (11), 113425 (2023)
   PUBMED   37950867
  REMARK    GeneRIF: Bcl6 is a subset-defining transcription factor of lymphoid
            tissue inducer-like ILC3.
REFERENCE   6  (residues 1 to 706)
  AUTHORS   Flenghi,L., Ye,B.H., Fizzotti,M., Bigerna,B., Cattoretti,G.,
            Venturi,S., Pacini,R., Pileri,S., Lo Coco,F., Pescarmona,E. et al.
  TITLE     A specific monoclonal antibody (PG-B6) detects expression of the
            BCL-6 protein in germinal center B cells
  JOURNAL   Am J Pathol 147 (2), 405-411 (1995)
   PUBMED   7639334
REFERENCE   7  (residues 1 to 706)
  AUTHORS   Cattoretti,G., Chang,C.C., Cechova,K., Zhang,J., Ye,B.H.,
            Falini,B., Louie,D.C., Offit,K., Chaganti,R.S. and Dalla-Favera,R.
  TITLE     BCL-6 protein is expressed in germinal-center B cells
  JOURNAL   Blood 86 (1), 45-53 (1995)
   PUBMED   7795255
REFERENCE   8  (residues 1 to 706)
  AUTHORS   Onizuka,T., Moriyama,M., Yamochi,T., Kuroda,T., Kazama,A.,
            Kanazawa,N., Sato,K., Kato,T., Ota,H. and Mori,S.
  TITLE     BCL-6 gene product, a 92- to 98-kD nuclear phosphoprotein, is
            highly expressed in germinal center B cells and their neoplastic
            counterparts
  JOURNAL   Blood 86 (1), 28-37 (1995)
   PUBMED   7795234
REFERENCE   9  (residues 1 to 706)
  AUTHORS   Lichter,P., Bray,P., Ried,T., Dawid,I.B. and Ward,D.C.
  TITLE     Clustering of C2-H2 zinc finger motif sequences within telomeric
            and fragile site regions of human chromosomes
  JOURNAL   Genomics 13 (4), 999-1007 (1992)
   PUBMED   1505991
REFERENCE   10 (residues 1 to 706)
  AUTHORS   Bray,P., Lichter,P., Thiesen,H.J., Ward,D.C. and Dawid,I.B.
  TITLE     Characterization and mapping of human genes encoding zinc finger
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 88 (21), 9563-9567 (1991)
   PUBMED   1946370
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB079847.1, BC150184.1 and
            BC146796.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 21, 2002 this sequence version replaced NP_001697.1.
            
            Summary: The protein encoded by this gene is a zinc finger
            transcription factor and contains an N-terminal POZ domain. This
            protein acts as a sequence-specific repressor of transcription, and
            has been shown to modulate the transcription of STAT-dependent IL-4
            responses of B cells. This protein can interact with a variety of
            POZ-containing proteins that function as transcription
            corepressors. This gene is found to be frequently translocated and
            hypermutated in diffuse large-cell lymphoma (DLCL), and may be
            involved in the pathogenesis of DLCL. Alternatively spliced
            transcript variants encoding different protein isoforms have been
            found for this gene. [provided by RefSeq, Aug 2015].
            
            Transcript Variant: This variant (1) and variant 2 encode the same
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150184.1, AK308162.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000406870.7/ ENSP00000384371.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.3"
     Protein         1..706
                     /product="B-cell lymphoma 6 protein isoform 1"
                     /note="lymphoma-associated zinc finger gene on chromosome
                     3; zinc finger protein 51; cys-his2 zinc finger
                     transcription factor; zinc finger transcription factor
                     BCL6S; B-cell lymphoma 6 protein transcript; zinc finger
                     and BTB domain-containing protein 27; BCL-5; BCL-6;
                     protein LAZ-3; B-cell lymphoma 5 protein; B cell
                     CLL/lymphoma 6"
                     /calculated_mol_wt=78716
     Region          8..125
                     /region_name="BTB_POZ_ZBTB27_BCL6"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in B-cell lymphoma
                     6 protein (BCL-6); cd18331"
                     /db_xref="CDD:349640"
     Site            order(8..14,17..18,21,24,28,51..55,58,114..116,120)
                     /site_type="other"
                     /note="co-repressor binding site [polypeptide binding]"
                     /db_xref="CDD:349640"
     Site            order(8..11,14..16,18..19,21..22,25,28,30..31,46..48,
                     51..53,58,67,89..90,93..97,116,120)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349640"
     Site            order(21,24..25,28,51..55,58,113..115)
                     /site_type="inhibition"
                     /note="inhibitor binding site [chemical binding]"
                     /db_xref="CDD:349640"
     Region          <172..426
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          317..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41182.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:9649500,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P41182.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:9649500; propagated from
                     UniProtKB/Swiss-Prot (P41182.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41183; propagated from
                     UniProtKB/Swiss-Prot (P41182.1)"
     Region          376..379
                     /region_name="Required for interaction with NuRD complex
                     and for transcriptional repressor activity"
                     /note="propagated from UniProtKB/Swiss-Prot (P41182.1)"
     Site            379
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:12402037; propagated from
                     UniProtKB/Swiss-Prot (P41182.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41183; propagated from
                     UniProtKB/Swiss-Prot (P41182.1)"
     Region          407..467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41182.1)"
     Region          520..541
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          548..568
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          560..585
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          576..596
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(581,583,585,587..588,591..592,595,609,611,615..616,
                     619..620,623,637,639,641,643..644,647..648,651)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          588..613
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          604..624
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          616..641
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          632..652
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          645..669
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          660..678
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..706
                     /gene="BCL6"
                     /gene_synonym="BCL5; BCL6A; LAZ3; ZBTB27; ZNF51"
                     /coded_by="NM_001706.5:109..2229"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3289.1"
                     /db_xref="GeneID:604"
                     /db_xref="HGNC:HGNC:1001"
                     /db_xref="MIM:109565"
ORIGIN      
        1 maspadsciq ftrhasdvll nlnrlrsrdi ltdvvivvsr eqfrahktvl macsglfysi
       61 ftdqlkcnls vinldpeinp egfcilldfm ytsrlnlreg nimavmatam ylqmehvvdt
      121 crkfikasea emvsaikppr eeflnsrmlm pqdimayrgr evvennlplr sapgcesraf
      181 apslysglst ppasysmysh lpvssllfsd eefrdvrmpv anpfpkeral pcdsarpvpg
      241 eysrptlevs pnvchsniys pketipeear sdmhysvaeg lkpaapsarn apyfpcdkas
      301 keeerpssed eialhfeppn aplnrkglvs pqspqksdcq pnsptescss knacilqasg
      361 sppaksptdp kacnwkkykf ivlnslnqna kpegpeqael grlsprayta ppacqppmep
      421 enldlqsptk lsasgedsti pqasrlnniv nrsmtgsprs sseshsplym hppkctscgs
      481 qspqhaemcl htagptfpee mgetqseysd sscengaffc necdcrfsee aslkrhtlqt
      541 hsdkpykcdr cqasfrykgn lashktvhtg ekpyrcnicg aqfnrpanlk thtrihsgek
      601 pykcetcgar fvqvahlrah vlihtgekpy pceicgtrfr hlqtlkshlr ihtgekpyhc
      661 ekcnlhfrhk sqlrlhlrqk hgaitntkvq yrvsatdlpp elpkac
//
LOCUS       NP_699195                241 aa            linear   PRI 27-APR-2025
DEFINITION  Golgi-associated RAB2 interactor protein 6 [Homo sapiens].
ACCESSION   NP_699195
VERSION     NP_699195.1
DBSOURCE    REFSEQ: accession NM_153364.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB055853.1, BC031221.1, AC141554.5, AA401734.1, DB514813.1 and
            AW181907.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.281509.1,
                                           SRR5189667.183011.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324341.2/ ENSP00000315247.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.1"
     Protein         1..241
                     /product="Golgi-associated RAB2 interactor protein 6"
                     /note="protein FAM71C; family with sequence similarity 71
                     member C; Golgi associated RAB2 interactor protein 6"
                     /calculated_mol_wt=27341
     Region          115..183
                     /region_name="DUF3699"
                     /note="Protein of unknown function (DUF3699); pfam12480"
                     /db_xref="CDD:463601"
     CDS             1..241
                     /gene="GARIN6"
                     /gene_synonym="FAM71C"
                     /coded_by="NM_153364.4:423..1148"
                     /db_xref="CCDS:CCDS9072.1"
                     /db_xref="GeneID:196472"
                     /db_xref="HGNC:HGNC:28594"
ORIGIN      
        1 medccmlpyy taqsspamgm fntsmgklqr qlykgeytif ryapmfesdf iqiskrgevi
       61 dvhnrarmvt mgivrtspcl tlpdvmllar paavcdnarc gpatqkresp paeileltrl
      121 lplmfvkiti hnsvkkqlhl klatgrsfyl qlcppsdase dlfvhwenlv yilrppveay
      181 sdtrailagn tldssvleev qrspvgyamk fceekeqfri srlhmnaemf gstycdytie
      241 i
//
LOCUS       NP_001351483             381 aa            linear   ROD 27-APR-2025
DEFINITION  ELMO domain-containing protein 3 [Mus musculus].
ACCESSION   NP_001351483 XP_011239601
VERSION     NP_001351483.1
DBSOURCE    REFSEQ: accession NM_001364554.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Turn,R.E., Hu,Y., Dewees,S.I., Devi,N., East,M.P., Hardin,K.R.,
            Khatib,T., Linnert,J., Wolfrum,U., Lim,M.J., Casanova,J.E.,
            Caspary,T. and Kahn,R.A.
  TITLE     The ARF GAPs ELMOD1 and ELMOD3 act at the Golgi and cilia to
            regulate ciliogenesis and ciliary protein traffic
  JOURNAL   Mol Biol Cell 33 (2), ar13 (2022)
   PUBMED   34818063
  REMARK    GeneRIF: The ARF GAPs ELMOD1 and ELMOD3 act at the Golgi and cilia
            to regulate ciliogenesis and ciliary protein traffic.
            Erratum:[Mol Biol Cell. 2022 Jun 1;33(7):cor1. doi:
            10.1091/mbc.E21-09-0443_corr. PMID: 35612986]
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Li,W., Feng,Y., Chen,A., Li,T., Huang,S., Liu,J., Liu,X., Liu,Y.,
            Gao,J., Yan,D., Sun,J., Mei,L., Liu,X. and Ling,J.
  TITLE     Elmod3 knockout leads to progressive hearing loss and abnormalities
            in cochlear hair cell stereocilia
  JOURNAL   Hum Mol Genet 28 (24), 4103-4112 (2019)
   PUBMED   31628468
  REMARK    GeneRIF: Finding associates Elmod3 deficiencies with stereocilia
            dysmorphologies and reveals that they might play roles in the actin
            cytoskeleton dynamics in cochlear hair cells, and thus relate to
            hearing impairment.
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Gineste,C., De Winter,J.M., Kohl,C., Witt,C.C., Giannesini,B.,
            Brohm,K., Le Fur,Y., Gretz,N., Vilmen,C., Pecchi,E., Jubeau,M.,
            Cozzone,P.J., Stienen,G.J., Granzier,H., Labeit,S.,
            Ottenheijm,C.A., Bendahan,D. and Gondin,J.
  TITLE     In vivo and in vitro investigations of heterozygous nebulin
            knock-out mice disclose a mild skeletal muscle phenotype
  JOURNAL   Neuromuscul Disord 23 (4), 357-369 (2013)
   PUBMED   23375831
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Sevajol,M., Reiser,J.B., Chouquet,A., Perard,J., Ayala,I., Gans,P.,
            Kleman,J.P. and Housset,D.
  TITLE     The C-terminal polyproline-containing region of ELMO contributes to
            an increase in the life-time of the ELMO-DOCK complex
  JOURNAL   Biochimie 94 (3), 823-828 (2012)
   PUBMED   22177965
  REMARK    GeneRIF: The data demonstrate the ability of the SH3 domain of
            DOCK180 to interact with ELMO1, regardless of the presence of the
            polyproline-containing C-terminal end.
REFERENCE   7  (residues 1 to 381)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU614609.1, AK049155.1, AK084010.1 and BE944793.1.
            
            On Jun 22, 2018 this sequence version replaced XP_011239601.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660817.20999.1,
                                           SRR7345562.4684786.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 32.27 cM"
     Protein         1..381
                     /product="ELMO domain-containing protein 3"
                     /note="RNA binding motif and ELMO domain 1; RNA-binding
                     motif and ELMO domain-containing protein 1"
                     /calculated_mol_wt=42528
     Region          154..313
                     /region_name="ELMO_CED12"
                     /note="ELMO/CED-12 family; pfam04727"
                     /db_xref="CDD:461411"
     CDS             1..381
                     /gene="Elmod3"
                     /gene_synonym="C330008I15Rik; Rbed1; RBM29"
                     /coded_by="NM_001364554.1:759..1904"
                     /db_xref="CCDS:CCDS20243.1"
                     /db_xref="GeneID:232089"
                     /db_xref="MGI:MGI:2445168"
ORIGIN      
        1 msetscsffi ekefqdgqle nvsaglsssy kdkgalmafr gipiseltnh gilqaltaet
       61 ngwqpgvvse evlraqeewe vvdtihpdie sgvhcqqpgq lisfnealeh fqsvdlssfk
      121 kriqptiqrt glaalrhclf gppklhqglr eerdlvltia qcgldsqnpt hgrvlqtiyk
      181 kltgskfdca lhgdhwedlg fqganpatdl rgagflallh llylvmdskt flmaqeifrl
      241 shhhiqqfpf clmsvnitri aiqalreecl srecnrrqkv ipvvnsfyaa tflhlarvwr
      301 tqqktildsg fvlkdleala kkspkrllkt lddylaqvsk gqtslleahk rpgsqgphsr
      361 dltftgvcdl qshsfesagl i
//
LOCUS       NP_001158764             449 aa            linear   VRT 27-APR-2025
DEFINITION  N-lysine methyltransferase setd6 [Salmo salar].
ACCESSION   NP_001158764
VERSION     NP_001158764.1
DBSOURCE    REFSEQ: accession NM_001165292.2
KEYWORDS    RefSeq.
SOURCE      Salmo salar (Atlantic salmon)
  ORGANISM  Salmo salar
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
            Salmoniformes; Salmonidae; Salmoninae; Salmo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Leong,J.S., Jantzen,S.G., von Schalburg,K.R., Cooper,G.A.,
            Messmer,A.M., Liao,N.Y., Munro,S., Moore,R., Holt,R.A., Jones,S.J.,
            Davidson,W.S. and Koop,B.F.
  TITLE     Salmo salar and Esox lucius full-length cDNA sequences reveal
            changes in evolutionary pressures on a post-tetraploidization
            genome
  JOURNAL   BMC Genomics 11, 279 (2010)
   PUBMED   20433749
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BT058638.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BT058638.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02864160, SAMN02864166
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Salmo salar"
                     /db_xref="taxon:8030"
                     /chromosome="ssa10"
                     /map="ssa10"
     Protein         1..449
                     /product="N-lysine methyltransferase setd6"
                     /EC_number="2.1.1.-"
                     /note="SET domain-containing protein 6"
                     /calculated_mol_wt=51202
     Region          28..273
                     /region_name="SET_SETD6"
                     /note="SET domain found in SET domain-containing protein 6
                     (SETD6) and similar proteins; cd19178"
                     /db_xref="CDD:380955"
     Site            order(43..45,192..193,219..224,256,268,270)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380955"
     Site            order(44..45,62,190..195,219..223,231,254..257)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380955"
     Region          300..440
                     /region_name="Rubis-subs-bind"
                     /note="Rubisco LSMT substrate-binding; pfam09273"
                     /db_xref="CDD:462737"
     CDS             1..449
                     /gene="setd6"
                     /coded_by="NM_001165292.2:103..1452"
                     /db_xref="GeneID:100306753"
ORIGIN      
        1 matdakrlkt egsdplqsfl qwcegvglkl nnkvyiskeg tvaeygmlak edidegellf
       61 tiprmallhq gttkvlavle egkaslents gwvplllalm yeytspqshw rpylslwsdf
      121 taldhpmfws kderdrllkg tgipeavdtd ltniqkeykd ivlpfitlhp dlwdperhtl
      181 dlyrslvafv maysfqepld eededekdpn ppmmvpiadm lnhvsnhnan leytpeclkm
      241 vsvrsirkge evfntygqma nwqllhmygl xepyqsnsnd tadipmsnvy kaavqvtrse
      301 aeqrllvekw sllcememvg dkgvfifgks gsltdtemyt tlkilcmsve efedfreneg
      361 weeadddeek mlqalsnegl pslppvwrcl vhaaarftld sygedmlkdk vlledkdgya
      421 klssrqrral qvrygqktil hqlleltkp
//
LOCUS       NP_002904               1147 aa            linear   PRI 27-APR-2025
DEFINITION  replication factor C subunit 1 isoform 1 [Homo sapiens].
ACCESSION   NP_002904 NP_006072
VERSION     NP_002904.3
DBSOURCE    REFSEQ: accession NM_002913.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1147)
  AUTHORS   Schaub,A., Erdmann,H., Scholz,V., Timmer,M., Cordts,I., Gunther,R.,
            Reilich,P., Abicht,A. and Schoberl,F.
  TITLE     Analysis and occurrence of biallelic pathogenic repeat expansions
            in RFC1 in a German cohort of patients with a main clinical
            phenotype of motor neuron disease
  JOURNAL   J Neurol 271 (9), 5804-5812 (2024)
   PUBMED   38916676
  REMARK    GeneRIF: Analysis and occurrence of biallelic pathogenic repeat
            expansions in RFC1 in a German cohort of patients with a main
            clinical phenotype of motor neuron disease.
REFERENCE   2  (residues 1 to 1147)
  AUTHORS   Milovanovic,A., Dragasevic-Miskovic,N., Thomsen,M., Borsche,M.,
            Hinrichs,F., Westenberger,A., Klein,C., Bruggemann,N.,
            Brankovic,M., Marjanovic,A., Svetel,M., Kostic,V.S. and Lohmann,K.
  TITLE     RFC1 and FGF14 Repeat Expansions in Serbian Patients with
            Cerebellar Ataxia
  JOURNAL   Mov Disord Clin Pract 11 (6), 626-633 (2024)
   PUBMED   38487929
  REMARK    GeneRIF: RFC1 and FGF14 Repeat Expansions in Serbian Patients with
            Cerebellar Ataxia.
REFERENCE   3  (residues 1 to 1147)
  AUTHORS   Kudo,K., Hori,K., Asamitsu,S., Maeda,K., Aida,Y., Hokimoto,M.,
            Matsuo,K., Yabuki,Y. and Shioda,N.
  TITLE     Structural polymorphism of the nucleic acids in pentanucleotide
            repeats associated with the neurological disorder CANVAS
  JOURNAL   J Biol Chem 300 (4), 107138 (2024)
   PUBMED   38447794
  REMARK    GeneRIF: Structural polymorphism of the nucleic acids in
            pentanucleotide repeats associated with the neurological disorder
            CANVAS.
REFERENCE   4  (residues 1 to 1147)
  AUTHORS   Miranda,C. M, Diaz,M., Hughes,G. R, Barreto,Y. M, Nakousi,C. N and
            Campero,S. M.
  TITLE     [Late-Onset Cerebellar Ataxia with Neuropathy: Uncovering the Role
            of RFC1 Gene Mutations]
  JOURNAL   Rev Med Chil 151 (4), 524-529 (2023)
   PUBMED   38687529
  REMARK    GeneRIF: [Late-Onset Cerebellar Ataxia with Neuropathy: Uncovering
            the Role of RFC1 Gene Mutations].
REFERENCE   5  (residues 1 to 1147)
  AUTHORS   Lu,Y. and Riegel,A.T.
  TITLE     The human DNA-binding protein, PO-GA, is homologous to the large
            subunit of mouse replication factor C: regulation by alternate 3'
            processing of mRNA
  JOURNAL   Gene 145 (2), 261-265 (1994)
   PUBMED   7914507
REFERENCE   6  (residues 1 to 1147)
  AUTHORS   Luckow,B., Bunz,F., Stillman,B., Lichter,P. and Schutz,G.
  TITLE     Cloning, expression, and chromosomal localization of the
            140-kilodalton subunit of replication factor C from mice and humans
  JOURNAL   Mol Cell Biol 14 (3), 1626-1634 (1994)
   PUBMED   8114700
REFERENCE   7  (residues 1 to 1147)
  AUTHORS   Bunz,F., Kobayashi,R. and Stillman,B.
  TITLE     cDNAs encoding the large subunit of human replication factor C
  JOURNAL   Proc Natl Acad Sci U S A 90 (23), 11014-11018 (1993)
   PUBMED   8248204
REFERENCE   8  (residues 1 to 1147)
  AUTHORS   Lu,Y., Zeft,A.S. and Riegel,A.T.
  TITLE     Cloning and expression of a novel human DNA binding protein, PO-GA
  JOURNAL   Biochem Biophys Res Commun 193 (2), 779-786 (1993)
   PUBMED   8512577
REFERENCE   9  (residues 1 to 1147)
  AUTHORS   Cortese,A., Reilly,M.M. and Houlden,H.
  TITLE     RFC1 CANVAS / Spectrum Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   33237689
REFERENCE   10 (residues 1 to 1147)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA336360.1, BC051751.1 and
            BC035297.1.
            
            On Jul 11, 2003 this sequence version replaced NP_002904.2.
            
            Summary: This gene encodes the large subunit of replication factor
            C, a five subunit DNA polymerase accessory protein, which is a
            DNA-dependent ATPase required for eukaryotic DNA replication and
            repair. The large subunit acts as an activator of DNA polymerases,
            binds to the 3' end of primers, and promotes coordinated synthesis
            of both strands. It may also have a role in telomere stability.
            Alternatively spliced transcript variants encoding different
            isoforms have been noted for this gene. [provided by RefSeq, Mar
            2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC051751.1, SRR1803615.88138.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000349703.7/ ENSP00000261424.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..1147
                     /product="replication factor C subunit 1 isoform 1"
                     /note="replication factor C1; MHC binding factor, beta; A1
                     140 kDa subunit; RF-C 140 kDa subunit; activator 1 subunit
                     1; DNA-binding protein PO-GA; activator 1 large subunit;
                     activator 1 140 kDa subunit; replication factor C large
                     subunit; replication factor C 140 kDa subunit; replication
                     factor C (activator 1) 1, 145kDa"
                     /calculated_mol_wt=128053
     Region          <14..404
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          46..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35251.4)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P35251.4)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35251.4)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P35251.4)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35251.4)"
     Region          228..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35251.4)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35601; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Region          402..480
                     /region_name="BRCT_RFC1"
                     /note="BRCT domain of replication factor C subunit 1
                     (RFC1) and similar proteins; cd17752"
                     /db_xref="CDD:349383"
     Site            order(414..416,423,436..440,452..458,461)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:349383"
     Region          496..538
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35251.4)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35601; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Region          584..>1002
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          914..1067
                     /region_name="RFC1"
                     /note="Replication factor RFC1 C terminal domain;
                     pfam08519"
                     /db_xref="CDD:462507"
     Region          1080..1147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35251.4)"
     Site            1103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Site            1105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35251.4)"
     Region          1119..1123
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35251.4)"
     CDS             1..1147
                     /gene="RFC1"
                     /gene_synonym="A1; CANVAS; MHCBFB; PO-GA; RECC1; RFC;
                     RFC140"
                     /coded_by="NM_002913.5:122..3565"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3450.1"
                     /db_xref="GeneID:5981"
                     /db_xref="HGNC:HGNC:9969"
                     /db_xref="MIM:102579"
ORIGIN      
        1 mdirkffgvi psgkklvset vkknektksd eetlkakkgi keikvnssrk eddfkqkqps
       61 kkkriiydsd seseetlqvk nakkppeklp vsskpgkisr qdpvtyiset deeddfmckk
      121 aaskskengr stnshlgtsn mkkneentkt knkplspikl tptsvldyfg tgsvqrsnkk
      181 mvaskrkels qntdesglnd eaiakqlqld edaelerqlh edeefartla mldeepktkk
      241 arkdteaget fssvqanlsk aekhkyphkv ktaqvsderk sysprkqsky esskesqqhs
      301 kssadkigev sspkasskla imkrkeessy keiepvaskr kenaiklkge tktpkktkss
      361 pakkesvspe dsekkrtnyq ayrsylnreg pkalgskeip kgaenclegl ifvitgvles
      421 ierdeaksli eryggkvtgn vskktnylvm grdsgqsksd kaaalgtkii dedgllnlir
      481 tmpgkkskye iavetemkke sklertpqkn vqgkrkisps kkeseskksr ptskrdslak
      541 tikketdvfw ksldfkeqva eetsgdskar nladdssenk venllwvdky kptslktiig
      601 qqgdqscank llrwlrnwqk sssedkkhak fgkfsgkddg ssfkaallsg ppgvgkttta
      661 slvcqelgys yvelnasdtr sksslkaiva eslnntsikg fysngaassv stkhalimde
      721 vdgmagnedr ggiqeligli khtkipiicm cndrnhpkir slvhycfdlr fqrprveqik
      781 gammsiafke glkipppamn eiilganqdi rqvlhnlsmw carskaltyd qakadshrak
      841 kdikmgpfdv arkvfaagee tahmslvdks dlffhdysia plfvqenyih vkpvaaggdm
      901 kkhlmllsra adsicdgdlv dsqirskqnw sllpaqaiya svlpgelmrg ymtqfptfps
      961 wlgkhsstgk hdrivqdlal hmslrtyssk rtvnmdylsl lrdalvqplt sqgvdgvqdv
     1021 valmdtyylm kedfenimei sswggkpspf skldpkvkaa ftraynkeah ltpyslqaik
     1081 asrhstspsl dseyneelne ddsqsdekdq daietdamik kktksskpsk pekdkeprkg
     1141 kgksskk
//
LOCUS       NP_001012661             399 aa            linear   PRI 27-APR-2025
DEFINITION  myb-related transcription factor, partner of profilin [Homo
            sapiens].
ACCESSION   NP_001012661 XP_290848
VERSION     NP_001012661.1
DBSOURCE    REFSEQ: accession NM_001012643.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Lederer,M., Jockusch,B.M. and Rothkegel,M.
  TITLE     Profilin regulates the activity of p42POP, a novel Myb-related
            transcription factor
  JOURNAL   J Cell Sci 118 (Pt 2), 331-341 (2005)
   PUBMED   15615774
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008623.4, BC044311.1 and BU196283.1.
            
            On Mar 8, 2005 this sequence version replaced XP_290848.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.448367.1,
                                           SRR3476690.560009.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162946 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322217.6/ ENSP00000325402.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..399
                     /product="myb-related transcription factor, partner of
                     profilin"
                     /note="p42 Myb-related transcription factor, partner of
                     profilin; myb-related protein p42POP"
                     /calculated_mol_wt=42377
     Region          16..92
                     /region_name="Myb_DNA-bind_5"
                     /note="Myb/SANT-like DNA-binding domain; pfam13873"
                     /db_xref="CDD:433544"
     Region          83..86
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE0.2)"
     Region          87..108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE0.2)"
     Region          127..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE0.2)"
     Region          297..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE0.2)"
     Region          358..399
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE0.2)"
     Region          382..385
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE0.2)"
     Region          390..393
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE0.2)"
     CDS             1..399
                     /gene="MYPOP"
                     /gene_synonym="P42pop"
                     /coded_by="NM_001012643.4:97..1296"
                     /db_xref="CCDS:CCDS33055.1"
                     /db_xref="GeneID:339344"
                     /db_xref="HGNC:HGNC:20178"
                     /db_xref="MIM:617861"
ORIGIN      
        1 masaaageae ettrlrkprf sfeenqilir evrahypqly gaqsrrvsva errrvwdgia
       61 akingitswk rtgqevqkrw ndfkrrtkek larvphstqg agpaaedafs aeeetifail
      121 gpgvaapgag agaeeppaap ssqppppsac pqryvlsedr redrradtsa hskagssspe
      181 pwarpsctpq eggcprpker espppsalqp vqlprlalsp pppapplppp pplaqvapsp
      241 psppppprpp ptlsasdpsl dflraqqeta nairelagtl rqglaklsea lsallpllpg
      301 tpvdslpppl pppppppppp rpvlpppapk veitpepvsv vaavvdgavv aargviiapr
      361 seegaprppp aplpphdspp hkrrkgfptr krrgrwksp
//
LOCUS       NP_004065                 69 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome c oxidase subunit 8A, mitochondrial [Homo sapiens].
ACCESSION   NP_004065
VERSION     NP_004065.1
DBSOURCE    REFSEQ: accession NM_004074.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Rotko,D., Kudin,A.P., Zsurka,G., Kulawiak,B., Szewczyk,A. and
            Kunz,W.S.
  TITLE     Molecular and Functional Effects of Loss of Cytochrome c Oxidase
            Subunit 8A
  JOURNAL   Biochemistry (Mosc) 86 (1), 33-43 (2021)
   PUBMED   33705280
  REMARK    GeneRIF: Molecular and Functional Effects of Loss of Cytochrome c
            Oxidase Subunit 8A.
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Zong,S., Wu,M., Gu,J., Liu,T., Guo,R. and Yang,M.
  TITLE     Structure of the intact 14-subunit human cytochrome c oxidase
  JOURNAL   Cell Res 28 (10), 1026-1034 (2018)
   PUBMED   30030519
REFERENCE   5  (residues 1 to 69)
  AUTHORS   Hallmann,K., Kudin,A.P., Zsurka,G., Kornblum,C., Reimann,J.,
            Stuve,B., Waltz,S., Hattingen,E., Thiele,H., Nurnberg,P., Rub,C.,
            Voos,W., Kopatz,J., Neumann,H. and Kunz,W.S.
  TITLE     Loss of the smallest subunit of cytochrome c oxidase, COX8A, causes
            Leigh-like syndrome and epilepsy
  JOURNAL   Brain 139 (Pt 2), 338-345 (2016)
   PUBMED   26685157
  REMARK    GeneRIF: COX8A is indispensable for function of human complex IV
            and its mutation causes Leigh-like syndrome and epilepsy.
REFERENCE   6  (residues 1 to 69)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 69)
  AUTHORS   Huttemann,M., Schmidt,T.R. and Grossman,L.I.
  TITLE     A third isoform of cytochrome c oxidase subunit VIII is present in
            mammals
  JOURNAL   Gene 312, 95-102 (2003)
   PUBMED   12909344
REFERENCE   8  (residues 1 to 69)
  AUTHORS   Chinnery,P.F., Taylor,R.W., Diekert,K., Lill,R., Turnbull,D.M. and
            Lightowlers,R.N.
  TITLE     Peptide nucleic acid delivery to human mitochondria
  JOURNAL   Gene Ther 6 (12), 1919-1928 (1999)
   PUBMED   10637443
  REMARK    Erratum:[Gene Ther 2000 May;7(9):813]
REFERENCE   9  (residues 1 to 69)
  AUTHORS   Rizzuto,R., Nakase,H., Darras,B., Francke,U., Fabrizi,G.M.,
            Mengel,T., Walsh,F., Kadenbach,B., DiMauro,S. and Schon,E.A.
  TITLE     A gene specifying subunit VIII of human cytochrome c oxidase is
            localized to chromosome 11 and is expressed in both muscle and
            non-muscle tissues
  JOURNAL   J Biol Chem 264 (18), 10595-10600 (1989)
   PUBMED   2543673
REFERENCE   10 (residues 1 to 69)
  AUTHORS   Van Kuilenburg,A.B., Muijsers,A.O., Demol,H., Dekker,H.L. and Van
            Beeumen,J.J.
  TITLE     Human heart cytochrome c oxidase subunit VIII. Purification and
            determination of the complete amino acid sequence
  JOURNAL   FEBS Lett 240 (1-2), 127-132 (1988)
   PUBMED   2847943
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC063025.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is the terminal enzyme of
            the respiratory chain, coupling the transfer of electrons from
            cytochrome c to molecular oxygen, with the concomitant production
            of a proton electrochemical gradient across the inner mitochondrial
            membrane. In addition to 3 mitochondrially encoded subunits, which
            perform the catalytic function, the eukaryotic enzyme contains
            nuclear-encoded smaller subunits, ranging in number from 4 in some
            organisms to 10 in mammals. It has been proposed that
            nuclear-encoded subunits may be involved in the modulation of the
            catalytic function. This gene encodes one of the nuclear-encoded
            subunits. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP271537.1, BP271677.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000314133.4/
                                                  ENSP00000321260.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..69
                     /product="cytochrome c oxidase subunit 8A, mitochondrial"
                     /EC_number="7.1.1.9"
                     /note="cytochrome c oxidase subunit VIII; cytochrome c
                     oxidase subunit 8A (ubiquitous); cytochrome c oxidase
                     subunit 8-2; cytochrome c oxidase polypeptide
                     VIII-liver/heart; cytochrome c oxidase subunit VIIIA
                     (ubiquitous)"
                     /calculated_mol_wt=7448
     Region          2..19
                     /region_name="SIFI-degron.
                     /evidence=ECO:0000269|PubMed:38297121"
                     /note="propagated from UniProtKB/Swiss-Prot (P10176.2)"
     Region          26..68
                     /region_name="Cyt_c_Oxidase_VIII"
                     /note="Cytochrome oxidase c subunit VIII. Cytochrome c
                     oxidase (CcO), the terminal oxidase in the respiratory
                     chains of eukaryotes and most bacteria, is a multi-chain
                     transmembrane protein located in the inner membrane of
                     mitochondria and the cell membrane of...; cd00930"
                     /db_xref="CDD:238470"
     Site            order(26..29,31..33,35,40,47..48,51,66)
                     /site_type="other"
                     /note="Subunit VIIIb/I interface [polypeptide binding]"
                     /db_xref="CDD:238470"
     Site            order(29,48)
                     /site_type="other"
                     /note="Subunit VIIIb/IV interface [polypeptide binding]"
                     /db_xref="CDD:238470"
     Site            order(33..35,39,50..51,55,57..58,65)
                     /site_type="other"
                     /note="Subunit VIIIb/VIIc interface [polypeptide binding]"
                     /db_xref="CDD:238470"
     Site            37..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P10176.2)"
     CDS             1..69
                     /gene="COX8A"
                     /gene_synonym="COX; COX8; COX8-2; COX8L; MC4DN15; VIII;
                     VIII-L"
                     /coded_by="NM_004074.3:62..271"
                     /db_xref="CCDS:CCDS8054.1"
                     /db_xref="GeneID:1351"
                     /db_xref="HGNC:HGNC:2294"
                     /db_xref="MIM:123870"
ORIGIN      
        1 msvltplllr gltgsarrlp vprakihslp pegklgimel avgltscfvt fllpagwils
       61 hletyrrpe
//
LOCUS       NP_001349847              70 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein eL38 [Mus musculus].
ACCESSION   NP_001349847
VERSION     NP_001349847.1
DBSOURCE    REFSEQ: accession NM_001362918.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Shi,L., Hu,H., Sun,P., Li,Z., Ji,L., Liu,S. and Zhang,J.
  TITLE     RPL38 knockdown inhibits the inflammation and apoptosis in
            chondrocytes through regulating METTL3-mediated SOCS2 m6A
            modification in osteoarthritis
  JOURNAL   Inflamm Res 71 (7-8), 977-989 (2022)
   PUBMED   35596790
  REMARK    GeneRIF: RPL38 knockdown inhibits the inflammation and apoptosis in
            chondrocytes through regulating METTL3-mediated SOCS2 m6A
            modification in osteoarthritis.
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Zhao,Q., Yan,S., Lu,J., Parker,D.J., Wu,H., Sun,Q., Crossman,D.K.,
            Liu,S., Wang,Q., Sesaki,H., Mitra,K., Liu,K. and Jiao,K.
  TITLE     Drp1 regulates transcription of ribosomal protein genes in
            embryonic hearts
  JOURNAL   J Cell Sci 135 (4) (2022)
   PUBMED   35099001
REFERENCE   4  (residues 1 to 70)
  AUTHORS   Khatter,H., Myasnikov,A.G., Natchiar,S.K. and Klaholz,B.P.
  TITLE     Structure of the human 80S ribosome
  JOURNAL   Nature 520 (7549), 640-645 (2015)
   PUBMED   25901680
REFERENCE   5  (residues 1 to 70)
  AUTHORS   Distler,U., Schmeisser,M.J., Pelosi,A., Reim,D., Kuharev,J.,
            Weiczner,R., Baumgart,J., Boeckers,T.M., Nitsch,R., Vogt,J. and
            Tenzer,S.
  TITLE     In-depth protein profiling of the postsynaptic density from mouse
            hippocampus using data-independent acquisition proteomics
  JOURNAL   Proteomics 14 (21-22), 2607-2613 (2014)
   PUBMED   25211037
REFERENCE   6  (residues 1 to 70)
  AUTHORS   Noben-Trauth,K. and Latoche,J.R.
  TITLE     Ectopic mineralization in the middle ear and chronic otitis media
            with effusion caused by RPL38 deficiency in the Tail-short (Ts)
            mouse
  JOURNAL   J Biol Chem 286 (4), 3079-3093 (2011)
   PUBMED   21062742
  REMARK    GeneRIF: Ectopic mineralization in the middle ear and chronic
            otitis media with effusion caused by RPL38 deficiency in the
            Tail-short (Ts) mouse.
REFERENCE   7  (residues 1 to 70)
  AUTHORS   Center,E.M., Marcus,N.M. and Wilson,D.B.
  TITLE     Abnormal development of the notochord and perinotochordal sheath in
            duplicitas posterior, patch and tail-short mice
  JOURNAL   Histol Histopathol 3 (4), 405-412 (1988)
   PUBMED   2980249
REFERENCE   8  (residues 1 to 70)
  AUTHORS   Munke,M., Cox,D.R., Jackson,I.J., Hogan,B.L. and Francke,U.
  TITLE     The murine Hox-2 cluster of homeo box containing genes maps distal
            on chromosome 11 near the tail-short (Ts) locus
  JOURNAL   Cytogenet Cell Genet 42 (4), 236-240 (1986)
   PUBMED   2875852
REFERENCE   9  (residues 1 to 70)
  AUTHORS   Brotherton,T.W., Chui,D.H., McFarland,E.C. and Russell,E.S.
  TITLE     Fetal erythropoiesis and hemoglobin ontogeny in tail-short (Ts/+)
            mutant mice
  JOURNAL   Blood 54 (3), 673-683 (1979)
   PUBMED   465735
REFERENCE   10 (residues 1 to 70)
  AUTHORS   Johnson,D.R.
  TITLE     The interfrontal bone and mutant genes in the mouse
  JOURNAL   J Anat 121 (Pt 3), 507-513 (1976)
   PUBMED   1018005
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL645484.14 and BY687415.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY312028.1, BY635141.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 79.82 cM"
     Protein         1..70
                     /product="large ribosomal subunit protein eL38"
                     /note="60S ribosomal protein L38"
                     /calculated_mol_wt=8073
     Region          2..68
                     /region_name="Ribosomal_L38e"
                     /note="Ribosomal L38e protein family; pfam01781"
                     /db_xref="CDD:460326"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P63173; propagated from
                     UniProtKB/Swiss-Prot (Q9JJI8.3)"
     Site            67
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63173; propagated from
                     UniProtKB/Swiss-Prot (Q9JJI8.3)"
     CDS             1..70
                     /gene="Rpl38"
                     /gene_synonym="0610025G13Rik; Rbt; Ts; Tss"
                     /coded_by="NM_001362918.1:233..445"
                     /db_xref="CCDS:CCDS36365.1"
                     /db_xref="GeneID:67671"
                     /db_xref="MGI:MGI:1914921"
ORIGIN      
        1 mprkieeikd flltarrkda ksvkikknkd nvkfkvrcsr ylytlvitdk ekaeklkqsl
       61 ppglavkdlk
//
LOCUS       NP_002553                595 aa            linear   PRI 27-APR-2025
DEFINITION  P2X purinoceptor 7 [Homo sapiens].
ACCESSION   NP_002553 NP_803177
VERSION     NP_002553.3
DBSOURCE    REFSEQ: accession NM_002562.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Yang,J.K., Kim,J., Ahn,Y.H., Bae,S.H., Baek,M.J., Lee,S.H. and
            Moon,J.S.
  TITLE     Inhibition of P2RX7 contributes to cytotoxicity by suppression of
            glycolysis and AKT activation in human hepatocellular carcinoma
  JOURNAL   BMB Rep 57 (10), 459-464 (2024)
   PUBMED   39219047
  REMARK    GeneRIF: Inhibition of P2RX7 contributes to cytotoxicity by
            suppression of glycolysis and AKT activation in human
            hepatocellular carcinoma.
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Agliardi,C., Guerini,F.R., Zanzottera,M., Bolognesi,E., Caputo,D.,
            Rovaris,M. and Clerici,M.
  TITLE     Increased concentrations of P2X7R in oligodendrocyte derived
            extracellular vesicles of Multiple sclerosis patients
  JOURNAL   Neurobiol Dis 199, 106601 (2024)
   PUBMED   38996986
  REMARK    GeneRIF: Increased concentrations of P2X7R in oligodendrocyte
            derived extracellular vesicles of Multiple sclerosis patients.
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Pegoraro,A., Grignolo,M., Ruo,L., Ricci,L. and Adinolfi,E.
  TITLE     P2X7 Variants in Pathophysiology
  JOURNAL   Int J Mol Sci 25 (12), 6673 (2024)
   PUBMED   38928378
  REMARK    GeneRIF: P2X7 Variants in Pathophysiology.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Chen,L., Liu,Y., Yue,S., Wang,H., Chen,J., Ma,W., Xu,W., Xu,M.,
            Chen,Z., Chen,X., Zhang,L. and Liang,C.
  TITLE     P2X7R Modulates NEK7-NLRP3 Interaction to Exacerbate Experimental
            Autoimmune Prostatitis via GSDMD-mediated Prostate Epithelial Cell
            Pyroptosis
  JOURNAL   Int J Biol Sci 20 (9), 3393-3411 (2024)
   PUBMED   38993566
  REMARK    GeneRIF: P2X7R Modulates NEK7-NLRP3 Interaction to Exacerbate
            Experimental Autoimmune Prostatitis via GSDMD-mediated Prostate
            Epithelial Cell Pyroptosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 595)
  AUTHORS   Lindo,J., Nogueira,C., Soares,R., Cunha,N., Almeida,M.R.,
            Rodrigues,L., Coelho,P., Rodrigues,F., Cunha,R.A. and Goncalves,T.
  TITLE     Genetic Polymorphisms of P2RX7 but Not of ADORA2A Are Associated
            with the Severity of SARS-CoV-2 Infection
  JOURNAL   Int J Mol Sci 25 (11), 6135 (2024)
   PUBMED   38892324
  REMARK    GeneRIF: Genetic Polymorphisms of P2RX7 but Not of ADORA2A Are
            Associated with the Severity of SARS-CoV-2 Infection.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 595)
  AUTHORS   Kim,M., Jiang,L.H., Wilson,H.L., North,R.A. and Surprenant,A.
  TITLE     Proteomic and functional evidence for a P2X7 receptor signalling
            complex
  JOURNAL   EMBO J 20 (22), 6347-6358 (2001)
   PUBMED   11707406
REFERENCE   7  (residues 1 to 595)
  AUTHORS   Gartland,A., Hipskind,R.A., Gallagher,J.A. and Bowler,W.B.
  TITLE     Expression of a P2X7 receptor by a subpopulation of human
            osteoblasts
  JOURNAL   J Bone Miner Res 16 (5), 846-856 (2001)
   PUBMED   11341329
  REMARK    GeneRIF: First description of the expression of functional P2X7
            receptors in a subpopulation of osteoblasts, activation of which
            can result in ATP-mediated apoptosis.
REFERENCE   8  (residues 1 to 595)
  AUTHORS   Gu,B.J., Zhang,W., Worthington,R.A., Sluyter,R., Dao-Ung,P.,
            Petrou,S., Barden,J.A. and Wiley,J.S.
  TITLE     A Glu-496 to Ala polymorphism leads to loss of function of the
            human P2X7 receptor
  JOURNAL   J Biol Chem 276 (14), 11135-11142 (2001)
   PUBMED   11150303
REFERENCE   9  (residues 1 to 595)
  AUTHORS   Buell,G.N., Talabot,F., Gos,A., Lorenz,J., Lai,E., Morris,M.A. and
            Antonarakis,S.E.
  TITLE     Gene structure and chromosomal localization of the human P2X7
            receptor
  JOURNAL   Recept Channels 5 (6), 347-354 (1998)
   PUBMED   9826911
REFERENCE   10 (residues 1 to 595)
  AUTHORS   Rassendren,F., Buell,G.N., Virginio,C., Collo,G., North,R.A. and
            Surprenant,A.
  TITLE     The permeabilizing ATP receptor, P2X7. Cloning and expression of a
            human cDNA
  JOURNAL   J Biol Chem 272 (9), 5482-5486 (1997)
   PUBMED   9038151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA302256.1, AK290405.1,
            AY847300.1, KF459557.1 and AC069209.38.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 2, 2010 this sequence version replaced NP_002553.2.
            
            Summary: The product of this gene belongs to the family of
            purinoceptors for ATP. This receptor functions as a ligand-gated
            ion channel and is responsible for ATP-dependent lysis of
            macrophages through the formation of membrane pores permeable to
            large molecules. Activation of this nuclear receptor by ATP in the
            cytoplasm may be a mechanism by which cellular activity can be
            coupled to changes in gene expression. Multiple alternatively
            spliced variants have been identified, most of which fit
            nonsense-mediated decay (NMD) criteria. [provided by RefSeq, Jul
            2010].
            
            Transcript Variant: This variant (1) encodes a functional protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.180805.1,
                                           SRR1660809.33577.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000328963.10/ ENSP00000330696.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..595
                     /product="P2X purinoceptor 7"
                     /note="ATP receptor; purinergic receptor P2X, ligand gated
                     ion channel, 7; P2Z receptor; P2X7 receptor; purnergic
                     receptor P2X 7"
                     /calculated_mol_wt=68454
     Region          11..390
                     /region_name="P2X_receptor"
                     /note="ATP P2X receptor; pfam00864"
                     /db_xref="CDD:459968"
     Site            14
                     /site_type="other"
                     /note="Selectivity filter 2.
                     /evidence=ECO:0000269|PubMed:39262850; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Site            23..46
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99572.4)"
     Site            187
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20450227; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Site            202
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20450227; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20450227; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20450227; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Site            284
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20450227; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Site            329..353
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99572.4)"
     Site            342
                     /site_type="other"
                     /note="Selectivity filter 1.
                     /evidence=ECO:0000269|PubMed:28235784,
                     ECO:0000269|PubMed:39262850; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:11707406; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Site            352
                     /site_type="other"
                     /note="Selectivity filter 2.
                     /evidence=ECO:0000269|PubMed:39262850; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Site            356
                     /site_type="other"
                     /note="Selectivity filter 2.
                     /evidence=ECO:0000269|PubMed:39262850; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Region          360..377
                     /region_name="C-cys anchor.
                     /evidence=ECO:0000250|UniProtKB:Q64663"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99572.4)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99572.4)"
     Region          395..595
                     /region_name="Cytoplasmic ballast.
                     /evidence=ECO:0000250|UniProtKB:Q64663"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99572.4)"
     Region          400..592
                     /region_name="P2RX7_C"
                     /note="P2X purinoreceptor 7 intracellular domain;
                     pfam20478"
                     /db_xref="CDD:466627"
     CDS             1..595
                     /gene="P2RX7"
                     /gene_synonym="P2X7"
                     /coded_by="NM_002562.6:96..1883"
                     /db_xref="CCDS:CCDS9213.1"
                     /db_xref="GeneID:5027"
                     /db_xref="HGNC:HGNC:8537"
                     /db_xref="MIM:602566"
ORIGIN      
        1 mpaccscsdv fqyetnkvtr iqsmnygtik wffhviifsy vcfalvsdkl yqrkepviss
       61 vhtkvkgiae vkeeivengv kklvhsvfdt adytfplqgn sffvmtnflk tegqeqrlcp
      121 eyptrrtlcs sdrgckkgwm dpqskgiqtg rcvvyegnqk tcevsawcpi eaveeaprpa
      181 llnsaenftv liknnidfpg hnyttrnilp glnitctfhk tqnpqcpifr lgdifretgd
      241 nfsdvaiqgg imgieiywdc nldrwfhhcr pkysfrrldd kttnvslypg ynfryakyyk
      301 ennvekrtli kvfgirfdil vfgtggkfdi iqlvvyigst lsyfglaavf idflidtyss
      361 nccrshiypw ckccqpcvvn eyyyrkkces ivepkptlky vsfvdeshir mvnqqllgrs
      421 lqdvkgqevp rpamdftdls rlplalhdtp pipgqpeeiq llrkeatprs rdspvwcqcg
      481 sclpsqlpes hrcleelccr kkpgacitts elfrklvlsr hvlqflllyq epllaldvds
      541 tnsrlrhcay rcyatwrfgs qdmadfailp sccrwrirke fpksegqysg fkspy
//
LOCUS       NP_001355927             342 aa            linear   PRI 27-APR-2025
DEFINITION  aprataxin isoform a [Homo sapiens].
ACCESSION   NP_001355927 XP_006716854
VERSION     NP_001355927.1
DBSOURCE    REFSEQ: accession NM_001368998.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_006716854.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.610310.1,
                                           SRR1803613.181256.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..342
                     /product="aprataxin isoform a"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=38973
     Region          3..102
                     /region_name="FHA_APTX"
                     /note="forkhead associated (FHA) domain found in aprataxin
                     and similar proteins; cd22735"
                     /db_xref="CDD:438787"
     Site            order(29..31,34..36,38..42,63..65,91)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438787"
     Region          164..265
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(258,260,262..264)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            260
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          283..342
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..342
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001368998.1:118..1146"
                     /note="isoform a is encoded by transcript variant 19"
                     /db_xref="CCDS:CCDS47956.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqvqlkae cnkgyvkvkq
       61 vgvnptsids vvigkdqevk lqpgqvlhmv nelypyivef eeeaknpgle thrkrkrsgn
      121 sdsierdaaq eaeagtglep gsnsgqcsvp lkkgkdapik keslghwsqg lkismqdpkm
      181 qvykdeqvvv ikdkypkary hwlvlpwtsi sslkavareh lellkhmhtv gekvivdfag
      241 ssklrfrlgy haipsmshvh lhvisqdfds pclknkkhwn sfnteyfles qaviemvqea
      301 grvtvrdgmp ellklplrch ecqqllpsip qlkehlrkhw tq
//
LOCUS       NP_001248770            1006 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane channel-like protein 5 isoform a [Homo sapiens].
ACCESSION   NP_001248770
VERSION     NP_001248770.1
DBSOURCE    REFSEQ: accession NM_001261841.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Zhang,W., Wang,S., Zhang,X., Liu,K., Song,J., Leng,X., Luo,R. and
            Ran,L.
  TITLE     Transmembrane Channel-Like 5 (TMC5) promotes prostate cancer cell
            proliferation through cell cycle regulation
  JOURNAL   Biochimie 165, 115-122 (2019)
   PUBMED   31356847
  REMARK    GeneRIF: This findings revealed that TMC5 promoted prostate cancer
            cell proliferation through cell cycle regulation and could be a
            powerful and hopeful target for prostate cancer treatment.
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Byrne,E.M., Gehrman,P.R., Medland,S.E., Nyholt,D.R., Heath,A.C.,
            Madden,P.A., Hickie,I.B., Van Duijn,C.M., Henders,A.K.,
            Montgomery,G.W., Martin,N.G. and Wray,N.R.
  CONSRTM   Chronogen Consortium
  TITLE     A genome-wide association study of sleep habits and insomnia
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 162B (5), 439-451 (2013)
   PUBMED   23728906
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Ng,D., Hu,N., Hu,Y., Wang,C., Giffen,C., Tang,Z.Z., Han,X.Y.,
            Yang,H.H., Lee,M.P., Goldstein,A.M. and Taylor,P.R.
  TITLE     Replication of a genome-wide case-control study of esophageal
            squamous cell carcinoma
  JOURNAL   Int J Cancer 123 (7), 1610-1615 (2008)
   PUBMED   18649358
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 1006)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   5  (residues 1 to 1006)
  AUTHORS   Kurima,K., Yang,Y., Sorber,K. and Griffith,A.J.
  TITLE     Characterization of the transmembrane channel-like (TMC) gene
            family: functional clues from hearing loss and epidermodysplasia
            verruciformis
  JOURNAL   Genomics 82 (3), 300-308 (2003)
   PUBMED   12906855
REFERENCE   6  (residues 1 to 1006)
  AUTHORS   Keresztes,G., Mutai,H. and Heller,S.
  TITLE     TMC and EVER genes belong to a larger novel family, the TMC gene
            family encoding transmembrane proteins
  JOURNAL   BMC Genomics 4 (1), 24 (2003)
   PUBMED   12812529
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK304431.1, DB222660.1, BC070101.1, AK023655.1 and CR749359.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and uses
            an alternate promoter, compared to variant 1. Variants 1 and 4
            encode the same isoform (A).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304431.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000542583.7/ ENSP00000446274.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..1006
                     /product="transmembrane channel-like protein 5 isoform a"
                     /note="transmembrane channel-like protein 5"
                     /calculated_mol_wt=114666
     Region          1..289
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     Region          36..>293
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            459..479
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     Site            486..508
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     Site            526..546
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     Site            620..640
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     Site            655..675
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     Site            699..719
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     Region          724..830
                     /region_name="TMC"
                     /note="TMC domain; pfam07810"
                     /db_xref="CDD:462275"
     Site            733..753
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     Site            787..807
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     Site            836..856
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     Site            901..921
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXY8.3)"
     CDS             1..1006
                     /gene="TMC5"
                     /coded_by="NM_001261841.2:518..3538"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS45431.1"
                     /db_xref="GeneID:79838"
                     /db_xref="HGNC:HGNC:22999"
                     /db_xref="MIM:617197"
ORIGIN      
        1 msayyrnnws eedpdypdys gsqnrtqgyl ktqgypdvpg plnnpdypgt rsnpysvasr
       61 trpdypgsla epnyprslsn pdysgtrsna ysaasrtspd hptslpepdy sefqshpyhr
      121 assrqpdypg sqrnpdfags sssgnyagsr thpdhfgsle pdypgaqsns dhpgpranln
      181 hpgsrknleh tsfrinpyad slgkpdypga diqpnsppff gepdypsaed nqnlpstwre
      241 pdysdaengh dygssetpkm trgvlsrtss iqpsfrhrsd dpvgslwgen dypegiemas
      301 memansyghs lpgapgsgyv npayvgesgp vhaygnppls ecdwhkspqg qkliaslipm
      361 tsrdrikair nqprtmeekr nlrkivdkek skqthrilql ncciqclnsi srayrrskns
      421 lseilnsisl wqktlkiigg kfgtsvlsyf nflrwllkfn ifsfilnfsf iiipqftvak
      481 kntlqftgle fftgvgyfrd tvmyygfytn stiqhgnsga synmqlayif tigaclttcf
      541 fsllfsmaky frnnfinphi ysggitklif cwdftvthek avklkqknls teirenlsel
      601 rqenskltfn qlltrfsaym vawvvstgva iaccaavyyl aeynleflkt hsnpgavlll
      661 pfvvscinla vpciysmfrl veryemprhe vyvllirnif lkisiigilc yywlntvals
      721 geecwetlig qdiyrlllmd fvfslvnsfl geflrriigm qlitslglqe fdiarnvlel
      781 iyaqtlvwig iffcpllpfi qmimlfimfy sknislmmnf qppskawras qmmtffifll
      841 ffpsftgvlc tlaitiwrlk psadcgpfrg lplfihsiys widtlstrpg ylwvvwiyrn
      901 ligsvhfffi ltlivliity lywqitegrk imirllheqi inegkdkmfl iekliklqdm
      961 ekkanpsslv lerreveqqg flhlgehdgs ldlrsrrsvq egnpra
//
LOCUS       NP_000991                 51 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein eL39 [Homo sapiens].
ACCESSION   NP_000991
VERSION     NP_000991.1
DBSOURCE    REFSEQ: accession NM_001000.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 51)
  AUTHORS   Sun,F., Wei,Y., Liu,Z., Jie,Q., Yang,X., Long,P., Wang,J.,
            Xiong,Y., Li,Q., Quan,S. and Ma,Y.
  TITLE     Acylglycerol kinase promotes ovarian cancer progression and
            regulates mitochondria function by interacting with ribosomal
            protein L39
  JOURNAL   J Exp Clin Cancer Res 41 (1), 238 (2022)
   PUBMED   35934718
  REMARK    GeneRIF: Acylglycerol kinase promotes ovarian cancer progression
            and regulates mitochondria function by interacting with ribosomal
            protein L39.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 51)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 51)
  AUTHORS   Dave,B., Gonzalez,D.D., Liu,Z.B., Li,X., Wong,H., Granados,S.,
            Ezzedine,N.E., Sieglaff,D.H., Ensor,J.E., Miller,K.D., Radovich,M.,
            KarinaEtrovic,A., Gross,S.S., Elemento,O., Mills,G.B.,
            Gilcrease,M.Z. and Chang,J.C.
  TITLE     Role of RPL39 in Metaplastic Breast Cancer
  JOURNAL   J Natl Cancer Inst 109 (6), 2758642 (2016)
   PUBMED   28040796
  REMARK    GeneRIF: RPL39 mediated its cancer-promoting actions through iNOS
            signaling, which was driven by the RNA editing enzyme adenosine
            deaminase acting on RNA 1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 51)
  AUTHORS   Behrmann,E., Loerke,J., Budkevich,T.V., Yamamoto,K., Schmidt,A.,
            Penczek,P.A., Vos,M.R., Burger,J., Mielke,T., Scheerer,P. and
            Spahn,C.M.
  TITLE     Structural snapshots of actively translating human ribosomes
  JOURNAL   Cell 161 (4), 845-857 (2015)
   PUBMED   25957688
REFERENCE   5  (residues 1 to 51)
  AUTHORS   Dave,B., Granados-Principal,S., Zhu,R., Benz,S., Rabizadeh,S.,
            Soon-Shiong,P., Yu,K.D., Shao,Z., Li,X., Gilcrease,M., Lai,Z.,
            Chen,Y., Huang,T.H., Shen,H., Liu,X., Ferrari,M., Zhan,M.,
            Wong,S.T., Kumaraswami,M., Mittal,V., Chen,X., Gross,S.S. and
            Chang,J.C.
  TITLE     Targeting RPL39 and MLF2 reduces tumor initiation and metastasis in
            breast cancer by inhibiting nitric oxide synthase signaling
  JOURNAL   Proc Natl Acad Sci U S A 111 (24), 8838-8843 (2014)
   PUBMED   24876273
  REMARK    GeneRIF: RPL39 and MLF2 have roles in tumor initiation and
            metastasis in breast cancer that involve nitric oxide synthase
            signaling
REFERENCE   6  (residues 1 to 51)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   7  (residues 1 to 51)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
   PUBMED   11401437
REFERENCE   8  (residues 1 to 51)
  AUTHORS   Tsui,S.K., Lee,S.M., Fung,K.P., Waye,M.M. and Lee,C.Y.
  TITLE     Primary structures and sequence analysis of human ribosomal
            proteins L39 and S27
  JOURNAL   Biochem Mol Biol Int 40 (3), 611-616 (1996)
   PUBMED   8908372
REFERENCE   9  (residues 1 to 51)
  AUTHORS   Otsuka,S., Tanaka,M., Saito,S., Yoshimoto,K. and Itakura,M.
  TITLE     Molecular cloning of a cDNA encoding human ribosomal protein L39
  JOURNAL   Biochim Biophys Acta 1308 (2), 119-121 (1996)
   PUBMED   8764829
REFERENCE   10 (residues 1 to 51)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BX476041.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the S39E family of ribosomal proteins. It is located in the
            cytoplasm. In rat, the protein is the smallest, and one of the most
            basic, proteins of the ribosome. This gene is co-transcribed with
            the U69 small nucleolar RNA gene, which is located in its second
            intron. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.98803.1,
                                           SRR5189661.155159.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361575.4/ ENSP00000355315.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..51
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq24"
     Protein         1..51
                     /product="large ribosomal subunit protein eL39"
                     /note="60S ribosomal protein L39"
                     /calculated_mol_wt=6276
     Region          10..50
                     /region_name="Ribosomal_L39"
                     /note="Ribosomal L39 protein; pfam00832"
                     /db_xref="CDD:425894"
     CDS             1..51
                     /gene="RPL39"
                     /gene_synonym="eL39; L39; RPL39P42; RPL39_23_1806"
                     /coded_by="NM_001000.4:55..210"
                     /db_xref="CCDS:CCDS14586.1"
                     /db_xref="GeneID:6170"
                     /db_xref="HGNC:HGNC:10350"
                     /db_xref="MIM:300899"
ORIGIN      
        1 msshktfrik rflakkqkqn rpipqwirmk tgnkirynsk rrhwrrtklg l
//
LOCUS       NP_001349885            1064 aa            linear   ROD 27-APR-2025
DEFINITION  rab GTPase-activating protein 1 isoform a [Mus musculus].
ACCESSION   NP_001349885 XP_006498057
VERSION     NP_001349885.1
DBSOURCE    REFSEQ: accession NM_001362956.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Oh,R.Y., Deshwar,A.R., Marwaha,A., Sabha,N., Tropak,M., Hou,H.,
            Yuki,K.E., Wilson,M.D., Rump,P., Lunsing,R., Elserafy,N.,
            Chung,C.W.T., Hewson,S., Klein-Rodewald,T., Calzada-Wack,J.,
            Sanz-Moreno,A., Kraiger,M., Marschall,S., Fuchs,H.,
            Gailus-Durner,V., Hrabe de Angelis,M., Dowling,J. and Schulze,A.
  TITLE     Biallelic loss-of-function variants in RABGAP1 cause a novel
            neurodevelopmental syndrome
  JOURNAL   Genet Med 24 (11), 2399-2407 (2022)
   PUBMED   36083289
  REMARK    GeneRIF: Biallelic loss-of-function variants in RABGAP1 cause a
            novel neurodevelopmental syndrome.
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Samarelli,A.V., Ziegler,T., Meves,A., Fassler,R. and Bottcher,R.T.
  TITLE     Rabgap1 promotes recycling of active beta1 integrins to support
            effective cell migration
  JOURNAL   J Cell Sci 133 (18) (2020)
   PUBMED   32843574
  REMARK    GeneRIF: Rabgap1 promotes recycling of active beta1 integrins to
            support effective cell migration.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1064)
  AUTHORS   Fededa,J.P., Esk,C., Mierzwa,B., Stanyte,R., Yuan,S., Zheng,H.,
            Ebnet,K., Yan,W., Knoblich,J.A. and Gerlich,D.W.
  TITLE     MicroRNA-34/449 controls mitotic spindle orientation during
            mammalian cortex development
  JOURNAL   EMBO J 35 (22), 2386-2398 (2016)
   PUBMED   27707753
REFERENCE   5  (residues 1 to 1064)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL953890.7.
            
            On May 3, 2018 this sequence version replaced XP_006498057.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6116558.60042.1,
                                           SRR1660811.107277.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 24.19 cM"
     Protein         1..1064
                     /product="rab GTPase-activating protein 1 isoform a"
                     /note="rab6 GTPase activating protein (GAP and
                     centrosome-associated); rab GTPase-activating protein 1;
                     GAP and centrosome-associated protein; rab6
                     GTPase-activating protein GAPCenA"
                     /calculated_mol_wt=120667
     Region          1..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2AWA9.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (A2AWA9.1)"
     Region          140..268
                     /region_name="PTB_Rab6GAP"
                     /note="GTPase activating protein for Rab 6
                     Phosphotyrosine-binding (PTB) domain; cd01211"
                     /db_xref="CDD:269922"
     Site            order(146,224,244)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269922"
     Site            order(210..215,231,252,256)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269922"
     Region          302..432
                     /region_name="DUF3694"
                     /note="Kinesin protein; pfam12473"
                     /db_xref="CDD:463599"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (A2AWA9.1)"
     Region          478..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2AWA9.1)"
     Region          558..767
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            603
                     /site_type="other"
                     /note="Arginine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (A2AWA9.1)"
     Site            644
                     /site_type="other"
                     /note="Glutamine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (A2AWA9.1)"
     Region          784..>1027
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            991
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (A2AWA9.1)"
     CDS             1..1064
                     /gene="Rabgap1"
                     /gene_synonym="Gapcena; mKIAA4104"
                     /coded_by="NM_001362956.1:99..3293"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS16002.1"
                     /db_xref="GeneID:227800"
                     /db_xref="MGI:MGI:2385139"
ORIGIN      
        1 mddkasvgki svssdsvstl nsedfvlvsr qgdetpstnn gsddektglk ivgngseqql
       61 qkeladvlmd ppmddqpger sqldgegdgp lsnqlsasst inpvplvglp kpemslpvkp
      121 gqgdsevssp ftpvadedsv vfnkltylgc asvnaprsev ealrmmsilr sqcqisldvt
      181 lsvpnvsegt vrlldpqtnt eianypiyki lfcvrghdgt pesdcfafte shynaelfri
      241 hvfrceiqea vsrilysfat afrrsakqtp lsataapqtp dsdiftfsvs leikeddgkg
      301 yfsavpkdkd rqcfklrqgi dkkivicvqq tankelaier cfglllspgk dvrnsdmhll
      361 dlesmgkssd gksyvitgsw npksphfqvv neetpkdkvl fmttavdlvi tevqepvrfl
      421 letkvrvcsp nerlfwpfsk rsttenfflk lkqikqkekk nnadtlyevv cleseserer
      481 rkttaspsvr lpqsgsqssm ipsppeddee edndepllsg fgdvskecae kiletwgell
      541 skwhlnlsvr pkqlsslvrs gvpealrgev wqllagchnn dhlvekyril itkespqdsa
      601 itrdinrtfp ahdyfkdtgg dgqdslykic kaysvydeei gycqgqsfla avlllhmpee
      661 qafsvlvkim fdyglrelfk qnfedlhckf yqlerlmqey ipdlynhfld isleahmyas
      721 qwfltlftak fplymvfhii dlllcegisv ifnvalgllk tskddllltd fegalkffrv
      781 qlpkryrsee nakrlmelac ntkisqkklk kfekeyhtmr eqqaqqedpi erferenrrl
      841 qeanmrleqe nddlahelvt skialrkdld naeekadaln kellmtkqkl idaedekrrl
      901 eeesaqlkem crreldkaes eikknssiig dykqicsqls erlekqqtan kveiekirqk
      961 vddcdrcrdf fnkegrvkgi ssakgvsded tdeeketlkn qlremelela qtklqlveae
     1021 ckiqdlehhl glalsevqaa kktwfnrtls siktatgvqg ketc
//
LOCUS       NP_002893                317 aa            linear   PRI 27-APR-2025
DEFINITION  reticulocalbin-2 isoform a precursor [Homo sapiens].
ACCESSION   NP_002893
VERSION     NP_002893.1
DBSOURCE    REFSEQ: accession NM_002902.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Yao,H., Zhang,S., Xie,H., Fan,Y., Miao,M., Zhu,R., Yuan,L., Gu,M.,
            You,Y. and You,B.
  TITLE     RCN2 promotes Nasopharyngeal carcinoma progression by curbing
            Calcium flow and Mitochondrial apoptosis
  JOURNAL   Cell Oncol (Dordr) 46 (4), 1031-1048 (2023)
   PUBMED   36952101
  REMARK    GeneRIF: RCN2 promotes Nasopharyngeal carcinoma progression by
            curbing Calcium flow and Mitochondrial apoptosis.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Li,J., Taylor,A.M., Manichaikul,A., Angle,J.F. and Shi,W.
  TITLE     Reticulocalbin 2 as a Potential Biomarker and Therapeutic Target
            for Atherosclerosis
  JOURNAL   Cells 11 (7), 1107 (2022)
   PUBMED   35406670
  REMARK    GeneRIF: Reticulocalbin 2 as a Potential Biomarker and Therapeutic
            Target for Atherosclerosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Gu,J., Liu,Y., Qi,T., Qian,W., Hu,D. and Feng,W.
  TITLE     Long non-coding RNA DUXAP8 elevates RCN2 expression and facilitates
            cell malignant behaviors and angiogenesis in cervical cancer via
            sponging miR-1297
  JOURNAL   Diagn Pathol 16 (1), 105 (2021)
   PUBMED   34774078
  REMARK    GeneRIF: Long non-coding RNA DUXAP8 elevates RCN2 expression and
            facilitates cell malignant behaviors and angiogenesis in cervical
            cancer via sponging miR-1297.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Kirkpatrick,L.L., Matzuk,M.M., Dodds,D.C. and Perin,M.S.
  TITLE     Biochemical interactions of the neuronal pentraxins. Neuronal
            pentraxin (NP) receptor binds to taipoxin and taipoxin-associated
            calcium-binding protein 49 via NP1 and NP2
  JOURNAL   J Biol Chem 275 (23), 17786-17792 (2000)
   PUBMED   10748068
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Dodds,D.C., Omeis,I.A., Cushman,S.J., Helms,J.A. and Perin,M.S.
  TITLE     Neuronal pentraxin receptor, a novel putative integral membrane
            pentraxin that interacts with neuronal pentraxin 1 and 2 and
            taipoxin-associated calcium-binding protein 49
  JOURNAL   J Biol Chem 272 (34), 21488-21494 (1997)
   PUBMED   9261167
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Wang,J.Y., Zhen,D.K., Bianchi,D.W., Androphy,E.J. and Chen,J.J.
  TITLE     Assignment of the gene for ERC-55 (RCN2) to human chromosome band
            15q22.33-->q24.1 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 60-61 (1997)
   PUBMED   9533013
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Chen,J.J., Reid,C.E., Band,V. and Androphy,E.J.
  TITLE     Interaction of papillomavirus E6 oncoproteins with a putative
            calcium-binding protein
  JOURNAL   Science 269 (5223), 529-531 (1995)
   PUBMED   7624774
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Weis,K., Griffiths,G. and Lamond,A.I.
  TITLE     The endoplasmic reticulum calcium-binding protein of 55 kDa is a
            novel EF-hand protein retained in the endoplasmic reticulum by a
            carboxyl-terminal His-Asp-Glu-Leu motif
  JOURNAL   J Biol Chem 269 (29), 19142-19150 (1994)
   PUBMED   8034671
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB452318.1, AK313833.1 and
            AC051643.5.
            
            Summary: The protein encoded by this gene is a calcium-binding
            protein located in the lumen of the ER. The protein contains six
            conserved regions with similarity to a high affinity Ca(+2)-binding
            motif, the EF-hand. This gene maps to the same region as type 4
            Bardet-Biedl syndrome, suggesting a possible causative role for
            this gene in the disorder. Alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) is a predominant transcript
            and encodes isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.133488.1,
                                           SRR3476690.466817.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394885.8/ ENSP00000378349.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.3"
     Protein         1..317
                     /product="reticulocalbin-2 isoform a precursor"
                     /note="reticulocalbin 2, EF-hand calcium binding domain
                     (endoplasmic reticulum calcium-binding protein, 55kD);
                     E6-binding protein; calcium-binding protein ERC-55"
                     /calculated_mol_wt=34784
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2111
     mat_peptide     23..317
                     /product="Reticulocalbin-2. /id=PRO_0000004148"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14257.1)"
                     /calculated_mol_wt=34784
     mat_peptide     26..317
                     /product="reticulocalbin-2 isoform a"
                     /calculated_mol_wt=34528
     Region          29..296
                     /region_name="EFh_CREC_RCN2"
                     /note="EF-hand, calcium binding motif, found in
                     reticulocalbin-2 (RCN2); cd16224"
                     /db_xref="CDD:320022"
     Region          29..59
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320022"
     Region          65..94
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320022"
     Region          101..130
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320022"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14257.1)"
     Region          153..182
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320022"
     Region          190..219
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320022"
     Region          231..260
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320022"
     Region          267..296
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320022"
     Region          314..317
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU10138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14257.1)"
     CDS             1..317
                     /gene="RCN2"
                     /gene_synonym="E6BP; ERC-55; ERC55; TCBP49"
                     /coded_by="NM_002902.3:94..1047"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10291.1"
                     /db_xref="GeneID:5955"
                     /db_xref="HGNC:HGNC:9935"
                     /db_xref="MIM:602584"
ORIGIN      
        1 mrlgprtaal gllllcaaaa gagkaeelhy plgerrsdyd reallgvqed vdeyvklghe
       61 eqqkrlqaii kkidldsdgf lteselsswi qmsfkhyamq eakqqfveyd knsddtvtwd
      121 eyniqmydrv idfdentald daeeesfrkl hlkdkkrfek anqdsgpgls leefiafehp
      181 eevdymtefv iqealeehdk ngdgfvslee flgdyrwdpt anedpewilv ekdrfvndyd
      241 kdndgrldpq ellpwvvpnn qgiaqeealh lidemdlngd kklseeeile npdlfltsea
      301 tdygrqlhdd yfyhdel
//
LOCUS       NP_060790                327 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin ligase RNF121 isoform a [Homo sapiens].
ACCESSION   NP_060790
VERSION     NP_060790.2
DBSOURCE    REFSEQ: accession NM_018320.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Xiang,P., Sun,Y., Liu,Y., Shu,Q. and Zhu,Y.
  TITLE     Really interesting new gene finger protein 121 is a tumor
            suppressor of renal cell carcinoma
  JOURNAL   Gene 676, 322-328 (2018)
   PUBMED   30149063
  REMARK    GeneRIF: Study found that RNF121 was less expressed in tumor
            tissues than adjacent normal tissues of renal cell carcinoma (RCC)
            patients. Overexpression of RNF121 inhibited the growth of human
            RCC cells in vivo. Moreover, RNF121 impeded the proliferation,
            migration and invasion of human RCC cells in vitro. In addition,
            RNF121 was found to activate NF-kappaB signaling pathway via
            promoting IkappaBalpha degradation in RCC cells.
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Choi,Y., Kwon,C.H., Lee,S.J., Park,J., Shin,J.Y. and Park,D.Y.
  TITLE     Integrative analysis of oncogenic fusion genes and their functional
            impact in colorectal cancer
  JOURNAL   Br J Cancer 119 (2), 230-240 (2018)
   PUBMED   29955133
  REMARK    GeneRIF: we identified and characterised oncogenic fusion genes and
            their function in CRC, and implicated NAGLU-IKZF3 and RNF121-FOLR2
            as novel molecular targets for personalised medicine development.
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Maghsoudlou,A., Meyer,R.D., Rezazadeh,K., Arafa,E., Pudney,J.,
            Hartsough,E. and Rahimi,N.
  TITLE     RNF121 Inhibits Angiogenic Growth Factor Signaling by Restricting
            Cell Surface Expression of VEGFR-2
  JOURNAL   Traffic 17 (3), 289-300 (2016)
   PUBMED   26602861
  REMARK    GeneRIF: Over-expression of RNF121 promoted ubiquitination of
            VEGFR-2, inhibited its maturation .  RNF121 knockdown in primary
            endothelial cells reduced VEGFR-2 ubiquitination and increased its
            cell surface level.
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Zemirli,N., Pourcelot,M., Dogan,N., Vazquez,A. and Arnoult,D.
  TITLE     The E3 ubiquitin ligase RNF121 is a positive regulator of NF-kappaB
            activation
  JOURNAL   Cell Commun Signal 12, 72 (2014)
   PUBMED   25388546
  REMARK    GeneRIF: These results unveil an unexpected role of Golgi Apparatus
            and reveal RNF121 as a new player involved in the signaling leading
            to NF-kappaB activation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Zhao,Y., Hongdu,B., Ma,D. and Chen,Y.
  TITLE     Really interesting new gene finger protein 121 is a novel
            Golgi-localized membrane protein that regulates apoptosis
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 46 (8), 668-674 (2014)
   PUBMED   24928685
  REMARK    GeneRIF: This is the first study to demonstrate that RNF121 is a
            novel regulator of apoptosis and provides a new potential target
            for cancer therapy
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA209781.1, AP002490.4,
            AK023139.1, CN392009.1, AI291325.1 and AL833638.1.
            
            On Jun 10, 2002 this sequence version replaced NP_060790.1.
            
            Summary: The protein encoded by this gene contains a RING finger, a
            motif present in a variety of functionally distinct proteins and
            known to be involved in protein-protein and protein-DNA
            interactions. Several alternatively spliced transcript variants
            have been noted for this gene, however, not all are likely to
            encode viable protein products. [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.215247.1,
                                           SRR1803615.131982.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361756.8/ ENSP00000354571.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..327
                     /product="E3 ubiquitin ligase RNF121 isoform a"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin ligase RNF121"
                     /calculated_mol_wt=37752
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H920.1)"
     Site            50..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H920.1)"
     Region          <56..212
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            79..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H920.1)"
     Site            100..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H920.1)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H920.1)"
     Site            172..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H920.1)"
     Region          224..278
                     /region_name="RING-H2_RNF121-like"
                     /note="RING finger, H2 subclass, found in RING finger
                     proteins RNF121, RNF175 and similar proteins; cd16475"
                     /db_xref="CDD:438138"
     Site            306..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H920.1)"
     CDS             1..327
                     /gene="RNF121"
                     /coded_by="NM_018320.5:17..1000"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8203.1"
                     /db_xref="GeneID:55298"
                     /db_xref="HGNC:HGNC:21070"
                     /db_xref="MIM:620529"
ORIGIN      
        1 maavvevevg ggaagereld evdmsdlspe eqwrveharm hakhrgheam haemvlilia
       61 tlvvaqlllv qwkqrhprsy nmvtlfqmwv vplyftvklh wwrflviwil fsavtafvtf
      121 ratrkplvqt tprlvykwfl liykisyatg ivgymavmft lfglnllfki kpedamdfgi
      181 sllfyglyyg vlerdfaemc adymastigf ysesgmptkh lsdsvcavcg qqifvdvsee
      241 giientyrls cnhvfhefci rgwcivgkkq tcpyckekvd lkrmfsnpwe rphvmygqll
      301 dwlrylvawq pviigvvqgi nyilgle
//
LOCUS       NP_001179692             714 aa            linear   MAM 27-APR-2025
DEFINITION  palmitoyltransferase ZDHHC5 [Bos taurus].
ACCESSION   NP_001179692 XP_612592
VERSION     NP_001179692.1
DBSOURCE    REFSEQ: accession NM_001192763.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            NKLS02000015.1.
            
            On Jul 17, 2010 this sequence version replaced XP_612592.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GGVH01110711.1, GGVG01054704.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA6648753, SAMEA6648754
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="15"
                     /map="15"
                     /breed="Hereford"
     Protein         1..714
                     /product="palmitoyltransferase ZDHHC5"
                     /EC_number="2.3.1.225"
                     /note="zinc finger DHHC domain-containing protein 5; zinc
                     finger DHHC-type containing 5"
                     /calculated_mol_wt=76845
     Site            14..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDZ4; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Region          99..224
                     /region_name="DHHC"
                     /note="DHHC palmitoyltransferase; pfam01529"
                     /db_xref="CDD:396215"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            192..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Region          289..714
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDZ4; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDZ4; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDZ4; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDZ4; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            616
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0B5; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     Site            696
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDZ4; propagated from
                     UniProtKB/Swiss-Prot (E1BLT8.1)"
     CDS             1..714
                     /gene="ZDHHC5"
                     /gene_synonym="DHHC-5"
                     /coded_by="NM_001192763.3:1..2145"
                     /db_xref="BGD:BT17632"
                     /db_xref="GeneID:533250"
                     /db_xref="VGNC:VGNC:37143"
ORIGIN      
        1 mpaesakrfk pskyvpvsaa aiflvgattl ffaftcpgls lsvspavpvy navvflfvla
       61 nfsmatfmdp gvfpraeede dkeddfrapl yktveikgiq vrmkwcatcr fyrpprcshc
      121 svcdncveef dhhcpwvnnc igrrnyryff lfllsltahi tgvfgfglly vlyhmeelsg
      181 vrtavtmavm cvaglffipv agltgfhvvl vargrttneq vtgkfrggvn pftngccnnv
      241 srvlcsspap rylgrpkkek tivirppflr pevsdgqitv kimdngiqge lrrtkskgsl
      301 evtesqsada epppppkpdl srytglrthl slatneessl lgkdspptpt mykyrpgyss
      361 ssasaamphs ssaklsrgds lkeppsiaes srqpsyrsep slepesfrsp tlgkgfpfdp
      421 lssgsrsssl ksaqgtgfel gplqsirseg ttstsyksla nqtrngslsy dslltpsdsp
      481 dfesvqagpe pepplgytsp flsarlaqqr eaerhprlap ggpaprepsp vrydnlsrhi
      541 vaslqerekl lrqspppgre eepglgdsgv qctpgsghap rtssssddsk rsplgktpla
      601 rpvaprfgkp dglrgrglas pepglpapyl grsvsyssqk appgvpetee valqplltpk
      661 devqlktays ksngqpksig sappgpgqpp lssptrggvk kvsgvggtty eisv
//
LOCUS       NP_054796                112 aa            linear   PRI 27-APR-2025
DEFINITION  protein FAM32A [Homo sapiens].
ACCESSION   NP_054796
VERSION     NP_054796.1
DBSOURCE    REFSEQ: accession NM_014077.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Fica,S.M., Oubridge,C., Wilkinson,M.E., Newman,A.J. and Nagai,K.
  TITLE     A human postcatalytic spliceosome structure reveals essential roles
            of metazoan factors for exon ligation
  JOURNAL   Science 363 (6428), 710-714 (2019)
   PUBMED   30705154
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Chen,X., Zhang,H., Aravindakshan,J.P., Gotlieb,W.H. and Sairam,M.R.
  TITLE     Anti-proliferative and pro-apoptotic actions of a novel human and
            mouse ovarian tumor-associated gene OTAG-12: downregulation,
            alternative splicing and drug sensitization
  JOURNAL   Oncogene 30 (25), 2874-2887 (2011)
   PUBMED   21339736
  REMARK    GeneRIF: study showed that hOTAG-12b increases mRNAs of
            pro-apoptotic genes such as BAD, GADD45alpha and CIEDB, while
            inhibiting anti-apoptotic NAIP and Akt1 expression, suggesting that
            hOTAG-12b-induced apoptosis might be p53-independent
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 112)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 112)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG749750.1 and BC000639.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1019033.1,
                                           SRR3476690.541569.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263384.12/ ENSP00000263384.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..112
                     /product="protein FAM32A"
                     /note="ovarian tumor associated gene-12"
                     /calculated_mol_wt=13047
     Region          23..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y421.2)"
     CDS             1..112
                     /gene="FAM32A"
                     /gene_synonym="OTAG-12; OTAG12"
                     /coded_by="NM_014077.4:34..372"
                     /db_xref="CCDS:CCDS12341.1"
                     /db_xref="GeneID:26017"
                     /db_xref="HGNC:HGNC:24563"
                     /db_xref="MIM:614554"
ORIGIN      
        1 meayeqvqkg plklkgvael gvtkrkkkkk dkdkakllea mgtskkneee krrgldkrtp
       61 aqaafekmqe krqmerilkk askthkqrve dfnrhldtlt ehydipkvsw tk
//
LOCUS       NP_059978                801 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor SOX-6 isoform b [Homo sapiens].
ACCESSION   NP_059978
VERSION     NP_059978.2
DBSOURCE    REFSEQ: accession NM_017508.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Lu,M.Y., Fang,C.Y., Hsieh,P.L., Chao,S.C., Liao,Y.W., Ohiro,Y.,
            Yu,C.C. and Ho,D.C.
  TITLE     MIAT promotes myofibroblastic activities and transformation in oral
            submucous fibrosis through sponging the miR-342-3p/SOX6 axis
  JOURNAL   Aging (Albany NY) 16 (19), 12909-12927 (2024)
   PUBMED   39379100
  REMARK    GeneRIF: MIAT promotes myofibroblastic activities and
            transformation in oral submucous fibrosis through sponging the
            miR-342-3p/SOX6 axis.
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Li,M., Niu,M., Fan,X., Chen,F., Cao,H., Liu,Q., Gan,S., Yue,P. and
            Gao,J.
  TITLE     LncRNA MIR181A2HG inhibits keratinocytes proliferation through
            miR-223-3p/SOX6 axis
  JOURNAL   Aging (Albany NY) 16 (11), 9846-9858 (2024)
   PUBMED   38848163
  REMARK    GeneRIF: LncRNA MIR181A2HG inhibits keratinocytes proliferation
            through miR-223-3p/SOX6 axis.
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Pastori,V., Zambanini,G., Citterio,E., Weiss,T., Nakamura,Y.,
            Cantu,C. and Ronchi,A.E.
  TITLE     Transcriptional repression of the oncofetal LIN28B gene by the
            transcription factor SOX6
  JOURNAL   Sci Rep 14 (1), 10287 (2024)
   PUBMED   38704454
  REMARK    GeneRIF: Transcriptional repression of the oncofetal LIN28B gene by
            the transcription factor SOX6.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Zheng,H., Liu,M., Shi,S., Huang,H., Yang,X., Luo,Z., Song,Y.,
            Xu,Q., Li,T., Xue,L., Lu,F. and Wang,J.
  TITLE     MAP4K4 and WT1 mediate SOX6-induced cellular senescence by
            synergistically activating the ATF2-TGFbeta2-Smad2/3 signaling
            pathway in cervical cancer
  JOURNAL   Mol Oncol 18 (5), 1327-1346 (2024)
   PUBMED   38383842
  REMARK    GeneRIF: MAP4K4 and WT1 mediate SOX6-induced cellular senescence by
            synergistically activating the ATF2-TGFbeta2-Smad2/3 signaling
            pathway in cervical cancer.
REFERENCE   5  (residues 1 to 801)
  AUTHORS   Li,S. and Wang,Y.
  TITLE     Regulatory mechanism of DDX5 in ox-LDL-induced endothelial cell
            injury through the miR-640/SOX6 axis
  JOURNAL   Clin Hemorheol Microcirc 88 (2), 157-170 (2024)
   PUBMED   39093065
  REMARK    GeneRIF: Regulatory mechanism of DDX5 in ox-LDL-induced endothelial
            cell injury through the miR-640/SOX6 axis.
REFERENCE   6  (residues 1 to 801)
  AUTHORS   Ueda,R., Iizuka,Y., Yoshida,K., Kawase,T., Kawakami,Y. and Toda,M.
  TITLE     Identification of a human glioma antigen, SOX6, recognized by
            patients' sera
  JOURNAL   Oncogene 23 (7), 1420-1427 (2004)
   PUBMED   14691456
REFERENCE   7  (residues 1 to 801)
  AUTHORS   Cohen-Barak,O., Hagiwara,N., Arlt,M.F., Horton,J.P. and
            Brilliant,M.H.
  TITLE     Cloning, characterization and chromosome mapping of the human SOX6
            gene
  JOURNAL   Gene 265 (1-2), 157-164 (2001)
   PUBMED   11255018
REFERENCE   8  (residues 1 to 801)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 801)
  AUTHORS   Hagiwara,N., Klewer,S.E., Samson,R.A., Erickson,D.T., Lyon,M.F. and
            Brilliant,M.H.
  TITLE     Sox6 is a candidate gene for p100H myopathy, heart block, and
            sudden neonatal death
  JOURNAL   Proc Natl Acad Sci U S A 97 (8), 4180-4185 (2000)
   PUBMED   10760285
REFERENCE   10 (residues 1 to 801)
  AUTHORS   Denny,P., Swift,S., Brand,N., Dabhade,N., Barton,P. and Ashworth,A.
  TITLE     A conserved family of genes related to the testis determining gene,
            SRY
  JOURNAL   Nucleic Acids Res 20 (11), 2887 (1992)
   PUBMED   1614875
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027016.4, AC013595.11,
            AC068405.5, AC103794.2 and AC009869.7.
            
            On Dec 22, 2018 this sequence version replaced NP_059978.1.
            
            Summary: This gene encodes a member of the D subfamily of sex
            determining region y-related transcription factors that are
            characterized by a conserved DNA-binding domain termed the high
            mobility group box and by their ability to bind the minor groove of
            DNA. The encoded protein is a transcriptional activator that is
            required for normal development of the central nervous system,
            chondrogenesis and maintenance of cardiac and skeletal muscle
            cells. The encoded protein interacts with other family members to
            cooperatively activate gene expression. Alternative splicing
            results in multiple transcript variants.[provided by RefSeq, Mar
            2009].
            
            Transcript Variant: This variant (1) encodes isoform b. Variants 1
            and 3 both encode the same isoform (b).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136780.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.2"
     Protein         1..801
                     /product="transcription factor SOX-6 isoform b"
                     /note="SRY-box containing gene 6; transcription factor
                     SOX-6; SRY-box 6; SRY (sex determining region Y)-box 6"
                     /calculated_mol_wt=88857
     Region          592..669
                     /region_name="HMG-box_EGL13-like"
                     /note="high mobility group (HMG)-box found in
                     Caenorhabditis elegans protein egg laying defective 13
                     (EGL-13) and similar proteins; cd22042"
                     /db_xref="CDD:438848"
     Site            order(593,595..596,598..599,601..602,606,609,613,620..622,
                     625..626,629,632..633,651,661,663..666)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438848"
     CDS             1..801
                     /gene="SOX6"
                     /gene_synonym="HSSOX6; SOXD; TOLCAS"
                     /coded_by="NM_017508.3:210..2615"
                     /note="isoform b is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53604.1"
                     /db_xref="GeneID:55553"
                     /db_xref="HGNC:HGNC:16421"
                     /db_xref="MIM:607257"
ORIGIN      
        1 msskqatspf acaadgedam tqdltsreke egsdqhvash lplhpimhnk phseelptlv
       61 stiqqdadwd svlssqqrme sennklcsly sfrntstsph kpdegsrdre imtsvtfgtp
      121 errkgsladv vdtlkqkkle emtrteqeds scmekllskd wkekmerlnt sellgeikgt
      181 peslaekerq lstmitqlis lreqllaahd eqkklaasqi ekqrqqmdla rqqqeqiarq
      241 qqqllqqqhk inllqqqiqv qghmpplmip ifphdqrtla aaaaaqqgfl fppgitykpg
      301 dnypvqfips tmaaaaasgl splqlqqlya aqlasmqvsp gakmpstpqp pntagtvspt
      361 giknekrgts pvtqvkdeaa aqplnlssrp ktaepvkspt sptqnlfpas ktspvnlpnk
      421 ssipspiggs lgrgsslgkw ksqhqeetye ldilsslnsp alfgdqdtvm kaiqearkmr
      481 eqiqreqqqq qphgvdgkls sinnmglnsc rnekertrfe nlgpqltgks nedgklgpgv
      541 idltrpedae gskamngsaa klqqyycwpt ggatvaearv yrdargrass ephikrpmna
      601 fmvwakderr kilqafpdmh nsniskilgs rwksmsnqek qpyyeeqarl skihlekypn
      661 ykykprpkrt civdgkklri geykqlmrsr rqemrqfftv gqqpqipitt gtgvvypgai
      721 tmatttpspq mtsdcsstsa spepslpviq stygmktdgg slagneming edememyddy
      781 eddpksdyss eneapeavsa n
//
LOCUS       NP_001356637             724 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger Y-chromosomal protein isoform 2 [Homo sapiens].
ACCESSION   NP_001356637 XP_016885566
VERSION     NP_001356637.1
DBSOURCE    REFSEQ: accession NM_001369708.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Ni,W., Perez,A.A., Schreiner,S., Nicolet,C.M. and Farnham,P.J.
  TITLE     Characterization of the ZFX family of transcription factors that
            bind downstream of the start site of CpG island promoters
  JOURNAL   Nucleic Acids Res 48 (11), 5986-6000 (2020)
   PUBMED   32406922
  REMARK    GeneRIF: Characterization of the ZFX family of transcription
            factors that bind downstream of the start site of CpG island
            promoters.
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Decarpentrie,F., Vernet,N., Mahadevaiah,S.K., Longepied,G.,
            Streichemberger,E., Aknin-Seifer,I., Ojarikre,O.A., Burgoyne,P.S.,
            Metzler-Guillemain,C. and Mitchell,M.J.
  TITLE     Human and mouse ZFY genes produce a conserved testis-specific
            transcript encoding a zinc finger protein with a short acidic
            domain and modified transactivation potential
  JOURNAL   Hum Mol Genet 21 (12), 2631-2645 (2012)
   PUBMED   22407129
  REMARK    GeneRIF: Studies identified a major testis-specific ZFY transcript
            that encodes a protein with the same short acidic domain.
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 724)
  AUTHORS   Tricoli,J.V. and Bracken,R.B.
  TITLE     ZFY gene expression and retention in human prostate adenocarcinoma
  JOURNAL   Genes Chromosomes Cancer 6 (2), 65-72 (1993)
   PUBMED   7680890
REFERENCE   7  (residues 1 to 724)
  AUTHORS   Kochoyan,M., Keutmann,H.T. and Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            refinement of the NMR structure of an even finger by selective
            deuterium labeling and implications for DNA recognition
  JOURNAL   Biochemistry 30 (29), 7063-7072 (1991)
   PUBMED   1854720
REFERENCE   8  (residues 1 to 724)
  AUTHORS   North,M., Sargent,C., O'Brien,J., Taylor,K., Wolfe,J., Affara,N.A.
            and Ferguson-Smith,M.A.
  TITLE     Comparison of ZFY and ZFX gene structure and analysis of
            alternative 3' untranslated regions of ZFY
  JOURNAL   Nucleic Acids Res 19 (10), 2579-2586 (1991)
   PUBMED   2041734
REFERENCE   9  (residues 1 to 724)
  AUTHORS   Kochoyan,M., Havel,T.F., Nguyen,D.T., Dahl,C.E., Keutmann,H.T. and
            Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            2D NMR structure of an even finger and implications for
            'jumping-linker' DNA recognition
  JOURNAL   Biochemistry 30 (14), 3371-3386 (1991)
   PUBMED   1849423
REFERENCE   10 (residues 1 to 724)
  AUTHORS   Palmer,M.S., Berta,P., Sinclair,A.H., Pym,B. and Goodfellow,P.N.
  TITLE     Comparison of human ZFY and ZFX transcripts
  JOURNAL   Proc Natl Acad Sci U S A 87 (5), 1681-1685 (1990)
   PUBMED   2308929
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006157.2.
            
            On Apr 16, 2019 this sequence version replaced XP_016885566.1.
            
            Summary: This gene encodes a zinc finger-containing protein that
            may function as a transcription factor. This gene was once a
            candidate gene for the testis-determining factor (TDF) and was
            erroneously referred to as TDF. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.122495.1,
                                           SRR1803612.248990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yp11.2"
     Protein         1..724
                     /product="zinc finger Y-chromosomal protein isoform 2"
                     /note="zinc finger Y-chromosomal protein"
                     /calculated_mol_wt=82034
     Region          45..329
                     /region_name="Zfx_Zfy_act"
                     /note="Zfx / Zfy transcription activation region;
                     pfam04704"
                     /db_xref="CDD:461400"
     Region          <340..515
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          <346..>368
                     /region_name="ROS_MUCR"
                     /note="ROS/MUCR transcriptional regulator protein;
                     cl19880"
                     /db_xref="CDD:473244"
     Region          346..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          377..401
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          409..429
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(414,416,418,420..421,424..425,428,474,476,480..481,
                     484..485,488,502,504,506,508..509,512..513,516)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          462..>599
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          481..505
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          497..516
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          526..575
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          583..603
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          638..660
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          640..660
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(645,647,649,651..652,655..656,659,673,675,679..680,
                     683..684,688,702,704,706,708..709,712..713,716)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          652..676
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          668..689
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          697..717
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..724
                     /gene="ZFY"
                     /gene_synonym="ZNF911"
                     /coded_by="NM_001369708.1:84..2258"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS48201.1"
                     /db_xref="GeneID:7544"
                     /db_xref="HGNC:HGNC:12870"
                     /db_xref="MIM:490000"
ORIGIN      
        1 mdgdqivvei qeavfvsniv dsditvhnfv pddpdsvviq dvvedvviee dvqcsdilee
       61 advsenviip eqvldsdvte evslphctvp ddvlasdits tsmsmpehvl tsesmhvcdi
      121 ghvehmvhds vveaeiitdp ltsdivseev lvadcapeav idasgisvdq qdndkasced
      181 ylmislddag kiehdgstgv tidaesemdp ckvdstcpev ikvyifkadp geddlggtvd
      241 ivesependh gvelldqnss irvprekmvy mtvndsqqed edlsnnsdgi enrngtasal
      301 lhidesaglg rlakqkpkkk rrpdsrqyqt aiiigpdghp ltvypcmicg kkfksrgflk
      361 rhmknhpehl akkkyhctdc dyttnkkisl hnhleshklt skaekaiecd ecgkhfshag
      421 alfthkmvhk ekgankmhkc kfceyetaeq gllnrhllav hsknfphicv ecgkgfrhps
      481 elrkhmriht gekpyqcqyc eyrsadssnl kthiktkhsk empfkcdicl ltfsdtkevq
      541 qhtlvhqesk thqclhcdhk ssnssdlkrh visvhtkdyp hkcemcekgf hrpselkkhv
      601 avhkgkkmhq crhcdfkiad pfvlsrhils vhtkdlpfrc krcrkgfrqq nelkkhmkth
      661 sgrkvyqcey ceysttdasg fkrhvisiht kdyphrceyc kkgfrrpsek nqhimrhhke
      721 vglp
//
LOCUS       NP_660347                177 aa            linear   PRI 27-APR-2025
DEFINITION  uncharacterized protein C7orf33 [Homo sapiens].
ACCESSION   NP_660347
VERSION     NP_660347.1
DBSOURCE    REFSEQ: accession NM_145304.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Scherer,S.W., Cheung,J., MacDonald,J.R., Osborne,L.R.,
            Nakabayashi,K., Herbrick,J.A., Carson,A.R., Parker-Katiraee,L.,
            Skaug,J., Khaja,R., Zhang,J., Hudek,A.K., Li,M., Haddad,M.,
            Duggan,G.E., Fernandez,B.A., Kanematsu,E., Gentles,S.,
            Christopoulos,C.C., Choufani,S., Kwasnicka,D., Zheng,X.H., Lai,Z.,
            Nusskern,D., Zhang,Q., Gu,Z., Lu,F., Zeesman,S., Nowaczyk,M.J.,
            Teshima,I., Chitayat,D., Shuman,C., Weksberg,R., Zackai,E.H.,
            Grebe,T.A., Cox,S.R., Kirkpatrick,S.J., Rahman,N., Friedman,J.M.,
            Heng,H.H., Pelicci,P.G., Lo-Coco,F., Belloni,E., Shaffer,L.G.,
            Pober,B., Morton,C.C., Gusella,J.F., Bruns,G.A., Korf,B.R.,
            Quade,B.J., Ligon,A.H., Ferguson,H., Higgins,A.W., Leach,N.T.,
            Herrick,S.R., Lemyre,E., Farra,C.G., Kim,H.G., Summers,A.M.,
            Gripp,K.W., Roberts,W., Szatmari,P., Winsor,E.J., Grzeschik,K.H.,
            Teebi,A., Minassian,B.A., Kere,J., Armengol,L., Pujana,M.A.,
            Estivill,X., Wilson,M.D., Koop,B.F., Tosi,S., Moore,G.E.,
            Boright,A.P., Zlotorynski,E., Kerem,B., Kroisel,P.M., Petek,E.,
            Oscier,D.G., Mould,S.J., Dohner,H., Dohner,K., Rommens,J.M.,
            Vincent,J.B., Venter,J.C., Li,P.W., Mural,R.J., Adams,M.D. and
            Tsui,L.C.
  TITLE     Human chromosome 7: DNA sequence and biology
  JOURNAL   Science 300 (5620), 767-772 (2003)
   PUBMED   12690205
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC021251.2 and AC005229.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021251.2, CV029100.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307003.3/ ENSP00000304071.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..177
                     /product="uncharacterized protein C7orf33"
                     /calculated_mol_wt=19344
     Region          1..177
                     /region_name="DUF5548"
                     /note="Family of unknown function (DUF5548); pfam17702"
                     /db_xref="CDD:465463"
     CDS             1..177
                     /gene="C7orf33"
                     /coded_by="NM_145304.4:161..694"
                     /db_xref="CCDS:CCDS5890.1"
                     /db_xref="GeneID:202865"
                     /db_xref="HGNC:HGNC:21724"
ORIGIN      
        1 mqvevqslsl eecpwrlpgp qceceallps garrridlrl sgravavwvh vrggpgqfnl
       61 syatgrhkkp nphqnmnrgm efiapvsapt ksgapwhfls qgptdaqrav rirpgtrmgl
      121 ssdpvvgtls ssyldlltls ykpgrtvtss ylnvrghevr klqnsveatr isrtdss
//
LOCUS       NP_001357428             266 aa            linear   PRI 27-APR-2025
DEFINITION  olfactomedin-like protein 1 isoform b [Homo sapiens].
ACCESSION   NP_001357428
VERSION     NP_001357428.1
DBSOURCE    REFSEQ: accession NM_001370499.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Murakami,K., Kikugawa,S., Kobayashi,Y., Uehara,S., Suzuki,T.,
            Kato,H., Udagawa,N. and Nakamura,Y.
  TITLE     Olfactomedin-like protein OLFML1 inhibits Hippo signaling and
            mineralization in osteoblasts
  JOURNAL   Biochem Biophys Res Commun 505 (2), 419-425 (2018)
   PUBMED   30266405
  REMARK    GeneRIF: mutation of OLFML1 leads to impaired osteoblast
            differentiation and abnormal development of bone tissue
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wan,B., Zhou,Y.B., Zhang,X., Zhu,H., Huo,K. and Han,Z.G.
  TITLE     hOLFML1, a novel secreted glycoprotein, enhances the proliferation
            of human cancer cell lines in vitro
  JOURNAL   FEBS Lett 582 (21-22), 3185-3192 (2008)
   PUBMED   18708057
  REMARK    GeneRIF: These findings suggest that hOLFML1 may play a significant
            role in the regulation of cell proliferation in vitro.
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK297778.1 and AC107884.15.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297778.1, DA554357.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..266
                     /product="olfactomedin-like protein 1 isoform b"
                     /note="olfactomedin-like protein 1"
                     /calculated_mol_wt=30196
     Region          9..259
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; pfam02191"
                     /db_xref="CDD:460482"
     CDS             1..266
                     /gene="OLFML1"
                     /gene_synonym="MVAL564; ONT2; UNQ564"
                     /coded_by="NM_001370499.1:254..1054"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:283298"
                     /db_xref="HGNC:HGNC:24473"
ORIGIN      
        1 mypscdnmlm gikslkivkk mmdthgswmk davynspkvy lligsrnntv wefanirafm
       61 edntkpaprk qiltlswqgt gqviykgflf fhnqatsnei ikynlqkrtv edrmllpggv
      121 gralvyqhsp styidlavde hglwaihsgp gthshlvltk iepgtlgveh swdtpcrsqd
      181 aeasfllcgv lyvvystggq gphritciyd plgtiseedl pnlffpkrpr shsmihynpr
      241 dkqlyawneg nqiiyklqtk rklplk
//
LOCUS       NP_064299                289 aa            linear   ROD 27-APR-2025
DEFINITION  T-cell ecto-ADP-ribosyltransferase 2 precursor [Mus musculus].
ACCESSION   NP_064299 XP_003946451
VERSION     NP_064299.2
DBSOURCE    REFSEQ: accession NM_019915.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Leutert,M., Duan,Y., Winzer,R., Menzel,S., Tolosa,E., Magnus,T.,
            Hottiger,M.O., Koch-Nolte,F. and Rissiek,B.
  TITLE     Identification of the Mouse T Cell ADP-Ribosylome Uncovers ARTC2.2
            Mediated Regulation of CD73 by ADP-Ribosylation
  JOURNAL   Front Immunol 12, 703719 (2021)
   PUBMED   34504490
  REMARK    GeneRIF: Identification of the Mouse T Cell ADP-Ribosylome Uncovers
            ARTC2.2 Mediated Regulation of CD73 by ADP-Ribosylation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Gonde,H., Demeules,M., Hardet,R., Scarpitta,A., Junge,M.,
            Pinto-Espinoza,C., Varin,R., Koch-Nolte,F., Boyer,O. and
            Adriouch,S.
  TITLE     A Methodological Approach Using rAAV Vectors Encoding
            Nanobody-Based Biologics to Evaluate ARTC2.2 and P2X7 In Vivo
  JOURNAL   Front Immunol 12, 704408 (2021)
   PUBMED   34489954
  REMARK    GeneRIF: A Methodological Approach Using rAAV Vectors Encoding
            Nanobody-Based Biologics to Evaluate ARTC2.2 and P2X7 In Vivo.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Georgiev,H., Ravens,I., Papadogianni,G., Malissen,B., Forster,R.
            and Bernhardt,G.
  TITLE     Blocking the ART2.2/P2X7-system is essential to avoid a detrimental
            bias in functional CD4 T cell studies
  JOURNAL   Eur J Immunol 48 (6), 1078-1081 (2018)
   PUBMED   29508376
  REMARK    GeneRIF: this study shows that blocking the ART2.2/P2X7-system is
            essential to avoid a detrimental bias in functional CD4 T cell
            studies
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Garcia-Rodriguez,S., Rosal-Vela,A., Botta,D., Cumba Garcia,L.M.,
            Zumaquero,E., Prados-Maniviesa,V., Cerezo-Wallis,D., Lo Buono,N.,
            Robles-Guirado,J.A., Guerrero,S., Gonzalez-Paredes,E.,
            Andres-Leon,E., Corbi,A., Mack,M., Koch-Nolte,F., Merino,R.,
            Zubiaur,M., Lund,F.E. and Sancho,J.
  TITLE     CD38 promotes pristane-induced chronic inflammation and increases
            susceptibility to experimental lupus by an apoptosis-driven and
            TRPM2-dependent mechanism
  JOURNAL   Sci Rep 8 (1), 3357 (2018)
   PUBMED   29463868
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Menzel,S., Rissiek,B., Bannas,P., Jakoby,T., Miksiewicz,M.,
            Schwarz,N., Nissen,M., Haag,F., Tholey,A. and Koch-Nolte,F.
  TITLE     Nucleotide-Induced Membrane-Proximal Proteolysis Controls the
            Substrate Specificity of T Cell Ecto-ADP-Ribosyltransferase ARTC2.2
  JOURNAL   J Immunol 195 (5), 2057-2066 (2015)
   PUBMED   26209623
  REMARK    GeneRIF: Data show that shedding of T Cell
            Ecto-ADP-ribosyltransferase ARTC2.2 alters its substrate profile.
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Koch-Nolte,F., Kuhl,M., Haag,F., Cetkovic-Cvrlje,M., Leiter,E.H.
            and Thiele,H.G.
  TITLE     Assignment of the human and mouse genes for muscle ecto mono
            (ADPribosyl)transferase to a conserved linkage group on human
            chromosome 11p15 and mouse chromosome 7
  JOURNAL   Genomics 36 (1), 215-216 (1996)
   PUBMED   8812442
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Hollmann,C., Haag,F., Schlott,M., Damaske,A., Bertuleit,H.,
            Matthes,M., Kuhl,M., Thiele,H.G. and Koch-Nolte,F.
  TITLE     Molecular characterization of mouse T-cell
            ecto-ADP-ribosyltransferase Rt6: cloning of a second functional
            gene and identification of the Rt6 gene products
  JOURNAL   Mol Immunol 33 (9), 807-817 (1996)
   PUBMED   8811076
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Koch-Nolte,F., Petersen,D., Balasubramanian,S., Haag,F., Kahlke,D.,
            Willer,T., Kastelein,R., Bazan,F. and Thiele,H.G.
  TITLE     Mouse T cell membrane proteins Rt6-1 and Rt6-2 are arginine/protein
            mono(ADPribosyl)transferases and share secondary structure motifs
            with ADP-ribosylating bacterial toxins
  JOURNAL   J Biol Chem 271 (13), 7686-7693 (1996)
   PUBMED   8631807
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Koch-Nolte,F., Klein,J., Hollmann,C., Kuhl,M., Haag,F.,
            Gaskins,H.R., Leiter,E. and Thiele,H.G.
  TITLE     Defects in the structure and expression of the genes for the T cell
            marker Rt6 in NZW and (NZB x NZW)F1 mice
  JOURNAL   Int Immunol 7 (5), 883-890 (1995)
   PUBMED   7547715
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Prochazka,M., Gaskins,H.R., Leiter,E.H., Koch-Nolte,F., Haag,F. and
            Thiele,H.G.
  TITLE     Chromosomal localization, DNA polymorphism, and expression of Rt-6,
            the mouse homologue of rat T-lymphocyte differentiation marker RT6
  JOURNAL   Immunogenetics 33 (2), 152-156 (1991)
   PUBMED   1671854
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF016465.1 and AC129609.3.
            
            On or before Oct 10, 2012 this sequence version replaced
            XP_003946451.1, NP_064299.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF016465.1, AF016463.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 54.61 cM"
     Protein         1..289
                     /product="T-cell ecto-ADP-ribosyltransferase 2 precursor"
                     /EC_number="2.4.2.31"
                     /EC_number="3.2.2.5"
                     /note="T-cell ecto-ADP-ribosyltransferase 2;
                     ADP-ribosyltransferase C2 and C3 toxin-like 2;
                     mono(ADP-ribosyl)transferase 2B; T-cell
                     mono(ADP-ribosyl)transferase 2; T-cell differentiation
                     marker Rt6 homolog 2; T-cell NAD(P)(+)--arginine
                     ADP-ribosyltransferase 2; NAD(+) glycohydrolase"
                     /calculated_mol_wt=30679
     sig_peptide     1..20
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O35975.2)"
                     /calculated_mol_wt=2463
     mat_peptide     21..260
                     /product="T-cell ecto-ADP-ribosyltransferase 2.
                     /id=PRO_0000019321"
                     /note="propagated from UniProtKB/Swiss-Prot (O35975.2)"
                     /calculated_mol_wt=27595
     Region          27..242
                     /region_name="ART"
                     /note="NAD:arginine ADP-ribosyltransferase; pfam01129"
                     /db_xref="CDD:279473"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35975.2)"
     Site            249
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35975.2)"
     CDS             1..289
                     /gene="Art2b"
                     /gene_synonym="Art; ART2.2; ARTC2; Ly92b; Rt-6; Rt6;
                     Rt6-2"
                     /coded_by="NM_019915.3:1..870"
                     /db_xref="CCDS:CCDS21512.1"
                     /db_xref="GeneID:11872"
                     /db_xref="MGI:MGI:107545"
ORIGIN      
        1 mtskifkffl twwltqqvtg lavpfmldma pnafddqyes cvedmekkap qllqedfnmn
       61 eelkleweka einwkeikns tsypagfhdf hgtalvaytg nlaidfnrav rdfkkspdnf
      121 hykafhyylt ravqllndqg cslvyrgtkv mfeytgkgsv rfgqfssssl tkrvalssnf
      181 fsnhgtlfii rtclgvnike fssfpreeev lipgyevyhk vtaqndngyn eifldsperk
      241 ksnfncfyng saqtvnidfs isgsrescvs lflvvllgll vqqltlael
//
LOCUS       NP_003995                226 aa            linear   PRI 27-APR-2025
DEFINITION  gap junction beta-2 protein [Homo sapiens].
ACCESSION   NP_003995
VERSION     NP_003995.2
DBSOURCE    REFSEQ: accession NM_004004.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Dou,M.M., Guan,J., Zhou,R., Li,J., Lan,L. and Wang,Q.J.
  TITLE     [Auditory characteristics and disease progression trends of
            patients with common recessive deafness genes GJB2 and SLC26A4]
  JOURNAL   Zhonghua Yi Xue Za Zhi 104 (38), 3600-3603 (2024)
   PUBMED   39414589
  REMARK    GeneRIF: [Auditory characteristics and disease progression trends
            of patients with common recessive deafness genes GJB2 and SLC26A4].
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Liu,H., Li,X., Zhang,C., Hao,X., Cao,Y., Wang,Y., Zhuang,H., Yu,N.,
            Huang,T., Liu,C., Cao,H., Lu,Z., Song,J., Liu,L., Wang,H., Li,Z.
            and Tang,W.
  TITLE     GJB2 Promotes HCC Progression by Activating Glycolysis Through
            Cytoplasmic Translocation and Generating a Suppressive Tumor
            Microenvironment Based on Single Cell RNA Sequencing
  JOURNAL   Adv Sci (Weinh) 11 (39), e2402115 (2024)
   PUBMED   39162005
  REMARK    GeneRIF: GJB2 Promotes HCC Progression by Activating Glycolysis
            Through Cytoplasmic Translocation and Generating a Suppressive
            Tumor Microenvironment Based on Single Cell RNA Sequencing.
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Brotherton,D.H., Nijjar,S., Savva,C.G., Dale,N. and Cameron,A.D.
  TITLE     Structures of wild-type and a constitutively closed mutant of
            connexin26 shed light on channel regulation by CO2
  JOURNAL   Elife 13, 93686 (2024)
   PUBMED   38829031
  REMARK    GeneRIF: Structures of wild-type and a constitutively closed mutant
            of connexin26 shed light on channel regulation by CO2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Baux,D., Faugere,V., Larrieu,L., Le Guedard-Mereuze,S., Hamroun,D.,
            Beroud,C., Malcolm,S., Claustres,M. and Roux,A.F.
  TITLE     UMD-USHbases: a comprehensive set of databases to record and
            analyse pathogenic mutations and unclassified variants in seven
            Usher syndrome causing genes
  JOURNAL   Hum Mutat 29 (8), E76-E87 (2008)
   PUBMED   18484607
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Smith,R.J.H. and Ranum,P.T.
  TITLE     Nonsyndromic Hearing Loss and Deafness, DFNA3 - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301708
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Smith,R.J.H., Azaiez,H. and Booth,K.
  TITLE     GJB2-Related Autosomal Recessive Nonsyndromic Hearing Loss
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301449
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Lee,S.W., Tomasetto,C., Paul,D., Keyomarsi,K. and Sager,R.
  TITLE     Transcriptional downregulation of gap-junction proteins blocks
            junctional communication in human mammary tumor cell lines
  JOURNAL   J Cell Biol 118 (5), 1213-1221 (1992)
   PUBMED   1324944
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Fishman,G.I., Moreno,A.P., Spray,D.C. and Leinwand,L.A.
  TITLE     Functional analysis of human cardiac gap junction channel mutants
  JOURNAL   Proc Natl Acad Sci U S A 88 (9), 3525-3529 (1991)
   PUBMED   1850831
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Verbov,J.
  TITLE     Palmoplantar keratoderma, deafness and atopy
  JOURNAL   Br J Dermatol 116 (6), 881-882 (1987)
   PUBMED   2956987
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA287424.1, BC017048.1,
            BC071703.1 and AA962716.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 17, 2004 this sequence version replaced NP_003995.1.
            
            Summary: This gene encodes a member of the gap junction protein
            family. The gap junctions were first characterized by electron
            microscopy as regionally specialized structures on plasma membranes
            of contacting adherent cells. These structures were shown to
            consist of cell-to-cell channels that facilitate the transfer of
            ions and small molecules between cells. The gap junction proteins,
            also known as connexins, purified from fractions of enriched gap
            junctions from different tissues differ. According to sequence
            similarities at the nucleotide and amino acid levels, the gap
            junction proteins are divided into two categories, alpha and beta.
            Mutations in this gene are responsible for as much as 50% of
            pre-lingual, recessive deafness. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279855.3065.1,
                                           SRR1660805.117664.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382848.5/ ENSP00000372299.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..226
                     /product="gap junction beta-2 protein"
                     /note="connexin 26; mutant gap junction beta 2 protein;
                     gap junction beta 2 proteinc; mutant gap junction protein
                     beta 2; gap junction protein, beta 2, 26kDa"
                     /calculated_mol_wt=26084
     Region          2..215
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            21..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29033.3)"
     Site            74..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29033.3)"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29033.3)"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29033.3)"
     CDS             1..226
                     /gene="GJB2"
                     /gene_synonym="BAPS; CX26; DFNA3; DFNA3A; DFNB1; DFNB1A;
                     HID; KID; NSRD1; PPK"
                     /coded_by="NM_004004.6:179..859"
                     /db_xref="CCDS:CCDS9290.1"
                     /db_xref="GeneID:2706"
                     /db_xref="HGNC:HGNC:4284"
                     /db_xref="MIM:121011"
ORIGIN      
        1 mdwgtlqtil ggvnkhstsi gkiwltvlfi frimilvvaa kevwgdeqad fvcntlqpgc
       61 knvcydhyfp ishirlwalq lifvstpall vamhvayrrh ekkrkfikge iksefkdiee
      121 iktqkvrieg slwwtytssi ffrvifeaaf myvfyvmydg fsmqrlvkcn awpcpntvdc
      181 fvsrptektv ftvfmiavsg icillnvtel cyllirycsg kskkpv
//
LOCUS       NP_065746               1221 aa            linear   PRI 27-APR-2025
DEFINITION  RNA exonuclease 1 homolog [Homo sapiens].
ACCESSION   NP_065746
VERSION     NP_065746.3
DBSOURCE    REFSEQ: accession NM_020695.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1221)
  AUTHORS   Bhatia,S., Pilquil,C., Roth-Albin,I. and Draper,J.S.
  TITLE     Demarcation of stable subpopulations within the pluripotent hESC
            compartment
  JOURNAL   PLoS One 8 (2), e57276 (2013)
   PUBMED   23437358
  REMARK    GeneRIF: Loss of REX1 expression demarcates stable, OCT4-positive
            lineage pluripotent human embryonic stem cells.
REFERENCE   2  (residues 1 to 1221)
  AUTHORS   Bhandari,D.R., Seo,K.W., Roh,K.H., Jung,J.W., Kang,S.K. and
            Kang,K.S.
  TITLE     REX-1 expression and p38 MAPK activation status can determine
            proliferation/differentiation fates in human mesenchymal stem cells
  JOURNAL   PLoS One 5 (5), e10493 (2010)
   PUBMED   20463961
  REMARK    GeneRIF: These findings showed that REX1 regulates the
            proliferation/differentiation of human mesenchymal stem cells
            through the suppression of p38 MAPK signaling via the direct
            suppression of MKK3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1221)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   4  (residues 1 to 1221)
  AUTHORS   Tamura,K., Miyata,K., Sugahara,K., Onishi,S., Shuin,T. and Aso,T.
  TITLE     Identification of EloA-BP1, a novel Elongin A binding protein with
            an exonuclease homology domain
  JOURNAL   Biochem Biophys Res Commun 309 (1), 189-195 (2003)
   PUBMED   12943681
  REMARK    GeneRIF: cloning and characterization of a novel human exonuclease
            domain-containing protein, Elongin A-binding protein 1; it is
            capable of binding not only the NH(2)-terminal approximately 120
            amino acid region of Elongin A, but also that of SII
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012615.4 and BC032244.1.
            
            On Apr 12, 2007 this sequence version replaced NP_065746.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB032964.1, BC032244.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000170168.9/ ENSP00000170168.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1221
                     /product="RNA exonuclease 1 homolog"
                     /note="REX1, RNA exonuclease 1 homolog; transcription
                     elongation factor B polypeptide 3-binding protein 1;
                     elongin-A-binding protein 1"
                     /calculated_mol_wt=131379
     Region          37..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Region          39..>477
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          116..598
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Site            191
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TT28; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TT28; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Region          <400..688
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Region          498..577
                     /region_name="Interaction with ELOA.
                     /evidence=ECO:0000269|PubMed:12943681"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TT28; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Region          619..692
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Region          <680..>884
                     /region_name="DUF1633"
                     /note="Protein of unknown function (DUF1633); pfam07794"
                     /db_xref="CDD:116408"
     Region          735..775
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Region          802..960
                     /region_name="EloA-BP1"
                     /note="ElonginA binding-protein 1; pfam15870"
                     /db_xref="CDD:464914"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G1.3)"
     Region          1061..1209
                     /region_name="REX1_like"
                     /note="DEDDh 3'-5' exonuclease domain of RNA exonuclease
                     1, -3 and similar eukaryotic proteins; cd06145"
                     /db_xref="CDD:99848"
     Site            order(1064..1067,1069,1142..1143,1145..1147,1196,1201)
                     /site_type="active"
                     /db_xref="CDD:99848"
     Site            order(1064..1067,1069,1142..1143,1145..1146,1196,1201)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99848"
     Site            order(1064,1066,1147,1196,1201)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99848"
     CDS             1..1221
                     /gene="REXO1"
                     /gene_synonym="EloA-BP1; ELOABP1; REX1; TCEB3BP1"
                     /coded_by="NM_020695.4:126..3791"
                     /db_xref="CCDS:CCDS32866.1"
                     /db_xref="GeneID:57455"
                     /db_xref="HGNC:HGNC:24616"
                     /db_xref="MIM:609614"
ORIGIN      
        1 mlrstgffra idcpywsgap ggpcrrpych frhrgargsg apgdggeapp aaglgydpyn
       61 pelpkppaqr engtlglgee prpdvlelel vnqaieavrs eveleqrryr ellettrehr
      121 saeapalapr gpnasptvgp dedafplafd yspgshglls pdagyqptpl aapaepgsky
      181 slasldrgqg rggggggale yvpkavsqpr rhsrpvpsgk yvvdnsrppt dleydplsny
      241 sarhlsrass rderaakrpr gsrgsepytp apkklcdpfg scdarfsdse deaatvpgne
      301 pttastpkar adpeikatgq ppskegleae ggglretket avqcdvgdlq pppakpaspa
      361 qvqssqdggc pkegkpkkkk tgappapsck dgaqgkdktk dkgrgrpvek pradkkgpqa
      421 ssprrkaerp egtkkkpssa tpvatsgkgr pdrparrpsp tsgdsrpaag rgpprplqlp
      481 drkstkapsg klverkarsl degasqdapk lkkralshad lfgdesedea agpgvpsvwp
      541 salpslssds dsdsdsslgf peaqgppkrl kaspppspap ssssssssst ssagadvdys
      601 alekevdfds dpmeeclrif nestsvkted rgrlarqppk eekseekgls glttlfpgqk
      661 rrishlskqg qevepprrgp avpparppta qevcylraqq aqrasasllq aparlaeksp
      721 svhisapgek rriahipnpr laaaptgakr tlaasgsqss ngpepggqql ktrtlsgmas
      781 kttttiipkr iahspslqsl kkpiipkefg gkvptvirqr ylnlfieecl kfctsnqeai
      841 ekalneekva ydrspskniy lnvavntlkk lrglapsavp glsktsgrrv vshevvlggr
      901 laaktsfsls rpssprvedl kgaalysrlr eylltqdqlk engypfphpe rpggaiifta
      961 eekrpkdssc rtccrcgtey lvsssgrcir deecyyhwgr lrrnrvaggw etqymccsaa
     1021 agsvgcqvak qhvqdgrker legfvktfek elsgdthpgi yaldcemsyt tygleltrvt
     1081 vvdtdvhvvy dtfvkpdnei vdyntrfsgv teadladtsv tlrdvqavll smfsadtili
     1141 ghslesdlla lkvihstvvd tsvlfphrlg lpykrslrnl madylrqiiq dnvdghssse
     1201 dagacmhlvi wkvredaktk r
//
LOCUS       NP_001356003             810 aa            linear   ROD 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 10 [Mus
            musculus].
ACCESSION   NP_001356003
VERSION     NP_001356003.1
DBSOURCE    REFSEQ: accession NM_001369074.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Thoren,L.A., Norgaard,G.A., Weischenfeldt,J., Waage,J.,
            Jakobsen,J.S., Damgaard,I., Bergstrom,F.C., Blom,A.M., Borup,R.,
            Bisgaard,H.C. and Porse,B.T.
  TITLE     UPF2 is a critical regulator of liver development, function and
            regeneration
  JOURNAL   PLoS One 5 (7), e11650 (2010)
   PUBMED   20657840
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Combes,A.N., Lesieur,E., Harley,V.R., Sinclair,A.H., Little,M.H.,
            Wilhelm,D. and Koopman,P.
  TITLE     Three-dimensional visualization of testis cord morphogenesis, a
            novel tubulogenic mechanism in development
  JOURNAL   Dev Dyn 238 (5), 1033-1041 (2009)
   PUBMED   19334288
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Hoffman,B.G., Zavaglia,B., Witzsche,J., Ruiz de Algara,T.,
            Beach,M., Hoodless,P.A., Jones,S.J., Marra,M.A. and Helgason,C.D.
  TITLE     Identification of transcripts with enriched expression in the
            developing and adult pancreas
  JOURNAL   Genome Biol 9 (6), R99 (2008)
   PUBMED   18554416
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   5  (residues 1 to 810)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Cobellis,G., Nicolaus,G., Iovino,M., Romito,A., Marra,E.,
            Barbarisi,M., Sardiello,M., Di Giorgio,F.P., Iovino,N., Zollo,M.,
            Ballabio,A. and Cortese,R.
  TITLE     Tagging genes with cassette-exchange sites
  JOURNAL   Nucleic Acids Res 33 (4), e44 (2005)
   PUBMED   15741177
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL627185.10 and AL627078.10.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.28183.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 67.34 cM"
     Protein         1..810
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 10"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein;
                     plenty-of-prolines-101"
                     /calculated_mol_wt=90780
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          511..>708
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..810
                     /gene="Srrm1"
                     /gene_synonym="POP101; Srm160"
                     /coded_by="NM_001369074.1:409..2841"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:51796"
                     /db_xref="MGI:MGI:1858303"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 lkkqdedkdk rdkeekessr ekrersrspr rtksrspspa pekkekspel pepsvrmkds
      121 svqeatstsd ilkapkpepv pepkepspek nskkekektr prsrsrsksr srtrsrspsh
      181 trprrrhrsr srsysprrrp sprrrpsprr rtpprrmppp prhrrsrspg rrrrrssasl
      241 sgssssssss rsrsppkkpp krtsspprkt rrlspsaspp rrrhrpsspa tpppktrhsp
      301 tpqqsnrtrk srvsvspgrt sgkvtkhkgt ekrespspap kprkvelses eedkgskmaa
      361 adsvqqrrqy rrqnqqsssd sgssstsede rpkrshvkng evgrrrrhsp srsaspsprk
      421 rqketsprmq mgkrwqspvt kssrrrrsps ppparrrrsp spappppppp ppprrrrspt
      481 ppprrrtpsp pprrrspspr rysppiqrry spspppkrrt aspppppkrr aspspppkrr
      541 vshspppkqr sptvtkrrsp slsskhrkgs spgrstrear spqpnkrhsp sprprapqts
      601 spppvrrgas aspqgrqsps pstrpirrvs rtpepkkikk aaspspqsvr rvsssrsvsg
      661 spepaakkpp appspvqsqs pstnwspavp akkaksptps lsparnsdqe gggkkkkkkk
      721 dkkhkkdkkh kkhkkhkkek avtiatpata apaavsaatt tsaqeepaaa peprketese
      781 aeddnlddle rhlrekalrs mrkaqvspqs
//
LOCUS       NP_653229                403 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 20 [Homo sapiens].
ACCESSION   NP_653229
VERSION     NP_653229.1
DBSOURCE    REFSEQ: accession NM_144628.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Abdel-Hamid,M.S., Abdel-Ghafar,S.F., Ismail,S.R., Desouky,L.M.,
            Issa,M.Y., Effat,L.K. and Zaki,M.S.
  TITLE     Micro and Martsolf syndromes in 34 new patients: Refining the
            phenotypic spectrum and further molecular insights
  JOURNAL   Clin Genet 98 (5), 445-456 (2020)
   PUBMED   32740904
  REMARK    GeneRIF: Micro and Martsolf syndromes in 34 new patients: Refining
            the phenotypic spectrum and further molecular insights.
            Review article
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Hozhabri,H., Talebi,M., Mehrjardi,M.Y.V., De Luca,A. and
            Dehghani,M.
  TITLE     Martsolf syndrome with novel mutation in the TBC1D20 gene in a
            family from Iran
  JOURNAL   Am J Med Genet A 182 (5), 957-961 (2020)
   PUBMED   32162791
  REMARK    GeneRIF: Martsolf syndrome with novel mutation in the TBC1D20 gene
            in a family from Iran.
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Liegel,R.P., Handley,M.T., Ronchetti,A., Brown,S., Langemeyer,L.,
            Linford,A., Chang,B., Morris-Rosendahl,D.J., Carpanini,S.,
            Posmyk,R., Harthill,V., Sheridan,E., Abdel-Salam,G.M., Terhal,P.A.,
            Faravelli,F., Accorsi,P., Giordano,L., Pinelli,L., Hartmann,B.,
            Ebert,A.D., Barr,F.A., Aligianis,I.A. and Sidjanin,D.J.
  TITLE     Loss-of-function mutations in TBC1D20 cause cataracts and male
            infertility in blind sterile mice and Warburg micro syndrome in
            humans
  JOURNAL   Am J Hum Genet 93 (6), 1001-1014 (2013)
   PUBMED   24239381
  REMARK    GeneRIF: Loss-of-function mutations in TBC1D20 cause cataracts and
            male infertility in blind sterile mice and Warburg micro syndrome
            in humans.
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Nevo-Yassaf,I., Yaffe,Y., Asher,M., Ravid,O., Eizenberg,S.,
            Henis,Y.I., Nahmias,Y., Hirschberg,K. and Sklan,E.H.
  TITLE     Role for TBC1D20 and Rab1 in hepatitis C virus replication via
            interaction with lipid droplet-bound nonstructural protein 5A
  JOURNAL   J Virol 86 (12), 6491-6502 (2012)
   PUBMED   22491470
  REMARK    GeneRIF: The NS5A interaction with TBC1D20 and Rab1 is essential
            for the viral life cycle.
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Sklan,E.H., Serrano,R.L., Einav,S., Pfeffer,S.R., Lambright,D.G.
            and Glenn,J.S.
  TITLE     TBC1D20 is a Rab1 GTPase-activating protein that mediates hepatitis
            C virus replication
  JOURNAL   J Biol Chem 282 (50), 36354-36361 (2007)
   PUBMED   17901050
  REMARK    GeneRIF: TBC1D20 was found to be the first known GAP for Rab1,
            which is implicated in the regulation of anterograde traffic
            between the endoplasmic reticulum and the Golgi complex
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Haas,A.K., Yoshimura,S., Stephens,D.J., Preisinger,C., Fuchs,E. and
            Barr,F.A.
  TITLE     Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs
            required to maintain a functional Golgi complex in human cells
  JOURNAL   J Cell Sci 120 (Pt 17), 2997-3010 (2007)
   PUBMED   17684057
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 403)
  AUTHORS   Handley,M. and Sheridan,E.
  TITLE     RAB18 Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29300443
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA238706.1, AK291648.1,
            BC047616.1, AL121747.41, AF116909.1 and BM984598.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that belongs to a family of
            GTPase activator proteins of Rab-like small GTPases. The encoded
            protein and its cognate GTPase, Rab1, bind the nonstructural
            protein 5A (NS5A) of the hepatitis C virus (HCV) to mediate viral
            replication. Depletion of this protein inhibits replication of the
            virus and HCV infection. Mutations in this gene are associated with
            Warburg micro syndrome 4. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127062.1, SRR14038193.847479.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354200.5/ ENSP00000346139.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..403
                     /product="TBC1 domain family member 20"
                     /calculated_mol_wt=45724
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BZ9.1)"
     Site            105
                     /site_type="other"
                     /note="Arginine finger.
                     /evidence=ECO:0000269|PubMed:23236136; propagated from
                     UniProtKB/Swiss-Prot (Q96BZ9.1)"
     Region          <136..266
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; pfam00566"
                     /db_xref="CDD:459855"
     Site            144
                     /site_type="other"
                     /note="Glutamine finger.
                     /evidence=ECO:0000269|PubMed:23236136; propagated from
                     UniProtKB/Swiss-Prot (Q96BZ9.1)"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BZ9.1)"
     Site            367..387
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BZ9.1)"
     CDS             1..403
                     /gene="TBC1D20"
                     /gene_synonym="C20orf140; WARBM4"
                     /coded_by="NM_144628.4:129..1340"
                     /db_xref="CCDS:CCDS13002.1"
                     /db_xref="GeneID:128637"
                     /db_xref="HGNC:HGNC:16133"
                     /db_xref="MIM:611663"
ORIGIN      
        1 malrsaqgdg ptsghwdgga ekadfnakrk kkvaeihqal nsdptdvaal rrmaiseggl
       61 ltdeirrkvw pkllnvnand pppisgknlr qmskdyqqvl ldvrrslrrf ppgmpeeqre
      121 glqeelidii llilernpql hyyqgyhdiv vtfllvvger latslvekls thhlrdfmdp
      181 tmdntkhiln ylmpiidqvn pelhdfmqsa evgtifalsw litwfghvls dfrhvvrlyd
      241 fflachplmp iyfaavivly reqevldcdc dmasvhhlls qipqdlpyet lisragdlfv
      301 qfppselare aaaqqqaert aastfkdfel asaqqrpdmv lrqrfrgllr pedrtkdvlt
      361 kprtnrfvkl avmgltvalg aaalavvksa lewapkfqlq lfp
//
LOCUS       NP_055610               1214 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger E-box-binding homeobox 2 isoform 1 [Homo sapiens].
ACCESSION   NP_055610 XP_001723593 XP_001724051 XP_001724969
VERSION     NP_055610.1
DBSOURCE    REFSEQ: accession NM_014795.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1214)
  AUTHORS   Cai,Y., Zhou,J., Xu,A., Huang,J., Zhang,H., Xie,G., Zhong,K.,
            Wu,Y., Ye,P., Wang,H. and Niu,H.
  TITLE     N6-methyladenosine triggers renal fibrosis via enhancing
            translation and stability of ZEB2 mRNA
  JOURNAL   J Biol Chem 300 (9), 107598 (2024)
   PUBMED   39059495
  REMARK    GeneRIF: N6-methyladenosine triggers renal fibrosis via enhancing
            translation and stability of ZEB2 mRNA.
REFERENCE   2  (residues 1 to 1214)
  AUTHORS   Feng,Y., Zhou,C., Zhao,F., Ma,T., Xiao,Y., Peng,K. and Xia,R.
  TITLE     ZEB2 alleviates Hirschsprung's-associated enterocolitis by
            promoting the proliferation and differentiation of enteric neural
            precursor cells via the Notch-1/Jagged-2 pathway
  JOURNAL   Gene 912, 148365 (2024)
   PUBMED   38485033
  REMARK    GeneRIF: ZEB2 alleviates Hirschsprung's-associated enterocolitis by
            promoting the proliferation and differentiation of enteric neural
            precursor cells via the Notch-1/Jagged-2 pathway.
REFERENCE   3  (residues 1 to 1214)
  AUTHORS   Zhang,W., Xiao,P., Liu,B. and Zhang,Y.
  TITLE     Circ-10720 as a ceRNA adsorbs microRNA-1238 and modulates ZEB2 to
            boost NSCLC development by activating EMT
  JOURNAL   Eur J Med Res 29 (1), 226 (2024)
   PUBMED   38610009
  REMARK    GeneRIF: Circ-10720 as a ceRNA adsorbs microRNA-1238 and modulates
            ZEB2 to boost NSCLC development by activating EMT.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1214)
  AUTHORS   Knox,J.J. and Cancro,M.P.
  TITLE     ABCs begin with ZEB2
  JOURNAL   Immunol Cell Biol 102 (4), 229-231 (2024)
   PUBMED   38525813
  REMARK    GeneRIF: ABCs begin with ZEB2.
REFERENCE   5  (residues 1 to 1214)
  AUTHORS   Comijn,J., Berx,G., Vermassen,P., Verschueren,K., van Grunsven,L.,
            Bruyneel,E., Mareel,M., Huylebroeck,D. and van Roy,F.
  TITLE     The two-handed E box binding zinc finger protein SIP1 downregulates
            E-cadherin and induces invasion
  JOURNAL   Mol Cell 7 (6), 1267-1278 (2001)
   PUBMED   11430829
  REMARK    GeneRIF: Conditional expression of SIP1 in E-cadherin-positive
            cells abrogates E-cadherin-mediated intercellular adhesion and
            induces invasion. SIP1 therefore appears to be a promoter of
            invasion in malignant epithelial tumors.
REFERENCE   6  (residues 1 to 1214)
  AUTHORS   Wakamatsu,N., Yamada,Y., Yamada,K., Ono,T., Nomura,N.,
            Taniguchi,H., Kitoh,H., Mutoh,N., Yamanaka,T., Mushiake,K.,
            Kato,K., Sonta,S. and Nagaya,M.
  TITLE     Mutations in SIP1, encoding Smad interacting protein-1, cause a
            form of Hirschsprung disease
  JOURNAL   Nat Genet 27 (4), 369-370 (2001)
   PUBMED   11279515
REFERENCE   7  (residues 1 to 1214)
  AUTHORS   Verschueren,K., Remacle,J.E., Collart,C., Kraft,H., Baker,B.S.,
            Tylzanowski,P., Nelles,L., Wuytens,G., Su,M.T., Bodmer,R.,
            Smith,J.C. and Huylebroeck,D.
  TITLE     SIP1, a novel zinc finger/homeodomain repressor, interacts with
            Smad proteins and binds to 5'-CACCT sequences in candidate target
            genes
  JOURNAL   J Biol Chem 274 (29), 20489-20498 (1999)
   PUBMED   10400677
REFERENCE   8  (residues 1 to 1214)
  AUTHORS   Ueki,N., Oda,T., Kondo,M., Yano,K., Noguchi,T. and Muramatsu,M.
  TITLE     Selection system for genes encoding nuclear-targeted proteins
  JOURNAL   Nat Biotechnol 16 (13), 1338-1342 (1998)
   PUBMED   9853615
REFERENCE   9  (residues 1 to 1214)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   10 (residues 1 to 1214)
  AUTHORS   Adam,M.P., Conta,J. and Bean,L.J.H.
  TITLE     Classic Mowat-Wilson Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301585
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA305985.1, AB056507.1,
            AC010130.12 and AI341193.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 2, 2009 this sequence version replaced
            XP_001724969.1, XP_001723593.1, XP_001724051.1.
            
            Summary: The protein encoded by this gene is a member of the Zfh1
            family of 2-handed zinc finger/homeodomain proteins. It is located
            in the nucleus and functions as a DNA-binding transcriptional
            repressor that interacts with activated SMADs. Mutations in this
            gene are associated with Hirschsprung disease/Mowat-Wilson
            syndrome. Alternatively spliced transcript variants have been found
            for this gene.[provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB011141.1, SRR1660805.72925.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000627532.3/ ENSP00000487174.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q22.3"
     Protein         1..1214
                     /product="zinc finger E-box-binding homeobox 2 isoform 1"
                     /note="zinc finger homeobox 1b; Smad-interacting protein
                     1; SMAD interacting protein 1"
                     /calculated_mol_wt=136317
     Region          1..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60315.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Region          209..263
                     /region_name="zf-Di19"
                     /note="Drought induced 19 protein (Di19), zinc-binding;
                     pfam05605"
                     /db_xref="CDD:428539"
     Region          213..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          241..263
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          243..263
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..304
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          284..304
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          296..319
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0G7; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0G7; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Site            377
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Region          437..487
                     /region_name="SMAD-MH2 binding domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O60315.1)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Region          702..740
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60315.1)"
     Site            731
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0G7; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Region          771..810
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60315.1)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0G7; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Site            782
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Site            784
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Region          832..857
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60315.1)"
     Region          1001..1021
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1006,1008,1010,1012..1013,1016..1017,1020,1034,1036,
                     1040..1041,1044..1045,1048,1062,1064,1066,1068..1069,
                     1072..1073)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1013..1038
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1029..1049
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1041..1066
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1057..1074
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1117..1214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60315.1)"
     Site            1122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Site            1124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0G7; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     Site            1203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0G7; propagated from
                     UniProtKB/Swiss-Prot (O60315.1)"
     CDS             1..1214
                     /gene="ZEB2"
                     /gene_synonym="HSPC082; SIP-1; SIP1; SMADIP1; ZFHX1B"
                     /coded_by="NM_014795.4:251..3895"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2186.1"
                     /db_xref="GeneID:9839"
                     /db_xref="HGNC:HGNC:14881"
                     /db_xref="MIM:605802"
ORIGIN      
        1 mkqpimadgp rckrrkqanp rrknvvnydn vvdtgsetde edklhiaedd gianpldqet
       61 spasvpnhes sphvsqallp reeeedeire ggvehpwhnn eilqasvdgp eemkedydtm
      121 gpeatiqtai nngtvknanc tsdfeeyfak rkleerdgha vsieeylqrs dtaiiypeap
      181 eelsrlgtpe angqeendlp pgtpdafaql ltcpycdrgy krltslkehi kyrhekneen
      241 fscplcsytf ayrtqlerhm vthkpgtdqh qmltqgagnr kfkctecgka fkykhhlkeh
      301 lrihsgekpy ecpnckkrfs hsgsysshis skkciglisv ngrmrnnikt gsspnsvsss
      361 ptnsaitqlr nklengkpls mseqtgllki ktepldfndy kvlmathgfs gtspfmnggl
      421 gatsplgvhp saqspmqhlg vgmeapllgf ptmnsnlsev qkvlqivdnt vsrqkmdcka
      481 eeisklkgyh mkdpcsqpee qgvtspnipp vglpvvshng atksiidytl ekvneakacl
      541 qslttdsrrq isnikkeklr tlidlvtddk mienhnistp fscqfckesf pgpiplhqhe
      601 rylckmneei kavlqpheni vpnkagvfvd nkalllssvl sekgmtspin pykdhmsvlk
      661 ayyamnmepn sdellkisia vglpqefvke wfeqrkvyqy snsrspsler sskplapnsn
      721 pptkdsllpr spvkpmdsit spsiaelhns vtncdpplrl tkpshftnik pvekldhsrs
      781 ntpsplnlss tssknshsss ytpnsfssee lqaepldlsl pkqmkepksi iatknktkas
      841 sisldhnsvs sssensdepl nltfikkefs nsnnldnkst npvfsmnpfs akplytalpp
      901 qsafppatfm ppvqtsipgl rpypgldqms flphmaytyp tgaatfadmq qrrkyqrkqg
      961 fqgelldgaq dymsglddmt dsdsclsrkk ikktesgmya cdlcdktfqk sssllrhkye
     1021 htgkrphqcq ickkafkhkh hliehsrlhs gekpyqcdkc gkrfshsgsy sqhmnhrysy
     1081 ckreaeerea aerearekgh leptellmnr aylqsitpqg ysdseeresm prdgesekeh
     1141 ekegedgygk lgrqdgdeef eeeeeesenk smdtdpetir deeetgdhsm ddssedgkme
     1201 tksdheednm edgm
//
LOCUS       NP_001036111             953 aa            linear   PRI 27-APR-2025
DEFINITION  trafficking kinesin-binding protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001036111
VERSION     NP_001036111.1
DBSOURCE    REFSEQ: accession NM_001042646.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Baltrusaitis,E.E., Ravitch,E.E., Fenton,A.R., Perez,T.A.,
            Holzbaur,E.L.F. and Dominguez,R.
  TITLE     Interaction between the mitochondrial adaptor MIRO and the motor
            adaptor TRAK
  JOURNAL   J Biol Chem 299 (12), 105441 (2023)
   PUBMED   37949220
  REMARK    GeneRIF: Interaction between the mitochondrial adaptor MIRO and the
            motor adaptor TRAK.
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Benhamida,J.K., Harmsen,H.J., Ma,D., William,C.M., Li,B.K.,
            Villafania,L., Sukhadia,P., Mullaney,K.A., Dewan,M.C., Vakiani,E.,
            Karajannis,M.A., Snuderl,M., Zagzag,D., Ladanyi,M., Rosenblum,M.K.
            and Bale,T.A.
  TITLE     Recurrent TRAK1::RAF1 Fusions in pediatric low-grade gliomas
  JOURNAL   Brain Pathol 33 (5), e13185 (2023)
   PUBMED   37399073
  REMARK    GeneRIF: Recurrent TRAK1::RAF1 Fusions in pediatric low-grade
            gliomas.
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 953)
  AUTHORS   Wu,H., Liu,Y., Li,H., Du,C., Li,K., Dong,S., Meng,Q. and Zhang,H.
  TITLE     TRAK1-Mediated Abnormality of Mitochondrial Fission Increases
            Seizure Susceptibility in Temporal Lobe Epilepsy
  JOURNAL   Mol Neurobiol 58 (3), 1237-1247 (2021)
   PUBMED   33119838
  REMARK    GeneRIF: TRAK1-Mediated Abnormality of Mitochondrial Fission
            Increases Seizure Susceptibility in Temporal Lobe Epilepsy.
REFERENCE   5  (residues 1 to 953)
  AUTHORS   Henrichs,V., Grycova,L., Barinka,C., Nahacka,Z., Neuzil,J.,
            Diez,S., Rohlena,J., Braun,M. and Lansky,Z.
  TITLE     Mitochondria-adaptor TRAK1 promotes kinesin-1 driven transport in
            crowded environments
  JOURNAL   Nat Commun 11 (1), 3123 (2020)
   PUBMED   32561740
  REMARK    GeneRIF: Mitochondria-adaptor TRAK1 promotes kinesin-1 driven
            transport in crowded environments.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 953)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
REFERENCE   7  (residues 1 to 953)
  AUTHORS   Brickley,K., Smith,M.J., Beck,M. and Stephenson,F.A.
  TITLE     GRIF-1 and OIP106, members of a novel gene family of coiled-coil
            domain proteins: association in vivo and in vitro with kinesin
  JOURNAL   J Biol Chem 280 (15), 14723-14732 (2005)
   PUBMED   15644324
  REMARK    GeneRIF: GRIF-1 and OIP106 have roles in protein and/or organelle
            transport in excitable cells in a manner analogous to glutamate
            receptor-interacting-protein 1
REFERENCE   8  (residues 1 to 953)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   9  (residues 1 to 953)
  AUTHORS   Iyer,S.P. and Hart,G.W.
  TITLE     Roles of the tetratricopeptide repeat domain in O-GlcNAc
            transferase targeting and protein substrate specificity
  JOURNAL   J Biol Chem 278 (27), 24608-24616 (2003)
   PUBMED   12724313
REFERENCE   10 (residues 1 to 953)
  AUTHORS   Iyer,S.P., Akimoto,Y. and Hart,G.W.
  TITLE     Identification and cloning of a novel family of coiled-coil domain
            proteins that interact with O-GlcNAc transferase
  JOURNAL   J Biol Chem 278 (7), 5399-5409 (2003)
   PUBMED   12435728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB028965.1, AC018358.20 and H05058.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB028965.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327628.10/ ENSP00000328998.5
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.1"
     Protein         1..953
                     /product="trafficking kinesin-binding protein 1 isoform 1"
                     /note="OGT(O-Glc-NAc transferase)-interacting protein 106
                     KDa; 106 kDa O-GlcNAc transferase-interacting protein;
                     milton homolog 1; O-linked N-acetylglucosamine transferase
                     interacting protein 106; protein Milton; trafficking
                     protein, kinesin binding 1"
                     /calculated_mol_wt=105909
     Region          48..353
                     /region_name="HAP1_N"
                     /note="HAP1 N-terminal conserved region; pfam04849"
                     /db_xref="CDD:461455"
     Region          359..509
                     /region_name="Interaction with HGS.
                     /evidence=ECO:0000269|PubMed:18675823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          414..583
                     /region_name="Milton"
                     /note="Kinesin associated protein; pfam12448"
                     /db_xref="CDD:463588"
     Site            447
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:24995978; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          472..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PD31; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          658..672
                     /region_name="Interaction with OGT.
                     /evidence=ECO:0000269|PubMed:24995978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            680
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:24995978; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            719
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:24995978; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PD31; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          777..796
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            919
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            935
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:24995978; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     CDS             1..953
                     /gene="TRAK1"
                     /gene_synonym="DEE68; EIEE68; MILT1; OIP106"
                     /coded_by="NM_001042646.3:114..2975"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43072.1"
                     /db_xref="GeneID:22906"
                     /db_xref="HGNC:HGNC:29947"
                     /db_xref="MIM:608112"
ORIGIN      
        1 malvfqfgqp vraqplpglc hgklirtnac dvcnstdlpe veiislleeq lphyklradt
       61 iygydhddwl htplispdan idltteqiee tlkyfllcae rvgqmtktyn didavtrlle
      121 ekerdlelaa rigqsllkkn ktlternell eeqvehiree vsqlrhelsm kdellqfyts
      181 aaeesepesv cstplkrnes sssvqnyfhl dslqkklkdl eeenvvlrse asqlktetit
      241 yeekeqqlvn dcvkelrdan vqiasiseel akktedaarq qeeithllsq ivdlqkkaka
      301 caveneelvq hlgaakdaqr qltaelrele dkyaecmeml heaqeelknl rnktmpntts
      361 rryhslglfp mdslaaeieg tmrkelqlee aespdithqk rvfetvrnin qvvkqrsltp
      421 spmnipgsnq ssamnsllss cvstprssfy gsdignvvld nktnsiilet eaadlgnder
      481 skkpgtpgtp gshdletalr rlslrrenyl serrffeeeq erklqelaek gelrsgsltp
      541 tesimslgth srfseftgfs gmsfssrsyl peklqivkpl egsatlhhwq qlaqphlggi
      601 ldprpgvvtk gfrtldvdld evyclndfee ddtgdhislp rlatstpvqh petsahhpgk
      661 cmsqtnstft fttcrilhps deltrvtpsl nsaptpacgs tshlkstpva tpctprrlsl
      721 aesftntres tttmstslgl vwllkergis aavydpqswd ragrgsllhs ytpkmavips
      781 tppnspmqtp tssppsfefk ctsppydnfl askpassilr evreknvrss esqtdvsvsn
      841 lnlvdkvrrf gvakvvnsgr ahvptlteeq gpllcgppgp apalvprglv peglplrcpt
      901 vtsaigglql nsgirrnrsf ptmvgssmqm kapvtltsgi lmgaklskqt slr
//
LOCUS       NP_115667                828 aa            linear   PRI 27-APR-2025
DEFINITION  SH3-containing GRB2-like protein 3-interacting protein 1 isoform 1
            [Homo sapiens].
ACCESSION   NP_115667
VERSION     NP_115667.2
DBSOURCE    REFSEQ: accession NM_032291.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Xie,G.F., Xu,Y.X., Xu,F., Sun,L.Y., Ye,Z.L., Ma,J.J., Wang,H.Y. and
            Shao,J.Y.
  TITLE     Plasma SGIP1 methylation in diagnosis and prognosis prediction in
            hepatocellular carcinoma
  JOURNAL   Neoplasma 68 (1), 62-70 (2021)
   PUBMED   33118832
  REMARK    GeneRIF: Plasma SGIP1 methylation in diagnosis and prognosis
            prediction in hepatocellular carcinoma.
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Zhang,Y., Feng,Y., Xin,Y. and Liu,X.
  TITLE     SGIP1 dimerizes via intermolecular disulfide bond in muHD domain
            during cellular endocytosis
  JOURNAL   Biochem Biophys Res Commun 505 (1), 99-105 (2018)
   PUBMED   30236986
  REMARK    GeneRIF: Data indicate that cysteine C632 residue is important for
            the function of SH3 domain GRB2 like endophilin interacting protein
            1 (SGIP1) during cellular endocytosis.
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Petko,J., Tranchina,T., Patel,G., Levenson,R. and Justice-Bitner,S.
  TITLE     Identifying novel members of the Wntless interactome through
            genetic and candidate gene approaches
  JOURNAL   Brain Res Bull 138, 96-105 (2018)
   PUBMED   28734904
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Chwedorowicz,R., Raszewski,G., Kapka-Skrzypczak,L., Sawicki,K. and
            Studzinski,T.
  TITLE     Event-related potentials (ERP) and SGIP1 gene polymorphisms in
            alcoholics: relation to family history of alcoholism and drug usage
  JOURNAL   Ann Agric Environ Med 23 (4), 618-624 (2016)
   PUBMED   28030933
  REMARK    GeneRIF: The present study demonstrated a possible association of
            target P300 evoked theta and of alcohol dependence with SNPs from
            the gene SGIP1 in the region of rs10889635, but further studies are
            required.
REFERENCE   5  (residues 1 to 828)
  AUTHORS   Shimada,A., Yamaguchi,A. and Kohda,D.
  TITLE     Structural basis for the recognition of two consecutive mutually
            interacting DPF motifs by the SGIP1 mu homology domain
  JOURNAL   Sci Rep 6, 19565 (2016)
   PUBMED   26822536
  REMARK    GeneRIF: crystal structures of the SGIP1 mu homology domains in
            complex with peptides containing two DPF motifs, are reported.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 828)
  AUTHORS   Luke,M.M., O'Meara,E.S., Rowland,C.M., Shiffman,D., Bare,L.A.,
            Arellano,A.R., Longstreth,W.T. Jr., Lumley,T., Rice,K., Tracy,R.P.,
            Devlin,J.J. and Psaty,B.M.
  TITLE     Gene variants associated with ischemic stroke: the cardiovascular
            health study
  JOURNAL   Stroke 40 (2), 363-368 (2009)
   PUBMED   19023099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 828)
  AUTHORS   Shiffman,D., O'Meara,E.S., Bare,L.A., Rowland,C.M., Louie,J.Z.,
            Arellano,A.R., Lumley,T., Rice,K., Iakoubova,O., Luke,M.M.,
            Young,B.A., Malloy,M.J., Kane,J.P., Ellis,S.G., Tracy,R.P.,
            Devlin,J.J. and Psaty,B.M.
  TITLE     Association of gene variants with incident myocardial infarction in
            the Cardiovascular Health Study
  JOURNAL   Arterioscler Thromb Vasc Biol 28 (1), 173-179 (2008)
   PUBMED   17975119
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 828)
  AUTHORS   Uezu,A., Horiuchi,A., Kanda,K., Kikuchi,N., Umeda,K., Tsujita,K.,
            Suetsugu,S., Araki,N., Yamamoto,H., Takenawa,T. and Nakanishi,H.
  TITLE     SGIP1alpha is an endocytic protein that directly interacts with
            phospholipids and Eps15
  JOURNAL   J Biol Chem 282 (36), 26481-26489 (2007)
   PUBMED   17626015
  REMARK    GeneRIF: SGIP1alpha plays an essential role in clathrin-mediated
            endocytosis by interacting with phospholipids and Eps15.
REFERENCE   9  (residues 1 to 828)
  AUTHORS   Trevaskis,J., Walder,K., Foletta,V., Kerr-Bayles,L., McMillan,J.,
            Cooper,A., Lee,S., Bolton,K., Prior,M., Fahey,R., Whitecross,K.,
            Morton,G.J., Schwartz,M.W. and Collier,G.R.
  TITLE     Src homology 3-domain growth factor receptor-bound 2-like
            (endophilin) interacting protein 1, a novel neuronal protein that
            regulates energy balance
  JOURNAL   Endocrinology 146 (9), 3757-3764 (2005)
   PUBMED   15919751
REFERENCE   10 (residues 1 to 828)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA491011.1, AL136561.1, BC040516.1, AL354978.20 and AW205180.1.
            
            On Oct 17, 2006 this sequence version replaced NP_115667.1.
            
            Summary: SGIP1 functions as an endocytic protein that affects
            signaling by receptors in neuronal systems involved in energy
            homeostasis via its interaction with endophilins (see SH3GL3; MIM
            603362) (Trevaskis et al., 2005 [PubMed 15919751] and Uezu et al.,
            2007 [PubMed 17626015]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.9408.1, AL136561.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2146411
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371037.9/ ENSP00000360076.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..828
                     /product="SH3-containing GRB2-like protein 3-interacting
                     protein 1 isoform 1"
                     /note="SH3-containing GRB2-like protein 3-interacting
                     protein 1; SH3 domain GRB2 like endophilin interacting
                     protein 1; endophilin-3-interacting protein"
                     /calculated_mol_wt=88978
     Region          1..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P0DJJ3; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P0DJJ3; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P0DJJ3; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Region          143..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P0DJJ3; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Region          223..278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P0DJJ3; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Region          313..524
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37; propagated from
                     UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Region          561..827
                     /region_name="SGIP1_MHD"
                     /note="mu-homology domain (MHD) of Scr homology 3
                     (SH3)-domain growth factor receptor-bound 2 (GRB2)-like
                     (endophilin) interacting protein 1 (also known as
                     endophilin-3-interacting protein, SGIP1) and similar
                     proteins; cd09266"
                     /db_xref="CDD:271172"
     Region          561..567
                     /region_name="Interaction with DPF motifs-containing
                     proteins. /evidence=ECO:0000269|PubMed:26822536,
                     ECO:0007744|PDB:5AWU"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Region          593..595
                     /region_name="Interaction with DPF motifs-containing
                     proteins. /evidence=ECO:0000269|PubMed:26822536,
                     ECO:0007744|PDB:5AWU"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Region          649..828
                     /region_name="Necessary and sufficient to mediate
                     interaction with CANX.
                     /evidence=ECO:0000250|UniProtKB:Q8VD37"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Region          667..670
                     /region_name="Interaction with DPF motifs-containing
                     proteins. /evidence=ECO:0000269|PubMed:26822536,
                     ECO:0007744|PDB:5AWT, ECO:0007744|PDB:5AWU"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQI5.2)"
     Region          813..818
                     /region_name="Interaction with DPF motifs-containing
                     proteins. /evidence=ECO:0000269|PubMed:26822536,
                     ECO:0007744|PDB:5AWT, ECO:0007744|PDB:5AWU"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQI5.2)"
     CDS             1..828
                     /gene="SGIP1"
                     /coded_by="NM_032291.4:207..2693"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30744.1"
                     /db_xref="GeneID:84251"
                     /db_xref="HGNC:HGNC:25412"
                     /db_xref="MIM:611540"
ORIGIN      
        1 mmeglkkrtr kafgirkkek dtdstgspdr dgiqpsphep pynskaecar eggkkvskks
       61 ngapngfyae idwerynspe ldeegysirp eepgstkgkh fyssseseee eeshkkfnik
      121 ikplqskdil knaatvdelk asignialsp spvrksprrs pgaikrnlss eevarprrst
      181 ptpeliskkp pddttalapl fgpplesafd eqktevlldq peiwgsgqpi npsmespklt
      241 rpfptgtppp lppknvpatp prtgspltig pgndqsatev kieklpsind ldsifgpvls
      301 pksvavnaee kwvhfsdtsp ehvtpeltpr ekvvsppatp dnpadspapg plgppgptgp
      361 pgppgpprnv lsplnleevq kkvaeqtfik ddyletissp kdfglgqrat ppppppptyr
      421 tvvsspgpgs gpgpgttsga ssparpatpl vpcrsttppp ppprppsrpk lppgkpgvgd
      481 vsrpfsppih ssspppiapl araestssis stnslsaatt ptveneqpsl vwfdrgkfyl
      541 tfegssrgps pltmgaqdtl pvaaaftetv nayfkgadps kcivkitgem vlsfpagitr
      601 hfannpspaa ltfrvinfsr lehvlpnpql lccdntqnda ntkefwvnmp nlmthlkkvs
      661 eqkpqatyyn vdmlkyqvsa qgiqstplnl avnwrcepss tdlridykyn tdamttaval
      721 nnvqflvpid ggvtklqavl ppavwnaeqq rilwkipdis qksenggvgs llarfqlseg
      781 pskpsplvvq ftsegstlsg cdielvgagy rfslikkrfa agkyladn
//
LOCUS       NP_005779                531 aa            linear   PRI 27-APR-2025
DEFINITION  protein arginine N-methyltransferase 3 isoform 1 [Homo sapiens].
ACCESSION   NP_005779 XP_058460
VERSION     NP_005779.1
DBSOURCE    REFSEQ: accession NM_005788.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Gupta,S., Verma,M., Kadumuri,R.V., Chutani,N., Khan,M.I.K.,
            Chavali,S. and Dhayalan,A.
  TITLE     The uncharacterized protein ZNF200 interacts with PRMT3 and aids
            its stability and nuclear translocation
  JOURNAL   Biochem J 481 (23), 1723-1740 (2024)
   PUBMED   39513743
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Wang,Y., Wang,C., Guan,X., Ma,Y., Zhang,S., Li,F., Yin,Y., Sun,Z.,
            Chen,X. and Yin,H.
  TITLE     PRMT3-Mediated Arginine Methylation of METTL14 Promotes Malignant
            Progression and Treatment Resistance in Endometrial Carcinoma
  JOURNAL   Adv Sci (Weinh) 10 (36), e2303812 (2023)
   PUBMED   37973560
  REMARK    GeneRIF: PRMT3-Mediated Arginine Methylation of METTL14 Promotes
            Malignant Progression and Treatment Resistance in Endometrial
            Carcinoma.
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Zhi,R., Wu,K., Zhang,J., Liu,H., Niu,C., Li,S. and Fu,L.
  TITLE     PRMT3 regulates the progression of invasive micropapillary
            carcinoma of the breast
  JOURNAL   Cancer Sci 114 (5), 1912-1928 (2023)
   PUBMED   36637351
  REMARK    GeneRIF: PRMT3 regulates the progression of invasive micropapillary
            carcinoma of the breast.
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Shi,Y., Niu,Y., Yuan,Y., Li,K., Zhong,C., Qiu,Z., Li,K., Lin,Z.,
            Yang,Z., Zuo,D., Qiu,J., He,W., Wang,C., Liao,Y., Wang,G., Yuan,Y.
            and Li,B.
  TITLE     PRMT3-mediated arginine methylation of IGF2BP1 promotes oxaliplatin
            resistance in liver cancer
  JOURNAL   Nat Commun 14 (1), 1932 (2023)
   PUBMED   37024475
  REMARK    GeneRIF: PRMT3-mediated arginine methylation of IGF2BP1 promotes
            oxaliplatin resistance in liver cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Hsu,S.H. and Hung,W.C.
  TITLE     Protein arginine methyltransferase 3: A crucial regulator in
            metabolic reprogramming and gene expression in cancers
  JOURNAL   Cancer Lett 554, 216008 (2023)
   PUBMED   36400311
  REMARK    GeneRIF: Protein arginine methyltransferase 3: A crucial regulator
            in metabolic reprogramming and gene expression in cancers.
            Review article
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Swiercz,R., Person,M.D. and Bedford,M.T.
  TITLE     Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein
            arginine methyltransferase 3)
  JOURNAL   Biochem J 386 (Pt 1), 85-91 (2005)
   PUBMED   15473865
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Singh,V., Miranda,T.B., Jiang,W., Frankel,A., Roemer,M.E.,
            Robb,V.A., Gutmann,D.H., Herschman,H.R., Clarke,S. and Newsham,I.F.
  TITLE     DAL-1/4.1B tumor suppressor interacts with protein arginine
            N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate
            substrates in vitro and in vivo
  JOURNAL   Oncogene 23 (47), 7761-7771 (2004)
   PUBMED   15334060
  REMARK    GeneRIF: DAL-1/4.1B protein significantly inhibits PRMT3
            methylation of cellular substrates, which may affect mechanism
            through which DAL-1/4.1B affects tumor cell growth.
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Bachand,F. and Silver,P.A.
  TITLE     PRMT3 is a ribosomal protein methyltransferase that affects the
            cellular levels of ribosomal subunits
  JOURNAL   EMBO J 23 (13), 2641-2650 (2004)
   PUBMED   15175657
  REMARK    GeneRIF: PRMT3 is a ribosomal protein methyltransferase that
            affects the cellular level of ribosomal subunits.
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Smith,J.J., Rucknagel,K.P., Schierhorn,A., Tang,J., Nemeth,A.,
            Linder,M., Herschman,H.R. and Wahle,E.
  TITLE     Unusual sites of arginine methylation in Poly(A)-binding protein II
            and in vitro methylation by protein arginine methyltransferases
            PRMT1 and PRMT3
  JOURNAL   J Biol Chem 274 (19), 13229-13234 (1999)
   PUBMED   10224081
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Tang,J., Gary,J.D., Clarke,S. and Herschman,H.R.
  TITLE     PRMT 3, a type I protein arginine N-methyltransferase that differs
            from PRMT1 in its oligomerization, subcellular localization,
            substrate specificity, and regulation
  JOURNAL   J Biol Chem 273 (27), 16935-16945 (1998)
   PUBMED   9642256
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025972.6, AC108005.8, KC877396.1 and KF459543.1.
            
            On Mar 22, 2004 this sequence version replaced XP_058460.2.
            
            Summary: This gene belongs to the protein arginine
            methyltransferase (PRMT) family. The encoded enzyme catalyzes the
            methylation of guanidino nitrogens of arginyl residues of proteins.
            The enzyme acts on 40S ribosomal protein S2 (rpS2), which is its
            major in-vivo substrate, and is involved in the proper maturation
            of the 80S ribosome. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.76860.1,
                                           SRR1803611.134617.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331079.11/ ENSP00000331879.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..531
                     /product="protein arginine N-methyltransferase 3 isoform
                     1"
                     /EC_number="2.1.1.319"
                     /note="protein arginine N-methyltransferase 3;
                     heterogeneous nuclear ribonucleoprotein
                     methyltransferase-like protein 3; HMT1 hnRNP
                     methyltransferase-like 3"
                     /calculated_mol_wt=59772
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60678.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylcysteine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (O60678.4)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21059412,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O60678.4)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21059412,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60678.4)"
     Region          48..71
                     /region_name="Interaction with ZNF200.
                     /evidence=ECO:0000269|PubMed:39513743"
                     /note="propagated from UniProtKB/Swiss-Prot (O60678.4)"
     Region          50..>99
                     /region_name="zf-C2H2_2"
                     /note="C2H2 type zinc-finger (2 copies); pfam12756"
                     /db_xref="CDD:463690"
     Site            87
                     /site_type="other"
                     /note="Not phosphorylated.
                     /evidence=ECO:0000269|PubMed:21059412; propagated from
                     UniProtKB/Swiss-Prot (O60678.4)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60678.4)"
     Region          186..531
                     /region_name="Mediates interaction with ALDH1A1.
                     /evidence=ECO:0000269|PubMed:33495566"
                     /note="propagated from UniProtKB/Swiss-Prot (O60678.4)"
     Region          230..>393
                     /region_name="COG4076"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:443253"
     CDS             1..531
                     /gene="PRMT3"
                     /gene_synonym="HRMT1L3"
                     /coded_by="NM_005788.4:32..1627"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7853.1"
                     /db_xref="GeneID:10196"
                     /db_xref="HGNC:HGNC:30163"
                     /db_xref="MIM:603190"
ORIGIN      
        1 mcslasgatg grgaveneed lpelsdsgde aawededdad lphgkqqtpc lfcnrlftsa
       61 eetfshckse hqfnidsmvh khglefygyi klinfirlkn ptveymnsiy npvpwekeey
      121 lkpvleddll lqfdvedlye pvsvpfsypn glsentsvve klkhmearal saeaalarar
      181 edlqkmkqfa qdfvmhtdvr tcssstsvia dlqededgvy fssyghygih eemlkdkirt
      241 esyrdfiyqn phifkdkvvl dvgcgtgils mfaakagakk vlgvdqseil yqamdiirln
      301 kledtitlik gkieevhlpv ekvdviisew mgyfllfesm ldsvlyaknk ylakggsvyp
      361 dictislvav sdvnkhadri afwddvygfk mscmkkavip eavvevldpk tlisepcgik
      421 hidchttsis dlefssdftl kitrtsmcta iagyfdiyfe knchnrvvfs tgpqstkthw
      481 kqtvfllekp fsvkagealk gkvtvhknkk dprsltvtlt lnnstqtygl q
//
LOCUS       NP_001352152             374 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-dependent glucokinase isoform 2 [Homo sapiens].
ACCESSION   NP_001352152
VERSION     NP_001352152.1
DBSOURCE    REFSEQ: accession NM_001365223.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Herrera-Morande,A., Vallejos-Baccelliere,G., Cea,P.A., Zamora,R.A.,
            Cid,D., Maturana,P., Gonzalez-Ordenes,F., Castro-Fernandez,V. and
            Guixe,V.
  TITLE     Kinetic characterization and phylogenetic analysis of human
            ADP-dependent glucokinase reveal new insights into its regulatory
            properties
  JOURNAL   Arch Biochem Biophys 741, 109602 (2023)
   PUBMED   37084804
  REMARK    GeneRIF: Kinetic characterization and phylogenetic analysis of
            human ADP-dependent glucokinase reveal new insights into its
            regulatory properties.
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tandon,A., Birkenhagen,J., Nagalla,D., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase as a novel onco-target for haematological
            malignancies
  JOURNAL   Sci Rep 10 (1), 13584 (2020)
   PUBMED   32788680
  REMARK    GeneRIF: ADP-dependent glucokinase as a novel onco-target for
            haematological malignancies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Jiang,H.Y. and Wang,Z.J.
  TITLE     ADPGK-AS1 promotes the progression of colorectal cancer via
            sponging miR-525 to upregulate FUT1
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2380-2386 (2020)
   PUBMED   32196589
  REMARK    GeneRIF: ADPGK-AS1 promotes the progression of colorectal cancer
            via sponging miR-525 to upregulate FUT1.
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Imle,R., Wang,B.T., Stutzenberger,N., Birkenhagen,J., Tandon,A.,
            Carl,M., Himmelreich,N., Thiel,C., Grone,H.J., Poschet,G.,
            Volkers,M., Gulow,K., Schroder,A., Carillo,S., Mittermayr,S.,
            Bones,J., Kaminski,M.M., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing
  JOURNAL   Sci Rep 9 (1), 14248 (2019)
   PUBMED   31582762
  REMARK    GeneRIF: ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Richter,J.P., Goroncy,A.K., Ronimus,R.S. and Sutherland-Smith,A.J.
  TITLE     The Structural and Functional Characterization of Mammalian
            ADP-dependent Glucokinase
  JOURNAL   J Biol Chem 291 (8), 3694-3704 (2016)
   PUBMED   26555263
  REMARK    GeneRIF: ADPGK is substrate inhibited by high glucose concentration
            and shows high specificity for glucose, with no activity for other
            sugars, as determined by NMR spectroscopy, including 2-deoxyglucose
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Cuesta-Munoz,A.L., Tuomi,T., Cobo-Vuilleumier,N., Koskela,H.,
            Odili,S., Stride,A., Buettger,C., Otonkoski,T., Froguel,P.,
            Grimsby,J., Garcia-Gimeno,M. and Matschinsky,F.M.
  TITLE     Clinical heterogeneity in monogenic diabetes caused by mutations in
            the glucokinase gene (GCK-MODY)
  JOURNAL   Diabetes Care 33 (2), 290-292 (2010)
   PUBMED   19903754
  REMARK    GeneRIF: Glucose and insulin response to oral glucose is higher in
            GCK(261) carriers, indicating clinical heterogeneity in GCK
            maturity diabetes carriers.
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 374)
  AUTHORS   Codner,E., Rocha,A., Deng,L., Martinez-Aguayo,A., Godoy,C.,
            Mericq,V. and Chung,W.K.
  TITLE     Mild fasting hyperglycemia in children: high rate of glucokinase
            mutations and some risk of developing type 1 diabetes mellitus
  JOURNAL   Pediatr Diabetes 10 (6), 382-388 (2009)
   PUBMED   19309449
  REMARK    GeneRIF: The presence of mild persistent hyperglycemia in any
            patient without autoantibodies should lead to genetic analysis of
            glucokinase, particularly if there is a positive family history.
REFERENCE   9  (residues 1 to 374)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 374)
  AUTHORS   Ronimus,R.S. and Morgan,H.W.
  TITLE     Cloning and biochemical characterization of a novel mouse
            ADP-dependent glucokinase
  JOURNAL   Biochem Biophys Res Commun 315 (3), 652-658 (2004)
   PUBMED   14975750
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA031990.1, DA208247.1, BC044589.1, AC009712.22 and AK075560.1.
            
            Summary: ADPGK (EC 2.7.1.147) catalyzes the ADP-dependent
            phosphorylation of glucose to glucose-6-phosphate and may play a
            role in glycolysis, possibly during ischemic conditions (Ronimus
            and Morgan, 2004 [PubMed 14975750]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.74716.1, BC044589.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..374
                     /product="ADP-dependent glucokinase isoform 2"
                     /EC_number="2.7.1.147"
                     /note="ATP-dependent glucokinase; rbBP-35"
                     /calculated_mol_wt=40900
     Region          1..369
                     /region_name="ADPGK_ADPPFK"
                     /note="ADP-dependent glucokinase (ADPGK) and
                     phosphofructokinase (ADPPFK). ADPGK and ADPPFK are
                     proteins that rely on ADP rather than ATP to donate a
                     phosphoryl group. They are found in certain
                     hyperthermophilic archaea and in higher eukaryotes. A
                     functional...; cd01938"
                     /db_xref="CDD:238913"
     Site            order(37,175,202,205,358)
                     /site_type="other"
                     /note="Mg2+ binding site [ion binding]"
                     /db_xref="CDD:238913"
     Site            order(202,259..260,345,347,350,356..357,360)
                     /site_type="other"
                     /note="ADP binding site [chemical binding]"
                     /db_xref="CDD:238913"
     CDS             1..374
                     /gene="ADPGK"
                     /gene_synonym="2610017G09Rik; ADP-GK"
                     /coded_by="NM_001365223.1:647..1771"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:83440"
                     /db_xref="HGNC:HGNC:25250"
                     /db_xref="MIM:611861"
ORIGIN      
        1 mgkgaaaerf fsdketfhdi aqvasefpga qhyvggnaal igqkfaansd lkvllcgpvg
       61 pklhellddn vfvppeslqe vdefhliley qageewgqlk aphanrfifs hdlsngamnm
      121 levfvsslee fqpdlvvlsg lhmmegqske lqrkrllevv tsisdiptgi pvhlelasmt
      181 nrelmssivh qvfpavtslg lneqellflt qsasgphssl sswngvpdvg mvsdilfwil
      241 kehgrsksra sdltrihfht lvyhilatvd ghwanqlaav aagarvagtq acatetidts
      301 rvslrapqef mtshseagsr ivlnpnkpvv ewhregisfh ftpvlvckdp irtvglgdai
      361 saeglfysev hphy
//
LOCUS       NP_071411                322 aa            linear   PRI 27-APR-2025
DEFINITION  ribokinase isoform 1 [Homo sapiens].
ACCESSION   NP_071411
VERSION     NP_071411.1
DBSOURCE    REFSEQ: accession NM_022128.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Quiroga-Roger,D., Babul,J. and Guixe,V.
  TITLE     Role of monovalent and divalent metal cations in human ribokinase
            catalysis and regulation
  JOURNAL   Biometals 28 (2), 401-413 (2015)
   PUBMED   25749547
  REMARK    GeneRIF: Asn199 and Glu202 play an important role in the regulation
            of human ribokinase activity.
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Park,J., van Koeverden,P., Singh,B. and Gupta,R.S.
  TITLE     Identification and characterization of human ribokinase and
            comparison of its properties with E. coli ribokinase and human
            adenosine kinase
  JOURNAL   FEBS Lett 581 (17), 3211-3216 (2007)
   PUBMED   17585908
  REMARK    GeneRIF: Identification and characterization of human ribokinase.
REFERENCE   8  (residues 1 to 322)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC017425.1, AJ404857.1 and
            BF436282.1.
            
            Summary: This gene encodes a member of the carbohydrate kinase PfkB
            family. The encoded protein phosphorylates ribose to form
            ribose-5-phosphate in the presence of ATP and magnesium as a first
            step in ribose metabolism. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Dec 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.602201.1,
                                           SRR1660805.200425.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302188.8/ ENSP00000306817.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.2"
     Protein         1..322
                     /product="ribokinase isoform 1"
                     /EC_number="2.7.1.15"
                     /calculated_mol_wt=34012
     Region          22..318
                     /region_name="D_ribokin_bact"
                     /note="ribokinase; TIGR02152"
                     /db_xref="CDD:274000"
     Site            order(25,27,52..54,57,109,111,121,123,154,265..266,269,
                     307)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238579"
     Site            order(28,30,35..41,54,108,110..112,118..125,180)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238579"
     Site            order(199,235..237,240,255,261,264,267..268,271,295,
                     298..299,302)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238579"
     CDS             1..322
                     /gene="RBKS"
                     /gene_synonym="RBSK; RK"
                     /coded_by="NM_022128.3:43..1011"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1762.1"
                     /db_xref="GeneID:64080"
                     /db_xref="HGNC:HGNC:30325"
                     /db_xref="MIM:611132"
ORIGIN      
        1 maasgepqrq wqeevaavvv vgscmtdlvs ltsrlpktge tihghkffig fggkganqcv
       61 qaarlgamts mvckvgkdsf gndyienlkq ndisteftyq tkdaatgtas iivnnegqni
      121 ivivaganll lntedlraaa nvisrakvmv cqleitpats lealtmarrs gvktlfnpap
      181 aiadldpqfy tlsdvfccne seaeiltglt vgsaadagea alvllkrgcq vviitlgaeg
      241 cvvlsqtepe pkhiptekvk avdttgagds fvgalafyla yypnlsledm lnrsnfiaav
      301 svqaagtqss ypykkdlplt lf
//
LOCUS       NP_006298                464 aa            linear   PRI 27-APR-2025
DEFINITION  sushi repeat-containing protein SRPX isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_006298
VERSION     NP_006298.1
DBSOURCE    REFSEQ: accession NM_006307.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Jiao,Y., Geng,R., Zhong,Z., Ni,S., Liu,W., He,Z., Gan,S., Huang,Q.,
            Liu,J. and Bai,J.
  TITLE     A Hypoxia Molecular Signature-Based Prognostic Model for
            Endometrial Cancer Patients
  JOURNAL   Int J Mol Sci 24 (2), 1675 (2023)
   PUBMED   36675190
  REMARK    GeneRIF: A Hypoxia Molecular Signature-Based Prognostic Model for
            Endometrial Cancer Patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Liu,C.L., Pan,H.W., Torng,P.L., Fan,M.H. and Mao,T.L.
  TITLE     SRPX and HMCN1 regulate cancer-associated fibroblasts to promote
            the invasiveness of ovarian carcinoma
  JOURNAL   Oncol Rep 42 (6), 2706-2715 (2019)
   PUBMED   31638245
  REMARK    GeneRIF: the findings of the present study suggest that targeting
            the Cancerassociated fibroblasts genes, SRPX and HMCN1, can inhibit
            ovarian cancer migration and invasion.
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Inoue,Y., Ueda,M., Tasaki,M., Takeshima,A., Nagatoshi,A.,
            Masuda,T., Misumi,Y., Kosaka,T., Nomura,T., Mizukami,M.,
            Matsumoto,S., Yamashita,T., Takahashi,H., Kakita,A. and Ando,Y.
  TITLE     Sushi repeat-containing protein 1: a novel disease-associated
            molecule in cerebral amyloid angiopathy
  JOURNAL   Acta Neuropathol 134 (4), 605-617 (2017)
   PUBMED   28478503
  REMARK    GeneRIF: SRPX1 co-accumulated with Abeta deposits in cerebral blood
            vessels of all autopsied cases with severe cerebral amyloid
            angiopathy (CAA); no SRPX1 co-accumulated with Abeta deposits in
            senile plaques. Furthermore, we demonstrated that both Abeta40 and
            Abeta42 bound to SRPX1 in vitro and enhanced SRPX1 expression in
            primary cultures of cerebrovascular smooth muscle cells. SRPX1
            enhanced caspase activity induced by Abeta40.
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Naba,A., Clauser,K.R., Whittaker,C.A., Carr,S.A., Tanabe,K.K. and
            Hynes,R.O.
  TITLE     Extracellular matrix signatures of human primary metastatic colon
            cancers and their metastases to liver
  JOURNAL   BMC Cancer 14, 518 (2014)
   PUBMED   25037231
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Burnicka-Turek,O., Kata,A., Buyandelger,B., Ebermann,L.,
            Kramann,N., Burfeind,P., Hoyer-Fender,S., Engel,W. and Adham,I.M.
  TITLE     Pelota interacts with HAX1, EIF3G and SRPX and the resulting
            protein complexes are associated with the actin cytoskeleton
  JOURNAL   BMC Cell Biol 11, 28 (2010)
   PUBMED   20406461
  REMARK    GeneRIF: PELO is subcellularly localized at the actin cytoskeleton,
            interacts with HAX1, EIF3G and SRPX proteins and that this
            interaction occurs at the cytoskeleton; this interaction may
            facilitate PELO to detect and degrade aberrant mRNAs.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Shimakage,M., Takami,K., Kodama,K., Mano,M., Yutsudo,M. and
            Inoue,H.
  TITLE     Expression of drs mRNA in human lung adenocarcinomas
  JOURNAL   Hum Pathol 33 (6), 615-619 (2002)
   PUBMED   12152160
  REMARK    GeneRIF: expression of drs mRNA in well-differentiated, moderately
            differentiated, and poorly differentiated lung adenocarcinoma
            tissues (drs; down-regulated by v-scr)
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Nangaku,M., Shankland,S.J., Kurokawa,K., Bomsztyk,K., Johnson,R.J.
            and Couser,W.G.
  TITLE     Cloning of a new human gene with short consensus repeats using the
            EST database
  JOURNAL   Immunogenetics 46 (2), 99-103 (1997)
   PUBMED   9162095
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Dry,K.L., Aldred,M.A., Edgar,A.J., Brown,J., Manson,F.D., Ho,M.F.,
            Prosser,J., Hardwick,L.J., Lennon,A.A., Thomson,K. et al.
  TITLE     Identification of a novel gene, ETX1 from Xp21.1, a candidate gene
            for X-linked retintis pigmentosa (RP3)
  JOURNAL   Hum Mol Genet 4 (12), 2347-2353 (1995)
   PUBMED   8634709
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Meindl,A., Carvalho,M.R., Herrmann,K., Lorenz,B., Achatz,H.,
            Lorenz,B., Apfelstedt-Sylla,E., Wittwer,B., Ross,M. and
            Meitinger,T.
  TITLE     A gene (SRPX) encoding a sushi-repeat-containing protein is deleted
            in patients with X-linked retinitis pigmentosa
  JOURNAL   Hum Mol Genet 4 (12), 2339-2346 (1995)
   PUBMED   8634708
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Arlotta,P., Santori,L. and de Vecchi,A.
  TITLE     [A case of mixed tumor of the palate]
  JOURNAL   Acta Biol Med Ger 2 (3), 34 (1976)
   PUBMED   209648
  REMARK    GeneRIF: The SRPX protein contains the P-DUDES structural domain in
            its C-terminal region. This domain has significant albeit remote
            sequence similarity to thioredoxin-like domains, and is predicted
            to possess an oxidoreductase function.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC020684.1, AL121578.1 and BM672597.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020684.1, SRR3476690.775677.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378533.4/ ENSP00000367794.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..464
                     /product="sushi repeat-containing protein SRPX isoform 1
                     precursor"
                     /note="sushi-repeat-containing protein, X chromosome;
                     sushi repeat-containing protein SRPX; epididymis secretory
                     sperm binding protein Li 83p"
                     /calculated_mol_wt=48335
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3255
     mat_peptide     31..464
                     /product="Sushi repeat-containing protein SRPX.
                     /id=PRO_0000022416"
                     /note="propagated from UniProtKB/Swiss-Prot (P78539.1)"
                     /calculated_mol_wt=48335
     Site            34
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:32337544,
                     ECO:0000269|PubMed:36213313; propagated from
                     UniProtKB/Swiss-Prot (P78539.1)"
     Region          <53..175
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          120..175
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(130,148)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          175..257
                     /region_name="HYR"
                     /note="HYR domain; pfam02494"
                     /db_xref="CDD:460572"
     Region          262..317
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(272,291)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          332..451
                     /region_name="DUF4174"
                     /note="Domain of unknown function (DUF4174); pfam13778"
                     /db_xref="CDD:463980"
     CDS             1..464
                     /gene="SRPX"
                     /gene_synonym="DRS; ETX1; HEL-S-83p; SRPX1"
                     /coded_by="NM_006307.5:80..1474"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS14245.1"
                     /db_xref="GeneID:8406"
                     /db_xref="HGNC:HGNC:11309"
                     /db_xref="MIM:300187"
ORIGIN      
        1 mgspahrpal llllppllll lllrvppsrs fpgsgdsple ddevgyshpr ykdtpwcspi
       61 kvkygdvycr apqggyykta lgtrcdircq kgyelhgssl licqsnkrws dkvickqkrc
      121 ptlampangg fkcvdgayfn srceyycspg ytlkgertvt cmdnkawsgr pascvdmepp
      181 rikcpsvker iaepnkltvr vswetpegrd tadgiltdvi lkglppgsnf pegdhkiqyt
      241 vydraenkgt ckfrvkvrvk rcgklnapen gymkcssdgd nygatcefsc iggyelqgsp
      301 arvcqsnlaw sgteptcaam nvnvgvrtaa alldqfyekr rllivstpta rnllyrlqlg
      361 mlqqaqcgld lrhitvvelv gvfptligri gakimppala lqlrlllrip lysfsmvlvd
      421 khgmdkeryv slvmpvalfn lidtfplrke emvlqaemsq tcnt
//
LOCUS       NP_080296                115 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein P2 isoform a [Mus musculus].
ACCESSION   NP_080296
VERSION     NP_080296.3
DBSOURCE    REFSEQ: accession NM_026020.7
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Khatter,H., Myasnikov,A.G., Natchiar,S.K. and Klaholz,B.P.
  TITLE     Structure of the human 80S ribosome
  JOURNAL   Nature 520 (7549), 640-645 (2015)
   PUBMED   25901680
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Vannella,K.M., Barron,L., Borthwick,L.A., Kindrachuk,K.N.,
            Narasimhan,P.B., Hart,K.M., Thompson,R.W., White,S., Cheever,A.W.,
            Ramalingam,T.R. and Wynn,T.A.
  TITLE     Incomplete deletion of IL-4Ralpha by LysM(Cre) reveals distinct
            subsets of M2 macrophages controlling inflammation and fibrosis in
            chronic schistosomiasis
  JOURNAL   PLoS Pathog 10 (9), e1004372 (2014)
   PUBMED   25211233
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Perucho,L., Artero-Castro,A., Guerrero,S., Ramon y Cajal,S.,
            LLeonart,M.E. and Wang,Z.Q.
  TITLE     RPLP1, a crucial ribosomal protein for embryonic development of the
            nervous system
  JOURNAL   PLoS One 9 (6), e99956 (2014)
   PUBMED   24959908
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Trinidad,J.C., Specht,C.G., Thalhammer,A., Schoepfer,R. and
            Burlingame,A.L.
  TITLE     Comprehensive identification of phosphorylation sites in
            postsynaptic density preparations
  JOURNAL   Mol Cell Proteomics 5 (5), 914-922 (2006)
   PUBMED   16452087
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   7  (residues 1 to 115)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158224.6.
            
            On Dec 20, 2005 this sequence version replaced NP_080296.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1 and 2
            both encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG085364.2, BG072570.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 86.8 cM"
     Protein         1..115
                     /product="large ribosomal subunit protein P2 isoform a"
                     /note="60S acidic ribosomal protein P2; large ribosomal
                     subunit protein P2; ribosomal protein, large P2"
                     /calculated_mol_wt=11520
     Region          1..>66
                     /region_name="Ribosomal_P2"
                     /note="Ribosomal protein P2. This subfamily represents the
                     eukaryotic large ribosomal protein P2. Eukaryotic P1 and
                     P2 are functionally equivalent to the bacterial protein
                     L7/L12, but are not homologous to L7/L12. P2 is located in
                     the L12 stalk, with proteins...; cd05833"
                     /db_xref="CDD:100111"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P05387; propagated from
                     UniProtKB/Swiss-Prot (P99027.3)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P99027.3)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05387; propagated from
                     UniProtKB/Swiss-Prot (P99027.3)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P99027.3)"
     Region          76..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P99027.3)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05387; propagated from
                     UniProtKB/Swiss-Prot (P99027.3)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P99027.3)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747,
                     ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (P99027.3)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747,
                     ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (P99027.3)"
     CDS             1..115
                     /gene="Rplp2"
                     /gene_synonym="2700049I22Rik"
                     /coded_by="NM_026020.7:59..406"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS40187.1"
                     /db_xref="GeneID:67186"
                     /db_xref="MGI:MGI:1914436"
ORIGIN      
        1 mryvasylla alggnsspsa kdikkildsv gieadddrln kviselngkn iedviaqgvg
       61 klasvpagga vavsaapgsa apaagsapaa aeekkdekke eseesdddmg fglfd
//
LOCUS       NP_057480                466 aa            linear   PRI 27-APR-2025
DEFINITION  CTD small phosphatase-like protein 2 [Homo sapiens].
ACCESSION   NP_057480
VERSION     NP_057480.2
DBSOURCE    REFSEQ: accession NM_016396.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Klerk,D.H., Kooi,E.M., Bos,A.F., Hulscher,J.B.,
            Verkaik-Schakel,R.N. and Plosch,T.
  TITLE     Hypermethylation of CTDSPL2 prior to necrotizing enterocolitis
            onset
  JOURNAL   Epigenomics 15 (8), 479-486 (2023)
   PUBMED   37309586
  REMARK    GeneRIF: Hypermethylation of CTDSPL2 prior to necrotizing
            enterocolitis onset.
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Xiao,Y., Chen,Y., Peng,A. and Dong,J.
  TITLE     The phosphatase CTDSPL2 is phosphorylated in mitosis and a target
            for restraining tumor growth and motility in pancreatic cancer
  JOURNAL   Cancer Lett 526, 53-65 (2022)
   PUBMED   34813892
  REMARK    GeneRIF: The phosphatase CTDSPL2 is phosphorylated in mitosis and a
            target for restraining tumor growth and motility in pancreatic
            cancer.
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Polyanskaya,S.A., Moreno,R.Y., Lu,B., Feng,R., Yao,Y., Irani,S.,
            Klingbeil,O., Yang,Z., Wei,Y., Demerdash,O.E., Benjamin,L.A.,
            Weiss,M.J., Zhang,Y.J. and Vakoc,C.R.
  TITLE     SCP4-STK35/PDIK1L complex is a dual phospho-catalytic signaling
            dependency in acute myeloid leukemia
  JOURNAL   Cell Rep 38 (2), 110233 (2022)
   PUBMED   35021089
  REMARK    GeneRIF: SCP4-STK35/PDIK1L complex is a dual phospho-catalytic
            signaling dependency in acute myeloid leukemia.
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 466)
  AUTHORS   Liu,X., Yu,R., Sun,L., Garibotto,G., Lin,X., Wang,Y., Thomas,S.S.,
            Li,R. and Hu,Z.
  TITLE     The nuclear phosphatase SCP4 regulates FoxO transcription factors
            during muscle wasting in chronic kidney disease
  JOURNAL   Kidney Int 92 (2), 336-348 (2017)
   PUBMED   28506762
  REMARK    GeneRIF: expression significantly increased in skeletal muscle of
            chronic kidney disease patients
REFERENCE   7  (residues 1 to 466)
  AUTHORS   St-Denis,N., Gupta,G.D., Lin,Z.Y., Gonzalez-Badillo,B., Veri,A.O.,
            Knight,J.D.R., Rajendran,D., Couzens,A.L., Currie,K.W., Tkach,J.M.,
            Cheung,S.W.T., Pelletier,L. and Gingras,A.C.
  TITLE     Phenotypic and Interaction Profiling of the Human Phosphatases
            Identifies Diverse Mitotic Regulators
  JOURNAL   Cell Rep 17 (9), 2488-2501 (2016)
   PUBMED   27880917
REFERENCE   8  (residues 1 to 466)
  AUTHORS   Wani,S., Sugita,A., Ohkuma,Y. and Hirose,Y.
  TITLE     Human SCP4 is a chromatin-associated CTD phosphatase and exhibits
            the dynamic translocation during erythroid differentiation
  JOURNAL   J Biochem 160 (2), 111-120 (2016)
   PUBMED   26920047
  REMARK    GeneRIF: SCP4 is a unique chromatin-associated, Ser5-preferential
            CTD phosphatase that preferentially distributes to
            transcriptionally silenced gene regions and may participate in gene
            regulation during erythroid differentiation.
REFERENCE   9  (residues 1 to 466)
  AUTHORS   Kang,N., Koo,J., Wang,S., Hur,S.J. and Bahk,Y.Y.
  TITLE     A systematic study of nuclear interactome of C-terminal domain
            small phosphatase-like 2 using inducible expression system and
            shotgun proteomics
  JOURNAL   BMB Rep 49 (6), 319-324 (2016)
   PUBMED   26674342
  REMARK    GeneRIF: proteomic screening was conducted to identify binding
            partners of CTDSPL2 in nuclear extract through immunoprecipitation
            of CTDSPL2 with its associated.
REFERENCE   10 (residues 1 to 466)
  AUTHORS   Ma,Y.N., Zhang,X., Yu,H.C. and Zhang,J.W.
  TITLE     CTD small phosphatase like 2 (CTDSPL2) can increase epsilon- and
            gamma-globin gene expression in K562 cells and CD34+ cells derived
            from umbilical cord blood
  JOURNAL   BMC Cell Biol 11, 75 (2010)
   PUBMED   20932329
  REMARK    GeneRIF: increases epsilon- and gamma-globin gene expression during
            erythroid differentiation
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF161478.1, BC035744.1 and AC009996.7.
            
            On May 24, 2006 this sequence version replaced NP_057480.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.13585.1,
                                           SRR1660803.252795.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260327.9/ ENSP00000260327.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.3-q21.1"
     Protein         1..466
                     /product="CTD small phosphatase-like protein 2"
                     /EC_number="3.1.3.-"
                     /note="CTDSP-like 2; CTD (carboxy-terminal domain, RNA
                     polymerase II, polypeptide A) small phosphatase like 2"
                     /calculated_mol_wt=52868
     Region          1..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05D32.2)"
     Site            26
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q05D32.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q05D32.2)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q05D32.2)"
     Site            57
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q05D32.2)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q05D32.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q05D32.2)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q05D32.2)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q05D32.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q05D32.2)"
     Region          220..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05D32.2)"
     Region          287..448
                     /region_name="HIF-SF_euk"
                     /note="Dullard-like phosphatase domain; TIGR02251"
                     /db_xref="CDD:274055"
     Site            order(293..297,301..302,348..351,355,388,404..405,
                     407..409)
                     /site_type="active"
                     /db_xref="CDD:319823"
     CDS             1..466
                     /gene="CTDSPL2"
                     /gene_synonym="HSPC058; HSPC129; SCP4"
                     /coded_by="NM_016396.3:169..1569"
                     /db_xref="CCDS:CCDS10110.1"
                     /db_xref="GeneID:51496"
                     /db_xref="HGNC:HGNC:26936"
                     /db_xref="MIM:618739"
ORIGIN      
        1 mrlrtrkasq qsnqiqtqrt arakrkysev ddslpsggek psknetglls sikkfikgst
       61 pkeerenpsk rsrierdidn nlitstprag ekpnkqisrv rrksqvngea gsyemtnqhv
      121 kqngklednp ssgspprttl lgtifspvfn ffspankngt sgsdspgqav eaeeivkqld
      181 meqvdeitts tttstngaay snqavqvrps lnngleeaee tvnrdipplt apvtpdsgys
      241 sahaeatyee dwevfdpyyf ikhvppltee qlnrkpalpl ktrstpefsl vldldetlvh
      301 cslneledaa ltfpvlfqdv iyqvyvrlrp ffreflerms qmyeiilfta skkvyadkll
      361 nildpkkqlv rhrlfrehcv cvqgnyikdl nilgrdlskt iiidnspqaf ayqlsngipi
      421 eswfmdkndn ellklipfle klvelnedvr phirdrfrlh dllppd
//
LOCUS       NP_005458                740 aa            linear   PRI 27-APR-2025
DEFINITION  N-acetylated-alpha-linked acidic dipeptidase 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_005458
VERSION     NP_005458.1
DBSOURCE    REFSEQ: accession NM_005467.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Suetsugu,H., Kim,K., Yamamoto,T., Bang,S.Y., Sakamoto,Y.,
            Shin,J.M., Sugano,N., Kim,J.S., Mukai,M., Lee,Y.K., Ohmura,K.,
            Park,D.J., Takahashi,D., Ahn,G.Y., Karino,K., Kwon,Y.C.,
            Miyamura,T., Kim,J., Nakamura,J., Motomura,G., Kuroda,T., Niiro,H.,
            Miyamoto,T., Takeuchi,T., Ikari,K., Amano,K., Tada,Y., Yamaji,K.,
            Shimizu,M., Atsumi,T., Seki,T., Tanaka,Y., Kubo,T., Hisada,R.,
            Yoshioka,T., Yamazaki,M., Kabata,T., Kajino,T., Ohta,Y., Okawa,T.,
            Naito,Y., Kaneuji,A., Yasunaga,Y., Ohzono,K., Tomizuka,K.,
            Koido,M., Matsuda,K., Okada,Y., Suzuki,A., Kim,B.J., Kochi,Y.,
            Lee,H.S., Ikegawa,S., Bae,S.C. and Terao,C.
  TITLE     Novel susceptibility loci for steroid-associated osteonecrosis of
            the femoral head in systemic lupus erythematosus
  JOURNAL   Hum Mol Genet 31 (7), 1082-1095 (2022)
   PUBMED   34850884
  REMARK    GeneRIF: Novel susceptibility loci for steroid-associated
            osteonecrosis of the femoral head in systemic lupus erythematosus.
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Daniunaite,K., Bakavicius,A., Zukauskaite,K., Rauluseviciute,I.,
            Lazutka,J.R., Ulys,A., Jankevicius,F. and Jarmalaite,S.
  TITLE     Promoter Methylation of PRKCB, ADAMTS12, and NAALAD2 Is Specific to
            Prostate Cancer and Predicts Biochemical Disease Recurrence
  JOURNAL   Int J Mol Sci 22 (11), 6091 (2021)
   PUBMED   34198725
  REMARK    GeneRIF: Promoter Methylation of PRKCB, ADAMTS12, and NAALAD2 Is
            Specific to Prostate Cancer and Predicts Biochemical Disease
            Recurrence.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Vorlova,B., Knedlik,T., Tykvart,J. and Konvalinka,J.
  TITLE     GCPII and its close homolog GCPIII: from a neuropeptidase to a
            cancer marker and beyond
  JOURNAL   Front Biosci (Landmark Ed) 24 (4), 648-687 (2019)
   PUBMED   30844704
  REMARK    GeneRIF: GCPII has been recognized as a neuropeptidase in the
            central nervous system, as a folate hydrolase participating in
            absorption of folates in the jejunum and, most importantly, as a
            prostate-specific membrane antigen that is highly expressed in
            prostate adenocarcinoma; GCPIII has not been associated with any
            specific physiolological functions [review]
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Navratil,M., Tykvart,J., Schimer,J., Pachl,P., Navratil,V.,
            Rokob,T.A., Hlouchova,K., Rulisek,L. and Konvalinka,J.
  TITLE     Comparison of human glutamate carboxypeptidases II and III reveals
            their divergent substrate specificities
  JOURNAL   FEBS J 283 (13), 2528-2545 (2016)
   PUBMED   27208881
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Hlouchova,K., Barinka,C., Konvalinka,J. and Lubkowski,J.
  TITLE     Structural insight into the evolutionary and pharmacologic homology
            of glutamate carboxypeptidases II and III
  JOURNAL   FEBS J 276 (16), 4448-4462 (2009)
   PUBMED   19678840
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Hlouchova,K., Barinka,C., Klusak,V., Sacha,P., Mlcochova,P.,
            Majer,P., Rulisek,L. and Konvalinka,J.
  TITLE     Biochemical characterization of human glutamate carboxypeptidase
            III
  JOURNAL   J Neurochem 101 (3), 682-696 (2007)
   PUBMED   17241121
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Lambert,L.A. and Mitchell,S.L.
  TITLE     Molecular evolution of the transferrin receptor/glutamate
            carboxypeptidase II family
  JOURNAL   J Mol Evol 64 (1), 113-128 (2007)
   PUBMED   17160644
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Semple,C.A., Devon,R.S., Le Hellard,S. and Porteous,D.J.
  TITLE     Identification of genes from a schizophrenia-linked translocation
            breakpoint region
  JOURNAL   Genomics 73 (1), 123-126 (2001)
   PUBMED   11352574
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Pangalos,M.N., Neefs,J.M., Somers,M., Verhasselt,P., Bekkers,M.,
            van der Helm,L., Fraiponts,E., Ashton,D. and Gordon,R.D.
  TITLE     Isolation and expression of novel human glutamate carboxypeptidases
            with N-acetylated alpha-linked acidic dipeptidase and dipeptidyl
            peptidase IV activity
  JOURNAL   J Biol Chem 274 (13), 8470-8483 (1999)
   PUBMED   10085079
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN355388.1, AK075390.1,
            AJ012370.1 and AP000648.5.
            
            Summary: This gene is a member of the N-acetylated alpha-linked
            acidic dipeptidase (NAALADase) gene family. The representative
            member of this family is the gene encoding human prostate-specific
            membrane antigen (PSM), which is a marker of prostatic carcinomas
            and is the first to be shown to possess NAALADase activity.
            NAALADase cleaves N-acetyl-L-aspartate-L-glutamate (NAAG), which is
            a neuropeptide expressed both in the central nervous systems and in
            the periphery and is thought to function as a neurotransmitter. The
            product of this gene is a type II integral membrane protein.
            Transient transfection of this gene confers both NAALADase and
            dipetidyl peptidase IV activities to mammalian cells. This gene is
            highly expressed in ovary and testis as well as within discrete
            brain areas. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK075390.1, AJ012370.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000534061.6/ ENSP00000432481.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.3"
     Protein         1..740
                     /product="N-acetylated-alpha-linked acidic dipeptidase 2
                     isoform 1"
                     /EC_number="3.4.17.21"
                     /note="N-acetylated alpha-linked acidic dipeptidase II;
                     NAALADase II; glutamate carboxypeptidase III; NAALADASE2"
                     /calculated_mol_wt=83461
     Site            8..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q0.1)"
     Region          59..>104
                     /region_name="Zinc_peptidase_like"
                     /note="Zinc peptidases M18, M20, M28, and M42; cl14876"
                     /db_xref="CDD:472712"
     Region          110..336
                     /region_name="PA_GCPII_like"
                     /note="Protease-associated domain containing protein,
                     glutamate carboxypeptidase II (GCPII)-like. This group
                     contains various PA domain-containing proteins similar to
                     GCPII including, GCPIII (NAALADase2) and NAALADase L.
                     These proteins belong to the peptidase...; cd02121"
                     /db_xref="CDD:239036"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19678840,
                     ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
                     ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3; propagated
                     from UniProtKB/Swiss-Prot (Q9Y3Q0.1)"
     Site            143
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q04609; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q0.1)"
     Site            order(154,243..245,247,253..256,259)
                     /site_type="other"
                     /note="apical/protease domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239036"
     Site            185
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19678840,
                     ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
                     ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3; propagated
                     from UniProtKB/Swiss-Prot (Q9Y3Q0.1)"
     Site            order(200,247)
                     /site_type="other"
                     /note="substrate binding [chemical binding]"
                     /db_xref="CDD:239036"
     Site            order(262..263,265,267)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239036"
     Region          264..577
                     /region_name="NAALADase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q0.1)"
     Site            314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q0.1)"
     Region          331..585
                     /region_name="M28_PSMA_like"
                     /note="M28 Zn-peptidase prostate-specific membrane
                     antigen; cd08022"
                     /db_xref="CDD:349942"
     Site            order(358..359,361,405,426..427,434)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349942"
     Site            order(367,377,414..415,417..418,443..444,446..447,
                     508..509,526,539,542..543)
                     /site_type="active"
                     /db_xref="CDD:349942"
     Site            449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19678840,
                     ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
                     ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3; propagated
                     from UniProtKB/Swiss-Prot (Q9Y3Q0.1)"
     Site            603
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q0.1)"
     Region          617..737
                     /region_name="TFR_dimer"
                     /note="Transferrin receptor-like dimerization domain;
                     pfam04253"
                     /db_xref="CDD:461238"
     Site            628
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19678840,
                     ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
                     ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3; propagated
                     from UniProtKB/Swiss-Prot (Q9Y3Q0.1)"
     CDS             1..740
                     /gene="NAALAD2"
                     /gene_synonym="GCP3; GCPIII; GPCIII"
                     /coded_by="NM_005467.4:97..2319"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8288.1"
                     /db_xref="GeneID:10003"
                     /db_xref="HGNC:HGNC:14526"
                     /db_xref="MIM:611636"
ORIGIN      
        1 maesrgrlyl wmclaaalas flmgfmvgwf ikplkettts vryhqsirwk lvsemkaeni
       61 ksflrsftkl phlagteqnf llakkiqtqw kkfgldsakl vhydvllsyp netnanyisi
      121 vdeheteifk tsylepppdg yenvtnivpp ynafsaqgmp egdlvyvnya rtedffkler
      181 emginctgki viarygkifr gnkvknamla gaigiilysd padyfapevq pypkgwnlpg
      241 taaqrgnvln lngagdpltp gypakeytfr ldveegvgip ripvhpigyn daeillrylg
      301 giappdkswk galnvsysig pgftgsdsfr kvrmhvynin kitriynvvg tirgsvepdr
      361 yvilgghrds wvfgaidpts gvavlqeiar sfgklmskgw rprrtiifas wdaeefgllg
      421 stewaeenvk ilqersiayi nsdssiegny tlrvdctpll yqlvykltke ipspddgfes
      481 kslyeswlek dpspenknlp rinklgsgsd feayfqrlgi asgrarytkn kktdkyssyp
      541 vyhtiyetfe lvekfydptf kkqlsvaqlr galvyelvds kiipfniqdy aealknyaas
      601 iynlskkhdq qltdhgvsfd slfsavknfs eaasdfhkrl iqvdlnnpia vrmmndqlml
      661 lerafidplg lpgklfyrhi ifapsshnky agesfpgiyd aifdienkan srlawkevkk
      721 hisiaaftiq aaagtlkevl
//
LOCUS       NP_001356530             572 aa            linear   PRI 27-APR-2025
DEFINITION  suppressor of tumorigenicity 7 protein isoform 4 [Homo sapiens].
ACCESSION   NP_001356530
VERSION     NP_001356530.1
DBSOURCE    REFSEQ: accession NM_001369601.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Liu,H., Lu,W., He,H., Wu,J., Zhang,C., Gong,H. and Yang,C.
  TITLE     Inflammation-dependent overexpression of c-Myc enhances CRL4DCAF4
            E3 ligase activity and promotes ubiquitination of ST7 in
            colitis-associated cancer
  JOURNAL   J Pathol 248 (4), 464-475 (2019)
   PUBMED   30945288
  REMARK    GeneRIF: Inflammation-dependent overexpression of c-Myc enhances
            CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7
            in colitis-associated cancer.
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Yan,F., Alinari,L., Lustberg,M.E., Martin,L.K.,
            Cordero-Nieves,H.M., Banasavadi-Siddegowda,Y., Virk,S.,
            Barnholtz-Sloan,J., Bell,E.H., Wojton,J., Jacob,N.K.,
            Chakravarti,A., Nowicki,M.O., Wu,X., Lapalombella,R., Datta,J.,
            Yu,B., Gordon,K., Haseley,A., Patton,J.T., Smith,P.L., Ryu,J.,
            Zhang,X., Mo,X., Marcucci,G., Nuovo,G., Kwon,C.H., Byrd,J.C.,
            Chiocca,E.A., Li,C., Sif,S., Jacob,S., Lawler,S., Kaur,B. and
            Baiocchi,R.A.
  TITLE     Genetic validation of the protein arginine methyltransferase PRMT5
            as a candidate therapeutic target in glioblastoma
  JOURNAL   Cancer Res 74 (6), 1752-1765 (2014)
   PUBMED   24453002
  REMARK    GeneRIF: The tumor suppressor ST7 is a key gene silenced by PRMT5.
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Hu,L., Wu,C., Zhao,X., Heist,R., Su,L., Zhao,Y., Han,B., Cao,S.,
            Chu,M., Dai,J., Dong,J., Shu,Y., Xu,L., Chen,Y., Wang,Y., Lu,F.,
            Jiang,Y., Yu,D., Chen,H., Tan,W., Ma,H., Chen,J., Jin,G., Wu,T.,
            Lu,D., Christiani,D.C., Lin,D., Hu,Z. and Shen,H.
  TITLE     Genome-wide association study of prognosis in advanced non-small
            cell lung cancer patients receiving platinum-based chemotherapy
  JOURNAL   Clin Cancer Res 18 (19), 5507-5514 (2012)
   PUBMED   22872573
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Zenklusen,J.C., Rodriguez,L.V., LaCava,M., Wang,Z., Goldstein,L.S.
            and Conti,C.J.
  TITLE     Novel susceptibility locus for mouse hepatomas: evidence for a
            conserved tumor suppressor gene
  JOURNAL   Genome Res 6 (11), 1070-1076 (1996)
   PUBMED   8938430
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Zenklusen,J.C., Weitzel,J.N., Ball,H.G. and Conti,C.J.
  TITLE     Allelic loss at 7q31.1 in human primary ovarian carcinomas suggests
            the existence of a tumor suppressor gene
  JOURNAL   Oncogene 11 (2), 359-363 (1995)
   PUBMED   7624150
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Zenklusen,J.C., Thompson,J.C., Troncoso,P., Kagan,J. and Conti,C.J.
  TITLE     Loss of heterozygosity in human primary prostate carcinomas: a
            possible tumor suppressor gene at 7q31.1
  JOURNAL   Cancer Res 54 (24), 6370-6373 (1994)
   PUBMED   7987830
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Zenklusen,J.C., Bieche,I., Lidereau,R. and Conti,C.J.
  TITLE     (C-A)n microsatellite repeat D7S522 is the most commonly deleted
            region in human primary breast cancer
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12155-12158 (1994)
   PUBMED   7991599
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Ogata,T., Ayusawa,D., Namba,M., Takahashi,E., Oshimura,M. and
            Oishi,M.
  TITLE     Chromosome 7 suppresses indefinite division of nontumorigenic
            immortalized human fibroblast cell lines KMST-6 and SUSM-1
  JOURNAL   Mol Cell Biol 13 (10), 6036-6043 (1993)
   PUBMED   8105370
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106873.3, AC002542.1 and
            AC003987.1.
            
            Summary: The gene for this product maps to a region on chromosome 7
            identified as an autism-susceptibility locus. Mutation screening of
            the entire coding region in autistic individuals failed to identify
            phenotype-specific variants, suggesting that coding mutations for
            this gene are unlikely to be involved in the etiology of autism.
            The function of this gene product has not been determined.
            Transcript variants encoding different isoforms of this protein
            have been described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.166753.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.2"
     Protein         1..572
                     /product="suppressor of tumorigenicity 7 protein isoform
                     4"
                     /note="family with sequence similarity 4, subfamily A,
                     member 1; suppression of tumorigenicity 7 (breast);
                     suppressor of tumorigenicity 7 protein"
                     /calculated_mol_wt=65390
     Site            15..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC1.1)"
     Region          18..571
                     /region_name="ST7"
                     /note="ST7 protein; pfam04184"
                     /db_xref="CDD:461214"
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRC1.1)"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC1.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9NRC1.1)"
     Site            507..527
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC1.1)"
     CDS             1..572
                     /gene="ST7"
                     /gene_synonym="ETS7q; FAM4A; FAM4A1; HELG; RAY1; SEN4;
                     TSG7"
                     /coded_by="NM_001369601.1:41..1759"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS94181.1"
                     /db_xref="GeneID:7982"
                     /db_xref="HGNC:HGNC:11351"
                     /db_xref="MIM:600833"
ORIGIN      
        1 maeaatgfle qlkscivwsw tylwtvwffi vlflvyilrv plkindnlst vsmflntltp
       61 kfyvaltgts slisglilif ewwyfrkygt sfieqvsvsh lrpllggvdn nssnnsnssn
      121 gdsdsnrqsv seckvwrnpl nlfrgaeynr ytwvtgrepl tyydmnlsaq dhqtfftcds
      181 dhlrpadaim qkawrernpq arisaaheal eineirsrve vpliasstiw eikllpkcat
      241 ayillaeeea ttiaeaeklf kqalkagdgc yrrsqqlqhh gsqyeaqhrr dtnvlvyikr
      301 rlamcarrlg rtreavkmmr dlmkefplls mfnihenlle allelqayad vqavlakydd
      361 islpksatic ytaallkara vsdkfspeaa srrglstaem naveaihrav efnphvpkyl
      421 lemkslilpp ehilkrgdse aiayaffhla hwkrvegaln llhsfrmipy plekghlfyp
      481 ypictetadr ellpsfhevs vypkkelpff ilftaglcsf tamlallthq fpelmgvfak
      541 aflstlfapl nfvmekvesi lpsslwhqlt ri
//
LOCUS       NP_006029                520 aa            linear   PRI 27-APR-2025
DEFINITION  spermatogenesis-associated protein 2 [Homo sapiens].
ACCESSION   NP_006029
VERSION     NP_006029.1
DBSOURCE    REFSEQ: accession NM_006038.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Wieser,V., Tsibulak,I., Degasper,C., Welponer,H., Leitner,K.,
            Parson,W., Zeimet,A.G., Marth,C. and Fiegl,H.
  TITLE     Tumor necrosis factor receptor modulator spermatogenesis-associated
            protein 2 is a novel predictor of outcome in ovarian cancer
  JOURNAL   Cancer Sci 110 (3), 1117-1126 (2019)
   PUBMED   30697874
  REMARK    GeneRIF: A role of SPATA2 in tumorigenesis.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Elliott,P.R., Leske,D., Hrdinka,M., Bagola,K., Fiil,B.K.,
            McLaughlin,S.H., Wagstaff,J., Volkmar,N., Christianson,J.C.,
            Kessler,B.M., Freund,S.M., Komander,D. and Gyrd-Hansen,M.
  TITLE     SPATA2 Links CYLD to LUBAC, Activates CYLD, and Controls LUBAC
            Signaling
  JOURNAL   Mol Cell 63 (6), 990-1005 (2016)
   PUBMED   27591049
  REMARK    GeneRIF: The data reveal SPATA2 as a high-affinity binding partner
            of CYLD and HOIP, and a regulatory component of linear ubiquitin
            chain assembly complex-mediated NF-kappaB signaling.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Sauce,D., Larsen,M., Abbott,R.J., Hislop,A.D., Leese,A.M., Khan,N.,
            Papagno,L., Freeman,G.J. and Rickinson,A.B.
  TITLE     Upregulation of interleukin 7 receptor alpha and programmed death 1
            marks an epitope-specific CD8+ T-cell response that disappears
            following primary Epstein-Barr virus infection
  JOURNAL   J Virol 83 (18), 9068-9078 (2009)
   PUBMED   19605492
  REMARK    GeneRIF: disappearance of TLD epitope reactivity from an otherwise
            stable EBV-specific response reflects selective loss of cognate
            antigen restimulation, not IL-7-dependent signals, and is
            immediately preceded by PD-1 upregulation to unprecedented levels.
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Capon,F., Bijlmakers,M.J., Wolf,N., Quaranta,M., Huffmeier,U.,
            Allen,M., Timms,K., Abkevich,V., Gutin,A., Smith,R., Warren,R.B.,
            Young,H.S., Worthington,J., Burden,A.D., Griffiths,C.E., Hayday,A.,
            Nestle,F.O., Reis,A., Lanchbury,J., Barker,J.N. and Trembath,R.C.
  TITLE     Identification of ZNF313/RNF114 as a novel psoriasis susceptibility
            gene
  JOURNAL   Hum Mol Genet 17 (13), 1938-1945 (2008)
   PUBMED   18364390
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Liliana Slongo,M., Zotti,L. and Onisto,M.
  TITLE     Cloning and characterization of the promoter region of human spata2
            (spermatogenesis-associated protein 2) gene
  JOURNAL   Biochim Biophys Acta 1625 (2), 192-196 (2003)
   PUBMED   12531478
  REMARK    GeneRIF: cloning and base sequence of the promoter region
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Graziotto,R., Foresta,C., Scannapieco,P., Zeilante,P., Russo,A.,
            Negro,A., Salmaso,R. and Onisto,M.
  TITLE     cDNA cloning and characterization of PD1: a novel human testicular
            protein with different expressions in various testiculopathies
  JOURNAL   Exp Cell Res 248 (2), 620-626 (1999)
   PUBMED   10222154
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK295536.1, BC009481.2, AL031685.18 and N62318.1.
            
            Transcript Variant: This variant (1) and variant 2 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.445800.1, AB018300.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2156266 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000289431.10/ ENSP00000289431.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.13"
     Protein         1..520
                     /product="spermatogenesis-associated protein 2"
                     /note="spermatogenesis associated PD1;
                     spermatogenesis-associated protein PD1; protein
                     phosphatase 1, regulatory subunit 145"
                     /calculated_mol_wt=58296
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UM82.2)"
     Region          301..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM82.2)"
     Region          327..344
                     /region_name="PIM motif.
                     /evidence=ECO:0000305|PubMed:27458237,
                     ECO:0000305|PubMed:27545878, ECO:0000305|PubMed:27591049"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM82.2)"
     Region          434..458
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM82.2)"
     Region          460..503
                     /region_name="Bbox1"
                     /note="B-box-type 1 zinc finger (Bbox1); cd19757"
                     /db_xref="CDD:380815"
     CDS             1..520
                     /gene="SPATA2"
                     /gene_synonym="PD1; PPP1R145; tamo"
                     /coded_by="NM_006038.4:253..1815"
                     /db_xref="CCDS:CCDS13422.1"
                     /db_xref="GeneID:9825"
                     /db_xref="HGNC:HGNC:14681"
                     /db_xref="MIM:607662"
ORIGIN      
        1 mgkpssmdtk fkddlfrkyv qfheskvdtt tsrqrpgsde clrvaastll slhkvdpfyr
       61 frliqfyevv esslrslsss slralhgafs mletvginlf lypwkkefrs iktytgpfvy
      121 yvkstlleed irailscmgy tpelgtaykl relvetlqvk mvsfelflak veceqmleih
      181 sqvkdkgyse ldivserkss aedvrgcsda lrrraegreh ltasmsrval qksaseraak
      241 dyykprvtkp srsvdaydsy wesrkpplka slslrkepva tdvgddlkde iirpspsllt
      301 massphgspd vlppaspsng pallrgtyfs tqddvdlytd sepratyrrq dalrpdvwll
      361 rndahslyhk rsppakesal skcqscglsc ssslcqrcds lltcppaskp safpskasth
      421 dslahgaslr ekypgqtqgl drlphlhsks kpsttptsrc gfcnrpgatn tctqcskvsc
      481 daclsayhyd pcykkselhk fmpnnqlnyk stqlshlvyr
//
LOCUS       NP_001182179             288 aa            linear   PRI 27-APR-2025
DEFINITION  aprataxin isoform h [Homo sapiens].
ACCESSION   NP_001182179
VERSION     NP_001182179.2
DBSOURCE    REFSEQ: accession NM_001195250.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Apr 23, 2019 this sequence version replaced NP_001182179.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (8) differs in the 5' UTR and has
            multiple differences in the coding region but maintains the reading
            frame, compared to variant 1. This variant encodes isoform h, which
            is shorter than isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.244812.1,
                                           SRR1803615.59668.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..288
                     /product="aprataxin isoform h"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=32994
     Region          3..>44
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Region          110..211
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(204,206,208..210)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            206
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          229..288
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..288
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001195250.2:67..933"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS75827.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqefeeea knpglethrk
       61 rkrsgnsdsi erdaaqeaea gtglepgsns gqcsvplkkg kdapikkesl ghwsqglkis
      121 mqdpkmqvyk deqvvvikdk ypkaryhwlv lpwtsisslk avarehlell khmhtvgekv
      181 ivdfagsskl rfrlgyhaip smshvhlhvi sqdfdspclk nkkhwnsfnt eyflesqavi
      241 emvqeagrvt vrdgmpellk lplrchecqq llpsipqlke hlrkhwtq
//
LOCUS       NP_620689                562 aa            linear   PRI 27-APR-2025
DEFINITION  homeobox protein ARX [Homo sapiens].
ACCESSION   NP_620689
VERSION     NP_620689.1
DBSOURCE    REFSEQ: accession NM_139058.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Gras,M., Heide,S., Keren,B., Valence,S., Garel,C., Whalen,S.,
            Jansen,A.C., Keymolen,K., Stouffs,K., Jennesson,M., Poirsier,C.,
            Lesca,G., Depienne,C., Nava,C., Rastetter,A., Curie,A., Cuisset,L.,
            Des Portes,V., Milh,M., Charles,P., Mignot,C. and Heron,D.
  TITLE     Further characterisation of ARX-related disorders in females due to
            inherited or de novo variants
  JOURNAL   J Med Genet 61 (2), 103-108 (2024)
   PUBMED   37879892
  REMARK    GeneRIF: Further characterisation of ARX-related disorders in
            females due to inherited or de novo variants.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Neyaz,A., Crotty,R., Rickelt,S., Pankaj,A., Stojanova,M.,
            Michelakos,T.P., Sekigami,Y., Kontos,F., Parrack,P.H., Patil,D.T.,
            Heaphy,C.M., Ferrone,C.R. and Deshpande,V.
  TITLE     Predicting recurrence in pancreatic neuroendocrine tumours: role of
            ARX and alternative lengthening of telomeres (ALT)
  JOURNAL   Histopathology 83 (4), 546-558 (2023)
   PUBMED   37455385
  REMARK    GeneRIF: Predicting recurrence in pancreatic neuroendocrine
            tumours: role of ARX and alternative lengthening of telomeres
            (ALT).
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Poeta,L., Malacarne,M., Padula,A., Drongitis,D., Verrillo,L.,
            Lioi,M.B., Chiariello,A.M., Bianco,S., Nicodemi,M., Piccione,M.,
            Salzano,E., Coviello,D. and Miano,M.G.
  TITLE     Further Delineation of Duplications of ARX Locus Detected in Male
            Patients with Varying Degrees of Intellectual Disability
  JOURNAL   Int J Mol Sci 23 (6), 3084 (2022)
   PUBMED   35328505
  REMARK    GeneRIF: Further Delineation of Duplications of ARX Locus Detected
            in Male Patients with Varying Degrees of Intellectual Disability.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Fujita,Y., Kozawa,J., Fukui,K., Iwahashi,H., Eguchi,H. and
            Shimomura,I.
  TITLE     Increased NKX6.1 expression and decreased ARX expression in alpha
            cells accompany reduced beta-cell volume in human subjects
  JOURNAL   Sci Rep 11 (1), 17796 (2021)
   PUBMED   34493754
  REMARK    GeneRIF: Increased NKX6.1 expression and decreased ARX expression
            in alpha cells accompany reduced beta-cell volume in human
            subjects.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Poeta,L., Padula,A., Lioi,M.B., van Bokhoven,H. and Miano,M.G.
  TITLE     Analysis of a Set of KDM5C Regulatory Genes Mutated in
            Neurodevelopmental Disorders Identifies Temporal Coexpression Brain
            Signatures
  JOURNAL   Genes (Basel) 12 (7), 1088 (2021)
   PUBMED   34356104
  REMARK    GeneRIF: Analysis of a Set of KDM5C Regulatory Genes Mutated in
            Neurodevelopmental Disorders Identifies Temporal Coexpression Brain
            Signatures.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Jemaa,L.B., des Portes,V., Zemni,R., Mrad,R., Maazoul,F.,
            Beldjord,C., Chaabouni,H. and Chelly,J.
  TITLE     Refined 2.7 centimorgan locus in Xp21.3-22.1 for a nonspecific
            X-linked mental retardation gene (MRX54)
  JOURNAL   Am J Med Genet 85 (3), 276-282 (1999)
   PUBMED   10398243
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Hane,B., Schroer,R.J., Arena,J.F., Lubs,H.A., Schwartz,C.E. and
            Stevenson,R.E.
  TITLE     Nonsyndromic X-linked mental retardation: review and mapping of
            MRX29 to Xp21
  JOURNAL   Clin Genet 50 (4), 176-183 (1996)
   PUBMED   9001795
  REMARK    Review article
REFERENCE   8  (residues 1 to 562)
  AUTHORS   Claes,S., Gu,X.X., Legius,E., Lorenzetti,E., Marynen,P.,
            Fryns,J.P., Cassiman,J.J. and Raeymaekers,P.
  TITLE     Linkage analysis in three families with nonspecific X-linked mental
            retardation
  JOURNAL   Am J Med Genet 64 (1), 137-146 (1996)
   PUBMED   8826464
REFERENCE   9  (residues 1 to 562)
  AUTHORS   Holinski-Feder,E., Golla,A., Rost,I., Seidel,H., Rittinger,O. and
            Meindl,A.
  TITLE     Regional localization of two MRX genes to Xq28 (MRX28) and to
            Xp11.4-Xp22.12 (MRX33)
  JOURNAL   Am J Med Genet 64 (1), 125-130 (1996)
   PUBMED   8826462
REFERENCE   10 (residues 1 to 562)
  AUTHORS   Schutz,C.K., Ives,E.J., Chalifoux,M., MacLaren,L., Farrell,S.,
            Robinson,P.D., White,B.N. and Holden,J.J.
  TITLE     Regional localization of an X-linked mental retardation gene to
            Xp21.1-Xp22.13 (MRX38)
  JOURNAL   Am J Med Genet 64 (1), 89-96 (1996)
   PUBMED   8826457
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002504.1, BQ100952.1,
            AY038071.1, CA775911.1, BF196892.1 and AA484051.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a homeobox-containing gene expressed during
            development. The expressed protein contains two conserved domains,
            a C-peptide (or aristaless domain) and the prd-like class homeobox
            domain. It is a member of the group-II aristaless-related protein
            family whose members are expressed primarily in the central and/or
            peripheral nervous system. This gene is thought to be involved in
            CNS development. Expansion of a polyalanine tract and other
            mutations in this gene cause X-linked cognitive disability and
            epilepsy. [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY038071.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379044.5/ ENSP00000368332.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.3"
     Protein         1..562
                     /product="homeobox protein ARX"
                     /note="cancer/testis antigen 121; aristaless-related
                     homeobox, X-linked"
                     /calculated_mol_wt=58029
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QS3.1)"
     Region          50..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QS3.1)"
     Region          102..111
                     /region_name="GCG-encoded polyalanine repeat"
                     /note="GCG-encoded 10A repeat"
     Region          118..255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QS3.1)"
     Region          329..385
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          526..544
                     /region_name="OAR"
                     /note="OAR motif; pfam03826"
                     /db_xref="CDD:461067"
     Region          530..543
                     /region_name="OAR.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QS3.1)"
     CDS             1..562
                     /gene="ARX"
                     /gene_synonym="CT121; EIEE1; ISSX; MRX29; MRX32; MRX33;
                     MRX36; MRX38; MRX43; MRX54; MRX76; MRX87; MRXS1; PRTS"
                     /coded_by="NM_139058.3:229..1917"
                     /db_xref="CCDS:CCDS14215.1"
                     /db_xref="GeneID:170302"
                     /db_xref="HGNC:HGNC:18060"
                     /db_xref="MIM:300382"
ORIGIN      
        1 msnqyqeegc serpecksks ptllssycid silgrrspck mrllgaaqsl papltsradp
       61 ekavqgspks ssapfeaelh lppklrrlyg pgggrllqga aaaaaaaaaa aaaaatatag
      121 prgeappppp ptarpgerpd gagaaaaaaa aaaaawdtlk isqapqvsis rsksyrenga
      181 pfvppppald elggpggvth peerlgvagg pgsapaaggg tgteddeeel ledeededee
      241 eelleddeee lleddarall keprrcpvaa tgavaaaaaa avateggels pkeelllhpe
      301 daegkdgeds vclsagsdse egllkrkqrr yrttftsyql eelerafqkt hypdvftree
      361 lamrldltea rvqvwfqnrr akwrkrekag aqthppglpf pgplsathpl spyldaspfp
      421 phhpaldsaw taaaaaaaaa fpslppppgs aslppsgapl glstflgaav frhpafispa
      481 fgrlfstmap ltsastaaal lrqptpaveg avasgaladp ataaadrras siaalrlkak
      541 ehaaqltqln ilpgtstgke vc
//
LOCUS       NP_064574                101 aa            linear   PRI 27-APR-2025
DEFINITION  transcription and mRNA export factor ENY2 isoform 1 [Homo sapiens].
ACCESSION   NP_064574
VERSION     NP_064574.1
DBSOURCE    REFSEQ: accession NM_020189.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Li,W., Atanassov,B.S., Lan,X., Mohan,R.D., Swanson,S.K.,
            Farria,A.T., Florens,L., Washburn,M.P., Workman,J.L. and
            Dent,S.Y.R.
  TITLE     Cytoplasmic ATXN7L3B Interferes with Nuclear Functions of the SAGA
            Deubiquitinase Module
  JOURNAL   Mol Cell Biol 36 (22), 2855-2866 (2016)
   PUBMED   27601583
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Atanassov,B.S., Mohan,R.D., Lan,X., Kuang,X., Lu,Y., Lin,K.,
            McIvor,E., Li,W., Zhang,Y., Florens,L., Byrum,S.D.,
            Mackintosh,S.G., Calhoun-Davis,T., Koutelou,E., Wang,L., Tang,D.G.,
            Tackett,A.J., Washburn,M.P., Workman,J.L. and Dent,S.Y.
  TITLE     ATXN7L3 and ENY2 Coordinate Activity of Multiple H2B
            Deubiquitinases Important for Cellular Proliferation and Tumor
            Growth
  JOURNAL   Mol Cell 62 (4), 558-571 (2016)
   PUBMED   27132940
  REMARK    GeneRIF: ATXN7L3 and ENY2 orchestrate activities of multiple
            deubiquitinating enzymes, including USP27x and USP51, and that
            imbalances in these activities likely potentiate human diseases
            including cancer.
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   7  (residues 1 to 101)
  AUTHORS   Georgieva,S., Nabirochkina,E., Dilworth,F.J., Eickhoff,H.,
            Becker,P., Tora,L., Georgiev,P. and Soldatov,A.
  TITLE     The novel transcription factor e(y)2 interacts with TAF(II)40 and
            potentiates transcription activation on chromatin templates
  JOURNAL   Mol Cell Biol 21 (15), 5223-5231 (2001)
   PUBMED   11438676
REFERENCE   8  (residues 1 to 101)
  AUTHORS   Brand,M., Moggs,J.G., Oulad-Abdelghani,M., Lejeune,F.,
            Dilworth,F.J., Stevenin,J., Almouzni,G. and Tora,L.
  TITLE     UV-damaged DNA-binding protein in the TFTC complex links DNA damage
            recognition to nucleosome acetylation
  JOURNAL   EMBO J 20 (12), 3187-3196 (2001)
   PUBMED   11406595
REFERENCE   9  (residues 1 to 101)
  AUTHORS   Brand,M., Yamamoto,K., Staub,A. and Tora,L.
  TITLE     Identification of TATA-binding protein-free TAFII-containing
            complex subunits suggests a role in nucleosome acetylation and
            signal transduction
  JOURNAL   J Biol Chem 274 (26), 18285-18289 (1999)
   PUBMED   10373431
REFERENCE   10 (residues 1 to 101)
  AUTHORS   Wieczorek,E., Brand,M., Jacq,X. and Tora,L.
  TITLE     Function of TAF(II)-containing complex without TBP in transcription
            by RNA polymerase II
  JOURNAL   Nature 393 (6681), 187-191 (1998)
   PUBMED   9603525
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF173296.1, AK095651.1 and BU737295.1.
            
            Transcript Variant: This variant (1) encodes the longer protein
            (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA292445.1, SRR1660805.187602.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000521688.6/ ENSP00000429986.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q23.1"
     Protein         1..101
                     /product="transcription and mRNA export factor ENY2
                     isoform 1"
                     /note="enhancer of yellow 2 transcription factor homolog;
                     transcription and mRNA export factor ENY2; enhancer of
                     yellow 2 homolog"
                     /calculated_mol_wt=11397
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NPA8.1)"
     Region          16..94
                     /region_name="EnY2"
                     /note="Transcription factor e(y)2; pfam10163"
                     /db_xref="CDD:462972"
     CDS             1..101
                     /gene="ENY2"
                     /gene_synonym="DC6; e(y)2; Sus1"
                     /coded_by="NM_020189.6:123..428"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43762.1"
                     /db_xref="GeneID:56943"
                     /db_xref="HGNC:HGNC:24449"
                     /db_xref="MIM:619015"
ORIGIN      
        1 mvvskmnkda qmraainqkl ietgererlk ellrakliec gwkdqlkahc kevikekgle
       61 hvtvddlvae itpkgralvp dsvkkellqr irtflaqhas l
//
LOCUS       NP_004536                 58 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 [Homo
            sapiens].
ACCESSION   NP_004536
VERSION     NP_004536.3
DBSOURCE    REFSEQ: accession NM_004545.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 58)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 58)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 58)
  AUTHORS   Guo,R., Zong,S., Wu,M., Gu,J. and Yang,M.
  TITLE     Architecture of Human Mitochondrial Respiratory Megacomplex
            I2III2IV2
  JOURNAL   Cell 170 (6), 1247-1257 (2017)
   PUBMED   28844695
REFERENCE   4  (residues 1 to 58)
  AUTHORS   Stroud,D.A., Surgenor,E.E., Formosa,L.E., Reljic,B., Frazier,A.E.,
            Dibley,M.G., Osellame,L.D., Stait,T., Beilharz,T.H., Thorburn,D.R.,
            Salim,A. and Ryan,M.T.
  TITLE     Accessory subunits are integral for assembly and function of human
            mitochondrial complex I
  JOURNAL   Nature 538 (7623), 123-126 (2016)
   PUBMED   27626371
REFERENCE   5  (residues 1 to 58)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   6  (residues 1 to 58)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   7  (residues 1 to 58)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
REFERENCE   8  (residues 1 to 58)
  AUTHORS   Emahazion,T., Beskow,A., Gyllensten,U. and Brookes,A.J.
  TITLE     Intron based radiation hybrid mapping of 15 complex I genes of the
            human electron transport chain
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 115-119 (1998)
   PUBMED   9763677
REFERENCE   9  (residues 1 to 58)
  AUTHORS   Ton,C., Hwang,D.M., Dempsey,A.A. and Liew,C.C.
  TITLE     Identification and primary structure of five human NADH-ubiquinone
            oxidoreductase subunits
  JOURNAL   Biochem Biophys Res Commun 241 (2), 589-594 (1997)
   PUBMED   9425316
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM052981.1 and BX476462.1.
            
            On Oct 20, 2018 this sequence version replaced NP_004536.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU960614.1, CB106658.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2153427
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000605997.6/
                                                  ENSP00000475170.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..58
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..58
                     /product="NADH dehydrogenase [ubiquinone] 1 beta
                     subcomplex subunit 1"
                     /note="complex I MNLL subunit; complex I-MNLL;
                     NADH-ubiquinone oxidoreductase MNLL subunit; NADH
                     dehydrogenase (ubiquinone) 1 beta subcomplex, 1, 7kDa"
                     /calculated_mol_wt=6830
     Region          3..58
                     /region_name="NADH_oxidored"
                     /note="MNLL subunit; pfam08040"
                     /db_xref="CDD:462345"
     Site            11..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75438.1)"
     CDS             1..58
                     /gene="NDUFB1"
                     /gene_synonym="CI-MNLL; CI-SGDH; MNLL"
                     /coded_by="NM_004545.4:71..247"
                     /db_xref="CCDS:CCDS9901.2"
                     /db_xref="GeneID:4707"
                     /db_xref="HGNC:HGNC:7695"
                     /db_xref="MIM:603837"
ORIGIN      
        1 mvnllqivrd hwvhvlvpmg fvigcyldrk sderltafrn ksmlfkrelq pseevtwk
//
LOCUS       NP_001075                738 aa            linear   PRI 27-APR-2025
DEFINITION  multifunctional procollagen lysine hydroxylase and
            glycosyltransferase LH3 precursor [Homo sapiens].
ACCESSION   NP_001075
VERSION     NP_001075.1
DBSOURCE    REFSEQ: accession NM_001084.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Ding,M., Wang,C., Hu,J., She,J., Shi,R., Liu,Y., Sun,Q., Xu,H.,
            Zhou,G., Wu,W. and Xia,H.
  TITLE     PLOD3 facilitated T cell activation in the colorectal tumor
            microenvironment and liver metastasis by the TNF-alpha/ NF-kappaB
            pathway
  JOURNAL   J Transl Med 22 (1), 30 (2024)
   PUBMED   38184566
  REMARK    GeneRIF: PLOD3 facilitated T cell activation in the colorectal
            tumor microenvironment and liver metastasis by the TNF-alpha/
            NF-kappaB pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Ishikawa,Y., Taga,Y., Coste,T., Tufa,S.F., Keene,D.R., Mizuno,K.,
            Tournier-Lasserve,E. and Gould,D.B.
  TITLE     Lysyl hydroxylase 3-mediated post-translational modifications are
            required for proper biosynthesis of collagen alpha1alpha1alpha2(IV)
  JOURNAL   J Biol Chem 298 (12), 102713 (2022)
   PUBMED   36403858
  REMARK    GeneRIF: Lysyl hydroxylase 3-mediated post-translational
            modifications are required for proper biosynthesis of collagen
            alpha1alpha1alpha2(IV).
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Li,W.H., Huang,K., Wen,F.B., Cui,G.H., Guo,H.Z. and Zhao,S.
  TITLE     PLOD3 regulates the expression of YAP1 to affect the progression of
            non-small cell lung cancer via the PKCdelta/CDK1/LIMD1 signaling
            pathway
  JOURNAL   Lab Invest 102 (4), 440-451 (2022)
   PUBMED   35039611
  REMARK    GeneRIF: PLOD3 regulates the expression of YAP1 to affect the
            progression of non-small cell lung cancer via the
            PKCdelta/CDK1/LIMD1 signaling pathway.
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Shi,J., Bao,M., Wang,W., Wu,X., Li,Y., Zhao,C. and Liu,W.
  TITLE     Integrated Profiling Identifies PLOD3 as a Potential Prognostic and
            Immunotherapy Relevant Biomarker in Colorectal Cancer
  JOURNAL   Front Immunol 12, 722807 (2021)
   PUBMED   34646265
  REMARK    GeneRIF: Integrated Profiling Identifies PLOD3 as a Potential
            Prognostic and Immunotherapy Relevant Biomarker in Colorectal
            Cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Gong,S., Duan,Y., Wu,C., Osterhoff,G., Schopow,N. and
            Kallendrusch,S.
  TITLE     A Human Pan-Cancer System Analysis of Procollagen-Lysine,
            2-Oxoglutarate 5-Dioxygenase 3 (PLOD3)
  JOURNAL   Int J Mol Sci 22 (18), 9903 (2021)
   PUBMED   34576068
  REMARK    GeneRIF: A Human Pan-Cancer System Analysis of Procollagen-Lysine,
            2-Oxoglutarate 5-Dioxygenase 3 (PLOD3).
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 738)
  AUTHORS   Ruotsalainen,H., Vanhatupa,S., Tampio,M., Sipila,L., Valtavaara,M.
            and Myllyla,R.
  TITLE     Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl
            hydroxylase 3/collagen glucosyltransferase
  JOURNAL   Matrix Biol 20 (2), 137-146 (2001)
   PUBMED   11334715
REFERENCE   7  (residues 1 to 738)
  AUTHORS   Heikkinen,J., Risteli,M., Wang,C., Latvala,J., Rossi,M.,
            Valtavaara,M. and Myllyla,R.
  TITLE     Lysyl hydroxylase 3 is a multifunctional protein possessing
            collagen glucosyltransferase activity
  JOURNAL   J Biol Chem 275 (46), 36158-36163 (2000)
   PUBMED   10934207
REFERENCE   8  (residues 1 to 738)
  AUTHORS   Rautavuoma,K., Passoja,K., Helaakoski,T. and Kivirikko,K.I.
  TITLE     Complete exon-intron organization of the gene for human lysyl
            hydroxylase 3 (LH3)
  JOURNAL   Matrix Biol 19 (1), 73-79 (2000)
   PUBMED   10686427
REFERENCE   9  (residues 1 to 738)
  AUTHORS   Passoja,K., Rautavuoma,K., Ala-Kokko,L., Kosonen,T. and
            Kivirikko,K.I.
  TITLE     Cloning and characterization of a third human lysyl hydroxylase
            isoform
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10482-10486 (1998)
   PUBMED   9724729
REFERENCE   10 (residues 1 to 738)
  AUTHORS   Valtavaara,M., Szpirer,C., Szpirer,J. and Myllyla,R.
  TITLE     Primary structure, tissue distribution, and chromosomal
            localization of a novel isoform of lysyl hydroxylase (lysyl
            hydroxylase 3)
  JOURNAL   J Biol Chem 273 (21), 12881-12886 (1998)
   PUBMED   9582318
  REMARK    Erratum:[J Biol Chem 2000 Jul 7;275(27):20956]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC011674.2, AC004876.2 and
            AL049952.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a membrane-bound
            homodimeric enzyme that is localized to the cisternae of the rough
            endoplasmic reticulum. The enzyme (cofactors iron and ascorbate)
            catalyzes the hydroxylation of lysyl residues in collagen-like
            peptides. The resultant hydroxylysyl groups are attachment sites
            for carbohydrates in collagen and thus are critical for the
            stability of intermolecular crosslinks. Some patients with
            Ehlers-Danlos syndrome type VIB have deficiencies in lysyl
            hydroxylase activity. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011674.2, AF068229.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000223127.8/ ENSP00000223127.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..738
                     /product="multifunctional procollagen lysine hydroxylase
                     and glycosyltransferase LH3 precursor"
                     /EC_number="1.14.11.4"
                     /EC_number="2.4.1.50"
                     /EC_number="2.4.1.66"
                     /note="lysyl hydroxylase 3; lysine hydroxylase 3; lysyl
                     hydroxlase 3; multifunctional procollagen lysine
                     hydroxylase and glycosyltransferase LH3"
                     /calculated_mol_wt=82384
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2420
     mat_peptide     25..738
                     /product="multifunctional procollagen lysine hydroxylase
                     and glycosyltransferase LH3"
                     /calculated_mol_wt=82384
     Region          25..290
                     /region_name="Required for glycosyltransferase activity.
                     /evidence=ECO:0000269|PubMed:18298658,
                     ECO:0000269|PubMed:30089812"
                     /note="propagated from UniProtKB/Swiss-Prot (O60568.1)"
     Region          37..266
                     /region_name="GT_LH3"
                     /note="catalytic glycosyltransferase (GT) domain found in
                     lysyl hydroxylase 3 (LH3) and similar proteins; cd23002"
                     /db_xref="CDD:438558"
     Site            order(44..46,75,89,112..113,115,253,255)
                     /site_type="other"
                     /note="UDP binding site [chemical binding]"
                     /db_xref="CDD:438558"
     Site            63
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30089812,
                     ECO:0007744|PDB:6FXY; propagated from UniProtKB/Swiss-Prot
                     (O60568.1)"
     Site            order(112,115,253)
                     /site_type="other"
                     /note="Mn binding site [ion binding]"
                     /db_xref="CDD:438558"
     Region          295..520
                     /region_name="Accessory region.
                     /evidence=ECO:0000269|PubMed:30089812"
                     /note="propagated from UniProtKB/Swiss-Prot (O60568.1)"
     Site            548
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30089812,
                     ECO:0007744|PDB:6FXY; propagated from UniProtKB/Swiss-Prot
                     (O60568.1)"
     Region          573..736
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     Region          672..715
                     /region_name="Important for dimerization.
                     /evidence=ECO:0000269|PubMed:30089812"
                     /note="propagated from UniProtKB/Swiss-Prot (O60568.1)"
     CDS             1..738
                     /gene="PLOD3"
                     /gene_synonym="BCARD; LH3"
                     /coded_by="NM_001084.5:308..2524"
                     /db_xref="CCDS:CCDS5715.1"
                     /db_xref="GeneID:8985"
                     /db_xref="HGNC:HGNC:9083"
                     /db_xref="MIM:603066"
ORIGIN      
        1 mtssgpgprf llllplllpp aasasdrprg rdpvnpekll vitvataete gylrflrsae
       61 ffnytvrtlg lgeewrggdv artvgggqkv rwlkkemeky adredmiimf vdsydvilag
      121 sptellkkfv qsgsrllfsa esfcwpewgl aeqypevgtg krflnsggfi gfattihqiv
      181 rqwkykdddd dqlfytrlyl dpglreklsl nldhksrifq nlngaldevv lkfdrnrvri
      241 rnvaydtlpi vvhgngptkl qlnylgnyvp ngwtpeggcg fcnqdrrtlp ggqppprvfl
      301 avfveqptpf lprflqrlll ldyppdrvtl flhnnevfhe phiadswpql qdhfsavklv
      361 gpeealspge ardmamdlcr qdpecefyfs ldadavltnl qtlrilieen rkviapmlsr
      421 hgklwsnfwg alspdeyyar sedyvelvqr krvgvwnvpy isqayvirgd tlrmelpqrd
      481 vfsgsdtdpd mafcksfrdk giflhlsnqh efgrllatsr ydtehlhpdl wqifdnpvdw
      541 keqyihenys ralegegive qpcpdvywfp llseqmcdel vaemehygqw sggrhedsrl
      601 aggyenvptv dihmkqvgye dqwlqllrty vgpmteslfp gyhtkaravm nfvvryrpde
      661 qpslrphhds stftlnvaln hkgldyeggg crflrydcvi ssprkgwall hpgrlthyhe
      721 glpttwgtry imvsfvdp
//
LOCUS       NP_006392                251 aa            linear   PRI 27-APR-2025
DEFINITION  acidic leucine-rich nuclear phosphoprotein 32 family member B [Homo
            sapiens].
ACCESSION   NP_006392
VERSION     NP_006392.1
DBSOURCE    REFSEQ: accession NM_006401.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Staller,E., Carrique,L., Swann,O.C., Fan,H., Keown,J.R.,
            Sheppard,C.M., Barclay,W.S., Grimes,J.M. and Fodor,E.
  TITLE     Structures of H5N1 influenza polymerase with ANP32B reveal
            mechanisms of genome replication and host adaptation
  JOURNAL   Nat Commun 15 (1), 4123 (2024)
   PUBMED   38750014
  REMARK    GeneRIF: Structures of H5N1 influenza polymerase with ANP32B reveal
            mechanisms of genome replication and host adaptation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Zhou,C., Ma,H., Yu,W., Zhou,Y., Zhang,X., Meng,Y., Chen,C.,
            Zhang,J. and Shi,G.
  TITLE     ANP32B inhibition suppresses the growth of prostate cancer cells by
            regulating c-Myc signaling
  JOURNAL   Biochem Biophys Res Commun 698, 149543 (2024)
   PUBMED   38266312
  REMARK    GeneRIF: ANP32B inhibition suppresses the growth of prostate cancer
            cells by regulating c-Myc signaling.
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Mandemaker,I.K., Fessler,E., Corujo,D., Kotthoff,C., Wegerer,A.,
            Rouillon,C., Buschbeck,M., Jae,L.T., Mattiroli,F. and Ladurner,A.G.
  TITLE     The histone chaperone ANP32B regulates chromatin incorporation of
            the atypical human histone variant macroH2A
  JOURNAL   Cell Rep 42 (10), 113300 (2023)
   PUBMED   37858472
  REMARK    GeneRIF: The histone chaperone ANP32B regulates chromatin
            incorporation of the atypical human histone variant macroH2A.
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Li,T., Wang,N., Li,S., Yan,H., Gao,S., Gao,W. and Xu,R.
  TITLE     ANP32B promotes lung cancer progression by regulating VDAC1
  JOURNAL   Gene 859, 147200 (2023)
   PUBMED   36642319
  REMARK    GeneRIF: ANP32B promotes lung cancer progression by regulating
            VDAC1.
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Matilla,A. and Radrizzani,M.
  TITLE     The Anp32 family of proteins containing leucine-rich repeats
  JOURNAL   Cerebellum 4 (1), 7-18 (2005)
   PUBMED   15895553
  REMARK    Review article
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Gallouzi,I.E. and Steitz,J.A.
  TITLE     Delineation of mRNA export pathways by the use of cell-permeable
            peptides
  JOURNAL   Science 294 (5548), 1895-1901 (2001)
   PUBMED   11729309
  REMARK    Erratum:[Science 2002 Apr 5;296(5565):47]
REFERENCE   8  (residues 1 to 251)
  AUTHORS   Brennan,C.M., Gallouzi,I.E. and Steitz,J.A.
  TITLE     Protein ligands to HuR modulate its interaction with target mRNAs
            in vivo
  JOURNAL   J Cell Biol 151 (1), 1-14 (2000)
   PUBMED   11018049
REFERENCE   9  (residues 1 to 251)
  AUTHORS   Mencinger,M., Panagopoulos,I., Contreras,J.A., Mitelman,F. and
            Aman,P.
  TITLE     Expression analysis and chromosomal mapping of a novel human gene,
            APRIL, encoding an acidic protein rich in leucines
  JOURNAL   Biochim Biophys Acta 1395 (2), 176-180 (1998)
   PUBMED   9473664
REFERENCE   10 (residues 1 to 251)
  AUTHORS   Zhu,L., Perlaky,L., Henning,D. and Valdez,B.C.
  TITLE     Cloning and characterization of a new silver-stainable protein
            SSP29, a member of the LRR family
  JOURNAL   Biochem Mol Biol Int 42 (5), 927-935 (1997)
   PUBMED   9285060
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AW296974.1, BC019658.1 and BP395780.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.903297.1,
                                           SRR3476690.857482.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000339399.5/ ENSP00000345848.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.33"
     Protein         1..251
                     /product="acidic leucine-rich nuclear phosphoprotein 32
                     family member B"
                     /note="acidic protein rich in leucines; silver-stainable
                     protein SSP29; putative HLA-DR-associated protein I-2;
                     acidic (leucine-rich) nuclear phosphoprotein 32 family,
                     member B"
                     /calculated_mol_wt=28657
     Region          16..40
                     /region_name="LRR 1.
                     /evidence=ECO:0000269|PubMed:20538007"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92688.1)"
     Region          43..64
                     /region_name="LRR 2.
                     /evidence=ECO:0000269|PubMed:20538007"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92688.1)"
     Region          65..84
                     /region_name="LRR 3.
                     /evidence=ECO:0000269|PubMed:20538007"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92688.1)"
     Region          <71..146
                     /region_name="LRR_9"
                     /note="Leucine-rich repeat; pfam14580"
                     /db_xref="CDD:405295"
     Site            86
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92688.1)"
     Region          89..110
                     /region_name="LRR 4.
                     /evidence=ECO:0000269|PubMed:20538007"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92688.1)"
     Region          90..113
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275382"
     Region          115..141
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275382"
     Region          149..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92688.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EST6; propagated from
                     UniProtKB/Swiss-Prot (Q92688.1)"
     Region          239..242
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:17178712"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92688.1)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17178712,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92688.1)"
     CDS             1..251
                     /gene="ANP32B"
                     /gene_synonym="APRIL; PHAPI2; SSP29"
                     /coded_by="NM_006401.3:216..971"
                     /db_xref="CCDS:CCDS6732.1"
                     /db_xref="GeneID:10541"
                     /db_xref="HGNC:HGNC:16677"
                     /db_xref="MIM:619823"
ORIGIN      
        1 mdmkrrihle lrnrtpaavr elvldncksn dgkiegltae fvnleflsli nvglisvsnl
       61 pklpklkkle lsenrifggl dmlaeklpnl thlnlsgnkl kdistleplk kleclksldl
      121 fncevtnlnd yresvfkllp qltyldgydr edqeapdsda evdgvdeeee deegedeede
      181 ddedgeeeef deeddededv egdedddevs eeeeefglde ededededee eeeggkgekr
      241 kretddeged d
//
LOCUS       NP_001020461             116 aa            linear   PRI 27-APR-2025
DEFINITION  developmental pluripotency-associated 5 protein [Homo sapiens].
ACCESSION   NP_001020461 XP_291161
VERSION     NP_001020461.1
DBSOURCE    REFSEQ: accession NM_001025290.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Taei,A., Kiani,T., Taghizadeh,Z., Moradi,S., Samadian,A.,
            Mollamohammadi,S., Sharifi-Zarchi,A., Guenther,S., Akhlaghpour,A.,
            Asgari Abibeiglou,B., Najar-Asl,M., Karamzadeh,R., Khalooghi,K.,
            Braun,T., Hassani,S.N. and Baharvand,H.
  TITLE     Temporal activation of LRH-1 and RAR-gamma in human pluripotent
            stem cells induces a functional naive-like state
  JOURNAL   EMBO Rep 21 (10), e47533 (2020)
   PUBMED   33252195
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Qian,X., Kim,J.K., Tong,W., Villa-Diaz,L.G. and Krebsbach,P.H.
  TITLE     DPPA5 Supports Pluripotency and Reprogramming by Regulating NANOG
            Turnover
  JOURNAL   Stem Cells 34 (3), 588-600 (2016)
   PUBMED   26661329
  REMARK    GeneRIF: Our study provides new insight into the function of DPPA5
            and NANOG regulation in human pluripotent stem cell .
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Aoki,T., Ohnishi,H., Oda,Y., Tadokoro,M., Sasao,M., Kato,H.,
            Hattori,K. and Ohgushi,H.
  TITLE     Generation of induced pluripotent stem cells from human
            adipose-derived stem cells without c-MYC
  JOURNAL   Tissue Eng Part A 16 (7), 2197-2206 (2010)
   PUBMED   20146561
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Tian,X., Pascal,G., Fouchecourt,S., Pontarotti,P. and Monget,P.
  TITLE     Gene birth, death, and divergence: the different scenarios of
            reproduction-related gene evolution
  JOURNAL   Biol Reprod 80 (4), 616-621 (2009)
   PUBMED   19129511
  REMARK    Review article
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Dansranjavin,T., Krehl,S., Mueller,T., Mueller,L.P., Schmoll,H.J.
            and Dammann,R.H.
  TITLE     The role of promoter CpG methylation in the epigenetic control of
            stem cell related genes during differentiation
  JOURNAL   Cell Cycle 8 (6), 916-924 (2009)
   PUBMED   19221495
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Pierre,A., Gautier,M., Callebaut,I., Bontoux,M., Jeanpierre,E.,
            Pontarotti,P. and Monget,P.
  TITLE     Atypical structure and phylogenomic evolution of the new eutherian
            oocyte- and embryo-expressed KHDC1/DPPA5/ECAT1/OOEP gene family
  JOURNAL   Genomics 90 (5), 583-594 (2007)
   PUBMED   17913455
REFERENCE   7  (residues 1 to 116)
  AUTHORS   Lagarkova,M.A., Volchkov,P.Y., Lyakisheva,A.V., Philonenko,E.S. and
            Kiselev,S.L.
  TITLE     Diverse epigenetic profile of novel human embryonic stem cell lines
  JOURNAL   Cell Cycle 5 (4), 416-420 (2006)
   PUBMED   16479162
REFERENCE   8  (residues 1 to 116)
  AUTHORS   Western,P., Maldonado-Saldivia,J., van den Bergen,J., Hajkova,P.,
            Saitou,M., Barton,S. and Surani,M.A.
  TITLE     Analysis of Esg1 expression in pluripotent cells and the germline
            reveals similarities with Oct4 and Sox2 and differences between
            human pluripotent cell lines
  JOURNAL   Stem Cells 23 (10), 1436-1442 (2005)
   PUBMED   16166252
REFERENCE   9  (residues 1 to 116)
  AUTHORS   Adjaye,J., Huntriss,J., Herwig,R., BenKahla,A., Brink,T.C.,
            Wierling,C., Hultschig,C., Groth,D., Yaspo,M.L., Picton,H.M.,
            Gosden,R.G. and Lehrach,H.
  TITLE     Primary differentiation in the human blastocyst: comparative
            molecular portraits of inner cell mass and trophectoderm cells
  JOURNAL   Stem Cells 23 (10), 1514-1525 (2005)
   PUBMED   16081659
REFERENCE   10 (residues 1 to 116)
  AUTHORS   Kim,S.K., Suh,M.R., Yoon,H.S., Lee,J.B., Oh,S.K., Moon,S.Y.,
            Moon,S.H., Lee,J.Y., Hwang,J.H., Cho,W.J. and Kim,K.S.
  TITLE     Identification of developmental pluripotency associated 5
            expression in human pluripotent stem cells
  JOURNAL   Stem Cells 23 (4), 458-462 (2005)
   PUBMED   15790765
  REMARK    GeneRIF: Dppa5 is specifically and differentially expressed in
            human cells that have pluripotency and can be used as a marker of
            pluripotent stem cells.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC137549.1 and AI365263.1.
            
            On Jul 13, 2005 this sequence version replaced XP_291161.1.
            
            Summary: This gene encodes a protein that may function in the
            control of cell pluripotency and early embryogenesis. Expression of
            this gene is a specific marker for pluripotent stem cells.
            Pseudogenes of this gene are located on the short arm of chromosome
            10 and the long arm of chromosomes 14 and 19. [provided by RefSeq,
            Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX092581.1, BC137549.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370370.4/ ENSP00000359396.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..116
                     /product="developmental pluripotency-associated 5 protein"
                     /note="embryonal stem cell specific gene 1"
                     /calculated_mol_wt=13367
     Region          10..94
                     /region_name="MOEP19"
                     /note="KH-like RNA-binding domain; pfam16005"
                     /db_xref="CDD:464969"
     CDS             1..116
                     /gene="DPPA5"
                     /gene_synonym="ESG1"
                     /coded_by="NM_001025290.3:52..402"
                     /db_xref="CCDS:CCDS34483.1"
                     /db_xref="GeneID:340168"
                     /db_xref="HGNC:HGNC:19201"
                     /db_xref="MIM:611111"
ORIGIN      
        1 mgtlparrhi ppwvkvpedl kdpevfqvqt rllkaifgpd gsripyieqv skamlelkal
       61 essdltevvv ygsylyklrt kwmlqsmaew hrqrqergml klaeamnale lgpwmk
//
LOCUS       NP_003430                563 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein with KRAB and SCAN domains 1 isoform a [Homo
            sapiens].
ACCESSION   NP_003430 XP_168302 XP_374496
VERSION     NP_003430.1
DBSOURCE    REFSEQ: accession NM_003439.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Song,R., Ma,S., Xu,J., Ren,X., Guo,P., Liu,H., Li,P., Yin,F.,
            Liu,M., Wang,Q., Yu,L., Liu,J., Duan,B., Rahman,N.A.,
            Wolczynski,S., Li,G. and Li,X.
  TITLE     A novel polypeptide encoded by the circular RNA ZKSCAN1 suppresses
            HCC via degradation of mTOR
  JOURNAL   Mol Cancer 22 (1), 16 (2023)
   PUBMED   36691031
  REMARK    GeneRIF: A novel polypeptide encoded by the circular RNA ZKSCAN1
            suppresses HCC via degradation of mTOR.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Li,J., Bao,S., Wang,L. and Wang,R.
  TITLE     CircZKSCAN1 Suppresses Hepatocellular Carcinoma Tumorigenesis by
            Regulating miR-873-5p/Downregulation of Deleted in Liver Cancer 1
  JOURNAL   Dig Dis Sci 66 (12), 4374-4383 (2021)
   PUBMED   33439397
  REMARK    GeneRIF: CircZKSCAN1 Suppresses Hepatocellular Carcinoma
            Tumorigenesis by Regulating miR-873-5p/Downregulation of Deleted in
            Liver Cancer 1.
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 563)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 563)
  AUTHORS   Jikuya,H., Takano,J., Kikuno,R., Hirosawa,M., Nagase,T., Nomura,N.
            and Ohara,O.
  TITLE     Characterization of long cDNA clones from human adult spleen. II.
            The complete sequences of 81 cDNA clones
  JOURNAL   DNA Res 10 (1), 49-57 (2003)
   PUBMED   12693554
REFERENCE   7  (residues 1 to 563)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
REFERENCE   8  (residues 1 to 563)
  AUTHORS   Rousseau-Merck,M.F., Duro,D., Berger,R. and Thiesen,H.J.
  TITLE     Chromosomal localization of two KOX zinc finger genes on chromosome
            bands 7q21-q22
  JOURNAL   Ann Genet 38 (2), 81-84 (1995)
   PUBMED   7486829
REFERENCE   9  (residues 1 to 563)
  AUTHORS   Huebner,K., Druck,T., Croce,C.M. and Thiesen,H.J.
  TITLE     Twenty-seven nonoverlapping zinc finger cDNAs from human T cells
            map to nine different chromosomes with apparent clustering
  JOURNAL   Am J Hum Genet 48 (4), 726-740 (1991)
   PUBMED   2014798
REFERENCE   10 (residues 1 to 563)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY140376.1, AK074116.1,
            AC093619.5 and AA873735.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Nov 22, 2004 this sequence version replaced
            XP_168302.1, XP_374496.1.
            
            Summary: This gene encodes a member of the Kruppel C2H2-type
            zinc-finger family of proteins. This encoded protein may function
            as a transcription factor that regulates the expression of GABA
            type-A receptors in the brain. Transcripts from this gene have been
            shown to form stable and abundant circular RNAs. Elevated
            expression of this gene has been observed in gastric cancer and the
            encoded protein may stimulate migration and invasion of human
            gastric cancer cells. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Both variants 1 and 6 encode isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL833578.1, SRR1803613.192182.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324306.11/ ENSP00000323148.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..563
                     /product="zinc finger protein with KRAB and SCAN domains 1
                     isoform a"
                     /note="zinc finger protein 36 (KOX 18); zinc finger
                     protein 139"
                     /calculated_mol_wt=63499
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17029.3)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P17029.3)"
     Region          52..162
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P17029.3)"
     Region          227..262
                     /region_name="KRAB_A-box"
                     /note="KRAB (Kruppel-associated box) domain -A box;
                     cd07765"
                     /db_xref="CDD:143639"
     Region          257..373
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17029.3)"
     Region          355..371
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <356..537
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          379..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(379,382,395,399)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          407..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(407,410,423,427)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(435,438,451,455)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(440,442,444,446..447,450..451,454,468,470,474..475,
                     478..479,482,496,498,500,502..503,506..507,510)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          463..483
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          491..511
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          519..539
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..563
                     /gene="ZKSCAN1"
                     /gene_synonym="KOX18; PHZ-37; ZNF139; ZNF36; ZSCAN33"
                     /coded_by="NM_003439.4:220..1911"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34698.1"
                     /db_xref="GeneID:7586"
                     /db_xref="HGNC:HGNC:13101"
                     /db_xref="MIM:601260"
ORIGIN      
        1 mmtaesreat glspqaaqek dgivivkvee edeedhmwgq dstlqdtppp dpeifrqrfr
       61 rfcyqntfgp realsrlkel chqwlrpein tkeqilellv leqflsilpk elqvwlqeyr
      121 pdsgeeavtl ledleldlsg qqvpgqvhgp emlargmvpl dpvqesssfd lhheatqshf
      181 khssrkprll qsralpaahi papphegspr dqamasalft adsqamvkie dmavslilee
      241 wgcqnlarrn lsrdnrqeny gsafpqggen rneneestsk aetsedsasr gettgrsqke
      301 fgekrdqegk tgerqqknpe ektrkekrds gpaigkdkkt itgergprek gkglgrsfsl
      361 ssnfttpeev ptgtkshrcd ecgkcftrss slirhkiiht gekpyecsec gkafslnsnl
      421 vlhqrihtge kphecnecgk afshssnlil hqrihsgekp yecnecgkaf sqssdltkhq
      481 rihtgekpye csecgkafnr nsylilhrri htrekpykct kcgkaftrss tltlhhriha
      541 reraseyspa sldafgaflk scv
//
LOCUS       NP_009117               2442 aa            linear   PRI 27-APR-2025
DEFINITION  centrosome-associated protein CEP250 isoform 1 [Homo sapiens].
ACCESSION   NP_009117
VERSION     NP_009117.2
DBSOURCE    REFSEQ: accession NM_007186.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2442)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   2  (residues 1 to 2442)
  AUTHORS   Mahen,R.
  TITLE     cNap1 bridges centriole contact sites to maintain centrosome
            cohesion
  JOURNAL   PLoS Biol 20 (10), e3001854 (2022)
   PUBMED   36282799
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2442)
  AUTHORS   Zhou,J., Peng,X., Ru,Y. and Xu,J.
  TITLE     Circ_0060077 Knockdown Alleviates High-Glucose-Induced Cell
            Apoptosis, Oxidative Stress, Inflammation and Fibrosis in HK-2
            Cells via miR-145-5p/VASN Pathway
  JOURNAL   Inflammation 45 (5), 1911-1923 (2022)
   PUBMED   35729462
  REMARK    GeneRIF: Circ_0060077 Knockdown Alleviates High-Glucose-Induced
            Cell Apoptosis, Oxidative Stress, Inflammation and Fibrosis in HK-2
            Cells via miR-145-5p/VASN Pathway.
            Erratum:[Inflammation. 2023 Apr;46(2):780. doi:
            10.1007/s10753-022-01740-y. PMID: 36112240]
REFERENCE   4  (residues 1 to 2442)
  AUTHORS   Igelman,A.D., Ku,C., da Palma,M.M., Georgiou,M., Schiff,E.R.,
            Lam,B.L., Sankila,E.M., Ahn,J., Pyers,L., Vincent,A., Ferraz
            Sallum,J.M., Zein,W.M., Oh,J.K., Maldonado,R.S., Ryu,J.,
            Tsang,S.H., Gorin,M.B., Webster,A.R., Michaelides,M., Yang,P. and
            Pennesi,M.E.
  TITLE     Expanding the clinical phenotype in patients with disease causing
            variants associated with atypical Usher syndrome
  JOURNAL   Ophthalmic Genet 42 (6), 664-673 (2021)
   PUBMED   34223797
  REMARK    GeneRIF: Expanding the clinical phenotype in patients with disease
            causing variants associated with atypical Usher syndrome.
REFERENCE   5  (residues 1 to 2442)
  AUTHORS   Zeng,L., Fan,X., Wang,X., Deng,H., Zhang,X., Zhang,K., He,S.,
            Li,N., Han,Q. and Liu,Z.
  TITLE     Involvement of NEK2 and its interaction with NDC80 and CEP250 in
            hepatocellular carcinoma
  JOURNAL   BMC Med Genomics 13 (1), 158 (2020)
   PUBMED   33109182
  REMARK    GeneRIF: Involvement of NEK2 and its interaction with NDC80 and
            CEP250 in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2442)
  AUTHORS   Hirsch,D.S., Pirone,D.M. and Burbelo,P.D.
  TITLE     A new family of Cdc42 effector proteins, CEPs, function in
            fibroblast and epithelial cell shape changes
  JOURNAL   J Biol Chem 276 (2), 875-883 (2001)
   PUBMED   11035016
REFERENCE   7  (residues 1 to 2442)
  AUTHORS   Helps,N.R., Luo,X., Barker,H.M. and Cohen,P.T.
  TITLE     NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase
            localized to centrosomes, is complexed to protein phosphatase 1
  JOURNAL   Biochem J 349 (Pt 2), 509-518 (2000)
   PUBMED   10880350
REFERENCE   8  (residues 1 to 2442)
  AUTHORS   Fry,A.M., Mayor,T., Meraldi,P., Stierhof,Y.D., Tanaka,K. and
            Nigg,E.A.
  TITLE     C-Nap1, a novel centrosomal coiled-coil protein and candidate
            substrate of the cell cycle-regulated protein kinase Nek2
  JOURNAL   J Cell Biol 141 (7), 1563-1574 (1998)
   PUBMED   9647649
REFERENCE   9  (residues 1 to 2442)
  AUTHORS   Mack,G.J., Rees,J., Sandblom,O., Balczon,R., Fritzler,M.J. and
            Rattner,J.B.
  TITLE     Autoantibodies to a group of centrosomal proteins in human
            autoimmune sera reactive with the centrosome
  JOURNAL   Arthritis Rheum 41 (3), 551-558 (1998)
   PUBMED   9506584
REFERENCE   10 (residues 1 to 2442)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FO393401.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 12, 2002 this sequence version replaced NP_009117.1.
            
            Summary: This gene encodes a core centrosomal protein required for
            centriole-centriole cohesion during interphase of the cell cycle.
            The encoded protein dissociates from the centrosomes when parental
            centrioles separate at the beginning of mitosis. The protein
            associates with and is phosphorylated by NIMA-related kinase 2,
            which is also associated with the centrosome. Alternative splicing
            results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF049105.1, AF022655.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2142853 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397527.6/ ENSP00000380661.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..2442
                     /product="centrosome-associated protein CEP250 isoform 1"
                     /note="centrosomal Nek2-associated protein 1;
                     centrosome-associated protein CEP250; 250 kDa centrosomal
                     protein"
                     /calculated_mol_wt=281007
     Region          39..213
                     /region_name="Rootletin"
                     /note="Ciliary rootlet component, centrosome cohesion;
                     pfam15035"
                     /db_xref="CDD:464459"
     Region          246..>491
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          <429..1052
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          790..1552
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1259..2019
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1273..1308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BV73.2)"
     Region          1699..1725
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BV73.2)"
     Region          <1746..>2313
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1820..1839
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BV73.2)"
     Site            2138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BV73.2)"
     Site            2218
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BV73.2)"
     Region          2223..2244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BV73.2)"
     Site            2229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BV73.2)"
     Site            2252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9BV73.2)"
     Region          2307..2345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BV73.2)"
     Site            2322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BV73.2)"
     Region          2416..2442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BV73.2)"
     Site            2417
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK2.
                     /evidence=ECO:0000269|PubMed:21076410; propagated from
                     UniProtKB/Swiss-Prot (Q9BV73.2)"
     Site            2421
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK2.
                     /evidence=ECO:0000269|PubMed:21076410; propagated from
                     UniProtKB/Swiss-Prot (Q9BV73.2)"
     CDS             1..2442
                     /gene="CEP250"
                     /gene_synonym="C-NAP1; CEP2; CNAP1; CRDHL2"
                     /coded_by="NM_007186.6:452..7780"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13255.1"
                     /db_xref="GeneID:11190"
                     /db_xref="HGNC:HGNC:1859"
                     /db_xref="MIM:609689"
ORIGIN      
        1 metrspglnn mkpqslqlvl eeqvlalqqq maenqaaswr klknsqeaqq rqatlvrklq
       61 akvlqyrswc qelekrleat ggpipqrwen veepnldell vrleeeqqrc eslaevntql
      121 rlhmekadvv nkalredvek ltvdwsrard elmrkesqwq meqeffkgyl kgehgrllsl
      181 wrevvtfrrh flemksatdr dlmelkaehv rlsgslltcc lrltvgaqsr epngsgrmdg
      241 repaqlllll aktqelekea hersqeliql ksqgdlekae lqdrvtelsa lltqsqkqne
      301 dyekmikalr etveiletnh telmeheasl srnaqeekls lqqvikditq vmveegdnia
      361 qgsghensle ldssifsqfd yqdadkaltl vrsvltrrrq avqdlrqqla gcqeavnllq
      421 qqhdqweeeg kalrqrlqkl tgerdtlagq tvdlqgevds lskerellqk areelrqqle
      481 vleqeawrlr rvnvelqlqg dsaqgqkeeq qeelhlavre rerlqemlmg leakqsesls
      541 elitlreale sshlegellr qeqtevtaal araeqsiael sssentlkte vadlraaavk
      601 lsalnealal dkvglnqqll qleeenqsvc srmeaaeqar nalqvdlaea ekrrealwek
      661 nthleaqlqk aeeagaelqa dlrdiqeeke eiqkklsesr hqqeaattql eqlhqeakrq
      721 eevlaravqe kealvrekaa levrlqaver drqdlaeqlq glssakelle sslfeaqqqn
      781 svievtkgql evqiqtvtqa keviqgevrc lkleldters qaeqerdaaa rqlaqaeqeg
      841 ktaleqqkaa hekevnqlre kwekerswhq qelakalesl erekmelemr lkeqqtemea
      901 iqaqreeert qaesalcqmq letekervsl letllqtqke ladasqqler lrqdmkvqkl
      961 keqettgilq tqlqeaqrel keaarqhrdd laalqeesss llqdkmdlqk qvedlksqlv
     1021 aqddsqrlve qevqeklret qeynriqkel erekasltls lmekeqrllv lqeadsirqq
     1081 elsalrqdmq eaqgeqkels aqmellrqev kekeadflaq eaqlleelea shiteqqlra
     1141 slwaqeakaa qlqlrlrste sqlealaaeq qpgnqaqaqa qlaslysalq qalgsvcesr
     1201 pelsgggdsa psvwglepdq ngarslfkrg plltalsaea vasalhklhq dlwktqqtrd
     1261 vlrdqvqkle erltdteaek sqvhtelqdl qrqlsqnqee kskwegkqns leselmelhe
     1321 tmaslqsrlr raelqrmeaq gerellqaak enltaqvehl qaavvearaq asaagileed
     1381 lrtarsalkl kneevesere raqalqeqge lkvaqgkalq enlalltqtl aereeevetl
     1441 rgqiqelekq remqkaalel lsldlkkrnq evdlqqeqiq elekcrsvle hlpmavqere
     1501 qkltvqreqi relekdretq rnvlehqlle lekkdqmies qrgqvqdlkk qlvtleclal
     1561 eleenhhkme cqqklikele gqretqrval thltldleer sqelqaqssq ihdleshstv
     1621 larelqerdq evksqreqie elqrqkehlt qdlerrdqel mlqkeriqvl edqrtrqtki
     1681 leedleqikl slrergrelt tqrqlmqera eegkgpskaq rgslehmkli lrdkekevec
     1741 qqehihelqe lkdqleqqlq glhrkvgets lllsqreqei vvlqqqlqea reqgelkeqs
     1801 lqsqldeaqr alaqrdqele alqqeqqqaq gqeervkeka dalqgaleqa hmtlkerhge
     1861 lqdhkeqarr leeelavegr rvqaleevlg dlraesreqe kallalqqqc aeqaqeheve
     1921 tralqdswlq aqavlkerdq elealraesq ssrhqeeaar araealqeal gkahaalqgk
     1981 eqhlleqael srsleastat lqasldacqa hsrqleealr iqegeiqdqd lryqedvqql
     2041 qqalaqrdee lrhqqereql lekslaqrvq enmiqekqnl gqereeeeir glhqsvrelq
     2101 ltlaqkeqei lelretqqrn nlealphshk tspmeeqslk ldsleprlqr elerlqaalr
     2161 qteareiewr ekaqdlalsl aqtkasvssl qevamflqas vlerdseqqr lqdeleltrr
     2221 alekerlhsp gatstaelgs rgeqgvqlge vsgveaepsp dgmekqswrq rlehlqqava
     2281 rleidrsrlq rhnvqlrstl eqvererrkl kreamraaqa gsleiskata ssptqqdgrg
     2341 qknsdakcva elqkevvllq aqltlerkqk qdyitrsaqt srelaglhhs lshsllavaq
     2401 apeatvleae trrldesltq sltspgpvll hpspsttqaa sr
//
LOCUS       NP_054861                219 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-sugar pyrophosphatase isoform 1 [Homo sapiens].
ACCESSION   NP_054861
VERSION     NP_054861.2
DBSOURCE    REFSEQ: accession NM_014142.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Qian,J., Ma,Y., Tahaney,W.M., Moyer,C.L., Lanier,A., Hill,J.,
            Coleman,D., Koupaei,N., Hilsenbeck,S.G., Savage,M.I., Page,B.D.G.,
            Mazumdar,A. and Brown,P.H.
  TITLE     The novel phosphatase NUDT5 is a critical regulator of
            triple-negative breast cancer growth
  JOURNAL   Breast Cancer Res 26 (1), 23 (2024)
   PUBMED   38317231
  REMARK    GeneRIF: The novel phosphatase NUDT5 is a critical regulator of
            triple-negative breast cancer growth.
            Erratum:[Breast Cancer Res. 2024 Mar 26;26(1):53. doi:
            10.1186/s13058-024-01814-9. PMID: 38532428]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Ding,H., Wu,C., Sun,W., Zhan,Q., Huang,Y., Liao,N., Jiang,Z.,
            Wang,K. and Li,Y.
  TITLE     NUDT5-Determines the fate of head and neck squamous cell carcinoma
            cells under endoplasmic reticulum stress by catalyzing nuclear ATP
            production to promote DNA repair
  JOURNAL   Oral Oncol 141, 106397 (2023)
   PUBMED   37156197
  REMARK    GeneRIF: NUDT5-Determines the fate of head and neck squamous cell
            carcinoma cells under endoplasmic reticulum stress by catalyzing
            nuclear ATP production to promote DNA repair.
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Tan,D. and Zhang,Y.
  TITLE     Silencing of Nudix type 5 represses proliferation and invasion and
            enhances chemosensitivity of gastric carcinoma cells by affecting
            the AKT/GSK-3beta/beta-catenin pathway
  JOURNAL   Toxicol Appl Pharmacol 441, 115968 (2022)
   PUBMED   35247377
  REMARK    GeneRIF: Silencing of Nudix type 5 represses proliferation and
            invasion and enhances chemosensitivity of gastric carcinoma cells
            by affecting the AKT/GSK-3beta/beta-catenin pathway.
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Zhang,H., Zhang,L.Q., Yang,C.C., Li,J., Tian,X.Y., Li,D.N., Cui,J.
            and Cai,J.P.
  TITLE     The high expression of NUDT5 indicates poor prognosis of breast
            cancer by modulating AKT / Cyclin D signaling
  JOURNAL   PLoS One 16 (2), e0245876 (2021)
   PUBMED   33571243
  REMARK    GeneRIF: The high expression of NUDT5 indicates poor prognosis of
            breast cancer by modulating AKT / Cyclin D signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Ishibashi,T., Hayakawa,H., Ito,R., Miyazawa,M., Yamagata,Y. and
            Sekiguchi,M.
  TITLE     Mammalian enzymes for preventing transcriptional errors caused by
            oxidative damage
  JOURNAL   Nucleic Acids Res 33 (12), 3779-3784 (2005)
   PUBMED   16002790
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Ishibashi,T., Hayakawa,H. and Sekiguchi,M.
  TITLE     A novel mechanism for preventing mutations caused by oxidation of
            guanine nucleotides
  JOURNAL   EMBO Rep 4 (5), 479-483 (2003)
   PUBMED   12717453
  REMARK    GeneRIF: degrades 8-oxo-dGDP to 8-oxo-dGMP, an unusable form for
            DNA synthesis, and promotes the cleavage of 8-oxo-dGTP by MTH1 to
            yield 8-oxo-dGMP also
REFERENCE   8  (residues 1 to 219)
  AUTHORS   Yang,H., Slupska,M.M., Wei,Y.F., Tai,J.H., Luther,W.M., Xia,Y.R.,
            Shih,D.M., Chiang,J.H., Baikalov,C., Fitz-Gibbon,S., Phan,I.T.,
            Conrad,A. and Miller,J.H.
  TITLE     Cloning and characterization of a new member of the Nudix
            hydrolases from human and mouse
  JOURNAL   J Biol Chem 275 (12), 8844-8853 (2000)
   PUBMED   10722730
REFERENCE   9  (residues 1 to 219)
  AUTHORS   Gasmi,L., Cartwright,J.L. and McLennan,A.G.
  TITLE     Cloning, expression and characterization of YSA1H, a human
            adenosine 5'-diphosphosugar pyrophosphatase possessing a MutT motif
  JOURNAL   Biochem J 344 Pt 2 (Pt 2), 331-337 (1999)
   PUBMED   10567213
REFERENCE   10 (residues 1 to 219)
  AUTHORS   McLennan,A.G.
  TITLE     The MutT motif family of nucleotide phosphohydrolases in man and
            human pathogens (review)
  JOURNAL   Int J Mol Med 4 (1), 79-89 (1999)
   PUBMED   10373642
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000025.2, AF155832.1, AC073160.8 and CA944803.1.
            
            On Oct 9, 2003 this sequence version replaced NP_054861.1.
            
            Summary: This gene belongs to the Nudix (nucleoside diphosphate
            linked moiety X) hydrolase superfamily. The encoded enzyme
            catalyzes the hydrolysis of modified nucleoside diphosphates,
            including ADP-ribose (ADPR) and 8-oxoGua-containing 8-oxo-dADP and
            8-oxo-dGDP. Protein-bound ADP ribose can be hazardous to the cell
            because it can modify some amino acid residues, resulting in the
            inhibition of ATP-activated potassium channels. 8-oxoGua is an
            oxidized form of guanine that can potentially alter genetic
            information by pairing with adenine and cytosine in RNA. Presence
            of 8-oxoGua in RNA results in formation of abnormal proteins due to
            translational errors. [provided by RefSeq, Aug 2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.15842.1,
                                           SRR1660805.30308.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000491614.6/ ENSP00000419628.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p14"
     Protein         1..219
                     /product="ADP-sugar pyrophosphatase isoform 1"
                     /EC_number="3.6.1.13"
                     /EC_number="3.6.1.58"
                     /EC_number="2.7.7.96"
                     /note="ADP-sugar pyrophosphatase; 8-oxo-dGDP phosphatase;
                     nudix (nucleoside diphosphate linked moiety X)-type motif
                     5; nuclear ATP-synthesis protein NUDIX5"
                     /calculated_mol_wt=24197
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9UKK9.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKK9.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UKK9.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:27257257; propagated from
                     UniProtKB/Swiss-Prot (Q9UKK9.1)"
     Region          58..205
                     /region_name="NUDIX_ADPRase_Nudt5"
                     /note="ADP-ribose pyrophosphatase; cd18888"
                     /db_xref="CDD:467598"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q9UKK9.1)"
     Region          97..118
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKK9.1)"
     Site            210
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UKK9.1)"
     Site            218
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UKK9.1)"
     CDS             1..219
                     /gene="NUDT5"
                     /gene_synonym="hNUDT5; YSA1; YSA1H; YSAH1"
                     /coded_by="NM_014142.4:164..823"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7089.1"
                     /db_xref="GeneID:11164"
                     /db_xref="HGNC:HGNC:8052"
                     /db_xref="MIM:609230"
ORIGIN      
        1 mesqeptess qngkqyiise elisegkwvk lekttymdpt gktrtwesvk rttrkeqtad
       61 gvavipvlqr tlhyecivlv kqfrppmggy ciefpaglid dgetpeaaal releeetgyk
      121 gdiaecspav cmdpglsnct ihivtvting ddaenarpkp kpgdgefvev islpkndllq
      181 rldalvaeeh ltvdarvysy alalkhanak pfevpflkf
//
LOCUS       NP_001349374             653 aa            linear   ROD 27-APR-2025
DEFINITION  actin-binding LIM protein 1 isoform 8 [Mus musculus].
ACCESSION   NP_001349374 XP_017173669
VERSION     NP_001349374.1
DBSOURCE    REFSEQ: accession NM_001362445.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Chen,X., Liu,Y., Xu,C., Ba,L., Liu,Z., Li,X., Huang,J., Simpson,E.,
            Gao,H., Cao,D., Sheng,W., Qi,H., Ji,H., Sanderson,M., Cai,C.L.,
            Li,X., Yang,L., Na,J., Yamamura,K., Liu,Y., Huang,G., Shou,W. and
            Sun,N.
  TITLE     QKI is a critical pre-mRNA alternative splicing regulator of
            cardiac myofibrillogenesis and contractile function
  JOURNAL   Nat Commun 12 (1), 89 (2021)
   PUBMED   33397958
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 653)
  AUTHORS   Jin,S.H., Kim,H., Gu,D.R., Park,K.H., Lee,Y.R., Choi,Y. and
            Lee,S.H.
  TITLE     Actin-binding LIM protein 1 regulates receptor activator of
            NF-kappaB ligand-mediated osteoclast differentiation and motility
  JOURNAL   BMB Rep 51 (7), 356-361 (2018)
   PUBMED   29921413
  REMARK    GeneRIF: ABLIM1 is associated with the regulation of preosteoclast
            motility via the PI3K/Akt/Rac1 pathway during RANKL-mediated
            osteoclastogenesis.
REFERENCE   4  (residues 1 to 653)
  AUTHORS   Zhang,Q., Huang,R., Ye,Y., Guo,X., Lu,J., Zhu,F., Gong,X.,
            Zhang,Q., Yan,J., Luo,L., Zhuang,S., Chen,Y., Zhao,X., Evans,S.M.,
            Jiang,C., Liang,X. and Sun,Y.
  TITLE     Temporal requirements for ISL1 in sympathetic neuron proliferation,
            differentiation, and diversification
  JOURNAL   Cell Death Dis 9 (2), 247 (2018)
   PUBMED   29445148
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 653)
  AUTHORS   Narahara,H., Sakai,E., Yamaguchi,Y., Narahara,S., Iwatake,M.,
            Okamoto,K., Yoshida,N. and Tsukuba,T.
  TITLE     Actin binding LIM 1 (abLIM1) negatively controls osteoclastogenesis
            by regulating cell migration and fusion
  JOURNAL   J Cell Physiol 234 (1), 486-499 (2018)
   PUBMED   29904924
  REMARK    GeneRIF: abLIM1 regulated the localization of tubulin, migration,
            and fusion in osteoclasts. Thus, these results indicate that abLIM1
            negatively controls osteoclast differentiation by regulating cell
            migration and fusion mediated via actin formation.
REFERENCE   6  (residues 1 to 653)
  AUTHORS   Erkman,L., Yates,P.A., McLaughlin,T., McEvilly,R.J., Whisenhunt,T.,
            O'Connell,S.M., Krones,A.I., Kirby,M.A., Rapaport,D.H.,
            Bermingham,J.R., O'Leary,D.D. and Rosenfeld,M.G.
  TITLE     A POU domain transcription factor-dependent program regulates axon
            pathfinding in the vertebrate visual system
  JOURNAL   Neuron 28 (3), 779-792 (2000)
   PUBMED   11163266
REFERENCE   7  (residues 1 to 653)
  AUTHORS   Suriyapperuma,S.P., Lozovatsky,L., Ciciotte,S.L., Peters,L.L. and
            Gilligan,D.M.
  TITLE     The mouse adducin gene family: alternative splicing and chromosomal
            localization
  JOURNAL   Mamm Genome 11 (1), 16-23 (2000)
   PUBMED   10602987
REFERENCE   8  (residues 1 to 653)
  AUTHORS   Kim,H.J., Noben-Trauth,K. and Morell,R.J.
  TITLE     Tectorin-beta (Tectb) maps to mouse chromosome 19
  JOURNAL   Genomics 53 (3), 419-420 (1998)
   PUBMED   9799617
REFERENCE   9  (residues 1 to 653)
  AUTHORS   Kim,A.C., Peters,L.L., Knoll,J.H., Van Huffel,C., Ciciotte,S.L.,
            Kleyn,P.W. and Chishti,A.H.
  TITLE     Limatin (LIMAB1), an actin-binding LIM protein, maps to mouse
            chromosome 19 and human chromosome 10q25, a region frequently
            deleted in human cancers
  JOURNAL   Genomics 46 (2), 291-293 (1997)
   PUBMED   9417918
REFERENCE   10 (residues 1 to 653)
  AUTHORS   Roof,D.J., Hayes,A., Adamian,M., Chishti,A.H. and Li,T.
  TITLE     Molecular characterization of abLIM, a novel actin-binding and
            double zinc finger protein
  JOURNAL   J Cell Biol 138 (3), 575-588 (1997)
   PUBMED   9245787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131756.3, AC102655.7 and AC161518.3.
            
            On Apr 18, 2018 this sequence version replaced XP_017173669.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 52.09 cM"
     Protein         1..653
                     /product="actin-binding LIM protein 1 isoform 8"
                     /note="actin-binding double zinc finger protein;
                     actin-binding LIM protein family member 1"
                     /calculated_mol_wt=73781
     Region          22..73
                     /region_name="LIM1_abLIM"
                     /note="The first LIM domain of actin binding LIM (abLIM)
                     proteins; cd09327"
                     /db_xref="CDD:188713"
     Site            order(22,25,42,45,48,51,69,72)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188713"
     Region          78..133
                     /region_name="LIM2_abLIM"
                     /note="The second LIM domain on actin binding LIM (abLIM)
                     proteins; cd09328"
                     /db_xref="CDD:188714"
     Site            order(81,84,101,104,107,110,129,132)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188714"
     Region          149..200
                     /region_name="LIM3_abLIM"
                     /note="The third LIM domain of actin binding LIM (abLIM)
                     proteins; cd09329"
                     /db_xref="CDD:188715"
     Site            order(149,152,170,173,176,179,196,199)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188715"
     Region          208..263
                     /region_name="LIM4_abLIM"
                     /note="The fourth LIM domain of actin binding LIM (abLIM)
                     proteins; cd09330"
                     /db_xref="CDD:188716"
     Site            order(208,211,228,231,234,237,256,259)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188716"
     Region          272..603
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          618..653
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..653
                     /gene="Ablim1"
                     /gene_synonym="2210411C18Rik; 2610209L21Rik;
                     4833406P10Rik; 9330196J19Rik; Limab1; mKIAA0059"
                     /coded_by="NM_001362445.1:215..2176"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:226251"
                     /db_xref="MGI:MGI:1194500"
ORIGIN      
        1 mstrvahpqd phhssekpvi hchkcgepck gevlrvqtkh fhikcftckv cgcdlaqggf
       61 fikngdylct ldyqrmygtr chgcgefveg evvtalgkty hpncfactic krpfppgdrv
      121 tfngrdclcq lcaqpmsssp keascssnca gcgrdikngq allaldkqwh lgcfkckscg
      181 kvltgeyisk dgspycekdy qglfgvkcea chqfitgkvl eagdkhyhps carcsrcnqm
      241 ftegeemylq gstvwhpdck qstkteeklr ptrtssesiy srpgssipgs pghtiyakvd
      301 neildykdla aipkvkaiyd ierpdlitye pfytsgyedk qerqslgesp rtlsptpsae
      361 gyqdvrdrmi hrstsqgsin spvysrhsyt pttsrspqhf hrpgnepssg rnsplpyrpd
      421 srpltptyaq apkhfhvpdq giniyrkppi ykqhgtdprr rssgreedee ellrrrqlqe
      481 eqlmklnsgl gqlilkeeme kesrerasla srydsplhsa shapssktss lpgygknglh
      541 rpvstdfaqy nsygdisggv rdyqtlpdgh mpavrmdrgv smpnmlepki fpyemlmvtn
      601 rgrnkilrdv drtrlerhla pevfweifgm siqefdklpl wrrndmkkka klf
//
LOCUS       NP_001357313             616 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 2 [Homo sapiens].
ACCESSION   NP_001357313 XP_006722684
VERSION     NP_001357313.1
DBSOURCE    REFSEQ: accession NM_001370384.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            On May 7, 2019 this sequence version replaced XP_006722684.1.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.218607.1,
                                           SRR1803615.52870.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..616
                     /product="zinc finger protein 266 isoform 2"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=69720
     Region          39..95
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          199..217
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          225..245
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          254..273
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          277..616
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          281..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          309..329
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(314,316,318,320..321,324..325,328,342,344,348..349,
                     352..353,356,370,372,374,376..377,380..381,384)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          337..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          365..385
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          393..413
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          421..441
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          449..469
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(454,456,458,460..461,464..465,468,482,484,488..489,
                     492..493,496,510,512,514,516..517,520..521,524)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          477..497
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          505..525
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          533..553
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(538,540,542,544..545,548..549,552,566,568,572..573,
                     576..577,580,594,596,598,600..601,604..605,608)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          561..581
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          589..609
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..616
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370384.1:729..2579"
                     /note="isoform 2 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS92507.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 maatdlsygl yrdpvclqek tevervvadc ltncyqdsvt fddlavdftp eewtlldptq
       61 rnlyrdvmle nyknlatvgy qlfkpslisw leqeesrtvq rgdfqasewk vqlktkelal
      121 qqdvlgepts sgiqmigshn ggevsdvkqc gdvssehscl kthvrtqnse ntfecylygv
      181 dfltlhkkts tgeqrsvfsq cgkafslnpd vvcqrtctge kafdcsdsgk sfinhshlqg
      241 hlrthngesl hewkecgrgf ihstdlavri qthrsekpyk ckecgkgfry saylnihmgt
      301 htgdnpyeck ecgkaftrsc qltqhrktht gekpykckdc graftvsscl sqhmkihvge
      361 kpyeckecgi aftrssqlte hlkthtakdp feckicgksf rnssclsdhf rihtgikpyk
      421 ckdcgkaftq nsdltkhart hsgerpyeck ecgkafarss rlsehtrtht gekpfecvkc
      481 gkafaissnl sghlrihtge kpfeclecgk afthssslnn hmrthsakkp ftcmecgkaf
      541 kfptcvnlhm rihtgekpyk ckqcgksfsy snsfqlhert htgekpyeck ecgkafssss
      601 sfrnherrha derlsa
//
LOCUS       NP_001346813            1014 aa            linear   ROD 27-APR-2025
DEFINITION  endosome/lysosome-associated apoptosis and autophagy regulator
            family member 2 isoform 2 precursor [Mus musculus].
ACCESSION   NP_001346813
VERSION     NP_001346813.1
DBSOURCE    REFSEQ: accession NM_001359884.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Araki,T., Kusakabe,M. and Nishida,E.
  TITLE     A transmembrane protein EIG121L is required for epidermal
            differentiation during early embryonic development
  JOURNAL   J Biol Chem 286 (8), 6760-6768 (2011)
   PUBMED   21177533
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158121.12, AC157783.7 and AC157555.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK045969.1, AK161902.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849387, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 3.69 cM"
     Protein         1..1014
                     /product="endosome/lysosome-associated apoptosis and
                     autophagy regulator family member 2 isoform 2 precursor"
                     /note="estrogen-induced gene 121-like protein; UPF0577
                     protein KIAA1324-like homolog"
                     /calculated_mol_wt=106862
     sig_peptide     1..47
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3UZV7.1)"
                     /calculated_mol_wt=5190
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3UZV7.1)"
     Region          286..320
                     /region_name="Ephrin_rec_like"
                     /note="Tyrosine-protein kinase ephrin type A/B
                     receptor-like; pfam07699"
                     /db_xref="CDD:429604"
     Region          401..>431
                     /region_name="Ephrin_rec_like"
                     /note="Tyrosine-protein kinase ephrin type A/B
                     receptor-like; pfam07699"
                     /db_xref="CDD:429604"
     Site            404
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3UZV7.1)"
     Site            690
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3UZV7.1)"
     Site            929..949
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UZV7.1)"
     CDS             1..1014
                     /gene="Elapor2"
                     /gene_synonym="9330182L06Rik; Eig121l"
                     /coded_by="NM_001359884.1:154..3198"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS89878.1"
                     /db_xref="GeneID:231014"
                     /db_xref="MGI:MGI:2443264"
ORIGIN      
        1 mllltlrrak grdrgrpagg prralslpws pawiccwala gcqavwagds sssgrplpac
       61 qekdyhfeyt ecdstgsrwr vaipnsavdc sglpdpvkgk ectfscasge ylemknqvcs
      121 kcvegtyslg sgikfdewde lpagfsnvat fmdtvvgpsd srpdgcnnss wlprgnyies
      181 nrddctvsli yavhlkksgy vffeyqyvdn niffeffiqn dqcqemdatt dkwvkltdng
      241 ewgshsvmlk sgtnilywrt tgilmgskav kpvlvkniti egvaytsecf pckpgtfsnk
      301 pgsfncqmcp rntysekgak ecirckedsq fseegasecv drppcttkdy fqihtpcdee
      361 gktqimykwi epkicredlt dairlppsge kkdcppcnpg fynngsssch pcppgtfsdg
      421 tkeckscpag tepalgfeyk wwnvlpanmk tscfnvgnsk cdgmngweva gdhirsgagg
      481 sdndylilnl hipgfkppts mtgatgselg ritfvfetlc sadcvlyfmv dinrkstnvv
      541 eswggtkekq aythvifkna tftftwafqr tnqgqdnrrf indvvkiysi tatnavdgva
      601 ascracalgs eqsasscvpc ppghyieket nqckecpadt ylsihqvygk eacipcgpgs
      661 kstqdhslcy sdcffyheke nqtlhydfrn lssvgslmng psftskgtky fhffnislcg
      721 hegrkmalct nnisdftvke mvtgsddytn lvgafvcqst iipseskgfr aalssqsiil
      781 admflgvtvd talqnvnike dmfpvspsqv pdvhffykss tattscingr stavkmrcnp
      841 mrpgagvisv pskcpagtcd gctfyflwes aeacplcteh dfheiegack rglqeilyvw
      901 nepkwcikgi slpekklstc etvdfwlkvg agvgaftavl lvaltcyfwk knqkleykys
      961 klvmttnske celpaadsca imegedneed vvysnkqsll gklkslatkv radf
//
LOCUS       NP_001186034             163 aa            linear   ROD 27-APR-2025
DEFINITION  tumor protein p53-inducible nuclear protein 1 isoform 2 [Mus
            musculus].
ACCESSION   NP_001186034
VERSION     NP_001186034.1
DBSOURCE    REFSEQ: accession NM_001199105.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Beauchamp,M.C., Boucher,A., Dong,Y., Aber,R. and
            Jerome-Majewska,L.A.
  TITLE     Craniofacial Defects in Embryos with Homozygous Deletion of Eftud2
            in Their Neural Crest Cells Are Not Rescued by Trp53 Deletion
  JOURNAL   Int J Mol Sci 23 (16), 9033 (2022)
   PUBMED   36012294
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Beauchamp,M.C., Djedid,A., Bareke,E., Merkuri,F., Aber,R.,
            Tam,A.S., Lines,M.A., Boycott,K.M., Stirling,P.C., Fish,J.L.,
            Majewski,J. and Jerome-Majewska,L.A.
  TITLE     Mutation in Eftud2 causes craniofacial defects in mice via
            mis-splicing of Mdm2 and increased P53
  JOURNAL   Hum Mol Genet 30 (9), 739-757 (2021)
   PUBMED   33601405
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Warnez-Soulie,J., Macia,M., Lac,S., Pecchi,E., Bernard,M.,
            Bendahan,D., Bartoli,M., Carrier,A. and Giannesini,B.
  TITLE     Tumor protein 53-induced nuclear protein 1 deficiency alters mouse
            gastrocnemius muscle function and bioenergetics in vivo
  JOURNAL   Physiol Rep 7 (10), e14055 (2019)
   PUBMED   31124296
  REMARK    GeneRIF: TP53INP1 plays a role in regulating muscle function and
            bioenergetics through oxidative capacity impairment possibly as the
            consequence of abnormal mitochondrial respiration regulation and/or
            defective blood supply.
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Tomasini,R., Seux,M., Nowak,J., Bontemps,C., Carrier,A.,
            Dagorn,J.C., Pebusque,M.J., Iovanna,J.L. and Dusetti,N.J.
  TITLE     TP53INP1 is a novel p73 target gene that induces cell cycle arrest
            and cell death by modulating p73 transcriptional activity
  JOURNAL   Oncogene 24 (55), 8093-8104 (2005)
   PUBMED   16044147
  REMARK    GeneRIF: TP53INP1s are functionally associated with p73 to regulate
            cell cycle progression and apoptosis.
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Tomasini,R., Samir,A.A., Pebusque,M.J., Calvo,E.L., Totaro,S.,
            Dagorn,J.C., Dusetti,N.J. and Iovanna,J.L.
  TITLE     P53-dependent expression of the stress-induced protein (SIP)
  JOURNAL   Eur J Cell Biol 81 (5), 294-301 (2002)
   PUBMED   12067065
  REMARK    GeneRIF: Data show that induction of the stress-induced proteins
            (SIPs) SIP18 and SIP27, in human- and mouse-derived cell lines, is
            absent from cells with deleted, mutated or inactive p53, suggesting
            that regulation of SIP gene expression is dependent on p53.
REFERENCE   8  (residues 1 to 163)
  AUTHORS   Tomasini,R., Samir,A.A., Vaccaro,M.I., Pebusque,M.J., Dagorn,J.C.,
            Iovanna,J.L. and Dusetti,N.J.
  TITLE     Molecular and functional characterization of the stress-induced
            protein (SIP) gene and its two transcripts generated by alternative
            splicing. SIP induced by stress and promotes cell death
  JOURNAL   J Biol Chem 276 (47), 44185-44192 (2001)
   PUBMED   11557757
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Carrier,A., Wurbel,M.A., Mattei,M.G., Kissenpfennig,A., Malissen,M.
            and Malissen,B.
  TITLE     Chromosomal localization of two mouse genes encoding
            thymus-specific serine peptidase and thymus-expressed acidic
            protein
  JOURNAL   Immunogenetics 51 (11), 984-986 (2000)
   PUBMED   11003393
REFERENCE   10 (residues 1 to 163)
  AUTHORS   Carrier,A., Nguyen,C., Victorero,G., Granjeaud,S., Rocha,D.,
            Bernard,K., Miazek,A., Ferrier,P., Malissen,M., Naquet,P.,
            Malissen,B. and Jordan,B.R.
  TITLE     Differential gene expression in CD3epsilon- and RAG1-deficient
            thymuses: definition of a set of genes potentially involved in
            thymocyte maturation
  JOURNAL   Immunogenetics 50 (5-6), 255-270 (1999)
   PUBMED   10630289
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL840625.9.
            
            Transcript Variant: This variant (2) has an additional exon in the
            coding region which results in a frameshift and early stop codon,
            compared to variant 1. It encodes a shorter isoform (2; also known
            as SIP18) with a distinct C-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY034611.1, SRR10223971.4500.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 5.03 cM"
     Protein         1..163
                     /product="tumor protein p53-inducible nuclear protein 1
                     isoform 2"
                     /note="stress induced protein; tumor protein p53-inducible
                     nuclear protein 1; thymus-expressed acidic protein;
                     p53-dependent damage-inducible nuclear protein 1"
                     /calculated_mol_wt=17879
     Region          24..>160
                     /region_name="DOR"
                     /note="DOR family; pfam14839"
                     /db_xref="CDD:464343"
     Region          25..37
                     /region_name="LIR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXE4.1)"
     CDS             1..163
                     /gene="Trp53inp1"
                     /gene_synonym="2700057G22Rik; p53DINP1; SIP; SIP18; SIP27;
                     Stinp; Teap; Tp53inp1"
                     /coded_by="NM_001199105.2:255..746"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:60599"
                     /db_xref="MGI:MGI:1926609"
ORIGIN      
        1 mfqrlnkmfv gevttsssqe pefsekedde wilvdfidtc pgfsaeeeee dedigeessa
       61 ehtsvfsclp aslecltdts dscflqfesc pmeeswfitp ppcftagglt tikvetspme
      121 nlliehpsms vyavhnscpg lseascgnde ynssgprark scl
//
LOCUS       NP_060184                420 aa            linear   PRI 27-APR-2025
DEFINITION  threonine aspartase 1 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_060184
VERSION     NP_060184.2
DBSOURCE    REFSEQ: accession NM_017714.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Oelschlager,L., Stahl,P., Kaschani,F., Stauber,R.H., Knauer,S.K.
            and Hensel,A.
  TITLE     Taspase1 Facilitates Topoisomerase IIbeta-Mediated DNA
            Double-Strand Breaks Driving Estrogen-Induced Transcription
  JOURNAL   Cells 12 (3), 363 (2023)
   PUBMED   36766705
  REMARK    GeneRIF: Taspase1 Facilitates Topoisomerase IIbeta-Mediated DNA
            Double-Strand Breaks Driving Estrogen-Induced Transcription.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Nagaratnam,N., Delker,S.L., Jernigan,R., Edwards,T.E., Snider,J.,
            Thifault,D., Williams,D., Nannenga,B.L., Stofega,M., Sambucetti,L.,
            Hsieh,J.J., Flint,A.J., Fromme,P. and Martin-Garcia,J.M.
  TITLE     Structural insights into the function of the catalytically active
            human Taspase1
  JOURNAL   Structure 29 (8), 873-885 (2021)
   PUBMED   33784495
  REMARK    GeneRIF: Structural insights into the function of the catalytically
            active human Taspase1.
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Lin,Y., Huang,Y., Liang,C., Xie,S. and Xie,A.
  TITLE     Silencing of circTASP1 inhibits proliferation and induces apoptosis
            of acute myeloid leukaemia cells through modulating
            miR-515-5p/HMGA2 axis
  JOURNAL   J Cell Mol Med 25 (15), 7367-7380 (2021)
   PUBMED   34197029
  REMARK    GeneRIF: Silencing of circTASP1 inhibits proliferation and induces
            apoptosis of acute myeloid leukaemia cells through modulating
            miR-515-5p/HMGA2 axis.
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Wan,X.M., Zhou,X.L., Du,Y.J., Shen,H., Yang,Z. and Ding,Y.
  TITLE     TASP1 Promotes Proliferation and Migration in Gastric Cancer via
            EMT and AKT/P-AKT Pathway
  JOURNAL   J Immunol Res 2021, 5521325 (2021)
   PUBMED   34012990
  REMARK    GeneRIF: TASP1 Promotes Proliferation and Migration in Gastric
            Cancer via EMT and AKT/P-AKT Pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Zhang,Y., Du,P., Li,Y., Zhu,Q., Song,X., Liu,S., Hao,J., Liu,L.,
            Liu,F., Hu,Y., Jiang,L., Ma,Q., Lu,W. and Liu,Y.
  TITLE     TASP1 Promotes Gallbladder Cancer Cell Proliferation and Metastasis
            by Up-regulating FAM49B via PI3K/AKT Pathway
  JOURNAL   Int J Biol Sci 16 (5), 739-751 (2020)
   PUBMED   32071545
  REMARK    GeneRIF: TASP1 Promotes Gallbladder Cancer Cell Proliferation and
            Metastasis by Up-regulating FAM49B via PI3K/AKT Pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Zhou,H., Spicuglia,S., Hsieh,J.J., Mitsiou,D.J., Hoiby,T.,
            Veenstra,G.J., Korsmeyer,S.J. and Stunnenberg,H.G.
  TITLE     Uncleaved TFIIA is a substrate for taspase 1 and active in
            transcription
  JOURNAL   Mol Cell Biol 26 (7), 2728-2735 (2006)
   PUBMED   16537915
  REMARK    GeneRIF: Transfected taspase 1 enhances cleavage of TFIIA, and RNA
            interference knockdown of endogenous taspase 1 diminishes cleavage
            of TFIIA in vivo.
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Khan,J.A., Dunn,B.M. and Tong,L.
  TITLE     Crystal structure of human Taspase1, a crucial protease regulating
            the function of MLL
  JOURNAL   Structure 13 (10), 1443-1452 (2005)
   PUBMED   16216576
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Hsieh,J.J., Cheng,E.H. and Korsmeyer,S.J.
  TITLE     Taspase1: a threonine aspartase required for cleavage of MLL and
            proper HOX gene expression
  JOURNAL   Cell 115 (3), 293-303 (2003)
   PUBMED   14636557
  REMARK    GeneRIF: purification and cloning of threonine aspartase 1
            responsible for cleaving MLL; RNAi-mediated knockdown of Taspase1
            results in the appearance of unprocessed MLL and the loss of proper
            HOX gene expression
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Hsieh,J.J., Ernst,P., Erdjument-Bromage,H., Tempst,P. and
            Korsmeyer,S.J.
  TITLE     Proteolytic cleavage of MLL generates a complex of N- and
            C-terminal fragments that confers protein stability and subnuclear
            localization
  JOURNAL   Mol Cell Biol 23 (1), 186-194 (2003)
   PUBMED   12482972
REFERENCE   10 (residues 1 to 420)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL601028.1, BC025266.1 and
            CA418131.1.
            
            On May 19, 2006 this sequence version replaced NP_060184.1.
            
            Summary: This gene encodes an endopeptidase that cleaves specific
            substrates following aspartate residues. The encoded protein
            undergoes posttranslational autoproteolytic processing to generate
            alpha and beta subunits, which reassemble into the active
            alpha2-beta2 heterotetramer. It is required to cleave MLL, a
            protein required for the maintenance of HOX gene expression, and
            TFIIA, a basal transcription factor. Alternatively spliced
            transcript variants have been described, but their biological
            validity has not been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.101399.1,
                                           SRR3476690.70013.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337743.9/ ENSP00000338624.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.1"
     Protein         1..420
                     /product="threonine aspartase 1 isoform 1 precursor"
                     /EC_number="3.4.25.-"
                     /note="threonine aspartase 1"
                     /calculated_mol_wt=44325
     mat_peptide     1..233
                     /product="Threonine aspartase subunit alpha.
                     /id=PRO_0000002350"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6P5.1)"
                     /calculated_mol_wt=25057
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6P5.1)"
     Region          42..416
                     /region_name="Taspase1_like"
                     /note="Taspase 1 (threonine aspartase 1) and similar
                     proteins; cd04514"
                     /db_xref="CDD:271336"
     Site            order(109,120,125..127,132,159..166,169,173,255..258,
                     260..263,268..269,274,276,295,298..299,301,304..305)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271336"
     mat_peptide     234..420
                     /product="Threonine aspartase subunit beta.
                     /id=PRO_0000002351"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6P5.1)"
                     /calculated_mol_wt=19417
     CDS             1..420
                     /gene="TASP1"
                     /gene_synonym="C20orf13; dJ585I14.2; SULEHS"
                     /coded_by="NM_017714.3:114..1376"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS13116.1"
                     /db_xref="GeneID:55617"
                     /db_xref="HGNC:HGNC:15859"
                     /db_xref="MIM:608270"
ORIGIN      
        1 mtmekgmssg eglpsrssqv sagkitakel etkqsykekr ggfvlvhaga gyhseskake
       61 ykhvckracq kaieklqaga latdavtaal veledspftn agmgsnlnll geiecdasim
      121 dgkslnfgav galsgiknpv svanrllceg qkgklsagri ppcflvgega yrwavdhgip
      181 scppnimttr fslaafkrnk rklelaervd tdfmqlkkrr qssekendsg tldtvgavvv
      241 dhegnvaaav ssgglalkhp grvgqaalyg cgcwaentga hnpystavst sgcgehlvrt
      301 ilarecshal qaedahqall etmqnkfiss pflasedgvl ggvivlrscr csaepdssqn
      361 kqtllveflw shttesmcvg ymsaqdgkak thisrlppga vagqsvaieg gvcrlespvn
//
LOCUS       NP_001012339             531 aa            linear   PRI 27-APR-2025
DEFINITION  dnaJ homolog subfamily C member 21 isoform 2 [Homo sapiens].
ACCESSION   NP_001012339
VERSION     NP_001012339.2
DBSOURCE    REFSEQ: accession NM_001012339.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Morini,J., Nacci,L., Babini,G., Cesaro,S., Valli,R., Ottolenghi,A.,
            Nicolis,E., Pintani,E., Maserati,E., Cipolli,M., Danesino,C.,
            Scotti,C. and Minelli,A.
  TITLE     Whole exome sequencing discloses heterozygous variants in the
            DNAJC21 and EFL1 genes but not in SRP54 in 6 out of 16 patients
            with Shwachman-Diamond Syndrome carrying biallelic SBDS mutations
  JOURNAL   Br J Haematol 185 (3), 627-630 (2019)
   PUBMED   30198570
  REMARK    GeneRIF: Whole exome sequencing discloses heterozygous variants in
            the DNAJC21 and EFL1 genes but not in SRP54 in 6 out of 16 patients
            with Shwachman-Diamond Syndrome carrying biallelic SBDS mutations.
REFERENCE   2  (residues 1 to 531)
  AUTHORS   D'Amours,G., Lopes,F., Gauthier,J., Saillour,V., Nassif,C.,
            Wynn,R., Alos,N., Leblanc,T., Capri,Y., Nizard,S., Lemyre,E.,
            Michaud,J.L., Pelletier,V.A., Pastore,Y.D. and Soucy,J.F.
  TITLE     Refining the phenotype associated with biallelic DNAJC21 mutations
  JOURNAL   Clin Genet 94 (2), 252-258 (2018)
   PUBMED   29700810
  REMARK    GeneRIF: We suggest that DNAJC21-related diseases constitute a
            distinct Inherited bone marrow failure syndromes (IBMFS) , with
            features overlapping Shwachman-Diamond syndrome and Dyskeratosis
            congenita, and additional characteristics that are specific to
            DNAJC21 mutations
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Warren,A.J.
  TITLE     Molecular basis of the human ribosomopathy Shwachman-Diamond
            syndrome
  JOURNAL   Adv Biol Regul 67, 109-127 (2018)
   PUBMED   28942353
  REMARK    Review article
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Dhanraj,S., Matveev,A., Li,H., Lauhasurayotin,S., Jardine,L.,
            Cada,M., Zlateska,B., Tailor,C.S., Zhou,J., Mendoza-Londono,R.,
            Vincent,A., Durie,P.R., Scherer,S.W., Rommens,J.M., Heon,E. and
            Dror,Y.
  TITLE     Biallelic mutations in DNAJC21 cause Shwachman-Diamond syndrome
  JOURNAL   Blood 129 (11), 1557-1562 (2017)
   PUBMED   28062395
  REMARK    GeneRIF: Biallelic mutations in DNAJC21 cause Shwachman-Diamond
            syndrome.
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Tummala,H., Walne,A.J., Williams,M., Bockett,N., Collopy,L.,
            Cardoso,S., Ellison,A., Wynn,R., Leblanc,T., Fitzgibbon,J.,
            Kelsell,D.P., van Heel,D.A., Payne,E., Plagnol,V., Dokal,I. and
            Vulliamy,T.
  TITLE     DNAJC21 Mutations Link a Cancer-Prone Bone Marrow Failure Syndrome
            to Corruption in 60S Ribosome Subunit Maturation
  JOURNAL   Am J Hum Genet 99 (1), 115-124 (2016)
   PUBMED   27346687
  REMARK    GeneRIF: findings demonstrate that mutations in DNAJC21 cause a
            cancer-prone bone marrow failure syndrome due to corruption of
            early nuclear rRNA biogenesis and late cytoplasmic maturation of
            the 60S subunit
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Kaltenbach,L.S., Romero,E., Becklin,R.R., Chettier,R., Bell,R.,
            Phansalkar,A., Strand,A., Torcassi,C., Savage,J., Hurlburt,A.,
            Cha,G.H., Ukani,L., Chepanoske,C.L., Zhen,Y., Sahasrabudhe,S.,
            Olson,J., Kurschner,C., Ellerby,L.M., Peltier,J.M., Botas,J. and
            Hughes,R.E.
  TITLE     Huntingtin interacting proteins are genetic modifiers of
            neurodegeneration
  JOURNAL   PLoS Genet 3 (5), e82 (2007)
   PUBMED   17500595
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Qiu,X.B., Shao,Y.M., Miao,S. and Wang,L.
  TITLE     The diversity of the DnaJ/Hsp40 family, the crucial partners for
            Hsp70 chaperones
  JOURNAL   Cell Mol Life Sci 63 (22), 2560-2570 (2006)
   PUBMED   16952052
  REMARK    Review article
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Chen,J., Yin,G., Lu,Y., Lou,M., Cheng,H., Ni,X., Hu,G., Luo,C.,
            Ying,K., Xie,Y. and Mao,Y.
  TITLE     Cloning and characterization of a novel human cDNA encoding a
            J-domain protein (DNAJA5) from the fetal brain
  JOURNAL   Int J Mol Med 13 (5), 735-740 (2004)
   PUBMED   15067379
  REMARK    GeneRIF: molecular cloning
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Nelson,A. and Myers,K.
  TITLE     Shwachman-Diamond Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301722
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026801.7, BC065745.1,
            AY258422.1 and AC008795.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 21, 2005 this sequence version replaced NP_001012339.1.
            
            Summary: This gene encodes a member of the DNAJ heat shock protein
            40 family of proteins that is characterized by two N-terminal
            tetratricopeptide repeat domains and a C-terminal DNAJ domain. This
            protein binds the precursor 45S ribosomal RNA and may be involved
            in early nuclear ribosomal RNA biogenesis and maturation of the 60S
            ribosomal subunit. Mutations in this gene result in Bone marrow
            failure syndrome 3. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Feb 2017].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            coding region, as compared to variant 1. The encoded isoform (2)
            lacks an internal segment, as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.89834.1,
                                           SRR1660809.2077.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000648817.1/
                                                ENSP00000497410.1
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..531
                     /product="dnaJ homolog subfamily C member 21 isoform 2"
                     /note="JJJ1 DnaJ domain protein homolog; dnaJ homolog
                     subfamily C member 21; DnaJ homology subfamily A member 5;
                     dnaJ homolog subfamily A member 5; DnaJ (Hsp40) homolog,
                     subfamily C, member 21"
                     /calculated_mol_wt=61897
     Region          2..>79
                     /region_name="PRK10767"
                     /note="chaperone protein DnaJ; Provisional"
                     /db_xref="CDD:236757"
     Region          4..>267
                     /region_name="ZUO1"
                     /note="Ribosome-associated chaperone zuotin [Translation,
                     ribosomal structure and biogenesis / Posttranslational
                     modification, protein turnover, chaperones]; COG5269"
                     /db_xref="CDD:227594"
     Region          279..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5F1R6.2)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q5F1R6.2)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q5F1R6.2)"
     Region          314..339
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          316..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          327..474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5F1R6.2)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5F1R6.2)"
     Region          502..531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5F1R6.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5F1R6.2)"
     CDS             1..531
                     /gene="DNAJC21"
                     /gene_synonym="BMFS3; DNAJA5; GS3; JJJ1"
                     /coded_by="NM_001012339.3:262..1857"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS34144.1"
                     /db_xref="GeneID:134218"
                     /db_xref="HGNC:HGNC:27030"
                     /db_xref="MIM:617048"
ORIGIN      
        1 mkchyealgv rrdaseeelk kayrklalkw hpdknldnaa eaaeqfkliq aaydvlsdpq
       61 erawydnhre allkggfdge yqddsldllr yftvtcysgy gddekgfytv yrnvfemiak
      121 eelesvleee vddfptfgds qsdydtvvhp fyaywqsfct qknfawkeey dtrqasnrwe
      181 kramekenkk irdkarkekn elvrqlvafi rkrdkrvqah rklveeqnae karkaeemrr
      241 qqklkqaklv eqyreqswmt manlekelqe mearyekefg dgsdenemee helkdeedgk
      301 dsdeaedael yddlycpacd ksfktekamk nhekskkhre mvallkqqle eeeenfsrpq
      361 idenplddns eeemedapkq klskkqkkkk qkpaqnyddn fnvngpgegv kvdpedtnln
      421 qdsakeleds pqenvsvtei ikpcddpkse aksvpkpkgk ktkdmkkpvr vpaepqtmsv
      481 liscttchse fpsrnklfdh lkatgharap sssslnsats sqskkekrkn r
//
LOCUS       NP_001357450             225 aa            linear   PRI 27-APR-2025
DEFINITION  phosphoserine phosphatase [Homo sapiens].
ACCESSION   NP_001357450
VERSION     NP_001357450.1
DBSOURCE    REFSEQ: accession NM_001370521.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Rawat,V., Malvi,P., Della Manna,D., Yang,E.S., Bugide,S., Zhang,X.,
            Gupta,R. and Wajapeyee,N.
  TITLE     PSPH promotes melanoma growth and metastasis by metabolic
            deregulation-mediated transcriptional activation of NR4A1
  JOURNAL   Oncogene 40 (13), 2448-2462 (2021)
   PUBMED   33674745
  REMARK    GeneRIF: PSPH promotes melanoma growth and metastasis by metabolic
            deregulation-mediated transcriptional activation of NR4A1.
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Park,S.M., Seo,E.H., Bae,D.H., Kim,S.S., Kim,J., Lin,W., Kim,K.H.,
            Park,J.B., Kim,Y.S., Yin,J. and Kim,S.Y.
  TITLE     Phosphoserine Phosphatase Promotes Lung Cancer Progression through
            the Dephosphorylation of IRS-1 and a Noncanonical
            L-Serine-Independent Pathway
  JOURNAL   Mol Cells 42 (8), 604-616 (2019)
   PUBMED   31446747
  REMARK    GeneRIF: a specific interaction between PSPH and IRS1 and the
            dephosphorylation of phospho-IRS-1 by PSPH in lung cancer cells,
            was identified.
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Haufroid,M., Mirgaux,M., Leherte,L. and Wouters,J.
  TITLE     Crystal structures and snapshots along the reaction pathway of
            human phosphoserine phosphatase
  JOURNAL   Acta Crystallogr D Struct Biol 75 (Pt 6), 592-604 (2019)
   PUBMED   31205021
  REMARK    GeneRIF: three new high-resolution crystal structures of hPSP
            (1.5-2.0 A) in complexes with phosphoserine and with serine, which
            are the substrate and the product of the reaction, respectively,
            and in complex with a noncleavable substrate analogue (homocysteic
            acid) are presented.
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Liao,L., Ge,M., Zhan,Q., Huang,R., Ji,X., Liang,X. and Zhou,X.
  TITLE     PSPH Mediates the Metastasis and Proliferation of Non-small Cell
            Lung Cancer through MAPK Signaling Pathways
  JOURNAL   Int J Biol Sci 15 (1), 183-194 (2019)
   PUBMED   30662358
  REMARK    GeneRIF: The results suggest that PSPH may act as a putative
            oncogene and a potential therapeutic target in NSCLC.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 225)
  AUTHORS   van der Crabben,S.N. and de Koning,T.J.
  TITLE     Serine Deficiency Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37347880
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Veeranna and Shetty,K.T.
  TITLE     Phosphoserine phosphatase of human brain: partial purification,
            characterization, regional distribution, and effect of certain
            modulators including psychoactive drugs
  JOURNAL   Neurochem Res 15 (12), 1203-1210 (1990)
   PUBMED   1965857
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Minelli,A., Piantanida,M., Maserati,E., Campagnoli,E., Pasquali,F.
            and Danesino,C.
  TITLE     Gene dosage effect in acquired monosomy 7: distinct behaviour of
            beta-glucuronidase and phosphoserine phosphatase
  JOURNAL   Genes Chromosomes Cancer 1 (3), 216-220 (1990)
   PUBMED   1964582
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Novelli,G. and Dallapiccola,B.
  TITLE     Gene dosage studies regionally assign the phosphoserine phosphatase
            gene to 7p15.1 or 2
  JOURNAL   Ann Genet 31 (3), 195-196 (1988)
   PUBMED   2851960
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Moro-Furlani,A.M., Turner,V.S. and Hopkinson,D.A.
  TITLE     Genetical and biochemical studies on human phosphoserine
            phosphatase
  JOURNAL   Ann Hum Genet 43 (4), 323-333 (1980)
   PUBMED   6249179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092579.3.
            
            Summary: The protein encoded by this gene belongs to a subfamily of
            the phosphotransferases. This encoded enzyme is responsible for the
            third and last step in L-serine formation. It catalyzes
            magnesium-dependent hydrolysis of L-phosphoserine and is also
            involved in an exchange reaction between L-serine and
            L-phosphoserine. Deficiency of this protein is thought to be linked
            to Williams syndrome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.98268.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p11.2"
     Protein         1..225
                     /product="phosphoserine phosphatase"
                     /EC_number="3.1.3.3"
                     /note="L-3-phosphoserine phosphatase; O-phosphoserine
                     phosphohydrolase; PSPase"
                     /calculated_mol_wt=24877
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P78330.2)"
     Region          15..216
                     /region_name="HAD_PSP_eu"
                     /note="phosphoserine phosphatase eukaryotic-like, similar
                     to human phosphoserine phosphatase; cd04309"
                     /db_xref="CDD:319801"
     Site            order(20..24,29,109..110,158,178..179,182..183)
                     /site_type="active"
                     /db_xref="CDD:319801"
     CDS             1..225
                     /gene="PSPH"
                     /gene_synonym="PSP; PSPHD"
                     /coded_by="NM_001370521.1:1007..1684"
                     /db_xref="CCDS:CCDS5522.1"
                     /db_xref="GeneID:5723"
                     /db_xref="HGNC:HGNC:9577"
                     /db_xref="MIM:172480"
ORIGIN      
        1 mvshselrkl fysadavcfd vdstvireeg idelakicgv edavsemtrr amggavpfka
       61 alterlaliq psreqvqrli aeqpphltpg irelvsrlqe rnvqvflisg gfrsivehva
      121 sklnipatnv fanrlkfyfn geyagfdetq ptaesggkgk vikllkekfh fkkiimigdg
      181 atdmeacppa dafigfggnv irqqvkdnak wyitdfvell gelee
//
LOCUS       NP_003446                648 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 202 isoform 1 [Homo sapiens].
ACCESSION   NP_003446
VERSION     NP_003446.2
DBSOURCE    REFSEQ: accession NM_003455.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Ravasi,T., Suzuki,H., Cannistraci,C.V., Katayama,S., Bajic,V.B.,
            Tan,K., Akalin,A., Schmeier,S., Kanamori-Katayama,M., Bertin,N.,
            Carninci,P., Daub,C.O., Forrest,A.R., Gough,J., Grimmond,S.,
            Han,J.H., Hashimoto,T., Hide,W., Hofmann,O., Kamburov,A., Kaur,M.,
            Kawaji,H., Kubosaki,A., Lassmann,T., van Nimwegen,E.,
            MacPherson,C.R., Ogawa,C., Radovanovic,A., Schwartz,A.,
            Teasdale,R.D., Tegner,J., Lenhard,B., Teichmann,S.A., Arakawa,T.,
            Ninomiya,N., Murakami,K., Tagami,M., Fukuda,S., Imamura,K., Kai,C.,
            Ishihara,R., Kitazume,Y., Kawai,J., Hume,D.A., Ideker,T. and
            Hayashizaki,Y.
  TITLE     An atlas of combinatorial transcriptional regulation in mouse and
            man
  JOURNAL   Cell 140 (5), 744-752 (2010)
   PUBMED   20211142
  REMARK    Erratum:[Cell. 2010 Apr 16;141(2):369. Kamburov, Atanas [added];
            Kaur, Mandeep [added]; MacPherson, Cameron Ross [added];
            Radovanovic, Aleksandar [added]; Schwartz, Ariel [added]]
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Porsch-Ozcurumez,M., Langmann,T., Heimerl,S., Borsukova,H.,
            Kaminski,W.E., Drobnik,W., Honer,C., Schumacher,C. and Schmitz,G.
  TITLE     The zinc finger protein 202 (ZNF202) is a transcriptional repressor
            of ATP binding cassette transporter A1 (ABCA1) and ABCG1 gene
            expression and a modulator of cellular lipid efflux
  JOURNAL   J Biol Chem 276 (15), 12427-12433 (2001)
   PUBMED   11279031
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Schumacher,C., Wang,H., Honer,C., Ding,W., Koehn,J., Lawrence,Q.,
            Coulis,C.M., Wang,L.L., Ballinger,D., Bowen,B.R. and Wagner,S.
  TITLE     The SCAN domain mediates selective oligomerization
  JOURNAL   J Biol Chem 275 (22), 17173-17179 (2000)
   PUBMED   10747874
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Wagner,S., Hess,M.A., Ormonde-Hanson,P., Malandro,J., Hu,H.,
            Chen,M., Kehrer,R., Frodsham,M., Schumacher,C., Beluch,M.,
            Honer,C., Skolnick,M., Ballinger,D. and Bowen,B.R.
  TITLE     A broad role for the zinc finger protein ZNF202 in human lipid
            metabolism
  JOURNAL   J Biol Chem 275 (21), 15685-15690 (2000)
   PUBMED   10748193
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Monaco,C., Helmer Citterich,M., Caprini,E., Vorechovsky,I.,
            Russo,G., Croce,C.M., Barbanti-Brodano,G. and Negrini,M.
  TITLE     Molecular cloning and characterization of ZNF202: a new gene at
            11q23.3 encoding testis-specific zinc finger proteins
  JOURNAL   Genomics 52 (3), 358-362 (1998)
   PUBMED   9790754
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY056142.1, BC013382.2, DA770117.1, AL162031.1, H89560.1, H89561.1
            and AP000868.4.
            
            On Dec 17, 2004 this sequence version replaced NP_003446.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013382.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000530393.6/ ENSP00000432504.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.1"
     Protein         1..648
                     /product="zinc finger protein 202 isoform 1"
                     /note="zinc finger protein with KRAB and SCAN domains 10"
                     /calculated_mol_wt=74590
     Region          43..153
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          146..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95125.4)"
     Region          237..297
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          397..>644
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          399..419
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(404,406,408,410..411,414..415,418,432,434,438..439,
                     442..443,446,488,490,492,494..495,498..499,502)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          427..447
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95125.4)"
     Region          483..503
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          511..531
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          539..559
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          567..587
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(572,574,576,578..579,582..583,586,600,602,606..607,
                     610..611,614,628,630,632,634..635,638..639,642)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          595..615
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          623..643
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..648
                     /gene="ZNF202"
                     /gene_synonym="ZKSCAN10; ZSCAN42"
                     /coded_by="NM_003455.4:406..2352"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8443.1"
                     /db_xref="GeneID:7753"
                     /db_xref="HGNC:HGNC:12994"
                     /db_xref="MIM:603430"
ORIGIN      
        1 matavepedq dlweeegilm vkleddftcr pesvlqrddp vletshqnfr rfryqeaasp
       61 realirlrel chqwlrperr tkeqilellv leqfltvlpg elqswvrgqr pesgeeavtl
      121 veglqkqprr prrwvtvhvh gqevlseetv hlgvepespn elqdpvqsst peqspeettq
      181 spdlgapaeq rphqeeelqt lqesevpvpe dpdlpaerss gdsemvallt alsqglvtfk
      241 dvavcfsqdq wsdldptqke fygeyvleed cgivvslsfp iprpdeisqv reeepwvpdi
      301 qepqetqepe ilsftytgdr skdeeecleq edlsledihr pvlgepeihq tpdweivfed
      361 npgrlnerrf gtnisqvnsf vnlrettpvh pllgrhhdcs vcgksftcns hlvrhlrtht
      421 gekpykcmec gksytrsshl arhqkvhkmn apykyplnrk nleetspvtq aertpsvekp
      481 yrcddcgkhf rwtsdlvrhq rthtgekpff cticgksfsq ksvltthqri hlggkpylcg
      541 ecgedfsehr rylahrktha aeelylcsec grcfthsaaf akhlrghasv rpcrcnecgk
      601 sfsrrdhlvr hqrthtgekp ftcptcgksf srgyhlirhq rthsekts
//
LOCUS       NP_001355931             254 aa            linear   PRI 27-APR-2025
DEFINITION  aprataxin isoform j [Homo sapiens].
ACCESSION   NP_001355931 XP_024303350
VERSION     NP_001355931.1
DBSOURCE    REFSEQ: accession NM_001369002.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_024303350.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.199964.1,
                                           SRR3476690.153681.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..254
                     /product="aprataxin isoform j"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=28977
     Region          76..177
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(170,172,174..176)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            172
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          195..254
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..254
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001369002.1:385..1149"
                     /note="isoform j is encoded by transcript variant 23"
                     /db_xref="CCDS:CCDS47957.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mvnelypyiv efeeeaknpg lethrkrkrs gnsdsierda aqeaeagtgl epgsnsgqcs
       61 vplkkgkdap ikkeslghws qglkismqdp kmqvykdeqv vvikdkypka ryhwlvlpwt
      121 sisslkavar ehlellkhmh tvgekvivdf agssklrfrl gyhaipsmsh vhlhvisqdf
      181 dspclknkkh wnsfnteyfl esqaviemvq eagrvtvrdg mpellklplr checqqllps
      241 ipqlkehlrk hwtq
//
LOCUS       NP_001366                360 aa            linear   PRI 27-APR-2025
DEFINITION  deoxyribonuclease-2-alpha precursor [Homo sapiens].
ACCESSION   NP_001366
VERSION     NP_001366.1
DBSOURCE    REFSEQ: accession NM_001375.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Ueki,M., Fujihara,J., Kimura-Kataoka,K., Yamada,K., Takinami,Y.,
            Takeshita,H., Iida,R. and Yasuda,T.
  TITLE     Low genetic heterogeneity of copy number variations (CNVs) in the
            genes encoding the human deoxyribonucleases 1-like 3 and II
            potentially relevant to autoimmunity
  JOURNAL   PLoS One 14 (4), e0215479 (2019)
   PUBMED   31022206
  REMARK    GeneRIF: Study of the copy number variations (CNVs) for DNASE1L3
            and DNASE2 in Japanese and German populations found that only 2
            diploid copy numbers for these DNASE CNVs was distributed in both
            populations; no copy loss or gain was evident for any of the
            autoimmune-related DNase genes. These human autoimmune-related
            DNase genes show low genetic diversity of CNVs resulting in
            alterations of the in vivo levels of DNase activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Rodero,M.P., Tesser,A., Bartok,E., Rice,G.I., Della Mina,E.,
            Depp,M., Beitz,B., Bondet,V., Cagnard,N., Duffy,D., Dussiot,M.,
            Fremond,M.L., Gattorno,M., Guillem,F., Kitabayashi,N.,
            Porcheray,F., Rieux-Laucat,F., Seabra,L., Uggenti,C., Volpi,S.,
            Zeef,L.A.H., Alyanakian,M.A., Beltrand,J., Bianco,A.M.,
            Boddaert,N., Brouzes,C., Candon,S., Caorsi,R., Charbit,M.,
            Fabre,M., Faletra,F., Girard,M., Harroche,A., Hartmann,E.,
            Lasne,D., Marcuzzi,A., Neven,B., Nitschke,P., Pascreau,T.,
            Pastore,S., Picard,C., Picco,P., Piscianz,E., Polak,M.,
            Quartier,P., Rabant,M., Stocco,G., Taddio,A., Uettwiller,F.,
            Valencic,E., Vozzi,D., Hartmann,G., Barchet,W., Hermine,O.,
            Bader-Meunier,B., Tommasini,A. and Crow,Y.J.
  TITLE     Type I interferon-mediated autoinflammation due to DNase II
            deficiency
  JOURNAL   Nat Commun 8 (1), 2176 (2017)
   PUBMED   29259162
  REMARK    GeneRIF: Study identifies biallelic mutations in DNASE2, associated
            with a loss of DNase II endonuclease activity causing type I
            interferonopathy in three patients from two unrelated families.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Fischer,H., Buchberger,M., Napirei,M., Tschachler,E. and Eckhart,L.
  TITLE     Inactivation of DNase1L2 and DNase2 in keratinocytes suppresses DNA
            degradation during epidermal cornification and results in
            constitutive parakeratosis
  JOURNAL   Sci Rep 7 (1), 6433 (2017)
   PUBMED   28743926
  REMARK    GeneRIF: DNase2 participate in the degradation of DNA during
            cornification in the interfollicular epidermis of
            mice.Cornification of epidermal keratinocytes depends on the
            cooperation of DNase1L2 and DNase2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Yasuda,T., Takeshita,H., Iida,R., Nakajima,T., Hosomi,O.,
            Nakashima,Y., Mogi,K. and Kishi,K.
  TITLE     Chromosomal localization of a human deoxyribonuclease II gene
            (DNASE2) to 19p13.2-p13.1 using both the polymerase chain reaction
            and fluorescence in situ hybridization analysis
  JOURNAL   Biochem Biophys Res Commun 244 (3), 815-818 (1998)
   PUBMED   9535749
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Yasuda,T., Takeshita,H., Iida,R., Nakajima,T., Hosomi,O.,
            Nakashima,Y. and Kishi,K.
  TITLE     Molecular cloning of the cDNA encoding human deoxyribonuclease II
  JOURNAL   J Biol Chem 273 (5), 2610-2616 (1998)
   PUBMED   9446563
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Yasuda,T., Nadano,D., Awazu,S. and Kishi,K.
  TITLE     Human urine deoxyribonuclease II (DNase II) isoenzymes: a novel
            immunoaffinity purification, biochemical multiplicity, genetic
            heterogeneity and broad distribution among tissues and body fluids
  JOURNAL   Biochim Biophys Acta 1119 (2), 185-193 (1992)
   PUBMED   1540651
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Yasuda,T., Nadano,D., Sawazaki,K. and Kishi,K.
  TITLE     Genetic polymorphism of human deoxyribonuclease II (DNase II): low
            activity levels in urine and leukocytes are due to an autosomal
            recessive allele
  JOURNAL   Ann Hum Genet 56 (1), 1-10 (1992)
   PUBMED   1586130
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Murai,K., Yamanaka,M., Akagi,K. and Anai,M.
  TITLE     Purification and properties of deoxyribonuclease II from human
            urine
  JOURNAL   J Biochem 87 (4), 1097-1103 (1980)
   PUBMED   6248503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF060222.1 and AC020934.9.
            
            Summary: This gene encodes a member of the DNase family. The
            protein, located in the lysosome, hydrolyzes DNA under acidic
            conditions and mediates the breakdown of DNA during erythropoiesis
            and apoptosis. Two codominant alleles have been characterized,
            DNASE2*L (low activity) and DNASE2*H (high activity), that differ
            at one nucleotide in the promoter region. The DNASE2*H allele is
            represented in this record. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.28874.1,
                                           SRR3476690.755593.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151358 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222219.8/ ENSP00000222219.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..360
                     /product="deoxyribonuclease-2-alpha precursor"
                     /EC_number="3.1.22.1"
                     /note="acid DNase; R31240_2; DNase II alpha;
                     deoxyribonuclease-2-alpha; DNase II, lysosomal; lysosomal
                     DNase II; deoxyribonuclease II alpha; deoxyribonuclease
                     II, lysosomal"
                     /calculated_mol_wt=38033
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1566
     Region          18..336
                     /region_name="DNase_II"
                     /note="Deoxyribonuclease II; pfam03265"
                     /db_xref="CDD:460868"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (O00115.2)"
     Site            212
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O00115.2)"
     Site            266
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (O00115.2)"
     Site            290
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (O00115.2)"
     CDS             1..360
                     /gene="DNASE2"
                     /gene_synonym="AIPCS; DNASE2A; DNL; DNL2"
                     /coded_by="NM_001375.3:75..1157"
                     /db_xref="CCDS:CCDS12284.1"
                     /db_xref="GeneID:1777"
                     /db_xref="HGNC:HGNC:2960"
                     /db_xref="MIM:126350"
ORIGIN      
        1 miplllaall cvpagaltcy gdsgqpvdwf vvyklpalrg sgeaaqrglq ykyldessgg
       61 wrdgralins pegavgrslq plyrsntsql afllyndqpp qpskaqdssm rghtkgvlll
      121 dhdggfwlvh svpnfpppas saayswphsa ctygqtllcv sfpfaqfskm gkqltytypw
      181 vynyqlegif aqefpdlenv vkghhvsqep wnssitltsq agavfqsfak fskfgddlys
      241 gwlaaalgtn lqvqfwhktv gilpsncsdi wqvlnvnqia fpgpagpsfn stedhskwcv
      301 spkgpwtcvg dmnrnqgeeq rgggtlcaql palwkafqpl vknyqpcngm arkpsrayki
//
LOCUS       NP_036357                271 aa            linear   PRI 27-APR-2025
DEFINITION  cytosolic Fe-S cluster assembly factor NUBP2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_036357
VERSION     NP_036357.1
DBSOURCE    REFSEQ: accession NM_012225.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Shin,S.Y., Fauman,E.B., Petersen,A.K., Krumsiek,J., Santos,R.,
            Huang,J., Arnold,M., Erte,I., Forgetta,V., Yang,T.P., Walter,K.,
            Menni,C., Chen,L., Vasquez,L., Valdes,A.M., Hyde,C.L., Wang,V.,
            Ziemek,D., Roberts,P., Xi,L., Grundberg,E., Waldenberger,M.,
            Richards,J.B., Mohney,R.P., Milburn,M.V., John,S.L., Trimmer,J.,
            Theis,F.J., Overington,J.P., Suhre,K., Brosnan,M.J., Gieger,C.,
            Kastenmuller,G., Spector,T.D. and Soranzo,N.
  CONSRTM   Multiple Tissue Human Expression Resource (MuTHER) Consortium
  TITLE     An atlas of genetic influences on human blood metabolites
  JOURNAL   Nat Genet 46 (6), 543-550 (2014)
   PUBMED   24816252
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Okuno,T., Yamabayashi,H. and Kogure,K.
  TITLE     Comparison of intracellular localization of Nubp1 and Nubp2 using
            GFP fusion proteins
  JOURNAL   Mol Biol Rep 37 (3), 1165-1168 (2010)
   PUBMED   19263241
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Stehling,O., Netz,D.J., Niggemeyer,B., Rosser,R., Eisenstein,R.S.,
            Puccio,H., Pierik,A.J. and Lill,R.
  TITLE     Human Nbp35 is essential for both cytosolic iron-sulfur protein
            assembly and iron homeostasis
  JOURNAL   Mol Cell Biol 28 (17), 5517-5528 (2008)
   PUBMED   18573874
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Roy,A., Solodovnikova,N., Nicholson,T., Antholine,W. and
            Walden,W.E.
  TITLE     A novel eukaryotic factor for cytosolic Fe-S cluster assembly
  JOURNAL   EMBO J 22 (18), 4826-4835 (2003)
   PUBMED   12970194
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Nakashima,H., Grahovac,M.J., Mazzarella,R., Fujiwara,H.,
            Kitchen,J.R., Threat,T.A. and Ko,M.S.
  TITLE     Two novel mouse genes--Nubp2, mapped to the t-complex on chromosome
            17, and Nubp1, mapped to chromosome 16--establish a new gene family
            of nucleotide-binding proteins in eukaryotes
  JOURNAL   Genomics 60 (2), 152-160 (1999)
   PUBMED   10486206
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU189242.1, BC002768.2,
            AK300696.1 and BF439443.1.
            
            Summary: This gene encodes an adenosine triphosphate (ATP) and
            metal-binding protein that is required for the assembly of
            cyotosolic iron-sulfur proteins. The encoded protein functions in a
            heterotetramer with nucleotide-binding protein 1 (NUBP1).
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Oct 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008005.1, AK001023.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262302.14/ ENSP00000262302.9
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..271
                     /product="cytosolic Fe-S cluster assembly factor NUBP2
                     isoform 1"
                     /note="homolog of yeast cytosolic Fe-S cluster deficient
                     1; nucleotide binding protein 2 (MinD homolog, E. coli);
                     nucleotide-binding protein 2; cytosolic Fe-S cluster
                     assembly factor NUBP2"
                     /calculated_mol_wt=28694
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03039,
                     ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9Y5Y2.1)"
     Region          12..263
                     /region_name="ParA"
                     /note="NUBPL iron-transfer P-loop NTPase; pfam10609"
                     /db_xref="CDD:431392"
     Site            order(23..30,163,165,190..191,227..229,232..233)
                     /site_type="active"
                     /db_xref="CDD:349757"
     Site            order(23..25,54..55,57,60..61,106..107,137,139,142,169,
                     172,228,230..231,233)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349757"
     CDS             1..271
                     /gene="NUBP2"
                     /gene_synonym="CFD1; CIAO6; NBP 2; NUBP1"
                     /coded_by="NM_012225.4:62..877"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10445.1"
                     /db_xref="GeneID:10101"
                     /db_xref="HGNC:HGNC:8042"
                     /db_xref="MIM:610779"
ORIGIN      
        1 meaaaepgnl agvrhiilvl sgkggvgkst istelalalr hagkkvgild vdlcgpsipr
       61 mlgaqgravh qcdrgwapvf ldreqsislm svgfllekpd eavvwrgpkk nalikqfvsd
      121 vawgeldylv vdtppgtsde hmatiealrp yqplgalvvt tpqavsvgdv rreltfcrkt
      181 glrvmgiven msgftcphct ectsvfsrgg geelaqlagv pflgsvpldp almrtleegh
      241 dfiqefpgsp afaaltsiaq kildatpacl p
//
LOCUS       NP_001181                392 aa            linear   PRI 27-APR-2025
DEFINITION  branched-chain-amino-acid aminotransferase, mitochondrial isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001181
VERSION     NP_001181.2
DBSOURCE    REFSEQ: accession NM_001190.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Kang,Z.R., Jiang,S., Han,J.X., Gao,Y., Xie,Y., Chen,J., Liu,Q.,
            Yu,J., Zhao,X., Hong,J., Chen,H., Chen,Y.X., Chen,H. and Fang,J.Y.
  TITLE     Deficiency of BCAT2-mediated branched-chain amino acid catabolism
            promotes colorectal cancer development
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (2), 166941 (2024)
   PUBMED   37926361
  REMARK    GeneRIF: Deficiency of BCAT2-mediated branched-chain amino acid
            catabolism promotes colorectal cancer development.
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Tian,Y., Ma,J., Wang,H., Yi,X., Wang,H., Zhang,H., Guo,S., Yang,Y.,
            Zhang,B., Du,J., Shi,Q., Gao,T., Guo,W. and Li,C.
  TITLE     BCAT2 promotes melanoma progression by activating lipogenesis via
            the epigenetic regulation of FASN and ACLY expressions
  JOURNAL   Cell Mol Life Sci 80 (11), 315 (2023)
   PUBMED   37801083
  REMARK    GeneRIF: BCAT2 promotes melanoma progression by activating
            lipogenesis via the epigenetic regulation of FASN and ACLY
            expressions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Vargas-Morales,J.M., Guizar-Heredia,R., Mendez-Garcia,A.L.,
            Palacios-Gonzalez,B., Schcolnik-Cabrera,A., Granados,O.,
            Lopez-Barradas,A.M., Vazquez-Manjarrez,N., Medina-Vera,I.,
            Aguilar-Lopez,M., Tovar-Palacio,C., Ordaz-Nava,G.,
            Rocha-Viggiano,A.K., Medina-Cerda,E., Torres,N., Ordovas,J.M.,
            Tovar,A.R., Guevara-Cruz,M. and Noriega,L.G.
  TITLE     Association of BCAT2 and BCKDH polymorphisms with clinical,
            anthropometric and biochemical parameters in young adults
  JOURNAL   Nutr Metab Cardiovasc Dis 31 (11), 3210-3218 (2021)
   PUBMED   34511290
  REMARK    GeneRIF: Association of BCAT2 and BCKDH polymorphisms with
            clinical, anthropometric and biochemical parameters in young
            adults.
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Yennawar,N., Dunbar,J., Conway,M., Hutson,S. and Farber,G.
  TITLE     The structure of human mitochondrial branched-chain
            aminotransferase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 57 (Pt 4), 506-515 (2001)
   PUBMED   11264579
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Than,N.G., Sumegi,B., Than,G.N., Bellyei,S. and Bohn,H.
  TITLE     Molecular cloning and characterization of placental tissue protein
            18 (PP18a)/human mitochondrial branched-chain aminotransferase
            (BCATm) and its novel alternatively spliced PP18b variant
  JOURNAL   Placenta 22 (2-3), 235-243 (2001)
   PUBMED   11170829
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Bledsoe,R.K., Dawson,P.A. and Hutson,S.M.
  TITLE     Cloning of the rat and human mitochondrial branched chain
            aminotransferases (BCATm)
  JOURNAL   Biochim Biophys Acta 1339 (1), 9-13 (1997)
   PUBMED   9165094
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Eden,A., Simchen,G. and Benvenisty,N.
  TITLE     Two yeast homologs of ECA39, a target for c-Myc regulation, code
            for cytosolic and mitochondrial branched-chain amino acid
            aminotransferases
  JOURNAL   J Biol Chem 271 (34), 20242-20245 (1996)
   PUBMED   8702755
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Bohn,H. and Winckler,W.
  TITLE     Isolation and characterization of four new placental tissue
            proteins (PP18, PP19, PP20, PP21)
  JOURNAL   Arch Gynecol 236 (4), 235-242 (1985)
   PUBMED   3896163
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Naylor,S.L. and Shows,T.B.
  TITLE     Branched-chain aminotransferase deficiency in Chinese hamster cells
            complemented by two independent genes on human chromosomes 12 and
            19
  JOURNAL   Somatic Cell Genet 6 (5), 641-652 (1980)
   PUBMED   6933702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA129578.1, BC001900.1 and
            CA310873.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 27, 2004 this sequence version replaced NP_001181.1.
            
            Summary: This gene encodes a branched chain aminotransferase found
            in mitochondria. The encoded protein forms a dimer that catalyzes
            the first step in the production of the branched chain amino acids
            leucine, isoleucine, and valine. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (a) encodes the longest isoform
            (a), also known as PP18a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.87615.1, AK223522.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000316273.11/
                                                  ENSP00000322991.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..392
                     /product="branched-chain-amino-acid aminotransferase,
                     mitochondrial isoform a precursor"
                     /EC_number="2.6.1.42"
                     /note="branched chain aminotransferase 2, mitochondrial;
                     placental protein 18; branched chain amino-acid
                     transaminase 2, mitochondrial"
                     /calculated_mol_wt=41264
     transit_peptide 1..27
                     /calculated_mol_wt=3042
     mat_peptide     28..392
                     /product="branched-chain-amino-acid aminotransferase,
                     mitochondrial isoform a"
                     /calculated_mol_wt=41264
     Region          87..382
                     /region_name="BCAT_beta_family"
                     /note="Branched-chain aminotransferase catalyses the
                     transamination of the branched-chain amino acids leusine,
                     isoleucine and valine to their respective alpha-keto
                     acids, alpha-ketoisocaproate,
                     alpha-keto-beta-methylvalerate and alpha-ketoisovalerate.
                     The...; cd01557"
                     /db_xref="CDD:238798"
     Site            order(87..91,94..98,100,102,133,170,172,178..180,184,191,
                     231,236,238,242,256)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:238798"
     Site            order(97,102,126,182,229,234,264,296..297,340)
                     /site_type="active"
                     /note="substrate-cofactor binding pocket [active]"
                     /db_xref="CDD:238798"
     Site            229
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238798"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15382.2)"
     CDS             1..392
                     /gene="BCAT2"
                     /gene_synonym="BCAM; BCATM; BCT2; HVLI; PP18"
                     /coded_by="NM_001190.4:23..1201"
                     /note="isoform a precursor is encoded by transcript
                     variant a"
                     /db_xref="CCDS:CCDS12735.1"
                     /db_xref="GeneID:587"
                     /db_xref="HGNC:HGNC:977"
                     /db_xref="MIM:113530"
ORIGIN      
        1 maaaalgqiw arkllsvpwl lcgprryass sfkaadlqle mtqkphkkpg pgeplvfgkt
       61 ftdhmlmvew ndkgwgqpri qpfqnltlhp assslhyslq lfegmkafkg kdqqvrlfrp
      121 wlnmdrmlrs amrlclpsfd klellecirr lievdkdwvp daagtslyvr pvlignepsl
      181 gvsqptrall fvilcpvgay fpggsvtpvs lladpafira wvggvgnykl ggnygptvlv
      241 qqealkrgce qvlwlygpdh qltevgtmni fvywthedgv lelvtpplng vilpgvvrqs
      301 lldmaqtwge frvvertitm kqllraleeg rvrevfgsgt acqvcpvhri lykdrnlhip
      361 tmengpelil rfqkelkeiq ygirahewmf pv
//
LOCUS       NP_001347274             192 aa            linear   ROD 27-APR-2025
DEFINITION  max-interacting protein 1 isoform c [Mus musculus].
ACCESSION   NP_001347274 XP_006526803
VERSION     NP_001347274.1
DBSOURCE    REFSEQ: accession NM_001360345.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Li,X., Xiao,S., Li,F., Fang,K., Wen,J. and Gong,H.
  TITLE     Max interacting protein 1 induces IL-17-producing T
            helper/regulatory T imbalance in osteoarthritis by upregulating
            tectonic family member 2
  JOURNAL   Tissue Cell 78, 101906 (2022)
   PUBMED   36049372
  REMARK    GeneRIF: Max interacting protein 1 induces IL-17-producing T
            helper/regulatory T imbalance in osteoarthritis by upregulating
            tectonic family member 2.
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Menendez-Montes,I., Escobar,B., Palacios,B., Gomez,M.J.,
            Izquierdo-Garcia,J.L., Flores,L., Jimenez-Borreguero,L.J.,
            Aragones,J., Ruiz-Cabello,J., Torres,M. and Martin-Puig,S.
  TITLE     Myocardial VHL-HIF Signaling Controls an Embryonic Metabolic Switch
            Essential for Cardiac Maturation
  JOURNAL   Dev Cell 39 (6), 724-739 (2016)
   PUBMED   27997827
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Cui,W., Dai,X., Marcho,C., Han,Z., Zhang,K., Tremblay,K.D. and
            Mager,J.
  TITLE     Towards Functional Annotation of the Preimplantation Transcriptome:
            An RNAi Screen in Mammalian Embryos
  JOURNAL   Sci Rep 6, 37396 (2016)
   PUBMED   27869233
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Childress,P., Stayrook,K.R., Alvarez,M.B., Wang,Z., Shao,Y.,
            Hernandez-Buquer,S., Mack,J.K., Grese,Z.R., He,Y., Horan,D.,
            Pavalko,F.M., Warden,S.J., Robling,A.G., Yang,F.C., Allen,M.R.,
            Krishnan,V., Liu,Y. and Bidwell,J.P.
  TITLE     Genome-Wide Mapping and Interrogation of the Nmp4 Antianabolic Bone
            Axis
  JOURNAL   Mol Endocrinol 29 (9), 1269-1285 (2015)
   PUBMED   26244796
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Dugast-Darzacq,C., Pirity,M., Blanck,J.K., Scherl,A. and
            Schreiber-Agus,N.
  TITLE     Mxi1-SRalpha: a novel Mxi1 isoform with enhanced transcriptional
            repression potential
  JOURNAL   Oncogene 23 (55), 8887-8899 (2004)
   PUBMED   15467743
  REMARK    GeneRIF: Mxi1-SRalpha is an isoform with enhanced transcriptional
            repression potential
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Hurlin,P.J., Queva,C., Koskinen,P.J., Steingrimsson,E., Ayer,D.E.,
            Copeland,N.G., Jenkins,N.A. and Eisenman,R.N.
  TITLE     Mad3 and Mad4: novel Max-interacting transcriptional repressors
            that suppress c-myc dependent transformation and are expressed
            during neural and epidermal differentiation
  JOURNAL   EMBO J 14 (22), 5646-5659 (1995)
   PUBMED   8521822
  REMARK    Erratum:[EMBO J. 1996 Apr 15;15(8):2030. PMID: 8617250]
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Steingrimsson,E., Sawadogo,M., Gilbert,D.J., Zervos,A.S., Brent,R.,
            Blanar,M.A., Fisher,D.E., Copeland,N.G. and Jenkins,N.A.
  TITLE     Murine chromosomal location of five bHLH-Zip transcription factor
            genes
  JOURNAL   Genomics 28 (2), 179-183 (1995)
   PUBMED   8530024
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Schreiber-Agus,N., Chin,L., Chen,K., Torres,R., Rao,G., Guida,P.,
            Skoultchi,A.I. and DePinho,R.A.
  TITLE     An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic
            activity and interacts with a homolog of the yeast transcriptional
            repressor SIN3
  JOURNAL   Cell 80 (5), 777-786 (1995)
   PUBMED   7889571
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Shimizu,E., Shirasawa,H., Kodama,K., Koseki,K., Sato,T. and
            Simizu,B.
  TITLE     Cloning and sequencing of the murine Mxi1 cDNA
  JOURNAL   Gene 152 (2), 283-284 (1995)
   PUBMED   7835718
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Edelhoff,S., Ayer,D.E., Zervos,A.S., Steingrimsson,E.,
            Jenkins,N.A., Copeland,N.G., Eisenman,R.N., Brent,R. and
            Disteche,C.M.
  TITLE     Mapping of two genes encoding members of a distinct subfamily of
            MAX interacting proteins: MAD to human chromosome 2 and mouse
            chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome
            19
  JOURNAL   Oncogene 9 (2), 665-668 (1994)
   PUBMED   8290278
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC133451.14.
            
            On Feb 1, 2018 this sequence version replaced XP_006526803.1.
            
            Summary: This gene encodes a protein containing a helix-loop-helix
            domain characteristic of transcription factors, which allows
            heterodimerization and sequence-specific DNA binding. The encoded
            protein is related to a family of Myc/Max/Mad proteins that are
            involved in the regulation of several cellular processes. The
            protein encoded by this gene is a transcriptional repressor thought
            to negatively regulate Myc function. Three alternatively spliced
            transcripts encoding different isoforms have been described.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and 5'
            coding region, compared to variant 1. The resulting isoform (c) is
            shorter and has a distinct N-terminus, compared to isoform a. This
            variant is supported by mRNAs and ESTs but the existence of the
            protein product has not been verified experimentally. Variants 3-6
            encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK144219.1, SRR1660813.145702.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 47.53 cM"
     Protein         1..192
                     /product="max-interacting protein 1 isoform c"
                     /note="max-interacting protein 1"
                     /calculated_mol_wt=21524
     Region          32..111
                     /region_name="bHLHzip_MXI1"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in Max-interacting protein 1 (MXI1) and similar
                     proteins; cd18930"
                     /db_xref="CDD:381500"
     Site            order(36..37,40..41,43..44,48,67..69)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381500"
     Site            order(47..48,50..55,57..58,70,73,77,79..81,83..84,86..87,
                     90,94,97..98,100..101,104..105,107..108)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381500"
     Site            order(47,50..51,53..54,57..58,70,73,77,79..81,83..84,
                     86..87,90,94,97..98,100..101,104..105,107..108)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381500"
     CDS             1..192
                     /gene="Mxi1"
                     /gene_synonym="bHLHc11; Gm10197; Mad2"
                     /coded_by="NM_001360345.1:429..1007"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS38023.1"
                     /db_xref="GeneID:17859"
                     /db_xref="MGI:MGI:97245"
ORIGIN      
        1 mpsprlqhsk pprrlsraqk hssgssntst anrsthnele knrrahlrlc lerlkvlipl
       61 gpdctrhttl gllnkakahi kkleeaerks qhqlenlere qrflkrrleq lqgpqemeri
      121 rmdsigstis sdrsdseree ievdvestef shgeadsvst tsisdlddhs slqsvgsdeg
      181 yssasvklsf as
//
LOCUS       NP_005730                797 aa            linear   PRI 27-APR-2025
DEFINITION  RAS guanyl-releasing protein 1 isoform a [Homo sapiens].
ACCESSION   NP_005730
VERSION     NP_005730.2
DBSOURCE    REFSEQ: accession NM_005739.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Zhou,J., Xu,B., He,F., Shu,Y., Chen,X., Liu,Z., Sun,B. and Zhang,W.
  TITLE     Association of RASGRP1 polymorphism with vascular complications in
            Chinese diabetic patients with glycemic control and
            antihypertensive treatment
  JOURNAL   Cardiovasc Diabetol 23 (1), 166 (2024)
   PUBMED   38730425
  REMARK    GeneRIF: Association of RASGRP1 polymorphism with vascular
            complications in Chinese diabetic patients with glycemic control
            and antihypertensive treatment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Hsu,T.C., Rodrigues,G.O.L., Winer,H., Hixon,J.A., Li,W.,
            Tarasova,N.I. and Durum,S.K.
  TITLE     A Focused Review of Ras Guanine Nucleotide-Releasing Protein 1 in
            Immune Cells and Cancer
  JOURNAL   Int J Mol Sci 24 (2), 1652 (2023)
   PUBMED   36675167
  REMARK    GeneRIF: A Focused Review of Ras Guanine Nucleotide-Releasing
            Protein 1 in Immune Cells and Cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 797)
  AUTHORS   De Rosa,A., Di Maio,A., Torretta,S., Garofalo,M., Giorgelli,V.,
            Masellis,R., Nuzzo,T., Errico,F., Bertolino,A., Subramaniam,S.,
            Rampino,A. and Usiello,A.
  TITLE     Abnormal RasGRP1 Expression in the Post-Mortem Brain and Blood
            Serum of Schizophrenia Patients
  JOURNAL   Biomolecules 12 (2), 328 (2022)
   PUBMED   35204828
  REMARK    GeneRIF: Abnormal RasGRP1 Expression in the Post-Mortem Brain and
            Blood Serum of Schizophrenia Patients.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Baars,M.J.D., Douma,T., Simeonov,D.R., Myers,D.R., Kulhanek,K.,
            Banerjee,S., Zwakenberg,S., Baltissen,M.P., Amini,M., de Roock,S.,
            van Wijk,F., Vermeulen,M., Marson,A., Roose,J.P. and Vercoulen,Y.
  TITLE     Dysregulated RASGRP1 expression through RUNX1 mediated
            transcription promotes autoimmunity
  JOURNAL   Eur J Immunol 51 (2), 471-482 (2021)
   PUBMED   33065764
  REMARK    GeneRIF: Dysregulated RASGRP1 expression through RUNX1 mediated
            transcription promotes autoimmunity.
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Rchiad,Z., Haidar,M., Ansari,H.R., Tajeri,S., Mfarrej,S., Ben
            Rached,F., Kaushik,A., Langsley,G. and Pain,A.
  TITLE     Novel tumour suppressor roles for GZMA and RASGRP1 in Theileria
            annulata-transformed macrophages and human B lymphoma cells
  JOURNAL   Cell Microbiol 22 (12), e13255 (2020)
   PUBMED   32830401
  REMARK    GeneRIF: Novel tumour suppressor roles for GZMA and RASGRP1 in
            Theileria annulata-transformed macrophages and human B lymphoma
            cells.
REFERENCE   6  (residues 1 to 797)
  AUTHORS   Topham,M.K. and Prescott,S.M.
  TITLE     Diacylglycerol kinase zeta regulates Ras activation by a novel
            mechanism
  JOURNAL   J Cell Biol 152 (6), 1135-1143 (2001)
   PUBMED   11257115
REFERENCE   7  (residues 1 to 797)
  AUTHORS   Ebinu,J.O., Stang,S.L., Teixeira,C., Bottorff,D.A., Hooton,J.,
            Blumberg,P.M., Barry,M., Bleakley,R.C., Ostergaard,H.L. and
            Stone,J.C.
  TITLE     RasGRP links T-cell receptor signaling to Ras
  JOURNAL   Blood 95 (10), 3199-3203 (2000)
   PUBMED   10807788
REFERENCE   8  (residues 1 to 797)
  AUTHORS   Bottorff,D., Ebinu,J. and Stone,J.C.
  TITLE     RasGRP, a Ras activator: mouse and human cDNA sequences and
            chromosomal positions
  JOURNAL   Mamm Genome 10 (4), 358-361 (1999)
   PUBMED   10087292
REFERENCE   9  (residues 1 to 797)
  AUTHORS   Kawasaki,H., Springett,G.M., Toki,S., Canales,J.J., Harlan,P.,
            Blumenstiel,J.P., Chen,E.J., Bany,I.A., Mochizuki,N., Ashbacher,A.,
            Matsuda,M., Housman,D.E. and Graybiel,A.M.
  TITLE     A Rap guanine nucleotide exchange factor enriched highly in the
            basal ganglia
  JOURNAL   Proc Natl Acad Sci U S A 95 (22), 13278-13283 (1998)
   PUBMED   9789079
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1999 Jan 5;96(1):318]
REFERENCE   10 (residues 1 to 797)
  AUTHORS   Ebinu,J.O., Bottorff,D.A., Chan,E.Y., Stang,S.L., Dunn,R.J. and
            Stone,J.C.
  TITLE     RasGRP, a Ras guanyl nucleotide- releasing protein with calcium-
            and diacylglycerol-binding motifs
  JOURNAL   Science 280 (5366), 1082-1086 (1998)
   PUBMED   9582122
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124306.4, DA993002.1,
            AK314091.1, BC109296.1, BU431038.1, AF081195.1 and AA742351.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 19, 2008 this sequence version replaced NP_005730.1.
            
            Summary: This gene is a member of a family of genes characterized
            by the presence of a Ras superfamily guanine nucleotide exchange
            factor (GEF) domain. It functions as a diacylglycerol
            (DAG)-regulated nucleotide exchange factor specifically activating
            Ras through the exchange of bound GDP for GTP. It activates the
            Erk/MAP kinase cascade and regulates T-cells and B-cells
            development, homeostasis and differentiation. Alternatively spliced
            transcript variants encoding different isoforms have been
            identified. Altered expression of the different isoforms of this
            protein may be a cause of susceptibility to systemic lupus
            erythematosus (SLE). [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript, and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF081195.1, BC032849.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310803.10/ ENSP00000310244.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..797
                     /product="RAS guanyl-releasing protein 1 isoform a"
                     /note="guanine nucleotide exchange factor, calcium- and
                     DAG-regulated, Rap1A; RAS guanyl nucleotide-releasing
                     protein 1; calcium and DAG-regulated guanine nucleotide
                     exchange factor II; ras activator RasGRP; RAS guanyl
                     releasing protein 1 (calcium and DAG-regulated); calcium-
                     and diacylglycerol-regulated guanine nucleotide exchange
                     factor II"
                     /calculated_mol_wt=90271
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95267.2)"
     Region          54..175
                     /region_name="RasGEFN"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     GTPases; N-terminal motif; smart00229"
                     /db_xref="CDD:214571"
     Region          57..110
                     /region_name="Ras exchanger motif region, required for
                     transforming activity. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O95267.2)"
     Site            order(72,123..124,127,130..131,166..167,170,177)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:100121"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000269|PubMed:15657177,
                     ECO:0000269|PubMed:15899849; propagated from
                     UniProtKB/Swiss-Prot (O95267.2)"
     Region          201..437
                     /region_name="RasGEF"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     small GTPases; smart00147"
                     /db_xref="CDD:214539"
     Site            order(234..236,244..245,247..249,251..252,255..256,259,
                     292,295..296,298..300,302..305,307..308,328,331,336..338,
                     341,354..356,359..361,363..365,367..370,385,389,424,
                     427..428)
                     /site_type="other"
                     /note="Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:238087"
     Region          <471..527
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          540..594
                     /region_name="C1_RASGRP1"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in RAS guanyl-releasing protein 1 (RASGRP1) and
                     similar proteins; cd20860"
                     /db_xref="CDD:410410"
     Site            order(547..553,561..565,568)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410410"
     Region          673..694
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95267.2)"
     Region          686..694
                     /region_name="Suppress the PT region-mediated
                     translocation to plasma membrane. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O95267.2)"
     Region          718..797
                     /region_name="PT region, mediates the BCR-dependent
                     translocation to plasma membrane. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O95267.2)"
     Region          739..793
                     /region_name="cc_RasGRP1_C"
                     /note="C-terminal coiled-coil domain of RAS
                     guanyl-releasing protein 1 (RasGRP1) and similar proteins;
                     cd22290"
                     /db_xref="CDD:412086"
     Site            order(745..748,751,754..755,758..759,761..762,765..766,
                     768..769,772,776,779..780,782)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:412086"
     CDS             1..797
                     /gene="RASGRP1"
                     /gene_synonym="CALDAG-GEFI; CALDAG-GEFII; IMD64; RASGRP"
                     /coded_by="NM_005739.4:187..2580"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45222.1"
                     /db_xref="GeneID:10125"
                     /db_xref="HGNC:HGNC:9878"
                     /db_xref="MIM:603962"
ORIGIN      
        1 mgtlgkarea prkpshgcra askarleakp anspfpshps lahitqfrmm vslghlakga
       61 slddlidsci qsfdadgnlc rsnqllqvml tmhrivissa ellqkvitly kdalaknspg
      121 lclkicyfvr ywitefwvmf kmdasltdtm eefqelvkak geelhcrlid ttqinardws
      181 rkltqriksn tskkrkvsll fdhlepeels ehltylefks frrisfsdyq nylvnscvke
      241 nptmersial cngisqwvql mvlsrptpql raevfikfiq vaqklhqlqn fntlmavigg
      301 lchssisrlk etsshvphei nkvlgemtel lsssrnydny rraygectdf kipilgvhlk
      361 dlislyeamp dyledgkvnv hkllalynhi selvqlqeva ppleankdlv hlltlsldly
      421 ytedeiyels yareprnhra ppltpskppv vvdwasgvsp kpdpktiskh vqrmvdsvfk
      481 nydhdqdgyi sqeefekiaa sfpfsfcvmd kdreglisrd eitayfmras siysklglgf
      541 phnfqettyl kptfcdncag flwgvikqgy rckdcgmnch kqckdlvvfe ckkraknpva
      601 ptenntsvgp vsnlcslgak dllhapeegp ftfpngeave hgeeskdrti mlmgvssqki
      661 slrlkravah katqtesqpw igsegpsgpf vlssprktaq dtlyvlpspt spcpspvlvr
      721 krafvkwenk dslikskeel rhlrlptyqe leqeintlka dndalkiqlk yaqkkieslq
      781 leksnhvlaq meqgdcs
//
LOCUS       NP_005515                280 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor HES-1 [Homo sapiens].
ACCESSION   NP_005515
VERSION     NP_005515.1
DBSOURCE    REFSEQ: accession NM_005524.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Lodewijk,G.A., de Geus,M., Guimaraes,R.L.F.P. and Jacobs,F.M.J.
  TITLE     Emergence of the ZNF675 Gene During Primate Evolution-Influenced
            Human Neurodevelopment Through Changing HES1 Autoregulation
  JOURNAL   J Comp Neurol 532 (7), e25648 (2024)
   PUBMED   38958676
  REMARK    GeneRIF: Emergence of the ZNF675 Gene During Primate
            Evolution-Influenced Human Neurodevelopment Through Changing HES1
            Autoregulation.
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Sfeir,N., Kajdan,M., Jalaguier,S., Bonnet,S., Teyssier,C.,
            Pyrdziak,S., Yuan,R., Bousquet,E., Maraver,A., Bernex,F., Pirot,N.,
            Boissiere-Michot,F., Castet-Nicolas,A., Lapierre,M. and
            Cavailles,V.
  TITLE     RIP140 regulates transcription factor HES1 oscillatory expression
            and mitogenic activity in colon cancer cells
  JOURNAL   Mol Oncol 18 (6), 1510-1530 (2024)
   PUBMED   38459621
  REMARK    GeneRIF: RIP140 regulates transcription factor HES1 oscillatory
            expression and mitogenic activity in colon cancer cells.
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Xu,Y., Mao,S., Fan,H., Wan,J., Wang,L., Zhang,M., Zhu,S., Yuan,J.,
            Lu,Y., Wang,Z., Yu,B., Jiang,Z. and Huang,Y.
  TITLE     LINC MIR503HG Controls SC-beta Cell Differentiation and Insulin
            Production by Targeting CDH1 and HES1
  JOURNAL   Adv Sci (Weinh) 11 (13), e2305631 (2024)
   PUBMED   38243869
  REMARK    GeneRIF: LINC MIR503HG Controls SC-beta Cell Differentiation and
            Insulin Production by Targeting CDH1 and HES1.
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Zhang,C., Ye,W., Zhao,M., Long,L., Xia,D. and Fan,Z.
  TITLE     MLL1 inhibits the neurogenic potential of SCAPs by interacting with
            WDR5 and repressing HES1
  JOURNAL   Int J Oral Sci 15 (1), 48 (2023)
   PUBMED   37852994
  REMARK    GeneRIF: MLL1 inhibits the neurogenic potential of SCAPs by
            interacting with WDR5 and repressing HES1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Wang,L., Gu,W., Zou,B., Kalady,M., Xin,W. and Zhou,L.
  TITLE     Loss of HES1 expression is associated with extracellular matrix
            remodeling and tumor immune suppression in KRAS mutant colon
            adenocarcinomas
  JOURNAL   Sci Rep 13 (1), 15999 (2023)
   PUBMED   37749297
  REMARK    GeneRIF: Loss of HES1 expression is associated with extracellular
            matrix remodeling and tumor immune suppression in KRAS mutant colon
            adenocarcinomas.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Votruba,M., Payne,A., Moore,A.T. and Bhattacharya,S.S.
  TITLE     Dominant optic atrophy: exclusion and fine genetic mapping of the
            candidate gene, HRY
  JOURNAL   Mamm Genome 9 (10), 784-787 (1998)
   PUBMED   9745030
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Strom,A., Castella,P., Rockwood,J., Wagner,J. and Caudy,M.
  TITLE     Mediation of NGF signaling by post-translational inhibition of
            HES-1, a basic helix-loop-helix repressor of neuronal
            differentiation
  JOURNAL   Genes Dev 11 (23), 3168-3181 (1997)
   PUBMED   9389649
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Grbavec,D. and Stifani,S.
  TITLE     Molecular interaction between TLE1 and the carboxyl-terminal domain
            of HES-1 containing the WRPW motif
  JOURNAL   Biochem Biophys Res Commun 223 (3), 701-705 (1996)
   PUBMED   8687460
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Feder,J.N., Li,L., Jan,L.Y. and Jan,Y.N.
  TITLE     Genomic cloning and chromosomal localization of HRY, the human
            homolog to the Drosophila segmentation gene, hairy
  JOURNAL   Genomics 20 (1), 56-61 (1994)
   PUBMED   8020957
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Takebayashi,K., Sasai,Y., Sakai,Y., Watanabe,T., Nakanishi,S. and
            Kageyama,R.
  TITLE     Structure, chromosomal locus, and promoter analysis of the gene
            encoding the mouse helix-loop-helix factor HES-1. Negative
            autoregulation through the multiple N box elements
  JOURNAL   J Biol Chem 269 (7), 5150-5156 (1994)
   PUBMED   7906273
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK000415.1, AI370424.1 and
            AC080129.26.
            
            Summary: This protein belongs to the basic helix-loop-helix family
            of transcription factors. It is a transcriptional repressor of
            genes that require a bHLH protein for their transcription. The
            protein has a particular type of basic domain that contains a helix
            interrupting protein that binds to the N-box rather than the
            canonical E-box. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA569975.1, AK000415.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000232424.4/ ENSP00000232424.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..280
                     /product="transcription factor HES-1"
                     /note="hairy-like protein; class B basic helix-loop-helix
                     protein 39; hairy homolog"
                     /calculated_mol_wt=29410
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14469.1)"
     Region          33..95
                     /region_name="bHLH-O_HES1_4"
                     /note="basic helix-loop-helix-orange (bHLH-O) domain found
                     in hairy and enhancer of split HES-1, HES-4 and similar
                     proteins; cd11459"
                     /db_xref="CDD:381465"
     Site            order(36,46..47,49..51,53..54,56..57,60..61,64,74,76..78,
                     81..82,84..85,87..89,91..92,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381465"
     Site            order(39..41,44,46..47,51,76..77)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381465"
     Region          109..148
                     /region_name="Hairy_orange"
                     /note="Hairy Orange; pfam07527"
                     /db_xref="CDD:462193"
     Region          157..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14469.1)"
     Region          254..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14469.1)"
     Region          275..278
                     /region_name="WRPW motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14469.1)"
     CDS             1..280
                     /gene="HES1"
                     /gene_synonym="bHLHb39; HES-1; HHL; HRY"
                     /coded_by="NM_005524.4:234..1076"
                     /db_xref="CCDS:CCDS3305.1"
                     /db_xref="GeneID:3280"
                     /db_xref="HGNC:HGNC:5192"
                     /db_xref="MIM:139605"
ORIGIN      
        1 mpadimekns sspvaatpas vnttpdkpkt asehrksskp imekrrrari neslsqlktl
       61 ildalkkdss rhsklekadi lemtvkhlrn lqraqmtaal stdpsvlgky ragfsecmne
      121 vtrflstceg vntevrtrll ghlancmtqi namtypgqph palqappppp pgpggpqhap
      181 fapppplvpi pggaapppgg apcklgsqag eaakvfggfq vvpapdgqfa flipngafah
      241 sgpvipvyts nsgtsvgpna vspssgpslt adsmwrpwrn
//
LOCUS       NP_001355106             473 aa            linear   ROD 27-APR-2025
DEFINITION  vasculin-like protein 1 [Mus musculus].
ACCESSION   NP_001355106
VERSION     NP_001355106.1
DBSOURCE    REFSEQ: accession NM_001368177.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Butterfield,N.C., Curry,K.F., Steinberg,J., Dewhurst,H.,
            Komla-Ebri,D., Mannan,N.S., Adoum,A.T., Leitch,V.D., Logan,J.G.,
            Waung,J.A., Ghirardello,E., Southam,L., Youlten,S.E.,
            Wilkinson,J.M., McAninch,E.A., Vancollie,V.E., Kussy,F.,
            White,J.K., Lelliott,C.J., Adams,D.J., Jacques,R., Bianco,A.C.,
            Boyde,A., Zeggini,E., Croucher,P.I., Williams,G.R. and
            Bassett,J.H.D.
  TITLE     Accelerating functional gene discovery in osteoarthritis
  JOURNAL   Nat Commun 12 (1), 467 (2021)
   PUBMED   33473114
  REMARK    Erratum:[Nat Commun. 2021 May 28;12(1):3302. doi:
            10.1038/s41467-021-23768-8. PMID: 34050183]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK077148.1, BC066034.1 and AL669953.7.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK077148.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384, SAMN00849387
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 53.22 cM"
     Protein         1..473
                     /product="vasculin-like protein 1"
                     /calculated_mol_wt=51835
     Region          14..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319; propagated from
                     UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Region          88..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Region          155..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9HC44; propagated from
                     UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Region          235..267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Region          281..316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9HC44; propagated from
                     UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Region          377..470
                     /region_name="Vasculin"
                     /note="Vascular protein family Vasculin-like 1; pfam15337"
                     /db_xref="CDD:464657"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9HC44; propagated from
                     UniProtKB/Swiss-Prot (Q6NZP2.1)"
     Region          453..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZP2.1)"
     CDS             1..473
                     /gene="Gpbp1l1"
                     /gene_synonym="5330440M15Rik"
                     /coded_by="NM_001368177.1:1143..2564"
                     /db_xref="CCDS:CCDS18511.1"
                     /db_xref="GeneID:77110"
                     /db_xref="MGI:MGI:1924360"
ORIGIN      
        1 maqhdfvpaw lnfstpqssk sstatfdkhg ehlsrgegrf gisrrrhnss dgffnngplr
       61 ttgdswhqps lfrhdsvdsg vskgayagtt gwhgssrghd gmsqrsggss tgnhrhwngs
      121 fhsrkgcafq ektpteiree kkedkveklq feeedfpsln peagkqnqpc rpvgtpsgvw
      181 enppsakqps kmlvikkisk edpaaafsaa ftssgshhan gnkvstmvps vyknlvpkpa
      241 pppskpnawk anrtehkpgs lcssresaft npisvtkpvg laagaglhsp kespssttpp
      301 ieisssrltk ltrrttdrks eflktlkder ngdcsesrdc dkleglrleg shtpepkeng
      361 eqgclqngls lpmveegevl shsleaehrl lkamgwqeyp endesclplt edelkefhlr
      421 teqlrrngfg kngllqsrsc slsspwrstc iaecedsdse tsssqtsddd awk
//
LOCUS       NP_694949                243 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 174 [Homo sapiens].
ACCESSION   NP_694949
VERSION     NP_694949.1
DBSOURCE    REFSEQ: accession NM_153217.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Sasaki,S., Shiozaki,Y., Hanazaki,A., Koike,M., Tanifuji,K., Uga,M.,
            Kawahara,K., Kaneko,I., Kawamoto,Y., Wiriyasermkul,P., Hasegawa,T.,
            Amizuka,N., Miyamoto,K.I., Nagamori,S., Kanai,Y. and Segawa,H.
  TITLE     Tmem174, a regulator of phosphate transporter prevents
            hyperphosphatemia
  JOURNAL   Sci Rep 12 (1), 6353 (2022)
   PUBMED   35428804
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Okada,Y., Sim,X., Go,M.J., Wu,J.Y., Gu,D., Takeuchi,F.,
            Takahashi,A., Maeda,S., Tsunoda,T., Chen,P., Lim,S.C., Wong,T.Y.,
            Liu,J., Young,T.L., Aung,T., Seielstad,M., Teo,Y.Y., Kim,Y.J.,
            Lee,J.Y., Han,B.G., Kang,D., Chen,C.H., Tsai,F.J., Chang,L.C.,
            Fann,S.J., Mei,H., Rao,D.C., Hixson,J.E., Chen,S., Katsuya,T.,
            Isono,M., Ogihara,T., Chambers,J.C., Zhang,W., Kooner,J.S.,
            Albrecht,E., Yamamoto,K., Kubo,M., Nakamura,Y., Kamatani,N.,
            Kato,N., He,J., Chen,Y.T., Cho,Y.S., Tai,E.S. and Tanaka,T.
  CONSRTM   KidneyGen Consortium; CKDGen Consortium; GUGC consortium
  TITLE     Meta-analysis identifies multiple loci associated with kidney
            function-related traits in east Asian populations
  JOURNAL   Nat Genet 44 (8), 904-909 (2012)
   PUBMED   22797727
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Wang,P., Sun,B., Hao,D., Zhang,X., Shi,T. and Ma,D.
  TITLE     Human TMEM174 that is highly expressed in kidney tissue activates
            AP-1 and promotes cell proliferation
  JOURNAL   Biochem Biophys Res Commun 394 (4), 993-999 (2010)
   PUBMED   20331980
  REMARK    GeneRIF: these results suggest the potential role of TMEM174 in
            renal development and physiological function.
            Erratum:[Biochem Biophys Res Commun. 2011 Jan 7;404(1):580]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116345.2 and AK315460.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG434015.1, AK315460.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296776.6/ ENSP00000296776.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.2"
     Protein         1..243
                     /product="transmembrane protein 174"
                     /calculated_mol_wt=26156
     Region          9..241
                     /region_name="TMEM174"
                     /note="Transmembrane protein 174; pfam15029"
                     /db_xref="CDD:434404"
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUU8.1)"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUU8.1)"
     CDS             1..243
                     /gene="TMEM174"
                     /coded_by="NM_153217.3:52..783"
                     /db_xref="CCDS:CCDS4018.1"
                     /db_xref="GeneID:134288"
                     /db_xref="HGNC:HGNC:28187"
                     /db_xref="MIM:614909"
ORIGIN      
        1 meqgsgrled fpvnvfsvtp ytpstadiqv sdddkagatl lfsgiflglv gitftvmgwi
       61 kyqgvshfew tqllgpvlls vgvtfiliav ckfkmlscql ckeseervpd seqtpggpsf
      121 vftginqpit fhgatvvqyi pppygspepm gintsylqsv vspcglitsg gaaaamsspp
      181 qyytiypqdn safvvdegcl sftdggnhrp npdvdqleet qleeeacacf spppyeeiys
      241 lpr
//
LOCUS       NP_001354472             550 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 36 [Homo sapiens].
ACCESSION   NP_001354472 XP_006718060
VERSION     NP_001354472.1
DBSOURCE    REFSEQ: accession NM_001367543.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_006718060.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.955657.1,
                                           SRR1803611.78624.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..550
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 36"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=61312
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          418..545
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..550
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367543.1:95..1747"
                     /note="isoform 36 is encoded by transcript variant 36"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmpqsnnkns lvspaqepap lqtamepqtt vvhnatdgik gstescnttt ededlkvrkq
      421 eiikiteqli eainngdfea ytkicdpglt sfepealgnl vegmdfhkfy fenllsknsk
      481 pihttilnph vhvigedaac iayirltqyi dgqgrprtsq seetrvwhrr dgkwlnvhyh
      541 csgapaaplq
//
LOCUS       NP_006589               1083 aa            linear   PRI 27-APR-2025
DEFINITION  solute carrier family 12 member 7 [Homo sapiens].
ACCESSION   NP_006589
VERSION     NP_006589.2
DBSOURCE    REFSEQ: accession NM_006598.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Jin,S.C., Furey,C.G., Zeng,X., Allocco,A., Nelson-Williams,C.,
            Dong,W., Karimy,J.K., Wang,K., Ma,S., Delpire,E. and Kahle,K.T.
  TITLE     SLC12A ion transporter mutations in sporadic and familial human
            congenital hydrocephalus
  JOURNAL   Mol Genet Genomic Med 7 (9), e892 (2019)
   PUBMED   31393094
  REMARK    GeneRIF: SLC12A ion transporter mutations in sporadic and familial
            human congenital hydrocephalus.
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Brown,T.C., Nicolson,N.G., Stenman,A., Juhlin,C.C., Gibson,C.E.,
            Callender,G.G., Korah,R. and Carling,T.
  TITLE     Insulin-Like Growth Factor and SLC12A7 Dysregulation: A Novel
            Signaling Hallmark of Non-Functional Adrenocortical Carcinoma
  JOURNAL   J Am Coll Surg 229 (3), 305-315 (2019)
   PUBMED   31034883
  REMARK    GeneRIF: The IGF1 gene was amplified in 9 of 19 ACC samples,
            similar to findings in The Cancer Genome Atlas database. The IGF1
            overexpression was observed in 5 samples and was associated with
            SLC12A7 overexpression and non-functional, early-stage tumors (p <
            0.05). endogenous overexpression and silencing of SLC12A7
            significantly altered IGF1 and IGF1R expression without impacting
            other IGFs.
REFERENCE   4  (residues 1 to 1083)
  AUTHORS   Brown,T.C., Murtha,T.D., Rubinstein,J.C., Korah,R. and Carling,T.
  TITLE     SLC12A7 alters adrenocortical carcinoma cell adhesion properties to
            promote an aggressive invasive behavior
  JOURNAL   Cell Commun Signal 16 (1), 27 (2018)
   PUBMED   29884238
  REMARK    GeneRIF: SLC12A7 alters adrenocortical carcinoma cell adhesion
            properties to promote an aggressive invasive behavior
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1083)
  AUTHORS   Fu,B., Wang,L., Li,S. and Dorf,M.E.
  TITLE     ZMPSTE24 defends against influenza and other pathogenic viruses
  JOURNAL   J Exp Med 214 (4), 919-929 (2017)
   PUBMED   28246125
REFERENCE   6  (residues 1 to 1083)
  AUTHORS   Brauer,M., Frei,E., Claes,L., Grissmer,S. and Jager,H.
  TITLE     Influence of K-Cl cotransporter activity on activation of
            volume-sensitive Cl- channels in human osteoblasts
  JOURNAL   Am J Physiol Cell Physiol 285 (1), C22-C30 (2003)
   PUBMED   12637262
  REMARK    GeneRIF: human osteoblasts express functional K-Cl cotransporters
            in their cell membrane that seem to be able to induce the indirect
            activation of volume-sensitive Cl- channels by KCl through an
            increase in the intracellular ions, water influx and cell swelling.
REFERENCE   7  (residues 1 to 1083)
  AUTHORS   Boettger,T., Hubner,C.A., Maier,H., Rust,M.B., Beck,F.X. and
            Jentsch,T.J.
  TITLE     Deafness and renal tubular acidosis in mice lacking the K-Cl
            co-transporter Kcc4
  JOURNAL   Nature 416 (6883), 874-878 (2002)
   PUBMED   11976689
  REMARK    GeneRIF: Mice lacking SLC12A7 function suffer from deafness and
            renal metabolic acidosis. The phenotype suggests a function in
            inner ear potassium recycling. A function in the proton secreting
            alpha-intercalating cells of the kidney is shown.
REFERENCE   8  (residues 1 to 1083)
  AUTHORS   Hattori,A., Okumura,K., Nagase,T., Kikuno,R., Hirosawa,M. and
            Ohara,O.
  TITLE     Characterization of long cDNA clones from human adult spleen
  JOURNAL   DNA Res 7 (6), 357-366 (2000)
   PUBMED   11214971
REFERENCE   9  (residues 1 to 1083)
  AUTHORS   Mercado,A., Song,L., Vazquez,N., Mount,D.B. and Gamba,G.
  TITLE     Functional comparison of the K+-Cl- cotransporters KCC1 and KCC4
  JOURNAL   J Biol Chem 275 (39), 30326-30334 (2000)
   PUBMED   10913127
REFERENCE   10 (residues 1 to 1083)
  AUTHORS   Mount,D.B., Mercado,A., Song,L., Xu,J., George,A.L. Jr., Delpire,E.
            and Gamba,G.
  TITLE     Cloning and characterization of KCC3 and KCC4, new members of the
            cation-chloride cotransporter gene family
  JOURNAL   J Biol Chem 274 (23), 16355-16362 (1999)
   PUBMED   10347194
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116351.2, DB451347.1, BC098390.1, AF105365.1, AK024497.1 and
            BU953746.1.
            
            On Jan 20, 2007 this sequence version replaced NP_006589.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098390.1, SRR1803614.120186.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264930.10/ ENSP00000264930.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.33"
     Protein         1..1083
                     /product="solute carrier family 12 member 7"
                     /note="potassium/chloride transporter KCC4; K-Cl
                     cotransporter 4; electroneutral potassium-chloride
                     cotransporter 4; solute carrier family 12
                     (potassium/chloride transporters), member 7; solute
                     carrier family 12 (potassium/chloride transporter), member
                     7; SUCO/SLC12A7 fusion"
                     /calculated_mol_wt=118975
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y666.3)"
     Region          45..1083
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; cl45918"
                     /db_xref="CDD:459263"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            120..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            150..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            197..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            250..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            272..300
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            312
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            360
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            420..440
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            451..473
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            505..531
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            555..571
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            574..598
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            613..632
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            636..651
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Region          664..680
                     /region_name="Scissor helix.
                     /evidence=ECO:0000269|PubMed:33310850,
                     ECO:0007744|PDB:7D99"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            973
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVL3; propagated from
                     UniProtKB/Swiss-Prot (Q9Y666.3)"
     Site            980
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVL3; propagated from
                     UniProtKB/Swiss-Prot (Q9Y666.3)"
     CDS             1..1083
                     /gene="SLC12A7"
                     /gene_synonym="KCC4"
                     /coded_by="NM_006598.3:73..3324"
                     /db_xref="CCDS:CCDS34129.1"
                     /db_xref="GeneID:10723"
                     /db_xref="HGNC:HGNC:10915"
                     /db_xref="MIM:604879"
ORIGIN      
        1 mptnftvvpv eahadgggde taerteapgt pegpeperps pgdgnprens pflnnveveq
       61 esffegknma lfeeemdsnp mvssllnkla nytnlsqgvv eheedeesrr reakaprmgt
      121 figvylpclq nilgvilflr ltwivgvagv lesflivamc ctctmltais msaiatngvv
      181 paggsyymis rslgpefgga vglcfylgtt fagamyilgt ieifltyisp gaaifqaeaa
      241 ggeaaamlhn mrvygtctlv lmalvvfvgv kyvnklalvf lacvvlsila iyagviksaf
      301 dppdipvcll gnrtlsrrsf dacvkaygih nnsatsalwg lfcngsqpsa acdeyfiqnn
      361 vteiqgipga asgvflenlw styahagafv ekkgvpsvpv aeesrasalp yvltdiaasf
      421 tllvgiyfps vtgimagsnr sgdlkdaqks iptgtilaiv ttsfiylsci vlfgaciegv
      481 vlrdkfgeal qgnlvigmla wpspwvivig sffstcgagl qsltgaprll qaiardgivp
      541 flqvfghgka ngeptwalll tvlicetgil iasldsvapi lsmfflmcyl fvnlacavqt
      601 llrtpnwrpr fkfyhwtlsf lgmslclalm ficswyyals amliagciyk yieyrgaeke
      661 wgdgirglsl naaryallrv ehgpphtknw rpqvlvmlnl daeqavkhpr llsftsqlka
      721 gkgltivgsv legtyldkhm eaqraeenir slmstektkg fcqlvvsssl rdgmshliqs
      781 aglgglkhnt vlmawpaswk qednpfswkn fvdtvrdtta ahqallvakn vdsfpqnqer
      841 fggghidvww ivhdggmlml lpfllrqhkv wrkcrmrift vaqvddnsiq mkkdlqmfly
      901 hlrisaevev vemvendisa ftyertlmme qrsqmlkqmq lskneqerea qlihdrntas
      961 htaaaartqa pptpdkvqmt wtrekliaek yrsrdtslsg fkdlfsmkpd qsnvrrmhta
     1021 vklngvvlnk sqdaqlvlln mpgppknrqg denymeflev lteglnrvll vrgggrevit
     1081 iys
//
LOCUS       NP_001348630             558 aa            linear   ROD 27-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 16 [Mus musculus].
ACCESSION   NP_001348630
VERSION     NP_001348630.1
DBSOURCE    REFSEQ: accession NM_001361701.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Peluso,G., Tian,E., Abusleme,L., Munemasa,T., Mukaibo,T. and Ten
            Hagen,K.G.
  TITLE     Loss of the disease-associated glycosyltransferase Galnt3 alters
            Muc10 glycosylation and the composition of the oral microbiome
  JOURNAL   J Biol Chem 295 (5), 1411-1425 (2020)
   PUBMED   31882545
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Tian,E., Wang,S., Zhang,L., Zhang,Y., Malicdan,M.C., Mao,Y.,
            Christoffersen,C., Tabak,L.A., Schjoldager,K.T. and Ten Hagen,K.G.
  TITLE     Galnt11 regulates kidney function by glycosylating the endocytosis
            receptor megalin to modulate ligand binding
  JOURNAL   Proc Natl Acad Sci U S A 116 (50), 25196-25202 (2019)
   PUBMED   31740596
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Tian,E., Stevens,S.R., Guan,Y., Springer,D.A., Anderson,S.A.,
            Starost,M.F., Patel,V., Ten Hagen,K.G. and Tabak,L.A.
  TITLE     Galnt1 is required for normal heart valve development and cardiac
            function
  JOURNAL   PLoS One 10 (1), e0115861 (2015)
   PUBMED   25615642
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Tian,E., Hoffman,M.P. and Ten Hagen,K.G.
  TITLE     O-glycosylation modulates integrin and FGF signalling by
            influencing the secretion of basement membrane components
  JOURNAL   Nat Commun 3, 869 (2012)
   PUBMED   22643896
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC163282.3 and AC125361.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110634.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN02415123
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 36.79 cM"
     Protein         1..558
                     /product="polypeptide N-acetylgalactosaminyltransferase
                     16"
                     /EC_number="2.4.1.41"
                     /note="putative polypeptide
                     N-acetylgalactosaminyltransferase-like protein 1;
                     galNAc-T-like protein 1; pp-GaNTase-like protein 1;
                     polypeptide GalNAc transferase-like protein 1; protein-UDP
                     acetylgalactosaminyltransferase-like protein 1;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 16;
                     UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase-like protein 1;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase-like 1; polypeptide
                     GalNAc transferase 16"
                     /calculated_mol_wt=62744
     Site            7..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ61.2)"
     Region          34..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ61.2)"
     Region          122..227
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ61.2)"
     Region          126..420
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(130..132,134,163,188,191,195,211..213,294..295,
                     317..318,320,345,348,353)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(211,213,345)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          286..348
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ61.2)"
     Region          426..557
                     /region_name="beta-trefoil_Ricin_GALNT16"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide N-acetylgalactosaminyltransferase 16
                     (GALNT16) and similar proteins; cd23479"
                     /db_xref="CDD:467357"
     Site            order(443..445,456,458,461,470..471)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467357"
     Site            order(488..491,502,504,507,512..513)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467357"
     Site            order(532..535,539,541,544,549..550)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467357"
     CDS             1..558
                     /gene="Galnt16"
                     /gene_synonym="5730405L21Rik; galNAc-T16; Galntl1;
                     mpp-GalNAc-T16"
                     /coded_by="NM_001361701.1:275..1951"
                     /db_xref="CCDS:CCDS36482.1"
                     /db_xref="GeneID:108760"
                     /db_xref="MGI:MGI:1917754"
ORIGIN      
        1 mrkiranaia iltvawilgt fyylwqdnra haasssgrga qraggrpeql redrtipliv
       61 tgtpskgfde kaylsakqlk pgedpyrqha fnqlesdkls sdrpirdtrh yscpslsyss
      121 dlpatsviit fhnearstll rtvksvlnrt pasliqeiil vddfssdped cllltripkv
      181 kclrndkreg lirsrvrgad vagatvltfl dshcevnvew lqpmlqrvme dhtrvvspii
      241 dvisldnfay laasadlrgg fdwslhfkwe qipleqkmtr tdptkpirtp viaggifvid
      301 kswfnhlgky daqmdiwgge nfelsfrvwm cggsleivpc srvghvfrkr hpynfpegna
      361 ltyirntkrt aevwmdeykq yyyearpsai gkafgsvatr ieqrkkmdck sfrwylenvy
      421 peltvpvkev lpgvikqgvn clesqgqnta gdlllgmgic rgsakspppa qawlfsdhli
      481 qqqgkclaat stlmsspgsp vilqtcnpke gkqkwrrkgs fiqhsvsglc letkpaqlvt
      541 skcqtdaqaq qwqllpht
//
LOCUS       NP_112217               1594 aa            linear   PRI 27-APR-2025
DEFINITION  A disintegrin and metalloproteinase with thrombospondin motifs 12
            isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_112217
VERSION     NP_112217.2
DBSOURCE    REFSEQ: accession NM_030955.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1594)
  AUTHORS   Hoeft,K., Koch,L., Ziegler,S., Zhang,L., Luetke,S., Tanzer,M.C.,
            Mohanta,D., Schumacher,D., Schreibing,F., Long,Q., Kim,H.,
            Klinkhammer,B.M., Schikarski,C., Maryam,S., Baens,M., Hermann,J.,
            Krieg,S., Peisker,F., De Laporte,L., Schaefer,G.J., Menzel,S.,
            Jankowski,J., Humphreys,B.D., Wahida,A., Schneider,R.K.,
            Versele,M., Boor,P., Mann,M., Sengle,G., Hayat,S. and Kramann,R.
  TITLE     ADAMTS12 promotes fibrosis by restructuring extracellular matrix to
            enable activation of injury-responsive fibroblasts
  JOURNAL   J Clin Invest 134 (18), e170246 (2024)
   PUBMED   39286973
  REMARK    GeneRIF: ADAMTS12 promotes fibrosis by restructuring extracellular
            matrix to enable activation of injury-responsive fibroblasts.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1594)
  AUTHORS   Dekky,B., Azar,F., Bonnier,D., Monseur,C., Kalebic,C., Arpigny,E.,
            Colige,A., Legagneux,V. and Theret,N.
  TITLE     ADAMTS12 is a stromal modulator in chronic liver disease
  JOURNAL   FASEB J 37 (11), e23237 (2023)
   PUBMED   37819632
  REMARK    GeneRIF: ADAMTS12 is a stromal modulator in chronic liver disease.
REFERENCE   3  (residues 1 to 1594)
  AUTHORS   Jiang,Y., Huang,J., Huang,Z., Li,W., Tan,R., Li,T., Chen,Z.,
            Tang,X., Zhao,Y., Qiu,J., Li,C., Chen,H. and Yang,Z.
  TITLE     ADAMTS12 promotes oxaliplatin chemoresistance and angiogenesis in
            gastric cancer through VEGF upregulation
  JOURNAL   Cell Signal 111, 110866 (2023)
   PUBMED   37619822
  REMARK    GeneRIF: ADAMTS12 promotes oxaliplatin chemoresistance and
            angiogenesis in gastric cancer through VEGF upregulation.
REFERENCE   4  (residues 1 to 1594)
  AUTHORS   He,R.Z., Zheng,J.H., Yao,H.F., Xu,D.P., Yang,M.W., Liu,D.J.,
            Sun,Y.W. and Huo,Y.M.
  TITLE     ADAMTS12 promotes migration and epithelial-mesenchymal transition
            and predicts poor prognosis for pancreatic cancer
  JOURNAL   Hepatobiliary Pancreat Dis Int 22 (2), 169-178 (2023)
   PUBMED   35508435
  REMARK    GeneRIF: ADAMTS12 promotes migration and epithelial-mesenchymal
            transition and predicts poor prognosis for pancreatic cancer.
REFERENCE   5  (residues 1 to 1594)
  AUTHORS   Liang,J.F., Li,P.H., Zhu,Y., Zheng,S.S., Liu,J.W. and Song,S.Q.
  TITLE     MicroRNA-186 suppresses cell proliferation and metastasis in
            bladder cancer
  JOURNAL   Afr Health Sci 22 (4), 56-63 (2022)
   PUBMED   37092087
  REMARK    GeneRIF: MicroRNA-186 suppresses cell proliferation and metastasis
            in bladder cancer.
REFERENCE   6  (residues 1 to 1594)
  AUTHORS   Luan,Y., Kong,L., Howell,D.R., Ilalov,K., Fajardo,M., Bai,X.H., Di
            Cesare,P.E., Goldring,M.B., Abramson,S.B. and Liu,C.J.
  TITLE     Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage
            oligomeric matrix protein by alpha-2-macroglobulin
  JOURNAL   Osteoarthritis Cartilage 16 (11), 1413-1420 (2008)
   PUBMED   18485748
REFERENCE   7  (residues 1 to 1594)
  AUTHORS   Llamazares,M., Obaya,A.J., Moncada-Pazos,A., Heljasvaara,R.,
            Espada,J., Lopez-Otin,C. and Cal,S.
  TITLE     The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties
            through modulation of the Ras-dependent ERK signalling pathway
  JOURNAL   J Cell Sci 120 (Pt 20), 3544-3552 (2007)
   PUBMED   17895370
  REMARK    GeneRIF: data suggest that ADAMTS12 confers tumour-protective
            functions upon cells that produce this proteolytic enzyme
REFERENCE   8  (residues 1 to 1594)
  AUTHORS   Liu,C.J., Kong,W., Xu,K., Luan,Y., Ilalov,K., Sehgal,B., Yu,S.,
            Howell,R.D. and Di Cesare,P.E.
  TITLE     ADAMTS-12 associates with and degrades cartilage oligomeric matrix
            protein
  JOURNAL   J Biol Chem 281 (23), 15800-15808 (2006)
   PUBMED   16611630
  REMARK    GeneRIF: ADAMTS-12 is a new COMP-interacting and -degrading enzyme
            and thus may play an important role in the COMP degradation in the
            initiation and progression of arthritis
REFERENCE   9  (residues 1 to 1594)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 1594)
  AUTHORS   Tang,B.L.
  TITLE     ADAMTS: a novel family of extracellular matrix proteases
  JOURNAL   Int J Biochem Cell Biol 33 (1), 33-44 (2001)
   PUBMED   11167130
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC058841.1, AY358745.1,
            AJ250725.1, AW938686.1, AC034232.8 and CA413137.1.
            
            On Aug 26, 2004 this sequence version replaced NP_112217.1.
            
            Summary: This gene encodes a member of the ADAMTS (a disintegrin
            and metalloproteinase with thrombospondin motifs) protein family.
            Members of the family share several distinct protein modules,
            including a propeptide region, a metalloproteinase domain, a
            disintegrin-like domain, and a thrombospondin type 1 (TS-1) motif.
            Individual members of this family differ in the number of
            C-terminal TS-1 motifs, and some have unique C-terminal domains.
            The enzyme encoded by this gene contains eight TS-1 motifs. It may
            play roles in pulmonary cells during fetal development or in tumor
            processes through its proteolytic activity or as a molecule
            potentially involved in regulation of cell adhesion. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ250725.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000504830.6/ ENSP00000422554.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1594
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.3-p13.2"
     Protein         1..1594
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 12 isoform 1 preproprotein"
                     /note="a disintegrin-like and metalloprotease (reprolysin
                     type) with thrombospondin type 1 motif, 12; a disintegrin
                     and metalloproteinase with thrombospondin motifs 12;
                     ADAM-TS12; ADAMTS-12; ADAM-TS 12"
                     /calculated_mol_wt=174768
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2926
     Region          54..195
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          208..213
                     /region_name="Cysteine switch. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Site            215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     mat_peptide     241..1594
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 12. /id=PRO_0000029187"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
                     /calculated_mol_wt=150210
     Region          246..453
                     /region_name="ZnMc_ADAMTS_like"
                     /note="Zinc-dependent metalloprotease, ADAMTS_like
                     subgroup. ADAMs (A Disintegrin And Metalloprotease) are
                     glycoproteins, which play roles in cell signaling, cell
                     fusion, and cell-cell interactions. This particular
                     subfamily represents domain architectures that...;
                     cd04273"
                     /db_xref="CDD:239801"
     Site            order(392..393,396,402)
                     /site_type="active"
                     /db_xref="CDD:239801"
     Region          468..532
                     /region_name="ADAMTS_CR_2"
                     /note="ADAMTS cysteine-rich domain 2; pfam17771"
                     /db_xref="CDD:465496"
     Site            485
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          545..596
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          603..701
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Site            685
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          701..827
                     /region_name="Spacer 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Region          703..812
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Site            790
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          828..882
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          886..940
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          948..996
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            952
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          997..1316
                     /region_name="Spacer 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Region          1002..1076
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Region          1095..1174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Site            1105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          1249..1283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P58397.2)"
     Site            1276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Site            1301
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          1317..1365
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            1321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          1368..1424
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            1372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Site            1379
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     Region          1427..1472
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1475..1531
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            1504
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58397.2)"
     CDS             1..1594
                     /gene="ADAMTS12"
                     /gene_synonym="PRO4389"
                     /coded_by="NM_030955.4:135..4919"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS34140.1"
                     /db_xref="GeneID:81792"
                     /db_xref="HGNC:HGNC:14605"
                     /db_xref="MIM:606184"
ORIGIN      
        1 mpcaqrswla nlsvvaqlln fgalcygrqp qpgpvrfpdr rqehfikglp eyhvvgpvrv
       61 dasghflsyg lhypitssrr krdldgsedw vyyrisheek dlffnltvnq gflsnsyime
      121 krygnlshvk mmassaplch lsgtvlqqgt rvgtaalsac hgltgffqlp hgdffiepvk
      181 khplveggyh phivyrrqkv petkeptcgl kdsvnisqkq elwrekwerh nlpsrslsrr
      241 siskerwvet lvvadtkmie yhgsenvesy iltimnmvtg lfhnpsigna ihivvvrlil
      301 leeeeqglki vhhaektlss fckwqksinp ksdlnpvhhd vavlltrkdi cagfnrpcet
      361 lglshlsgmc qphrscnine dsglplafti ahelghsfgi qhdgkendce pvgrhpyims
      421 rqlqydptpl twskcseeyi trfldrgwgf clddipkkkg lkskviapgv iydvhhqcql
      481 qygpnatfcq evenvcqtlw csvkgfcrsk ldaaadgtqc gekkwcmagk citvgkkpes
      541 ipggwgrwsp wshcsrtcga gvqsaerlcn npepkfggky ctgerkryrl cnvhpcrsea
      601 ptfrqmqcse fdtvpyknel yhwfpifnpa hpcelycrpi dgqfsekmld avidgtpcfe
      661 ggnsrnvcin gickmvgcdy eidsnatedr cgvclgdgss cqtvrkmfkq kegsgyvdig
      721 lipkgardir vmeiegagnf lairsedpek yylnggfiiq wngnyklagt vfqydrkgdl
      781 eklmatgptn esvwiqllfq vtnpgikyey tiqkdgldnd veqqmyfwqy ghwtecsvtc
      841 gtgirrqtah cikkgrgmvk atfcdpetqp ngrqkkchek acpprwwage weacsatcgp
      901 hgekkrtvlc iqtmvsdeqa lpptdcqhll kpktllscnr dilcpsdwtv gnwsecsvsc
      961 gggvrirsvt caknhdepcd vtrkpnsral cglqqcpssr rvlkpnkgti sngknpptlk
     1021 pvppptsrpr mlttptgpes mststpaiss pspttaskeg dlggkqwqds stqpelssry
     1081 listgstsqp iltsqslsiq pseenvsssd tgptsegglv atttsgsgls ssrnpitwpv
     1141 tpfyntltkg pemeihsgsg eereqpedkd esnpviwtki rvpgndapve stemplappl
     1201 tpdlsresww ppfstvmegl lpsqrpttse tgtprvegmv tekpantllp lggdhqpeps
     1261 gktanrnhlk lpnnmnqtks sepvlteeda tslitegfll nasnykqltn ghgsahwivg
     1321 nwsecsttcg lgaywrrvec stqmdsdcaa iqrpdpakrc hlrpcagwkv gnwskcsrnc
     1381 sggfkireiq cvdsrdhrnl rpfhcqflag ippplsmscn pepceawqve pwsqcsrscg
     1441 ggvqergvfc pgglcdwtkr ptstmscneh lcchwatgnw dlcstscggg fqkrtvqcvp
     1501 segnktedqd qclcdhkprp pefkkcnqqa ckksadllct kdklsasfcq tlkamkkcsv
     1561 ptvraeccfs cpqthithtq rqrrqrllqk skel
//
LOCUS       NP_001346203            1009 aa            linear   ROD 27-APR-2025
DEFINITION  E3 SUMO-protein ligase ZNF451 isoform 4 [Mus musculus].
ACCESSION   NP_001346203 XP_006496433
VERSION     NP_001346203.1
DBSOURCE    REFSEQ: accession NM_001359274.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Peng,H., Zhang,Y., Min,J., Tan,Y. and Liu,S.
  TITLE     Loss of ZNF451 mediates fibroblast activation and promotes lung
            fibrosis
  JOURNAL   Respir Res 25 (1), 160 (2024)
   PUBMED   38600524
  REMARK    GeneRIF: Loss of ZNF451 mediates fibroblast activation and promotes
            lung fibrosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Zhang,Y., Wang,W., Min,J., Liu,S., Wang,Q., Wang,Y., Xiao,Y.,
            Li,X., Zhou,Z. and Liu,S.
  TITLE     ZNF451 favors triple-negative breast cancer progression by
            enhancing SLUG-mediated CCL5 transcriptional expression
  JOURNAL   Cell Rep 42 (6), 112654 (2023)
   PUBMED   37342906
REFERENCE   4  (residues 1 to 1009)
  AUTHORS   Antonio Urrutia,G., Ramachandran,H., Cauchy,P., Boo,K.,
            Ramamoorthy,S., Boller,S., Dogan,E., Clapes,T., Trompouki,E.,
            Torres-Padilla,M.E., Palvimo,J.J., Pichler,A. and Grosschedl,R.
  TITLE     ZFP451-mediated SUMOylation of SATB2 drives embryonic stem cell
            differentiation
  JOURNAL   Genes Dev 35 (15-16), 1142-1160 (2021)
   PUBMED   34244292
REFERENCE   5  (residues 1 to 1009)
  AUTHORS   Koidl,S., Eisenhardt,N., Fatouros,C., Droescher,M., Chaugule,V.K.
            and Pichler,A.
  TITLE     The SUMO2/3 specific E3 ligase ZNF451-1 regulates PML stability
  JOURNAL   Int J Biochem Cell Biol 79, 478-487 (2016)
   PUBMED   27343429
  REMARK    GeneRIF: a regulatory role of ZNF451-1 in fine-tuning physiological
            PML levels
REFERENCE   6  (residues 1 to 1009)
  AUTHORS   Tamplin,O.J., Kinzel,D., Cox,B.J., Bell,C.E., Rossant,J. and
            Lickert,H.
  TITLE     Microarray analysis of Foxa2 mutant mouse embryos reveals novel
            gene expression and inductive roles for the gastrula organizer and
            its derivatives
  JOURNAL   BMC Genomics 9, 511 (2008)
   PUBMED   18973680
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1009)
  AUTHORS   Karvonen,U., Jaaskelainen,T., Rytinki,M., Kaikkonen,S. and
            Palvimo,J.J.
  TITLE     ZNF451 is a novel PML body- and SUMO-associated transcriptional
            coregulator
  JOURNAL   J Mol Biol 382 (3), 585-600 (2008)
   PUBMED   18656483
REFERENCE   8  (residues 1 to 1009)
  AUTHORS   Jensen,P., Magdaleno,S., Lehman,K.M., Rice,D.S., Lavallie,E.R.,
            Collins-Racie,L., McCoy,J.M. and Curran,T.
  TITLE     A neurogenomics approach to gene expression analysis in the
            developing brain
  JOURNAL   Brain Res Mol Brain Res 132 (2), 116-127 (2004)
   PUBMED   15582152
REFERENCE   9  (residues 1 to 1009)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Aizawa,H., Yuasa,S.,
            Nakajima,D., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: II. The complete nucleotide sequences of 400 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (1), 35-48 (2003)
   PUBMED   12693553
REFERENCE   10 (residues 1 to 1009)
  AUTHORS   Eggenschwiler,J.T., Espinoza,E. and Anderson,K.V.
  TITLE     Rab23 is an essential negative regulator of the mouse Sonic
            hedgehog signalling pathway
  JOURNAL   Nature 412 (6843), 194-198 (2001)
   PUBMED   11449277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC163668.5.
            
            On Dec 30, 2017 this sequence version replaced XP_006496433.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660813.260370.1,
                                           SRR17784645.1003654.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 12.81 cM"
     Protein         1..1009
                     /product="E3 SUMO-protein ligase ZNF451 isoform 4"
                     /note="E3 SUMO-protein ligase ZNF451; E3 SUMO-protein
                     transferase ZNF451"
                     /calculated_mol_wt=114358
     Region          <867..952
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
     CDS             1..1009
                     /gene="Zfp451"
                     /gene_synonym="4930515K21Rik; 4933435G09Rik; COASTER;
                     Kiaa0576-hp; mKIAA1702; Znf451"
                     /coded_by="NM_001359274.1:238..3267"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:98403"
                     /db_xref="MGI:MGI:2137896"
ORIGIN      
        1 mgdpgpeiie svppagpeas esttdenedd iqfvsegplr pvleyidlvs sddeepstsh
       61 sdenfkckdy idhqkdkval tlarlarhve vekqqkeekn rafrekidfq hahglqelef
      121 iqghseteaa rqcvdqwlkm pglrtnaans gtkrsfqrgg rmwrsekpil cpimhcnkef
      181 dnghlllghl krfdhspcdp titlhgplan sfacavcyeh fvtqqqykdh llsrtaaadg
      241 hsnsllpqii qcyacpqcfl lfstkdeclk hmstknhfhq sfklsdnkgt arpisfpsfa
      301 kkrlvslckd vpfqvkcvac hqtlrshmel tahfrvrcqn agpvaiaeks itqvakefiv
      361 rgycsdcnqv fmdvastqsh knsghkitla nsveesvlly chisegsrpp cdlhlfsqpk
      421 isslkrilsv kessaedciv ptkkvnlgve slggatrvqr qspavtawfc ecrrqfpsee
      481 avekhvfsan tmcykcvvcg kvcedsgvmr lhmsrfhgga hlnnflfwcr tckkelvkkd
      541 aimahitefh sghryfyemd eveeeeeeam psssveshln tdkppspiav vdhcpanspp
      601 rgrwqcrice dmfesqecvk qhcmsltshr fhryscahcr ktfhkvetly rhcqdehdse
      661 immkyfcglc dlifnkeeef lshykehhsi dyvfvsektk tsiktegdfk ivetssllsc
      721 gchesymcki nrkedydrcl pvllekgrlw frcsscsata qnvtdinthv cqvhrkekse
      781 eeqqyvikcg ictkafqnte saqqhfhrkh aalqkptatp gganrsstcq laasashaek
      841 nlkqpssqkh sdvekgaehd vrcqniggnt nwkpplsckv ynylsrigcf flhprcskrk
      901 daadfaicmh agrldeqlpk qipftilsgd qgflelenqf kktqrpahil nphhlegdmm
      961 callnsisdt tkecdsddss gmkgspaeel ratedvelee airrsleem
//
LOCUS       NP_780730                833 aa            linear   ROD 27-APR-2025
DEFINITION  neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter
            1 isoform 1 [Mus musculus].
ACCESSION   NP_780730 XP_983736
VERSION     NP_780730.2
DBSOURCE    REFSEQ: accession NM_175521.4
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Kurz,J., Weiss,A.C., Thiesler,H., Qasrawi,F., Deuper,L., Kaur,J.,
            Rudat,C., Ludtke,T.H., Wojahn,I., Hildebrandt,H., Trowe,M.O. and
            Kispert,A.
  TITLE     Notch signaling is a novel regulator of visceral smooth muscle cell
            differentiation in the murine ureter
  JOURNAL   Development 149 (4) (2022)
   PUBMED   35103284
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Wang,S., Li,X., Zhang,Q., Chai,X., Wang,Y., Forster,E., Zhu,X. and
            Zhao,S.
  TITLE     Nyap1 Regulates Multipolar-Bipolar Transition and Morphology of
            Migrating Neurons by Fyn Phosphorylation during Corticogenesis
  JOURNAL   Cereb Cortex 30 (3), 929-941 (2020)
   PUBMED   31609430
  REMARK    GeneRIF: Nyap1 Regulates Multipolar-Bipolar Transition and
            Morphology of Migrating Neurons by Fyn Phosphorylation during
            Corticogenesis.
REFERENCE   4  (residues 1 to 833)
  AUTHORS   Yokoyama,K., Tezuka,T., Kotani,M., Nakazawa,T., Hoshina,N.,
            Shimoda,Y., Kakuta,S., Sudo,K., Watanabe,K., Iwakura,Y. and
            Yamamoto,T.
  TITLE     NYAP: a phosphoprotein family that links PI3K to WAVE1 signalling
            in neurons
  JOURNAL   EMBO J 30 (23), 4739-4754 (2011)
   PUBMED   21946561
  REMARK    GeneRIF: Phosphorylated NYAPs interact with PI3K p85 and activate
            PI3K, Akt, and Rac1. Moreover, the NYAPs interact with the WAVE1
            complex which mediates remodelling of the actin cytoskeleton after
            activation by PI3K-produced PIP3 and Rac1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 833)
  AUTHORS   Lin,J.C., Ho,W.H., Gurney,A. and Rosenthal,A.
  TITLE     The netrin-G1 ligand NGL-1 promotes the outgrowth of
            thalamocortical axons
  JOURNAL   Nat Neurosci 6 (12), 1270-1276 (2003)
   PUBMED   14595443
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC057372.1, AK032567.1 and CJ292493.1.
            
            On or before May 4, 2006 this sequence version replaced
            XP_983736.1, NP_780730.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057372.1, SRR10662773.1727782.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164139 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 76.62 cM"
     Protein         1..833
                     /product="neuronal tyrosine-phosphorylated
                     phosphoinositide-3-kinase adapter 1 isoform 1"
                     /note="neuronal tyrosine phosphorylated adaptor for
                     phosphoinositide 3-kinase adaptor 1; neuronal
                     tyrosine-phosphorylated phosphoinositide-3-kinase adapter
                     1"
                     /calculated_mol_wt=87538
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PFX7.1)"
     Region          4..416
                     /region_name="NYAP_N"
                     /note="Neuronal tyrosine-phosphorylated
                     phosphoinositide-3-kinase adapter; pfam15439"
                     /db_xref="CDD:464717"
     Region          64..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PFX7.1)"
     Region          76..181
                     /region_name="Involved in CYFIP1-and NCKAP1-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PFX7.1)"
     Region          219..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PFX7.1)"
     Region          577..833
                     /region_name="NYAP_C"
                     /note="Neuronal tyrosine-phosphorylated
                     phosphoinositide-3-kinase adapter; pfam15452"
                     /db_xref="CDD:464724"
     Region          645..674
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PFX7.1)"
     Region          736..765
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PFX7.1)"
     CDS             1..833
                     /gene="Nyap1"
                     /gene_synonym="6430598A04Rik"
                     /coded_by="NM_175521.4:85..2586"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS19775.1"
                     /db_xref="GeneID:243300"
                     /db_xref="MGI:MGI:2443880"
ORIGIN      
        1 mnllyrktkl ewrqhkeeea krssskeaap tgpvgpgavp gpgvrvrdia slrrslrmgf
       61 mtmpasqeht phpcrstmap rslschsvgs mdsvgggpgg gltedsstrr ppakprrhps
      121 tklsmagpga etppskkags qkpapecres srkvppqkpr rspntqlsvs fdescapaps
      181 prganlplqr lsrasritgd ldagaqeeep vyiemvgdvf rgggrsgggl agpplgsggp
      241 tppaaadsds edseaiyeem kyplpeeagd grangppplt apsppqqthi lqphphphrr
      301 pasalpsrrd gtptkttpce ipppfpnllq hrppllafpq aksasrapgd gvsrlpvlch
      361 skepagstpa pqvpareret pplpppppaa nllllgpsgr arshstplpp qgsgqtrger
      421 elpnshsmic pkaagvpaah papaallpgp pkdkavsytm vysavkvtth svlpagpplg
      481 vgepkteeis vlhgmlcass rppvpgkssp hsgamgsaag vlhhrsclas phslpdptgg
      541 sltplwtypa taaglkrppa ydslkaggvl nkgcgmgaps pmvkiqlqeq gtdggafasi
      601 scahviasag tpeeeeemga afgagwalqr kvlyggrkak evdteedgar awngstegpg
      661 kvehedrgpv psgipvrsqg aegllarihh drggsrtalp vpcqtfpach rngdftggyr
      721 lgrsastsgv rqaalhtprp csqprdalsq thpvlplplp pqparerdgk llevierkrc
      781 vckeikarhr pdrglckqes mpilpswrrv peprksgtpp crrqhtvlwd tai
//
LOCUS       NP_003293                476 aa            linear   PRI 27-APR-2025
DEFINITION  thyroid receptor-interacting protein 6 [Homo sapiens].
ACCESSION   NP_003293
VERSION     NP_003293.2
DBSOURCE    REFSEQ: accession NM_003302.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Liu,X.S., Chen,Y.X., Wan,H.B., Wang,Y.L., Wang,Y.Y., Gao,Y.,
            Wu,L.B. and Pei,Z.J.
  TITLE     TRIP6 a potential diagnostic marker for colorectal cancer with
            glycolysis and immune infiltration association
  JOURNAL   Sci Rep 14 (1), 4042 (2024)
   PUBMED   38369589
  REMARK    GeneRIF: TRIP6 a potential diagnostic marker for colorectal cancer
            with glycolysis and immune infiltration association.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Daniel,P., Balusikova,K., Vaclavikova,R., Seborova,K.,
            Ransdorfova,S., Valerianova,M., Wei,L., Jelinek,M., Tlapakova,T.,
            Fleischer,T., Kristensen,V.N., Soucek,P., Ojima,I. and Kovar,J.
  TITLE     ABCB1 Amplicon Contains Cyclic AMP Response Element-Driven TRIP6
            Gene in Taxane-Resistant MCF-7 Breast Cancer Sublines
  JOURNAL   Genes (Basel) 14 (2), 296 (2023)
   PUBMED   36833223
  REMARK    GeneRIF: ABCB1 Amplicon Contains Cyclic AMP Response Element-Driven
            TRIP6 Gene in Taxane-Resistant MCF-7 Breast Cancer Sublines.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Seborova,K., Kloudova-Spalenkova,A., Koucka,K., Holy,P.,
            Ehrlichova,M., Wang,C., Ojima,I., Voleska,I., Daniel,P.,
            Balusikova,K., Jelinek,M., Kovar,J., Rob,L., Hruda,M., Mrhalova,M.,
            Soucek,P. and Vaclavikova,R.
  TITLE     The Role of TRIP6, ABCC3 and CPS1 Expression in Resistance of
            Ovarian Cancer to Taxanes
  JOURNAL   Int J Mol Sci 23 (1), 73 (2021)
   PUBMED   35008510
  REMARK    GeneRIF: The Role of TRIP6, ABCC3 and CPS1 Expression in Resistance
            of Ovarian Cancer to Taxanes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Yang,F., Li,L., Zhang,J., Zhang,J. and Yang,L.
  TITLE     TRIP6 accelerates the proliferation and invasion of cervical cancer
            by upregulating oncogenic YAP signaling
  JOURNAL   Exp Cell Res 396 (1), 112248 (2020)
   PUBMED   32853630
  REMARK    GeneRIF: TRIP6 accelerates the proliferation and invasion of
            cervical cancer by upregulating oncogenic YAP signaling.
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Murthy,K.K., Clark,K., Fortin,Y., Shen,S.H. and Banville,D.
  TITLE     ZRP-1, a zyxin-related protein, interacts with the second PDZ
            domain of the cytosolic protein tyrosine phosphatase hPTP1E
  JOURNAL   J Biol Chem 274 (29), 20679-20687 (1999)
   PUBMED   10400701
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Zhao,M.K., Wang,Y., Murphy,K., Yi,J., Beckerle,M.C. and
            Gilmore,T.D.
  TITLE     LIM domain-containing protein trip6 can act as a coactivator for
            the v-Rel transcription factor
  JOURNAL   Gene Expr 8 (4), 207-217 (1999)
   PUBMED   10794523
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Yi,J. and Beckerle,M.C.
  TITLE     The human TRIP6 gene encodes a LIM domain protein and maps to
            chromosome 7q22, a region associated with tumorigenesis
  JOURNAL   Genomics 49 (2), 314-316 (1998)
   PUBMED   9598321
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Williams,J.M., Chen,G.C., Zhu,L. and Rest,R.F.
  TITLE     Using the yeast two-hybrid system to identify human epithelial cell
            proteins that bind gonococcal Opa proteins: intracellular gonococci
            bind pyruvate kinase via their Opa proteins and require host
            pyruvate for growth
  JOURNAL   Mol Microbiol 27 (1), 171-186 (1998)
   PUBMED   9466265
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM800083.1 and BC004999.1.
            
            On Apr 7, 2006 this sequence version replaced NP_003293.1.
            
            Summary: This gene is a member of the zyxin family and encodes a
            protein with three LIM zinc-binding domains. This protein localizes
            to focal adhesion sites and along actin stress fibers. Recruitment
            of this protein to the plasma membrane occurs in a lysophosphatidic
            acid (LPA)-dependent manner and it regulates LPA-induced cell
            migration. Alternatively spliced variants which encode different
            protein isoforms have been described; however, not all variants
            have been fully characterized. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.193113.1,
                                           SRR3476690.676481.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000200457.9/ ENSP00000200457.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..476
                     /product="thyroid receptor-interacting protein 6"
                     /note="OPA-interacting protein 1; zyxin related protein 1;
                     thyroid hormone receptor interacting protein 6;
                     TR-interacting protein 6"
                     /calculated_mol_wt=50157
     Region          1..93
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15654.3)"
     Region          <8..251
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            25
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1Y4;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:15988003,
                     ECO:0000269|PubMed:17591779; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Region          108..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15654.3)"
     Site            111
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Site            179
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Site            186
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Site            205
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Site            236
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Site            238
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15654.3)"
     Region          279..332
                     /region_name="LIM1_TRIP6"
                     /note="The first LIM domain of Thyroid
                     receptor-interacting protein 6 (TRIP6); cd09350"
                     /db_xref="CDD:188736"
     Site            order(279,282,301,304,307,310,328,331)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188736"
     Region          339..398
                     /region_name="LIM"
                     /note="LIM is a small protein-protein interaction domain,
                     containing two zinc fingers; cl02475"
                     /db_xref="CDD:413332"
     Site            order(339,342,359,362,365,368,387,390)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188740"
     Region          399..461
                     /region_name="LIM3_Zyxin_like"
                     /note="The third LIM domain of Zyxin-like family; cd09357"
                     /db_xref="CDD:188743"
     Site            order(399,402,426,429,432,435,457,460)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188743"
     Region          469..476
                     /region_name="Interaction with MAGI1 and PTPN13.
                     /evidence=ECO:0000269|PubMed:19017743"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15654.3)"
     CDS             1..476
                     /gene="TRIP6"
                     /gene_synonym="OIP-1; OIP1; TRIP-6; TRIP6i2; ZRP-1"
                     /coded_by="NM_003302.3:112..1542"
                     /db_xref="CCDS:CCDS5708.1"
                     /db_xref="GeneID:7205"
                     /db_xref="HGNC:HGNC:12311"
                     /db_xref="MIM:602933"
ORIGIN      
        1 msgptwlppk qpeparapqg raiprgtpgp ppahgaalqp hprvnfcplp seqcyqapgg
       61 pedrgpawvg shgvlqhtqg lpadrgglrp gsldaeidll sstlaelngg rghasrrpdr
      121 qayepppppa yrtgslkpnp asplpaspyg gptpasytta stpagpafpv qvkvaqpvrg
      181 cgpprrgasq asgplpgphf plpgrgevwg pgyrsqrepg pgakeeaagv sgpagrgrgg
      241 ehgpqvplsq ppedeldrlt kklvhdmnhp psgeyfgqcg gcgedvvgdg agvvaldrvf
      301 hvgcfvcstc raqlrgqhfy averrayceg cyvatlekca tcsqpildri lramgkayhp
      361 gcftcvvchr gldgipftvd atsqihcied fhrkfaprcs vcggaimpep gqeetvriva
      421 ldrsfhigcy kceecgllls segecqgcyp ldghilckac sawriqelsa tvttdc
//
LOCUS       NP_001353786             421 aa            linear   PRI 27-APR-2025
DEFINITION  GRB2-associated-binding protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001353786 XP_024307924
VERSION     NP_001353786.1
DBSOURCE    REFSEQ: accession NM_001366857.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006548.22.
            
            On Oct 24, 2018 this sequence version replaced XP_024307924.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.204350.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.1"
     Protein         1..421
                     /product="GRB2-associated-binding protein 4 isoform 2"
                     /note="GRB2-associated binder 2-like protein;
                     GRB2-associated-binding protein 4; GRB2-associated binder
                     4; growth factor receptor bound protein 2-associated
                     protein 4"
                     /calculated_mol_wt=45879
     Region          38..158
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     CDS             1..421
                     /gene="GAB4"
                     /coded_by="NM_001366857.1:109..1374"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:128954"
                     /db_xref="HGNC:HGNC:18325"
ORIGIN      
        1 mslpspspsr elcppdpafa plsswpgsgp aggstrsghv lysgwlrksp pekklrlfaw
       61 rkrwfilrrg qtssdpdvle yykndgskkp lrtinlnlce qldvdvtlnf nkkeiqkgym
      121 fdiktsertf ylvaetredm newvqsicqi cgfrqeesta ssgkytqhgg gnasrpaesm
      181 hegvcsflpg rtlvglsdsi asegscvpmn pgsptlpavk qagddsqgvc ipvgsclvrf
      241 dllgspltel smhqdlsqgh evqlppvnrs lkpnqkanpt ppnlrnnrvi nelsfkppvt
      301 epwsgtshtf dssssqhpis tqsitntdse dsgerylfpn pasafpvsgg tsssapprst
      361 gnihyaaldf qpskpsigsv tsgkkvdyvq vdlektqalq ktmheqmclr qssepprgak
      421 l
//
LOCUS       NP_001135875             189 aa            linear   PRI 27-APR-2025
DEFINITION  sialomucin core protein 24 isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001135875
VERSION     NP_001135875.1
DBSOURCE    REFSEQ: accession NM_001142403.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Liu,J., Knopp,K.A., Rackaityte,E., Wang,C.Y., Laurie,M.T.,
            Sunshine,S., Puschnik,A.S. and DeRisi,J.L.
  TITLE     Genome-Wide Knockout Screen Identifies Human Sialomucin CD164 as an
            Essential Entry Factor for Lymphocytic Choriomeningitis Virus
  JOURNAL   mBio 13 (3), e0020522 (2022)
   PUBMED   35502904
  REMARK    GeneRIF: Genome-Wide Knockout Screen Identifies Human Sialomucin
            CD164 as an Essential Entry Factor for Lymphocytic Choriomeningitis
            Virus.
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Ozieblo,D., Lee,S.Y., Leja,M.L., Sarosiak,A., Baldyga,N.,
            Skarzynski,H., Kim,Y., Han,J.H., Yoo,H.S., Park,M.H., Choi,B.Y. and
            Oldak,M.
  TITLE     Update on CD164 and LMX1A genes to strengthen their causative role
            in autosomal dominant hearing loss
  JOURNAL   Hum Genet 141 (3-4), 445-453 (2022)
   PUBMED   35254497
  REMARK    GeneRIF: Update on CD164 and LMX1A genes to strengthen their
            causative role in autosomal dominant hearing loss.
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Bakkers,M.J.G., Moon-Walker,A., Herlo,R., Brusic,V., Stubbs,S.H.,
            Hastie,K.M., Saphire,E.O., Kirchhausen,T.L. and Whelan,S.P.J.
  TITLE     CD164 is a host factor for lymphocytic choriomeningitis virus entry
  JOURNAL   Proc Natl Acad Sci U S A 119 (10), e2119676119 (2022)
   PUBMED   35235462
  REMARK    GeneRIF: CD164 is a host factor for lymphocytic choriomeningitis
            virus entry.
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Zhang,X.W., Li,S.L., Zhang,D., Sun,X.L. and Zhai,H.J.
  TITLE     RP11-619L19.2 promotes colon cancer development by regulating the
            miR-1271-5p/CD164 axis
  JOURNAL   Oncol Rep 44 (6), 2419-2428 (2020)
   PUBMED   33125110
  REMARK    GeneRIF: RP11619L19.2 promotes colon cancer development by
            regulating the miR12715p/CD164 axis.
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Zhang,L., Wang,Y. and Su,H.
  TITLE     Long non-coding RNA LINC00152/miR-613/CD164 axis regulates cell
            proliferation, apoptosis, migration and invasion in glioma via
            PI3K/AKT pathway
  JOURNAL   Neoplasma 67 (4), 762-772 (2020)
   PUBMED   32726126
  REMARK    GeneRIF: Long non-coding RNA LINC00152/miR-613/CD164 axis regulates
            cell proliferation, apoptosis, migration and invasion in glioma via
            PI3K/AKT pathway.
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Doyonnas,R., Yi-Hsin Chan,J., Butler,L.H., Rappold,I.,
            Lee-Prudhoe,J.E., Zannettino,A.C., Simmons,P.J., Buhring,H.J.,
            Levesque,J.P. and Watt,S.M.
  TITLE     CD164 monoclonal antibodies that block hemopoietic progenitor cell
            adhesion and proliferation interact with the first mucin domain of
            the CD164 receptor
  JOURNAL   J Immunol 165 (2), 840-851 (2000)
   PUBMED   10878358
REFERENCE   7  (residues 1 to 189)
  AUTHORS   Kurosawa,N., Kanemitsu,Y., Matsui,T., Shimada,K., Ishihama,H. and
            Muramatsu,T.
  TITLE     Genomic analysis of a murine cell-surface sialomucin, MGC-24/CD164
  JOURNAL   Eur J Biochem 265 (1), 466-472 (1999)
   PUBMED   10491205
REFERENCE   8  (residues 1 to 189)
  AUTHORS   Zannettino,A.C., Buhring,H.J., Niutta,S., Watt,S.M., Benton,M.A.
            and Simmons,P.J.
  TITLE     The sialomucin CD164 (MGC-24v) is an adhesive glycoprotein
            expressed by human hematopoietic progenitors and bone marrow
            stromal cells that serves as a potent negative regulator of
            hematopoiesis
  JOURNAL   Blood 92 (8), 2613-2628 (1998)
   PUBMED   9763543
REFERENCE   9  (residues 1 to 189)
  AUTHORS   Watt,S.M., Buhring,H.J., Rappold,I., Chan,J.Y., Lee-Prudhoe,J.,
            Jones,T., Zannettino,A.C., Simmons,P.J., Doyonnas,R., Sheer,D. and
            Butler,L.H.
  TITLE     CD164, a novel sialomucin on CD34(+) and erythroid subsets, is
            located on human chromosome 6q21
  JOURNAL   Blood 92 (3), 849-866 (1998)
   PUBMED   9680353
REFERENCE   10 (residues 1 to 189)
  AUTHORS   Masuzawa,Y., Miyauchi,T., Hamanoue,M., Ando,S., Yoshida,J.,
            Takao,S., Shimazu,H., Adachi,M. and Muramatsu,T.
  TITLE     A novel core protein as well as polymorphic epithelial mucin carry
            peanut agglutinin binding sites in human gastric carcinoma cells:
            sequence analysis and examination of gene expression
  JOURNAL   J Biochem 112 (5), 609-615 (1992)
   PUBMED   1478919
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359711.18.
            
            Summary: This gene encodes a transmembrane sialomucin and cell
            adhesion molecule that regulates the proliferation, adhesion and
            migration of hematopoietic progenitor cells. The encoded protein
            also interacts with the C-X-C chemokine receptor type 4 and may
            regulate muscle development. Elevated expression of this gene has
            been observed in human patients with Sezary syndrome, a type of
            blood cancer, and a mutation in this gene may be associated with
            impaired hearing. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (4) uses alternate splice sites in
            the 3' coding region, compared to variant 1. It encodes isoform 4
            which is shorter and has a distinct C-terminus, compared to isoform
            1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D14043.1, SRR14038191.3610770.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..189
                     /product="sialomucin core protein 24 isoform 4 precursor"
                     /note="CD164 antigen, sialomucin; sialomucin core protein
                     24; multi-glycosylated core protein 24"
                     /calculated_mol_wt=17578
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2451
     Site            26
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            32
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Region          60..174
                     /region_name="MGC-24"
                     /note="Multi-glycosylated core protein 24 (MGC-24),
                     sialomucin; pfam05283"
                     /db_xref="CDD:461610"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Region          118..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04900.2)"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            142
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     CDS             1..189
                     /gene="CD164"
                     /gene_synonym="DFNA66; endolyn; MGC-24; MGC-24v; MUC-24"
                     /coded_by="NM_001142403.3:90..659"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS47463.1"
                     /db_xref="GeneID:8763"
                     /db_xref="HGNC:HGNC:1632"
                     /db_xref="MIM:603356"
ORIGIN      
        1 msrlsrsllw aatclgvlcv lsadknttqh pnvttlapis nvtsapvtsl plvttpapet
       61 cegrnscvsc fnvsvvnttc fwieckdesy cshnstvsdc qvgnttdfcs vstatpvpta
      121 nstakptvqp spsttsktvt tsgttnntvt ptsqpvrkst fdaasfiggi vlvleircht
      181 rnyipdlkk
//
LOCUS       NP_001014451             448 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX19B isoform 2 [Homo sapiens].
ACCESSION   NP_001014451
VERSION     NP_001014451.1
DBSOURCE    REFSEQ: accession NM_001014451.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Banerjee,P., Markande,S., Kalarikkal,M. and Joseph,J.
  TITLE     SUMOylation modulates the function of DDX19 in mRNA export
  JOURNAL   J Cell Sci 135 (4) (2022)
   PUBMED   35080244
  REMARK    GeneRIF: SUMOylation modulates the function of DDX19 in mRNA
            export.
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Park,Y., Park,J., Hwang,H.J., Kim,L., Jeong,K., Song,H.K.,
            Rufener,S.C., Muhlemann,O. and Kim,Y.K.
  TITLE     Translation mediated by the nuclear cap-binding complex is confined
            to the perinuclear region via a CTIF-DDX19B interaction
  JOURNAL   Nucleic Acids Res 49 (14), 8261-8276 (2021)
   PUBMED   34232997
  REMARK    GeneRIF: Translation mediated by the nuclear cap-binding complex is
            confined to the perinuclear region via a CTIF-DDX19B interaction.
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Arul Nambi Rajan,A. and Montpetit,B.
  TITLE     Emerging molecular functions and novel roles for the DEAD-box
            protein Dbp5/DDX19 in gene expression
  JOURNAL   Cell Mol Life Sci 78 (5), 2019-2030 (2021)
   PUBMED   33205304
  REMARK    GeneRIF: Emerging molecular functions and novel roles for the
            DEAD-box protein Dbp5/DDX19 in gene expression.
            Review article
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Yin,L., Li,J., Zhu,H., Lin,M., Cheng,L., Wang,Y., Zhou,Z. and
            Sha,J.
  TITLE     Identification and characterization of a gene coding a novel
            isoform of DEAD-box protein
  JOURNAL   Reprod Fertil Dev 14 (3-4), 185-189 (2002)
   PUBMED   12219940
  REMARK    GeneRIF: identification and characterization of a gene coding a
            novel isoform
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Schmitt,C., von Kobbe,C., Bachi,A., Pante,N., Rodrigues,J.P.,
            Boscheron,C., Rigaut,G., Wilm,M., Seraphin,B., Carmo-Fonseca,M. and
            Izaurralde,E.
  TITLE     Dbp5, a DEAD-box protein required for mRNA export, is recruited to
            the cytoplasmic fibrils of nuclear pore complex via a conserved
            interaction with CAN/Nup159p
  JOURNAL   EMBO J 18 (15), 4332-4347 (1999)
   PUBMED   10428971
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Mattioni,T., Hume,C.R., Konigorski,S., Hayes,P., Osterweil,Z. and
            Lee,J.S.
  TITLE     A cDNA clone for a novel nuclear protein with DNA binding activity
  JOURNAL   Chromosoma 101 (10), 618-624 (1992)
   PUBMED   1424986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012184.7, DC385044.1,
            BI756088.1, AL136639.1 and BC003626.2.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. This gene encodes a DEAD box protein,
            which exhibits RNA-dependent ATPase and ATP-dependent RNA-unwinding
            activities. This protein is recruited to the cytoplasmic fibrils of
            the nuclear pore complex, where it participates in the export of
            mRNA from the nucleus. Multiple alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.209930.1,
                                           SRR1803613.87238.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..448
                     /product="ATP-dependent RNA helicase DDX19B isoform 2"
                     /EC_number="3.6.4.13"
                     /note="DEAD-box protein 5; yeast Dbp5 homolog; DEAD/H
                     (Asp-Glu-Ala-Asp/His) box polypeptide 19 (Dbp5, yeast,
                     homolog); ATP-dependent RNA helicase DDX19; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 19B; ATP-dependent RNA
                     helicase DDX19B; DEAD-box RNA helicase DEAD5; DEAD box
                     protein 19B; DEAD (Asp-Glu-Ala-As) box polypeptide 19B;
                     dead box protein 5 homolog"
                     /calculated_mol_wt=50359
     Region          75..272
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          101..445
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Site            order(109..115,211)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     CDS             1..448
                     /gene="DDX19B"
                     /gene_synonym="DBP5; DDX19; RNAh"
                     /coded_by="NM_001014451.3:246..1592"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS32475.1"
                     /db_xref="GeneID:11269"
                     /db_xref="HGNC:HGNC:2742"
                     /db_xref="MIM:605812"
ORIGIN      
        1 matdswalav deqeaaaesl snlhlkeeki kpdtngavvk tnanaektde eekedraaqs
       61 llnklirsnl vdntnqvevl qrdpnsplys vksfeelrlp qnliaqsqsg tgktaafvla
      121 mlsqvepank ypqclclspt yelalqtgkv ieqmgkfype lklayavrgn klergqkise
      181 qivigtpgtv ldwcsklkfi dpkkikvfvl deadvmiatq ghqdqsiriq rmlprncqml
      241 lfsatfedsv wkfaqkvvpd pnviklkree etldtikqyy vlcssrdekf qalcnlygai
      301 tiaqamifch trktaswlaa elskeghqva llsgemmveq raavierfre gkekvlvttn
      361 vcargidveq vsvvinfdlp vdkdgnpdne tylhrigrtg rfgkrglavn mvdskhsmni
      421 lnriqehfnk kierldtddl deiekian
//
LOCUS       NP_081697               1198 aa            linear   ROD 27-APR-2025
DEFINITION  integrator complex subunit 2 isoform 2 [Mus musculus].
ACCESSION   NP_081697
VERSION     NP_081697.2
DBSOURCE    REFSEQ: accession NM_027421.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1198)
  AUTHORS   Alvarez-Dominguez,J.R., Zhang,X. and Hu,W.
  TITLE     Widespread and dynamic translational control of red blood cell
            development
  JOURNAL   Blood 129 (5), 619-629 (2017)
   PUBMED   27899360
REFERENCE   4  (residues 1 to 1198)
  AUTHORS   Tkatchenko,T.V., Moreno-Rodriguez,R.A., Conway,S.J.,
            Molkentin,J.D., Markwald,R.R. and Tkatchenko,A.V.
  TITLE     Lack of periostin leads to suppression of Notch1 signaling and
            calcific aortic valve disease
  JOURNAL   Physiol Genomics 39 (3), 160-168 (2009)
   PUBMED   19723774
REFERENCE   5  (residues 1 to 1198)
  AUTHORS   Baillat,D., Hakimi,M.A., Naar,A.M., Shilatifard,A., Cooch,N. and
            Shiekhattar,R.
  TITLE     Integrator, a multiprotein mediator of small nuclear RNA
            processing, associates with the C-terminal repeat of RNA polymerase
            II
  JOURNAL   Cell 123 (2), 265-276 (2005)
   PUBMED   16239144
  REMARK    GeneRIF: characterization of the human Integrator complex
REFERENCE   6  (residues 1 to 1198)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Kitamura,H., Nakagawa,T., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of FLJ
            genes: the complete nucleotide sequences of 110 mouse
            FLJ-homologous cDnas identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (2), 127-135 (2004)
   PUBMED   15449545
REFERENCE   7  (residues 1 to 1198)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   8  (residues 1 to 1198)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL592065.7, CF166557.1, AK129323.1, BC059056.1 and AK164097.1.
            
            On Feb 4, 2006 this sequence version replaced NP_081697.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK129323.1, BC050081.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 51.71 cM"
     Protein         1..1198
                     /product="integrator complex subunit 2 isoform 2"
                     /note="int2"
                     /calculated_mol_wt=133385
     Region          27..1131
                     /region_name="INTS2"
                     /note="Integrator complex subunit 2; pfam14750"
                     /db_xref="CDD:464296"
     Site            421..437
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80UK8.2)"
     CDS             1..1198
                     /gene="Ints2"
                     /gene_synonym="2810417D08Rik; mKIAA1287"
                     /coded_by="NM_027421.3:403..3999"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS25198.1"
                     /db_xref="GeneID:70422"
                     /db_xref="MGI:MGI:1917672"
ORIGIN      
        1 mtpegtglqf vspfafeamq kvdvvrlasl sdpelrlllp clvrmalcap adqsqswaqd
       61 kklilrllsg veavnsival lsvdfhaleq daskeqqlrh klgggsgesi lvsqlqhglt
      121 lefehsdspr rlrlvlsell aimnkvsecn gefffkssel fesavyleea advlcilqae
      181 lpsllpivdv aeallrvrng awflcllvan vpdsfnevcr glikngerqd eeslggrrrt
      241 dalrflcrmn psqalkvrgm vveechlpgl gvaltldhtk teacedgvsd lvcfvsglll
      301 gtnakvrtwf gtfirngqqr kretsgsvlw qmrrqlllel mgilptvrst riveeadvem
      361 eptvsvysgl keehvvkasa llrlycalmg iaglkpteee aeqllqlmts rppatpagvr
      421 fvslsfcmll afstlvstpe qeqlmvlwls wmikeeayfe stsgvsasfg emlllvamyf
      481 hsnqlsaiid lvcstlgmki vikpsslsrm ktiftqeift eqvvtahavr vpvtsnlsan
      541 itgflpihci yqllrsrsft khkvsikdwi yrqlcetstp lhpqllplid vyinsiltpa
      601 sksnpeatnq pvteqeilnl fqeviggdsv rltqrfsita qllvlyyils yeeallantk
      661 tlasmqrkpk syssslmdqi pikflirqaq glqqelgglh sallrllatn yphlcivddw
      721 iceeeitgtd allrrmllts nakthspkql qeafsavpvs htqvmqimeh ltllsaseli
      781 pyaevltsnm nqllnsgvpr rilqtvnklw mvlntvmprr lwvmtvnalq psikfirqqk
      841 ytqndlmidp livlrcdrrv hrcpplmdvt lhmlngylla skaylsahlk etaeqdrpsp
      901 nntvglvgqt dapevtreel knallaaqds aavqilleic lpteeekakg ansdislrnt
      961 qgvttistps keteegednl lcnlrevqcl iccllhqmyi adpniaklvh fqgypcellp
     1021 ltvagipsmh icldfipeli aqpelekqif aiqllshlci qyalpkslsv arlavnvmgt
     1081 lltvltqakr ysffmptlps lvsfcrafpp lyedimslli qigqvcasdv atqtrdidpi
     1141 itrlqqikek psgwsqickd psykngsrdt gsmdpdvqlc hciestiiei inmsvsgi
//
LOCUS       NP_001354473             577 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 37 [Homo sapiens].
ACCESSION   NP_001354473 XP_005270252
VERSION     NP_001354473.1
DBSOURCE    REFSEQ: accession NM_001367544.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 577)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 577)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 577)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 577)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_005270252.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.492485.1,
                                           SRR3476690.634999.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..577
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 37"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=63870
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          445..572
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..577
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367544.1:95..1828"
                     /note="isoform 37 is encoded by transcript variant 37"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kpqsnnknsl
      361 vspaqepapl qtamepqttv vhnatdgikg stescnttte dedlkaaplr tgngssvpeg
      421 rssrdrtaps agmqpqpslc ssamrkqeii kiteqlieai nngdfeaytk icdpgltsfe
      481 pealgnlveg mdfhkfyfen llsknskpih ttilnphvhv igedaaciay irltqyidgq
      541 grprtsqsee trvwhrrdgk wlnvhyhcsg apaaplq
//
LOCUS       NP_919337                288 aa            linear   PRI 27-APR-2025
DEFINITION  syntaxin-2 isoform 2 [Homo sapiens].
ACCESSION   NP_919337
VERSION     NP_919337.1
DBSOURCE    REFSEQ: accession NM_194356.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Kang,F., Xie,L., Qin,T., Miao,Y., Kang,Y., Takahashi,T., Liang,T.,
            Xie,H. and Gaisano,H.Y.
  TITLE     Plasma membrane flipping of Syntaxin-2 regulates its inhibitory
            action on insulin granule exocytosis
  JOURNAL   Nat Commun 13 (1), 6512 (2022)
   PUBMED   36316316
  REMARK    GeneRIF: Plasma membrane flipping of Syntaxin-2 regulates its
            inhibitory action on insulin granule exocytosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Wang,Y.X., Li,Y.Z., Zhu,H.F., Zhang,Z.Y., Qian,X.L. and He,G.Y.
  TITLE     STX2 drives colorectal cancer proliferation via upregulation of
            EXOSC4
  JOURNAL   Life Sci 263, 118597 (2020)
   PUBMED   33075373
  REMARK    GeneRIF: STX2 drives colorectal cancer proliferation via
            upregulation of EXOSC4.
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wang,Y., Xu,H., Jiao,H., Wang,S., Xiao,Z., Zhao,Y., Bi,J., Wei,W.,
            Liu,S., Qiu,J., Li,T., Liang,L., Ye,Y., Liao,W. and Ding,Y.
  TITLE     STX2 promotes colorectal cancer metastasis through a positive
            feedback loop that activates the NF-kappaB pathway
  JOURNAL   Cell Death Dis 9 (6), 664 (2018)
   PUBMED   29855462
  REMARK    GeneRIF: STX2 as a crucial modulator of the aggressive colorectal
            cancer phenotype.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Zha,H., Remmers,E.F., Szpirer,C., Szpirer,J., Zhang,H., Kozak,C.A.
            and Wilder,R.L.
  TITLE     The epimorphin gene is highly conserved among humans, mice, and
            rats and maps to human chromosome 7, mouse chromosome 5, and rat
            chromosome 12
  JOURNAL   Genomics 37 (3), 386-389 (1996)
   PUBMED   8938452
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Oka,Y. and Hirai,Y.
  TITLE     Inductive influences of epimorphin on endothelial cells in vitro
  JOURNAL   Exp Cell Res 222 (1), 189-198 (1996)
   PUBMED   8549663
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Li,C., Ullrich,B., Zhang,J.Z., Anderson,R.G., Brose,N. and
            Sudhof,T.C.
  TITLE     Ca(2+)-dependent and -independent activities of neural and
            non-neural synaptotagmins
  JOURNAL   Nature 375 (6532), 594-599 (1995)
   PUBMED   7791877
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Hirai,Y.
  TITLE     Molecular cloning of human epimorphin: identification of isoforms
            and their unique properties
  JOURNAL   Biochem Biophys Res Commun 191 (3), 1332-1337 (1993)
   PUBMED   8466509
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Hirai,Y., Takebe,K., Takashina,M., Kobayashi,S. and Takeichi,M.
  TITLE     Epimorphin: a mesenchymal protein essential for epithelial
            morphogenesis
  JOURNAL   Cell 69 (3), 471-481 (1992)
   PUBMED   1581962
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073912.38.
            
            Summary: The product of this gene belongs to the
            syntaxin/epimorphin family of proteins. The syntaxins are a large
            protein family implicated in the targeting and fusion of
            intracellular transport vesicles. The product of this gene
            regulates epithelial-mesenchymal interactions and epithelial cell
            morphogenesis and activation. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) encodes the longest isoform
            (2). Variants 2 and 9 both encode the same isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.83728.1,
                                           SRR1803617.74079.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392373.7/ ENSP00000376178.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..288
                     /product="syntaxin-2 isoform 2"
                     /note="epimorphin"
                     /calculated_mol_wt=33210
     Region          31..226
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          227..278
                     /region_name="SNARE"
                     /note="SNARE domain; pfam05739"
                     /db_xref="CDD:461727"
     Site            265..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32856.3)"
     CDS             1..288
                     /gene="STX2"
                     /gene_synonym="EPIM; EPM; STX2A; STX2B; STX2C"
                     /coded_by="NM_194356.4:152..1018"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9270.1"
                     /db_xref="GeneID:2054"
                     /db_xref="HGNC:HGNC:3403"
                     /db_xref="MIM:132350"
ORIGIN      
        1 mrdrlpdlta crknddgdtv vvvekdhfmd dffhqveeir nsidkitqyv eevkknhsii
       61 lsapnpegki keeledlnke ikktankira klkaieqsfd qdesgnrtsv dlrirrtqhs
      121 vlsrkfveam aeyneaqtlf rerskgriqr qleitgrttt ddeleemles gkpsiftsdi
      181 isdsqitrqa lneiesrhkd imkletsire lhemfmdmam fvetqgemin niernvmnat
      241 dyvehakeet kkaikyqska rrkkwiiiav svvlvaiial iiglsvgk
//
LOCUS       NP_660151                393 aa            linear   PRI 27-APR-2025
DEFINITION  short-chain dehydrogenase/reductase family 42E member 1 [Homo
            sapiens].
ACCESSION   NP_660151
VERSION     NP_660151.2
DBSOURCE    REFSEQ: accession NM_145168.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Hendi,N.N. and Nemer,G.
  TITLE     In silico characterization of the novel SDR42E1 as a potential
            vitamin D modulator
  JOURNAL   J Steroid Biochem Mol Biol 238, 106447 (2024)
   PUBMED   38160768
  REMARK    GeneRIF: In silico characterization of the novel SDR42E1 as a
            potential vitamin D modulator.
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Bouhouche,A., Albaroudi,N., El Alaoui,M.A., Askander,O.,
            Habbadi,Z., El Hassani,A., Iraqi,H., El Fahime,E. and Belmekki,M.
  TITLE     Identification of the novel SDR42E1 gene that affects steroid
            biosynthesis associated with the oculocutaneous genital syndrome
  JOURNAL   Exp Eye Res 209, 108671 (2021)
   PUBMED   34133966
  REMARK    GeneRIF: Identification of the novel SDR42E1 gene that affects
            steroid biosynthesis associated with the oculocutaneous genital
            syndrome.
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX482154.1, BC019670.1, AK026740.1, CB851753.1 and AC092142.5.
            
            On Oct 19, 2006 this sequence version replaced NP_660151.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026740.1, AK315652.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000328945.7/ ENSP00000332407.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.3"
     Protein         1..393
                     /product="short-chain dehydrogenase/reductase family 42E
                     member 1"
                     /EC_number="1.1.1.-"
                     /calculated_mol_wt=44153
     Region          10..350
                     /region_name="3b-HSD_like_1_SDR_e"
                     /note="3beta-hydroxysteroid dehydrogenase (3b-HSD)-like,
                     subgroup1, extended (e) SDRs; cd09812"
                     /db_xref="CDD:187672"
     Site            order(15,17..20,39..41,79..81,98,121..123,152,156,
                     185..188)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187672"
     Site            order(99,123,152,156)
                     /site_type="active"
                     /db_xref="CDD:187672"
     Site            order(123,152,187,200,211,216)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187672"
     Site            282..302
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUS8.2)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUS8.2)"
     CDS             1..393
                     /gene="SDR42E1"
                     /gene_synonym="HSPC105"
                     /coded_by="NM_145168.3:111..1292"
                     /db_xref="CCDS:CCDS42205.1"
                     /db_xref="GeneID:93517"
                     /db_xref="HGNC:HGNC:29834"
                     /db_xref="MIM:616164"
ORIGIN      
        1 mdpkrsqkes vlitggsgyf gfrlgcalnq ngvhvilfdi sspaqtipeg ikfiqgdirh
       61 lsdvekafqd advtcvfhia sygmsgreql nrnlikevnv rgtdnilqvc qrrrvprlvy
      121 tstfnvifgg qvirngdesl pylplhlhpd hysrtksiae qkvleanatp ldrgdgvlrt
      181 calrpagiyg pgeqrhlpri vsyiekglfk fvygdprslv efvhvdnlvq ahilasealr
      241 adkghiasgq pyfisdgrpv nnfeffrplv eglgytfpst rlpltlvycf afltemvhfi
      301 lgrlynfqpf ltrtevyktg vthyfsleka kkelgykaqp fdlqeavewf kahghgrssg
      361 srdsecfvwd gllvflliia vlmwlpssvi lsl
//
LOCUS       NP_689620                225 aa            linear   PRI 27-APR-2025
DEFINITION  grpE protein homolog 2, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_689620
VERSION     NP_689620.2
DBSOURCE    REFSEQ: accession NM_152407.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Manjunath,P., Stojkovic,G., Euro,L., Konovalova,S., Wanrooij,S.,
            Koski,K. and Tyynismaa,H.
  TITLE     Preferential binding of ADP-bound mitochondrial HSP70 to the
            nucleotide exchange factor GRPEL1 over GRPEL2
  JOURNAL   Protein Sci 33 (11), e5190 (2024)
   PUBMED   39445986
  REMARK    GeneRIF: Preferential binding of ADP-bound mitochondrial HSP70 to
            the nucleotide exchange factor GRPEL1 over GRPEL2.
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Tang,C.T., Li,Y.F., Chou,C.H., Huang,L.C., Huang,S.M., Hueng,D.Y.,
            Tsai,C.K. and Chen,Y.H.
  TITLE     GRPEL2 Knockdown Exerts Redox Regulation in Glioblastoma
  JOURNAL   Int J Mol Sci 22 (23), 12705 (2021)
   PUBMED   34884508
  REMARK    GeneRIF: GRPEL2 Knockdown Exerts Redox Regulation in Glioblastoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Konovalova,S., Liu,X., Manjunath,P., Baral,S., Neupane,N.,
            Hilander,T., Yang,Y., Balboa,D., Terzioglu,M., Euro,L.,
            Varjosalo,M. and Tyynismaa,H.
  TITLE     Redox regulation of GRPEL2 nucleotide exchange factor for
            mitochondrial HSP70 chaperone
  JOURNAL   Redox Biol 19, 37-45 (2018)
   PUBMED   30098457
  REMARK    GeneRIF: The dimerization of GRPEL2 may activate the folding
            machinery responsible for protein import into mitochondrial matrix
            or enhance the chaperone activity of mitochondrial HSP70, thus
            protecting mitochondrial proteostasis in oxidative stress.
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Srivastava,S., Savanur,M.A., Sinha,D., Birje,A., R,V., Saha,P.P.
            and D'Silva,P.
  TITLE     Regulation of mitochondrial protein import by the nucleotide
            exchange factors GrpEL1 and GrpEL2 in human cells
  JOURNAL   J Biol Chem 292 (44), 18075-18090 (2017)
   PUBMED   28848044
  REMARK    GeneRIF: Data suggest that two putative NEF (nucleotide exchange
            factors) orthologs, GRPEL1 and GRPEL2, modulate function of
            mitochondrial HSP70 (mtHSP70); both GRPEL1 and GRPEL2 associate
            with mtHSP70 as hetero-oligomeric subcomplex and regulate mtHSP70
            transport. (GRPEL = mitochondrial GrpE-like protein; HSP70 =
            heat-shock protein 70)
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Bauer,M.F., Gempel,K., Reichert,A.S., Rappold,G.A., Lichtner,P.,
            Gerbitz,K.D., Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     Genetic and structural characterization of the human mitochondrial
            inner membrane translocase
  JOURNAL   J Mol Biol 289 (1), 69-82 (1999)
   PUBMED   10339406
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Naylor,D.J., Stines,A.P., Hoogenraad,N.J. and Hoj,P.B.
  TITLE     Evidence for the existence of distinct mammalian cytosolic,
            microsomal, and two mitochondrial GrpE-like proteins, the
            Co-chaperones of specific Hsp70 members
  JOURNAL   J Biol Chem 273 (33), 21169-21177 (1998)
   PUBMED   9694873
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL704536.1, BC036678.1 and AC131025.1.
            
            On Dec 20, 2003 this sequence version replaced NP_689620.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036678.1, SRR1803616.222430.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000329271.8/
                                                  ENSP00000329558.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..225
                     /product="grpE protein homolog 2, mitochondrial precursor"
                     /note="grpE protein homolog 2, mitochondrial"
                     /calculated_mol_wt=21709
     transit_peptide 1..32
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q8TAA5.1)"
                     /calculated_mol_wt=3740
     mat_peptide     33..225
                     /product="GrpE protein homolog 2, mitochondrial.
                     /id=PRO_0000013052"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAA5.1)"
                     /calculated_mol_wt=21709
     Region          74..217
                     /region_name="GrpE"
                     /note="nucleotide exchange factor GrpE; cd00446"
                     /db_xref="CDD:271355"
     Region          74..124
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
     Site            order(76,79..80,83..84,86..87,90..92,94,97..98,101..102,
                     105..106,108..109,112..114,116..120,122..123,146..147,
                     149..151,154,160..161)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271355"
     Site            order(92,100,122,125,173,175..176,178..182,199,208,212,
                     214,217)
                     /site_type="other"
                     /note="Hsp70 (ATPase domain) interactions [polypeptide
                     binding]"
                     /db_xref="CDD:271355"
     Site            142
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8TAA5.1)"
     Region          146..161
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
     CDS             1..225
                     /gene="GRPEL2"
                     /gene_synonym="Mt-GrpE#2"
                     /coded_by="NM_152407.4:42..719"
                     /db_xref="CCDS:CCDS4295.1"
                     /db_xref="GeneID:134266"
                     /db_xref="HGNC:HGNC:21060"
                     /db_xref="MIM:618545"
ORIGIN      
        1 mavrslwagr lrvqrllaws aaweskgwpl pfstatqrta gedcrsedpp delgpplaer
       61 alrvkavkle kevqdltvry qraiadceni rrrtqrcved akifgiqsfc kdlvevadil
      121 ekttecisee sepedqkltl ekvfrgllll eaklksvfak hglekltpig dkydphehel
      181 ichvpagvgv qpgtvalvrq dgyklhgrti rlarvevave sqrrl
//
LOCUS       NP_001350742             778 aa            linear   PRI 27-APR-2025
DEFINITION  axin-2 isoform 2 [Homo sapiens].
ACCESSION   NP_001350742 XP_016880683
VERSION     NP_001350742.1
DBSOURCE    REFSEQ: accession NM_001363813.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Alhazmi,N., Alaqla,A., Almuzzaini,B., Aldrees,M., Alnaqa,G.,
            Almasoud,F., Aldibasi,O. and Alshamlan,H.
  TITLE     What could be the role of genetic tests and machine learning of
            AXIN2 variant dominance in non-syndromic hypodontia? A case-control
            study in orthodontically treated patients
  JOURNAL   Prog Orthod 25 (1), 31 (2024)
   PUBMED   39183201
  REMARK    GeneRIF: What could be the role of genetic tests and machine
            learning of AXIN2 variant dominance in non-syndromic hypodontia? A
            case-control study in orthodontically treated patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Zheng,Y., Wang,Y., Qi,B., Gao,W., Liu,Y. and Li,T.
  TITLE     Axin2 depletion in macrophages alleviated senescence and increased
            immune response after myocardial infarction
  JOURNAL   Inflamm Res 73 (3), 407-414 (2024)
   PUBMED   38158447
  REMARK    GeneRIF: Axin2 depletion in macrophages alleviated senescence and
            increased immune response after myocardial infarction.
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Cao,W., Dai,S., Ruan,W., Long,T., Zeng,Z. and Lei,S.
  TITLE     Pancreatic stellate cell-derived exosomal tRF-19-PNR8YPJZ promotes
            proliferation and mobility of pancreatic cancer through AXIN2
  JOURNAL   J Cell Mol Med 27 (17), 2533-2546 (2023)
   PUBMED   37488774
  REMARK    GeneRIF: Pancreatic stellate cell-derived exosomal tRF-19-PNR8YPJZ
            promotes proliferation and mobility of pancreatic cancer through
            AXIN2.
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Zhai,J., Chen,H., Wong,C.C., Peng,Y., Gou,H., Zhang,J., Pan,Y.,
            Chen,D., Lin,Y., Wang,S., Kang,W., To,K.F., Chen,Z., Nie,Y.,
            He,H.H., Sung,J.J. and Yu,J.
  TITLE     ALKBH5 Drives Immune Suppression Via Targeting AXIN2 to Promote
            Colorectal Cancer and Is a Target for Boosting Immunotherapy
  JOURNAL   Gastroenterology 165 (2), 445-462 (2023)
   PUBMED   37169182
  REMARK    GeneRIF: ALKBH5 Drives Immune Suppression Via Targeting AXIN2 to
            Promote Colorectal Cancer and Is a Target for Boosting
            Immunotherapy.
REFERENCE   5  (residues 1 to 778)
  AUTHORS   Wang,L., Guo,M., Gao,L., Liu,K., Bai,J. and Liu,Z.
  TITLE     JNK2 Promotes Progression of Esophageal Squamous Cell Carcinoma via
            Inhibiting Axin2
  JOURNAL   Curr Pharm Des 29 (37), 2977-2987 (2023)
   PUBMED   37957865
  REMARK    GeneRIF: JNK2 Promotes Progression of Esophageal Squamous Cell
            Carcinoma via Inhibiting Axin2.
REFERENCE   6  (residues 1 to 778)
  AUTHORS   von Kries,J.P., Winbeck,G., Asbrand,C., Schwarz-Romond,T.,
            Sochnikova,N., Dell'Oro,A., Behrens,J. and Birchmeier,W.
  TITLE     Hot spots in beta-catenin for interactions with LEF-1, conductin
            and APC
  JOURNAL   Nat Struct Biol 7 (9), 800-807 (2000)
   PUBMED   10966653
REFERENCE   7  (residues 1 to 778)
  AUTHORS   Ikeda,S., Kishida,M., Matsuura,Y., Usui,H. and Kikuchi,A.
  TITLE     GSK-3beta-dependent phosphorylation of adenomatous polyposis coli
            gene product can be modulated by beta-catenin and protein
            phosphatase 2A complexed with Axin
  JOURNAL   Oncogene 19 (4), 537-545 (2000)
   PUBMED   10698523
REFERENCE   8  (residues 1 to 778)
  AUTHORS   Kikuchi,A.
  TITLE     Modulation of Wnt signaling by Axin and Axil
  JOURNAL   Cytokine Growth Factor Rev 10 (3-4), 255-265 (1999)
   PUBMED   10647780
  REMARK    Review article
REFERENCE   9  (residues 1 to 778)
  AUTHORS   Mai,M., Qian,C., Yokomizo,A., Smith,D.I. and Liu,W.
  TITLE     Cloning of the human homolog of conductin (AXIN2), a gene mapping
            to chromosome 17q23-q24
  JOURNAL   Genomics 55 (3), 341-344 (1999)
   PUBMED   10049590
REFERENCE   10 (residues 1 to 778)
  AUTHORS   Hart,M.J., de los Santos,R., Albert,I.N., Rubinfeld,B. and
            Polakis,P.
  TITLE     Downregulation of beta-catenin by human Axin and its association
            with the APC tumor suppressor, beta-catenin and GSK3 beta
  JOURNAL   Curr Biol 8 (10), 573-581 (1998)
   PUBMED   9601641
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC115994.24.
            
            On Jun 3, 2018 this sequence version replaced XP_016880683.1.
            
            Summary: The Axin-related protein, Axin2, presumably plays an
            important role in the regulation of the stability of beta-catenin
            in the Wnt signaling pathway, like its rodent homologs, mouse
            conductin/rat axil. In mouse, conductin organizes a multiprotein
            complex of APC (adenomatous polyposis of the colon), beta-catenin,
            glycogen synthase kinase 3-beta, and conductin, which leads to the
            degradation of beta-catenin. Apparently, the deregulation of
            beta-catenin is an important event in the genesis of a number of
            malignancies. The AXIN2 gene has been mapped to 17q23-q24, a region
            that shows frequent loss of heterozygosity in breast cancer,
            neuroblastoma, and other tumors. Mutations in this gene have been
            associated with colorectal cancer with defective mismatch repair.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2087211.1,
                                           SRR18074969.3238424.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.1"
     Protein         1..778
                     /product="axin-2 isoform 2"
                     /note="conductin; axin-like protein; axis inhibition
                     protein 2"
                     /calculated_mol_wt=86550
     Region          10..75
                     /region_name="AXIN1_TNKS_BD"
                     /note="Axin-1 tankyrase binding domain; pfam16646"
                     /db_xref="CDD:465215"
     Region          82..198
                     /region_name="RGS_Axin"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the Axin protein; cd08707"
                     /db_xref="CDD:188662"
     Site            order(86..89,92,109,112..113,116..117,119,129..130,
                     132..134,136..137)
                     /site_type="other"
                     /note="APC binding site [polypeptide binding]"
                     /db_xref="CDD:188662"
     Region          433..468
                     /region_name="Axin_b-cat_bind"
                     /note="Axin beta-catenin binding motif; pfam08833"
                     /db_xref="CDD:462616"
     Region          696..778
                     /region_name="DAX"
                     /note="Domain present in Dishevelled and axin; smart00021"
                     /db_xref="CDD:197474"
     CDS             1..778
                     /gene="AXIN2"
                     /gene_synonym="AXIL; ODCRCS"
                     /coded_by="NM_001363813.1:316..2652"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS86634.1"
                     /db_xref="GeneID:8313"
                     /db_xref="HGNC:HGNC:904"
                     /db_xref="MIM:604025"
ORIGIN      
        1 mssamlvtcl pdpsssfred aprppvpgee getppcqpgv gkgqvtkpmp vssntrrned
       61 glgepegras pdspltrwtk slhsllgdqd gaylfrtfle rekcvdtldf wfacngfrqm
      121 nlkdtktlrv akaiykryie nnsivskqlk patktyirdg ikkqqidsim fdqaqteiqs
      181 vmeenayqmf ltsdiyleyv rsggentaym sngglgslkv vcgylptlne eeewtcadfk
      241 cklsptvvgl ssktlratas vrstetvdsg yrsfkrsdpv npyhigsgyv fapatsands
      301 eissdaltdd smsmtdssvd gippyrvgsk kqlqremhrs vkangqvslp hfprthrlpk
      361 emtpvepatf aaelisrlek lklelesrhs leerlqqire deeregselt lnsregaptq
      421 hplsllpsgs yeedpqtild dhlsrvlktp gcqspgvgry sprsrspdhh hhhhsqyhsl
      481 lppggklppa aaspgacpll ggkgfvtkqt tkhvhhhyih hhavpktkee ieaeatqrvh
      541 cfcpggseyy cyskckshsk apetmpseqf gaqstkkayp lesarsspge rasrhhlwgg
      601 nsghprttpr ahlftqdpam ppltppntla qleeacrrla evskppkqrc cvasqqrdrn
      661 hsatvqtgat pfsnpslape dhkepkklag vhalqaselv vtyffcgeei pyrrmlkaqs
      721 ltlghfkeql skkgnyryyf kkasdefacg avfeeiwede tvlpmyegri lgkverid
//
LOCUS       NP_000659                375 aa            linear   PRI 27-APR-2025
DEFINITION  all-trans-retinol dehydrogenase [NAD(+)] ADH1B isoform 1 [Homo
            sapiens].
ACCESSION   NP_000659
VERSION     NP_000659.2
DBSOURCE    REFSEQ: accession NM_000668.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Yokoyama,A., Yokoyama,T., Yumoto,Y., Takimura,T., Toyama,T.,
            Yoneda,J., Nishimura,K., Minobe,R., Matsuzaki,T., Kimura,M. and
            Matsushita,S.
  TITLE     Associations of ADH1B and ALDH2 genotypes and alcohol flushing with
            drinking history, withdrawal symptoms, and ICD-10 criteria in
            Japanese alcohol-dependent men
  JOURNAL   Pharmacogenet Genomics 34 (5), 139-148 (2024)
   PUBMED   38465575
  REMARK    GeneRIF: Associations of ADH1B and ALDH2 genotypes and alcohol
            flushing with drinking history, withdrawal symptoms, and ICD-10
            criteria in Japanese alcohol-dependent men.
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Gautheron,J., Elsayed,S., Pistorio,V., Lockhart,S., Zammouri,J.,
            Auclair,M., Koulman,A., Meadows,S.R., Lhomme,M., Ponnaiah,M.,
            Si-Bouazza,R., Fabrega,S., Belkadi,A., Delaunay,J.L.,
            Ait-Slimane,T., Feve,B., Vigouroux,C., Abdel Ghaffar,T.Y.,
            O'Rahilly,S. and Jeru,I.
  CONSRTM   Qatar Genome Project
  TITLE     ADH1B, the adipocyte-enriched alcohol dehydrogenase, plays an
            essential, cell-autonomous role in human adipogenesis
  JOURNAL   Proc Natl Acad Sci U S A 121 (24), e2319301121 (2024)
   PUBMED   38838011
  REMARK    GeneRIF: ADH1B, the adipocyte-enriched alcohol dehydrogenase, plays
            an essential, cell-autonomous role in human adipogenesis.
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Chuah,M.H., Leask,M.P., Topless,R.K., Gamble,G.D., Sumpter,N.A.,
            Stamp,L.K., Merriman,T.R. and Dalbeth,N.
  TITLE     Interaction of genetic variation at ADH1B and MLXIPL with alcohol
            consumption for elevated serum urate level and gout among people of
            European ethnicity
  JOURNAL   Arthritis Res Ther 26 (1), 45 (2024)
   PUBMED   38331848
  REMARK    GeneRIF: Interaction of genetic variation at ADH1B and MLXIPL with
            alcohol consumption for elevated serum urate level and gout among
            people of European ethnicity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Yin,D., Zhang,Y., Li,H. and Cheng,L.
  TITLE     Association of TOP2A and ADH1B with lipid levels and prognosis in
            patients with lung adenocarcinoma and squamous cell carcinoma
  JOURNAL   Clin Respir J 17 (12), 1301-1315 (2023)
   PUBMED   37985446
  REMARK    GeneRIF: Association of TOP2A and ADH1B with lipid levels and
            prognosis in patients with lung adenocarcinoma and squamous cell
            carcinoma.
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Jiang,C., Liu,R. and Wu,X.
  TITLE     Alcohol dehydrogenase-1B represses the proliferation, invasion and
            migration of breast cancer cells by inactivating the
            mitogen-activated protein kinase signalling pathway
  JOURNAL   J Physiol Pharmacol 74 (5) (2023)
   PUBMED   38085522
  REMARK    GeneRIF: Alcohol dehydrogenase-1B represses the proliferation,
            invasion and migration of breast cancer cells by inactivating the
            mitogen-activated protein kinase signalling pathway.
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Hurley,T.D., Bosron,W.F., Hamilton,J.A. and Amzel,L.M.
  TITLE     Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic
            effects of non-active-site substitutions
  JOURNAL   Proc Natl Acad Sci U S A 88 (18), 8149-8153 (1991)
   PUBMED   1896463
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Winter,L.A., Stewart,M.J., Shean,M.L., Dong,Y., Poellinger,L.,
            Okret,S., Gustafsson,J.A. and Duester,G.
  TITLE     A hormone response element upstream from the human alcohol
            dehydrogenase gene ADH2 consists of three tandem glucocorticoid
            receptor binding sites
  JOURNAL   Gene 91 (2), 233-240 (1990)
   PUBMED   2210383
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Stewart,M.J., McBride,M.S., Winter,L.A. and Duester,G.
  TITLE     Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and
            ADH3: interaction of CCAAT/enhancer-binding protein with elements
            flanking the ADH2 TATA box
  JOURNAL   Gene 90 (2), 271-279 (1990)
   PUBMED   2169444
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Carr,L.G. and Edenberg,H.J.
  TITLE     cis-acting sequences involved in protein binding and in vitro
            transcription of the human alcohol dehydrogenase gene ADH2
  JOURNAL   J Biol Chem 265 (3), 1658-1664 (1990)
   PUBMED   2295648
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Lange,L.G., Sytkowski,A.J. and Vallee,B.L.
  TITLE     Human liver alcohol dehydrogenase: purification, composition, and
            catalytic features
  JOURNAL   Biochemistry 15 (21), 4687-4693 (1976)
   PUBMED   9982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC033009.2, AF153821.1,
            AK301018.1, AC097530.3 and BU687181.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 11, 2003 this sequence version replaced NP_000659.1.
            
            Summary: The protein encoded by this gene is a member of the
            alcohol dehydrogenase family. Members of this enzyme family
            metabolize a wide variety of substrates, including ethanol,
            retinol, other aliphatic alcohols, hydroxysteroids, and lipid
            peroxidation products. This encoded protein, consisting of several
            homo- and heterodimers of alpha, beta, and gamma subunits, exhibits
            high activity for ethanol oxidation and plays a major role in
            ethanol catabolism. Three genes encoding alpha, beta and gamma
            subunits are tandemly organized in a genomic segment as a gene
            cluster. Two transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, Nov 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ224285.1, AF153821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162895, SAMN03267776
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305046.13/ ENSP00000306606.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..375
                     /product="all-trans-retinol dehydrogenase [NAD(+)] ADH1B
                     isoform 1"
                     /EC_number="1.1.1.105"
                     /note="ADH, beta subunit; alcohol dehydrogenase 2 (class
                     I), beta polypeptide; aldehyde reductase; alcohol
                     dehydrogenase subunit beta; epididymis secretory protein
                     Li 117; all-trans-retinol dehydrogenase [NAD(+)] ADH1B"
                     /calculated_mol_wt=39705
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:6391920; propagated from
                     UniProtKB/Swiss-Prot (P00325.3)"
     Region          3..375
                     /region_name="alcohol_DH_class_I_II_IV"
                     /note="class I, II, IV alcohol dehydrogenases; cd08299"
                     /db_xref="CDD:176259"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P00325.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P00325.3)"
     Site            order(47,68,175)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176259"
     Site            order(48..49,175,179,200..204,224..225,229,269..270,
                     274..275,293..294,318..320,370)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176259"
     Site            order(49,68,94,117,142,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176259"
     Site            order(98..99,101,104,112)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176259"
     Site            order(102..103,106,111,261..262,273,286..287,292..293,
                     301..306,309..319)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176259"
     CDS             1..375
                     /gene="ADH1B"
                     /gene_synonym="ADH2; HEL-S-117"
                     /coded_by="NM_000668.6:71..1198"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34033.1"
                     /db_xref="GeneID:125"
                     /db_xref="HGNC:HGNC:250"
                     /db_xref="MIM:103720"
ORIGIN      
        1 mstagkvikc kaavlwevkk pfsiedveva ppkayevrik mvavgichtd dhvvsgnlvt
       61 plpvilghea agivesvgeg vttvkpgdkv iplftpqcgk crvcknpesn yclkndlgnp
      121 rgtlqdgtrr ftcrgkpihh flgtstfsqy tvvdenavak idaasplekv cligcgfstg
      181 ygsavnvakv tpgstcavfg lggvglsavm gckaagaari iavdinkdkf akakelgate
      241 cinpqdykkp iqevlkemtd ggvdfsfevi grldtmmasl lccheacgts vivgvppasq
      301 nlsinpmlll tgrtwkgavy ggfkskegip klvadfmakk fsldalithv lpfekinegf
      361 dllhsgksir tvltf
//
LOCUS       NP_001356682             141 aa            linear   PRI 27-APR-2025
DEFINITION  ATP synthase F(0) complex subunit C2, mitochondrial isoform c
            precursor [Homo sapiens].
ACCESSION   NP_001356682
VERSION     NP_001356682.1
DBSOURCE    REFSEQ: accession NM_001369753.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Tebbenkamp,A.T.N., Varela,L., Choi,J., Paredes,M.I., Giani,A.M.,
            Song,J.E., Sestan-Pesa,M., Franjic,D., Sousa,A.M.M., Liu,Z.W.,
            Li,M., Bichsel,C., Koch,M., Szigeti-Buck,K., Liu,F., Li,Z.,
            Kawasawa,Y.I., Paspalas,C.D., Mineur,Y.S., Prontera,P., Merla,G.,
            Picciotto,M.R., Arnsten,A.F.T., Horvath,T.L. and Sestan,N.
  TITLE     The 7q11.23 Protein DNAJC30 Interacts with ATP Synthase and Links
            Mitochondria to Brain Development
  JOURNAL   Cell 175 (4), 1088-1104 (2018)
   PUBMED   30318146
REFERENCE   3  (residues 1 to 141)
  AUTHORS   He,J., Ford,H.C., Carroll,J., Ding,S., Fearnley,I.M. and
            Walker,J.E.
  TITLE     Persistence of the mitochondrial permeability transition in the
            absence of subunit c of human ATP synthase
  JOURNAL   Proc Natl Acad Sci U S A 114 (13), 3409-3414 (2017)
   PUBMED   28289229
  REMARK    GeneRIF: ATP5G1, ATP5G2, and ATP5G3 of the ATP synthase are not
            involved in forming the permeability transition pore.
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Fujikawa,M., Sugawara,K., Tanabe,T. and Yoshida,M.
  TITLE     Assembly of human mitochondrial ATP synthase through two separate
            intermediates, F1-c-ring and b-e-g complex
  JOURNAL   FEBS Lett 589 (19 Pt B), 2707-2712 (2015)
   PUBMED   26297831
REFERENCE   5  (residues 1 to 141)
  AUTHORS   He,M., Xu,M., Zhang,B., Liang,J., Chen,P., Lee,J.Y., Johnson,T.A.,
            Li,H., Yang,X., Dai,J., Liang,L., Gui,L., Qi,Q., Huang,J., Li,Y.,
            Adair,L.S., Aung,T., Cai,Q., Cheng,C.Y., Cho,M.C., Cho,Y.S.,
            Chu,M., Cui,B., Gao,Y.T., Go,M.J., Gu,D., Gu,W., Guo,H., Hao,Y.,
            Hong,J., Hu,Z., Hu,Y., Huang,J., Hwang,J.Y., Ikram,M.K., Jin,G.,
            Kang,D.H., Khor,C.C., Kim,B.J., Kim,H.T., Kubo,M., Lee,J., Lee,J.,
            Lee,N.R., Li,R., Li,J., Liu,J., Longe,J., Lu,W., Lu,X., Miao,X.,
            Okada,Y., Ong,R.T., Qiu,G., Seielstad,M., Sim,X., Song,H.,
            Takeuchi,F., Tanaka,T., Taylor,P.R., Wang,L., Wang,W., Wang,Y.,
            Wu,C., Wu,Y., Xiang,Y.B., Yamamoto,K., Yang,H., Liao,M., Yokota,M.,
            Young,T., Zhang,X., Kato,N., Wang,Q.K., Zheng,W., Hu,F.B., Lin,D.,
            Shen,H., Teo,Y.Y., Mo,Z., Wong,T.Y., Lin,X., Mohlke,K.L., Ning,G.,
            Tsunoda,T., Han,B.G., Shu,X.O., Tai,E.S., Wu,T. and Qi,L.
  TITLE     Meta-analysis of genome-wide association studies of adult height in
            East Asians identifies 17 novel loci
  JOURNAL   Hum Mol Genet 24 (6), 1791-1800 (2015)
   PUBMED   25429064
REFERENCE   6  (residues 1 to 141)
  AUTHORS   Houstek,J., Andersson,U., Tvrdik,P., Nedergaard,J. and Cannon,B.
  TITLE     The expression of subunit c correlates with and thus may limit the
            biosynthesis of the mitochondrial F0F1-ATPase in brown adipose
            tissue
  JOURNAL   J Biol Chem 270 (13), 7689-7694 (1995)
   PUBMED   7706317
REFERENCE   7  (residues 1 to 141)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   8  (residues 1 to 141)
  AUTHORS   Yan,W.L., Lerner,T.J., Haines,J.L. and Gusella,J.F.
  TITLE     Sequence analysis and mapping of a novel human mitochondrial ATP
            synthase subunit 9 cDNA (ATP5G3)
  JOURNAL   Genomics 24 (2), 375-377 (1994)
   PUBMED   7698763
REFERENCE   9  (residues 1 to 141)
  AUTHORS   Dyer,M.R. and Walker,J.E.
  TITLE     Sequences of members of the human gene family for the c subunit of
            mitochondrial ATP synthase
  JOURNAL   Biochem J 293 (Pt 1) (Pt 1), 51-64 (1993)
   PUBMED   8328972
REFERENCE   10 (residues 1 to 141)
  AUTHORS   Farrell,L.B. and Nagley,P.
  TITLE     Human liver cDNA clones encoding proteolipid subunit 9 of the
            mitochondrial ATPase complex
  JOURNAL   Biochem Biophys Res Commun 144 (3), 1257-1264 (1987)
   PUBMED   2883974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073594.31.
            
            Summary: This gene encodes a subunit of mitochondrial ATP synthase.
            Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an
            electrochemical gradient of protons across the inner membrane
            during oxidative phosphorylation. ATP synthase is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, comprising the proton channel.
            The catalytic portion of mitochondrial ATP synthase consists of 5
            different subunits (alpha, beta, gamma, delta, and epsilon)
            assembled with a stoichiometry of 3 alpha, 3 beta, and single
            representatives of the gamma, delta, and epsilon subunits. The
            proton channel likely has nine subunits (a, b, c, d, e, f, g, F6
            and 8). There are three separate genes which encode subunit c of
            the proton channel and they specify precursors with different
            import sequences but identical mature proteins. The protein encoded
            by this gene is one of three precursors of subunit c. This gene has
            multiple pseudogenes. [provided by RefSeq, Jan 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.318977.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..141
                     /product="ATP synthase F(0) complex subunit C2,
                     mitochondrial isoform c precursor"
                     /note="ATP synthase, H+ transporting, mitochondrial F0
                     complex, subunit C2 (subunit 9); ATP synthase
                     lipid-binding protein, mitochondrial; ATP synthase
                     proteolipid P2; ATPase protein 9; ATPase subunit C; ATP
                     synthase c subunit; ATP synthase proton-transporting
                     mitochondrial F(0) complex subunit C2; ATP synthase, H+
                     transporting, mitochondrial Fo complex subunit C2 (subunit
                     9); ATP synthase F(0) complex subunit C2, mitochondrial;
                     dicyclohexylcarbodiimide (DCCD)-reactive proteolipid
                     subunit"
                     /calculated_mol_wt=7608
     transit_peptide 1..66
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q06055.1)"
                     /calculated_mol_wt=7047
     mat_peptide     67..141
                     /product="ATP synthase F(0) complex subunit C2,
                     mitochondrial. /id=PRO_0000002562"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
                     /calculated_mol_wt=7608
     Region          67..141
                     /region_name="ATP9"
                     /note="ATP synthase F0 subunit 9; Provisional; MTH00222"
                     /db_xref="CDD:164765"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
     Site            109
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000269|PubMed:30530489; propagated from
                     UniProtKB/Swiss-Prot (Q06055.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
     Site            124
                     /site_type="other"
                     /note="Reversibly protonated during proton transport.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q06055.1)"
     CDS             1..141
                     /gene="ATP5MC2"
                     /gene_synonym="ATP5A; ATP5G2"
                     /coded_by="NM_001369753.1:161..586"
                     /note="isoform c precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS81694.1"
                     /db_xref="GeneID:517"
                     /db_xref="HGNC:HGNC:842"
                     /db_xref="MIM:603193"
ORIGIN      
        1 mfacskfvst pslvkstsql lsrplsavvl krpeiltdes lsslavscpl tslvssrsfq
       61 tsaisrdidt aakfigagaa tvgvagsgag igtvfgslii gyarnpslkq qlfsyailgf
      121 alseamglfc lmvaflilfa m
//
LOCUS       NP_057517                209 aa            linear   PRI 27-APR-2025
DEFINITION  glycolipid transfer protein [Homo sapiens].
ACCESSION   NP_057517
VERSION     NP_057517.1
DBSOURCE    REFSEQ: accession NM_016433.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Zhang,C., Chen,Z., Zhang,D., Wang,X., Qiu,M. and Tan,Z.
  TITLE     Role of Gltp in Maturation of Oligodendrocytes Under the Regulation
            of Nkx2.2
  JOURNAL   Mol Neurobiol 60 (9), 4897-4908 (2023)
   PUBMED   37191854
  REMARK    GeneRIF: Role of Gltp in Maturation of Oligodendrocytes Under the
            Regulation of Nkx2.2.
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nurmi,H., Backman,A.P.E., Halin,J., Lonnfors,M., Blom,T.,
            Roos-Mattjus,P. and Mattjus,P.
  TITLE     Glycolipid transfer protein knockout disrupts vesicle trafficking
            to the plasma membrane
  JOURNAL   J Biol Chem 299 (4), 104607 (2023)
   PUBMED   36924944
  REMARK    GeneRIF: Glycolipid transfer protein knockout disrupts vesicle
            trafficking to the plasma membrane.
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Mishra,S.K., Gao,Y.G., Zou,X., Stephenson,D.J., Malinina,L.,
            Hinchcliffe,E.H., Chalfant,C.E. and Brown,R.E.
  TITLE     Emerging roles for human glycolipid transfer protein superfamily
            members in the regulation of autophagy, inflammation, and cell
            death
  JOURNAL   Prog Lipid Res 78, 101031 (2020)
   PUBMED   32339554
  REMARK    GeneRIF: Emerging roles for human glycolipid transfer protein
            superfamily members in the regulation of autophagy, inflammation,
            and cell death.
            Review article
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Ochoa-Lizarralde,B., Gao,Y.G., Popov,A.N., Samygina,V.R., Zhai,X.,
            Mishra,S.K., Boldyrev,I.A., Molotkovsky,J.G., Simanshu,D.K.,
            Patel,D.J., Brown,R.E. and Malinina,L.
  TITLE     Structural analyses of 4-phosphate adaptor protein 2 yield
            mechanistic insights into sphingolipid recognition by the
            glycolipid transfer protein family
  JOURNAL   J Biol Chem 293 (43), 16709-16723 (2018)
   PUBMED   30206120
  REMARK    GeneRIF: Four bulky, conserved hydrophobic residues involved in
            'sensor-like' interactions with lipid chains in protein hydrophobic
            pockets and FF motifs in GLTP and FAPP2.
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Rao,C.S., Lin,X., Pike,H.M., Molotkovsky,J.G. and Brown,R.E.
  TITLE     Glycolipid transfer protein mediated transfer of glycosphingolipids
            between membranes: a model for action based on kinetic and
            thermodynamic analyses
  JOURNAL   Biochemistry 43 (43), 13805-13815 (2004)
   PUBMED   15504043
  REMARK    GeneRIF: The rate-limiting step for glycolipid transfer protein
            (GLTP) action appears to be the surface processes leading to the
            GLTP-glycosphingolipid complex formation and release associated
            with a shuttle/carrier mode of action.
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Malinina,L., Malakhova,M.L., Teplov,A., Brown,R.E. and Patel,D.J.
  TITLE     Structural basis for glycosphingolipid transfer specificity
  JOURNAL   Nature 430 (7003), 1048-1053 (2004)
   PUBMED   15329726
  REMARK    GeneRIF: crystal structures of apo-GLTP (1.65 A resolution) and
            lactosylceramide-bound (1.95 A) GLTP, in which the bound
            glycosphingolipid is sandwiched, after adaptive recognition, within
            a previously unknown two-layer all-alpha-helical topology
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Li,X.M., Malakhova,M.L., Lin,X., Pike,H.M., Chung,T.,
            Molotkovsky,J.G. and Brown,R.E.
  TITLE     Human glycolipid transfer protein: probing conformation using
            fluorescence spectroscopy
  JOURNAL   Biochemistry 43 (31), 10285-10294 (2004)
   PUBMED   15287756
  REMARK    GeneRIF: First insights into human GLTP structural dynamics by
            fluorescence spectroscopy, including global conformational changes
            that accompany GLTP folding into an active conformational state.
REFERENCE   9  (residues 1 to 209)
  AUTHORS   Lin,X., Mattjus,P., Pike,H.M., Windebank,A.J. and Brown,R.E.
  TITLE     Cloning and expression of glycolipid transfer protein from bovine
            and porcine brain
  JOURNAL   J Biol Chem 275 (7), 5104-5110 (2000)
   PUBMED   10671554
  REMARK    GeneRIF: This paper describes the first cloning of the cDNAs
            encoding the glycolipid transfer proteins of bovine and porcine
            brain.  The cDNAs are highly homologous to the human cDNA
            (AF209704).
REFERENCE   10 (residues 1 to 209)
  AUTHORS   Abe,A.
  TITLE     Primary structure of glycolipid transfer protein from pig brain
  JOURNAL   J Biol Chem 265 (17), 9634-9637 (1990)
   PUBMED   2190982
  REMARK    GeneRIF: The paper describes the complete primary amino acid
            sequence of glycolipid transfer protein (GLTP) from porcine brain.
            The sequence was determined by Edman degradation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007834.40, BC009932.2,
            AF209704.1, AY372530.1, BQ227117.1 and CA310913.1.
            
            Summary: The protein encoded by this gene is similar to bovine and
            porcine proteins which accelerate transfer of certain
            glycosphingolipids and glyceroglycolipids between membranes. It is
            thought to be a cytoplasmic protein. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.644161.1,
                                           SRR3476690.808760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145893 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000318348.9/ ENSP00000315263.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..209
                     /product="glycolipid transfer protein"
                     /calculated_mol_wt=23719
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P68266; propagated from
                     UniProtKB/Swiss-Prot (Q9NZD2.3)"
     Region          18..163
                     /region_name="GLTP"
                     /note="Glycolipid transfer protein (GLTP); pfam08718"
                     /db_xref="CDD:462575"
     Region          45..66
                     /region_name="2 X 12 AA approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZD2.3)"
     CDS             1..209
                     /gene="GLTP"
                     /coded_by="NM_016433.4:168..797"
                     /db_xref="CCDS:CCDS9136.1"
                     /db_xref="GeneID:51228"
                     /db_xref="HGNC:HGNC:24867"
                     /db_xref="MIM:608949"
ORIGIN      
        1 mallaehllk plpadkqiet gpfleavshl ppffdclgsp vftpikadis gnitkikavy
       61 dtnpakfrtl qnilevekem ygaewpkvga tlalmwlkrg lrfiqvflqs icdgerdenh
      121 pnlirvnatk ayemalkkyh gwivqkifqa alyaapyksd flkalskgqn vteeecleki
      181 rlflvnytat idviyemytq mnaelnykv
//
LOCUS       NP_001355295             291 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 59-like isoform 2 precursor [Mus musculus].
ACCESSION   NP_001355295 XP_011240624
VERSION     NP_001355295.1
DBSOURCE    REFSEQ: accession NM_001368366.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Rutledge,E.A. and McMahon,A.P.
  TITLE     Mutational analysis of genes with ureteric progenitor cell-specific
            expression in branching morphogenesis of the mouse kidney
  JOURNAL   Dev Dyn 249 (6), 765-774 (2020)
   PUBMED   32017326
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Rutledge,E.A., Benazet,J.D. and McMahon,A.P.
  TITLE     Cellular heterogeneity in the ureteric progenitor niche and
            distinct profiles of branching morphogenesis in organ development
  JOURNAL   Development 144 (17), 3177-3188 (2017)
   PUBMED   28705898
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC157774.5.
            
            On Feb 8, 2019 this sequence version replaced XP_011240624.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.1912209.1,
                                           SRR5189670.127539.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164136
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 34.15 cM"
     Protein         1..291
                     /product="transmembrane protein 59-like isoform 2
                     precursor"
                     /note="brain-specific membrane-anchored protein"
                     /calculated_mol_wt=29700
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2076
     Region          36..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNI2.1)"
     Region          72..>235
                     /region_name="BSMAP"
                     /note="Brain specific membrane anchored protein;
                     pfam12280"
                     /db_xref="CDD:463519"
     Site            90
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNI2.1)"
     CDS             1..291
                     /gene="Tmem59l"
                     /gene_synonym="5330410G16Rik"
                     /coded_by="NM_001368366.1:32..907"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:67937"
                     /db_xref="MGI:MGI:1915187"
ORIGIN      
        1 maavalplll llaslvtptp ardpfapqlg dtqrcqqrcr qhhpgsppaq pepegpsesp
       61 nnkailisac ergcrlfsic rfvakssrpn ateteceaac teayvkaaeq racsegcwgq
      121 ipepetqleq kdlaldpprg rlslrylfsm lcsdlmssaq gflssswtys lqtdnrkvvv
      181 fqtqpvaenf afqgshlqrv evtwrrshpk alelhmdpvg pldkvrkakp rvktskakal
      241 raasmgpill slpvhpdhal aellhsghht rpapqvpasn crtaqgplgg v
//
LOCUS       NP_001350307             346 aa            linear   PRI 27-APR-2025
DEFINITION  sugar phosphate exchanger 3 isoform 9 [Homo sapiens].
ACCESSION   NP_001350307 XP_024302743
VERSION     NP_001350307.1
DBSOURCE    REFSEQ: accession NM_001363378.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Yu,Z., Surface,L.E., Park,C.Y., Horlbeck,M.A., Wyant,G.A.,
            Abu-Remaileh,M., Peterson,T.R., Sabatini,D.M., Weissman,J.S. and
            O'Shea,E.K.
  TITLE     Identification of a transporter complex responsible for the
            cytosolic entry of nitrogen-containing bisphosphonates
  JOURNAL   Elife 7, e36620 (2018)
   PUBMED   29745899
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Palmieri,M., Impey,S., Kang,H., di Ronza,A., Pelz,C., Sardiello,M.
            and Ballabio,A.
  TITLE     Characterization of the CLEAR network reveals an integrated control
            of cellular clearance pathways
  JOURNAL   Hum Mol Genet 20 (19), 3852-3866 (2011)
   PUBMED   21752829
  REMARK    GeneRIF: SLC37A3 protein localizes in lysosomes in HeLa cells
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Pan,C.J., Chen,S.Y., Jun,H.S., Lin,S.R., Mansfield,B.C. and
            Chou,J.Y.
  TITLE     SLC37A1 and SLC37A2 are phosphate-linked, glucose-6-phosphate
            antiporters
  JOURNAL   PLoS One 6 (9), e23157 (2011)
   PUBMED   21949678
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Bartoloni,L. and Antonarakis,S.E.
  TITLE     The human sugar-phosphate/phosphate exchanger family SLC37
  JOURNAL   Pflugers Arch 447 (5), 780-783 (2004)
   PUBMED   12811562
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB481623.1, BC046567.1, DA582415.1, AK074823.1 and BM669953.1.
            
            On May 17, 2018 this sequence version replaced XP_024302743.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..346
                     /product="sugar phosphate exchanger 3 isoform 9"
                     /note="sugar phosphate exchanger 3; solute carrier family
                     37 (glycerol-3-phosphate transporter), member 3;
                     sugar-phosphate exchange protein 3"
                     /calculated_mol_wt=38650
     Site            16..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Region          20..328
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            177..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            209..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            266
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NCC5.2)"
     CDS             1..346
                     /gene="SLC37A3"
                     /gene_synonym="SPX3"
                     /coded_by="NM_001363378.1:186..1226"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:84255"
                     /db_xref="HGNC:HGNC:20651"
                     /db_xref="MIM:619137"
ORIGIN      
        1 mawpnvfqrg sllsqfshhh vvvflltffs ysllhasrkt fsnvkvsise qwtpsafnts
       61 velpveiwss nhlfpsaeka tlflgtldti flfsyavglf isgivgdrln lrwvlsfgmc
      121 ssalvvfvfg altewlrfyn kwlycclwiv ngllqstgwp cvvavmgnwf gkagrgvvfg
      181 lwsacasvgn ilgaclassv lqygyeyafl vtasvqfagg iviffgllvs peeiglsgie
      241 aeenfeedsh rplinggene deyepnysiq ddssvaqvka isfyqacclp gvipylvsli
      301 rdklgwmwvf yffilmtsct ivfisplivr eifslvlrrq ahilre
//
LOCUS       NP_003005                346 aa            linear   PRI 27-APR-2025
DEFINITION  secreted frizzled-related protein 4 precursor [Homo sapiens].
ACCESSION   NP_003005
VERSION     NP_003005.2
DBSOURCE    REFSEQ: accession NM_003014.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Qi,B., Wang,H.Y., Ma,X., Chi,Y.F. and Gui,C.
  TITLE     Exploring the predictive values of SERP4 and FRZB in dilated
            cardiomyopathy based on an integrated analysis
  JOURNAL   BMC Cardiovasc Disord 24 (1), 577 (2024)
   PUBMED   39425025
  REMARK    GeneRIF: Exploring the predictive values of SERP4 and FRZB in
            dilated cardiomyopathy based on an integrated analysis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Sanchez-Pozos,K., Granados-Silvestre,M.A., Nieto-Velazquez,N.G.,
            Mejia-Blanquel,M.A., Galicia-Martinez,N., Mandujano-Ceron,J.,
            Jaimes-Santoyo,J. and Ortiz-Lopez,M.G.
  TITLE     Role of secreted frizzled-related protein 4 in prediabetes and type
            2 diabetes: a cross sectional study
  JOURNAL   BMC Endocr Disord 24 (1), 78 (2024)
   PUBMED   38834984
  REMARK    GeneRIF: Role of secreted frizzled-related protein 4 in prediabetes
            and type 2 diabetes: a cross sectional study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Kida,H., Jiang,J.J., Matsui,Y., Takahashi,I., Hasebe,R.,
            Kawamura,D., Endo,T., Shibayama,H., Kondo,M., Nishio,Y.,
            Nishida,K., Matsuno,Y., Oikawa,T., Kubota,S.I., Hojyo,S.,
            Iwasaki,N., Hashimoto,S., Tanaka,Y. and Murakami,M.
  TITLE     Dupuytren's contracture-associated SNPs increase SFRP4 expression
            in non-immune cells including fibroblasts to enhance inflammation
            development
  JOURNAL   Int Immunol 35 (7), 303-312 (2023)
   PUBMED   36719100
  REMARK    GeneRIF: Dupuytren's contracture-associated SNPs increase SFRP4
            expression in non-immune cells including fibroblasts to enhance
            inflammation development.
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Guo,L., Chen,H., Chen,J., Gao,C., Fu,X., Zhou,S., Wu,W., Li,T.,
            Lin,J., Yang,T., Chen,Z. and Cao,L.
  TITLE     PBX1-promoted SFRP4 transcription inhibits cell proliferation and
            epithelial-mesenchymal transition in endometrial carcinoma
  JOURNAL   Tissue Cell 82, 102083 (2023)
   PUBMED   37054536
  REMARK    GeneRIF: PBX1-promoted SFRP4 transcription inhibits cell
            proliferation and epithelial-mesenchymal transition in endometrial
            carcinoma.
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Takaya,K., Asou,T. and Kishi,K.
  TITLE     Downregulation of senescence-associated secretory phenotype by
            knockdown of secreted frizzled-related protein 4 contributes to the
            prevention of skin aging
  JOURNAL   Aging (Albany NY) 14 (20), 8167-8178 (2022)
   PUBMED   36084952
  REMARK    GeneRIF: Downregulation of senescence-associated secretory
            phenotype by knockdown of secreted frizzled-related protein 4
            contributes to the prevention of skin aging.
REFERENCE   6  (residues 1 to 346)
  AUTHORS   James,I.E., Kumar,S., Barnes,M.R., Gress,C.J., Hand,A.T.,
            Dodds,R.A., Connor,J.R., Bradley,B.R., Campbell,D.A., Grabill,S.E.,
            Williams,K., Blake,S.M., Gowen,M. and Lark,M.W.
  TITLE     FrzB-2: a human secreted frizzled-related protein with a potential
            role in chondrocyte apoptosis
  JOURNAL   Osteoarthritis Cartilage 8 (6), 452-463 (2000)
   PUBMED   11069730
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Schumann,H., Holtz,J., Zerkowski,H.R. and Hatzfeld,M.
  TITLE     Expression of secreted frizzled related proteins 3 and 4 in human
            ventricular myocardium correlates with apoptosis related gene
            expression
  JOURNAL   Cardiovasc Res 45 (3), 720-728 (2000)
   PUBMED   10728394
REFERENCE   8  (residues 1 to 346)
  AUTHORS   Abu-Jawdeh,G., Comella,N., Tomita,Y., Brown,L.F., Tognazzi,K.,
            Sokol,S.Y. and Kocher,O.
  TITLE     Differential expression of frpHE: a novel human stromal protein of
            the secreted frizzled gene family, during the endometrial cycle and
            malignancy
  JOURNAL   Lab Invest 79 (4), 439-447 (1999)
   PUBMED   10211996
REFERENCE   9  (residues 1 to 346)
  AUTHORS   Wolf,V., Ke,G., Dharmarajan,A.M., Bielke,W., Artuso,L., Saurer,S.
            and Friis,R.
  TITLE     DDC-4, an apoptosis-associated gene, is a secreted frizzled
            relative
  JOURNAL   FEBS Lett 417 (3), 385-389 (1997)
   PUBMED   9409757
REFERENCE   10 (residues 1 to 346)
  AUTHORS   Rattner,A., Hsieh,J.C., Smallwood,P.M., Gilbert,D.J.,
            Copeland,N.G., Jenkins,N.A. and Nathans,J.
  TITLE     A family of secreted proteins contains homology to the
            cysteine-rich ligand-binding domain of frizzled receptors
  JOURNAL   Proc Natl Acad Sci U S A 94 (7), 2859-2863 (1997)
   PUBMED   9096311
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018634.3 and BT019679.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 26, 2008 this sequence version replaced NP_003005.1.
            
            Summary: Secreted frizzled-related protein 4 (SFRP4) is a member of
            the SFRP family that contains a cysteine-rich domain homologous to
            the putative Wnt-binding site of Frizzled proteins. SFRPs act as
            soluble modulators of Wnt signaling. The expression of SFRP4 in
            ventricular myocardium correlates with apoptosis related gene
            expression. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.46119.1,
                                           SRR1803614.178948.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            MANE Ensembl match               :: ENST00000436072.7/
                                                ENSP00000410715.2
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.1"
     Protein         1..346
                     /product="secreted frizzled-related protein 4 precursor"
                     /note="frizzled protein, human endometrium; secreted
                     frizzled-related protein 4; secreted frizzled-related
                     protein 4"
                     /calculated_mol_wt=37519
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2326
     Region          20..146
                     /region_name="CRD_FZ"
                     /note="CRD_domain cysteine-rich domain, also known as Fz
                     (frizzled) domain; cl02447"
                     /db_xref="CDD:470581"
     Site            order(31,33..34,37..39)
                     /site_type="other"
                     /note="putative Wnt binding site [polypeptide binding]"
                     /db_xref="CDD:143551"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6FHJ7.2)"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6FHJ7.2)"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6FHJ7.2)"
     Region          188..296
                     /region_name="NTR_like"
                     /note="NTR_like domain; a beta barrel with an
                     oligosaccharide/oligonucleotide-binding fold found in
                     netrins, complement proteins, tissue inhibitors of
                     metalloproteases (TIMP), and procollagen C-proteinase
                     enhancers (PCOLCE), amongst others. In netrins, the...;
                     cl02512"
                     /db_xref="CDD:470599"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6FHJ7.2)"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6FHJ7.2)"
     Region          292..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6FHJ7.2)"
     CDS             1..346
                     /gene="SFRP4"
                     /gene_synonym="FRP-4; FRPHE; FRZB-2; PYL; sFRP-4"
                     /coded_by="NM_003014.4:281..1321"
                     /db_xref="CCDS:CCDS5453.1"
                     /db_xref="GeneID:6424"
                     /db_xref="HGNC:HGNC:10778"
                     /db_xref="MIM:606570"
ORIGIN      
        1 mflsilvalc lwlhlalgvr gapceavrip mcrhmpwnit rmpnhlhhst qenailaieq
       61 yeelvdvncs avlrfflcam yapictlefl hdpikpcksv cqrarddcep lmkmynhswp
      121 eslacdelpv ydrgvcispe aivtdlpedv kwiditpdmm vqerpldvdc krlspdrckc
      181 kkvkptlaty lsknysyvih akikavqrsg cnevttvvdv keifkssspi prtqvplitn
      241 sscqcphilp hqdvlimcye wrsrmmllen clvekwrdql skrsiqweer lqeqrrtvqd
      301 kkktagrtsr snppkpkgkp papkpaspkk niktrsaqkr tnpkrv
//
LOCUS       NP_001095231             463 aa            linear   VRT 27-APR-2025
DEFINITION  elongation factor 1-alpha [Xenopus laevis].
ACCESSION   NP_001095231 NP_001095232
VERSION     NP_001095231.2
DBSOURCE    REFSEQ: accession NM_001101761.2
KEYWORDS    RefSeq.
SOURCE      Xenopus laevis (African clawed frog)
  ORGANISM  Xenopus laevis
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae;
            Xenopus; Xenopus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Loeber,J., Claussen,M., Jahn,O. and Pieler,T.
  TITLE     Interaction of 42Sp50 with the vegetal RNA localization machinery
            in Xenopus laevis oocytes
  JOURNAL   FEBS J 277 (22), 4722-4731 (2010)
   PUBMED   20977669
  REMARK    GeneRIF: Data provide evidence for a novel function of 42Sp50 in
            the context of vegetal mRNA transport in Xenopus oocytes.
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Klein,S.L., Strausberg,R.L., Wagner,L., Pontius,J., Clifton,S.W.
            and Richardson,P.
  TITLE     Genetic and genomic tools for Xenopus research: The NIH Xenopus
            initiative
  JOURNAL   Dev Dyn 225 (4), 384-391 (2002)
   PUBMED   12454917
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Zorn,A.M. and Krieg,P.A.
  TITLE     The KH domain protein encoded by quaking functions as a dimer and
            is essential for notochord development in Xenopus embryos
  JOURNAL   Genes Dev 11 (17), 2176-2190 (1997)
   PUBMED   9303534
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Cheng,F.M., Darby,M.K. and Joho,K.E.
  TITLE     Correction of the nucleotide and amino acid sequence of Xenopus
            laevis 42Sp50
  JOURNAL   Nucleic Acids Res 21 (9), 2259 (1993)
   PUBMED   8502575
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Deschamps,S., Morales,J., Mazabraud,A., le Maire,M., Denis,H. and
            Brown,D.D.
  TITLE     Two forms of elongation factor 1 alpha (EF-1 alpha O and 42Sp50),
            present in oocytes, but absent in somatic cells of Xenopus laevis
  JOURNAL   J Cell Biol 114 (6), 1109-1111 (1991)
   PUBMED   1894690
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Viel,A., le Maire,M., Philippe,H., Morales,J., Mazabraud,A. and
            Denis,H.
  TITLE     Structural and functional properties of thesaurin a (42Sp50), the
            major protein of the 42 S particles present in Xenopus laevis
            previtellogenic oocytes
  JOURNAL   J Biol Chem 266 (16), 10392-10399 (1991)
   PUBMED   2037589
REFERENCE   7  (residues 1 to 463)
  AUTHORS   Dje,M.K., Mazabraud,A., Viel,A., le Maire,M., Denis,H., Crawford,E.
            and Brown,D.D.
  TITLE     Three genes under different developmental control encode elongation
            factor 1-alpha in Xenopus laevis
  JOURNAL   Nucleic Acids Res 18 (12), 3489-3493 (1990)
   PUBMED   2362804
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC133768.1.
            
            On Jan 10, 2019 this sequence version replaced NP_001095231.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC133768.1, Z19545.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04111048, SAMN04111052
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Xenopus laevis"
                     /db_xref="taxon:8355"
                     /chromosome="6L"
                     /map="6L"
     Protein         1..463
                     /product="elongation factor 1-alpha"
                     /note="EF-1-alpha; thesaurin A"
                     /calculated_mol_wt=50489
     Region          7..458
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          17..24
                     /region_name="G1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P17506.2)"
     Site            17..24
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206670"
     Site            order(18,20,24..25,28,31..32,79..80,98..99,122..123,172,
                     176)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206670"
     Site            order(20,22..25,156..157,159,197..199)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206670"
     Site            order(24,67,70..71,73,75,77..79,81,92,94,96..98,100,103)
                     /site_type="other"
                     /note="EF1Balpha binding site [polypeptide binding]"
                     /db_xref="CDD:206670"
     Site            69..79
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206670"
     Region          73..77
                     /region_name="G2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P17506.2)"
     Site            75
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206670"
     Region          94..97
                     /region_name="G3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P17506.2)"
     Site            94..97
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206670"
     Site            96..114
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206670"
     Region          156..159
                     /region_name="G4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P17506.2)"
     Site            156..159
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206670"
     Region          197..199
                     /region_name="G5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P17506.2)"
     Site            197..199
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206670"
     CDS             1..463
                     /gene="42sp50.L"
                     /gene_synonym="42sp50; Thesaurin-A"
                     /coded_by="NM_001101761.2:43..1434"
                     /db_xref="GeneID:397889"
                     /db_xref="Xenbase:XB-GENE-5853356"
ORIGIN      
        1 mtgkapqkth lniviighvd sgkstttghl iykcggfdpr alekveaaaa qlgkssfkfa
       61 wildklkaer ergitidisl wkfqtnrfti tiidapghrd fiknmitgts qadvallvvs
      121 aatgefeagv srngqtreha llaytmgvkq livcvnkmdl tdppyshkrf devvrnvmvy
      181 lkkigynpat ipfvpvsgwt genisspsqk mgwfkgwkvk rkdgftkgqs llevldalvp
      241 pvrpankplr lplqdvykig gigtvpvgki etgilkpgmt isfapsgfsa evksiemhhe
      301 plqmafpgfn igfnvkniav kslkrgnvag nsksdpptea ssftaqviil nhpgfikagy
      361 spvidchtah itcqfaelqe kidrrtgkkl ednpgllksg daaiitlkpi kpfcverffd
      421 ypplgrfaar dlkqtvavgv vksvehkaga aarrqvqkpv lvk
//
LOCUS       NP_006030               1479 aa            linear   PRI 27-APR-2025
DEFINITION  C-type mannose receptor 2 precursor [Homo sapiens].
ACCESSION   NP_006030
VERSION     NP_006030.2
DBSOURCE    REFSEQ: accession NM_006039.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1479)
  AUTHORS   Cakilkaya,P., Sorensen,R.R., Jurgensen,H.J., Krigslund,O.,
            Gardsvoll,H., Nielsen,C.F., Santoni-Rugiu,E., Behrendt,N. and
            Engelholm,L.H.
  TITLE     The Collagen Receptor uPARAP in Malignant Mesothelioma: A Potential
            Diagnostic Marker and Therapeutic Target
  JOURNAL   Int J Mol Sci 22 (21), 11452 (2021)
   PUBMED   34768883
  REMARK    GeneRIF: The Collagen Receptor uPARAP in Malignant Mesothelioma: A
            Potential Diagnostic Marker and Therapeutic Target.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1479)
  AUTHORS   Li,L., Chen,X., Zhang,H., Wang,M. and Lu,W.
  TITLE     MRC2 Promotes Proliferation and Inhibits Apoptosis of Diabetic
            Nephropathy
  JOURNAL   Anal Cell Pathol (Amst) 2021, 6619870 (2021)
   PUBMED   34012764
  REMARK    GeneRIF: MRC2 Promotes Proliferation and Inhibits Apoptosis of
            Diabetic Nephropathy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1479)
  AUTHORS   Ji,B., Chen,J., Zhen,C., Yang,Q. and Yu,N.
  TITLE     Mathematical modelling of the role of Endo180 network in the
            development of metastatic bone disease in prostate cancer
  JOURNAL   Comput Biol Med 117, 103619 (2020)
   PUBMED   32072971
  REMARK    GeneRIF: Mathematical modelling of the role of Endo180 network in
            the development of metastatic bone disease in prostate cancer.
REFERENCE   4  (residues 1 to 1479)
  AUTHORS   Iwahashi,H., Kawashima,Y. and Masaki,H.
  TITLE     Interleukin-1 alpha derived from ultraviolet B-exposed
            keratinocytes is associated with a decrease of endocytic collagen
            receptor Endo180
  JOURNAL   Photodermatol Photoimmunol Photomed 36 (1), 34-41 (2020)
   PUBMED   31376337
  REMARK    GeneRIF: These results indicate that a substance secreted from
            UVB-exposed keratinocytes regulates Endo180 expression and that
            IL-1alpha may play an important role in the maintenance of Endo180.
REFERENCE   5  (residues 1 to 1479)
  AUTHORS   Caldwell,R.L., Egan,B.S. and Shepherd,V.L.
  TITLE     HIV-1 Tat represses transcription from the mannose receptor
            promoter
  JOURNAL   J Immunol 165 (12), 7035-7041 (2000)
   PUBMED   11120831
REFERENCE   6  (residues 1 to 1479)
  AUTHORS   Sheikh,H., Yarwood,H., Ashworth,A. and Isacke,C.M.
  TITLE     Endo180, an endocytic recycling glycoprotein related to the
            macrophage mannose receptor is expressed on fibroblasts,
            endothelial cells and macrophages and functions as a lectin
            receptor
  JOURNAL   J Cell Sci 113 (Pt 6), 1021-1032 (2000)
   PUBMED   10683150
REFERENCE   7  (residues 1 to 1479)
  AUTHORS   Behrendt,N., Jensen,O.N., Engelholm,L.H., Mortz,E., Mann,M. and
            Dano,K.
  TITLE     A urokinase receptor-associated protein with specific collagen
            binding properties
  JOURNAL   J Biol Chem 275 (3), 1993-2002 (2000)
   PUBMED   10636902
REFERENCE   8  (residues 1 to 1479)
  AUTHORS   Tajima,Y., Tashiro,K. and Camerini,D.
  TITLE     Cloning of human chromosome 17-specific cDNAs using
            representational difference analysis and human-mouse hybrid cells
  JOURNAL   Genomics 42 (2), 353-355 (1997)
   PUBMED   9192860
REFERENCE   9  (residues 1 to 1479)
  AUTHORS   Wu,K., Yuan,J. and Lasky,L.A.
  TITLE     Characterization of a novel member of the macrophage mannose
            receptor type C lectin family
  JOURNAL   J Biol Chem 271 (35), 21323-21330 (1996)
   PUBMED   8702911
REFERENCE   10 (residues 1 to 1479)
  AUTHORS   Behrendt,N., Ronne,E. and Dano,K.
  TITLE     A novel, specific pro-urokinase complex on monocyte-like cells,
            detected by transglutaminase-catalyzed cross-linking
  JOURNAL   FEBS Lett 336 (3), 394-396 (1993)
   PUBMED   7904248
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC153884.1, BC146647.1,
            BC032763.1 and AI458446.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 22, 2006 this sequence version replaced NP_006030.1.
            
            Summary: This gene encodes a member of the mannose receptor family
            of proteins that contain a fibronectin type II domain and multiple
            C-type lectin-like domains. The encoded protein plays a role in
            extracellular matrix remodeling by mediating the internalization
            and lysosomal degradation of collagen ligands. Expression of this
            gene may play a role in the tumorigenesis and metastasis of several
            malignancies including breast cancer, gliomas and metastatic bone
            disease. [provided by RefSeq, Feb 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150212.1, BC146647.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303375.10/ ENSP00000307513.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.2"
     Protein         1..1479
                     /product="C-type mannose receptor 2 precursor"
                     /note="endocytic receptor (macrophage mannose receptor
                     family); endocytic receptor 180; UPAR-associated protein;
                     macrophage mannose receptor 2; C-type lectin domain family
                     13 member E; urokinase-type plasminogen activator
                     receptor-associated protein"
                     /calculated_mol_wt=163408
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3285
     mat_peptide     31..1479
                     /product="C-type mannose receptor 2. /id=PRO_0000046078"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBG0.2)"
                     /calculated_mol_wt=163408
     Region          42..165
                     /region_name="beta-trefoil_Ricin_MRC2"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in macrophage mannose receptor 2 (MRC2) and similar
                     proteins; cd23408"
                     /db_xref="CDD:467786"
     Site            order(56..58,63,65,74..75)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467786"
     Site            order(69,72)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467786"
     Site            69
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9UBG0.2)"
     Site            order(95..96,108,110,118..119)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467786"
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBG0.2)"
     Region          180..228
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(191,193,198,212,219,225,227)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          247..361
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cd00037"
                     /db_xref="CDD:153057"
     Site            order(333,337,339,345,347..350,353..355)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBG0.2)"
     Region          382..505
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            order(439,470,472,479,485..486,492..495)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(446,450,473,479..480)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(450,480)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Region          521..644
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            588
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBG0.2)"
     Site            order(617,620,622,629,631..634,637,639..640)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          669..809
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            order(783,787,789,794,796..799,802..804)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          829..951
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            order(925,929,931,938..941,944..946)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            954
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBG0.2)"
     Region          972..1108
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            1029
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBG0.2)"
     Site            order(1076,1080,1082,1092,1094..1097,1101..1103)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          1137..1245
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cd00037"
                     /db_xref="CDD:153057"
     Site            order(1218,1222,1224,1228,1230..1233,1236..1238)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          1261..1394
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            1350
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBG0.2)"
     Site            order(1367,1371,1373,1378,1380..1383,1386,1388..1389)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            1415..1435
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBG0.2)"
     Region          1450..1479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBG0.2)"
     CDS             1..1479
                     /gene="MRC2"
                     /gene_synonym="CD280; CLEC13E; ENDO180; UPARAP"
                     /coded_by="NM_006039.5:134..4573"
                     /db_xref="CCDS:CCDS11634.1"
                     /db_xref="GeneID:9902"
                     /db_xref="HGNC:HGNC:16875"
                     /db_xref="MIM:612264"
ORIGIN      
        1 mgpgrpapap wprhllrcvl llgclhlgrp gapgdaalpe pnvflifshg lqgcleaqgg
       61 qvrvtpacnt slpaqrwkwv srnrlfnlgt mqclgtgwpg tnttaslgmy ecdrealnlr
      121 whcrtlgdql slllgartsn iskpgtlerg dqtrsgqwri ygseedlcal pyhevytiqg
      181 nshgkpctip fkydnqwfhg ctstgredgh lwcattqdyg kderwgfcpi ksndcetfwd
      241 kdqltdscyq fnfqstlswr eawasceqqg adllsiteih eqtyingllt gysstlwigl
      301 ndldtsggwq wsdnsplkyl nwesdqpdnp seencgvirt essggwqnrd csialpyvck
      361 kkpnataept ppdrwanvkv ecepswqpfq ghcyrlqaek rswqeskkac lrgggdlvsi
      421 hsmaelefit kqikqeveel wiglndlklq mnfewsdgsl vsfthwhpfe pnnfrdsled
      481 cvtiwgpegr wndspcnqsl psickkagql sqgaaeedhg crkgwtwhsp scywlgedqv
      541 tysearrlct dhgsqlvtit nrfeqafvss liynwegeyf wtalqdlnst gsffwlsgde
      601 vmythwnrdq pgysrggcva latgsamglw evknctsfra ryicrqslgt pvtpelpgpd
      661 ptpsltgscp qgwasdtklr ycykvfsser lqdkkswvqa qgacqelgaq llslasyeee
      721 hfvanmlnki fgesepeihe qhwfwiglnr rdprggqswr wsdgvgfsyh nfdrsrhddd
      781 dirgcavldl aslqwvamqc dtqldwicki prgtdvrepd dspqgrrewl rfqeaeykff
      841 ehhstwaqaq rictwfqael tsvhsqaeld flshnlqkfs raqeqhwwig lhtsesdgrf
      901 rwtdgsiinf iswapgkprp vgkdkkcvym tasredwgdq rcltalpyic krsnvtketq
      961 ppdlpttalg gcpsdwiqfl nkcfqvqgqe pqsrvkwsea qfsceqqeaq lvtitnpleq
     1021 afitaslpnv tfdlwiglha sqrdfqwveq eplmyanwap gepsgpspap sgnkptscav
     1081 vlhspsahft grwddrscte ethgficqkg tdpslspspa alppapgtel sylngtfrll
     1141 qkplrwhdal llcesrnasl ayvpdpytqa fltqaarglr tplwiglage egsrryswvs
     1201 eeplnyvgwq dgepqqpggc tyvdvdgawr ttscdtklqg avcgvssgpp pprrisyhgs
     1261 cpqgladsaw ipfrehcysf hmelllghke arqrcqragg avlsildeme nvfvwehlqs
     1321 yegqsrgawl gmnfnpkggt lvwqdntavn ysnwgppglg psmlshnscy wiqsnsglwr
     1381 pgactnitmg vvcklpraeq ssfspsalpe npaalvvvlm avllllallt aalilyrrrq
     1441 siergafega rysrsssspt eateknilvs dmemneqqe
//
LOCUS       NP_003001                399 aa            linear   PRI 27-APR-2025
DEFINITION  dual specificity mitogen-activated protein kinase kinase 4 isoform
            1 [Homo sapiens].
ACCESSION   NP_003001
VERSION     NP_003001.1
DBSOURCE    REFSEQ: accession NM_003010.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Pan,C., Su,Z., Xie,H., Ning,Y., Li,S. and Xiao,H.
  TITLE     Hsa_circ_0081069 facilitates tongue squamous cell carcinoma
            progression by modulating MAP2K4 expression via miR-634
  JOURNAL   Odontology 111 (2), 474-486 (2023)
   PUBMED   36181561
  REMARK    GeneRIF: Hsa_circ_0081069 facilitates tongue squamous cell
            carcinoma progression by modulating MAP2K4 expression via miR-634.
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Wang,B., Yang,S., Jia,Y., Yang,J., Du,K., Luo,Y., Li,Y., Wang,Z.,
            Liu,Y. and Zhu,B.
  TITLE     PCAT19 Regulates the Proliferation and Apoptosis of Lung Cancer
            Cells by Inhibiting miR-25-3p via Targeting the MAP2K4 Signal Axis
  JOURNAL   Dis Markers 2022, 2442094 (2022)
   PUBMED   35615401
  REMARK    GeneRIF: PCAT19 Regulates the Proliferation and Apoptosis of Lung
            Cancer Cells by Inhibiting miR-25-3p via Targeting the MAP2K4
            Signal Axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Kragelj,J., Orand,T., Delaforge,E., Tengo,L., Blackledge,M.,
            Palencia,A. and Jensen,M.R.
  TITLE     Enthalpy-Entropy Compensation in the Promiscuous Interaction of an
            Intrinsically Disordered Protein with Homologous Protein Partners
  JOURNAL   Biomolecules 11 (8), 1204 (2021)
   PUBMED   34439869
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Liu,X.D., Zhang,Z.W., Wu,H.W. and Liang,Z.Y.
  TITLE     A new prognosis prediction model combining TNM stage with MAP2K4
            and JNK in postoperative pancreatic cancer patients
  JOURNAL   Pathol Res Pract 217, 153313 (2021)
   PUBMED   33341545
  REMARK    GeneRIF: A new prognosis prediction model combining TNM stage with
            MAP2K4 and JNK in postoperative pancreatic cancer patients.
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Salmeron,A., Ahmad,T.B., Carlile,G.W., Pappin,D., Narsimhan,R.P.
            and Ley,S.C.
  TITLE     Activation of MEK-1 and SEK-1 by Tpl-2 proto-oncoprotein, a novel
            MAP kinase kinase kinase
  JOURNAL   EMBO J 15 (4), 817-826 (1996)
   PUBMED   8631303
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Lin,A., Minden,A., Martinetto,H., Claret,F.X., Lange-Carter,C.,
            Mercurio,F., Johnson,G.L. and Karin,M.
  TITLE     Identification of a dual specificity kinase that activates the Jun
            kinases and p38-Mpk2
  JOURNAL   Science 268 (5208), 286-290 (1995)
   PUBMED   7716521
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Derijard,B., Raingeaud,J., Barrett,T., Wu,I.H., Han,J.,
            Ulevitch,R.J. and Davis,R.J.
  TITLE     Independent human MAP-kinase signal transduction pathways defined
            by MEK and MKK isoforms
  JOURNAL   Science 267 (5198), 682-685 (1995)
   PUBMED   7839144
  REMARK    Erratum:[Science 1995 Jul 7;269(5220):17]
REFERENCE   10 (residues 1 to 399)
  AUTHORS   Yan,M., Dai,T., Deak,J.C., Kyriakis,J.M., Zon,L.I., Woodgett,J.R.
            and Templeton,D.J.
  TITLE     Activation of stress-activated protein kinase by MEKK1
            phosphorylation of its activator SEK1
  JOURNAL   Nature 372 (6508), 798-800 (1994)
   PUBMED   7997270
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC036032.1, L36870.1,
            BQ028457.1 and AU150695.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the mitogen-activated
            protein kinase (MAPK) family. Members of this family act as an
            integration point for multiple biochemical signals and are involved
            in a wide variety of cellular processes such as proliferation,
            differentiation, transcription regulation, and development. They
            form a three-tiered signaling module composed of MAPKKKs, MAPKKs,
            and MAPKs. This protein is phosphorylated at serine and threonine
            residues by MAPKKKs and subsequently phosphorylates downstream MAPK
            targets at threonine and tyrosine residues. A similar protein in
            mouse has been reported to play a role in liver organogenesis. A
            pseudogene of this gene is located on the long arm of chromosome X.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.39130.1, BC060764.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000353533.10/ ENSP00000262445.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..399
                     /product="dual specificity mitogen-activated protein
                     kinase kinase 4 isoform 1"
                     /EC_number="2.7.12.2"
                     /note="dual specificity mitogen-activated protein kinase
                     kinase 4; MAP kinase kinase 4; c-Jun N-terminal kinase
                     kinase 1; SAPK/ERK kinase 1; MAPK/ERK kinase 4;
                     JNK-activated kinase 1; MEK 4; MAPKK 4; JNK-activating
                     kinase 1; stress-activated protein kinase kinase 1; c-Jun
                     NH2-terminal kinase kinase 1"
                     /calculated_mol_wt=44157
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45985.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P45985.1)"
     Region          37..52
                     /region_name="D domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P45985.1)"
     Site            45..46
                     /site_type="cleavage"
                     /note="Cleavage, by anthrax lethal factor; propagated from
                     UniProtKB/Swiss-Prot (P45985.1)"
     Site            58..59
                     /site_type="cleavage"
                     /note="Cleavage, by anthrax lethal factor; propagated from
                     UniProtKB/Swiss-Prot (P45985.1)"
     Site            58
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P45985.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P45985.1)"
     Region          95..385
                     /region_name="PKc_MKK4"
                     /note="Catalytic domain of the dual-specificity Protein
                     Kinase, Mitogen-activated protein Kinase Kinase 4;
                     cd06616"
                     /db_xref="CDD:270790"
     Site            order(95..99,121,126,128,146,165,167..169,177)
                     /site_type="other"
                     /note="allosteric peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270790"
     Site            order(108..112,116,129,131,162,178..181,183..184,187,229,
                     231..234,236,246..247,250,263..266,268,299,308)
                     /site_type="active"
                     /db_xref="CDD:270790"
     Site            order(108..112,114,116,129,131,162,178..181,183..184,
                     186..187,231,233..234,236,247)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270790"
     Site            order(111..112,229,231..233,250,263..266,268,299,308)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270790"
     Site            246..268
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270790"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P45985.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAP3K.
                     /evidence=ECO:0000269|PubMed:9003778; propagated from
                     UniProtKB/Swiss-Prot (P45985.1)"
     Region          364..387
                     /region_name="DVD domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P45985.1)"
     CDS             1..399
                     /gene="MAP2K4"
                     /gene_synonym="JNKK; JNKK1; MAPKK4; MEK4; MKK4; PRKMK4;
                     SAPKK-1; SAPKK1; SEK1; SERK1; SKK1"
                     /coded_by="NM_003010.4:11..1210"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11162.1"
                     /db_xref="GeneID:6416"
                     /db_xref="HGNC:HGNC:6844"
                     /db_xref="MIM:601335"
ORIGIN      
        1 maapspsggg gsgggsgsgt pgpvgspapg hpavssmqgk rkalklnfan ppfkstarft
       61 lnpnptgvqn phierlrths iessgklkis peqhwdftae dlkdlgeigr gaygsvnkmv
      121 hkpsgqimav krirstvdek eqkqllmdld vvmrssdcpy ivqfygalfr egdcwicmel
      181 mstsfdkfyk yvysvlddvi peeilgkitl atvkalnhlk enlkiihrdi kpsnilldrs
      241 gniklcdfgi sgqlvdsiak trdagcrpym aperidpsas rqgydvrsdv wslgitlyel
      301 atgrfpypkw nsvfdqltqv vkgdppqlsn seerefspsf infvnlcltk deskrpkyke
      361 llkhpfilmy eeravevacy vckildqmpa tpsspmyvd
//
LOCUS       NP_062550                393 aa            linear   PRI 27-APR-2025
DEFINITION  cytotoxic and regulatory T-cell molecule isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_062550
VERSION     NP_062550.2
DBSOURCE    REFSEQ: accession NM_019604.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Zheng,S., Yang,B., Li,L., Chen,M., Zhang,L., Chi,W., Shao,Z.M.,
            Xiu,B., Chi,Y. and Wu,J.
  TITLE     CRTAM promotes antitumor immune response in triple negative breast
            cancer by enhancing CD8+ T cell infiltration
  JOURNAL   Int Immunopharmacol 129, 111625 (2024)
   PUBMED   38354509
  REMARK    GeneRIF: CRTAM promotes antitumor immune response in triple
            negative breast cancer by enhancing CD8+ T cell infiltration.
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Barragan-Galvez,J.C., Gonzalez-Orozco,M., Hernandez-Flores,A.,
            Maravillas-Montero,J.L., Chavez-Guerrero,Y. and Ortiz-Navarrete,V.
  TITLE     Prokaryotic Expression of the Immunoglobulin's Domains of CRTAM to
            Characterize a Monoclonal Antibody
  JOURNAL   Protein J 39 (3), 224-231 (2020)
   PUBMED   32300914
  REMARK    GeneRIF: Prokaryotic Expression of the Immunoglobulin's Domains of
            CRTAM to Characterize a Monoclonal Antibody.
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Ramirez-Ramirez,D., Padilla-Castaneda,S., Galan-Enriquez,C.S.,
            Vadillo,E., Prieto-Chavez,J.L., Jimenez-Hernandez,E.,
            Vilchis-Ordonez,A., Sandoval,A., Balandran,J.C., Perez-Tapia,S.M.,
            Ortiz-Navarrete,V. and Pelayo,R.
  TITLE     CRTAM+ NK cells endowed with suppressor properties arise in
            leukemic bone marrow
  JOURNAL   J Leukoc Biol 105 (5), 999-1013 (2019)
   PUBMED   30791148
  REMARK    GeneRIF: The findings suggest, for the first time, that the tumor
            microenvironment in acute lymphoblastic leukemia directly
            contribute to exhaustion of NK cell functions by the CRTAM/Necl-2
            interaction, and that the potential regulatory role of
            exhausted-like NK cells may favor malignant progression at the
            expense of anti-tumor responses.
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Takeuchi,A., Badr Mel,S., Miyauchi,K., Ishihara,C., Onishi,R.,
            Guo,Z., Sasaki,Y., Ike,H., Takumi,A., Tsuji,N.M., Murakami,Y.,
            Katakai,T., Kubo,M. and Saito,T.
  TITLE     CRTAM determines the CD4+ cytotoxic T lymphocyte lineage
  JOURNAL   J Exp Med 213 (1), 123-138 (2016)
   PUBMED   26694968
  REMARK    GeneRIF: These results reveal that CRTAM is critical to instruct
            the differentiation of CD4(+)CTL through the induction of Eomes and
            CTL-related gene.
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Rojas-Marquez,C., Valle-Rios,R., Lopez-Bayghen,E. and
            Ortiz-Navarrete,V.
  TITLE     CRTAM is negatively regulated by ZEB1 in T cells
  JOURNAL   Mol Immunol 66 (2), 290-298 (2015)
   PUBMED   25910959
  REMARK    GeneRIF: CRTAM is negatively regulated by ZEB1 in T cells.
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Yeh,J.H., Sidhu,S.S. and Chan,A.C.
  TITLE     Regulation of a late phase of T cell polarity and effector
            functions by Crtam
  JOURNAL   Cell 132 (5), 846-859 (2008)
   PUBMED   18329370
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Patino-Lopez,G., Hevezi,P., Lee,J., Willhite,D., Verge,G.M.,
            Lechner,S.M., Ortiz-Navarrete,V. and Zlotnik,A.
  TITLE     Human class-I restricted T cell associated molecule is highly
            expressed in the cerebellum and is a marker for activated NKT and
            CD8+ T lymphocytes
  JOURNAL   J Neuroimmunol 171 (1-2), 145-155 (2006)
   PUBMED   16300832
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Boles,K.S., Barchet,W., Diacovo,T., Cella,M. and Colonna,M.
  TITLE     The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell
            responses through the cell-surface receptor CRTAM
  JOURNAL   Blood 106 (3), 779-786 (2005)
   PUBMED   15811952
  REMARK    GeneRIF: NK cells and T8 cells recognize Necl-2 through CRTAM,
            expressed only on activated cells. CRTAM-Necl-2 interactions
            promote cytotoxicity of NK cells and IFN-gamma secretion of T8
            cells as well as NK cell-mediated rejection of tumors expressing
            Necl-2
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Galibert,L., Diemer,G.S., Liu,Z., Johnson,R.S., Smith,J.L.,
            Walzer,T., Comeau,M.R., Rauch,C.T., Wolfson,M.F., Sorensen,R.A.,
            Van der Vuurst de Vries,A.R., Branstetter,D.G., Koelling,R.M.,
            Scholler,J., Fanslow,W.C., Baum,P.R., Derry,J.M. and Yan,W.
  TITLE     Nectin-like protein 2 defines a subset of T-cell zone dendritic
            cells and is a ligand for class-I-restricted T-cell-associated
            molecule
  JOURNAL   J Biol Chem 280 (23), 21955-21964 (2005)
   PUBMED   15781451
  REMARK    GeneRIF: Necl2/CRTAM molecular pair could regulate a large panel of
            cell/cell interactions both within and outside of the immune system
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Kennedy,J., Vicari,A.P., Saylor,V., Zurawski,S.M., Copeland,N.G.,
            Gilbert,D.J., Jenkins,N.A. and Zlotnik,A.
  TITLE     A molecular analysis of NKT cells: identification of a class-I
            restricted T cell-associated molecule (CRTAM)
  JOURNAL   J Leukoc Biol 67 (5), 725-734 (2000)
   PUBMED   10811014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC070266.1, AF001622.1, AB209830.1 and AP004318.2.
            
            On Aug 30, 2004 this sequence version replaced NP_062550.1.
            
            Summary: The CRTAM gene is upregulated in CD4 (see MIM
            186940)-positive and CD8 (see CD8A; MIM 186910)-positive T cells
            and encodes a type I transmembrane protein with V and C1-like Ig
            domains (Yeh et al., 2008 [PubMed 18329370]).[supplied by OMIM, Feb
            2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313578.1, BC070266.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000227348.9/ ENSP00000227348.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.1"
     Protein         1..393
                     /product="cytotoxic and regulatory T-cell molecule isoform
                     1 precursor"
                     /note="class-I MHC-restricted T-cell-associated molecule"
                     /calculated_mol_wt=42512
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2147
     mat_peptide     18..393
                     /product="Cytotoxic and regulatory T-cell molecule.
                     /id=PRO_0000292602"
                     /note="propagated from UniProtKB/Swiss-Prot (O95727.2)"
                     /calculated_mol_wt=42512
     Region          21..114
                     /region_name="IgV_1_Necl_like"
                     /note="First (N-terminal) immunoglobulin (Ig)-like domain
                     of the nectin-like molecules; member of the V-set of Ig
                     superfamily (IgSF) domains; cd05717"
                     /db_xref="CDD:409382"
     Region          21..39
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409382"
     Region          21..23
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409382"
     Site            21
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95727.2)"
     Region          24..30
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409382"
     Region          32..40
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409382"
     Region          40..45
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409382"
     Site            order(46,49,54..55,57,63,65,101)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409382"
     Region          46..53
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409382"
     Region          46..52
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409382"
     Region          54..65
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409382"
     Region          56..60
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409382"
     Region          62..65
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409382"
     Region          66..101
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409382"
     Region          70..77
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409382"
     Region          80..86
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409382"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95727.2)"
     Region          93..101
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409382"
     Region          102..105
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409382"
     Region          105..114
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409382"
     Region          107..114
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409382"
     Region          121..207
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          137..141
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          151..155
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95727.2)"
     Region          181..185
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          193..198
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          209..212
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          225..273
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95727.2)"
     Site            288..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95727.2)"
     Region          328..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95727.2)"
     Region          374..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95727.2)"
     Region          390..393
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000250|UniProtKB:Q149L7"
                     /note="propagated from UniProtKB/Swiss-Prot (O95727.2)"
     CDS             1..393
                     /gene="CRTAM"
                     /gene_synonym="CD355"
                     /coded_by="NM_019604.4:48..1229"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8437.1"
                     /db_xref="GeneID:56253"
                     /db_xref="HGNC:HGNC:24313"
                     /db_xref="MIM:612597"
ORIGIN      
        1 mwwrvlslla wfplqeaslt nhtetitvee gqtltlkcvt slrknsslqw ltpsgftifl
       61 neypalknsk yqllhhsanq lsitvpnvtl qdegvykclh ysdsvstkev kvivlatpfk
      121 pileasvirk qngeehvvlm cstmrskppp qitwllgnsm evsggtlhef etdgkkcntt
      181 stliihtygk nstvdciirh rglqgrklva pfrfedlvtd eetasdaler nslssqdpqq
      241 ptstvsvted sstseidkee keqttqdpdl tteanpqylg larkksgill ltlvsflifi
      301 lfiivqlfim klrkahviwk kenevsehtl esyrsrsnne etsseekngq sshpmrcmny
      361 itklyseakt krkenvqhsk leekhiqvpe siv
//
LOCUS       NP_001356636             750 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger Y-chromosomal protein isoform 5 [Homo sapiens].
ACCESSION   NP_001356636 XP_016885565
VERSION     NP_001356636.1
DBSOURCE    REFSEQ: accession NM_001369707.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Ni,W., Perez,A.A., Schreiner,S., Nicolet,C.M. and Farnham,P.J.
  TITLE     Characterization of the ZFX family of transcription factors that
            bind downstream of the start site of CpG island promoters
  JOURNAL   Nucleic Acids Res 48 (11), 5986-6000 (2020)
   PUBMED   32406922
  REMARK    GeneRIF: Characterization of the ZFX family of transcription
            factors that bind downstream of the start site of CpG island
            promoters.
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Decarpentrie,F., Vernet,N., Mahadevaiah,S.K., Longepied,G.,
            Streichemberger,E., Aknin-Seifer,I., Ojarikre,O.A., Burgoyne,P.S.,
            Metzler-Guillemain,C. and Mitchell,M.J.
  TITLE     Human and mouse ZFY genes produce a conserved testis-specific
            transcript encoding a zinc finger protein with a short acidic
            domain and modified transactivation potential
  JOURNAL   Hum Mol Genet 21 (12), 2631-2645 (2012)
   PUBMED   22407129
  REMARK    GeneRIF: Studies identified a major testis-specific ZFY transcript
            that encodes a protein with the same short acidic domain.
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Tricoli,J.V. and Bracken,R.B.
  TITLE     ZFY gene expression and retention in human prostate adenocarcinoma
  JOURNAL   Genes Chromosomes Cancer 6 (2), 65-72 (1993)
   PUBMED   7680890
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Kochoyan,M., Keutmann,H.T. and Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            refinement of the NMR structure of an even finger by selective
            deuterium labeling and implications for DNA recognition
  JOURNAL   Biochemistry 30 (29), 7063-7072 (1991)
   PUBMED   1854720
REFERENCE   8  (residues 1 to 750)
  AUTHORS   North,M., Sargent,C., O'Brien,J., Taylor,K., Wolfe,J., Affara,N.A.
            and Ferguson-Smith,M.A.
  TITLE     Comparison of ZFY and ZFX gene structure and analysis of
            alternative 3' untranslated regions of ZFY
  JOURNAL   Nucleic Acids Res 19 (10), 2579-2586 (1991)
   PUBMED   2041734
REFERENCE   9  (residues 1 to 750)
  AUTHORS   Kochoyan,M., Havel,T.F., Nguyen,D.T., Dahl,C.E., Keutmann,H.T. and
            Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            2D NMR structure of an even finger and implications for
            'jumping-linker' DNA recognition
  JOURNAL   Biochemistry 30 (14), 3371-3386 (1991)
   PUBMED   1849423
REFERENCE   10 (residues 1 to 750)
  AUTHORS   Palmer,M.S., Berta,P., Sinclair,A.H., Pym,B. and Goodfellow,P.N.
  TITLE     Comparison of human ZFY and ZFX transcripts
  JOURNAL   Proc Natl Acad Sci U S A 87 (5), 1681-1685 (1990)
   PUBMED   2308929
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006157.2.
            
            On Apr 16, 2019 this sequence version replaced XP_016885565.1.
            
            Summary: This gene encodes a zinc finger-containing protein that
            may function as a transcription factor. This gene was once a
            candidate gene for the testis-determining factor (TDF) and was
            erroneously referred to as TDF. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.98610.1,
                                           SRR1803615.262460.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yp11.2"
     Protein         1..750
                     /product="zinc finger Y-chromosomal protein isoform 5"
                     /note="zinc finger Y-chromosomal protein"
                     /calculated_mol_wt=84956
     Region          71..355
                     /region_name="Zfx_Zfy_act"
                     /note="Zfx / Zfy transcription activation region;
                     pfam04704"
                     /db_xref="CDD:461400"
     Region          <366..541
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          <372..>394
                     /region_name="ROS_MUCR"
                     /note="ROS/MUCR transcriptional regulator protein;
                     cl19880"
                     /db_xref="CDD:473244"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          403..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(440,442,444,446..447,450..451,454,500,502,506..507,
                     510..511,514,528,530,532,534..535,538..539,542)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          488..>625
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          495..515
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          507..531
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          523..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          552..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          609..629
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          664..686
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          666..686
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(671,673,675,677..678,681..682,685,699,701,705..706,
                     709..710,714,728,730,732,734..735,738..739,742)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          678..702
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          694..715
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          723..743
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..750
                     /gene="ZFY"
                     /gene_synonym="ZNF911"
                     /coded_by="NM_001369707.1:95..2347"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:7544"
                     /db_xref="HGNC:HGNC:12870"
                     /db_xref="MIM:490000"
ORIGIN      
        1 mdedefelqp qepnsffdgi gadathmdgd qivveiqeav fvsnivdsdi tvhnfvpddp
       61 dsvviqdvve dvvieedvqc sdileeadvs enviipeqvl dsdvteevsl phctvpddvl
      121 asditstsms mpehvltses mhvcdighve hmvhdsvvea eiitdpltsd ivseevlvad
      181 capeavidas gisvdqqdnd kascedylmi slddagkieh dgstgvtida esemdpckvd
      241 stcpevikvy ifkadpgedd lggtvdives ependhgvel ldqnssirvp rekmvymtvn
      301 dsqqededls nnsdgienrn gtasallhid esaglgrlak qkpkkkrrpd srqyqtaiii
      361 gpdghpltvy pcmicgkkfk srgflkrhmk nhpehlakkk yhctdcdytt nkkislhnhl
      421 eshkltskae kaiecdecgk hfshagalft hkmvhkekga nkmhkckfce yetaeqglln
      481 rhllavhskn fphicvecgk gfrhpselrk hmrihtgekp yqcqyceyrs adssnlkthi
      541 ktkhskempf kcdiclltfs dtkevqqhtl vhqeskthqc lhcdhkssns sdlkrhvisv
      601 htkdyphkce mcekgfhrps elkkhvavhk gkkmhqcrhc dfkiadpfvl srhilsvhtk
      661 dlpfrckrcr kgfrqqnelk khmkthsgrk vyqceyceys ttdasgfkrh visihtkdyp
      721 hrceyckkgf rrpseknqhi mrhhkevglp
//
LOCUS       NP_001354556             179 aa            linear   MAM 27-APR-2025
DEFINITION  insulin-like growth factor 2 preproprotein [Bos taurus].
ACCESSION   NP_001354556 XP_015316818
VERSION     NP_001354556.1
DBSOURCE    REFSEQ: accession NM_001367627.1
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Willhelm,B.R., Ticiani,E., Campagnolo,K., Rodrigues,J.L.,
            Roberts,A.J., Anderson,G.B. and Bertolini,M.
  TITLE     Components of the insulin-like growth factor system in in vivo -
            and in vitro-derived fetuses of cattle, and the association with
            growth and development
  JOURNAL   Anim Reprod Sci 234, 106856 (2021)
   PUBMED   34626867
  REMARK    GeneRIF: Components of the insulin-like growth factor system in in
            vivo - and in vitro-derived fetuses of cattle, and the association
            with growth and development.
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Ghanipoor-Samami,M., Javadmanesh,A., Burns,B.M., Thomsen,D.A.,
            Nattrass,G.S., Estrella,C.A.S., Kind,K.L. and Hiendleder,S.
  TITLE     Atlas of tissue- and developmental stage specific gene expression
            for the bovine insulin-like growth factor (IGF) system
  JOURNAL   PLoS One 13 (7), e0200466 (2018)
   PUBMED   30001361
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Bouwman,A.C., Daetwyler,H.D., Chamberlain,A.J., Ponce,C.H.,
            Sargolzaei,M., Schenkel,F.S., Sahana,G., Govignon-Gion,A.,
            Boitard,S., Dolezal,M., Pausch,H., Brondum,R.F., Bowman,P.J.,
            Thomsen,B., Guldbrandtsen,B., Lund,M.S., Servin,B., Garrick,D.J.,
            Reecy,J., Vilkki,J., Bagnato,A., Wang,M., Hoff,J.L., Schnabel,R.D.,
            Taylor,J.F., Vinkhuyzen,A.A.E., Panitz,F., Bendixen,C., Holm,L.E.,
            Gredler,B., Hoze,C., Boussaha,M., Sanchez,M.P., Rocha,D.,
            Capitan,A., Tribout,T., Barbat,A., Croiseau,P., Drogemuller,C.,
            Jagannathan,V., Vander Jagt,C., Crowley,J.J., Bieber,A.,
            Purfield,D.C., Berry,D.P., Emmerling,R., Gotz,K.U.,
            Frischknecht,M., Russ,I., Solkner,J., Van Tassell,C.P., Fries,R.,
            Stothard,P., Veerkamp,R.F., Boichard,D., Goddard,M.E. and
            Hayes,B.J.
  TITLE     Meta-analysis of genome-wide association studies for cattle stature
            identifies common genes that regulate body size in mammals
  JOURNAL   Nat Genet 50 (3), 362-367 (2018)
   PUBMED   29459679
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Su,J., Wang,Y., Xing,X., Zhang,L., Sun,H. and Zhang,Y.
  TITLE     Melatonin significantly improves the developmental competence of
            bovine somatic cell nuclear transfer embryos
  JOURNAL   J Pineal Res 59 (4), 455-468 (2015)
   PUBMED   26331949
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Mendonca Ados,S., Guimaraes,A.L., da Silva,N.M., Caetano,A.R.,
            Dode,M.A. and Franco,M.M.
  TITLE     Characterization of the IGF2 Imprinted Gene Methylation Status in
            Bovine Oocytes during Folliculogenesis
  JOURNAL   PLoS One 10 (10), e0142072 (2015)
   PUBMED   26517264
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Congote,L.F., Mazza,L. and Palfree,R.G.
  TITLE     Nucleotide sequence of the central coding region of bovine
            erythrotropin/insulin-like growth factor II cDNA from fetal
            intestine and northern analysis of the major IGF II transcripts at
            the time of hepatic erythropoiesis
  JOURNAL   Comp Biochem Physiol B 103 (1), 127-131 (1992)
   PUBMED   1280544
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Brown,W.M., Dziegielewska,K.M., Foreman,R.C. and Saunders,N.R.
  TITLE     The nucleotide and deduced amino acid sequences of insulin-like
            growth factor II cDNAs from adult bovine and fetal sheep liver
  JOURNAL   Nucleic Acids Res 18 (15), 4614 (1990)
   PUBMED   2388846
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Li,Q.G., Blacher,R., Esch,F. and Congote,L.F.
  TITLE     A heparin-binding erythroid cell stimulating factor from fetal
            bovine serum has the N-terminal sequence of insulin-like growth
            factor II
  JOURNAL   Biochem Biophys Res Commun 166 (2), 557-561 (1990)
   PUBMED   2302223
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Francis,G.L., Upton,F.M., Ballard,F.J., McNeil,K.A. and
            Wallace,J.C.
  TITLE     Insulin-like growth factors 1 and 2 in bovine colostrum. Sequences
            and biological activities compared with those of a potent truncated
            form
  JOURNAL   Biochem J 251 (1), 95-103 (1988)
   PUBMED   3390164
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Honegger,A. and Humbel,R.E.
  TITLE     Insulin-like growth factors I and II in fetal and adult bovine
            serum. Purification, primary structures, and immunological
            cross-reactivities
  JOURNAL   J Biol Chem 261 (2), 569-575 (1986)
   PUBMED   3941093
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from NKLS02000029.1.
            
            On Dec 12, 2018 this sequence version replaced XP_015316818.1.
            
            Summary: This gene encodes a member of the insulin family of
            protein growth factors, which are involved in fetal development and
            growth. It is an imprinted gene that is expressed from the paternal
            allele while the maternal allele is silenced. The encoded protein
            is proteolytically processed to generate the mature peptide
            hormone, which binds to receptors of the insulin receptor family.
            This peptide plays a role in oocyte development and
            folliculogenesis in female cattle. Polymorphisms in this gene may
            be associated with cattle body mass. [provided by RefSeq, Dec
            2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5571260.39726.1,
                                           SRR5571257.1973.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03145427, SAMN04019641
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="29"
                     /map="29"
                     /breed="Hereford"
     Protein         1..179
                     /product="insulin-like growth factor 2 preproprotein"
                     /note="insulin-like growth factor II; IGF-II;
                     erythrotropin; insulin-like growth factor 2 (somatomedin
                     A)"
                     /calculated_mol_wt=17250
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2450
     mat_peptide     25..91
                     /product="Insulin-like growth factor 2.
                     /id=PRO_0000015711"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
                     /calculated_mol_wt=7533
     Region          25..52
                     /region_name="B"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Region          28..91
                     /region_name="IlGF"
                     /note="insulin_like growth factors; specific to
                     vertebrates. Members include a number of peptides
                     including insulin-like growth factors I and II, which play
                     a variety of roles in controlling processes such as
                     growth, differentiation, and reproduction. On a...;
                     cd04368"
                     /db_xref="CDD:239834"
     Site            order(30,39,47..51)
                     /site_type="active"
                     /note="IGFBP binding surface [active]"
                     /db_xref="CDD:239834"
     Site            order(48,50..51,67)
                     /site_type="active"
                     /note="type 1 IGF- and insulin-receptor binding surface
                     [active]"
                     /db_xref="CDD:239834"
     Site            48
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          53..64
                     /region_name="C"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Site            58
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Site            61
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Site            62
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          65..85
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Site            order(72..74,78..79)
                     /site_type="active"
                     /note="type 2 IGF-receptor binding surface [active]"
                     /db_xref="CDD:239834"
     Region          86..91
                     /region_name="D"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     mat_peptide     93..126
                     /product="Preptin. /id=PRO_0000370373"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
                     /calculated_mol_wt=3877
     Site            106
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19674964; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          112..166
                     /region_name="IGF2_C"
                     /note="Insulin-like growth factor II E-peptide; pfam08365"
                     /db_xref="CDD:462445"
     Site            154
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:19674964; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          160..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Site            163
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19674964; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     CDS             1..179
                     /gene="IGF2"
                     /coded_by="NM_001367627.1:101..640"
                     /db_xref="BGD:BT11333"
                     /db_xref="GeneID:281240"
                     /db_xref="VGNC:VGNC:30078"
ORIGIN      
        1 mgitagksvl vllaflafas ccyaayrpse tlcggelvdt lqfvcgdrgf yfsrpssrin
       61 rrsrgiveec cfrscdlall etycatpaks erdvsasttv lpddvtaypv gkffqydiwk
      121 qstqrlrrgl paflrarrgr tlakelealr eakshrplia lptqdpathg gasskassd
//
LOCUS       NP_001243793             970 aa            linear   PRI 27-APR-2025
DEFINITION  auxilin isoform 1 [Homo sapiens].
ACCESSION   NP_001243793
VERSION     NP_001243793.1
DBSOURCE    REFSEQ: accession NM_001256864.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Chiu,C.C., Chen,Y.L., Weng,Y.H., Liu,S.Y., Li,H.L., Yeh,T.H. and
            Wang,H.L.
  TITLE     Downregulation of Protease Cathepsin D and Upregulation of
            Pathologic alpha-Synuclein Mediate Paucity of DNAJC6-Induced
            Degeneration of Dopaminergic Neurons
  JOURNAL   Int J Mol Sci 25 (12), 6711 (2024)
   PUBMED   38928416
  REMARK    GeneRIF: Downregulation of Protease Cathepsin D and Upregulation of
            Pathologic alpha-Synuclein Mediate Paucity of DNAJC6-Induced
            Degeneration of Dopaminergic Neurons.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Benussi,L., Longobardi,A., Kocoglu,C., Carrara,M., Bellini,S.,
            Ferrari,C., Nicsanu,R., Saraceno,C., Bonvicini,C., Fostinelli,S.,
            Zanardini,R., Catania,M., Moisse,M., Van Damme,P., Di Fede,G.,
            Binetti,G., Van Broeckhoven,C., van der Zee,J. and Ghidoni,R.
  TITLE     Investigating the Endo-Lysosomal System in Major Neurocognitive
            Disorders Due to Alzheimer's Disease, Frontotemporal Lobar
            Degeneration and Lewy Body Disease: Evidence for SORL1 as a
            Cross-Disease Gene
  JOURNAL   Int J Mol Sci 22 (24), 13633 (2021)
   PUBMED   34948429
  REMARK    GeneRIF: Investigating the Endo-Lysosomal System in Major
            Neurocognitive Disorders Due to Alzheimer's Disease, Frontotemporal
            Lobar Degeneration and Lewy Body Disease: Evidence for SORL1 as a
            Cross-Disease Gene.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 970)
  AUTHORS   Wulansari,N., Darsono,W.H.W., Woo,H.J., Chang,M.Y., Kim,J.,
            Bae,E.J., Sun,W., Lee,J.H., Cho,I.J., Shin,H., Lee,S.J. and
            Lee,S.H.
  TITLE     Neurodevelopmental defects and neurodegenerative phenotypes in
            human brain organoids carrying Parkinson's disease-linked DNAJC6
            mutations
  JOURNAL   Sci Adv 7 (8) (2021)
   PUBMED   33597231
  REMARK    GeneRIF: Neurodevelopmental defects and neurodegenerative
            phenotypes in human brain organoids carrying Parkinson's
            disease-linked DNAJC6 mutations.
            Erratum:[Sci Adv. 2023 Nov 3;9(44):eadl1498. doi:
            10.1126/sciadv.adl1498. PMID: 37922364]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 970)
  AUTHORS   Ng,J., Cortes-Saladelafont,E., Abela,L., Termsarasab,P., Mankad,K.,
            Sudhakar,S., Gorman,K.M., Heales,S.J.R., Pope,S., Biassoni,L.,
            Csanyi,B., Cain,J., Rakshi,K., Coutts,H., Jayawant,S.,
            Jefferson,R., Hughes,D., Garcia-Cazorla,A., Grozeva,D.,
            Raymond,F.L., Perez-Duenas,B., De Goede,C., Pearson,T.S., Meyer,E.
            and Kurian,M.A.
  TITLE     DNAJC6 Mutations Disrupt Dopamine Homeostasis in Juvenile
            Parkinsonism-Dystonia
  JOURNAL   Mov Disord 35 (8), 1357-1368 (2020)
   PUBMED   32472658
  REMARK    GeneRIF: DNAJC6 Mutations Disrupt Dopamine Homeostasis in Juvenile
            Parkinsonism-Dystonia.
REFERENCE   5  (residues 1 to 970)
  AUTHORS   Shen,T., Zhao,S., Jiang,Y., Pu,J., Lai,H.Y., Yan,Y., Tian,J.,
            Chen,Y. and Zhang,B.
  TITLE     Haplotype Analysis on the Relationship of the DNAJC6 Gene with
            Early-Onset Parkinson's Disease Risk in a Chinese Population
  JOURNAL   J Parkinsons Dis 9 (1), 109-120 (2019)
   PUBMED   30373961
  REMARK    GeneRIF: Early onset Parkinson is associated with several SNPs and
            haplotypes of DNAJC6 gene.
REFERENCE   6  (residues 1 to 970)
  AUTHORS   Scheele,U., Kalthoff,C. and Ungewickell,E.
  TITLE     Multiple interactions of auxilin 1 with clathrin and the AP-2
            adaptor complex
  JOURNAL   J Biol Chem 276 (39), 36131-36138 (2001)
   PUBMED   11470803
REFERENCE   7  (residues 1 to 970)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   8  (residues 1 to 970)
  AUTHORS   Ohtsuka,K. and Hata,M.
  TITLE     Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a
            proposal for their classification and nomenclature
  JOURNAL   Cell Stress Chaperones 5 (2), 98-112 (2000)
   PUBMED   11147971
REFERENCE   9  (residues 1 to 970)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   10 (residues 1 to 970)
  AUTHORS   Ungewickell,E., Ungewickell,H., Holstein,S.E., Lindner,R.,
            Prasad,K., Barouch,W., Martin,B., Greene,L.E. and Eisenberg,E.
  TITLE     Role of auxilin in uncoating clathrin-coated vesicles
  JOURNAL   Nature 378 (6557), 632-635 (1995)
   PUBMED   8524399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR002818.1, BX647203.1,
            BC109280.1 and AC119800.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: DNAJC6 belongs to the evolutionarily conserved DNAJ/HSP40
            family of proteins, which regulate molecular chaperone activity by
            stimulating ATPase activity. DNAJ proteins may have up to 3
            distinct domains: a conserved 70-amino acid J domain, usually at
            the N terminus, a glycine/phenylalanine (G/F)-rich region, and a
            cysteine-rich domain containing 4 motifs resembling a zinc finger
            domain (Ohtsuka and Hata, 2000 [PubMed 11147971]).[supplied by
            OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647203.1, SRR1660809.45874.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371069.5/ ENSP00000360108.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..970
                     /product="auxilin isoform 1"
                     /EC_number="3.1.3.48"
                     /note="auxilin; DnaJ (Hsp40) homolog, subfamily B, member
                     6; putative tyrosine-protein phosphatase auxilin; DnaJ
                     (Hsp40) homolog, subfamily C, member 6"
                     /calculated_mol_wt=105544
     Region          113..275
                     /region_name="PTP_auxilin_N"
                     /note="N-terminal protein tyrosine phosphatase-like domain
                     of auxilin; cd14563"
                     /db_xref="CDD:350411"
     Region          283..421
                     /region_name="PTEN_C2"
                     /note="C2 domain of PTEN tumour-suppressor protein;
                     pfam10409"
                     /db_xref="CDD:463081"
     Region          <562..829
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <918..963
                     /region_name="DnaJ"
                     /note="DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock
                     protein 40) proteins are highly conserved and play crucial
                     roles in protein translation, folding, unfolding,
                     translocation, and degradation. They act primarily by
                     stimulating the ATPase activity of Hsp70s; cd06257"
                     /db_xref="CDD:99751"
     Site            order(934..936,948,951..952,955..956)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     CDS             1..970
                     /gene="DNAJC6"
                     /gene_synonym="DJC6; PARK19"
                     /coded_by="NM_001256864.2:204..3116"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS58004.1"
                     /db_xref="GeneID:9829"
                     /db_xref="HGNC:HGNC:15469"
                     /db_xref="MIM:608375"
ORIGIN      
        1 msllgsyrkk tsndgyeslq lvdsngdlsa gsggvggkqr vnagaaarsp arqppdrast
       61 mdssgasspd mepsyggglf dmvkggagrl fsnlkdnlkd tlkdtssrvi qsvtsytkgd
      121 ldftyvtsri ivmsfpldnv digfrnqvdd irsfldsrhl dhytvynlsp ksyrtakfhs
      181 rvsecswpir qapslhnlfa vcrnmynwll qnpknvcvvh cldgraassi lvgamfifcn
      241 lystpgpair llyakrpgig lspshrrylg ymcdlladkp yrphfkplti ksitvspipf
      301 fnkqrngcrp ycdvligetk iystctdfer mkeyrvqdgk ifiplnitvq gdvvvsmyhl
      361 rstigsrlqa kvtntqifql qfhtgfipld ttvlkftkpe ldacdvpeky pqlfqvtldv
      421 elqphdkvid ltppwehyct kdvnpsilfs shqehqdtla lggqapidip pdnprhygqs
      481 gffaslcwqd qkseksfcee dhaalvnqes eqsddelltl ssphgnangd kphgvkkpsk
      541 kqqepaappp pedvdllgle gsamsnsfsp paapptnsel lsdlfgggga agptqagqsg
      601 vedvfhpsgp astqstprrs atstsasptl rvgegatfdp fgapskpsgq dllgsflnts
      661 sassdpflqp trspsptvha sstpavniqp dvsggwdwha kpggfgmgsk saatsptgss
      721 hgtpthqskp qtldpfadlg tlgsssfask pttptglggg fpplsspqka spqpmgggwq
      781 qggaynwqqp qpkpqpsmph sspqnrpnyn vsfsampggq nergkgssnl egkqkaadfe
      841 dllsgqgfna hkdkkgprti aemrkeemak emdpeklkil ewiegkerni rallstmhtv
      901 lwagetkwkp vgmadlvtpe qvkkvyrkav lvvhpdkatg qpyeqyakmi fmelndawse
      961 fenqgqkply
//
LOCUS       NP_065906                531 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 492 [Homo sapiens].
ACCESSION   NP_065906 XP_047550
VERSION     NP_065906.1
DBSOURCE    REFSEQ: accession NM_020855.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Kim,Y.J., Jang,W., Piao,X.M., Yoon,H.Y., Byun,Y.J., Kim,J.S.,
            Kim,S.M., Lee,S.K., Seo,S.P., Kang,H.W., Kim,W.T., Yun,S.J.,
            Shon,H.S., Ryu,K.H., Kim,S.W., Ha,Y.S., Yoon,G.S., Lee,S.C.,
            Kwon,T.G. and Kim,W.J.
  TITLE     ZNF492 and GPR149 methylation patterns as prognostic markers for
            clear cell renal cell carcinoma: Array-based DNA methylation
            profiling
  JOURNAL   Oncol Rep 42 (1), 453-460 (2019)
   PUBMED   31115548
  REMARK    GeneRIF: Data revealed that hypermethylation of ZNF492 and GPR149
            was significantly associated with shorter timetoprogression of
            patients with clear cell renal cell carcinoma (ccRCC).
            Hypermethylation of ZNF492 and GPR149 may be independent predictors
            of tumor progression. Similarly, the methylation status of these
            two genes was significantly associated with poor outcomes in the
            independent external validation cohort.
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Figueiredo,J.C., Hsu,L., Hutter,C.M., Lin,Y., Campbell,P.T.,
            Baron,J.A., Berndt,S.I., Jiao,S., Casey,G., Fortini,B., Chan,A.T.,
            Cotterchio,M., Lemire,M., Gallinger,S., Harrison,T.A., Le
            Marchand,L., Newcomb,P.A., Slattery,M.L., Caan,B.J., Carlson,C.S.,
            Zanke,B.W., Rosse,S.A., Brenner,H., Giovannucci,E.L., Wu,K.,
            Chang-Claude,J., Chanock,S.J., Curtis,K.R., Duggan,D., Gong,J.,
            Haile,R.W., Hayes,R.B., Hoffmeister,M., Hopper,J.L., Jenkins,M.A.,
            Kolonel,L.N., Qu,C., Rudolph,A., Schoen,R.E., Schumacher,F.R.,
            Seminara,D., Stelling,D.L., Thibodeau,S.N., Thornquist,M.,
            Warnick,G.S., Henderson,B.E., Ulrich,C.M., Gauderman,W.J.,
            Potter,J.D., White,E. and Peters,U.
  CONSRTM   CCFR; GECCO
  TITLE     Genome-wide diet-gene interaction analyses for risk of colorectal
            cancer
  JOURNAL   PLoS Genet 10 (4), e1004228 (2014)
   PUBMED   24743840
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Tsuritani,K., Irie,T., Yamashita,R., Sakakibara,Y., Wakaguri,H.,
            Kanai,A., Mizushima-Sugano,J., Sugano,S., Nakai,K. and Suzuki,Y.
  TITLE     Distinct class of putative 'non-conserved' promoters in humans:
            comparative studies of alternative promoters of human and mouse
            genes
  JOURNAL   Genome Res 17 (7), 1005-1014 (2007)
   PUBMED   17567985
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Lu,Z., Poliakov,E. and Redmond,T.M.
  TITLE     Identification of a KRAB-zinc finger protein binding to the Rpe65
            gene promoter
  JOURNAL   Curr Eye Res 31 (5), 457-466 (2006)
   PUBMED   16714237
  REMARK    GeneRIF: This KRAB-zinc finger protein serves as a moderate
            transcriptional factor for Rpe65 gene upregulation.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP871882.1, AB040906.1 and AC011467.7.
            
            On Jun 15, 2007 this sequence version replaced XP_047550.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP871882.1, AB040906.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000456783.3/ ENSP00000413660.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p12"
     Protein         1..531
                     /product="zinc finger protein 492"
                     /note="zinc finger protein 115 (Y20)"
                     /calculated_mol_wt=61028
     Region          <1..32
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          138..522
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          143..163
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(143,146,159,163)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          171..191
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(171,174,187,191)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          199..219
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(199,202,215,219)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(204,206,208,210..211,214..215,218,232,234,238..239,
                     242..243,246,260,262,264,266..267,270..271,274)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          227..247
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          255..275
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          283..303
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(283,286,299,303)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(288,290,292,294..295,298..299,302,316,318,322..323,
                     326..327,330,344,346,348,350..351,354..355,358)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          311..331
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          339..359
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          367..387
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          395..415
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          423..443
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          451..471
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          479..499
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..531
                     /gene="ZNF492"
                     /gene_synonym="ZNF115"
                     /coded_by="NM_020855.3:245..1840"
                     /db_xref="CCDS:CCDS46032.1"
                     /db_xref="GeneID:57615"
                     /db_xref="HGNC:HGNC:23707"
                     /db_xref="MIM:620124"
ORIGIN      
        1 mlenyrnlvf vgiaaskpdl itcleqgkep wnvkrhemva eppvvcsyfa rdlwpkqgkk
       61 nyfqkvilrr ykkcgcenlq lrkycksmde ckvhkecyng lnqcltttqn kifqcdkyvk
      121 vfhkfsnsnr htirhtgkks fkckeceksf cmlshlaqhk rihsgekpyk ckecgkayne
      181 tsnlsthkri htgkkpykce ecgkafnrls hltthkiiht gkkpykceec gkafnqsanl
      241 tthkrihtge kpykceecgr afsqsstlta hkiihagekp ykceecgkaf sqsstltthk
      301 iihtgekfyk ceecgkafsq lshltthkri hsgekpykce ecgkafkqss tltthkriha
      361 gekfykcevc skafsrfshl tthkrihtge kpykceecgk afnlssqltt hkiihtgekp
      421 ykceecgkaf nqsstlskhk vihtgekpyk yeecgkafnq sshltthkmi htgekpykce
      481 ecgkafnnss ilnrhkmiht geklykpesc nnacdniaki skykrncage k
//
LOCUS       NP_003747                352 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 3 subunit H [Homo
            sapiens].
ACCESSION   NP_003747
VERSION     NP_003747.1
DBSOURCE    REFSEQ: accession NM_003756.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Jin,H., Huang,X., Pan,Q., Ma,N., Xie,X., Wei,Y., Yu,F., Wen,W.,
            Zhang,B., Zhang,P., Chen,X., Wang,J., Liu,R.Y., Lin,J., Meng,X. and
            Lee,M.H.
  TITLE     The EIF3H-HAX1 axis increases RAF-MEK-ERK signaling activity to
            promote colorectal cancer progression
  JOURNAL   Nat Commun 15 (1), 2551 (2024)
   PUBMED   38514606
  REMARK    GeneRIF: The EIF3H-HAX1 axis increases RAF-MEK-ERK signaling
            activity to promote colorectal cancer progression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Mukamel,R.E., Handsaker,R.E., Sherman,M.A., Barton,A.R.,
            Hujoel,M.L.A., McCarroll,S.A. and Loh,P.R.
  TITLE     Repeat polymorphisms underlie top genetic risk loci for glaucoma
            and colorectal cancer
  JOURNAL   Cell 186 (17), 3659-3673 (2023)
   PUBMED   37527660
  REMARK    GeneRIF: Repeat polymorphisms underlie top genetic risk loci for
            glaucoma and colorectal cancer.
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Tang,J., Long,G., Li,X., Zhou,L., Zhou,Y. and Wu,Z.
  TITLE     The deubiquitinase EIF3H promotes hepatocellular carcinoma
            progression by stabilizing OGT and inhibiting ferroptosis
  JOURNAL   Cell Commun Signal 21 (1), 198 (2023)
   PUBMED   37559097
  REMARK    GeneRIF: The deubiquitinase EIF3H promotes hepatocellular carcinoma
            progression by stabilizing OGT and inhibiting ferroptosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Wei,Y., Chen,W., Li,Z., Xie,K. and Liu,F.
  TITLE     EIF3H stabilizes CCND1 to promotes intrahepatic cholangiocarcinoma
            progression via Wnt/beta-catenin signaling
  JOURNAL   FASEB J 36 (12), e22647 (2022)
   PUBMED   36350008
  REMARK    GeneRIF: EIF3H stabilizes CCND1 to promotes intrahepatic
            cholangiocarcinoma progression via Wnt/beta-catenin signaling.
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Saramaki,O., Willi,N., Bratt,O., Gasser,T.C., Koivisto,P.,
            Nupponen,N.N., Bubendorf,L. and Visakorpi,T.
  TITLE     Amplification of EIF3S3 gene is associated with advanced stage in
            prostate cancer
  JOURNAL   Am J Pathol 159 (6), 2089-2094 (2001)
   PUBMED   11733359
  REMARK    GeneRIF: Gain of EIF3S3 was associated with poor cancer-specific
            survival in incidentally found prostate carcinomas.
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Block,K.L., Vornlocher,H.P. and Hershey,J.W.
  TITLE     Characterization of cDNAs encoding the p44 and p35 subunits of
            human translation initiation factor eIF3
  JOURNAL   J Biol Chem 273 (48), 31901-31908 (1998)
   PUBMED   9822659
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Asano,K., Vornlocher,H.P., Richter-Cook,N.J., Merrick,W.C.,
            Hinnebusch,A.G. and Hershey,J.W.
  TITLE     Structure of cDNAs encoding human eukaryotic initiation factor 3
            subunits. Possible roles in RNA binding and macromolecular assembly
  JOURNAL   J Biol Chem 272 (43), 27042-27052 (1997)
   PUBMED   9341143
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Methot,N., Rom,E., Olsen,H. and Sonenberg,N.
  TITLE     The human homologue of the yeast Prt1 protein is an integral part
            of the eukaryotic initiation factor 3 complex and interacts with
            p170
  JOURNAL   J Biol Chem 272 (2), 1110-1116 (1997)
   PUBMED   8995410
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Asano,K., Kinzy,T.G., Merrick,W.C. and Hershey,J.W.
  TITLE     Conservation and diversity of eukaryotic translation initiation
            factor eIF3
  JOURNAL   J Biol Chem 272 (2), 1101-1109 (1997)
   PUBMED   8995409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AU117206.1, U54559.1, AA902770.1 and AC023520.7.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.10123.1,
                                           SRR1803616.67188.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMN03267776
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000521861.6/ ENSP00000429931.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q23.3-q24.11"
     Protein         1..352
                     /product="eukaryotic translation initiation factor 3
                     subunit H"
                     /note="eukaryotic translation initiation factor 3, subunit
                     2 (beta, 36kD); eukaryotic translation initiation factor
                     3, subunit 3 (gamma, 40kD); eukaryotic translation
                     initiation factor 3, subunit 3 gamma, 40kDa; eIF-3-gamma;
                     eIF3 p40 subunit; eukaryotic translation initiation factor
                     3 subunit 3"
                     /calculated_mol_wt=39799
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15372.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15372.1)"
     Region          37..300
                     /region_name="MPN_eIF3h"
                     /note="Mpr1p, Pad1p N-terminal (MPN) domains without
                     catalytic isopeptidase activity, found in eIF2h; cd08065"
                     /db_xref="CDD:163696"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03007,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15372.1)"
     Region          265..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15372.1)"
     CDS             1..352
                     /gene="EIF3H"
                     /gene_synonym="eIF3-gamma; eIF3-p40; EIF3S3"
                     /coded_by="NM_003756.3:27..1085"
                     /db_xref="CCDS:CCDS6319.1"
                     /db_xref="GeneID:8667"
                     /db_xref="HGNC:HGNC:3273"
                     /db_xref="MIM:603912"
ORIGIN      
        1 masrkegtgs tatsssstag aagkgkgkgg sgdsavkqvq idglvvlkii khyqeegqgt
       61 evvqgvllgl vvedrleitn cfpfpqhted dadfdevqyq memmrslrhv nidhlhvgwy
      121 qstyygsfvt ralldsqfsy qhaieesvvl iydpiktaqg slslkayrlt pklmevckek
      181 dfspealkka nitfeymfee vpiviknshl invlmwelek ksavadkhel lslassnhlg
      241 knlqllmdrv demsqdivky ntymrntskq qqqkhqyqqr rqqenmqrqs rgepplpeed
      301 lsklfkppqp parmdsllia gqintycqni keftaqnlgk lfmaqalqey nn
//
LOCUS       NP_689498                433 aa            linear   PRI 27-APR-2025
DEFINITION  arrestin domain-containing protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_689498
VERSION     NP_689498.1
DBSOURCE    REFSEQ: accession NM_152285.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Zhao,Q., Jiang,F., Zhuang,H., Chu,Y., Zhang,F. and Wang,C.
  TITLE     MicroRNA miR-124-3p suppresses proliferation and
            epithelial-mesenchymal transition of hepatocellular carcinoma via
            ARRDC1 (arrestin domain containing 1)
  JOURNAL   Bioengineered 13 (4), 8255-8265 (2022)
   PUBMED   35300565
  REMARK    GeneRIF: MicroRNA miR-124-3p suppresses proliferation and
            epithelial-mesenchymal transition of hepatocellular carcinoma via
            ARRDC1 (arrestin domain containing 1).
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Xu,H., Yu,X., Yang,Z., Song,Q., Cheng,S., He,Z. and Dai,L.
  TITLE     PAX5-activated lncRNA ARRDC1-AS1 accelerates the autophagy and
            progression of DLBCL through sponging miR-2355-5p to regulate ATG5
  JOURNAL   Life Sci 286, 119932 (2021)
   PUBMED   34499929
  REMARK    GeneRIF: PAX5-activated lncRNA ARRDC1-AS1 accelerates the autophagy
            and progression of DLBCL through sponging miR-2355-5p to regulate
            ATG5.
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Nabhan,J.F., Hu,R., Oh,R.S., Cohen,S.N. and Lu,Q.
  TITLE     Formation and release of arrestin domain-containing protein
            1-mediated microvesicles (ARMMs) at plasma membrane by recruitment
            of TSG101 protein
  JOURNAL   Proc Natl Acad Sci U S A 109 (11), 4146-4151 (2012)
   PUBMED   22315426
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Shea,F.F., Rowell,J.L., Li,Y., Chang,T.H. and Alvarez,C.E.
  TITLE     Mammalian alpha arrestins link activated seven transmembrane
            receptors to Nedd4 family e3 ubiquitin ligases and interact with
            beta arrestins
  JOURNAL   PLoS One 7 (12), e50557 (2012)
   PUBMED   23236378
REFERENCE   8  (residues 1 to 433)
  AUTHORS   Rauch,S. and Martin-Serrano,J.
  TITLE     Multiple interactions between the ESCRT machinery and
            arrestin-related proteins: implications for PPXY-dependent budding
  JOURNAL   J Virol 85 (7), 3546-3556 (2011)
   PUBMED   21191027
  REMARK    GeneRIF: The authors show that WWP1 changes the ubiquitination
            status of ARRDC1, suggesting that the arrestins may provide a
            platform for ubiquitination in PPXY-dependent budding.
REFERENCE   9  (residues 1 to 433)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   10 (residues 1 to 433)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC032346.1 and AA552336.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the shorter isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ420420.1, SRR1660807.74277.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371421.9/ ENSP00000360475.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..433
                     /product="arrestin domain-containing protein 1 isoform 1"
                     /note="arrestin domain-containing protein 1;
                     alpha-arrestin 1"
                     /calculated_mol_wt=45850
     Region          7..139
                     /region_name="Arrestin_N"
                     /note="Arrestin (or S-antigen), N-terminal domain;
                     cl22903"
                     /db_xref="CDD:451447"
     Region          162..284
                     /region_name="Arrestin_C"
                     /note="Arrestin (or S-antigen), C-terminal domain;
                     pfam02752"
                     /db_xref="CDD:460676"
     Region          296..322
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5I2.1)"
     Region          349..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5I2.1)"
     Region          402..405
                     /region_name="PPxY motif 1.
                     /evidence=ECO:0000269|PubMed:23886940"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5I2.1)"
     Region          415..418
                     /region_name="PPxY motif 2.
                     /evidence=ECO:0000269|PubMed:23886940"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5I2.1)"
     CDS             1..433
                     /gene="ARRDC1"
                     /coded_by="NM_152285.4:33..1334"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7049.1"
                     /db_xref="GeneID:92714"
                     /db_xref="HGNC:HGNC:28633"
                     /db_xref="MIM:619768"
ORIGIN      
        1 mgrvqlfeis lshgrvvysp geplagtvrv rlgaplpfra irvtcigscg vsnkandtaw
       61 vveegyfnss lsladkgslp agehsfpfqf llpataptsf egpfgkivhq vraaihtprf
      121 skdhkcslvf yilsplnlns ipdieqpnva satkkfsykl vktgsvvlta stdlrgyvvg
      181 qalqlhadve nqsgkdtspv vasllqkvsy kakrwihdvr tiaevegagv kawrraqwhe
      241 qilvpalpqs alpgcslihi dyylqvslka peatvtlpvf igniavnhap vsprpglglp
      301 pgapplvvps appqeeaeae aaaggphfld pvflstkshs qrqpllatls svpgapepcp
      361 qdgspashpl hpplcistga tvpyfaegsg gpvpttstli lppeysswgy pyeappsyeq
      421 scggvepslt pes
//
LOCUS       NP_115911                361 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 37 isoform b [Homo
            sapiens].
ACCESSION   NP_115911
VERSION     NP_115911.1
DBSOURCE    REFSEQ: accession NM_032522.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136170.14 and KF455104.1.
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (b)
            has a shorter and distinct C-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC006315.2 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1"
     Protein         1..361
                     /product="zinc finger and BTB domain-containing protein 37
                     isoform b"
                     /note="zinc finger and BTB domain-containing protein 37"
                     /calculated_mol_wt=39636
     Region          7..129
                     /region_name="BTB_POZ_ZBTB37"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 37 (ZBTB37); cd18222"
                     /db_xref="CDD:349531"
     Region          140..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TC79.1)"
     CDS             1..361
                     /gene="ZBTB37"
                     /gene_synonym="D430004I08Rik; ZNF908"
                     /coded_by="NM_032522.5:249..1334"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1312.1"
                     /db_xref="GeneID:84614"
                     /db_xref="HGNC:HGNC:28365"
ORIGIN      
        1 mekggniqle ipdfsnsvls hlnqlrmqgr lcdivvnvqg qafrahkvvl aasspyfrdh
       61 mslnemstvs isviknptvf eqllsfcytg riclqladii syltaasflq mqhiidkctq
      121 ilegihfkin vaeveaelsq trtkhqerpp eshrvtpnln rslsprhntp kgnrrgqvsa
      181 vldirelspp eestspqiie pssdvesrep ilrinragqw yvetgvadrg grsddevrvl
      241 gavhiktenl eewlgpenqp sgedgssaee vtamvidttg hgsvgqenyt lgssgakvar
      301 ptssevdrfs psgsvvplte rhrarsespg rmdepkqpss qvwscgfrta lvvggiatvy
      361 e
//
LOCUS       NP_001116242             503 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 37 isoform a [Homo
            sapiens].
ACCESSION   NP_001116242 XP_005245603
VERSION     NP_001116242.1
DBSOURCE    REFSEQ: accession NM_001122770.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136170.14 and KF455104.1.
            
            On Sep 24, 2016 this sequence version replaced XP_005245603.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302696.1, SRR1660803.259660.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367701.10/ ENSP00000356674.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1"
     Protein         1..503
                     /product="zinc finger and BTB domain-containing protein 37
                     isoform a"
                     /note="zinc finger and BTB domain-containing protein 37"
                     /calculated_mol_wt=55924
     Region          7..129
                     /region_name="BTB_POZ_ZBTB37"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 37 (ZBTB37); cd18222"
                     /db_xref="CDD:349531"
     Region          140..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TC79.1)"
     Region          280..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TC79.1)"
     Region          375..395
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(380,382,384,386..387,390..391,394,408,410,414..415,
                     418..419,422,436,438,440,442..443,446..447)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          387..412
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          401..423
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          403..423
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          416..438
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          431..449
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          457..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TC79.1)"
     CDS             1..503
                     /gene="ZBTB37"
                     /gene_synonym="D430004I08Rik; ZNF908"
                     /coded_by="NM_001122770.3:249..1760"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44278.1"
                     /db_xref="GeneID:84614"
                     /db_xref="HGNC:HGNC:28365"
ORIGIN      
        1 mekggniqle ipdfsnsvls hlnqlrmqgr lcdivvnvqg qafrahkvvl aasspyfrdh
       61 mslnemstvs isviknptvf eqllsfcytg riclqladii syltaasflq mqhiidkctq
      121 ilegihfkin vaeveaelsq trtkhqerpp eshrvtpnln rslsprhntp kgnrrgqvsa
      181 vldirelspp eestspqiie pssdvesrep ilrinragqw yvetgvadrg grsddevrvl
      241 gavhiktenl eewlgpenqp sgedgssaee vtamvidttg hgsvgqenyt lgssgakvar
      301 ptssevdrfs psgsvvplte rhrarsespg rmdepkqpss qveesammgv sgyveylreq
      361 evserwfryn prltciycak sfnqkgsldr hmrlhmgitp fvcrmcgkky trkdqleyhi
      421 rkhtgnkpfh chvcgksfpf qailnqhfrk nhpgcipleg phsispettv tsrgqaeees
      481 psqeetvapg eavqgsvstt gpd
//
LOCUS       NP_079243                456 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 556 isoform 1 [Homo sapiens].
ACCESSION   NP_079243
VERSION     NP_079243.1
DBSOURCE    REFSEQ: accession NM_024967.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK021699.1, BC009374.2 and AC006130.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK021699.1, SRR1660803.119357.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307635.3/ ENSP00000302603.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..456
                     /product="zinc finger protein 556 isoform 1"
                     /calculated_mol_wt=51450
     Region          <14..44
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          93..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAH1.1)"
     Region          123..139
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <146..294
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          149..169
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(154,156,158,160..161,164..165,168,182,184,188..189,
                     192..193,196,210,212,214,216..217,220..221,224)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          177..197
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          205..225
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          233..253
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          261..281
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(266,268,270,272..273,276..277,280,294,296,300..301,
                     304..305,308,322,324,326,328..329,332..333,336)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          289..309
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..324
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          317..337
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          331..365
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAH1.1)"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          386..406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAH1.1)"
     Region          427..447
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..456
                     /gene="ZNF556"
                     /coded_by="NM_024967.3:88..1458"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12097.1"
                     /db_xref="GeneID:80032"
                     /db_xref="HGNC:HGNC:25669"
ORIGIN      
        1 mdtvvfedvv vdftleewal lnpaqrklyr dvmletfkhl asvdneaqlk asgsisqqdt
       61 sgeklslkqk iekftrkniw asllgknwee hsvkdkhntk erhlsrnprv erpcksskgn
      121 krgrtfrktr ncnrhlrknc ctsvrryecs qcgklfthss slirhkrahs gqklykckec
      181 gkafsrpsyl qthekthsge kpyacqscgk tflrshslte hvrthtgekp yecgqcgkgf
      241 scpksfrahv mmhaggrpye ckhcgkafrc qksfrvhmim haggrpyeck qcgkaycwat
      301 sfqrhvrihn gekpykcgkc gkafgwpssl hkharthakk kpvsggsvgk ssarprpstd
      361 vksqtrekvy kcetcgktyg wssslhkher khtgekpvna asvgkpsggl cssknvrtqi
      421 gqkpskcekc gkafscpkaf qghvrshtgk ksctsk
//
LOCUS       NP_714913                293 aa            linear   PRI 27-APR-2025
DEFINITION  ELMO domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_714913
VERSION     NP_714913.1
DBSOURCE    REFSEQ: accession NM_153702.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Schiavon,C.R., Turn,R.E., Newman,L.E. and Kahn,R.A.
  TITLE     ELMOD2 regulates mitochondrial fusion in a mitofusin-dependent
            manner, downstream of ARL2
  JOURNAL   Mol Biol Cell 30 (10), 1198-1213 (2019)
   PUBMED   30865555
  REMARK    GeneRIF: Results suggest that ELMOD2 is functioning as an effector
            downstream of ARL2 and upstream of the mitofusins to promote
            mitochondrial fusion. Data provide insights into the pathway by
            which mitochondrial fusion is regulated in the cell.
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Ivanova,A.A., East,M.P., Yi,S.L. and Kahn,R.A.
  TITLE     Characterization of recombinant ELMOD (cell engulfment and motility
            domain) proteins as GTPase-activating proteins (GAPs) for ARF
            family GTPases
  JOURNAL   J Biol Chem 289 (16), 11111-11121 (2014)
   PUBMED   24616099
  REMARK    GeneRIF: The non-opioid sigma-1 receptor (S1R) was identified as a
            novel effector of GAP activity of ELMOD1-3 proteins as its direct
            binding to either ELMOD1 or ELMOD2 resulted in loss of GAP
            activity.
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Pulkkinen,V., Bruce,S., Rintahaka,J., Hodgson,U., Laitinen,T.,
            Alenius,H., Kinnula,V.L., Myllarniemi,M., Matikainen,S. and Kere,J.
  TITLE     ELMOD2, a candidate gene for idiopathic pulmonary fibrosis,
            regulates antiviral responses
  JOURNAL   FASEB J 24 (4), 1167-1177 (2010)
   PUBMED   19966137
  REMARK    GeneRIF: TLR3 pathway is dependent on ELMOD2
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Bowzard,J.B., Cheng,D., Peng,J. and Kahn,R.A.
  TITLE     ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs
  JOURNAL   J Biol Chem 282 (24), 17568-17580 (2007)
   PUBMED   17452337
  REMARK    GeneRIF: Results describe the purification from bovine testis of an
            Arl2 GAP and its identity as ELMOD2, a protein with no previously
            described function.
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Hodgson,U., Pulkkinen,V., Dixon,M., Peyrard-Janvid,M., Rehn,M.,
            Lahermo,P., Ollikainen,V., Salmenkivi,K., Kinnula,V., Kere,J.,
            Tukiainen,P. and Laitinen,T.
  TITLE     ELMOD2 is a candidate gene for familial idiopathic pulmonary
            fibrosis
  JOURNAL   Am J Hum Genet 79 (1), 149-154 (2006)
   PUBMED   16773575
  REMARK    GeneRIF: results suggest ELMOD2 as a novel candidate gene for
            susceptibility in familial idiopathic pulmonary fibrosis
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK312800.1, BX648843.1,
            AC093671.3 and BX648349.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes one of six engulfment and motility
            (ELMO) domain-containing proteins. This gene is thought to play a
            role in antiviral responses. Mutations in this gene may be involved
            in the cause of familial idiopathic pulmonary fibrosis. [provided
            by RefSeq, Sep 2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX648349.1, SRR1803611.232066.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323570.8/ ENSP00000326342.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..293
                     /product="ELMO domain-containing protein 2"
                     /note="ELMO/CED-12 domain containing 2"
                     /calculated_mol_wt=34830
     Region          112..268
                     /region_name="ELMO_CED12"
                     /note="ELMO/CED-12 family; pfam04727"
                     /db_xref="CDD:461411"
     CDS             1..293
                     /gene="ELMOD2"
                     /gene_synonym="9830169G11Rik"
                     /coded_by="NM_153702.4:123..1004"
                     /db_xref="CCDS:CCDS3752.1"
                     /db_xref="GeneID:255520"
                     /db_xref="HGNC:HGNC:28111"
                     /db_xref="MIM:610196"
ORIGIN      
        1 mfislweffy ghffrfwmkw llrqmtgkce lqrifdtyvg aqrthriens ltysknkvlq
       61 kathvvqsev dkyvddimke kninpekdas fkicmkmcll qitgykqlyl dvesvrkrpy
      121 dsdnlqheel lmklwnllmp tkklnarisk qwaeigfqgd dpktdfrgmg ilglinlvyf
      181 senytseahq ilsrsnhpkl gysyaivgin ltemaysllk sealkfhlyn lvpgiptmeh
      241 fhqfycylvy efdkfwfeee pesimyfnly rekfhekikg llldcnvalt lkv
//
LOCUS       NP_077000                288 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat and SOCS box protein 8 isoform a [Homo sapiens].
ACCESSION   NP_077000
VERSION     NP_077000.1
DBSOURCE    REFSEQ: accession NM_024095.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Guo,Y., Li,R., Tan,Z., Shi,J., Fu,Y., Song,Y., Zhu,M., Zhang,L. and
            Huang,J.
  TITLE     E3 ubiquitin ligase ASB8 negatively regulates interferon via
            regulating TBK1/IKKi homeostasis
  JOURNAL   Mol Immunol 121, 195-203 (2020)
   PUBMED   32298923
  REMARK    GeneRIF: E3 ubiquitin ligase ankyrin repeat and SOCS box-containing
            8(ASB8) interacted with TBK1/IKKi and phosphorylation modification
            of ASB8 at site of Ser17 to further strengthen its ubiquitination
            activity were verified. Phosphorylated ASB8 accelerates K48-linked
            ubiquitination and degradation of TBK1/IKKi, which further reduces
            phosphorylation level of IRF3 and inhibits production of IFN-beta.
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Liu,Y., Li,J., Zhang,F., Qin,W., Yao,G., He,X., Xue,P., Ge,C.,
            Wan,D. and Gu,J.
  TITLE     Molecular cloning and characterization of the human ASB-8 gene
            encoding a novel member of ankyrin repeat and SOCS box containing
            protein family
  JOURNAL   Biochem Biophys Res Commun 300 (4), 972-979 (2003)
   PUBMED   12559969
  REMARK    GeneRIF: molecular cloning and characterization of the human ASB-8
            gene
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Kile,B.T., Schulman,B.A., Alexander,W.S., Nicola,N.A., Martin,H.M.
            and Hilton,D.J.
  TITLE     The SOCS box: a tale of destruction and degradation
  JOURNAL   Trends Biochem Sci 27 (5), 235-241 (2002)
   PUBMED   12076535
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM837218.1, BC001321.1 and AF464877.1.
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' UTR compared to variant 1. Variants 1, 2, and 3 encode the same
            isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.215110.1,
                                           SRR1163655.98531.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317697.8/ ENSP00000320893.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..288
                     /product="ankyrin repeat and SOCS box protein 8 isoform a"
                     /note="ankyrin repeat and SOCS box protein 8"
                     /calculated_mol_wt=31511
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32298923; propagated from
                     UniProtKB/Swiss-Prot (Q9H765.1)"
     Region          <26..>188
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          52..81
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H765.1)"
     Region          56..83
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(58..59,62..64,66..67,71,74,83,85,87,91..92,95..96,
                     98..99,103,106,115,117,119,123..124,127..129,131..132,136,
                     139,148)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          85..115
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          85..113
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H765.1)"
     Region          117..148
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          117..146
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H765.1)"
     Region          150..181
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          150..179
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H765.1)"
     Region          245..287
                     /region_name="SOCS_ASB8"
                     /note="SOCS (suppressors of cytokine signaling) box of
                     ASB8-like proteins. ASB family members have a C-terminal
                     SOCS box and an N-terminal ankyrin-related sequence. Human
                     ASB8 is highly transcribed in skeletal muscle and in lung
                     carcinoma cell lines. The...; cd03727"
                     /db_xref="CDD:239697"
     Site            order(246..251,257,268,274,279)
                     /site_type="other"
                     /note="putative elongin B/C interaction [polypeptide
                     binding]"
                     /db_xref="CDD:239697"
     CDS             1..288
                     /gene="ASB8"
                     /gene_synonym="PP14212"
                     /coded_by="NM_024095.5:91..957"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8761.1"
                     /db_xref="GeneID:140461"
                     /db_xref="HGNC:HGNC:17183"
                     /db_xref="MIM:615053"
ORIGIN      
        1 msssmwyimq siqskyslse rlirtiaair sfphdnvedl irggadvnct hgtlkplhca
       61 cmvsdadcve lllekgaevn aldgynrtal hyaaekdeac vevlleygan pnaldgnrdt
      121 plhwaafknn aecvralles gasvnaldyn ndtplswaam kgnlesvsil ldygaevrvi
      181 nligqtpisr lvallvrglg tekedscfel lhravghfel rkngtmprev ardpqlcekl
      241 tvlcsapgtl ktlaryavrr slglqylpda vkglplpasl keylllle
//
LOCUS       NP_056392                980 aa            linear   PRI 27-APR-2025
DEFINITION  ankycorbin isoform a [Homo sapiens].
ACCESSION   NP_056392
VERSION     NP_056392.2
DBSOURCE    REFSEQ: accession NM_015577.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Jeong,W., Kwon,H., Park,S.K., Lee,I.S. and Jho,E.H.
  TITLE     Retinoic acid-induced protein 14 links mechanical forces to Hippo
            signaling
  JOURNAL   EMBO Rep 25 (9), 4033-4061 (2024)
   PUBMED   39160347
  REMARK    GeneRIF: Retinoic acid-induced protein 14 links mechanical forces
            to Hippo signaling.
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cui,R., Zou,J., Zhao,Y., Zhao,T., Ren,L. and Li,Y.
  TITLE     The dual-crosslinked prospective values of RAI14 for the diagnosis
            and chemosurveillance in triple negative breast cancer
  JOURNAL   Ann Med 55 (1), 820-836 (2023)
   PUBMED   36880986
  REMARK    GeneRIF: The dual-crosslinked prospective values of RAI14 for the
            diagnosis and chemosurveillance in triple negative breast cancer.
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Zhang,R., Hu,M., Chen,H.N., Wang,X., Xia,Z., Liu,Y., Wang,R.,
            Xia,X., Shu,Y., Du,D., Meng,W., Qi,S., Li,Y., Xu,H., Zhou,Z.G. and
            Dai,L.
  TITLE     Phenotypic Heterogeneity Analysis of APC-Mutant Colon Cancer by
            Proteomics and Phosphoproteomics Identifies RAI14 as a Key
            Prognostic Determinant in East Asians and Westerners
  JOURNAL   Mol Cell Proteomics 22 (5), 100532 (2023)
   PUBMED   36934880
  REMARK    GeneRIF: Phenotypic Heterogeneity Analysis of APC-Mutant Colon
            Cancer by Proteomics and Phosphoproteomics Identifies RAI14 as a
            Key Prognostic Determinant in East Asians and Westerners.
REFERENCE   4  (residues 1 to 980)
  AUTHORS   Yang,Q., Yan,D., Zou,C., Xue,Q., Lin,S., Huang,Q., Li,X., Tang,D.,
            Chen,X. and Liu,J.
  TITLE     The deubiquitinating enzyme STAMBP is a newly discovered driver of
            triple-negative breast cancer progression that maintains RAI14
            protein stability
  JOURNAL   Exp Mol Med 54 (11), 2047-2059 (2022)
   PUBMED   36434041
  REMARK    GeneRIF: The deubiquitinating enzyme STAMBP is a newly discovered
            driver of triple-negative breast cancer progression that maintains
            RAI14 protein stability.
REFERENCE   5  (residues 1 to 980)
  AUTHORS   Arnett,D.K., Li,N., Tang,W., Rao,D.C., Devereux,R.B., Claas,S.A.,
            Kraemer,R. and Broeckel,U.
  TITLE     Genome-wide association study identifies single-nucleotide
            polymorphism in KCNB1 associated with left ventricular mass in
            humans: the HyperGEN Study
  JOURNAL   BMC Med Genet 10, 43 (2009)
   PUBMED   19454037
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 980)
  AUTHORS   Kutty,R.K., Chen,S., Samuel,W., Vijayasarathy,C., Duncan,T.,
            Tsai,J.Y., Fariss,R.N., Carper,D., Jaworski,C. and Wiggert,B.
  TITLE     Cell density-dependent nuclear/cytoplasmic localization of NORPEG
            (RAI14) protein
  JOURNAL   Biochem Biophys Res Commun 345 (4), 1333-1341 (2006)
   PUBMED   16729964
  REMARK    GeneRIF: Subcellular localization of NORPEG in retinal pigment
            epithelial (ARPE-19) cells varies with cell density, with
            predominantly nuclear localization in nonconfluent cells, but a
            cytoplasmic localization in confluent cultures.
REFERENCE   7  (residues 1 to 980)
  AUTHORS   Yuan,W., Zheng,Y., Huo,R., Lu,L., Huang,X.Y., Yin,L.L., Li,J.M.,
            Zhou,Z.M. and Sha,J.H.
  TITLE     Expression of a novel alternative transcript of the novel retinal
            pigment epithelial cell gene NORPEG in human testes
  JOURNAL   Asian J Androl 7 (3), 277-288 (2005)
   PUBMED   16110356
REFERENCE   8  (residues 1 to 980)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 980)
  AUTHORS   Kutty,R.K., Kutty,G., Samuel,W., Duncan,T., Bridges,C.C.,
            El-Sherbeeny,A., Nagineni,C.N., Smith,S.B. and Wiggert,B.
  TITLE     Molecular characterization and developmental expression of NORPEG,
            a novel gene induced by retinoic acid
  JOURNAL   J Biol Chem 276 (4), 2831-2840 (2001)
   PUBMED   11042181
REFERENCE   10 (residues 1 to 980)
  AUTHORS   Peng,Y.F., Mandai,K., Sakisaka,T., Okabe,N., Yamamoto,Y.,
            Yokoyama,S., Mizoguchi,A., Shiozaki,H., Monden,M. and Takai,Y.
  TITLE     Ankycorbin: a novel actin cytoskeleton-associated protein
  JOURNAL   Genes Cells 5 (12), 1001-1008 (2000)
   PUBMED   11168586
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA485361.1, AF155135.1 and BC028681.1.
            
            On Mar 11, 2009 this sequence version replaced NP_056392.1.
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (a). Variants 1-3 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052988.1, SRR1660809.229465.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265109.8/ ENSP00000265109.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..980
                     /product="ankycorbin isoform a"
                     /note="novel retinal pigment epithelial cell protein;
                     ankycorbin; ankyrin repeat and coiled-coil
                     structure-containing protein; retinoic acid-induced
                     protein 14"
                     /calculated_mol_wt=109911
     Region          1..248
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          18..51
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          23..50
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          52..83
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          52..81
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          85..114
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          86..116
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(118,120,124..125,128..130,132..133,137,140,149,151,
                     153,157..158,161..163,165..166,170,173,182,184,186,
                     190..191,194..196,198..199,203,206,215)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          118..149
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          118..147
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          151..182
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          151..180
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          184..215
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          184..213
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          217..247
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          247..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          270..276
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000305|PubMed:16729964"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EP71; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5U312; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          387..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          <430..>946
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EP71; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     CDS             1..980
                     /gene="RAI14"
                     /gene_synonym="NORPEG; RAI13"
                     /coded_by="NM_015577.3:197..3139"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34142.1"
                     /db_xref="GeneID:26064"
                     /db_xref="HGNC:HGNC:14873"
                     /db_xref="MIM:606586"
ORIGIN      
        1 mkslkakfrk sdtnewnknd drllqaveng daekvasllg kkgasatkhd segktafhla
       61 aakghveclr vmithgvdvt aqdttghsal hlaaknshhe cirkllqskc paesvdssgk
      121 talhyaaaqg clqavqilce hkspinlkdl dgniplllav qnghseichf lldhgadvns
      181 rnksgrtalm laceigssna vealikkgad lnlvdslgyn alhysklsen agiqslllsk
      241 isqdadlktp tkpkqhdqvs kissersgtp kkrkappppi sptqlsdvss prsitstpls
      301 gkesvffaep pfkaeissir enkdrlsdst tgadslldis seadqqdlls llqakvaslt
      361 lhnkelqdkl qakspkeaea dlsfdsyhst qtdlgpslgk pgetsppdsk sspsvlihsl
      421 gksttdndvr iqqlqeilqd lqkrlessea erkqlqvelq srraelvcln nteisenssd
      481 lsqklketqs kyeeamkevl svqkqmklgl vspesmdnys hfhelrvtee einvlkqdlq
      541 naleesernk ekvreleekl verekgtvik ppveeyeemk ssycsvienm nkekaflfek
      601 yqeaqeeimk lkdtlksqmt qeasdeaedm keamnrmide lnkqvselsq lykeaqaele
      661 dyrkrksled vtaeyihkae heklmqltnv srakaedals emksqyskvl neltqlkqlv
      721 daqkensvsi tehlqvittl rtaakemeek isnlkehlas kevevaklek qlleekaamt
      781 damvprssye klqsslesev svlasklkes vkekekvhse vvqirsevsq vkrekeniqt
      841 llkskeqevn ellqkfqqaq eelaemkrya essskleedk dkkinemske vtklkealns
      901 lsqlsystss skrqsqqlea lqqqvkqlqn qlaeckkqhq evisvyrmhl lyavqgqmde
      961 dvqkvlkqil tmcknqsqkk
//
LOCUS       NP_061137                655 aa            linear   PRI 27-APR-2025
DEFINITION  sphingomyelin phosphodiesterase 3 [Homo sapiens].
ACCESSION   NP_061137 NP_078979
VERSION     NP_061137.1
DBSOURCE    REFSEQ: accession NM_018667.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Schempp,R., Eilts,J., Schol,M., Grijalva Yepez,M.F., Fekete,A.,
            Wigger,D., Schumacher,F., Kleuser,B., van Ham,M., Jansch,L.,
            Sauer,M. and Avota,E.
  TITLE     The Role of Neutral Sphingomyelinase-2 (NSM2) in the Control of
            Neutral Lipid Storage in T Cells
  JOURNAL   Int J Mol Sci 25 (6), 3247 (2024)
   PUBMED   38542220
  REMARK    GeneRIF: The Role of Neutral Sphingomyelinase-2 (NSM2) in the
            Control of Neutral Lipid Storage in T Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 655)
  AUTHORS   El-Amouri,S., Karakashian,A., Bieberich,E. and
            Nikolova-Karakashian,M.
  TITLE     Regulated translocation of neutral sphingomyelinase-2 to the plasma
            membrane drives insulin resistance in steatotic hepatocytes
  JOURNAL   J Lipid Res 64 (10), 100435 (2023)
   PUBMED   37640282
  REMARK    GeneRIF: Regulated translocation of neutral sphingomyelinase-2 to
            the plasma membrane drives insulin resistance in steatotic
            hepatocytes.
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Pavlic,A., Poelman,H., Wasilewski,G., Wichapong,K., Lux,P.,
            Maassen,C., Lutgens,E., Schurgers,L.J., Reutelingsperger,C.P. and
            Nicolaes,G.A.F.
  TITLE     Inhibition of Neutral Sphingomyelinase 2 by Novel Small Molecule
            Inhibitors Results in Decreased Release of Extracellular Vesicles
            by Vascular Smooth Muscle Cells and Attenuated Calcification
  JOURNAL   Int J Mol Sci 24 (3), 2027 (2023)
   PUBMED   36768348
  REMARK    GeneRIF: Inhibition of Neutral Sphingomyelinase 2 by Novel Small
            Molecule Inhibitors Results in Decreased Release of Extracellular
            Vesicles by Vascular Smooth Muscle Cells and Attenuated
            Calcification.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Zietzer,A., Jahnel,A.L., Bulic,M., Gutbrod,K., Dusing,P.,
            Hosen,M.R., Dormann,P., Werner,N., Nickenig,G. and Jansen,F.
  TITLE     Activation of neutral sphingomyelinase 2 through hyperglycemia
            contributes to endothelial apoptosis via vesicle-bound
            intercellular transfer of ceramides
  JOURNAL   Cell Mol Life Sci 79 (1), 48 (2021)
   PUBMED   34951654
  REMARK    GeneRIF: Activation of neutral sphingomyelinase 2 through
            hyperglycemia contributes to endothelial apoptosis via
            vesicle-bound intercellular transfer of ceramides.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Kalinichenko,L.S., Muhle,C., Jia,T., Anderheiden,F., Datz,M.,
            Eberle,A.L., Eulenburg,V., Granzow,J., Hofer,M., Hohenschild,J.,
            Huber,S.E., Kampf,S., Kogias,G., Lacatusu,L., Lugmair,C.,
            Taku,S.M., Meixner,D., Tesch,N., Praetner,M., Rhein,C., Sauer,C.,
            Scholz,J., Ulrich,F., Valenta,F., Weigand,E., Werner,M., Tay,N., Mc
            Veigh,C.J., Haase,J., Wang,A.L., Abdel-Hafiz,L., Huston,J.P.,
            Smaga,I., Frankowska,M., Filip,M., Lourdusamy,A., Kirchner,P.,
            Ekici,A.B., Marx,L.M., Suresh,N.P., Frischknecht,R., Fejtova,A.,
            Saied,E.M., Arenz,C., Bozec,A., Wank,I., Kreitz,S., Hess,A.,
            Bauerle,T., Ledesma,M.D., Mitroi,D.N., Miranda,A.M., Oliveira,T.G.,
            Gulbins,E., Lenz,B., Schumann,G., Kornhuber,J. and Muller,C.P.
  TITLE     Neutral sphingomyelinase mediates the co-morbidity trias of alcohol
            abuse, major depression and bone defects
  JOURNAL   Mol Psychiatry 26 (12), 7403-7416 (2021)
   PUBMED   34584229
  REMARK    GeneRIF: Neutral sphingomyelinase mediates the co-morbidity trias
            of alcohol abuse, major depression and bone defects.
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Marchesini,N., Osta,W., Bielawski,J., Luberto,C., Obeid,L.M. and
            Hannun,Y.A.
  TITLE     Role for mammalian neutral sphingomyelinase 2 in confluence-induced
            growth arrest of MCF7 cells
  JOURNAL   J Biol Chem 279 (24), 25101-25111 (2004)
   PUBMED   15051724
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Miura,Y., Gotoh,E., Nara,F., Nishijima,M. and Hanada,K.
  TITLE     Hydrolysis of sphingosylphosphocholine by neutral sphingomyelinases
  JOURNAL   FEBS Lett 557 (1-3), 288-292 (2004)
   PUBMED   14741383
  REMARK    Erratum:[FEBS Lett. 2004 May 7;565(1-3):207]
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Marchesini,N., Luberto,C. and Hannun,Y.A.
  TITLE     Biochemical properties of mammalian neutral sphingomyelinase 2 and
            its role in sphingolipid metabolism
  JOURNAL   J Biol Chem 278 (16), 13775-13783 (2003)
   PUBMED   12566438
  REMARK    GeneRIF: nSMase2 is a structural gene for nSMase, acts as a bona
            fide N-SMase in cells, and has a role in the regulation of cell
            growth and cell signaling
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Chagnon,P., Michaud,J., Mitchell,G., Mercier,J., Marion,J.F.,
            Drouin,E., Rasquin-Weber,A., Hudson,T.J. and Richter,A.
  TITLE     A missense mutation (R565W) in cirhin (FLJ14728) in North American
            Indian childhood cirrhosis
  JOURNAL   Am J Hum Genet 71 (6), 1443-1449 (2002)
   PUBMED   12417987
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Hofmann,K., Tomiuk,S., Wolff,G. and Stoffel,W.
  TITLE     Cloning and characterization of the mammalian brain-specific,
            Mg2+-dependent neutral sphingomyelinase
  JOURNAL   Proc Natl Acad Sci U S A 97 (11), 5895-5900 (2000)
   PUBMED   10823942
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099521.2, AK289651.1 and BC112238.1.
            
            On Apr 12, 2004 this sequence version replaced NP_078979.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK289651.1, BC041828.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153946 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219334.10/ ENSP00000219334.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..655
                     /product="sphingomyelin phosphodiesterase 3"
                     /EC_number="3.1.4.12"
                     /note="neutral sphingomyelinase 2; nSMase-2; neutral
                     sphingomyelinase II"
                     /calculated_mol_wt=70950
     Region          171..>321
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJY3; propagated from
                     UniProtKB/Swiss-Prot (Q9NY59.1)"
     Region          210..319
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY59.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NY59.1)"
     Region          338..646
                     /region_name="nSMase"
                     /note="Neutral sphingomyelinases (nSMase) catalyze the
                     hydrolysis of sphingomyelin in biological membranes to
                     ceramide and phosphorylcholine; cd09078"
                     /db_xref="CDD:197312"
     Site            order(364,406,461,510,512,607,638..639)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197312"
     Site            order(364,638..639)
                     /site_type="other"
                     /note="phosphate binding site [ion binding]"
                     /db_xref="CDD:197312"
     Site            order(366,368,403..404)
                     /site_type="metal-binding"
                     /note="metal binding site C [ion binding]"
                     /db_xref="CDD:197312"
     Site            order(510,512,639)
                     /site_type="metal-binding"
                     /note="metal binding site B [ion binding]"
                     /db_xref="CDD:197312"
     Site            512
                     /site_type="other"
                     /note="Important for substrate recognition.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9NY59.1)"
     CDS             1..655
                     /gene="SMPD3"
                     /gene_synonym="NSMASE2"
                     /coded_by="NM_018667.4:425..2392"
                     /db_xref="CCDS:CCDS10867.1"
                     /db_xref="GeneID:55512"
                     /db_xref="HGNC:HGNC:14240"
                     /db_xref="MIM:605777"
ORIGIN      
        1 mvlyttpfpn sclsalhcvs walifpcywl vdrlaasfip ttyekrqrad dpcclqllct
       61 alftpiylal lvaslpfafl gflfwsplqs arrpyiysrl edkglaggaa llsewkgtgp
      121 gksfcfatan vcllpdslar vnnlfntqar akeigqrirn gaarpqikiy idsptntsis
      181 aasfsslvsp qggdgvarav pgsikrtasv eykgdggrhp gdeaangpas gdpvdssspe
      241 dacivrigge eggrppeadd pvpggqarng agggprgqtp nhnqqdgdsg slgspsasre
      301 slvkgragpd tsasgepgan skllykasvv kkaaarrrrh pdeafdhevs affpanldfl
      361 clqevfdkra atklkeqlhg yfeyilydvg vygcqgccsf kclnsgllfa srypimdvay
      421 hcypnkcndd alaskgalfl kvqvgstpqd qrivgyiact hlhapqedsa ircgqldllq
      481 dwladfrkst ssssaanpee lvafdvvcgd fnfdncssdd kleqqhslft hyrdpcrlgp
      541 geekpwaigt lldtnglyde dvctpdnlqk vleseegrre ylafptskss gqkgrkellk
      601 gngrridyml haeeglcpdw kaeveefsfi tqlsgltdhl pvamrlmvss geeea
//
LOCUS       NP_056618               1148 aa            linear   ROD 27-APR-2025
DEFINITION  phospholipid-transporting ATPase IB [Mus musculus].
ACCESSION   NP_056618
VERSION     NP_056618.1
DBSOURCE    REFSEQ: accession NM_015803.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1148)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1148)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1148)
  AUTHORS   Collin,G.B., Gogna,N., Chang,B., Damkham,N., Pinkney,J., Hyde,L.F.,
            Stone,L., Naggert,J.K., Nishina,P.M. and Krebs,M.P.
  TITLE     Mouse Models of Inherited Retinal Degeneration with Photoreceptor
            Cell Loss
  JOURNAL   Cells 9 (4), 931 (2020)
   PUBMED   32290105
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1148)
  AUTHORS   Zhang,L., Yang,Y., Li,S., Zhang,S., Zhu,X., Tai,Z., Yang,M.,
            Liu,Y., Guo,X., Chen,B., Jiang,Z., Lu,F. and Zhu,X.
  TITLE     Loss of Tmem30a leads to photoreceptor degeneration
  JOURNAL   Sci Rep 7 (1), 9296 (2017)
   PUBMED   28839191
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1148)
  AUTHORS   Lee,S., Uchida,Y., Wang,J., Matsudaira,T., Nakagawa,T.,
            Kishimoto,T., Mukai,K., Inaba,T., Kobayashi,T., Molday,R.S.,
            Taguchi,T. and Arai,H.
  TITLE     Transport through recycling endosomes requires EHD1 recruitment by
            a phosphatidylserine translocase
  JOURNAL   EMBO J 34 (5), 669-688 (2015)
   PUBMED   25595798
REFERENCE   6  (residues 1 to 1148)
  AUTHORS   Carroll,E.W., Curtis,R.L., Sullivan,D.A. and Melvin,J.L.
  TITLE     Wallerian degeneration in the optic nerve of the wabbler-lethal
            (wl/wl) mouse
  JOURNAL   Brain Res Bull 29 (3-4), 411-418 (1992)
   PUBMED   1382814
REFERENCE   7  (residues 1 to 1148)
  AUTHORS   Bronson,R.T., Sweet,H.O., Spencer,C.A. and Davisson,M.T.
  TITLE     Genetic and age related models of neurodegeneration in mice:
            dystrophic axons
  JOURNAL   J Neurogenet 8 (2), 71-83 (1992)
   PUBMED   1634998
REFERENCE   8  (residues 1 to 1148)
  AUTHORS   Murad,S. and Kishimoto,Y.
  TITLE     Alpha hydroxylation of lignoceric acid to cerebronic acid during
            brain development. Diminished hydroxylase activity in
            myelin-deficient mouse mutants
  JOURNAL   J Biol Chem 250 (15), 5841-5846 (1975)
   PUBMED   1150661
REFERENCE   9  (residues 1 to 1148)
  AUTHORS   Siegel,S.J. and Rauch,H.
  TITLE     Aromatic amino acid metabolism in the wabbler-lethal mouse
  JOURNAL   Biochem Genet 2 (4), 311-318 (1969)
   PUBMED   4388883
REFERENCE   10 (residues 1 to 1148)
  AUTHORS   Luse,S.A., Chenard,C. and Finke,E.H.
  TITLE     The wabbler-lethal mouse. An electron microscopic study of the
            nervous system
  JOURNAL   Arch Neurol 17 (2), 153-161 (1967)
   PUBMED   6028244
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131687.4, AC159320.3, AC126684.4, AC161375.4 and AC123534.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF156550.1, BC137896.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1148
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 31.49 cM"
     Protein         1..1148
                     /product="phospholipid-transporting ATPase IB"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase IB;
                     ATPase class I type 8A member 2; ATPase, class 1, member
                     a; ATPase 8A2, p type; P4-ATPase flippase complex alpha
                     subunit ATP8A2; ATPase 8A2, class I"
                     /calculated_mol_wt=129286
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P98200.1)"
     Region          28..1066
                     /region_name="ATPase-Plipid"
                     /note="phospholipid-translocating P-type ATPase, flippase;
                     TIGR01652"
                     /db_xref="CDD:273734"
     Site            45..66
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98200.1)"
     Site            72..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98200.1)"
     Site            277..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98200.1)"
     Site            324..345
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98200.1)"
     Site            331
                     /site_type="other"
                     /note="Involved in the recognition of the lipid substrate
                     on the exoplasmic side.
                     /evidence=ECO:0000250|UniProtKB:C7EXK4; propagated from
                     UniProtKB/Swiss-Prot (P98200.1)"
     Site            336
                     /site_type="other"
                     /note="Involved in the release of the transported lipid
                     into the cytosolic leaflet.
                     /evidence=ECO:0000250|UniProtKB:C7EXK4; propagated from
                     UniProtKB/Swiss-Prot (P98200.1)"
     Site            order(388..390,529,552..554,618,665..667,755,758,761,781,
                     784)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            838..858
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98200.1)"
     Site            871..890
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98200.1)"
     Site            921..942
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98200.1)"
     Site            957..979
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98200.1)"
     Site            986..1006
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98200.1)"
     Site            1025..1049
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98200.1)"
     CDS             1..1148
                     /gene="Atp8a2"
                     /gene_synonym="agil; Atpc1b; wl"
                     /coded_by="NM_015803.3:233..3679"
                     /db_xref="CCDS:CCDS27174.1"
                     /db_xref="GeneID:50769"
                     /db_xref="MGI:MGI:1354710"
ORIGIN      
        1 msratsvgdq leapariiyl nqshlnkfcd nristakysv ltflprflye qirraanaff
       61 lfiallqqip dvsptgrytt lvplviilti agikeiiedf krhkadnavn kkktivlrng
      121 mwhtimwkev avgdivkvln gqylpadmvl fsssepqgmc yvetanldge tnlkirqgls
      181 httdmqtrdv lmklsgriec egpnrhlydf tgnlhldgks svalgpdqil lrgtqlrntq
      241 wvfgvvvytg hdsklmqnst kaplkrsnve kvtnvqilvl fgillvmalv ssvgalfwng
      301 shggkswyik kmdtnsdnfg ynlltfiily nnlipisllv tlevvkytqa lfinwdmdmy
      361 yiendtpama rtsnlneelg qvkylfsdkt gtltcnimnf kkcsiagvty ghfpelareq
      421 ssddfcrmts ctndscdfnd prllkniedq hptapciqef ltllavchtv vpekdgdeii
      481 yqasspdeaa lvkgakklgf vftgrtpysv iieamgqeqt fgilnvlefs sdrkrmsviv
      541 rlpsgqlrly ckgadnvife rlskdskyme etlchleyfa teglrtlcva yadlseneye
      601 ewlkvyqeas iilkdraqrl eecyeiiekn llllgataie drlqagvpet iatllkaeik
      661 iwvltgdkqe tainigyscr lvsqnmalil lkedsldatr aaitqhctdl gnllgkendv
      721 aliidghtlk yalsfevrrs fldlalscka viccrvsplq kseivdvvkk rvkaitlaig
      781 dgandvgmiq tahvgvgisg negmqatnns dyaiaqfsyl eklllvhgaw synrvtkcil
      841 ycfyknvvly iielwfafvn gfsgqilfer wciglynvif talppftlgi fersctqesm
      901 lrfpqlyrit qnaegfntkv fwghcinalv hslilfwvpm kalehdtpvt sghatdylfv
      961 gnivytyvvv tvclkaglet tawtkfshla vwgsmliwlv ffgvystiwp tipiapdmkg
     1021 qatmvlssay fwlglflvpt acliedvawr aakhtckktl leevqeletk srvmgkamlr
     1081 dsngkrmner drlikrlsrk tpptlfrtgs iqqcvshgya fsqeehgavt qeeivraydt
     1141 tkensrkk
//
LOCUS       NP_001032208             857 aa            linear   PRI 27-APR-2025
DEFINITION  arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1
            isoform 1 [Homo sapiens].
ACCESSION   NP_001032208
VERSION     NP_001032208.1
DBSOURCE    REFSEQ: accession NM_001037131.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Cheng,N., Zhang,H., Zhang,S., Ma,X. and Meng,G.
  TITLE     Crystal structure of the GTP-binding protein-like domain of AGAP1
  JOURNAL   Acta Crystallogr F Struct Biol Commun 77 (Pt 4), 105-112 (2021)
   PUBMED   33830075
  REMARK    GeneRIF: Crystal structure of the GTP-binding protein-like domain
            of AGAP1.
REFERENCE   2  (residues 1 to 857)
  AUTHORS   Lv,Q., Wang,G., Zhang,Y., Shen,A., Tang,J., Sun,Y., Ma,C. and
            Wang,P.
  TITLE     CircAGAP1 promotes tumor progression by sponging miR-15-5p in clear
            cell renal cell carcinoma
  JOURNAL   J Exp Clin Cancer Res 40 (1), 76 (2021)
   PUBMED   33618745
  REMARK    GeneRIF: CircAGAP1 promotes tumor progression by sponging miR-15-5p
            in clear cell renal cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 857)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 857)
  AUTHORS   Tsutsumi,K., Nakamura,Y., Kitagawa,Y., Suzuki,Y., Shibagaki,Y.,
            Hattori,S. and Ohta,Y.
  TITLE     AGAP1 regulates subcellular localization of FilGAP and control
            cancer cell invasion
  JOURNAL   Biochem Biophys Res Commun 522 (3), 676-683 (2020)
   PUBMED   31785816
  REMARK    GeneRIF: AGAP1 regulates subcellular localization of FilGAP and
            control cancer cell invasion.
REFERENCE   5  (residues 1 to 857)
  AUTHORS   Nie,Z., Fei,J., Premont,R.T. and Randazzo,P.A.
  TITLE     The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor
            protein complexes AP-1 and AP-3
  JOURNAL   J Cell Sci 118 (Pt 15), 3555-3566 (2005)
   PUBMED   16079295
  REMARK    GeneRIF: The AGAP1 has been found to associate with the adaptor
            protein complex AP-3 and regulate the function of AP-3 endosomes.
REFERENCE   6  (residues 1 to 857)
  AUTHORS   Wassink,T.H., Piven,J., Vieland,V.J., Jenkins,L., Frantz,R.,
            Bartlett,C.W., Goedken,R., Childress,D., Spence,M.A., Smith,M. and
            Sheffield,V.C.
  TITLE     Evaluation of the chromosome 2q37.3 gene CENTG2 as an autism
            susceptibility gene
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 136B (1), 36-44 (2005)
   PUBMED   15892143
  REMARK    GeneRIF: CENTG2 is an intriguing candidate gene that merits further
            scrutiny for its role in autism.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 857)
  AUTHORS   Meurer,S., Pioch,S., Wagner,K., Muller-Esterl,W. and Gross,S.
  TITLE     AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl
            cyclase
  JOURNAL   J Biol Chem 279 (47), 49346-49354 (2004)
   PUBMED   15381706
  REMARK    GeneRIF: AGAP1 is a novel binding partner of nitric oxide-sensitive
            guanylyl cyclase
REFERENCE   8  (residues 1 to 857)
  AUTHORS   Nie,Z., Boehm,M., Boja,E.S., Vass,W.C., Bonifacino,J.S., Fales,H.M.
            and Randazzo,P.A.
  TITLE     Specific regulation of the adaptor protein complex AP-3 by the Arf
            GAP AGAP1
  JOURNAL   Dev Cell 5 (3), 513-521 (2003)
   PUBMED   12967569
REFERENCE   9  (residues 1 to 857)
  AUTHORS   Xia,C., Ma,W., Stafford,L.J., Liu,C., Gong,L., Martin,J.F. and
            Liu,M.
  TITLE     GGAPs, a new family of bifunctional GTP-binding and
            GTPase-activating proteins
  JOURNAL   Mol Cell Biol 23 (7), 2476-2488 (2003)
   PUBMED   12640130
REFERENCE   10 (residues 1 to 857)
  AUTHORS   Nie,Z., Stanley,K.T., Stauffer,S., Jacques,K.M., Hirsch,D.S.,
            Takei,J. and Randazzo,P.A.
  TITLE     AGAP1, an endosome-associated, phosphoinositide-dependent
            ADP-ribosylation factor GTPase-activating protein that affects
            actin cytoskeleton
  JOURNAL   J Biol Chem 277 (50), 48965-48975 (2002)
   PUBMED   12388557
  REMARK    GeneRIF: overexpression inhibited formation of platelet-derived
            growth factor-induced ruffles and also induced loss of actin stress
            fibers
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012305.7, BC060814.1,
            BC167153.1, BC140856.1, AY033765.1, AK001722.1, AC019047.7 and
            CA446024.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of an ADP-ribosylation factor
            GTPase-activating protein family involved in membrane trafficking
            and cytoskeleton dynamics. This gene functions as a direct
            regulator of the adaptor-related protein complex 3 on endosomes.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Oct 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC140856.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304032.13/ ENSP00000307634.7
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.2"
     Protein         1..857
                     /product="arf-GAP with GTPase, ANK repeat and PH
                     domain-containing protein 1 isoform 1"
                     /EC_number="3.6.5.2"
                     /note="Arf GAP with GTP-binding protein-like, ANK repeat
                     and PH domains 1; centaurin, gamma 2; GTP-binding and
                     GTPase-activating protein 1; arf-GAP with GTPase, ANK
                     repeat and PH domain-containing protein 1"
                     /calculated_mol_wt=94339
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     Region          66..276
                     /region_name="Small GTPase-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     Region          72..229
                     /region_name="Centaurin_gamma"
                     /note="Centaurin gamma (CENTG) GTPase; cd04103"
                     /db_xref="CDD:133303"
     Site            78..85
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133303"
     Site            order(80..86,124,127,178..179,181,211..212)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133303"
     Site            99..107
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133303"
     Site            102
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133303"
     Site            124..127
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133303"
     Site            126..139
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133303"
     Site            178..181
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133303"
     Site            211..213
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133303"
     Region          267..343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     Region          344..592
                     /region_name="PH_AGAP"
                     /note="Arf-GAP with GTPase, ANK repeat and PH
                     domain-containing protein Pleckstrin homology (PH) domain;
                     cd01250"
                     /db_xref="CDD:241281"
     Region          406..449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     Region          496..547
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     Region          609..717
                     /region_name="ArfGap_AGAP2"
                     /note="ArfGAP with GTPase domain, ANK repeat and PH domain
                     2; cd08853"
                     /db_xref="CDD:350078"
     Site            order(624,627,644,647,652)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350078"
     Site            order(624,627,644,647)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350078"
     Site            663
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BXK8; propagated from
                     UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     Region          <736..>825
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(737..738,741..743,745..746,750,753,761,768,770,
                     774..775,778..780,782..783,787,790,799,801,803,807..808,
                     811..813,815..816,820,823)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          768..799
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          768..797
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     Region          801..830
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     Region          801..826
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            836
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPQ3.4)"
     CDS             1..857
                     /gene="AGAP1"
                     /gene_synonym="AGAP-1; CENTG2; cnt-g2; GGAP1"
                     /coded_by="NM_001037131.3:645..3218"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33408.1"
                     /db_xref="GeneID:116987"
                     /db_xref="HGNC:HGNC:16922"
                     /db_xref="MIM:608651"
ORIGIN      
        1 mnyqqqlans aairaeiqrf esvhpniysi yellerveep vlqnqirehv iaiedafvns
       61 qewtlsrsvp elkvgivgnl asgksalvhr yltgtyvqee speggrfkke ivvdgqsyll
      121 lirdeggppe aqfamwvdav ifvfsledei sfqtvyhyys rmanyrntse iplvlvgtqd
      181 aissanprvi ddararklsn dlkrctyyet catyglnver vfqdvaqkiv atrkkqqlsi
      241 gpckslpnsp shssvcsaqv savhisqtsn gggslsdyss svpstpstsq kelridvppt
      301 antptpvrkq skrrsnlfts rkgsdpdkek kglesradsi gsgraipikq gmllkrsgks
      361 lnkewkkkyv tlcdngvlty hpslhdymqn vhgkeidllr ttvkvpgkrp pratsacapi
      421 sspktnglsk dmsslhispn sgnvtsasgs qmasgislvs fnsrpdgmhq rsysvssadq
      481 wseatvians aissdtglgd svcsspsiss ttspkldppp sphanrkkhr rkkstsnfka
      541 dglsgtaeeq eenfefiivs ltgqtwhfea ttyeerdawv qaiesqilas lqscessknk
      601 srltsqseam alqsirnmrg nshcvdcetq npnwaslnlg almciecsgi hrnlgthlsr
      661 vrsldlddwp velikvmssi gnelansvwe essqgrtkps vdstreeker wirakyeqkl
      721 flaplpctel slgqhllrat adedlrtail llahgsrdev netcgegdgr talhlacrkg
      781 nvvlaqlliw ygvdvtarda hgntalayar qassqecidv llqygcpder fvlmatpnls
      841 rrnnnrnnss grvptii
//
LOCUS       NP_003127                504 aa            linear   PRI 27-APR-2025
DEFINITION  signal recognition particle subunit SRP54 isoform 1 [Homo sapiens].
ACCESSION   NP_003127 XP_945638
VERSION     NP_003127.1
DBSOURCE    REFSEQ: accession NM_003136.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   McCarthy,P., Cotter,M. and Smith,O.P.
  TITLE     Autosomal dominant Shwachman-Diamond syndrome with a novel
            heterozygous missense variant in the SRP54 gene causing severe
            phenotypic features
  JOURNAL   Br J Haematol 196 (3), e39-e42 (2022)
   PUBMED   34549814
  REMARK    GeneRIF: Autosomal dominant Shwachman-Diamond syndrome with a novel
            heterozygous missense variant in the SRP54 gene causing severe
            phenotypic features.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Schurch,C., Schaefer,T., Muller,J.S., Hanns,P., Arnone,M.,
            Dumlin,A., Scharer,J., Sinning,I., Wild,K., Skokowa,J., Welte,K.,
            Carapito,R., Bahram,S., Konantz,M. and Lengerke,C.
  TITLE     SRP54 mutations induce congenital neutropenia via dominant-negative
            effects on XBP1 splicing
  JOURNAL   Blood 137 (10), 1340-1352 (2021)
   PUBMED   33227812
  REMARK    GeneRIF: SRP54 mutations induce congenital neutropenia via
            dominant-negative effects on XBP1 splicing.
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Juaire,K.D., Lapouge,K., Becker,M.M.M., Kotova,I., Michelhans,M.,
            Carapito,R., Wild,K., Bahram,S. and Sinning,I.
  TITLE     Structural and Functional Impact of SRP54 Mutations Causing Severe
            Congenital Neutropenia
  JOURNAL   Structure 29 (1), 15-28 (2021)
   PUBMED   33053321
  REMARK    GeneRIF: Structural and Functional Impact of SRP54 Mutations
            Causing Severe Congenital Neutropenia.
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Goldberg,L., Simon,A.J., Rechavi,G., Lev,A., Barel,O., Kunik,V.,
            Toren,A., Schiby,G., Tamary,H., Steinberg-Shemer,O. and Somech,R.
  TITLE     Congenital neutropenia with variable clinical presentation in novel
            mutation of the SRP54 gene
  JOURNAL   Pediatr Blood Cancer 67 (6), e28237 (2020)
   PUBMED   32277798
  REMARK    GeneRIF: Congenital neutropenia with variable clinical presentation
            in novel mutation of the SRP54 gene.
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Wild,K., Juaire,K.D., Soni,K., Shanmuganathan,V., Hendricks,A.,
            Segnitz,B., Beckmann,R. and Sinning,I.
  TITLE     Reconstitution of the human SRP system and quantitative and
            systematic analysis of its ribosome interactions
  JOURNAL   Nucleic Acids Res 47 (6), 3184-3196 (2019)
   PUBMED   30649417
  REMARK    GeneRIF: e show that SRP RNA does not bind to the ribosome, while
            SRP binds with nanomolar affinity involving a two-step mechanism of
            the key-player SRP54. Ultrasensitive binding of SRP68/72 indicates
            avidity by multiple binding sites that are dominated by the
            C-terminus of SRP72
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Gowda,K., Chittenden,K. and Zwieb,C.
  TITLE     Binding site of the M-domain of human protein SRP54 determined by
            systematic site-directed mutagenesis of signal recognition particle
            RNA
  JOURNAL   Nucleic Acids Res 25 (2), 388-394 (1997)
   PUBMED   9016569
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Bacher,G., Lutcke,H., Jungnickel,B., Rapoport,T.A. and
            Dobberstein,B.
  TITLE     Regulation by the ribosome of the GTPase of the signal-recognition
            particle during protein targeting
  JOURNAL   Nature 381 (6579), 248-251 (1996)
   PUBMED   8622769
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Patel,S. and Austen,B.
  TITLE     Sequence of the highly conserved gene encoding the human 54kDa
            subunit of signal recognition particle
  JOURNAL   DNA Seq 6 (3), 167-170 (1996)
   PUBMED   8722571
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Miller,J.D., Wilhelm,H., Gierasch,L., Gilmore,R. and Walter,P.
  TITLE     GTP binding and hydrolysis by the signal recognition particle
            during initiation of protein translocation
  JOURNAL   Nature 366 (6453), 351-354 (1993)
   PUBMED   8247130
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Nelson,A. and Myers,K.
  TITLE     Shwachman-Diamond Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301722
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA495064.1 and BC000652.2.
            
            On Mar 4, 2006 this sequence version replaced XP_945638.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.126494.1,
                                           SRR5189658.194175.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216774.11/ ENSP00000216774.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.2"
     Protein         1..504
                     /product="signal recognition particle subunit SRP54
                     isoform 1"
                     /EC_number="3.6.5.4"
                     /note="signal recognition particle 54 kDa protein; signal
                     recognition particle 54kD; signal recognition particle
                     54kDa; signal recognition particle subunit SRP54"
                     /calculated_mol_wt=55574
     Region          1..295
                     /region_name="NG domain.
                     /evidence=ECO:0000303|PubMed:34020957"
                     /note="propagated from UniProtKB/Swiss-Prot (P61011.1)"
     Region          2..430
                     /region_name="SRP54_euk"
                     /note="signal recognition particle protein SRP54;
                     TIGR01425"
                     /db_xref="CDD:273615"
     Region          296..504
                     /region_name="M-domain.
                     /evidence=ECO:0000303|PubMed:34020957"
                     /note="propagated from UniProtKB/Swiss-Prot (P61011.1)"
     CDS             1..504
                     /gene="SRP54"
                     /gene_synonym="SCN8"
                     /coded_by="NM_003136.4:258..1772"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9652.1"
                     /db_xref="GeneID:6729"
                     /db_xref="HGNC:HGNC:11301"
                     /db_xref="MIM:604857"
ORIGIN      
        1 mvladlgrki tsalrslsna tiineevlna mlkevctall eadvniklvk qlrenvksai
       61 dleemasgln krkmiqhavf kelvklvdpg vkawtptkgk qnvimfvglq gsgktttcsk
      121 layyyqrkgw ktclicadtf ragafdqlkq natkaripfy gsytemdpvi iasegvekfk
      181 nenfeiiivd tsgrhkqeds lfeemlqvan aiqpdnivyv mdasigqace aqakafkdkv
      241 dvasvivtkl dghakgggal savaatkspi ifigtgehid dfepfktqpf iskllgmgdi
      301 eglidkvnel klddnealie klkhgqftlr dmyeqfqnim kmgpfsqilg mipgfgtdfm
      361 skgneqesma rlkklmtimd smndqeldst dgakvfskqp griqrvargs gvstrdvqel
      421 ltqytkfaqm vkkmggikgl fkggdmsknv sqsqmaklnq qmakmmdprv lhhmggmagl
      481 qsmmrqfqqg aagnmkgmmg fnnm
//
LOCUS       NP_001356032             320 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 11 [Homo
            sapiens].
ACCESSION   NP_001356032
VERSION     NP_001356032.1
DBSOURCE    REFSEQ: accession NM_001369103.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.226673.1,
                                           SRR1803612.228129.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..320
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 11"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=36568
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..281
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..320
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369103.1:104..1066"
                     /note="isoform 11 is encoded by transcript variant 24"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefikl qelvdrvler fqasglivke wnsvklhatv
      241 mntlfrkdpn aegrynlyta egkyifkere sfdgrnilks fallprleyn daisahcnlc
      301 lpgssdspas asqvagitvv
//
LOCUS       NP_056299                243 aa            linear   PRI 27-APR-2025
DEFINITION  pre-mRNA-splicing factor SYF2 isoform 1 [Homo sapiens].
ACCESSION   NP_056299
VERSION     NP_056299.1
DBSOURCE    REFSEQ: accession NM_015484.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Tanaka,I., Chakraborty,A., Saulnier,O., Benoit-Pilven,C.,
            Vacher,S., Labiod,D., Lam,E.W.F., Bieche,I., Delattre,O.,
            Pouzoulet,F., Auboeuf,D., Vagner,S. and Dutertre,M.
  TITLE     ZRANB2 and SYF2-mediated splicing programs converging on ECT2 are
            involved in breast cancer cell resistance to doxorubicin
  JOURNAL   Nucleic Acids Res 48 (5), 2676-2693 (2020)
   PUBMED   31943118
  REMARK    GeneRIF: These data identify Aletrnative splicing programs
            controlled by ZRANB2 and SYF2 and converging on ECT2, that
            participate to breast cancer cell resistance to doxorubicin.
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Chen,Z.Y., Liu,H.Y., Jiang,N. and Yuan,J.M.
  TITLE     LncRNA HOST2 enhances gefitinib-resistance in non-small cell lung
            cancer by down-regulating miRNA-621
  JOURNAL   Eur Rev Med Pharmacol Sci 23 (22), 9939-9946 (2019)
   PUBMED   31799663
  REMARK    GeneRIF: LncRNA HOST2 enhances gefitinib-resistance in non-small
            cell lung cancer by down-regulating miRNA-621.
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Bertram,K., Agafonov,D.E., Liu,W.T., Dybkov,O., Will,C.L.,
            Hartmuth,K., Urlaub,H., Kastner,B., Stark,H. and Luhrmann,R.
  TITLE     Cryo-EM structure of a human spliceosome activated for step 2 of
            splicing
  JOURNAL   Nature 542 (7641), 318-323 (2017)
   PUBMED   28076346
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Zhang,S., Shi,W., Chen,Y., Xu,Z., Zhu,J., Zhang,T., Huang,W.,
            Ni,R., Lu,C. and Zhang,X.
  TITLE     Overexpression of SYF2 correlates with enhanced cell growth and
            poor prognosis in human hepatocellular carcinoma
  JOURNAL   Mol Cell Biochem 410 (1-2), 1-9 (2015)
   PUBMED   26260052
  REMARK    GeneRIF: SYF2 might play a regulatory role in the proliferation of
            hepatocellular carcinoma cells.
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Chu,P.C., Yang,Y.C., Lu,Y.T., Chen,H.T., Yu,L.C. and Chang,M.S.
  TITLE     Silencing of p29 affects DNA damage responses with UV irradiation
  JOURNAL   Cancer Res 66 (17), 8484-8491 (2006)
   PUBMED   16951160
  REMARK    GeneRIF: novel function of p29 in the regulation of DNA replication
            checkpoint responses in Hela cells.
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Chang,M.S., Chang,C.L., Huang,C.J. and Yang,Y.C.
  TITLE     p29, a novel GCIP-interacting protein, localizes in the nucleus
  JOURNAL   Biochem Biophys Res Commun 279 (2), 732-737 (2000)
   PUBMED   11118353
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR155437.1, BC010862.1 and
            AL031432.1.
            
            Summary: This gene encodes a nuclear protein that interacts with
            cyclin D-type binding-protein 1, which is thought to be a cell
            cycle regulator at the G1/S transition. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.285144.1,
                                           SRR3476690.1175308.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000236273.9/ ENSP00000236273.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..243
                     /product="pre-mRNA-splicing factor SYF2 isoform 1"
                     /note="GCIP-interacting protein p29; CCNDBP1 interactor;
                     functional spliceosome-associated protein 29;
                     pre-mRNA-splicing factor SYF2; SYF2 homolog, RNA splicing
                     factor"
                     /calculated_mol_wt=28591
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O95926.1)"
     Region          90..238
                     /region_name="SYF2"
                     /note="SYF2 splicing factor; pfam08231"
                     /db_xref="CDD:462400"
     CDS             1..243
                     /gene="SYF2"
                     /gene_synonym="CBPIN; fSAP29; NTC31; P29"
                     /coded_by="NM_015484.5:36..767"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS259.1"
                     /db_xref="GeneID:25949"
                     /db_xref="HGNC:HGNC:19824"
                     /db_xref="MIM:607090"
ORIGIN      
        1 maaiaasevl vdsaeegsla aaaelaaqkr eqrlrkfrel hlmrnearkl nhqevveedk
       61 rlklpanwea kkarlewelk eeekkkecaa rgedyekvkl leisaedaer werkkkrknp
      121 dlgfsdyaaa qlrqyhrltk qikpdmetye rlrekhgeef fptsnsllhg thvpsteeid
      181 rmvidlekqi ekrdkysrrr pynddadidy inernakfnk kaerfygkyt aeikqnlerg
      241 tav
//
LOCUS       NP_000009                655 aa            linear   PRI 27-APR-2025
DEFINITION  very long-chain specific acyl-CoA dehydrogenase, mitochondrial
            isoform 1 precursor [Homo sapiens].
ACCESSION   NP_000009
VERSION     NP_000009.1
DBSOURCE    REFSEQ: accession NM_000018.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Flowers,M., Dickson,A., Miller,M.J., Spector,E., Enns,G.M.,
            Baudet,H., Pasquali,M., Racacho,L., Sadre-Bazzaz,K., Wen,T.,
            Fogarty,M., Fernandez,R., Weaver,M.A., Feigenbaum,A., Graham,B.H.
            and Mao,R.
  TITLE     Specifications of the ACMG/AMP guidelines for ACADVL variant
            interpretation
  JOURNAL   Mol Genet Metab 140 (3), 107668 (2023)
   PUBMED   37549443
  REMARK    GeneRIF: Specifications of the ACMG/AMP guidelines for ACADVL
            variant interpretation.
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Hsu,C.C., Wang,J.S., Shyu,Y.C., Fu,T.C., Juan,Y.H., Yuan,S.S.,
            Wang,C.H., Yeh,C.H., Liao,P.C., Wu,H.Y. and Hsu,P.H.
  TITLE     Hypermethylation of ACADVL is involved in the high-intensity
            interval training-associated reduction of cardiac fibrosis in heart
            failure patients
  JOURNAL   J Transl Med 21 (1), 187 (2023)
   PUBMED   36894992
  REMARK    GeneRIF: Hypermethylation of ACADVL is involved in the
            high-intensity interval training-associated reduction of cardiac
            fibrosis in heart failure patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 655)
  AUTHORS   D'Annibale,O.M., Phua,Y.L., Van't Land,C., Karunanidhi,A.,
            Dorenbaum,A., Mohsen,A.W. and Vockley,J.
  TITLE     Treatment of VLCAD-Deficient Patient Fibroblasts with Peroxisome
            Proliferator-Activated Receptor delta Agonist Improves Cellular
            Bioenergetics
  JOURNAL   Cells 11 (17), 2635 (2022)
   PUBMED   36078043
  REMARK    GeneRIF: Treatment of VLCAD-Deficient Patient Fibroblasts with
            Peroxisome Proliferator-Activated Receptor delta Agonist Improves
            Cellular Bioenergetics.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Prew,M.S., Camara,C.M., Botzanowski,T., Moroco,J.A., Bloch,N.B.,
            Levy,H.R., Seo,H.S., Dhe-Paganon,S., Bird,G.H., Herce,H.D.,
            Gygi,M.A., Escudero,S., Wales,T.E., Engen,J.R. and Walensky,L.D.
  TITLE     Structural basis for defective membrane targeting of mutant enzyme
            in human VLCAD deficiency
  JOURNAL   Nat Commun 13 (1), 3669 (2022)
   PUBMED   35760926
  REMARK    GeneRIF: Structural basis for defective membrane targeting of
            mutant enzyme in human VLCAD deficiency.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 655)
  AUTHORS   D'Annibale,O.M., Koppes,E.A., Sethuraman,M., Bloom,K., Mohsen,A.W.
            and Vockley,J.
  TITLE     Characterization of exonic variants of uncertain significance in
            very long-chain acyl-CoA dehydrogenase identified through newborn
            screening
  JOURNAL   J Inherit Metab Dis 45 (3), 529-540 (2022)
   PUBMED   35218577
  REMARK    GeneRIF: Characterization of exonic variants of uncertain
            significance in very long-chain acyl-CoA dehydrogenase identified
            through newborn screening.
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Strauss,A.W., Powell,C.K., Hale,D.E., Anderson,M.M., Ahuja,A.,
            Brackett,J.C. and Sims,H.F.
  TITLE     Molecular basis of human mitochondrial very-long-chain acyl-CoA
            dehydrogenase deficiency causing cardiomyopathy and sudden death in
            childhood
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10496-10500 (1995)
   PUBMED   7479827
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Aoyama,T., Souri,M., Ueno,I., Kamijo,T., Yamaguchi,S., Rhead,W.J.,
            Tanaka,K. and Hashimoto,T.
  TITLE     Cloning of human very-long-chain acyl-coenzyme A dehydrogenase and
            molecular characterization of its deficiency in two patients
  JOURNAL   Am J Hum Genet 57 (2), 273-283 (1995)
   PUBMED   7668252
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Aoyama,T., Souri,M., Ushikubo,S., Kamijo,T., Yamaguchi,S.,
            Kelley,R.I., Rhead,W.J., Uetake,K., Tanaka,K. and Hashimoto,T.
  TITLE     Purification of human very-long-chain acyl-coenzyme A dehydrogenase
            and characterization of its deficiency in seven patients
  JOURNAL   J Clin Invest 95 (6), 2465-2473 (1995)
   PUBMED   7769092
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Aoyama,T., Uchida,Y., Kelley,R.I., Marble,M., Hofman,K.,
            Tonsgard,J.H., Rhead,W.J. and Hashimoto,T.
  TITLE     A novel disease with deficiency of mitochondrial very-long-chain
            acyl-CoA dehydrogenase
  JOURNAL   Biochem Biophys Res Commun 191 (3), 1369-1372 (1993)
   PUBMED   8466512
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Leslie,N.D. and Saenz-Ayala,S.
  TITLE     Very Long-Chain Acyl-Coenzyme A Dehydrogenase Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301763
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC000399.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is targeted to the inner
            mitochondrial membrane where it catalyzes the first step of the
            mitochondrial fatty acid beta-oxidation pathway. This acyl-Coenzyme
            A dehydrogenase is specific to long-chain and very-long-chain fatty
            acids. A deficiency in this gene product reduces myocardial fatty
            acid beta-oxidation and is associated with cardiomyopathy.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000399.2, SRR3476690.1110131.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000356839.10/
                                                  ENSP00000349297.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..655
                     /product="very long-chain specific acyl-CoA dehydrogenase,
                     mitochondrial isoform 1 precursor"
                     /EC_number="1.3.8.9"
                     /note="acyl-Coenzyme A dehydrogenase, very long chain;
                     very long-chain specific acyl-CoA dehydrogenase,
                     mitochondrial"
                     /calculated_mol_wt=66176
     transit_peptide 1..40
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:7668252,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
                     /calculated_mol_wt=4233
     Region          23..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49748.1)"
     mat_peptide     41..655
                     /product="Very long-chain specific acyl-CoA dehydrogenase,
                     mitochondrial. /id=PRO_0000000515"
                     /note="propagated from UniProtKB/Swiss-Prot (P49748.1)"
                     /calculated_mol_wt=66176
     Region          41..482
                     /region_name="Catalytic.
                     /evidence=ECO:0000305|PubMed:18227065"
                     /note="propagated from UniProtKB/Swiss-Prot (P49748.1)"
     Site            51
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50544; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Site            71
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P50544; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Region          72..481
                     /region_name="VLCAD"
                     /note="Very long chain acyl-CoA dehydrogenase; cd01161"
                     /db_xref="CDD:173850"
     Site            order(214,216..217,222..223,249,251,457,464,466)
                     /site_type="other"
                     /note="FAD binding site [chemical binding]"
                     /db_xref="CDD:173850"
     Site            order(223,330,337..338,341,461..462)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:173850"
     Site            239
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Site            276
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P50544; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Site            278
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P50544; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Site            298
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50544; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Site            331
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Site            462
                     /site_type="active"
                     /note="catalytic base [active]"
                     /db_xref="CDD:173850"
     Site            482
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P50544; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Region          483..516
                     /region_name="Membrane-anchoring.
                     /evidence=ECO:0000305|PubMed:18227065"
                     /note="propagated from UniProtKB/Swiss-Prot (P49748.1)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Site            550
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50544; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     Site            556
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P50544; propagated from
                     UniProtKB/Swiss-Prot (P49748.1)"
     CDS             1..655
                     /gene="ACADVL"
                     /gene_synonym="ACAD6; LCACD; VLCAD"
                     /coded_by="NM_000018.4:48..2015"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS11090.1"
                     /db_xref="GeneID:37"
                     /db_xref="HGNC:HGNC:92"
                     /db_xref="MIM:609575"
ORIGIN      
        1 mqaarmaasl grqllrlggg ssrltallgq prpgparrpy aggaaqlald ksdshpsdal
       61 trkkpakaes ksfavgmfkg qlttdqvfpy psvlneeqtq flkelvepvs rffeevndpa
      121 kndalemvee ttwqglkelg afglqvpsel ggvglcntqy arlveivgmh dlgvgitlga
      181 hqsigfkgil lfgtkaqkek ylpklasget vaafclteps sgsdaasirt savpspcgky
      241 ytlngsklwi snggladift vfaktpvtdp atgavkekit afvvergfgg ithgppekkm
      301 gikasntaev ffdgvrvpse nvlgevgsgf kvamhilnng rfgmaaalag tmrgiiakav
      361 dhatnrtqfg ekihnfgliq eklarmvmlq yvtesmaymv sanmdqgatd fqieaaiski
      421 fgseaawkvt deciqimggm gfmkepgver vlrdlrifri fegtndilrl fvalqgcmdk
      481 gkelsglgsa lknpfgnagl llgeagkqlr rraglgsgls lsglvhpels rsgelavral
      541 eqfatvveak likhkkgivn eqfllqrlad gaidlyamvv vlsrasrsls eghptaqhek
      601 mlcdtwciea aariregmaa lqsdpwqqel yrnfksiska lverggvvts nplgf
//
LOCUS       NP_001348414            1290 aa            linear   ROD 27-APR-2025
DEFINITION  cleavage and polyadenylation specificity factor subunit 1 isoform 3
            [Mus musculus].
ACCESSION   NP_001348414 XP_006521666
VERSION     NP_001348414.1
DBSOURCE    REFSEQ: accession NM_001361485.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1290)
  AUTHORS   Quille,M.L., Carat,S., Quemener-Redon,S., Hirchaud,E., Baron,D.,
            Benech,C., Guihot,J., Placet,M., Mignen,O., Ferec,C., Houlgatte,R.
            and Friocourt,G.
  TITLE     High-throughput analysis of promoter occupancy reveals new targets
            for Arx, a gene mutated in mental retardation and
            interneuronopathies
  JOURNAL   PLoS One 6 (9), e25181 (2011)
   PUBMED   21966449
REFERENCE   2  (residues 1 to 1290)
  AUTHORS   Nakanishi,T., Kumagai,S., Kimura,M., Watanabe,H., Sakurai,T.,
            Kimura,M., Kashiwabara,S. and Baba,T.
  TITLE     Disruption of mouse poly(A) polymerase mGLD-2 does not alter
            polyadenylation status in oocytes and somatic cells
  JOURNAL   Biochem Biophys Res Commun 364 (1), 14-19 (2007)
   PUBMED   17927953
REFERENCE   3  (residues 1 to 1290)
  AUTHORS   Dass,B., Attaya,E.N., Michelle Wallace,A. and MacDonald,C.C.
  TITLE     Overexpression of the CstF-64 and CPSF-160 polyadenylation protein
            messenger RNAs in mouse male germ cells
  JOURNAL   Biol Reprod 64 (6), 1722-1729 (2001)
   PUBMED   11369601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC056388.1 and BC049941.1.
            
            On Mar 28, 2018 this sequence version replaced XP_006521666.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC049941.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1290
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 36.13 cM"
     Protein         1..1290
                     /product="cleavage and polyadenylation specificity factor
                     subunit 1 isoform 3"
                     /EC_number="2.4.2.30"
                     /note="cleavage and polyadenylation specificity factor
                     subunit 1; CPSF 160 kDa subunit; cleavage and
                     polyadenylation specificity factor 160 kDa subunit"
                     /calculated_mol_wt=143751
     Region          36..1284
                     /region_name="SFT1"
                     /note="Pre-mRNA cleavage and polyadenylation specificity
                     factor [RNA processing and modification]; COG5161"
                     /db_xref="CDD:227490"
     CDS             1..1290
                     /gene="Cpsf1"
                     /gene_synonym="CPSF160"
                     /coded_by="NM_001361485.1:491..4363"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:94230"
                     /db_xref="MGI:MGI:2679722"
ORIGIN      
        1 mliygtrlvv lpfrreslae eheglmgegq rssflpsyii dvraldekll niidlqflhg
       61 yyeptllilf epnqtwpgrv avrqdtcsiv aislnitqkv hpviwsltsl pfdctqalav
      121 pkpiggvvif avnsllylnq svppygvaln slttgttafp lrtqegvrit ldcaqaafis
      181 ydkmvislkg geiyvltlit dgmrsvrafh fdkaaasvlt tsmvtmepgy lflgsrlgns
      241 lllkyteklq eppassvrea adkeeppskk krvepavgwt ggktvpqdev deievygsea
      301 qsgtqlatys fevcdsmlni gpcanaavge paflseefqn spepdleivv csgygkngal
      361 svlqksirpq vvttfelpgc ydmwtviapv rkeeeetpka esteqepsap kaeedgrrhg
      421 flilsredst milqtgqeim eldtsgfatq gptvfagnig dnryivqvsp lgirllegvn
      481 qlhfipvdlg apivqcavad pyvvimsaeg hvtmfllksd syggrhhrla lhkpplhhqs
      541 kvialclyrd vsgmfttesr lggardelgg rsgseaeglg setsptvdde eemlygdssa
      601 lfspskeear rssqppadrd papfkadpth wcllvrengt meiyqlpdwr lvflvknfpv
      661 gqrvlvdssf gqpttqgevr keeatrqgel plvkevllva lgsrqsrpyl lvhvdqelli
      721 yeafphdsql gqgnlkvrfk kvphninfre kkpkpskkka egcsteegsg grgrvarfry
      781 fediygysgv ficgpsphwl lvtgrgalrl hpmgidgpid sfapfhnvnc prgflyfnrq
      841 gelrisvlpa ylsydapwpv rkiplrctah yvayhveskv yavatstntp ctriprmtge
      901 ekefeaierd dryihpqqea fsiqlispvs weaipnarie leewehvtcm ktvslrseet
      961 vsglkgyvaa gtclmqgeev tcrgrilimd vievvpepgq pltknkfkvl yekeqkgpvt
     1021 alchcnghlv saigqkiflw slraseltgm afidtqlyih qmisvknfil aadvmksisl
     1081 lryqeesktl slvsrdakpl evysvdfmvd naqlgflvsd rdrnlmvymy lpeakesfgg
     1141 mrllrradfh vgahvntfwr tpcrgaaegp skksvvwenk hitwfatldg giglllpmqe
     1201 ktyrrllmlq nalttmlphh aglnprafrm lhvdrrilqn avrnvldgel lnrylylstm
     1261 erselakkig ttpdiilddl letdrvtahf
//
LOCUS       NP_084257                957 aa            linear   ROD 27-APR-2025
DEFINITION  ADAMTS-like protein 2 precursor [Mus musculus].
ACCESSION   NP_084257 XP_130065
VERSION     NP_084257.1
DBSOURCE    REFSEQ: accession NM_029981.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 957)
  AUTHORS   Iwanaga,Y., Tsuji,K., Nishimura,A., Tateishi,K., Kakiuchi,M. and
            Tsuji,T.
  TITLE     A nonsense mutation in mouse Adamtsl2 causes uterine hypoplasia and
            an irregular estrous cycle
  JOURNAL   Mamm Genome 34 (4), 559-571 (2023)
   PUBMED   37656189
  REMARK    GeneRIF: A nonsense mutation in mouse Adamtsl2 causes uterine
            hypoplasia and an irregular estrous cycle.
REFERENCE   2  (residues 1 to 957)
  AUTHORS   Taye,N., Singh,M., Baldock,C. and Hubmacher,D.
  TITLE     Secreted ADAMTS-like 2 promotes myoblast differentiation by
            potentiating WNT signaling
  JOURNAL   Matrix Biol 120, 24-42 (2023)
   PUBMED   37187448
  REMARK    GeneRIF: Secreted ADAMTS-like 2 promotes myoblast differentiation
            by potentiating WNT signaling.
REFERENCE   3  (residues 1 to 957)
  AUTHORS   Rypdal,K.B., Erusappan,P.M., Melleby,A.O., Seifert,D.E.,
            Palmero,S., Strand,M.E., Tonnessen,T., Dahl,C.P., Almaas,V.,
            Hubmacher,D., Apte,S.S., Christensen,G. and Lunde,I.G.
  TITLE     The extracellular matrix glycoprotein ADAMTSL2 is increased in
            heart failure and inhibits TGFbeta signalling in cardiac
            fibroblasts
  JOURNAL   Sci Rep 11 (1), 19757 (2021)
   PUBMED   34611183
  REMARK    GeneRIF: The extracellular matrix glycoprotein ADAMTSL2 is
            increased in heart failure and inhibits TGFbeta signalling in
            cardiac fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 957)
  AUTHORS   Zhang,A., Berardinelli,S.J., Leonhard-Melief,C., Vasudevan,D.,
            Liu,T.W., Taibi,A., Giannone,S., Apte,S.S., Holdener,B.C. and
            Haltiwanger,R.S.
  TITLE     O-Fucosylation of ADAMTSL2 is required for secretion and is
            impacted by geleophysic dysplasia-causing mutations
  JOURNAL   J Biol Chem 295 (46), 15742-15753 (2020)
   PUBMED   32913123
  REMARK    GeneRIF: O-Fucosylation of ADAMTSL2 is required for secretion and
            is impacted by geleophysic dysplasia-causing mutations.
REFERENCE   5  (residues 1 to 957)
  AUTHORS   Hubmacher,D., Taye,N., Balic,Z., Thacker,S., Adams,S.M., Birk,D.E.,
            Schweitzer,R. and Apte,S.S.
  TITLE     Limb- and tendon-specific Adamtsl2 deletion identifies a role for
            ADAMTSL2 in tendon growth in a mouse model for geleophysic
            dysplasia
  JOURNAL   Matrix Biol 82, 38-53 (2019)
   PUBMED   30738849
REFERENCE   6  (residues 1 to 957)
  AUTHORS   Jensen,L.D., Hot,B., Ramskold,D., Germano,R.F.V., Yokota,C.,
            Giatrellis,S., Lauschke,V.M., Hubmacher,D., Li,M.X., Hupe,M.,
            Arnold,T.D., Sandberg,R., Frisen,J., Trusohamn,M., Martowicz,A.,
            Wisniewska-Kruk,J., Nyqvist,D., Adams,R.H., Apte,S.S.,
            Vanhollebeke,B., Stenman,J.M. and Kele,J.
  TITLE     Disruption of the Extracellular Matrix Progressively Impairs
            Central Nervous System Vascular Maturation Downstream of
            beta-Catenin Signaling
  JOURNAL   Arterioscler Thromb Vasc Biol 39 (7), 1432-1447 (2019)
   PUBMED   31242033
REFERENCE   7  (residues 1 to 957)
  AUTHORS   Delhon,L., Mahaut,C., Goudin,N., Gaudas,E., Piquand,K., Le Goff,W.,
            Cormier-Daire,V. and Le Goff,C.
  TITLE     Impairment of chondrogenesis and microfibrillar network in Adamtsl2
            deficiency
  JOURNAL   FASEB J 33 (2), 2707-2718 (2019)
   PUBMED   30303737
  REMARK    GeneRIF: Adamtsl2 deficiency is associated with Impairment of
            chondrogenesis and microfibrillar network.
REFERENCE   8  (residues 1 to 957)
  AUTHORS   Aviram,R., Zaffryar-Eilot,S., Hubmacher,D., Grunwald,H., Maki,J.M.,
            Myllyharju,J., Apte,S.S. and Hasson,P.
  TITLE     Interactions between lysyl oxidases and ADAMTS proteins suggest a
            novel crosstalk between two extracellular matrix families
  JOURNAL   Matrix Biol 75-76, 114-125 (2019)
   PUBMED   29758265
REFERENCE   9  (residues 1 to 957)
  AUTHORS   Hubmacher,D., Wang,L.W., Mecham,R.P., Reinhardt,D.P. and Apte,S.S.
  TITLE     Adamtsl2 deletion results in bronchial fibrillin microfibril
            accumulation and bronchial epithelial dysplasia--a novel mouse
            model providing insights into geleophysic dysplasia
  JOURNAL   Dis Model Mech 8 (5), 487-499 (2015)
   PUBMED   25762570
  REMARK    GeneRIF: the bronchial epithelial dysplasia accompanying
            microfibril dysregulation in Adamtsl2(-/-) mice cannot be reversed
            by TGFbeta neutralization, and thus might be mediated by other
            mechanisms.
REFERENCE   10 (residues 1 to 957)
  AUTHORS   Koo,B.H., Le Goff,C., Jungers,K.A., Vasanji,A., O'Flaherty,J.,
            Weyman,C.M. and Apte,S.S.
  TITLE     ADAMTS-like 2 (ADAMTSL2) is a secreted glycoprotein that is widely
            expressed during mouse embryogenesis and is regulated during
            skeletal myogenesis
  JOURNAL   Matrix Biol 26 (6), 431-441 (2007)
   PUBMED   17509843
  REMARK    GeneRIF: Data suggest that induction of Adamtsl2 mRNA is an
            integral feature of myogenesis.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL845266.2, AB096928.1 and AI844377.1.
            
            On Jan 24, 2005 this sequence version replaced XP_130065.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK156991.1, BC128568.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 19.22 cM"
     Protein         1..957
                     /product="ADAMTS-like protein 2 precursor"
                     /note="ADAMTS-like protein 2; TSP1-repeats-containing
                     protein 1; TSP1-repeat-containing protein 1"
                     /calculated_mol_wt=102610
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3055
     mat_peptide     30..957
                     /product="ADAMTS-like protein 2. /id=PRO_0000249683"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSK7.1)"
                     /calculated_mol_wt=102610
     Region          50..106
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Region          <167..213
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Region          216..330
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Site            374
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Site            435
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Site            482
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Site            518
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Site            530
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Region          532..568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Site            539
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Site            550
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Region          632..691
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          695..743
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            737
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Region          747..800
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          804..860
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            813
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSK7.1)"
     Region          863..913
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          922..953
                     /region_name="PLAC"
                     /note="PLAC (protease and lacunin) domain; pfam08686"
                     /db_xref="CDD:462560"
     CDS             1..957
                     /gene="Adamtsl2"
                     /gene_synonym="A930008K15Rik; tcp-1"
                     /coded_by="NM_029981.2:197..3070"
                     /db_xref="CCDS:CCDS15824.1"
                     /db_xref="GeneID:77794"
                     /db_xref="MGI:MGI:1925044"
ORIGIN      
        1 mdgrrqhphw awsllavavv aggaapteas dnsptsnsle ggadttayww gewtkwtacs
       61 rscgggvtsq erhclqqrrk svpgtgnrtc vgtskryqlc rvqecppdgr sfreeqcvsf
      121 nsrvydgray qwkplypddy vhisskpcdl hcstvdgqrq ltvpardgts ckltdlrgvc
      181 vsgkcepigc dgvlfsthtl dkcgvcqgdg sscthvtgny rkgnnhlgys lvthipagar
      241 diqiverkks advlaladea gfyffngnyk vdspknfnia gtvvkyrrpm dvyetgieyi
      301 vaqgptnqgl nvmvwnqngk spsitfeytl lqsphmhhlp pvyysfseaa sqstesterq
      361 eldsarllgf mqhngslyrq tsserlglns qlfqppapev elgpsrgqes nevckqasgg
      421 vcegpprgkg fqdhnatgra fsadkddrei sahftshell santisdqll gtgseseefs
      481 lnetmnsifa qgaprsspae slyvdyeene gpaaylings ylelssdrin tsseapfpnt
      541 sasppnlagn rthkartrpk arkqgvspad myrwklsshe pcsatcttgv mstyamcvry
      601 dgvevddsyc daltrpepvh efcagrecqp rwetsswsec srtcgeghqf rivrcwkmls
      661 pgfdssvysd lceateavrp eerktcrnpa cgpqwemsew sectakcger svvtrdircs
      721 edeklcdpst kpvgeknctg ppcdrqwtvs dwgpcsgscg qgrtirhvyc ktsdgrvvpe
      781 sqcqtetkpl aihpcgdknc pahwlaqdwe rcnttcgrgv kkrlvlcmel angkpqirsg
      841 pecglarkpp eestcferpc fkwytspwse ctktcgvgvr mrdvkcyqgt divrgcdplv
      901 kpvgrqacdl qpcpteppdd scqdqpgtnc alaikvnlcg hwyyskaccr scrpphs
//
LOCUS       NP_001355974             334 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 9 isoform 14 [Homo sapiens].
ACCESSION   NP_001355974
VERSION     NP_001355974.1
DBSOURCE    REFSEQ: accession NM_001369045.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Ma,X., Yan,W., Xu,P., Ma,L., Zan,Y., Huang,L., Wang,G., Liu,L. and
            Hui,W.
  TITLE     LncRNA-p21 suppresses cell proliferation and induces apoptosis in
            gastric cancer by sponging miR-514b-3p and up-regulating ARHGEF9
            expression
  JOURNAL   Biol Chem 403 (10), 945-958 (2022)
   PUBMED   35947460
  REMARK    GeneRIF: LncRNA-p21 suppresses cell proliferation and induces
            apoptosis in gastric cancer by sponging miR-514b-3p and
            up-regulating ARHGEF9 expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Yang,H., Liao,H., Gan,S., Xiao,T. and Wu,L.
  TITLE     ARHGEF9 gene variant leads to developmental and epileptic
            encephalopathy: Genotypic phenotype analysis and treatment
            exploration
  JOURNAL   Mol Genet Genomic Med 10 (7), e1967 (2022)
   PUBMED   35638461
  REMARK    GeneRIF: ARHGEF9 gene variant leads to developmental and epileptic
            encephalopathy: Genotypic phenotype analysis and treatment
            exploration.
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Hines,D.J., Contreras,A., Garcia,B., Barker,J.S., Boren,A.J.,
            Moufawad El Achkar,C., Moss,S.J. and Hines,R.M.
  TITLE     Human ARHGEF9 intellectual disability syndrome is phenocopied by a
            mutation that disrupts collybistin binding to the GABAA receptor
            alpha2 subunit
  JOURNAL   Mol Psychiatry 27 (3), 1729-1741 (2022)
   PUBMED   35169261
  REMARK    GeneRIF: Human ARHGEF9 intellectual disability syndrome is
            phenocopied by a mutation that disrupts collybistin binding to the
            GABAA receptor alpha2 subunit.
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Ghesh,L., Besnard,T., Nizon,M., Trochu,E., Landeau-Trottier,G.,
            Breheret,F., Thauvin-Robinet,C., Bruel,A.L., Kuentz,P., Coubes,C.,
            Cuisset,L., Mignot,C., Keren,B., Bezieau,S. and Cogne,B.
  TITLE     Loss-of-function variants in ARHGEF9 are associated with an
            X-linked intellectual disability dominant disorder
  JOURNAL   Hum Mutat 42 (5), 498-505 (2021)
   PUBMED   33600053
  REMARK    GeneRIF: Loss-of-function variants in ARHGEF9 are associated with
            an X-linked intellectual disability dominant disorder.
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Scala,M., Zonneveld-Huijssoon,E., Brienza,M., Mecarelli,O., van der
            Hout,A.H., Zambrelli,E., Turner,K., Zara,F., Peron,A., Vignoli,A.
            and Striano,P.
  TITLE     De novo ARHGEF9 missense variants associated with
            neurodevelopmental disorder in females: expanding the genotypic and
            phenotypic spectrum of ARHGEF9 disease in females
  JOURNAL   Neurogenetics 22 (1), 87-94 (2021)
   PUBMED   32939676
  REMARK    GeneRIF: De novo ARHGEF9 missense variants associated with
            neurodevelopmental disorder in females: expanding the genotypic and
            phenotypic spectrum of ARHGEF9 disease in females.
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Harrington,A.W., Kim,J.Y. and Yoon,S.O.
  TITLE     Activation of Rac GTPase by p75 is necessary for c-jun N-terminal
            kinase-mediated apoptosis
  JOURNAL   J Neurosci 22 (1), 156-166 (2002)
   PUBMED   11756498
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Grosskreutz,Y., Hermann,A., Kins,S., Fuhrmann,J.C., Betz,H. and
            Kneussel,M.
  TITLE     Identification of a gephyrin-binding motif in the GDP/GTP exchange
            factor collybistin
  JOURNAL   Biol Chem 382 (10), 1455-1462 (2001)
   PUBMED   11727829
  REMARK    GeneRIF: Here we identified residues critical for interaction with
            gephyrin in the linker region between the SH3 and the DH domains of
            collybistin.
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Kins,S., Betz,H. and Kirsch,J.
  TITLE     Collybistin, a newly identified brain-specific GEF, induces
            submembrane clustering of gephyrin
  JOURNAL   Nat Neurosci 3 (1), 22-29 (2000)
   PUBMED   10607391
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Reid,T., Bathoorn,A., Ahmadian,M.R. and Collard,J.G.
  TITLE     Identification and characterization of hPEM-2, a guanine nucleotide
            exchange factor specific for Cdc42
  JOURNAL   J Biol Chem 274 (47), 33587-33593 (1999)
   PUBMED   10559246
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Balint,B. and Thomas,R.
  TITLE     Hereditary Hyperekplexia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL451106.9, BC043497.1 and
            AL391277.16.
            
            Summary: The protein encoded by this gene is a Rho-like GTPase that
            switches between the active (GTP-bound) state and inactive
            (GDP-bound) state to regulate CDC42 and other genes. This
            brain-specific protein also acts as an adaptor protein for the
            recruitment of gephyrin and together these proteins facilitate
            receceptor recruitement in GABAnergic and glycinergic synapses.
            Defects in this gene are the cause of startle disease with epilepsy
            (STHEE), also known as hyperekplexia with epilepsy, as well as
            several other types of cognitive disability. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC043497.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq11.1"
     Protein         1..334
                     /product="rho guanine nucleotide exchange factor 9 isoform
                     14"
                     /note="hPEM-2 collybistin; rho guanine nucleotide exchange
                     factor 9; PEM-2 homolog; rac/Cdc42 guanine nucleotide
                     exchange factor 9; Cdc42 guanine nucleotide exchange
                     factor (GEF) 9"
                     /calculated_mol_wt=39586
     Region          1..148
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; smart00325"
                     /db_xref="CDD:214619"
     Site            order(71,98..99,102..103,105..106,109..110,113..114,117,
                     143,147)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          153..248
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     CDS             1..334
                     /gene="ARHGEF9"
                     /gene_synonym="COLLYBISTIN; DEE8; EIEE8; HPEM-2; PEM-2;
                     PEM2"
                     /coded_by="NM_001369045.1:1250..2254"
                     /note="isoform 14 is encoded by transcript variant 27"
                     /db_xref="GeneID:23229"
                     /db_xref="HGNC:HGNC:14561"
                     /db_xref="MIM:300429"
ORIGIN      
        1 mfsdeqlkvi fgniediyrf qmgfvrdlek qynnddphls eigpcflehq dgfwiyseyc
       61 nnhldacmel sklmkdsryq hffeacrllq qmidiaidgf lltpvqkick yplqlaellk
      121 ytaqdhsdyr yvaaalavmr nvtqqinerk rrlenidkia qwqasvldwe dlirrdilyy
      181 kgridmdkye vvdiedgrdd dfnvsmknaf klhnketeei hlffakklee kirwlrafre
      241 erkmvqedek igfeisenqk rqaamtvrkv pkqkgvnsar svppsypppq dplnhgqylv
      301 pdgiaqsqvf eftepkrsqs pfwqnfsrlt pfkk
//
LOCUS       NP_001356145              93 aa            linear   PRI 27-APR-2025
DEFINITION  small integral membrane protein 41 [Homo sapiens].
ACCESSION   NP_001356145
VERSION     NP_001356145.1
DBSOURCE    REFSEQ: accession NM_001369216.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025259.49, BC042060.1 and AC078864.20.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000546390.2/ ENSP00000493663.2
            NMD candidate          :: translation inferred from conservation
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..93
                     /product="small integral membrane protein 41"
                     /calculated_mol_wt=9214
     CDS             1..93
                     /gene="SMIM41"
                     /coded_by="NM_001369216.1:77..358"
                     /db_xref="CCDS:CCDS91699.1"
                     /db_xref="GeneID:113523638"
                     /db_xref="HGNC:HGNC:54075"
ORIGIN      
        1 mngsqagaaa qaawlssccn qsasppeppe gpravqavvl gvlsllvlcg vlflggglll
       61 raqgltallt reqrasrepe pgsasgedgd dds
//
LOCUS       NP_079216               1870 aa            linear   PRI 27-APR-2025
DEFINITION  dedicator of cytokinesis protein 5 isoform 1 [Homo sapiens].
ACCESSION   NP_079216 XP_209883
VERSION     NP_079216.4
DBSOURCE    REFSEQ: accession NM_024940.8
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1870)
  AUTHORS   Qu,H., Liu,X., Zhu,J., Xiong,X., Li,L., He,Q., Wang,Y., Yang,G.,
            Zhang,L., Yang,Q., Luo,G., Zheng,Y. and Zheng,H.
  TITLE     Dock5 Deficiency Promotes Proteinuric Kidney Diseases via
            Modulating Podocyte Lipid Metabolism
  JOURNAL   Adv Sci (Weinh) 11 (11), e2306365 (2024)
   PUBMED   38161229
  REMARK    GeneRIF: Dock5 Deficiency Promotes Proteinuric Kidney Diseases via
            Modulating Podocyte Lipid Metabolism.
REFERENCE   2  (residues 1 to 1870)
  AUTHORS   Liu,C., Li,G., Zheng,S., She,L., Lu,S., Wang,Y., Huang,D.,
            Zhang,X., Sun,L., Liu,Y. and Qiu,Y.
  TITLE     PHF5A regulates the expression of the DOCK5 variant to promote
            HNSCC progression through p38 MAPK activation
  JOURNAL   Biol Direct 18 (1), 39 (2023)
   PUBMED   37434235
  REMARK    GeneRIF: PHF5A regulates the expression of the DOCK5 variant to
            promote HNSCC progression through p38 MAPK activation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1870)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   4  (residues 1 to 1870)
  AUTHORS   Meng,L., Zheng,Y., Liu,S., Ju,Y., Ren,S., Sang,Y., Zhu,Y., Gu,L.,
            Liu,F., Zhao,Y., Zhang,X. and Sang,M.
  TITLE     ZEB1 represses biogenesis of circ-DOCK5 to facilitate metastasis in
            esophageal squamous cell carcinoma via a positive feedback loop
            with TGF-beta
  JOURNAL   Cancer Lett 519, 117-129 (2021)
   PUBMED   34216686
  REMARK    GeneRIF: ZEB1 represses biogenesis of circ-DOCK5 to facilitate
            metastasis in esophageal squamous cell carcinoma via a positive
            feedback loop with TGF-beta.
REFERENCE   5  (residues 1 to 1870)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1870)
  AUTHORS   El-Sayed Moustafa,J.S., Eleftherohorinou,H., de Smith,A.J.,
            Andersson-Assarsson,J.C., Alves,A.C., Hadjigeorgiou,E.,
            Walters,R.G., Asher,J.E., Bottolo,L., Buxton,J.L., Sladek,R.,
            Meyre,D., Dina,C., Visvikis-Siest,S., Jacobson,P., Sjostrom,L.,
            Carlsson,L.M., Walley,A., Falchi,M., Froguel,P., Blakemore,A.I. and
            Coin,L.J.
  TITLE     Novel association approach for variable number tandem repeats
            (VNTRs) identifies DOCK5 as a susceptibility gene for severe
            obesity
  JOURNAL   Hum Mol Genet 21 (16), 3727-3738 (2012)
   PUBMED   22595969
  REMARK    GeneRIF: the potential role of DOCK5 in human obesity
REFERENCE   7  (residues 1 to 1870)
  AUTHORS   Kang,H., Davis-Dusenbery,B.N., Nguyen,P.H., Lal,A., Lieberman,J.,
            Van Aelst,L., Lagna,G. and Hata,A.
  TITLE     Bone morphogenetic protein 4 promotes vascular smooth muscle
            contractility by activating microRNA-21 (miR-21), which
            down-regulates expression of family of dedicator of cytokinesis
            (DOCK) proteins
  JOURNAL   J Biol Chem 287 (6), 3976-3986 (2012)
   PUBMED   22158624
REFERENCE   8  (residues 1 to 1870)
  AUTHORS   Sanders,M.A., Ampasala,D. and Basson,M.D.
  TITLE     DOCK5 and DOCK1 regulate Caco-2 intestinal epithelial cell
            spreading and migration on collagen IV
  JOURNAL   J Biol Chem 284 (1), 27-35 (2009)
   PUBMED   19004829
  REMARK    GeneRIF: along with DOCK1, DOCK5 is an important mediator of
            CrkII/CrkL regulation of Caco-2 spreading and migration on collagen
            IV.
REFERENCE   9  (residues 1 to 1870)
  AUTHORS   Nusbaum,C., Mikkelsen,T.S., Zody,M.C., Asakawa,S., Taudien,S.,
            Garber,M., Kodira,C.D., Schueler,M.G., Shimizu,A., Whittaker,C.A.,
            Chang,J.L., Cuomo,C.A., Dewar,K., FitzGerald,M.G., Yang,X.,
            Allen,N.R., Anderson,S., Asakawa,T., Blechschmidt,K., Bloom,T.,
            Borowsky,M.L., Butler,J., Cook,A., Corum,B., DeArellano,K.,
            DeCaprio,D., Dooley,K.T., Dorris,L. 3rd, Engels,R., Glockner,G.,
            Hafez,N., Hagopian,D.S., Hall,J.L., Ishikawa,S.K., Jaffe,D.B.,
            Kamat,A., Kudoh,J., Lehmann,R., Lokitsang,T., Macdonald,P.,
            Major,J.E., Matthews,C.D., Mauceli,E., Menzel,U., Mihalev,A.H.,
            Minoshima,S., Murayama,Y., Naylor,J.W., Nicol,R., Nguyen,C.,
            O'Leary,S.B., O'Neill,K., Parker,S.C., Polley,A., Raymond,C.K.,
            Reichwald,K., Rodriguez,J., Sasaki,T., Schilhabel,M., Siddiqui,R.,
            Smith,C.L., Sneddon,T.P., Talamas,J.A., Tenzin,P., Topham,K.,
            Venkataraman,V., Wen,G., Yamazaki,S., Young,S.K., Zeng,Q.,
            Zimmer,A.R., Rosenthal,A., Birren,B.W., Platzer,M., Shimizu,N. and
            Lander,E.S.
  TITLE     DNA sequence and analysis of human chromosome 8
  JOURNAL   Nature 439 (7074), 331-335 (2006)
   PUBMED   16421571
REFERENCE   10 (residues 1 to 1870)
  AUTHORS   Cote,J.F. and Vuori,K.
  TITLE     Identification of an evolutionarily conserved superfamily of
            DOCK180-related proteins with guanine nucleotide exchange activity
  JOURNAL   J Cell Sci 115 (Pt 24), 4901-4913 (2002)
   PUBMED   12432077
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC041005.20, BC015352.1,
            BC011877.2, BF884637.1, CR749353.1, AC091185.6, AK126249.1,
            BC041761.2, AK024687.1, BX648352.1, AK026663.1, CR627414.1,
            BE549612.1 and BF195734.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 3, 2006 this sequence version replaced NP_079216.3.
            
            Summary: This gene encodes a member of the dedicator of cytokinesis
            protein family. Members of this family act as guanine nucleotide
            exchange factors for small Rho family G proteins. The protein
            encoded by this gene is thought to associate with adaptors CRK and
            CRKL, and function in regulation of intestinal epithelial cell
            spreading and migration on collagen IV. Similar proteins in mouse
            and zebrafish also function in myoblast fusion. [provided by
            RefSeq, Oct 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC137175.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000276440.12/ ENSP00000276440.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1870
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..1870
                     /product="dedicator of cytokinesis protein 5 isoform 1"
                     /note="dedicator of cytokinesis protein 5"
                     /calculated_mol_wt=215179
     Region          12..67
                     /region_name="SH3_DOCK1_5_A"
                     /note="Src Homology 3 domain of Class A Dedicator of
                     Cytokinesis proteins 1 and 5; cd12051"
                     /db_xref="CDD:212984"
     Site            order(14..18,25,30..32,34,38..39,43..44,46,54,56,58,60,
                     62..63,65,67)
                     /site_type="other"
                     /note="ELMO interaction site [polypeptide binding]"
                     /db_xref="CDD:212984"
     Site            order(17,19,22,26,43..44,60,62..63)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212984"
     Region          75..434
                     /region_name="DOCK_N"
                     /note="DOCK N-terminus; pfam16172"
                     /db_xref="CDD:465040"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Region          442..637
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Site            818
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Region          1238..1637
                     /region_name="DHR2_DOCK5"
                     /note="Dock Homology Region 2, a GEF domain, of Class A
                     Dedicator of Cytokinesis 5; cd11708"
                     /db_xref="CDD:212581"
     Site            order(1322,1329..1331,1333,1335..1336,1338..1339,
                     1342..1343,1345..1346,1349..1350,1353,1440,1444..1447,
                     1450)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:212581"
     Site            order(1388,1390..1393,1409..1411,1428..1430,1464..1467,
                     1478..1479,1482,1521,1525,1545..1546,1548..1549,
                     1553..1554,1557..1563,1566,1596,1612,1614..1615,1618,1621)
                     /site_type="other"
                     /note="Rac binding site [polypeptide binding]"
                     /db_xref="CDD:212581"
     Site            1557..1562
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212581"
     Region          1679..1702
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Site            1756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Site            1766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Region          1772..1870
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Site            1785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Site            1789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Site            1794
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Site            1814
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Site            1834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H7D0.3)"
     Site            1869
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H7D0.3)"
     CDS             1..1870
                     /gene="DOCK5"
                     /coded_by="NM_024940.8:221..5833"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6047.1"
                     /db_xref="GeneID:80005"
                     /db_xref="HGNC:HGNC:23476"
                     /db_xref="MIM:616904"
ORIGIN      
        1 marwiptkrq kygvaiynyn asqdvelslq igdtvhilem yegwyrgytl qnkskkgifp
       61 etyihlkeat vedlgqhetv ipgelplvqe ltstlrewav iwrklyvnnk ltlfrqlqqm
      121 tysliewrsq ilsgtlpkde laelkkkvta kidhgnrmlg ldlvvrddng nildpdetst
      181 ialfkaheva skrieekiqe eksilqnldl rgqsifstih tyglyvnfkn fvcnigedae
      241 lfmalydpdq stfisenyli rwgsngmpke ieklnnlqav ftdlssmdli rprvslvcqi
      301 vrvghmelke gkkhtcglrr pfgvavmdit diihgkvdde ekqhfipfqq iametyirqr
      361 qlimsplits hvigeneplt svlnkviaak evnhkgqglw vslkllpgdl tqvqknfshl
      421 vdrstaiark mgfpeiilpg dvrndiyvtl ihgefdkgkk ktpknvevtm svhdeegkll
      481 ekaihpgagy egiseyksvv yyqvkqpcwy etvkvsiaie evtrchirft frhrssqetr
      541 dkserafgva fvklmnpdgt tlqdgrhdlv vykgdnkkme dakfyltlpg tkmemeekel
      601 qasknlvtft pskdstkdsf qiatlicstk ltqnvdllgl lnwrsnsqni khnlkklmev
      661 dggeivkflq dtldalfnim memsdsetyd flvfdalvfi isligdikfq hfnpvletyi
      721 ykhfsatlay vklskvlnfy vanaddsskt ellfaalkal kylfrfiiqs rvlylrfygq
      781 skdgdefnns irqlflafnm lmdrpleeav kikgaalkyl psiindvklv fdpvelsvlf
      841 ckfiqsipdn qlvrqklncm tkivestlfr qsecrevllp lltdqlsgql ddnsnkpdhe
      901 assqllsnil evldrkdvga tavhiqlime rllrrinrtv igmnrqsphi gsfvacmial
      961 lqqmddshys hyistfktrq diidflmetf imfkdligkn vyakdwmvmn mtqnrvflra
     1021 inqfaevltr ffmdqasfel qlwnnyfhla vafltheslq letfsqakrn kivkkygdmr
     1081 keigfrirdm wynlgphkik fipsmvgpil evtltpevel rkatipiffd mmqcefnfsg
     1141 ngnfhmfene litkldqeve ggrgdeqykv lleklllehc rkhkylsssg evfallvssl
     1201 lenlldyrti imqdeskenr msctvnvlnf ykekkrediy irylyklrdl hrdcenytea
     1261 aytlllhael lqwsdkpcvp hllqkdsyyv ytqqelkekl yqeiisyfdk gkmwekaikl
     1321 skelaetyes kvfdyeglgn llkkrasfye niikamrpqp eyfavgyygq gfpsflrnki
     1381 fiyrgkeyer redfslrllt qfpnaekmts ttppgediks spkqymqcft vkpvmslpps
     1441 ykdkpvpeqi lnyyranevq qfrysrpfrk gekdpdnefa tmwierttyt taytfpgilk
     1501 wfevkqiste eisplenaie tmeltneris ncvqqhawdr slsvhplsml lsgivdpavm
     1561 ggfsnyekaf ftekylqehp edqekvellk rlialqmpll tegirihgek lteqlkplhe
     1621 rlsscfrelk ekvekhygvi tlppnlterk qsrtgsivlp yimsstlrrl sitsvtssvv
     1681 stssnssdna psrpgsdgsi lepllerras sgarvedlsl reensenris kfkrkdwsls
     1741 ksqviaekap epdlmsptrk aqrpkslqlm dnrlspfhgs sppqstplsp ppltpkatrt
     1801 lsspslqtdg iaatpvpppp ppkskpyegs qrnstelapp lpvrreakap pppppkarks
     1861 giptsepgsq
//
LOCUS       NP_002237                394 aa            linear   PRI 27-APR-2025
DEFINITION  potassium channel subfamily K member 3 [Homo sapiens].
ACCESSION   NP_002237
VERSION     NP_002237.1
DBSOURCE    REFSEQ: accession NM_002246.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Rinne,S., Schick,F., Vowinkel,K., Schutte,S., Krasel,C.,
            Kauferstein,S., Schafer,M.K., Kiper,A.K., Muller,T. and Decher,N.
  TITLE     Potassium channel TASK-5 forms functional heterodimers with TASK-1
            and TASK-3 to break its silence
  JOURNAL   Nat Commun 15 (1), 7548 (2024)
   PUBMED   39215006
  REMARK    GeneRIF: Potassium channel TASK-5 forms functional heterodimers
            with TASK-1 and TASK-3 to break its silence.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Huang,D., Shang,W., Xu,M., Wan,Q., Zhang,J., Tang,X., Shen,Y.,
            Wang,Y. and Yu,Y.
  TITLE     Genome-Wide Methylation Analysis Reveals a KCNK3-Prominent Causal
            Cascade on Hypertension
  JOURNAL   Circ Res 135 (3), e76-e93 (2024)
   PUBMED   38841840
  REMARK    GeneRIF: Genome-Wide Methylation Analysis Reveals a KCNK3-Prominent
            Causal Cascade on Hypertension.
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Wiedmann,F., Paasche,A., Nietfeld,J., Kraft,M., Meyer,A.L.,
            Warnecke,G., Karck,M., Frey,N. and Schmidt,C.
  TITLE     Activation of neurokinin-III receptors modulates human atrial
            TASK-1 currents
  JOURNAL   J Mol Cell Cardiol 184, 26-36 (2023)
   PUBMED   37793594
  REMARK    GeneRIF: Activation of neurokinin-III receptors modulates human
            atrial TASK-1 currents.
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Yeo,Y., Jeong,H., Kim,M., Choi,Y., Kim,K.L. and Suh,W.
  TITLE     Crosstalk between BMP signaling and KCNK3 in phenotypic switching
            of pulmonary vascular smooth muscle cells
  JOURNAL   BMB Rep 55 (11), 565-570 (2022)
   PUBMED   36016502
  REMARK    GeneRIF: Crosstalk between BMP signaling and KCNK3 in phenotypic
            switching of pulmonary vascular smooth muscle cells.
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Sormann,J., Schewe,M., Proks,P., Jouen-Tachoire,T., Rao,S.,
            Riel,E.B., Agre,K.E., Begtrup,A., Dean,J., Descartes,M.,
            Fischer,J., Gardham,A., Lahner,C., Mark,P.R., Muppidi,S.,
            Pichurin,P.N., Porrmann,J., Schallner,J., Smith,K., Straub,V.,
            Vasudevan,P., Willaert,R., Carpenter,E.P., Rodstrom,K.E.J.,
            Hahn,M.G., Muller,T., Baukrowitz,T., Hurles,M.E., Wright,C.F. and
            Tucker,S.J.
  TITLE     Gain-of-function mutations in KCNK3 cause a developmental disorder
            with sleep apnea
  JOURNAL   Nat Genet 54 (10), 1534-1543 (2022)
   PUBMED   36195757
  REMARK    GeneRIF: Gain-of-function mutations in KCNK3 cause a developmental
            disorder with sleep apnea.
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Patel,A.J., Honore,E., Lesage,F., Fink,M., Romey,G. and
            Lazdunski,M.
  TITLE     Inhalational anesthetics activate two-pore-domain background K+
            channels
  JOURNAL   Nat Neurosci 2 (5), 422-426 (1999)
   PUBMED   10321245
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Manjunath,N.A., Bray-Ward,P., Goldstein,S.A. and Gallagher,P.G.
  TITLE     Assignment of the 2P domain, acid-sensitive potassium channel OAT1
            gene KCNK3 to human chromosome bands 2p24.1-->p23.3 and murine 5B
            by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 86 (3-4), 242-243 (1999)
   PUBMED   10575216
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Lesage,F. and Lazdunski,M.
  TITLE     Mapping of human potassium channel genes TREK-1 (KCNK2) and TASK
            (KCNK3) to chromosomes 1q41 and 2p23
  JOURNAL   Genomics 51 (3), 478-479 (1998)
   PUBMED   9721223
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Duprat,F., Lesage,F., Fink,M., Reyes,R., Heurteaux,C. and
            Lazdunski,M.
  TITLE     TASK, a human background K+ channel to sense external pH variations
            near physiological pH
  JOURNAL   EMBO J 16 (17), 5464-5471 (1997)
   PUBMED   9312005
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Austin,E.D., Phillips,J.A. III and Loyd,J.E.
  TITLE     Heritable Pulmonary Arterial Hypertension Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301658
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015977.9 and AF065163.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the superfamily of potassium
            channel proteins that contain two pore-forming P domains. The
            encoded protein is an outwardly rectifying channel that is
            sensitive to changes in extracellular pH and is inhibited by
            extracellular acidification. Also referred to as an acid-sensitive
            potassium channel, it is activated by the anesthetics halothane and
            isoflurane. Although three transcripts are detected in northern
            blots, there is currently no sequence available to confirm
            transcript variants for this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF006823.1, AF065163.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302909.4/ ENSP00000306275.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..394
                     /product="potassium channel subfamily K member 3"
                     /note="potassium inwardly-rectifying channel, subfamily K,
                     member 3; TWIK-related acid-sensitive K+ 1; acid-sensitive
                     potassium channel protein TASK; two P domain potassium
                     channel; cardiac potassium channel; TWIK-related
                     acid-sensitive K+ channel; potassium channel, two pore
                     domain subfamily K, member 3; two pore K(+) channel KT3.1;
                     two pore potassium channel KT3.1; TWIK-related
                     acid-sensitive K(+) channel 1; acid-sensitive potassium
                     channel protein TASK-1"
                     /calculated_mol_wt=43387
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14649.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14649.1)"
     Region          <73..132
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          93..98
                     /region_name="Selectivity filter 1.
                     /evidence=ECO:0000305|PubMed:26919430"
                     /note="propagated from UniProtKB/Swiss-Prot (O14649.1)"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14649.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14649.1)"
     Region          167..243
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          199..204
                     /region_name="Selectivity filter 2.
                     /evidence=ECO:0000305|PubMed:26919430"
                     /note="propagated from UniProtKB/Swiss-Prot (O14649.1)"
     Site            223..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14649.1)"
     Region          243..248
                     /region_name="X-gate.
                     /evidence=ECO:0000269|PubMed:32499642"
                     /note="propagated from UniProtKB/Swiss-Prot (O14649.1)"
     Region          266..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14649.1)"
     Region          338..357
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14649.1)"
     CDS             1..394
                     /gene="KCNK3"
                     /gene_synonym="K2p3.1; OAT1; PPH4; TASK; TASK-1; TASK1;
                     TBAK1"
                     /coded_by="NM_002246.3:155..1339"
                     /db_xref="CCDS:CCDS1727.1"
                     /db_xref="GeneID:3777"
                     /db_xref="HGNC:HGNC:6278"
                     /db_xref="MIM:603220"
ORIGIN      
        1 mkrqnvrtla livctftyll vgaavfdale sepelierqr lelrqqelra rynlsqggye
       61 elervvlrlk phkagvqwrf agsfyfaitv ittigyghaa pstdggkvfc mfyallgipl
      121 tlvmfqslge rintlvryll hrakkglgmr radvsmanmv ligffscist lcigaaafsh
      181 yehwtffqay yycfitltti gfgdyvalqk dqalqtqpqy vafsfvyilt gltvigafln
      241 lvvlrfmtmn aedekrdaeh ralltrngqa gggggggsah ttdtasstaa aggggfrnvy
      301 aevlhfqsmc sclwyksrek lqysipmiip rdlstsdtcv eqshsspggg grysdtpsrr
      361 clcsgaprsa issvstglhs lstfrglmkr rssv
//
LOCUS       NP_001355682             327 aa            linear   ROD 27-APR-2025
DEFINITION  tripartite motif-containing protein 12A isoform 1 [Mus musculus].
ACCESSION   NP_001355682
VERSION     NP_001355682.1
DBSOURCE    REFSEQ: accession NM_001368753.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Schafer,A., Marzi,A., Furuyama,W., Catanzaro,N.J., Nguyen,C.,
            Haddock,E., Feldmann,F., Meade-White,K., Thomas,T., Hubbard,M.L.,
            Gully,K.L., Leist,S.R., Hock,P., Bell,T.A., De la Cruz,G.E.,
            Midkiff,B.R., Martinez,D.R., Shaw,G.D., Miller,D.R., Vernon,M.J.,
            Graham,R.L., Cowley,D.O., Montgomery,S.A., Schughart,K., de
            Villena,F.P.M., Wilkerson,G.K., Ferris,M.T., Feldmann,H. and
            Baric,R.S.
  TITLE     Mapping of susceptibility loci for Ebola virus pathogenesis in mice
  JOURNAL   Cell Rep 43 (5), 114127 (2024)
   PUBMED   38652660
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Orozco,L.D., Cokus,S.J., Ghazalpour,A., Ingram-Drake,L., Wang,S.,
            van Nas,A., Che,N., Araujo,J.A., Pellegrini,M. and Lusis,A.J.
  TITLE     Copy number variation influences gene expression and metabolic
            traits in mice
  JOURNAL   Hum Mol Genet 18 (21), 4118-4129 (2009)
   PUBMED   19648292
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Boon,A.C., deBeauchamp,J., Hollmann,A., Luke,J., Kotb,M., Rowe,S.,
            Finkelstein,D., Neale,G., Lu,L., Williams,R.W. and Webby,R.J.
  TITLE     Host genetic variation affects resistance to infection with a
            highly pathogenic H5N1 influenza A virus in mice
  JOURNAL   J Virol 83 (20), 10417-10426 (2009)
   PUBMED   19706712
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Tareen,S.U., Sawyer,S.L., Malik,H.S. and Emerman,M.
  TITLE     An expanded clade of rodent Trim5 genes
  JOURNAL   Virology 385 (2), 473-483 (2009)
   PUBMED   19147168
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Blackburn,A.C., Hill,L.Z., Roberts,A.L., Wang,J., Aud,D., Jung,J.,
            Nikolcheva,T., Allard,J., Peltz,G., Otis,C.N., Cao,Q.J.,
            Ricketts,R.S., Naber,S.P., Mollenhauer,J., Poustka,A., Malamud,D.
            and Jerry,D.J.
  TITLE     Genetic mapping in mice identifies DMBT1 as a candidate modifier of
            mammary tumors and breast cancer risk
  JOURNAL   Am J Pathol 170 (6), 2030-2041 (2007)
   PUBMED   17525270
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Norman,B., Davis,J. and Piatigorsky,J.
  TITLE     Postnatal gene expression in the normal mouse cornea by SAGE
  JOURNAL   Invest Ophthalmol Vis Sci 45 (2), 429-440 (2004)
   PUBMED   14744882
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC142110.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094899.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN00849374,
                                           SAMN00849375 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 55.69 cM"
     Protein         1..327
                     /product="tripartite motif-containing protein 12A isoform
                     1"
                     /note="tripartite motif protein 12; tripartite
                     motif-containing protein 12; tripartite motif-containing
                     12; tripartite motif-containing protein 12A"
                     /calculated_mol_wt=37753
     Region          8..78
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(15,18,30,32,35,38,55,58)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438111"
     Region          96..133
                     /region_name="Bbox2_TRIM5-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34,
                     TRIM38 and similar proteins; cd19761"
                     /db_xref="CDD:380819"
     Region          <130..>209
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     CDS             1..327
                     /gene="Trim12a"
                     /gene_synonym="2310043C01Rik; Trim12"
                     /coded_by="NM_001368753.1:142..1125"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:76681"
                     /db_xref="MGI:MGI:1923931"
ORIGIN      
        1 masqfmknlk eevtcpvcln lmvkpvsadc ghtfcqgcit lyfesikcdk kvficpvcri
       61 syqfsnlrpn rnvaniverl kmfkpspeee qkvfncarhg kklqlfcrkd mmaicwlcer
      121 sqehrghkta lieevaqeyk nqiqkdvqnv rsefkrmrdi mdseekkelq klrqekedil
      181 nnlaeseseh aqqsklledf isdvehqlqc sdieilqgve niiershtfs mkkpkaiare
      241 qrkfrapdlq gmlqvlqghr gssllgvflp ppwtnfrthl wtltsgqege ifhpgrsgee
      301 kpgtgfnqpn qpaappflfw lgvwgrn
//
LOCUS       NP_001029048             402 aa            linear   ROD 27-APR-2025
DEFINITION  potassium channel subfamily K member 9 precursor [Mus musculus].
ACCESSION   NP_001029048 XP_139425
VERSION     NP_001029048.1
DBSOURCE    REFSEQ: accession NM_001033876.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Steponenaite,A., Lalic,T., Atkinson,L., Tanday,N., Brown,L.,
            Mathie,A., Cader,Z.M. and Lall,G.S.
  TITLE     TASK-3, two-pore potassium channels, contribute to circadian
            rhythms in the electrical properties of the suprachiasmatic nucleus
            and play a role in driving stable behavioural photic entrainment
  JOURNAL   Chronobiol Int 41 (6), 802-816 (2024)
   PUBMED   38757583
  REMARK    GeneRIF: TASK-3, two-pore potassium channels, contribute to
            circadian rhythms in the electrical properties of the
            suprachiasmatic nucleus and play a role in driving stable
            behavioural photic entrainment.
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Rengifo Rojas,C., Cercy,J., Perillous,S., Gonthier-Gueret,C.,
            Montibus,B., Maupetit-Mehouas,S., Espinadel,A., Dupre,M.,
            Hong,C.C., Hata,K., Nakabayashi,K., Plagge,A., Bouschet,T.,
            Arnaud,P., Vaillant,I. and Court,F.
  TITLE     Biallelic non-productive enhancer-promoter interactions precede
            imprinted expression of Kcnk9 during mouse neural commitment
  JOURNAL   HGG Adv 5 (2), 100271 (2024)
   PUBMED   38297831
  REMARK    GeneRIF: Biallelic non-productive enhancer-promoter interactions
            precede imprinted expression of Kcnk9 during mouse neural
            commitment.
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Song,H.C., Zhang,Y., Ma,Z.X., Yao,Q.L. and Ma,X.J.
  TITLE     TWIK-related acid-sensitive potassium channels TASK-1 and TASK-3
            may participate in the process of the coexistence of asthma and OSA
  JOURNAL   Sleep Breath 28 (1), 123-131 (2024)
   PUBMED   37428352
  REMARK    GeneRIF: TWIK-related acid-sensitive potassium channels TASK-1 and
            TASK-3 may participate in the process of the coexistence of asthma
            and OSA.
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Loftus,D., Bae,B., Whilden,C.M. and Whipple,A.J.
  TITLE     Allelic chromatin structure precedes imprinted expression of Kcnk9
            during neurogenesis
  JOURNAL   Genes Dev 37 (17-18), 829-843 (2023)
   PUBMED   37821107
  REMARK    GeneRIF: Allelic chromatin structure precedes imprinted expression
            of Kcnk9 during neurogenesis.
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Wen,X., Liao,P., Luo,Y., Yang,L., Yang,H., Liu,L. and Jiang,R.
  TITLE     Tandem pore domain acid-sensitive K channel 3 (TASK-3) regulates
            visual sensitivity in healthy and aging retina
  JOURNAL   Sci Adv 8 (36), eabn8785 (2022)
   PUBMED   36070380
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Ruf,N., Bahring,S., Galetzka,D., Pliushch,G., Luft,F.C.,
            Nurnberg,P., Haaf,T., Kelsey,G. and Zechner,U.
  TITLE     Sequence-based bioinformatic prediction and QUASEP identify genomic
            imprinting of the KCNK9 potassium channel gene in mouse and human
  JOURNAL   Hum Mol Genet 16 (21), 2591-2599 (2007)
   PUBMED   17704508
  REMARK    GeneRIF: Kcnk9 gene is imprinted, with preferential expression from
            the maternal allele in mouse brain.
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Meuth,S.G., Kanyshkova,T., Meuth,P., Landgraf,P., Munsch,T.,
            Ludwig,A., Hofmann,F., Pape,H.C. and Budde,T.
  TITLE     Membrane resting potential of thalamocortical relay neurons is
            shaped by the interaction among TASK3 and HCN2 channels
  JOURNAL   J Neurophysiol 96 (3), 1517-1529 (2006)
   PUBMED   16760342
  REMARK    GeneRIF: TASK3 and HCN2 channels stabilize the membrane potential
            by a mutual functional interactions.
REFERENCE   8  (residues 1 to 402)
  AUTHORS   Torborg,C.L., Berg,A.P., Jeffries,B.W., Bayliss,D.A. and
            McBain,C.J.
  TITLE     TASK-like conductances are present within hippocampal CA1 stratum
            oriens interneuron subpopulations
  JOURNAL   J Neurosci 26 (28), 7362-7367 (2006)
   PUBMED   16837582
  REMARK    GeneRIF: TASK-like conductances are more prevalent in inhibitory
            interneurons than previously supposed.
REFERENCE   9  (residues 1 to 402)
  AUTHORS   Burdakov,D., Jensen,L.T., Alexopoulos,H., Williams,R.H.,
            Fearon,I.M., O'Kelly,I., Gerasimenko,O., Fugger,L. and
            Verkhratsky,A.
  TITLE     Tandem-pore K+ channels mediate inhibition of orexin neurons by
            glucose
  JOURNAL   Neuron 50 (5), 711-722 (2006)
   PUBMED   16731510
  REMARK    GeneRIF: inhibition by glucose in neurons is mediated by ion
            channels not previously implicated in central or peripheral glucose
            sensing: tandem-pore K(+) (K(2P)) channels
REFERENCE   10 (residues 1 to 402)
  AUTHORS   Czirjak,G. and Enyedi,P.
  TITLE     Zinc and mercuric ions distinguish TRESK from the other
            two-pore-domain K+ channels
  JOURNAL   Mol Pharmacol 69 (3), 1024-1032 (2006)
   PUBMED   16354767
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC118008.14 and AC161195.4.
            
            On Sep 30, 2005 this sequence version replaced XP_139425.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC139167.1, DQ185133.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849379, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            imprinted gene                   :: PMID: 17704508
            RefSeq Select criteria           :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15"
     Protein         1..402
                     /product="potassium channel subfamily K member 9
                     precursor"
                     /note="TWIK-related acid-sensitive K(+) channel 3;
                     acid-sensitive potassium channel protein TASK-3"
                     /calculated_mol_wt=41898
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3032
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3LS21.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3LS21.1)"
     Region          <73..132
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Site            78
                     /site_type="other"
                     /note="Forms a cation-pi interaction with protonated H-98,
                     stabilizing the C-type inactivated state.
                     /evidence=ECO:0000250|UniProtKB:Q9NPC2; propagated from
                     UniProtKB/Swiss-Prot (Q3LS21.1)"
     Region          93..98
                     /region_name="Selectivity filter 1.
                     /evidence=ECO:0000250|UniProtKB:Q9NPC2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3LS21.1)"
     Site            98
                     /site_type="other"
                     /note="pH sensor. /evidence=ECO:0000250|UniProtKB:Q9NPC2;
                     propagated from UniProtKB/Swiss-Prot (Q3LS21.1)"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3LS21.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3LS21.1)"
     Region          <184..243
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          199..204
                     /region_name="Selectivity filter 2.
                     /evidence=ECO:0000250|UniProtKB:Q9NPC2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3LS21.1)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3LS21.1)"
     Region          243..248
                     /region_name="X-gate.
                     /evidence=ECO:0000250|UniProtKB:Q9NPC2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3LS21.1)"
     CDS             1..402
                     /gene="Kcnk9"
                     /gene_synonym="A930009L07Rik; Task3"
                     /coded_by="NM_001033876.2:1421..2629"
                     /db_xref="CCDS:CCDS27515.1"
                     /db_xref="GeneID:223604"
                     /db_xref="MGI:MGI:3521816"
ORIGIN      
        1 mkrqnvrtls liactftyll vgaavfdale sdhemreeek lkaeevrlrg kynissddyq
       61 qlelvilqse phragvqwkf agsfyfaitv ittigyghaa pgtdagkafc mfyavlgipl
      121 tlvmfqslge rmntfvryll krikkccgmr ntevsmenmv tvgffscmgt lclgaaafsq
      181 cedwsffhay yycfitltti gfgdfvalqa kgalqrkpfy vafsfmyilv gltvigafln
      241 lvvlrfltmn tdeellegev aeilagnprr vsvrapqrrk rhhamyflrk ygrtlcylcf
      301 pgtnwgkddd ddddddvvdn vvvtapisap apapapapap aavaagatir svratvhtvs
      361 crveeippdv lrntyfrsvf gaippgmhtc gdhrlhlrrk si
//
LOCUS       NP_001357228             522 aa            linear   PRI 27-APR-2025
DEFINITION  amphoterin-induced protein 2 precursor [Homo sapiens].
ACCESSION   NP_001357228 XP_005268894
VERSION     NP_001357228.1
DBSOURCE    REFSEQ: accession NM_001370299.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Iida,Y., Osaki,M., Sato,S., Izutsu,R., Seong,H., Komatsu,H.,
            Taniguchi,F. and Okada,F.
  TITLE     AMIGO2 is involved in the spread of peritoneal metastasis in serous
            ovarian cancer via promoting adhesion to the peritoneal mesothelial
            cells
  JOURNAL   Int J Clin Oncol 29 (9), 1354-1363 (2024)
   PUBMED   38811439
  REMARK    GeneRIF: AMIGO2 is involved in the spread of peritoneal metastasis
            in serous ovarian cancer via promoting adhesion to the peritoneal
            mesothelial cells.
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Chen,S., Du,W., Feng,K., Liu,K., Li,C., Li,S. and Yin,H.
  TITLE     AMIGO2 is a pivotal therapeutic target related to M2 polarization
            of macrophages in pancreatic ductal adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (2), 1111-1127 (2024)
   PUBMED   38189855
  REMARK    GeneRIF: AMIGO2 is a pivotal therapeutic target related to M2
            polarization of macrophages in pancreatic ductal adenocarcinoma.
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Chen,L.K., Lin,S.P., Xie,Y.H., Tan,X.P., Xiong,B.H., Zeng,X.F.,
            Zhu,C.R., Cao,S.Y., Ye,X.Y., Liu,H.J. and Wu,X.P.
  TITLE     AMIGO2 attenuates innate cisplatin sensitivity by suppression of
            GSDME-conferred pyroptosis in non-small cell lung cancer
  JOURNAL   J Cell Mol Med 27 (16), 2412-2423 (2023)
   PUBMED   37438979
  REMARK    GeneRIF: AMIGO2 attenuates innate cisplatin sensitivity by
            suppression of GSDME-conferred pyroptosis in non-small cell lung
            cancer.
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Izutsu,R., Osaki,M., Jehung,J.P., Seong,H.K. and Okada,F.
  TITLE     Liver Metastasis Formation Is Defined by AMIGO2 Expression via
            Adhesion to Hepatic Endothelial Cells in Human Gastric and
            Colorectal Cancer Cells
  JOURNAL   Pathol Res Pract 237, 154015 (2022)
   PUBMED   35843033
  REMARK    GeneRIF: Liver Metastasis Formation Is Defined by AMIGO2 Expression
            via Adhesion to Hepatic Endothelial Cells in Human Gastric and
            Colorectal Cancer Cells.
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Goto,K., Morimoto,M., Osaki,M., Tanio,A., Izutsu,R., Fujiwara,Y.
            and Okada,F.
  TITLE     The impact of AMIGO2 on prognosis and hepatic metastasis in gastric
            cancer patients
  JOURNAL   BMC Cancer 22 (1), 280 (2022)
   PUBMED   35296279
  REMARK    GeneRIF: The impact of AMIGO2 on prognosis and hepatic metastasis
            in gastric cancer patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Tao,S., Wang,Z., Feng,J., Hsu,F.C., Jin,G., Kim,S.T., Zhang,Z.,
            Gronberg,H., Zheng,L.S., Isaacs,W.B., Xu,J. and Sun,J.
  TITLE     A genome-wide search for loci interacting with known prostate
            cancer risk-associated genetic variants
  JOURNAL   Carcinogenesis 33 (3), 598-603 (2012)
   PUBMED   22219177
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Kahle,J.J., Gulbahce,N., Shaw,C.A., Lim,J., Hill,D.E.,
            Barabasi,A.L. and Zoghbi,H.Y.
  TITLE     Comparison of an expanded ataxia interactome with patient medical
            records reveals a relationship between macular degeneration and
            ataxia
  JOURNAL   Hum Mol Genet 20 (3), 510-527 (2011)
   PUBMED   21078624
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Rabenau,K.E., O'Toole,J.M., Bassi,R., Kotanides,H., Witte,L.,
            Ludwig,D.L. and Pereira,D.S.
  TITLE     DEGA/AMIGO-2, a leucine-rich repeat family member, differentially
            expressed in human gastric adenocarcinoma: effects on ploidy,
            chromosomal stability, cell adhesion/migration and tumorigenicity
  JOURNAL   Oncogene 23 (29), 5056-5067 (2004)
   PUBMED   15107827
  REMARK    GeneRIF: Stable expression of a DEGA/AMIGO-2 antisense construct
            led to altered morphology, increased ploidy, chromosomal
            instability, decreased cell adhesion/migration, and a nearly
            complete abrogation of tumorigenicity in nude mice.
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Ono,T., Sekino-Suzuki,N., Kikkawa,Y., Yonekawa,H. and Kawashima,S.
  TITLE     Alivin 1, a novel neuronal activity-dependent gene, inhibits
            apoptosis and promotes survival of cerebellar granule neurons
  JOURNAL   J Neurosci 23 (13), 5887-5896 (2003)
   PUBMED   12843293
  REMARK    GeneRIF: Expression of ali1 promotes depolarization-dependent
            survival of cerebellar granule neurons. Mouse ali1 mapped to a
            chromosome 15 locus syntenic to candidate loci for familial
            Alzheimer's disease type 5 and Parkinson's disease 8 on human
            chromosome 12.
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Kuja-Panula,J., Kiiltomaki,M., Yamashiro,T., Rouhiainen,A. and
            Rauvala,H.
  TITLE     AMIGO, a transmembrane protein implicated in axon tract
            development, defines a novel protein family with leucine-rich
            repeats
  JOURNAL   J Cell Biol 160 (6), 963-973 (2003)
   PUBMED   12629050
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004010.1.
            
            On May 4, 2019 this sequence version replaced XP_005268894.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138514.18657.1, AL833007.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000550413.2/ ENSP00000449034.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..522
                     /product="amphoterin-induced protein 2 precursor"
                     /note="amphoterin induced gene 2; amphoterin-induced
                     protein 2; transmembrane protein AMIGO2; differentially
                     expressed in gastric adenocarcinoma; alivin 1;
                     differentially expressed in gastric adenocarcinomas"
                     /calculated_mol_wt=53919
     sig_peptide     1..39
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86SJ2.1)"
                     /calculated_mol_wt=4033
     mat_peptide     40..522
                     /product="Amphoterin-induced protein 2.
                     /evidence=ECO:0000255. /id=PRO_0000014509"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SJ2.1)"
                     /calculated_mol_wt=53919
     Region          <51..>230
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          51..72
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          69..90
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          73..95
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          94..115
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          97..118
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          118..139
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          119..142
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          142..163
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          143..166
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          166..187
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          167..193
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          193..214
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          194..219
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          228..283
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          298..380
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          306..310
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          320..324
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          338..342
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            345
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          360..365
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            373
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Site            384
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Site            399..419
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SJ2.1)"
     Region          501..522
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SJ2.1)"
     CDS             1..522
                     /gene="AMIGO2"
                     /gene_synonym="ALI1; AMIGO-2; DEGA"
                     /coded_by="NM_001370299.1:669..2237"
                     /db_xref="CCDS:CCDS8751.1"
                     /db_xref="GeneID:347902"
                     /db_xref="HGNC:HGNC:24073"
                     /db_xref="MIM:615690"
ORIGIN      
        1 mslrvhtlpt llgavvrpgc rellcllmit vtvgpgasgv cptacicatd ivsctnknls
       61 kvpgnlfrli krldlsynri glldsewipv sfaklntlil rhnnitsist gsfsttpnlk
      121 cldlssnklk tvknavfqel kvlevlllyn nhisyldpsa fgglsqlqkl ylsgnfltqf
      181 pmdlyvgrfk laelmfldvs ynripsmpmh hinlvpgkql rgiylhgnpf vcdcslysll
      241 vfwyrrhfss vmdfkndytc rlwsdsrhsr qvlllqdsfm ncsdsiings fralgfihea
      301 qvgerlmvhc dsktgnantd fiwvgpdnrl lepdkemenf yvfhngslvi esprfedagv
      361 ysciamnkqr llnetvdvti nvsnftvsrs haheafntaf ttlaacvasi vlvllylylt
      421 pcpckcktkr qknmlhqsna hssilspgpa sdasaderka gagkrvvfle plkdtaagqn
      481 gkvrlfpsea viaegilkst rgksdsdsvn svfsdtpfva st
//
LOCUS       NP_612388                378 aa            linear   PRI 27-APR-2025
DEFINITION  T-cell immunoglobulin and mucin domain-containing protein 4 isoform
            1 precursor [Homo sapiens].
ACCESSION   NP_612388
VERSION     NP_612388.2
DBSOURCE    REFSEQ: accession NM_138379.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Wang,Y., Wang,Y., Liu,W., Ding,L., Zhang,X., Wang,B., Tong,Z.,
            Yue,X., Li,C., Xu,L., Wu,Z., Liang,X., Ma,C. and Gao,L.
  TITLE     TIM-4 orchestrates mitochondrial homeostasis to promote lung cancer
            progression via ANXA2/PI3K/AKT/OPA1 axis
  JOURNAL   Cell Death Dis 14 (2), 141 (2023)
   PUBMED   36806050
  REMARK    GeneRIF: TIM-4 orchestrates mitochondrial homeostasis to promote
            lung cancer progression via ANXA2/PI3K/AKT/OPA1 axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Qin,D., Liu,P., Zhou,H., Jin,J., Gong,W., Liu,K., Chen,S.,
            Huang,J., Fan,W., Tao,Z. and Xu,Y.
  TITLE     TIM-4 in macrophages contributes to nasal polyp formation through
            the TGF-beta1-mediated epithelial to mesenchymal transition in
            nasal epithelial cells
  JOURNAL   Front Immunol 13, 941608 (2022)
   PUBMED   35990621
  REMARK    GeneRIF: TIM-4 in macrophages contributes to nasal polyp formation
            through the TGF-beta1-mediated epithelial to mesenchymal transition
            in nasal epithelial cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Chow,A., Schad,S., Green,M.D., Hellmann,M.D., Allaj,V., Ceglia,N.,
            Zago,G., Shah,N.S., Sharma,S.K., Mattar,M., Chan,J., Rizvi,H.,
            Zhong,H., Liu,C., Bykov,Y., Zamarin,D., Shi,H., Budhu,S.,
            Wohlhieter,C., Uddin,F., Gupta,A., Khodos,I., Waninger,J.J.,
            Qin,A., Markowitz,G.J., Mittal,V., Balachandran,V., Durham,J.N.,
            Le,D.T., Zou,W., Shah,S.P., McPherson,A., Panageas,K., Lewis,J.S.,
            Perry,J.S.A., de Stanchina,E., Sen,T., Poirier,J.T., Wolchok,J.D.,
            Rudin,C.M. and Merghoub,T.
  TITLE     Tim-4+ cavity-resident macrophages impair anti-tumor CD8+ T cell
            immunity
  JOURNAL   Cancer Cell 39 (7), 973-988 (2021)
   PUBMED   34115989
  REMARK    GeneRIF: Tim-4(+) cavity-resident macrophages impair anti-tumor
            CD8(+) T cell immunity.
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Moon,B., Yang,S., Kim,K., Lee,J., Jeong,D. and Park,D.
  TITLE     EphA2 Interacts with Tim-4 through Association between Its FN3
            Domain and the IgV Domain of Tim-4
  JOURNAL   Cells 10 (6), 1290 (2021)
   PUBMED   34067457
  REMARK    GeneRIF: EphA2 Interacts with Tim-4 through Association between Its
            FN3 Domain and the IgV Domain of Tim-4.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Omori,S., Tsugita,M., Hoshikawa,Y., Morita,M., Ito,F.,
            Yamaguchi,S.I., Xie,Q., Noyori,O., Yamaguchi,T., Takada,A.,
            Saitoh,T., Toyokuni,S., Akiba,H., Nagata,S., Kinoshita,K. and
            Nakayama,M.
  TITLE     Tim4 recognizes carbon nanotubes and mediates phagocytosis leading
            to granuloma formation
  JOURNAL   Cell Rep 34 (6), 108734 (2021)
   PUBMED   33567275
  REMARK    GeneRIF: Tim4 recognizes carbon nanotubes and mediates phagocytosis
            leading to granuloma formation.
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Santiago,C., Ballesteros,A., Martinez-Munoz,L., Mellado,M.,
            Kaplan,G.G., Freeman,G.J. and Casasnovas,J.M.
  TITLE     Structures of T cell immunoglobulin mucin protein 4 show a
            metal-Ion-dependent ligand binding site where phosphatidylserine
            binds
  JOURNAL   Immunity 27 (6), 941-951 (2007)
   PUBMED   18083575
  REMARK    GeneRIF: Structures of T cell immunoglobulin mucin protein 4 show a
            metal-Ion-dependent ligand binding site where phosphatidylserine
            binds.
REFERENCE   7  (residues 1 to 378)
  AUTHORS   Kobayashi,N., Karisola,P., Pena-Cruz,V., Dorfman,D.M., Jinushi,M.,
            Umetsu,S.E., Butte,M.J., Nagumo,H., Chernova,I., Zhu,B.,
            Sharpe,A.H., Ito,S., Dranoff,G., Kaplan,G.G., Casasnovas,J.M.,
            Umetsu,D.T., Dekruyff,R.H. and Freeman,G.J.
  TITLE     TIM-1 and TIM-4 glycoproteins bind phosphatidylserine and mediate
            uptake of apoptotic cells
  JOURNAL   Immunity 27 (6), 927-940 (2007)
   PUBMED   18082433
  REMARK    GeneRIF: TIM-4 and TIM-1 are immunologically restricted members of
            the group of receptors whose recognition of PS is critical for the
            efficient clearance of apoptotic cells and prevention of
            autoimmunity.
REFERENCE   8  (residues 1 to 378)
  AUTHORS   Liu,T., He,S.H., Zheng,P.Y., Zhang,T.Y., Wang,B.Q. and Yang,P.C.
  TITLE     Staphylococcal enterotoxin B increases TIM4 expression in human
            dendritic cells that drives naive CD4 T cells to differentiate into
            Th2 cells
  JOURNAL   Mol Immunol 44 (14), 3580-3587 (2007)
   PUBMED   17439824
  REMARK    GeneRIF: The results demonstrate that Staphylococcus aureus derived
            Staphylococcal enterotoxin B promotes the TIM4 production in human
            dendritic cells.
REFERENCE   9  (residues 1 to 378)
  AUTHORS   Xia,Y.P., Cui,T.P. and Wu,J.M.
  TITLE     [Study on relationship between polymorphism sites of TIM4 and
            allergic asthma in the population of Han nationality from Hubei
            province of China]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 24 (2), 213-216 (2007)
   PUBMED   17407086
  REMARK    GeneRIF: The polymorphism of 8570G > A in TIM4 may be associated
            with allergic asthma in the population of Han nationality from
            Hubei province of China.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 378)
  AUTHORS   Page,N.S., Jones,G. and Stewart,G.J.
  TITLE     Genetic association studies between the T cell immunoglobulin mucin
            (TIM) gene locus and childhood atopic dermatitis
  JOURNAL   Int Arch Allergy Immunol 141 (4), 331-336 (2006)
   PUBMED   16940744
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC008988.1, AC008491.6 and AA843555.1.
            
            On Apr 11, 2009 this sequence version replaced NP_612388.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.3602.1, SRR5189664.461.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274532.7/ ENSP00000274532.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..378
                     /product="T-cell immunoglobulin and mucin
                     domain-containing protein 4 isoform 1 precursor"
                     /note="T-cell immunoglobulin and mucin domain-containing
                     protein 4; TIM-4; TIMD-4; T-cell membrane protein 4;
                     T-cell immunoglobulin mucin receptor 4"
                     /calculated_mol_wt=38599
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2998
     mat_peptide     25..378
                     /product="T-cell immunoglobulin and mucin
                     domain-containing protein 4. /id=PRO_0000042103"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96H15.2)"
                     /calculated_mol_wt=38599
     Region          28..129
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          36..40
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409574"
     Region          51..55
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409574"
     Region          95..99
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409574"
     Region          109..114
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409574"
     Region          124..127
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409574"
     Region          136..160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96H15.2)"
     Region          269..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96H15.2)"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96H15.2)"
     Site            315..335
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96H15.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6U7R4; propagated from
                     UniProtKB/Swiss-Prot (Q96H15.2)"
     CDS             1..378
                     /gene="TIMD4"
                     /gene_synonym="SMUCKLER; TIM4"
                     /coded_by="NM_138379.3:29..1165"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4332.1"
                     /db_xref="GeneID:91937"
                     /db_xref="HGNC:HGNC:25132"
                     /db_xref="MIM:610096"
ORIGIN      
        1 mskeplilwl miefwwlylt pvtsetvvte vlghrvtlpc lysswshnsn smcwgkdqcp
       61 ysgckealir tdgmrvtsrk sakyrlqgti prgdvsltil npsesdsgvy ccrievpgwf
      121 ndvkinvrln lqrasttthr tattttrrtt ttsptttrqm tttpaalptt vvttpdlttg
      181 tplqmttiav fttantclsl tpstlpeeat glltpepske gpiltaeset vlpsdswssv
      241 estsadtvll tskeskvwdl pstshvsmwk tsdsvsspqp gasdtavpeq nkttktgqmd
      301 gipmsmknem pisqllmiia pslgfvlfal fvafllrgkl metycsqkht rldyigdskn
      361 vlndvqhgre dedglftl
//
LOCUS       NP_443073                268 aa            linear   PRI 27-APR-2025
DEFINITION  testis-specific serine/threonine-protein kinase 3 [Homo sapiens].
ACCESSION   NP_443073
VERSION     NP_443073.1
DBSOURCE    REFSEQ: accession NM_052841.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Nayyab,S., Gervasi,M.G., Tourzani,D.A., Caraballo,D.A., Jha,K.N.,
            Teves,M.E., Cui,W., Georg,G.I., Visconti,P.E. and Salicioni,A.M.
  TITLE     TSSK3, a novel target for male contraception, is required for
            spermiogenesis
  JOURNAL   Mol Reprod Dev 88 (11), 718-730 (2021)
   PUBMED   34623009
  REMARK    GeneRIF: TSSK3, a novel target for male contraception, is required
            for spermiogenesis.
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Bucko-Justyna,M., Lipinski,L., Burgering,B.M. and Trzeciak,L.
  TITLE     Characterization of testis-specific serine-threonine kinase 3 and
            its activation by phosphoinositide-dependent kinase-1-dependent
            signalling
  JOURNAL   FEBS J 272 (24), 6310-6323 (2005)
   PUBMED   16336268
  REMARK    GeneRIF: PDK1-induced phosphorylation increased in vitro TSSK3
            kinase activity, suggesting that TSSK3 can be regulated in the same
            way as AGC kinase family members. The peptide sequence RRSSSY
            containing Ser5 is identified as a target for TSSK3 phosphorylation
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Visconti,P.E., Hao,Z., Purdon,M.A., Stein,P., Balsara,B.R.,
            Testa,J.R., Herr,J.C., Moss,S.B. and Kopf,G.S.
  TITLE     Cloning and chromosomal localization of a gene encoding a novel
            serine/threonine kinase belonging to the subfamily of
            testis-specific kinases
  JOURNAL   Genomics 77 (3), 163-170 (2001)
   PUBMED   11597141
  REMARK    GeneRIF: human homolog of mouse stk22d; It was cloned and found it
            to be expressed exclusively in the testis.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC035354.1.
            
            Summary: This gene encodes a kinase expressed exclusively in the
            testis that is thought to play a role in either germ cell
            differentiation or mature sperm function. [provided by RefSeq, Jul
            2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035354.1, SRR5189667.54114.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373534.4/ ENSP00000362634.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..268
                     /product="testis-specific serine/threonine-protein kinase
                     3"
                     /EC_number="2.7.11.1"
                     /note="spermiogenesis associated 3; testis-specific
                     serine/threonine kinase 22C; TSK-3; TSSK-3;
                     testis-specific kinase 3; serine/threonine-protein kinase
                     22C"
                     /calculated_mol_wt=29971
     Region          9..265
                     /region_name="STKc_TSSK3-like"
                     /note="Catalytic domain of testis-specific
                     serine/threonine kinase 3 and similar proteins; cd14163"
                     /db_xref="CDD:271065"
     Site            order(16..20,24,37,39,71,88..91,95,97..98,100,133..134,
                     136,138..139,141,150..151,154,170..174,176,206..209)
                     /site_type="active"
                     /db_xref="CDD:271065"
     Site            order(16..19,24,37,39,71,88..91,95,138..139,141,150..151)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271065"
     Site            order(95,97..98,100,134,136,138,154,170..174,176,206..209)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271065"
     Site            150..174
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271065"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2E1; propagated from
                     UniProtKB/Swiss-Prot (Q96PN8.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2E1; propagated from
                     UniProtKB/Swiss-Prot (Q96PN8.1)"
     CDS             1..268
                     /gene="TSSK3"
                     /gene_synonym="SPOGA3; STK22C; STK22D; TSK3"
                     /coded_by="NM_052841.4:164..970"
                     /db_xref="CCDS:CCDS362.1"
                     /db_xref="GeneID:81629"
                     /db_xref="HGNC:HGNC:15473"
                     /db_xref="MIM:607660"
ORIGIN      
        1 medfllsngy qlgktigegt yskvkeafsk khqrkvaikv idkmggpeef iqrflprelq
       61 ivrtldhkni iqvyemlesa dgkiclvmel aeggdvfdcv lnggplpesr akalfrqmve
      121 airychgcgv ahrdlkcena llqgfnlklt dfgfakvlpk shrelsqtfc gstayaapev
      181 lqgiphdskk gdvwsmgvvl yvmlcaslpf ddtdipkmlw qqqkgvsfpt hlsisadcqd
      241 llkrllepdm ilrpsieevs whpwlast
//
LOCUS       NP_001013756             263 aa            linear   PRI 27-APR-2025
DEFINITION  ret finger protein-like 4B [Homo sapiens].
ACCESSION   NP_001013756 XP_498131
VERSION     NP_001013756.2
DBSOURCE    REFSEQ: accession NM_001013734.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK122906.1, BC132796.1 and AL365214.16.
            
            On Jul 25, 2007 this sequence version replaced NP_001013756.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK122906.1, SRR5189667.138965.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000441065.3/ ENSP00000423391.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..263
                     /product="ret finger protein-like 4B"
                     /note="RING finger protein 211"
                     /calculated_mol_wt=29791
     Region          1..63
                     /region_name="RING-HC_RFPL4B"
                     /note="RING finger, HC subclass, found in Ret finger
                     protein-like 4B (RFPL4B) and similar proteins; cd16623"
                     /db_xref="CDD:438285"
     Region          93..262
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     CDS             1..263
                     /gene="RFPL4B"
                     /gene_synonym="RNF211"
                     /coded_by="NM_001013734.3:313..1104"
                     /db_xref="CCDS:CCDS34515.1"
                     /db_xref="GeneID:442247"
                     /db_xref="HGNC:HGNC:33264"
ORIGIN      
        1 makrlqaels cpvcldffsc sislscthvf cfdciqryil enhdframcp lcrdvvkvpa
       61 leewqvsvlt lmtkqhnsrl eqslhvreel rhfredvtld aatassllvf sndlrsaqck
      121 kihhdltkdp rlacvlgtpc fssgqhywev evgevkswsl gvckepadrk sndlfpehgf
      181 wismkagaih anthleripa sprlrrvgif ldadleeiqf fdvdnnvliy thdgffslel
      241 lcpffclell gegesgnvlt icp
//
LOCUS       NP_006576                548 aa            linear   PRI 27-APR-2025
DEFINITION  T-complex protein 1 subunit theta isoform 1 [Homo sapiens].
ACCESSION   NP_006576 XP_375936
VERSION     NP_006576.2
DBSOURCE    REFSEQ: accession NM_006585.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Gestaut,D., Roh,S.H., Ma,B., Pintilie,G., Joachimiak,L.A.,
            Leitner,A., Walzthoeni,T., Aebersold,R., Chiu,W. and Frydman,J.
  TITLE     The Chaperonin TRiC/CCT Associates with Prefoldin through a
            Conserved Electrostatic Interface Essential for Cellular
            Proteostasis
  JOURNAL   Cell 177 (3), 751-765 (2019)
   PUBMED   30955883
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Yang,X., Ren,H., Shao,Y., Sun,Y., Zhang,L., Li,H., Zhang,X.,
            Yang,X., Yu,W. and Fu,J.
  TITLE     Chaperonin-containing T-complex protein 1 subunit 8 promotes cell
            migration and invasion in human esophageal squamous cell carcinoma
            by regulating alpha-actin and beta-tubulin expression
  JOURNAL   Int J Oncol 52 (6), 2021-2030 (2018)
   PUBMED   29620162
  REMARK    GeneRIF: Study demonstrated that CCT8 expression is widely
            upregulated in esophageal squamous cell carcinoma (ESCC), and
            enhanced the migration and invasion of ESCC cells, indicating that
            ectopic CCT8 expression contributes to the highly aggressive nature
            of ESCC probably by increasing alpha-actin and beta-tubulin
            expression.
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Yokota,S., Yanagi,H., Yura,T. and Kubota,H.
  TITLE     Cytosolic chaperonin-containing t-complex polypeptide 1 changes the
            content of a particular subunit species concomitant with substrate
            binding and folding activities during the cell cycle
  JOURNAL   Eur J Biochem 268 (17), 4664-4673 (2001)
   PUBMED   11532003
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Hynes,G.M. and Willison,K.R.
  TITLE     Individual subunits of the eukaryotic cytosolic chaperonin mediate
            interactions with binding sites located on subdomains of beta-actin
  JOURNAL   J Biol Chem 275 (25), 18985-18994 (2000)
   PUBMED   10748209
REFERENCE   8  (residues 1 to 548)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   9  (residues 1 to 548)
  AUTHORS   Yamazaki,M., Ono,A., Watanabe,K., Sasaki,K., Tashiro,H. and
            Nomura,T.
  TITLE     Nucleotide sequence surrounding the locus marker D21S246 on human
            chromosome 21
  JOURNAL   DNA Res 2 (4), 187-189 (1995)
   PUBMED   8590283
REFERENCE   10 (residues 1 to 548)
  AUTHORS   Kubota,H., Hynes,G. and Willison,K.
  TITLE     The eighth Cct gene, Cctq, encoding the theta subunit of the
            cytosolic chaperonin containing TCP-1
  JOURNAL   Gene 154 (2), 231-236 (1995)
   PUBMED   7890169
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC072001.1.
            
            On or before Aug 30, 2004 this sequence version replaced
            XP_375936.1, NP_006576.1.
            
            Summary: This gene encodes the theta subunit of the CCT chaperonin,
            which is abundant in the eukaryotic cytosol and may be involved in
            the transport and assembly of newly synthesized proteins.
            Alternative splicing results in multiple transcript variants of
            this gene. A pseudogene related to this gene is located on
            chromosome 1. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072001.1, SRR1660807.58830.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000286788.9/ ENSP00000286788.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..548
                     /product="T-complex protein 1 subunit theta isoform 1"
                     /note="T-complex protein 1 subunit theta; CCT-theta;
                     TCP-1-theta; renal carcinoma antigen NY-REN-15; chaperonin
                     containing TCP1, subunit 8 (theta); chaperonin containing
                     T-complex polypeptide 1 subunit 8"
                     /calculated_mol_wt=59490
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.7;
                     propagated from UniProtKB/Swiss-Prot (P50990.4)"
     Region          10..539
                     /region_name="chap_CCT_theta"
                     /note="T-complex protein 1, theta subunit; TIGR02346"
                     /db_xref="CDD:274087"
     Site            order(20,24,52..55,57,75,77,81,85,88,382,520..526)
                     /site_type="other"
                     /note="ring oligomerisation interface [polypeptide
                     binding]"
                     /db_xref="CDD:239457"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P50990.4)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            order(47..49,99,103,166,394,412,452,497,499)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239457"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            400
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            order(432,450,459,461..462,465)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239457"
     Site            466
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Region          529..548
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50990.4)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     CDS             1..548
                     /gene="CCT8"
                     /gene_synonym="C21orf112; Cctq; D21S246; PRED71"
                     /coded_by="NM_006585.4:59..1705"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33528.1"
                     /db_xref="GeneID:10694"
                     /db_xref="HGNC:HGNC:1623"
                     /db_xref="MIM:617786"
ORIGIN      
        1 malhvpkapg faqmlkegak hfsgleeavy rniqackela qttrtaygpn gmnkmvinhl
       61 eklfvtndaa tilrelevqh paakmivmas hmqeqevgdg tnfvlvfaga llelaeellr
      121 iglsvsevie gyeiacrkah eilpnlvccs aknlrdidev ssllrtsims kqygnevfla
      181 kliaqacvsi fpdsghfnvd nirvckilgs gissssvlhg mvfkketegd vtsvkdakia
      241 vyscpfdgmi tetkgtvlik taeelmnfsk geenlmdaqv kaiadtganv vvtggkvadm
      301 alhyankyni mlvrlnskwd lrrlcktvga talprltppv leemghcdsv ylsevgdtqv
      361 vvfkhekedg aistivlrgs tdnlmddier avddgvntfk vltrdkrlvp gggateiela
      421 kqitsygetc pgleqyaikk faeafeaipr alaensgvka nevisklyav hqegnknvgl
      481 dieaevpavk dmleagildt ylgkywaikl atnaavtvlr vdqiimakpa ggpkppsgkk
      541 dwdddqnd
//
LOCUS       NP_110445                396 aa            linear   PRI 27-APR-2025
DEFINITION  probable splicing factor YJU2B isoform a [Homo sapiens].
ACCESSION   NP_110445
VERSION     NP_110445.1
DBSOURCE    REFSEQ: accession NM_030818.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Lammers,R., Gross,G., Mayr,U. and Collins,J.
  TITLE     Alternative mechanisms for gene activation induced by
            poly(rI).poly(rC) and Newcastle disease virus
  JOURNAL   Eur J Biochem 178 (1), 93-99 (1988)
   PUBMED   3203696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM547551.1 and BC002905.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1, 2, 3, and 4 all encode the same isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.965470.1,
                                           SRR3476690.961148.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221554.13/ ENSP00000221554.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..396
                     /product="probable splicing factor YJU2B isoform a"
                     /note="coiled-coil domain-containing protein 130; 9 kDa
                     protein; coiled-coil domain containing 130; probable
                     splicing factor YJU2B"
                     /calculated_mol_wt=44671
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13994.2)"
     Region          9..395
                     /region_name="Saf4_Yju2"
                     /note="Saf4/Yju2 protein; pfam04502"
                     /db_xref="CDD:461333"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P13994.2)"
     Region          295..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13994.2)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P13994.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P13994.2)"
     CDS             1..396
                     /gene="YJU2B"
                     /gene_synonym="CCDC130"
                     /coded_by="NM_030818.4:262..1452"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12296.1"
                     /db_xref="GeneID:81576"
                     /db_xref="HGNC:HGNC:28118"
ORIGIN      
        1 mgerkgvnky yppdfnpekh gslnryhnsh plrerarkls qgiliirfem pyniwcdgck
       61 nhigmgvryn aekkkvgnyy ttpiyrfrmk chlcvnyiem qtdpancdyv ivsgaqrkee
      121 rwdmadneqv lttehekkqk letdamfrle hgeadrstlk kalptlshiq eaqsawkddf
      181 alnsmlrrrf rekkkaiqee eerdqalqak asltiplvpe teddrklaal lkfhtldsye
      241 dkqklkrtei isrswfpsap gsassskvsg vlkklaqsrr talatspitv gdlgivrrrs
      301 rdvpespqha adtpksgepr vpeeaaqdrp mspgdcppet tetpkcsspr gqegsrqdkp
      361 lspagssqea adtpdtrhpc slgsslvady sdsese
//
LOCUS       NP_001180552             186 aa            linear   PRI 27-APR-2025
DEFINITION  piRNA-mediated silencing protein C19orf84 [Homo sapiens].
ACCESSION   NP_001180552 XP_001134195 XP_001134326 XP_001726110
VERSION     NP_001180552.1
DBSOURCE    REFSEQ: accession NM_001193623.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Zoch,A., Konieczny,G., Auchynnikava,T., Stallmeyer,B., Rotte,N.,
            Heep,M., Berrens,R.V., Schito,M., Kabayama,Y., Schopp,T.,
            Kliesch,S., Houston,B., Nagirnaja,L., O'Bryan,M.K., Aston,K.I.,
            Conrad,D.F., Rappsilber,J., Allshire,R.C., Cook,A.G., Tuttelmann,F.
            and O'Carroll,D.
  TITLE     C19ORF84 connects piRNA and DNA methylation machineries to defend
            the mammalian germ line
  JOURNAL   Mol Cell 84 (6), 1021-1035 (2024)
   PUBMED   38359823
  REMARK    GeneRIF: C19ORF84 connects piRNA and DNA methylation machineries to
            defend the mammalian germ line.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008750.9 and BC043532.1.
            
            On or before Aug 7, 2010 this sequence version replaced
            XP_001134195.1, XP_001726110.1, XP_001134326.1.
            
            Transcript Variant: This variant (1) encodes the supported protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC043532.1, BI827168.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000574814.2/ ENSP00000458772.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..186
                     /product="piRNA-mediated silencing protein C19orf84"
                     /note="uncharacterized protein C19orf84"
                     /calculated_mol_wt=19483
     Region          1..186
                     /region_name="DUF5549"
                     /note="Family of unknown function (DUF5549); pfam17703"
                     /db_xref="CDD:407588"
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (I3L1E1.1)"
     Region          89..186
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (I3L1E1.1)"
     CDS             1..186
                     /gene="C19orf84"
                     /coded_by="NM_001193623.2:80..640"
                     /db_xref="CCDS:CCDS58676.1"
                     /db_xref="GeneID:147646"
                     /db_xref="HGNC:HGNC:27112"
ORIGIN      
        1 meqpkdgagp egnnlslpss gtepwppapl pappplllns tdpthlglpe svasvtvpir
       61 ldtlscllhs allgaytfqq alpscpccsq aghsqpgavr rpprgrggwe vrhrpgwgrg
      121 lhrrglgrae qpergraggp gagprtppmt lpspptlpaq dgkkeargpe ppletplaae
      181 dwetey
//
LOCUS       NP_001070143             528 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 626 isoform 1 [Homo sapiens].
ACCESSION   NP_001070143
VERSION     NP_001070143.1
DBSOURCE    REFSEQ: accession NM_001076675.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Del-Aguila,J.L., Beitelshees,A.L., Cooper-Dehoff,R.M.,
            Chapman,A.B., Gums,J.G., Bailey,K., Gong,Y., Turner,S.T.,
            Johnson,J.A. and Boerwinkle,E.
  TITLE     Genome-wide association analyses suggest NELL1 influences adverse
            metabolic response to HCTZ in African Americans
  JOURNAL   Pharmacogenomics J 14 (1), 35-40 (2014)
   PUBMED   23400010
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010636.6.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.128093.1,
                                           SRR1803611.194313.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMN03267765
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000601440.6/ ENSP00000469958.1
            RefSeq Select criteria :: based on manual assertion
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p12"
     Protein         1..528
                     /product="zinc finger protein 626 isoform 1"
                     /note="CTC-513N18.7"
                     /calculated_mol_wt=60762
     Region          4..62
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          177..195
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          199..520
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          203..223
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(208,210,212,214..215,218..219,222,236,238,242..243,
                     246..247,250,264,266,268,270..271,274..275,278)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          231..251
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          259..279
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          287..307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          315..335
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          343..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(348,350,352,354..355,358..359,362,376,378,382..383,
                     386..387,390,404,406,408,410..411,414..415,418)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          371..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          399..419
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          427..447
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          455..475
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          483..502
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..528
                     /gene="ZNF626"
                     /coded_by="NM_001076675.3:126..1712"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42535.1"
                     /db_xref="GeneID:199777"
                     /db_xref="HGNC:HGNC:30461"
ORIGIN      
        1 mgplqfrdva iefsleewhc ldtaqrnlyr nvmlenysnl vflgitvskp dlitcleqgr
       61 kpltmkrnem iakpsvmcsh faqdlwpeqs mkdsfqkvvl rryekcehdn lqlkkgcisv
      121 deckvhkegy nelnqclttt prkicqcdky vkvlhqfpns ngqkrghtgk kpfkyiecgk
      181 afkqfstltt hkkihtggkp ykceecgkaf nhscsltrhk kihtgekpyk ceecgkafkh
      241 sstltthkrn htgekpykcd kcgkafmsss tlskheiiht ekkpykceec gkafnrsstl
      301 tthkiihtge kpykceecdk afkysytltt hkrihtedkp ykceecgkaf kysstltthk
      361 rihtgekpyk ceecgkafkr ssdltthkii htgekpykce ecgkafkyss nltthkkiht
      421 gerpykceec gkafnqssil tthrrihtge kfykceecgk afkcssnltt hkkihtgerp
      481 ykceecgkaf nqssiltthe riilernstn vknvakpssg phtllhir
//
LOCUS       NP_001265492             441 aa            linear   PRI 27-APR-2025
DEFINITION  collagen alpha-1(XXVI) chain isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001265492
VERSION     NP_001265492.1
DBSOURCE    REFSEQ: accession NM_001278563.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Cappelletto,A., Alfi,E., Volf,N., Vu,T.V.A., Bortolotti,F.,
            Ciucci,G., Vodret,S., Fantuz,M., Perin,M., Colliva,A., Rozzi,G.,
            Rossi,M., Ruozi,G., Zentilin,L., Vuerich,R., Borin,D., Lapasin,R.,
            Piazza,S., Chiesa,M., Lorizio,D., Triboli,L., Kumar,S., Morello,G.,
            Tripodo,C., Pinamonti,M., Piperno,G.M., Benvenuti,F., Rustighi,A.,
            Jo,H., Piccolo,S., Del Sal,G., Carrer,A., Giacca,M. and
            Zacchigna,S.
  TITLE     EMID2 is a novel biotherapeutic for aggressive cancers identified
            by in vivo screening
  JOURNAL   J Exp Clin Cancer Res 43 (1), 15 (2024)
   PUBMED   38195652
  REMARK    GeneRIF: EMID2 is a novel biotherapeutic for aggressive cancers
            identified by in vivo screening.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Deng,X., Sabino,E.C., Cunha-Neto,E., Ribeiro,A.L., Ianni,B.,
            Mady,C., Busch,M.P. and Seielstad,M.
  CONSRTM   REDSII Chagas Study Group from the NHLBI Retrovirus Epidemiology
            Donor Study-II Component International
  TITLE     Genome wide association study (GWAS) of Chagas cardiomyopathy in
            Trypanosoma cruzi seropositive subjects
  JOURNAL   PLoS One 8 (11), e79629 (2013)
   PUBMED   24324551
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Soteriou,D., Iskender,B., Byron,A., Humphries,J.D.,
            Borg-Bartolo,S., Haddock,M.C., Baxter,M.A., Knight,D.,
            Humphries,M.J. and Kimber,S.J.
  TITLE     Comparative proteomic analysis of supportive and unsupportive
            extracellular matrix substrates for human embryonic stem cell
            maintenance
  JOURNAL   J Biol Chem 288 (26), 18716-18731 (2013)
   PUBMED   23658023
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Pasaje,C.F., Bae,J.S., Park,B.L., Cheong,H.S., Kim,J.H., Jang,A.S.,
            Uh,S.T., Park,C.S. and Shin,H.D.
  TITLE     Possible role of EMID2 on nasal polyps pathogenesis in Korean
            asthma patients
  JOURNAL   BMC Med Genet 13, 2 (2012)
   PUBMED   22217332
  REMARK    GeneRIF: 13 EMID2 variants were significantly associated with the
            presence of nasal polyps in the overall asthma group.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Lettice,L.A., Daniels,S., Sweeney,E., Venkataraman,S.,
            Devenney,P.S., Gautier,P., Morrison,H., Fantes,J., Hill,R.E. and
            FitzPatrick,D.R.
  TITLE     Enhancer-adoption as a mechanism of human developmental disease
  JOURNAL   Hum Mutat 32 (12), 1492-1499 (2011)
   PUBMED   21948517
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Pasaje,C.F., Kim,J.H., Park,B.L., Cheong,H.S., Kim,M.K., Choi,I.S.,
            Cho,S.H., Hong,C.S., Lee,Y.W., Lee,J.Y., Koh,I.S., Park,T.J.,
            Lee,J.S., Kim,Y., Bae,J.S., Park,C.S. and Shin,H.D.
  TITLE     A possible association of EMID2 polymorphisms with aspirin
            hypersensitivity in asthma
  JOURNAL   Immunogenetics 63 (1), 13-21 (2011)
   PUBMED   21086123
  REMARK    GeneRIF: EMID2 may be a susceptible genetic factor for aspirin
            hypersensitivity among asthmatics in Korean population.
            GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 441)
  AUTHORS   Sato,K., Yomogida,K., Wada,T., Yorihuzi,T., Nishimune,Y.,
            Hosokawa,N. and Nagata,K.
  TITLE     Type XXVI collagen, a new member of the collagen family, is
            specifically expressed in the testis and ovary
  JOURNAL   J Biol Chem 277 (40), 37678-37684 (2002)
   PUBMED   12145293
REFERENCE   9  (residues 1 to 441)
  AUTHORS   Leimeister,C., Steidl,C., Schumacher,N., Erhard,S. and Gessler,M.
  TITLE     Developmental expression and biochemical characterization of Emu
            family members
  JOURNAL   Dev Biol 249 (2), 204-218 (2002)
   PUBMED   12221002
REFERENCE   10 (residues 1 to 441)
  AUTHORS   van der Rest,M. and Garrone,R.
  TITLE     Collagen family of proteins
  JOURNAL   FASEB J 5 (13), 2814-2823 (1991)
   PUBMED   1916105
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CX163123.1, AJ416091.1,
            BC085006.1, BU845945.1 and BC110393.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein containing an emilin domain
            and two collagen stretches. This gene may be associated with
            aspirin-intolerant asthma. Alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.56930.1,
                                           SRR1660807.420982.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145774, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313669.12/ ENSP00000318234.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..441
                     /product="collagen alpha-1(XXVI) chain isoform 1
                     precursor"
                     /note="collagen alpha-1(XXVI) chain; emilin and multimerin
                     domain-containing protein 2; EMI domain containing 2;
                     collagen, type XXVI, alpha 1"
                     /calculated_mol_wt=43319
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2081
     mat_peptide     21..441
                     /product="Collagen alpha-1(XXVI) chain.
                     /id=PRO_0000007825"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96A83.1)"
                     /calculated_mol_wt=43319
     Region          53..123
                     /region_name="EMI"
                     /note="EMI domain; pfam07546"
                     /db_xref="CDD:462204"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96A83.1)"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96A83.1)"
     Region          156..362
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96A83.1)"
     Region          390..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96A83.1)"
     CDS             1..441
                     /gene="COL26A1"
                     /gene_synonym="EMI6; EMID2; EMU2; SH2B"
                     /coded_by="NM_001278563.3:159..1484"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS64739.1"
                     /db_xref="GeneID:136227"
                     /db_xref="HGNC:HGNC:18038"
                     /db_xref="MIM:608927"
ORIGIN      
        1 mklalllpwa ccclcgsala tgflypfsaa alqqhgypep gagspgsgya srrhwchhtv
       61 trtvscqvqn gsetvvqrvy qscrwpgpca nlvsyrtlir ptyrvsyrtv tvlewrccpg
      121 ftgsncdeec mnctrlsdms erlttleakv llleaaerps spdndlpape stpptwnedf
      181 lpdaiplahp vprqrrptgp agppgqtgpp gpagppgskg drgqtgekgp agppgllgpp
      241 gprglpgemg rpgppgppgp agnpgpspns pqgalyslqp ptdkdngdsr lasaivdtvl
      301 agvpgprgpp gppgppgprg ppgppgtpgs qglagergtv gpsgepgvkg eegekaatae
      361 gegvqqlrea lkilaervli lehmigihdp laspeggsgq daalranlkm krggaqpdgv
      421 laallgpdpg qksvdqassr k
//
LOCUS       NP_932763                172 aa            linear   ROD 27-APR-2025
DEFINITION  bone marrow stromal antigen 2 [Mus musculus].
ACCESSION   NP_932763 XP_134266
VERSION     NP_932763.1
DBSOURCE    REFSEQ: accession NM_198095.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Li,Y., Chen,W., Zhu,X., Mei,H., Steinhoff,M., Buddenkotte,J.,
            Wang,J., Zhang,W., Li,Z., Dai,X., Shan,C., Wang,J. and Meng,J.
  TITLE     Neuronal BST2: A Pruritic Mediator alongside Protease-Activated
            Receptor 2 in the IL-27-Driven Itch Pathway
  JOURNAL   J Invest Dermatol 144 (8), 1829-1842 (2024)
   PUBMED   38360199
  REMARK    GeneRIF: Neuronal BST2: A Pruritic Mediator alongside
            Protease-Activated Receptor 2 in the IL-27-Driven Itch Pathway.
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Liu,H., Zhou,R., Li,S., Dong,J., Fang,Y., Luo,Y., Su,H., Lai,B.,
            Liang,L., Zhang,D., Zhang,Y., Shyy,J.Y., Zhou,B., Yuan,Z. and
            Wang,Y.
  TITLE     Epigenetic repression of Cend1 by lysine-specific demethylase 1 is
            essential for murine heart development
  JOURNAL   iScience 27 (1), 108722 (2023)
   PUBMED   38226173
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Li,J., He,Y., Qu,Y., Ren,C., Wang,X., Cheng,Y., Sun,L., Zhang,X.
            and Zhang,G.
  TITLE     Promotion of BST2 expression by the transcription factor IRF6
            affects the progression of endometriosis
  JOURNAL   Front Immunol 14, 1115504 (2023)
   PUBMED   37143676
  REMARK    GeneRIF: Promotion of BST2 expression by the transcription factor
            IRF6 affects the progression of endometriosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Urata,S., Yamaguchi,S., Nambu,A., Sudo,K., Nakae,S. and Yasuda,J.
  TITLE     The roles of BST-2 in murine B cell development and on virus
            propagation
  JOURNAL   Microbiol Immunol 67 (3), 105-113 (2023)
   PUBMED   36604771
  REMARK    GeneRIF: The roles of BST-2 in murine B cell development and on
            virus propagation.
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Radoshitzky,S.R., Dong,L., Chi,X., Clester,J.C., Retterer,C.,
            Spurgers,K., Kuhn,J.H., Sandwick,S., Ruthel,G., Kota,K., Boltz,D.,
            Warren,T., Kranzusch,P.J., Whelan,S.P. and Bavari,S.
  TITLE     Infectious Lassa virus, but not filoviruses, is restricted by
            BST-2/tetherin
  JOURNAL   J Virol 84 (20), 10569-10580 (2010)
   PUBMED   20686043
  REMARK    GeneRIF: Elevated cellular levels of BST-2 inhibited the release of
            virus-like particles consisting of the matrix proteins of multiple
            highly virulent NIAID Priority Pathogens
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Schliemann,C., Roesli,C., Kamada,H., Borgia,B., Fugmann,T.,
            Klapper,W. and Neri,D.
  TITLE     In vivo biotinylation of the vasculature in B-cell lymphoma
            identifies BST-2 as a target for antibody-based therapy
  JOURNAL   Blood 115 (3), 736-744 (2010)
   PUBMED   19903902
  REMARK    GeneRIF: Targeting BST-2 with 2 independent monoclonal antibodies
            delayed lymphoma growth in a syngeneic mouse model of the disease.
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Li,X., Kaloyanova,D., van Eijk,M., Eerland,R., van der Goot,G.,
            Oorschot,V., Klumperman,J., Lottspeich,F., Starkuviene,V.,
            Wieland,F.T. and Helms,J.B.
  TITLE     Involvement of a Golgi-resident GPI-anchored protein in maintenance
            of the Golgi structure
  JOURNAL   Mol Biol Cell 18 (4), 1261-1271 (2007)
   PUBMED   17251550
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Blasius,A.L., Giurisato,E., Cella,M., Schreiber,R.D., Shaw,A.S. and
            Colonna,M.
  TITLE     Bone marrow stromal cell antigen 2 is a specific marker of type I
            IFN-producing cells in the naive mouse, but a promiscuous cell
            surface antigen following IFN stimulation
  JOURNAL   J Immunol 177 (5), 3260-3265 (2006)
   PUBMED   16920966
  REMARK    GeneRIF: BST2 resides within an intracellular compartment
            corresponding to the Golgi apparatus, and may be involved in
            trafficking secreted cytokines in type I IFN-producing cells
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Ohtomo,T., Sugamata,Y., Ozaki,Y., Ono,K., Yoshimura,Y., Kawai,S.,
            Koishihara,Y., Ozaki,S., Kosaka,M., Hirano,T. and Tsuchiya,M.
  TITLE     Molecular cloning and characterization of a surface antigen
            preferentially overexpressed on multiple myeloma cells
  JOURNAL   Biochem Biophys Res Commun 258 (3), 583-591 (1999)
   PUBMED   10329429
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY166837.1 and BC087949.1.
            
            On Dec 17, 2003 this sequence version replaced XP_134266.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087949.1, SRR7345562.1840805.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 34.43 cM"
     Protein         1..172
                     /product="bone marrow stromal antigen 2"
                     /note="HM1.24 antigen; DAMP-1 protein homolog; tetherin"
                     /calculated_mol_wt=19021
     mat_peptide     1..152
                     /product="Bone marrow stromal antigen 2.
                     /id=PRO_0000253553"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2Q8.1)"
                     /calculated_mol_wt=17031
     Site            31..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2Q8.1)"
     Region          54..143
                     /region_name="BST2"
                     /note="Bone marrow stromal antigen 2; pfam16716"
                     /db_xref="CDD:465245"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q8R2Q8.1)"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, atypical.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q8R2Q8.1)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R2Q8.1)"
     CDS             1..172
                     /gene="Bst2"
                     /gene_synonym="2310015I10Rik; Bst-2; CD317; DAMP-1; GREG"
                     /coded_by="NM_198095.3:46..564"
                     /db_xref="CCDS:CCDS22397.1"
                     /db_xref="GeneID:69550"
                     /db_xref="MGI:MGI:1916800"
ORIGIN      
        1 mapsfyhylp vpmdemggkq gwgshrqwlg aailvvlfgv tlviltiyfa vtansvacrd
       61 glraqaecrn tthllqrqlt rtqdsllqae tqanscnltv vtlqeslekk vsqaleqqar
      121 ikelenevtk lnqelenlri qketsstvqv nsgssmvvss llvlkvslfl lf
//
LOCUS       NP_001357434             225 aa            linear   PRI 27-APR-2025
DEFINITION  phosphoserine phosphatase [Homo sapiens].
ACCESSION   NP_001357434 XP_005271831
VERSION     NP_001357434.1
DBSOURCE    REFSEQ: accession NM_001370505.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Rawat,V., Malvi,P., Della Manna,D., Yang,E.S., Bugide,S., Zhang,X.,
            Gupta,R. and Wajapeyee,N.
  TITLE     PSPH promotes melanoma growth and metastasis by metabolic
            deregulation-mediated transcriptional activation of NR4A1
  JOURNAL   Oncogene 40 (13), 2448-2462 (2021)
   PUBMED   33674745
  REMARK    GeneRIF: PSPH promotes melanoma growth and metastasis by metabolic
            deregulation-mediated transcriptional activation of NR4A1.
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Park,S.M., Seo,E.H., Bae,D.H., Kim,S.S., Kim,J., Lin,W., Kim,K.H.,
            Park,J.B., Kim,Y.S., Yin,J. and Kim,S.Y.
  TITLE     Phosphoserine Phosphatase Promotes Lung Cancer Progression through
            the Dephosphorylation of IRS-1 and a Noncanonical
            L-Serine-Independent Pathway
  JOURNAL   Mol Cells 42 (8), 604-616 (2019)
   PUBMED   31446747
  REMARK    GeneRIF: a specific interaction between PSPH and IRS1 and the
            dephosphorylation of phospho-IRS-1 by PSPH in lung cancer cells,
            was identified.
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Haufroid,M., Mirgaux,M., Leherte,L. and Wouters,J.
  TITLE     Crystal structures and snapshots along the reaction pathway of
            human phosphoserine phosphatase
  JOURNAL   Acta Crystallogr D Struct Biol 75 (Pt 6), 592-604 (2019)
   PUBMED   31205021
  REMARK    GeneRIF: three new high-resolution crystal structures of hPSP
            (1.5-2.0 A) in complexes with phosphoserine and with serine, which
            are the substrate and the product of the reaction, respectively,
            and in complex with a noncleavable substrate analogue (homocysteic
            acid) are presented.
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Liao,L., Ge,M., Zhan,Q., Huang,R., Ji,X., Liang,X. and Zhou,X.
  TITLE     PSPH Mediates the Metastasis and Proliferation of Non-small Cell
            Lung Cancer through MAPK Signaling Pathways
  JOURNAL   Int J Biol Sci 15 (1), 183-194 (2019)
   PUBMED   30662358
  REMARK    GeneRIF: The results suggest that PSPH may act as a putative
            oncogene and a potential therapeutic target in NSCLC.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 225)
  AUTHORS   van der Crabben,S.N. and de Koning,T.J.
  TITLE     Serine Deficiency Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37347880
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Veeranna and Shetty,K.T.
  TITLE     Phosphoserine phosphatase of human brain: partial purification,
            characterization, regional distribution, and effect of certain
            modulators including psychoactive drugs
  JOURNAL   Neurochem Res 15 (12), 1203-1210 (1990)
   PUBMED   1965857
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Minelli,A., Piantanida,M., Maserati,E., Campagnoli,E., Pasquali,F.
            and Danesino,C.
  TITLE     Gene dosage effect in acquired monosomy 7: distinct behaviour of
            beta-glucuronidase and phosphoserine phosphatase
  JOURNAL   Genes Chromosomes Cancer 1 (3), 216-220 (1990)
   PUBMED   1964582
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Novelli,G. and Dallapiccola,B.
  TITLE     Gene dosage studies regionally assign the phosphoserine phosphatase
            gene to 7p15.1 or 2
  JOURNAL   Ann Genet 31 (3), 195-196 (1988)
   PUBMED   2851960
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Moro-Furlani,A.M., Turner,V.S. and Hopkinson,D.A.
  TITLE     Genetical and biochemical studies on human phosphoserine
            phosphatase
  JOURNAL   Ann Hum Genet 43 (4), 323-333 (1980)
   PUBMED   6249179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092579.3.
            
            On May 9, 2019 this sequence version replaced XP_005271831.1.
            
            Summary: The protein encoded by this gene belongs to a subfamily of
            the phosphotransferases. This encoded enzyme is responsible for the
            third and last step in L-serine formation. It catalyzes
            magnesium-dependent hydrolysis of L-phosphoserine and is also
            involved in an exchange reaction between L-serine and
            L-phosphoserine. Deficiency of this protein is thought to be linked
            to Williams syndrome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.178442.1,
                                           SRR1803613.261159.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p11.2"
     Protein         1..225
                     /product="phosphoserine phosphatase"
                     /EC_number="3.1.3.3"
                     /note="L-3-phosphoserine phosphatase; O-phosphoserine
                     phosphohydrolase; PSPase"
                     /calculated_mol_wt=24877
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P78330.2)"
     Region          15..216
                     /region_name="HAD_PSP_eu"
                     /note="phosphoserine phosphatase eukaryotic-like, similar
                     to human phosphoserine phosphatase; cd04309"
                     /db_xref="CDD:319801"
     Site            order(20..24,29,109..110,158,178..179,182..183)
                     /site_type="active"
                     /db_xref="CDD:319801"
     CDS             1..225
                     /gene="PSPH"
                     /gene_synonym="PSP; PSPHD"
                     /coded_by="NM_001370505.1:761..1438"
                     /db_xref="CCDS:CCDS5522.1"
                     /db_xref="GeneID:5723"
                     /db_xref="HGNC:HGNC:9577"
                     /db_xref="MIM:172480"
ORIGIN      
        1 mvshselrkl fysadavcfd vdstvireeg idelakicgv edavsemtrr amggavpfka
       61 alterlaliq psreqvqrli aeqpphltpg irelvsrlqe rnvqvflisg gfrsivehva
      121 sklnipatnv fanrlkfyfn geyagfdetq ptaesggkgk vikllkekfh fkkiimigdg
      181 atdmeacppa dafigfggnv irqqvkdnak wyitdfvell gelee
//
LOCUS       NP_619727               1549 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear factor of activated T-cells 5 isoform b [Homo sapiens].
ACCESSION   NP_619727
VERSION     NP_619727.2
DBSOURCE    REFSEQ: accession NM_138713.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1549)
  AUTHORS   Deng,D., Begum,H., Liu,T., Zhang,J., Zhang,Q., Chu,T.Y., Li,H.,
            Lemenze,A., Hoque,M., Soteropoulos,P. and Hou,P.
  TITLE     NFAT5 governs cellular plasticity-driven resistance to
            KRAS-targeted therapy in pancreatic cancer
  JOURNAL   J Exp Med 221 (11) (2024)
   PUBMED   39432061
  REMARK    GeneRIF: NFAT5 governs cellular plasticity-driven resistance to
            KRAS-targeted therapy in pancreatic cancer.
REFERENCE   2  (residues 1 to 1549)
  AUTHORS   Li,J.Y., Feng,T.S., Gao,J., Yang,X.X., Li,X.C., Deng,Z.H., Xia,Y.X.
            and Wu,Z.S.
  TITLE     Differentiation and immunosuppressive function of CD19+CD24hiCD27+
            regulatory B cells are regulated through the miR-29a-3p/NFAT5
            pathway
  JOURNAL   Hepatobiliary Pancreat Dis Int 23 (5), 472-480 (2024)
   PUBMED   38724321
  REMARK    GeneRIF: Differentiation and immunosuppressive function of
            CD19[+]CD24[hi]CD27[+] regulatory B cells are regulated through the
            miR-29a-3p/NFAT5 pathway.
REFERENCE   3  (residues 1 to 1549)
  AUTHORS   Okumura,T., Raja Xavier,J.P., Pasternak,J., Yang,Z., Hang,C.,
            Nosirov,B., Singh,Y., Admard,J., Brucker,S.Y., Kommoss,S.,
            Takeda,S., Staebler,A., Lang,F. and Salker,M.S.
  TITLE     Rel Family Transcription Factor NFAT5 Upregulates COX2 via
            HIF-1alpha Activity in Ishikawa and HEC1a Cells
  JOURNAL   Int J Mol Sci 25 (7), 3666 (2024)
   PUBMED   38612478
  REMARK    GeneRIF: Rel Family Transcription Factor NFAT5 Upregulates COX2 via
            HIF-1alpha Activity in Ishikawa and HEC1a Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1549)
  AUTHORS   Song,H.J., Kim,Y.H., Choi,H.N., Kim,T., Kim,S.J., Kang,M.W. and
            Lee,S.D.
  TITLE     TonEBP/NFAT5 expression is associated with cisplatin resistance and
            migration in macrophage-induced A549 cells
  JOURNAL   BMC Mol Cell Biol 25 (1), 6 (2024)
   PUBMED   38438872
  REMARK    GeneRIF: TonEBP/NFAT5 expression is associated with cisplatin
            resistance and migration in macrophage-induced A549 cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1549)
  AUTHORS   Zhou,G., Chen,C., Wu,H., Lin,J., Liu,H., Tao,Y. and Huang,B.
  TITLE     LncRNA AP000842.3 Triggers the Malignant Progression of Prostate
            Cancer by Regulating Cuproptosis Related Gene NFAT5
  JOURNAL   Technol Cancer Res Treat 23, 15330338241255585 (2024)
   PUBMED   38780486
  REMARK    GeneRIF: LncRNA AP000842.3 Triggers the Malignant Progression of
            Prostate Cancer by Regulating Cuproptosis Related Gene NFAT5.
REFERENCE   6  (residues 1 to 1549)
  AUTHORS   Trama,J., Lu,Q., Hawley,R.G. and Ho,S.N.
  TITLE     The NFAT-related protein NFATL1 (TonEBP/NFAT5) is induced upon T
            cell activation in a calcineurin-dependent manner
  JOURNAL   J Immunol 165 (9), 4884-4894 (2000)
   PUBMED   11046013
  REMARK    GeneRIF: Induced upon T cell activation in a calcineurin-dependent
            manner, which contrasts with the calcineurin-independent induction
            mediated by hyperosmotic stress.
REFERENCE   7  (residues 1 to 1549)
  AUTHORS   Ko,B.C., Turck,C.W., Lee,K.W., Yang,Y. and Chung,S.S.
  TITLE     Purification, identification, and characterization of an osmotic
            response element binding protein
  JOURNAL   Biochem Biophys Res Commun 270 (1), 52-61 (2000)
   PUBMED   10733904
REFERENCE   8  (residues 1 to 1549)
  AUTHORS   Lopez-Rodriguez,C., Aramburu,J., Rakeman,A.S. and Rao,A.
  TITLE     NFAT5, a constitutively nuclear NFAT protein that does not
            cooperate with Fos and Jun
  JOURNAL   Proc Natl Acad Sci U S A 96 (13), 7214-7219 (1999)
   PUBMED   10377394
REFERENCE   9  (residues 1 to 1549)
  AUTHORS   Miyakawa,H., Woo,S.K., Dahl,S.C., Handler,J.S. and Kwon,H.M.
  TITLE     Tonicity-responsive enhancer binding protein, a rel-like protein
            that stimulates transcription in response to hypertonicity
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 2538-2542 (1999)
   PUBMED   10051678
REFERENCE   10 (residues 1 to 1549)
  AUTHORS   Adams,M.D., Soares,M.B., Kerlavage,A.R., Fields,C. and Venter,J.C.
  TITLE     Rapid cDNA sequencing (expressed sequence tags) from a
            directionally cloned human infant brain cDNA library
  JOURNAL   Nat Genet 4 (4), 373-380 (1993)
   PUBMED   8401585
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009032.8, AJ243299.1,
            BC131509.1, AC012321.8 and AA291524.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 2, 2008 this sequence version replaced NP_619727.1.
            
            Summary: The product of this gene is a member of the nuclear
            factors of activated T cells family of transcription factors.
            Proteins belonging to this family play a central role in inducible
            gene transcription during the immune response. This protein
            regulates gene expression induced by osmotic stress in mammalian
            cells. Unlike monomeric members of this protein family, this
            protein exists as a homodimer and forms stable dimers with DNA
            elements. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an exon in the 5'
            region, compared to variant 1. This difference causes translation
            initiation at an upstream start codon and results in an isoform (b)
            with a longer N-terminus compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ243299.1, SRR1803615.141797.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000349945.7/ ENSP00000338806.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..1549
                     /product="nuclear factor of activated T-cells 5 isoform b"
                     /note="osmotic response element-binding protein; glutamine
                     rich protein H65; NFAT-like protein 1; TonE-binding
                     protein; nuclear factor of activated T-cells 5,
                     tonicity-responsive; T-cell transcription factor NFAT5;
                     tonicity-responsive enhancer-binding protein"
                     /calculated_mol_wt=167677
     Region          52..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94916.1)"
     Region          132..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94916.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21209322; propagated from
                     UniProtKB/Swiss-Prot (O94916.1)"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV30; propagated from
                     UniProtKB/Swiss-Prot (O94916.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21209322; propagated from
                     UniProtKB/Swiss-Prot (O94916.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK5.
                     /evidence=ECO:0000269|PubMed:21209322,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94916.1)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21209322; propagated from
                     UniProtKB/Swiss-Prot (O94916.1)"
     Region          193..238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94916.1)"
     Region          259..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94916.1)"
     Region          298..458
                     /region_name="RHD-n_TonEBP"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of tonicity-responsive enhancer binding protein
                     (TonEBP); cd07882"
                     /db_xref="CDD:143642"
     Site            order(311,314,316..321,407,409..410,425,427,458)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143642"
     Region          462..561
                     /region_name="IPT_NFAT"
                     /note="IPT domain of the NFAT family of transcription
                     factors. NFAT transcription complexes are a target of
                     calcineurin, a calcium dependent phosphatase, and activate
                     genes mainly involved in cell-cell-interaction; cd01178"
                     /db_xref="CDD:238583"
     Site            order(486,549)
                     /site_type="DNA binding"
                     /note="DNA binding sites [nucleotide binding]"
                     /db_xref="CDD:238583"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94916.1)"
     Region          658..684
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94916.1)"
     Region          859..909
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94916.1)"
     Region          976..1014
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94916.1)"
     Region          <1205..>1341
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     Region          1229..1322
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94916.1)"
     Region          1334..1389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94916.1)"
     Region          1491..1520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94916.1)"
     CDS             1..1549
                     /gene="NFAT5"
                     /gene_synonym="NF-AT5; NFATL1; NFATZ; OREBP; TONEBP"
                     /coded_by="NM_138713.4:337..4986"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45518.1"
                     /db_xref="GeneID:10725"
                     /db_xref="HGNC:HGNC:7774"
                     /db_xref="MIM:604708"
ORIGIN      
        1 mpsdfislls adldlespks lysrdslklh psqnfhragl leesvydllp kelqlppsre
       61 tsvasmsqts ggeagspppa vvaadassap ssssmggacs sfttssspti ystsvtdska
      121 mqvescssav gvsnrgvsek qltsntvqqh pstpkrhtvl yispppedll dnsrmscqde
      181 gcgleseqsc smwmedspsn fsnmstssyn dntevprksr krnpkqrpgv krrdceesnm
      241 difdadsaka phyvlsqltt dnkgnskagn gtlenqkgtg vkkspmlcgq ypvksegkel
      301 kivvqpetqh raryltegsr gsvkdrtqqg fptvkleghn epvvlqvfvg ndsgrvkphg
      361 fyqacrvtgr nttpckevdi egttvievgl dpsnnmtlav dcvgilklrn advearigia
      421 gskkkstrar lvfrvnimrk dgstltlqtp sspilctqpa gvpeilkksl hscsvkgeee
      481 vfligknflk gtkvifqenv sdenswksea eidmelfhqn hlivkvppyh dqhitlpvsv
      541 giyvvtnagr shdvqpftyt pdpaaagaln vnvkkeissp arpcsfeeam kamkttgcnl
      601 dkvniipnal mtplipssmi ksedvtpmev taekrsstif kttksvgstq qtlenisnia
      661 gngsfsspss shlpsenekq qqiqpkaynp etlttiqtqd isqpgtfpav sassqlpnsd
      721 allqqatqfq tretqsreil qsdgtvvnls qlteasqqqq qsplqeqaqt lqqqissnif
      781 pspnsvsqlq ntiqqlqags ftgstasgss gsvdlvqqvl eaqqqlssvl fsapdgnenv
      841 qeqlsadifq qvsqiqsgvs pgmfsstept vhtrpdnllp graesvhpqs entlsnqqqq
      901 qqqqqqvmes saamvmemqq sicqaaaqiq selfpstasa ngnlqqspvy qqtshmmsal
      961 stnedmqmqc elfssppavs gnetsttttq qvatpgttmf qtsssgdgee tgtqakqiqn
     1021 svfqtmvqmq hsgdnqpqvn lfsstksmms vqnsgtqqqg nglfqqgnem mslqsgnflq
     1081 qsshsqaqlf hpqnpiadaq nlsqetqgsl fhspnpivhs qtsttsseqm qppmfhsqst
     1141 iavlqgssvp qdqqstnifl sqspmnnlqt ntvaqeaffa apnsisplqs tsnseqqaaf
     1201 qqqapishiq tpmlsqeqaq ppqqglfqpq valgslppnp mpqsqqgtmf qsqhsivamq
     1261 snspsqeqqq qqqqqqqqqq qqqqsilfsn qntmatmasp kqpppnmifn pnqnpmanqe
     1321 qqnqsifhqq snmapmnqeq qpmqfqsqst vsslqnpgpt qsessqtplf hsspqiqlvq
     1381 gspssqeqqv tlflspasms alqtsinqqd mqqsplyspq nnmpgiqgat sspqpqatlf
     1441 hntaggtmnq lqnspgssqq tsgmflfgiq nncsqlltsg patlpdqlma isqpgqpqne
     1501 gqppvttlls qqmpenspla ssintnqnie kidllvslqn qgnnltgsf
//
LOCUS       NP_003099                441 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor SOX-11 [Homo sapiens].
ACCESSION   NP_003099 XP_943168
VERSION     NP_003099.1
DBSOURCE    REFSEQ: accession NM_003108.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Sureda-Gomez,M., Iaccarino,I., De Bolos,A., Meyer,M., Balsas,P.,
            Richter,J., Rodriguez,M.L., Lopez,C., Carreras-Caballe,M.,
            Glaser,S., Nadeu,F., Jares,P., Clot,G., Siciliano,M.C., Bellan,C.,
            Tornambe,S., Boccacci,R., Leoncini,L., Campo,E., Siebert,R.,
            Amador,V. and Klapper,W.
  TITLE     SOX11 expression is restricted to EBV-negative Burkitt lymphoma and
            is associated with molecular genetic features
  JOURNAL   Blood 144 (2), 187-200 (2024)
   PUBMED   38620074
  REMARK    GeneRIF: SOX11 expression is restricted to EBV-negative Burkitt
            lymphoma and is associated with molecular genetic features.
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Treekitkarnmongkol,W., Shah,V., Kai,K., Katayama,H., Wong,J.,
            Ladha,F.A., Nguyen,T., Menegaz,B., Lu,W., Yang,F., Mino,B.,
            Tang,X., Gagea,M., Batra,H., Raso,M.G., Wistuba,I.I.,
            Krishnamurthy,S., Pinder,S.E., Sawyer,E.J., Thompson,A.M. and
            Sen,S.
  TITLE     Epigenetic activation of SOX11 is associated with recurrence and
            progression of ductal carcinoma in situ to invasive breast cancer
  JOURNAL   Br J Cancer 131 (1), 171-183 (2024)
   PUBMED   38760444
  REMARK    GeneRIF: Epigenetic activation of SOX11 is associated with
            recurrence and progression of ductal carcinoma in situ to invasive
            breast cancer.
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Abdelrazak Morsy,M.H., Lilienthal,I., Lord,M., Merrien,M.,
            Wasik,A.M., Sureda-Gomez,M., Amador,V., Johansson,H.J., Lehtio,J.,
            Garcia-Torre,B., Martin-Subero,J.I., Tsesmetzis,N., Tao,S.,
            Schinazi,R.F., Kim,B., Sorteberg,A.L., Wickstrom,M., Sheppard,D.,
            Rassidakis,G.Z., Taylor,I.A., Christensson,B., Campo,E., Herold,N.
            and Sander,B.
  TITLE     SOX11 is a novel binding partner and endogenous inhibitor of SAMHD1
            ara-CTPase activity in mantle cell lymphoma
  JOURNAL   Blood 143 (19), 1953-1964 (2024)
   PUBMED   38237141
  REMARK    GeneRIF: SOX11 is a novel binding partner and endogenous inhibitor
            of SAMHD1 ara-CTPase activity in mantle cell lymphoma.
REFERENCE   4  (residues 1 to 441)
  AUTHORS   De Bolos,A., Sureda-Gomez,M., Carreras-Caballe,M., Rodriguez,M.L.,
            Clot,G., Bea,S., Gine,E., Campo,E., Balsas,P. and Amador,V.
  TITLE     SOX11/PRDX2 axis modulates redox homeostasis and chemoresistance in
            aggressive mantle cell lymphoma
  JOURNAL   Sci Rep 14 (1), 7863 (2024)
   PUBMED   38570586
  REMARK    GeneRIF: SOX11/PRDX2 axis modulates redox homeostasis and
            chemoresistance in aggressive mantle cell lymphoma.
            Erratum:[Sci Rep. 2024 Jun 11;14(1):13426. doi:
            10.1038/s41598-024-61080-9. PMID: 38862588]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Smith,H., Al-Jawahiri,R., Stokes,L., Freeth,M., Fricke,S.,
            Matthews,D. and McNeill,A.
  TITLE     Impaired communication ability in SOX11 syndrome
  JOURNAL   J Intellect Disabil Res 68 (3), 285-292 (2024)
   PUBMED   37916390
  REMARK    GeneRIF: Impaired communication ability in SOX11 syndrome.
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Azuma,T., Ao,S., Saito,Y., Yano,K., Seki,N., Wakao,H., Masuho,Y.
            and Muramatsu,M.
  TITLE     Human SOX11, an upregulated gene during the neural differentiation,
            has a long 3' untranslated region
  JOURNAL   DNA Res 6 (5), 357-360 (1999)
   PUBMED   10574465
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Kuhlbrodt,K., Herbarth,B., Sock,E., Enderich,J.,
            Hermans-Borgmeyer,I. and Wegner,M.
  TITLE     Cooperative function of POU proteins and SOX proteins in glial
            cells
  JOURNAL   J Biol Chem 273 (26), 16050-16057 (1998)
   PUBMED   9632656
REFERENCE   8  (residues 1 to 441)
  AUTHORS   Jay,P., Goze,C., Marsollier,C., Taviaux,S., Hardelin,J.P.,
            Koopman,P. and Berta,P.
  TITLE     The human SOX11 gene: cloning, chromosomal assignment and tissue
            expression
  JOURNAL   Genomics 29 (2), 541-545 (1995)
   PUBMED   8666406
REFERENCE   9  (residues 1 to 441)
  AUTHORS   Goze,C., Poulat,F. and Berta,P.
  TITLE     Partial cloning of SOX-11 and SOX-12, two new human SOX genes
  JOURNAL   Nucleic Acids Res 21 (12), 2943 (1993)
   PUBMED   8332506
REFERENCE   10 (residues 1 to 441)
  AUTHORS   Santiago,J.V.
  TITLE     Overview of the complications of diabetes
  JOURNAL   Clin Chem 32 (10 Suppl), B48-B53 (1986)
   PUBMED   3530540
  REMARK    GeneRIF: Overview of the complications of diabetes.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC108025.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_943168.1.
            
            Summary: This intronless gene encodes a member of the SOX
            (SRY-related HMG-box) family of transcription factors involved in
            the regulation of embryonic development and in the determination of
            the cell fate. The encoded protein may act as a transcriptional
            regulator after forming a protein complex with other proteins. The
            protein may function in the developing nervous system and play a
            role in tumorigenesis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322002.5/ ENSP00000322568.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.2"
     Protein         1..441
                     /product="transcription factor SOX-11"
                     /note="SRY (sex-determining region Y)-box 11; SRY-related
                     HMG-box gene 11; SRY-box 11"
                     /calculated_mol_wt=46548
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35716.2)"
     Region          38..129
                     /region_name="HMG-box_SoxC_SOX11"
                     /note="high mobility group (HMG)-box found in sex
                     determining region Y (SRY)-box 11 (SOX11) and similar
                     proteins; cd22037"
                     /db_xref="CDD:438846"
     Site            order(48,50..51,53..54,56..57,61,64,68,75..77,80..81,84,
                     87..88,106,118,120..122)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438846"
     Region          116..216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35716.2)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35716.2)"
     Region          240..292
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35716.2)"
     Region          319..359
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35716.2)"
     Region          409..441
                     /region_name="Required for transcriptional activation
                     activity and synergistic coactivation of transcriptional
                     activity with POU3F2.
                     /evidence=ECO:0000250|UniProtKB:Q7M6Y2"
                     /note="propagated from UniProtKB/Swiss-Prot (P35716.2)"
     CDS             1..441
                     /gene="SOX11"
                     /gene_synonym="CSS9; IDDMOH; MRD27"
                     /coded_by="NM_003108.4:339..1664"
                     /db_xref="CCDS:CCDS1654.1"
                     /db_xref="GeneID:6664"
                     /db_xref="HGNC:HGNC:11191"
                     /db_xref="MIM:600898"
ORIGIN      
        1 mvqqaeslea esnlpreald teegefmacs pvaldesdpd wcktasghik rpmnafmvws
       61 kierrkimeq spdmhnaeis krlgkrwkml kdsekipfir eaerlrlkhm adypdykyrp
      121 rkkpkmdpsa kpsasqspek saagggggsa gggaggakts kgsskkcgkl kapaaagaka
      181 gagkaaqsgd yggagddyvl gslrvsgsgg ggagktvkcv fldedddddd dddelqlqik
      241 qepdeedeep phqqllqppg qqpsqllrry nvakvpaspt lsssaespeg aslydevrag
      301 atsgagggsr lyysfknitk qhppplaqpa lspassrsvs tssssssgss sgssgedadd
      361 lmfdlslnfs qsahsaseqq lgggaaagnl slslvdkdld sfsegslgsh fefpdyctpe
      421 lsemiagdwl eanfsdlvft y
//
LOCUS       NP_001352153             258 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-dependent glucokinase isoform 3 [Homo sapiens].
ACCESSION   NP_001352153
VERSION     NP_001352153.1
DBSOURCE    REFSEQ: accession NM_001365224.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Herrera-Morande,A., Vallejos-Baccelliere,G., Cea,P.A., Zamora,R.A.,
            Cid,D., Maturana,P., Gonzalez-Ordenes,F., Castro-Fernandez,V. and
            Guixe,V.
  TITLE     Kinetic characterization and phylogenetic analysis of human
            ADP-dependent glucokinase reveal new insights into its regulatory
            properties
  JOURNAL   Arch Biochem Biophys 741, 109602 (2023)
   PUBMED   37084804
  REMARK    GeneRIF: Kinetic characterization and phylogenetic analysis of
            human ADP-dependent glucokinase reveal new insights into its
            regulatory properties.
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Tandon,A., Birkenhagen,J., Nagalla,D., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase as a novel onco-target for haematological
            malignancies
  JOURNAL   Sci Rep 10 (1), 13584 (2020)
   PUBMED   32788680
  REMARK    GeneRIF: ADP-dependent glucokinase as a novel onco-target for
            haematological malignancies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Jiang,H.Y. and Wang,Z.J.
  TITLE     ADPGK-AS1 promotes the progression of colorectal cancer via
            sponging miR-525 to upregulate FUT1
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2380-2386 (2020)
   PUBMED   32196589
  REMARK    GeneRIF: ADPGK-AS1 promotes the progression of colorectal cancer
            via sponging miR-525 to upregulate FUT1.
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Imle,R., Wang,B.T., Stutzenberger,N., Birkenhagen,J., Tandon,A.,
            Carl,M., Himmelreich,N., Thiel,C., Grone,H.J., Poschet,G.,
            Volkers,M., Gulow,K., Schroder,A., Carillo,S., Mittermayr,S.,
            Bones,J., Kaminski,M.M., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing
  JOURNAL   Sci Rep 9 (1), 14248 (2019)
   PUBMED   31582762
  REMARK    GeneRIF: ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Richter,J.P., Goroncy,A.K., Ronimus,R.S. and Sutherland-Smith,A.J.
  TITLE     The Structural and Functional Characterization of Mammalian
            ADP-dependent Glucokinase
  JOURNAL   J Biol Chem 291 (8), 3694-3704 (2016)
   PUBMED   26555263
  REMARK    GeneRIF: ADPGK is substrate inhibited by high glucose concentration
            and shows high specificity for glucose, with no activity for other
            sugars, as determined by NMR spectroscopy, including 2-deoxyglucose
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Cuesta-Munoz,A.L., Tuomi,T., Cobo-Vuilleumier,N., Koskela,H.,
            Odili,S., Stride,A., Buettger,C., Otonkoski,T., Froguel,P.,
            Grimsby,J., Garcia-Gimeno,M. and Matschinsky,F.M.
  TITLE     Clinical heterogeneity in monogenic diabetes caused by mutations in
            the glucokinase gene (GCK-MODY)
  JOURNAL   Diabetes Care 33 (2), 290-292 (2010)
   PUBMED   19903754
  REMARK    GeneRIF: Glucose and insulin response to oral glucose is higher in
            GCK(261) carriers, indicating clinical heterogeneity in GCK
            maturity diabetes carriers.
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Codner,E., Rocha,A., Deng,L., Martinez-Aguayo,A., Godoy,C.,
            Mericq,V. and Chung,W.K.
  TITLE     Mild fasting hyperglycemia in children: high rate of glucokinase
            mutations and some risk of developing type 1 diabetes mellitus
  JOURNAL   Pediatr Diabetes 10 (6), 382-388 (2009)
   PUBMED   19309449
  REMARK    GeneRIF: The presence of mild persistent hyperglycemia in any
            patient without autoantibodies should lead to genetic analysis of
            glucokinase, particularly if there is a positive family history.
REFERENCE   9  (residues 1 to 258)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 258)
  AUTHORS   Ronimus,R.S. and Morgan,H.W.
  TITLE     Cloning and biochemical characterization of a novel mouse
            ADP-dependent glucokinase
  JOURNAL   Biochem Biophys Res Commun 315 (3), 652-658 (2004)
   PUBMED   14975750
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK055526.1, AK075560.1 and AC009712.22.
            
            Summary: ADPGK (EC 2.7.1.147) catalyzes the ADP-dependent
            phosphorylation of glucose to glucose-6-phosphate and may play a
            role in glycolysis, possibly during ischemic conditions (Ronimus
            and Morgan, 2004 [PubMed 14975750]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055526.1, SRR1803614.188318.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153427 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..258
                     /product="ADP-dependent glucokinase isoform 3"
                     /EC_number="2.7.1.147"
                     /note="ATP-dependent glucokinase; rbBP-35"
                     /calculated_mol_wt=28282
     Region          <1..253
                     /region_name="ribokinase_pfkB_like"
                     /note="ribokinase/pfkB superfamily: Kinases that accept a
                     wide variety of substrates, including carbohydrates and
                     aromatic small molecules, all are phosphorylated at a
                     hydroxyl group. The superfamily includes ribokinase,
                     fructokinase, ketohexokinase; cl00192"
                     /db_xref="CDD:469648"
     Site            order(86,143,237,240..241,244)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238177"
     CDS             1..258
                     /gene="ADPGK"
                     /gene_synonym="2610017G09Rik; ADP-GK"
                     /coded_by="NM_001365224.1:496..1272"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:83440"
                     /db_xref="HGNC:HGNC:25250"
                     /db_xref="MIM:611861"
ORIGIN      
        1 mnmlevfvss leefqpdlvv lsglhmmegq skelqrkrll evvtsisdip tgipvhlela
       61 smtnrelmss ivhqqvfpav tslglneqel lfltqsasgp hsslsswngv pdvgmvsdil
      121 fwilkehgrs ksrasdltri hfhtlvyhil atvdghwanq laavaagarv agtqacatet
      181 idtsrvslra pqefmtshse agsrivlnpn kpvvewhreg isfhftpvlv ckdpirtvgl
      241 gdaisaeglf ysevhphy
//
LOCUS       NP_001157750             451 aa            linear   PRI 27-APR-2025
DEFINITION  glucose-6-phosphate exchanger SLC37A4 isoform 2 [Homo sapiens].
ACCESSION   NP_001157750
VERSION     NP_001157750.1
DBSOURCE    REFSEQ: accession NM_001164278.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Tanigaki,K., Matsumura,R., Sasaki,N., Kato,Y., Tamamori,T.,
            Yamaga,S., Nakamura,E., Sakanaka,A., Kuboniwa,M., Matsusaki,M.,
            Amano,A. and Takeuchi,H.
  TITLE     SLC37A4, gene responsible for glycogen storage disease type 1b,
            regulates gingival epithelial barrier function via JAM1 expression
  JOURNAL   Sci Rep 14 (1), 24797 (2024)
   PUBMED   39433915
  REMARK    GeneRIF: SLC37A4, gene responsible for glycogen storage disease
            type 1b, regulates gingival epithelial barrier function via JAM1
            expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Wang,Z., Zhao,R., Jia,X., Li,X., Ma,L. and Fu,H.
  TITLE     Three novel SLC37A4 variants in glycogen storage disease type 1b
            and a literature review
  JOURNAL   J Int Med Res 51 (12), 3000605231216633 (2023)
   PUBMED   38087503
  REMARK    GeneRIF: Three novel SLC37A4 variants in glycogen storage disease
            type 1b and a literature review.
            Review article
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Ng,B.G., Sosicka,P., Fenaille,F., Harroche,A.,
            Vuillaumier-Barrot,S., Porterfield,M., Xia,Z.J., Wagner,S.,
            Bamshad,M.J., Vergnes-Boiteux,M.C., Cholet,S., Dalton,S., Dell,A.,
            Dupre,T., Fiore,M., Haslam,S.M., Huguenin,Y., Kumagai,T., Kulik,M.,
            McGoogan,K., Michot,C., Nickerson,D.A., Pascreau,T., Borgel,D.,
            Raymond,K., Warad,D., Flanagan-Steet,H., Steet,R., Tiemeyer,M.,
            Seta,N., Bruneel,A. and Freeze,H.H.
  CONSRTM   University of Washington Center for Mendelian Genomics (UW-CMG)
  TITLE     A mutation in SLC37A4 causes a dominantly inherited congenital
            disorder of glycosylation characterized by liver dysfunction
  JOURNAL   Am J Hum Genet 108 (6), 1040-1052 (2021)
   PUBMED   33964207
  REMARK    GeneRIF: A mutation in SLC37A4 causes a dominantly inherited
            congenital disorder of glycosylation characterized by liver
            dysfunction.
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Xu,Q., Tang,H., Duan,L., Zuo,X., Shi,X., Li,Y., Zhao,H. and
            Zhang,H.
  TITLE     A novel SLC37A4 missense mutation in GSD-Ib without hepatomegaly
            causes enhanced leukocytes endoplasmic reticulum stress and
            apoptosis
  JOURNAL   Mol Genet Genomic Med 9 (1), e1568 (2021)
   PUBMED   33280276
  REMARK    GeneRIF: A novel SLC37A4 missense mutation in GSD-Ib without
            hepatomegaly causes enhanced leukocytes endoplasmic reticulum
            stress and apoptosis.
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Veiga-da-Cunha,M., Gerin,I., Chen,Y.T., de Barsy,T., de Lonlay,P.,
            Dionisi-Vici,C., Fenske,C.D., Lee,P.J., Leonard,J.V., Maire,I.,
            McConkie-Rosell,A., Schweitzer,S., Vikkula,M. and Van
            Schaftingen,E.
  TITLE     A gene on chromosome 11q23 coding for a putative glucose-
            6-phosphate translocase is mutated in glycogen-storage disease
            types Ib and Ic
  JOURNAL   Am J Hum Genet 63 (4), 976-983 (1998)
   PUBMED   9758626
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Annabi,B., Hiraiwa,H., Mansfield,B.C., Lei,K.J., Ubagai,T.,
            Polymeropoulos,M.H., Moses,S.W., Parvari,R., Hershkovitz,E.,
            Mandel,H., Fryman,M. and Chou,J.Y.
  TITLE     The gene for glycogen-storage disease type 1b maps to chromosome
            11q23
  JOURNAL   Am J Hum Genet 62 (2), 400-405 (1998)
   PUBMED   9463334
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Ihara,K., Takabayashi,A., Terasaki,K. and Hara,T.
  TITLE     Assignment1 of glucose 6-phosphate translocase (G6PT1) to human
            chromosome band 11q23.3 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 50-51 (1998)
   PUBMED   9925924
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Gerin,I., Veiga-da-Cunha,M., Achouri,Y., Collet,J.F. and Van
            Schaftingen,E.
  TITLE     Sequence of a putative glucose 6-phosphate translocase, mutated in
            glycogen storage disease type Ib
  JOURNAL   FEBS Lett 419 (2-3), 235-238 (1997)
   PUBMED   9428641
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Bali,D.S., El-Gharbawy,A., Austin,S., Pendyal,S. and Kishnani,P.S.
  TITLE     Glycogen Storage Disease Type I
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301489
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Narisawa,K., Igarashi,Y., Otomo,H. and Tada,K.
  TITLE     A new variant of glycogen storage disease type I probably due to a
            defect in the glucose-6-phosphate transport system
  JOURNAL   Biochem Biophys Res Commun 83 (4), 1360-1364 (1978)
   PUBMED   212064
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003392.2 and FP885832.1.
            
            Summary: This gene regulates glucose-6-phosphate transport from the
            cytoplasm to the lumen of the endoplasmic reticulum, in order to
            maintain glucose homeostasis. It also plays a role in ATP-mediated
            calcium sequestration in the lumen of the endoplasmic reticulum.
            Mutations in this gene have been associated with various forms of
            glycogen storage disease. Alternative splicing in this gene results
            in multiple transcript variants.[provided by RefSeq, Aug 2009].
            
            Transcript Variant: This variant (2) contains an alternate exon in
            the 5' UTR and an alternate in-frame exon in the 3' coding region,
            compared to variant 1. This results in a longer protein (isoform
            2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK312628.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..451
                     /product="glucose-6-phosphate exchanger SLC37A4 isoform 2"
                     /note="glucose-6-phosphate translocase;
                     glucose-6-phosphatase, transport (glucose-6-phosphate)
                     protein 1; glucose-6-phosphatase, transport
                     (phosphate/pyrophosphate) protein 2;
                     glucose-6-phosphatase, transport (glucose) protein 3;
                     microsomal glucose-6-phosphate transporter;
                     glucose-5-phosphate transporter; transformation-related
                     gene 19 protein; solute carrier family 37
                     (glucose-6-phosphate transporter), member 4;
                     glucose-6-phosphate exchanger SLC37A4;
                     glucose-6-phosphatase transporter; sugar-phosphate
                     exchange protein 4"
                     /calculated_mol_wt=48709
     Region          10..439
                     /region_name="MFS_SLC37A4"
                     /note="Solute carrier family 37 member 4 of the Major
                     Facilitator Superfamily of transporters; cd17343"
                     /db_xref="CDD:340901"
     Site            order(24..25,28..29,32,64,114..115,117..119,122,142,
                     145..146,149,233,236..237,240..242,245,273,277,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340901"
     CDS             1..451
                     /gene="SLC37A4"
                     /gene_synonym="CDG2W; G6PT; G6PT1; G6PT2; G6PT3; GSD1b;
                     GSD1c; GSD1d; PRO0685; SPX4; TRG-19; TRG19"
                     /coded_by="NM_001164278.2:413..1768"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:2542"
                     /db_xref="HGNC:HGNC:4061"
                     /db_xref="MIM:602671"
ORIGIN      
        1 maaqgygyyr tvifsamfgg yslyyfnrkt fsfvmpslve eipldkddlg fitssqsaay
       61 aiskfvsgvl sdqmsarwlf ssglllvglv niffawsstv pvfaalwfln glaqglgwpp
      121 cgkvlrkwfe psqfgtwwai lstsmnlagg lgpilatila qsyswrstla lsgalcvvvs
      181 flclllihne padvglrnld pmpsegkkgs lkeestlqel llspylwvls tgylvvfgvk
      241 tcctdwgqff liqekgqsal vgssymsale vgglvgsiaa gylsdramak aglsnygnpr
      301 hglllfmmag mtvsmylfrv tvtsdspkdv afwtlalhpl aeltgftehe lwilvlgavf
      361 gfssygpial fgvianesap pnlcgtshai vglmanvggf laglpfstia khyswstafw
      421 vaevicaast aaffllrnir tkmgrvskka e
//
LOCUS       NP_079736                196 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 126A [Mus musculus].
ACCESSION   NP_079736
VERSION     NP_079736.1
DBSOURCE    REFSEQ: accession NM_025460.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Kim,E.C., Moon,J.H., Kang,S.W., Kwon,B. and Lee,H.W.
  TITLE     TMEM126A, a CD137 ligand binding protein, couples with the TLR4
            signal transduction pathway in macrophages
  JOURNAL   Mol Immunol 64 (2), 244-251 (2015)
   PUBMED   25549946
  REMARK    GeneRIF: TMEM126A contributes to the TLR4 signal up-regulating the
            expression of genes whose products are involved in antigen
            presentation.
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Ryder,E., Gleeson,D., Sethi,D., Vyas,S., Miklejewska,E., Dalvi,P.,
            Habib,B., Cook,R., Hardy,M., Jhaveri,K., Bottomley,J.,
            Wardle-Jones,H., Bussell,J.N., Houghton,R., Salisbury,J.,
            Skarnes,W.C. and Ramirez-Solis,R.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Molecular characterization of mutant mouse strains generated from
            the EUCOMM/KOMP-CSD ES cell resource
  JOURNAL   Mamm Genome 24 (7-8), 286-294 (2013)
   PUBMED   23912999
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Bae,J.S., Choi,J.K., Moon,J.H., Kim,E.C., Croft,M. and Lee,H.W.
  TITLE     Novel transmembrane protein 126A (TMEM126A) couples with CD137L
            reverse signals in myeloid cells
  JOURNAL   Cell Signal 24 (12), 2227-2236 (2012)
   PUBMED   22885069
  REMARK    GeneRIF: TMEM126A binds to the extracellular domain of CD137L and
            is detected on cell surface by flow cytometry, cell surface
            expression of TMEM126A may be essential for CD137L reverse
            signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK007559.1 and AC100322.8.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC023171.1, BG919400.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 50.59 cM"
     Protein         1..196
                     /product="transmembrane protein 126A"
                     /calculated_mol_wt=21408
     Region          14..192
                     /region_name="TMEM126"
                     /note="Transmembrane protein 126; pfam07114"
                     /db_xref="CDD:462092"
     Site            35..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D8Y1.1)"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D8Y1.1)"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D8Y1.1)"
     Site            160..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D8Y1.1)"
     CDS             1..196
                     /gene="Tmem126a"
                     /gene_synonym="1810020E01Rik"
                     /coded_by="NM_025460.3:140..730"
                     /db_xref="CCDS:CCDS21447.1"
                     /db_xref="GeneID:66271"
                     /db_xref="MGI:MGI:1913521"
ORIGIN      
        1 meshkpstsk ddlilniisr kikqlpesdr nlleygsayi glnaafggli anslfrriln
       61 vtqarlassl pmavipflta nlsyqslvsl plstgdlnce tctttrgalv glvmgglypi
      121 llaipvnggl aaryessplp qrgnifnywi tvskpvfrkm lfptllqtvf asylgsrqyk
      181 llikalqlpe pdleih
//
LOCUS       NP_001166244             545 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 548 isoform 1 [Homo sapiens].
ACCESSION   NP_001166244
VERSION     NP_001166244.1
DBSOURCE    REFSEQ: accession NM_001172773.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Suzuki,Y., Yamashita,R., Shirota,M., Sakakibara,Y., Chiba,J.,
            Mizushima-Sugano,J., Nakai,K. and Sugano,S.
  TITLE     Sequence comparison of human and mouse genes reveals a homologous
            block structure in the promoter regions
  JOURNAL   Genome Res 14 (9), 1711-1718 (2004)
   PUBMED   15342556
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC030788.2, BP244372.1, AC003002.1 and AW449330.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA554194.1, SRR1803614.177616.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336128.12/ ENSP00000337555.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..545
                     /product="zinc finger protein 548 isoform 1"
                     /calculated_mol_wt=63839
     Region          20..60
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          211..231
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <215..311
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          239..259
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          267..287
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <292..507
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          295..315
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(300,302,304,306..307,310..311,314,328,330,334..335,
                     338..339,342,356,358,360,362..363,366..367,370)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          323..343
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          351..371
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          379..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          407..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(440,442,444,446..447,450..451,454,468,470,474..475,
                     478..479,482,496,498,500,502..503,506..507,510)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          463..483
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          491..511
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..545
                     /gene="ZNF548"
                     /coded_by="NM_001172773.2:247..1884"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54324.1"
                     /db_xref="GeneID:147694"
                     /db_xref="HGNC:HGNC:26561"
ORIGIN      
        1 mnltegplam aemdptqgrv vfedvaiyfs qeewghldea qrllyrdvml enlallsslg
       61 swhgaedeea psqqgfsvgv sevtaskpcl ssqkvhpset cgpplkdilc lvehngihpe
      121 qhiyiceael fqhpkqqige nlsrgddwip sfgknhrvhm aeeiftcmeg wkdlpatscl
      181 lqhqgpqsew kpyrdtedre afqtgqndyk csecgktftc sysfvehqki htgersyecn
      241 kcgkffkysa nfmkhqtvht sertyecrec gksfmynyrl mrhkrvhtge rpyecntcgk
      301 ffrysstfvr hqrvhtgerp yecrecgkff mdsstlikhq rvhtgerpyk cndcgkffry
      361 istlirhqri htgerpyecs vcgelfryns slvkhwrnht gerpykcsec gksfryhcrl
      421 irhqrvhtge rpyecsecgk ffrynsnlik hwrnhtgerp yecrecgkaf shkhilvehq
      481 kihsgerpye csecqkafir kshlvhhqki hseerlvcsm nvgnslaktp tslnirdftm
      541 ekvyh
//
LOCUS       NP_060496                963 aa            linear   PRI 27-APR-2025
DEFINITION  phosphofurin acidic cluster sorting protein 1 [Homo sapiens].
ACCESSION   NP_060496
VERSION     NP_060496.2
DBSOURCE    REFSEQ: accession NM_018026.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Moller-Hansen,A., Hejla,D., Lee,H.K., Lyles,J.B., Yang,Y., Chen,K.,
            Li,W.L., Thomas,G. and Boerkoel,C.F.
  TITLE     Do PACS1 variants impeding adaptor protein binding predispose to
            syndromic intellectual disability?
  JOURNAL   Am J Med Genet A 191 (8), 2181-2187 (2023)
   PUBMED   37141437
  REMARK    GeneRIF: Do PACS1 variants impeding adaptor protein binding
            predispose to syndromic intellectual disability?
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Bruno,L.P., Doddato,G., Baldassarri,M., Rizzo,C.L., Resciniti,S.,
            Bruttini,M., Mirjam,L., Zguro,K., Furini,S., Mencarelli,M.A.,
            Renieri,A. and Ariani,F.
  TITLE     Expanding the clinical spectrum associated with the PACS1
            p.Arg203Trp mutational hot-spot: Two additional Italian patients
  JOURNAL   Am J Med Genet A 191 (1), 284-288 (2023)
   PUBMED   36210549
  REMARK    GeneRIF: Expanding the clinical spectrum associated with the PACS1
            p.Arg203Trp mutational hot-spot: Two additional Italian patients.
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Sorokina,E.A., Reis,L.M., Thompson,S., Agre,K.,
            Babovic-Vuksanovic,D., Ellingson,M.S., Hasadsri,L., van Bever,Y.
            and Semina,E.V.
  TITLE     WDR37 syndrome: identification of a distinct new cluster of
            disease-associated variants and functional analyses of mutant
            proteins
  JOURNAL   Hum Genet 140 (12), 1775-1789 (2021)
   PUBMED   34642815
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Tenorio-Castano,J., Morte,B., Nevado,J., Martinez-Glez,V.,
            Santos-Simarro,F., Garcia-Minaur,S., Palomares-Bralo,M.,
            Pacio-Miguez,M., Gomez,B., Arias,P., Alcochea,A., Carrion,J.,
            Arias,P., Almoguera,B., Lopez-Grondona,F., Lorda-Sanchez,I.,
            Galan-Gomez,E., Valenzuela,I., Mendez Perez,M.P., Cusco,I.,
            Barros,F., Pie,J., Ramos,S., Ramos,F.J., Kuechler,A., Tizzano,E.,
            Ayuso,C., Kaiser,F.J., Perez-Jurado,L.A., Carracedo,A., The
            ENoD-Ciberer,Consortium., The Side,Consortium. and Lapunzina,P.
  TITLE     Schuurs-Hoeijmakers Syndrome (PACS1 Neurodevelopmental Disorder):
            Seven Novel Patients and a Review
  JOURNAL   Genes (Basel) 12 (5), 738 (2021)
   PUBMED   34068396
  REMARK    GeneRIF: Schuurs-Hoeijmakers Syndrome (PACS1 Neurodevelopmental
            Disorder): Seven Novel Patients and a Review.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 963)
  AUTHORS   Sakaguchi,Y., Yoshihashi,H., Uehara,T., Miyama,S., Kosaki,K. and
            Takenouchi,T.
  TITLE     Coloboma may be a shared feature in a spectrum of disorders caused
            by mutations in the WDR37-PACS1-PACS2 axis
  JOURNAL   Am J Med Genet A 185 (3), 884-888 (2021)
   PUBMED   33369122
  REMARK    GeneRIF: Coloboma may be a shared feature in a spectrum of
            disorders caused by mutations in the WDR37-PACS1-PACS2 axis.
            Review article
REFERENCE   6  (residues 1 to 963)
  AUTHORS   Blagoveshchenskaya,A.D., Thomas,L., Feliciangeli,S.F., Hung,C.H.
            and Thomas,G.
  TITLE     HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6
            endocytic pathway
  JOURNAL   Cell 111 (6), 853-866 (2002)
   PUBMED   12526811
  REMARK    GeneRIF: PACS-1 along with HIV-1 nef, has a role in downregulating
            cell surface MHC-I to the trans-Golgi network and usurping the ARF6
            endocytic pathway
REFERENCE   7  (residues 1 to 963)
  AUTHORS   Crump,C.M., Xiang,Y., Thomas,L., Gu,F., Austin,C., Tooze,S.A. and
            Thomas,G.
  TITLE     PACS-1 binding to adaptors is required for acidic cluster
            motif-mediated protein traffic
  JOURNAL   EMBO J 20 (9), 2191-2201 (2001)
   PUBMED   11331585
REFERENCE   8  (residues 1 to 963)
  AUTHORS   Piguet,V., Wan,L., Borel,C., Mangasarian,A., Demaurex,N., Thomas,G.
            and Trono,D.
  TITLE     HIV-1 Nef protein binds to the cellular protein PACS-1 to
            downregulate class I major histocompatibility complexes
  JOURNAL   Nat Cell Biol 2 (3), 163-167 (2000)
   PUBMED   10707087
REFERENCE   9  (residues 1 to 963)
  AUTHORS   Wan,L., Molloy,S.S., Thomas,L., Liu,G., Xiang,Y., Rybak,S.L. and
            Thomas,G.
  TITLE     PACS-1 defines a novel gene family of cytosolic sorting proteins
            required for trans-Golgi network localization
  JOURNAL   Cell 94 (2), 205-216 (1998)
   PUBMED   9695949
REFERENCE   10 (residues 1 to 963)
  AUTHORS   Lusk,L., Smith,S., Martin,C., Taylor,C. and Chung,W.
  TITLE     PACS1 Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32672908
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP006287.2, AK096644.1,
            BC010096.1 and BQ772654.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 24, 2003 this sequence version replaced NP_060496.1.
            
            Summary: This gene encodes a protein with a putative role in the
            localization of trans-Golgi network (TGN) membrane proteins. Mouse
            and rat homologs have been identified and studies of the homologous
            rat protein indicate a role in directing TGN localization of furin
            by binding to the protease's phosphorylated cytosolic domain. In
            addition, the human protein plays a role in HIV-1 Nef-mediated
            downregulation of cell surface MHC-I molecules to the TGN, thereby
            enabling HIV-1 to escape immune surveillance. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052577.1, BC010096.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000320580.9/ ENSP00000316454.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1-q13.2"
     Protein         1..963
                     /product="phosphofurin acidic cluster sorting protein 1"
                     /note="cytosolic sorting protein PACS-1"
                     /calculated_mol_wt=104768
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K212; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8K212; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Region          78..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6VY07.2)"
     Region          168..175
                     /region_name="Involved in binding to AP-1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8K212; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Region          262..299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6VY07.2)"
     Region          377..428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Region          476..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88588; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Site            534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6VY07.2)"
     Region          548..960
                     /region_name="Pacs-1"
                     /note="PACS-1 cytosolic sorting protein; pfam10254"
                     /db_xref="CDD:463027"
     Region          760..804
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6VY07.2)"
     CDS             1..963
                     /gene="PACS1"
                     /gene_synonym="MRD17; SHMS"
                     /coded_by="NM_018026.4:216..3107"
                     /db_xref="CCDS:CCDS8129.1"
                     /db_xref="GeneID:55690"
                     /db_xref="HGNC:HGNC:30032"
                     /db_xref="MIM:607492"
ORIGIN      
        1 maerggaggg pggagggsgq rgsgvaqspq qpppqqqqqq ppqqptppkl aqatssssst
       61 saaaasssss ststsmavav asgsappggp gpgrtpapvq mnlyatwevd rsssscvprl
      121 fsltlkklvm lkemdkdlns vviavklqgs krilrsneiv lpasglvete lqltfslqyp
      181 hflkrdankl qimlqrrkry knrtilgykt lavglinmae vmqhpnegal vlglhsnvkd
      241 vsvpvaeiki yslssqpidh egiksklsdr spdidnysee eeesfsseqe gsddplhgqd
      301 lfyededlrk vkktrrklts tsaitrqpni kqkfvallkr fkvsdevgfg lehvsreqir
      361 eveedldely dslemynpsd sgpemeetes ilstpkpklk pffegmsqss sqteigslns
      421 kgslgkdtts pmelaaleki kstwiknqdd sltetdtlei tdqdmfgdas tslvvpekvk
      481 tpmkssktdl qgsaspskve gvhtprqkrs tplkerqlsk plsertnssd serspdlghs
      541 tqiprkvvyd qlnqilvsda alpenvilvn ttdwqgqyva ellqdqrkpv vctcstvevq
      601 avlsalltri qrycncnssm prpvkvaavg gqsylssilr ffvkslankt sdwlgymrfl
      661 iiplgshpva kylgsvdsky sssfldsgwr dlfsrseppv seqldvagrv mqyvngaatt
      721 hqlpvaeaml tcrhkfpded syqkfipfig vvkvglveds pstagdgdds pvvsltvpst
      781 sppsssglsr datatppssp smssalaivg spnspygdvi glqvdywlgh pgerrregdk
      841 rdasskntlk svfrsvqvsr lphsgeaqls gtmamtvvtk eknkkvptif lskkprekev
      901 dsksqviegi srlicsakqq qtmlrvsidg vewsdikffq laaqwpthvk hfpvglfsgs
      961 kat
//
LOCUS       NP_054825                691 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 770 [Homo sapiens].
ACCESSION   NP_054825 XP_090970
VERSION     NP_054825.2
DBSOURCE    REFSEQ: accession NM_014106.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Wang,H., St Julien,K.R., Stevenson,D.K., Hoffmann,T.J., Witte,J.S.,
            Lazzeroni,L.C., Krasnow,M.A., Quaintance,C.C., Oehlert,J.W.,
            Jelliffe-Pawlowski,L.L., Gould,J.B., Shaw,G.M. and O'Brodovich,H.M.
  TITLE     A genome-wide association study (GWAS) for bronchopulmonary
            dysplasia
  JOURNAL   Pediatrics 132 (2), 290-297 (2013)
   PUBMED   23897914
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA331762.1, BC071603.1, AK131433.1, AK127201.1, AC114546.14 and
            AI031776.1.
            
            On or before Apr 5, 2004 this sequence version replaced
            XP_090970.5, NP_054825.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.259756.1,
                                           SRR1660809.43153.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356321.4/ ENSP00000348673.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..691
                     /product="zinc finger protein 770"
                     /calculated_mol_wt=79876
     Region          29..49
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(34,36,38,40..41,44..45,48,62,64,68..69,72..73,76,88,
                     90,92,94..95,98..99,102)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          42..66
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          57..77
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          83..103
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          162..182
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(167,169,171,173..174,177..178,181,195,197,201..202,
                     205..206,209,223,225,227,229..230,233..234,237)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          185..530
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          190..210
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          218..238
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          258..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IQ21.1)"
     Region          477..497
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(482,484,486,488..489,492..493,496,510,512,516..517,
                     520..521,524,537,539,541,543..544,547..548)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          505..525
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          627..647
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          640..664
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          655..675
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..691
                     /gene="ZNF770"
                     /gene_synonym="PRO1914"
                     /coded_by="NM_014106.4:346..2421"
                     /db_xref="CCDS:CCDS10042.1"
                     /db_xref="GeneID:54989"
                     /db_xref="HGNC:HGNC:26061"
ORIGIN      
        1 mmaennlkml kiqqcvvank lprnrpyvcn icfkhfetps klarhyliht gqkpfecdvc
       61 hktfrqlvhl erhqlthslp fkcsicqrhf knlktfvkhq qlhnetyqnn vkqvrrllea
      121 kqeksmygvy ntftteerwa lhpcsksdpm ysmkrrknih acticgkmfp sqskldrhvl
      181 ihtgqrpfkc vlctksfrqs thlkihqlth seerpfqccf cqkgfkiqsk llkhkqihtr
      241 nkafralllk krrtesrplp nklnanqggf engeigesee nnpldvhsiy ivpfqcpkce
      301 kcfeseqiln ehscfaarsg kipsrfkrsy nyktivkkil aklkrarskk ldnfqsekkv
      361 fkksflrncd lisgeqsseq tqrtfvgslg khgtyktign rkkktltlpf swqnmgknlk
      421 gilttenils idnsvnkkdl sicgssgeef fnncevlqcg fsvprenirt rhkicpcdkc
      481 ekvfpsiskl krhylihtgq rpfgcnicgk sfrqsahlkr heqthneksp yaslcqvefg
      541 nfnnlsnhsg nnvnynasqq cqapgvqkye vsesdqmsgv kaesqdfipg stgqpclpnv
      601 lleseqsnpf csysehqekn dvflyrcsvc aksfrspskl erhylihagq kpfecsvcgk
      661 tfrqaphwkr hqlthfkerp qgkvvaldsv m
//
LOCUS       NP_003396                246 aa            linear   PRI 27-APR-2025
DEFINITION  14-3-3 protein eta [Homo sapiens].
ACCESSION   NP_003396
VERSION     NP_003396.1
DBSOURCE    REFSEQ: accession NM_003405.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Diao,S., Han,X., Ye,W.L., Zhang,C., Yang,D.M., Fan,Z.P. and
            Wang,S.L.
  TITLE     GREM1 Negatively Regulates Osteo-/Dentinogenic Differentiation of
            Dental Pulp Stem Cells via Association with YWHAH
  JOURNAL   Chin J Dent Res 27 (3), 203-213 (2024)
   PUBMED   39221981
  REMARK    GeneRIF: GREM1 Negatively Regulates Osteo-/Dentinogenic
            Differentiation of Dental Pulp Stem Cells via Association with
            YWHAH.
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Chan,Y.J., Liu,N.T., Hsin,F., Lu,J.Y., Lin,J.Y. and Liu,H.M.
  TITLE     Temporal regulation of MDA5 inactivation by Caspase-3 dependent
            cleavage of 14-3-3eta
  JOURNAL   PLoS Pathog 20 (6), e1012287 (2024)
   PUBMED   38843304
  REMARK    GeneRIF: Temporal regulation of MDA5 inactivation by Caspase-3
            dependent cleavage of 14-3-3eta.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Zhou,H., Sun,X., Dai,Y., Wang,X., Dai,Z. and Li,X.
  TITLE     14-3-3-eta interacts with BCL-2 to protect human endothelial
            progenitor cells from ox-LDL-triggered damage
  JOURNAL   Cell Biol Int 48 (3), 290-299 (2024)
   PUBMED   38100125
  REMARK    GeneRIF: 14-3-3-eta interacts with BCL-2 to protect human
            endothelial progenitor cells from ox-LDL-triggered damage.
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Liu,Y.Q., Xu,Y.C. and Shuai,Z.W.
  TITLE     Mir-142-3P regulates MAPK protein family by inhibiting 14-3-3eta to
            enhance bone marrow mesenchymal stem cells osteogenesis
  JOURNAL   Sci Rep 13 (1), 22862 (2023)
   PUBMED   38129425
  REMARK    GeneRIF: Mir-142-3P regulates MAPK protein family by inhibiting
            14-3-3eta to enhance bone marrow mesenchymal stem cells
            osteogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Pierga,A., Matusiak,R., Cauhape,M., Branchu,J., Danglot,L.,
            Boutry,M. and Darios,F.
  TITLE     Spatacsin regulates directionality of lysosome trafficking by
            promoting the degradation of its partner AP5Z1
  JOURNAL   PLoS Biol 21 (10), e3002337 (2023)
   PUBMED   37871017
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Ichimura,T., Uchiyama,J., Kunihiro,O., Ito,M., Horigome,T.,
            Omata,S., Shinkai,F., Kaji,H. and Isobe,T.
  TITLE     Identification of the site of interaction of the 14-3-3 protein
            with phosphorylated tryptophan hydroxylase
  JOURNAL   J Biol Chem 270 (48), 28515-28518 (1995)
   PUBMED   7499362
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Jones,D.H., Ley,S. and Aitken,A.
  TITLE     Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo
            and in vitro: implications for function as adapter proteins
  JOURNAL   FEBS Lett 368 (1), 55-58 (1995)
   PUBMED   7615088
REFERENCE   8  (residues 1 to 246)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   9  (residues 1 to 246)
  AUTHORS   Ichimura-Ohshima,Y., Morii,K., Ichimura,T., Araki,K., Takahashi,Y.,
            Isobe,T., Minoshima,S., Fukuyama,R., Shimizu,N. and Kuwano,R.
  TITLE     cDNA cloning and chromosome assignment of the gene for human brain
            14-3-3 protein eta chain
  JOURNAL   J Neurosci Res 31 (4), 600-605 (1992)
   PUBMED   1578511
REFERENCE   10 (residues 1 to 246)
  AUTHORS   Ichimura,T., Isobe,T., Okuyama,T., Takahashi,N., Araki,K.,
            Kuwano,R. and Takahashi,Y.
  TITLE     Molecular cloning of cDNA coding for brain-specific 14-3-3 protein,
            a protein kinase-dependent activator of tyrosine and tryptophan
            hydroxylases
  JOURNAL   Proc Natl Acad Sci U S A 85 (19), 7084-7088 (1988)
   PUBMED   2902623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z82248.1, BC003047.1 and
            AY007132.1.
            
            Summary: This gene product belongs to the 14-3-3 family of proteins
            which mediate signal transduction by binding to
            phosphoserine-containing proteins. This highly conserved protein
            family is found in both plants and mammals, and this protein is 99%
            identical to the mouse, rat and bovine orthologs. This gene
            contains a 7 bp repeat sequence in its 5' UTR, and changes in the
            number of this repeat have been associated with early-onset
            schizophrenia and psychotic bipolar disorder. [provided by RefSeq,
            Jun 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.310288.1,
                                           SRR3476690.534567.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248975.6/ ENSP00000248975.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..246
                     /product="14-3-3 protein eta"
                     /note="14-3-3 eta; tyrosine 3-monooxygenase/tryptophan
                     5-monooxygenase activation protein, eta polypeptide"
                     /calculated_mol_wt=28088
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine. /evidence=ECO:0000269|Ref.11;
                     propagated from UniProtKB/Swiss-Prot (Q04917.4)"
     Region          3..241
                     /region_name="14-3-3_eta"
                     /note="14-3-3 eta, an isoform of 14-3-3 protein; cd10025"
                     /db_xref="CDD:206761"
     Site            order(10,13..14,16..17,19,22,59,62..63,66,85,88..89,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:206761"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q04917.4)"
     Site            order(50,57,132..133,177..178,181,222,225,229)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:206761"
     Site            57
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein; propagated from UniProtKB/Swiss-Prot (Q04917.4)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P68510; propagated from
                     UniProtKB/Swiss-Prot (Q04917.4)"
     Site            132
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein; propagated from UniProtKB/Swiss-Prot (Q04917.4)"
     CDS             1..246
                     /gene="YWHAH"
                     /gene_synonym="YWHA1"
                     /coded_by="NM_003405.4:200..940"
                     /db_xref="CCDS:CCDS13901.1"
                     /db_xref="GeneID:7533"
                     /db_xref="HGNC:HGNC:12853"
                     /db_xref="MIM:113508"
ORIGIN      
        1 mgdreqllqr arlaeqaery ddmasamkav telneplsne drnllsvayk nvvgarrssw
       61 rvissieqkt madgnekkle kvkayrekie keletvcndv lslldkflik ncndfqyesk
      121 vfylkmkgdy yrylaevasg ekknsvveas eaaykeafei skeqmqpthp irlglalnfs
      181 vfyyeiqnap eqacllakqa fddaiaeldt lnedsykdst limqllrdnl tlwtsdqqde
      241 eagegn
//
LOCUS       NP_065984                595 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 317 isoform 1 [Homo sapiens].
ACCESSION   NP_065984
VERSION     NP_065984.3
DBSOURCE    REFSEQ: accession NM_020933.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 595)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   5  (residues 1 to 595)
  AUTHORS   Takashima,H., Nishio,H., Wakao,H., Nishio,M., Koizumi,K., Oda,A.,
            Koike,T. and Sawada,K.
  TITLE     Molecular cloning and characterization of a KRAB-containing zinc
            finger protein, ZNF317, and its isoforms
  JOURNAL   Biochem Biophys Res Commun 288 (4), 771-779 (2001)
   PUBMED   11688974
  REMARK    GeneRIF: molecular cloning and characterization of isoforms
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA757943.1 and BC078154.1.
            
            On Jun 18, 2008 this sequence version replaced NP_065984.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056570.1, SRR1803611.199849.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247956.11/ ENSP00000247956.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..595
                     /product="zinc finger protein 317 isoform 1"
                     /note="KRAB-containing zinc finger protein 317"
                     /calculated_mol_wt=67828
     Region          57..109
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          109..128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PQ6.2)"
     Region          222..580
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          224..244
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          252..272
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          280..300
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(285,287,289,291..292,295..296,299,313,315,319..320,
                     323..324,327,341,343,345,347..348,351..352,355)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          308..328
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          336..356
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          364..384
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          392..412
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          420..440
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(425,427,429,431..432,435..436,439,453,455,459..460,
                     463..464,467,481,483,485,487..488,491..492,495)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          448..468
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          476..496
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          504..524
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(509,511,513,515..516,519..520,523,537,539,543..544,
                     547..548,551,565,567,569,571..572,575..576,579)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          532..552
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          560..580
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..595
                     /gene="ZNF317"
                     /coded_by="NM_020933.5:289..2076"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12210.1"
                     /db_xref="GeneID:57693"
                     /db_xref="HGNC:HGNC:13507"
                     /db_xref="MIM:613864"
ORIGIN      
        1 maalsptfat stqdstclqd sefpvsskdh scpqnldlfv csglephtps vgsqesvtfq
       61 dvavdfteke wplldssqrk lykdvmleny snltslgyqv gkpslishle qeeeprteer
      121 gahqgacadw etpsktkwsl lmedifgket psgvtmerag lgeksteyah lfevfgmdph
      181 ltqpmgrhag krpyhrrdyg vafkgrphlt qhmsmydgrk mhechqcqka fttsasltrh
      241 rrihtgekpy ecsdcgkafn dpsalrshar thlkekpfdc sqcgnafrtl salkihmrvh
      301 tgerpykcdq cgkaygrsch liahkrthtg erpyechdcg kafqhpshlk ehvrnhtgek
      361 pyactqcgka frwksnfnlh kknhmvekty eckecgksfg dlvsrrkhmr ihivkkpvec
      421 rqcgktfrnq silkthmnsh tgekpygcdl cgkafsassn ltahrkihtq erryecaacg
      481 kvfgdylsrr rhmsvhlvkk rvecrqcgka frnqstlkth mrshtgekpy ecdhcgkafs
      541 igsnlnvhrr ihtgekpyec lvcgkafsdh sslrshvkth rgeklfvssv wkrlq
//
LOCUS       NP_663622               1066 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 31 isoform 1 [Homo sapiens].
ACCESSION   NP_663622
VERSION     NP_663622.2
DBSOURCE    REFSEQ: accession NM_145647.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 1066)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 1066)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK056434.1, BC143525.1, BC101724.1 and CA429516.1.
            
            On Feb 9, 2009 this sequence version replaced NP_663622.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056434.1, SRR1803615.254251.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287380.6/ ENSP00000287380.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..1066
                     /product="TBC1 domain family member 31 isoform 1"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=124059
     Region          33..74
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          44..340
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          46..81
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          75..116
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          86..123
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          117..157
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          130..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          158..200
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          201..248
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          215..253
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          249..296
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          261..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          297..334
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          309..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          462..605
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <684..>962
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          989..1020
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          1053..1056
                     /region_name="Mediates direct interaction with PJA2.
                     /evidence=ECO:0000269|PubMed:33934390"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     CDS             1..1066
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_145647.4:64..3264"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6338.1"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
ORIGIN      
        1 mqstdlgnke sgkiwhrkps patrdgiivn iihntsdyhp kvlrflnvaf dgtgdcliag
       61 dhqgniyvfd lhgnrfnlvq rtaqactala fnlrrksefl valadysikc fdtvtkelvs
      121 wmrghessvf sisvhasgky aittssdtaq lwdldtfqrk rklnirqsvg iqkvfflpls
      181 ntilscfkdn sifawecdtl fckyqlpapp esssilykvf avtrdgrila aggksnhlhl
      241 wclearqlfr iiqmptkvra irhleflpds fdagsnqvlg vlsqdgimrf inmqtckllf
      301 eigsldegis ssaisphgry iasimengsl niysvqaltq einkpppplv kviedlpknk
      361 lsssdlkmkv tsgrvqqpak sreskmqtri lkqdltgdfe skknelpdgl nkkrlqillk
      421 gygeyptkyr mfiwrsllql penhtafstl idkgthvafl nlqkkypiks rkllrvlqrt
      481 lsalahwsvi fsdtpylpll afpfvklfqn nqlicfevia tliinwcqhw feyfpnppin
      541 ilsmienvla fhdkellqhf idhditsqly awplletvfs evltreewlk lfdnifsnhp
      601 sfllmtvvay nicsrtplls cnlkddfeff fhhrnnldin vvirqvyhlm ettptdihpd
      661 smlnvfvalt kgqypvfnqy pkfivdyqtq ererirndel dylrerqtve dmqakvdqqr
      721 vedeawyqkq ellrkaeetr remllqeeek miqqrqrlaa vkrelkvkem hlqdaarrrf
      781 lklqqdqqem elrrlddeig rkvymrdrei aatardlemr qlelesqkrl yeknltenqe
      841 alakemrada dayrrkvdle ehmfhkliea getqsqktqk vikenlakae qaclntdwqi
      901 qslhkqkcdd lqrnkcyqev akllrenrrk eieiinamve eeakkwkeae gkefrlrsak
      961 kasalsdasr kwflkqeina avehaenpch keeprfqneq dssclprtsq lndssemdps
     1021 tqislnrrav ewdttgqnli kkvrnlrqrl tararhrcqt phllaa
//
LOCUS       NP_001013721             135 aa            linear   PRI 27-APR-2025
DEFINITION  histone H3.3C [Homo sapiens].
ACCESSION   NP_001013721 XP_495919
VERSION     NP_001013721.2
DBSOURCE    REFSEQ: accession NM_001013699.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Seal,R.L., Denny,P., Bruford,E.A., Gribkova,A.K., Landsman,D.,
            Marzluff,W.F., McAndrews,M., Panchenko,A.R., Shaytan,A.K. and
            Talbert,P.B.
  TITLE     A standardized nomenclature for mammalian histone genes
  JOURNAL   Epigenetics Chromatin 15 (1), 34 (2022)
   PUBMED   36180920
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Shiraishi,K., Shindo,A., Harada,A., Kurumizaka,H., Kimura,H.,
            Ohkawa,Y. and Matsuyama,H.
  TITLE     Roles of histone H3.5 in human spermatogenesis and spermatogenic
            disorders
  JOURNAL   Andrology 6 (1), 158-165 (2018)
   PUBMED   29179259
  REMARK    GeneRIF: H3.5 may play roles in DNA synthesis, but not apoptosis,
            and its expression is regulated by gonadotropins
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Urahama,T., Harada,A., Maehara,K., Horikoshi,N., Sato,K., Sato,Y.,
            Shiraishi,K., Sugino,N., Osakabe,A., Tachiwana,H., Kagawa,W.,
            Kimura,H., Ohkawa,Y. and Kurumizaka,H.
  TITLE     Histone H3.5 forms an unstable nucleosome and accumulates around
            transcription start sites in human testis
  JOURNAL   Epigenetics Chromatin 9, 2 (2016)
   PUBMED   26779285
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 135)
  AUTHORS   Sadakierska-Chudy,A., Kostrzewa,R.M. and Filip,M.
  TITLE     A comprehensive view of the epigenetic landscape part I: DNA
            methylation, passive and active DNA demethylation pathways and
            histone variants
  JOURNAL   Neurotox Res 27 (1), 84-97 (2015)
   PUBMED   25362550
  REMARK    Review article
REFERENCE   7  (residues 1 to 135)
  AUTHORS   Schenk,R., Jenke,A., Zilbauer,M., Wirth,S. and Postberg,J.
  TITLE     H3.5 is a novel hominid-specific histone H3 variant that is
            specifically expressed in the seminiferous tubules of human testes
  JOURNAL   Chromosoma 120 (3), 275-285 (2011)
   PUBMED   21274551
  REMARK    GeneRIF: H3.5 preferentially colocalizes with euchromatin, and it
            is associated with actively transcribed genes and can replace an
            essential function of RNAi-depleted H3.3 in cell growth.
REFERENCE   8  (residues 1 to 135)
  AUTHORS   Scherer,S.E., Muzny,D.M., Buhay,C.J., Chen,R., Cree,A., Ding,Y.,
            Dugan-Rocha,S., Gill,R., Gunaratne,P., Harris,R.A., Hawes,A.C.,
            Hernandez,J., Hodgson,A.V., Hume,J., Jackson,A., Khan,Z.M.,
            Kovar-Smith,C., Lewis,L.R., Lozado,R.J., Metzker,M.L.,
            Milosavljevic,A., Miner,G.R., Montgomery,K.T., Morgan,M.B.,
            Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z., Steffen,D.,
            Lovering,R.C., Wheeler,D.A., Worley,K.C., Yuan,Y., Zhang,Z.,
            Adams,C.Q., Ansari-Lari,M.A., Ayele,M., Brown,M.J., Chen,G.,
            Chen,Z., Clerc-Blankenburg,K.P., Davis,C., Delgado,O., Dinh,H.H.,
            Draper,H., Gonzalez-Garay,M.L., Havlak,P., Jackson,L.R.,
            Jacob,L.S., Kelly,S.H., Li,L., Li,Z., Liu,J., Liu,W., Lu,J.,
            Maheshwari,M., Nguyen,B.V., Okwuonu,G.O., Pasternak,S., Perez,L.M.,
            Plopper,F.J., Santibanez,J., Shen,H., Tabor,P.E., Verduzco,D.,
            Waldron,L., Wang,Q., Williams,G.A., Zhang,J., Zhou,J., Allen,C.C.,
            Amin,A.G., Anyalebechi,V., Bailey,M., Barbaria,J.A., Bimage,K.E.,
            Bryant,N.P., Burch,P.E., Burkett,C.E., Burrell,K.L., Calderon,E.,
            Cardenas,V., Carter,K., Casias,K., Cavazos,I., Cavazos,S.R.,
            Ceasar,H., Chacko,J., Chan,S.N., Chavez,D., Christopoulos,C.,
            Chu,J., Cockrell,R., Cox,C.D., Dang,M., Dathorne,S.R., David,R.,
            Davis,C.M., Davy-Carroll,L., Deshazo,D.R., Donlin,J.E., D'Souza,L.,
            Eaves,K.A., Simons,R., Emery-Cohen,A.J., Escotto,M., Flagg,N.,
            Forbes,L.D., Gabisi,A.M., Garza,M., Hamilton,C., Henderson,N.,
            Hernandez,O., Hines,S., Hogues,M.E., Huang,M., Idlebird,D.G.,
            Johnson,R., Jolivet,A., Jones,S., Kagan,R., King,L.M., Leal,B.,
            Lebow,H., Lee,S., LeVan,J.M., Lewis,L.C., London,P.,
            Lorensuhewa,L.M., Loulseged,H., Lovett,D.A., Lucier,A.,
            Lucier,R.L., Ma,J., Madu,R.C., Mapua,P., Martindale,A.D.,
            Martinez,E., Massey,E., Mawhiney,S., Meador,M.G., Mendez,S.,
            Mercado,C., Mercado,I.C., Merritt,C.E., Miner,Z.L., Minja,E.,
            Mitchell,T., Mohabbat,F., Mohabbat,K., Montgomery,B., Moore,N.,
            Morris,S., Munidasa,M., Ngo,R.N., Nguyen,N.B., Nickerson,E.,
            Nwaokelemeh,O.O., Nwokenkwo,S., Obregon,M., Oguh,M., Oragunye,N.,
            Oviedo,R.J., Parish,B.J., Parker,D.N., Parrish,J., Parks,K.L.,
            Paul,H.A., Payton,B.A., Perez,A., Perrin,W., Pickens,A.,
            Primus,E.L., Pu,L.L., Puazo,M., Quiles,M.M., Quiroz,J.B.,
            Rabata,D., Reeves,K., Ruiz,S.J., Shao,H., Sisson,I., Sonaike,T.,
            Sorelle,R.P., Sutton,A.E., Svatek,A.F., Svetz,L.A., Tamerisa,K.S.,
            Taylor,T.R., Teague,B., Thomas,N., Thorn,R.D., Trejos,Z.Y.,
            Trevino,B.K., Ukegbu,O.N., Urban,J.B., Vasquez,L.I., Vera,V.A.,
            Villasana,D.M., Wang,L., Ward-Moore,S., Warren,J.T., Wei,X.,
            White,F., Williamson,A.L., Wleczyk,R., Wooden,H.S., Wooden,S.H.,
            Yen,J., Yoon,L., Yoon,V., Zorrilla,S.E., Nelson,D.,
            Kucherlapati,R., Weinstock,G. and Gibbs,R.A.
  CONSRTM   Baylor College of Medicine Human Genome Sequencing Center Sequence
            Production Team
  TITLE     The finished DNA sequence of human chromosome 12
  JOURNAL   Nature 440 (7082), 346-351 (2006)
   PUBMED   16541075
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC023050.36.
            
            On May 17, 2008 this sequence version replaced NP_001013721.1.
            
            Summary: Histones are basic nuclear proteins that are responsible
            for the nucleosome structure of the chromosomal fiber in
            eukaryotes. Nucleosomes consist of approximately 146 bp of DNA
            wrapped around a histone octamer composed of pairs of each of the
            four core histones (H2A, H2B, H3, and H4). The chromatin fiber is
            further compacted through the interaction of a linker histone, H1,
            with the DNA between the nucleosomes to form higher order chromatin
            structures. This gene contains introns and its mRNA is
            polyadenylated, unlike most histone genes. The protein encoded by
            this gene is a replication-independent histone that is a member of
            the histone H3 family. [provided by RefSeq, Oct 2015].
            
            ##Evidence-Data-START##
            Transcript is intronless :: HQ873957.1, BC066906.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match              :: ENST00000340398.5/
                                               ENSP00000339835.3
            RefSeq Select criteria          :: based on single protein-coding
                                               transcript
            replication-independent histone :: PMID: 21274551
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.21"
     Protein         1..135
                     /product="histone H3.3C"
                     /note="histone variant H3.5; histone H3.5; H3 histone,
                     family 3C; H3 histone family member 3C"
                     /calculated_mol_wt=15083
     Region          1..135
                     /region_name="PTZ00018"
                     /note="histone H3; Provisional"
                     /db_xref="CDD:185400"
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            3
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by HASPIN.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            5
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; N6-methyllysine,
                     alternate. /evidence=ECO:0000250|UniProtKB:P68431;
                     propagated from UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            9
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT5, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68433; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            10
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68432;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68432; N6-methyllysine,
                     alternate. /evidence=ECO:0000250|UniProtKB:P68432;
                     propagated from UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            10
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate, by AURKB, AURKC, RPS6KA3,
                     RPS6KA4 and RPS6KA5.
                     /evidence=ECO:0000250|UniProtKB:P68432; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            15
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68432; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            18
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by CARM1, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            19
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            19
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            24
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68432; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            24
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            28
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68432;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68432; N6-methyllysine,
                     alternate. /evidence=ECO:0000250|UniProtKB:P68432;
                     propagated from UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate, by AURKB, AURKC and
                     RPS6KA5. /evidence=ECO:0000250|UniProtKB:P68432;
                     propagated from UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P84243; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            37
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            order(39..47,49,63..66,69,72,83..86,116..118,120)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:467036"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            order(44,47,50..51,54..55,57,59,61..62,66..67,69..71,
                     73..74,76,78,81..85,87..88,91..92,95..97,99..101,103..105,
                     108,117..121,125,128)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467036"
     Site            order(48,51..52,55..56,58,94,98,101,108,112,117)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467036"
     Site            56
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; N6-methyllysine,
                     by EHMT2, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            56
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20850016; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            64
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:20850016; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P84243; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            order(106,109..110,113..114,116,122..123,126..127,
                     129..131)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:467036"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q71DI3; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            115
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            122
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     Site            122
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P68431; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT2.3)"
     CDS             1..135
                     /gene="H3-5"
                     /gene_synonym="H3.3C; H3.5; H3F3C"
                     /coded_by="NM_001013699.3:133..540"
                     /db_xref="CCDS:CCDS31769.1"
                     /db_xref="GeneID:440093"
                     /db_xref="HGNC:HGNC:33164"
                     /db_xref="MIM:616134"
ORIGIN      
        1 martkqtark stggkaprkq latkaarkst pstcgvkphr yrpgtvalre irryqkstel
       61 lirklpfqrl vreiaqdfnt dlrfqsaavg alqeaseayl vglledtnlc aihakrvtim
      121 pkdiqlarri rgera
//
LOCUS       NP_006077                450 aa            linear   PRI 27-APR-2025
DEFINITION  tubulin beta-3 chain isoform 1 [Homo sapiens].
ACCESSION   NP_006077
VERSION     NP_006077.2
DBSOURCE    REFSEQ: accession NM_006086.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Sun,X., Zhang,Y., Xin,S., Jin,L., Cao,Q., Wang,H., Wang,K., Liu,X.,
            Tang,C., Li,W., Li,Z., Wen,X., Yang,G., Guo,C., Liu,Z. and Ye,L.
  TITLE     NOTCH3 promotes docetaxel resistance of prostate cancer cells
            through regulating TUBB3 and MAPK signaling pathway
  JOURNAL   Cancer Sci 115 (2), 412-426 (2024)
   PUBMED   38115797
  REMARK    GeneRIF: NOTCH3 promotes docetaxel resistance of prostate cancer
            cells through regulating TUBB3 and MAPK signaling pathway.
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Xie,X., Laster,K.V., Li,J., Nie,W., Yi,Y.W., Liu,K., Seong,Y.S.,
            Dong,Z. and Kim,D.J.
  TITLE     OSGIN1 is a novel TUBB3 regulator that promotes tumor progression
            and gefitinib resistance in non-small cell lung cancer
  JOURNAL   Cell Mol Life Sci 80 (9), 272 (2023)
   PUBMED   37646890
  REMARK    GeneRIF: OSGIN1 is a novel TUBB3 regulator that promotes tumor
            progression and gefitinib resistance in non-small cell lung cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Radwitz,J., Hausrat,T.J., Heisler,F.F., Janiesch,P.C., Pechmann,Y.,
            Rubhausen,M. and Kneussel,M.
  TITLE     Tubb3 expression levels are sensitive to neuronal activity changes
            and determine microtubule growth and kinesin-mediated transport
  JOURNAL   Cell Mol Life Sci 79 (11), 575 (2022)
   PUBMED   36309617
  REMARK    GeneRIF: Tubb3 expression levels are sensitive to neuronal activity
            changes and determine microtubule growth and kinesin-mediated
            transport.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Jang,Y., Kwak,E., An,J.Y. and Jung,J.H.
  TITLE     Infantile esotropia in a family with TUBB3 mutation associated
            congenital fibrosis of extraocular muscles
  JOURNAL   Ophthalmic Genet 43 (5), 716-719 (2022)
   PUBMED   35765833
  REMARK    GeneRIF: Infantile esotropia in a family with TUBB3 mutation
            associated congenital fibrosis of extraocular muscles.
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Ranganathan,S., Dexter,D.W., Benetatos,C.A. and Hudes,G.R.
  TITLE     Cloning and sequencing of human betaIII-tubulin cDNA: induction of
            betaIII isotype in human prostate carcinoma cells by acute exposure
            to antimicrotubule agents
  JOURNAL   Biochim Biophys Acta 1395 (2), 237-245 (1998)
   PUBMED   9473684
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Vinores,S.A., Derevjanik,N.L., Mahlow,J., Hackett,S.F.,
            Haller,J.A., deJuan,E., Frankfurter,A. and Campochiaro,P.A.
  TITLE     Class III beta-tubulin in human retinal pigment epithelial cells in
            culture and in epiretinal membranes
  JOURNAL   Exp Eye Res 60 (4), 385-400 (1995)
   PUBMED   7789418
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Bahi-Buisson,N. and Maillard,C.
  TITLE     Tubulinopathies Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27010057
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Whitman,M.C., Jurgens,J.A., Hunter,D.G. and Engle,E.C.
  TITLE     Congenital Fibrosis of the Extraocular Muscles Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301522
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Burgoyne,R.D., Cambray-Deakin,M.A., Lewis,S.A., Sarkar,S. and
            Cowan,N.J.
  TITLE     Differential distribution of beta-tubulin isotypes in cerebellum
  JOURNAL   EMBO J 7 (8), 2311-2319 (1988)
   PUBMED   2461292
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Sullivan,K.F. and Cleveland,D.W.
  TITLE     Identification of conserved isotype-defining variable region
            sequences for four vertebrate beta tubulin polypeptide classes
  JOURNAL   Proc Natl Acad Sci U S A 83 (12), 4327-4331 (1986)
   PUBMED   3459176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA054466.1, AK223039.1 and
            BC003021.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 26, 2004 this sequence version replaced NP_006077.1.
            
            Summary: This gene encodes a class III member of the beta tubulin
            protein family. Beta tubulins are one of two core protein families
            (alpha and beta tubulins) that heterodimerize and assemble to form
            microtubules. This protein is primarily expressed in neurons and
            may be involved in neurogenesis and axon guidance and maintenance.
            Mutations in this gene are the cause of congenital fibrosis of the
            extraocular muscles type 3. Alternate splicing results in multiple
            transcript variants. A pseudogene of this gene is found on
            chromosome 6. [provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.636719.1,
                                           SRR3476690.954592.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315491.12/ ENSP00000320295.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..450
                     /product="tubulin beta-3 chain isoform 1"
                     /note="class III beta-tubulin; tubulin beta-III; tubulin
                     beta-4 chain; tubulin, beta 3"
                     /calculated_mol_wt=50302
     Region          1..447
                     /region_name="PLN00220"
                     /note="tubulin beta chain; Provisional"
                     /db_xref="CDD:215107"
     Region          1..4
                     /region_name="MREI motif.
                     /evidence=ECO:0000250|UniProtKB:P07437"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13509.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:16371510; propagated from
                     UniProtKB/Swiss-Prot (Q13509.2)"
     Region          425..450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13509.2)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q2T9S0; propagated from
                     UniProtKB/Swiss-Prot (Q13509.2)"
     CDS             1..450
                     /gene="TUBB3"
                     /gene_synonym="beta-4; CDCBM; CDCBM1; CFEOM3; CFEOM3A;
                     FEOM3; TUBB4"
                     /coded_by="NM_006086.4:61..1413"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10988.1"
                     /db_xref="GeneID:10381"
                     /db_xref="HGNC:HGNC:20772"
                     /db_xref="MIM:602661"
ORIGIN      
        1 mreivhiqag qcgnqigakf wevisdehgi dpsgnyvgds dlqlerisvy yneasshkyv
       61 prailvdlep gtmdsvrsga fghlfrpdnf ifgqsgagnn wakghytega elvdsvldvv
      121 rkecencdcl qgfqlthslg ggtgsgmgtl liskvreeyp drimntfsvv pspkvsdtvv
      181 epynatlsih qlventdety cidnealydi cfrtlklatp tygdlnhlvs atmsgvttsl
      241 rfpgqlnadl rklavnmvpf prlhffmpgf apltargsqq yraltvpelt qqmfdaknmm
      301 aacdprhgry ltvatvfrgr msmkevdeqm laiqsknssy fvewipnnvk vavcdipprg
      361 lkmsstfign staiqelfkr iseqftamfr rkaflhwytg egmdemefte aesnmndlvs
      421 eyqqyqdata eeegemyedd eeeseaqgpk
//
LOCUS       NP_113679                135 aa            linear   PRI 27-APR-2025
DEFINITION  retinol-binding protein 5 isoform 1 [Homo sapiens].
ACCESSION   NP_113679
VERSION     NP_113679.1
DBSOURCE    REFSEQ: accession NM_031491.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Ho,J.C., Cheung,S.T., Poon,W.S., Lee,Y.T., Ng,I.O. and Fan,S.T.
  TITLE     Down-regulation of retinol binding protein 5 is associated with
            aggressive tumor features in hepatocellular carcinoma
  JOURNAL   J Cancer Res Clin Oncol 133 (12), 929-936 (2007)
   PUBMED   17497168
  REMARK    GeneRIF: Our study revealed that RBP5 down-regulation in HCC was
            associated with aggressive tumor features, suggesting an
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Folli,C., Calderone,V., Ottonello,S., Bolchi,A., Zanotti,G.,
            Stoppini,M. and Berni,R.
  TITLE     Identification, retinoid binding, and x-ray analysis of a human
            retinol-binding protein
  JOURNAL   Proc Natl Acad Sci U S A 98 (7), 3710-3715 (2001)
   PUBMED   11274389
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC029355.1 and AA912830.1.
            
            Summary: The protein encoded by this gene is a cellular
            retinol-binding protein expressed highly in kidney and liver.
            Down-regulation of the encoded protein in hepatocellular carcinoma
            was associated with large tumor size and poor patient survival
            rates. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223378.1, SRR5189664.38728.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159080, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000266560.8/ ENSP00000266560.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..135
                     /product="retinol-binding protein 5 isoform 1"
                     /note="putative cellular retinol-binding protein CRBP III;
                     cellular retinol-binding protein III; retinol binding
                     protein 5, cellular"
                     /calculated_mol_wt=15800
     Region          4..134
                     /region_name="CRBP3"
                     /note="cellular retinol-binding protein 3; cd19464"
                     /db_xref="CDD:381239"
     Site            order(5,11,17,20..21,24,26,30..31,33..34,37,39,41,43,50,
                     52,54,56,58..61,63,65,73,75,78,94,96,105,107,109,116,118,
                     120,129,131)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381239"
     Site            order(5,11,17,20..21,24,26,30,33..34,37,39,41,43,50,52,54,
                     56,58..61,63,78,94,105,107,109,118,120,131)
                     /site_type="other"
                     /note="retinol binding site [chemical binding]"
                     /db_xref="CDD:381239"
     CDS             1..135
                     /gene="RBP5"
                     /gene_synonym="CRBP-III; CRBP3; CRBPIII; HRBPiso"
                     /coded_by="NM_031491.4:115..522"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8574.1"
                     /db_xref="GeneID:83758"
                     /db_xref="HGNC:HGNC:15847"
                     /db_xref="MIM:611866"
ORIGIN      
        1 mppnltgyyr fvsqknmedy lqalnislav rkialllkpd keiehqgnhm tvrtlstfrn
       61 ytvqfdvgve feedlrsvdg rkcqtivtwe eehlvcvqkg evpnrgwrhw legemlylel
      121 tardavceqv frkvr
//
LOCUS       NP_001356346             273 aa            linear   PRI 27-APR-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 3 [Homo sapiens].
ACCESSION   NP_001356346 XP_016881955
VERSION     NP_001356346.1
DBSOURCE    REFSEQ: accession NM_001369417.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
            Review article
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Du,P., Li,G., Wu,L. and Huang,M.
  TITLE     Perspectives of ERCC1 in early-stage and advanced cervical cancer:
            From experiments to clinical applications
  JOURNAL   Front Immunol 13, 1065379 (2023)
   PUBMED   36713431
  REMARK    GeneRIF: Perspectives of ERCC1 in early-stage and advanced cervical
            cancer: From experiments to clinical applications.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 273)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 273)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138128.1, AC139353.3 and
            AC092309.3.
            
            On Apr 9, 2019 this sequence version replaced XP_016881955.1.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.299199.1,
                                           SRR14038194.191105.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..273
                     /product="DNA excision repair protein ERCC-1 isoform 3"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=29862
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          235..264
                     /region_name="HHH"
                     /note="Helix-hairpin-helix motif; pfam00633"
                     /db_xref="CDD:425789"
     CDS             1..273
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369417.1:206..1027"
                     /note="isoform 3 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS54279.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrsleqli
      241 aasredlalc pglgpqkarr lfdvlhepfl kvp
//
LOCUS       NP_789846                 61 aa            linear   PRI 27-APR-2025
DEFINITION  metallothionein-1M [Homo sapiens].
ACCESSION   NP_789846
VERSION     NP_789846.2
DBSOURCE    REFSEQ: accession NM_176870.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Li,K., Sun,S., Lu,Y., Liang,W., Xu,X., Zhang,H., Chang,Z., Wang,C.,
            Gao,Y. and Chen,L.
  TITLE     MT1M regulates gastric cancer progression and stemness by
            modulating the Hedgehog pathway protein GLI1
  JOURNAL   Biochem Biophys Res Commun 670, 63-72 (2023)
   PUBMED   37276792
  REMARK    GeneRIF: MT1M regulates gastric cancer progression and stemness by
            modulating the Hedgehog pathway protein GLI1.
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Li,D., Peng,W., Wu,B., Liu,H., Zhang,R., Zhou,R., Yao,L. and Ye,L.
  TITLE     Metallothionein MT1M Suppresses Carcinogenesis of Esophageal
            Carcinoma Cells through Inhibition of the Epithelial-Mesenchymal
            Transition and the SOD1/PI3K Axis
  JOURNAL   Mol Cells 44 (4), 267-278 (2021)
   PUBMED   33820882
  REMARK    GeneRIF: Metallothionein MT1M Suppresses Carcinogenesis of
            Esophageal Carcinoma Cells through Inhibition of the
            Epithelial-Mesenchymal Transition and the SOD1/PI3K Axis.
REFERENCE   3  (residues 1 to 61)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 61)
  AUTHORS   Maleckaite,R., Zalimas,A., Bakavicius,A., Jankevicius,F.,
            Jarmalaite,S. and Daniunaite,K.
  TITLE     DNA methylation of metallothionein genes is associated with the
            clinical features of renal cell carcinoma
  JOURNAL   Oncol Rep 41 (6), 3535-3544 (2019)
   PUBMED   31002354
  REMARK    GeneRIF: In clear cell renal cell carcinoma (RCC) MT1E, MT1G and
            MT1M expression was higher than that noted in other histological
            tumor subtypes (all P<0.0500). In addition, some associations were
            observed between metabolic syndromerelated clinical parameters and
            promoter methylation or gene expression
REFERENCE   5  (residues 1 to 61)
  AUTHORS   Changjun,L., Feizhou,H., Dezhen,P., Zhao,L. and Xianhai,M.
  TITLE     MiR-545-3p/MT1M axis regulates cell proliferation, invasion and
            migration in hepatocellular carcinoma
  JOURNAL   Biomed Pharmacother 108, 347-354 (2018)
   PUBMED   30227328
  REMARK    GeneRIF: MiR-545-3p, which served as a tumor promoter,
            post-transcriptionally regulate MT1M in HCC through binding to its
            untranslated region (3'UTR).
REFERENCE   6  (residues 1 to 61)
  AUTHORS   Izmailova,E., Bertley,F.M., Huang,Q., Makori,N., Miller,C.J.,
            Young,R.A. and Aldovini,A.
  TITLE     HIV-1 Tat reprograms immature dendritic cells to express
            chemoattractants for activated T cells and macrophages
  JOURNAL   Nat Med 9 (2), 191-197 (2003)
   PUBMED   12539042
REFERENCE   7  (residues 1 to 61)
  AUTHORS   Vandeghinste,N., Proost,P. and De Ley,M.
  TITLE     Metallothionein isoform gene expression in zinc-treated human
            peripheral blood lymphocytes
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 46 (2), 419-433 (2000)
   PUBMED   10774930
REFERENCE   8  (residues 1 to 61)
  AUTHORS   Hellemans,G., Soumillion,A., Proost,P., Van Damme,J., Van
            Poppel,H., Baert,L. and De Ley,M.
  TITLE     Metallothioneins in human kidneys and associated tumors
  JOURNAL   Nephron 83 (4), 331-340 (1999)
   PUBMED   10575295
REFERENCE   9  (residues 1 to 61)
  AUTHORS   Stennard,F.A., Holloway,A.F., Hamilton,J. and West,A.K.
  TITLE     Characterisation of six additional human metallothionein genes
  JOURNAL   Biochim Biophys Acta 1218 (3), 357-365 (1994)
   PUBMED   8049263
REFERENCE   10 (residues 1 to 61)
  AUTHORS   West,A.K., Stallings,R., Hildebrand,C.E., Chiu,R., Karin,M. and
            Richards,R.I.
  TITLE     Human metallothionein genes: structure of the functional locus at
            16q13
  JOURNAL   Genomics 8 (3), 513-518 (1990)
   PUBMED   2286373
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026461.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_789846.1.
            
            Summary: This gene encodes a member of the metallothionein
            superfamily, type 1 family. Metallothioneins have a high content of
            cysteine residues that bind various heavy metals. These genes are
            transcriptionally regulated by both heavy metals and
            glucocorticoids. [provided by RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM918307.1, AF136177.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379818.4/ ENSP00000369146.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..61
                     /product="metallothionein-1M"
                     /note="metallothionein 1K; metallothionein 1Y"
                     /calculated_mol_wt=5979
     Region          1..29
                     /region_name="Beta"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N339.2)"
     Region          4..61
                     /region_name="Metallothio"
                     /note="Metallothionein; pfam00131"
                     /db_xref="CDD:395080"
     Region          30..61
                     /region_name="Alpha"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N339.2)"
     CDS             1..61
                     /gene="MT1M"
                     /gene_synonym="MT-1M; MT-IM; MT1; MT1K"
                     /coded_by="NM_176870.3:74..259"
                     /db_xref="CCDS:CCDS42166.1"
                     /db_xref="GeneID:4499"
                     /db_xref="HGNC:HGNC:14296"
                     /db_xref="MIM:156357"
ORIGIN      
        1 mdpncscttg vscactgsct ckeckctsck ksccsccpvg cakcahgcvc kgtlencscc
       61 a
//
LOCUS       NP_005763                373 aa            linear   PRI 27-APR-2025
DEFINITION  RNA 3'-terminal phosphate cyclase-like protein isoform a [Homo
            sapiens].
ACCESSION   NP_005763
VERSION     NP_005763.3
DBSOURCE    REFSEQ: accession NM_005772.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Amin,N., de Vrij,F.M.S., Baghdadi,M., Brouwer,R.W.W., van
            Rooij,J.G.J., Jovanova,O., Uitterlinden,A.G., Hofman,A.,
            Janssen,H.L.A., Darwish Murad,S., Kraaij,R., Stedehouder,J., van
            den Hout,M.C.G.N., Kros,J.M., van IJcken,W.F.J., Tiemeier,H.,
            Kushner,S.A. and van Duijn,C.M.
  TITLE     A rare missense variant in RCL1 segregates with depression in
            extended families
  JOURNAL   Mol Psychiatry 23 (5), 1120-1126 (2018)
   PUBMED   28322274
  REMARK    GeneRIF: we identified a rare (minor allele frequency (MAF)=1%)
            missense c.1114C>T mutation (rs115482041) in the RCL1 gene
            segregating with depression across multiple generations.
            Rs115482041 showed significant association with depressive symptoms
            (N=2393, betaT-allele=2.33, P-value=1 x 10-4) and explained 2.9% of
            the estimated genetic variance of depressive symptoms
REFERENCE   6  (residues 1 to 373)
  AUTHORS   van der Harst,P., Zhang,W., Mateo Leach,I., Rendon,A., Verweij,N.,
            Sehmi,J., Paul,D.S., Elling,U., Allayee,H., Li,X.,
            Radhakrishnan,A., Tan,S.T., Voss,K., Weichenberger,C.X.,
            Albers,C.A., Al-Hussani,A., Asselbergs,F.W., Ciullo,M., Danjou,F.,
            Dina,C., Esko,T., Evans,D.M., Franke,L., Gogele,M., Hartiala,J.,
            Hersch,M., Holm,H., Hottenga,J.J., Kanoni,S., Kleber,M.E.,
            Lagou,V., Langenberg,C., Lopez,L.M., Lyytikainen,L.P., Melander,O.,
            Murgia,F., Nolte,I.M., O'Reilly,P.F., Padmanabhan,S., Parsa,A.,
            Pirastu,N., Porcu,E., Portas,L., Prokopenko,I., Ried,J.S.,
            Shin,S.Y., Tang,C.S., Teumer,A., Traglia,M., Ulivi,S., Westra,H.J.,
            Yang,J., Zhao,J.H., Anni,F., Abdellaoui,A., Attwood,A., Balkau,B.,
            Bandinelli,S., Bastardot,F., Benyamin,B., Boehm,B.O., Cookson,W.O.,
            Das,D., de Bakker,P.I., de Boer,R.A., de Geus,E.J., de Moor,M.H.,
            Dimitriou,M., Domingues,F.S., Doring,A., Engstrom,G.,
            Eyjolfsson,G.I., Ferrucci,L., Fischer,K., Galanello,R.,
            Garner,S.F., Genser,B., Gibson,Q.D., Girotto,G., Gudbjartsson,D.F.,
            Harris,S.E., Hartikainen,A.L., Hastie,C.E., Hedblad,B., Illig,T.,
            Jolley,J., Kahonen,M., Kema,I.P., Kemp,J.P., Liang,L.,
            Lloyd-Jones,H., Loos,R.J., Meacham,S., Medland,S.E., Meisinger,C.,
            Memari,Y., Mihailov,E., Miller,K., Moffatt,M.F., Nauck,M.,
            Novatchkova,M., Nutile,T., Olafsson,I., Onundarson,P.T.,
            Parracciani,D., Penninx,B.W., Perseu,L., Piga,A., Pistis,G.,
            Pouta,A., Puc,U., Raitakari,O., Ring,S.M., Robino,A., Ruggiero,D.,
            Ruokonen,A., Saint-Pierre,A., Sala,C., Salumets,A., Sambrook,J.,
            Schepers,H., Schmidt,C.O., Sillje,H.H., Sladek,R., Smit,J.H.,
            Starr,J.M., Stephens,J., Sulem,P., Tanaka,T., Thorsteinsdottir,U.,
            Tragante,V., van Gilst,W.H., van Pelt,L.J., van Veldhuisen,D.J.,
            Volker,U., Whitfield,J.B., Willemsen,G., Winkelmann,B.R.,
            Wirnsberger,G., Algra,A., Cucca,F., d'Adamo,A.P., Danesh,J.,
            Deary,I.J., Dominiczak,A.F., Elliott,P., Fortina,P., Froguel,P.,
            Gasparini,P., Greinacher,A., Hazen,S.L., Jarvelin,M.R., Khaw,K.T.,
            Lehtimaki,T., Maerz,W., Martin,N.G., Metspalu,A., Mitchell,B.D.,
            Montgomery,G.W., Moore,C., Navis,G., Pirastu,M., Pramstaller,P.P.,
            Ramirez-Solis,R., Schadt,E., Scott,J., Shuldiner,A.R., Smith,G.D.,
            Smith,J.G., Snieder,H., Sorice,R., Spector,T.D., Stefansson,K.,
            Stumvoll,M., Tang,W.H., Toniolo,D., Tonjes,A., Visscher,P.M.,
            Vollenweider,P., Wareham,N.J., Wolffenbuttel,B.H., Boomsma,D.I.,
            Beckmann,J.S., Dedoussis,G.V., Deloukas,P., Ferreira,M.A.,
            Sanna,S., Uda,M., Hicks,A.A., Penninger,J.M., Gieger,C.,
            Kooner,J.S., Ouwehand,W.H., Soranzo,N. and Chambers,J.C.
  TITLE     Seventy-five genetic loci influencing the human red blood cell
  JOURNAL   Nature 492 (7429), 369-375 (2012)
   PUBMED   23222517
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   8  (residues 1 to 373)
  AUTHORS   Billy,E., Wegierski,T., Nasr,F. and Filipowicz,W.
  TITLE     Rcl1p, the yeast protein similar to the RNA 3'-phosphate cyclase,
            associates with U3 snoRNP and is required for 18S rRNA biogenesis
  JOURNAL   EMBO J 19 (9), 2115-2126 (2000)
   PUBMED   10790377
REFERENCE   9  (residues 1 to 373)
  AUTHORS   Genschik,P., Billy,E., Swianiewicz,M. and Filipowicz,W.
  TITLE     The human RNA 3'-terminal phosphate cyclase is a member of a new
            family of proteins conserved in Eucarya, Bacteria and Archaea
  JOURNAL   EMBO J 16 (10), 2955-2967 (1997)
   PUBMED   9184239
REFERENCE   10 (residues 1 to 373)
  AUTHORS   Vicente,O. and Filipowicz,W.
  TITLE     Purification of RNA 3'-terminal phosphate cyclase from HeLa cells.
            Covalent modification of the enzyme with different nucleotides
  JOURNAL   Eur J Biochem 176 (2), 431-439 (1988)
   PUBMED   3416880
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC001025.2, AF067172.1, BI859171.1, AI688431.1 and CA422524.1.
            
            On Sep 22, 2007 this sequence version replaced NP_005763.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.95535.1, AK022904.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381750.9/ ENSP00000371169.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.1"
     Protein         1..373
                     /product="RNA 3'-terminal phosphate cyclase-like protein
                     isoform a"
                     /note="RNA cyclase homolog; RNA 3'-terminal phosphate
                     cyclase-like protein"
                     /calculated_mol_wt=40712
     Region          8..371
                     /region_name="18S_RNA_Rcl1p"
                     /note="18S rRNA biogenesis protein RCL1; TIGR03400"
                     /db_xref="CDD:274564"
     CDS             1..373
                     /gene="RCL1"
                     /gene_synonym="RNAC; RPCL1"
                     /coded_by="NM_005772.5:149..1270"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6456.1"
                     /db_xref="GeneID:10171"
                     /db_xref="HGNC:HGNC:17687"
                     /db_xref="MIM:611405"
ORIGIN      
        1 matqahslsy agcnflrqrl vlstlsgrpv kirkirardd npglrdfeas firlldkitn
       61 gsrieinqtg ttlyyqpgll yggsvehdcs vlrgigyyle sllclapfmk hplkivlrgv
      121 tndqvdpsvd vlkatalpll kqfgidgesf elkivrrgmp pggggevvfs cpvrkvlkpi
      181 qltdpgkikr irgmaysvrv spqmanrivd sarsilnkfi pdiyiytdhm kgvnsgkspg
      241 fglslvaett sgtflsaela snpqgqgaav lpedlgrnca rllleeiyrg gcvdstnqsl
      301 alllmtlgqq dvskvllgpl spytieflrh lksffqimfk ietkpcgeel kggdkvlmtc
      361 vgigfsnlsk tlk
//
LOCUS       NP_001124314             521 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 286A isoform 2 [Homo sapiens].
ACCESSION   NP_001124314
VERSION     NP_001124314.1
DBSOURCE    REFSEQ: accession NM_001130842.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Murakami,T., Sun,Z.S., Lee,C.C. and Lupski,J.R.
  TITLE     Isolation of novel genes from the CMT1A duplication/HNPP deletion
            critical region in 17p11.2-p12
  JOURNAL   Genomics 39 (1), 99-103 (1997)
   PUBMED   9027492
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK315062.1, AF217226.1, AC005324.1 and BU687070.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA193229.1, SRR1660803.69054.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000583566.6/ ENSP00000464063.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..521
                     /product="zinc finger protein 286A isoform 2"
                     /note="zinc finger protein ZNF286"
                     /calculated_mol_wt=60044
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBT8.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HBT8.1)"
     Region          45..98
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          91..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBT8.1)"
     Region          <222..357
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <352..507
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          356..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          384..404
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(389,391,393,395..396,399..400,403,417,419,423..424,
                     427..428,431,445,447,449,451..452,455..456,459)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          412..432
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          440..460
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          468..488
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          496..516
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..521
                     /gene="ZNF286A"
                     /gene_synonym="ZNF286"
                     /coded_by="NM_001130842.2:222..1787"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11172.1"
                     /db_xref="GeneID:57335"
                     /db_xref="HGNC:HGNC:13501"
ORIGIN      
        1 metdlaempe kgalssqdsp hfqeksteeg evaalrltar sqetvtfkdv amdftpeewg
       61 kldpaqrdvm lenyrnlvsl wlpvskpesy nlengkeplk lerkapkssy sdmetrpqsk
      121 dstsvqdfsk aesckvaiid rltrnsvyds nleaalecen wlenqqgnqe rhlremfthm
      181 nslseetdhk hdvywksfnq ksvlitedrv pkgsyafhtl ekslkqksnl mkkqrtykek
      241 kphkcndcge lftyhsvlir hqrvhtgekp ytcnecgksf shranltkhq rthtrilfec
      301 seckktftes sslathqrih vgerpyecne cgkgfnrsth lvqhqlihtg vkpyecnecd
      361 kafihssali khqrthtgek pykcqecgka fshcssltkh qrvhtgekpy ecsecgktfs
      421 qsthlvqhqr ihtgekpyec necgktfsrs snfakhqrih igkkpykcse cgkafihssa
      481 liqhqrthtg ekpfrcnecg ksfkcsssli rhqrvhteeq p
//
LOCUS       NP_001346989              79 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim10 B
            isoform g [Mus musculus].
ACCESSION   NP_001346989
VERSION     NP_001346989.1
DBSOURCE    REFSEQ: accession NM_001360060.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Kitamura,H., Nakagawa,T., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of FLJ
            genes: the complete nucleotide sequences of 110 mouse
            FLJ-homologous cDnas identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (2), 127-135 (2004)
   PUBMED   15449545
REFERENCE   4  (residues 1 to 79)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 79)
  AUTHORS   Bauer,M.F., Rothbauer,U., Muhlenbein,N., Smith,R.J., Gerbitz,K.,
            Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     The mitochondrial TIM22 preprotein translocase is highly conserved
            throughout the eukaryotic kingdom
  JOURNAL   FEBS Lett 464 (1-2), 41-47 (1999)
   PUBMED   10611480
REFERENCE   6  (residues 1 to 79)
  AUTHORS   Jin,H., Kendall,E., Freeman,T.C., Roberts,R.G. and Vetrie,D.L.
  TITLE     The human family of Deafness/Dystonia peptide (DDP) related
            mitochondrial import proteins
  JOURNAL   Genomics 61 (3), 259-267 (1999)
   PUBMED   10552927
REFERENCE   7  (residues 1 to 79)
  AUTHORS   Hadjiargyrou,M., Halsey,M.F., Ahrens,W., Rightmire,E.P.,
            McLeod,K.J. and Rubin,C.T.
  TITLE     Cloning of a novel cDNA expressed during the early stages of
            fracture healing
  JOURNAL   Biochem Biophys Res Commun 249 (3), 879-884 (1998)
   PUBMED   9731230
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125227.6 and AK003421.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK003421.1, BY703678.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849376
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 55.93 cM"
     Protein         1..79
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim10 B isoform g"
                     /note="small zinc finger-like protein; fractured callus 1;
                     mitochondrial import inner membrane translocase subunit
                     Tim9 B; Fracture Callus 1; fractured callus expressed
                     transcript 1; mitochondrial import inner membrane
                     translocase subunit Tim10 B"
                     /calculated_mol_wt=8723
     Region          <1..44
                     /region_name="zf-Tim10_DDP"
                     /note="Tim10/DDP family zinc finger; pfam02953"
                     /db_xref="CDD:460764"
     CDS             1..79
                     /gene="Timm10b"
                     /gene_synonym="Fxc1; Tim10b; Tim9b"
                     /coded_by="NM_001360060.1:262..501"
                     /note="isoform g is encoded by transcript variant 9"
                     /db_xref="GeneID:14356"
                     /db_xref="MGI:MGI:1315196"
ORIGIN      
        1 mtelcfqrcv pslhhralda eeeaclhsca gklihsnhrl maayvhlmpa lvqrriadye
       61 aasaapavkk ncceprgrr
//
LOCUS       NP_001353026             854 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 654 isoform 4 [Homo sapiens].
ACCESSION   NP_001353026
VERSION     NP_001353026.1
DBSOURCE    REFSEQ: accession NM_001366097.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Perry,J.R., Day,F., Elks,C.E., Sulem,P., Thompson,D.J.,
            Ferreira,T., He,C., Chasman,D.I., Esko,T., Thorleifsson,G.,
            Albrecht,E., Ang,W.Q., Corre,T., Cousminer,D.L., Feenstra,B.,
            Franceschini,N., Ganna,A., Johnson,A.D., Kjellqvist,S.,
            Lunetta,K.L., McMahon,G., Nolte,I.M., Paternoster,L., Porcu,E.,
            Smith,A.V., Stolk,L., Teumer,A., Tsernikova,N., Tikkanen,E.,
            Ulivi,S., Wagner,E.K., Amin,N., Bierut,L.J., Byrne,E.M.,
            Hottenga,J.J., Koller,D.L., Mangino,M., Pers,T.H.,
            Yerges-Armstrong,L.M., Zhao,J.H., Andrulis,I.L., Anton-Culver,H.,
            Atsma,F., Bandinelli,S., Beckmann,M.W., Benitez,J., Blomqvist,C.,
            Bojesen,S.E., Bolla,M.K., Bonanni,B., Brauch,H., Brenner,H.,
            Buring,J.E., Chang-Claude,J., Chanock,S., Chen,J.,
            Chenevix-Trench,G., Collee,J.M., Couch,F.J., Couper,D.,
            Coveillo,A.D., Cox,A., Czene,K., D'adamo,A.P., Smith,G.D., De
            Vivo,I., Demerath,E.W., Dennis,J., Devilee,P., Dieffenbach,A.K.,
            Dunning,A.M., Eiriksdottir,G., Eriksson,J.G., Fasching,P.A.,
            Ferrucci,L., Flesch-Janys,D., Flyger,H., Foroud,T., Franke,L.,
            Garcia,M.E., Garcia-Closas,M., Geller,F., de Geus,E.E., Giles,G.G.,
            Gudbjartsson,D.F., Gudnason,V., Guenel,P., Guo,S., Hall,P.,
            Hamann,U., Haring,R., Hartman,C.A., Heath,A.C., Hofman,A.,
            Hooning,M.J., Hopper,J.L., Hu,F.B., Hunter,D.J., Karasik,D.,
            Kiel,D.P., Knight,J.A., Kosma,V.M., Kutalik,Z., Lai,S.,
            Lambrechts,D., Lindblom,A., Magi,R., Magnusson,P.K., Mannermaa,A.,
            Martin,N.G., Masson,G., McArdle,P.F., McArdle,W.L., Melbye,M.,
            Michailidou,K., Mihailov,E., Milani,L., Milne,R.L., Nevanlinna,H.,
            Neven,P., Nohr,E.A., Oldehinkel,A.J., Oostra,B.A., Palotie,A.,
            Peacock,M., Pedersen,N.L., Peterlongo,P., Peto,J., Pharoah,P.D.,
            Postma,D.S., Pouta,A., Pylkas,K., Radice,P., Ring,S.,
            Rivadeneira,F., Robino,A., Rose,L.M., Rudolph,A., Salomaa,V.,
            Sanna,S., Schlessinger,D., Schmidt,M.K., Southey,M.C., Sovio,U.,
            Stampfer,M.J., Stockl,D., Storniolo,A.M., Timpson,N.J., Tyrer,J.,
            Visser,J.A., Vollenweider,P., Volzke,H., Waeber,G.,
            Waldenberger,M., Wallaschofski,H., Wang,Q., Willemsen,G.,
            Winqvist,R., Wolffenbuttel,B.H., Wright,M.J., Boomsma,D.I.,
            Econs,M.J., Khaw,K.T., Loos,R.J., McCarthy,M.I., Montgomery,G.W.,
            Rice,J.P., Streeten,E.A., Thorsteinsdottir,U., van Duijn,C.M.,
            Alizadeh,B.Z., Bergmann,S., Boerwinkle,E., Boyd,H.A., Crisponi,L.,
            Gasparini,P., Gieger,C., Harris,T.B., Ingelsson,E., Jarvelin,M.R.,
            Kraft,P., Lawlor,D., Metspalu,A., Pennell,C.E., Ridker,P.M.,
            Snieder,H., Sorensen,T.I., Spector,T.D., Strachan,D.P.,
            Uitterlinden,A.G., Wareham,N.J., Widen,E., Zygmunt,M., Murray,A.,
            Easton,D.F., Stefansson,K., Murabito,J.M. and Ong,K.K.
  CONSRTM   Australian Ovarian Cancer Study; GENICA Network; kConFab; LifeLines
            Cohort Study; InterAct Consortium; Early Growth Genetics (EGG)
            Consortium
  TITLE     Parent-of-origin-specific allelic associations among 106 genomic
            loci for age at menarche
  JOURNAL   Nature 514 (7520), 92-97 (2014)
   PUBMED   25231870
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC119733.2 and AC128650.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.237729.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p11.1"
     Protein         1..854
                     /product="zinc finger protein 654 isoform 4"
                     /note="melanoma-associated antigen"
                     /calculated_mol_wt=97138
     Region          273..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(278,280,281,283..284,287..288,291,305,307..309,
                     311..312,316,319)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          515..535
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(520,522,524,526..527,530..531,534,550,552,556..557,
                     560..561,564,579,581,583,585..586,589..590,593)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          543..565
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          572..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..854
                     /gene="ZNF654"
                     /coded_by="NM_001366097.1:719..3283"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="GeneID:55279"
                     /db_xref="HGNC:HGNC:25612"
ORIGIN      
        1 mlalqlcesf lipqlqngdm yciwelifiw sklqlksnps kqvfvdqcyq llrtatnvrv
       61 ifpfmkiikd eveeeglqic veicgcalql dlhddpktkc liyktiahfl pndleilric
      121 alsifflers leayrtveel ykrpdeeyne gtssvqnrvr fellpilkkg lffdpefwnf
      181 vmikkncval lsdksavrfl nestlennag nlkrteeqqg ldegfdsltd qstgetdpdd
      241 vsgvqpkghi ntkknltals tskvdhnvpr hrcmlcnkef lgghivrhaq ahqkkgsfac
      301 vicgrkfrnr glmqkhlknh vkkiqrqqia aaqqddqevt aleeincsss sisfengnsd
      361 skdlevetlt assegnkevi pehvaefiei pisvpedvie nviengspnn slnnvfkplt
      421 ecgddyeeee deegdyeedd ydlnqetsvi hkingtvchp kdiyatdqeg nfkcpalgcv
      481 rifkrigfln khamtvhptd lnvrqtvmkw skgkckfcqr qfedsqhfid hlnrhsypnv
      541 yfclhfncne sfklpfqlaq htkshrifqa qcsfpechel fedlpllyeh eaqhylsktp
      601 essaqpseti lwdvqtdsnp nqekdsssne kqtislpvst sksrkestep ktciesmekk
      661 tdslvqngne rsddtvsnis lidqkmpdie pnsenncsss divnghseie qtplvssdpa
      721 lkidtnrirt engsilpsvv pqehntlpvs qapskpnlts ehtsyglilt kpyvrplpps
      781 ylderylsmp krrkfltdrv dacsdqdnvy kksvkrlrcg kclttycnae aleahlaqkk
      841 cqtlfgfdsd desa
//
LOCUS       NP_000785                446 aa            linear   PRI 27-APR-2025
DEFINITION  D(1A) dopamine receptor [Homo sapiens].
ACCESSION   NP_000785
VERSION     NP_000785.1
DBSOURCE    REFSEQ: accession NM_000794.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Grant,C.E., Flis,A.L., Toulabi,L., Zingone,A., Rossi,E., Aploks,K.,
            Sheppard,H. and Ryan,B.M.
  TITLE     DRD1 suppresses cell proliferation and reduces EGFR activation and
            PD-L1 expression in NSCLC
  JOURNAL   Mol Oncol 18 (6), 1631-1648 (2024)
   PUBMED   38572507
  REMARK    GeneRIF: DRD1 suppresses cell proliferation and reduces EGFR
            activation and PD-L1 expression in NSCLC.
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Pedersen,R., Johansson,J., Nordin,K., Rieckmann,A., Wahlin,A.,
            Nyberg,L., Backman,L. and Salami,A.
  TITLE     Dopamine D1-Receptor Organization Contributes to Functional Brain
            Architecture
  JOURNAL   J Neurosci 44 (11), e0621232024 (2024)
   PUBMED   38302439
  REMARK    GeneRIF: Dopamine D1-Receptor Organization Contributes to
            Functional Brain Architecture.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Gao,A.Y., Diaz Espinosa,A.M., Nguyen,B.B.N., Link,P.A., Meridew,J.,
            Jones,D.L., Gibbard,D.F., Tschumperlin,D.J. and Haak,A.J.
  TITLE     Dopamine Receptor D1 Is Exempt from Transforming Growth Factor
            beta-Mediated Antifibrotic G Protein-Coupled Receptor Landscape
            Tampering in Lung Fibroblasts
  JOURNAL   J Pharmacol Exp Ther 386 (3), 277-287 (2023)
   PUBMED   37024146
  REMARK    GeneRIF: Dopamine Receptor D1 Is Exempt from Transforming Growth
            Factor beta-Mediated Antifibrotic G Protein-Coupled Receptor
            Landscape Tampering in Lung Fibroblasts.
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Andreska,T., Luningschror,P., Wolf,D., McFleder,R.L.,
            Ayon-Olivas,M., Rattka,M., Drechsler,C., Perschin,V., Blum,R.,
            Aufmkolk,S., Granado,N., Moratalla,R., Sauer,M., Monoranu,C.,
            Volkmann,J., Ip,C.W., Stigloher,C. and Sendtner,M.
  TITLE     DRD1 signaling modulates TrkB turnover and BDNF sensitivity in
            direct pathway striatal medium spiny neurons
  JOURNAL   Cell Rep 42 (6), 112575 (2023)
   PUBMED   37252844
  REMARK    GeneRIF: DRD1 signaling modulates TrkB turnover and BDNF
            sensitivity in direct pathway striatal medium spiny neurons.
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Zhao,Y., Li,Y., Li,H. and Shi,S.
  TITLE     Dopamine D1 receptor activation ameliorates ox-LDL-induced
            endothelial cell senescence via CREB/Nrf2 pathway
  JOURNAL   Exp Cell Res 425 (2), 113542 (2023)
   PUBMED   36894051
  REMARK    GeneRIF: Dopamine D1 receptor activation ameliorates ox-LDL-induced
            endothelial cell senescence via CREB/Nrf2 pathway.
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Liu,Y.F., Civelli,O., Zhou,Q.Y. and Albert,P.R.
  TITLE     Cholera toxin-sensitive 3',5'-cyclic adenosine monophosphate and
            calcium signals of the human dopamine-D1 receptor: selective
            potentiation by protein kinase A
  JOURNAL   Mol Endocrinol 6 (11), 1815-1824 (1992)
   PUBMED   1282671
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Minowa,M.T., Minowa,T., Monsma,F.J. Jr., Sibley,D.R. and
            Mouradian,M.M.
  TITLE     Characterization of the 5' flanking region of the human D1A
            dopamine receptor gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3045-3049 (1992)
   PUBMED   1557411
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1992 May 1;89(9):4220]
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Tiberi,M., Jarvie,K.R., Silvia,C., Falardeau,P., Gingrich,J.A.,
            Godinot,N., Bertrand,L., Yang-Feng,T.L., Fremeau,R.T. Jr. and
            Caron,M.G.
  TITLE     Cloning, molecular characterization, and chromosomal assignment of
            a gene encoding a second D1 dopamine receptor subtype: differential
            expression pattern in rat brain compared with the D1A receptor
  JOURNAL   Proc Natl Acad Sci U S A 88 (17), 7491-7495 (1991)
   PUBMED   1831904
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Grandy,D.K., Zhou,Q.Y., Allen,L., Litt,R., Magenis,R.E., Civelli,O.
            and Litt,M.
  TITLE     A human D1 dopamine receptor gene is located on chromosome 5 at
            q35.1 and identifies an EcoRI RFLP
  JOURNAL   Am J Hum Genet 47 (5), 828-834 (1990)
   PUBMED   1977312
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Sunahara,R.K., Niznik,H.B., Weiner,D.M., Stormann,T.M., Brann,M.R.,
            Kennedy,J.L., Gelernter,J.E., Rozmahel,R., Yang,Y.L., Israel,Y. et
            al.
  TITLE     Human dopamine D1 receptor encoded by an intronless gene on
            chromosome 5
  JOURNAL   Nature 347 (6288), 80-83 (1990)
   PUBMED   1975640
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091393.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the D1 subtype of the dopamine receptor.
            The D1 subtype is the most abundant dopamine receptor in the
            central nervous system. This G-protein coupled receptor stimulates
            adenylyl cyclase and activates cyclic AMP-dependent protein
            kinases. D1 receptors regulate neuronal growth and development,
            mediate some behavioral responses, and modulate dopamine receptor
            D2-mediated events. Alternate transcription initiation sites result
            in two transcript variants of this gene. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA249160.1, SRR1803611.17628.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393752.3/ ENSP00000377353.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..446
                     /product="D(1A) dopamine receptor"
                     /note="dopamine D1 receptor"
                     /calculated_mol_wt=49162
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21728.1)"
     Region          23..341
                     /region_name="7tmA_D1A_dopamine_R"
                     /note="D1A (or D1) subtype dopamine receptor, member of
                     the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15320"
                     /db_xref="CDD:320443"
     Site            24..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21728.1)"
     Region          25..51
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320443"
     Region          59..86
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320443"
     Site            61..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21728.1)"
     Region          96..126
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320443"
     Site            97..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21728.1)"
     Site            order(99,103..104,107..108,188,195,198..199,202,285,
                     288..289,292,313,317,321)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320443"
     Region          138..161
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320443"
     Site            139..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21728.1)"
     Region          191..221
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320443"
     Site            193..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21728.1)"
     Region          265..295
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320443"
     Site            273..299
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21728.1)"
     Region          310..335
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320443"
     Site            313..337
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21728.1)"
     CDS             1..446
                     /gene="DRD1"
                     /gene_synonym="D1R; DADR; DRD1A"
                     /coded_by="NM_000794.5:968..2308"
                     /db_xref="CCDS:CCDS4393.1"
                     /db_xref="GeneID:1812"
                     /db_xref="HGNC:HGNC:3020"
                     /db_xref="MIM:126449"
ORIGIN      
        1 mrtlntsamd gtglvverdf svriltacfl sllilstllg ntlvcaavir frhlrskvtn
       61 ffvislavsd llvavlvmpw kavaeiagfw pfgsfcniwv afdimcstas ilnlcvisvd
      121 rywaisspfr yerkmtpkaa filisvawtl svlisfipvq lswhkakpts psdgnatsla
      181 etidncdssl srtyaisssv isfyipvaim ivtytriyri aqkqirriaa leraavhakn
      241 cqtttgngkp vecsqpessf kmsfkretkv lktlsvimgv fvccwlpffi lncilpfcgs
      301 getqpfcids ntfdvfvwfg wansslnpii yafnadfrka fstllgcyrl cpatnnaiet
      361 vsinnngaam fsshheprgs iskecnlvyl iphavgssed lkkeeaagia rpleklspal
      421 svildydtdv slekiqpitq ngqhpt
//
LOCUS       NP_031374                670 aa            linear   PRI 27-APR-2025
DEFINITION  cyclic AMP-dependent transcription factor ATF-6 alpha isoform 1
            [Homo sapiens].
ACCESSION   NP_031374
VERSION     NP_031374.2
DBSOURCE    REFSEQ: accession NM_007348.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Klyosova,E., Azarova,I., Petrukhina,I., Khabibulin,R. and
            Polonikov,A.
  TITLE     The rs2341471-G/G genotype of activating transcription factor 6
            (ATF6) is the risk factor of type 2 diabetes in subjects with
            obesity or overweight
  JOURNAL   Int J Obes (Lond) 48 (11), 1638-1649 (2024)
   PUBMED   39134692
  REMARK    GeneRIF: The rs2341471-G/G genotype of activating transcription
            factor 6 (ATF6) is the risk factor of type 2 diabetes in subjects
            with obesity or overweight.
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Mori,K.
  TITLE     Divest yourself of a preconceived idea: transcription factor ATF6
            is not a soluble protein!
  JOURNAL   Mol Biol Cell 21 (9), 1435-1438 (2010)
   PUBMED   20219975
  REMARK    GeneRIF: Studies show that ATF6, rather than being a soluble
            nuclear protein, was an active transcription factor and synthesized
            as a transmembrane protein embedded in the ER.
REFERENCE   3  (residues 1 to 670)
  AUTHORS   Meex,S.J., Weissglas-Volkov,D., van der Kallen,C.J., Thuerauf,D.J.,
            van Greevenbroek,M.M., Schalkwijk,C.G., Stehouwer,C.D.,
            Feskens,E.J., Heldens,L., Ayoubi,T.A., Hofker,M.H., Wouters,B.G.,
            Vlietinck,R., Sinsheimer,J.S., Taskinen,M.R., Kuusisto,J.,
            Laakso,M., de Bruin,T.W., Pajukanta,P. and Glembotski,C.C.
  TITLE     The ATF6-Met[67]Val substitution is associated with increased
            plasma cholesterol levels
  JOURNAL   Arterioscler Thromb Vasc Biol 29 (9), 1322-1327 (2009)
   PUBMED   19667116
  REMARK    GeneRIF: The ATF6-Met[67]Val substitution is associated with
            increased plasma cholesterol levels.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Schewe,D.M. and Aguirre-Ghiso,J.A.
  TITLE     ATF6alpha-Rheb-mTOR signaling promotes survival of dormant tumor
            cells in vivo
  JOURNAL   Proc Natl Acad Sci U S A 105 (30), 10519-10524 (2008)
   PUBMED   18650380
  REMARK    GeneRIF: ATF6alpha-Rheb-mTOR signaling promotes survival of dormant
            tumor cells in vivo
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Kerbiriou,M., Le Drevo,M.A., Ferec,C. and Trouve,P.
  TITLE     Coupling cystic fibrosis to endoplasmic reticulum stress:
            Differential role of Grp78 and ATF6
  JOURNAL   Biochim Biophys Acta 1772 (11-12), 1236-1249 (2007)
   PUBMED   18022401
  REMARK    GeneRIF: The aim was to study the activation of ATF6 and Grp78 in
            transfected human epithelial cells expressing the DeltaF508-CFTR
            protein.
REFERENCE   6  (residues 1 to 670)
  AUTHORS   Haze,K., Yoshida,H., Yanagi,H., Yura,T. and Mori,K.
  TITLE     Mammalian transcription factor ATF6 is synthesized as a
            transmembrane protein and activated by proteolysis in response to
            endoplasmic reticulum stress
  JOURNAL   Mol Biol Cell 10 (11), 3787-3799 (1999)
   PUBMED   10564271
REFERENCE   7  (residues 1 to 670)
  AUTHORS   Yoshida,H., Haze,K., Yanagi,H., Yura,T. and Mori,K.
  TITLE     Identification of the cis-acting endoplasmic reticulum stress
            response element responsible for transcriptional induction of
            mammalian glucose-regulated proteins. Involvement of basic leucine
            zipper transcription factors
  JOURNAL   J Biol Chem 273 (50), 33741-33749 (1998)
   PUBMED   9837962
  REMARK    Erratum:[J Biol Chem 1999 Jan 22;274(4):2592]
REFERENCE   8  (residues 1 to 670)
  AUTHORS   Zhu,C., Johansen,F.E. and Prywes,R.
  TITLE     Interaction of ATF6 and serum response factor
  JOURNAL   Mol Cell Biol 17 (9), 4957-4966 (1997)
   PUBMED   9271374
REFERENCE   9  (residues 1 to 670)
  AUTHORS   Kohl,S., Jagle,H., Wissinger,B. and Zobor,D.
  TITLE     Achromatopsia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301591
REFERENCE   10 (residues 1 to 670)
  AUTHORS   Hai,T.W., Liu,F., Coukos,W.J. and Green,M.R.
  TITLE     Transcription factor ATF cDNA clones: an extensive family of
            leucine zipper proteins able to selectively form DNA-binding
            heterodimers
  JOURNAL   Genes Dev 3 (12B), 2083-2090 (1989)
   PUBMED   2516827
  REMARK    Erratum:[Genes Dev 1990 Apr;4(4):682]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP380917.1, BC014969.1,
            AK290498.1, AB015856.1, AL391825.15 and BM683233.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 22, 2004 this sequence version replaced NP_031374.1.
            
            Summary: This gene encodes a transcription factor that activates
            target genes for the unfolded protein response (UPR) during
            endoplasmic reticulum (ER) stress. Although it is a transcription
            factor, this protein is unusual in that it is synthesized as a
            transmembrane protein that is embedded in the ER. It functions as
            an ER stress sensor/transducer, and following ER stress-induced
            proteolysis, it functions as a nuclear transcription factor via a
            cis-acting ER stress response element (ERSE) that is present in the
            promoters of genes encoding ER chaperones. This protein has been
            identified as a survival factor for quiescent but not proliferative
            squamous carcinoma cells. There have been conflicting reports about
            the association of polymorphisms in this gene with diabetes in
            different populations, but another polymorphism has been associated
            with increased plasma cholesterol levels. This gene is also thought
            to be a potential therapeutic target for cystic fibrosis. [provided
            by RefSeq, Aug 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290498.1, SRR14038194.1191928.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367942.4/ ENSP00000356919.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..670
                     /product="cyclic AMP-dependent transcription factor ATF-6
                     alpha isoform 1"
                     /note="cyclic AMP-dependent transcription factor ATF-6
                     alpha; cAMP-dependent transcription factor ATF-6 alpha"
                     /calculated_mol_wt=74454
     Region          1..150
                     /region_name="Transcription activation.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P18850.3)"
     Region          91..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18850.3)"
     Region          308..339
                     /region_name="Basic motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P18850.3)"
     Region          309..360
                     /region_name="bZIP_ATF6"
                     /note="Basic leucine zipper (bZIP) domain of Activating
                     Transcription Factor-6 (ATF-6) and similar proteins: a
                     DNA-binding and dimerization domain; cd14700"
                     /db_xref="CDD:269848"
     Region          309..360
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269848"
     Site            order(312..313,315..317,319..324,326..328)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269848"
     Site            order(327,330..331,334..335,337..338,341..342,344..345,
                     348..349,351..352,355..356,358..359)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269848"
     Region          348..355
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P18850.3)"
     Site            378..398
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18850.3)"
     Site            419..420
                     /site_type="cleavage"
                     /note="Cleavage, by MBTPS1.
                     /evidence=ECO:0000305|PubMed:11163209; propagated from
                     UniProtKB/Swiss-Prot (P18850.3)"
     Region          468..589
                     /region_name="Interaction with THBS4.
                     /evidence=ECO:0000269|PubMed:22682248"
                     /note="propagated from UniProtKB/Swiss-Prot (P18850.3)"
     Site            472
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14699159; propagated from
                     UniProtKB/Swiss-Prot (P18850.3)"
     Site            584
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14699159; propagated from
                     UniProtKB/Swiss-Prot (P18850.3)"
     Site            643
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14699159; propagated from
                     UniProtKB/Swiss-Prot (P18850.3)"
     CDS             1..670
                     /gene="ATF6"
                     /gene_synonym="ACHM7; ATF6A; ATP6alpha"
                     /coded_by="NM_007348.4:42..2054"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1235.1"
                     /db_xref="GeneID:22926"
                     /db_xref="HGNC:HGNC:791"
                     /db_xref="MIM:605537"
ORIGIN      
        1 mgepagvagt mespfspglf hrldedwdsa lfaelgyftd tdelqleaan etyennfdnl
       61 dfdldlmpwe sdiwdinnqi ctvkdikaep qplspasssy svssprsvds ysstqhvpee
      121 ldlssssqms plslygensn slssaeplke dkpvtgprnk tengltpkkk iqvnskpsiq
      181 pkplllpaap ktqtnssvpa ktiiiqtvpt lmplakqqpi islqpaptkg qtvllsqptv
      241 vqlqapgvlp saqpvlavag gvtqlpnhvv nvvpapsans pvngklsvtk pvlqstmrnv
      301 gsdiavlrrq qrmiknresa cqsrkkkkey mlglearlka alseneqlkk engtlkrqld
      361 evvsenqrlk vpspkrrvvc vmivlafiil nygpmsmleq dsrrmnpsvs panqrrhllg
      421 fsakeaqdts dgiiqknsyr ydhsvsndka lmvlteepll yippppcqpl intteslrln
      481 helrgwvhrh evertksrrm tnnqqktril qgaleqgsns qlmavqytet tssisrnsgs
      541 elqvyyaspr syqdffeair rrgdtfyvvs frrdhlllpa tthnkttrpk msivlpaini
      601 nenvingqdy evmmqidcqv mdtrilhiks ssvppylrdq qrnqtntffg sppaateath
      661 vvstipeslq
//
LOCUS       NP_115655               1196 aa            linear   PRI 27-APR-2025
DEFINITION  probable cation-transporting ATPase 13A4 [Homo sapiens].
ACCESSION   NP_115655 XP_039929
VERSION     NP_115655.2
DBSOURCE    REFSEQ: accession NM_032279.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   van Veen,S., Kourti,A., Ausloos,E., Van Asselberghs,J., Van den
            Haute,C., Baekelandt,V., Eggermont,J. and Vangheluwe,P.
  TITLE     ATP13A4 Upregulation Drives the Elevated Polyamine Transport System
            in the Breast Cancer Cell Line MCF7
  JOURNAL   Biomolecules 13 (6), 918 (2023)
   PUBMED   37371498
  REMARK    GeneRIF: ATP13A4 Upregulation Drives the Elevated Polyamine
            Transport System in the Breast Cancer Cell Line MCF7.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Gibbons,A.S., Bell,L.M., Udawela,M. and Dean,B.
  TITLE     mRNA expression of the P5 ATPase ATP13A4 is increased in Broca's
            area from subjects with schizophrenia
  JOURNAL   World J Biol Psychiatry 21 (5), 402-408 (2020)
   PUBMED   30501451
  REMARK    GeneRIF: mRNA expression of the P5 ATPase ATP13A4 is increased in
            Broca's area from subjects with schizophrenia.
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Kwasnicka-Crawford,D.A., Carson,A.R., Roberts,W., Summers,A.M.,
            Rehnstrom,K., Jarvela,I. and Scherer,S.W.
  TITLE     Characterization of a novel cation transporter ATPase gene
            (ATP13A4) interrupted by 3q25-q29 inversion in an individual with
            language delay
  JOURNAL   Genomics 86 (2), 182-194 (2005)
   PUBMED   15925480
  REMARK    GeneRIF: ATP13A4 is a novel gene coding for a cation-transporting
            P-type ATPase and is interrupted by 3q25-q29 inversion in an
            individual with language delay
REFERENCE   4  (residues 1 to 1196)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA117883.1, AY823162.1, BC101496.1, AK096510.1, AY358110.1 and
            AC105057.7.
            
            On Jun 3, 2005 this sequence version replaced NP_115655.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY823162.1, SRR11853560.21566.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342695.9/ ENSP00000339182.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..1196
                     /product="probable cation-transporting ATPase 13A4"
                     /EC_number="3.6.3.-"
                     /note="cation-transporting P5-ATPase; ATPase type 13A4"
                     /calculated_mol_wt=133856
     Region          16..141
                     /region_name="P5-ATPase"
                     /note="P5-type ATPase cation transporter; pfam12409"
                     /db_xref="CDD:463565"
     Region          173..1015
                     /region_name="P-type_ATPase_cation"
                     /note="P-type cation-transporting ATPases, similar to
                     human ATPase type 13A2 (ATP13A2) protein and Saccharomyces
                     cerevisiae Ypk9p; cd07542"
                     /db_xref="CDD:319842"
     Site            198..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VNC1.3)"
     Site            224..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VNC1.3)"
     Site            401..421
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VNC1.3)"
     Site            437..457
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VNC1.3)"
     Site            order(486..488,601,624..626,658,717..719,823,826,829,848,
                     851)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319842"
     Site            901..921
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VNC1.3)"
     Site            order(905,909..910,912..913,929,932..933)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319842"
     Site            933..953
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VNC1.3)"
     Site            973..993
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VNC1.3)"
     Site            1036..1056
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VNC1.3)"
     Site            1071..1091
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VNC1.3)"
     Site            1110..1130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VNC1.3)"
     CDS             1..1196
                     /gene="ATP13A4"
                     /coded_by="NM_032279.4:97..3687"
                     /db_xref="CCDS:CCDS3304.2"
                     /db_xref="GeneID:84239"
                     /db_xref="HGNC:HGNC:25422"
                     /db_xref="MIM:609556"
ORIGIN      
        1 mghfekgqha llnegeenem eifgyrtqgc rkslclagsi fsfgilplvf ywrpawhvwa
       61 hcvpcslqea dtvllrttde fqiyswkkvi wiylsalnsa fgltpdhplm tdeeyiinra
      121 irkpdlkvrc ikvqkiryvw nylegqfqki gsledwlssa kihqkfgsgl treeqeirrl
      181 icgpntidve vtpiwkllik evlnpfyifq lfsvclwfse dykeyafaii imsiisislt
      241 vydlreqsvk lhhlveshns itvsvcgrka gvqelesrvl vpgdlliltg nkvlmpcdav
      301 liegscvvde gmltgesipv tktplpkmds svpwktqsea dykrhvlfcg teviqakaac
      361 sgtvravvlq tgfntakgdl vrsilypkpv nfqlyrdair fllclvgtat igmiytlcvy
      421 vlsgeppeev vrkaldviti avppalpaal ttgiiyaqrr lkkrgifcis pqrinvcgql
      481 nlvcfdktgt ltrdgldlwg vvscdrngfq evhsfasgqa lpwgplcaam aschslilld
      541 gtiqgdpldl kmfeattwem afsgddfhik gvpahamvvk pcrtasqvpv egiailhqfp
      601 fssalqrmtv ivqemggdrl afmkgaperv asfcqpetvp tsfvselqiy ttqgfrvial
      661 aykklendhh attltretve sdliflglli lenrlkeetk pvleelisar irtvmitgdn
      721 lqtaitvark sgmvsesqkv ilieanettg sssasiswtl veekkhimyg nqdnyinird
      781 evsdkgregs yhfaltgksf hvisqhfssl lpkilingti farmspgqks slveefqkld
      841 yfvgmcgdga ndcgalkmah vgislseqea svaspftskt pniecvphli kegraalvts
      901 fcmfkymaly smiqyvgvll lywetnslsn yqflfqdlai ttligvtmnl ngaypklvpf
      961 rpagrlispp lllsvifnil lslamhiagf ilvqrqpwys veihsactvq nesiseltms
     1021 ptapekmesn stftsfentt vwflgtinci tvalvfskgk pfrqptytny ifvlvliiql
     1081 gvclfilfad ipelyrrldl lctpvlwras ivimlslnfi vslvaeeavi enralwmmik
     1141 rcfgyqsksq yriwqrdlan dpswpplnqt shsdmpecgr gvsysnpvfe sneeql
//
LOCUS       NP_001036100             315 aa            linear   PRI 27-APR-2025
DEFINITION  neuroguidin isoform 1 [Homo sapiens].
ACCESSION   NP_001036100
VERSION     NP_001036100.1
DBSOURCE    REFSEQ: accession NM_001042635.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Scaturro,P., Stukalov,A., Haas,D.A., Cortese,M., Draganova,K.,
            Plaszczyca,A., Bartenschlager,R., Gotz,M. and Pichlmair,A.
  TITLE     An orthogonal proteomic survey uncovers novel Zika virus host
            factors
  JOURNAL   Nature 561 (7722), 253-257 (2018)
   PUBMED   30177828
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Sihn,C.R., Lee,Y.S., Jeong,J.S., Park,K. and Kim,S.H.
  TITLE     CANu1, a novel nucleolar protein, accumulated on centromere in
            response to DNA damage
  JOURNAL   Genes Cells 13 (8), 787-796 (2008)
   PUBMED   18547334
  REMARK    GeneRIF: Study isolated a novel human gene, to be called as CANu1,
            by the large-scale genome-wide association analysis to screen
            specific Single nucleotide polymorphisms in colon cancer.
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Jung,M.Y., Lorenz,L. and Richter,J.D.
  TITLE     Translational control by neuroguidin, a eukaryotic initiation
            factor 4E and CPEB binding protein
  JOURNAL   Mol Cell Biol 26 (11), 4277-4287 (2006)
   PUBMED   16705177
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC030817.1 and AL132855.4.
            
            Summary: Neuroguidin is an EIF4E (MIM 133440)-binding protein that
            interacts with CPEB (MIM 607342) and functions as a translational
            regulatory protein during development of the vertebrate nervous
            system (Jung et al., 2006 [PubMed 16705177]).[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030817.1, SRR5189667.18874.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000408901.8/ ENSP00000386134.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..315
                     /product="neuroguidin isoform 1"
                     /note="eukaryotic initiation factor 4E and CPEB binding
                     protein; EIF4E-binding protein; centromere accumulated
                     nuclear protein 1; neuroguidin, EIF4E binding protein"
                     /calculated_mol_wt=35763
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8NEJ9.1)"
     Region          18..98
                     /region_name="Sas10_Utp3"
                     /note="Sas10/Utp3/C1D family; pfam04000"
                     /db_xref="CDD:461123"
     Region          41..174
                     /region_name="Necessary for interaction with EIF4E.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEJ9.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEJ9.1)"
     Region          124..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEJ9.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEJ9.1)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEJ9.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEJ9.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEJ9.1)"
     Region          277..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEJ9.1)"
     CDS             1..315
                     /gene="NGDN"
                     /gene_synonym="C14orf120; CANu1; LCP5; lpd-2; NGD"
                     /coded_by="NM_001042635.2:14..961"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41926.1"
                     /db_xref="GeneID:25983"
                     /db_xref="HGNC:HGNC:20271"
                     /db_xref="MIM:610777"
ORIGIN      
        1 maalgvlesd lpsavtllkn lqeqvmavta qvksltqkvq agayptekgl sflevkdqll
       61 lmylmdlthl ildkasggsl qghdavlrlv eirtvleklr pldqklkyqi dkliktavtg
      121 slsendplrf kphpsnmmsk lssedeeede aeddqseasg kksvkgvskk yvpprlvpvh
      181 ydeteaerek krlerakrra lsssvirelk eqysdapeei rdarhphvtr qsqedqhrin
      241 yeesmmvrls vskrekgrrk ranvmssqlh slthfsdisa ltggtvhlde dqnpikkrkk
      301 ipqkgrkkkg frrrr
//
LOCUS       NP_079229                972 aa            linear   PRI 27-APR-2025
DEFINITION  N-alpha-acetyltransferase 25, NatB auxiliary subunit [Homo
            sapiens].
ACCESSION   NP_079229
VERSION     NP_079229.2
DBSOURCE    REFSEQ: accession NM_024953.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Morrison,J., Altuwaijri,N.K., Bronstad,K., Aksnes,H., Alsaif,H.S.,
            Evans,A., Hashem,M., Wheeler,P.G., Webb,B.D., Alkuraya,F.S. and
            Arnesen,T.
  TITLE     Missense NAA20 variants impairing the NatB protein N-terminal
            acetyltransferase cause autosomal recessive developmental delay,
            intellectual disability, and microcephaly
  JOURNAL   Genet Med 23 (11), 2213-2218 (2021)
   PUBMED   34230638
REFERENCE   2  (residues 1 to 972)
  AUTHORS   Xu,J.K., Li,G.Z., Li,Z., Li,W.J., Chen,R.S., Zhang,B. and
            Zhang,X.J.
  TITLE     Genome-wide long non-coding RNA association study on Han Chinese
            women identifies lncHSAT164 as a novel susceptibility gene for
            breast cancer
  JOURNAL   Chin Med J (Engl) 134 (10), 1138-1145 (2021)
   PUBMED   34018994
  REMARK    GeneRIF: Genome-wide long non-coding RNA association study on Han
            Chinese women identifies lncHSAT164 as a novel susceptibility gene
            for breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 972)
  AUTHORS   Bozpolat,A., Unal,E., Topaloglu,T., Taheri,S., Bayram,A.K.,
            Ozcan,A., Karakukcu,M., Ozdemir,M.A. and Per,H.
  TITLE     The relationship between the prognosis of children with acute
            arterial stroke and polymorphisms of CDKN2B, HDAC9, NINJ2, NAA25
            genes
  JOURNAL   J Thromb Thrombolysis 47 (4), 578-584 (2019)
   PUBMED   30656483
  REMARK    GeneRIF: The relationship between the prognosis of children with
            acute arterial stroke and polymorphisms of CDKN2B, HDAC9, NINJ2,
            NAA25 genes.
REFERENCE   4  (residues 1 to 972)
  AUTHORS   Yasuda,K., Takahashi,M. and Mori,N.
  TITLE     Mdm20 Modulates Actin Remodeling through the mTORC2 Pathway via Its
            Effect on Rictor Expression
  JOURNAL   PLoS One 10 (11), e0142943 (2015)
   PUBMED   26600389
  REMARK    GeneRIF: Mdm20 acts as a novel regulator of Rictor, thereby
            controlling mTORC2 activity, and leading to the activation of
            PKCalphaS657 and FoxO1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 972)
  AUTHORS   Dichgans,M., Malik,R., Konig,I.R., Rosand,J., Clarke,R.,
            Gretarsdottir,S., Thorleifsson,G., Mitchell,B.D., Assimes,T.L.,
            Levi,C., O'Donnell,C.J., Fornage,M., Thorsteinsdottir,U.,
            Psaty,B.M., Hengstenberg,C., Seshadri,S., Erdmann,J., Bis,J.C.,
            Peters,A., Boncoraglio,G.B., Marz,W., Meschia,J.F., Kathiresan,S.,
            Ikram,M.A., McPherson,R., Stefansson,K., Sudlow,C., Reilly,M.P.,
            Thompson,J.R., Sharma,P., Hopewell,J.C., Chambers,J.C., Watkins,H.,
            Rothwell,P.M., Roberts,R., Markus,H.S., Samani,N.J., Farrall,M. and
            Schunkert,H.
  CONSRTM   METASTROKE Consortium; CARDIoGRAM Consortium; C4D Consortium;
            International Stroke Genetics Consortium
  TITLE     Shared genetic susceptibility to ischemic stroke and coronary
            artery disease: a genome-wide analysis of common variants
  JOURNAL   Stroke 45 (1), 24-36 (2014)
   PUBMED   24262325
  REMARK    Review article
REFERENCE   6  (residues 1 to 972)
  AUTHORS   Polevoda,B., Arnesen,T. and Sherman,F.
  TITLE     A synopsis of eukaryotic Nalpha-terminal acetyltransferases:
            nomenclature, subunits and substrates
  JOURNAL   BMC Proc 3 Suppl 6 (Suppl 6), S2 (2009)
   PUBMED   19660095
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 972)
  AUTHORS   Prahalad,S., Hansen,S., Whiting,A., Guthery,S.L., Clifford,B.,
            McNally,B., Zeft,A.S., Bohnsack,J.F. and Jorde,L.B.
  TITLE     Variants in TNFAIP3, STAT4, and C12orf30 loci associated with
            multiple autoimmune diseases are also associated with juvenile
            idiopathic arthritis
  JOURNAL   Arthritis Rheum 60 (7), 2124-2130 (2009)
   PUBMED   19565500
  REMARK    GeneRIF: There are associations between juvenile idiopathic
            arthritis and variants in the TNFAIP3, STAT4, and C12orf30 regions
            that have previously shown associations with other autoimmune
            diseases, including rheumatoid arthritis and systemic lupus
            erythematosus.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 972)
  AUTHORS   Cooper,J.D., Smyth,D.J., Smiles,A.M., Plagnol,V., Walker,N.M.,
            Allen,J.E., Downes,K., Barrett,J.C., Healy,B.C., Mychaleckyj,J.C.,
            Warram,J.H. and Todd,J.A.
  TITLE     Meta-analysis of genome-wide association study data identifies
            additional type 1 diabetes risk loci
  JOURNAL   Nat Genet 40 (12), 1399-1401 (2008)
   PUBMED   18978792
REFERENCE   9  (residues 1 to 972)
  AUTHORS   Starheim,K.K., Arnesen,T., Gromyko,D., Ryningen,A., Varhaug,J.E.
            and Lillehaug,J.R.
  TITLE     Identification of the human N(alpha)-acetyltransferase complex B
            (hNatB): a complex important for cell-cycle progression
  JOURNAL   Biochem J 415 (2), 325-331 (2008)
   PUBMED   18570629
  REMARK    GeneRIF: Human N-acetyltransferase complexe NatB consists of human
            N-acetyltransferase 3 and human MDM20. The hMDM20 knockdown
            decreased the fraction of cells in G(0)/G(1)-phase and increased
            the fraction of cells in the sub-G(0)/G(1)-phase.
            GeneRIF: hMdm20 (C12orf30) is an auxiliary subunit of the human
            NatB N-terminal acetyltransferase complex while hNat3 (NAT5) is the
            catalytic subunit. This ribosome associated complex acetylates
            nascent Met-Asp/Glu- polypeptides.
REFERENCE   10 (residues 1 to 972)
  AUTHORS   Todd,J.A., Walker,N.M., Cooper,J.D., Smyth,D.J., Downes,K.,
            Plagnol,V., Bailey,R., Nejentsev,S., Field,S.F., Payne,F.,
            Lowe,C.E., Szeszko,J.S., Hafler,J.P., Zeitels,L., Yang,J.H.,
            Vella,A., Nutland,S., Stevens,H.E., Schuilenburg,H., Coleman,G.,
            Maisuria,M., Meadows,W., Smink,L.J., Healy,B., Burren,O.S.,
            Lam,A.A., Ovington,N.R., Allen,J., Adlem,E., Leung,H.T.,
            Wallace,C., Howson,J.M., Guja,C., Ionescu-Tirgoviste,C.,
            Simmonds,M.J., Heward,J.M., Gough,S.C., Dunger,D.B., Wicker,L.S.
            and Clayton,D.G.
  CONSRTM   Genetics of Type 1 Diabetes in Finland; Wellcome Trust Case Control
            Consortium
  TITLE     Robust associations of four new chromosome regions from genome-wide
            analyses of type 1 diabetes
  JOURNAL   Nat Genet 39 (7), 857-864 (2007)
   PUBMED   17554260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC113587.1, BX647450.1,
            BC047640.1 and AA653507.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 4, 2003 this sequence version replaced NP_079229.1.
            
            Summary: This gene encodes the auxiliary subunit of the heteromeric
            N-terminal acetyltransferase B complex. This complex acetylates
            methionine residues that are followed by acidic or asparagine
            residues.[provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647450.1, SRR1803615.8597.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261745.9/ ENSP00000261745.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.13"
     Protein         1..972
                     /product="N-alpha-acetyltransferase 25, NatB auxiliary
                     subunit"
                     /note="mitochondrial distribution and morphology 20; natB
                     complex subunit MDM20; N-terminal acetyltransferase B
                     complex subunit NAA25"
                     /calculated_mol_wt=112162
     Region          11..44
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CX7.1)"
     Region          21..146
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          45..78
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CX7.1)"
     Region          47..73
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(48,51..52,56,80,83..84,87..88,90..91,114,117..118,
                     121..122,125)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          78..108
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          79..112
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CX7.1)"
     Region          114..146
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CX7.1)"
     Region          263..658
                     /region_name="NatB_MDM20"
                     /note="N-acetyltransferase B complex (NatB) non catalytic
                     subunit; pfam09797"
                     /db_xref="CDD:430834"
     CDS             1..972
                     /gene="NAA25"
                     /gene_synonym="C12orf30; MDM20; NAP1"
                     /coded_by="NM_024953.4:11..2929"
                     /db_xref="CCDS:CCDS9159.1"
                     /db_xref="GeneID:80018"
                     /db_xref="HGNC:HGNC:25783"
                     /db_xref="MIM:612755"
ORIGIN      
        1 matrghvqdp ndrrlrpiyd yldngnnkma iqqadkllkk hkdlhcakvl kaiglqrtgk
       61 qeeaftlaqe vaaleptddn slqaltilyr emhrpelvtk lyeaavkkvp nseeyhshlf
      121 mayarvgeyk kmqqagmaly kivpknpyyf wsvmslimqs isaqdenlsk tmflplaerm
      181 vekmvkedki eaeaevelyy milerlgkyq ealdvirgkl gekltseiqs renkcmamyk
      241 klsrwpecna lsrrlllkns ddwqfyltyf dsvfrlieea wsppaegehs legevhysae
      301 kavkfiedri teeskssrhl rgphlaklel irrlrsqgcn deyklgdpee lmfqyfkkfg
      361 dkpccftdlk vfvdllpatq ctkfinqllg vvplstpted klalpadira lqqhlcvvql
      421 trllglyhtm dknqklsvvr elmlryqhgl efgktclkte lqfsdyycll avhalidvwr
      481 etgdettvwq altlleeglt hspsnaqfkl llvriycmlg afepvvdlys sldakhiqhd
      541 tigylltrya eslgqyaaas qscnfalrff hsnqkdtsey iiqaykygaf ekipefiafr
      601 nrlnnslhfa qvrtermlld llleanists laesiksmnl rpeeddipwe dlrdnrdlnv
      661 ffswdpkdrd vseehkklsl eeetlwlrir sltlrlisgl pslnhpvepk nsektaengv
      721 ssridilrll lqqleatlet gkrfiekdiq ypflgpvptr mggffnsgcs qcqissfylv
      781 ndiyeldtsg ledtmeiqer iensfkslld qlkdvfskck gdllevkdgn lkthptllen
      841 lvffvetisv ilwvssyces vlrpyklnlq kkkkkkkets iimppvftsf qdyvtglqtl
      901 isnvvdhikg lethlialkl eeliledtsl speerkfskt vqgkvqssyl hsllemgell
      961 kkrlettkkl ki
//
LOCUS       NP_002898                649 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-dependent DNA helicase Q1 [Homo sapiens].
ACCESSION   NP_002898
VERSION     NP_002898.2
DBSOURCE    REFSEQ: accession NM_002907.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Silva,J.P.L., Donaires,F.S., Gutierrez-Rodrigues,F., Martins,D.J.,
            Carvalho,V.S., Santana,B.A., Cunha,R.L.G., Kajigaya,S.,
            Menck,C.F.M., Young,N.S., Kjeldsen,E. and Calado,R.T.
  TITLE     RecQ helicase expression in patients with telomeropathies
  JOURNAL   Mol Biol Rep 51 (1), 754 (2024)
   PUBMED   38874681
  REMARK    GeneRIF: RecQ helicase expression in patients with telomeropathies.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Debnath,S., Lu,X., Lal,A. and Sharma,S.
  TITLE     Genome-wide investigations on regulatory functions of RECQ1
            helicase
  JOURNAL   Methods 204, 263-268 (2022)
   PUBMED   35231585
  REMARK    GeneRIF: Genome-wide investigations on regulatory functions of
            RECQ1 helicase.
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Abu-Libdeh,B., Jhujh,S.S., Dhar,S., Sommers,J.A., Datta,A.,
            Longo,G.M., Grange,L.J., Reynolds,J.J., Cooke,S.L., McNee,G.S.,
            Hollingworth,R., Woodward,B.L., Ganesh,A.N., Smerdon,S.J.,
            Nicolae,C.M., Durlacher-Betzer,K., Molho-Pessach,V., Abu-Libdeh,A.,
            Meiner,V., Moldovan,G.L., Roukos,V., Harel,T., Brosh,R.M. Jr. and
            Stewart,G.S.
  TITLE     RECON syndrome is a genome instability disorder caused by mutations
            in the DNA helicase RECQL1
  JOURNAL   J Clin Invest 132 (5) (2022)
   PUBMED   35025765
  REMARK    GeneRIF: RECON syndrome is a genome instability disorder caused by
            mutations in the DNA helicase RECQL1.
REFERENCE   5  (residues 1 to 649)
  AUTHORS   Mukhopadhyay,S., Das,T., Bose,M., Jain,C.K., Chakraborty,M.,
            Mukherjee,S., Shikha,K., Das,A.K. and Ganguly,A.
  TITLE     Residues at the interface between zinc binding and winged helix
            domains of human RECQ1 play a significant role in DNA strand
            annealing activity
  JOURNAL   Nucleic Acids Res 49 (20), 11834-11854 (2021)
   PUBMED   34751402
  REMARK    GeneRIF: Residues at the interface between zinc binding and winged
            helix domains of human RECQ1 play a significant role in DNA strand
            annealing activity.
REFERENCE   6  (residues 1 to 649)
  AUTHORS   Seki,T., Tada,S., Katada,T. and Enomoto,T.
  TITLE     Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1:
            discrimination of Qip1 and Rch1 from hSrp1 by their ability to
            interact with DNA helicase Q1/RecQL
  JOURNAL   Biochem Biophys Res Commun 234 (1), 48-53 (1997)
   PUBMED   9168958
REFERENCE   7  (residues 1 to 649)
  AUTHORS   Puranam,K.L., Kennington,E., Sait,S.N., Shows,T.B., Rochelle,J.M.,
            Seldin,M.F. and Blackshear,P.J.
  TITLE     Chromosomal localization of the gene encoding the human DNA
            helicase RECQL and its mouse homologue
  JOURNAL   Genomics 26 (3), 595-598 (1995)
   PUBMED   7607686
REFERENCE   8  (residues 1 to 649)
  AUTHORS   Puranam,K.L. and Blackshear,P.J.
  TITLE     Cloning and characterization of RECQL, a potential human homologue
            of the Escherichia coli DNA helicase RecQ
  JOURNAL   J Biol Chem 269 (47), 29838-29845 (1994)
   PUBMED   7961977
REFERENCE   9  (residues 1 to 649)
  AUTHORS   Seki,M., Miyazawa,H., Tada,S., Yanagisawa,J., Yamaoka,T.,
            Hoshino,S., Ozawa,K., Eki,T., Nogami,M., Okumura,K. et al.
  TITLE     Molecular cloning of cDNA encoding human DNA helicase Q1 which has
            homology to Escherichia coli Rec Q helicase and localization of the
            gene at chromosome 12p12
  JOURNAL   Nucleic Acids Res 22 (22), 4566-4573 (1994)
   PUBMED   7527136
REFERENCE   10 (residues 1 to 649)
  AUTHORS   Seki,M., Yanagisawa,J., Kohda,T., Sonoyama,T., Ui,M. and Enomoto,T.
  TITLE     Purification of two DNA-dependent adenosinetriphosphatases having
            DNA helicase activity from HeLa cells and comparison of the
            properties of the two enzymes
  JOURNAL   J Biochem 115 (3), 523-531 (1994)
   PUBMED   8056767
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA547846.1, CN414472.1,
            AK291627.1, D37984.1, CX784110.1, T94514.1 and CA431135.1.
            
            On Jul 3, 2001 this sequence version replaced NP_002898.1.
            
            Summary: The protein encoded by this gene is a member of the RecQ
            DNA helicase family. DNA helicases are enzymes involved in various
            types of DNA repair, including mismatch repair, nucleotide excision
            repair and direct repair. The encoded protein is involved in the
            processing of Holliday junctions, the suppression of sister
            chromatid exchanges, telomere maintenance, and is required for
            genotoxic stress resistance. Defects in this gene have been
            associated with several types of cancer. [provided by RefSeq, Jan
            2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.111623.1,
                                           SRR1660805.238344.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000444129.7/ ENSP00000416739.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..649
                     /product="ATP-dependent DNA helicase Q1"
                     /EC_number="5.6.2.4"
                     /note="recQ protein-like 1; RecQ helicase-like;
                     DNA-dependent ATPase Q1; RecQ protein-like (DNA helicase
                     Q1-like); DNA helicase, RecQ-like type 1; DNA 3'-5'
                     helicase Q1"
                     /calculated_mol_wt=73327
     Region          81..543
                     /region_name="recQ_fam"
                     /note="ATP-dependent DNA helicase, RecQ family; TIGR00614"
                     /db_xref="CDD:129701"
     Region          219..222
                     /region_name="DEVH box"
                     /note="propagated from UniProtKB/Swiss-Prot (P46063.3)"
     Region          481..592
                     /region_name="Winged-helix domain.
                     /evidence=ECO:0000269|PubMed:19151156"
                     /note="propagated from UniProtKB/Swiss-Prot (P46063.3)"
     Site            514
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P46063.3)"
     Site            522
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P46063.3)"
     Region          595..649
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46063.3)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46063.3)"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AYJ1; propagated from
                     UniProtKB/Swiss-Prot (P46063.3)"
     Site            634
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46063.3)"
     CDS             1..649
                     /gene="RECQL"
                     /gene_synonym="RECON; RecQ1; RECQL1"
                     /coded_by="NM_002907.4:512..2461"
                     /db_xref="CCDS:CCDS31756.1"
                     /db_xref="GeneID:5965"
                     /db_xref="HGNC:HGNC:9948"
                     /db_xref="MIM:600537"
ORIGIN      
        1 masvsaltee ldsitselha veiqiqelte rqqeliqkkk vltkkikqcl edsdagasne
       61 ydsspaawnk edfpwsgkvk dilqnvfkle kfrplqleti nvtmagkevf lvmptgggks
      121 lcyqlpalcs dgftlvicpl islmedqlmv lkqlgisatm lnassskehv kwvhaemvnk
      181 nselkliyvt pekiakskmf msrlekayea rrftriavde vhccsqwghd frpdykalgi
      241 lkrqfpnasl igltatatnh vltdaqkilc iekcftftas fnrpnlyyev rqkpsntedf
      301 iedivkling rykgqsgiiy cfsqkdseqv tvslqnlgih agayhanlep edkttvhrkw
      361 saneiqvvva tvafgmgidk pdvrfvihhs msksmenyyq esgragrddm kadcilyygf
      421 gdifrissmv vmenvgqqkl yemvsycqni skcrrvlmaq hfdevwnsea cnkmcdncck
      481 dsaferknit eycrdlikil kqaeelnekl tplklidswm gkgaaklrva gvvaptlpre
      541 dlekiiahfl iqqylkedys ftayatisyl kigpkanlln neahaitmqv tkstqnsfra
      601 essqtchseq gdkkmeekns gnfqkkaanm lqqsgskntg akkrkidda
//
LOCUS       NP_115519               1079 aa            linear   PRI 27-APR-2025
DEFINITION  DNA annealing helicase and endonuclease ZRANB3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_115519
VERSION     NP_115519.2
DBSOURCE    REFSEQ: accession NM_032143.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Moore,C.E., Yalcindag,S.E., Czeladko,H., Ravindranathan,R.,
            Wijesekara Hanthi,Y., Levy,J.C., Sannino,V., Schindler,D.,
            Ciccia,A., Costanzo,V. and Elia,A.E.H.
  TITLE     RFWD3 promotes ZRANB3 recruitment to regulate the remodeling of
            stalled replication forks
  JOURNAL   J Cell Biol 222 (5) (2023)
   PUBMED   37036693
  REMARK    GeneRIF: RFWD3 promotes ZRANB3 recruitment to regulate the
            remodeling of stalled replication forks.
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Joseph,S.A., Taglialatela,A., Leuzzi,G., Huang,J.W.,
            Cuella-Martin,R. and Ciccia,A.
  TITLE     Time for remodeling: SNF2-family DNA translocases in replication
            fork metabolism and human disease
  JOURNAL   DNA Repair (Amst) 95, 102943 (2020)
   PUBMED   32971328
  REMARK    GeneRIF: Time for remodeling: SNF2-family DNA translocases in
            replication fork metabolism and human disease.
            Review article
REFERENCE   4  (residues 1 to 1079)
  AUTHORS   Adeyemo,A.A., Zaghloul,N.A., Chen,G., Doumatey,A.P., Leitch,C.C.,
            Hostelley,T.L., Nesmith,J.E., Zhou,J., Bentley,A.R., Shriner,D.,
            Fasanmade,O., Okafor,G., Eghan,B. Jr., Agyenim-Boateng,K.,
            Chandrasekharappa,S., Adeleye,J., Balogun,W., Owusu,S., Amoah,A.,
            Acheampong,J., Johnson,T., Oli,J., Adebamowo,C., Collins,F.,
            Dunston,G. and Rotimi,C.N.
  CONSRTM   South Africa Zulu Type 2 Diabetes Case-Control Study
  TITLE     ZRANB3 is an African-specific type 2 diabetes locus associated with
            beta-cell mass and insulin response
  JOURNAL   Nat Commun 10 (1), 3195 (2019)
   PUBMED   31324766
  REMARK    GeneRIF: ZRANB3 is an African-specific type 2 diabetes locus
            associated with beta-cell mass and insulin response.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1079)
  AUTHORS   Fu,Y., Long,M.J.C., Wisitpitthaya,S., Inayat,H., Pierpont,T.M.,
            Elsaid,I.M., Bloom,J.C., Ortega,J., Weiss,R.S. and Aye,Y.
  TITLE     Nuclear RNR-alpha antagonizes cell proliferation by directly
            inhibiting ZRANB3
  JOURNAL   Nat Chem Biol 14 (10), 943-954 (2018)
   PUBMED   30150681
  REMARK    GeneRIF: Nuclear RNR-alpha antagonizes cell proliferation by
            directly inhibiting ZRANB3
REFERENCE   6  (residues 1 to 1079)
  AUTHORS   Badu-Nkansah,A., Mason,A.C., Eichman,B.F. and Cortez,D.
  TITLE     Identification of a Substrate Recognition Domain in the Replication
            Stress Response Protein Zinc Finger Ran-binding Domain-containing
            Protein 3 (ZRANB3)
  JOURNAL   J Biol Chem 291 (15), 8251-8257 (2016)
   PUBMED   26884333
  REMARK    GeneRIF: Here is described a substrate recognition domain within
            ZRANB3 that is needed for it to recognize forked DNA structures,
            hydrolyze ATP, catalyze fork remodeling, and act as a
            structure-specific endonuclease.
REFERENCE   7  (residues 1 to 1079)
  AUTHORS   Yuan,J., Ghosal,G. and Chen,J.
  TITLE     The HARP-like domain-containing protein AH2/ZRANB3 binds to PCNA
            and participates in cellular response to replication stress
  JOURNAL   Mol Cell 47 (3), 410-421 (2012)
   PUBMED   22705370
  REMARK    GeneRIF: AH2 is recruited to stalled replication forks and that
            cells depleted of AH2 are hypersensitive to replication stresses.
REFERENCE   8  (residues 1 to 1079)
  AUTHORS   Ciccia,A., Nimonkar,A.V., Hu,Y., Hajdu,I., Achar,Y.J., Izhar,L.,
            Petit,S.A., Adamson,B., Yoon,J.C., Kowalczykowski,S.C.,
            Livingston,D.M., Haracska,L. and Elledge,S.J.
  TITLE     Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain
            genomic integrity after replication stress
  JOURNAL   Mol Cell 47 (3), 396-409 (2012)
   PUBMED   22704558
  REMARK    GeneRIF: ZRANB3 translocase, a SNF2 family member related to the
            SIOD disorder SMARCAL1 protein, is recruited by polyubiquitinated
            PCNA to promote fork restart following replication arrest.
REFERENCE   9  (residues 1 to 1079)
  AUTHORS   Weston,R., Peeters,H. and Ahel,D.
  TITLE     ZRANB3 is a structure-specific ATP-dependent endonuclease involved
            in replication stress response
  JOURNAL   Genes Dev 26 (14), 1558-1572 (2012)
   PUBMED   22759634
  REMARK    GeneRIF: a role for ZRANB3 in the replication stress response and
            suggest new insights into how DNA repair is coordinated with DNA
            replication to maintain genome stability.
REFERENCE   10 (residues 1 to 1079)
  AUTHORS   Yusufzai,T. and Kadonaga,J.T.
  TITLE     Annealing helicase 2 (AH2), a DNA-rewinding motor with an HNH motif
  JOURNAL   Proc Natl Acad Sci U S A 107 (49), 20970-20973 (2010)
   PUBMED   21078962
  REMARK    GeneRIF: structural and functional differences between AH2 and HARP
            suggest that different annealing helicases have distinct functions
            in the cell.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC089429.1, AC017031.10 and AI670931.1.
            
            On Apr 22, 2005 this sequence version replaced NP_115519.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.226493.1,
                                           SRR1803613.283075.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264159.11/ ENSP00000264159.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.3"
     Protein         1..1079
                     /product="DNA annealing helicase and endonuclease ZRANB3
                     isoform 1"
                     /note="zinc finger Ran-binding domain-containing protein
                     3; annealing helicase 2; DNA annealing helicase and
                     endonuclease ZRANB3; zinc finger, RAN-binding domain
                     containing 3"
                     /calculated_mol_wt=123118
     Region          37..256
                     /region_name="DEXHc_HARP_SMARCAL1"
                     /note="DEXH-box helicase domain of SMARCAL1; cd18010"
                     /db_xref="CDD:350768"
     Region          46..481
                     /region_name="DNA annealing helicase activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FWF4.2)"
     Site            order(61..67,97,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350768"
     Region          157..160
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FWF4.2)"
     Region          321..446
                     /region_name="SF2_C_SNF"
                     /note="C-terminal helicase domain of the SNF family
                     helicases; cd18793"
                     /db_xref="CDD:350180"
     Site            order(347..348,356,398,419..420)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350180"
     Site            order(404..405,407,430,433)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350180"
     Region          519..526
                     /region_name="PIP-box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FWF4.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5FWF4.2)"
     Region          582..601
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FWF4.2)"
     Region          625..647
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          625..644
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     Site            630
                     /site_type="methylation"
                     /note="(Microbial infection) S-methylcysteine.
                     /evidence=ECO:0000269|PubMed:25412445; propagated from
                     UniProtKB/Swiss-Prot (Q5FWF4.2)"
     Region          689..725
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FWF4.2)"
     Region          1011..1079
                     /region_name="Endonuclease activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FWF4.2)"
     Region          <1011..1049
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(1018,1020..1022,1024,1036..1037,1041..1042,1045,
                     1049)
                     /site_type="active"
                     /db_xref="CDD:238038"
     Region          1074..1078
                     /region_name="APIM motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FWF4.2)"
     CDS             1..1079
                     /gene="ZRANB3"
                     /gene_synonym="4933425L19Rik; AH2"
                     /coded_by="NM_032143.4:100..3339"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46419.1"
                     /db_xref="GeneID:84083"
                     /db_xref="HGNC:HGNC:25249"
                     /db_xref="MIM:615655"
ORIGIN      
        1 mprvhnikks ltphiscvtn esdnlldflp drlrakllpf qkdgiifalk rngrcmvade
       61 mglgktiqai gityfykeew pllivvpssl rypwteeiek wipelspeei nviqnktdvr
      121 rmstskvtvl gyglltadak tlidalnnqn fkvvivdesh ymksrnatrs rillpivqka
      181 rrailltgtp algrpeelfm qiealfpqkf grwtdyakry cnahiryfgk rpqwdcrgas
      241 nlnelhqlls dimirrlkte vltqlppkvr qripfdlpsa aakelntsfe ewekimrtpn
      301 sgametvmgl itrmfkqtai akagavkdyi kmmlqndslk flvfahhlsm lqacteavie
      361 nktryiridg svssserihl vnqfqkdpdt rvailsiqaa gqgltftaas hvvfaelywd
      421 pghikqaedr ahrigqcssv nihyliangt ldtlmwgmln rkaqvtgstl ngrkekiqae
      481 egdkekwdfl qfaeawtpnd sseelrkeal fthfekekqh dirsffvpqp kkrqlmtscd
      541 eskrfreent vvssdptkta ardiidyesd vepetkrlkl aasedhcsps eetpsqskqi
      601 rtplvesvqe akaqlttpaf pvegwqcslc tyinnselpy cemcetpqgs avmqidslnh
      661 iqdknekdds qkdtskkvqt isdcekqala qsepgqlads keetpkieke dgltsqpgne
      721 qwkssdtlpv ydtlmfcasr ntdrihiytk dgkqmscnfi pldikldlwe dlpasfqlkq
      781 yrslilrfvr ewssltamkq riirksgqlf cspilaleei tkqqtkqnct kryitkedva
      841 vasmdkvknv gghvrlitke srprdpftkk lledgacvpf lnpytvqadl tvkpstskgy
      901 lqavdnegnp lclrcqqptc qtkqackans wdsrfcslkc qeefwirsnn sylrakvfet
      961 ehgvcqlcnv naqelflrlr dapksqrknl lyatwtsklp leqlnemirn pgeghfwqvd
     1021 hikpvygggg qcsldnlqtl ctvchkerta rqakersqvr rqslaskhgs ditrflvkk
//
LOCUS       NP_003717                359 aa            linear   PRI 27-APR-2025
DEFINITION  src kinase-associated phosphoprotein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_003717
VERSION     NP_003717.3
DBSOURCE    REFSEQ: accession NM_003726.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Zhu,L., Yu,Q., Li,Y., Zhang,M., Peng,Z., Wang,S., Quan,Z. and
            Gao,D.
  TITLE     SKAP1 Is a Novel Biomarker and Therapeutic Target for Gastric
            Cancer: Evidence from Expression, Functional, and Bioinformatic
            Analyses
  JOURNAL   Int J Mol Sci 24 (14), 11870 (2023)
   PUBMED   37511629
  REMARK    GeneRIF: SKAP1 Is a Novel Biomarker and Therapeutic Target for
            Gastric Cancer: Evidence from Expression, Functional, and
            Bioinformatic Analyses.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Canson,D.M., O'Mara,T.A., Spurdle,A.B. and Glubb,D.M.
  TITLE     Splicing annotation of endometrial cancer GWAS risk loci reveals
            potentially causal variants and supports a role for NF1 and SKAP1
            as susceptibility genes
  JOURNAL   HGG Adv 4 (2), 100185 (2023)
   PUBMED   36908940
  REMARK    GeneRIF: Splicing annotation of endometrial cancer GWAS risk loci
            reveals potentially causal variants and supports a role for NF1 and
            SKAP1 as susceptibility genes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Pu,Y., Wei,J., Wu,Y., Zhao,K., Wu,Y., Wu,S., Yang,X. and Xing,C.
  TITLE     THUMPD3-AS1 facilitates cell growth and aggressiveness by the
            miR-218-5p/SKAP1 axis in colorectal cancer
  JOURNAL   Cell Biochem Biophys 80 (3), 483-494 (2022)
   PUBMED   35538197
  REMARK    GeneRIF: THUMPD3-AS1 facilitates cell growth and aggressiveness by
            the miR-218-5p/SKAP1 axis in colorectal cancer.
            Erratum:[Cell Biochem Biophys. 2024 Mar;82(1):315. doi:
            10.1007/s12013-023-01199-0. PMID: 38010601]
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Dadwal,N., Mix,C., Reinhold,A., Witte,A., Freund,C., Schraven,B.
            and Kliche,S.
  TITLE     The Multiple Roles of the Cytosolic Adapter Proteins ADAP, SKAP1
            and SKAP2 for TCR/CD3 -Mediated Signaling Events
  JOURNAL   Front Immunol 12, 703534 (2021)
   PUBMED   34295339
  REMARK    GeneRIF: The Multiple Roles of the Cytosolic Adapter Proteins ADAP,
            SKAP1 and SKAP2 for TCR/CD3 -Mediated Signaling Events.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Kouroku,Y., Soyama,A., Fujita,E., Urase,K., Tsukahara,T. and
            Momoi,T.
  TITLE     RA70 is a src kinase-associated protein expressed ubiquitously
  JOURNAL   Biochem Biophys Res Commun 252 (3), 738-742 (1998)
   PUBMED   9837776
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Marie-Cardine,A., Hendricks-Taylor,L.R., Boerth,N.J., Zhao,H.,
            Schraven,B. and Koretzky,G.A.
  TITLE     Molecular interaction between the Fyn-associated protein SKAP55 and
            the SLP-76-associated phosphoprotein SLAP-130
  JOURNAL   J Biol Chem 273 (40), 25789-25795 (1998)
   PUBMED   9748251
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Liu,J., Kang,H., Raab,M., da Silva,A.J., Kraeft,S.K. and Rudd,C.E.
  TITLE     FYB (FYN binding protein) serves as a binding partner for lymphoid
            protein and FYN kinase substrate SKAP55 and a SKAP55-related
            protein in T cells
  JOURNAL   Proc Natl Acad Sci U S A 95 (15), 8779-8784 (1998)
   PUBMED   9671755
REFERENCE   9  (residues 1 to 359)
  AUTHORS   Marie-Cardine,A., Bruyns,E., Eckerskorn,C., Kirchgessner,H.,
            Meuer,S.C. and Schraven,B.
  TITLE     Molecular cloning of SKAP55, a novel protein that associates with
            the protein tyrosine kinase p59fyn in human T-lymphocytes
  JOURNAL   J Biol Chem 272 (26), 16077-16080 (1997)
   PUBMED   9195899
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Schraven,B., Marie-Cardine,A. and Koretzky,G.
  TITLE     Molecular analysis of the fyn-complex: cloning of SKAP55 and
            SLAP-130, two novel adaptor proteins which associate with fyn and
            may participate in the regulation of T cell receptor-mediated
            signaling
  JOURNAL   Immunol Lett 57 (1-3), 165-169 (1997)
   PUBMED   9232446
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR007155.1, Y11215.1 and
            BC047870.1.
            
            On Oct 4, 2006 this sequence version replaced NP_003717.2.
            
            Summary: This gene encodes a T cell adaptor protein, a class of
            intracellular molecules with modular domains capable of recruiting
            additional proteins but that exhibit no intrinsic enzymatic
            activity. The encoded protein contains a unique N-terminal region
            followed by a PH domain and C-terminal SH3 domain. Along with the
            adhesion and degranulation-promoting adaptor protein, the encoded
            protein plays a critical role in inside-out signaling by coupling
            T-cell antigen receptor stimulation to the activation of integrins.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y11215.1, SRR18074968.2842179.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336915.11/ ENSP00000338171.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..359
                     /product="src kinase-associated phosphoprotein 1 isoform
                     1"
                     /note="src kinase-associated phosphoprotein of 55 kDa;
                     pp55; SKAP-55; src family-associated phosphoprotein 1;
                     epididymis secretory sperm binding protein Li 81p"
                     /calculated_mol_wt=41301
     Region          108..213
                     /region_name="PH_Skap1"
                     /note="Src kinase-associated phosphoprotein 1 Pleckstrin
                     homology (PH) domain; cd13380"
                     /db_xref="CDD:270180"
     Site            order(116..119,121,131,142,152,186)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270180"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q3UUV5; propagated from
                     UniProtKB/Swiss-Prot (Q86WV1.3)"
     Region          219..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86WV1.3)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:11909961; propagated from
                     UniProtKB/Swiss-Prot (Q86WV1.3)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:11909961; propagated from
                     UniProtKB/Swiss-Prot (Q86WV1.3)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FYN.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q86WV1.3)"
     Region          290..295
                     /region_name="Interaction with FYB1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86WV1.3)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FYN. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q86WV1.3)"
     Region          298..350
                     /region_name="SH3_SKAP1"
                     /note="Src Homology 3 domain of Src Kinase-Associated
                     Phosphoprotein 1; cd12044"
                     /db_xref="CDD:212977"
     Site            order(303,305,308,312,332..333,346,348..349)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212977"
     CDS             1..359
                     /gene="SKAP1"
                     /gene_synonym="HEL-S-81p; SCAP1; SKAP55"
                     /coded_by="NM_003726.4:95..1174"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32674.1"
                     /db_xref="GeneID:8631"
                     /db_xref="HGNC:HGNC:15605"
                     /db_xref="MIM:604969"
ORIGIN      
        1 mqaaalpeei rwlledaeef laeglrnenl savardhrdh ilrgfqqika ryywdfqpqg
       61 gdigqdssdd nhsgtlglsl tsdapflsdy qdegmedivk gaqeldnvik qgylekkskd
      121 hsffgsewqk rwcvvsrglf yyyanekskq pkgtflikgy gvrmaphlrr dskkescfel
      181 tsqdrrsyef tatspaeard wvdqisfllk dlssltipye edeeeeekee tyddidgfds
      241 pscgsqcrpt ilpgsvgike pteekeeedi yevlpdeehd leedesgtrr kgvdyasyyq
      301 glwdchgdqp delsfqrgdl irilskeynm ygwwvgelns lvgivpkeyl ttafeveer
//
LOCUS       NP_001074476             579 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 382 isoform 1 [Mus musculus].
ACCESSION   NP_001074476 XP_001000443
VERSION     NP_001074476.1
DBSOURCE    REFSEQ: accession NM_001081007.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Ma,L., Yu,L., Jiang,B.C., Wang,J., Guo,X., Huang,Y., Ren,J.,
            Sun,N., Gao,D.S., Ding,H., Lu,J., Zhou,H., Zou,L., Gao,Y., Wang,L.,
            Sun,K., Ming,Y., Meng,Z., Tao,Y.X. and Yan,M.
  TITLE     ZNF382 controls mouse neuropathic pain via silencer-based
            epigenetic inhibition of Cxcl13 in DRG neurons
  JOURNAL   J Exp Med 218 (12) (2021)
   PUBMED   34762123
  REMARK    GeneRIF: ZNF382 controls mouse neuropathic pain via silencer-based
            epigenetic inhibition of Cxcl13 in DRG neurons.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC164703.3.
            
            On Feb 6, 2007 this sequence version replaced XP_001000443.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.59896.1,
                                           SRR1660821.68555.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7"
     Protein         1..579
                     /product="zinc finger protein 382 isoform 1"
                     /note="KRAB/zinc finger suppressor protein 1; multiple
                     zinc finger and krueppel-associated box protein KS1"
                     /calculated_mol_wt=66416
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RXC5.1)"
     Region          12..135
                     /region_name="Mediates interaction with TRIM28.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RXC5.1)"
     Region          40..81
                     /region_name="Represses transcription.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RXC5.1)"
     Region          42..102
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          105..240
                     /region_name="Represses transcription.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RXC5.1)"
     Region          303..319
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          325..579
                     /region_name="Required for transcriptional repression
                     activity, probably mediates sequence-specific DNA-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RXC5.1)"
     Region          325..347
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          327..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          355..375
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          383..403
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <411..562
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          411..431
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(416,418,420,422..423,426..427,430,444,446,450..451,
                     454..455,458,472,474,476,478..479,482..483,486)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          439..459
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          467..487
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          495..515
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          523..543
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          551..571
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..579
                     /gene="Zfp382"
                     /gene_synonym="4930428B01Rik; 5930415A09Rik; KS1; Znf382"
                     /coded_by="NM_001081007.2:103..1842"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS39877.1"
                     /db_xref="GeneID:233060"
                     /db_xref="MGI:MGI:3588204"
ORIGIN      
        1 mgrpgrkprg rarpglfpfp keelrqggss panlnamskg pvsfkdvtvd ftqeewqrld
       61 paqkalyrdv mlenychfis vgfhitkpdm irkleqgeel wterifpsqs yleeeevlvk
      121 fsdyqdkppk siviikhkkl ikerssvyge algknrvvsk tlfeyksdgk vlknisefis
      181 rdinpamgkl ggskewegsi ltskqekthp asilhkqigr alssewdlaq hqktqipeqr
      241 feynkcdssf lmtgvefphg rahrgggnfn yskdditlfe ksdlgihphd lmekkcssyn
      301 kygellcrks vfvmhpssqm derpfqcpyc gnsfrrksyl ieherihtge kpyiccqcgr
      361 afrqktaltl hekthtegkp ylcvdcgksf rqkatltrhh kahtgekaye ctqcgsafgk
      421 ksylidhqrt htgekpyqct ecgkafiqkt tltvhqrtht gekpyicsec gksfcqkttl
      481 tlhqrihtge kpyicsdcgk sfrqkailtv hyrihtgeks ngcpqcgkaf srksnlirhq
      541 kihtgekpye cqecgkffsc ksnlithqkt hktetmrfq
//
LOCUS       NP_061944                418 aa            linear   PRI 27-APR-2025
DEFINITION  inhibitor of growth protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_061944
VERSION     NP_061944.2
DBSOURCE    REFSEQ: accession NM_019071.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Cheng,S., Li,M., Zheng,W., Li,C., Hao,Z., Dai,Y., Wang,J., Zhuo,J.
            and Zhang,L.
  TITLE     ING3 inhibits the malignant progression of lung adenocarcinoma by
            negatively regulating ITGB4 expression to inactivate Src/FAK
            signaling
  JOURNAL   Cell Signal 117, 111066 (2024)
   PUBMED   38281617
  REMARK    GeneRIF: ING3 inhibits the malignant progression of lung
            adenocarcinoma by negatively regulating ITGB4 expression to
            inactivate Src/FAK signaling.
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Song,Y., Hou,G., Diep,J., Ooi,Y.S., Akopyants,N.S., Beverley,S.M.,
            Carette,J.E., Greenberg,H.B. and Ding,S.
  TITLE     Inhibitor of growth protein 3 epigenetically silences endogenous
            retroviral elements and prevents innate immune activation
  JOURNAL   Nucleic Acids Res 49 (22), 12706-12715 (2021)
   PUBMED   34791430
  REMARK    GeneRIF: Inhibitor of growth protein 3 epigenetically silences
            endogenous retroviral elements and prevents innate immune
            activation.
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Melekhova,A. and Baniahmad,A.
  TITLE     ING Tumour Suppressors and ING Splice Variants as Coregulators of
            the Androgen Receptor Signalling in Prostate Cancer
  JOURNAL   Cells 10 (10), 2599 (2021)
   PUBMED   34685579
  REMARK    GeneRIF: ING Tumour Suppressors and ING Splice Variants as
            Coregulators of the Androgen Receptor Signalling in Prostate
            Cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Martinez-Vargas,Y.D.C., Silva-Filho,T.J.D., Oliveira,D.H.I.P.,
            Goncalo,R.I.C. and Queiroz,L.M.G.
  TITLE     ING3 and ING4 immunoexpression and their relation to the
            development of benign odontogenic lesions
  JOURNAL   Braz Dent J 32 (4), 74-82 (2021)
   PUBMED   34787253
  REMARK    GeneRIF: ING3 and ING4 immunoexpression and their relation to the
            development of benign odontogenic lesions.
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Doyon,Y. and Cote,J.
  TITLE     The highly conserved and multifunctional NuA4 HAT complex
  JOURNAL   Curr Opin Genet Dev 14 (2), 147-154 (2004)
   PUBMED   15196461
  REMARK    Review article
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Doyon,Y., Selleck,W., Lane,W.S., Tan,S. and Cote,J.
  TITLE     Structural and functional conservation of the NuA4 histone
            acetyltransferase complex from yeast to humans
  JOURNAL   Mol Cell Biol 24 (5), 1884-1896 (2004)
   PUBMED   14966270
REFERENCE   8  (residues 1 to 418)
  AUTHORS   Cai,Y., Jin,J., Tomomori-Sato,C., Sato,S., Sorokina,I.,
            Parmely,T.J., Conaway,R.C. and Conaway,J.W.
  TITLE     Identification of new subunits of the multiprotein mammalian
            TRRAP/TIP60-containing histone acetyltransferase complex
  JOURNAL   J Biol Chem 278 (44), 42733-42736 (2003)
   PUBMED   12963728
REFERENCE   9  (residues 1 to 418)
  AUTHORS   Nagashima,M., Shiseki,M., Pedeux,R.M., Okamura,S.,
            Kitahama-Shiseki,M., Miura,K., Yokota,J. and Harris,C.C.
  TITLE     A novel PHD-finger motif protein, p47ING3, modulates p53-mediated
            transcription, cell cycle control, and apoptosis
  JOURNAL   Oncogene 22 (3), 343-350 (2003)
   PUBMED   12545155
  REMARK    GeneRIF: we have isolated a novel ING family gene, p47ING3, which
            modulates p53-mediated transcription, cell cycle control, and
            apoptosis. The p47ING3 gene is located at chromosome 7q31.3 and
            consists of 12 exons that encode 418 amino acids
REFERENCE   10 (residues 1 to 418)
  AUTHORS   Gunduz,M., Ouchida,M., Fukushima,K., Ito,S., Jitsumori,Y.,
            Nakashima,T., Nagai,N., Nishizaki,K. and Shimizu,K.
  TITLE     Allelic loss and reduced expression of the ING3, a candidate tumor
            suppressor gene at 7q31, in human head and neck cancers
  JOURNAL   Oncogene 21 (28), 4462-4470 (2002)
   PUBMED   12080476
  REMARK    GeneRIF: Allelic loss and reduced expression of the ING3, a
            candidate tumor suppressor gene at 7q31, in human head and neck
            cancers.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK000096.1, AF074968.1,
            BU684039.1, BU677936.1 and AC004537.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 7, 2003 this sequence version replaced NP_061944.1.
            
            Summary: The protein encoded by this gene is similar to ING1, a
            tumor suppressor protein that can interact with TP53, inhibit cell
            growth, and induce apoptosis. This protein contains a PHD-finger,
            which is a common motif in proteins involved in chromatin
            remodeling. This gene can activate p53 trans-activated promoters,
            including promoters of p21/waf1 and bax. Overexpression of this
            gene has been shown to inhibit cell growth and induce apoptosis.
            Allelic loss and reduced expression of this gene were detected in
            head and neck cancers. Two alternatively spliced transcript
            variants encoding different isoforms have been observed. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.133292.1,
                                           SRR1660805.170840.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315870.10/ ENSP00000320566.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.31"
     Protein         1..418
                     /product="inhibitor of growth protein 3 isoform 1"
                     /note="inhibitor of growth protein 3"
                     /calculated_mol_wt=46612
     Region          3..102
                     /region_name="ING"
                     /note="Inhibitor of growth proteins N-terminal
                     histone-binding; pfam12998"
                     /db_xref="CDD:463768"
     Region          4..410
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          127..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXR8.2)"
     Site            181
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK6; propagated from
                     UniProtKB/Swiss-Prot (Q9NXR8.2)"
     Site            264
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NXR8.2)"
     Region          286..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXR8.2)"
     Region          362..406
                     /region_name="PHD_ING3"
                     /note="PHD finger found in inhibitor of growth protein 3
                     (ING3) and similar proteins; cd15585"
                     /db_xref="CDD:277060"
     Site            order(362,372..377,384..385,388,396..397,399,401)
                     /site_type="other"
                     /note="H3K4me3 binding site [polypeptide binding]"
                     /db_xref="CDD:277060"
     Site            362
                     /site_type="other"
                     /note="Histone H3K4me3 binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UK53; propagated from
                     UniProtKB/Swiss-Prot (Q9NXR8.2)"
     Site            373
                     /site_type="other"
                     /note="Histone H3K4me3 binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UK53; propagated from
                     UniProtKB/Swiss-Prot (Q9NXR8.2)"
     Site            377
                     /site_type="other"
                     /note="Histone H3K4me3 binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UK53; propagated from
                     UniProtKB/Swiss-Prot (Q9NXR8.2)"
     Site            385
                     /site_type="other"
                     /note="Histone H3K4me3 binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UK53; propagated from
                     UniProtKB/Swiss-Prot (Q9NXR8.2)"
     CDS             1..418
                     /gene="ING3"
                     /gene_synonym="Eaf4; ING2; MEAF4; p47ING3"
                     /coded_by="NM_019071.3:121..1377"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5778.1"
                     /db_xref="GeneID:54556"
                     /db_xref="HGNC:HGNC:14587"
                     /db_xref="MIM:607493"
ORIGIN      
        1 mlyledylem ieqlpmdlrd rftemremdl qvqnamdqle qrvseffmna kknkpewree
       61 qmasikkdyy kaledadekv qlanqiydlv drhlrkldqe lakfkmelea dnagiteile
      121 rrsleldtps qpvnnhhahs htpvekrkyn ptshhtttdh ipekkfksea llstltsdas
      181 kentlgcrnn nstassnnay nvnssqplgs ynigslssgt gagaitmaaa qavqataqmk
      241 egrrtsslka syeafknndf qlgkefsmar etvgyssssa lmttltqnas ssaadsrsgr
      301 ksknnnksss qqssssssss slsscsssst vvqeisqqtt vvpesdsnsq vdwtydpnep
      361 rycicnqvsy gemvgcdnqd cpiewfhygc vglteapkgk wycpqctaam krrgsrhk
//
LOCUS       NP_001034682             204 aa            linear   ROD 27-APR-2025
DEFINITION  spermatogenesis-associated protein 46 [Mus musculus].
ACCESSION   NP_001034682 XP_355274 XP_922601
VERSION     NP_001034682.1
DBSOURCE    REFSEQ: accession NM_001039593.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Chen,J., Gu,Y., Zhang,Z., Zheng,W., Yang,L., Huang,W., Lin,S.,
            Li,Y., Guo,H., Luo,M., Ma,Q., Jiang,Z., Tang,A. and Gui,Y.
  TITLE     Deficiency of SPATA46, a Novel Nuclear Membrane Protein, Causes
            Subfertility in Male Mice
  JOURNAL   Biol Reprod 95 (3), 58 (2016)
   PUBMED   27488028
  REMARK    GeneRIF: In the present study, we demonstrated that deletion of
            Spata46, a gene encoding a novel protein of unknown function found
            in mouse testis, was responsible for male subfertility, and the
            cause of subfertility was characterized as abnormal sperm head
            shape and a failure of sperm-egg fusion.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC119431.13.
            
            On or before Feb 26, 2006 this sequence version replaced
            XP_922601.1, XP_355274.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099563.1, AK005990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 76.84 cM"
     Protein         1..204
                     /product="spermatogenesis-associated protein 46"
                     /note="uncharacterized protein C1orf111 homolog"
                     /calculated_mol_wt=22866
     Region          1..185
                     /region_name="Spt46"
                     /note="Spermatogenesis-associated protein 46; pfam17734"
                     /db_xref="CDD:375300"
     Region          101..120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZF2.1)"
     CDS             1..204
                     /gene="Spata46"
                     /gene_synonym="1700015E13Rik"
                     /coded_by="NM_001039593.2:64..678"
                     /db_xref="CCDS:CCDS15471.1"
                     /db_xref="GeneID:76925"
                     /db_xref="MGI:MGI:1924175"
ORIGIN      
        1 mdnysllstp rprisssals afpdimssla tslpdlgdtq ngeqlrrnct iyrpwfspys
       61 yfvctdkesh leaygfpevd reegrgdncl ledvaesvcs ssssqentyp reanrkskhg
      121 ldsitsqdil maskwhpaqq ngykcasccr myptlhslks hikggfkegf sckvyyrklk
      181 tlwgkeqkar tgdrislgsc qafk
//
LOCUS       NP_938040               1965 aa            linear   ROD 27-APR-2025
DEFINITION  probable helicase with zinc finger domain isoform 1 [Mus musculus].
ACCESSION   NP_938040 XP_126554
VERSION     NP_938040.1
DBSOURCE    REFSEQ: accession NM_198298.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1965)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1965)
  AUTHORS   Bian,Y., Pang,P., Li,X., Yu,S., Wang,X., Liu,K., Ju,J., Wu,H.,
            Gao,Y., Liu,Q., Jia,Y., Qu,Z., Bi,X., Mei,Z., Yin,X., Wang,N.,
            Du,W. and Yang,B.
  TITLE     CircHelz activates NLRP3 inflammasome to promote myocardial injury
            by sponging miR-133a-3p in mouse ischemic heart
  JOURNAL   J Mol Cell Cardiol 158, 128-139 (2021)
   PUBMED   34043986
  REMARK    GeneRIF: CircHelz activates NLRP3 inflammasome to promote
            myocardial injury by sponging miR-133a-3p in mouse ischemic heart.
REFERENCE   3  (residues 1 to 1965)
  AUTHORS   Hasgall,P.A., Hoogewijs,D., Faza,M.B., Panse,V.G., Wenger,R.H. and
            Camenisch,G.
  TITLE     The putative RNA helicase HELZ promotes cell proliferation,
            translation initiation and ribosomal protein S6 phosphorylation
  JOURNAL   PLoS One 6 (7), e22107 (2011)
   PUBMED   21765940
  REMARK    GeneRIF: Downregulation of HELZ reduced translational initiation,
            resulting in the disassembly of polysomes, in a reduction of cell
            proliferation and hypophosphorylation of ribosomal protein S6.
REFERENCE   4  (residues 1 to 1965)
  AUTHORS   Diehl,F., Brown,M.A., van Amerongen,M.J., Novoyatleva,T.,
            Wietelmann,A., Harriss,J., Ferrazzi,F., Bottger,T., Harvey,R.P.,
            Tucker,P.W. and Engel,F.B.
  TITLE     Cardiac deletion of Smyd2 is dispensable for mouse heart
            development
  JOURNAL   PLoS One 5 (3), e9748 (2010)
   PUBMED   20305823
  REMARK    GeneRIF: Smyd2, similar to Smyd3, interacts with RNA Polymerase II
            as well as to the RNA helicase, HELZ
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1965)
  AUTHORS   Corbo,J.C. and Cepko,C.L.
  TITLE     A hybrid photoreceptor expressing both rod and cone genes in a
            mouse model of enhanced S-cone syndrome
  JOURNAL   PLoS Genet 1 (2), e11 (2005)
   PUBMED   16110338
  REMARK    Erratum:[PLoS Genet. 2008 Jan;4(1):e18]
REFERENCE   6  (residues 1 to 1965)
  AUTHORS   Cobellis,G., Nicolaus,G., Iovino,M., Romito,A., Marra,E.,
            Barbarisi,M., Sardiello,M., Di Giorgio,F.P., Iovino,N., Zollo,M.,
            Ballabio,A. and Cortese,R.
  TITLE     Tagging genes with cassette-exchange sites
  JOURNAL   Nucleic Acids Res 33 (4), e44 (2005)
   PUBMED   15741177
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1965)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   8  (residues 1 to 1965)
  AUTHORS   Wagner,D.S., Gan,L. and Klein,W.H.
  TITLE     Identification of a differentially expressed RNA helicase by gene
            trapping
  JOURNAL   Biochem Biophys Res Commun 262 (3), 677-684 (1999)
   PUBMED   10471385
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL645947.9.
            
            On Sep 3, 2004 this sequence version replaced XP_126554.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC076626.1, SRR10223970.14820.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1965
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 70.29 cM"
     Protein         1..1965
                     /product="probable helicase with zinc finger domain
                     isoform 1"
                     /note="probable helicase with zinc finger domain"
                     /calculated_mol_wt=219837
     Region          181..205
                     /region_name="zf-CCCH"
                     /note="Zinc finger C-x8-C-x5-C-x3-H type (and similar);
                     pfam00642"
                     /db_xref="CDD:459885"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42694; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Region          641..868
                     /region_name="DEXXQc_HELZ"
                     /note="DEXXQ-box helicase domain of HELZ; cd18077"
                     /db_xref="CDD:350835"
     Site            order(646,671..676,826,867..868)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350835"
     Region          <766..1075
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
     Region          795..798
                     /region_name="DEAA box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Region          1117..1136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Site            1164
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P42694; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Region          <1225..1414
                     /region_name="Tymo_45kd_70kd"
                     /note="Tymovirus 45/70Kd protein; pfam03251"
                     /db_xref="CDD:281269"
     Site            1246
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P42694; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Region          1249..1351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Region          <1338..>1414
                     /region_name="Amelogenin"
                     /note="Amelogenins, cell adhesion proteins, play a role in
                     the biomineralisation of teeth; smart00818"
                     /db_xref="CDD:197891"
     Region          1361..1380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Region          1389..1450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Region          1464..1492
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Region          1632..1656
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Site            1637
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42694; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Region          1744..1965
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Site            1761
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42694; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Site            1764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV5.2)"
     Site            1789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42694; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV5.2)"
     CDS             1..1965
                     /gene="Helz"
                     /gene_synonym="3110078M01Rik; 9430093I07Rik;
                     9630002H22Rik; DRHC"
                     /coded_by="NM_198298.2:124..6021"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS25569.1"
                     /db_xref="GeneID:78455"
                     /db_xref="MGI:MGI:1925705"
ORIGIN      
        1 medrraersc eqacaslqrq dydmalqhct dallslgqys madftgpcpv everikiesl
       61 lyriasflql knygqadedc rhvlgeglak gerafravlc cmqlkgklql vssilaksls
      121 geslngmvtk dltrlktllt etetatsnvl sgchvedlde gscngwhfrp pprgitssee
      181 ytlckrfleq gicrygaqct sahsqeelae wqkryasrli klkqqsenkq lsgsymetli
      241 ekwmsslspe kvlseciegv qvehspdlsv tvntkkshqt wtfaltckpa rmlyrvally
      301 dahrphfsii aisagdsttq vsqevpencq ewiggkmaqn gldhyvykvg iafnteifgt
      361 frqtivfdfg lepvlmqrvm idaastedle ylmhakrqlv ttakrwdsss ktivdfepne
      421 ttdlekslli ryqiplsadq lftqsvldks ltktnyqarl hdllyieeia qykevsrfnl
      481 kvqlqilasf mltgvsggak yaqngqlfgr fkltetlsed tlagrlvmtr vnavyllpvp
      541 keklvqsqgt kekvyeatie ektkdyvflr isrecceels lrpdcdiqve lqfqlnrlpl
      601 cemhyaldri kdnavlfpdi smtptipwsp nrqwdeqldp rlnakqkeav laittplsiq
      661 lppvliigpy gtgktftlaq aakhilqqqe tsrilicths nsaadlyikd ylhpyveagn
      721 pqarplrvyf rnrwvktvhp vvhqycliss tqstfqmpqk edilkhrvvv vtlstsqylc
      781 qldlepgfft hvlldeaaqa mecetimpla latkntrivl agdhmqlspf vysefarern
      841 lhvslldrly ehypaefpcr illcenyrsh eaiinytsel fyegklmasg kqpahkdfyp
      901 ltfftarged vqeknstafy nnaevfevve rveelrrkwp vawgklddgs igvvtpyadq
      961 vfriraelrk krlsdvnver vlnvqgkqfr vlflstvrtr htckhkqtpi kkkeqlleds
     1021 tedldygfls nykllntait raqslvavvg dpvalcsigr crkfwerfia lchenhslhg
     1081 itfeqikaql ealelkktyv lnplapefip ralrlqhsgn ssrqqqsppk vkslyhpqsd
     1141 hfqsdgivqp npsvlignpi raytpppplg phpnlgksps pvqridphtg tsilyvpavy
     1201 ggnvvmsvpl pvpwtgyqgr favdpriith qaamaynmnl lhthgrgspi pyglghhppv
     1261 slgqpqsqha ekdqqeqnrn gktdtnnpgp einkirtpek kptepkqvdl esnpqnrspe
     1321 srpgvvysnt kfprkdhlnp rhinnlplpa phaqyaipsr hfhplpqlpr ppfpasqpht
     1381 llnqqqnnlp eqpnqmapqp nqvapqpnqm tpqpnqvapq pnqvvqqqsq appqapqpap
     1441 qlspafqagp tnaffnnava hrpqspaaea vgpeqppppg lpdghsplra itqpgpilas
     1501 plnnfvdess pglpieeald gvhgsvalet lrqqqarlqq wsehhaylsq ggipyshhhh
     1561 phlphlphtp iglhqppvra ewkvagradd etettfsrfq dllrelshrd qgdtgelaem
     1621 pppqsrllqy rqvqprsppa vpsppsstdh ssqfanfnds srdievansp afpqrlppql
     1681 fgspfslpse hlappplkyl apegawnfan lqqnhligpg fpyglpplpp rppqnpfihi
     1741 qnhqhaagqe pfhplssrtv sasslpslee yeprgpgrpl yqrrissssa qpcveeasap
     1801 qdslaqgkes qghsnppafn fpapeswant tssapyqnip cngssrtsqp reliappktv
     1861 kppedqlkpe sgevsssfny smlqhlgqfp plmpnkqiae sancssqqsp agskpamsya
     1921 salrappkpr pppeqakkgs dplsllqels lgsspgsngf ysyfk
//
LOCUS       NP_001346681             642 aa            linear   ROD 27-APR-2025
DEFINITION  voltage-gated potassium channel KCNC2 isoform 1 [Mus musculus].
ACCESSION   NP_001346681 XP_006513751
VERSION     NP_001346681.1
DBSOURCE    REFSEQ: accession NM_001359752.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Russell,N.X., Burra,K., Shah,R.M., Bottasso-Arias,N.,
            Mohanakrishnan,M., Snowball,J., Ediga,H.H., Madala,S.K. and
            Sinner,D.
  TITLE     Wnt signaling regulates ion channel expression to promote smooth
            muscle and cartilage formation in developing mouse trachea
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 325 (6), L788-L802 (2023)
   PUBMED   37873566
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Bedogni,F., Cobolli Gigli,C., Pozzi,D., Rossi,R.L., Scaramuzza,L.,
            Rossetti,G., Pagani,M., Kilstrup-Nielsen,C., Matteoli,M. and
            Landsberger,N.
  TITLE     Defects During Mecp2 Null Embryonic Cortex Development Precede the
            Onset of Overt Neurological Symptoms
  JOURNAL   Cereb Cortex 26 (6), 2517-2529 (2016)
   PUBMED   25979088
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Kraushar,M.L., Viljetic,B., Wijeratne,H.R., Thompson,K., Jiao,X.,
            Pike,J.W., Medvedeva,V., Groszer,M., Kiledjian,M., Hart,R.P. and
            Rasin,M.R.
  TITLE     Thalamic WNT3 Secretion Spatiotemporally Regulates the Neocortical
            Ribosome Signature and mRNA Translation to Specify Neocortical Cell
            Subtypes
  JOURNAL   J Neurosci 35 (31), 10911-10926 (2015)
   PUBMED   26245956
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Roe,M.W., Worley,J.F. 3rd, Mittal,A.A., Kuznetsov,A., DasGupta,S.,
            Mertz,R.J., Witherspoon,S.M. 3rd, Blair,N., Lancaster,M.E.,
            McIntyre,M.S., Shehee,W.R., Dukes,I.D. and Philipson,L.H.
  TITLE     Expression and function of pancreatic beta-cell delayed rectifier
            K+ channels. Role in stimulus-secretion coupling
  JOURNAL   J Biol Chem 271 (50), 32241-32246 (1996)
   PUBMED   8943282
REFERENCE   7  (residues 1 to 642)
  AUTHORS   Lock,L.F., Gilbert,D.J., Street,V.A., Migeon,M.B., Jenkins,N.A.,
            Copeland,N.G. and Tempel,B.L.
  TITLE     Voltage-gated potassium channel genes are clustered in paralogous
            regions of the mouse genome
  JOURNAL   Genomics 20 (3), 354-362 (1994)
   PUBMED   8034307
REFERENCE   8  (residues 1 to 642)
  AUTHORS   Haas,M., Ward,D.C., Lee,J., Roses,A.D., Clarke,V., D'Eustachio,P.,
            Lau,D., Vega-Saenz de Miera,E. and Rudy,B.
  TITLE     Localization of Shaw-related K+ channel genes on mouse and human
            chromosomes
  JOURNAL   Mamm Genome 4 (12), 711-715 (1993)
   PUBMED   8111118
REFERENCE   9  (residues 1 to 642)
  AUTHORS   Klocke,R., Roberds,S.L., Tamkun,M.M., Gronemeier,M., Augustin,A.,
            Albrecht,B., Pongs,O. and Jockusch,H.
  TITLE     Chromosomal mapping in the mouse of eight K(+)-channel genes
            representing the four Shaker-like subfamilies Shaker, Shab, Shaw,
            and Shal
  JOURNAL   Genomics 18 (3), 568-574 (1993)
   PUBMED   7905852
REFERENCE   10 (residues 1 to 642)
  AUTHORS   Ghanshani,S., Pak,M., McPherson,J.D., Strong,M., Dethlefs,B.,
            Wasmuth,J.J., Salkoff,L., Gutman,G.A. and Chandy,K.G.
  TITLE     Genomic organization, nucleotide sequence, and cellular
            distribution of a Shaw-related potassium channel gene, Kv3.3, and
            mapping of Kv3.3 and Kv3.4 to human chromosomes 19 and 1
  JOURNAL   Genomics 12 (2), 190-196 (1992)
   PUBMED   1740329
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC116289.1, AC121610.2 and AI835316.1.
            
            On Jan 18, 2018 this sequence version replaced XP_006513751.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC116289.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 60.3 cM"
     Protein         1..642
                     /product="voltage-gated potassium channel KCNC2 isoform 1"
                     /note="potassium voltage-gated channel subfamily C member
                     2; voltage-gated potassium channel Kv3.2; shaw-like
                     potassium channel; voltage-gated potassium channel KCNC2"
                     /calculated_mol_wt=70372
     Region          7..170
                     /region_name="BTB_KCNC2_4"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     voltage-gated channel subfamily C members KCNC2 and KCNC4;
                     cd18415"
                     /db_xref="CDD:349722"
     Site            order(13,15..22,25,107,109..110,113,116,120,123,126,128,
                     136..137,140)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349722"
     Region          45..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14B80.1)"
     Region          232..488
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            234..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14B80.1)"
     Site            263
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14B80.1)"
     Site            270
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14B80.1)"
     Site            287..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14B80.1)"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14B80.1)"
     Site            350..372
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14B80.1)"
     Site            386..406
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14B80.1)"
     Region          441..446
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14B80.1)"
     Site            457..477
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14B80.1)"
     Region          542..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14B80.1)"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q14B80.1)"
     CDS             1..642
                     /gene="Kcnc2"
                     /gene_synonym="B230117I07; KShIIIA; Kv3.2"
                     /coded_by="NM_001359752.1:67..1995"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS88085.1"
                     /db_xref="GeneID:268345"
                     /db_xref="MGI:MGI:96668"
ORIGIN      
        1 mgkiesnerv ilnvggtrhe tyrstlktlp gtrlallass epqgdcltaa gdklqplppp
       61 lsppprpppl spvpsgcfeg gagncsshgg nggnggsdhp gggrefffdr hpgvfayvln
      121 yyrtgklhcp advcgplfee elafwgidet dvepccwmty rqhrdaeeal difetpdlig
      181 gdpgddedla akrlgiedaa glggpdgksg rwrklqprmw alfedpyssr aarfiafasl
      241 ffilvsittf cletheafni vknktepvin gtspvlqyei etdpaltyve gvcvvwftfe
      301 flvrivfspn klefiknlln iidfvailpf ylevglsgls skaakdvlgf lrvvrfvril
      361 rifkltrhfv glrvlghtlr astnefllli iflalgvlif atmiyyaerv gaqpndpsas
      421 ehtqfknipi gfwwavvtmt tlgygdmypq twsgmlvgal calagvltia mpvpvivnnf
      481 gmyyslamak qklprkrkkh ippaplassp tfcktelnma cnstqsdtcl gkenrllehn
      541 rsvlsgddst gsepplsppe rlpirrsstr dknrrgetcf llttgdytca sdggirkgye
      601 ksrslnniag lagnalrlsp vtspynspcp lrrsrspips il
//
LOCUS       NP_001348279             125 aa            linear   ROD 27-APR-2025
DEFINITION  syntaxin-8 isoform 3 [Mus musculus].
ACCESSION   NP_001348279
VERSION     NP_001348279.1
DBSOURCE    REFSEQ: accession NM_001361350.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Castonguay,J., Orth,J.H.C., Muller,T., Sleman,F., Grimm,C.,
            Wahl-Schott,C., Biel,M., Mallmann,R.T., Bildl,W., Schulte,U. and
            Klugbauer,N.
  TITLE     The two-pore channel TPC1 is required for efficient protein
            processing through early and recycling endosomes
  JOURNAL   Sci Rep 7 (1), 10038 (2017)
   PUBMED   28855648
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Raspa,M., Guan,M., Paoletti,R., Montoliu,L., Ayadi,A.,
            Marschall,S., Fray,M. and Scavizzi,F.
  CONSRTM   EMMA/Infrafrontier Technical Working Group
  TITLE     Dry ice is a reliable substrate for the distribution of frozen
            mouse spermatozoa: A multi-centric study
  JOURNAL   Theriogenology 96, 49-57 (2017)
   PUBMED   28532839
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Golebiewska,E.M., Harper,M.T., Williams,C.M., Savage,J.S.,
            Goggs,R., Fischer von Mollard,G. and Poole,A.W.
  TITLE     Syntaxin 8 regulates platelet dense granule secretion, aggregation,
            and thrombus stability
  JOURNAL   J Biol Chem 290 (3), 1536-1545 (2015)
   PUBMED   25404741
  REMARK    GeneRIF: Syntaxin 8 has a role in regulating platelet dense granule
            secretion, aggregation, and thrombus stability
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Pirooz,S.D., He,S., Zhang,T., Zhang,X., Zhao,Z., Oh,S.,
            O'Connell,D., Khalilzadeh,P., Amini-Bavil-Olyaee,S., Farzan,M. and
            Liang,C.
  TITLE     UVRAG is required for virus entry through combinatorial interaction
            with the class C-Vps complex and SNAREs
  JOURNAL   Proc Natl Acad Sci U S A 111 (7), 2716-2721 (2014)
   PUBMED   24550300
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Zhang,L., Kang,L., Bond,W. and Zhang,N.
  TITLE     Interaction between syntaxin 8 and HECTd3, a HECT domain ligase
  JOURNAL   Cell Mol Neurobiol 29 (1), 115-121 (2009)
   PUBMED   18821010
  REMARK    GeneRIF: Syntaxin 8 and HECTd3 have similar subcellular
            localization.
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Salazar,G., Craige,B., Styers,M.L., Newell-Litwa,K.A.,
            Doucette,M.M., Wainer,B.H., Falcon-Perez,J.M., Dell'Angelica,E.C.,
            Peden,A.A., Werner,E. and Faundez,V.
  TITLE     BLOC-1 complex deficiency alters the targeting of adaptor protein
            complex-3 cargoes
  JOURNAL   Mol Biol Cell 17 (9), 4014-4026 (2006)
   PUBMED   16760431
REFERENCE   9  (residues 1 to 125)
  AUTHORS   MacLaren,E.J., Bennett,B., Johnson,T.E. and Sikela,J.M.
  TITLE     Expression profiling identifies novel candidate genes for ethanol
            sensitivity QTLs
  JOURNAL   Mamm Genome 17 (2), 147-156 (2006)
   PUBMED   16465594
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Kim,B.Y., Ueda,M., Kominami,E., Akagawa,K., Kohsaka,S. and
            Akazawa,C.
  TITLE     Identification of mouse Vps16 and biochemical characterization of
            mammalian class C Vps complex
  JOURNAL   Biochem Biophys Res Commun 311 (3), 577-582 (2003)
   PUBMED   14623309
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL663076.17 and AL669842.11.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU841844.1, SRR7345562.636162.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 41.2 cM"
     Protein         1..125
                     /product="syntaxin-8 isoform 3"
                     /note="syntaxin-like protein 3I35"
                     /calculated_mol_wt=13975
     Region          41..95
                     /region_name="SNARE_Syntaxin8"
                     /note="SNARE motif of syntaxin 8; cd15852"
                     /db_xref="CDD:277205"
     Site            order(43..44,46..48,50..51,53..55,57..62,64..69,71..72,
                     74..76,78..80,82..83,85..87,89..90,92..94)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277205"
     Site            68
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277205"
     CDS             1..125
                     /gene="Stx8"
                     /gene_synonym="0610007H08Rik; 1110002H11Rik;
                     4930571E13Rik; CARB"
                     /coded_by="NM_001361350.1:171..548"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:55943"
                     /db_xref="MGI:MGI:1890156"
ORIGIN      
        1 mseeakrgtp npwlceepee trglgfdeir qqqqkiiqeq dagldalssi isrqkqmgqe
       61 igneldeqne iiddlanlve ntdeklrtea rrvtlvdrks tscgmimvil lllvaivvva
      121 vwptn
//
LOCUS       NP_003633                419 aa            linear   PRI 27-APR-2025
DEFINITION  histone acetyltransferase type B catalytic subunit [Homo sapiens].
ACCESSION   NP_003633
VERSION     NP_003633.2
DBSOURCE    REFSEQ: accession NM_003642.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Kou,F., Wu,L., Zheng,Y., Yi,Y., Ji,Z., Huang,Z., Guo,S. and Yang,L.
  TITLE     HMGB1/SET/HAT1 complex-mediated SASH1 repression drives glycolysis
            and metastasis in lung adenocarcinoma
  JOURNAL   Oncogene 42 (46), 3407-3421 (2023)
   PUBMED   37794134
  REMARK    GeneRIF: HMGB1/SET/HAT1 complex-mediated SASH1 repression drives
            glycolysis and metastasis in lung adenocarcinoma.
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Guo,B., Zhang,S., Wang,S., Zhang,H., Fang,J., Kang,N., Zhen,X.,
            Zhang,Y., Zhou,J., Yan,G., Sun,H., Ding,L. and Liu,C.
  TITLE     Decreased HAT1 expression in granulosa cells disturbs oocyte
            meiosis during mouse ovarian aging
  JOURNAL   Reprod Biol Endocrinol 21 (1), 103 (2023)
   PUBMED   37907924
  REMARK    GeneRIF: Decreased HAT1 expression in granulosa cells disturbs
            oocyte meiosis during mouse ovarian aging.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Ortega,M.A., De Leon-Oliva,D., Garcia-Montero,C.,
            Fraile-Martinez,O., Boaru,D.L., Del Val Toledo Lobo,M.,
            Garcia-Tunon,I., Royuela,M., Garcia-Honduvilla,N., Bujan,J.,
            Guijarro,L.G., Alvarez-Mon,M. and Alvarez-Mon,M.A.
  TITLE     Understanding HAT1: A Comprehensive Review of Noncanonical Roles
            and Connection with Disease
  JOURNAL   Genes (Basel) 14 (4), 915 (2023)
   PUBMED   37107673
  REMARK    GeneRIF: Understanding HAT1: A Comprehensive Review of Noncanonical
            Roles and Connection with Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Capone,V., Della Torre,L., Carannante,D., Babaei,M., Altucci,L.,
            Benedetti,R. and Carafa,V.
  TITLE     HAT1: Landscape of Biological Function and Role in Cancer
  JOURNAL   Cells 12 (7), 1075 (2023)
   PUBMED   37048148
  REMARK    GeneRIF: HAT1: Landscape of Biological Function and Role in Cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Sarkar,T., Dhar,S., Chakraborty,D., Pati,S., Bose,S., Panda,A.K.,
            Basak,U., Chakraborty,S., Mukherjee,S., Guin,A., Jana,K.,
            Sarkar,D.K. and Sa,G.
  TITLE     FOXP3/HAT1 Axis Controls Treg Infiltration in the Tumor
            Microenvironment by Inducing CCR4 Expression in Breast Cancer
  JOURNAL   Front Immunol 13, 740588 (2022)
   PUBMED   35222362
  REMARK    GeneRIF: FOXP3/HAT1 Axis Controls Treg Infiltration in the Tumor
            Microenvironment by Inducing CCR4 Expression in Breast Cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Tagami,H., Ray-Gallet,D., Almouzni,G. and Nakatani,Y.
  TITLE     Histone H3.1 and H3.3 complexes mediate nucleosome assembly
            pathways dependent or independent of DNA synthesis
  JOURNAL   Cell 116 (1), 51-61 (2004)
   PUBMED   14718166
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Makowski,A.M., Dutnall,R.N. and Annunziato,A.T.
  TITLE     Effects of acetylation of histone H4 at lysines 8 and 16 on
            activity of the Hat1 histone acetyltransferase
  JOURNAL   J Biol Chem 276 (47), 43499-43502 (2001)
   PUBMED   11585814
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Marmorstein,R.
  TITLE     Structure of histone acetyltransferases
  JOURNAL   J Mol Biol 311 (3), 433-444 (2001)
   PUBMED   11492997
  REMARK    Review article
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Verreault,A., Kaufman,P.D., Kobayashi,R. and Stillman,B.
  TITLE     Nucleosomal DNA regulates the core-histone-binding subunit of the
            human Hat1 acetyltransferase
  JOURNAL   Curr Biol 8 (2), 96-108 (1998)
   PUBMED   9427644
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114745.6.
            
            On Nov 23, 2018 this sequence version replaced NP_003633.1.
            
            Summary: The protein encoded by this gene is a type B histone
            acetyltransferase (HAT) that is involved in the rapid acetylation
            of newly synthesized cytoplasmic histones, which are in turn
            imported into the nucleus for de novo deposition onto nascent DNA
            chains. Histone acetylation, particularly of histone H4, plays an
            important role in replication-dependent chromatin assembly.
            Specifically, this HAT can acetylate soluble but not nucleosomal
            histone H4 at lysines 5 and 12, and to a lesser degree, histone H2A
            at lysine 5. Alternatively spliced transcript variants have been
            identified for this gene. [provided by RefSeq, Jun 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.357536.1,
                                           SRR1803611.237430.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264108.5/ ENSP00000264108.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..419
                     /product="histone acetyltransferase type B catalytic
                     subunit"
                     /EC_number="2.3.1.48"
                     /calculated_mol_wt=49410
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (O14929.2)"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BY71; propagated from
                     UniProtKB/Swiss-Prot (O14929.2)"
     Site            15
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BY71; propagated from
                     UniProtKB/Swiss-Prot (O14929.2)"
     Region          25..187
                     /region_name="Hat1_N"
                     /note="Histone acetyl transferase HAT1 N-terminus;
                     pfam10394"
                     /db_xref="CDD:463071"
     Region          62..64
                     /region_name="Interaction with histone H4 N-terminus.
                     /evidence=ECO:0000269|PubMed:22615379"
                     /note="propagated from UniProtKB/Swiss-Prot (O14929.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:28143904; propagated from
                     UniProtKB/Swiss-Prot (O14929.2)"
     Site            199
                     /site_type="other"
                     /note="Interaction with histone H4 N-terminus.
                     /evidence=ECO:0000269|PubMed:22615379; propagated from
                     UniProtKB/Swiss-Prot (O14929.2)"
     Region          225..227
                     /region_name="Interaction with histone H4 N-terminus.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O14929.2)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14929.2)"
     CDS             1..419
                     /gene="HAT1"
                     /gene_synonym="KAT1"
                     /coded_by="NM_003642.4:41..1300"
                     /db_xref="CCDS:CCDS2245.1"
                     /db_xref="GeneID:8520"
                     /db_xref="HGNC:HGNC:4821"
                     /db_xref="MIM:603053"
ORIGIN      
        1 magfgamekf lveyksavek klaeykcntn taielklvrf pedlendirt ffpeythqlf
       61 gddetafgyk glkillyyia gslstmfrve yaskvdenfd cveaddvegk irqiippgfc
      121 tntndflsll ekevdfkpfg tllhtysvls ptggenftfq iykadmtcrg freyherlqt
      181 flmwfietas fidvdderwh yflvfekynk dgatlfatvg ymtvynyyvy pdktrprvsq
      241 mliltpfqgq ghgaqlletv hryytefptv lditaedpsk syvklrdfvl vklcqdlpcf
      301 sreklmqgfn edmvieaqqk fkinkqharr vyeilrllvt dmsdaeqyrs yrldikrrli
      361 spykkkqrdl akmrkclrpe eltnqmnqie ismqheqlee sfqelvedyr rvierlaqe
//
LOCUS       NP_071736                243 aa            linear   PRI 27-APR-2025
DEFINITION  peptide deformylase, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_071736
VERSION     NP_071736.1
DBSOURCE    REFSEQ: accession NM_022341.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Gao,J., Wang,T., Qiu,S., Zhu,Y., Liang,L. and Zheng,Y.
  TITLE     Structure-Based Drug Design of Small Molecule Peptide Deformylase
            Inhibitors to Treat Cancer
  JOURNAL   Molecules 21 (4), 396 (2016)
   PUBMED   27023495
  REMARK    GeneRIF: compound M7594_0037 exhibited potent anticancer activities
            against HeLa, A549 and MCF-7 cell lines with IC50s of 35.26, 29.63
            and 24.63 muM, respectively. Molecular docking studies suggested
            that M7594_0037 and its three derivatives could interact with Human
            peptide deformylase by several conserved hydrogen bonds.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Sheth,A., Escobar-Alvarez,S., Gardner,J., Ran,L., Heaney,M.L. and
            Scheinberg,D.A.
  TITLE     Inhibition of human mitochondrial peptide deformylase causes
            apoptosis in c-myc-overexpressing hematopoietic cancers
  JOURNAL   Cell Death Dis 5 (3), e1152 (2014)
   PUBMED   24675470
  REMARK    GeneRIF: c-myc regulated the expression of human PDF.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Randhawa,H., Chikara,S., Gehring,D., Yildirim,T., Menon,J. and
            Reindl,K.M.
  TITLE     Overexpression of peptide deformylase in breast, colon, and lung
            cancers
  JOURNAL   BMC Cancer 13, 321 (2013)
   PUBMED   23815882
  REMARK    GeneRIF: This is the first report showing that PDF is
            over-expressed in breast, colon, and lung cancers
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Pereira-Castro,I., Costa,L.T., Amorim,A. and Azevedo,L.
  TITLE     Transcriptional regulation of the human mitochondrial peptide
            deformylase (PDF)
  JOURNAL   Biochem Biophys Res Commun 421 (4), 825-831 (2012)
   PUBMED   22554513
  REMARK    GeneRIF: these data reveals that PDF has several transcription
            start sites, the most important of which only 18 bp from the
            initiation codon.
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Serero,A., Giglione,C., Sardini,A., Martinez-Sanz,J. and Meinnel,T.
  TITLE     An unusual peptide deformylase features in the human mitochondrial
            N-terminal methionine excision pathway
  JOURNAL   J Biol Chem 278 (52), 52953-52963 (2003)
   PUBMED   14532271
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Lee,M.D., Antczak,C., Li,Y., Sirotnak,F.M., Bornmann,W.G. and
            Scheinberg,D.A.
  TITLE     A new human peptide deformylase inhibitable by actinonin
  JOURNAL   Biochem Biophys Res Commun 312 (2), 309-315 (2003)
   PUBMED   14637138
  REMARK    GeneRIF: The inhibition of HsPDF may provide an explanation for the
            mechanism by which actinonin is cytotoxic against various human
            tumor cell lines.
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Nguyen,K.T., Hu,X., Colton,C., Chakrabarti,R., Zhu,M.X. and Pei,D.
  TITLE     Characterization of a human peptide deformylase: implications for
            antibacterial drug design
  JOURNAL   Biochemistry 42 (33), 9952-9958 (2003)
   PUBMED   12924944
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Chagnon,P., Michaud,J., Mitchell,G., Mercier,J., Marion,J.F.,
            Drouin,E., Rasquin-Weber,A., Hudson,T.J. and Richter,A.
  TITLE     A missense mutation (R565W) in cirhin (FLJ14728) in North American
            Indian childhood cirrhosis
  JOURNAL   Am J Hum Genet 71 (6), 1443-1449 (2002)
   PUBMED   12417987
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Giglione,C., Serero,A., Pierre,M., Boisson,B. and Meinnel,T.
  TITLE     Identification of eukaryotic peptide deformylases reveals
            universality of N-terminal protein processing mechanisms
  JOURNAL   EMBO J 19 (21), 5916-5929 (2000)
   PUBMED   11060042
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF239156.1 and AC026464.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Protein synthesis proceeds after formylation of methionine
            by methionyl-tRNA formyl transferase (FMT) and transfer of the
            charged initiator f-met tRNA to the ribosome. In eubacteria and
            eukaryotic organelles the product of this gene, peptide deformylase
            (PDF), removes the formyl group from the initiating methionine of
            nascent peptides. In eubacteria, deformylation of nascent peptides
            is required for subsequent cleavage of initiating methionines by
            methionine aminopeptidase. The discovery that a natural inhibitor
            of PDF, actinonin, acts as an antimicrobial agent in some bacteria
            has spurred intensive research into the design of
            bacterial-specific PDF inhibitors. In human cells, only
            mitochondrial proteins have N-formylation of initiating
            methionines. Protein inhibitors of PDF or siRNAs of PDF block the
            growth of cancer cell lines but have no effect on normal cell
            growth. In humans, PDF function may therefore be restricted to
            rapidly growing cells. [provided by RefSeq, Nov 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.381020.1, AF239156.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000288022.2/
                                                  ENSP00000288022.1
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..243
                     /product="peptide deformylase, mitochondrial precursor"
                     /EC_number="3.5.1.88"
                     /note="peptide deformylase-like protein; polypeptide
                     deformylase"
                     /calculated_mol_wt=19472
     transit_peptide 1..70
                     /note="mitochondrial targeting sequence"
                     /calculated_mol_wt=7560
     Region          67..224
                     /region_name="Pep_deformylase"
                     /note="Polypeptide or peptide deformylase; a family of
                     metalloenzymes that catalyzes the removal of the
                     N-terminal formyl group in a growing polypeptide chain
                     following translation initiation during protein synthesis
                     in prokaryotes. These enzymes utilize Fe(II)...; cd00487"
                     /db_xref="CDD:238271"
     mat_peptide     71..243
                     /product="peptide deformylase, mitochondrial"
                     /calculated_mol_wt=19472
     Site            order(108..110,115,171..173,214..215,218)
                     /site_type="active"
                     /db_xref="CDD:238271"
     Site            order(110,115,173,215)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238271"
     Region          165..175
                     /region_name="Hydrophobic dimerization interface.
                     /evidence=ECO:0000269|PubMed:19236878"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBH1.1)"
     Site            order(172,214,218)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:238271"
     CDS             1..243
                     /gene="PDF"
                     /coded_by="NM_022341.2:19..750"
                     /db_xref="CCDS:CCDS10875.1"
                     /db_xref="GeneID:64146"
                     /db_xref="HGNC:HGNC:30012"
                     /db_xref="MIM:618720"
ORIGIN      
        1 marlwgalsl wplwaavpwg gaaavgvrac sstaapdgve gpalrrsywr hlrrlvlgpp
       61 eppfshvcqv gdpvlrgvaa pveraqlggp elqrltqrlv qvmrrrrcvg lsapqlgvpr
      121 qvlalelpea lcrecpprqr alrqmepfpl rvfvnpslrv ldsrlvtfpe gcesvagfla
      181 cvprfqavqi sgldpngeqv vwqasgwaar iiqhemdhlq gclfidkmds rtftnvywmk
      241 vnd
//
LOCUS       NP_080902                164 aa            linear   ROD 27-APR-2025
DEFINITION  dynein regulatory complex protein 8 [Mus musculus].
ACCESSION   NP_080902
VERSION     NP_080902.1
DBSOURCE    REFSEQ: accession NM_026626.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Shawki,H.H., Ishikawa-Yamauchi,Y., Kawashima,A., Katoh,Y.,
            Matsuda,M., Al-Soudy,A.S., Minisy,F.M., Kuno,A., Gulibaikelamu,X.,
            Hirokawa,T., Takahashi,S. and Oishi,H.
  TITLE     EFCAB2 is a novel calcium-binding protein in mouse testis and sperm
  JOURNAL   PLoS One 14 (4), e0214687 (2019)
   PUBMED   30933994
  REMARK    GeneRIF: EFCAB2 is a novel calcium-binding protein in mouse testis
            and sperm.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Lewandowski,J.P., Du,F., Zhang,S., Powell,M.B., Falkenstein,K.N.,
            Ji,H. and Vokes,S.A.
  TITLE     Spatiotemporal regulation of GLI target genes in the mammalian limb
            bud
  JOURNAL   Dev Biol 406 (1), 92-103 (2015)
   PUBMED   26238476
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC157809.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK029880.1, BC025062.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 83.16 cM"
     Protein         1..164
                     /product="dynein regulatory complex protein 8"
                     /note="EF-hand calcium-binding domain-containing protein
                     2"
                     /calculated_mol_wt=18798
     Region          10..160
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     CDS             1..164
                     /gene="Efcab2"
                     /gene_synonym="1700073K01Rik; D830011E08Rik"
                     /coded_by="NM_026626.3:86..580"
                     /db_xref="CCDS:CCDS15557.1"
                     /db_xref="GeneID:68226"
                     /db_xref="MGI:MGI:1915476"
ORIGIN      
        1 maeerdaegt ealiaelhkk ikdafevfdh esnntvdvre igtiirslgc cptegelhdf
       61 iaeieeeept gyirfekfip vmtralverr yrpaaedill rafevldpak rgfltkdelv
      121 kymteegepf sqeemeemls aaidpesnti nyrdyitmmv vden
//
LOCUS       NP_835224                696 aa            linear   PRI 27-APR-2025
DEFINITION  SEC14 domain and spectrin repeat-containing protein 1 [Homo
            sapiens].
ACCESSION   NP_835224
VERSION     NP_835224.3
DBSOURCE    REFSEQ: accession NM_178123.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Fujiwara,S., Matsui,T.S., Ohashi,K., Deguchi,S. and Mizuno,K.
  TITLE     Solo, a RhoA-targeting guanine nucleotide exchange factor, is
            critical for hemidesmosome formation and acinar development in
            epithelial cells
  JOURNAL   PLoS One 13 (4), e0195124 (2018)
   PUBMED   29672603
  REMARK    GeneRIF: Solo plays a crucial role in HD formation and acinar
            development in epithelial cells by regulating mechanical
            force-induced RhoA activation and keratin filament organization.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 696)
  AUTHORS   Fujiwara,S., Ohashi,K., Mashiko,T., Kondo,H. and Mizuno,K.
  TITLE     Interplay between Solo and keratin filaments is crucial for
            mechanical force-induced stress fiber reinforcement
  JOURNAL   Mol Biol Cell 27 (6), 954-966 (2016)
   PUBMED   26823019
  REMARK    GeneRIF: The interplay between Solo protein and keratin 8/keratin
            18 filaments plays a crucial role in tensile force-induced RhoA
            activation and consequent actin cytoskeletal reinforcement in
            endothelial cells.
REFERENCE   5  (residues 1 to 696)
  AUTHORS   Slonchak,A., Shannon,R.P., Pali,G. and Khromykh,A.A.
  TITLE     Human MicroRNA miR-532-5p Exhibits Antiviral Activity against West
            Nile Virus via Suppression of Host Genes SESTD1 and TAB3 Required
            for Virus Replication
  JOURNAL   J Virol 90 (5), 2388-2402 (2015)
   PUBMED   26676784
  REMARK    GeneRIF: Upregulation of miR-532-5p and subsequent suppression of
            the SESTD1 and TAB3 genes represent an antiviral response aimed at
            limiting West Nile virus infection.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 696)
  AUTHORS   Kamboh,M.I., Wang,X., Kao,A.H., Barmada,M.M., Clarke,A.,
            Ramsey-Goldman,R., Manzi,S. and Demirci,F.Y.
  TITLE     Genome-wide association study of antiphospholipid antibodies
  JOURNAL   Autoimmune Dis 2013, 761046 (2013)
   PUBMED   23509613
REFERENCE   7  (residues 1 to 696)
  AUTHORS   Miehe,S., Bieberstein,A., Arnould,I., Ihdene,O., Rutten,H. and
            Strubing,C.
  TITLE     The phospholipid-binding protein SESTD1 is a novel regulator of the
            transient receptor potential channels TRPC4 and TRPC5
  JOURNAL   J Biol Chem 285 (16), 12426-12434 (2010)
   PUBMED   20164195
  REMARK    GeneRIF: SESTD1 was found to associate with TRPC4 and TRPC5 via the
            channel's calmodulin- and inositol 1,4,5-trisphosphate
            receptor-binding domain.
REFERENCE   8  (residues 1 to 696)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 696)
  AUTHORS   Sato,T. and Mishina,M.
  TITLE     Representational difference analysis, high-resolution physical
            mapping, and transcript identification of the zebrafish genomic
            region for a motor behavior
  JOURNAL   Genomics 82 (2), 218-229 (2003)
   PUBMED   12837271
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093911.2, BC047578.1, AY209190.1, AK096232.1 and AC016755.6.
            
            On May 17, 2008 this sequence version replaced NP_835224.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3673092.1, BC047578.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000428443.8/ ENSP00000415332.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.2"
     Protein         1..696
                     /product="SEC14 domain and spectrin repeat-containing
                     protein 1"
                     /note="huntingtin-interacting protein-like protein;
                     protein Solo; SEC14 and spectrin domains 1"
                     /calculated_mol_wt=79218
     Region          33..153
                     /region_name="CRAL_TRIO_2"
                     /note="Divergent CRAL/TRIO domain; pfam13716"
                     /db_xref="CDD:463965"
     Region          273..478
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Region          275..378
                     /region_name="Spectrin 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VW0.2)"
     Region          381..494
                     /region_name="Spectrin 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VW0.2)"
     Region          413..605
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Site            496..501
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          500..602
                     /region_name="Spectrin 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VW0.2)"
     CDS             1..696
                     /gene="SESTD1"
                     /gene_synonym="Solo"
                     /coded_by="NM_178123.5:360..2450"
                     /db_xref="CCDS:CCDS33338.1"
                     /db_xref="GeneID:91404"
                     /db_xref="HGNC:HGNC:18379"
                     /db_xref="MIM:621011"
ORIGIN      
        1 measvilpil kkklaflsgg kdrrsglilt iplcleqtnm delsvtldyl lsipsekcka
       61 rgftvivdgr ksqwnvvktv vvmlqnvvpa evslvcvvkp defwdkkvth fcfwkekdrl
      121 gfevilvsan kltryiepcq ltedfggslt ydhmdwlnkr lvfekftkes tslldelali
      181 nngsdkgnqq ekersvdlnf lpsvdpetvl qtghellsel qqrrfngsdg gvswspmdde
      241 llaqpqvmkl ldslreqytr yqevcrqrsk rtqleeiqqk vmqvvnwleg pgseqlraqw
      301 gigdsirasq alqqkheeie sqhsewfavy velnqqiaal lnagdeedlv elkslqqqls
      361 dvcyrqasql efrqnllqaa lefhgvaqdl sqqldgllgm lcvdvapadg asiqqtlkll
      421 eeklksvdvg lqglrekgqg lldqisnqas waygkdvtie nkenvdhiqg vmedmqlrkq
      481 rcedmvdvrr lkmlqmvqlf kceedaaqav ewlselldal lkthirlgdd aqetkvllek
      541 hrkfvdvaqs tydygrqllq atvvlcqslr ctsrssgdtl prlnrvwkqf tiaseervhr
      601 lemaiafhsn aekilqdcpe epeaindeeq fdeieavgks lldrltvpvv ypdgteqyfg
      661 spsdmastae nirdrmklvn lkrqqlrhpe mvttes
//
LOCUS       NP_001350713             197 aa            linear   PRI 27-APR-2025
DEFINITION  potassium channel subfamily K member 16 isoform 5 [Homo sapiens].
ACCESSION   NP_001350713 XP_011513237
VERSION     NP_001350713.1
DBSOURCE    REFSEQ: accession NM_001363784.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Khoubza,L., Gilbert,N., Kim,E.J., Chatelain,F.C., Feliciangeli,S.,
            Abelanet,S., Kang,D., Lesage,F. and Bichet,D.
  TITLE     Alkaline-sensitive two-pore domain potassium channels form
            functional heteromers in pancreatic beta-cells
  JOURNAL   J Biol Chem 298 (10), 102447 (2022)
   PUBMED   36063992
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Graff,S.M., Johnson,S.R., Leo,P.J., Dadi,P.K., Dickerson,M.T.,
            Nakhe,A.Y., McInerney-Leo,A.M., Marshall,M., Zaborska,K.E.,
            Schaub,C.M., Brown,M.A., Jacobson,D.A. and Duncan,E.L.
  TITLE     A KCNK16 mutation causing TALK-1 gain of function is associated
            with maturity-onset diabetes of the young
  JOURNAL   JCI Insight 6 (13), 138057 (2021)
   PUBMED   34032641
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Vierra,N.C., Dadi,P.K., Milian,S.C., Dickerson,M.T., Jordan,K.L.,
            Gilon,P. and Jacobson,D.A.
  TITLE     TALK-1 channels control beta cell endoplasmic reticulum Ca2+
            homeostasis
  JOURNAL   Sci Signal 10 (497) (2017)
   PUBMED   28928238
  REMARK    GeneRIF: data establish TALK-1 channels as key regulators of beta
            cell ER Ca(2+) and suggest that TALK-1 may be a therapeutic target
            to reduce ER Ca(2+) handling defects in beta cells during the
            pathogenesis of diabetes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Dickerson,M.T., Vierra,N.C., Milian,S.C., Dadi,P.K. and
            Jacobson,D.A.
  TITLE     Osteopontin activates the diabetes-associated potassium channel
            TALK-1 in pancreatic beta-cells
  JOURNAL   PLoS One 12 (4), e0175069 (2017)
   PUBMED   28403169
  REMARK    GeneRIF: The TALK-1/iOPN complex caused Vm hyperpolarization and
            reduced beta-cell glucose-stimulated Ca2+ influx, which is
            predicted to inhibit glucose stimulated insulin secretion.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Schewe,M., Nematian-Ardestani,E., Sun,H., Musinszki,M.,
            Cordeiro,S., Bucci,G., de Groot,B.L., Tucker,S.J., Rapedius,M. and
            Baukrowitz,T.
  TITLE     A Non-canonical Voltage-Sensing Mechanism Controls Gating in K2P
            K(+) Channels
  JOURNAL   Cell 164 (5), 937-949 (2016)
   PUBMED   26919430
REFERENCE   6  (residues 1 to 197)
  AUTHORS   Goldstein,S.A., Bayliss,D.A., Kim,D., Lesage,F., Plant,L.D. and
            Rajan,S.
  TITLE     International Union of Pharmacology. LV. Nomenclature and molecular
            relationships of two-P potassium channels
  JOURNAL   Pharmacol Rev 57 (4), 527-540 (2005)
   PUBMED   16382106
  REMARK    Review article
REFERENCE   7  (residues 1 to 197)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   8  (residues 1 to 197)
  AUTHORS   Han,J., Kang,D. and Kim,D.
  TITLE     Functional properties of four splice variants of a human pancreatic
            tandem-pore K+ channel, TALK-1
  JOURNAL   Am J Physiol Cell Physiol 285 (3), C529-C538 (2003)
   PUBMED   12724142
  REMARK    GeneRIF: at least two functional TALK-1 variants are present and
            may serve as background K+ currents in certain cells of the human
            pancreas.
REFERENCE   9  (residues 1 to 197)
  AUTHORS   Girard,C., Duprat,F., Terrenoire,C., Tinel,N., Fosset,M., Romey,G.,
            Lazdunski,M. and Lesage,F.
  TITLE     Genomic and functional characteristics of novel human pancreatic 2P
            domain K(+) channels
  JOURNAL   Biochem Biophys Res Commun 282 (1), 249-256 (2001)
   PUBMED   11263999
REFERENCE   10 (residues 1 to 197)
  AUTHORS   Goldstein,S.A., Bockenhauer,D., O'Kelly,I. and Zilberberg,N.
  TITLE     Potassium leak channels and the KCNK family of two-P-domain
            subunits
  JOURNAL   Nat Rev Neurosci 2 (3), 175-184 (2001)
   PUBMED   11256078
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136087.12.
            
            On Jun 3, 2018 this sequence version replaced XP_011513237.1.
            
            Summary: The protein encoded by this gene belongs to the family of
            potassium channel proteins containing two pore-forming P domains.
            This channel is an open rectifier which primarily passes outward
            current under physiological K+ concentrations. This gene is
            expressed predominantly in the pancreas and is activated at
            alkaline pH. Several alternatively spliced transcript variants
            encoding different isoforms have been identified for this gene.
            [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            coding sequence and in the 3' UTR and coding sequence compared to
            variant 1. The resulting isoform (5) is shorter at the N-terminus
            and has a shorter and distinct C-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ925824.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2142586,
                                           SAMEA2144120 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..197
                     /product="potassium channel subfamily K member 16 isoform
                     5"
                     /note="TWIK-related alkaline pH-activated K(+) channel 1;
                     2P domain potassium channel Talk-1; pancreatic potassium
                     channel Talk-1; potassium channel, subfamily K, member 16;
                     potassium channel, two pore domain subfamily K, member 16"
                     /calculated_mol_wt=21260
     Region          22..80
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          115..>154
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     CDS             1..197
                     /gene="KCNK16"
                     /gene_synonym="K2p16.1; TALK-1; TALK1"
                     /coded_by="NM_001363784.1:242..835"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS87391.1"
                     /db_xref="GeneID:83795"
                     /db_xref="HGNC:HGNC:14464"
                     /db_xref="MIM:607369"
ORIGIN      
        1 meqfvqvime awvkgvnpkg nstnpsnwdf gssfffagtv vttigygnla psteagqvfc
       61 vfyallgipl nviflnhlgt glrahlaaie rwedrprrsq vlqvlglalf ltlgtlvili
      121 fppmvfshve gwsfsegfyf afitlstigf gdyvvglrqg cgakaapgrr prrgstaarg
      181 vqvtpqdfpi skkglgs
//
LOCUS       NP_003421               1191 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 91 isoform 1 [Homo sapiens].
ACCESSION   NP_003421
VERSION     NP_003421.2
DBSOURCE    REFSEQ: accession NM_003430.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1191)
  AUTHORS   Zeng,Z., Zhao,Y., Chen,Q., Zhu,S., Niu,Y., Ye,Z., Hu,P., Chen,D.,
            Xu,P., Chen,J., Hu,C., Hu,Y., Xu,F., Tang,J., Wang,F., Han,S.,
            Huang,M., Wang,C. and Zhao,G.
  TITLE     Hypoxic exosomal HIF-1alpha-stabilizing circZNF91 promotes
            chemoresistance of normoxic pancreatic cancer cells via enhancing
            glycolysis
  JOURNAL   Oncogene 40 (36), 5505-5517 (2021)
   PUBMED   34294845
  REMARK    GeneRIF: Hypoxic exosomal HIF-1alpha-stabilizing circZNF91 promotes
            chemoresistance of normoxic pancreatic cancer cells via enhancing
            glycolysis.
REFERENCE   2  (residues 1 to 1191)
  AUTHORS   Jacobs,F.M., Greenberg,D., Nguyen,N., Haeussler,M., Ewing,A.D.,
            Katzman,S., Paten,B., Salama,S.R. and Haussler,D.
  TITLE     An evolutionary arms race between KRAB zinc-finger genes ZNF91/93
            and SVA/L1 retrotransposons
  JOURNAL   Nature 516 (7530), 242-245 (2014)
   PUBMED   25274305
REFERENCE   3  (residues 1 to 1191)
  AUTHORS   Wang,W., Cai,J., Wu,Y., Hu,L., Chen,Z., Hu,J., Chen,Z., Li,W.,
            Guo,M. and Huang,Z.
  TITLE     Novel activity of KRAB domain that functions to reinforce nuclear
            localization of KRAB-containing zinc finger proteins by interacting
            with KAP1
  JOURNAL   Cell Mol Life Sci 70 (20), 3947-3958 (2013)
   PUBMED   23665872
REFERENCE   4  (residues 1 to 1191)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 1191)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 1191)
  AUTHORS   Tsang,H.T., Connell,J.W., Brown,S.E., Thompson,A., Reid,E. and
            Sanderson,C.M.
  TITLE     A systematic analysis of human CHMP protein interactions:
            additional MIT domain-containing proteins bind to multiple
            components of the human ESCRT III complex
  JOURNAL   Genomics 88 (3), 333-346 (2006)
   PUBMED   16730941
REFERENCE   7  (residues 1 to 1191)
  AUTHORS   Nishimura,T., Narita,T., Miyazaki,E., Ito,T., Nishimoto,N.,
            Yoshizaki,K., Martial,J.A., Bellfroid,E.J., Vissing,H. and
            Taniyama,T.
  TITLE     Characterization of the human Fc gamma RIIB gene promoter: human
            zinc-finger proteins (ZNF140 and ZNF91) that bind to different
            regions function as transcription repressors
  JOURNAL   Int Immunol 13 (8), 1075-1084 (2001)
   PUBMED   11470777
REFERENCE   8  (residues 1 to 1191)
  AUTHORS   Bellefroid,E.J., Marine,J.C., Ried,T., Lecocq,P.J., Riviere,M.,
            Amemiya,C., Poncelet,D.A., Coulie,P.G., de Jong,P., Szpirer,C. et
            al.
  TITLE     Clustered organization of homologous KRAB zinc-finger genes with
            enhanced expression in human T lymphoid cells
  JOURNAL   EMBO J 12 (4), 1363-1374 (1993)
   PUBMED   8467795
REFERENCE   9  (residues 1 to 1191)
  AUTHORS   Bellefroid,E.J., Poncelet,D.A., Lecocq,P.J., Revelant,O. and
            Martial,J.A.
  TITLE     The evolutionarily conserved Kruppel-associated box domain defines
            a subfamily of eukaryotic multifingered proteins
  JOURNAL   Proc Natl Acad Sci U S A 88 (9), 3608-3612 (1991)
   PUBMED   2023909
REFERENCE   10 (residues 1 to 1191)
  AUTHORS   Bellefroid,E.J., Lecocq,P.J., Benhida,A., Poncelet,D.A., Belayew,A.
            and Martial,J.A.
  TITLE     The human genome contains hundreds of genes coding for finger
            proteins of the Kruppel type
  JOURNAL   DNA 8 (6), 377-387 (1989)
   PUBMED   2505992
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB068854.1, AK291256.1, AK300294.1, L11672.1, AC016628.6,
            AC010300.8 and AI590336.1.
            
            On Dec 2, 2006 this sequence version replaced NP_003421.1.
            
            Summary: The ZNF91 gene encodes a zinc finger protein of the KRAB
            (Kruppel-associated box) subfamily (Bellefroid et al., 1991, 1993
            [PubMed 2023909] [PubMed 8467795]).[supplied by OMIM, May 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.271042.1, AK291256.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300619.12/ ENSP00000300619.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p12"
     Protein         1..1191
                     /product="zinc finger protein 91 isoform 1"
                     /note="zinc finger protein 91 (HPF7, HTF10); zinc finger
                     protein HTF10; zinc finger protein HPF7"
                     /calculated_mol_wt=137087
     Region          13..73
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          155..176
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          212..232
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          240..260
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          268..288
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(273,275,277,279..280,283..284,287,301,303,307..308,
                     311..312,315,329,331,333,335..336,339..340,343)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          281..305
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          296..316
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          320..708
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          324..344
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          352..372
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          380..400
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          408..428
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(413,415,417,419..420,423..424,427,441,443,447..448,
                     451..452,455,469,471,473,475..476,479..480,483)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          436..456
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          464..484
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          492..512
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          520..540
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          548..568
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          576..596
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          604..624
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(609,611,613,615..616,619..620,623,637,639,643..644,
                     647..648,651,665,667,669,671..672,675..676,679)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          628..1069
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          632..652
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          660..680
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          688..708
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          716..736
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          744..764
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(749,751,753,755..756,759..760,763,777,779,783..784,
                     787..788,791,805,807,809,811..812,815..816,819)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          772..792
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          800..820
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          828..848
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          856..876
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          885..904
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          912..932
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          940..960
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(945,947,949,951..952,955..956,959,973,975,979..980,
                     983..984,987,1001,1003,1005,1007..1008,1011..1012,1015)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          968..988
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          996..1016
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1024..1044
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1052..1072
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <1075..1154
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          1080..1100
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1108..1128
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1136..1156
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1191
                     /gene="ZNF91"
                     /gene_synonym="HPF7; HTF10"
                     /coded_by="NM_003430.4:118..3693"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42541.1"
                     /db_xref="GeneID:7644"
                     /db_xref="HGNC:HGNC:13166"
                     /db_xref="MIM:603971"
ORIGIN      
        1 mpgtpgslem glltfrdvai efspeewqcl dtaqqnlyrn vmlenyrnla flgialskpd
       61 lityleqgke pwnmkqhemv deptgicphf pqdfwpeqsm edsfqkvllr kyekcghenl
      121 qlrkgcksvd eckvhkegyn klnqclttaq skvfqcgkyl kvfykflnsn rhtirhtgkk
      181 cfkckkcvks fcirlhktqh kcvyiteksc kckecektfh wsstltnhke ihtedkpykc
      241 eecgkafkql stltthkiic akekiykcee cgkaflwsst ltrhkrihtg ekpykceecg
      301 kafshsstla khkrihtgek pykceecgka fsrsstlakh krihtgekpy kckecgkafs
      361 nsstlanhki thteekpykc kecdkafkrl stltkhkiih ageklykcee cgkafnrssn
      421 ltihkfihtg ekpykceecg kafnwssslt khkrfhtrek pfkckecgka fiwsstltrh
      481 krihtgekpy kceecgkafr qsstltkhki ihtgekpykf eecgkafrqs ltlnkhkiih
      541 srekpykcke cgkafkqfst ltthkiihag kklykceecg kafnhsssls thkiihtgek
      601 sykceecgka flwsstlrrh krihtgekpy kceecgkafs hssalakhkr ihtgekpykc
      661 kecgkafsns stlanhkith teekpykcke cdktfkrlst ltkhkiihag eklykceecg
      721 kafnrssnlt ihkfihtgek pykceecgka fnwsssltkh krihtrekpf kckecgkafi
      781 wsstltrhkr ihtgekpykc eecgkafsrs stltkhktih tgekpykcke cgkafkhssa
      841 lakhkiihag eklykceecg kafnqssnlt thkiihtkek pskseecdka fiwsstlteh
      901 krihtrekty kceecgkafs qpshltthkr mhtgekpykc eecgkafsqs stltthkiih
      961 tgekpykcee cgkafrksst ltehkiihtg ekpykceecg kafsqsstlt rhtrmhtgek
     1021 pykceecgka fnrsskltth kiihtgekpy kceecgkafi ssstlnghkr ihtrekpykc
     1081 eecgkafsqs stltrhkrlh tgekpykcge cgkafkessa ltkhkiihtg ekpykcekcg
     1141 kafnqssilt nhkkihtitp vipllweaea ggsrgqemet ilantvkpll y
//
LOCUS       NP_001273463             259 aa            linear   PRI 27-APR-2025
DEFINITION  cell cycle checkpoint control protein RAD9B isoform c [Homo
            sapiens].
ACCESSION   NP_001273463
VERSION     NP_001273463.1
DBSOURCE    REFSEQ: accession NM_001286534.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Barroso-Chinea,P., Salas-Hernandez,J., Cruz-Muros,I.,
            Lopez-Fernandez,J., Freire,R. and Afonso-Oramas,D.
  TITLE     Expression of RAD9B in the mesostriatal system of rats and humans:
            Overexpression in a 6-OHDA rat model of Parkinson's disease
  JOURNAL   Ann Anat 250, 152135 (2023)
   PUBMED   37460044
  REMARK    GeneRIF: Expression of RAD9B in the mesostriatal system of rats and
            humans: Overexpression in a 6-OHDA rat model of Parkinson's
            disease.
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Cao,X., Tian,T., Steele,J.W., Cabrera,R.M., Aguiar-Pulido,V.,
            Wadhwa,S., Bhavani,N., Bi,P., Gargurevich,N.H., Hoffman,E.N.,
            Cai,C.Q., Marini,N.J., Yang,W., Shaw,G.M., Ross,M.E., Finnell,R.H.
            and Lei,Y.
  TITLE     Loss of RAD9B impairs early neural development and contributes to
            the risk for human spina bifida
  JOURNAL   Hum Mutat 41 (4), 786-799 (2020)
   PUBMED   31898828
  REMARK    GeneRIF: Loss of RAD9B impairs early neural development and
            contributes to the risk for human spina bifida.
            Erratum:[Hum Mutat. 2021 Apr;42(4):487. doi: 10.1002/humu.24175.
            PMID: 33856736]
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Lyndaker,A.M., Vasileva,A., Wolgemuth,D.J., Weiss,R.S. and
            Lieberman,H.B.
  TITLE     Clamping down on mammalian meiosis
  JOURNAL   Cell Cycle 12 (19), 3135-3145 (2013)
   PUBMED   24013428
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Perez-Castro,A.J. and Freire,R.
  TITLE     Rad9B responds to nucleolar stress through ATR and JNK signalling,
            and delays the G1-S transition
  JOURNAL   J Cell Sci 125 (Pt 5), 1152-1164 (2012)
   PUBMED   22399810
  REMARK    GeneRIF: Rad9B responds to nucleolar stress after the activation of
            JNK-dependent stress signalling and ATR-dependent DNA damage
            response pathways, and actively accumulates within nucleoli, where
            it does not cause a transcription block.
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Lieberman,H.B.
  TITLE     Rad9, an evolutionarily conserved gene with multiple functions for
            preserving genomic integrity
  JOURNAL   J Cell Biochem 97 (4), 690-697 (2006)
   PUBMED   16365875
  REMARK    GeneRIF: The encoded mammalian proteins participate in promoting
            resistance to DNA damage, cell cycle checkpoint control, DNA
            repair, and apoptosis.
            Review article
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Dufault,V.M., Oestreich,A.J., Vroman,B.T. and Karnitz,L.M.
  TITLE     Identification and characterization of RAD9B, a paralog of the RAD9
            checkpoint gene
  JOURNAL   Genomics 82 (6), 644-651 (2003)
   PUBMED   14611806
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Hopkins,K.M., Wang,X., Berlin,A., Hang,H., Thaker,H.M. and
            Lieberman,H.B.
  TITLE     Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint
            control genes in normal and cancerous testicular tissue
  JOURNAL   Cancer Res 63 (17), 5291-5298 (2003)
   PUBMED   14500360
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Zou,L. and Elledge,S.J.
  TITLE     Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
  JOURNAL   Science 300 (5625), 1542-1548 (2003)
   PUBMED   12791985
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002350.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            contains multiple differences in both the 5' and 3' coding regions,
            compared to variant 1, including initiation of translation from a
            downstream in-frame start codon. The encoded isoform (c) has a
            shorter N-terminus and a distinct C-terminus, and is shorter than
            isoform a. Variants 4 and 5 encode the same isoform (c).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK097665.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..259
                     /product="cell cycle checkpoint control protein RAD9B
                     isoform c"
                     /EC_number="3.1.11.2"
                     /note="DNA repair exonuclease rad9 homolog B; cell cycle
                     checkpoint control protein RAD9B; RAD9 homolog B"
                     /calculated_mol_wt=28387
     Region          <1..118
                     /region_name="Rad9"
                     /note="pfam04139"
                     /db_xref="CDD:427739"
     CDS             1..259
                     /gene="RAD9B"
                     /coded_by="NM_001286534.2:694..1473"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="GeneID:144715"
                     /db_xref="HGNC:HGNC:21700"
                     /db_xref="MIM:608368"
ORIGIN      
        1 miqprllada ivlftssqee vtlavtplnf clkssneesm dlsnavhsem fvgsdefdff
       61 qigmdteitf cfkelkgilt fseathapis iyfdfpgkpl alsiddmlve anfilatlad
      121 eqsrasspqs lclsqkrkrs dliekkagkn vtgqalecis kkaaprrlyp ketltnisal
      181 encgspamkr vdgdvsevse ssvsnteevp gslclrkfsc mffgavssdq qehfnhpfds
      241 larasdseed mnngsfsif
//
LOCUS       NP_001350236             258 aa            linear   ROD 27-APR-2025
DEFINITION  transducin beta-like protein 2 isoform 2 [Mus musculus].
ACCESSION   NP_001350236 XP_006504496
VERSION     NP_001350236.1
DBSOURCE    REFSEQ: accession NM_001363307.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   DeSilva,U., Elnitski,L., Idol,J.R., Doyle,J.L., Gan,W.,
            Thomas,J.W., Schwartz,S., Dietrich,N.L., Beckstrom-Sternberg,S.M.,
            McDowell,J.C., Blakesley,R.W., Bouffard,G.G., Thomas,P.J.,
            Touchman,J.W., Miller,W. and Green,E.D.
  TITLE     Generation and comparative analysis of approximately 3.3 Mb of
            mouse genomic sequence orthologous to the region of human
            chromosome 7q11.23 implicated in Williams syndrome
  JOURNAL   Genome Res 12 (1), 3-15 (2002)
   PUBMED   11779826
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Valero,M.C., de Luis,O., Cruces,J. and Perez Jurado,L.A.
  TITLE     Fine-scale comparative mapping of the human 7q11.23 region and the
            orthologous region on mouse chromosome 5G: the low-copy repeats
            that flank the Williams-Beuren syndrome deletion arose at
            breakpoint sites of an evolutionary inversion(s)
  JOURNAL   Genomics 69 (1), 1-13 (2000)
   PUBMED   11013070
REFERENCE   3  (residues 1 to 258)
  AUTHORS   de Luis,O., Valero,M.C. and Jurado,L.A.
  TITLE     WBSCR14, a putative transcription factor gene deleted in
            Williams-Beuren syndrome: complete characterisation of the human
            gene and the mouse ortholog
  JOURNAL   Eur J Hum Genet 8 (3), 215-222 (2000)
   PUBMED   10780788
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Perez Jurado,L.A., Wang,Y.K., Francke,U. and Cruces,J.
  TITLE     TBL2, a novel transducin family member in the WBS deletion:
            characterization of the complete sequence, genomic structure,
            transcriptional variants and the mouse ortholog
  JOURNAL   Cytogenet Cell Genet 86 (3-4), 277-284 (1999)
   PUBMED   10575226
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC024607.3.
            
            On May 17, 2018 this sequence version replaced XP_006504496.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK088198.1, ERR3363658.4906300.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 75.02 cM"
     Protein         1..258
                     /product="transducin beta-like protein 2 isoform 2"
                     /note="transducin beta-like protein 2"
                     /calculated_mol_wt=28757
     Region          <12..209
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          45..89
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          94..134
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          142..180
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          187..222
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..258
                     /gene="Tbl2"
                     /gene_synonym="WS-bTRP"
                     /coded_by="NM_001363307.1:453..1229"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:27368"
                     /db_xref="MGI:MGI:1351652"
ORIGIN      
        1 mppwyasalt agkfimtass dttvliwnlk gqvlstintn qmnnshavis pcsrfvgscg
       61 ftpdvkvwev cfgkkgefqe vlrafelkgh sasvhsfafs ndsrrmasvs kdgtwklwdt
      121 dveykkqqdp yllrtgrfee astmpcrlal spdthvlala tgtnihlfnt rrgekeeyfe
      181 cvhgeciadl tfditgrfla scgdravrlf hntpghravv eemqsllkra ssestrqrlq
      241 qqltqaqeal kslgalkk
//
LOCUS       NP_062369                344 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear protein AMMECR1 [Mus musculus].
ACCESSION   NP_062369
VERSION     NP_062369.1
DBSOURCE    REFSEQ: accession NM_019496.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Cox,B.J., Vollmer,M., Tamplin,O., Lu,M., Biechele,S.,
            Gertsenstein,M., van Campenhout,C., Floss,T., Kuhn,R., Wurst,W.,
            Lickert,H. and Rossant,J.
  TITLE     Phenotypic annotation of the mouse X chromosome
  JOURNAL   Genome Res 20 (8), 1154-1164 (2010)
   PUBMED   20548051
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Vitelli,F., Meloni,I., Fineschi,S., Favara,F., Tiziana
            Storlazzi,C., Rocchi,M. and Renieri,A.
  TITLE     Identification and characterization of mouse orthologs of the
            AMMECR1 and FACL4 genes deleted in AMME syndrome: orthology of
            Xq22.3 and MmuXF1-F3
  JOURNAL   Cytogenet Cell Genet 88 (3-4), 259-263 (2000)
   PUBMED   10828604
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL731548.13 and AL731674.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK051736.1, SRR13948564.1709596.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="X"
                     /map="X 63.74 cM"
     Protein         1..344
                     /product="nuclear protein AMMECR1"
                     /note="AMME syndrome candidate gene 1 protein homolog"
                     /calculated_mol_wt=35900
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHT5.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4X0; propagated from
                     UniProtKB/Swiss-Prot (Q9JHT5.1)"
     Region          143..312
                     /region_name="AMMECR1"
                     /note="pfam01871"
                     /db_xref="CDD:460368"
     CDS             1..344
                     /gene="Ammecr1"
                     /gene_synonym="6230420G18Rik"
                     /coded_by="NM_019496.4:14..1048"
                     /db_xref="CCDS:CCDS30452.1"
                     /db_xref="GeneID:56068"
                     /db_xref="MGI:MGI:1860206"
ORIGIN      
        1 maagccgvkk qklsssppsg sgggggasss shcsgesqcr agelglggag trlnglggls
       61 ggggsggggg cplsppqgcg gggggggggg sgsggggisl spplscgvgt llstpaaata
      121 sspssssssp gsrkmvvsae mccfcfdvly chlygyqqpr tprftnepyp lfvtwkigrd
      181 krlrgcigtf samnlhsglr eytltsalkd srfppmtrde lprlfcsvsl ltnfedvcdy
      241 ldwevgvhgi riefinekgs krtatylpev akeqgwdhiq tidsllrkgg ykapitnefr
      301 ktikltryrs ekmtlsyaey lahrqhhhfq ngighplppy nhys
//
LOCUS       NP_005617                494 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine-rich splicing factor 4 [Homo sapiens].
ACCESSION   NP_005617
VERSION     NP_005617.2
DBSOURCE    REFSEQ: accession NM_005626.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Miano,M., Bertola,N., Grossi,A., Dell'Orso,G., Regis,S.,
            Rusmini,M., Uva,P., Vozzi,D., Fioredda,F., Palmisani,E., Lupia,M.,
            Lanciotti,M., Grilli,F., Corsolini,F., Arcuri,L., Giarratana,M.C.,
            Ceccherini,I., Dufour,C., Cappelli,E. and Ravera,S.
  TITLE     Impaired Mitochondrial Function and Marrow Failure in Patients
            Carrying a Variant of the SRSF4 Gene
  JOURNAL   Int J Mol Sci 25 (4), 2083 (2024)
   PUBMED   38396760
  REMARK    GeneRIF: Impaired Mitochondrial Function and Marrow Failure in
            Patients Carrying a Variant of the SRSF4 Gene.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Sun,Y., Liu,X., Wu,Z., Wang,X., Zhang,Y., Yan,W. and You,Y.
  TITLE     SRSF4 Confers Temozolomide Resistance of Glioma via Accelerating
            Double Strand Break Repair
  JOURNAL   J Mol Neurosci 73 (4-5), 259-268 (2023)
   PUBMED   37014544
  REMARK    GeneRIF: SRSF4 Confers Temozolomide Resistance of Glioma via
            Accelerating Double Strand Break Repair.
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Manley,J.L. and Krainer,A.R.
  TITLE     A rational nomenclature for serine/arginine-rich protein splicing
            factors (SR proteins)
  JOURNAL   Genes Dev 24 (11), 1073-1074 (2010)
   PUBMED   20516191
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Lareau,L.F., Inada,M., Green,R.E., Wengrod,J.C. and Brenner,S.E.
  TITLE     Unproductive splicing of SR genes associated with highly conserved
            and ultraconserved DNA elements
  JOURNAL   Nature 446 (7138), 926-929 (2007)
   PUBMED   17361132
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Zimowska,G., Shi,J., Munguba,G., Jackson,M.R., Alpatov,R.,
            Simmons,M.N., Shi,Y. and Sugrue,S.P.
  TITLE     Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal
            epithelial cells
  JOURNAL   Invest Ophthalmol Vis Sci 44 (11), 4715-4723 (2003)
   PUBMED   14578391
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Ramchatesingh,J., Zahler,A.M., Neugebauer,K.M., Roth,M.B. and
            Cooper,T.A.
  TITLE     A subset of SR proteins activates splicing of the cardiac troponin
            T alternative exon by direct interactions with an exonic enhancer
  JOURNAL   Mol Cell Biol 15 (9), 4898-4907 (1995)
   PUBMED   7651409
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Zahler,A.M., Neugebauer,K.M., Stolk,J.A. and Roth,M.B.
  TITLE     Human SR proteins and isolation of a cDNA encoding SRp75
  JOURNAL   Mol Cell Biol 13 (7), 4023-4028 (1993)
   PUBMED   8321209
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Zahler,A.M., Lane,W.S., Stolk,J.A. and Roth,M.B.
  TITLE     SR proteins: a conserved family of pre-mRNA splicing factors
  JOURNAL   Genes Dev 6 (5), 837-847 (1992)
   PUBMED   1577277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590729.14, BC002781.2 and
            CV814357.1.
            
            On Jun 10, 2002 this sequence version replaced NP_005617.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.805643.1,
                                           SRR1660803.180030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373795.7/ ENSP00000362900.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..494
                     /product="serine/arginine-rich splicing factor 4"
                     /note="SR splicing factor 4; splicing factor,
                     arginine/serine-rich 4; SRP001LB; pre-mRNA-splicing factor
                     SRP75"
                     /calculated_mol_wt=56547
     Region          1..87
                     /region_name="RRM1_SRSF4"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     serine/arginine-rich splicing factor 4 (SRSF4); cd12594"
                     /db_xref="CDD:410007"
     Region          72..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08170.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Region          104..175
                     /region_name="RRM2_SRSF4_like"
                     /note="RNA recognition motif 2 (RRM2) found in
                     serine/arginine-rich splicing factor 4 (SRSF4) and similar
                     proteins; cd12600"
                     /db_xref="CDD:410012"
     Region          169..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08170.2)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     CDS             1..494
                     /gene="SRSF4"
                     /gene_synonym="SFRS4; SRP75"
                     /coded_by="NM_005626.5:149..1633"
                     /db_xref="CCDS:CCDS333.1"
                     /db_xref="GeneID:6429"
                     /db_xref="HGNC:HGNC:10786"
                     /db_xref="MIM:601940"
ORIGIN      
        1 mprvyigrls yqarerdver ffkgygkile vdlkngygfv efddlrdadd avyelngkdl
       61 cgerviveha rgprrdgsyg sgrsgygyrr sgrdkygppt rteyrliven lssrcswqdl
      121 kdymrqagev tyadahkgrk negviefvsy sdmkralekl dgtevngrki rlvedkpgsr
      181 rrrsysrsrs hsrsrsrsrh srksrsrsgs sksshsksrs rsrsgsrsrs ksrsrsqsrs
      241 rskkeksrsp skeksrsrsh sagksrsksk dqaeekiqnn dnvgkpksrs psrhksksks
      301 rsrsqerrve eekrgsvsrg rsqekslrqs rsrsrskggs rsrsrsrsks kdkrkgrkrs
      361 reesrsrsrs rsksersrkr gskrdskags skkkkkedtd rsqsrspsrs vskerehaks
      421 essqregrge senagtnqet rsrsrsnsks kpnlpsesrs rsksasktrs rsksrsrsas
      481 rspsrsrsrs hsrs
//
LOCUS       NP_037483                535 aa            linear   PRI 27-APR-2025
DEFINITION  T-box transcription factor TBX21 [Homo sapiens].
ACCESSION   NP_037483
VERSION     NP_037483.1
DBSOURCE    REFSEQ: accession NM_013351.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Li,L., Shan,J., Fang,H., An,G., Zhang,M., Zhou,P., Xie,K., Jin,B.,
            Zhu,H., Jin,X., Yang,P. and Du,L.
  TITLE     Correlation of TBX21 gene polymorphisms with ankylosing spondylitis
            in a Chinese population
  JOURNAL   Int J Immunogenet 51 (3), 143-148 (2024)
   PUBMED   38468428
  REMARK    GeneRIF: Correlation of TBX21 gene polymorphisms with ankylosing
            spondylitis in a Chinese population.
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Rodrigues,R.R., Freitas,V.S., Alves,P.M., Almeida Freitas,R.,
            Souza,L.B. and Andrade Santos,P.P.
  TITLE     Evaluation of the presence of Th1 response through T-bet and
            IFN-gamma immunohistochemical expression in lower lip and oral
            tongue squamous cell carcinomas
  JOURNAL   Pathol Res Pract 253, 155010 (2024)
   PUBMED   38101155
  REMARK    GeneRIF: Evaluation of the presence of Th1 response through T-bet
            and IFN-gamma immunohistochemical expression in lower lip and oral
            tongue squamous cell carcinomas.
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Jiang,X., Du,W., Yang,C., Wang,S., Li,Y., Shen,X., Yang,X., Yao,J.,
            Du,R., Zhang,X., Huang,Y. and Shen,W.
  TITLE     TBX21 attenuates colorectal cancer progression via an
            ARHGAP29/RSK/GSK3beta dependent manner
  JOURNAL   Cell Oncol (Dordr) 46 (5), 1269-1283 (2023)
   PUBMED   37067748
  REMARK    GeneRIF: TBX21 attenuates colorectal cancer progression via an
            ARHGAP29/RSK/GSK3beta dependent manner.
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Wong,P., Foltz,J.A., Chang,L., Neal,C.C., Yao,T., Cubitt,C.C.,
            Tran,J., Kersting-Schadek,S., Palakurty,S., Jaeger,N.,
            Russler-Germain,D.A., Marin,N.D., Gang,M., Wagner,J.A., Zhou,A.Y.,
            Jacobs,M.T., Foster,M., Schappe,T., Marsala,L., McClain,E.,
            Pence,P., Becker-Hapak,M., Fisk,B., Petti,A.A., Griffith,O.L.,
            Griffith,M., Berrien-Elliott,M.M. and Fehniger,T.A.
  TITLE     T-BET and EOMES sustain mature human NK cell identity and antitumor
            function
  JOURNAL   J Clin Invest 133 (13), e162530 (2023)
   PUBMED   37279078
  REMARK    GeneRIF: T-BET and EOMES sustain mature human NK cell identity and
            antitumor function.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Ganjali,F., Asri,N., Rostami-Nejad,M., Hashemi,M., Ainy,E.,
            Masotti,A. and Asadzadeh Aghdaei,H.
  TITLE     Expression analysis of IL-2, TBX21 and SOCS1 in peripheral blood
            cells of celiac disease patients reveals the diagnostic potential
            of IL-2
  JOURNAL   Mol Biol Rep 50 (6), 4841-4849 (2023)
   PUBMED   37039998
  REMARK    GeneRIF: Expression analysis of IL-2, TBX21 and SOCS1 in peripheral
            blood cells of celiac disease patients reveals the diagnostic
            potential of IL-2.
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Yu,H.R., Chang,J.C., Chen,R.F., Chuang,H., Hong,K.C., Wang,L. and
            Yang,K.D.
  TITLE     Different antigens trigger different Th1/Th2 reactions in neonatal
            mononuclear cells (MNCs) relating to T-bet/GATA-3 expression
  JOURNAL   J Leukoc Biol 74 (5), 952-958 (2003)
   PUBMED   12960249
  REMARK    GeneRIF: VZV virus and mite antigens induce expression of this
            transcriptionn factor in cord blood mononuclear cells,
            differenetially affecting Th1 and Th2 cells.
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Chung,H.T., Kim,L.H., Park,B.L., Lee,J.H., Park,H.S., Choi,B.W.,
            Hong,S.J., Chae,S.C., Kim,J.J., Park,C.S. and Shin,H.D.
  TITLE     Association analysis of novel TBX21 variants with asthma phenotypes
  JOURNAL   Hum Mutat 22 (3), 257 (2003)
   PUBMED   12938094
  REMARK    GeneRIF: Among twenty-three novel polymorphisms identified in the
            human TBX21 gene of Korean asthma patients, no significant
            associations of TBX21 variants with risk of asthma were observed.
            GeneRIF: Observational study of genotype prevalence and
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 535)
  AUTHORS   Faedo,A., Ficara,F., Ghiani,M., Aiuti,A., Rubenstein,J.L. and
            Bulfone,A.
  TITLE     Developmental expression of the T-box transcription factor
            T-bet/Tbx21 during mouse embryogenesis
  JOURNAL   Mech Dev 116 (1-2), 157-160 (2002)
   PUBMED   12128215
  REMARK    GeneRIF: distribution of T-BET/TBX21 expression in the
            haematopoietic compartment
REFERENCE   9  (residues 1 to 535)
  AUTHORS   Zhang,W.X. and Yang,S.Y.
  TITLE     Cloning and characterization of a new member of the T-box gene
            family
  JOURNAL   Genomics 70 (1), 41-48 (2000)
   PUBMED   11087660
REFERENCE   10 (residues 1 to 535)
  AUTHORS   Szabo,S.J., Kim,S.T., Costa,G.L., Zhang,X., Fathman,C.G. and
            Glimcher,L.H.
  TITLE     A novel transcription factor, T-bet, directs Th1 lineage commitment
  JOURNAL   Cell 100 (6), 655-669 (2000)
   PUBMED   10761931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015674.12 and AF093098.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of a phylogenetically conserved
            family of genes that share a common DNA-binding domain, the T-box.
            T-box genes encode transcription factors involved in the regulation
            of developmental processes. This gene is the human ortholog of
            mouse Tbx21/Tbet gene. Studies in mouse show that Tbx21 protein is
            a Th1 cell-specific transcription factor that controls the
            expression of the hallmark Th1 cytokine, interferon-gamma (IFNG).
            Expression of the human ortholog also correlates with IFNG
            expression in Th1 and natural killer cells, suggesting a role for
            this gene in initiating Th1 lineage development from naive Th
            precursor cells. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF093098.1, BC039739.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000177694.2/ ENSP00000177694.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..535
                     /product="T-box transcription factor TBX21"
                     /note="T-box expressed in T cells; T-box protein 21;
                     transcription factor TBLYM; T-cell-specific T-box
                     transcription factor T-bet; T-box 21; T-box transcription
                     factor expressed in T cells"
                     /calculated_mol_wt=58197
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL17.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     Region          83..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL17.1)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     Region          136..326
                     /region_name="T-box_TBX21"
                     /note="DNA-binding domain of T-box transcription factor 21
                     and related T-box proteins; cd20203"
                     /db_xref="CDD:410329"
     Site            order(164..165,198,200,243,246,262..263,303,305,311,314,
                     318..320,323..324)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410329"
     Site            order(182,184,194,214..215,217..219,225..226,253..256,
                     275..279,289)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:410329"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     Site            305
                     /site_type="other"
                     /note="Essential for its interaction with RUNX1 and its
                     ability to inhibit RUNX1 transcriptional activity and
                     suppress TH17 lineage development.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     Region          <394..525
                     /region_name="T-box_assoc"
                     /note="T-box transcription factor-associated; pfam16176"
                     /db_xref="CDD:465042"
     Region          449..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL17.1)"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ITK.
                     /evidence=ECO:0000250|UniProtKB:Q9JKD8; propagated from
                     UniProtKB/Swiss-Prot (Q9UL17.1)"
     CDS             1..535
                     /gene="TBX21"
                     /gene_synonym="IMD88; T-bet; T-PET; TBET; TBLYM"
                     /coded_by="NM_013351.2:220..1827"
                     /db_xref="CCDS:CCDS11514.1"
                     /db_xref="GeneID:30009"
                     /db_xref="HGNC:HGNC:11599"
                     /db_xref="MIM:604895"
ORIGIN      
        1 mgivepgcgd mltgtepmpg sdegrapgad pqhryfypep gaqdaderrg ggslgspypg
       61 galvpappsr flgayayppr pqaagfpgag esfpppadae gyqpgegyaa pdpraglypg
      121 predyalpag levsgklrva lnnhllwskf nqhqtemiit kqgrrmfpfl sftvaglept
      181 shyrmfvdvv lvdqhhwryq sgkwvqcgka egsmpgnrly vhpdspntga hwmrqevsfg
      241 klkltnnkga snnvtqmivl qslhkyqprl hivevndgep eaacnasnth iftfqetqfi
      301 avtayqnaei tqlkidnnpf akgfrenfes mytsvdtsip sppgpncqfl ggdhyspllp
      361 nqypvpsrfy pdlpgqakdv vpqaywlgap rdhsyeaefr avsmkpaflp sapgptmsyy
      421 rgqevlapga gwpvapqypp kmgpaswfrp mrtlpmepgp ggsegrgped qgpplvwtei
      481 apirpessds glgegdskrr rvspypssgd ssspagapsp fdkeaegqfy nyfpn
//
LOCUS       NP_116165               2540 aa            linear   PRI 27-APR-2025
DEFINITION  probable JmjC domain-containing histone demethylation protein 2C
            isoform a [Homo sapiens].
ACCESSION   NP_116165
VERSION     NP_116165.1
DBSOURCE    REFSEQ: accession NM_032776.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2540)
  AUTHORS   Xu,R., Lan,H., Zhang,L., Yang,S., Mao,Y. and Che,H.
  TITLE     circ_JMJD1C expedites breast cancer progression by regulating
            miR-182-5p/JMJD1C/SOX4 axis
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (3), 204-211 (2024)
   PUBMED   38650133
  REMARK    GeneRIF: circ_JMJD1C expedites breast cancer progression by
            regulating miR-182-5p/JMJD1C/SOX4 axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2540)
  AUTHORS   Long,X., Zhang,S., Wang,Y., Chen,J., Lu,Y., Hou,H., Lin,B., Li,X.,
            Shen,C., Yang,R., Zhu,H., Cui,R., Cao,D., Chen,G., Wang,D.,
            Chen,Y., Zhai,S., Zeng,Z., Wu,S., Lou,M., Chen,J., Zou,J.,
            Zheng,M., Qin,J. and Wang,X.
  TITLE     Targeting JMJD1C to selectively disrupt tumor Treg cell fitness
            enhances antitumor immunity
  JOURNAL   Nat Immunol 25 (3), 525-536 (2024)
   PUBMED   38356061
  REMARK    GeneRIF: Targeting JMJD1C to selectively disrupt tumor Treg cell
            fitness enhances antitumor immunity.
REFERENCE   3  (residues 1 to 2540)
  AUTHORS   Wang,J., Liu,X., Wang,H., Qin,L., Feng,A., Qi,D., Wang,H., Zhao,Y.,
            Kong,L., Wang,H., Wang,L., Hu,Z. and Xu,X.
  TITLE     JMJD1C Regulates Megakaryopoiesis in In Vitro Models through the
            Actin Network
  JOURNAL   Cells 11 (22), 3660 (2022)
   PUBMED   36429088
  REMARK    GeneRIF: JMJD1C Regulates Megakaryopoiesis in In Vitro Models
            through the Actin Network.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2540)
  AUTHORS   Zhao,L., Qi,F., Du,D. and Wu,N.
  TITLE     Histone demethylase KDM3C regulates the lncRNA GAS5-miR-495-3p-PHF8
            axis in cardiac hypertrophy
  JOURNAL   Ann N Y Acad Sci 1516 (1), 286-299 (2022)
   PUBMED   35777757
  REMARK    GeneRIF: Histone demethylase KDM3C regulates the lncRNA
            GAS5-miR-495-3p-PHF8 axis in cardiac hypertrophy.
REFERENCE   5  (residues 1 to 2540)
  AUTHORS   Tarnopolsky,M., Phillips,S., Parise,G., Varbanov,A., Demuth,J.,
            Stevens,P., Qu,A., Wang,F. and Isfort,R.
  TITLE     Gene expression, fiber type, and strength are similar between left
            and right legs in older adults
  JOURNAL   J Gerontol A Biol Sci Med Sci 62 (10), 1088-1095 (2007)
   PUBMED   17921420
REFERENCE   6  (residues 1 to 2540)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Comparative integromics on JMJD1C gene encoding histone
            demethylase: conserved POU5F1 binding site elucidating mechanism of
            JMJD1C expression in undifferentiated ES cells and diffuse-type
            gastric cancer
  JOURNAL   Int J Oncol 31 (1), 219-223 (2007)
   PUBMED   17549425
  REMARK    GeneRIF: Human JMJD1C variant 2 with TRI8H1, TRI8H2, and JmjC
            domains showed 85.7% total-amino-acid identity with mouse Jmjd1c.
REFERENCE   7  (residues 1 to 2540)
  AUTHORS   Wolf,S.S., Patchev,V.K. and Obendorf,M.
  TITLE     A novel variant of the putative demethylase gene, s-JMJD1C, is a
            coactivator of the AR
  JOURNAL   Arch Biochem Biophys 460 (1), 56-66 (2007)
   PUBMED   17353003
  REMARK    GeneRIF: the discovery of a new Receptors, Androgen coactivator
            which belongs to the JmjC containing enzyme family as a novel
            variant of JMJD1C
REFERENCE   8  (residues 1 to 2540)
  AUTHORS   Castermans,D., Vermeesch,J.R., Fryns,J.P., Steyaert,J.G., Van de
            Ven,W.J., Creemers,J.W. and Devriendt,K.
  TITLE     Identification and characterization of the TRIP8 and REEP3 genes on
            chromosome 10q21.3 as novel candidate genes for autism
  JOURNAL   Eur J Hum Genet 15 (4), 422-431 (2007)
   PUBMED   17290275
  REMARK    GeneRIF: TRIP8 gene codes for a protein predicted to be a
            transcriptional regulator associated with nuclear thyroid hormone
            receptors. Positional candidate gene for autism.
REFERENCE   9  (residues 1 to 2540)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of TRIP8 gene in silico
  JOURNAL   Int J Mol Med 12 (5), 817-821 (2003)
   PUBMED   14533015
REFERENCE   10 (residues 1 to 2540)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022022.10, AL607128.8,
            AL713895.8 and AL590502.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene interacts with thyroid
            hormone receptors and contains a jumonji domain. It is a candidate
            histone demethylase and is thought to be a coactivator for key
            transcription factors. It plays a role in the DNA-damage response
            pathway by demethylating the mediator of DNA damage checkpoint 1
            (MDC1) protein, and is required for the survival of acute myeloid
            leukemia. Mutations in this gene are associated with Rett syndrome
            and intellectual disability. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.208395.1,
                                           SRR1660803.50811.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399262.7/ ENSP00000382204.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2540
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..2540
                     /product="probable JmjC domain-containing histone
                     demethylation protein 2C isoform a"
                     /EC_number="1.14.11.65"
                     /note="thyroid hormone receptor interactor 8; probable
                     JmjC domain-containing histone demethylation protein 2C;
                     TR-interacting protein 8; thyroid receptor-interacting
                     protein 8"
                     /calculated_mol_wt=284395
     Region          127..>175
                     /region_name="RX-CC_like"
                     /note="Coiled-coil domain of the potato virux X resistance
                     protein and similar proteins; cl36576"
                     /db_xref="CDD:453100"
     Region          278..478
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15652.2)"
     Region          <307..672
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZK6; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZK6; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Region          631..656
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15652.2)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15652.2)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Site            943
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Region          1242..1263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15652.2)"
     Region          1614..1692
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15652.2)"
     Region          1971..2064
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15652.2)"
     Site            1989
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15652.2)"
     Region          2066..2070
                     /region_name="LXXLL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15652.2)"
     Region          2278..2350
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          2382..2481
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     CDS             1..2540
                     /gene="JMJD1C"
                     /gene_synonym="KDM3C; TRIP-8; TRIP8"
                     /coded_by="NM_032776.3:316..7938"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41532.1"
                     /db_xref="GeneID:221037"
                     /db_xref="HGNC:HGNC:12313"
                     /db_xref="MIM:604503"
ORIGIN      
        1 mavetraelv gkrflcvavg dearserwes grgwrswrag viravshrds rnpdlavyve
       61 fddlewdkre wvkvyedfst flveyhliwa krndpsqtqg skskqiqwpa ltfkplvern
      121 ipssvtavef lvdkqldflt edsafqpyqd didslnpvlr dnpqlheevk vwvkeqkvqe
      181 ifmqgpysln gyrvrvyrqd satqwftgii thhdlftrtm ivmndqvlep qnvdpsmvqm
      241 tflddvvhsl lkgenigits rrrsranqnv navhshytra qansprpamn sqaavpkqnt
      301 hqqqqqrsir pnkrkgsdss ipdeekmkee kydyisrgen pkgknkhlmn krrkpeedek
      361 klnmkrlrtd nvsdfsessd sensnkriid nsseqkpene lknkntskin geegkphnne
      421 kageetlkns qppwdqiqed kkheeaekrk svdtqlqedm iihsseqstv sdhnsndllp
      481 qecnmdktht mellpkekfv srpptpkcvi ditndtnlek vaqensstfg lqtlqkmdpn
      541 vsdskhsian akfletakkd sdqswvsdvv kvdltqssvt nassgndhln mekekyvsyi
      601 splsavsvme dklhkrsppp etiksklnts vdthkikssp spevvkpkit hspdsvkska
      661 tyvnsqatge rrlankiehe lsrcsfhpip trsstlettk spliidkneh ftvyrdpali
      721 gsetganhis pflsqhpfpl hssshrtcln pgthhpaltp aphllagsss qtplptinth
      781 pltsgphhav hhphllptvl pgvptasllg ghprlesaha sslshlalah qqqqqllqhq
      841 sphllgqahp sasynqlgly piiwqypngt haysglglps skwvhpenav naeaslrrns
      901 pspwlhqptp vtsadgigll shipvrpssa ephrplkita hssppltktl vdhhkeeler
      961 kafmeplrsv astsakndld lnrsqtgkdc hlhrhfvdpv lnqlqrppqe tgerlnkyke
     1021 ehrrilqesi dvapfttkik glegerenys rvassssspk shiikqdmdv ersvsdlykm
     1081 khsvpqslpq snyfttlsns vvnepprsyp skevsniygd kqsnalaaaa anpqtltsfi
     1141 tslskpppli khqpeseglv gkipehlphq iashsvttfr ndcrspthlt vsstntlrsm
     1201 palhrapvfh ppihhslerk egsysslspp tltpvmpvna ggkvqesqkp ptlipepkds
     1261 qanfkssseq sltemwrpnn nlskektewh vekssgklqa amasvivrps sstktdsmpa
     1321 mqlaskdrvs erssagahkt dclklaeage tgriilpnvn sdsvhtksek nfqavsqgsv
     1381 pssvmsavnt mcntktdvit saadttsvss wggsevissl sntilastss ecvssksvsq
     1441 pvaqkqeckv sttapvtlas sktgsvvqps sgfsgttdfi hlkkhkaala aaqykssnas
     1501 etepnaiknq tlsaslplds tvicstinka nsvgngqasq tsqpnyhtkl kkawltrhse
     1561 edkntnkmen sgnsvseiik pcsvnliast ssdiqnsvds kiivdkyvkd dkvnrrkakr
     1621 tyesgsesgd sdeseskseq rtkrqpkpty kkkqndlqkr kgeieedlkp ngvlsrsake
     1681 rsklklqsns ntgiprsvlk dwrkvkklkq tgesflqdds cceigpnlqk crecrlirsk
     1741 kgeepahspv fcrfyyfrrl sfskngvvri dgfsspdqyd deamslwthe nfeddeldie
     1801 tskyildiig dkfcqlvtse ktalswvkkd akiawkravr gvremcdace atlfnihwvc
     1861 qkcgfvvcld cykakerkss rdkelyawmk cvkgqphdhk hlmptqiipg svltdlldam
     1921 htlrekygik shchctnkqn lqvgnfptmn gvsqvlqnvl nhsnkislcm pesqqqntpp
     1981 kseknggssp esdvgtdnkl tppesqsplh wladlaeqka reekkenkel tlenqikeer
     2041 eqdnsespng rtsplvsqnn eqgstlrdll tttagklrvg stdagiafap vysmgapssk
     2101 sgrtmpnild diiasvvenk ippsktskin vkpelkeepe esiisavden nklysdiphs
     2161 wicekhilwl kdyknssnwk lfkecwkqgq pavvsgvhkk mnislwkaes isldfgdhqa
     2221 dllnckdsii snanvkefwd gfeevskrqk nksgetvvlk lkdwpsgedf ktmmparyed
     2281 llkslplpey cnpegkfnla shlpgffvrp dlgprlcsay gvvaakdhdi gttnlhievs
     2341 dvvnilvyvg iakgngilsk agilkkfeee dlddilrkrl kdsseipgal whiyagkdvd
     2401 kireflqkis keqglevlpe hdpirdqswy vnkklrqrll eeygvrtctl iqflgdaivl
     2461 pagalhqvqn fhsciqvted fvspehlves fhltqelrll keeinyddkl qvknilyhav
     2521 kemvralkih edevedmeen
//
LOCUS       NP_001333044             308 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 37 isoform c [Homo
            sapiens].
ACCESSION   NP_001333044
VERSION     NP_001333044.1
DBSOURCE    REFSEQ: accession NM_001346115.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136170.14 and KF455104.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            lacks an alternate coding exon compared to variant 1, that causes a
            frameshift. The resulting isoform (c) is shorter at the C-terminus
            compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1"
     Protein         1..308
                     /product="zinc finger and BTB domain-containing protein 37
                     isoform c"
                     /note="zinc finger and BTB domain-containing protein 37"
                     /calculated_mol_wt=33905
     Region          7..129
                     /region_name="BTB_POZ_ZBTB37"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 37 (ZBTB37); cd18222"
                     /db_xref="CDD:349531"
     Region          140..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TC79.1)"
     CDS             1..308
                     /gene="ZBTB37"
                     /gene_synonym="D430004I08Rik; ZNF908"
                     /coded_by="NM_001346115.2:397..1323"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS86033.1"
                     /db_xref="GeneID:84614"
                     /db_xref="HGNC:HGNC:28365"
ORIGIN      
        1 mekggniqle ipdfsnsvls hlnqlrmqgr lcdivvnvqg qafrahkvvl aasspyfrdh
       61 mslnemstvs isviknptvf eqllsfcytg riclqladii syltaasflq mqhiidkctq
      121 ilegihfkin vaeveaelsq trtkhqerpp eshrvtpnln rslsprhntp kgnrrgqvsa
      181 vldirelspp eestspqiie pssdvesrep ilrinragqw yvetgvadrg grsddevrvl
      241 gavhiktenl eewlgpenqp sgedgssaee vtamvidttg hgsvgqenyt lgssgakvar
      301 ptssevdr
//
LOCUS       NP_001353284             186 aa            linear   PRI 27-APR-2025
DEFINITION  androgen-induced gene 1 protein isoform q [Homo sapiens].
ACCESSION   NP_001353284
VERSION     NP_001353284.1
DBSOURCE    REFSEQ: accession NM_001366355.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Nakada-Tsukui,K., Sekizuka,T., Sato-Ebine,E., Escueta-de Cadiz,A.,
            Ji,D.D., Tomii,K., Kuroda,M. and Nozaki,T.
  TITLE     AIG1 affects in vitro and in vivo virulence in clinical isolates of
            Entamoeba histolytica
  JOURNAL   PLoS Pathog 14 (3), e1006882 (2018)
   PUBMED   29554130
  REMARK    GeneRIF: High AIG1 expression is associated with virulence in
            clinical isolates of Entamoeba histolytica.
            Erratum:[PLoS Pathog. 2018 May 31;14(5):e1007091. doi:
            10.1371/journal.ppat.1007091. PMID: 29851996]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Parsons,W.H., Kolar,M.J., Kamat,S.S., Cognetta,A.B. 3rd,
            Hulce,J.J., Saez,E., Kahn,B.B., Saghatelian,A. and Cravatt,B.F.
  TITLE     AIG1 and ADTRP are atypical integral membrane hydrolases that
            degrade bioactive FAHFAs
  JOURNAL   Nat Chem Biol 12 (5), 367-372 (2016)
   PUBMED   27018888
  REMARK    GeneRIF: These results indicate that AIG1 and ADTRP are founding
            members of an evolutionarily conserved class of transmembrane
            threonine hydrolases involved in bioactive lipid metabolism.
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Wu,G., Sun,M., Zhang,W. and Huo,K.
  TITLE     AIG1 is a novel Pirh2-interacting protein that activates the NFAT
            signaling pathway
  JOURNAL   Front Biosci (Elite Ed) 3 (3), 834-842 (2011)
   PUBMED   21622095
  REMARK    GeneRIF: identified a novel Pirh2-interacting protein, AIG1, by
            yeast two-hybrid screening and confirmed its interaction with p53
            both in vitro and in vivo
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Seo,J., Kim,J. and Kim,M.
  TITLE     Cloning of androgen-inducible gene 1 (AIG1) from human dermal
            papilla cells
  JOURNAL   Mol Cells 11 (1), 35-40 (2001)
   PUBMED   11266118
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL023581.1, AL391726.8 and AL136116.11.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.57787.1, BX538067.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.2"
     Protein         1..186
                     /product="androgen-induced gene 1 protein isoform q"
                     /note="androgen-induced gene 1 protein; FAHFA hydrolase
                     AIG1; fatty acid esters of hydroxy fatty acids hydrolase
                     AIG1"
                     /calculated_mol_wt=21584
     Region          12..167
                     /region_name="Far-17a_AIG1"
                     /note="FAR-17a/AIG1-like protein; pfam04750"
                     /db_xref="CDD:428104"
     CDS             1..186
                     /gene="AIG1"
                     /gene_synonym="AIG-1; dJ95L4.1"
                     /coded_by="NM_001366355.1:38..598"
                     /note="isoform q is encoded by transcript variant 17"
                     /db_xref="GeneID:51390"
                     /db_xref="HGNC:HGNC:21607"
                     /db_xref="MIM:608514"
ORIGIN      
        1 malvpcqvlr maillsycsi lcnykaiemp shqtyggswk fltfidlfvv avfwiiyayd
       61 remiypklld nfipgwlnhg mhttvlpfil iemrtshhqy psrssgltai ctfsvgyilw
      121 vcwvhhvtgm wvypflehig pgariiffgs ttilmnflyl lgevlnnyiw dtqksmeeek
      181 ekpkle
//
LOCUS       NP_998769                471 aa            linear   PRI 27-APR-2025
DEFINITION  ADAMTS-like protein 5 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_998769 XP_005259607
VERSION     NP_998769.2
DBSOURCE    REFSEQ: accession NM_213604.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Kong,S., Tian,S., Wang,Z., Shi,Y., Zhang,J. and Zhuo,H.
  TITLE     Circular RNA circPFKP suppresses the proliferation and metastasis
            of gastric cancer cell via sponging miR-644 and regulating ADAMTSL5
            expression
  JOURNAL   Bioengineered 13 (5), 12326-12337 (2022)
   PUBMED   35587154
  REMARK    GeneRIF: Circular RNA circPFKP suppresses the proliferation and
            metastasis of gastric cancer cell via sponging miR-644 and
            regulating ADAMTSL5 expression.
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Abdullah,M., Choo,C.W., Alias,H., Abdul Rahman,E.J., Mohd
            Ibrahim,H., Jamal,R. and Hussin,N.H.
  TITLE     ADAMTSL5 and CDH11: putative epigenetic markers for therapeutic
            resistance in acute lymphoblastic leukemia
  JOURNAL   Hematology 22 (7), 386-391 (2017)
   PUBMED   28292214
  REMARK    GeneRIF: Chemoresistant B-ALL patients are associated with
            increased methylation in ADAMTSL5 and CDH11.
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Arakawa,A., Siewert,K., Stohr,J., Besgen,P., Kim,S.M., Ruhl,G.,
            Nickel,J., Vollmer,S., Thomas,P., Krebs,S., Pinkert,S.,
            Spannagl,M., Held,K., Kammerbauer,C., Besch,R., Dornmair,K. and
            Prinz,J.C.
  TITLE     Melanocyte antigen triggers autoimmunity in human psoriasis
  JOURNAL   J Exp Med 212 (13), 2203-2212 (2015)
   PUBMED   26621454
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Bader,H.L., Wang,L.W., Ho,J.C., Tran,T., Holden,P., Fitzgerald,J.,
            Atit,R.P., Reinhardt,D.P. and Apte,S.S.
  TITLE     A disintegrin-like and metalloprotease domain containing
            thrombospondin type 1 motif-like 5 (ADAMTSL5) is a novel
            fibrillin-1-, fibrillin-2-, and heparin-binding member of the
            ADAMTS superfamily containing a netrin-like module
  JOURNAL   Matrix Biol 31 (7-8), 398-411 (2012)
   PUBMED   23010571
  REMARK    GeneRIF: ADAMTSL5 could have a role in modulating microfibril
            functions.
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Kim,Y.C., Jung,Y.C., Xuan,Z., Dong,H., Zhang,M.Q. and Wang,S.M.
  TITLE     Pan-genome isolation of low abundance transcripts using SAGE tag
  JOURNAL   FEBS Lett 580 (28-29), 6721-6729 (2006)
   PUBMED   17113583
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC040620.1, BC119796.1, AK131571.1 and DR979736.1.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_005259607.1, NP_998769.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131571.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330475.9/ ENSP00000327608.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..471
                     /product="ADAMTS-like protein 5 isoform 2 precursor"
                     /note="thrombospondin, type I, domain containing 6;
                     ADAMTS-like protein 5; ADAMTSL-5; thrombospondin type-1
                     domain-containing protein 6"
                     /calculated_mol_wt=48509
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3555
     Region          38..87
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          93..190
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Region          205..301
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Region          365..466
                     /region_name="NTR_like"
                     /note="NTR_like domain; a beta barrel with an
                     oligosaccharide/oligonucleotide-binding fold found in
                     netrins, complement proteins, tissue inhibitors of
                     metalloproteases (TIMP), and procollagen C-proteinase
                     enhancers (PCOLCE), amongst others. In netrins, the...;
                     cd03523"
                     /db_xref="CDD:239600"
     CDS             1..471
                     /gene="ADAMTSL5"
                     /gene_synonym="THSD6"
                     /coded_by="NM_213604.3:275..1690"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS12071.1"
                     /db_xref="GeneID:339366"
                     /db_xref="HGNC:HGNC:27912"
ORIGIN      
        1 mdsaplfprp hlfqnlllfl wallncglgv saqgpgewtp wvswtrcsss cgrgvsvrsr
       61 rclrlpgeep cwgdsheyrl cqlpdcppga vpfrdlqcal yngrpvlgtq ktyqwvpfhg
      121 apnqcdlncl aeghafyhsf grvldgtacs pgaqgvcvag rclsagcdgl lgsgaledrc
      181 grcggandsc lfvqrvfrda gafagywnvt lipegarhir vehrsrnhla lmggdgryvl
      241 nghwvvsppg tyeaagthvv ytrdtgpqet lqaagptshd lllqvllqep npgiefefwl
      301 preryspfqa rvqalgwplr qpqprgvepq ppaapavtpa qtptlapdpc ppcpdtrgra
      361 hrllhycgsd fvfqarvlgh hhqaqetrye vriqlvyknr splrareyvw apghcpcpml
      421 aphrdylmav qrlvspdgtq dqlllphagy arpwspaeds rirltarrcp g
//
LOCUS       NP_001357534             200 aa            linear   PRI 27-APR-2025
DEFINITION  ATP synthase subunit s, mitochondrial isoform a precursor [Homo
            sapiens].
ACCESSION   NP_001357534
VERSION     NP_001357534.1
DBSOURCE    REFSEQ: accession NM_001370605.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Wen,F., Li,B., Huang,C., Wei,Z., Zhou,Y., Liu,J. and Zhang,H.
  TITLE     MiR-34a is Involved in the Decrease of ATP Contents Induced by
            Resistin Through Target on ATP5S in HepG2 Cells
  JOURNAL   Biochem Genet 53 (11-12), 301-309 (2015)
   PUBMED   26385595
  REMARK    GeneRIF: The study is the first to show that ATP5S is one of the
            target genes of miR-34a.
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Shaffer,J.R., Polk,D.E., Wang,X., Feingold,E., Weeks,D.E.,
            Lee,M.K., Cuenco,K.T., Weyant,R.J., Crout,R.J., McNeil,D.W. and
            Marazita,M.L.
  TITLE     Genome-wide association study of periodontal health measured by
            probing depth in adults ages 18-49 years
  JOURNAL   G3 (Bethesda) 4 (2), 307-314 (2014)
   PUBMED   24347629
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Belogrudov,G.I. and Hatefi,Y.
  TITLE     Factor B and the mitochondrial ATP synthase complex
  JOURNAL   J Biol Chem 277 (8), 6097-6103 (2002)
   PUBMED   11744738
REFERENCE   7  (residues 1 to 200)
  AUTHORS   Kinosita,K. Jr., Yasuda,R. and Noji,H.
  TITLE     F1-ATPase: a highly efficient rotary ATP machine
  JOURNAL   Essays Biochem 35, 3-18 (2000)
   PUBMED   12471886
  REMARK    Review article
REFERENCE   8  (residues 1 to 200)
  AUTHORS   Wang,H. and Oster,G.
  TITLE     Energy transduction in the F1 motor of ATP synthase
  JOURNAL   Nature 396 (6708), 279-282 (1998)
   PUBMED   9834036
REFERENCE   9  (residues 1 to 200)
  AUTHORS   Elston,T., Wang,H. and Oster,G.
  TITLE     Energy transduction in ATP synthase
  JOURNAL   Nature 391 (6666), 510-513 (1998)
   PUBMED   9461222
REFERENCE   10 (residues 1 to 200)
  AUTHORS   Sanadi,D.R., Pringle,M., Kantham,L., Hughes,J.B. and Srivastava,A.
  TITLE     Evidence for the involvement of coupling factor B in the H+ channel
            of the mitochondrial H+-ATPase
  JOURNAL   Proc Natl Acad Sci U S A 81 (5), 1371-1374 (1984)
   PUBMED   6143319
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359397.3.
            
            Summary: This gene encodes a subunit of mitochondrial ATP synthase.
            Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an
            electrochemical gradient of protons across the inner membrane
            during oxidative phosphorylation. ATP synthase is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, comprising the proton channel.
            This gene encodes the subunit s, also known as factor B, of the
            proton channel. This subunit is necessary for the energy
            transduction activity of the ATP synthase complexes. Alternatively
            spliced transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) represents the longest
            transcript and encodes the longest isoform (a). Variants 1 and 4
            both encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CK299357.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2146982
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q21.3"
     Protein         1..200
                     /product="ATP synthase subunit s, mitochondrial isoform a
                     precursor"
                     /EC_number="3.6.1.14"
                     /note="ATP synthase, H+ transporting, mitochondrial F0
                     complex, subunit s (factor B); distal membrane arm
                     assembly complex 2-like protein; distal membrane arm
                     assembly complex 2 like; ATP synthase, H+ transporting,
                     mitochondrial Fo complex subunit s (factor B);
                     mitochondrial ATP synthase regulatory component factor B;
                     ATP synthase coupling factor B, mitochondrial; ATP
                     synthase coupling factor B-like 1; ATP synthase subunit s,
                     mitochondrial; ATP synthase-coupling factor B"
                     /calculated_mol_wt=23095
     Region          1..61
                     /region_name="N-terminal domain.
                     /evidence=ECO:0000250|UniProtKB:P22027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99766.4)"
     Region          62..87
                     /region_name="LRR 1.
                     /evidence=ECO:0000250|UniProtKB:P22027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99766.4)"
     Region          88..116
                     /region_name="LRR 2.
                     /evidence=ECO:0000250|UniProtKB:P22027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99766.4)"
     Region          111..135
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          117..141
                     /region_name="LRR 3.
                     /evidence=ECO:0000250|UniProtKB:P22027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99766.4)"
     Region          136..164
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          142..173
                     /region_name="LRR 4.
                     /evidence=ECO:0000250|UniProtKB:P22027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99766.4)"
     CDS             1..200
                     /gene="DMAC2L"
                     /gene_synonym="ATP5S; ATPW; FB; HSU79253"
                     /coded_by="NM_001370605.1:779..1381"
                     /note="isoform a precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS32075.2"
                     /db_xref="GeneID:27109"
                     /db_xref="HGNC:HGNC:18799"
                     /db_xref="MIM:618579"
ORIGIN      
        1 mmpfgkisqq lcgvkklpws cdsryfwgwl navfnkvdyd rirdvgpdra asewllrcga
       61 mvryhgqerw qkdynhlptg pldkykiqai datdscimsi gfdhmegleh vekirlckch
      121 yieddcllrl sqlenlqkti lemeiiscgn itdkgiialr hlrnlkylll sdlpgvreke
      181 nlvqafktal pslelklqlk
//
LOCUS       NP_060921               1338 aa            linear   PRI 27-APR-2025
DEFINITION  centrosomal P4.1-associated protein [Homo sapiens].
ACCESSION   NP_060921
VERSION     NP_060921.3
DBSOURCE    REFSEQ: accession NM_018451.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1338)
  AUTHORS   Jaiswal,S., Sanghi,S. and Singh,P.
  TITLE     Separation-of-function MCPH-associated mutations in CPAP affect
            centriole number and length
  JOURNAL   J Cell Sci 136 (21) (2023)
   PUBMED   37823337
  REMARK    GeneRIF: Separation-of-function MCPH-associated mutations in CPAP
            affect centriole number and length.
REFERENCE   2  (residues 1 to 1338)
  AUTHORS   Vijayan,K., Arang,N., Wei,L., Morrison,R., Geiger,R., Parks,K.R.,
            Lewis,A.J., Mast,F.D., Douglass,A.N., Kain,H.S., Aitchison,J.D.,
            Johnson,J.S., Aderem,A. and Kaushansky,A.
  TITLE     A genome-wide CRISPR-Cas9 screen identifies CENPJ as a host
            regulator of altered microtubule organization during Plasmodium
            liver infection
  JOURNAL   Cell Chem Biol 29 (9), 1419-1433 (2022)
   PUBMED   35738280
  REMARK    GeneRIF: A genome-wide CRISPR-Cas9 screen identifies CENPJ as a
            host regulator of altered microtubule organization during
            Plasmodium liver infection.
REFERENCE   3  (residues 1 to 1338)
  AUTHORS   Vasquez-Limeta,A., Lukasik,K., Kong,D., Sullenberger,C.,
            Luvsanjav,D., Sahabandu,N., Chari,R. and Loncarek,J.
  TITLE     CPAP insufficiency leads to incomplete centrioles that duplicate
            but fragment
  JOURNAL   J Cell Biol 221 (5) (2022)
   PUBMED   35404385
  REMARK    GeneRIF: CPAP insufficiency leads to incomplete centrioles that
            duplicate but fragment.
REFERENCE   4  (residues 1 to 1338)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1338)
  AUTHORS   Khan,N.M., Masoud,M.S., Baig,S.M., Qasim,M. and Chang,J.
  TITLE     Identification of Pathogenic Mutations in Primary Microcephaly-
            (MCPH-) Related Three Genes CENPJ, CASK, and MCPH1 in
            Consanguineous Pakistani Families
  JOURNAL   Biomed Res Int 2022, 3769948 (2022)
   PUBMED   35281599
  REMARK    GeneRIF: Identification of Pathogenic Mutations in Primary
            Microcephaly- (MCPH-) Related Three Genes CENPJ, CASK, and MCPH1 in
            Consanguineous Pakistani Families.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1338)
  AUTHORS   Iouzalen,N., Andreae,S., Hannier,S. and Triebel,F.
  TITLE     LAP, a lymphocyte activation gene-3 (LAG-3)-associated protein that
            binds to a repeated EP motif in the intracellular region of LAG-3,
            may participate in the down-regulation of the CD3/TCR activation
            pathway
  JOURNAL   Eur J Immunol 31 (10), 2885-2891 (2001)
   PUBMED   11592063
REFERENCE   7  (residues 1 to 1338)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   8  (residues 1 to 1338)
  AUTHORS   Hung,L.Y., Tang,C.J. and Tang,T.K.
  TITLE     Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP)
            which is associated with the gamma-tubulin complex
  JOURNAL   Mol Cell Biol 20 (20), 7813-7825 (2000)
   PUBMED   11003675
REFERENCE   9  (residues 1 to 1338)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 1338)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354798.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 14, 2007 this sequence version replaced NP_060921.2.
            
            Summary: This gene encodes a protein that belongs to the centromere
            protein family. During cell division, this protein plays a
            structural role in the maintenance of centrosome integrity and
            normal spindle morphology, and it is involved in microtubule
            disassembly at the centrosome. This protein can function as a
            transcriptional coactivator in the Stat5 signaling pathway, and
            also as a coactivator of NF-kappaB-mediated transcription, likely
            via its interaction with the coactivator p300/CREB-binding protein.
            Mutations in this gene are associated with primary autosomal
            recessive microcephaly, a disorder characterized by severely
            reduced brain size and cognitive disability. Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Apr 2012].
            
            Transcript Variant: This variant (1) represents the protein coding
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC113664.1, AK292406.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381884.9/ ENSP00000371308.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.12-q12.13"
     Protein         1..1338
                     /product="centrosomal P4.1-associated protein"
                     /note="LYST-interacting protein LIP1; LAG-3-associated
                     protein; LYST-interacting protein LIP7; LYST-interacting
                     protein 1; Spindle assembly abnormal 4; centromere protein
                     J"
                     /calculated_mol_wt=152870
     Region          190..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC77.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HC77.2)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HC77.2)"
     Region          319..394
                     /region_name="Alpha/beta-tubulin binding.
                     /evidence=ECO:0000269|PubMed:19131341"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC77.2)"
     Region          386..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC77.2)"
     Region          436..479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC77.2)"
     Region          521..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC77.2)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HC77.2)"
     Site            589
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000269|PubMed:20531387; propagated from
                     UniProtKB/Swiss-Prot (Q9HC77.2)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2 and PLK4.
                     /evidence=ECO:0000269|PubMed:20531387; propagated from
                     UniProtKB/Swiss-Prot (Q9HC77.2)"
     Region          611..789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC77.2)"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9HC77.2)"
     Region          845..865
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC77.2)"
     Region          <886..1148
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          895..1338
                     /region_name="Interaction with STIL.
                     /evidence=ECO:0000269|PubMed:22020124,
                     ECO:0000269|PubMed:25385835"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC77.2)"
     Region          1096..1153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC77.2)"
     Region          1152..1180
                     /region_name="Tcp10_C"
                     /note="T-complex protein 10 C-terminus; pfam07202"
                     /db_xref="CDD:462118"
     Region          1225..1253
                     /region_name="Tcp10_C"
                     /note="T-complex protein 10 C-terminus; pfam07202"
                     /db_xref="CDD:462118"
     Region          1261..1289
                     /region_name="Tcp10_C"
                     /note="T-complex protein 10 C-terminus; pfam07202"
                     /db_xref="CDD:462118"
     Region          1296..1325
                     /region_name="Tcp10_C"
                     /note="T-complex protein 10 C-terminus; pfam07202"
                     /db_xref="CDD:462118"
     CDS             1..1338
                     /gene="CPAP"
                     /gene_synonym="BM032; CENP-J; CENPJ; LAP; LIP1; MCPH6;
                     Sas-4; SASS4; SCKL4"
                     /coded_by="NM_018451.5:168..4184"
                     /db_xref="CCDS:CCDS9310.1"
                     /db_xref="GeneID:55835"
                     /db_xref="HGNC:HGNC:17272"
                     /db_xref="MIM:609279"
ORIGIN      
        1 mflmptssel nsgqnfltqw mtnpsragvi lnrgfpilea dkekraavdi stsfpikgth
       61 fsdsfsfine edslleeqkl esnnpykpqs dksethtafp cikkgpqvaa chsapghqee
      121 nkndfipdla sefkegaykd plfkkleqlk evqqkkqeql krqqleqlqr lmeeqekllt
      181 mvsgqctlpg lsllpddqsq khrspgnttt geratccfps yvypdptqee typsnilshe
      241 qsnfcrtahg dfvltskras pnlfseaqyq eapveknnlk eenrnhptge silcwekvte
      301 qiqeandknl qkhddsseva nieerpikaa igerkqtfed yleeqiqlee qelkqkqlke
      361 aegplpikak pkqpflkrge glarftnaks kfqkgkeskl vtnqstsedq plfkmdrqql
      421 qrktalknke lcadnpilkk dskartksgs vtlsqkpkml kcsnrkslsp sglkiqtgkk
      481 cdgqfrdqik fenkvtsnnk envtecpkpc dtgctgwnkt qgkdrlplst gpasrlaaks
      541 piretmkese ssldvslqkk letwerekek enleldeflf leqaadeisf ssnssfvlki
      601 lerdqqickg hrmsstpvka vpqktnpadp ishcnrsedl dhtarekese cevapkqlhs
      661 lssadelreq pckirkavqk stsenqtewn arddegvpns dsstdseeql dvtikpsted
      721 rergissred spqvcddkgp fkdtrtqedk rrdvdldlsd kdyssdesim esikhkvsep
      781 srssslslsk mdfddertwt dleenlcnhd vvlgnestyg tpqtcypnne igildktikr
      841 kiapvkrged lsksrrsrsp ptselmmkff pslkpkpksd shlgnelkln isqdqppgdn
      901 arsqvlreki ieleteiekf kaenaslakl rieresalek lrkeiadfeq qkakelarie
      961 efkkeemrkl qkerkvfeky ttaartfpdk kereeiqtlk qqiadlredl krketkwsst
     1021 hsrlrsqiqm lvrentdlre eikvmerfrl dawkraeaie sslevekkdk lantsvrfqn
     1081 sqissgtqve kykknylpmq gnpprrsksa pprdlgnldk gqaasprepl eplnfpdpey
     1141 keeeedqdiq geishpdgkv ekvykngcrv ilfpngtrke vsadgktitv tffngdvkqv
     1201 mpdqrviyyy aaaqtthtty peglevlhfs sgqiekhypd grkeitfpdq tvknlfpdgq
     1261 eesifpdgti vrvqrdgnkl iefnngqrel htaqfkrrey pdgtvktvya nghqetkyrs
     1321 grirvkdkeg nvlmdtel
//
LOCUS       NP_001357011             507 aa            linear   PRI 27-APR-2025
DEFINITION  pro-neuregulin-3, membrane-bound isoform isoform 5 [Homo sapiens].
ACCESSION   NP_001357011
VERSION     NP_001357011.1
DBSOURCE    REFSEQ: accession NM_001370082.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,T., Vullhorst,D., Chaudhuri,R., Guardia,C.M., Chaudhary,N.,
            Karavanova,I., Bonifacino,J.S. and Buonanno,A.
  TITLE     Transcytosis and trans-synaptic retention by postsynaptic ErbB4
            underlie axonal accumulation of NRG3
  JOURNAL   J Cell Biol 221 (7) (2022)
   PUBMED   35579602
  REMARK    GeneRIF: Transcytosis and trans-synaptic retention by postsynaptic
            ErbB4 underlie axonal accumulation of NRG3.
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Kara,H.G., Erdal,M.E., Yilmaz,S.G., Sengul,C., Sengul,C.B. and
            Karakulah,K.
  TITLE     Association of NRG3 and ERBB4 gene polymorphism with nicotine
            dependence in Turkish population
  JOURNAL   Mol Biol Rep 48 (6), 5319-5326 (2021)
   PUBMED   34247340
  REMARK    GeneRIF: Association of NRG3 and ERBB4 gene polymorphism with
            nicotine dependence in Turkish population.
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Zhou,Y., Li,Y., Meng,Y., Wang,J., Wu,F., Ning,Y., Li,Y.,
            Cassidy,R.M., Li,Z. and Zhang,X.Y.
  TITLE     Neuregulin 3 rs10748842 polymorphism contributes to the effect of
            body mass index on cognitive impairment in patients with
            schizophrenia
  JOURNAL   Transl Psychiatry 10 (1), 62 (2020)
   PUBMED   32066712
  REMARK    GeneRIF: Neuregulin 3 rs10748842 polymorphism contributes to the
            effect of body mass index on cognitive impairment in patients with
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Li,Z., Liu,L., Lin,W., Zhou,Y., Zhang,G., Du,X., Li,Y., Tang,W. and
            Zhang,X.
  TITLE     NRG3 contributes to cognitive deficits in chronic patients with
            schizophrenia
  JOURNAL   Schizophr Res 215, 134-139 (2020)
   PUBMED   31753594
  REMARK    GeneRIF: NRG3 contributes to cognitive deficits in chronic patients
            with schizophrenia.
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Pinto,R., Assis,J., Nogueira,A., Pereira,C., Coelho,S., Brandao,M.,
            Dias,J., Alves,S., Pereira,D. and Medeiros,R.
  TITLE     Pharmacogenomics in epithelial ovarian cancer first-line treatment
            outcome: validation of GWAS-associated NRG3 rs1649942 and BRE
            rs7572644 variants in an independent cohort
  JOURNAL   Pharmacogenomics J 19 (1), 25-32 (2019)
   PUBMED   30287910
  REMARK    GeneRIF: The BRE rs7572644 and NRG3 rs1649942 genetic variants were
            validated in an independent cohort of EOC Portuguese patients.
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Benzel,I., Bansal,A., Browning,B.L., Galwey,N.W., Maycox,P.R.,
            McGinnis,R., Smart,D., St Clair,D., Yates,P. and Purvis,I.
  TITLE     Interactions among genes in the ErbB-Neuregulin signalling network
            are associated with increased susceptibility to schizophrenia
  JOURNAL   Behav Brain Funct 3, 31 (2007)
   PUBMED   17598910
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Carteron,C., Ferrer-Montiel,A. and Cabedo,H.
  TITLE     Characterization of a neural-specific splicing form of the human
            neuregulin 3 gene involved in oligodendrocyte survival
  JOURNAL   J Cell Sci 119 (Pt 5), 898-909 (2006)
   PUBMED   16478787
  REMARK    GeneRIF: The NRG3 protein is a new post-translationally regulated
            isoform of neuregulin 3 expressed in the developing human central
            nervous system with a role in oligodendrocyte survival.
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Hobbs,S.S., Coffing,S.L., Le,A.T., Cameron,E.M., Williams,E.E.,
            Andrew,M., Blommel,E.N., Hammer,R.P., Chang,H. and Riese,D.J. 2nd.
  TITLE     Neuregulin isoforms exhibit distinct patterns of ErbB family
            receptor activation
  JOURNAL   Oncogene 21 (55), 8442-8452 (2002)
   PUBMED   12466964
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Gizatullin,R.Z., Muravenko,O.V., Al-Amin,A.N., Wang,F.,
            Protopopov,A.I., Kashuba,V.I., Zelenin,A.V. and Zabarovsky,E.R.
  TITLE     Human NRG3 gene Map position 10q22-q23
  JOURNAL   Chromosome Res 8 (6), 560 (2000)
   PUBMED   11032326
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Zhang,D., Sliwkowski,M.X., Mark,M., Frantz,G., Akita,R., Sun,Y.,
            Hillan,K., Crowley,C., Brush,J. and Godowski,P.J.
  TITLE     Neuregulin-3 (NRG3): a novel neural tissue-enriched protein that
            binds and activates ErbB4
  JOURNAL   Proc Natl Acad Sci U S A 94 (18), 9562-9567 (1997)
   PUBMED   9275162
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL096706.10, AC010157.12,
            AL391478.14, AL513204.10, AL354749.6, AL136085.12 and AL589782.7.
            
            Summary: This gene is a member of the neuregulin gene family. This
            gene family encodes ligands for the transmembrane tyrosine kinase
            receptors ERBB3 and ERBB4 - members of the epidermal growth factor
            receptor family. Ligand binding activates intracellular signaling
            cascades and the induction of cellular responses including
            proliferation, migration, differentiation, and survival or
            apoptosis. This gene encodes neuregulin 3 (NRG3). NRG3 has been
            shown to activate the tyrosine phosphorylation of its cognate
            receptor, ERBB4, and is thought to influence neuroblast
            proliferation, migration and differentiation by signalling through
            ERBB4. NRG3 also promotes mammary differentiation during
            embryogenesis. Linkage studies have implicated this gene as a
            susceptibility locus for schizophrenia and schizoaffective
            disorder. Alternative splicing results in multiple transcript
            variants encoding distinct isoforms. Additional transcript variants
            have been described but their biological validity has not been
            verified.[provided by RefSeq, Sep 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..507
                     /product="pro-neuregulin-3, membrane-bound isoform isoform
                     5"
                     /note="neuregulin-3-like polypeptide"
                     /calculated_mol_wt=56934
     Region          <82..142
                     /region_name="PHA02887"
                     /note="EGF-like protein; Provisional"
                     /db_xref="CDD:165214"
     CDS             1..507
                     /gene="NRG3"
                     /gene_synonym="HRG3; pro-NRG3"
                     /coded_by="NM_001370082.1:893..2416"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:10718"
                     /db_xref="HGNC:HGNC:7999"
                     /db_xref="MIM:605533"
ORIGIN      
        1 mlppllpllp pplppphqkl apapnfinii iwyyfpsawr tcfnisssvg llltnsykfc
       61 prdrrhaihg nmgktrvvrr qkqeqdttty stersehfkp crdkdlaycl ndgecfviet
      121 ltgshkhcrc kegyqgvrcd qflpktdsil sdptdhlgie fmeseevyqr qvlsisciif
      181 givivgmfca afyfkskkqa kqiqeqlkvp qngksyslka sstmaksenl vkshvqlqny
      241 skverhpvta lekmmessfv gpqsfpevps pdrgsqsvkh hrslssccsp gqrsgmlhrn
      301 afrrtppspr srlggivgpa yqqleesrip dqdtipcqgy sssglktqrn tsinmqlpsr
      361 etnpyfnsle qkdlvgysst rassvpiips vgleetclqm pgisevksik wcknsysadv
      421 vnvsipvsdc liaeqqevki lletvqeqir iltdarrsed yelasveted sasentaflp
      481 lsptaksere aqfvlrneiq rdsaltk
//
LOCUS       NP_001357393             322 aa            linear   PRI 27-APR-2025
DEFINITION  mas-related G-protein coupled receptor member X3 [Homo sapiens].
ACCESSION   NP_001357393 XP_011518184
VERSION     NP_001357393.1
DBSOURCE    REFSEQ: accession NM_001370464.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Chen,L.Y., You,Q., Lv,D.Z., Li,S.H. and Zhang,S.Y.
  TITLE     GPCR-mediated EGFR transactivation ameliorates skin toxicities
            induced by afatinib
  JOURNAL   Acta Pharmacol Sin 43 (6), 1534-1543 (2022)
   PUBMED   34552215
  REMARK    GeneRIF: GPCR-mediated EGFR transactivation ameliorates skin
            toxicities induced by afatinib.
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Schmid,C.D., Schledzewski,K., Mogler,C., Waldburger,N., Kalna,V.,
            Marx,A., Randi,A.M., Geraud,C., Goerdt,S. and Koch,P.S.
  TITLE     GPR182 is a novel marker for sinusoidal endothelial differentiation
            with distinct GPCR signaling activity in vitro
  JOURNAL   Biochem Biophys Res Commun 497 (1), 32-38 (2018)
   PUBMED   29408502
  REMARK    GeneRIF: Our data demonstrate that GPR182 is an endothelial
            subtype-specific marker for human sinusoidal EC of the liver,
            spleen, lymph node and bone marrow. In addition, we provide
            evidence for GPR182-dependent downstream signaling via ERK and SRF
            pathways that may be involved in regulating endothelial
            subtype-specific sinusoidal differentiation and sinusoidal
            functions such as permeability.
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Franco,R., Martinez-Pinilla,E., Navarro,G. and Zamarbide,M.
  TITLE     Potential of GPCRs to modulate MAPK and mTOR pathways in
            Alzheimer's disease
  JOURNAL   Prog Neurobiol 149-150, 21-38 (2017)
   PUBMED   28189739
  REMARK    GeneRIF: Potential of GPCRs to modulate MAPK and mTOR pathways in
            different stages of the neurodegenerative disease.
            Review article
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Burstein,E.S., Ott,T.R., Feddock,M., Ma,J.N., Fuhs,S., Wong,S.,
            Schiffer,H.H., Brann,M.R. and Nash,N.R.
  TITLE     Characterization of the Mas-related gene family: structural and
            functional conservation of human and rhesus MrgX receptors
  JOURNAL   Br J Pharmacol 147 (1), 73-82 (2006)
   PUBMED   16284629
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Kaisho,Y., Watanabe,T., Nakata,M., Yano,T., Yasuhara,Y.,
            Shimakawa,K., Mori,I., Sakura,Y., Terao,Y., Matsui,H. and
            Taketomi,S.
  TITLE     Transgenic rats overexpressing the human MrgX3 gene show cataracts
            and an abnormal skin phenotype
  JOURNAL   Biochem Biophys Res Commun 330 (3), 653-657 (2005)
   PUBMED   15809047
  REMARK    GeneRIF: overexpression of the human MrgX3 gene causes a
            disturbance of the normal cell-differentiation process
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Lembo,P.M., Grazzini,E., Groblewski,T., O'Donnell,D., Roy,M.O.,
            Zhang,J., Hoffert,C., Cao,J., Schmidt,R., Pelletier,M., Labarre,M.,
            Gosselin,M., Fortin,Y., Banville,D., Shen,S.H., Strom,P., Payza,K.,
            Dray,A., Walker,P. and Ahmad,S.
  TITLE     Proenkephalin A gene products activate a new family of sensory
            neuron--specific GPCRs
  JOURNAL   Nat Neurosci 5 (3), 201-209 (2002)
   PUBMED   11850634
REFERENCE   8  (residues 1 to 322)
  AUTHORS   Dong,X., Han,S., Zylka,M.J., Simon,M.I. and Anderson,D.J.
  TITLE     A diverse family of GPCRs expressed in specific subsets of
            nociceptive sensory neurons
  JOURNAL   Cell 106 (5), 619-632 (2001)
   PUBMED   11551509
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090099.14.
            
            On May 8, 2019 this sequence version replaced XP_011518184.1.
            
            Summary: This gene encodes a member of the mas-related/sensory
            neuron specific subfamily of G protein coupled receptors. The
            encoded protein may be involved in sensory neuron regulation and in
            the modulation of pain. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CA455045.1, BE439409.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000621697.2/ ENSP00000481943.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..322
                     /product="mas-related G-protein coupled receptor member
                     X3"
                     /note="G protein-coupled receptor MRGX3; sensory
                     neuron-specific G-protein coupled receptor 1/2; G
                     protein-coupled receptor SNSR1; mas-related GPCR member
                     X3; G protein-coupled receptor SNSR2; MAS-related GPR,
                     member X3"
                     /calculated_mol_wt=36353
     Region          28..299
                     /region_name="7tmA_MrgprX-like"
                     /note="primate-specific mas-related G protein-coupled
                     receptor subtype X-like, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15106"
                     /db_xref="CDD:320234"
     Region          29..55
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320234"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LB0.2)"
     Region          61..87
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320234"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LB0.2)"
     Site            order(82,85..86,97..102,104..105,108,151,153..157,180,
                     183..185,187..189,191..192,229,232..233,235..236,239,
                     250..251,253..255,258,261..262)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320234"
     Region          97..125
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320234"
     Site            97..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LB0.2)"
     Region          137..157
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320234"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LB0.2)"
     Site            178..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LB0.2)"
     Region          180..205
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320234"
     Region          209..239
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320234"
     Site            214..234
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LB0.2)"
     Region          251..276
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320234"
     Site            255..275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LB0.2)"
     CDS             1..322
                     /gene="MRGPRX3"
                     /gene_synonym="GPCR; MRGX3; SNSR1; SNSR2"
                     /coded_by="NM_001370464.1:195..1163"
                     /db_xref="CCDS:CCDS7830.1"
                     /db_xref="GeneID:117195"
                     /db_xref="HGNC:HGNC:17980"
                     /db_xref="MIM:607229"
ORIGIN      
        1 mdstipvlgt eltpingree tpcykqtlsf tgltcivslv altgnavvlw llgcrmrrna
       61 vsiyilnlva adflflsghi icsplrlini rhpiskilsp vmtfpyfigl smlsaister
      121 clsilwpiwy hcrrprylss vmcvllwals llrsilewmf cdflfsgans vwcetsdfit
      181 iawlvflcvv lcgsslvllv rilcgsrkmp ltrlyvtill tvlvfllcgl pfgiqwalfs
      241 rihldwkvlf chvhlvsifl salnssanpi iyffvgsfrq rqnrqnlklv lqralqdtpe
      301 vdegggwlpq etlelsgsrl eq
//
LOCUS       NP_001357385             108 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 577 isoform d [Homo sapiens].
ACCESSION   NP_001357385
VERSION     NP_001357385.1
DBSOURCE    REFSEQ: accession NM_001370456.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Lorenzo,P.M., Izquierdo,A.G., Diaz-Lagares,A., Carreira,M.C.,
            Macias-Gonzalez,M., Sandoval,J., Cueva,J., Lopez-Lopez,R.,
            Casanueva,F.F. and Crujeiras,A.B.
  TITLE     ZNF577 Methylation Levels in Leukocytes From Women With Breast
            Cancer Is Modulated by Adiposity, Menopausal State, and the
            Mediterranean Diet
  JOURNAL   Front Endocrinol (Lausanne) 11, 245 (2020)
   PUBMED   32390948
  REMARK    GeneRIF: ZNF577 Methylation Levels in Leukocytes From Women With
            Breast Cancer Is Modulated by Adiposity, Menopausal State, and the
            Mediterranean Diet.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011460.3, AC074141.3 and AC006272.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803614.308464.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2144120, SAMEA2162568 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..108
                     /product="zinc finger protein 577 isoform d"
                     /calculated_mol_wt=11965
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSK1.3)"
     Region          25..83
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     CDS             1..108
                     /gene="ZNF577"
                     /coded_by="NM_001370456.1:1350..1676"
                     /note="isoform d is encoded by transcript variant 9"
                     /db_xref="GeneID:84765"
                     /db_xref="HGNC:HGNC:28673"
ORIGIN      
        1 mknativmsv rreqgsssge gslsfedvav gftreewqfl dqsqkvlyke vmlenyinlv
       61 sigyrgtkpd slfkleqgep pgiaegaahs qicpdlhyrw ktaasepq
//
LOCUS       NP_653232                541 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 513 isoform 1 [Homo sapiens].
ACCESSION   NP_653232
VERSION     NP_653232.3
DBSOURCE    REFSEQ: accession NM_144631.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Chen,J., Xu,X., Chen,S., Lu,T., Zheng,Y., Gan,Z., Shen,Z., Ma,S.,
            Wang,D., Su,L., He,F., Shang,X., Xu,H., Chen,D., Zhang,L. and
            Xiong,F.
  TITLE     Double heterozygous pathogenic mutations in KIF3C and ZNF513 cause
            hereditary gingival fibromatosis
  JOURNAL   Int J Oral Sci 15 (1), 46 (2023)
   PUBMED   37752101
  REMARK    GeneRIF: Double heterozygous pathogenic mutations in KIF3C and
            ZNF513 cause hereditary gingival fibromatosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Li,L., Nakaya,N., Chavali,V.R., Ma,Z., Jiao,X., Sieving,P.A.,
            Riazuddin,S., Tomarev,S.I., Ayyagari,R., Riazuddin,S.A. and
            Hejtmancik,J.F.
  TITLE     A mutation in ZNF513, a putative regulator of photoreceptor
            development, causes autosomal-recessive retinitis pigmentosa
  JOURNAL   Am J Hum Genet 87 (3), 400-409 (2010)
   PUBMED   20797688
  REMARK    GeneRIF: These results suggest that the ZNF513 p.C339R mutation is
            responsible for retinitis pigmentosa and that ZNF513 plays a key
            role in the regulation of photoreceptor-specific genes in retinal
            development and photoreceptor maintenance.
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB024976.1, BC052282.1 and
            AI766724.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 9, 2004 this sequence version replaced NP_653232.2.
            
            Summary: The protein encoded by this gene is a possible
            transcriptional regulator involved in retinal development. Defects
            in this gene can be a cause of autosomal-recessive retinitis
            pigmentosa. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052282.1, AK290690.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323703.11/ ENSP00000318373.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..541
                     /product="zinc finger protein 513 isoform 1"
                     /calculated_mol_wt=57751
     Region          1..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8E2.2)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N8E2.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PD29; propagated from
                     UniProtKB/Swiss-Prot (Q8N8E2.2)"
     Region          152..172
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(157,159,161,163..164,167..168,171,185,187,191..192,
                     195..196,199,213,215,217,219..220,223..224,227)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          164..189
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          180..200
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          192..217
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          208..228
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          362..382
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(367,369,371,373..374,377..378,381,395,397,401..402,
                     405..406,409,423,425,427,429..430,433..434,437)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          374..399
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          390..410
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          402..425
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          414..>487
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          418..438
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          446..466
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          474..493
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          492..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8E2.2)"
     CDS             1..541
                     /gene="ZNF513"
                     /gene_synonym="HMFT0656; RP58; Zfp513"
                     /coded_by="NM_144631.6:209..1834"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1751.1"
                     /db_xref="GeneID:130557"
                     /db_xref="HGNC:HGNC:26498"
                     /db_xref="MIM:613598"
ORIGIN      
        1 mprrkqshpq pvkcegvkvd tedsldegpg alvlesdlll gqdlefeeee eeeegdgnsd
       61 qlmgferdse gdslgarpgl pyglsddesg ggralsaese veepargpge argerpgpac
      121 qlcggptgeg pccgaggpgg gpllpprlly scrlctfvsh ysshlkrhmq thsgekpfrc
      181 grcpyasaql vnltrhtrth tgekpyrcph cpfacsslgn lrrhqrthag pptppcptcg
      241 frcctprpar ppspteqega vprrpedall lpdlslhvpp ggasflpdcg qlrgegeglc
      301 gtgseplpel lfpwtcrgcg qeleegegsr lgaamcgrcm rgeagggasg gpqgpsdkgf
      361 acslcpfath ypnhlarhmk thsgekpfrc arcpyasahl dnlkrhqrvh tgekpykcpl
      421 cpyacgnlan lkrhgrihsg dkpfrcslcn yscnqsmnlk rhmlrhtgek pfrcatcayt
      481 tghwdnykrh qkvhghggag gpglsasegw apphsppsvl ssrgppalgt agsravhtds
      541 s
//
LOCUS       NP_001357372             448 aa            linear   PRI 27-APR-2025
DEFINITION  nucleoporin NUP42 isoform 1 [Homo sapiens].
ACCESSION   NP_001357372 XP_005249649
VERSION     NP_001357372.1
DBSOURCE    REFSEQ: accession NM_001370443.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Schwartz,T.U.
  TITLE     The Structure Inventory of the Nuclear Pore Complex
  JOURNAL   J Mol Biol 428 (10 Pt A), 1986-2000 (2016)
   PUBMED   27016207
  REMARK    Review article
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Bui,K.H., von Appen,A., DiGuilio,A.L., Ori,A., Sparks,L.,
            Mackmull,M.T., Bock,T., Hagen,W., Andres-Pons,A., Glavy,J.S. and
            Beck,M.
  TITLE     Integrated structural analysis of the human nuclear pore complex
            scaffold
  JOURNAL   Cell 155 (6), 1233-1243 (2013)
   PUBMED   24315095
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Waldmann,I., Spillner,C. and Kehlenbach,R.H.
  TITLE     The nucleoporin-like protein NLP1 (hCG1) promotes CRM1-dependent
            nuclear protein export
  JOURNAL   J Cell Sci 125 (Pt 1), 144-154 (2012)
   PUBMED   22250199
  REMARK    GeneRIF: NLP1 functions as an accessory factor in CRM1-dependent
            nuclear protein export
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Farjot,G., Sergeant,A. and Mikaelian,I.
  TITLE     A new nucleoporin-like protein interacts with both HIV-1 Rev
            nuclear export signal and CRM-1
  JOURNAL   J Biol Chem 274 (24), 17309-17317 (1999)
   PUBMED   10358091
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Katahira,J., Strasser,K., Podtelejnikov,A., Mann,M., Jung,J.U. and
            Hurt,E.
  TITLE     The Mex67p-mediated nuclear mRNA export pathway is conserved from
            yeast to human
  JOURNAL   EMBO J 18 (9), 2593-2609 (1999)
   PUBMED   10228171
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Fouchier,R.A., Meyer,B.E., Simon,J.H., Fischer,U., Albright,A.V.,
            Gonzalez-Scarano,F. and Malim,M.H.
  TITLE     Interaction of the human immunodeficiency virus type 1 Vpr protein
            with the nuclear pore complex
  JOURNAL   J Virol 72 (7), 6004-6013 (1998)
   PUBMED   9621063
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Van Laer,L., Van Camp,G., van Zuijlen,D., Green,E.D.,
            Verstreken,M., Schatteman,I., Van de Heyning,P., Balemans,W.,
            Coucke,P., Greinwald,J.H., Smith,R.J., Huizing,E. and Willems,P.
  TITLE     Refined mapping of a gene for autosomal dominant progressive
            sensorineural hearing loss (DFNA5) to a 2-cM region, and exclusion
            of a candidate gene that is expressed in the cochlea
  JOURNAL   Eur J Hum Genet 5 (6), 397-405 (1997)
   PUBMED   9450185
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005082.3.
            
            On May 8, 2019 this sequence version replaced XP_005249649.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.88777.1,
                                           SRR3476690.39481.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.3"
     Protein         1..448
                     /product="nucleoporin NUP42 isoform 1"
                     /note="nucleoporin-like protein 1; H_RG271G13.9;
                     nucleoporin-like protein 2; NUP42 homolog; nucleoporin
                     hCG1; nucleoporin like 2; nucleoporin NUP42"
                     /calculated_mol_wt=47694
     Region          4..22
                     /region_name="zf_CCCH_4"
                     /note="Zinc finger domain; pfam18345"
                     /db_xref="CDD:465719"
     Region          <235..414
                     /region_name="PPE"
                     /note="PPE-repeat protein [Function unknown]; COG5651"
                     /db_xref="CDD:444372"
     CDS             1..448
                     /gene="NUP42"
                     /gene_synonym="CG1; hCG1; NLP-1; NLP1; NLP_1; NUPL2; UIP1"
                     /coded_by="NM_001370443.1:39..1385"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:11097"
                     /db_xref="HGNC:HGNC:17010"
                     /db_xref="MIM:619998"
ORIGIN      
        1 maicqfflqg rcrfgdrcwn ehpgargagg grqqpqqqps gnnrrgwntt sqrysnviqp
       61 ssfskstpwg gsrdqekpyf ssfdsgastn rkegfglsen pfaslspdeq kdekkllegi
      121 vkdmevwess gqwmfsvysp vkkkpnisgf tdispeelrl eyhnfltsnn lqsylnsvqr
      181 linqwrnrvn elkslnistk valkclwkiy thlspkiygp dcgkfiifls dvkdgvnqaa
      241 pafgfgssqa atfmspgfpv nnsssdnaqn fsfktnsgfa aassgspagf gsspafgaaa
      301 stssgistsa pafgfgkpev tsaasfsfks paassfgspg fsglpaslat gpvrapvapa
      361 fgggssvagf gspgshshta fskpssdtfg nssistslsa sssiiatdnv lftprdkltv
      421 eeleqfqskk ftlgkiplkp pplellnv
//
LOCUS       NP_055706                181 aa            linear   PRI 27-APR-2025
DEFINITION  28 kDa heat- and acid-stable phosphoprotein [Homo sapiens].
ACCESSION   NP_055706
VERSION     NP_055706.1
DBSOURCE    REFSEQ: accession NM_014891.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Chirichella,M., Bianchi,N., Dzafo,E., Foli,E., Gualdrini,F.,
            Kenyon,A., Natoli,G. and Monticelli,S.
  TITLE     RFX transcription factors control a miR-150/PDAP1 axis that
            restrains the proliferation of human T cells
  JOURNAL   PLoS Biol 20 (2), e3001538 (2022)
   PUBMED   35143476
  REMARK    GeneRIF: RFX transcription factors control a miR-150/PDAP1 axis
            that restrains the proliferation of human T cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Weston,V.J., Wei,W., Stankovic,T. and Kearns,P.
  TITLE     Synergistic action of dual IGF1/R and MEK inhibition sensitizes
            childhood acute lymphoblastic leukemia (ALL) cells to cytotoxic
            agents and involves downregulation of STAT6 and PDAP1
  JOURNAL   Exp Hematol 63, 52-63 (2018)
   PUBMED   29656114
  REMARK    GeneRIF: AG1024+U0126 acted synergistically to downregulate
            'synergy' genes, especially STAT6 and PDAP1, which displayed
            significant expression codependency and a common expression pattern
            linked with other key 'synergy' genes, supporting their predicted
            role in an STAT6-ERK-nuclear factor kappa beta (NF-kappaB) network.
            Daunorubicin and PDAP1 loss were synergistic, so PDAP1 is important
            for the response to this anthracycline.
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Sharma,V.K., Singh,A., Srivastava,S.K., Kumar,V., Gardi,N.L.,
            Nalwa,A., Dinda,A.K., Chattopadhyay,P. and Yadav,S.
  TITLE     Increased expression of platelet-derived growth factor associated
            protein-1 is associated with PDGF-B mediated glioma progression
  JOURNAL   Int J Biochem Cell Biol 78, 194-205 (2016)
   PUBMED   27448842
  REMARK    GeneRIF: PDAP-1 as an effecter of PDGF signaling in glioma cells
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 181)
  AUTHORS   LaRochelle,W.J., Jeffers,M., McDonald,W.F., Chillakuru,R.A.,
            Giese,N.A., Lokker,N.A., Sullivan,C., Boldog,F.L., Yang,M.,
            Vernet,C., Burgess,C.E., Fernandes,E., Deegler,L.L., Rittman,B.,
            Shimkets,J., Shimkets,R.A., Rothberg,J.M. and Lichenstein,H.S.
  TITLE     PDGF-D, a new protease-activated growth factor
  JOURNAL   Nat Cell Biol 3 (5), 517-521 (2001)
   PUBMED   11331882
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Fischer,W.H. and Schubert,D.
  TITLE     Characterization of a novel platelet-derived growth
            factor-associated protein
  JOURNAL   J Neurochem 66 (5), 2213-2216 (1996)
   PUBMED   8780057
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI460344.1, BC000684.2,
            AC004922.2 and BC001578.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a phosphoprotein that
            may upregulate the PDGFA-stimulated growth of fibroblasts and also
            downregulate the mitogenicity of PDGFB. The encoded protein in
            rodents has been shown to bind PDGFA with a low affinity. [provided
            by RefSeq, Dec 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.482920.1,
                                           SRR3476690.121608.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000350498.8/ ENSP00000222968.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..181
                     /product="28 kDa heat- and acid-stable phosphoprotein"
                     /note="PDGF-associated protein"
                     /calculated_mol_wt=20499
     Region          1..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13442.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13442.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13442.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13442.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13442.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13442.1)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHX2; propagated from
                     UniProtKB/Swiss-Prot (Q13442.1)"
     Region          85..149
                     /region_name="PP28"
                     /note="Casein kinase substrate phosphoprotein PP28;
                     pfam10252"
                     /db_xref="CDD:463025"
     Site            126
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13442.1)"
     Site            132
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13442.1)"
     Region          151..181
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13442.1)"
     Site            164
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHX2; propagated from
                     UniProtKB/Swiss-Prot (Q13442.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13442.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13442.1)"
     CDS             1..181
                     /gene="PDAP1"
                     /gene_synonym="HASPP28; PAP; PAP1"
                     /coded_by="NM_014891.7:50..595"
                     /db_xref="CCDS:CCDS5662.1"
                     /db_xref="GeneID:11333"
                     /db_xref="HGNC:HGNC:14634"
                     /db_xref="MIM:607075"
ORIGIN      
        1 mpkggrkggh kgrarqytsp eeidaqlqae kqkareeeeq keggdgaagd pkkekkslds
       61 desedeeddy qqkrkgvegl idienpnrva qttkkvtqld ldgpkelsrr ereeiekqka
      121 kerymkmhla gkteqakadl arlaiirkqr eeaarkkeee rkakddatls gkrmqslsln
      181 k
//
LOCUS       NP_001350095             663 aa            linear   ROD 27-APR-2025
DEFINITION  RING finger protein 145 isoform 1 [Mus musculus].
ACCESSION   NP_001350095 XP_006534419
VERSION     NP_001350095.1
DBSOURCE    REFSEQ: accession NM_001363166.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Menzies,S.A., Volkmar,N., van den Boomen,D.J., Timms,R.T.,
            Dickson,A.S., Nathan,J.A. and Lehner,P.J.
  TITLE     The sterol-responsive RNF145 E3 ubiquitin ligase mediates the
            degradation of HMG-CoA reductase together with gp78 and Hrd1
  JOURNAL   Elife 7, e40009 (2018)
   PUBMED   30543180
  REMARK    GeneRIF: n the absence of both RNF145 and gp78, Hrd1, a third
            UBE2G2-dependent E3 ligase, partially regulates HMGCR activity. Our
            findings reveal a critical role for the sterol-responsive RNF145 in
            HMGCR regulation and elucidate the complexity of sterol-accelerated
            HMGCR degradation
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Zhang,L., Rajbhandari,P., Priest,C., Sandhu,J., Wu,X., Temel,R.,
            Castrillo,A., de Aguiar Vallim,T.Q., Sallam,T. and Tontonoz,P.
  TITLE     Inhibition of cholesterol biosynthesis through RNF145-dependent
            ubiquitination of SCAP
  JOURNAL   Elife 6, e28766 (2017)
   PUBMED   29068315
  REMARK    GeneRIF: Mechanistic studies show that RNF145 triggers
            ubiquitination of SCAP on lysine residues within a cytoplasmic loop
            essential for COPII binding, potentially inhibiting its transport
            to Golgi and subsequent processing of SREBP-2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Cook,E.C., Nelson,J.K., Sorrentino,V., Koenis,D., Moeton,M.,
            Scheij,S., Ottenhoff,R., Bleijlevens,B., Loregger,A. and Zelcer,N.
  TITLE     Identification of the ER-resident E3 ubiquitin ligase RNF145 as a
            novel LXR-regulated gene
  JOURNAL   PLoS One 12 (2), e0172721 (2017)
   PUBMED   28231341
  REMARK    GeneRIF: we report the identification of RNF145 as an ER-resident
            E3 ubiquitin ligase that is transcriptionally controlled by LXR.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Graham,D.B., Becker,C.E., Doan,A., Goel,G., Villablanca,E.J.,
            Knights,D., Mok,A., Ng,A.C.Y., Doench,J.G., Root,D.E., Clish,C.B.
            and Xavier,R.J.
  TITLE     Functional genomics identifies negative regulatory nodes
            controlling phagocyte oxidative burst
  JOURNAL   Nat Commun 6, 7838 (2015)
   PUBMED   26194095
  REMARK    GeneRIF: implicated in proteostasis of Nox2 complex
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 663)
  AUTHORS   Gineste,C., De Winter,J.M., Kohl,C., Witt,C.C., Giannesini,B.,
            Brohm,K., Le Fur,Y., Gretz,N., Vilmen,C., Pecchi,E., Jubeau,M.,
            Cozzone,P.J., Stienen,G.J., Granzier,H., Labeit,S.,
            Ottenheijm,C.A., Bendahan,D. and Gondin,J.
  TITLE     In vivo and in vitro investigations of heterozygous nebulin
            knock-out mice disclose a mild skeletal muscle phenotype
  JOURNAL   Neuromuscul Disord 23 (4), 357-369 (2013)
   PUBMED   23375831
REFERENCE   7  (residues 1 to 663)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 663)
  AUTHORS   Mager,J., Schultz,R.M., Brunk,B.P. and Bartolomei,M.S.
  TITLE     Identification of candidate maternal-effect genes through
            comparison of multiple microarray data sets
  JOURNAL   Mamm Genome 17 (9), 941-949 (2006)
   PUBMED   16964442
REFERENCE   9  (residues 1 to 663)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL603913.14.
            
            On May 10, 2018 this sequence version replaced XP_006534419.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.169141.1,
                                           SRR3224856.8064.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 25.94 cM"
     Protein         1..663
                     /product="RING finger protein 145 isoform 1"
                     /EC_number="2.3.2.27"
                     /calculated_mol_wt=74517
     Region          8..506
                     /region_name="TRC8_N"
                     /note="TRC8 N-terminal domain; pfam13705"
                     /db_xref="CDD:463960"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Region          81..84
                     /region_name="YLYF motif.
                     /evidence=ECO:0000269|PubMed:29374057"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            123..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            146..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            168..188
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            205..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            316..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            340..360
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            410..430
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            460..480
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            482..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Region          <520..627
                     /region_name="HRD1"
                     /note="HRD ubiquitin ligase complex, ER membrane component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5243"
                     /db_xref="CDD:227568"
     Region          533..575
                     /region_name="RING-H2_RNF145"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 145 (RNF145) and similar proteins; cd16684"
                     /db_xref="CDD:319598"
     Region          587..663
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     CDS             1..663
                     /gene="Rnf145"
                     /gene_synonym="3732413I11Rik; TMRF1"
                     /coded_by="NM_001363166.1:243..2234"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS24565.1"
                     /db_xref="GeneID:74315"
                     /db_xref="MGI:MGI:1921565"
ORIGIN      
        1 maakekleav lnvalrvpsi mlldvlyrwd vssffqqiqr sslnnnplfq ykylalnmhy
       61 vgyilsvvll tlprqhlvql ylyfvtalll yaghqisrdy vrselesaye gpmyleplsm
      121 nrfttaligq lvvctlcscv mktkqiwlfs ahmlpllarl clvpletivi inkfamiftg
      181 levlyflgsn llvpynlaks ayrelvqvve vygllalgms lwnqlvvpvl fmvfwlvlfa
      241 lqiysyfstr dqpasrerll flfltsiaec cstpysllgl vftvsfvalg vltlckfylq
      301 gyrafmndpa mnrgmtegvt llilavqtgl ielqvvhraf llsiilfivv asilqsmlei
      361 adpivlalga srdkslwkhf ravslclfll vfpaymaymi cqffhmdfwl liiisssilt
      421 slqvlgtlfi yvlfmveefr kepvenmddv iyyvngtyrl lefvvalcvv aygvsetifg
      481 ewtvmgsmii fihsyynvwl raqlgwksfl lrrdavnkik slpvatqeql ekhndicaic
      541 yqdmksavit pcshffhagc lkkwlyvqdt cplchchlkn ssqlpglgte aapqppagae
      601 qnivlqegpe ppdhesppgt gtqegsgdss ehinrgsasq egaadagegp qipegevcpv
      661 esa
//
LOCUS       NP_001352749             913 aa            linear   PRI 27-APR-2025
DEFINITION  type II inositol 1,4,5-trisphosphate 5-phosphatase isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001352749
VERSION     NP_001352749.1
DBSOURCE    REFSEQ: accession NM_001365820.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Droubi,A., Wallis,C., Anderson,K.E., Rahman,S., de Sa,A.,
            Rahman,T., Stephens,L.R., Hawkins,P.T. and Lowe,M.
  TITLE     The inositol 5-phosphatase INPP5B regulates B cell receptor
            clustering and signaling
  JOURNAL   J Cell Biol 221 (9) (2022)
   PUBMED   35878408
  REMARK    GeneRIF: The inositol 5-phosphatase INPP5B regulates B cell
            receptor clustering and signaling.
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Nakatsu,F., Messa,M., Nandez,R., Czapla,H., Zou,Y.,
            Strittmatter,S.M. and De Camilli,P.
  TITLE     Sac2/INPP5F is an inositol 4-phosphatase that functions in the
            endocytic pathway
  JOURNAL   J Cell Biol 209 (1), 85-95 (2015)
   PUBMED   25869668
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Montjean,R., Aoidi,R., Desbois,P., Rucci,J., Trichet,M.,
            Salomon,R., Rendu,J., Faure,J., Lunardi,J., Gacon,G., Billuart,P.
            and Dorseuil,O.
  TITLE     OCRL-mutated fibroblasts from patients with Dent-2 disease exhibit
            INPP5B-independent phenotypic variability relatively to Lowe
            syndrome cells
  JOURNAL   Hum Mol Genet 24 (4), 994-1006 (2015)
   PUBMED   25305077
  REMARK    GeneRIF: OCRL-mutated fibroblasts from patients with Dent-2 disease
            exhibit INPP5B-independent phenotypic variability relatively to
            Lowe syndrome cells
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Pirruccello,M., Nandez,R., Idevall-Hagren,O., Alcazar-Roman,A.,
            Abriola,L., Berwick,S.A., Lucast,L., Morel,D. and De Camilli,P.
  TITLE     Identification of inhibitors of inositol 5-phosphatases through
            multiple screening strategies
  JOURNAL   ACS Chem Biol 9 (6), 1359-1368 (2014)
   PUBMED   24742366
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Tresaugues,L., Silvander,C., Flodin,S., Welin,M., Nyman,T.,
            Graslund,S., Hammarstrom,M., Berglund,H. and Nordlund,P.
  TITLE     Structural basis for phosphoinositide substrate recognition,
            catalysis, and membrane interactions in human inositol
            polyphosphate 5-phosphatases
  JOURNAL   Structure 22 (5), 744-755 (2014)
   PUBMED   24704254
  REMARK    GeneRIF: The crystal structures of human INPP5B in complex with
            phosphoinositide substrate analogs revealed a membrane interaction
            patch likely to assist in sequestering substrates from the lipid
            bilayer.
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Speed,C.J., Matzaris,M., Bird,P.I. and Mitchell,C.A.
  TITLE     Tissue distribution and intracellular localisation of the 75-kDa
            inositol polyphosphate 5-phosphatase
  JOURNAL   Eur J Biochem 234 (1), 216-224 (1995)
   PUBMED   8529643
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Jefferson,A.B. and Majerus,P.W.
  TITLE     Properties of type II inositol polyphosphate 5-phosphatase
  JOURNAL   J Biol Chem 270 (16), 9370-9377 (1995)
   PUBMED   7721860
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Janne,P.A., Dutra,A.S., Dracopoli,N.C., Charnas,L.R., Puck,J.M. and
            Nussbaum,R.L.
  TITLE     Localization of the 75-kDa inositol polyphosphate-5-phosphatase
            (INPP5B) to human chromosome band 1p34
  JOURNAL   Cytogenet Cell Genet 66 (3), 164-166 (1994)
   PUBMED   8125013
REFERENCE   9  (residues 1 to 913)
  AUTHORS   Ross,T.S., Jefferson,A.B., Mitchell,C.A. and Majerus,P.W.
  TITLE     Cloning and expression of human 75-kDa inositol
            polyphosphate-5-phosphatase
  JOURNAL   J Biol Chem 266 (30), 20283-20289 (1991)
   PUBMED   1718960
REFERENCE   10 (residues 1 to 913)
  AUTHORS   Mitchell,C.A., Connolly,T.M. and Majerus,P.W.
  TITLE     Identification and isolation of a 75-kDa inositol
            polyphosphate-5-phosphatase from human platelets
  JOURNAL   J Biol Chem 264 (15), 8873-8877 (1989)
   PUBMED   2542294
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL603790.41 and AL929472.21.
            
            Summary: This gene encodes a member of a family of inositol
            polyphosphate-5-phosphatases. These enzymes function in the
            regulation of calcium signaling by inactivating inositol
            phosphates. The encoded protein is localized to the cytosol and
            mitochondria, and associates with membranes through an isoprenyl
            modification near the C-terminus. Alternatively spliced transcript
            variants of this gene have been described. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (5), as well as variant 1, encodes
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..913
                     /product="type II inositol 1,4,5-trisphosphate
                     5-phosphatase isoform 1 precursor"
                     /EC_number="3.1.3.36"
                     /note="phosphoinositide 5-phosphatase; type II inositol
                     1,4,5-trisphosphate 5-phosphatase; inositol
                     polyphosphate-5-phosphatase, 75kDa"
                     /calculated_mol_wt=103857
     Region          1..146
                     /region_name="INPP5B_PH"
                     /note="Type II inositol 1,4,5-trisphosphate 5-phosphatase
                     PH domain; pfam16776"
                     /db_xref="CDD:465268"
     Region          265..558
                     /region_name="INPP5c_INPP5B"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of Type II inositol polyphosphate
                     5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and
                     related proteins; cd09093"
                     /db_xref="CDD:197327"
     Site            order(273,275,303,306,308,311,373,379..380,400,403..404,
                     447,449,451,502..503,516,518,524,548..549)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197327"
     Site            order(273,303,400,447,449,524,548..549)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197327"
     Site            order(275,303,548)
                     /site_type="other"
                     /note="Mg binding site [ion binding]"
                     /db_xref="CDD:197327"
     Site            order(303,306,308,311,373,379..380,400,403..404,451,
                     502..503,516,518,548)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197327"
     Site            order(400,449,549)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197327"
     Region          692..912
                     /region_name="RhoGAP_OCRL1"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain present in OCRL1-like proteins.
                     OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins
                     contain two conserved domains: a central inositol
                     polyphosphate 5-phosphatase domain and...; cd04380"
                     /db_xref="CDD:239845"
     Site            order(772,807,811,874,877..878,903)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239845"
     Site            772
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239845"
     CDS             1..913
                     /gene="INPP5B"
                     /gene_synonym="5PTase"
                     /coded_by="NM_001365820.1:123..2864"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS41306.1"
                     /db_xref="GeneID:3633"
                     /db_xref="HGNC:HGNC:6077"
                     /db_xref="MIM:147264"
ORIGIN      
        1 mdqsvaiqet laegeycvia vqgvlcegds rqsrllglvr yrlehggqeh alflythrrm
       61 aitgddvsld qivpvsrdft leevspdgel yilgsdvtvq ldtaelslvf qlpfgsqtrm
      121 flhevaracp gfdsatrdpe flwlsryrca elelemptpr gcnsalvtwp gyatiggggs
      181 nfdglrpngk gvpmdqssrg qdkpeslqpr qnkskseitd mvrsstitvs dkahilsmqk
      241 fglrdtivks hllqkeedyt yiqnfrffag tynvngqspk eclrlwlsng iqapdvycvg
      301 fqeldlskea fffhdtpkee ewfkavsegl hpdakyakvk lirlvgimll lyvkqehaay
      361 iseveaetvg tgimgrmgnk ggvairfqfh ntsicvvnsh laahieeyer rnqdykdics
      421 rmqfcqpdps lppltisnhd vilwlgdlny rieeldvekv kklieekdfq mlyaydqlki
      481 qvaaktvfeg ftegeltfqp tykydtgsdd wdtsekcrap awcdrilwkg knitqlsyqs
      541 hmalktsdhk pvssvfdigv rvvndelyrk tleeivrsld kmenanipsv slskrefcfq
      601 nvkymqlkve sftihngqvp chfefinkpd eesyckqwln anpsrgfllp dsdveidlel
      661 fvnkmtatkl nsgedkiedi lvlhldrgkd yflsvsgnyl pscfgspiht lcymrepild
      721 lpletiselt lmpvwtgddg sqldspmeip kelwmmvdyl yrnavqqedl fqqpglrsef
      781 ehirdcldtg midnlsasnh svaealllfl eslpepvicy styhnclecs gnytaskqvi
      841 stlpifhknv fhylmaflre llknsaknhl denilasifg slllrnpagh qkldmtekkk
      901 aqefihqflc npl
//
LOCUS       NP_061129                136 aa            linear   PRI 27-APR-2025
DEFINITION  cytokine-like protein 1 precursor [Homo sapiens].
ACCESSION   NP_061129
VERSION     NP_061129.1
DBSOURCE    REFSEQ: accession NM_018659.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Zhou,F., Lin,Q. and Zheng,Z.
  TITLE     Cytokine-Like Protein 1 (CYTL1) as a Key Target of M-Stage Immune
            Infiltration in Stomach Adenocarcinoma
  JOURNAL   Biomed Res Int 2023, 2926218 (2023)
   PUBMED   36825034
  REMARK    GeneRIF: Cytokine-Like Protein 1 (CYTL1) as a Key Target of M-Stage
            Immune Infiltration in Stomach Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Xue,W., Li,X., Li,W., Wang,Y., Jiang,C., Zhou,L., Gao,J., Yu,Y.,
            Shen,Y. and Xu,Q.
  TITLE     Intracellular CYTL1, a novel tumor suppressor, stabilizes NDUFV1 to
            inhibit metabolic reprogramming in breast cancer
  JOURNAL   Signal Transduct Target Ther 7 (1), 35 (2022)
   PUBMED   35115484
  REMARK    GeneRIF: Intracellular CYTL1, a novel tumor suppressor, stabilizes
            NDUFV1 to inhibit metabolic reprogramming in breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Sevin,M., Debeurme,F., Laplane,L., Badel,S., Morabito,M.,
            Newman,H.L., Torres-Martin,M., Yang,Q., Badaoui,B.,
            Wagner-Ballon,O., Saada,V., Selimoglu-Buet,D., Kraus-Berthier,L.,
            Banquet,S., Derreal,A., Fenaux,P., Itzykson,R., Braun,T.,
            Etienne,G., Berthon,C., Thepot,S., Kepp,O., Kroemer,G., Padron,E.,
            Figueroa,M.E., Droin,N. and Solary,E.
  TITLE     Cytokine-like protein 1-induced survival of monocytes suggests a
            combined strategy targeting MCL1 and MAPK in CMML
  JOURNAL   Blood 137 (24), 3390-3402 (2021)
   PUBMED   33690800
  REMARK    GeneRIF: Cytokine-like protein 1-induced survival of monocytes
            suggests a combined strategy targeting MCL1 and MAPK in CMML.
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Zhu,W., Yang,X., Liu,S., Wang,M., Ye,S., Luo,H. and Cui,S.
  TITLE     The involvement of cytokine-like 1 (Cytl1) in chondrogenesis and
            cartilage metabolism
  JOURNAL   Biochem Biophys Res Commun 529 (3), 608-614 (2020)
   PUBMED   32736681
  REMARK    GeneRIF: The involvement of cytokine-like 1 (Cytl1) in
            chondrogenesis and cartilage metabolism.
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Zhu,S., Kuek,V., Bennett,S., Xu,H., Rosen,V. and Xu,J.
  TITLE     Protein Cytl1: its role in chondrogenesis, cartilage homeostasis,
            and disease
  JOURNAL   Cell Mol Life Sci 76 (18), 3515-3523 (2019)
   PUBMED   31089746
  REMARK    Review article
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Deng,X., Zhao,H.S., Peng,Z., Deng,W.W., Li,N., Guo,S. and Shi,T.P.
  TITLE     [Study on the mechanism of C17orf62 induced cell death]
  JOURNAL   Beijing Da Xue Xue Bao Yi Xue Ban 43 (2), 168-172 (2011)
   PUBMED   21503106
  REMARK    GeneRIF: C17orf62-L could induce cell death accompanied with rising
            of cleaved PARP.
REFERENCE   7  (residues 1 to 136)
  AUTHORS   Tomczak,A. and Pisabarro,M.T.
  TITLE     Identification of CCR2-binding features in Cytl1 by a CCL2-like
            chemokine model
  JOURNAL   Proteins 79 (4), 1277-1292 (2011)
   PUBMED   21322034
  REMARK    GeneRIF: We report a structural-functional characterization of
            cytokine-like protein 1 (Cytl1) by a combination of different
            computational structure-based techniques.
REFERENCE   8  (residues 1 to 136)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   9  (residues 1 to 136)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 136)
  AUTHORS   Liu,X., Rapp,N., Deans,R. and Cheng,L.
  TITLE     Molecular cloning and chromosomal mapping of a candidate cytokine
            gene selectively expressed in human CD34+ cells
  JOURNAL   Genomics 65 (3), 283-292 (2000)
   PUBMED   10857752
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC108139.5.
            
            Summary: C17 is a cytokine-like protein specifically expressed in
            bone marrow and cord blood mononuclear cells that bear the CD34
            (MIM 142230) surface marker (Liu et al., 2000 [PubMed
            10857752]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC031391.1, AF193766.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307746.9/ ENSP00000303550.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.2"
     Protein         1..136
                     /product="cytokine-like protein 1 precursor"
                     /note="cytokine-like protein C17; cytokine-like protein 1"
                     /calculated_mol_wt=13371
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2225
     Region          21..133
                     /region_name="CYTL1"
                     /note="Cytokine-like protein 1; pfam15153"
                     /db_xref="CDD:434505"
     mat_peptide     23..136
                     /product="Cytokine-like protein 1. /id=PRO_0000020838"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRR1.1)"
                     /calculated_mol_wt=13371
     CDS             1..136
                     /gene="CYTL1"
                     /gene_synonym="C17; C4orf4"
                     /coded_by="NM_018659.3:14..424"
                     /db_xref="CCDS:CCDS3379.1"
                     /db_xref="GeneID:54360"
                     /db_xref="HGNC:HGNC:24435"
                     /db_xref="MIM:607930"
ORIGIN      
        1 mrtpgplpvl llllagapaa rptpptcysr mralsqeitr dfnllqvsep sepcvrylpr
       61 lyldihnycv ldklrdfvas ppcwkvaqvd slkdkarkly timnsfcrrd lvfllddcna
      121 leypipvttv lpdrqr
//
LOCUS       NP_001137146             127 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial pyruvate carrier 2 [Homo sapiens].
ACCESSION   NP_001137146
VERSION     NP_001137146.1
DBSOURCE    REFSEQ: accession NM_001143674.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Pujol,C., Lebigot,E., Gaignard,P., Galai,S., Kraoua,I., Bault,J.P.,
            Dard,R., Youssef-Turki,I.B., Omar,S., Boutron,A., Wai,T. and
            Slama,A.
  TITLE     MPC2 variants disrupt mitochondrial pyruvate metabolism and cause
            an early-onset mitochondriopathy
  JOURNAL   Brain 146 (3), 858-864 (2023)
   PUBMED   36417180
  REMARK    GeneRIF: MPC2 variants disrupt mitochondrial pyruvate metabolism
            and cause an early-onset mitochondriopathy.
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Tavoulari,S., Schirris,T.J.J., Mavridou,V., Thangaratnarajah,C.,
            King,M.S., Jones,D.T.D., Ding,S., Fearnley,I.M. and Kunji,E.R.S.
  TITLE     Key features of inhibitor binding to the human mitochondrial
            pyruvate carrier hetero-dimer
  JOURNAL   Mol Metab 60, 101469 (2022)
   PUBMED   35278701
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Xu,L., Phelix,C.F. and Chen,L.Y.
  TITLE     Structural Insights into the Human Mitochondrial Pyruvate Carrier
            Complexes
  JOURNAL   J Chem Inf Model 61 (11), 5614-5625 (2021)
   PUBMED   34664967
  REMARK    GeneRIF: Structural Insights into the Human Mitochondrial Pyruvate
            Carrier Complexes.
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Bricker,D.K., Taylor,E.B., Schell,J.C., Orsak,T., Boutron,A.,
            Chen,Y.C., Cox,J.E., Cardon,C.M., Van Vranken,J.G., Dephoure,N.,
            Redin,C., Boudina,S., Gygi,S.P., Brivet,M., Thummel,C.S. and
            Rutter,J.
  TITLE     A mitochondrial pyruvate carrier required for pyruvate uptake in
            yeast, Drosophila, and humans
  JOURNAL   Science 337 (6090), 96-100 (2012)
   PUBMED   22628558
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Shi,Y., Li,Z., Xu,Q., Wang,T., Li,T., Shen,J., Zhang,F., Chen,J.,
            Zhou,G., Ji,W., Li,B., Xu,Y., Liu,D., Wang,P., Yang,P., Liu,B.,
            Sun,W., Wan,C., Qin,S., He,G., Steinberg,S., Cichon,S., Werge,T.,
            Sigurdsson,E., Tosato,S., Palotie,A., Nothen,M.M., Rietschel,M.,
            Ophoff,R.A., Collier,D.A., Rujescu,D., Clair,D.S., Stefansson,H.,
            Stefansson,K., Ji,J., Wang,Q., Li,W., Zheng,L., Zhang,H., Feng,G.
            and He,L.
  TITLE     Common variants on 8p12 and 1q24.2 confer risk of schizophrenia
  JOURNAL   Nat Genet 43 (12), 1224-1227 (2011)
   PUBMED   22037555
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 127)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Tsou,A.P., Lai,C., Danielson,P., Noonan,D.J. and Sutcliffe,J.G.
  TITLE     Structural characterization of a heterogeneous family of rat brain
            mRNAs
  JOURNAL   Mol Cell Biol 6 (3), 768-778 (1986)
   PUBMED   3022128
  REMARK    GeneRIF: characterization of the rat ortholog
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            KF455056.1, AL035304.1 and Z97876.1.
            
            Transcript Variant: This variant (1) encodes a functional protein.
            Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.374384.1,
                                           SRR5189667.392642.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000271373.9/
                                                  ENSP00000271373.4
            RefSeq Select criteria             :: based on conservation,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..127
                     /product="mitochondrial pyruvate carrier 2"
                     /note="brain protein 44"
                     /calculated_mol_wt=14148
     Region          27..125
                     /region_name="MPC"
                     /note="Mitochondrial pyruvate carriers; pfam03650"
                     /db_xref="CDD:427425"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95563.1)"
     Site            73..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95563.1)"
     Site            96..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95563.1)"
     CDS             1..127
                     /gene="MPC2"
                     /gene_synonym="BRP44; SLC54A2"
                     /coded_by="NM_001143674.4:192..575"
                     /db_xref="CCDS:CCDS1266.1"
                     /db_xref="GeneID:25874"
                     /db_xref="HGNC:HGNC:24515"
                     /db_xref="MIM:614737"
ORIGIN      
        1 msaagarglr atyhrlldkv elmlpeklrp lynhpagprt vffwapimkw glvcagladm
       61 arpaeklsta qsavlmatgf iwsryslvii pknwslfavn ffvgaagasq lfriwrynqe
      121 lkakahk
//
LOCUS       NP_060441                149 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein bL20m isoform 1 [Homo sapiens].
ACCESSION   NP_060441 XP_001125910 XP_935879 XP_935902
VERSION     NP_060441.2
DBSOURCE    REFSEQ: accession NM_017971.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 149)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   7  (residues 1 to 149)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   8  (residues 1 to 149)
  AUTHORS   Koc,E.C., Burkhart,W., Blackburn,K., Moyer,M.B., Schlatzer,D.M.,
            Moseley,A. and Spremulli,L.L.
  TITLE     The large subunit of the mammalian mitochondrial ribosome. Analysis
            of the complement of ribosomal proteins present
  JOURNAL   J Biol Chem 276 (47), 43958-43969 (2001)
   PUBMED   11551941
REFERENCE   9  (residues 1 to 149)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   10 (residues 1 to 149)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Structural compensation for the deficit of rRNA with proteins in
            the mammalian mitochondrial ribosome. Systematic analysis of
            protein components of the large ribosomal subunit from mammalian
            mitochondria
  JOURNAL   J Biol Chem 276 (24), 21724-21736 (2001)
   PUBMED   11279069
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG700526.1, BC009515.1 and
            AW015403.1.
            
            On or before May 22, 2007 this sequence version replaced
            XP_935902.2, XP_001125910.1, XP_935879.1, NP_060441.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein. A pseudogene
            corresponding to this gene is found on chromosome 21q. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.386128.1,
                                           SRR1163658.400595.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147920, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000344843.12/
                                                  ENSP00000341082.7
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..149
                     /product="large ribosomal subunit protein bL20m isoform 1"
                     /note="39S ribosomal protein L20, mitochondrial;
                     mitochondrial large ribosomal subunit protein bL20m"
                     /calculated_mol_wt=17311
     Region          13..118
                     /region_name="Ribosomal_L20"
                     /note="Ribosomal protein L20; cd07026"
                     /db_xref="CDD:197305"
     Site            order(13..18,20..23,28..35,37..40,43..44,48..49,52..66,
                     68..70,73,77,83..84,87..88,91,99..101)
                     /site_type="other"
                     /note="23S rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:197305"
     Site            order(43,47,50..51,53..54,57,96..99,102,108..109,115..116)
                     /site_type="other"
                     /note="L21 binding site [polypeptide binding]"
                     /db_xref="CDD:197305"
     Site            order(64,67..68,71,74..75,77,101,104,107)
                     /site_type="other"
                     /note="L13 binding site [polypeptide binding]"
                     /db_xref="CDD:197305"
     CDS             1..149
                     /gene="MRPL20"
                     /gene_synonym="bL20m; L20mt; MRP-L20"
                     /coded_by="NM_017971.4:77..526"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS26.1"
                     /db_xref="GeneID:55052"
                     /db_xref="HGNC:HGNC:14478"
                     /db_xref="MIM:611833"
ORIGIN      
        1 mvfltaqlwl rnrvtdryfr iqevlkharh frgrknrcyr lavrtviraf vkctkarylk
       61 kknmrtlwin ritaasqehg lkypalignl vkcqvelnrk vladlaiyep ktfkslaala
      121 srrrhegfaa algdgkepeg ifsrvvqyh
//
LOCUS       NP_001354753            1015 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 18 isoform a [Homo sapiens].
ACCESSION   NP_001354753 XP_006722771
VERSION     NP_001354753.1
DBSOURCE    REFSEQ: accession NM_001367824.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Li,D., Sun,Y., Kong,X., Luan,C., Yu,Y., Chen,F. and Chen,P.
  TITLE     Association between a Single Nucleotide Polymorphism in the 3'-UTR
            of ARHGEF18 and the Risk of Nonidiopathic Pulmonary Arterial
            Hypertension in Chinese Population
  JOURNAL   Dis Markers 2018, 2461845 (2018)
   PUBMED   30405854
  REMARK    GeneRIF: ARHGEF18 rs3745357 variant is associated with
            nonidiopathic pulmonary arterial hypertension susceptibility in
            Chinese population.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Turton,K.B., Wilkerson,E.M., Hebert,A.S., Fogerty,F.J.,
            Schira,H.M., Botros,F.E., Coon,J.J. and Mosher,D.F.
  TITLE     Expression of novel 'LOCGEF' isoforms of ARHGEF18 in eosinophils
  JOURNAL   J Leukoc Biol 104 (1), 135-145 (2018)
   PUBMED   29601110
  REMARK    GeneRIF: We suggest that a portion of a 1361-residue isoform of
            ARHGEF18, which is unlike any other protein domain, has unique
            functions in control of polarity in activated eosinophils and other
            leukocytes
REFERENCE   4  (residues 1 to 1015)
  AUTHORS   Arno,G., Carss,K.J., Hull,S., Zihni,C., Robson,A.G., Fiorentino,A.,
            Hardcastle,A.J., Holder,G.E., Cheetham,M.E., Plagnol,V.,
            Moore,A.T., Raymond,F.L., Matter,K., Balda,M.S. and Webster,A.R.
  CONSRTM   UK Inherited Retinal Disease Consortium; NIHR Bioresource - Rare
            Diseases Consortium
  TITLE     Biallelic Mutation of ARHGEF18, Involved in the Determination of
            Epithelial Apicobasal Polarity, Causes Adult-Onset Retinal
            Degeneration
  JOURNAL   Am J Hum Genet 100 (2), 334-342 (2017)
   PUBMED   28132693
  REMARK    GeneRIF: mutation of ARHGEF18 is a likely cause of inherited
            retinal dystrophy
REFERENCE   5  (residues 1 to 1015)
  AUTHORS   Loie,E., Charrier,L.E., Sollier,K., Masson,J.Y. and Laprise,P.
  TITLE     CRB3A Controls the Morphology and Cohesion of Cancer Cells through
            Ehm2/p114RhoGEF-Dependent Signaling
  JOURNAL   Mol Cell Biol 35 (19), 3423-3435 (2015)
   PUBMED   26217016
  REMARK    GeneRIF: CRB3A recruits p114RhoGEF and its activator Ehm2 to the
            cell periphery using both functional motifs of its cytoplasmic tail
            and increases RhoA activation levels.
REFERENCE   6  (residues 1 to 1015)
  AUTHORS   Rabizadeh,S. and Bredesen,D.E.
  TITLE     Ten years on: mediation of cell death by the common neurotrophin
            receptor p75(NTR)
  JOURNAL   Cytokine Growth Factor Rev 14 (3-4), 225-239 (2003)
   PUBMED   12787561
  REMARK    Review article
REFERENCE   7  (residues 1 to 1015)
  AUTHORS   Salehi,A.H., Xanthoudakis,S. and Barker,P.A.
  TITLE     NRAGE, a p75 neurotrophin receptor-interacting protein, induces
            caspase activation and cell death through a JNK-dependent
            mitochondrial pathway
  JOURNAL   J Biol Chem 277 (50), 48043-48050 (2002)
   PUBMED   12376548
REFERENCE   8  (residues 1 to 1015)
  AUTHORS   Harrington,A.W., Kim,J.Y. and Yoon,S.O.
  TITLE     Activation of Rac GTPase by p75 is necessary for c-jun N-terminal
            kinase-mediated apoptosis
  JOURNAL   J Neurosci 22 (1), 156-166 (2002)
   PUBMED   11756498
REFERENCE   9  (residues 1 to 1015)
  AUTHORS   Acierno,J.S. Jr., Kennedy,J.C., Falardeau,J.L., Leyne,M.,
            Bromley,M.C., Colman,M.W., Sun,M., Bove,C., Ashworth,L.K.,
            Chadwick,L.H., Schiripo,T., Ma,S., Goldin,E., Schiffmann,R. and
            Slaugenhaupt,S.A.
  TITLE     A physical and transcript map of the MCOLN1 gene region on human
            chromosome 19p13.3-p13.2
  JOURNAL   Genomics 73 (2), 203-210 (2001)
   PUBMED   11318610
REFERENCE   10 (residues 1 to 1015)
  AUTHORS   Blomquist,A., Schworer,G., Schablowski,H., Psoma,A., Lehnen,M.,
            Jakobs,K.H. and Rumenapp,U.
  TITLE     Identification and characterization of a novel Rho-specific guanine
            nucleotide exchange factor
  JOURNAL   Biochem J 352 Pt 2 (Pt 2), 319-325 (2000)
   PUBMED   11085924
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC119396.3 and AC008878.10.
            
            On Dec 19, 2018 this sequence version replaced XP_006722771.1.
            
            Summary: Rho GTPases are GTP binding proteins that regulate a wide
            spectrum of cellular functions. These cellular processes include
            cytoskeletal rearrangements, gene transcription, cell growth and
            motility. Activation of Rho GTPases is under the direct control of
            guanine nucleotide exchange factors (GEFs). The protein encoded by
            this gene is a guanine nucleotide exchange factor and belongs to
            the Rho GTPase GEF family. Family members share a common feature, a
            Dbl (DH) homology domain followed by a pleckstrin (PH) homology
            domain. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Nov
            2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB011093.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1015
                     /product="rho guanine nucleotide exchange factor 18
                     isoform a"
                     /note="Rho-specific guanine nucleotide exchange factor
                     p114; septin-associated RhoGEF; 114 kDa Rho-specific
                     guanine nucleotide exchange factor; Rho/Rac guanine
                     nucleotide exchange factor (GEF) 18"
                     /calculated_mol_wt=113946
     Region          102..296
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(108,112,219,247..248,251..252,254..255,258..259,
                     262..263,266,292,296)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          336..454
                     /region_name="PH_ARHGEF18"
                     /note="Rho guanine nucleotide exchange factor 18
                     Pleckstrin homology (PH) domain; cd15794"
                     /db_xref="CDD:275437"
     Region          <642..>788
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          738..>882
                     /region_name="PRK13729"
                     /note="conjugal transfer pilus assembly protein TraB;
                     Provisional"
                     /db_xref="CDD:184281"
     CDS             1..1015
                     /gene="ARHGEF18"
                     /gene_synonym="P114-RhoGEF; p114RhoGEF; RP78; SA-RhoGEF"
                     /coded_by="NM_001367824.1:330..3377"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS12177.1"
                     /db_xref="GeneID:23370"
                     /db_xref="HGNC:HGNC:17090"
                     /db_xref="MIM:616432"
ORIGIN      
        1 mtvsqkggpq ptpspagpgt qlgpitgemd eadsaflkfk qtaddslslt spntesifve
       61 dpytaslrse iesdghefea eswslavdaa yakkqkrevv krqdvlyelm qtevhhvrtl
      121 kimlkvysra lqeelqfssk aigrlfpcad dllethshfl arlkerrqes leegsdrnyv
      181 iqkigdllvq qfsgengerm kekygvfcsg hneavshykl llqqnkkfqn likkignfsi
      241 vrrlgvqeci llvtqritky pvlveriiqn teagtedyed ltqalnlikd iisqvdakvs
      301 ecekgqrlre iagkmdlkss sklkngltfr kedmlqrqlh legmlcwktt sgrlkdilai
      361 lltdvllllq ekdqkyvfas vdskppvisl qklivrevan eekamflisa slqgpemyei
      421 ytsskedrna wmahiqrave scpdeeegpf slpeeerkvv earatrlrdf qerlsmkdql
      481 iaqsllekqq iylemaemgg ledlpqprgl frggdpsetl qgelilksam seiegiqsli
      541 crqlgsangq aedggsstgp prraetfagy dctnsptkng sfkkkvsstd prprdwrgpp
      601 nspdlklsds dipgsseesp qvveapgtes dprlptvles elvqriqtls qlllnlqavi
      661 ahqdsyvetq raaiqerekq frlqstrgnl lleqerqrnf ekqreeraal eklqsqlrhe
      721 qqrwererqw qhqeleraga rlqeregear qlrerleqer aelerqrqay qhdlerlrea
      781 qravererer lellrrlkkq ntapgalppd tlaeaqppsh ppsfngegle gprvsmlpsg
      841 vgpeyaerpe varrdsapte nrlaksdvpi qllsatnqfq rqaavqqqip tklaastkgg
      901 kdkggksrgs qrwessasfd lkqqlllnkl mgkdestsrn rrslspilpg rhspapppdp
      961 gfpapspppa dspsegfslk aggtallpgp papsplpatp lsakedaske dviff
//
LOCUS       NP_878919                498 aa            linear   PRI 27-APR-2025
DEFINITION  metalloreductase STEAP3 isoform a [Homo sapiens].
ACCESSION   NP_878919
VERSION     NP_878919.2
DBSOURCE    REFSEQ: accession NM_182915.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Lv,J., Liu,X., Sun,Z., Gao,J., Yu,X., Zhang,M., Zhang,Z., Ren,S.
            and Zuo,Y.
  TITLE     STEAP3 promotes colon cancer cell proliferation and migration via
            regulating histone acetylation
  JOURNAL   Hum Genet 143 (3), 343-355 (2024)
   PUBMED   38480539
  REMARK    GeneRIF: STEAP3 promotes colon cancer cell proliferation and
            migration via regulating histone acetylation.
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Han,Y., Fu,L., Kong,Y., Jiang,C., Huang,L. and Zhang,H.
  TITLE     STEAP3 Affects Ovarian Cancer Progression by Regulating Ferroptosis
            through the p53/SLC7A11 Pathway
  JOURNAL   Mediators Inflamm 2024, 4048527 (2024)
   PUBMED   38440354
  REMARK    GeneRIF: STEAP3 Affects Ovarian Cancer Progression by Regulating
            Ferroptosis through the p53/SLC7A11 Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Ding,T., Chen,S., Xiao,W., Liu,Z., Tu,J., Yu,Y., Dong,B., Chen,W.
            and Zeng,Y.
  TITLE     Six-Transmembrane Epithelial Antigen of Prostate 3 Promotes Hepatic
            Insulin Resistance and Steatosis
  JOURNAL   J Lipid Res 64 (1), 100318 (2023)
   PUBMED   36495944
  REMARK    GeneRIF: Six-Transmembrane Epithelial Antigen of Prostate 3
            Promotes Hepatic Insulin Resistance and Steatosis.
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Ye,C.L., Du,Y., Yu,X., Chen,Z.Y., Wang,L., Zheng,Y.F. and Liu,X.H.
  TITLE     STEAP3 Affects Ferroptosis and Progression of Renal Cell Carcinoma
            Through the p53/xCT Pathway
  JOURNAL   Technol Cancer Res Treat 21, 15330338221078728 (2022)
   PUBMED   35275508
  REMARK    GeneRIF: STEAP3 Affects Ferroptosis and Progression of Renal Cell
            Carcinoma Through the p53/xCT Pathway.
REFERENCE   5  (residues 1 to 498)
  AUTHORS   Grunewald,T.G., Bach,H., Cossarizza,A. and Matsumoto,I.
  TITLE     The STEAP protein family: versatile oxidoreductases and targets for
            cancer immunotherapy with overlapping and distinct cellular
            functions
  JOURNAL   Biol Cell 104 (11), 641-657 (2012)
   PUBMED   22804687
REFERENCE   6  (residues 1 to 498)
  AUTHORS   Lu,Y., Zhang,X., Beheshti,B. and Zhang,J.
  TITLE     Adenoviral-mediated pHyde gene transfer and cisplatin additively
            inhibit human prostate cancer growth by enhancing apoptosis
  JOURNAL   Prostate 69 (3), 234-248 (2009)
   PUBMED   19016247
REFERENCE   7  (residues 1 to 498)
  AUTHORS   Passer,B.J., Nancy-Portebois,V., Amzallag,N., Prieur,S., Cans,C.,
            Roborel de Climens,A., Fiucci,G., Bouvard,V., Tuynder,M.,
            Susini,L., Morchoisne,S., Crible,V., Lespagnol,A., Dausset,J.,
            Oren,M., Amson,R. and Telerman,A.
  TITLE     The p53-inducible TSAP6 gene product regulates apoptosis and the
            cell cycle and interacts with Nix and the Myt1 kinase
  JOURNAL   Proc Natl Acad Sci U S A 100 (5), 2284-2289 (2003)
   PUBMED   12606722
  REMARK    GeneRIF: TSAP6 may augment Myt1 activity and act downstream to p53
            to interface apoptosis and cell-cycle progression
REFERENCE   8  (residues 1 to 498)
  AUTHORS   Korkmaz,K.S., Elbi,C., Korkmaz,C.G., Loda,M., Hager,G.L. and
            Saatcioglu,F.
  TITLE     Molecular cloning and characterization of STAMP1, a highly
            prostate-specific six transmembrane protein that is overexpressed
            in prostate cancer
  JOURNAL   J Biol Chem 277 (39), 36689-36696 (2002)
   PUBMED   12095985
REFERENCE   9  (residues 1 to 498)
  AUTHORS   Zhang,X., Steiner,M.S., Rinaldy,A. and Lu,Y.
  TITLE     Apoptosis induction in prostate cancer cells by a novel gene
            product, pHyde, involves caspase-3
  JOURNAL   Oncogene 20 (42), 5982-5990 (2001)
   PUBMED   11593405
REFERENCE   10 (residues 1 to 498)
  AUTHORS   Steiner,M.S., Zhang,X., Wang,Y. and Lu,Y.
  TITLE     Growth inhibition of prostate cancer by an adenovirus expressing a
            novel tumor suppressor gene, pHyde
  JOURNAL   Cancer Res 60 (16), 4419-4425 (2000)
   PUBMED   10969787
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL833624.1, BX538047.1 and
            AC016736.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 10, 2004 this sequence version replaced NP_878919.1.
            
            Summary: This gene encodes a multipass membrane protein that
            functions as an iron transporter. The encoded protein can reduce
            both iron (Fe3+) and copper (Cu2+) cations. This protein may
            mediate downstream responses to p53, including promoting apoptosis.
            Deficiency in this gene can cause anemia. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Aug
            2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL833624.1, BX538047.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393110.7/ ENSP00000376822.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.2"
     Protein         1..498
                     /product="metalloreductase STEAP3 isoform a"
                     /EC_number="1.16.1.-"
                     /note="metalloreductase STEAP3; tumor suppressor pHyde;
                     STEAP family member 3, metalloreductase; tumor
                     suppressor-activated pathway protein 6; six-transmembrane
                     epithelial antigen of prostate 3; ferrireductase"
                     /calculated_mol_wt=55521
     Region          41..232
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
     Region          272..415
                     /region_name="Ferric_reduct"
                     /note="Ferric reductase like transmembrane component;
                     pfam01794"
                     /db_xref="CDD:426438"
     CDS             1..498
                     /gene="STEAP3"
                     /gene_synonym="AHMIO2; dudlin-2; dudulin-2; pHyde; STMP3;
                     TSAP6"
                     /coded_by="NM_182915.3:449..1945"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42738.1"
                     /db_xref="GeneID:55240"
                     /db_xref="HGNC:HGNC:24592"
                     /db_xref="MIM:609671"
ORIGIN      
        1 mshqpavatk mpeemdkpli slhlvdsdss lakvpdeapk vgilgsgdfa rslatrlvgs
       61 gfkvvvgsrn pkrtarlfps aaqvtfqeea vsspevifva vfrehysslc slsdqlagki
      121 lvdvsnpteq ehlqhresna eylaslfptc tvvkafnvis awtlqagprd gnrqvpicgd
      181 qpeakravse malamgfmpv dmgslasawe veamplrllp awkvptllal glfvcfyayn
      241 fvrdvlqpyv qesqnkffkl pvsvvnttlp cvayvllslv ylpgvlaaal qlrrgtkyqr
      301 fpdwldhwlq hrkqigllsf fcaalhalys fclplrrahr ydlvnlavkq vlankshlwv
      361 eeevwrmeiy lslgvlalgt lsllavtslp sianslnwre fsfvqsslgf valvlstlht
      421 ltygwtrafe esrykfylpp tftltllvpc vvilakalfl lpcisrrlar irrgwerest
      481 ikftlptdha laektshv
//
LOCUS       NP_001035799             272 aa            linear   PRI 27-APR-2025
DEFINITION  synaptophysin-like protein 2 [Homo sapiens].
ACCESSION   NP_001035799 XP_001134408 XP_001134453
VERSION     NP_001035799.1
DBSOURCE    REFSEQ: accession NM_001040709.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Jiao,H., Arner,P., Gerdhem,P., Strawbridge,R.J., Naslund,E.,
            Thorell,A., Hamsten,A., Kere,J. and Dahlman,I.
  TITLE     Exome sequencing followed by genotyping suggests SYPL2 as a
            susceptibility gene for morbid obesity
  JOURNAL   Eur J Hum Genet 23 (9), 1216-1222 (2015)
   PUBMED   25406998
  REMARK    GeneRIF: SYPL2 is a susceptibility gene for morbid obesity.
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Chen,S., Lu,F.F., Seeman,P. and Liu,F.
  TITLE     Quantitative proteomic analysis of human substantia nigra in
            Alzheimer's disease, Huntington's disease and Multiple sclerosis
  JOURNAL   Neurochem Res 37 (12), 2805-2813 (2012)
   PUBMED   22926577
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Satoh,K., Akatsu,H., Yamamoto,T., Kosaka,K., Yokota,H. and
            Yamada,T.
  TITLE     Mitsugumin 29 is transcriptionally induced in senile
            plaque-associated astrocytes
  JOURNAL   Brain Res 1441, 9-16 (2012)
   PUBMED   22290180
  REMARK    GeneRIF: Mitsugumin (MG)29 is expressed in astrocytes of Alzheimer
            disease brains associated with senile plaques, but is is not
            expressed in neurons around lesions.
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Shi,J., Potash,J.B., Knowles,J.A., Weissman,M.M., Coryell,W.,
            Scheftner,W.A., Lawson,W.B., DePaulo,J.R. Jr., Gejman,P.V.,
            Sanders,A.R., Johnson,J.K., Adams,P., Chaudhury,S., Jancic,D.,
            Evgrafov,O., Zvinyatskovskiy,A., Ertman,N., Gladis,M., Neimanas,K.,
            Goodell,M., Hale,N., Ney,N., Verma,R., Mirel,D., Holmans,P. and
            Levinson,D.F.
  TITLE     Genome-wide association study of recurrent early-onset major
            depressive disorder
  JOURNAL   Mol Psychiatry 16 (2), 193-201 (2011)
   PUBMED   20125088
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Kottgen,A., Pattaro,C., Boger,C.A., Fuchsberger,C., Olden,M.,
            Glazer,N.L., Parsa,A., Gao,X., Yang,Q., Smith,A.V., O'Connell,J.R.,
            Li,M., Schmidt,H., Tanaka,T., Isaacs,A., Ketkar,S., Hwang,S.J.,
            Johnson,A.D., Dehghan,A., Teumer,A., Pare,G., Atkinson,E.J.,
            Zeller,T., Lohman,K., Cornelis,M.C., Probst-Hensch,N.M.,
            Kronenberg,F., Tonjes,A., Hayward,C., Aspelund,T., Eiriksdottir,G.,
            Launer,L.J., Harris,T.B., Rampersaud,E., Mitchell,B.D.,
            Arking,D.E., Boerwinkle,E., Struchalin,M., Cavalieri,M.,
            Singleton,A., Giallauria,F., Metter,J., de Boer,I.H.,
            Haritunians,T., Lumley,T., Siscovick,D., Psaty,B.M.,
            Zillikens,M.C., Oostra,B.A., Feitosa,M., Province,M., de
            Andrade,M., Turner,S.T., Schillert,A., Ziegler,A., Wild,P.S.,
            Schnabel,R.B., Wilde,S., Munzel,T.F., Leak,T.S., Illig,T.,
            Klopp,N., Meisinger,C., Wichmann,H.E., Koenig,W., Zgaga,L.,
            Zemunik,T., Kolcic,I., Minelli,C., Hu,F.B., Johansson,A., Igl,W.,
            Zaboli,G., Wild,S.H., Wright,A.F., Campbell,H., Ellinghaus,D.,
            Schreiber,S., Aulchenko,Y.S., Felix,J.F., Rivadeneira,F.,
            Uitterlinden,A.G., Hofman,A., Imboden,M., Nitsch,D.,
            Brandstatter,A., Kollerits,B., Kedenko,L., Magi,R., Stumvoll,M.,
            Kovacs,P., Boban,M., Campbell,S., Endlich,K., Volzke,H.,
            Kroemer,H.K., Nauck,M., Volker,U., Polasek,O., Vitart,V.,
            Badola,S., Parker,A.N., Ridker,P.M., Kardia,S.L., Blankenberg,S.,
            Liu,Y., Curhan,G.C., Franke,A., Rochat,T., Paulweber,B.,
            Prokopenko,I., Wang,W., Gudnason,V., Shuldiner,A.R., Coresh,J.,
            Schmidt,R., Ferrucci,L., Shlipak,M.G., van Duijn,C.M., Borecki,I.,
            Kramer,B.K., Rudan,I., Gyllensten,U., Wilson,J.F., Witteman,J.C.,
            Pramstaller,P.P., Rettig,R., Hastie,N., Chasman,D.I., Kao,W.H.,
            Heid,I.M. and Fox,C.S.
  TITLE     New loci associated with kidney function and chronic kidney disease
  JOURNAL   Nat Genet 42 (5), 376-384 (2010)
   PUBMED   20383146
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB071160.1, DA097637.1, DB291596.1, AI983207.1, DN831287.1 and
            AL355145.31.
            
            On or before Sep 20, 2006 this sequence version replaced
            XP_001134408.1, XP_001134453.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293082.1, AB158472.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369872.4/ ENSP00000358888.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..272
                     /product="synaptophysin-like protein 2"
                     /note="mitsugumin 29"
                     /calculated_mol_wt=30025
     Region          30..232
                     /region_name="MARVEL"
                     /note="Membrane-associating domain; pfam01284"
                     /db_xref="CDD:366555"
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VXT5.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VXT5.1)"
     Site            151..171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VXT5.1)"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VXT5.1)"
     Site            214..234
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VXT5.1)"
     Region          240..272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VXT5.1)"
     CDS             1..272
                     /gene="SYPL2"
                     /gene_synonym="MG29"
                     /coded_by="NM_001040709.2:299..1117"
                     /db_xref="CCDS:CCDS41365.1"
                     /db_xref="GeneID:284612"
                     /db_xref="HGNC:HGNC:27638"
ORIGIN      
        1 msstesagrt adksprqqvd rllvglrwrr leeplgfikv lqwlfaifaf gscgsysget
       61 gamvrcnnea kdvssiivaf gypfrlhriq yemplcdees ssktmhlmgd fsapaeffvt
      121 lgifsffytm aalviylrfh nlytenkrfp lvdfcvtvsf tffwlvaaaa wgkgltdvkg
      181 atrpssltaa msvchgeeav csagatpsmg lanisvlfgf infflwagnc wfvfketpwh
      241 gqgqgqdqdq dqdqgqgpsq esaaeqgave kq
//
LOCUS       NP_005477                476 aa            linear   PRI 27-APR-2025
DEFINITION  TOM1-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_005477 XP_001723736 XP_001725581 XP_001726726
VERSION     NP_005477.2
DBSOURCE    REFSEQ: accession NM_005486.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Cabral-Dias,R., Lucarelli,S., Zak,K., Rahmani,S., Judge,G.,
            Abousawan,J., DiGiovanni,L.F., Vural,D., Anderson,K.E.,
            Sugiyama,M.G., Genc,G., Hong,W., Botelho,R.J., Fairn,G.D., Kim,P.K.
            and Antonescu,C.N.
  TITLE     Fyn and TOM1L1 are recruited to clathrin-coated pits and regulate
            Akt signaling
  JOURNAL   J Cell Biol 221 (4) (2022)
   PUBMED   35238864
  REMARK    GeneRIF: Fyn and TOM1L1 are recruited to clathrin-coated pits and
            regulate Akt signaling.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Li,W., Marshall,C., Mei,L., Dzubow,L., Schmults,C., Dans,M. and
            Seykora,J.
  TITLE     Srcasm modulates EGF and Src-kinase signaling in keratinocytes
  JOURNAL   J Biol Chem 280 (7), 6036-6046 (2005)
   PUBMED   15579470
  REMARK    GeneRIF: Srcasm plays a role in linking EGF receptor- and
            SFK-dependent signaling to differentiation in keratinocytes
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Katoh,Y., Shiba,Y., Mitsuhashi,H., Yanagida,Y., Takatsu,H. and
            Nakayama,K.
  TITLE     Tollip and Tom1 form a complex and recruit ubiquitin-conjugated
            proteins onto early endosomes
  JOURNAL   J Biol Chem 279 (23), 24435-24443 (2004)
   PUBMED   15047686
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Seykora,J.T., Mei,L., Dotto,G.P. and Stein,P.L.
  TITLE     'Srcasm: a novel Src activating and signaling molecule
  JOURNAL   J Biol Chem 277 (4), 2812-2822 (2002)
   PUBMED   11711534
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Seroussi,E., Kedra,D., Kost-Alimova,M., Sandberg-Nordqvist,A.C.,
            Fransson,I., Jacobs,J.F., Fu,Y., Pan,H.Q., Roe,B.A., Imreh,S. and
            Dumanski,J.P.
  TITLE     TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1
            and encode proteins similar to the endosomal proteins HGS and STAM
  JOURNAL   Genomics 57 (3), 380-388 (1999)
   PUBMED   10329004
REFERENCE   10 (residues 1 to 476)
  CONSRTM   Ministerial Meeting on Population of the Non-Aligned Movement
            (1993: Bali)
  TITLE     Non-aligned movement support for South-South collaboration in the
            field of population and family planning
  JOURNAL   Integration (40), 37-42 (1994)
   PUBMED   12345679
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN284148.1, AK315039.1, AK223125.1, AJ010071.1 and AW139144.1.
            
            On or before Jun 22, 2008 this sequence version replaced
            XP_001723736.1, XP_001726726.1, XP_001725581.1, NP_005477.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ010071.1, AK223125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000575882.6/ ENSP00000460823.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q22"
     Protein         1..476
                     /product="TOM1-like protein 1 isoform 1"
                     /note="TOM1-like protein 1; target of Myb-like protein 1;
                     src-activating and signaling molecule protein"
                     /calculated_mol_wt=52858
     Region          14..150
                     /region_name="VHS_Tom1L1"
                     /note="VHS (Vps27/Hrs/STAM) domain of TOM1-like protein 1;
                     cd16997"
                     /db_xref="CDD:340794"
     Site            order(32..33,36,40,81..82)
                     /site_type="other"
                     /note="putative intraprotein/interprotein binding site
                     [polypeptide binding]"
                     /db_xref="CDD:340794"
     Site            order(50,54,57..58)
                     /site_type="active"
                     /note="putative membrane binding residues [active]"
                     /db_xref="CDD:340794"
     Region          155..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75674.2)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q923U0; propagated from
                     UniProtKB/Swiss-Prot (O75674.2)"
     Region          199..290
                     /region_name="GAT_TM1L1"
                     /note="canonical GAT domain found in target of Myb-like
                     protein 1 (Tom1L1); cd14237"
                     /db_xref="CDD:410584"
     Site            order(210..211,214..215,217..218,221..222,225,238,
                     241..242)
                     /site_type="other"
                     /note="putative ubiquitin binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410584"
     Region          298..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75674.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (O75674.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75674.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75674.2)"
     Region          392..395
                     /region_name="Interaction with GRB2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75674.2)"
     Region          421..425
                     /region_name="SH3-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75674.2)"
     Region          442..445
                     /region_name="Interaction with PIK3R1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75674.2)"
     Region          460..463
                     /region_name="SH2-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75674.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q923U0; propagated from
                     UniProtKB/Swiss-Prot (O75674.2)"
     CDS             1..476
                     /gene="TOM1L1"
                     /gene_synonym="SRCASM"
                     /coded_by="NM_005486.3:15..1445"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11582.1"
                     /db_xref="GeneID:10040"
                     /db_xref="HGNC:HGNC:11983"
                     /db_xref="MIM:604701"
ORIGIN      
        1 mafgkshrdp yatsvghlie katfagvqte dwgqfmhicd iinttqdgpk davkalkkri
       61 sknynhkeiq ltlslidmcv qncgpsfqsl ivkkefvken lvkllnpryn lpldiqnril
      121 nfiktwsqgf pggvdvsevk evyldlvkkg vqfppseaea etarqetaqi ssnpptsvpt
      181 apalssviap knstvtlvpe qigklhseld mvkmnvrvms ailmentpgs enhediellq
      241 klyktgremq erimdllvvv enedvtveli qvnedlnnai lgyerftrnq qrileqnknq
      301 keatnttsep sapsqdlldl spsprmprat lgelntmnnq lsglnfslps sdvtnnlkps
      361 lhpqmnllal enteippfaq rtsqnltssh aydnflehsn svflqpvslq tiaaapsnqs
      421 lpplpsnhpa mtksdlqppn yyevmefdpl apavtteaiy eeidahqhkg aqndgd
//
LOCUS       NP_033769                241 aa            linear   ROD 27-APR-2025
DEFINITION  cysteine-rich secretory protein 3 precursor [Mus musculus].
ACCESSION   NP_033769 XP_001002056
VERSION     NP_033769.1
DBSOURCE    REFSEQ: accession NM_009639.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Curci,L., Brukman,N.G., Weigel Munoz,M., Rojo,D., Carvajal,G.,
            Sulzyk,V., Gonzalez,S.N., Rubinstein,M., Da Ros,V.G. and
            Cuasnicu,P.S.
  TITLE     Functional redundancy and compensation: Deletion of multiple murine
            Crisp genes reveals their essential role for male fertility
  JOURNAL   FASEB J 34 (12), 15718-15733 (2020)
   PUBMED   33037689
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Evans,J., D'Sylva,R., Volpert,M., Jamsai,D., Merriner,D.J., Nie,G.,
            Salamonsen,L.A. and O'Bryan,M.K.
  TITLE     Endometrial CRISP3 is regulated throughout the mouse estrous and
            human menstrual cycle and facilitates adhesion and proliferation of
            endometrial epithelial cells
  JOURNAL   Biol Reprod 92 (4), 99 (2015)
   PUBMED   25715794
  REMARK    GeneRIF: These data suggest roles for epithelial and
            neutrophil-derived CRISP3 in endometrial repair and regeneration
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Islam,M.N., Itoh,S., Yanagita,T., Sumiyoshi,K., Hayano,S.,
            Kuremoto,K., Kurosaka,H., Honjo,T., Kawanabe,N., Kamioka,H.,
            Sakai,T., Ishimaru,N., Taniuchi,I. and Yamashiro,T.
  TITLE     Runx/Cbfb signaling regulates postnatal development of granular
            convoluted tubule in the mouse submandibular gland
  JOURNAL   Dev Dyn 244 (3), 488-496 (2015)
   PUBMED   25410786
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Dike,S., Balija,V.S., Nascimento,L.U., Xuan,Z., Ou,J., Zutavern,T.,
            Palmer,L.E., Hannon,G., Zhang,M.Q. and McCombie,W.R.
  TITLE     The mouse genome: experimental examination of gene predictions and
            transcriptional start sites
  JOURNAL   Genome Res 14 (12), 2424-2429 (2004)
   PUBMED   15574821
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Haendler,B., Habenicht,U.F., Schwidetzky,U., Schuttke,I. and
            Schleuning,W.D.
  TITLE     Differential androgen regulation of the murine genes for
            cysteine-rich secretory proteins (CRISP)
  JOURNAL   Eur J Biochem 250 (2), 440-446 (1997)
   PUBMED   9428696
REFERENCE   7  (residues 1 to 241)
  AUTHORS   Schwidetzky,U., Haendler,B. and Schleuning,W.D.
  TITLE     Isolation and characterization of the androgen-dependent mouse
            cysteine-rich secretory protein-3 (CRISP-3) gene
  JOURNAL   Biochem J 309 (Pt 3) (Pt 3), 831-836 (1995)
   PUBMED   7639699
REFERENCE   8  (residues 1 to 241)
  AUTHORS   Kasahara,M., Hayashi,M., Yoshida,M.C., Nadeau,J.H., Fujimoto,S. and
            Ishibashi,T.
  TITLE     Mapping of acidic epididymal glycoprotein (Aeg) genes to mouse
            chromosome 17
  JOURNAL   Mamm Genome 6 (1), 52-54 (1995)
   PUBMED   7719028
REFERENCE   9  (residues 1 to 241)
  AUTHORS   Haendler,B., Kratzschmar,J., Theuring,F. and Schleuning,W.D.
  TITLE     Transcripts for cysteine-rich secretory protein-1 (CRISP-1; DE/AEG)
            and the novel related CRISP-3 are expressed under androgen control
            in the mouse salivary gland
  JOURNAL   Endocrinology 133 (1), 192-198 (1993)
   PUBMED   8319566
REFERENCE   10 (residues 1 to 241)
  AUTHORS   Mizuki,N. and Kasahara,M.
  TITLE     Mouse submandibular glands express an androgen-regulated transcript
            encoding an acidic epididymal glycoprotein-like molecule
  JOURNAL   Mol Cell Endocrinol 89 (1-2), 25-32 (1992)
   PUBMED   1301383
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CV307357.1 and L05560.1.
            
            On May 4, 2006 this sequence version replaced XP_001002056.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L05560.1, BC022573.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849375,
                                           SAMN00849378 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 19.45 cM"
     Protein         1..241
                     /product="cysteine-rich secretory protein 3 precursor"
                     /note="SCP 2; sperm-coating glycoprotein 2; acidic
                     epididymal glycoprotein 2"
                     /calculated_mol_wt=25273
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2060
     mat_peptide     20..241
                     /product="Cysteine-rich secretory protein 3.
                     /id=PRO_0000006269"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03402.1)"
                     /calculated_mol_wt=25273
     Region          37..172
                     /region_name="CAP"
                     /note="CAP (cysteine-rich secretory proteins, antigen 5,
                     and pathogenesis-related 1 proteins) domain family;
                     cl00133"
                     /db_xref="CDD:412178"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03402.1)"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03402.1)"
     Site            175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03402.1)"
     Region          194..241
                     /region_name="Crisp"
                     /note="pfam08562"
                     /db_xref="CDD:462519"
     CDS             1..241
                     /gene="Crisp3"
                     /gene_synonym="Aeg2; CRISP-3; CRS3; SGP28"
                     /coded_by="NM_009639.3:56..781"
                     /db_xref="CCDS:CCDS28783.1"
                     /db_xref="GeneID:11572"
                     /db_xref="MGI:MGI:102552"
ORIGIN      
        1 malmlvlffl aavlppsllq dnsqenslek lstskksvqe eivskhnqlr rkvspsgsdl
       61 lnmewnydaq vnaqqradkc tfshspielr ttnlkcgenl fmssylvpws sviqgwynes
      121 kglifgvgpk qnvsvvghht qvvwksnlqv acgvaecpen plryfyvcry cpvlnysghy
      181 psrpylayta rapcascpdr cedglctksc qykdmsfwck rleyvckhpg lkkrclatcq
      241 c
//
LOCUS       NP_803237                826 aa            linear   PRI 27-APR-2025
DEFINITION  protein FAM171B precursor [Homo sapiens].
ACCESSION   NP_803237
VERSION     NP_803237.3
DBSOURCE    REFSEQ: accession NM_177454.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Hu,W.M., Li,M., Ning,J.Z., Tang,Y.Q., Song,T.B., Li,L.Z., Zou,F.,
            Cheng,F. and Yu,W.M.
  TITLE     FAM171B stabilizes vimentin and enhances CCL2-mediated TAM
            infiltration to promote bladder cancer progression
  JOURNAL   J Exp Clin Cancer Res 42 (1), 290 (2023)
   PUBMED   37915048
  REMARK    GeneRIF: FAM171B stabilizes vimentin and enhances CCL2-mediated TAM
            infiltration to promote bladder cancer progression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Tran,Q., Sudasinghe,A., Jones,B., Xiong,K., Cohen,R.E.,
            Sharlin,D.S., Hartert,K.T. and Goellner,G.M.
  TITLE     FAM171B is a novel polyglutamine protein widely expressed in the
            mammalian brain
  JOURNAL   Brain Res 1766, 147540 (2021)
   PUBMED   34052262
  REMARK    GeneRIF: FAM171B is a novel polyglutamine protein widely expressed
            in the mammalian brain.
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Liang,H., Xu,Y., Zhang,Q., Yang,Y., Mou,Y., Gao,Y., Chen,R.,
            Chen,C. and Dai,P.
  TITLE     MiR-483-3p regulates oxaliplatin resistance by targeting FAM171B in
            human colorectal cancer cells
  JOURNAL   Artif Cells Nanomed Biotechnol 47 (1), 725-736 (2019)
   PUBMED   30861353
  REMARK    GeneRIF: FAM171B expression is up-regulated in
            oxaliplatin-resistant colorectal cancer cell line. Transfection of
            miR-483-3p mimics markedly decreases the levels of FAM171B and
            restores oxaliplatin responsiveness, and this alteration enhances
            cell apoptosis and weakens cell migration. Knockdown of FAM171B in
            oxaliplatin-resistant colorectal cancer cell line sensitizes its
            reaction of the treatment with oxaliplatin.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC017101.10, BC060872.1 and AB075826.1.
            
            On Oct 31, 2006 this sequence version replaced NP_803237.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.80452.1,
                                           SRR1660809.225950.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304698.10/ ENSP00000304108.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.1"
     Protein         1..826
                     /product="protein FAM171B precursor"
                     /note="protein FAM171B"
                     /calculated_mol_wt=88783
     sig_peptide     1..32
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P995.3)"
                     /calculated_mol_wt=3416
     mat_peptide     33..826
                     /product="Protein FAM171B. /id=PRO_0000287148"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P995.3)"
                     /calculated_mol_wt=88783
     Region          52..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P995.3)"
     Region          85..826
                     /region_name="UPF0560"
                     /note="Uncharacterized protein family UPF0560; pfam10577"
                     /db_xref="CDD:463154"
     Site            108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P995.3)"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P995.3)"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P995.3)"
     Site            268
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P995.3)"
     Site            354..374
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P995.3)"
     Region          429..448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P995.3)"
     Region          474..493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P995.3)"
     Region          774..826
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P995.3)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14CH0; propagated from
                     UniProtKB/Swiss-Prot (Q6P995.3)"
     CDS             1..826
                     /gene="FAM171B"
                     /gene_synonym="KIAA1946"
                     /coded_by="NM_177454.4:115..2595"
                     /db_xref="CCDS:CCDS33347.1"
                     /db_xref="GeneID:165215"
                     /db_xref="HGNC:HGNC:29412"
                     /db_xref="MIM:620309"
ORIGIN      
        1 marlcrrvpc tlllglavvl lkarlvpaaa raelsrsdls liqqqqqqqq qqqqqqkqle
       61 eaeeertevp gatstltvpv svfmlkvqvn diisrqylsq avvevfvnyt ktnstvtksn
      121 gavlikvpyk lglsltiiay kdgyvltplp wktrrmpiys svtlslfpqs qaniwlfedt
      181 vlitgklada ksqpsvqfsk aliklpdnhh isnvtgyltv lqqflkvdnf lhttgitlnk
      241 pgfenieltp laaicvkiys ggkelkvngs iqvslpllrl ndisagdrip awtfdmntga
      301 wvnhgrgmvk ehnnhliwty daphlgywia aplpgtrgsg inedskdita yhtvfltail
      361 ggtivivigf favllcycrd kcgtpqkrer nitklevlkr dqttstthin histvkvalk
      421 aedksqlfna knssyspqkk epskaeteer vsmvktrddf kiynedvsfl svnqnnysrn
      481 ptqslepnvg skqpkhinnn lssslgdaqd ekryltgnee aygrshipeq lmhiysqpia
      541 ilqtsdlfst peqlhtaksa tlprkgqlvy gqlmepvnre nftqtlpkmp ihshaqppda
      601 reediilegq qslpsqasdw sryssslles vsvpgtlnea vvmtpfssel qgiseqtlle
      661 lskgkpsphp rawfvsldgk pvaqvrhsfi dlkkgkrtqs ndtsldsgvd mnelhssrkl
      721 erektfiksm hqpkilyled ldlsssesgt tvcspedpal rhildggsgv imehpgeesp
      781 grkstvedfe antsptkrrg rpplakrdsk tniwkkreer plipin
//
LOCUS       NP_001338018             585 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein Eos isoform a [Homo sapiens].
ACCESSION   NP_001338018 XP_016875294
VERSION     NP_001338018.1
DBSOURCE    REFSEQ: accession NM_001351089.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Miao,Y., Qi,S., Hu,R., Sheng,Y. and Yang,Q.
  TITLE     Association analysis of the IKZF4 gene with Alopecia Areata in the
            Chinese Han population
  JOURNAL   Altern Ther Health Med 30 (10), 314-317 (2024)
   PUBMED   38330583
  REMARK    GeneRIF: Association analysis of the IKZF4 gene with Alopecia
            Areata in the Chinese Han population.
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Weng,N., Zhou,C., Zhou,Y., Zhong,Y., Jia,Z., Rao,X., Qiu,H.,
            Zeng,G., Jin,X., Zhang,J., Zhuang,Z., Liang,Z., Deng,Y., Li,Q.,
            Yang,S., Luo,H., Wang,H. and Wu,X.
  TITLE     IKZF4/NONO-RAB11FIP3 axis promotes immune evasion in gastric cancer
            via facilitating PD-L1 endosome recycling
  JOURNAL   Cancer Lett 584, 216618 (2024)
   PUBMED   38211652
  REMARK    GeneRIF: IKZF4/NONO-RAB11FIP3 axis promotes immune evasion in
            gastric cancer via facilitating PD-L1 endosome recycling.
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Wang,Y., Zhao,H., He,Y., Zhang,P., Zeng,C., Du,T., Shen,Q., Chen,Y.
            and Zhao,S.
  TITLE     IKZF4 acts as a novel tumor suppressor in non-small cell lung
            cancer by suppressing Notch signaling pathway
  JOURNAL   Cell Signal 107, 110679 (2023)
   PUBMED   37044192
  REMARK    GeneRIF: IKZF4 acts as a novel tumor suppressor in non-small cell
            lung cancer by suppressing Notch signaling pathway.
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Vandewalle,J., Van der Auwera,B.J., Amin,H., Quartier,E.,
            Desouter,A.K., Tenoutasse,S., Gillard,P., De Block,C.,
            Keymeulen,B., Gorus,F.K. and Van de Casteele,M.
  CONSRTM   Belgian Diabetes Registry
  TITLE     Genetic variation at ERBB3/IKZF4 and sexual dimorphism in epitope
            spreading in single autoantibody-positive relatives
  JOURNAL   Diabetologia 64 (11), 2511-2516 (2021)
   PUBMED   34448034
  REMARK    GeneRIF: Genetic variation at ERBB3/IKZF4 and sexual dimorphism in
            epitope spreading in single autoantibody-positive relatives.
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 585)
  AUTHORS   Westman,B.J., Perdomo,J., Matthews,J.M., Crossley,M. and
            Mackay,J.P.
  TITLE     Structural studies on a protein-binding zinc-finger domain of Eos
            reveal both similarities and differences to classical zinc fingers
  JOURNAL   Biochemistry 43 (42), 13318-13327 (2004)
   PUBMED   15491138
REFERENCE   7  (residues 1 to 585)
  AUTHORS   Perdomo,J. and Crossley,M.
  TITLE     The Ikaros family protein Eos associates with C-terminal-binding
            protein corepressors
  JOURNAL   Eur J Biochem 269 (23), 5885-5892 (2002)
   PUBMED   12444977
REFERENCE   8  (residues 1 to 585)
  AUTHORS   Koipally,J. and Georgopoulos,K.
  TITLE     A molecular dissection of the repression circuitry of Ikaros
  JOURNAL   J Biol Chem 277 (31), 27697-27705 (2002)
   PUBMED   12015313
REFERENCE   9  (residues 1 to 585)
  AUTHORS   Perdomo,J., Holmes,M., Chong,B. and Crossley,M.
  TITLE     Eos and pegasus, two members of the Ikaros family of proteins with
            distinct DNA binding activities
  JOURNAL   J Biol Chem 275 (49), 38347-38354 (2000)
   PUBMED   10978333
REFERENCE   10 (residues 1 to 585)
  AUTHORS   Honma,Y., Kiyosawa,H., Mori,T., Oguri,A., Nikaido,T., Kanazawa,K.,
            Tojo,M., Takeda,J., Tanno,Y., Yokoya,S., Kawabata,I., Ikeda,H. and
            Wanaka,A.
  TITLE     Eos: a novel member of the Ikaros gene family expressed
            predominantly in the developing nervous system
  JOURNAL   FEBS Lett 447 (1), 76-80 (1999)
   PUBMED   10218586
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC034102.32.
            
            On Dec 22, 2018 this sequence version replaced XP_016875294.1.
            
            Summary: Members of the Ikaros (ZNFN1A1; MIM 603023) family of
            transcription factors, which includes Eos, are expressed in
            lymphocytes and are implicated in the control of lymphoid
            development.[supplied by OMIM, Jul 2002].
            
            Transcript Variant: This variant (2), as well as variant 1, encodes
            isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BX647761.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2145240 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..585
                     /product="zinc finger protein Eos isoform a"
                     /note="zinc finger transcription factor Eos; zinc finger
                     protein, subfamily 1A, 4 (Eos); zinc finger protein Eos;
                     ikaros family zinc finger protein 4"
                     /calculated_mol_wt=63975
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Region          68..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKS7; propagated from
                     UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Region          161..181
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(166,168,170,172..173,176..177,180,194,196,200..201,
                     204..205,208,222,224,226,228..229,232..233,236)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          174..198
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          189..209
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          201..226
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          <211..271
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          250..271
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          281..585
                     /region_name="Interaction with FOXP3.
                     /evidence=ECO:0000250|UniProtKB:Q8C208"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Site            335
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKS7; propagated from
                     UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Region          410..489
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Region          425..429
                     /region_name="CTBP-binding motif PEDLA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S9.2)"
     CDS             1..585
                     /gene="IKZF4"
                     /gene_synonym="EOS; ZNFN1A4"
                     /coded_by="NM_001351089.2:523..2280"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44917.1"
                     /db_xref="GeneID:64375"
                     /db_xref="HGNC:HGNC:13179"
                     /db_xref="MIM:606239"
ORIGIN      
        1 mhtppalprr fqgggrvrtp gshrqgkdnl erdpsggcvp dflpqaqdsn hfimeslfce
       61 ssgdssleke flgapvgpsv stpnsqhssp srslsansik vemysdeess rllgpderll
      121 ekddsvived slseplgycd gsgpephspg girlpngklk cdvcgmvcig pnvlmvhkrs
      181 htgerpfhcn qcgasftqkg nllrhiklhs gekpfkcpfc nyacrrrdal tghlrthsvs
      241 sptvgkpykc nycgrsykqq stleehkerc hnylqslste aqalagqpgd eirdlemvpd
      301 smlhssserp tfidrlansl tkrkrstpqk fvgekqmrfs lsdlpydvns ggyekdvelv
      361 ahhslepgfg sslafvgaeh lrplrlpptn ciseltpvis svytqmqplp grlelpgsre
      421 agegpedlad ggpllyrprg pltdpgasps ngcqdstdte snhedrvagv vslpqgpppq
      481 ppptivvgrh spayakedpk pqegllrgtp gpskevlrvv gesgepvkaf kcehcrilfl
      541 dhvmftihmg chgfrdpfec nicgyhsqdr yefsshivrg ehkvg
//
LOCUS       NP_001346667             384 aa            linear   ROD 27-APR-2025
DEFINITION  septin-7 isoform 3 [Mus musculus].
ACCESSION   NP_001346667 XP_006510255
VERSION     NP_001346667.1
DBSOURCE    REFSEQ: accession NM_001359738.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Choi,E.S., Hnath,B., Sha,C.M. and Dokholyan,N.V.
  TITLE     Unveiling the double-edged sword: SOD1 trimers possess
            tissue-selective toxicity and bind septin-7 in motor neuron-like
            cells
  JOURNAL   Structure 32 (10), 1776-1792 (2024)
   PUBMED   39208794
  REMARK    GeneRIF: Unveiling the double-edged sword: SOD1 trimers possess
            tissue-selective toxicity and bind septin-7 in motor neuron-like
            cells.
REFERENCE   2  (residues 1 to 384)
  AUTHORS   De Gasperi,R., Csernoch,L., Dienes,B., Gonczi,M., Chakrabarty,J.K.,
            Goeta,S., Aslan,A., Toro,C.A., Karasik,D., Brown,L.M., Brotto,M.
            and Cardozo,C.P.
  TITLE     Septin 7 interacts with Numb to preserve sarcomere structural
            organization and muscle contractile function
  JOURNAL   Elife 12, 89424 (2024)
   PUBMED   38695862
  REMARK    GeneRIF: Septin 7 interacts with Numb to preserve sarcomere
            structural organization and muscle contractile function.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Szabo,L., Telek,A., Fodor,J., Dobrosi,N., Docs,K., Hegyi,Z.,
            Gonczi,M., Csernoch,L. and Dienes,B.
  TITLE     Reduced Expression of Septin7 Hinders Skeletal Muscle Regeneration
  JOURNAL   Int J Mol Sci 24 (17), 13536 (2023)
   PUBMED   37686339
  REMARK    GeneRIF: Reduced Expression of Septin7 Hinders Skeletal Muscle
            Regeneration.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Raduly,Z., Szabo,L., Dienes,B., Szentesi,P., Bana,A.V., Hajdu,T.,
            Kokai,E., Hegedus,C., Csernoch,L. and Gonczi,M.
  TITLE     Migration of Myogenic Cells Is Highly Influenced by Cytoskeletal
            Septin7
  JOURNAL   Cells 12 (14), 1825 (2023)
   PUBMED   37508490
  REMARK    GeneRIF: Migration of Myogenic Cells Is Highly Influenced by
            Cytoskeletal Septin7.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Hinson,S.R., Honorat,J.A., Grund,E.M., Clarkson,B.D., Miske,R.,
            Scharf,M., Zivelonghi,C., Al-Lozi,M.T., Bucelli,R.C., Budhram,A.,
            Cho,T., Choi,E., Grell,J., Lopez-Chiriboga,A.S., Levin,M.,
            Merati,M., Montalvo,M., Pittock,S.J., Wilson,M.R., Howe,C.L. and
            McKeon,A.
  TITLE     Septin-5 and -7-IgGs: Neurologic, Serologic, and Pathophysiologic
            Characteristics
  JOURNAL   Ann Neurol 92 (6), 1090-1101 (2022)
   PUBMED   36053822
  REMARK    GeneRIF: Septin-5 and -7-IgGs: Neurologic, Serologic, and
            Pathophysiologic Characteristics.
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Cobellis,G., Nicolaus,G., Iovino,M., Romito,A., Marra,E.,
            Barbarisi,M., Sardiello,M., Di Giorgio,F.P., Iovino,N., Zollo,M.,
            Ballabio,A. and Cortese,R.
  TITLE     Tagging genes with cassette-exchange sites
  JOURNAL   Nucleic Acids Res 33 (4), e44 (2005)
   PUBMED   15741177
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Peng,X.R., Jia,Z., Zhang,Y., Ware,J. and Trimble,W.S.
  TITLE     The septin CDCrel-1 is dispensable for normal development and
            neurotransmitter release
  JOURNAL   Mol Cell Biol 22 (1), 378-387 (2002)
   PUBMED   11739749
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Kinoshita,A., Noda,M. and Kinoshita,M.
  TITLE     Differential localization of septins in the mouse brain
  JOURNAL   J Comp Neurol 428 (2), 223-239 (2000)
   PUBMED   11064363
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Thomas,J.W., Summers,T.J., Lee-Lin,S.Q., Maduro,V.V., Idol,J.R.,
            Mastrian,S.D., Ryan,J.F., Jamison,D.C. and Green,E.D.
  TITLE     Comparative genome mapping in the sequence-based era: early
            experience with human chromosome 7
  JOURNAL   Genome Res 10 (5), 624-633 (2000)
   PUBMED   10810084
  REMARK    Review article
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Soulier,S. and Vilotte,J.L.
  TITLE     Sequence of murine CDC10 cDNA, gene organization and expression
            analysis
  JOURNAL   Biochim Biophys Acta 1442 (2-3), 339-346 (1998)
   PUBMED   9804986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CT025561.11.
            
            On Jan 12, 2018 this sequence version replaced XP_006510255.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1660817.166202.1, SRR1660825.41338.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN00849380, SAMN00849381 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 10.25 cM"
     Protein         1..384
                     /product="septin-7 isoform 3"
                     /note="cell division cycle 10 homolog; CDC10 protein
                     homolog"
                     /calculated_mol_wt=44725
     Region          1..264
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Site            4..11
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(6..12,60,63,141..142,144,197..198)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            35..43
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Site            60..63
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(62..97,98..107)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Site            141..144
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            197..199
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     Region          284..>380
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     CDS             1..384
                     /gene="Septin7"
                     /gene_synonym="Cdc10; E430034N22; Sept7"
                     /coded_by="NM_001359738.1:355..1509"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:235072"
                     /db_xref="MGI:MGI:1335094"
ORIGIN      
        1 mvvgesglgk stlinslflt dlyspeypgp shrikktvqv eqskvlikeg gvqllltivd
       61 tpgfgdavdn sncwqpvidy idskfedyln aesrvnrrqm pdnrvqccly fiapsghglk
      121 pldiefmkrl hekvniipli akadtltpee cqqfkkqimk eiqehkikiy efpetddeee
      181 nklvkkikdr lplavvgsnt iievngkrvr grqypwgvae vengehcdft ilrnmlirth
      241 mqdlkdvtnn vhyenyrsrk laavtyngvd nnknkgqltk splaqmeeer rehvakmkkm
      301 ememeqvfem kvkekvqklk dseaelqrrh eqmkknleaq hkeleekrrq feeekanwea
      361 qqrileqqns srtleknkkk gkif
//
LOCUS       NP_001092314             351 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 236 [Homo sapiens].
ACCESSION   NP_001092314 XP_291757
VERSION     NP_001092314.1
DBSOURCE    REFSEQ: accession NM_001098844.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Maurya,N.S., Kushwaha,S., Chawade,A. and Mani,A.
  TITLE     Transcriptome profiling by combined machine learning and
            statistical R analysis identifies TMEM236 as a potential novel
            diagnostic biomarker for colorectal cancer
  JOURNAL   Sci Rep 11 (1), 14304 (2021)
   PUBMED   34253750
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Kamatani,Y., Matsuda,K., Okada,Y., Kubo,M., Hosono,N., Daigo,Y.,
            Nakamura,Y. and Kamatani,N.
  TITLE     Genome-wide association study of hematological and biochemical
            traits in a Japanese population
  JOURNAL   Nat Genet 42 (3), 210-215 (2010)
   PUBMED   20139978
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139238.13, BC157856.1 and BX097915.1.
            
            On Jul 5, 2007 this sequence version replaced XP_291757.5.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377495.2/ ENSP00000366715.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.33"
     Protein         1..351
                     /product="transmembrane protein 236"
                     /note="family with sequence similarity 23, member B;
                     family with sequence similarity 23, member A"
                     /calculated_mol_wt=39532
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B7.1)"
     Site            49..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B7.1)"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B7.1)"
     Site            121..141
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B7.1)"
     Region          177..216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B7.1)"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5W0B7.1)"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B7.1)"
     Site            301..321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5W0B7.1)"
     CDS             1..351
                     /gene="TMEM236"
                     /gene_synonym="bA162I21.2; bA16O1.2; FAM23A; FAM23B"
                     /coded_by="NM_001098844.3:96..1151"
                     /db_xref="CCDS:CCDS41492.1"
                     /db_xref="GeneID:653567"
                     /db_xref="HGNC:HGNC:23473"
ORIGIN      
        1 masgrlikfv vfellefaaf siptlviteq fatayqgtra rsdnthywli iscsiayval
       61 vtlliwvpvk vilhkkryiy rkikgwrpvl mmcvvlttlp cltfsiavte vqksingsad
      121 vlpdmlpdlp vslvllslim vdiieklriy plrgsqksse nghihstslq hiktvteqvr
      181 qspenaaspq atnstqvsqp sgamtrsqes vfmgpqepsc dsgilrmmsr rdvraelflw
      241 sfllwsdtie mvrvaghpnv yksswlypvy ifsfisllri tftpqnplln slsvllqdlp
      301 fvfvrlglii algtitpvlg lcknilvtls yiyfnyltri rifsafemsp f
//
LOCUS       NP_060242                505 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 22B [Homo sapiens].
ACCESSION   NP_060242
VERSION     NP_060242.2
DBSOURCE    REFSEQ: accession NM_017772.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Kovacs,I.A., Luck,K., Spirohn,K., Wang,Y., Pollis,C., Schlabach,S.,
            Bian,W., Kim,D.K., Kishore,N., Hao,T., Calderwood,M.A., Vidal,M.
            and Barabasi,A.L.
  TITLE     Network-based prediction of protein interactions
  JOURNAL   Nat Commun 10 (1), 1240 (2019)
   PUBMED   30886144
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Greninger,A.L., Knudsen,G.M., Betegon,M., Burlingame,A.L. and
            DeRisi,J.L.
  TITLE     ACBD3 interaction with TBC1 domain 22 protein is differentially
            affected by enteroviral and kobuviral 3A protein binding
  JOURNAL   mBio 4 (2), e00098-e00013 (2013)
   PUBMED   23572552
  REMARK    GeneRIF: Using affinity purification-mass spectrometry, we
            identified the putative Rab33 GTPase-activating proteins TBC1D22A
            and TBC1D22B as ACBD3-interacting factors.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY313781.1, CN423653.1 and BC001927.1.
            
            On Dec 18, 2003 this sequence version replaced NP_060242.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY313781.1, AK096340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373491.3/ ENSP00000362590.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..505
                     /product="TBC1 domain family member 22B"
                     /calculated_mol_wt=58950
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:23572552; propagated from
                     UniProtKB/Swiss-Prot (Q9NU19.3)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NU19.3)"
     Region          105..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU19.3)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NU19.3)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23572552,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NU19.3)"
     Region          207..457
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..505
                     /gene="TBC1D22B"
                     /gene_synonym="C6orf197"
                     /coded_by="NM_017772.4:147..1664"
                     /db_xref="CCDS:CCDS4832.1"
                     /db_xref="GeneID:55633"
                     /db_xref="HGNC:HGNC:21602"
                     /db_xref="MIM:616880"
ORIGIN      
        1 maaenskqfw krsaklpgsi qpvygaqhpp ldprltknfi kerskvntvp lknkkassfh
       61 efarntsdaw digddeeedf sspsfqtlns kvalataaqv lenhsklrvk persqsttsd
      121 vpanykviks ssdaqlsrns sdtclrnplh kqqslplrpi iplvarisdq nasgappmtv
      181 rektrlekfr qllssqntdl delrkcswpg vprevrpitw rllsgylpan terrkltlqr
      241 kreeyfgfie qyydsrneeh hqdtyrqihi diprtnplip lfqqplvqei ferilfiwai
      301 rhpasgyvqg indlvtpffv vflseyveed venfdvtnls qdmlrsiead sfwcmsklld
      361 giqdnytfaq pgiqkkvkal eelvsrideq vhnhfrryev eylqfafrwm nnllmrelpl
      421 rctirlwdty qsepegfshf hlyvcaafli kwrkeildee dfqgllmllq nlptihwgne
      481 eiglllaeay rlkymfadap nhyrr
//
LOCUS       NP_006071                771 aa            linear   PRI 27-APR-2025
DEFINITION  semaphorin-3A precursor [Homo sapiens].
ACCESSION   NP_006071
VERSION     NP_006071.1
DBSOURCE    REFSEQ: accession NM_006080.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Yang,R., Yang,F., Wei,Y., Huang,B., Cao,T., Tan,H., Liu,D., Zou,Q.,
            Wen,J., Wen,L., Lu,X., Yu,C., Cai,H., Xie,X., Jiang,S., Yao,S. and
            Liang,Y.
  TITLE     Hypoxia-induced Semaphorin 3A promotes the development of
            endometriosis through regulating macrophage polarization
  JOURNAL   Int Immunopharmacol 138, 112559 (2024)
   PUBMED   38955028
  REMARK    GeneRIF: Hypoxia-induced Semaphorin 3A promotes the development of
            endometriosis through regulating macrophage polarization.
REFERENCE   2  (residues 1 to 771)
  AUTHORS   Huang,P., Jiang,R.X., Wang,F., Qiao,W.W., Ji,Y.T., Meng,L.Y. and
            Bian,Z.
  TITLE     PIEZO1 Promotes Odontoblast-Mediated Reactionary Dentinogenesis via
            SEMA3A
  JOURNAL   J Dent Res 103 (9), 889-898 (2024)
   PUBMED   38910430
  REMARK    GeneRIF: PIEZO1 Promotes Odontoblast-Mediated Reactionary
            Dentinogenesis via SEMA3A.
REFERENCE   3  (residues 1 to 771)
  AUTHORS   Yang,Y., Guan,W., Sheng,X.M. and Gu,H.J.
  TITLE     Role of Semaphorin 3A in common psychiatric illnesses such as
            schizophrenia, depression, and anxiety
  JOURNAL   Biochem Pharmacol 226, 116358 (2024)
   PUBMED   38857830
  REMARK    GeneRIF: Role of Semaphorin 3A in common psychiatric illnesses such
            as schizophrenia, depression, and anxiety.
            Review article
REFERENCE   4  (residues 1 to 771)
  AUTHORS   Lupo,F., Pezzini,F., Pasini,D., Fiorini,E., Adamo,A., Veghini,L.,
            Bevere,M., Frusteri,C., Delfino,P., D'agosto,S., Andreani,S.,
            Piro,G., Malinova,A., Wang,T., De Sanctis,F., Lawlor,R.T.,
            Hwang,C.I., Carbone,C., Amelio,I., Bailey,P., Bronte,V.,
            Tuveson,D., Scarpa,A., Ugel,S. and Corbo,V.
  TITLE     Axon guidance cue SEMA3A promotes the aggressive phenotype of
            basal-like PDAC
  JOURNAL   Gut 73 (8), 1321-1335 (2024)
   PUBMED   38670629
  REMARK    GeneRIF: Axon guidance cue SEMA3A promotes the aggressive phenotype
            of basal-like PDAC.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 771)
  AUTHORS   Takahashi,T., Nakamura,F., Jin,Z., Kalb,R.G. and Strittmatter,S.M.
  TITLE     Semaphorins A and E act as antagonists of neuropilin-1 and agonists
            of neuropilin-2 receptors
  JOURNAL   Nat Neurosci 1 (6), 487-493 (1998)
   PUBMED   10196546
REFERENCE   6  (residues 1 to 771)
  AUTHORS   Chen,H., Chedotal,A., He,Z., Goodman,C.S. and Tessier-Lavigne,M.
  TITLE     Neuropilin-2, a novel member of the neuropilin family, is a high
            affinity receptor for the semaphorins Sema E and Sema IV but not
            Sema III
  JOURNAL   Neuron 19 (3), 547-559 (1997)
   PUBMED   9331348
  REMARK    Erratum:[Neuron 1997 Sep;19(3):559]
REFERENCE   7  (residues 1 to 771)
  AUTHORS   Puschel,A.W., Adams,R.H. and Betz,H.
  TITLE     Murine semaphorin D/collapsin is a member of a diverse gene family
            and creates domains inhibitory for axonal extension
  JOURNAL   Neuron 14 (5), 941-948 (1995)
   PUBMED   7748561
REFERENCE   8  (residues 1 to 771)
  AUTHORS   Kolodkin,A.L., Matthes,D.J. and Goodman,C.S.
  TITLE     The semaphorin genes encode a family of transmembrane and secreted
            growth cone guidance molecules
  JOURNAL   Cell 75 (7), 1389-1399 (1993)
   PUBMED   8269517
REFERENCE   9  (residues 1 to 771)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   10 (residues 1 to 771)
  AUTHORS   Balasubramanian,R. and Crowley,W.F. Jr.
  TITLE     Isolated Gonadotropin-Releasing Hormone (GnRH) Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301509
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX491494.1, DR002146.1,
            L26081.1, BM723807.1, AC006322.2 and CR748125.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the semaphorin family and encodes
            a protein with an Ig-like C2-type (immunoglobulin-like) domain, a
            PSI domain and a Sema domain. This secreted protein can function as
            either a chemorepulsive agent, inhibiting axonal outgrowth, or as a
            chemoattractive agent, stimulating the growth of apical dendrites.
            In both cases, the protein is vital for normal neuronal pattern
            development. Increased expression of this protein is associated
            with schizophrenia and is seen in a variety of human tumor cell
            lines. Also, aberrant release of this protein is associated with
            the progression of Alzheimer's disease. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1441051.1, AK289954.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265362.9/ ENSP00000265362.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.11"
     Protein         1..771
                     /product="semaphorin-3A precursor"
                     /note="semaphorin L; semaphorin III; collapsin 1;
                     semaphorin D; sema domain, immunoglobulin domain (Ig),
                     short basic domain, secreted, (semaphorin) 3A"
                     /calculated_mol_wt=86487
     sig_peptide     1..21
                     /calculated_mol_wt=2421
     mat_peptide     22..771
                     /product="semaphorin-3A"
                     /calculated_mol_wt=86487
     Region          26..518
                     /region_name="Sema_3A"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 3A (Sema3A); cd11249"
                     /db_xref="CDD:200510"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14563.1)"
     Site            order(104..107,166..167,171,192,194..195,202,212,215..216,
                     218,223,252,276..280,282,397,401,404)
                     /site_type="other"
                     /note="putative plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200510"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14563.1)"
     Site            order(253..254,256,259..261,295,298..299,301,303,307,
                     330..337,363..366,410,425)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200510"
     Region          516..>552
                     /region_name="PSI"
                     /note="domain found in Plexins, Semaphorins and Integrins;
                     smart00423"
                     /db_xref="CDD:214655"
     Region          579..670
                     /region_name="Ig_Sema3"
                     /note="Immunoglobulin (Ig)-like domain of class III
                     semaphorin Sema3; cd05871"
                     /db_xref="CDD:409455"
     Region          579..585
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409455"
     Region          590..598
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409455"
     Site            590
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14563.1)"
     Site            order(592,637)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409455"
     Region          604..610
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409455"
     Region          612..615
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409455"
     Region          625..629
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409455"
     Region          632..639
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409455"
     Region          645..654
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409455"
     Region          657..670
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409455"
     Region          728..771
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14563.1)"
     CDS             1..771
                     /gene="SEMA3A"
                     /gene_synonym="coll-1; COLL1; HH16; Hsema-I; Hsema-III;
                     SEMA1; SEMAD; SEMAIII; SEMAL; SemD"
                     /coded_by="NM_006080.3:204..2519"
                     /db_xref="CCDS:CCDS5599.1"
                     /db_xref="GeneID:10371"
                     /db_xref="HGNC:HGNC:10723"
                     /db_xref="MIM:603961"
ORIGIN      
        1 mgwltrivcl fwgvlltara nyqngknnvp rlklsykeml esnnvitfng lansssyhtf
       61 lldeersrly vgakdhifsf dlvnikdfqk ivwpvsytrr deckwagkdi lkecanfikv
      121 lkaynqthly acgtgafhpi ctyieighhp ednifklens hfengrgksp ydpklltasl
      181 lidgelysgt aadfmgrdfa ifrtlghhhp irteqhdsrw lndpkfisah lisesdnped
      241 dkvyfffren aidgehsgka tharigqick ndfgghrslv nkwttflkar licsvpgpng
      301 idthfdelqd vflmnfkdpk npvvygvftt ssnifkgsav cmysmsdvrr vflgpyahrd
      361 gpnyqwvpyq grvpyprpgt cpsktfggfd stkdlpddvi tfarshpamy npvfpmnnrp
      421 iviktdvnyq ftqivvdrvd aedgqydvmf igtdvgtvlk vvsipketwy dleevlleem
      481 tvfreptais amelstkqqq lyigstagva qlplhrcdiy gkacaeccla rdpycawdgs
      541 acsryfptak rrtrrqdirn gdplthcsdl hhdnhhghsp eeriiygven sstflecspk
      601 sqralvywqf qrrneerkee irvddhiirt dqglllrslq qkdsgnylch avehgfiqtl
      661 lkvtlevidt ehleellhkd ddgdgsktke msnsmtpsqk vwyrdfmqli nhpnlntmde
      721 fceqvwkrdr kqrrqrpght pgnsnkwkhl qenkkgrnrr theferaprs v
//
LOCUS       NP_001354270             115 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 142 isoform 4 [Homo sapiens].
ACCESSION   NP_001354270
VERSION     NP_001354270.1
DBSOURCE    REFSEQ: accession NM_001367341.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Mir,A., Song,Y., Lee,H., Montazer-Zohouri,M., Reisi,M. and
            Tabatabaiefar,M.A.
  TITLE     A deleterious frameshift insertion mutation in the ZNF142 gene
            leads to intellectual developmental disorder with impaired speech
            in three affected siblings: Clinical features and literature review
  JOURNAL   Mol Genet Genomic Med 11 (12), e2261 (2023)
   PUBMED   37496384
  REMARK    GeneRIF: A deleterious frameshift insertion mutation in the ZNF142
            gene leads to intellectual developmental disorder with impaired
            speech in three affected siblings: Clinical features and literature
            review.
            Review article
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Christensen,M.B., Levy,A.M., Mohammadi,N.A., Niceta,M.,
            Kaiyrzhanov,R., Dentici,M.L., Al Alam,C., Alesi,V., Benoit,V.,
            Bhatia,K.P., Bierhals,T., Bosselmann,C.M., Buratti,J.,
            Callewaert,B., Ceulemans,B., Charles,P., De Wachter,M.,
            Dehghani,M., D'haenens,E., Doco-Fenzy,M., Gessner,M., Gobert,C.,
            Guliyeva,U., Haack,T.B., Hammer,T.B., Heinrich,T., Hempel,M.,
            Herget,T., Hoffmann,U., Horvath,J., Houlden,H., Keren,B.,
            Kresge,C., Kumps,C., Lederer,D., Lermine,A., Magrinelli,F.,
            Maroofian,R., Vahidi Mehrjardi,M.Y., Moudi,M., Muller,A.J.,
            Oostra,A.J., Pletcher,B.A., Ros-Pardo,D., Samarasekera,S.,
            Tartaglia,M., Van Schil,K., Vogt,J., Wassmer,E., Winkelmann,J.,
            Zaki,M.S., Zech,M., Lerche,H., Radio,F.C., Gomez-Puertas,P.,
            Moller,R.S. and Tumer,Z.
  TITLE     Biallelic variants in ZNF142 lead to a syndromic neurodevelopmental
            disorder
  JOURNAL   Clin Genet 102 (2), 98-109 (2022)
   PUBMED   35616059
  REMARK    GeneRIF: Biallelic variants in ZNF142 lead to a syndromic
            neurodevelopmental disorder.
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Kamal,N., Khamirani,H.J., Mohammadi,S., Dastgheib,S.A.,
            Dianatpour,M. and Tabei,S.M.B.
  TITLE     ZNF142 mutation causes neurodevelopmental disorder with speech
            impairment and seizures: Novel variants and literature review
  JOURNAL   Eur J Med Genet 65 (7), 104522 (2022)
   PUBMED   35618198
  REMARK    GeneRIF: ZNF142 mutation causes neurodevelopmental disorder with
            speech impairment and seizures: Novel variants and literature
            review.
            Review article
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Kameyama,S., Mizuguchi,T., Fukuda,H., Moey,L.H., Keng,W.T.,
            Okamoto,N., Tsuchida,N., Uchiyama,Y., Koshimizu,E., Hamanaka,K.,
            Fujita,A., Miyatake,S. and Matsumoto,N.
  TITLE     Biallelic null variants in ZNF142 cause global developmental delay
            with familial epilepsy and dysmorphic features
  JOURNAL   J Hum Genet 67 (3), 169-173 (2022)
   PUBMED   34531528
  REMARK    GeneRIF: Biallelic null variants in ZNF142 cause global
            developmental delay with familial epilepsy and dysmorphic features.
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Ahmeti,K.B., Ajroud-Driss,S., Al-Chalabi,A., Andersen,P.M.,
            Armstrong,J., Birve,A., Blauw,H.M., Brown,R.H., Bruijn,L., Chen,W.,
            Chio,A., Comeau,M.C., Cronin,S., Diekstra,F.P., Soraya Gkazi,A.,
            Glass,J.D., Grab,J.D., Groen,E.J., Haines,J.L., Hardiman,O.,
            Heller,S., Huang,J., Hung,W.Y., Jaworski,J.M., Jones,A., Khan,H.,
            Landers,J.E., Langefeld,C.D., Leigh,P.N., Marion,M.C.,
            McLaughlin,R.L., Meininger,V., Melki,J., Miller,J.W., Mora,G.,
            Pericak-Vance,M.A., Rampersaud,E., Robberecht,W., Russell,L.P.,
            Salachas,F., Saris,C.G., Shatunov,A., Shaw,C.E., Siddique,N.,
            Siddique,T., Smith,B.N., Sufit,R., Topp,S., Traynor,B.J., Vance,C.,
            van Damme,P., van den Berg,L.H., van Es,M.A., van Vught,P.W.,
            Veldink,J.H., Yang,Y. and Zheng,J.G.
  CONSRTM   ITALSGEN consortium; ALSGEN Consortium
  TITLE     Age of onset of amyotrophic lateral sclerosis is modulated by a
            locus on 1p34.1
  JOURNAL   Neurobiol Aging 34 (1), 357 (2013)
   PUBMED   22959728
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079810.4 and AC012510.8.
            
            Summary: The protein encoded by this gene belongs to the Kruppel
            family of C2H2-type zinc finger proteins. It contains 31 C2H2-type
            zinc fingers and may be involved in transcriptional regulation.
            Alternatively spliced transcript variants have been found for this
            gene. [provided by RefSeq, Jan 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.465583.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..115
                     /product="zinc finger protein 142 isoform 4"
                     /note="zinc finger protein 142 (clone pHZ-49)"
                     /calculated_mol_wt=11607
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52746.4)"
     CDS             1..115
                     /gene="ZNF142"
                     /gene_synonym="HA4654; NEDISHM; pHZ-49"
                     /coded_by="NM_001367341.1:617..964"
                     /note="isoform 4 is encoded by transcript variant 9"
                     /db_xref="GeneID:7701"
                     /db_xref="HGNC:HGNC:12927"
                     /db_xref="MIM:604083"
ORIGIN      
        1 mtdplldsqp asstgemdgl cpelllippp lsnrgilgpv qspcpsrdpa piptepgcll
       61 veatateegp gnmeiivetv agtltpgapg etpgtntvas rpvgqaalrf clgyf
//
LOCUS       NP_001346227             312 aa            linear   ROD 27-APR-2025
DEFINITION  protein YIPF2 [Mus musculus].
ACCESSION   NP_001346227 XP_011240919
VERSION     NP_001346227.1
DBSOURCE    REFSEQ: accession NM_001359298.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC163748.6.
            
            On Dec 30, 2017 this sequence version replaced XP_011240919.1.
            
            Transcript Variant: This variant (5) differs in the 3' UTR,
            compared to variant 1. Variants 1, 2, 3, 5 and 6 encode the same
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.642733.1,
                                           SRR7345562.4842572.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135, SAMN01164138
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 7.83 cM"
     Protein         1..312
                     /product="protein YIPF2"
                     /calculated_mol_wt=34769
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWQ6; propagated from
                     UniProtKB/Swiss-Prot (Q99LP8.1)"
     Region          99..261
                     /region_name="Yip1"
                     /note="Yip1 domain; pfam04893"
                     /db_xref="CDD:461468"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LP8.1)"
     Site            161..181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LP8.1)"
     Site            194..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LP8.1)"
     Site            229..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LP8.1)"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LP8.1)"
     CDS             1..312
                     /gene="Yipf2"
                     /gene_synonym="1300010K09Rik"
                     /coded_by="NM_001359298.1:274..1212"
                     /db_xref="CCDS:CCDS22907.1"
                     /db_xref="GeneID:74766"
                     /db_xref="MGI:MGI:1922016"
ORIGIN      
        1 maaadelafh efeeatnlla etpdaattsq sdeltsrehv avvvgsgigy gaevgeeedd
       61 ktsllqeekp qprfwtfdyy qsffdvdtsq vldrikgsll phpghnfvrh hlrnrpdlyg
      121 pfwicatlaf vlavtgnltl vlaqrrdpsi hyspqfhkvt iagitiycya wlvplalwgf
      181 lrwrqgtrer mglytfletv cvygyslfvf iptvvlwlip vqwiqwlfga lglalsaagl
      241 vftlwpvvre dtrlvaaall stvvllhall algcklyffq plpldhvvpa pqatppspnv
      301 llpssiqpmt ts
//
LOCUS       NP_001019846             245 aa            linear   PRI 27-APR-2025
DEFINITION  actin-like protein 10 [Homo sapiens].
ACCESSION   NP_001019846
VERSION     NP_001019846.1
DBSOURCE    REFSEQ: accession NM_001024675.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC137111.1 and AW006704.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC137114.1, DRR138520.599244.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000677665.1/ ENSP00000504425.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..245
                     /product="actin-like protein 10"
                     /calculated_mol_wt=26620
     Region          <5..236
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
     CDS             1..245
                     /gene="ACTL10"
                     /gene_synonym="C20orf134; dJ63M2.2"
                     /coded_by="NM_001024675.2:556..1293"
                     /db_xref="CCDS:CCDS33463.1"
                     /db_xref="GeneID:170487"
                     /db_xref="HGNC:HGNC:16127"
ORIGIN      
        1 mastallalc stgafsglav eagagvchat piyaghswhq atfrlnvags tlsrylrdll
       61 vaanpdllqq alprkaithl kkrscyvsld fegdlrdpar hhpasfsvgn gccvclsser
      121 frcpepifqp gllgqaeqgl palafralqk mpktlrtrla dtvvlaggst lfpgfaerld
      181 keleaqcrrh gyaalrphlv akhgrgmavw tggsmvaslh sfqrrwitra myqecgsrll
      241 ydvfn
//
LOCUS       NP_033431                182 aa            linear   ROD 27-APR-2025
DEFINITION  troponin I, fast skeletal muscle [Mus musculus].
ACCESSION   NP_033431 XP_006508602
VERSION     NP_033431.1
DBSOURCE    REFSEQ: accession NM_009405.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Montanes-Agudo,P., Aufiero,S., Schepers,E.N., van der Made,I.,
            Cocera-Ortega,L., Ernault,A.C., Richard,S., Kuster,D.W.D.,
            Christoffels,V.M., Pinto,Y.M. and Creemers,E.E.
  TITLE     The RNA-binding protein QKI governs a muscle-specific alternative
            splicing program that shapes the contractile function of
            cardiomyocytes
  JOURNAL   Cardiovasc Res 119 (5), 1161-1174 (2023)
   PUBMED   36627242
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Gao,M., Liu,X., Guo,P., Wang,J., Li,J., Wang,W., Stoddart,M.J.,
            Grad,S., Li,Z., Wu,H., Li,B., He,Z., Zhou,G., Liu,S., Zhu,W.,
            Chen,D., Zou,X. and Zhou,Z.
  TITLE     Deciphering postnatal limb development at single-cell resolution
  JOURNAL   iScience 26 (1), 105808 (2022)
   PUBMED   36619982
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Wu,T., Liang,Z., Zhang,Z., Liu,C., Zhang,L., Gu,Y., Peterson,K.L.,
            Evans,S.M., Fu,X.D. and Chen,J.
  TITLE     PRDM16 Is a Compact Myocardium-Enriched Transcription Factor
            Required to Maintain Compact Myocardial Cardiomyocyte Identity in
            Left Ventricle
  JOURNAL   Circulation 145 (8), 586-602 (2022)
   PUBMED   34915728
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Tan,C., Zhu,S., Chen,Z., Liu,C., Li,Y.E., Zhu,M., Zhang,Z.,
            Zhang,Z., Zhang,L., Gu,Y., Liang,Z., Boyer,T.G., Ouyang,K.,
            Evans,S.M. and Fang,X.
  TITLE     Mediator complex proximal Tail subunit MED30 is critical for
            Mediator core stability and cardiomyocyte transcriptional network
  JOURNAL   PLoS Genet 17 (9), e1009785 (2021)
   PUBMED   34506481
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Guenet,J.L., Simon-Chazottes,D., Gravel,M., Hastings,K.E. and
            Schiaffino,S.
  TITLE     Cardiac and skeletal muscle troponin I isoforms are encoded by a
            dispersed gene family on mouse chromosomes 1 and 7
  JOURNAL   Mamm Genome 7 (1), 13-15 (1996)
   PUBMED   8903721
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Zhu,L., Lyons,G.E., Juhasz,O., Joya,J.E., Hardeman,E.C. and Wade,R.
  TITLE     Developmental regulation of troponin I isoform genes in striated
            muscles of transgenic mice
  JOURNAL   Dev Biol 169 (2), 487-503 (1995)
   PUBMED   7781893
REFERENCE   8  (residues 1 to 182)
  AUTHORS   Braun,T. and Arnold,H.H.
  TITLE     Inactivation of Myf-6 and Myf-5 genes in mice leads to alterations
            in skeletal muscle development
  JOURNAL   EMBO J 14 (6), 1176-1186 (1995)
   PUBMED   7720708
REFERENCE   9  (residues 1 to 182)
  AUTHORS   Chen,Z., Friedrich,G.A. and Soriano,P.
  TITLE     Transcriptional enhancer factor 1 disruption by a retroviral gene
            trap leads to heart defects and embryonic lethality in mice
  JOURNAL   Genes Dev 8 (19), 2293-2301 (1994)
   PUBMED   7958896
REFERENCE   10 (residues 1 to 182)
  AUTHORS   Koppe,R.I., Hallauer,P.L., Karpati,G. and Hastings,K.E.
  TITLE     cDNA clone and expression analysis of rodent fast and slow skeletal
            muscle troponin I mRNAs
  JOURNAL   J Biol Chem 264 (24), 14327-14333 (1989)
   PUBMED   2760067
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL603651.14.
            
            On Jun 5, 2018 this sequence version replaced XP_006508602.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB575219.1, CB588547.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 87.93 cM"
     Protein         1..182
                     /product="troponin I, fast skeletal muscle"
                     /calculated_mol_wt=21226
     Region          2..48
                     /region_name="Involved in binding TNC"
                     /note="propagated from UniProtKB/Swiss-Prot (P13412.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0000250|UniProtKB:P02643; propagated from
                     UniProtKB/Swiss-Prot (P13412.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02643; propagated from
                     UniProtKB/Swiss-Prot (P13412.2)"
     Region          15..145
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     Region          29..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13412.2)"
     Region          97..117
                     /region_name="Involved in binding TNC and actin"
                     /note="propagated from UniProtKB/Swiss-Prot (P13412.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02643; propagated from
                     UniProtKB/Swiss-Prot (P13412.2)"
     CDS             1..182
                     /gene="Tnni2"
                     /coded_by="NM_009405.3:76..624"
                     /db_xref="CCDS:CCDS40192.1"
                     /db_xref="GeneID:21953"
                     /db_xref="MGI:MGI:105070"
ORIGIN      
        1 mgdeekrnra itarrqhlks vmlqiaatel ekeesrrese kenylsehcp plhipgsmse
       61 vqelckqlha kidvaeeeky dmevkvqkss keledmnqkl fdlrgkfkrp plrrvrmsad
      121 amlkallgsk hkvcmdlran lkqvkkedte kerdlrdvgd wrknieeksg megrkkmfes
      181 es
//
LOCUS       NP_036370                747 aa            linear   PRI 27-APR-2025
DEFINITION  NAD-dependent protein deacetylase sirtuin-1 isoform a [Homo
            sapiens].
ACCESSION   NP_036370
VERSION     NP_036370.2
DBSOURCE    REFSEQ: accession NM_012238.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Zhao,Y., Wang,Y., Zheng,H., Xu,Q., Zhou,K., Liu,H., Xia,Y.,
            Wei,D.H., Jiang,M., Tang,Z.H., Liu,L.S., Zheng,H. and Jiang,Z.
  TITLE     Hydrogen sulfide upregulates SIRT1 to inhibit ox-HDL-induced
            endothelial cell damage and mitochondrial dysfunction
  JOURNAL   Nitric Oxide 152, 78-89 (2024)
   PUBMED   39305980
  REMARK    GeneRIF: Hydrogen sulfide upregulates SIRT1 to inhibit
            ox-HDL-induced endothelial cell damage and mitochondrial
            dysfunction.
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Nevoral,J., Drutovic,D., Vaskovicova,M., Benc,M., Liska,F.,
            Valentova,I., Stachovicova,S., Kubovciak,J., Havrankova,J.,
            Shavit,M., Monsef,L., Iniesta-Cuerda,M., Zalmanova,T., Hosek,P.,
            Strejcek,F., Kralickova,M. and Petr,J.
  TITLE     Dynamics and necessity of SIRT1 for maternal-zygotic transition
  JOURNAL   Sci Rep 14 (1), 21598 (2024)
   PUBMED   39285243
  REMARK    GeneRIF: Dynamics and necessity of SIRT1 for maternal-zygotic
            transition.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Chen,J., Chen,K., Zhang,S. and Huang,X.
  TITLE     SIRT1 silencing ameliorates malignancy of non-small cell lung
            cancer via activating FOXO1
  JOURNAL   Sci Rep 14 (1), 19948 (2024)
   PUBMED   39198693
  REMARK    GeneRIF: SIRT1 silencing ameliorates malignancy of non-small cell
            lung cancer via activating FOXO1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Yang,K., Wu,Y., Zhang,R., Lei,X.P., Kang,L. and Dong,W.B.
  TITLE     [Role of reactive oxygen species/silent information regulator 1 in
            hyperoxia-induced bronchial epithelial cell injury]
  JOURNAL   Zhongguo Dang Dai Er Ke Za Zhi 26 (8), 852-860 (2024)
   PUBMED   39148391
  REMARK    GeneRIF: [Role of reactive oxygen species/silent information
            regulator 1 in hyperoxia-induced bronchial epithelial cell injury].
REFERENCE   5  (residues 1 to 747)
  AUTHORS   Zhang,X., Wang,Y., Xu,F., Zhao,B., Liang,X. and Shu,J.
  TITLE     Downregulation of miR-138-5p alleviates propofol-induced
            neurotoxicity and autophagy by regulating SIRT1
  JOURNAL   Hum Exp Toxicol 43, 9603271241269021 (2024)
   PUBMED   39441175
  REMARK    GeneRIF: Downregulation of miR-138-5p alleviates propofol-induced
            neurotoxicity and autophagy by regulating SIRT1.
REFERENCE   6  (residues 1 to 747)
  AUTHORS   Giblin,W., Skinner,M.E. and Lombard,D.B.
  TITLE     Sirtuins: guardians of mammalian healthspan
  JOURNAL   Trends Genet 30 (7), 271-286 (2014)
   PUBMED   24877878
  REMARK    Review article
REFERENCE   7  (residues 1 to 747)
  AUTHORS   Vaziri,H., Dessain,S.K., Ng Eaton,E., Imai,S.I., Frye,R.A.,
            Pandita,T.K., Guarente,L. and Weinberg,R.A.
  TITLE     hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
  JOURNAL   Cell 107 (2), 149-159 (2001)
   PUBMED   11672523
REFERENCE   8  (residues 1 to 747)
  AUTHORS   Luo,J., Nikolaev,A.Y., Imai,S., Chen,D., Su,F., Shiloh,A.,
            Guarente,L. and Gu,W.
  TITLE     Negative control of p53 by Sir2alpha promotes cell survival under
            stress
  JOURNAL   Cell 107 (2), 137-148 (2001)
   PUBMED   11672522
  REMARK    GeneRIF: SIRT1(Sir2alpha) deacetylates p53 and promotes survival
REFERENCE   9  (residues 1 to 747)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   10 (residues 1 to 747)
  AUTHORS   Frye,R.A.
  TITLE     Characterization of five human cDNAs with homology to the yeast
            SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may
            have protein ADP-ribosyltransferase activity
  JOURNAL   Biochem Biophys Res Commun 260 (1), 273-279 (1999)
   PUBMED   10381378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133551.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 27, 2000 this sequence version replaced NP_036370.1.
            
            Summary: This gene encodes a member of the sirtuin family of
            proteins, homologs to the yeast Sir2 protein. Members of the
            sirtuin family are characterized by a sirtuin core domain and
            grouped into four classes. The functions of human sirtuins have not
            yet been determined; however, yeast sirtuin proteins are known to
            regulate epigenetic gene silencing and suppress recombination of
            rDNA. Studies suggest that the human sirtuins may function as
            intracellular regulatory proteins with mono-ADP-ribosyltransferase
            activity. The protein encoded by this gene is included in class I
            of the sirtuin family. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Dec 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012499.1, AF083106.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000212015.11/ ENSP00000212015.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..747
                     /product="NAD-dependent protein deacetylase sirtuin-1
                     isoform a"
                     /EC_number="2.3.1.286"
                     /note="sirtuin type 1; SIR2-like protein 1; regulatory
                     protein SIR2 homolog 1; NAD-dependent protein deacetylase
                     sirtuin-1; NAD-dependent protein deacylase sirtuin-1"
                     /calculated_mol_wt=81550
     Region          1..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     mat_peptide     2..533
                     /product="SirtT1 75 kDa fragment. /id=PRO_0000415289"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
                     /calculated_mol_wt=58224
     Region          2..268
                     /region_name="Interaction with H1-4.
                     /evidence=ECO:0000269|PubMed:15469825"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          2..139
                     /region_name="Interaction with CLOCK.
                     /evidence=ECO:0000250|UniProtKB:Q923E4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19107194,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19107194; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8.
                     /evidence=ECO:0000269|PubMed:18838864,
                     ECO:0000269|PubMed:19107194, ECO:0000269|PubMed:20027304,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          32..39
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8.
                     /evidence=ECO:0000269|PubMed:18838864,
                     ECO:0000269|PubMed:19107194, ECO:0000269|PubMed:20027304,
                     ECO:0000269|PubMed:21471201, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          138..145
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          143..541
                     /region_name="Interaction with CCAR2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:19107194; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:19107194; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19107194; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19107194; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          223..230
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            238
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q923E4; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          254..489
                     /region_name="SIRT1"
                     /note="Eukaryotic group (class1) which includes human
                     sirtuins SIRT1-3 and yeast Hst1-4; and are members of the
                     SIR2 family of proteins, silent information regulator 2
                     (Sir2) enzymes which catalyze NAD+-dependent
                     protein/histone deacetylation. Sir2 proteins...; cd01408"
                     /db_xref="CDD:238699"
     Region          256..259
                     /region_name="Required for interaction with the sumoylated
                     form of CCAR2. /evidence=ECO:0000269|PubMed:25406032"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            order(263,265..266,273..274,327,345..346,348,363,440,445,
                     466..467,481)
                     /site_type="other"
                     /note="NAD+ binding site [chemical binding]"
                     /db_xref="CDD:238699"
     Site            order(347,363,412,414..418,444..446)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238699"
     Site            order(371,374,395,398)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:238699"
     Site            377
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q923E4; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          425..431
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            430
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q923E4; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            513
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q923E4; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          523..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by DYRK1A, DYRK3 and MAPK8.
                     /evidence=ECO:0000269|PubMed:19107194,
                     ECO:0000269|PubMed:20027304, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          538..540
                     /region_name="Phosphorylated at one of three serine
                     residues"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:19107194; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:19107194; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          562..587
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            610
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q923E4; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2.
                     /evidence=ECO:0000250|UniProtKB:Q923E4; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2.
                     /evidence=ECO:0000305|PubMed:19236849; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     Region          663..726
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19107194,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96EB6.2)"
     Site            747
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19107194; propagated from
                     UniProtKB/Swiss-Prot (Q96EB6.2)"
     CDS             1..747
                     /gene="SIRT1"
                     /gene_synonym="SIR2; SIR2alpha; SIR2L1"
                     /coded_by="NM_012238.5:67..2310"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7273.1"
                     /db_xref="GeneID:23411"
                     /db_xref="HGNC:HGNC:14929"
                     /db_xref="MIM:604479"
ORIGIN      
        1 madeaalalq pggspsaaga dreaasspag eplrkrprrd gpglerspge pggaaperev
       61 paaargcpga aaaalwreae aeaaaaggeq eaqataaage gdngpglqgp sreppladnl
      121 ydeddddege eeeeaaaaai gyrdnllfgd eiitngfhsc esdeedrash asssdwtprp
      181 rigpytfvqq hlmigtdprt ilkdllpeti pppelddmtl wqivinilse ppkrkkrkdi
      241 ntiedavkll qeckkiivlt gagvsvscgi pdfrsrdgiy arlavdfpdl pdpqamfdie
      301 yfrkdprpff kfakeiypgq fqpslchkfi alsdkegkll rnytqnidtl eqvagiqrii
      361 qchgsfatas clickykvdc eavrgdifnq vvprcprcpa deplaimkpe ivffgenlpe
      421 qfhramkydk devdllivig sslkvrpval ipssiphevp qilinreplp hlhfdvellg
      481 dcdviinelc hrlggeyakl ccnpvklsei tekpprtqke laylselppt plhvsedsss
      541 pertsppdss vivtlldqaa ksnddldvse skgcmeekpq evqtsrnves iaeqmenpdl
      601 knvgsstgek nertsvagtv rkcwpnrvak eqisrrldgn qylflppnry ifhgaevysd
      661 seddvlssss cgsnsdsgtc qspsleepme deseieefyn gledepdvpe raggagfgtd
      721 gddqeainea isvkqevtdm nypsnks
//
LOCUS       NP_859054                358 aa            linear   PRI 27-APR-2025
DEFINITION  gap junction alpha-5 protein [Homo sapiens].
ACCESSION   NP_859054
VERSION     NP_859054.1
DBSOURCE    REFSEQ: accession NM_181703.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Zhai,P., Zhang,H., Li,Q., Yang,M., Guo,Y. and Xing,C.
  TITLE     DNMT1-mediated NR3C1 DNA methylation enables transcription
            activation of connexin40 and augments angiogenesis during
            colorectal cancer progression
  JOURNAL   Gene 892, 147887 (2024)
   PUBMED   37813207
  REMARK    GeneRIF: DNMT1-mediated NR3C1 DNA methylation enables transcription
            activation of connexin40 and augments angiogenesis during
            colorectal cancer progression.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Lian,Z., Ma,Z., Zhang,Z.L., Liu,P.L., Zhang,G.Y. and Guo,C.X.
  TITLE     Association between polymorphisms in connexin 40 gene (Cx40) and
            risk of atrial fibrillation: a meta-analysis based on 3,452
            subjects
  JOURNAL   Biomarkers 28 (6), 519-530 (2023)
   PUBMED   37382580
  REMARK    GeneRIF: Association between polymorphisms in connexin 40 gene
            (Cx40) and risk of atrial fibrillation: a meta-analysis based on
            3,452 subjects.
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Touat-Hamici,Z., Blancard,M., Ma,R., Lin,L., Iddir,Y., Denjoy,I.,
            Leenhardt,A., Yuchi,Z. and Guicheney,P.
  TITLE     A SPRY1 domain cardiac ryanodine receptor variant associated with
            short-coupled torsade de pointes
  JOURNAL   Sci Rep 11 (1), 5243 (2021)
   PUBMED   33664309
  REMARK    GeneRIF: A SPRY1 domain cardiac ryanodine receptor variant
            associated with short-coupled torsade de pointes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Zhao,Z., Liu,G., Zhang,H., Ruan,P., Ge,J. and Liu,Q.
  TITLE     BIRC5, GAJ5, and lncRNA NPHP3-AS1 Are Correlated with the
            Development of Atrial Fibrillation-Valvular Heart Disease
  JOURNAL   Int Heart J 62 (1), 153-161 (2021)
   PUBMED   33518654
  REMARK    GeneRIF: BIRC5, GAJ5, and lncRNA NPHP3-AS1 Are Correlated with the
            Development of Atrial Fibrillation-Valvular Heart Disease.
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Chen,S.C., Davis,L.M., Westphale,E.M., Beyer,E.C. and Saffitz,J.E.
  TITLE     Expression of multiple gap junction proteins in human fetal and
            infant hearts
  JOURNAL   Pediatr Res 36 (5), 561-566 (1994)
   PUBMED   7877871
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Kanter,H.L., Saffitz,J.E. and Beyer,E.C.
  TITLE     Molecular cloning of two human cardiac gap junction proteins,
            connexin40 and connexin45
  JOURNAL   J Mol Cell Cardiol 26 (7), 861-868 (1994)
   PUBMED   7966354
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Guo,R. and Haldeman-Englert,C.R.
  TITLE     1q21.1 Recurrent Deletion
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21348049
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Kanter,H.L., Saffitz,J.E. and Beyer,E.C.
  TITLE     Cardiac myocytes express multiple gap junction proteins
  JOURNAL   Circ Res 70 (2), 438-444 (1992)
   PUBMED   1310450
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Willecke,K., Jungbluth,S., Dahl,E., Hennemann,H., Heynkes,R. and
            Grzeschik,K.H.
  TITLE     Six genes of the human connexin gene family coding for gap
            junctional proteins are assigned to four different human
            chromosomes
  JOURNAL   Eur J Cell Biol 53 (2), 275-280 (1990)
   PUBMED   1964417
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX377692.2, BC013313.2,
            AF074995.1 and BM970701.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the connexin gene family. The
            encoded protein is a component of gap junctions, which are composed
            of arrays of intercellular channels that provide a route for the
            diffusion of low molecular weight materials from cell to cell.
            Mutations in this gene may be associated with atrial fibrillation.
            Alternatively spliced transcript variants encoding the same isoform
            have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (B) differs in the 5' UTR compared
            to variant A. Variants A and B encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013313.2, SRR7346977.1420562.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMN03568912
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000579774.3/ ENSP00000463851.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..358
                     /product="gap junction alpha-5 protein"
                     /note="connexin 40; gap junction protein alpha 5 40kDa"
                     /calculated_mol_wt=40249
     Region          3..211
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36382.3)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36382.3)"
     Site            165..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36382.3)"
     Site            206..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36382.3)"
     Region          258..358
                     /region_name="Connexin40_C"
                     /note="Connexin 40 C-terminal domain; pfam16791"
                     /db_xref="CDD:465272"
     Region          319..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36382.3)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28234; propagated from
                     UniProtKB/Swiss-Prot (P36382.3)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28234; propagated from
                     UniProtKB/Swiss-Prot (P36382.3)"
     CDS             1..358
                     /gene="GJA5"
                     /gene_synonym="ATFB11; CX40"
                     /coded_by="NM_181703.4:138..1214"
                     /db_xref="CCDS:CCDS929.1"
                     /db_xref="GeneID:2702"
                     /db_xref="HGNC:HGNC:4279"
                     /db_xref="MIM:121013"
ORIGIN      
        1 mgdwsflgnf leevhkhstv vgkvwltvlf ifrmlvlgta aesswgdeqa dfrcdtiqpg
       61 cqnvcydqaf pishirywvl qiifvstpsl vymghamhtv rmqekrklre aerakevrgs
      121 gsyeypvaek aelscweegn grialqgtll ntyvcsilir ttmevgfivg qyfiygiflt
      181 tlhvcrrspc phpvncyvsr pteknvfivf mlavaalsll lslaelyhlg wkkirqrfvk
      241 prqhmakcql sgpsvgivqs ctpppdfnqc lengpggkff npfsnnmasq qntdnlvteq
      301 vrgqeqtpge gfiqvrygqk pevpngvspg hrlphgyhsd krrlskassk arsddlsv
//
LOCUS       NP_001346893             404 aa            linear   ROD 27-APR-2025
DEFINITION  N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D isoform
            a [Mus musculus].
ACCESSION   NP_001346893 XP_006535773
VERSION     NP_001346893.1
DBSOURCE    REFSEQ: accession NM_001359964.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Tevosian,M., Todorov,H., Lomazzo,E., Bindila,L., Ueda,N.,
            Bassetti,D., Warm,D., Kirischuk,S., Luhmann,H.J., Gerber,S. and
            Lutz,B.
  TITLE     NAPE-PLD deletion in stress-TRAPed neurons results in an anxiogenic
            phenotype
  JOURNAL   Transl Psychiatry 13 (1), 152 (2023)
   PUBMED   37149657
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Palese,F., Pontis,S., Realini,N. and Piomelli,D.
  TITLE     NAPE-specific phospholipase D regulates LRRK2 association with
            neuronal membranes
  JOURNAL   Adv Pharmacol 90, 217-238 (2021)
   PUBMED   33706934
  REMARK    GeneRIF: NAPE-specific phospholipase D regulates LRRK2 association
            with neuronal membranes.
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Rastelli,M., Van Hul,M., Terrasi,R., Lefort,C., Regnier,M.,
            Beiroa,D., Delzenne,N.M., Everard,A., Nogueiras,R., Luquet,S.,
            Muccioli,G.G. and Cani,P.D.
  TITLE     Intestinal NAPE-PLD contributes to short-term regulation of food
            intake via gut-to-brain axis
  JOURNAL   Am J Physiol Endocrinol Metab 319 (3), E647-E657 (2020)
   PUBMED   32776827
  REMARK    GeneRIF: Intestinal NAPE-PLD contributes to short-term regulation
            of food intake via gut-to-brain axis.
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Aggarwal,G., Zarrow,J.E., Mashhadi,Z., Flynn,C.R., Vinson,P.,
            Weaver,C.D. and Davies,S.S.
  TITLE     Symmetrically substituted dichlorophenes inhibit
            N-acyl-phosphatidylethanolamine phospholipase D
  JOURNAL   J Biol Chem 295 (21), 7289-7300 (2020)
   PUBMED   32284327
  REMARK    GeneRIF: Symmetrically substituted dichlorophenes inhibit
            N-acyl-phosphatidylethanolamine phospholipase D.
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Lefort,C., Roumain,M., Van Hul,M., Rastelli,M., Manco,R.,
            Leclercq,I., Delzenne,N.M., Marzo,V.D., Flamand,N., Luquet,S.,
            Silvestri,C., Muccioli,G.G. and Cani,P.D.
  TITLE     Hepatic NAPE-PLD Is a Key Regulator of Liver Lipid Metabolism
  JOURNAL   Cells 9 (5), 1247 (2020)
   PUBMED   32443626
  REMARK    GeneRIF: Hepatic NAPE-PLD Is a Key Regulator of Liver Lipid
            Metabolism.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Simon,G.M. and Cravatt,B.F.
  TITLE     Endocannabinoid biosynthesis proceeding through
            glycerophospho-N-acyl ethanolamine and a role for
            alpha/beta-hydrolase 4 in this pathway
  JOURNAL   J Biol Chem 281 (36), 26465-26472 (2006)
   PUBMED   16818490
  REMARK    GeneRIF: Results support the existence of an N-acyl
            phosphatidylethanolamine (NAPE)-phospholipase D-independent route
            for N-acyl ethanolamine (NAE) biosynthesis and suggest that Abh4
            plays a role in this pathway by acting as a (lyso)NAPE-selective
            lipase.
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Wang,J., Okamoto,Y., Morishita,J., Tsuboi,K., Miyatake,A. and
            Ueda,N.
  TITLE     Functional analysis of the purified anandamide-generating
            phospholipase D as a member of the metallo-beta-lactamase family
  JOURNAL   J Biol Chem 281 (18), 12325-12335 (2006)
   PUBMED   16527816
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Leung,D., Saghatelian,A., Simon,G.M. and Cravatt,B.F.
  TITLE     Inactivation of N-acyl phosphatidylethanolamine phospholipase D
            reveals multiple mechanisms for the biosynthesis of
            endocannabinoids
  JOURNAL   Biochemistry 45 (15), 4720-4726 (2006)
   PUBMED   16605240
  REMARK    GeneRIF: Inactivation of N-acyl phosphatidylethanolamine
            phospholipase D reveals multiple mechanisms for the biosynthesis of
            endocannabinoids.
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Okamoto,Y., Morishita,J., Wang,J., Schmid,P.C., Krebsbach,R.J.,
            Schmid,H.H. and Ueda,N.
  TITLE     Mammalian cells stably overexpressing
            N-acylphosphatidylethanolamine-hydrolysing phospholipase D exhibit
            significantly decreased levels of N-acylphosphatidylethanolamines
  JOURNAL   Biochem J 389 (Pt 1), 241-247 (2005)
   PUBMED   15760304
  REMARK    GeneRIF: results confirm that overexpressed NAPE-PLD is capable of
            forming NAEs, including anandamide, in living cells
REFERENCE   10 (residues 1 to 404)
  AUTHORS   Okamoto,Y., Morishita,J., Tsuboi,K., Tonai,T. and Ueda,N.
  TITLE     Molecular characterization of a phospholipase D generating
            anandamide and its congeners
  JOURNAL   J Biol Chem 279 (7), 5298-5305 (2004)
   PUBMED   14634025
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125343.2 and AC161484.4.
            
            On Jan 20, 2018 this sequence version replaced XP_006535773.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.15778.1,
                                           ERR3363658.3440394.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164141, SAMN01164143
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 9.97 cM"
     Protein         1..404
                     /product="N-acyl-phosphatidylethanolamine-hydrolyzing
                     phospholipase D isoform a"
                     /EC_number="3.1.4.54"
                     /note="Metallo-beta-lactamase domain containing 1;
                     N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase
                     D; NAPE-hydrolyzing phospholipase D"
                     /calculated_mol_wt=46703
     Region          137..324
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
     Site            order(193,195,197..198,271..272,292,324)
                     /site_type="active"
                     /db_xref="CDD:293792"
     CDS             1..404
                     /gene="Napepld"
                     /gene_synonym="A530089G06; Mbldc1; NAPE-PLD"
                     /coded_by="NM_001359964.1:231..1445"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:242864"
                     /db_xref="MGI:MGI:2140885"
ORIGIN      
        1 mhffsprdmd eyedsqspap syqypketlr krqnsvqnsg gsvssrfsrk sfkldyrlee
       61 dvtkskkgkd grfvnpwptw knisipnvlr wlimeknhsg vpgskeeldk elpvlkpyfv
      121 sdpedagvre aglrvtwlgh atlmvemdel ifltdpmfss raspsqymgp krfrrppcti
      181 selptidavl ishnhydhld ygsvlalner fgselrwfvp lglldwmqkc gcenvieldw
      241 weencvpghd kvtfvftpsq hwckrtlldd nkvlwgswsv lgpwsrfffa gdtgycpafe
      301 eigkrfgpfd laaipigaye prwfmkyqha dpedavrihi dlqtkrsvai hwgtfalane
      361 hyleppvkln ealeryglsc edffilkhge srylntddra feet
//
LOCUS       NP_000150                438 aa            linear   PRI 27-APR-2025
DEFINITION  glutaryl-CoA dehydrogenase, mitochondrial isoform a precursor [Homo
            sapiens].
ACCESSION   NP_000150
VERSION     NP_000150.1
DBSOURCE    REFSEQ: accession NM_000159.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Lao,Y., Cui,X., Xu,Z., Yan,H., Zhang,Z., Zhang,Z., Geng,L., Li,B.,
            Lu,Y., Guan,Q., Pu,X., Zhao,S., Zhu,J., Qin,X. and Sun,B.
  TITLE     Glutaryl-CoA dehydrogenase suppresses tumor progression and shapes
            an anti-tumor microenvironment in hepatocellular carcinoma
  JOURNAL   J Hepatol 81 (5), 847-861 (2024)
   PUBMED   38825017
  REMARK    GeneRIF: Glutaryl-CoA dehydrogenase suppresses tumor progression
            and shapes an anti-tumor microenvironment in hepatocellular
            carcinoma.
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhou,J., Li,G., Deng,L., Zhao,P., Zeng,Y., Qiu,X., Luo,J. and Xu,L.
  TITLE     Biochemical and molecular features of chinese patients with
            glutaric acidemia type 1 from Fujian Province, southeastern China
  JOURNAL   Orphanet J Rare Dis 18 (1), 215 (2023)
   PUBMED   37496092
  REMARK    GeneRIF: Biochemical and molecular features of chinese patients
            with glutaric acidemia type 1 from Fujian Province, southeastern
            China.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Guo,Z., Gong,A., Liu,S. and Liang,H.
  TITLE     Two novel compound heterozygous variants of the GCDH gene in two
            Chinese families with glutaric acidaemia type I identified by
            high-throughput sequencing and a literature review
  JOURNAL   Mol Genet Genomics 298 (3), 603-614 (2023)
   PUBMED   36906724
  REMARK    GeneRIF: Two novel compound heterozygous variants of the GCDH gene
            in two Chinese families with glutaric acidaemia type I identified
            by high-throughput sequencing and a literature review.
            Review article
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Schwartz,M., Christensen,E., Superti-Furga,A. and Brandt,N.J.
  TITLE     The human glutaryl-CoA dehydrogenase gene: report of intronic
            sequences and of 13 novel mutations causing glutaric aciduria type
            I
  JOURNAL   Hum Genet 102 (4), 452-458 (1998)
   PUBMED   9600243
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Biery,B.J., Stein,D.E., Morton,D.H. and Goodman,S.I.
  TITLE     Gene structure and mutations of glutaryl-coenzyme A dehydrogenase:
            impaired association of enzyme subunits that is due to an A421V
            substitution causes glutaric acidemia type I in the Amish
  JOURNAL   Am J Hum Genet 59 (5), 1006-1011 (1996)
   PUBMED   8900227
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Goodman,S.I., Kratz,L.E., DiGiulio,K.A., Biery,B.J., Goodman,K.E.,
            Isaya,G. and Frerman,F.E.
  TITLE     Cloning of glutaryl-CoA dehydrogenase cDNA, and expression of wild
            type and mutant enzymes in Escherichia coli
  JOURNAL   Hum Mol Genet 4 (9), 1493-1498 (1995)
   PUBMED   8541831
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Larson,A. and Goodman,S.
  TITLE     Glutaric Acidemia Type 1
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31536184
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Goodman,S.I., Kratz,L.E. and Frerman,F.E.
  TITLE     Pork and human cDNAs encoding glutaryl-CoA dehydrogenase
  JOURNAL   Prog Clin Biol Res 375, 169-173 (1992)
   PUBMED   1438360
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Lenich,A.C. and Goodman,S.I.
  TITLE     The purification and characterization of glutaryl-coenzyme A
            dehydrogenase from porcine and human liver
  JOURNAL   J Biol Chem 261 (9), 4090-4096 (1986)
   PUBMED   3081514
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290407.1, U69141.1 and
            BM855466.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the acyl-CoA
            dehydrogenase family. It catalyzes the oxidative decarboxylation of
            glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway
            of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses
            electron transfer flavoprotein as its electron acceptor. The enzyme
            exists in the mitochondrial matrix as a homotetramer of 45-kD
            subunits. Mutations in this gene result in the metabolic disorder
            glutaric aciduria type 1, which is also known as glutaric acidemia
            type I. Alternative splicing of this gene results in multiple
            transcript variants. A related pseudogene has been identified on
            chromosome 12. [provided by RefSeq, Mar 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform (a,
            also known as the long isoform).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KR674114.1, KT996148.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000222214.10/
                                                  ENSP00000222214.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..438
                     /product="glutaryl-CoA dehydrogenase, mitochondrial
                     isoform a precursor"
                     /EC_number="1.3.8.6"
                     /note="glutaryl-Coenzyme A dehydrogenase; glutaryl-CoA
                     dehydrogenase, mitochondrial"
                     /calculated_mol_wt=43467
     transit_peptide 1..44
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q92947.1)"
                     /calculated_mol_wt=4678
     mat_peptide     45..438
                     /product="Glutaryl-CoA dehydrogenase, mitochondrial.
                     /id=PRO_0000000526"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92947.1)"
                     /calculated_mol_wt=43467
     Region          48..434
                     /region_name="GCD"
                     /note="Glutaryl-CoA dehydrogenase; cd01151"
                     /db_xref="CDD:173840"
     Site            order(177,179..180,185..186,212,214,409,416,418)
                     /site_type="other"
                     /note="FAD binding site [chemical binding]"
                     /db_xref="CDD:173840"
     Site            order(186,283,290..291,294,413..414)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:173840"
     Site            240
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60759; propagated from
                     UniProtKB/Swiss-Prot (Q92947.1)"
     Site            414
                     /site_type="active"
                     /note="catalytic base [active]"
                     /db_xref="CDD:173840"
     CDS             1..438
                     /gene="GCDH"
                     /gene_synonym="ACAD5; GCD"
                     /coded_by="NM_000159.4:78..1394"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12286.1"
                     /db_xref="GeneID:2639"
                     /db_xref="HGNC:HGNC:4189"
                     /db_xref="MIM:608801"
ORIGIN      
        1 malrgvsvrl lsrgpglhvl rtwvssaaqt ekggrtqsql akssrpefdw qdplvleeql
       61 ttdeilirdt frtycqerlm prillanrne vfhreiisem gelgvlgpti kgygcagvss
      121 vaygllarel ervdsgyrsa msvqsslvmh piyaygseeq rqkylpqlak gellgcfglt
      181 epnsgsdpss metrahynss nksytlngtk twitnspmad lfvvwarced gcirgfllek
      241 gmrglsapri qgkfslrasa tgmiimdgve vpeenvlpga sslggpfgcl nnarygiawg
      301 vlgasefclh tarqyaldrm qfgvplarnq liqkkladml teitlglhac lqlgrlkdqd
      361 kaapemvsll krnncgkald iarqardmlg gngisdeyhv irhamnleav ntyegthdih
      421 alilgraitg iqaftask
//
LOCUS       NP_006299                150 aa            linear   PRI 27-APR-2025
DEFINITION  heat shock protein beta-3 [Homo sapiens].
ACCESSION   NP_006299
VERSION     NP_006299.1
DBSOURCE    REFSEQ: accession NM_006308.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Han,J.E., Kang,K.H., Kim,H., Hong,Y.B., Choi,B.O. and Koh,H.
  TITLE     PINK1 and Parkin rescue motor defects and mitochondria dysfunction
            induced by a patient-derived HSPB3 mutant in Drosophila models
  JOURNAL   Biochem Biophys Res Commun 682, 71-76 (2023)
   PUBMED   37804589
  REMARK    GeneRIF: PINK1 and Parkin rescue motor defects and mitochondria
            dysfunction induced by a patient-derived HSPB3 mutant in Drosophila
            models.
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Gianniou,D.D., Sklirou,A.D., Papadimitriou,M.A., Pilala,K.M.,
            Stravodimos,K., Avgeris,M., Scorilas,A. and Trougakos,I.P.
  TITLE     Evaluation of the Small Heat Shock Protein Family Members HSPB2 and
            HSPB3 in Bladder Cancer Prognosis and Progression
  JOURNAL   Int J Mol Sci 24 (3), 2609 (2023)
   PUBMED   36768927
  REMARK    GeneRIF: Evaluation of the Small Heat Shock Protein Family Members
            HSPB2 and HSPB3 in Bladder Cancer Prognosis and Progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Tiago,T., Hummel,B., Morelli,F.F., Basile,V., Vinet,J., Galli,V.,
            Mediani,L., Antoniani,F., Pomella,S., Cassandri,M., Garone,M.G.,
            Silvestri,B., Cimino,M., Cenacchi,G., Costa,R., Mouly,V., Poser,I.,
            Yeger-Lotem,E., Rosa,A., Alberti,S., Rota,R., Ben-Zvi,A.,
            Sawarkar,R. and Carra,S.
  TITLE     Small heat-shock protein HSPB3 promotes myogenesis by regulating
            the lamin B receptor
  JOURNAL   Cell Death Dis 12 (5), 452 (2021)
   PUBMED   33958580
  REMARK    GeneRIF: Small heat-shock protein HSPB3 promotes myogenesis by
            regulating the lamin B receptor.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Kalioraki,M.A., Artemaki,P.I., Sklirou,A.D., Kontos,C.K.,
            Adamopoulos,P.G., Papadopoulos,I.N., Trougakos,I.P. and Scorilas,A.
  TITLE     Heat shock protein beta 3 (HSPB3) is an unfavorable molecular
            biomarker in colorectal adenocarcinoma
  JOURNAL   Mol Carcinog 59 (1), 116-125 (2020)
   PUBMED   31709619
  REMARK    GeneRIF: High HSPB3 expression is associated with poor relapse-free
            survival (RFS) and overall survival (OS) of patients with
            colorectal adenocarcinoma.
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Kolb,S.J., Snyder,P.J., Poi,E.J., Renard,E.A., Bartlett,A., Gu,S.,
            Sutton,S., Arnold,W.D., Freimer,M.L., Lawson,V.H., Kissel,J.T. and
            Prior,T.W.
  TITLE     Mutant small heat shock protein B3 causes motor neuropathy: utility
            of a candidate gene approach
  JOURNAL   Neurology 74 (6), 502-506 (2010)
   PUBMED   20142617
  REMARK    GeneRIF: an HSPB3 mutation associated with an axonal motor
            neuropathy
REFERENCE   6  (residues 1 to 150)
  AUTHORS   Vos,M.J., Kanon,B. and Kampinga,H.H.
  TITLE     HSPB7 is a SC35 speckle resident small heat shock protein
  JOURNAL   Biochim Biophys Acta 1793 (8), 1343-1353 (2009)
   PUBMED   19464326
  REMARK    Erratum:[Biochim Biophys Acta. 2009 Dec;1793(12):1929-30]
REFERENCE   7  (residues 1 to 150)
  AUTHORS   Fontaine,J.M., Sun,X., Benndorf,R. and Welsh,M.J.
  TITLE     Interactions of HSP22 (HSPB8) with HSP20, alphaB-crystallin, and
            HSPB3
  JOURNAL   Biochem Biophys Res Commun 337 (3), 1006-1011 (2005)
   PUBMED   16225851
  REMARK    GeneRIF: Our results suggest that a variety of oligomers composed
            of different proportions of different sHSPs may form in cell types
            expressing multiple sHSPs.
REFERENCE   8  (residues 1 to 150)
  AUTHORS   Sugiyama,Y., Suzuki,A., Kishikawa,M., Akutsu,R., Hirose,T.,
            Waye,M.M., Tsui,S.K., Yoshida,S. and Ohno,S.
  TITLE     Muscle develops a specific form of small heat shock protein complex
            composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation
  JOURNAL   J Biol Chem 275 (2), 1095-1104 (2000)
   PUBMED   10625651
REFERENCE   9  (residues 1 to 150)
  AUTHORS   Boelens,W.C., Van Boekel,M.A. and De Jong,W.W.
  TITLE     HspB3, the most deviating of the six known human small heat shock
            proteins
  JOURNAL   Biochim Biophys Acta 1388 (2), 513-516 (1998)
   PUBMED   9858786
REFERENCE   10 (residues 1 to 150)
  AUTHORS   Lam,W.Y., Wing Tsui,S.K., Law,P.T., Luk,S.C., Fung,K.P., Lee,C.Y.
            and Waye,M.M.
  TITLE     Isolation and characterization of a human heart cDNA encoding a new
            member of the small heat shock protein family--HSPL27
  JOURNAL   Biochim Biophys Acta 1314 (1-2), 120-124 (1996)
   PUBMED   8972725
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U15590.1, BX106905.1 and
            N74672.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a muscle-specific small heat shock
            protein. A mutation in this gene is the cause of autosomal dominant
            distal hereditary motor neuropathy type 2C.[provided by RefSeq, Sep
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR5189655.146331.1, SRR5189655.40478.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302005.3/ ENSP00000303394.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q11.2"
     Protein         1..150
                     /product="heat shock protein beta-3"
                     /note="protein 3; HSP 17; heat shock 17 kDa protein; heat
                     shock 27kDa protein 3; heat shock protein family B member
                     3"
                     /calculated_mol_wt=16834
     Region          63..145
                     /region_name="ACD_HspB3_Like"
                     /note="Alpha crystallin domain (ACD) found in mammalian
                     HspB3, also known as heat-shock protein 27-like protein
                     (HSPL27, 17-kDa) and similar proteins. sHsps are molecular
                     chaperones that suppress protein aggregation and protect
                     against cell stress, and are...; cd06477"
                     /db_xref="CDD:107232"
     Site            order(63..67,74,76,78..79,116,137..138)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:107232"
     CDS             1..150
                     /gene="HSPB3"
                     /gene_synonym="DHMN2C; HMN2C; HMND4; HSPL27"
                     /coded_by="NM_006308.3:92..544"
                     /db_xref="CCDS:CCDS3961.1"
                     /db_xref="GeneID:8988"
                     /db_xref="HGNC:HGNC:5248"
                     /db_xref="MIM:604624"
ORIGIN      
        1 makiilrhli eipvryqeef eargledcrl dhalyalpgp tivdlrktra aqsppvdsaa
       61 etppregksh fqilldvvqf lpediiiqtf egwllikaqh gtrmdehgfi srsftrqykl
      121 pdgveikdls avlchdgilv vevkdpvgtk
//
LOCUS       NP_001347277             235 aa            linear   ROD 27-APR-2025
DEFINITION  max-interacting protein 1 isoform d [Mus musculus].
ACCESSION   NP_001347277 XP_017173568
VERSION     NP_001347277.1
DBSOURCE    REFSEQ: accession NM_001360348.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Li,X., Xiao,S., Li,F., Fang,K., Wen,J. and Gong,H.
  TITLE     Max interacting protein 1 induces IL-17-producing T
            helper/regulatory T imbalance in osteoarthritis by upregulating
            tectonic family member 2
  JOURNAL   Tissue Cell 78, 101906 (2022)
   PUBMED   36049372
  REMARK    GeneRIF: Max interacting protein 1 induces IL-17-producing T
            helper/regulatory T imbalance in osteoarthritis by upregulating
            tectonic family member 2.
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Menendez-Montes,I., Escobar,B., Palacios,B., Gomez,M.J.,
            Izquierdo-Garcia,J.L., Flores,L., Jimenez-Borreguero,L.J.,
            Aragones,J., Ruiz-Cabello,J., Torres,M. and Martin-Puig,S.
  TITLE     Myocardial VHL-HIF Signaling Controls an Embryonic Metabolic Switch
            Essential for Cardiac Maturation
  JOURNAL   Dev Cell 39 (6), 724-739 (2016)
   PUBMED   27997827
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Cui,W., Dai,X., Marcho,C., Han,Z., Zhang,K., Tremblay,K.D. and
            Mager,J.
  TITLE     Towards Functional Annotation of the Preimplantation Transcriptome:
            An RNAi Screen in Mammalian Embryos
  JOURNAL   Sci Rep 6, 37396 (2016)
   PUBMED   27869233
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Childress,P., Stayrook,K.R., Alvarez,M.B., Wang,Z., Shao,Y.,
            Hernandez-Buquer,S., Mack,J.K., Grese,Z.R., He,Y., Horan,D.,
            Pavalko,F.M., Warden,S.J., Robling,A.G., Yang,F.C., Allen,M.R.,
            Krishnan,V., Liu,Y. and Bidwell,J.P.
  TITLE     Genome-Wide Mapping and Interrogation of the Nmp4 Antianabolic Bone
            Axis
  JOURNAL   Mol Endocrinol 29 (9), 1269-1285 (2015)
   PUBMED   26244796
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Dugast-Darzacq,C., Pirity,M., Blanck,J.K., Scherl,A. and
            Schreiber-Agus,N.
  TITLE     Mxi1-SRalpha: a novel Mxi1 isoform with enhanced transcriptional
            repression potential
  JOURNAL   Oncogene 23 (55), 8887-8899 (2004)
   PUBMED   15467743
  REMARK    GeneRIF: Mxi1-SRalpha is an isoform with enhanced transcriptional
            repression potential
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Hurlin,P.J., Queva,C., Koskinen,P.J., Steingrimsson,E., Ayer,D.E.,
            Copeland,N.G., Jenkins,N.A. and Eisenman,R.N.
  TITLE     Mad3 and Mad4: novel Max-interacting transcriptional repressors
            that suppress c-myc dependent transformation and are expressed
            during neural and epidermal differentiation
  JOURNAL   EMBO J 14 (22), 5646-5659 (1995)
   PUBMED   8521822
  REMARK    Erratum:[EMBO J. 1996 Apr 15;15(8):2030. PMID: 8617250]
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Steingrimsson,E., Sawadogo,M., Gilbert,D.J., Zervos,A.S., Brent,R.,
            Blanar,M.A., Fisher,D.E., Copeland,N.G. and Jenkins,N.A.
  TITLE     Murine chromosomal location of five bHLH-Zip transcription factor
            genes
  JOURNAL   Genomics 28 (2), 179-183 (1995)
   PUBMED   8530024
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Schreiber-Agus,N., Chin,L., Chen,K., Torres,R., Rao,G., Guida,P.,
            Skoultchi,A.I. and DePinho,R.A.
  TITLE     An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic
            activity and interacts with a homolog of the yeast transcriptional
            repressor SIN3
  JOURNAL   Cell 80 (5), 777-786 (1995)
   PUBMED   7889571
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Shimizu,E., Shirasawa,H., Kodama,K., Koseki,K., Sato,T. and
            Simizu,B.
  TITLE     Cloning and sequencing of the murine Mxi1 cDNA
  JOURNAL   Gene 152 (2), 283-284 (1995)
   PUBMED   7835718
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Edelhoff,S., Ayer,D.E., Zervos,A.S., Steingrimsson,E.,
            Jenkins,N.A., Copeland,N.G., Eisenman,R.N., Brent,R. and
            Disteche,C.M.
  TITLE     Mapping of two genes encoding members of a distinct subfamily of
            MAX interacting proteins: MAD to human chromosome 2 and mouse
            chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome
            19
  JOURNAL   Oncogene 9 (2), 665-668 (1994)
   PUBMED   8290278
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC133451.14.
            
            On Feb 1, 2018 this sequence version replaced XP_017173568.1.
            
            Summary: This gene encodes a protein containing a helix-loop-helix
            domain characteristic of transcription factors, which allows
            heterodimerization and sequence-specific DNA binding. The encoded
            protein is related to a family of Myc/Max/Mad proteins that are
            involved in the regulation of several cellular processes. The
            protein encoded by this gene is a transcriptional repressor thought
            to negatively regulate Myc function. Three alternatively spliced
            transcripts encoding different isoforms have been described.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7) differs in the 5' UTR and 5'
            coding region, compared to variant 1. The resulting isoform (d) is
            longer and has a distinct N-terminus, compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.168105.1,
                                           SRR1660821.189511.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849377, SAMN00849378
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 47.53 cM"
     Protein         1..235
                     /product="max-interacting protein 1 isoform d"
                     /note="max-interacting protein 1"
                     /calculated_mol_wt=26478
     Region          75..154
                     /region_name="bHLHzip_MXI1"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in Max-interacting protein 1 (MXI1) and similar
                     proteins; cd18930"
                     /db_xref="CDD:381500"
     Site            order(79..80,83..84,86..87,91,110..112)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381500"
     Site            order(90..91,93..98,100..101,113,116,120,122..124,
                     126..127,129..130,133,137,140..141,143..144,147..148,
                     150..151)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381500"
     Site            order(90,93..94,96..97,100..101,113,116,120,122..124,
                     126..127,129..130,133,137,140..141,143..144,147..148,
                     150..151)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381500"
     CDS             1..235
                     /gene="Mxi1"
                     /gene_synonym="bHLHc11; Gm10197; Mad2"
                     /coded_by="NM_001360348.1:306..1013"
                     /note="isoform d is encoded by transcript variant 7"
                     /db_xref="GeneID:17859"
                     /db_xref="MGI:MGI:97245"
ORIGIN      
        1 mprplvpskk qargtrqrrq psldlrscar wecehgyass fpsmpsprlq hskpprrlsr
       61 aqkhssgssn tstanrsthn eleknrrahl rlclerlkvl iplgpdctrh ttlgllnkak
      121 ahikkleeae rksqhqlenl ereqrflkrr leqlqgpqem erirmdsigs tissdrsdse
      181 reeievdves tefshgeads vsttsisdld dhsslqsvgs degyssasvk lsfas
//
LOCUS       NP_001356038             317 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 13 [Homo
            sapiens].
ACCESSION   NP_001356038
VERSION     NP_001356038.1
DBSOURCE    REFSEQ: accession NM_001369109.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.37349.1,
                                           SRR1660805.54523.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..317
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 13"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=36746
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..316
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..317
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369109.1:209..1162"
                     /note="isoform 13 is encoded by transcript variant 30"
                     /db_xref="CCDS:CCDS91260.1"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefikl qelvdrvler fqasglivke wnsvklhatv
      241 mntlfrkdpn aegrynlyta egkyifkere sfdgrnilkl fenfyfgslk lnsihisqrf
      301 tvdsfgnyas cgqidfs
//
LOCUS       NP_001355231            1111 aa            linear   PRI 27-APR-2025
DEFINITION  general transcription factor II-I repeat domain-containing protein
            2B isoform 3 [Homo sapiens].
ACCESSION   NP_001355231
VERSION     NP_001355231.1
DBSOURCE    REFSEQ: accession NM_001368302.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Dougherty,M.L., Underwood,J.G., Nelson,B.J., Tseng,E., Munson,K.M.,
            Penn,O., Nowakowski,T.J., Pollen,A.A. and Eichler,E.E.
  TITLE     Transcriptional fates of human-specific segmental duplications in
            brain
  JOURNAL   Genome Res 28 (10), 1566-1576 (2018)
   PUBMED   30228200
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Gunbin,K.V. and Ruvinsky,A.
  TITLE     Evolution of general transcription factors
  JOURNAL   J Mol Evol 76 (1-2), 28-47 (2013)
   PUBMED   23229069
REFERENCE   4  (residues 1 to 1111)
  AUTHORS   Hinsley,T.A., Cunliffe,P., Tipney,H.J., Brass,A. and Tassabehji,M.
  TITLE     Comparison of TFII-I gene family members deleted in Williams-Beuren
            syndrome
  JOURNAL   Protein Sci 13 (10), 2588-2599 (2004)
   PUBMED   15388857
REFERENCE   5  (residues 1 to 1111)
  AUTHORS   Tipney,H.J., Hinsley,T.A., Brass,A., Metcalfe,K., Donnai,D. and
            Tassabehji,M.
  TITLE     Isolation and characterisation of GTF2IRD2, a novel fusion gene and
            member of the TFII-I family of transcription factors, deleted in
            Williams-Beuren syndrome
  JOURNAL   Eur J Hum Genet 12 (7), 551-560 (2004)
   PUBMED   15100712
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from MH721920.1 and BX647624.1.
            
            Summary: This gene encodes a glycosylated phosphoprotein with a
            leucine zipper motif, two helix-loop-helix motifs (I repeats) that
            are similar to domains found in the TFII-I family of transcription
            factors, one CHARLIE8 transposable element-like sequence, and a BED
            zinc finger. This gene lies within a region that is deleted in
            Williams-Beuren syndrome. Alternatively spliced variants which
            encode different protein isoforms have been described; however, not
            all variants have been fully characterized. [provided by RefSeq,
            Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: MH721920.1, SRR7410570.416259.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..1111
                     /product="general transcription factor II-I repeat
                     domain-containing protein 2B isoform 3"
                     /note="general transcription factor II-I repeat
                     domain-containing protein 2B; general transcription factor
                     2 I repeat domain-containing 2 beta; GTF2IRD2 beta;
                     transcription factor GTF2IRD2-beta; GTF2I repeat
                     domain-containing protein 2B; General transcription factor
                     II-I repeat domain-containing protein 2A; GTF2I repeat
                     domain-containing protein 2A; Transcription factor
                     GTF2IRD2-alpha"
                     /calculated_mol_wt=125878
     Region          17..70
                     /region_name="CENP-B_N"
                     /note="CENP-B N-terminal DNA-binding domain; pfam04218"
                     /db_xref="CDD:461229"
     Region          91..156
                     /region_name="HTH_Tnp_Tc5"
                     /note="Tc5 transposase DNA-binding domain; pfam03221"
                     /db_xref="CDD:460850"
     Region          269..343
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          494..568
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          591..653
                     /region_name="DUF4371"
                     /note="Domain of unknown function (DUF4371); cl46273"
                     /db_xref="CDD:480613"
     Region          <709..792
                     /region_name="DUF4371"
                     /note="Domain of unknown function (DUF4371); cl46273"
                     /db_xref="CDD:480613"
     CDS             1..1111
                     /gene="GTF2IRD2B"
                     /gene_synonym="GTF2IRD2; GTF2IRD2A"
                     /coded_by="NM_001368302.1:518..3853"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:389524"
                     /db_xref="HGNC:HGNC:33125"
                     /db_xref="MIM:608900"
ORIGIN      
        1 mapkhkssda gnldrpkrsr kvlplsekvk vldlirkdkk syaevakiyg knessireiv
       61 kkekeirasf avspptakvt atvrdkclvk meqalhlwve emnrkrvpid snmlrqkals
      121 lyqdfckgcs etdtkpftas kgwlhrfrhr fshhykkkkk gimaqvavst lpveeessse
      181 trmvvtflvs alesmckela kskaevacia vyetdvfvvg tergcafvna rtdfqkdfak
      241 ycvaeglcev kppcpvngmq vhsgeteilr kavedyfcfc ygkalgttvm vpvpyekmlr
      301 dqsavvvqgl pegvafqhpe nydlatlkwi lenkagisfi inrpflgpes qlggpgmvtd
      361 aersivspse scgpinvkte pmedsgislk aeavsvkkes edpnyyqynm qgshpsstsn
      421 eviemelpme dstplvpsee pnedpeaevk iegntnsssv tnsaagvedl nivqvtvpdn
      481 ekerlssiek ikqlreqvnd lfsrkfgeai gvdfpvkvpy rkitfnpgcv vidgmppgvv
      541 fkapgyleis smrrileaae fikftvirpl pglelsnvgk rkidqegrvf qekwerayff
      601 vevqniptcl ickqsmsvsk eynlrrhyqt nhskhydqyt ermrdeklhe lkkglrkyll
      661 gssdtecpeq kqvfanpspt qkspvqpved lagnlweklr ekirsfvays iaideitdin
      721 nttqlaifir gvdenfdvse elldtvpmtg tksgneiflr vekslkkfci nwsrlvsvas
      781 tgtpamvdan nglvtklksr vatfckgael ksicciihpe slcaqklkmd hvmdvvvksv
      841 nwicsrglnh sefttllyel dsqygsllyy teikwlsrgl vlkrffesle eidsfmssrg
      901 kplpqlssid wirdlaflvd mtmhlnalni slqghsqivt qmydlirafl aklclwethl
      961 trnnlahfpt lklvsrnesd glnyipkiae lktefqkrls dfklyeselt lfsspfstki
     1021 dsvheelqme vidlqcntvl ktkydkvgip efykylwgsy pkykhhcaki lsmfgstyic
     1081 eqlfsimkls ktkycsqlkd sqwdsvlhia t
//
LOCUS       NP_064547                707 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DHX33 isoform 1 [Homo sapiens].
ACCESSION   NP_064547
VERSION     NP_064547.2
DBSOURCE    REFSEQ: accession NM_020162.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Wang,X., Chen,S., Wen,F., Zeng,Y. and Zhang,Y.
  TITLE     RNA helicase DHX33 regulates HMGB family genes in human cancer
            cells
  JOURNAL   Cell Signal 110, 110832 (2023)
   PUBMED   37543097
  REMARK    GeneRIF: RNA helicase DHX33 regulates HMGB family genes in human
            cancer cells.
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Ding,J., Zhou,J., Shen,X., Zhang,M., Feng,X. and Xu,Z.
  TITLE     Systematic analysis of the prognostic and immunological role of
            DHX33 in pan-cancer
  JOURNAL   Environ Toxicol 38 (8), 2011-2021 (2023)
   PUBMED   37256545
  REMARK    GeneRIF: Systematic analysis of the prognostic and immunological
            role of DHX33 in pan-cancer.
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Zhang,X., Shao,Y., Zhou,Y., Zhu,Z. and Wang,X.
  TITLE     Comprehensive analysis of immune implication and prognostic value
            of DHX33 in sarcoma
  JOURNAL   Medicine (Baltimore) 102 (17), e33654 (2023)
   PUBMED   37115050
  REMARK    GeneRIF: Comprehensive analysis of immune implication and
            prognostic value of DHX33 in sarcoma.
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Zhang,Y., Chen,S. and Peng,C.
  TITLE     GSK-3beta phosphorylation of DHX33 leads to its ubiquitination
            mediated protein degradation
  JOURNAL   Cell Signal 101, 110526 (2023)
   PUBMED   36403931
  REMARK    GeneRIF: GSK-3beta phosphorylation of DHX33 leads to its
            ubiquitination mediated protein degradation.
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Zhang,Y., Forys,J.T., Miceli,A.P., Gwinn,A.S. and Weber,J.D.
  TITLE     Identification of DHX33 as a mediator of rRNA synthesis and cell
            growth
  JOURNAL   Mol Cell Biol 31 (23), 4676-4691 (2011)
   PUBMED   21930779
  REMARK    GeneRIF: we show the mechanistic importance of DHX33 in rRNA
            transcription and proliferation
REFERENCE   7  (residues 1 to 707)
  AUTHORS   Rajaraman,P., Brenner,A.V., Neta,G., Pfeiffer,R., Wang,S.S.,
            Yeager,M., Thomas,G., Fine,H.A., Linet,M.S., Rothman,N.,
            Chanock,S.J. and Inskip,P.D.
  TITLE     Risk of meningioma and common variation in genes related to innate
            immunity
  JOURNAL   Cancer Epidemiol Biomarkers Prev 19 (5), 1356-1361 (2010)
   PUBMED   20406964
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 707)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   9  (residues 1 to 707)
  AUTHORS   Rajaraman,P., Brenner,A.V., Butler,M.A., Wang,S.S., Pfeiffer,R.M.,
            Ruder,A.M., Linet,M.S., Yeager,M., Wang,Z., Orr,N., Fine,H.A.,
            Kwon,D., Thomas,G., Rothman,N., Inskip,P.D. and Chanock,S.J.
  TITLE     Common variation in genes related to innate immunity and risk of
            adult glioma
  JOURNAL   Cancer Epidemiol Biomarkers Prev 18 (5), 1651-1658 (2009)
   PUBMED   19423540
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 707)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK295760.1, AC004148.1 and
            BQ775963.1.
            
            On Apr 28, 2002 this sequence version replaced NP_064547.1.
            
            Summary: This gene encodes a member of the DEAD box protein family.
            The DEAD box proteins are characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this DEAD box
            protein family are believed to be involved in embryogenesis,
            spermatogenesis, and cellular growth and division. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK025625.1, SRR1803612.231335.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000225296.8/ ENSP00000225296.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..707
                     /product="ATP-dependent RNA helicase DHX33 isoform 1"
                     /EC_number="3.6.4.13"
                     /note="DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 33;
                     putative ATP-dependent RNA helicase DHX33; DEAH box
                     protein 33; DEAH (Asp-Glu-Ala-His) box polypeptide 33"
                     /calculated_mol_wt=78743
     Region          1..80
                     /region_name="Required for nucleolar location.
                     /evidence=ECO:0000269|PubMed:26100019"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6R0.2)"
     Region          1..64
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6R0.2)"
     Region          73..>700
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
     Region          194..197
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6R0.2)"
     Region          471..562
                     /region_name="HA2, required for interaction with EIF3G and
                     RPL26. /evidence=ECO:0000269|PubMed:26100019"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6R0.2)"
     Region          547..558
                     /region_name="Critical for rDNA-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6R0.2)"
     CDS             1..707
                     /gene="DHX33"
                     /gene_synonym="DDX33"
                     /coded_by="NM_020162.4:124..2247"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11072.1"
                     /db_xref="GeneID:56919"
                     /db_xref="HGNC:HGNC:16718"
                     /db_xref="MIM:614405"
ORIGIN      
        1 mpeeagfppa krfrpgsgpp sragsfppgr qvvmlltags ggrgggggrr qqpplaqpsa
       61 spypeavelq rrslpifqar gqllaqlrnl dnavligetg sgkttqipqy lyeggisrqg
      121 iiavtqprrv aaislatrvs dekrtelgkl vgytvrfddv tsedtrikfl tdgmllreai
      181 sdsllrkysc vildeahert ihtdvlfgvv kaaqkrrkel gklplkvivm satmdvdlfs
      241 qyfngapvly legrqhpiqv fytkqpqndy lhaalvsvfq ihqeapssqd ilvfltgqee
      301 ieamsktcrd iakhlpdgcp amlvlplyas lpyaqqlrvf qgapkgyrkv iistniaets
      361 ititgikyvv dtgmvkakky npdsglevla vqrvsktqaw qrtgragred sgicyrlyte
      421 defekfdkmt vpeiqrcnla svmlqllamk vpnvltfdfm skpspdhiqa aiaqldllga
      481 lehkddqltl tpmgrkmaaf plepkfakti lmspkfhcte eiltivslls vdsvlhnpps
      541 rreevqgvrk kfissegdhm tllniyrtfk nlggnkdwck enfvnsknmt lvaevraqlr
      601 diclkmsmpi assrgdvesv rrclahslfm staelqpdgt yattdthqpv aihpssvlfh
      661 ckpacvvyte llytnkcymr dlcvidaqwl yeaapeyfrr klrtarn
//
LOCUS       NP_000112                508 aa            linear   PRI 27-APR-2025
DEFINITION  erythropoietin receptor precursor [Homo sapiens].
ACCESSION   NP_000112
VERSION     NP_000112.1
DBSOURCE    REFSEQ: accession NM_000121.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Zakaria,M.F., Sonoda,S., Kato,H., Ma,L., Uehara,N.,
            Kyumoto-Nakamura,Y., Sharifa,M.M., Yu,L., Dai,L.,
            Yamauchi-Tomoda,E., Aijima,R., Yamaza,H., Nishimura,F. and
            Yamaza,T.
  TITLE     Erythropoietin receptor signal is crucial for periodontal ligament
            stem cell-based tissue reconstruction in periodontal disease
  JOURNAL   Sci Rep 14 (1), 6719 (2024)
   PUBMED   38509204
  REMARK    GeneRIF: Erythropoietin receptor signal is crucial for periodontal
            ligament stem cell-based tissue reconstruction in periodontal
            disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Han,Y., Gao,C., Liu,Y., Zhang,H., Wang,S., Zhao,H., Bao,W., Guo,X.,
            Vinchi,F., Lobo,C., Shi,P., Mendelson,A., Luchsinger,L., Zhong,H.,
            Yazdanbakhsh,K. and An,X.
  TITLE     Hemolysis-driven IFNalpha production impairs erythropoiesis by
            negatively regulating EPO signaling in sickle cell disease
  JOURNAL   Blood 143 (11), 1018-1031 (2024)
   PUBMED   38127913
  REMARK    GeneRIF: Hemolysis-driven IFNalpha production impairs
            erythropoiesis by negatively regulating EPO signaling in sickle
            cell disease.
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Zhang,Y., Zhu,Y., Wang,S., Feng,Y.C. and Li,H.
  TITLE     Erythropoietin receptor is a risk factor for prognosis: A potential
            biomarker in lung adenocarcinoma
  JOURNAL   Pathol Res Pract 251, 154891 (2023)
   PUBMED   37844485
  REMARK    GeneRIF: Erythropoietin receptor is a risk factor for prognosis: A
            potential biomarker in lung adenocarcinoma.
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Prchal,J.
  TITLE     Primary Familial and Congenital Erythrocytosis
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27831681
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Nakamura,Y., Komatsu,N. and Nakauchi,H.
  TITLE     A truncated erythropoietin receptor that fails to prevent
            programmed cell death of erythroid cells
  JOURNAL   Science 257 (5073), 1138-1141 (1992)
   PUBMED   1324524
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Yoshimura,A. and Lodish,H.F.
  TITLE     In vitro phosphorylation of the erythropoietin receptor and an
            associated protein, pp130
  JOURNAL   Mol Cell Biol 12 (2), 706-715 (1992)
   PUBMED   1310150
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Penny,L.A. and Forget,B.G.
  TITLE     Genomic organization of the human erythropoietin receptor gene
  JOURNAL   Genomics 11 (4), 974-980 (1991)
   PUBMED   1664413
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Maouche,L., Tournamille,C., Hattab,C., Boffa,G., Cartron,J.P. and
            Chretien,S.
  TITLE     Cloning of the gene encoding the human erythropoietin receptor
  JOURNAL   Blood 78 (10), 2557-2563 (1991)
   PUBMED   1668607
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Ehrenman,K. and St John,T.
  TITLE     The erythropoietin receptor gene: cloning and identification of
            multiple transcripts in an erythroid cell line OCIM1
  JOURNAL   Exp Hematol 19 (9), 973-977 (1991)
   PUBMED   1654273
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Jones,S.S., D'Andrea,A.D., Haines,L.L. and Wong,G.G.
  TITLE     Human erythropoietin receptor: cloning, expression, and biologic
            characterization
  JOURNAL   Blood 76 (1), 31-35 (1990)
   PUBMED   2163696
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC019092.2, M60459.1,
            AC024575.6 and BU619338.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the erythropoietin receptor which is a
            member of the cytokine receptor family. Upon erythropoietin
            binding, this receptor activates Jak2 tyrosine kinase which
            activates different intracellular pathways including: Ras/MAP
            kinase, phosphatidylinositol 3-kinase and STAT transcription
            factors. The stimulated erythropoietin receptor appears to have a
            role in erythroid cell survival. Defects in the erythropoietin
            receptor may produce erythroleukemia and familial erythrocytosis.
            Dysregulation of this gene may affect the growth of certain tumors.
            Alternate splicing results in multiple transcript
            variants.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) encodes the functional
            protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M60459.1, BC112153.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222139.11/ ENSP00000222139.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..508
                     /product="erythropoietin receptor precursor"
                     /calculated_mol_wt=52574
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
                     /calculated_mol_wt=2510
     mat_peptide     25..508
                     /product="Erythropoietin receptor. /id=PRO_0000010868"
                     /note="propagated from UniProtKB/Swiss-Prot (P19235.1)"
                     /calculated_mol_wt=52574
     Region          37..140
                     /region_name="EpoR_lig-bind"
                     /note="Erythropoietin receptor, ligand binding; pfam09067"
                     /db_xref="CDD:401127"
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
     Site            117
                     /site_type="other"
                     /note="Required for ligand binding.
                     /evidence=ECO:0000269|PubMed:8662939; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
     Region          146..244
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Region          233..237
                     /region_name="WSXWS motif.
                     /evidence=ECO:0000269|PubMed:9774108"
                     /note="propagated from UniProtKB/Swiss-Prot (P19235.1)"
     Site            order(233..234,236..237)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            251..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19235.1)"
     Region          282..290
                     /region_name="Box 1 motif.
                     /evidence=ECO:0000250|UniProtKB:P16310"
                     /note="propagated from UniProtKB/Swiss-Prot (P19235.1)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:11781573; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
     Region          452..457
                     /region_name="ITIM motif.
                     /evidence=ECO:0000250|UniProtKB:P14753"
                     /note="propagated from UniProtKB/Swiss-Prot (P19235.1)"
     Region          454..456
                     /region_name="Required for high-affinity SOCS3 binding.
                     /evidence=ECO:0000269|PubMed:12027890"
                     /note="propagated from UniProtKB/Swiss-Prot (P19235.1)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
     Region          467..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19235.1)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (P19235.1)"
     CDS             1..508
                     /gene="EPOR"
                     /gene_synonym="EPO-R"
                     /coded_by="NM_000121.4:108..1634"
                     /db_xref="CCDS:CCDS12260.1"
                     /db_xref="GeneID:2057"
                     /db_xref="HGNC:HGNC:3416"
                     /db_xref="MIM:133171"
ORIGIN      
        1 mdhlgaslwp qvgslcllla gaawapppnl pdpkfeskaa llaargpeel lcfterledl
       61 vcfweeaasa gvgpgnysfs yqledepwkl crlhqaptar gavrfwcslp tadtssfvpl
      121 elrvtaasga pryhrvihin evvlldapvg lvarladesg hvvlrwlppp etpmtshiry
      181 evdvsagnga gsvqrveile grtecvlsnl rgrtrytfav rarmaepsfg gfwsawsepv
      241 slltpsdldp liltlslilv vilvlltvla llshrralkq kiwpgipspe sefeglftth
      301 kgnfqlwlyq ndgclwwspc tpftedppas levlsercwg tmqavepgtd degpllepvg
      361 sehaqdtylv ldkwllprnp psedlpgpgg svdivamdeg seasscssal askpspegas
      421 aasfeytild pssqllrpwt lcpelpptpp hlkylylvvs dsgistdyss gdsqgaqggl
      481 sdgpysnpye nslipaaepl ppsyvacs
//
LOCUS       NP_001353653            1102 aa            linear   PRI 27-APR-2025
DEFINITION  glutamate receptor-interacting protein 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001353653 XP_016874590
VERSION     NP_001353653.1
DBSOURCE    REFSEQ: accession NM_001366724.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Koprulu,M., Kumare,A., Bibi,A., Malik,S. and Tolun,A.
  TITLE     The first adolescent case of Fraser syndrome 3, with a novel
            nonsense variant in GRIP1
  JOURNAL   Am J Med Genet A 185 (6), 1858-1863 (2021)
   PUBMED   33709629
REFERENCE   4  (residues 1 to 1102)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1102)
  AUTHORS   Twelvetrees,A.E., Lesept,F., Holzbaur,E.L.F. and Kittler,J.T.
  TITLE     The adaptor proteins HAP1a and GRIP1 collaborate to activate the
            kinesin-1 isoform KIF5C
  JOURNAL   J Cell Sci 132 (24) (2019)
   PUBMED   31757889
  REMARK    GeneRIF: The adaptor proteins HAP1a and GRIP1 collaborate to
            activate the kinesin-1 isoform KIF5C.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1102)
  AUTHORS   Lu,W. and Ziff,E.B.
  TITLE     PICK1 interacts with ABP/GRIP to regulate AMPA receptor trafficking
  JOURNAL   Neuron 47 (3), 407-421 (2005)
   PUBMED   16055064
REFERENCE   7  (residues 1 to 1102)
  AUTHORS   Charych,E.I., Yu,W., Li,R., Serwanski,D.R., Miralles,C.P., Li,X.,
            Yang,B.Y., Pinal,N., Walikonis,R. and De Blas,A.L.
  TITLE     A four PDZ domain-containing splice variant form of GRIP1 is
            localized in GABAergic and glutamatergic synapses in the brain
  JOURNAL   J Biol Chem 279 (37), 38978-38990 (2004)
   PUBMED   15226318
  REMARK    GeneRIF: GRIP1c 4-7 plays a role not only in glutamatergic synapses
            but also in GABAergic synapses
REFERENCE   8  (residues 1 to 1102)
  AUTHORS   Braithwaite,S.P., Xia,H. and Malenka,R.C.
  TITLE     Differential roles for NSF and GRIP/ABP in AMPA receptor cycling
  JOURNAL   Proc Natl Acad Sci U S A 99 (10), 7096-7101 (2002)
   PUBMED   12011465
  REMARK    GeneRIF: after regulated endocytosis, binding to GRIP/ABP
            stabilizes the internalized receptors in an intracellular pool and
            prevents them from being recycled back to the plasma membrane or
            entering a degradative pathway.
REFERENCE   9  (residues 1 to 1102)
  AUTHORS   Lin,S.H., Arai,A.C., Wang,Z., Nothacker,H.P. and Civelli,O.
  TITLE     The carboxyl terminus of the prolactin-releasing peptide receptor
            interacts with PDZ domain proteins involved in
            alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor
            clustering
  JOURNAL   Mol Pharmacol 60 (5), 916-923 (2001)
   PUBMED   11641419
REFERENCE   10 (residues 1 to 1102)
  AUTHORS   Bruckner,K., Pablo Labrador,J., Scheiffele,P., Herb,A.,
            Seeburg,P.H. and Klein,R.
  TITLE     EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft
            membrane microdomains
  JOURNAL   Neuron 22 (3), 511-524 (1999)
   PUBMED   10197531
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078888.22, AC090710.16,
            AC135251.2 and AC078889.20.
            
            On Oct 17, 2018 this sequence version replaced XP_016874590.1.
            
            Summary: This gene encodes a member of the glutamate receptor
            interacting protein family. The encoded scaffold protein binds to
            and mediates the trafficking and membrane organization of a number
            of transmembrane proteins. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, May 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.3"
     Protein         1..1102
                     /product="glutamate receptor-interacting protein 1 isoform
                     5"
                     /calculated_mol_wt=119678
     Region          78..160
                     /region_name="PDZ1_GRIP1-2-like"
                     /note="PDZ domain 1 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06687"
                     /db_xref="CDD:467175"
     Site            order(89..95,107,110,140,144,147..148)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467175"
     Region          175..263
                     /region_name="PDZ2_GRIP1-2-like"
                     /note="PDZ domain 2 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06681"
                     /db_xref="CDD:467169"
     Site            order(187..193,209,212,242,246,249..250)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467169"
     Region          275..360
                     /region_name="PDZ3_GRIP1-2-like"
                     /note="PDZ domain 3 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06684"
                     /db_xref="CDD:467172"
     Site            order(288..294,307,310,340,344,347..348)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467172"
     Region          438..538
                     /region_name="PDZ4_GRIP1-2-like"
                     /note="PDZ domain 4 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06686"
                     /db_xref="CDD:467174"
     Site            order(443..446,487..488,490..492,531,533..538)
                     /site_type="other"
                     /note="PDZ5 interface [polypeptide binding]"
                     /db_xref="CDD:467174"
     Site            order(456..462,478,481,511,515,518..519)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467174"
     Region          546..630
                     /region_name="PDZ5_GRIP1-2-like"
                     /note="PDZ domain 5 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06682"
                     /db_xref="CDD:467170"
     Site            order(557..563,577,580,610,614,617..618)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467170"
     Region          643..727
                     /region_name="PDZ6_GRIP1-2-like"
                     /note="PDZ domain 6 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06683"
                     /db_xref="CDD:467171"
     Site            order(656..662,674,677,707,711,714..715)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467171"
     Region          974..1058
                     /region_name="PDZ7_GRIP1-2-like"
                     /note="PDZ domain 7 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06685"
                     /db_xref="CDD:467173"
     Site            order(989..995,1006,1009,1038,1042,1045..1046)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467173"
     Site            order(1028,1031,1036,1039..1040,1043..1044)
                     /site_type="other"
                     /note="GRASP-1 binding site [polypeptide binding]"
                     /db_xref="CDD:467173"
     CDS             1..1102
                     /gene="GRIP1"
                     /gene_synonym="FRASRS3; GRIP"
                     /coded_by="NM_001366724.1:85..3393"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:23426"
                     /db_xref="HGNC:HGNC:18708"
                     /db_xref="MIM:604597"
ORIGIN      
        1 mdrflgfvka irrsrrrkgk kyrpeedyhe gyedvyyyas ehfrnespyt ksasqtkppd
       61 galavrrqsi peefkgstvv elmkkegttl gltvsggidk dgkprvsnlr qggiaarsdq
      121 ldvgdyikav nginlakfrh deiisllknv gervvlevey elppvsvqgs svifrtvevt
      181 lhkegntfgf virggahddr nksrpvvitc vrpggpadre gtikpgdrll svdgirllgt
      241 thaeamsilk qcgqeaalli eydvsvmdsv atasgpllve vaktpgaslg valttsmccn
      301 kqvividkik sasiadrcga lhvgdhilsi dgtsmeyctl aeatqflant tdqvkleilp
      361 hhqtrlalkg pdhaalvsss fsptsmsays lsslnmgtlp rslystsprg tmmrrrlkkk
      421 dfksslslas stvglagqvv htettevvlt adpvtgfgiq lqgsvfatet lsspplisyi
      481 eadspaercg vlqigdrvma ingiptedst feeasqllrd ssitskvtle iefdvaesvi
      541 pssgtfhvkl pkkhnvelgi tisspssrkp gdplvisdik kgsvahrtgt lelgdkllai
      601 dnirldncsm edavqilqqc edlvklkirk dednsdeqes sgaiiytvel kryggplgit
      661 isgteepfdp iiissltkgg laertgaihi gdrilainss slkgkplsea ihllqmaget
      721 vtlkikkqtd aqsasspkkf pisshlsdlg dveedsspaq kpgklsdmyp stvpsvdsav
      781 dswdgsaidt sygtqgtsfq asgynfntyd wrspkqrgsl spvtkprsqt ypdvglsyed
      841 wdrstasgfa gaadsaeteq eenfwsqale dletcgqsgi lreleekadr rvslrnmtll
      901 atimsgstms lnheaptprs qlgrqasfqe rsssrphysq ttrsntlpsd vgrksvtlrk
      961 mkqeikeims ptpvelhkvt lykdsdmedf gfsvadglle kgvyvknirp agpgdlgglk
     1021 pydrllqvnh vrtrdfdccl vvpliaesgn kldlvisrnp lasqksidqq slpgdwseqn
     1081 saffqqpshg gnletreptn tl
//
LOCUS       NP_003052               1534 aa            linear   PRI 27-APR-2025
DEFINITION  slit homolog 1 protein precursor [Homo sapiens].
ACCESSION   NP_003052
VERSION     NP_003052.2
DBSOURCE    REFSEQ: accession NM_003061.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1534)
  AUTHORS   Zheng,Y., Xiao,M., Zhang,J. and Chang,F.
  TITLE     Micro RNA-640 Targeting SLIT1 Enhances Glioma Radiosensitivity by
            Restraining the Activation of Wnt/beta-Catenin Signaling Pathway
  JOURNAL   Br J Biomed Sci 79, 10067 (2022)
   PUBMED   35996510
  REMARK    GeneRIF: Micro RNA-640 Targeting SLIT1 Enhances Glioma
            Radiosensitivity by Restraining the Activation of Wnt/beta-Catenin
            Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1534)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1534)
  AUTHORS   Hosokawa,K., Mizumaki,H., Elbadry,M.I., Saito,C., Espinoza,J.L.,
            Thi Thanh Dao,A., Katagiri,T., Harashima,A., Kikuchi,A., Kanai,A.,
            Matsui,H., Inaba,T., Taniwaki,M., Yamamoto,Y. and Nakao,S.
  TITLE     Clonal hematopoiesis by SLIT1-mutated hematopoietic stem cells due
            to a breakdown of the autocrine loop involving Slit1 in acquired
            aplastic anemia
  JOURNAL   Leukemia 33 (11), 2732-2766 (2019)
   PUBMED   31186493
  REMARK    GeneRIF: SLIT1-mutated hematopoietic stem cells have a role in
            clonal hematopoiesis in acquired aplastic anemia
REFERENCE   4  (residues 1 to 1534)
  AUTHORS   Shuai,W., Wu,J., Chen,S., Liu,R., Ye,Z., Kuang,C., Fu,X., Wang,G.,
            Li,Y., Peng,Q., Shi,W., Li,Y., Zhou,Q. and Huang,W.
  TITLE     SUV39H2 promotes colorectal cancer proliferation and metastasis via
            tri-methylation of the SLIT1 promoter
  JOURNAL   Cancer Lett 422, 56-69 (2018)
   PUBMED   29458143
  REMARK    GeneRIF: Findings show that SLIT1 is a direct target of SUV39H2
            which binds to its promoter and catalyzes H3K9 tri-methylation to
            silence SLIT1 expression.
REFERENCE   5  (residues 1 to 1534)
  AUTHORS   Simino,J., Sung,Y.J., Kume,R., Schwander,K. and Rao,D.C.
  TITLE     Gene-alcohol interactions identify several novel blood pressure
            loci including a promising locus near SLC16A9
  JOURNAL   Front Genet 4, 277 (2013)
   PUBMED   24376456
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1534)
  AUTHORS   Yuan,W., Zhou,L., Chen,J.H., Wu,J.Y., Rao,Y. and Ornitz,D.M.
  TITLE     The mouse SLIT family: secreted ligands for ROBO expressed in
            patterns that suggest a role in morphogenesis and axon guidance
  JOURNAL   Dev Biol 212 (2), 290-306 (1999)
   PUBMED   10433822
REFERENCE   7  (residues 1 to 1534)
  AUTHORS   Wu,W., Wong,K., Chen,J., Jiang,Z., Dupuis,S., Wu,J.Y. and Rao,Y.
  TITLE     Directional guidance of neuronal migration in the olfactory system
            by the protein Slit
  JOURNAL   Nature 400 (6742), 331-336 (1999)
   PUBMED   10432110
REFERENCE   8  (residues 1 to 1534)
  AUTHORS   Liang,Y., Annan,R.S., Carr,S.A., Popp,S., Mevissen,M.,
            Margolis,R.K. and Margolis,R.U.
  TITLE     Mammalian homologues of the Drosophila slit protein are ligands of
            the heparan sulfate proteoglycan glypican-1 in brain
  JOURNAL   J Biol Chem 274 (25), 17885-17892 (1999)
   PUBMED   10364234
REFERENCE   9  (residues 1 to 1534)
  AUTHORS   Itoh,A., Miyabayashi,T., Ohno,M. and Sakano,S.
  TITLE     Cloning and expressions of three mammalian homologues of Drosophila
            slit suggest possible roles for Slit in the formation and
            maintenance of the nervous system
  JOURNAL   Brain Res Mol Brain Res 62 (2), 175-186 (1998)
   PUBMED   9813312
REFERENCE   10 (residues 1 to 1534)
  AUTHORS   Nakayama,M., Nakajima,D., Nagase,T., Nomura,N., Seki,N. and
            Ohara,O.
  TITLE     Identification of high-molecular-weight proteins with multiple
            EGF-like motifs by motif-trap screening
  JOURNAL   Genomics 51 (1), 27-34 (1998)
   PUBMED   9693030
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL512424.14, BC146761.1, BC028105.1 and CD671648.1.
            
            On May 17, 2008 this sequence version replaced NP_003052.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC146761.1, AB017167.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000266058.9/ ENSP00000266058.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.1"
     Protein         1..1534
                     /product="slit homolog 1 protein precursor"
                     /note="multiple EGF-like domains protein 4; multiple
                     epidermal growth factor-like domains protein 4; slit
                     homolog 1; multiple EGF like domains 4"
                     /calculated_mol_wt=164452
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3493
     Region          <28..>217
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     mat_peptide     34..1534
                     /product="Slit homolog 1 protein. /id=PRO_0000007722"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
                     /calculated_mol_wt=164452
     Region          43..62
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..83
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          63..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Region          86..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          87..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          110..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          111..134
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          134..155
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          135..158
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          158..179
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          159..182
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          182..203
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          183..206
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          188..>328
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Region          207..334
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          310..331
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          312..369
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          334..355
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          335..358
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          358..379
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          359..379
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          382..403
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          383..406
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          389..441
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          406..427
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Region          407..428
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          412..>475
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          431..528
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          522..>820
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          529..566
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          541..562
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          566..587
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          567..590
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            571
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Region          590..611
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          591..614
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          614..635
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          615..638
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            630
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Region          638..659
                     /region_name="LRR 16"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          639..660
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          644..>730
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          663..762
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          733..760
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; pfam01462"
                     /db_xref="CDD:396168"
     Region          762..783
                     /region_name="LRR 17"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Site            762
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Region          763..785
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          785..806
                     /region_name="LRR 18"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          786..809
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            801
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Site            806
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Region          809..830
                     /region_name="LRR 19"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          810..830
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          833..854
                     /region_name="LRR 20"
                     /note="propagated from UniProtKB/Swiss-Prot (O75093.4)"
     Region          834..857
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          842..>1002
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          1005..1041
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1005,1008,1022)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1026
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Region          1044..1080
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            1079
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Region          1085..1119
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          <1136..1163
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1189..1322
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Site            1189
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Site            1259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     Site            1306
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75093.4)"
     CDS             1..1534
                     /gene="SLIT1"
                     /gene_synonym="MEGF4; SLIL1; SLIT-1; SLIT3"
                     /coded_by="NM_003061.3:286..4890"
                     /db_xref="CCDS:CCDS7453.1"
                     /db_xref="GeneID:6585"
                     /db_xref="HGNC:HGNC:11085"
                     /db_xref="MIM:603742"
ORIGIN      
        1 maltpgwgss agpvrpelwl llwaaawrlg asacpalctc tgttvdchgt glqaipknip
       61 rnterlelng nnitrihknd faglkqlrvl qlmenqigav ergafddmke lerlrlnrnq
      121 lhmlpellfq nnqalsrldl senaiqaipr kafrgatdlk nlqldknqis cieegafral
      181 rglevltlnn nnittipvss fnhmpklrtf rlhsnhlfcd chlawlsqwl rqrptiglft
      241 qcsgpaslrg lnvaevqkse fscsgqgeag rvptctlssg scpamctcsn givdcrgkgl
      301 taipanlpet mteirlelng iksippgafs pyrklrridl snnqiaeiap dafqglrsln
      361 slvlygnkit dlprgvfggl ytlqllllna nkincirpda fqdlqnlsll slydnkiqsl
      421 akgtftslra iqtlhlaqnp ficdcnlkwl adflrtnpie tsgarcaspr rlankrigqi
      481 kskkfrcsak eqyfipgted yqlnsecnsd vvcphkcrce anvvecsslk ltkiperipq
      541 staelrlnnn eisileatgm fkklthlkki nlsnnkvsei edgafegaas vselhltanq
      601 lesirsgmfr gldglrtlml rnnriscihn dsftglrnvr llslydnqit tvspgafdtl
      661 qslstlnlla npfncncqla wlggwlrkrk ivtgnprcqn pdflrqiplq dvafpdfrce
      721 egqeeggclp rpqcpqecac ldtvvrcsnk hlralpkgip knvtelyldg nqftlvpgql
      781 stfkylqlvd lsnnkissls nssftnmsql ttlilsynal qcipplafqg lrslrllslh
      841 gndistlqeg ifadvtslsh laiganplyc dchlrwlssw vktgykepgi arcagpqdme
      901 gklllttpak kfecqgpptl avqakcdlcl sspcqnqgtc hndplevyrc acpsgykgrd
      961 cevsldscss gpcenggtch aqegedapft cscptgfegp tcgvntddcv dhacanggvc
     1021 vdgvgnytcq cplqyegkac eqlvdlcspd lnpcqheaqc vgtpdgprce cmpgyagdnc
     1081 senqddcrdh rcqngaqcmd evnsysclca egysgqlcei pphlpapksp cegtecqnga
     1141 ncvdqgnrpv cqclpgfggp ecekllsvnf vdrdtylqft dlqnwprani tlqvstaedn
     1201 gillyngdnd hiavelyqgh vrvsydpgsy pssaiysaet indgqfhtve lvafdqmvnl
     1261 sidggspmtm dnfgkhytln seaplyvggm pvdvnsaafr lwqilngtgf hgcirnlyin
     1321 nelqdftktq mkpgvvpgce pcrklyclhg icqpnatpgp mchceagwvg lhcdqpadgp
     1381 chghkcvhgq cvpldalsys cqcqdgysga lcnqagalae pcrglqclhg hcqasgtkga
     1441 hcvcdpgfsg elceqesecr gdpvrdfhqv qrgyaicqtt rplswvecrg scpgqgccqg
     1501 lrlkrrkftf ecsdgtsfae evekptkcgc alca
//
LOCUS       NP_001075294             192 aa            linear   MAM 27-APR-2025
DEFINITION  erythropoietin precursor [Equus caballus].
ACCESSION   NP_001075294
VERSION     NP_001075294.1
DBSOURCE    REFSEQ: accession NM_001081825.2
KEYWORDS    RefSeq.
SOURCE      Equus caballus (horse)
  ORGANISM  Equus caballus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Hestand,M.S., Kalbfleisch,T.S., Coleman,S.J., Zeng,Z., Liu,J.,
            Orlando,L. and MacLeod,J.N.
  TITLE     Annotation of the Protein Coding Regions of the Equine Genome
  JOURNAL   PLoS One 10 (6), e0124375 (2015)
   PUBMED   26107351
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Sato,F., Yamashita,S., Kugo,T., Hasegawa,T., Mitsui,I. and
            Kijima-Suda,I.
  TITLE     Nucleotide sequence of equine erythropoietin and characterization
            of region-specific antibodies
  JOURNAL   Am J Vet Res 65 (1), 15-19 (2004)
   PUBMED   14719696
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB100030.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB100030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA104728729, SAMEA104728763
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Equus caballus"
                     /db_xref="taxon:9796"
                     /chromosome="13"
                     /map="13"
     Protein         1..192
                     /product="erythropoietin precursor"
                     /calculated_mol_wt=18332
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2670
     mat_peptide     27..192
                     /product="Erythropoietin. /id=PRO_0000008400"
                     /note="propagated from UniProtKB/Swiss-Prot (Q867B1.1)"
                     /calculated_mol_wt=18332
     Region          30..190
                     /region_name="EPO_TPO"
                     /note="Erythropoietin/thrombopoietin; pfam00758"
                     /db_xref="CDD:459927"
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q867B1.1)"
     Site            64
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q867B1.1)"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q867B1.1)"
     CDS             1..192
                     /gene="EPO"
                     /coded_by="NM_001081825.2:13..591"
                     /db_xref="GeneID:100033849"
                     /db_xref="VGNC:VGNC:51127"
ORIGIN      
        1 mgvrecpall lllslllppl glpalgappr licdsrvler yileareaen vtmgcaegcs
       61 fgenvtvpdt kvnfyswkrm eveqqavevw qglallseai lqgqallans sqpsetlrlh
      121 vdkavsslrs ltsllralga qkeaisppda asaaplrtfa vdtlcklfri ysnflrgklk
      181 lytgeacrrg dr
//
LOCUS       NP_037460                320 aa            linear   PRI 27-APR-2025
DEFINITION  pyrroline-5-carboxylate reductase 2 isoform 1 [Homo sapiens].
ACCESSION   NP_037460
VERSION     NP_037460.2
DBSOURCE    REFSEQ: accession NM_013328.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Wang,S., Yi,W., Xu,Z. and Shi,M.
  TITLE     PYCR2 promotes growth and aerobic glycolysis in human liver cancer
            by regulating the AKT signaling pathway
  JOURNAL   Biochem Biophys Res Commun 680, 15-24 (2023)
   PUBMED   37708598
  REMARK    GeneRIF: PYCR2 promotes growth and aerobic glycolysis in human
            liver cancer by regulating the AKT signaling pathway.
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Lama Tamang,R., Kumar,B., Patel,S.M., Thapa,I., Ahmad,A., Kumar,V.,
            Ahmad,R., Becker,D.F., Bastola,D.K., Dhawan,P. and Singh,A.B.
  TITLE     Pyrroline-5-Carboxylate Reductase-2 Promotes Colorectal
            Carcinogenesis by Modulating Microtubule-Associated
            Serine/Threonine Kinase-like/Wnt/beta-Catenin Signaling
  JOURNAL   Cells 12 (14), 1883 (2023)
   PUBMED   37508547
  REMARK    GeneRIF: Pyrroline-5-Carboxylate Reductase-2 Promotes Colorectal
            Carcinogenesis by Modulating Microtubule-Associated
            Serine/Threonine Kinase-like/Wnt/beta-Catenin Signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Sager,G., Turkyilmaz,A., Gunbey,H.P., Tas,I., Ozhelvaci,F. and
            Akin,Y.
  TITLE     Pyrroline-5-carboxylate reductase 2 (PYCR2) deficiency causes
            hereditary spastic paraplaegia in late childhood
  JOURNAL   Eur J Paediatr Neurol 44, 51-56 (2023)
   PUBMED   37141741
  REMARK    GeneRIF: Pyrroline-5-carboxylate reductase 2 (PYCR2) deficiency
            causes hereditary spastic paraplaegia in late childhood.
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Geng,Y., Chen,P., Zhang,L., Li,X., Song,C., Wei,X. and Gong,H.
  TITLE     LncRNA MALAT1 regulates growth of carcinoma of the lung through
            modulating miR-338-3p/PYCR2 axis
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (4), 133-140 (2023)
   PUBMED   37329534
  REMARK    GeneRIF: LncRNA MALAT1 regulates growth of carcinoma of the lung
            through modulating miR-338-3p/PYCR2 axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Ou,R., Zhang,X., Cai,J., Shao,X., Lv,M., Qiu,W., Xuan,X., Liu,J.,
            Li,Z. and Xu,Y.
  TITLE     Downregulation of pyrroline-5-carboxylate reductase-2 induces the
            autophagy of melanoma cells via AMPK/mTOR pathway
  JOURNAL   Tumour Biol 37 (5), 6485-6491 (2016)
   PUBMED   26634742
  REMARK    GeneRIF: It was found that silence of PYCR2 resulted in the
            decrease of proliferative ability and activation of
            AMPK/mTOR-induced autophagy of A375 cells. PYCR2 silencing also
            activated AMPK/mTOR pathway in another melanoma cell line, CHL-1.
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Kuo,M.L., Lee,M.B., Tang,M., den Besten,W., Hu,S., Sweredoski,M.J.,
            Hess,S., Chou,C.M., Changou,C.A., Su,M., Jia,W., Su,L. and Yen,Y.
  TITLE     PYCR1 and PYCR2 Interact and Collaborate with RRM2B to Protect
            Cells from Overt Oxidative Stress
  JOURNAL   Sci Rep 6, 18846 (2016)
   PUBMED   26733354
  REMARK    GeneRIF: Silencing of both PYCR1 and PYCR2 completely abolished
            anti-oxidation activity of RRM2B, demonstrating a functional
            collaboration of these metabolic enzymes in response to oxidative
            stress.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Nakayama,T., Al-Maawali,A., El-Quessny,M., Rajab,A., Khalil,S.,
            Stoler,J.M., Tan,W.H., Nasir,R., Schmitz-Abe,K., Hill,R.S.,
            Partlow,J.N., Al-Saffar,M., Servattalab,S., LaCoursiere,C.M.,
            Tambunan,D.E., Coulter,M.E., Elhosary,P.C., Gorski,G.,
            Barkovich,A.J., Markianos,K., Poduri,A. and Mochida,G.H.
  TITLE     Mutations in PYCR2, Encoding Pyrroline-5-Carboxylate Reductase 2,
            Cause Microcephaly and Hypomyelination
  JOURNAL   Am J Hum Genet 96 (5), 709-719 (2015)
   PUBMED   25865492
  REMARK    GeneRIF: Hypomyelination and the absence of lax caused by
            previously reported mutations in the gene encoding PYCR2's isozyme,
            PYCR1, suggesting a unique and indispensable role for PYCR2 in the
            human CNS during development.
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Togashi,Y., Arao,T., Kato,H., Matsumoto,K., Terashima,M.,
            Hayashi,H., de Velasco,M.A., Fujita,Y., Kimura,H., Yasuda,T.,
            Shiozaki,H. and Nishio,K.
  TITLE     Frequent amplification of ORAOV1 gene in esophageal squamous cell
            cancer promotes an aggressive phenotype via proline metabolism and
            ROS production
  JOURNAL   Oncotarget 5 (10), 2962-2973 (2014)
   PUBMED   24930674
REFERENCE   10 (residues 1 to 320)
  AUTHORS   De Ingeniis,J., Ratnikov,B., Richardson,A.D., Scott,D.A.,
            Aza-Blanc,P., De,S.K., Kazanov,M., Pellecchia,M., Ronai,Z.,
            Osterman,A.L. and Smith,J.W.
  TITLE     Functional specialization in proline biosynthesis of melanoma
  JOURNAL   PLoS One 7 (9), e45190 (2012)
   PUBMED   23024808
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC020553.1 and AW166558.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_037460.1.
            
            Summary: This gene belongs to the pyrroline-5-carboxylate reductase
            family. The encoded mitochondrial protein catalyzes the conversion
            of pyrroline-5-carboxylate to proline, which is the last step in
            proline biosynthesis. Alternatively spliced transcript variants
            have been described for this gene. [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.273299.1,
                                           SRR3476690.534714.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000343818.11/ ENSP00000342502.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.12"
     Protein         1..320
                     /product="pyrroline-5-carboxylate reductase 2 isoform 1"
                     /EC_number="1.5.1.2"
                     /note="P5C reductase 2; pyrroline-5-carboxylate reductase
                     family member 2"
                     /calculated_mol_wt=33506
     Region          1..268
                     /region_name="ProC"
                     /note="Pyrroline-5-carboxylate reductase [Amino acid
                     transport and metabolism]; COG0345"
                     /db_xref="CDD:440114"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.6;
                     propagated from UniProtKB/Swiss-Prot (Q96C36.1)"
     Region          295..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C36.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C36.1)"
     CDS             1..320
                     /gene="PYCR2"
                     /gene_synonym="HLD10; P5CR2"
                     /coded_by="NM_013328.4:141..1103"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31043.1"
                     /db_xref="GeneID:29920"
                     /db_xref="HGNC:HGNC:30262"
                     /db_xref="MIM:616406"
ORIGIN      
        1 msvgfigagq layalargft aagilsahki iasspemnlp tvsalrkmgv nltrsnketv
       61 khsdvlflav kphiipfild eigadvqarh ivvscaagvt issvekklma fqpapkvirc
      121 mtntpvvvqe gatvyatgth alvedgqlle qlmssvgfct eveedlidav tglsgsgpay
      181 afmaldalad ggvkmglprr laiqlgaqal lgaakmllds eqhpcqlkdn vcspggatih
      241 alhflesggf rsllinavea scirtrelqs madqekispa alkktlldrv klesptvstl
      301 tpsspgkllt rslalggkkd
//
LOCUS       NP_149108                190 aa            linear   PRI 27-APR-2025
DEFINITION  probable RNA-binding protein 18 [Homo sapiens].
ACCESSION   NP_149108
VERSION     NP_149108.1
DBSOURCE    REFSEQ: accession NM_033117.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Tsuritani,K., Irie,T., Yamashita,R., Sakakibara,Y., Wakaguri,H.,
            Kanai,A., Mizushima-Sugano,J., Sugano,S., Nakai,K. and Suzuki,Y.
  TITLE     Distinct class of putative 'non-conserved' promoters in humans:
            comparative studies of alternative promoters of human and mouse
            genes
  JOURNAL   Genome Res 17 (7), 1005-1014 (2007)
   PUBMED   17567985
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP870502.1, DA308339.1, BC008942.2, AL162424.20, AL389986.1 and
            CA314508.1.
            
            Transcript Variant: This variant (1) represents the shortest
            transcript and encodes the functional protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL389986.1, AK057676.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000417201.4/ ENSP00000409315.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.2"
     Protein         1..190
                     /product="probable RNA-binding protein 18"
                     /calculated_mol_wt=21518
     Region          <26..>189
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Region          26..105
                     /region_name="RRM_RBM18"
                     /note="RNA recognition motif (RRM) found in eukaryotic
                     RNA-binding protein 18 and similar proteins; cd12355"
                     /db_xref="CDD:409791"
     Region          166..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96H35.1)"
     CDS             1..190
                     /gene="RBM18"
                     /coded_by="NM_033117.4:143..715"
                     /db_xref="CCDS:CCDS6839.1"
                     /db_xref="GeneID:92400"
                     /db_xref="HGNC:HGNC:28413"
ORIGIN      
        1 meaetktlpl enasilsegs lqeghrlwig nldpkiteyh llkllqkfgk vkqfdflfhk
       61 sgalegqprg ycfvnfetkq eaeqaiqcln gklalskklv vrwahaqvkr ydhnkndkil
      121 pislepssst eptqsnlsvt akikaieakl kmmaenpdae ypaapvysyf kppdkkrttp
      181 ysrtawksrr
//
LOCUS       NP_055901                711 aa            linear   PRI 27-APR-2025
DEFINITION  dendrin [Homo sapiens].
ACCESSION   NP_055901 XP_290598
VERSION     NP_055901.2
DBSOURCE    REFSEQ: accession NM_015086.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Levin,A., Schwarz,A., Hulkko,J., He,L., Sun,Y., Barany,P.,
            Bruchfeld,A., Herthelius,M., Wennberg,L., Ebefors,K., Patrakka,J.,
            Betsholtz,C., Nystrom,J., Molne,J., Hultenby,K., Witasp,A. and
            Wernerson,A.
  TITLE     The role of dendrin in IgA nephropathy
  JOURNAL   Nephrol Dial Transplant 38 (2), 311-321 (2023)
   PUBMED   35767852
  REMARK    GeneRIF: The role of dendrin in IgA nephropathy.
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Mizdrak,M., Vukojevic,K., Filipovic,N., Capkun,V., Benzon,B. and
            Durdov,M.G.
  TITLE     Expression of DENDRIN in several glomerular diseases and
            correlation to pathological parameters and renal failure -
            preliminary study
  JOURNAL   Diagn Pathol 13 (1), 90 (2018)
   PUBMED   30458823
  REMARK    GeneRIF: The number of dendrin positive nuclei was higher in
            podocytopathies than in inflammatory glomerular diseases and
            correlated with chronic tubulointerstitial changes and lower
            creatinine clearance.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Kodama,F., Asanuma,K., Takagi,M., Hidaka,T., Asanuma,E., Fukuda,H.,
            Seki,T., Takeda,Y., Hosoe-Nagai,Y., Asao,R., Horikoshi,S. and
            Tomino,Y.
  TITLE     Translocation of dendrin to the podocyte nucleus in acute
            glomerular injury in patients with IgA nephropathy
  JOURNAL   Nephrol Dial Transplant 28 (7), 1762-1772 (2013)
   PUBMED   23143340
  REMARK    GeneRIF: Increasing number of dendrin-positive nuclei in the
            glomeruli suggest acute glomerular injury in IgA nephropathy.
REFERENCE   4  (residues 1 to 711)
  AUTHORS   Campbell,K.N., Wong,J.S., Gupta,R., Asanuma,K., Sudol,M., He,J.C.
            and Mundel,P.
  TITLE     Yes-associated protein (YAP) promotes cell survival by inhibiting
            proapoptotic dendrin signaling
  JOURNAL   J Biol Chem 288 (24), 17057-17062 (2013)
   PUBMED   23667252
  REMARK    GeneRIF: YAP binding to dendrin is a prosurvival mechanism in
            podocytes.
REFERENCE   5  (residues 1 to 711)
  AUTHORS   Asanuma,K., Akiba-Takagi,M., Kodama,F., Asao,R., Nagai,Y.,
            Lydia,A., Fukuda,H., Tanaka,E., Shibata,T., Takahara,H., Hidaka,T.,
            Asanuma,E., Kominami,E., Ueno,T. and Tomino,Y.
  TITLE     Dendrin location in podocytes is associated with disease
            progression in animal and human glomerulopathy
  JOURNAL   Am J Nephrol 33 (6), 537-549 (2011)
   PUBMED   21606645
  REMARK    GeneRIF: Relocation of dendrin to the podocyte nuclei is useful as
            a novel marker of podocyte injury in human glomerulopathy.
REFERENCE   6  (residues 1 to 711)
  AUTHORS   Duner,F., Patrakka,J., Xiao,Z., Larsson,J., Vlamis-Gardikas,A.,
            Pettersson,E., Tryggvason,K., Hultenby,K. and Wernerson,A.
  TITLE     Dendrin expression in glomerulogenesis and in human minimal change
            nephrotic syndrome
  JOURNAL   Nephrol Dial Transplant 23 (8), 2504-2511 (2008)
   PUBMED   18356187
  REMARK    GeneRIF: In minimal change nephrotic syndrome, dendrin and ZO-1 are
            re-distributed within the podocytes. Whether this is a cause or a
            consequence of foot process effacement remains unclear.
REFERENCE   7  (residues 1 to 711)
  AUTHORS   Kawata,A., Iida,J., Ikeda,M., Sato,Y., Mori,H., Kansaku,A.,
            Sumita,K., Fujiwara,N., Rokukawa,C., Hamano,M., Hirabayashi,S. and
            Hata,Y.
  TITLE     CIN85 is localized at synapses and forms a complex with S-SCAM via
            dendrin
  JOURNAL   J Biochem 139 (5), 931-939 (2006)
   PUBMED   16751601
REFERENCE   8  (residues 1 to 711)
  AUTHORS   Kremerskothen,J., Kindler,S., Finger,I., Veltel,S. and Barnekow,A.
  TITLE     Postsynaptic recruitment of Dendrin depends on both dendritic mRNA
            transport and synaptic anchoring
  JOURNAL   J Neurochem 96 (6), 1659-1666 (2006)
   PUBMED   16464232
REFERENCE   9  (residues 1 to 711)
  AUTHORS   Kremerskothen,J., Plaas,C., Buther,K., Finger,I., Veltel,S.,
            Matanis,T., Liedtke,T. and Barnekow,A.
  TITLE     Characterization of KIBRA, a novel WW domain-containing protein
  JOURNAL   Biochem Biophys Res Commun 300 (4), 862-867 (2003)
   PUBMED   12559952
REFERENCE   10 (residues 1 to 711)
  AUTHORS   Neuner-Jehle,M., Denizot,J.P., Borbely,A.A. and Mallet,J.
  TITLE     Characterization and sleep deprivation-induced expression
            modulation of dendrin, a novel dendritic protein in rat brain
            neurons
  JOURNAL   J Neurosci Res 46 (2), 138-151 (1996)
   PUBMED   8915891
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011603.37, BC039264.1 and AB018292.1.
            
            On Jul 16, 2008 this sequence version replaced NP_055901.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC039264.1, AB018292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000421952.3/ ENSP00000390590.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..711
                     /product="dendrin"
                     /calculated_mol_wt=75865
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94850.3)"
     Region          49..273
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94850.3)"
     Region          55..709
                     /region_name="Dendrin"
                     /note="Nephrin and CD2AP-binding protein, Dendrin;
                     pfam15498"
                     /db_xref="CDD:464749"
     Region          113..131
                     /region_name="Nuclear localization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O94850.3)"
     Region          186..236
                     /region_name="Interaction with MAGI2"
                     /note="propagated from UniProtKB/Swiss-Prot (O94850.3)"
     Region          324..446
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94850.3)"
     Region          341..436
                     /region_name="Interaction with ACTN1.
                     /evidence=ECO:0000269|PubMed:16464232"
                     /note="propagated from UniProtKB/Swiss-Prot (O94850.3)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80TS7; propagated from
                     UniProtKB/Swiss-Prot (O94850.3)"
     Region          408..709
                     /region_name="Interaction with CD2AP and NPHS1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O94850.3)"
     Region          479..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94850.3)"
     CDS             1..711
                     /gene="DDN"
                     /coded_by="NM_015086.2:89..2224"
                     /db_xref="CCDS:CCDS31791.2"
                     /db_xref="GeneID:23109"
                     /db_xref="HGNC:HGNC:24458"
                     /db_xref="MIM:610588"
ORIGIN      
        1 mldgplfseg pdsprelqde esgsclwvqk skllvievkt ischysrrap srqpmdfqas
       61 hwargfqnrt cgprpgspqp pprrpwasrv lqeatnwrag plaevrareq ekrkaasqer
      121 eaketerkrr kaggarrspp grprpeprna prvaqlaglp aplrperlap vgraprpsaq
      181 pqsdpgsawa gpwggrrpgp psyeahlllr gsagtaprrr wdrpppyvap psyegphrtl
      241 gtkrgpgnsq vptssapaat partdggrtk krldpriyrd vlgawglrqg qgllggspgc
      301 gaararpepg kgvvekslgl aaadlnsgsd shpqakatgs agteiapags ataapcaphp
      361 aprsrhhlkg sregkegeqi wfpkcwipsp kkqpprhsqt lprpwapggt gwreslglge
      421 gagpetlegw katrrahtlp rssqglsrge gvfvidatcv virsqyvptp rtqqvqllps
      481 gvtrvvgdsp sqskpgkeeg egatvfpspc qkrlsssrll hqpgggrgge aeggrpgdst
      541 leertfrilg lpapevnlrd aptqpgspeh qalgpaasga qgraegseva vvqrragrgw
      601 artpgpyaga lreavsrirr htapdsdtde aeelsvhsgs sdgsdteapg aswrnertlp
      661 evgnsspeed gktaelsdsv geildvisqt eevlfgvrdi rgtqqgnrkr q
//
LOCUS       NP_919248                209 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding protein with multiple splicing 2 [Homo sapiens].
ACCESSION   NP_919248 XP_496072
VERSION     NP_919248.1
DBSOURCE    REFSEQ: accession NM_194272.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Cheng,M., Zhan,X., Xu,Y., Wang,S., Zhang,H., Fang,L., Jin,H. and
            Chen,W.
  TITLE     DNA methylation of RNA-binding protein for multiple splicing 2
            functions as diagnosis biomarker in gastric cancer pathogenesis and
            its potential clinical significance
  JOURNAL   Bioengineered 13 (2), 4347-4360 (2022)
   PUBMED   35137653
  REMARK    GeneRIF: DNA methylation of RNA-binding protein for multiple
            splicing 2 functions as diagnosis biomarker in gastric cancer
            pathogenesis and its potential clinical significance.
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Sagnol,S., Yang,Y., Bessin,Y., Allemand,F., Hapkova,I.,
            Notarnicola,C., Guichou,J.F., Faure,S., Labesse,G. and de Santa
            Barbara,P.
  TITLE     Homodimerization of RBPMS2 through a new RRM-interaction motif is
            necessary to control smooth muscle plasticity
  JOURNAL   Nucleic Acids Res 42 (15), 10173-10184 (2014)
   PUBMED   25064856
  REMARK    GeneRIF: The study shows that RBPMS2 homodimerizes through a
            particular sequence motif located in its RNA recognition motif
            domain.
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Farazi,T.A., Leonhardt,C.S., Mukherjee,N., Mihailovic,A., Li,S.,
            Max,K.E., Meyer,C., Yamaji,M., Cekan,P., Jacobs,N.C.,
            Gerstberger,S., Bognanni,C., Larsson,E., Ohler,U. and Tuschl,T.
  TITLE     Identification of the RNA recognition element of the RBPMS family
            of RNA-binding proteins and their transcriptome-wide mRNA targets
  JOURNAL   RNA 20 (7), 1090-1102 (2014)
   PUBMED   24860013
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Hapkova,I., Skarda,J., Rouleau,C., Thys,A., Notarnicola,C.,
            Janikova,M., Bernex,F., Rypka,M., Vanderwinden,J.M., Faure,S.,
            Vesely,J. and de Santa Barbara,P.
  TITLE     High expression of the RNA-binding protein RBPMS2 in
            gastrointestinal stromal tumors
  JOURNAL   Exp Mol Pathol 94 (2), 314-321 (2013)
   PUBMED   23295309
  REMARK    GeneRIF: RBPMS2 is up-regulated in Gastrointestinal stromal tumors
            compared to normal adult gastrointestinal tissues, indicating that
            RBPMS2 might represent a new diagnostic marker for GISTs and a
            potential target for cancer therapy.
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Notarnicola,C., Rouleau,C., Le Guen,L., Virsolvy,A., Richard,S.,
            Faure,S. and De Santa Barbara,P.
  TITLE     The RNA-binding protein RBPMS2 regulates development of
            gastrointestinal smooth muscle
  JOURNAL   Gastroenterology 143 (3), 687-697 (2012)
   PUBMED   22683258
  REMARK    GeneRIF: RBPMS3 transcripts are up-regulation in colons of patients
            with chronic psuedo obstruction syndrome.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091582.17, AK127873.1 and
            AI274305.1.
            
            On May 1, 2005 this sequence version replaced XP_496072.1.
            
            Summary: The protein encoded by this gene is a member of the RNA
            recognition motif (RRM)-containing protein family and is involved
            in the development and dedifferentiation of digestive smooth muscle
            cells. The encoded protein functions as a homodimer and indirectly
            inhibits the bone morphogenetic protein pathway. [provided by
            RefSeq, Aug 2016].
            
            Transcript Variant: This variant (1) represents the protein-coding
            transcript.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY369207.1, AK127873.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300069.5/ ENSP00000300069.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..209
                     /product="RNA-binding protein with multiple splicing 2"
                     /note="RNA binding protein with multiple splicing 2"
                     /calculated_mol_wt=22365
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZRY4.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6ZRY4.1)"
     Region          30..105
                     /region_name="RRM_RBPMS2"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     RNA-binding protein with multiple splicing 2 (RBP-MS2);
                     cd12683"
                     /db_xref="CDD:410084"
     Region          41..51
                     /region_name="Important for homodimerization.
                     /evidence=ECO:0000269|PubMed:25064856"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZRY4.1)"
     CDS             1..209
                     /gene="RBPMS2"
                     /coded_by="NM_194272.3:271..900"
                     /db_xref="CCDS:CCDS32271.1"
                     /db_xref="GeneID:348093"
                     /db_xref="HGNC:HGNC:19098"
                     /db_xref="MIM:619034"
ORIGIN      
        1 msnlkpdgeh ggstgtgsga gsggaleeev rtlfvsglpv dikprelyll frpfkgyegs
       61 likltarqpv gfvifdsrag aeaaknalng irfdpenpqt lrlefakant kmaksklmat
      121 pnpsnvhpal gahfiardpy dlmgaalipa speawapypl ytteltpais haaftyptat
      181 aaaaalhaqv rwypssdttq qgwkyrqfc
//
LOCUS       NP_612418                205 aa            linear   PRI 27-APR-2025
DEFINITION  melanocortin-2 receptor accessory protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_612418
VERSION     NP_612418.2
DBSOURCE    REFSEQ: accession NM_138409.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   da Fonseca,A.C.P., Abreu,G.M., Zembrzuski,V.M., Campos Junior,M.,
            Carneiro,J.R.I., Nogueira Neto,J.F., Magno,F.C.C.M., Rosado,E.L.,
            Bozza,P.T., de Cabello,G.M.K. and Cabello,P.H.
  TITLE     Study of LEP, MRAP2 and POMC genes as potential causes of severe
            obesity in Brazilian patients
  JOURNAL   Eat Weight Disord 26 (5), 1399-1408 (2021)
   PUBMED   32578125
  REMARK    GeneRIF: Study of LEP, MRAP2 and POMC genes as potential causes of
            severe obesity in Brazilian patients.
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Chen,V., Bruno,A.E., Britt,L.L., Hernandez,C.C., Gimenez,L.E.,
            Peisley,A., Cone,R.D. and Millhauser,G.L.
  TITLE     Membrane orientation and oligomerization of the melanocortin
            receptor accessory protein 2
  JOURNAL   J Biol Chem 295 (48), 16370-16379 (2020)
   PUBMED   32943551
  REMARK    GeneRIF: Membrane orientation and oligomerization of the
            melanocortin receptor accessory protein 2.
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Rouault,A.A.J., Rosselli-Murai,L.K., Hernandez,C.C., Gimenez,L.E.,
            Tall,G.G. and Sebag,J.A.
  TITLE     The GPCR accessory protein MRAP2 regulates both biased signaling
            and constitutive activity of the ghrelin receptor GHSR1a
  JOURNAL   Sci Signal 13 (613) (2020)
   PUBMED   31911434
  REMARK    GeneRIF: The GPCR accessory protein MRAP2 regulates both biased
            signaling and constitutive activity of the ghrelin receptor GHSR1a.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Sebag,J.A. and Hinkle,P.M.
  TITLE     Regulation of G protein-coupled receptor signaling: specific
            dominant-negative effects of melanocortin 2 receptor accessory
            protein 2
  JOURNAL   Sci Signal 3 (116), ra28 (2010)
   PUBMED   20371771
  REMARK    GeneRIF: MRAP2 is an endogenous inhibitor that competes with MRAP
            for binding to MC2R and decreases the potency of
            adrenocorticotropic hormone (ACTH).
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Chan,L.F., Webb,T.R., Chung,T.T., Meimaridou,E., Cooray,S.N.,
            Guasti,L., Chapple,J.P., Egertova,M., Elphick,M.R., Cheetham,M.E.,
            Metherell,L.A. and Clark,A.J.
  TITLE     MRAP and MRAP2 are bidirectional regulators of the melanocortin
            receptor family
  JOURNAL   Proc Natl Acad Sci U S A 106 (15), 6146-6151 (2009)
   PUBMED   19329486
  REMARK    GeneRIF: identify MRAP and MRAP2 as unique bidirectional regulators
            of the melanocortin receptor family
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Sebag,J.A. and Hinkle,P.M.
  TITLE     Regions of melanocortin 2 (MC2) receptor accessory protein
            necessary for dual topology and MC2 receptor trafficking and
            signaling
  JOURNAL   J Biol Chem 284 (1), 610-618 (2009)
   PUBMED   18981183
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Metherell,L.A., Chapple,J.P., Cooray,S., David,A., Becker,C.,
            Ruschendorf,F., Naville,D., Begeot,M., Khoo,B., Nurnberg,P.,
            Huebner,A., Cheetham,M.E. and Clark,A.J.
  TITLE     Mutations in MRAP, encoding a new interacting partner of the ACTH
            receptor, cause familial glucocorticoid deficiency type 2
  JOURNAL   Nat Genet 37 (2), 166-170 (2005)
   PUBMED   15654338
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC010003.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 28, 2007 this sequence version replaced NP_612418.1.
            
            Summary: This gene encodes a protein that modulates melanocortin
            receptor signaling. The encoded protein has been shown to interact
            with all known melanocortin receptors and may regulate both
            receptor trafficking and activation in response to ligands. Mice
            lacking a functional copy of this gene exhibit severe obesity and a
            mutation in this gene may be associated with severe obesity in
            human patients. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Variants 1, 3 and 5 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC010003.2, SRR1660803.215804.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257776.5/ ENSP00000257776.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.2"
     Protein         1..205
                     /product="melanocortin-2 receptor accessory protein 2
                     isoform 1"
                     /note="MC2R accessory protein 2"
                     /calculated_mol_wt=23417
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19329486; propagated from
                     UniProtKB/Swiss-Prot (Q96G30.2)"
     Region          13..99
                     /region_name="MRAP"
                     /note="Melanocortin-2 receptor accessory protein family;
                     pfam15183"
                     /db_xref="CDD:464550"
     Site            45..65
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96G30.2)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96G30.2)"
     CDS             1..205
                     /gene="MRAP2"
                     /gene_synonym="bA51G5.2; C6orf117"
                     /coded_by="NM_138409.4:120..737"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5001.1"
                     /db_xref="GeneID:112609"
                     /db_xref="HGNC:HGNC:21232"
                     /db_xref="MIM:615410"
ORIGIN      
        1 msaqrlisnr tsqqsasnsd ytweyeyyei gpvsfeglka hkysivigfw vglavfvifm
       61 ffvltlltkt gaphqdnaes sekrfrmnsf vsdfgrplep dkvfsrqgne esrslfhcyi
      121 neverldrak achqttalds dvqlqeairs sgqpeeelnr lmkfdipnfv ntdqnyfged
      181 dlliseppiv letkplsqts hkdld
//
LOCUS       NP_001258085             198 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 41 homolog [Homo sapiens].
ACCESSION   NP_001258085 XP_005250949
VERSION     NP_001258085.3
DBSOURCE    REFSEQ: accession NM_001271156.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Teng,Y., Xu,J., Wang,Y., Wen,N., Ye,H. and Li,B.
  TITLE     Combining a glycolysis-related prognostic model based on scRNA-Seq
            with experimental verification identifies ZFP41 as a potential
            prognostic biomarker for HCC
  JOURNAL   Mol Med Rep 29 (5) (2024)
   PUBMED   38516783
  REMARK    GeneRIF: Combining a glycolysis-related prognostic model based on
            scRNA-Seq with experimental verification identifies ZFP41 as a
            potential prognostic biomarker for HCC.
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Noce,T., Fujiwara,Y., Sezaki,M., Fujimoto,H. and Higashinakagawa,T.
  TITLE     Expression of a mouse zinc finger protein gene in both
            spermatocytes and oocytes during meiosis
  JOURNAL   Dev Biol 153 (2), 356-367 (1992)
   PUBMED   1397691
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138696.4, BC034608.1 and DA216172.1.
            
            On Jul 14, 2018 this sequence version replaced NP_001258085.2.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034608.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            NMD candidate                    :: translation inferred from
                                                conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..198
                     /product="zinc finger protein 41 homolog"
                     /calculated_mol_wt=22675
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8Y5.1)"
     Region          <8..>72
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          <85..198
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          89..109
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          117..137
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(122,124,126,128..129,132..133,136,150,152,156..157,
                     160..161,164,178,180,182,184..185,188..189,192)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          145..165
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          157..182
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          173..193
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..198
                     /gene="ZFP41"
                     /gene_synonym="zfp-41; ZNF753"
                     /coded_by="NM_001271156.3:966..1562"
                     /db_xref="CCDS:CCDS6397.3"
                     /db_xref="GeneID:286128"
                     /db_xref="HGNC:HGNC:26786"
ORIGIN      
        1 mekpagrkkk tptpreeadv qksalreekv sgdrkpperp tvprkprtep clspedeehv
       61 fdafdasfkd dfegvpvfip fqrkkpyecs ecgrifkhkt dhirhqrvht gekpfkcaqc
      121 gkafrhssdv tkhqrthtge kpfkcgecgk afncgsnllk hqkthtgekp yecthcgkaf
      181 ayssclirhq krhprkkp
//
LOCUS       NP_000018                346 aa            linear   PRI 27-APR-2025
DEFINITION  N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase isoform 1
            preproprotein [Homo sapiens].
ACCESSION   NP_000018
VERSION     NP_000018.2
DBSOURCE    REFSEQ: accession NM_000027.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Saarela,J., Oinonen,C., Jalanko,A., Rouvinen,J. and Peltonen,L.
  TITLE     Autoproteolytic activation of human aspartylglucosaminidase
  JOURNAL   Biochem J 378 (Pt 2), 363-371 (2004)
   PUBMED   14616088
  REMARK    GeneRIF: Molecular mechanism for the autoproteolytic activation of
            aspartylglucosaminidase.
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Goodspeed,K., Chen,X. and Tchan,M.
  TITLE     Aspartylglucosaminuria
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   38252773
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Rip,J.W., Coulter-Mackie,M.B., Rupar,C.A. and Gordon,B.A.
  TITLE     Purification and structure of human liver aspartylglucosaminidase
  JOURNAL   Biochem J 288 (Pt 3) (Pt 3), 1005-1010 (1992)
   PUBMED   1281977
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Ikonen,E. and Peltonen,L.
  TITLE     Mutations causing aspartylglucosaminuria (AGU): a lysosomal
            accumulation disease
  JOURNAL   Hum Mutat 1 (5), 361-365 (1992)
   PUBMED   1301945
  REMARK    Review article
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Park,H., Fisher,K.J. and Aronson,N.N. Jr.
  TITLE     Genomic structure of human lysosomal glycosylasparaginase
  JOURNAL   FEBS Lett 288 (1-2), 168-172 (1991)
   PUBMED   1840528
REFERENCE   8  (residues 1 to 346)
  AUTHORS   Fisher,K.J. and Aronson,N.N. Jr.
  TITLE     Characterization of the mutation responsible for
            aspartylglucosaminuria in three Finnish patients. Amino acid
            substitution Cys163----Ser abolishes the activity of lysosomal
            glycosylasparaginase and its conversion into subunits
  JOURNAL   J Biol Chem 266 (18), 12105-12113 (1991)
   PUBMED   1904874
REFERENCE   9  (residues 1 to 346)
  AUTHORS   Mononen,I., Heisterkamp,N., Kaartinen,V., Williams,J.C., Yates,J.R.
            3rd, Griffin,P.R., Hood,L.E. and Groffen,J.
  TITLE     Aspartylglycosaminuria in the Finnish population: identification of
            two point mutations in the heavy chain of glycoasparaginase
  JOURNAL   Proc Natl Acad Sci U S A 88 (7), 2941-2945 (1991)
   PUBMED   2011603
REFERENCE   10 (residues 1 to 346)
  AUTHORS   Fisher,K.J., Tollersrud,O.K. and Aronson,N.N. Jr.
  TITLE     Cloning and sequence analysis of a cDNA for human
            glycosylasparaginase. A single gene encodes the subunits of this
            lysosomal amidase
  JOURNAL   FEBS Lett 269 (2), 440-444 (1990)
   PUBMED   2401370
  REMARK    Erratum:[FEBS Lett 1990 Dec 10;276(1-2):232]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA346002.1, BC012392.1,
            AW467768.1, AC027627.6 and BM968469.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 30, 2010 this sequence version replaced NP_000018.1.
            
            Summary: This gene encodes a member of the N-terminal nucleophile
            (Ntn) hydrolase family of proteins. The encoded preproprotein is
            proteolytically processed to generate alpha and beta chains that
            comprise the mature enzyme. This enzyme is involved in the
            catabolism of N-linked oligosaccharides of glycoproteins. It
            cleaves asparagine from N-acetylglucosamines as one of the final
            steps in the lysosomal breakdown of glycoproteins. Mutations in
            this gene are associated with the lysosomal storage disease
            aspartylglycosaminuria that results in progressive
            neurodegeneration. Alternative splicing results in multiple
            transcript variants, at least one of which encodes an isoform that
            is subject to proteolytic processing. [provided by RefSeq, Nov
            2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.973824.1,
                                           SRR1803612.248008.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264595.7/ ENSP00000264595.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q34.3"
     Protein         1..346
                     /product="N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
                     isoform 1 preproprotein"
                     /EC_number="3.5.1.26"
                     /note="N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase;
                     glycosylasparaginase;
                     N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase;
                     aspartylglucosylamine deaspartylase"
                     /calculated_mol_wt=34641
     sig_peptide     1..23
                     /note="/evidence=ECO:0000269|PubMed:2011603,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P20933.2)"
                     /calculated_mol_wt=2585
     mat_peptide     24..205
                     /product="Glycosylasparaginase alpha chain.
                     /id=PRO_0000002333"
                     /note="propagated from UniProtKB/Swiss-Prot (P20933.2)"
                     /calculated_mol_wt=19591
     Site            24
                     /site_type="blocked"
                     /note="Blocked amino end (Ser); propagated from
                     UniProtKB/Swiss-Prot (P20933.2)"
     Region          29..332
                     /region_name="Glycosylasparaginase"
                     /note="Glycosylasparaginase and similar proteins; cd04513"
                     /db_xref="CDD:271335"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:1281977,
                     ECO:0000269|PubMed:2401370, ECO:0000269|PubMed:8846222,
                     ECO:0007744|PDB:1APY, ECO:0007744|PDB:1APZ; propagated
                     from UniProtKB/Swiss-Prot (P20933.2)"
     Site            order(97..99,104,124..128,130..131,134..135,232..235,
                     240..242,246,261,264,270,274,292)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271335"
     mat_peptide     206..346
                     /product="Glycosylasparaginase beta chain.
                     /id=PRO_0000002334"
                     /note="propagated from UniProtKB/Swiss-Prot (P20933.2)"
                     /calculated_mol_wt=15068
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:8846222,
                     ECO:0007744|PDB:1APY, ECO:0007744|PDB:1APZ; propagated
                     from UniProtKB/Swiss-Prot (P20933.2)"
     CDS             1..346
                     /gene="AGA"
                     /gene_synonym="AGU; ASRG; GA"
                     /coded_by="NM_000027.4:63..1103"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3829.1"
                     /db_xref="GeneID:175"
                     /db_xref="HGNC:HGNC:318"
                     /db_xref="MIM:613228"
ORIGIN      
        1 marksnlpvl lvpfllcqal vrcssplplv vntwpfknat eaawralasg gsaldavesg
       61 camcereqcd gsvgfggspd elgettldam imdgttmdvg avgdlrrikn aigvarkvle
      121 htthtllvge sattfaqsmg finedlstta sqalhsdwla rncqpnywrn vipdpskycg
      181 pykppgilkq dipihketed drghdtigmv vihktghiaa gtstngikfk ihgrvgdspi
      241 pgagayaddt agaaaatgng dilmrflpsy qaveymrrge dptiacqkvi sriqkhfpef
      301 fgavicanvt gsygaacnkl stftqfsfmv ynseknqpte ekvdci
//
LOCUS       NP_067289               1036 aa            linear   ROD 27-APR-2025
DEFINITION  transforming acidic coiled-coil-containing protein 2 isoform b [Mus
            musculus].
ACCESSION   NP_067289
VERSION     NP_067289.2
DBSOURCE    REFSEQ: accession NM_021314.5
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Mallampalli,R.K., Li,X., Jang,J.H., Kaminski,T., Hoji,A., Coon,T.,
            Chandra,D., Welty,S., Teng,Y., Sembrat,J., Rojas,M., Zhao,Y.,
            Lafyatis,R., Zou,C., Sciurba,F., Sundd,P., Lan,L. and Nyunoya,T.
  TITLE     Cigarette smoke exposure enhances transforming acidic
            coiled-coil-containing protein 2 turnover and thereby promotes
            emphysema
  JOURNAL   JCI Insight 5 (2), 125895 (2020)
   PUBMED   31996486
  REMARK    GeneRIF: Cigarette smoke exposure enhances transforming acidic
            coiled-coil-containing protein 2 turnover and thereby promotes
            emphysema.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Ray,J.P., Staron,M.M., Shyer,J.A., Ho,P.C., Marshall,H.D.,
            Gray,S.M., Laidlaw,B.J., Araki,K., Ahmed,R., Kaech,S.M. and
            Craft,J.
  TITLE     The Interleukin-2-mTORc1 Kinase Axis Defines the Signaling,
            Differentiation, and Metabolism of T Helper 1 and Follicular B
            Helper T Cells
  JOURNAL   Immunity 43 (4), 690-702 (2015)
   PUBMED   26410627
REFERENCE   4  (residues 1 to 1036)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1036)
  AUTHORS   Tei,S., Saitoh,N., Funahara,T., Iida,S., Nakatsu,Y., Kinoshita,K.,
            Kinoshita,Y., Saya,H. and Nakao,M.
  TITLE     Simian virus 40 large T antigen targets the microtubule-stabilizing
            protein TACC2
  JOURNAL   J Cell Sci 122 (Pt 17), 3190-3198 (2009)
   PUBMED   19671663
REFERENCE   6  (residues 1 to 1036)
  AUTHORS   Schuendeln,M.M., Piekorz,R.P., Wichmann,C., Lee,Y., McKinnon,P.J.,
            Boyd,K., Takahashi,Y. and Ihle,J.N.
  TITLE     The centrosomal, putative tumor suppressor protein TACC2 is
            dispensable for normal development, and deficiency does not lead to
            cancer
  JOURNAL   Mol Cell Biol 24 (14), 6403-6409 (2004)
   PUBMED   15226440
  REMARK    GeneRIF: Results suggest that TACC2 is not required for mouse
            development and normal cell proliferation and is not a tumor
            suppressor protein.
REFERENCE   7  (residues 1 to 1036)
  AUTHORS   Still,I.H., Vettaikkorumakankauv,A.K., DiMatteo,A. and Liang,P.
  TITLE     Structure-function evolution of the transforming acidic coiled coil
            genes revealed by analysis of phylogenetically diverse organisms
  JOURNAL   BMC Evol Biol 4, 16 (2004)
   PUBMED   15207008
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1036)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 1036)
  AUTHORS   Piekorz,R.P., Hoffmeyer,A., Duntsch,C.D., McKay,C., Nakajima,H.,
            Sexl,V., Snyder,L., Rehg,J. and Ihle,J.N.
  TITLE     The centrosomal protein TACC3 is essential for hematopoietic stem
            cell function and genetically interfaces with p53-regulated
            apoptosis
  JOURNAL   EMBO J 21 (4), 653-664 (2002)
   PUBMED   11847113
REFERENCE   10 (residues 1 to 1036)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC145294.4.
            
            On Sep 22, 2004 this sequence version replaced NP_067289.1.
            
            Summary: This gene encodes a member of the transforming, acidic
            coiled-coil (TACC) family of proteins. Members of this family are
            centrosomal proteins that interact with microtubules and tubulin.
            TACC proteins are thought to be involved in centrosome/mitotic
            spindle dynamics and gene regulation. Alternative splicing of this
            gene results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849375,
                              SAMN01164132 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 73.19 cM"
     Protein         1..1036
                     /product="transforming acidic coiled-coil-containing
                     protein 2 isoform b"
                     /calculated_mol_wt=112805
     Region          183..>294
                     /region_name="PRK13335"
                     /note="superantigen-like protein SSL3; Reviewed"
                     /db_xref="CDD:139494"
     Region          <529..786
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          830..1030
                     /region_name="TACC_C"
                     /note="Transforming acidic coiled-coil-containing protein
                     (TACC), C-terminal; pfam05010"
                     /db_xref="CDD:461517"
     CDS             1..1036
                     /gene="Tacc2"
                     /gene_synonym="mKIAA4180"
                     /coded_by="NM_021314.5:303..3413"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS21905.1"
                     /db_xref="GeneID:57752"
                     /db_xref="MGI:MGI:1928899"
ORIGIN      
        1 mggsqslqpa pasdlnlevs eamssdseea fetpesttpv kappappppp pevtpepevi
       61 dppapeepgc iseppvvvpd gprssesveg spfrpshsss avfdedkpia ssgtynldfd
      121 sielvdnfqs lepcsadskg qeckvstrrk stesvppsks tlsrslslqa sdfdgascpg
      181 speagtlttd acgtgsnsas stlkrtkktr ppslkkkqat kkptetppvk etqqepgees
      241 pvpseehlap etktesatpe gagctlsddt plespavpta tcpltlesae dvsplvsggg
      301 rvqnsppvgr ksvplttase avevtlsdsg gqedlpakgl svrlefdyse dkgswesqqe
      361 napptkkigk kpvakmplrr pkmkktpekl dntpaspprs ptepsdtpia kgtytfdidk
      421 wddpnfnpfs stskmqespk lsqqsynfdp daceesldpf kassktpssp skspasfeip
      481 astteadgdg lnkpakkkkt plktmvedvm svcslfdtfr vkkspkrspl sdppsqdptp
      541 aatpeapsai stvvhatdee klavtsqkwt cmtvdldadk qdfpqpsdls nfvnetkfns
      601 pseeldyrns yeieymeklg sslpqdddtp kkqalylmfd tpqespvksp pvrmsdsptp
      661 csgssfedte alvnaatklq hpvarglpss qepllqvpek psqkeleama lgtpaeaiei
      721 tapegafasa dtllsrlahp aslcgalgyl epdlaeknpp vfaqklqeel efavmrieal
      781 klarqialas rsrqdtkrea ahppdvsisk talysrigst evekppgllf qqpdldsalq
      841 varaeviake revsewrdky eesrrevvem rkivaeyekt iaqmiedeqr eksishqtvq
      901 qlvlekeqal adlnsveksl adlfrryekm kevlegfrkn eevlkkcaqe ylsrvkkeeq
      961 ryqalkvhae ekldranaei aqvrgkaqqe qaayqaslrk eqlrvdaler tleqknkeie
     1021 eltkicdeli akmgks
//
LOCUS       NP_036390                304 aa            linear   PRI 27-APR-2025
DEFINITION  hairy/enhancer-of-split related with YRPW motif protein 1 isoform a
            [Homo sapiens].
ACCESSION   NP_036390
VERSION     NP_036390.3
DBSOURCE    REFSEQ: accession NM_012258.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Ren,R., Ding,S., Ma,K., Jiang,Y., Wang,Y., Chen,J., Wang,Y.,
            Kou,Y., Fan,X., Zhu,X., Qin,L., Qiu,C., Simons,M., Wei,X. and Yu,L.
  TITLE     SUMOylation Fine-Tunes Endothelial HEY1 in the Regulation of
            Angiogenesis
  JOURNAL   Circ Res 134 (2), 203-222 (2024)
   PUBMED   38166414
  REMARK    GeneRIF: SUMOylation Fine-Tunes Endothelial HEY1 in the Regulation
            of Angiogenesis.
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Gao,J., Li,Y., Zou,X., Lei,T., Xu,T., Chen,Y. and Wang,Z.
  TITLE     HEY1-mediated cisplatin resistance in lung adenocarcinoma via
            epithelial-mesenchymal transition
  JOURNAL   Med Oncol 40 (1), 18 (2022)
   PUBMED   36396748
  REMARK    GeneRIF: HEY1-mediated cisplatin resistance in lung adenocarcinoma
            via epithelial-mesenchymal transition.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Wang,G., Li,H. and Hou,Y.
  TITLE     LncRNA MAGI2-AS3 inhibits tumor progression and angiogenesis by
            regulating ACY1 via interacting with transcription factor HEY1 in
            clear cell renal cell carcinoma
  JOURNAL   Cancer Gene Ther 29 (5), 585-596 (2022)
   PUBMED   34002044
  REMARK    GeneRIF: LncRNA MAGI2-AS3 inhibits tumor progression and
            angiogenesis by regulating ACY1 via interacting with transcription
            factor HEY1 in clear cell renal cell carcinoma.
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Maier,M.M. and Gessler,M.
  TITLE     Comparative analysis of the human and mouse Hey1 promoter: Hey
            genes are new Notch target genes
  JOURNAL   Biochem Biophys Res Commun 275 (2), 652-660 (2000)
   PUBMED   10964718
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Steidl,C., Leimeister,C., Klamt,B., Maier,M., Nanda,I., Dixon,M.,
            Clarke,R., Schmid,M. and Gessler,M.
  TITLE     Characterization of the human and mouse HEY1, HEY2, and HEYL genes:
            cloning, mapping, and mutation screening of a new bHLH gene family
  JOURNAL   Genomics 66 (2), 195-203 (2000)
   PUBMED   10860664
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Chin,M.T., Maemura,K., Fukumoto,S., Jain,M.K., Layne,M.D.,
            Watanabe,M., Hsieh,C.M. and Lee,M.E.
  TITLE     Cardiovascular basic helix loop helix factor 1, a novel
            transcriptional repressor expressed preferentially in the
            developing and adult cardiovascular system
  JOURNAL   J Biol Chem 275 (9), 6381-6387 (2000)
   PUBMED   10692439
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Kokubo,H., Lun,Y. and Johnson,R.L.
  TITLE     Identification and expression of a novel family of bHLH cDNAs
            related to Drosophila hairy and enhancer of split
  JOURNAL   Biochem Biophys Res Commun 260 (2), 459-465 (1999)
   PUBMED   10403790
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Leimeister,C., Externbrink,A., Klamt,B. and Gessler,M.
  TITLE     Hey genes: a novel subfamily of hairy- and Enhancer of split
            related genes specifically expressed during mouse embryogenesis
  JOURNAL   Mech Dev 85 (1-2), 173-177 (1999)
   PUBMED   10415358
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA561783.1, BC001873.1 and
            AF232239.1.
            
            On Jun 1, 2006 this sequence version replaced NP_036390.2.
            
            Summary: This gene encodes a nuclear protein belonging to the hairy
            and enhancer of split-related (HESR) family of basic
            helix-loop-helix (bHLH)-type transcriptional repressors. Expression
            of this gene is induced by the Notch and c-Jun signal transduction
            pathways. Two similar and redundant genes in mouse are required for
            embryonic cardiovascular development, and are also implicated in
            neurogenesis and somitogenesis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK226041.1, SRR1803613.170156.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMN03267763
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354724.8/ ENSP00000346761.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.13"
     Protein         1..304
                     /product="hairy/enhancer-of-split related with YRPW motif
                     protein 1 isoform a"
                     /note="HES-related repressor protein 2; cardiovascular
                     helix-loop-helix factor 2; hairy-related transcription
                     factor 1; basic helix-loop-helix protein OAF1;
                     hairy/enhancer-of-split related with YRPW motif protein 1;
                     HES-related repressor protein 1; class B basic
                     helix-loop-helix protein 31; hairy and enhancer of
                     split-related protein 1; hairy/enhancer-of-split related
                     with YRPW motif 1"
                     /calculated_mol_wt=32482
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5J3.1)"
     Region          41..122
                     /region_name="bHLH_SF"
                     /note="basic Helix Loop Helix (bHLH) domain superfamily;
                     cl00081"
                     /db_xref="CDD:469605"
     Region          48..117
                     /region_name="Transcriptional repression and interaction
                     with NCOR1 and SIN3A. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5J3.1)"
     Site            order(58..59,61,66,89..90)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381392"
     Site            order(64..65,68..69,71..72,76,90..91,94..95,98,100..101,
                     104..105)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381392"
     Region          120..166
                     /region_name="ORANGE"
                     /note="Orange domain; smart00511"
                     /db_xref="CDD:128787"
     Region          196..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5J3.1)"
     Region          294..297
                     /region_name="YRPW motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5J3.1)"
     CDS             1..304
                     /gene="HEY1"
                     /gene_synonym="BHLHb31; CHF2; HERP2; HESR1; hHRT1; HRT-1;
                     NERP2; OAF1"
                     /coded_by="NM_012258.4:105..1019"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6225.1"
                     /db_xref="GeneID:23462"
                     /db_xref="HGNC:HGNC:4880"
                     /db_xref="MIM:602953"
ORIGIN      
        1 mkrahpeyss sdseldetie vekesadeng nlssalgsms pttssqilar krrrgiiekr
       61 rrdrinnsls elrrlvpsaf ekqgsaklek aeilqmtvdh lkmlhtaggk gyfdahalam
      121 dyrslgfrec laevarylsi iegldasdpl rvrlvshlnn yasqreaasg ahaglghipw
      181 gtvfghhphi ahplllpqng hgnagttasp tephhqgrlg sahpeapalr appsgslgpv
      241 lpvvtsaskl sppllssvas lsafpfsfgs fhllspnals psaptqaanl gkpyrpwgte
      301 igaf
//
LOCUS       NP_076870                591 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor COE1 isoform 2 [Homo sapiens].
ACCESSION   NP_076870
VERSION     NP_076870.1
DBSOURCE    REFSEQ: accession NM_024007.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Mladenic,T., Wagner,J., Kadivnik,M., Pereza,N., Ostojic,S.,
            Peterlin,B. and Devic Pavlic,S.
  TITLE     Protective Effect of EBF Transcription Factor 1 (EBF1) Polymorphism
            in Sporadic and Familial Spontaneous Preterm Birth: Insights from a
            Case-Control Study
  JOURNAL   Int J Mol Sci 25 (20), 11192 (2024)
   PUBMED   39456973
  REMARK    GeneRIF: Protective Effect of EBF Transcription Factor 1 (EBF1)
            Polymorphism in Sporadic and Familial Spontaneous Preterm Birth:
            Insights from a Case-Control Study.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Wu,Y., Chen,S., Huang,G., Zhang,L., Zhong,L., Feng,Y., Wen,P. and
            Liu,J.
  TITLE     Transcriptome analysis reveals EBF1 ablation-induced injuries in
            cardiac system
  JOURNAL   Theranostics 14 (12), 4894-4915 (2024)
   PUBMED   39239522
  REMARK    GeneRIF: Transcriptome analysis reveals EBF1 ablation-induced
            injuries in cardiac system.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Li,L., Zhang,D. and Cao,X.
  TITLE     EBF1, PAX5, and MYC: regulation on B cell development and
            association with hematologic neoplasms
  JOURNAL   Front Immunol 15, 1320689 (2024)
   PUBMED   38318177
  REMARK    GeneRIF: EBF1, PAX5, and MYC: regulation on B cell development and
            association with hematologic neoplasms.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Liu,Y., Fan,M., Xian,S., Hu,P., Zhang,M., Zhang,X., Zhang,H.,
            Zhang,J., Dai,L., Lin,M., Mei,W., Huang,D., Huang,R., Zhang,J. and
            Huang,Z.
  TITLE     RBP7 Regulated by EBF1 Affects Th2 Cells and the Oocyte Meiosis
            Pathway in Bone Metastases of Bladder Urothelial Carcinoma
  JOURNAL   Front Biosci (Landmark Ed) 28 (8), 189 (2023)
   PUBMED   37664915
  REMARK    GeneRIF: RBP7 Regulated by EBF1 Affects Th2 Cells and the Oocyte
            Meiosis Pathway in Bone Metastases of Bladder Urothelial Carcinoma.
REFERENCE   5  (residues 1 to 591)
  AUTHORS   Al Madhoun,A., Haddad,D., Nizam,R., Miranda,L., Kochumon,S.,
            Thomas,R., Thanaraj,T.A., Ahmad,R., Bitar,M.S. and Al-Mulla,F.
  TITLE     Caveolin-1 rs1997623 Single Nucleotide Polymorphism Creates a New
            Binding Site for the Early B-Cell Factor 1 That Instigates Adipose
            Tissue CAV1 Protein Overexpression
  JOURNAL   Cells 11 (23), 3937 (2022)
   PUBMED   36497195
  REMARK    GeneRIF: Caveolin-1 rs1997623 Single Nucleotide Polymorphism
            Creates a New Binding Site for the Early B-Cell Factor 1 That
            Instigates Adipose Tissue CAV1 Protein Overexpression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 591)
  AUTHORS   Tsai,R.Y. and Reed,R.R.
  TITLE     Cloning and functional characterization of Roaz, a zinc finger
            protein that interacts with O/E-1 to regulate gene expression:
            implications for olfactory neuronal development
  JOURNAL   J Neurosci 17 (11), 4159-4169 (1997)
   PUBMED   9151733
REFERENCE   7  (residues 1 to 591)
  AUTHORS   Hagman,J., Gutch,M.J., Lin,H. and Grosschedl,R.
  TITLE     EBF contains a novel zinc coordination motif and multiple
            dimerization and transcriptional activation domains
  JOURNAL   EMBO J 14 (12), 2907-2916 (1995)
   PUBMED   7796816
REFERENCE   8  (residues 1 to 591)
  AUTHORS   Milatovich,A., Qiu,R.G., Grosschedl,R. and Francke,U.
  TITLE     Gene for a tissue-specific transcriptional activator (EBF or
            Olf-1), expressed in early B lymphocytes, adipocytes, and olfactory
            neurons, is located on human chromosome 5, band q34, and proximal
            mouse chromosome 11
  JOURNAL   Mamm Genome 5 (4), 211-215 (1994)
   PUBMED   8012110
REFERENCE   9  (residues 1 to 591)
  AUTHORS   Travis,A., Hagman,J., Hwang,L. and Grosschedl,R.
  TITLE     Purification of early-B-cell factor and characterization of its
            DNA-binding specificity
  JOURNAL   Mol Cell Biol 13 (6), 3392-3400 (1993)
   PUBMED   8497258
REFERENCE   10 (residues 1 to 591)
  AUTHORS   Hagman,J., Belanger,C., Travis,A., Turck,C.W. and Grosschedl,R.
  TITLE     Cloning and functional characterization of early B-cell factor, a
            regulator of lymphocyte-specific gene expression
  JOURNAL   Genes Dev 7 (5), 760-773 (1993)
   PUBMED   8491377
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC134043.1, DA485473.1, BC038805.1, AC008442.6 and BM802733.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction at the 5' end of an exon compared to variant 1. The
            resulting isoform (2) has the same N- and C-termini but is one aa
            shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.169524.1, BC038805.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313708.11/ ENSP00000322898.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..591
                     /product="transcription factor COE1 isoform 2"
                     /note="olfactory neuronal transcription factor 1; early B
                     cell factor 1; Collier, Olf and EBF transcription factor
                     1; transcription factor COE1"
                     /calculated_mol_wt=64333
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH73.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UH73.2)"
     Region          21..247
                     /region_name="COE1_DBD"
                     /note="Transcription factor COE1 DNA-binding domain;
                     pfam16422"
                     /db_xref="CDD:435333"
     Site            order(63..67,157,160..163,169..172,174,197,199,201..205,
                     233,235..240)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212156"
     Region          63..66
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:Q07802"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH73.2)"
     Site            163
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:Q07802; propagated from
                     UniProtKB/Swiss-Prot (Q9UH73.2)"
     Site            172
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:Q07802; propagated from
                     UniProtKB/Swiss-Prot (Q9UH73.2)"
     Region          197..204
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:Q07802"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH73.2)"
     Region          236..239
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:Q07802"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH73.2)"
     Region          262..346
                     /region_name="IPT_COE"
                     /note="IPT domain of the COE family (Col/Olf-1/EBF) of
                     non-basic, helix-loop-helix (HLH)-containing transcription
                     factors. COE family proteins are all transcription factors
                     and play an important role in variety of developmental
                     processes. Mouse EBF is involved...; cd01175"
                     /db_xref="CDD:238580"
     Region          347..390
                     /region_name="COE1_HLH"
                     /note="Transcription factor COE1 helix-loop-helix domain;
                     pfam16423"
                     /db_xref="CDD:406751"
     Region          457..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH73.2)"
     CDS             1..591
                     /gene="EBF1"
                     /gene_synonym="COE1; EBF; O/E-1; OLF1"
                     /coded_by="NM_024007.5:439..2214"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4343.1"
                     /db_xref="GeneID:1879"
                     /db_xref="HGNC:HGNC:3126"
                     /db_xref="MIM:164343"
ORIGIN      
        1 mfgiqesiqr sgssmkeepl gsgmnavrtw mqgagvldan taaqsgvgla rahfekqpps
       61 nlrksnffhf vlalydrqgq pveiertafv gfvekekean sektnngihy rlqllysngi
      121 rteqdfyvrl idsmtkqaiv yegqdknpem crvlltheim csrccdkksc gnrnetpsdp
      181 viidrfflkf flkcnqnclk nagnprdmrr fqvvvsttvn vdghvlavsd nmfvhnnskh
      241 grrarrldps egtpsyleha tpcikaisps egwttggatv iiigdnffdg lqvifgtmlv
      301 wselitphai rvqtpprhip gvvevtlsyk skqfckgtpg rfiytalnep tidygfqrlq
      361 kviprhpgdp erlpkevilk raadlvealy gmphnnqeii lkraadiaea lysvprnhnq
      421 lpalantsvh agmmgvnsfs gqlavnvsea sqatnqgftr nsssvsphgy vpsttpqqtn
      481 ynsvttsmng ygsaamsnlg gsptflngsa anspyaivps sptmasstsl psncssssgi
      541 fsfspanmvs avkqksafap vvrpqtsppp tctstngnsl qaisgmivpp m
//
LOCUS       NP_065851                777 aa            linear   PRI 27-APR-2025
DEFINITION  intraflagellar transport protein 80 homolog isoform a [Homo
            sapiens].
ACCESSION   NP_065851
VERSION     NP_065851.1
DBSOURCE    REFSEQ: accession NM_020800.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Bizaoui,V., Huber,C., Kohaut,E., Roume,J., Bonniere,M.,
            Attie-Bitach,T. and Cormier-Daire,V.
  TITLE     Mutations in IFT80 cause SRPS Type IV. Report of two families and
            review
  JOURNAL   Am J Med Genet A 179 (4), 639-644 (2019)
   PUBMED   30767363
  REMARK    GeneRIF: Mutations in IFT80 cause Short rib-polydactyly syndrome,
            Beemer type.
REFERENCE   2  (residues 1 to 777)
  AUTHORS   Wang,R., Deng,X., Yuan,C., Xin,H., Liu,G., Zhu,Y., Jiang,X. and
            Wang,C.
  TITLE     IFT80 Improves Invasion Ability in Gastric Cancer Cell Line via
            ift80/p75NGFR/MMP9 Signaling
  JOURNAL   Int J Mol Sci 19 (11), 3616 (2018)
   PUBMED   30453504
  REMARK    GeneRIF: IFT80 plays an important role in invasion of gastric
            cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 777)
  AUTHORS   Katoh,Y., Terada,M., Nishijima,Y., Takei,R., Nozaki,S., Hamada,H.
            and Nakayama,K.
  TITLE     Overall Architecture of the Intraflagellar Transport (IFT)-B
            Complex Containing Cluap1/IFT38 as an Essential Component of the
            IFT-B Peripheral Subcomplex
  JOURNAL   J Biol Chem 291 (21), 10962-10975 (2016)
   PUBMED   26980730
REFERENCE   4  (residues 1 to 777)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 777)
  AUTHORS   Cavalcanti,D.P., Huber,C., Sang,K.H., Baujat,G., Collins,F.,
            Delezoide,A.L., Dagoneau,N., Le Merrer,M., Martinovic,J.,
            Mello,M.F., Vekemans,M., Munnich,A. and Cormier-Daire,V.
  TITLE     Mutation in IFT80 in a fetus with the phenotype of Verma-Naumoff
            provides molecular evidence for Jeune-Verma-Naumoff dysplasia
            spectrum
  JOURNAL   J Med Genet 48 (2), 88-92 (2011)
   PUBMED   19648123
  REMARK    GeneRIF: Mutations in IFT80 can be responsible for a lethal form of
            short-rib polydactyly and provide the molecular basis for the
            Jeune-Verma-Naumoff dysplasia spectrum.
REFERENCE   6  (residues 1 to 777)
  AUTHORS   Huang,W., Kane,J.K. and Li,M.D.
  TITLE     Identification and characterization of a long isoform of human
            IFT80, IFT80-L
  JOURNAL   Biochem Biophys Res Commun 373 (4), 653-658 (2008)
   PUBMED   18601909
  REMARK    GeneRIF: Identification and characterization of a human IFT80 long
            isoform (namely IFT80-L), the carboxyl terminus of which shares the
            protein sequence of IFT80, is reported.
REFERENCE   7  (residues 1 to 777)
  AUTHORS   Beales,P.L., Bland,E., Tobin,J.L., Bacchelli,C., Tuysuz,B.,
            Hill,J., Rix,S., Pearson,C.G., Kai,M., Hartley,J., Johnson,C.,
            Irving,M., Elcioglu,N., Winey,M., Tada,M. and Scambler,P.J.
  TITLE     IFT80, which encodes a conserved intraflagellar transport protein,
            is mutated in Jeune asphyxiating thoracic dystrophy
  JOURNAL   Nat Genet 39 (6), 727-729 (2007)
   PUBMED   17468754
  REMARK    GeneRIF: Mutations in IFT80 is associated with Jeune asphyxiating
            thoracic dystrophy
REFERENCE   8  (residues 1 to 777)
  AUTHORS   Muzny,D.M., Scherer,S.E., Kaul,R., Wang,J., Yu,J., Sudbrak,R.,
            Buhay,C.J., Chen,R., Cree,A., Ding,Y., Dugan-Rocha,S., Gill,R.,
            Gunaratne,P., Harris,R.A., Hawes,A.C., Hernandez,J., Hodgson,A.V.,
            Hume,J., Jackson,A., Khan,Z.M., Kovar-Smith,C., Lewis,L.R.,
            Lozado,R.J., Metzker,M.L., Milosavljevic,A., Miner,G.R.,
            Morgan,M.B., Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z.,
            Steffen,D., Wei,S., Wheeler,D.A., Wright,M.W., Worley,K.C.,
            Yuan,Y., Zhang,Z., Adams,C.Q., Ansari-Lari,M.A., Ayele,M.,
            Brown,M.J., Chen,G., Chen,Z., Clendenning,J.,
            Clerc-Blankenburg,K.P., Chen,R., Chen,Z., Davis,C., Delgado,O.,
            Dinh,H.H., Dong,W., Draper,H., Ernst,S., Fu,G.,
            Gonzalez-Garay,M.L., Garcia,D.K., Gillett,W., Gu,J., Hao,B.,
            Haugen,E., Havlak,P., He,X., Hennig,S., Hu,S., Huang,W.,
            Jackson,L.R., Jacob,L.S., Kelly,S.H., Kube,M., Levy,R., Li,Z.,
            Liu,B., Liu,J., Liu,W., Lu,J., Maheshwari,M., Nguyen,B.V.,
            Okwuonu,G.O., Palmeiri,A., Pasternak,S., Perez,L.M., Phelps,K.A.,
            Plopper,F.J., Qiang,B., Raymond,C., Rodriguez,R.,
            Saenphimmachak,C., Santibanez,J., Shen,H., Shen,Y., Subramanian,S.,
            Tabor,P.E., Verduzco,D., Waldron,L., Wang,J., Wang,J., Wang,Q.,
            Williams,G.A., Wong,G.K., Yao,Z., Zhang,J., Zhang,X., Zhao,G.,
            Zhou,J., Zhou,Y., Nelson,D., Lehrach,H., Reinhardt,R., Naylor,S.L.,
            Yang,H., Olson,M., Weinstock,G. and Gibbs,R.A.
  TITLE     The DNA sequence, annotation and analysis of human chromosome 3
  JOURNAL   Nature 440 (7088), 1194-1198 (2006)
   PUBMED   16641997
REFERENCE   9  (residues 1 to 777)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 777)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK125342.1, AB037795.1 and
            CA421514.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is part of the
            intraflagellar transport complex B and is necessary for the
            function of motile and sensory cilia. Defects in this gene are a
            cause of asphyxiating thoracic dystrophy 2 (ATD2). Three transcript
            variants encoding two different isoforms have been found for this
            gene.[provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.83383.1,
                                           SRR1803616.40152.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326448.12/ ENSP00000312778.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.33"
     Protein         1..777
                     /product="intraflagellar transport protein 80 homolog
                     isoform a"
                     /note="WD repeat domain 56; WD repeat-containing protein
                     56; intraflagellar transport 80 homolog"
                     /calculated_mol_wt=87904
     Region          12..50
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          17..62
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <28..293
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          104..143
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          110..145
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          145..185
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          150..183
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          186..225
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          192..225
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          227..265
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          232..265
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..306
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          504..542
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          758..777
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     CDS             1..777
                     /gene="IFT80"
                     /gene_synonym="ATD2; CFAP167; FAP167; SRTD2; WDR56"
                     /coded_by="NM_020800.3:127..2460"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3188.1"
                     /db_xref="GeneID:57560"
                     /db_xref="HGNC:HGNC:29262"
                     /db_xref="MIM:611177"
ORIGIN      
        1 mrlkisllke pkhqelvscv gwttaeelys csddhqivkw nlltsettqi vklpddiypi
       61 dfhwfpkslg vkkqtqaesf vltssdgkfh lisklgrvek sveahcgavl agrwnyegta
      121 lvtvgedgqi kiwsktgmlr stlaqqgtpv ysvawgpdse kvlytagkql iikplqpnak
      181 vlqwkahdgi ilkvdwnsvn dlilsagedc kykvwdsygr plynsqpheh pitsvawapd
      241 gelfavgsfh tlrlcdktgw syalekpntg sifniawsid gtqiagacgn ghvvfahvve
      301 qhwewknfqv tltkrramqv rnvlndavdl lefrdrvika slnyahlvvs tslqcyvfst
      361 knwntpiifd lkegtvslil qaerhfllvd gssiylysye grfisspkfp gmrtdilnaq
      421 tvslsndtia irdkadekii flfeastgkp lgdgkflshk neileialdq kgltndrkia
      481 fidknrdlci tsvkrfgkee qiiklgtmvh tlawndtcni lcglqdtrfi vwyypntvyv
      541 drdilpktly erdasefskn phivsfvgnq vtirradgsl vhisitpypa ilheyvsssk
      601 wedavrlcrf vkeqtmwacl aamavanrdm ttaeiayaai geidkvqyin siknlpskes
      661 kmahillfsg niqeaeivll qaglvyqaiq ininlynwer alelavkykt hvdtvlayrq
      721 kfletfgkqe tnkrylhyae glqidwekik akiemeitke reqssssqss ksiglkp
//
LOCUS       NP_002970                547 aa            linear   PRI 27-APR-2025
DEFINITION  sterol carrier protein 2 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_002970
VERSION     NP_002970.2
DBSOURCE    REFSEQ: accession NM_002979.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Zou,J., Pei,X., Xing,D., Wu,X. and Chen,S.
  TITLE     LINC00261 elevation inhibits angiogenesis and cell cycle
            progression of pancreatic cancer cells by upregulating SCP2 via
            targeting FOXP3
  JOURNAL   J Cell Mol Med 25 (20), 9826-9836 (2021)
   PUBMED   34541823
  REMARK    GeneRIF: LINC00261 elevation inhibits angiogenesis and cell cycle
            progression of pancreatic cancer cells by upregulating SCP2 via
            targeting FOXP3.
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Bai,L., Li,J., Panagal,M., M,B. and Sekar,D.
  TITLE     Methylation dependent microRNA 1285-5p and sterol carrier proteins
            2 in type 2 diabetes mellitus
  JOURNAL   Artif Cells Nanomed Biotechnol 47 (1), 3417-3422 (2019)
   PUBMED   31407919
  REMARK    GeneRIF: Methylation dependent microRNA 1285-5p and sterol carrier
            proteins 2 in type 2 diabetes mellitus
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Dansen,T.B., Kops,G.J., Denis,S., Jelluma,N., Wanders,R.J.,
            Bos,J.L., Burgering,B.M. and Wirtz,K.W.
  TITLE     Regulation of sterol carrier protein gene expression by the
            forkhead transcription factor FOXO3a
  JOURNAL   J Lipid Res 45 (1), 81-88 (2004)
   PUBMED   14563822
  REMARK    GeneRIF: SCP2 in the cellular defense against oxidative damage and
            found that a fluorescent fatty acid analog bound to SCP2 is
            protected against H2O2/Cu2+-induced oxidative damage
REFERENCE   5  (residues 1 to 547)
  AUTHORS   Ohba,T., Holt,J.A., Billheimer,J.T. and Strauss,J.F. 3rd.
  TITLE     Human sterol carrier protein x/sterol carrier protein 2 gene has
            two promoters
  JOURNAL   Biochemistry 34 (33), 10660-10668 (1995)
   PUBMED   7654720
REFERENCE   6  (residues 1 to 547)
  AUTHORS   Ohba,T., Rennert,H., Pfeifer,S.M., He,Z., Yamamoto,R., Holt,J.A.,
            Billheimer,J.T. and Strauss,J.F. 3rd.
  TITLE     The structure of the human sterol carrier protein X/sterol carrier
            protein 2 gene (SCP2)
  JOURNAL   Genomics 24 (2), 370-374 (1994)
   PUBMED   7698762
REFERENCE   7  (residues 1 to 547)
  AUTHORS   Seedorf,U., Brysch,P., Engel,T., Schrage,K. and Assmann,G.
  TITLE     Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A
            thiolase with intrinsic sterol carrier and lipid transfer activity
  JOURNAL   J Biol Chem 269 (33), 21277-21283 (1994)
   PUBMED   8063752
REFERENCE   8  (residues 1 to 547)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   9  (residues 1 to 547)
  AUTHORS   Heikoop,J.C., Ossendorp,B.C., Wanders,R.J., Wirtz,K.W. and
            Tager,J.M.
  TITLE     Subcellular localisation and processing of non-specific lipid
            transfer protein are not aberrant in Rhizomelic Chondrodysplasia
            Punctata fibroblasts
  JOURNAL   FEBS Lett 299 (2), 201-204 (1992)
   PUBMED   1347505
REFERENCE   10 (residues 1 to 547)
  AUTHORS   Yamamoto,R., Kallen,C.B., Babalola,G.O., Rennert,H.,
            Billheimer,J.T. and Strauss,J.F. 3rd.
  TITLE     Cloning and expression of a cDNA encoding human sterol carrier
            protein 2
  JOURNAL   Proc Natl Acad Sci U S A 88 (2), 463-467 (1991)
   PUBMED   1703300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC330171.1, AK312856.1,
            AL445183.19, AB208789.1 and AA664009.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_002970.1.
            
            Summary: This gene encodes two proteins: sterol carrier protein X
            (SCPx) and sterol carrier protein 2 (SCP2), as a result of
            transcription initiation from 2 independently regulated promoters.
            The transcript initiated from the proximal promoter encodes the
            longer SCPx protein, and the transcript initiated from the distal
            promoter encodes the shorter SCP2 protein, with the 2 proteins
            sharing a common C-terminus. Evidence suggests that the SCPx
            protein is a peroxisome-associated thiolase that is involved in the
            oxidation of branched chain fatty acids, while the SCP2 protein is
            thought to be an intracellular lipid transfer protein. This gene is
            highly expressed in organs involved in lipid metabolism, and may
            play a role in Zellweger syndrome, in which cells are deficient in
            peroxisomes and have impaired bile acid synthesis. Alternative
            splicing of this gene produces multiple transcript variants, some
            encoding different isoforms.[provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1, also known as SCPx).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.18490.1,
                                           SRR3476690.1001248.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371514.8/ ENSP00000360569.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..547
                     /product="sterol carrier protein 2 isoform 1 precursor"
                     /EC_number="2.3.1.16"
                     /EC_number="2.3.1.176"
                     /EC_number="2.3.1.155"
                     /note="sterol carrier protein X; non-specific
                     lipid-transfer protein; propanoyl-CoA C-acyltransferase;
                     epididymis secretory sperm binding protein;
                     SCP-2/thiolase; SCP-2/3-oxoacyl-CoA thiolase;
                     straight-chain acyl-CoA oxidase; acetyl-CoA
                     C-myristoyltransferase"
                     /calculated_mol_wt=58863
     mat_peptide     1..404
                     /product="sterol carrier protein 2 isoform 1"
                     /experiment="EXISTENCE:western blot[PMID:14563822]"
                     /calculated_mol_wt=43611
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11915; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Region          12..404
                     /region_name="PRK08256"
                     /note="lipid-transfer protein; Provisional"
                     /db_xref="CDD:181327"
     Site            20..21
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            132
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P32020; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P32020; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            177
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P32020; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            183
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P32020; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            432
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P32020; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            438
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            443
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P32020; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Region          452..538
                     /region_name="SCP2"
                     /note="SCP-2 sterol transfer family; pfam02036"
                     /db_xref="CDD:460423"
     Site            453
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P32020; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            470
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            491
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P32020; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P32020; propagated from
                     UniProtKB/Swiss-Prot (P22307.2)"
     Region          545..547
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P22307.2)"
     CDS             1..547
                     /gene="SCP2"
                     /gene_synonym="NLTP; NSL-TP; SCOX; SCP-2; SCP-CHI; SCP-X;
                     SCPX"
                     /coded_by="NM_002979.5:122..1765"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS572.1"
                     /db_xref="GeneID:6342"
                     /db_xref="HGNC:HGNC:10606"
                     /db_xref="MIM:184755"
ORIGIN      
        1 mssspwepat lrrvfvvgvg mtkfvkpgae nsrdypdlae eagkkalada qipysavdqa
       61 cvgyvfgdst cgqraiyhsl gmtgipiinv nnncatgsta lfmarqliqg gvaecvlalg
      121 fekmskgslg ikfsdrtipt dkhvdllink yglsahpvap qmfgyagkeh mekygtkieh
      181 fakigwknhk hsvnnpysqf qdeysldevm askevfdflt ilqccptsdg aaaailasea
      241 fvqkyglqsk aveilaqemm tdlpssfeek siikmvgfdm skeaarkcye ksgltpndid
      301 vielhdcfst nelltyealg lcpegqgatl vdrgdntygg kwvinpsggl iskghplgat
      361 glaqcaelcw qlrgeagkrq vpgakvalqh nlgiggavvv tlykmgfpea assfrthqie
      421 avptssasdg fkanlvfkei ekkleeegeq fvkkiggifa fkvkdgpggk eatwvvdvkn
      481 gkgsvlpnsd kkadctitma dsdflalmtg kmnpqsaffq gklkitgnmg lamklqnlql
      541 qpgnakl
//
LOCUS       NP_001182470             221 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 225B [Homo sapiens].
ACCESSION   NP_001182470 XP_002342783 XP_002344413 XP_002346060 XP_002346946
VERSION     NP_001182470.1
DBSOURCE    REFSEQ: accession NM_001195541.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Polasek,O., Marusic,A., Rotim,K., Hayward,C., Vitart,V.,
            Huffman,J., Campbell,S., Jankovic,S., Boban,M., Biloglav,Z.,
            Kolcic,I., Krzelj,V., Terzic,J., Matec,L., Tometic,G., Nonkovic,D.,
            Nincevic,J., Pehlic,M., Zedelj,J., Velagic,V., Juricic,D.,
            Kirac,I., Belak Kovacevic,S., Wright,A.F., Campbell,H. and Rudan,I.
  TITLE     Genome-wide association study of anthropometric traits in Korcula
            Island, Croatia
  JOURNAL   Croat Med J 50 (1), 7-16 (2009)
   PUBMED   19260139
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB477974.1, DB462723.1, AA781117.1 and HY200726.1.
            
            On or before Sep 16, 2010 this sequence version replaced
            XP_002342783.1, XP_002346946.1, XP_002346060.1, XP_002344413.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1-3 all encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.29651.1,
                                           SRR5189667.333299.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000431679.6/ ENSP00000492416.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..221
                     /product="transmembrane protein 225B"
                     /note="transmembrane protein 225-like"
                     /calculated_mol_wt=24896
     Site            14..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     Site            109..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     CDS             1..221
                     /gene="TMEM225B"
                     /gene_synonym="GS1-259H13.2"
                     /coded_by="NM_001195541.3:200..865"
                     /db_xref="CCDS:CCDS87525.1"
                     /db_xref="GeneID:100289187"
                     /db_xref="HGNC:HGNC:53075"
ORIGIN      
        1 mltledkdmk gfswaivpal tslgyliilv vsifpfwvrl tneeshevff sglfencfna
       61 kcwkprplsi yiilgrvfll savflafvtt fimmpfasef fprtwkqnfv lacisfftga
      121 caflalvlha leikalrmkl gplqfsvlwp yyvlgfgifl fivagticli qemvcpcwhl
      181 lstsqsmeed hgslyldnle slggepssvq ketqvtaetv i
//
LOCUS       NP_116200                411 aa            linear   PRI 27-APR-2025
DEFINITION  transforming growth factor beta regulator 1 [Homo sapiens].
ACCESSION   NP_116200
VERSION     NP_116200.2
DBSOURCE    REFSEQ: accession NM_032811.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Slezak-Prochazka,I., Kluiver,J., de Jong,D., Smigielska-Czepiel,K.,
            Kortman,G., Winkle,M., Rutgers,B., Koerts,J., Visser,L.,
            Diepstra,A., Kroesen,B.J. and van den Berg,A.
  TITLE     Inhibition of the miR-155 target NIAM phenocopies the growth
            promoting effect of miR-155 in B-cell lymphoma
  JOURNAL   Oncotarget 7 (3), 2391-2400 (2016)
   PUBMED   26497687
  REMARK    GeneRIF: In primary B-cell lymphoma NIAM-positive cases have
            significant lower levels of miR-155 as compared to NIAM-negative
            cases, suggesting that NIAM is regulated by miR-155 in primary
            B-cell lymphoma.
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Reed,S.M., Hagen,J., Tompkins,V.S., Thies,K., Quelle,F.W. and
            Quelle,D.E.
  TITLE     Nuclear interactor of ARF and Mdm2 regulates multiple pathways to
            activate p53
  JOURNAL   Cell Cycle 13 (8), 1288-1298 (2014)
   PUBMED   24621507
  REMARK    GeneRIF: NIAM regulates 2 critical pathways that control p53
            function and are altered in human cancers, implying an important
            role for NIAM in tumorigenesis.
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Hagen,J., Tompkins,V., Dudakovic,A., Weydert,J.A. and Quelle,D.E.
  TITLE     Generation and characterization of monoclonal antibodies to NIAM: a
            nuclear interactor of ARF and Mdm2
  JOURNAL   Hybridoma (Larchmt) 27 (3), 159-166 (2008)
   PUBMED   18582208
  REMARK    GeneRIF: NIAM is a nuclear interactor of ARF and Mdm2
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Tompkins,V.S., Hagen,J., Frazier,A.A., Lushnikova,T.,
            Fitzgerald,M.P., di Tommaso,A., Ladeveze,V., Domann,F.E.,
            Eischen,C.M. and Quelle,D.E.
  TITLE     A novel nuclear interactor of ARF and MDM2 (NIAM) that maintains
            chromosomal stability
  JOURNAL   J Biol Chem 282 (2), 1322-1333 (2007)
   PUBMED   17110379
  REMARK    GeneRIF: novel protein with tumor suppressor-like behaviors and
            functional links to ARF-MDM2-p53 signaling
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Tompkins,V., Hagen,J., Zediak,V.P. and Quelle,D.E.
  TITLE     Identification of novel ARF binding proteins by two-hybrid
            screening
  JOURNAL   Cell Cycle 5 (6), 641-646 (2006)
   PUBMED   16582619
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Babalola,G.O. and Schultz,R.M.
  TITLE     Modulation of gene expression in the preimplantation mouse embryo
            by TGF-alpha and TGF-beta
  JOURNAL   Mol Reprod Dev 41 (2), 133-139 (1995)
   PUBMED   7654366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA292015.1, DQ144542.1 and AP001524.4.
            
            On Mar 21, 2008 this sequence version replaced NP_116200.1.
            
            Transcript Variant: This variant (1) represents the longer,
            protein-coding transcript.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.223413.1,
                                           SRR1660805.219109.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000441174.8/ ENSP00000409016.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.2"
     Protein         1..411
                     /product="transforming growth factor beta regulator 1"
                     /note="nuclear interactor of ARF and MDM2"
                     /calculated_mol_wt=44815
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3YBR2.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q3YBR2.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q3YBR2.1)"
     Region          119..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3YBR2.1)"
     Region          188..238
                     /region_name="FYRN"
                     /note="F/Y-rich N-terminus; pfam05964"
                     /db_xref="CDD:461787"
     Region          244..325
                     /region_name="FYRC"
                     /note="F/Y rich C-terminus; pfam05965"
                     /db_xref="CDD:461788"
     CDS             1..411
                     /gene="TBRG1"
                     /gene_synonym="NIAM; TB-5"
                     /coded_by="NM_032811.3:221..1456"
                     /db_xref="CCDS:CCDS8448.2"
                     /db_xref="GeneID:84897"
                     /db_xref="HGNC:HGNC:29551"
                     /db_xref="MIM:610614"
ORIGIN      
        1 mslldglass praplqsska rmkklpkksq nekyrlkylr lrkaakatvf enaaicdeia
       61 rleekflkak eerryllkkl lqlqaltege vqaaapshss slpltygvas svgtiqgagp
      121 isgpstgaee pfgkktkkek kekgkennkl evlkktckkk kmaggarklv qpialdpsgr
      181 pvfpiglggl tvyslgeiit drpgfhdesa iypvgycstr iyasmkcpdq kclytcqikd
      241 ggvqpqfeiv peddpqnaiv sssadachae llrtisttmg klmpnllpag adffgfshpa
      301 ihnliqscpg arkcinyqwv kfdvckpgdg qlpeglpend aamsfeafqr qifdedqndp
      361 llpgsldlpe lqpaafvssy qpmylthepl vdthlqhlks psqgspiqss d
//
LOCUS       NP_060956                377 aa            linear   PRI 27-APR-2025
DEFINITION  histone deacetylase 8 isoform 1 [Homo sapiens].
ACCESSION   NP_060956
VERSION     NP_060956.1
DBSOURCE    REFSEQ: accession NM_018486.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Sang,C., Li,X., Liu,J., Chen,Z., Xia,M., Yu,M. and Yu,W.
  TITLE     Reversible acetylation of HDAC8 regulates cell cycle
  JOURNAL   EMBO Rep 25 (9), 3925-3943 (2024)
   PUBMED   39043961
  REMARK    GeneRIF: Reversible acetylation of HDAC8 regulates cell cycle.
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Wang,L., Bai,X., Zhang,X., Wang,X., Chen,S., Wu,S. and Lin,L.
  TITLE     Activation of HDAC8 Can Suppress the Proliferation of Osteosarcoma
            Cells via TP53 and STAT3/ERK Signaling Pathways
  JOURNAL   Ann Clin Lab Sci 53 (6), 920-930 (2023)
   PUBMED   38182151
  REMARK    GeneRIF: Activation of HDAC8 Can Suppress the Proliferation of
            Osteosarcoma Cells via TP53 and STAT3/ERK Signaling Pathways.
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Vannini,A., Volpari,C., Filocamo,G., Casavola,E.C., Brunetti,M.,
            Renzoni,D., Chakravarty,P., Paolini,C., De Francesco,R.,
            Gallinari,P., Steinkuhler,C. and Di Marco,S.
  TITLE     Crystal structure of a eukaryotic zinc-dependent histone
            deacetylase, human HDAC8, complexed with a hydroxamic acid
            inhibitor
  JOURNAL   Proc Natl Acad Sci U S A 101 (42), 15064-15069 (2004)
   PUBMED   15477595
  REMARK    GeneRIF: crystal structure
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Buggy,J.J., Sideris,M.L., Mak,P., Lorimer,D.D., McIntosh,B. and
            Clark,J.M.
  TITLE     Cloning and characterization of a novel human histone deacetylase,
            HDAC8
  JOURNAL   Biochem J 350 Pt 1 (Pt 1), 199-205 (2000)
   PUBMED   10926844
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Van den Wyngaert,I., de Vries,W., Kremer,A., Neefs,J.,
            Verhasselt,P., Luyten,W.H. and Kass,S.U.
  TITLE     Cloning and characterization of human histone deacetylase 8
  JOURNAL   FEBS Lett 478 (1-2), 77-83 (2000)
   PUBMED   10922473
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Hu,E., Chen,Z., Fredrickson,T., Zhu,Y., Kirkpatrick,R., Zhang,G.F.,
            Johanson,K., Sung,C.M., Liu,R. and Winkler,J.
  TITLE     Cloning and characterization of a novel human class I histone
            deacetylase that functions as a transcription repressor
  JOURNAL   J Biol Chem 275 (20), 15254-15264 (2000)
   PUBMED   10748112
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Deardorff,M.A., Noon,S.E. and Krantz,I.D.
  TITLE     Cornelia de Lange Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301283
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Mulley,J.C., Kerr,B., Stevenson,R. and Lubs,H.
  TITLE     Nomenclature guidelines for X-linked mental retardation
  JOURNAL   Am J Med Genet 43 (1-2), 383-391 (1992)
   PUBMED   1605216
  REMARK    Review article
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Wilson,M., Mulley,J., Gedeon,A., Robinson,H. and Turner,G.
  TITLE     New X-linked syndrome of mental retardation, gynecomastia, and
            obesity is linked to DXS255
  JOURNAL   Am J Med Genet 40 (4), 406-413 (1991)
   PUBMED   1746601
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP229332.1, AJ277724.1 and
            BC050433.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene belongs to class I of the histone deacetylase family. It
            catalyzes the deacetylation of lysine residues in the histone
            N-terminal tails and represses transcription in large multiprotein
            complexes with transcriptional co-repressors. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: A downstream translational start codon is selected
            for this RefSeq based on a strong Kozak signal and transcript
            support. An upstream in-frame start codon is also present but has a
            weaker Kozak signal and sparse transcript support. Use of the
            upstream start codon would result in a protein that is 38 aa longer
            at the N-terminus. Leaky scanning by ribosomes may allow
            translation initiation at the downstream start codon, which is
            supported by 5'RACE experiments described in PubMed: 10922473 and
            encodes a protein with an N-terminus similar to other family
            members.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ277724.1, BC050433.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373573.9/ ENSP00000362674.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..377
                     /product="histone deacetylase 8 isoform 1"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase-like 1; protein deacetylase
                     HDAC8; protein decrotonylase HDAC8"
                     /calculated_mol_wt=41627
     Region          14..324
                     /region_name="Histone deacetylase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BY41.2)"
     Region          16..377
                     /region_name="HDAC8"
                     /note="Histone deacetylase 8 (HDAC8); cd10000"
                     /db_xref="CDD:212524"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15242608; propagated from
                     UniProtKB/Swiss-Prot (Q9BY41.2)"
     Site            order(100..101,141..143,151..152,178,180,208,267,274,304,
                     306)
                     /site_type="active"
                     /db_xref="CDD:212524"
     CDS             1..377
                     /gene="HDAC8"
                     /gene_synonym="CDA07; CDLS5; HD8; HDACL1; KDAC8; MRXS6;
                     RPD3; WTS"
                     /coded_by="NM_018486.3:83..1216"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14420.1"
                     /db_xref="GeneID:55869"
                     /db_xref="HGNC:HGNC:13315"
                     /db_xref="MIM:300269"
ORIGIN      
        1 meepeepads gqslvpvyiy speyvsmcds lakipkrasm vhslieayal hkqmrivkpk
       61 vasmeematf htdaylqhlq kvsqegdddh pdsieyglgy dcpategifd yaaaiggati
      121 taaqclidgm ckvainwsgg whhakkdeas gfcylndavl gilrlrrkfe rilyvdldlh
      181 hgdgvedafs ftskvmtvsl hkfspgffpg tgdvsdvglg kgryysvnvp iqdgiqdeky
      241 yqicesvlke vyqafnpkav vlqlgadtia gdpmcsfnmt pvgigkclky ilqwqlatli
      301 lggggynlan tarcwtyltg vilgktlsse ipdhefftay gpdyvleitp scrpdrneph
      361 riqqilnyik gnlkhvv
//
LOCUS       NP_001001850             294 aa            linear   PRI 27-APR-2025
DEFINITION  syntaxin-19 [Homo sapiens].
ACCESSION   NP_001001850
VERSION     NP_001001850.1
DBSOURCE    REFSEQ: accession NM_001001850.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Weimann,M., Grossmann,A., Woodsmith,J., Ozkan,Z., Birth,P.,
            Meierhofer,D., Benlasfer,N., Valovka,T., Timmermann,B.,
            Wanker,E.E., Sauer,S. and Stelzl,U.
  TITLE     A Y2H-seq approach defines the human protein methyltransferase
            interactome
  JOURNAL   Nat Methods 10 (4), 339-342 (2013)
   PUBMED   23455924
REFERENCE   8  (residues 1 to 294)
  AUTHORS   Gordon,D.E., Bond,L.M., Sahlender,D.A. and Peden,A.A.
  TITLE     A targeted siRNA screen to identify SNAREs required for
            constitutive secretion in mammalian cells
  JOURNAL   Traffic 11 (9), 1191-1204 (2010)
   PUBMED   20545907
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC034696.1, AF461456.1 and AC117474.7.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034696.1, BG674749.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315099.3/ ENSP00000320679.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q11.2"
     Protein         1..294
                     /product="syntaxin-19"
                     /calculated_mol_wt=34193
     Region          49..244
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          212..278
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(240,247,250)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277229"
     Site            243
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277229"
     CDS             1..294
                     /gene="STX19"
                     /coded_by="NM_001001850.3:245..1129"
                     /db_xref="CCDS:CCDS33793.1"
                     /db_xref="GeneID:415117"
                     /db_xref="HGNC:HGNC:19300"
ORIGIN      
        1 mkdrlqelkq rtkeielsrd shvsttetee qgvflqqavi yerepvaerh lheiqklqes
       61 innladnvqk fgqqqkslva smrrfsllkr estitkeiki qaeyinrsln dlvkevkkse
      121 vengpssvvt rilksqhaam frhfqqimfi yndtiaakqe kcktfilrql evagkemsee
      181 dvndmlhqgk wevfnesllt einitkaqls eieqrhkelv nlenqikdlr dlfiqisllv
      241 eeqgesinni emtvnstkey vnntkekfgl avkykkrnpc rvlccwccpc cssk
//
LOCUS       NP_997213                410 aa            linear   PRI 27-APR-2025
DEFINITION  magnesium transporter NIPA3 [Homo sapiens].
ACCESSION   NP_997213
VERSION     NP_997213.1
DBSOURCE    REFSEQ: accession NM_207330.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Zhang,Y., Grant,R.A., Shivakumar,M.K., Zaleski,M., Sofoluke,N.,
            Slotkin,J.R., Williams,M.S. and Lee,M.T.M.
  TITLE     Genome-wide Association Analysis Across 16,956 Patients Identifies
            a Novel Genetic Association Between BMP6, NIPAL1, CNGA1 and
            Spondylosis
  JOURNAL   Spine (Phila Pa 1976) 46 (11), E625-E631 (2021)
   PUBMED   33332786
  REMARK    GeneRIF: Genome-wide Association Analysis Across 16,956 Patients
            Identifies a Novel Genetic Association Between BMP6, NIPAL1, CNGA1
            and Spondylosis.
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Sasahira,T., Nishiguchi,Y., Kurihara-Shimomura,M., Nakashima,C.,
            Kuniyasu,H. and Kirita,T.
  TITLE     NIPA-like domain containing 1 is a novel tumor-promoting factor in
            oral squamous cell carcinoma
  JOURNAL   J Cancer Res Clin Oncol 144 (5), 875-882 (2018)
   PUBMED   29464350
  REMARK    GeneRIF: Findings suggest that NIPA like domain containing 1
            (NIPAL1) might be a novel factor promoting oral squamous cell
            carcinoma (OSCC) tumorigenesis, as well as a useful molecular
            marker of OSCC.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Nakayama,A., Nakaoka,H., Yamamoto,K., Sakiyama,M., Shaukat,A.,
            Toyoda,Y., Okada,Y., Kamatani,Y., Nakamura,T., Takada,T., Inoue,K.,
            Yasujima,T., Yuasa,H., Shirahama,Y., Nakashima,H., Shimizu,S.,
            Higashino,T., Kawamura,Y., Ogata,H., Kawaguchi,M., Ohkawa,Y.,
            Danjoh,I., Tokumasu,A., Ooyama,K., Ito,T., Kondo,T., Wakai,K.,
            Stiburkova,B., Pavelka,K., Stamp,L.K., Dalbeth,N., Sakurai,Y.,
            Suzuki,H., Hosoyamada,M., Fujimori,S., Yokoo,T., Hosoya,T.,
            Inoue,I., Takahashi,A., Kubo,M., Ooyama,H., Shimizu,T., Ichida,K.,
            Shinomiya,N., Merriman,T.R. and Matsuo,H.
  CONSRTM   Eurogout Consortium; Eurogout Consortium
  TITLE     GWAS of clinically defined gout and subtypes identifies multiple
            susceptibility loci that include urate transporter genes
  JOURNAL   Ann Rheum Dis 76 (5), 869-877 (2017)
   PUBMED   27899376
  REMARK    GeneRIF: Together with previous reports, our findings support the
            hypothesis that there could be some relationship between gout and
            magnesium handling via magnesium transporters including NIPAL1.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB960388.1, BC067881.1, DA730492.1, DA830885.1, AK095299.1,
            AL832997.1, CR749484.1, AC096749.2 and AK023734.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749484.1, AK095299.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295461.10/ ENSP00000295461.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p12"
     Protein         1..410
                     /product="magnesium transporter NIPA3"
                     /note="NIPA-like protein 1; non-imprinted in
                     Prader-Willi/Angelman syndrome region protein 3"
                     /calculated_mol_wt=44507
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            35
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Region          66..358
                     /region_name="EamA"
                     /note="EamA-like transporter family; cl23754"
                     /db_xref="CDD:474045"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            166..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            208..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            234..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            274..294
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            306..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NVV3.1)"
     Site            337..357
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NVV3.1)"
     CDS             1..410
                     /gene="NIPAL1"
                     /gene_synonym="NIPA3; NPAL1; SLC57A3"
                     /coded_by="NM_207330.3:69..1301"
                     /db_xref="CCDS:CCDS3479.1"
                     /db_xref="GeneID:152519"
                     /db_xref="HGNC:HGNC:27194"
                     /db_xref="MIM:620340"
ORIGIN      
        1 mgaqvrlppg epcregyvls lvcpnssqaw ceitnvsqll aspvlytdln ysinnlsisa
       61 nvenkyslyv glvlavsssi figssfilkk kgllqlaskg ftragqgghs ylkewlwwvg
      121 llsmgageaa nfaayafapa tlvtplgals vlisailssy flnehlnihg kigcilsilg
      181 stvmvihapq eeevtslhem emklrdpgfi sfaviitvis lvlilivapk kgqtnilvyi
      241 sicsligafs vssvkglgia ikeliewkpv ykhplvfvll avlvlsvttq inylnkaldt
      301 fntslvtpiy yvfftsmvvt csailfqewy gmtagdiigt lsgfftiiig ifllhafknt
      361 ditwseltst akkeavslnv nennyvllen lecsapgynd dvtlfsrtdd
//
LOCUS       NP_001355274             256 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 330 isoform 4 [Mus musculus].
ACCESSION   NP_001355274
VERSION     NP_001355274.1
DBSOURCE    REFSEQ: accession NM_001368345.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Bolivar,J., Diaz,I., Iglesias,C. and Valdivia,M.M.
  TITLE     Molecular cloning of a zinc finger autoantigen transiently
            associated with interphase nucleolus and mitotic centromeres and
            midbodies. Orthologous proteins with nine CXXC motifs highly
            conserved from nematodes to humans
  JOURNAL   J Biol Chem 274 (51), 36456-36464 (1999)
   PUBMED   10593942
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC124757.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3811091.1,
                                           SRR11927936.1518042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164141, SAMN01164143
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 39.58 cM"
     Protein         1..256
                     /product="zinc finger protein 330 isoform 4"
                     /note="nucleolar cysteine-rich protein; nucleolar
                     autoantigen 36"
                     /calculated_mol_wt=28534
     Region          <11..233
                     /region_name="NOA36"
                     /note="NOA36 protein; pfam06524"
                     /db_xref="CDD:368953"
     CDS             1..256
                     /gene="Zfp330"
                     /gene_synonym="Noa36; Znf330"
                     /coded_by="NM_001368345.1:211..981"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:30932"
                     /db_xref="MGI:MGI:1353574"
ORIGIN      
        1 mlqwnatnvr gktkcmmkss dcvikhagvy stglamvgai cdfceawvch grkclsthac
       61 acpltdaecv ecergvwdhg grifscsfch nflceddqfe hqascqvlea etfkcvscnr
      121 lgqhsclrck acfcdehtrs kvfkqekgkq ppcpkcghet qetkdlsmst rslkfgrqtg
      181 geedgasgyd aywknlssdk ygdtgyhddd eeedeaedee eedgkdsdae ssdlfnnlnl
      241 grtyasgyah yeeqes
//
LOCUS       NP_001099133             238 aa            linear   PRI 27-APR-2025
DEFINITION  peroxisomal coenzyme A diphosphatase NUDT7 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001099133 XP_001127131 XP_001131284
VERSION     NP_001099133.1
DBSOURCE    REFSEQ: accession NM_001105663.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Dastani,Z., Pajukanta,P., Marcil,M., Rudzicz,N., Ruel,I.,
            Bailey,S.D., Lee,J.C., Lemire,M., Faith,J., Platko,J., Rioux,J.,
            Hudson,T.J., Gaudet,D., Engert,J.C. and Genest,J.
  TITLE     Fine mapping and association studies of a high-density lipoprotein
            cholesterol linkage region on chromosome 16 in French-Canadian
            subjects
  JOURNAL   Eur J Hum Genet 18 (3), 342-347 (2010)
   PUBMED   19844255
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Gasmi,L. and McLennan,A.G.
  TITLE     The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific
            for coenzyme A and its derivatives
  JOURNAL   Biochem J 357 (Pt 1), 33-38 (2001)
   PUBMED   11415433
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX387030.2, BU579534.1,
            AK296963.1 and AI927964.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Oct 2, 2007 this sequence version replaced
            XP_001131284.1, XP_001127131.1.
            
            Summary: The protein encoded by this gene is a member of the Nudix
            hydrolase family. Nudix hydrolases eliminate potentially toxic
            nucleotide metabolites from the cell and regulate the
            concentrations and availability of many different nucleotide
            substrates, cofactors, and signaling molecules. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            found for this gene. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.207152.1,
                                           SRR5189652.51129.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268533.9/ ENSP00000268533.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..238
                     /product="peroxisomal coenzyme A diphosphatase NUDT7
                     isoform 1"
                     /EC_number="3.6.1.77"
                     /note="peroxisomal coenzyme A diphosphatase NUDT7; nudix
                     (nucleoside diphosphate linked moiety X)-type motif 7"
                     /calculated_mol_wt=26811
     Region          38..195
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
     Site            66
                     /site_type="other"
                     /note="Important for coenzyme A binding.
                     /evidence=ECO:0000250|UniProtKB:Q99P30; propagated from
                     UniProtKB/Swiss-Prot (P0C024.1)"
     Region          77..98
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C024.1)"
     Region          236..238
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C024.1)"
     CDS             1..238
                     /gene="NUDT7"
                     /coded_by="NM_001105663.3:70..786"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42195.1"
                     /db_xref="GeneID:283927"
                     /db_xref="HGNC:HGNC:8054"
                     /db_xref="MIM:609231"
ORIGIN      
        1 msrlglpeep vrnsllddak arlrkydigg kyshlpynky svllplvake gklhllftvr
       61 seklrrapge vcfpggkrdp tdmddaatal reaqeevglr phqvevvccl vpclidtdtl
      121 itpfvglidh nfqaqpnpae vkdvflvpla yflhpqvhdq hyvtrlghrf inhifeytnp
      181 edgvtyqikg mtanlavlva fiilekkptf evqfnlndvl asseelflkv hkkatsrl
//
LOCUS       NP_660321                135 aa            linear   PRI 27-APR-2025
DEFINITION  germinal center-associated signaling and motility-like protein
            isoform a [Homo sapiens].
ACCESSION   NP_660321
VERSION     NP_660321.1
DBSOURCE    REFSEQ: accession NM_145278.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 135)
  AUTHORS   de Sa Machado Araujo,G., da Silva Francisco Junior,R., Dos Santos
            Ferreira,C., Mozer Rodrigues,P.T., Terra Machado,D., Louvain de
            Souza,T., Teixeira de Souza,J., Figueiredo Osorio da Silva,C.,
            Alves da Silva,A.F., Andrade,C.C.F., da Silva,A.T., Ramos,V.,
            Garcia,A.B., Machado,F.B. and Medina-Acosta,E.
  TITLE     Maternal 5mCpG Imprints at the PARD6G-AS1 and GCSAML Differentially
            Methylated Regions Are Decoupled From Parent-of-Origin Expression
            Effects in Multiple Human Tissues
  JOURNAL   Front Genet 9, 36 (2018)
   PUBMED   29545821
  REMARK    GeneRIF: Maternal 5mCpG imprints at the GCSAML somatic (secondary)
            differentially methylated region (iDMR) are decoupled from
            parent-of-origin expression effects in multiple human tissues.
            Despite the constitutive methylation asymmetry observed for the
            parental alleles at the iDMR, GCSAML was expressed biallelically in
            five tissues: visceral adipose tissue, brain - cerebellar
            hemisphere, brain cerebellum, prostate, and testis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Gieger,C., Radhakrishnan,A., Cvejic,A., Tang,W., Porcu,E.,
            Pistis,G., Serbanovic-Canic,J., Elling,U., Goodall,A.H.,
            Labrune,Y., Lopez,L.M., Magi,R., Meacham,S., Okada,Y., Pirastu,N.,
            Sorice,R., Teumer,A., Voss,K., Zhang,W., Ramirez-Solis,R.,
            Bis,J.C., Ellinghaus,D., Gogele,M., Hottenga,J.J., Langenberg,C.,
            Kovacs,P., O'Reilly,P.F., Shin,S.Y., Esko,T., Hartiala,J.,
            Kanoni,S., Murgia,F., Parsa,A., Stephens,J., van der Harst,P.,
            Ellen van der Schoot,C., Allayee,H., Attwood,A., Balkau,B.,
            Bastardot,F., Basu,S., Baumeister,S.E., Biino,G., Bomba,L.,
            Bonnefond,A., Cambien,F., Chambers,J.C., Cucca,F., D'Adamo,P.,
            Davies,G., de Boer,R.A., de Geus,E.J., Doring,A., Elliott,P.,
            Erdmann,J., Evans,D.M., Falchi,M., Feng,W., Folsom,A.R.,
            Frazer,I.H., Gibson,Q.D., Glazer,N.L., Hammond,C.,
            Hartikainen,A.L., Heckbert,S.R., Hengstenberg,C., Hersch,M.,
            Illig,T., Loos,R.J., Jolley,J., Khaw,K.T., Kuhnel,B.,
            Kyrtsonis,M.C., Lagou,V., Lloyd-Jones,H., Lumley,T., Mangino,M.,
            Maschio,A., Mateo Leach,I., McKnight,B., Memari,Y., Mitchell,B.D.,
            Montgomery,G.W., Nakamura,Y., Nauck,M., Navis,G., Nothlings,U.,
            Nolte,I.M., Porteous,D.J., Pouta,A., Pramstaller,P.P., Pullat,J.,
            Ring,S.M., Rotter,J.I., Ruggiero,D., Ruokonen,A., Sala,C.,
            Samani,N.J., Sambrook,J., Schlessinger,D., Schreiber,S.,
            Schunkert,H., Scott,J., Smith,N.L., Snieder,H., Starr,J.M.,
            Stumvoll,M., Takahashi,A., Tang,W.H., Taylor,K., Tenesa,A., Lay
            Thein,S., Tonjes,A., Uda,M., Ulivi,S., van Veldhuisen,D.J.,
            Visscher,P.M., Volker,U., Wichmann,H.E., Wiggins,K.L.,
            Willemsen,G., Yang,T.P., Hua Zhao,J., Zitting,P., Bradley,J.R.,
            Dedoussis,G.V., Gasparini,P., Hazen,S.L., Metspalu,A., Pirastu,M.,
            Shuldiner,A.R., Joost van Pelt,L., Zwaginga,J.J., Boomsma,D.I.,
            Deary,I.J., Franke,A., Froguel,P., Ganesh,S.K., Jarvelin,M.R.,
            Martin,N.G., Meisinger,C., Psaty,B.M., Spector,T.D., Wareham,N.J.,
            Akkerman,J.W., Ciullo,M., Deloukas,P., Greinacher,A., Jupe,S.,
            Kamatani,N., Khadake,J., Kooner,J.S., Penninger,J., Prokopenko,I.,
            Stemple,D., Toniolo,D., Wernisch,L., Sanna,S., Hicks,A.A.,
            Rendon,A., Ferreira,M.A., Ouwehand,W.H. and Soranzo,N.
  TITLE     New gene functions in megakaryopoiesis and platelet formation
  JOURNAL   Nature 480 (7376), 201-208 (2011)
   PUBMED   22139419
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Trevino,L.R., Yang,W., French,D., Hunger,S.P., Carroll,W.L.,
            Devidas,M., Willman,C., Neale,G., Downing,J., Raimondi,S.C.,
            Pui,C.H., Evans,W.E. and Relling,M.V.
  TITLE     Germline genomic variants associated with childhood acute
            lymphoblastic leukemia
  JOURNAL   Nat Genet 41 (9), 1001-1005 (2009)
   PUBMED   19684603
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK124520.1, BC024174.1,
            AL606804.11 and BU852381.1.
            
            Summary: This gene encodes a protein thought to be a signaling
            molecule associated with germinal centers, the sites of
            proliferation and differentiation of mature B lymphocytes.
            Alternate splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). The 5' UTR splicing pattern has not been determined for this
            variant. Variants 1 and 7 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.75240.1, BC024174.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366488.5/ ENSP00000355444.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..135
                     /product="germinal center-associated signaling and
                     motility-like protein isoform a"
                     /note="germinal center-associated signaling and
                     motility-like protein"
                     /calculated_mol_wt=15581
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JQS6.1)"
     Region          48..134
                     /region_name="HGAL"
                     /note="Germinal center-associated lymphoma; pfam15666"
                     /db_xref="CDD:464789"
     CDS             1..135
                     /gene="GCSAML"
                     /gene_synonym="C1orf150"
                     /coded_by="NM_145278.5:59..466"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1635.1"
                     /db_xref="GeneID:148823"
                     /db_xref="HGNC:HGNC:29583"
ORIGIN      
        1 mgnyllrkls clgenqkkpk kgnpdeerkr qemttferkl qdqdkksqev sstsnqenen
       61 gsgseevcyt vinhiphqrs slssnddgye nidsltrkvr qfrersetey allrtsvsrp
      121 cscthehdye vvfph
//
LOCUS       NP_001353103             714 aa            linear   PRI 27-APR-2025
DEFINITION  ribonucleoprotein PTB-binding 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001353103 XP_011525973
VERSION     NP_001353103.1
DBSOURCE    REFSEQ: accession NM_001366174.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Wedler,A., Bley,N., Glass,M., Muller,S., Rausch,A., Lederer,M.,
            Urbainski,J., Schian,L., Obika,K.B., Simon,T., Peters,L.M.,
            Misiak,C., Fuchs,T., Kohn,M., Jacob,R., Gutschner,T., Ihling,C.,
            Sinz,A. and Huttelmaier,S.
  TITLE     RAVER1 hinders lethal EMT and modulates miR/RISC activity by the
            control of alternative splicing
  JOURNAL   Nucleic Acids Res 52 (7), 3971-3988 (2024)
   PUBMED   38300787
  REMARK    GeneRIF: RAVER1 hinders lethal EMT and modulates miR/RISC activity
            by the control of alternative splicing.
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Fink-Baldauf,I.M., Stuart,W.D., Brewington,J.J., Guo,M. and
            Maeda,Y.
  TITLE     CRISPRi links COVID-19 GWAS loci to LZTFL1 and RAVER1
  JOURNAL   EBioMedicine 75, 103806 (2022)
   PUBMED   34998241
  REMARK    GeneRIF: CRISPRi links COVID-19 GWAS loci to LZTFL1 and RAVER1.
REFERENCE   3  (residues 1 to 714)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 714)
  CONSRTM   COVID-19 Host Genetics Initiative
  TITLE     Mapping the human genetic architecture of COVID-19
  JOURNAL   Nature 600 (7889), 472-477 (2021)
   PUBMED   34237774
REFERENCE   5  (residues 1 to 714)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 714)
  AUTHORS   Miyasaka,T., Morita,M., Ito,K., Suzuki,T., Fukuda,H., Takeda,S.,
            Inoue,J., Semba,K. and Yamamoto,T.
  TITLE     Interaction of antiproliferative protein Tob with the CCR4-NOT
            deadenylase complex
  JOURNAL   Cancer Sci 99 (4), 755-761 (2008)
   PUBMED   18377426
REFERENCE   7  (residues 1 to 714)
  AUTHORS   Romanelli,M.G., Lorenzi,P., Avesani,F. and Morandi,C.
  TITLE     Functional characterization of the ribonucleoprotein, PTB-binding
            1/Raver1 promoter region
  JOURNAL   Gene 405 (1-2), 79-87 (2007)
   PUBMED   17931803
  REMARK    GeneRIF: Raver1 gene promoter region shares common features of
            ubiquitously expressed gene with the interacting splicing regulator
            PTB
REFERENCE   8  (residues 1 to 714)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 714)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 714)
  AUTHORS   Huttelmaier,S., Illenberger,S., Grosheva,I., Rudiger,M.,
            Singer,R.H. and Jockusch,B.M.
  TITLE     Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and
            microfilament attachment proteins
  JOURNAL   J Cell Biol 155 (5), 775-786 (2001)
   PUBMED   11724819
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114271.2 and AC011511.12.
            
            On Sep 25, 2018 this sequence version replaced XP_011525973.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.97595.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..714
                     /product="ribonucleoprotein PTB-binding 1 isoform 2"
                     /note="protein raver-1"
                     /calculated_mol_wt=75172
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY67.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IY67.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IY67.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IY67.1)"
     Region          45..60
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY67.1)"
     Region          59..129
                     /region_name="RRM1_RAVER1"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     ribonucleoprotein PTB-binding 1 (raver-1); cd12663"
                     /db_xref="CDD:410064"
     Site            order(67..69,91..93,117,119..121)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410064"
     Region          133..209
                     /region_name="RRM2_RAVER1"
                     /note="RNA recognition motif 2 (RRM2) found found in
                     vertebrate ribonucleoprotein PTB-binding 1 (raver-1);
                     cd12665"
                     /db_xref="CDD:410066"
     Region          219..306
                     /region_name="RRM3_RAVER1"
                     /note="RNA recognition motif 3 (RRM3) found in vertebrate
                     ribonucleoprotein PTB-binding 1 (raver-1); cd12667"
                     /db_xref="CDD:410068"
     Region          307..395
                     /region_name="Interaction with PTBP1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY67.1)"
     Region          <364..612
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          391..474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY67.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IY67.1)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IY67.1)"
     CDS             1..714
                     /gene="RAVER1"
                     /coded_by="NM_001366174.1:23..2167"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:125950"
                     /db_xref="HGNC:HGNC:30296"
                     /db_xref="MIM:609950"
ORIGIN      
        1 maadvsvthr pplspksgae veagdaaerr apeeelppld peeirkrleh terqfrnrrk
       61 ilirglpgdv tnqevhdlls dyelkycfvd kykgtafvtl lngeqaeaai nafhqsrlre
      121 relsvqlqpt dallcvanlp psltqqqfee lvrpfgsler cflvysertg qskgygfaey
      181 mkkdsaarak sdllgkplgp rtlyvhwtda gqltpallhs rclcvdrlpp gfndvdalcr
      241 alsavhsptf cqlacgqdgq lkgfavleye taemaeeaqq qadglslggs hlrvsfcapg
      301 ppgrsmlaal iaaqatalnr gkgllpepni lqllnnlgps aslqlllnpl lhgsaggkqg
      361 llgappampl lngpalstal lqlalqtqgq kkpgilgdsp lgalqpgaqp anpllgelpa
      421 ggglppelpp rrgkpppllp svlgpaggdr ealglgppaa qltpppapvg lrgsglrglq
      481 kdsgplptpp gvsllgeppk dyriplnpyl nlhsllpasn laapgggsss skafqlksrl
      541 lsplssarlp pepglsdsys fdypsdmgpr rlfshprepa lgphgpsrhk mspppsgfge
      601 rssggsgggp lshfysgspt syftsglqag lkqshlskai gssplgsgeg llglspgpng
      661 hshllktplg gqkrsfahll pspepspegs yvgqhsqglg ghyadsylkr krif
//
LOCUS       NP_061841                539 aa            linear   PRI 27-APR-2025
DEFINITION  gamma-2-syntrophin [Homo sapiens].
ACCESSION   NP_061841 XP_352506
VERSION     NP_061841.2
DBSOURCE    REFSEQ: accession NM_018968.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Jales Neto,L.H., Wicik,Z., Torres,G.H.F., Takayama,L.,
            Caparbo,V.F., Lopes,N.H.M., Pereira,A.C. and Pereira,R.M.R.
  TITLE     Overexpression of SNTG2, TRAF3IP2, and ITGA6 transcripts is
            associated with osteoporotic vertebral fracture in elderly women
            from community
  JOURNAL   Mol Genet Genomic Med 8 (9), e1391 (2020)
   PUBMED   32602654
  REMARK    GeneRIF: Overexpression of SNTG2, TRAF3IP2, and ITGA6 transcripts
            is associated with osteoporotic vertebral fracture in elderly women
            from community.
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Rio,M., Royer,G., Gobin,S., de Blois,M.C., Ozilou,C., Bernheim,A.,
            Nizon,M., Munnich,A., Bonnefont,J.P., Romana,S., Vekemans,M.,
            Turleau,C. and Malan,V.
  TITLE     Monozygotic twins discordant for submicroscopic chromosomal
            anomalies in 2p25.3 region detected by array CGH
  JOURNAL   Clin Genet 84 (1), 31-36 (2013)
   PUBMED   23061379
  REMARK    GeneRIF: MYT1L and the SNTG2 genes within the reported region could
            probably relate to the phenotypic discordance of the monozygotic
            twins.
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Yamakawa,H., Oyama,S., Mitsuhashi,H., Sasagawa,N., Uchino,S.,
            Kohsaka,S. and Ishiura,S.
  TITLE     Neuroligins 3 and 4X interact with syntrophin-gamma2, and the
            interactions are affected by autism-related mutations
  JOURNAL   Biochem Biophys Res Commun 355 (1), 41-46 (2007)
   PUBMED   17292328
  REMARK    GeneRIF: A de novo binding partner of X-linked neuroligin 4 and
            neuroligin 3, which correlates with autism-related mutations.
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Ou,Y., Strege,P., Miller,S.M., Makielski,J., Ackerman,M.,
            Gibbons,S.J. and Farrugia,G.
  TITLE     Syntrophin gamma 2 regulates SCN5A gating by a PDZ domain-mediated
            interaction
  JOURNAL   J Biol Chem 278 (3), 1915-1923 (2003)
   PUBMED   12429735
  REMARK    GeneRIF: role in regulating SCN5A gating by a PDZ domain-mediated
            interaction
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Piluso,G., Mirabella,M., Ricci,E., Belsito,A., Abbondanza,C.,
            Servidei,S., Puca,A.A., Tonali,P., Puca,G.A. and Nigro,V.
  TITLE     Gamma1- and gamma2-syntrophins, two novel dystrophin-binding
            proteins localized in neuronal cells
  JOURNAL   J Biol Chem 275 (21), 15851-15860 (2000)
   PUBMED   10747910
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC116614.6, BC035783.1,
            AJ003029.1 and BG208326.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 24, 2009 this sequence version replaced NP_061841.1.
            
            Summary: This gene encodes a protein belonging to the syntrophin
            family. Syntrophins are cytoplasmic peripheral membrane proteins
            that bind to components of mechanosenstive sodium channels and the
            extreme carboxy-terminal domain of dystrophin and
            dystrophin-related proteins. The PDZ domain of this protein product
            interacts with a protein component of a mechanosensitive sodium
            channel that affects channel gating. Absence or reduction of this
            protein product has been associated with Duchenne muscular
            dystrophy. There is evidence of alternative splicing yet the
            full-length nature of these variants has not been described.
            [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ003029.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2154125
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308624.10/ ENSP00000311837.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.3"
     Protein         1..539
                     /product="gamma-2-syntrophin"
                     /note="syntrophin-5"
                     /calculated_mol_wt=60086
     Region          72..154
                     /region_name="PDZ_syntrophin-like"
                     /note="PDZ domain of syntrophins, and related domains;
                     cd06801"
                     /db_xref="CDD:467262"
     Site            order(83..89,101,104,134,138,141..142)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467262"
     Region          168..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY99.2)"
     CDS             1..539
                     /gene="SNTG2"
                     /gene_synonym="G2SYN; SYN5"
                     /coded_by="NM_018968.4:149..1768"
                     /db_xref="CCDS:CCDS46220.1"
                     /db_xref="GeneID:54221"
                     /db_xref="HGNC:HGNC:13741"
                     /db_xref="MIM:608715"
ORIGIN      
        1 mgtegppppa asrgrqgcll vpartkttia llydeesena ydirlkltke vltiqkqdvv
       61 cvggshqgrn rrtvtlrrqp vgglglsikg gsehnvpvvi skifedqaad qtgmlfvgda
      121 vlqvngihve natheevvhl lrnagdevti tveylreapa flklplgspg pssdhssgas
      181 splfdsglhl ngnssttaps spsspiakdp ryekrwldtl svplsmaris rykagteklr
      241 wnafevlald gvssgilrfy taqdgtdwlr avsanirelt lqnmkmankc cspsdqvvhm
      301 gwvneklqga dssqtfrpkf lalkgpsfyv fstppvstfd wvraertyhl cevlfkvhkf
      361 wltedcwlqa nlylglqdfd fedqrpycfs ivaghgkshv fnvelgsela mweksfqrat
      421 fmevqrtgsr tymcswqgem lcftvdfalg ftcfesktkn vlwrfkfsql kgssddgktr
      481 vkllfqnldt kqietkelef qdlravlhci hsfiaakvas vdpgfmdsqs larkymyss
//
LOCUS       NP_004429                986 aa            linear   PRI 27-APR-2025
DEFINITION  ephrin type-A receptor 4 isoform a precursor [Homo sapiens].
ACCESSION   NP_004429 XP_379155
VERSION     NP_004429.1
DBSOURCE    REFSEQ: accession NM_004438.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Verma,M., Chopra,M. and Kumar,H.
  TITLE     Unraveling the Potential of EphA4: A Breakthrough Target and Beacon
            of Hope for Neurological Diseases
  JOURNAL   Cell Mol Neurobiol 43 (7), 3375-3391 (2023)
   PUBMED   37477786
  REMARK    GeneRIF: Unraveling the Potential of EphA4: A Breakthrough Target
            and Beacon of Hope for Neurological Diseases.
            Review article
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Kina,S., Kawabata-Iwakawa,R., Miyamoto,S., Kato,T., Kina-Tanada,M.
            and Arasaki,A.
  TITLE     EphA4 signaling is involved in the phenotype of well-differentiated
            oral squamous cell arcinoma with decreased tumor immunity
  JOURNAL   Eur J Pharmacol 945, 175611 (2023)
   PUBMED   36804938
  REMARK    GeneRIF: EphA4 signaling is involved in the phenotype of
            well-differentiated oral squamous cell arcinoma with decreased
            tumor immunity.
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Ganguly,D., Thomas,J.A., Ali,A. and Kumar,R.
  TITLE     Mechanistic and therapeutic implications of EphA-4 receptor
            tyrosine kinase in the pathogenesis of Alzheimer's disease
  JOURNAL   Eur J Neurosci 56 (9), 5532-5546 (2022)
   PUBMED   34989046
  REMARK    GeneRIF: Mechanistic and therapeutic implications of EphA-4
            receptor tyrosine kinase in the pathogenesis of Alzheimer's
            disease.
            Review article
REFERENCE   4  (residues 1 to 986)
  AUTHORS   Liu,C., Han,S., Zheng,J., Wang,H., Li,S. and Li,J.
  TITLE     EphA4 regulates white matter remyelination after ischemic stroke
            through Ephexin-1/RhoA/ROCK signaling pathway
  JOURNAL   Glia 70 (10), 1971-1991 (2022)
   PUBMED   35762396
  REMARK    GeneRIF: EphA4 regulates white matter remyelination after ischemic
            stroke through Ephexin-1/RhoA/ROCK signaling pathway.
REFERENCE   5  (residues 1 to 986)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   6  (residues 1 to 986)
  AUTHORS   Karidis,N.P., Giaginis,C., Tsourouflis,G., Alexandrou,P.,
            Delladetsima,I. and Theocharis,S.
  TITLE     Eph-A2 and Eph-A4 expression in human benign and malignant thyroid
            lesions: an immunohistochemical study
  JOURNAL   Med Sci Monit 17 (9), BR257-BR265 (2011)
   PUBMED   21873938
  REMARK    GeneRIF: The present data suggest that Eph-A2, but not Eph-A4,
            overexpression may be associated with the malignant transformation
            of thyroid neoplasia.
REFERENCE   7  (residues 1 to 986)
  AUTHORS   Aasheim,H.C., Terstappen,L.W. and Logtenberg,T.
  TITLE     Regulated expression of the Eph-related receptor tyrosine kinase
            Hek11 in early human B lymphopoiesis
  JOURNAL   Blood 90 (9), 3613-3622 (1997)
   PUBMED   9345045
REFERENCE   8  (residues 1 to 986)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   9  (residues 1 to 986)
  AUTHORS   Ellis,C., Kasmi,F., Ganju,P., Walls,E., Panayotou,G. and Reith,A.D.
  TITLE     A juxtamembrane autophosphorylation site in the Eph family receptor
            tyrosine kinase, Sek, mediates high affinity interaction with
            p59fyn
  JOURNAL   Oncogene 12 (8), 1727-1736 (1996)
   PUBMED   8622893
REFERENCE   10 (residues 1 to 986)
  AUTHORS   Fox,G.M., Holst,P.L., Chute,H.T., Lindberg,R.A., Janssen,A.M.,
            Basu,R. and Welcher,A.A.
  TITLE     cDNA cloning and tissue distribution of five human EPH-like
            receptor protein-tyrosine kinases
  JOURNAL   Oncogene 10 (5), 897-905 (1995)
   PUBMED   7898931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA451606.1, BC105000.1,
            AC010899.8 and BM676153.1.
            
            On Mar 23, 2004 this sequence version replaced XP_379155.1.
            
            Summary: This gene belongs to the ephrin receptor subfamily of the
            protein-tyrosine kinase family. EPH and EPH-related receptors have
            been implicated in mediating developmental events, particularly in
            the nervous system. Receptors in the EPH subfamily typically have a
            single kinase domain and an extracellular region containing a
            Cys-rich domain and 2 fibronectin type III repeats. The ephrin
            receptors are divided into 2 groups based on the similarity of
            their extracellular domain sequences and their affinities for
            binding ephrin-A and ephrin-B ligands. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.89906.1,
                                           SRR1803614.85638.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281821.7/ ENSP00000281821.2
            NMD candidate          :: PMID: 21873938
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q36.1"
     Protein         1..986
                     /product="ephrin type-A receptor 4 isoform a precursor"
                     /EC_number="2.7.10.1"
                     /note="receptor protein-tyrosine kinase HEK8; ephrin
                     type-A receptor 4; tyrosine-protein kinase receptor SEK;
                     TYRO1 protein tyrosine kinase; EPH-like kinase 8;
                     tyrosine-protein kinase TYRO1"
                     /calculated_mol_wt=107789
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2090
     Region          30..203
                     /region_name="EphR_LBD_A4"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 4;
                     cd10482"
                     /db_xref="CDD:198450"
     Site            order(40,42,51,55..60,62,64,68,71,73,104..106,111..112,
                     154,157..158,163..164,166,191..193,195)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198450"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54764.1)"
     Region          329..436
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(329,405,418)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54764.1)"
     Site            408
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54764.1)"
     Site            order(419..420,422,429)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          441..532
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(441,505,520)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(521..522,524..525)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            545
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54764.1)"
     Site            548..569
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54764.1)"
     Region          562..618
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q03137; propagated from
                     UniProtKB/Swiss-Prot (P54764.1)"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q03137; propagated from
                     UniProtKB/Swiss-Prot (P54764.1)"
     Region          616..882
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(627,629..631,635,651,653,699..700,702,746,750..751,
                     753,764,783..787,796,830)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(627..631,635,651,653,699..702,705..706,750..751,753,
                     764)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            order(746,750,783..787,796,830)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            763..789
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Site            779
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54764.1)"
     Region          911..981
                     /region_name="SAM_EPH-A4"
                     /note="SAM domain of EPH-A4 subfamily of tyrosine kinase
                     receptors; cd09545"
                     /db_xref="CDD:188944"
     Site            order(913..914,940,944,972,976,979)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:188944"
     Site            order(928,961)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188944"
     Site            928
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54764.1)"
     Region          984..986
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P54764.1)"
     CDS             1..986
                     /gene="EPHA4"
                     /gene_synonym="EK8; HEK8; SEK; TYRO1"
                     /coded_by="NM_004438.5:57..3017"
                     /note="isoform a precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS2447.1"
                     /db_xref="GeneID:2043"
                     /db_xref="HGNC:HGNC:3388"
                     /db_xref="MIM:602188"
ORIGIN      
        1 magifyfalf sclfgicdav tgsrvypane vtlldsrsvq gelgwiaspl eggweevsim
       61 dekntpirty qvcnvmepsq nnwlrtdwit regaqrvyie ikftlrdcns lpgvmgtcke
      121 tfnlyyyesd ndkerfiren qfvkidtiaa desftqvdig drimklntei rdvgplskkg
      181 fylafqdvga cialvsvrvf ykkcpltvrn laqfpdtitg adtsslvevr gscvnnseek
      241 dvpkmycgad gewlvpignc lcnagheers gecqackigy ykalstdatc akcpphsysv
      301 wegatsctcd rgffradnda asmpctrpps aplnlisnvn etsvnlewss pqntggrqdi
      361 synvvckkcg agdpskcrpc gsgvhytpqq nglkttkvsi tdllahtnyt feiwavngvs
      421 kynpnpdqsv svtvttnqaa pssialvqak evtrysvala wlepdrpngv ileyevkyye
      481 kdqnersyri vrtaarntdi kglnpltsyv fhvrartaag ygdfseplev ttntvpsrii
      541 gdganstvll vsvsgsvvlv viliaafvis rrrskyskak qeadeekhln qgvrtyvdpf
      601 tyedpnqavr efakeidasc ikiekvigvg efgevcsgrl kvpgkreicv aiktlkagyt
      661 dkqrrdflse asimgqfdhp niihlegvvt kckpvmiite ymengsldaf lrkndgrftv
      721 iqlvgmlrgi gsgmkylsdm syvhrdlaar nilvnsnlvc kvsdfgmsrv leddpeaayt
      781 trggkipirw tapeaiayrk ftsasdvwsy givmwevmsy gerpywdmsn qdvikaieeg
      841 yrlpppmdcp ialhqlmldc wqkersdrpk fgqivnmldk lirnpnslkr tgtessrpnt
      901 alldpsspef savvsvgdwl qaikmdrykd nftaagyttl eavvhvnqed larigitait
      961 hqnkilssvq amrtqmqqmh grmvpv
//
LOCUS       NP_001107570            1893 aa            linear   ROD 27-APR-2025
DEFINITION  microtubule cross-linking factor 1 isoform 1 [Mus musculus].
ACCESSION   NP_001107570
VERSION     NP_001107570.1
DBSOURCE    REFSEQ: accession NM_001114098.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1893)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1893)
  AUTHORS   Satake,T., Yamashita,K., Hayashi,K., Miyatake,S., Tamura-Nakano,M.,
            Doi,H., Furuta,Y., Shioi,G., Miura,E., Takeo,Y.H., Yoshida,K.,
            Yahikozawa,H., Matsumoto,N., Yuzaki,M. and Suzuki,A.
  TITLE     MTCL1 plays an essential role in maintaining Purkinje neuron axon
            initial segment
  JOURNAL   EMBO J 36 (9), 1227-1242 (2017)
   PUBMED   28283581
  REMARK    GeneRIF: These results indicate that MTCL1-mediated formation of
            stable microtubule bundles is crucial for maintenance of AnkG
            localization.
REFERENCE   3  (residues 1 to 1893)
  AUTHORS   Araujo,D.J., Anderson,A.G., Berto,S., Runnels,W., Harper,M.,
            Ammanuel,S., Rieger,M.A., Huang,H.C., Rajkovich,K., Loerwald,K.W.,
            Dekker,J.D., Tucker,H.O., Dougherty,J.D., Gibson,J.R. and
            Konopka,G.
  TITLE     FoxP1 orchestration of ASD-relevant signaling pathways in the
            striatum
  JOURNAL   Genes Dev 29 (20), 2081-2096 (2015)
   PUBMED   26494785
REFERENCE   4  (residues 1 to 1893)
  AUTHORS   Sato,Y., Akitsu,M., Amano,Y., Yamashita,K., Ide,M., Shimada,K.,
            Yamashita,A., Hirano,H., Arakawa,N., Maki,T., Hayashi,I., Ohno,S.
            and Suzuki,A.
  TITLE     The novel PAR-1-binding protein MTCL1 has crucial roles in
            organizing microtubules in polarizing epithelial cells
  JOURNAL   J Cell Sci 126 (Pt 20), 4671-4683 (2013)
   PUBMED   23902687
REFERENCE   5  (residues 1 to 1893)
  AUTHORS   Nishimura,M., Yokoi,N., Miki,T., Horikawa,Y., Yoshioka,H.,
            Takeda,J., Ohara,O. and Seino,S.
  TITLE     Construction of a multi-functional cDNA library specific for mouse
            pancreatic islets and its application to microarray
  JOURNAL   DNA Res 11 (5), 315-323 (2004)
   PUBMED   15747579
REFERENCE   6  (residues 1 to 1893)
  AUTHORS   Sousa-Nunes,R., Rana,A.A., Kettleborough,R., Brickman,J.M.,
            Clements,M., Forrest,A., Grimmond,S., Avner,P., Smith,J.C.,
            Dunwoodie,S.L. and Beddington,R.S.
  TITLE     Characterizing embryonic gene expression patterns in the mouse
            using nonredundant sequence-based selection
  JOURNAL   Genome Res 13 (12), 2609-2620 (2003)
   PUBMED   14613977
REFERENCE   7  (residues 1 to 1893)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Aizawa,H., Yuasa,S.,
            Nakajima,D., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: II. The complete nucleotide sequences of 400 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (1), 35-48 (2003)
   PUBMED   12693553
REFERENCE   8  (residues 1 to 1893)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CT010496.14 and CT025601.7.
            
            Transcript Variant: This variant (1) represents the longer
            transcript but encodes the shorter isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK147691.1, AK147631.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1893
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 35.3 cM"
     Protein         1..1893
                     /product="microtubule cross-linking factor 1 isoform 1"
                     /note="coiled-coil domain-containing protein 165; protein
                     SOGA2; SOGA family member 2; PAR-1-interacting protein;
                     microtubule cross-linking factor 1"
                     /calculated_mol_wt=207977
     Region          1..500
                     /region_name="Necessary for self-assembly, microtubule
                     bundling activity and apicobasal microtubule organization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          1..316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          1..241
                     /region_name="Necessary for colocalization and binding
                     with microtubules"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          <13..317
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          <342..648
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          493..587
                     /region_name="SOGA"
                     /note="Protein SOGA; pfam11365"
                     /db_xref="CDD:463264"
     Region          536..555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          599..622
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          622..714
                     /region_name="SOGA"
                     /note="Protein SOGA; pfam11365"
                     /db_xref="CDD:463264"
     Site            677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          728..792
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            768
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          829..857
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            891
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            913
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          <1104..>1274
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1220..1341
                     /region_name="DUF4482"
                     /note="Domain of unknown function (DUF4482); pfam14818"
                     /db_xref="CDD:464333"
     Region          1257..1368
                     /region_name="Necessary for interaction with MARK2 and
                     apicobasal microtubule bundle formation in polarized
                     epithelial cells. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          1272..1302
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1403
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1413
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1577
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1586
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          1653..1683
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1661
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1669
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          1672..1767
                     /region_name="Necessary for colocalization and binding
                     with microtubules. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          1701..1752
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Region          1771..1829
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4B5; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     Site            1801
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UHU5.1)"
     CDS             1..1893
                     /gene="Mtcl1"
                     /gene_synonym="1110012J17Rik; Ccdc165; D130071O13;
                     Kiaa0802; mKIAA0802; Soga2; t8219b25"
                     /coded_by="NM_001114098.2:406..6087"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS50168.1"
                     /db_xref="GeneID:68617"
                     /db_xref="MGI:MGI:1915867"
ORIGIN      
        1 metlngpagg gapdtkpqpa gqhhrhhhlh plaerrrlhr apsparpflk dlhtrpatat
       61 psagraptpa aprspslagk appspgppaa pgrlsrrsgv vpgakdkppp gagarsagga
      121 kavpgtrraa ragpaeplsr vgrptgaepp pavakgrktk rgpgtppara vvpparasrv
      181 pavtlsvtsv agcrinhtds ssdlsdcase plsdeqrllp aassdaesgt gssdrepirg
      241 aptpssgsrg pppgspeppi llaappvasa clggrsspgg astgspgpgs qedvggrapp
      301 ertilgtske pslgeqprll vvaeeeellr emeelrsend ylkdeldelr aemeemrdsy
      361 leedgyqlqe lrreldrank ncrilqyrlr kaeqkslkva etgqvdgeli rsleqdlkva
      421 kdvsvrlhhe letveekrak aeddnetlrq qmievevsrq alqneverlr esslkrrgsr
      481 emykekklvn qddsadlkcq lqfvkeeasl mrkkmaklgr ekdeleqelq kykslygdvd
      541 splptgeagg ppstreaelk lrlklveeea silgrkivel evenrglkae medirvqher
      601 egtgrdhvps tptspfgdsm esstelrrhl qfveeeaell rrsiseiedh nrqlthelsk
      661 fkfephqesg wlgdgvskgp aasvplqeel ksarlqidel sgkvlklqce nrlllsnaqr
      721 gdlaahlglr apsprdsdae sdagkkesdg eegrlpqpkr egpvggesds edmfektsgf
      781 gsgkpsease pcpaellrvr edteclvtik leaqrlertv erlisdtdgf ihdsglrgng
      841 laspgvqggg gegnspseph lletinvrmk afrkelqafl eqmsrivdgl splshltess
      901 sflstvtsvs rdspigtlgk elgpdlqskl reqlewqlnq drgdereglr lratrelhrr
      961 adgdsgshhg lggqscfnle meedhlyalr wkelemhsla lqntlhkrtw sdeknllqqe
     1021 lrslkqnifl fyvklrwllk hwrqgkqmee ggedleeseh penvpglael gvqgvhqtdg
     1081 idqedadqgc slpmgehaph slvqisehgs rlqssdggpl nkqvvenqql fralkalled
     1141 frselredeh arlrlqqqya sdkaawdvew avlkcrleql eektekslge ldssaegkga
     1201 lkkerevhqk lladshslvm dlrwqihhre knwnrekvel lerldserqe wgrqkeellw
     1261 rveqlqkeks prrsgsflcs rreddtrpyp hqgslhssrp vsmwpcedad sipfedrpls
     1321 klkesdrcsa senlyldals ldddpgdppp lrnclaeeee srkgnlqrav svscmsefqr
     1381 lmdvspflpe kglpsagske dvtpplspdd lkyieefhsn dwdyasprae adrppdpwad
     1441 rtemgrvghe attepcpdps wylttsvtmt tdtmtspehc qkqplrthvl teqsgvhvlh
     1501 sppairrvds iasggegrsr adpegpfpms rargnladak gghpepvlnr wpctpprhpr
     1561 dcvegslrpl drpicpslgf asplnsldms knmsddmkev afsvrnaica gpaephvrdm
     1621 acqtngsrta gtqtiqtisv glqtealras gvtssphkcl tpkagggttp vsspsrslrs
     1681 rqvapaiekv qakfertccs pkygspklqr kplskadqpn srtspgipqk gfsesawars
     1741 tttrespvht tindglsslf niidhspigv ragsrsrsae prqelgpgqe tgtssrgrsp
     1801 splgvgsetf reeggestpv rqdlsappgy tltenvaril nkkllehalk eerkqashgs
     1861 sgltsdshtg epvpaepgsm enqtvlltap wgl
//
LOCUS       NP_001352046             200 aa            linear   ROD 27-APR-2025
DEFINITION  transcription elongation factor A protein-like 5 [Mus musculus].
ACCESSION   NP_001352046 XP_006528639
VERSION     NP_001352046.1
DBSOURCE    REFSEQ: accession NM_001365117.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Sawada,A., Yamamoto,T. and Sato,T.
  TITLE     Tceal5 and Tceal7 Function in C2C12 Myogenic Differentiation via
            Exosomes in Fetal Bovine Serum
  JOURNAL   Int J Mol Sci 23 (4), 2036 (2022)
   PUBMED   35216152
  REMARK    GeneRIF: Tceal5 and Tceal7 Function in C2C12 Myogenic
            Differentiation via Exosomes in Fetal Bovine Serum.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Navas-Perez,E., Vicente-Garcia,C., Mirra,S., Burguera,D.,
            Fernandez-Castillo,N., Ferran,J.L., Lopez-Mayorga,M.,
            Alaiz-Noya,M., Suarez-Pereira,I., Anton-Galindo,E., Ulloa,F.,
            Herrera-Ubeda,C., Cusco,P., Falcon-Moya,R., Rodriguez-Moreno,A.,
            D'Aniello,S., Cormand,B., Marfany,G., Soriano,E., Carrion,A.M.,
            Carvajal,J.J. and Garcia-Fernandez,J.
  TITLE     Characterization of an eutherian gene cluster generated after
            transposon domestication identifies Bex3 as relevant for advanced
            neurological functions
  JOURNAL   Genome Biol 21 (1), 267 (2020)
   PUBMED   33100228
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Gergics,P., Christian,H.C., Choo,M.S., Ajmal,A. and Camper,S.A.
  TITLE     Gene Expression in Mouse Thyrotrope Adenoma: Transcription
            Elongation Factor Stimulates Proliferation
  JOURNAL   Endocrinology 157 (9), 3631-3646 (2016)
   PUBMED   27580811
  REMARK    GeneRIF: sufficient to increase the growth rate of pituitary
            progenitors, suggesting a role as a proto-oncogene
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY136503.1, AK032140.1 and BE991033.1.
            
            On Jul 28, 2018 this sequence version replaced XP_006528639.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.4096532.1,
                                           SRR7345562.2769826.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="X"
                     /map="X 57.4 cM"
     Protein         1..200
                     /product="transcription elongation factor A protein-like
                     5"
                     /note="TCEA-like protein 5; transcription elongation
                     factor S-II protein-like 5"
                     /calculated_mol_wt=21907
     Region          1..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CCT4.1)"
     Region          <6..>151
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          80..174
                     /region_name="BEX"
                     /note="Brain expressed X-linked like family; pfam04538"
                     /db_xref="CDD:461346"
     CDS             1..200
                     /gene="Tceal5"
                     /gene_synonym="6430401A05Rik"
                     /coded_by="NM_001365117.1:190..792"
                     /db_xref="CCDS:CCDS30416.1"
                     /db_xref="GeneID:331532"
                     /db_xref="MGI:MGI:3036236"
ORIGIN      
        1 mekfykeneg kpenkgraed egsteeggka dedksdaegk parqgkleve ggpgeqaqqk
       61 gegkpekqgk sdgegkrqge skpdsqaksa searaaekrp aedyvprkak rktdrgtdds
      121 pknsqedlqd rhvsseemmr ecadmtraqe elrkrqkmgg fhwvprdaqd alvprgqrgv
      181 rgvrggggrg qkdledapfv
//
LOCUS       NP_870992                614 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and SCAN domain-containing protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_870992
VERSION     NP_870992.2
DBSOURCE    REFSEQ: accession NM_181877.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 614)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Nicolas,E., Poitelon,Y., Chouery,E., Salem,N., Levy,N.,
            Megarbane,A. and Delague,V.
  TITLE     CAMOS, a nonprogressive, autosomal recessive, congenital cerebellar
            ataxia, is caused by a mutant zinc-finger protein, ZNF592
  JOURNAL   Eur J Hum Genet 18 (10), 1107-1113 (2010)
   PUBMED   20531441
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Denny,P. and Ashworth,A.
  TITLE     A zinc finger protein-encoding gene expressed in the post-meiotic
            phase of spermatogenesis
  JOURNAL   Gene 106 (2), 221-227 (1991)
   PUBMED   1937051
  REMARK    GeneRIF: PMID:1937051 pertains to studies in mouse.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC048382.7, BC041620.1,
            AY262259.1, AK128624.1, CK003500.1 and BU733585.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 11, 2005 this sequence version replaced NP_870992.1.
            
            Summary: The protein encoded by this gene contains several copies
            of zinc finger motif, which is commonly found in transcriptional
            regulatory proteins. Studies in mice show that this gene is
            expressed during embryonic development, and specifically in the
            testis in adult mice, suggesting that it may play a role in
            regulating genes in germ cells. Alternative splicing of this gene
            results in several transcript variants encoding different isoforms.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.154141.1,
                                           SRR1803615.73229.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000546148.6/ ENSP00000445451.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..614
                     /product="zinc finger and SCAN domain-containing protein 2
                     isoform 1"
                     /note="zfp-29; zinc finger protein 29 homolog; zinc finger
                     protein 854"
                     /calculated_mol_wt=69417
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L9.2)"
     Region          43..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L9.2)"
     Region          72..134
                     /region_name="SCAN"
                     /note="SCAN domain; pfam02023"
                     /db_xref="CDD:460417"
     Region          220..600
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          224..244
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          252..272
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(257,259,261,263..264,267..268,271,285,287,291..292,
                     295..296,299,313,315,317,319..320,323..324,327)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          280..300
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          308..328
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          336..356
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          364..384
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(369,371,373,375..376,379..380,383,397,399,403..404,
                     407..408,411,425,427,429,431..432,435..436,439)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          392..412
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          420..440
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          448..468
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(453,455,457,459..460,463..464,467,481,483,487..488,
                     491..492,495,509,511,513,515..516,519..520,523)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          476..496
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          504..524
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          532..552
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(537,539,541,543..544,547..548,551,565,567,571..572,
                     575..576,579,593,595,597,599..600,603..604,607)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          560..580
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          588..608
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..614
                     /gene="ZSCAN2"
                     /gene_synonym="ZFP29; ZNF854"
                     /coded_by="NM_181877.4:236..2080"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10329.2"
                     /db_xref="GeneID:54993"
                     /db_xref="HGNC:HGNC:20994"
ORIGIN      
        1 mmaadiprvt tplsslvqvp qeedrqeeev ttmileddsw vqeavlqedg pesepfpqsa
       61 gkggpqeevt rgpqgalgrl relcrrwlrp evhtkeqmlt mlpkeiqawl qehrpessee
      121 aaalvedltq tlqdsdfeiq sengencnqd mfenesrkif sempegesaq hsdgesdfer
      181 dagiqrlqgh spgedhgevv sqdrevgqli glqgtylgek pyecpqcgkt fsrkshlith
      241 erthtgekyy kcdecgksfs dgsnfsrhqt thtgekpykc rdcgksfsrs anlithqrih
      301 tgekpfqcae cgksfsrspn liahqrthtg ekpyscpecg ksfgnrssln thqgihtgek
      361 pyeckecges fsynsnlirh qrihtgekpy kctdcgqrfs qssalithrr thtgekpyqc
      421 secgksfsrs snlathrrth mvekpykcgv cgksfsqsss liahqgmhtg ekpyecltcg
      481 esfswssnll khqrihtgek pykcsecgkc fsqrsqlvvh qrthtgekpy kclmcgksfs
      541 rgsilvmhqr ahlgdkpyrc pecgkgfswn svliihqrih tgekpykcpe cgkgfsnssn
      601 fithqrthmk ekly
//
LOCUS       NP_001350295             353 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding protein 48 isoform 2 [Homo sapiens].
ACCESSION   NP_001350295 XP_006716213
VERSION     NP_001350295.1
DBSOURCE    REFSEQ: accession NM_001363366.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Siebert,A.E., Corll,J., Paige Gronevelt,J., Levine,L., Hobbs,L.M.,
            Kenney,C., Powell,C.L.E., Battistuzzi,F.U., Davenport,R., Mark
            Settles,A., Brad Barbazuk,W., Westrick,R.J., Madlambayan,G.J. and
            Lal,S.
  TITLE     Genetic analysis of human RNA binding motif protein 48 (RBM48)
            reveals an essential role in U12-type intron splicing
  JOURNAL   Genetics 222 (2) (2022)
   PUBMED   36040194
  REMARK    GeneRIF: Genetic analysis of human RNA binding motif protein 48
            (RBM48) reveals an essential role in U12-type intron splicing.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC044570.1, AC005156.1 and BX113088.1.
            
            On May 17, 2018 this sequence version replaced XP_006716213.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.38784.1,
                                           SRR3476690.888661.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..353
                     /product="RNA-binding protein 48 isoform 2"
                     /note="UPF0712 protein C7orf64; RNA-binding protein 48"
                     /calculated_mol_wt=40093
     Region          36..135
                     /region_name="RRM_RBM48"
                     /note="RNA recognition motif (RRM) found in RNA-binding
                     protein 48 (RBM48) and similar proteins; cd12442"
                     /db_xref="CDD:409876"
     Region          217..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RL73.1)"
     Region          280..302
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RL73.1)"
     CDS             1..353
                     /gene="RBM48"
                     /gene_synonym="C7orf64; HSPC304"
                     /coded_by="NM_001363366.1:20..1081"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:84060"
                     /db_xref="HGNC:HGNC:21785"
                     /db_xref="MIM:621015"
ORIGIN      
        1 massggelgs lfdhhvqrav cdtrakyreg rrpravkvyt inlesqylli qgvpavgvmk
       61 elverfalyg aieqynalde ypaedftevy likfmnlqsa rtakrkmdeq sffggllhvc
      121 yapefetvee trkklqmrka yvvkttenkd hyvtkkklvt ehkdtedfrq dfhsemsgfc
      181 kaalntsagn snpylpysce lplcyfsskc mcssggpvdr apdsskdgrn hhktmghynh
      241 ndslrktqin slknsvacpg aqkaitssea vdrfmprttq lqerkrrred drklgtflqt
      301 nptgneimig pllpdiskvd mhddslntta nlirhklkee iedytascsf lqr
//
LOCUS       NP_001357317             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357317 XP_006722693
VERSION     NP_001357317.1
DBSOURCE    REFSEQ: accession NM_001370388.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            On May 7, 2019 this sequence version replaced XP_006722693.1.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.118671.1,
                                           SRR1803617.42688.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370388.1:935..2584"
                     /note="isoform 1 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_079988                438 aa            linear   ROD 27-APR-2025
DEFINITION  sorting nexin-31 isoform 1 [Mus musculus].
ACCESSION   NP_079988 XP_916307
VERSION     NP_079988.3
DBSOURCE    REFSEQ: accession NM_025712.5
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Xu,N., Cai,Y., Li,J., Tao,T., Liu,C., Shen,Y., Li,X., Zhang,L.,
            Zhao,M., Shi,X., Li,J. and Huang,L.
  TITLE     An SNX31 variant underlies dominant familial exudative
            vitreoretinopathy-like pathogenesis
  JOURNAL   JCI Insight 8 (10), e167032 (2023)
   PUBMED   37053012
  REMARK    GeneRIF: An SNX31 variant underlies dominant familial exudative
            vitreoretinopathy-like pathogenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Vieira,N., Deng,F.M., Liang,F.X., Liao,Y., Chang,J., Zhou,G.,
            Zheng,W., Simon,J.P., Ding,M., Wu,X.R., Romih,R., Kreibich,G. and
            Sun,T.T.
  TITLE     SNX31: a novel sorting nexin associated with the
            uroplakin-degrading multivesicular bodies in terminally
            differentiated urothelial cells
  JOURNAL   PLoS One 9 (6), e99644 (2014)
   PUBMED   24914955
  REMARK    GeneRIF: These data support a model in which SNX31 mediates the
            endocytic degradation of uroplakins.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Yu,Z., Mannik,J., Soto,A., Lin,K.K. and Andersen,B.
  TITLE     The epidermal differentiation-associated Grainyhead gene Get1/Grhl3
            also regulates urothelial differentiation
  JOURNAL   EMBO J 28 (13), 1890-1903 (2009)
   PUBMED   19494835
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC137871.18.
            
            On or before Dec 7, 2005 this sequence version replaced
            XP_916307.1, NP_079988.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK034196.1, AK035226.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164133 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 14.48 cM"
     Protein         1..438
                     /product="sorting nexin-31 isoform 1"
                     /calculated_mol_wt=50603
     Region          4..106
                     /region_name="PX_SNX17_31"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexins 17 and 31; cd06885"
                     /db_xref="CDD:132795"
     Site            order(37..39,61..62,75)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132795"
     Region          119..209
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          270..384
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     CDS             1..438
                     /gene="Snx31"
                     /gene_synonym="4631426E05Rik"
                     /coded_by="NM_025712.5:61..1377"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS27430.1"
                     /db_xref="GeneID:66696"
                     /db_xref="MGI:MGI:1913946"
ORIGIN      
        1 mkmhfcipvs qqrpdalggr yvlysvyldg flfckvrysq lhrwdeqlrr vfgnclppfp
       61 pkyylamtta maeerrdqle rylqnvtadp rvtrsdvfte fltlvqlhtl nitiqnvela
      121 vflpdgrsik vegltsdtae rvlevmahkl glqpdlvgyf glfliqcfpe gklsvvkkla
      181 dfelpytslq ssemenckig lrkwyldpal dsmlmdcraa gdllymqavq diekewmkpt
      241 qaqreelkal qkkenqtkfl elsqevrhyg yvqldpctcn hpepgcgaql signneiscc
      301 itlpngqiqd iafqmsrvkc wqvtflgtll dtdgpqrtln qnlelrfqys edscqqwfvi
      361 ytkqafflss clkkmiserm tklteqspem qievpeqgrs kkhpsqpsqk vyfnflrkgk
      421 mkrsegdyvw dtlmeegl
//
LOCUS       NP_000215                430 aa            linear   PRI 27-APR-2025
DEFINITION  keratin, type I cytoskeletal 18 [Homo sapiens].
ACCESSION   NP_000215
VERSION     NP_000215.1
DBSOURCE    REFSEQ: accession NM_000224.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Pagano,S., Bakker,S.J.L., Juillard,C., Dullaart,R.P.F. and
            Vuilleumier,N.
  TITLE     Serum Level of Cytokeratin 18 (M65) as a Prognostic Marker of High
            Cardiovascular Disease Risk in Individuals with Non-Alcoholic Fatty
            Liver Disease
  JOURNAL   Biomolecules 13 (7), 1128 (2023)
   PUBMED   37509164
  REMARK    GeneRIF: Serum Level of Cytokeratin 18 (M65) as a Prognostic Marker
            of High Cardiovascular Disease Risk in Individuals with
            Non-Alcoholic Fatty Liver Disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Heinrich,S., Austgen,T., Castven,D., Hess,M., Labenz,C.,
            Kirstein,M., Zimpel,C., Stockhoff,L., Maasoumy,B., Heinrich,B.,
            Wedemeyer,H.H., Galle,P.R., Binder,H., Nguyen-Tat,M. and
            Marquardt,J.U.
  TITLE     Markers of cell death predict therapy response in patients with
            cirrhosis and hepatorenal syndrome
  JOURNAL   United European Gastroenterol J 11 (1), 92-102 (2023)
   PUBMED   36441143
  REMARK    GeneRIF: Markers of cell death predict therapy response in patients
            with cirrhosis and hepatorenal syndrome.
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Singh Bhangu,J., Macher-Beer,A., Schimek,V., Garmroudi,B.,
            Tamandl,D., Unger,L.W., Bachleitner-Hofmann,T. and Oehler,R.
  TITLE     Circulating caspase-cleaved cytokeratin 18 correlates with tumour
            burden and response to therapy in patients with colorectal cancer
            liver metastasis
  JOURNAL   Clin Chim Acta 538, 53-59 (2023)
   PUBMED   36375525
  REMARK    GeneRIF: Circulating caspase-cleaved cytokeratin 18 correlates with
            tumour burden and response to therapy in patients with colorectal
            cancer liver metastasis.
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Eguchi,A., Iwasa,M., Yamada,M., Tamai,Y., Shigefuku,R.,
            Hasegawa,H., Hirokawa,Y., Hayashi,A., Okuno,K., Matsushita,Y.,
            Nakatsuka,T., Enooku,K., Sakaguchi,K., Kobayashi,Y., Yamaguchi,T.,
            Watanabe,M., Takei,Y. and Nakagawa,H.
  TITLE     A new detection system for serum fragmented cytokeratin 18 as a
            biomarker reflecting histologic activities of human nonalcoholic
            steatohepatitis
  JOURNAL   Hepatol Commun 6 (8), 1987-1999 (2022)
   PUBMED   35485207
  REMARK    GeneRIF: A new detection system for serum fragmented cytokeratin 18
            as a biomarker reflecting histologic activities of human
            nonalcoholic steatohepatitis.
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Omary,M.B., Baxter,G.T., Chou,C.F., Riopel,C.L., Lin,W.Y. and
            Strulovici,B.
  TITLE     PKC epsilon-related kinase associates with and phosphorylates
            cytokeratin 8 and 18
  JOURNAL   J Cell Biol 117 (3), 583-593 (1992)
   PUBMED   1374067
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Heath,P., Elvin,P., Jenner,D., Gammack,A., Morten,J. and Markham,A.
  TITLE     Localisation of a cDNA clone for human cytokeratin 18 to chromosome
            17p11-p12 by in situ hybridisation
  JOURNAL   Hum Genet 85 (6), 669-670 (1990)
   PUBMED   1699878
REFERENCE   8  (residues 1 to 430)
  AUTHORS   Waseem,A., Gough,A.C., Spurr,N.K. and Lane,E.B.
  TITLE     Localization of the gene for human simple epithelial keratin 18 to
            chromosome 12 using polymerase chain reaction
  JOURNAL   Genomics 7 (2), 188-194 (1990)
   PUBMED   1693358
REFERENCE   9  (residues 1 to 430)
  AUTHORS   Waseem,A., Alexander,C.M., Steel,J.B. and Lane,E.B.
  TITLE     Embryonic simple epithelial keratins 8 and 18: chromosomal location
            emphasizes difference from other keratin pairs
  JOURNAL   New Biol 2 (5), 464-478 (1990)
   PUBMED   1705144
REFERENCE   10 (residues 1 to 430)
  AUTHORS   Romano,V., Hatzfeld,M., Magin,T.M., Zimbelmann,R., Franke,W.W.,
            Maier,G. and Ponstingl,H.
  TITLE     Cytokeratin expression in simple epithelia. I. Identification of
            mRNA coding for human cytokeratin no. 18 by a cDNA clone
  JOURNAL   Differentiation 30 (3), 244-253 (1986)
   PUBMED   2422083
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD106591.1, X12881.1 and
            AC107016.20.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: KRT18 encodes the type I intermediate filament chain
            keratin 18. Keratin 18, together with its filament partner keratin
            8, are perhaps the most commonly found members of the intermediate
            filament gene family. They are expressed in single layer epithelial
            tissues of the body. Mutations in this gene have been linked to
            cryptogenic cirrhosis. Two transcript variants encoding the same
            protein have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.34370.1,
                                           SRR3476690.69100.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000388835.4/ ENSP00000373487.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..430
                     /product="keratin, type I cytoskeletal 18"
                     /note="cytokeratin 18; cell proliferation-inducing gene 46
                     protein; keratin 18, type I"
                     /calculated_mol_wt=47927
     Region          2..79
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:7538124; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            30
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000269|PubMed:20729549,
                     ECO:0000269|PubMed:7538124. /id=CAR_000175; propagated
                     from UniProtKB/Swiss-Prot (P05783.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05784; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            31
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000269|PubMed:20729549,
                     ECO:0000269|PubMed:7538124. /id=CAR_000193; propagated
                     from UniProtKB/Swiss-Prot (P05783.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05784; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:15368451,
                     ECO:0000269|PubMed:9524113, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P05784; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            45
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            49
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000269|PubMed:20729549,
                     ECO:0000269|PubMed:7538124. /id=CAR_000194; propagated
                     from UniProtKB/Swiss-Prot (P05783.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2 and MAPKAPK3.
                     /evidence=ECO:0000250|UniProtKB:P05784; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK, PKC/PRKCE and AURKA.
                     /evidence=ECO:0000269|PubMed:15368451,
                     ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:7523419;
                     propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Site            55
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Region          70..373
                     /region_name="Necessary for interaction with PNN.
                     /evidence=ECO:0000269|PubMed:10809736"
                     /note="propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Region          77..128
                     /region_name="Interaction with TRADD.
                     /evidence=ECO:0000269|PubMed:11684708"
                     /note="propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Region          79..391
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          80..115
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Region          116..132
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Site            131
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Region          133..224
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Region          225..248
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Site            238..239
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3, caspase-6 or caspase-7;
                     propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Region          243..391
                     /region_name="Interaction with DNAJB6.
                     /evidence=ECO:0000269|PubMed:10954706"
                     /note="propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Region          249..387
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Site            271
                     /site_type="other"
                     /note="Stutter; propagated from UniProtKB/Swiss-Prot
                     (P05783.2)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            331
                     /site_type="other"
                     /note="Stutter; propagated from UniProtKB/Swiss-Prot
                     (P05783.2)"
     Region          388..430
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P05783.2)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     Site            426
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P05783.2)"
     CDS             1..430
                     /gene="KRT18"
                     /gene_synonym="CK-18; CYK18; K18"
                     /coded_by="NM_000224.3:57..1349"
                     /db_xref="CCDS:CCDS31809.1"
                     /db_xref="GeneID:3875"
                     /db_xref="HGNC:HGNC:6430"
                     /db_xref="MIM:148070"
ORIGIN      
        1 msfttrstfs tnyrslgsvq apsygarpvs saasvyagag gsgsrisvsr stsfrggmgs
       61 gglatgiagg lagmggiqne ketmqslndr lasyldrvrs letenrrles kirehlekkg
      121 pqvrdwshyf kiiedlraqi fantvdnari vlqidnarla addfrvkyet elamrqsven
      181 dihglrkvid dtnitrlqle teiealkeel lfmkknheee vkglqaqias sgltvevdap
      241 ksqdlakima diraqydela rknreeldky wsqqieestt vvttqsaevg aaettltelr
      301 rtvqsleidl dsmrnlkasl enslrevear yalqmeqlng illhlesela qtraegqrqa
      361 qeyeallnik vkleaeiaty rrlledgedf nlgdaldssn smqtiqkttt rrivdgkvvs
      421 etndtkvlrh
//
LOCUS       NP_065149                447 aa            linear   PRI 27-APR-2025
DEFINITION  protein phosphatase 2, regulatory subunit B, gamma isoform a [Homo
            sapiens].
ACCESSION   NP_065149 XP_005248034
VERSION     NP_065149.2
DBSOURCE    REFSEQ: accession NM_020416.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Daily,J.W., Liu,M. and Park,S.
  TITLE     High genetic risk scores of SLIT3, PLEKHA5 and PPP2R2C variants
            increased insulin resistance and interacted with coffee and
            caffeine consumption in middle-aged adults
  JOURNAL   Nutr Metab Cardiovasc Dis 29 (1), 79-89 (2019)
   PUBMED   30454882
  REMARK    GeneRIF: High genetic risk scores of SLIT3, PLEKHA5 and PPP2R2C
            variants increase susceptibility to increased insulin resistance by
            50% and its risk may be exacerbated by consuming more than 10 cups
            coffee/week or 220 mg caffeine/day.
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Serguienko,A., Hanes,R., Grad,I., Wang,M.Y., Myklebost,O. and
            Munthe,E.
  TITLE     PP2A Regulatory Subunit B55gamma is a Gatekeeper of Osteoblast
            Maturation and Lineage Maintenance
  JOURNAL   Stem Cells Dev 26 (19), 1375-1383 (2017)
   PUBMED   28805158
  REMARK    GeneRIF: B55gamma is induced by glucocorticoid receptor in human
            primary BM-MSCs during differentiation to osteoblast and is
            required for osteoblast morphogenesis.
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Bi,D., Ning,H., Liu,S., Que,X. and Ding,K.
  TITLE     miR-1301 promotes prostate cancer proliferation through directly
            targeting PPP2R2C
  JOURNAL   Biomed Pharmacother 81, 25-30 (2016)
   PUBMED   27261573
  REMARK    GeneRIF: miR-1301 promoted prostate cancer proliferation by
            inhibiting PPP2R2C.
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Hu,P., Yu,L., Zhang,M., Zheng,L., Zhao,Y., Fu,Q. and Zhao,S.
  TITLE     Molecular cloning and mapping of the brain-abundant B1gamma subunit
            of protein phosphatase 2A, PPP2R2C, to human chromosome 4p16
  JOURNAL   Genomics 67 (1), 83-86 (2000)
   PUBMED   10945473
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Torres,R., Ide,S.E., Dehejia,A., Baras,A. and Polymeropoulos,M.H.
  TITLE     Genomic structure and localization of the human protein phosphatase
            2A BRgamma regulatory subunit
  JOURNAL   DNA Res 6 (5), 323-327 (1999)
   PUBMED   10574460
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Strack,S., Zaucha,J.A., Ebner,F.F., Colbran,R.J. and Wadzinski,B.E.
  TITLE     Brain protein phosphatase 2A: developmental regulation and distinct
            cellular and subcellular localization by B subunits
  JOURNAL   J Comp Neurol 392 (4), 515-527 (1998)
   PUBMED   9514514
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Ruediger,R., Brewis,N., Ohst,K. and Walter,G.
  TITLE     Increasing the ratio of PP2A core enzyme to holoenzyme inhibits
            Tat-stimulated HIV-1 transcription and virus production
  JOURNAL   Virology 238 (2), 432-443 (1997)
   PUBMED   9400615
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114815.5, BM551976.1,
            AK093115.1 and AC116317.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jun 24, 2014 this sequence version replaced
            XP_005248034.1, NP_065149.1.
            
            Summary: The product of this gene belongs to the phosphatase 2
            regulatory subunit B family. Protein phosphatase 2 is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a gamma isoform of the regulatory subunit B55 subfamily.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.179732.1,
                                           SRR1660803.89891.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382599.9/ ENSP00000372042.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.1"
     Protein         1..447
                     /product="protein phosphatase 2, regulatory subunit B,
                     gamma isoform a"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2A1 B gamma subunit;
                     phosphoprotein phosphatase 2A BR gamma regulatory chain;
                     protein phosphatase 2, regulatory subunit B, gamma"
                     /calculated_mol_wt=51384
     Region          21..438
                     /region_name="CDC55"
                     /note="Serine/threonine protein phosphatase 2A, regulatory
                     subunit [Signal transduction mechanisms]; COG5170"
                     /db_xref="CDD:227498"
     Region          22..61
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T4.4)"
     Region          27..75
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          87..128
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T4.4)"
     Region          93..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..209
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T4.4)"
     Region          176..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          220..260
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T4.4)"
     Region          226..277
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          279..317
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T4.4)"
     Region          284..320
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          334..375
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T4.4)"
     Region          341..376
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          410..446
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2T4.4)"
     Region          415..438
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..447
                     /gene="PPP2R2C"
                     /gene_synonym="B55-GAMMA; B55gamma; IMYPNO; IMYPNO1; PR52;
                     PR55G"
                     /coded_by="NM_020416.4:386..1729"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3387.1"
                     /db_xref="GeneID:5522"
                     /db_xref="HGNC:HGNC:9306"
                     /db_xref="MIM:605997"
ORIGIN      
        1 mgedtdtrki nhsflrdhsy vteadiistv efnhtgella tgdkggrvvi fqrepeskna
       61 phsqgeydvy stfqshepef dylksleiee kinkikwlpq qnaahsllst ndktiklwki
      121 terdkrpegy nlkdeegklk dlstvtslqv pvlkpmdlmv evsprrifan ghtyhinsis
      181 vnsdcetyms addlrinlwh laitdrsfni vdikpanmed ltevitasef hphhcnlfvy
      241 ssskgslrlc dmraaalcdk hsklfeeped psnrsffsei issvsdvkfs hsgrymltrd
      301 yltvkvwdln mearpietyq vhdylrsklc slyendcifd kfecawngsd svimtgaynn
      361 ffrmfdrntk rdvtleasre sskpravlkp rrvcvggkrr rddisvdsld ftkkilhtaw
      421 hpaeniiaia atnnlyifqd kvnsdmh
//
LOCUS       NP_001349916             445 aa            linear   ROD 27-APR-2025
DEFINITION  tRNA-queuosine alpha-mannosyltransferase [Mus musculus].
ACCESSION   NP_001349916 XP_011237391
VERSION     NP_001349916.1
DBSOURCE    REFSEQ: accession NM_001362987.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL929120.7, BX293544.7, AL935057.7 and AL844891.7.
            
            On May 4, 2018 this sequence version replaced XP_011237391.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1-3 all encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR3363657.316778.1,
                                           SRR7974084.20251.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 27.27 cM"
     Protein         1..445
                     /product="tRNA-queuosine alpha-mannosyltransferase"
                     /EC_number="2.4.1.110"
                     /note="glycosyltransferase-like domain-containing protein
                     1"
                     /calculated_mol_wt=50886
     Region          2..164
                     /region_name="DUF3524"
                     /note="Domain of unknown function (DUF3524); pfam12038"
                     /db_xref="CDD:432280"
     Region          199..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BW56.2)"
     Region          <275..386
                     /region_name="Glycosyltransferase_GTB-type"
                     /note="glycosyltransferase family 1 and related proteins
                     with GTB topology; cd01635"
                     /db_xref="CDD:340816"
     Region          345..437
                     /region_name="RfaB"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0438"
                     /db_xref="CDD:440207"
     CDS             1..445
                     /gene="Gtdc1"
                     /gene_synonym="E330008O22Rik; QTMAN"
                     /coded_by="NM_001362987.1:146..1483"
                     /db_xref="CCDS:CCDS71050.1"
                     /db_xref="GeneID:227835"
                     /db_xref="MGI:MGI:2444269"
ORIGIN      
        1 msiviieafy ggshrqlvel lreelddcvl ytlpakkwhw rartaalyfs qnipssehyr
       61 tlfassvlnl telaalrpdl gklkkilyfh enqlvypvkk yqerdfqygy nqilsclvad
      121 vvvfnssfnm esfltsigkf lklipdhrpk dlesiirpkc qviyfpirfp dvsrfmpkhk
      181 iahlrrmlsl igdaaasqsv apcpqpgqrv sekspences ksdehpdlda eqealdnpsv
      241 hksgslpvsk enlpldpstl lcgaedpqrp lhitwphrwe hdkdpetflk ilmslkqlnl
      301 nfhvsvlget ftdtpdifse akkalgssvl hwgylprked yfrvlcmadv vistakheff
      361 gvamleavyc gcyplcpkal vypeifpaey lystpeqlsk rlksfckrpd iirkhlykge
      421 vapfswaalh gkfrslltte predl
//
LOCUS       NP_001356620             363 aa            linear   PRI 27-APR-2025
DEFINITION  deoxyhypusine synthase isoform e [Homo sapiens].
ACCESSION   NP_001356620
VERSION     NP_001356620.1
DBSOURCE    REFSEQ: accession NM_001369691.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Liao,T.Y., Huang,Y.T., Lee,T.F., Hsueh,P.R., Yu,C.J. and Chien,J.Y.
  TITLE     Clinical significance of mutations in dihydropteroate synthase in
            Pneumocystis jirovecii pneumonia among non-HIV-infected patients
  JOURNAL   Int J Antimicrob Agents 63 (1), 107019 (2024)
   PUBMED   37925109
  REMARK    GeneRIF: Clinical significance of mutations in dihydropteroate
            synthase in Pneumocystis jirovecii pneumonia among non-HIV-infected
            patients.
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Padgett,L.R., Shinkle,M.R., Rosario,S., Stewart,T.M., Foley,J.R.,
            Casero,R.A. Jr., Park,M.H., Chung,W.K. and Mastracci,T.L.
  TITLE     Deoxyhypusine synthase mutations alter the post-translational
            modification of eukaryotic initiation factor 5A resulting in
            impaired human and mouse neural homeostasis
  JOURNAL   HGG Adv 4 (3), 100206 (2023)
   PUBMED   37333770
  REMARK    GeneRIF: Deoxyhypusine synthase mutations alter the
            post-translational modification of eukaryotic initiation factor 5A
            resulting in impaired human and mouse neural homeostasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Wator,E., Wilk,P., Biela,A., Rawski,M., Zak,K.M., Steinchen,W.,
            Bange,G., Glatt,S. and Grudnik,P.
  TITLE     Cryo-EM structure of human eIF5A-DHS complex reveals the molecular
            basis of hypusination-associated neurodegenerative disorders
  JOURNAL   Nat Commun 14 (1), 1698 (2023)
   PUBMED   36973244
  REMARK    GeneRIF: Cryo-EM structure of human eIF5A-DHS complex reveals the
            molecular basis of hypusination-associated neurodegenerative
            disorders.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Becker,A.E., Wu,P.K. and Park,J.I.
  TITLE     eIF5A-Independent Role of DHPS in p21CIP1 and Cell Fate Regulation
  JOURNAL   Int J Mol Sci 22 (24), 13187 (2021)
   PUBMED   34947982
  REMARK    GeneRIF: eIF5A-Independent Role of DHPS in p21(CIP1) and Cell Fate
            Regulation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Yan,Y.P., Tao,Y. and Chen,K.Y.
  TITLE     Molecular cloning and functional expression of human deoxyhypusine
            synthase cDNA based on expressed sequence tag information
  JOURNAL   Biochem J 315 (Pt 2) (Pt 2), 429-434 (1996)
   PUBMED   8615810
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Bevec,D., Kappel,B., Jaksche,H., Csonga,R., Hauber,J., Klier,H. and
            Steinkasserer,A.
  TITLE     Molecular characterization of a cDNA encoding functional human
            deoxyhypusine synthase and chromosomal mapping of the corresponding
            gene locus
  JOURNAL   FEBS Lett 378 (2), 195-198 (1996)
   PUBMED   8549832
REFERENCE   8  (residues 1 to 363)
  AUTHORS   Joe,Y.A., Wolff,E.C. and Park,M.H.
  TITLE     Cloning and expression of human deoxyhypusine synthase cDNA.
            Structure-function studies with the recombinant enzyme and mutant
            proteins
  JOURNAL   J Biol Chem 270 (38), 22386-22392 (1995)
   PUBMED   7673224
REFERENCE   9  (residues 1 to 363)
  AUTHORS   Klier,H., Csonga,R., Steinkasserer,A., Wohl,T., Lottspeich,F. and
            Eder,J.
  TITLE     Purification and characterization of human deoxyhypusine synthase
            from HeLa cells
  JOURNAL   FEBS Lett 364 (2), 207-210 (1995)
   PUBMED   7750572
REFERENCE   10 (residues 1 to 363)
  AUTHORS   Joe,Y.A. and Park,M.H.
  TITLE     Structural features of the eIF-5A precursor required for
            posttranslational synthesis of deoxyhypusine
  JOURNAL   J Biol Chem 269 (41), 25916-25921 (1994)
   PUBMED   7929297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010422.7.
            
            Summary: This gene encodes a protein that is required for the
            formation of hypusine, a unique amino acid formed by the
            posttranslational modification of only one protein, eukaryotic
            translation initiation factor 5A. The encoded protein catalyzes the
            first step in hypusine formation by transferring the butylamine
            moiety of spermidine to a specific lysine residue of the eukaryotic
            translation initiation factor 5A precursor, forming an intermediate
            deoxyhypusine residue. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene.
            [provided by RefSeq, May 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.651036.1,
                                           SRR5189667.234586.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..363
                     /product="deoxyhypusine synthase isoform e"
                     /EC_number="2.5.1.46"
                     /note="migration-inducing gene 13"
                     /calculated_mol_wt=40567
     Region          44..>296
                     /region_name="DS"
                     /note="Deoxyhypusine synthase; pfam01916"
                     /db_xref="CDD:460382"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P49366.1)"
     CDS             1..363
                     /gene="DHPS"
                     /gene_synonym="DHS; DS; MIG13; NEDSSWI"
                     /coded_by="NM_001369691.1:115..1206"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="GeneID:1725"
                     /db_xref="HGNC:HGNC:2869"
                     /db_xref="MIM:600944"
ORIGIN      
        1 megslereap agalaavlkh sstlppestq vrgydfnrgv nyralleafg ttgfqatnfg
       61 ravqqvnami ekkleplsqd edqhadltqs rrpltsctif lgytsnliss giretirylv
      121 qhnmvdvlvt taggveedli kclaptylge fslrgkelre nginrignll vpnenyckfe
      181 dwlmpildqm vmeqntegvk wtpskmiarl gkeinnpesv yywaqknhip vfspaltdgs
      241 lgdmiffhsy knpglvldiv edlrlintqa ifakctgmii lgggvvkhhi ananlmvpdq
      301 trlspgarsg wmhspsrsml tppwsspclw lkplprrwmp scmrrtrter lrsqegltps
      361 siy
//
LOCUS       NP_001511               2109 aa            linear   PRI 27-APR-2025
DEFINITION  general transcription factor 3C polypeptide 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001511
VERSION     NP_001511.2
DBSOURCE    REFSEQ: accession NM_001520.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2109)
  AUTHORS   Basu,M., Bhatt,R., Sharma,A., Boopathi,R., Das,S. and Kundu,T.K.
  TITLE     The Largest Subunit of Human TFIIIC Complex, TFIIIC220, a Lysine
            Acetyltransferase Targets Histone H3K18
  JOURNAL   J Biochem 175 (2), 205-213 (2024)
   PUBMED   37963603
  REMARK    GeneRIF: The Largest Subunit of Human TFIIIC Complex, TFIIIC220, a
            Lysine Acetyltransferase Targets Histone H3K18.
            Erratum:[J Biochem. 2024 Apr 29;175(5):573. doi:
            10.1093/jb/mvae025. PMID: 38478019]
REFERENCE   2  (residues 1 to 2109)
  AUTHORS   Sachs,P., Bergmaier,P., Treutwein,K. and Mermoud,J.E.
  TITLE     The Conserved Chromatin Remodeler SMARCAD1 Interacts with TFIIIC
            and Architectural Proteins in Human and Mouse
  JOURNAL   Genes (Basel) 14 (9), 1793 (2023)
   PUBMED   37761933
  REMARK    GeneRIF: The Conserved Chromatin Remodeler SMARCAD1 Interacts with
            TFIIIC and Architectural Proteins in Human and Mouse.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2109)
  AUTHORS   Vezzoli,M., de Llobet Cucalon,L.I., Di Vona,C., Morselli,M.,
            Montanini,B., de la Luna,S., Teichmann,M., Dieci,G. and Ferrari,R.
  TITLE     TFIIIC as a Potential Epigenetic Modulator of Histone Acetylation
            in Human Stem Cells
  JOURNAL   Int J Mol Sci 24 (4), 3624 (2023)
   PUBMED   36835038
  REMARK    GeneRIF: TFIIIC as a Potential Epigenetic Modulator of Histone
            Acetylation in Human Stem Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2109)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 2109)
  AUTHORS   Crepaldi,L., Policarpi,C., Coatti,A., Sherlock,W.T.,
            Jongbloets,B.C., Down,T.A. and Riccio,A.
  TITLE     Binding of TFIIIC to sine elements controls the relocation of
            activity-dependent neuronal genes to transcription factories
  JOURNAL   PLoS Genet 9 (8), e1003699 (2013)
   PUBMED   23966877
  REMARK    GeneRIF: These findings reveal a novel and essential regulatory
            function of both SINEs and TFIIIC in mediating gene relocation and
            transcription
REFERENCE   6  (residues 1 to 2109)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     DNA topoisomerase I and PC4 can interact with human TFIIIC to
            promote both accurate termination and transcription reinitiation by
            RNA polymerase III
  JOURNAL   Mol Cell 1 (5), 749-757 (1998)
   PUBMED   9660958
REFERENCE   7  (residues 1 to 2109)
  AUTHORS   Lagna,G., Kovelman,R., Sukegawa,J. and Roeder,R.G.
  TITLE     Cloning and characterization of an evolutionarily divergent
            DNA-binding subunit of mammalian TFIIIC
  JOURNAL   Mol Cell Biol 14 (5), 3053-3064 (1994)
   PUBMED   8164661
REFERENCE   8  (residues 1 to 2109)
  AUTHORS   L'Etoile,N.D., Fahnestock,M.L., Shen,Y., Aebersold,R. and Berk,A.J.
  TITLE     Human transcription factor IIIC box B binding subunit
  JOURNAL   Proc Natl Acad Sci U S A 91 (5), 1652-1656 (1994)
   PUBMED   8127861
REFERENCE   9  (residues 1 to 2109)
  AUTHORS   Kovelman,R. and Roeder,R.G.
  TITLE     Purification and characterization of two forms of human
            transcription factor IIIC
  JOURNAL   J Biol Chem 267 (34), 24446-24456 (1992)
   PUBMED   1447193
REFERENCE   10 (residues 1 to 2109)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP283960.1, BC137229.1, BC044857.2 and CA414192.1.
            
            On May 25, 2006 this sequence version replaced NP_001511.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX648143.1, CR627430.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356183.9/ ENSP00000348510.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2109
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.1"
     Protein         1..2109
                     /product="general transcription factor 3C polypeptide 1
                     isoform 1"
                     /note="general transcription factor 3C polypeptide 1;
                     general transcription factor IIIC, polypeptide 1 (alpha
                     subunit); TF3C-alpha; TFIIIC 220 kDa subunit; TFIIIC box
                     B-binding subunit; transcription factor IIIC subunit
                     alpha; transcription factor IIIC 220 kDa subunit; general
                     transcription factor IIIC, polypeptide 1, alpha 220kDa"
                     /calculated_mol_wt=238745
     Region          174..250
                     /region_name="B-block_TFIIIC"
                     /note="B-block binding subunit of TFIIIC; pfam04182"
                     /db_xref="CDD:367858"
     Region          467..521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Region          586..609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Region          611..707
                     /region_name="Tau138_eWH"
                     /note="extended winged-helix domain of tau138 and related
                     proteins; cd16169"
                     /db_xref="CDD:320085"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q12789.4)"
     Region          718..775
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Region          836..857
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Region          1059..1082
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1062
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1068
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Region          1202..1241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12789.4)"
     Region          1608..1631
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1611
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12789.4)"
     Region          <1762..1956
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          1823..1961
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1856
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1865
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1868
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K284; propagated from
                     UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1911
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12789.4)"
     Site            1969
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q12789.4)"
     CDS             1..2109
                     /gene="GTF3C1"
                     /gene_synonym="TFIIIC; TFIIIC220; TFIIICalpha"
                     /coded_by="NM_001520.4:24..6353"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32414.1"
                     /db_xref="GeneID:2975"
                     /db_xref="HGNC:HGNC:4664"
                     /db_xref="MIM:603246"
ORIGIN      
        1 mdalesllde valegldglc lpalwsrlet rvppfplple pctqeflwra lathpgisfy
       61 eeprerpdlq lqdryeeidl etgilesrrd pvaledvypi hmilenkdgi qgscryfker
      121 knitndirtk slqprctmve afdrwgkkli ivasqamryr aligqegdpd lklpdfsyci
      181 lerlgrsrwq gelqrdlhtt afkvdagklh yhrkilnkng litmqshvir lptgaqqhsi
      241 llllnrfhvd rrskydilme klsvmlstrt nhietlgklr eelglcertf krlyqymlna
      301 glakvvslrl qeihpecgpc ktkkgtdvmv rclkllkefk rndhdddede evisktvppv
      361 divferdmlt qtydlierrg tkgisqaeir vamnvgklea rmlcrllqrf kvvkgfmede
      421 grqrttkyis cvfaeesdls rqyqrekars ellttvslas mqeesllpeg edtflsesds
      481 eeerssskrr grgsqkdtra sanlrpktqp hhstptkggw kvvnlhplkk qppsfpgaae
      541 eracqslasr dslldtssvs epnvsfvshc adsnsgdiav ieevrmenpk esssslktgr
      601 hssgqdkphe tyrllkrrnl iieavtnlrl ieslftiqkm imdqekqegv stkcckksiv
      661 rlvrnlseeg llrlyrttvi qdgikkkvdl vvhpsmdqnd plvrsaieqv rfrisnssta
      721 nrvktsqppv pqgeaeedsq gkegpsgsgd sqlsassrse sgrmkksdnk mgitplrnyh
      781 pivvpglgrs lgflpkmprl rvvhmflwyl iyghpasntv ekpsfiserr tikqesgrag
      841 vrpsssgsaw eacseapskg sqdgvtweae velatetvyv ddaswmryip pipvhrdfgf
      901 gwalvsdill clplsifiqi vqvsykvdnl eeflndplkk htlirflprp irqqllykrr
      961 yifsvvenlq rlcymgllqf gptekfqdkd qvfiflkkna vivdtticdp hynlarssrp
     1021 ferrlyvlns mqdvenywfd lqcvclntpl gvvrcprvrk nsstdqgsde egslqkeqes
     1081 amdkhnlerk camleyttgs revvdeglip gdglgaagld ssfyghlkrn wiwtsyiinq
     1141 akkentaaen gltvrlqtfl skrpmplsar gnsrlniwge arvgselcag weeqfevdre
     1201 psldrnrrvr ggksqkrkrl kkdpgkkikr kkkgefpgek skrlryhdea dqsalqrmtr
     1261 lrvtwsmqed gllvlcrias nvlntkvkgp fvtwqvvrdi lhatfeesld ktshsvgrra
     1321 ryivknpqay lnykvclaev yqdkalvgdf mnrrgdyddp kvcanefkef veklkekfss
     1381 alrnsnleip dtlqelfary rvlaigdekd qtrkedelns vddihflvlq nliqstlals
     1441 dsqmksyqsf qtfrlyreyk dhvlvkafme cqkrslvnrr rvnhtlgpkk nralpfvpms
     1501 yqlsqtyyri ftwrfpstic tesfqfldrm raagkldqpd rfsfkdqdnn eptndmvafs
     1561 ldgpggncva vltlfslgli svdvripeqi ivvdssmven evikslgkdg sleddedeed
     1621 dldegvggkr rsmevkpaqa shtnyllmrg yyspgivstr nlnpndsivv nscqmkfqlr
     1681 ctpvparlrp aaapleeltm gtsclpdtft klinpqentc sleefvlqle lsgyspedlt
     1741 aaleileaii atgcfgidke elrrrfsale kagggrtrtf adciqalleq hqvlevggnt
     1801 arlvamgsaw pwllhsvrlk dredadiqre dpqarplegs ssedsppegq appshsprgt
     1861 krraswasen getdaegtqm tpakrpalqd snlapslgpg aedgaeaqap spppaledta
     1921 aagaaqedqe gvgefsspgq eqlsgqaqpp egsedprgft esfgaanisq aarerdcesv
     1981 cfigrpwrvv dghlnlpvck gmmeamlyhi mtrpgipess llrhyqgvlq pvavlellqg
     2041 leslgcirkr wlrkprpvsl fstpvveeve vpssldespm afyeptldct lrlgrvfphe
     2101 vnwnkwihl
//
LOCUS       NP_060904                419 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF130 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_060904
VERSION     NP_060904.2
DBSOURCE    REFSEQ: accession NM_018434.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Zhang,J., Chen,W., Du,J., Chu,L., Zhou,Z., Zhong,W., Liu,D.,
            Huang,H., Huang,Y., Qiao,Y., Meng,X., Zou,F., Cai,S. and Dong,H.
  TITLE     RNF130 protects against pulmonary fibrosis through suppressing
            aerobic glycolysis by mediating c-myc ubiquitination
  JOURNAL   Int Immunopharmacol 117, 109985 (2023)
   PUBMED   36893517
  REMARK    GeneRIF: RNF130 protects against pulmonary fibrosis through
            suppressing aerobic glycolysis by mediating c-myc ubiquitination.
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Li,Z., Wong,K.Y., Calin,G.A., Chng,W.J., Chan,G.C. and Chim,C.S.
  TITLE     Epigenetic silencing of miR-340-5p in multiple myeloma: mechanisms
            and prognostic impact
  JOURNAL   Clin Epigenetics 11 (1), 71 (2019)
   PUBMED   31064412
  REMARK    GeneRIF: In myeloma cell lines but not normal plasma cells, DNA
            methylation correlated inversely with the expression of both
            miR-340 and RNF130. RNF130/miR-340 methylation at diagnosis was
            associated with inferior overall survival.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Kim,S.J., Lee,S.Y., Lee,C., Kim,I., An,H.J., Kim,J.Y., Baek,K.H.,
            Kim,E.J., Kim,J.M., Lee,J.B., Lee,J.W., Jung,W.W., Chun,T. and
            Oh,Y.K.
  TITLE     Differential expression profiling of genes in a complete
            hydatidiform mole using cDNA microarray analysis
  JOURNAL   Gynecol Oncol 103 (2), 654-660 (2006)
   PUBMED   16797685
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Guais,A., Siegrist,S., Solhonne,B., Jouault,H., Guellaen,G. and
            Bulle,F.
  TITLE     h-Goliath, paralog of GRAIL, is a new E3 ligase protein, expressed
            in human leukocytes
  JOURNAL   Gene 374, 112-120 (2006)
   PUBMED   16549277
  REMARK    GeneRIF: GOLIATH, a paralog of GRAIL, is a new E3 ligase protein,
            expressed in leukocytes.
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Guais,A., Solhonne,B., Melaine,N., Guellaen,G. and Bulle,F.
  TITLE     Goliath, a ring-H2 mitochondrial protein, regulated by luteinizing
            hormone/human chorionic gonadotropin in rat leydig cells
  JOURNAL   Biol Reprod 70 (1), 204-213 (2004)
   PUBMED   13679316
  REMARK    GeneRIF: Cloning and functional analysis of the rat counterpart.
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Baker,S.J. and Reddy,E.P.
  TITLE     Cloning of murine G1RP, a novel gene related to Drosophila
            melanogaster g1
  JOURNAL   Gene 248 (1-2), 33-40 (2000)
   PUBMED   10806348
  REMARK    GeneRIF: Cloning and functional analysis of the mouse counterpart.
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB209800.1, AK313089.1,
            BC017100.1, BP390145.1, DB572650.2 and AA339219.1.
            
            On Apr 11, 2003 this sequence version replaced NP_060904.1.
            
            Summary: The protein encoded by this gene contains a RING finger
            motif and is similar to g1, a Drosophila zinc-finger protein that
            is expressed in mesoderm and involved in embryonic development. The
            expression of the mouse counterpart was found to be upregulated in
            myeloblastic cells following IL3 deprivation, suggesting that this
            gene may regulate growth factor withdrawal-induced apoptosis of
            myeloid precursor cells. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.114642.1,
                                           SRR1660807.217301.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000521389.6/ ENSP00000430237.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..419
                     /product="E3 ubiquitin-protein ligase RNF130 isoform 1
                     precursor"
                     /EC_number="2.3.2.27"
                     /note="g1-related zinc finger protein; goliath homolog; E3
                     ubiquitin-protein ligase RNF130; RING-type E3 ubiquitin
                     transferase RNF130"
                     /calculated_mol_wt=43695
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2728
     mat_peptide     28..419
                     /product="E3 ubiquitin-protein ligase RNF130.
                     /id=PRO_0000030718"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XS8.1)"
                     /calculated_mol_wt=43695
     Site            29
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XS8.1)"
     Region          40..179
                     /region_name="PA_GRAIL_like"
                     /note="PA _GRAIL_like: Protease-associated (PA) domain
                     GRAIL-like. This group includes PA domain containing E3
                     (ubiquitin ligases) similar to human GRAIL (gene related
                     to anergy in lymphocytes) protein. Proteins in this group
                     contain a C3H2C3 RING finger. E3...; cd02122"
                     /db_xref="CDD:239037"
     Site            40
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q86XS8.1)"
     Site            112
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XS8.1)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XS8.1)"
     Site            140..142
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:239037"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XS8.1)"
     Site            189
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XS8.1)"
     Site            195..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XS8.1)"
     Region          <197..>306
                     /region_name="HRD1"
                     /note="HRD ubiquitin ligase complex, ER membrane component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5243"
                     /db_xref="CDD:227568"
     Region          262..310
                     /region_name="RING-H2_RNF130"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 130 (RNF130) and similar proteins; cd16803"
                     /db_xref="CDD:319717"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q86XS8.1)"
     CDS             1..419
                     /gene="RNF130"
                     /gene_synonym="G1RP; G1RZFP; GOLIATH; GP"
                     /coded_by="NM_018434.6:58..1317"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4451.1"
                     /db_xref="GeneID:55819"
                     /db_xref="HGNC:HGNC:18280"
                     /db_xref="MIM:619163"
ORIGIN      
        1 mscagragpa rlaalalltc slwparadna sqeyytalin vtvqepgrga pltfridrgr
       61 ygldspkaev rgqvlaplpl hgvadhlgcd pqtrffvppn ikqwiallqr gnctfkekis
      121 raafhnavav viynnkskee pvtmthpgtg diiavmitel rgkdilsyle knisvqmtia
      181 vgtrmppknf srgslvfvsi sfivlmiiss awlifyfiqk irytnardrn qrrlgdaakk
      241 aisklttrtv kkgdketdpd fdhcavcies ykqndvvril pckhvfhksc vdpwlsehct
      301 cpmcklnilk algivpnlpc tdnvafdmer ltrtqavnrr salgdlagdn slgleplrts
      361 gisplpqdge ltprtgeini avtkewfiia sfgllsaltl cymiiratas lnanevewf
//
LOCUS       NP_001354772             256 aa            linear   PRI 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 6 [Homo sapiens].
ACCESSION   NP_001354772
VERSION     NP_001354772.1
DBSOURCE    REFSEQ: accession NM_001367843.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Lu,J., Li,H., Zhang,H., Lin,Z., Xu,C., Xu,X., Hu,L., Luan,Z.,
            Lou,Y. and Tang,S.
  TITLE     The distal arthrogryposis-linked p.R63C variant promotes the
            stability and nuclear accumulation of TNNT3
  JOURNAL   J Clin Lab Anal 35 (12), e24089 (2021)
   PUBMED   34766372
  REMARK    GeneRIF: The distal arthrogryposis-linked p.R63C variant promotes
            the stability and nuclear accumulation of TNNT3.
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Nunez Lopez,Y.O., Messi,M.L., Pratley,R.E., Zhang,T. and Delbono,O.
  TITLE     Troponin T3 associates with DNA consensus sequence that overlaps
            with p53 binding motifs
  JOURNAL   Exp Gerontol 108, 35-40 (2018)
   PUBMED   29596868
  REMARK    GeneRIF: The TnT3 appears to contribute to age-related sarcopenia
            and possibly other age-related deficiencies such as muscle insulin
            resistance and beta cell dysfunction by interacting with
            TnT3-binding sequences in the promoter area of p53-related genes,
            among others, and consequently modulating the transcriptional
            regulation of these target genes.
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Wei,B. and Jin,J.P.
  TITLE     TNNT1, TNNT2, and TNNT3: Isoform genes, regulation, and
            structure-function relationships
  JOURNAL   Gene 582 (1), 1-13 (2016)
   PUBMED   26774798
  REMARK    GeneRIF: Three homologous genes have evolved in vertebrates to
            encode three muscle type-specific TnT isoforms: TNNT1 for slow
            skeletal muscle TnT, TNNT2 for cardiac muscle TnT, and TNNT3 for
            fast skeletal muscle TnT.
            Review article
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Vorster,A.A., Beighton,P. and Ramesar,R.S.
  TITLE     Digitotalar dysmorphism: Molecular elucidation
  JOURNAL   S Afr Med J 106 (3), 253-255 (2016)
   PUBMED   26915936
  REMARK    GeneRIF: The presence of the p.(Arg63His) missense mutation at
            position 63 of TNNT3 was confirmed through direct cycle sequencing
            of genomic DNA in six affected South African family members for
            whom DNA had been archived.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Lindstrom,S., Thompson,D.J., Paterson,A.D., Li,J., Gierach,G.L.,
            Scott,C., Stone,J., Douglas,J.A., dos-Santos-Silva,I.,
            Fernandez-Navarro,P., Verghase,J., Smith,P., Brown,J., Luben,R.,
            Wareham,N.J., Loos,R.J., Heit,J.A., Pankratz,V.S., Norman,A.,
            Goode,E.L., Cunningham,J.M., deAndrade,M., Vierkant,R.A., Czene,K.,
            Fasching,P.A., Baglietto,L., Southey,M.C., Giles,G.G., Shah,K.P.,
            Chan,H.P., Helvie,M.A., Beck,A.H., Knoblauch,N.W., Hazra,A.,
            Hunter,D.J., Kraft,P., Pollan,M., Figueroa,J.D., Couch,F.J.,
            Hopper,J.L., Hall,P., Easton,D.F., Boyd,N.F., Vachon,C.M. and
            Tamimi,R.M.
  TITLE     Genome-wide association study identifies multiple loci associated
            with both mammographic density and breast cancer risk
  JOURNAL   Nat Commun 5, 5303 (2014)
   PUBMED   25342443
  REMARK    Erratum:[Nat Commun. 2015 Sep 09;6:8358. doi: 10.1038/ncomms9358.
            PMID: 26349435]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Stefancsik,R., Randall,J.D., Mao,C. and Sarkar,S.
  TITLE     Structure and sequence of the human fast skeletal troponin T
            (TNNT3) gene: insight into the evolution of the gene and the origin
            of the developmentally regulated isoforms
  JOURNAL   Comp Funct Genomics 4 (6), 609-625 (2003)
   PUBMED   18629027
  REMARK    Erratum:[Comp Funct Genomics. 2004;5(2):205]
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Briggs,M.M., Maready,M., Schmidt,J.M. and Schachat,F.
  TITLE     Identification of a fetal exon in the human fast troponin T gene
  JOURNAL   FEBS Lett 350 (1), 37-40 (1994)
   PUBMED   8062920
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Wu,Q.L., Jha,P.K., Raychowdhury,M.K., Du,Y., Leavis,P.C. and
            Sarkar,S.
  TITLE     Isolation and characterization of human fast skeletal beta troponin
            T cDNA: comparative sequence analysis of isoforms and insight into
            the evolution of members of a multigene family
  JOURNAL   DNA Cell Biol 13 (3), 217-233 (1994)
   PUBMED   8172653
REFERENCE   10 (residues 1 to 256)
  AUTHORS   Chong,P.C. and Hodges,R.S.
  TITLE     Photochemical cross-linking between rabbit skeletal troponin
            subunits. Troponin I-troponin T interactions
  JOURNAL   J Biol Chem 257 (19), 11667-11672 (1982)
   PUBMED   7118902
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC051649.21.
            
            Summary: The binding of Ca(2+) to the trimeric troponin complex
            initiates the process of muscle contraction. Increased Ca(2+)
            concentrations produce a conformational change in the troponin
            complex that is transmitted to tropomyosin dimers situated along
            actin filaments. The altered conformation permits increased
            interaction between a myosin head and an actin filament which,
            ultimately, produces a muscle contraction. The troponin complex has
            protein subunits C, I, and T. Subunit C binds Ca(2+) and subunit I
            binds to actin and inhibits actin-myosin interaction. Subunit T
            binds the troponin complex to the tropomyosin complex and is also
            required for Ca(2+)-mediated activation of actomyosin ATPase
            activity. There are 3 different troponin T genes that encode
            tissue-specific isoforms of subunit T for fast skeletal-, slow
            skeletal-, and cardiac-muscle. This gene encodes fast skeletal
            troponin T protein; also known as troponin T type 3. Alternative
            splicing results in multiple transcript variants encoding
            additional distinct troponin T type 3 isoforms. A developmentally
            regulated switch between fetal/neonatal and adult troponin T type 3
            isoforms occurs. Additional splice variants have been described but
            their biological validity has not been established. Mutations in
            this gene may cause distal arthrogryposis multiplex congenita type
            2B (DA2B). [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279831.7263.1, DRR138525.641883.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158800, SAMEA2162946
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..256
                     /product="troponin T, fast skeletal muscle isoform 6"
                     /note="troponin T, fast skeletal muscle; troponin T type 3
                     (skeletal, fast)"
                     /calculated_mol_wt=30228
     Region          60..196
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..256
                     /gene="TNNT3"
                     /gene_synonym="beta-TnTF; DA2B2; TNTF"
                     /coded_by="NM_001367843.1:45..815"
                     /note="isoform 6 is encoded by transcript variant 8"
                     /db_xref="GeneID:7140"
                     /db_xref="HGNC:HGNC:11950"
                     /db_xref="MIM:600692"
ORIGIN      
        1 msdeeveqve eqyeeeeeaq eeaaevheev hepeekprpk ltapkipege kvdfddiqkk
       61 rqnkdlmelq alidshfear kkeeeelval keriekrrae raeqqrirae kererqnrla
      121 eekarreeed akrraeddlk kkkalssmga nyssylakad qkrgkkqtar emkkkilaer
      181 rkplnidhlg edklrdkake lwetlhqlei dkfefgeklk rqkydimnvr arvqmlakfs
      241 kkagtpakgk vggrwk
//
LOCUS       NP_004040                175 aa            linear   PRI 27-APR-2025
DEFINITION  bcl-2-related protein A1 isoform 1 [Homo sapiens].
ACCESSION   NP_004040
VERSION     NP_004040.1
DBSOURCE    REFSEQ: accession NM_004049.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Zhao,S., Wang,Q., Zhang,X., Ma,B., Shi,Y., Yin,Y., Kong,W.,
            Zhang,W., Li,J. and Yang,H.
  TITLE     MARCH5-mediated downregulation of ACC2 promotes fatty acid
            oxidation and tumor progression in ovarian cancer
  JOURNAL   Free Radic Biol Med 212, 464-476 (2024)
   PUBMED   38211832
  REMARK    GeneRIF: MARCH5-mediated downregulation of ACC2 promotes fatty acid
            oxidation and tumor progression in ovarian cancer.
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Dai,J., SoRelle,E.D., Heckenberg,E., Song,L., Cable,J.M.,
            Crawford,G.E. and Luftig,M.A.
  TITLE     Epstein-Barr virus induces germinal center light zone chromatin
            architecture and promotes survival through enhancer looping at the
            BCL2A1 locus
  JOURNAL   mBio 15 (1), e0244423 (2024)
   PUBMED   38059622
  REMARK    GeneRIF: Epstein-Barr virus induces germinal center light zone
            chromatin architecture and promotes survival through enhancer
            looping at the BCL2A1 locus.
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Decombis,S., Bellanger,C., Le Bris,Y., Madiot,C., Jardine,J.,
            Santos,J.C., Boulet,D., Dousset,C., Menard,A., Kervoelen,C.,
            Douillard,E., Moreau,P., Minvielle,S., Moreau-Aubry,A.,
            Tessoulin,B., Roue,G., Bidere,N., Le Gouill,S.,
            Pellat-Deceunynck,C. and Chiron,D.
  TITLE     CARD11 gain of function upregulates BCL2A1 expression and promotes
            resistance to targeted therapies combination in B-cell lymphoma
  JOURNAL   Blood 142 (18), 1543-1555 (2023)
   PUBMED   37562004
  REMARK    GeneRIF: CARD11 gain of function upregulates BCL2A1 expression and
            promotes resistance to targeted therapies combination in B-cell
            lymphoma.
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Gao,L., Ye,Z., Peng,S., Lei,P., Song,P., Li,Z., Zhou,L., Hua,Q.,
            Cheng,L., Wei,H., Liu,J. and Cai,Q.
  TITLE     BCL2A1 is associated with tumor-associated macrophages and
            unfavorable prognosis in human gliomas
  JOURNAL   Aging (Albany NY) 15 (20), 11611-11638 (2023)
   PUBMED   37889551
  REMARK    GeneRIF: BCL2A1 is associated with tumor-associated macrophages and
            unfavorable prognosis in human gliomas.
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Li,J., Sun,L., Xie,F., Shao,T., Wu,S., Li,X., Zhang,L. and Wang,R.
  TITLE     MiR-3976 regulates HCT-8 cell apoptosis and parasite burden by
            targeting BCL2A1 in response to Cryptosporidium parvum infection
  JOURNAL   Parasit Vectors 16 (1), 221 (2023)
   PUBMED   37415254
  REMARK    GeneRIF: MiR-3976 regulates HCT-8 cell apoptosis and parasite
            burden by targeting BCL2A1 in response to Cryptosporidium parvum
            infection.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Karsan,A., Yee,E. and Harlan,J.M.
  TITLE     Endothelial cell death induced by tumor necrosis factor-alpha is
            inhibited by the Bcl-2 family member, A1
  JOURNAL   J Biol Chem 271 (44), 27201-27204 (1996)
   PUBMED   8910286
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Karsan,A., Yee,E., Kaushansky,K. and Harlan,J.M.
  TITLE     Cloning of human Bcl-2 homologue: inflammatory cytokines induce
            human A1 in cultured endothelial cells
  JOURNAL   Blood 87 (8), 3089-3096 (1996)
   PUBMED   8605321
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Choi,S.S., Park,I.C., Yun,J.W., Sung,Y.C., Hong,S.I. and Shin,H.S.
  TITLE     A novel Bcl-2 related gene, Bfl-1, is overexpressed in stomach
            cancer and preferentially expressed in bone marrow
  JOURNAL   Oncogene 11 (9), 1693-1698 (1995)
   PUBMED   7478596
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Savitsky,K., Sfez,S., Tagle,D.A., Ziv,Y., Sartiel,A., Collins,F.S.,
            Shiloh,Y. and Rotman,G.
  TITLE     The complete sequence of the coding region of the ATM gene reveals
            similarity to cell cycle regulators in different species
  JOURNAL   Hum Mol Genet 4 (11), 2025-2032 (1995)
   PUBMED   8589678
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Lin,E.Y., Orlofsky,A., Berger,M.S. and Prystowsky,M.B.
  TITLE     Characterization of A1, a novel hemopoietic-specific early-response
            gene with sequence similarity to bcl-2
  JOURNAL   J Immunol 151 (4), 1979-1988 (1993)
   PUBMED   8345191
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG198875.1 and U27467.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the BCL-2 protein family.
            The proteins of this family form hetero- or homodimers and act as
            anti- and pro-apoptotic regulators that are involved in a wide
            variety of cellular activities such as embryonic development,
            homeostasis and tumorigenesis. The protein encoded by this gene is
            able to reduce the release of pro-apoptotic cytochrome c from
            mitochondria and block caspase activation. This gene is a direct
            transcription target of NF-kappa B in response to inflammatory
            mediators, and is up-regulated by different extracellular signals,
            such as granulocyte-macrophage colony-stimulating factor (GM-CSF),
            CD40, phorbol ester and inflammatory cytokine TNF and IL-1, which
            suggests a cytoprotective function that is essential for lymphocyte
            activation as well as cell survival. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y09397.1, SRR1163655.13913.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267953.4/ ENSP00000267953.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..175
                     /product="bcl-2-related protein A1 isoform 1"
                     /note="hematopoietic BCL2-related protein A1; bcl2-L-5;
                     protein BFL-1; bcl-2-like protein 5; hemopoietic-specific
                     early response protein"
                     /calculated_mol_wt=20001
     Region          10..146
                     /region_name="Bcl-2_like"
                     /note="Apoptosis regulator proteins of the Bcl-2 family,
                     named after B-cell lymphoma 2. This alignment model spans
                     what have been described as Bcl-2 homology regions BH1,
                     BH2, BH3, and BH4. Many members of this family have an
                     additional C-terminal transmembrane...; cd06845"
                     /db_xref="CDD:132900"
     Site            37..45
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(40..41,43..44,48,51..52,69..70,73..74,77..78,85,
                     87..88,90..91,95,99)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          77..97
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16548.1)"
     Site            order(77..79,84..96)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          132..147
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16548.1)"
     Site            order(132..141,143..146)
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     CDS             1..175
                     /gene="BCL2A1"
                     /gene_synonym="ACC-1; ACC-2; ACC1; ACC2; BCL2L5; BFL1;
                     GRS; HBPA1"
                     /coded_by="NM_004049.4:78..605"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10312.1"
                     /db_xref="GeneID:597"
                     /db_xref="HGNC:HGNC:991"
                     /db_xref="MIM:601056"
ORIGIN      
        1 mtdcefgyiy rlaqdylqcv lqipqpgsgp sktsrvlqnv afsvqkevek nlkscldnvn
       61 vvsvdtartl fnqvmekefe dgiinwgriv tifafegili kkllrqqiap dvdtykeisy
      121 fvaefimnnt gewirqnggw engfvkkfep ksgwmtflev tgkicemlsl lkqyc
//
LOCUS       NP_002156                155 aa            linear   PRI 27-APR-2025
DEFINITION  DNA-binding protein inhibitor ID-1 isoform a [Homo sapiens].
ACCESSION   NP_002156
VERSION     NP_002156.2
DBSOURCE    REFSEQ: accession NM_002165.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Shang,S., Yang,C., Chen,F., Xiang,R.S., Zhang,H., Dai,S.Y., Liu,J.,
            Lv,X.X., Zhang,C., Liu,X.T., Zhang,Q., Lu,S.B., Song,J.W., Yu,J.J.,
            Zhou,J.C., Zhang,X.W., Cui,B., Li,P.P., Zhu,S.T., Zhang,H.Z. and
            Hua,F.
  TITLE     ID1 expressing macrophages support cancer cell stemness and limit
            CD8+ T cell infiltration in colorectal cancer
  JOURNAL   Nat Commun 14 (1), 7661 (2023)
   PUBMED   37996458
  REMARK    GeneRIF: ID1 expressing macrophages support cancer cell stemness
            and limit CD8[+] T cell infiltration in colorectal cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Nguyen,A., Sung,Y., Lee,S.H., Martin,C.E., Srikanth,S., Chen,W.,
            Kang,M.K., Kim,R.H., Park,N.H., Gwack,Y., Kim,Y. and Shin,K.H.
  TITLE     Orai3 Calcium Channel Contributes to Oral/Oropharyngeal Cancer
            Stemness through the Elevation of ID1 Expression
  JOURNAL   Cells 12 (18), 2225 (2023)
   PUBMED   37759448
  REMARK    GeneRIF: Orai3 Calcium Channel Contributes to Oral/Oropharyngeal
            Cancer Stemness through the Elevation of ID1 Expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Fei,M.Y., Wang,Y., Chang,B.H., Xue,K., Dong,F., Huang,D., Li,X.Y.,
            Li,Z.J., Hu,C.L., Liu,P., Wu,J.C., Yu,P.C., Hong,M.H., Chen,S.B.,
            Xu,C.H., Chen,B.Y., Jiang,Y.L., Liu,N., Zhao,C., Jin,J.C., Hou,D.,
            Chen,X.C., Ren,Y.Y., Deng,C.H., Zhang,J.Y., Zong,L.J., Wang,R.J.,
            Gao,F.F., Liu,H., Zhang,Q.L., Wu,L.Y., Yan,J., Shen,S., Chang,C.K.,
            Sun,X.J. and Wang,L.
  TITLE     The non-cell-autonomous function of ID1 promotes AML progression
            via ANGPTL7 from the microenvironment
  JOURNAL   Blood 142 (10), 903-917 (2023)
   PUBMED   37319434
  REMARK    GeneRIF: The non-cell-autonomous function of ID1 promotes AML
            progression via ANGPTL7 from the microenvironment.
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Ma,J., Wen,X., Xu,Z., Xia,P., Jin,Y., Lin,J. and Qian,J.
  TITLE     Abnormal regulation of miR-29b-ID1 signaling is involved in the
            process of decitabine resistance in leukemia cells
  JOURNAL   Cell Cycle 22 (10), 1215-1231 (2023)
   PUBMED   37032592
  REMARK    GeneRIF: Abnormal regulation of miR-29b-ID1 signaling is involved
            in the process of decitabine resistance in leukemia cells.
REFERENCE   5  (residues 1 to 155)
  AUTHORS   Tang,Y., Zhang,S., Li,J., Wu,C. and Fan,Q.
  TITLE     ID1 marks the tumorigenesis of pancreatic ductal adenocarcinoma in
            mouse and human
  JOURNAL   Sci Rep 12 (1), 13555 (2022)
   PUBMED   35941362
  REMARK    GeneRIF: ID1 marks the tumorigenesis of pancreatic ductal
            adenocarcinoma in mouse and human.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 155)
  AUTHORS   Mathew,S., Chen,W., Murty,V.V., Benezra,R. and Chaganti,R.S.
  TITLE     Chromosomal assignment of human ID1 and ID2 genes
  JOURNAL   Genomics 30 (2), 385-387 (1995)
   PUBMED   8586447
REFERENCE   7  (residues 1 to 155)
  AUTHORS   Zhu,W., Dahmen,J., Bulfone,A., Rigolet,M., Hernandez,M.C.,
            Kuo,W.L., Puelles,L., Rubenstein,J.L. and Israel,M.A.
  TITLE     Id gene expression during development and molecular cloning of the
            human Id-1 gene
  JOURNAL   Brain Res Mol Brain Res 30 (2), 312-326 (1995)
   PUBMED   7637581
REFERENCE   8  (residues 1 to 155)
  AUTHORS   Pagliuca,A., Bartoli,P.C., Saccone,S., Della Valle,G. and Lania,L.
  TITLE     Molecular cloning of ID4, a novel dominant negative
            helix-loop-helix human gene on chromosome 6p21.3-p22
  JOURNAL   Genomics 27 (1), 200-203 (1995)
   PUBMED   7665172
REFERENCE   9  (residues 1 to 155)
  AUTHORS   Deed,R.W., Jasiok,M. and Norton,J.D.
  TITLE     Nucleotide sequence of the cDNA encoding human helix-loop-helix
            Id-1 protein: identification of functionally conserved residues
            common to Id proteins
  JOURNAL   Biochim Biophys Acta 1219 (1), 160-162 (1994)
   PUBMED   8086456
REFERENCE   10 (residues 1 to 155)
  AUTHORS   Hara,E., Yamaguchi,T., Nojima,H., Ide,T., Campisi,J., Okayama,H.
            and Oda,K.
  TITLE     Id-related genes encoding helix-loop-helix proteins are required
            for G1 progression and are repressed in senescent human fibroblasts
  JOURNAL   J Biol Chem 269 (3), 2139-2145 (1994)
   PUBMED   8294468
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA839689.1, BC012420.1 and
            AI304595.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 1, 2003 this sequence version replaced NP_002156.1.
            
            Summary: The protein encoded by this gene is a helix-loop-helix
            (HLH) protein that can form heterodimers with members of the basic
            HLH family of transcription factors. The encoded protein has no DNA
            binding activity and therefore can inhibit the DNA binding and
            transcriptional activation ability of basic HLH proteins with which
            it interacts. This protein may play a role in cell growth,
            senescence, and differentiation. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform (a,
            also called ID-1H).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.26681.1, BM809372.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376112.4/ ENSP00000365280.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..155
                     /product="DNA-binding protein inhibitor ID-1 isoform a"
                     /note="inhibitor of differentiation 1; dJ857M17.1.2
                     (inhibitor of DNA binding 1, dominant negative
                     helix-loop-helix protein); class B basic helix-loop-helix
                     protein 24; inhibitor of DNA binding 1, HLH protein"
                     /calculated_mol_wt=16001
     Region          62..113
                     /region_name="bHLH_dnHLH_ID1"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     DNA-binding protein inhibitor ID1 and similar proteins;
                     cd19691"
                     /db_xref="CDD:381534"
     Site            order(65,68..69,72..73,75..76,79,91..92,95..96,98..99,
                     101..103,105..106,109,113)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381534"
     Region          98..111
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P41134.3)"
     CDS             1..155
                     /gene="ID1"
                     /gene_synonym="bHLHb24; ID"
                     /coded_by="NM_002165.4:100..567"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13185.1"
                     /db_xref="GeneID:3397"
                     /db_xref="HGNC:HGNC:5360"
                     /db_xref="MIM:600349"
ORIGIN      
        1 mkvasgstat aaagpscalk agktasgage vvrclseqsv aisrcaggag arlpalldeq
       61 qvnvllydmn gcysrlkelv ptlpqnrkvs kveilqhvid yirdlqleln sesevgtpgg
      121 rglpvrapls tlngeisalt aeaacvpadd rilcr
//
LOCUS       NP_659453                294 aa            linear   PRI 27-APR-2025
DEFINITION  glycine N-acyltransferase-like protein 2 [Homo sapiens].
ACCESSION   NP_659453
VERSION     NP_659453.3
DBSOURCE    REFSEQ: accession NM_145016.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Waluk,D.P., Sucharski,F., Sipos,L., Silberring,J. and Hunt,M.C.
  TITLE     Reversible lysine acetylation regulates activity of human glycine
            N-acyltransferase-like 2 (hGLYATL2): implications for production of
            glycine-conjugated signaling molecules
  JOURNAL   J Biol Chem 287 (20), 16158-16167 (2012)
   PUBMED   22408254
  REMARK    GeneRIF: acetylation of lysine(s) in hGLYATL2 regulates the enzyme
            activity, thus linking post-translational modification of proteins
            with the production of biological signaling molecules, the N-acyl
            glycines.
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Matsuo,M., Terai,K., Kameda,N., Matsumoto,A., Kurokawa,Y.,
            Funase,Y., Nishikawa,K., Sugaya,N., Hiruta,N. and Kishimoto,T.
  TITLE     Designation of enzyme activity of glycine-N-acyltransferase family
            genes and depression of glycine-N-acyltransferase in human
            hepatocellular carcinoma
  JOURNAL   Biochem Biophys Res Commun 420 (4), 901-906 (2012)
   PUBMED   22475485
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Waluk,D.P., Schultz,N. and Hunt,M.C.
  TITLE     Identification of glycine N-acyltransferase-like 2 (GLYATL2) as a
            transferase that produces N-acyl glycines in humans
  JOURNAL   FASEB J 24 (8), 2795-2803 (2010)
   PUBMED   20305126
  REMARK    GeneRIF: report on the characterization of human glycine
            N-acyltransferase-like 2 (hGLYATL2) and show that it synthesizes
            various N-acyl glycines.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001652.4, BC021682.1 and AW264415.1.
            
            On Jun 29, 2007 this sequence version replaced NP_659453.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF426250.1, BC021682.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2146982
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287275.6/ ENSP00000287275.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..294
                     /product="glycine N-acyltransferase-like protein 2"
                     /EC_number="2.3.1.13"
                     /note="glycine acyltransferase family-B; acyl-CoA:glycine
                     N-acyltransferase-like protein 2"
                     /calculated_mol_wt=34146
     Region          1..199
                     /region_name="Gly_acyl_tr_N"
                     /note="Aralkyl acyl-CoA:amino acid N-acyltransferase;
                     pfam06021"
                     /db_xref="CDD:461802"
     Site            19
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:22408254; propagated from
                     UniProtKB/Swiss-Prot (Q8WU03.1)"
     Region          202..290
                     /region_name="Gly_acyl_tr_C"
                     /note="Aralkyl acyl-CoA:amino acid N-acyltransferase,
                     C-terminal region; pfam08444"
                     /db_xref="CDD:117021"
     CDS             1..294
                     /gene="GLYATL2"
                     /gene_synonym="BXMAS2-10; GATF-B"
                     /coded_by="NM_145016.4:312..1196"
                     /db_xref="CCDS:CCDS41649.1"
                     /db_xref="GeneID:219970"
                     /db_xref="HGNC:HGNC:24178"
                     /db_xref="MIM:614762"
ORIGIN      
        1 mlvlhnsqkl qilyksleks ipesikvyga ifnikdknpf nmevlvdawp dyqivitrpq
       61 kqemkddqdh ytntyhiftk apdkleevls ysnvisweqt lqiqgcqegl deairkvats
      121 ksvqvdymkt ilfipelpkk hktssndkme lfevdddnke gnfsnmflda shaglvnehw
      181 afgknerslk yierclqdfl gfgvlgpegq lvswivmeqs celrmgytvp kyrhqgnmlq
      241 igyhlekyls qkeipfyfhv adnnekslqa lnnlgfkicp cgwhqwkctp kkyc
//
LOCUS       NP_079684                267 aa            linear   ROD 27-APR-2025
DEFINITION  alkaline ceramidase 3 isoform 1 [Mus musculus].
ACCESSION   NP_079684
VERSION     NP_079684.2
DBSOURCE    REFSEQ: accession NM_025408.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Li,F., Xu,R., Lin,C.L., Low,B.E., Cai,L., Li,S., Ji,P., Huang,L.,
            Wiles,M.V., Hannun,Y.A., Obeid,L.M., Chen,Y. and Mao,C.
  TITLE     Maternal and fetal alkaline ceramidase 2 is required for placental
            vascular integrity in mice
  JOURNAL   FASEB J 34 (11), 15252-15268 (2020)
   PUBMED   32959379
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Wang,K., Li,C., Lin,X., Sun,H., Xu,R., Li,Q., Wei,Y., Li,Y.,
            Qian,J., Liu,C., Zhang,Q., Yu,S., Cui,Z., Huang,X., Zhu,B., Zhou,J.
            and Mao,C.
  TITLE     Targeting alkaline ceramidase 3 alleviates the severity of
            nonalcoholic steatohepatitis by reducing oxidative stress
  JOURNAL   Cell Death Dis 11 (1), 28 (2020)
   PUBMED   31949129
  REMARK    GeneRIF: Targeting alkaline ceramidase 3 alleviates the severity of
            nonalcoholic steatohepatitis by reducing oxidative stress.
            Erratum:[Cell Death Dis. 2020 Mar 17;11(3):191. doi:
            10.1038/s41419-020-2396-1. PMID: 32184395]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Li,F., Xu,R., Low,B.E., Lin,C.L., Garcia-Barros,M., Schrandt,J.,
            Mileva,I., Snider,A., Luo,C.K., Jiang,X.C., Li,M.S., Hannun,Y.A.,
            Obeid,L.M., Wiles,M.V. and Mao,C.
  TITLE     Alkaline ceramidase 2 is essential for the homeostasis of plasma
            sphingoid bases and their phosphates
  JOURNAL   FASEB J 32 (6), 3058-3069 (2018)
   PUBMED   29401619
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Wang,K., Xu,R., Snider,A.J., Schrandt,J., Li,Y., Bialkowska,A.B.,
            Li,M., Zhou,J., Hannun,Y.A., Obeid,L.M., Yang,V.W. and Mao,C.
  TITLE     Alkaline ceramidase 3 deficiency aggravates colitis and
            colitis-associated tumorigenesis in mice by hyperactivating the
            innate immune system
  JOURNAL   Cell Death Dis 7 (3), e2124 (2016)
   PUBMED   26938296
  REMARK    GeneRIF: Alkaline ceramidase 3 expression has an important role in
            the innate immune response by regulating the expression of
            pro-inflammatory cytokines in cells of the innate immune system
            through C18:1-ceramide.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Wang,K., Xu,R., Schrandt,J., Shah,P., Gong,Y.Z., Preston,C.,
            Wang,L., Yi,J.K., Lin,C.L., Sun,W., Spyropoulos,D.D., Rhee,S.,
            Li,M., Zhou,J., Ge,S., Zhang,G., Snider,A.J., Hannun,Y.A.,
            Obeid,L.M. and Mao,C.
  TITLE     Alkaline Ceramidase 3 Deficiency Results in Purkinje Cell
            Degeneration and Cerebellar Ataxia Due to Dyshomeostasis of
            Sphingolipids in the Brain
  JOURNAL   PLoS Genet 11 (10), e1005591 (2015)
   PUBMED   26474409
  REMARK    GeneRIF: Acer3 plays critically protective roles in controlling the
            homeostasis of various sphingolipids, including ceramides,
            sphingosine, S1P, and certain complex sphingolipids in the brain
            and protects Purkinje cells from premature degeneration.
            Erratum:[PLoS Genet. 2018 Jan 23;14(1):e1007190. doi:
            10.1371/journal.pgen.1007190. PMID: 29360825]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Wang,Z., Kirkwood,J.S., Taylor,A.W., Stevens,J.F., Leid,M.,
            Ganguli-Indra,G. and Indra,A.K.
  TITLE     Transcription factor Ctip2 controls epidermal lipid metabolism and
            regulates expression of genes involved in sphingolipid biosynthesis
            during skin development
  JOURNAL   J Invest Dermatol 133 (3), 668-676 (2013)
   PUBMED   23096701
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Boon,A.C., deBeauchamp,J., Hollmann,A., Luke,J., Kotb,M., Rowe,S.,
            Finkelstein,D., Neale,G., Lu,L., Williams,R.W. and Webby,R.J.
  TITLE     Host genetic variation affects resistance to infection with a
            highly pathogenic H5N1 influenza A virus in mice
  JOURNAL   J Virol 83 (20), 10417-10426 (2009)
   PUBMED   19706712
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC111084.12 and AC119880.11.
            
            On Jan 12, 2006 this sequence version replaced NP_079684.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK162403.1, AK080977.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164142, SAMN01164143
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 53.65 cM"
     Protein         1..267
                     /product="alkaline ceramidase 3 isoform 1"
                     /EC_number="3.5.1.23"
                     /note="phytoceramidase, alkaline; alkCDase 3; alkaline
                     CDase 3; alkaline phytoceramidase"
                     /calculated_mol_wt=31434
     Region          12..263
                     /region_name="Ceramidase"
                     /note="pfam05875"
                     /db_xref="CDD:461766"
     Site            34..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D099.1)"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D099.1)"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D099.1)"
     Site            119..139
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D099.1)"
     Site            142..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D099.1)"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D099.1)"
     Site            216..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D099.1)"
     CDS             1..267
                     /gene="Acer3"
                     /gene_synonym="1110057L18Rik; 5430429L08Rik; aPHC; Phca"
                     /coded_by="NM_025408.3:93..896"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS21468.1"
                     /db_xref="GeneID:66190"
                     /db_xref="MGI:MGI:1913440"
ORIGIN      
        1 mapavdrkgy wgpttstldw ceenyvvtlf vaefwntvsn limiippifg aiqgirdrle
       61 kryiaaylal tvvgmgswcf hmtlkyemql ldelpmiysc cifvycmfec fktkssinyh
      121 llftlflysl tvttiylkvk epifhqvmyg mlvftlvlrs iyivtwvypw lrglgytslt
      181 vfllgfllwn idnifcdslr nfrkrvppvl gvttqfhaww hiltglgsyl hilfslytrt
      241 lylryrpkvk flfgiwpavm fepqrkh
//
LOCUS       NP_660302                493 aa            linear   PRI 27-APR-2025
DEFINITION  activin receptor type-1C isoform 1 precursor [Homo sapiens].
ACCESSION   NP_660302
VERSION     NP_660302.2
DBSOURCE    REFSEQ: accession NM_145259.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Tangseefa,P., Jin,H., Zhang,H., Xie,M. and Ibanez,C.F.
  TITLE     Human ACVR1C missense variants that correlate with altered body fat
            distribution produce metabolic alterations of graded severity in
            knock-in mutant mice
  JOURNAL   Mol Metab 81, 101890 (2024)
   PUBMED   38307384
  REMARK    GeneRIF: Human ACVR1C missense variants that correlate with altered
            body fat distribution produce metabolic alterations of graded
            severity in knock-in mutant mice.
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Ibanez,C.F.
  TITLE     Regulation of metabolic homeostasis by the TGF-beta superfamily
            receptor ALK7
  JOURNAL   FEBS J 289 (19), 5776-5797 (2022)
   PUBMED   34173336
  REMARK    GeneRIF: Regulation of metabolic homeostasis by the TGF-beta
            superfamily receptor ALK7.
            Review article
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Liu,L., Zhou,X., Zhang,Q., Li,L., Shang,Y., Wang,Z., Zhong,M.,
            Chen,Y., Zhang,W. and Tang,M.
  TITLE     Activin receptor-like kinase 7 silencing alleviates cardiomyocyte
            apoptosis, cardiac fibrosis, and dysfunction in diabetic rats
  JOURNAL   Exp Biol Med (Maywood) 247 (16), 1397-1409 (2022)
   PUBMED   35666032
  REMARK    GeneRIF: Activin receptor-like kinase 7 silencing alleviates
            cardiomyocyte apoptosis, cardiac fibrosis, and dysfunction in
            diabetic rats.
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Tian,Y.D., Chung,M.H., Quan,Q.L., Lee,D.H., Kim,E.J. and Chung,J.H.
  TITLE     UV-Induced Reduction of ACVR1C Decreases SREBP1 and ACC Expression
            by the Suppression of SMAD2 Phosphorylation in Normal Human
            Epidermal Keratinocytes
  JOURNAL   Int J Mol Sci 22 (3), 1101 (2021)
   PUBMED   33499275
  REMARK    GeneRIF: UV-Induced Reduction of ACVR1C Decreases SREBP1 and ACC
            Expression by the Suppression of SMAD2 Phosphorylation in Normal
            Human Epidermal Keratinocytes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Marmol,P., Krapacher,F. and Ibanez,C.F.
  TITLE     Control of brown adipose tissue adaptation to nutrient stress by
            the activin receptor ALK7
  JOURNAL   Elife 9, e54721 (2020)
   PUBMED   32366358
  REMARK    GeneRIF: Control of brown adipose tissue adaptation to nutrient
            stress by the activin receptor ALK7.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Munir,S., Xu,G., Wu,Y., Yang,B., Lala,P.K. and Peng,C.
  TITLE     Nodal and ALK7 inhibit proliferation and induce apoptosis in human
            trophoblast cells
  JOURNAL   J Biol Chem 279 (30), 31277-31286 (2004)
   PUBMED   15150278
  REMARK    GeneRIF: the Nodal-ALK7 pathway inhibits cell proliferation by
            inducing G(1) cell cycle arrest
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Kim,B.C., van Gelder,H., Kim,T.A., Lee,H.J., Baik,K.G., Chun,H.H.,
            Lee,D.A., Choi,K.S. and Kim,S.J.
  TITLE     Activin receptor-like kinase-7 induces apoptosis through activation
            of MAPKs in a Smad3-dependent mechanism in hepatoma cells
  JOURNAL   J Biol Chem 279 (27), 28458-28465 (2004)
   PUBMED   15107418
  REMARK    GeneRIF: ALK7 induces apoptosis through activation of the
            traditional TGF-beta pathway components
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Roberts,H.J., Hu,S., Qiu,Q., Leung,P.C., Caniggia,I., Gruslin,A.,
            Tsang,B. and Peng,C.
  TITLE     Identification of novel isoforms of activin receptor-like kinase 7
            (ALK7) generated by alternative splicing and expression of ALK7 and
            its ligand, Nodal, in human placenta
  JOURNAL   Biol Reprod 68 (5), 1719-1726 (2003)
   PUBMED   12606401
  REMARK    GeneRIF: ALK7 and its isoforms are expressed in human placentae of
            different stages of pregnancy and that their expression is
            developmentally regulated
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Reissmann,E., Jornvall,H., Blokzijl,A., Andersson,O., Chang,C.,
            Minchiotti,G., Persico,M.G., Ibanez,C.F. and Brivanlou,A.H.
  TITLE     The orphan receptor ALK7 and the Activin receptor ALK4 mediate
            signaling by Nodal proteins during vertebrate development
  JOURNAL   Genes Dev 15 (15), 2010-2022 (2001)
   PUBMED   11485994
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Bondestam,J., Huotari,M.A., Moren,A., Ustinov,J., Kaivo-Oja,N.,
            Kallio,J., Horelli-Kuitunen,N., Aaltonen,J., Fujii,M.,
            Moustakas,A., Ten Dijke,P., Otonkoski,T. and Ritvos,O.
  TITLE     cDNA cloning, expression studies and chromosome mapping of human
            type I serine/threonine kinase receptor ALK7 (ACVR1C)
  JOURNAL   Cytogenet Cell Genet 95 (3-4), 157-162 (2001)
   PUBMED   12063393
  REMARK    GeneRIF: cDNA cloning, expression studies and chromosome mapping
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019186.9 and AC079750.5.
            
            On Nov 29, 2007 this sequence version replaced NP_660302.1.
            
            Summary: ACVR1C is a type I receptor for the TGFB (see MIM 190180)
            family of signaling molecules. Upon ligand binding, type I
            receptors phosphorylate cytoplasmic SMAD transcription factors,
            which then translocate to the nucleus and interact directly with
            DNA or in complex with other transcription factors (Bondestam et
            al., 2001 [PubMed 12063393]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.4842.1,
                                           SRR1660809.124916.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000243349.13/ ENSP00000243349.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.1"
     Protein         1..493
                     /product="activin receptor type-1C isoform 1 precursor"
                     /EC_number="2.7.11.30"
                     /note="activin receptor-like kinase 7; activin receptor
                     type-1C; ALK-7; ACTR-IC; activin receptor type IC; activin
                     A receptor, type IC"
                     /calculated_mol_wt=52832
     sig_peptide     1..20
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NER5.1)"
                     /calculated_mol_wt=2058
     mat_peptide     21..493
                     /product="Activin receptor type-1C. /id=PRO_0000042628"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NER5.1)"
                     /calculated_mol_wt=52832
     Region          24..99
                     /region_name="TFP_LU_ECD_ALK7"
                     /note="extracellular domain (ECD) found in activin
                     receptor-like kinase 7 (ALK-7) and similar proteins;
                     cd23540"
                     /db_xref="CDD:467070"
     Site            114..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NER5.1)"
     Region          166..193
                     /region_name="TGF_beta_GS"
                     /note="Transforming growth factor beta type I GS-motif;
                     pfam08515"
                     /db_xref="CDD:462503"
     Region          199..486
                     /region_name="STKc_TGFbR1_ACVR1b_ACVR1c"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Transforming Growth Factor beta Type I Receptor and
                     Activin Type IB/IC Receptors; cd14143"
                     /db_xref="CDD:271045"
     Site            order(201..205,209,220,222,250,270..273,277,279,323,325,
                     327..328,330,341,344,364..367)
                     /site_type="active"
                     /db_xref="CDD:271045"
     Site            order(201..207,209,220,222,270..271,273,277,327..328,330,
                     341)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271045"
     Site            order(205,277,279,323,325,327,344,364..367)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271045"
     Site            order(232..233,236..237,240..241,255,257)
                     /site_type="other"
                     /note="FKBP12 binding site [polypeptide binding]"
                     /db_xref="CDD:271045"
     Site            340..367
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271045"
     CDS             1..493
                     /gene="ACVR1C"
                     /gene_synonym="ACVRLK7; ALK7"
                     /coded_by="NM_145259.3:221..1702"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2205.1"
                     /db_xref="GeneID:130399"
                     /db_xref="HGNC:HGNC:18123"
                     /db_xref="MIM:608981"
ORIGIN      
        1 mtralcsalr qallllaaaa elspglkcvc llcdssnftc qtegacwasv mltngkeqvi
       61 kscvslpeln aqvfchssnn vtkteccftd fcnnitlhlp taspnapklg pmelaiiitv
      121 pvcllsiaam ltvwacqgrq csyrkkkrpn veeplsecnl vnagktlkdl iydvtasgsg
      181 sglpllvqrt iartivlqei vgkgrfgevw hgrwcgedva vkifssrder swfreaeiyq
      241 tvmlrhenil gfiaadnkdn gtwtqlwlvs eyheqgslyd ylnrnivtva gmiklalsia
      301 sglahlhmei vgtqgkpaia hrdiksknil vkkcetcaia dlglavkhds ilntidipqn
      361 pkvgtkryma pemlddtmnv nifesfkrad iysvglvywe iarrcsvggi veeyqlpyyd
      421 mvpsdpsiee mrkvvcdqkf rpsipnqwqs cealrvmgri mrecwyanga arltalrikk
      481 tisqlcvked cka
//
LOCUS       NP_001346987              99 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim10 B
            isoform e [Mus musculus].
ACCESSION   NP_001346987
VERSION     NP_001346987.1
DBSOURCE    REFSEQ: accession NM_001360058.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Kitamura,H., Nakagawa,T., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of FLJ
            genes: the complete nucleotide sequences of 110 mouse
            FLJ-homologous cDnas identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (2), 127-135 (2004)
   PUBMED   15449545
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Bauer,M.F., Rothbauer,U., Muhlenbein,N., Smith,R.J., Gerbitz,K.,
            Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     The mitochondrial TIM22 preprotein translocase is highly conserved
            throughout the eukaryotic kingdom
  JOURNAL   FEBS Lett 464 (1-2), 41-47 (1999)
   PUBMED   10611480
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Jin,H., Kendall,E., Freeman,T.C., Roberts,R.G. and Vetrie,D.L.
  TITLE     The human family of Deafness/Dystonia peptide (DDP) related
            mitochondrial import proteins
  JOURNAL   Genomics 61 (3), 259-267 (1999)
   PUBMED   10552927
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Hadjiargyrou,M., Halsey,M.F., Ahrens,W., Rightmire,E.P.,
            McLeod,K.J. and Rubin,C.T.
  TITLE     Cloning of a novel cDNA expressed during the early stages of
            fracture healing
  JOURNAL   Biochem Biophys Res Commun 249 (3), 879-884 (1998)
   PUBMED   9731230
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125227.6 and CK622744.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CN839757.1, AV486056.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 55.93 cM"
     Protein         1..99
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim10 B isoform e"
                     /note="small zinc finger-like protein; fractured callus 1;
                     mitochondrial import inner membrane translocase subunit
                     Tim9 B; Fracture Callus 1; fractured callus expressed
                     transcript 1; mitochondrial import inner membrane
                     translocase subunit Tim10 B"
                     /calculated_mol_wt=11298
     Region          9..64
                     /region_name="zf-Tim10_DDP"
                     /note="Tim10/DDP family zinc finger; pfam02953"
                     /db_xref="CDD:460764"
     CDS             1..99
                     /gene="Timm10b"
                     /gene_synonym="Fxc1; Tim10b; Tim9b"
                     /coded_by="NM_001360058.1:149..448"
                     /note="isoform e is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS90302.1"
                     /db_xref="GeneID:14356"
                     /db_xref="MGI:MGI:1315196"
ORIGIN      
        1 meqqqqqlrn lrdfllvynr mtelcfqrcv pslhhralda eeeaclhsca gklihsnhrl
       61 maayvhlmpa lvqrriadye aasaapavkk ncceprgrr
//
LOCUS       NP_001353118             499 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 565 isoform 1 [Homo sapiens].
ACCESSION   NP_001353118 XP_016881830
VERSION     NP_001353118.1
DBSOURCE    REFSEQ: accession NM_001366189.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012617.7 and AC008848.9.
            
            On Sep 25, 2018 this sequence version replaced XP_016881830.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1-4 encode the same isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.181321.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..499
                     /product="zinc finger protein 565 isoform 1"
                     /calculated_mol_wt=57696
     Region          6..66
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          169..189
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(174,176,178,180..181,184..185,188,202,204,208..209,
                     212..213,216,230,232,234,236..237,240..241,244)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          193..498
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          197..217
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          225..245
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          253..273
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          281..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          309..329
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(314,316,318,320..321,324..325,328,342,344,348..349,
                     352..353,356,370,372,374,376..377,380..381,384)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          337..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          365..385
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          393..413
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          421..441
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          449..469
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          477..497
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..499
                     /gene="ZNF565"
                     /coded_by="NM_001366189.1:806..2305"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS12491.1"
                     /db_xref="GeneID:147929"
                     /db_xref="HGNC:HGNC:26726"
                     /db_xref="MIM:614275"
ORIGIN      
        1 maqglvtfrd vaiefsleew kclepaqrdl yrevtlenfg hlaslglsis kpdvvslleq
       61 gkepwmiand vtgpwcpdle srcekflqkd ifeigafnwe imeslkcsdl egsdfradwe
      121 cegqferqvn eecyfkqvnv tyghmpvfqh htshtvrqsr etgeklmech ecgkafsrgs
      181 hliqhqkiht gekpfgckec gkafsrashl vqhqrihtge kpydckdcgk afgrtselil
      241 hqrlhtgvkp yeckecgktf rqhsqlilhq rthtgekpyv ckdcgkafir gsqltvhrri
      301 htgarpyeck ecgkafrqhs qltvhqriht gekpyeckec gkgfihssev trhqrihsge
      361 kpyeckecgk afrqhaqltr hqrvhtgdrp yeckdcgkaf srssyliqhq rihtgdkpye
      421 ckecgkafir vsqlthhqri htcekpyecr ecgmafirss qltehqrihp gikpyecrec
      481 gqafilgsql iehyrihtg
//
LOCUS       NP_001354449             569 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 13 [Homo sapiens].
ACCESSION   NP_001354449 XP_016872215
VERSION     NP_001354449.1
DBSOURCE    REFSEQ: accession NM_001367520.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 569)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 569)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 569)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_016872215.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.154189.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..569
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 13"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=63111
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          410..>465
                     /region_name="NTF2_like"
                     /note="Nuclear transport factor 2 (NTF2-like) superfamily.
                     This family includes members of the NTF2 family,
                     Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases,
                     and the beta subunit of Ring hydroxylating dioxygenases.
                     This family is a classic example of...; cl09109"
                     /db_xref="CDD:471850"
     CDS             1..569
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367520.1:95..1804"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk pqsnnknsle pqttvvhnat dgikgstesc
      361 ntttededlk aaplrtgngs svpegrssrd rtapsagmqp qpslcssamr kqeiikiteq
      421 lieainngdf eaytkicdpg ltsfepealg nlvegmdfhk fyfenrewvr aadillpapl
      481 plclcllltf ssqlptfplf dlraalllcm lvplcpdgcr qaplkallls skchsfcscf
      541 vavpvttikl tyflpgavay acnpntlgg
//
LOCUS       NP_001289875             414 aa            linear   PRI 27-APR-2025
DEFINITION  CCA tRNA nucleotidyltransferase 1, mitochondrial isoform 2 [Homo
            sapiens].
ACCESSION   NP_001289875
VERSION     NP_001289875.2
DBSOURCE    REFSEQ: accession NM_001302946.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Fatica,T., Naas,T., Liwak,U., Slaa,H., Souaid,M., Frangione,B.,
            Kattini,R., Gaudreau-Lapierre,A., Trinkle-Mulcahy,L.,
            Chakraborty,P. and Holcik,M.
  TITLE     TRNT-1 Deficiency Is Associated with Loss of tRNA Integrity and
            Imbalance of Distinct Proteins
  JOURNAL   Genes (Basel) 14 (5), 1043 (2023)
   PUBMED   37239403
  REMARK    GeneRIF: TRNT-1 Deficiency Is Associated with Loss of tRNA
            Integrity and Imbalance of Distinct Proteins.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Seki,M., Komuro,A., Ishikawa,T., Takahashi,M. and Nashimoto,M.
  TITLE     Genes for tRNA recycling are upregulated in response to infection
            with Theiler's mouse encephalitis virus
  JOURNAL   Biochem Biophys Res Commun 587, 63-68 (2022)
   PUBMED   34864548
  REMARK    GeneRIF: Genes for tRNA recycling are upregulated in response to
            infection with Theiler's mouse encephalitis virus.
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Odom,J., Amin,H., Gijavanekar,C., Elsea,S.H., Kralik,S., Chinen,J.,
            Lin,Y., Yates,A.M.M., Mizerik,E., Potocki,L. and Scaglia,F.
  TITLE     A phenotypic expansion of TRNT1 associated sideroblastic anemia
            with immunodeficiency, fevers, and developmental delay
  JOURNAL   Am J Med Genet A 188 (1), 259-268 (2022)
   PUBMED   34510712
  REMARK    GeneRIF: A phenotypic expansion of TRNT1 associated sideroblastic
            anemia with immunodeficiency, fevers, and developmental delay.
            Review article
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Wang,J., Deng,Q., He,X., Chen,D., Hang,S., Gao,Y. and Chen,Y.
  TITLE     Two cases of sideroblastic anemia with B-cell immunodeficiency,
            periodic fevers, and developmental delay (SIFD) syndrome in Chinese
            Han children caused by novel compound heterozygous variants of the
            TRNT1 gene
  JOURNAL   Clin Chim Acta 521, 244-250 (2021)
   PUBMED   34310935
  REMARK    GeneRIF: Two cases of sideroblastic anemia with B-cell
            immunodeficiency, periodic fevers, and developmental delay (SIFD)
            syndrome in Chinese Han children caused by novel compound
            heterozygous variants of the TRNT1 gene.
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Augustin,M.A., Reichert,A.S., Betat,H., Huber,R., Morl,M. and
            Steegborn,C.
  TITLE     Crystal structure of the human CCA-adding enzyme: insights into
            template-independent polymerization
  JOURNAL   J Mol Biol 328 (5), 985-994 (2003)
   PUBMED   12729736
  REMARK    GeneRIF: The crystal structure reveals a four domain architecture
            with a cluster of conserved residues forming a positively charged
            cleft between the first two domains.
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Nagaike,T., Suzuki,T., Tomari,Y., Takemoto-Hori,C., Negayama,F.,
            Watanabe,K. and Ueda,T.
  TITLE     Identification and characterization of mammalian mitochondrial tRNA
            nucleotidyltransferases
  JOURNAL   J Biol Chem 276 (43), 40041-40049 (2001)
   PUBMED   11504732
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Reichert,A.S., Thurlow,D.L. and Morl,M.
  TITLE     A eubacterial origin for the human tRNA nucleotidyltransferase?
  JOURNAL   Biol Chem 382 (10), 1431-1438 (2001)
   PUBMED   11727826
  REMARK    GeneRIF: human gene transcript CGI-47 (#AF151805) was cloned and
            encodes a bona fide CCA-adding enzyme and not a poly(A) polymerase.
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024060.6 and AL834397.1.
            
            On Nov 19, 2018 this sequence version replaced NP_001289875.1.
            
            Summary: The protein encoded by this gene is a CCA-adding enzyme
            which belongs to the tRNA nucleotidyltransferase/poly(A) polymerase
            family. This essential enzyme functions by catalyzing the addition
            of the conserved nucleotide triplet CCA to the 3' terminus of tRNA
            molecules. Mutations in this gene result in sideroblastic anemia
            with B-cell immunodeficiency, periodic fevers, and developmental
            delay. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1. This
            results in a shorter protein (isoform 2), compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL834397.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p26.2"
     Protein         1..414
                     /product="CCA tRNA nucleotidyltransferase 1, mitochondrial
                     isoform 2"
                     /EC_number="2.7.7.72"
                     /note="mitochondrial CCA-adding
                     tRNA-nucleotidyltransferase; tRNA nucleotidyl transferase,
                     CCA-adding, 1; tRNA-nucleotidyltransferase 1,
                     mitochondrial; CCA tRNA nucleotidyltransferase 1,
                     mitochondrial; mt CCA-adding enzyme; mt tRNA
                     CCA-diphosphorylase; mt tRNA adenylyltransferase; mt tRNA
                     CCA-pyrophosphorylase; tRNA CCA nucleotidyl transferase 1;
                     ATP(CTP):tRNA nucleotidyltransferase"
                     /calculated_mol_wt=47698
     Region          43..408
                     /region_name="PcnB"
                     /note="tRNA nucleotidyltransferase/poly(A) polymerase
                     [Translation, ribosomal structure and biogenesis];
                     COG0617"
                     /db_xref="CDD:440382"
     CDS             1..414
                     /gene="TRNT1"
                     /gene_synonym="CCA1; CGI-47; MtCCA; RPEM; SIFD"
                     /coded_by="NM_001302946.2:79..1323"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77691.1"
                     /db_xref="GeneID:51095"
                     /db_xref="HGNC:HGNC:17341"
                     /db_xref="MIM:612907"
ORIGIN      
        1 mlrclyhwhr pvlnrrwsrl clpkqylftm klqspefqsl fteglkslte lfvkenhelr
       61 iaggavrdll ngvkpqdidf attatptqmk emfqsagirm innrgekhgt itarlheenf
      121 eittlridvt tdgrhaevef ttdwqkdaer rdltinsmfl gfdgtlfdyf ngyedlknkk
      181 vrfvghakqr iqedylrilr yfrfygrivd kpgdhdpetl eaiaenakgl agisgeriwv
      241 elkkilvglp anasleefdk vsknvdgfsp kpvtllaslf kvqddvtkld lrlkiakeek
      301 nlglfivknr kdlikatdss dplkpyqdfi idsrepdatt rvcellkyqg ehcllkemqq
      361 wsippfpvsg hdirkvgiss gkeigallqq lreqwkksgy qmekdellsy ikkt
//
LOCUS       NP_076381                262 aa            linear   ROD 27-APR-2025
DEFINITION  intercellular adhesion molecule 4 isoform 1 precursor [Mus
            musculus].
ACCESSION   NP_076381
VERSION     NP_076381.1
DBSOURCE    REFSEQ: accession NM_023892.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Maynard,T.M., Horvath,A., Bernot,J.P., Karpinski,B.A.,
            Tavares,A.L.P., Shah,A., Zheng,Q., Spurr,L., Olender,J.,
            Moody,S.A., Fraser,C.M., LaMantia,A.S. and Lee,N.H.
  TITLE     Transcriptional dysregulation in developing trigeminal sensory
            neurons in the LgDel mouse model of DiGeorge 22q11.2 deletion
            syndrome
  JOURNAL   Hum Mol Genet 29 (6), 1002-1017 (2020)
   PUBMED   32047912
  REMARK    Erratum:[Hum Mol Genet. 2020 Jun 3;29(9):1580. doi:
            10.1093/hmg/ddaa067. PMID: 32358605]
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Wang,L., Yu,H., Cheng,H., He,K., Fang,Z., Ge,L., Cheng,T. and
            Jin,Y.
  TITLE     Deletion of Stk40 impairs definitive erythropoiesis in the mouse
            fetal liver
  JOURNAL   Cell Death Dis 8 (3), e2722 (2017)
   PUBMED   28358362
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Mitsui,S., Saito,M., Mori,K. and Yoshihara,Y.
  TITLE     A transcriptional enhancer that directs telencephalon-specific
            transgene expression in mouse brain
  JOURNAL   Cereb Cortex 17 (3), 522-530 (2007)
   PUBMED   16581979
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Lee,G., Lo,A., Short,S.A., Mankelow,T.J., Spring,F., Parsons,S.F.,
            Yazdanbakhsh,K., Mohandas,N., Anstee,D.J. and Chasis,J.A.
  TITLE     Targeted gene deletion demonstrates that the cell adhesion molecule
            ICAM-4 is critical for erythroblastic island formation
  JOURNAL   Blood 108 (6), 2064-2071 (2006)
   PUBMED   16690966
  REMARK    GeneRIF: ICAM-4 is critical in erythroblastic island formation via
            ICAM-4/alpha(V) adhesion
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Sugino,H.
  TITLE     ICAM-3, a ligand for DC-SIGN, was duplicated from ICAM-1 in
            mammalian evolution, but was lost in the rodent genome
  JOURNAL   FEBS Lett 579 (13), 2901-2906 (2005)
   PUBMED   15890347
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Leeb,T. and Muller,M.
  TITLE     Comparative human-mouse-rat sequence analysis of the ICAM gene
            cluster on HSA 19p13.2 and a 185-kb porcine region from SSC 2q
  JOURNAL   Gene 343 (2), 239-244 (2004)
   PUBMED   15588578
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Lee,G., Spring,F.A., Parsons,S.F., Mankelow,T.J., Peters,L.L.,
            Koury,M.J., Mohandas,N., Anstee,D.J. and Chasis,J.A.
  TITLE     Novel secreted isoform of adhesion molecule ICAM-4: potential
            regulator of membrane-associated ICAM-4 interactions
  JOURNAL   Blood 101 (5), 1790-1797 (2003)
   PUBMED   12406883
  REMARK    GeneRIF: A novel second splice cDNA encodes an ICAM-4 isoform
            lacking the membrane-spanning domain. Erythroblasts express both
            isoforms. This new isoform, ICAM-4S, may modulate
            membrane-associated ICAM-4 binding & regulate erythroblast
            molecular attachments.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC116909.1 and D19050.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC116909.1, AF296282.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 7.69 cM"
     Protein         1..262
                     /product="intercellular adhesion molecule 4 isoform 1
                     precursor"
                     /note="LW glycoprotein"
                     /calculated_mol_wt=26258
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2256
     mat_peptide     23..262
                     /product="Intercellular adhesion molecule 4.
                     /id=PRO_0000014797"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERM2.1)"
                     /calculated_mol_wt=26258
     Region          40..123
                     /region_name="ICAM_N"
                     /note="Intercellular adhesion molecule (ICAM), N-terminal
                     domain; pfam03921"
                     /db_xref="CDD:397829"
     Site            60
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERM2.1)"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERM2.1)"
     Region          <124..>167
                     /region_name="PHA03271"
                     /note="envelope glycoprotein C; Provisional"
                     /db_xref="CDD:223030"
     Region          125..219
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          141..145
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          157..161
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            182
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERM2.1)"
     Region          183..187
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          199..204
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          216..219
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERM2.1)"
     CDS             1..262
                     /gene="Icam4"
                     /gene_synonym="1810015M19Rik; Cd242; ICAM-4"
                     /coded_by="NM_023892.3:23..811"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS22890.1"
                     /db_xref="GeneID:78369"
                     /db_xref="MGI:MGI:1925619"
ORIGIN      
        1 mesalllpsl llvaayprgg spqqewmqsp papsvtsapf wvrlnpelea vppggsawln
       61 cshncplpvh sslrtqlrqg kivngsgwvs yqlldvrawn skvrcvvtca getreatari
      121 taykrprsvi leppvlvghk ytlrcyvthv fpvgflvvsl rrggrviyhe slerftgsdl
      181 anvtltyvmr aglndlwqpl tcharlnldg lvvrsssapv mltvlalspa sialastsia
      241 tlvgillavg avyvrkylav qt
//
LOCUS       NP_001352752             848 aa            linear   PRI 27-APR-2025
DEFINITION  type II inositol 1,4,5-trisphosphate 5-phosphatase isoform 6 [Homo
            sapiens].
ACCESSION   NP_001352752
VERSION     NP_001352752.1
DBSOURCE    REFSEQ: accession NM_001365823.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Droubi,A., Wallis,C., Anderson,K.E., Rahman,S., de Sa,A.,
            Rahman,T., Stephens,L.R., Hawkins,P.T. and Lowe,M.
  TITLE     The inositol 5-phosphatase INPP5B regulates B cell receptor
            clustering and signaling
  JOURNAL   J Cell Biol 221 (9) (2022)
   PUBMED   35878408
  REMARK    GeneRIF: The inositol 5-phosphatase INPP5B regulates B cell
            receptor clustering and signaling.
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Nakatsu,F., Messa,M., Nandez,R., Czapla,H., Zou,Y.,
            Strittmatter,S.M. and De Camilli,P.
  TITLE     Sac2/INPP5F is an inositol 4-phosphatase that functions in the
            endocytic pathway
  JOURNAL   J Cell Biol 209 (1), 85-95 (2015)
   PUBMED   25869668
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Montjean,R., Aoidi,R., Desbois,P., Rucci,J., Trichet,M.,
            Salomon,R., Rendu,J., Faure,J., Lunardi,J., Gacon,G., Billuart,P.
            and Dorseuil,O.
  TITLE     OCRL-mutated fibroblasts from patients with Dent-2 disease exhibit
            INPP5B-independent phenotypic variability relatively to Lowe
            syndrome cells
  JOURNAL   Hum Mol Genet 24 (4), 994-1006 (2015)
   PUBMED   25305077
  REMARK    GeneRIF: OCRL-mutated fibroblasts from patients with Dent-2 disease
            exhibit INPP5B-independent phenotypic variability relatively to
            Lowe syndrome cells
REFERENCE   4  (residues 1 to 848)
  AUTHORS   Pirruccello,M., Nandez,R., Idevall-Hagren,O., Alcazar-Roman,A.,
            Abriola,L., Berwick,S.A., Lucast,L., Morel,D. and De Camilli,P.
  TITLE     Identification of inhibitors of inositol 5-phosphatases through
            multiple screening strategies
  JOURNAL   ACS Chem Biol 9 (6), 1359-1368 (2014)
   PUBMED   24742366
REFERENCE   5  (residues 1 to 848)
  AUTHORS   Tresaugues,L., Silvander,C., Flodin,S., Welin,M., Nyman,T.,
            Graslund,S., Hammarstrom,M., Berglund,H. and Nordlund,P.
  TITLE     Structural basis for phosphoinositide substrate recognition,
            catalysis, and membrane interactions in human inositol
            polyphosphate 5-phosphatases
  JOURNAL   Structure 22 (5), 744-755 (2014)
   PUBMED   24704254
  REMARK    GeneRIF: The crystal structures of human INPP5B in complex with
            phosphoinositide substrate analogs revealed a membrane interaction
            patch likely to assist in sequestering substrates from the lipid
            bilayer.
REFERENCE   6  (residues 1 to 848)
  AUTHORS   Speed,C.J., Matzaris,M., Bird,P.I. and Mitchell,C.A.
  TITLE     Tissue distribution and intracellular localisation of the 75-kDa
            inositol polyphosphate 5-phosphatase
  JOURNAL   Eur J Biochem 234 (1), 216-224 (1995)
   PUBMED   8529643
REFERENCE   7  (residues 1 to 848)
  AUTHORS   Jefferson,A.B. and Majerus,P.W.
  TITLE     Properties of type II inositol polyphosphate 5-phosphatase
  JOURNAL   J Biol Chem 270 (16), 9370-9377 (1995)
   PUBMED   7721860
REFERENCE   8  (residues 1 to 848)
  AUTHORS   Janne,P.A., Dutra,A.S., Dracopoli,N.C., Charnas,L.R., Puck,J.M. and
            Nussbaum,R.L.
  TITLE     Localization of the 75-kDa inositol polyphosphate-5-phosphatase
            (INPP5B) to human chromosome band 1p34
  JOURNAL   Cytogenet Cell Genet 66 (3), 164-166 (1994)
   PUBMED   8125013
REFERENCE   9  (residues 1 to 848)
  AUTHORS   Ross,T.S., Jefferson,A.B., Mitchell,C.A. and Majerus,P.W.
  TITLE     Cloning and expression of human 75-kDa inositol
            polyphosphate-5-phosphatase
  JOURNAL   J Biol Chem 266 (30), 20283-20289 (1991)
   PUBMED   1718960
REFERENCE   10 (residues 1 to 848)
  AUTHORS   Mitchell,C.A., Connolly,T.M. and Majerus,P.W.
  TITLE     Identification and isolation of a 75-kDa inositol
            polyphosphate-5-phosphatase from human platelets
  JOURNAL   J Biol Chem 264 (15), 8873-8877 (1989)
   PUBMED   2542294
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL603790.41 and AL929472.21.
            
            Summary: This gene encodes a member of a family of inositol
            polyphosphate-5-phosphatases. These enzymes function in the
            regulation of calcium signaling by inactivating inositol
            phosphates. The encoded protein is localized to the cytosol and
            mitochondria, and associates with membranes through an isoprenyl
            modification near the C-terminus. Alternatively spliced transcript
            variants of this gene have been described. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (8), as well as variant 9, encodes
            isoform 6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..848
                     /product="type II inositol 1,4,5-trisphosphate
                     5-phosphatase isoform 6"
                     /EC_number="3.1.3.36"
                     /note="phosphoinositide 5-phosphatase; type II inositol
                     1,4,5-trisphosphate 5-phosphatase; inositol
                     polyphosphate-5-phosphatase, 75kDa"
                     /calculated_mol_wt=96534
     Region          <29..81
                     /region_name="INPP5B_PH"
                     /note="Type II inositol 1,4,5-trisphosphate 5-phosphatase
                     PH domain; pfam16776"
                     /db_xref="CDD:465268"
     Region          200..493
                     /region_name="INPP5c_INPP5B"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of Type II inositol polyphosphate
                     5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and
                     related proteins; cd09093"
                     /db_xref="CDD:197327"
     Site            order(208,210,238,241,243,246,308,314..315,335,338..339,
                     382,384,386,437..438,451,453,459,483..484)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197327"
     Site            order(208,238,335,382,384,459,483..484)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197327"
     Site            order(210,238,483)
                     /site_type="other"
                     /note="Mg binding site [ion binding]"
                     /db_xref="CDD:197327"
     Site            order(238,241,243,246,308,314..315,335,338..339,386,
                     437..438,451,453,483)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197327"
     Site            order(335,384,484)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197327"
     Region          627..847
                     /region_name="RhoGAP_OCRL1"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain present in OCRL1-like proteins.
                     OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins
                     contain two conserved domains: a central inositol
                     polyphosphate 5-phosphatase domain and...; cd04380"
                     /db_xref="CDD:239845"
     Site            order(707,742,746,809,812..813,838)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239845"
     Site            707
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239845"
     CDS             1..848
                     /gene="INPP5B"
                     /gene_synonym="5PTase"
                     /coded_by="NM_001365823.1:469..3015"
                     /note="isoform 6 is encoded by transcript variant 8"
                     /db_xref="GeneID:3633"
                     /db_xref="HGNC:HGNC:6077"
                     /db_xref="MIM:147264"
ORIGIN      
        1 mshrtgpksg fshssmrlsl faspfygqgs dvtvqldtae lslvfqlpfg sqtrmflhev
       61 aracpgfdsa trdpeflwls ryrcaelele mptprgcnsa lvtwpgyati ggggsnfdgl
      121 rpngkgvpmd qssrgqdkpe slqprqnksk seitdmvrss titvsdkahi lsmqkfglrd
      181 tivkshllqk eedytyiqnf rffagtynvn gqspkeclrl wlsngiqapd vycvgfqeld
      241 lskeafffhd tpkeeewfka vseglhpdak yakvklirlv gimlllyvkq ehaayiseve
      301 aetvgtgimg rmgnkggvai rfqfhntsic vvnshlaahi eeyerrnqdy kdicsrmqfc
      361 qpdpslpplt isnhdvilwl gdlnyrieel dvekvkklie ekdfqmlyay dqlkiqvaak
      421 tvfegftege ltfqptykyd tgsddwdtse kcrapawcdr ilwkgknitq lsyqshmalk
      481 tsdhkpvssv fdigvrvvnd elyrktleei vrsldkmena nipsvslskr efcfqnvkym
      541 qlkvesftih ngqvpchfef inkpdeesyc kqwlnanpsr gfllpdsdve idlelfvnkm
      601 tatklnsged kiedilvlhl drgkdyflsv sgnylpscfg spihtlcymr epildlplet
      661 iseltlmpvw tgddgsqlds pmeipkelwm mvdylyrnav qqedlfqqpg lrsefehird
      721 cldtgmidnl sasnhsvaea lllfleslpe pvicystyhn clecsgnyta skqvistlpi
      781 fhknvfhylm aflrellkns aknhldenil asifgslllr npaghqkldm tekkkaqefi
      841 hqflcnpl
//
LOCUS       NP_620133                452 aa            linear   PRI 27-APR-2025
DEFINITION  diphthine methyltransferase isoform a [Homo sapiens].
ACCESSION   NP_620133
VERSION     NP_620133.1
DBSOURCE    REFSEQ: accession NM_138778.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Wei,H., Bera,T.K., Wayne,A.S., Xiang,L., Colantonio,S., Chertov,O.
            and Pastan,I.
  TITLE     A modified form of diphthamide causes immunotoxin resistance in a
            lymphoma cell line with a deletion of the WDR85 gene
  JOURNAL   J Biol Chem 288 (17), 12305-12312 (2013)
   PUBMED   23486472
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Zhang,F., Baumer,N., Rode,M., Ji,P., Zhang,T., Berdel,W.E. and
            Muller-Tidow,C.
  TITLE     The inhibitor of growth protein 5 (ING5) depends on INCA1 as a
            co-factor for its antiproliferative effects
  JOURNAL   PLoS One 6 (7), e21505 (2011)
   PUBMED   21750715
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Carette,J.E., Guimaraes,C.P., Varadarajan,M., Park,A.S.,
            Wuethrich,I., Godarova,A., Kotecki,M., Cochran,B.H., Spooner,E.,
            Ploegh,H.L. and Brummelkamp,T.R.
  TITLE     Haploid genetic screens in human cells identify host factors used
            by pathogens
  JOURNAL   Science 326 (5957), 1231-1235 (2009)
   PUBMED   19965467
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK075115.1, BC017335.2,
            AL365502.57 and AA252248.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Diphthamide is a post-translationally modified histidine
            residue present in elongation factor 2, and is the target of
            diphtheria toxin. This gene encodes a protein that contains a WD-40
            domain, and is thought to be involved in diphthamide biosynthesis.
            A similar protein in yeast functions as a methylesterase,
            converting methylated diphthine to diphthine, which can then
            undergo amidation to produce diphthamide. [provided by RefSeq, Oct
            2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.77732.1,
                                           SRR3476690.181613.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000277540.7/ ENSP00000277540.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..452
                     /product="diphthine methyltransferase isoform a"
                     /EC_number="3.1.1.97"
                     /note="WD repeat-containing protein 85; diphthine
                     methyltransferase"
                     /calculated_mol_wt=50444
     Region          79..130
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTV6.2)"
     Region          91..135
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          131..185
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTV6.2)"
     Region          141..193
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <186..292
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          186..229
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTV6.2)"
     Region          198..236
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          230..273
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTV6.2)"
     Region          244..278
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          274..313
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTV6.2)"
     Region          285..326
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          314..403
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTV6.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BTV6.2)"
     Region          371..402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTV6.2)"
     Region          404..448
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTV6.2)"
     CDS             1..452
                     /gene="DPH7"
                     /gene_synonym="C9orf112; RRT2; WDR85"
                     /coded_by="NM_138778.5:149..1507"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7047.1"
                     /db_xref="GeneID:92715"
                     /db_xref="HGNC:HGNC:25199"
                     /db_xref="MIM:613210"
ORIGIN      
        1 mmgcfalqtv dteltadsve wcplqgcrhl lacgtyqlrr pedrpagpqn kggmevkepq
       61 vrlgrlflys fndnnsihpl vevqrkdtsa ildmkwchip vaghallgla dasgsiqllr
      121 lvesekshvl eplsslalee qclalsldws tgktgragdq plkiissdst gqlhllmvne
      181 trprlqkvas wqahqfeawi aafnywhpei vysggddgll rgwdtrvpgk flftskrhtm
      241 gvcsiqssph rehilatgsy dehillwdtr nmkqpladtp vqggvwrikw hpfhhhllla
      301 acmhsgfkil ncqkameerq eatvltshtl pdslvygadw swllfrslqr apswsfpsnl
      361 gtktadlkga selptpchec redndgegha rpqsgmkplt egmrkngtwl qataattrdc
      421 gvnpeeadsa fsllatcsfy dhalhlwewe gn
//
LOCUS       NP_054754                169 aa            linear   PRI 27-APR-2025
DEFINITION  sorting nexin-24 [Homo sapiens].
ACCESSION   NP_054754
VERSION     NP_054754.1
DBSOURCE    REFSEQ: accession NM_014035.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Lacey,J., Webster,S.J., Heath,P.R., Hill,C.J., Nicholson-Goult,L.,
            Wagner,B.E., Khan,A.O., Morgan,N.V., Makris,M. and Daly,M.E.
  TITLE     Sorting nexin 24 is required for alpha-granule biogenesis and cargo
            delivery in megakaryocytes
  JOURNAL   Haematologica 107 (8), 1902-1913 (2022)
   PUBMED   35021601
  REMARK    GeneRIF: Sorting nexin 24 is required for alpha-granule biogenesis
            and cargo delivery in megakaryocytes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Anttila,V., Winsvold,B.S., Gormley,P., Kurth,T., Bettella,F.,
            McMahon,G., Kallela,M., Malik,R., de Vries,B., Terwindt,G.,
            Medland,S.E., Todt,U., McArdle,W.L., Quaye,L., Koiranen,M.,
            Ikram,M.A., Lehtimaki,T., Stam,A.H., Ligthart,L., Wedenoja,J.,
            Dunham,I., Neale,B.M., Palta,P., Hamalainen,E., Schurks,M.,
            Rose,L.M., Buring,J.E., Ridker,P.M., Steinberg,S., Stefansson,H.,
            Jakobsson,F., Lawlor,D.A., Evans,D.M., Ring,S.M., Farkkila,M.,
            Artto,V., Kaunisto,M.A., Freilinger,T., Schoenen,J., Frants,R.R.,
            Pelzer,N., Weller,C.M., Zielman,R., Heath,A.C., Madden,P.A.F.,
            Montgomery,G.W., Martin,N.G., Borck,G., Gobel,H., Heinze,A.,
            Heinze-Kuhn,K., Williams,F.M.K., Hartikainen,A.L., Pouta,A., van
            den Ende,J., Uitterlinden,A.G., Hofman,A., Amin,N., Hottenga,J.J.,
            Vink,J.M., Heikkila,K., Alexander,M., Muller-Myhsok,B.,
            Schreiber,S., Meitinger,T., Wichmann,H.E., Aromaa,A.,
            Eriksson,J.G., Traynor,B., Trabzuni,D., Rossin,E., Lage,K.,
            Jacobs,S.B.R., Gibbs,J.R., Birney,E., Kaprio,J., Penninx,B.W.,
            Boomsma,D.I., van Duijn,C., Raitakari,O., Jarvelin,M.R.,
            Zwart,J.A., Cherkas,L., Strachan,D.P., Kubisch,C., Ferrari,M.D.,
            van den Maagdenberg,A.M.J.M., Dichgans,M., Wessman,M., Smith,G.D.,
            Stefansson,K., Daly,M.J., Nyholt,D.R., Chasman,D. and Palotie,A.
  CONSRTM   North American Brain Expression Consortium; UK Brain Expression
            Consortium
  TITLE     Genome-wide meta-analysis identifies new susceptibility loci for
            migraine
  JOURNAL   Nat Genet 45 (8), 912-917 (2013)
   PUBMED   23793025
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ278046.1, BC010886.1, AF139461.1 and BU623609.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes a protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.282706.1,
                                           SRR1660807.231209.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261369.9/ ENSP00000261369.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.2"
     Protein         1..169
                     /product="sorting nexin-24"
                     /note="sorting nexing 24"
                     /calculated_mol_wt=19687
     Region          1..111
                     /region_name="PX_SNX22"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 22; cd06880"
                     /db_xref="CDD:132790"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9Y343.1)"
     Site            order(38..40,61..62,74)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132790"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CRB0; propagated from
                     UniProtKB/Swiss-Prot (Q9Y343.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CRB0; propagated from
                     UniProtKB/Swiss-Prot (Q9Y343.1)"
     CDS             1..169
                     /gene="SNX24"
                     /gene_synonym="PRO1284; SBBI31"
                     /coded_by="NM_014035.4:22..531"
                     /db_xref="CCDS:CCDS4132.1"
                     /db_xref="GeneID:28966"
                     /db_xref="HGNC:HGNC:21533"
ORIGIN      
        1 mevyipsfry eesdlergyt vfkievlmng rkhfvekrys efhalhkklk kciktpeips
       61 khvrnwvpkv leqrrqglet ylqavilene elpklfldfl nvrhlpslpk aescgsfdet
      121 eseessklsh qpvllflrdp yvlpaasdfp nvviegvlhg ifyphlqpr
//
LOCUS       NP_001356480             321 aa            linear   PRI 27-APR-2025
DEFINITION  BDNF/NT-3 growth factors receptor isoform k [Homo sapiens].
ACCESSION   NP_001356480
VERSION     NP_001356480.1
DBSOURCE    REFSEQ: accession NM_001369551.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Gupta,R., Dittmeier,M., Wohlleben,G., Nickl,V., Bischler,T.,
            Luzak,V., Wegat,V., Doll,D., Sodmann,A., Bady,E., Langlhofer,G.,
            Wachter,B., Havlicek,S., Gupta,J., Horn,E., Luningschror,P.,
            Villmann,C., Polat,B., Wischhusen,J., Monoranu,C.M., Kuper,J. and
            Blum,R.
  TITLE     Atypical cellular responses mediated by intracellular constitutive
            active TrkB (NTRK2) kinase domains and a solely intracellular
            NTRK2-fusion oncogene
  JOURNAL   Cancer Gene Ther 31 (9), 1357-1379 (2024)
   PUBMED   39039193
  REMARK    GeneRIF: Atypical cellular responses mediated by intracellular
            constitutive active TrkB (NTRK2) kinase domains and a solely
            intracellular NTRK2-fusion oncogene.
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Zhang,X., Zhang,Y., Yan,H., Yu,H., Zhang,D., Mattay,V.S., Tan,H.Y.
            and Yue,W.
  TITLE     Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2
  JOURNAL   BMC Med 22 (1), 146 (2024)
   PUBMED   38561734
  REMARK    GeneRIF: Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Ikhlef,L., Yassine,M., Chandouri,B., Riviere,L., Naves,T.,
            Dmytruk,N., Gachard,N., Jauberteau,M.O. and Gallet,P.F.
  TITLE     Targeting the NTSR2/TrkB oncogenic pathway in chronic lymphocytic
            leukemia
  JOURNAL   Sci Rep 14 (1), 6084 (2024)
   PUBMED   38480783
  REMARK    GeneRIF: Targeting the NTSR2/TrkB oncogenic pathway in chronic
            lymphocytic leukemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Wang,Y., Liang,J., Xu,B., Yang,J., Wu,Z. and Cheng,L.
  TITLE     TrkB/BDNF signaling pathway and its small molecular agonists in CNS
            injury
  JOURNAL   Life Sci 336, 122282 (2024)
   PUBMED   38008209
  REMARK    GeneRIF: TrkB/BDNF signaling pathway and its small molecular
            agonists in CNS injury.
            Review article
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Luberg,K., Wong,J., Weickert,C.S. and Timmusk,T.
  TITLE     Human TrkB gene: novel alternative transcripts, protein isoforms
            and expression pattern in the prefrontal cerebral cortex during
            postnatal development
  JOURNAL   J Neurochem 113 (4), 952-964 (2010)
   PUBMED   20193039
  REMARK    GeneRIF: Identification of 36 potential TrkB protein isoforms
            suggests high complexity in the synthesis, regulation and function
            of this important neurotrophin receptor emphasizing the need for
            further study of these novel TrkB variants.
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Stoilov,P., Castren,E. and Stamm,S.
  TITLE     Analysis of the human TrkB gene genomic organization reveals novel
            TrkB isoforms, unusual gene length, and splicing mechanism
  JOURNAL   Biochem Biophys Res Commun 290 (3), 1054-1065 (2002)
   PUBMED   11798182
  REMARK    GeneRIF: analysis of TrkB gene reveals novel gene length and
            splicing mechanism
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Haniu,M., Talvenheimo,J., Le,J., Katta,V., Welcher,A. and
            Rohde,M.F.
  TITLE     Extracellular domain of neurotrophin receptor trkB: disulfide
            structure, N-glycosylation sites, and ligand binding
  JOURNAL   Arch Biochem Biophys 322 (1), 256-264 (1995)
   PUBMED   7574684
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Nakagawara,A., Liu,X.G., Ikegaki,N., White,P.S., Yamashiro,D.J.,
            Nycum,L.M., Biegel,J.A. and Brodeur,G.M.
  TITLE     Cloning and chromosomal localization of the human TRK-B tyrosine
            kinase receptor gene (NTRK2)
  JOURNAL   Genomics 25 (2), 538-546 (1995)
   PUBMED   7789988
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Squinto,S.P., Stitt,T.N., Aldrich,T.H., Davis,S., Blanco,S.M.,
            RadzieJewski,C., Glass,D.J., Masiakowski,P., Furth,M.E.,
            Valenzuela,D.M., Distefano,P.S. and Yancopoulos,G.D.
  TITLE     trkB encodes a functional receptor for brain-derived neurotrophic
            factor and neurotrophin-3 but not nerve growth factor
  JOURNAL   Cell 65 (5), 885-893 (1991)
   PUBMED   1710174
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Soppet,D., Escandon,E., Maragos,J., Middlemas,D.S., Reid,S.W.,
            Blair,J., Burton,L.E., Stanton,B.R., Kaplan,D.R., Hunter,T.,
            Nikolics,K. and Parada,L.F.
  TITLE     The neurotrophic factors brain-derived neurotrophic factor and
            neurotrophin-3 are ligands for the trkB tyrosine kinase receptor
  JOURNAL   Cell 65 (5), 895-903 (1991)
   PUBMED   1645620
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390777.13.
            
            Summary: This gene encodes a member of the neurotrophic tyrosine
            receptor kinase (NTRK) family. This kinase is a membrane-bound
            receptor that, upon neurotrophin binding, phosphorylates itself and
            members of the MAPK pathway. Signalling through this kinase leads
            to cell differentiation. Mutations in this gene have been
            associated with obesity and mood disorders. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (z), as well as variants y and aa,
            encodes isoform k.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.436149.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..321
                     /product="BDNF/NT-3 growth factors receptor isoform k"
                     /EC_number="2.7.10.1"
                     /note="BDNF/NT-3 growth factors receptor; tyrosine kinase
                     receptor B; BDNF-tropomyosine receptor kinase B;
                     tropomyosin-related kinase B; neurotrophic tyrosine kinase
                     receptor type 2"
                     /calculated_mol_wt=35201
     Region          1..39
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Region          49..127
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          58..62
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          71..74
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          89..96
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          106..112
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          120..123
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          130..223
                     /region_name="IgI_TrkB_d5"
                     /note="Fifth domain (immunoglobulin-like) of Trk receptor
                     TrkB; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05855"
                     /db_xref="CDD:409441"
     Region          130..138
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409441"
     Region          139..142
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409441"
     Region          145..153
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409441"
     Site            154
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409441"
     Region          156..163
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409441"
     Region          166..169
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409441"
     Region          174..179
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409441"
     Site            order(179,193..194,197)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:409441"
     Region          185..193
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409441"
     Region          201..209
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409441"
     Region          212..220
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409441"
     CDS             1..321
                     /gene="NTRK2"
                     /gene_synonym="DEE58; EIEE58; GP145-TrkB; OBHD; trk-B;
                     TRKB"
                     /coded_by="NM_001369551.1:365..1330"
                     /note="isoform k is encoded by transcript variant z"
                     /db_xref="CCDS:CCDS94429.1"
                     /db_xref="GeneID:4915"
                     /db_xref="HGNC:HGNC:8032"
                     /db_xref="MIM:600456"
ORIGIN      
        1 mwiktlqeak sspdtqdlyc lnessknipl anlqipncgl psanlaapnl tveegksitl
       61 scsvagdpvp nmywdvgnlv skhmnetsht qgslritnis sddsgkqisc vaenlvgedq
      121 dsvnltvhfa ptitflespt sdhhwcipft vkgnpkpalq wfyngailne skyictkihv
      181 tnhteyhgcl qldnpthmnn gdytliakne ygkdekqisa hfmgwpgidd ganpnypdvi
      241 yedygtaand igdttnrsne ipstdvtdkt grehlsvyav vviasvvgfc llvmlfllkl
      301 arhskfgmkg fvlfhkipld g
//
LOCUS       NP_001171656            1395 aa            linear   PRI 27-APR-2025
DEFINITION  G-protein coupled receptor-associated sorting protein 1 [Homo
            sapiens].
ACCESSION   NP_001171656
VERSION     NP_001171656.1
DBSOURCE    REFSEQ: accession NM_001184727.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1395)
  AUTHORS   Du,J., Chen,Y., Liu,G., Zeng,Q., Zhou,N. and Du,D.
  TITLE     Comprehensive pan-cancer analysis of role of GPRASP1, associated
            with clinical outcomes, immune microenvironment, and
            immunotherapeutic efficiency in pancreatic cancer
  JOURNAL   Pathol Res Pract 243, 154374 (2023)
   PUBMED   36801507
  REMARK    GeneRIF: Comprehensive pan-cancer analysis of role of GPRASP1,
            associated with clinical outcomes, immune microenvironment, and
            immunotherapeutic efficiency in pancreatic cancer.
REFERENCE   2  (residues 1 to 1395)
  AUTHORS   Zhang,T., Liu,G., Zhang,J., Chen,S., Deng,Z. and Xie,M.
  TITLE     GPRASP1 is a candidate anti-oncogene and correlates with immune
            microenvironment and immunotherapeutic efficiency in head and neck
            cancer
  JOURNAL   J Oral Pathol Med 52 (3), 232-244 (2023)
   PUBMED   36264603
  REMARK    GeneRIF: GPRASP1 is a candidate anti-oncogene and correlates with
            immune microenvironment and immunotherapeutic efficiency in head
            and neck cancer.
REFERENCE   3  (residues 1 to 1395)
  AUTHORS   Zheng,X., Chang,F., Rong,Y. and Tuszynski,G.P.
  TITLE     G-protein coupled receptor-associated sorting protein 1 (GASP-1), a
            ubiquitous tumor marker, promotes proliferation and invasion of
            triple negative breast cancer
  JOURNAL   Exp Mol Pathol 125, 104751 (2022)
   PUBMED   35122807
  REMARK    GeneRIF: G-protein coupled receptor-associated sorting protein 1
            (GASP-1), a ubiquitous tumor marker, promotes proliferation and
            invasion of triple negative breast cancer.
REFERENCE   4  (residues 1 to 1395)
  AUTHORS   Manfra,O., Van Craenenbroeck,K., Skieterska,K., Frimurer,T.,
            Schwartz,T.W., Levy,F.O. and Andressen,K.W.
  TITLE     Downregulation of 5-HT7 Serotonin Receptors by the Atypical
            Antipsychotics Clozapine and Olanzapine. Role of Motifs in the
            C-Terminal Domain and Interaction with GASP-1
  JOURNAL   ACS Chem Neurosci 6 (7), 1206-1218 (2015)
   PUBMED   25706089
  REMARK    GeneRIF: Study demonstrated that binding of clozapine or olanzapine
            to the 5-HT7 receptor leads to antagonist-mediated lysosomal
            degradation by exposing key residues in the C-terminal tail that
            interact with GASP-1
REFERENCE   5  (residues 1 to 1395)
  AUTHORS   He,C., Wei,Y., Sun,K., Li,B., Dong,X., Zou,Z., Liu,Y., Kinch,L.N.,
            Khan,S., Sinha,S., Xavier,R.J., Grishin,N.V., Xiao,G.,
            Eskelinen,E.L., Scherer,P.E., Whistler,J.L. and Levine,B.
  TITLE     Beclin 2 functions in autophagy, degradation of G protein-coupled
            receptors, and metabolism
  JOURNAL   Cell 154 (5), 1085-1099 (2013)
   PUBMED   23954414
REFERENCE   6  (residues 1 to 1395)
  AUTHORS   Bartlett,S.E., Enquist,J., Hopf,F.W., Lee,J.H., Gladher,F.,
            Kharazia,V., Waldhoer,M., Mailliard,W.S., Armstrong,R., Bonci,A.
            and Whistler,J.L.
  TITLE     Dopamine responsiveness is regulated by targeted sorting of D2
            receptors
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11521-11526 (2005)
   PUBMED   16049099
  REMARK    GeneRIF: Modulation of the D2-GASP interaction is important for the
            functional down-regulation of D2 dopamine receptors.
REFERENCE   7  (residues 1 to 1395)
  AUTHORS   Ross,M.T., Grafham,D.V., Coffey,A.J., Scherer,S., McLay,K.,
            Muzny,D., Platzer,M., Howell,G.R., Burrows,C., Bird,C.P.,
            Frankish,A., Lovell,F.L., Howe,K.L., Ashurst,J.L., Fulton,R.S.,
            Sudbrak,R., Wen,G., Jones,M.C., Hurles,M.E., Andrews,T.D.,
            Scott,C.E., Searle,S., Ramser,J., Whittaker,A., Deadman,R.,
            Carter,N.P., Hunt,S.E., Chen,R., Cree,A., Gunaratne,P., Havlak,P.,
            Hodgson,A., Metzker,M.L., Richards,S., Scott,G., Steffen,D.,
            Sodergren,E., Wheeler,D.A., Worley,K.C., Ainscough,R.,
            Ambrose,K.D., Ansari-Lari,M.A., Aradhya,S., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Ballabio,A., Banerjee,R., Barker,G.E.,
            Barlow,K.F., Barrett,I.P., Bates,K.N., Beare,D.M., Beasley,H.,
            Beasley,O., Beck,A., Bethel,G., Blechschmidt,K., Brady,N.,
            Bray-Allen,S., Bridgeman,A.M., Brown,A.J., Brown,M.J., Bonnin,D.,
            Bruford,E.A., Buhay,C., Burch,P., Burford,D., Burgess,J.,
            Burrill,W., Burton,J., Bye,J.M., Carder,C., Carrel,L., Chako,J.,
            Chapman,J.C., Chavez,D., Chen,E., Chen,G., Chen,Y., Chen,Z.,
            Chinault,C., Ciccodicola,A., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S., Clerc-Blankenburg,K., Clifford,K., Cobley,V., Cole,C.G.,
            Conquer,J.S., Corby,N., Connor,R.E., David,R., Davies,J., Davis,C.,
            Davis,J., Delgado,O., Deshazo,D., Dhami,P., Ding,Y., Dinh,H.,
            Dodsworth,S., Draper,H., Dugan-Rocha,S., Dunham,A., Dunn,M.,
            Durbin,K.J., Dutta,I., Eades,T., Ellwood,M., Emery-Cohen,A.,
            Errington,H., Evans,K.L., Faulkner,L., Francis,F., Frankland,J.,
            Fraser,A.E., Galgoczy,P., Gilbert,J., Gill,R., Glockner,G.,
            Gregory,S.G., Gribble,S., Griffiths,C., Grocock,R., Gu,Y.,
            Gwilliam,R., Hamilton,C., Hart,E.A., Hawes,A., Heath,P.D.,
            Heitmann,K., Hennig,S., Hernandez,J., Hinzmann,B., Ho,S., Hoffs,M.,
            Howden,P.J., Huckle,E.J., Hume,J., Hunt,P.J., Hunt,A.R.,
            Isherwood,J., Jacob,L., Johnson,D., Jones,S., de Jong,P.J.,
            Joseph,S.S., Keenan,S., Kelly,S., Kershaw,J.K., Khan,Z.,
            Kioschis,P., Klages,S., Knights,A.J., Kosiura,A., Kovar-Smith,C.,
            Laird,G.K., Langford,C., Lawlor,S., Leversha,M., Lewis,L., Liu,W.,
            Lloyd,C., Lloyd,D.M., Loulseged,H., Loveland,J.E., Lovell,J.D.,
            Lozado,R., Lu,J., Lyne,R., Ma,J., Maheshwari,M., Matthews,L.H.,
            McDowall,J., McLaren,S., McMurray,A., Meidl,P., Meitinger,T.,
            Milne,S., Miner,G., Mistry,S.L., Morgan,M., Morris,S., Muller,I.,
            Mullikin,J.C., Nguyen,N., Nordsiek,G., Nyakatura,G., O'Dell,C.N.,
            Okwuonu,G., Palmer,S., Pandian,R., Parker,D., Parrish,J.,
            Pasternak,S., Patel,D., Pearce,A.V., Pearson,D.M., Pelan,S.E.,
            Perez,L., Porter,K.M., Ramsey,Y., Reichwald,K., Rhodes,S.,
            Ridler,K.A., Schlessinger,D., Schueler,M.G., Sehra,H.K.,
            Shaw-Smith,C., Shen,H., Sheridan,E.M., Shownkeen,R., Skuce,C.D.,
            Smith,M.L., Sotheran,E.C., Steingruber,H.E., Steward,C.A.,
            Storey,R., Swann,R.M., Swarbreck,D., Tabor,P.E., Taudien,S.,
            Taylor,T., Teague,B., Thomas,K., Thorpe,A., Timms,K., Tracey,A.,
            Trevanion,S., Tromans,A.C., d'Urso,M., Verduzco,D., Villasana,D.,
            Waldron,L., Wall,M., Wang,Q., Warren,J., Warry,G.L., Wei,X.,
            West,A., Whitehead,S.L., Whiteley,M.N., Wilkinson,J.E.,
            Willey,D.L., Williams,G., Williams,L., Williamson,A.,
            Williamson,H., Wilming,L., Woodmansey,R.L., Wray,P.W., Yen,J.,
            Zhang,J., Zhou,J., Zoghbi,H., Zorilla,S., Buck,D., Reinhardt,R.,
            Poustka,A., Rosenthal,A., Lehrach,H., Meindl,A., Minx,P.J.,
            Hillier,L.W., Willard,H.F., Wilson,R.K., Waterston,R.H., Rice,C.M.,
            Vaudin,M., Coulson,A., Nelson,D.L., Weinstock,G., Sulston,J.E.,
            Durbin,R., Hubbard,T., Gibbs,R.A., Beck,S., Rogers,J. and
            Bentley,D.R.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
REFERENCE   8  (residues 1 to 1395)
  AUTHORS   Heydorn,A., Sondergaard,B.P., Ersboll,B., Holst,B., Nielsen,F.C.,
            Haft,C.R., Whistler,J. and Schwartz,T.W.
  TITLE     A library of 7TM receptor C-terminal tails. Interactions with the
            proposed post-endocytic sorting proteins ERM-binding phosphoprotein
            50 (EBP50), N-ethylmaleimide-sensitive factor (NSF), sorting nexin
            1 (SNX1), and G protein-coupled receptor-associated sorting protein
            (GASP)
  JOURNAL   J Biol Chem 279 (52), 54291-54303 (2004)
   PUBMED   15452121
REFERENCE   9  (residues 1 to 1395)
  AUTHORS   Simonin,F., Karcher,P., Boeuf,J.J., Matifas,A. and Kieffer,B.L.
  TITLE     Identification of a novel family of G protein-coupled receptor
            associated sorting proteins
  JOURNAL   J Neurochem 89 (3), 766-775 (2004)
   PUBMED   15086532
REFERENCE   10 (residues 1 to 1395)
  AUTHORS   Whistler,J.L., Enquist,J., Marley,A., Fong,J., Gladher,F.,
            Tsuruda,P., Murray,S.R. and Von Zastrow,M.
  TITLE     Modulation of postendocytic sorting of G protein-coupled receptors
  JOURNAL   Science 297 (5581), 615-620 (2002)
   PUBMED   12142540
  REMARK    GeneRIF: identified a protein that binds preferentially to the
            cytoplasmic tail of the delta opioid receptor as a candidate
            heterotrimeric GTP-binding protein (G protein)-coupled
            receptor-associated sorting protein (GASP) [GASP]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX954816.1, BX489726.1,
            BC114552.1, AY044233.1 and AW293629.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the GPRASP (G
            protein-coupled receptor associated sorting protein) family. The
            protein may modulate lysosomal sorting and functional
            down-regulation of a variety of G-protein coupled receptors. It
            targets receptors for degradation in lysosomes. The receptors
            interacting with this sorting protein include D2 dopamine receptor
            (DRD2), delta opioid receptor (OPRD1), beta-2 adrenergic receptor
            (ADRB2), D4 dopamine receptor (DRD4) and cannabinoid 1 receptor
            (CB1R). Multiple alternatively spliced transcript variants encoding
            the same protein have been identified. [provided by RefSeq, May
            2010].
            
            Transcript Variant: This variant (4) has an additional exon in the
            5' UTR and encodes the same protein, as compared to variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.256013.1,
                                           SRR1803613.156277.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000537097.2/ ENSP00000445683.1
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..1395
                     /product="G-protein coupled receptor-associated sorting
                     protein 1"
                     /calculated_mol_wt=156735
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JY77.3)"
     Region          45..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JY77.3)"
     Region          269..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JY77.3)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5U4C1; propagated from
                     UniProtKB/Swiss-Prot (Q5JY77.3)"
     Region          446..469
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JY77.3)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5U4C1; propagated from
                     UniProtKB/Swiss-Prot (Q5JY77.3)"
     Region          899..1395
                     /region_name="OPRD1-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JY77.3)"
     Site            899
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q920R4; propagated from
                     UniProtKB/Swiss-Prot (Q5JY77.3)"
     Region          1167..1370
                     /region_name="Arm_2"
                     /note="Armadillo-like; pfam04826"
                     /db_xref="CDD:461447"
     CDS             1..1395
                     /gene="GPRASP1"
                     /gene_synonym="GASP; GASP-1; GASP1"
                     /coded_by="NM_001184727.2:732..4919"
                     /db_xref="CCDS:CCDS35352.1"
                     /db_xref="GeneID:9737"
                     /db_xref="HGNC:HGNC:24834"
                     /db_xref="MIM:300417"
ORIGIN      
        1 mtgaeiesga qvkpekkpge evvggaeien dvplvvrpkv rtqaqimpga rpknkskvmp
       61 gastkvetsa vggarpkska kaipvsrfke eaqmwaqprf gaerlskter nsqtniiasp
      121 lvstdsvlva ktkylsedre lvntdtesfp rrkahyqagf qpsfrskeet nmgswccprp
      181 tskqeaspns dfkwvdksvs slfwsgdevt akfhpgnrvk dsnrsmhman qeantmsrsq
      241 tnqelyiass sgsedesvkt pwfwardktn twsgpredpn srsrfrskke vyvesssgse
      301 hedhleswfg agkeakfrsk mragkeannr arhrakreac idfmpgsidv ikkescfwpe
      361 enantfsrpm ikkeararam tkeeaktkar arakqearse eealigtwfw atdessmade
      421 asiesslqve desiigswfw teeeasmgtg assksrprtd gerigdslfg arektsmktg
      481 aeatsesila addeqviigs wfwageevnq eaeeetifgs wfwvidaasv esgvgvsces
      541 rtrseeeevi gpwfwsgeqv dieagigeea rpgaeeetif gswfwaenqt ymdcraetsc
      601 dtmqgaeeee piigswfwtr veacvegdvn skssledkee amipcfgake evsmkhgtgv
      661 rcrfmagaee tnnkscfwae kepcmypagg gswksrpeee edivnswfws rkytkpeaii
      721 gswlwatees nidgtgekak llteeetiin swfwkedeai seatdreesr peaeegdiig
      781 swfwageedr lepaaetree drlaaekegi vgswfgaree tirreagscs ksspkaeeee
      841 viigswfwee easpeavagv gfeskpgtee eeitvgswfw peeeasiqag sqaveemese
      901 teeetifgsw fwdgkevsee agpccvskpe ddeemivesw fwsrdkaike tgtvatcesk
      961 peneegaivg swfeaedevd nrtdngsncg srtladedea ivgswfwagd eahfesnpsp
     1021 vfraicrstc sveqepdpsr rpqsweevtv qfkpgpwgrv gfpsispfrf pkeaaslfce
     1081 mfggkprnmv lspegedqes llqpdqpspe fpfqydpsyr svqeirehlr akestepess
     1141 scnciqcelk igseefeell llmekirdpf iheiskiamg mrsasqftrd firdsgvvsl
     1201 ietllnypss rvrtsflenm irmappypnl niiqtyickv ceetlaysvd speqlsgirm
     1261 irhlttttdy htlvanymsg flsllatgna ktrfhvlkml lnlsenlfmt kellsaeavs
     1321 efiglfnree tndniqivla ifenignnik ketvfsdddf nieplisafh kvekfakelq
     1381 gktdnqndpe gdqen
//
LOCUS       NP_989695                314 aa            linear   VRT 27-APR-2025
DEFINITION  homeobox protein SIX3 [Gallus gallus].
ACCESSION   NP_989695 XP_015139313
VERSION     NP_989695.1
DBSOURCE    REFSEQ: accession NM_204364.2
KEYWORDS    RefSeq.
SOURCE      Gallus gallus (chicken)
  ORGANISM  Gallus gallus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
            Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
            Phasianidae; Phasianinae; Gallus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Tang,H., Finn,R.D. and Thomas,P.D.
  TITLE     TreeGrafter: phylogenetic tree-based annotation of proteins with
            Gene Ontology terms and other annotations
  JOURNAL   Bioinformatics 35 (3), 518-520 (2019)
   PUBMED   30032202
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Bovolenta,P., Mallamaci,A., Puelles,L. and Boncinelli,E.
  TITLE     Expression pattern of cSix3, a member of the Six/sine oculis family
            of transcription factors
  JOURNAL   Mech Dev 70 (1-2), 201-203 (1998)
   PUBMED   9510037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AADN05000005.1.
            
            On Jan 17, 2016 this sequence version replaced XP_015139313.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns
                              SAMEA103992432, SAMEA103992440 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Gallus gallus"
                     /db_xref="taxon:9031"
                     /chromosome="3"
                     /map="3"
                     /breed="Red Jungle Fowl"
     Protein         1..314
                     /product="homeobox protein SIX3"
                     /note="sine oculis homeobox homolog 3"
                     /calculated_mol_wt=34546
     Region          69..182
                     /region_name="SIX1_SD"
                     /note="Transcriptional regulator, SIX1, N-terminal SD
                     domain; pfam16878"
                     /db_xref="CDD:465293"
     Region          190..238
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(191,194,234,237..238)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          214..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O42406.2)"
     Region          240..314
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O42406.2)"
     CDS             1..314
                     /gene="SIX3"
                     /gene_synonym="CSIX3"
                     /coded_by="NM_204364.2:209..1153"
                     /db_xref="CGNC:49119"
                     /db_xref="GeneID:378786"
ORIGIN      
        1 mvfrsplely pthfflpnfa adphhrslll asggsgsgsg cspgaggggg ssrapheels
       61 mfqlptlnfs peqvasvcet leetgdierl grflwslpva pgaceainkh esilraravv
      121 afhtgnfrdl yhilenhkft keshgklqam wleahyqeae klrgrplgpv dkyrvrkkfp
      181 lprtiwdgeq kthcfkertr sllrewylqd pypnpskkre laqatgltpt qvgnwfknrr
      241 qrdraaaakn rlqhqaigqs gmrslaepgc pthssaesps taaspttsvs slteraetgt
      301 silsvtssds ecdv
//
LOCUS       NP_001037850             408 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 237 isoform a [Homo sapiens].
ACCESSION   NP_001037850
VERSION     NP_001037850.1
DBSOURCE    REFSEQ: accession NM_001044385.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Skiba,N.P., Cady,M.A., Molday,L., Han,J.Y.S., Lewis,T.R.,
            Spencer,W.J., Thompson,W.J., Hiles,S., Philp,N.J., Molday,R.S. and
            Arshavsky,V.Y.
  TITLE     TMEM67, TMEM237, and Embigin in Complex With Monocarboxylate
            Transporter MCT1 Are Unique Components of the Photoreceptor Outer
            Segment Plasma Membrane
  JOURNAL   Mol Cell Proteomics 20, 100088 (2021)
   PUBMED   33933680
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Zuniga,F.I. and Craft,C.M.
  TITLE     Deciphering the structure and function of Als2cr4 in the mouse
            retina
  JOURNAL   Invest Ophthalmol Vis Sci 51 (9), 4407-4415 (2010)
   PUBMED   20375344
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Hadano,S., Hand,C.K., Osuga,H., Yanagisawa,Y., Otomo,A.,
            Devon,R.S., Miyamoto,N., Showguchi-Miyata,J., Okada,Y.,
            Singaraja,R., Figlewicz,D.A., Kwiatkowski,T., Hosler,B.A.,
            Sagie,T., Skaug,J., Nasir,J., Brown,R.H. Jr., Scherer,S.W.,
            Rouleau,G.A., Hayden,M.R. and Ikeda,J.E.
  TITLE     A gene encoding a putative GTPase regulator is mutated in familial
            amyotrophic lateral sclerosis 2
  JOURNAL   Nat Genet 29 (2), 166-173 (2001)
   PUBMED   11586298
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP226834.1, AB053301.1 and
            AC007282.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a tetraspanin protein
            that is thought to be involved in WNT signaling. Defects in this
            gene are a cause of Joubert syndrome-14. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2012].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.11420.1,
                                           SRR1803615.79417.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409883.7/ ENSP00000386264.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..408
                     /product="transmembrane protein 237 isoform a"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 4; amyotrophic lateral
                     sclerosis 2 chromosomal region candidate gene 4 protein"
                     /calculated_mol_wt=45395
     Region          1..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q45.2)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96Q45.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96Q45.2)"
     Region          140..383
                     /region_name="TMEM237"
                     /note="Transmembrane protein 237; pfam15383"
                     /db_xref="CDD:464690"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q45.2)"
     Site            268..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q45.2)"
     Site            303..323
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q45.2)"
     Site            358..378
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q45.2)"
     CDS             1..408
                     /gene="TMEM237"
                     /gene_synonym="ALS2CR4; JBTS14"
                     /coded_by="NM_001044385.3:104..1330"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46489.1"
                     /db_xref="GeneID:65062"
                     /db_xref="HGNC:HGNC:14432"
                     /db_xref="MIM:614423"
ORIGIN      
        1 mrtdsgarle eghlrppral ppvpsqddip lsrpkkkkpr tkntpasasl eglaqtagrr
       61 psegnepstk elkehpeapv qrrqkktrlp leletsstqk ksssssllrn engidaepae
      121 eaviqkprrk tkktqpaelq yanelgvede diitdeqttv eqqsvftapt gisqpvgkvf
      181 veksrrfqaa drseliktte nidvsmdvkp swttrdvalt vhrafrmigl fshgflagca
      241 vwnivviyvl agdqlsnlsn llqqyktlay pfqsllylll alstisafdr idfakisvai
      301 rnflaldpta lasflyftal ilslsqqmts drihlytpss vngslweagi eeqilqpwiv
      361 vnlvvallvg lswlflsyrp gmdlseelmf sseveeypdk ekeikass
//
LOCUS       NP_620166                590 aa            linear   PRI 27-APR-2025
DEFINITION  sperm-associated microtubule inner protein 4 [Homo sapiens].
ACCESSION   NP_620166
VERSION     NP_620166.3
DBSOURCE    REFSEQ: accession NM_138811.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Leung,M.R., Zeng,J., Wang,X., Roelofs,M.C., Huang,W., Zenezini
            Chiozzi,R., Hevler,J.F., Heck,A.J.R., Dutcher,S.K., Brown,A.,
            Zhang,R. and Zeev-Ben-Mordehai,T.
  TITLE     Structural specializations of the sperm tail
  JOURNAL   Cell 186 (13), 2880-2896 (2023)
   PUBMED   37327785
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Liu,S., Xu,Y. and Zhang,S.
  TITLE     LINGO1, C7orf31 and VEGFA are prognostic genes of primary
            glioblastoma: analysis of gene expression microarray
  JOURNAL   Neoplasma 65 (4), 532-541 (2018)
   PUBMED   30064229
  REMARK    GeneRIF: LINGO1 might be a positive primary glioblastoma prognostic
            gene and C7orf31 and VEGFA might be negative prognosticators.
REFERENCE   5  (residues 1 to 590)
  AUTHORS   Firat-Karalar,E.N., Sante,J., Elliott,S. and Stearns,T.
  TITLE     Proteomic analysis of mammalian sperm cells identifies new
            components of the centrosome
  JOURNAL   J Cell Sci 127 (Pt 19), 4128-4133 (2014)
   PUBMED   25074808
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004129.2, BC043269.2, BI830207.1, BC060879.1 and BX640851.1.
            
            On Dec 1, 2003 this sequence version replaced NP_620166.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All three variants encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060879.1, SRR1803612.109165.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283905.8/ ENSP00000283905.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.3"
     Protein         1..590
                     /product="sperm-associated microtubule inner protein 4"
                     /note="uncharacterized protein C7orf31; sperm associated
                     microtubule inner protein 4"
                     /calculated_mol_wt=68334
     Region          1..283
                     /region_name="DUF4555"
                     /note="Domain of unknown function (DUF4555); pfam15093"
                     /db_xref="CDD:464498"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6AYM0; propagated from
                     UniProtKB/Swiss-Prot (Q8N865.3)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AYM0; propagated from
                     UniProtKB/Swiss-Prot (Q8N865.3)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AYM0; propagated from
                     UniProtKB/Swiss-Prot (Q8N865.3)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q6AYM0; propagated from
                     UniProtKB/Swiss-Prot (Q8N865.3)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AYM0; propagated from
                     UniProtKB/Swiss-Prot (Q8N865.3)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AYM0; propagated from
                     UniProtKB/Swiss-Prot (Q8N865.3)"
     CDS             1..590
                     /gene="SPMIP4"
                     /gene_synonym="C7orf31"
                     /coded_by="NM_138811.4:718..2490"
                     /db_xref="CCDS:CCDS5394.1"
                     /db_xref="GeneID:136895"
                     /db_xref="HGNC:HGNC:21722"
                     /db_xref="MIM:616071"
ORIGIN      
        1 mevihgrpyc crelegadil sntfysnelh nplqtvtrpt asedryqelr eslqqcrlpw
       61 gaereyggii pislpedhrp kyepprvmgk ghqhygfgge twprklpveq fyyltqnkks
      121 dvygndslip kppnstvgei clpypiehpy hthicrgamf ptftspedly tgikartqqp
      181 fpptvptkay dstvlktrgn pyryelidip mdskkkaltw pgqgvyydfp rgveknkpvf
      241 ypkppktfap ntslnswdpi csakeaniqr nlershwlts ythdftglgp mdplelddyh
      301 ekmvaeltrk igfdpepqek fhpvfkpprp legriarliq nrrsleaivq qrprscpdct
      361 prvlcnfhtf vpsskemval sdnipagvth knqdieekii eeqsllstye lpscyptkdl
      421 tsiydikpfp kitdtkkted lywrqqslkt qptpyckpdh wihyenlksp lrdqynmcpd
      481 pvslskpsvl qnkqdteaft lehflskpee elflnmenne etrpvlgwip ragvtkpqtn
      541 llelknsfsk tgaqkrfhks iledhkdlrd nehsgmkhqf yghnsyyfyn
//
LOCUS       NP_001354268             115 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 142 isoform 4 [Homo sapiens].
ACCESSION   NP_001354268
VERSION     NP_001354268.1
DBSOURCE    REFSEQ: accession NM_001367339.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Mir,A., Song,Y., Lee,H., Montazer-Zohouri,M., Reisi,M. and
            Tabatabaiefar,M.A.
  TITLE     A deleterious frameshift insertion mutation in the ZNF142 gene
            leads to intellectual developmental disorder with impaired speech
            in three affected siblings: Clinical features and literature review
  JOURNAL   Mol Genet Genomic Med 11 (12), e2261 (2023)
   PUBMED   37496384
  REMARK    GeneRIF: A deleterious frameshift insertion mutation in the ZNF142
            gene leads to intellectual developmental disorder with impaired
            speech in three affected siblings: Clinical features and literature
            review.
            Review article
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Christensen,M.B., Levy,A.M., Mohammadi,N.A., Niceta,M.,
            Kaiyrzhanov,R., Dentici,M.L., Al Alam,C., Alesi,V., Benoit,V.,
            Bhatia,K.P., Bierhals,T., Bosselmann,C.M., Buratti,J.,
            Callewaert,B., Ceulemans,B., Charles,P., De Wachter,M.,
            Dehghani,M., D'haenens,E., Doco-Fenzy,M., Gessner,M., Gobert,C.,
            Guliyeva,U., Haack,T.B., Hammer,T.B., Heinrich,T., Hempel,M.,
            Herget,T., Hoffmann,U., Horvath,J., Houlden,H., Keren,B.,
            Kresge,C., Kumps,C., Lederer,D., Lermine,A., Magrinelli,F.,
            Maroofian,R., Vahidi Mehrjardi,M.Y., Moudi,M., Muller,A.J.,
            Oostra,A.J., Pletcher,B.A., Ros-Pardo,D., Samarasekera,S.,
            Tartaglia,M., Van Schil,K., Vogt,J., Wassmer,E., Winkelmann,J.,
            Zaki,M.S., Zech,M., Lerche,H., Radio,F.C., Gomez-Puertas,P.,
            Moller,R.S. and Tumer,Z.
  TITLE     Biallelic variants in ZNF142 lead to a syndromic neurodevelopmental
            disorder
  JOURNAL   Clin Genet 102 (2), 98-109 (2022)
   PUBMED   35616059
  REMARK    GeneRIF: Biallelic variants in ZNF142 lead to a syndromic
            neurodevelopmental disorder.
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Kamal,N., Khamirani,H.J., Mohammadi,S., Dastgheib,S.A.,
            Dianatpour,M. and Tabei,S.M.B.
  TITLE     ZNF142 mutation causes neurodevelopmental disorder with speech
            impairment and seizures: Novel variants and literature review
  JOURNAL   Eur J Med Genet 65 (7), 104522 (2022)
   PUBMED   35618198
  REMARK    GeneRIF: ZNF142 mutation causes neurodevelopmental disorder with
            speech impairment and seizures: Novel variants and literature
            review.
            Review article
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Kameyama,S., Mizuguchi,T., Fukuda,H., Moey,L.H., Keng,W.T.,
            Okamoto,N., Tsuchida,N., Uchiyama,Y., Koshimizu,E., Hamanaka,K.,
            Fujita,A., Miyatake,S. and Matsumoto,N.
  TITLE     Biallelic null variants in ZNF142 cause global developmental delay
            with familial epilepsy and dysmorphic features
  JOURNAL   J Hum Genet 67 (3), 169-173 (2022)
   PUBMED   34531528
  REMARK    GeneRIF: Biallelic null variants in ZNF142 cause global
            developmental delay with familial epilepsy and dysmorphic features.
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Ahmeti,K.B., Ajroud-Driss,S., Al-Chalabi,A., Andersen,P.M.,
            Armstrong,J., Birve,A., Blauw,H.M., Brown,R.H., Bruijn,L., Chen,W.,
            Chio,A., Comeau,M.C., Cronin,S., Diekstra,F.P., Soraya Gkazi,A.,
            Glass,J.D., Grab,J.D., Groen,E.J., Haines,J.L., Hardiman,O.,
            Heller,S., Huang,J., Hung,W.Y., Jaworski,J.M., Jones,A., Khan,H.,
            Landers,J.E., Langefeld,C.D., Leigh,P.N., Marion,M.C.,
            McLaughlin,R.L., Meininger,V., Melki,J., Miller,J.W., Mora,G.,
            Pericak-Vance,M.A., Rampersaud,E., Robberecht,W., Russell,L.P.,
            Salachas,F., Saris,C.G., Shatunov,A., Shaw,C.E., Siddique,N.,
            Siddique,T., Smith,B.N., Sufit,R., Topp,S., Traynor,B.J., Vance,C.,
            van Damme,P., van den Berg,L.H., van Es,M.A., van Vught,P.W.,
            Veldink,J.H., Yang,Y. and Zheng,J.G.
  CONSRTM   ITALSGEN consortium; ALSGEN Consortium
  TITLE     Age of onset of amyotrophic lateral sclerosis is modulated by a
            locus on 1p34.1
  JOURNAL   Neurobiol Aging 34 (1), 357 (2013)
   PUBMED   22959728
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079810.4 and AC012510.8.
            
            Summary: The protein encoded by this gene belongs to the Kruppel
            family of C2H2-type zinc finger proteins. It contains 31 C2H2-type
            zinc fingers and may be involved in transcriptional regulation.
            Alternatively spliced transcript variants have been found for this
            gene. [provided by RefSeq, Jan 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP248229.1, BP314194.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..115
                     /product="zinc finger protein 142 isoform 4"
                     /note="zinc finger protein 142 (clone pHZ-49)"
                     /calculated_mol_wt=11607
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52746.4)"
     CDS             1..115
                     /gene="ZNF142"
                     /gene_synonym="HA4654; NEDISHM; pHZ-49"
                     /coded_by="NM_001367339.1:855..1202"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:7701"
                     /db_xref="HGNC:HGNC:12927"
                     /db_xref="MIM:604083"
ORIGIN      
        1 mtdplldsqp asstgemdgl cpelllippp lsnrgilgpv qspcpsrdpa piptepgcll
       61 veatateegp gnmeiivetv agtltpgapg etpgtntvas rpvgqaalrf clgyf
//
LOCUS       NP_848644                580 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 678 isoform 1 [Homo sapiens].
ACCESSION   NP_848644
VERSION     NP_848644.2
DBSOURCE    REFSEQ: accession NM_178549.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Lee,J.J., Essers,J.B., Kugathasan,S., Escher,J.C., Lettre,G.,
            Butler,J.L., Stephens,M.C., Ramoni,M.F., Grand,R.J. and
            Hirschhorn,J.
  TITLE     Association of linear growth impairment in pediatric Crohn's
            disease and a known height locus: a pilot study
  JOURNAL   Ann Hum Genet 74 (6), 489-497 (2010)
   PUBMED   20846217
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Zhao,J., Li,M., Bradfield,J.P., Zhang,H., Mentch,F.D., Wang,K.,
            Sleiman,P.M., Kim,C.E., Glessner,J.T., Hou,C., Keating,B.J.,
            Thomas,K.A., Garris,M.L., Deliard,S., Frackelton,E.C., Otieno,F.G.,
            Chiavacci,R.M., Berkowitz,R.I., Hakonarson,H. and Grant,S.F.
  TITLE     The role of height-associated loci identified in genome wide
            association studies in the determination of pediatric stature
  JOURNAL   BMC Med Genet 11, 96 (2010)
   PUBMED   20546612
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Weedon,M.N., Lango,H., Lindgren,C.M., Wallace,C., Evans,D.M.,
            Mangino,M., Freathy,R.M., Perry,J.R., Stevens,S., Hall,A.S.,
            Samani,N.J., Shields,B., Prokopenko,I., Farrall,M., Dominiczak,A.,
            Johnson,T., Bergmann,S., Beckmann,J.S., Vollenweider,P.,
            Waterworth,D.M., Mooser,V., Palmer,C.N., Morris,A.D.,
            Ouwehand,W.H., Zhao,J.H., Li,S., Loos,R.J., Barroso,I.,
            Deloukas,P., Sandhu,M.S., Wheeler,E., Soranzo,N., Inouye,M.,
            Wareham,N.J., Caulfield,M., Munroe,P.B., Hattersley,A.T.,
            McCarthy,M.I. and Frayling,T.M.
  CONSRTM   Diabetes Genetics Initiative; Wellcome Trust Case Control
            Consortium; Cambridge GEM Consortium
  TITLE     Genome-wide association analysis identifies 20 loci that influence
            adult height
  JOURNAL   Nat Genet 40 (5), 575-583 (2008)
   PUBMED   18391952
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL451054.22 and AL592310.6.
            
            On Dec 30, 2009 this sequence version replaced NP_848644.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA745424.1, SRR1660805.372926.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.13"
     Protein         1..580
                     /product="zinc finger protein 678 isoform 1"
                     /note="hypothetical protein MGC42493"
                     /calculated_mol_wt=67965
     Region          43..83
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          138..536
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          154..174
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(159,161,163,165..166,169..170,173,187,189,193..194,
                     197..198,201,215,217,219,221..222,225..226,229)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          182..202
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..230
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          238..258
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          266..286
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          294..314
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          322..342
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          350..370
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          378..398
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(383,385,387,389..390,393..394,397,411,413,417..418,
                     421..422,425,439,441,443,445..446,449..450,453)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          406..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          434..454
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          462..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(467,469,471,473..474,477..478,481,495,497,501..502,
                     505..506,509,523,525,527,529..530,533..534,537)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          490..510
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..555
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     CDS             1..580
                     /gene="ZNF678"
                     /coded_by="NM_178549.4:140..1882"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:339500"
                     /db_xref="HGNC:HGNC:28652"
ORIGIN      
        1 mpghpesrkt rriltmlprl vlnsfpqvil lpnppkvlrl qgllafsdvv iefspeewac
       61 ldpaqrnlyr dvmfenyrnl vslailsysi qdllpeqdmk dlcqkvtltr hrswgldnlh
      121 lvkdwrtvne gkgqkeycnr ltqcsstksk ifqciecgrn fswrsilteh krihtgekpy
      181 kceecgkvfn rcsnltkhkr ihtgekpykc decgkvfnww sqltnhkkih tgekpykcde
      241 cdkvfnwwsq ltshkkihsg ekpypceecg kaftqfsnlt qhkrihtgek pykckeccka
      301 fnkfsnltqh krihtgekpy kceecgnvfn ecshltrhrr ihtgekpykc eecgkaftqf
      361 asltrhkrih tgekpyqcee cgktfnrcsh lsshkrihtg ekpykceecg rtftqfsnlt
      421 qhkrihtgek pykckecgka fnkfssltqh rrihtgvkpy kceecgkvfk qcshltshkr
      481 ihtgekpykc kecgkafyqs silskhkrih teekpykcee cgkafnqfss ltrhkrihtg
      541 ekrykckecg kgfyqssihs kykriytgee pdkckkcgsl
//
LOCUS       NP_055558               1395 aa            linear   PRI 27-APR-2025
DEFINITION  uncharacterized protein KIAA0232 [Homo sapiens].
ACCESSION   NP_055558 XP_291106
VERSION     NP_055558.2
DBSOURCE    REFSEQ: accession NM_014743.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1395)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 1395)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   3  (residues 1 to 1395)
  AUTHORS   Shameer,K., Denny,J.C., Ding,K., Jouni,H., Crosslin,D.R., de
            Andrade,M., Chute,C.G., Peissig,P., Pacheco,J.A., Li,R.,
            Bastarache,L., Kho,A.N., Ritchie,M.D., Masys,D.R., Chisholm,R.L.,
            Larson,E.B., McCarty,C.A., Roden,D.M., Jarvik,G.P. and Kullo,I.J.
  TITLE     A genome- and phenome-wide association study to identify genetic
            variants influencing platelet count and volume and their
            pleiotropic effects
  JOURNAL   Hum Genet 133 (1), 95-109 (2014)
   PUBMED   24026423
REFERENCE   4  (residues 1 to 1395)
  AUTHORS   Gieger,C., Radhakrishnan,A., Cvejic,A., Tang,W., Porcu,E.,
            Pistis,G., Serbanovic-Canic,J., Elling,U., Goodall,A.H.,
            Labrune,Y., Lopez,L.M., Magi,R., Meacham,S., Okada,Y., Pirastu,N.,
            Sorice,R., Teumer,A., Voss,K., Zhang,W., Ramirez-Solis,R.,
            Bis,J.C., Ellinghaus,D., Gogele,M., Hottenga,J.J., Langenberg,C.,
            Kovacs,P., O'Reilly,P.F., Shin,S.Y., Esko,T., Hartiala,J.,
            Kanoni,S., Murgia,F., Parsa,A., Stephens,J., van der Harst,P.,
            Ellen van der Schoot,C., Allayee,H., Attwood,A., Balkau,B.,
            Bastardot,F., Basu,S., Baumeister,S.E., Biino,G., Bomba,L.,
            Bonnefond,A., Cambien,F., Chambers,J.C., Cucca,F., D'Adamo,P.,
            Davies,G., de Boer,R.A., de Geus,E.J., Doring,A., Elliott,P.,
            Erdmann,J., Evans,D.M., Falchi,M., Feng,W., Folsom,A.R.,
            Frazer,I.H., Gibson,Q.D., Glazer,N.L., Hammond,C.,
            Hartikainen,A.L., Heckbert,S.R., Hengstenberg,C., Hersch,M.,
            Illig,T., Loos,R.J., Jolley,J., Khaw,K.T., Kuhnel,B.,
            Kyrtsonis,M.C., Lagou,V., Lloyd-Jones,H., Lumley,T., Mangino,M.,
            Maschio,A., Mateo Leach,I., McKnight,B., Memari,Y., Mitchell,B.D.,
            Montgomery,G.W., Nakamura,Y., Nauck,M., Navis,G., Nothlings,U.,
            Nolte,I.M., Porteous,D.J., Pouta,A., Pramstaller,P.P., Pullat,J.,
            Ring,S.M., Rotter,J.I., Ruggiero,D., Ruokonen,A., Sala,C.,
            Samani,N.J., Sambrook,J., Schlessinger,D., Schreiber,S.,
            Schunkert,H., Scott,J., Smith,N.L., Snieder,H., Starr,J.M.,
            Stumvoll,M., Takahashi,A., Tang,W.H., Taylor,K., Tenesa,A., Lay
            Thein,S., Tonjes,A., Uda,M., Ulivi,S., van Veldhuisen,D.J.,
            Visscher,P.M., Volker,U., Wichmann,H.E., Wiggins,K.L.,
            Willemsen,G., Yang,T.P., Hua Zhao,J., Zitting,P., Bradley,J.R.,
            Dedoussis,G.V., Gasparini,P., Hazen,S.L., Metspalu,A., Pirastu,M.,
            Shuldiner,A.R., Joost van Pelt,L., Zwaginga,J.J., Boomsma,D.I.,
            Deary,I.J., Franke,A., Froguel,P., Ganesh,S.K., Jarvelin,M.R.,
            Martin,N.G., Meisinger,C., Psaty,B.M., Spector,T.D., Wareham,N.J.,
            Akkerman,J.W., Ciullo,M., Deloukas,P., Greinacher,A., Jupe,S.,
            Kamatani,N., Khadake,J., Kooner,J.S., Penninger,J., Prokopenko,I.,
            Stemple,D., Toniolo,D., Wernisch,L., Sanna,S., Hicks,A.A.,
            Rendon,A., Ferreira,M.A., Ouwehand,W.H. and Soranzo,N.
  TITLE     New gene functions in megakaryopoiesis and platelet formation
  JOURNAL   Nature 480 (7376), 201-208 (2011)
   PUBMED   22139419
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC106045.5.
            
            On Aug 3, 2007 this sequence version replaced NP_055558.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150286.1, D86985.3 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267753, SAMN03465406
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307659.6/ ENSP00000303928.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.1"
     Protein         1..1395
                     /product="uncharacterized protein KIAA0232"
                     /calculated_mol_wt=154658
     Region          27..1298
                     /region_name="DUF4603"
                     /note="Domain of unknown function (DUF4603); pfam15376"
                     /db_xref="CDD:464684"
     Region          146..166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92628.5)"
     Region          205..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92628.5)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92628.5)"
     Site            1080
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92628.5)"
     Region          1110..1132
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92628.5)"
     Site            1194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80U59; propagated from
                     UniProtKB/Swiss-Prot (Q92628.5)"
     Site            1338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92628.5)"
     Region          1346..1395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92628.5)"
     CDS             1..1395
                     /gene="KIAA0232"
                     /coded_by="NM_014743.3:469..4656"
                     /db_xref="CCDS:CCDS43209.1"
                     /db_xref="GeneID:9778"
                     /db_xref="HGNC:HGNC:28992"
                     /db_xref="MIM:619237"
ORIGIN      
        1 mypictvvvd glpsesssss ypgpvsvsem sllhalgpvq twlgqelekc gidamiytry
       61 vlslllhdsy dydlqeqend iflgwekgay kkwgkskkkc sdltleemkk qaavqclrsa
      121 sdessgietl veelcsrlkd lqskqeekih kklegspspe aelsppakdq vemyyeafpp
      181 lsekpvclqe imtvwnkskv csysssssss tappastdts spkdcnsese vtkerssevp
      241 ttvhektqsk sknekenkfs ngtieekpal ykkqirhkpe gkirprswss gsseagssss
      301 gnqgelkasm kyvkvrhkar eirnkkgrng qsrlslkhge kaernihtgs ssssssgsvk
      361 qlckrgkrpl keigrkdpgs tegkdlymen rkdteykeep lwytepiaey fvplsrkskl
      421 ettyrnrqdt sdltseavee lsesvhglci snnnlhktyl aagtfidghf vempavined
      481 idltgtslcs lpednkyldd ihlselthfy evdidqsmld pgasetmqge srilnmirqk
      541 skentdfeae ccivldgmel qgeraiwtds tssvgaeglf lqdlgnlaqf weccssssgd
      601 adgesfggds pvrlspilds tvlnshllag nqelfsdine gsginscfsv fevqcsnsvl
      661 pfsfetlnlg nentdssanm lgktqsrlli wtknsafeen ehcsnlstrt cspwshseet
      721 rsdnetlniq feestqfnae dinyvvprvs snyvdeelld flqdetcqqn srtlgeiptl
      781 vfkktskles vcgiqleqkt enknfettqv cnesphgdgy ssgvikdiwt kmadtnsvat
      841 veiertdael fsadvnnycc cldaeaelet lqepdkavrr seyhlwegqk eslekrafas
      901 selsnvdggd yttpskpwdv aqdkentfil ggvygelktf nsdgewavvp pshtkgsllq
      961 caasdvvtia gtdvfmtpgn sfapghrqlw kpfvsfeqnd qpksgengln kgfsfifhed
     1021 llgacgnfqv edpgleysfs sfdlsnpfsq vlhvecsfep egiasfspsf kpksilcsds
     1081 dsevfhpric gvdrtqyrai risprthfrp isaselspgg gsesefesek deanipipsq
     1141 vdifedpqad lkpleedaek eghyygksel esgkflprlk ksgmeksaqt sldsqeestg
     1201 ilsvgkqnqc lecsmnesle idlesseanc kimaqceeei nnfcgckagc qfpayednpv
     1261 ssgqleefpv lntdiqgmnr sqekqtwwek alysplfpas eceecytnak gesgleeypd
     1321 aketpsneer lldfnrvssv yearctgerd sgaksdgfrg kmcssassts eetgseggge
     1381 wvgpseeelf srthl
//
LOCUS       NP_766388               2176 aa            linear   ROD 27-APR-2025
DEFINITION  protein sidekick-2 precursor [Mus musculus].
ACCESSION   NP_766388
VERSION     NP_766388.2
DBSOURCE    REFSEQ: accession NM_172800.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 2176)
  AUTHORS   Rochon,P.L., Theriault,C., Rangel Olguin,A.G. and Krishnaswamy,A.
  TITLE     The cell adhesion molecule Sdk1 shapes assembly of a retinal
            circuit that detects localized edges
  JOURNAL   Elife 10, e70870 (2021)
   PUBMED   34545809
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2176)
  AUTHORS   Wang,Q., Ding,S.L., Li,Y., Royall,J., Feng,D., Lesnar,P.,
            Graddis,N., Naeemi,M., Facer,B., Ho,A., Dolbeare,T., Blanchard,B.,
            Dee,N., Wakeman,W., Hirokawa,K.E., Szafer,A., Sunkin,S.M., Oh,S.W.,
            Bernard,A., Phillips,J.W., Hawrylycz,M., Koch,C., Zeng,H.,
            Harris,J.A. and Ng,L.
  TITLE     The Allen Mouse Brain Common Coordinate Framework: A 3D Reference
            Atlas
  JOURNAL   Cell 181 (4), 936-953 (2020)
   PUBMED   32386544
REFERENCE   3  (residues 1 to 2176)
  AUTHORS   Yamagata,M. and Sanes,J.R.
  TITLE     Expression and Roles of the Immunoglobulin Superfamily Recognition
            Molecule Sidekick1 in Mouse Retina
  JOURNAL   Front Mol Neurosci 11, 485 (2019)
   PUBMED   30687002
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2176)
  AUTHORS   Tang,H., Chang,H., Dong,Y., Guo,L., Shi,X., Wu,Y., Huang,Y. and
            He,Y.
  TITLE     Architecture of cell-cell adhesion mediated by sidekicks
  JOURNAL   Proc Natl Acad Sci U S A 115 (37), 9246-9251 (2018)
   PUBMED   30150416
  REMARK    GeneRIF: The results suggest that the Ig-like domains and the
            fibronectin III (FnIII) domains of Sidekicks play different roles
            in cell adhesion. The Ig-like domains mediate the homophilic
            transinteractions bridging adjacent cells, while the FnIII domains
            interact with membranes, resulting in a tight adhesion interface
            between cells
REFERENCE   5  (residues 1 to 2176)
  AUTHORS   Yamagata,M. and Sanes,J.R.
  TITLE     Reporter-nanobody fusions (RANbodies) as versatile, small,
            sensitive immunohistochemical reagents
  JOURNAL   Proc Natl Acad Sci U S A 115 (9), 2126-2131 (2018)
   PUBMED   29440485
REFERENCE   6  (residues 1 to 2176)
  AUTHORS   Trimarchi,J.M., Cho,S.H. and Cepko,C.L.
  TITLE     Identification of genes expressed preferentially in the developing
            peripheral margin of the optic cup
  JOURNAL   Dev Dyn 238 (9), 2327-2329 (2009)
   PUBMED   19449303
REFERENCE   7  (residues 1 to 2176)
  AUTHORS   Yoshida,Y., Han,B., Mendelsohn,M. and Jessell,T.M.
  TITLE     PlexinA1 signaling directs the segregation of proprioceptive
            sensory axons in the developing spinal cord
  JOURNAL   Neuron 52 (5), 775-788 (2006)
   PUBMED   17145500
REFERENCE   8  (residues 1 to 2176)
  AUTHORS   Hayashi,K., Kaufman,L., Ross,M.D. and Klotman,P.E.
  TITLE     Definition of the critical domains required for homophilic
            targeting of mouse sidekick molecules
  JOURNAL   FASEB J 19 (6), 614-616 (2005)
   PUBMED   15703275
  REMARK    GeneRIF: results establish that the first and second immunoglobulin
            domains of sidekick-1 and -2 are necessary and sufficient to
            mediate and target homophilic adhesion
REFERENCE   9  (residues 1 to 2176)
  AUTHORS   Kaufman,L., Hayashi,K., Ross,M.J., Ross,M.D. and Klotman,P.E.
  TITLE     Sidekick-1 is upregulated in glomeruli in HIV-associated
            nephropathy
  JOURNAL   J Am Soc Nephrol 15 (7), 1721-1730 (2004)
   PUBMED   15213259
REFERENCE   10 (residues 1 to 2176)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL627323.6, AL663117.14 and AL603706.13.
            
            On Dec 20, 2003 this sequence version replaced NP_766388.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY351699.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2176
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 79.3 cM"
     Protein         1..2176
                     /product="protein sidekick-2 precursor"
                     /note="protein sidekick-2; sidekick 2; sidekick homolog 2"
                     /calculated_mol_wt=237126
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2795
     mat_peptide     25..2176
                     /product="Protein sidekick-2. /id=PRO_0000226979"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6V4S5.1)"
                     /calculated_mol_wt=237126
     Region          29..99
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          126..201
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          134..138
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          148..152
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          170..174
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          184..189
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          197..200
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Region          226..290
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          312..401
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          330..334
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          343..347
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          367..371
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          381..386
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          394..397
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          408..496
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          423..427
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409544"
     Region          436..440
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409544"
     Region          462..466
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409544"
     Region          476..481
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409544"
     Region          489..492
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409544"
     Region          502..590
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          517..521
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409544"
     Region          530..536
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409544"
     Region          556..560
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409544"
     Region          570..575
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409544"
     Region          583..586
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409544"
     Region          594..685
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(594,661,676)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(677..678,680..681)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          737..1220
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            747
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Site            940
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Site            952
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Region          1103..1198
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            1106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Site            order(1187..1188,1190..1191)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1207..1292
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          <1276..>1526
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            order(1288..1289,1291..1292)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1507..1620
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            1592
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Site            order(1611..1612,1614..1615)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1630..1723
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Region          <1698..>1929
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          1712..1734
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Site            order(1712..1713,1715..1716)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            1937..1957
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Region          2013..2032
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Region          2043..2070
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Region          2102..2176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6V4S5.1)"
     Region          2170..2176
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000269|PubMed:20219992"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6V4S5.1)"
     CDS             1..2176
                     /gene="Sdk2"
                     /gene_synonym="4632412F08Rik; 5330435L01Rik; mKIAA1514;
                     Sdk-2"
                     /coded_by="NM_172800.3:1152..7682"
                     /db_xref="CCDS:CCDS25605.1"
                     /db_xref="GeneID:237979"
                     /db_xref="MGI:MGI:2443847"
ORIGIN      
        1 mfssmwrlpl wtllalhrih sagaqddvpp yfktepvrtq vhlegnrlvl tcmaegswpl
       61 efkwlhnnre ltrfsleyry mitsldrtha gfyrcivrnr mgallqrqte vqvaymgsfe
      121 egekrqsvnh geaavirapr issfprpqvt wfrdgrkipp ssriaitlen tlvilstvap
      181 dagryyvqav ndkngdnkts qpitlavenv ggpadpiapt iiippkntsv vagtsevtme
      241 cvanarplik lhivwkkdga plssgisdyn rrltianptv sdagyyecea mlrsssvapv
      301 trgaylsvle ppqfvreper hitaemekvv dipcrakgvp ppsitwykda alvevgkltr
      361 fkqrsdgglq isgllpddtg mlqcfahnaa geaqtstyla vtsiapnitr gpldstvidg
      421 msvvlacets gaprpaitwq kgerilasgs vqlprftlle sgsllispth isdagtytcl
      481 atnsrgvdea sadlvvwart ritkppqdqs vikgtqasmv cgvthdprvt vryvwekdga
      541 tlavetnpri rldrngslhi sqtwsgdigt ytcrvlsagg ndsrnahlrv rqlphapehp
      601 vatlstverr ainltwakpf dgnsplmryv lemsennapw tillasvdpe atsvmvkglv
      661 parsyqfrlc avndvgkgqf skdtervslp eepptappqn viasgrtnqs imiqwqpppe
      721 shqngilkgy iiryclaglp vgyqfknitd advnnllled liiwtnyeie vaaynsaglg
      781 vysskvtewt lqgvptvppg nvhaeatnst tirftwnaps pqfinginqg ykliawepaq
      841 eeevtmvtar pnfqdsihvg fvsglkkfte yftsvlcftt pgdgprsspq lvrthedvpg
      901 pvghlsfndi ldtslkvswq epgekngilt gyrisweeyn rtntrvthyl pnvtleyrvt
      961 gltalttyti evaamtskgq gqvsastiss gvppelpgap tnlgisnigp rsvtlqfrpg
     1021 ydgktsisrw vveaqvgvig egeewlliyq lgnepdarsm evpdlnpfty ysfrmrqvni
     1081 vgtsppsqps rkiqtlqapp diapanvtlr tasetslwlr wmplpemeyn gnpesvgyki
     1141 kygrsdghgk tlshtvqdrv ereytiedle ewteyrvqvq afnaigsgpw sqavvgrtre
     1201 svpssgptnv salattsssm lvrwseipea drnglvlgyk vrykekdsds qprfwlvegn
     1261 ssrsaqltgl gkyvlyevqv laftrigdgs pshppilert lddvpgppmg ilfpevrtts
     1321 vrliwqppaa pngiilayqi thrlnattan tatvevlaps arqymatglk pesvylfrit
     1381 aqtrkgwgea aealvvttek rdrpqppskp vvqqedvkar svllswepgs dglspvryyt
     1441 iqtrelpsgr walhsasvsh nasaftvdrl kpftsykfrv katndigdse fseesesltt
     1501 lqaapdeapt ilsvtphttt svlirwqpps edkingillg friryrelly dglrgftlrg
     1561 innpgakwae ltslysmrnl trpsltqyel dnlskhrrye irmsiynavg egplsppqev
     1621 fvgeavptaa pqnvaihsat atqldvtwep ppldnqngdi qgykiyfwev qrrnltervk
     1681 tlflaensvk lknltgytay mvsvaafnaa gdgprstptr gqtqqaapsa pgsvkfselt
     1741 ttsvnvswda pqfpngpleg yrlvyepctp vdgvskivtv dvkgnsplwl kvkdlaegmt
     1801 yrfrikaktf tygpeieani ttgpgegapg ppgvpiivry ssaiaihwss gdpgkgpitr
     1861 yviearpsde glwdilikdi pkevtsytfs mdilkpgvsy dfrviavndy gfgtpsspsq
     1921 svpaqkaspf yeewwflvvi alvglifill lvfvliirgq skkyskktds ggntksgalg
     1981 hgemlsldes sfpalelnnr rlsvknsfcr knglytrspp rpspgslhys dedvtkyndl
     2041 ipaessslte kpseisdsqg sdseyevdtn tqkahsfvnh yisdptyyns wrrqqkgisr
     2101 aqaysytesd sgepdhvtvp nsnstqqgsl frpkasrtpt pqnppnpqsq qstlyrppss
     2161 lapgsrapia gfssfv
//
LOCUS       NP_001173                539 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-aminoadipic semialdehyde dehydrogenase isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001173 XP_943057
VERSION     NP_001173.2
DBSOURCE    REFSEQ: accession NM_001182.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Korasick,D.A., Buckley,D.P., Palpacelli,A., Cursio,I., Cesaroni,E.,
            Cheng,J. and Tanner,J.J.
  TITLE     Biochemical, structural, and computational analyses of two new
            clinically identified missense mutations of ALDH7A1
  JOURNAL   Chem Biol Interact 394, 110993 (2024)
   PUBMED   38604394
  REMARK    GeneRIF: Biochemical, structural, and computational analyses of two
            new clinically identified missense mutations of ALDH7A1.
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Lu,H.J., Chuang,C.Y., Chen,M.K., Su,C.W., Yang,W.E., Yeh,C.M.,
            Lai,K.M., Tang,C.H., Lin,C.W. and Yang,S.F.
  TITLE     The impact of ALDH7A1 variants in oral cancer development and
            prognosis
  JOURNAL   Aging (Albany NY) 14 (10), 4556-4571 (2022)
   PUBMED   35613852
  REMARK    GeneRIF: The impact of ALDH7A1 variants in oral cancer development
            and prognosis.
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Tan,M., Meng,J., Sun,X., Fu,X. and Wang,R.
  TITLE     EPS8 supports pancreatic cancer growth by inhibiting BMI1 mediated
            proteasomal degradation of ALDH7A1
  JOURNAL   Exp Cell Res 407 (1), 112782 (2021)
   PUBMED   34391775
  REMARK    GeneRIF: EPS8 supports pancreatic cancer growth by inhibiting BMI1
            mediated proteasomal degradation of ALDH7A1.
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Brocker,C., Lassen,N., Estey,T., Pappa,A., Cantore,M., Orlova,V.V.,
            Chavakis,T., Kavanagh,K.L., Oppermann,U. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in
            cellular defense against hyperosmotic stress
  JOURNAL   J Biol Chem 285 (24), 18452-18463 (2010)
   PUBMED   20207735
  REMARK    GeneRIF: ALDH7A1 is a novel aldehyde dehydrogenase expressed in
            multiple subcellular compartments that protects against
            hyperosmotic stress by generating osmolytes and metabolizing toxic
            aldehydes
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Wong,J.W., Chan,C.L., Tang,W.K., Cheng,C.H. and Fong,W.P.
  TITLE     Is antiquitin a mitochondrial Enzyme?
  JOURNAL   J Cell Biochem 109 (1), 74-81 (2010)
   PUBMED   19885858
  REMARK    GeneRIF: antiquitin was present not only in the cytosol but also in
            the mitochondria.
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Cormier-Daire,V., Dagoneau,N., Nabbout,R., Burglen,L., Penet,C.,
            Soufflet,C., Desguerre,I., Munnich,A. and Dulac,O.
  TITLE     A gene for pyridoxine-dependent epilepsy maps to chromosome 5q31
  JOURNAL   Am J Hum Genet 67 (4), 991-993 (2000)
   PUBMED   10978228
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Skvorak,A.B., Robertson,N.G., Yin,Y., Weremowicz,S., Her,H.,
            Bieber,F.R., Beisel,K.W., Lynch,E.D., Beier,D.R. and Morton,C.C.
  TITLE     An ancient conserved gene expressed in the human inner ear:
            identification, expression analysis, and chromosomal mapping of
            human and mouse antiquitin (ATQ1)
  JOURNAL   Genomics 46 (2), 191-199 (1997)
   PUBMED   9417906
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Lee,P., Kuhl,W., Gelbart,T., Kamimura,T., West,C. and Beutler,E.
  TITLE     Homology between a human protein and a protein of the green garden
            pea
  JOURNAL   Genomics 21 (2), 371-378 (1994)
   PUBMED   8088832
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Gospe,S.M. Jr.
  TITLE     Pyridoxine-Dependent Epilepsy - ALDH7A1
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301659
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099513.3 and AC093535.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 14, 2008 this sequence version replaced NP_001173.1.
            
            Summary: The protein encoded by this gene is a member of subfamily
            7 in the aldehyde dehydrogenase gene family. These enzymes are
            thought to play a major role in the detoxification of aldehydes
            generated by alcohol metabolism and lipid peroxidation. This
            particular member has homology to a previously described protein
            from the green garden pea, the 26g pea turgor protein. It is also
            involved in lysine catabolism that is known to occur in the
            mitochondrial matrix. Recent reports show that this protein is
            found both in the cytosol and the mitochondria, and the two forms
            likely arise from the use of alternative translation initiation
            sites. An additional variant encoding a different isoform has also
            been found for this gene. Mutations in this gene are associated
            with pyridoxine-dependent epilepsy. Several related pseudogenes
            have also been identified. [provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) encodes two isoforms resulting
            from the use of alternative in-frame translation initiation codons.
            The longer isoform (1) is derived from an upstream AUG (at nt
            193-195), while the shorter isoform (2) is derived from a
            downstream AUG (at nt 277-279). This RefSeq represents the longer
            isoform, which resides in the mitochondria (PMIDs: 20207735 and
            19885858).
            
            Sequence Note: This Refseq, containing three potential in-frame
            translation initiation codons (all with weak Kozak signals), is
            annotated with a CDS starting from a downstream start codon (at nt
            193-195) based on better conservation, N-terminal consistency with
            homologous proteins, and the presence of a transit peptide, which
            is essential for the localization of this isoform in the
            mitochondria (PMIDs: 20207735 and 19885858), and is consistent with
            the function of this gene in lysine catabolism (which is known to
            occur in the mitochondria). The use of an upstream start codon (at
            nt 112-114) that is present in only a subset of higher mammals,
            would increase the protein length by 27 aa. A shorter, soluble
            isoform resulting from the use of another downstream start codon
            (at nt 277-279) is represented in a separate RefSeq
            (NM_001201377.1). This RefSeq record was created from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.67118.1,
                                           SRR1660809.42696.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000409134.8/
                                                  ENSP00000387123.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.2"
     Protein         1..539
                     /product="alpha-aminoadipic semialdehyde dehydrogenase
                     isoform 1 precursor"
                     /EC_number="1.2.1.3"
                     /EC_number="1.2.1.8"
                     /EC_number="1.2.1.31"
                     /note="26g turgor protein homolog; alpha-aminoadipic
                     semialdehyde dehydrogenase; alpha-AASA dehydrogenase; P6c
                     dehydrogenase; antiquitin-1; betaine aldehyde
                     dehydrogenase; delta1-piperideine-6-carboxylate
                     dehydrogenase; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=55585
     transit_peptide 1..26
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P49419.5)"
                     /calculated_mol_wt=2921
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P49419.5)"
     mat_peptide     27..539
                     /product="Alpha-aminoadipic semialdehyde dehydrogenase.
                     /id=PRO_0000056490"
                     /note="propagated from UniProtKB/Swiss-Prot (P49419.5)"
                     /calculated_mol_wt=55585
     Region          53..527
                     /region_name="ALDH_F7_AASADH"
                     /note="NAD+-dependent alpha-aminoadipic semialdehyde
                     dehydrogenase, ALDH family members 7A1 and 7B; cd07130"
                     /db_xref="CDD:143448"
     Site            94
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBF1; propagated from
                     UniProtKB/Swiss-Prot (P49419.5)"
     Site            order(100,106,109,115,122,161..162,164,166,168,170..173,
                     180..181,183,280,283..284,287,292..293,320,356,368,442,
                     465,471..472,476,479,481..484,490..491,495,499,506,
                     510..511,514,518..523,525..526)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143448"
     Site            order(192..195,218,220..221,258..259,272..275,278,281,
                     296..298,330,427,496)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143448"
     Site            order(195,296,327,330)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143448"
     Site            195
                     /site_type="other"
                     /note="Transition state stabilizer. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P49419.5)"
     Site            462
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBF1; propagated from
                     UniProtKB/Swiss-Prot (P49419.5)"
     Site            500
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBF1; propagated from
                     UniProtKB/Swiss-Prot (P49419.5)"
     CDS             1..539
                     /gene="ALDH7A1"
                     /gene_synonym="ATQ1; EPD; EPEO4; PDE"
                     /coded_by="NM_001182.5:22..1641"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4137.2"
                     /db_xref="GeneID:501"
                     /db_xref="HGNC:HGNC:877"
                     /db_xref="MIM:107323"
ORIGIN      
        1 mwrlpralcv haaktsklsg pwsrpaafms tllinqpqya wlkelglree negvyngswg
       61 grgevittyc pannepiarv rqasvadyee tvkkareawk iwadipapkr geivrqigda
      121 lrekiqvlgs lvslemgkil vegvgevqey vdicdyavgl srmiggpilp sersghalie
      181 qwnpvglvgi itafnfpvav ygwnnaiami cgnvclwkga pttslisvav tkiiakvled
      241 nklpgaicsl tcggadigta makdervnll sftgstqvgk qvglmvqerf grsllelggn
      301 naiiafedad lslvvpsalf aavgtagqrc ttarrlfihe sihdevvnrl kkayaqirvg
      361 npwdpnvlyg plhtkqavsm flgaveeakk eggtvvyggk vmdrpgnyve ptivtglghd
      421 asiahtetfa pilyvfkfkn eeevfawnne vkqglsssif tkdlgrifrw lgpkgsdcgi
      481 vnvniptsga eiggafggek htgggresgs dawkqymrrs tctinyskdl plaqgikfq
//
LOCUS       NP_001186014            1035 aa            linear   PRI 27-APR-2025
DEFINITION  tudor domain-containing protein 5 isoform 1 [Homo sapiens].
ACCESSION   NP_001186014
VERSION     NP_001186014.1
DBSOURCE    REFSEQ: accession NM_001199085.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Babakhanzadeh,E., Khodadadian,A., Rostami,S., Alipourfard,I.,
            Aghaei,M., Nazari,M., Hosseinnia,M., Mehrjardi,M.Y.V., Jamshidi,Y.
            and Ghasemi,N.
  TITLE     Testicular expression of TDRD1, TDRD5, TDRD9 and TDRD12 in
            azoospermia
  JOURNAL   BMC Med Genet 21 (1), 33 (2020)
   PUBMED   32059713
  REMARK    GeneRIF: Here we evaluate gene and protein expression levels of
            four key TDRDs (TDRD1, TDRD5, TDRD9 and TDRD12) in testicular
            biopsy samples obtained from men with obstructive azoospermia (OA,
            n = 29), as controls, and various types of non-obstructive
            azoospermia containing hypospermatogenesis (HP, 28), maturation
            arrest (MA, n = 30), and Sertoli cell-only syndrome (SCOS, n = 32)
            as cases.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Sun,Y.H., Jiang,F. and Li,X.Z.
  TITLE     Disruption of Tdrd5 decouples the stepwise processing of long
            precursor transcripts during pachytene PIWI-interacting RNA
            biogenesis
  JOURNAL   Biol Reprod 99 (4), 684-685 (2018)
   PUBMED   29733347
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Yabuta,Y., Ohta,H., Abe,T., Kurimoto,K., Chuma,S. and Saitou,M.
  TITLE     TDRD5 is required for retrotransposon silencing, chromatoid body
            assembly, and spermiogenesis in mice
  JOURNAL   J Cell Biol 192 (5), 781-795 (2011)
   PUBMED   21383078
REFERENCE   4  (residues 1 to 1035)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA418635.1, AK127370.1, BC089387.1 and BC144058.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1). Variants 1 and 2
            both encode the same isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144058.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000444136.6/ ENSP00000406052.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1035
                     /product="tudor domain-containing protein 5 isoform 1"
                     /note="tudor domain-containing protein 5; testicular
                     tissue protein Li 194"
                     /calculated_mol_wt=115912
     Region          4..98
                     /region_name="LOTUS_1_TDRD5"
                     /note="The first LOTUS domain on Tudor-containing protein
                     5 (TDRD5); cd09985"
                     /db_xref="CDD:193599"
     Region          132..201
                     /region_name="LOTUS_2_TDRD5"
                     /note="The second LOTUS domain on Tudor-containing protein
                     5 (TDRD5); cd09975"
                     /db_xref="CDD:193589"
     Region          296..369
                     /region_name="LOTUS_3_TDRD5"
                     /note="The third LOTUS domain on Tudor-containing protein
                     5 (TDRD5); cd09976"
                     /db_xref="CDD:193590"
     Region          476..593
                     /region_name="Tudor_TDRD5"
                     /note="Tudor domain found in Tudor domain-containing
                     protein 5 (TDRD5) and similar proteins; cd20419"
                     /db_xref="CDD:410490"
     Site            order(536,543,560,563,565)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410490"
     CDS             1..1035
                     /gene="TDRD5"
                     /gene_synonym="TUDOR3"
                     /coded_by="NM_001199085.3:309..3416"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS55663.1"
                     /db_xref="GeneID:163589"
                     /db_xref="HGNC:HGNC:20614"
                     /db_xref="MIM:617748"
ORIGIN      
        1 mseqeriqec lrkeirslli stkdglspqe lekeyllmvg nhlplrilgy rstmelvldm
       61 pdvvrvcpga ggtvilkaip destkgiasl vakqrsshkl rnsmhkgrps iysgprshrr
      121 vpyrgrvapi lpavvkselk dllalspvll sdfekafakr fgrsfqymqy gflsmfevln
      181 aasdvisveq tragsllmlk ksvteekprg cpagkiftqp frmkqgsyst gfpvakpcfs
      241 qptsnmeppk qimsmektsk lnvvetsrln hteklnqlen tfksviaqig pggtisselk
      301 hkikfvvskf peglfiskll geyevifkeq lspkklgfln vtelvgalsd ilhvefrkgh
      361 qdllvfdadk kplppvqsdk kieakacvss pprnslstaa vketvwncps kkqkepqqki
      421 ckkpnlvvkp lqlqvetnks elnlamanhd ippdavpnkk lcrlppldts sligvfveyi
      481 ispsqfyiri ysrdsselle dmmiemrrcy snqlvsdryv mpecfiqpgh lccvrisedk
      541 wwyrviihrv lekqevevfy pdfgnigivq ksslrflkcc ytklpaqaip cslawvrpve
      601 ehwtskailq fqklcglkpl vgvvdeyvdg ilniflcdts snedvyfhhv lrteghaivc
      661 renisskgfs elnplalytt ssggpedivl telgypsqqh yfnedrkisp qskeselril
      721 qdindeksls hlkseskepl kdsefeslkt cnksfeedpk wsnpepndlk eenedeiptg
      781 mpclesvtig ddiwdenwlp lqakmgkggd aashlftasl ggknqyssck empqkdwcfs
      841 tpkdtwddsw qpsglvngtk vevhkpevlg aqekntgtnr tqkqldings sdsstlpkle
      901 efctsltqse qsadgsqsep nnsqtqpkqi qlstaapcst tavddsaekp sgsvesspei
      961 lknedfsssr aitlykdkrq esvdqlslil syecqisqkl yiprstataa lgaaarlats
     1021 rsllhwypsv krmea
//
LOCUS       NP_001159983            1669 aa            linear   MAM 27-APR-2025
DEFINITION  collagen alpha-1(IV) chain precursor [Bos taurus].
ACCESSION   NP_001159983 XP_580317
VERSION     NP_001159983.2
DBSOURCE    REFSEQ: accession NM_001166511.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 1669)
  AUTHORS   Yamane,T., Mitsumata,M., Yamaguchi,N., Nakazawa,T., Mochizuki,K.,
            Kondo,T., Kawasaki,T., Murata,S., Yoshida,Y. and Katoh,R.
  TITLE     Laminar high shear stress up-regulates type IV collagen synthesis
            and down-regulates MMP-2 secretion in endothelium. A quantitative
            analysis
  JOURNAL   Cell Tissue Res 340 (3), 471-479 (2010)
   PUBMED   20490867
  REMARK    GeneRIF: High shear stress up-regulates type IV collagen synthesis
            and down-regulates MMP-2 secretion in endothelial cells.
REFERENCE   2  (residues 1 to 1669)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   3  (residues 1 to 1669)
  AUTHORS   Vanacore,R.M., Shanmugasundararaj,S., Friedman,D.B., Bondar,O.,
            Hudson,B.G. and Sundaramoorthy,M.
  TITLE     The alpha1.alpha2 network of collagen IV. Reinforced stabilization
            of the noncollagenous domain-1 by noncovalent forces and the
            absence of Met-Lys cross-links
  JOURNAL   J Biol Chem 279 (43), 44723-44730 (2004)
   PUBMED   15299013
  REMARK    GeneRIF: alpha1.alpha2 stabilize the noncollagenous domain-1 by
            noncovalent forces and the absence of Met-Lys cross-links
REFERENCE   4  (residues 1 to 1669)
  AUTHORS   Sundaramoorthy,M., Meiyappan,M., Todd,P. and Hudson,B.G.
  TITLE     Crystal structure of NC1 domains. Structural basis for type IV
            collagen assembly in basement membranes
  JOURNAL   J Biol Chem 277 (34), 31142-31153 (2002)
   PUBMED   11970952
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            NKLS02000012.1.
            
            On Jun 30, 2017 this sequence version replaced NP_001159983.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5571261.5929.1, SRR5765710.6779.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA6648753,
                                           SAMEA6648754 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1669
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="12"
                     /map="12"
                     /breed="Hereford"
     Protein         1..1669
                     /product="collagen alpha-1(IV) chain precursor"
                     /note="collagen alpha-1(IV) chain; collagen, type IV,
                     alpha 1"
                     /calculated_mol_wt=157529
     sig_peptide     1..27
                     /note="/evidence=ECO:0000250|UniProtKB:P02462; propagated
                     from UniProtKB/Swiss-Prot (Q7SIB2.2)"
                     /calculated_mol_wt=2902
     mat_peptide     28..1669
                     /product="Collagen alpha-1(IV) chain. /id=PRO_0000059399"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7SIB2.2)"
                     /calculated_mol_wt=157529
     Region          <46..>331
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          50..1445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Region          173..1440
                     /region_name="Triple-helical region.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            204
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:24368846; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            207
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:24368846; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            210
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:24368846; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Region          <271..>577
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <495..>766
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            587
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:24368846; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            602
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:24368846; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            603
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            605
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:24368846; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            606
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            623
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            626
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            629
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            632
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Site            647
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:24368846; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Region          <777..>1011
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <948..>1163
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1079..>1326
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            1214
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:24368846; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Region          <1262..>1443
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            1424
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:24368846; propagated from
                     UniProtKB/Swiss-Prot (Q7SIB2.2)"
     Region          1446..1553
                     /region_name="C4"
                     /note="C-terminal tandem repeated domain in type 4
                     procollagen; pfam01413"
                     /db_xref="CDD:460201"
     Region          1556..1667
                     /region_name="C4"
                     /note="C-terminal tandem repeated domain in type 4
                     procollagen; pfam01413"
                     /db_xref="CDD:460201"
     CDS             1..1669
                     /gene="COL4A1"
                     /coded_by="NM_001166511.3:17..5026"
                     /db_xref="BGD:BT11988"
                     /db_xref="GeneID:282191"
                     /db_xref="VGNC:VGNC:50081"
ORIGIN      
        1 mgprlgvwll lllaalllhe essraaakgg cagsgcgkcd chgvkgqkge rglpglqgvi
       61 gfpgmqgpeg pqgppgqkgd tgepglpgtk gtrgpsgvpg ypgnpglpgi pgqdgppgpp
      121 gipgcngtkg ergpvgppgl pgfagnpgpp glpgmkgdpg eilghipgtl lkgergypgq
      181 pgapgspglp glqgpvgppg ftgppgppgp pgppgekgqm glsfqgpkge kgdqgvsgpp
      241 glpgqaqvit kgdtamrgek gqkgepgfpg lpgfgekgep gkpgprgkpg kdgekgekgs
      301 pgfpgdsgyp gqpgqdglkg ekgeagppgl pgtvigtgpl gekgepgypg gpgakgetgp
      361 kgfpgipgqp gppgfptpgl igapgfpgdr gekgepglpg vslpgpsgrd glpgppgppg
      421 ppgqpghtng ivecqpgppg dqgppgipgq pgltgevgek gqkgdsclvc dtaelrgppg
      481 pqgppgeigf pgqpgakgdr glpgrdgleg lpgpqgapgl mgqpgakgep geiyfdirlk
      541 gdkgdpgfpg qpgmpgrags pgrdgqpglp gprgspgsvg lkgergppgg vgfpgsrgdi
      601 gppgppgfgp igpigdkgqi gfpgtpgapg qpgpkgeagk vvplpgppga eglpgspgfq
      661 gpqgdrgfpg spgrpglpge kgaigqpgig fpgppgpkgv dglpgdagpp gnpgrqgfng
      721 lpgnpgppgq kgepgvglpg lkglpgipgi pgtpgekgnv ggpgipgehg aigppglqgl
      781 rgdpgppgfq gpkgapgvpg igppgamgpp ggqgppgssg ppgvkgekgf pgfpgldmpg
      841 pkgdkgsqgl pgltgqsglp glpgqqgtpg qpgipgpkge mgvmgtpgqp gspgpagvpg
      901 lpgakgdhgf pgssgprgdp gfkgdkgdvg lpgkpgsmdk vdmgsmkgek gdqgekgqtg
      961 ptgdkgsrgd pgtpgvpgkd gqaghpgqpg pkgdpgvsgi pgapglpgpk gsaggmglpg
     1021 mpgpkgvagi pgpqgipglp gdkgakgekg qaglpgigip grpgdkgdqg lagfpgspge
     1081 kgekgstgip gmpgspgpkg spgsvgypgs pglpgekgdk glpgldgipg ikgeaglpgk
     1141 pgptgpagqk gepgsdgipg svgekgesgl pgrgfpgfpg skgdkgskgd vgfpglsgsp
     1201 gipgskgeqg fmgppgpqgq pglpgtpgha vegpkgdrgp qgqpglpgrp gpmgppglpg
     1261 leglkgergn pgwpgtpgap gpkgdpgfqg mpgiggspgi tgakgdvgpp gvpgfhgqkg
     1321 apglqgvkgd qgdqgfpgtk glpgppgppg pfsiikgepg lpgpegpagl kglqgppgpk
     1381 gqqgvtgsvg lpgppgepgf dgapgqkget gpfgppgprg fpgppgpdgl pgsmgppgtp
     1441 svdhgflvtr hsqttddpqc ppgtkilyhg ysllyvqgne rahgqdlgta gsclrkfstm
     1501 pflfcninnv cnfasrndys ywlstpepmp msmapitgen irpfisrcav ceapamvmav
     1561 hsqtiqipqc ptgwsslwig ysfvmhtsag aegsgqalas pgscleefrs apfiechgrg
     1621 tcnyyanays fwlatierse mfkkptpstl kagelrthvs rcqvcmrrt
//
LOCUS       NP_060372                349 aa            linear   PRI 27-APR-2025
DEFINITION  hypoxia-inducible factor 1-alpha inhibitor [Homo sapiens].
ACCESSION   NP_060372 NP_115591
VERSION     NP_060372.2
DBSOURCE    REFSEQ: accession NM_017902.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Liu,B., Rui,Y., Li,M. and Huang,L.
  TITLE     Cancer cell-derived exosomes promote NSCLC progression via the
            miR-199b-5p/HIF1AN axis
  JOURNAL   Mol Immunol 174, 32-40 (2024)
   PUBMED   39154583
  REMARK    GeneRIF: Cancer cell-derived exosomes promote NSCLC progression via
            the miR-199b-5p/HIF1AN axis.
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Li,N., Zhou,Q., Yi,Z., Zhang,H. and Zhou,D.
  TITLE     Ubiquitin protein E3 ligase ASB9 suppresses proliferation and
            promotes apoptosis in human spermatogonial stem cell line by
            inducing HIF1AN degradation
  JOURNAL   Biol Res 56 (1), 4 (2023)
   PUBMED   36683111
  REMARK    GeneRIF: Ubiquitin protein E3 ligase ASB9 suppresses proliferation
            and promotes apoptosis in human spermatogonial stem cell line by
            inducing HIF1AN degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Volkova,Y.L., Pickel,C., Jucht,A.E., Wenger,R.H. and Scholz,C.C.
  TITLE     The Asparagine Hydroxylase FIH: A Unique Oxygen Sensor
  JOURNAL   Antioxid Redox Signal 37 (13-15), 913-935 (2022)
   PUBMED   35166119
  REMARK    GeneRIF: The Asparagine Hydroxylase FIH: A Unique Oxygen Sensor.
            Review article
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Leissing,T.M., Hardy,A.P., Chan,H., Wang,Y., Tumber,A.,
            Chowdhury,R., Feng,T., Coleman,M.L., Cockman,M.E., Kramer,H.B.,
            Berridge,G., Fischer,R., Kessler,B.M., Ratcliffe,P.J., Lu,X. and
            Schofield,C.J.
  TITLE     Factor inhibiting HIF can catalyze two asparaginyl hydroxylations
            in VNVN motifs of ankyrin fold proteins
  JOURNAL   J Biol Chem 298 (6), 102020 (2022)
   PUBMED   35537551
  REMARK    GeneRIF: Factor inhibiting HIF can catalyze two asparaginyl
            hydroxylations in VNVN motifs of ankyrin fold proteins.
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Shi,Z., Li,G., Li,Z., Liu,J. and Tang,Y.
  TITLE     TMEM161B-AS1 suppresses proliferation, invasion and glycolysis by
            targeting miR-23a-3p/HIF1AN signal axis in oesophageal squamous
            cell carcinoma
  JOURNAL   J Cell Mol Med 25 (14), 6535-6549 (2021)
   PUBMED   34046994
  REMARK    GeneRIF: TMEM161B-AS1 suppresses proliferation, invasion and
            glycolysis by targeting miR-23a-3p/HIF1AN signal axis in
            oesophageal squamous cell carcinoma.
            Erratum:[J Cell Mol Med. 2023 Feb;27(4):591-592. doi:
            10.1111/jcmm.17661. PMID: 36790069]
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Hewitson,K.S., McNeill,L.A., Riordan,M.V., Tian,Y.M., Bullock,A.N.,
            Welford,R.W., Elkins,J.M., Oldham,N.J., Bhattacharya,S.,
            Gleadle,J.M., Ratcliffe,P.J., Pugh,C.W. and Schofield,C.J.
  TITLE     Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical
            to factor inhibiting HIF (FIH) and is related to the cupin
            structural family
  JOURNAL   J Biol Chem 277 (29), 26351-26355 (2002)
   PUBMED   12042299
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Lando,D., Peet,D.J., Gorman,J.J., Whelan,D.A., Whitelaw,M.L. and
            Bruick,R.K.
  TITLE     FIH-1 is an asparaginyl hydroxylase enzyme that regulates the
            transcriptional activity of hypoxia-inducible factor
  JOURNAL   Genes Dev 16 (12), 1466-1471 (2002)
   PUBMED   12080085
  REMARK    GeneRIF: FIH-1 is an asparaginyl hydroxylase enzyme that regulates
            the transcriptional activity of hypoxia-inducible factor
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Freedman,S.J., Sun,Z.Y., Poy,F., Kung,A.L., Livingston,D.M.,
            Wagner,G. and Eck,M.J.
  TITLE     Structural basis for recruitment of CBP/p300 by hypoxia-inducible
            factor-1 alpha
  JOURNAL   Proc Natl Acad Sci U S A 99 (8), 5367-5372 (2002)
   PUBMED   11959990
  REMARK    GeneRIF: Structural basis for recruitment of CBP/p300 by
            hypoxia-inducible factor-1 alpha
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Lando,D., Peet,D.J., Whelan,D.A., Gorman,J.J. and Whitelaw,M.L.
  TITLE     Asparagine hydroxylation of the HIF transactivation domain a
            hypoxic switch
  JOURNAL   Science 295 (5556), 858-861 (2002)
   PUBMED   11823643
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Mahon,P.C., Hirota,K. and Semenza,G.L.
  TITLE     FIH-1: a novel protein that interacts with HIF-1alpha and VHL to
            mediate repression of HIF-1 transcriptional activity
  JOURNAL   Genes Dev 15 (20), 2675-2686 (2001)
   PUBMED   11641274
  REMARK    GeneRIF: Gene name = FIH1Encoded protein (factor inhibiting HIF-1)
            is a co-repressor that interacts with hypoxia-inducible factor 1
            (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to
            mediate repression of HIF-1 transcriptional activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL133352.12, AF395830.1 and AW015561.1.
            
            On Jun 5, 2007 this sequence version replaced NP_060372.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.170885.1,
                                           SRR1660805.138351.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299163.7/ ENSP00000299163.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..349
                     /product="hypoxia-inducible factor 1-alpha inhibitor"
                     /EC_number="1.14.11.30"
                     /EC_number="1.14.11.n4"
                     /note="factor inhibiting HIF1; peptide-aspartate
                     beta-dioxygenase; FIH-1; factor inhibiting HIF-1;
                     hypoxia-inducible factor asparagine hydroxylase; hypoxia
                     inducible factor 1 alpha subunit inhibitor"
                     /calculated_mol_wt=40154
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWT6.2)"
     Region          2..125
                     /region_name="Interaction with VHL.
                     /evidence=ECO:0000269|PubMed:11641274"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWT6.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9NWT6.2)"
     Region          53..302
                     /region_name="Cupin_8"
                     /note="Cupin-like domain; pfam13621"
                     /db_xref="CDD:463936"
     Site            340
                     /site_type="other"
                     /note="Important for dimer formation; propagated from
                     UniProtKB/Swiss-Prot (Q9NWT6.2)"
     CDS             1..349
                     /gene="HIF1AN"
                     /gene_synonym="FIH1"
                     /coded_by="NM_017902.3:17..1066"
                     /db_xref="CCDS:CCDS7498.1"
                     /db_xref="GeneID:55662"
                     /db_xref="HGNC:HGNC:17113"
                     /db_xref="MIM:606615"
ORIGIN      
        1 maataaeava sgsgepreea galgpawdes qlrsysfptr piprlsqsdp raeelienee
       61 pvvltdtnlv ypalkwdley lqenigngdf svysasthkf lyydekkman fqnfkprsnr
      121 eemkfhefve klqdiqqrgg eerlylqqtl ndtvgrkivm dflgfnwnwi nkqqgkrgwg
      181 qltsnlllig megnvtpahy deqqnffaqi kgykrcilfp pdqfeclypy pvhhpcdrqs
      241 qvdfdnpdye rfpnfqnvvg yetvvgpgdv lyipmywwhh iesllnggit itvnfwykga
      301 ptpkrieypl kahqkvaimr niekmlgeal gnpqevgpll ntmikgryn
//
LOCUS       NP_001258647             134 aa            linear   PRI 27-APR-2025
DEFINITION  serine protease inhibitor Kazal-type 2 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001258647
VERSION     NP_001258647.1
DBSOURCE    REFSEQ: accession NM_001271718.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Pitts,H.A., Cheng,C.K., Cheung,J.S., Sun,M.K., Yung,Y.L.,
            Chan,H.Y., Wong,R.S.M., Yip,S.F., Lau,K.N., Wong,W.S.,
            Raghupathy,R., Chan,N.P.H. and Ng,M.H.L.
  TITLE     SPINK2 Protein Expression Is an Independent Adverse Prognostic
            Marker in AML and Is Potentially Implicated in the Regulation of
            Ferroptosis and Immune Response
  JOURNAL   Int J Mol Sci 24 (11), 9696 (2023)
   PUBMED   37298647
  REMARK    GeneRIF: SPINK2 Protein Expression Is an Independent Adverse
            Prognostic Marker in AML and Is Potentially Implicated in the
            Regulation of Ferroptosis and Immune Response.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Shyu,R.Y., Wang,C.H., Wu,C.C., Wang,L.K., Chen,M.L., Kuo,C.Y.,
            Lee,M.C., Lin,Y.Y. and Tsai,F.M.
  TITLE     Tazarotene-Induced Gene 1 (TIG1) Interacts with Serine Protease
            Inhibitor Kazal-Type 2 (SPINK2) to Inhibit Cellular Invasion of
            Testicular Carcinoma Cells
  JOURNAL   Biomed Res Int 2019, 6171065 (2019)
   PUBMED   31886233
  REMARK    GeneRIF: Investigated whether tazarotene-induced gene 1 protein
            (TIG1) affects the activity of urokinase plasminogen-type
            activator, which is negatively regulated by serine peptidase
            inhibitor Kazal type 2 (SPINK2), potentially preventing epithelial
            mesenchymal transition and suppressing cell migration and invasion.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Nishimiya,D., Kawaguchi,Y., Kodama,S., Nasu,H., Yano,H.,
            Yamaguchi,A., Tamura,M. and Hashimoto,R.
  TITLE     A protein scaffold, engineered SPINK2, for generation of inhibitors
            with high affinity and specificity against target proteases
  JOURNAL   Sci Rep 9 (1), 11436 (2019)
   PUBMED   31391482
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 134)
  AUTHORS   Kherraf,Z.E., Christou-Kent,M., Karaouzene,T., Amiri-Yekta,A.,
            Martinez,G., Vargas,A.S., Lambert,E., Borel,C., Dorphin,B.,
            Aknin-Seifer,I., Mitchell,M.J., Metzler-Guillemain,C.,
            Escoffier,J., Nef,S., Grepillat,M., Thierry-Mieg,N., Satre,V.,
            Bailly,M., Boitrelle,F., Pernet-Gallay,K., Hennebicq,S., Faure,J.,
            Bottari,S.P., Coutton,C., Ray,P.F. and Arnoult,C.
  TITLE     SPINK2 deficiency causes infertility by inducing sperm defects in
            heterozygotes and azoospermia in homozygotes
  JOURNAL   EMBO Mol Med 9 (8), 1132-1149 (2017)
   PUBMED   28554943
  REMARK    GeneRIF: These results demonstrate that SPINK2 is necessary to
            neutralize proteases during their cellular transit toward the
            acrosome and that its deficiency induces a pathological continuum
            ranging from oligoasthenoteratozoospermia in heterozygotes to
            azoospermia in homozygotes.
REFERENCE   6  (residues 1 to 134)
  AUTHORS   Moritz,A., Grzeschik,K.H., Wingender,E. and Fink,E.
  TITLE     Organization and sequence of the gene encoding the human
            acrosin-trypsin inhibitor (HUSI-II)
  JOURNAL   Gene 123 (2), 277-281 (1993)
   PUBMED   8428671
REFERENCE   7  (residues 1 to 134)
  AUTHORS   Moritz,A., Lilja,H. and Fink,E.
  TITLE     Molecular cloning and sequence analysis of the cDNA encoding the
            human acrosin-trypsin inhibitor (HUSI-II)
  JOURNAL   FEBS Lett 278 (1), 127-130 (1991)
   PUBMED   1704312
REFERENCE   8  (residues 1 to 134)
  AUTHORS   Collins,J., Taube,W., Fink,E., Moritz,A. and Fritz,H.
  TITLE     Variants of human seminal acrosin inhibitor (HUSI-II) which inhibit
            human leukocyte elastase
  JOURNAL   Biomed Biochim Acta 50 (4-6), 683-685 (1991)
   PUBMED   1801743
REFERENCE   9  (residues 1 to 134)
  AUTHORS   Fink,E., Hehlein-Fink,C. and Eulitz,M.
  TITLE     Amino acid sequence elucidation of human acrosin-trypsin inhibitor
            (HUSI-II) reveals that Kazal-type proteinase inhibitors are
            structurally related to beta-subunits of glycoprotein hormones
  JOURNAL   FEBS Lett 270 (1-2), 222-224 (1990)
   PUBMED   2226783
REFERENCE   10 (residues 1 to 134)
  AUTHORS   Dietl,T., Kruck,J., Schill,W.B. and Fritz,H.
  TITLE     Localization of seminal plasma proteinase inhibitors in human
            spermatozoa as revealed by the indirect immunofluorescence
            technique
  JOURNAL   Hoppe Seylers Z Physiol Chem 357 (10), 1333-1337 (1976)
   PUBMED   791787
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY028205.1, BI561149.1,
            BI562269.1 and AA973772.1.
            
            Summary: This gene encodes a member of the family of serine
            protease inhibitors of the Kazal type (SPINK). The encoded protein
            acts as a trypsin and acrosin inhibitor in the genital tract and is
            localized in the spermatozoa. The protein has been associated with
            the progression of lymphomas. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI561149.1, SRR5189667.50130.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2158188
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000506738.6/ ENSP00000425961.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..134
                     /product="serine protease inhibitor Kazal-type 2 isoform 1
                     precursor"
                     /note="serine protease inhibitor Kazal-type 2; epididymis
                     tissue protein Li 172; serine peptidase inhibitor, Kazal
                     type 2 (acrosin-trypsin inhibitor)"
                     /calculated_mol_wt=11535
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2374
     Region          86..134
                     /region_name="Kazal_1"
                     /note="Kazal-type serine protease inhibitor domain;
                     pfam00050"
                     /db_xref="CDD:395004"
     CDS             1..134
                     /gene="SPINK2"
                     /gene_synonym="HUSI-II; SPGF29"
                     /coded_by="NM_001271718.2:40..444"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS63971.1"
                     /db_xref="GeneID:6691"
                     /db_xref="HGNC:HGNC:11245"
                     /db_xref="MIM:605753"
ORIGIN      
        1 malsvlrlal lllavtfags arsgpgergp peksgfgsqt gggpcpapgg lgdgtrapvt
       61 ggspedlpas lipqfglfsk yrtpncsqyr lpgcprhfnp vcgsdmstya nectlcmkir
      121 egghnikiir ngpc
//
LOCUS       NP_001357264             592 aa            linear   PRI 27-APR-2025
DEFINITION  protein phosphatase EYA1 isoform 1 [Homo sapiens].
ACCESSION   NP_001357264
VERSION     NP_001357264.1
DBSOURCE    REFSEQ: accession NM_001370335.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Shao,H., Li,Y., Zhao,H., Lin,K., Gao,Y., Ming,C. and Ma,J.
  TITLE     [Clinical phenotypic and genetic analysis of syndrome families with
            EYA1 gene variants]
  JOURNAL   Lin Chuang Er Bi Yan Hou Tou Jing Wai Ke Za Zhi 38 (7), 636-640
            (2024)
   PUBMED   38973045
  REMARK    GeneRIF: [Clinical phenotypic and genetic analysis of syndrome
            families with EYA1 gene variants].
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Zhang,H., Gao,J., Wang,H., Liu,M., Lu,S., Xu,H., Tang,W. and
            Zheng,G.
  TITLE     Novel likely pathogenic variant in the EYA1 gene causing Branchio
            oto renal syndrome and the exploration of pathogenic mechanisms
  JOURNAL   BMC Med Genomics 17 (1), 89 (2024)
   PUBMED   38627775
  REMARK    GeneRIF: Novel likely pathogenic variant in the EYA1 gene causing
            Branchio oto renal syndrome and the exploration of pathogenic
            mechanisms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Wang,F., Zhang,R., Jian,J., Sun,Y. and Li,Q.
  TITLE     Identification and Functional Study of Enhancers of EYA1: The
            Causative Gene of Branchio-Oto-Renal Syndrome
  JOURNAL   Dev Neurosci 46 (5), 333-340 (2024)
   PUBMED   38228108
  REMARK    GeneRIF: Identification and Functional Study of Enhancers of EYA1:
            The Causative Gene of Branchio-Oto-Renal Syndrome.
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Yalcouye,A., Traore,O., Diarra,S., Schrauwen,I., Esoh,K.,
            Kadlubowska,M.K., Bharadwaj,T., Adadey,S.M., Keita,M., Guinto,C.O.,
            Leal,S.M., Landoure,G. and Wonkam,A.
  TITLE     A monoallelic variant in EYA1 is associated with Branchio-Otic
            syndrome in a Malian family
  JOURNAL   Mol Genet Genomic Med 10 (7), e1995 (2022)
   PUBMED   35698919
  REMARK    GeneRIF: A monoallelic variant in EYA1 is associated with
            Branchio-Otic syndrome in a Malian family.
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Pignoni,F., Hu,B., Zavitz,K.H., Xiao,J., Garrity,P.A. and
            Zipursky,S.L.
  TITLE     The eye-specification proteins So and Eya form a complex and
            regulate multiple steps in Drosophila eye development
  JOURNAL   Cell 91 (7), 881-891 (1997)
   PUBMED   9428512
  REMARK    Erratum:[Cell 1998 Feb 20;92(4):following 585]
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Abdelhak,S., Kalatzis,V., Heilig,R., Compain,S., Samson,D.,
            Vincent,C., Levi-Acobas,F., Cruaud,C., Le Merrer,M., Mathieu,M.,
            Konig,R., Vigneron,J., Weissenbach,J., Petit,C. and Weil,D.
  TITLE     Clustering of mutations responsible for branchio-oto-renal (BOR)
            syndrome in the eyes absent homologous region (eyaHR) of EYA1
  JOURNAL   Hum Mol Genet 6 (13), 2247-2255 (1997)
   PUBMED   9361030
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Abdelhak,S., Kalatzis,V., Heilig,R., Compain,S., Samson,D.,
            Vincent,C., Weil,D., Cruaud,C., Sahly,I., Leibovici,M.,
            Bitner-Glindzicz,M., Francis,M., Lacombe,D., Vigneron,J.,
            Charachon,R., Boven,K., Bedbeder,P., Van Regemorter,N.,
            Weissenbach,J. and Petit,C.
  TITLE     A human homologue of the Drosophila eyes absent gene underlies
            branchio-oto-renal (BOR) syndrome and identifies a novel gene
            family
  JOURNAL   Nat Genet 15 (2), 157-164 (1997)
   PUBMED   9020840
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Smith,R.J.H.
  TITLE     Branchiootorenal Spectrum Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301554
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Stoppa-Lyonnet,D., Carter,P.E., Meo,T. and Tosi,M.
  TITLE     Clusters of intragenic Alu repeats predispose the human C1
            inhibitor locus to deleterious rearrangements
  JOURNAL   Proc Natl Acad Sci U S A 87 (4), 1551-1555 (1990)
   PUBMED   2154751
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099805.2, AC016465.8 and
            AC022858.8.
            
            Summary: This gene encodes a member of the eyes absent (EYA) family
            of proteins. The encoded protein may play a role in the developing
            kidney, branchial arches, eye, and ear. Mutations of this gene have
            been associated with branchiootorenal dysplasia syndrome,
            branchiootic syndrome, and sporadic cases of congenital cataracts
            and ocular anterior segment anomalies. A similar protein in mice
            can act as a transcriptional activator. Alternatively spliced
            transcript variants have been identified for this gene. [provided
            by RefSeq, Dec 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.90343.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.3"
     Protein         1..592
                     /product="protein phosphatase EYA1 isoform 1"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="eyes absent homolog 1; protein phosphatase EYA1"
                     /calculated_mol_wt=64463
     Region          1..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99502.2)"
     Region          97..>275
                     /region_name="Chi1"
                     /note="Chitinase [Carbohydrate transport and metabolism];
                     COG3469"
                     /db_xref="CDD:442692"
     Region          240..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99502.2)"
     Region          321..592
                     /region_name="HAD_Eya"
                     /note="protein tyrosine phosphatase domain of the nuclear
                     transcription factor of Eyes absent (Eya) and related
                     phosphatase domains; cd02601"
                     /db_xref="CDD:319789"
     Site            order(323,550,552,568,570..573,579,582,585..586,589..592)
                     /site_type="other"
                     /note="SIX1 interface [polypeptide binding]"
                     /db_xref="CDD:319789"
     Site            order(328..332,422..423,531,555..556,560..561)
                     /site_type="active"
                     /db_xref="CDD:319789"
     CDS             1..592
                     /gene="EYA1"
                     /gene_synonym="BOP; BOR; BOS1; OFC1; OTFCS"
                     /coded_by="NM_001370335.1:680..2458"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS34906.1"
                     /db_xref="GeneID:2138"
                     /db_xref="HGNC:HGNC:3519"
                     /db_xref="MIM:601653"
ORIGIN      
        1 memqdltsph srlsgssesp sgpklgnshi nsnsmtpngt evktepmsss etasttadgs
       61 lnnfsgsaig sssfsprpth qfsppqiyps nrpyphilpt pssqtmaayg qtqfttgmqq
      121 atayatypqp gqpygissyg alwagikteg glsqsqspgq tgflsygtsf stpqpgqapy
      181 syqmqgssft tssgiytgnn sltnssgfns sqqdypsyps fgqgqyaqyy nsspypahym
      241 tssntspttp stnatyqlqe ppsgitsqav tdptaeysti hspstpikds dsdrlrrgsd
      301 gksrgrgrrn nnpspppdsd lervfiwdld etiivfhsll tgsyanrygr dpptsvslgl
      361 rmeemifnla dthlffndle ecdqvhiddv ssddngqdls tynfgtdgfp aaatsanlcl
      421 atgvrggvdw mrklafryrr vkeiyntykn nvggllgpak reawlqlrae iealtdswlt
      481 lalkalslih srtncvnilv tttqlipala kvllyglgiv fpieniysat kigkescfer
      541 iiqrfgrkvv yvvigdgvee eqgakkhamp fwrisshsdl malhhalele yl
//
LOCUS       NP_597705               1099 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 132D precursor [Homo sapiens].
ACCESSION   NP_597705 XP_062545
VERSION     NP_597705.2
DBSOURCE    REFSEQ: accession NM_133448.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Chuang,H.K., Hsieh,A.R., Ang,T.Y., Chen,S.W., Yang,Y.P.,
            Huang,H.J., Chiou,S.H., Lin,T.C., Chen,S.J., Hsu,C.C. and
            Hwang,D.K.
  TITLE     TMEM132D and VIPR2 Polymorphisms as Genetic Risk Loci for Retinal
            Detachment: A Genome-Wide Association Study and Polygenic Risk
            Score Analysis
  JOURNAL   Invest Ophthalmol Vis Sci 64 (12), 17 (2023)
   PUBMED   37695605
  REMARK    GeneRIF: TMEM132D and VIPR2 Polymorphisms as Genetic Risk Loci for
            Retinal Detachment: A Genome-Wide Association Study and Polygenic
            Risk Score Analysis.
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Wang,X., Jiang,W., Luo,S., Yang,X., Wang,C., Wang,B., Dang,Y.,
            Shen,Y. and Ma,D.K.
  TITLE     The C. elegans homolog of human panic-disorder risk gene TMEM132D
            orchestrates neuronal morphogenesis through the WAVE-regulatory
            complex
  JOURNAL   Mol Brain 14 (1), 54 (2021)
   PUBMED   33726789
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Sanchez-Pulido,L. and Ponting,C.P.
  TITLE     TMEM132: an ancient architecture of cohesin and immunoglobulin
            domains define a new family of neural adhesion molecules
  JOURNAL   Bioinformatics 34 (5), 721-724 (2018)
   PUBMED   29088312
REFERENCE   4  (residues 1 to 1099)
  AUTHORS   Naik,R.R., Sotnikov,S.V., Diepold,R.P., Iurato,S., Markt,P.O.,
            Bultmann,A., Brehm,N., Mattheus,T., Lutz,B., Erhardt,A.,
            Binder,E.B., Schmidt,U., Holsboer,F., Landgraf,R. and Czibere,L.
  TITLE     Polymorphism in Tmem132d regulates expression and anxiety-related
            behavior through binding of RNA polymerase II complex
  JOURNAL   Transl Psychiatry 8 (1), 1 (2018)
   PUBMED   29317594
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1099)
  AUTHORS   Shimada-Sugimoto,M., Otowa,T., Miyagawa,T., Khor,S.S., Omae,Y.,
            Toyo-Oka,L., Sugaya,N., Kawamura,Y., Umekage,T., Miyashita,A.,
            Kuwano,R., Kaiya,H., Kasai,K., Tanii,H., Okazaki,Y., Tokunaga,K.
            and Sasaki,T.
  TITLE     Polymorphisms in the TMEM132D region are associated with panic
            disorder in HLA-DRB1*13:02-negative individuals of a Japanese
            population
  JOURNAL   Hum Genome Var 3, 16001 (2016)
   PUBMED   27081567
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1099)
  AUTHORS   Quast,C., Altmann,A., Weber,P., Arloth,J., Bader,D., Heck,A.,
            Pfister,H., Muller-Myhsok,B., Erhardt,A. and Binder,E.B.
  TITLE     Rare variants in TMEM132D in a case-control sample for panic
            disorder
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 159B (8), 896-907 (2012)
   PUBMED   22911938
  REMARK    GeneRIF: data suggest that not only common but also putatively
            functional and/or rare variants within TMEM132D might contribute to
            the risk to develop anxiety disorders
REFERENCE   7  (residues 1 to 1099)
  AUTHORS   Mick,E., McGough,J., Loo,S., Doyle,A.E., Wozniak,J., Wilens,T.E.,
            Smalley,S., McCracken,J., Biederman,J. and Faraone,S.V.
  TITLE     Genome-wide association study of the child behavior checklist
            dysregulation profile
  JOURNAL   J Am Acad Child Adolesc Psychiatry 50 (8), 807-17 (2011)
   PUBMED   21784300
  REMARK    GeneRIF: We found no genome-wide statistically significant
            associations but identified several plausible candidate genes among
            findings at p < 5E-05: TMEM132D, LRRC7, SEMA3A, ALK, and STIP1.
REFERENCE   8  (residues 1 to 1099)
  AUTHORS   Erhardt,A., Czibere,L., Roeske,D., Lucae,S., Unschuld,P.G.,
            Ripke,S., Specht,M., Kohli,M.A., Kloiber,S., Ising,M., Heck,A.,
            Pfister,H., Zimmermann,P., Lieb,R., Putz,B., Uhr,M., Weber,P.,
            Deussing,J.M., Gonik,M., Bunck,M., Kebler,M.S., Frank,E.,
            Hohoff,C., Domschke,K., Krakowitzky,P., Maier,W., Bandelow,B.,
            Jacob,C., Deckert,J., Schreiber,S., Strohmaier,J., Nothen,M.,
            Cichon,S., Rietschel,M., Bettecken,T., Keck,M.E., Landgraf,R.,
            Muller-Myhsok,B., Holsboer,F. and Binder,E.B.
  TITLE     TMEM132D, a new candidate for anxiety phenotypes: evidence from
            human and mouse studies
  JOURNAL   Mol Psychiatry 16 (6), 647-663 (2011)
   PUBMED   20368705
  REMARK    GeneRIF: TMEM132D may be an important new candidate gene for PD as
            well as more generally for anxiety-related behavior.
REFERENCE   9  (residues 1 to 1099)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   10 (residues 1 to 1099)
  AUTHORS   Nomoto,H., Yonezawa,T., Itoh,K., Ono,K., Yamamoto,K., Oohashi,T.,
            Shiraga,F., Ohtsuki,H. and Ninomiya,Y.
  TITLE     Molecular cloning of a novel transmembrane protein MOLT expressed
            by mature oligodendrocytes
  JOURNAL   J Biochem 134 (2), 231-238 (2003)
   PUBMED   12966072
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC055717.36, AB061814.1, BC114626.1 and AC107033.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 29, 2008 this sequence version replaced NP_597705.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB061814.1, BC114626.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000422113.7/ ENSP00000408581.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..1099
                     /product="transmembrane protein 132D precursor"
                     /note="mature OL transmembrane protein; mature
                     oligodendrocytes transmembrane protein; protein
                     phosphatase 1, regulatory subunit 153"
                     /calculated_mol_wt=118999
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3329
     mat_peptide     31..1099
                     /product="Transmembrane protein 132D. /id=PRO_0000287100"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C87.1)"
                     /calculated_mol_wt=118999
     Region          49..177
                     /region_name="TMEM132D_N"
                     /note="Mature oligodendrocyte transmembrane protein,
                     TMEM132D, N-term; pfam15705"
                     /db_xref="CDD:464813"
     Region          436..779
                     /region_name="TMEM132"
                     /note="Transmembrane protein family 132; pfam16070"
                     /db_xref="CDD:465003"
     Site            505
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14C87.1)"
     Region          797..858
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C87.1)"
     Region          886..970
                     /region_name="TMEM132D_C"
                     /note="Mature oligodendrocyte transmembrane protein,
                     TMEM132D, C-term; pfam15706"
                     /db_xref="CDD:464814"
     Site            916..936
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C87.1)"
     CDS             1..1099
                     /gene="TMEM132D"
                     /gene_synonym="MOLT; PPP1R153"
                     /coded_by="NM_133448.3:687..3986"
                     /db_xref="CCDS:CCDS9266.1"
                     /db_xref="GeneID:121256"
                     /db_xref="HGNC:HGNC:29411"
                     /db_xref="MIM:611257"
ORIGIN      
        1 mcpsemgtlw hhwspvlisl aalfskvteg rgilesiqrf sllptylpvt yhinnadvsf
       61 flkeanqdim rnsslqsrve sfliyksrrl pvlnasygpf sieqvvpqdl mlpsnpfgft
      121 nkfslnwklk ahilrdkvyl srpkvqvlfh imgrdwddrs ageklpclrv fafretrevr
      181 gscrlqgdlg lcvaelells swfspptvva grrksvdqpe gtpvelyytv hpggergdcv
      241 redarrsngi rtghsdides gpplqrigsi flyqthrkps lrelrldnsv aihyipktvr
      301 kgdvltfpvs isrnstedrf tlrakvkkgv niigvrassp siwdvkertd ytgkyapavi
      361 vcqkkaagse nsadgasyev mqidveveep gdlpatqlvt wqveypgeit sdlgvskiyv
      421 spkdligvvp lameaeilnt ailtgktvav pvkvvsvedd gtvtellesv ecrssdedvi
      481 kvsdrcdyvf vngkemkgkv nvvvnftyqh lssplemtvw vprlplqiev sdtelnqikg
      541 wrvpivssrr pagdseeeed derrgrgctl qyqhamvrvl tqfvaeaagp gghlahllgs
      601 dwqvditeli ndfmqveepr iaklqggqil mgqelgmtti qilsplsdti laektitvld
      661 ekvtitdlgv qlvtglslsl qlspgsnrai fatavaqell qrpkqeaais cwvqfsdgsv
      721 tpldiydgkd fslmatslde kvvsihqdpk fkwpiiaaet egqgtlvkve mvisescqks
      781 krksvlavgt anikvkfgqn danpntsdsr htgagvhmen nvsdrrpkkp sqewgsqegq
      841 yygsssmglm egrgtttdrs ilqkkkgqes llddnshlqt ipsdltsfpa qvdlprsnge
      901 mdgndlmqas kglsdleigm yallgvfcla ilvflincvt falkyrhkqv pfeeqegmsh
      961 shdwvglsnr tellenhinf assqdeqita idrgmdfees kyllstnsqk singqlfkpl
     1021 gpiiidgkdq ksepptspts krkrvkfttf tavssddeyp trnsivmsse ddikwvcqdl
     1081 dpgdckelhn ymerlhenv
//
LOCUS       NP_001103689             261 aa            linear   PRI 27-APR-2025
DEFINITION  gap junction beta-6 protein [Homo sapiens].
ACCESSION   NP_001103689
VERSION     NP_001103689.1
DBSOURCE    REFSEQ: accession NM_001110219.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   O'Shaughnessy,E.M., Duffy,W., Garcia-Vega,L., Hussey,K.,
            Burden,A.D., Zamiri,M. and Martin,P.E.
  TITLE     Dysregulation of Connexin Expression Plays a Pivotal Role in
            Psoriasis
  JOURNAL   Int J Mol Sci 22 (11), 6060 (2021)
   PUBMED   34199748
  REMARK    GeneRIF: Dysregulation of Connexin Expression Plays a Pivotal Role
            in Psoriasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Buonfiglio,P., Bruque,C.D., Luce,L., Giliberto,F., Lotersztein,V.,
            Menazzi,S., Paoli,B., Elgoyhen,A.B. and Dalamon,V.
  TITLE     GJB2 and GJB6 Genetic Variant Curation in an Argentinean
            Non-Syndromic Hearing-Impaired Cohort
  JOURNAL   Genes (Basel) 11 (10), 1233 (2020)
   PUBMED   33096615
  REMARK    GeneRIF: GJB2 and GJB6 Genetic Variant Curation in an Argentinean
            Non-Syndromic Hearing-Impaired Cohort.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Zhan,Y., Luo,S., Pi,Z. and Zhang,G.
  TITLE     A recurrent mutation of GJB6 in a big Chinese family with Hidrotic
            ectodermal dysplasia
  JOURNAL   Hereditas 157 (1), 34 (2020)
   PUBMED   32843087
  REMARK    GeneRIF: A recurrent mutation of GJB6 in a big Chinese family with
            Hidrotic ectodermal dysplasia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Eggena,M., Targan,S.R., Iwanczyk,L., Vidrich,A., Gordon,L.K. and
            Braun,J.
  TITLE     Phage display cloning and characterization of an immunogenetic
            marker (perinuclear anti-neutrophil cytoplasmic antibody) in
            ulcerative colitis
  JOURNAL   J Immunol 156 (10), 4005-4011 (1996)
   PUBMED   8621942
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Kibar,Z., Der Kaloustian,V.M., Brais,B., Hani,V., Fraser,F.C. and
            Rouleau,G.A.
  TITLE     The gene responsible for Clouston hidrotic ectodermal dysplasia
            maps to the pericentromeric region of chromosome 13q
  JOURNAL   Hum Mol Genet 5 (4), 543-547 (1996)
   PUBMED   8845850
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Stoppini,M., Bellotti,V., Negri,A., Merlini,G., Garver,F. and
            Ferri,G.
  TITLE     Characterization of the two unique human anti-flavin monoclonal
            immunoglobulins
  JOURNAL   Eur J Biochem 228 (3), 886-893 (1995)
   PUBMED   7737190
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Smith,R.J.H. and Ranum,P.T.
  TITLE     Nonsyndromic Hearing Loss and Deafness, DFNA3 - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301708
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Smith,R.J.H., Azaiez,H. and Booth,K.
  TITLE     GJB2-Related Autosomal Recessive Nonsyndromic Hearing Loss
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301449
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Mellerio,J. and Greenblatt,D.
  TITLE     Hidrotic Ectodermal Dysplasia 2
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301379
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN998505.1, BP227986.1,
            AK075247.1, CF453597.1 and BC038934.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Gap junctions allow the transport of ions and metabolites
            between the cytoplasm of adjacent cells. They are formed by two
            hemichannels, made up of six connexin proteins assembled in groups.
            Each connexin protein has four transmembrane segments, two
            extracellular loops, a cytoplasmic loop formed between the two
            inner transmembrane segments, and the N- and C-terminus both being
            in the cytoplasm. The specificity of the gap junction is determined
            by which connexin proteins comprise the hemichannel. In the past,
            connexin protein names were based on their molecular weight,
            however the new nomenclature uses sequential numbers based on which
            form (alpha or beta) of the gap junction is present. This gene
            encodes one of the connexin proteins. Mutations in this gene have
            been found in some forms of deafness and in some families with
            hidrotic ectodermal dysplasia. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.232839.1,
                                           SRR1660807.230555.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147596 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000647029.1/ ENSP00000493834.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..261
                     /product="gap junction beta-6 protein"
                     /note="ectodermal dysplasia 2, hidrotic (Clouston
                     syndrome); connexin 30; gap junction protein, beta 6,
                     30kDa"
                     /calculated_mol_wt=30256
     Region          2..215
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            23..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     Site            76..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     Site            132..154
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     Site            193..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     CDS             1..261
                     /gene="GJB6"
                     /gene_synonym="CX30; DFNA3; DFNA3B; DFNB1B; ECTD2; ED2;
                     EDH; HED; HED2"
                     /coded_by="NM_001110219.3:546..1331"
                     /db_xref="CCDS:CCDS9291.1"
                     /db_xref="GeneID:10804"
                     /db_xref="HGNC:HGNC:4288"
                     /db_xref="MIM:604418"
ORIGIN      
        1 mdwgtlhtfi ggvnkhstsi gkvwitvifi frvmilvvaa qevwgdeqed fvcntlqpgc
       61 knvcydhffp vshirlwalq lifvstpall vamhvayyrh ettrkfrrge krndfkdied
      121 ikkqkvrieg slwwtytssi ffriifeaaf myvfyflyng yhlpwvlkcg idpcpnlvdc
      181 fisrptektv ftifmisasv icmllnvael cylllkvcfr rskraqtqkn hpnhalkesk
      241 qnemnelisd sgqnaitgfp s
//
LOCUS       NP_001265170             906 aa            linear   PRI 27-APR-2025
DEFINITION  proline-, glutamic acid- and leucine-rich protein 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001265170
VERSION     NP_001265170.1
DBSOURCE    REFSEQ: accession NM_001278241.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 906)
  AUTHORS   Skibinska,I., Andrusiewicz,M., Jendraszak,M., Zbikowska,A., Zaba,C.
            and Kotwicka,M.
  TITLE     PELP1 and SRC kinase as important molecules in the
            estrogen-mediated pathway in human testis and epididymis
  JOURNAL   Acta Biochim Pol 70 (2), 447-456 (2023)
   PUBMED   37159918
  REMARK    GeneRIF: PELP1 and SRC kinase as important molecules in the
            estrogen-mediated pathway in human testis and epididymis.
REFERENCE   2  (residues 1 to 906)
  AUTHORS   Skibinska,I., Andrusiewicz,M., Jendraszak,M., Zbikowska,A.,
            Jedrzejczak,P. and Kotwicka,M.
  TITLE     Expression of estrogen receptors, PELP1, and SRC in human
            spermatozoa and their associations with semen quality
  JOURNAL   Hum Cell 36 (2), 554-567 (2023)
   PUBMED   36577884
  REMARK    GeneRIF: Expression of estrogen receptors, PELP1, and SRC in human
            spermatozoa and their associations with semen quality.
REFERENCE   3  (residues 1 to 906)
  AUTHORS   Gordon,J., Chapus,F.L., Viverette,E.G., Williams,J.G.,
            Deterding,L.J., Krahn,J.M., Borgnia,M.J., Rodriguez,J., Warren,A.J.
            and Stanley,R.E.
  TITLE     Cryo-EM reveals the architecture of the PELP1-WDR18 molecular
            scaffold
  JOURNAL   Nat Commun 13 (1), 6783 (2022)
   PUBMED   36351913
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 906)
  AUTHORS   Wang,X., Yin,W. and Liang,L.
  TITLE     PELP1 is overexpressed in lung cancer and promotes tumor cell
            malignancy and resistance to tyrosine kinase inhibitor drug
  JOURNAL   Pathol Res Pract 237, 154065 (2022)
   PUBMED   35969940
  REMARK    GeneRIF: PELP1 is overexpressed in lung cancer and promotes tumor
            cell malignancy and resistance to tyrosine kinase inhibitor drug.
REFERENCE   5  (residues 1 to 906)
  AUTHORS   Zhang,D., Dai,J., Pan,Y., Wang,X., Qiao,J., Sasano,H., Zhao,B.,
            McNamara,K.M., Guan,X., Liu,L., Zhang,Y., Chan,M.S.M., Cao,S.,
            Liu,M., Song,S. and Wang,L.
  TITLE     Overexpression of PELP1 in Lung Adenocarcinoma Promoted E2 Induced
            Proliferation, Migration and Invasion of the Tumor Cells and
            Predicted a Worse Outcome of the Patients
  JOURNAL   Pathol Oncol Res 27, 582443 (2021)
   PUBMED   34257530
  REMARK    GeneRIF: Overexpression of PELP1 in Lung Adenocarcinoma Promoted E2
            Induced Proliferation, Migration and Invasion of the Tumor Cells
            and Predicted a Worse Outcome of the Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 906)
  AUTHORS   Choi,Y.B., Ko,J.K. and Shin,J.
  TITLE     The transcriptional corepressor, PELP1, recruits HDAC2 and masks
            histones using two separate domains
  JOURNAL   J Biol Chem 279 (49), 50930-50941 (2004)
   PUBMED   15456770
  REMARK    GeneRIF: PELP1 recruits HDAC2 and masks histones using two separate
            domains
REFERENCE   7  (residues 1 to 906)
  AUTHORS   Nair,S.S., Mishra,S.K., Yang,Z., Balasenthil,S., Kumar,R. and
            Vadlamudi,R.K.
  TITLE     Potential role of a novel transcriptional coactivator PELP1 in
            histone H1 displacement in cancer cells
  JOURNAL   Cancer Res 64 (18), 6416-6423 (2004)
   PUBMED   15374949
  REMARK    GeneRIF: Results provide novel insights about the transcription
            regulation of PELP1 and suggest that PELP1 participates in
            chromatin remodeling activity via displacement of histone 1 in
            cancer cells.
REFERENCE   8  (residues 1 to 906)
  AUTHORS   Barletta,F., Wong,C.W., McNally,C., Komm,B.S., Katzenellenbogen,B.
            and Cheskis,B.J.
  TITLE     Characterization of the interactions of estrogen receptor and MNAR
            in the activation of cSrc
  JOURNAL   Mol Endocrinol 18 (5), 1096-1108 (2004)
   PUBMED   14963108
REFERENCE   9  (residues 1 to 906)
  AUTHORS   Balasenthil,S. and Vadlamudi,R.K.
  TITLE     Functional interactions between the estrogen receptor coactivator
            PELP1/MNAR and retinoblastoma protein
  JOURNAL   J Biol Chem 278 (24), 22119-22127 (2003)
   PUBMED   12682072
  REMARK    GeneRIF: PELP1, a steroid coactivator, plays a permissive role in
            E2-mediated cell cycle progression, presumably via its regulatory
            interaction with the pRb pathway
REFERENCE   10 (residues 1 to 906)
  AUTHORS   Vadlamudi,R.K., Wang,R.A., Mazumdar,A., Kim,Y., Shin,J., Sahin,A.
            and Kumar,R.
  TITLE     Molecular cloning and characterization of PELP1, a novel human
            coregulator of estrogen receptor alpha
  JOURNAL   J Biol Chem 276 (41), 38272-38279 (2001)
   PUBMED   11481323
  REMARK    GeneRIF: PELP1 is a coactivator of estrogen receptor (ER),
            interacts with ER, and may have a role in mammary tumorigenesis.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC417876.1, AK293838.1,
            AK299084.1, BC010457.2 and AC091153.10.
            
            Summary: This gene encodes a transcription factor which coactivates
            transcription of estrogen receptor responsive genes and corepresses
            genes activated by other hormone receptors or sequence-specific
            transcription factors. Expression of this gene is regulated by both
            members of the estrogen receptor family. This gene may be involved
            in the progression of several types of cancer. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2013].
            
            Transcript Variant: This variant (2) differs in its 5' UTR, uses a
            downstream in-frame start codon, and lacks an alternate in-frame
            segment in the 3' coding region, compared to variant 1. The encoded
            isoform (2) is shorter, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293838.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..906
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..906
                     /product="proline-, glutamic acid- and leucine-rich
                     protein 1 isoform 2"
                     /note="proline-, glutamic acid- and leucine-rich protein
                     1; proline and glutamic acid rich nuclear protein;
                     transcription factor HMX3; modulator of non-genomic
                     activity of estrogen receptor"
                     /calculated_mol_wt=96776
     Region          <2..79
                     /region_name="RIX1"
                     /note="rRNA processing/ribosome biogenesis; pfam08167"
                     /db_xref="CDD:429855"
     Region          276..342
                     /region_name="NUC202"
                     /note="NUC202 domain; pfam08166"
                     /db_xref="CDD:149302"
     Region          422..>490
                     /region_name="NUC202"
                     /note="NUC202 domain; pfam08166"
                     /db_xref="CDD:149302"
     CDS             1..906
                     /gene="PELP1"
                     /gene_synonym="MNAR; P160"
                     /coded_by="NM_001278241.2:550..3270"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS62038.1"
                     /db_xref="GeneID:27043"
                     /db_xref="HGNC:HGNC:30134"
                     /db_xref="MIM:609455"
ORIGIN      
        1 melavavlrd llryaaqlpa lfrdismnhl pglltsllgl rpeceqsale gmkacmtyfp
       61 racgslkgkl asfflsrvda lspqlqqlac ecysrlpslg agfsqglkht esweqelhsl
      121 laslhtllga lyegaetapv qnegpgveml lssedgdahv llqlrqrfsg larclglmls
      181 sefgapvsvp vqeildficr tlsvssknis lhgdgplrll llpsihleal dllsalilac
      241 gsrllrfgil igrllpqvln swsigrdsls pgqerpystv rtkvyailel wvqvcgasag
      301 mlqggasgea llthllsdis ppadalklrs prgspdgslq tgkpsapkkl kldvgeamap
      361 pshrkgdsna nsdvcaaalr glsrtilmcg plikeethrr lhdlvlplvm gvqqgevlgs
      421 spytssrcrr elyclllall lapsprcppp lacalqafsl gqredslevs sfcsealvtc
      481 aalthprvpp lqpmgptcpt papvpppeap spfrappfhp pgpmpsvgsm psagpmpsag
      541 pmpsagpvps arpgppttan hlglsvpglv svpprllpgp enhragsned pilapsgtpp
      601 ptippdetfg grvprpafvh ydkeeasdve islesdsdds vvivpeglpp lpppppsgat
      661 pppiaptgpp tasppvpake epeelpaapg plpppppppp pvpgpvtlpp pqlvpegtpg
      721 gggppaleed ltvininssd eeeeeeeeee eeeeeeeeee edfeeeeede eeyfeeeeee
      781 eeefeeefee eegeleeeee eedeeeeeel eeveregesp aagpppqelv eeepsapptl
      841 leeetedgsd kvqpppetpa eeemetetea ealqekeqdd taamladfid cppddekppp
      901 ptepds
//
LOCUS       NP_003408                627 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 264 [Homo sapiens].
ACCESSION   NP_003408 XP_375660
VERSION     NP_003408.1
DBSOURCE    REFSEQ: accession NM_003417.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 627)
  AUTHORS   Dolmans,G.H., Werker,P.M., Hennies,H.C., Furniss,D., Festen,E.A.,
            Franke,L., Becker,K., van der Vlies,P., Wolffenbuttel,B.H.,
            Tinschert,S., Toliat,M.R., Nothnagel,M., Franke,A., Klopp,N.,
            Wichmann,H.E., Nurnberg,P., Giele,H., Ophoff,R.A. and Wijmenga,C.
  CONSRTM   Dutch Dupuytren Study Group; German Dupuytren Study Group;
            LifeLines Cohort Study; BSSH-GODD Consortium
  TITLE     Wnt signaling and Dupuytren's disease
  JOURNAL   N Engl J Med 365 (4), 307-317 (2011)
   PUBMED   21732829
REFERENCE   5  (residues 1 to 627)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   6  (residues 1 to 627)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   7  (residues 1 to 627)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 627)
  AUTHORS   Kim,J., Bergmann,A., Wehri,E., Lu,X. and Stubbs,L.
  TITLE     Imprinting and evolution of two Kruppel-type zinc-finger genes,
            ZIM3 and ZNF264, located in the PEG3/USP29 imprinted domain
  JOURNAL   Genomics 77 (1-2), 91-98 (2001)
   PUBMED   11543637
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292504.1, AB007872.1,
            AC005261.2 and BF063192.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2004 this sequence version replaced XP_375660.1.
            
            Summary: This gene encodes a zinc finger protein and belongs to the
            krueppel C2H2-type zinc-finger protein family. Zinc finger proteins
            are often localized in the nucleus, bind nucleic acids, and
            regulate transcription. [provided by RefSeq, Jan 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292504.1, AB007872.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263095.10/ ENSP00000263095.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..627
                     /product="zinc finger protein 264"
                     /calculated_mol_wt=70456
     Region          14..74
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          74..155
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43296.1)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (O43296.1)"
     Region          174..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43296.1)"
     Region          205..225
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          221..240
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          233..253
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(238,240,242,244..245,248..249,252,266,268,272..273,
                     276..277,280,294,296,298,300..301,304..305,308)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          257..561
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          261..281
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          289..309
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          317..337
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (O43296.1)"
     Region          345..365
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          373..393
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          401..421
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(406,408,410,412..413,416..417,420,434,436,440..441,
                     444..445,448,462,464,466,468..469,472..473,476)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          429..449
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          457..477
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          485..505
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(490,492,494,496..497,500..501,504,518,520,524..525,
                     528..529,532,546,548,550,552..553,556..557,560)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (O43296.1)"
     Region          513..533
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          541..561
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          605..627
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43296.1)"
     CDS             1..627
                     /gene="ZNF264"
                     /coded_by="NM_003417.5:415..2298"
                     /db_xref="CCDS:CCDS33127.1"
                     /db_xref="GeneID:9422"
                     /db_xref="HGNC:HGNC:13057"
                     /db_xref="MIM:604668"
ORIGIN      
        1 maaavltdra qvsvtfddva vtftkeewgq ldlaqrtlyq evmlencgll vslgcpvpka
       61 elichlehgq epwtrkedls qdtcpgdkgk pkttepttce palsegislq gqvtqgnsvd
      121 sqlgqaedqd glsemqeghf rpgidpqeks pgkmspecdg lgtadgvcsr igqeqvspgd
      181 rvrshnsces gkdpmiqeee nnfkcsecgk vfnkkhllag hekihsgvkp yectecgktf
      241 iksthllqhh mihtgerpye cmecgkafnr ksyltqhqri hsgekpykcn ecgkafthrs
      301 nfvlhnrrht geksfvctec gqvfrhrpgf lrhyvvhsge npyeclecgk vfkhrsylmw
      361 hqqthtgekp yecsecgkvf lesaalihhy vihtgekpfe clecgkafnh rsylkrhqri
      421 htgekpfvcs ecgkafthcs tfilhkraht gekpfeckec gkafsnrkdl irhfsihtge
      481 kpyecvecgk aftrmsgltr hkrihsgekp yecvecgksf cwstnlirha iihtgekpyk
      541 csecgkafsr sssltqhqrm htgknpisvt dvgrpftsgq tsvtlrelll gkdflnvtte
      601 anilpeetss sasdqpyqre tpqvssl
//
LOCUS       NP_000623               1152 aa            linear   PRI 27-APR-2025
DEFINITION  integrin alpha-M isoform 2 precursor [Homo sapiens].
ACCESSION   NP_000623
VERSION     NP_000623.2
DBSOURCE    REFSEQ: accession NM_000632.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1152)
  AUTHORS   Liu,Y.G., Peng,H.R., Ren,R.W., Zhao,P. and Zhao,L.J.
  TITLE     CD11b maintains West Nile virus replication through modulation of
            immune response in human neuroblastoma cells
  JOURNAL   Virol J 21 (1), 158 (2024)
   PUBMED   39004752
  REMARK    GeneRIF: CD11b maintains West Nile virus replication through
            modulation of immune response in human neuroblastoma cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1152)
  AUTHORS   Yang,C., Li,L., Ye,Z., Zhang,A., Bao,Y., Wu,X., Ren,G., Jiang,C.,
            Wang,O. and Wang,Z.
  TITLE     Mechanisms underlying neutrophils adhesion to triple-negative
            breast cancer cells via CD11b-ICAM1 in promoting breast cancer
            progression
  JOURNAL   Cell Commun Signal 22 (1), 340 (2024)
   PUBMED   38907234
  REMARK    GeneRIF: Mechanisms underlying neutrophils adhesion to
            triple-negative breast cancer cells via CD11b-ICAM1 in promoting
            breast cancer progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1152)
  AUTHORS   Duan,M., Zhang,X., Lou,Y., Feng,J., Guo,P., Ye,S., Lv,P. and
            Chen,Y.
  TITLE     Deletion of Tmem268 in mice suppresses anti-infectious immune
            responses by downregulating CD11b signaling
  JOURNAL   EMBO Rep 25 (6), 2550-2570 (2024)
   PUBMED   38730209
REFERENCE   4  (residues 1 to 1152)
  AUTHORS   Hou,L., Li,Z., Guo,X., Lv,J., Chong,Z., Xiao,Y., Zhang,L. and Li,Z.
  TITLE     ITGAM is a critical gene in ischemic stroke
  JOURNAL   Aging (Albany NY) 16 (8), 6852-6867 (2024)
   PUBMED   38637126
  REMARK    GeneRIF: ITGAM is a critical gene in ischemic stroke.
REFERENCE   5  (residues 1 to 1152)
  AUTHORS   Lou,Y., Li,P.H., Liu,X.Q., Wang,T.X., Liu,Y.L., Chen,C.C. and
            Ma,K.L.
  TITLE     ITGAM-mediated macrophages contribute to basement membrane damage
            in diabetic nephropathy and atherosclerosis
  JOURNAL   BMC Nephrol 25 (1), 72 (2024)
   PUBMED   38413872
  REMARK    GeneRIF: ITGAM-mediated macrophages contribute to basement membrane
            damage in diabetic nephropathy and atherosclerosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1152)
  AUTHORS   Pahl,H.L., Rosmarin,A.G. and Tenen,D.G.
  TITLE     Characterization of the myeloid-specific CD11b promoter
  JOURNAL   Blood 79 (4), 865-870 (1992)
   PUBMED   1346576
REFERENCE   7  (residues 1 to 1152)
  AUTHORS   Shelley,C.S. and Arnaout,M.A.
  TITLE     The promoter of the CD11b gene directs myeloid-specific and
            developmentally regulated expression
  JOURNAL   Proc Natl Acad Sci U S A 88 (23), 10525-10529 (1991)
   PUBMED   1683702
REFERENCE   8  (residues 1 to 1152)
  AUTHORS   Hickstein,D.D., Hickey,M.J., Ozols,J., Baker,D.M., Back,A.L. and
            Roth,G.J.
  TITLE     cDNA sequence for the alpha M subunit of the human neutrophil
            adherence receptor indicates homology to integrin alpha subunits
  JOURNAL   Proc Natl Acad Sci U S A 86 (1), 257-261 (1989)
   PUBMED   2563162
REFERENCE   9  (residues 1 to 1152)
  AUTHORS   Corbi,A.L., Kishimoto,T.K., Miller,L.J. and Springer,T.A.
  TITLE     The human leukocyte adhesion glycoprotein Mac-1 (complement
            receptor type 3, CD11b) alpha subunit. Cloning, primary structure,
            and relation to the integrins, von Willebrand factor and factor B
  JOURNAL   J Biol Chem 263 (25), 12403-12411 (1988)
   PUBMED   2457584
REFERENCE   10 (residues 1 to 1152)
  AUTHORS   Arnaout,M.A., Gupta,S.K., Pierce,M.W. and Tenen,D.G.
  TITLE     Amino acid sequence of the alpha subunit of human leukocyte
            adhesion receptor Mo1 (complement receptor type 3)
  JOURNAL   J Cell Biol 106 (6), 2153-2158 (1988)
   PUBMED   2454931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK057856.1, BC096348.3,
            AA436312.1 and AC093520.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 20, 2006 this sequence version replaced NP_000623.1.
            
            Summary: This gene encodes the integrin alpha M chain. Integrins
            are heterodimeric integral membrane proteins composed of an alpha
            chain and a beta chain. This I-domain containing alpha integrin
            combines with the beta 2 chain (ITGB2) to form a leukocyte-specific
            integrin referred to as macrophage receptor 1 ('Mac-1'), or
            inactivated-C3b (iC3b) receptor 3 ('CR3'). The alpha M beta 2
            integrin is important in the adherence of neutrophils and monocytes
            to stimulated endothelium, and also in the phagocytosis of
            complement coated particles. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Mar 2009].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1.
            The resulting isoform (2) lacks one internal amino acid, compared
            to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.90372.1, BC096346.3
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000544665.9/ ENSP00000441691.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1152
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..1152
                     /product="integrin alpha-M isoform 2 precursor"
                     /note="antigen CD11b (p170); macrophage antigen alpha
                     polypeptide; neutrophil adherence receptor alpha-M
                     subunit; integrin alpha-M; CR-3 alpha chain; leukocyte
                     adhesion receptor MO1; CD11 antigen-like family member B;
                     cell surface glycoprotein MAC-1 subunit alpha; integrin,
                     alpha M (complement component 3 receptor 3 subunit);
                     macrophage-1 antigen alpha subunit"
                     /calculated_mol_wt=125472
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1725
     mat_peptide     17..1152
                     /product="Integrin alpha-M. /id=PRO_0000016289"
                     /note="propagated from UniProtKB/Swiss-Prot (P11215.2)"
                     /calculated_mol_wt=125472
     Region          18..75
                     /region_name="FG-GAP 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11215.2)"
     Region          76..135
                     /region_name="FG-GAP 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11215.2)"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Region          149..324
                     /region_name="vWA_integrins_alpha_subunit"
                     /note="Integrins are a class of adhesion receptors that
                     link the extracellular matrix to the cytoskeleton and
                     cooperate with growth factor receptors to promote celll
                     survival, cell cycle progression and cell migration.
                     Integrins consist of an alpha and a beta...; cd01469"
                     /db_xref="CDD:238746"
     Site            order(149,151,172,252,254,283,313)
                     /site_type="active"
                     /note="integrin inhibitor binding pocket [active]"
                     /db_xref="CDD:238746"
     Site            order(156,158,160,225,258)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238746"
     Site            order(158..160,162,225)
                     /site_type="active"
                     /note="integrin-collagen binding site [active]"
                     /db_xref="CDD:238746"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Region          339..390
                     /region_name="FG-GAP 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11215.2)"
     Region          391..442
                     /region_name="FG-GAP 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11215.2)"
     Site            391
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Region          443..503
                     /region_name="FG-GAP 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11215.2)"
     Region          453..509
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Site            469
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Region          506..564
                     /region_name="FG-GAP 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11215.2)"
     Region          516..562
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          569..629
                     /region_name="FG-GAP 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P11215.2)"
     Region          615..978
                     /region_name="Integrin_alpha2"
                     /note="Integrin alpha; pfam08441"
                     /db_xref="CDD:462478"
     Site            692
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            696
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            734
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            801
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            880
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            900
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            911
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            940
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            946
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            978
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            993
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            1021
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            1044
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            1050
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            1075
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11215.2)"
     Site            1105..1128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11215.2)"
     Region          1129..1143
                     /region_name="Integrin_alpha"
                     /note="Integrin alpha cytoplasmic region; pfam00357"
                     /db_xref="CDD:459778"
     Region          1131..1135
                     /region_name="GFFKR motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P11215.2)"
     CDS             1..1152
                     /gene="ITGAM"
                     /gene_synonym="CD11B; CR3A; MAC-1; MAC1A; MO1A; SLEB6"
                     /coded_by="NM_000632.4:91..3549"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS45470.1"
                     /db_xref="GeneID:3684"
                     /db_xref="HGNC:HGNC:6149"
                     /db_xref="MIM:120980"
ORIGIN      
        1 malrvlllta ltlchgfnld tenamtfqen argfgqsvvq lqgsrvvvga pqeivaanqr
       61 gslyqcdyst gscepirlqv pveavnmslg lslaattspp qllacgptvh qtcsentyvk
      121 glcflfgsnl rqqpqkfpea lrgcpqedsd iaflidgsgs iiphdfrrmk efvstvmeql
      181 kksktlfslm qyseefrihf tfkefqnnpn prslvkpitq llgrthtatg irkvvrelfn
      241 itngarknaf kilvvitdge kfgdplgyed vipeadregv iryvigvgda frseksrqel
      301 ntiaskpprd hvfqvnnfea lktiqnqlre kifaiegtqt gssssfehem sqegfsaait
      361 sngpllstvg sydwaggvfl ytskekstfi nmtrvdsdmn daylgyaaai ilrnrvqslv
      421 lgapryqhig lvamfrqntg mwesnanvkg tqigayfgas lcsvdvdsng stdlvligap
      481 hyyeqtrggq vsvcplprgr arwqcdavly geqgqpwgrf gaaltvlgdv ngdkltdvai
      541 gapgeednrg avylfhgtsg sgispshsqr iagsklsprl qyfgqslsgg qdltmdglvd
      601 ltvgaqghvl llrsqpvlrv kaimefnpre varnvfecnd qvvkgkeage vrvclhvqks
      661 trdrlregqi qsvvtydlal dsgrphsrav fnetknstrr qtqvlgltqt cetlklqlpn
      721 ciedpvspiv lrlnfslvgt plsafgnlrp vlaedaqrlf talfpfeknc gndnicqddl
      781 sitfsfmsld clvvggpref nvtvtvrndg edsyrtqvtf ffpldlsyrk vstlqnqrsq
      841 rswrlacesa sstevsgalk stscsinhpi fpensevtfn itfdvdskas lgnklllkan
      901 vtsennmprt nktefqlelp vkyavymvvt shgvstkyln ftasentsrv mqhqyqvsnl
      961 gqrslpislv flvpvrlnqt viwdrpqvtf senlsstcht kerlpshsdf laelrkapvv
     1021 ncsiavcqri qcdipffgiq eefnatlkgn lsfdwyikts hnhllivsta eilfndsvft
     1081 llpgqgafvr sqtetkvepf evpnplpliv gssvggllll alitaalykl gffkrqykdm
     1141 mseggppgae pq
//
LOCUS       NP_001346256             261 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 106A [Mus musculus].
ACCESSION   NP_001346256
VERSION     NP_001346256.1
DBSOURCE    REFSEQ: accession NM_001359327.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Zhang,X., Feng,T., Zhou,X., Sullivan,P.M., Hu,F., Lou,Y., Yu,J.,
            Feng,J., Liu,H. and Chen,Y.
  TITLE     Inactivation of TMEM106A promotes lipopolysaccharide-induced
            inflammation via the MAPK and NF-kappaB signaling pathways in
            macrophages
  JOURNAL   Clin Exp Immunol 203 (1), 125-136 (2021)
   PUBMED   33006758
  REMARK    GeneRIF: Inactivation of TMEM106A promotes
            lipopolysaccharide-induced inflammation via the MAPK and NF-kappaB
            signaling pathways in macrophages.
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Dai,H., Xu,D., Su,J., Jang,J. and Chen,Y.
  TITLE     Transmembrane protein 106a activates mouse peritoneal macrophages
            via the MAPK and NF-kappaB signaling pathways
  JOURNAL   Sci Rep 5, 12461 (2015)
   PUBMED   26215746
  REMARK    GeneRIF: data suggest that mouse Tmem106a might be a new trigger of
            macrophage activation and have some influence toward the M1 state
            through the activation of the MAPKs and NF-kappaB pathway
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Abdallah,B.M., Ditzel,N., Mahmood,A., Isa,A., Traustadottir,G.A.,
            Schilling,A.F., Ruiz-Hidalgo,M.J., Laborda,J., Amling,M. and
            Kassem,M.
  TITLE     DLK1 is a novel regulator of bone mass that mediates estrogen
            deficiency-induced bone loss in mice
  JOURNAL   J Bone Miner Res 26 (7), 1457-1471 (2011)
   PUBMED   21308776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY199928.1, AK150285.1 and AK149650.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR,
            compared to variant 1. Variants 1 through 4 encode the same
            protein.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849374,
                              SAMN00849375 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 65.44 cM"
     Protein         1..261
                     /product="transmembrane protein 106A"
                     /calculated_mol_wt=28978
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC04.1)"
     Region          24..251
                     /region_name="DUF1356"
                     /note="Protein of unknown function (DUF1356); pfam07092"
                     /db_xref="CDD:462088"
     Site            93..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC04.1)"
     CDS             1..261
                     /gene="Tmem106a"
                     /gene_synonym="0610008L10Rik"
                     /coded_by="NM_001359327.1:166..951"
                     /db_xref="CCDS:CCDS25476.1"
                     /db_xref="GeneID:217203"
                     /db_xref="MGI:MGI:1922056"
ORIGIN      
        1 mgkavsqlts rkdedkpilp dnpamasqaa nyfstgsskp ahscmpyeka asssfvtcpt
       61 cqgngeipqe qekqlvalip ygdqrlkprr tklfvflsva icllifslti fflyprpiav
      121 rpvglnsstv tfedahvqln ttnvlnifns nfypitvtql taevlhqasv vgqvtsslrl
      181 higplaseqm pyevasrild entykictwp kirvhhilln iqgsltcsfl shpqqlpfes
      241 feyvdcrenm slphlelprp a
//
LOCUS       NP_689603                297 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 178A isoform 1 precursor [Homo sapiens].
ACCESSION   NP_689603
VERSION     NP_689603.2
DBSOURCE    REFSEQ: accession NM_152390.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Decker,C.E., Yang,Z., Rimer,R., Park-Min,K.H., Macaubas,C.,
            Mellins,E.D., Novack,D.V. and Faccio,R.
  TITLE     Tmem178 acts in a novel negative feedback loop targeting NFATc1 to
            regulate bone mass
  JOURNAL   Proc Natl Acad Sci U S A 112 (51), 15654-15659 (2015)
   PUBMED   26644563
  REMARK    GeneRIF: Tmem178 localizes to the ER membrane and regulates
            RANKL-induced Ca(2+) fluxes, thus controlling NFATc1 induction
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN993805.1, BC029530.1 and AC007246.3.
            
            On Nov 25, 2009 this sequence version replaced NP_689603.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029530.1, AK075440.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281961.3/ ENSP00000281961.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.1"
     Protein         1..297
                     /product="transmembrane protein 178A isoform 1 precursor"
                     /note="transmembrane protein 178"
                     /calculated_mol_wt=30508
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NBL3.1)"
                     /calculated_mol_wt=2529
     mat_peptide     26..297
                     /product="Transmembrane protein 178A. /id=PRO_0000287280"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBL3.1)"
                     /calculated_mol_wt=30508
     Region          41..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBL3.1)"
     Region          106..274
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NBL3.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBL3.1)"
     Site            209..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBL3.1)"
     Site            258..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBL3.1)"
     CDS             1..297
                     /gene="TMEM178A"
                     /gene_synonym="TMEM178"
                     /coded_by="NM_152390.3:59..952"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1804.1"
                     /db_xref="GeneID:130733"
                     /db_xref="HGNC:HGNC:28517"
ORIGIN      
        1 mepralvtal slglslcslg llvtaiftdh wyetdprrhk escersraga dppdqknrlm
       61 plshlplrds pplgrrllpg gpgradpesw rsllglggld aecgrplfat ysglwrkcyf
      121 lgidrdidtl ilkgiaqrct aikyhfsqpi rlrnipfnlt ktiqqdewhl lhlrritagf
      181 lgmavavllc gcivatvsff weesltqhva gllflmtgif ctislctyaa sisydlnrlp
      241 kliyslpadv ehgyswsifc awcslgfiva agglciaypf isrtkiaqlk sgrdstv
//
LOCUS       NP_005584                255 aa            linear   PRI 27-APR-2025
DEFINITION  myogenic factor 5 [Homo sapiens].
ACCESSION   NP_005584
VERSION     NP_005584.2
DBSOURCE    REFSEQ: accession NM_005593.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Ocieczek,P., Oluonye,N., Mejecase,C., Schiff,E., Tailor,V. and
            Moosajee,M.
  TITLE     Identification of a Novel Frameshift Variant in MYF5 Leading to
            External Ophthalmoplegia with Rib and Vertebral Anomalies
  JOURNAL   Genes (Basel) 15 (6), 699 (2024)
   PUBMED   38927634
  REMARK    GeneRIF: Identification of a Novel Frameshift Variant in MYF5
            Leading to External Ophthalmoplegia with Rib and Vertebral
            Anomalies.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Di Gioia,S.A., Shaaban,S., Tuysuz,B., Elcioglu,N.H., Chan,W.M.,
            Robson,C.D., Ecklund,K., Gilette,N.M., Hamzaoglu,A., Tayfun,G.A.,
            Traboulsi,E.I. and Engle,E.C.
  TITLE     Recessive MYF5 Mutations Cause External Ophthalmoplegia, Rib, and
            Vertebral Anomalies
  JOURNAL   Am J Hum Genet 103 (1), 115-124 (2018)
   PUBMED   29887215
  REMARK    GeneRIF: The direct role of MYF5 in rib, spine, and extraocular
            muscle formation in humans.
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Skrzypek,K., Kusienicka,A., Trzyna,E., Szewczyk,B., Ulman,A.,
            Konieczny,P., Adamus,T., Badyra,B., Kortylewski,M. and Majka,M.
  TITLE     SNAIL is a key regulator of alveolar rhabdomyosarcoma tumor growth
            and differentiation through repression of MYF5 and MYOD function
  JOURNAL   Cell Death Dis 9 (6), 643 (2018)
   PUBMED   29844345
  REMARK    GeneRIF: SNAIL silencing allows the re-expression of MYF5 and
            canonical MYOD binding, promoting alveolar rhabdomyosarcoma cell
            myogenic differentiation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Tenente,I.M., Hayes,M.N., Ignatius,M.S., McCarthy,K., Yohe,M.,
            Sindiri,S., Gryder,B., Oliveira,M.L., Ramakrishnan,A., Tang,Q.,
            Chen,E.Y., Petur Nielsen,G., Khan,J. and Langenau,D.M.
  TITLE     Myogenic regulatory transcription factors regulate growth in
            rhabdomyosarcoma
  JOURNAL   Elife 6, e19214 (2017)
   PUBMED   28080960
  REMARK    GeneRIF: Analysis of human rhabdomyosarcoma revealed that MYF5 and
            MYOD are mutually-exclusively expressed and each is required for
            sustained tumor growth.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Chen,C.M., Kraut,N., Groudine,M. and Weintraub,H.
  TITLE     I-mf, a novel myogenic repressor, interacts with members of the
            MyoD family
  JOURNAL   Cell 86 (5), 731-741 (1996)
   PUBMED   8797820
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Dechesne,C.A., Wei,Q., Eldridge,J., Gannoun-Zaki,L., Millasseau,P.,
            Bougueleret,L., Caterina,D. and Paterson,B.M.
  TITLE     E-box- and MEF-2-independent muscle-specific expression, positive
            autoregulation, and cross-activation of the chicken MyoD (CMD1)
            promoter reveal an indirect regulatory pathway
  JOURNAL   Mol Cell Biol 14 (8), 5474-5486 (1994)
   PUBMED   8035824
REFERENCE   8  (residues 1 to 255)
  AUTHORS   Braun,T., Winter,B., Bober,E. and Arnold,H.H.
  TITLE     Transcriptional activation domain of the muscle-specific
            gene-regulatory protein myf5
  JOURNAL   Nature 346 (6285), 663-665 (1990)
   PUBMED   2385294
REFERENCE   9  (residues 1 to 255)
  AUTHORS   Braun,T., Bober,E., Winter,B., Rosenthal,N. and Arnold,H.H.
  TITLE     Myf-6, a new member of the human gene family of myogenic
            determination factors: evidence for a gene cluster on chromosome 12
  JOURNAL   EMBO J 9 (3), 821-831 (1990)
   PUBMED   2311584
REFERENCE   10 (residues 1 to 255)
  AUTHORS   Braun,T., Buschhausen-Denker,G., Bober,E., Tannich,E. and
            Arnold,H.H.
  TITLE     A novel human muscle factor related to but distinct from MyoD1
            induces myogenic conversion in 10T1/2 fibroblasts
  JOURNAL   EMBO J 8 (3), 701-709 (1989)
   PUBMED   2721498
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025568.25, BP231293.1, X14894.1, BC069373.1 and BX089431.1.
            
            On Aug 17, 2007 this sequence version replaced NP_005584.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X14894.1, BC069373.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158800, SAMEA2162946
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000228644.4/ ENSP00000228644.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.31"
     Protein         1..255
                     /product="myogenic factor 5"
                     /note="myf-5; class C basic helix-loop-helix protein 2"
                     /calculated_mol_wt=28165
     Region          1..88
                     /region_name="BASIC"
                     /note="Basic domain in HLH proteins of MYOD family;
                     smart00520"
                     /db_xref="CDD:128794"
     Region          83..146
                     /region_name="bHLH_TS_Myf5"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     myogenic factor 5 (Myf-5) and similar proteins; cd18937"
                     /db_xref="CDD:381507"
     Site            order(84..85,89,91..93,95,100,117..120)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381507"
     Site            order(98..99,102..103,105..106,121,124,128,130..131,135,
                     137..138)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381507"
     Region          143..214
                     /region_name="Myf5"
                     /note="Myogenic determination factor 5; pfam12232"
                     /db_xref="CDD:463500"
     CDS             1..255
                     /gene="MYF5"
                     /gene_synonym="bHLHc2; EORVA"
                     /coded_by="NM_005593.3:153..920"
                     /db_xref="CCDS:CCDS9020.1"
                     /db_xref="GeneID:4617"
                     /db_xref="HGNC:HGNC:7565"
                     /db_xref="MIM:159990"
ORIGIN      
        1 mdvmdgcqfs pseyfydgsc ipspegefgd efvprvaafg ahkaelqgsd edehvraptg
       61 hhqaghclmw ackackrkst tmdrrkaatm rerrrlkkvn qafetlkrct ttnpnqrlpk
      121 veilrnairy ieslqellre qvenyyslpg qscseptspt sncsdgmpec nspvwsrkss
      181 tfdsiycpdv snvyatdkns lssldclsni vdritsseqp glplqdlasl spvastdsqp
      241 atpgasssrl iyhvl
//
LOCUS       NP_001355320             643 aa            linear   ROD 27-APR-2025
DEFINITION  SURP and G-patch domain-containing protein 1 [Mus musculus].
ACCESSION   NP_001355320 XP_006509801
VERSION     NP_001355320.1
DBSOURCE    REFSEQ: accession NM_001368391.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Benbarche,S., Pineda,J.M.B., Galvis,L.B., Biswas,J., Liu,B.,
            Wang,E., Zhang,Q., Hogg,S.J., Lyttle,K., Dahi,A., Lewis,A.M.,
            Sarchi,M., Rahman,J., Fox,N., Ai,Y., Mehta,S., Garippa,R.,
            Ortiz-Pacheco,J., Li,Z., Monetti,M., Stanley,R.F., Doulatov,S.,
            Bradley,R.K. and Abdel-Wahab,O.
  TITLE     GPATCH8 modulates mutant SF3B1 mis-splicing and pathogenicity in
            hematologic malignancies
  JOURNAL   Mol Cell 84 (10), 1886-1903 (2024)
   PUBMED   38688280
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Kim,M.J., Yu,C.Y., Theusch,E., Naidoo,D., Stevens,K., Kuang,Y.L.,
            Schuetz,E., Chaudhry,A.S. and Medina,M.W.
  TITLE     SUGP1 is a novel regulator of cholesterol metabolism
  JOURNAL   Hum Mol Genet 25 (14), 3106-3116 (2016)
   PUBMED   27206982
  REMARK    GeneRIF: Our results strongly support a role for SUGP1 as a novel
            regulator of cholesterol metabolism and suggest that it contributes
            to the relationship between rs10401969 and plasma cholesterol
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Sampson,N.D. and Hewitt,J.E.
  TITLE     SF4 and SFRS14, two related putative splicing factors on human
            chromosome 19p13.11
  JOURNAL   Gene 305 (1), 91-100 (2003)
   PUBMED   12594045
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC167132.12.
            
            On Feb 9, 2019 this sequence version replaced XP_006509801.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.56529.1,
                                           SRR13861859.1119118.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 34.15 cM"
     Protein         1..643
                     /product="SURP and G-patch domain-containing protein 1"
                     /note="splicing factor 4"
                     /calculated_mol_wt=72518
     Region          48..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          97..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWZ8; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          186..237
                     /region_name="Surp"
                     /note="Surp module; pfam01805"
                     /db_xref="CDD:460339"
     Region          187..229
                     /region_name="SURP motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWZ8; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          261..312
                     /region_name="Surp"
                     /note="Surp module; pfam01805"
                     /db_xref="CDD:460339"
     Region          262..305
                     /region_name="SURP motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          293..>416
                     /region_name="kgd"
                     /note="multifunctional oxoglutarate
                     decarboxylase/oxoglutarate dehydrogenase thiamine
                     pyrophosphate-binding subunit/dihydrolipoyllysine-residue
                     succinyltransferase subunit; cl39092"
                     /db_xref="CDD:476867"
     Region          316..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWZ8; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          360..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          378..384
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWZ8; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          561..605
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     CDS             1..643
                     /gene="Sugp1"
                     /gene_synonym="5730496N02Rik; Sf4"
                     /coded_by="NM_001368391.1:118..2049"
                     /db_xref="CCDS:CCDS22356.1"
                     /db_xref="GeneID:70616"
                     /db_xref="MGI:MGI:1917866"
ORIGIN      
        1 mslkmdnrdv agkanrwfgm aqpksgkmnm nilhqeelia qkkreiearm eqkarqshvp
       61 spqpphpgei adahnscisn kfandgsflq qflklqkaqt stdsaprapp smptpsslkk
      121 plvlskrtgl glssptgpvk nyshakqlpv ahrpsvfqsp dddeeedyeq wleikvsppe
      181 gaetrrviek larfvaeggp elekvamedy kdnpaftflh dknsreflyy rrkvaeirke
      241 aqkpqaatqk vsppedeeak nlaeklarfi adggpeveti alqnnrenqa fsflydpnsq
      301 gyryyrqkld efrkakagst gsfpapapnp slrrksapea lsgavppita cptpvapapa
      361 vnptpsipgk ptataavkrk rksrwgpeed kvelppaela qrdidaspsp lsvqdlkglg
      421 yekgkpvglv gvtelsdaqk kqlkeqqemq qmydmimqhk ramqdmqllw ekalqqhqhg
      481 ydsdeevdse lgtwehqlrr memdktrewa eqltqmgrgk hfigdflppd elekfmetfk
      541 alkegrepdy seykefkltv enigyqmlmk mgwkegeglg tegqgiknpv nkgattidga
      601 gfgidrpael skeddeyeaf rkrmmlayrf rpnplnnprr pyy
//
LOCUS       NP_001348574             193 aa            linear   ROD 27-APR-2025
DEFINITION  hippocalcin-like protein 1 [Mus musculus].
ACCESSION   NP_001348574 XP_006515219
VERSION     NP_001348574.1
DBSOURCE    REFSEQ: accession NM_001361645.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Chen,T., Yuan,Z., Lei,Z., Duan,J., Xue,J., Lu,T., Yan,G., Zhang,L.,
            Liu,Y., Li,Q. and Zhang,Y.
  TITLE     Hippocalcin-Like 1 blunts liver lipid metabolism to suppress
            tumorigenesis via directly targeting RUVBL1-mTOR signaling
  JOURNAL   Theranostics 12 (17), 7450-7464 (2022)
   PUBMED   36438486
  REMARK    GeneRIF: Hippocalcin-Like 1 blunts liver lipid metabolism to
            suppress tumorigenesis via directly targeting RUVBL1-mTOR
            signaling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Li,H., Bishop,K.M. and O'Leary,D.D.
  TITLE     Potential target genes of EMX2 include Odz/Ten-M and other gene
            families with implications for cortical patterning
  JOURNAL   Mol Cell Neurosci 33 (2), 136-149 (2006)
   PUBMED   16919471
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Oikawa,K., Kimura,S., Aoki,N., Atsuta,Y., Takiyama,Y., Nagato,T.,
            Yanai,M., Kobayashi,H., Sato,K., Sasajima,T. and Tateno,M.
  TITLE     Neuronal calcium sensor protein visinin-like protein-3 interacts
            with microsomal cytochrome b5 in a Ca2+-dependent manner
  JOURNAL   J Biol Chem 279 (15), 15142-15152 (2004)
   PUBMED   14739275
  REMARK    GeneRIF: visinin-like protein-3 interacts with microsomal
            cytochrome b5 in a Ca2+-dependent manner
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Kannan,K., Kaminski,N., Rechavi,G., Jakob-Hirsch,J., Amariglio,N.
            and Givol,D.
  TITLE     DNA microarray analysis of genes involved in p53 mediated
            apoptosis: activation of Apaf-1
  JOURNAL   Oncogene 20 (26), 3449-3455 (2001)
   PUBMED   11423996
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138342.11 and AC154636.2.
            
            On Mar 29, 2018 this sequence version replaced XP_006515219.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.328041.1,
                                           SRR7345562.1283833.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 8.13 cM"
     Protein         1..193
                     /product="hippocalcin-like protein 1"
                     /note="neural visinin-like protein 3"
                     /calculated_mol_wt=22207
     Region          21..175
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..193
                     /gene="Hpcal1"
                     /gene_synonym="NVL-3; NVP-3; Nvp3; VILIP3; Vnsl3; Vsnl3"
                     /coded_by="NM_001361645.1:349..930"
                     /db_xref="CCDS:CCDS25830.1"
                     /db_xref="GeneID:53602"
                     /db_xref="MGI:MGI:1855689"
ORIGIN      
        1 mgkqnsklrp evlqdlreht eftdhelqew ykgflkdcpt ghltvdefkk iyanffpygd
       61 askfaehvfr tfdtnsdgti dfrefiials vtsrgkleqk lkwafsmydl dgngyisrse
      121 mleivqaiyk mvssvmkmpe destpekrtd kifrqmdtnn dgklsleefi kgaksdpsiv
      181 rllqcdpssa sqf
//
LOCUS       NP_079457                523 aa            linear   PRI 27-APR-2025
DEFINITION  solute carrier family 35 member F5 isoform 1 [Homo sapiens].
ACCESSION   NP_079457
VERSION     NP_079457.2
DBSOURCE    REFSEQ: accession NM_025181.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC017074.9 and AY358620.1.
            
            On Jun 10, 2002 this sequence version replaced NP_079457.1.
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.180419.1,
                                           SRR1660807.75915.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000245680.7/ ENSP00000245680.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.1"
     Protein         1..523
                     /product="solute carrier family 35 member F5 isoform 1"
                     /note="HCV NS5A-transactivated protein 3; hepatitis C
                     virus NS5A-transactivated protein 3"
                     /calculated_mol_wt=58756
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV83.1)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV83.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WV83.1)"
     Region          230..470
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
     Site            243..263
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV83.1)"
     Site            268..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV83.1)"
     Site            296..316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV83.1)"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV83.1)"
     Site            361..381
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV83.1)"
     Site            395..415
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV83.1)"
     Site            420..440
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV83.1)"
     Site            452..472
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV83.1)"
     CDS             1..523
                     /gene="SLC35F5"
                     /coded_by="NM_025181.5:234..1805"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2119.1"
                     /db_xref="GeneID:80255"
                     /db_xref="HGNC:HGNC:23617"
                     /db_xref="MIM:619997"
ORIGIN      
        1 mvpprrhrga grpgvlsssp pfrlrsakfs gialedlrra lktrlqmvcv fvmnrmnsqn
       61 sgftqrrrma lgivilllvd viwvasselt syvftqynkp ffstfaktsm fvlyllgfii
      121 wkpwrqqctr glrgkhaaff adaegyfaac ttdttmnssl seplyvpvkf hdlpsekpes
      181 tnidtektpk ksrvrfsnim eirqlpssha leaklsrmsy pvkeqesilk tvgkltatqv
      241 akisfffcfv wflanlsyqe alsdtqvaiv nilsstsglf tlilaavfps nsgdrftlsk
      301 llavilsigg vvlvnlagse kpagrdtvgs iwslagamly avyivmikrk vdredkldip
      361 mffgfvglfn llllwpgffl lhytgfedfe fpnkvvlmci iingligtvl seflwlwgcf
      421 ltssligtla lsltiplsii admcmqkvqf swlffagaip vffsffivtl lchynnwdpv
      481 mvgirrifaf icrkhriqrv pedseqcesl ismhsvsqed gas
//
LOCUS       NP_006278                304 aa            linear   PRI 27-APR-2025
DEFINITION  tissue factor pathway inhibitor isoform a precursor [Homo sapiens].
ACCESSION   NP_006278
VERSION     NP_006278.1
DBSOURCE    REFSEQ: accession NM_006287.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Sletten,M., Skogstrom,K.B., Lind,S.M., Tinholt,M., Stavik,B.,
            Rayner,S. and Iversen,N.
  TITLE     Elevated TFPI is a prognostic factor in hepatocellular carcinoma:
            Putative role of miR-7-5p and miR-1236-3p
  JOURNAL   Thromb Res 241, 109073 (2024)
   PUBMED   38945092
  REMARK    GeneRIF: Elevated TFPI is a prognostic factor in hepatocellular
            carcinoma: Putative role of miR-7-5p and miR-1236-3p.
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Wang,B., Fan,X., Wang,L. and Wei,X.
  TITLE     The RNA-binding protein sorbin and SH3 domain-containing 2 are
            transcriptionally regulated by specificity protein 1 and function
            as tumor suppressors in bladder cancer by stabilizing tissue factor
            pathway inhibitor
  JOURNAL   Mol Carcinog 63 (6), 1174-1187 (2024)
   PUBMED   38501385
  REMARK    GeneRIF: The RNA-binding protein sorbin and SH3 domain-containing 2
            are transcriptionally regulated by specificity protein 1 and
            function as tumor suppressors in bladder cancer by stabilizing
            tissue factor pathway inhibitor.
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Li,X., Song,X., Mahmood,D.F.D., Sim,M.M.S., Bidarian,S.J. and
            Wood,J.P.
  TITLE     Activated protein C, protein S, and tissue factor pathway inhibitor
            cooperate to inhibit thrombin activation
  JOURNAL   Thromb Res 230, 84-93 (2023)
   PUBMED   37660436
  REMARK    GeneRIF: Activated protein C, protein S, and tissue factor pathway
            inhibitor cooperate to inhibit thrombin activation.
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Wittig,J., Drekolia,M.K., Kyselova,A., Delgado Lagos,F.,
            Bochenek,M.L., Hu,J., Schafer,K., Fleming,I. and Bibli,S.I.
  TITLE     Endothelial-dependent S-Sulfhydration of tissue factor pathway
            inhibitor regulates blood coagulation
  JOURNAL   Redox Biol 62, 102694 (2023)
   PUBMED   37030150
  REMARK    GeneRIF: Endothelial-dependent S-Sulfhydration of tissue factor
            pathway inhibitor regulates blood coagulation.
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Mast,A.E.
  TITLE     Tissue Factor Pathway Inhibitor: Multiple Anticoagulant Activities
            for a Single Protein
  JOURNAL   Arterioscler Thromb Vasc Biol 36 (1), 9-14 (2016)
   PUBMED   26603155
  REMARK    Review article
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Maroney,S.A., Ellery,P.E. and Mast,A.E.
  TITLE     Alternatively spliced isoforms of tissue factor pathway inhibitor
  JOURNAL   Thromb Res 125 Suppl 1, S52-S56 (2010)
   PUBMED   20176395
  REMARK    Review article
            Erratum:[Thromb Res. 2010 Oct;126(4):361]
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Van der Logt,C.P., Kluck,P.M., Wiegant,J., Landegent,J.E. and
            Reitsma,P.H.
  TITLE     Refined regional assignment of the human tissue factor pathway
            inhibitor (TFPI) gene to chromosome band 2q32 by non-isotopic in
            situ hybridization
  JOURNAL   Hum Genet 89 (5), 577-578 (1992)
   PUBMED   1353057
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Higuchi,D.A., Wun,T.C., Likert,K.M. and Broze,G.J. Jr.
  TITLE     The effect of leukocyte elastase on tissue factor pathway inhibitor
  JOURNAL   Blood 79 (7), 1712-1719 (1992)
   PUBMED   1558967
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Girard,T.J., Eddy,R., Wesselschmidt,R.L., MacPhail,L.A.,
            Likert,K.M., Byers,M.G., Shows,T.B. and Broze,G.J. Jr.
  TITLE     Structure of the human lipoprotein-associated coagulation inhibitor
            gene. Intro/exon gene organization and localization of the gene to
            chromosome 2
  JOURNAL   J Biol Chem 266 (8), 5036-5041 (1991)
   PUBMED   2002045
REFERENCE   10 (residues 1 to 304)
  AUTHORS   van der Logt,C.P., Reitsma,P.H. and Bertina,R.M.
  TITLE     Intron-exon organization of the human gene coding for the
            lipoprotein-associated coagulation inhibitor: the factor Xa
            dependent inhibitor of the extrinsic pathway of coagulation
  JOURNAL   Biochemistry 30 (6), 1571-1577 (1991)
   PUBMED   1993173
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY175080.1, J03225.1,
            AC007319.2 and CA418214.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a Kunitz-type serine protease inhibitor
            that regulates the tissue factor (TF)-dependent pathway of blood
            coagulation. The coagulation process initiates with the formation
            of a factor VIIa-TF complex, which proteolytically activates
            additional proteases (factors IX and X) and ultimately leads to the
            formation of a fibrin clot. The product of this gene inhibits the
            activated factor X and VIIa-TF proteases in an autoregulatory loop.
            Inhibition of the encoded protein restores hemostasis in animal
            models of hemophilia. This gene encodes multiple protein isoforms
            that differ in their inhibitory activity, specificity and cellular
            localization. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform (a,
            also known as TFPIalpha), which is secreted. Variants 1 and 4-6
            encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.23742.1,
                                           SRR1803616.170461.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000233156.9/ ENSP00000233156.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.1"
     Protein         1..304
                     /product="tissue factor pathway inhibitor isoform a
                     precursor"
                     /note="anti-convertin; extrinsic pathway inhibitor; tissue
                     factor pathway inhibitor (lipoprotein-associated
                     coagulation inhibitor)"
                     /calculated_mol_wt=31951
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3083
     mat_peptide     29..304
                     /product="Tissue factor pathway inhibitor.
                     /evidence=ECO:0000269|PubMed:2452157. /id=PRO_0000016871"
                     /note="propagated from UniProtKB/Swiss-Prot (P10646.1)"
                     /calculated_mol_wt=31951
     Site            42
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine, partial.
                     /evidence=ECO:0000269|PubMed:19017259; propagated from
                     UniProtKB/Swiss-Prot (P10646.1)"
     Region          51..105
                     /region_name="Kunitz_TFPI1_1-like"
                     /note="Kunitz protease inhibitor (KPI) domain 1 (KPI-1 or
                     K1) of tissue factor pathway inhibitor (TFPI); cd22613"
                     /db_xref="CDD:438656"
     Site            order(52..53,63,65,67,69,84..91,93..96,99,102..103)
                     /site_type="other"
                     /note="antibody binding site [polypeptide binding]"
                     /db_xref="CDD:438656"
     Site            order(60..69,83..88,93)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438656"
     Site            64..65
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P10646.1)"
     Region          121..176
                     /region_name="Kunitz_TFPI1_2-like"
                     /note="Kunitz protease inhibitor (KPI) domain 2 (KPI-2 or
                     K2) of tissue factor pathway inhibitor (TFPI); cd22614"
                     /db_xref="CDD:438657"
     Site            order(133..137,156,158..159)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438657"
     Site            135..136
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P10646.1)"
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19017259, ECO:0000269|PubMed:8639592;
                     propagated from UniProtKB/Swiss-Prot (P10646.1)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19017259,
                     ECO:0000269|PubMed:8639592; propagated from
                     UniProtKB/Swiss-Prot (P10646.1)"
     Site            202
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine, partial.
                     /evidence=ECO:0000269|PubMed:19017259,
                     ECO:0000269|PubMed:8639592; propagated from
                     UniProtKB/Swiss-Prot (P10646.1)"
     Site            203
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19017259,
                     ECO:0000269|PubMed:8639592; propagated from
                     UniProtKB/Swiss-Prot (P10646.1)"
     Region          214..267
                     /region_name="Kunitz_TFPI1_TFPI2_3-like"
                     /note="Kunitz protease inhibitor (KPI) domain 3 (KPI-3 or
                     K3) of tissue factor pathway inhibitor (TFPI) and TFPI2,
                     and similar proteins; cd22615"
                     /db_xref="CDD:438658"
     Site            227..228
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P10646.1)"
     Site            256
                     /site_type="other"
                     /note="Not glycosylated; propagated from
                     UniProtKB/Swiss-Prot (P10646.1)"
     CDS             1..304
                     /gene="TFPI"
                     /gene_synonym="EPI; LACI; TFI; TFPI1"
                     /coded_by="NM_006287.6:239..1153"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2294.1"
                     /db_xref="GeneID:7035"
                     /db_xref="HGNC:HGNC:11760"
                     /db_xref="MIM:152310"
ORIGIN      
        1 miytmkkvha lwasvcllln lapaplnads eedeehtiit dtelpplklm hsfcafkadd
       61 gpckaimkrf ffniftrqce efiyggcegn qnrfesleec kkmctrdnan riikttlqqe
      121 kpdfcfleed pgicrgyitr yfynnqtkqc erfkyggclg nmnnfetlee cknicedgpn
      181 gfqvdnygtq lnavnnsltp qstkvpslfe fhgpswcltp adrglcrane nrfyynsvig
      241 kcrpfkysgc ggnennftsk qeclrackkg fiqriskggl iktkrkrkkq rvkiayeeif
      301 vknm
//
LOCUS       NP_001344223             257 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF170 isoform 1 [Mus musculus].
ACCESSION   NP_001344223 XP_006509278
VERSION     NP_001344223.2
DBSOURCE    REFSEQ: accession NM_001357294.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Song,X., Liu,S., Wang,W., Ma,Z., Cao,X. and Jiang,M.
  TITLE     E3 ubiquitin ligase RNF170 inhibits innate immune responses by
            targeting and degrading TLR3 in murine cells
  JOURNAL   Cell Mol Immunol 17 (8), 865-874 (2020)
   PUBMED   31076723
  REMARK    GeneRIF: E3 ubiquitin ligase RNF170 inhibits innate immune
            responses by targeting and degrading TLR3 in murine cells.
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Kim,Y., Kim,S.H., Kim,K.H., Chae,S., Kim,C., Kim,J., Shin,H.S.,
            Lee,M.S. and Kim,D.
  TITLE     Age-dependent gait abnormalities in mice lacking the Rnf170 gene
            linked to human autosomal-dominant sensory ataxia
  JOURNAL   Hum Mol Genet 24 (25), 7196-7206 (2015)
   PUBMED   26433933
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Lu,J.P., Wang,Y., Sliter,D.A., Pearce,M.M. and Wojcikiewicz,R.J.
  TITLE     RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase,
            mediates inositol 1,4,5-trisphosphate receptor ubiquitination and
            degradation
  JOURNAL   J Biol Chem 286 (27), 24426-24433 (2011)
   PUBMED   21610068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093366.9.
            
            On May 14, 2019 this sequence version replaced NP_001344223.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.1509473.1,
                                           SRR7974084.29095.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 14.38 cM"
     Protein         1..257
                     /product="E3 ubiquitin-protein ligase RNF170 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF170; RING-type E3
                     ubiquitin transferase RNF170"
                     /calculated_mol_wt=29687
     Region          84..139
                     /region_name="RING-HC_RNF170"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 170 (RNF170) and similar proteins; cd16553"
                     /db_xref="CDD:438215"
     Region          203..238
                     /region_name="DUF1232"
                     /note="Protein of unknown function (DUF1232); pfam06803"
                     /db_xref="CDD:462011"
     CDS             1..257
                     /gene="Rnf170"
                     /gene_synonym="6720407G21Rik"
                     /coded_by="NM_001357294.2:467..1240"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS22207.1"
                     /db_xref="GeneID:77733"
                     /db_xref="MGI:MGI:1924983"
ORIGIN      
        1 maryysegqs lqqddsfieg vsdqvlvavv vslaltatll yallrnvqqn ihpenqelvr
       61 vlreqfqteq dvpaparqqf ytemycpicl hqasfpvetn cghlfcgsci iaywrygswl
      121 gaiscpicrq tvtllltvfg eddqsqdvir lrqdvndynr rfsgqprsim erimdlptll
      181 rhafrevfsv gglfwmfrir imlclmgaff ylispldfvp ealfgilgfl ddffviflll
      241 iyisimyrev itqrltr
//
LOCUS       NP_001347354             750 aa            linear   ROD 27-APR-2025
DEFINITION  tripartite motif-containing protein 3 isoform c [Mus musculus].
ACCESSION   NP_001347354 XP_006508100
VERSION     NP_001347354.1
DBSOURCE    REFSEQ: accession NM_001360425.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Zuo,Q., Xu,Q., Li,Z., Luo,D., Peng,H. and Duan,Z.
  TITLE     TRIM3 inhibits colorectal cancer cell migration and lipid droplet
            formation by promoting FABP4 degradation
  JOURNAL   Histol Histopathol 39 (2), 239-250 (2024)
   PUBMED   37212515
  REMARK    GeneRIF: TRIM3 inhibits colorectal cancer cell migration and lipid
            droplet formation by promoting FABP4 degradation.
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Dong,W., Luo,B., Qiu,C., Jiang,X., Shen,B., Zhang,L., Liu,W. and
            Zhang,W.
  TITLE     TRIM3 attenuates apoptosis in Parkinson's disease via activating
            PI3K/AKT signal pathway
  JOURNAL   Aging (Albany NY) 13 (1), 735-749 (2020)
   PUBMED   33253119
  REMARK    GeneRIF: TRIM3 attenuates apoptosis in Parkinson's disease via
            activating PI3K/AKT signal pathway.
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Li,W.W., Nie,Y., Yang,Y., Ran,Y., Luo,W.W., Xiong,M.G., Wang,S.Y.,
            Xu,Z.S. and Wang,Y.Y.
  TITLE     Ubiquitination of TLR3 by TRIM3 signals its ESCRT-mediated
            trafficking to the endolysosomes for innate antiviral response
  JOURNAL   Proc Natl Acad Sci U S A 117 (38), 23707-23716 (2020)
   PUBMED   32878999
  REMARK    GeneRIF: Ubiquitination of TLR3 by TRIM3 signals its ESCRT-mediated
            trafficking to the endolysosomes for innate antiviral response.
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Cheung,C.C., Yang,C., Berger,T., Zaugg,K., Reilly,P., Elia,A.J.,
            Wakeham,A., You-Ten,A., Chang,N., Li,L., Wan,Q. and Mak,T.W.
  TITLE     Identification of BERP (brain-expressed RING finger protein) as a
            p53 target gene that modulates seizure susceptibility through
            interacting with GABA(A) receptors
  JOURNAL   Proc Natl Acad Sci U S A 107 (26), 11883-11888 (2010)
   PUBMED   20543135
  REMARK    GeneRIF: brain-expressed RING finger protein (BERP) is a gene whose
            expression is up-regulated in a p53-dependent manner
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Trinidad,J.C., Specht,C.G., Thalhammer,A., Schoepfer,R. and
            Burlingame,A.L.
  TITLE     Comprehensive identification of phosphorylation sites in
            postsynaptic density preparations
  JOURNAL   Mol Cell Proteomics 5 (5), 914-922 (2006)
   PUBMED   16452087
REFERENCE   8  (residues 1 to 750)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   9  (residues 1 to 750)
  AUTHORS   El-Husseini,A.E., Fretier,P. and Vincent,S.R.
  TITLE     Cloning and characterization of a gene (RNF22) encoding a novel
            brain expressed ring finger protein (BERP) that maps to human
            chromosome 11p15.5
  JOURNAL   Genomics 71 (3), 363-367 (2001)
   PUBMED   11170753
REFERENCE   10 (residues 1 to 750)
  AUTHORS   Arama,E., Dickman,D., Kimchie,Z., Shearn,A. and Lev,Z.
  TITLE     Mutations in the beta-propeller domain of the Drosophila brain
            tumor (brat) protein induce neoplasm in the larval brain
  JOURNAL   Oncogene 19 (33), 3706-3716 (2000)
   PUBMED   10949924
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125227.6.
            
            On Feb 3, 2018 this sequence version replaced XP_006508100.1.
            
            Transcript Variant: This variant (5) encodes the longest isoform
            (c).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660825.86219.1,
                                           SRR7974084.20726.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849387, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 55.91 cM"
     Protein         1..750
                     /product="tripartite motif-containing protein 3 isoform c"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 22; tripartite motif protein 3;
                     tripartite motif-containing protein 3; RING finger protein
                     HAC1"
                     /calculated_mol_wt=81412
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O75382; propagated from
                     UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Region          16..63
                     /region_name="RING-HC_TRIM3"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 3 (TRIM3); cd16768"
                     /db_xref="CDD:438424"
     Region          107..159
                     /region_name="Bbox_SF"
                     /note="B-box-type zinc finger superfamily; cl00034"
                     /db_xref="CDD:469587"
     Region          164..290
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Site            order(168,171..172,174..176,179,182,196..197,200,203..204,
                     207..208,211,218..219,222,225..226,229..230,233,243..244,
                     247,251,254..255,258..259,261..262,270,273..274,277,
                     280..281)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467844"
     Region          323..424
                     /region_name="Filamin"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Region          328..425
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          425..470
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Region          477..750
                     /region_name="NHL_TRIM2_like"
                     /note="NHL repeat domain of the tripartite
                     motif-containing protein 2 (TRIM2) and related proteins;
                     cd14960"
                     /db_xref="CDD:271330"
     Region          479..522
                     /region_name="NHL 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Region          495..534
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          526..569
                     /region_name="NHL 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Region          542..581
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          570..611
                     /region_name="NHL 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Region          584..621
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          615..658
                     /region_name="NHL 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Region          628..669
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          662..705
                     /region_name="NHL 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Region          675..717
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          706..749
                     /region_name="NHL 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1R2.1)"
     Region          720..746
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     CDS             1..750
                     /gene="Trim3"
                     /gene_synonym="BERP1; HAC1; Rnf22"
                     /coded_by="NM_001360425.1:231..2483"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="GeneID:55992"
                     /db_xref="MGI:MGI:1860040"
ORIGIN      
        1 makredspgp evqpmdkqfl vcsicldryr cpkvlpclht fcerclqnyi ppqsltlscp
       61 vcrqtsilpe qgvsalqnnf fisslmeamq qapegahdpe dphplsavag rplscpnheg
      121 keplyhqtme fyceacetam cgecragehr ehgtvllrdv veqhkaalqr qleavrgrlp
      181 qlsaaialvg gisqqlqerk aealaqisaa fedleqalqq rkqalvsdle sicgakqkvl
      241 qtqldtlrqg qehigsscsf aeqalrlgsa pevllvrkhm rerlaalaaq afperphena
      301 qlelvlevdg lrrsvlnlga llttsatahe tvatgeglrq alvgqpaslt vttkdkdgrl
      361 vrtgsaelca eitgpdgvrl avpvvdhkng tyelvytart egdlllsvll ygqpvrgspf
      421 rvralrpgdl ppspddvkrr vkspggpgsh vrqkavrrps smystggkrk dnpiedelvf
      481 rvgsrgrekg eftnlqgvsa assgrivvad snnqciqvfs negqfkfrfg vrgrspgqlq
      541 rptgvavdtn gdiivadydn rwvsifspeg kfktkigagr lmgpkgvavd rnghiivvdn
      601 ksccvftfqp ngklvgrfgg rgatdrhfag phfvavnnkn eivvtdfhnh svkvysadge
      661 flfkfgshge gngqfnaptg vavdsngnii vadwgnsriq vfdssgsfls yintsaeply
      721 gpqglaltsd ghvvvadagn hcfkayrylq
//
LOCUS       NP_008826                292 aa            linear   PRI 27-APR-2025
DEFINITION  histamine N-methyltransferase isoform 1 [Homo sapiens].
ACCESSION   NP_008826
VERSION     NP_008826.1
DBSOURCE    REFSEQ: accession NM_006895.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Lu,Y., Dong,C.Z., Bao,D., Zhong,C., Liu,K., Chen,L., Wang,W. and
            Yang,B.
  TITLE     The Thr105Ile Variant (rs11558538) of the Histamine
            N-methyltransferase Gene may be associated with Reduced Risk of
            Parkinson Disease: A Meta-analysis
  JOURNAL   Genet Test Mol Biomarkers 26 (11), 543-549 (2022)
   PUBMED   36378841
  REMARK    GeneRIF: The Thr105Ile Variant (rs11558538) of the Histamine
            N-methyltransferase Gene may be associated with Reduced Risk of
            Parkinson Disease: A Meta-analysis.
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Kuo,K.T., Lin,C.H., Wang,C.H., Pikatan,N.W., Yadav,V.K., Fong,I.H.,
            Yeh,C.T., Lee,W.H. and Huang,W.C.
  TITLE     HNMT Upregulation Induces Cancer Stem Cell Formation and Confers
            Protection against Oxidative Stress through Interaction with HER2
            in Non-Small-Cell Lung Cancer
  JOURNAL   Int J Mol Sci 23 (3), 1663 (2022)
   PUBMED   35163585
  REMARK    GeneRIF: HNMT Upregulation Induces Cancer Stem Cell Formation and
            Confers Protection against Oxidative Stress through Interaction
            with HER2 in Non-Small-Cell Lung Cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Flores-Clemente,C., Nicolas-Vazquez,M.I., Mera Jimenez,E. and
            Hernandez-Rodriguez,M.
  TITLE     Inhibition of Astrocytic Histamine N-Methyltransferase as a
            Possible Target for the Treatment of Alzheimer's Disease
  JOURNAL   Biomolecules 11 (10), 1408 (2021)
   PUBMED   34680041
  REMARK    GeneRIF: Inhibition of Astrocytic Histamine N-Methyltransferase as
            a Possible Target for the Treatment of Alzheimer's Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Chen,Y., Cao,B., Ou,R., Wei,Q., Chen,X., Zhao,B., Wu,Y., Song,W.
            and Shang,H.F.
  TITLE     Determining the Effect of the HNMT, STK39, and NMD3 Polymorphisms
            on the Incidence of Parkinson's Disease, Amyotrophic Lateral
            Sclerosis, and Multiple System Atrophy in Chinese Populations
  JOURNAL   J Mol Neurosci 64 (4), 574-580 (2018)
   PUBMED   29564728
  REMARK    GeneRIF: NHMT polymorphisms are not associated with Parkinson's
            disease, ALS and multiple system atrophy in Chinese population.
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Jia,H.Z., Liu,S.L., Zou,Y.F., Chen,X.F., Yu,L., Wan,J., Zhang,H.Y.,
            Chen,Q., Xiong,Y., Yu,B. and Zhang,W.
  TITLE     MicroRNA-223 is involved in the pathogenesis of atopic dermatitis
            by affecting histamine-N-methyltransferase
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 64 (3), 103-107 (2018)
   PUBMED   29506638
  REMARK    GeneRIF: miR-223 participates in the pathogenesis of atopic
            dermatitis through upregulating HNMT indirectly to degrade the
            excessive histamine.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Yan,L., Galinsky,R.E., Bernstein,J.A., Liggett,S.B. and
            Weinshilboum,R.M.
  TITLE     Histamine N-methyltransferase pharmacogenetics: association of a
            common functional polymorphism with asthma
  JOURNAL   Pharmacogenetics 10 (3), 261-266 (2000)
   PUBMED   10803682
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Preuss,C.V., Wood,T.C., Szumlanski,C.L., Raftogianis,R.B.,
            Otterness,D.M., Girard,B., Scott,M.C. and Weinshilboum,R.M.
  TITLE     Human histamine N-methyltransferase pharmacogenetics: common
            genetic polymorphisms that alter activity
  JOURNAL   Mol Pharmacol 53 (4), 708-717 (1998)
   PUBMED   9547362
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Aksoy,S., Raftogianis,R. and Weinshilboum,R.
  TITLE     Human histamine N-methyltransferase gene: structural
            characterization and chromosomal location
  JOURNAL   Biochem Biophys Res Commun 219 (2), 548-554 (1996)
   PUBMED   8605025
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Yamauchi,K., Sekizawa,K., Suzuki,H., Nakazawa,H., Ohkawara,Y.,
            Katayose,D., Ohtsu,H., Tamura,G., Shibahara,S., Takemura,M. et al.
  TITLE     Structure and function of human histamine N-methyltransferase:
            critical enzyme in histamine metabolism in airway
  JOURNAL   Am J Physiol 267 (3 Pt 1), L342-L349 (1994)
   PUBMED   7943261
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Girard,B., Otterness,D.M., Wood,T.C., Honchel,R., Wieben,E.D. and
            Weinshilboum,R.M.
  TITLE     Human histamine N-methyltransferase pharmacogenetics: cloning and
            expression of kidney cDNA
  JOURNAL   Mol Pharmacol 45 (3), 461-468 (1994)
   PUBMED   8145732
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF523358.1, AF523360.1,
            AC093674.2 and AA935821.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: In mammals, histamine is metabolized by two major
            pathways: N(tau)-methylation via histamine N-methyltransferase and
            oxidative deamination via diamine oxidase. This gene encodes the
            first enzyme which is found in the cytosol and uses
            S-adenosyl-L-methionine as the methyl donor. In the mammalian
            brain, the neurotransmitter activity of histamine is controlled by
            N(tau)-methylation as diamine oxidase is not found in the central
            nervous system. A common genetic polymorphism affects the activity
            levels of this gene product in red blood cells. Multiple
            alternatively spliced transcript variants that encode different
            proteins have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and it encodes the longest protein (isoform 1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.114944.1,
                                           SRR1660805.150107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280097.5/ ENSP00000280097.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q22.1"
     Protein         1..292
                     /product="histamine N-methyltransferase isoform 1"
                     /EC_number="2.1.1.8"
                     /calculated_mol_wt=33164
     Region          32..217
                     /region_name="Methyltransf_23"
                     /note="Methyltransferase domain; pfam13489"
                     /db_xref="CDD:404385"
     Site            order(59..65,89..90,118..120,142)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
     CDS             1..292
                     /gene="HNMT"
                     /gene_synonym="HMT; HNMT-S1; HNMT-S2; MRT51"
                     /coded_by="NM_006895.3:20..898"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2181.1"
                     /db_xref="GeneID:3176"
                     /db_xref="HGNC:HGNC:5028"
                     /db_xref="MIM:605238"
ORIGIN      
        1 massmrslfs dhgkyvesfr rflnhstehq cmqefmdkkl pgiigrigdt kseikilsig
       61 ggageidlqi lskvqaqypg vcinnevvep saeqiakyke lvaktsnlen vkfawhkets
      121 seyqsrmlek kelqkwdfih miqmlyyvkd ipatlkffhs llgtnakmli ivvsgssgwd
      181 klwkkygsrf pqddlcqyit sddltqmldn lglkyecydl lstmdisdcf idgnengdll
      241 wdfltetcnf natappdlra elgkdlqepe fsakkegkvl fnntlsfivi ea
//
LOCUS       NP_002929                190 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF4 isoform 1 [Homo sapiens].
ACCESSION   NP_002929
VERSION     NP_002929.1
DBSOURCE    REFSEQ: accession NM_002938.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Fu,A., Luo,Z., Ziv,T., Bi,X., Lulu-Shimron,C., Cohen-Kaplan,V. and
            Ciechanover,A.
  TITLE     Nuclear p62 condensates stabilize the promyelocytic leukemia
            nuclear bodies by sequestering their ubiquitin ligase RNF4
  JOURNAL   Proc Natl Acad Sci U S A 121 (43), e2414377121 (2024)
   PUBMED   39418304
  REMARK    GeneRIF: Nuclear p62 condensates stabilize the promyelocytic
            leukemia nuclear bodies by sequestering their ubiquitin ligase
            RNF4.
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Her,J., Zheng,H. and Bunting,S.F.
  TITLE     RNF4 sustains Myc-driven tumorigenesis by facilitating DNA
            replication
  JOURNAL   J Clin Invest 134 (10), e167419 (2024)
   PUBMED   38530355
  REMARK    GeneRIF: RNF4 sustains Myc-driven tumorigenesis by facilitating DNA
            replication.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Oram,M.K., Baxley,R.M., Simon,E.M., Lin,K., Chang,Y.C., Wang,L.,
            Myers,C.L. and Bielinsky,A.K.
  TITLE     RNF4 prevents genomic instability caused by chronic DNA
            under-replication
  JOURNAL   DNA Repair (Amst) 135, 103646 (2024)
   PUBMED   38340377
  REMARK    GeneRIF: RNF4 prevents genomic instability caused by chronic DNA
            under-replication.
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Huang,J., Yang,W., Jiang,K., Liu,Y., Tan,X. and Luo,J.
  TITLE     RNF4 promotes tumorigenesis, therapy resistance of
            cholangiocarcinoma and affects cell cycle by regulating the
            ubiquitination degradation of p27kip1 in the nucleus
  JOURNAL   Exp Cell Res 419 (1), 113295 (2022)
   PUBMED   35926659
  REMARK    GeneRIF: RNF4 promotes tumorigenesis, therapy resistance of
            cholangiocarcinoma and affects cell cycle by regulating the
            ubiquitination degradation of p27kip1 in the nucleus.
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Novak,R., Ahmad,Y.A., Timaner,M., Bitman-Lotan,E.,
            Oknin-Vaisman,A., Horwitz,R., Hartmann,O., Reissland,M., Buck,V.,
            Rosenfeldt,M., Nikomarov,D., Diefenbacher,M.E., Shaked,Y. and
            Orian,A.
  TITLE     RNF4 RGMb BMP6 axis required for osteogenic differentiation and
            cancer cell survival
  JOURNAL   Cell Death Dis 13 (9), 820 (2022)
   PUBMED   36153321
  REMARK    GeneRIF: RNF4~RGMb~BMP6 axis required for osteogenic
            differentiation and cancer cell survival.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 190)
  AUTHORS   Fedele,M., Benvenuto,G., Pero,R., Majello,B., Battista,S.,
            Lembo,F., Vollono,E., Day,P.M., Santoro,M., Lania,L., Bruni,C.B.,
            Fusco,A. and Chiariotti,L.
  TITLE     A novel member of the BTB/POZ family, PATZ, associates with the
            RNF4 RING finger protein and acts as a transcriptional repressor
  JOURNAL   J Biol Chem 275 (11), 7894-7901 (2000)
   PUBMED   10713105
REFERENCE   7  (residues 1 to 190)
  AUTHORS   Poukka,H., Aarnisalo,P., Santti,H., Janne,O.A. and Palvimo,J.J.
  TITLE     Coregulator small nuclear RING finger protein (SNURF) enhances Sp1-
            and steroid receptor-mediated transcription by different mechanisms
  JOURNAL   J Biol Chem 275 (1), 571-579 (2000)
   PUBMED   10617653
REFERENCE   8  (residues 1 to 190)
  AUTHORS   Moilanen,A.M., Poukka,H., Karvonen,U., Hakli,M., Janne,O.A. and
            Palvimo,J.J.
  TITLE     Identification of a novel RING finger protein as a coregulator in
            steroid receptor-mediated gene transcription
  JOURNAL   Mol Cell Biol 18 (9), 5128-5139 (1998)
   PUBMED   9710597
REFERENCE   9  (residues 1 to 190)
  AUTHORS   Hadano,S., Ishida,Y. and Ikeda,J.E.
  TITLE     The primary structure and genomic organization of five novel
            transcripts located close to the Huntington's disease gene on human
            chromosome 4p16.3
  JOURNAL   DNA Res 5 (3), 177-186 (1998)
   PUBMED   9734812
REFERENCE   10 (residues 1 to 190)
  AUTHORS   Chiariotti,L., Benvenuto,G., Fedele,M., Santoro,M., Simeone,A.,
            Fusco,A. and Bruni,C.B.
  TITLE     Identification and characterization of a novel RING-finger gene
            (RNF4) mapping at 4p16.3
  JOURNAL   Genomics 47 (2), 258-265 (1998)
   PUBMED   9479498
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA342512.1, AB000468.1,
            U95140.1 and BX322586.11.
            
            Summary: The protein encoded by this gene contains a RING finger
            motif and acts as a transcription regulator. This protein has been
            shown to interact with, and inhibit the activity of, TRPS1, a
            transcription suppressor of GATA-mediated transcription.
            Transcription repressor ZNF278/PATZ is found to interact with this
            protein, and thus reduce the enhancement of androgen
            receptor-dependent transcription mediated by this protein. Studies
            of the mouse and rat counterparts suggested a role of this protein
            in spermatogenesis. A pseudogene of this gene is found on
            chromosome 1.[provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1057758.1,
                                           SRR3476690.759234.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000314289.13/ ENSP00000315212.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..190
                     /product="E3 ubiquitin-protein ligase RNF4 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="small nuclear RING finger protein; E3 ubiquitin
                     ligase RNF4; E3 ubiquitin-protein ligase RNF4; RING-type
                     E3 ubiquitin transferase RNF4"
                     /calculated_mol_wt=21188
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78317.1)"
     Region          1..16
                     /region_name="Required for ubiquitination activity.
                     /evidence=ECO:0000250|UniProtKB:Q9QZS2"
                     /note="propagated from UniProtKB/Swiss-Prot (P78317.1)"
     Region          4..61
                     /region_name="Mediates interaction with TRPS1.
                     /evidence=ECO:0000250|UniProtKB:Q9QZS2"
                     /note="propagated from UniProtKB/Swiss-Prot (P78317.1)"
     Region          36..39
                     /region_name="SUMO interaction motif 1.
                     /evidence=ECO:0000269|PubMed:18408734"
                     /note="propagated from UniProtKB/Swiss-Prot (P78317.1)"
     Region          46..49
                     /region_name="SUMO interaction motif 2.
                     /evidence=ECO:0000269|PubMed:18408734"
                     /note="propagated from UniProtKB/Swiss-Prot (P78317.1)"
     Region          57..59
                     /region_name="SUMO interaction motif 3.
                     /evidence=ECO:0000269|PubMed:18408734"
                     /note="propagated from UniProtKB/Swiss-Prot (P78317.1)"
     Region          67..70
                     /region_name="SUMO interaction motif 4.
                     /evidence=ECO:0000269|PubMed:18408734"
                     /note="propagated from UniProtKB/Swiss-Prot (P78317.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78317.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78317.1)"
     Region          127..183
                     /region_name="RING-HC_RNF4"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 4 (RNF4) and similar proteins; cd16533"
                     /db_xref="CDD:438195"
     Site            order(127,156,174..177)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438195"
     Site            order(133..137,141,162,165..166,169,174,177)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438195"
     CDS             1..190
                     /gene="RNF4"
                     /gene_synonym="RES4-26; SLX5; SNURF"
                     /coded_by="NM_002938.5:311..883"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47001.1"
                     /db_xref="GeneID:6047"
                     /db_xref="HGNC:HGNC:10067"
                     /db_xref="MIM:602850"
ORIGIN      
        1 mstrkrrgga insrqaqkrt reatstpeis leaepielve tagdeivdlt ceslepvvvd
       61 lthndsvviv derrrprrna rrlpqdhads cvvssddeel srdrdvyvtt htprnardeg
      121 atglrpsgtv scpicmdgys eivqngrliv stecghvfcs qclrdslkna ntcptcrkki
      181 nhkryhpiyi
//
LOCUS       NP_001009608             408 aa            linear   PRI 27-APR-2025
DEFINITION  protein SLX4IP [Homo sapiens].
ACCESSION   NP_001009608 XP_059267
VERSION     NP_001009608.1
DBSOURCE    REFSEQ: accession NM_001009608.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Mangosh,T.L., Awadallah,W.N., Grabowska,M.M. and Taylor,D.J.
  TITLE     SLX4IP Promotes Telomere Maintenance in Androgen
            Receptor-Independent Castration-Resistant Prostate Cancer through
            ALT-like Telomeric PML Localization
  JOURNAL   Mol Cancer Res 19 (2), 301-316 (2021)
   PUBMED   33188147
  REMARK    GeneRIF: SLX4IP Promotes Telomere Maintenance in Androgen
            Receptor-Independent Castration-Resistant Prostate Cancer through
            ALT-like Telomeric PML Localization.
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Robinson,N.J., Morrison-Smith,C.D., Gooding,A.J., Schiemann,B.J.,
            Jackson,M.W., Taylor,D.J. and Schiemann,W.P.
  TITLE     SLX4IP and telomere dynamics dictate breast cancer metastasis and
            therapeutic responsiveness
  JOURNAL   Life Sci Alliance 3 (4), e201900427 (2020)
   PUBMED   32071280
  REMARK    GeneRIF: SLX4IP and telomere dynamics dictate breast cancer
            metastasis and therapeutic responsiveness.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Zhang,H., Chen,Z., Ye,Y., Ye,Z., Cao,D., Xiong,Y., Srivastava,M.,
            Feng,X., Tang,M., Wang,C., Tainer,J.A. and Chen,J.
  TITLE     SLX4IP acts with SLX4 and XPF-ERCC1 to promote interstrand
            crosslink repair
  JOURNAL   Nucleic Acids Res 47 (19), 10181-10201 (2019)
   PUBMED   31495888
  REMARK    GeneRIF: The binding of SLX4IP to both SLX4 and XPF-ERCC1 not only
            is vital for maintaining the stability of SLX4IP protein, but also
            promotes the interaction between SLX4 and XPF-ERCC1, especially
            after DNA damage. Collectively, these results demonstrate a new
            regulatory role for SLX4IP in maintaining an efficient
            SLX4-XPF-ERCC1 complex in interstrand crosslinks (ICLs) repair.
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Panier,S., Maric,M., Hewitt,G., Mason-Osann,E., Gali,H., Dai,A.,
            Labadorf,A., Guervilly,J.H., Ruis,P., Segura-Bayona,S., Belan,O.,
            Marzec,P., Gaillard,P.L., Flynn,R.L. and Boulton,S.J.
  TITLE     SLX4IP Antagonizes Promiscuous BLM Activity during ALT Maintenance
  JOURNAL   Mol Cell 76 (1), 27-43 (2019)
   PUBMED   31447390
  REMARK    GeneRIF: SLX4IP antagonizes promiscuous BLM Activity during
            alternative lengthening of telomeres maintenance in osteosarcoma
            cells.
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Meissner,B., Bartram,T., Eckert,C., Trka,J., Panzer-Grumayer,R.,
            Hermanova,I., Ellinghaus,E., Franke,A., Moricke,A., Schrauder,A.,
            Teigler-Schlegel,A., Dorge,P., von Stackelberg,A., Basso,G.,
            Bartram,C.R., Kirschner-Schwabe,R., Bornhauser,B., Bourquin,J.P.,
            Cazzaniga,G., Hauer,J., Attarbaschi,A., Izraeli,S., Zaliova,M.,
            Cario,G., Zimmermann,M., Avigad,S., Sokalska-Duhme,M., Metzler,M.,
            Schrappe,M., Koehler,R., Te Kronnie,G. and Stanulla,M.
  TITLE     Frequent and sex-biased deletion of SLX4IP by illegitimate
            V(D)J-mediated recombination in childhood acute lymphoblastic
            leukemia
  JOURNAL   Hum Mol Genet 23 (3), 590-601 (2014)
   PUBMED   24045615
  REMARK    GeneRIF: The association of SLX4IP deletion with male sex suggest
            that differential illegitimate V(D)J-mediated recombination events
            contribute to the higher incidence rates of childhood acute
            lymphoblastic leukemia in boys compared with girls.
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Svendsen,J.M., Smogorzewska,A., Sowa,M.E., O'Connell,B.C.,
            Gygi,S.P., Elledge,S.J. and Harper,J.W.
  TITLE     Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and
            is required for DNA repair
  JOURNAL   Cell 138 (1), 63-77 (2009)
   PUBMED   19596235
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC026094.1, AL035456.26 and CA416447.1.
            
            On Mar 15, 2005 this sequence version replaced XP_059267.4.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020787.1, SRR5189661.147636.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2163623
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334534.10/ ENSP00000335557.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.2"
     Protein         1..408
                     /product="protein SLX4IP"
                     /calculated_mol_wt=45421
     Region          10..368
                     /region_name="UPF0492"
                     /note="Uncharacterized protein family UPF0492; pfam15744"
                     /db_xref="CDD:464840"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VYV7.1)"
     Region          173..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VYV7.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VYV7.1)"
     Region          243..313
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VYV7.1)"
     Region          365..408
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VYV7.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VYV7.1)"
     CDS             1..408
                     /gene="SLX4IP"
                     /gene_synonym="bA204H22.1; bA254M13.1; C20orf94;
                     dJ1099D15.3"
                     /coded_by="NM_001009608.3:179..1405"
                     /db_xref="CCDS:CCDS33439.1"
                     /db_xref="GeneID:128710"
                     /db_xref="HGNC:HGNC:16225"
                     /db_xref="MIM:615958"
ORIGIN      
        1 maskkfavkc gnfavlvdlh ilpqgsnkdt swfseqkkee vclllketid srvqeylevr
       61 kqhrpsnaef trsnplslkg ygfqitayfl krgirlrcir stqnaelcvf pdrfvvcvsq
      121 lafsrdllas qnedltervl hgvsdyfaec aesslppsak lrrnalkeiv krtetkssvt
      181 sksqtrrdtv etssdsviae iarrrndgqa sssppsesmg qakdsikaae shwglpvqkl
      241 ekvnqtqped tsgqqkphpg erlktgllsr spvcscesas pcpkqsprva ktqqkrrncs
      301 saedfdhhgr vslgsdrlvp reiivekska vrvlpasels dpglllkqdl akttskeelh
      361 vleslssrhl mknnpgqaqq tglatnterl stiqnsptkk rkkyergh
//
LOCUS       NP_001121620             760 aa            linear   PRI 27-APR-2025
DEFINITION  transferrin receptor protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001121620
VERSION     NP_001121620.1
DBSOURCE    REFSEQ: accession NM_001128148.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Xing,P., Zhou,M., Sun,J., Wang,D., Huang,W. and An,P.
  TITLE     NAT10-mediated ac4C acetylation of TFRC promotes sepsis-induced
            pulmonary injury through regulating ferroptosis
  JOURNAL   Mol Med 30 (1), 140 (2024)
   PUBMED   39251905
  REMARK    GeneRIF: NAT10-mediated ac[4]C acetylation of TFRC promotes
            sepsis-induced pulmonary injury through regulating ferroptosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 760)
  AUTHORS   Ji,W., Zhang,W., Zhang,X. and Ke,Y.
  TITLE     TRIM33 enhances the ubiquitination of TFRC to enhance the
            susceptibility of liver cancer cells to ferroptosis
  JOURNAL   Cell Signal 121, 111268 (2024)
   PUBMED   38909931
  REMARK    GeneRIF: TRIM33 enhances the ubiquitination of TFRC to enhance the
            susceptibility of liver cancer cells to ferroptosis.
REFERENCE   3  (residues 1 to 760)
  AUTHORS   Shang,X., Wang,H., Gu,J., Zhao,X., Zhang,J., Sun,B. and Zhu,X.
  TITLE     Ferroptosis-related gene transferrin receptor protein 1 expression
            correlates with the prognosis and tumor immune microenvironment in
            cervical cancer
  JOURNAL   PeerJ 12, e17842 (2024)
   PUBMED   39131609
  REMARK    GeneRIF: Ferroptosis-related gene transferrin receptor protein 1
            expression correlates with the prognosis and tumor immune
            microenvironment in cervical cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 760)
  AUTHORS   Qin,J., Li,Z., Su,L., Wen,X., Tang,X., Huang,M. and Wu,J.
  TITLE     Expression of transferrin receptor/TFRC protein in bladder cancer
            cell T24 and its role in inducing iron death in bladder cancer
  JOURNAL   Int J Biol Macromol 274 (Pt 1), 133323 (2024)
   PUBMED   38908617
  REMARK    GeneRIF: Expression of transferrin receptor/TFRC protein in bladder
            cancer cell T24 and its role in inducing iron death in bladder
            cancer.
REFERENCE   5  (residues 1 to 760)
  AUTHORS   Pacella,I., Pinzon Grimaldos,A., Rossi,A., Tucci,G., Zagaglioni,M.,
            Potenza,E., Pinna,V., Rotella,I., Cammarata,I., Cancila,V.,
            Belmonte,B., Tripodo,C., Pietropaolo,G., Di Censo,C., Sciume,G.,
            Licursi,V., Peruzzi,G., Antonucci,Y., Campello,S., Guerrieri,F.,
            Iebba,V., Prota,R., Di Chiara,M., Terrin,G., De Peppo,V.,
            Grazi,G.L., Barnaba,V. and Piconese,S.
  TITLE     Iron capture through CD71 drives perinatal and tumor-associated
            Treg expansion
  JOURNAL   JCI Insight 9 (15), e167967 (2024)
   PUBMED   38954474
  REMARK    GeneRIF: Iron capture through CD71 drives perinatal and
            tumor-associated Treg expansion.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 760)
  AUTHORS   Chicz,R.M., Urban,R.G., Lane,W.S., Gorga,J.C., Stern,L.J.,
            Vignali,D.A. and Strominger,J.L.
  TITLE     Predominant naturally processed peptides bound to HLA-DR1 are
            derived from MHC-related molecules and are heterogeneous in size
  JOURNAL   Nature 358 (6389), 764-768 (1992)
   PUBMED   1380674
REFERENCE   7  (residues 1 to 760)
  AUTHORS   Hayes,G.R., Enns,C.A. and Lucas,J.J.
  TITLE     Identification of the O-linked glycosylation site of the human
            transferrin receptor
  JOURNAL   Glycobiology 2 (4), 355-359 (1992)
   PUBMED   1421757
REFERENCE   8  (residues 1 to 760)
  AUTHORS   Do,S.I. and Cummings,R.D.
  TITLE     Presence of O-linked oligosaccharide on a threonine residue in the
            human transferrin receptor
  JOURNAL   Glycobiology 2 (4), 345-353 (1992)
   PUBMED   1421756
REFERENCE   9  (residues 1 to 760)
  AUTHORS   Baynes,R.D., Shih,Y.J., Hudson,B.G. and Cook,J.D.
  TITLE     Characterization of transferrin receptor released by K562
            erythroleukemia cells
  JOURNAL   Proc Soc Exp Biol Med 197 (4), 416-423 (1991)
   PUBMED   1871153
REFERENCE   10 (residues 1 to 760)
  AUTHORS   Shih,Y.J., Baynes,R.D., Hudson,B.G., Flowers,C.H., Skikne,B.S. and
            Cook,J.D.
  TITLE     Serum transferrin receptor is a truncated form of tissue receptor
  JOURNAL   J Biol Chem 265 (31), 19077-19081 (1990)
   PUBMED   2229063
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CF994006.1, BC001188.1,
            X01060.1 and BX537966.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a cell surface receptor necessary for
            cellular iron uptake by the process of receptor-mediated
            endocytosis. This receptor is required for erythropoiesis and
            neurologic development. Multiple alternatively spliced variants
            have been identified. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.18761.1,
                                           SRR1660809.22598.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360110.9/ ENSP00000353224.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..760
                     /product="transferrin receptor protein 1 isoform 1"
                     /note="transferrin receptor protein 1"
                     /calculated_mol_wt=84741
     Region          1..67
                     /region_name="Mediates interaction with SH3BP4.
                     /evidence=ECO:0000269|PubMed:16325581"
                     /note="propagated from UniProtKB/Swiss-Prot (P02786.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02786.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62351; propagated from
                     UniProtKB/Swiss-Prot (P02786.2)"
     Region          20..23
                     /region_name="Endocytosis signal.
                     /evidence=ECO:0000269|PubMed:2298808"
                     /note="propagated from UniProtKB/Swiss-Prot (P02786.2)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02786.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P02786.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9782058; propagated from
                     UniProtKB/Swiss-Prot (P02786.2)"
     Region          58..61
                     /region_name="Stop-transfer sequence.
                     /evidence=ECO:0000303|PubMed:6090955"
                     /note="propagated from UniProtKB/Swiss-Prot (P02786.2)"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P02786.2)"
     Site            100..101
                     /site_type="cleavage"
                     /note="Cleavage, by trypsin, to produce soluble form;
                     propagated from UniProtKB/Swiss-Prot (P02786.2)"
     mat_peptide     101..760
                     /product="Transferrin receptor protein 1, serum form.
                     /id=PRO_0000292265"
                     /note="propagated from UniProtKB/Swiss-Prot (P02786.2)"
                     /calculated_mol_wt=73806
     Site            104
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1421756,
                     ECO:0000269|PubMed:1421757. /id=CAR_000072; propagated
                     from UniProtKB/Swiss-Prot (P02786.2)"
     Region          201..377
                     /region_name="PA_TfR"
                     /note="Protease-associated domain containing proteins like
                     transferrin receptor (TfR). This group contains various PA
                     domain-containing proteins similar to human TfR1 and TfR2.
                     TfR1 and TfR2 are type II membrane proteins, belonging to
                     the peptidase M28 family; cd02128"
                     /db_xref="CDD:239043"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:10531064,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19349973, ECO:0007744|PDB:1CX8;
                     propagated from UniProtKB/Swiss-Prot (P02786.2)"
     Site            order(287,295..298,300,304..307,310,312..314)
                     /site_type="other"
                     /note="PA/protease-like domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239043"
     Site            order(305,311)
                     /site_type="other"
                     /note="PA/helical domain interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            order(310,313)
                     /site_type="other"
                     /note="Ca2+ binding [ion binding]"
                     /db_xref="CDD:239043"
     Site            order(314,316,320..321)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            317
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:10531064,
                     ECO:0007744|PDB:1CX8; propagated from UniProtKB/Swiss-Prot
                     (P02786.2)"
     Region          364..610
                     /region_name="M28_TfR"
                     /note="M28 Zn-peptidase Transferrin Receptor family;
                     cd09848"
                     /db_xref="CDD:349946"
     Site            order(377,379..380,382,392,394,397,399..400,402,447,449,
                     466,469..477)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349946"
     Region          569..760
                     /region_name="Ligand-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P02786.2)"
     Region          637..750
                     /region_name="TFR_dimer"
                     /note="Transferrin receptor-like dimerization domain;
                     pfam04253"
                     /db_xref="CDD:461238"
     Region          646..648
                     /region_name="Cell attachment site, required for binding
                     to transferrin"
                     /note="propagated from UniProtKB/Swiss-Prot (P02786.2)"
     Site            727
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:10531064,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7780197,
                     ECO:0007744|PDB:1CX8. /id=CAR_000173; propagated from
                     UniProtKB/Swiss-Prot (P02786.2)"
     CDS             1..760
                     /gene="TFRC"
                     /gene_synonym="CD71; IMD46; p90; T9; TFR; TFR1; TR; TRFR"
                     /coded_by="NM_001128148.3:72..2354"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3312.1"
                     /db_xref="GeneID:7037"
                     /db_xref="HGNC:HGNC:11763"
                     /db_xref="MIM:190010"
ORIGIN      
        1 mmdqarsafs nlfggeplsy trfslarqvd gdnshvemkl avdeeenadn ntkanvtkpk
       61 rcsgsicygt iavivfflig fmigylgyck gvepktecer lagtespvre epgedfpaar
      121 rlywddlkrk lsekldstdf tgtikllnen syvpreagsq kdenlalyve nqfrefklsk
      181 vwrdqhfvki qvkdsaqnsv iivdkngrlv ylvenpggyv ayskaatvtg klvhanfgtk
      241 kdfedlytpv ngsivivrag kitfaekvan aeslnaigvl iymdqtkfpi vnaelsffgh
      301 ahlgtgdpyt pgfpsfnhtq fppsrssglp nipvqtisra aaeklfgnme gdcpsdwktd
      361 stcrmvtses knvkltvsnv lkeikilnif gvikgfvepd hyvvvgaqrd awgpgaaksg
      421 vgtalllkla qmfsdmvlkd gfqpsrsiif aswsagdfgs vgatewlegy lsslhlkaft
      481 yinldkavlg tsnfkvsasp llytliektm qnvkhpvtgq flyqdsnwas kvekltldna
      541 afpflaysgi pavsfcfced tdypylgttm dtykelieri pelnkvaraa aevagqfvik
      601 lthdvelnld yerynsqlls fvrdlnqyra dikemglslq wlysargdff ratsrlttdf
      661 gnaektdrfv mkklndrvmr veyhflspyv spkespfrhv fwgsgshtlp allenlklrk
      721 qnngafnetl frnqlalatw tiqgaanals gdvwdidnef
//
LOCUS       NP_071423                686 aa            linear   PRI 27-APR-2025
DEFINITION  band 4.1-like protein 4A isoform 2 [Homo sapiens].
ACCESSION   NP_071423
VERSION     NP_071423.4
DBSOURCE    REFSEQ: accession NM_022140.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Antoni,G., Oudot-Mellakh,T., Dimitromanolakis,A., Germain,M.,
            Cohen,W., Wells,P., Lathrop,M., Gagnon,F., Morange,P.E. and
            Tregouet,D.A.
  TITLE     Combined analysis of three genome-wide association studies on vWF
            and FVIII plasma levels
  JOURNAL   BMC Med Genet 12, 102 (2011)
   PUBMED   21810271
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Ishiguro,H., Furukawa,Y., Daigo,Y., Miyoshi,Y., Nagasawa,Y.,
            Nishiwaki,T., Kawasoe,T., Fujita,M., Satoh,S., Miwa,N., Fujii,Y.
            and Nakamura,Y.
  TITLE     Isolation and characterization of human NBL4, a gene involved in
            the beta-catenin/tcf signaling pathway
  JOURNAL   Jpn J Cancer Res 91 (6), 597-603 (2000)
   PUBMED   10874211
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Shimizu,K., Nagamachi,Y., Tani,M., Kimura,K., Shiroishi,T.,
            Wakana,S. and Yokota,J.
  TITLE     Molecular cloning of a novel NF2/ERM/4.1 superfamily gene, ehm2,
            that is expressed in high-metastatic K1735 murine melanoma cells
  JOURNAL   Genomics 65 (2), 113-120 (2000)
   PUBMED   10783258
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Takeuchi,K., Kawashima,A., Nagafuchi,A. and Tsukita,S.
  TITLE     Structural diversity of band 4.1 superfamily members
  JOURNAL   J Cell Sci 107 (Pt 7), 1921-1928 (1994)
   PUBMED   7983158
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC031042.1, AB030240.1,
            AA350575.1, AK096057.1, CB048933.1, BC114632.1, AC010261.5 and
            BC015441.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 17, 2016 this sequence version replaced NP_071423.3.
            
            Summary: The protein encoded by this gene is a member of the band
            4.1 protein superfamily. Members of this superfamily are thought to
            play an important role in regulating interactions between the
            cytoskeleton and plasma membrane, and contain an amino terminal
            conserved domain that binds glycophorin C. This gene product is
            thought to be involved in the beta-catenin signaling pathway.
            [provided by RefSeq, Dec 2016].
            
            Transcript Variant: This variant (2) lacks two consecutive exons at
            the 3' end, and includes an alternate 3' terminal exon, compared to
            variant 1. The encoded isoform (2) is shorter and has a distinct
            C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.132871.1,
                                           SRR1803616.89046.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261486.6/ ENSP00000261486.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.1-q22.2"
     Protein         1..686
                     /product="band 4.1-like protein 4A isoform 2"
                     /note="erythrocyte protein band 4.1-like 4; band 4.1-like
                     protein 4A"
                     /calculated_mol_wt=78928
     Region          13..211
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          207..296
                     /region_name="FERM_C_NBL4_NBL5"
                     /note="FERM domain C-lobe of Novel band 4.1-like protein 4
                     and 5 (NBL4 and 5); cd13186"
                     /db_xref="CDD:270007"
     Site            order(215,232,234,240)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270007"
     Site            order(244,249..252,285,289,292..293)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Site            285..296
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCS5.2)"
     Region          311..355
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     Region          331..686
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCS5.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCS5.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCS5.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q9HCS5.2)"
     CDS             1..686
                     /gene="EPB41L4A"
                     /gene_synonym="EPB41L4; NBL4"
                     /coded_by="NM_022140.5:239..2299"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43350.1"
                     /db_xref="GeneID:64097"
                     /db_xref="HGNC:HGNC:13278"
                     /db_xref="MIM:612141"
ORIGIN      
        1 mgcfcavpee fycevlllde skltlttqqq gikkstkgsv vldhvfhhvn lveidyfglr
       61 ycdrshqtyw ldpaktlaeh kelintgppy tlyfgikfya edpcklkeei tryqfflqvk
      121 qdvlqgrlpc pvntaaqlga yaiqselgdy dpykhtagyv seyrfvpdqk eeleeaieri
      181 hktlmgqips eaelnylrta kslemygvdl hpvygenkse yflgltpvgv vvyknkkqvg
      241 kyfwpritkv hfketqfelr vlgkdcnets fffearskta ckhlwkcsve hhtffrmpen
      301 esnslsrkls kfgsirykhr ysgrtalqms rdlsiqlprp dqnvtrsrsk typkriaqtq
      361 paesnsisri tanmengene gtikiiapsp vksfkkakne nspdtqrsks hapweengpq
      421 sglynspsdr tkspkfpytr rrnpscgsdn dsvqpvrrrk ahnsgedsdl kqrrrsrsrc
      481 ntssgsesen snreyrkkrn rirqendmvd sapqweavlr rqkeknqadp nnrrsrhrsr
      541 srspdiqake elwkhiqkel vdpsglseeq lkeipytkie tqgdpirirh shsprsyrqy
      601 rrsqcsdger svlsevnskt dlvpplpvtr ssdaqgsgda tvhqrrngsk dslmeekpqt
      661 stnnlagkht aktiktiqas rlktet
//
LOCUS       NP_694776                323 aa            linear   ROD 27-APR-2025
DEFINITION  8-oxo-dGDP phosphatase NUDT18 isoform 1 [Mus musculus].
ACCESSION   NP_694776
VERSION     NP_694776.2
DBSOURCE    REFSEQ: accession NM_153136.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Tamplin,O.J., Cox,B.J. and Rossant,J.
  TITLE     Integrated microarray and ChIP analysis identifies multiple Foxa2
            dependent target genes in the notochord
  JOURNAL   Dev Biol 360 (2), 415-425 (2011)
   PUBMED   22008794
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC122268.5, AK157937.1 and AK089446.1.
            
            On Jan 13, 2006 this sequence version replaced NP_694776.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK157937.1, AK155086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 36.32 cM"
     Protein         1..323
                     /product="8-oxo-dGDP phosphatase NUDT18 isoform 1"
                     /EC_number="3.6.1.58"
                     /note="mutT homolog 3; 2-hydroxy-dADP phosphatase;
                     7,8-dihydro-8-oxoguanine phosphatase; 8-oxo-dGDP
                     phosphatase NUDT18; nudix (nucleoside diphosphate linked
                     moiety X)-type motif 18"
                     /calculated_mol_wt=35563
     Region          44..173
                     /region_name="NUDIX_8DGDPP_Nudt18"
                     /note="8-oxo-DGDP phosphatase; cd04671"
                     /db_xref="CDD:467555"
     Region          76..97
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U2V3.1)"
     CDS             1..323
                     /gene="Nudt18"
                     /coded_by="NM_153136.5:126..1097"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS27258.1"
                     /db_xref="GeneID:213484"
                     /db_xref="MGI:MGI:2385853"
ORIGIN      
        1 mateglagal atvlggkgll vqscdsepag kplfpvrlrk nvcyvvlavf lneqdevlmi
       61 qeakrecrgt wylpagrmep getiveamqr evkeeagllc epvtllsvee rgaswirfvf
      121 larptggvlk tskdadsesl qagwyprvsl ptplrahdvl hlvelgakfc qqamhplilp
      181 qelpcsvvcq rlvttfttvq svwvlvgtvg tphlpitacg ftpmeqrggi kvailrllqe
      241 cltlhslave tkgllglqhl grdhvdgvcl nvlvtvafrn pgiqdeppki rgenyfwwkv
      301 leedlqklll yrlqessvip lsr
//
LOCUS       NP_035970                448 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity mitogen-activated protein kinase kinase 5 isoform
            1 [Mus musculus].
ACCESSION   NP_035970 XP_986571 XP_986623 XP_986663 XP_986702 XP_986739
VERSION     NP_035970.1
DBSOURCE    REFSEQ: accession NM_011840.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Tsitsikov,E.N., Phan,K.P., Liu,Y., Tsytsykova,A.V., Kinter,M.,
            Selland,L., Garman,L., Griffin,C. and Dunn,I.F.
  TITLE     TRAF7 is an essential regulator of blood vessel integrity during
            mouse embryonic and neonatal development
  JOURNAL   iScience 26 (8), 107474 (2023)
   PUBMED   37583551
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Huang,Y., Wang,P., Morales,R., Luo,Q. and Ma,J.
  TITLE     Map2k5-Deficient Mice Manifest Phenotypes and Pathological Changes
            of Dopamine Deficiency in the Central Nervous System
  JOURNAL   Front Aging Neurosci 13, 651638 (2021)
   PUBMED   34168549
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Luiz,J.P.M., Toller-Kawahisa,J.E., Viacava,P.R., Nascimento,D.C.,
            Pereira,P.T., Saraiva,A.L., Prado,D.S., LeBert,M., Giurisato,E.,
            Tournier,C., Cunha,T.M., Cunha,F.Q., Quesniaux,V., Ryffel,B. and
            Alves-Filho,J.C.
  TITLE     MEK5/ERK5 signaling mediates IL-4-induced M2 macrophage
            differentiation through regulation of c-Myc expression
  JOURNAL   J Leukoc Biol 108 (4), 1215-1223 (2020)
   PUBMED   32745297
  REMARK    GeneRIF: MEK5/ERK5 signaling mediates IL-4-induced M2 macrophage
            differentiation through regulation of c-Myc expression.
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Sanchez-Fdez,A., Ortiz-Ruiz,M.J., Re-Louhau,M.F., Ramos,I.,
            Blanco-Munez,O., Ludena,D., Abad,M., Sanchez-Martin,M.,
            Pandiella,A. and Esparis-Ogando,A.
  TITLE     MEK5 promotes lung adenocarcinoma
  JOURNAL   Eur Respir J 53 (2), 1801327 (2019)
   PUBMED   30442718
  REMARK    GeneRIF: MEK5 promotes lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Nakamura,K. and Johnson,G.L.
  TITLE     PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain
            for activation of the ERK5 pathway
  JOURNAL   J Biol Chem 278 (39), 36989-36992 (2003)
   PUBMED   12912994
  REMARK    GeneRIF: PB1 domain mediates the association of MEKK2 and MEKK3
            with MEK5 and that the respective PB1 domains of these kinases are
            critical for regulation of the ERK5 pathway.
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Lamark,T., Perander,M., Outzen,H., Kristiansen,K., Overvatn,A.,
            Michaelsen,E., Bjorkoy,G. and Johansen,T.
  TITLE     Interaction codes within the family of mammalian Phox and Bem1p
            domain-containing proteins
  JOURNAL   J Biol Chem 278 (36), 34568-34581 (2003)
   PUBMED   12813044
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Nicol,R.L., Frey,N., Pearson,G., Cobb,M., Richardson,J. and
            Olson,E.N.
  TITLE     Activated MEK5 induces serial assembly of sarcomeres and eccentric
            cardiac hypertrophy
  JOURNAL   EMBO J 20 (11), 2757-2767 (2001)
   PUBMED   11387209
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Kamakura,S., Moriguchi,T. and Nishida,E.
  TITLE     Activation of the protein kinase ERK5/BMK1 by receptor tyrosine
            kinases. Identification and characterization of a signaling pathway
            to the nucleus
  JOURNAL   J Biol Chem 274 (37), 26563-26571 (1999)
   PUBMED   10473620
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC124753.3 and AC160392.2.
            
            On or before May 4, 2006 this sequence version replaced
            XP_986739.1, XP_986702.1, XP_986663.1, XP_986623.1, XP_986571.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK159261.1, AB019374.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 33.96 cM"
     Protein         1..448
                     /product="dual specificity mitogen-activated protein
                     kinase kinase 5 isoform 1"
                     /EC_number="2.7.12.2"
                     /note="dual specificity mitogen-activated protein kinase
                     kinase 5; MAP kinase kinase 5; MAPK/ERK kinase 5"
                     /calculated_mol_wt=49974
     Region          17..107
                     /region_name="PB1_Map2k5"
                     /note="PB1 domain is essential part of the
                     mitogen-activated protein kinase kinase 5 (Map2k5, alias
                     MEK5) one of the key member of the signaling kinases
                     cascade which involved in angiogenesis and early
                     cardiovascular development. The PB1 domain of Map2k5...;
                     cd06395"
                     /db_xref="CDD:99717"
     Region          18..25
                     /region_name="Interaction with MAPK7.
                     /evidence=ECO:0000269|PubMed:16507987"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVS7.1)"
     Site            order(64,66,68,77)
                     /site_type="other"
                     /note="PB1 interaction surface [polypeptide binding]"
                     /db_xref="CDD:99717"
     Region          64..68
                     /region_name="Interaction with MAP3K2/MAP3K3.
                     /evidence=ECO:0000269|PubMed:12813044,
                     ECO:0000269|PubMed:16507987"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVS7.1)"
     Region          116..144
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVS7.1)"
     Region          117..131
                     /region_name="Interaction with MAPK7.
                     /evidence=ECO:0000269|PubMed:16507987"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVS7.1)"
     Region          164..442
                     /region_name="PKc_MKK5"
                     /note="Catalytic domain of the dual-specificity Protein
                     Kinase, Mitogen-activated protein Kinase Kinase 5;
                     cd06619"
                     /db_xref="CDD:132950"
     Site            order(172..176,180,193,195,225,241..244,247..248,251,283,
                     285..288,290,300..301,304,316..319,321,348,357)
                     /site_type="active"
                     /db_xref="CDD:132950"
     Site            order(172..176,178,180,193,195,225,241..244,247..248,
                     250..251,285,287..288,290,301)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:132950"
     Site            order(175..176,283,285..287,304,316..319,321,348,357)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:132950"
     Site            300..321
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:132950"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13163; propagated from
                     UniProtKB/Swiss-Prot (Q9WVS7.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13163; propagated from
                     UniProtKB/Swiss-Prot (Q9WVS7.1)"
     CDS             1..448
                     /gene="Map2k5"
                     /gene_synonym="Mapkk5; MEK5; Prkmk5"
                     /coded_by="NM_011840.3:646..1992"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS23269.1"
                     /db_xref="GeneID:23938"
                     /db_xref="MGI:MGI:1346345"
ORIGIN      
        1 mlwlalgpfc amenqvlvir ikipnsgavd wtvhsgpqll frdvldvigq vlpeatttaf
       61 eyededgdri tvrsdeemka mlsyyystvm eqqvngqlie plqifprack ppgernihgl
      121 kvntragpsq htspvvsdsl psnslkkssa elrkilangq mneqdiryrd tlghgnggtv
      181 ykahhvpsgk ilavkvilld itlelqkqim seleilykcd ssyiigfyga ffvenrisic
      241 tefmdggsld vyrkipehvl griavavvkg ltylwslkil hrdvkpsnml vntggqvklc
      301 dfgvstqlvn siaktyvgtn aymaperisg eqygihsdvw slgisfmela lgrfpypqiq
      361 knqgslmplq llqcivdeds pvlplgefse pfvhfitqcm rkqpkerpap eelmghpfiv
      421 qfndgnstvv smwvcralee rrsqqgpp
//
LOCUS       NP_542389                319 aa            linear   PRI 27-APR-2025
DEFINITION  N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)
            [Homo sapiens].
ACCESSION   NP_542389
VERSION     NP_542389.1
DBSOURCE    REFSEQ: accession NM_080658.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Yu,B., Zheng,Y., Alexander,D., Morrison,A.C., Coresh,J. and
            Boerwinkle,E.
  TITLE     Genetic determinants influencing human serum metabolome among
            African Americans
  JOURNAL   PLoS Genet 10 (3), e1004212 (2014)
   PUBMED   24625756
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   8  (residues 1 to 319)
  AUTHORS   Chen,Y.R., Chen,T.Y., Zhang,S.L., Lin,S.M., Zhao,Y.R., Ye,F.,
            Zhang,X., Shi,L., Dang,S.S. and Liu,M.
  TITLE     Identification of a novel protein binding to hepatitis C virus core
            protein
  JOURNAL   J Gastroenterol Hepatol 24 (7), 1300-1304 (2009)
   PUBMED   19486448
  REMARK    GeneRIF: Suggest that ACY3 is an HCV core binding protein, which
            may play a role in the development of HCV-associated diseases.
REFERENCE   9  (residues 1 to 319)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   10 (residues 1 to 319)
  AUTHORS   Pushkin,A., Carpenito,G., Abuladze,N., Newman,D., Tsuprun,V.,
            Ryazantsev,S., Motemoturu,S., Sassani,P., Solovieva,N.,
            Dukkipati,R. and Kurtz,I.
  TITLE     Structural characterization, tissue distribution, and functional
            expression of murine aminoacylase III
  JOURNAL   Am J Physiol Cell Physiol 286 (4), C848-C856 (2004)
   PUBMED   14656720
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003385.2 and BC008689.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008689.1, SRR5189664.85078.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000255082.8/ ENSP00000255082.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..319
                     /product="N-acyl-aromatic-L-amino acid amidohydrolase
                     (carboxylate-forming)"
                     /EC_number="3.5.1.114"
                     /note="acylase III; aspartoacylase-2; hepatitis C virus
                     core-binding protein 1; aspartoacylase (aminocyclase) 3;
                     aspartoacylase (aminoacylase) 3; HCV core-binding protein
                     1"
                     /calculated_mol_wt=35110
     Region          1..210
                     /region_name="Hydrolytic domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HD9.1)"
     Region          11..300
                     /region_name="Peptidase_M14_like"
                     /note="M14 family of metallocarboxypeptidases and related
                     proteins; cl11393"
                     /db_xref="CDD:472171"
     Site            order(21,24,63,70..71,116..117,127,164,168,178)
                     /site_type="active"
                     /db_xref="CDD:349480"
     Region          211..318
                     /region_name="Shielding domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HD9.1)"
     CDS             1..319
                     /gene="ACY3"
                     /gene_synonym="ACY-3; ASPA2; HCBP1"
                     /coded_by="NM_080658.2:243..1202"
                     /db_xref="CCDS:CCDS8175.1"
                     /db_xref="GeneID:91703"
                     /db_xref="HGNC:HGNC:24104"
                     /db_xref="MIM:614413"
ORIGIN      
        1 mcslpvprep lrrvavtggt hgnemsgvyl arhwlhapae lqrasfsavp vlanpaatsg
       61 crryvdhdln rtftssflns rptpddpyev trarelnqll gpkasgqafd fvldlhntta
      121 nmgtcliaks shevfamhlc rhlqlqypel scqvflyqrs geesynldsv aknglglelg
      181 pqpqgvlrad ifsrmrtlva tvldfielfn qgtafpafem eayrpvgvvd fprteaghla
      241 gtvhpqlqdr dfqplqpgap ifqmfsgedl lyegestvyp vfineaayye kgvafvqtek
      301 ftftvpampa ltpapspas
//
LOCUS       NP_066575                575 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 8 [Homo sapiens].
ACCESSION   NP_066575
VERSION     NP_066575.2
DBSOURCE    REFSEQ: accession NM_021089.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Zhang,Y., Yang,Y., Hou,Y., Yan,W., Zhang,X., Huang,X., Song,Q.,
            He,F., Wang,J., Sun,A. and Tian,C.
  TITLE     ZNF8 promotes progression of gastrointestinal cancers via a
            p53-dependent mechanism
  JOURNAL   Cell Signal 123, 111354 (2024)
   PUBMED   39173856
  REMARK    GeneRIF: ZNF8 promotes progression of gastrointestinal cancers via
            a p53-dependent mechanism.
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Geng,W., An,J., Dong,K., Zhang,H., Zhang,X., Liu,Y., Xu,R., Liu,Y.,
            Huang,X., Song,H., Yan,W., Sun,A., He,F., Wang,J., Gao,H. and
            Tian,C.
  TITLE     ZNF8 Orchestrates with Smad3 to Promote Lung Metastasis by
            Recruiting SMYD3 in Breast Cancer
  JOURNAL   Adv Sci (Weinh) 11 (40), e2404904 (2024)
   PUBMED   39225541
  REMARK    GeneRIF: ZNF8 Orchestrates with Smad3 to Promote Lung Metastasis by
            Recruiting SMYD3 in Breast Cancer.
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Yang,H., Sun,W., Bi,T., Sun,J., Lu,Z., Li,J. and Wei,H.
  TITLE     ZNF8-miR-552-5p Axis Modulates ACSL4-Mediated Ferroptosis in
            Hepatocellular Carcinoma
  JOURNAL   DNA Cell Biol 42 (6), 336-347 (2023)
   PUBMED   37126948
  REMARK    GeneRIF: ZNF8-miR-552-5p Axis Modulates ACSL4-Mediated Ferroptosis
            in Hepatocellular Carcinoma.
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 575)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   6  (residues 1 to 575)
  AUTHORS   Jiao,K., Zhou,Y. and Hogan,B.L.
  TITLE     Identification of mZnf8, a mouse Kruppel-like transcriptional
            repressor, as a novel nuclear interaction partner of Smad1
  JOURNAL   Mol Cell Biol 22 (21), 7633-7644 (2002)
   PUBMED   12370310
REFERENCE   7  (residues 1 to 575)
  AUTHORS   Lania,L., Donti,E., Pannuti,A., Pascucci,A., Pengue,G.,
            Feliciello,I., La Mantia,G., Lanfrancone,L. and Pelicci,P.G.
  TITLE     cDNA isolation, expression analysis, and chromosomal localization
            of two human zinc finger genes
  JOURNAL   Genomics 6 (2), 333-340 (1990)
   PUBMED   2106481
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK093110.1, AK225825.1 and AC020915.6.
            
            On May 17, 2008 this sequence version replaced NP_066575.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225825.1, AK093110.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000621650.2/ ENSP00000477716.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..575
                     /product="zinc finger protein 8"
                     /note="zinc finger protein 272; zinc finger protein 8
                     (clone HF.18); zinc finger protein HF.18"
                     /calculated_mol_wt=64839
     Region          25..85
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          92..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17098.2)"
     Region          <167..404
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          210..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17098.2)"
     Region          259..279
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(264,266,268,270..271,274..275,278,292,294,298..299,
                     302..303,306,320,322,324,326..327,330..331,334)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          287..307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          315..335
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          343..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          371..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          397..419
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          399..419
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          467..489
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          488..533
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17098.2)"
     CDS             1..575
                     /gene="ZNF8"
                     /gene_synonym="HF.18; Zfp128"
                     /coded_by="NM_021089.3:128..1855"
                     /db_xref="CCDS:CCDS12974.1"
                     /db_xref="GeneID:7554"
                     /db_xref="HGNC:HGNC:13154"
                     /db_xref="MIM:194532"
ORIGIN      
        1 mdpedegvag vmsvgppaar lqepvtfrdv avdftqeewg qldptqrily rdvmletfgh
       61 llsigpelpk pevisqleqg telwvaergt tqgchpawep rsesqasrke eglpeeepsh
      121 vtgregfptd apypttlgkd recqsqslal keqnnlkqle fglkeapvqd qgyktlrlre
      181 ncvlssspnp fpeisrgeyl ytydsqitds ehnsslvsqq tgspgkqpge nsdchrdssq
      241 aipiteltks qvqdkpykct dcgksfnhna hltvhkriht gerpymckec gkafsqnssl
      301 vqherihtgd kpykcaecgk sfchsthltv hrrihtgekp yecqdcgraf nqnsslgrhk
      361 rthtgekpyt csvcgksfsr ttclflhlrt hteerpyecn hcgkgfrhss slaqhqrkha
      421 gekpfecrqr lifeqtpalt khewtealgc dpplsqdert hrsdrpfkcn qcgkcfiqss
      481 hlirhqitht reeqphgrsr rreqsssrns hlvqhqhpns rkssaggaka gqpesralal
      541 fdiqkimqek npvhvigvee psvgasmlfd irest
//
LOCUS       NP_001476                348 aa            linear   PRI 27-APR-2025
DEFINITION  homeobox protein GBX-2 isoform 1 [Homo sapiens].
ACCESSION   NP_001476
VERSION     NP_001476.2
DBSOURCE    REFSEQ: accession NM_001485.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Lin,Y.H., Zhang,B.Y. and Chen,Z.S.
  TITLE     circRERE regulates the expression of GBX2 through miR-1299 and
            ZC3H13/N6-methyladenosine (m6A) to promote growth and invasion of
            hepatocellular carcinoma cells
  JOURNAL   J Biosci 47 (2022)
   PUBMED   36222159
  REMARK    GeneRIF: circRERE regulates the expression of GBX2 through miR-1299
            and ZC3H13/N(6)-methyladenosine (m(6)A) to promote growth and
            invasion of hepatocellular carcinoma cells.
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Chen,X., Cheng,P. and Hu,C.
  TITLE     LncRNA FEZF1-AS1 accelerates the migration and invasion of
            laryngeal squamous cell carcinoma cells through miR-4497 targeting
            GBX2
  JOURNAL   Eur Arch Otorhinolaryngol 278 (5), 1523-1535 (2021)
   PUBMED   33550476
  REMARK    GeneRIF: LncRNA FEZF1-AS1 accelerates the migration and invasion of
            laryngeal squamous cell carcinoma cells through miR-4497 targeting
            GBX2.
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Li,X., Zhang,F., Ma,J., Ruan,X., Liu,X., Zheng,J., Liu,Y., Cao,S.,
            Shen,S., Shao,L., Cai,H., Li,Z. and Xue,Y.
  TITLE     NCBP3/SNHG6 inhibits GBX2 transcription in a histone modification
            manner to facilitate the malignant biological behaviour of glioma
            cells
  JOURNAL   RNA Biol 18 (1), 47-63 (2021)
   PUBMED   32618493
  REMARK    GeneRIF: NCBP3/SNHG6 inhibits GBX2 transcription in a histone
            modification manner to facilitate the malignant biological
            behaviour of glioma cells.
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Wang,Y., Hui,J., Li,R., Fu,Q., Yang,P., Xiao,Y. and Hui,J.
  TITLE     GBX2, as a tumor promoter in lung adenocarcinoma, enhances cells
            viability, invasion and migration by regulating the AKT/ERK
            signaling pathway
  JOURNAL   J Gene Med 22 (2), e3147 (2020)
   PUBMED   31758726
  REMARK    GeneRIF: GBX2, as a tumor promoter in lung adenocarcinoma, enhances
            cells viability, invasion and migration by regulating the AKT/ERK
            signaling pathway.
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Jeyapala,R., Savio,A.J., Olkhov-Mitsel,E., Kamdar,S., Zhao,F.,
            Cuizon,C., Liu,R.S.C., Zlotta,A., Fleshner,N., van der Kwast,T. and
            Bapat,B.
  TITLE     GBX2 Methylation Is a Novel Prognostic Biomarker and Improves
            Prediction of Biochemical Recurrence Among Patients with Prostate
            Cancer Negative for Intraductal Carcinoma and Cribriform
            Architecture
  JOURNAL   Eur Urol Oncol 2 (3), 231-238 (2019)
   PUBMED   31200836
  REMARK    GeneRIF: Gastrulation brain homeobox 2 (GBX2) methylation is
            associated with Gleason score (GS), pathologic stage (pT), and
            biochemical recurrence (BCR) in prostate cancer (PCa). Among
            intraductal carcinoma/cribriform architecture (IDC/C)-negative
            patients, GBX2 methylation improves prediction of BCR.  Loss of
            TET2 in prostate cells results in greater GBX2 methylation.
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Gao,A.C., Lou,W. and Isaacs,J.T.
  TITLE     Enhanced GBX2 expression stimulates growth of human prostate cancer
            cells via transcriptional up-regulation of the interleukin 6 gene
  JOURNAL   Clin Cancer Res 6 (2), 493-497 (2000)
   PUBMED   10690529
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Gao,A.C., Lou,W. and Isaacs,J.T.
  TITLE     Down-regulation of homeobox gene GBX2 expression inhibits human
            prostate cancer clonogenic ability and tumorigenicity
  JOURNAL   Cancer Res 58 (7), 1391-1394 (1998)
   PUBMED   9537237
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Kowenz-Leutz,E., Herr,P., Niss,K. and Leutz,A.
  TITLE     The homeobox gene GBX2, a target of the myb oncogene, mediates
            autocrine growth and monocyte differentiation
  JOURNAL   Cell 91 (2), 185-195 (1997)
   PUBMED   9346236
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Lin,X., Swaroop,A., Vaccarino,F.M., Murtha,M.T., Haas,M., Ji,X.,
            Ruddle,F.H. and Leckman,J.F.
  TITLE     Characterization and sequence analysis of the human
            homeobox-containing gene GBX2
  JOURNAL   Genomics 31 (3), 335-342 (1996)
   PUBMED   8838315
  REMARK    GeneRIF: The accession number for the cDNA listed for the sequence
            data at the bottom of page 335 on the left side is incorrect. It
            should read U31468 instead of U31458.
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Matsui,T., Hirai,M., Hirano,M. and Kurosawa,Y.
  TITLE     The HOX complex neighbored by the EVX gene, as well as two other
            homeobox-containing genes, the GBX-class and the EN-class, are
            located on the same chromosomes 2 and 7 in humans
  JOURNAL   FEBS Lett 336 (1), 107-110 (1993)
   PUBMED   7903253
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079135.6, BC137448.1, BF115559.1, AA176205.1 and BE463746.1.
            
            On Mar 19, 2004 this sequence version replaced NP_001476.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC137449.1, AF118452.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306318.5/ ENSP00000302251.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.2"
     Protein         1..348
                     /product="homeobox protein GBX-2 isoform 1"
                     /note="homeobox protein GBX-2; gastrulation and
                     brain-specific homeobox protein 2"
                     /calculated_mol_wt=37217
     Region          59..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52951.3)"
     Region          111..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52951.3)"
     Region          179..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52951.3)"
     Region          248..304
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..348
                     /gene="GBX2"
                     /coded_by="NM_001485.4:416..1462"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2515.1"
                     /db_xref="GeneID:2637"
                     /db_xref="HGNC:HGNC:4186"
                     /db_xref="MIM:601135"
ORIGIN      
        1 msaafppslm mmqrplgsst afsidsligs ppqpspghfv ytgypmfmpy rpvvlppppp
       61 pppalpqaal qpalppahph hqipslptgf csslaqgmal tstlmatlpg gfsaspqhqe
      121 aaaarkfapq plpgggnfdk aealqadaed gkgflakegs llafsaaetv qaslvgavrg
      181 qgkdeskved dpkgkeesfs lesdvdyssd dnltgqaahk eedpghalee tppssgaags
      241 ttstgknrrr rtaftseqll elekefhckk ylsltersqi ahalklsevq vkiwfqnrra
      301 kwkrvkagna nsktgepsrn pkivvpipvh vsrfairsqh qqleqarp
//
LOCUS       NP_004778               1529 aa            linear   PRI 27-APR-2025
DEFINITION  slit homolog 2 protein isoform 1 precursor [Homo sapiens].
ACCESSION   NP_004778
VERSION     NP_004778.1
DBSOURCE    REFSEQ: accession NM_004787.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1529)
  AUTHORS   Xia,Y., Jiang,T., Li,Y., Gu,C., Lv,J., Lu,C., Xu,P., Fang,L.,
            Chen,Z., Liu,H., Zhang,D., Xu,H., Yang,L., Xu,Z. and Wang,L.
  TITLE     circVAPA-rich small extracellular vesicles derived from gastric
            cancer promote neural invasion by inhibiting SLIT2 expression in
            neuronal cells
  JOURNAL   Cancer Lett 592, 216926 (2024)
   PUBMED   38714291
  REMARK    GeneRIF: circVAPA-rich small extracellular vesicles derived from
            gastric cancer promote neural invasion by inhibiting SLIT2
            expression in neuronal cells.
REFERENCE   2  (residues 1 to 1529)
  AUTHORS   He,C., Gu,L., Li,A., Li,Y., Xiao,R., Liao,J., Mu,J., Gan,Y.,
            Peng,M., Mohan,G., Liu,W., Xu,L. and Guo,S.
  TITLE     Recombinant Slit2 attenuates tracheal fibroblast activation in
            benign central airway obstruction by inhibiting the TGF-beta1/Smad3
            signaling pathway
  JOURNAL   Mol Cell Probes 73, 101947 (2024)
   PUBMED   38122948
  REMARK    GeneRIF: Recombinant Slit2 attenuates tracheal fibroblast
            activation in benign central airway obstruction by inhibiting the
            TGF-beta1/Smad3 signaling pathway.
REFERENCE   3  (residues 1 to 1529)
  AUTHORS   Bhosle,V.K., Sun,C., Patel,S., Ho,T.W.W., Westman,J.,
            Ammendolia,D.A., Langari,F.M., Fine,N., Toepfner,N., Li,Z.,
            Sharma,M., Glogauer,J., Capurro,M.I., Jones,N.L., Maynes,J.T.,
            Lee,W.L., Glogauer,M., Grinstein,S. and Robinson,L.A.
  TITLE     The chemorepellent, SLIT2, bolsters innate immunity against
            Staphylococcus aureus
  JOURNAL   Elife 12, e87392 (2023)
   PUBMED   37773612
  REMARK    GeneRIF: The chemorepellent, SLIT2, bolsters innate immunity
            against Staphylococcus aureus.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1529)
  AUTHORS   Seiradake,E., von Philipsborn,A.C., Henry,M., Fritz,M.,
            Lortat-Jacob,H., Jamin,M., Hemrika,W., Bastmeyer,M., Cusack,S. and
            McCarthy,A.A.
  TITLE     Structure and functional relevance of the Slit2 homodimerization
            domain
  JOURNAL   EMBO Rep 10 (7), 736-741 (2009)
   PUBMED   19498462
  REMARK    GeneRIF: Fourth Slit2 domain heparan sulphate binding contributes
            to a Slit-Robo signalling mechanism more intricate than previously
            thought.
REFERENCE   5  (residues 1 to 1529)
  AUTHORS   Li,H.S., Chen,J.H., Wu,W., Fagaly,T., Zhou,L., Yuan,W., Dupuis,S.,
            Jiang,Z.H., Nash,W., Gick,C., Ornitz,D.M., Wu,J.Y. and Rao,Y.
  TITLE     Vertebrate slit, a secreted ligand for the transmembrane protein
            roundabout, is a repellent for olfactory bulb axons
  JOURNAL   Cell 96 (6), 807-818 (1999)
   PUBMED   10102269
REFERENCE   6  (residues 1 to 1529)
  AUTHORS   Brose,K., Bland,K.S., Wang,K.H., Arnott,D., Henzel,W.,
            Goodman,C.S., Tessier-Lavigne,M. and Kidd,T.
  TITLE     Slit proteins bind Robo receptors and have an evolutionarily
            conserved role in repulsive axon guidance
  JOURNAL   Cell 96 (6), 795-806 (1999)
   PUBMED   10102268
REFERENCE   7  (residues 1 to 1529)
  AUTHORS   Wang,K.H., Brose,K., Arnott,D., Kidd,T., Goodman,C.S., Henzel,W.
            and Tessier-Lavigne,M.
  TITLE     Biochemical purification of a mammalian slit protein as a positive
            regulator of sensory axon elongation and branching
  JOURNAL   Cell 96 (6), 771-784 (1999)
   PUBMED   10102266
REFERENCE   8  (residues 1 to 1529)
  AUTHORS   Georgas,K., Burridge,L., Smith,K., Holmes,G.P., Chenevix-Trench,G.,
            Ioannou,P.A. and Little,M.H.
  TITLE     Assignment of the human slit homologue SLIT2 to human chromosome
            band 4p15.2
  JOURNAL   Cytogenet Cell Genet 86 (3-4), 246-247 (1999)
   PUBMED   10575218
REFERENCE   9  (residues 1 to 1529)
  AUTHORS   Itoh,A., Miyabayashi,T., Ohno,M. and Sakano,S.
  TITLE     Cloning and expressions of three mammalian homologues of Drosophila
            slit suggest possible roles for Slit in the formation and
            maintenance of the nervous system
  JOURNAL   Brain Res Mol Brain Res 62 (2), 175-186 (1998)
   PUBMED   9813312
REFERENCE   10 (residues 1 to 1529)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA721496.1, AC096718.3,
            BC117190.1, AK126459.1, DB207352.1, CV370469.1, BF112143.1,
            AC021118.6, BM474839.1, BI494498.1 and AA489463.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the slit family of secreted
            glycoproteins, which are ligands for the Robo family of
            immunoglobulin receptors. Slit proteins play highly conserved roles
            in axon guidance and neuronal migration and may also have functions
            during other cell migration processes including leukocyte
            migration. Members of the slit family are characterized by an
            N-terminal signal peptide, four leucine-rich repeats, nine
            epidermal growth factor repeats, and a C-terminal cysteine knot.
            Proteolytic processing of this protein gives rise to an N-terminal
            fragment that contains the four leucine-rich repeats and five
            epidermal growth factor repeats and a C-terminal fragment that
            contains four epidermal growth factor repeats and the cysteine
            knot. Both full length and cleaved proteins are secreted
            extracellularly and can function in axon repulsion as well as other
            specific processes. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB017168.1, BC117190.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000504154.6/ ENSP00000422591.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.31"
     Protein         1..1529
                     /product="slit homolog 2 protein isoform 1 precursor"
                     /note="slit homolog 2 protein"
                     /calculated_mol_wt=166751
     sig_peptide     1..30
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
                     /calculated_mol_wt=3138
     Region          27..58
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     mat_peptide     31..1529
                     /product="Slit homolog 2 protein. /id=PRO_0000007725"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
                     /calculated_mol_wt=166751
     mat_peptide     31..1121
                     /product="Slit homolog 2 protein N-product.
                     /id=PRO_0000007726"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
                     /calculated_mol_wt=122245
     Region          38..56
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <56..>211
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          56..77
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          57..80
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Region          80..101
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          81..104
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          104..125
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          105..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          128..149
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          129..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          152..173
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          153..176
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          176..197
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          177..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          182..>319
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Region          201..325
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          301..322
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          <319..667
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          325..346
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          326..349
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          349..370
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          350..370
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          373..394
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          374..397
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          397..418
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          398..419
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          422..523
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          515..>861
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          534..555
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          537..559
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          559..580
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          560..583
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            564
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Region          583..604
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          584..607
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          607..628
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          608..631
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            623
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Region          631..652
                     /region_name="LRR 16"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          632..655
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          656..747
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          748..778
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          755..777
                     /region_name="LRR 17"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          778..799
                     /region_name="LRR 18"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          779..802
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            794
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Site            799
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Region          802..823
                     /region_name="LRR 19"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          803..826
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          826..847
                     /region_name="LRR 20"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
     Region          827..848
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          832..>1013
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          851..863
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          998..1034
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(998,1001,1015)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1009
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Site            1010
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Site            1019
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Region          1038..1073
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1076..1112
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1076,1079,1093)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1121..1122
                     /site_type="cleavage"
                     /note="Cleavage; propagated from UniProtKB/Swiss-Prot
                     (O94813.1)"
     mat_peptide     1122..1529
                     /product="Slit homolog 2 protein C-product.
                     /id=PRO_0000007727"
                     /note="propagated from UniProtKB/Swiss-Prot (O94813.1)"
                     /calculated_mol_wt=44525
     Region          <1130..1157
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1183..1316
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Site            1183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Site            1266
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     Site            1300
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94813.1)"
     CDS             1..1529
                     /gene="SLIT2"
                     /gene_synonym="SLIL3; Slit-2"
                     /coded_by="NM_004787.4:1912..6501"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3426.1"
                     /db_xref="GeneID:9353"
                     /db_xref="HGNC:HGNC:11086"
                     /db_xref="MIM:603746"
ORIGIN      
        1 mrgvgwqmls lslglvlail nkvapqacpa qcscsgstvd chglalrsvp rniprnterl
       61 dlngnnitri tktdfaglrh lrvlqlmenk istiergafq dlkelerlrl nrnhlqlfpe
      121 llflgtakly rldlsenqiq aiprkafrga vdiknlqldy nqisciedga fralrdlevl
      181 tlnnnnitrl svasfnhmpk lrtfrlhsnn lycdchlawl sdwlrqrprv glytqcmgps
      241 hlrghnvaev qkrefvcsgh qsfmapscsv lhcpaactcs nnivdcrgkg lteiptnlpe
      301 titeirleqn tikvippgaf spykklrrid lsnnqisela pdafqglrsl nslvlygnki
      361 telpkslfeg lfslqlllln ankinclrvd afqdlhnlnl lslydnklqt iakgtfsplr
      421 aiqtmhlaqn pficdchlkw ladylhtnpi etsgarctsp rrlankrigq ikskkfrcsa
      481 keqyfipgte dyrsklsgdc fadlacpekc rcegttvdcs nqklnkipeh ipqytaelrl
      541 nnneftvlea tgifkklpql rkinfsnnki tdieegafeg asgvneillt snrlenvqhk
      601 mfkgleslkt lmlrsnritc vgndsfigls svrllslydn qittvapgaf dtlhslstln
      661 llanpfncnc ylawlgewlr kkrivtgnpr cqkpyflkei piqdvaiqdf tcddgnddns
      721 csplsrcpte ctcldtvvrc snkglkvlpk giprdvtely ldgnqftlvp kelsnykhlt
      781 lidlsnnris tlsnqsfsnm tqlltlilsy nrlrcipprt fdglkslrll slhgndisvv
      841 pegafndlsa lshlaiganp lycdcnmqwl sdwvkseyke pgiarcagpg emadkllltt
      901 pskkftcqgp vdvnilakcn pclsnpcknd gtcnsdpvdf yrctcpygfk gqdcdvpiha
      961 cisnpckhgg tchlkegeed gfwcicadgf egencevnvd dcedndcenn stcvdginny
     1021 tclcppeytg elceekldfc aqdlnpcqhd skciltpkgf kcdctpgyvg ehcdidfddc
     1081 qdnkckngah ctdavngytc icpegysglf cefsppmvlp rtspcdnfdc qngaqcivri
     1141 nepicqclpg yqgekceklv svnfinkesy lqipsakvrp qtnitlqiat dedsgillyk
     1201 gdkdhiavel yrgrvrasyd tgshpasaiy svetindgnf hivellaldq slslsvdggn
     1261 pkiitnlskq stlnfdsply vggmpgksnv aslrqapgqn gtsfhgcirn lyinselqdf
     1321 qkvpmqtgil pgcepchkkv cahgtcqpss qagftcecqe gwmgplcdqr tndpclgnkc
     1381 vhgtclpina fsysckcleg hggvlcdeee dlfnpcqaik ckhgkcrlsg lgqpycecss
     1441 gytgdscdre iscrgerird yyqkqqgyaa cqttkkvsrl ecrggcaggq ccgplrskrr
     1501 kysfectdgs sfvdevekvv kcgctrcvs
//
LOCUS       NP_001356461             822 aa            linear   PRI 27-APR-2025
DEFINITION  BDNF/NT-3 growth factors receptor isoform c precursor [Homo
            sapiens].
ACCESSION   NP_001356461
VERSION     NP_001356461.1
DBSOURCE    REFSEQ: accession NM_001369532.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Gupta,R., Dittmeier,M., Wohlleben,G., Nickl,V., Bischler,T.,
            Luzak,V., Wegat,V., Doll,D., Sodmann,A., Bady,E., Langlhofer,G.,
            Wachter,B., Havlicek,S., Gupta,J., Horn,E., Luningschror,P.,
            Villmann,C., Polat,B., Wischhusen,J., Monoranu,C.M., Kuper,J. and
            Blum,R.
  TITLE     Atypical cellular responses mediated by intracellular constitutive
            active TrkB (NTRK2) kinase domains and a solely intracellular
            NTRK2-fusion oncogene
  JOURNAL   Cancer Gene Ther 31 (9), 1357-1379 (2024)
   PUBMED   39039193
  REMARK    GeneRIF: Atypical cellular responses mediated by intracellular
            constitutive active TrkB (NTRK2) kinase domains and a solely
            intracellular NTRK2-fusion oncogene.
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Zhang,X., Zhang,Y., Yan,H., Yu,H., Zhang,D., Mattay,V.S., Tan,H.Y.
            and Yue,W.
  TITLE     Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2
  JOURNAL   BMC Med 22 (1), 146 (2024)
   PUBMED   38561734
  REMARK    GeneRIF: Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Ikhlef,L., Yassine,M., Chandouri,B., Riviere,L., Naves,T.,
            Dmytruk,N., Gachard,N., Jauberteau,M.O. and Gallet,P.F.
  TITLE     Targeting the NTSR2/TrkB oncogenic pathway in chronic lymphocytic
            leukemia
  JOURNAL   Sci Rep 14 (1), 6084 (2024)
   PUBMED   38480783
  REMARK    GeneRIF: Targeting the NTSR2/TrkB oncogenic pathway in chronic
            lymphocytic leukemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Wang,Y., Liang,J., Xu,B., Yang,J., Wu,Z. and Cheng,L.
  TITLE     TrkB/BDNF signaling pathway and its small molecular agonists in CNS
            injury
  JOURNAL   Life Sci 336, 122282 (2024)
   PUBMED   38008209
  REMARK    GeneRIF: TrkB/BDNF signaling pathway and its small molecular
            agonists in CNS injury.
            Review article
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Luberg,K., Wong,J., Weickert,C.S. and Timmusk,T.
  TITLE     Human TrkB gene: novel alternative transcripts, protein isoforms
            and expression pattern in the prefrontal cerebral cortex during
            postnatal development
  JOURNAL   J Neurochem 113 (4), 952-964 (2010)
   PUBMED   20193039
  REMARK    GeneRIF: Identification of 36 potential TrkB protein isoforms
            suggests high complexity in the synthesis, regulation and function
            of this important neurotrophin receptor emphasizing the need for
            further study of these novel TrkB variants.
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Stoilov,P., Castren,E. and Stamm,S.
  TITLE     Analysis of the human TrkB gene genomic organization reveals novel
            TrkB isoforms, unusual gene length, and splicing mechanism
  JOURNAL   Biochem Biophys Res Commun 290 (3), 1054-1065 (2002)
   PUBMED   11798182
  REMARK    GeneRIF: analysis of TrkB gene reveals novel gene length and
            splicing mechanism
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Haniu,M., Talvenheimo,J., Le,J., Katta,V., Welcher,A. and
            Rohde,M.F.
  TITLE     Extracellular domain of neurotrophin receptor trkB: disulfide
            structure, N-glycosylation sites, and ligand binding
  JOURNAL   Arch Biochem Biophys 322 (1), 256-264 (1995)
   PUBMED   7574684
REFERENCE   8  (residues 1 to 822)
  AUTHORS   Nakagawara,A., Liu,X.G., Ikegaki,N., White,P.S., Yamashiro,D.J.,
            Nycum,L.M., Biegel,J.A. and Brodeur,G.M.
  TITLE     Cloning and chromosomal localization of the human TRK-B tyrosine
            kinase receptor gene (NTRK2)
  JOURNAL   Genomics 25 (2), 538-546 (1995)
   PUBMED   7789988
REFERENCE   9  (residues 1 to 822)
  AUTHORS   Squinto,S.P., Stitt,T.N., Aldrich,T.H., Davis,S., Blanco,S.M.,
            RadzieJewski,C., Glass,D.J., Masiakowski,P., Furth,M.E.,
            Valenzuela,D.M., Distefano,P.S. and Yancopoulos,G.D.
  TITLE     trkB encodes a functional receptor for brain-derived neurotrophic
            factor and neurotrophin-3 but not nerve growth factor
  JOURNAL   Cell 65 (5), 885-893 (1991)
   PUBMED   1710174
REFERENCE   10 (residues 1 to 822)
  AUTHORS   Soppet,D., Escandon,E., Maragos,J., Middlemas,D.S., Reid,S.W.,
            Blair,J., Burton,L.E., Stanton,B.R., Kaplan,D.R., Hunter,T.,
            Nikolics,K. and Parada,L.F.
  TITLE     The neurotrophic factors brain-derived neurotrophic factor and
            neurotrophin-3 are ligands for the trkB tyrosine kinase receptor
  JOURNAL   Cell 65 (5), 895-903 (1991)
   PUBMED   1645620
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390777.13, AL596132.7 and
            AL445532.8.
            
            Summary: This gene encodes a member of the neurotrophic tyrosine
            receptor kinase (NTRK) family. This kinase is a membrane-bound
            receptor that, upon neurotrophin binding, phosphorylates itself and
            members of the MAPK pathway. Signalling through this kinase leads
            to cell differentiation. Mutations in this gene have been
            associated with obesity and mood disorders. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (k), as well as variants c and l,
            encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.12281.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..822
                     /product="BDNF/NT-3 growth factors receptor isoform c
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="BDNF/NT-3 growth factors receptor; tyrosine kinase
                     receptor B; BDNF-tropomyosine receptor kinase B;
                     tropomyosin-related kinase B; neurotrophic tyrosine kinase
                     receptor type 2"
                     /calculated_mol_wt=88320
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3697
     mat_peptide     32..822
                     /product="BDNF/NT-3 growth factors receptor.
                     /id=PRO_0000016727"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
                     /calculated_mol_wt=88320
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          92..150
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          92..113
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          116..137
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          151..195
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          205..283
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          214..218
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          227..230
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          245..252
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            254
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          262..268
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          276..279
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          286..379
                     /region_name="IgI_TrkB_d5"
                     /note="Fifth domain (immunoglobulin-like) of Trk receptor
                     TrkB; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05855"
                     /db_xref="CDD:409441"
     Region          286..294
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409441"
     Region          295..298
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409441"
     Region          301..309
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409441"
     Site            310
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409441"
     Region          312..319
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409441"
     Region          322..325
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409441"
     Site            325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          330..335
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409441"
     Site            order(335,349..350,353)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:409441"
     Site            338
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          341..349
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409441"
     Region          357..365
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409441"
     Region          368..376
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409441"
     Site            412
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Site            431..454
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Region          455..466
                     /region_name="Interaction with MAPK8IP3/JIP3.
                     /evidence=ECO:0000250|UniProtKB:Q63604"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Region          475..498
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            516
                     /site_type="other"
                     /note="Interaction with SHC1. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P15209; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          532..819
                     /region_name="PTKc_TrkB"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Tropomyosin Related Kinase B; cd05093"
                     /db_xref="CDD:270675"
     Site            order(544..548,552,570,572,617..620,623..624,676,680..681,
                     683,694,712..716,725,759)
                     /site_type="active"
                     /db_xref="CDD:270675"
     Site            order(544..545,547..548,552,570,572,617..620,623..624,
                     680..681,683,694)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270675"
     Site            order(676,680,712..716,725,759)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270675"
     Site            693..718
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270675"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q63604; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Site            706
                     /site_type="other"
                     /note="Interaction with SH2D1A. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            706
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q63604; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Site            707
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q63604; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Site            817
                     /site_type="other"
                     /note="Interaction with PLCG1. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            817
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q63604; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     CDS             1..822
                     /gene="NTRK2"
                     /gene_synonym="DEE58; EIEE58; GP145-TrkB; OBHD; trk-B;
                     TRKB"
                     /coded_by="NM_001369532.1:846..3314"
                     /note="isoform c precursor is encoded by transcript
                     variant k"
                     /db_xref="CCDS:CCDS35050.1"
                     /db_xref="GeneID:4915"
                     /db_xref="HGNC:HGNC:8032"
                     /db_xref="MIM:600456"
ORIGIN      
        1 msswirwhgp amarlwgfcw lvvgfwraaf acptsckcsa sriwcsdpsp givafprlep
       61 nsvdpenite ifianqkrle iineddveay vglrnltivd sglkfvahka flknsnlqhi
      121 nftrnkltsl srkhfrhldl selilvgnpf tcscdimwik tlqeaksspd tqdlyclnes
      181 skniplanlq ipncglpsan laapnltvee gksitlscsv agdpvpnmyw dvgnlvskhm
      241 netshtqgsl ritnissdds gkqiscvaen lvgedqdsvn ltvhfaptit flesptsdhh
      301 wcipftvkgn pkpalqwfyn gailneskyi ctkihvtnht eyhgclqldn pthmnngdyt
      361 liakneygkd ekqisahfmg wpgiddganp nypdviyedy gtaandigdt tnrsneipst
      421 dvtdktgreh lsvyavvvia svvgfcllvm lfllklarhs kfgmkgpasv isndddsasp
      481 lhhisngsnt pssseggpda viigmtkipv ienpqyfgit nsqlkpdtfv qhikrhnivl
      541 krelgegafg kvflaecynl cpeqdkilva vktlkdasdn arkdfhreae lltnlqhehi
      601 vkfygvcveg dplimvfeym khgdlnkflr ahgpdavlma egnppteltq sqmlhiaqqi
      661 aagmvylasq hfvhrdlatr nclvgenllv kigdfgmsrd vystdyyrvg ghtmlpirwm
      721 ppesimyrkf ttesdvwslg vvlweiftyg kqpwyqlsnn eviecitqgr vlqrprtcpq
      781 evyelmlgcw qrephmrkni kgihtllqnl akaspvyldi lg
//
LOCUS       NP_001355189              88 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 234 isoform 6 [Mus musculus].
ACCESSION   NP_001355189
VERSION     NP_001355189.1
DBSOURCE    REFSEQ: accession NM_001368260.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Tang,T., Li,L., Tang,J., Li,Y., Lin,W.Y., Martin,F., Grant,D.,
            Solloway,M., Parker,L., Ye,W., Forrest,W., Ghilardi,N., Oravecz,T.,
            Platt,K.A., Rice,D.S., Hansen,G.M., Abuin,A., Eberhart,D.E.,
            Godowski,P., Holt,K.H., Peterson,A., Zambrowicz,B.P. and de
            Sauvage,F.J.
  TITLE     A mouse knockout library for secreted and transmembrane proteins
  JOURNAL   Nat Biotechnol 28 (7), 749-755 (2010)
   PUBMED   20562862
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL671759.10.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.704464.1, BF534453.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 63.26 cM"
     Protein         1..88
                     /product="transmembrane protein 234 isoform 6"
                     /calculated_mol_wt=9052
     Region          <5..74
                     /region_name="TMEM234"
                     /note="Putative transmembrane family 234; cl46810"
                     /db_xref="CDD:481150"
     CDS             1..88
                     /gene="Tmem234"
                     /gene_synonym="1500002D11Rik; 2510006D16Rik;
                     4933407D05Rik"
                     /coded_by="NM_001368260.1:521..787"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:76799"
                     /db_xref="MGI:MGI:1924049"
ORIGIN      
        1 maayylmpfl lnqsgsllyy ltlastdltl avpicnslai vftlivgkvl gediggkeav
       61 agmvltitgi tvcitssvsk tqgqpshs
//
LOCUS       NP_001004304             193 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 740 [Homo sapiens].
ACCESSION   NP_001004304 XP_374982
VERSION     NP_001004304.1
DBSOURCE    REFSEQ: accession NM_001004304.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073573.27, BC053557.1 and AK091946.1.
            
            On Sep 16, 2004 this sequence version replaced XP_374982.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.250393.1,
                                           SRR1803611.223829.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000416904.5/ ENSP00000409463.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..193
                     /product="zinc finger protein 740"
                     /note="oriLyt TD-element-binding protein 7"
                     /calculated_mol_wt=21726
     Region          33..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX6.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NDX6.1)"
     Region          103..123
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(108,110,112,114..115,118..119,122,136,138,142..143,
                     146..147,150,164,166,168,170..171,174..175)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          115..140
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          131..151
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(131,134,147,151)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          143..168
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          159..177
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..193
                     /gene="ZNF740"
                     /gene_synonym="Zfp740"
                     /coded_by="NM_001004304.4:424..1005"
                     /db_xref="CCDS:CCDS44896.1"
                     /db_xref="GeneID:283337"
                     /db_xref="HGNC:HGNC:27465"
                     /db_xref="MIM:620976"
ORIGIN      
        1 maqasllace glagvslvpt aaskkmmlsq iaskqaenge ragspdvlrc ssqghrkdsd
       61 ksrsrkddds lseashskkt vkkvvvveqn gsfqvkipkn fvcehcfgaf rssyhlkrhi
      121 lihtgekpfe cdicdmrfiq kyhlerhkrv hsgekpyqce rchqcfsrtd rllrhkrmcq
      181 gcqsktsdgq fsl
//
LOCUS       NP_057081                475 aa            linear   PRI 27-APR-2025
DEFINITION  methyltransferase-like protein 25B isoform 1 [Homo sapiens].
ACCESSION   NP_057081
VERSION     NP_057081.3
DBSOURCE    REFSEQ: accession NM_015997.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Peterson,R.J. and Marsh,C.L.
  TITLE     The relationship of alpha1-antitrypsin to inflammatory periodontal
            disease
  JOURNAL   J Periodontol 50 (1), 31-35 (1979)
   PUBMED   310876
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590666.8 and BX094595.1.
            
            On Dec 9, 2008 this sequence version replaced NP_057081.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011382.1, SRR1163655.398205.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368216.9/ ENSP00000357199.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.1"
     Protein         1..475
                     /product="methyltransferase-like protein 25B isoform 1"
                     /note="protein RRNAD1; ribosomal RNA adenine dimethylase
                     domain-containing protein 1; ribosomal RNA adenine
                     dimethylase domain containing 1; methyltransferase-like
                     protein 25B"
                     /calculated_mol_wt=52850
     Region          133..293
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
     Site            406..426
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FB5.2)"
     CDS             1..475
                     /gene="METTL25B"
                     /gene_synonym="C1orf66; CGI-41; RRNAD1"
                     /coded_by="NM_015997.4:637..2064"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1154.1"
                     /db_xref="GeneID:51093"
                     /db_xref="HGNC:HGNC:24273"
ORIGIN      
        1 mpgisargls hegrkqlavn ltrvlalyrs ildayiieff tdnlwdtlpc swqealdglk
       61 ppqlatmllg mpgegevvry rsvwpltlla lkstacalaf trmpgfqtps eflenpsqss
      121 rltapfrkhv rpkkqheirr lgelvkklsd ftgctqvvdv gsgqghlsrf malglglmvk
      181 siegdqrlve raqrldqell qalekeekrn pqvvqtsprh sphhvvrwvd ptalceelll
      241 plenpcqgra rllltglhac gdlsvallrh fsccpevval asvgccymkl sdpggyplsq
      301 wvaglpgyel pyrlregach aleeyaerlq kagpglrthc yraaletvir rarpelrrpg
      361 vqgiprvhel kieeyvqrgl qrvgldpqlp lnlaalqahv aqenrvvaff slalllaplv
      421 etlilldrll ylqeqgfhae llpifspels prnlvlvatk mplgqalsvl eteds
//
LOCUS       NP_689478                158 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor BTF3 homolog 4 isoform 1 [Homo sapiens].
ACCESSION   NP_689478 XP_371577 XP_496364
VERSION     NP_689478.1
DBSOURCE    REFSEQ: accession NM_152265.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Lu,B., Lu,T., Shi,J., Sun,P., Zhang,X., Yang,L., Wang,Z. and
            Huang,J.
  TITLE     Basic Transcription Factor 3 Like 4 Enhances Malignant Phenotypes
            through Modulating Tumor Cell Function and Immune Microenvironment
            in Glioma
  JOURNAL   Am J Pathol 194 (5), 772-784 (2024)
   PUBMED   38320629
  REMARK    GeneRIF: Basic Transcription Factor 3 Like 4 Enhances Malignant
            Phenotypes through Modulating Tumor Cell Function and Immune
            Microenvironment in Glioma.
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Ji,Y.H., Ji,J.L., Sun,F.Y., Zeng,Y.Y., He,X.H., Zhao,J.X., Yu,Y.,
            Yu,S.H. and Wu,W.
  TITLE     Quantitative proteomics analysis of chondrogenic differentiation of
            C3H10T1/2 mesenchymal stem cells by iTRAQ labeling coupled with
            on-line two-dimensional LC/MS/MS
  JOURNAL   Mol Cell Proteomics 9 (3), 550-564 (2010)
   PUBMED   20008835
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC070378.1 and AL139156.11.
            
            On or before Mar 11, 2005 this sequence version replaced
            XP_371577.1, XP_496364.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.26945.1,
                                           SRR1803611.61306.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313334.13/ ENSP00000360664.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..158
                     /product="transcription factor BTF3 homolog 4 isoform 1"
                     /note="transcription factor BTF3 homolog 4"
                     /calculated_mol_wt=17139
     Region          4..120
                     /region_name="NAC_BTF3"
                     /note="basal transcription factor BTF3; cd22055"
                     /db_xref="CDD:409234"
     Site            5
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P20290; propagated from
                     UniProtKB/Swiss-Prot (Q96K17.1)"
     Site            22..26
                     /site_type="other"
                     /note="ribosome binding motif"
                     /db_xref="CDD:409234"
     Site            order(52..62,67,69,81..87,89,103..105)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409234"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P20290; propagated from
                     UniProtKB/Swiss-Prot (Q96K17.1)"
     Region          122..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K17.1)"
     CDS             1..158
                     /gene="BTF3L4"
                     /coded_by="NM_152265.5:99..575"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30713.1"
                     /db_xref="GeneID:91408"
                     /db_xref="HGNC:HGNC:30547"
ORIGIN      
        1 mnqeklaklq aqvriggkgt arrkkkvvhr tataddkklq sslkklavnn iagieevnmi
       61 kddgtvihfn npkvqaslsa ntfaitghae akpitemlpg ilsqlgadsl tslrklaeqf
      121 prqvldskap kpedideedd dvpdlvenfd easknean
//
LOCUS       NP_001353501             820 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001353501 XP_016855516
VERSION     NP_001353501.1
DBSOURCE    REFSEQ: accession NM_001366572.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 820)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 820)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 820)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 820)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 820)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 820)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 820)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855516.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.73674.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..820
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 9"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=92398
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <522..>656
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..820
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366572.1:2055..4517"
                     /note="isoform 9 is encoded by transcript variant 12"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels esedkggkma aadsvqqrrq yrrqnqqsss dsgsssssed
      421 erpkrshvkn gevgrrrrhs psrsaspspr krqketsprg rrrrspsppp trrrrspspa
      481 ppprrrrtpt ppprrrtpsp pprrrspspr rysppiqrry spspppkrrt aspppppkrr
      541 aspspppkrr vshspppkqr sspvtkrrsp slsskhrkgs spsrstrear spqpnkrhsp
      601 sprprapqts sspppvrrga ssspqrrqsp spstrpirrv srtpepkkik kaaspspqsv
      661 rrvsssrsvs gspepaakkp pappspvqsq spstnwspav pvkkaksptp spspprnsdq
      721 egggkkkkkk kdkkhkkdkk hkkhkkhkke kavaaaaaaa vtpaaiaaat ttlaqeepva
      781 apepkketes eaednlddle khlrekalrs mrkaqvspqs
//
LOCUS       NP_775107                403 aa            linear   PRI 27-APR-2025
DEFINITION  tripartite motif-containing protein 59 [Homo sapiens].
ACCESSION   NP_775107
VERSION     NP_775107.1
DBSOURCE    REFSEQ: accession NM_173084.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Cheng,P., Wang,Y., Wu,Q., Zhang,H., Fang,W. and Feng,F.
  TITLE     Role of TRIM59 in regulating PPM1A in the pathogenesis of silicosis
            and the intervention effect of tanshinone IIA
  JOURNAL   Biomed Pharmacother 177, 117014 (2024)
   PUBMED   38908195
  REMARK    GeneRIF: Role of TRIM59 in regulating PPM1A in the pathogenesis of
            silicosis and the intervention effect of tanshinone IIA.
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Zhang,L., Li,G. and Li,Y.
  TITLE     TRIM59 suppresses the brain ischaemia/reperfusion injury and
            pyroptosis of microglial through mediating the ubiquitination of
            NLRP3
  JOURNAL   Sci Rep 14 (1), 2511 (2024)
   PUBMED   38291200
  REMARK    GeneRIF: TRIM59 suppresses the brain ischaemia/reperfusion injury
            and pyroptosis of microglial through mediating the ubiquitination
            of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Liu,Y., Zhu,L., Ming,Y., Wu,Z., Zhang,L., Chen,Q. and Qi,Y.
  TITLE     A role of TRIM59 in pulmonary hypertension: modulating the protein
            ubiquitylation modification
  JOURNAL   J Transl Med 21 (1), 821 (2023)
   PUBMED   37978515
  REMARK    GeneRIF: A role of TRIM59 in pulmonary hypertension: modulating the
            protein ubiquitylation modification.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Che,B., Du,Y., Yuan,R., Xiao,H., Zhang,W., Shao,J., Lu,H., Yu,Y.,
            Xiang,M., Hao,L., Zhang,S., Du,X., Liu,X., Zhou,W., Wang,K. and
            Chen,L.
  TITLE     SLC35F2-SYVN1-TRIM59 axis critically regulates ferroptosis of
            pancreatic cancer cells by inhibiting endogenous p53
  JOURNAL   Oncogene 42 (44), 3260-3273 (2023)
   PUBMED   37740007
  REMARK    GeneRIF: SLC35F2-SYVN1-TRIM59 axis critically regulates ferroptosis
            of pancreatic cancer cells by inhibiting endogenous p53.
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Fan,L., Gong,Y., He,Y., Gao,W.Q., Dong,X., Dong,B., Zhu,H.H. and
            Xue,W.
  TITLE     TRIM59 is suppressed by androgen receptor and acts to promote
            lineage plasticity and treatment-induced neuroendocrine
            differentiation in prostate cancer
  JOURNAL   Oncogene 42 (8), 559-571 (2023)
   PUBMED   36544044
  REMARK    GeneRIF: TRIM59 is suppressed by androgen receptor and acts to
            promote lineage plasticity and treatment-induced neuroendocrine
            differentiation in prostate cancer.
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Zhan,W., Han,T., Zhang,C., Xie,C., Gan,M., Deng,K., Fu,M. and
            Wang,J.B.
  TITLE     TRIM59 Promotes the Proliferation and Migration of Non-Small Cell
            Lung Cancer Cells by Upregulating Cell Cycle Related Proteins
  JOURNAL   PLoS One 10 (11), e0142596 (2015)
   PUBMED   26599082
  REMARK    GeneRIF: we knocked down TRIM59 and found that p53 protein
            expression levels did not upregulate, so we proposed that TRIM59
            may promote NSCLC cell growth through other pathways but not the
            p53 signaling pathway
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Zhou,Z., Ji,Z., Wang,Y., Li,J., Cao,H., Zhu,H.H. and Gao,W.Q.
  TITLE     TRIM59 is up-regulated in gastric tumors, promoting ubiquitination
            and degradation of p53
  JOURNAL   Gastroenterology 147 (5), 1043-1054 (2014)
   PUBMED   25046164
  REMARK    GeneRIF: TRIM59 interacts with P53, promoting its ubiquitination
            and degradation, and TRIM59 might promote gastric carcinogenesis
            via this mechanism.
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Kondo,T., Watanabe,M. and Hatakeyama,S.
  TITLE     TRIM59 interacts with ECSIT and negatively regulates NF-kappaB and
            IRF-3/7-mediated signal pathways
  JOURNAL   Biochem Biophys Res Commun 422 (3), 501-507 (2012)
   PUBMED   22588174
  REMARK    GeneRIF: These findings indicate that TRIM59 may serve as a
            multifunctional regulator for innate immune signaling pathways.
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Georgescu,S.P., Li,J.H., Lu,Q., Karas,R.H., Brown,M. and
            Mendelsohn,M.E.
  TITLE     Modulator recognition factor 1, an AT-rich interaction domain
            family member, is a novel corepressor for estrogen receptor alpha
  JOURNAL   Mol Endocrinol 19 (10), 2491-2501 (2005)
   PUBMED   15941852
REFERENCE   10 (residues 1 to 403)
  AUTHORS   Chang,R., Xu,X. and Li,M.D.
  TITLE     Molecular cloning, mapping and characterization of a novel mouse
            RING finger gene, Mrf1
  JOURNAL   Gene 291 (1-2), 241-249 (2002)
   PUBMED   12095697
  REMARK    GeneRIF: PMID:12095697 pertains to mouse Mrf1 gene which appears to
            be the homolog of human TSBF1.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY159379.1, BC109260.1, AC024221.23 and AI215011.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB155321.1, SRR1803614.102419.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309784.9/ ENSP00000311219.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.33"
     Protein         1..403
                     /product="tripartite motif-containing protein 59"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing 57; tumor suppressor
                     TSBF1; RING finger protein 104; tumor suppressor TSBF-1"
                     /calculated_mol_wt=46983
     Region          5..60
                     /region_name="RING-HC_TRIM59_C-V"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 59 (TRIM59) and similar proteins;
                     cd16763"
                     /db_xref="CDD:438419"
     Region          95..134
                     /region_name="Bbox2_TRIM59_C-XI"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 59 (TRIM59) and similar proteins;
                     cd19790"
                     /db_xref="CDD:380848"
     Site            order(97,100,109,112,117,120,126,129)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380848"
     Region          160..311
                     /region_name="Spore_III_AF"
                     /note="Stage III sporulation protein AF (Spore_III_AF);
                     cl17562"
                     /db_xref="CDD:473083"
     Site            329..349
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWR1.1)"
     CDS             1..403
                     /gene="TRIM59"
                     /gene_synonym="IFT80L; MRF1; RNF104; TRIM57; TSBF1"
                     /coded_by="NM_173084.3:144..1355"
                     /db_xref="CCDS:CCDS3190.1"
                     /db_xref="GeneID:286827"
                     /db_xref="HGNC:HGNC:30834"
                     /db_xref="MIM:616148"
ORIGIN      
        1 mhnfeeeltc picysifedp rvlpcshtfc rnclenilqa sgnfyiwrpl riplkcpncr
       61 siteiaptgi eslpvnfalr aiiekyqqed hpdivtcpeh yrqplnvycl ldkklvcghc
      121 ltigqhhghp iddlqsaylk ekdtpqklle qltdthwtdl thlieklkeq kshsekmiqg
      181 dkeavlqyfk elndtleqkk ksfltalcdv gnlinqeytp qiermkeire qqlelmalti
      241 slqeesplkf lekvddvrqh vqilkqrplp evqpveiypr vskilkeews rteigqiknv
      301 lipkmkispk rmscswpgkd ekeveflkil nivvvtlisv ilmsilffnq hiitflseit
      361 liwfseasls vyqslsnslh kvknilchif yllkefvwki vsh
//
LOCUS       NP_006286               1264 aa            linear   PRI 27-APR-2025
DEFINITION  valine--tRNA ligase [Homo sapiens].
ACCESSION   NP_006286 XP_941254 XP_941297
VERSION     NP_006286.1
DBSOURCE    REFSEQ: accession NM_006295.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1264)
  AUTHORS   El-Hachem,N., Leclercq,M., Susaeta Ruiz,M., Vanleyssem,R.,
            Shostak,K., Korner,P.R., Capron,C., Martin-Morales,L.,
            Roncarati,P., Lavergne,A., Blomme,A., Turchetto,S., Goffin,E.,
            Thandapani,P., Tarassov,I., Nguyen,L., Pirotte,B., Chariot,A.,
            Marine,J.C., Herfs,M., Rapino,F., Agami,R. and Close,P.
  TITLE     Valine aminoacyl-tRNA synthetase promotes therapy resistance in
            melanoma
  JOURNAL   Nat Cell Biol 26 (7), 1154-1164 (2024)
   PUBMED   38849541
  REMARK    GeneRIF: Valine aminoacyl-tRNA synthetase promotes therapy
            resistance in melanoma.
REFERENCE   2  (residues 1 to 1264)
  AUTHORS   Shi,R., DU,W., He,Y., Hu,J., Yu,H., Zhou,W., Guo,J. and Feng,X.
  TITLE     High expression of VARS promotes the growth of multiple myeloma
            cells by causing imbalance in valine metabolism
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (6), 795-808 (2023)
   PUBMED   37587064
  REMARK    GeneRIF: High expression of VARS promotes the growth of multiple
            myeloma cells by causing imbalance in valine metabolism.
REFERENCE   3  (residues 1 to 1264)
  AUTHORS   Hu,W., Liu,Z., Yu,W., Wen,S., Wang,X., Qi,X., Hao,H., Lu,Y., Li,J.,
            Li,S. and Zhou,H.
  TITLE     Effects of PPM1K rs1440581 and rs7678928 on serum branched-chain
            amino acid levels and risk of cardiovascular disease
  JOURNAL   Ann Med 53 (1), 1316-1326 (2021)
   PUBMED   34382495
  REMARK    GeneRIF: Effects of PPM1K rs1440581 and rs7678928 on serum
            branched-chain amino acid levels and risk of cardiovascular
            disease.
REFERENCE   4  (residues 1 to 1264)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1264)
  AUTHORS   Friedman,J., Smith,D.E., Issa,M.Y., Stanley,V., Wang,R.,
            Mendes,M.I., Wright,M.S., Wigby,K., Hildreth,A., Crawford,J.R.,
            Koehler,A.E., Chowdhury,S., Nahas,S., Zhai,L., Xu,Z., Lo,W.S.,
            James,K.N., Musaev,D., Accogli,A., Guerrero,K., Tran,L.T.,
            Omar,T.E.I., Ben-Omran,T., Dimmock,D., Kingsmore,S.F.,
            Salomons,G.S., Zaki,M.S., Bernard,G. and Gleeson,J.G.
  TITLE     Biallelic mutations in valyl-tRNA synthetase gene VARS are
            associated with a progressive neurodevelopmental epileptic
            encephalopathy
  JOURNAL   Nat Commun 10 (1), 707 (2019)
   PUBMED   30755602
  REMARK    GeneRIF: Variants map to the VARS tRNA binding domain and adjacent
            to the anticodon domain, and disrupt highly conserved residues.
            Patient primary cells show intact VARS protein but reduced
            enzymatic activity, suggesting partial loss of function. The
            implication of VARS in pediatric neurodegeneration broadens the
            spectrum of human diseases due to mutations in tRNA synthetase
            genes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1264)
  AUTHORS   Bec,G., Kerjan,P. and Waller,J.P.
  TITLE     Reconstitution in vitro of the valyl-tRNA synthetase-elongation
            factor (EF) 1 beta gamma delta complex. Essential roles of the
            NH2-terminal extension of valyl-tRNA synthetase and of the EF-1
            delta subunit in complex formation
  JOURNAL   J Biol Chem 269 (3), 2086-2092 (1994)
   PUBMED   8294461
REFERENCE   7  (residues 1 to 1264)
  AUTHORS   Hsieh,S.L. and Campbell,R.D.
  TITLE     Evidence that gene G7a in the human major histocompatibility
            complex encodes valyl-tRNA synthetase
  JOURNAL   Biochem J 278 (Pt 3) (Pt 3), 809-816 (1991)
   PUBMED   1898367
  REMARK    Erratum:[Biochem J 1992 Feb 1;281(Pt 3):879]
REFERENCE   8  (residues 1 to 1264)
  AUTHORS   Bec,G., Kerjan,P., Zha,X.D. and Waller,J.P.
  TITLE     Valyl-tRNA synthetase from rabbit liver. I. Purification as a
            heterotypic complex in association with elongation factor 1
  JOURNAL   J Biol Chem 264 (35), 21131-21137 (1989)
   PUBMED   2556394
REFERENCE   9  (residues 1 to 1264)
  AUTHORS   Sargent,C.A., Dunham,I. and Campbell,R.D.
  TITLE     Identification of multiple HTF-island associated genes in the human
            major histocompatibility complex class III region
  JOURNAL   EMBO J 8 (8), 2305-2312 (1989)
   PUBMED   2477242
REFERENCE   10 (residues 1 to 1264)
  AUTHORS   Motorin,Yu.A., Wolfson,A.D., Orlovsky,A.F. and Gladilin,K.L.
  TITLE     Mammalian valyl-tRNA synthetase forms a complex with the first
            elongation factor
  JOURNAL   FEBS Lett 238 (2), 262-264 (1988)
   PUBMED   3169261
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CX781162.1, CX167000.1,
            BC012808.2 and M98326.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_941254.1, XP_941297.1.
            
            Summary: Aminoacyl-tRNA synthetases catalyze the aminoacylation of
            tRNA by their cognate amino acid. Because of their central role in
            linking amino acids with nucleotide triplets contained in tRNAs,
            aminoacyl-tRNA synthetases are thought to be among the first
            proteins that appeared in evolution. The protein encoded by this
            gene belongs to class-I aminoacyl-tRNA synthetase family and is
            located in the class III region of the major histocompatibility
            complex. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X59303.1, BC012808.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000375663.8/
                                                  ENSP00000364815.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1264
                     /product="valine--tRNA ligase"
                     /EC_number="6.1.1.9"
                     /note="valyl-tRNA synthetase 2; valine tRNA ligase 1,
                     cytoplasmic; valRS; protein G7a"
                     /calculated_mol_wt=140346
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P26640.4)"
     Region          92..213
                     /region_name="GST_C_ValRS_N"
                     /note="Glutathione S-transferase C-terminal-like, alpha
                     helical domain of vertebrate Valyl-tRNA synthetase;
                     cd10294"
                     /db_xref="CDD:198327"
     Site            order(97..99,101..104,107,109..110,138,141)
                     /site_type="other"
                     /note="putative protein interface 1"
                     /db_xref="CDD:198327"
     Region          217..296
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26640.4)"
     Region          282..1264
                     /region_name="PTZ00419"
                     /note="valyl-tRNA synthetase-like protein; Provisional"
                     /db_xref="CDD:240411"
     Region          344..354
                     /region_name="'HIGH' region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26640.4)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26640.4)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26640.4)"
     Site            645
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P26640.4)"
     Region          862..866
                     /region_name="'KMSKS' region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26640.4)"
     CDS             1..1264
                     /gene="VARS1"
                     /gene_synonym="G7A; NDMSCA; VARS; VARS2"
                     /coded_by="NM_006295.3:241..4035"
                     /db_xref="CCDS:CCDS34412.1"
                     /db_xref="GeneID:7407"
                     /db_xref="HGNC:HGNC:12651"
                     /db_xref="MIM:192150"
ORIGIN      
        1 mstlyvsphp dafpslrali aarygeageg pgwggahpri clqppptsrt pfppprlpal
       61 eqgpgglwvw gatavaqllw paglggpggs raavlvqqwv syadtelipa acgatlpalg
      121 lrssaqdpqa vlgalgrals pleewlrlht ylageaptla dlaavtalll pfryvldppa
      181 rriwnnvtrw fvtcvrqpef ravlgevvly sgarplshqp gpeapalpkt aaqlkkeakk
      241 reklekfqqk qkiqqqqppp gekkpkpekr ekrdpgvity dlptppgekk dvsgpmpdsy
      301 spryveaawy pwweqqgffk peygrpnvsa anprgvfmmc ipppnvtgsl hlghaltnai
      361 qdsltrwhrm rgettlwnpg cdhagiatqv vvekklwreq glsrhqlgre aflqevwkwk
      421 eekgdriyhq lkklgssldw dracftmdpk lsaavteafv rlheegiiyr strlvnwsct
      481 lnsaisdiev dkkeltgrtl lsvpgykekv efgvlvsfay kvqgsdsdee vvvattriet
      541 mlgdvavavh pkdtryqhlk gknvihpfls rslpivfdef vdmdfgtgav kitpahdqnd
      601 yevgqrhgle aisimdsrga linvpppflg lprfearkav lvalkerglf rgiednpmvv
      661 plcnrskdvv epllrpqwyv rcgemaqaas aavtrgdlri lpeahqrtwh awmdnirewc
      721 isrqlwwghr ipayfvtvsd pavppgedpd grywvsgrne aearekaake fgvspdkisl
      781 qqdedvldtw fssglfplsi lgwpnqsedl svfypgtlle tghdilffwv armvmlglkl
      841 tgrlpfrevy lhaivrdahg rkmskslgnv idpldviygi slqglhnqll nsnldpseve
      901 kakegqkadf pagipecgtd alrfglcaym sqgrdinldv nrilgyrhfc nklwnatkfa
      961 lrglgkgfvp sptsqpgghe slvdrwirsr lteavrlsnq gfqaydfpav ttaqysfwly
     1021 elcdvylecl kpvlngvdqv aaecarqtly tcldvglrll spfmpfvtee lfqrlprrmp
     1081 qappslcvtp ypepsecswk dpeaeaalel alsitravrs lradynltri rpdcflevad
     1141 eatgalasav sgyvqalasa gvvavlalga papqgcaval asdrcsihlq lqglvdpare
     1201 lgklqakrve aqrqaqrlre rraasgypvk vplevqeade aklqqteael rkvdeaialf
     1261 qkml
//
LOCUS       NP_000575                 99 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-8 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_000575
VERSION     NP_000575.1
DBSOURCE    REFSEQ: accession NM_000584.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Si,W., Liu,J., Wang,Y., Mao,Y., Zhang,Y., Xu,S., Guo,K., Zhang,Y.,
            Hu,Y. and Zhang,F.
  TITLE     IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113074 (2024)
   PUBMED   39244903
  REMARK    GeneRIF: IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway.
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Dhurua,S., Maity,S., Maity,B. and Jana,M.
  TITLE     Comparative Bindings of Glycosaminoglycans with CXCL8 Monomer and
            Dimer: Insights from Conformational Dynamics and Kinetics of
            Hydrogen Bonds
  JOURNAL   J Phys Chem B 128 (42), 10348-10362 (2024)
   PUBMED   39405497
  REMARK    GeneRIF: Comparative Bindings of Glycosaminoglycans with CXCL8
            Monomer and Dimer: Insights from Conformational Dynamics and
            Kinetics of Hydrogen Bonds.
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Carpi,S., Polini,B., Nieri,D., Doccini,S., Conti,M., Bazzan,E.,
            Pagnini,M., Santorelli,F.M., Cecchini,M., Nieri,P., Celi,A. and
            Neri,T.
  TITLE     Extracellular Vesicles Induce Nuclear Factor-kappaB Activation and
            Interleukin-8 Synthesis through miRNA-191-5p Contributing to
            Inflammatory Processes: Potential Implications in the Pathogenesis
            of Chronic Obstructive Pulmonary Disease
  JOURNAL   Biomolecules 14 (8), 1030 (2024)
   PUBMED   39199417
  REMARK    GeneRIF: Extracellular Vesicles Induce Nuclear Factor-kappaB
            Activation and Interleukin-8 Synthesis through miRNA-191-5p
            Contributing to Inflammatory Processes: Potential Implications in
            the Pathogenesis of Chronic Obstructive Pulmonary Disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Asiri,A., Hazeldine,J., Moiemen,N. and Harrison,P.
  TITLE     IL-8 Induces Neutrophil Extracellular Trap Formation in Severe
            Thermal Injury
  JOURNAL   Int J Mol Sci 25 (13), 7216 (2024)
   PUBMED   39000323
  REMARK    GeneRIF: IL-8 Induces Neutrophil Extracellular Trap Formation in
            Severe Thermal Injury.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Vukolova,Y., Gubareva,I., Galati,G. and Germanova,O.
  TITLE     Diagnostic utility of sortilin & other biomarkers in the diagnosis
            of carotid & coronary atherosclerosis in individuals with arterial
            hypertension
  JOURNAL   Indian J Med Res 159 (5), 511-518 (2024)
   PUBMED   39382416
  REMARK    GeneRIF: Diagnostic utility of sortilin & other biomarkers in the
            diagnosis of carotid & coronary atherosclerosis in individuals with
            arterial hypertension.
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Koch,A.E., Polverini,P.J., Kunkel,S.L., Harlow,L.A., DiPietro,L.A.,
            Elner,V.M., Elner,S.G. and Strieter,R.M.
  TITLE     Interleukin-8 as a macrophage-derived mediator of angiogenesis
  JOURNAL   Science 258 (5089), 1798-1801 (1992)
   PUBMED   1281554
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Morris,S.W., Nelson,N., Valentine,M.B., Shapiro,D.N., Look,A.T.,
            Kozlosky,C.J., Beckmann,M.P. and Cerretti,D.P.
  TITLE     Assignment of the genes encoding human interleukin-8 receptor types
            1 and 2 and an interleukin-8 receptor pseudogene to chromosome 2q35
  JOURNAL   Genomics 14 (3), 685-691 (1992)
   PUBMED   1427896
REFERENCE   8  (residues 1 to 99)
  AUTHORS   Shimoya,K., Matsuzaki,N., Taniguchi,T., Kameda,T., Koyama,M.,
            Neki,R., Saji,F. and Tanizawa,O.
  TITLE     Human placenta constitutively produces interleukin-8 during
            pregnancy and enhances its production in intrauterine infection
  JOURNAL   Biol Reprod 47 (2), 220-226 (1992)
   PUBMED   1391327
REFERENCE   9  (residues 1 to 99)
  AUTHORS   Baggiolini,M. and Clark-Lewis,I.
  TITLE     Interleukin-8, a chemotactic and inflammatory cytokine
  JOURNAL   FEBS Lett 307 (1), 97-101 (1992)
   PUBMED   1639201
  REMARK    Review article
REFERENCE   10 (residues 1 to 99)
  AUTHORS   Schall,T.J., Bacon,K., Toy,K.J. and Goeddel,D.V.
  TITLE     Selective attraction of monocytes and T lymphocytes of the memory
            phenotype by cytokine RANTES
  JOURNAL   Nature 347 (6294), 669-671 (1990)
   PUBMED   1699135
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG497712.1 and BC013615.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the CXC
            chemokine family and is a major mediator of the inflammatory
            response. The encoded protein is commonly referred to as
            interleukin-8 (IL-8). IL-8 is secreted by mononuclear macrophages,
            neutrophils, eosinophils, T lymphocytes, epithelial cells, and
            fibroblasts. It functions as a chemotactic factor by guiding the
            neutrophils to the site of infection. Bacterial and viral products
            rapidly induce IL-8 expression. IL-8 also participates with other
            cytokines in the proinflammatory signaling cascade and plays a role
            in systemic inflammatory response syndrome (SIRS). This gene is
            believed to play a role in the pathogenesis of the lower
            respiratory tract infection bronchiolitis, a common respiratory
            tract disease caused by the respiratory syncytial virus (RSV). The
            overproduction of this proinflammatory protein is thought to cause
            the lung inflammation associated with csytic fibrosis. This
            proinflammatory protein is also suspected of playing a role in
            coronary artery disease and endothelial dysfunction. This protein
            is also secreted by tumor cells and promotes tumor migration,
            invasion, angiogenesis and metastasis. This chemokine is also a
            potent angiogenic factor. The binding of IL-8 to one of its
            receptors (IL-8RB/CXCR2) increases the permeability of blood
            vessels and increasing levels of IL-8 are positively correlated
            with increased severity of multiple disease outcomes (eg, sepsis).
            This gene and other members of the CXC chemokine gene family form a
            gene cluster in a region of chromosome 4q. [provided by RefSeq, May
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131067.1, SRR5189667.172257.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in cytokine storm inflammatory
                                      response
            MANE Ensembl match     :: ENST00000307407.8/ ENSP00000306512.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.3"
     Protein         1..99
                     /product="interleukin-8 isoform 1 precursor"
                     /note="tumor necrosis factor-induced gene 1; alveolar
                     macrophage chemotactic factor I; lymphocyte derived
                     neutrophil activating peptide; lung giant cell
                     carcinoma-derived chemotactic protein; beta endothelial
                     cell-derived neutrophil activating peptide; granulocyte
                     chemotactic protein 1; beta-thromboglobulin-like protein;
                     emoctakin; monocyte-derived neutrophil chemotactic factor;
                     chemokine (C-X-C motif) ligand 8; neutrophil-activating
                     peptide 1; small inducible cytokine subfamily B, member 8;
                     interleukin 8; T-cell chemotactic factor; monocyte-derived
                     neutrophil-activating peptide"
                     /calculated_mol_wt=9109
     sig_peptide     1..20
                     /note="/evidence=ECO:0000269|PubMed:2145175,
                     ECO:0000269|PubMed:2523801, ECO:0000269|PubMed:2648135;
                     propagated from UniProtKB/Swiss-Prot (P10145.1)"
                     /calculated_mol_wt=2008
     mat_peptide     21..99
                     /product="MDNCF-a. /id=PRO_0000005126"
                     /note="propagated from UniProtKB/Swiss-Prot (P10145.1)"
                     /calculated_mol_wt=9109
     mat_peptide     23..99
                     /product="Interleukin-8. /id=PRO_0000005127"
                     /note="propagated from UniProtKB/Swiss-Prot (P10145.1)"
                     /calculated_mol_wt=8922
     mat_peptide     27..99
                     /product="IL-8(5-77). /id=PRO_0000041948"
                     /note="propagated from UniProtKB/Swiss-Prot (P10145.1)"
                     /calculated_mol_wt=8542
     Site            27..28
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P10145.1)"
     mat_peptide     28..99
                     /product="IL-8(6-77). /id=PRO_0000005128"
                     /note="propagated from UniProtKB/Swiss-Prot (P10145.1)"
                     /calculated_mol_wt=8386
     Site            28..29
                     /site_type="cleavage"
                     /note="Cleavage, by MMP9; propagated from
                     UniProtKB/Swiss-Prot (P10145.1)"
     mat_peptide     29..99
                     /product="IL-8(7-77). /id=PRO_0000005129"
                     /note="propagated from UniProtKB/Swiss-Prot (P10145.1)"
                     /calculated_mol_wt=8299
     mat_peptide     30..99
                     /product="IL-8(8-77). /id=PRO_0000005130"
                     /note="propagated from UniProtKB/Swiss-Prot (P10145.1)"
                     /calculated_mol_wt=8228
     mat_peptide     31..99
                     /product="IL-8(9-77). /id=PRO_0000005131"
                     /note="propagated from UniProtKB/Swiss-Prot (P10145.1)"
                     /calculated_mol_wt=8099
     Region          31..94
                     /region_name="Chemokine_CXC"
                     /note="1 of 4 subgroup designations based on the
                     arrangement of the two N-terminal cysteine residues;
                     includes a number of secreted growth factors and
                     interferons involved in mitogenic, chemotactic, and
                     inflammatory activity; many members contain an RCxC
                     motif...; cd00273"
                     /db_xref="CDD:238171"
     Site            order(31..33,39,44..49,58..60,70..71,74..76,82,87)
                     /site_type="active"
                     /note="receptor binding site [active]"
                     /db_xref="CDD:238171"
     Site            31..33
                     /site_type="active"
                     /note="ELR motif [active]"
                     /db_xref="CDD:238171"
     Site            order(32,35,49..50,53..55,65..68,70,74..75,78,85,89,
                     92..93)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238171"
     Site            order(32,35,53,55,65,67,70,74..75)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238171"
     Site            order(33..34,36)
                     /site_type="active"
                     /note="RCXC motif [active]"
                     /db_xref="CDD:238171"
     Site            order(35..41,44..49)
                     /site_type="active"
                     /note="N-loop [active]"
                     /db_xref="CDD:238171"
     Site            order(37..38,40,44,48,67,70,74,76)
                     /site_type="active"
                     /note="receptor binding cleft [active]"
                     /db_xref="CDD:238171"
     Site            order(45,47,81,84,86..89,91,94)
                     /site_type="other"
                     /note="glycosaminoglycan (GAG) binding site [chemical
                     binding]"
                     /db_xref="CDD:238171"
     Site            order(47,50,69,71,74..75)
                     /site_type="other"
                     /note="putative glycosaminoglycan (GAG) binding site
                     [chemical binding]"
                     /db_xref="CDD:238171"
     Site            order(49..50,54,66,68,78,85,89,92..93)
                     /site_type="other"
                     /note="dimer interface (I form) [polypeptide binding]"
                     /db_xref="CDD:238171"
     Site            58..60
                     /site_type="other"
                     /note="30s-loop"
                     /db_xref="CDD:238171"
     Site            58..60
                     /site_type="other"
                     /note="GPH motif"
                     /db_xref="CDD:238171"
     Site            71..73
                     /site_type="other"
                     /note="40s-loop"
                     /db_xref="CDD:238171"
     CDS             1..99
                     /gene="CXCL8"
                     /gene_synonym="GCP-1; GCP1; IL8; LECT; LUCT; LYNAP; MDNCF;
                     MONAP; NAF; NAP-1; NAP1; SCYB8"
                     /coded_by="NM_000584.4:91..390"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS34005.1"
                     /db_xref="GeneID:3576"
                     /db_xref="HGNC:HGNC:6025"
                     /db_xref="MIM:146930"
ORIGIN      
        1 mtsklavall aaflisaalc egavlprsak elrcqcikty skpfhpkfik elrviesgph
       61 canteiivkl sdgrelcldp kenwvqrvve kflkraens
//
LOCUS       NP_001034262             331 aa            linear   ROD 27-APR-2025
DEFINITION  docking protein 6 [Mus musculus].
ACCESSION   NP_001034262 XP_892800 XP_892821 XP_909393
VERSION     NP_001034262.1
DBSOURCE    REFSEQ: accession NM_001039173.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Guo,Y., Xiang,P., Sun,X., Liu,W., Zhou,J., Yin,B., Hou,L.,
            Qiang,B., Li,H., Shu,P. and Peng,X.
  TITLE     Docking protein 6 (DOK6) selectively docks the neurotrophic
            signaling transduction to restrain peripheral neuropathy
  JOURNAL   Signal Transduct Target Ther 9 (1), 32 (2024)
   PUBMED   38351062
  REMARK    GeneRIF: Docking protein 6 (DOK6) selectively docks the
            neurotrophic signaling transduction to restrain peripheral
            neuropathy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Rutledge,E.A., Benazet,J.D. and McMahon,A.P.
  TITLE     Cellular heterogeneity in the ureteric progenitor niche and
            distinct profiles of branching morphogenesis in organ development
  JOURNAL   Development 144 (17), 3177-3188 (2017)
   PUBMED   28705898
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Li,Wq., Shi,L., You,Yg., Gong,Yh., Yin,B., Yuan,Jg. and Peng,Xz.
  TITLE     Downstream of tyrosine kinase/docking protein 6, as a novel
            substrate of tropomyosin-related kinase C receptor, is involved in
            neurotrophin 3-mediated neurite outgrowth in mouse cortex neurons
  JOURNAL   BMC Biol 8, 86 (2010)
   PUBMED   20565848
  REMARK    GeneRIF: Dok6 selectively binds to the NPQY motif of TrkC through
            its phosphotyrosine-binding (PTB) domain in a kinase
            activity-dependent manner.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Chatterjee,B., Richards,K., Bucan,M. and Lo,C.
  TITLE     Nt mutation causing laterality defects associated with deletion of
            rotatin
  JOURNAL   Mamm Genome 18 (5), 310-315 (2007)
   PUBMED   17551791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116877.18, AC164619.5, AC110375.4 and AC116387.7.
            
            On or before Jan 25, 2006 this sequence version replaced
            XP_892800.1, XP_892821.1, XP_909393.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.31127.1,
                                           SRR10662773.2254547.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 59.05 cM"
     Protein         1..331
                     /product="docking protein 6"
                     /note="downstream of tyrosine kinases 6; downstream of
                     tyrosine kinase 6"
                     /calculated_mol_wt=38156
     Region          9..113
                     /region_name="PH_DOK4_DOK5_DOK6"
                     /note="Pleckstrin homology (PH) domain of Downstream of
                     tyrosine kinase 4, 5, and 6 proteins; cd14678"
                     /db_xref="CDD:270197"
     Region          133..235
                     /region_name="PTB_DOK4_DOK5_DOK6"
                     /note="Downstream of tyrosine kinase 4, 5, and 6 proteins
                     phosphotyrosine-binding domain (PTBi); cd13164"
                     /db_xref="CDD:241318"
     Site            order(184..189,195,199..200,210,223)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:241318"
     Region          263..273
                     /region_name="DKFBH motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MHE5.1)"
     Region          293..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MHE5.1)"
     CDS             1..331
                     /gene="Dok6"
                     /gene_synonym="Dok-6"
                     /coded_by="NM_001039173.2:405..1400"
                     /db_xref="CCDS:CCDS37878.1"
                     /db_xref="GeneID:623279"
                     /db_xref="MGI:MGI:3639495"
ORIGIN      
        1 masnfndivk qgyvkirsrk lgifrrcwlv fkkasskgpr rlekfpdeka ayfrnfhkvt
       61 elhniknitr lpretkkhav aiifhdetsk tfaceselea eewckhlcme clgtrlndis
      121 lgepdllaag vqreqnerfn vylmptpnld iygectmqit heniylwdih nakvklvmwp
      181 lsslrrygrd stwftfesgr mcdtgeglft fqtregemiy qkvhsatlai aeqherlmle
      241 meqkarlqts ltepmtlsks islprsaywh hitrqnsvge iyslqghgfg sskmsraqtf
      301 psyapeqsee aqpplsrsss ygfsysssli q
//
LOCUS       NP_055462               1742 aa            linear   PRI 27-APR-2025
DEFINITION  meiosis regulator and mRNA stability factor 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_055462
VERSION     NP_055462.2
DBSOURCE    REFSEQ: accession NM_014647.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1742)
  AUTHORS   Brothers,W.R., Fakim,H., Kajjo,S. and Fabian,M.R.
  TITLE     P-bodies directly regulate MARF1-mediated mRNA decay in human cells
  JOURNAL   Nucleic Acids Res 50 (13), 7623-7636 (2022)
   PUBMED   35801873
  REMARK    GeneRIF: P-bodies directly regulate MARF1-mediated mRNA decay in
            human cells.
REFERENCE   2  (residues 1 to 1742)
  AUTHORS   Brothers,W.R., Hebert,S., Kleinman,C.L. and Fabian,M.R.
  TITLE     A non-canonical role for the EDC4 decapping factor in regulating
            MARF1-mediated mRNA decay
  JOURNAL   Elife 9, e54995 (2020)
   PUBMED   32510323
  REMARK    GeneRIF: A non-canonical role for the EDC4 decapping factor in
            regulating MARF1-mediated mRNA decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1742)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1742)
  AUTHORS   Nishimura,T., Fakim,H., Brandmann,T., Youn,J.Y., Gingras,A.C.,
            Jinek,M. and Fabian,M.R.
  TITLE     Human MARF1 is an endoribonuclease that interacts with the DCP1:2
            decapping complex and degrades target mRNAs
  JOURNAL   Nucleic Acids Res 46 (22), 12008-12021 (2018)
   PUBMED   30364987
  REMARK    GeneRIF: Human MARF1 is an endoribonuclease that interacts with the
            DCP1:DCP2 decapping complex and degrades target mRNAs.
REFERENCE   5  (residues 1 to 1742)
  AUTHORS   Guan,W., Steffen,B.T., Lemaitre,R.N., Wu,J.H.Y., Tanaka,T.,
            Manichaikul,A., Foy,M., Rich,S.S., Wang,L., Nettleton,J.A.,
            Tang,W., Gu,X., Bandinelli,S., King,I.B., McKnight,B., Psaty,B.M.,
            Siscovick,D., Djousse,L., Chen,Y.I., Ferrucci,L., Fornage,M.,
            Mozafarrian,D., Tsai,M.Y. and Steffen,L.M.
  TITLE     Genome-wide association study of plasma N6 polyunsaturated fatty
            acids within the cohorts for heart and aging research in genomic
            epidemiology consortium
  JOURNAL   Circ Cardiovasc Genet 7 (3), 321-331 (2014)
   PUBMED   24823311
REFERENCE   6  (residues 1 to 1742)
  AUTHORS   Su,Y.Q., Sun,F., Handel,M.A., Schimenti,J.C. and Eppig,J.J.
  TITLE     Meiosis arrest female 1 (MARF1) has nuage-like function in
            mammalian oocytes
  JOURNAL   Proc Natl Acad Sci U S A 109 (46), 18653-18660 (2012)
   PUBMED   23090997
REFERENCE   7  (residues 1 to 1742)
  AUTHORS   Su,Y.Q., Sugiura,K., Sun,F., Pendola,J.K., Cox,G.A., Handel,M.A.,
            Schimenti,J.C. and Eppig,J.J.
  TITLE     MARF1 regulates essential oogenic processes in mice
  JOURNAL   Science 335 (6075), 1496-1499 (2012)
   PUBMED   22442484
REFERENCE   8  (residues 1 to 1742)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   9  (residues 1 to 1742)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   10 (residues 1 to 1742)
  AUTHORS   Dunster,K., Lai,F.P. and Sentry,J.W.
  TITLE     Limkain b1, a novel human autoantigen localized to a subset of
            ABCD3 and PXF marked peroxisomes
  JOURNAL   Clin Exp Immunol 140 (3), 556-563 (2005)
   PUBMED   15932519
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC064914.1, BC137165.1, AB007890.3 and DB360504.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 27, 2006 this sequence version replaced NP_055462.1.
            
            Summary: This gene encodes a putative peroxisomal protein that
            appears to be conserved across Euteleostomi. In humans, it may be
            autoantigenic. [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (1) encodes isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC137165.1, SRR1803612.107373.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396368.8/ ENSP00000379654.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1742
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.11"
     Protein         1..1742
                     /product="meiosis regulator and mRNA stability factor 1
                     isoform 1"
                     /note="limkain-b1; protein phosphatase 1, regulatory
                     subunit 34; meiosis arrest female protein 1; meiosis
                     arrest female 1"
                     /calculated_mol_wt=192729
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4F3.6)"
     Region          352..474
                     /region_name="PIN_limkain_b1_N_like"
                     /note="N-terminal LabA-like PIN domain of limkain b1 and
                     similar proteins; cd10910"
                     /db_xref="CDD:350234"
     Region          510..582
                     /region_name="RRM1_LKAP"
                     /note="RNA recognition motif 1 (RRM1) found in Limkain-b1
                     (LKAP) and similar proteins; cd12255"
                     /db_xref="CDD:409700"
     Region          619..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4F3.6)"
     Region          681..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4F3.6)"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8BJ34; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4F3.6)"
     Site            760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4F3.6)"
     Region          787..875
                     /region_name="RRM2_LKAP"
                     /note="RNA recognition motif 2 (RRM2) found in Limkain-b1
                     (LKAP) and similar proteins; cd12256"
                     /db_xref="CDD:409701"
     Region          878..1088
                     /region_name="MARF1_LOTUS"
                     /note="MARF1 LOTUS domain; pfam19687"
                     /db_xref="CDD:437519"
     Site            1091
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4F3.6)"
     Site            1093
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4F3.6)"
     Region          1100..1171
                     /region_name="LOTUS_3_Limkain_b1"
                     /note="The third LOTUS domain on Limkain b1(LKAP);
                     cd09979"
                     /db_xref="CDD:193593"
     Region          1176..1247
                     /region_name="LOTUS_4_Limkain_b1"
                     /note="The fourth LOTUS domain on Limkain b1(LKAP);
                     cd09980"
                     /db_xref="CDD:193594"
     Region          1260..1330
                     /region_name="LOTUS_5_Limkain_b1"
                     /note="The fifth LOTUS domain on Limkain b1(LKAP);
                     cd09981"
                     /db_xref="CDD:193595"
     Region          1336..1406
                     /region_name="LOTUS_6_Limkain_b1"
                     /note="The sixth LOTUS domain on Limkain b1(LKAP);
                     cd09982"
                     /db_xref="CDD:193596"
     Region          1412..1484
                     /region_name="LOTUS_7_Limkain_b1"
                     /note="The seventh LOTUS domain on Limkain b1(LKAP);
                     cd09983"
                     /db_xref="CDD:193597"
     Region          1487..1562
                     /region_name="LOTUS_8_Limkain_b1"
                     /note="The eighth LOTUS domain on Limkain b1(LKAP);
                     cd09984"
                     /db_xref="CDD:193598"
     Site            1571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4F3.6)"
     Region          1677..1726
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4F3.6)"
     CDS             1..1742
                     /gene="MARF1"
                     /gene_synonym="KIAA0430; LKAP; LMKB; PPP1R34"
                     /coded_by="NM_014647.4:196..5424"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10562.2"
                     /db_xref="GeneID:9665"
                     /db_xref="HGNC:HGNC:29562"
                     /db_xref="MIM:614593"
ORIGIN      
        1 mmegngtens csrtrgwlqq dndakpwlwk fsncfsrpeq tlphspqtke ymenkkvave
       61 lkdvpsplha gsklfpavpl pdirslqqpk iqlssvpkvs ccahcpneps tspmrfgggg
      121 ggsggtssli hpgalldsqs trtitcqvgs gfafqsassl qnasarnnla giasdfpsmc
      181 lesnlssckh lpccgklhfq schgnvhklh qfpslqgcts agyfpcsdft sgapghleeh
      241 isqseltphl ctnslhlnvv ppvclkgsly cedclnkpar nsiidaakvw pnipppntqp
      301 aplavplcng cgtkgtgket tlllatslgk aaskfgspev avagqvlenl ppigvfwdie
      361 ncsvpsgrsa tavvqrirek ffkghreaef icvcdisken keviqelnnc qvtvahinat
      421 aknaaddklr qslrrfanth tapatvvlvs tdvnfalels dlrhrhgfhi ilvhknqase
      481 allhhaneli rfeefisdlp prlplkmpqc htllyvynlp ankdgksvsn rlrrlsdncg
      541 gkvlsitgcs ailrfinqds aeraqkrmen edvfgnriiv sftpknrelc etkssnaiad
      601 kvkspkklkn pklclikdas eqsssakatp gkgsqansgs atkntnvksl qelcrmeskt
      661 ghrnsehqqg hlrlvvpthg nssaavstpk nsgvaepvyk tsqkkenlsa rsvtsspvek
      721 kdkeetvfqv sypsafsklv asrqvsplla sqswssrsms pnllnraspl afnianssse
      781 adcpdpfang advqvsnidy rlsrkelqql lqeafarhgk vksvelspht dyqlkavvqm
      841 enlqdaigav nslhrykigs kkilvslatg aaskslslls aetmsvlqda pacclplfkf
      901 tdiyekkfgh klnvsdlykl tdtvaireqg ngrlvcllps sqarqsplgs sqshdgsstn
      961 cspiifeele yhepvcrqhc snkdfsehef dpdsykipfv ilslktfapq vhsllqtheg
     1021 tvpllsfpdc yiaefgdlev vqenqggvpl ehfitcvpgv niataqngik vvkwihnkpp
     1081 ppntdpwllr skspvgnpql iqfsrevidl lksqpscvip ishfipsyhh hfakqcrvsd
     1141 ygyskliell eavphvlqil gmgskrlltl thraqvkrft qdllkllksq askqvivref
     1201 sqayhwcfsk dwdvteygvc elidivseip dtticlsqqd nemvicipkr ertqdeiert
     1261 kqfskdvvdl lrhqphfrmp fnkfipsyhh hfgrqcklay ygftkllelf eaipdtlqvl
     1321 ecgeekiltl teverfkala aqfvkllrsq kdnclmmtdl lteyaktfgy tfrlqdydvs
     1381 sisaltqklc hvvkvadies grqiqlinrk slrsltaqll vllmswegtt hlsveelkrh
     1441 yesthntpln pceygfmtlt ellkslpylv evftndkmee cvkltslylf aknvrsllht
     1501 yhyqqiflhe fsmaytkyvg etlqpktygh ssveellgai pqvvwikghg hkrivvlknd
     1561 mksrlsslsl spanhenqps egerilevpe shtaselklg adgsgpshte qellrltdds
     1621 pvdllcapvp sclpspqlrp dpvilqsadl iqfeerpqep seimilnqee kmeipipgks
     1681 ktltsdssss cisaavpvpp cpssetsesl lskdpvespa kkqpknrvkl aanfslapit
     1741 kl
//
LOCUS       NP_001354794             180 aa            linear   PRI 27-APR-2025
DEFINITION  sialidase-3 isoform d [Homo sapiens].
ACCESSION   NP_001354794
VERSION     NP_001354794.1
DBSOURCE    REFSEQ: accession NM_001367865.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Wu,G., Cao,B., Zhai,H., Liu,B., Huang,Y., Chen,X., Ling,H.,
            Ling,S., Jin,S., Yang,X. and Wang,J.
  TITLE     EPO promotes the progression of rheumatoid arthritis by inducing
            desialylation via increasing the expression of neuraminidase 3
  JOURNAL   Ann Rheum Dis 83 (5), 564-575 (2024)
   PUBMED   38272667
  REMARK    GeneRIF: EPO promotes the progression of rheumatoid arthritis by
            inducing desialylation via increasing the expression of
            neuraminidase 3.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Kirolos,S.A., Pilling,D. and Gomer,R.H.
  TITLE     The extracellular sialidase NEU3 primes neutrophils
  JOURNAL   J Leukoc Biol 112 (6), 1399-1411 (2022)
   PUBMED   35899930
  REMARK    GeneRIF: The extracellular sialidase NEU3 primes neutrophils.
            Erratum:[J Leukoc Biol. 2024 Feb 23;115(3):583. doi:
            10.1093/jleuko/qiad154. PMID: 38206829]
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Miyagi,T. and Yamamoto,K.
  TITLE     Sialidase NEU3 and its pathological significance
  JOURNAL   Glycoconj J 39 (5), 677-683 (2022)
   PUBMED   35675020
  REMARK    GeneRIF: Sialidase NEU3 and its pathological significance.
            Review article
            Erratum:[Glycoconj J. 2022 Aug;39(4):543. doi:
            10.1007/s10719-022-10075-7. PMID: 35834088]
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Bovio,F., Epistolio,S., Mozzi,A., Monti,E., Fusi,P., Forcella,M.
            and Frattini,M.
  TITLE     Role of NEU3 Overexpression in the Prediction of Efficacy of
            EGFR-Targeted Therapies in Colon Cancer Cell Lines
  JOURNAL   Int J Mol Sci 21 (22), 8805 (2020)
   PUBMED   33233823
  REMARK    GeneRIF: Role of NEU3 Overexpression in the Prediction of Efficacy
            of EGFR-Targeted Therapies in Colon Cancer Cell Lines.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Ghiroldi,A., Piccoli,M., Creo,P., Cirillo,F., Rota,P.,
            D'Imperio,S., Ciconte,G., Monasky,M.M., Micaglio,E., Garatti,A.,
            Aureli,M., Carsana,E.V., Menicanti,L., Pappone,C. and Anastasia,L.
  TITLE     Role of sialidase Neu3 and ganglioside GM3 in cardiac fibroblasts
            activation
  JOURNAL   Biochem J 477 (17), 3401-3415 (2020)
   PUBMED   32869836
  REMARK    GeneRIF: Role of sialidase Neu3 and ganglioside GM3 in cardiac
            fibroblasts activation.
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Kakugawa,Y., Wada,T., Yamaguchi,K., Yamanami,H., Ouchi,K., Sato,I.
            and Miyagi,T.
  TITLE     Up-regulation of plasma membrane-associated ganglioside sialidase
            (Neu3) in human colon cancer and its involvement in apoptosis
            suppression
  JOURNAL   Proc Natl Acad Sci U S A 99 (16), 10718-10723 (2002)
   PUBMED   12149448
  REMARK    GeneRIF: up-regulation of plasma membrane-associated ganglioside
            sialidase (Neu3) in human colon cancer and its involvement in
            apoptosis suppression
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Wang,Y., Yamaguchi,K., Wada,T., Hata,K., Zhao,X., Fujimoto,T. and
            Miyagi,T.
  TITLE     A close association of the ganglioside-specific sialidase Neu3 with
            caveolin in membrane microdomains
  JOURNAL   J Biol Chem 277 (29), 26252-26259 (2002)
   PUBMED   12011038
  REMARK    GeneRIF: Neu3 functions as a caveolin-related signaling molecule
            within caveolin-rich microdomains
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Wang,Y., Yamaguchi,K., Shimada,Y., Zhao,X. and Miyagi,T.
  TITLE     Site-directed mutagenesis of human membrane-associated ganglioside
            sialidase: identification of amino-acid residues contributing to
            substrate specificity
  JOURNAL   Eur J Biochem 268 (8), 2201-2208 (2001)
   PUBMED   11298736
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Monti,E., Bassi,M.T., Papini,N., Riboni,M., Manzoni,M.,
            Venerando,B., Croci,G., Preti,A., Ballabio,A., Tettamanti,G. and
            Borsani,G.
  TITLE     Identification and expression of NEU3, a novel human sialidase
            associated to the plasma membrane
  JOURNAL   Biochem J 349 (Pt 1), 343-351 (2000)
   PUBMED   10861246
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Wada,T., Yoshikawa,Y., Tokuyama,S., Kuwabara,M., Akita,H. and
            Miyagi,T.
  TITLE     Cloning, expression, and chromosomal mapping of a human ganglioside
            sialidase
  JOURNAL   Biochem Biophys Res Commun 261 (1), 21-27 (1999)
   PUBMED   10405317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001992.4.
            
            Summary: This gene product belongs to a family of glycohydrolytic
            enzymes which remove sialic acid residues from glycoproteins and
            glycolipids. It is localized in the plasma membrane, and its
            activity is specific for gangliosides. It may play a role in
            modulating the ganglioside content of the lipid bilayer. [provided
            by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..180
                     /product="sialidase-3 isoform d"
                     /EC_number="3.2.1.18"
                     /note="ganglioside sialidase; N-acetyl-alpha-neuraminidase
                     3; sialidase-3; membrane sialidase; sialidase 3 (membrane
                     sialidase); ganglioside sialidasedis"
                     /calculated_mol_wt=20174
     Region          44..>173
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          57..110
                     /region_name="Sialidase propeller 1"
                     /note="Sialidase propeller 1 [structural motif]"
                     /db_xref="CDD:271234"
     Region          119..173
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     CDS             1..180
                     /gene="NEU3"
                     /gene_synonym="SIAL3"
                     /coded_by="NM_001367865.1:126..668"
                     /note="isoform d is encoded by transcript variant 7"
                     /db_xref="GeneID:10825"
                     /db_xref="HGNC:HGNC:7760"
                     /db_xref="MIM:604617"
ORIGIN      
        1 mrpadlpprp meespasssa pteteepgss aevmeevttc sfnsplfrqe ddrgityrip
       61 allyipptht flafaekrst rrdedalhlv lrrglrigql vqwgplkplm eatlpghrtm
      121 npcpvweqks gcvflfficv rghvterqqi vsgrnaarlc fiysqdagcs wseskmkilp
//
LOCUS       NP_001356479             321 aa            linear   PRI 27-APR-2025
DEFINITION  BDNF/NT-3 growth factors receptor isoform k [Homo sapiens].
ACCESSION   NP_001356479
VERSION     NP_001356479.1
DBSOURCE    REFSEQ: accession NM_001369550.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Gupta,R., Dittmeier,M., Wohlleben,G., Nickl,V., Bischler,T.,
            Luzak,V., Wegat,V., Doll,D., Sodmann,A., Bady,E., Langlhofer,G.,
            Wachter,B., Havlicek,S., Gupta,J., Horn,E., Luningschror,P.,
            Villmann,C., Polat,B., Wischhusen,J., Monoranu,C.M., Kuper,J. and
            Blum,R.
  TITLE     Atypical cellular responses mediated by intracellular constitutive
            active TrkB (NTRK2) kinase domains and a solely intracellular
            NTRK2-fusion oncogene
  JOURNAL   Cancer Gene Ther 31 (9), 1357-1379 (2024)
   PUBMED   39039193
  REMARK    GeneRIF: Atypical cellular responses mediated by intracellular
            constitutive active TrkB (NTRK2) kinase domains and a solely
            intracellular NTRK2-fusion oncogene.
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Zhang,X., Zhang,Y., Yan,H., Yu,H., Zhang,D., Mattay,V.S., Tan,H.Y.
            and Yue,W.
  TITLE     Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2
  JOURNAL   BMC Med 22 (1), 146 (2024)
   PUBMED   38561734
  REMARK    GeneRIF: Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Ikhlef,L., Yassine,M., Chandouri,B., Riviere,L., Naves,T.,
            Dmytruk,N., Gachard,N., Jauberteau,M.O. and Gallet,P.F.
  TITLE     Targeting the NTSR2/TrkB oncogenic pathway in chronic lymphocytic
            leukemia
  JOURNAL   Sci Rep 14 (1), 6084 (2024)
   PUBMED   38480783
  REMARK    GeneRIF: Targeting the NTSR2/TrkB oncogenic pathway in chronic
            lymphocytic leukemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Wang,Y., Liang,J., Xu,B., Yang,J., Wu,Z. and Cheng,L.
  TITLE     TrkB/BDNF signaling pathway and its small molecular agonists in CNS
            injury
  JOURNAL   Life Sci 336, 122282 (2024)
   PUBMED   38008209
  REMARK    GeneRIF: TrkB/BDNF signaling pathway and its small molecular
            agonists in CNS injury.
            Review article
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Luberg,K., Wong,J., Weickert,C.S. and Timmusk,T.
  TITLE     Human TrkB gene: novel alternative transcripts, protein isoforms
            and expression pattern in the prefrontal cerebral cortex during
            postnatal development
  JOURNAL   J Neurochem 113 (4), 952-964 (2010)
   PUBMED   20193039
  REMARK    GeneRIF: Identification of 36 potential TrkB protein isoforms
            suggests high complexity in the synthesis, regulation and function
            of this important neurotrophin receptor emphasizing the need for
            further study of these novel TrkB variants.
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Stoilov,P., Castren,E. and Stamm,S.
  TITLE     Analysis of the human TrkB gene genomic organization reveals novel
            TrkB isoforms, unusual gene length, and splicing mechanism
  JOURNAL   Biochem Biophys Res Commun 290 (3), 1054-1065 (2002)
   PUBMED   11798182
  REMARK    GeneRIF: analysis of TrkB gene reveals novel gene length and
            splicing mechanism
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Haniu,M., Talvenheimo,J., Le,J., Katta,V., Welcher,A. and
            Rohde,M.F.
  TITLE     Extracellular domain of neurotrophin receptor trkB: disulfide
            structure, N-glycosylation sites, and ligand binding
  JOURNAL   Arch Biochem Biophys 322 (1), 256-264 (1995)
   PUBMED   7574684
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Nakagawara,A., Liu,X.G., Ikegaki,N., White,P.S., Yamashiro,D.J.,
            Nycum,L.M., Biegel,J.A. and Brodeur,G.M.
  TITLE     Cloning and chromosomal localization of the human TRK-B tyrosine
            kinase receptor gene (NTRK2)
  JOURNAL   Genomics 25 (2), 538-546 (1995)
   PUBMED   7789988
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Squinto,S.P., Stitt,T.N., Aldrich,T.H., Davis,S., Blanco,S.M.,
            RadzieJewski,C., Glass,D.J., Masiakowski,P., Furth,M.E.,
            Valenzuela,D.M., Distefano,P.S. and Yancopoulos,G.D.
  TITLE     trkB encodes a functional receptor for brain-derived neurotrophic
            factor and neurotrophin-3 but not nerve growth factor
  JOURNAL   Cell 65 (5), 885-893 (1991)
   PUBMED   1710174
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Soppet,D., Escandon,E., Maragos,J., Middlemas,D.S., Reid,S.W.,
            Blair,J., Burton,L.E., Stanton,B.R., Kaplan,D.R., Hunter,T.,
            Nikolics,K. and Parada,L.F.
  TITLE     The neurotrophic factors brain-derived neurotrophic factor and
            neurotrophin-3 are ligands for the trkB tyrosine kinase receptor
  JOURNAL   Cell 65 (5), 895-903 (1991)
   PUBMED   1645620
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390777.13.
            
            Summary: This gene encodes a member of the neurotrophic tyrosine
            receptor kinase (NTRK) family. This kinase is a membrane-bound
            receptor that, upon neurotrophin binding, phosphorylates itself and
            members of the MAPK pathway. Signalling through this kinase leads
            to cell differentiation. Mutations in this gene have been
            associated with obesity and mood disorders. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (y), as well as variants z and aa,
            encodes isoform k.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.276671.1,
                                           SRR1803614.230360.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..321
                     /product="BDNF/NT-3 growth factors receptor isoform k"
                     /EC_number="2.7.10.1"
                     /note="BDNF/NT-3 growth factors receptor; tyrosine kinase
                     receptor B; BDNF-tropomyosine receptor kinase B;
                     tropomyosin-related kinase B; neurotrophic tyrosine kinase
                     receptor type 2"
                     /calculated_mol_wt=35201
     Region          1..39
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Region          49..127
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          58..62
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          71..74
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          89..96
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          106..112
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          120..123
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          130..223
                     /region_name="IgI_TrkB_d5"
                     /note="Fifth domain (immunoglobulin-like) of Trk receptor
                     TrkB; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05855"
                     /db_xref="CDD:409441"
     Region          130..138
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409441"
     Region          139..142
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409441"
     Region          145..153
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409441"
     Site            154
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409441"
     Region          156..163
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409441"
     Region          166..169
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409441"
     Region          174..179
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409441"
     Site            order(179,193..194,197)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:409441"
     Region          185..193
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409441"
     Region          201..209
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409441"
     Region          212..220
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409441"
     CDS             1..321
                     /gene="NTRK2"
                     /gene_synonym="DEE58; EIEE58; GP145-TrkB; OBHD; trk-B;
                     TRKB"
                     /coded_by="NM_001369550.1:338..1303"
                     /note="isoform k is encoded by transcript variant y"
                     /db_xref="CCDS:CCDS94429.1"
                     /db_xref="GeneID:4915"
                     /db_xref="HGNC:HGNC:8032"
                     /db_xref="MIM:600456"
ORIGIN      
        1 mwiktlqeak sspdtqdlyc lnessknipl anlqipncgl psanlaapnl tveegksitl
       61 scsvagdpvp nmywdvgnlv skhmnetsht qgslritnis sddsgkqisc vaenlvgedq
      121 dsvnltvhfa ptitflespt sdhhwcipft vkgnpkpalq wfyngailne skyictkihv
      181 tnhteyhgcl qldnpthmnn gdytliakne ygkdekqisa hfmgwpgidd ganpnypdvi
      241 yedygtaand igdttnrsne ipstdvtdkt grehlsvyav vviasvvgfc llvmlfllkl
      301 arhskfgmkg fvlfhkipld g
//
LOCUS       NP_001963                267 aa            linear   PRI 27-APR-2025
DEFINITION  neutrophil elastase preproprotein [Homo sapiens].
ACCESSION   NP_001963
VERSION     NP_001963.1
DBSOURCE    REFSEQ: accession NM_001972.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Birk,D., Siepmann,E., Simon,S. and Sommerhoff,C.P.
  TITLE     Human Neutrophil Elastase: Characterization of Intra- vs.
            Extracellular Inhibition
  JOURNAL   Int J Mol Sci 25 (14), 7917 (2024)
   PUBMED   39063160
  REMARK    GeneRIF: Human Neutrophil Elastase: Characterization of Intra- vs.
            Extracellular Inhibition.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Fragoso,J.M., Vargas-Alarcon,G., Martinez-Flores,A.E.,
            Montufar-Robles,I., Barbosa-Cobos,R.E., Rojas-Velasco,G. and
            Ramirez-Bello,J.
  TITLE     ELANE rs17223045C/T and rs3761007G/A variants: Protective factors
            against COVID-19
  JOURNAL   Biomol Biomed 24 (3), 665-672 (2024)
   PUBMED   38226800
  REMARK    GeneRIF: ELANE rs17223045C/T and rs3761007G/A variants: Protective
            factors against COVID-19.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Zheng,S., Bulut,G.B., Kummarapurugu,A.B., Ma,J. and Voynow,J.A.
  TITLE     Neutrophil Elastase Degrades Histone Deacetylases and Sirtuin 1 in
            Primary Human Monocyte Derived Macrophages
  JOURNAL   Int J Mol Sci 25 (8), 4265 (2024)
   PUBMED   38673851
  REMARK    GeneRIF: Neutrophil Elastase Degrades Histone Deacetylases and
            Sirtuin 1 in Primary Human Monocyte Derived Macrophages.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Wang,L., Zhou,Z., Xu,X., Li,Y., Zhang,R., Yu,Z., Huang,X., Zang,S.
            and Sun,T.
  TITLE     Elevated first-trimester neutrophil elastase and proteinase 3
            increase the risk of gestational diabetes mellitus and adverse
            fetal outcomes
  JOURNAL   Reprod Biol Endocrinol 22 (1), 2 (2024)
   PUBMED   38167145
  REMARK    GeneRIF: Elevated first-trimester neutrophil elastase and
            proteinase 3 increase the risk of gestational diabetes mellitus and
            adverse fetal outcomes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Horwitz,M.S., Corey,S.J., Grimes,H.L. and Tidwell,T.
  TITLE     ELANE mutations in cyclic and severe congenital neutropenia:
            genetics and pathophysiology
  JOURNAL   Hematol Oncol Clin North Am 27 (1), 19-41 (2013)
   PUBMED   23351986
  REMARK    GeneRIF: A review discusses how ELANE mutations provide clues into
            the pathogenesis of cyclic and severe congenital neutropenia.
            Review article
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Dale,D.C. and Makaryan,V.
  TITLE     ELANE-Related Neutropenia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301705
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Zimmer,M., Medcalf,R.L., Fink,T.M., Mattmann,C., Lichter,P. and
            Jenne,D.E.
  TITLE     Three human elastase-like genes coordinately expressed in the
            myelomonocyte lineage are organized as a single genetic locus on
            19pter
  JOURNAL   Proc Natl Acad Sci U S A 89 (17), 8215-8219 (1992)
   PUBMED   1518849
REFERENCE   8  (residues 1 to 267)
  AUTHORS   Higuchi,D.A., Wun,T.C., Likert,K.M. and Broze,G.J. Jr.
  TITLE     The effect of leukocyte elastase on tissue factor pathway inhibitor
  JOURNAL   Blood 79 (7), 1712-1719 (1992)
   PUBMED   1558967
REFERENCE   9  (residues 1 to 267)
  AUTHORS   Aoki,Y. and Hase,T.
  TITLE     The primary structure and elastinolytic activity of medullasin (a
            serine protease of bone marrow)
  JOURNAL   Biochem Biophys Res Commun 178 (2), 501-506 (1991)
   PUBMED   1859409
REFERENCE   10 (residues 1 to 267)
  AUTHORS   Fletcher,T.S., Shen,W.F. and Largman,C.
  TITLE     Primary structure of human pancreatic elastase 2 determined by
            sequence analysis of the cloned mRNA
  JOURNAL   Biochemistry 26 (23), 7256-7261 (1987)
   PUBMED   3427074
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M34379.1 and BI254663.1.
            
            Summary: Elastases form a subfamily of serine proteases that
            hydrolyze many proteins in addition to elastin. Humans have six
            elastase genes which encode structurally similar proteins. The
            encoded preproprotein is proteolytically processed to generate the
            active protease. Following activation, this protease hydrolyzes
            proteins within specialized neutrophil lysosomes, called azurophil
            granules, as well as proteins of the extracellular matrix. The
            enzyme may play a role in degenerative and inflammatory diseases
            through proteolysis of collagen-IV and elastin. This protein also
            degrades the outer membrane protein A (OmpA) of E. coli as well as
            the virulence factors of such bacteria as Shigella, Salmonella and
            Yersinia. Mutations in this gene are associated with cyclic
            neutropenia and severe congenital neutropenia (SCN). This gene is
            present in a gene cluster on chromosome 19. [provided by RefSeq,
            Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M34379.1, X05875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263621.2/ ENSP00000263621.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..267
                     /product="neutrophil elastase preproprotein"
                     /EC_number="3.4.21.37"
                     /note="medullasin; elastase 2, neutrophil; bone marrow
                     serine protease; leukocyte elastase; polymorphonuclear
                     elastase; granulocyte-derived elastase; elastase-2; PMN
                     elastase; polymorphonuclear leukocyte elastase"
                     /calculated_mol_wt=25778
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2759
     mat_peptide     30..267
                     /product="Neutrophil elastase. /id=PRO_0000027704"
                     /note="propagated from UniProtKB/Swiss-Prot (P08246.1)"
                     /calculated_mol_wt=25562
     Region          30..245
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            30
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(70,117,202)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P08246.1)"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26274980,
                     ECO:0000269|PubMed:3550808; propagated from
                     UniProtKB/Swiss-Prot (P08246.1)"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:3550808; propagated from
                     UniProtKB/Swiss-Prot (P08246.1)"
     Site            order(196,217,219)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..267
                     /gene="ELANE"
                     /gene_synonym="ELA2; GE; HLE; HNE; NE; PMN-E; SCN1"
                     /coded_by="NM_001972.4:27..830"
                     /db_xref="CCDS:CCDS12045.1"
                     /db_xref="GeneID:1991"
                     /db_xref="HGNC:HGNC:3309"
                     /db_xref="MIM:130130"
ORIGIN      
        1 mtlgrrlacl flacvlpall lggtalasei vggrrarpha wpfmvslqlr gghfcgatli
       61 apnfvmsaah cvanvnvrav rvvlgahnls rreptrqvfa vqrifengyd pvnllndivi
      121 lqlngsatin anvqvaqlpa qgrrlgngvq clamgwgllg rnrgiasvlq elnvtvvtsl
      181 crrsnvctlv rgrqagvcfg dsgsplvcng lihgiasfvr ggcasglypd afapvaqfvn
      241 widsiiqrse dnpcphprdp dpasrth
//
LOCUS       NP_005222                550 aa            linear   PRI 27-APR-2025
DEFINITION  src substrate cortactin isoform a [Homo sapiens].
ACCESSION   NP_005222
VERSION     NP_005222.2
DBSOURCE    REFSEQ: accession NM_005231.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Chen,S., Duan,X., He,Y. and Chen,W.
  TITLE     METTL3 promotes osteogenic differentiation of human umbilical cord
            mesenchymal stem cells by up-regulating m6A modification of
            circCTTN
  JOURNAL   Biosci Rep 44 (3) (2024)
   PUBMED   38358895
  REMARK    GeneRIF: METTL3 promotes osteogenic differentiation of human
            umbilical cord mesenchymal stem cells by up-regulating m6A
            modification of circCTTN.
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Inoue,H., Kanda,T., Hayashi,G., Munenaga,R., Yoshida,M.,
            Hasegawa,K., Miyagawa,T., Kurumada,Y., Hasegawa,J., Wada,T.,
            Horiuchi,M., Yoshimatsu,Y., Itoh,F., Maemoto,Y., Arasaki,K.,
            Wakana,Y., Watabe,T., Matsushita,H., Harada,H. and Tagaya,M.
  TITLE     A MAP1B-cortactin-Tks5 axis regulates TNBC invasion and
            tumorigenesis
  JOURNAL   J Cell Biol 223 (3) (2024)
   PUBMED   38353696
  REMARK    GeneRIF: A MAP1B-cortactin-Tks5 axis regulates TNBC invasion and
            tumorigenesis.
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Kumar,R., Rottner,K. and Rao,G.N.
  TITLE     Requirement of Site-Specific Tyrosine Phosphorylation of Cortactin
            in Retinal Neovascularization and Vascular Leakage
  JOURNAL   Arterioscler Thromb Vasc Biol 44 (2), 366-390 (2024)
   PUBMED   38126170
  REMARK    GeneRIF: Requirement of Site-Specific Tyrosine Phosphorylation of
            Cortactin in Retinal Neovascularization and Vascular Leakage.
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Yun,S.I., Kwak,C., Lee,S.Y., Shin,S., Oh,C., Kim,J.S., Rhee,H.W.
            and Kim,K.K.
  TITLE     Binding of USP4 to cortactin enhances cell migration in HCT116
            human colon cancer cells
  JOURNAL   FASEB J 37 (5), e22900 (2023)
   PUBMED   37039823
  REMARK    GeneRIF: Binding of USP4 to cortactin enhances cell migration in
            HCT116 human colon cancer cells.
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Senguven Tokozlu,B., Sapkota,D., Vallenari,E.M., Schreurs,O. and
            Soland,T.M.
  TITLE     Cortactin expression in a Norwegian cohort of human papilloma virus
            negative oral squamous cell carcinomas of the mobile tongue
  JOURNAL   Eur J Oral Sci 131 (2), e12925 (2023)
   PUBMED   36790139
  REMARK    GeneRIF: Cortactin expression in a Norwegian cohort of human
            papilloma virus negative oral squamous cell carcinomas of the
            mobile tongue.
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Schuuring,E., Verhoeven,E., Litvinov,S. and Michalides,R.J.
  TITLE     The product of the EMS1 gene, amplified and overexpressed in human
            carcinomas, is homologous to a v-src substrate and is located in
            cell-substratum contact sites
  JOURNAL   Mol Cell Biol 13 (5), 2891-2898 (1993)
   PUBMED   8474448
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Brookes,S., Lammie,G.A., Schuuring,E., de Boer,C., Michalides,R.,
            Dickson,C. and Peters,G.
  TITLE     Amplified region of chromosome band 11q13 in breast and squamous
            cell carcinomas encompasses three CpG islands telomeric of FGF3,
            including the expressed gene EMS1
  JOURNAL   Genes Chromosomes Cancer 6 (4), 222-231 (1993)
   PUBMED   7685625
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Wu,H. and Parsons,J.T.
  TITLE     Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous
            actin-binding protein enriched in the cell cortex
  JOURNAL   J Cell Biol 120 (6), 1417-1426 (1993)
   PUBMED   7680654
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Schuuring,E., Verhoeven,E., Mooi,W.J. and Michalides,R.J.
  TITLE     Identification and cloning of two overexpressed genes, U21B31/PRAD1
            and EMS1, within the amplified chromosome 11q13 region in human
            carcinomas
  JOURNAL   Oncogene 7 (2), 355-361 (1992)
   PUBMED   1532244
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA716772.1, AK222613.1,
            AK291097.1 and BC008799.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 30, 2002 this sequence version replaced NP_005222.1.
            
            Summary: This gene is overexpressed in breast cancer and squamous
            cell carcinomas of the head and neck. The encoded protein is
            localized in the cytoplasm and in areas of the cell-substratum
            contacts. This gene has two roles: (1) regulating the interactions
            between components of adherens-type junctions and (2) organizing
            the cytoskeleton and cell adhesion structures of epithelia and
            carcinoma cells. During apoptosis, the encoded protein is degraded
            in a caspase-dependent manner. The aberrant regulation of this gene
            contributes to tumor cell invasion and metastasis. Three splice
            variants that encode different isoforms have been identified for
            this gene. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) is the longest transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GQ900949.1, SRR3476690.713548.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301843.13/ ENSP00000301843.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.3"
     Protein         1..550
                     /product="src substrate cortactin isoform a"
                     /note="oncogene EMS1; ems1 sequence (mammary tumor and
                     squamous cell carcinoma-associated (p80/85 src substrate);
                     amplaxin; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=61455
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Region          80..116
                     /region_name="Cortactin 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Region          83..116
                     /region_name="HS1_rep"
                     /note="Repeat in HS1/Cortactin; pfam02218"
                     /db_xref="CDD:460497"
     Site            87
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            107
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          117..153
                     /region_name="Cortactin 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Site            119
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          120..155
                     /region_name="HS1_rep"
                     /note="Repeat in HS1/Cortactin; pfam02218"
                     /db_xref="CDD:460497"
     Site            124
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            152
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          154..190
                     /region_name="Cortactin 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Region          157..192
                     /region_name="HS1_rep"
                     /note="Repeat in HS1/Cortactin; pfam02218"
                     /db_xref="CDD:460497"
     Site            161
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            181
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          191..227
                     /region_name="Cortactin 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Site            193
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          194..228
                     /region_name="HS1_rep"
                     /note="Repeat in HS1/Cortactin; pfam02218"
                     /db_xref="CDD:460497"
     Site            198
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          228..264
                     /region_name="Cortactin 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Region          231..266
                     /region_name="HS1_rep"
                     /note="Repeat in HS1/Cortactin; pfam02218"
                     /db_xref="CDD:460497"
     Site            235
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          265..301
                     /region_name="Cortactin 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Region          268..303
                     /region_name="HS1_rep"
                     /note="Repeat in HS1/Cortactin; pfam02218"
                     /db_xref="CDD:460497"
     Site            272
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            295
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          302..324
                     /region_name="Cortactin 7, truncated"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Site            304
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          305..>331
                     /region_name="HS1_rep"
                     /note="Repeat in HS1/Cortactin; pfam02218"
                     /db_xref="CDD:460497"
     Site            309
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            314
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          <325..>430
                     /region_name="PspC_subgroup_1"
                     /note="pneumococcal surface protein PspC, choline-binding
                     form; NF033838"
                     /db_xref="CDD:468201"
     Region          344..419
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Site            346
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          358..>396
                     /region_name="Casc1_N"
                     /note="Cancer susceptibility candidate 1 N-terminus;
                     pfam15927"
                     /db_xref="CDD:464947"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14247.2)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FAK1.
                     /evidence=ECO:0000250|UniProtKB:Q66HL2; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:15561106,
                     ECO:0000269|PubMed:17959782; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:Q60598; propagated from
                     UniProtKB/Swiss-Prot (Q14247.2)"
     Region          496..548
                     /region_name="SH3_Cortactin"
                     /note="Src homology 3 domain of Cortactin; cd11959"
                     /db_xref="CDD:212892"
     Site            order(501,503,506,509..510,528..529,540,542,544..545)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212892"
     CDS             1..550
                     /gene="CTTN"
                     /gene_synonym="EMS1"
                     /coded_by="NM_005231.4:184..1836"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41680.1"
                     /db_xref="GeneID:2017"
                     /db_xref="HGNC:HGNC:3338"
                     /db_xref="MIM:164765"
ORIGIN      
        1 mwkasaghav siaqddagad dwetdpdfvn dvsekeqrwg aktvqgsghq ehinihklre
       61 nvfqehqtlk ekeletgpka shgyggkfgv eqdrmdksav gheyqsklsk hcsqvdsvrg
      121 fggkfgvqmd rvdqsavgfe yqgktekhas qkdyssgfgg kygvqadrvd ksavgfdyqg
      181 ktekhesqrd yskgfggkyg idkdkvdksa vgfeyqgkte khesqkdyvk gfggkfgvqt
      241 drqdkcalgw dhqeklqlhe sqkdyktgfg gkfgvqserq dsaavgfdyk eklakhesqq
      301 dyskgfggky gvqkdrmdkn astfedvtqv ssayqktvpv eavtsktsni ranfenlake
      361 keqedrrkae aeraqrmake rqeqeearrk leeqaraktq tppvspapqp teerlpsspv
      421 yedaasfkae lsyrgpvsgt epepvysmea adyreassqq glayateavy esaeapghyp
      481 aedstydeye ndlgitaval ydyqaagdde isfdpddiit niemiddgww rgvckgrygl
      541 fpanyvelrq
//
LOCUS       NP_001077862             134 aa            linear   PRI 27-APR-2025
DEFINITION  D-dopachrome decarboxylase-like protein [Homo sapiens].
ACCESSION   NP_001077862
VERSION     NP_001077862.1
DBSOURCE    REFSEQ: accession NM_001084393.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Florez-Sampedro,L., Brandsma,C.A., de Vries,M., Timens,W.,
            Bults,R., Vermeulen,C.J., van den Berge,M., Obeidat,M., Joubert,P.,
            Nickle,D.C., Poelarends,G.J., Faiz,A. and Melgert,B.N.
  TITLE     Genetic regulation of gene expression of MIF family members in lung
            tissue
  JOURNAL   Sci Rep 10 (1), 16980 (2020)
   PUBMED   33046825
  REMARK    GeneRIF: Genetic regulation of gene expression of MIF family
            members in lung tissue.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Nakamura,T., Ohnuma,T., Hanzawa,R., Takebayashi,Y., Takeda,M.,
            Nishimon,S., Sannohe,T., Katsuta,N., Higashiyama,R., Shibata,N. and
            Arai,H.
  TITLE     Associations of common copy number variants in glutathione
            S-transferase mu 1 and D-dopachrome tautomerase-like protein genes
            with risk of schizophrenia in a Japanese population
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 168 (7), 630-636 (2015)
   PUBMED   26175060
  REMARK    GeneRIF: Authors performed genetic case-control CNV analyses to
            test for possible associations between schizophrenia and CNVs for
            the three genes GSTT1, DDTL, and GSTM1 in Japanese patients.
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Chambers,J.C., Zhang,W., Sehmi,J., Li,X., Wass,M.N., Van der
            Harst,P., Holm,H., Sanna,S., Kavousi,M., Baumeister,S.E.,
            Coin,L.J., Deng,G., Gieger,C., Heard-Costa,N.L., Hottenga,J.J.,
            Kuhnel,B., Kumar,V., Lagou,V., Liang,L., Luan,J., Vidal,P.M., Mateo
            Leach,I., O'Reilly,P.F., Peden,J.F., Rahmioglu,N., Soininen,P.,
            Speliotes,E.K., Yuan,X., Thorleifsson,G., Alizadeh,B.Z.,
            Atwood,L.D., Borecki,I.B., Brown,M.J., Charoen,P., Cucca,F.,
            Das,D., de Geus,E.J., Dixon,A.L., Doring,A., Ehret,G.,
            Eyjolfsson,G.I., Farrall,M., Forouhi,N.G., Friedrich,N.,
            Goessling,W., Gudbjartsson,D.F., Harris,T.B., Hartikainen,A.L.,
            Heath,S., Hirschfield,G.M., Hofman,A., Homuth,G., Hypponen,E.,
            Janssen,H.L., Johnson,T., Kangas,A.J., Kema,I.P., Kuhn,J.P.,
            Lai,S., Lathrop,M., Lerch,M.M., Li,Y., Liang,T.J., Lin,J.P.,
            Loos,R.J., Martin,N.G., Moffatt,M.F., Montgomery,G.W., Munroe,P.B.,
            Musunuru,K., Nakamura,Y., O'Donnell,C.J., Olafsson,I.,
            Penninx,B.W., Pouta,A., Prins,B.P., Prokopenko,I., Puls,R.,
            Ruokonen,A., Savolainen,M.J., Schlessinger,D., Schouten,J.N.,
            Seedorf,U., Sen-Chowdhry,S., Siminovitch,K.A., Smit,J.H.,
            Spector,T.D., Tan,W., Teslovich,T.M., Tukiainen,T.,
            Uitterlinden,A.G., Van der Klauw,M.M., Vasan,R.S., Wallace,C.,
            Wallaschofski,H., Wichmann,H.E., Willemsen,G., Wurtz,P., Xu,C.,
            Yerges-Armstrong,L.M., Abecasis,G.R., Ahmadi,K.R., Boomsma,D.I.,
            Caulfield,M., Cookson,W.O., van Duijn,C.M., Froguel,P., Matsuda,K.,
            McCarthy,M.I., Meisinger,C., Mooser,V., Pietilainen,K.H.,
            Schumann,G., Snieder,H., Sternberg,M.J., Stolk,R.P., Thomas,H.C.,
            Thorsteinsdottir,U., Uda,M., Waeber,G., Wareham,N.J.,
            Waterworth,D.M., Watkins,H., Whitfield,J.B., Witteman,J.C.,
            Wolffenbuttel,B.H., Fox,C.S., Ala-Korpela,M., Stefansson,K.,
            Vollenweider,P., Volzke,H., Schadt,E.E., Scott,J., Jarvelin,M.R.,
            Elliott,P. and Kooner,J.S.
  CONSRTM   Alcohol Genome-wide Association (AlcGen) Consortium; Diabetes
            Genetics Replication and Meta-analyses (DIAGRAM+) Study; Genetic
            Investigation of Anthropometric Traits (GIANT) Consortium; Global
            Lipids Genetics Consortium; Genetics of Liver Disease (GOLD)
            Consortium; International Consortium for Blood Pressure
            (ICBP-GWAS); Meta-analyses of Glucose and Insulin-Related Traits
            Consortium (MAGIC)
  TITLE     Genome-wide association study identifies loci influencing
            concentrations of liver enzymes in plasma
  JOURNAL   Nat Genet 43 (11), 1131-1138 (2011)
   PUBMED   22001757
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   5  (residues 1 to 134)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 134)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   7  (residues 1 to 134)
  AUTHORS   Coggan,M., Whitbread,L., Whittington,A. and Board,P.
  TITLE     Structure and organization of the human theta-class glutathione
            S-transferase and D-dopachrome tautomerase gene complex
  JOURNAL   Biochem J 334 (Pt 3) (Pt 3), 617-623 (1998)
   PUBMED   9729470
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB157727.1, AC253536.1 and AI686044.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296110.1, SRR3476690.165579.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215770.6/ ENSP00000215770.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.23"
     Protein         1..134
                     /product="D-dopachrome decarboxylase-like protein"
                     /EC_number="4.1.1.-"
                     /note="D-dopachrome tautomerase-like protein; D-dopachrome
                     decarboxylase; Phenylpyruvate tautomerase II"
                     /calculated_mol_wt=14064
     Region          2..95
                     /region_name="4Oxalocrotonate_Tautomerase"
                     /note="4-Oxalocrotonate Tautomerase: Catalyzes the
                     isomerization of unsaturated ketones. The structure is a
                     homohexamer that is arranged as a trimer of dimers. The
                     hexamer contains six active sites, each formed by residues
                     from three monomers, two from one...; cl00235"
                     /db_xref="CDD:444774"
     CDS             1..134
                     /gene="DDTL"
                     /gene_synonym="DDT; KB-226F1.2"
                     /coded_by="NM_001084393.2:28..432"
                     /db_xref="CCDS:CCDS42988.1"
                     /db_xref="GeneID:100037417"
                     /db_xref="HGNC:HGNC:33446"
ORIGIN      
        1 mpfleldtnl panrvpagle krlcaaaasi lgkpadrvnv tvrpglamal sgstepcaql
       61 sissigvvgt aednrshsah ffefltkela lgqdrfptvl stspaahggp rcpgeiiegk
      121 ksclneealf iyfi
//
LOCUS       NP_083657                189 aa            linear   ROD 27-APR-2025
DEFINITION  testis-expressed protein 22 [Mus musculus].
ACCESSION   NP_083657 XP_127115
VERSION     NP_083657.1
DBSOURCE    REFSEQ: accession NM_029381.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Miyata,H., Castaneda,J.M., Fujihara,Y., Yu,Z., Archambeault,D.R.,
            Isotani,A., Kiyozumi,D., Kriseman,M.L., Mashiko,D., Matsumura,T.,
            Matzuk,R.M., Mori,M., Noda,T., Oji,A., Okabe,M.,
            Prunskaite-Hyyrylainen,R., Ramirez-Solis,R., Satouh,Y., Zhang,Q.,
            Ikawa,M. and Matzuk,M.M.
  TITLE     Genome engineering uncovers 54 evolutionarily conserved and
            testis-enriched genes that are not required for male fertility in
            mice
  JOURNAL   Proc Natl Acad Sci U S A 113 (28), 7704-7710 (2016)
   PUBMED   27357688
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Neesen,J., Hartwich,T., Brandhorst,G., Aumuller,G., Glaser,B.,
            Burfeind,P. and Mendoza-Lujambio,I.
  TITLE     Tep22, a novel testicular expressed gene, is involved in the
            biogenesis of the acrosome and the midpiece of the sperm tail
  JOURNAL   Biochem Biophys Res Commun 297 (4), 737-748 (2002)
   PUBMED   12359214
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073562.6.
            
            On Jan 24, 2005 this sequence version replaced XP_127115.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF522069.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 61.57 cM"
     Protein         1..189
                     /product="testis-expressed protein 22"
                     /note="testis-expressed sequence 22 protein;
                     testis-expressed protein of 22 kDa"
                     /calculated_mol_wt=21371
     Region          1..120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D9U4.1)"
     CDS             1..189
                     /gene="Tex22"
                     /gene_synonym="1700028O09Rik; Tep22"
                     /coded_by="NM_029381.2:677..1246"
                     /db_xref="CCDS:CCDS26203.1"
                     /db_xref="GeneID:75671"
                     /db_xref="MGI:MGI:1922921"
ORIGIN      
        1 mdsrqqrpqr ktlqwqlaqe qrqqsppqgl avassqpdtk skpqddlqtq dwvcepqelr
       61 rpgsrwnisi derrrlalqr mqertdtara psgdplglhp egqqtetsps tqsvptpplq
      121 acetmadplq diahvlaelm segverdvli sqplrstens nafqdflaqd aplwkdenfe
      181 aqtsrwphs
//
LOCUS       NP_003650                658 aa            linear   PRI 27-APR-2025
DEFINITION  alkyldihydroxyacetonephosphate synthase, peroxisomal precursor
            [Homo sapiens].
ACCESSION   NP_003650
VERSION     NP_003650.1
DBSOURCE    REFSEQ: accession NM_003659.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Zhang,Y., Huang,Z., Li,K., Xie,G., Feng,Y., Wang,Z., Li,N., Liu,R.,
            Ding,Y., Wang,J., Yang,J. and Jia,Z.
  TITLE     TrkA promotes MDM2-mediated AGPS ubiquitination and degradation to
            trigger prostate cancer progression
  JOURNAL   J Exp Clin Cancer Res 43 (1), 16 (2024)
   PUBMED   38200609
  REMARK    GeneRIF: TrkA promotes MDM2-mediated AGPS ubiquitination and
            degradation to trigger prostate cancer progression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Zhou,W., Liu,Y., Li,H., Song,Z., Ma,Y. and Zhu,Y.
  TITLE     Mass Spectrometry and Computer Simulation Predict the Interactions
            of AGPS and HNRNPK in Glioma
  JOURNAL   Biomed Res Int 2021, 6181936 (2021)
   PUBMED   34621897
  REMARK    GeneRIF: Mass Spectrometry and Computer Simulation Predict the
            Interactions of AGPS and HNRNPK in Glioma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 658)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 658)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 658)
  AUTHORS   Zhu,Y., Liu,A., Zhang,X., Qi,L., Zhang,L., Xue,J., Liu,Y. and
            Yang,P.
  TITLE     The effect of benzyl isothiocyanate and its computer-aided design
            derivants targeting alkylglycerone phosphate synthase on the
            inhibition of human glioma U87MG cell line
  JOURNAL   Tumour Biol 36 (5), 3499-3509 (2015)
   PUBMED   25542233
  REMARK    GeneRIF: we optimized the BITC construction targeting
            alkylglycerone phosphate synthase (AGPS) by computer-aided design,
            and the derivants also showed anti-tumor potential in vitro.
REFERENCE   6  (residues 1 to 658)
  AUTHORS   Wanders,R.J., Dekker,C., Hovarth,V.A., Schutgens,R.B., Tager,J.M.,
            Van Laer,P. and Lecoutere,D.
  TITLE     Human alkyldihydroxyacetonephosphate synthase deficiency: a new
            peroxisomal disorder
  JOURNAL   J Inherit Metab Dis 17 (3), 315-318 (1994)
   PUBMED   7807941
REFERENCE   7  (residues 1 to 658)
  AUTHORS   Brown,A. and Snyder,F.
  TITLE     Alkyldihydroxyacetonephosphate synthase
  JOURNAL   Methods Enzymol 209, 377-384 (1992)
   PUBMED   1495418
REFERENCE   8  (residues 1 to 658)
  AUTHORS   Singh,H., Usher,S. and Poulos,A.
  TITLE     Dihydroxyacetone phosphate acyltransferase and
            alkyldihydroxyacetone phosphate synthase activities in rat liver
            subcellular fractions and human skin fibroblasts
  JOURNAL   Arch Biochem Biophys 268 (2), 676-686 (1989)
   PUBMED   2464339
REFERENCE   9  (residues 1 to 658)
  AUTHORS   Webber,K.O., Datta,N.S. and Hajra,A.K.
  TITLE     Properties of the enzymes catalyzing the biosynthesis of
            lysophosphatidate and its ether analog in cultured fibroblasts from
            Zellweger syndrome patients and normal controls
  JOURNAL   Arch Biochem Biophys 254 (2), 611-620 (1987)
   PUBMED   3646870
REFERENCE   10 (residues 1 to 658)
  AUTHORS   Schrakamp,G., Roosenboom,C.F., Schutgens,R.B., Wanders,R.J.,
            Heymans,H.S., Tager,J.M. and van den Bosch,H.
  TITLE     Alkyl dihydroxyacetone phosphate synthase in human fibroblasts and
            its deficiency in Zellweger syndrome
  JOURNAL   J Lipid Res 26 (7), 867-873 (1985)
   PUBMED   4031664
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314259.1, AC073834.6 and
            AA832354.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the FAD-binding
            oxidoreductase/transferase type 4 family. It encodes a protein that
            catalyzes the second step of ether lipid biosynthesis in which
            acyl-dihydroxyacetonephosphate (DHAP) is converted to alkyl-DHAP by
            the addition of a long chain alcohol and the removal of a
            long-chain acid anion. The protein is localized to the inner aspect
            of the peroxisomal membrane and requires FAD as a cofactor.
            Mutations in this gene have been associated with rhizomelic
            chondrodysplasia punctata, type 3 and Zellweger syndrome. [provided
            by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.69648.1,
                                           SRR1660807.66305.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264167.11/ ENSP00000264167.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.2"
     Protein         1..658
                     /product="alkyldihydroxyacetonephosphate synthase,
                     peroxisomal precursor"
                     /EC_number="2.5.1.26"
                     /note="alkyldihydroxyacetonephosphate synthase,
                     peroxisomal; alkyl-DHAP synthase; aging-associated protein
                     5; aging-associated gene 5 protein"
                     /calculated_mol_wt=67065
     sig_peptide     1..58
                     /note="includes a peroxisomal targeting signal 2 (PTS2)
                     sequence"
                     /calculated_mol_wt=5865
     transit_peptide 1..58
                     /note="Peroxisome. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O00116.1)"
                     /calculated_mol_wt=5865
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00116.1)"
     mat_peptide     59..658
                     /product="alkyldihydroxyacetonephosphate synthase,
                     peroxisomal"
                     /calculated_mol_wt=67065
     Region          63..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00116.1)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00116.1)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00116.1)"
     Site            102
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O00116.1)"
     Region          200..652
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Site            347
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O00116.1)"
     Site            419
                     /site_type="other"
                     /note="Important for enzyme activity.
                     /evidence=ECO:0000269|PubMed:9553082; propagated from
                     UniProtKB/Swiss-Prot (O00116.1)"
     Region          615..617
                     /region_name="Important for enzyme activity.
                     /evidence=ECO:0000250|UniProtKB:P97275"
                     /note="propagated from UniProtKB/Swiss-Prot (O00116.1)"
     Region          654..658
                     /region_name="Important for enzyme activity.
                     /evidence=ECO:0000250|UniProtKB:P97275"
                     /note="propagated from UniProtKB/Swiss-Prot (O00116.1)"
     CDS             1..658
                     /gene="AGPS"
                     /gene_synonym="ADAP-S; ADAS; ADHAPS; ADPS; ALDHPSY; RCDP3"
                     /coded_by="NM_003659.4:18..1994"
                     /db_xref="CCDS:CCDS2275.1"
                     /db_xref="GeneID:8540"
                     /db_xref="HGNC:HGNC:327"
                     /db_xref="MIM:603051"
ORIGIN      
        1 maeaaaaagg tglgagasyg saadrdrdpd pdragrrlrv lsghllgrpr ealstnecka
       61 rraasaataa ptatpaaqes gtipkkrqev mkwngwgynd skfifnkkgq ieltgkrypl
      121 sgmglptfke wiqntlgvnv ehkttskasl npsdtppsvv nedflhdlke tnisysqead
      181 drvfrahghc lheifllreg mferipdivl wptchddvvk ivnlackynl ciipigggts
      241 vsyglmcpad etrtiisldt sqmnrilwvd ennltahvea gitgqelerq lkesgyctgh
      301 epdslefstv ggwvstrasg mkkniygnie dlvvhikmvt prgiiekscq gprmstgpdi
      361 hhfimgsegt lgviteatik irpvpeyqky gsvafpnfeq gvaclreiak qrcapasirl
      421 mdnkqfqfgh alkpqvssif tsfldglkkf yitkfkgfdp nqlsvatllf egdrekvlqh
      481 ekqvydiaak fgglaagedn gqrgylltyv iayirdlale yyvlgesfet sapwdrvvdl
      541 crnvkeritr eckekgvqfa pfstcrvtqt ydagaciyfy fafnyrgisd pltvfeqtea
      601 aareeilang gslshhhgvg klrkqwlkes isdvgfgmlk svkeyvdpnn ifgnrnll
//
LOCUS       NP_006803                667 aa            linear   PRI 27-APR-2025
DEFINITION  protein OS-9 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_006803
VERSION     NP_006803.1
DBSOURCE    REFSEQ: accession NM_006812.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Li,W., Chung,C.Y.L., Wang,C.C., Chan,T.F., Leung,M.B.W., Chan,O.K.,
            Wu,L., Appiah,K., Chaemsaithong,P., Cheng,Y.K.Y., Poon,L.C.Y. and
            Leung,T.Y.
  TITLE     Monochorionic twins with selective fetal growth restriction:
            insight from placental whole-transcriptome analysis
  JOURNAL   Am J Obstet Gynecol 223 (5), 749 (2020)
   PUBMED   32437666
  REMARK    GeneRIF: Monochorionic twins with selective fetal growth
            restriction: insight from placental whole-transcriptome analysis.
REFERENCE   5  (residues 1 to 667)
  AUTHORS   van der Goot,A.T., Pearce,M.M.P., Leto,D.E., Shaler,T.A. and
            Kopito,R.R.
  TITLE     Redundant and Antagonistic Roles of XTP3B and OS9 in Decoding
            Glycan and Non-glycan Degrons in ER-Associated Degradation
  JOURNAL   Mol Cell 70 (3), 516-530 (2018)
   PUBMED   29706535
  REMARK    GeneRIF: The relative expression of OS9 and XTP3B and the
            distribution of glycan and non-glycan degrons within the same
            protein contribute to the fidelity.
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Kimura,Y., Nakazawa,M. and Yamada,M.
  TITLE     Cloning and characterization of three isoforms of OS-9 cDNA and
            expression of the OS-9 gene in various human tumor cell lines
  JOURNAL   J Biochem 123 (5), 876-882 (1998)
   PUBMED   9562620
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Kimura,Y., Nakazawa,M., Tsuchiya,N., Asakawa,S., Shimizu,N. and
            Yamada,M.
  TITLE     Genomic organization of the OS-9 gene amplified in human sarcomas
  JOURNAL   J Biochem 122 (6), 1190-1195 (1997)
   PUBMED   9498564
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Elkahloun,A.G., Krizman,D.B., Wang,Z., Hofmann,T.A., Roe,B. and
            Meltzer,P.S.
  TITLE     Transcript mapping in a 46-kb sequenced region at the core of
            12q13.3 amplification in human cancers
  JOURNAL   Genomics 42 (2), 295-301 (1997)
   PUBMED   9192850
REFERENCE   9  (residues 1 to 667)
  AUTHORS   Su,Y.A., Hutter,C.M., Trent,J.M. and Meltzer,P.S.
  TITLE     Complete sequence analysis of a gene (OS-9) ubiquitously expressed
            in human tissues and amplified in sarcomas
  JOURNAL   Mol Carcinog 15 (4), 270-275 (1996)
   PUBMED   8634085
REFERENCE   10 (residues 1 to 667)
  AUTHORS   Su,Y.A., Trent,J.M., Guan,X.Y. and Meltzer,P.S.
  TITLE     Direct isolation of genes encoded within a homogeneously staining
            region by chromosome microdissection
  JOURNAL   Proc Natl Acad Sci U S A 91 (19), 9121-9125 (1994)
   PUBMED   8090779
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU132426.1, BC000532.2,
            U41635.1 and BC023513.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that is highly expressed in
            osteosarcomas. This protein binds to the hypoxia-inducible factor 1
            (HIF-1), a key regulator of the hypoxic response and angiogenesis,
            and promotes the degradation of one of its subunits. Alternate
            transcriptional splice variants, encoding different isoforms, have
            been characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1, also referred to as
            OS-9-1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.837461.1,
                                           SRR1660809.22245.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315970.12/ ENSP00000318165.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3-q14.1"
     Protein         1..667
                     /product="protein OS-9 isoform 1 precursor"
                     /note="erlectin 2; endoplasmic reticulum lectin 2;
                     osteosarcoma amplified 9, endoplasmic reticulum associated
                     protein; protein OS-9; amplified in osteosarcoma 9;
                     osteosarcoma amplified 9, endoplasmic reticulum lectin"
                     /calculated_mol_wt=72942
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2638
     mat_peptide     26..667
                     /product="protein OS-9 isoform 1"
                     /calculated_mol_wt=73056
     Region          110..181
                     /region_name="PRKCSH"
                     /note="Glucosidase II beta subunit-like protein;
                     pfam07915"
                     /db_xref="CDD:400321"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13438.1)"
     Region          284..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13438.1)"
     Region          372..452
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13438.1)"
     Region          464..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13438.1)"
     Region          504..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13438.1)"
     Region          633..667
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13438.1)"
     CDS             1..667
                     /gene="OS9"
                     /gene_synonym="ERLEC2; OS-9"
                     /coded_by="NM_006812.4:31..2034"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS31843.1"
                     /db_xref="GeneID:10956"
                     /db_xref="HGNC:HGNC:16994"
                     /db_xref="MIM:609677"
ORIGIN      
        1 maaetllssl lgllllglll pasltggvgs lnleelsemr ygieilplpv mggqsqssdv
       61 vivsskykqr yecrlpagai hfqrereeet payqgpgipe llspmrdapc llktkdwwty
      121 efcygrhiqq yhmedseikg evlylgyyqs afdwddetak askqhrlkry hsqtygngsk
      181 cdlngrprea evrflcdega gisgdyidrv deplscsyvl tirtprlcph pllrpppsaa
      241 pqailchpsl qpeeymayvq rqadskqygd kiieelqdlg pqvwsetksg vapqkmagas
      301 ptkddskdsd fwkmlneped qapggeevpa eeqdpspeaa dsasgapndf qnnvqvkvir
      361 spadlirfie elkggtkkgk pnigqeqpvd daaevpqrep ekergdperq remeeeeded
      421 ededededer qllgefekel egillpsdrd rlrsevkagm ereleniiqe tekeldpdgl
      481 kkeserdram laltstlnkl ikrleekqsp elvkkhkkkr vvpkkpppsp qpteedpehr
      541 vrvrvtklrl ggpnqdltvl emkrenpqlk qieglvkell eregltaagk ieikivrpwa
      601 egteegarwl tdedtrnlke iffnilvpga eeaqkerqrq kelesnyrrv wgspggegtg
      661 dldefdf
//
LOCUS       NP_055033                348 aa            linear   PRI 27-APR-2025
DEFINITION  killer cell immunoglobulin-like receptor 2DL1 precursor [Homo
            sapiens].
ACCESSION   NP_055033 XP_006725501 XP_006725719 XP_006725854
VERSION     NP_055033.2
DBSOURCE    REFSEQ: accession NM_014218.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Simeni,L.K., Ekali,G.L., Yengo,C.K., Wouambo,R.K., Fischer,J.,
            Bessong,O.M.A., Fokam,J., Yindom,L.M. and Nguedia,J.C.A.
  TITLE     KIR2DL1 gene is a surrogate marker of protection against
            infection-related hospitalization among HIV-1 unexposed versus
            exposed uninfected infants in Cameroon
  JOURNAL   BMC Immunol 25 (1), 54 (2024)
   PUBMED   39090586
  REMARK    GeneRIF: KIR2DL1 gene is a surrogate marker of protection against
            infection-related hospitalization among HIV-1 unexposed versus
            exposed uninfected infants in Cameroon.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Leijonhufvud,C., Sanz-Ortega,L., Schlums,H., Gaballa,A.,
            Andersson,A., Eriksson,C., Segerberg,F., Uhlin,M., Bryceson,Y.T.
            and Carlsten,M.
  TITLE     KIR2DS1 and KIR2DL1-C245 Dominantly Repress NK Cell Degranulation
            Triggered by Monoclonal or Bispecific Antibodies, whereas Education
            by Uptuning Inhibitory Killer Ig-related Receptors Exerts No
            Advantage in Ab-dependent Cellular Cytotoxicity
  JOURNAL   J Immunol 212 (5), 868-880 (2024)
   PUBMED   38240527
  REMARK    GeneRIF: KIR2DS1 and KIR2DL1-C245 Dominantly Repress NK Cell
            Degranulation Triggered by Monoclonal or Bispecific Antibodies,
            whereas Education by Uptuning Inhibitory Killer Ig-related
            Receptors Exerts No Advantage in Ab-dependent Cellular
            Cytotoxicity.
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Halimi,H., Mirzazadeh,S., Kalantar,K., Hajimaghsoodi,M., Ramzi,M.
            and Farjadian,S.
  TITLE     Activating KIR/HLA-I combinations as a risk factor of adult B-ALL
  JOURNAL   Hum Immunol 85 (2), 110750 (2024)
   PUBMED   38262874
  REMARK    GeneRIF: Activating KIR/HLA-I combinations as a risk factor of
            adult B-ALL.
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Wright,P.W., Li,H., Rahman,M.A., Anderson,E.M., Karwan,M.,
            Carrell,J. and Anderson,S.K.
  TITLE     The KIR2DL1 intermediate upstream element participates in gene
            activation
  JOURNAL   Immunogenetics 75 (6), 495-506 (2023)
   PUBMED   37801092
  REMARK    GeneRIF: The KIR2DL1 intermediate upstream element participates in
            gene activation.
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Woon,E.V., Nikolaou,D., MacLaran,K., Norman-Taylor,J., Bhagwat,P.,
            Cuff,A.O., Johnson,M.R. and Male,V.
  TITLE     Uterine NK cells underexpress KIR2DL1/S1 and LILRB1 in reproductive
            failure
  JOURNAL   Front Immunol 13, 1108163 (2023)
   PUBMED   36713400
  REMARK    GeneRIF: Uterine NK cells underexpress KIR2DL1/S1 and LILRB1 in
            reproductive failure.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Kim,J., Chwae,Y.J., Kim,M.Y., Choi,I.H., Park,J.H. and Kim,S.J.
  TITLE     Molecular basis of HLA-C recognition by p58 natural killer cell
            inhibitory receptors
  JOURNAL   J Immunol 159 (8), 3875-3882 (1997)
   PUBMED   9378975
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Fan,Q.R., Mosyak,L., Winter,C.C., Wagtmann,N., Long,E.O. and
            Wiley,D.C.
  TITLE     Structure of the inhibitory receptor for human natural killer cells
            resembles haematopoietic receptors
  JOURNAL   Nature 389 (6646), 96-100 (1997)
   PUBMED   9288975
  REMARK    Erratum:[Nature 1997 Nov 20;390(6657):315]
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Fry,A.M., Lanier,L.L. and Weiss,A.
  TITLE     Phosphotyrosines in the killer cell inhibitory receptor motif of
            NKB1 are required for negative signaling and for association with
            protein tyrosine phosphatase 1C
  JOURNAL   J Exp Med 184 (1), 295-300 (1996)
   PUBMED   8691146
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Wagtmann,N., Biassoni,R., Cantoni,C., Verdiani,S., Malnati,M.S.,
            Vitale,M., Bottino,C., Moretta,L., Moretta,A. and Long,E.O.
  TITLE     Molecular clones of the p58 NK cell receptor reveal
            immunoglobulin-related molecules with diversity in both the extra-
            and intracellular domains
  JOURNAL   Immunity 2 (5), 439-449 (1995)
   PUBMED   7749980
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Colonna,M. and Samaridis,J.
  TITLE     Cloning of immunoglobulin-superfamily members associated with HLA-C
            and HLA-B recognition by human natural killer cells
  JOURNAL   Science 268 (5209), 405-408 (1995)
   PUBMED   7716543
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245128.3, AY366240.1,
            AY366237.1 and AC011501.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Feb 9, 2014 this sequence version replaced
            XP_006725854.1, XP_006725501.1, XP_006725719.1, NP_055033.1.
            
            Summary: Killer cell immunoglobulin-like receptors (KIRs) are
            transmembrane glycoproteins expressed by natural killer cells and
            subsets of T cells. The KIR genes are polymorphic and highly
            homologous and they are found in a cluster on chromosome 19q13.4
            within the 1 Mb leukocyte receptor complex (LRC). The gene content
            of the KIR gene cluster varies among haplotypes, although several
            'framework' genes are found in all haplotypes (KIR3DL3, KIR3DP1,
            KIR3DL4, KIR3DL2). The KIR proteins are classified by the number of
            extracellular immunoglobulin domains (2D or 3D) and by whether they
            have a long (L) or short (S) cytoplasmic domain. KIR proteins with
            the long cytoplasmic domain transduce inhibitory signals upon
            ligand binding via an immune tyrosine-based inhibitory motif
            (ITIM), while KIR proteins with the short cytoplasmic domain lack
            the ITIM motif and instead associate with the TYRO protein tyrosine
            kinase binding protein to transduce activating signals. The ligands
            for several KIR proteins are subsets of HLA class I molecules;
            thus, KIR proteins are thought to play an important role in
            regulation of the immune response. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L41267.1, U24076.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2163105 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336077.11/ ENSP00000336769.5
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..348
                     /product="killer cell immunoglobulin-like receptor 2DL1
                     precursor"
                     /note="natural killer-associated transcript 1; killer cell
                     immunoglobulin-like receptor 2DL1; KIR2DL1/3DL2; KIR2DL
                     protein; p58 NK cell inhibitory receptor NKR-K6; killer
                     inhibitory receptor 2-2-1; p58 killer cell inhibitory
                     receptor KIR-K64; p58 NK receptor CL-42/47.11; MHC class I
                     NK cell receptor; CD158 antigen-like family member A;
                     p58.1 MHC class-I-specific NK receptor; p58 natural killer
                     cell receptor clones CL-42/47.11; killer cell
                     immunoglobulin-like receptor, two domains, long
                     cytoplasmic tail, 1"
                     /calculated_mol_wt=36328
     sig_peptide     1..21
                     /note="/evidence=ECO:0000269|PubMed:7749980; propagated
                     from UniProtKB/Swiss-Prot (P43626.2)"
                     /calculated_mol_wt=2270
     mat_peptide     22..348
                     /product="Killer cell immunoglobulin-like receptor 2DL1.
                     /id=PRO_0000015078"
                     /note="propagated from UniProtKB/Swiss-Prot (P43626.2)"
                     /calculated_mol_wt=36328
     Region          28..122
                     /region_name="IgC2_D2_LILR_KIR_like"
                     /note="Second immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors, Natural killer inhibitory
                     receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05711"
                     /db_xref="CDD:409376"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409376"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409376"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409376"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409376"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43626.2)"
     Region          77..79
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409376"
     Region          84..88
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409376"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43626.2)"
     Region          96..102
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409376"
     Region          115..122
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409376"
     Region          128..216
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43626.2)"
     Region          145..149
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          157..161
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43626.2)"
     Region          183..187
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          195..200
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          213..216
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          220..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43626.2)"
     Site            246..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43626.2)"
     Region          296..308
                     /region_name="immune tyrosine-based inhibitory motif
                     (ITIM)"
     CDS             1..348
                     /gene="KIR2DL1"
                     /gene_synonym="CD158A; KIR-K64; KIR221; KIR2DL3; NKAT;
                     NKAT-1; NKAT1; p58.1"
                     /coded_by="NM_014218.3:59..1105"
                     /db_xref="CCDS:CCDS12904.1"
                     /db_xref="GeneID:3802"
                     /db_xref="HGNC:HGNC:6329"
                     /db_xref="MIM:604936"
ORIGIN      
        1 msllvvsmac vgffllqgaw phegvhrkps llahpgrlvk seetvilqcw sdvmfehfll
       61 hregmfndtl rligehhdgv skanfsisrm tqdlagtyrc ygsvthspyq vsapsdpldi
      121 viiglyekps lsaqlgptvl agenvtlscs srssydmyhl sregeaherr lpagpkvngt
      181 fqadfplgpa thggtyrcfg sfhdspyews kssdpllvsv tgnpsnswps ptepssktgn
      241 prhlhiligt svviilfill ffllhrwcsn kknaavmdqe sagnrtanse dsdeqdpqev
      301 tytqlnhcvf tqrkitrpsq rpktpptdii vytelpnaes rskvvscp
//
LOCUS       NP_001308138              99 aa            linear   PRI 27-APR-2025
DEFINITION  protein dpy-30 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_001308138 XP_006712182
VERSION     NP_001308138.1
DBSOURCE    REFSEQ: accession NM_001321209.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Su,W.C., Mao,X.M., Li,S.Y., Luo,C.Y., Fan,R., Jiang,H.F.,
            Zhang,L.J., Wang,Y.T., Su,G.Q. and Shen,D.Y.
  TITLE     DPY30 Promotes Proliferation and Cell Cycle Progression of
            Colorectal Cancer Cells via Mediating H3K4 Trimethylation
  JOURNAL   Int J Med Sci 20 (7), 901-917 (2023)
   PUBMED   37324189
  REMARK    GeneRIF: DPY30 Promotes Proliferation and Cell Cycle Progression of
            Colorectal Cancer Cells via Mediating H3K4 Trimethylation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Dixit,D., Prager,B.C., Gimple,R.C., Miller,T.E., Wu,Q.,
            Yomtoubian,S., Kidwell,R.L., Lv,D., Zhao,L., Qiu,Z., Zhang,G.,
            Lee,D., Park,D.E., Wechsler-Reya,R.J., Wang,X., Bao,S. and
            Rich,J.N.
  TITLE     Glioblastoma stem cells reprogram chromatin in vivo to generate
            selective therapeutic dependencies on DPY30 and phosphodiesterases
  JOURNAL   Sci Transl Med 14 (626), eabf3917 (2022)
   PUBMED   34985972
  REMARK    GeneRIF: Glioblastoma stem cells reprogram chromatin in vivo to
            generate selective therapeutic dependencies on DPY30 and
            phosphodiesterases.
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Lee,Y.T., Ayoub,A., Park,S.H., Sha,L., Xu,J., Mao,F., Zheng,W.,
            Zhang,Y., Cho,U.S. and Dou,Y.
  TITLE     Mechanism for DPY30 and ASH2L intrinsically disordered regions to
            modulate the MLL/SET1 activity on chromatin
  JOURNAL   Nat Commun 12 (1), 2953 (2021)
   PUBMED   34012049
  REMARK    GeneRIF: Mechanism for DPY30 and ASH2L intrinsically disordered
            regions to modulate the MLL/SET1 activity on chromatin.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Cho,Y.W., Hong,T., Hong,S., Guo,H., Yu,H., Kim,D., Guszczynski,T.,
            Dressler,G.R., Copeland,T.D., Kalkum,M. and Ge,K.
  TITLE     PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
            methyltransferase complex
  JOURNAL   J Biol Chem 282 (28), 20395-20406 (2007)
   PUBMED   17500065
  REMARK    GeneRIF: hDPY-30 (dpy-30-like protein) binds ASH2L directly. The
            evolutionarily conserved hDPY-30, ASH2L, RBBP5 and WDR5 likely
            constitute a subcomplex that is shared by all human Set1-like HMT
            complexes.
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Tsang,H.T., Connell,J.W., Brown,S.E., Thompson,A., Reid,E. and
            Sanderson,C.M.
  TITLE     A systematic analysis of human CHMP protein interactions:
            additional MIT domain-containing proteins bind to multiple
            components of the human ESCRT III complex
  JOURNAL   Genomics 88 (3), 333-346 (2006)
   PUBMED   16730941
REFERENCE   8  (residues 1 to 99)
  AUTHORS   Dong,X., Peng,Y., Peng,Y., Xu,F., He,X., Wang,F., Peng,X.,
            Qiang,B., Yuan,J. and Rao,Z.
  TITLE     Characterization and crystallization of human DPY-30-like protein,
            an essential component of dosage compensation complex
  JOURNAL   Biochim Biophys Acta 1753 (2), 257-262 (2005)
   PUBMED   16260194
REFERENCE   9  (residues 1 to 99)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   10 (residues 1 to 99)
  AUTHORS   Gubin,A.N., Njoroge,J.M., Bouffard,G.G. and Miller,J.L.
  TITLE     Gene expression in proliferating human erythroid cells
  JOURNAL   Genomics 59 (2), 168-177 (1999)
   PUBMED   10409428
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ276899.1, BC015970.1 and BM505380.1.
            
            On Mar 18, 2016 this sequence version replaced XP_006712182.1.
            
            Summary: This gene encodes an integral core subunit of the SET1/MLL
            family of H3K4 methyltransferases. The encoded protein directly
            controls cell cycle regulators and plays an important role in the
            proliferation and differentiation of human hematopoietic progenitor
            cells. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.186655.1,
                                           SRR5189652.190175.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342166.10/ ENSP00000345837.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.3"
     Protein         1..99
                     /product="protein dpy-30 homolog isoform 1"
                     /note="dpy-30-like protein; protein dpy-30 homolog;
                     dpy-30L"
                     /calculated_mol_wt=11119
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C005.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9C005.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9C005.1)"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9C005.1)"
     Region          53..92
                     /region_name="DD_DPY30_SDC1"
                     /note="dimerization/docking (D/D) domain found in the
                     DPY30/SDC1 family; cd22965"
                     /db_xref="CDD:438534"
     Site            order(53,56..57,60..61,64,69,72,76..77,80..82,84..85,
                     88..89)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:438534"
     Site            order(53..54,58..59,61..62,66,69..70,73..74)
                     /site_type="other"
                     /note="Bre2 binding site [polypeptide binding]"
                     /db_xref="CDD:438534"
     CDS             1..99
                     /gene="DPY30"
                     /gene_synonym="Cps25; HDPY-30; Saf19"
                     /coded_by="NM_001321209.2:110..409"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1777.1"
                     /db_xref="GeneID:84661"
                     /db_xref="HGNC:HGNC:24590"
                     /db_xref="MIM:612032"
ORIGIN      
        1 mepeqmlegq tqvaenphse ygltdnveri venekinaek sskqkvdlqs lptrayldqt
       61 vvpillqgla vlakerppnp ieflasyllk nkaqfedrn
//
LOCUS       NP_001357085             177 aa            linear   PRI 27-APR-2025
DEFINITION  DPY30 domain-containing protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001357085
VERSION     NP_001357085.1
DBSOURCE    REFSEQ: accession NM_001370156.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Li,S., Qiao,Y., Di,Q., Le,X., Zhang,L., Zhang,X., Zhang,C.,
            Cheng,J., Zong,S., Koide,S.S., Miao,S. and Wang,L.
  TITLE     Interaction of SH3P13 and DYDC1 protein: a germ cell component that
            regulates acrosome biogenesis during spermiogenesis
  JOURNAL   Eur J Cell Biol 88 (9), 509-520 (2009)
   PUBMED   19545932
  REMARK    Erratum:[Eur J Cell Biol. 2019 Jan;98(1):51-52. doi:
            10.1016/j.ejcb.2018.11.002. PMID: 30497823]
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Kuhl,A., Melberg,A., Meinl,E., Nurnberg,G., Nurnberg,P.,
            Kehrer-Sawatzki,H. and Jenne,D.E.
  TITLE     Myofibrillar myopathy with arrhythmogenic right ventricular
            cardiomyopathy 7: corroboration and narrowing of the critical
            region on 10q22.3
  JOURNAL   Eur J Hum Genet 16 (3), 367-373 (2008)
   PUBMED   18197198
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359195.24 and DB091778.1.
            
            Summary: This gene encodes a member of a family of proteins that
            contains a DPY30 domain. The encoded protein is involved in
            acrosome formation during spermatid development. This gene locus
            overlaps with a closely related gene on the opposite strand.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 3. Variants 1-4 all encode the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: HY206727.1, CV024331.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1968968,
                                    SAMEA2144333 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..177
                     /product="DPY30 domain-containing protein 1 isoform a"
                     /note="DPY30 domain-containing protein 1"
                     /calculated_mol_wt=20762
     Region          2..43
                     /region_name="DD_DYDC-like"
                     /note="dimerization/docking (D/D) domain found in the
                     DPY30 domain-containing protein (DYDC)-like family;
                     cd22966"
                     /db_xref="CDD:438535"
     CDS             1..177
                     /gene="DYDC1"
                     /gene_synonym="DPY30D1"
                     /coded_by="NM_001370156.1:152..685"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS7366.1"
                     /db_xref="GeneID:143241"
                     /db_xref="HGNC:HGNC:23460"
                     /db_xref="MIM:615154"
ORIGIN      
        1 mesiylqkhl gacltqglae varvrpvdpi eylalwiyky kenvtmeqlr qkemaklere
       61 relalmeqem merlkaeell lqqqqlalql elemqekerq riqelqraqe qlgkemrmnm
      121 enlvrnedil hseeatldsg ktlaeisdry gapnlsrvee ldepmfsdia lnidqdl
//
LOCUS       NP_001354749             344 aa            linear   PRI 27-APR-2025
DEFINITION  aldo-keto reductase family 1 member B15 isoform a [Homo sapiens].
ACCESSION   NP_001354749
VERSION     NP_001354749.1
DBSOURCE    REFSEQ: accession NM_001367820.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Gimenez-Dejoz,J., Kolar,M.H., Ruiz,F.X., Crespo,I.,
            Cousido-Siah,A., Podjarny,A., Barski,O.A., Fanfrlik,J., Pares,X.,
            Farres,J. and Porte,S.
  TITLE     Substrate Specificity, Inhibitor Selectivity and Structure-Function
            Relationships of Aldo-Keto Reductase 1B15: A Novel Human
            Retinaldehyde Reductase
  JOURNAL   PLoS One 10 (7), e0134506 (2015)
   PUBMED   26222439
  REMARK    GeneRIF: Amino acid substitutions clustered in loops A and C result
            in a smaller more hydrophobic and more rigid active site in AKR1B15
            compared with the AKR1B10 pocket, consistent with distinct
            substrate specificity and narrower inhibitor selectivity for
            AKR1B15.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Weber,S., Salabei,J.K., Moller,G., Kremmer,E., Bhatnagar,A.,
            Adamski,J. and Barski,O.A.
  TITLE     Aldo-keto Reductase 1B15 (AKR1B15): a mitochondrial human aldo-keto
            reductase with activity toward steroids and 3-keto-acyl-CoA
            conjugates
  JOURNAL   J Biol Chem 290 (10), 6531-6545 (2015)
   PUBMED   25577493
  REMARK    GeneRIF: AKR1B15.2 localizes to the cytosol and displays no
            enzymatic activity with the substrates tested.
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Jagoe,W.N., Howe,K., O'Brien,S.C. and Carroll,J.
  TITLE     Identification of a role for a mouse sperm surface aldo-keto
            reductase (AKR1B7) and its human analogue in the detoxification of
            the reactive aldehyde, acrolein
  JOURNAL   Andrologia 45 (5), 326-331 (2013)
   PUBMED   22970857
  REMARK    GeneRIF: human sperm possess an aldo-keto reductase on their
            membrane surface and are thus enzymatically protected against
            reactive aldehyde species both in the male and female reproductive
            tract
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Calvo,S.E., Compton,A.G., Hershman,S.G., Lim,S.C., Lieber,D.S.,
            Tucker,E.J., Laskowski,A., Garone,C., Liu,S., Jaffe,D.B.,
            Christodoulou,J., Fletcher,J.M., Bruno,D.L., Goldblatt,J.,
            Dimauro,S., Thorburn,D.R. and Mootha,V.K.
  TITLE     Molecular diagnosis of infantile mitochondrial disease with
            targeted next-generation sequencing
  JOURNAL   Sci Transl Med 4 (118), 118ra10 (2012)
   PUBMED   22277967
  REMARK    GeneRIF: Strong candidate gene for mitochondrial disease, based on
            recessive mutations detected in infantile patients
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Salabei,J.K., Li,X.P., Petrash,J.M., Bhatnagar,A. and Barski,O.A.
  TITLE     Functional expression of novel human and murine AKR1B genes
  JOURNAL   Chem Biol Interact 191 (1-3), 177-184 (2011)
   PUBMED   21276782
  REMARK    GeneRIF: AKR1B15 and Akr1b16 genes are expressed as functional
            proteins in human and murine tissues
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC078847.2.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279832.1334.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465410 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..344
                     /product="aldo-keto reductase family 1 member B15 isoform
                     a"
                     /EC_number="1.1.1.64"
                     /EC_number="1.1.1.300"
                     /EC_number="1.1.1.216"
                     /EC_number="1.1.1.54"
                     /note="putative aldo-keto reductase family 1 member B15;
                     estradiol 17-beta-dehydrogenase AKR1B15; farnesol
                     dehydrogenase; testosterone 17beta-dehydrogenase"
                     /calculated_mol_wt=39329
     Region          51..344
                     /region_name="AKR_AKR1B1-19"
                     /note="AKR1B family of aldo-keto reductase (AKR); cd19107"
                     /db_xref="CDD:381333"
     Site            order(72,76..77,106,108,139..140,142,144,151,188..189,212,
                     238..245,248,257,274,289..294,297,300..301,327..329,332,
                     338..339)
                     /site_type="active"
                     /db_xref="CDD:381333"
     Site            order(72,77,106,139)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381333"
     CDS             1..344
                     /gene="AKR1B15"
                     /gene_synonym="AK1R1B7; AKR1B10L; AKR1R1B7"
                     /coded_by="NM_001367820.1:163..1197"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47715.2"
                     /db_xref="GeneID:441282"
                     /db_xref="HGNC:HGNC:37281"
                     /db_xref="MIM:616336"
ORIGIN      
        1 mvlqmepqvn stnnfhqgpl dqpvgpltgl kssllkdtts agpllrpypa sllgkvkeav
       61 kvaidaeyrh idcayfyenq hevgeaiqek iqekavmred lfivskvwpt fferplvrka
      121 fektlkdlkl syldvylihw pqgfktgddf fpkddkgnmi sgkgtfldaw eameelvdeg
      181 lvkalgvsnf nhfqierlln kpglkykpvt nqvechpylt qekliqychs kgitvtaysp
      241 lgspdrpwak pedpslledp kikeiaakhk kttaqvlirf hiqrnvtvip ksmtpahive
      301 niqvfdfkls deematilsf nrnwrafdfk efshledfpf daey
//
LOCUS       NP_001352753             848 aa            linear   PRI 27-APR-2025
DEFINITION  type II inositol 1,4,5-trisphosphate 5-phosphatase isoform 6 [Homo
            sapiens].
ACCESSION   NP_001352753 XP_006710684
VERSION     NP_001352753.1
DBSOURCE    REFSEQ: accession NM_001365824.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Droubi,A., Wallis,C., Anderson,K.E., Rahman,S., de Sa,A.,
            Rahman,T., Stephens,L.R., Hawkins,P.T. and Lowe,M.
  TITLE     The inositol 5-phosphatase INPP5B regulates B cell receptor
            clustering and signaling
  JOURNAL   J Cell Biol 221 (9) (2022)
   PUBMED   35878408
  REMARK    GeneRIF: The inositol 5-phosphatase INPP5B regulates B cell
            receptor clustering and signaling.
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Nakatsu,F., Messa,M., Nandez,R., Czapla,H., Zou,Y.,
            Strittmatter,S.M. and De Camilli,P.
  TITLE     Sac2/INPP5F is an inositol 4-phosphatase that functions in the
            endocytic pathway
  JOURNAL   J Cell Biol 209 (1), 85-95 (2015)
   PUBMED   25869668
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Montjean,R., Aoidi,R., Desbois,P., Rucci,J., Trichet,M.,
            Salomon,R., Rendu,J., Faure,J., Lunardi,J., Gacon,G., Billuart,P.
            and Dorseuil,O.
  TITLE     OCRL-mutated fibroblasts from patients with Dent-2 disease exhibit
            INPP5B-independent phenotypic variability relatively to Lowe
            syndrome cells
  JOURNAL   Hum Mol Genet 24 (4), 994-1006 (2015)
   PUBMED   25305077
  REMARK    GeneRIF: OCRL-mutated fibroblasts from patients with Dent-2 disease
            exhibit INPP5B-independent phenotypic variability relatively to
            Lowe syndrome cells
REFERENCE   4  (residues 1 to 848)
  AUTHORS   Pirruccello,M., Nandez,R., Idevall-Hagren,O., Alcazar-Roman,A.,
            Abriola,L., Berwick,S.A., Lucast,L., Morel,D. and De Camilli,P.
  TITLE     Identification of inhibitors of inositol 5-phosphatases through
            multiple screening strategies
  JOURNAL   ACS Chem Biol 9 (6), 1359-1368 (2014)
   PUBMED   24742366
REFERENCE   5  (residues 1 to 848)
  AUTHORS   Tresaugues,L., Silvander,C., Flodin,S., Welin,M., Nyman,T.,
            Graslund,S., Hammarstrom,M., Berglund,H. and Nordlund,P.
  TITLE     Structural basis for phosphoinositide substrate recognition,
            catalysis, and membrane interactions in human inositol
            polyphosphate 5-phosphatases
  JOURNAL   Structure 22 (5), 744-755 (2014)
   PUBMED   24704254
  REMARK    GeneRIF: The crystal structures of human INPP5B in complex with
            phosphoinositide substrate analogs revealed a membrane interaction
            patch likely to assist in sequestering substrates from the lipid
            bilayer.
REFERENCE   6  (residues 1 to 848)
  AUTHORS   Speed,C.J., Matzaris,M., Bird,P.I. and Mitchell,C.A.
  TITLE     Tissue distribution and intracellular localisation of the 75-kDa
            inositol polyphosphate 5-phosphatase
  JOURNAL   Eur J Biochem 234 (1), 216-224 (1995)
   PUBMED   8529643
REFERENCE   7  (residues 1 to 848)
  AUTHORS   Jefferson,A.B. and Majerus,P.W.
  TITLE     Properties of type II inositol polyphosphate 5-phosphatase
  JOURNAL   J Biol Chem 270 (16), 9370-9377 (1995)
   PUBMED   7721860
REFERENCE   8  (residues 1 to 848)
  AUTHORS   Janne,P.A., Dutra,A.S., Dracopoli,N.C., Charnas,L.R., Puck,J.M. and
            Nussbaum,R.L.
  TITLE     Localization of the 75-kDa inositol polyphosphate-5-phosphatase
            (INPP5B) to human chromosome band 1p34
  JOURNAL   Cytogenet Cell Genet 66 (3), 164-166 (1994)
   PUBMED   8125013
REFERENCE   9  (residues 1 to 848)
  AUTHORS   Ross,T.S., Jefferson,A.B., Mitchell,C.A. and Majerus,P.W.
  TITLE     Cloning and expression of human 75-kDa inositol
            polyphosphate-5-phosphatase
  JOURNAL   J Biol Chem 266 (30), 20283-20289 (1991)
   PUBMED   1718960
REFERENCE   10 (residues 1 to 848)
  AUTHORS   Mitchell,C.A., Connolly,T.M. and Majerus,P.W.
  TITLE     Identification and isolation of a 75-kDa inositol
            polyphosphate-5-phosphatase from human platelets
  JOURNAL   J Biol Chem 264 (15), 8873-8877 (1989)
   PUBMED   2542294
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL603790.41 and AL929472.21.
            
            On Sep 13, 2018 this sequence version replaced XP_006710684.2.
            
            Summary: This gene encodes a member of a family of inositol
            polyphosphate-5-phosphatases. These enzymes function in the
            regulation of calcium signaling by inactivating inositol
            phosphates. The encoded protein is localized to the cytosol and
            mitochondria, and associates with membranes through an isoprenyl
            modification near the C-terminus. Alternatively spliced transcript
            variants of this gene have been described. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (9), as well as variant 8, encodes
            isoform 6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..848
                     /product="type II inositol 1,4,5-trisphosphate
                     5-phosphatase isoform 6"
                     /EC_number="3.1.3.36"
                     /note="phosphoinositide 5-phosphatase; type II inositol
                     1,4,5-trisphosphate 5-phosphatase; inositol
                     polyphosphate-5-phosphatase, 75kDa"
                     /calculated_mol_wt=96534
     Region          <29..81
                     /region_name="INPP5B_PH"
                     /note="Type II inositol 1,4,5-trisphosphate 5-phosphatase
                     PH domain; pfam16776"
                     /db_xref="CDD:465268"
     Region          200..493
                     /region_name="INPP5c_INPP5B"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of Type II inositol polyphosphate
                     5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and
                     related proteins; cd09093"
                     /db_xref="CDD:197327"
     Site            order(208,210,238,241,243,246,308,314..315,335,338..339,
                     382,384,386,437..438,451,453,459,483..484)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197327"
     Site            order(208,238,335,382,384,459,483..484)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197327"
     Site            order(210,238,483)
                     /site_type="other"
                     /note="Mg binding site [ion binding]"
                     /db_xref="CDD:197327"
     Site            order(238,241,243,246,308,314..315,335,338..339,386,
                     437..438,451,453,483)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197327"
     Site            order(335,384,484)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197327"
     Region          627..847
                     /region_name="RhoGAP_OCRL1"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain present in OCRL1-like proteins.
                     OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins
                     contain two conserved domains: a central inositol
                     polyphosphate 5-phosphatase domain and...; cd04380"
                     /db_xref="CDD:239845"
     Site            order(707,742,746,809,812..813,838)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239845"
     Site            707
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239845"
     CDS             1..848
                     /gene="INPP5B"
                     /gene_synonym="5PTase"
                     /coded_by="NM_001365824.1:472..3018"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="GeneID:3633"
                     /db_xref="HGNC:HGNC:6077"
                     /db_xref="MIM:147264"
ORIGIN      
        1 mshrtgpksg fshssmrlsl faspfygqgs dvtvqldtae lslvfqlpfg sqtrmflhev
       61 aracpgfdsa trdpeflwls ryrcaelele mptprgcnsa lvtwpgyati ggggsnfdgl
      121 rpngkgvpmd qssrgqdkpe slqprqnksk seitdmvrss titvsdkahi lsmqkfglrd
      181 tivkshllqk eedytyiqnf rffagtynvn gqspkeclrl wlsngiqapd vycvgfqeld
      241 lskeafffhd tpkeeewfka vseglhpdak yakvklirlv gimlllyvkq ehaayiseve
      301 aetvgtgimg rmgnkggvai rfqfhntsic vvnshlaahi eeyerrnqdy kdicsrmqfc
      361 qpdpslpplt isnhdvilwl gdlnyrieel dvekvkklie ekdfqmlyay dqlkiqvaak
      421 tvfegftege ltfqptykyd tgsddwdtse kcrapawcdr ilwkgknitq lsyqshmalk
      481 tsdhkpvssv fdigvrvvnd elyrktleei vrsldkmena nipsvslskr efcfqnvkym
      541 qlkvesftih ngqvpchfef inkpdeesyc kqwlnanpsr gfllpdsdve idlelfvnkm
      601 tatklnsged kiedilvlhl drgkdyflsv sgnylpscfg spihtlcymr epildlplet
      661 iseltlmpvw tgddgsqlds pmeipkelwm mvdylyrnav qqedlfqqpg lrsefehird
      721 cldtgmidnl sasnhsvaea lllfleslpe pvicystyhn clecsgnyta skqvistlpi
      781 fhknvfhylm aflrellkns aknhldenil asifgslllr npaghqkldm tekkkaqefi
      841 hqflcnpl
//
LOCUS       NP_001350961             887 aa            linear   ROD 27-APR-2025
DEFINITION  transportin-2 isoform 2 [Mus musculus].
ACCESSION   NP_001350961 XP_017168136
VERSION     NP_001350961.1
DBSOURCE    REFSEQ: accession NM_001364032.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Han,Y., Xiong,Y., Shi,X., Wu,J., Zhao,Y. and Jiang,J.
  TITLE     Regulation of Gli ciliary localization and Hedgehog signaling by
            the PY-NLS/karyopherin-beta2 nuclear import system
  JOURNAL   PLoS Biol 15 (8), e2002063 (2017)
   PUBMED   28777795
  REMARK    GeneRIF: essential for Hedgehog pathway activation; mediates
            ciliary translocation of Gli proteins
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   4  (residues 1 to 887)
  AUTHORS   Lo,J.C., Jamsai,D., O'Connor,A.E., Borg,C., Clark,B.J.,
            Whisstock,J.C., Field,M.C., Adams,V., Ishikawa,T., Aitken,R.J.,
            Whittle,B., Goodnow,C.C., Ormandy,C.J. and O'Bryan,M.K.
  TITLE     RAB-like 2 has an essential role in male fertility, sperm
            intra-flagellar transport, and tail assembly
  JOURNAL   PLoS Genet 8 (10), e1002969 (2012)
   PUBMED   23055941
REFERENCE   5  (residues 1 to 887)
  AUTHORS   Young,J.C., Major,A.T., Miyamoto,Y., Loveland,K.L. and Jans,D.A.
  TITLE     Distinct effects of importin alpha2 and alpha4 on Oct3/4
            localization and expression in mouse embryonic stem cells
  JOURNAL   FASEB J 25 (11), 3958-3965 (2011)
   PUBMED   21840941
REFERENCE   6  (residues 1 to 887)
  AUTHORS   van der Giessen,K. and Gallouzi,I.E.
  TITLE     Involvement of transportin 2-mediated HuR import in muscle cell
            differentiation
  JOURNAL   Mol Biol Cell 18 (7), 2619-2629 (2007)
   PUBMED   17475777
  REMARK    GeneRIF: Early in muscle differentiation, HuR is localized to the
            nucleus of myoblasts by active Transportin 2 (TRN2)-mediated
            import.
REFERENCE   7  (residues 1 to 887)
  AUTHORS   Bulfone,A., Carotenuto,P., Faedo,A., Aglio,V., Garzia,L.,
            Bello,A.M., Basile,A., Andre,A., Cocchia,M., Guardiola,O.,
            Ballabio,A., Rubenstein,J.L. and Zollo,M.
  TITLE     Telencephalic embryonic subtractive sequences: a unique collection
            of neurodevelopmental genes
  JOURNAL   J Neurosci 25 (33), 7586-7600 (2005)
   PUBMED   16107646
REFERENCE   8  (residues 1 to 887)
  AUTHORS   Cobellis,G., Nicolaus,G., Iovino,M., Romito,A., Marra,E.,
            Barbarisi,M., Sardiello,M., Di Giorgio,F.P., Iovino,N., Zollo,M.,
            Ballabio,A. and Cortese,R.
  TITLE     Tagging genes with cassette-exchange sites
  JOURNAL   Nucleic Acids Res 33 (4), e44 (2005)
   PUBMED   15741177
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 887)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY149255.1, BY233571.1, AK155760.1, BQ771085.1, AK029774.1,
            CB246525.1 and AC163703.4.
            
            On Jun 6, 2018 this sequence version replaced XP_017168136.1.
            
            Transcript Variant: This variant (4), as well as variants 5 and 6,
            encodes isoform 2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR9219382.200468.1,
                                           SRR1660811.146967.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 41.51 cM"
     Protein         1..887
                     /product="transportin-2 isoform 2"
                     /note="karyopherin (importin) beta 2b; transportin-2;
                     karyopherin beta-2b"
                     /calculated_mol_wt=100326
     Region          9..36
                     /region_name="HEAT 1.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          22..756
                     /region_name="KAP95"
                     /note="Karyopherin (importin) beta [Intracellular
                     trafficking and secretion]; COG5215"
                     /db_xref="CDD:227540"
     Region          41..79
                     /region_name="HEAT 2.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          88..121
                     /region_name="HEAT 3.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          93..114
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(106..107,110,113..114,144..145,148,151..152,155,
                     190..191,194,197..198,201,231..232,235,238..239,272..273,
                     276,279..280)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          127..164
                     /region_name="HEAT 4.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          127..155
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          165..202
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          171..201
                     /region_name="HEAT 5.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          213..239
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          214..241
                     /region_name="HEAT 6.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          252..281
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          253..280
                     /region_name="HEAT 7.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          296..386
                     /region_name="HEAT 8.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          344..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          394..422
                     /region_name="HEAT 9.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Site            order(412..413,416,419..420,453..454,457,460..461,464,
                     495..496,499,502..503,506,536..537,540,543..544,579..580,
                     585,588..589)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          434..461
                     /region_name="HEAT 10.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          436..464
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          475..508
                     /region_name="HEAT 11.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          477..507
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          516..549
                     /region_name="HEAT 12.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          518..544
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          557..595
                     /region_name="HEAT 13.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          559..590
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          603..654
                     /region_name="HEAT 14.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          659..693
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          665..696
                     /region_name="HEAT 15.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          704..737
                     /region_name="HEAT 16.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          705..735
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          745..780
                     /region_name="HEAT 17.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          746..774
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          788..821
                     /region_name="HEAT 18.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          830..861
                     /region_name="HEAT 19.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     Site            852
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O14787; propagated from
                     UniProtKB/Swiss-Prot (Q99LG2.1)"
     Region          864..884
                     /region_name="HEAT 20.
                     /evidence=ECO:0000250|UniProtKB:Q92973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99LG2.1)"
     CDS             1..887
                     /gene="Tnpo2"
                     /gene_synonym="1110034O24Rik; IPO3; Knpb2b; Kpnb2b; TRN2"
                     /coded_by="NM_001364032.1:142..2805"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS90431.1"
                     /db_xref="GeneID:212999"
                     /db_xref="MGI:MGI:2384849"
ORIGIN      
        1 mdwqpdeqgl qqvlqllkds qspntatqri vqdklkqlnq fpdfnnylif vltrlksede
       61 ptrslsglil knnvkahyqs fpppvadfik qeclnnigda ssliratigi littiaskge
      121 lqmwpellpq lcnllnsedy ntcegafgal qkicedssel ldsdalnrpl nimipkflqf
      181 fkhcspkirs haiacvnqfi mdraqalmdn idtfiehlfa lavdddpevr knvcralvml
      241 levridrlip hmhsiiqyml qrtqdhdenv aleacefwlt laeqpickev lashlvqlip
      301 ilvngmkyse idiillkgdv eedeavpdse qdikprfhks rtvtltheae rpdssedaed
      361 dddddalsdw nlrkcsaaal dvlanvfree llphllpllk gllfhpewvv kesgilvlga
      421 iaegcmqgmv pylpeliphl iqclsdkkal vrsiacwtls ryahwvvsqp pdmhlkplmt
      481 ellkrildgn krvqeaacsa fatleeeact elvpylsyil dtlvfafgky qhknllilyd
      541 aigtladsvg hhlnqpeyiq klmppliqkw nelkdedkdl fplleclssv atalqsgflp
      601 ycepvyqrcv tlvqktlaqa mmytqhpeqy eapdkdfmiv aldllsglae glgghveqlv
      661 arsnimtllf qcmqdsmpev rqssfallgd ltkacfihvk pciaefmpil gtnlnpefis
      721 vcnnatwaig eicmqmgaem qpyvqmvlnn lveiinrpnt pktllentai tigrlgyvcp
      781 qevapmlqqf irpwctslrn irdneekdsa frgicmmigv npggvvqdfi ffcdavaswv
      841 spkddlrdmf ykilhgfkdq vgeenwqqfs eqfppllker laafygv
//
LOCUS       NP_003845                575 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-1 receptor-like 2 isoform a precursor [Homo sapiens].
ACCESSION   NP_003845
VERSION     NP_003845.2
DBSOURCE    REFSEQ: accession NM_003854.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Ahmad,F., Alam,M.A., Ansari,A.W., Jochebeth,A., Leo,R.,
            Al-Abdulla,M.N., Al-Khawaga,S., AlHammadi,A., Al-Malki,A., Al
            Naama,K., Ahmad,A., Buddenkotte,J. and Steinhoff,M.
  TITLE     Emerging Role of the IL-36/IL-36R Axis in Multiple Inflammatory
            Skin Diseases
  JOURNAL   J Invest Dermatol 144 (2), 206-224 (2024)
   PUBMED   38189700
  REMARK    GeneRIF: Emerging Role of the IL-36/IL-36R Axis in Multiple
            Inflammatory Skin Diseases.
            Review article
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Hassi,N.K., Weston,T., Rinaldi,G., Ng,J.C., Smahi,A., Twelves,S.,
            Davan-Wetton,C., Fakhreddine,D., Fraternali,F. and Capon,F.
  TITLE     In Silico and In Vitro Analysis of IL36RN Alterations Reveals
            Critical Residues for the Function of the Interleukin-36 Receptor
            Complex
  JOURNAL   J Invest Dermatol 143 (12), 2468-2475 (2023)
   PUBMED   37414245
  REMARK    GeneRIF: In Silico and In Vitro Analysis of IL36RN Alterations
            Reveals Critical Residues for the Function of the Interleukin-36
            Receptor Complex.
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Baker,K.J., Brint,E. and Houston,A.
  TITLE     Transcriptomic and functional analyses reveal a tumour-promoting
            role for the IL-36 receptor in colon cancer and crosstalk between
            IL-36 signalling and the IL-17/ IL-23 axis
  JOURNAL   Br J Cancer 128 (5), 735-747 (2023)
   PUBMED   36482185
  REMARK    GeneRIF: Transcriptomic and functional analyses reveal a
            tumour-promoting role for the IL-36 receptor in colon cancer and
            crosstalk between IL-36 signalling and the IL-17/ IL-23 axis.
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Sullivan,G.P., Davidovich,P., Munoz-Wolf,N., Ward,R.W., Hernandez
            Santana,Y.E., Clancy,D.M., Gorman,A., Najda,Z., Turk,B.,
            Walsh,P.T., Lavelle,E.C. and Martin,S.J.
  TITLE     Myeloid cell-derived proteases produce a proinflammatory form of
            IL-37 that signals via IL-36 receptor engagement
  JOURNAL   Sci Immunol 7 (78), eade5728 (2022)
   PUBMED   36525507
  REMARK    GeneRIF: Myeloid cell-derived proteases produce a proinflammatory
            form of IL-37 that signals via IL-36 receptor engagement.
REFERENCE   5  (residues 1 to 575)
  AUTHORS   Manzanares-Meza,L.D., Valle-Rios,R. and Medina-Contreras,O.
  TITLE     Interleukin-1 Receptor-Like 2: One Receptor, Three Agonists, and
            Many Implications
  JOURNAL   J Interferon Cytokine Res 42 (2), 49-61 (2022)
   PUBMED   35171706
  REMARK    GeneRIF: Interleukin-1 Receptor-Like 2: One Receptor, Three
            Agonists, and Many Implications.
            Review article
REFERENCE   6  (residues 1 to 575)
  AUTHORS   Ozkara,C., Uzan,M., Tanriverdi,T., Baykara,O., Ekinci,B., Yeni,N.,
            Kafadar,A. and Buyru,N.
  TITLE     Lack of association between IL-1beta/alpha gene polymorphisms and
            temporal lobe epilepsy with hippocampal sclerosis
  JOURNAL   Seizure 15 (5), 288-291 (2006)
   PUBMED   16546408
  REMARK    GeneRIF: IL-1alpha and IL-1beta gene polymorphisms do not act as a
            strong susceptibility factor for MTLE-HS in individuals of Turkish
            ancestry
REFERENCE   7  (residues 1 to 575)
  AUTHORS   Debets,R., Timans,J.C., Homey,B., Zurawski,S., Sana,T.R., Lo,S.,
            Wagner,J., Edwards,G., Clifford,T., Menon,S., Bazan,J.F. and
            Kastelein,R.A.
  TITLE     Two novel IL-1 family members, IL-1 delta and IL-1 epsilon,
            function as an antagonist and agonist of NF-kappa B activation
            through the orphan IL-1 receptor-related protein 2
  JOURNAL   J Immunol 167 (3), 1440-1446 (2001)
   PUBMED   11466363
REFERENCE   8  (residues 1 to 575)
  AUTHORS   Dale,M. and Nicklin,M.J.
  TITLE     Interleukin-1 receptor cluster: gene organization of IL1R2, IL1R1,
            IL1RL2 (IL-1Rrp2), IL1RL1 (T1/ST2), and IL18R1 (IL-1Rrp) on human
            chromosome 2q
  JOURNAL   Genomics 57 (1), 177-179 (1999)
   PUBMED   10191101
REFERENCE   9  (residues 1 to 575)
  AUTHORS   Torigoe,K., Ushio,S., Okura,T., Kobayashi,S., Taniai,M.,
            Kunikata,T., Murakami,T., Sanou,O., Kojima,H., Fujii,M., Ohta,T.,
            Ikeda,M., Ikegami,H. and Kurimoto,M.
  TITLE     Purification and characterization of the human interleukin-18
            receptor
  JOURNAL   J Biol Chem 272 (41), 25737-25742 (1997)
   PUBMED   9325300
REFERENCE   10 (residues 1 to 575)
  AUTHORS   Lovenberg,T.W., Crowe,P.D., Liu,C., Chalmers,D.T., Liu,X.J.,
            Liaw,C., Clevenger,W., Oltersdorf,T., De Souza,E.B. and Maki,R.A.
  TITLE     Cloning of a cDNA encoding a novel interleukin-1 receptor related
            protein (IL 1R-rp2)
  JOURNAL   J Neuroimmunol 70 (2), 113-122 (1996)
   PUBMED   8898719
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF284434.1, BC107064.2 and
            CA448166.1.
            
            On Feb 19, 2003 this sequence version replaced NP_003845.1.
            
            Summary: The protein encoded by this gene is a member of the
            interleukin 1 receptor family. An experiment with transient gene
            expression demonstrated that this receptor was incapable of binding
            to interleukin 1 alpha and interleukin 1 beta with high affinity.
            This gene and four other interleukin 1 receptor family genes,
            including interleukin 1 receptor, type I (IL1R1), interleukin 1
            receptor, type II (IL1R2), interleukin 1 receptor-like 1 (IL1RL1),
            and interleukin 18 receptor 1 (IL18R1), form a cytokine receptor
            gene cluster in a region mapped to chromosome 2q12. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1), as well as variant 2, encodes
            the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF284434.1, U49065.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264257.7/ ENSP00000264257.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.1"
     Protein         1..575
                     /product="interleukin-1 receptor-like 2 isoform a
                     precursor"
                     /EC_number="3.2.2.6"
                     /note="interleukin-1 receptor-related protein 2; IL-1
                     receptor-related protein 2; IL-36 receptor"
                     /calculated_mol_wt=63434
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1988
     mat_peptide     20..575
                     /product="Interleukin-1 receptor-like 2.
                     /id=PRO_0000015445"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB29.2)"
                     /calculated_mol_wt=63434
     Region          24..113
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          38..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HB29.2)"
     Region          53..57
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            59
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HB29.2)"
     Region          78..82
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          92..97
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          105..108
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HB29.2)"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HB29.2)"
     Region          130..218
                     /region_name="Ig2_IL1R-like"
                     /note="Second immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd05757"
                     /db_xref="CDD:409415"
     Site            order(130..132,134..137,143,148,150,179,217)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409415"
     Region          132..137
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409415"
     Region          142..146
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409415"
     Region          158..163
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409415"
     Region          166..168
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409415"
     Region          172..176
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409415"
     Region          178..183
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409415"
     Site            184
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HB29.2)"
     Region          192..201
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409415"
     Region          204..217
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409415"
     Region          227..327
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            234
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HB29.2)"
     Region          245..249
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HB29.2)"
     Region          260..264
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            266
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HB29.2)"
     Region          297..300
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HB29.2)"
     Region          313..318
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          322..325
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            336..356
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB29.2)"
     Region          386..536
                     /region_name="TIR"
                     /note="TIR domain; pfam01582"
                     /db_xref="CDD:396246"
     CDS             1..575
                     /gene="IL1RL2"
                     /gene_synonym="IL-1Rrp2; IL-36R; IL1R-rp2; IL1RRP2"
                     /coded_by="NM_003854.4:77..1804"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2056.1"
                     /db_xref="GeneID:8808"
                     /db_xref="HGNC:HGNC:5999"
                     /db_xref="MIM:604512"
ORIGIN      
        1 mwslllcgls ialplsvtad gckdifmkne ilsasqpfaf nctfppitsg evsvtwykns
       61 skipvskiiq srihqdetwi lflpmewgds gvyqcvikgr dschrihvnl tvfekhwcdt
      121 sigglpnlsd eykqilhlgk ddsltchlhf pkscvlgpik wykdcneikg erftvletrl
      181 lvsnvsaedr gnyacqailt hsgkqyevln gitvsitera gyggsvpkii ypknhsievq
      241 lgttlivdcn vtdtkdntnl rcwrvnntlv ddyydeskri regvethvsf rehnlytvni
      301 tflevkmedy glpfmchagv stayiilqlp apdfraylig glialvavav svvyiynifk
      361 idivlwyrsa fhstetivdg klydayvlyp kphkesqrha vdalvlnilp evlerqcgyk
      421 lfifgrdefp gqavanvide nvklcrrliv ivvpeslgfg llknlseeqi avysaliqdg
      481 mkvilielek iedytvmpes iqyikqkhga irwhgdfteq sqcmktkfwk tvryhmpprr
      541 crpfppvqll qhtpcyrtag pelgsrrkkc tlttg
//
LOCUS       NP_001349701             226 aa            linear   ROD 27-APR-2025
DEFINITION  threonine synthase-like 1 isoform b [Mus musculus].
ACCESSION   NP_001349701 XP_006497497
VERSION     NP_001349701.1
DBSOURCE    REFSEQ: accession NM_001362772.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   VanBuren,V., Piao,Y., Dudekula,D.B., Qian,Y., Carter,M.G.,
            Martin,P.R., Stagg,C.A., Bassey,U.C., Aiba,K., Hamatani,T.,
            Kargul,G.J., Luo,A.G., Kelso,J., Hide,W. and Ko,M.S.
  TITLE     Assembly, verification, and initial annotation of the NIA mouse
            7.4K cDNA clone set
  JOURNAL   Genome Res 12 (12), 1999-2003 (2002)
   PUBMED   12466305
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL929117.7 and BB664224.1.
            
            On Apr 26, 2018 this sequence version replaced XP_006497497.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2, 3, and
            4 all encode the same isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK087148.1, BB664224.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 14.83 cM"
     Protein         1..226
                     /product="threonine synthase-like 1 isoform b"
                     /note="TSH1"
                     /calculated_mol_wt=25576
     Region          <1..212
                     /region_name="Trp-synth-beta_II"
                     /note="Tryptophan synthase beta superfamily (fold type
                     II); this family of pyridoxal phosphate (PLP)-dependent
                     enzymes catalyzes beta-replacement and beta-elimination
                     reactions. This CD corresponds to
                     aminocyclopropane-1-carboxylate deaminase (ACCD),
                     tryptophan...; cl00342"
                     /db_xref="CDD:444852"
     CDS             1..226
                     /gene="Thnsl1"
                     /coded_by="NM_001362772.1:462..1142"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS15721.1"
                     /db_xref="GeneID:208967"
                     /db_xref="MGI:MGI:2139347"
ORIGIN      
        1 mmgipirkfi casnqnhvlt dfiktghydl rnrklaqtfs psidilkssn lerhlylman
       61 kdgqlmanly hqlesqlhfr iekmlveklq qefvadwcse geclaaistt ynasgyildp
      121 htavakvvad kmqdkscpvl iastahyskf apaimqalgi kelnqtsssq lyllssynal
      181 ppphealler mkqkekmdyq vcvadvdvlk shaekliqnw fvrkse
//
LOCUS       NP_005935                269 aa            linear   PRI 27-APR-2025
DEFINITION  OX-2 membrane glycoprotein isoform a precursor [Homo sapiens].
ACCESSION   NP_005935
VERSION     NP_005935.4
DBSOURCE    REFSEQ: accession NM_005944.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wedig,J., Jasani,S., Mukherjee,D., Lathrop,H., Matreja,P., Pfau,T.,
            D'Alesio,L., Guenther,A., Fenn,L., Kaiser,M., Torok,M.A., McGue,J.,
            Sizemore,G.M., Noonan,A.M., Dillhoff,M.E., Blaser,B.W.,
            Frankel,T.L., Culp,S., Hart,P.A., Cruz-Monserrate,Z. and Mace,T.A.
  TITLE     CD200 is overexpressed in the pancreatic tumor microenvironment and
            predictive of overall survival
  JOURNAL   Cancer Immunol Immunother 73 (6), 96 (2024)
   PUBMED   38619621
  REMARK    GeneRIF: CD200 is overexpressed in the pancreatic tumor
            microenvironment and predictive of overall survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Gonzalez-Montes,Y., Osca-Gelis,G., Rodriguez-Romanos,R.,
            Villavicencio,A., Gonzalez-Bartulos,M., Llopis,F., Clapes,V.,
            Oriol,A., Sureda,A., Escoda,L., Sarra,J., Garzo,A., Lloveras,N.,
            Gomez,B., Granada,I. and Gallardo,D.
  TITLE     CD200 genotype is associated with clinical outcome of patients with
            multiple myeloma
  JOURNAL   Front Immunol 15, 1252445 (2024)
   PUBMED   38455039
  REMARK    GeneRIF: CD200 genotype is associated with clinical outcome of
            patients with multiple myeloma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Tang,Y., Liu,W., Kadu,S., Johnson,O., Hasanali,Z.S., Kelly,A.,
            Shestov,A., Pajarillo,R., Greenblatt,E., Holmes,M., Wang,L.P.,
            Shih,N., O'Connor,R.S., Ruella,M., Garfall,A.L., Allman,D.,
            Vogl,D.T., Cohen,A., June,C.H. and Sheppard,N.C.
  TITLE     Exploiting the CD200-CD200R immune checkpoint axis in multiple
            myeloma to enhance CAR T-cell therapy
  JOURNAL   Blood 143 (2), 139-151 (2024)
   PUBMED   37616575
  REMARK    GeneRIF: Exploiting the CD200-CD200R immune checkpoint axis in
            multiple myeloma to enhance CAR T-cell therapy.
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Zhang,M., Qian,X.H., Hu,J., Zhang,Y., Lin,X., Hai,W., Shi,K.,
            Jiang,X., Li,Y., Tang,H.D. and Li,B.
  TITLE     Integrating TSPO PET imaging and transcriptomics to unveil the role
            of neuroinflammation and amyloid-beta deposition in Alzheimer's
            disease
  JOURNAL   Eur J Nucl Med Mol Imaging 51 (2), 455-467 (2024)
   PUBMED   37801139
  REMARK    GeneRIF: Integrating TSPO PET imaging and transcriptomics to unveil
            the role of neuroinflammation and amyloid-beta deposition in
            Alzheimer's disease.
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Moon,S.Y., Han,M., Ryu,G., Shin,S.A., Lee,J.H. and Lee,C.S.
  TITLE     Emerging Immune Checkpoint Molecules on Cancer Cells: CD24 and
            CD200
  JOURNAL   Int J Mol Sci 24 (20), 15072 (2023)
   PUBMED   37894750
  REMARK    GeneRIF: Emerging Immune Checkpoint Molecules on Cancer Cells: CD24
            and CD200.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Chen,Z., Marsden,P.A. and Gorczynski,R.M.
  TITLE     Cloning and characterization of the human CD200 promoter region
  JOURNAL   Mol Immunol 43 (6), 579-587 (2006)
   PUBMED   15955564
  REMARK    GeneRIF: revealed a 169 bp region responsible for constitutive
            expression of CD200; positive regulatory domains were identified in
            the core promoter; and documented evidence for C/EBPbeta as being
            important in transcriptional regulation of CD200
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Preston,S., Wright,G.J., Starr,K., Barclay,A.N. and Brown,M.H.
  TITLE     The leukocyte/neuron cell surface antigen OX2 binds to a ligand on
            macrophages
  JOURNAL   Eur J Immunol 27 (8), 1911-1918 (1997)
   PUBMED   9295026
REFERENCE   8  (residues 1 to 269)
  AUTHORS   Douglas,J., Albertson,D.G., Barclay,A.N., Davis,M. and
            Rabbitts,P.H.
  TITLE     RFLP and mapping of human MOX-1 gene on chromosome 3
  JOURNAL   Nucleic Acids Res 16 (18), 9067 (1988)
   PUBMED   2902568
REFERENCE   9  (residues 1 to 269)
  AUTHORS   McCaughan,G.W., Clark,M.J., Hurst,J., Grosveld,F. and Barclay,A.N.
  TITLE     The gene for MRC OX-2 membrane glycoprotein is localized on human
            chromosome 3
  JOURNAL   Immunogenetics 25 (2), 133-135 (1987)
   PUBMED   3817906
REFERENCE   10 (residues 1 to 269)
  AUTHORS   McCaughan,G.W., Clark,M.J. and Barclay,A.N.
  TITLE     Characterization of the human homolog of the rat MRC OX-2 membrane
            glycoprotein
  JOURNAL   Immunogenetics 25 (5), 329-335 (1987)
   PUBMED   3032785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA544134.1, BC022522.1 and
            AL832529.1.
            
            On Mar 31, 2006 this sequence version replaced NP_005935.3.
            
            Summary: This gene encodes a type I membrane glycoprotein
            containing two extracellular immunoglobulin domains, a
            transmembrane and a cytoplasmic domain. This gene is expressed by
            various cell types, including B cells, a subset of T cells,
            thymocytes, endothelial cells, and neurons. The encoded protein
            plays an important role in immunosuppression and regulation of
            anti-tumor activity. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.139571.1,
                                           SRR3476690.781140.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315711.12/ ENSP00000312766.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.2"
     Protein         1..269
                     /product="OX-2 membrane glycoprotein isoform a precursor"
                     /note="CD200 antigen; antigen identified by monoclonal
                     antibody MRC OX-2; OX-2 membrane glycoprotein"
                     /calculated_mol_wt=26924
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3425
     Region          32..139
                     /region_name="IgV_1_MRC-OX-2_like"
                     /note="First immunoglobulin (Ig) variable (V) domain of
                     rat MRC OX-2 antigen, and similar domains; cd05846"
                     /db_xref="CDD:409433"
     Region          32..52
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409433"
     Region          32..36
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409433"
     Region          38..42
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409433"
     Region          45..53
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409433"
     Region          53..59
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409433"
     Region          60..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409433"
     Region          61..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409433"
     Region          70..87
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409433"
     Region          70..78
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409433"
     Region          83..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409433"
     Region          93..123
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409433"
     Region          93..100
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409433"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P41217.4)"
     Region          103..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409433"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P41217.4)"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P41217.4)"
     Region          117..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409433"
     Region          124..130
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409433"
     Region          130..139
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409433"
     Region          131..139
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409433"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P41217.4)"
     Region          <159..230
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          169..173
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409384"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P41217.4)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P41217.4)"
     Region          197..201
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409384"
     Region          211..216
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409384"
     Region          226..229
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409384"
     Site            233..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P41217.4)"
     CDS             1..269
                     /gene="CD200"
                     /gene_synonym="MOX1; MOX2; MRC; OX-2"
                     /coded_by="NM_005944.7:58..867"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2965.1"
                     /db_xref="GeneID:4345"
                     /db_xref="HGNC:HGNC:7203"
                     /db_xref="MIM:155970"
ORIGIN      
        1 merlvirmpf shlstyslvw vmaavvlcta qvqvvtqder eqlytpaslk cslqnaqeal
       61 ivtwqkkkav spenmvtfse nhgvviqpay kdkinitqlg lqnstitfwn itledegcym
      121 clfntfgfgk isgtacltvy vqpivslhyk fsedhlnitc satarpapmv fwkvprsgie
      181 nstvtlshpn gttsvtsilh ikdpknqvgk evicqvlhlg tvtdfkqtvn kgywfsvpll
      241 lsivslvill vlisillywk rhrnqdrep
//
LOCUS       NP_001356534             177 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-19 precursor [Homo sapiens].
ACCESSION   NP_001356534
VERSION     NP_001356534.1
DBSOURCE    REFSEQ: accession NM_001369605.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Parhoudeh,S., Saadaty,A., Khashei Varnamkhasti,K., Khashei
            Varnamkhasti,S., Naeimi,L. and Naeimi,S.
  TITLE     Highlighting allelic variations at the interleukin-19 locus in term
            of preeclampsia predisposing factors and access to an accurate
            diagnostic/screening option
  JOURNAL   BMC Pregnancy Childbirth 23 (1), 839 (2023)
   PUBMED   38057745
  REMARK    GeneRIF: Highlighting allelic variations at the interleukin-19
            locus in term of preeclampsia predisposing factors and access to an
            accurate diagnostic/screening option.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dumycz,K., Kunkiel,K., Stelmaszczyk-Emmel,A., Jozefczuk,P.,
            Adamiec,A., Kulus,M. and Feleszko,W.
  TITLE     Interleukin-19 is associated with severity and age-related
            phenotype of atopic dermatitis in children
  JOURNAL   Clin Exp Allergy 53 (1), 109-112 (2023)
   PUBMED   36161738
  REMARK    GeneRIF: Interleukin-19 is associated with severity and age-related
            phenotype of atopic dermatitis in children.
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Saheb Sharif-Askari,F., Saheb Sharif-Askari,N., Hafezi,S., Goel,S.,
            Ali Hussain Alsayed,H., Ansari,A.W., Mahboub,B., Al-Muhsen,S.,
            Temsah,M.H., Hamid,Q. and Halwani,R.
  TITLE     Upregulation of interleukin-19 in saliva of patients with COVID-19
  JOURNAL   Sci Rep 12 (1), 16019 (2022)
   PUBMED   36163397
  REMARK    GeneRIF: Upregulation of interleukin-19 in saliva of patients with
            COVID-19.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Mohammed,A.K.
  TITLE     Comparison of TNF-alpha and IL-19 concentrations at different
            stages of breast cancer
  JOURNAL   J Med Life 15 (6), 845-849 (2022)
   PUBMED   35928364
  REMARK    GeneRIF: Comparison of TNF-alpha and IL-19 concentrations at
            different stages of breast cancer.
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Sang,Z., Tan,W., Wu,H., Tian,T. and Li,L.
  TITLE     Association between interleukin-19 gene polymorphisms and maternal
            puerperal infection
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 68 (4), 24-30 (2022)
   PUBMED   35988273
  REMARK    GeneRIF: Association between interleukin-19 gene polymorphisms and
            maternal puerperal infection.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Wolk,K., Kunz,S., Asadullah,K. and Sabat,R.
  TITLE     Cutting edge: immune cells as sources and targets of the IL-10
            family members?
  JOURNAL   J Immunol 168 (11), 5397-5402 (2002)
   PUBMED   12023331
REFERENCE   7  (residues 1 to 177)
  AUTHORS   Fickenscher,H., Hor,S., Kupers,H., Knappe,A., Wittmann,S. and
            Sticht,H.
  TITLE     The interleukin-10 family of cytokines
  JOURNAL   Trends Immunol 23 (2), 89-96 (2002)
   PUBMED   11929132
REFERENCE   8  (residues 1 to 177)
  AUTHORS   Dumoutier,L., Leemans,C., Lejeune,D., Kotenko,S.V. and Renauld,J.C.
  TITLE     Cutting edge: STAT activation by IL-19, IL-20 and mda-7 through
            IL-20 receptor complexes of two types
  JOURNAL   J Immunol 167 (7), 3545-3549 (2001)
   PUBMED   11564763
REFERENCE   9  (residues 1 to 177)
  AUTHORS   Blumberg,H., Conklin,D., Xu,W.F., Grossmann,A., Brender,T.,
            Carollo,S., Eagan,M., Foster,D., Haldeman,B.A., Hammond,A.,
            Haugen,H., Jelinek,L., Kelly,J.D., Madden,K., Maurer,M.F.,
            Parrish-Novak,J., Prunkard,D., Sexson,S., Sprecher,C., Waggie,K.,
            West,J., Whitmore,T.E., Yao,L., Kuechle,M.K., Dale,B.A. and
            Chandrasekher,Y.A.
  TITLE     Interleukin 20: discovery, receptor identification, and role in
            epidermal function
  JOURNAL   Cell 104 (1), 9-19 (2001)
   PUBMED   11163236
REFERENCE   10 (residues 1 to 177)
  AUTHORS   Gallagher,G., Dickensheets,H., Eskdale,J., Izotova,L.S.,
            Mirochnitchenko,O.V., Peat,J.D., Vazquez,N., Pestka,S.,
            Donnelly,R.P. and Kotenko,S.V.
  TITLE     Cloning, expression and initial characterization of interleukin-19
            (IL-19), a novel homologue of human interleukin-10 (IL-10)
  JOURNAL   Genes Immun 1 (7), 442-450 (2000)
   PUBMED   11196675
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF453946.1, AL513315.15,
            AY040367.1 and CA309757.1.
            
            Summary: The protein encoded by this gene is a cytokine that
            belongs to the IL10 cytokine subfamily. This cytokine is found to
            be preferentially expressed in monocytes. It can bind the IL20
            receptor complex and lead to the activation of the signal
            transducer and activator of transcription 3 (STAT3). A similar
            cytokine in mouse is reported to up-regulate the expression of IL6
            and TNF-alpha and induce apoptosis, which suggests a role of this
            cytokine in inflammatory responses. Alternatively spliced
            transcript variants encoding the distinct isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF192498.1, CR985515.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..177
                     /product="interleukin-19 precursor"
                     /note="melanoma differentiation associated protein-like
                     protein"
                     /calculated_mol_wt=17813
     sig_peptide     1..24
                     /note="/evidence=ECO:0000269|PubMed:15340161; propagated
                     from UniProtKB/Swiss-Prot (Q9UHD0.2)"
                     /calculated_mol_wt=2657
     Region          21..167
                     /region_name="IL10"
                     /note="Interleukin 10; cl02501"
                     /db_xref="CDD:413341"
     mat_peptide     25..177
                     /product="Interleukin-19. /id=PRO_0000015379"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHD0.2)"
                     /calculated_mol_wt=17813
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD0.2)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD0.2)"
     CDS             1..177
                     /gene="IL19"
                     /gene_synonym="IL-10C; MDA1; NG.1; ZMDA1"
                     /coded_by="NM_001369605.1:55..588"
                     /db_xref="CCDS:CCDS1469.1"
                     /db_xref="GeneID:29949"
                     /db_xref="HGNC:HGNC:5990"
                     /db_xref="MIM:605687"
ORIGIN      
        1 mklqcvslwl lgtililcsv dnhglrrcli stdmhhiees fqeikraiqa kdtfpnvtil
       61 stletlqiik pldvccvtkn llafyvdrvf kdhqepnpki lrkissians flymqktlrq
      121 cqeqrqchcr qeatnatrvi hdnydqlevh aaaikslgel dvflawinkn hevmfsa
//
LOCUS       NP_001353199              93 aa            linear   PRI 27-APR-2025
DEFINITION  protein archease isoform 13 [Homo sapiens].
ACCESSION   NP_001353199
VERSION     NP_001353199.1
DBSOURCE    REFSEQ: accession NM_001366270.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Mason,C.C., Khorashad,J.S., Tantravahi,S.K., Kelley,T.W.,
            Zabriskie,M.S., Yan,D., Pomicter,A.D., Reynolds,K.R., Eiring,A.M.,
            Kronenberg,Z., Sherman,R.L., Tyner,J.W., Dalley,B.K., Dao,K.H.,
            Yandell,M., Druker,B.J., Gotlib,J., O'Hare,T. and Deininger,M.W.
  TITLE     Age-related mutations and chronic myelomonocytic leukemia
  JOURNAL   Leukemia 30 (4), 906-913 (2016)
   PUBMED   26648538
  REMARK    GeneRIF: ARCH mutation is associated with chronic myelomonocytic
            leukemia.
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Jurkin,J., Henkel,T., Nielsen,A.F., Minnich,M., Popow,J.,
            Kaufmann,T., Heindl,K., Hoffmann,T., Busslinger,M. and Martinez,J.
  TITLE     The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA
            and controls antibody secretion in plasma cells
  JOURNAL   EMBO J 33 (24), 2922-2936 (2014)
   PUBMED   25378478
  REMARK    GeneRIF: RTCB, the catalytic subunit of the tRNA ligase complex,
            and its co-factor archease mediate XBP1 mRNA splicing both in vitro
            and in vivo.
REFERENCE   5  (residues 1 to 93)
  AUTHORS   Popow,J., Jurkin,J., Schleiffer,A. and Martinez,J.
  TITLE     Analysis of orthologous groups reveals archease and DDX1 as tRNA
            splicing factors
  JOURNAL   Nature 511 (7507), 104-107 (2014)
   PUBMED   24870230
  REMARK    GeneRIF: archease (also called ZBTB8OS), a protein of unknown
            function, is required for full activity of the human tRNA ligase
            complex and, in cooperation with DDX1, facilitates the formation of
            an RTCB-guanylate intermediate central to mammalian RNA ligation
REFERENCE   6  (residues 1 to 93)
  AUTHORS   Popow,J., Englert,M., Weitzer,S., Schleiffer,A., Mierzwa,B.,
            Mechtler,K., Trowitzsch,S., Will,C.L., Luhrmann,R., Soll,D. and
            Martinez,J.
  TITLE     HSPC117 is the essential subunit of a human tRNA splicing ligase
            complex
  JOURNAL   Science 331 (6018), 760-764 (2011)
   PUBMED   21311021
REFERENCE   7  (residues 1 to 93)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 93)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2 and AL033529.25.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.112936.1, BG716113.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2153733
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..93
                     /product="protein archease isoform 13"
                     /note="protein archease; archease-like protein; archease
                     (ARCH); zinc finger and BTB domain-containing opposite
                     strand protein 8"
                     /calculated_mol_wt=10565
     Region          <54..93
                     /region_name="Archease"
                     /note="Archease protein family (MTH1598/TM1083); cl00606"
                     /db_xref="CDD:469838"
     CDS             1..93
                     /gene="ZBTB8OS"
                     /gene_synonym="ARCH; ARCH2"
                     /coded_by="NM_001366270.1:368..649"
                     /note="isoform 13 is encoded by transcript variant 23"
                     /db_xref="GeneID:339487"
                     /db_xref="HGNC:HGNC:24094"
                     /db_xref="MIM:615891"
ORIGIN      
        1 mkggsrvsnp avmaqeeedv rdynlteeqk aikakyppvn rkyeyldhta dvqwgeefsl
       61 skhpqgtevk aitysamqvy neenpevfvi idi
//
LOCUS       NP_006523                621 aa            linear   PRI 27-APR-2025
DEFINITION  RNA polymerase II elongation factor ELL [Homo sapiens].
ACCESSION   NP_006523
VERSION     NP_006523.1
DBSOURCE    REFSEQ: accession NM_006532.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Zha,J., Zhong,M., Pan,G., Chen,Q., Jiang,Y., Lai,Q., Tan,J.,
            Zhou,H., Wu,H. and Xu,B.
  TITLE     Stratification and therapeutic potential of ELL in cytogenetic
            normal acute myeloid leukemia
  JOURNAL   Gene 856, 147110 (2023)
   PUBMED   36543308
  REMARK    GeneRIF: Stratification and therapeutic potential of ELL in
            cytogenetic normal acute myeloid leukemia.
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Pal,S., Yadav,D. and Biswas,D.
  TITLE     ATM-mediated ELL phosphorylation enhances its self-association
            through increased EAF1 interaction and inhibits global
            transcription during genotoxic stress
  JOURNAL   Nucleic Acids Res 50 (19), 10995-11012 (2022)
   PUBMED   36305813
  REMARK    GeneRIF: ATM-mediated ELL phosphorylation enhances its
            self-association through increased EAF1 interaction and inhibits
            global transcription during genotoxic stress.
            Erratum:[Nucleic Acids Res. 2023 Jul 7;51(12):6507. doi:
            10.1093/nar/gkad454. PMID: 37194690]
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Li,J., Bansal,V., Tiwari,M., Chen,Y. and Sen,G.L.
  TITLE     ELL Facilitates RNA Polymerase II-Mediated Transcription of Human
            Epidermal Proliferation Genes
  JOURNAL   J Invest Dermatol 141 (5), 1352-1356 (2021)
   PUBMED   33157094
  REMARK    GeneRIF: ELL Facilitates RNA Polymerase II-Mediated Transcription
            of Human Epidermal Proliferation Genes.
REFERENCE   4  (residues 1 to 621)
  AUTHORS   Basu,S., Barad,M., Yadav,D., Nandy,A., Mukherjee,B., Sarkar,J.,
            Chakrabarti,P., Mukhopadhyay,S. and Biswas,D.
  TITLE     DBC1, p300, HDAC3, and Siah1 coordinately regulate ELL stability
            and function for expression of its target genes
  JOURNAL   Proc Natl Acad Sci U S A 117 (12), 6509-6520 (2020)
   PUBMED   32152128
  REMARK    GeneRIF: E1A-associated p300 protein -mediated site-specific
            acetylation increases, whereas histone deacetylase 3-mediated
            deacetylation decreases, transcriptional elongation factor ELL
            stability through polyubiquitylation by the E3 ubiquitin ligase
            Siah1. Knockdown of human cell cycle and apoptosis regulator 2
            reduces ELL levels and expression of a significant number of genes,
            including those involved in glucose metabolism.
REFERENCE   5  (residues 1 to 621)
  AUTHORS   Anwar,D., Takahashi,H., Watanabe,M., Suzuki,M., Fukuda,S. and
            Hatakeyama,S.
  TITLE     p53 represses the transcription of snRNA genes by preventing the
            formation of little elongation complex
  JOURNAL   Biochim Biophys Acta 1859 (8), 975-982 (2016)
   PUBMED   27268141
  REMARK    GeneRIF: The results indicate that p53 interferes with the
            interaction between ELL/EAF and ICE1 and represses transcription of
            small nuclear RNA genes by Pol II.
REFERENCE   6  (residues 1 to 621)
  AUTHORS   Shilatifard,A.
  TITLE     Identification and purification of the Holo-ELL complex. Evidence
            for the presence of ELL-associated proteins that suppress the
            transcriptional inhibitory activity of ELL
  JOURNAL   J Biol Chem 273 (18), 11212-11217 (1998)
   PUBMED   9556611
REFERENCE   7  (residues 1 to 621)
  AUTHORS   Shilatifard,A., Haque,D., Conaway,R.C. and Conaway,J.W.
  TITLE     Structure and function of RNA polymerase II elongation factor ELL.
            Identification of two overlapping ELL functional domains that
            govern its interaction with polymerase and the ternary elongation
            complex
  JOURNAL   J Biol Chem 272 (35), 22355-22363 (1997)
   PUBMED   9268387
REFERENCE   8  (residues 1 to 621)
  AUTHORS   Shilatifard,A., Lane,W.S., Jackson,K.W., Conaway,R.C. and
            Conaway,J.W.
  TITLE     An RNA polymerase II elongation factor encoded by the human ELL
            gene
  JOURNAL   Science 271 (5257), 1873-1876 (1996)
   PUBMED   8596958
REFERENCE   9  (residues 1 to 621)
  AUTHORS   Thirman,M.J., Levitan,D.A., Kobayashi,H., Simon,M.C. and
            Rowley,J.D.
  TITLE     Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1)
            in acute myeloid leukemia
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12110-12114 (1994)
   PUBMED   7991593
REFERENCE   10 (residues 1 to 621)
  AUTHORS   Iwabuchi,K., Bartel,P.L., Li,B., Marraccino,R. and Fields,S.
  TITLE     Two cellular proteins that bind to wild-type but not mutant p53
  JOURNAL   Proc Natl Acad Sci U S A 91 (13), 6098-6102 (1994)
   PUBMED   8016121
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI458899.1, U16282.1 and BC033673.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.64888.1,
                                           SRR1803617.73868.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262809.9/ ENSP00000262809.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..621
                     /product="RNA polymerase II elongation factor ELL"
                     /note="ELL gene (11-19 lysine-rich leukemia gene);
                     eleven-nineteen lysine-rich leukemia protein; protein
                     phosphatase 1, regulatory subunit 68; elongation factor
                     RNA polymerase II; KMT2A/ELL fusion protein; ELL/KMT2A
                     fusion protein"
                     /calculated_mol_wt=68134
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P55199.1)"
     Region          6..292
                     /region_name="ELL"
                     /note="RNA polymerase II elongation factor ELL; pfam10390"
                     /db_xref="CDD:463068"
     Site            46
                     /site_type="other"
                     /note="KMT2A/MLL1 fusion point (in acute myeloid leukemia
                     patient). /evidence=ECO:0000269|PubMed:7991593; propagated
                     from UniProtKB/Swiss-Prot (P55199.1)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55199.1)"
     Region          296..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55199.1)"
     Region          <304..485
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P55199.1)"
     Region          431..504
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55199.1)"
     Region          445..459
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P55199.1)"
     Region          513..614
                     /region_name="Occludin_ELL"
                     /note="Occludin homology domain; pfam07303"
                     /db_xref="CDD:462140"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (P55199.1)"
     CDS             1..621
                     /gene="ELL"
                     /gene_synonym="C19orf17; ELL1; MEN; PPP1R68"
                     /coded_by="NM_006532.4:16..1881"
                     /db_xref="CCDS:CCDS12380.1"
                     /db_xref="GeneID:8178"
                     /db_xref="HGNC:HGNC:23114"
                     /db_xref="MIM:600284"
ORIGIN      
        1 maalkedrsy glscgrvsdg skvsvfhvkl tdsalrafes yrarqdsvsl rpsirfqgsq
       61 ghisipqpdc paeartfsfy lsnigrdnpq gsfdciqqyv sshgevhldc lgsiqdkitv
      121 catddsyqka rqsmaqaeee trsrsaivik aggrylgkkv qfrkpapgat davpsrkrat
      181 pinlasairk sgasavsggs gvsqrpfrdr vlhllalrpy rkaelllrlq kdgltqadkd
      241 aldgllqqva nmsakdgtct lqdcmykdvq kdwpgysegd qqllkrvlvr klcqpqstgs
      301 llgdpaassp pgergrsasp pqkrlqppdf idplankkpr ishftqraqp avngklgvpn
      361 greallptpg ppastdtlss sthlpprlep prahdpladv sndlghsgrd cehgeaaapa
      421 ptvrlglpll tdcaqpsrph gspsrskpkk kskkhkdker aaedkpraql pdcapathat
      481 pgapadtpgl ngtcsvssvp tstsetpdyl lkyaaissse qrqsykndfn aeyseyrdlh
      541 arieritrrf tqldaqlrql sqgseeyett rgqilqeyrk ikktntnysq ekhrceylhs
      601 klahikrlia eydqrqlqaw p
//
LOCUS       NP_001041695             326 aa            linear   PRI 27-APR-2025
DEFINITION  adenosine receptor A1 isoform 1 [Homo sapiens].
ACCESSION   NP_001041695
VERSION     NP_001041695.1
DBSOURCE    REFSEQ: accession NM_001048230.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Zhu,W., Hong,Y., Tong,Z., He,X., Li,Y., Wang,H., Gao,X., Song,P.,
            Zhang,X., Wu,X., Tan,Z., Huang,W., Liu,Z., Bao,Y., Ma,J., Zheng,N.,
            Xie,C., Ke,X., Zhou,W., Jia,W., Li,M., Zhong,J., Sheng,L. and Li,H.
  TITLE     Activation of hepatic adenosine A1 receptor ameliorates MASH via
            inhibiting SREBPs maturation
  JOURNAL   Cell Rep Med 5 (3), 101477 (2024)
   PUBMED   38508143
  REMARK    GeneRIF: Activation of hepatic adenosine A1 receptor ameliorates
            MASH via inhibiting SREBPs maturation.
            Erratum:[Cell Rep Med. 2024 May 21;5(5):101563. doi:
            10.1016/j.xcrm.2024.101563. PMID: 38718795]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Tzortzini,E., Corey,R.A. and Kolocouris,A.
  TITLE     Comparative Study of Receptor-, Receptor State-, and
            Membrane-Dependent Cholesterol Binding Sites in A2A and A1
            Adenosine Receptors Using Coarse-Grained Molecular Dynamics
            Simulations
  JOURNAL   J Chem Inf Model 63 (3), 928-949 (2023)
   PUBMED   36637988
  REMARK    GeneRIF: Comparative Study of Receptor-, Receptor State-, and
            Membrane-Dependent Cholesterol Binding Sites in A2A and A1
            Adenosine Receptors Using Coarse-Grained Molecular Dynamics
            Simulations.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Sarasola,L.I., Del Torrent,C.L., Perez-Arevalo,A., Argerich,J.,
            Casajuana-Martin,N., Chevigne,A., Fernandez-Duenas,V., Ferre,S.,
            Pardo,L. and Ciruela,F.
  TITLE     The ADORA1 mutation linked to early-onset Parkinson's disease
            alters adenosine A1-A2A receptor heteromer formation and function
  JOURNAL   Biomed Pharmacother 156, 113896 (2022)
   PUBMED   36279718
  REMARK    GeneRIF: The ADORA1 mutation linked to early-onset Parkinson's
            disease alters adenosine A1-A2A receptor heteromer formation and
            function.
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Deluigi,M., Morstein,L., Schuster,M., Klenk,C., Merklinger,L.,
            Cridge,R.R., de Zhang,L.A., Klipp,A., Vacca,S., Vaid,T.M.,
            Mittl,P.R.E., Egloff,P., Eberle,S.A., Zerbe,O., Chalmers,D.K.,
            Scott,D.J. and Pluckthun,A.
  TITLE     Crystal structure of the alpha1B-adrenergic receptor reveals
            molecular determinants of selective ligand recognition
  JOURNAL   Nat Commun 13 (1), 382 (2022)
   PUBMED   35046410
  REMARK    GeneRIF: Crystal structure of the alpha1B-adrenergic receptor
            reveals molecular determinants of selective ligand recognition.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Tian,D., Li,J., Zou,L., Lin,M., Shi,X., Hu,Y., Lang,J., Xu,L.,
            Ye,W., Li,X. and Chen,L.
  TITLE     Adenosine A1 Receptor Deficiency Aggravates Extracellular Matrix
            Accumulation in Diabetic Nephropathy through Disturbance of
            Peritubular Microenvironment
  JOURNAL   J Diabetes Res 2021, 5584871 (2021)
   PUBMED   34671682
  REMARK    GeneRIF: Adenosine A1 Receptor Deficiency Aggravates Extracellular
            Matrix Accumulation in Diabetic Nephropathy through Disturbance of
            Peritubular Microenvironment.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Townsend-Nicholson,A. and Shine,J.
  TITLE     Molecular cloning and characterisation of a human brain A1
            adenosine receptor cDNA
  JOURNAL   Brain Res Mol Brain Res 16 (3-4), 365-370 (1992)
   PUBMED   1339301
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Libert,F., Van Sande,J., Lefort,A., Czernilofsky,A., Dumont,J.E.,
            Vassart,G., Ensinger,H.A. and Mendla,K.D.
  TITLE     Cloning and functional characterization of a human A1 adenosine
            receptor
  JOURNAL   Biochem Biophys Res Commun 187 (2), 919-926 (1992)
   PUBMED   1530647
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Stiles,G.L.
  TITLE     Adenosine receptors
  JOURNAL   J Biol Chem 267 (10), 6451-6454 (1992)
   PUBMED   1551861
  REMARK    Review article
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Libert,F., Passage,E., Parmentier,M., Simons,M.J., Vassart,G. and
            Mattei,M.G.
  TITLE     Chromosomal mapping of A1 and A2 adenosine receptors, VIP receptor,
            and a new subtype of serotonin receptor
  JOURNAL   Genomics 11 (1), 225-227 (1991)
   PUBMED   1662665
  REMARK    Erratum:[Genomics 1994 Sep 1;23(1):305]
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Libert,F., Parmentier,M., Lefort,A., Dinsart,C., Van Sande,J.,
            Maenhaut,C., Simons,M.J., Dumont,J.E. and Vassart,G.
  TITLE     Selective amplification and cloning of four new members of the G
            protein-coupled receptor family
  JOURNAL   Science 244 (4904), 569-572 (1989)
   PUBMED   2541503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA343445.1, AK127752.1,
            AC105940.2 and BU740906.1.
            
            Summary: The protein encoded by this gene is an adenosine receptor
            that belongs to the G-protein coupled receptor 1 family. There are
            3 types of adenosine receptors, each with a specific pattern of
            ligand binding and tissue distribution, and together they regulate
            a diverse set of physiologic functions. The type A1 receptors
            inhibit adenylyl cyclase, and play a role in the fertilization
            process. Animal studies also suggest a role for A1 receptors in
            kidney function and ethanol intoxication. Transcript variants with
            alternative splicing in the 5' UTR have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127752.1, BC026340.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..326
                     /product="adenosine receptor A1 isoform 1"
                     /calculated_mol_wt=36381
     Region          10..299
                     /region_name="7tmA_Adenosine_R_A1"
                     /note="adenosine receptor subtype A1, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15071"
                     /db_xref="CDD:341323"
     Region          10..37
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341323"
     Site            11..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30542.1)"
     Site            order(12,16,66,70,87..88,91,171..172,177,180,247,250..251,
                     254,270..271,274)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:341323"
     Region          44..71
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341323"
     Site            47..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30542.1)"
     Region          80..110
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341323"
     Site            81..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30542.1)"
     Site            124..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30542.1)"
     Region          124..142
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341323"
     Site            159
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30542.1)"
     Region          177..207
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341323"
     Site            177..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30542.1)"
     Region          227..257
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341323"
     Site            236..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30542.1)"
     Region          267..292
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341323"
     Site            268..292
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30542.1)"
     CDS             1..326
                     /gene="ADORA1"
                     /gene_synonym="RDC7"
                     /coded_by="NM_001048230.2:261..1241"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1434.1"
                     /db_xref="GeneID:134"
                     /db_xref="HGNC:HGNC:262"
                     /db_xref="MIM:102775"
ORIGIN      
        1 mppsisafqa ayigievlia lvsvpgnvlv iwavkvnqal rdatfcfivs lavadvavga
       61 lviplailin igpqtyfhtc lmvacpvlil tqssilalla iavdrylrvk iplrykmvvt
      121 prraavaiag cwilsfvvgl tpmfgwnnls averawaang smgepvikce fekvismeym
      181 vyfnffvwvl pplllmvliy levfylirkq lnkkvsassg dpqkyygkel kiakslalil
      241 flfalswlpl hilncitlfc pschkpsilt yiaiflthgn samnpivyaf riqkfrvtfl
      301 kiwndhfrcq pappidedlp eerpdd
//
LOCUS       NP_981951                279 aa            linear   PRI 27-APR-2025
DEFINITION  acyl-coenzyme A thioesterase MBLAC2 [Homo sapiens].
ACCESSION   NP_981951 XP_087657
VERSION     NP_981951.2
DBSOURCE    REFSEQ: accession NM_203406.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Malgapo,M.I.P., Safadi,J.M. and Linder,M.E.
  TITLE     Metallo-beta-lactamase domain-containing protein 2 is
            S-palmitoylated and exhibits acyl-CoA hydrolase activity
  JOURNAL   J Biol Chem 296, 100106 (2021)
   PUBMED   33219126
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Diene,S.M., Pinault,L., Keshri,V., Armstrong,N., Khelaifia,S.,
            Chabriere,E., Caetano-Anolles,G., Colson,P., La Scola,B.,
            Rolain,J.M., Pontarotti,P. and Raoult,D.
  TITLE     Human metallo-beta-lactamase enzymes degrade penicillin
  JOURNAL   Sci Rep 9 (1), 12173 (2019)
   PUBMED   31434986
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093510.2.
            
            On Nov 23, 2018 this sequence version replaced NP_981951.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.246008.1,
                                           SRR1660807.71450.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316610.7/ ENSP00000314776.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.3"
     Protein         1..279
                     /product="acyl-coenzyme A thioesterase MBLAC2"
                     /EC_number="3.1.2.2"
                     /EC_number="3.5.2.6"
                     /note="metallo-beta-lactamase domain-containing protein 2;
                     beta-lactamase MBLAC2; acyl-CoA thioesterase MBLAC2;
                     palmitoyl-coenzyme A thioesterase MBLAC2"
                     /calculated_mol_wt=31240
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q68D91.3)"
     Region          22..231
                     /region_name="MBLAC2-like_MBL-fold"
                     /note="uncharacterized human metallo-beta-lactamase
                     domain-containing protein 2 and related proteins; MBL-fold
                     metallo hydrolase domain; cd07712"
                     /db_xref="CDD:293798"
     Site            order(83,85,87..88,170..171,189,231)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293798"
     CDS             1..279
                     /gene="MBLAC2"
                     /coded_by="NM_203406.2:480..1319"
                     /db_xref="CCDS:CCDS4067.1"
                     /db_xref="GeneID:153364"
                     /db_xref="HGNC:HGNC:33711"
                     /db_xref="MIM:620907"
ORIGIN      
        1 msalewyahk slgdgifwiq erfyesgnra niwlvrgseq dvvidtglgl rslpeylyss
       61 gllqdreake daarrpllav athvhfdhsg glyqfdrvav hhaeaealar gdnfetvtwl
      121 sdsevvrtps pgwrarqfrv qavqptlilq dgdvinlgdr qltvmhmpgh srgsiclhdk
      181 drkilfsgdv vydgslidwl pysrisdyvg tcerlielvd rglvekvlpg hfntfgaerl
      241 frlasnyisk agichkvstf amrslaslal rvtnsrtsp
//
LOCUS       NP_002117                295 aa            linear   PRI 27-APR-2025
DEFINITION  hepatic leukemia factor isoform 1 [Homo sapiens].
ACCESSION   NP_002117
VERSION     NP_002117.1
DBSOURCE    REFSEQ: accession NM_002126.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Zhou,H. and Wang,F.
  TITLE     Tensin 1 regulated by hepatic leukemia factor represses the
            progression of prostate cancer
  JOURNAL   Mutagenesis 38 (6), 295-304 (2023)
   PUBMED   37712764
  REMARK    GeneRIF: Tensin 1 regulated by hepatic leukemia factor represses
            the progression of prostate cancer.
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Han,T., Chen,T., Chen,L., Li,K., Xiang,D., Dou,L., Li,H. and Gu,Y.
  TITLE     HLF promotes ovarian cancer progression and chemoresistance via
            regulating Hippo signaling pathway
  JOURNAL   Cell Death Dis 14 (9), 606 (2023)
   PUBMED   37709768
  REMARK    GeneRIF: HLF promotes ovarian cancer progression and
            chemoresistance via regulating Hippo signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Xiang,D., Gu,M., Liu,J., Dong,W., Yang,Z., Wang,K., Fu,J. and
            Wang,H.
  TITLE     m6A RNA methylation-mediated upregulation of HLF promotes
            intrahepatic cholangiocarcinoma progression by regulating the
            FZD4/beta-catenin signaling pathway
  JOURNAL   Cancer Lett 560, 216144 (2023)
   PUBMED   36958694
  REMARK    GeneRIF: m6A RNA methylation-mediated upregulation of HLF promotes
            intrahepatic cholangiocarcinoma progression by regulating the
            FZD4/beta-catenin signaling pathway.
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Li,H., Yang,P., Wang,J., Zhang,J., Ma,Q., Jiang,Y., Wu,Y., Han,T.
            and Xiang,D.
  TITLE     HLF regulates ferroptosis, development and chemoresistance of
            triple-negative breast cancer by activating tumor cell-macrophage
            crosstalk
  JOURNAL   J Hematol Oncol 15 (1), 2 (2022)
   PUBMED   34991659
  REMARK    GeneRIF: HLF regulates ferroptosis, development and chemoresistance
            of triple-negative breast cancer by activating tumor
            cell-macrophage crosstalk.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Hu,P., Guo,J., Zhao,B., Zhang,Z., Zhu,J. and Liu,F.
  TITLE     CircCHD2/miR-200b-3p/HLF Axis Promotes Liver Cirrhosis
  JOURNAL   J Environ Pathol Toxicol Oncol 41 (4), 1-10 (2022)
   PUBMED   36374958
  REMARK    GeneRIF: CircCHD2/miR-200b-3p/HLF Axis Promotes Liver Cirrhosis.
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Falvey,E., Fleury-Olela,F. and Schibler,U.
  TITLE     The rat hepatic leukemia factor (HLF) gene encodes two
            transcriptional activators with distinct circadian rhythms, tissue
            distributions and target preferences
  JOURNAL   EMBO J 14 (17), 4307-4317 (1995)
   PUBMED   7556072
  REMARK    GeneRIF: The authors characterize variants of rat HLF, including
            use of two alternative promoters and a non-AUG translation
            initiation site that has not been confirmed in human.
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Hunger,S.P., Brown,R. and Cleary,M.L.
  TITLE     DNA-binding and transcriptional regulatory properties of hepatic
            leukemia factor (HLF) and the t(17;19) acute lymphoblastic leukemia
            chimera E2A-HLF
  JOURNAL   Mol Cell Biol 14 (9), 5986-5996 (1994)
   PUBMED   8065331
REFERENCE   8  (residues 1 to 295)
  AUTHORS   Inaba,T., Shapiro,L.H., Funabiki,T., Sinclair,A.E., Jones,B.G.,
            Ashmun,R.A. and Look,A.T.
  TITLE     DNA-binding specificity and trans-activating potential of the
            leukemia-associated E2A-hepatic leukemia factor fusion protein
  JOURNAL   Mol Cell Biol 14 (5), 3403-3413 (1994)
   PUBMED   8164688
REFERENCE   9  (residues 1 to 295)
  AUTHORS   Hunger,S.P., Ohyashiki,K., Toyama,K. and Cleary,M.L.
  TITLE     Hlf, a novel hepatic bZIP protein, shows altered DNA-binding
            properties following fusion to E2A in t(17;19) acute lymphoblastic
            leukemia
  JOURNAL   Genes Dev 6 (9), 1608-1620 (1992)
   PUBMED   1516826
REFERENCE   10 (residues 1 to 295)
  AUTHORS   Inaba,T., Roberts,W.M., Shapiro,L.H., Jolly,K.W., Raimondi,S.C.,
            Smith,S.D. and Look,A.T.
  TITLE     Fusion of the leucine zipper gene HLF to the E2A gene in human
            acute B-lineage leukemia
  JOURNAL   Science 257 (5069), 531-534 (1992)
   PUBMED   1386162
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA104709.1, BC036093.1,
            M95585.1, AF035305.1, AA021027.1 and AC007638.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the proline and acidic-rich
            (PAR) protein family, a subset of the bZIP transcription factors.
            The encoded protein forms homodimers or heterodimers with other PAR
            family members and binds sequence-specific promoter elements to
            activate transcription. Chromosomal translocations fusing portions
            of this gene with the E2A gene cause a subset of childhood
            B-lineage acute lymphoid leukemias. Alternatively spliced
            transcript variants have been described, but their biological
            validity has not been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.43262.1,
                                           SRR1660809.156869.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000226067.10/ ENSP00000226067.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q22"
     Protein         1..295
                     /product="hepatic leukemia factor isoform 1"
                     /note="hepatic leukemia factor; HLF, PAR bZIP
                     transcription factor; E2A-HLF fusion transcript protein"
                     /calculated_mol_wt=33068
     Region          37..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16534.1)"
     Region          93..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16534.1)"
     Region          224..283
                     /region_name="bZIP_HLF"
                     /note="Basic leucine zipper (bZIP) domain of Hepatic
                     leukemia factor (HLF) and similar proteins: a DNA-binding
                     and dimerization domain; cd14695"
                     /db_xref="CDD:269843"
     Region          225..283
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269843"
     Region          227..247
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16534.1)"
     Site            order(231..232,234..236,238..243,245..247)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269843"
     Site            order(246,249..250,253..254,256..257,260..261,263..264,
                     267..268,270..271,274..275,277..278)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269843"
     Region          248..255
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16534.1)"
     CDS             1..295
                     /gene="HLF"
                     /coded_by="NM_002126.5:526..1413"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11585.1"
                     /db_xref="GeneID:3131"
                     /db_xref="HGNC:HGNC:4977"
                     /db_xref="MIM:142385"
ORIGIN      
        1 mekmsrplpl nptfipppyg vlrsllenpl klplhhedaf skdkdkekkl ddesnsptvp
       61 qsaflgptlw dktlpydgdt fqleymdlee flsengipps psqhdhsphp pglqpassaa
      121 psvmdlssra saplhpgips pncmqspirp gqllpanrnt pspidpdtiq vpvgyepdpa
      181 dlalssipgq emfdprkrkf seeelkpqpm ikkarkvfip ddlkddkywa rrrknnmaak
      241 rsrdarrlke nqiairasfl ekensalrqe vadlrkelgk cknilakyea rhgpl
//
LOCUS       NP_891548                479 aa            linear   PRI 27-APR-2025
DEFINITION  transcriptional regulator ERG isoform 1 [Homo sapiens].
ACCESSION   NP_891548
VERSION     NP_891548.1
DBSOURCE    REFSEQ: accession NM_182918.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Yamashita,T., Kaplan,U., Chakraborty,A., Marden,G., Gritli,S.,
            Roh,D., Bujor,A., Trojanowski,M., Ligresti,G., Browning,J.L. and
            Trojanowska,M.
  TITLE     ERG Regulates Lymphatic Vessel Specification Genes and Its
            Deficiency Impairs Wound Healing-Associated Lymphangiogenesis
  JOURNAL   Arthritis Rheumatol 76 (11), 1645-1657 (2024)
   PUBMED   38965683
  REMARK    GeneRIF: ERG Regulates Lymphatic Vessel Specification Genes and Its
            Deficiency Impairs Wound Healing-Associated Lymphangiogenesis.
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Wang,C., Hu,M., Yu,K., Liu,W., Hu,A., Kuang,Y., Huang,L.,
            Gajendran,B., Zacksenhaus,E., Xiao,X. and Ben-David,Y.
  TITLE     An intricate regulatory circuit between FLI1 and
            GATA1/GATA2/LDB1/ERG dictates erythroid vs. megakaryocytic
            differentiation
  JOURNAL   Mol Med Rep 29 (6) (2024)
   PUBMED   38695236
  REMARK    GeneRIF: An intricate regulatory circuit between FLI1 and
            GATA1/GATA2/LDB1/ERG dictates erythroid vs. megakaryocytic
            differentiation.
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Tao,T., Chen,H., Xu,Q., Li,Z., Chen,X., Zhou,X. and Luo,W.
  TITLE     NKX2-1-AS1 promotes the lymphangiogenesis of lung adenocarcinoma
            through regulation of ERG-mediated FABP4
  JOURNAL   Tissue Cell 87, 102314 (2024)
   PUBMED   38309204
  REMARK    GeneRIF: NKX2-1-AS1 promotes the lymphangiogenesis of lung
            adenocarcinoma through regulation of ERG-mediated FABP4.
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Behrens,K., Brajanovski,N., Xu,Z., Viney,E.M., DiRago,L.,
            Hediyeh-Zadeh,S., Davis,M.J., Pearson,R.B., Sanij,E.,
            Alexander,W.S. and Ng,A.P.
  TITLE     ERG and c-MYC regulate a critical gene network in BCR::ABL1-driven
            B cell acute lymphoblastic leukemia
  JOURNAL   Sci Adv 10 (10), eadj8803 (2024)
   PUBMED   38457494
  REMARK    GeneRIF: ERG and c-MYC regulate a critical gene network in
            BCR::ABL1-driven B cell acute lymphoblastic leukemia.
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Guo,L., Wu,D., Shen,J. and Gao,Y.
  TITLE     ERG mediates the inhibition of NK cell cytotoxicity through the
            HLX/STAT4/Perforin signaling pathway, thereby promoting the
            progression of myocardial infarction
  JOURNAL   J Physiol Biochem 80 (1), 219-233 (2024)
   PUBMED   38091230
  REMARK    GeneRIF: ERG mediates the inhibition of NK cell cytotoxicity
            through the HLX/STAT4/Perforin signaling pathway, thereby promoting
            the progression of myocardial infarction.
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Zammarchi,F., Boutsalis,G. and Cartegni,L.
  TITLE     5' UTR control of native ERG and of Tmprss2:ERG variants activity
            in prostate cancer
  JOURNAL   PLoS One 8 (3), e49721 (2013)
   PUBMED   23472063
  REMARK    GeneRIF: characterization of native ERG and Tmprss2:ERG variants
            reveals that their different oncogenic potential is affected by the
            status of the Ets domain and the configuration of the 5' UTR region
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Peterson,A., Patil,N., Robbins,C., Wang,L., Cox,D.R. and Myers,R.M.
  TITLE     A transcript map of the Down syndrome critical region on chromosome
            21
  JOURNAL   Hum Mol Genet 3 (10), 1735-1742 (1994)
   PUBMED   7849696
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Rao,V.N., Modi,W.S., Drabkin,H.D., Patterson,D., O'Brien,S.J.,
            Papas,T.S. and Reddy,E.S.
  TITLE     The human erg gene maps to chromosome 21, band q22: relationship to
            the 8; 21 translocation of acute myelogenous leukemia
  JOURNAL   Oncogene 3 (5), 497-500 (1988)
   PUBMED   3274086
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Reddy,E.S., Rao,V.N. and Papas,T.S.
  TITLE     The erg gene: a human gene related to the ets oncogene
  JOURNAL   Proc Natl Acad Sci U S A 84 (17), 6131-6135 (1987)
   PUBMED   3476934
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Rao,V.N., Papas,T.S. and Reddy,E.S.
  TITLE     erg, a human ets-related gene on chromosome 21: alternative
            splicing, polyadenylation, and translation
  JOURNAL   Science 237 (4815), 635-639 (1987)
   PUBMED   3299708
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA850637.1, AK300395.1,
            BC040168.1, AP001423.1, AP001422.1 and BF431907.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the erythroblast
            transformation-specific (ETS) family of transcriptions factors. All
            members of this family are key regulators of embryonic development,
            cell proliferation, differentiation, angiogenesis, inflammation,
            and apoptosis. The protein encoded by this gene is mainly expressed
            in the nucleus. It contains an ETS DNA-binding domain and a PNT
            (pointed) domain which is implicated in the self-association of
            chimeric oncoproteins. This protein is required for platelet
            adhesion to the subendothelium, inducing vascular cell remodeling.
            It also regulates hematopoesis, and the differentiation and
            maturation of megakaryocytic cells. This gene is involved in
            chromosomal translocations, resulting in different fusion gene
            products, such as TMPSSR2-ERG and NDRG1-ERG in prostate cancer,
            EWS-ERG in Ewing's sarcoma and FUS-ERG in acute myeloid leukemia.
            More than two dozens of transcript variants generated from
            combinatorial usage of three alternative promoters and multiple
            alternative splicing events have been reported, but the full-length
            nature of many of these variants has not been determined. [provided
            by RefSeq, Apr 2014].
            
            Transcript Variant: This variant (1) contains a different segment
            for its 5' UTR and 5' coding region, compared to variant 3. The
            resulting protein (isoform 1) has a shorter and distinct N-terminus
            when it is compared to isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.109992.1, BC040168.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000288319.12/ ENSP00000288319.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.2"
     Protein         1..479
                     /product="transcriptional regulator ERG isoform 1"
                     /note="v-ets avian erythroblastosis virus E26 oncogene
                     related; ets-related; ERG, ETS transcription factor;
                     FUS/ERG fusion protein; v-ets erythroblastosis virus E26
                     oncogene like; transcriptional regulator ERG (transforming
                     protein ERG); TMPRSS2/ERG fusion; v-ets erythroblastosis
                     virus E26 oncogene homolog; v-ets avian erythroblastosis
                     virus E26 oncogene homolog"
                     /calculated_mol_wt=53707
     Region          34..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11308.3)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P81270; propagated from
                     UniProtKB/Swiss-Prot (P11308.3)"
     Region          72..92
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11308.3)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P81270; propagated from
                     UniProtKB/Swiss-Prot (P11308.3)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P81270; propagated from
                     UniProtKB/Swiss-Prot (P11308.3)"
     Region          127..201
                     /region_name="SAM_PNT-ERG"
                     /note="Sterile alpha motif (SAM)/Pointed domain of ERG
                     transcription factor; cd08540"
                     /db_xref="CDD:176090"
     Region          242..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11308.3)"
     Region          310..393
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     Site            462..463
                     /site_type="other"
                     /note="Breakpoint for translocation to form ELF4-ERG
                     oncogene; propagated from UniProtKB/Swiss-Prot (P11308.3)"
     CDS             1..479
                     /gene="ERG"
                     /gene_synonym="erg-3; LMPHM14; p55"
                     /coded_by="NM_182918.4:98..1537"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13658.1"
                     /db_xref="GeneID:2078"
                     /db_xref="HGNC:HGNC:3446"
                     /db_xref="MIM:165080"
ORIGIN      
        1 mastikeals vvsedqslfe caygtphlak temtassssd ygqtskmspr vpqqdwlsqp
       61 parvtikmec npsqvngsrn spdecsvakg gkmvgspdtv gmnygsymee khmpppnmtt
      121 nerrvivpad ptlwstdhvr qwlewavkey glpdvnillf qnidgkelck mtkddfqrlt
      181 psynadills hlhylretpl phltsddvdk alqnsprlmh arntggaafi fpntsvypea
      241 tqrittrpdl pyepprrsaw tghghptpqs kaaqpspstv pktedqrpql dpyqilgpts
      301 srlanpgsgq iqlwqfllel lsdssnssci twegtngefk mtdpdevarr wgerkskpnm
      361 nydklsralr yyydknimtk vhgkryaykf dfhgiaqalq phppesslyk ypsdlpymgs
      421 yhahpqkmnf vaphppalpv tsssffaapn pywnsptggi ypntrlptsh mpshlgtyy
//
LOCUS       NP_071906                392 aa            linear   PRI 27-APR-2025
DEFINITION  5-azacytidine-induced protein 2 isoform a [Homo sapiens].
ACCESSION   NP_071906
VERSION     NP_071906.1
DBSOURCE    REFSEQ: accession NM_022461.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Endo,R., Kinefuchi,H., Sawada,M., Kikuchi,R., Kojima,W., Matsuda,N.
            and Yamano,K.
  TITLE     TBK1 adaptor AZI2/NAP1 regulates NDP52-driven mitochondrial
            autophagy
  JOURNAL   J Biol Chem 300 (10), 107775 (2024)
   PUBMED   39276928
  REMARK    GeneRIF: TBK1 adaptor AZI2/NAP1 regulates NDP52-driven
            mitochondrial autophagy.
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Yeo,S.K., Haas,M., Manupati,K., Hao,M., Yang,F., Chen,S. and
            Guan,J.L.
  TITLE     AZI2 mediates TBK1 activation at unresolved selective autophagy
            cargo receptor complexes with implications for CD8 T-cell
            infiltration in breast cancer
  JOURNAL   Autophagy 20 (3), 525-540 (2024)
   PUBMED   37733921
  REMARK    GeneRIF: AZI2 mediates TBK1 activation at unresolved selective
            autophagy cargo receptor complexes with implications for CD8 T-cell
            infiltration in breast cancer.
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Paul,S., Sarraf,S.A., Nam,K.H., Zavar,L., DeFoor,N., Biswas,S.R.,
            Fritsch,L.E., Yaron,T.M., Johnson,J.L., Huntsman,E.M.,
            Cantley,L.C., Ordureau,A. and Pickrell,A.M.
  TITLE     NAK-associated protein 1/NAP1 activates TBK1 to ensure accurate
            mitosis and cytokinesis
  JOURNAL   J Cell Biol 223 (2) (2024)
   PUBMED   38059900
  REMARK    GeneRIF: NAK-associated protein 1/NAP1 activates TBK1 to ensure
            accurate mitosis and cytokinesis.
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Shang,J., Xia,T., Han,Q.Q., Zhao,X., Hu,M.M., Shu,H.B. and Guo,L.
  TITLE     Quantitative Proteomics Identified TTC4 as a TBK1 Interactor and a
            Positive Regulator of SeV-Induced Innate Immunity
  JOURNAL   Proteomics 18 (2) (2018)
   PUBMED   29251827
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Sasai,M., Shingai,M., Funami,K., Yoneyama,M., Fujita,T.,
            Matsumoto,M. and Seya,T.
  TITLE     NAK-associated protein 1 participates in both the TLR3 and the
            cytoplasmic pathways in type I IFN induction
  JOURNAL   J Immunol 177 (12), 8676-8683 (2006)
   PUBMED   17142768
  REMARK    GeneRIF: Both the cytoplasmic and TLR3-mediated dsRNA recognition
            pathways converge upon NAP1 for the activation of the IRF-3 and
            IFN-beta promoter.
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Sasai,M., Oshiumi,H., Matsumoto,M., Inoue,N., Fujita,F.,
            Nakanishi,M. and Seya,T.
  TITLE     Cutting Edge: NF-kappaB-activating kinase-associated protein 1
            participates in TLR3/Toll-IL-1 homology domain-containing adapter
            molecule-1-mediated IFN regulatory factor 3 activation
  JOURNAL   J Immunol 174 (1), 27-30 (2005)
   PUBMED   15611223
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Fujita,F., Taniguchi,Y., Kato,T., Narita,Y., Furuya,A., Ogawa,T.,
            Sakurai,H., Joh,T., Itoh,M., Delhase,M., Karin,M. and Nakanishi,M.
  TITLE     Identification of NAP1, a regulatory subunit of IkappaB
            kinase-related kinases that potentiates NF-kappaB signaling
  JOURNAL   Mol Cell Biol 23 (21), 7780-7793 (2003)
   PUBMED   14560022
  REMARK    GeneRIF: These results define NAK-associated protein 1 (NAP1) as an
            activator of IkappaB kinase-related kinases and suggest that the
            NAK-NAP1 complex may protect cells from TNF-alpha-induced apoptosis
            by promoting NF-kappaB activation.
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Miyagawa,J., Muguruma,M., Aoto,H., Suetake,I., Nakamura,M. and
            Tajima,S.
  TITLE     Isolation of the novel cDNA of a gene of which expression is
            induced by a demethylating stimulus
  JOURNAL   Gene 240 (2), 289-295 (1999)
   PUBMED   10580148
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290637.1, AK025592.1, BX648471.1 and AC098616.2.
            
            Summary: AZI2, or NAP1, contributes to the activation of NFKB (see
            MIM 164011)-dependent gene expression by activating IKK-related
            kinases, such as NAK (TBK1; MIM 604834) (Fujita et al., 2003
            [PubMed 14560022]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.239794.1,
                                           SRR1660803.212983.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000479665.6/ ENSP00000419371.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.1"
     Protein         1..392
                     /product="5-azacytidine-induced protein 2 isoform a"
                     /note="NAK-associated protein 1; 5-azacytidine induced
                     gene 2; 5-azacytidine-induced protein 2;
                     NF-kappa-B-activating kinase-associated protein 1"
                     /calculated_mol_wt=44804
     Region          1..197
                     /region_name="Homodimerization.
                     /evidence=ECO:0000250|UniProtKB:Q9QYP6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6S1.1)"
     Region          <13..>242
                     /region_name="SCP-1"
                     /note="Synaptonemal complex protein 1 (SCP-1); pfam05483"
                     /db_xref="CDD:114219"
     Region          213..265
                     /region_name="TBD"
                     /note="TBD domain; pfam12845"
                     /db_xref="CDD:463729"
     Region          216..257
                     /region_name="Interaction with TBK1 and IKBKE.
                     /evidence=ECO:0000269|PubMed:14560022"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6S1.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4KMA0; propagated from
                     UniProtKB/Swiss-Prot (Q9H6S1.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H6S1.1)"
     CDS             1..392
                     /gene="AZI2"
                     /gene_synonym="AZ2; NAP1; TILP"
                     /coded_by="NM_022461.5:230..1408"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2647.1"
                     /db_xref="GeneID:64343"
                     /db_xref="HGNC:HGNC:24002"
                     /db_xref="MIM:609916"
ORIGIN      
        1 mdalveddic ilnhekahkr dtvtpvsiys gdesvashfa lvtayedikk rlkdsekens
       61 llkkrirfle ekliarfeee tssvgreqvn kayhayrevc idrdnlkskl dkmnkdnses
      121 lkvlneqlqs kevellqlrt evetqqvmrn lnppssnwev eklscdlkih gleqelelmr
      181 kecsdlkiel qkakqtdpyq ednlksrdlq klsissdnmq haywelkrem snlhlvtqvq
      241 aellrklkts taikkacapv gcsedlgrds tklhlmnfta tytrhppllp ngkalchtts
      301 splpgdvkvl sekailqswt dnersipndg tcfqehssyg rnslednswv fpsppksset
      361 afgetktktl plpnlpplhy ldqhnqncly kn
//
LOCUS       NP_000660                375 aa            linear   PRI 27-APR-2025
DEFINITION  alcohol dehydrogenase 1C [Homo sapiens].
ACCESSION   NP_000660
VERSION     NP_000660.1
DBSOURCE    REFSEQ: accession NM_000669.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Yu,Y. and Liu,Y.
  TITLE     LncRNA LINC01339 Hinders the Development of Wilms' Tumor via
            MiR-135b-3p/ADH1C Axis
  JOURNAL   Horm Metab Res 56 (3), 244-254 (2024)
   PUBMED   37890508
  REMARK    GeneRIF: LncRNA LINC01339 Hinders the Development of Wilms' Tumor
            via MiR-135b-3p/ADH1C Axis.
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Kukowka,A., Brzuchalski,B., Kurzawski,M., Malinowski,D. and
            Bialecka,M.A.
  TITLE     ADH1B, ADH1B/C and CYP2E1 Gene Polymorphism and the Risk of Fetal
            Alcohol Spectrum Disorder
  JOURNAL   Genes (Basel) 14 (7), 1392 (2023)
   PUBMED   37510297
  REMARK    GeneRIF: ADH1B, ADH1B/C and CYP2E1 Gene Polymorphism and the Risk
            of Fetal Alcohol Spectrum Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Hoang,Y.T.T., Nguyen,Y.T., Vu,L.T., Bui,H.T.T., Nguyen,Q.V.,
            Vu,N.P., Nguyen,T.D. and Nguyen,H.H.
  TITLE     Association of ADH1B rs1229984, ADH1C rs698, and ALDH2 rs671 with
            Alcohol abuse and Alcoholic Cirrhosis in People Living in Northeast
            Vietnam
  JOURNAL   Asian Pac J Cancer Prev 24 (6), 2073-2082 (2023)
   PUBMED   37378938
  REMARK    GeneRIF: Association of ADH1B rs1229984, ADH1C rs698, and ALDH2
            rs671 with Alcohol abuse and Alcoholic Cirrhosis in People Living
            in Northeast Vietnam.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Aliyeva,G., Muslumov,G., Bayramov,B., Zeynalov,N. and Behbudov,V.
  TITLE     INVESTIGATION OF ALCOHOL DEHYDROGENASE (ADH3) GENE POLYMOPHISM IN
            PATIENTS WITH CHRONIC ALCOHOLIC PANCRATITIS IN AZERBAIJAN
            POPULATION
  JOURNAL   Georgian Med News (332), 113-117 (2022)
   PUBMED   36701787
  REMARK    GeneRIF: INVESTIGATION OF ALCOHOL DEHYDROGENASE (ADH3) GENE
            POLYMOPHISM IN PATIENTS WITH CHRONIC ALCOHOLIC PANCRATITIS IN
            AZERBAIJAN POPULATION.
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Yokoyama,S., Matsuo,Y., Rajasekharan,S. and Yokoyama,R.
  TITLE     Molecular structure of the human alcohol dehydrogenase 3 gene
  JOURNAL   Jpn J Genet 67 (2), 167-171 (1992)
   PUBMED   1524834
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Hurley,T.D., Bosron,W.F., Hamilton,J.A. and Amzel,L.M.
  TITLE     Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic
            effects of non-active-site substitutions
  JOURNAL   Proc Natl Acad Sci U S A 88 (18), 8149-8153 (1991)
   PUBMED   1896463
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Stewart,M.J., McBride,M.S., Winter,L.A. and Duester,G.
  TITLE     Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and
            ADH3: interaction of CCAAT/enhancer-binding protein with elements
            flanking the ADH2 TATA box
  JOURNAL   Gene 90 (2), 271-279 (1990)
   PUBMED   2169444
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Yasunami,M., Kikuchi,I., Sarapata,D. and Yoshida,A.
  TITLE     The human class I alcohol dehydrogenase gene cluster: three genes
            are tandemly organized in an 80-kb-long segment of the genome
  JOURNAL   Genomics 7 (2), 152-158 (1990)
   PUBMED   2347582
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Ikuta,T., Szeto,S. and Yoshida,A.
  TITLE     Three human alcohol dehydrogenase subunits: cDNA structure and
            molecular and evolutionary divergence
  JOURNAL   Proc Natl Acad Sci U S A 83 (3), 634-638 (1986)
   PUBMED   2935875
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Lange,L.G., Sytkowski,A.J. and Vallee,B.L.
  TITLE     Human liver alcohol dehydrogenase: purification, composition, and
            catalytic features
  JOURNAL   Biochemistry 15 (21), 4687-4693 (1976)
   PUBMED   9982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA562068.1, BC074786.2 and
            CD014078.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes class I alcohol dehydrogenase, gamma
            subunit, which is a member of the alcohol dehydrogenase family.
            Members of this enzyme family metabolize a wide variety of
            substrates, including ethanol, retinol, other aliphatic alcohols,
            hydroxysteroids, and lipid peroxidation products. Class I alcohol
            dehydrogenase, consisting of several homo- and heterodimers of
            alpha, beta, and gamma subunits, exhibits high activity for ethanol
            oxidation to acetaldehyde, thus playing a major role in ethanol
            catabolism. Three genes encoding alpha, beta and gamma subunits are
            tandemly organized in a genomic segment as a gene cluster. An
            association between ADH1C polymorphism and alcohol dependence has
            not been established. [provided by RefSeq, Sep 2019].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.164929.1,
                                           SRR5189664.65250.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2152474
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000515683.6/ ENSP00000426083.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..375
                     /product="alcohol dehydrogenase 1C"
                     /EC_number="1.1.1.1"
                     /note="ADH, gamma subunit; alcohol dehydrogenase 3 (class
                     I), gamma polypeptide; aldehyde reductase"
                     /calculated_mol_wt=39737
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:6391921; propagated from
                     UniProtKB/Swiss-Prot (P00326.2)"
     Region          3..375
                     /region_name="alcohol_DH_class_I_II_IV"
                     /note="class I, II, IV alcohol dehydrogenases; cd08299"
                     /db_xref="CDD:176259"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00325; propagated from
                     UniProtKB/Swiss-Prot (P00326.2)"
     Site            order(47,68,175)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176259"
     Site            order(48..49,175,179,200..204,224..225,229,269..270,
                     274..275,293..294,318..320,370)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176259"
     Site            order(49,68,94,117,142,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176259"
     Site            order(98..99,101,104,112)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176259"
     Site            order(102..103,106,111,261..262,273,286..287,292..293,
                     301..306,309..319)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176259"
     CDS             1..375
                     /gene="ADH1C"
                     /gene_synonym="ADH3"
                     /coded_by="NM_000669.5:72..1199"
                     /db_xref="CCDS:CCDS54780.1"
                     /db_xref="GeneID:126"
                     /db_xref="HGNC:HGNC:251"
                     /db_xref="MIM:103730"
ORIGIN      
        1 mstagkvikc kaavlwelkk pfsieeveva ppkahevrik mvaagicrsd ehvvsgnlvt
       61 plpvilghea agivesvgeg vttvkpgdkv iplftpqcgk cricknpesn yclkndlgnp
      121 rgtlqdgtrr ftcsgkpihh fvgvstfsqy tvvdenavak idaasplekv cligcgfstg
      181 ygsavkvakv tpgstcavfg lggvglsvvm gckaagaari iavdinkdkf akakelgate
      241 cinpqdykkp iqevlkemtd ggvdfsfevi grldtmmasl lccheacgts vivgvppdsq
      301 nlsinpmlll tgrtwkgaif ggfkskesvp klvadfmakk fsldalitni lpfekinegf
      361 dllrsgksir tvltf
//
LOCUS       NP_000383               1545 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-binding cassette sub-family C member 2 [Homo sapiens].
ACCESSION   NP_000383
VERSION     NP_000383.2
DBSOURCE    REFSEQ: accession NM_000392.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1545)
  AUTHORS   Nakayama,H., Ishida,H., Iidaka,M., Kato,S., Nakatani,K.,
            Nakayama,A., Noguchi,T., Nishihara,S., Oikawa,S., Usami,T.,
            Mitsui,Y., Ishii,Y.U., Toshima,H., Kobayashi,K., Murase,R.,
            Matsumoto,N., Suzuki,K., Shimada,K., Yoshida,H. and Fujita,K.I.
  TITLE     Association Between ABCC2 -24C>T and Nab-Paclitaxel-induced
            Peripheral Neuropathy in Japanese Patients With Pancreatic Cancer
  JOURNAL   Anticancer Res 44 (11), 5023-5033 (2024)
   PUBMED   39477313
  REMARK    GeneRIF: Association Between ABCC2 -24C>T and
            Nab-Paclitaxel-induced Peripheral Neuropathy in Japanese Patients
            With Pancreatic Cancer.
REFERENCE   2  (residues 1 to 1545)
  AUTHORS   Kolz,C., Gaugaz,F.Z., Handin,N., Schaeffeler,E., Tremmel,R.,
            Winter,S., Klein,K., Zanger,U.M., Artursson,P., Schwab,M. and
            Nies,A.T.
  TITLE     In silico and biological analyses of missense variants of the human
            biliary efflux transporter ABCC2: effects of novel rare missense
            variants
  JOURNAL   Br J Pharmacol 181 (22), 4593-4609 (2024)
   PUBMED   39096023
  REMARK    GeneRIF: In silico and biological analyses of missense variants of
            the human biliary efflux transporter ABCC2: effects of novel rare
            missense variants.
REFERENCE   3  (residues 1 to 1545)
  AUTHORS   Wang,Y., Gan,X., Cheng,X., Jia,Y., Wang,G., Tang,X., Du,H., Li,X.,
            Liu,X., Xing,X., Ji,J. and Li,Z.
  TITLE     ABCC2 induces metabolic vulnerability and cellular ferroptosis via
            enhanced glutathione efflux in gastric cancer
  JOURNAL   Clin Transl Med 14 (8), e1754 (2024)
   PUBMED   39095325
  REMARK    GeneRIF: ABCC2 induces metabolic vulnerability and cellular
            ferroptosis via enhanced glutathione efflux in gastric cancer.
REFERENCE   4  (residues 1 to 1545)
  AUTHORS   Mao,Y.X., Chen,Z.P., Wang,L., Wang,J., Zhou,C.Z., Hou,W.T. and
            Chen,Y.
  TITLE     Transport mechanism of human bilirubin transporter ABCC2 tuned by
            the inter-module regulatory domain
  JOURNAL   Nat Commun 15 (1), 1061 (2024)
   PUBMED   38316776
  REMARK    GeneRIF: Transport mechanism of human bilirubin transporter ABCC2
            tuned by the inter-module regulatory domain.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1545)
  AUTHORS   Zhang,Y., Zhao,T., Li,W. and Vore,M.
  TITLE     The 5'-untranslated region of multidrug resistance associated
            protein 2 (MRP2; ABCC2) regulates downstream open reading frame
            expression through translational regulation
  JOURNAL   Mol Pharmacol 77 (2), 237-246 (2010)
   PUBMED   19890061
  REMARK    GeneRIF: The 5'-untranslated region of MRP2 markedly influences
            MRP2 mRNA translation regulation.
REFERENCE   6  (residues 1 to 1545)
  AUTHORS   Tanaka,T., Uchiumi,T., Hinoshita,E., Inokuchi,A., Toh,S., Wada,M.,
            Takano,H., Kohno,K. and Kuwano,M.
  TITLE     The human multidrug resistance protein 2 gene: functional
            characterization of the 5'-flanking region and expression in
            hepatic cells
  JOURNAL   Hepatology 30 (6), 1507-1512 (1999)
   PUBMED   10573531
REFERENCE   7  (residues 1 to 1545)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
REFERENCE   8  (residues 1 to 1545)
  AUTHORS   Taniguchi,K., Wada,M., Kohno,K., Nakamura,T., Kawabe,T.,
            Kawakami,M., Kagotani,K., Okumura,K., Akiyama,S. and Kuwano,M.
  TITLE     A human canalicular multispecific organic anion transporter (cMOAT)
            gene is overexpressed in cisplatin-resistant human cancer cell
            lines with decreased drug accumulation
  JOURNAL   Cancer Res 56 (18), 4124-4129 (1996)
   PUBMED   8797578
REFERENCE   9  (residues 1 to 1545)
  AUTHORS   Buchler,M., Konig,J., Brom,M., Kartenbeck,J., Spring,H., Horie,T.
            and Keppler,D.
  TITLE     cDNA cloning of the hepatocyte canalicular isoform of the multidrug
            resistance protein, cMrp, reveals a novel conjugate export pump
            deficient in hyperbilirubinemic mutant rats
  JOURNAL   J Biol Chem 271 (25), 15091-15098 (1996)
   PUBMED   8662992
REFERENCE   10 (residues 1 to 1545)
  AUTHORS   Mayer,R., Kartenbeck,J., Buchler,M., Jedlitschky,G., Leier,I. and
            Keppler,D.
  TITLE     Expression of the MRP gene-encoded conjugate export pump in liver
            and its selective absence from the canalicular membrane in
            transport-deficient mutant hepatocytes
  JOURNAL   J Cell Biol 131 (1), 137-150 (1995)
   PUBMED   7559771
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133353.6, U49248.1, U63970.1
            and AL392107.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 10, 2018 this sequence version replaced NP_000383.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the MRP subfamily which is involved in
            multi-drug resistance. This protein is expressed in the canalicular
            (apical) part of the hepatocyte and functions in biliary transport.
            Substrates include anticancer drugs such as vinblastine; therefore,
            this protein appears to contribute to drug resistance in mammalian
            cells. Several different mutations in this gene have been observed
            in patients with Dubin-Johnson syndrome (DJS), an autosomal
            recessive disorder characterized by conjugated hyperbilirubinemia.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.4000.1, U49248.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2144835
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000647814.1/ ENSP00000497274.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            regulatory uORF        :: PMID: 19890061
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..1545
                     /product="ATP-binding cassette sub-family C member 2"
                     /EC_number="7.6.2.2"
                     /EC_number="7.6.2.3"
                     /note="canalicular multispecific organic anion transporter
                     1; canalicular multidrug resistance protein; multidrug
                     resistance-associated protein 2; ATP-binding cassette,
                     sub-family C (CFTR/MRP), member 2"
                     /calculated_mol_wt=174077
     Site            7
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92887.3)"
     Region          8..1537
                     /region_name="MRP_assoc_pro"
                     /note="multi drug resistance-associated protein (MRP);
                     TIGR00957"
                     /db_xref="CDD:188098"
     Site            12
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92887.3)"
     Site            28..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            127..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            166..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Region          253..284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63120; propagated from
                     UniProtKB/Swiss-Prot (Q92887.3)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92887.3)"
     Site            314..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            361..381
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            438..458
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            462..482
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            545..565
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            588..608
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            878
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92887.3)"
     Site            926
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92887.3)"
     Site            930
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92887.3)"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92887.3)"
     Site            972..992
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            1011
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92887.3)"
     Site            1034..1054
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            1098..1118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            1120..1140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            1212..1232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            1235..1255
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92887.3)"
     Site            1438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92887.3)"
     CDS             1..1545
                     /gene="ABCC2"
                     /gene_synonym="ABC30; CMOAT; cMRP; DJS; MRP2"
                     /coded_by="NM_000392.5:206..4843"
                     /db_xref="CCDS:CCDS7484.1"
                     /db_xref="GeneID:1244"
                     /db_xref="HGNC:HGNC:53"
                     /db_xref="MIM:601107"
ORIGIN      
        1 mlekfcnstf wnssfldspe adlplcfeqt vlvwiplgyl wllapwqllh vyksrtkrss
       61 ttklylakqv fvgfllilaa ielalvlted sgqatvpavr ytnpslylgt wllvlliqys
      121 rqwcvqknsw flslfwilsi lcgtfqfqtl irtllqgdns nlaysclffi sygfqilili
      181 fsafsennes snnpssiasf lssityswyd siilkgykrp ltledvwevd eemktktlvs
      241 kfethmkrel qkarralqrr qekssqqnsg arlpglnknq sqsqdalvle dvekkkkksg
      301 tkkdvpkswl mkalfktfym vllksfllkl vndiftfvsp qllkllisfa sdrdtylwig
      361 ylcaillfta aliqsfclqc yfqlcfklgv kvrtaimasv ykkaltlsnl arkeytvget
      421 vnlmsvdaqk lmdvtnfmhm lwssvlqivl sifflwrelg psvlagvgvm vlvipinail
      481 stksktiqvk nmknkdkrlk imneilsgik ilkyfaweps frdqvqnlrk kelknllafs
      541 qlqcvvifvf qltpvlvsvv tfsvyvlvds nnildaqkaf tsitlfnilr fplsmlpmmi
      601 ssmlqasvst erlekylggd dldtsairhd cnfdkamqfs easftwehds eatvrdvnld
      661 imagqlvavi gpvgsgkssl isamlgemen vhghitikgt tayvpqqswi qngtikdnil
      721 fgtefnekry qqvleacall pdlemlpggd laeigekgin lsggqkqris laratyqnld
      781 iyllddplsa vdahvgkhif nkvlgpngll kgktrllvth smhflpqvde ivvlgngtiv
      841 ekgsysalla kkgefaknlk tflrhtgpee eatvhdgsee edddygliss veeipedaas
      901 itmrrensfr rtlsrssrsn grhlkslrns lktrnvnslk edeelvkgqk likkefietg
      961 kvkfsiyley lqaiglfsif fiilafvmns vafigsnlwl sawtsdskif nstdypasqr
     1021 dmrvgvygal glaqgifvfi ahfwsafgfv hasnilhkql lnnilrapmr ffdttptgri
     1081 vnrfagdist vddtlpqslr switcflgii stlvmicmat pvftiivipl giiyvsvqmf
     1141 yvstsrqlrr ldsvtrspiy shfsetvsgl pvirafehqq rflkhnevri dtnqkcvfsw
     1201 itsnrwlair lelvgnltvf fsalmmviyr dtlsgdtvgf vlsnalnitq tlnwlvrmts
     1261 eietnivave riteytkven eapwvtdkrp ppdwpskgki qfnnyqvryr peldlvlrgi
     1321 tcdigsmeki gvvgrtgagk ssltnclfri leaaggqiii dgvdiasigl hdlrekltii
     1381 pqdpilfsgs lrmnldpfnn ysdeeiwkal elahlksfva slqlglshev teaggnlsig
     1441 qrqllclgra llrkskilvl deataavdle tdnliqttiq nefahctvit iahrlhtimd
     1501 sdkvmvldng kiiecgspee llqipgpfyf makeagienv nstkf
//
LOCUS       NP_056209                573 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 10 [Homo sapiens].
ACCESSION   NP_056209
VERSION     NP_056209.2
DBSOURCE    REFSEQ: accession NM_015394.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Lorenz,P., Steinbeck,F., Krause,L. and Thiesen,H.J.
  TITLE     The KRAB Domain of ZNF10 Guides the Identification of Specific
            Amino Acids That Transform the Ancestral KRAB-A-Related Domain
            Present in Human PRDM9 into a Canonical Modern KRAB-A Domain
  JOURNAL   Int J Mol Sci 23 (3), 1072 (2022)
   PUBMED   35162997
  REMARK    GeneRIF: The KRAB Domain of ZNF10 Guides the Identification of
            Specific Amino Acids That Transform the Ancestral KRAB-A-Related
            Domain Present in Human PRDM9 into a Canonical Modern KRAB-A
            Domain.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Nishitsuji,H., Sawada,L., Sugiyama,R. and Takaku,H.
  TITLE     ZNF10 inhibits HIV-1 LTR activity through interaction with
            NF-kappaB and Sp1 binding motifs
  JOURNAL   FEBS Lett 589 (15), 2019-2025 (2015)
   PUBMED   26096782
  REMARK    GeneRIF: results indicate that ZNF10 could be involved in a potent
            intrinsic antiretroviral defense
REFERENCE   5  (residues 1 to 573)
  AUTHORS   Born,N., Thiesen,H.J. and Lorenz,P.
  TITLE     The B-subdomain of the Xenopus laevis XFIN KRAB-AB domain is
            responsible for its weaker transcriptional repressor activity
            compared to human ZNF10/Kox1
  JOURNAL   PLoS One 9 (2), e87609 (2014)
   PUBMED   24498343
  REMARK    GeneRIF: Data indicate that Xenopus laevis XFIN-AB displayed
            reduced potency in repression compared to human ZNF10 KRAB-AB.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 573)
  AUTHORS   Vissing,H., Meyer,W.K., Aagaard,L., Tommerup,N. and Thiesen,H.J.
  TITLE     Repression of transcriptional activity by heterologous KRAB domains
            present in zinc finger proteins
  JOURNAL   FEBS Lett 369 (2-3), 153-157 (1995)
   PUBMED   7649249
REFERENCE   7  (residues 1 to 573)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
REFERENCE   8  (residues 1 to 573)
  AUTHORS   Rousseau-Merck,M.F., Hillion,J., Jonveaux,P., Couillin,P.,
            Seite,P., Thiesen,H.J. and Berger,R.
  TITLE     Chromosomal localization of 9 KOX zinc finger genes: physical
            linkages suggest clustering of KOX genes on chromosomes 12, 16, and
            19
  JOURNAL   Hum Genet 92 (6), 583-587 (1993)
   PUBMED   8262519
REFERENCE   9  (residues 1 to 573)
  AUTHORS   Huebner,K., Druck,T., Croce,C.M. and Thiesen,H.J.
  TITLE     Twenty-seven nonoverlapping zinc finger cDNAs from human T cells
            map to nine different chromosomes with apparent clustering
  JOURNAL   Am J Hum Genet 48 (4), 726-740 (1991)
   PUBMED   2014798
REFERENCE   10 (residues 1 to 573)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026786.5, BC024182.2,
            AL110188.1, BE895826.1 and AI972895.1.
            
            On Jun 3, 2002 this sequence version replaced NP_056209.1.
            
            Summary: The protein encoded by this gene contains a C2H2 zinc
            finger, and has been shown to function as a transcriptional
            repressor. The Kruppel-associated box (KRAB) domain of this protein
            is found to be responsible for its transcriptional repression
            activity. RING finger containing protein TIF1 was reported to
            interact with the KRAB domain, and may serve as a mediator for the
            repression activity of this protein. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC024182.2, SRR1660805.254984.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248211.11/ ENSP00000248211.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..573
                     /product="zinc finger protein 10"
                     /note="zinc finger protein 10 (KOX 1); zinc finger protein
                     KOX1"
                     /calculated_mol_wt=66324
     Region          14..73
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          213..232
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          267..287
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <272..474
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Site            order(272,274,276,278..279,282..283,286,300,302,306..307,
                     310..311,314,328,330,332,334..335,338..339,342)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          295..315
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          323..343
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          351..371
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          379..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          407..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(440,442,444,446..447,450..451,454,468,470,474..475,
                     478..479,482,496,498,500,502..503,506..507,510)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          463..483
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          475..500
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          491..511
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          519..539
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          547..567
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..573
                     /gene="ZNF10"
                     /gene_synonym="KOX1"
                     /coded_by="NM_015394.5:188..1909"
                     /db_xref="CCDS:CCDS9283.1"
                     /db_xref="GeneID:7556"
                     /db_xref="HGNC:HGNC:12879"
                     /db_xref="MIM:194538"
ORIGIN      
        1 mdaksltaws rtlvtfkdvf vdftreewkl ldtaqqivyr nvmlenyknl vslgyqltkp
       61 dvilrlekge epwlvereih qethpdseta feikssvssr sifkdkqscd ikmegmarnd
      121 lwylsleevw kcrdqldkyq enperhlrqv aftqkkvltq ervsesgkyg gncllpaqlv
      181 lreyfhkrds htkslkhdlv lnghqdscas nsnecgqtfc qnihliqfar thtgdksykc
      241 pdndnslthg sslgiskgih rekpyeckec gkffswrsnl trhqlihtge kpyeckecgk
      301 sfsrsshlig hqkthtgeep yeckecgksf swfshlvthq rthtgdklyt cnqcgksfvh
      361 ssrlirhqrt htgekpyecp ecgksfrqst hlilhqrthv rvrpyecnec gksysqrshl
      421 vvhhrihtgl kpfeckdcgk cfsrsshlys hqrthtgekp yechdcgksf sqssalivhq
      481 rihtgekpye ccqcgkafir kndlikhqri hvgeetykcn qcgiifsqns pfivhqiaht
      541 geqfltcnqc gtalvntsnl igyqtnhire nay
//
LOCUS       NP_699187                336 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 21 isoform 1 [Homo sapiens].
ACCESSION   NP_699187
VERSION     NP_699187.1
DBSOURCE    REFSEQ: accession NM_153356.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wang,Y.Y., Ke,C.C., Chen,Y.L., Lin,Y.H., Yu,I.S., Ku,W.C.,
            O'Bryan,M.K. and Lin,Y.H.
  TITLE     Deficiency of the Tbc1d21 gene causes male infertility with
            morphological abnormalities of the sperm mitochondria and flagellum
            in mice
  JOURNAL   PLoS Genet 16 (9), e1009020 (2020)
   PUBMED   32976492
  REMARK    GeneRIF: Deficiency of the Tbc1d21 gene causes male infertility
            with morphological abnormalities of the sperm mitochondria and
            flagellum in mice.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Lin,Y.H., Ke,C.C., Wang,Y.Y., Chen,M.F., Chen,T.M., Ku,W.C.,
            Chiang,H.S. and Yeh,C.H.
  TITLE     RAB10 Interacts with the Male Germ Cell-Specific GTPase-Activating
            Protein during Mammalian Spermiogenesis
  JOURNAL   Int J Mol Sci 18 (1), 97 (2017)
   PUBMED   28067790
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Nakano,M., Ikeda,Y., Tokuda,Y., Fuwa,M., Ueno,M., Imai,K., Sato,R.,
            Omi,N., Adachi,H., Kageyama,M., Mori,K., Kinoshita,S. and
            Tashiro,K.
  TITLE     Novel common variants and susceptible haplotype for exfoliation
            glaucoma specific to Asian population
  JOURNAL   Sci Rep 4, 5340 (2014)
   PUBMED   24938310
  REMARK    GeneRIF: Data indicate that single-nucleotide polymorphisms (SNPs)
            distributing in not only lysyl oxidase-like 1 gene (LOXL1) but also
            TBC1 domain family member 21 protein (TBC1D21) and promyelocytic
            leukemia protein (PML).
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Lin,Y.H., Lin,Y.M., Kuo,Y.C., Wang,Y.Y. and Kuo,P.L.
  TITLE     Identification and characterization of a novel Rab
            GTPase-activating protein in spermatids
  JOURNAL   Int J Androl 34 (5 Pt 2), e358-e367 (2011)
   PUBMED   21128978
  REMARK    GeneRIF: MgcRabGAP is involved in acrosome/acroplaxome formation
            and cytoskeletal reorganization via Rab activity during mammalian
            spermiogenesis
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   8  (residues 1 to 336)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 336)
  AUTHORS   Itoh,T., Satoh,M., Kanno,E. and Fukuda,M.
  TITLE     Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16)
            domain-containing proteins based on their Rab-binding activity
  JOURNAL   Genes Cells 11 (9), 1023-1037 (2006)
   PUBMED   16923123
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018943.10, HY018107.1, BC033516.1 and AB449907.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.354487.1,
                                           SRR5189667.124064.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300504.7/ ENSP00000300504.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..336
                     /product="TBC1 domain family member 21 isoform 1"
                     /note="male germ cell-specific expressed, containing a
                     RabGAP domain; male germ cell Rab GTPase-activating
                     protein"
                     /calculated_mol_wt=39090
     Region          62..287
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            124
                     /site_type="other"
                     /note="Arginine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q8IYX1.1)"
     Site            163
                     /site_type="other"
                     /note="Glutamine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q8IYX1.1)"
     CDS             1..336
                     /gene="TBC1D21"
                     /gene_synonym="MgcRabGAP"
                     /coded_by="NM_153356.3:147..1157"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10252.1"
                     /db_xref="GeneID:161514"
                     /db_xref="HGNC:HGNC:28536"
                     /db_xref="MIM:620387"
ORIGIN      
        1 mttlspensl sarqsasfil vkrkppidkt ewdsffdesg hlaksrdfic vnilerglhp
       61 fvrteawkfl tgyfswqssq derltvdsmr rknykalcqm yekiqpllen lhrnftetrn
      121 niardiqkiy dkdplgnvli dkkrlekill lsyvcntqae yqqgfhemmm lfqlmvehdh
      181 etfwlfqffl qktehscvin igvaknldml stlitfldpv faehlkgkga gavqslfpwf
      241 cfcfqrafks fddvwrlwev lltgkpcrnf qvlvaysmlq mvreqvlqes mggddillac
      301 nnlidldade lisaacvvya eliqkdvpqt lkdffl
//
LOCUS       NP_037416                494 aa            linear   PRI 27-APR-2025
DEFINITION  DNA-directed DNA/RNA polymerase mu isoform 1 [Homo sapiens].
ACCESSION   NP_037416 XP_498189
VERSION     NP_037416.1
DBSOURCE    REFSEQ: accession NM_013284.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Guo,M., Wang,Y., Tang,Y., Chen,Z., Hou,J., Dai,J., Wang,Y.,
            Wang,L., Xu,H., Tian,B., Hua,Y. and Zhao,Y.
  TITLE     Mechanism of genome instability mediated by human DNA polymerase mu
            misincorporation
  JOURNAL   Nat Commun 12 (1), 3759 (2021)
   PUBMED   34145298
  REMARK    GeneRIF: Mechanism of genome instability mediated by human DNA
            polymerase mu misincorporation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Shilkin,E.S., Gromova,A.S., Smal,M.P. and Makarova,A.V.
  TITLE     DNA Polymerase and dRP-lyase activities of polymorphic variants of
            human Pol iota
  JOURNAL   Biochem J 478 (7), 1399-1412 (2021)
   PUBMED   33600564
  REMARK    GeneRIF: DNA Polymerase and dRP-lyase activities of polymorphic
            variants of human Pol iota.
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Kaminski,A.M., Bebenek,K., Pedersen,L.C. and Kunkel,T.A.
  TITLE     DNA polymerase mu: An inflexible scaffold for substrate flexibility
  JOURNAL   DNA Repair (Amst) 93, 102932 (2020)
   PUBMED   33087269
  REMARK    GeneRIF: DNA polymerase mu: An inflexible scaffold for substrate
            flexibility.
            Review article
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Caglayan,M. and Wilson,S.H.
  TITLE     Pol mu dGTP mismatch insertion opposite T coupled with ligation
            reveals promutagenic DNA repair intermediate
  JOURNAL   Nat Commun 9 (1), 4213 (2018)
   PUBMED   30310068
  REMARK    GeneRIF: pol mu-mediated deoxyguanosine triphosphate mismatch
            insertion opposite template base T coupled with ligation could be a
            feature of mutation prone nonhomologous end joining during
            double-strand break repair.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Sastre-Moreno,G., Pryor,J.M., Diaz-Talavera,A., Ruiz,J.F.,
            Ramsden,D.A. and Blanco,L.
  TITLE     Polmu tumor variants decrease the efficiency and accuracy of NHEJ
  JOURNAL   Nucleic Acids Res 45 (17), 10018-10031 (2017)
   PUBMED   28973441
  REMARK    GeneRIF: Polmu point mutations affecting 2 conserved adjacent
            residues located in the 8 kDa domain, G174S and R175H, limit the
            efficiency of accurate NHEJ by Polmu in vitro and in vivo due to
            decreased template dependency during NHEJ, which renders the
            error-rate of the mutants higher due to the ability of Polmu to
            randomly incorporate nucleotides at DSBs.
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Duvauchelle,J.B., Blanco,L., Fuchs,R.P. and Cordonnier,A.M.
  TITLE     Human DNA polymerase mu (Pol mu) exhibits an unusual replication
            slippage ability at AAF lesion
  JOURNAL   Nucleic Acids Res 30 (9), 2061-2067 (2002)
   PUBMED   11972346
  REMARK    GeneRIF: DNA polymerase mu performs DNA synthesis at a AAF lesion
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Shimazaki,N., Fujita,K. and Koiwai,O.
  TITLE     [Expression and function of terminal deoxynucleotidyl-transferase
            and discovery of novel DNA polymerase mu]
  JOURNAL   Seikagaku 74 (3), 227-232 (2002)
   PUBMED   11974916
  REMARK    GeneRIF: role in DNA repair
            Review article
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Haracska,L., Johnson,R.E., Unk,I., Phillips,B.B., Hurwitz,J.,
            Prakash,L. and Prakash,S.
  TITLE     Targeting of human DNA polymerase iota to the replication machinery
            via interaction with PCNA
  JOURNAL   Proc Natl Acad Sci U S A 98 (25), 14256-14261 (2001)
   PUBMED   11724965
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Aoufouchi,S., Flatter,E., Dahan,A., Faili,A., Bertocci,B.,
            Storck,S., Delbos,F., Cocea,L., Gupta,N., Weill,J.C. and
            Reynaud,C.A.
  TITLE     Two novel human and mouse DNA polymerases of the polX family
  JOURNAL   Nucleic Acids Res 28 (18), 3684-3693 (2000)
   PUBMED   10982892
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Dominguez,O., Ruiz,J.F., Lain de Lera,T., Garcia-Diaz,M.,
            Gonzalez,M.A., Kirchhoff,T., Martinez-A,C., Bernad,A. and Blanco,L.
  TITLE     DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA
            mutator in eukaryotic cells
  JOURNAL   EMBO J 19 (7), 1731-1742 (2000)
   PUBMED   10747040
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AU309799.1, AF176097.1 and AA917987.1.
            
            On Aug 30, 2004 this sequence version replaced XP_498189.1.
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ131891.2, AF176097.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242248.10/ ENSP00000242248.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..494
                     /product="DNA-directed DNA/RNA polymerase mu isoform 1"
                     /EC_number="2.7.7.7"
                     /note="polymerase (DNA-directed), mu; Pol iota; polymerase
                     (DNA) mu; DNA-directed DNA/RNA polymerase mu; terminal
                     transferase"
                     /calculated_mol_wt=54685
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP87.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NP87.1)"
     Region          26..123
                     /region_name="BRCT_polymerase_mu"
                     /note="BRCT domain of DNA-directed DNA/RNA polymerase mu
                     (polymerase mu) and similar proteins; cd18442"
                     /db_xref="CDD:349395"
     Region          156..492
                     /region_name="NT_POLXc"
                     /note="Nucleotidyltransferase (NT) domain of family X DNA
                     Polymerases; cd00141"
                     /db_xref="CDD:143386"
     Site            order(241,243,245..250,253,275,289,319..320,323,325,
                     327..330,332,387,389,416,418,433..438,441,458)
                     /site_type="active"
                     /db_xref="CDD:143386"
     Site            order(241,243,245..250,253,275,319,323,329..330,332,387,
                     389,416,418,433..438,441)
                     /site_type="other"
                     /note="primer binding site [nucleotide binding]"
                     /db_xref="CDD:143386"
     Site            order(289,319..320,323,325,327..330,332,387,418,433..436,
                     438,441,458)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143386"
     Region          323..332
                     /region_name="Involved in ssDNA binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP87.1)"
     Site            order(330,332,418)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143386"
     Site            433
                     /site_type="other"
                     /note="Responsible for the low discrimination between dNTP
                     and rNTP; propagated from UniProtKB/Swiss-Prot (Q9NP87.1)"
     CDS             1..494
                     /gene="POLM"
                     /gene_synonym="Pol Mu; Tdt-N"
                     /coded_by="NM_013284.4:93..1577"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34625.1"
                     /db_xref="GeneID:27434"
                     /db_xref="HGNC:HGNC:9185"
                     /db_xref="MIM:606344"
ORIGIN      
        1 mlpkrrrarv gspsgdaass tppstrfpgv aiylveprmg rsrrafltgl arskgfrvld
       61 acsseathvv meetsaeeav swqerrmaaa ppgctppall diswlteslg agqpvpvecr
      121 hrlevagprk gplspawmpa yacqrptplt hhntglseal eilaeaagfe gsegrlltfc
      181 raasvlkalp spvttlsqlq glphfgehss rvvqellehg vceevervrr seryqtmklf
      241 tqifgvgvkt adrwyreglr tlddlreqpq kltqqqkagl qhhqdlstpv lrsdvdalqq
      301 vveeavgqal pgatvtltgg frrgklqghd vdflithpke gqeagllprv mcrlqdqgli
      361 lyhqhqhscc esptrlaqqs hmdafersfc ifrlpqppga avggstrpcp swkavrvdlv
      421 vapvsqfpfa llgwtgsklf qrelrrfsrk ekglwlnshg lfdpeqktff qaaseedifr
      481 hlgleylppe qrna
//
LOCUS       NP_004761                911 aa            linear   PRI 27-APR-2025
DEFINITION  potassium voltage-gated channel subfamily B member 2 [Homo
            sapiens].
ACCESSION   NP_004761
VERSION     NP_004761.2
DBSOURCE    REFSEQ: accession NM_004770.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Li,Z., Dong,W., Zhang,X., Lu,J.M., Mei,Y.A. and Hu,C.
  TITLE     Protein Kinase C Controls the Excitability of Cortical Pyramidal
            Neurons by Regulating Kv2.2 Channel Activity
  JOURNAL   Neurosci Bull 38 (2), 135-148 (2022)
   PUBMED   34542799
  REMARK    GeneRIF: Protein Kinase C Controls the Excitability of Cortical
            Pyramidal Neurons by Regulating Kv2.2 Channel Activity.
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Maverick,E.E., Leek,A.N. and Tamkun,M.M.
  TITLE     Kv2 channel-AMIGO beta-subunit assembly modulates both channel
            function and cell adhesion molecule surface trafficking
  JOURNAL   J Cell Sci 134 (12) (2021)
   PUBMED   34137443
  REMARK    GeneRIF: Kv2 channel-AMIGO beta-subunit assembly modulates both
            channel function and cell adhesion molecule surface trafficking.
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Di Mattia,T., Martinet,A., Ikhlef,S., McEwen,A.G., Nomine,Y.,
            Wendling,C., Poussin-Courmontagne,P., Voilquin,L., Eberling,P.,
            Ruffenach,F., Cavarelli,J., Slee,J., Levine,T.P., Drin,G.,
            Tomasetto,C. and Alpy,F.
  TITLE     FFAT motif phosphorylation controls formation and lipid transfer
            function of inter-organelle contacts
  JOURNAL   EMBO J 39 (23), e104369 (2020)
   PUBMED   33124732
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Fu,J., Dai,X., Plummer,G., Suzuki,K., Bautista,A., Githaka,J.M.,
            Senior,L., Jensen,M., Greitzer-Antes,D., Manning Fox,J.E.,
            Gaisano,H.Y., Newgard,C.B., Touret,N. and MacDonald,P.E.
  TITLE     Kv2.1 Clustering Contributes to Insulin Exocytosis and Rescues
            Human beta-Cell Dysfunction
  JOURNAL   Diabetes 66 (7), 1890-1900 (2017)
   PUBMED   28607108
  REMARK    GeneRIF: Kv2.1, but not Kv2.2 (KCNB2), forms clusters of 6-12
            tetrameric channels at the plasma membrane and facilitates insulin
            exocytosis
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Naranjo,D., Moldenhauer,H., Pincuntureo,M. and Diaz-Franulic,I.
  TITLE     Pore size matters for potassium channel conductance
  JOURNAL   J Gen Physiol 148 (4), 277-291 (2016)
   PUBMED   27619418
  REMARK    Review article
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Gutman,G.A., Chandy,K.G., Grissmer,S., Lazdunski,M., McKinnon,D.,
            Pardo,L.A., Robertson,G.A., Rudy,B., Sanguinetti,M.C., Stuhmer,W.
            and Wang,X.
  TITLE     International Union of Pharmacology. LIII. Nomenclature and
            molecular relationships of voltage-gated potassium channels
  JOURNAL   Pharmacol Rev 57 (4), 473-508 (2005)
   PUBMED   16382104
  REMARK    Review article
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Yan,L., Figueroa,D.J., Austin,C.P., Liu,Y., Bugianesi,R.M.,
            Slaughter,R.S., Kaczorowski,G.J. and Kohler,M.G.
  TITLE     Expression of voltage-gated potassium channels in human and rhesus
            pancreatic islets
  JOURNAL   Diabetes 53 (3), 597-607 (2004)
   PUBMED   14988243
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Schmalz,F., Kinsella,J., Koh,S.D., Vogalis,F., Schneider,A.,
            Flynn,E.R., Kenyon,J.L. and Horowitz,B.
  TITLE     Molecular identification of a component of delayed rectifier
            current in gastrointestinal smooth muscles
  JOURNAL   Am J Physiol 274 (5), G901-G911 (1998)
   PUBMED   9612272
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Hugnot,J.P., Salinas,M., Lesage,F., Guillemare,E., de Weille,J.,
            Heurteaux,C., Mattei,M.G. and Lazdunski,M.
  TITLE     Kv8.1, a new neuronal potassium channel subunit with specific
            inhibitory properties towards Shab and Shaw channels
  JOURNAL   EMBO J 15 (13), 3322-3331 (1996)
   PUBMED   8670833
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011131.6 and AC022893.6.
            
            On Dec 31, 2002 this sequence version replaced NP_004761.1.
            
            Summary: Voltage-gated potassium (Kv) channels represent the most
            complex class of voltage-gated ion channels from both functional
            and structural standpoints. Their diverse functions include
            regulating neurotransmitter release, heart rate, insulin secretion,
            neuronal excitability, epithelial electrolyte transport, smooth
            muscle contraction, and cell volume. Four sequence-related
            potassium channel genes - shaker, shaw, shab, and shal - have been
            identified in Drosophila, and each has been shown to have human
            homolog(s). This gene encodes a member of the potassium channel,
            voltage-gated, shab-related subfamily. This member is a delayed
            rectifier potassium channel. The gene is expressed in
            gastrointestinal smooth muscle cells. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF338730.1, SRR1660803.155026.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000523207.2/ ENSP00000430846.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..911
                     /product="potassium voltage-gated channel subfamily B
                     member 2"
                     /note="delayed rectifier potassium channel protein;
                     potassium channel Kv2.2; voltage-gated potassium channel
                     subunit Kv2.2; potassium voltage-gated channel,
                     Shab-related subfamily, member 2; potassium channel,
                     voltage gated Shab related subfamily B, member 2"
                     /calculated_mol_wt=102432
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Region          19..145
                     /region_name="BTB_POZ_KCNB2"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     voltage-gated channel subfamily B member 2 (KCNB2);
                     cd18412"
                     /db_xref="CDD:349719"
     Site            order(40,42..49,52,88,90..91,94,97,101,104,107,109,
                     117..118,121)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349719"
     Site            191..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Region          192..428
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            233..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Site            266..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Site            287
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92953.2)"
     Site            297..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Site            333..354
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Region          381..386
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Site            396..424
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63099; propagated from
                     UniProtKB/Swiss-Prot (Q92953.2)"
     Region          471..759
                     /region_name="Kv2channel"
                     /note="Kv2 voltage-gated K+ channel; pfam03521"
                     /db_xref="CDD:397541"
     Region          503..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Region          549..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Region          605..611
                     /region_name="FFAT. /evidence=ECO:0000269|PubMed:33124732"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:33124732; propagated from
                     UniProtKB/Swiss-Prot (Q92953.2)"
     Region          637..665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Region          685..739
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Region          760..865
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     Region          892..911
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92953.2)"
     CDS             1..911
                     /gene="KCNB2"
                     /gene_synonym="KV2.2"
                     /coded_by="NM_004770.3:755..3490"
                     /note="Kv2.2"
                     /db_xref="CCDS:CCDS6209.1"
                     /db_xref="GeneID:9312"
                     /db_xref="HGNC:HGNC:6232"
                     /db_xref="MIM:607738"
ORIGIN      
        1 maekappgln rktsrstlsl ppepvdiirs ktcsrrvkin vgglnhevlw rtldrlprtr
       61 lgklrdcnth esllevcddy nlneneyffd rhpgaftsil nfyrtgklhm meemcalsfg
      121 qeldywgide iylesccqar yhqkkeqmne elrreaetmr eregeefdnt ccpdkrkklw
      181 dllekpnssv aakilaivsi lfivlstial slntlpelqe tdefgqlndn rqlahveavc
      241 iawftmeyll rflsspnkwk ffkgplnvid llailpyyvt ifltesnksv lqfqnvrrvv
      301 qifrimrilr ilklarhstg lqslgftlrr synelgllil flamgimifs slvffaekde
      361 datkftsipa sfwwatitmt tvgygdiypk tllgkivggl cciagvlvia lpipiivnnf
      421 sefykeqkrq ekaikrreal erakrngsiv smnlkdafar smelidvave kagesantkd
      481 saddnhlsps rwkwarkals etssnksfen kyqevsqkds heqlnntsss spqhlsaqkl
      541 emlyneitkt qphshpnpdc qekperpsay eeeiemeevv cpqeqlavaq tevivdmkst
      601 ssidsftsca tdftetersp lpppsashlq mkfptdlpgt eehqrargpp fltlsrekgp
      661 aardgtleya pvditvnlda sgsqcglhsp lqsdnatdsp ksslkgsnpl ksrslkvnfk
      721 enrgsapqtp pstarplpvt tadfslttpq histilleet psqgdrpllg tevsapcqgp
      781 skglsprfpk qklfpfssre rrsfteidtg ddedflelpg areekqvdss pncfadkpsd
      841 grdplreegs vgssspqdtg hncrqdiyha vsevkkdssq egckmenhlf apeihsnpgd
      901 tgycptrets m
//
LOCUS       NP_004416                540 aa            linear   PRI 27-APR-2025
DEFINITION  extracellular matrix protein 1 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_004416
VERSION     NP_004416.2
DBSOURCE    REFSEQ: accession NM_004425.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Sun,C., Fan,W., Basha,S., Tian,T., Jin-Smith,B., Barkin,J., Xie,H.,
            Zhou,J., Yin,X.M., Ling,C., Sun,B., Petersen,B. and Pi,L.
  TITLE     Extracellular matrix protein 1 binds to connective tissue growth
            factor against liver fibrosis and ductular reaction
  JOURNAL   Hepatol Commun 8 (11), e0564 (2024)
   PUBMED   39470347
  REMARK    GeneRIF: Extracellular matrix protein 1 binds to connective tissue
            growth factor against liver fibrosis and ductular reaction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Tasdelen,E., Sezer,A. and An,I.
  TITLE     A founder deletion in ECM1 of 1163 bp causes lipoid proteinosis in
            the southeast region of Turkiye
  JOURNAL   Am J Med Genet A 194 (10), e63782 (2024)
   PUBMED   38842389
  REMARK    GeneRIF: A founder deletion in ECM1 of 1163 bp causes lipoid
            proteinosis in the southeast region of Turkiye.
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Yu,Y., Lyu,C., Li,X., Yang,L., Wang,J., Li,H., Xin,Z., Xu,X.,
            Ren,C. and Yang,G.
  TITLE     Remodeling of tumor microenvironment by extracellular matrix
            protein 1a differentially regulates ovarian cancer metastasis
  JOURNAL   Cancer Lett 596, 217022 (2024)
   PUBMED   38849014
  REMARK    GeneRIF: Remodeling of tumor microenvironment by extracellular
            matrix protein 1a differentially regulates ovarian cancer
            metastasis.
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Shinomiya,Y., Kouchi,Y., Harada-Kagitani,S., Ishige,T., Takano,S.,
            Ohtsuka,M., Ikeda,J.I. and Kishimoto,T.
  TITLE     ECM1 and KRT6A are involved in tumor progression and
            chemoresistance in the effect of dexamethasone on pancreatic cancer
  JOURNAL   Cancer Sci 115 (6), 1948-1963 (2024)
   PUBMED   38613239
  REMARK    GeneRIF: ECM1 and KRT6A are involved in tumor progression and
            chemoresistance in the effect of dexamethasone on pancreatic
            cancer.
REFERENCE   5  (residues 1 to 540)
  AUTHORS   Deckers,M.M., Smits,P., Karperien,M., Ni,J., Tylzanowski,P.,
            Feng,P., Parmelee,D., Zhang,J., Bouffard,E., Gentz,R., Lowik,C.W.
            and Merregaert,J.
  TITLE     Recombinant human extracellular matrix protein 1 inhibits alkaline
            phosphatase activity and mineralization of mouse embryonic
            metatarsals in vitro
  JOURNAL   Bone 28 (1), 14-20 (2001)
   PUBMED   11165938
REFERENCE   6  (residues 1 to 540)
  AUTHORS   Smits,P., Poumay,Y., Karperien,M., Tylzanowski,P., Wauters,J.,
            Huylebroeck,D., Ponec,M. and Merregaert,J.
  TITLE     Differentiation-dependent alternative splicing and expression of
            the extracellular matrix protein 1 gene in human keratinocytes
  JOURNAL   J Invest Dermatol 114 (4), 718-724 (2000)
   PUBMED   10733679
REFERENCE   7  (residues 1 to 540)
  AUTHORS   Smits,P., Ni,J., Feng,P., Wauters,J., Van Hul,W., Boutaibi,M.E.,
            Dillon,P.J. and Merregaert,J.
  TITLE     The human extracellular matrix gene 1 (ECM1): genomic structure,
            cDNA cloning, expression pattern, and chromosomal localization
  JOURNAL   Genomics 45 (3), 487-495 (1997)
   PUBMED   9367673
REFERENCE   8  (residues 1 to 540)
  AUTHORS   Johnson,M.R., Wilkin,D.J., Vos,H.L., Ortiz de Luna,R.I.,
            Dehejia,A.M., Polymeropoulos,M.H. and Francomano,C.A.
  TITLE     Characterization of the human extracellular matrix protein 1 gene
            on chromosome 1q21
  JOURNAL   Matrix Biol 16 (5), 289-292 (1997)
   PUBMED   9501329
REFERENCE   9  (residues 1 to 540)
  AUTHORS   Vahidnezhad,H., Youssefian,L. and Uitto,J.
  TITLE     Lipoid Proteinosis
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26803878
REFERENCE   10 (residues 1 to 540)
  AUTHORS   Viliavin,G.D., Panchenko,K.P., Nishanov,F. and Budaev,K.D.
  TITLE     [Acid-producing function of the stomach in pyloric ulcers]
  JOURNAL   Sov Med (12), 43-45 (1977)
   PUBMED   601588
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA963826.1, U68186.1,
            AL356356.17 and CA413352.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 24, 2009 this sequence version replaced NP_004416.1.
            
            Summary: This gene encodes a soluble protein that is involved in
            endochondral bone formation, angiogenesis, and tumor biology. It
            also interacts with a variety of extracellular and structural
            proteins, contributing to the maintenance of skin integrity and
            homeostasis. Mutations in this gene are associated with lipoid
            proteinosis disorder (also known as hyalinosis cutis et mucosae or
            Urbach-Wiethe disease) that is characterized by generalized
            thickening of skin, mucosae and certain viscera. Alternatively
            spliced transcript variants encoding distinct isoforms have been
            described for this gene. [provided by RefSeq, Feb 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005374.1, AK292435.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369047.9/ ENSP00000358043.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..540
                     /product="extracellular matrix protein 1 isoform 1
                     precursor"
                     /note="secretory component p85; testicular tissue protein
                     Li 61"
                     /calculated_mol_wt=58812
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1880
     mat_peptide     20..540
                     /product="extracellular matrix protein 1 isoform 1"
                     /calculated_mol_wt=58812
     Region          41..540
                     /region_name="ECM1"
                     /note="Extracellular matrix protein 1 (ECM1); pfam05782"
                     /db_xref="CDD:461739"
     Region          41..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16610.2)"
     Region          120..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16610.2)"
     Region          150..405
                     /region_name="2 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16610.2)"
     Site            354
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16610.2)"
     Site            444
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q16610.2)"
     Region          515..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16610.2)"
     Site            530
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16610.2)"
     CDS             1..540
                     /gene="ECM1"
                     /gene_synonym="URBWD"
                     /coded_by="NM_004425.4:102..1724"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS953.1"
                     /db_xref="GeneID:1893"
                     /db_xref="HGNC:HGNC:3153"
                     /db_xref="MIM:602201"
ORIGIN      
        1 mgttaraalv ltylavasaa seggftatgq rqlrpehfqe vgyaappspp lsrslpmdhp
       61 dssqhgppfe gqsqvqppps qeatplqqek llpaqlpaek evgpplpqea vplqkelpsl
      121 qhpneqkegt papfgdqshp epeswnaaqh cqqdrsqggw ghrldgfppg rpspdnlnqi
      181 clpnrqhvvy gpwnlpqssy shltrqgetl nfleigysrc chcrshtnrl ecaklvweea
      241 msrfceaefs vktrphwcct rqgearfscf qeeapqphyq lracpshqpd issglelpfp
      301 pgvptldnik nichlrrfrs vprnlpatdp lqrellaliq lerefqrccr qgnnhtctwk
      361 awedtldkyc dreyavkthh hlccrhppsp trdecfarra pypnydrdil tidigrvtpn
      421 lmghlcgnqr vltkhkhipg lihnmtarcc dlpfpeqacc aeeekltfin dlcgprrniw
      481 rdpalccyls pgdeqvncfn inylrnvalv sgdtenakgq geqgstggtn isstsepkee
//
LOCUS       NP_690601                300 aa            linear   PRI 27-APR-2025
DEFINITION  actin-related protein 2/3 complex subunit 2 [Homo sapiens].
ACCESSION   NP_690601
VERSION     NP_690601.1
DBSOURCE    REFSEQ: accession NM_152862.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Poh,J., Ponsford,A.H., Boyd,J., Woodsmith,J., Stelzl,U., Wanker,E.,
            Harper,N., MacEwan,D. and Sanderson,C.M.
  TITLE     A functionally defined high-density NRF2 interactome reveals new
            conditional regulators of ARE transactivation
  JOURNAL   Redox Biol 37, 101686 (2020)
   PUBMED   32911434
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Skruber,K., Warp,P.V., Shklyarov,R., Thomas,J.D., Swanson,M.S.,
            Henty-Ridilla,J.L., Read,T.A. and Vitriol,E.A.
  TITLE     Arp2/3 and Mena/VASP Require Profilin 1 for Actin Network Assembly
            at the Leading Edge
  JOURNAL   Curr Biol 30 (14), 2651-2664 (2020)
   PUBMED   32470361
  REMARK    GeneRIF: Arp2/3 and Mena/VASP Require Profilin 1 for Actin Network
            Assembly at the Leading Edge.
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Al-Zeer,M.A., Dutkiewicz,M., von Hacht,A., Kreuzmann,D., Rohrs,V.
            and Kurreck,J.
  TITLE     Alternatively spliced variants of the 5'-UTR of the ARPC2 mRNA
            regulate translation by an internal ribosome entry site (IRES)
            harboring a guanine-quadruplex motif
  JOURNAL   RNA Biol 16 (11), 1622-1632 (2019)
   PUBMED   31387452
  REMARK    GeneRIF: Study provides evidence that the 5'-UTR1 of ARPC2 has
            internal ribosome entry site activity and regulates translation
            during stressful cellular conditions such as high cell density.
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Cheng,Z., Wei,W., Wu,Z., Wang,J., Ding,X., Sheng,Y., Han,Y. and
            Wu,Q.
  TITLE     ARPC2 promotes breast cancer proliferation and metastasis
  JOURNAL   Oncol Rep 41 (6), 3189-3200 (2019)
   PUBMED   31002363
  REMARK    GeneRIF: These results collectively indicated that ARPC2 promoted
            the tumorigenesis of breast carcinoma and the initiation of
            epithelialmesenchymal transition. Therefore, ARPC2 was revealed to
            be a potential therapeutic target in patients with breast cancer
            (BrCa) .
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Chen,P., Yue,X., Xiong,H., Lu,X. and Ji,Z.
  TITLE     RBM3 upregulates ARPC2 by binding the 3'UTR and contributes to
            breast cancer progression
  JOURNAL   Int J Oncol 54 (4), 1387-1397 (2019)
   PUBMED   30720048
  REMARK    GeneRIF: Results find that ARPC2 expression is upregulated in
            breast cancer tissues and cell lines. ARPC2 promotes the
            proliferation and metastasis of human breast cancer cells. ARPC2 is
            regulated by RBM2 in a posttranscriptional 3'UTRbinding manner.
            Also, ARPC2 plays an oncogenic role and mediates the promoting role
            of RBM3 in the proliferation and metastasis of human breast cancer
            cells.
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Robinson,R.C., Turbedsky,K., Kaiser,D.A., Marchand,J.B.,
            Higgs,H.N., Choe,S. and Pollard,T.D.
  TITLE     Crystal structure of Arp2/3 complex
  JOURNAL   Science 294 (5547), 1679-1684 (2001)
   PUBMED   11721045
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Zhao,X., Yang,Z., Qian,M. and Zhu,X.
  TITLE     Interactions among subunits of human Arp2/3 complex: p20-Arc as the
            hub
  JOURNAL   Biochem Biophys Res Commun 280 (2), 513-517 (2001)
   PUBMED   11162547
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Naar,A.M., Beaurang,P.A., Zhou,S., Abraham,S., Solomon,W. and
            Tjian,R.
  TITLE     Composite co-activator ARC mediates chromatin-directed
            transcriptional activation
  JOURNAL   Nature 398 (6730), 828-832 (1999)
   PUBMED   10235267
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Machesky,L.M., Reeves,E., Wientjes,F., Mattheyse,F.J., Grogan,A.,
            Totty,N.F., Burlingame,A.L., Hsuan,J.J. and Segal,A.W.
  TITLE     Mammalian actin-related protein 2/3 complex localizes to regions of
            lamellipodial protrusion and is composed of evolutionarily
            conserved proteins
  JOURNAL   Biochem J 328 (Pt 1) (Pt 1), 105-112 (1997)
   PUBMED   9359840
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Welch,M.D., DePace,A.H., Verma,S., Iwamatsu,A. and Mitchison,T.J.
  TITLE     The human Arp2/3 complex is composed of evolutionarily conserved
            subunits and is localized to cellular regions of dynamic actin
            filament assembly
  JOURNAL   J Cell Biol 138 (2), 375-384 (1997)
   PUBMED   9230079
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG282181.1, AK290268.1 and
            CN291458.1.
            
            Summary: This gene encodes one of seven subunits of the human
            Arp2/3 protein complex. The Arp2/3 protein complex has been
            implicated in the control of actin polymerization in cells and has
            been conserved through evolution. The exact role of the protein
            encoded by this gene, the p34 subunit, has yet to be determined.
            Two alternatively spliced variants have been characterized to date.
            Additional alternatively spliced variants have been described but
            their full length nature has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.750238.1,
                                           SRR5189652.54299.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315717.10/ ENSP00000327137.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..300
                     /product="actin-related protein 2/3 complex subunit 2"
                     /note="ARP2/3 protein complex subunit 34; arp2/3 complex
                     34 kDa subunit; actin related protein 2/3 complex, subunit
                     2, 34kDa; testis tissue sperm-binding protein Li 53e"
                     /calculated_mol_wt=34202
     Region          57..284
                     /region_name="P34-Arc"
                     /note="Arp2/3 complex, 34 kD subunit p34-Arc; pfam04045"
                     /db_xref="CDD:461144"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15144.1)"
     Site            295
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15144.1)"
     CDS             1..300
                     /gene="ARPC2"
                     /gene_synonym="ARC34; p34-Arc; PNAS-139; PRO2446"
                     /coded_by="NM_152862.3:75..977"
                     /db_xref="CCDS:CCDS2410.1"
                     /db_xref="GeneID:10109"
                     /db_xref="HGNC:HGNC:705"
                     /db_xref="MIM:604224"
ORIGIN      
        1 millevnnri ieetlalkfe naaagnkpea vevtfadfdg vlyhisnpng dktkvmvsis
       61 lkfykelqah gadellkrvy gsflvnpesg ynvsllydle nlpaskdsiv hqagmlkrnc
      121 fasvfekyfq fqeegkegen ravihyrdde tmyveskkdr vtvvfstvfk ddddvvigkv
      181 fmqefkegrr ashtapqvlf shrepplelk dtdaavgdni gyitfvlfpr htnasardnt
      241 inlihtfrdy lhyhikcska yihtrmrakt sdflkvlnra rpdaekkemk titgktfssr
//
LOCUS       NP_001355752             956 aa            linear   ROD 27-APR-2025
DEFINITION  cation channel sperm-associated auxiliary subunit epsilon precursor
            [Mus musculus].
ACCESSION   NP_001355752 XP_006497146
VERSION     NP_001355752.1
DBSOURCE    REFSEQ: accession NM_001368823.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 956)
  AUTHORS   Lin,S., Ke,M., Zhang,Y., Yan,Z. and Wu,J.
  TITLE     Structure of a mammalian sperm cation channel complex
  JOURNAL   Nature 595 (7869), 746-750 (2021)
   PUBMED   34225353
REFERENCE   2  (residues 1 to 956)
  AUTHORS   Chung,J.J., Miki,K., Kim,D., Shim,S.H., Shi,H.F., Hwang,J.Y.,
            Cai,X., Iseri,Y., Zhuang,X. and Clapham,D.E.
  TITLE     CatSperzeta regulates the structural continuity of sperm Ca2+
            signaling domains and is required for normal fertility
  JOURNAL   Elife 6, e23082 (2017)
   PUBMED   28226241
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC157787.6 and AC163217.9.
            
            On Feb 28, 2019 this sequence version replaced XP_006497146.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849384
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            inferred exon combination        :: based on alignments, homology
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..956
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 82.82 cM"
     Protein         1..956
                     /product="cation channel sperm-associated auxiliary
                     subunit epsilon precursor"
                     /note="catSperepsilon; catSper-epsilon; C1orf101-like
                     protein; cation channel sperm-associated protein subunit
                     epsilon; cation channel sperm-associated auxiliary subunit
                     epsilon"
                     /calculated_mol_wt=108687
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2148
     Region          <690..955
                     /region_name="CATSPERD"
                     /note="Cation channel sperm-associated protein subunit
                     delta; pfam15020"
                     /db_xref="CDD:464451"
     CDS             1..956
                     /gene="Catspere1"
                     /gene_synonym="Catspere; EG631584; Gm7068"
                     /coded_by="NM_001368823.1:132..3002"
                     /db_xref="CCDS:CCDS87930.1"
                     /db_xref="GeneID:631584"
                     /db_xref="MGI:MGI:3647531"
ORIGIN      
        1 mlarqvvaal llwlsccvsa lwryyinsqd ysifstrssi kleyegnsfv swkipesckv
       61 enttspkttl hckragihti kpiagnqeve rhltvdnsyi cylwyftvvd vyynlsqivt
      121 iwvydpesas teeliwtakk pslssrvltk qmntlgqrpf iftvekrlty hpgpltsegt
      181 wvihlpmssd diakvirgnk vafqdcfian lyfmltypmt iiseppgyep ltvppgsplm
      241 lswdtcistf allatdqetf qtndsfqtwt rvrappgils daqrhslrdv iifdqgtlfl
      301 vdgtvylrte deftkldesr gisetgilgf skrrwcqiry lyklaskksi liawskttvy
      361 agyatfrfvt ltdtaklkdf lklpqtdtle vmsveylwhp leaavllshc svcttntrni
      421 riviysaifq twtlqdfelq lpkeailefr flysampdii mwdqhhvyys yknftvvgti
      481 stpsgetnls slsqgskihq vltdrignvv vkmennvmfy ikaditeavi lhtwvnttak
      541 tvvlfdksfe vcilyynenl dekyqlqtqp yplilelqsi nkdlgdwcpy lafqhnihsq
      601 fyhmdkgesl tiwsqivype nrglyivveh ygssvmtwtq nleyeiasgf ctktmitrff
      661 qttnyelvdn yyqlqkentg lmllqfrpse fsrtcltakp vfeidvgcds skyimvrgfn
      721 ksrcqrrdfs yvidkellre slsdnlkvry dvakygcplt lelgqmfqpi velydengfi
      781 kivdanfilw eihgrndytf nstmeqngci neaqtwdsmi eenpdipldd vwgpqnyrpc
      841 fsyaigkpgd lgqpyeilny snknhikwpm tyagmyvyrl kildpnysfc nlttifaies
      901 lgmiprssvy lvaalifvlm ltfisilvls yfwylkiyrq fiieplhkrp akqkkn
//
LOCUS       NP_001348629             558 aa            linear   ROD 27-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 16 [Mus musculus].
ACCESSION   NP_001348629 XP_006515435
VERSION     NP_001348629.1
DBSOURCE    REFSEQ: accession NM_001361700.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Peluso,G., Tian,E., Abusleme,L., Munemasa,T., Mukaibo,T. and Ten
            Hagen,K.G.
  TITLE     Loss of the disease-associated glycosyltransferase Galnt3 alters
            Muc10 glycosylation and the composition of the oral microbiome
  JOURNAL   J Biol Chem 295 (5), 1411-1425 (2020)
   PUBMED   31882545
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Tian,E., Wang,S., Zhang,L., Zhang,Y., Malicdan,M.C., Mao,Y.,
            Christoffersen,C., Tabak,L.A., Schjoldager,K.T. and Ten Hagen,K.G.
  TITLE     Galnt11 regulates kidney function by glycosylating the endocytosis
            receptor megalin to modulate ligand binding
  JOURNAL   Proc Natl Acad Sci U S A 116 (50), 25196-25202 (2019)
   PUBMED   31740596
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Tian,E., Stevens,S.R., Guan,Y., Springer,D.A., Anderson,S.A.,
            Starost,M.F., Patel,V., Ten Hagen,K.G. and Tabak,L.A.
  TITLE     Galnt1 is required for normal heart valve development and cardiac
            function
  JOURNAL   PLoS One 10 (1), e0115861 (2015)
   PUBMED   25615642
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Tian,E., Hoffman,M.P. and Ten Hagen,K.G.
  TITLE     O-glycosylation modulates integrin and FGF signalling by
            influencing the secretion of basement membrane components
  JOURNAL   Nat Commun 3, 869 (2012)
   PUBMED   22643896
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC163282.3 and AC125361.4.
            
            On Mar 29, 2018 this sequence version replaced XP_006515435.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK173105.1, SRR6116558.97873.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 36.79 cM"
     Protein         1..558
                     /product="polypeptide N-acetylgalactosaminyltransferase
                     16"
                     /EC_number="2.4.1.41"
                     /note="putative polypeptide
                     N-acetylgalactosaminyltransferase-like protein 1;
                     galNAc-T-like protein 1; pp-GaNTase-like protein 1;
                     polypeptide GalNAc transferase-like protein 1; protein-UDP
                     acetylgalactosaminyltransferase-like protein 1;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 16;
                     UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase-like protein 1;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase-like 1; polypeptide
                     GalNAc transferase 16"
                     /calculated_mol_wt=62744
     Site            7..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ61.2)"
     Region          34..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ61.2)"
     Region          122..227
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ61.2)"
     Region          126..420
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(130..132,134,163,188,191,195,211..213,294..295,
                     317..318,320,345,348,353)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(211,213,345)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          286..348
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ61.2)"
     Region          426..557
                     /region_name="beta-trefoil_Ricin_GALNT16"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide N-acetylgalactosaminyltransferase 16
                     (GALNT16) and similar proteins; cd23479"
                     /db_xref="CDD:467357"
     Site            order(443..445,456,458,461,470..471)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467357"
     Site            order(488..491,502,504,507,512..513)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467357"
     Site            order(532..535,539,541,544,549..550)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467357"
     CDS             1..558
                     /gene="Galnt16"
                     /gene_synonym="5730405L21Rik; galNAc-T16; Galntl1;
                     mpp-GalNAc-T16"
                     /coded_by="NM_001361700.1:292..1968"
                     /db_xref="CCDS:CCDS36482.1"
                     /db_xref="GeneID:108760"
                     /db_xref="MGI:MGI:1917754"
ORIGIN      
        1 mrkiranaia iltvawilgt fyylwqdnra haasssgrga qraggrpeql redrtipliv
       61 tgtpskgfde kaylsakqlk pgedpyrqha fnqlesdkls sdrpirdtrh yscpslsyss
      121 dlpatsviit fhnearstll rtvksvlnrt pasliqeiil vddfssdped cllltripkv
      181 kclrndkreg lirsrvrgad vagatvltfl dshcevnvew lqpmlqrvme dhtrvvspii
      241 dvisldnfay laasadlrgg fdwslhfkwe qipleqkmtr tdptkpirtp viaggifvid
      301 kswfnhlgky daqmdiwgge nfelsfrvwm cggsleivpc srvghvfrkr hpynfpegna
      361 ltyirntkrt aevwmdeykq yyyearpsai gkafgsvatr ieqrkkmdck sfrwylenvy
      421 peltvpvkev lpgvikqgvn clesqgqnta gdlllgmgic rgsakspppa qawlfsdhli
      481 qqqgkclaat stlmsspgsp vilqtcnpke gkqkwrrkgs fiqhsvsglc letkpaqlvt
      541 skcqtdaqaq qwqllpht
//
LOCUS       NP_001350643            1241 aa            linear   PRI 27-APR-2025
DEFINITION  MYND-type zinc finger-containing chromatin reader ZMYND8 isoform s
            [Homo sapiens].
ACCESSION   NP_001350643 XP_005260413
VERSION     NP_001350643.1
DBSOURCE    REFSEQ: accession NM_001363714.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1241)
  AUTHORS   Tang,K., Yin,T., Deng,B., Wang,M., Ren,Z., Wang,S., Liu,X., Li,H.,
            Wang,J., Du,Y., Zhou,J., Chen,Y. and Wang,Y.
  TITLE     USP7 deubiquitinates epigenetic reader ZMYND8 to promote breast
            cancer cell migration and invasion
  JOURNAL   J Biol Chem 300 (9), 107672 (2024)
   PUBMED   39128723
  REMARK    GeneRIF: USP7 deubiquitinates epigenetic reader ZMYND8 to promote
            breast cancer cell migration and invasion.
REFERENCE   2  (residues 1 to 1241)
  AUTHORS   Guha,D., Singh,V., Nandi,S., Ramos,E.I., Gadad,S.S. and Das,C.
  TITLE     ZMYND8 Is a Regulator of Sonic Hedgehog Signaling in ATRA-Mediated
            Differentiation of Neuroblastoma Cells
  JOURNAL   Biochemistry 63 (12), 1534-1542 (2024)
   PUBMED   38804064
  REMARK    GeneRIF: ZMYND8 Is a Regulator of Sonic Hedgehog Signaling in
            ATRA-Mediated Differentiation of Neuroblastoma Cells.
REFERENCE   3  (residues 1 to 1241)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1241)
  AUTHORS   Adhikary,S., Singh,V., Choudhari,R., Yang,B., Adhikari,S.,
            Ramos,E.I., Chaudhuri,S., Roy,S., Gadad,S.S. and Das,C.
  TITLE     ZMYND8 suppresses MAPT213 LncRNA transcription to promote neuronal
            differentiation
  JOURNAL   Cell Death Dis 13 (9), 766 (2022)
   PUBMED   36064715
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1241)
  AUTHORS   Dias,K.R., Carlston,C.M., Blok,L.E.R., De Hayr,L., Nawaz,U.,
            Evans,C.A., Bayrak-Toydemir,P., Htun,S., Zhu,Y., Ma,A., Lynch,S.A.,
            Moorwood,C., Stals,K., Ellard,S., Bainbridge,M.N., Friedman,J.,
            Pappas,J.G., Rabin,R., Nowak,C.B., Douglas,J., Wilson,T.E., Guillen
            Sacoto,M.J., Mullegama,S.V., Palculict,T.B., Kirk,E.P.,
            Pinner,J.R., Edwards,M., Montanari,F., Graziano,C., Pippucci,T.,
            Dingmann,B., Glass,I., Mefford,H.C., Shimoji,T., Suzuki,T.,
            Yamakawa,K., Streff,H., Schaaf,C.P., Slavotinek,A.M., Voineagu,I.,
            Carey,J.C., Buckley,M.F., Schenck,A., Harvey,R.J. and Roscioli,T.
  TITLE     De Novo ZMYND8 variants result in an autosomal dominant
            neurodevelopmental disorder with cardiac malformations
  JOURNAL   Genet Med 24 (9), 1952-1966 (2022)
   PUBMED   35916866
  REMARK    GeneRIF: De Novo ZMYND8 variants result in an autosomal dominant
            neurodevelopmental disorder with cardiac malformations.
REFERENCE   6  (residues 1 to 1241)
  AUTHORS   Nelson,D., Yoshida,E.M., Paulson,M.S., Hengen,P.N., Ge,D.,
            Kanwar,B., McNally,J., Pang,P.S., Subramanian,G.M.,
            McHutchison,J.G., Urbanek,P., Lawitz,E. and Urban,T.J.
  TITLE     Genome-wide association study to characterize serum bilirubin
            elevations in patients with HCV treated with GS-9256, an HCV NS3
            serine protease inhibitor
  JOURNAL   Antivir Ther 19 (7), 679-686 (2014)
   PUBMED   24503447
REFERENCE   7  (residues 1 to 1241)
  AUTHORS   Miles,R.R., Crockett,D.K., Lim,M.S. and Elenitoba-Johnson,K.S.
  TITLE     Analysis of BCL6-interacting proteins by tandem mass spectrometry
  JOURNAL   Mol Cell Proteomics 4 (12), 1898-1909 (2005)
   PUBMED   16147992
REFERENCE   8  (residues 1 to 1241)
  AUTHORS   Westendorf,J.J. and Koka,S.
  TITLE     Identification of FHOD1-binding proteins and mechanisms of
            FHOD1-regulated actin dynamics
  JOURNAL   J Cell Biochem 92 (1), 29-41 (2004)
   PUBMED   15095401
REFERENCE   9  (residues 1 to 1241)
  AUTHORS   Eichmuller,S., Usener,D., Dummer,R., Stein,A., Thiel,D. and
            Schadendorf,D.
  TITLE     Serological detection of cutaneous T-cell lymphoma-associated
            antigens
  JOURNAL   Proc Natl Acad Sci U S A 98 (2), 629-634 (2001)
   PUBMED   11149944
REFERENCE   10 (residues 1 to 1241)
  AUTHORS   Fossey,S.C., Kuroda,S., Price,J.A., Pendleton,J.K., Freedman,B.I.
            and Bowden,D.W.
  TITLE     Identification and characterization of PRKCBP1, a candidate
            RACK-like protein
  JOURNAL   Mamm Genome 11 (10), 919-925 (2000)
   PUBMED   11003709
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK295747.1, AL031666.6 and
            AL022342.7.
            
            On May 25, 2018 this sequence version replaced XP_005260413.1.
            
            Summary: The protein encoded by this gene is a receptor for
            activated C-kinase (RACK) protein. The encoded protein has been
            shown to bind in vitro to activated protein kinase C beta I. In
            addition, this protein is a cutaneous T-cell lymphoma-associated
            antigen. Finally, the protein contains a bromodomain and two zinc
            fingers, and is thought to be a transcriptional regulator. Multiple
            transcript variants encoding several different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295747.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1241
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..1241
                     /product="MYND-type zinc finger-containing chromatin
                     reader ZMYND8 isoform s"
                     /note="CTCL tumor antigen se14-3; RACK like clone 7;
                     protein kinase C-binding protein 1; predicted protein of
                     HQ2893; zinc finger MYND domain-containing protein 8;
                     cutaneous T-cell lymphoma-associated antigen se14-3;
                     transcription coregulator ZMYND8; MYND-type zinc
                     finger-containing chromatin reader ZMYND8"
                     /calculated_mol_wt=137899
     Region          <31..160
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          117..157
                     /region_name="PHD_PRKCBP1"
                     /note="PHD finger found in protein kinase C-binding
                     protein 1 (PRKCBP1); cd15538"
                     /db_xref="CDD:277013"
     Site            order(117,126..130,134,152)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277013"
     Region          178..276
                     /region_name="Bromo_RACK7"
                     /note="Bromodomain, RACK7_like subfamily. RACK7 (also
                     called human protein kinase C-binding protein) was
                     identified as a potential tumor suppressor genes, it
                     shares domain architecture with BS69/ZMYND11; both have
                     been implicated in the regulation of cellular...; cd05508"
                     /db_xref="CDD:99940"
     Site            order(204,209,212,251,255,261)
                     /site_type="other"
                     /note="putative acetyllysine binding site [chemical
                     binding]"
                     /db_xref="CDD:99940"
     Region          299..389
                     /region_name="PWWP_PRKCBP1"
                     /note="PWWP domain found in protein kinase C-binding
                     protein 1 (PRKCBP1) and similar proteins; cd20160"
                     /db_xref="CDD:438988"
     Site            order(301,305)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:438988"
     Site            order(311,313,361,363,367..368)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438988"
     Site            order(312,314..315,334,336..339,341,362..365)
                     /site_type="other"
                     /note="regulatory protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438988"
     Site            order(315,318,334)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438988"
     Site            316..319
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438988"
     Region          449..647
                     /region_name="DUF3544"
                     /note="Protein kinase C-binding protein 1; pfam12064"
                     /db_xref="CDD:463452"
     Region          <629..>787
                     /region_name="TFIIF_alpha"
                     /note="Transcription initiation factor IIF, alpha subunit
                     (TFIIF-alpha); pfam05793"
                     /db_xref="CDD:310411"
     Region          <984..>1051
                     /region_name="AtpF"
                     /note="FoF1-type ATP synthase, membrane subunit b or b'
                     [Energy production and conversion]; COG0711"
                     /db_xref="CDD:440475"
     Region          1055..1089
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..1241
                     /gene="ZMYND8"
                     /gene_synonym="PRKCBP1; PRO2893; RACK7"
                     /coded_by="NM_001363714.1:23..3748"
                     /note="isoform s is encoded by transcript variant 19"
                     /db_xref="CCDS:CCDS86962.1"
                     /db_xref="GeneID:23613"
                     /db_xref="HGNC:HGNC:9397"
                     /db_xref="MIM:615713"
ORIGIN      
        1 mvfleefear sclaeeeikt eqevvegmdi strskdpgsa ertaqkrkfp spphssnghs
       61 pqdtstspik kkkkpgllns nnkeqselrh gpfyymkqpl ttdpvdvvpq dgrndfycwv
      121 chregqvlcc elcprvyhak clrltsepeg dwfcpeceki tvaecietqs kamtmltieq
      181 lsyllkfaiq kmkqpgtdaf qkpvpleqhp dyaeyifhpm dlctleknak kkmygcteaf
      241 ladakwilhn ciiynggnhk ltqiakvvik icehemneie vcpecylaac qkrdnwfcep
      301 csnphplvwa klkgfpfwpa kalrdkdgqv darffgqhdr awvpinncyl mskeipfsvk
      361 ktksifnsam qemevyveni rrkfgvfnys pfrtpytpns qyqmlldptn psagtakidk
      421 qekvklnfdm taspkilmsk pvlsggtgrr islsdmprsp mstnssvhtg sdveqdaekk
      481 atsshfsase esmdfldkst aspastktgq agslsgspkp fspqlsapit tktdktsttg
      541 silnlnldrs kaemdlkels esvqqqstpv plispkrqir srfqlnldkt iesckaqlgi
      601 neisedvyta vehsdsedse ksdssdseyi sddeqkskne pedtedkegc qmdkepsavk
      661 kkpkptnpve ikeelkstsp asekadpgav kdkaspepek dfsekakpsp hpikdklkgk
      721 detdsptvhl gldsdsesel vidlgedhsg regrknkkep kepspkqdvv gktppsttvg
      781 shsppetpvl trssaqtsaa gatattstss tvtvtapapa atgspvkkqr pllpketapa
      841 vqrvvwnsss kfqtssqkwh mqkmqrqqqq qqqqnqqqqp qssqgtryqt rqavkavqqk
      901 eitqspstst itlvtstqss plvtssgsms tlvssvnadl piatasadva adiakytskm
      961 mdaikgtmte iyndlskntt gstiaeirrl rieieklqwl hqqelsemkh nleltmaemr
     1021 qsleqerdrl iaevkkqlel ekqqavdetk kkqwcanckk eaifyccwnt sycdypcqqa
     1081 hwpehmksct qsatapqqea daevntetln kssqgsssst qsapsetasa skeketsaek
     1141 skesgstldl sgsretpssi llgsnqgsvs krcdkqpaya ptttdhqphp nypaqkyhsr
     1201 snksswsssd ekrgstrsdh ntststksll pkesrldtfw d
//
LOCUS       NP_001182181             270 aa            linear   PRI 27-APR-2025
DEFINITION  aprataxin isoform i [Homo sapiens].
ACCESSION   NP_001182181
VERSION     NP_001182181.2
DBSOURCE    REFSEQ: accession NM_001195252.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Apr 23, 2019 this sequence version replaced NP_001182181.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (11) differs in the 5' UTR and
            uses an alternate in-frame splice site in the 5' coding region,
            compared to variant 1. The encoded isoform (i) is shorter than
            isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY208831.1, SRR7346977.508966.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..270
                     /product="aprataxin isoform i"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=31134
     Region          3..89
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Site            order(28..29,41..42,44,64..65)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438714"
     Region          92..193
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(186,188,190..192)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          211..270
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..270
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001195252.2:67..879"
                     /note="isoform i is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS94395.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqvqlkae cnkgyvkvkq
       61 vgvnptsids vvigkdqevk lqpgqvlhme slghwsqglk ismqdpkmqv ykdeqvvvik
      121 dkypkaryhw lvlpwtsiss lkavarehle llkhmhtvge kvivdfagss klrfrlgyha
      181 ipsmshvhlh visqdfdspc lknkkhwnsf nteyflesqa viemvqeagr vtvrdgmpel
      241 lklplrchec qqllpsipql kehlrkhwtq
//
LOCUS       NP_653297               1012 aa            linear   PRI 27-APR-2025
DEFINITION  axonemal dynein light chain domain-containing protein 1 [Homo
            sapiens].
ACCESSION   NP_653297
VERSION     NP_653297.3
DBSOURCE    REFSEQ: accession NM_144696.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Houston,B.J., Nguyen,J., Merriner,D.J., O'Connor,A.E., Lopes,A.M.,
            Nagirnaja,L., Friedrich,C., Kliesch,S., Tuttelmann,F., Aston,K.I.,
            Conrad,D.F., Hobbs,R.M., Dunleavy,J.E.M. and O'Bryan,M.K.
  TITLE     AXDND1 is required to balance spermatogonial commitment and for
            sperm tail formation in mice and humans
  JOURNAL   Cell Death Dis 15 (7), 499 (2024)
   PUBMED   38997255
  REMARK    GeneRIF: AXDND1 is required to balance spermatogonial commitment
            and for sperm tail formation in mice and humans.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Ma,Q., Cao,C., Zhuang,C., Luo,X., Li,X., Wan,H., Ye,J., Chen,F.,
            Cui,L., Zhang,Y., Wen,Y., Yuan,S. and Gui,Y.
  TITLE     AXDND1, a novel testis-enriched gene, is required for
            spermiogenesis and male fertility
  JOURNAL   Cell Death Discov 7 (1), 348 (2021)
   PUBMED   34759295
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Pineau,C., Hikmet,F., Zhang,C., Oksvold,P., Chen,S., Fagerberg,L.,
            Uhlen,M. and Lindskog,C.
  TITLE     Cell Type-Specific Expression of Testis Elevated Genes Based on
            Transcriptomics and Antibody-Based Proteomics
  JOURNAL   J Proteome Res 18 (12), 4215-4230 (2019)
   PUBMED   31429579
REFERENCE   4  (residues 1 to 1012)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   5  (residues 1 to 1012)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 1012)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1012)
  AUTHORS   Baranzini,S.E., Wang,J., Gibson,R.A., Galwey,N., Naegelin,Y.,
            Barkhof,F., Radue,E.W., Lindberg,R.L., Uitdehaag,B.M.,
            Johnson,M.R., Angelakopoulou,A., Hall,L., Richardson,J.C.,
            Prinjha,R.K., Gass,A., Geurts,J.J., Kragt,J., Sombekke,M.,
            Vrenken,H., Qualley,P., Lincoln,R.R., Gomez,R., Caillier,S.J.,
            George,M.F., Mousavi,H., Guerrero,R., Okuda,D.T., Cree,B.A.,
            Green,A.J., Waubant,E., Goodin,D.S., Pelletier,D., Matthews,P.M.,
            Hauser,S.L., Kappos,L., Polman,C.H. and Oksenberg,J.R.
  TITLE     Genome-wide association analysis of susceptibility and clinical
            phenotype in multiple sclerosis
  JOURNAL   Hum Mol Genet 18 (4), 767-778 (2009)
   PUBMED   19010793
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX647935.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 10, 2004 this sequence version replaced NP_653297.2.
            
            Transcript Variant: This variant (1) represents the longer,
            protein-coding transcript.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647935.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367618.8/ ENSP00000356590.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1012
                     /product="axonemal dynein light chain domain-containing
                     protein 1"
                     /calculated_mol_wt=117896
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1B0.1)"
     Region          <261..357
                     /region_name="Ax_dynein_light"
                     /note="Axonemal dynein light chain; pfam10211"
                     /db_xref="CDD:463000"
     Region          841..879
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1B0.1)"
     Region          963..1012
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1B0.1)"
     CDS             1..1012
                     /gene="AXDND1"
                     /gene_synonym="C1orf125"
                     /coded_by="NM_144696.6:137..3175"
                     /db_xref="CCDS:CCDS30948.1"
                     /db_xref="GeneID:126859"
                     /db_xref="HGNC:HGNC:26564"
ORIGIN      
        1 mslpktpstp lnststsesk klkvsvakeg trglpelkek knmvdrskll ptslqnefip
       61 kevllsltya anagpcpenl lppkkiktpk gtlprlvdhv whhpvrrnkf kylidhpvsl
      121 tgagrdisfl ydvtyakgqt rekavcpphl arslqshdgv ivphkpktlt dtlipeefhi
      181 vsstgvsgle cyddkyttll tdsenrlllf psmkpnkrve vaqlndvmdt mleragvenq
      241 eytgptkmhk llhilkkeqt iynmifheli rqvsvdcadr gellskvrer yvqmldqiar
      301 qmidfykdlv tqrvmdqril eelynfkhvi eeltrelclv rahdvkltke tekahkdlaq
      361 allnaeknak iveeyhdlyt lqrermendm kklvaerdiw ssatyelalk viernrvila
      421 rrlylnekgw nkytkhfiil lsnkdtedla llqkltqkwr nlvnklkqev eqmeestset
      481 lkivkdglik wqeffnekdi lspnkgnifn svlldfkqwq kilnekkeef tgdvllskyd
      541 tlkiikhlqe nwadiglgif nrhkslegem pserqymeei ikniqklyke yeiringdng
      601 yskilpslis sldfcsfkle nlefpdtple ewqeidekin emkshldill nltgivpqhi
      661 dvdsvsvlqa yifnmiqqwl lkigneinng nielqhhmde lhismiqwmv nllilmipnf
      721 tdqdcllkle eesaekhdig varleldaie ltrklyqyss ylsscckgmv tamalskstn
      781 shknatedly evdklkkecy ewintcscll snikgrkitl ltyeeierll eeeavkefie
      841 peidesfked eeeskedrkl qeenkeraee qpststekek lirfigeden vhskplfetd
      901 vlsswresak qgtlaqkyle amaviehmqe kllevenrar qaeekfeday eklhhtlikn
      961 kdleelvmts rkeskeeken qderevkeee eqqeeeevrs aensskspkk gh
//
LOCUS       NP_115502                233 aa            linear   PRI 27-APR-2025
DEFINITION  testis-expressed protein 35 isoform 1 [Homo sapiens].
ACCESSION   NP_115502
VERSION     NP_115502.2
DBSOURCE    REFSEQ: accession NM_032126.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Tang,A., Yu,Z., Gui,Y., Guo,X., Long,Y. and Cai,Z.
  TITLE     Identification and characteristics of a novel testis-specific gene,
            Tsc24, in human and mice
  JOURNAL   Biol Pharm Bull 29 (11), 2187-2191 (2006)
   PUBMED   17077512
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136694.1, AL552172.3 and AW628627.1.
            
            On Dec 30, 2009 this sequence version replaced NP_115502.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.142172.1, AL136694.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319416.7/ ENSP00000323795.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..233
                     /product="testis-expressed protein 35 isoform 1"
                     /note="Testis-Specific Conserved gene 24kDa;
                     testis-expressed sequence 35 protein; testis-expressed
                     protein 35"
                     /calculated_mol_wt=26387
     Region          1..208
                     /region_name="Tsc35"
                     /note="Testis-specific protein 35; pfam15079"
                     /db_xref="CDD:464490"
     Region          199..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T0J7.1)"
     CDS             1..233
                     /gene="TEX35"
                     /gene_synonym="C1orf49; TSC24"
                     /coded_by="NM_032126.5:81..782"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1323.1"
                     /db_xref="GeneID:84066"
                     /db_xref="HGNC:HGNC:25366"
ORIGIN      
        1 msakraelkk thlsknykav clelkpeptk tfdykavkqe grftkagvtq dlknelrevr
       61 eelkekmeei kqikdlmdkd fdklhefvei mkemqkdmde kmdilintqk nyklplrrap
      121 keqqelrlmg kthrepqlrp kkmdgasgvn gapcalhkkt mapqktkqgs ldplhhcgtc
      181 cekcllcalk nnynrgnips easglykgge epvttqpsvg havpapksqt egr
//
LOCUS       NP_904358               1073 aa            linear   PRI 27-APR-2025
DEFINITION  TSC22 domain family protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_904358
VERSION     NP_904358.2
DBSOURCE    REFSEQ: accession NM_183422.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Kamimura,R., Uchida,D., Kanno,S.I., Shiraishi,R., Hyodo,T.,
            Sawatani,Y., Shimura,M., Hasegawa,T., Tsubura-Okubo,M., Yaguchi,E.,
            Komiyama,Y., Fukumoto,C., Izumi,S., Fujita,A., Wakui,T. and
            Kawamata,H.
  TITLE     Identification of Binding Proteins for TSC22D1 Family Proteins
            Using Mass Spectrometry
  JOURNAL   Int J Mol Sci 22 (20), 10913 (2021)
   PUBMED   34681573
  REMARK    GeneRIF: Identification of Binding Proteins for TSC22D1 Family
            Proteins Using Mass Spectrometry.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1073)
  AUTHORS   Homig-Holzel,C., van Doorn,R., Vogel,C., Germann,M., Cecchini,M.G.,
            Verdegaal,E. and Peeper,D.S.
  TITLE     Antagonistic TSC22D1 variants control BRAF(E600)-induced senescence
  JOURNAL   EMBO J 30 (9), 1753-1765 (2011)
   PUBMED   21448135
  REMARK    GeneRIF: Differential regulation of antagonistic TSC22D1 variants
            is required for the establishment of oncogene-induced cellular
            senescence.
REFERENCE   5  (residues 1 to 1073)
  AUTHORS   Lu,Y., Kitaura,J., Oki,T., Komeno,Y., Ozaki,K., Kiyono,M.,
            Kumagai,H., Nakajima,H., Nosaka,T., Aburatani,H. and Kitamura,T.
  TITLE     Identification of TSC-22 as a potential tumor suppressor that is
            upregulated by Flt3-D835V but not Flt3-ITD
  JOURNAL   Leukemia 21 (11), 2246-2257 (2007)
   PUBMED   17690703
  REMARK    GeneRIF: TSC-22 is a potential tumor suppressor that is upregulated
            by Flt3-D835V but not Flt3-ITD
REFERENCE   6  (residues 1 to 1073)
  AUTHORS   Sugawara,F., Yamada,Y., Watanabe,R., Ban,N., Miyawaki,K., Kuroe,A.,
            Hamasaki,A., Ikeda,H., Kurose,T., Usami,M., Ikeda,M. and Seino,Y.
  TITLE     The role of the TSC-22 (-396) A/G variant in the development of
            diabetic nephropathy
  JOURNAL   Diabetes Res Clin Pract 60 (3), 191-197 (2003)
   PUBMED   12757981
  REMARK    GeneRIF: findings suggest that the TSC-22 gene (-396) A allele is
            associated with an increasing risk of diabetic nephropathy
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1073)
  AUTHORS   Kester,H.A., Blanchetot,C., den Hertog,J., van der Saag,P.T. and
            van der Burg,B.
  TITLE     Transforming growth factor-beta-stimulated clone-22 is a member of
            a family of leucine zipper proteins that can homo- and
            heterodimerize and has transcriptional repressor activity
  JOURNAL   J Biol Chem 274 (39), 27439-27447 (1999)
   PUBMED   10488076
REFERENCE   8  (residues 1 to 1073)
  AUTHORS   Ohta,S., Shimekake,Y. and Nagata,K.
  TITLE     Molecular cloning and characterization of a transcription factor
            for the C-type natriuretic peptide gene promoter
  JOURNAL   Eur J Biochem 242 (3), 460-466 (1996)
   PUBMED   9022669
REFERENCE   9  (residues 1 to 1073)
  AUTHORS   Jay,P., Ji,J.W., Marsollier,C., Taviaux,S., Berge-Lefranc,J.L. and
            Berta,P.
  TITLE     Cloning of the human homologue of the TGF beta-stimulated clone 22
            gene
  JOURNAL   Biochem Biophys Res Commun 222 (3), 821-826 (1996)
   PUBMED   8651929
REFERENCE   10 (residues 1 to 1073)
  AUTHORS   Shibanuma,M., Kuroki,T. and Nose,K.
  TITLE     Isolation of a gene encoding a putative leucine zipper structure
            that is induced by transforming growth factor beta 1 and other
            growth factors
  JOURNAL   J Biol Chem 267 (15), 10219-10224 (1992)
   PUBMED   1587811
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB082525.1, AL356107.21 and
            AL138960.16.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 29, 2008 this sequence version replaced NP_904358.1.
            
            Summary: This gene encodes a member of the TSC22 domain family of
            leucine zipper transcription factors. The encoded protein is
            stimulated by transforming growth factor beta, and regulates the
            transcription of multiple genes including C-type natriuretic
            peptide. The encoded protein may play a critical role in tumor
            suppression through the induction of cancer cell apoptosis, and a
            single nucleotide polymorphism in the promoter of this gene has
            been associated with diabetic nephropathy. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1, also known as
            TSC22D1.1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB082525.1, BC136475.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000458659.3/ ENSP00000397435.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.11"
     Protein         1..1073
                     /product="TSC22 domain family protein 1 isoform 1"
                     /note="transforming growth factor beta-stimulated protein
                     TSC-22; cerebral protein 2; regulatory protein TSC-22;
                     TGFB-stimulated clone 22 homolog; transforming growth
                     factor beta-1-induced transcript 4 protein;
                     transcriptional regulator TSC-22; TGFbeta-stimulated clone
                     22"
                     /calculated_mol_wt=109546
     Region          1..98
                     /region_name="Required for interaction with TGFBR1 and
                     promotion of TGF-beta signaling.
                     /evidence=ECO:0000269|PubMed:21791611"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Region          22..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Region          125..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Region          220..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15714.3)"
     Region          458..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Region          607..628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Region          <685..899
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          742..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Region          983..1061
                     /region_name="ZIP_TSC22D1"
                     /note="leucine zipper domain found in TSC22 domain family
                     protein 1; cd21938"
                     /db_xref="CDD:409278"
     Site            order(1001..1003,1006,1009..1010,1013..1014,1016..1017,
                     1020..1021,1023..1024,1027..1028,1031,1035)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409278"
     Region          1006..1027
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Region          1037..1073
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     CDS             1..1073
                     /gene="TSC22D1"
                     /gene_synonym="HUCEP-2; Ptg-2; TGFB1I4; TSC22"
                     /coded_by="NM_183422.4:257..3478"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31966.1"
                     /db_xref="GeneID:8848"
                     /db_xref="HGNC:HGNC:16826"
                     /db_xref="MIM:607715"
ORIGIN      
        1 mhqppestaa aaaaadisar kmahpamfpr rgsgsgsasa lnaagtgvgs natssedfpp
       61 psllqppppa asstsgpqpp ppqslnllsq aqlqaqplap ggtqmkkksg fqitsvtpaq
      121 isasissnns iaedtesydd ldeshtedls sseildvsls ratdlgeper ssseetlnnf
      181 qeaetpgavs pnqphlpqph lphlpqqnvv ingnahphhl hhhhqihhgh hlqhghhhps
      241 hvavasasit ggppsspvsr klsttgssds itpvaptsav sssgspasvm tnmrapsttg
      301 giginsvtgt stvnnvnita vgsfnpnvts smlgnvnist snipsaagvs vgpgvtsgvn
      361 vnilsgmgng tisssaavss vpnaaagmtg gsvssqqqqp tvntsrfrvv kldsssepfk
      421 kgrwtctefy ekenavpate gvlinkvvet vkqnpievts erestsgssv sssvstlshy
      481 tesvgsgemg aptvvvqqqq qqqqqqqqqp alqgvtlqqm dfgstgpqsi pavsipqsis
      541 qsqisqvqlq sqelsyqqkq glqpvplqat msaatgiqps pvnvvgvtsa lgqqpsissl
      601 aqpqlpysqa appvqtplpg apppqqlqyg qqqpmvstqm apghvksvtq npaseyvqqq
      661 pilqtamssg qpssagvgag ttvipvaqpq giqlpvqpta vpaqpagasv qpvgqapaav
      721 savptgsqia nigqqanipt avqqpstqvp psviqqgapp ssqvvppaqt giihqgvqts
      781 apslpqqlvi asqsslltvp pqpqgvepva qgivsqqlpa vsslpsassi svtsqvsstg
      841 psgmpsaptn lvppqniaqt patqngnlvq svsqppliat ntnlplaqqi plsstqfsaq
      901 slaqaigsqi edarraaeps lvglpqtisg dsggmsavsd gsssslaasa slfplkvlpl
      961 ttplvdgede sssgasvvai dnkieqamdl vkshlmyavr eevevlkeqi kelieknsql
     1021 eqennllktl aspeqlaqfq aqlqtgsppa ttqpqgttqp paqpasqgsg pta
//
LOCUS       NP_001346771             193 aa            linear   ROD 27-APR-2025
DEFINITION  neurocalcin-delta [Mus musculus].
ACCESSION   NP_001346771 XP_017172186
VERSION     NP_001346771.1
DBSOURCE    REFSEQ: accession NM_001359842.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Kolesova,H., Hrabalova,P., Bohuslavova,R., Abaffy,P.,
            Fabriciova,V., Sedmera,D. and Pavlinkova,G.
  TITLE     Reprogramming of the developing heart by Hif1a-deficient
            sympathetic system and maternal diabetes exposure
  JOURNAL   Front Endocrinol (Lausanne) 15, 1344074 (2024)
   PUBMED   38505753
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Ahuja,N., Hiltabidle,M.S., Rajasekhar,H., Voss,S., Lu,S.Z.,
            Barlow,H.R., Cowdin,M.A., Daniel,E., Vaddaraju,V., Anandakumar,T.,
            Black,E., Cleaver,O. and Maynard,C.
  TITLE     Endothelial Cyp26b1 restrains murine heart valve growth during
            development
  JOURNAL   Dev Biol 486, 81-95 (2022)
   PUBMED   35364055
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Del Aguila,A., Adam,M., Ullom,K., Shaw,N., Qin,S., Ehrman,J.,
            Nardini,D., Salomone,J., Gebelein,B., Lu,Q.R., Potter,S.S.,
            Waclaw,R., Campbell,K. and Nakafuku,M.
  TITLE     Olig2 defines a subset of neural stem cells that produce specific
            olfactory bulb interneuron subtypes in the subventricular zone of
            adult mice
  JOURNAL   Development 149 (5) (2022)
   PUBMED   35132995
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Upadhyay,A., Hosseinibarkooie,S., Schneider,S., Kaczmarek,A.,
            Torres-Benito,L., Mendoza-Ferreira,N., Overhoff,M., Rombo,R.,
            Grysko,V., Kye,M.J., Kononenko,N.L. and Wirth,B.
  TITLE     Neurocalcin Delta Knockout Impairs Adult Neurogenesis Whereas Half
            Reduction Is Not Pathological
  JOURNAL   Front Mol Neurosci 12, 19 (2019)
   PUBMED   30853885
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Duda,T., Pertzev,A. and Sharma,R.K.
  TITLE     Ca(2+) modulation of ANF-RGC: new signaling paradigm interlocked
            with blood pressure regulation
  JOURNAL   Biochemistry 51 (46), 9394-9405 (2012)
   PUBMED   23088492
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Brouns,M.R., De Castro,S.C., Terwindt-Rouwenhorst,E.A., Massa,V.,
            Hekking,J.W., Hirst,C.S., Savery,D., Munts,C., Partridge,D.,
            Lamers,W., Kohler,E., van Straaten,H.W., Copp,A.J. and Greene,N.D.
  TITLE     Over-expression of Grhl2 causes spina bifida in the Axial defects
            mutant mouse
  JOURNAL   Hum Mol Genet 20 (8), 1536-1546 (2011)
   PUBMED   21262862
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Kotani,T., Murata,Y., Ohnishi,H., Mori,M., Kusakari,S., Saito,Y.,
            Okazawa,H., Bixby,J.L. and Matozaki,T.
  TITLE     Expression of PTPRO in the interneurons of adult mouse olfactory
            bulb
  JOURNAL   J Comp Neurol 518 (2), 119-136 (2010)
   PUBMED   19924828
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Murias,A.R., Weruaga,E., Recio,J.S., Airado,C., Diaz,D. and
            Alonso,J.R.
  TITLE     Distribution of neurocalcin-containing neurons reveals sexual
            dimorphism in the mouse olfactory bulb
  JOURNAL   Chem Senses 32 (7), 673-680 (2007)
   PUBMED   17548529
  REMARK    GeneRIF: According to their distribution in the olfactory bulb,
            neurocalcin-immunoreactive interneurons could reflect a sexually
            dimorphic regulation of specific odorants.
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Germana,A., del Valle,M.E., Laura,R., Ciriaco,E., Vega,J.A. and
            Germana,G.
  TITLE     Effects of neurotrophin-3 gene mutation in the expression of
            neurocalcin
  JOURNAL   Ital J Anat Embryol 110 (2 Suppl 1), 37-47 (2005)
   PUBMED   16101019
  REMARK    GeneRIF: Neurocalcin-containing DRG neurons include all
            proprioceptive, and a subset of mechanoreceptive and
            proprioceptive. Furthermore, NT-3 is involved in the maturation of
            motor end-plates.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC121814.3.
            
            On Jan 13, 2018 this sequence version replaced XP_017172186.1.
            
            Transcript Variant: This variant (8) differs in the 5' UTR compared
            to variant 1. Variants 1 through 11 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660813.52263.1,
                                           SRR7652917.792301.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849385
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 14.94 cM"
     Protein         1..193
                     /product="neurocalcin-delta"
                     /calculated_mol_wt=22114
     Region          21..175
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..193
                     /gene="Ncald"
                     /gene_synonym="D030020D09Rik; D15Ertd412e"
                     /coded_by="NM_001359842.1:95..676"
                     /db_xref="CCDS:CCDS27435.1"
                     /db_xref="GeneID:52589"
                     /db_xref="MGI:MGI:1196326"
ORIGIN      
        1 mgkqnsklrp evmqdllest dfteheiqew ykgflrdcps ghlsmeefkk iygnffpygd
       61 askfaehvfr tfdangdgti dfrefiials vtsrgkleqk lkwafsmydl dgngyiskae
      121 mleivqaiyk mvssvmkmpe destpekrte kifrqmdtnr dgklsleefi rgaksdpsiv
      181 rllqcdpssa gqf
//
LOCUS       NP_653240                676 aa            linear   PRI 27-APR-2025
DEFINITION  urocanate hydratase isoform 1 [Homo sapiens].
ACCESSION   NP_653240
VERSION     NP_653240.1
DBSOURCE    REFSEQ: accession NM_144639.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Wang,Q.Y., Liu,Y.J., Hu,Y., Xiao,H., Xia,L.L. and Wu,Y.G.
  TITLE     Prognostic and immune roles of UROC1 in human cancers: from
            mechanism exploration of NAFLD and HCC to pan-cancer analysis
  JOURNAL   Eur Rev Med Pharmacol Sci 28 (2), 622-644 (2024)
   PUBMED   38305606
  REMARK    GeneRIF: Prognostic and immune roles of UROC1 in human cancers:
            from mechanism exploration of NAFLD and HCC to pan-cancer analysis.
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Espinos,C., Pineda,M., Martinez-Rubio,D., Lupo,V., Ormazabal,A.,
            Vilaseca,M.A., Spaapen,L.J., Palau,F. and Artuch,R.
  TITLE     Mutations in the urocanase gene UROC1 are associated with urocanic
            aciduria
  JOURNAL   J Med Genet 46 (6), 407-411 (2009)
   PUBMED   19304569
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
REFERENCE   5  (residues 1 to 676)
  AUTHORS   Retey,J.
  TITLE     The urocanase story: a novel role of NAD+ as electrophile
  JOURNAL   Arch Biochem Biophys 314 (1), 1-16 (1994)
   PUBMED   7944380
  REMARK    Review article
REFERENCE   6  (residues 1 to 676)
  AUTHORS   Kalafatic,Z., Lipovac,K., Jezerinac,Z., Juretic,D., Dumic,M.,
            Zurga,B. and Res,L.
  TITLE     A liver urocanase deficiency
  JOURNAL   Metabolism 29 (11), 1013-1019 (1980)
   PUBMED   6107814
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA638082.1, BC115405.1,
            AK055862.1, AC024558.21 and BX108463.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an enzyme involved in the second step of
            histidine catabolism, metabolizing urocanic acid to
            formiminoglutamic acid. Deficiency of this enzyme results in
            urocanic aciduria, and is an apparent cause of mental retardation.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Apr 2021].
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055862.1, BC115405.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000290868.7/ ENSP00000290868.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.3"
     Protein         1..676
                     /product="urocanate hydratase isoform 1"
                     /EC_number="4.2.1.49"
                     /note="imidazolonepropionate hydrolase; urocanase domain
                     containing 1; urocanase 1"
                     /calculated_mol_wt=74700
     Region          15..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96N76.1)"
     Region          68..669
                     /region_name="HutU"
                     /note="Urocanate hydratase [Amino acid transport and
                     metabolism]; COG2987"
                     /db_xref="CDD:442226"
     CDS             1..676
                     /gene="UROC1"
                     /gene_synonym="HMFN0320; UROCD"
                     /coded_by="NM_144639.3:55..2085"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3038.1"
                     /db_xref="GeneID:131669"
                     /db_xref="HGNC:HGNC:26444"
                     /db_xref="MIM:613012"
ORIGIN      
        1 msslqalcsg lplrplpenr grqagvphap vrtpslspve kqlalrnalr yfppdvqell
       61 apefaqelql yghiymyrfc pdiemraypi eqypcqtkva aaimhmimnn ldpavaqfpq
      121 elvtyggngq vfsnwaqfwl tmfylskmte eqtlvmysgh plglfpssrs aprlvitngm
      181 vipnyssrte yeklfalgvt mygqmtagsy cyigpqgivh gtvltvlnaa rrylgiedla
      241 gkvfvtsglg gmsgaqakaa vivgcigvia evdkaalekr hrqgwlmevt dsldrciqrl
      301 rearkkkevl slgyhgnvva lwerlvheld ttgeclvdlg sdqtschnpf nggyypvqls
      361 fteaqslmas npavfkdlvq eslrrqvsai nrlaeekfff wdygnaflle aqragadvek
      421 kgagrtefry psyvqhimgd ifsqgfgpfr wvctsgdpqd lavtdelats vleeaiadgv
      481 kvsvklqymd nirwireaar hrlvvgsqar ilysdqkgrv aiavainqai acrrikapvv
      541 lsrdhhdvsg tdspfretsn iydgsafcad mavqnfvgda crgatwvalh ngggvgwgev
      601 inggfglvld gtpeaegrar lmlswdvsng varrcwsgnq kayeiicqtm qenstlvvtl
      661 phkvedervl qqalql
//
LOCUS       NP_998771                516 aa            linear   PRI 27-APR-2025
DEFINITION  monocarboxylate transporter 12 [Homo sapiens].
ACCESSION   NP_998771
VERSION     NP_998771.3
DBSOURCE    REFSEQ: accession NM_213606.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Flogel,S., Strater,M., Fischer,D. and Grundemann,D.
  TITLE     A creatine efflux transporter in oligodendrocytes
  JOURNAL   FEBS J 292 (5), 1124-1140 (2025)
   PUBMED   39792585
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Jomura,R., Tanno,Y., Akanuma,S.I., Kubo,Y., Tachikawa,M. and
            Hosoya,K.I.
  TITLE     Monocarboxylate transporter 12 as a guanidinoacetate efflux
            transporter in renal proximal tubular epithelial cells
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (11), 183434 (2020)
   PUBMED   32781157
  REMARK    GeneRIF: Monocarboxylate transporter 12 as a guanidinoacetate
            efflux transporter in renal proximal tubular epithelial cells.
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Takahashi,M., Kishimoto,H., Shirasaka,Y. and Inoue,K.
  TITLE     Functional characterization of monocarboxylate transporter 12
            (SLC16A12/MCT12) as a facilitative creatine transporter
  JOURNAL   Drug Metab Pharmacokinet 35 (3), 281-287 (2020)
   PUBMED   32249133
  REMARK    GeneRIF: Functional characterization of monocarboxylate transporter
            12 (SLC16A12/MCT12) as a facilitative creatine transporter.
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 516)
  AUTHORS   Futagi,Y., Narumi,K., Furugen,A., Kobayashi,M. and Iseki,K.
  TITLE     Molecular characterization of the orphan transporter SLC16A9, an
            extracellular pH- and Na+-sensitive creatine transporter
  JOURNAL   Biochem Biophys Res Commun 522 (2), 539-544 (2020)
   PUBMED   31784090
REFERENCE   6  (residues 1 to 516)
  AUTHORS   Abplanalp,J., Laczko,E., Philp,N.J., Neidhardt,J., Zuercher,J.,
            Braun,P., Schorderet,D.F., Munier,F.L., Verrey,F., Berger,W.,
            Camargo,S.M. and Kloeckener-Gruissem,B.
  TITLE     The cataract and glucosuria associated monocarboxylate transporter
            MCT12 is a new creatine transporter
  JOURNAL   Hum Mol Genet 22 (16), 3218-3226 (2013)
   PUBMED   23578822
  REMARK    GeneRIF: study identified a second creatine transporter
            monocarboxylate transporter 12 (MCT12), encoded by the cataract and
            glucosuria associated gene SLC16A12; Rssults show SLC6A8 was
            predominantly found in brain, heart and muscle, while SLC16A12 was
            more abundant in kidney and retina. In the lens, the two
            transcripts were found at comparable levels.
REFERENCE   7  (residues 1 to 516)
  AUTHORS   Castorino,J.J., Gallagher-Colombo,S.M., Levin,A.V.,
            Fitzgerald,P.G., Polishook,J., Kloeckener-Gruissem,B., Ostertag,E.
            and Philp,N.J.
  TITLE     Juvenile cataract-associated mutation of solute carrier SLC16A12
            impairs trafficking of the protein to the plasma membrane
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6774-6784 (2011)
   PUBMED   21778275
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 516)
  AUTHORS   Zuercher,J., Neidhardt,J., Magyar,I., Labs,S., Moore,A.T.,
            Tanner,F.C., Waseem,N., Schorderet,D.F., Munier,F.L.,
            Bhattacharya,S., Berger,W. and Kloeckener-Gruissem,B.
  TITLE     Alterations of the 5'untranslated region of SLC16A12 lead to
            age-related cataract
  JOURNAL   Invest Ophthalmol Vis Sci 51 (7), 3354-3361 (2010)
   PUBMED   20181839
  REMARK    GeneRIF: The monocarboxylate transporter SLC16A12 may contribute to
            age-related cataract. Sequences within the 5'UTR modulate
            translational efficiency with pathogenic consequences.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 516)
  AUTHORS   Kloeckener-Gruissem,B., Vandekerckhove,K., Nurnberg,G.,
            Neidhardt,J., Zeitz,C., Nurnberg,P., Schipper,I. and Berger,W.
  TITLE     Mutation of solute carrier SLC16A12 associates with a syndrome
            combining juvenile cataract with microcornea and renal glucosuria
  JOURNAL   Am J Hum Genet 82 (3), 772-779 (2008)
   PUBMED   18304496
  REMARK    GeneRIF: SLC16A12 is important for lens and kidney homeostasis; its
            potential role in age-related cataract is discussed.
REFERENCE   10 (residues 1 to 516)
  AUTHORS   Halestrap,A.P. and Meredith,D.
  TITLE     The SLC16 gene family-from monocarboxylate transporters (MCTs) to
            aromatic amino acid transporters and beyond
  JOURNAL   Pflugers Arch 447 (5), 619-628 (2004)
   PUBMED   12739169
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL355342.12, AK127303.1, AL353146.9 and BC086873.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 27, 2010 this sequence version replaced NP_998771.2.
            
            Summary: This gene encodes a transmembrane transporter that likely
            plays a role in monocarboxylic acid transport. A mutation in this
            gene has been associated with juvenile cataracts with microcornea
            and renal glucosuria. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127303.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1970526
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371790.5/ ENSP00000360855.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.31"
     Protein         1..516
                     /product="monocarboxylate transporter 12"
                     /note="monocarboxylic acid transporter 12; creatine
                     transporter 2"
                     /calculated_mol_wt=56367
     Region          48..461
                     /region_name="MFS_MCT12"
                     /note="Monocarboxylate transporter 12 of the of the Major
                     Facilitator Superfamily of transporters; cd17424"
                     /db_xref="CDD:340982"
     Site            51..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            order(59..60,63..64,67,102,153..154,156..158,161,180,
                     183..184,187,290,293..294,297..299,302,329,333,386..387,
                     391,395,411,414..415,418..419,422)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340982"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            178..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            207..227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            283..303
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            319..339
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            350..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            377..397
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            410..430
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     Site            440..460
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSM3.3)"
     CDS             1..516
                     /gene="SLC16A12"
                     /gene_synonym="CJMG; CRT2; CTRCT47; MCT12"
                     /coded_by="NM_213606.4:340..1890"
                     /db_xref="CCDS:CCDS7404.2"
                     /db_xref="GeneID:387700"
                     /db_xref="HGNC:HGNC:23094"
                     /db_xref="MIM:611910"
ORIGIN      
        1 mpsgshwtan sskiitwlle qpgkeekrkt makvnrarst sppdggwgwm ivagcflvti
       61 ctravtrcis iffvefqtyf tqdyaqtawi hsivdcvtml caplgsvvsn hlscqvgiml
      121 ggllastgli lssfatslkh lyltlgvltg lgfalcyspa iamvgkyfsr rkalaygiam
      181 sgsgigtfil apvvqllieq fswrgallil ggfvlnlcvc galmrpitlk edhttpeqnh
      241 vcrtqkedik rvspyssltk ewaqtclccc lqqeysfllm sdfvvlavsv lfmaygcspl
      301 fvylvpyals vgvshqqaaf lmsilgvidi ignitfgwlt drrclknyqy vcylfavgmd
      361 glcylclpml qslpllvpfs ctfgyfdgay vtlipvvtte ivgttslssa lgvvyflhav
      421 pylvsppiag rlvdttgsyt aafllcgfsm ifssvllgfa rlikrmrktq lqfiakesdp
      481 klqlwtngsv aysvareldq khgepvatav pgyslt
//
LOCUS       NP_001357525            1191 aa            linear   PRI 27-APR-2025
DEFINITION  phospholipid-transporting ATPase ID isoform d [Homo sapiens].
ACCESSION   NP_001357525
VERSION     NP_001357525.1
DBSOURCE    REFSEQ: accession NM_001370596.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1191)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   2  (residues 1 to 1191)
  AUTHORS   Takatsu,H., Tanaka,G., Segawa,K., Suzuki,J., Nagata,S., Nakayama,K.
            and Shin,H.W.
  TITLE     Phospholipid flippase activities and substrate specificities of
            human type IV P-type ATPases localized to the plasma membrane
  JOURNAL   J Biol Chem 289 (48), 33543-33556 (2014)
   PUBMED   25315773
  REMARK    Erratum:[J Biol Chem. 2016 Oct 7;291(41):21421. doi:
            10.1074/jbc.A114.593012. PMID: 27825076]
REFERENCE   3  (residues 1 to 1191)
  AUTHORS   Bryde,S., Hennrich,H., Verhulst,P.M., Devaux,P.F., Lenoir,G. and
            Holthuis,J.C.
  TITLE     CDC50 proteins are critical components of the human class-1
            P4-ATPase transport machinery
  JOURNAL   J Biol Chem 285 (52), 40562-40572 (2010)
   PUBMED   20961850
REFERENCE   4  (residues 1 to 1191)
  AUTHORS   van der Velden,L.M., Wichers,C.G., van Breevoort,A.E.,
            Coleman,J.A., Molday,R.S., Berger,R., Klomp,L.W. and van de
            Graaf,S.F.
  TITLE     Heteromeric interactions required for abundance and subcellular
            localization of human CDC50 proteins and class 1 P4-ATPases
  JOURNAL   J Biol Chem 285 (51), 40088-40096 (2010)
   PUBMED   20947505
REFERENCE   5  (residues 1 to 1191)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 1191)
  AUTHORS   Paulusma,C.C. and Oude Elferink,R.P.
  TITLE     The type 4 subfamily of P-type ATPases, putative aminophospholipid
            translocases with a role in human disease
  JOURNAL   Biochim Biophys Acta 1741 (1-2), 11-24 (2005)
   PUBMED   15919184
  REMARK    Review article
REFERENCE   7  (residues 1 to 1191)
  AUTHORS   Kuhlbrandt,W.
  TITLE     Biology, structure and mechanism of P-type ATPases
  JOURNAL   Nat Rev Mol Cell Biol 5 (4), 282-295 (2004)
   PUBMED   15071553
  REMARK    Review article
REFERENCE   8  (residues 1 to 1191)
  AUTHORS   Harris,M.J. and Arias,I.M.
  TITLE     FIC1, a P-type ATPase linked to cholestatic liver disease, has
            homologues (ATP8B2 and ATP8B3) expressed throughout the body
  JOURNAL   Biochim Biophys Acta 1633 (2), 127-131 (2003)
   PUBMED   12880872
REFERENCE   9  (residues 1 to 1191)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1191)
  AUTHORS   Abbott,W.M., Mellor,A., Edwards,Y. and Feizi,T.
  TITLE     Soluble bovine galactose-binding lectin. cDNA cloning reveals the
            complete amino acid sequence and an antigenic relationship with the
            major encephalitogenic domain of myelin basic protein
  JOURNAL   Biochem J 259 (1), 283-290 (1989)
   PUBMED   2470348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162591.16.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of
            aminophospholipid-transporting ATPases. The aminophospholipid
            translocases transport phosphatidylserine and
            phosphatidylethanolamine from one side of a bilayer to another.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.116486.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..1191
                     /product="phospholipid-transporting ATPase ID isoform d"
                     /EC_number="7.6.2.1"
                     /note="phospholipid-transporting ATPase ID; probable
                     phospholipid-transporting ATPase ID; ATPase, class I, type
                     8B, member 2; P4-ATPase flippase complex alpha subunit
                     ATP8B2; 36/8-9 fusion protein with epitope for anti-lectin
                     antibody; ATPase, aminophospholipid transporter, class I,
                     type 8B, member 2"
                     /calculated_mol_wt=135277
     Region          31..973
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            order(392..394,537,560..562,627,675..677,789,792,795,815,
                     818)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     CDS             1..1191
                     /gene="ATP8B2"
                     /gene_synonym="ATPID"
                     /coded_by="NM_001370596.1:216..3791"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:57198"
                     /db_xref="HGNC:HGNC:13534"
                     /db_xref="MIM:605867"
ORIGIN      
        1 mavcakkrpp eeerrarand reynekfqya snciktskyn iltflpvnlf eqfqevanty
       61 flfllilqli pqisslswft tivplvlvlt itavkdatdd yfrhksdnqv nnrqsqvlin
      121 gilqqeqwmn vcvgdiikle nnqfvaadll llsssephgl cyietaeldg etnmkvrqai
      181 pvtselgdis klakfdgevi ceppnnkldk fsgtlywken kfplsnqnml lrgcvlrnte
      241 wcfglvifag pdtklmqnsg rtkfkrtsid rlmntlvlwi fgflvcmgvi laignaiweh
      301 evgmrfqvyl pwdeavdsaf fsgflsfwsy iiilntvvpi slyvsvevir lghsyfinwd
      361 kkmfcmkkrt paeartttln eelgqveyif sdktgtltqn imvfnkcsin ghsygdvfdv
      421 lghkaelger pepvdfsfnp ladkkflfwd pslleavkig dphtheffrl lslchtvmse
      481 eknegelyyk aqspdegalv taarnfgfvf rsrtpktitv hemgtaityq llaildfnni
      541 rkrmsvivrn pegkirlyck gadtilldrl hhstqellnt tmdhlneyag eglrtlvlay
      601 kdldeeyyee waerrlqasl aqdsredrla siyeeeslwy fqllgataie dklqqgvpet
      661 ialltlanik iwvltgdkqe tavnigysck mltddmtevf ivtghtvlev reelrkarek
      721 mmdssrsvgn gftyqdklss skltsvleav ageyalving hslahalead melefletac
      781 ackaviccrv tplqkaqvve lvkkykkavt laigdgandv smiktahigv gisgqegiqa
      841 vlasdysfsq fkflqrlllv hgrwsylrmc kflcyffykn faftmvhfwf gffcgfsaqt
      901 vydqyfitly nivytslpvl amgvfdqdvp eqrsmeypkl yepgqlnllf nkrefficia
      961 qgiytsvlmf fipygvfada trddgtqlad yqsfavtvat slvivvsvqi gldtgywtai
     1021 nhffiwgsla vyfailfamh snglfdmfpn qfrfvgnaqn tlaqptvwlt ivlttvvcim
     1081 pvvafrflrl nlkpdlsdtv rytqlvrkkq kaqhrcmrrv grtgsrrsgy afshqegfge
     1141 limsgknmrl sslalssftt rsssswiesl rrkksdsass psggadkplk g
//
LOCUS       NP_001351698             532 aa            linear   ROD 27-APR-2025
DEFINITION  telomerase Cajal body protein 1 [Mus musculus].
ACCESSION   NP_001351698
VERSION     NP_001351698.1
DBSOURCE    REFSEQ: accession NM_001364769.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Guo,T., Han,X., He,J., Feng,J., Jing,J., Janeckova,E., Lei,J.,
            Ho,T.V., Xu,J. and Chai,Y.
  TITLE     KDM6B interacts with TFDP1 to activate P53 signaling in regulating
            mouse palatogenesis
  JOURNAL   Elife 11, e74595 (2022)
   PUBMED   35212626
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Chen,L., Roake,C.M., Freund,A., Batista,P.J., Tian,S., Yin,Y.A.,
            Gajera,C.R., Lin,S., Lee,B., Pech,M.F., Venteicher,A.S., Das,R.,
            Chang,H.Y. and Artandi,S.E.
  TITLE     An Activity Switch in Human Telomerase Based on RNA Conformation
            and Shaped by TCAB1
  JOURNAL   Cell 174 (1), 218-230 (2018)
   PUBMED   29804836
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Kannan,M., Bayam,E., Wagner,C., Rinaldi,B., Kretz,P.F., Tilly,P.,
            Roos,M., McGillewie,L., Bar,S., Minocha,S., Chevalier,C., Po,C.,
            Chelly,J., Mandel,J.L., Borgatti,R., Piton,A., Kinnear,C., Loos,B.,
            Adams,D.J., Herault,Y., Collins,S.C., Friant,S., Godin,J.D. and
            Yalcin,B.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     WD40-repeat 47, a microtubule-associated protein, is essential for
            brain development and autophagy
  JOURNAL   Proc Natl Acad Sci U S A 114 (44), E9308-E9317 (2017)
   PUBMED   29078390
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Sun,Y., Yang,C., Chen,J., Song,X., Li,Z., Duan,M., Li,J., Hu,X.,
            Wu,K., Yan,G., Yang,C., Liu,J., Tan,W. and Ye,M.
  TITLE     Overexpression of WDR79 in non-small cell lung cancer is linked to
            tumour progression
  JOURNAL   J Cell Mol Med 20 (4), 698-709 (2016)
   PUBMED   26849396
  REMARK    GeneRIF: Overexpression of WDR79 in non-small cell lung cancer is
            linked to tumor progression.
REFERENCE   7  (residues 1 to 532)
  AUTHORS   Mahmoudi,S., Henriksson,S., Corcoran,M., Mendez-Vidal,C.,
            Wiman,K.G. and Farnebo,M.
  TITLE     Wrap53, a natural p53 antisense transcript required for p53
            induction upon DNA damage
  JOURNAL   Mol Cell 33 (4), 462-471 (2009)
   PUBMED   19250907
  REMARK    Erratum:[Mol Cell. 2016 Dec 1;64(5):1009. doi:
            10.1016/j.molcel.2016.11.027. PMID: 27912092]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL731687.13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC069868.1, SRR7652917.1279647.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 42.81 cM"
     Protein         1..532
                     /product="telomerase Cajal body protein 1"
                     /note="WD repeat-containing protein 79; WD40
                     repeat-containing protein encoded by RNA antisense to p53;
                     WD repeat domain 79; WD repeat containing, antisense to
                     TP53; WD repeat-containing protein WRAP53; WD40
                     repeat-containing protein antisense to TP53 gene homolog"
                     /calculated_mol_wt=58020
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q8VC51.1)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          80..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          151..190
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          159..204
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <161..466
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          206..251
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          211..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          256..297
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          264..303
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          307..348
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          313..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          349..389
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          354..394
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          395..434
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          402..442
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q8VC51.1)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          510..532
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     CDS             1..532
                     /gene="Wrap53"
                     /gene_synonym="Wdr79"
                     /coded_by="NM_001364769.1:311..1909"
                     /db_xref="CCDS:CCDS24897.1"
                     /db_xref="GeneID:216853"
                     /db_xref="MGI:MGI:2384933"
ORIGIN      
        1 mktseerlla pdslppdlap apvpqgspae kntdfepvpp pcggddqpql atdpvaslvv
       61 sqelqqgdsv plevefntss elspgieeqd vsehaslpge etnlpelesg eategvseer
      121 aevdegdtfw tysfsqvpry lsgswsefst rsenflkgck wapdgscilt nsadnvlriy
      181 nlppelyseq eqvdyaemvp vlrmvegdti ydycwyslms stqpdtsyva sssrenpihi
      241 wdaftgelra sfraynhlde ltaahslcfs pdgsqlfcgf nrtvrvfsts rpgrdcevra
      301 tfakkqgqsg iisciafsps qplyacgsyg rtiglyawdd gsplallggh qggithlcfh
      361 pdgnlffsga rkdaellcwd lrqpghllws lsrevttnqr iyfdldpsgq flvsgntsgv
      421 vsvwdisgal sddsklepvv tflpqkdctn gvslhptlpl latasgqrvf peptnsgdeg
      481 elelelplls lchahpecql qlwwcgggpd psspvddqde kgqrrteavg ms
//
LOCUS       NP_001352179             491 aa            linear   PRI 27-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 2
            [Homo sapiens].
ACCESSION   NP_001352179
VERSION     NP_001352179.1
DBSOURCE    REFSEQ: accession NM_001365250.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Zhang,S., Huang,J., Lan,Z., Xiao,Y., Liao,Y., Basnet,S., Huang,P.,
            Li,Y., Yan,J., Sheng,Y., Zhou,W., Liu,Q., Tan,H., Tan,Y., Yuan,L.,
            Wang,L., Dai,L., Zhang,W. and Du,C.
  TITLE     CPEB1 Controls NRF2 Proteostasis and Ferroptosis Susceptibility in
            Pancreatic Cancer
  JOURNAL   Int J Biol Sci 20 (8), 3156-3172 (2024)
   PUBMED   38904009
  REMARK    GeneRIF: CPEB1 Controls NRF2 Proteostasis and Ferroptosis
            Susceptibility in Pancreatic Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Pico,S., Parras,A., Santos-Galindo,M., Pose-Utrilla,J., Castro,M.,
            Fraga,E., Hernandez,I.H., Elorza,A., Anta,H., Wang,N.,
            Marti-Sanchez,L., Belloc,E., Garcia-Esparcia,P., Garrido,J.J.,
            Ferrer,I., Macias-Garcia,D., Mir,P., Artuch,R., Perez,B.,
            Hernandez,F., Navarro,P., Lopez-Sendon,J.L., Iglesias,T.,
            Yang,X.W., Mendez,R. and Lucas,J.J.
  TITLE     CPEB alteration and aberrant transcriptome-polyadenylation lead to
            a treatable SLC19A3 deficiency in Huntington's disease
  JOURNAL   Sci Transl Med 13 (613), eabe7104 (2021)
   PUBMED   34586830
  REMARK    GeneRIF: CPEB alteration and aberrant transcriptome-polyadenylation
            lead to a treatable SLC19A3 deficiency in Huntington's disease.
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Shao,K., Pu,W., Zhang,J., Guo,S., Qian,F., Glurich,I., Jin,Q.,
            Ma,Y., Ju,S., Zhang,Z. and Ding,W.
  TITLE     DNA hypermethylation contributes to colorectal cancer metastasis by
            regulating the binding of CEBPB and TFCP2 to the CPEB1 promoter
  JOURNAL   Clin Epigenetics 13 (1), 89 (2021)
   PUBMED   33892791
  REMARK    GeneRIF: DNA hypermethylation contributes to colorectal cancer
            metastasis by regulating the binding of CEBPB and TFCP2 to the
            CPEB1 promoter.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Sovijit,W., Sovijit,W., Ishii,Y., Kambe,J., Fujita,T., Watanabe,G.,
            Yamaguchi,H. and Nagaoka,K.
  TITLE     Estrogen promotes increased breast cancer cell proliferation and
            migration through downregulation of CPEB1 expression
  JOURNAL   Biochem Biophys Res Commun 534, 871-876 (2021)
   PUBMED   33162033
  REMARK    GeneRIF: Estrogen promotes increased breast cancer cell
            proliferation and migration through downregulation of CPEB1
            expression.
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Jiao,W., Zhao,S., Liu,R., Guo,T. and Qin,Y.
  TITLE     CPEB1 deletion is not a common explanation for premature ovarian
            insufficiency in a Chinese cohort
  JOURNAL   J Ovarian Res 13 (1), 49 (2020)
   PUBMED   32354341
  REMARK    GeneRIF: CPEB1 deletion is not a common explanation for premature
            ovarian insufficiency in a Chinese cohort.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Hagele,S., Kuhn,U., Boning,M. and Katschinski,D.M.
  TITLE     Cytoplasmic polyadenylation-element-binding protein (CPEB)1 and 2
            bind to the HIF-1alpha mRNA 3'-UTR and modulate HIF-1alpha protein
            expression
  JOURNAL   Biochem J 417 (1), 235-246 (2009)
   PUBMED   18752464
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Sasayama,T., Marumoto,T., Kunitoku,N., Zhang,D., Tamaki,N.,
            Kohmura,E., Saya,H. and Hirota,T.
  TITLE     Over-expression of Aurora-A targets cytoplasmic polyadenylation
            element binding protein and promotes mRNA polyadenylation of Cdk1
            and cyclin B1
  JOURNAL   Genes Cells 10 (7), 627-638 (2005)
   PUBMED   15966895
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Wilczynska,A., Aigueperse,C., Kress,M., Dautry,F. and Weil,D.
  TITLE     The translational regulator CPEB1 provides a link between dcp1
            bodies and stress granules
  JOURNAL   J Cell Sci 118 (Pt 5), 981-992 (2005)
   PUBMED   15731006
  REMARK    GeneRIF: CPEB1 has a role in compartmentalization of mRNA
            metabolism in the cytoplasm, between dcp1 bodies and stress
            granules
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Mendez,R. and Richter,J.D.
  TITLE     Translational control by CPEB: a means to the end
  JOURNAL   Nat Rev Mol Cell Biol 2 (7), 521-529 (2001)
   PUBMED   11433366
  REMARK    Review article
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Welk,J.F., Charlesworth,A., Smith,G.D. and MacNicol,A.M.
  TITLE     Identification and characterization of the gene encoding human
            cytoplasmic polyadenylation element binding protein
  JOURNAL   Gene 263 (1-2), 113-120 (2001)
   PUBMED   11223249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245033.2.
            
            Summary: This gene encodes a member of the cytoplasmic
            polyadenylation element binding protein family. This highly
            conserved protein binds to a specific RNA sequence, called the
            cytoplasmic polyadenylation element, found in the 3' untranslated
            region of some mRNAs. The encoded protein functions in both the
            cytoplasm and the nucleus. It is involved in the regulation of mRNA
            translation, as well as processing of the 3' untranslated region,
            and may play a role in cell proliferation and tumorigenesis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.123673.1,
                                           SRR1803615.260728.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..491
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 2"
                     /note="CPE-binding protein 1"
                     /calculated_mol_wt=54032
     Region          <1..232
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          234..341
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          352..435
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          429..484
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..491
                     /gene="CPEB1"
                     /gene_synonym="CPE-BP1; CPEB; CPEB-1; h-CPEB; hCPEB-1"
                     /coded_by="NM_001365250.1:201..1676"
                     /note="isoform 2 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS42072.2"
                     /db_xref="GeneID:64506"
                     /db_xref="HGNC:HGNC:21744"
                     /db_xref="MIM:607342"
ORIGIN      
        1 mlfptsaqes srglpdandl clglqslslt gwdrpwstqd sdssaqssth svlsmlhnpl
       61 gnvlgkppls flpldplgsd lvdkfpapsv rgsrldtrpi ldsrssspsd sdtsgfssgs
      121 dhlsdlissl rispplpfls lsgggprdpl kmgvgsrmdq eqaalaavtp sptsaskrwp
      181 gasvwpswdl leapkdpfsi erearlhrqa aavneatctw sgqlpprnyk npiysckvfl
      241 ggvpwditea glvntfrvfg slsvewpgkd gkhprcppkg nmpkgyvylv feleksvrsl
      301 lqacshdpls pdglseyyfk mssrrmrcke vqvipwvlad snfvrspsqr ldpsrtvfvg
      361 alhgmlnaea laailndlfg gvvyagidtd khkypigsgr vtfnnqrsyl kavsaafvei
      421 kttkftkkvq idpyledslc hicssqpgpf fcrdqvcfky fcrscwhwrh smeglrhhsp
      481 lmrnqknrds s
//
LOCUS       NP_001028445             404 aa            linear   ROD 27-APR-2025
DEFINITION  uncharacterized protein KIAA0930 homolog isoform 2 [Mus musculus].
ACCESSION   NP_001028445 XP_128281 XP_907045 XP_907051 XP_916374 XP_927052
VERSION     NP_001028445.2
DBSOURCE    REFSEQ: accession NM_001033273.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Ling,K.H., Hewitt,C.A., Beissbarth,T., Hyde,L., Banerjee,K.,
            Cheah,P.S., Cannon,P.Z., Hahn,C.N., Thomas,P.Q., Smyth,G.K.,
            Tan,S.S., Thomas,T. and Scott,H.S.
  TITLE     Molecular networks involved in mouse cerebral corticogenesis and
            spatio-temporal regulation of Sox4 and Sox11 novel antisense
            transcripts revealed by transcriptome profiling
  JOURNAL   Genome Biol 10 (10), R104 (2009)
   PUBMED   19799774
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL513352.12.
            
            On Feb 14, 2019 this sequence version replaced NP_001028445.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK149782.1, AK170532.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164137
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 40.25 cM"
     Protein         1..404
                     /product="uncharacterized protein KIAA0930 homolog isoform
                     2"
                     /calculated_mol_wt=45829
     Region          30..258
                     /region_name="DUF2045"
                     /note="Uncharacterized conserved protein (DUF2045);
                     pfam09741"
                     /db_xref="CDD:462872"
     Region          262..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UE31.2)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ICG6; propagated from
                     UniProtKB/Swiss-Prot (Q3UE31.2)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UE31.2)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UE31.2)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UE31.2)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UE31.2)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ICG6; propagated from
                     UniProtKB/Swiss-Prot (Q3UE31.2)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ICG6; propagated from
                     UniProtKB/Swiss-Prot (Q3UE31.2)"
     Region          319..340
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UE31.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UE31.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4G008; propagated from
                     UniProtKB/Swiss-Prot (Q3UE31.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ICG6; propagated from
                     UniProtKB/Swiss-Prot (Q3UE31.2)"
     CDS             1..404
                     /gene="5031439G07Rik"
                     /gene_synonym="mKIAA0930"
                     /coded_by="NM_001033273.3:300..1514"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS27715.2"
                     /db_xref="GeneID:223739"
                     /db_xref="MGI:MGI:2444899"
ORIGIN      
        1 mlraiaeerg rlslrrevcg lgcfkddriv fwtwmfstyf meklaprqdd mlfyvrrkra
       61 ypgnegtidg rkaeaepeve vevyrrdskk lpglgdpdid weesvclnli lqkldymvtc
      121 avctradggd ihihrkksqq vfaspskhpm dskgeeskms ypniffmids feevfsdmtv
      181 gegemvcvel vasdktntfq gvifqgsiry ealkkvydnr vsvaarmaqk msfgfykynn
      241 mefvrmkgpq gkghaemavs rvstgdtspc gtedsspasp mhervtsfst pptpernnrp
      301 affspslkrk vprnriaemk kshsandsee ffreddsgad lhnatnlrsr slsgtgrslv
      361 gswlklnrad gnfllyahlt yvtlplhril tdilevrqkp ilmt
//
LOCUS       NP_000957                454 aa            linear   PRI 27-APR-2025
DEFINITION  retinoic acid receptor gamma isoform 1 [Homo sapiens].
ACCESSION   NP_000957 XP_352903
VERSION     NP_000957.1
DBSOURCE    REFSEQ: accession NM_000966.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Li,X.M., Yang,Y., Jiang,F.Q., Hu,G., Wan,S., Yan,W.Y., He,X.S.,
            Xiao,F., Yang,X.M., Guo,X., Lu,J.H., Yang,X.Q., Chen,J.J., Ye,W.L.,
            Liu,Y., He,K., Duan,H.X., Zhou,Y.J., Gan,W.J., Liu,F. and Wu,H.
  TITLE     Histone lactylation inhibits RARgamma expression in macrophages to
            promote colorectal tumorigenesis through activation of
            TRAF6-IL-6-STAT3 signaling
  JOURNAL   Cell Rep 43 (2), 113688 (2024)
   PUBMED   38245869
  REMARK    GeneRIF: Histone lactylation inhibits RARgamma expression in
            macrophages to promote colorectal tumorigenesis through activation
            of TRAF6-IL-6-STAT3 signaling.
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Gunduz,A., Duman,D., Basbinar,Y., Tasdelen,B., Kupeli,S. and
            Karpuz,D.
  TITLE     The Role of RARG rs2229774, SLC28A3 rs7853758, and UGT1A6*4
            rs17863783 Single-nucleotide Polymorphisms in the
            Doxorubicin-induced Cardiotoxicity in Solid Childhood Tumors
  JOURNAL   J Pediatr Hematol Oncol 46 (1), e65-e70 (2024)
   PUBMED   37828659
  REMARK    GeneRIF: The Role of RARG rs2229774, SLC28A3 rs7853758, and
            UGT1A6*4 rs17863783 Single-nucleotide Polymorphisms in the
            Doxorubicin-induced Cardiotoxicity in Solid Childhood Tumors.
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Zhang,F.X., Xu,P., Zhang,L.J., Fan,R., Zhang,H.X., Liu,D.H., Liu,K.
            and Shen,D.Y.
  TITLE     RARgamma promotes the invasion and metastasis of thyroid carcinoma
            by activating the JAK1-STAT3-CD24/MMPs axis
  JOURNAL   Int Immunopharmacol 125 (Pt A), 111129 (2023)
   PUBMED   37897947
  REMARK    GeneRIF: RARgamma promotes the invasion and metastasis of thyroid
            carcinoma by activating the JAK1-STAT3-CD24/MMPs axis.
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Ji,K., Dou,W., Zhang,N., Wen,B., Zhong,M., Zhang,Q., Xu,S., Zhou,J.
            and Liu,J.
  TITLE     Retinoic acid receptor gamma is required for proliferation of
            pancreatic cancer cells
  JOURNAL   Cell Biol Int 47 (1), 144-155 (2023)
   PUBMED   36183362
  REMARK    GeneRIF: Retinoic acid receptor gamma is required for proliferation
            of pancreatic cancer cells.
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Homma,H., Watanabe,M., Inoue,N., Isono,M., Hidaka,Y. and Iwatani,Y.
  TITLE     Polymorphisms in Vitamin A-Related Genes and Their Functions in
            Autoimmune Thyroid Disease
  JOURNAL   Thyroid 31 (11), 1749-1756 (2021)
   PUBMED   34470463
  REMARK    GeneRIF: Polymorphisms in Vitamin A-Related Genes and Their
            Functions in Autoimmune Thyroid Disease.
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Lehmann,J.M., Zhang,X.K. and Pfahl,M.
  TITLE     RAR gamma 2 expression is regulated through a retinoic acid
            response element embedded in Sp1 sites
  JOURNAL   Mol Cell Biol 12 (7), 2976-2985 (1992)
   PUBMED   1320193
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Vollberg,T.M. Sr., Nervi,C., George,M.D., Fujimoto,W., Krust,A. and
            Jetten,A.M.
  TITLE     Retinoic acid receptors as regulators of human epidermal
            keratinocyte differentiation
  JOURNAL   Mol Endocrinol 6 (5), 667-676 (1992)
   PUBMED   1318502
REFERENCE   8  (residues 1 to 454)
  AUTHORS   Leid,M., Kastner,P., Lyons,R., Nakshatri,H., Saunders,M.,
            Zacharewski,T., Chen,J.Y., Staub,A., Garnier,J.M., Mader,S. et al.
  TITLE     Purification, cloning, and RXR identity of the HeLa cell factor
            with which RAR or TR heterodimerizes to bind target sequences
            efficiently
  JOURNAL   Cell 68 (2), 377-395 (1992)
   PUBMED   1310259
  REMARK    Erratum:[Cell. 1992 Nov 27;71(5):887. PMID: 1330328]
REFERENCE   9  (residues 1 to 454)
  AUTHORS   Mattei,M.G., Riviere,M., Krust,A., Ingvarsson,S., Vennstrom,B.,
            Islam,M.Q., Levan,G., Kautner,P., Zelent,A., Chambon,P. et al.
  TITLE     Chromosomal assignment of retinoic acid receptor (RAR) genes in the
            human, mouse, and rat genomes
  JOURNAL   Genomics 10 (4), 1061-1069 (1991)
   PUBMED   1655630
REFERENCE   10 (residues 1 to 454)
  AUTHORS   Lehmann,J.M., Hoffmann,B. and Pfahl,M.
  TITLE     Genomic organization of the retinoic acid receptor gamma gene
  JOURNAL   Nucleic Acids Res 19 (3), 573-578 (1991)
   PUBMED   1849262
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA436501.1 and BC072462.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 18, 2003 this sequence version replaced XP_352903.1.
            
            Summary: This gene encodes a retinoic acid receptor that belongs to
            the nuclear hormone receptor family. Retinoic acid receptors (RARs)
            act as ligand-dependent transcriptional regulators. When bound to
            ligands, RARs activate transcription by binding as heterodimers to
            the retinoic acid response elements (RARE) found in the promoter
            regions of the target genes. In their unbound form, RARs repress
            transcription of their target genes. RARs are involved in various
            biological processes, including limb bud development, skeletal
            growth, and matrix homeostasis. Alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072462.1, SRR14038194.390989.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000425354.7/ ENSP00000388510.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..454
                     /product="retinoic acid receptor gamma isoform 1"
                     /note="RAR-gamma; nuclear receptor subfamily 1 group B
                     member 3"
                     /calculated_mol_wt=50211
     Region          1..89
                     /region_name="Modulating"
                     /note="propagated from UniProtKB/Swiss-Prot (P13631.1)"
     Site            34
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P18911; propagated from
                     UniProtKB/Swiss-Prot (P13631.1)"
     Region          58..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13631.1)"
     Region          85..165
                     /region_name="NR_DBD_RAR"
                     /note="DNA-binding domain of retinoic acid receptor (RAR)
                     is composed of two C4-type zinc fingers; cd06964"
                     /db_xref="CDD:143522"
     Site            order(90,93,107,110,126,132,142,145)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143522"
     Site            order(100..102,108..109,111,113,115..116,119,139..140,143,
                     146,159..161)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143522"
     Site            order(137,140..143)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:143522"
     Region          156..184
                     /region_name="Hinge"
                     /note="propagated from UniProtKB/Swiss-Prot (P13631.1)"
     Region          161..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13631.1)"
     Region          188..418
                     /region_name="NR_LBD_RAR"
                     /note="The ligand binding domain (LBD) of retinoic acid
                     receptor (RAR), a members of the nuclear receptor
                     superfamily; cd06937"
                     /db_xref="CDD:132735"
     Site            order(230,233..234,237,268,271..272,275,278,288..289,304,
                     396..397,400,416)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132735"
     Site            order(242,246,256,259..260,263..264,410..411,414..415)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132735"
     Site            order(317,339..340,351,354..355,358..359,362,366,377..378,
                     380..381,384,387..388)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:132735"
     Region          408..454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13631.1)"
     CDS             1..454
                     /gene="RARG"
                     /gene_synonym="NR1B3; RARC; RARgamma"
                     /coded_by="NM_000966.6:446..1810"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8850.1"
                     /db_xref="GeneID:5916"
                     /db_xref="HGNC:HGNC:9866"
                     /db_xref="MIM:180190"
ORIGIN      
        1 matnkerlfa agalgpgsgy pgagfpfafp galrgsppfe mlspsfrglg qpdlpkemas
       61 lsvetqstss eemvpsspsp pppprvykpc fvcndkssgy hygvsscegc kgffrrsiqk
      121 nmvytchrdk nciinkvtrn rcqycrlqkc fevgmskeav rndrnkkkke vkeegspdsy
      181 elspqleeli tkvskahqet fpslcqlgky ttnssadhrv qldlglwdkf selatkciik
      241 ivefakrlpg ftglsiadqi tllkaacldi lmlrictryt peqdtmtfsd gltlnrtqmh
      301 nagfgpltdl vfafagqllp lemddtetgl lsaiclicgd rmdleepekv dklqepllea
      361 lrlyarrrrp sqpymfprml mkitdlrgis tkgaeraitl kmeipgpmpp liremlenpe
      421 mfeddssqpg phpnassede vpggqgkggl kspa
//
LOCUS       NP_005992                450 aa            linear   PRI 27-APR-2025
DEFINITION  tubulin alpha-3C chain [Homo sapiens].
ACCESSION   NP_005992
VERSION     NP_005992.1
DBSOURCE    REFSEQ: accession NM_006001.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Bhagwat,S., Dalvi,V., Chandrasekhar,D., Matthew,T., Acharya,K.,
            Gajbhiye,R., Kulkarni,V., Sonawane,S., Ghosalkar,M. and Parte,P.
  TITLE     Acetylated alpha-tubulin is reduced in individuals with poor sperm
            motility
  JOURNAL   Fertil Steril 101 (1), 95-104 (2014)
   PUBMED   24268707
  REMARK    GeneRIF: TUBA3C (and TUBA4A) are differentially expressed in
            individuals with poor sperm motility.
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Manning,A.K., Hivert,M.F., Scott,R.A., Grimsby,J.L.,
            Bouatia-Naji,N., Chen,H., Rybin,D., Liu,C.T., Bielak,L.F.,
            Prokopenko,I., Amin,N., Barnes,D., Cadby,G., Hottenga,J.J.,
            Ingelsson,E., Jackson,A.U., Johnson,T., Kanoni,S., Ladenvall,C.,
            Lagou,V., Lahti,J., Lecoeur,C., Liu,Y., Martinez-Larrad,M.T.,
            Montasser,M.E., Navarro,P., Perry,J.R., Rasmussen-Torvik,L.J.,
            Salo,P., Sattar,N., Shungin,D., Strawbridge,R.J., Tanaka,T., van
            Duijn,C.M., An,P., de Andrade,M., Andrews,J.S., Aspelund,T.,
            Atalay,M., Aulchenko,Y., Balkau,B., Bandinelli,S., Beckmann,J.S.,
            Beilby,J.P., Bellis,C., Bergman,R.N., Blangero,J., Boban,M.,
            Boehnke,M., Boerwinkle,E., Bonnycastle,L.L., Boomsma,D.I.,
            Borecki,I.B., Bottcher,Y., Bouchard,C., Brunner,E., Budimir,D.,
            Campbell,H., Carlson,O., Chines,P.S., Clarke,R., Collins,F.S.,
            Corbaton-Anchuelo,A., Couper,D., de Faire,U., Dedoussis,G.V.,
            Deloukas,P., Dimitriou,M., Egan,J.M., Eiriksdottir,G., Erdos,M.R.,
            Eriksson,J.G., Eury,E., Ferrucci,L., Ford,I., Forouhi,N.G.,
            Fox,C.S., Franzosi,M.G., Franks,P.W., Frayling,T.M., Froguel,P.,
            Galan,P., de Geus,E., Gigante,B., Glazer,N.L., Goel,A., Groop,L.,
            Gudnason,V., Hallmans,G., Hamsten,A., Hansson,O., Harris,T.B.,
            Hayward,C., Heath,S., Hercberg,S., Hicks,A.A., Hingorani,A.,
            Hofman,A., Hui,J., Hung,J., Jarvelin,M.R., Jhun,M.A., Johnson,P.C.,
            Jukema,J.W., Jula,A., Kao,W.H., Kaprio,J., Kardia,S.L.,
            Keinanen-Kiukaanniemi,S., Kivimaki,M., Kolcic,I., Kovacs,P.,
            Kumari,M., Kuusisto,J., Kyvik,K.O., Laakso,M., Lakka,T.,
            Lannfelt,L., Lathrop,G.M., Launer,L.J., Leander,K., Li,G., Lind,L.,
            Lindstrom,J., Lobbens,S., Loos,R.J., Luan,J., Lyssenko,V., Magi,R.,
            Magnusson,P.K., Marmot,M., Meneton,P., Mohlke,K.L., Mooser,V.,
            Morken,M.A., Miljkovic,I., Narisu,N., O'Connell,J., Ong,K.K.,
            Oostra,B.A., Palmer,L.J., Palotie,A., Pankow,J.S., Peden,J.F.,
            Pedersen,N.L., Pehlic,M., Peltonen,L., Penninx,B., Pericic,M.,
            Perola,M., Perusse,L., Peyser,P.A., Polasek,O., Pramstaller,P.P.,
            Province,M.A., Raikkonen,K., Rauramaa,R., Rehnberg,E., Rice,K.,
            Rotter,J.I., Rudan,I., Ruokonen,A., Saaristo,T., Sabater-Lleal,M.,
            Salomaa,V., Savage,D.B., Saxena,R., Schwarz,P., Seedorf,U.,
            Sennblad,B., Serrano-Rios,M., Shuldiner,A.R., Sijbrands,E.J.,
            Siscovick,D.S., Smit,J.H., Small,K.S., Smith,N.L., Smith,A.V.,
            Stancakova,A., Stirrups,K., Stumvoll,M., Sun,Y.V., Swift,A.J.,
            Tonjes,A., Tuomilehto,J., Trompet,S., Uitterlinden,A.G.,
            Uusitupa,M., Vikstrom,M., Vitart,V., Vohl,M.C., Voight,B.F.,
            Vollenweider,P., Waeber,G., Waterworth,D.M., Watkins,H.,
            Wheeler,E., Widen,E., Wild,S.H., Willems,S.M., Willemsen,G.,
            Wilson,J.F., Witteman,J.C., Wright,A.F., Yaghootkar,H.,
            Zelenika,D., Zemunik,T., Zgaga,L., Wareham,N.J., McCarthy,M.I.,
            Barroso,I., Watanabe,R.M., Florez,J.C., Dupuis,J., Meigs,J.B. and
            Langenberg,C.
  CONSRTM   DIAbetes Genetics Replication And Meta-analysis (DIAGRAM)
            Consortium; Multiple Tissue Human Expression Resource (MUTHER)
            Consortium
  TITLE     A genome-wide approach accounting for body mass index identifies
            genetic variants influencing fasting glycemic traits and insulin
            resistance
  JOURNAL   Nat Genet 44 (6), 659-669 (2012)
   PUBMED   22581228
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 450)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Dode,C., Weil,D., Levilliers,J., Crozet,F., Chaib,H.,
            Levi-Acobas,F., Guilford,P. and Petit,C.
  TITLE     Sequence characterization of a newly identified human alpha-tubulin
            gene (TUBA2)
  JOURNAL   Genomics 47 (1), 125-130 (1998)
   PUBMED   9465305
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Crepieux,P., Kwon,H., Leclerc,N., Spencer,W., Richard,S., Lin,R.
            and Hiscott,J.
  TITLE     I kappaB alpha physically interacts with a cytoskeleton-associated
            protein through its signal response domain
  JOURNAL   Mol Cell Biol 17 (12), 7375-7385 (1997)
   PUBMED   9372968
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Marie-Cardine,A., Kirchgessner,H., Eckerskorn,C., Meuer,S.C. and
            Schraven,B.
  TITLE     Human T lymphocyte activation induces tyrosine phosphorylation of
            alpha-tubulin and its association with the SH2 domain of the p59fyn
            protein tyrosine kinase
  JOURNAL   Eur J Immunol 25 (12), 3290-3297 (1995)
   PUBMED   8566014
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Guilford,P., Dode,C., Crozet,F., Blanchard,S., Chaib,H.,
            Levilliers,J., Levi-Acobas,F., Weil,D., Weissenbach,J., Cohen,D. et
            al.
  TITLE     A YAC contig and an EST map in the pericentromeric region of
            chromosome 13 surrounding the loci for neurosensory nonsyndromic
            deafness (DFNB1 and DFNA3) and limb-girdle muscular dystrophy type
            2C (LGMD2C)
  JOURNAL   Genomics 29 (1), 163-169 (1995)
   PUBMED   8530067
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Alexandrova,N., Niklinski,J., Bliskovsky,V., Otterson,G.A.,
            Blake,M., Kaye,F.J. and Zajac-Kaye,M.
  TITLE     The N-terminal domain of c-Myc associates with alpha-tubulin and
            microtubules in vivo and in vitro
  JOURNAL   Mol Cell Biol 15 (9), 5188-5195 (1995)
   PUBMED   7651436
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB026664.1, AL139327.18,
            DB524026.1 and AA412719.1.
            
            Summary: Microtubules of the eukaryotic cytoskeleton perform
            essential and diverse functions and are composed of a heterodimer
            of alpha and beta tubulin. The genes encoding these microtubule
            constituents are part of the tubulin superfamily, which is composed
            of six distinct families. Genes from the alpha, beta and gamma
            tubulin families are found in all eukaryotes. The alpha and beta
            tubulins represent the major components of microtubules, while
            gamma tubulin plays a critical role in the nucleation of
            microtubule assembly. There are multiple alpha and beta tubulin
            genes and they are highly conserved among and between species. This
            gene is an alpha tubulin gene that encodes a protein 99% identical
            to the mouse testis-specific Tuba3 and Tuba7 gene products. This
            gene is located in the 13q11 region, which is associated with the
            genetic diseases Clouston hidrotic ectodermal dysplasia and Kabuki
            syndrome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.139094.1,
                                           SRR5189667.143419.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000400113.8/ ENSP00000382982.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..450
                     /product="tubulin alpha-3C chain"
                     /note="tubulin, alpha 2; tubulin alpha-3C/D chain; Tubulin
                     alpha-3D chain; alpha-tubulin 3C; alpha-tubulin 2;
                     alpha-tubulin 3C/D; tubulin alpha-2 chain; Alpha-tubulin
                     3D"
                     /calculated_mol_wt=49829
     Region          1..440
                     /region_name="PTZ00335"
                     /note="tubulin alpha chain; Provisional"
                     /db_xref="CDD:185562"
     Region          1..4
                     /region_name="MREC motif.
                     /evidence=ECO:0000250|UniProtKB:P68363"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DPH7.1)"
     Site            40
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24906155; propagated from
                     UniProtKB/Swiss-Prot (P0DPH7.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P68373; propagated from
                     UniProtKB/Swiss-Prot (P0DPH7.1)"
     Site            450
                     /site_type="other"
                     /note="Involved in polymerization; propagated from
                     UniProtKB/Swiss-Prot (P0DPH7.1)"
     CDS             1..450
                     /gene="TUBA3C"
                     /gene_synonym="bA408E5.3; TUBA2"
                     /coded_by="NM_006001.3:78..1430"
                     /db_xref="CCDS:CCDS9284.1"
                     /db_xref="GeneID:7278"
                     /db_xref="HGNC:HGNC:12408"
                     /db_xref="MIM:602528"
ORIGIN      
        1 mrecisihvg qagvqignac welyclehgi qpdgqmpsdk tigggddsfn tffsetgagk
       61 hvpravfvdl eptvvdevrt gtyrqlfhpe qlitgkedaa nnyarghyti gkeivdlvld
      121 rirkladlct glqgflifhs fgggtgsgfa sllmerlsvd ygkksklefa iypapqvsta
      181 vvepynsilt thttlehsdc afmvdneaiy dicrrnldie rptytnlnrl igqivssita
      241 slrfdgalnv dltefqtnlv pyprihfpla tyapvisaek ayheqlsvae itnacfepan
      301 qmvkcdprhg kymaccmlyr gdvvpkdvna aiatiktkrt iqfvdwcptg fkvginyqpp
      361 tvvpggdlak vqravcmlsn ttaiaeawar ldhkfdlmya krafvhwyvg egmeegefse
      421 aredlaalek dyeevgvdsv eaeaeegeey
//
LOCUS       NP_009103                468 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear pore complex protein Nup50 isoform b [Homo sapiens].
ACCESSION   NP_009103
VERSION     NP_009103.2
DBSOURCE    REFSEQ: accession NM_007172.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Smitherman,M., Lee,K., Swanger,J., Kapur,R. and Clurman,B.E.
  TITLE     Characterization and targeted disruption of murine Nup50, a
            p27(Kip1)-interacting component of the nuclear pore complex
  JOURNAL   Mol Cell Biol 20 (15), 5631-5642 (2000)
   PUBMED   10891500
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Guan,T., Kehlenbach,R.H., Schirmer,E.C., Kehlenbach,A., Fan,F.,
            Clurman,B.E., Arnheim,N. and Gerace,L.
  TITLE     Nup50, a nucleoplasmically oriented nucleoporin with a role in
            nuclear protein export
  JOURNAL   Mol Cell Biol 20 (15), 5619-5630 (2000)
   PUBMED   10891499
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Trichet,V., Shkolny,D., Dunham,I., Beare,D. and McDermid,H.E.
  TITLE     Mapping and complex expression pattern of the human NPAP60L
            nucleoporin gene
  JOURNAL   Cytogenet Cell Genet 85 (3-4), 221-226 (1999)
   PUBMED   10449902
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z82243.1, BC070133.1 and
            AL008718.23.
            
            On Nov 3, 2002 this sequence version replaced NP_009103.1.
            
            Summary: The nuclear pore complex is a massive structure that
            extends across the nuclear envelope, forming a gateway that
            regulates the flow of macromolecules between the nucleus and the
            cytoplasm. Nucleoporins are the main components of the nuclear pore
            complex in eukaryotic cells. The protein encoded by this gene is a
            member of the FG-repeat containing nucleoporins that functions as a
            soluble cofactor in importin-alpha:beta-mediated nuclear protein
            import. Pseudogenes of this gene are found on chromosomes 5, 6, and
            14. Two transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) represents the longer
            transcript and encodes the longer isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.49356.1,
                                           SRR1660809.157675.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000347635.9/ ENSP00000345895.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..468
                     /product="nuclear pore complex protein Nup50 isoform b"
                     /note="nuclear pore-associated protein 60L; nuclear pore
                     complex protein Nup50; nucleoporin Nup50; 50 kDa
                     nucleoporin; nucleoporin 50kD; nucleoporin 50kDa"
                     /calculated_mol_wt=50013
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          2..67
                     /region_name="NUP50"
                     /note="NUP50 (Nucleoporin 50 kDa); pfam08911"
                     /db_xref="CDD:462629"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH2; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          76..304
                     /region_name="5 X 2 AA repeats of F-G"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            83
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          122..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH2; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          144..206
                     /region_name="Binding to CDKN1B. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          201..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH2; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          238..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          304..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          350..466
                     /region_name="RanBD_NUP50"
                     /note="Nucleoporin 50 Ran-binding domain; cd13170"
                     /db_xref="CDD:269991"
     Site            order(364,366..368,372..376,392,394,396..397,402..404,407,
                     409,413,417,425,427,444,448)
                     /site_type="other"
                     /note="putative RAN binding site [polypeptide binding]"
                     /db_xref="CDD:269991"
     Site            450
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH2; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     CDS             1..468
                     /gene="NUP50"
                     /gene_synonym="NPAP60; NPAP60L"
                     /coded_by="NM_007172.4:383..1789"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS14062.1"
                     /db_xref="GeneID:10762"
                     /db_xref="HGNC:HGNC:8065"
                     /db_xref="MIM:604646"
ORIGIN      
        1 makrnaekel tdrnwdqede aeevgtfsma seevlknrai kkakrrnvgf esdtggafkg
       61 fkglvvpsgg grfsgfgsga ggkpleglsn gnnitsappf asakaaadpk vafgslaang
      121 pttlvdkvsn pktngdsqqp sssglasska cvgnayhkql aalncsvrdw ivkhvntnpl
      181 cdltpifkdy ekylanieqq hgnsgrnses esnkvaaetq spslfgstkl qqestflfhg
      241 nktedtpdkk mevasekktd psslgatsas fnfgkkvdss vlgslssvpl tgfsfspgns
      301 slfgkdttqs kpvsspfptk plegqaegds geckggdeee ndeppkvvvt evkeedafys
      361 kkcklfykkd nefkekgigt lhlkptanqk tqllvradtn lgnillnvli ppnmpctrtg
      421 knnvlivcvp nppideknat mpvtmlirvk tsedadelhk illekkda
//
LOCUS       NP_001350296             192 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding protein 48 isoform 3 [Homo sapiens].
ACCESSION   NP_001350296 XP_024302735
VERSION     NP_001350296.1
DBSOURCE    REFSEQ: accession NM_001363367.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Siebert,A.E., Corll,J., Paige Gronevelt,J., Levine,L., Hobbs,L.M.,
            Kenney,C., Powell,C.L.E., Battistuzzi,F.U., Davenport,R., Mark
            Settles,A., Brad Barbazuk,W., Westrick,R.J., Madlambayan,G.J. and
            Lal,S.
  TITLE     Genetic analysis of human RNA binding motif protein 48 (RBM48)
            reveals an essential role in U12-type intron splicing
  JOURNAL   Genetics 222 (2) (2022)
   PUBMED   36040194
  REMARK    GeneRIF: Genetic analysis of human RNA binding motif protein 48
            (RBM48) reveals an essential role in U12-type intron splicing.
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC044570.1, DC319375.1, AC007566.2, AC005156.1 and BX113088.1.
            
            On May 17, 2018 this sequence version replaced XP_024302735.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.19909.1,
                                           SRR1660807.132184.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..192
                     /product="RNA-binding protein 48 isoform 3"
                     /note="UPF0712 protein C7orf64; RNA-binding protein 48"
                     /calculated_mol_wt=21326
     CDS             1..192
                     /gene="RBM48"
                     /gene_synonym="C7orf64; HSPC304"
                     /coded_by="NM_001363367.1:709..1287"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84060"
                     /db_xref="HGNC:HGNC:21785"
                     /db_xref="MIM:621015"
ORIGIN      
        1 msgfckaaln tsagnsnpyl pyscelplcy fsskcmcssg gpvdrapdss kdgrnhhktm
       61 ghynhndslr ktqinslkns vacpgaqkai tsseavdrfm prttqlqerk rrreddrklg
      121 tflqtnptgn eimigpllpd iskvdmhdds lnttanlirh klkevissvp kppedkpedv
      181 htshplkqrr ri
//
LOCUS       NP_612450                522 aa            linear   PRI 27-APR-2025
DEFINITION  cyclic GMP-AMP synthase isoform 1 [Homo sapiens].
ACCESSION   NP_612450
VERSION     NP_612450.2
DBSOURCE    REFSEQ: accession NM_138441.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Zhang,X., He,B., Lu,J., Bao,Q., Wang,J. and Yang,Y.
  TITLE     The crucial roles and research advances of cGAS-STING pathway in
            liver diseases
  JOURNAL   Ann Med 56 (1), 2394588 (2024)
   PUBMED   39183465
  REMARK    GeneRIF: The crucial roles and research advances of cGAS-STING
            pathway in liver diseases.
            Review article
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Soh,L.J., Lee,S.Y., Roebuck,M.M. and Wong,P.F.
  TITLE     Unravelling the interplay between ER stress, UPR and the cGAS-STING
            pathway: Implications for osteoarthritis pathogenesis and treatment
            strategy
  JOURNAL   Life Sci 357, 123112 (2024)
   PUBMED   39378929
  REMARK    GeneRIF: Unravelling the interplay between ER stress, UPR and the
            cGAS-STING pathway: Implications for osteoarthritis pathogenesis
            and treatment strategy.
            Review article
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Lant,S., Hood,A.J.M., Holley,J.A., Ellis,A., Eke,L., Sumner,R.P.,
            Ulaeto,D.O. and Maluquer de Motes,C.
  TITLE     Poxin-deficient poxviruses are sensed by cGAS prior to genome
            replication
  JOURNAL   J Gen Virol 105 (10) (2024)
   PUBMED   39431915
  REMARK    GeneRIF: Poxin-deficient poxviruses are sensed by cGAS prior to
            genome replication.
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Li,H., Liu,C., Li,R., Zhou,L., Ran,Y., Yang,Q., Huang,H., Lu,H.,
            Song,H., Yang,B., Ru,H., Lin,S. and Zhang,L.
  TITLE     AARS1 and AARS2 sense L-lactate to regulate cGAS as global lysine
            lactyltransferases
  JOURNAL   Nature 634 (8036), 1229-1237 (2024)
   PUBMED   39322678
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Zannini,L., Cardano,M., Liberi,G. and Buscemi,G.
  TITLE     R-loops and impaired autophagy trigger cGAS-dependent inflammation
            via micronuclei formation in Senataxin-deficient cells
  JOURNAL   Cell Mol Life Sci 81 (1), 339 (2024)
   PUBMED   39120648
  REMARK    GeneRIF: R-loops and impaired autophagy trigger cGAS-dependent
            inflammation via micronuclei formation in Senataxin-deficient
            cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Sun,L., Wu,J., Du,F., Chen,X. and Chen,Z.J.
  TITLE     Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates
            the type I interferon pathway
  JOURNAL   Science 339 (6121), 786-791 (2013)
   PUBMED   23258413
  REMARK    GeneRIF: These results indicate that cGAS is a cytosolic DNA sensor
            that induces interferons by producing the second messenger cGAMP.
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Wu,J., Sun,L., Chen,X., Du,F., Shi,H., Chen,C. and Chen,Z.J.
  TITLE     Cyclic GMP-AMP is an endogenous second messenger in innate immune
            signaling by cytosolic DNA
  JOURNAL   Science 339 (6121), 826-830 (2013)
   PUBMED   23258412
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Schoggins,J.W., Wilson,S.J., Panis,M., Murphy,M.Y., Jones,C.T.,
            Bieniasz,P. and Rice,C.M.
  TITLE     A diverse range of gene products are effectors of the type I
            interferon antiviral response
  JOURNAL   Nature 472 (7344), 481-485 (2011)
   PUBMED   21478870
  REMARK    Erratum:[Nature. 2015 Sep 3;525(7567):144. doi:
            10.1038/nature14554. PMID: 26153858]
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA375117.1, BC108714.1, AK097148.1 and AC019205.4.
            
            On Oct 4, 2006 this sequence version replaced NP_612450.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.43969.1,
                                           SRR1803612.161903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162946 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370315.4/ ENSP00000359339.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..522
                     /product="cyclic GMP-AMP synthase isoform 1"
                     /EC_number="2.7.7.86"
                     /note="protein MB21D1; mab-21 domain-containing protein 1;
                     Mab-21 domain containing 1; cGAMP synthase; 2'3'-cGAMP
                     synthase; DANGER family member 4"
                     /calculated_mol_wt=58684
     Region          1..160
                     /region_name="DNA-binding.
                     /evidence=ECO:0000269|PubMed:28363908"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          1..144
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:30799039,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:33542149; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          <15..>189
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32817552; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:33542149; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            47
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32817552; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            50
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:30799039,
                     ECO:0000269|PubMed:32817552; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            56
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32817552; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            62
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32817552; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            63
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32817552; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          64..75
                     /region_name="Required for association with the cell
                     membrane. /evidence=ECO:0000269|PubMed:30827685"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:33542149; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:33273464,
                     ECO:0000269|PubMed:33542149; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            82
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32817552; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            83
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32817552; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:32474700,
                     ECO:0000269|PubMed:33542149; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32474700; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:33542149; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          120..160
                     /region_name="Required for activation upon DNA viral
                     infection. /evidence=ECO:0000269|PubMed:28314590"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:33542149; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            140..141
                     /site_type="cleavage"
                     /note="Cleavage, by CASP1.
                     /evidence=ECO:0000269|PubMed:28314590; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:33542149,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            157..158
                     /site_type="cleavage"
                     /note="Cleavage, by CASP1.
                     /evidence=ECO:0000269|PubMed:28314590; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          169..174
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000269|PubMed:33406424"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          173..215
                     /region_name="DNA-binding.
                     /evidence=ECO:0000269|PubMed:30007416,
                     ECO:0000305|PubMed:23707061, ECO:0007744|PDB:6CTA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            187
                     /site_type="other"
                     /note="Important for preferential detection of curved long
                     DNA. /evidence=ECO:0000269|PubMed:30007416; propagated
                     from UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            195
                     /site_type="other"
                     /note="Important for preferential detection of curved long
                     DNA. /evidence=ECO:0000269|PubMed:30007416; propagated
                     from UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:33273464; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          214..389
                     /region_name="Mab-21"
                     /note="Mab-21 protein nucleotidyltransferase domain;
                     pfam03281"
                     /db_xref="CDD:460873"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by BLK.
                     /evidence=ECO:0000269|PubMed:30356214; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            255
                     /site_type="other"
                     /note="Arginine-anchor.
                     /evidence=ECO:0000269|PubMed:32911482,
                     ECO:0000269|PubMed:32912999, ECO:0000269|PubMed:33051594;
                     propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          295..305
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:30356214"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          299..302
                     /region_name="KRKR-loop.
                     /evidence=ECO:0000269|PubMed:31142647"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and PKB.
                     /evidence=ECO:0000269|PubMed:26440888,
                     ECO:0000269|PubMed:32351706, ECO:0000269|PubMed:33542149;
                     propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            319..320
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000269|PubMed:30878284; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          341..382
                     /region_name="Interaction with collided ribosomes.
                     /evidence=ECO:0000269|PubMed:34111399"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          384..407
                     /region_name="DNA-binding.
                     /evidence=ECO:0000305|PubMed:23707061"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            384
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:30799039; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            392
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:30799039; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            394
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:30799039; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          405..510
                     /region_name="Mab-21_C"
                     /note="Mab-21 protein HhH/H2TH-like domain; pfam20266"
                     /db_xref="CDD:466416"
     Site            414
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:30799039,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Region          427..429
                     /region_name="KKH-loop.
                     /evidence=ECO:0000269|PubMed:31142647"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32474700; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32474700; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     Site            506
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:35210392; propagated from
                     UniProtKB/Swiss-Prot (Q8N884.2)"
     CDS             1..522
                     /gene="CGAS"
                     /gene_synonym="C6orf150; D4; h-cGAS; MB21D1"
                     /coded_by="NM_138441.3:117..1685"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4978.1"
                     /db_xref="GeneID:115004"
                     /db_xref="HGNC:HGNC:21367"
                     /db_xref="MIM:613973"
ORIGIN      
        1 mqpwhgkamq raseagatap kasarnarga pmdptespaa peaalpkagk fgparksgsr
       61 qkksapdtqe rppvratgar akkapqraqd tqpsdatsap gaegleppaa repalsrags
      121 crqrgarcst kprpppgpwd vpspglpvsa pilvrrdaap gasklravle klklsrddis
      181 taagmvkgvv dhlllrlkcd safrgvglln tgsyyehvki sapnefdvmf klevpriqle
      241 eysntrayyf vkfkrnpken plsqflegei lsaskmlskf rkiikeeind ikdtdvimkr
      301 krggspavtl lisekisvdi tlaleskssw pastqeglri qnwlsakvrk qlrlkpfylv
      361 pkhakegngf qeetwrlsfs hiekeilnnh gksktccenk eekccrkdcl klmkylleql
      421 kerfkdkkhl dkfssyhvkt affhvctqnp qdsqwdrkdl glcfdncvty flqclrtekl
      481 enyfipefnl fssnlidkrs kefltkqiey ernnefpvfd ef
//
LOCUS       NP_149981                436 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 101 isoform 1 [Homo sapiens].
ACCESSION   NP_149981
VERSION     NP_149981.2
DBSOURCE    REFSEQ: accession NM_033204.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Cornelis,M.C., Fornage,M., Foy,M., Xun,P., Gladyshev,V.N.,
            Morris,S., Chasman,D.I., Hu,F.B., Rimm,E.B., Kraft,P., Jordan,J.M.,
            Mozaffarian,D. and He,K.
  TITLE     Genome-wide association study of selenium concentrations
  JOURNAL   Hum Mol Genet 24 (5), 1469-1477 (2015)
   PUBMED   25343990
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Demirkan,A., van Duijn,C.M., Ugocsai,P., Isaacs,A.,
            Pramstaller,P.P., Liebisch,G., Wilson,J.F., Johansson,A., Rudan,I.,
            Aulchenko,Y.S., Kirichenko,A.V., Janssens,A.C., Jansen,R.C.,
            Gnewuch,C., Domingues,F.S., Pattaro,C., Wild,S.H., Jonasson,I.,
            Polasek,O., Zorkoltseva,I.V., Hofman,A., Karssen,L.C.,
            Struchalin,M., Floyd,J., Igl,W., Biloglav,Z., Broer,L., Pfeufer,A.,
            Pichler,I., Campbell,S., Zaboli,G., Kolcic,I., Rivadeneira,F.,
            Huffman,J., Hastie,N.D., Uitterlinden,A., Franke,L., Franklin,C.S.,
            Vitart,V., Nelson,C.P., Preuss,M., Bis,J.C., O'Donnell,C.J.,
            Franceschini,N., Witteman,J.C., Axenovich,T., Oostra,B.A.,
            Meitinger,T., Hicks,A.A., Hayward,C., Wright,A.F., Gyllensten,U.,
            Campbell,H. and Schmitz,G.
  CONSRTM   DIAGRAM Consortium; CARDIoGRAM Consortium; CHARGE Consortium;
            EUROSPAN consortium
  TITLE     Genome-wide association study identifies novel loci associated with
            circulating phospho- and sphingolipid concentrations
  JOURNAL   PLoS Genet 8 (2), e1002490 (2012)
   PUBMED   22359512
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Waterworth,D.M., Ricketts,S.L., Song,K., Chen,L., Zhao,J.H.,
            Ripatti,S., Aulchenko,Y.S., Zhang,W., Yuan,X., Lim,N., Luan,J.,
            Ashford,S., Wheeler,E., Young,E.H., Hadley,D., Thompson,J.R.,
            Braund,P.S., Johnson,T., Struchalin,M., Surakka,I., Luben,R.,
            Khaw,K.T., Rodwell,S.A., Loos,R.J., Boekholdt,S.M., Inouye,M.,
            Deloukas,P., Elliott,P., Schlessinger,D., Sanna,S., Scuteri,A.,
            Jackson,A., Mohlke,K.L., Tuomilehto,J., Roberts,R., Stewart,A.,
            Kesaniemi,Y.A., Mahley,R.W., Grundy,S.M., McArdle,W., Cardon,L.,
            Waeber,G., Vollenweider,P., Chambers,J.C., Boehnke,M.,
            Abecasis,G.R., Salomaa,V., Jarvelin,M.R., Ruokonen,A., Barroso,I.,
            Epstein,S.E., Hakonarson,H.H., Rader,D.J., Reilly,M.P.,
            Witteman,J.C., Hall,A.S., Samani,N.J., Strachan,D.P., Barter,P.,
            van Duijn,C.M., Kooner,J.S., Peltonen,L., Wareham,N.J.,
            McPherson,R., Mooser,V. and Sandhu,M.S.
  CONSRTM   Wellcome Trust Case Control Consortium
  TITLE     Genetic variants influencing circulating lipid levels and risk of
            coronary artery disease
  JOURNAL   Arterioscler Thromb Vasc Biol 30 (11), 2264-2276 (2010)
   PUBMED   20864672
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Aulchenko,Y.S., Ripatti,S., Lindqvist,I., Boomsma,D., Heid,I.M.,
            Pramstaller,P.P., Penninx,B.W., Janssens,A.C., Wilson,J.F.,
            Spector,T., Martin,N.G., Pedersen,N.L., Kyvik,K.O., Kaprio,J.,
            Hofman,A., Freimer,N.B., Jarvelin,M.R., Gyllensten,U., Campbell,H.,
            Rudan,I., Johansson,A., Marroni,F., Hayward,C., Vitart,V.,
            Jonasson,I., Pattaro,C., Wright,A., Hastie,N., Pichler,I.,
            Hicks,A.A., Falchi,M., Willemsen,G., Hottenga,J.J., de Geus,E.J.,
            Montgomery,G.W., Whitfield,J., Magnusson,P., Saharinen,J.,
            Perola,M., Silander,K., Isaacs,A., Sijbrands,E.J.,
            Uitterlinden,A.G., Witteman,J.C., Oostra,B.A., Elliott,P.,
            Ruokonen,A., Sabatti,C., Gieger,C., Meitinger,T., Kronenberg,F.,
            Doring,A., Wichmann,H.E., Smit,J.H., McCarthy,M.I., van Duijn,C.M.
            and Peltonen,L.
  CONSRTM   ENGAGE Consortium
  TITLE     Loci influencing lipid levels and coronary heart disease risk in 16
            European population cohorts
  JOURNAL   Nat Genet 41 (1), 47-55 (2009)
   PUBMED   19060911
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Looman,C., Hellman,L. and Abrink,M.
  TITLE     A novel Kruppel-Associated Box identified in a panel of mammalian
            zinc finger proteins
  JOURNAL   Mamm Genome 15 (1), 35-40 (2004)
   PUBMED   14727140
REFERENCE   7  (residues 1 to 436)
  AUTHORS   Bellefroid,E.J., Marine,J.C., Ried,T., Lecocq,P.J., Riviere,M.,
            Amemiya,C., Poncelet,D.A., Coulie,P.G., de Jong,P., Szpirer,C. et
            al.
  TITLE     Clustered organization of homologous KRAB zinc-finger genes with
            enhanced expression in human T lymphoid cells
  JOURNAL   EMBO J 12 (4), 1363-1374 (1993)
   PUBMED   8467795
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CR999939.1, AY149174.1, AC011458.7 and BM972114.1.
            
            On Nov 2, 2002 this sequence version replaced NP_149981.1.
            
            Summary: Zinc finger proteins (ZNFs), such as ZNF101, bind nucleic
            acids and perform many key functions, the most important of which
            is regulating transcription (summary by Bellefroid et al., 1993
            [PubMed 8467795]). See ZNF91 (MIM 603971) for general information
            on ZNFs.[supplied by OMIM, Nov 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB138422.1, SRR1803614.63819.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000592502.2/ ENSP00000468049.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..436
                     /product="zinc finger protein 101 isoform 1"
                     /note="zinc finger protein 101 (Y2); zinc finger protein
                     12; zinc finger protein HZF12"
                     /calculated_mol_wt=50209
     Region          3..44
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          104..124
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          128..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC7.1)"
     Region          149..>209
                     /region_name="lambda-1"
                     /note="inner capsid protein lambda-1 or VP3; cd11674"
                     /db_xref="CDD:212564"
     Region          171..191
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(171,174,187,191)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:212564"
     Region          199..219
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          227..247
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <237..410
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          255..276
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          284..304
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          312..332
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          340..360
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(345,347,349,351..352,355..356,359,373,375,379..380,
                     383..384,387,401,403,405,407..408,411..412,415)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          368..388
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          396..416
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..436
                     /gene="ZNF101"
                     /gene_synonym="HZF12"
                     /coded_by="NM_033204.4:126..1436"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32971.1"
                     /db_xref="GeneID:94039"
                     /db_xref="HGNC:HGNC:12881"
                     /db_xref="MIM:603983"
ORIGIN      
        1 mdsvafedva vnftqeewal lspsqknlyr dvtletfrnl asvgiqwkdq dienlyqnlg
       61 iklrslverl cgrkegnehr etfsqipdch lnkksqtgvk pckcsvcgkv flrhsfldrh
      121 mrahaghkrs ecggewretp rkqkqhgkas ispssgarrt vtptrkrpye ckvcgkafns
      181 pnlfqihqrt htgkrsykcr eivraftvss ffrkhgkmht gekryeckyc gkpidypslf
      241 qihvrthtge kpykckqcgk afisagylrt heirshalek shqcqecgkk lscssslhrh
      301 erthsggkly ecqkcakvfr cptslqaher ahtgerpyec nkcgktfnyp scfrrhkkth
      361 sgekpyectr cgkafgwcss lrrhemthtg ekpfdckqcg kvftfsnylr lherthlagr
      421 sqcfgrrqgd hlspgv
//
LOCUS       NP_060480                429 aa            linear   PRI 27-APR-2025
DEFINITION  intraflagellar transport protein 57 homolog [Homo sapiens].
ACCESSION   NP_060480
VERSION     NP_060480.1
DBSOURCE    REFSEQ: accession NM_018010.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Dong,K., Nihal,R., Meyer,T.J., Singh,S.P., Kaur,S. and Roberts,D.D.
  TITLE     CD47 and IFT57 Are Colinear Genes That Are Highly Coexpressed in
            Most Cancers and Exhibit Parallel Cancer-Specific Correlations with
            Survival
  JOURNAL   Int J Mol Sci 25 (16), 8956 (2024)
   PUBMED   39201643
  REMARK    GeneRIF: CD47 and IFT57 Are Colinear Genes That Are Highly
            Coexpressed in Most Cancers and Exhibit Parallel Cancer-Specific
            Correlations with Survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Sorusch,N., Yildirim,A., Knapp,B., Janson,J., Fleck,W., Scharf,C.
            and Wolfrum,U.
  TITLE     SANS (USH1G) Molecularly Links the Human Usher Syndrome Protein
            Network to the Intraflagellar Transport Module by Direct Binding to
            IFT-B Proteins
  JOURNAL   Front Cell Dev Biol 7, 216 (2019)
   PUBMED   31637240
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Baker,S.A., Freeman,K., Luby-Phelps,K., Pazour,G.J. and
            Besharse,J.C.
  TITLE     IFT20 links kinesin II with a mammalian intraflagellar transport
            complex that is conserved in motile flagella and sensory cilia
  JOURNAL   J Biol Chem 278 (36), 34211-34218 (2003)
   PUBMED   12821668
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Cheng,C.M., Huang,S.P., Chang,Y.F., Chung,W.Y. and Yuo,C.Y.
  TITLE     The viral death protein Apoptin interacts with Hippi, the protein
            interactor of Huntingtin-interacting protein 1
  JOURNAL   Biochem Biophys Res Commun 305 (2), 359-364 (2003)
   PUBMED   12745083
  REMARK    GeneRIF: Hippi interacts with the viral death protein Apoptin.
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Gervais,F.G., Singaraja,R., Xanthoudakis,S., Gutekunst,C.A.,
            Leavitt,B.R., Metzler,M., Hackam,A.S., Tam,J., Vaillancourt,J.P.,
            Houtzager,V., Rasper,D.M., Roy,S., Hayden,M.R. and Nicholson,D.W.
  TITLE     Recruitment and activation of caspase-8 by the
            Huntingtin-interacting protein Hip-1 and a novel partner Hippi
  JOURNAL   Nat Cell Biol 4 (2), 95-105 (2002)
   PUBMED   11788820
  REMARK    GeneRIF: Results show that pro-apoptotic Hippi-Hip-1 heterodimers
            can recruit procaspase-8 into a complex of Hippi, Hip-1 and
            procaspase-8, and launch apoptosis through components of the
            'extrinsic' cell-death pathway.
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Mattson,M.P.
  TITLE     Accomplices to neuronal death
  JOURNAL   Nature 415 (6870), 377-379 (2002)
   PUBMED   11807533
  REMARK    GeneRIF: critical for the death-promoting effects of mutant
            huntingtin protein in cultured cells
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Kalchman,M.A., Koide,H.B., McCutcheon,K., Graham,R.K., Nichol,K.,
            Nishiyama,K., Kazemi-Esfarjani,P., Lynn,F.C., Wellington,C.,
            Metzler,M., Goldberg,Y.P., Kanazawa,I., Gietz,R.D. and Hayden,M.R.
  TITLE     HIP1, a human homologue of S. cerevisiae Sla2p, interacts with
            membrane-associated huntingtin in the brain
  JOURNAL   Nat Genet 16 (1), 44-53 (1997)
   PUBMED   9140394
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA362330.1, BC011899.2, AC012020.17 and AF139576.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF139576.1, SRR1660803.177068.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2159764
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264538.4/ ENSP00000264538.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.12-q13.13"
     Protein         1..429
                     /product="intraflagellar transport protein 57 homolog"
                     /note="HIP1 protein interactor; estrogen-related receptor
                     beta like 1; huntingtin interacting protein-1 interacting
                     protein; HIP1-interacting protein; dermal papilla-derived
                     protein 8; estrogen-related receptor beta-like protein 1;
                     intraflagellar transport 57 homolog"
                     /calculated_mol_wt=48977
     Region          44..401
                     /region_name="IFT57"
                     /note="Intra-flagellar transport protein 57; pfam10498"
                     /db_xref="CDD:463118"
     Region          335..426
                     /region_name="pDED"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWB7.1)"
     CDS             1..429
                     /gene="IFT57"
                     /gene_synonym="ESRRBL1; HIPPI; MHS4R2; OFD18"
                     /coded_by="NM_018010.4:103..1392"
                     /db_xref="CCDS:CCDS2951.1"
                     /db_xref="GeneID:55081"
                     /db_xref="HGNC:HGNC:17367"
                     /db_xref="MIM:606621"
ORIGIN      
        1 mtaalavvtt sgledgvprs rgegtgevvl ergpgaayhm fvvmedlvek lkllryeeef
       61 lrksnlkaps rhyfalptnp geqfymfctl aawlinkagr pfeqpqeydd pnatisnils
      121 elrsfgrtad fppsklksgy gehvcyvldc faeealkyig ftwkrpiypv eeleeesvae
      181 ddaeltlnkv deefveeetd neenfidlnv lkaqtyhldm netakqedil esttdaaews
      241 levervlpql kvtirtdnkd wrihvdqmhq hrsgiesalk etkgfldklh neitrtleki
      301 ssrekyinnq lenlvqeyra aqaqlseake ryqqgnggvt ertrllsevm eelekvkqem
      361 eekgssmtdg aplvkikqsl tklkqetvem dirigiveht llqsklkeks nmtrnmhatv
      421 ipepatgfy
//
LOCUS       NP_001074689            2293 aa            linear   ROD 27-APR-2025
DEFINITION  G-protein coupled receptor 179 precursor [Mus musculus].
ACCESSION   NP_001074689 XP_006533087 XP_484070
VERSION     NP_001074689.1
DBSOURCE    REFSEQ: accession NM_001081220.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 2293)
  AUTHORS   Wilmet,B., Callebert,J., Duvoisin,R., Goulet,R., Tourain,C.,
            Michiels,C., Frederiksen,H., Schaeffel,F., Marre,O., Sahel,J.A.,
            Audo,I., Picaud,S. and Zeitz,C.
  TITLE     Mice Lacking Gpr179 with Complete Congenital Stationary Night
            Blindness Are a Good Model for Myopia
  JOURNAL   Int J Mol Sci 24 (1), 219 (2022)
   PUBMED   36613663
  REMARK    GeneRIF: Mice Lacking Gpr179 with Complete Congenital Stationary
            Night Blindness Are a Good Model for Myopia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2293)
  AUTHORS   Cao,Y., Fajardo,D., Guerrero-Given,D., Samuel,M.A., Ohtsuka,T.,
            Boye,S.E., Kamasawa,N. and Martemyanov,K.A.
  TITLE     Post-developmental plasticity of the primary rod pathway allows
            restoration of visually guided behaviors
  JOURNAL   Curr Biol 32 (22), 4783-4796 (2022)
   PUBMED   36179691
REFERENCE   3  (residues 1 to 2293)
  AUTHORS   Gong,Y., Laheji,F., Berenson,A., Qian,A., Park,S.O., Kok,R.,
            Selig,M., Hahn,R., Sadjadi,R., Kemp,S. and Eichler,F.
  TITLE     Peroxisome Metabolism Contributes to PIEZO2-Mediated Mechanical
            Allodynia
  JOURNAL   Cells 11 (11), 1842 (2022)
   PUBMED   35681537
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2293)
  AUTHORS   Bachert,W., Klotz,L., Sticht,H. and Enz,R.
  TITLE     Homodimerization of a proximal region within the C-terminus of the
            orphan G-protein coupled receptor GPR179
  JOURNAL   Neurochem Int 149, 105150 (2021)
   PUBMED   34333057
  REMARK    GeneRIF: Homodimerization of a proximal region within the
            C-terminus of the orphan G-protein coupled receptor GPR179.
REFERENCE   5  (residues 1 to 2293)
  AUTHORS   Orhan,E., Neuille,M., de Sousa Dias,M., Pugliese,T., Michiels,C.,
            Condroyer,C., Antonio,A., Sahel,J.A., Audo,I. and Zeitz,C.
  TITLE     A New Mouse Model for Complete Congenital Stationary Night
            Blindness Due to Gpr179 Deficiency
  JOURNAL   Int J Mol Sci 22 (9), 4424 (2021)
   PUBMED   33922602
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2293)
  AUTHORS   Peachey,N.S. and Sturgill-Short,G.M.
  TITLE     Response properties of slow PIII in the Large (vls) mutant
  JOURNAL   Doc Ophthalmol 125 (3), 203-209 (2012)
   PUBMED   22865473
REFERENCE   7  (residues 1 to 2293)
  AUTHORS   Peachey,N.S., Pearring,J.N., Bojang,P. Jr., Hirschtritt,M.E.,
            Sturgill-Short,G., Ray,T.A., Furukawa,T., Koike,C., Goldberg,A.F.,
            Shen,Y., McCall,M.A., Nawy,S., Nishina,P.M. and Gregg,R.G.
  TITLE     Depolarizing bipolar cell dysfunction due to a Trpm1 point mutation
  JOURNAL   J Neurophysiol 108 (9), 2442-2451 (2012)
   PUBMED   22896717
REFERENCE   8  (residues 1 to 2293)
  AUTHORS   Orlandi,C., Posokhova,E., Masuho,I., Ray,T.A., Hasan,N., Gregg,R.G.
            and Martemyanov,K.A.
  TITLE     GPR158/179 regulate G protein signaling by controlling localization
            and activity of the RGS7 complexes
  JOURNAL   J Cell Biol 197 (6), 711-719 (2012)
   PUBMED   22689652
  REMARK    GeneRIF: The loss of GPR179 in a mouse model of night blindness
            prevented targeting of RGS to the postsynaptic compartment of
            bipolar neurons in the retina, illuminating the role of GPR179 in
            night vision.
REFERENCE   9  (residues 1 to 2293)
  AUTHORS   Peachey,N.S., Ray,T.A., Florijn,R., Rowe,L.B., Sjoerdsma,T.,
            Contreras-Alcantara,S., Baba,K., Tosini,G., Pozdeyev,N.,
            Iuvone,P.M., Bojang,P. Jr., Pearring,J.N., Simonsz,H.J., van
            Genderen,M., Birch,D.G., Traboulsi,E.I., Dorfman,A., Lopez,I.,
            Ren,H., Goldberg,A.F., Nishina,P.M., Lachapelle,P., McCall,M.A.,
            Koenekoop,R.K., Bergen,A.A., Kamermans,M. and Gregg,R.G.
  TITLE     GPR179 is required for depolarizing bipolar cell function and is
            mutated in autosomal-recessive complete congenital stationary night
            blindness
  JOURNAL   Am J Hum Genet 90 (2), 331-339 (2012)
   PUBMED   22325362
REFERENCE   10 (residues 1 to 2293)
  AUTHORS   Bjarnadottir,T.K., Fredriksson,R. and Schioth,H.B.
  TITLE     The gene repertoire and the common evolutionary history of
            glutamate, pheromone (V2R), taste(1) and other related G
            protein-coupled receptors
  JOURNAL   Gene 362, 70-84 (2005)
   PUBMED   16229975
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL596088.14.
            
            On or before Jul 6, 2018 this sequence version replaced
            XP_006533087.1, XP_484070.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN02415123
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2293
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 60.95 cM"
     Protein         1..2293
                     /product="G-protein coupled receptor 179 precursor"
                     /note="GPR158-like 1 receptor; probable G-protein coupled
                     receptor 179"
                     /calculated_mol_wt=246048
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2686
     mat_peptide     28..2293
                     /product="G-protein coupled receptor 179.
                     /evidence=ECO:0000255. /id=PRO_5003245698"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
                     /calculated_mol_wt=246048
     Region          62..245
                     /region_name="Cache-like region.
                     /evidence=ECO:0000250|UniProtKB:Q5T848"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          278..327
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(278,281,304)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          379..632
                     /region_name="7tmC_GPR158-like"
                     /note="orphan GPR158 and similar proteins, member of the
                     class C family of seven-transmembrane G protein-coupled
                     receptors; cd15293"
                     /db_xref="CDD:320420"
     Region          379..404
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320420"
     Site            order(382,385..386,389..390,392..393,427,431,434..435,443,
                     447)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320420"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          416..437
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320420"
     Site            416..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Site            order(436,448..449,452..453,456,538,543,546..547,550,584,
                     587..588,591,595,607..608,611,614,618)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320420"
     Site            445..465
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          446..470
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320420"
     Region          490..510
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320420"
     Site            494..514
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          539..565
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320420"
     Site            544..564
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          573..596
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320420"
     Site            585..602
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          605..630
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320420"
     Site            608..628
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Site            661
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          733..812
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Site            823
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          872..935
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          1046..1235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          1275..1294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          1326..1345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          1388..1411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          1479..1560
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          1578..1770
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          1792..1828
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          1844..1882
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          1924..2051
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     Region          2212..2293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PY61.1)"
     CDS             1..2293
                     /gene="Gpr179"
                     /gene_synonym="5330439C02Rik; Gpr158l1"
                     /coded_by="NM_001081220.2:78..6959"
                     /db_xref="CCDS:CCDS36292.1"
                     /db_xref="GeneID:217143"
                     /db_xref="MGI:MGI:2443409"
ORIGIN      
        1 mgaravviss lawgllsccf lcsgalgsqr plrslpplps qakprsepmw mppkgaeaal
       61 aflysgdvqr lsgancseky evrgaegkag vppvlqraag tlaqaanfln mllqandire
      121 ssveedvewy qalvrsvaeg dpkayrallt fnpapgashl qlalqatrmg detvlqdlsg
      181 nkvqeetpge dldrpvlqkr vltndlrsld spkwprgdgy vgdiqqvkls ppflechegq
      241 lrpgwlvtvs atfyglkpdl tpevrgqvqm didlqsvdin qcasgpgwys nthlcdlnst
      301 qcvplesqgf vlgrylcrcr pgfygasgsg gleesatqaa gqfgspqdsl gkllrcqpcp
      361 egctscldat pclveealal rtavlacqac cmlavflsml vayrcrgskr irasgivlle
      421 tilfgsllly fpvfilyfkp svfrcvalrw vrllgfavvy gtiilklyrv lqlflsrtaq
      481 rvphpssgql lrrlgqllll vlgflvvwta galepgtqht alvtrghtpt grhfylchhd
      541 hwdyimvvae mlllcwgsfl cyatravpsa fheprymsia lhnelllsta fhtarfvlvp
      601 slhpdwtlll fflhthstvt atlalifipk fwkpgappre eildevyede ldlqrsgsyl
      661 nssiasawse rslepgdird elkklyaqle irktkemaan nphlpkkrgs shqglgrsfm
      721 rylaefpeal arqhsrdsgs lglgslpgss rrrllssslq etekppalrk trstydhhre
      781 hntlpfdstl rrtlskkasp tdgresladg ppalgfrsas ahnltvgerl prarpislqk
      841 slsvaagsre kallvasqay leetyrqake reerkkaeaa mvspvrrpst rrlewplrap
      901 lsappspgks ssmdssqtta rpheeagrrl phppirhqvs tpvlalsgic lgeprmlspt
      961 pastlapill papapapapv lapvskppqs ptlltficpw enaelpgkke nvvqedpagp
     1021 ersghspasa rtkiwralsv avekrgtges ealtegghvq geaddtdeek pkvfskshsl
     1081 ktplqqgsvr slglaikalt rsrstykekd ggegtpetek gkptevstga plrsprlgrp
     1141 kavskqvala pcedeeslqn qqnahtsrml hvcqkegsre qedrnkrvap gpgerkvert
     1201 gkitmttlrq vfgeknaeqa kespagyqev pnpalqslgs adhrvaevcp wevtepesgm
     1261 dppesvnkak vyswertegg slekkpsrqv lsrsweerek vlaesetegv gaiprkkper
     1321 lvrsqeavcp wespdsggls pqlvhqesdr tggrfvvvsk gdahpealps haakaelclw
     1381 emsdvgegts tqrvqelpee rqkspkkatf wgernlggdl vslcpwestd frgpsavslq
     1441 apgssgslgs giaevcpwea eniandkkae vcpwelgeel agsdglnpga dgkslpgket
     1501 psrkgclaes geqtvrakpt vpqgqesvcp wedeaperss pqpdkasska gekllshggs
     1561 qvlqvcpwea vkpeekqatl staeicpwev dgqpetrtse hpskgevhkd eekmpgrari
     1621 kaqeeaegri qkqeaicpwe smapgstpqr dtekaqaslq rqgsvagraa eicpwevgte
     1681 vgeertigae asearpndag hastdsgsrq vaasapkkse rlgsekevvc pwdslspgds
     1741 sqqpdtpnte klkdelqehg ssrpievcpw eaeevptgek akicpwelne gtvgkglere
     1801 pgceperqrr qnleeaglpf qeegtskgdt klcreqegea icpwkppaqv pkvsdlplst
     1861 vgqgvegqsl easdrasekg elrqdlkmgs lpeyitqvvp vdgggassel qpislqegmv
     1921 lagssshphi qcpdqprvss qplvstgdgt aevcpwdapd sdsdtkvepc aqkvtgrvte
     1981 temsrqdeke ksqeekerap etrdhegvav qkmpqtsnfg kqeavcpres qdfgvqaatd
     2041 asdgskggse kvcpweveev psikeaeicp weaspgavge galdlgqdge sqgegraerh
     2101 llkaaetvcp legtmssglf tqedvvdtdl pkvglhgass pgkglaelcv wevtdpegnk
     2161 ikgtmadicp weetraqsde sgplalpvtq agvpaapeks vclsvhgple sflpesksvr
     2221 pdiskppgss rpegvreqep leletgaksv pkpsptetea pesftltddq glmasegeag
     2281 elspppdypw dce
//
LOCUS       NP_003153                780 aa            linear   PRI 27-APR-2025
DEFINITION  striatin [Homo sapiens].
ACCESSION   NP_003153
VERSION     NP_003153.2
DBSOURCE    REFSEQ: accession NM_003162.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Gholami,S.K., Heydarpour,M., Williams,J.S., Pojoga,L.H.,
            Adler,G.K., Williams,G.H. and Romero,J.R.
  TITLE     Striatin Gene Variants Are Associated With Salt Sensitivity of
            Blood Pressure by Mechanisms That Differ in Women and Men
  JOURNAL   Hypertension 81 (2), 330-339 (2024)
   PUBMED   38018471
  REMARK    GeneRIF: Striatin Gene Variants Are Associated With Salt
            Sensitivity of Blood Pressure by Mechanisms That Differ in Women
            and Men.
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Viveka,M., Chaturvedula,L., Ram,A.K. and Vairappan,B.
  TITLE     Placental expression of striatin & endothelial nitric oxide
            synthase in women with & without pre-eclampsia
  JOURNAL   Indian J Med Res 157 (4), 345-352 (2023)
   PUBMED   37147942
  REMARK    GeneRIF: Placental expression of striatin & endothelial nitric
            oxide synthase in women with & without pre-eclampsia.
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Liu,L., Weber,A., Linne,U., Shehata,M., Pleschka,S., Kracht,M. and
            Schmitz,M.L.
  TITLE     Phosphorylation of Influenza A Virus Matrix Protein 1 at Threonine
            108 Controls Its Multimerization State and Functional Association
            with the STRIPAK Complex
  JOURNAL   mBio 14 (1), e0323122 (2023)
   PUBMED   36602306
  REMARK    GeneRIF: Phosphorylation of Influenza A Virus Matrix Protein 1 at
            Threonine 108 Controls Its Multimerization State and Functional
            Association with the STRIPAK Complex.
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Hu,Z., Sankar,D.S., Vu,B., Leytens,A., Vionnet,C., Wu,W.,
            Stumpe,M., Martinez-Martinez,E., Stork,B. and Dengjel,J.
  TITLE     ULK1 phosphorylation of striatin activates protein phosphatase 2A
            and autophagy
  JOURNAL   Cell Rep 36 (13), 109762 (2021)
   PUBMED   34592149
  REMARK    GeneRIF: ULK1 phosphorylation of striatin activates protein
            phosphatase 2A and autophagy.
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Gaillard,S., Bartoli,M., Castets,F. and Monneron,A.
  TITLE     Striatin, a calmodulin-dependent scaffolding protein, directly
            binds caveolin-1
  JOURNAL   FEBS Lett 508 (1), 49-52 (2001)
   PUBMED   11707266
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Castets,F., Rakitina,T., Gaillard,S., Moqrich,A., Mattei,M.G. and
            Monneron,A.
  TITLE     Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat
            proteins principally expressed in the brain
  JOURNAL   J Biol Chem 275 (26), 19970-19977 (2000)
   PUBMED   10748158
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Moreno,C.S., Park,S., Nelson,K., Ashby,D., Hubalek,F., Lane,W.S.
            and Pallas,D.C.
  TITLE     WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are
            members of a novel family of calmodulin-binding proteins that
            associate with protein phosphatase 2A
  JOURNAL   J Biol Chem 275 (8), 5257-5263 (2000)
   PUBMED   10681496
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Moqrich,A., Mattei,M.G., Bartoli,M., Rakitina,T., Baillat,G.,
            Monneron,A. and Castets,F.
  TITLE     Cloning of human striatin cDNA (STRN), gene mapping to 2p22-p21,
            and preferential expression in brain
  JOURNAL   Genomics 51 (1), 136-139 (1998)
   PUBMED   9693043
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Castets,F., Bartoli,M., Barnier,J.V., Baillat,G., Salin,P.,
            Moqrich,A., Bourgeois,J.P., Denizot,F., Rougon,G., Calothy,G. and
            Monneron,A.
  TITLE     A novel calmodulin-binding protein, belonging to the WD-repeat
            family, is localized in dendrites of a subset of CNS neurons
  JOURNAL   J Cell Biol 134 (4), 1051-1062 (1996)
   PUBMED   8769426
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007404.4, AJ223814.1, AK026934.1 and AC007382.3.
            
            On Aug 16, 2004 this sequence version replaced NP_003153.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.9708.1,
                                           SRR1803617.227778.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263918.9/ ENSP00000263918.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.2"
     Protein         1..780
                     /product="striatin"
                     /note="striatin, calmodulin binding protein; protein
                     phosphatase 2 regulatory subunit B'''alpha"
                     /calculated_mol_wt=86001
     Region          49..173
                     /region_name="Striatin"
                     /note="Striatin family; pfam08232"
                     /db_xref="CDD:462401"
     Region          55..63
                     /region_name="Caveolin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          124..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55106; propagated from
                     UniProtKB/Swiss-Prot (O43815.4)"
     Region          149..166
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O55106; propagated from
                     UniProtKB/Swiss-Prot (O43815.4)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43815.4)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43815.4)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43815.4)"
     Region          289..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          365..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          455..779
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          461..500
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Site            order(462,480,484,490..491,514..515,533,537,543..544,
                     567..568,585,590,596..597,616,633,642..643,655..656,681,
                     685,691..692,704..705,722,727,733..734,746..747,769,773,
                     779)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          468..514
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          514..553
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          520..567
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          567..606
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          572..608
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          616..654
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          662..701
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          667..703
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          704..743
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          709..745
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          750..780
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          755..779
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..780
                     /gene="STRN"
                     /gene_synonym="PPP2R6A; SG2NA; STRN1"
                     /coded_by="NM_003162.4:74..2416"
                     /db_xref="CCDS:CCDS1784.1"
                     /db_xref="GeneID:6801"
                     /db_xref="HGNC:HGNC:11424"
                     /db_xref="MIM:614765"
ORIGIN      
        1 mdeqagpgvf fsnnhpgagg akglgplaea aaagdgaaaa gaaraqyslp gilhflqhew
       61 arfeveraqw everaelqaq iaflqgerkg qenlkkdlvr rikmleyalk qerakyhklk
      121 ygtelnqgdm kppsydsdeg netevqpqqn sqlmwkqgrq llrqylqevg ytdtildvks
      181 krvrallgfs sdvtdreddk nqdsvvngte aevketamia kseltdsasv ldnfkflesa
      241 aadfsdeded ddvdgreksv idtstivrkk alpdsgedrd tkealkefdf lvtseegdne
      301 srsagdgtdw ekedqclmpe awnvdqgvit klkeqykker kgkkgvkrpn rsklqdmlan
      361 lrdvdelpsl qpsvgspsrp sssrlpehei nradevealt fppssgksfi mgadealese
      421 lglgelaglt vaneadslty diannkdalr ktwnpkftlr shfdgirala fhpiepvlit
      481 asedhtlkmw nlqktapakk stsldvepiy tfrahkgpvl cvvmssngeq cysggtdgli
      541 qgwnttnpni dpydsydpsv lrgpllghtd avwglaysaa hqrllscsad gtlrlwntte
      601 vapalsvfnd tkelgipasv dlvssdpshm vasfskgyts ifnmetqqri ltlesnvdtt
      661 ansscqinrv ishptlpisi tahedrhikf ydnntgklih smvahleavt slavdpngly
      721 lmsgshdcsi rlwnlesktc iqeftahrkk feesihdvaf hpskcyiasa gadalakvfv
//
LOCUS       NP_001136028             725 aa            linear   PRI 27-APR-2025
DEFINITION  hyaluronan mediated motility receptor isoform a [Homo sapiens].
ACCESSION   NP_001136028
VERSION     NP_001136028.1
DBSOURCE    REFSEQ: accession NM_001142556.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Su,Z., He,Y., You,L., Zhang,G., Chen,J. and Liu,Z.
  TITLE     Coupled scRNA-seq and Bulk-seq reveal the role of HMMR in
            hepatocellular carcinoma
  JOURNAL   Front Immunol 15, 1363834 (2024)
   PUBMED   38633247
  REMARK    GeneRIF: Coupled scRNA-seq and Bulk-seq reveal the role of HMMR in
            hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Hinneh,J.A., Gillis,J.L., Mah,C.Y., Irani,S., Shrestha,R.K.,
            Ryan,N.K., Atsushi,E., Nassar,Z.D., Lynn,D.J., Selth,L.A., Kato,M.,
            Centenera,M.M. and Butler,L.M.
  TITLE     Targeting hyaluronan-mediated motility receptor (HMMR) enhances
            response to androgen receptor signalling inhibitors in prostate
            cancer
  JOURNAL   Br J Cancer 129 (8), 1350-1361 (2023)
   PUBMED   37673961
  REMARK    GeneRIF: Targeting hyaluronan-mediated motility receptor (HMMR)
            enhances response to androgen receptor signalling inhibitors in
            prostate cancer.
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Tarullo,S.E., He,Y., Daughters,C., Knutson,T.P., Henzler,C.M.,
            Price,M.A., Shanley,R., Witschen,P., Tolg,C., Kaspar,R.E.,
            Hallstrom,C., Gittsovich,L., Sulciner,M.L., Zhang,X., Forster,C.L.,
            Lange,C.A., Shats,O., Desler,M., Cowan,K.H., Yee,D.,
            Schwertfeger,K.L., Turley,E.A., McCarthy,J.B. and Nelson,A.C.
  TITLE     Receptor for hyaluronan-mediated motility (RHAMM) defines an
            invasive niche associated with tumor progression and predicts poor
            outcomes in breast cancer patients
  JOURNAL   J Pathol 260 (3), 289-303 (2023)
   PUBMED   37186300
  REMARK    GeneRIF: Receptor for hyaluronan-mediated motility (RHAMM) defines
            an invasive niche associated with tumor progression and predicts
            poor outcomes in breast cancer patients.
REFERENCE   4  (residues 1 to 725)
  AUTHORS   Nakano,M., Taguchi,R., Kikushige,Y., Isobe,T., Miyawaki,K.,
            Mizuno,S., Tsuruta,N., Hanamura,F., Yamaguchi,K., Yamauchi,T.,
            Ariyama,H., Kusaba,H., Nakamura,M., Maeda,T., Kuo,C.J., Baba,E. and
            Akashi,K.
  TITLE     RHAMM marks proliferative subpopulation of human colorectal cancer
            stem cells
  JOURNAL   Cancer Sci 114 (7), 2895-2906 (2023)
   PUBMED   36945114
  REMARK    GeneRIF: RHAMM marks proliferative subpopulation of human
            colorectal cancer stem cells.
REFERENCE   5  (residues 1 to 725)
  AUTHORS   Wang,Q., Wu,G., Fu,L., Li,Z., Wu,Y., Zhu,T. and Yu,G.
  TITLE     Tumor-promoting roles of HMMR in lung adenocarcinoma
  JOURNAL   Mutat Res 826, 111811 (2023)
   PUBMED   36603370
  REMARK    GeneRIF: Tumor-promoting roles of HMMR in lung adenocarcinoma.
REFERENCE   6  (residues 1 to 725)
  AUTHORS   Wang,C., Entwistle,J., Hou,G., Li,Q. and Turley,E.A.
  TITLE     The characterization of a human RHAMM cDNA: conservation of the
            hyaluronan-binding domains
  JOURNAL   Gene 174 (2), 299-306 (1996)
   PUBMED   8890751
REFERENCE   7  (residues 1 to 725)
  AUTHORS   Spicer,A.P., Roller,M.L., Camper,S.A., McPherson,J.D.,
            Wasmuth,J.J., Hakim,S., Wang,C., Turley,E.A. and McDonald,J.A.
  TITLE     The human and mouse receptors for hyaluronan-mediated motility,
            RHAMM, genes (HMMR) map to human chromosome 5q33.2-qter and mouse
            chromosome 11
  JOURNAL   Genomics 30 (1), 115-117 (1995)
   PUBMED   8595891
REFERENCE   8  (residues 1 to 725)
  AUTHORS   Hall,C.L., Yang,B., Yang,X., Zhang,S., Turley,M., Samuel,S.,
            Lange,L.A., Wang,C., Curpen,G.D., Savani,R.C., Greenberg,A.H. and
            Turley,E.A.
  TITLE     Overexpression of the hyaluronan receptor RHAMM is transforming and
            is also required for H-ras transformation
  JOURNAL   Cell 82 (1), 19-26 (1995)
   PUBMED   7541721
REFERENCE   9  (residues 1 to 725)
  AUTHORS   Pilarski,L.M., Miszta,H. and Turley,E.A.
  TITLE     Regulated expression of a receptor for hyaluronan-mediated motility
            on human thymocytes and T cells
  JOURNAL   J Immunol 150 (10), 4292-4302 (1993)
   PUBMED   7683315
REFERENCE   10 (residues 1 to 725)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB091289.1, AY623426.1 and
            AW629232.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is involved in cell
            motility. It is expressed in breast tissue and together with other
            proteins, it forms a complex with BRCA1 and BRCA2, thus is
            potentially associated with higher risk of breast cancer.
            Alternatively spliced transcript variants encoding different
            isoforms have been noted for this gene. [provided by RefSeq, Dec
            2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.160573.1,
                                           SRR1803615.238483.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393915.9/ ENSP00000377492.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..725
                     /product="hyaluronan mediated motility receptor isoform a"
                     /note="receptor for hyaluronan-mediated motility;
                     intracellular hyaluronic acid-binding protein"
                     /calculated_mol_wt=84098
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75330.2)"
     Region          16..339
                     /region_name="HMMR_N"
                     /note="Hyaluronan mediated motility receptor N-terminal;
                     pfam15905"
                     /db_xref="CDD:464932"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75330.2)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75330.2)"
     Region          <193..577
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          366..547
                     /region_name="Required for interaction with FAM83D.
                     /evidence=ECO:0000269|PubMed:22965910"
                     /note="propagated from UniProtKB/Swiss-Prot (O75330.2)"
     Site            478
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75330.2)"
     Region          553..709
                     /region_name="HMMR_C"
                     /note="Hyaluronan mediated motility receptor C-terminal;
                     pfam15908"
                     /db_xref="CDD:464934"
     Site            568
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75330.2)"
     Site            589
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75330.2)"
     Region          636..646
                     /region_name="Hyaluronic acid-binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75330.2)"
     Region          658..667
                     /region_name="Hyaluronic acid-binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75330.2)"
     Site            704
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75330.2)"
     CDS             1..725
                     /gene="HMMR"
                     /gene_synonym="CD168; IHABP; RHAMM"
                     /coded_by="NM_001142556.2:62..2239"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47334.1"
                     /db_xref="GeneID:3161"
                     /db_xref="HGNC:HGNC:5012"
                     /db_xref="MIM:600936"
ORIGIN      
        1 msfpkaplkr fndpsgcaps pgaydvktle vlkgpvsfqk sqrfkqqkes kqnlnvdkdt
       61 tlpasarkvk sseskkesqk ndkdlkilek eirvllqerg aqdrriqdle telekmearl
      121 naalrektsl sannatlekq lieltrtnel lkskfsengn qknlrilsle lmklrnkret
      181 kmrgmmakqe gmemklqvtq rsleesqgki aqlegklvsi ekekidekse teklleyiee
      241 iscasdqvek ykldiaqlee nlkekndeil slkqsleeni vilskqvedl nvkcqlleke
      301 kedhvnrnre hnenlnaemq nlkqkfileq qereklqqke lqidsllqqe kelssslhqk
      361 lcsfqeemvk eknlfeeelk qtldeldklq qkeeqaerlv kqleeeaksr aeelklleek
      421 lkgkeaelek ssaahtqatl llqekydsmv qsledvtaqf esykaltase iedlklenss
      481 lqekaakagk naedvqhqil atessnqeyv rmlldlqtks alketeikei tvsflqkitd
      541 lqnqlkqqee dfrkqledee grkaekentt aelteeinkw rllyeelynk tkpfqlqlda
      601 fevekqalln ehgaaqeqln kirdsyakll ghqnlkqkik hvvklkdens qlksevsklr
      661 cqlakkkqse tklqeelnkv lgikhfdpsk afhheskenf alktplkegn tncyrapmec
      721 qeswk
//
LOCUS       NP_006464                622 aa            linear   PRI 27-APR-2025
DEFINITION  TAF6-like RNA polymerase II p300/CBP-associated factor-associated
            factor 65 kDa subunit 6L [Homo sapiens].
ACCESSION   NP_006464 NP_060806
VERSION     NP_006464.1
DBSOURCE    REFSEQ: accession NM_006473.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 622)
  AUTHORS   Nagy,Z., Riss,A., Romier,C., le Guezennec,X., Dongre,A.R.,
            Orpinell,M., Han,J., Stunnenberg,H. and Tora,L.
  TITLE     The human SPT20-containing SAGA complex plays a direct role in the
            regulation of endoplasmic reticulum stress-induced genes
  JOURNAL   Mol Cell Biol 29 (6), 1649-1660 (2009)
   PUBMED   19114550
REFERENCE   5  (residues 1 to 622)
  AUTHORS   Clarke,D.L., Sutcliffe,A., Deacon,K., Bradbury,D., Corbett,L. and
            Knox,A.J.
  TITLE     PKCbetaII augments NF-kappaB-dependent transcription at the CCL11
            promoter via p300/CBP-associated factor recruitment and histone H4
            acetylation
  JOURNAL   J Immunol 181 (5), 3503-3514 (2008)
   PUBMED   18714023
  REMARK    GeneRIF: protein kinase C betaII augments NF-kappaB-mediated
            TNF-alpha-induced transcription of the target gene CCL11, promoting
            p65 association with the CCL11 promoter, in human airway smooth
            muscle cells by phosphorylating p300/CBP-associated factor
REFERENCE   6  (residues 1 to 622)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   7  (residues 1 to 622)
  AUTHORS   Brand,M., Moggs,J.G., Oulad-Abdelghani,M., Lejeune,F.,
            Dilworth,F.J., Stevenin,J., Almouzni,G. and Tora,L.
  TITLE     UV-damaged DNA-binding protein in the TFTC complex links DNA damage
            recognition to nucleosome acetylation
  JOURNAL   EMBO J 20 (12), 3187-3196 (2001)
   PUBMED   11406595
REFERENCE   8  (residues 1 to 622)
  AUTHORS   Schiltz,R.L., Mizzen,C.A., Vassilev,A., Cook,R.G., Allis,C.D. and
            Nakatani,Y.
  TITLE     Overlapping but distinct patterns of histone acetylation by the
            human coactivators p300 and PCAF within nucleosomal substrates
  JOURNAL   J Biol Chem 274 (3), 1189-1192 (1999)
   PUBMED   9880483
REFERENCE   9  (residues 1 to 622)
  AUTHORS   Ogryzko,V.V., Kotani,T., Zhang,X., Schiltz,R.L., Howard,T.,
            Yang,X.J., Howard,B.H., Qin,J. and Nakatani,Y.
  TITLE     Histone-like TAFs within the PCAF histone acetylase complex
  JOURNAL   Cell 94 (1), 35-44 (1998)
   PUBMED   9674425
REFERENCE   10 (residues 1 to 622)
  AUTHORS   Struhl,K. and Moqtaderi,Z.
  TITLE     The TAFs in the HAT
  JOURNAL   Cell 94 (1), 1-4 (1998)
   PUBMED   9674419
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC311213.1, BC008785.2 and
            AK289499.1.
            
            On Jan 9, 2004 this sequence version replaced NP_060806.1.
            
            Summary: Initiation of transcription by RNA polymerase II requires
            the activities of more than 70 polypeptides. The protein that
            coordinates these activities is transcription factor IID (TFIID),
            which binds to the core promoter to position the polymerase
            properly, serves as the scaffold for assembly of the remainder of
            the transcription complex, and acts as a channel for regulatory
            signals. TFIID is composed of the TATA-binding protein (TBP) and a
            group of evolutionarily conserved proteins known as TBP-associated
            factors or TAFs. TAFs may participate in basal transcription, serve
            as coactivators, function in promoter recognition or modify general
            transcription factors (GTFs) to facilitate complex assembly and
            transcription initiation. This gene encodes a protein that is a
            component of the PCAF histone acetylase complex and structurally
            similar to one of the histone-like TAFs, TAF6. The PCAF histone
            acetylase complex, which is composed of more than 20 polypeptides
            some of which are TAFs, is required for myogenic transcription and
            differentiation. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008785.2, AK289499.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294168.8/ ENSP00000294168.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..622
                     /product="TAF6-like RNA polymerase II p300/CBP-associated
                     factor-associated factor 65 kDa subunit 6L"
                     /note="p300/CBP-associated factor (PCAF)-associated factor
                     65; PAF65-alpha; PCAF-associated factor 65-alpha;
                     TAF6-like RNA polymerase II, p300/CBP-associated factor
                     (PCAF)-associated factor, 65kDa"
                     /calculated_mol_wt=67683
     Region          12..82
                     /region_name="HFD_TAF6L"
                     /note="histone-fold domain found in TAF6-like RNA
                     polymerase II p300/CBP-associated factor-associated factor
                     65 kDa subunit 6L (TAF6L) and similar proteins; cd22932"
                     /db_xref="CDD:467056"
     Region          153..365
                     /region_name="TAF6C"
                     /note="C-terminal domain of TATA Binding Protein (TBP)
                     Associated Factor 6 (TAF6); cd08050"
                     /db_xref="CDD:381749"
     Site            order(155..157,159..160,163,174..175,178,182,185..186,192)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:381749"
     Region          155..186
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          193..225
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          235..278
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          285..317
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          319..364
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          403..430
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6J9.1)"
     Region          457..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6J9.1)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6J9.1)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6J9.1)"
     Site            555
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6J9.1)"
     Site            561
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6J9.1)"
     Site            593
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6J9.1)"
     CDS             1..622
                     /gene="TAF6L"
                     /gene_synonym="PAF65A"
                     /coded_by="NM_006473.4:109..1977"
                     /db_xref="CCDS:CCDS8035.1"
                     /db_xref="GeneID:10629"
                     /db_xref="HGNC:HGNC:17305"
                     /db_xref="MIM:602946"
ORIGIN      
        1 msereerrfv eipresvrlm aestglelsd evaallaedv cyrlreatqn ssqfmkhtkr
       61 rkltvedfnr alrwssveav cgygsqealp mrparegely fpedrevnlv elalatnipk
      121 gcaetavrvh vsyldgkgnl apqgsvpsav ssltddllky yhqvtravlg ddpqlmkval
      181 qdlqtnskig allpyfvyvv sgvksvshdl eqlhrllqva rslfrnphlc lgpyvrclvg
      241 svlycvlepl aasinplndh wtlrdgaall lshifwthgd lvsglyqhil lslqkiladp
      301 vrplcchyga vvglhalgwk avervlyphl stywtnlqav lddysvsnaq vkadghkvyg
      361 ailvaverll kmkaqaaepn rggpggrgcr rlddlpwdsl lfqesssggg aepsfgsglp
      421 lppggagped pslsvtladi yrelyaffgd slatrfgtgq paptaprppg dkkepaaapd
      481 svrkmpqlta saivsphgde sprgsggggp asasgpaase srplprvhra rgaprqqgpg
      541 tgtrdvfqks rfaprgaphf rfiiagrqag rrcrgrlfqt afpapygpsp asryvqklpm
      601 igrtsrparr walsdyslyl pl
//
LOCUS       NP_076974                176 aa            linear   PRI 27-APR-2025
DEFINITION  kxDL motif-containing protein 1 [Homo sapiens].
ACCESSION   NP_076974
VERSION     NP_076974.2
DBSOURCE    REFSEQ: accession NM_024069.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Tunganuntarat,J., Kanjanasirirat,P., Khumpanied,T.,
            Benjaskulluecha,S., Wongprom,B., Palaga,T., Siregar,T.A.P.,
            Borwornpinyo,S., Chaiprasert,A., Palittapongarnpim,P. and
            Ponpuak,M.
  TITLE     BORC complex specific components and Kinesin-1 mediate autophagy
            evasion by the autophagy-resistant Mycobacterium tuberculosis
            Beijing strain
  JOURNAL   Sci Rep 13 (1), 1663 (2023)
   PUBMED   36717601
  REMARK    GeneRIF: BORC complex specific components and Kinesin-1 mediate
            autophagy evasion by the autophagy-resistant Mycobacterium
            tuberculosis Beijing strain.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 176)
  AUTHORS   Pu,J., Schindler,C., Jia,R., Jarnik,M., Backlund,P. and
            Bonifacino,J.S.
  TITLE     BORC, a multisubunit complex that regulates lysosome positioning
  JOURNAL   Dev Cell 33 (2), 176-188 (2015)
   PUBMED   25898167
REFERENCE   7  (residues 1 to 176)
  AUTHORS   Yang,Q., He,X., Yang,L., Zhou,Z., Cullinane,A.R., Wei,A., Zhang,Z.,
            Hao,Z., Zhang,A., He,M., Feng,Y., Gao,X., Gahl,W.A., Huizing,M. and
            Li,W.
  TITLE     The BLOS1-interacting protein KXD1 is involved in the biogenesis of
            lysosome-related organelles
  JOURNAL   Traffic 13 (8), 1160-1169 (2012)
   PUBMED   22554196
  REMARK    GeneRIF: KXD1 interacts with BLOS1.
REFERENCE   8  (residues 1 to 176)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   9  (residues 1 to 176)
  AUTHORS   Hayes,M.J., Bryon,K., Satkurunathan,J. and Levine,T.P.
  TITLE     Yeast homologues of three BLOC-1 subunits highlight KxDL proteins
            as conserved interactors of BLOC-1
  JOURNAL   Traffic 12 (3), 260-268 (2011)
   PUBMED   21159114
REFERENCE   10 (residues 1 to 176)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK098346.1 and AC005253.1.
            
            On Feb 3, 2010 this sequence version replaced NP_076974.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001080.2, SRR3476690.619265.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222307.9/ ENSP00000222307.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..176
                     /product="kxDL motif-containing protein 1"
                     /note="UPF0459 protein C19orf50; BLOC-1 related complex
                     subunit 4"
                     /calculated_mol_wt=19537
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BQD3.2)"
     Region          14..93
                     /region_name="KxDL"
                     /note="Uncharacterized conserved protein; pfam10241"
                     /db_xref="CDD:463018"
     Region          95..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQD3.2)"
     CDS             1..176
                     /gene="KXD1"
                     /gene_synonym="BORCS4; C10orf50; C19orf50; KXDL; MST096;
                     MSTP096"
                     /coded_by="NM_024069.4:67..597"
                     /db_xref="CCDS:CCDS12381.1"
                     /db_xref="GeneID:79036"
                     /db_xref="HGNC:HGNC:28420"
                     /db_xref="MIM:615178"
ORIGIN      
        1 mdlpdsasrv fcgrilsmvn tddvnaiila qknmldrfek tnemllnfnn lssarlqqms
       61 erflhhtrtl vemkrdldsi frrirtlkgk larqhpeafs hipeasflee ededpippst
      121 tttiatseqs tgscdtspdt vspslspgfe dlshvqpgsp aingrsqtdd eemtge
//
LOCUS       NP_003601                368 aa            linear   PRI 27-APR-2025
DEFINITION  mRNA export factor RAE1 [Homo sapiens].
ACCESSION   NP_003601
VERSION     NP_003601.1
DBSOURCE    REFSEQ: accession NM_003610.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Makio,T., Zhang,K., Love,N., Mast,F.D., Liu,X., Elaish,M.,
            Hobman,T., Aitchison,J.D., Fontoura,B.M.A. and Wozniak,R.W.
  TITLE     SARS-CoV-2 Orf6 is positioned in the nuclear pore complex by Rae1
            to inhibit nucleocytoplasmic transport
  JOURNAL   Mol Biol Cell 35 (5), ar62 (2024)
   PUBMED   38507240
  REMARK    GeneRIF: SARS-CoV-2 Orf6 is positioned in the nuclear pore complex
            by Rae1 to inhibit nucleocytoplasmic transport.
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Berkel,C. and Cacan,E.
  TITLE     Super-Enhancer-Driven RAE1 Shows Higher Protein Levels in Tumor
            Compared to Adjacent Nonmalignant Stroma in High-Grade Serous
            Ovarian Cancer Patients
  JOURNAL   Reprod Sci 30 (8), 2397-2400 (2023)
   PUBMED   36810690
  REMARK    GeneRIF: Super-Enhancer-Driven RAE1 Shows Higher Protein Levels in
            Tumor Compared to Adjacent Nonmalignant Stroma in High-Grade Serous
            Ovarian Cancer Patients.
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Krachmarova,E., Petkov,P., Lilkova,E., Ilieva,N., Rangelov,M.,
            Todorova,N., Malinova,K., Hristova,R., Nacheva,G., Gospodinov,A.
            and Litov,L.
  TITLE     Insights into the SARS-CoV-2 ORF6 Mechanism of Action
  JOURNAL   Int J Mol Sci 24 (14), 11589 (2023)
   PUBMED   37511350
  REMARK    GeneRIF: Insights into the SARS-CoV-2 ORF6 Mechanism of Action.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Pritchard,C.E., Fornerod,M., Kasper,L.H. and van Deursen,J.M.
  TITLE     RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like
            NUP98 motif at the nuclear pore complex through multiple domains
  JOURNAL   J Cell Biol 145 (2), 237-254 (1999)
   PUBMED   10209021
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Matsuoka,Y., Takagi,M., Ban,T., Miyazaki,M., Yamamoto,T., Kondo,Y.
            and Yoneda,Y.
  TITLE     Identification and characterization of nuclear pore subcomplexes in
            mitotic extract of human somatic cells
  JOURNAL   Biochem Biophys Res Commun 254 (2), 417-423 (1999)
   PUBMED   9918853
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Bharathi,A., Ghosh,A., Whalen,W.A., Yoon,J.H., Pu,R., Dasso,M. and
            Dhar,R.
  TITLE     The human RAE1 gene is a functional homologue of
            Schizosaccharomyces pombe rae1 gene involved in nuclear export of
            Poly(A)+ RNA
  JOURNAL   Gene 198 (1-2), 251-258 (1997)
   PUBMED   9370289
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Kraemer,D. and Blobel,G.
  TITLE     mRNA binding protein mrnp 41 localizes to both nucleus and
            cytoplasm
  JOURNAL   Proc Natl Acad Sci U S A 94 (17), 9119-9124 (1997)
   PUBMED   9256445
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135939.12, U84720.1,
            AY349350.1, AI341915.1 and AL109955.38.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Mutations in the Schizosaccharomyces pombe Rae1 and
            Saccharomyces cerevisiae Gle2 genes have been shown to result in
            accumulation of poly(A)-containing mRNA in the nucleus, suggesting
            that the encoded proteins are involved in RNA export. The protein
            encoded by this gene is a homolog of yeast Rae1. It contains four
            WD40 motifs, and has been shown to localize to distinct foci in the
            nucleoplasm, to the nuclear rim, and to meshwork-like structures
            throughout the cytoplasm. This gene is thought to be involved in
            nucleocytoplasmic transport, and in directly or indirectly
            attaching cytoplasmic mRNPs to the cytoskeleton. Alternatively
            spliced transcript variants encoding the same protein have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) differs from variant 2 in the
            5' UTR and encodes the same protein as variant 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.225034.1,
                                           SRR1660803.95178.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395841.7/ ENSP00000379182.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.31"
     Protein         1..368
                     /product="mRNA export factor RAE1"
                     /note="homolog of yeast Rae1 (Bharathi) mRNA-associated
                     protein of 41 kDa (Kraemer); mRNA-associated protein MRNP
                     41; mRNA export protein; RAE1 RNA export 1 homolog;
                     mRNA-binding protein, 41-kD; mRNA export factor;
                     migration-inducing gene 14; rae1 protein homolog"
                     /calculated_mol_wt=40837
     Region          15..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78406.1)"
     Region          37..79
                     /region_name="WD 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:20498086"
                     /note="propagated from UniProtKB/Swiss-Prot (P78406.1)"
     Region          <39..335
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          42..84
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          84..114
                     /region_name="WD 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:20498086"
                     /note="propagated from UniProtKB/Swiss-Prot (P78406.1)"
     Region          90..125
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..157
                     /region_name="WD 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:20498086"
                     /note="propagated from UniProtKB/Swiss-Prot (P78406.1)"
     Region          130..168
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..206
                     /region_name="WD 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:20498086"
                     /note="propagated from UniProtKB/Swiss-Prot (P78406.1)"
     Region          174..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          215..258
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          215..255
                     /region_name="WD 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:20498086"
                     /note="propagated from UniProtKB/Swiss-Prot (P78406.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P78406.1)"
     Region          271..301
                     /region_name="WD 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:20498086"
                     /note="propagated from UniProtKB/Swiss-Prot (P78406.1)"
     Region          276..326
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          310..346
                     /region_name="WD 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:20498086"
                     /note="propagated from UniProtKB/Swiss-Prot (P78406.1)"
     CDS             1..368
                     /gene="RAE1"
                     /gene_synonym="dJ481F12.3; dJ800J21.1; Gle2; MIG14;
                     Mnrp41; MRNP41"
                     /coded_by="NM_003610.4:176..1282"
                     /db_xref="CCDS:CCDS13458.1"
                     /db_xref="GeneID:8480"
                     /db_xref="HGNC:HGNC:9828"
                     /db_xref="MIM:603343"
ORIGIN      
        1 mslfgttsgf gtsgtsmfgs attdnhnpmk dievtsspdd sigclsfspp tlpgnfliag
       61 swandvrcwe vqdsgqtipk aqqmhtgpvl dvcwsddgsk vftascdkta kmwdlssnqa
      121 iqiaqhdapv ktihwikapn yscvmtgswd ktlkfwdtrs snpmmvlqlp ercycadviy
      181 pmavvataer glivyqlenq psefrriesp lkhqhrcvai fkdkqnkptg falgsiegrv
      241 aihyinppnp akdnftfkch rsngtntsap qdiyavngia fhpvhgtlat vgsdgrfsfw
      301 dkdartklkt seqldqpisa ccfnhngnif ayassydwsk ghefynpqkk nyiflrnaae
      361 elkprnkk
//
LOCUS       NP_071914                168 aa            linear   PRI 27-APR-2025
DEFINITION  gremlin-2 precursor [Homo sapiens].
ACCESSION   NP_071914
VERSION     NP_071914.3
DBSOURCE    REFSEQ: accession NM_022469.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Zhang,Z. and Zhu,X.
  TITLE     MiR-103a-3p Contributes to the Progression of Colorectal Cancer by
            Regulating GREM2 Expression
  JOURNAL   Yonsei Med J 63 (6), 520-529 (2022)
   PUBMED   35619575
  REMARK    GeneRIF: MiR-103a-3p Contributes to the Progression of Colorectal
            Cancer by Regulating GREM2 Expression.
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Liu,W., Li,D., Yang,M., Wang,L., Xu,Y., Chen,N., Zhang,Z., Shi,J.,
            Li,W., Zhao,S., Gao,A., Chen,Y., Ma,Q., Zheng,R., Wu,S., Zhang,Y.,
            Chen,Y., Qian,S., Bi,Y., Gu,W., Tang,Q., Ning,G., Liu,R., Wang,W.,
            Hong,J. and Wang,J.
  TITLE     GREM2 is associated with human central obesity and inhibits
            visceral preadipocyte browning
  JOURNAL   EBioMedicine 78, 103969 (2022)
   PUBMED   35349825
  REMARK    GeneRIF: GREM2 is associated with human central obesity and
            inhibits visceral preadipocyte browning.
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Williams,M., Zeng,Y., Chiquet,B., Jacob,H., Kurtis Kasper,F.,
            Harrington,D.A., English,J., Akyalcin,S. and Letra,A.
  TITLE     Functional characterization of ATF1, GREM2 AND WNT10B variants
            associated with tooth agenesis
  JOURNAL   Orthod Craniofac Res 24 (4), 486-493 (2021)
   PUBMED   33369218
  REMARK    GeneRIF: Functional characterization of ATF1, GREM2 AND WNT10B
            variants associated with tooth agenesis.
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Shan,G., Gu,J., Zhou,D., Li,L., Cheng,W., Wang,Y., Tang,T. and
            Wang,X.
  TITLE     Cancer-associated fibroblast-secreted exosomal miR-423-5p promotes
            chemotherapy resistance in prostate cancer by targeting GREM2
            through the TGF-beta signaling pathway
  JOURNAL   Exp Mol Med 52 (11), 1809-1822 (2020)
   PUBMED   33144675
  REMARK    GeneRIF: Cancer-associated fibroblast-secreted exosomal miR-423-5p
            promotes chemotherapy resistance in prostate cancer by targeting
            GREM2 through the TGF-beta signaling pathway.
REFERENCE   5  (residues 1 to 168)
  AUTHORS   Feng,Y., Zhu,L., Gu,Y., Wang,L.J., Niu,B.J., Cai,F. and Chen,L.
  TITLE     Association of Gremlin-2 gene polymorphisms with osteoporosis risk
            in Chinese postmenopausal women
  JOURNAL   Biosci Rep 40 (4) (2020)
   PUBMED   32297643
  REMARK    GeneRIF: Association of Gremlin-2 gene polymorphisms with
            osteoporosis risk in Chinese postmenopausal women.
REFERENCE   6  (residues 1 to 168)
  AUTHORS   Gazzerro,E. and Canalis,E.
  TITLE     Bone morphogenetic proteins and their antagonists
  JOURNAL   Rev Endocr Metab Disord 7 (1-2), 51-65 (2006)
   PUBMED   17029022
  REMARK    Review article
REFERENCE   7  (residues 1 to 168)
  AUTHORS   Chen,D., Zhao,M. and Mundy,G.R.
  TITLE     Bone morphogenetic proteins
  JOURNAL   Growth Factors 22 (4), 233-241 (2004)
   PUBMED   15621726
  REMARK    Review article
REFERENCE   8  (residues 1 to 168)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of human CKTSF1B2 and CKTSF1B3
            genes in silico
  JOURNAL   Oncol Rep 12 (2), 423-427 (2004)
   PUBMED   15254711
REFERENCE   9  (residues 1 to 168)
  AUTHORS   Sudo,S., Avsian-Kretchmer,O., Wang,L.S. and Hsueh,A.J.
  TITLE     Protein related to DAN and cerberus is a bone morphogenetic protein
            antagonist that participates in ovarian paracrine regulation
  JOURNAL   J Biol Chem 279 (22), 23134-23141 (2004)
   PUBMED   15039429
REFERENCE   10 (residues 1 to 168)
  AUTHORS   Avsian-Kretchmer,O. and Hsueh,A.J.
  TITLE     Comparative genomic analysis of the eight-membered ring cystine
            knot-containing bone morphogenetic protein antagonists
  JOURNAL   Mol Endocrinol 18 (1), 1-12 (2004)
   PUBMED   14525956
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL358176.22, AK024848.1 and
            BQ005641.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 26, 2005 this sequence version replaced NP_071914.2.
            
            Summary: This gene encodes a member of the BMP (bone morphogenic
            protein) antagonist family. Like BMPs, BMP antagonists contain
            cystine knots and typically form homo- and heterodimers. The CAN
            (cerberus and dan) subfamily of BMP antagonists, to which this gene
            belongs, is characterized by a C-terminal cystine knot with an
            eight-membered ring. The antagonistic effect of the secreted
            glycosylated protein encoded by this gene is likely due to its
            direct binding to BMP proteins. As an antagonist of BMP, this gene
            may play a role in regulating organogenesis, body patterning, and
            tissue differentiation. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC046632.1, SRR14038194.1304091.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000318160.5/ ENSP00000318650.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..168
                     /product="gremlin-2 precursor"
                     /note="protein related to DAN and cerberus; cysteine knot
                     superfamily 1, BMP antagonist 2; gremlin-2; DAN domain
                     family member 3; gremlin 2, cysteine knot superfamily,
                     homolog"
                     /calculated_mol_wt=16974
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2365
     mat_peptide     22..168
                     /product="gremlin-2"
                     /calculated_mol_wt=16974
     Site            40
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H772.1)"
     Region          51..158
                     /region_name="DAN"
                     /note="DAN domain; pfam03045"
                     /db_xref="CDD:460786"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H772.1)"
     CDS             1..168
                     /gene="GREM2"
                     /gene_synonym="CKTSF1B2; DAND3; PRDC; STHAG9"
                     /coded_by="NM_022469.4:274..780"
                     /db_xref="CCDS:CCDS31070.1"
                     /db_xref="GeneID:64388"
                     /db_xref="HGNC:HGNC:17655"
                     /db_xref="MIM:608832"
ORIGIN      
        1 mfwklslslf lvavlvkvae arknrpagai pspykdgssn nserwqhqik evlassqeal
       61 vvterkylks dwcktqplrq tvseegcrsr tilnrfcygq cnsfyiprhv kkeeesfqsc
      121 afckpqrvts vlvelecpgl dppfrlkkiq kvkqcrcmsv nlsdsdkq
//
LOCUS       NP_061943                483 aa            linear   PRI 27-APR-2025
DEFINITION  probable ATP-dependent RNA helicase DDX49 [Homo sapiens].
ACCESSION   NP_061943
VERSION     NP_061943.2
DBSOURCE    REFSEQ: accession NM_019070.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Tao,J., Ge,Q., Meng,J., Liang,C., Hao,Z. and Zhou,J.
  TITLE     Overexpression of DDX49 in prostate cancer is associated with poor
            prognosis
  JOURNAL   BMC Urol 23 (1), 66 (2023)
   PUBMED   37106339
  REMARK    GeneRIF: Overexpression of DDX49 in prostate cancer is associated
            with poor prognosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Chen,Y., Ma,Q. and Sun,N.
  TITLE     DDX49 Promotes Proliferation and Metastasis of Cervical Cancer by
            Regulation of AKT and Wnt/beta-Catenin Signalings
  JOURNAL   Ann Clin Lab Sci 53 (2), 271-277 (2023)
   PUBMED   37094865
  REMARK    GeneRIF: DDX49 Promotes Proliferation and Metastasis of Cervical
            Cancer by Regulation of AKT and Wnt/beta-Catenin Signalings.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Serfecz,J.C., Hong,Y., Gay,L.A., Shekhar,R., Turner,P.C. and
            Renne,R.
  TITLE     DExD/H Box Helicases DDX24 and DDX49 Inhibit Reactivation of
            Kaposi's Sarcoma Associated Herpesvirus by Interacting with Viral
            mRNAs
  JOURNAL   Viruses 14 (10), 2083 (2022)
   PUBMED   36298642
  REMARK    GeneRIF: DExD/H Box Helicases DDX24 and DDX49 Inhibit Reactivation
            of Kaposi's Sarcoma Associated Herpesvirus by Interacting with
            Viral mRNAs.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Dai,H., Feng,J., Nan,Z., Wei,L., Lin,F., Jin,R., Zhang,S., Wang,X.
            and Pan,L.
  TITLE     Morphine may act via DDX49 to inhibit hepatocellular carcinoma cell
            growth
  JOURNAL   Aging (Albany NY) 13 (9), 12766-12779 (2021)
   PUBMED   33952717
  REMARK    GeneRIF: Morphine may act via DDX49 to inhibit hepatocellular
            carcinoma cell growth.
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Lian,X., Xiang,D., Peng,C., Chen,J., Liao,M., Sun,G. and Zhang,Z.
  TITLE     DDX49 is a novel biomarker and therapeutic target for lung cancer
            metastases
  JOURNAL   J Cell Mol Med 24 (1), 1141-1145 (2020)
   PUBMED   31749282
  REMARK    GeneRIF: DDX49 is a novel biomarker and therapeutic target for lung
            cancer metastases.
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Awasthi,S., Verma,M., Mahesh,A., K Khan,M.I., Govindaraju,G.,
            Rajavelu,A., Chavali,P.L., Chavali,S. and Dhayalan,A.
  TITLE     DDX49 is an RNA helicase that affects translation by regulating
            mRNA export and the levels of pre-ribosomal RNA
  JOURNAL   Nucleic Acids Res 46 (12), 6304-6317 (2018)
   PUBMED   29618122
  REMARK    GeneRIF: DDX49 displays a robust ATPase and RNA helicase activity
            and it is involved in the export of poly (A)+ mRNAs to cytoplasm.
            DDX49 is localized in the nucleolus and regulates the steady state
            levels of pre-ribosomal 47S RNA and global translation.
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC002674.2 and AU148229.1.
            
            On Jun 9, 2003 this sequence version replaced NP_061943.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.537247.1, BC002674.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247003.9/ ENSP00000247003.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..483
                     /product="probable ATP-dependent RNA helicase DDX49"
                     /EC_number="3.6.4.13"
                     /note="DEAD box protein 49; DEAD (Asp-Glu-Ala-Asp) box
                     polypeptide 49"
                     /calculated_mol_wt=54095
     Region          1..441
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          2..30
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6V7.1)"
     Region          152..155
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6V7.1)"
     Region          444..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6V7.1)"
     CDS             1..483
                     /gene="DDX49"
                     /gene_synonym="Dbp8; R27090_2"
                     /coded_by="NM_019070.5:28..1479"
                     /db_xref="CCDS:CCDS12390.1"
                     /db_xref="GeneID:54555"
                     /db_xref="HGNC:HGNC:18684"
ORIGIN      
        1 magfaelgls swlveqcrql glkqptpvql gcipailegr dclgcaktgs gktaafvlpi
       61 lqklsedpyg ifclvltptr elayqiaeqf rvlgkplglk dciivggmdm vaqalelsrk
      121 phvviatpgr ladhlrssnt fsikkirflv mdeadrlleq gctdftvdle ailaavparr
      181 qtllfsatlt dtlrelqgla tnqpffweaq apvstveqld qryllvpekv kdaylvhliq
      241 rfqdehedws iiiftntckt cqilcmmlrk fsfptvalhs mmkqkerfaa lakfkssiyr
      301 iliatdvasr gldiptvqvv inhntpglpk iyihrvgrta ragrqgqait lvtqydihlv
      361 haieeqikkk leefsveeae vlqiltqvnv vrreceikle aahfdekkei nkrkqlileg
      421 kdpdleakrk aelakikqkn rrfkekveet lkrqkagrag hkgrpprtps gshsgpvpsq
      481 glv
//
LOCUS       NP_078896                541 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 329 [Homo sapiens].
ACCESSION   NP_078896
VERSION     NP_078896.3
DBSOURCE    REFSEQ: accession NM_024620.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Zhang,L., Feng,X.K., Ng,Y.K. and Li,S.C.
  TITLE     Reconstructing directed gene regulatory network by only gene
            expression data
  JOURNAL   BMC Genomics 17 Suppl 4 (Suppl 4), 430 (2016)
   PUBMED   27556418
  REMARK    GeneRIF: TYROBP influences a batch of genes that are related to
            Alzheimer's disease; ZNF329 and RB1 significantly regulate those
            'mesenchymal' gene expression signature genes for brain tumors.  By
            merely leveraging gene expression data, Context Based Dependency
            Network (CBDN) can efficiently infer the existence of gene-gene
            interactions as well as their regulatory directions.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008751.7, AK095349.1 and BC047501.1.
            
            On Jul 20, 2005 this sequence version replaced NP_078896.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB033762.1, SRR1660809.244312.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1968540 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000598312.6/ ENSP00000470008.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..541
                     /product="zinc finger protein 329"
                     /calculated_mol_wt=61595
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6GQR8; propagated from
                     UniProtKB/Swiss-Prot (Q86UD4.2)"
     Region          177..539
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          205..225
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          233..253
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(238,240,242,244..245,248..249,252,266,268,272..273,
                     276..277,280,294,296,298,300..301,304..305,308)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          261..281
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          289..309
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          317..337
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(322,324,326,328..329,332..333,336,350,352,356..357,
                     360..361,364,378,380,382,384..385,388..389,392)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          345..365
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          373..393
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          401..421
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          429..449
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(434,436,438,440..441,444..445,448,462,464,468..469,
                     472..473,476,490,492,494,496..497,500..501,504)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          457..477
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          485..505
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          513..533
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..541
                     /gene="ZNF329"
                     /coded_by="NM_024620.4:246..1871"
                     /db_xref="CCDS:CCDS12972.1"
                     /db_xref="GeneID:79673"
                     /db_xref="HGNC:HGNC:14209"
ORIGIN      
        1 mrlkmttrnf perevpcdve verftrevpc lsslgdgwdc enqeghlrqs altlekpgtq
       61 eaiceypgfg ehliassdlp psqrvlatng fhapdsnvsg ldcdpalpsy pksyadkrtg
      121 dsdacgkgfn hsmevihgrn pvrekpykyp esvksfnhft slghqkimkr gkksyegknf
      181 eniftlsssl nenqrnlpge kqyrctecgk cfkrnsslvl hhrthtgekp ytcnecgksf
      241 sknynlivhq rihtgekpye cskcgkafsd gsaltqhqri htgekpyecl ecgktfnrns
      301 slilhqrtht gekpyrcnec gkpftdishl tvhlrihtge kpyecskcgk afrdgsyltq
      361 herthtgekp fecaecgksf nrnshlivhq kihsgekpye ckecgktfie saylirhqri
      421 htgekpygcn qcqklfrnia glirhqrtht gekpyecnqc gkafrdsscl tkhqrihtke
      481 tpyqcpecgk sfkqnshlav hqrlhsregp srcpqcgkmf qkssslvrhq rahlgeqpme
      541 t
//
LOCUS       NP_036271                458 aa            linear   PRI 27-APR-2025
DEFINITION  secretion-regulating guanine nucleotide exchange factor [Homo
            sapiens].
ACCESSION   NP_036271
VERSION     NP_036271.1
DBSOURCE    REFSEQ: accession NM_012139.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Weimann,M., Grossmann,A., Woodsmith,J., Ozkan,Z., Birth,P.,
            Meierhofer,D., Benlasfer,N., Valovka,T., Timmermann,B.,
            Wanker,E.E., Sauer,S. and Stelzl,U.
  TITLE     A Y2H-seq approach defines the human protein methyltransferase
            interactome
  JOURNAL   Nat Methods 10 (4), 339-342 (2013)
   PUBMED   23455924
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Sjolinder,M., Uhlmann,J. and Ponstingl,H.
  TITLE     Characterisation of an evolutionary conserved protein interacting
            with the putative guanine nucleotide exchange factor DelGEF and
            modulating secretion
  JOURNAL   Exp Cell Res 294 (1), 68-76 (2004)
   PUBMED   14980502
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Sjolinder,M., Uhlmann,J. and Ponstingl,H.
  TITLE     DelGEF, a homologue of the Ran guanine nucleotide exchange factor
            RanGEF, binds to the exocyst component Sec5 and modulates secretion
  JOURNAL   FEBS Lett 532 (1-2), 211-215 (2002)
   PUBMED   12459492
  REMARK    GeneRIF: DelGEF binds to the human homologue of Sec5 and modulates
            secretion.
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Uhlmann,J., Wiemann,S. and Ponstingl,H.
  TITLE     DelGEF, an RCC1-related protein encoded by a gene on chromosome
            11p14 critical for two forms of hereditary deafness
  JOURNAL   FEBS Lett 460 (1), 153-160 (1999)
   PUBMED   10571079
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK292286.1 and BC065375.1.
            
            Transcript Variant: This variant (1) represents the protein-coding
            transcript.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065375.1, AK292286.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265965.10/ ENSP00000265965.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..458
                     /product="secretion-regulating guanine nucleotide exchange
                     factor"
                     /note="deafness locus associated putative guanine
                     nucleotide exchange factor; guanine nucleotide exchange
                     factor-related protein"
                     /calculated_mol_wt=48850
     Region          15..67
                     /region_name="RCC1 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGK8.2)"
     Region          23..375
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          68..119
                     /region_name="RCC1 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGK8.2)"
     Region          120..171
                     /region_name="RCC1 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGK8.2)"
     Region          172..230
                     /region_name="RCC1 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGK8.2)"
     Region          231..283
                     /region_name="RCC1 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGK8.2)"
     Region          284..351
                     /region_name="RCC1 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGK8.2)"
     Region          352..402
                     /region_name="RCC1 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGK8.2)"
     Region          420..458
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGK8.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UGK8.2)"
     CDS             1..458
                     /gene="SERGEF"
                     /gene_synonym="DELGEF; Gnefr"
                     /coded_by="NM_012139.4:38..1414"
                     /db_xref="CCDS:CCDS7828.1"
                     /db_xref="GeneID:26297"
                     /db_xref="HGNC:HGNC:17499"
                     /db_xref="MIM:606051"
ORIGIN      
        1 merepsasea apaaaalfaw gansygqlgl ghkedvllpq qlndfckprs vrritggggh
       61 savvtdggdl fvcglnkdgq lglghtedip yftpckslfg cpiqqvacgw dftimlteng
      121 qvlscgsnsf gqlgvphgpr rcvvpqaiel hkekvvciaa glrhavaata sgivfqwgtg
      181 lascgrrlcp gqtlplffta kepsrvtgle nskamcvlag sdhsasltda gevyvwgsnk
      241 hgqlaneaaf lpvpqkieah cfqnekvtai wsgwthlvaq tetgkmftwg radygqlgrk
      301 letyegwkle kqdsflpcsr ppnsmpssph cltgatevsc gsehnlaiig gvcyswgwne
      361 hgmcgdgtea nvwapkpvqa llsssgllvg cgaghslalc qlpahpalvq dpkvtylspd
      421 aiedtesqka mdkernwker qsetstqsqs dwsrnggl
//
LOCUS       NP_001347819             591 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF180 isoform 2 [Mus musculus].
ACCESSION   NP_001347819 XP_006517825
VERSION     NP_001347819.1
DBSOURCE    REFSEQ: accession NM_001360890.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Wang,K., Liu,F., Muchu,B., Deng,J., Peng,J., Xu,Y., Li,F. and
            Ouyang,M.
  TITLE     E3 ubiquitin ligase RNF180 mediates the ALKBH5/SMARCA5 axis to
            promote colon inflammation and Th17/Treg imbalance in ulcerative
            colitis mice
  JOURNAL   Arch Pharm Res 47 (7), 645-658 (2024)
   PUBMED   39060657
  REMARK    GeneRIF: E3 ubiquitin ligase RNF180 mediates the ALKBH5/SMARCA5
            axis to promote colon inflammation and Th17/Treg imbalance in
            ulcerative colitis mice.
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Zhao,Q., Liu,N., Xu,T. and Song,K.
  TITLE     RING finger gene 180 inhibits osteosarcoma progression through
            regulating chromobox homolog 4 ubiquitination
  JOURNAL   Cell Cycle 22 (10), 1246-1258 (2023)
   PUBMED   37095741
  REMARK    GeneRIF: RING finger gene 180 inhibits osteosarcoma progression
            through regulating chromobox homolog 4 ubiquitination.
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Kabayama,M., Sakoori,K., Yamada,K., Ornthanalai,V.G., Ota,M.,
            Morimura,N., Katayama,K., Murphy,N.P. and Aruga,J.
  TITLE     Rines E3 ubiquitin ligase regulates MAO-A levels and emotional
            responses
  JOURNAL   J Neurosci 33 (32), 12940-12953 (2013)
   PUBMED   23926250
  REMARK    GeneRIF: Rines is a critical regulator of the monoaminergic system
            and emotional behavior and identify a promising candidate drug
            target for treating diseases associated with emotion.
REFERENCE   5  (residues 1 to 591)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 591)
  AUTHORS   Ogawa,M., Mizugishi,K., Ishiguro,A., Koyabu,Y., Imai,Y.,
            Takahashi,R., Mikoshiba,K. and Aruga,J.
  TITLE     Rines/RNF180, a novel RING finger gene-encoded product, is a
            membrane-bound ubiquitin ligase
  JOURNAL   Genes Cells 13 (4), 397-409 (2008)
   PUBMED   18363970
  REMARK    GeneRIF: The involvement of RNF180 in the ubiquitin-proteasome
            pathway was further supported by its binding to the UbcH6
            ubiquitin-conjugating enzyme and by its trans-ubiquitination
            enhancing activities.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC075700.1 and AC154203.2.
            
            On Feb 16, 2018 this sequence version replaced XP_006517825.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC046775.1, AK157911.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164139 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 56.92 cM"
     Protein         1..591
                     /product="E3 ubiquitin-protein ligase RNF180 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF180; RING-type E3
                     ubiquitin transferase RNF180"
                     /calculated_mol_wt=67112
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3U827.2)"
     Region          281..488
                     /region_name="Interaction with ZIC2.
                     /evidence=ECO:0000269|PubMed:18363970"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U827.2)"
     Region          427..485
                     /region_name="RING-HC_RNF180"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 180 (RNF180) and similar proteins; cd16554"
                     /db_xref="CDD:438216"
     Region          490..590
                     /region_name="RNF180_C"
                     /note="E3 ubiquitin-protein ligase RNF180 C-terminus;
                     pfam19332"
                     /db_xref="CDD:437164"
     Site            564..584
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U827.2)"
     CDS             1..591
                     /gene="Rnf180"
                     /gene_synonym="3110001E11Rik; Rines"
                     /coded_by="NM_001360890.1:224..1999"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS88517.1"
                     /db_xref="GeneID:71816"
                     /db_xref="MGI:MGI:1919066"
ORIGIN      
        1 mkrseestst qspeeqtgtl hcwrcrkcia ssgcfmtple tqvvedrhes vdaqntchlw
       61 hmnvdalpew iscllqkaqw tvgklncpfc garlggfnfv stpkcscgql aavhlcksrt
      121 dhqaaqggrl mrpalkhlph pgvpsgcdke tlltgggskt rnhwllsmar nsnglgrlte
      181 alclevraty femknekllf kasdpkcqpf vpqpdtgrcp srashrkshs ldlnisekli
      241 llptlyeihr kptayprlne tgpidlsgla lpcsnsscsf qsppsfdpnm llhrlsvaph
      301 etqaqrgrec qcgleassvy sdhananslp flmdlpsagr svleasdqee hlsqldflrs
      361 asfplgtinh rlnnrerskl rtlrrqqrre rwlqkqgkys gvglldhmtv snemstdeet
      421 efpeekdsym cavcldvyfn pymcypchhi fcepclrtla kdnpastpcp lcrtiisrvf
      481 lqtelnnatk tfftkeylki kqsfqksssa kwplpscrkg fhlfggfhrr aapvtrrqfp
      541 hgahrmdylh feddsrgwwf dmdmviiyiy svnwvigfvv fcflcyfffp f
//
LOCUS       NP_001020371             263 aa            linear   PRI 27-APR-2025
DEFINITION  chymotrypsinogen B2 precursor [Homo sapiens].
ACCESSION   NP_001020371 XP_496169
VERSION     NP_001020371.3
DBSOURCE    REFSEQ: accession NM_001025200.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Nemeth,B.Z., Demcsak,A., Micsonai,A., Kiss,B., Schlosser,G.,
            Geisz,A., Hegyi,E., Sahin-Toth,M. and Pal,G.
  TITLE     Arg236 in human chymotrypsin B2 (CTRB2) is a key determinant of
            high enzyme activity, trypsinogen degradation capacity, and
            protection against pancreatitis
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1870 (9), 140831 (2022)
   PUBMED   35934298
  REMARK    GeneRIF: Arg236 in human chymotrypsin B2 (CTRB2) is a key
            determinant of high enzyme activity, trypsinogen degradation
            capacity, and protection against pancreatitis.
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Jermusyk,A., Zhong,J., Connelly,K.E., Gordon,N., Perera,S.,
            Abdolalizadeh,E., Zhang,T., O'Brien,A., Hoskins,J.W., Collins,I.,
            Eiser,D., Yuan,C., Risch,H.A., Jacobs,E.J., Li,D., Du,M.,
            Stolzenberg-Solomon,R.Z., Klein,A.P., Smith,J.P., Wolpin,B.M.,
            Chanock,S.J., Shi,J., Petersen,G.M., Westlake,C.J. and
            Amundadottir,L.T.
  CONSRTM   PanScan Consortium; PanC4 Consortium
  TITLE     A 584 bp deletion in CTRB2 inhibits chymotrypsin B2 activity and
            secretion and confers risk of pancreatic cancer
  JOURNAL   Am J Hum Genet 108 (10), 1852-1865 (2021)
   PUBMED   34559995
  REMARK    GeneRIF: A 584 bp deletion in CTRB2 inhibits chymotrypsin B2
            activity and secretion and confers risk of pancreatic cancer.
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Seltsam,K., Pentner,C., Weigl,F., Sutedjo,S., Zimmer,C., Beer,S.,
            Bugert,P., Ewers,M., Ruffert,C., Michl,P., Laumen,H., Witt,H. and
            Rosendahl,J.
  TITLE     Sequencing of the complex CTRB1-CTRB2 locus in chronic pancreatitis
  JOURNAL   Pancreatology 20 (8), 1598-1603 (2020)
   PUBMED   33036922
  REMARK    GeneRIF: Sequencing of the complex CTRB1-CTRB2 locus in chronic
            pancreatitis.
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Rosendahl,J., Kirsten,H., Hegyi,E., Kovacs,P., Weiss,F.U.,
            Laumen,H., Lichtner,P., Ruffert,C., Chen,J.M., Masson,E., Beer,S.,
            Zimmer,C., Seltsam,K., Algul,H., Buhler,F., Bruno,M.J., Bugert,P.,
            Burkhardt,R., Cavestro,G.M., Cichoz-Lach,H., Farre,A., Frank,J.,
            Gambaro,G., Gimpfl,S., Grallert,H., Griesmann,H., Grutzmann,R.,
            Hellerbrand,C., Hegyi,P., Hollenbach,M., Iordache,S., Jurkowska,G.,
            Keim,V., Kiefer,F., Krug,S., Landt,O., Leo,M.D., Lerch,M.M.,
            Levy,P., Loffler,M., Lohr,M., Ludwig,M., Macek,M., Malats,N.,
            Malecka-Panas,E., Malerba,G., Mann,K., Mayerle,J., Mohr,S., Te
            Morsche,R.H.M., Motyka,M., Mueller,S., Muller,T., Nothen,M.M.,
            Pedrazzoli,S., Pereira,S.P., Peters,A., Pfutzer,R., Real,F.X.,
            Rebours,V., Ridinger,M., Rietschel,M., Rosmann,E., Saftoiu,A.,
            Schneider,A., Schulz,H.U., Soranzo,N., Soyka,M., Simon,P.,
            Skipworth,J., Stickel,F., Strauch,K., Stumvoll,M., Testoni,P.A.,
            Tonjes,A., Werner,L., Werner,J., Wodarz,N., Ziegler,M.,
            Masamune,A., Mossner,J., Ferec,C., Michl,P., P H Drenth,J.,
            Witt,H., Scholz,M. and Sahin-Toth,M.
  CONSRTM   all members of the PanEuropean Working group on ACP
  TITLE     Genome-wide association study identifies inversion in the
            CTRB1-CTRB2 locus to modify risk for alcoholic and non-alcoholic
            chronic pancreatitis
  JOURNAL   Gut 67 (10), 1855-1863 (2018)
   PUBMED   28754779
  REMARK    GeneRIF: An inversion in the CTRB1-CTRB2 locus modifies risk for
            Alcoholic and Non-alcoholic Chronic Pancreatitis indicating that
            common pathomechanisms are involved in these inflammatory
            disorders.
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Tang,X.Y., Zou,W.B., Masson,E., Hu,L.H., Ferec,C., Chen,J.M.,
            Li,Z.S. and Liao,Z.
  TITLE     The CTRB1-CTRB2 risk allele for chronic pancreatitis discovered in
            European populations does not contribute to disease risk variation
            in the Chinese population due to near allele fixation
  JOURNAL   Gut 67 (7), 1368-1369 (2018)
   PUBMED   28951524
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Wolpin,B.M., Rizzato,C., Kraft,P., Kooperberg,C., Petersen,G.M.,
            Wang,Z., Arslan,A.A., Beane-Freeman,L., Bracci,P.M., Buring,J.,
            Canzian,F., Duell,E.J., Gallinger,S., Giles,G.G., Goodman,G.E.,
            Goodman,P.J., Jacobs,E.J., Kamineni,A., Klein,A.P., Kolonel,L.N.,
            Kulke,M.H., Li,D., Malats,N., Olson,S.H., Risch,H.A., Sesso,H.D.,
            Visvanathan,K., White,E., Zheng,W., Abnet,C.C., Albanes,D.,
            Andreotti,G., Austin,M.A., Barfield,R., Basso,D., Berndt,S.I.,
            Boutron-Ruault,M.C., Brotzman,M., Buchler,M.W.,
            Bueno-de-Mesquita,H.B., Bugert,P., Burdette,L., Campa,D.,
            Caporaso,N.E., Capurso,G., Chung,C., Cotterchio,M., Costello,E.,
            Elena,J., Funel,N., Gaziano,J.M., Giese,N.A., Giovannucci,E.L.,
            Goggins,M., Gorman,M.J., Gross,M., Haiman,C.A., Hassan,M.,
            Helzlsouer,K.J., Henderson,B.E., Holly,E.A., Hu,N., Hunter,D.J.,
            Innocenti,F., Jenab,M., Kaaks,R., Key,T.J., Khaw,K.T., Klein,E.A.,
            Kogevinas,M., Krogh,V., Kupcinskas,J., Kurtz,R.C., LaCroix,A.,
            Landi,M.T., Landi,S., Le Marchand,L., Mambrini,A., Mannisto,S.,
            Milne,R.L., Nakamura,Y., Oberg,A.L., Owzar,K., Patel,A.V.,
            Peeters,P.H., Peters,U., Pezzilli,R., Piepoli,A., Porta,M.,
            Real,F.X., Riboli,E., Rothman,N., Scarpa,A., Shu,X.O.,
            Silverman,D.T., Soucek,P., Sund,M., Talar-Wojnarowska,R.,
            Taylor,P.R., Theodoropoulos,G.E., Thornquist,M., Tjonneland,A.,
            Tobias,G.S., Trichopoulos,D., Vodicka,P., Wactawski-Wende,J.,
            Wentzensen,N., Wu,C., Yu,H., Yu,K., Zeleniuch-Jacquotte,A.,
            Hoover,R., Hartge,P., Fuchs,C., Chanock,S.J.,
            Stolzenberg-Solomon,R.S. and Amundadottir,L.T.
  TITLE     Genome-wide association study identifies multiple susceptibility
            loci for pancreatic cancer
  JOURNAL   Nat Genet 46 (9), 994-1000 (2014)
   PUBMED   25086665
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Hou,D.X., Ozawa,K., Tomita,N., Maeda,Y., Hashiguchi,T., Yokoyama,K.
            and Soeda,E.
  TITLE     Genomic cloning and partial characterization of human
            chymotrypsinogen gene
  JOURNAL   Jpn J Hum Genet 38 (4), 371-380 (1993)
   PUBMED   8186414
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Tomita,N., Izumoto,Y., Horii,A., Doi,S., Yokouchi,H., Ogawa,M.,
            Mori,T. and Matsubara,K.
  TITLE     Molecular cloning and nucleotide sequence of human pancreatic
            prechymotrypsinogen cDNA
  JOURNAL   Biochem Biophys Res Commun 158 (2), 569-575 (1989)
   PUBMED   2917002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK225933.1.
            
            On Nov 30, 2006 this sequence version replaced NP_001020371.2.
            
            Summary: This gene encodes a member of the serine protease family
            of enzymes and forms a principal precursor of the pancreatic
            proteolytic enzymes. The encoded preproprotein is synthesized in
            the acinar cells of the pancreas and secreted into the small
            intestine where it undergoes proteolytic activation to generate a
            functional enzyme. This CTRB2 gene is located head-to-head with the
            related CTRB1 gene. Some human populations have an alternate
            haplotype which inverts a 16.6 Kb region containing portions of
            intron 1, exon 1, and the upstream sequence of the CTRB1 and CTRB2
            genes. In this inversion haplotype exon 1 and flanking sequence is
            swapped in CTRB1 and CTRB2. This inversion is associated with
            differential gene expression and increased risk for chronic
            pancreatitis. The GRCh38 assembly represents the minor allele for
            SNP rs8048956 of the CTRB1 gene. SNP rs8048956 is diagnostic for
            this inversion. [provided by RefSeq, Jan 2021].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225933.1, AK291822.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303037.13/ ENSP00000303963.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..263
                     /product="chymotrypsinogen B2 precursor"
                     /EC_number="3.4.21.1"
                     /note="chymotrypsin B2"
                     /calculated_mol_wt=25911
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2030
     mat_peptide     19..263
                     /product="Chymotrypsinogen B2. /id=PRO_0000285870"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GPI1.2)"
                     /calculated_mol_wt=25911
     mat_peptide     19..31
                     /product="Chymotrypsin B2 chain A. /id=PRO_0000285871"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GPI1.2)"
                     /calculated_mol_wt=1263
     Region          34..259
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     mat_peptide     34..164
                     /product="Chymotrypsin B2 chain B. /id=PRO_0000285872"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GPI1.2)"
                     /calculated_mol_wt=14049
     Site            34
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(75,120,213)
                     /site_type="active"
                     /db_xref="CDD:238113"
     mat_peptide     167..263
                     /product="Chymotrypsin B2 chain C. /id=PRO_0000285873"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GPI1.2)"
                     /calculated_mol_wt=10207
     Site            order(207,232,234)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..263
                     /gene="CTRB2"
                     /coded_by="NM_001025200.4:21..812"
                     /db_xref="CCDS:CCDS32489.1"
                     /db_xref="GeneID:440387"
                     /db_xref="HGNC:HGNC:2522"
                     /db_xref="MIM:619620"
ORIGIN      
        1 maflwllscw allgttfgcg vpaihpvlsg lsrivngeda vpgswpwqvs lqdktgfhfc
       61 ggslisedwv vtaahcgvrt sdvvvagefd qgsdeeniqv lkiakvfknp kfsiltvnnd
      121 itllklatpa rfsqtvsavc lpsadddfpa gtlcattgwg ktkynanktp dklqqaalpl
      181 lsnaeckksw grritdvmic agasgvsscm gdsggplvcq kdgawtlvgi vswgsrtcst
      241 ttpavyarva klipwvqkil aan
//
LOCUS       NP_034977                228 aa            linear   ROD 27-APR-2025
DEFINITION  max-interacting protein 1 isoform a [Mus musculus].
ACCESSION   NP_034977
VERSION     NP_034977.1
DBSOURCE    REFSEQ: accession NM_010847.4
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Li,X., Xiao,S., Li,F., Fang,K., Wen,J. and Gong,H.
  TITLE     Max interacting protein 1 induces IL-17-producing T
            helper/regulatory T imbalance in osteoarthritis by upregulating
            tectonic family member 2
  JOURNAL   Tissue Cell 78, 101906 (2022)
   PUBMED   36049372
  REMARK    GeneRIF: Max interacting protein 1 induces IL-17-producing T
            helper/regulatory T imbalance in osteoarthritis by upregulating
            tectonic family member 2.
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Menendez-Montes,I., Escobar,B., Palacios,B., Gomez,M.J.,
            Izquierdo-Garcia,J.L., Flores,L., Jimenez-Borreguero,L.J.,
            Aragones,J., Ruiz-Cabello,J., Torres,M. and Martin-Puig,S.
  TITLE     Myocardial VHL-HIF Signaling Controls an Embryonic Metabolic Switch
            Essential for Cardiac Maturation
  JOURNAL   Dev Cell 39 (6), 724-739 (2016)
   PUBMED   27997827
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Cui,W., Dai,X., Marcho,C., Han,Z., Zhang,K., Tremblay,K.D. and
            Mager,J.
  TITLE     Towards Functional Annotation of the Preimplantation Transcriptome:
            An RNAi Screen in Mammalian Embryos
  JOURNAL   Sci Rep 6, 37396 (2016)
   PUBMED   27869233
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Childress,P., Stayrook,K.R., Alvarez,M.B., Wang,Z., Shao,Y.,
            Hernandez-Buquer,S., Mack,J.K., Grese,Z.R., He,Y., Horan,D.,
            Pavalko,F.M., Warden,S.J., Robling,A.G., Yang,F.C., Allen,M.R.,
            Krishnan,V., Liu,Y. and Bidwell,J.P.
  TITLE     Genome-Wide Mapping and Interrogation of the Nmp4 Antianabolic Bone
            Axis
  JOURNAL   Mol Endocrinol 29 (9), 1269-1285 (2015)
   PUBMED   26244796
REFERENCE   5  (residues 1 to 228)
  AUTHORS   Dugast-Darzacq,C., Pirity,M., Blanck,J.K., Scherl,A. and
            Schreiber-Agus,N.
  TITLE     Mxi1-SRalpha: a novel Mxi1 isoform with enhanced transcriptional
            repression potential
  JOURNAL   Oncogene 23 (55), 8887-8899 (2004)
   PUBMED   15467743
  REMARK    GeneRIF: Mxi1-SRalpha is an isoform with enhanced transcriptional
            repression potential
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Hurlin,P.J., Queva,C., Koskinen,P.J., Steingrimsson,E., Ayer,D.E.,
            Copeland,N.G., Jenkins,N.A. and Eisenman,R.N.
  TITLE     Mad3 and Mad4: novel Max-interacting transcriptional repressors
            that suppress c-myc dependent transformation and are expressed
            during neural and epidermal differentiation
  JOURNAL   EMBO J 14 (22), 5646-5659 (1995)
   PUBMED   8521822
  REMARK    Erratum:[EMBO J. 1996 Apr 15;15(8):2030. PMID: 8617250]
REFERENCE   7  (residues 1 to 228)
  AUTHORS   Steingrimsson,E., Sawadogo,M., Gilbert,D.J., Zervos,A.S., Brent,R.,
            Blanar,M.A., Fisher,D.E., Copeland,N.G. and Jenkins,N.A.
  TITLE     Murine chromosomal location of five bHLH-Zip transcription factor
            genes
  JOURNAL   Genomics 28 (2), 179-183 (1995)
   PUBMED   8530024
REFERENCE   8  (residues 1 to 228)
  AUTHORS   Schreiber-Agus,N., Chin,L., Chen,K., Torres,R., Rao,G., Guida,P.,
            Skoultchi,A.I. and DePinho,R.A.
  TITLE     An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic
            activity and interacts with a homolog of the yeast transcriptional
            repressor SIN3
  JOURNAL   Cell 80 (5), 777-786 (1995)
   PUBMED   7889571
REFERENCE   9  (residues 1 to 228)
  AUTHORS   Shimizu,E., Shirasawa,H., Kodama,K., Koseki,K., Sato,T. and
            Simizu,B.
  TITLE     Cloning and sequencing of the murine Mxi1 cDNA
  JOURNAL   Gene 152 (2), 283-284 (1995)
   PUBMED   7835718
REFERENCE   10 (residues 1 to 228)
  AUTHORS   Edelhoff,S., Ayer,D.E., Zervos,A.S., Steingrimsson,E.,
            Jenkins,N.A., Copeland,N.G., Eisenman,R.N., Brent,R. and
            Disteche,C.M.
  TITLE     Mapping of two genes encoding members of a distinct subfamily of
            MAX interacting proteins: MAD to human chromosome 2 and mouse
            chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome
            19
  JOURNAL   Oncogene 9 (2), 665-668 (1994)
   PUBMED   8290278
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CJ170779.1, AK140465.1 and
            AC133451.14.
            
            Summary: This gene encodes a protein containing a helix-loop-helix
            domain characteristic of transcription factors, which allows
            heterodimerization and sequence-specific DNA binding. The encoded
            protein is related to a family of Myc/Max/Mad proteins that are
            involved in the regulation of several cellular processes. The
            protein encoded by this gene is a transcriptional repressor thought
            to negatively regulate Myc function. Three alternatively spliced
            transcripts encoding different isoforms have been described.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1), also referred to as SRbeta,
            encodes the predominant isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK140465.1, U24674.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 47.53 cM"
     Protein         1..228
                     /product="max-interacting protein 1 isoform a"
                     /note="max-interacting protein 1"
                     /calculated_mol_wt=25847
     Region          30..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50540.1)"
     Region          68..147
                     /region_name="bHLHzip_MXI1"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in Max-interacting protein 1 (MXI1) and similar
                     proteins; cd18930"
                     /db_xref="CDD:381500"
     Site            order(72..73,76..77,79..80,84,103..105)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381500"
     Site            order(83..84,86..91,93..94,106,109,113,115..117,119..120,
                     122..123,126,130,133..134,136..137,140..141,143..144)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381500"
     Site            order(83,86..87,89..90,93..94,106,109,113,115..117,
                     119..120,122..123,126,130,133..134,136..137,140..141,
                     143..144)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381500"
     Region          160..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50540.1)"
     CDS             1..228
                     /gene="Mxi1"
                     /gene_synonym="bHLHc11; Gm10197; Mad2"
                     /coded_by="NM_010847.4:236..922"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS29901.1"
                     /db_xref="GeneID:17859"
                     /db_xref="MGI:MGI:97245"
ORIGIN      
        1 mervrminvq rlleaaefle rrerecehgy assfpsmpsp rlqhskpprr lsraqkhssg
       61 ssntstanrs thneleknrr ahlrlclerl kvliplgpdc trhttlglln kakahikkle
      121 eaerksqhql enlereqrfl krrleqlqgp qemerirmds igstissdrs dsereeievd
      181 vestefshge adsvsttsis dlddhsslqs vgsdegyssa svklsfas
//
LOCUS       NP_001275914            1621 aa            linear   PRI 27-APR-2025
DEFINITION  ABC-type organic anion transporter ABCA8 isoform 1 [Homo sapiens].
ACCESSION   NP_001275914 XP_005256996
VERSION     NP_001275914.1
DBSOURCE    REFSEQ: accession NM_001288985.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1621)
  AUTHORS   Yang,K., Li,X., Jiang,Z., Li,J., Deng,Q., He,J., Chen,J., Li,X.,
            Xu,S. and Jiang,Z.
  TITLE     Tumour suppressor ABCA8 inhibits malignant progression of
            colorectal cancer via Wnt/beta-catenin pathway
  JOURNAL   Dig Liver Dis 56 (5), 880-893 (2024)
   PUBMED   37968146
  REMARK    GeneRIF: Tumour suppressor ABCA8 inhibits malignant progression of
            colorectal cancer via Wnt/beta-catenin pathway.
REFERENCE   2  (residues 1 to 1621)
  AUTHORS   Lv,C., Yang,H., Yu,J. and Dai,X.
  TITLE     ABCA8 inhibits breast cancer cell proliferation by regulating the
            AMP activated protein kinase/mammalian target of rapamycin
            signaling pathway
  JOURNAL   Environ Toxicol 37 (6), 1423-1431 (2022)
   PUBMED   35191604
  REMARK    GeneRIF: ABCA8 inhibits breast cancer cell proliferation by
            regulating the AMP activated protein kinase/mammalian target of
            rapamycin signaling pathway.
REFERENCE   3  (residues 1 to 1621)
  AUTHORS   Guo,Y., Wang,Z.W., Su,W.H., Chen,J. and Wang,Y.L.
  TITLE     Prognostic Value and Immune Infiltrates of ABCA8 and FABP4 in
            Stomach Adenocarcinoma
  JOURNAL   Biomed Res Int 2020, 4145164 (2020)
   PUBMED   32685482
  REMARK    GeneRIF: Prognostic Value and Immune Infiltrates of ABCA8 and FABP4
            in Stomach Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1621)
  AUTHORS   Cui,Y., Liang,S., Zhang,S., Zhang,C., Zhao,Y., Wu,D., Wang,J.,
            Song,R., Wang,J., Yin,D., Liu,Y., Pan,S., Liu,X., Wang,Y., Han,J.,
            Meng,F., Zhang,B., Guo,H., Lu,Z. and Liu,L.
  TITLE     ABCA8 is regulated by miR-374b-5p and inhibits proliferation and
            metastasis of hepatocellular carcinoma through the ERK/ZEB1 pathway
  JOURNAL   J Exp Clin Cancer Res 39 (1), 90 (2020)
   PUBMED   32430024
  REMARK    GeneRIF: ABCA8 is regulated by miR-374b-5p and inhibits
            proliferation and metastasis of hepatocellular carcinoma through
            the ERK/ZEB1 pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1621)
  AUTHORS   Sasaki,K., Tachikawa,M., Uchida,Y., Hirano,S., Kadowaki,F.,
            Watanabe,M., Ohtsuki,S. and Terasaki,T.
  TITLE     ATP-Binding Cassette Transporter A Subfamily 8 Is a Sinusoidal
            Efflux Transporter for Cholesterol and Taurocholate in Mouse and
            Human Liver
  JOURNAL   Mol Pharm 15 (2), 343-355 (2018)
   PUBMED   29300488
  REMARK    GeneRIF: Study results suggest that mABCA8b/ABCA8 functions as a
            sinusoidal efflux transporter for at least cholesterol and
            taurocholate in mouse and human liver.
REFERENCE   6  (residues 1 to 1621)
  AUTHORS   Kim,W.S., Weickert,C.S. and Garner,B.
  TITLE     Role of ATP-binding cassette transporters in brain lipid transport
            and neurological disease
  JOURNAL   J Neurochem 104 (5), 1145-1166 (2008)
   PUBMED   17973979
  REMARK    Review article
REFERENCE   7  (residues 1 to 1621)
  AUTHORS   Kim,W.S., Guillemin,G.J., Glaros,E.N., Lim,C.K. and Garner,B.
  TITLE     Quantitation of ATP-binding cassette subfamily-A transporter gene
            expression in primary human brain cells
  JOURNAL   Neuroreport 17 (9), 891-896 (2006)
   PUBMED   16738483
REFERENCE   8  (residues 1 to 1621)
  AUTHORS   Tsuruoka,S., Ishibashi,K., Yamamoto,H., Wakaumi,M., Suzuki,M.,
            Schwartz,G.J., Imai,M. and Fujimura,A.
  TITLE     Functional analysis of ABCA8, a new drug transporter
  JOURNAL   Biochem Biophys Res Commun 298 (1), 41-45 (2002)
   PUBMED   12379217
  REMARK    GeneRIF: Functional analysis of the transport properties of ABCA8.
REFERENCE   9  (residues 1 to 1621)
  AUTHORS   Iida,A., Saito,S., Sekine,A., Mishima,C., Kitamura,Y., Kondo,K.,
            Harigae,S., Osawa,S. and Nakamura,Y.
  TITLE     Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13
            genes encoding human ATP-binding cassette transporters: ABCA4,
            ABCA7, ABCA8, ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2,
            ABCG4, ABCG5, and ABCG8
  JOURNAL   J Hum Genet 47 (6), 285-310 (2002)
   PUBMED   12111378
REFERENCE   10 (residues 1 to 1621)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC024003.1, BC130280.1,
            AB020629.1, AC015844.12 and AW590229.1.
            
            On Jan 9, 2014 this sequence version replaced XP_005256996.1.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intracellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White). This protein is a member of the ABC1 subfamily. Members of
            the ABC1 subfamily comprise the only major ABC subfamily found
            exclusively in multicellular eukaryotes. The encoded protein may
            regulate lipid metabolism and be involved in the formation and
            maintenance of myelin. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.231196.1,
                                           SRR1660807.261621.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000586539.6/ ENSP00000467271.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1621
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..1621
                     /product="ABC-type organic anion transporter ABCA8 isoform
                     1"
                     /note="ATP-binding cassette, sub-family A (ABC1), member
                     8; ABC-type organic anion transporter ABCA8"
                     /calculated_mol_wt=183546
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            220..240
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Region          <235..>790
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            243
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            268..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            299..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            359..379
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            397..417
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Region          480..703
                     /region_name="ABC_subfamily_A"
                     /note="ATP-binding cassette domain of the lipid
                     transporters, subfamily A; cd03263"
                     /db_xref="CDD:213230"
     Site            484
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            516..523
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213230"
     Site            order(519..520,522..524,565,641..642,673)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:213230"
     Site            555
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            562..565
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213230"
     Site            616
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            617..626
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213230"
     Site            637..642
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213230"
     Site            645..648
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213230"
     Site            669..675
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213230"
     Site            724
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            797
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            864..884
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            919
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            948
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            967
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            1019..1039
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Region          <1033..1598
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            1070..1090
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            1106..1126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            1136..1156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            1161..1181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            1197..1217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94911.4)"
     Site            1270
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Region          1285..1506
                     /region_name="ABC_subfamily_A"
                     /note="ATP-binding cassette domain of the lipid
                     transporters, subfamily A; cd03263"
                     /db_xref="CDD:213230"
     Site            1308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            1323..1330
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213230"
     Site            order(1326..1327,1329..1331,1366,1442..1443,1476)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:213230"
     Site            1363..1366
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213230"
     Site            1373
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            1418..1427
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213230"
     Site            1435
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94911.4)"
     Site            1438..1443
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213230"
     Site            1446..1449
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213230"
     Site            1472..1478
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213230"
     CDS             1..1621
                     /gene="ABCA8"
                     /coded_by="NM_001288985.2:341..5206"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS74139.1"
                     /db_xref="GeneID:10351"
                     /db_xref="HGNC:HGNC:38"
                     /db_xref="MIM:612505"
ORIGIN      
        1 mrkrkisvcq qtwallcknf lkkwrmkres lmewlnslll llclyiyphs hqvndfssll
       61 tmdlgrvdtf nesrfsvvyt pvtnttqqim nkvastpfla gkevlglpde esikeftany
      121 peeivrvtft ntysyhlkfl lghgmpakke hkdhtahcye tnedvycevs vfwkegfval
      181 qaainaaiie ittnhsvmee lmsvtgknmk mhsfigqsgv itdlylfsci isfssfiyya
      241 svnvtrerkr mkalmtmmgl rdsafwlswg llyagfifim alflalvirs tqfiilsgfm
      301 vvfslfllyg lslvalaflm silvkksflt glvvflltvf wgclgftsly rhlpaslewi
      361 lsllspfafm lgmaqllhld ydlnsnafph psdgsnliva tnfmlafdtc lylalaiyfe
      421 kilpneyghr rpplfflkss fwsqtqktdh valedemdad psfhdsfeqa ppefqgkeai
      481 rirnvtkeyk gkpdkiealk dlvfdiyegq itailghsga gkstllnils glsvptkgsv
      541 tiynnklsem adlenlsklt gvcpqsnvqf dfltvrenlr lfakikgilp qevdkeiqrv
      601 llelemkniq dvlaqnlsgg qkrkltfgia ilgdpqifll deptagldpf srhqvwnllk
      661 erktdrvilf stqfmdeadi ladrkvflsq gklkcagssl flkkkwgigy hlslqlneic
      721 veenitslvk qhipdaklsa ksegkliytl plertnkfpe lykdldsypd lgienygvsm
      781 ttlnevflkl egkstinesd iailgevqae kaddterlve meqvlsslnk mrktiggval
      841 wrqqicaiar vrllklkher kallalllil magfcpllve ytmvkiyqns ytwelsphly
      901 flapgqqphd pltqlliink tgasiddfiq svehqniale vdafgtrngt ddpsyngait
      961 vccneknysf slacnakrln cfpvlmdivs ngllgmvkps vhirterstf lengqdnpig
     1021 flayimfwlv ltsscppyia mssiddyknr arsqlrisgl spsaywfgqa lvdvslyflv
     1081 fvfiylmsyi snfedmllti ihiiqipcav gysfslifmt yvisfifrkg rknsgiwsfc
     1141 fyvvtvfsva gfafsifesd ipfiftflip patmigclfl sshllfsslf seermdvqpf
     1201 lvflipflhf iiflftlrcl ewkfgkksmr kdpffrispr ssdvcqnpee pegededvqm
     1261 ervrtanaln stnfdekpvi iasclrkeya gkrkgcfskr knkiatrnvs fcvrkgevlg
     1321 llghngagks tsikvitgdt kptagqvllk gsgggdalef lgycpqenal wpnltvrqhl
     1381 evyaavkglr kgdaevaitr lvdalklqdq lkspvktlse gikrklcfvl silgnpsvvl
     1441 ldepstgmdp egqqqmwqai ratfrnterg alltthymae aeavcdrvai mvsgrlrcig
     1501 siqhlkskfg kdyllemkvk nlaqveplha eilrlfpqaa rqerysslmv yklpvedvqp
     1561 laqaffklek vkqsfdleey slsqstleqv flelskeqel gdfeedfdps vkwkllpqee
     1621 p
//
LOCUS       NP_001348947             789 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 4 [Mus musculus].
ACCESSION   NP_001348947
VERSION     NP_001348947.1
DBSOURCE    REFSEQ: accession NM_001362018.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 789)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 789)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 789)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 789)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 789)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 789)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 789)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 789)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            Transcript Variant: This variant (28), as well as variants 4, 26,
            and 27, encodes isoform 4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164131
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..789
                     /product="cAMP-regulated phosphoprotein 21 isoform 4"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=85487
     Region          162..223
                     /region_name="R3H_encore_like"
                     /note="R3H domain of encore-like and DIP1-like proteins.
                     Drosophila encore is involved in the germline exit after
                     four mitotic divisions, by facilitating
                     SCF-ubiquitin-proteasome-dependent proteolysis. Maize
                     DBF1-interactor protein 1 (DIP1) containing an R3H...;
                     cd02642"
                     /db_xref="CDD:100071"
     Site            order(195,199)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100071"
     Region          535..>764
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..789
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362018.1:474..2843"
                     /note="isoform 4 is encoded by transcript variant 28"
                     /db_xref="CCDS:CCDS52944.1"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqesih lqlssfpslq eedksrkdds erekekdknr
      121 eklserpkir mlskdcsqey tdstgidlhg flintlknns rdrmillkme qemidfiads
      181 nnhykkfpqm ssyqrmlvhr vaayfgldhn vdqtgksvii nktsstripe qrfcehlkde
      241 kseesqkrfi lkrdnssidk ednqsvcsqe slfldnrahr dssgrtsgsr qsssetelrw
      301 pdhqrawsst dsdssnrnlk ptmtktasfg gitvltrgds tsstrsagkl sktgsessss
      361 agssgslsrt hpqstaltss vaagspgcma ysengmggqv ppsstsyill plesatgipp
      421 gsillnphtg qpfvnpdgtp aiynppgsqq tlrgtvggqp qqppqqqpsp qpqqqvqasq
      481 pqmagplvtq svqslqpssq svqypavsfp pqhllpmspt qhfplreela aqfsqlsmsr
      541 qssgdtpepp sgtvypasll pqtaqpqsyv itsagqqlst ggfsdsgppi sqqvlqapps
      601 pqgfvqqppp aqmsvyyyps gqyptstsqq yrplasvqys aqrsqqipqt tqqagyqpvl
      661 sgqqgfqgmm gvqqsahsqg vmssqqgapv hgvmvsyptm ssyqvpmtqg sqavpqqtyq
      721 ppimlpsqag qgslpatgmp vycnvtppnp qnnlrlmgph cpsstvpvms ascrtncgnv
      781 snagwqvkf
//
LOCUS       NP_001355925             342 aa            linear   PRI 27-APR-2025
DEFINITION  aprataxin isoform a [Homo sapiens].
ACCESSION   NP_001355925 XP_024303345
VERSION     NP_001355925.1
DBSOURCE    REFSEQ: accession NM_001368996.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_024303345.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.103016.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..342
                     /product="aprataxin isoform a"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=38973
     Region          3..102
                     /region_name="FHA_APTX"
                     /note="forkhead associated (FHA) domain found in aprataxin
                     and similar proteins; cd22735"
                     /db_xref="CDD:438787"
     Site            order(29..31,34..36,38..42,63..65,91)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438787"
     Region          164..265
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(258,260,262..264)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            260
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          283..342
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..342
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001368996.1:103..1131"
                     /note="isoform a is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS47956.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqvqlkae cnkgyvkvkq
       61 vgvnptsids vvigkdqevk lqpgqvlhmv nelypyivef eeeaknpgle thrkrkrsgn
      121 sdsierdaaq eaeagtglep gsnsgqcsvp lkkgkdapik keslghwsqg lkismqdpkm
      181 qvykdeqvvv ikdkypkary hwlvlpwtsi sslkavareh lellkhmhtv gekvivdfag
      241 ssklrfrlgy haipsmshvh lhvisqdfds pclknkkhwn sfnteyfles qaviemvqea
      301 grvtvrdgmp ellklplrch ecqqllpsip qlkehlrkhw tq
//
LOCUS       NP_631900                120 aa            linear   PRI 27-APR-2025
DEFINITION  protein crumbs homolog 3 isoform a precursor [Homo sapiens].
ACCESSION   NP_631900
VERSION     NP_631900.1
DBSOURCE    REFSEQ: accession NM_139161.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Wang,Z., Wang,X., Liu,L., Guo,X., Zhang,H., Yin,J., Lin,R., Shao,Y.
            and Cai,D.
  TITLE     Fructose-bisphosphatase1 (FBP1) alleviates experimental
            osteoarthritis by regulating Protein crumbs homolog 3 (CRB3)
  JOURNAL   Arthritis Res Ther 25 (1), 235 (2023)
   PUBMED   38049890
  REMARK    GeneRIF: Fructose-bisphosphatase1 (FBP1) alleviates experimental
            osteoarthritis by regulating Protein crumbs homolog 3 (CRB3).
            Erratum:[Arthritis Res Ther. 2023 Dec 28;25(1):250. doi:
            10.1186/s13075-023-03247-9. PMID: 38155346]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Tilston-Lunel,A., Mazzilli,S., Kingston,N.M., Szymaniak,A.D.,
            Hicks-Berthet,J., Kern,J.G., Abo,K., Reid,M.E., Perdomo,C.,
            Wilson,A.A., Spira,A., Beane,J. and Varelas,X.
  TITLE     Aberrant epithelial polarity cues drive the development of
            precancerous airway lesions
  JOURNAL   Proc Natl Acad Sci U S A 118 (18) (2021)
   PUBMED   33903236
  REMARK    GeneRIF: Aberrant epithelial polarity cues drive the development of
            precancerous airway lesions.
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Iioka,H., Saito,K. and Kondo,E.
  TITLE     Crumbs3 regulates the expression of glycosphingolipids on the
            plasma membrane to promote colon cancer cell migration
  JOURNAL   Biochem Biophys Res Commun 519 (2), 287-293 (2019)
   PUBMED   31500807
  REMARK    GeneRIF: The Crb3 may promote colon cancer cell migration by
            regulating the expression of GSLs on the cell surface.
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Madigan,V.J., Tyson,T.O., Yuziuk,J.A., Pillai,M., Moller-Tank,S.
            and Asokan,A.
  TITLE     A CRISPR Screen Identifies the Cell Polarity Determinant Crumbs 3
            as an Adeno-associated Virus Restriction Factor in Hepatocytes
  JOURNAL   J Virol 93 (21), e00943-19 (2019)
   PUBMED   31391273
  REMARK    GeneRIF: Knockout (KO) of apical polarity determinant Crumbs 3
            (Crb3) enhances Adeno-associated viruses (AAV) transduction, while
            overexpression exerts the opposite effect. Crb3 restricts AAV
            transduction in a serotype- and cell type-specific manner.
            Increased availability of galactosylated glycans on the surfaces of
            Crb3 KO cells, but not the universal AAV receptor, leads to
            increased capsid attachment and enhanced transduction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Fogg,V.C., Liu,C.J. and Margolis,B.
  TITLE     Multiple regions of Crumbs3 are required for tight junction
            formation in MCF10A cells
  JOURNAL   J Cell Sci 118 (Pt 13), 2859-2869 (2005)
   PUBMED   15976445
  REMARK    GeneRIF: The crumbs3 protein plays an important role in epithelial
            tight junction formation, and also provide the first known
            functional role for the mammalian Crumbs FERM binding domain.
REFERENCE   7  (residues 1 to 120)
  AUTHORS   Lemmers,C., Michel,D., Lane-Guermonprez,L., Delgrossi,M.H.,
            Medina,E., Arsanto,J.P. and Le Bivic,A.
  TITLE     CRB3 binds directly to Par6 and regulates the morphogenesis of the
            tight junctions in mammalian epithelial cells
  JOURNAL   Mol Biol Cell 15 (3), 1324-1333 (2004)
   PUBMED   14718572
  REMARK    GeneRIF: CRB3, through its cytoplasmic domain and its interactors,
            plays a role in apical membrane morphogenesis and tight junction
            regulation.
REFERENCE   8  (residues 1 to 120)
  AUTHORS   Roh,M.H., Fan,S., Liu,C.J. and Margolis,B.
  TITLE     The Crumbs3-Pals1 complex participates in the establishment of
            polarity in mammalian epithelial cells
  JOURNAL   J Cell Sci 116 (Pt 14), 2895-2906 (2003)
   PUBMED   12771187
  REMARK    GeneRIF: the Crumbs3-Pals1 complex has a role in development of
            polarity in mammalian epithelial cells
REFERENCE   9  (residues 1 to 120)
  AUTHORS   Makarova,O., Roh,M.H., Liu,C.J., Laurinec,S. and Margolis,B.
  TITLE     Mammalian Crumbs3 is a small transmembrane protein linked to
            protein associated with Lin-7 (Pals1)
  JOURNAL   Gene 302 (1-2), 21-29 (2003)
   PUBMED   12527193
REFERENCE   10 (residues 1 to 120)
  AUTHORS   Lemmers,C., Medina,E., Delgrossi,M.H., Michel,D., Arsanto,J.P. and
            Le Bivic,A.
  TITLE     hINADl/PATJ, a homolog of discs lost, interacts with crumbs and
            localizes to tight junctions in human epithelial cells
  JOURNAL   J Biol Chem 277 (28), 25408-25415 (2002)
   PUBMED   11964389
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB215367.1, AF503290.1 and
            BC002652.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the Crumbs family of
            proteins. This gene is widely expressed in epithelial tissues where
            the encoded protein isoforms play various roles such as the control
            of cytokinesis and ciliogenesis or the formation of tight
            junctions. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Mar
            2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF503290.1, AK292956.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000600229.6/ ENSP00000472010.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..120
                     /product="protein crumbs homolog 3 isoform a precursor"
                     /note="crumbs family member 3; protein crumbs homolog 3;
                     crumbs 3, cell polarity complex component"
                     /calculated_mol_wt=10108
     sig_peptide     1..26
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BUF7.3)"
                     /calculated_mol_wt=2764
     mat_peptide     27..120
                     /product="Protein crumbs homolog 3. /id=PRO_0000021005"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUF7.3)"
                     /calculated_mol_wt=10108
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12527193; propagated from
                     UniProtKB/Swiss-Prot (Q9BUF7.3)"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUF7.3)"
     Region          84..120
                     /region_name="Interaction with EPB41L5.
                     /evidence=ECO:0000269|PubMed:17920587"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUF7.3)"
     Region          87..120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUF7.3)"
     Region          117..120
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUF7.3)"
     CDS             1..120
                     /gene="CRB3"
                     /coded_by="NM_139161.5:175..537"
                     /note="isoform a precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS12167.1"
                     /db_xref="GeneID:92359"
                     /db_xref="HGNC:HGNC:20237"
                     /db_xref="MIM:609737"
ORIGIN      
        1 manpglglll alglpfllar wgrawgqiqt tsanenstvl psstssssdg nlrpeaitai
       61 ivvfsllaal llavglallv rklrekrqte gtyrpsseeq vgarvpptpn lklppeerli
//
LOCUS       NP_066969                346 aa            linear   PRI 27-APR-2025
DEFINITION  angiopoietin-related protein 7 precursor [Homo sapiens].
ACCESSION   NP_066969
VERSION     NP_066969.1
DBSOURCE    REFSEQ: accession NM_021146.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Brown,S.F., Nguyen,H., Mzyk,P., De Ieso,M.L., Unser,A.M., Brown,I.,
            Ramesh,P., Afzaal,H., Ahmed,F., Torrejon,K.Y., Nhan,A.,
            Markrush,D., Daly,T., Knecht,E., McConaughy,W., Halmos,S.,
            Liu,Z.L., Rennard,R., Peterson,A. and Stamer,W.D.
  TITLE     ANGPTL7 and Its Role in IOP and Glaucoma
  JOURNAL   Invest Ophthalmol Vis Sci 65 (3), 22 (2024)
   PUBMED   38497513
  REMARK    GeneRIF: ANGPTL7 and Its Role in IOP and Glaucoma.
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Fei,M.Y., Wang,Y., Chang,B.H., Xue,K., Dong,F., Huang,D., Li,X.Y.,
            Li,Z.J., Hu,C.L., Liu,P., Wu,J.C., Yu,P.C., Hong,M.H., Chen,S.B.,
            Xu,C.H., Chen,B.Y., Jiang,Y.L., Liu,N., Zhao,C., Jin,J.C., Hou,D.,
            Chen,X.C., Ren,Y.Y., Deng,C.H., Zhang,J.Y., Zong,L.J., Wang,R.J.,
            Gao,F.F., Liu,H., Zhang,Q.L., Wu,L.Y., Yan,J., Shen,S., Chang,C.K.,
            Sun,X.J. and Wang,L.
  TITLE     The non-cell-autonomous function of ID1 promotes AML progression
            via ANGPTL7 from the microenvironment
  JOURNAL   Blood 142 (10), 903-917 (2023)
   PUBMED   37319434
  REMARK    GeneRIF: The non-cell-autonomous function of ID1 promotes AML
            progression via ANGPTL7 from the microenvironment.
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Aboobakar,I.F., Collantes,E.R.A., Hauser,M.A., Stamer,W.D. and
            Wiggs,J.L.
  TITLE     Rare protective variants and glaucoma-relevant cell stressors
            modulate Angiopoietin-like 7 expression
  JOURNAL   Hum Mol Genet 32 (15), 2523-2531 (2023)
   PUBMED   37220876
  REMARK    GeneRIF: Rare protective variants and glaucoma-relevant cell
            stressors modulate Angiopoietin-like 7 expression.
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Yamamoto,A., Huang,Y., Krajina,B.A., McBirney,M., Doak,A.E., Qu,S.,
            Wang,C.L., Haffner,M.C. and Cheung,K.J.
  TITLE     Metastasis from the tumor interior and necrotic core formation are
            regulated by breast cancer-derived angiopoietin-like 7
  JOURNAL   Proc Natl Acad Sci U S A 120 (10), e2214888120 (2023)
   PUBMED   36853945
  REMARK    GeneRIF: Metastasis from the tumor interior and necrotic core
            formation are regulated by breast cancer-derived angiopoietin-like
            7.
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Praveen,K., Patel,G.C., Gurski,L., Ayer,A.H., Persaud,T.,
            Still,M.D., Miloscio,L., Van Zyl,T., Di Gioia,S.A., Brumpton,B.,
            Krebs,K., Asvold,B.O., Chen,E., Chavali,V.R.M., Fury,W.,
            Gudiseva,H.V., Hyde,S., Jorgenson,E., Lefebvre,S., Li,D., Li,A.,
            Mclninch,J., Patel,B., Rabinowitz,J.S., Salowe,R., Schurmann,C.,
            Seidelin,A.S., Stahl,E., Sun,D., Teslovich,T.M.,
            Tybjaerg-Hansen,A., Willer,C., Waldron,S., Walley,S., Yang,H.,
            Zaveri,S., Hu,Y., Hveem,K., Melander,O., Milani,L., Stender,S.,
            O'Brien,J.M., Jones,M.B., Abecasis,G.R., Cantor,M.N., Weyne,J.,
            Karalis,K., Economides,A., Della Gatta,G., Ferreira,M.A.,
            Yancopoulos,G.D., Baras,A., Romano,C. and Coppola,G.
  CONSRTM   Regeneron Genetics Center; GHS-RGC DiscovEHR Collaboration;
            Estonian Biobank Research Team
  TITLE     ANGPTL7, a therapeutic target for increased intraocular pressure
            and glaucoma
  JOURNAL   Commun Biol 5 (1), 1051 (2022)
   PUBMED   36192519
  REMARK    GeneRIF: ANGPTL7, a therapeutic target for increased intraocular
            pressure and glaucoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Peek,R., Kammerer,R.A., Frank,S., Otte-Holler,I. and Westphal,J.R.
  TITLE     The angiopoietin-like factor cornea-derived transcript 6 is a
            putative morphogen for human cornea
  JOURNAL   J Biol Chem 277 (1), 686-693 (2002)
   PUBMED   11682471
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Stover,C., Endo,Y., Takahashi,M., Lynch,N.J., Constantinescu,C.,
            Vorup-Jensen,T., Thiel,S., Friedl,H., Hankeln,T., Hall,R.,
            Gregory,S., Fujita,T. and Schwaeble,W.
  TITLE     The human gene for mannan-binding lectin-associated serine
            protease-2 (MASP-2), the effector component of the lectin route of
            complement activation, is part of a tightly linked gene cluster on
            chromosome 1p36.2-3
  JOURNAL   Genes Immun 2 (3), 119-127 (2001)
   PUBMED   11426320
REFERENCE   8  (residues 1 to 346)
  AUTHORS   Peek,R., van Gelderen,B.E., Bruinenberg,M. and Kijlstra,A.
  TITLE     Molecular cloning of a new angiopoietinlike factor from the human
            cornea
  JOURNAL   Invest Ophthalmol Vis Sci 39 (10), 1782-1788 (1998)
   PUBMED   9727400
REFERENCE   9  (residues 1 to 346)
  AUTHORS   Lim,Y.S., Cha,M.K., Kim,H.K. and Kim,I.H.
  TITLE     The thiol-specific antioxidant protein from human brain: gene
            cloning and analysis of conserved cysteine regions
  JOURNAL   Gene 140 (2), 279-284 (1994)
   PUBMED   8144038
REFERENCE   10 (residues 1 to 346)
  AUTHORS   Shau,H., Butterfield,L.H., Chiu,R. and Kim,A.
  TITLE     Cloning and sequence analysis of candidate human natural
            killer-enhancing factor genes
  JOURNAL   Immunogenetics 40 (2), 129-134 (1994)
   PUBMED   8026862
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC001881.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001881.1, AY358301.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376819.4/ ENSP00000366015.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..346
                     /product="angiopoietin-related protein 7 precursor"
                     /note="angiopoietin-related protein 7; angiopoietin-like
                     factor (CDT6); angiopoietin-like protein 7; cornea-derived
                     transcript 6 protein"
                     /calculated_mol_wt=37065
     sig_peptide     1..26
                     /note="/evidence=ECO:0000269|PubMed:15340161; propagated
                     from UniProtKB/Swiss-Prot (O43827.1)"
                     /calculated_mol_wt=2972
     mat_peptide     27..346
                     /product="Angiopoietin-related protein 7.
                     /id=PRO_0000009131"
                     /note="propagated from UniProtKB/Swiss-Prot (O43827.1)"
                     /calculated_mol_wt=37065
     Region          <37..>109
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43827.1)"
     Region          129..341
                     /region_name="FReD"
                     /note="Fibrinogen-related domains (FReDs); C terminal
                     globular domain of fibrinogen. Fibrinogen is involved in
                     blood clotting, being activated by thrombin to assemble
                     into fibrin clots. The N-termini of 2 times 3 chains come
                     together to form a globular...; cd00087"
                     /db_xref="CDD:238040"
     Site            248
                     /site_type="other"
                     /note="gamma-gamma dimer interface [polypeptide binding]"
                     /db_xref="CDD:238040"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43827.1)"
     Site            267
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43827.1)"
     Site            order(277,279,281)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238040"
     Site            order(285,288..289,298..299)
                     /site_type="active"
                     /note="polymerization pocket [active]"
                     /db_xref="CDD:238040"
     CDS             1..346
                     /gene="ANGPTL7"
                     /gene_synonym="AngX; CDT6; dJ647M16.1"
                     /coded_by="NM_021146.4:226..1266"
                     /db_xref="CCDS:CCDS128.1"
                     /db_xref="GeneID:10218"
                     /db_xref="HGNC:HGNC:24078"
                     /db_xref="MIM:618517"
ORIGIN      
        1 mlkkplsavt wlcifivafv shpawlqkls khktpaqpql kaancceevk elkaqvanls
       61 sllselnkkq erdwvsvvmq vmelesnskr mesrltdaes kysemnnqid imqlqaaqtv
      121 tqtsadaiyd csslyqknyr isgvyklppd dflgspelev fcdmetsggg wtiiqrrksg
      181 lvsfyrdwkq ykqgfgsirg dfwlgnehih rlsrqptrlr vemedwegnl ryaeyshfvl
      241 gnelnsyrlf lgnytgnvgn dalqyhnnta fstkdkdndn cldkcaqlrk ggywyncctd
      301 snlngvyyrl gehnkhldgi twygwhgsty slkrvemkir pedfkp
//
LOCUS       NP_001167543             461 aa            linear   PRI 27-APR-2025
DEFINITION  serine incorporator 5 isoform 1 [Homo sapiens].
ACCESSION   NP_001167543
VERSION     NP_001167543.1
DBSOURCE    REFSEQ: accession NM_001174072.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Raghunath,G., Abbott,E.H., Marin,M., Wu,H., Reyes Ballista,J.M.,
            Brindley,M.A. and Melikyan,G.B.
  TITLE     Disruption of Transmembrane Phosphatidylserine Asymmetry by HIV-1
            Incorporated SERINC5 Is Not Responsible for Virus Restriction
  JOURNAL   Biomolecules 14 (5), 570 (2024)
   PUBMED   38785977
  REMARK    GeneRIF: Disruption of Transmembrane Phosphatidylserine Asymmetry
            by HIV-1 Incorporated SERINC5 Is Not Responsible for Virus
            Restriction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Sid Ahmed,S., Bajak,K. and Fackler,O.T.
  TITLE     Beyond Impairment of Virion Infectivity: New Activities of the
            Anti-HIV Host Cell Factor SERINC5
  JOURNAL   Viruses 16 (2), 284 (2024)
   PUBMED   38400059
  REMARK    GeneRIF: Beyond Impairment of Virion Infectivity: New Activities of
            the Anti-HIV Host Cell Factor SERINC5.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Nkuwi,E., Judicate,G.P., Tan,T.S., Barabona,G., Toyoda,M.,
            Sunguya,B., Kamori,D. and Ueno,T.
  TITLE     Relative resistance of patient-derived envelope sequences to
            SERINC5-mediated restriction of HIV-1 infectivity
  JOURNAL   J Virol 97 (10), e0082323 (2023)
   PUBMED   37768085
  REMARK    GeneRIF: Relative resistance of patient-derived envelope sequences
            to SERINC5-mediated restriction of HIV-1 infectivity.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Leonhardt,S.A., Purdy,M.D., Grover,J.R., Yang,Z., Poulos,S.,
            McIntire,W.E., Tatham,E.A., Erramilli,S.K., Nosol,K., Lai,K.K.,
            Ding,S., Lu,M., Uchil,P.D., Finzi,A., Rein,A., Kossiakoff,A.A.,
            Mothes,W. and Yeager,M.
  TITLE     Antiviral HIV-1 SERINC restriction factors disrupt virus membrane
            asymmetry
  JOURNAL   Nat Commun 14 (1), 4368 (2023)
   PUBMED   37474505
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Ramdas,P. and Chande,A.
  TITLE     SERINC5 Mediates a Postintegration Block to HIV-1 Gene Expression
            in Macrophages
  JOURNAL   mBio 14 (2), e0016623 (2023)
   PUBMED   36976020
  REMARK    GeneRIF: SERINC5 Mediates a Postintegration Block to HIV-1 Gene
            Expression in Macrophages.
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Lubke,G.H., Laurin,C., Amin,N., Hottenga,J.J., Willemsen,G., van
            Grootheest,G., Abdellaoui,A., Karssen,L.C., Oostra,B.A., van
            Duijn,C.M., Penninx,B.W. and Boomsma,D.I.
  TITLE     Genome-wide analyses of borderline personality features
  JOURNAL   Mol Psychiatry 19 (8), 923-929 (2014)
   PUBMED   23979607
  REMARK    GeneRIF: results from a first genome-wide association study of
            Borderline personality disorder, which shows a promising signal on
            chromosome 5 corresponding to SERINC5, a protein involved in
            myelination.
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Szafranski,K., Schindler,S., Taudien,S., Hiller,M., Huse,K.,
            Jahn,N., Schreiber,S., Backofen,R. and Platzer,M.
  TITLE     Violating the splicing rules: TG dinucleotides function as
            alternative 3' splice sites in U2-dependent introns
  JOURNAL   Genome Biol 8 (8), R154 (2007)
   PUBMED   17672918
  REMARK    GeneRIF: the apparent occurrence of an unusual TG 3' splice site in
            intron 11 is discussed
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Uemura,T., Tachihara,K., Tomitori,H., Kashiwagi,K. and Igarashi,K.
  TITLE     Characteristics of the polyamine transporter TPO1 and regulation of
            its activity and cellular localization by phosphorylation
  JOURNAL   J Biol Chem 280 (10), 9646-9652 (2005)
   PUBMED   15637075
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Xu,J., Ji,C., Wang,L., Cao,Y., Dai,J., Ye,X., Zeng,L., Dai,J.,
            Wu,Q., Xie,Y. and Mao,Y.
  TITLE     Cloning and expression of a novel human C5orf12 gene*, a member of
            the TMS_TDE family
  JOURNAL   Mol Biol Rep 30 (1), 47-52 (2003)
   PUBMED   12688535
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010260.7, AK297467.1 and BU681476.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.42.1, SRR1803611.72085.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000507668.7/ ENSP00000426237.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..461
                     /product="serine incorporator 5 isoform 1"
                     /calculated_mol_wt=51204
     Region          11..457
                     /region_name="Serinc"
                     /note="Serine incorporator (Serinc); pfam03348"
                     /db_xref="CDD:460891"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE9.1)"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE9.1)"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86VE9.1)"
     Site            125..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE9.1)"
     Site            157..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE9.1)"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86VE9.1)"
     Site            199..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE9.1)"
     Site            231..251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE9.1)"
     Site            259..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE9.1)"
     Site            312..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE9.1)"
     Site            386..406
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VE9.1)"
     CDS             1..461
                     /gene="SERINC5"
                     /gene_synonym="C5orf12; TPO1"
                     /coded_by="NM_001174072.3:127..1512"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54874.1"
                     /db_xref="GeneID:256987"
                     /db_xref="HGNC:HGNC:18825"
                     /db_xref="MIM:614551"
ORIGIN      
        1 msaqccagql acccgsagcs lccdccprir qslstrfmya lyfilvvvlc cimmsttvah
       61 kmkehipffe dmckgikagd tceklvgysa vyrvcfgmac fffifclltl kinnskscra
      121 hihngfwffk llllgamcsg affipdqdtf lnawryvgav ggflfigiql lllvefahkw
      181 nknwtagtas nklwyaslal vtlimysiat gglvlmavfy tqkdscmenk illgvngglc
      241 llislvaisp wvqnrqphsg llqsgviscy vtyltfsals skpaevvlde hgknvticvp
      301 dfgqdlyrde nlvtilgtsl ligcilyscl tsttrsssda lqgryaapel eiarccfcfs
      361 pggedteeqq pgkegprviy dekkgtvyiy syfhfvffla slyvmmtvtn wfnyesanie
      421 sffsgswsif wvkmascwic vllylctlva plccptrefs v
//
LOCUS       NP_001138906             577 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 880 [Homo sapiens].
ACCESSION   NP_001138906
VERSION     NP_001138906.1
DBSOURCE    REFSEQ: accession NM_001145434.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Dong,X., Zhang,Y., Sun,Y., Nan,Q., Li,M., Ma,L., Zhang,L., Luo,J.,
            Qi,Y. and Miao,Y.
  TITLE     Promoter hypermethylation and comprehensive regulation of ncRNA
            lead to the down-regulation of ZNF880, providing a new insight for
            the therapeutics and research of colorectal cancer
  JOURNAL   BMC Med Genomics 16 (1), 148 (2023)
   PUBMED   37370088
  REMARK    GeneRIF: Promoter hypermethylation and comprehensive regulation of
            ncRNA lead to the down-regulation of ZNF880, providing a new
            insight for the therapeutics and research of colorectal cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Jia,L., Young,M.F., Powell,J., Yang,L., Ho,N.C., Hotchkiss,R.,
            Robey,P.G. and Francomano,C.A.
  TITLE     Gene expression profile of human bone marrow stromal cells:
            high-throughput expressed sequence tag sequencing analysis
  JOURNAL   Genomics 79 (1), 7-17 (2002)
   PUBMED   11827452
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC419753.1, AK297834.1, AF086165.1 and AI754748.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DC360343.1, SRR1803613.3357.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000422689.3/ ENSP00000406318.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..577
                     /product="zinc finger protein 880"
                     /note="zinc finger protein LOC400713"
                     /calculated_mol_wt=66631
     Region          7..65
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          186..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          208..542
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(219,221,223,225..226,229..230,233,247,249,253..254,
                     257..258,261,275,277,279,281..282,285..286,289)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(499,501,503,505..506,509..510,513,527,529,533..534,
                     537..538,541,555,557,559,561..562,565..566,569)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          534..559
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          550..570
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..577
                     /gene="ZNF880"
                     /coded_by="NM_001145434.2:44..1777"
                     /db_xref="CCDS:CCDS46164.1"
                     /db_xref="GeneID:400713"
                     /db_xref="HGNC:HGNC:37249"
ORIGIN      
        1 mlrrghlafr dvaiefpqee wkcldpaqrt lyrevmveny rnlvflgicl pdlsvismle
       61 qrrdprnlqs evkiannpgg recikgvnae sssklgsnag nkslknqlgl tfqlhlselq
      121 lfqaernisg ckhvekpinn slvsplqkiy ssvkshilnk yrndfddspf lpqeqkaqir
      181 ekpcecnehg kafrvssrla nnqvihtadn pykcnecdkv fsnssnlvqh qrihtgekpy
      241 kchecgklfn risllarhqr ihtgekpykc hecgkvftqn shlanhhrih tgekpykcne
      301 cgkvfnrnah larhqkihsg ekpykckecg kafsggsglt ahlvihtgek lykcnkcgkv
      361 fnrnahltrh qrihtgekpy eckecgkvfr hkfcltnhhr mhtgeqpykc necgkafrdc
      421 sgltahllih tgekpykcke cakvfrhrls lsnhqrfhtg ekpyrcdecg kdftrnsnla
      481 nhhrihtgek pykcsechkv fshnshlarh rqihtgeksy kcnecgkvfs hklylkkher
      541 ihtgekpyrc hecgkdftrn snlanhhrih tgekpyr
//
LOCUS       NP_006832                504 aa            linear   PRI 27-APR-2025
DEFINITION  sodium-coupled neutral amino acid transporter 3 [Homo sapiens].
ACCESSION   NP_006832
VERSION     NP_006832.1
DBSOURCE    REFSEQ: accession NM_006841.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Tan,Z., Boyapati,K., Tressler,C.M., Jenkinson,N.M. and Glunde,K.
  TITLE     Glutamine transporter SLC38A3 promotes breast cancer metastasis via
            Gsk3beta/beta-catenin/EMT pathway
  JOURNAL   Cancer Lett 586, 216653 (2024)
   PUBMED   38309615
  REMARK    GeneRIF: Glutamine transporter SLC38A3 promotes breast cancer
            metastasis via Gsk3beta/beta-catenin/EMT pathway.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Marafi,D., Fatih,J.M., Kaiyrzhanov,R., Ferla,M.P., Gijavanekar,C.,
            Al-Maraghi,A., Liu,N., Sites,E., Alsaif,H.S., Al-Owain,M.,
            Zakkariah,M., El-Anany,E., Guliyeva,U., Guliyeva,S., Gaba,C.,
            Haseeb,A., Alhashem,A.M., Danish,E., Karageorgou,V., Beetz,C.,
            Subhi,A.A., Mullegama,S.V., Torti,E., Sebastin,M., Breilyn,M.S.,
            Duberstein,S., Abdel-Hamid,M.S., Mitani,T., Du,H., Rosenfeld,J.A.,
            Jhangiani,S.N., Coban Akdemir,Z., Gibbs,R.A., Taylor,J.C.,
            Fakhro,K.A., Hunter,J.V., Pehlivan,D., Zaki,M.S., Gleeson,J.G.,
            Maroofian,R., Houlden,H., Posey,J.E., Sutton,V.R., Alkuraya,F.S.,
            Elsea,S.H. and Lupski,J.R.
  TITLE     Biallelic variants in SLC38A3 encoding a glutamine transporter
            cause epileptic encephalopathy
  JOURNAL   Brain 145 (3), 909-924 (2022)
   PUBMED   34605855
  REMARK    GeneRIF: Biallelic variants in SLC38A3 encoding a glutamine
            transporter cause epileptic encephalopathy.
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Sweeney,M.D., Zhao,Z., Montagne,A., Nelson,A.R. and Zlokovic,B.V.
  TITLE     Blood-Brain Barrier: From Physiology to Disease and Back
  JOURNAL   Physiol Rev 99 (1), 21-78 (2019)
   PUBMED   30280653
  REMARK    Review article
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Wang,Y., Fu,L., Cui,M., Wang,Y., Xu,Y., Li,M. and Mi,J.
  TITLE     Amino acid transporter SLC38A3 promotes metastasis of non-small
            cell lung cancer cells by activating PDK1
  JOURNAL   Cancer Lett 393, 8-15 (2017)
   PUBMED   28202352
  REMARK    GeneRIF: SLC38A3 activated PDK1/AKT signaling and promoted
            metastasis of non-small cell lung cancer cells through regulating
            glutamine and histidine transport.
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Zhao,Z., Nelson,A.R., Betsholtz,C. and Zlokovic,B.V.
  TITLE     Establishment and Dysfunction of the Blood-Brain Barrier
  JOURNAL   Cell 163 (5), 1064-1078 (2015)
   PUBMED   26590417
  REMARK    Review article
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Boehmer,C., Okur,F., Setiawan,I., Broer,S. and Lang,F.
  TITLE     Properties and regulation of glutamine transporter SN1 by protein
            kinases SGK and PKB
  JOURNAL   Biochem Biophys Res Commun 306 (1), 156-162 (2003)
   PUBMED   12788082
  REMARK    GeneRIF: SN1 is a target for the ubiquitin ligase Nedd4-2, which is
            inactivated by the serum and glucocorticoid inducible kinase SGK1,
            its isoform SGK3, and protein kinase B.
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Lerman,M.I. and Minna,J.D.
  TITLE     The 630-kb lung cancer homozygous deletion region on human
            chromosome 3p21.3: identification and evaluation of the resident
            candidate tumor suppressor genes. The International Lung Cancer
            Chromosome 3p21.3 Tumor Suppressor Gene Consortium
  JOURNAL   Cancer Res 60 (21), 6116-6133 (2000)
   PUBMED   11085536
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Fei,Y.J., Sugawara,M., Nakanishi,T., Huang,W., Wang,H.,
            Prasad,P.D., Leibach,F.H. and Ganapathy,V.
  TITLE     Primary structure, genomic organization, and functional and
            electrogenic characteristics of human system N 1, a Na+- and
            H+-coupled glutamine transporter
  JOURNAL   J Biol Chem 275 (31), 23707-23717 (2000)
   PUBMED   10823827
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Chaudhry,F.A., Reimer,R.J., Krizaj,D., Barber,D.,
            Storm-Mathisen,J., Copenhagen,D.R. and Edwards,R.H.
  TITLE     Molecular analysis of system N suggests novel physiological roles
            in nitrogen metabolism and synaptic transmission
  JOURNAL   Cell 99 (7), 769-780 (1999)
   PUBMED   10619430
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP362985.1, BX537382.1, BM662099.1 and AC002077.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.25344.1, BX537382.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000614032.5/ ENSP00000481301.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..504
                     /product="sodium-coupled neutral amino acid transporter 3"
                     /note="system N1 Na+ and H+-coupled glutamine transporter;
                     N-system amino acid transporter 1; system N amino acid
                     transporter 1; Na(+)-coupled neutral amino acid
                     transporter 3"
                     /calculated_mol_wt=55642
     Region          64..491
                     /region_name="Aa_trans"
                     /note="Transmembrane amino acid transporter protein;
                     pfam01490"
                     /db_xref="CDD:279788"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99624.1)"
     Site            77
                     /site_type="other"
                     /note="Modulates L-glutamine-induced conductances and
                     Na(+) binding. /evidence=ECO:0000250|UniProtKB:Q9JHZ9;
                     propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99624.1)"
     Site            248
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99624.1)"
     Site            252
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99624.1)"
     Site            323
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99624.1)"
     Site            324..344
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     Site            366..386
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     Site            408..428
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     Site            431..451
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     Site            471..491
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99624.1)"
     CDS             1..504
                     /gene="SLC38A3"
                     /gene_synonym="DEE102; G17; NAT1; SN1; SNAT3"
                     /coded_by="NM_006841.6:130..1644"
                     /db_xref="CCDS:CCDS74940.1"
                     /db_xref="GeneID:10991"
                     /db_xref="HGNC:HGNC:18044"
                     /db_xref="MIM:604437"
ORIGIN      
        1 meaplqtemv elvpngkhse gllpvitpma gnqrvedpar scmegksflq kspskephft
       61 dfegktsfgm svfnlsnaim gsgilglaya mantgiilfl flltavalls sysihlllks
      121 sgvvgiraye qlgyrafgtp gklaaalait lqnigamssy lyiikselpl viqtflnlee
      181 ktsdwymngn ylvilvsvti ilplalmrql gylgyssgfs lscmvfflia viykkfhvpc
      241 plppnfnntt gnfshveivk ekvqlqvepe asafctpsyf tlnsqtayti pimafafvch
      301 pevlpiytel kdpskkkmqh isnlsiavmy imyflaalfg yltfyngves ellhtyskvd
      361 pfdvlilcvr vavltavtlt vpivlfpvrr aiqqmlfpnq efswlrhvli avglltcinl
      421 lvifapnilg ifgvigatsa pflififpai fyfrimptek eparstpkil alcfamlgfl
      481 lmtmslsfii idwasgtsrh ggnh
//
LOCUS       NP_061155               1124 aa            linear   PRI 27-APR-2025
DEFINITION  anillin isoform 1 [Homo sapiens].
ACCESSION   NP_061155
VERSION     NP_061155.2
DBSOURCE    REFSEQ: accession NM_018685.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Lin,L., Ye,Y., Fu,H., Gu,W., Zhao,M., Sun,J., Cao,Z., Huang,G.,
            Xie,Y., Liu,F., Li,L., Li,Q., Mao,J. and Hu,L.
  TITLE     Effects of a novel ANLN E841K mutation associated with SRNS on
            podocytes and its mechanism
  JOURNAL   Cell Commun Signal 21 (1), 324 (2023)
   PUBMED   37957688
  REMARK    GeneRIF: Effects of a novel ANLN E841K mutation associated with
            SRNS on podocytes and its mechanism.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Sheng,L., Kang,Y., Chen,D. and Shi,L.
  TITLE     Knockdown of ANLN inhibits the progression of lung adenocarcinoma
            via pyroptosis activation
  JOURNAL   Mol Med Rep 28 (3) (2023)
   PUBMED   37539739
  REMARK    GeneRIF: Knockdown of ANLN inhibits the progression of lung
            adenocarcinoma via pyroptosis activation.
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Saito,Y., Yin,D., Kubota,N., Wang,X., Filliol,A., Remotti,H.,
            Nair,A., Fazlollahi,L., Hoshida,Y., Tabas,I., Wangensteen,K.J. and
            Schwabe,R.F.
  TITLE     A Therapeutically Targetable TAZ-TEAD2 Pathway Drives the Growth of
            Hepatocellular Carcinoma via ANLN and KIF23
  JOURNAL   Gastroenterology 164 (7), 1279-1292 (2023)
   PUBMED   36894036
  REMARK    GeneRIF: A Therapeutically Targetable TAZ-TEAD2 Pathway Drives the
            Growth of Hepatocellular Carcinoma via ANLN and KIF23.
REFERENCE   4  (residues 1 to 1124)
  AUTHORS   Husser,M.C., Ozugergin,I., Resta,T., Martin,V.J.J. and Piekny,A.J.
  TITLE     Cytokinetic diversity in mammalian cells is revealed by the
            characterization of endogenous anillin, Ect2 and RhoA
  JOURNAL   Open Biol 12 (11), 220247 (2022)
   PUBMED   36416720
  REMARK    GeneRIF: Cytokinetic diversity in mammalian cells is revealed by
            the characterization of endogenous anillin, Ect2 and RhoA.
REFERENCE   5  (residues 1 to 1124)
  AUTHORS   Gbadegesin,R.A., Hall,G., Adeyemo,A., Hanke,N., Tossidou,I.,
            Burchette,J., Wu,G., Homstad,A., Sparks,M.A., Gomez,J., Jiang,R.,
            Alonso,A., Lavin,P., Conlon,P., Korstanje,R., Stander,M.C.,
            Shamsan,G., Barua,M., Spurney,R., Singhal,P.C., Kopp,J.B.,
            Haller,H., Howell,D., Pollak,M.R., Shaw,A.S., Schiffer,M. and
            Winn,M.P.
  TITLE     Mutations in the gene that encodes the F-actin binding protein
            anillin cause FSGS
  JOURNAL   J Am Soc Nephrol 25 (9), 1991-2002 (2014)
   PUBMED   24676636
  REMARK    GeneRIF: Identified a missense mutation R431C in anillin (ANLN), an
            F-actin binding cell cycle gene, as a cause of FSGS. We screened
            250 additional families with FSGS and found another variant, G618C,
            that segregates with disease in a second family with FSGS.
REFERENCE   6  (residues 1 to 1124)
  AUTHORS   Straight,A.F., Field,C.M. and Mitchison,T.J.
  TITLE     Anillin binds nonmuscle myosin II and regulates the contractile
            ring
  JOURNAL   Mol Biol Cell 16 (1), 193-201 (2005)
   PUBMED   15496454
  REMARK    GeneRIF: anillin has a role in spatially regulating the contractile
            activity of myosin II during cytokinesis
REFERENCE   7  (residues 1 to 1124)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1124)
  AUTHORS   Straight,A.F., Cheung,A., Limouze,J., Chen,I., Westwood,N.J.,
            Sellers,J.R. and Mitchison,T.J.
  TITLE     Dissecting temporal and spatial control of cytokinesis with a
            myosin II Inhibitor
  JOURNAL   Science 299 (5613), 1743-1747 (2003)
   PUBMED   12637748
REFERENCE   9  (residues 1 to 1124)
  AUTHORS   Kinoshita,M., Field,C.M., Coughlin,M.L., Straight,A.F. and
            Mitchison,T.J.
  TITLE     Self- and actin-templated assembly of Mammalian septins
  JOURNAL   Dev Cell 3 (6), 791-802 (2002)
   PUBMED   12479805
REFERENCE   10 (residues 1 to 1124)
  AUTHORS   Oegema,K., Savoian,M.S., Mitchison,T.J. and Field,C.M.
  TITLE     Functional analysis of a human homologue of the Drosophila actin
            binding protein anillin suggests a role in cytokinesis
  JOURNAL   J Cell Biol 150 (3), 539-552 (2000)
   PUBMED   10931866
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006960.1, AF273437.1 and
            BC070066.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 12, 2003 this sequence version replaced NP_061155.1.
            
            Summary: This gene encodes an actin-binding protein that plays a
            role in cell growth and migration, and in cytokinesis. The encoded
            protein is thought to regulate actin cytoskeletal dynamics in
            podocytes, components of the glomerulus. Mutations in this gene are
            associated with focal segmental glomerulosclerosis 8. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Oct 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.68164.1,
                                           SRR1803614.80044.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265748.7/ ENSP00000265748.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.2"
     Protein         1..1124
                     /product="anillin isoform 1"
                     /calculated_mol_wt=124068
     Region          1..230
                     /region_name="Nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          1..155
                     /region_name="Interaction with CD2AP.
                     /evidence=ECO:0000269|PubMed:15800069"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          1..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          1..45
                     /region_name="Required for ubiquitination"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K298; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          136..196
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          142..229
                     /region_name="Anillin_N"
                     /note="Anillin N-terminus; pfam16018"
                     /db_xref="CDD:435074"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          231..676
                     /region_name="Interaction with F-actin"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K298; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          294..328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            371
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          380..399
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          428..505
                     /region_name="Anillin_N"
                     /note="Anillin N-terminus; pfam16018"
                     /db_xref="CDD:435074"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          579..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          625..664
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8K298; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          730..1124
                     /region_name="Localization to the cleavage furrow"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Site            792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          800..953
                     /region_name="Anillin"
                     /note="Cell division protein anillin; pfam08174"
                     /db_xref="CDD:462393"
     Site            927
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQW6.2)"
     Region          983..1110
                     /region_name="PH_anillin"
                     /note="Anillin Pleckstrin homology (PH) domain; cd01263"
                     /db_xref="CDD:269964"
     CDS             1..1124
                     /gene="ANLN"
                     /gene_synonym="FSGS8; scra; Scraps"
                     /coded_by="NM_018685.5:166..3540"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5447.1"
                     /db_xref="GeneID:54443"
                     /db_xref="HGNC:HGNC:14082"
                     /db_xref="MIM:616027"
ORIGIN      
        1 mdpfteklle rtrarrenlq rkmaerptaa prsmthakra rqplseasnq qplsggeeks
       61 ctkpspskkr csdntevevs nlenkqpves tsakscspsp vspqvqpqaa dtisdsvavp
      121 asllgmrrgl nsrleataas svktrmqkla eqrrrwdndd mtddipessl fspmpseeka
      181 aspprpllsn asatpvgrrg rlanlaatic sweddvnhsf akqnsvqeqp gtaclskfss
      241 asgasarins ssvkqeatfc sqrdgdasln kalsssadda slvnasisss vkatspvkst
      301 tsitdaksce gqnpellpkt pisplktgvs kpivkstlsq tvpskgelsr eiclqsqskd
      361 ksttpggtgi kpflerfger cqehskespa rstphrtpii tpntkaiqer lfkqdtssst
      421 thlaqqlkqe rqkelaclrg rfdkgniwsa ekggnskskq letkqethcq stplkkhqgv
      481 sktqslpvte kvtenqipak nsstepkgft ecemtksspl kitlfleedk slkvtsdpkv
      541 eqkievirei emsvddddin sskvindlfs dvleegeldm eksqeemdqa laesseeqed
      601 alnissmsll aplaqtvgvv speslvstpr lelkdtsrsd espkpgkfqr trvpraesgd
      661 slgsedrdll ysidayrsqr fketerpsik qvivrkedvt skldeknnaf pcqvnikqkm
      721 qelnneinmq qtviyqasqa lnccvdeehg kgsleeaeae rllliatgkr tllidelnkl
      781 knegpqrknk aspqsefmps kgsvtlseir lplkadfvcs tvqkpdaany yyliilkaga
      841 enmvatplas tsnslngdal tftttftlqd vsndfeinie vyslvqkkdp sgldkkkkts
      901 kskaitpkrl ltsittksni hssvmaspgg lsavrtsnfa lvgsytlsls svgntkfvld
      961 kvpflssleg hiylkikcqv nssveergfl tifedvsgfg awhrrwcvls gncisywtyp
     1021 ddekrknpig rinlanctsr qiepanrefc arrntfelit vrpqreddre tlvsqcrdtl
     1081 cvtknwlsad tkeerdlwmq klnqvlvdir lwqpdacykp igkp
//
LOCUS       NP_001356098             554 aa            linear   ROD 27-APR-2025
DEFINITION  ankyrin repeat and death domain-containing protein 1B isoform 1
            [Mus musculus].
ACCESSION   NP_001356098
VERSION     NP_001356098.1
DBSOURCE    REFSEQ: accession NM_001369169.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Diez-Roux,G., Banfi,S., Sultan,M., Geffers,L., Anand,S., Rozado,D.,
            Magen,A., Canidio,E., Pagani,M., Peluso,I., Lin-Marq,N., Koch,M.,
            Bilio,M., Cantiello,I., Verde,R., De Masi,C., Bianchi,S.A.,
            Cicchini,J., Perroud,E., Mehmeti,S., Dagand,E., Schrinner,S.,
            Nurnberger,A., Schmidt,K., Metz,K., Zwingmann,C., Brieske,N.,
            Springer,C., Hernandez,A.M., Herzog,S., Grabbe,F., Sieverding,C.,
            Fischer,B., Schrader,K., Brockmeyer,M., Dettmer,S., Helbig,C.,
            Alunni,V., Battaini,M.A., Mura,C., Henrichsen,C.N.,
            Garcia-Lopez,R., Echevarria,D., Puelles,E., Garcia-Calero,E.,
            Kruse,S., Uhr,M., Kauck,C., Feng,G., Milyaev,N., Ong,C.K.,
            Kumar,L., Lam,M., Semple,C.A., Gyenesei,A., Mundlos,S., Radelof,U.,
            Lehrach,H., Sarmientos,P., Reymond,A., Davidson,D.R., Dolle,P.,
            Antonarakis,S.E., Yaspo,M.L., Martinez,S., Baldock,R.A., Eichele,G.
            and Ballabio,A.
  TITLE     A high-resolution anatomical atlas of the transcriptome in the
            mouse embryo
  JOURNAL   PLoS Biol 9 (1), e1000582 (2011)
   PUBMED   21267068
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125534.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849376,
                              SAMN00849389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 50.56 cM"
     Protein         1..554
                     /product="ankyrin repeat and death domain-containing
                     protein 1B isoform 1"
                     /note="ankyrin repeat and death domain-containing protein
                     ENSP00000345065 homolog; ankyrin repeat and death
                     domain-containing protein 1B"
                     /calculated_mol_wt=61701
     Region          68..157
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Site            order(70..72,74..75,79,82,91,93,95,99..100,103..105,
                     107..108,112,115,124,126,128,132..133,136..138,140..141,
                     145,148,157)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          93..124
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          126..157
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          142..415
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          163..192
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(194,196,200..201,204..206,208..209,213,216,225,227,
                     229,233..234,237..239,241..242,246,249,258,260,262,
                     266..267,270..272,274..275,279,282,291)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          194..225
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          227..258
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          260..291
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          293..321
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          330..357
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(332..333,336..338,340..341,345,348,357,359,361,
                     365..366,369..371,373..374,378,381,390,392,394,398..399,
                     402..404,406..407,411,414)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          359..390
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          466..540
                     /region_name="Death"
                     /note="Death domain; pfam00531"
                     /db_xref="CDD:459845"
     CDS             1..554
                     /gene="Ankdd1b"
                     /gene_synonym="9330128J19Rik"
                     /coded_by="NM_001369169.1:109..1773"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS88501.1"
                     /db_xref="GeneID:271144"
                     /db_xref="MGI:MGI:2444730"
ORIGIN      
        1 mnpesaqghg arapmlqaar glkanlrdva trpwrslarm pkpevqdpet aaagheglla
       61 iersfqnaak ssnldlmekl fekkvninav nnmnrtalhf avgrnslsav dfllshkarv
      121 dvadkhgltv ihlaawsgsf eimlmlvkag adqraknqeg mnalhlaaqn nnlhivdyli
      181 hdlhlhdlnq pnergrkpfh laaerghvem iekliflnlh tsekdkdgnt alhlaamhgh
      241 spavqvlltq wsevnesnen getpfllavv ggheecsrvl laggsdvnip nklnvsalqt
      301 atrnghtalv nfllgenadl qqqkeskepp lhlavinnrp avvnsllsar hdvdvldqrr
      361 qtplhvaadl gnvelvetll kagcnlkitd kqgktalava arsqhslvvd mlikaeryya
      421 wreehresiq dsavsstltf kqdhsletrq irtllwnlay rqlkkkdwqr larlwsfted
      481 qiraieeqws gndsfhehgy ralliwlhga lltqldpakq lyeellcagf pelaekirqf
      541 ksktdssskk cavs
//
LOCUS       NP_689509               1013 aa            linear   PRI 27-APR-2025
DEFINITION  sodium/potassium-transporting ATPase subunit alpha-3 isoform 1
            [Homo sapiens].
ACCESSION   NP_689509 NP_000694
VERSION     NP_689509.1
DBSOURCE    REFSEQ: accession NM_152296.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Depierre,P., Ginet,V., Truttmann,A.C. and Puyal,J.
  TITLE     Neuronal autosis is Na+/K+-ATPase alpha 3-dependent and involved in
            hypoxic-ischemic neuronal death
  JOURNAL   Cell Death Dis 15 (5), 363 (2024)
   PUBMED   38796484
  REMARK    GeneRIF: Neuronal autosis is Na[+]/K[+]-ATPase alpha 3-dependent
            and involved in hypoxic-ischemic neuronal death.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Muthaffar,O.Y., Alqarni,A., Shafei,J.A., Bahowarth,S.Y.,
            Alyazidi,A.S. and Naseer,M.I.
  TITLE     Childhood-related neural genotype-phenotype in ATP1A3 mutations:
            comprehensive analysis
  JOURNAL   Genes Genomics 46 (4), 475-487 (2024)
   PUBMED   38243045
  REMARK    GeneRIF: Childhood-related neural genotype-phenotype in ATP1A3
            mutations: comprehensive analysis.
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   You,Y., Zhang,Z., Sultana,N., Ericsson,M., Martens,Y.A., Sun,M.,
            Kanekiyo,T., Ikezu,S., Shaffer,S.A. and Ikezu,T.
  TITLE     ATP1A3 as a target for isolating neuron-specific extracellular
            vesicles from human brain and biofluids
  JOURNAL   Sci Adv 9 (37), eadi3647 (2023)
   PUBMED   37713494
  REMARK    GeneRIF: ATP1A3 as a target for isolating neuron-specific
            extracellular vesicles from human brain and biofluids.
REFERENCE   4  (residues 1 to 1013)
  AUTHORS   Alyamani,S.A., Aldhalaan,H.M., Almuhaizea,M.A. and Abukhalid,M.F.
  TITLE     Expanding the Allelic spectrum in ATP1A3-related disorders with 3
            novel mutations and clinic features
  JOURNAL   Neurosciences (Riyadh) 28 (3), 195-198 (2023)
   PUBMED   37482377
  REMARK    GeneRIF: Expanding the Allelic spectrum in ATP1A3-related disorders
            with 3 novel mutations and clinic features.
REFERENCE   5  (residues 1 to 1013)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   6  (residues 1 to 1013)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   7  (residues 1 to 1013)
  AUTHORS   Brashear,A., Sweadner,K.J., Haq,I., Napoli,E. and Ozelius,L.
  TITLE     ATP1A3-Related Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301294
REFERENCE   8  (residues 1 to 1013)
  AUTHORS   Lingrel,J.B., Orlowski,J., Shull,M.M. and Price,E.M.
  TITLE     Molecular genetics of Na,K-ATPase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 38, 37-89 (1990)
   PUBMED   2158121
  REMARK    Review article
REFERENCE   9  (residues 1 to 1013)
  AUTHORS   Ovchinnikov,Yu.A., Monastyrskaya,G.S., Broude,N.E.,
            Ushkaryov,Yu.A., Melkov,A.M., Smirnov,Yu.V., Malyshev,I.V.,
            Allikmets,R.L., Kostina,M.B., Dulubova,I.E. et al.
  TITLE     Family of human Na+, K+-ATPase genes. Structure of the gene for the
            catalytic subunit (alpha III-form) and its relationship with
            structural features of the protein
  JOURNAL   FEBS Lett 233 (1), 87-94 (1988)
   PUBMED   2838329
REFERENCE   10 (residues 1 to 1013)
  AUTHORS   Sverdlov,E.D., Monastyrskaia,G.S., Broude,N.E., Ushkarev,Iu.A. and
            Melkov,A.M.
  TITLE     [The family of human Na+,K+-ATPase genes. Structure of the gene for
            isozyme alphaII]
  JOURNAL   Dokl Akad Nauk SSSR 297 (6), 1488-1494 (1987)
   PUBMED   2834163
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB482528.1, AK223569.1,
            AK295078.1 and BC009282.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 3, 2002 this sequence version replaced NP_000694.1.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of Na+/K+
            -ATPases. Na+/K+ -ATPase is an integral membrane protein
            responsible for establishing and maintaining the electrochemical
            gradients of Na and K ions across the plasma membrane. These
            gradients are essential for osmoregulation, for sodium-coupled
            transport of a variety of organic and inorganic molecules, and for
            electrical excitability of nerve and muscle. This enzyme is
            composed of two subunits, a large catalytic subunit (alpha) and a
            smaller glycoprotein subunit (beta). The catalytic subunit of
            Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an
            alpha 3 subunit. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jan 2012].
            
            Transcript Variant: This variant (1) is the predominant transcript
            and encodes isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009394.2, AK223569.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000648268.1/ ENSP00000498113.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..1013
                     /product="sodium/potassium-transporting ATPase subunit
                     alpha-3 isoform 1"
                     /EC_number="7.2.2.13"
                     /note="sodium-potassium-ATPase, alpha 3 polypeptide;
                     Na+/K+ ATPase 3; sodium/potassium-transporting ATPase
                     alpha-3 chain; sodium/potassium-transporting ATPase
                     subunit alpha-3; sodium pump subunit alpha-3; Na(+)/K(+)
                     ATPase alpha-3 subunit; Na(+)/K(+) ATPase alpha(III)
                     subunit; sodium-potassium ATPase catalytic subunit
                     alpha-3; ATPase, Na+/K+ transporting, alpha 3 polypeptide;
                     Na+, K+ activated adenosine triphosphatase alpha subunit"
                     /calculated_mol_wt=111618
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Region          17..1013
                     /region_name="ATPase-IIC_X-K"
                     /note="sodium or proton efflux -- potassium uptake
                     antiporter, P-type ATPase, alpha subunit; TIGR01106"
                     /db_xref="CDD:273445"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06687; propagated from
                     UniProtKB/Swiss-Prot (P13637.3)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PIC6; propagated from
                     UniProtKB/Swiss-Prot (P13637.3)"
     Region          72..74
                     /region_name="Interaction with phosphoinositide-3 kinase.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PIC6; propagated from
                     UniProtKB/Swiss-Prot (P13637.3)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PIC6; propagated from
                     UniProtKB/Swiss-Prot (P13637.3)"
     Site            279..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            311..328
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06687; propagated from
                     UniProtKB/Swiss-Prot (P13637.3)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q6PIC6; propagated from
                     UniProtKB/Swiss-Prot (P13637.3)"
     Site            763..782
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            793..813
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            834..856
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            909..928
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            933
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            942..960
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     Site            976..996
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13637.3)"
     CDS             1..1013
                     /gene="ATP1A3"
                     /gene_synonym="AHC2; ATP1A1; CAPOS; DEE99; DYT12; RDP"
                     /coded_by="NM_152296.5:155..3196"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12594.1"
                     /db_xref="GeneID:478"
                     /db_xref="HGNC:HGNC:801"
                     /db_xref="MIM:182350"
ORIGIN      
        1 mgdkkddkds pkknkgkerr dlddlkkeva mtehkmsvee vcrkyntdcv qglthskaqe
       61 ilardgpnal tpppttpewv kfcrqlfggf sillwigail cflaygiqag teddpsgdnl
      121 ylgivlaavv iitgcfsyyq eaksskimes fknmvpqqal viregekmqv naeevvvgdl
      181 veikggdrvp adlriisahg ckvdnssltg esepqtrspd cthdnpletr nitffstncv
      241 egtargvvva tgdrtvmgri atlasglevg ktpiaieieh fiqlitgvav flgvsffils
      301 lilgytwlea vifligiiva nvpegllatv tvcltltakr marknclvkn leavetlgst
      361 sticsdktgt ltqnrmtvah mwfdnqihea dttedqsgts fdksshtwva lshiaglcnr
      421 avfkggqdni pvlkrdvagd asesallkci elssgsvklm rernkkvaei pfnstnkyql
      481 sihetedpnd nryllvmkga perildrcst illqgkeqpl deemkeafqn aylelgglge
      541 rvlgfchyyl peeqfpkgfa fdcddvnftt dnlcfvglms midppraavp davgkcrsag
      601 ikvimvtgdh pitakaiakg vgiisegnet vediaarlni pvsqvnprda kacvihgtdl
      661 kdftseqide ilqnhteivf artspqqkli ivegcqrqga ivavtgdgvn dspalkkadi
      721 gvamgiagsd vskqaadmil lddnfasivt gveegrlifd nlkksiaytl tsnipeitpf
      781 llfimanipl plgtitilci dlgtdmvpai slayeaaesd imkrqprnpr tdklvnerli
      841 smaygqigmi qalggffsyf vilaengflp gnlvgirlnw ddrtvndled sygqqwtyeq
      901 rkvveftcht affvsivvvq wadliicktr rnsvfqqgmk nkilifglfe etalaaflsy
      961 cpgmdvalrm yplkpswwfc afpysflifv ydeirklilr rnpggwveke tyy
//
LOCUS       NP_001349943             281 aa            linear   PRI 27-APR-2025
DEFINITION  antizyme inhibitor 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001349943 XP_016869054
VERSION     NP_001349943.1
DBSOURCE    REFSEQ: accession NM_001363014.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Xing,Y., Nakahama,T., Wu,Y., Inoue,M., Kim,J.I., Todo,H.,
            Shibuya,T., Kato,Y. and Kawahara,Y.
  TITLE     RNA editing of AZIN1 coding sites is catalyzed by ADAR1 p150 after
            splicing
  JOURNAL   J Biol Chem 299 (7), 104840 (2023)
   PUBMED   37209819
  REMARK    GeneRIF: RNA editing of AZIN1 coding sites is catalyzed by ADAR1
            p150 after splicing.
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Nakamura,K., Shigeyasu,K., Okamoto,K., Matsuoka,H. and Masuyama,H.
  TITLE     ADAR1 and AZIN1 RNA editing function as an oncogene and contributes
            to immortalization in endometrial cancer
  JOURNAL   Gynecol Oncol 166 (2), 326-333 (2022)
   PUBMED   35697535
  REMARK    GeneRIF: ADAR1 and AZIN1 RNA editing function as an oncogene and
            contributes to immortalization in endometrial cancer.
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Wei,Y., Zhang,H., Feng,Q., Wang,S., Shao,Y., Wu,J., Jin,G., Lin,W.,
            Peng,X. and Xu,X.
  TITLE     A novel mechanism for A-to-I RNA-edited AZIN1 in promoting tumor
            angiogenesis in colorectal cancer
  JOURNAL   Cell Death Dis 13 (4), 294 (2022)
   PUBMED   35365616
  REMARK    GeneRIF: A novel mechanism for A-to-I RNA-edited AZIN1 in promoting
            tumor angiogenesis in colorectal cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Chen,L., Li,Y., Lin,C.H., Chan,T.H., Chow,R.K., Song,Y., Liu,M.,
            Yuan,Y.F., Fu,L., Kong,K.L., Qi,L., Li,Y., Zhang,N., Tong,A.H.,
            Kwong,D.L., Man,K., Lo,C.M., Lok,S., Tenen,D.G. and Guan,X.Y.
  TITLE     Recoding RNA editing of AZIN1 predisposes to hepatocellular
            carcinoma
  JOURNAL   Nat Med 19 (2), 209-216 (2013)
   PUBMED   23291631
  REMARK    GeneRIF: edited form has a stronger affinity to antizyme, and the
            resultant higher AZIN1 protein stability promotes cell
            proliferation through the neutralization of antizyme-mediated
            degradation of ornithine decarboxylase (ODC) and cyclin D1
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Paris,A.J., Snapir,Z., Christopherson,C.D., Kwok,S.Y., Lee,U.E.,
            Ghiassi-Nejad,Z., Kocabayoglu,P., Sninsky,J.J., Llovet,J.M.,
            Kahana,C. and Friedman,S.L.
  TITLE     A polymorphism that delays fibrosis in hepatitis C promotes
            alternative splicing of AZIN1, reducing fibrogenesis
  JOURNAL   Hepatology 54 (6), 2198-2207 (2011)
   PUBMED   21837750
  REMARK    GeneRIF: minor allelic SNP variant in 12th exon of AZIN1 associated
            with slower rates of fibrosis progression favors expression of
            novel splice form, AZIN1 SV2, that inhibits expression of
            fibrogenic genes in hepatic stellate cells.
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Lopez-Contreras,A.J., Ramos-Molina,B., Cremades,A. and Penafiel,R.
  TITLE     Antizyme inhibitor 2 (AZIN2/ODCp) stimulates polyamine uptake in
            mammalian cells
  JOURNAL   J Biol Chem 283 (30), 20761-20769 (2008)
   PUBMED   18508777
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Choi,K.S., Suh,Y.H., Kim,W.H., Lee,T.H. and Jung,M.H.
  TITLE     Stable siRNA-mediated silencing of antizyme inhibitor: regulation
            of ornithine decarboxylase activity
  JOURNAL   Biochem Biophys Res Commun 328 (1), 206-212 (2005)
   PUBMED   15670771
  REMARK    GeneRIF: This study also suggests that highly expressed AZI may be
            partly responsible for increased ODC activity and cellular
            transformation.
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Imabayashi,H., Mori,T., Gojo,S., Kiyono,T., Sugiyama,T., Irie,R.,
            Isogai,T., Hata,J., Toyama,Y. and Umezawa,A.
  TITLE     Redifferentiation of dedifferentiated chondrocytes and
            chondrogenesis of human bone marrow stromal cells via chondrosphere
            formation with expression profiling by large-scale cDNA analysis
  JOURNAL   Exp Cell Res 288 (1), 35-50 (2003)
   PUBMED   12878157
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Koguchi,K., Kobayashi,S., Hayashi,T., Matsufuji,S., Murakami,Y. and
            Hayashi,S.
  TITLE     Cloning and sequencing of a human cDNA encoding ornithine
            decarboxylase antizyme inhibitor
  JOURNAL   Biochim Biophys Acta 1353 (3), 209-216 (1997)
   PUBMED   9349715
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB092816.1, BC042404.1,
            CX781377.1, BU507334.1, BC013420.2, BM716557.1 and AI671875.1.
            
            On May 4, 2018 this sequence version replaced XP_016869054.1.
            
            Summary: The protein encoded by this gene belongs to the antizyme
            inhibitor family, which plays a role in cell growth and
            proliferation by maintaining polyamine homeostasis within the cell.
            Antizyme inhibitors are homologs of ornithine decarboxylase (ODC,
            the key enzyme in polyamine biosynthesis) that have lost the
            ability to decarboxylase ornithine; however, retain the ability to
            bind to antizymes. Antizymes negatively regulate intracellular
            polyamine levels by binding to ODC and targeting it for
            degradation, as well as by inhibiting polyamine uptake. Antizyme
            inhibitors function as positive regulators of polyamine levels by
            sequestering antizymes and neutralizing their effect. This gene
            encodes antizyme inhibitor 1, the first member of this gene family
            that is ubiquitously expressed, and is localized in the nucleus and
            cytoplasm. Overexpression of antizyme inhibitor 1 gene has been
            associated with increased proliferation, cellular transformation
            and tumorigenesis. Gene knockout studies showed that homozygous
            mutant mice lacking functional antizyme inhibitor 1 gene died at
            birth with abnormal liver morphology. RNA editing of this gene,
            predominantly in the liver tissue, has been linked to the
            progression of hepatocellular carcinoma. Alternatively spliced
            transcript variants have been described for this gene. [provided by
            RefSeq, Sep 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.107503.1,
                                           SRR1803612.63331.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            undergoes RNA editing :: PMID: 23291631
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..281
                     /product="antizyme inhibitor 1 isoform 4"
                     /note="ornithine decarboxylase antizyme inhibitor"
                     /calculated_mol_wt=31273
     Region          <1..252
                     /region_name="PLPDE_III"
                     /note="Type III Pyridoxal 5-phosphate (PLP)-Dependent
                     Enzymes; cl00261"
                     /db_xref="CDD:469695"
     CDS             1..281
                     /gene="AZIN1"
                     /gene_synonym="AZI; AZI1; AZIA1; OAZI; OAZIN; ODC1L"
                     /coded_by="NM_001363014.1:1426..2271"
                     /note="isoform 4 is encoded by transcript variant 10"
                     /db_xref="GeneID:51582"
                     /db_xref="HGNC:HGNC:16432"
                     /db_xref="MIM:607909"
ORIGIN      
        1 mkfgttlknc rhllecakel dvqiigvkfh vssackesqv yvhalsdarc vfdmageigf
       61 tmnmldiggg ftgtefqlee vnhvisplld iyfpegsgvk iisepgsyyv ssaftlavni
      121 iakkvvendk fpsgvektgs depafmyymn dgvygsfask lsedlntipe vhkkykedep
      181 lftsslwgps cdeldqives cllpelnvgd wlifdnmgad sfhepsafnd fqrpaiyymm
      241 sfsdwyemqd agitsdsmmk nfffvpsciq lsqedsfsae a
//
LOCUS       NP_001354840             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 678 isoform 3 [Homo sapiens].
ACCESSION   NP_001354840
VERSION     NP_001354840.1
DBSOURCE    REFSEQ: accession NM_001367911.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Lee,J.J., Essers,J.B., Kugathasan,S., Escher,J.C., Lettre,G.,
            Butler,J.L., Stephens,M.C., Ramoni,M.F., Grand,R.J. and
            Hirschhorn,J.
  TITLE     Association of linear growth impairment in pediatric Crohn's
            disease and a known height locus: a pilot study
  JOURNAL   Ann Hum Genet 74 (6), 489-497 (2010)
   PUBMED   20846217
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Zhao,J., Li,M., Bradfield,J.P., Zhang,H., Mentch,F.D., Wang,K.,
            Sleiman,P.M., Kim,C.E., Glessner,J.T., Hou,C., Keating,B.J.,
            Thomas,K.A., Garris,M.L., Deliard,S., Frackelton,E.C., Otieno,F.G.,
            Chiavacci,R.M., Berkowitz,R.I., Hakonarson,H. and Grant,S.F.
  TITLE     The role of height-associated loci identified in genome wide
            association studies in the determination of pediatric stature
  JOURNAL   BMC Med Genet 11, 96 (2010)
   PUBMED   20546612
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Weedon,M.N., Lango,H., Lindgren,C.M., Wallace,C., Evans,D.M.,
            Mangino,M., Freathy,R.M., Perry,J.R., Stevens,S., Hall,A.S.,
            Samani,N.J., Shields,B., Prokopenko,I., Farrall,M., Dominiczak,A.,
            Johnson,T., Bergmann,S., Beckmann,J.S., Vollenweider,P.,
            Waterworth,D.M., Mooser,V., Palmer,C.N., Morris,A.D.,
            Ouwehand,W.H., Zhao,J.H., Li,S., Loos,R.J., Barroso,I.,
            Deloukas,P., Sandhu,M.S., Wheeler,E., Soranzo,N., Inouye,M.,
            Wareham,N.J., Caulfield,M., Munroe,P.B., Hattersley,A.T.,
            McCarthy,M.I. and Frayling,T.M.
  CONSRTM   Diabetes Genetics Initiative; Wellcome Trust Case Control
            Consortium; Cambridge GEM Consortium
  TITLE     Genome-wide association analysis identifies 20 loci that influence
            adult height
  JOURNAL   Nat Genet 40 (5), 575-583 (2008)
   PUBMED   18391952
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL451054.22 and AL592310.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.153302.1,
                                           SRR1660803.179974.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.13"
     Protein         1..549
                     /product="zinc finger protein 678 isoform 3"
                     /note="hypothetical protein MGC42493"
                     /calculated_mol_wt=64346
     Region          12..52
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          107..505
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          123..143
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(128,130,132,134..135,138..139,142,156,158,162..163,
                     166..167,170,184,186,188,190..191,194..195,198)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          151..171
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          179..199
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          207..227
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          235..255
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          263..283
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          291..311
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          319..339
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          347..367
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(352,354,356,358..359,362..363,366,380,382,386..387,
                     390..391,394,408,410,412,414..415,418..419,422)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          375..395
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          403..423
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          431..451
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(436,438,440,442..443,446..447,450,464,466,470..471,
                     474..475,478,492,494,496,498..499,502..503,506)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          459..479
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          487..507
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          499..524
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     CDS             1..549
                     /gene="ZNF678"
                     /coded_by="NM_001367911.1:140..1789"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:339500"
                     /db_xref="HGNC:HGNC:28652"
ORIGIN      
        1 mpghpesrkt gllafsdvvi efspeewacl dpaqrnlyrd vmfenyrnlv slailsysiq
       61 dllpeqdmkd lcqkvtltrh rswgldnlhl vkdwrtvneg kgqkeycnrl tqcsstkski
      121 fqciecgrnf swrsiltehk rihtgekpyk ceecgkvfnr csnltkhkri htgekpykcd
      181 ecgkvfnwws qltnhkkiht gekpykcdec dkvfnwwsql tshkkihsge kpypceecgk
      241 aftqfsnltq hkrihtgekp ykckecckaf nkfsnltqhk rihtgekpyk ceecgnvfne
      301 cshltrhrri htgekpykce ecgkaftqfa sltrhkriht gekpyqceec gktfnrcshl
      361 sshkrihtge kpykceecgr tftqfsnltq hkrihtgekp ykckecgkaf nkfssltqhr
      421 rihtgvkpyk ceecgkvfkq cshltshkri htgekpykck ecgkafyqss ilskhkriht
      481 eekpykceec gkafnqfssl trhkrihtge krykckecgk gfyqssihsk ykriytgeep
      541 dkckkcgsl
//
LOCUS       NP_008933                407 aa            linear   PRI 27-APR-2025
DEFINITION  proteasomal ubiquitin receptor ADRM1 isoform 1 [Homo sapiens].
ACCESSION   NP_008933
VERSION     NP_008933.2
DBSOURCE    REFSEQ: accession NM_007002.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Shao,Z., Wang,Y., He,Y., Zhang,C., Zhao,Y., Zhang,M., Li,Q. and
            Wang,J.
  TITLE     The high expression of ADRM1 in hepatocellular carcinoma is closely
            related to tumor immune infiltration and is regulated by
            miR-891a-5p
  JOURNAL   Sci Rep 14 (1), 14002 (2024)
   PUBMED   38890391
  REMARK    GeneRIF: The high expression of ADRM1 in hepatocellular carcinoma
            is closely related to tumor immune infiltration and is regulated by
            miR-891a-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Osei-Amponsa,V., Chandravanshi,M., Lu,X., Magidson,V., Das,S.,
            Andresson,T., Dyba,M., Sabbasani,V.R., Swenson,R.E., Fromont,C.,
            Shrestha,B., Zhao,Y., Clapp,M.E., Chari,R. and Walters,K.J.
  TITLE     hRpn13 shapes the proteome and transcriptome through epigenetic
            factors HDAC8, PADI4, and transcription factor NF-kappaB p50
  JOURNAL   Mol Cell 84 (3), 522-537 (2024)
   PUBMED   38151017
  REMARK    GeneRIF: hRpn13 shapes the proteome and transcriptome through
            epigenetic factors HDAC8, PADI4, and transcription factor NF-kappaB
            p50.
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Zhu,D. and Zhong,Q.
  TITLE     Potential of adhesion-regulating molecule 1 (ADRM1) as a biomarker
            for patients with renal clear-cell carcinoma or papillary-cell
            carcinoma
  JOURNAL   Asian J Surg 46 (10), 4666-4668 (2023)
   PUBMED   37268471
  REMARK    GeneRIF: Potential of adhesion-regulating molecule 1 (ADRM1) as a
            biomarker for patients with renal clear-cell carcinoma or
            papillary-cell carcinoma.
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Xiao,J., Xie,Y., Duan,Q., Liu,T., Ye,R., Duan,X., Le,Z., Deng,N.
            and Liu,F.
  TITLE     LIM Homeobox 2 Increases Adhesion-Regulating Molecule 1
            Transcription to Facilitate the Pathological Progression of
            Oxidized Low-Density Lipoprotein-Stimulated Atherosclerotic Cell
            Models
  JOURNAL   Int Heart J 64 (4), 750-758 (2023)
   PUBMED   37518356
  REMARK    GeneRIF: LIM Homeobox 2 Increases Adhesion-Regulating Molecule 1
            Transcription to Facilitate the Pathological Progression of
            Oxidized Low-Density Lipoprotein-Stimulated Atherosclerotic Cell
            Models.
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Lu,X., Sabbasani,V.R., Osei-Amponsa,V., Evans,C.N., King,J.C.,
            Tarasov,S.G., Dyba,M., Das,S., Chan,K.C., Schwieters,C.D.,
            Choudhari,S., Fromont,C., Zhao,Y., Tran,B., Chen,X., Matsuo,H.,
            Andresson,T., Chari,R., Swenson,R.E., Tarasova,N.I. and
            Walters,K.J.
  TITLE     Structure-guided bifunctional molecules hit a DEUBAD-lacking hRpn13
            species upregulated in multiple myeloma
  JOURNAL   Nat Commun 12 (1), 7318 (2021)
   PUBMED   34916494
  REMARK    GeneRIF: Structure-guided bifunctional molecules hit a
            DEUBAD-lacking hRpn13 species upregulated in multiple myeloma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Yao,T., Song,L., Xu,W., DeMartino,G.N., Florens,L., Swanson,S.K.,
            Washburn,M.P., Conaway,R.C., Conaway,J.W. and Cohen,R.E.
  TITLE     Proteasome recruitment and activation of the Uch37 deubiquitinating
            enzyme by Adrm1
  JOURNAL   Nat Cell Biol 8 (9), 994-1002 (2006)
   PUBMED   16906146
  REMARK    GeneRIF: Neither Uch37 alone nor the Uch37-Adrm1 or Uch37-Adrm1-S1
            complexes can hydrolyse di-ubiquitin efficiently; rather,
            incorporation into the 19S complex is required to enable processing
            of polyubiquitin chains.
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Jorgensen,J.P., Lauridsen,A.M., Kristensen,P., Dissing,K.,
            Johnsen,A.H., Hendil,K.B. and Hartmann-Petersen,R.
  TITLE     Adrm1, a putative cell adhesion regulating protein, is a novel
            proteasome-associated factor
  JOURNAL   J Mol Biol 360 (5), 1043-1052 (2006)
   PUBMED   16815440
  REMARK    GeneRIF: Adrm1 has a specialised role in proteasome function.
            Identified Adrm1 as a novel component of the regulatory ATPase
            complex of the 26 S proteasome
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Lamerant,N. and Kieda,C.
  TITLE     Adhesion properties of adhesion-regulating molecule 1 protein on
            endothelial cells
  JOURNAL   FEBS J 272 (8), 1833-1844 (2005)
   PUBMED   15819879
  REMARK    GeneRIF: ARM-1 is a cytosolic protein associated with the plasma
            membrane. However, no cell surface expression of the protein was
            observed. These results suggest an indirect role of ARM-1 in
            adhesion rather than a direct role as an adhesion molecule
            itself.[ARM-1]
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Simins,A.B., Weighardt,H., Weidner,K.M., Weidle,U.H. and
            Holzmann,B.
  TITLE     Functional cloning of ARM-1, an adhesion-regulating molecule
            upregulated in metastatic tumor cells
  JOURNAL   Clin Exp Metastasis 17 (8), 641-648 (1999)
   PUBMED   10919708
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Shimada,S., Ogawa,M., Takahashi,M., Schlom,J. and Greiner,J.W.
  TITLE     Molecular cloning and characterization of the complementary DNA of
            an M(r) 110,000 antigen expressed by human gastric carcinoma cells
            and upregulated by gamma-interferon
  JOURNAL   Cancer Res 54 (14), 3831-3836 (1994)
   PUBMED   8033103
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354836.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 13, 2003 this sequence version replaced NP_008933.1.
            
            Summary: This gene encodes a member of the adhesion regulating
            molecule 1 protein family. The encoded protein is a component of
            the proteasome where it acts as a ubiquitin receptor and recruits
            the deubiquitinating enzyme, ubiquitin carboxyl-terminal hydrolase
            L5. Increased levels of the encoded protein are associated with
            increased cell adhesion, which is likely an indirect effect of this
            intracellular protein. Dysregulation of this gene has been
            implicated in carcinogenesis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Variants 1 and 2
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093021.1, SRR3476690.381698.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253003.7/ ENSP00000253003.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..407
                     /product="proteasomal ubiquitin receptor ADRM1 isoform 1"
                     /note="110 kDa cell membrane glycoprotein; M(r) 110,000
                     surface antigen; proteasomal ubiquitin receptor ADRM1;
                     rpn13 homolog; proteasome regulatory particle non-ATPase
                     13; proteasome ubiquitin receptor; adhesion regulating
                     molecule 1"
                     /calculated_mol_wt=42022
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Region          24..128
                     /region_name="PH_Rpn13"
                     /note="Pleckstrin homology-like domain of Regulatory
                     Particle Non-ATPase 13; cd13314"
                     /db_xref="CDD:270124"
     Site            order(53..54,56,73..80,98..100,103)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:270124"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Region          194..259
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Region          253..407
                     /region_name="Interaction with UCHL5.
                     /evidence=ECO:0000269|PubMed:20471946"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Region          274..381
                     /region_name="RPN13_C"
                     /note="UCH-binding domain; pfam16550"
                     /db_xref="CDD:465170"
     Region          379..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JMB5; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     CDS             1..407
                     /gene="ADRM1"
                     /gene_synonym="ARM-1; ARM1; GP110; PSMD16"
                     /coded_by="NM_007002.4:55..1278"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13496.1"
                     /db_xref="GeneID:11047"
                     /db_xref="HGNC:HGNC:15759"
                     /db_xref="MIM:610650"
ORIGIN      
        1 mttsgalfps lvpgsrgasn kylvefragk mslkgttvtp dkrkglvyiq qtddslihfc
       61 wkdrtsgnve ddliifpddc efkrvpqcps grvyvlkfka gskrlffwmq epktdqdeeh
      121 crkvneylnn ppmpgalgas gssghelsal ggegglqsll gnmshsqlmq ligpaglggl
      181 gglgaltgpg lasllgssgp pgsssssssr sqsaavtpss ttsstratpa psapaaasat
      241 spspapssgn gastaasptq piqlsdlqsi latmnvpagp aggqqvdlas vltpeimapi
      301 lanadvqerl lpylpsgesl pqtadeiqnt ltspqfqqal gmfsaalasg qlgplmcqfg
      361 lpaeaveaan kgdveafaka mqnnakpeqk egdtkdkkde eedmsld
//
LOCUS       NP_001356337             323 aa            linear   PRI 27-APR-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 1 [Homo sapiens].
ACCESSION   NP_001356337 XP_005258692
VERSION     NP_001356337.1
DBSOURCE    REFSEQ: accession NM_001369408.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
            Review article
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Du,P., Li,G., Wu,L. and Huang,M.
  TITLE     Perspectives of ERCC1 in early-stage and advanced cervical cancer:
            From experiments to clinical applications
  JOURNAL   Front Immunol 13, 1065379 (2023)
   PUBMED   36713431
  REMARK    GeneRIF: Perspectives of ERCC1 in early-stage and advanced cervical
            cancer: From experiments to clinical applications.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 323)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 323)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139353.3.
            
            On Apr 9, 2019 this sequence version replaced XP_005258692.1.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1159961.1,
                                           SRR1803612.211387.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..323
                     /product="DNA excision repair protein ERCC-1 isoform 1"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=35432
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P07992.1)"
     Region          17..23
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          <250..>281
                     /region_name="PRK00024"
                     /note="DNA repair protein RadC"
                     /db_xref="CDD:178801"
     CDS             1..323
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369408.1:103..1074"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS12663.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrvteclt
      241 tvksvnktds qtllttfgsl eqliaasred lalcpglgpq kvralgknpr swgkerapnk
      301 hnlrpqsfkv kkepktrhsg frl
//
LOCUS       NP_065174                489 aa            linear   PRI 27-APR-2025
DEFINITION  coronin-1B [Homo sapiens].
ACCESSION   NP_065174
VERSION     NP_065174.1
DBSOURCE    REFSEQ: accession NM_020441.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Hachimi,M., Grabowski,C., Campanario,S., Herranz,G., Baonza,G.,
            Serrador,J.M., Gomez-Lopez,S., Barea,M.D., Bosch-Fortea,M.,
            Gilmour,D., Bagnat,M., Rodriguez-Fraticelli,A.E. and
            Martin-Belmonte,F.
  TITLE     Smoothelin-like 2 Inhibits Coronin-1B to Stabilize the Apical Actin
            Cortex during Epithelial Morphogenesis
  JOURNAL   Curr Biol 31 (4), 696-706 (2021)
   PUBMED   33275893
  REMARK    GeneRIF: Smoothelin-like 2 Inhibits Coronin-1B to Stabilize the
            Apical Actin Cortex during Epithelial Morphogenesis.
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Kim,G.Y., Lim,H.J., Kim,W.H. and Park,H.Y.
  TITLE     Coronin 1B regulates the TNFalpha-induced apoptosis of HUVECs by
            mediating the interaction between TRADD and FADD
  JOURNAL   Biochem Biophys Res Commun 526 (4), 999-1004 (2020)
   PUBMED   32303335
  REMARK    GeneRIF: Coronin 1B regulates the TNFalpha-induced apoptosis of
            HUVECs by mediating the interaction between TRADD and FADD.
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Cai,L., Marshall,T.W., Uetrecht,A.C., Schafer,D.A. and Bear,J.E.
  TITLE     Coronin 1B coordinates Arp2/3 complex and cofilin activities at the
            leading edge
  JOURNAL   Cell 128 (5), 915-929 (2007)
   PUBMED   17350576
  REMARK    GeneRIF: Study concludes that Coronin 1B's coordination of filament
            formation by Arp2/3 complex and filament turnover by Cofilin is
            required for effective lamellipodial protrusion and cell migration.
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Cai,L., Holoweckyj,N., Schaller,M.D. and Bear,J.E.
  TITLE     Phosphorylation of coronin 1B by protein kinase C regulates
            interaction with Arp2/3 and cell motility
  JOURNAL   J Biol Chem 280 (36), 31913-31923 (2005)
   PUBMED   16027158
  REMARK    GeneRIF: Coronin 1B regulates leading edge dynamics and controls
            cell motility and interactions with the actin-related protein
            (Arp)2/3 complex
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Gatfield,J., Albrecht,I., Zanolari,B., Steinmetz,M.O. and
            Pieters,J.
  TITLE     Association of the leukocyte plasma membrane with the actin
            cytoskeleton through coiled coil-mediated trimeric coronin 1
            molecules
  JOURNAL   Mol Biol Cell 16 (6), 2786-2798 (2005)
   PUBMED   15800061
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Parente,J.A. Jr., Chen,X., Zhou,C., Petropoulos,A.C. and Chew,C.S.
  TITLE     Isolation, cloning, and characterization of a new mammalian coronin
            family member, coroninse, which is regulated within the protein
            kinase C signaling pathway
  JOURNAL   J Biol Chem 274 (5), 3017-3025 (1999)
   PUBMED   9915840
  REMARK    GeneRIF: In rabbits, cholinergic stimulation increases the
            phosphorylation of coronin 1B in gastric mucosal cells
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Okumura,M., Kung,C., Wong,S., Rodgers,M. and Thomas,M.L.
  TITLE     Definition of family of coronin-related proteins conserved between
            humans and mice: close genetic linkage between coronin-2 and
            CD45-associated protein
  JOURNAL   DNA Cell Biol 17 (9), 779-787 (1998)
   PUBMED   9778037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003419.3 and BC006449.1.
            
            Summary: Members of the coronin family, such as CORO1B, are WD
            repeat-containing actin-binding proteins that regulate cell
            motility (Cai et al., 2005 [PubMed 16027158]).[supplied by OMIM,
            Mar 2008].
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 2. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1134815.1, AK000860.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341356.10/ ENSP00000340211.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..489
                     /product="coronin-1B"
                     /note="coronin, actin binding protein, 1B"
                     /calculated_mol_wt=54104
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:16027158; propagated from
                     UniProtKB/Swiss-Prot (Q9BR76.1)"
     Region          10..485
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          18..72
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR76.1)"
     Region          38..80
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          73..122
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR76.1)"
     Region          86..130
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          123..166
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR76.1)"
     Region          135..172
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          167..210
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR76.1)"
     Region          180..215
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          211..256
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR76.1)"
     Region          223..263
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          257..296
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR76.1)"
     Region          270..311
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          408..444
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BR76.1)"
     CDS             1..489
                     /gene="CORO1B"
                     /gene_synonym="CORONIN-2"
                     /coded_by="NM_020441.3:76..1545"
                     /db_xref="CCDS:CCDS8164.1"
                     /db_xref="GeneID:57175"
                     /db_xref="HGNC:HGNC:2253"
                     /db_xref="MIM:609849"
ORIGIN      
        1 msfrkvvrqs kfrhvfgqpv kndqcyedir vsrvtwdstf cavnpkflav iveasgggaf
       61 lvlplsktgr idkayptvcg htgpvldidw cphndevias gsedctvmvw qipengltsp
      121 ltepvvvleg htkrvgiiaw hptarnvlls agcdnvvliw nvgtaeelyr ldslhpdliy
      181 nvswnhngsl fcsackdksv riidprrgtl vaerekaheg arpmraifla dgkvfttgfs
      241 rmserqlalw dpenleepma lqeldssnga llpfydpdts vvyvcgkgds siryfeitee
      301 ppyihflntf tskepqrgmg smpkrglevs kceiarfykl herkcepivm tvprksdlfq
      361 ddlypdtagp eaaleaeewv sgrdadpili slreayvpsk qrdlkisrrn vlsdsrpama
      421 pgsshlgapa stttaadatp sgslaragea gkleevmqel ralralvkeq gdricrleeq
      481 lgrmengda
//
LOCUS       NP_077178                284 aa            linear   ROD 27-APR-2025
DEFINITION  GPN-loop GTPase 3 [Mus musculus].
ACCESSION   NP_077178
VERSION     NP_077178.1
DBSOURCE    REFSEQ: accession NM_024216.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113285.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC003341.1, AK080720.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 62.33 cM"
     Protein         1..284
                     /product="GPN-loop GTPase 3"
                     /note="protein x 0004; ATP-binding domain 1 family member
                     C"
                     /calculated_mol_wt=32659
     Region          4..249
                     /region_name="GPN3"
                     /note="GPN-loop GTPase 3; cd17872"
                     /db_xref="CDD:349781"
     Site            order(11..18,174..175,177..178,234..236)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:349781"
     Region          72..74
                     /region_name="Gly-Pro-Asn (GPN)-loop, involved in dimer
                     interface. /evidence=ECO:0000250|UniProtKB:Q9UYR9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D3W4.1)"
     Site            74
                     /site_type="other"
                     /note="Stabilizes the phosphate intermediate, shared with
                     dimeric partner. /evidence=ECO:0000250|UniProtKB:Q9UYR9;
                     propagated from UniProtKB/Swiss-Prot (Q9D3W4.1)"
     Region          262..284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D3W4.1)"
     CDS             1..284
                     /gene="Gpn3"
                     /gene_synonym="A930018B01Rik; Atpbd1c; D5Ertd708e"
                     /coded_by="NM_024216.2:102..956"
                     /db_xref="CCDS:CCDS19647.1"
                     /db_xref="GeneID:68080"
                     /db_xref="MGI:MGI:1289326"
ORIGIN      
        1 mpryaqlvmg pagsgkstyc stmvqhceal nrsvqvvnld paaehfnypv madireliev
       61 ddvmedeslr fgpngglvfc meyfannfdw lenclghved dyilfdcpgq ielythlpvm
      121 kqlvqqleqw efrvcgvflv dsqfmvesfk fisgilaals amvsleipqv nimtkmdlls
      181 kkakkeiekf ldpdmyslid dstgdlrsqk fkkltkavcg lvddysmvrf lpydqsdees
      241 mnivlqhidf aiqygedlef kepreheees ssmfdeyfqe rqne
//
LOCUS       NP_055488                297 aa            linear   PRI 27-APR-2025
DEFINITION  ER membrane protein complex subunit 2 isoform 2 [Homo sapiens].
ACCESSION   NP_055488
VERSION     NP_055488.1
DBSOURCE    REFSEQ: accession NM_014673.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Pleiner,T., Hazu,M., Tomaleri,G.P., Januszyk,K., Oania,R.S.,
            Sweredoski,M.J., Moradian,A., Guna,A. and Voorhees,R.M.
  TITLE     WNK1 is an assembly factor for the human ER membrane protein
            complex
  JOURNAL   Mol Cell 81 (13), 2693-2704 (2021)
   PUBMED   33964204
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Pleiner,T., Tomaleri,G.P., Januszyk,K., Inglis,A.J., Hazu,M. and
            Voorhees,R.M.
  TITLE     Structural basis for membrane insertion by the human ER membrane
            protein complex
  JOURNAL   Science 369 (6502), 433-436 (2020)
   PUBMED   32439656
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Guna,A., Volkmar,N., Christianson,J.C. and Hegde,R.S.
  TITLE     The ER membrane protein complex is a transmembrane domain insertase
  JOURNAL   Science 359 (6374), 470-473 (2018)
   PUBMED   29242231
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 297)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   9  (residues 1 to 297)
  AUTHORS   Ma,H., Dang,Y., Wu,Y., Jia,G., Anaya,E., Zhang,J., Abraham,S.,
            Choi,J.G., Shi,G., Qi,L., Manjunath,N. and Wu,H.
  TITLE     A CRISPR-Based Screen Identifies Genes Essential for
            West-Nile-Virus-Induced Cell Death
  JOURNAL   Cell Rep 12 (4), 673-683 (2015)
   PUBMED   26190106
REFERENCE   10 (residues 1 to 297)
  AUTHORS   Christianson,J.C., Olzmann,J.A., Shaler,T.A., Sowa,M.E.,
            Bennett,E.J., Richter,C.M., Tyler,R.E., Greenblatt,E.J.,
            Harper,J.W. and Kopito,R.R.
  TITLE     Defining human ERAD networks through an integrative mapping
            strategy
  JOURNAL   Nat Cell Biol 14 (1), 93-105 (2011)
   PUBMED   22119785
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC021667.1 and AC022634.8.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.64161.1,
                                           SRR1660807.119227.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000220853.8/ ENSP00000220853.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q23.1"
     Protein         1..297
                     /product="ER membrane protein complex subunit 2 isoform 2"
                     /note="tetratricopeptide repeat protein 35; TPR repeat
                     protein 35; tetratricopeptide repeat domain 35"
                     /calculated_mol_wt=34703
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q15006.1)"
     Region          55..>235
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          87..120
                     /region_name="TPR 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15006.1)"
     Site            order(95..96,98,122,125..126,129..130,132..133,156,
                     159..160,163..164,167)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          120..150
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          155..188
                     /region_name="TPR 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15006.1)"
     Region          155..182
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          188..221
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          192..225
                     /region_name="TPR 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15006.1)"
     Site            255
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15006.1)"
     CDS             1..297
                     /gene="EMC2"
                     /gene_synonym="KIAA0103; TTC35"
                     /coded_by="NM_014673.5:36..929"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6309.1"
                     /db_xref="GeneID:9694"
                     /db_xref="HGNC:HGNC:28963"
                     /db_xref="MIM:607722"
ORIGIN      
        1 makvselydv tweemrdkmr kwreensrns eqivevgeel ineyasklgd diwiiyeqvm
       61 iaaldygrdd lalfclqelr rqfpgshrvk rltgmrfeam eryddaiqly drilqedptn
      121 taarkrkiai rkaqgknvea irelneyleq fvgdqeawhe laelyinehd yakaafclee
      181 lmmtnphnhl ycqqyaevky tqgglenlel srkyfaqalk lnnrnmralf glymsashia
      241 snpkasaktk kdnmkyaswa asqinrayqf agrskketky slkavedmle tlqitqs
//
LOCUS       NP_068735                446 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 70 [Homo sapiens].
ACCESSION   NP_068735 NP_852101
VERSION     NP_068735.1
DBSOURCE    REFSEQ: accession NM_021916.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Zhang,Z., Li,M., Tai,Y., Xing,Y., Zuo,H., Jin,X. and Ma,J.
  TITLE     ZNF70 regulates IL-1beta secretion of macrophages to promote the
            proliferation of HCT116 cells via activation of NLRP3 inflammasome
            and STAT3 pathway in colitis-associated colorectal cancer
  JOURNAL   Cell Signal 114, 110979 (2024)
   PUBMED   38000525
  REMARK    GeneRIF: ZNF70 regulates IL-1beta secretion of macrophages to
            promote the proliferation of HCT116 cells via activation of NLRP3
            inflammasome and STAT3 pathway in colitis-associated colorectal
            cancer.
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Han,G.L., Wang,J., Guo,K., Chen,J.K., Shang,R.X. and Jiang,T.
  TITLE     miRNA-574-5p downregulates ZNF70 and influences the progression of
            human esophageal squamous cell carcinoma through reactive oxygen
            species generation and MAPK pathway activation
  JOURNAL   Anticancer Drugs 31 (3), 282-291 (2020)
   PUBMED   32053575
  REMARK    GeneRIF: miRNA-574-5p downregulates ZNF70 and influences the
            progression of human esophageal squamous cell carcinoma through
            reactive oxygen species generation and MAPK pathway activation.
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Watanabe,K., Nakayama,K., Ohta,S., Tago,K., Boonvisut,S.,
            Millings,E.J., Fischer,S.G., LeDuc,C.A., Leibel,R.L. and Iwamoto,S.
  TITLE     ZNF70, a novel ILDR2-interacting protein, contributes to the
            regulation of HES1 gene expression
  JOURNAL   Biochem Biophys Res Commun 477 (4), 712-716 (2016)
   PUBMED   27353377
  REMARK    GeneRIF: We demonstrated that ZNF70 interacts with ZFP64 and
            activates HES1 transcription by binding to the HES1 promoter. In
            addition, HES1 gene expression is increased in ILDR2-knockdown
            HepG2 cells, in which ZNF70 is translocated from the cytoplasm to
            the nucleus, suggesting that ZNF70 migration to the nucleus after
            dissociating from the ILDR2-ZNF70 complex activates HES1
            transcription. These results support a novel link betwee
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Aubry,M., Marineau,C., Zhang,F.R., Zahed,L., Figlewicz,D.,
            Delattre,O., Thomas,G., de Jong,P.J., Julien,J.P. and Rouleau,G.A.
  TITLE     Cloning of six new genes with zinc finger motifs mapping to short
            and long arms of human acrocentric chromosome 22 (p and q11.2)
  JOURNAL   Genomics 13 (3), 641-648 (1992)
   PUBMED   1639391
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP000348.1, BC040161.1 and AK122721.1.
            
            On Jun 19, 2003 this sequence version replaced NP_852101.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040161.1, SRR1803612.243713.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341976.5/ ENSP00000339314.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.23"
     Protein         1..446
                     /product="zinc finger protein 70"
                     /note="zinc finger protein N27C7-1"
                     /calculated_mol_wt=50671
     Region          92..108
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          114..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UC06.2)"
     Region          138..442
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(147,149,151,153..154,157..158,161,175,177,181..182,
                     185..186,189,203,205,207,209..210,213..214,217)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(315,317,319,321..322,325..326,329,343,345,349..350,
                     353..354,357,371,373,375,377..378,381..382,385)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..413
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          421..441
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..446
                     /gene="ZNF70"
                     /gene_synonym="Cos17"
                     /coded_by="NM_021916.4:482..1822"
                     /db_xref="CCDS:CCDS13812.1"
                     /db_xref="GeneID:7621"
                     /db_xref="HGNC:HGNC:13140"
                     /db_xref="MIM:194544"
ORIGIN      
        1 mevppatkfg etfafenrle sqqglfpged lgdpflqerg leqmaviyke iplgeqdeen
       61 ddyegnfslc sspvqhqsip pgtrpqddel fgqtflqksd lsmcqiihse epspcdcaet
      121 drgdsgpnap hrtpqpakpy acrecgkafs qsshllrhlv ihtgekpyec cecgkafsqs
      181 shllrhqiih tgekpyecre cgkafrqssa ltqhqkihtg krpyecrecg kdfsrssslr
      241 kherihtger pyqckecgks fnqssglsqh rkihtlkkph ecdlcgkafc hrshlirhqr
      301 ihtgkkpykc decgkafsqs snliehrkth tgekpykcqk cgkafsqsss liehqrihtg
      361 ekpyeccqcg kafchssali qhqrihtgkk pytcecgkaf rhrsaliehy kthtrekpyv
      421 cnlcgksfrg sshlirhqki hsgekl
//
LOCUS       NP_057041                242 aa            linear   PRI 27-APR-2025
DEFINITION  methylthioribulose-1-phosphate dehydratase [Homo sapiens].
ACCESSION   NP_057041
VERSION     NP_057041.2
DBSOURCE    REFSEQ: accession NM_015957.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Li,J., Wang,R., Li,M., Zhang,Z., Jin,S. and Ma,H.
  TITLE     APIP regulated by YAP propels methionine cycle and metastasis in
            head and neck squamous cell carcinoma
  JOURNAL   Cancer Lett 588, 216756 (2024)
   PUBMED   38423248
  REMARK    GeneRIF: APIP regulated by YAP propels methionine cycle and
            metastasis in head and neck squamous cell carcinoma.
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Moravcikova,E., Krepela,E., Prochazka,J., Rousalova,I., Cermak,J.
            and Benkova,K.
  TITLE     Down-regulated expression of apoptosis-associated genes APIP and
            UACA in non-small cell lung carcinoma
  JOURNAL   Int J Oncol 40 (6), 2111-2121 (2012)
   PUBMED   22407486
  REMARK    GeneRIF: The down-regulation of APIP and UACA expression suggests
            that the threshold to activate the apoptosome apparatus may be
            decreased in non-small cell lung cancer cells.
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Wright,F.A., Strug,L.J., Doshi,V.K., Commander,C.W., Blackman,S.M.,
            Sun,L., Berthiaume,Y., Cutler,D., Cojocaru,A., Collaco,J.M.,
            Corey,M., Dorfman,R., Goddard,K., Green,D., Kent,J.W. Jr.,
            Lange,E.M., Lee,S., Li,W., Luo,J., Mayhew,G.M., Naughton,K.M.,
            Pace,R.G., Pare,P., Rommens,J.M., Sandford,A., Stonebraker,J.R.,
            Sun,W., Taylor,C., Vanscoy,L.L., Zou,F., Blangero,J., Zielenski,J.,
            O'Neal,W.K., Drumm,M.L., Durie,P.R., Knowles,M.R. and Cutting,G.R.
  TITLE     Genome-wide association and linkage identify modifier loci of lung
            disease severity in cystic fibrosis at 11p13 and 20q13.2
  JOURNAL   Nat Genet 43 (6), 539-546 (2011)
   PUBMED   21602797
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   10 (residues 1 to 242)
  AUTHORS   Cho,D.H., Hong,Y.M., Lee,H.J., Woo,H.N., Pyo,J.O., Mak,T.W. and
            Jung,Y.K.
  TITLE     Induced inhibition of ischemic/hypoxic injury by APIP, a novel
            Apaf-1-interacting protein
  JOURNAL   J Biol Chem 279 (38), 39942-39950 (2004)
   PUBMED   15262985
  REMARK    GeneRIF: APIP functions to inhibit muscle ischemic damage by
            binding to Apaf-1 in the Apaf-1/caspase-9 apoptosis pathway.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC107928.3, BP200131.1, BC009077.1 and AF088034.1.
            
            On Jan 30, 2008 this sequence version replaced NP_057041.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.129302.1,
                                           SRR5189667.244568.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395787.4/ ENSP00000379133.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..242
                     /product="methylthioribulose-1-phosphate dehydratase"
                     /EC_number="4.2.1.109"
                     /note="probable methylthioribulose-1-phosphate
                     dehydratase; MTRu-1-P dehydratase"
                     /calculated_mol_wt=26994
     Region          28..227
                     /region_name="salvage_mtnB"
                     /note="methylthioribulose-1-phosphate dehydratase;
                     TIGR03328"
                     /db_xref="CDD:274521"
     Site            order(30,34,42,64,66..67,117,119..120,125..127,136,
                     138..139,166,194,205,212,216,223)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(47,61..62,89,96..97,115,117,195)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96GX9.1)"
     Site            order(115,117,195)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     CDS             1..242
                     /gene="APIP"
                     /gene_synonym="APIP2; CGI-29; CGI29; hAPIP; MMRP19"
                     /coded_by="NM_015957.4:96..824"
                     /db_xref="CCDS:CCDS7895.1"
                     /db_xref="GeneID:51074"
                     /db_xref="HGNC:HGNC:17581"
                     /db_xref="MIM:612491"
ORIGIN      
        1 msgcdaregd ccsrrcgaqd kehprylipe lckqfyhlgw vtgtgggisl khgdeiyiap
       61 sgvqkeriqp edmfvcdine kdisgpspsk klkksqctpl fmnaytmrga gavihthska
      121 avmatllfpg refkithqem ikgikkctsg gyyryddmlv vpiientpee kdlkdrmaha
      181 mneypdscav lvrrhgvyvw getwekaktm cecydylfdi avsmkkvgld psqlpvgeng
      241 iv
//
LOCUS       NP_001138846             261 aa            linear   PRI 27-APR-2025
DEFINITION  DNA oxidative demethylase ALKBH2 isoform 1 [Homo sapiens].
ACCESSION   NP_001138846
VERSION     NP_001138846.1
DBSOURCE    REFSEQ: accession NM_001145374.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Davletgildeeva,A.T., Tyugashev,T.E., Zhao,M., Kuznetsov,N.A.,
            Ishchenko,A.A., Saparbaev,M. and Kuznetsova,A.A.
  TITLE     Individual Contributions of Amido Acid Residues Tyr122, Ile168, and
            Asp173 to the Activity and Substrate Specificity of Human DNA
            Dioxygenase ABH2
  JOURNAL   Cells 12 (14), 1839 (2023)
   PUBMED   37508504
  REMARK    GeneRIF: Individual Contributions of Amido Acid Residues Tyr122,
            Ile168, and Asp173 to the Activity and Substrate Specificity of
            Human DNA Dioxygenase ABH2.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Kanazhevskaya,L.Y., Smyshliaev,D.A., Timofeyeva,N.A.,
            Ishchenko,A.A., Saparbaev,M., Kuznetsov,N.A. and Fedorova,O.S.
  TITLE     Conformational Dynamics of Human ALKBH2 Dioxygenase in the Course
            of DNA Repair as Revealed by Stopped-Flow Fluorescence Spectroscopy
  JOURNAL   Molecules 27 (15), 4960 (2022)
   PUBMED   35956910
  REMARK    GeneRIF: Conformational Dynamics of Human ALKBH2 Dioxygenase in the
            Course of DNA Repair as Revealed by Stopped-Flow Fluorescence
            Spectroscopy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Ke,B., Ye,K. and Cheng,S.
  TITLE     ALKBH2 inhibition alleviates malignancy in colorectal cancer by
            regulating BMI1-mediated activation of NF-kappaB pathway
  JOURNAL   World J Surg Oncol 18 (1), 328 (2020)
   PUBMED   33302959
  REMARK    GeneRIF: ALKBH2 inhibition alleviates malignancy in colorectal
            cancer by regulating BMI1-mediated activation of NF-kappaB pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Lenz,S.A.P., Li,D. and Wetmore,S.D.
  TITLE     Insights into the Direct Oxidative Repair of Etheno Lesions: MD and
            QM/MM Study on the Substrate Scope of ALKBH2 and AlkB
  JOURNAL   DNA Repair (Amst) 96, 102944 (2020)
   PUBMED   33161373
  REMARK    GeneRIF: Insights into the Direct Oxidative Repair of Etheno
            Lesions: MD and QM/MM Study on the Substrate Scope of ALKBH2 and
            AlkB.
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Yang,C.G., Yi,C., Duguid,E.M., Sullivan,C.T., Jian,X., Rice,P.A.
            and He,C.
  TITLE     Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to
            dsDNA
  JOURNAL   Nature 452 (7190), 961-965 (2008)
   PUBMED   18432238
  REMARK    GeneRIF: first crystal structure of ABH2
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Bethke,L., Murray,A., Webb,E., Schoemaker,M., Muir,K., McKinney,P.,
            Hepworth,S., Dimitropoulou,P., Lophatananon,A., Feychting,M.,
            Lonn,S., Ahlbom,A., Malmer,B., Henriksson,R., Auvinen,A., Kiuru,A.,
            Salminen,T., Johansen,C., Christensen,H.C., Kosteljanetz,M.,
            Swerdlow,A. and Houlston,R.
  TITLE     Comprehensive analysis of DNA repair gene variants and risk of
            meningioma
  JOURNAL   J Natl Cancer Inst 100 (4), 270-276 (2008)
   PUBMED   18270339
  REMARK    GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Lee,D.H., Jin,S.G., Cai,S., Chen,Y., Pfeifer,G.P. and O'Connor,T.R.
  TITLE     Repair of methylation damage in DNA and RNA by mammalian AlkB
            homologues
  JOURNAL   J Biol Chem 280 (47), 39448-39459 (2005)
   PUBMED   16174769
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Aas,P.A., Otterlei,M., Falnes,P.O., Vagbo,C.B., Skorpen,F.,
            Akbari,M., Sundheim,O., Bjoras,M., Slupphaug,G., Seeberg,E. and
            Krokan,H.E.
  TITLE     Human and bacterial oxidative demethylases repair alkylation damage
            in both RNA and DNA
  JOURNAL   Nature 421 (6925), 859-863 (2003)
   PUBMED   12594517
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Duncan,T., Trewick,S.C., Koivisto,P., Bates,P.A., Lindahl,T. and
            Sedgwick,B.
  TITLE     Reversal of DNA alkylation damage by two human dioxygenases
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16660-16665 (2002)
   PUBMED   12486230
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA182735.1, BM820131.1, AC011596.27 and AI278638.1.
            
            Summary: The Escherichia coli AlkB protein protects against the
            cytotoxicity of methylating agents by repair of the specific DNA
            lesions generated in single-stranded DNA. ALKBH2 and ALKBH3 (MIM
            610603) are E. coli AlkB homologs that catalyze the removal of
            1-methyladenine and 3-methylcytosine (Duncan et al., 2002 [PubMed
            12486230]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1-3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.570673.1,
                                           SRR1660803.6962.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000429722.3/ ENSP00000398181.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..261
                     /product="DNA oxidative demethylase ALKBH2 isoform 1"
                     /EC_number="1.14.11.33"
                     /note="alpha-ketoglutarate-dependent dioxygenase alkB
                     homolog 2; alkylated DNA repair protein alkB homolog 2;
                     2OG-Fe(II) oxy DC1; DNA oxidative demethylase ALKBH2;
                     alkB, alkylation repair homolog 2"
                     /calculated_mol_wt=29191
     Region          1..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NS38.1)"
     Region          3..7
                     /region_name="PCNA-binding.
                     /evidence=ECO:0000269|PubMed:19736315"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NS38.1)"
     Region          72..256
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
     CDS             1..261
                     /gene="ALKBH2"
                     /gene_synonym="ABH2"
                     /coded_by="NM_001145374.2:378..1163"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31897.1"
                     /db_xref="GeneID:121642"
                     /db_xref="HGNC:HGNC:32487"
                     /db_xref="MIM:610602"
ORIGIN      
        1 mdrflvkgaq ggllrkqeeq eptgeepavl ggdkestrkr prreapgngg hsagpswrhi
       61 raegldcsyt vlfgkaeade ifqelekeve yftgalarvq vfgkwhsvpr kqatygdagl
      121 tytfsgltls pkpwipvler irdhvsgvtg qtfnfvlinr ykdgcdhige hrdderelap
      181 gspiasvsfg acrdfvfrhk dsrgkspsrr vavvrlplah gsllmmnhpt nthwyhslpv
      241 rkkvlaprvn ltfrkilltk k
//
LOCUS       NP_001002909            1502 aa            linear   PRI 27-APR-2025
DEFINITION  G patch domain-containing protein 8 isoform 1 [Homo sapiens].
ACCESSION   NP_001002909 XP_290758
VERSION     NP_001002909.1
DBSOURCE    REFSEQ: accession NM_001002909.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1502)
  AUTHORS   Benbarche,S., Pineda,J.M.B., Galvis,L.B., Biswas,J., Liu,B.,
            Wang,E., Zhang,Q., Hogg,S.J., Lyttle,K., Dahi,A., Lewis,A.M.,
            Sarchi,M., Rahman,J., Fox,N., Ai,Y., Mehta,S., Garippa,R.,
            Ortiz-Pacheco,J., Li,Z., Monetti,M., Stanley,R.F., Doulatov,S.,
            Bradley,R.K. and Abdel-Wahab,O.
  TITLE     GPATCH8 modulates mutant SF3B1 mis-splicing and pathogenicity in
            hematologic malignancies
  JOURNAL   Mol Cell 84 (10), 1886-1903 (2024)
   PUBMED   38688280
  REMARK    GeneRIF: GPATCH8 modulates mutant SF3B1 mis-splicing and
            pathogenicity in hematologic malignancies.
REFERENCE   2  (residues 1 to 1502)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   3  (residues 1 to 1502)
  AUTHORS   Kaneko,H., Kitoh,H., Matsuura,T., Masuda,A., Ito,M., Mottes,M.,
            Rauch,F., Ishiguro,N. and Ohno,K.
  TITLE     Hyperuricemia cosegregating with osteogenesis imperfecta is
            associated with a mutation in GPATCH8
  JOURNAL   Hum Genet 130 (5), 671-683 (2011)
   PUBMED   21594610
  REMARK    GeneRIF: Two missense single-nucleotide variants in ZPBP2 and
            GPATCH8 on chromosome 17 were identified that cosegregated with
            hyperuricemia in the Japanese family.
REFERENCE   4  (residues 1 to 1502)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   5  (residues 1 to 1502)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 1502)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   7  (residues 1 to 1502)
  AUTHORS   Thornton,M.A., Poncz,M., Korostishevsky,M., Yakobson,E., Usher,S.,
            Seligsohn,U. and Peretz,H.
  TITLE     The human platelet alphaIIb gene is not closely linked to its
            integrin partner beta3
  JOURNAL   Blood 94 (6), 2039-2047 (1999)
   PUBMED   10477733
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY048299.1, AK025600.1,
            BC136629.1 and BC024147.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 30, 2004 this sequence version replaced XP_290758.5.
            
            Summary: The protein encoded by this gene contains an
            RNA-processing domain, a zinc finger domain, a lysine-rich region
            and a serine-rich region. A mutation in the serine-rich region of
            the protein is thought to be associated with hyperuricemia (PMID:
            21594610). Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Feb
            2015].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.12881.1,
                                           SRR1660805.222318.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000591680.6/ ENSP00000467556.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1502
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1502
                     /product="G patch domain-containing protein 8 isoform 1"
                     /note="g patch domain-containing protein 8"
                     /calculated_mol_wt=164067
     Region          40..82
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     Region          <82..>207
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Region          136..163
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          172..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          323..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          419..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            479
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          579..1301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            911
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1009
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          <1056..1316
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            1081
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     CDS             1..1502
                     /gene="GPATCH8"
                     /gene_synonym="GPATC8; KIAA0553"
                     /coded_by="NM_001002909.4:37..4545"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32666.1"
                     /db_xref="GeneID:23131"
                     /db_xref="HGNC:HGNC:29066"
                     /db_xref="MIM:614396"
ORIGIN      
        1 madrfsrfne drdfqgnhfd qyeeghleie qasldkpies dnighrllqk hgwklgqglg
       61 kslqgrtdpi pivvkydvmg mgrmemeldy aedaterrrv levekedtee lrqkykdyvd
      121 kekaiakale dlranfycel cdkqyqkhqe fdnhinsydh ahkqrlkdlk qrefarnvss
      181 rsrkdekkqe kalrrlhela eqrkqaecap gsgpmfkptt vavdeegged dkdesatnsg
      241 tgatascglg sefstdkggp ftavqitntt glaqapglas qgisfgiknn lgtplqklgv
      301 sfsfakkapv klesiasvfk dhaeegtsed gtkpdekssd qglqkvgdsd gssnldgkke
      361 dedpqdggsl astlsklkrm kreegagate peyyhyippa hckvkpnfpf llfmraseqm
      421 dgdntthpkn apeskkgssp kpkscikaaa sqgaektvse vseqpketsm tepsepgska
      481 eakkalggdv sdqsleshsq kvsetqmces nssketslat pagkesqegp khptgpffpv
      541 lskdestalq wpselliftk aepsisyscn plyfdfklsr nkdartkgte kpkdigsssk
      601 dhlqgldpge pnkskevgge kivrssggrm dapasgsacs glnkqepggs hgsetedtgr
      661 slpskkersg kshrhkkkkk hkksskhkrk hkadteekss kaesgekskk rkkrkrkknk
      721 ssapadserg pkpeppgsgs papprrrrra qddsqrrslp aeegssgkkd eggggsssqd
      781 hggrkhkgel ppsscqrrag tkrssrsshr sqpssgdeds ddasshrlhq kspsqyseee
      841 eeedsgsehs rsrsrsgrrh sshrssrrsy ssssdassdq scysrqrsys ddsysdysdr
      901 srrhskrshd sddsdyassk hrskrhkyss sdddyslscs qsrsrsrsht rersrsrgrs
      961 rssscsrsrs krrsrsttah swqrsrsysr drsrstrsps qrsgsrkrsw ghespeerhs
     1021 grrdfirski yrsqsphyfr sgrgegpgkk ddgrgddska tgppsqnsni gtgrgsegdc
     1081 spedknsvta klllekiqsr kverkpsvse evqatpnkag pklkdppqgy fgpklppslg
     1141 nkpvlpligk lpatrkpnkk ceesglerge eqeqseteeg ppgssdalfg hqfpseettg
     1201 plldpppees ksgeatadhp vaplgtpahs dcypgdptis hnylpdpsdg dtlesldsss
     1261 qpgpvessll piapdlehfp syappsgdps iestdgaeda slaplesqpi tftpeemeky
     1321 sklqqaaqqh iqqqllakqv kafpasaala patpalqpih iqqpatasat sittvqhail
     1381 qhhaaaaaaa igihphphpq plaqvhhipq phltpislsh lthsiipghp atflashpih
     1441 iipasaihpg pftfhpvpha alyptllapr paaaaatalh lhpllhpifs gqdlqhppsh
     1501 gt
//
LOCUS       NP_071910                585 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein Eos isoform a [Homo sapiens].
ACCESSION   NP_071910
VERSION     NP_071910.3
DBSOURCE    REFSEQ: accession NM_022465.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Miao,Y., Qi,S., Hu,R., Sheng,Y. and Yang,Q.
  TITLE     Association analysis of the IKZF4 gene with Alopecia Areata in the
            Chinese Han population
  JOURNAL   Altern Ther Health Med 30 (10), 314-317 (2024)
   PUBMED   38330583
  REMARK    GeneRIF: Association analysis of the IKZF4 gene with Alopecia
            Areata in the Chinese Han population.
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Weng,N., Zhou,C., Zhou,Y., Zhong,Y., Jia,Z., Rao,X., Qiu,H.,
            Zeng,G., Jin,X., Zhang,J., Zhuang,Z., Liang,Z., Deng,Y., Li,Q.,
            Yang,S., Luo,H., Wang,H. and Wu,X.
  TITLE     IKZF4/NONO-RAB11FIP3 axis promotes immune evasion in gastric cancer
            via facilitating PD-L1 endosome recycling
  JOURNAL   Cancer Lett 584, 216618 (2024)
   PUBMED   38211652
  REMARK    GeneRIF: IKZF4/NONO-RAB11FIP3 axis promotes immune evasion in
            gastric cancer via facilitating PD-L1 endosome recycling.
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Wang,Y., Zhao,H., He,Y., Zhang,P., Zeng,C., Du,T., Shen,Q., Chen,Y.
            and Zhao,S.
  TITLE     IKZF4 acts as a novel tumor suppressor in non-small cell lung
            cancer by suppressing Notch signaling pathway
  JOURNAL   Cell Signal 107, 110679 (2023)
   PUBMED   37044192
  REMARK    GeneRIF: IKZF4 acts as a novel tumor suppressor in non-small cell
            lung cancer by suppressing Notch signaling pathway.
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Vandewalle,J., Van der Auwera,B.J., Amin,H., Quartier,E.,
            Desouter,A.K., Tenoutasse,S., Gillard,P., De Block,C.,
            Keymeulen,B., Gorus,F.K. and Van de Casteele,M.
  CONSRTM   Belgian Diabetes Registry
  TITLE     Genetic variation at ERBB3/IKZF4 and sexual dimorphism in epitope
            spreading in single autoantibody-positive relatives
  JOURNAL   Diabetologia 64 (11), 2511-2516 (2021)
   PUBMED   34448034
  REMARK    GeneRIF: Genetic variation at ERBB3/IKZF4 and sexual dimorphism in
            epitope spreading in single autoantibody-positive relatives.
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 585)
  AUTHORS   Westman,B.J., Perdomo,J., Matthews,J.M., Crossley,M. and
            Mackay,J.P.
  TITLE     Structural studies on a protein-binding zinc-finger domain of Eos
            reveal both similarities and differences to classical zinc fingers
  JOURNAL   Biochemistry 43 (42), 13318-13327 (2004)
   PUBMED   15491138
REFERENCE   7  (residues 1 to 585)
  AUTHORS   Perdomo,J. and Crossley,M.
  TITLE     The Ikaros family protein Eos associates with C-terminal-binding
            protein corepressors
  JOURNAL   Eur J Biochem 269 (23), 5885-5892 (2002)
   PUBMED   12444977
REFERENCE   8  (residues 1 to 585)
  AUTHORS   Koipally,J. and Georgopoulos,K.
  TITLE     A molecular dissection of the repression circuitry of Ikaros
  JOURNAL   J Biol Chem 277 (31), 27697-27705 (2002)
   PUBMED   12015313
REFERENCE   9  (residues 1 to 585)
  AUTHORS   Perdomo,J., Holmes,M., Chong,B. and Crossley,M.
  TITLE     Eos and pegasus, two members of the Ikaros family of proteins with
            distinct DNA binding activities
  JOURNAL   J Biol Chem 275 (49), 38347-38354 (2000)
   PUBMED   10978333
REFERENCE   10 (residues 1 to 585)
  AUTHORS   Honma,Y., Kiyosawa,H., Mori,T., Oguri,A., Nikaido,T., Kanazawa,K.,
            Tojo,M., Takeda,J., Tanno,Y., Yokoya,S., Kawabata,I., Ikeda,H. and
            Wanaka,A.
  TITLE     Eos: a novel member of the Ikaros gene family expressed
            predominantly in the developing nervous system
  JOURNAL   FEBS Lett 447 (1), 76-80 (1999)
   PUBMED   10218586
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC034102.32, DA797441.1 and BX647761.1.
            
            On Jan 17, 2007 this sequence version replaced NP_071910.2.
            
            Summary: Members of the Ikaros (ZNFN1A1; MIM 603023) family of
            transcription factors, which includes Eos, are expressed in
            lymphocytes and are implicated in the control of lymphoid
            development.[supplied by OMIM, Jul 2002].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a). Variants 1 and 2
            both encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BX647761.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1966682, SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000547167.6/ ENSP00000448419.1
            RefSeq Select criteria    :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..585
                     /product="zinc finger protein Eos isoform a"
                     /note="zinc finger transcription factor Eos; zinc finger
                     protein, subfamily 1A, 4 (Eos); zinc finger protein Eos;
                     ikaros family zinc finger protein 4"
                     /calculated_mol_wt=63975
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Region          68..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKS7; propagated from
                     UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Region          161..181
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(166,168,170,172..173,176..177,180,194,196,200..201,
                     204..205,208,222,224,226,228..229,232..233,236)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          174..198
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          189..209
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          201..226
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          <211..271
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          250..271
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          281..585
                     /region_name="Interaction with FOXP3.
                     /evidence=ECO:0000250|UniProtKB:Q8C208"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Site            335
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKS7; propagated from
                     UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Region          410..489
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S9.2)"
     Region          425..429
                     /region_name="CTBP-binding motif PEDLA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S9.2)"
     CDS             1..585
                     /gene="IKZF4"
                     /gene_synonym="EOS; ZNFN1A4"
                     /coded_by="NM_022465.4:452..2209"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44917.1"
                     /db_xref="GeneID:64375"
                     /db_xref="HGNC:HGNC:13179"
                     /db_xref="MIM:606239"
ORIGIN      
        1 mhtppalprr fqgggrvrtp gshrqgkdnl erdpsggcvp dflpqaqdsn hfimeslfce
       61 ssgdssleke flgapvgpsv stpnsqhssp srslsansik vemysdeess rllgpderll
      121 ekddsvived slseplgycd gsgpephspg girlpngklk cdvcgmvcig pnvlmvhkrs
      181 htgerpfhcn qcgasftqkg nllrhiklhs gekpfkcpfc nyacrrrdal tghlrthsvs
      241 sptvgkpykc nycgrsykqq stleehkerc hnylqslste aqalagqpgd eirdlemvpd
      301 smlhssserp tfidrlansl tkrkrstpqk fvgekqmrfs lsdlpydvns ggyekdvelv
      361 ahhslepgfg sslafvgaeh lrplrlpptn ciseltpvis svytqmqplp grlelpgsre
      421 agegpedlad ggpllyrprg pltdpgasps ngcqdstdte snhedrvagv vslpqgpppq
      481 ppptivvgrh spayakedpk pqegllrgtp gpskevlrvv gesgepvkaf kcehcrilfl
      541 dhvmftihmg chgfrdpfec nicgyhsqdr yefsshivrg ehkvg
//
LOCUS       NP_001307466             533 aa            linear   PRI 27-APR-2025
DEFINITION  glucose-6-phosphate exchanger SLC37A1 [Homo sapiens].
ACCESSION   NP_001307466 XP_005261198
VERSION     NP_001307466.1
DBSOURCE    REFSEQ: accession NM_001320537.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Pan,C.J., Chen,S.Y., Jun,H.S., Lin,S.R., Mansfield,B.C. and
            Chou,J.Y.
  TITLE     SLC37A1 and SLC37A2 are phosphate-linked, glucose-6-phosphate
            antiporters
  JOURNAL   PLoS One 6 (9), e23157 (2011)
   PUBMED   21949678
  REMARK    GeneRIF: Data show that SLC37A1 and SLC37A2 are endoplasmic
            reticulum associated, P(i)-linked antiporters, that can transport
            glucose-6-phosphate.
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Pope,S.N. and Lee,I.R.
  TITLE     Yeast two-hybrid identification of prostatic proteins interacting
            with human sex hormone-binding globulin
  JOURNAL   J Steroid Biochem Mol Biol 94 (1-3), 203-208 (2005)
   PUBMED   15862967
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Bartoloni,L., Wattenhofer,M., Kudoh,J., Berry,A., Shibuya,K.,
            Kawasaki,K., Wang,J., Asakawa,S., Talior,I., Bonne-Tamir,B.,
            Rossier,C., Michaud,J., McCabe,E.R., Minoshima,S., Shimizu,N.,
            Scott,H.S. and Antonarakis,S.E.
  TITLE     Cloning and characterization of a putative human glycerol
            3-phosphate permease gene (SLC37A1 or G3PP) on 21q22.3: mutation
            analysis in two candidate phenotypes, DFNB10 and a glycerol kinase
            deficiency
  JOURNAL   Genomics 70 (2), 190-200 (2000)
   PUBMED   11112347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001625.1, DA755019.1,
            AF311320.1, BM550728.1 and BI912541.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 27, 2016 this sequence version replaced XP_005261198.1.
            
            Summary: The protein encoded by this gene localizes to the
            endoplasmic reticulum (ER) membrane. This protein translocates
            glucose-6-phosphate from the cytoplasm into the lumen of the ER for
            hydrolysis into glucose by another ER membrane protein. This gene
            is a member of the solute carrier 37 gene family. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and is inferred to be translated from a downstream start
            codon via ribosomal leaky scanning. Variants 1 and 2 encode the
            same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF311320.1, SRR1803612.235414.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000352133.3/ ENSP00000344648.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..533
                     /product="glucose-6-phosphate exchanger SLC37A1"
                     /note="glycerol-3-phosphate permease; glycerol-3-phosphate
                     transporter; G-3-P permease; G-3-P transporter;
                     sugar-phosphate exchange protein 1; solute carrier family
                     37 (glycerol-3-phosphate transporter), member 1; solute
                     carrier family 37 (glucose-6-phosphate transporter),
                     member 1"
                     /calculated_mol_wt=57517
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Region          21..516
                     /region_name="MFS_SLC37A1_2"
                     /note="Solute carrier family 37 members 1 and 2 of the
                     Major Facilitator Superfamily of transporters; cd17344"
                     /db_xref="CDD:340902"
     Site            order(35..36,39..40,43,114,169..170,172..174,177,197,
                     200..201,204,336,339..340,343..345,348,376,380,432..433,
                     437,441,465,468..469,472..473,476)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340902"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57057.2)"
     Site            100..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Site            157..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Site            263
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57057.2)"
     Site            304..324
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Site            334..354
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Site            366..386
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Site            394..414
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Site            423..443
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Site            466..486
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     Site            490..510
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57057.2)"
     CDS             1..533
                     /gene="SLC37A1"
                     /gene_synonym="G3PP; SPX1"
                     /coded_by="NM_001320537.2:1045..2646"
                     /db_xref="CCDS:CCDS13689.1"
                     /db_xref="GeneID:54020"
                     /db_xref="HGNC:HGNC:11024"
                     /db_xref="MIM:608094"
ORIGIN      
        1 marlpagirf iisfsrdqwy rafifiltfl lyasfhlsrk pisivkgelh kyctawdead
       61 vrfssqnrks gsaaphqlpd netdcgwapf dknnyqqllg aldysflcay avgmylsgii
      121 gerlpiryyl tfgmlasgaf talfglgyfy nihsfgfyvv tqvinglvqt tgwpsvvtcl
      181 gnwfgkgrrg limgvwnsht svgnilgsli agywvstcwg lsfvvpgaiv aamgivcflf
      241 liehpndvrc sstlvthskg yengtnrlrl qkqilksekn kpldpemqcl llsdgkgsih
      301 pnhvvilpgd ggsgtaaisf tgalkipgvi efslcllfak lvsytflfwl plyitnvdhl
      361 dakkagelst lfdvggifgg ilagvisdrl ekrastcglm lllaaptlyi fstvskmgle
      421 atiamlllsg alvsgpytli ttavsadlgt hkslkgnaha lstvtaiidg tgsvgaalgp
      481 llagllspsg wsnvfymlmf adacallfli rlihkelscp gsatgdqvpf keq
//
LOCUS       NP_001040                391 aa            linear   PRI 27-APR-2025
DEFINITION  somatostatin receptor type 1 [Homo sapiens].
ACCESSION   NP_001040
VERSION     NP_001040.1
DBSOURCE    REFSEQ: accession NM_001049.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Sagie,N., Romanov,E., Kezerle,Y., Meirovitz,A. and Sheva,K.
  TITLE     Expression Analysis of SSTR 1, 2 and 3 in Small-cell Lung Cancer
            Patients as Targets for Future Peptide Receptor Radionuclide
            Therapy
  JOURNAL   Anticancer Res 44 (9), 3807-3812 (2024)
   PUBMED   39197921
  REMARK    GeneRIF: Expression Analysis of SSTR 1, 2 and 3 in Small-cell Lung
            Cancer Patients as Targets for Future Peptide Receptor Radionuclide
            Therapy.
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Vitali,E., Piccini,S., Trivellin,G., Smiroldo,V., Lavezzi,E.,
            Zerbi,A., Pepe,G. and Lania,A.G.
  TITLE     The impact of SST2 trafficking and signaling in the treatment of
            pancreatic neuroendocrine tumors
  JOURNAL   Mol Cell Endocrinol 527, 111226 (2021)
   PUBMED   33675866
  REMARK    GeneRIF: The impact of SST2 trafficking and signaling in the
            treatment of pancreatic neuroendocrine tumors.
            Review article
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Guo,R.Y., Wang,H.M., Dong,X., Hu,Y., Li,J., Zang,Y. and Li,X.
  TITLE     Selectivity Comparison of Tumor-Imaging Probes Designed Based on
            Various Tumor-Targeting Strategies: A Proof of Concept Study
  JOURNAL   ACS Appl Bio Mater 4 (3), 2058-2065 (2021)
   PUBMED   35014332
  REMARK    GeneRIF: Selectivity Comparison of Tumor-Imaging Probes Designed
            Based on Various Tumor-Targeting Strategies: A Proof of Concept
            Study.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Soukup,J., Hornychova,H., Manethova,M., Michalova,K., Michnova,L.,
            Popovska,L., Skarkova,V., Cesak,T., Netuka,D., Ryska,A., Cap,J.,
            Hana,V., Hana,V. Jr., Krsek,M., Dvorakova,E., Krcma,M.,
            Lazurova,I., Olsovska,V., Stary,K., Vanuga,P. and Gabalec,F.
  TITLE     Predictive and prognostic significance of tumour subtype, SSTR1-5
            and e-cadherin expression in a well-defined cohort of patients with
            acromegaly
  JOURNAL   J Cell Mol Med 25 (5), 2484-2492 (2021)
   PUBMED   33491286
  REMARK    GeneRIF: Predictive and prognostic significance of tumour subtype,
            SSTR1-5 and e-cadherin expression in a well-defined cohort of
            patients with acromegaly.
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Kaemmerer,D., Schindler,R., Mussbach,F., Dahmen,U.,
            Altendorf-Hofmann,A., Dirsch,O., Sanger,J., Schulz,S. and Lupp,A.
  TITLE     Somatostatin and CXCR4 chemokine receptor expression in
            hepatocellular and cholangiocellular carcinomas: tumor capillaries
            as promising targets
  JOURNAL   BMC Cancer 17 (1), 896 (2017)
   PUBMED   29282035
  REMARK    GeneRIF: High SSTR1 expression is associated with hepatocellular
            and cholangiocellular carcinomas in tumor capillaries.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Le Romancer,M., Cherifi,Y., Levasseur,S., Laigneau,J.P.,
            Peranzi,G., Jais,P., Lewin,M.J. and Reyl-Desmars,F.
  TITLE     Messenger RNA expression of somatostatin receptor subtypes in human
            and rat gastric mucosae
  JOURNAL   Life Sci 58 (13), 1091-1098 (1996)
   PUBMED   8622562
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Fujita,T., Yamaji,Y., Sato,M., Murao,K. and Takahara,J.
  TITLE     Gene expression of somatostatin receptor subtypes, SSTR1 and SSTR2,
            in human lung cancer cell lines
  JOURNAL   Life Sci 55 (23), 1797-1806 (1994)
   PUBMED   7968260
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Kaupmann,K., Bruns,C., Hoyer,D., Seuwen,K. and Lubbert,H.
  TITLE     Distribution and second messenger coupling of four somatostatin
            receptor subtypes expressed in brain
  JOURNAL   FEBS Lett 331 (1-2), 53-59 (1993)
   PUBMED   8405411
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Yamada,Y., Stoffel,M., Espinosa,R. 3rd, Xiang,K.S., Seino,M.,
            Seino,S., Le Beau,M.M. and Bell,G.I.
  TITLE     Human somatostatin receptor genes: localization to human
            chromosomes 14, 17, and 22 and identification of simple tandem
            repeat polymorphisms
  JOURNAL   Genomics 15 (2), 449-452 (1993)
   PUBMED   8449518
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Yamada,Y., Post,S.R., Wang,K., Tager,H.S., Bell,G.I. and Seino,S.
  TITLE     Cloning and functional characterization of a family of human and
            mouse somatostatin receptors expressed in brain, gastrointestinal
            tract, and kidney
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 251-255 (1992)
   PUBMED   1346068
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL450109.3.
            
            Summary: Somatostatins are peptide hormones that regulate diverse
            cellular functions such as neurotransmission, cell proliferation,
            and endocrine signaling as well as inhibiting the release of many
            hormones and other secretory proteins. Somatostatin has two active
            forms of 14 and 28 amino acids. The biological effects of
            somatostatins are mediated by a family of G-protein coupled
            somatostatin receptors that are expressed in a tissue-specific
            manner. The protein encoded by this gene is a member of the
            superfamily of somatostatin receptors having seven transmembrane
            segments. Somatostatin receptors form homodimers and heterodimers
            with other members of the superfamily as well as with other
            G-protein coupled receptors and receptor tyrosine kinases. This
            somatostatin receptor has greater affinity for somatostatin-14 than
            -28. [provided by RefSeq, Jul 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX248780.1, AL556152.3 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267377.3/ ENSP00000267377.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q21.1"
     Protein         1..391
                     /product="somatostatin receptor type 1"
                     /calculated_mol_wt=42555
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30872.1)"
     Site            4
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30872.1)"
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30872.1)"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30872.1)"
     Site            57..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30872.1)"
     Region          59..334
                     /region_name="7tmA_SSTR1"
                     /note="somatostatin receptor type 1, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15970"
                     /db_xref="CDD:320636"
     Region          60..86
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320636"
     Region          93..119
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320636"
     Site            95..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30872.1)"
     Site            order(114,117..118,130..135,137..138,141,186,188..192,220,
                     223..225,227..229,231..232,284,287..288,290..291,294,
                     301..302,304..306,309,312..313)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320636"
     Region          130..160
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320636"
     Site            132..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30872.1)"
     Region          172..194
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320636"
     Site            176..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30872.1)"
     Region          220..249
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320636"
     Site            220..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30872.1)"
     Region          264..294
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320636"
     Site            271..296
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30872.1)"
     Region          302..327
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320636"
     Site            304..327
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30872.1)"
     CDS             1..391
                     /gene="SSTR1"
                     /gene_synonym="SRIF-2; SS-1-R; SS1-R; SS1R; SST1"
                     /coded_by="NM_001049.3:713..1888"
                     /db_xref="CCDS:CCDS9666.1"
                     /db_xref="GeneID:6751"
                     /db_xref="HGNC:HGNC:11330"
                     /db_xref="MIM:182451"
ORIGIN      
        1 mfpngtassp ssspspspgs cgegggsrgp gagaadgmee pgrnasqngt lsegqgsail
       61 isfiysvvcl vglcgnsmvi yvilryakmk tatniyilnl aiadellmls vpflvtstll
      121 rhwpfgallc rlvlsvdavn mftsiycltv lsvdryvavv hpikaaryrr ptvakvvnlg
      181 vwvlsllvil pivvfsrtaa nsdgtvacnm lmpepaqrwl vgfvlytflm gfllpvgaic
      241 lcyvliiakm rmvalkagwq qrkrserkit lmvmmvvmvf vicwmpfyvv qlvnvfaeqd
      301 datvsqlsvi lgyanscanp ilygflsdnf krsfqrilcl swmdnaaeep vdyyatalks
      361 raysvedfqp enlesggvfr ngtctsritt l
//
LOCUS       NP_065873               1235 aa            linear   PRI 27-APR-2025
DEFINITION  potassium channel subfamily T member 1 isoform 1 [Homo sapiens].
ACCESSION   NP_065873 XP_029962
VERSION     NP_065873.2
DBSOURCE    REFSEQ: accession NM_020822.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1235)
  AUTHORS   Cole,B.A., Kalli,A.C., Pilati,N., Muench,S.P. and Lippiat,J.D.
  TITLE     A molecular switch in RCK2 triggers sodium-dependent activation of
            KNa1.1 (KCNT1) potassium channels
  JOURNAL   Biophys J 123 (14), 2145-2153 (2024)
   PUBMED   38605520
  REMARK    GeneRIF: A molecular switch in RCK2 triggers sodium-dependent
            activation of KNa1.1 (KCNT1) potassium channels.
REFERENCE   2  (residues 1 to 1235)
  AUTHORS   Yuan,T., Wang,Y., Jin,Y., Yang,H., Xu,S., Zhang,H., Chen,Q., Li,N.,
            Ma,X., Song,H., Peng,C., Geng,Z., Dong,J., Duan,G., Sun,Q.,
            Yang,Y., Yang,F. and Huang,Z.
  TITLE     Coupling of Slack and NaV1.6 sensitizes Slack to quinidine blockade
            and guides anti-seizure strategy development
  JOURNAL   Elife 12, 87559 (2024)
   PUBMED   38289338
  REMARK    GeneRIF: Coupling of Slack and NaV1.6 sensitizes Slack to quinidine
            blockade and guides anti-seizure strategy development.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1235)
  AUTHORS   Zhang,J., Liu,S., Fan,J., Yan,R., Huang,B., Zhou,F., Yuan,T.,
            Gong,J., Huang,Z. and Jiang,D.
  TITLE     Structural basis of human Slo2.2 channel gating and modulation
  JOURNAL   Cell Rep 42 (8), 112858 (2023)
   PUBMED   37494189
REFERENCE   4  (residues 1 to 1235)
  AUTHORS   Hinckley,C.A., Zhu,Z., Chu,J.H., Gubbels,C., Danker,T.,
            Cherry,J.J., Whelan,C.D., Engle,S.J. and Nguyen,V.
  TITLE     Functional evaluation of epilepsy-associated KCNT1 variants in
            multiple cellular systems reveals a predominant gain of function
            impact on channel properties
  JOURNAL   Epilepsia 64 (8), 2126-2136 (2023)
   PUBMED   37177976
  REMARK    GeneRIF: Functional evaluation of epilepsy-associated KCNT1
            variants in multiple cellular systems reveals a predominant gain of
            function impact on channel properties.
REFERENCE   5  (residues 1 to 1235)
  AUTHORS   Barcia,G., Fleming,M.R., Deligniere,A., Gazula,V.R., Brown,M.R.,
            Langouet,M., Chen,H., Kronengold,J., Abhyankar,A., Cilio,R.,
            Nitschke,P., Kaminska,A., Boddaert,N., Casanova,J.L., Desguerre,I.,
            Munnich,A., Dulac,O., Kaczmarek,L.K., Colleaux,L. and Nabbout,R.
  TITLE     De novo gain-of-function KCNT1 channel mutations cause malignant
            migrating partial seizures of infancy
  JOURNAL   Nat Genet 44 (11), 1255-1259 (2012)
   PUBMED   23086397
  REMARK    GeneRIF: Our data identify KCNT1 as a major disease-associated gene
            in Malignant migrating partial seizures of infancy .
REFERENCE   6  (residues 1 to 1235)
  AUTHORS   Heron,S.E., Smith,K.R., Bahlo,M., Nobili,L., Kahana,E.,
            Licchetta,L., Oliver,K.L., Mazarib,A., Afawi,Z., Korczyn,A.,
            Plazzi,G., Petrou,S., Berkovic,S.F., Scheffer,I.E. and Dibbens,L.M.
  TITLE     Missense mutations in the sodium-gated potassium channel gene KCNT1
            cause severe autosomal dominant nocturnal frontal lobe epilepsy
  JOURNAL   Nat Genet 44 (11), 1188-1190 (2012)
   PUBMED   23086396
  REMARK    GeneRIF: Mutations in KCNT1 cause a severe form of ADNFLE and
            sporadic NFLE.
REFERENCE   7  (residues 1 to 1235)
  AUTHORS   Wei,A.D., Gutman,G.A., Aldrich,R., Chandy,K.G., Grissmer,S. and
            Wulff,H.
  TITLE     International Union of Pharmacology. LII. Nomenclature and
            molecular relationships of calcium-activated potassium channels
  JOURNAL   Pharmacol Rev 57 (4), 463-472 (2005)
   PUBMED   16382103
  REMARK    Review article
REFERENCE   8  (residues 1 to 1235)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   9  (residues 1 to 1235)
  AUTHORS   Gertler,T., Bearden,D., Bhattacharjee,A. and Carvill,G.
  TITLE     KCNT1-Related Epilepsy
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30234941
REFERENCE   10 (residues 1 to 1235)
  AUTHORS   Kurahashi,H. and Hirose,S.
  TITLE     Autosomal Dominant Sleep-Related Hypermotor (Hyperkinetic) Epilepsy
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK127272.1, BC171770.1,
            DA095802.1, BX110871.1 and AL158822.19.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 19, 2009 this sequence version replaced NP_065873.1.
            
            Summary: Potassium channels represent the most complex class of
            voltage-gated ion channels from both functional and structural
            standpoints. Their diverse functions include regulating
            neurotransmitter release, heart rate, insulin secretion, neuronal
            excitability, epithelial electrolyte transport, smooth muscle
            contraction, and cell volume. This gene encodes a sodium-activated
            potassium channel subunit which is thought to function in ion
            conductance and developmental signaling pathways. Mutations in this
            gene cause the early-onset epileptic disorders, malignant migrating
            partial seizures of infancy and autosomal dominant nocturnal
            frontal lobe epilepsy. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC136618.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371757.7/ ENSP00000360822.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..1235
                     /product="potassium channel subfamily T member 1 isoform
                     1"
                     /note="potassium channel, subfamily T, member 1; Sequence
                     like a calcium-activated K+ channel; potassium channel,
                     sodium activated subfamily T, member 1; sodium and
                     chloride-activated ATP-sensitive potassium channel Slo2.2"
                     /calculated_mol_wt=139569
     Region          162..342
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          277..350
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          504..598
                     /region_name="BK_channel_a"
                     /note="Calcium-activated BK potassium channel alpha
                     subunit; pfam03493"
                     /db_xref="CDD:460947"
     CDS             1..1235
                     /gene="KCNT1"
                     /gene_synonym="bA100C15.2; DEE14; EIEE14; ENFL5; KCa4.1;
                     KNa1.1; SLACK; Slo2.2"
                     /coded_by="NM_020822.3:75..3782"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35175.2"
                     /db_xref="GeneID:57582"
                     /db_xref="HGNC:HGNC:18865"
                     /db_xref="MIM:608167"
ORIGIN      
        1 mplpdgartp ggvcreargg gytnrtfefd dgqcaprrpc agdgalldta gfkmsdldse
       61 vlplppryrf rdlllgdpsf qnddrvqvef yvnentfker lklffiknqr sslrirlfnf
      121 slklltclly ivrvllddpa lgigcwgcpk qnysfndsss einwapilwv erkmtlwaiq
      181 vivaiisfle tmlliylsyk gniweqifrv sfvlemintl pfiitifwpp lrnlfipvfl
      241 ncwlakhale nmindfhrai lrtqsamfnq vlilfctllc lvftgtcgiq hleragenls
      301 lltsfyfciv tfstvgygdv tpkiwpsqll vvimicvalv vlplqfeelv ylwmerqksg
      361 gnysrhraqt ekhvvlcvss lkidllmdfl nefyahprlq dyyvvilcpt emdvqvrrvl
      421 qiplwsqrvi ylqgsalkdq dlmrakmdng eacfilssrn evdrtaadhq tilrawavkd
      481 fapncplyvq ilkpenkfhv kfadhvvcee eckyamlaln cicpatstli tllvhtsrgq
      541 egqespeqwq rmygrcsgne vyhirmgdsk ffreyegksf tyaafhahkk ygvcliglkr
      601 ednksillnp gprhilaasd tcfyinitke ensafifkqe ekrkkrafsg qglhegparl
      661 pvhsiiasmg tvamdlqgte hrptqsgggg ggsklalpte ngsgsrrpsi apvleladss
      721 allpcdllsd qsedevtpsd deglsvveyv kgyppnspyi gssptlchll pvkapfcclr
      781 ldkgckhnsy edakaygfkn kliivsaeta gnglynfivp lrayyrsrke lnpivllldn
      841 kpdhhfleai ccfpmvyyme gsvdnldsll qcgiiyadnl vvvdkestms aeedymadak
      901 tivnvqtmfr lfpslsitte lthpsnmrfm qfrakdsysl alsklekrer engsnlafmf
      961 rlpfaagrvf sismldtlly qsfvkdymit itrlllgldt tpgsgylcam kitegdlwir
     1021 tygrlfqklc sssaeipigi yrteshvfst sephdlraqs qisvnvedce dtrevkgpwg
     1081 sragtggssq grhtgggdpa ehpllrrksl qwarrlsrka pkqagraaaa ewisqqrlsl
     1141 yrrserqels elvknrmkhl glpttgydem ndhqntlsyv linpppdtrl epsdivylir
     1201 sdplahvass sqsrksscsh klsscnpetr detql
//
LOCUS       NP_005508                 90 aa            linear   PRI 27-APR-2025
DEFINITION  non-histone chromosomal protein HMG-17 [Homo sapiens].
ACCESSION   NP_005508 NP_116138
VERSION     NP_005508.1
DBSOURCE    REFSEQ: accession NM_005517.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Bin-Alee,F., Arayataweegool,A., Buranapraditkun,S.,
            Mahattanasakul,P., Tangjaturonrasme,N., Hirankarn,N.,
            Mutirangura,A. and Kitkumthorn,N.
  TITLE     Transcriptomic analysis of peripheral blood mononuclear cells in
            head and neck squamous cell carcinoma patients
  JOURNAL   Oral Dis 27 (6), 1394-1402 (2021)
   PUBMED   32892371
  REMARK    GeneRIF: Transcriptomic analysis of peripheral blood mononuclear
            cells in head and neck squamous cell carcinoma patients.
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Craig,J.M., Turner,T.H., Harrell,J.C. and Clevenger,C.V.
  TITLE     Prolactin Drives a Dynamic STAT5A/HDAC6/HMGN2 Cis-Regulatory
            Landscape Exploitable in ER+ Breast Cancer
  JOURNAL   Endocrinology 162 (5) (2021)
   PUBMED   33589921
  REMARK    GeneRIF: Prolactin Drives a Dynamic STAT5A/HDAC6/HMGN2
            Cis-Regulatory Landscape Exploitable in ER+ Breast Cancer.
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Cui,W., Liu,Y., Tan,Y., Peng,X., Cui,L., Cheng,Z., Dai,Y., Fu,L.,
            Zeng,T. and Liu,Y.
  TITLE     Prognostic value of HMGN family expression in acute myeloid
            leukemia
  JOURNAL   Future Oncol 17 (5), 541-548 (2021)
   PUBMED   33467898
  REMARK    GeneRIF: Prognostic value of HMGN family expression in acute
            myeloid leukemia.
REFERENCE   5  (residues 1 to 90)
  AUTHORS   Geng,F., Liu,Z., Chen,X., Chen,H., Liu,Y., Yang,J., Zheng,M.,
            Yang,L. and Teng,Y.
  TITLE     High mobility group nucleosomal binding 2 reduces integrin
            alpha5/beta1-mediated adhesion of Klebsiella pneumoniae on human
            pulmonary epithelial cells via nuclear factor I
  JOURNAL   Microbiol Immunol 64 (12), 825-834 (2020)
   PUBMED   33034909
  REMARK    GeneRIF: High mobility group nucleosomal binding 2 reduces integrin
            alpha5/beta1-mediated adhesion of Klebsiella pneumoniae on human
            pulmonary epithelial cells via nuclear factor I.
REFERENCE   6  (residues 1 to 90)
  AUTHORS   Feng,Y., Huang,N., Wu,Q. and Wang,B.
  TITLE     HMGN2: a novel antimicrobial effector molecule of human mononuclear
            leukocytes?
  JOURNAL   J Leukoc Biol 78 (5), 1136-1141 (2005)
   PUBMED   16204630
  REMARK    GeneRIF: A polypeptide, HMGN2, was isolated and may be an
            antimicrobial effector molecule of mononuclear leukocytes.
REFERENCE   7  (residues 1 to 90)
  AUTHORS   Giancotti,V., Bandiera,A., Buratti,E., Fusco,A., Marzari,R.,
            Coles,B. and Goodwin,G.H.
  TITLE     Comparison of multiple forms of the high mobility group I proteins
            in rodent and human cells. Identification of the human high
            mobility group I-C protein
  JOURNAL   Eur J Biochem 198 (1), 211-216 (1991)
   PUBMED   2040281
REFERENCE   8  (residues 1 to 90)
  AUTHORS   Dracopoli,N.C., O'Connell,P., Elsner,T.I., Lalouel,J.M.,
            White,R.L., Buetow,K.H., Nishimura,D.Y., Murray,J.C., Helms,C.,
            Mishra,S.K. et al.
  TITLE     The CEPH consortium linkage map of human chromosome 1
  JOURNAL   Genomics 9 (4), 686-700 (1991)
   PUBMED   2037294
REFERENCE   9  (residues 1 to 90)
  AUTHORS   Popescu,N., Landsman,D. and Bustin,M.
  TITLE     Mapping the human gene coding for chromosomal protein HMG-17
  JOURNAL   Hum Genet 85 (3), 376-378 (1990)
   PUBMED   2394451
REFERENCE   10 (residues 1 to 90)
  AUTHORS   Abercrombie,B.D., Kneale,G.G., Crane-Robinson,C., Bradbury,E.M.,
            Goodwin,G.H., Walker,J.M. and Johns,E.W.
  TITLE     Studies on the conformational properties of the high-mobility-group
            chromosomal protein HMG 17 and its interaction with DNA
  JOURNAL   Eur J Biochem 84 (1), 173-177 (1978)
   PUBMED   565710
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU100588.1, BC071707.1,
            BU074476.1, BC110390.1 and AL513365.27.
            
            On Sep 3, 2001 this sequence version replaced NP_116138.1.
            
            Summary: The protein encoded by this gene binds nucleosomal DNA and
            is associated with transcriptionally active chromatin. Along with a
            similar protein, HMGN1, the encoded protein may help maintain an
            open chromatin configuration around transcribable genes. The
            protein has also been found to have antimicrobial activity against
            bacteria, viruses and fungi. [provided by RefSeq, Oct 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.264967.1,
                                           SRR1803617.180791.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000361427.6/
                                                  ENSP00000355228.5
            Protein has antimicrobial activity :: PMID: 16204630
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..90
                     /product="non-histone chromosomal protein HMG-17"
                     /note="high mobility group protein N2; high-mobility group
                     (nonhistone chromosomal) protein 17; nonhistone
                     chromosomal protein HMG-17; high mobility group
                     nucleosome-binding domain-containing protein 2"
                     /calculated_mol_wt=9262
     Region          1..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05204.3)"
     mat_peptide     2..90
                     /product="non-histone chromosomal protein HMG-17"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     16204630]"
                     /calculated_mol_wt=9262
     Region          2..89
                     /region_name="HMG14_17"
                     /note="HMG14 and HMG17; pfam01101"
                     /db_xref="CDD:460064"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10739259; propagated from
                     UniProtKB/Swiss-Prot (P05204.3)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000269|PubMed:10739259; propagated from
                     UniProtKB/Swiss-Prot (P05204.3)"
     Site            82
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P05204.3)"
     CDS             1..90
                     /gene="HMGN2"
                     /gene_synonym="HMG17"
                     /coded_by="NM_005517.4:174..446"
                     /db_xref="CCDS:CCDS283.1"
                     /db_xref="GeneID:3151"
                     /db_xref="HGNC:HGNC:4986"
                     /db_xref="MIM:163910"
ORIGIN      
        1 mpkrkaegda kgdkakvkde pqrrsarlsa kpappkpepk pkkapakkge kvpkgkkgka
       61 dagkegnnpa engdaktdqa qkaegagdak
//
LOCUS       NP_004995                186 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8,
            mitochondrial isoform 1 precursor [Homo sapiens].
ACCESSION   NP_004995
VERSION     NP_004995.1
DBSOURCE    REFSEQ: accession NM_005004.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Piekutowska-Abramczuk,D., Assouline,Z., Matakovic,L.,
            Feichtinger,R.G., Konarikova,E., Jurkiewicz,E., Stawinski,P.,
            Gusic,M., Koller,A., Pollak,A., Gasperowicz,P., Trubicka,J.,
            Ciara,E., Iwanicka-Pronicka,K., Rokicki,D., Hanein,S.,
            Wortmann,S.B., Sperl,W., Rotig,A., Prokisch,H., Pronicka,E.,
            Ploski,R., Barcia,G. and Mayr,J.A.
  TITLE     NDUFB8 Mutations Cause Mitochondrial Complex I Deficiency in
            Individuals with Leigh-like Encephalomyopathy
  JOURNAL   Am J Hum Genet 102 (3), 460-467 (2018)
   PUBMED   29429571
  REMARK    GeneRIF: NDUFB8 is a relevant gene in childhood-onset mitochondrial
            disease.
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Ahmed,S.T., Alston,C.L., Hopton,S., He,L., Hargreaves,I.P.,
            Falkous,G., Olahova,M., McFarland,R., Turnbull,D.M., Rocha,M.C. and
            Taylor,R.W.
  TITLE     Using a quantitative quadruple immunofluorescent assay to diagnose
            isolated mitochondrial Complex I deficiency
  JOURNAL   Sci Rep 7 (1), 15676 (2017)
   PUBMED   29142257
  REMARK    GeneRIF: We observed loss of NDUFB8 immunoreactivity in all
            patients with mutations affecting nuclear-encoding structural
            subunits and assembly factors, whilst only 3 of the 10 patients
            with mutations affecting mtDNA-encoded structural subunits showed
            loss of NDUFB8, confirmed by BN-PAGE analysis of CI assembly and
            IHC using an alternative, commercially-available CI (NDUFS3)
            antibody.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Guo,R., Zong,S., Wu,M., Gu,J. and Yang,M.
  TITLE     Architecture of Human Mitochondrial Respiratory Megacomplex
            I2III2IV2
  JOURNAL   Cell 170 (6), 1247-1257 (2017)
   PUBMED   28844695
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Emahazion,T., Jobs,M., Howell,W.M., Siegfried,M., Wyoni,P.I.,
            Prince,J.A. and Brookes,A.J.
  TITLE     Identification of 167 polymorphisms in 88 genes from candidate
            neurodegeneration pathways
  JOURNAL   Gene 238 (2), 315-324 (1999)
   PUBMED   10570959
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Emahazion,T. and Brookes,A.J.
  TITLE     Mapping of the NDUFA2, NDUFA6, NDUFA7, NDUFB8, and NDUFS8 electron
            transport chain genes by intron based radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 114 (1998)
   PUBMED   9763676
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Dunbar,D.R., Shibasaki,Y., Dobbie,L., Andersson,B. and Brookes,A.J.
  TITLE     In situ hybridisation mapping of genomic clones for five human
            respiratory chain complex I genes
  JOURNAL   Cytogenet Cell Genet 78 (1), 21-24 (1997)
   PUBMED   9345899
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA428446.1 and BC000466.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.67268.1, BU601073.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162946 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000299166.9/
                                                  ENSP00000299166.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..186
                     /product="NADH dehydrogenase [ubiquinone] 1 beta
                     subcomplex subunit 8, mitochondrial isoform 1 precursor"
                     /note="complex I ASHI subunit; NADH dehydrogenase
                     [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;
                     NADH:ubiquinone oxidoreductase ASHI subunit; complex
                     I-ASHI; NADH dehydrogenase (ubiquinone) 1 beta subcomplex,
                     8, 19kDa"
                     /calculated_mol_wt=18774
     transit_peptide 1..28
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (O95169.1)"
                     /calculated_mol_wt=3010
     Region          21..186
                     /region_name="NDUF_B8"
                     /note="NADH-ubiquinone oxidoreductase ASHI subunit
                     (CI-ASHI or NDUFB8); pfam05821"
                     /db_xref="CDD:428637"
     mat_peptide     29..186
                     /product="NADH dehydrogenase [ubiquinone] 1 beta
                     subcomplex subunit 8, mitochondrial. /id=PRO_0000020046"
                     /note="propagated from UniProtKB/Swiss-Prot (O95169.1)"
                     /calculated_mol_wt=18774
     Site            133..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95169.1)"
     CDS             1..186
                     /gene="NDUFB8"
                     /gene_synonym="ASHI; CI-ASHI; MC1DN32"
                     /coded_by="NM_005004.4:21..581"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS7497.1"
                     /db_xref="GeneID:4714"
                     /db_xref="HGNC:HGNC:7703"
                     /db_xref="MIM:602140"
ORIGIN      
        1 mavaragvlg vqwlqrasrn vmplgartas hmtkdmfpgp yprtpeeraa aakkynmrve
       61 dyepypddgm gygdypklpd rsqherdpwy swdqpglrln wgepmhwhld mynrnrvdts
      121 ptpvswhvmc mqlfgflafm ifmcwvgdvy pvyqpvgpkq ypynnlyler ggdpskeper
      181 vvhyei
//
LOCUS       NP_055557                642 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane 9 superfamily member 4 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_055557
VERSION     NP_055557.2
DBSOURCE    REFSEQ: accession NM_014742.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Meng,Z., Li,Z., Xie,M., Yu,H., Jiang,L. and Yao,X.
  TITLE     TM9SF4 is an F-actin disassembly factor that promotes tumor
            progression and metastasis
  JOURNAL   Nat Commun 13 (1), 5728 (2022)
   PUBMED   36175399
  REMARK    GeneRIF: TM9SF4 is an F-actin disassembly factor that promotes
            tumor progression and metastasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Xie,M., Mak,J.W.Y., Yu,H., Cheng,C.T.Y., Chan,H.C.H., Chan,T.T.,
            Lau,L.H.S., Wong,M.T.L., Ko,W.H., Jiang,L. and Yao,X.
  TITLE     TM9SF4 Is a Crucial Regulator of Inflammation and ER Stress in
            Inflammatory Bowel Disease
  JOURNAL   Cell Mol Gastroenterol Hepatol 14 (2), 245-270 (2022)
   PUBMED   35398597
  REMARK    GeneRIF: TM9SF4 Is a Crucial Regulator of Inflammation and ER
            Stress in Inflammatory Bowel Disease.
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Zhu,Y., Xie,M., Meng,Z., Leung,L.K., Chan,F.L., Hu,X., Chi,K.,
            Liu,C. and Yao,X.
  TITLE     Knockdown of TM9SF4 boosts ER stress to trigger cell death of
            chemoresistant breast cancer cells
  JOURNAL   Oncogene 38 (29), 5778-5791 (2019)
   PUBMED   31249383
  REMARK    GeneRIF: results uncovered a novel role of TM9SF4 proteins in
            alleviating endoplasmic reticulum stress and protecting
            chemoresistant breast cancer cells from apoptotic/necrotic cell
            death
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Vernay,A., Lamrabet,O., Perrin,J. and Cosson,P.
  TITLE     TM9SF4 levels determine sorting of transmembrane domains in the
            early secretory pathway
  JOURNAL   J Cell Sci 131 (21) (2018)
   PUBMED   30301779
  REMARK    GeneRIF: Results show that TM9SF4 controls the sorting of TMDs at
            the ER-Golgi interface. Remarkably, sorting of T-R1 in HCT116 cells
            was different from that in HEK cells: in HCT116 cells, a
            substantial fraction of T-R1 was localized to the Golgi complex,
            and it was relocated to the ER by genetic ablation of TM9SF4.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Lozupone,F., Borghi,M., Marzoli,F., Azzarito,T., Matarrese,P.,
            Iessi,E., Venturi,G., Meschini,S., Canitano,A., Bona,R., Cara,A.
            and Fais,S.
  TITLE     TM9SF4 is a novel V-ATPase-interacting protein that modulates tumor
            pH alterations associated with drug resistance and invasiveness of
            colon cancer cells
  JOURNAL   Oncogene 34 (40), 5163-5174 (2015)
   PUBMED   25659576
  REMARK    GeneRIF: Our study shows for the first time the important role of
            TM9SF4 in the aberrant constitutive activation of the V-ATPase, and
            the development of a malignant phenotype.
REFERENCE   7  (residues 1 to 642)
  AUTHORS   Paolillo,R., Spinello,I., Quaranta,M.T., Pasquini,L., Pelosi,E., Lo
            Coco,F., Testa,U. and Labbaye,C.
  TITLE     Human TM9SF4 Is a New Gene Down-Regulated by Hypoxia and Involved
            in Cell Adhesion of Leukemic Cells
  JOURNAL   PLoS One 10 (5), e0126968 (2015)
   PUBMED   25961573
  REMARK    GeneRIF: TM9SF4 is a direct target of HIF-1alpha, down-regulated in
            leukemic cells by hypoxia and involved in cell adhesion.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 642)
  AUTHORS   Jostins,L., Ripke,S., Weersma,R.K., Duerr,R.H., McGovern,D.P.,
            Hui,K.Y., Lee,J.C., Schumm,L.P., Sharma,Y., Anderson,C.A.,
            Essers,J., Mitrovic,M., Ning,K., Cleynen,I., Theatre,E.,
            Spain,S.L., Raychaudhuri,S., Goyette,P., Wei,Z., Abraham,C.,
            Achkar,J.P., Ahmad,T., Amininejad,L., Ananthakrishnan,A.N.,
            Andersen,V., Andrews,J.M., Baidoo,L., Balschun,T., Bampton,P.A.,
            Bitton,A., Boucher,G., Brand,S., Buning,C., Cohain,A., Cichon,S.,
            D'Amato,M., De Jong,D., Devaney,K.L., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Ferguson,L.R., Franchimont,D., Fransen,K.,
            Gearry,R., Georges,M., Gieger,C., Glas,J., Haritunians,T., Hart,A.,
            Hawkey,C., Hedl,M., Hu,X., Karlsen,T.H., Kupcinskas,L.,
            Kugathasan,S., Latiano,A., Laukens,D., Lawrance,I.C., Lees,C.W.,
            Louis,E., Mahy,G., Mansfield,J., Morgan,A.R., Mowat,C., Newman,W.,
            Palmieri,O., Ponsioen,C.Y., Potocnik,U., Prescott,N.J.,
            Regueiro,M., Rotter,J.I., Russell,R.K., Sanderson,J.D., Sans,M.,
            Satsangi,J., Schreiber,S., Simms,L.A., Sventoraityte,J.,
            Targan,S.R., Taylor,K.D., Tremelling,M., Verspaget,H.W., De Vos,M.,
            Wijmenga,C., Wilson,D.C., Winkelmann,J., Xavier,R.J., Zeissig,S.,
            Zhang,B., Zhang,C.K., Zhao,H., Silverberg,M.S., Annese,V.,
            Hakonarson,H., Brant,S.R., Radford-Smith,G., Mathew,C.G.,
            Rioux,J.D., Schadt,E.E., Daly,M.J., Franke,A., Parkes,M.,
            Vermeire,S., Barrett,J.C. and Cho,J.H.
  CONSRTM   International IBD Genetics Consortium (IIBDGC)
  TITLE     Host-microbe interactions have shaped the genetic architecture of
            inflammatory bowel disease
  JOURNAL   Nature 491 (7422), 119-124 (2012)
   PUBMED   23128233
REFERENCE   9  (residues 1 to 642)
  AUTHORS   Lozupone,F., Perdicchio,M., Brambilla,D., Borghi,M., Meschini,S.,
            Barca,S., Marino,M.L., Logozzi,M., Federici,C., Iessi,E., de
            Milito,A. and Fais,S.
  TITLE     The human homologue of Dictyostelium discoideum phg1A is expressed
            by human metastatic melanoma cells
  JOURNAL   EMBO Rep 10 (12), 1348-1354 (2009)
   PUBMED   19893578
  REMARK    GeneRIF: TM9SF4 is a new marker of malignancy, representing a
            potential new target for anti-tumour strategies with a specific
            role in tumour cannibalism and in the establishment of a metastatic
            phenotype.
REFERENCE   10 (residues 1 to 642)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC381660.1, BC021107.1, D87444.1 and BM976438.1.
            
            On Jan 9, 2008 this sequence version replaced NP_055557.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.112811.1,
                                           SRR1803612.622.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398022.7/ ENSP00000381104.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..642
                     /product="transmembrane 9 superfamily member 4 isoform 1
                     precursor"
                     /note="dinucleotide oxidase disulfide thiol exchanger 3
                     superfamily member 4; transmembrane 9 superfamily protein
                     member 4; tumor cannibalism associated protein 1"
                     /calculated_mol_wt=71919
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2618
     mat_peptide     24..642
                     /product="Transmembrane 9 superfamily member 4.
                     /id=PRO_0000210178"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92544.2)"
                     /calculated_mol_wt=71919
     Region          55..599
                     /region_name="EMP70"
                     /note="Endomembrane protein 70; pfam02990"
                     /db_xref="CDD:460774"
     Site            282..302
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92544.2)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q92544.2)"
     Site            347..367
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92544.2)"
     Site            377..397
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92544.2)"
     Site            417..437
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92544.2)"
     Site            450..470
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92544.2)"
     Site            502..522
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92544.2)"
     Site            536..556
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92544.2)"
     Site            571..591
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92544.2)"
     Site            599..619
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92544.2)"
     CDS             1..642
                     /gene="TM9SF4"
                     /gene_synonym="dJ836N17.2"
                     /coded_by="NM_014742.4:28..1956"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS13196.2"
                     /db_xref="GeneID:9777"
                     /db_xref="HGNC:HGNC:30797"
                     /db_xref="MIM:617727"
ORIGIN      
        1 matamdwlpw slllfslmce tsafyvpgva pinfhqndpv eikavkltss rtqlpyeyys
       61 lpfcqpskit ykaenlgevl rgdrivntpf qvlmnsekkc evlcsqsnkp vtltveqsrl
      121 vaeritedyy vhliadnlpv atrlelysnr dsddkkkekd vqfehgyrlg ftdvnkiylh
      181 nhlsfilyyh redmeedqeh tyrvvrfevi pqsirledlk adekssctlp egtnsspqei
      241 dptkenqlyf tysvhweesd ikwasrwdty ltmsdvqihw fsiinsvvvv fflsgilsmi
      301 iirtlrkdia nynkeddied tmeesgwklv hgdvfrppqy pmilssllgs giqlfcmili
      361 vifvamlgml spssrgalmt tacflfmfmg vfggfsagrl yrtlkghrwk kgafctatly
      421 pgvvfgicfv lncfiwgkhs sgavpfptmv allcmwfgis lplvylgyyf gfrkqpydnp
      481 vrtnqiprqi peqrwymnrf vgilmagilp fgamfielff ifsaiwenqf yylfgflflv
      541 fiilvvscsq isivmvyfql caedyrwwwr nflvsggsaf yvlvyaifyf vnkldivefi
      601 psllyfgyta lmvlsfwllt gtigfyaaym fvrkiyaavk id
//
LOCUS       NP_001159442             299 aa            linear   PRI 27-APR-2025
DEFINITION  STE20-related kinase adapter protein alpha isoform 6 [Homo
            sapiens].
ACCESSION   NP_001159442
VERSION     NP_001159442.1
DBSOURCE    REFSEQ: accession NM_001165970.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Smith,R.H.B., Khan,Z.M., Ung,P.M., Scopton,A.P., Silber,L.,
            Mack,S.M., Real,A.M., Schlessinger,A. and Dar,A.C.
  TITLE     Type II Binders Targeting the 'GLR-Out' Conformation of the
            Pseudokinase STRADalpha
  JOURNAL   Biochemistry 60 (4), 289-302 (2021)
   PUBMED   33440120
  REMARK    GeneRIF: Type II Binders Targeting the ''GLR-Out'' Conformation of
            the Pseudokinase STRADalpha.
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Alsaif,H.S., Khashab,H.Y.E.L. and Alkuraya,F.S.
  TITLE     Two further cases of polyhydramnios, megalencephaly, and
            symptomatic epilepsy syndrome, caused by a truncating variant in
            STRADA
  JOURNAL   Am J Med Genet A 185 (2), 604-607 (2021)
   PUBMED   33247513
  REMARK    GeneRIF: Two further cases of polyhydramnios, megalencephaly, and
            symptomatic epilepsy syndrome, caused by a truncating variant in
            STRADA.
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Milburn,C.C., Boudeau,J., Deak,M., Alessi,D.R. and van Aalten,D.M.
  TITLE     Crystal structure of MO25 alpha in complex with the C terminus of
            the pseudo kinase STE20-related adaptor
  JOURNAL   Nat Struct Mol Biol 11 (2), 193-200 (2004)
   PUBMED   14730349
REFERENCE   8  (residues 1 to 299)
  AUTHORS   Boudeau,J., Baas,A.F., Deak,M., Morrice,N.A., Kieloch,A.,
            Schutkowski,M., Prescott,A.R., Clevers,H.C. and Alessi,D.R.
  TITLE     MO25alpha/beta interact with STRADalpha/beta enhancing their
            ability to bind, activate and localize LKB1 in the cytoplasm
  JOURNAL   EMBO J 22 (19), 5102-5114 (2003)
   PUBMED   14517248
REFERENCE   9  (residues 1 to 299)
  AUTHORS   Baas,A.F., Boudeau,J., Sapkota,G.P., Smit,L., Medema,R.,
            Morrice,N.A., Alessi,D.R. and Clevers,H.C.
  TITLE     Activation of the tumour suppressor kinase LKB1 by the STE20-like
            pseudokinase STRAD
  JOURNAL   EMBO J 22 (12), 3062-3072 (2003)
   PUBMED   12805220
  REMARK    GeneRIF: Identification and characterization of an LKB1-specific
            adaptor protein and substrate, STRAD. Results imply that STRAD
            plays a key role in regulating the tumor suppressor activities of
            LKB1.
REFERENCE   10 (residues 1 to 299)
  AUTHORS   Scanlan,M.J., Gout,I., Gordon,C.M., Williamson,B., Stockert,E.,
            Gure,A.O., Jager,D., Chen,Y.T., Mackay,A., O'Hare,M.J. and Old,L.J.
  TITLE     Humoral immunity to human breast cancer: antigen definition and
            quantitative analysis of mRNA expression
  JOURNAL   Cancer Immun 1, 4 (2001)
   PUBMED   12747765
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA049174.1, AY290821.2,
            AK293160.1, AL832407.1 and BQ682133.1.
            
            Summary: The protein encoded by this gene contains a STE20-like
            kinase domain, but lacks several residues that are critical for
            catalytic activity, so it is termed a 'pseudokinase'. The protein
            forms a heterotrimeric complex with serine/threonine kinase 11
            (STK11, also known as LKB1) and the scaffolding protein calcium
            binding protein 39 (CAB39, also known as MO25). The protein
            activates STK11 leading to the phosphorylation of both proteins and
            excluding STK11 from the nucleus. The protein is necessary for
            STK11-induced G1 cell cycle arrest. A mutation in this gene has
            been shown to result in polyhydramnios, megalencephaly, and
            symptomatic epilepsy (PMSE) syndrome. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            Additional transcript variants have been described but their
            full-length nature is not known. [provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293160.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..299
                     /product="STE20-related kinase adapter protein alpha
                     isoform 6"
                     /note="STE20-like pseudokinase; STE20-related kinase
                     adapter protein alpha; protein kinase LYK5; serologically
                     defined breast cancer antigen NY-BR-96; STE20-related
                     kinase adaptor alpha"
                     /calculated_mol_wt=33146
     Region          32..297
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(32..34,39,41,54,56,87,103..106,151,155..156,158,
                     168..169)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173767"
     CDS             1..299
                     /gene="STRADA"
                     /gene_synonym="LYK5; NY-BR-96; PMSE; Stlk; STRAD; STRAD
                     alpha"
                     /coded_by="NM_001165970.2:291..1190"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS54156.1"
                     /db_xref="GeneID:92335"
                     /db_xref="HGNC:HGNC:30172"
                     /db_xref="MIM:608626"
ORIGIN      
        1 msflvskper irrwvsekfi veglrdlelf ggkgfedlmt vnlarykptg eyvtvrrinl
       61 eacsnemvtf lqgelhvskl fnhpnivpyr atfiadnelw vvtsfmaygs akdlicthfm
      121 dgmnelaiay ilqgvlkald yihhmgyvhr svkashilis vdgkvylsgl rsnlsmishg
      181 qrqrvvhdfp kysvkvlpwl spevlqqnlq gydaksdiys vgitacelan ghvpfkdmpa
      241 tqmlleklng tvpclldtst ipaeeltmsp srsvansgls dslttstprp sngpvpaps
//
LOCUS       NP_055562                308 aa            linear   PRI 27-APR-2025
DEFINITION  regulating synaptic membrane exocytosis protein 3 [Homo sapiens].
ACCESSION   NP_055562 XP_375720
VERSION     NP_055562.2
DBSOURCE    REFSEQ: accession NM_014747.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Huang,X.F., Mao,J.Y., Huang,Z.Q., Rao,F.Q., Cheng,F.F., Li,F.F.,
            Wang,Q.F. and Jin,Z.B.
  TITLE     Genome-Wide Detection of Copy Number Variations in Unsolved
            Inherited Retinal Disease
  JOURNAL   Invest Ophthalmol Vis Sci 58 (1), 424-429 (2017)
   PUBMED   28118666
  REMARK    GeneRIF: We identified four novel CNVs in three different genes
            (one duplication in USH2A gene, two duplications in CEP290 gene,
            and one duplication in RIMS2 gene) in total four families, at a
            detection rate of 8% (4/50).
REFERENCE   6  (residues 1 to 308)
  AUTHORS   Kumar,R.A., Sudi,J., Babatz,T.D., Brune,C.W., Oswald,D., Yen,M.,
            Nowak,N.J., Cook,E.H., Christian,S.L. and Dobyns,W.B.
  TITLE     A de novo 1p34.2 microdeletion identifies the synaptic vesicle gene
            RIMS3 as a novel candidate for autism
  JOURNAL   J Med Genet 47 (2), 81-90 (2010)
   PUBMED   19546099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 308)
  AUTHORS   Weidenhofer,J., Scott,R.J. and Tooney,P.A.
  TITLE     Investigation of the expression of genes affecting cytomatrix
            active zone function in the amygdala in schizophrenia: effects of
            antipsychotic drugs
  JOURNAL   J Psychiatr Res 43 (3), 282-290 (2009)
   PUBMED   18490030
  REMARK    GeneRIF: Western blot analysis shows increased piccolo protein
            expression in the amygdala in schizophrenia.
REFERENCE   8  (residues 1 to 308)
  AUTHORS   Sudhof,T.C.
  TITLE     The synaptic vesicle cycle
  JOURNAL   Annu Rev Neurosci 27, 509-547 (2004)
   PUBMED   15217342
  REMARK    Review article
REFERENCE   9  (residues 1 to 308)
  AUTHORS   Wang,Y. and Sudhof,T.C.
  TITLE     Genomic definition of RIM proteins: evolutionary amplification of a
            family of synaptic regulatory proteins
  JOURNAL   Genomics 81 (2), 126-137 (2003)
   PUBMED   12620390
REFERENCE   10 (residues 1 to 308)
  AUTHORS   Wang,Y., Sugita,S. and Sudhof,T.C.
  TITLE     The RIM/NIM family of neuronal C2 domain proteins. Interactions
            with Rab3 and a new class of Src homology 3 domain proteins
  JOURNAL   J Biol Chem 275 (26), 20033-20044 (2000)
   PUBMED   10748113
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031289.1.
            
            On or before Aug 30, 2004 this sequence version replaced
            XP_375720.1, NP_055562.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D87074.1, SRR18074967.2952452.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372684.8/ ENSP00000361769.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..308
                     /product="regulating synaptic membrane exocytosis protein
                     3"
                     /note="Rab-3 interacting molecule 3; RIM3 gamma;
                     rab-3-interacting molecule 3"
                     /calculated_mol_wt=32665
     Region          86..120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJD0.1)"
     Region          141..286
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80U57; propagated from
                     UniProtKB/Swiss-Prot (Q9UJD0.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80U57; propagated from
                     UniProtKB/Swiss-Prot (Q9UJD0.1)"
     CDS             1..308
                     /gene="RIMS3"
                     /gene_synonym="NIM3; RIM 3; RIM3"
                     /coded_by="NM_014747.3:496..1422"
                     /db_xref="CCDS:CCDS30687.1"
                     /db_xref="GeneID:9783"
                     /db_xref="HGNC:HGNC:21292"
                     /db_xref="MIM:611600"
ORIGIN      
        1 mfngepgpas sgasrnvvrs ssisgeicgs qqagggagtt takkrrsslg akmvaivglt
       61 qwskstlqlp qpegatkklr snirrstetg iavemrsrvt rqgsrestdg stnsnssdgt
      121 fifpttrlga esqfsdfldg lgpaqivgrq tlatppmgdv hiaimdrsgq leveviearg
      181 ltpkpgsksl patyikvyll engaclakkk tkmtkktcdp lyqqallfde gpqgkvlqvi
      241 vwgdygrmdh kcfmgmaqim ldeldlsaav tgwyklfpts svadstlgsl trrlsqssle
      301 satspscs
//
LOCUS       NP_003122                508 aa            linear   PRI 27-APR-2025
DEFINITION  serum response factor isoform 1 [Homo sapiens].
ACCESSION   NP_003122
VERSION     NP_003122.1
DBSOURCE    REFSEQ: accession NM_003131.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Gong,Y., Liu,M., Zhang,Q., Li,J., Cai,H., Ran,J., Ma,L., Ma,Y. and
            Quan,S.
  TITLE     Lysine acetyltransferase 14 mediates TGF-beta-induced fibrosis in
            ovarian endometrioma via co-operation with serum response factor
  JOURNAL   J Transl Med 22 (1), 561 (2024)
   PUBMED   38867256
  REMARK    GeneRIF: Lysine acetyltransferase 14 mediates TGF-beta-induced
            fibrosis in ovarian endometrioma via co-operation with serum
            response factor.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Yang,D., Yang,D., He,Y., Liu,J., Song,Y., Zhou,Y., Jiang,L.,
            Zeng,X., Xu,X., Xu,H., Li,J. and Dan,H.
  TITLE     MRTF-A/SRF signaling suppresses invasion of oral squamous cell
            carcinoma
  JOURNAL   Oral Dis 30 (4), 1919-1934 (2024)
   PUBMED   37154247
  REMARK    GeneRIF: MRTF-A/SRF signaling suppresses invasion of oral squamous
            cell carcinoma.
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Park,J., Shim,J.K., Lee,M., Kim,D., Yoon,S.J., Moon,J.H., Kim,E.H.,
            Park,J.Y., Chang,J.H. and Kang,S.G.
  TITLE     Classification of IDH wild-type glioblastoma tumorspheres into low-
            and high-invasion groups based on their transcriptional program
  JOURNAL   Br J Cancer 129 (7), 1061-1070 (2023)
   PUBMED   37558923
  REMARK    GeneRIF: Classification of IDH wild-type glioblastoma tumorspheres
            into low- and high-invasion groups based on their transcriptional
            program.
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Papa,B., Nguyen,M.A., Kumar,A., Song,L., Dorwal,P. and Cheah,A.L.
  TITLE     Cellular myofibromas with SRF fusions: clinicopathological and
            molecular study of 3 cases of a rare entity and a potential mimic
            of sarcoma
  JOURNAL   Hum Pathol 138, 41-48 (2023)
   PUBMED   37245628
  REMARK    GeneRIF: Cellular myofibromas with SRF fusions: clinicopathological
            and molecular study of 3 cases of a rare entity and a potential
            mimic of sarcoma.
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Al-Hetty,H.R.A.K., Ismaeel,G.L., Mohammad,W.T., Toama,M.A.,
            Kandeel,M., Saleh,M.M. and Turki Jalil,A.
  TITLE     SRF/MRTF-A and liver cirrhosis: Pathologic associations
  JOURNAL   J Dig Dis 23 (11), 614-619 (2022)
   PUBMED   36601855
  REMARK    GeneRIF: SRF/MRTF-A and liver cirrhosis: Pathologic associations.
            Review article
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Reason,A.J., Morris,H.R., Panico,M., Marais,R., Treisman,R.H.,
            Haltiwanger,R.S., Hart,G.W., Kelly,W.G. and Dell,A.
  TITLE     Localization of O-GlcNAc modification on the serum response
            transcription factor
  JOURNAL   J Biol Chem 267 (24), 16911-16921 (1992)
   PUBMED   1512232
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Grueneberg,D.A., Natesan,S., Alexandre,C. and Gilman,M.Z.
  TITLE     Human and Drosophila homeodomain proteins that enhance the
            DNA-binding activity of serum response factor
  JOURNAL   Science 257 (5073), 1089-1095 (1992)
   PUBMED   1509260
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Janknecht,R., Hipskind,R.A., Houthaeve,T., Nordheim,A. and
            Stunnenberg,H.G.
  TITLE     Identification of multiple SRF N-terminal phosphorylation sites
            affecting DNA binding properties
  JOURNAL   EMBO J 11 (3), 1045-1054 (1992)
   PUBMED   1547771
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Marais,R.M., Hsuan,J.J., McGuigan,C., Wynne,J. and Treisman,R.
  TITLE     Casein kinase II phosphorylation increases the rate of serum
            response factor-binding site exchange
  JOURNAL   EMBO J 11 (1), 97-105 (1992)
   PUBMED   1740119
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Manak,J.R. and Prywes,R.
  TITLE     Mutation of serum response factor phosphorylation sites and the
            mechanism by which its DNA-binding activity is increased by casein
            kinase II
  JOURNAL   Mol Cell Biol 11 (7), 3652-3659 (1991)
   PUBMED   2046671
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355385.15 and BC052572.1.
            
            Summary: This gene encodes a ubiquitous nuclear protein that
            stimulates both cell proliferation and differentiation. It is a
            member of the MADS (MCM1, Agamous, Deficiens, and SRF) box
            superfamily of transcription factors. This protein binds to the
            serum response element (SRE) in the promoter region of target
            genes. This protein regulates the activity of many immediate-early
            genes, for example c-fos, and thereby participates in cell cycle
            regulation, apoptosis, cell growth, and cell differentiation. This
            gene is the downstream target of many pathways; for example, the
            mitogen-activated protein kinase pathway (MAPK) that acts through
            the ternary complex factors (TCFs). Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052572.1, J03161.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265354.6/ ENSP00000265354.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..508
                     /product="serum response factor isoform 1"
                     /note="c-fos serum response element-binding transcription
                     factor; minichromosome maintenance 1 homolog"
                     /calculated_mol_wt=51462
     Region          1..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11831.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:1547771,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:1547771,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:1547771,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:1547771,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:1547771; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     Region          142..223
                     /region_name="MADS_SRF_like"
                     /note="SRF-like/Type I subfamily of MADS (MCM1, Agamous,
                     Deficiens, and SRF (serum response factor) box family of
                     eukaryotic transcriptional regulators. Binds DNA and
                     exists as hetero- and homo-dimers. Differs from the
                     MEF-like/Type II subgroup mainly in...; cd00266"
                     /db_xref="CDD:238166"
     Site            order(143,145,159,162..164,167,170..171)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238166"
     Site            order(161,164,168..169,172,175,177..178,184,186,188,194,
                     198,204..205,211,214..215,219)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238166"
     Region          168..222
                     /region_name="Involved in dimerization"
                     /note="propagated from UniProtKB/Swiss-Prot (P11831.1)"
     Site            order(169..170,173,177,193..200,206,212,215..216,219..220)
                     /site_type="other"
                     /note="protein interaction site [polypeptide binding]"
                     /db_xref="CDD:238166"
     Site            199
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238166"
     Region          219..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11831.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P11831.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8375385; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     Site            277
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:1512232. /id=CAR_000181;
                     propagated from UniProtKB/Swiss-Prot (P11831.1)"
     Site            307
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000305|PubMed:1512232; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     Site            309
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000305|PubMed:1512232; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     Site            316
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:1512232. /id=CAR_000196;
                     propagated from UniProtKB/Swiss-Prot (P11831.1)"
     Region          362..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11831.1)"
     Site            383
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000305|PubMed:1512232; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by dsDNA kinase.
                     /evidence=ECO:0000269|PubMed:8407951; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by dsDNA kinase.
                     /evidence=ECO:0000269|PubMed:8407951; propagated from
                     UniProtKB/Swiss-Prot (P11831.1)"
     CDS             1..508
                     /gene="SRF"
                     /gene_synonym="MCM1"
                     /coded_by="NM_003131.4:389..1915"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4889.1"
                     /db_xref="GeneID:6722"
                     /db_xref="HGNC:HGNC:11291"
                     /db_xref="MIM:600589"
ORIGIN      
        1 mlptqagaaa algrgsalgg slnrtptgrp gggggtrgan ggrvpgngag lgpgrlerea
       61 aaaaattpap tagalysgse gdsesgeeee lgaerrglkr slsemeigmv vggpeasaaa
      121 tggygpvsga vsgakpgkkt rgrvkikmef idnklrrytt fskrktgimk kayelstltg
      181 tqvlllvase tghvytfatr klqpmitset gkaliqtcln spdspprsdp ttdqrmsatg
      241 feetdltyqv sesdssgetk dtlkpaftvt nlpgttstiq tapststtmq vssgpsfpit
      301 nylapvsasv spsavssang tvlkstgsgp vssgglmqlp tsftlmpgga vaqqvpvqai
      361 qvhqapqqas psrdsstdlt qtsssgtvtl patimtssvp ttvgghmmyp sphavmyapt
      421 sglgdgsltv lnafsqapst mqvshsqvqe pggvpqvflt assgtvqipv savqlhqmav
      481 igqqagsssn ltelqvvnld tahstkse
//
LOCUS       NP_073583                337 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial amidoxime-reducing component 1 precursor [Homo
            sapiens].
ACCESSION   NP_073583
VERSION     NP_073583.3
DBSOURCE    REFSEQ: accession NM_022746.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Hou,W., Watson,C., Cecconie,T., Bolaki,M.N., Brady,J.J., Lu,Q.,
            Gatto,G.J. Jr. and Day,T.A.
  TITLE     Biochemical and functional characterization of the p.A165T missense
            variant of mitochondrial amidoxime-reducing component 1
  JOURNAL   J Biol Chem 300 (6), 107353 (2024)
   PUBMED   38723751
  REMARK    GeneRIF: Biochemical and functional characterization of the p.A165T
            missense variant of mitochondrial amidoxime-reducing component 1.
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Dutta,T., Sasidharan,K., Ciociola,E., Pennisi,G., Noto,F.R.,
            Kovooru,L., Kroon,T., Lindblom,A., Du,Y., Pirmoradian,M.,
            Wallin,S., Mancina,R.M., Linden,D. and Romeo,S.
  TITLE     Mitochondrial amidoxime-reducing component 1 p.Ala165Thr increases
            protein degradation mediated by the proteasome
  JOURNAL   Liver Int 44 (5), 1219-1232 (2024)
   PUBMED   38375985
  REMARK    GeneRIF: Mitochondrial amidoxime-reducing component 1 p.Ala165Thr
            increases protein degradation mediated by the proteasome.
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Jones,A.K., Bajrami,B., Campbell,M.K., Erzurumluoglu,A.M., Guo,Q.,
            Chen,H., Zhang,X., Zeveleva,S., Kvaskoff,D., Brunner,A.D.,
            Muller,S., Gathey,V., Dave,R.M., Tanner,J.W., Rixen,S.,
            Struwe,M.A., Phoenix,K., Klumph,K.J., Robinson,H., Veyel,D.,
            Muller,A., Noyvert,B., Bartholdy,B.A., Steixner-Kumar,A.A.,
            Stutzki,J., Drichel,D., Omland,S., Sheehan,R., Hill,J.,
            Bretschneider,T., Gottschling,D., Scheidig,A.J., Clement,B.,
            Giera,M., Ding,Z., Broadwater,J. and Warren,C.R.
  TITLE     mARC1 in MASLD: Modulation of lipid accumulation in human
            hepatocytes and adipocytes
  JOURNAL   Hepatol Commun 8 (5), e0365 (2024)
   PUBMED   38619429
  REMARK    GeneRIF: mARC1 in MASLD: Modulation of lipid accumulation in human
            hepatocytes and adipocytes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Wu,M., Tie,M., Hu,L., Yang,Y., Chen,Y., Ferguson,D., Chen,Y. and
            He,A.
  TITLE     Fatty liver disease protective MTARC1 p.A165T variant reduces the
            protein stability of MTARC1
  JOURNAL   Biochem Biophys Res Commun 702, 149655 (2024)
   PUBMED   38340654
  REMARK    GeneRIF: Fatty liver disease protective MTARC1 p.A165T variant
            reduces the protein stability of MTARC1.
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Smagris,E., Shihanian,L.M., Mintah,I.J., Bigdelou,P., Livson,Y.,
            Brown,H., Verweij,N., Hunt,C., Johnson,R.O., Greer,T.J.,
            Hartford,S.A., Hindy,G., Sun,L., Nielsen,J.B., Halasz,G.,
            Lotta,L.A., Murphy,A.J., Sleeman,M.W. and Gusarova,V.
  TITLE     Divergent role of Mitochondrial Amidoxime Reducing Component 1
            (MARC1) in human and mouse
  JOURNAL   PLoS Genet 20 (3), e1011179 (2024)
   PUBMED   38437227
  REMARK    GeneRIF: Divergent role of Mitochondrial Amidoxime Reducing
            Component 1 (MARC1) in human and mouse.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Wahl,B., Reichmann,D., Niks,D., Krompholz,N., Havemeyer,A.,
            Clement,B., Messerschmidt,T., Rothkegel,M., Biester,H., Hille,R.,
            Mendel,R.R. and Bittner,F.
  TITLE     Biochemical and spectroscopic characterization of the human
            mitochondrial amidoxime reducing components hmARC-1 and hmARC-2
            suggests the existence of a new molybdenum enzyme family in
            eukaryotes
  JOURNAL   J Biol Chem 285 (48), 37847-37859 (2010)
   PUBMED   20861021
  REMARK    GeneRIF: Arc1(MOSC-1) and Arc2(MOSC-2) proteins are monomeric in
            their active forms.
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Teslovich,T.M., Musunuru,K., Smith,A.V., Edmondson,A.C.,
            Stylianou,I.M., Koseki,M., Pirruccello,J.P., Ripatti,S.,
            Chasman,D.I., Willer,C.J., Johansen,C.T., Fouchier,S.W., Isaacs,A.,
            Peloso,G.M., Barbalic,M., Ricketts,S.L., Bis,J.C., Aulchenko,Y.S.,
            Thorleifsson,G., Feitosa,M.F., Chambers,J., Orho-Melander,M.,
            Melander,O., Johnson,T., Li,X., Guo,X., Li,M., Shin Cho,Y., Jin
            Go,M., Jin Kim,Y., Lee,J.Y., Park,T., Kim,K., Sim,X., Twee-Hee
            Ong,R., Croteau-Chonka,D.C., Lange,L.A., Smith,J.D., Song,K., Hua
            Zhao,J., Yuan,X., Luan,J., Lamina,C., Ziegler,A., Zhang,W.,
            Zee,R.Y., Wright,A.F., Witteman,J.C., Wilson,J.F., Willemsen,G.,
            Wichmann,H.E., Whitfield,J.B., Waterworth,D.M., Wareham,N.J.,
            Waeber,G., Vollenweider,P., Voight,B.F., Vitart,V.,
            Uitterlinden,A.G., Uda,M., Tuomilehto,J., Thompson,J.R., Tanaka,T.,
            Surakka,I., Stringham,H.M., Spector,T.D., Soranzo,N., Smit,J.H.,
            Sinisalo,J., Silander,K., Sijbrands,E.J., Scuteri,A., Scott,J.,
            Schlessinger,D., Sanna,S., Salomaa,V., Saharinen,J., Sabatti,C.,
            Ruokonen,A., Rudan,I., Rose,L.M., Roberts,R., Rieder,M.,
            Psaty,B.M., Pramstaller,P.P., Pichler,I., Perola,M., Penninx,B.W.,
            Pedersen,N.L., Pattaro,C., Parker,A.N., Pare,G., Oostra,B.A.,
            O'Donnell,C.J., Nieminen,M.S., Nickerson,D.A., Montgomery,G.W.,
            Meitinger,T., McPherson,R., McCarthy,M.I., McArdle,W., Masson,D.,
            Martin,N.G., Marroni,F., Mangino,M., Magnusson,P.K., Lucas,G.,
            Luben,R., Loos,R.J., Lokki,M.L., Lettre,G., Langenberg,C.,
            Launer,L.J., Lakatta,E.G., Laaksonen,R., Kyvik,K.O., Kronenberg,F.,
            Konig,I.R., Khaw,K.T., Kaprio,J., Kaplan,L.M., Johansson,A.,
            Jarvelin,M.R., Janssens,A.C., Ingelsson,E., Igl,W., Kees
            Hovingh,G., Hottenga,J.J., Hofman,A., Hicks,A.A., Hengstenberg,C.,
            Heid,I.M., Hayward,C., Havulinna,A.S., Hastie,N.D., Harris,T.B.,
            Haritunians,T., Hall,A.S., Gyllensten,U., Guiducci,C., Groop,L.C.,
            Gonzalez,E., Gieger,C., Freimer,N.B., Ferrucci,L., Erdmann,J.,
            Elliott,P., Ejebe,K.G., Doring,A., Dominiczak,A.F., Demissie,S.,
            Deloukas,P., de Geus,E.J., de Faire,U., Crawford,G., Collins,F.S.,
            Chen,Y.D., Caulfield,M.J., Campbell,H., Burtt,N.P.,
            Bonnycastle,L.L., Boomsma,D.I., Boekholdt,S.M., Bergman,R.N.,
            Barroso,I., Bandinelli,S., Ballantyne,C.M., Assimes,T.L.,
            Quertermous,T., Altshuler,D., Seielstad,M., Wong,T.Y., Tai,E.S.,
            Feranil,A.B., Kuzawa,C.W., Adair,L.S., Taylor,H.A. Jr.,
            Borecki,I.B., Gabriel,S.B., Wilson,J.G., Holm,H.,
            Thorsteinsdottir,U., Gudnason,V., Krauss,R.M., Mohlke,K.L.,
            Ordovas,J.M., Munroe,P.B., Kooner,J.S., Tall,A.R., Hegele,R.A.,
            Kastelein,J.J., Schadt,E.E., Rotter,J.I., Boerwinkle,E.,
            Strachan,D.P., Mooser,V., Stefansson,K., Reilly,M.P., Samani,N.J.,
            Schunkert,H., Cupples,L.A., Sandhu,M.S., Ridker,P.M., Rader,D.J.,
            van Duijn,C.M., Peltonen,L., Abecasis,G.R., Boehnke,M. and
            Kathiresan,S.
  TITLE     Biological, clinical and population relevance of 95 loci for blood
            lipids
  JOURNAL   Nature 466 (7307), 707-713 (2010)
   PUBMED   20686565
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Gruenewald,S., Wahl,B., Bittner,F., Hungeling,H., Kanzow,S.,
            Kotthaus,J., Schwering,U., Mendel,R.R. and Clement,B.
  TITLE     The fourth molybdenum containing enzyme mARC: cloning and
            involvement in the activation of N-hydroxylated prodrugs
  JOURNAL   J Med Chem 51 (24), 8173-8177 (2008)
   PUBMED   19053771
  REMARK    GeneRIF: molybdoprotein mARC1 is involved in the activation of
            N-hydroxylated prodrugs.
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA878171.1, AK290812.1, CB048738.1, CA439234.1 and AL445423.13.
            
            On Mar 6, 2009 this sequence version replaced NP_073583.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026043.1, BC010619.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000366910.10/
                                                  ENSP00000355877.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..337
                     /product="mitochondrial amidoxime-reducing component 1
                     precursor"
                     /note="MOSC domain-containing protein 1, mitochondrial;
                     MOCO sulphurase C-terminal domain containing 1; moco
                     sulfurase C-terminal domain-containing protein 1;
                     molybdenum cofactor sulfurase C-terminal domain-containing
                     protein 1"
                     /calculated_mol_wt=37368
     Site            21..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VT66.1)"
     Region          55..336
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
     Region          93..183
                     /region_name="MOSC N-terminal region.
                     /evidence=ECO:0000269|PubMed:30397129"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VT66.1)"
     CDS             1..337
                     /gene="MTARC1"
                     /gene_synonym="MARC1; MOSC1"
                     /coded_by="NM_022746.4:33..1046"
                     /db_xref="CCDS:CCDS1526.1"
                     /db_xref="GeneID:64757"
                     /db_xref="HGNC:HGNC:26189"
                     /db_xref="MIM:614126"
ORIGIN      
        1 mgaagssala rfvllaqsrp gwlgvaalgl tavalgavaw rrawptrrrr llqqvgtvaq
       61 lwiypvksck gvpvseaect amglrsgnlr drfwlvinqe gnmvtarqep rlvlisltcd
      121 gdtltlsaay tkdlllpikt pttnavhkcr vhgleiegrd cgeataqwit sflksqpyrl
      181 vhfephmrpr rphqiadlfr pkdqiaysdt spflilseas ladlnsrlek kvkatnfrpn
      241 ivisgcdvya edswdellig dvelkrvmac srcilttvdp dtgvmsrkep letlksyrqc
      301 dpserklygk splfgqyfvl enpgtikvgd pvyllgq
//
LOCUS       NP_055596               1594 aa            linear   PRI 27-APR-2025
DEFINITION  RB1-inducible coiled-coil protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_055596
VERSION     NP_055596.3
DBSOURCE    REFSEQ: accession NM_014781.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1594)
  AUTHORS   Eickhorst,C., Babic,R., Rush-Kittle,J., Lucya,L., Imam,F.L.,
            Sanchez-Martin,P., Hollenstein,D.M., Michaelis,J., Munch,C.,
            Meisinger,C., Slade,D., Gamez-Diaz,L. and Kraft,C.
  TITLE     FIP200 Phosphorylation Regulates Late Steps in Mitophagy
  JOURNAL   J Mol Biol 436 (15), 168631 (2024)
   PUBMED   38821350
  REMARK    GeneRIF: FIP200 Phosphorylation Regulates Late Steps in Mitophagy.
REFERENCE   2  (residues 1 to 1594)
  AUTHORS   Liang,J., Cai,H., Hou,C., Song,F., Jiang,Y., Wang,Z., Qiu,D.,
            Zhu,Y., Wang,F., Yu,D. and Hou,J.
  TITLE     METTL14 inhibits malignant progression of oral squamous cell
            carcinoma by targeting the autophagy-related gene RB1CC1 in an
            m6A-IGF2BP2-dependent manner
  JOURNAL   Clin Sci (Lond) 137 (17), 1373-1389 (2023)
   PUBMED   37615536
  REMARK    GeneRIF: METTL14 inhibits malignant progression of oral squamous
            cell carcinoma by targeting the autophagy-related gene RB1CC1 in an
            m6A-IGF2BP2-dependent manner.
REFERENCE   3  (residues 1 to 1594)
  AUTHORS   Yang,Y. and Klionsky,D.J.
  TITLE     A novel role of ATG9A and RB1CC1/FIP200 in mediating cell-death
            checkpoints to repress TNF cytotoxicity
  JOURNAL   Autophagy 19 (6), 1617-1618 (2023)
   PUBMED   36892222
  REMARK    GeneRIF: A novel role of ATG9A and RB1CC1/FIP200 in mediating
            cell-death checkpoints to repress TNF cytotoxicity.
REFERENCE   4  (residues 1 to 1594)
  AUTHORS   Yi,F., Cai,C., Ruan,B., Hao,M., Yeo,S.K., Haas,M., Yang,F.,
            Zhang,X. and Guan,J.L.
  TITLE     Regulation of RB1CC1/FIP200 stability and autophagy function by
            CREBBP-mediated acetylation in an intrinsically disordered region
  JOURNAL   Autophagy 19 (6), 1662-1677 (2023)
   PUBMED   36394358
  REMARK    GeneRIF: Regulation of RB1CC1/FIP200 stability and autophagy
            function by CREBBP-mediated acetylation in an intrinsically
            disordered region.
REFERENCE   5  (residues 1 to 1594)
  AUTHORS   Wen,J., Zellner,A., Braun,N.C., Bajaj,T., Gassen,N.C., Peitz,M. and
            Brustle,O.
  TITLE     Loss of function of FIP200 in human pluripotent stem cell-derived
            neurons leads to axonal pathology and hyperactivity
  JOURNAL   Transl Psychiatry 13 (1), 143 (2023)
   PUBMED   37137886
  REMARK    GeneRIF: Loss of function of FIP200 in human pluripotent stem
            cell-derived neurons leads to axonal pathology and hyperactivity.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1594)
  AUTHORS   Chano,T., Kontani,K., Teramoto,K., Okabe,H. and Ikegawa,S.
  TITLE     Truncating mutations of RB1CC1 in human breast cancer
  JOURNAL   Nat Genet 31 (3), 285-288 (2002)
   PUBMED   12068296
  REMARK    GeneRIF: RB1CC1 is frequently mutated in breast cancer and shows
            characteristics of a classical tumor-suppressor gene.
REFERENCE   7  (residues 1 to 1594)
  AUTHORS   Chano,T., Ikegawa,S., Saito-Ohara,F., Inazawa,J., Mabuchi,A.,
            Saeki,Y. and Okabe,H.
  TITLE     Isolation, characterization and mapping of the mouse and human
            RB1CC1 genes
  JOURNAL   Gene 291 (1-2), 29-34 (2002)
   PUBMED   12095676
REFERENCE   8  (residues 1 to 1594)
  AUTHORS   Chano,T., Ikegawa,S., Kontani,K., Okabe,H., Baldini,N. and Saeki,Y.
  TITLE     Identification of RB1CC1, a novel human gene that can induce RB1 in
            various human cells
  JOURNAL   Oncogene 21 (8), 1295-1298 (2002)
   PUBMED   11850849
REFERENCE   9  (residues 1 to 1594)
  AUTHORS   Ueda,H., Abbi,S., Zheng,C. and Guan,J.L.
  TITLE     Suppression of Pyk2 kinase and cellular activities by FIP200
  JOURNAL   J Cell Biol 149 (2), 423-430 (2000)
   PUBMED   10769033
REFERENCE   10 (residues 1 to 1594)
  AUTHORS   Maucuer,A., Camonis,J.H. and Sobel,A.
  TITLE     Stathmin interaction with a putative kinase and coiled-coil-forming
            protein domains
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3100-3104 (1995)
   PUBMED   7724523
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA326842.1, BC017556.1,
            AC113139.2, AC090814.2 and AB059622.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 30, 2007 this sequence version replaced NP_055596.2.
            
            Summary: The protein encoded by this gene interacts with signaling
            pathways to coordinately regulate cell growth, cell proliferation,
            apoptosis, autophagy, and cell migration. This tumor suppressor
            also enhances retinoblastoma 1 gene expression in cancer cells.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript matching the
            genomic sequence was available for the full length of the gene. The
            extent of this transcript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB059622.1, SRR1803611.125219.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000025008.10/ ENSP00000025008.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1594
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.23"
     Protein         1..1594
                     /product="RB1-inducible coiled-coil protein 1 isoform 1"
                     /note="200 kDa FAK family kinase-interacting protein;
                     RB1-inducible coiled-coil protein 1; FAK family
                     kinase-interacting protein of 200 kDa; phosphatase 1,
                     regulatory subunit 131"
                     /calculated_mol_wt=182961
     Region          2..76
                     /region_name="Ubl_RB1CC1"
                     /note="ubiquitin-like (Ubl) domain found in retinoblastoma
                     1-inducible coiled-coil protein 1 (RB1CC1) and similar
                     proteins; cd17060"
                     /db_xref="CDD:340580"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESK9; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESK9; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Region          <404..538
                     /region_name="ATG17_like"
                     /note="Autophagy protein ATG17-like domain; pfam04108"
                     /db_xref="CDD:427715"
     Region          566..569
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Region          638..673
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESK9; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Region          731..737
                     /region_name="FFAT. /evidence=ECO:0000269|PubMed:33124732"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            734
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:33124732; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Region          871..1375
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Site            1091
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESK9; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            1222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Region          1439..1588
                     /region_name="ATG11"
                     /note="Autophagy-related protein 11; pfam10377"
                     /db_xref="CDD:463063"
     Site            1484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     CDS             1..1594
                     /gene="RB1CC1"
                     /gene_synonym="ATG17; CC1; FIP200; PPP1R131"
                     /coded_by="NM_014781.5:528..5312"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34892.1"
                     /db_xref="GeneID:9821"
                     /db_xref="HGNC:HGNC:15574"
                     /db_xref="MIM:606837"
ORIGIN      
        1 mklyvflvnt gttltfdtel tvqtvadlkh aiqskykiai qhqvlvvngg ecmaadrrvc
       61 tysagtdtnp iflfnkemil cdrppaipkt tfstendmei kveeslmmpa vfhtvasrtq
      121 lalemyevak klcsfceglv hdehlqhqgw aaimanledc snsyqkllfk fesiysnylq
      181 siediklklt hlgtavsvma kipllecltr hsyreclgrl dslpehedse kaemkrstel
      241 vlspdmprtt neslltsfpk svehvspdta daesgkeire scqstvhqqd ettidtkdgd
      301 lpffnvslld winvqdrpnd veslvrkcfd smsrldprii rpfiaecrqt iakldnqnmk
      361 aikgledrly aldqmiascg rlvneqkela qgflanqkra enlkdasvlp dlclshanql
      421 mimlqnhrkl ldikqkctta kqelannlhv rlkwccfvml hadqdgeklq allrlviell
      481 ervkiveals tvpqmyclav vevvrrkmfi khyrewagal vkdgkrlyea ekskresfgk
      541 lfrksflrnr lfrgldswpp sfctqkprkf dcelpdislk dlqflqsfcp sevqpflrvp
      601 llcdfeplhq hvlalhnlvk aaqsldemsq titdllseqk asvsqtspqs assprmesta
      661 gittttsprt pppltvqdpl cpavcpleel spdsidahtf dfetiphpni eqtihqvsld
      721 ldslaespes dfmsavnefv ieenlsspnp isdpqspemm veslyssvin aidsrrmqdt
      781 nvcgkedfgd htslnvqler crvvaqdshf siqtikedlc hfrtfvqkeq cdfsnslkct
      841 aveirniiek vkcsleitlk ekhqkellsl kneyegkldg liketeenen kikklkgelv
      901 cleevlqnkd nefalvkhek eaviclqnek dqkllemeni mhsqnceike lkqsreivle
      961 dlkklhvend eklqllrael qsleqshlke ledtlqvrhi qefekvmtdh rvsleelkke
     1021 nqqiinqiqe shaeiiqeke kqlqelklkv sdlsdtrckl evelalkeae tdeikillee
     1081 sraqqketlk slleqetenl rteisklnqk iqdnnenyqv glaelrtlmt iekdqcisel
     1141 isrheeesni lkaelnkvts lhnqafeiek nlkeqiielq skldselsal erqkdekitq
     1201 qeekyeaiiq nlekdrqklv ssqeqdreql iqklncekde aiqtalkefk lerevvekel
     1261 lekvkhlenq iakspaidst rgdssslvae lqeklqeeka kfleqleeqe krkneemqnv
     1321 rtsliaeqqt nfntvltrek mrkeniindl sdklkstmqq qerdkdlies lsedrarlle
     1381 ekkkleeevs klrsssfvps pyvatapely gacapelpge sdrsavetad egrvdsamet
     1441 smmsvqenih mlseekqrim llertlqlke eenkrlnqrl msqsmssvss rhsekiaird
     1501 fqvgdlvlii lderhdnyvl ftvsptlyfl hseslpaldl kpgegasgas rrpwvlgkvm
     1561 ekeycqakka qnrfkvplgt kfyrvkavsw nkkv
//
LOCUS       NP_056117                633 aa            linear   PRI 27-APR-2025
DEFINITION  HAUS augmin-like complex subunit 5 [Homo sapiens].
ACCESSION   NP_056117 XP_049237 XP_937266 XP_937287 XP_947397 XP_950983
            XP_950991
VERSION     NP_056117.1
DBSOURCE    REFSEQ: accession NM_015302.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Zhang,W., Yang,C., Hu,Y., Yi,K., Xiao,W., Xu,X. and Chen,Z.
  TITLE     Comprehensive analysis of the correlation of the pan-cancer gene
            HAUS5 with prognosis and immune infiltration in liver cancer
  JOURNAL   Sci Rep 13 (1), 2409 (2023)
   PUBMED   36765148
  REMARK    GeneRIF: Comprehensive analysis of the correlation of the
            pan-cancer gene HAUS5 with prognosis and immune infiltration in
            liver cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Luo,J., Yang,B., Xin,G., Sun,M., Zhang,B., Guo,X., Jiang,Q. and
            Zhang,C.
  TITLE     The microtubule-associated protein EML3 regulates mitotic spindle
            assembly by recruiting the Augmin complex to spindle microtubules
  JOURNAL   J Biol Chem 294 (14), 5643-5656 (2019)
   PUBMED   30723163
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Cunha-Ferreira,I., Chazeau,A., Buijs,R.R., Stucchi,R., Will,L.,
            Pan,X., Adolfs,Y., van der Meer,C., Wolthuis,J.C., Kahn,O.I.,
            Schatzle,P., Altelaar,M., Pasterkamp,R.J., Kapitein,L.C. and
            Hoogenraad,C.C.
  TITLE     The HAUS Complex Is a Key Regulator of Non-centrosomal Microtubule
            Organization during Neuronal Development
  JOURNAL   Cell Rep 24 (4), 791-800 (2018)
   PUBMED   30044976
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Ding,Y., Herman,J.A., Toledo,C.M., Lang,J.M., Corrin,P.,
            Girard,E.J., Basom,R., Delrow,J.J., Olson,J.M. and Paddison,P.J.
  TITLE     ZNF131 suppresses centrosome fragmentation in glioblastoma
            stem-like cells through regulation of HAUS5
  JOURNAL   Oncotarget 8 (30), 48545-48562 (2017)
   PUBMED   28596487
  REMARK    GeneRIF: Our results suggest that GSCs differentially rely on
            ZNF131-dependent expression of HAUS5 as well as the Augmin/HAUS
            complex activity to maintain the integrity of centrosome function
            and viability.
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   7  (residues 1 to 633)
  AUTHORS   Hutchins,J.R., Toyoda,Y., Hegemann,B., Poser,I., Heriche,J.K.,
            Sykora,M.M., Augsburg,M., Hudecz,O., Buschhorn,B.A., Bulkescher,J.,
            Conrad,C., Comartin,D., Schleiffer,A., Sarov,M., Pozniakovsky,A.,
            Slabicki,M.M., Schloissnig,S., Steinmacher,I., Leuschner,M.,
            Ssykor,A., Lawo,S., Pelletier,L., Stark,H., Nasmyth,K.,
            Ellenberg,J., Durbin,R., Buchholz,F., Mechtler,K., Hyman,A.A. and
            Peters,J.M.
  TITLE     Systematic analysis of human protein complexes identifies
            chromosome segregation proteins
  JOURNAL   Science 328 (5978), 593-599 (2010)
   PUBMED   20360068
REFERENCE   8  (residues 1 to 633)
  AUTHORS   Lawo,S., Bashkurov,M., Mullin,M., Ferreria,M.G., Kittler,R.,
            Habermann,B., Tagliaferro,A., Poser,I., Hutchins,J.R., Hegemann,B.,
            Pinchev,D., Buchholz,F., Peters,J.M., Hyman,A.A., Gingras,A.C. and
            Pelletier,L.
  TITLE     HAUS, the 8-subunit human Augmin complex, regulates centrosome and
            spindle integrity
  JOURNAL   Curr Biol 19 (10), 816-826 (2009)
   PUBMED   19427217
REFERENCE   9  (residues 1 to 633)
  AUTHORS   Uehara,R., Nozawa,R.S., Tomioka,A., Petry,S., Vale,R.D., Obuse,C.
            and Goshima,G.
  TITLE     The augmin complex plays a critical role in spindle microtubule
            generation for mitotic progression and cytokinesis in human cells
  JOURNAL   Proc Natl Acad Sci U S A 106 (17), 6998-7003 (2009)
   PUBMED   19369198
REFERENCE   10 (residues 1 to 633)
  AUTHORS   Goshima,G., Mayer,M., Zhang,N., Stuurman,N. and Vale,R.D.
  TITLE     Augmin: a protein complex required for centrosome-independent
            microtubule generation within the spindle
  JOURNAL   J Cell Biol 181 (3), 421-429 (2008)
   PUBMED   18443220
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002115.1, BC064390.1 and AB020648.1.
            
            On or before Jun 29, 2007 this sequence version replaced
            XP_937287.1, XP_049237.2, XP_937266.1, XP_947397.1, XP_950991.1,
            XP_950983.1.
            
            Summary: HAUS5 is 1 of 8 subunits of the 390-kD human augmin
            complex, or HAUS complex. The augmin complex was first identified
            in Drosophila, and its name comes from the Latin verb 'augmentare,'
            meaning 'to increase.' The augmin complex is a microtubule-binding
            complex involved in microtubule generation within the mitotic
            spindle and is vital to mitotic spindle assembly (Goshima et al.,
            2008 [PubMed 18443220]; Uehara et al., 2009 [PubMed
            19369198]).[supplied by OMIM, Jun 2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.78718.1, AB020648.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000203166.10/ ENSP00000439056.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..633
                     /product="HAUS augmin-like complex subunit 5"
                     /calculated_mol_wt=71552
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O94927.2)"
     Region          7..619
                     /region_name="HAUS5"
                     /note="HAUS augmin-like complex subunit 5; pfam14817"
                     /db_xref="CDD:464332"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94927.2)"
     Region          264..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94927.2)"
     CDS             1..633
                     /gene="HAUS5"
                     /gene_synonym="dgt5; KIAA0841"
                     /coded_by="NM_015302.2:61..1962"
                     /db_xref="CCDS:CCDS42550.1"
                     /db_xref="GeneID:23354"
                     /db_xref="HGNC:HGNC:29130"
                     /db_xref="MIM:613432"
ORIGIN      
        1 melaqearel gcwaveemgv pvaarapest lrrlclgqga diwayilqhv hsqrtvkkir
       61 gnllwyghqd spqvrrklel eaavtrlrae iqeldqslel merdteaqdt ameqarqhtq
      121 dtqrralllr aqagamrrqq htlrdpmqrl qnqlrrlqdm erkakvdvtf gsltsaalgl
      181 epvvlrdvrt actlraqflq nlllpqakrg slptphddhf gtsyqqwlss vetlltnhpp
      241 ghvlaalehl aaereaeirs lcsgdglgdt eisrpqapdq sdssqtlpsm vhliqegwrt
      301 vgvlvsqrst llkerqvltq rlqglveeve rrvlgsserq vlilglrrcc lwtelkalhd
      361 qsqelqdaag hrqlllrelq akqqrilhwr qlveetqeqv rllikgnsas ktrlcrspge
      421 vlalvqrkvv ptfeavapqs rellrcleee vrhlphillg tllrhrpgel kplptvlpsi
      481 hqlhpasprg ssfialshkl glppgkasel llpaaaslrq dllllqdqrs lwcwdllhmk
      541 tslppglptq ellqiqasqe kqqkenlgqa lkrlekllkq aleripelqg ivgdwweqpg
      601 qaalseelcq glslpqwrlr wvqaqgalqk lcs
//
LOCUS       NP_000993                317 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein uL10 [Homo sapiens].
ACCESSION   NP_000993
VERSION     NP_000993.1
DBSOURCE    REFSEQ: accession NM_001002.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Ge,Y.L., Li,P.J., Bu,Y.R., Zhang,B., Xu,J., He,S.Y., Cao,Q.L.,
            Bai,Y.G., Ma,J., Zhang,L., Zhou,J. and Xie,M.J.
  TITLE     TNF-alpha and RPLP0 drive the apoptosis of endothelial cells and
            increase susceptibility to high-altitude pulmonary edema
  JOURNAL   Apoptosis 29 (9-10), 1600-1618 (2024)
   PUBMED   39110356
  REMARK    GeneRIF: TNF-alpha and RPLP0 drive the apoptosis of endothelial
            cells and increase susceptibility to high-altitude pulmonary edema.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Wang,Y.L., Zhao,W.W., Bai,S.M., Ma,Y., Yin,X.K., Feng,L.L.,
            Zeng,G.D., Wang,F., Feng,W.X., Zheng,J., Wang,Y.N., Zeng,B.,
            Liu,Q., Hung,M.C. and Wan,X.B.
  TITLE     DNA damage-induced paraspeckle formation enhances DNA repair and
            tumor radioresistance by recruiting ribosomal protein P0
  JOURNAL   Cell Death Dis 13 (8), 709 (2022)
   PUBMED   35974014
  REMARK    GeneRIF: DNA damage-induced paraspeckle formation enhances DNA
            repair and tumor radioresistance by recruiting ribosomal protein
            P0.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Borrello,M.T., Santofimia-Castano,P., Bocchio,M., Listi,A.,
            Fraunhoffer,N., Soubeyran,P., Chevet,E., Pin,C. and Iovanna,J.
  TITLE     NUPR1 interacts with eIF2alpha and is required for resolution of
            the ER stress response in pancreatic tissue
  JOURNAL   FEBS J 288 (13), 4081-4097 (2021)
   PUBMED   33403797
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Filipek,K., Michalec-Wawiorka,B., Boguszewska,A., Kmiecik,S. and
            Tchorzewski,M.
  TITLE     Phosphorylation of the N-terminal domain of ribosomal P-stalk
            protein uL10 governs its association with the ribosome
  JOURNAL   FEBS Lett 594 (18), 3002-3019 (2020)
   PUBMED   32668052
  REMARK    GeneRIF: Phosphorylation of the N-terminal domain of ribosomal
            P-stalk protein uL10 governs its association with the ribosome.
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Gress,T.M., Muller-Pillasch,F., Geng,M., Zimmerhackl,F.,
            Zehetner,G., Friess,H., Buchler,M., Adler,G. and Lehrach,H.
  TITLE     A pancreatic cancer-specific expression profile
  JOURNAL   Oncogene 13 (8), 1819-1830 (1996)
   PUBMED   8895530
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Rich,B.E. and Steitz,J.A.
  TITLE     Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
            cDNA clones, in vitro synthesis, and assembly
  JOURNAL   Mol Cell Biol 7 (11), 4065-4074 (1987)
   PUBMED   3323886
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Towbin,H., Ramjoue,H.P., Kuster,H., Liverani,D. and Gordon,J.
  TITLE     Monoclonal antibodies against eucaryotic ribosomes. Use to
            characterize a ribosomal protein not previously identified and
            antigenically related to the acidic phosphoproteins P1/P2
  JOURNAL   J Biol Chem 257 (21), 12709-12715 (1982)
   PUBMED   6182142
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BF131912.1, BC000087.2, BC019014.2 and AC004263.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein, which
            is the functional equivalent of the E. coli L10 ribosomal protein,
            belongs to the L10P family of ribosomal proteins. It is a neutral
            phosphoprotein with a C-terminal end that is nearly identical to
            the C-terminal ends of the acidic ribosomal phosphoproteins P1 and
            P2. The P0 protein can interact with P1 and P2 to form a pentameric
            complex consisting of P1 and P2 dimers, and a P0 monomer. The
            protein is located in the cytoplasm. Transcript variants derived
            from alternative splicing exist; they encode the same protein. As
            is typical for genes encoding ribosomal proteins, there are
            multiple processed pseudogenes of this gene dispersed through the
            genome. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the predominant transcript.
            It has a different 5' UTR than variant 2. They encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.187834.1,
                                           SRR5189664.41454.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392514.9/ ENSP00000376299.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.23"
     Protein         1..317
                     /product="large ribosomal subunit protein uL10"
                     /note="acidic ribosomal phosphoprotein P0; 60S acidic
                     ribosomal protein P0; 60S ribosomal protein L10E;
                     ribosomal protein, large, P0; neutral ribosomal
                     phosphoprotein P0"
                     /calculated_mol_wt=34142
     Region          1..317
                     /region_name="PTZ00135"
                     /note="60S acidic ribosomal protein P0; Provisional"
                     /db_xref="CDD:240285"
     Site            order(10..11,14,57..60,63)
                     /site_type="other"
                     /note="23S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:240221"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P14869; propagated from
                     UniProtKB/Swiss-Prot (P05388.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05388.1)"
     Site            order(96,116,120,139,142..143,146..147,149..152,170..172,
                     175..176,178..179,181)
                     /site_type="other"
                     /note="putative Interface with L7/L12 ribosomal proteins
                     [polypeptide binding]"
                     /db_xref="CDD:240221"
     Region          294..317
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05388.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P05388.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P05388.1)"
     CDS             1..317
                     /gene="RPLP0"
                     /gene_synonym="L10E; LP0; P0; PRLP0; RPP0; uL10"
                     /coded_by="NM_001002.4:78..1031"
                     /db_xref="CCDS:CCDS9193.1"
                     /db_xref="GeneID:6175"
                     /db_xref="HGNC:HGNC:10371"
                     /db_xref="MIM:180510"
ORIGIN      
        1 mpredratwk snyflkiiql lddypkcfiv gadnvgskqm qqirmslrgk avvlmgkntm
       61 mrkairghle nnpalekllp hirgnvgfvf tkedlteird mllankvpaa aragaiapce
      121 vtvpaqntgl gpektsffqa lgittkisrg tieilsdvql iktgdkvgas eatllnmlni
      181 spfsfglviq qvfdngsiyn pevlditeet lhsrflegvr nvasvclqig yptvasvphs
      241 iingykrvla lsvetdytfp laekvkafla dpsafvaaap vaaattaapa aaaapakvea
      301 keeseesded mgfglfd
//
LOCUS       NP_001306875             406 aa            linear   PRI 27-APR-2025
DEFINITION  5' exonuclease Apollo isoform b [Homo sapiens].
ACCESSION   NP_001306875 XP_005271187
VERSION     NP_001306875.1
DBSOURCE    REFSEQ: accession NM_001319946.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Sonmez,C., Toia,B., Eickhoff,P., Matei,A.M., El Beyrouthy,M.,
            Wallner,B., Douglas,M.E., de Lange,T. and Lottersberger,F.
  TITLE     DNA-PK controls Apollo's access to leading-end telomeres
  JOURNAL   Nucleic Acids Res 52 (8), 4313-4327 (2024)
   PUBMED   38407308
  REMARK    GeneRIF: DNA-PK controls Apollo's access to leading-end telomeres.
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Bories,C., Lejour,T., Adolphe,F., Kermasson,L., Couve,S.,
            Tanguy,L., Luszczewska,G., Watzky,M., Poillerat,V., Garnier,P.,
            Groisman,R., Ferlicot,S., Richard,S., Saparbaev,M., Revy,P., Gad,S.
            and Renaud,F.
  TITLE     DCLRE1B/Apollo germline mutations associated with renal cell
            carcinoma impair telomere protection
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (4), 167107 (2024)
   PUBMED   38430974
  REMARK    GeneRIF: DCLRE1B/Apollo germline mutations associated with renal
            cell carcinoma impair telomere protection.
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Li,L., Wang,F., Deng,Z., Zhang,G., Zhu,L., Zhao,Z. and Liu,R.
  TITLE     DCLRE1B promotes tumor progression and predicts immunotherapy
            response through METTL3-mediated m6A modification in pancreatic
            cancer
  JOURNAL   BMC Cancer 23 (1), 1073 (2023)
   PUBMED   37936074
  REMARK    GeneRIF: DCLRE1B promotes tumor progression and predicts
            immunotherapy response through METTL3-mediated m6A modification in
            pancreatic cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Yosaatmadja,Y., Baddock,H.T., Newman,J.A., Bielinski,M.,
            Gavard,A.E., Mukhopadhyay,S.M.M., Dannerfjord,A.A., Schofield,C.J.,
            McHugh,P.J. and Gileadi,O.
  TITLE     Structural and mechanistic insights into the Artemis endonuclease
            and strategies for its inhibition
  JOURNAL   Nucleic Acids Res 49 (16), 9310-9326 (2021)
   PUBMED   34387696
  REMARK    GeneRIF: Structural and mechanistic insights into the Artemis
            endonuclease and strategies for its inhibition.
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Baddock,H.T., Newman,J.A., Yosaatmadja,Y., Bielinski,M.,
            Schofield,C.J., Gileadi,O. and McHugh,P.J.
  TITLE     A phosphate binding pocket is a key determinant of exo- versus
            endo-nucleolytic activity in the SNM1 nuclease family
  JOURNAL   Nucleic Acids Res 49 (16), 9294-9309 (2021)
   PUBMED   34387694
  REMARK    GeneRIF: A phosphate binding pocket is a key determinant of exo-
            versus endo-nucleolytic activity in the SNM1 nuclease family.
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Lenain,C., Bauwens,S., Amiard,S., Brunori,M., Giraud-Panis,M.J. and
            Gilson,E.
  TITLE     The Apollo 5' exonuclease functions together with TRF2 to protect
            telomeres from DNA repair
  JOURNAL   Curr Biol 16 (13), 1303-1310 (2006)
   PUBMED   16730175
  REMARK    GeneRIF: SNM1B (Apollo) protein exhibits a 5'-to-3' DNA exonuclease
            activity and functions together with TRF2 to protect telomeres from
            damage and fusion.
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Freibaum,B.D. and Counter,C.M.
  TITLE     hSnm1B is a novel telomere-associated protein
  JOURNAL   J Biol Chem 281 (22), 15033-15036 (2006)
   PUBMED   16606622
  REMARK    GeneRIF: the C terminus of Snm1B was shown to interact with the TRF
            homology domain of TRF2 indicating that Snm1B is likely recruited
            to the telomere via interaction with the double-stranded
            telomere-binding protein TRF2
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Ishiai,M., Kimura,M., Namikoshi,K., Yamazoe,M., Yamamoto,K.,
            Arakawa,H., Agematsu,K., Matsushita,N., Takeda,S., Buerstedde,J.M.
            and Takata,M.
  TITLE     DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear
            focus formation
  JOURNAL   Mol Cell Biol 24 (24), 10733-10741 (2004)
   PUBMED   15572677
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Demuth,I., Digweed,M. and Concannon,P.
  TITLE     Human SNM1B is required for normal cellular response to both DNA
            interstrand crosslink-inducing agents and ionizing radiation
  JOURNAL   Oncogene 23 (53), 8611-8618 (2004)
   PUBMED   15467758
  REMARK    GeneRIF: siRNA knockdown of hSNM1B rendered cells sensitive to
            ionizing radiation, suggesting the possibility of hSNM1B
            involvement in homologous recombination repair of double-strand
            breaks arising as intermediates of ICL repair
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Dronkert,M.L., de Wit,J., Boeve,M., Vasconcelos,M.L., van Steeg,H.,
            Tan,T.L., Hoeijmakers,J.H. and Kanaar,R.
  TITLE     Disruption of mouse SNM1 causes increased sensitivity to the DNA
            interstrand cross-linking agent mitomycin C
  JOURNAL   Mol Cell Biol 20 (13), 4553-4561 (2000)
   PUBMED   10848582
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR005221.1, CR936679.1 and
            AI669133.1.
            
            On Feb 6, 2016 this sequence version replaced XP_005271187.1.
            
            Summary: DNA interstrand cross-links prevent strand separation,
            thereby physically blocking transcription, replication, and
            segregation of DNA. DCLRE1B is one of several evolutionarily
            conserved genes involved in repair of interstrand cross-links
            (Dronkert et al., 2000 [PubMed 10848582]).[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (2) lacks an alternate 5' exon
            compared to variant 1. The resulting isoform (b) is shorter at the
            N-terminus compared to isoform a. Variants 2 and 3 both encode the
            same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.167069.1, CR936679.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..406
                     /product="5' exonuclease Apollo isoform b"
                     /EC_number="3.5.2.6"
                     /note="DNA cross-link repair 1B (PSO2 homolog, S.
                     cerevisiae); 5' exonuclease Apollo; SNM1 homolog B;
                     beta-lactamase DCLRE1B"
                     /calculated_mol_wt=45681
     Region          <1..25
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
     Region          90..173
                     /region_name="DRMBL"
                     /note="DNA repair metallo-beta-lactamase; pfam07522"
                     /db_xref="CDD:429512"
     Region          370..403
                     /region_name="apollo_TRF2_binding"
                     /note="TRF2-binding region of apollo and similar proteins;
                     cd11662"
                     /db_xref="CDD:212560"
     Site            order(372,374..384)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:212560"
     CDS             1..406
                     /gene="DCLRE1B"
                     /gene_synonym="APOLLO; DKCB8; SNM1B; SNMIB"
                     /coded_by="NM_001319946.2:474..1694"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:64858"
                     /db_xref="HGNC:HGNC:17641"
                     /db_xref="MIM:609683"
ORIGIN      
        1 mlkepaltlg kqihtlyldn tncnpalvlp srqeaahqiv qlirkhpqhn ikiglyslgk
       61 eslleqlale fqtwvvlspr rlelvqllgl advftveeka grihavdhme ichsnmlrwn
      121 qthptiailp tsrkihsshp dihvipysdh ssyselrafv aalkpcqvvp ivsrrpcggf
      181 qdslsprisv plipdsvqqy mssssrkpsl lwllerrlkr prtqgvvfes peesadqsqa
      241 drdskkakke klspwpadle kqpshhplri kkqlfpdlys kewnkavpfc esqkrvtmlt
      301 aplgfsvhlr stdeefisqk treeiglgsp lvpmgdddgg peatgnqsaw mghgsplshs
      361 skgtpllate frglalkyll tpvnffqagy ssrrfdqqve kyhkpc
//
LOCUS       NP_071750                486 aa            linear   PRI 27-APR-2025
DEFINITION  dipeptidase 2 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_071750
VERSION     NP_071750.1
DBSOURCE    REFSEQ: accession NM_022355.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Wang,Y., Zhang,T., Du,H., Yang,M., Xie,G., Liu,T., Deng,S.,
            Yuan,W., He,S., Wu,D. and Xu,Y.
  TITLE     Dipeptidase-2 is a prognostic marker in lung adenocarcinoma that is
            correlated with its sensitivity to cisplatin
  JOURNAL   Oncol Rep 50 (2) (2023)
   PUBMED   37449493
  REMARK    GeneRIF: Dipeptidase-2 is a prognostic marker in lung
            adenocarcinoma that is correlated with its sensitivity to
            cisplatin.
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Hayashi,K., Longenecker,K.L., Koenig,P., Prashar,A., Hampl,J.,
            Stoll,V. and Vivona,S.
  TITLE     Structure of human DPEP3 in complex with the SC-003 antibody Fab
            fragment reveals basis for lack of dipeptidase activity
  JOURNAL   J Struct Biol 211 (1), 107512 (2020)
   PUBMED   32325220
REFERENCE   3  (residues 1 to 486)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Willer,C.J., Sanna,S., Jackson,A.U., Scuteri,A., Bonnycastle,L.L.,
            Clarke,R., Heath,S.C., Timpson,N.J., Najjar,S.S., Stringham,H.M.,
            Strait,J., Duren,W.L., Maschio,A., Busonero,F., Mulas,A., Albai,G.,
            Swift,A.J., Morken,M.A., Narisu,N., Bennett,D., Parish,S., Shen,H.,
            Galan,P., Meneton,P., Hercberg,S., Zelenika,D., Chen,W.M., Li,Y.,
            Scott,L.J., Scheet,P.A., Sundvall,J., Watanabe,R.M., Nagaraja,R.,
            Ebrahim,S., Lawlor,D.A., Ben-Shlomo,Y., Davey-Smith,G.,
            Shuldiner,A.R., Collins,R., Bergman,R.N., Uda,M., Tuomilehto,J.,
            Cao,A., Collins,F.S., Lakatta,E., Lathrop,G.M., Boehnke,M.,
            Schlessinger,D., Mohlke,K.L. and Abecasis,G.R.
  TITLE     Newly identified loci that influence lipid concentrations and risk
            of coronary artery disease
  JOURNAL   Nat Genet 40 (2), 161-169 (2008)
   PUBMED   18193043
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Habib,G.M., Shi,Z.Z., Cuevas,A.A. and Lieberman,M.W.
  TITLE     Identification of two additional members of the membrane-bound
            dipeptidase family
  JOURNAL   FASEB J 17 (10), 1313-1315 (2003)
   PUBMED   12738806
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP299049.1, AJ295149.1 and CB528462.1.
            
            Summary: DPEP2 belongs to the membrane-bound dipeptidase (EC
            3.4.13.19) family. These enzymes hydrolyze a variety of dipeptides,
            including leukotriene D4, the beta-lactam ring of some antibiotics,
            and cystinyl-bis-glycine (cys-bis-gly) formed during glutathione
            degradation (Habib et al., 2003 [PubMed 12738806]).[supplied by
            OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ295149.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393847.6/ ENSP00000377430.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..486
                     /product="dipeptidase 2 isoform 1 precursor"
                     /EC_number="3.4.13.19"
                     /calculated_mol_wt=49919
     sig_peptide     1..32
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A9.3)"
                     /calculated_mol_wt=3464
     mat_peptide     33..463
                     /product="Dipeptidase 2. /id=PRO_0000231603"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A9.3)"
                     /calculated_mol_wt=47446
     Region          79..399
                     /region_name="Peptidase_M19"
                     /note="Membrane dipeptidase (Peptidase family M19);
                     pfam01244"
                     /db_xref="CDD:395996"
     Site            order(89,91,135,188,261,282,293,351,354)
                     /site_type="active"
                     /db_xref="CDD:238626"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A9.3)"
     Site            order(137,146..148,150..151,154,158,198..199,201..202,
                     205..206)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238626"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A9.3)"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A9.3)"
     CDS             1..486
                     /gene="DPEP2"
                     /gene_synonym="MBD2"
                     /coded_by="NM_022355.4:156..1616"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10857.1"
                     /db_xref="GeneID:64174"
                     /db_xref="HGNC:HGNC:23028"
                     /db_xref="MIM:609925"
ORIGIN      
        1 mqpsglegpg tfgrwpllsl lllllllqpv tcayttpgpp ralttlgapr ahtmpgtyap
       61 sttlsspstq glqeqaralm rdfplvdghn dlplvlrqvy qkglqdvnlr nfsygqtsld
      121 rlrdglvgaq fwsayvpcqt qdrdalrltl eqidlirrmc asyselelvt sakalndtqk
      181 lacligvegg hsldnslsil rtfymlgvry ltlthtcntp waessakgvh sfynnisglt
      241 dfgekvvaem nrlgmmvdls hvsdavarra levsqapvif shsaargvcn sarnvpddil
      301 qllkknggvv mvslsmgviq cnpsanvstv adhfdhikav igskfigigg dydgagkfpq
      361 gledvstypv lieellsrgw seeelqgvlr gnllrvfrqv ekvqeenkwq spledkfpde
      421 qlssschsdl srlrqrqslt sgqelteipi hwtaklpakw svsessphma pvlavvatfp
      481 vlilwl
//
LOCUS       NP_060083                566 aa            linear   PRI 27-APR-2025
DEFINITION  protein downstream neighbor of Son [Homo sapiens].
ACCESSION   NP_060083
VERSION     NP_060083.1
DBSOURCE    REFSEQ: accession NM_017613.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Evrin,C., Alvarez,V., Ainsworth,J., Fujisawa,R., Alabert,C. and
            Labib,K.P.
  TITLE     DONSON is required for CMG helicase assembly in the mammalian cell
            cycle
  JOURNAL   EMBO Rep 24 (11), e57677 (2023)
   PUBMED   37781960
  REMARK    GeneRIF: DONSON is required for CMG helicase assembly in the
            mammalian cell cycle.
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Kingsley,G., Skagia,A., Passaretti,P., Fernandez-Cuesta,C.,
            Reynolds-Winczura,A., Koscielniak,K. and Gambus,A.
  TITLE     DONSON facilitates Cdc45 and GINS chromatin association and is
            essential for DNA replication initiation
  JOURNAL   Nucleic Acids Res 51 (18), 9748-9763 (2023)
   PUBMED   37638758
  REMARK    GeneRIF: DONSON facilitates Cdc45 and GINS chromatin association
            and is essential for DNA replication initiation.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Hashimoto,Y., Sadano,K., Miyata,N., Ito,H. and Tanaka,H.
  TITLE     Novel role of DONSON in CMG helicase assembly during vertebrate DNA
            replication initiation
  JOURNAL   EMBO J 42 (17), e114131 (2023)
   PUBMED   37458194
  REMARK    GeneRIF: Novel role of DONSON in CMG helicase assembly during
            vertebrate DNA replication initiation.
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Zhang,J., Bellani,M.A., James,R.C., Pokharel,D., Zhang,Y.,
            Reynolds,J.J., McNee,G.S., Jackson,A.P., Stewart,G.S. and
            Seidman,M.M.
  TITLE     DONSON and FANCM associate with different replisomes distinguished
            by replication timing and chromatin domain
  JOURNAL   Nat Commun 11 (1), 3951 (2020)
   PUBMED   32769987
  REMARK    GeneRIF: DONSON and FANCM associate with different replisomes
            distinguished by replication timing and chromatin domain.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Zou,Z., Dong,Y.S., Liu,J.M., Zhao,Z.H., Li,G. and Liu,D.D.
  TITLE     Circ-DONSON promotes malignant progression of glioma through
            modulating FOXO3
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (2), 749-757 (2020)
   PUBMED   32016978
  REMARK    GeneRIF: Circ-DONSON promotes malignant progression of glioma
            through modulating FOXO3.
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Denoeud,F., Kapranov,P., Ucla,C., Frankish,A., Castelo,R.,
            Drenkow,J., Lagarde,J., Alioto,T., Manzano,C., Chrast,J., Dike,S.,
            Wyss,C., Henrichsen,C.N., Holroyd,N., Dickson,M.C., Taylor,R.,
            Hance,Z., Foissac,S., Myers,R.M., Rogers,J., Hubbard,T., Harrow,J.,
            Guigo,R., Gingeras,T.R., Antonarakis,S.E. and Reymond,A.
  TITLE     Prominent use of distal 5' transcription start sites and discovery
            of a large number of additional exons in ENCODE regions
  JOURNAL   Genome Res 17 (6), 746-759 (2007)
   PUBMED   17567994
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Wynn,S.L., Fisher,R.A., Pagel,C., Price,M., Liu,Q.Y., Khan,I.M.,
            Zammit,P., Dadrah,K., Mazrani,W., Kessling,A., Lee,J.S. and
            Buluwela,L.
  TITLE     Organization and conservation of the GART/SON/DONSON locus in mouse
            and human genomes
  JOURNAL   Genomics 68 (1), 57-62 (2000)
   PUBMED   10950926
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Slavov,D., Hattori,M., Sakaki,Y., Rosenthal,A., Shimizu,N.,
            Minoshima,S., Kudoh,J., Yaspo,M.L., Ramser,J., Reinhardt,R.,
            Reimer,C., Clancy,K., Rynditch,A. and Gardiner,K.
  TITLE     Criteria for gene identification and features of genome
            organization: analysis of 6.5 Mb of DNA sequence from human
            chromosome 21
  JOURNAL   Gene 247 (1-2), 215-232 (2000)
   PUBMED   10773462
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI463648.1, BC048266.1, BM451848.1, AP000304.1 and BM679236.1.
            
            Summary: This gene lies downstream of the SON gene and spans 10 kb
            on chromosome 21. The function of this gene is unknown. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.679886.1,
                                           SRR1163658.280858.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303071.10/ ENSP00000307143.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..566
                     /product="protein downstream neighbor of Son"
                     /note="downstream neighbor of SON"
                     /calculated_mol_wt=62616
     Region          1..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYP3.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYP3.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYP3.2)"
     CDS             1..566
                     /gene="DONSON"
                     /gene_synonym="B17; C21orf60; MIMIS; MISSLA"
                     /coded_by="NM_017613.4:44..1744"
                     /db_xref="CCDS:CCDS13632.1"
                     /db_xref="GeneID:29980"
                     /db_xref="HGNC:HGNC:2993"
                     /db_xref="MIM:611428"
ORIGIN      
        1 malsvpgysp gfrkppevvr lrrkrarsrg aaaspprelt epaarraalv aglplrpfpa
       61 aggrgggsgg gpaaarrnpf arldnrprva aeppdgpare qpeapvpfld snqendllwe
      121 ekfperttvt elpqtshvsf sepdipssks telpvdwsik trllftssqp ftwadhlkaq
      181 eeaqglvqhc ratevtlpks iqdpklssel rctfqqsliy wlhpalswlp lfprigadrk
      241 magktspwsn datlqhvlms dwsvsftsly nllktklcpy fyvctyqftv lfraaglags
      301 dlitalispt trglreamrn egiefslpli kesghkketa sgtslgygee qaisdedeee
      361 sfswleemgv qdkikkpdil siklrkekhe vqmdhrpesv vlvkgintft llnflinsks
      421 lvatsgpqag lpptllspva frgatmqmlk arsvnvktqa lsgyrdqfsl eitgpimphs
      481 lhsltmllks sqsgsfsavl ypheptavfn iclqmdkvld mevvhkeltn cglhpntleq
      541 lsqipllgks slrnvvlrdy iynwrs
//
LOCUS       NP_001317240             695 aa            linear   PRI 27-APR-2025
DEFINITION  segment polarity protein dishevelled homolog DVL-1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001317240 XP_005244788
VERSION     NP_001317240.1
DBSOURCE    REFSEQ: accession NM_001330311.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Carr,H.S., Zuo,Y. and Frost,J.A.
  TITLE     The Wnt pathway protein Dvl1 targets somatostatin receptor 2 for
            lysosome-dependent degradation
  JOURNAL   J Biol Chem 299 (5), 104645 (2023)
   PUBMED   36965619
  REMARK    GeneRIF: The Wnt pathway protein Dvl1 targets somatostatin receptor
            2 for lysosome-dependent degradation.
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Caliskan,C., Yuce,Z. and Ogun Sercan,H.
  TITLE     Dvl proteins regulate SMAD1, AHR, mTOR, BRD7 protein expression
            while differentially regulating canonical and non-canonical Wnt
            signaling pathways in CML cell lines
  JOURNAL   Gene 854, 147109 (2023)
   PUBMED   36509295
  REMARK    GeneRIF: Dvl proteins regulate SMAD1, AHR, mTOR, BRD7 protein
            expression while differentially regulating canonical and
            non-canonical Wnt signaling pathways in CML cell lines.
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Pruller,J., Figeac,N. and Zammit,P.S.
  TITLE     DVL1 and DVL3 require nuclear localisation to regulate
            proliferation in human myoblasts
  JOURNAL   Sci Rep 12 (1), 8388 (2022)
   PUBMED   35589804
  REMARK    GeneRIF: DVL1 and DVL3 require nuclear localisation to regulate
            proliferation in human myoblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Bukovac,A., Dragicevic,K., Kafka,A., Oreskovic,D.,
            Cesarec-Augustinovic,S. and Pecina-Slaus,N.
  TITLE     Decoding the Role of DVL1 in Intracranial Meningioma
  JOURNAL   Int J Mol Sci 22 (21), 11996 (2021)
   PUBMED   34769425
  REMARK    GeneRIF: Decoding the Role of DVL1 in Intracranial Meningioma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Chen,Z., Liu,X., Liu,F., Zhang,G., Tu,H., Lin,W. and Lin,H.
  TITLE     Identification of 4-methylation driven genes based prognostic
            signature in thyroid cancer: an integrative analysis based on the
            methylmix algorithm
  JOURNAL   Aging (Albany NY) 13 (16), 20164-20178 (2021)
   PUBMED   34456184
  REMARK    GeneRIF: Identification of 4-methylation driven genes based
            prognostic signature in thyroid cancer: an integrative analysis
            based on the methylmix algorithm.
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Steitz,S.A., Tsang,M. and Sussman,D.J.
  TITLE     Wnt-mediated relocalization of dishevelled proteins
  JOURNAL   In Vitro Cell Dev Biol Anim 32 (7), 441-445 (1996)
   PUBMED   8856345
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Pizzuti,A., Amati,F., Calabrese,G., Mari,A., Colosimo,A.,
            Silani,V., Giardino,L., Ratti,A., Penso,D., Calza,L., Palka,G.,
            Scarlato,G., Novelli,G. and Dallapiccola,B.
  TITLE     cDNA characterization and chromosomal mapping of two human
            homologues of the Drosophila dishevelled polarity gene
  JOURNAL   Hum Mol Genet 5 (7), 953-958 (1996)
   PUBMED   8817329
REFERENCE   8  (residues 1 to 695)
  AUTHORS   Pizzuti,A., Novelli,G., Mari,A., Ratti,A., Colosimo,A., Amati,F.,
            Penso,D., Sangiuolo,F., Calabrese,G., Palka,G., Silani,V.,
            Gennarelli,M., Mingarelli,R., Scarlato,G., Scambler,P. and
            Dallapiccola,B.
  TITLE     Human homologue sequences to the Drosophila dishevelled
            segment-polarity gene are deleted in the DiGeorge syndrome
  JOURNAL   Am J Hum Genet 58 (4), 722-729 (1996)
   PUBMED   8644734
REFERENCE   9  (residues 1 to 695)
  AUTHORS   Klingensmith,J., Nusse,R. and Perrimon,N.
  TITLE     The Drosophila segment polarity gene dishevelled encodes a novel
            protein required for response to the wingless signal
  JOURNAL   Genes Dev 8 (1), 118-130 (1994)
   PUBMED   8288125
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Roifman,M., Brunner,H., Lohr,J., Mazzeu,J. and Chitayat,D.
  TITLE     Autosomal Dominant Robinow Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25577943
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139287.24.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 23, 2016 this sequence version replaced XP_005244788.1.
            
            Summary: DVL1, the human homolog of the Drosophila dishevelled gene
            (dsh) encodes a cytoplasmic phosphoprotein that regulates cell
            proliferation, acting as a transducer molecule for developmental
            processes, including segmentation and neuroblast specification.
            DVL1 is a candidate gene for neuroblastomatous transformation. The
            Schwartz-Jampel syndrome and Charcot-Marie-Tooth disease type 2A
            have been mapped to the same region as DVL1. The phenotypes of
            these diseases may be consistent with defects which might be
            expected from aberrant expression of a DVL gene during development.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378888.10/ ENSP00000368166.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..695
                     /product="segment polarity protein dishevelled homolog
                     DVL-1 isoform 1"
                     /note="dishevelled 1 (homologous to Drosophila dsh);
                     dishevelled, dsh homolog 1; segment polarity protein
                     dishevelled homolog DVL-1; DSH homolog 1; dishevelled-1"
                     /calculated_mol_wt=75056
     Region          1..85
                     /region_name="DAX"
                     /note="Domain present in Dishevelled and axin; smart00021"
                     /db_xref="CDD:197474"
     Region          89..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14640.2)"
     Region          90..247
                     /region_name="Dishevelled"
                     /note="Dishevelled specific domain; pfam02377"
                     /db_xref="CDD:460544"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVB9; propagated from
                     UniProtKB/Swiss-Prot (O14640.2)"
     Region          251..337
                     /region_name="PDZ_Dishevelled-like"
                     /note="PDZ domain of segment polarity protein dishevelled
                     homolog DVL1, DVL2, DVL3, and related domains; cd06717"
                     /db_xref="CDD:467201"
     Site            order(261..267,281,284,314,318,321..322)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467201"
     Region          417..499
                     /region_name="DEP_dishevelled"
                     /note="DEP (Dishevelled, Egl-10, and Pleckstrin) domain
                     found in dishevelled-like proteins. Dishevelled-like
                     proteins play a key role in the transduction of the Wnt
                     signal from the cell surface to the nucleus, which in turn
                     is an important regulatory pathway...; cd04438"
                     /db_xref="CDD:239885"
     Region          503..685
                     /region_name="Dsh_C"
                     /note="Segment polarity protein dishevelled (Dsh) C
                     terminal; pfam12316"
                     /db_xref="CDD:463531"
     Region          543..667
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14640.2)"
     CDS             1..695
                     /gene="DVL1"
                     /gene_synonym="DRS2; DVL; DVL1L1; DVL1P1"
                     /coded_by="NM_001330311.2:354..2441"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS81252.1"
                     /db_xref="GeneID:1855"
                     /db_xref="HGNC:HGNC:3084"
                     /db_xref="MIM:601365"
ORIGIN      
        1 maetkiiyhm deeetpylvk lpvapervtl adfknvlsnr pvhaykfffk smdqdfgvvk
       61 eeifddnakl pcfngrvvsw lvlaegahsd agsqgtdsht dlppplertg gigdsrppsf
      121 hpnvassrdg mdnetgtesm vshrrerarr rnreeaartn ghprgdrrrd vglppdsast
      181 alsselesss fvdsdedgst srlsssteqs tssrlirkhk rrrrkqrlrq adrassfssi
      241 tdstmslniv tvtlnmerhh flgisivgqs ndrgdggiyi gsimkggava adgriepgdm
      301 llqvndvnfe nmsnddavrv lreivsqtgp isltvakcwd ptprsyftvp radpvrpidp
      361 aawlshtaal tgalprygts pcssavtrts sssltssvpg apqleeaplt vksdmsavvr
      421 vmqlpdsgle irdrmwlkit ianavigadv vdwlythveg fkerrearky assllkhgfl
      481 rhtvnkitfs eqcyyvfgdl csnlatlnln sgssgtsdqd tlaplphpaa pwplgqgypy
      541 qypgpppcfp payqdpgfsy gsgstgsqqs egskssgstr ssrrapgrek erraagaggs
      601 gsesdhtaps gvgsswrerp agqlsrgssp rsqasatapg lppphpttka ytvvggppgg
      661 ppvrelaavp peltgsrqsf qkamgnpcef fvdim
//
LOCUS       NP_001357265             585 aa            linear   PRI 27-APR-2025
DEFINITION  protein phosphatase EYA1 isoform 7 [Homo sapiens].
ACCESSION   NP_001357265 XP_016868699
VERSION     NP_001357265.1
DBSOURCE    REFSEQ: accession NM_001370336.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Shao,H., Li,Y., Zhao,H., Lin,K., Gao,Y., Ming,C. and Ma,J.
  TITLE     [Clinical phenotypic and genetic analysis of syndrome families with
            EYA1 gene variants]
  JOURNAL   Lin Chuang Er Bi Yan Hou Tou Jing Wai Ke Za Zhi 38 (7), 636-640
            (2024)
   PUBMED   38973045
  REMARK    GeneRIF: [Clinical phenotypic and genetic analysis of syndrome
            families with EYA1 gene variants].
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Zhang,H., Gao,J., Wang,H., Liu,M., Lu,S., Xu,H., Tang,W. and
            Zheng,G.
  TITLE     Novel likely pathogenic variant in the EYA1 gene causing Branchio
            oto renal syndrome and the exploration of pathogenic mechanisms
  JOURNAL   BMC Med Genomics 17 (1), 89 (2024)
   PUBMED   38627775
  REMARK    GeneRIF: Novel likely pathogenic variant in the EYA1 gene causing
            Branchio oto renal syndrome and the exploration of pathogenic
            mechanisms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Wang,F., Zhang,R., Jian,J., Sun,Y. and Li,Q.
  TITLE     Identification and Functional Study of Enhancers of EYA1: The
            Causative Gene of Branchio-Oto-Renal Syndrome
  JOURNAL   Dev Neurosci 46 (5), 333-340 (2024)
   PUBMED   38228108
  REMARK    GeneRIF: Identification and Functional Study of Enhancers of EYA1:
            The Causative Gene of Branchio-Oto-Renal Syndrome.
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Yalcouye,A., Traore,O., Diarra,S., Schrauwen,I., Esoh,K.,
            Kadlubowska,M.K., Bharadwaj,T., Adadey,S.M., Keita,M., Guinto,C.O.,
            Leal,S.M., Landoure,G. and Wonkam,A.
  TITLE     A monoallelic variant in EYA1 is associated with Branchio-Otic
            syndrome in a Malian family
  JOURNAL   Mol Genet Genomic Med 10 (7), e1995 (2022)
   PUBMED   35698919
  REMARK    GeneRIF: A monoallelic variant in EYA1 is associated with
            Branchio-Otic syndrome in a Malian family.
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Pignoni,F., Hu,B., Zavitz,K.H., Xiao,J., Garrity,P.A. and
            Zipursky,S.L.
  TITLE     The eye-specification proteins So and Eya form a complex and
            regulate multiple steps in Drosophila eye development
  JOURNAL   Cell 91 (7), 881-891 (1997)
   PUBMED   9428512
  REMARK    Erratum:[Cell 1998 Feb 20;92(4):following 585]
REFERENCE   6  (residues 1 to 585)
  AUTHORS   Abdelhak,S., Kalatzis,V., Heilig,R., Compain,S., Samson,D.,
            Vincent,C., Levi-Acobas,F., Cruaud,C., Le Merrer,M., Mathieu,M.,
            Konig,R., Vigneron,J., Weissenbach,J., Petit,C. and Weil,D.
  TITLE     Clustering of mutations responsible for branchio-oto-renal (BOR)
            syndrome in the eyes absent homologous region (eyaHR) of EYA1
  JOURNAL   Hum Mol Genet 6 (13), 2247-2255 (1997)
   PUBMED   9361030
REFERENCE   7  (residues 1 to 585)
  AUTHORS   Abdelhak,S., Kalatzis,V., Heilig,R., Compain,S., Samson,D.,
            Vincent,C., Weil,D., Cruaud,C., Sahly,I., Leibovici,M.,
            Bitner-Glindzicz,M., Francis,M., Lacombe,D., Vigneron,J.,
            Charachon,R., Boven,K., Bedbeder,P., Van Regemorter,N.,
            Weissenbach,J. and Petit,C.
  TITLE     A human homologue of the Drosophila eyes absent gene underlies
            branchio-oto-renal (BOR) syndrome and identifies a novel gene
            family
  JOURNAL   Nat Genet 15 (2), 157-164 (1997)
   PUBMED   9020840
REFERENCE   8  (residues 1 to 585)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
REFERENCE   9  (residues 1 to 585)
  AUTHORS   Smith,R.J.H.
  TITLE     Branchiootorenal Spectrum Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301554
REFERENCE   10 (residues 1 to 585)
  AUTHORS   Stoppa-Lyonnet,D., Carter,P.E., Meo,T. and Tosi,M.
  TITLE     Clusters of intragenic Alu repeats predispose the human C1
            inhibitor locus to deleterious rearrangements
  JOURNAL   Proc Natl Acad Sci U S A 87 (4), 1551-1555 (1990)
   PUBMED   2154751
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099805.2, AC016465.8 and
            AC022858.8.
            
            On May 7, 2019 this sequence version replaced XP_016868699.1.
            
            Summary: This gene encodes a member of the eyes absent (EYA) family
            of proteins. The encoded protein may play a role in the developing
            kidney, branchial arches, eye, and ear. Mutations of this gene have
            been associated with branchiootorenal dysplasia syndrome,
            branchiootic syndrome, and sporadic cases of congenital cataracts
            and ocular anterior segment anomalies. A similar protein in mice
            can act as a transcriptional activator. Alternatively spliced
            transcript variants have been identified for this gene. [provided
            by RefSeq, Dec 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.274378.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.3"
     Protein         1..585
                     /product="protein phosphatase EYA1 isoform 7"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="eyes absent homolog 1; protein phosphatase EYA1"
                     /calculated_mol_wt=63353
     Region          <61..302
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          344..585
                     /region_name="HAD_Eya"
                     /note="protein tyrosine phosphatase domain of the nuclear
                     transcription factor of Eyes absent (Eya) and related
                     phosphatase domains; cd02601"
                     /db_xref="CDD:319789"
     Site            order(346,543,545,561,563..566,572,575,578..579,582..585)
                     /site_type="other"
                     /note="SIX1 interface [polypeptide binding]"
                     /db_xref="CDD:319789"
     Site            order(351..355,415..416,524,548..549,553..554)
                     /site_type="active"
                     /db_xref="CDD:319789"
     CDS             1..585
                     /gene="EYA1"
                     /gene_synonym="BOP; BOR; BOS1; OFC1; OTFCS"
                     /coded_by="NM_001370336.1:304..2061"
                     /note="isoform 7 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS94312.1"
                     /db_xref="GeneID:2138"
                     /db_xref="HGNC:HGNC:3519"
                     /db_xref="MIM:601653"
ORIGIN      
        1 medprgingq svqtsqassd vavssscrsm emqdltsphs rlsgssesps gpklgnshin
       61 snsmtpngte vktepmssse tasttadgsl nnfsgsaigs ssfsprpthq fsppqiypsk
      121 pyphilptps sqtmaaygqt qfttgmqqat ayatypqpgq pygissygik tegglsqsqs
      181 pgqtgflsyg tsfstpqpgq apysyqmqgs sfttssgiyt gnnsltnssg fnssqqdyps
      241 ypsfgqgqya qyynsspypa hymtssntsp ttpstnatyq lqeppsgits qavtdptaey
      301 stihspstpi kdsdsdrlrr gsdgksrgrg rrnnnpsppp dsdlervfiw dldetiivfh
      361 slltgsyanr ygrecdqvhi ddvssddngq dlstynfgtd gfpaaatsan lclatgvrgg
      421 vdwmrklafr yrrvkeiynt yknnvggllg pakreawlql raeiealtds wltlalkals
      481 lihsrtncvn ilvtttqlip alakvllygl givfpieniy satkigkesc feriiqrfgr
      541 kvvyvvigdg veeeqgakkh ampfwrissh sdlmalhhal eleyl
//
LOCUS       NP_001357214            1087 aa            linear   PRI 27-APR-2025
DEFINITION  DNA helicase B [Homo sapiens].
ACCESSION   NP_001357214 XP_005269291
VERSION     NP_001357214.1
DBSOURCE    REFSEQ: accession NM_001370285.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hormeno,S., Wilkinson,O.J., Aicart-Ramos,C., Kuppa,S., Antony,E.,
            Dillingham,M.S. and Moreno-Herrero,F.
  TITLE     Human HELB is a processive motor protein that catalyzes RPA
            clearance from single-stranded DNA
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2112376119 (2022)
   PUBMED   35385349
  REMARK    GeneRIF: Human HELB is a processive motor protein that catalyzes
            RPA clearance from single-stranded DNA.
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Zafar,M.K., Hazeslip,L., Chauhan,M.Z. and Byrd,A.K.
  TITLE     The Expression of Human DNA Helicase B Is Affected by
            G-Quadruplexes in the Promoter
  JOURNAL   Biochemistry 59 (26), 2401-2409 (2020)
   PUBMED   32478505
  REMARK    GeneRIF: The Expression of Human DNA Helicase B Is Affected by
            G-Quadruplexes in the Promoter.
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Hazeslip,L., Zafar,M.K., Chauhan,M.Z. and Byrd,A.K.
  TITLE     Genome Maintenance by DNA Helicase B
  JOURNAL   Genes (Basel) 11 (5), 578 (2020)
   PUBMED   32455610
  REMARK    GeneRIF: Genome Maintenance by DNA Helicase B.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1087)
  AUTHORS   Tkac,J., Xu,G., Adhikary,H., Young,J.T.F., Gallo,D.,
            Escribano-Diaz,C., Krietsch,J., Orthwein,A., Munro,M., Sol,W.,
            Al-Hakim,A., Lin,Z.Y., Jonkers,J., Borst,P., Brown,G.W.,
            Gingras,A.C., Rottenberg,S., Masson,J.Y. and Durocher,D.
  TITLE     HELB Is a Feedback Inhibitor of DNA End Resection
  JOURNAL   Mol Cell 61 (3), 405-418 (2016)
   PUBMED   26774285
  REMARK    GeneRIF: Conclude that mammalian DNA end resection triggers its own
            inhibition via the recruitment of HELB.
REFERENCE   5  (residues 1 to 1087)
  AUTHORS   Gerhardt,J., Guler,G.D. and Fanning,E.
  TITLE     Human DNA helicase B interacts with the replication initiation
            protein Cdc45 and facilitates Cdc45 binding onto chromatin
  JOURNAL   Exp Cell Res 334 (2), 283-293 (2015)
   PUBMED   25933514
  REMARK    GeneRIF: The depletion of HDHB from human cells diminishes Cdc45
            association with chromatin, suggesting that HDHB may facilitate
            Cdc45 recruitment at G1/S in human cells.
REFERENCE   6  (residues 1 to 1087)
  AUTHORS   Liu,H., Yan,P. and Fanning,E.
  TITLE     Human DNA helicase B functions in cellular homologous recombination
            and stimulates Rad51-mediated 5'-3' heteroduplex extension in vitro
  JOURNAL   PLoS One 10 (1), e0116852 (2015)
   PUBMED   25617833
  REMARK    GeneRIF: HDHB promotes homologous recombination in vivo and
            stimulates 5'-3' heteroduplex extension during Rad51-mediated
            strand exchange in vitro
            Erratum:[PLoS One. 2018 Oct 10;13(10):e0205766. doi:
            10.1371/journal.pone.0205766. PMID: 30304027]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1087)
  AUTHORS   Guler,G.D., Liu,H., Vaithiyalingam,S., Arnett,D.R., Kremmer,E.,
            Chazin,W.J. and Fanning,E.
  TITLE     Human DNA helicase B (HDHB) binds to replication protein A and
            facilitates cellular recovery from replication stress
  JOURNAL   J Biol Chem 287 (9), 6469-6481 (2012)
   PUBMED   22194613
  REMARK    GeneRIF: Replication stress-induced recruitment of HDHB to
            chromatin is independent of checkpoint signaling but correlates
            with the level of replication protein A (RPA) recruited to
            chromatin.
REFERENCE   8  (residues 1 to 1087)
  AUTHORS   Gu,J., Xia,X., Yan,P., Liu,H., Podust,V.N., Reynolds,A.B. and
            Fanning,E.
  TITLE     Cell cycle-dependent regulation of a human DNA helicase that
            localizes in DNA damage foci
  JOURNAL   Mol Biol Cell 15 (7), 3320-3332 (2004)
   PUBMED   15146062
REFERENCE   9  (residues 1 to 1087)
  AUTHORS   Taneja,P., Gu,J., Peng,R., Carrick,R., Uchiumi,F., Ott,R.D.,
            Gustafson,E., Podust,V.N. and Fanning,E.
  TITLE     A dominant-negative mutant of human DNA helicase B blocks the onset
            of chromosomal DNA replication
  JOURNAL   J Biol Chem 277 (43), 40853-40861 (2002)
   PUBMED   12181327
  REMARK    GeneRIF: role of dominant-negative mutant in blocking onset of
            chromosomal DNA replication
REFERENCE   10 (residues 1 to 1087)
  AUTHORS   Tada,S., Kobayashi,T., Omori,A., Kusa,Y., Okumura,N., Kodaira,H.,
            Ishimi,Y., Seki,M. and Enomoto,T.
  TITLE     Molecular cloning of a cDNA encoding mouse DNA helicase B, which
            has homology to Escherichia coli RecD protein, and identification
            of a mutation in the DNA helicase B from tsFT848
            temperature-sensitive DNA replication mutant cells
  JOURNAL   Nucleic Acids Res 29 (18), 3835-3840 (2001)
   PUBMED   11557815
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078889.20.
            
            On May 4, 2019 this sequence version replaced XP_005269291.1.
            
            Summary: This gene encodes a DNA-dependent ATPase which catalyzes
            the unwinding of DNA necessary for DNA replication, repair,
            recombination, and transcription. This gene is thought to function
            specifically during the S phase entry of the cell cycle.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Feb 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.41586.1, AF319995.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247815.9/ ENSP00000247815.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.3"
     Protein         1..1087
                     /product="DNA helicase B"
                     /EC_number="3.6.4.12"
                     /note="helicase (DNA) B"
                     /calculated_mol_wt=123122
     Region          <433..952
                     /region_name="RecD"
                     /note="ATPase/5#-3# helicase helicase subunit RecD of the
                     DNA repair enzyme RecBCD (exonuclease V) [Replication,
                     recombination and repair]; COG0507"
                     /db_xref="CDD:440273"
     Region          953..989
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NG08.2)"
     Site            967
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:15146062,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NG08.2)"
     Site            971
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NVF4; propagated from
                     UniProtKB/Swiss-Prot (Q8NG08.2)"
     Region          1015..1051
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NG08.2)"
     Site            1027
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8NG08.2)"
     Site            1048
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NVF4; propagated from
                     UniProtKB/Swiss-Prot (Q8NG08.2)"
     Region          1055..1078
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000269|PubMed:15146062"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NG08.2)"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NG08.2)"
     CDS             1..1087
                     /gene="HELB"
                     /gene_synonym="DHB; hDHB"
                     /coded_by="NM_001370285.1:112..3375"
                     /db_xref="CCDS:CCDS8976.1"
                     /db_xref="GeneID:92797"
                     /db_xref="HGNC:HGNC:17196"
                     /db_xref="MIM:614539"
ORIGIN      
        1 marsspylrq lqgpllpprd lveedddyln ddveedeesv fidaeelcsg gvkagslpgc
       61 lrvsicdent qetckvfgrf pitgawwrvk vqvkpvvgsr syqyqvqgfp syflqsdmsp
      121 pnqkhicalf lkecevssdd vnkfltwvke vsnyknlnfe nlretlrtfh ketgrkdqkq
      181 ptqngqeelf ldnemslple ntipfrnvmt alqfpkimef lpvllprhfk wiigsgskem
      241 lkeieeilgt hpwklgfski tyrewkllrc easwiafcqc esllqlmtdl eknalimysr
      301 lkqicredgh tyvevndltl tlsnhmsfha aseslkflkd igvvtyeksc vfpydlyhae
      361 raiafsicdl mkkppwhlcv dvekvlasih ttkpenssdd alneskpdev rlenpvdvvd
      421 tqdngdhiwt ngeneinaei sevqldqdqv evpldrdqva alemicsnpv tvisgkggcg
      481 kttivsrlfk hieqleerev kkacedfeqd qnaseewitf teqsqleadk aievlltapt
      541 gkaagllrqk tglhaytlcq vnysfyswtq tmmttnkpwk fssvrvlvvd egslvsvgif
      601 ksvlnllceh sklskliilg dirqlpsiep gnllkdlfet lksrncaiel ktnhraesql
      661 ivdnatrisr rqfpkfdael nisdnptlpi siqdktfifv rlpeedassq ssktnhhscl
      721 ysavktllqe nnlqnaktsq fiafrrqdcd lindccckhy tghltkdhqs rlvfgigdki
      781 cctrnaylsd llpenisgsq qnndldasse dfsgtlpdfa knkrdfesnv rlcngeiffi
      841 tndvtdvtfg krrsltinnm aglevtvdfk klmkycrikh awartihtfq gseeqtvvyv
      901 vgkagrqhwq hvytavtrgr crvyviaees qlrnaimkns fprktrlkhf lqsklsssga
      961 ppadfpsprk ssgdsggpst psasplpvvt dhamtndvtw seasspdert ltfaerwqls
     1021 spdgvdtddd lpksraskrt cgvnddesps kifmvgespq vssrlqnlrl nnliprqlfk
     1081 ptdnqet
//
LOCUS       NP_004298                759 aa            linear   PRI 27-APR-2025
DEFINITION  amyloid beta precursor protein binding family B member 2 isoform a
            [Homo sapiens].
ACCESSION   NP_004298
VERSION     NP_004298.1
DBSOURCE    REFSEQ: accession NM_004307.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Xu,L.B., Xiong,J., Zhang,Y.H., Dai,Y., Ren,X.P., Ren,Y.J., Han,D.,
            Wei,S.H. and Qi,M.
  TITLE     miR-205-3p promotes lung cancer progression by targeting APBB2
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165160
  REMARK    GeneRIF: miR2053p promotes lung cancer progression by targeting
            APBB2.
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Zhou,K., Cao,D., Wang,Y., Wang,L. and Meng,X.
  TITLE     Hsa-miR-30a-3p attenuates gastric adenocarcinoma proliferation and
            metastasis via APBB2
  JOURNAL   Aging (Albany NY) 13 (12), 16763-16772 (2021)
   PUBMED   34182542
  REMARK    GeneRIF: Hsa-miR-30a-3p attenuates gastric adenocarcinoma
            proliferation and metastasis via APBB2.
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 759)
  AUTHORS   Chang,Y., Tesco,G., Jeong,W.J., Lindsley,L., Eckman,E.A.,
            Eckman,C.B., Tanzi,R.E. and Guenette,S.Y.
  TITLE     Generation of the beta-amyloid peptide and the amyloid precursor
            protein C-terminal fragment gamma are potentiated by FE65L1
  JOURNAL   J Biol Chem 278 (51), 51100-51107 (2003)
   PUBMED   14527950
  REMARK    GeneRIF: FE65L1 potentiates gamma-secretase processing of APP CTFs.
            This requires binding of FE65L1 to APP and APP CTFs. Enhanced APP
            CTF processing can be detected in early endosome vesicles
REFERENCE   7  (residues 1 to 759)
  AUTHORS   Bruni,P., Minopoli,G., Brancaccio,T., Napolitano,M., Faraonio,R.,
            Zambrano,N., Hansen,U. and Russo,T.
  TITLE     Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein,
            blocks cell cycle progression by down-regulating thymidylate
            synthase expression
  JOURNAL   J Biol Chem 277 (38), 35481-35488 (2002)
   PUBMED   12089154
REFERENCE   8  (residues 1 to 759)
  AUTHORS   Blanco,G., Irving,N.G., Brown,S.D., Miller,C.C. and McLoughlin,D.M.
  TITLE     Mapping of the human and murine X11-like genes (APBA2 and apba2),
            the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2):
            genes encoding phosphotyrosine-binding domain proteins that
            interact with the Alzheimer's disease amyloid precursor protein
  JOURNAL   Mamm Genome 9 (6), 473-475 (1998)
   PUBMED   9585438
REFERENCE   9  (residues 1 to 759)
  AUTHORS   McLoughlin,D.M. and Miller,C.C.
  TITLE     The intracellular cytoplasmic domain of the Alzheimer's disease
            amyloid precursor protein interacts with phosphotyrosine-binding
            domain proteins in the yeast two-hybrid system
  JOURNAL   FEBS Lett 397 (2-3), 197-200 (1996)
   PUBMED   8955346
REFERENCE   10 (residues 1 to 759)
  AUTHORS   Guenette,S.Y., Chen,J., Jondro,P.D. and Tanzi,R.E.
  TITLE     Association of a novel human FE65-like protein with the cytoplasmic
            domain of the beta-amyloid precursor protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10832-10837 (1996)
   PUBMED   8855266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB236935.1, AK226179.1,
            AK295974.1, AC131953.1 and AL080130.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene interacts with the
            cytoplasmic domains of amyloid beta (A4) precursor protein and
            amyloid beta (A4) precursor-like protein 2. This protein contains
            two phosphotyrosine binding (PTB) domains, which are thought to
            function in signal transduction. Polymorphisms in this gene have
            been associated with Alzheimer's disease. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.137914.1, AK226179.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000508593.6/ ENSP00000427211.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14-p13"
     Protein         1..759
                     /product="amyloid beta precursor protein binding family B
                     member 2 isoform a"
                     /note="Fe65-like 1; protein Fe65-like 1"
                     /calculated_mol_wt=83314
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92870.3)"
     Region          134..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92870.3)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92870.3)"
     Region          176..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92870.3)"
     Region          293..321
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          327..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92870.3)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92870.3)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR4; propagated from
                     UniProtKB/Swiss-Prot (Q92870.3)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR4; propagated from
                     UniProtKB/Swiss-Prot (Q92870.3)"
     Region          417..554
                     /region_name="PTB1_Fe65"
                     /note="Fe65 N-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01272"
                     /db_xref="CDD:269970"
     Site            order(432,500,517)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269970"
     Site            order(499..504,517,539,543)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269970"
     Region          583..709
                     /region_name="PTB2_Fe65"
                     /note="Fe65 C-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01271"
                     /db_xref="CDD:269969"
     Site            order(594,668,687)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269969"
     Site            order(605,607,655..656,658..665,667,675,681,691,693,696,
                     700,703..704,706..707)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269969"
     CDS             1..759
                     /gene="APBB2"
                     /gene_synonym="FE65L; FE65L1"
                     /coded_by="NM_004307.2:555..2834"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54762.1"
                     /db_xref="GeneID:323"
                     /db_xref="HGNC:HGNC:582"
                     /db_xref="MIM:602710"
ORIGIN      
        1 msevlpadsg vdtlavfmas sgttdvtnrn spatppntln lrsshnelln aeikhtetkn
       61 stppkcrkky altniqaamg lsdpaaqpll gngsaniklv kngenqlrka aeqgqqdpnk
      121 nlsptavini tseklegkep hpqdssscei lpsqprrtks flnyyadlet sareleqnrg
      181 nhhgtaeeks qpvqgqasti igngdlllqk pnrpqssped gqvatvsssp etkkdhpktg
      241 aktdcalhri qnlapsdees swttlsqdsa spsspdetad iwsdhsfqtd pdlppgwkrv
      301 sdiagtyywh iptgttqwer pvsipadlqg srkgslssvt psptpenekq pwsdfavlng
      361 gkinsdiwkd lhaatvnpdp slkefegatl ryaslklrna phpddddscs insdpeakcf
      421 avrslgwvem aeedlapgks svavnncirq lsyckndird tvgiwgegkd mylilendml
      481 slvdpmdrsv lhsqpivsir vwgvgrdngr dfayvardkd trilkchvfr cdtpakaiat
      541 slheicskim aerknakala csslqeranv nldvplqvdf ptpktelvqk fhvqylgmlp
      601 vdkpvgmdil nsaienlmts snkedwlsvn mnvadatvtv isekneeevl vecrvrflsf
      661 mgvgkdvhtf afimdtgnqr fechvfwcep nagnvseavq aacmlryqkc lvarppsqkv
      721 rpppppadsv trrvttnvkr gvlslidtlk qkrpvtemp
//
LOCUS       NP_001356318             381 aa            linear   PRI 27-APR-2025
DEFINITION  cAMP-dependent protein kinase type I-alpha regulatory subunit
            isoform a [Homo sapiens].
ACCESSION   NP_001356318 XP_011523287
VERSION     NP_001356318.1
DBSOURCE    REFSEQ: accession NM_001369389.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Calvo,S.E., Pagliarini,D.J. and Mootha,V.K.
  TITLE     Upstream open reading frames cause widespread reduction of protein
            expression and are polymorphic among humans
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7507-7512 (2009)
   PUBMED   19372376
  REMARK    GeneRIF: Includes the study of a disease-related upstream ORF in
            this gene, and shows that it functions to reduce protein levels by
            ~95%.
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Gupte,R.S., Pozarowski,P., Grabarek,J., Traganos,F.,
            Darzynkiewicz,Z. and Lee,M.Y.
  TITLE     RIalpha influences cellular proliferation in cancer cells by
            transporting RFC40 into the nucleus
  JOURNAL   Cancer Biol Ther 4 (4), 429-437 (2005)
   PUBMED   15846072
  REMARK    GeneRIF: A nonconventional nuclear localization sequence (NLS) has
            been found for PRKAR1A. This suggests a new function for PRKAR1A as
            a nuclear transport protein for the second subunit of RFC40.
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Bossis,I. and Stratakis,C.A.
  TITLE     Minireview: PRKAR1A: normal and abnormal functions
  JOURNAL   Endocrinology 145 (12), 5452-5458 (2004)
   PUBMED   15331577
  REMARK    GeneRIF: PRKAR1A might function as a tumor suppressor gene
            Review article
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Stergiopoulos,S.G. and Stratakis,C.A.
  TITLE     Human tumors associated with Carney complex and germline PRKAR1A
            mutations: a protein kinase A disease!
  JOURNAL   FEBS Lett 546 (1), 59-64 (2003)
   PUBMED   12829237
  REMARK    Review article
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Stratakis,C.A.
  TITLE     Carney Complex
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301463
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Jones,K.W., Shapero,M.H., Chevrette,M. and Fournier,R.E.
  TITLE     Subtractive hybridization cloning of a tissue-specific
            extinguisher: TSE1 encodes a regulatory subunit of protein kinase A
  JOURNAL   Cell 66 (5), 861-872 (1991)
   PUBMED   1889088
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Boshart,M., Weih,F., Nichols,M. and Schutz,G.
  TITLE     The tissue-specific extinguisher locus TSE1 encodes a regulatory
            subunit of cAMP-dependent protein kinase
  JOURNAL   Cell 66 (5), 849-859 (1991)
   PUBMED   1832337
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Sandberg,M., Skalhegg,B. and Jahnsen,T.
  TITLE     The two mRNA forms for the type I alpha regulatory subunit of
            cAMP-dependent protein kinase from human testis are due to the use
            of different polyadenylation site signals
  JOURNAL   Biochem Biophys Res Commun 167 (1), 323-330 (1990)
   PUBMED   2310396
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Sandberg,M., Tasken,K., Oyen,O., Hansson,V. and Jahnsen,T.
  TITLE     Molecular cloning, cDNA structure and deduced amino acid sequence
            for a type I regulatory subunit of cAMP-dependent protein kinase
            from human testis
  JOURNAL   Biochem Biophys Res Commun 149 (3), 939-945 (1987)
   PUBMED   3426618
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Geahlen,R.L., Carmichael,D.F., Hashimoto,E. and Krebs,E.G.
  TITLE     Phosphorylation of cAMP-dependent protein kinase subunits
  JOURNAL   Adv Enzyme Regul 20, 195-209 (1982)
   PUBMED   6287816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079210.12.
            
            On Apr 8, 2019 this sequence version replaced XP_011523287.1.
            
            Summary: cAMP is a signaling molecule important for a variety of
            cellular functions. cAMP exerts its effects by activating the
            cAMP-dependent protein kinase, which transduces the signal through
            phosphorylation of different target proteins. The inactive kinase
            holoenzyme is a tetramer composed of two regulatory and two
            catalytic subunits. cAMP causes the dissociation of the inactive
            holoenzyme into a dimer of regulatory subunits bound to four cAMP
            and two free monomeric catalytic subunits. Four different
            regulatory subunits and three catalytic subunits have been
            identified in humans. This gene encodes one of the regulatory
            subunits. This protein was found to be a tissue-specific
            extinguisher that down-regulates the expression of seven liver
            genes in hepatoma x fibroblast hybrids. Mutations in this gene
            cause Carney complex (CNC). This gene can fuse to the RET
            protooncogene by gene rearrangement and form the thyroid
            tumor-specific chimeric oncogene known as PTC2. A nonconventional
            nuclear localization sequence (NLS) has been found for this protein
            which suggests a role in DNA replication via the protein serving as
            a nuclear transport protein for the second subunit of the
            Replication Factor C (RFC40). Several alternatively spliced
            transcript variants encoding two different isoforms have been
            observed. [provided by RefSeq, Jan 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.30130.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..381
                     /product="cAMP-dependent protein kinase type I-alpha
                     regulatory subunit isoform a"
                     /EC_number="2.7.11.1"
                     /note="tissue-specific extinguisher 1; cAMP-dependent
                     protein kinase type I-alpha regulatory chain;
                     cAMP-dependent protein kinase regulatory subunit RIalpha;
                     protein kinase A type 1a regulatory subunit; epididymis
                     secretory sperm binding protein; protein kinase,
                     cAMP-dependent, regulatory, type I, alpha; Carney complex
                     type 1; protein kinase, cAMP-dependent, regulatory subunit
                     type I alpha"
                     /calculated_mol_wt=42851
     Region          1..136
                     /region_name="Dimerization and phosphorylation"
                     /note="propagated from UniProtKB/Swiss-Prot (P10644.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09456; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Region          14..63
                     /region_name="DD_RIalpha_PKA"
                     /note="dimerization/docking (D/D) domain of the Type I
                     alpha Regulatory subunit of cAMP-dependent protein kinase;
                     cd12101"
                     /db_xref="CDD:438522"
     Site            order(15,18..19,28..29,31..32,35..36)
                     /site_type="other"
                     /note="AKAP interaction site [polypeptide binding]"
                     /db_xref="CDD:438522"
     Site            order(18,21..22,27,30..31,34..35,38..39,43,45..48,50..51,
                     54..55,58)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:438522"
     Region          64..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10644.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Region          96..100
                     /region_name="Pseudophosphorylation motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P10644.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBC7; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Region          137..246
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(201..202,211..213)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(233..235,239..241)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          255..370
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09456; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            order(325..326,335..337)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(357..359,363..365)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     CDS             1..381
                     /gene="PRKAR1A"
                     /gene_synonym="ACRDYS1; ADOHR; CAR; CNC; CNC1; PKR1;
                     PPNAD1; PRKAR1; Prkar1alpha; TSE1"
                     /coded_by="NM_001369389.1:283..1428"
                     /note="isoform a is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS11678.1"
                     /db_xref="GeneID:5573"
                     /db_xref="HGNC:HGNC:9388"
                     /db_xref="MIM:188830"
ORIGIN      
        1 mesgstaase earslrecel yvqkhniqal lkdsivqlct arperpmafl reyferleke
       61 eakqiqnlqk agtrtdsred eisppppnpv vkgrrrrgai saevyteeda asyvrkvipk
      121 dyktmaalak aieknvlfsh lddnersdif damfsvsfia getviqqgde gdnfyvidqg
      181 etdvyvnnew atsvgeggsf gelaliygtp raatvkaktn vklwgidrds yrrilmgstl
      241 rkrkmyeefl skvsilesld kwerltvada lepvqfedgq kivvqgepgd effiilegsa
      301 avlqrrsene efvevgrlgp sdyfgeiall mnrpraatvv argplkcvkl drprfervlg
      361 pcsdilkrni qqynsfvsls v
//
LOCUS       NP_001348413             410 aa            linear   ROD 27-APR-2025
DEFINITION  NIPA-like protein 3 isoform 2 [Mus musculus].
ACCESSION   NP_001348413 XP_017175906
VERSION     NP_001348413.1
DBSOURCE    REFSEQ: accession NM_001361484.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Grzmil,P., Konietzko,J., Boehm,D., Holter,S.M.,
            Aguilar-Pimentel,A., Javaheri,A., Kalaydjiev,S., Adler,T.,
            Bolle,I., Adham,I., Dixkens,C., Wolf,S., Fuchs,H.,
            Gailus-Durner,V., Wurst,W., Ollert,M., Busch,D.H., Schulz,H., de
            Angelis,M.H. and Burfeind,P.
  TITLE     Targeted disruption of the mouse Npal3 gene leads to deficits in
            behavior, increased IgE levels, and impaired lung function
  JOURNAL   Cytogenet Genome Res 125 (3), 186-200 (2009)
   PUBMED   19738379
  REMARK    GeneRIF: disruption of the Npal3 gene results in a pleiotropic
            phenotype; The function of the nervous system was impaired in both
            mutant males and females which could be demonstrated in behavioral
            tests and the the immune system is also affected.
            Erratum:[Cytogenet Genome Res. 2009;125(4):285. Hoelter, S M
            [corrected to Holter, S M]; Aguilar, A [corrected to
            Aguilar-Pimentel, A]; Gailus-Durne, V [corrected to Gailus-Durner,
            V]; Busch, D [corrected to Busch, D H]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL670720.7 and AL627185.10.
            
            On Mar 28, 2018 this sequence version replaced XP_017175906.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.22084.1,
                                           ERR3363660.870086.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 67.64 cM"
     Protein         1..410
                     /product="NIPA-like protein 3 isoform 2"
                     /note="NIPA-like protein 3"
                     /calculated_mol_wt=44677
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Region          36..330
                     /region_name="EamA"
                     /note="EamA-like transporter family; cl23754"
                     /db_xref="CDD:474045"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Site            80..100
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Site            139..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Site            175..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Site            206..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Site            304..324
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P499; propagated from
                     UniProtKB/Swiss-Prot (Q8BGN5.1)"
     Region          389..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGN5.1)"
     CDS             1..410
                     /gene="Nipal3"
                     /gene_synonym="9130020G22Rik; Npal3"
                     /coded_by="NM_001361484.1:493..1725"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS18786.1"
                     /db_xref="GeneID:74552"
                     /db_xref="MGI:MGI:1921802"
ORIGIN      
        1 mdgahsaglq lqplpptsga tstslssseg sfsykenlig allaifghlv vsialnlqky
       61 chirlagskd prayfktktw wlgllllllg elgvfasyaf aplslivpls avsviasaii
      121 giifikekwk pkdfvrryvl sfvgcglaiv gtyllvtfap nshekmtgen iarhlvswpf
      181 llymlvaivl fclllyfyke rnansivvil llvallgsmt vvtvkavsgm lvlsiqgnlq
      241 ldypifyvmf vcmvataiyq atflseasqi ydssliasvg yilsttaait agaifyldfl
      301 geealhicmf algcliaflg vflitrnrkk aipfepyism dampgmqdmh akgttvqpdl
      361 kasfsygale sndsiselyt patlpvmqee hssrstpgvp yrvlehtkke
//
LOCUS       NP_001269463             374 aa            linear   PRI 27-APR-2025
DEFINITION  potassium channel subfamily K member 9 precursor [Homo sapiens].
ACCESSION   NP_001269463
VERSION     NP_001269463.1
DBSOURCE    REFSEQ: accession NM_001282534.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Rinne,S., Schick,F., Vowinkel,K., Schutte,S., Krasel,C.,
            Kauferstein,S., Schafer,M.K., Kiper,A.K., Muller,T. and Decher,N.
  TITLE     Potassium channel TASK-5 forms functional heterodimers with TASK-1
            and TASK-3 to break its silence
  JOURNAL   Nat Commun 15 (1), 7548 (2024)
   PUBMED   39215006
  REMARK    GeneRIF: Potassium channel TASK-5 forms functional heterodimers
            with TASK-1 and TASK-3 to break its silence.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Lin,H., Li,J., Zhang,Q., Yang,H. and Chen,S.
  TITLE     C-type inactivation and proton modulation mechanisms of the TASK3
            channel
  JOURNAL   Proc Natl Acad Sci U S A 121 (17), e2320345121 (2024)
   PUBMED   38630723
  REMARK    GeneRIF: C-type inactivation and proton modulation mechanisms of
            the TASK3 channel.
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Saito,M., Tanaka,C., Toyoda,H. and Kang,Y.
  TITLE     Subcellular Localization of Homomeric TASK3 Channels and Its
            Presumed Functional Significances in Trigeminal Motoneurons
  JOURNAL   Int J Mol Sci 24 (1), 344 (2022)
   PUBMED   36613787
  REMARK    GeneRIF: Subcellular Localization of Homomeric TASK3 Channels and
            Its Presumed Functional Significances in Trigeminal Motoneurons.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Ruf,N., Bahring,S., Galetzka,D., Pliushch,G., Luft,F.C.,
            Nurnberg,P., Haaf,T., Kelsey,G. and Zechner,U.
  TITLE     Sequence-based bioinformatic prediction and QUASEP identify genomic
            imprinting of the KCNK9 potassium channel gene in mouse and human
  JOURNAL   Hum Mol Genet 16 (21), 2591-2599 (2007)
   PUBMED   17704508
  REMARK    GeneRIF: KCNK9 gene is imprinted in human and mouse, exhibiting
            preferential expression from the maternal allele in brain.
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Vega-Saenz de Miera,E., Lau,D.H., Zhadina,M., Pountney,D.,
            Coetzee,W.A. and Rudy,B.
  TITLE     KT3.2 and KT3.3, two novel human two-pore K(+) channels closely
            related to TASK-1
  JOURNAL   J Neurophysiol 86 (1), 130-142 (2001)
   PUBMED   11431495
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Meadows,H.J. and Randall,A.D.
  TITLE     Functional characterisation of human TASK-3, an acid-sensitive
            two-pore domain potassium channel
  JOURNAL   Neuropharmacology 40 (4), 551-559 (2001)
   PUBMED   11249964
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Chapman,C.G., Meadows,H.J., Godden,R.J., Campbell,D.A.,
            Duckworth,M., Kelsell,R.E., Murdock,P.R., Randall,A.D., Rennie,G.I.
            and Gloger,I.S.
  TITLE     Cloning, localisation and functional expression of a novel human,
            cerebellum specific, two pore domain potassium channel
  JOURNAL   Brain Res Mol Brain Res 82 (1-2), 74-83 (2000)
   PUBMED   11042359
REFERENCE   8  (residues 1 to 374)
  AUTHORS   Rajan,S., Wischmeyer,E., Xin Liu,G., Preisig-Muller,R., Daut,J.,
            Karschin,A. and Derst,C.
  TITLE     TASK-3, a novel tandem pore domain acid-sensitive K+ channel. An
            extracellular histiding as pH sensor
  JOURNAL   J Biol Chem 275 (22), 16650-16657 (2000)
   PUBMED   10747866
REFERENCE   9  (residues 1 to 374)
  AUTHORS   Kim,Y., Bang,H. and Kim,D.
  TITLE     TASK-3, a new member of the tandem pore K(+) channel family
  JOURNAL   J Biol Chem 275 (13), 9340-9347 (2000)
   PUBMED   10734076
REFERENCE   10 (residues 1 to 374)
  AUTHORS   Zadeh,N. and Graham,J.M. Jr.
  TITLE     KCNK9 Imprinting Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28333430
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007869.2, AF248241.1,
            AF212829.1, DA416784.1, BX092753.1 and AW085193.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that contains multiple
            transmembrane regions and two pore-forming P domains and functions
            as a pH-dependent potassium channel. Amplification and
            overexpression of this gene have been observed in several types of
            human carcinomas. This gene is imprinted in the brain, with
            preferential expression from the maternal allele. A mutation in
            this gene was associated with Birk-Barel dysmorphism syndrome.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.325644.1,
                                           SRR1660809.181174.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene         :: PMID: 17704508
            MANE Ensembl match     :: ENST00000520439.3/ ENSP00000430676.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..374
                     /product="potassium channel subfamily K member 9
                     precursor"
                     /note="acid-sensitive potassium channel protein TASK-3;
                     two pore K(+) channel KT3.2; potassium channel, two pore
                     domain subfamily K, member 9; two pore potassium channel
                     KT3.2; TWIK-related acid-sensitive K(+) channel 3;
                     TWIK-related acid-sensitive K+ 3; potassium 2-pore domain
                     leak channel TASK3"
                     /calculated_mol_wt=39222
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3060
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPC2.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPC2.1)"
     Region          <73..132
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Site            78
                     /site_type="other"
                     /note="Forms a cation-pi interaction with protonated H-98,
                     stabilizing the C-type inactivated state.
                     /evidence=ECO:0000269|PubMed:38630723; propagated from
                     UniProtKB/Swiss-Prot (Q9NPC2.1)"
     Region          93..98
                     /region_name="Selectivity filter 1.
                     /evidence=ECO:0000305|PubMed:26919430"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPC2.1)"
     Site            98
                     /site_type="other"
                     /note="pH sensor. /evidence=ECO:0000269|PubMed:38630723;
                     propagated from UniProtKB/Swiss-Prot (Q9NPC2.1)"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPC2.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPC2.1)"
     Region          <183..243
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          199..204
                     /region_name="Selectivity filter 2.
                     /evidence=ECO:0000305|PubMed:26919430"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPC2.1)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPC2.1)"
     Region          243..248
                     /region_name="X-gate.
                     /evidence=ECO:0000269|PubMed:38630723"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPC2.1)"
     CDS             1..374
                     /gene="KCNK9"
                     /gene_synonym="BIBARS; K2p9.1; KT3.2; TASK-3; TASK3;
                     TASK32"
                     /coded_by="NM_001282534.2:132..1256"
                     /db_xref="CCDS:CCDS6377.1"
                     /db_xref="GeneID:51305"
                     /db_xref="HGNC:HGNC:6283"
                     /db_xref="MIM:605874"
ORIGIN      
        1 mkrqnvrtls livctftyll vgaavfdale sdhemreeek lkaeeirikg kynissedyr
       61 qlelvilqse phragvqwkf agsfyfaitv ittigyghaa pgtdagkafc mfyavlgipl
      121 tlvmfqslge rmntfvryll krikkccgmr ntdvsmenmv tvgffscmgt lcigaaafsq
      181 ceewsffhay yycfitltti gfgdyvalqt kgalqkkply vafsfmyilv gltvigafln
      241 lvvlrfltmn sederrdaee raslagnrns mvihipeepr psrprykadv pdlqsvcsct
      301 cyrsqdyggr svapqnsfsa klaphyfhsi sykieeisps tlknslfpsp issispglhs
      361 ftdhqrlmkr rksv
//
LOCUS       NP_001348198             485 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF14 isoform a [Mus musculus].
ACCESSION   NP_001348198 XP_006526184
VERSION     NP_001348198.1
DBSOURCE    REFSEQ: accession NM_001361269.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Ingham,A.B., Osborne,S.A., Menzies,M., Briscoe,S., Chen,W.,
            Kongsuwan,K., Reverter,A., Jeanes,A., Dalrymple,B.P., Wijffels,G.,
            Seymour,R. and Hudson,N.J.
  TITLE     RNF14 is a regulator of mitochondrial and immune function in muscle
  JOURNAL   BMC Syst Biol 8, 10 (2014)
   PUBMED   24472305
  REMARK    GeneRIF: RNF14 influences the expression of both mitochondrial and
            immune related genes
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Grimont,A., Bloch-Faure,M., El Abida,B. and Crambert,G.
  TITLE     Mapping of sex hormone receptors and their modulators along the
            nephron of male and female mice
  JOURNAL   FEBS Lett 583 (10), 1644-1648 (2009)
   PUBMED   19401201
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   7  (residues 1 to 485)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
REFERENCE   8  (residues 1 to 485)
  AUTHORS   van der Reijden,B.A., Erpelinck-Verschueren,C.A., Lowenberg,B. and
            Jansen,J.H.
  TITLE     TRIADs: a new class of proteins with a novel cysteine-rich
            signature
  JOURNAL   Protein Sci 8 (7), 1557-1561 (1999)
   PUBMED   10422847
REFERENCE   9  (residues 1 to 485)
  AUTHORS   Kang,H.Y., Yeh,S., Fujimoto,N. and Chang,C.
  TITLE     Cloning and characterization of human prostate coactivator ARA54, a
            novel protein that associates with the androgen receptor
  JOURNAL   J Biol Chem 274 (13), 8570-8576 (1999)
   PUBMED   10085091
REFERENCE   10 (residues 1 to 485)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC152450.4.
            
            On Mar 13, 2018 this sequence version replaced XP_006526184.1.
            
            Transcript Variant: This variant (9) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 4 through 9 encode the same
            isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR10662774.3508625.1,
                                           SRR1660815.252506.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 20.2 cM"
     Protein         1..485
                     /product="E3 ubiquitin-protein ligase RNF14 isoform a"
                     /EC_number="2.3.2.31"
                     /note="TRIAD2 type I; E3 ubiquitin-protein ligase RNF14;
                     protein Triad2; androgen receptor-associated protein 54"
                     /calculated_mol_wt=54795
     Region          9..135
                     /region_name="RWD_RNF14"
                     /note="RWD domain of RING finger protein 14 (RNF14) and
                     related proteins; cd23820"
                     /db_xref="CDD:467656"
     Region          37..45
                     /region_name="D-box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JI90.2)"
     Region          214..272
                     /region_name="RING-HC_RBR_RNF14"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 14 (RNF14) and similar proteins; cd16628"
                     /db_xref="CDD:438290"
     Region          217..458
                     /region_name="TRIAD supradomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JI90.2)"
     Region          301..357
                     /region_name="BRcat_RBR_RNF14"
                     /note="BRcat domain found in RING finger protein 14
                     (RNF14); cd20341"
                     /db_xref="CDD:439002"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBS8; propagated from
                     UniProtKB/Swiss-Prot (Q9JI90.2)"
     Region          390..457
                     /region_name="Rcat_RBR_RNF14"
                     /note="Rcat domain found in RING finger protein 14
                     (RNF14); cd20354"
                     /db_xref="CDD:439015"
     CDS             1..485
                     /gene="Rnf14"
                     /gene_synonym="2310075C09Rik; 2610005D23Rik; D18Ertd188e;
                     D7Bwg0165e; Triad2"
                     /coded_by="NM_001361269.1:543..2000"
                     /note="isoform a is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS29200.1"
                     /db_xref="GeneID:56736"
                     /db_xref="MGI:MGI:1929668"
ORIGIN      
        1 msaedleaqe dellalasiy dadefrkaes vqggetriyl dlpqnfkifv sgnsneslqn
       61 sgfeyticfl pplvlnfelp pdypssspps ftlsgkwlsp tqlsalckhl dnlweehrgr
      121 vvlfawmqfl keetltylni vspfelkmgs qkkvqrrata qassstelgv ggaaaadvdq
      181 eetvderavq dveslssliq eildfnqarq tkcfnsklfl csicfceklg sdcmyfleck
      241 hvyckaclkd yfeiqikdgq vkclncpepq cpsvatpgqv kelveadlfa rydrlllqst
      301 ldlmadvvyc prpccqlpvm qepggtmaic sscnfafctl crltyhglsp ckvtaeklid
      361 lrneylqade atkrfleqry gkrviqkale emeskdwlek nskscpccgt piqkldgcnk
      421 mtctgcmqyf cwicmgslsr anpyrhftds espcfnrlfh avdingdmwe deieedddde
      481 ddddd
//
LOCUS       NP_776089                841 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 15 [Homo sapiens].
ACCESSION   NP_776089 NP_055773
VERSION     NP_776089.2
DBSOURCE    REFSEQ: accession NM_173728.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Sell,G.L., Schaffer,T.B. and Margolis,S.S.
  TITLE     Reducing expression of synapse-restricting protein Ephexin5
            ameliorates Alzheimer's-like impairment in mice
  JOURNAL   J Clin Invest 127 (5), 1646-1650 (2017)
   PUBMED   28346227
  REMARK    GeneRIF: pathological elevation of Ephexin5 expression critically
            drives Abeta-induced memory impairment
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Fukushima,H., Yasumoto,M., Ogasawara,S., Akiba,J., Kitasato,Y.,
            Nakayama,M., Naito,Y., Ishida,Y., Okabe,Y., Yasunaga,M.,
            Horiuchi,H., Sakamoto,E., Itadani,H., Mizuarai,S., Oie,S. and
            Yano,H.
  TITLE     ARHGEF15 overexpression worsens the prognosis in patients with
            pancreatic ductal adenocarcinoma through enhancing the motility and
            proliferative activity of the cancer cells
  JOURNAL   Mol Cancer 15 (1), 32 (2016)
   PUBMED   27145964
  REMARK    GeneRIF: upregulation of ARHGEF15 contributes to the development of
            aggressive PDAC by increasing the growth and motility of the
            pancreatic cancer cells, thereby worsening the prognosis of these
            patients.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 841)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 841)
  AUTHORS   Kusuhara,S., Fukushima,Y., Fukuhara,S., Jakt,L.M., Okada,M.,
            Shimizu,Y., Hata,M., Nishida,K., Negi,A., Hirashima,M.,
            Mochizuki,N., Nishikawa,S. and Uemura,A.
  TITLE     Arhgef15 promotes retinal angiogenesis by mediating VEGF-induced
            Cdc42 activation and potentiating RhoJ inactivation in endothelial
            cells
  JOURNAL   PLoS One 7 (9), e45858 (2012)
   PUBMED   23029280
  REMARK    GeneRIF: Arhgef15 acts as an endothelial cell-specific GEF to
            mediate VEGF-induced Cdc42 activation and potentiate RhoJ
            inactivation, thereby promoting actin polymerization and cell
            motility.
REFERENCE   6  (residues 1 to 841)
  AUTHORS   Dalva,M.B.
  TITLE     Ephecting excitatory synapse development
  JOURNAL   Cell 143 (3), 341-342 (2010)
   PUBMED   21029857
REFERENCE   7  (residues 1 to 841)
  AUTHORS   Ogita,H., Kunimoto,S., Kamioka,Y., Sawa,H., Masuda,M. and
            Mochizuki,N.
  TITLE     EphA4-mediated Rho activation via Vsm-RhoGEF expressed specifically
            in vascular smooth muscle cells
  JOURNAL   Circ Res 93 (1), 23-31 (2003)
   PUBMED   12775584
  REMARK    GeneRIF: This paper presents functional studies determined in rat,
            mouse, and human tissues and cell lines.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB279954.1, AB020722.1,
            BC036749.1 and BQ877184.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jun 27, 2003 this sequence version replaced
            NP_055773.1, NP_776089.1.
            
            Summary: Rho GTPases play a fundamental role in numerous cellular
            processes that are initiated by extracellular stimuli that work
            through G protein-coupled receptors. This gene encodes a protein
            that functions as a specific guanine nucleotide exchange factor for
            RhoA. It also interacts with ephrin A4 in vascular smooth muscle
            cells. Two alternatively spliced transcripts variants that encode
            the same protein have been found for this gene. [provided by
            RefSeq, Aug 2010].
            
            Transcript Variant: This variant (1) is the longer transcript. It
            encodes the same protein as variant 2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036749.1, AK291626.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361926.8/ ENSP00000355026.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..841
                     /product="rho guanine nucleotide exchange factor 15"
                     /note="ephexin-5; Rho guanine nucleotide exchange factor
                     (GEF) 15"
                     /calculated_mol_wt=91809
     Region          1..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94989.4)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5FWH6; propagated from
                     UniProtKB/Swiss-Prot (O94989.4)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5FWH6; propagated from
                     UniProtKB/Swiss-Prot (O94989.4)"
     Region          239..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94989.4)"
     Region          279..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94989.4)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by EPHB2.
                     /evidence=ECO:0000250|UniProtKB:Q5FWH6; propagated from
                     UniProtKB/Swiss-Prot (O94989.4)"
     Region          422..598
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; smart00325"
                     /db_xref="CDD:214619"
     Site            order(424,428,522,550..551,554..555,557..558,561..562,
                     565..566,569,595)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          622..742
                     /region_name="PH_ephexin"
                     /note="Ephexin Pleckstrin homology (PH) domain; cd01221"
                     /db_xref="CDD:269929"
     Region          765..793
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94989.4)"
     CDS             1..841
                     /gene="ARHGEF15"
                     /gene_synonym="ARGEF15; E5; Ephexin5; Vsm-RhoGEF"
                     /coded_by="NM_173728.4:153..2678"
                     /db_xref="CCDS:CCDS11139.1"
                     /db_xref="GeneID:22899"
                     /db_xref="HGNC:HGNC:15590"
                     /db_xref="MIM:608504"
ORIGIN      
        1 msaqslpaat pptqkpprii rprppsrsra aqspgpphng sspqelprns ndaptpmctp
       61 ifweppaasl kppallppsa srasldsqts pdspsstptp spvsrrsasp epaprspvpp
      121 pkpsgspctp llpmagvlaq ngsasapgtv rrlagrfegg aegraqdada pepglqarad
      181 vngereaplt gsgsqengap daglacppcc pcvchttrpg lelrwvpvgg yeevprvprr
      241 asplrtsrsr phppsighpa vvltsyrsta erkllpllkp pkptrvrqda tifgdppqpd
      301 ldllsedgiq tgdspdeapq ntppatvegr eeeglevlke qnwelplqde plyqtyraav
      361 lseelwgvge dgspspanag daptfprppg prntlwqelp avqasglldt lspqerrmqe
      421 slfevvtsea sylrslrllt dtfvlsqalr dtltprdhht lfsnvqrvqg vserflatll
      481 srvrssphis dlcdvvhaha vgpfsvyvdy vrnqqyqeet ysrlmdtnvr fsaelrrlqs
      541 lpkcerlplp sflllpfqri trlrmllqni lrqteegssr qenaqkalga vskiiercsa
      601 evgrmkqtee lirltqrlrf hkvkalplvs wsrrlefqge ltelgcrrgg vlfasrprft
      661 plclllfsdl llitqpksgq rlqvldyahr slvqaqqvpd psgpptfrls llsnhqgrpt
      721 hrllqassls dmqrwlgafp tpgplpcspd tiyedcdcsq elcsessapa ktegrslesr
      781 aapkhlhktp egwlkglpga fpaqlvcevt geherrrhlr qnqrlleavg sssgtpnapp
      841 p
//
LOCUS       NP_001354539             925 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear envelope pore membrane protein POM 121 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001354539
VERSION     NP_001354539.1
DBSOURCE    REFSEQ: accession NM_001367610.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Yu,Y., Farooq,M.S., Eberhart Meessen,S., Jiang,Y., Kato,D.,
            Zhan,T., Weiss,C., Seger,R., Kang,W., Zhang,X., Yu,J., Ebert,M.P.A.
            and Burgermeister,E.
  TITLE     Nuclear pore protein POM121 regulates subcellular localization and
            transcriptional activity of PPARgamma
  JOURNAL   Cell Death Dis 15 (1), 7 (2024)
   PUBMED   38177114
  REMARK    GeneRIF: Nuclear pore protein POM121 regulates subcellular
            localization and transcriptional activity of PPARgamma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Becker,F., Offermann,A., Roesch,M.C., Joerg,V., Roth,D.,
            Lubczyk,V., Kuefer,R., Sailer,V., Kirfel,J., Merseburger,A.S. and
            Perner,S.
  TITLE     Up-regulation of POM121 is linked to prostate cancer aggressiveness
            and serves as a prognostic biomarker
  JOURNAL   Urol Oncol 40 (8), 380 (2022)
   PUBMED   35725938
  REMARK    GeneRIF: Up-regulation of POM121 is linked to prostate cancer
            aggressiveness and serves as a prognostic biomarker.
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   4  (residues 1 to 925)
  AUTHORS   Zhang,S., Zheng,C., Li,D., Bei,C., Zhang,H., Tian,R., Song,X.,
            Zhu,X. and Tan,S.
  TITLE     Clinical Significance of POM121 Expression in Lung Cancer
  JOURNAL   Genet Test Mol Biomarkers 24 (12), 819-824 (2020)
   PUBMED   33296260
  REMARK    GeneRIF: Clinical Significance of POM121 Expression in Lung Cancer.
REFERENCE   5  (residues 1 to 925)
  AUTHORS   Zhao,R., Tang,G., Wang,T., Zhang,L., Wang,W., Zhao,Q. and Zhao,K.
  TITLE     POM121 is a novel marker for predicting the prognosis of laryngeal
            cancer
  JOURNAL   Histol Histopathol 35 (11), 1285-1293 (2020)
   PUBMED   33016327
  REMARK    GeneRIF: POM121 is a novel marker for predicting the prognosis of
            laryngeal cancer.
REFERENCE   6  (residues 1 to 925)
  AUTHORS   Funakoshi,T., Maeshima,K., Yahata,K., Sugano,S., Imamoto,F. and
            Imamoto,N.
  TITLE     Two distinct human POM121 genes: requirement for the formation of
            nuclear pore complexes
  JOURNAL   FEBS Lett 581 (25), 4910-4916 (2007)
   PUBMED   17900573
  REMARK    GeneRIF: RNAi experiments showed that efficient depletion of both
            Pom121 proteins significantly reduces assembled nuclear pore
            complexes on nuclear envelope.
REFERENCE   7  (residues 1 to 925)
  AUTHORS   Le Rouzic,E., Mousnier,A., Rustum,C., Stutz,F., Hallberg,E.,
            Dargemont,C. and Benichou,S.
  TITLE     Docking of HIV-1 Vpr to the nuclear envelope is mediated by the
            interaction with the nucleoporin hCG1
  JOURNAL   J Biol Chem 277 (47), 45091-45098 (2002)
   PUBMED   12228227
REFERENCE   8  (residues 1 to 925)
  AUTHORS   Daigle,N., Beaudouin,J., Hartnell,L., Imreh,G., Hallberg,E.,
            Lippincott-Schwartz,J. and Ellenberg,J.
  TITLE     Nuclear pore complexes form immobile networks and have a very low
            turnover in live mammalian cells
  JOURNAL   J Cell Biol 154 (1), 71-84 (2001)
   PUBMED   11448991
REFERENCE   9  (residues 1 to 925)
  AUTHORS   Bodoor,K., Shaikh,S., Enarson,P., Chowdhury,S., Salina,D.,
            Raharjo,W.H. and Burke,B.
  TITLE     Function and assembly of nuclear pore complex proteins
  JOURNAL   Biochem Cell Biol 77 (4), 321-329 (1999)
   PUBMED   10546895
  REMARK    Review article
REFERENCE   10 (residues 1 to 925)
  AUTHORS   Hallberg,E., Wozniak,R.W. and Blobel,G.
  TITLE     An integral membrane protein of the pore membrane domain of the
            nuclear envelope contains a nucleoporin-like region
  JOURNAL   J Cell Biol 122 (3), 513-521 (1993)
   PUBMED   8335683
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC211469.4 and AC211476.5.
            
            Summary: This gene encodes a transmembrane protein that localizes
            to the inner nuclear membrane and forms a core component of the
            nuclear pore complex, which mediates transport to and from the
            nucleus. The encoded protein may anchor this complex to the nuclear
            envelope. There are multiple related genes and pseudogenes for this
            gene on chromosomes 5, 7, 15, and 22. Alternatively spliced
            transcript variants encoding different isoforms have been observed.
            [provided by RefSeq, Jul 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2144335,
                              SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..925
                     /product="nuclear envelope pore membrane protein POM 121
                     isoform 3"
                     /note="nuclear pore membrane protein 121 kDa; nuclear
                     envelope pore membrane protein POM 121; nucleoporin
                     Nup121; nuclear envelope pore membrane protein POM 121A;
                     POM121 membrane glycoprotein"
                     /calculated_mol_wt=92896
     Region          56..287
                     /region_name="POM121"
                     /note="POM121 family; pfam15229"
                     /db_xref="CDD:464572"
     Region          <303..666
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          715..>889
                     /region_name="Chi1"
                     /note="Chitinase [Carbohydrate transport and metabolism];
                     COG3469"
                     /db_xref="CDD:442692"
     CDS             1..925
                     /gene="POM121"
                     /gene_synonym="P145; POM121A"
                     /coded_by="NM_001367610.1:1256..4033"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:9883"
                     /db_xref="HGNC:HGNC:19702"
                     /db_xref="MIM:615753"
ORIGIN      
        1 mvcspvtvri appdrrfsrs aipeqiisst lsspssnapd pcaketvlsa lkekekkrtv
       61 eeedqifldg qenkrrrhds sgsghsafep lvangvpasf vpkpgslkrg lnsqssddhl
      121 nkrsrsssms sltgayasgi psssrnaits sysstrgisq lwkrngpsss pfsspassrs
      181 qtperpakki reeelchhss sstplaadre sqgekaadtt prkkqnsnsq stpgssgqrk
      241 rkvqllpsrr geqltlpppp qlgysitaed ldlekkaslq wfnqaledks esagaattea
      301 lsppktpsll pplglsqsgp pgllpspsfd skppttllgl ipapsmvpat dtkapptlqa
      361 etatkpqats apspapkqsf lfgtqntsps spaapaassa ppmfkpifta ppksekegpt
      421 ppgpsvtata psssslpttt sttaptfqpv fssmgppasv plpapffkqt ttpatapttt
      481 aplftglasa tsavapitsa spstdsaskp afgfginsvs sssvstttst ataasqpflf
      541 gapqasaasf tpamgsifqf gkppalpttt tvttfsqslh tavptatsss aadfsgfgst
      601 latsapatss qptltfsnts tptfnipfgs saksplpsyp ganpqpafga aegqppgaak
      661 palapsfgss ftfgnsaapa aaptpappsm ikvvpayvpt pihpifggat hsafglkata
      721 safgapassq pafggstavf fgaatssgfg attqtassgs sssvfgsttp spftfggsaa
      781 pagsgsfgin vatpgssttt gafsfgagqs gstatstpfa gglgqnalgt tgqstpfafn
      841 vsstteskpv fggtatptfg lntpapgvgt sgsslsfgas sapaqgfvgv apfgsaalsf
      901 sigagsktpg arqrlqarrq htrkk
//
LOCUS       NP_919262                611 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 4 [Homo sapiens].
ACCESSION   NP_919262
VERSION     NP_919262.2
DBSOURCE    REFSEQ: accession NM_194286.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Labrecque,M.P., Brown,L.G., Coleman,I.M., Lakely,B., Brady,N.J.,
            Lee,J.K., Nguyen,H.M., Li,D., Hanratty,B., Haffner,M.C.,
            Rickman,D.S., True,L.D., Lin,D.W., Lam,H.M., Alumkal,J.J.,
            Corey,E., Nelson,P.S. and Morrissey,C.
  TITLE     RNA Splicing Factors SRRM3 and SRRM4 Distinguish Molecular
            Phenotypes of Castration-Resistant Neuroendocrine Prostate Cancer
  JOURNAL   Cancer Res 81 (18), 4736-4750 (2021)
   PUBMED   34312180
  REMARK    GeneRIF: RNA Splicing Factors SRRM3 and SRRM4 Distinguish Molecular
            Phenotypes of Castration-Resistant Neuroendocrine Prostate Cancer.
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Conn,V.M., Gabryelska,M., Marri,S., Stringer,B.W., Ormsby,R.J.,
            Penn,T., Poonnoose,S., Kichenadasse,G. and Conn,S.J.
  TITLE     SRRM4 Expands the Repertoire of Circular RNAs by Regulating
            Microexon Inclusion
  JOURNAL   Cells 9 (11), 2488 (2020)
   PUBMED   33207694
  REMARK    GeneRIF: SRRM4 Expands the Repertoire of Circular RNAs by
            Regulating Microexon Inclusion.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Coleman,D.J., Sampson,D.A., Sehrawat,A., Kumaraswamy,A., Sun,D.,
            Wang,Y., Schwartzman,J., Urrutia,J., Lee,A.R., Coleman,I.M.,
            Nelson,P.S., Dong,X., Morrissey,C., Corey,E., Xia,Z., Yates,J.A.
            and Alumkal,J.J.
  TITLE     Alternative splicing of LSD1+8a in neuroendocrine prostate cancer
            is mediated by SRRM4
  JOURNAL   Neoplasia 22 (6), 253-262 (2020)
   PUBMED   32403054
  REMARK    GeneRIF: Alternative splicing of LSD1+8a in neuroendocrine prostate
            cancer is mediated by SRRM4.
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Shimojo,M., Kasahara,Y., Inoue,M., Tsunoda,S.I., Shudo,Y.,
            Kurata,T. and Obika,S.
  TITLE     A gapmer antisense oligonucleotide targeting SRRM4 is a novel
            therapeutic medicine for lung cancer
  JOURNAL   Sci Rep 9 (1), 7618 (2019)
   PUBMED   31110284
  REMARK    GeneRIF: A gapmer antisense oligonucleotide targeting SRRM4 is a
            novel therapeutic medicine for lung cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 611)
  AUTHORS   Irimia,M., Weatheritt,R.J., Ellis,J.D., Parikshak,N.N.,
            Gonatopoulos-Pournatzis,T., Babor,M., Quesnel-Vallieres,M.,
            Tapial,J., Raj,B., O'Hanlon,D., Barrios-Rodiles,M., Sternberg,M.J.,
            Cordes,S.P., Roth,F.P., Wrana,J.L., Geschwind,D.H. and
            Blencowe,B.J.
  TITLE     A highly conserved program of neuronal microexons is misregulated
            in autistic brains
  JOURNAL   Cell 159 (7), 1511-1523 (2014)
   PUBMED   25525873
  REMARK    GeneRIF: Neural microexons are regulated by the neuronal-specific
            splicing factor nSR100/SRRM4, through its binding to adjacent
            intronic enhancer motifs; neural microexons are frequently
            misregulated in the brains of individuals with autism spectrum
            disorder, and this misregulation is associated with reduced levels
            of nSR100.
REFERENCE   7  (residues 1 to 611)
  AUTHORS   Shimojo,M., Shudo,Y., Ikeda,M., Kobashi,T. and Ito,S.
  TITLE     The small cell lung cancer-specific isoform of RE1-silencing
            transcription factor (REST) is regulated by neural-specific Ser/Arg
            repeat-related protein of 100 kDa (nSR100)
  JOURNAL   Mol Cancer Res 11 (10), 1258-1268 (2013)
   PUBMED   23928058
  REMARK    GeneRIF: findings show that nSR100 plays a role in the alternative
            splicing of REST in small cell lung cancer (SCLC); study provides
            new insight into the role of nSR100 in the expression of sREST,
            possibly in the pathogenesis of SCLC
REFERENCE   8  (residues 1 to 611)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   9  (residues 1 to 611)
  AUTHORS   Calarco,J.A., Superina,S., O'Hanlon,D., Gabut,M., Raj,B., Pan,Q.,
            Skalska,U., Clarke,L., Gelinas,D., van der Kooy,D., Zhen,M.,
            Ciruna,B. and Blencowe,B.J.
  TITLE     Regulation of vertebrate nervous system alternative splicing and
            development by an SR-related protein
  JOURNAL   Cell 138 (5), 898-910 (2009)
   PUBMED   19737518
REFERENCE   10 (residues 1 to 611)
  AUTHORS   Behrends,U., Schneider,I., Rossler,S., Frauenknecht,H., Golbeck,A.,
            Lechner,B., Eigenstetter,G., Zobywalski,C., Muller-Weihrich,S.,
            Graubner,U., Schmid,I., Sackerer,D., Spath,M., Goetz,C., Prantl,F.,
            Asmuss,H.P., Bise,K. and Mautner,J.
  TITLE     Novel tumor antigens identified by autologous antibody screening of
            childhood medulloblastoma cDNA libraries
  JOURNAL   Int J Cancer 106 (2), 244-251 (2003)
   PUBMED   12800201
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK291361.1, AB058756.1, AC084361.19 and BM680369.1.
            
            On Jul 9, 2004 this sequence version replaced NP_919262.1.
            
            Summary: SRRM4 promotes alternative splicing and inclusion of
            neural-specific exons in target mRNAs (Calarco et al., 2009 [PubMed
            19737518]).[supplied by OMIM, Oct 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC152471.1, AB058756.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267260.5/ ENSP00000267260.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.23"
     Protein         1..611
                     /product="serine/arginine repetitive matrix protein 4"
                     /note="neural-specific SR-related protein of 100 kDa;
                     medulloblastoma antigen MU-MB-2.76; neural-specific
                     serine/arginine repetitive splicing factor of 100 kDa"
                     /calculated_mol_wt=68428
     Region          38..248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A7MD48.2)"
     Region          263..611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A7MD48.2)"
     Region          465..522
                     /region_name="SRRM_C"
                     /note="Serine/arginine repetitive matrix protein
                     C-terminus; pfam15230"
                     /db_xref="CDD:464573"
     CDS             1..611
                     /gene="SRRM4"
                     /gene_synonym="KIAA1853; MU-MB-2.76; nSR100"
                     /coded_by="NM_194286.4:343..2178"
                     /db_xref="CCDS:CCDS44994.1"
                     /db_xref="GeneID:84530"
                     /db_xref="HGNC:HGNC:29389"
                     /db_xref="MIM:613103"
ORIGIN      
        1 masvqqgekq lfekfwrgtf kavatprpes iivasitark plprtepqnn pvvpaqdgps
       61 eklgqhlate plgtnswerd ktcrelgatr ghsashdkdl tpppssrgkk kkkkstrkkr
      121 rrsssyspsp vkkkkkkssk khkrrrsfsk krrhsssspk skrrdekrhk kqsrsrprks
      181 hrhrhhrcps rsqssesrps scesrhrgrs peegqksrrr hsrrcsktlc kdspeaqssr
      241 ppsqplqmlg ylsargvitg sgsaadlftk tasplttsrg rsqeydsgnd tssppstqts
      301 sarsrgqekg spsgglsksr elnsgntsds gnsfttsspq nkgamlenls ptsrgresrg
      361 fqspclecae vkksslvpst arsspmkgcs rsssyastrs sshssrspnp rasprytqsr
      421 stssekrsys rspsyssksg krsppsrssr srrspsysry spsrerdpky sekdsqqrer
      481 erarrrrrsy spmrkrrrds pshlearrit sarkrpipyy rpspsssgsl sstsswysss
      541 ssrsasrsys rsrsrsrsrr rsrtrtssss ssrspspgsr srsrsrsrsr srsrsqsrsy
      601 ssadsysstr r
//
LOCUS       NP_001357267             658 aa            linear   PRI 27-APR-2025
DEFINITION  cationic amino acid transporter 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001357267 XP_005273667
VERSION     NP_001357267.1
DBSOURCE    REFSEQ: accession NM_001370338.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Gaudet,I.D., Xu,H., Gordon,E., Cannestro,G.A., Lu,M.L. and Wei,J.
  TITLE     Elevated SLC7A2 expression is associated with an abnormal
            neuroinflammatory response and nitrosative stress in Huntington's
            disease
  JOURNAL   J Neuroinflammation 21 (1), 59 (2024)
   PUBMED   38419038
  REMARK    GeneRIF: Elevated SLC7A2 expression is associated with an abnormal
            neuroinflammatory response and nitrosative stress in Huntington's
            disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Sun,Y., Li,Y., Jiang,C., Liu,C. and Song,Y.
  TITLE     SLC7A2-Mediated Lysine Catabolism Inhibits Immunosuppression in
            Triple Negative Breast Cancer
  JOURNAL   Crit Rev Eukaryot Gene Expr 34 (5), 31-43 (2024)
   PUBMED   38842202
  REMARK    GeneRIF: SLC7A2-Mediated Lysine Catabolism Inhibits
            Immunosuppression in Triple Negative Breast Cancer.
REFERENCE   3  (residues 1 to 658)
  AUTHORS   Huang,T., Zhou,J., Wang,B., Wang,X., Xiao,W., Yang,M., Liu,Y.,
            Wang,Q., Xiang,Y. and Lan,X.
  TITLE     Integrated Amino Acids and Transcriptome Analysis Reveals Arginine
            Transporter SLC7A2 Is a Novel Regulator of Myogenic Differentiation
  JOURNAL   Int J Mol Sci 25 (1), 95 (2023)
   PUBMED   38203268
  REMARK    GeneRIF: Integrated Amino Acids and Transcriptome Analysis Reveals
            Arginine Transporter SLC7A2 Is a Novel Regulator of Myogenic
            Differentiation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 658)
  AUTHORS   Jiang,S., Zou,J., Dong,J., Shi,H., Chen,J., Li,Y., Duan,X. and
            Li,W.
  TITLE     Lower SLC7A2 expression is associated with enhanced multidrug
            resistance, less immune infiltrates and worse prognosis of NSCLC
  JOURNAL   Cell Commun Signal 21 (1), 9 (2023)
   PUBMED   36639771
  REMARK    GeneRIF: Lower SLC7A2 expression is associated with enhanced
            multidrug resistance, less immune infiltrates and worse prognosis
            of NSCLC.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 658)
  AUTHORS   Xia,S., Wu,J., Zhou,W., Zhang,M., Zhao,K., Liu,J., Tian,D. and
            Liao,J.
  TITLE     SLC7A2 deficiency promotes hepatocellular carcinoma progression by
            enhancing recruitment of myeloid-derived suppressors cells
  JOURNAL   Cell Death Dis 12 (6), 570 (2021)
   PUBMED   34108444
  REMARK    GeneRIF: SLC7A2 deficiency promotes hepatocellular carcinoma
            progression by enhancing recruitment of myeloid-derived suppressors
            cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 658)
  AUTHORS   Hammermann,R., Brunn,G. and Racke,K.
  TITLE     Analysis of the genomic organization of the human cationic amino
            acid transporters CAT-1, CAT-2 and CAT-4
  JOURNAL   Amino Acids 21 (2), 211-219 (2001)
   PUBMED   11665818
  REMARK    GeneRIF: analysis of the genomic organization
REFERENCE   7  (residues 1 to 658)
  AUTHORS   Suzuki,Y., Ishihara,D., Sasaki,M., Nakagawa,H., Hata,H.,
            Tsunoda,T., Watanabe,M., Komatsu,T., Ota,T., Isogai,T., Suyama,A.
            and Sugano,S.
  TITLE     Statistical analysis of the 5' untranslated region of human mRNA
            using 'Oligo-Capped' cDNA libraries
  JOURNAL   Genomics 64 (3), 286-297 (2000)
   PUBMED   10756096
REFERENCE   8  (residues 1 to 658)
  AUTHORS   Closs,E.I., Graf,P., Habermeier,A., Cunningham,J.M. and
            Forstermann,U.
  TITLE     Human cationic amino acid transporters hCAT-1, hCAT-2A, and
            hCAT-2B: three related carriers with distinct transport properties
  JOURNAL   Biochemistry 36 (21), 6462-6468 (1997)
   PUBMED   9174363
REFERENCE   9  (residues 1 to 658)
  AUTHORS   Hoshide,R., Ikeda,Y., Karashima,S., Matsuura,T., Komaki,S.,
            Kishino,T., Niikawa,N., Endo,F. and Matsuda,I.
  TITLE     Molecular cloning, tissue distribution, and chromosomal
            localization of human cationic amino acid transporter 2 (HCAT2)
  JOURNAL   Genomics 38 (2), 174-178 (1996)
   PUBMED   8954799
REFERENCE   10 (residues 1 to 658)
  AUTHORS   Chinen,K., Isomura,M., Izawa,K., Fujiwara,Y., Ohata,H., Iwamasa,T.
            and Nakamura,Y.
  TITLE     Isolation of 45 exon-like fragments from 8p22-->p21.3, a region
            that is commonly deleted in hepatocellular, colorectal, and
            non-small cell lung carcinomas
  JOURNAL   Cytogenet Cell Genet 75 (2-3), 190-196 (1996)
   PUBMED   9040790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP006248.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 7, 2019 this sequence version replaced XP_005273667.1.
            
            Summary: The protein encoded by this gene is a cationic amino acid
            transporter and a member of the APC (amino
            acid-polyamine-organocation) family of transporters. The encoded
            membrane protein is responsible for the cellular uptake of
            arginine, lysine and ornithine. Three transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.141769.1,
                                           DRR138518.382821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000494857.6/ ENSP00000419140.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..658
                     /product="cationic amino acid transporter 2 isoform 2"
                     /note="low affinity cationic amino acid transporter 2;
                     solute carrier family 7 (cationic amino acid transporter,
                     y+ system), member 2"
                     /calculated_mol_wt=71542
     Region          5..608
                     /region_name="2A0303"
                     /note="cationic amino acid transport permease; TIGR00906"
                     /db_xref="CDD:273330"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52569.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52569.2)"
     Site            38..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            64..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P52569.2)"
     Site            164..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            193..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P52569.2)"
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P52569.2)"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            290..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            340..360
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            387..407
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52569.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P52569.2)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52569.2)"
     Site            491..511
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            525..549
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            558..578
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            583..603
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            646
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P52569.2)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52569.2)"
     CDS             1..658
                     /gene="SLC7A2"
                     /gene_synonym="ATRC2; CAT-2A; CAT-2B; CAT2; HCAT2;
                     SLC7A2A; SLC7A2B"
                     /coded_by="NM_001370338.1:219..2195"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS34852.1"
                     /db_xref="GeneID:6542"
                     /db_xref="HGNC:HGNC:11060"
                     /db_xref="MIM:601872"
ORIGIN      
        1 mipcraaltf arclirrkiv tldsledtkl crclstmdli algvgstlga gvyvlageva
       61 kadsgpsivv sfliaalasv maglcyaefg arvpktgsay lytyvtvgel wafitgwnli
      121 lsyvigtssv arawsgtfde llskqigqfl rtyfrmnytg laeypdffav clilllagll
      181 sfgvkesawv nkvftavnil vllfvmvagf vkgnvanwki seeflknisa sareppseng
      241 tsiygaggfm pygftgtlag aatcfyafvg fdciattgee vrnpqkaipi givtsllvcf
      301 mayfgvsaal tlmmpyylld eksplpvafe yvgwgpakyv vaagslcals tsllgsifpm
      361 prviyamaed gllfkclaqi nsktktpiia tlssgavaal maflfdlkal vdmmsigtlm
      421 ayslvaacvl ilryqpglsy dqpkcspekd glgssprvts ksesqvtmlq rqgfsmrtlf
      481 cpsllptqqs aslvsflvgf laflvlglsv lttygvhait rleawslall alflvlfvai
      541 vltiwrqpqn qqkvafmvpf lpflpafsil vniylmvqls adtwvrfsiw maigfliyfs
      601 ygirhslegh lrdenneeda ypdnvhaaae eksaiqandh hprnlsspfi fhektsef
//
LOCUS       NP_003043                639 aa            linear   PRI 27-APR-2025
DEFINITION  sodium-dependent phosphate transport protein 2A isoform 1 [Homo
            sapiens].
ACCESSION   NP_003043 XP_005266030
VERSION     NP_003043.3
DBSOURCE    REFSEQ: accession NM_003052.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Sneddon,W.B., Ramineni,S., Van Doorn,G.E., Hepler,J.R. and
            Friedman,P.A.
  TITLE     Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport
  JOURNAL   Biochem Biophys Res Commun 733, 150700 (2024)
   PUBMED   39293332
  REMARK    GeneRIF: Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport.
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Wang,Q., Chen,J.J., Wei,L.Y., Ding,Y., Liu,M., Li,W.J., Su,C. and
            Gong,C.X.
  TITLE     Biallelic and monoallelic pathogenic variants in CYP24A1 and
            SLC34A1 genes cause idiopathic infantile hypercalcemia
  JOURNAL   Orphanet J Rare Dis 19 (1), 126 (2024)
   PUBMED   38504242
  REMARK    GeneRIF: Biallelic and monoallelic pathogenic variants in CYP24A1
            and SLC34A1 genes cause idiopathic infantile hypercalcemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Marini,F., Giusti,F., Marasco,E., Xumerle,L., Kwiatkowska,K.M.,
            Garagnani,P., Biver,E., Ferrari,S., Iolascon,G., Iantomasi,T. and
            Brandi,M.L.
  TITLE     High frequency of heterozygous rare variants of the SLC34A1 and
            SLC9A3R1 genes in patients with atypical femur fracture
  JOURNAL   Eur J Endocrinol 188 (1) (2023)
   PUBMED   36762943
  REMARK    GeneRIF: High frequency of heterozygous rare variants of the
            SLC34A1 and SLC9A3R1 genes in patients with atypical femur
            fracture.
REFERENCE   4  (residues 1 to 639)
  AUTHORS   Bieri,C., Daryadel,A., Bettoni,C., Pastor-Arroyo,E.M.,
            Schnitzbauer,U., Hernando,N. and Wagner,C.A.
  TITLE     The human pathogenic 91del7 mutation in SLC34A1 has no effect in
            mineral homeostasis in mice
  JOURNAL   Sci Rep 12 (1), 6102 (2022)
   PUBMED   35414099
  REMARK    GeneRIF: The human pathogenic 91del7 mutation in SLC34A1 has no
            effect in mineral homeostasis in mice.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 639)
  AUTHORS   Rousseau-Nepton,I., Jones,G., Schlingmann,K., Kaufmann,M.,
            Zuijdwijk,C.S., Khatchadourian,K., Gupta,I.R., Pacaud,D.,
            Pinsk,M.N., Mokashi,A., Nour,M.A., Alexander,R.T. and Rodd,C.J.
  TITLE     CYP24A1 and SLC34A1 Pathogenic Variants Are Uncommon in a Canadian
            Cohort of Children with Hypercalcemia or Hypercalciuria
  JOURNAL   Horm Res Paediatr 94 (3-4), 124-132 (2021)
   PUBMED   34320495
  REMARK    GeneRIF: CYP24A1 and SLC34A1 Pathogenic Variants Are Uncommon in a
            Canadian Cohort of Children with Hypercalcemia or Hypercalciuria.
REFERENCE   6  (residues 1 to 639)
  AUTHORS   Taketani,Y., Miyamoto,Ki., Tanaka,K., Katai,K., Chikamori,M.,
            Tatsumi,S., Segawa,H., Yamamoto,H., Morita,K. and Takeda,E.
  TITLE     Gene structure and functional analysis of the human Na+/phosphate
            co-transporter
  JOURNAL   Biochem J 324 (Pt 3) (Pt 3), 927-934 (1997)
   PUBMED   9210418
REFERENCE   7  (residues 1 to 639)
  AUTHORS   Wagner,C.A., Waldegger,S., Osswald,H., Biber,J., Murer,H.,
            Busch,A.E. and Lang,F.
  TITLE     Heavy metals inhibit Pi-induced currents through human brush-border
            NaPi-3 cotransporter in Xenopus oocytes
  JOURNAL   Am J Physiol 271 (4 Pt 2), F926-F930 (1996)
   PUBMED   8898024
REFERENCE   8  (residues 1 to 639)
  AUTHORS   Hartmann,C.M., Hewson,A.S., Kos,C.H., Hilfiker,H., Soumounou,Y.,
            Murer,H. and Tenenhouse,H.S.
  TITLE     Structure of murine and human renal type II Na+-phosphate
            cotransporter genes (Npt2 and NPT2)
  JOURNAL   Proc Natl Acad Sci U S A 93 (14), 7409-7414 (1996)
   PUBMED   8693007
REFERENCE   9  (residues 1 to 639)
  AUTHORS   Kos,C.H., Tihy,F., Econs,M.J., Murer,H., Lemieux,N. and
            Tenenhouse,H.S.
  TITLE     Localization of a renal sodium-phosphate cotransporter gene to
            human chromosome 5q35
  JOURNAL   Genomics 19 (1), 176-177 (1994)
   PUBMED   8188224
REFERENCE   10 (residues 1 to 639)
  AUTHORS   Magagnin,S., Werner,A., Markovich,D., Sorribas,V., Stange,G.,
            Biber,J. and Murer,H.
  TITLE     Expression cloning of human and rat renal cortex Na/Pi cotransport
  JOURNAL   Proc Natl Acad Sci U S A 90 (13), 5979-5983 (1993)
   PUBMED   8327470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP275443.1, BC053349.1 and
            BC050385.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_005266030.1, NP_003043.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053349.1, AK096088.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324417.6/ ENSP00000321424.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..639
                     /product="sodium-dependent phosphate transport protein 2A
                     isoform 1"
                     /note="sodium/phosphate co-transporter; solute carrier
                     family 17 (sodium phosphate), member 2; sodium-dependent
                     phosphate transport protein 2A; renal sodium-dependent
                     phosphate transporter; Na+-phosphate cotransporter type
                     II; naPi-2a; sodium/phosphate cotransporter 2A;
                     sodium-phosphate transport protein 2A; Na(+)/Pi
                     cotransporter 2A; Na(+)-dependent phosphate cotransporter
                     2A; solute carrier family 34 (sodium phosphate), member 1;
                     solute carrier family 34 (type II sodium/phosphate
                     cotransporter), member 1"
                     /calculated_mol_wt=68807
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06496; propagated from
                     UniProtKB/Swiss-Prot (Q06495.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60825; propagated from
                     UniProtKB/Swiss-Prot (Q06495.1)"
     Site            104..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06495.1)"
     Region          108..590
                     /region_name="2a58"
                     /note="Phosphate:Na+ Symporter (PNaS) Family; TIGR01013"
                     /db_xref="CDD:162157"
     Site            146..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06495.1)"
     Site            166..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06495.1)"
     Site            298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06495.1)"
     Site            323
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06495.1)"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06495.1)"
     Site            348..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06495.1)"
     Site            413..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06495.1)"
     Site            467..487
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06495.1)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q06495.1)"
     Site            514..534
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06495.1)"
     Site            540..561
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06495.1)"
     Site            607
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06496; propagated from
                     UniProtKB/Swiss-Prot (Q06495.1)"
     Site            623
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q60825; propagated from
                     UniProtKB/Swiss-Prot (Q06495.1)"
     Site            625
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60825; propagated from
                     UniProtKB/Swiss-Prot (Q06495.1)"
     CDS             1..639
                     /gene="SLC34A1"
                     /gene_synonym="FRTS2; HCINF2; NAPI-3; NPHLOP1; NPT2;
                     NPTIIa; SLC11; SLC17A2"
                     /coded_by="NM_003052.5:102..2021"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4418.1"
                     /db_xref="GeneID:6569"
                     /db_xref="HGNC:HGNC:11019"
                     /db_xref="MIM:182309"
ORIGIN      
        1 mlsygerlgs pavsplpvrg ghvmrgtafa yvpspqvlhr ipgtsayafp slgpvalaeh
       61 tcpcgevler heplpaklal eeeqkpesrl vpklrqagam llkvplmltf lylfvcsldm
      121 lssafqlagg kvagdifkdn ailsnpvagl vvgilvtvlv qssststsii vsmvssglle
      181 vssaipiimg snigtsvtnt ivalmqagdr tdfrrafaga tvhdcfnwls vlvllpleaa
      241 tgylhhitrl vvasfnihgg rdapdllkii tepftkliiq ldesvitsia tgdeslrnhs
      301 liqiwchpds lqaptsmsra eanssqtlgn atmekcnhif vdtglpdlav glillagslv
      361 llctclillv kmlnsllkgq vakviqkvin tdfpapftwv tgyfamvvga smtfvvqsss
      421 vftsaitpli glgvisiera ypltlgsnig ttttailaal aspreklssa fqialchfff
      481 nisgillwyp vpctrlpirm akalgkrtak yrwfavlyll vcflllpslv fgismagwqv
      541 mvgvgtpfga llafvvlinv lqsrspghlp kwlqtwdflp rwmhslkpld hlitratlcc
      601 arpeprsppl pprvfleelp patpsprlal pahhnatrl
//
LOCUS       NP_001356190             868 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 245 isoform 3 [Mus musculus].
ACCESSION   NP_001356190
VERSION     NP_001356190.1
DBSOURCE    REFSEQ: accession NM_001369261.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 868)
  AUTHORS   Hoffman,B.G., Zavaglia,B., Witzsche,J., Ruiz de Algara,T.,
            Beach,M., Hoodless,P.A., Jones,S.J., Marra,M.A. and Helgason,C.D.
  TITLE     Identification of transcripts with enriched expression in the
            developing and adult pancreas
  JOURNAL   Genome Biol 9 (6), R99 (2008)
   PUBMED   18554416
REFERENCE   2  (residues 1 to 868)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX470220.11 and AL929577.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR13862062.200442.1,
                                           SRR13422598.250638.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 31.66 cM"
     Protein         1..868
                     /product="transmembrane protein 245 isoform 3"
                     /note="likely ortholog of H. sapiens chromosome 9 open
                     reading frame 5 (C9orf5); transmembrane 245"
                     /calculated_mol_wt=96120
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            56..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            181..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            237..257
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Region          289..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZXD8; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            377..397
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            449..469
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            489
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            540
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            564
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            615..635
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Region          <637..829
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
     Site            639..659
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            720..740
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            741..761
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            765..785
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            804..824
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     CDS             1..868
                     /gene="Tmem245"
                     /gene_synonym="A630051L19Rik; D730040F13Rik"
                     /coded_by="NM_001369261.1:19..2625"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:242474"
                     /db_xref="MGI:MGI:2445107"
ORIGIN      
        1 madrggpaea psprgsprpe sraprtvgpg etprtaalal rfdkpikqaf yntgavlfvc
       61 lccgaavlvy fileaflrpl lwavlcgtfl hpfkssltrl grlwlrrlhr ahtpivlaal
      121 llplcfadyg vealgeqalr rrrlllllga ggpllyglyc lgsylgvqvl lahagalicr
      181 gldyfsslwi wtlvvgyvlm vsfkwnastq rylravsipv wmillfhias lagswripvf
      241 lvivflmsvg tlyekqneke sagaelpgqv ismaastlan laisitgyes stedqpsdpp
      301 teptdkgepp palsasssss srsspsspsp tlgrqrpemg tflrkkktsd iyfvslvwai
      361 iavqlwlnlw ivqllpvpva vwiikklvih fgvvgflekr chawwqviec flkerqeala
      421 pwpiiglgkf llkvdskmii wlekmldkii sifiifllvi gtlllalllt akvhqesvhm
      481 ievtssline tlanhpewan wlpeaqvvqr alnsaannvy qygrewithk lhkilgdkvn
      541 ntaviekqvl elwdrlyhsw fvknvthsgr hkghkmhvsr qnswlgdild wqdiasfvhe
      601 nietflsile slwivmsrnv sllfttvttl ltilfysgta llnfvlslii flttlfylls
      661 ssdeyykpvk wvisltplsq pgpssniigq sveeairgvf daslkmagfy glytwlthti
      721 fginivfips alaailgavp flgtywaavp avldlwltqg lgckailllv fhllptyfvd
      781 taiysdisgg ghpyltglav aggayylgle gaiigpillc ilvvasniys amlvsptnsm
      841 ptpnqtpwpa qtqrtfrdis edlkssvd
//
LOCUS       NP_612367                260 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim29 [Homo
            sapiens].
ACCESSION   NP_612367
VERSION     NP_612367.1
DBSOURCE    REFSEQ: accession NM_138358.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Guo,L., Liu,J.J., Long,S.Y., Wang,P.Y., Li,S., Wang,J.L., Wei,X.F.,
            Li,J., Lei,L., Huang,A.L. and Hu,J.L.
  TITLE     TIM22 and TIM29 inhibit HBV replication by up-regulating SRSF1
            expression
  JOURNAL   J Med Virol 96 (2), e29439 (2024)
   PUBMED   38294104
  REMARK    GeneRIF: TIM22 and TIM29 inhibit HBV replication by up-regulating
            SRSF1 expression.
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Valpadashi,A., Callegari,S., Linden,A., Neumann,P., Ficner,R.,
            Urlaub,H., Deckers,M. and Rehling,P.
  TITLE     Defining the architecture of the human TIM22 complex by chemical
            crosslinking
  JOURNAL   FEBS Lett 595 (2), 157-168 (2021)
   PUBMED   33125709
  REMARK    GeneRIF: Defining the architecture of the human TIM22 complex by
            chemical crosslinking.
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Muriungi,N.G. and Ueda,K.
  TITLE     TIMM29 interacts with hepatitis B virus preS1 to modulate the HBV
            life cycle
  JOURNAL   Microbiol Immunol 64 (12), 792-809 (2020)
   PUBMED   32970362
  REMARK    GeneRIF: TIMM29 interacts with hepatitis B virus preS1 to modulate
            the HBV life cycle.
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Kang,Y., Stroud,D.A., Baker,M.J., De Souza,D.P., Frazier,A.E.,
            Liem,M., Tull,D., Mathivanan,S., McConville,M.J., Thorburn,D.R.,
            Ryan,M.T. and Stojanovski,D.
  TITLE     Sengers Syndrome-Associated Mitochondrial Acylglycerol Kinase Is a
            Subunit of the Human TIM22 Protein Import Complex
  JOURNAL   Mol Cell 67 (3), 457-470 (2017)
   PUBMED   28712726
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Vukotic,M., Nolte,H., Konig,T., Saita,S., Ananjew,M., Kruger,M.,
            Tatsuta,T. and Langer,T.
  TITLE     Acylglycerol Kinase Mutated in Sengers Syndrome Is a Subunit of the
            TIM22 Protein Translocase in Mitochondria
  JOURNAL   Mol Cell 67 (3), 471-483 (2017)
   PUBMED   28712724
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Callegari,S., Richter,F., Chojnacka,K., Jans,D.C., Lorenzi,I.,
            Pacheu-Grau,D., Jakobs,S., Lenz,C., Urlaub,H., Dudek,J.,
            Chacinska,A. and Rehling,P.
  TITLE     TIM29 is a subunit of the human carrier translocase required for
            protein transport
  JOURNAL   FEBS Lett 590 (23), 4147-4158 (2016)
   PUBMED   27718247
  REMARK    GeneRIF: TIM29 is required for the structural integrity of the
            TIM22 complex and for import of substrate proteins by the carrier
            translocase
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Kang,Y., Baker,M.J., Liem,M., Louber,J., McKenzie,M., Atukorala,I.,
            Ang,C.S., Keerthikumar,S., Mathivanan,S. and Stojanovski,D.
  TITLE     Tim29 is a novel subunit of the human TIM22 translocase and is
            involved in complex assembly and stability
  JOURNAL   Elife 5, e17463 (2016)
   PUBMED   27554484
  REMARK    GeneRIF: Here, the authors identify Tim29 (C19orf52) as a novel,
            metazoan-specific subunit of the human TIM22 complex. The protein
            is integrated into the mitochondrial inner membrane with it's
            C-terminus exposed to the intermembrane space.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011442.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007244.1, SRR3476690.518010.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000270502.7/
                                                  ENSP00000270502.5
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..260
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim29"
                     /note="uncharacterized protein C19orf52"
                     /calculated_mol_wt=25811
     transit_peptide 1..31
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9BSF4.2)"
                     /calculated_mol_wt=3440
     Region          24..186
                     /region_name="Tim29"
                     /note="Translocase of the Inner Mitochondrial membrane 29;
                     pfam10171"
                     /db_xref="CDD:462977"
     mat_peptide     32..260
                     /product="Mitochondrial import inner membrane translocase
                     subunit Tim29. /id=PRO_0000271006"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSF4.2)"
                     /calculated_mol_wt=25811
     Site            60..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSF4.2)"
     CDS             1..260
                     /gene="TIMM29"
                     /gene_synonym="C19orf52; TIM29"
                     /coded_by="NM_138358.4:13..795"
                     /db_xref="CCDS:CCDS12252.1"
                     /db_xref="GeneID:90580"
                     /db_xref="HGNC:HGNC:25152"
                     /db_xref="MIM:617380"
ORIGIN      
        1 maaaalrrfw srrraeagda vvakpgvwar lgswarallr dyaeacrdas aeararpgra
       61 avyvgllgga aacftlapse gafeeallea sgtllllapa trnreseafv qrllwlrgrg
      121 rlryvnlglc slvyeapfda qaslyqarcr ylqprwtdfp grvldvgfvg rwwvlgawmr
      181 dcdinddefl hlpahlrvvg pqqlhsetne rlfdekykpv vltddqvdqa lweeqvlqke
      241 kkdrlalsqa hslvqaeapr
//
LOCUS       NP_438169                243 aa            linear   PRI 27-APR-2025
DEFINITION  NEDD4-binding protein 2-like 1 isoform 1 [Homo sapiens].
ACCESSION   NP_438169
VERSION     NP_438169.2
DBSOURCE    REFSEQ: accession NM_052818.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Rao,P., Li,J., Xiong,J., Shen,S., Zeng,J. and Zhao,H.
  TITLE     MicroRNA-150-5p-mediated Inhibition of Cell Proliferation, G1/S
            Transition, and Migration in Bladder Cancer through Targeting
            NEDD4-binding Protein 2-like 1 Gene
  JOURNAL   J Physiol Investig 67 (3), 118-128 (2024)
   PUBMED   38910572
  REMARK    GeneRIF: MicroRNA-150-5p-mediated Inhibition of Cell Proliferation,
            G1/S Transition, and Migration in Bladder Cancer through Targeting
            NEDD4-binding Protein 2-like 1 Gene.
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Sasahira,T., Kurihara,M., Nishiguchi,Y., Fujiwara,R., Kirita,T. and
            Kuniyasu,H.
  TITLE     NEDD 4 binding protein 2-like 1 promotes cancer cell invasion in
            oral squamous cell carcinoma
  JOURNAL   Virchows Arch 469 (2), 163-172 (2016)
   PUBMED   27184799
  REMARK    GeneRIF: Cox proportional hazards analysis identified N4BP2L1
            expression as an independent predictor of disease-free survival
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Couch,F.J., Rommens,J.M., Neuhausen,S.L., Belanger,C., Dumont,M.,
            Abel,K., Bell,R., Berry,S., Bogden,R., Cannon-Albright,L.,
            Farid,L., Frye,C., Hattier,T., Janecki,T., Jiang,P., Kehrer,R.,
            Leblanc,J.F., McArthur-Morrison,J., Meney,D., Miki,Y., Peng,Y.,
            Samson,C., Schroeder,M., Snyder,S.C., Simard,J. et al.
  TITLE     Generation of an integrated transcription map of the BRCA2 region
            on chromosome 13q12-q13
  JOURNAL   Genomics 36 (1), 86-99 (1996)
   PUBMED   8812419
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI551105.1, AL137247.14 and AI783635.1.
            
            On Dec 9, 2006 this sequence version replaced NP_438169.1.
            
            Transcript Variant: This variant (1) encodes isoform 1. Variants 1
            and 3 both encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.158658.1,
                                           SRR1660809.62060.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380130.7/ ENSP00000369473.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q13.1"
     Protein         1..243
                     /product="NEDD4-binding protein 2-like 1 isoform 1"
                     /note="hypothetical gene CG018"
                     /calculated_mol_wt=28850
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TBK1.1)"
     Region          44..177
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
     CDS             1..243
                     /gene="N4BP2L1"
                     /gene_synonym="CG018"
                     /coded_by="NM_052818.3:49..780"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9345.2"
                     /db_xref="GeneID:90634"
                     /db_xref="HGNC:HGNC:25037"
                     /db_xref="MIM:621053"
ORIGIN      
        1 medsflqsfg rlslqpqqqq qrqrpprppp rgtpprrhsf rkhlyllrgl pgsgkttlar
       61 qlqhdfpral ifstddfffr edgayefnpd fleeahewnq krarkamrng ispiiidntn
      121 lhawemkpya vmalennyev ifrepdtrwk fnvqelarrn ihgvsrekih rmkeryehdv
      181 tfhsvlhaek psrmnrnqdr nnalpsnnar ywnsytefpn rrahggftne ssyhrrggch
      241 hgy
//
LOCUS       NP_001275669             129 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 273 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001275669
VERSION     NP_001275669.1
DBSOURCE    REFSEQ: accession NM_001288740.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CA396219.1, AL524299.3, BC047724.1 and BC031641.1.
            
            Transcript Variant: This variant (2) contains an alternate exon in
            the central coding region, which results in a frameshift, compared
            to variant 1. The encoded isoform (2) has a longer and distinct
            C-terminus.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL524299.3 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374153.7/ ENSP00000363268.1
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.23"
     Protein         1..129
                     /product="transmembrane protein 273 isoform 2 precursor"
                     /calculated_mol_wt=11981
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5T292.1)"
                     /calculated_mol_wt=2020
     Region          15..74
                     /region_name="DUF4514"
                     /note="Domain of unknown function (DUF4514); pfam14986"
                     /db_xref="CDD:464422"
     Site            39..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T292.1)"
     CDS             1..129
                     /gene="TMEM273"
                     /gene_synonym="C10orf128"
                     /coded_by="NM_001288740.3:56..445"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS73128.1"
                     /db_xref="GeneID:170371"
                     /db_xref="HGNC:HGNC:27274"
ORIGIN      
        1 mnlgvsmlri lflldvggaq vlatgktpga eidfkyalig tavgvaisag flalkicmir
       61 rhlfdddssd lkstpgglsd tiplkkrapr klqastlfsf ksllqchhci meglfkakpq
      121 flqkrctgd
//
LOCUS       NP_775838                362 aa            linear   PRI 27-APR-2025
DEFINITION  epoxide hydrolase 4 [Homo sapiens].
ACCESSION   NP_775838
VERSION     NP_775838.3
DBSOURCE    REFSEQ: accession NM_173567.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Shen,N., Gao,G., Lu,X., Jin,J., Lin,L., Qian,M. and Qin,Y.
  TITLE     Comprehensive analysis of the immune implication of EPHX4 gene in
            laryngeal squamous cell carcinoma
  JOURNAL   Braz J Otorhinolaryngol 90 (4), 101411 (2024)
   PUBMED   38663041
  REMARK    GeneRIF: Comprehensive analysis of the immune implication of EPHX4
            gene in laryngeal squamous cell carcinoma.
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Morisseau,C., Kodani,S.D., Kamita,S.G., Yang,J., Lee,K.S.S. and
            Hammock,B.D.
  TITLE     Relative Importance of Soluble and Microsomal Epoxide Hydrolases
            for the Hydrolysis of Epoxy-Fatty Acids in Human Tissues
  JOURNAL   Int J Mol Sci 22 (9), 4993 (2021)
   PUBMED   34066758
  REMARK    GeneRIF: Relative Importance of Soluble and Microsomal Epoxide
            Hydrolases for the Hydrolysis of Epoxy-Fatty Acids in Human
            Tissues.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Decker,M., Adamska,M., Cronin,A., Di Giallonardo,F., Burgener,J.,
            Marowsky,A., Falck,J.R., Morisseau,C., Hammock,B.D., Gruzdev,A.,
            Zeldin,D.C. and Arand,M.
  TITLE     EH3 (ABHD9): the first member of a new epoxide hydrolase family
            with high activity for fatty acid epoxides
  JOURNAL   J Lipid Res 53 (10), 2038-2045 (2012)
   PUBMED   22798687
  REMARK    GeneRIF: The identification of two human epoxide hydrolases: EH3
            and EH4.
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Bagryantseva,Y., Novotna,B., Rossner,P. Jr., Chvatalova,I.,
            Milcova,A., Svecova,V., Lnenickova,Z., Solansky,I. and Sram,R.J.
  TITLE     Oxidative damage to biological macromolecules in Prague bus drivers
            and garagemen: impact of air pollution and genetic polymorphisms
  JOURNAL   Toxicol Lett 199 (1), 60-68 (2010)
   PUBMED   20723587
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB475492.1, BC041475.1, AK074822.1 and AC104836.2.
            
            On Dec 25, 2008 this sequence version replaced NP_775838.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.50840.1,
                                           SRR1660807.55026.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370383.5/ ENSP00000359410.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..362
                     /product="epoxide hydrolase 4"
                     /note="abhydrolase domain containing 7; epoxide
                     hydrolase-related protein; abhydrolase domain-containing
                     protein 7"
                     /calculated_mol_wt=42194
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUS5.2)"
     Region          70..356
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     CDS             1..362
                     /gene="EPHX4"
                     /gene_synonym="ABHD7; EH4; EPHXRP"
                     /coded_by="NM_173567.5:96..1184"
                     /db_xref="CCDS:CCDS736.1"
                     /db_xref="GeneID:253152"
                     /db_xref="HGNC:HGNC:23758"
                     /db_xref="MIM:617401"
ORIGIN      
        1 marlrdclpr lmltlrsllf wslvycycgl casihllkll wslgkgpaqt frrparehpp
       61 aclsdpslgt hcyvrikdsg lrfhyvaage rgkplmlllh gfpefwyswr yqlrefksey
      121 rvvaldlrgy getdapihrq nykldclitd ikdildslgy skcvlighdw ggmiawliai
      181 cypemvmkli vinfphpnvf teyilrhpaq llkssyyyff qipwfpefmf sindfkvlkh
      241 lftshstgig rkgcqltted leayiyvfsq pgalsgpinh yrnifsclpl khhmvttptl
      301 llwgendafm evemaevtki yvknyfrlti lseashwlqq dqpdivnkli wtflkeetrk
      361 kd
//
LOCUS       NP_001193602             362 aa            linear   PRI 27-APR-2025
DEFINITION  protein ABHD12B isoform a [Homo sapiens].
ACCESSION   NP_001193602
VERSION     NP_001193602.1
DBSOURCE    REFSEQ: accession NM_001206673.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL358334.3 and AY311396.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY311396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337334.7/ ENSP00000336693.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.1"
     Protein         1..362
                     /product="protein ABHD12B isoform a"
                     /note="abhydrolase domain-containing protein 12B;
                     alpha/beta hydrolase domain-containing protein 12B;
                     protein ABHD12B"
                     /calculated_mol_wt=40645
     Region          <78..>169
                     /region_name="PTZ00360"
                     /note="sexual stage antigen; Provisional"
                     /db_xref="CDD:240379"
     Region          130..343
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
     CDS             1..362
                     /gene="ABHD12B"
                     /gene_synonym="BEM46L3; C14orf29; c14_5314"
                     /coded_by="NM_001206673.2:123..1211"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS55916.1"
                     /db_xref="GeneID:145447"
                     /db_xref="HGNC:HGNC:19837"
ORIGIN      
        1 mdaqdcqaaa speppgppar scvaawwdmv drnlryfphs csmlgrkiaa lydsftsksl
       61 kehvflplid mliyfnffka pflvdlkkpe lkiphtvnfy lrvepgvmlg iwhtvpscrg
      121 edakgkdccw yeaalrdgnp iivylhgsae hraashrlkl vkvlsdggfh vlsvdyrgfg
      181 dstgkpteeg lttdaicvye wtkarsgitp vclwghslgt gvatnaakvl eekgcpvdai
      241 vleapftnmw vasinypllk iyrnipgflr tlmdalrkdk iifpndenvk flsspllilh
      301 geddrtvple ygkklyeiar nayrnkervk mvifppgfqh nllcksptll itvrdflskq
      361 ws
//
LOCUS       NP_077229               1082 aa            linear   ROD 27-APR-2025
DEFINITION  importin-4 isoform 1 [Mus musculus].
ACCESSION   NP_077229
VERSION     NP_077229.4
DBSOURCE    REFSEQ: accession NM_024267.7
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Young,J.C., Major,A.T., Miyamoto,Y., Loveland,K.L. and Jans,D.A.
  TITLE     Distinct effects of importin alpha2 and alpha4 on Oct3/4
            localization and expression in mouse embryonic stem cells
  JOURNAL   FASEB J 25 (11), 3958-3965 (2011)
   PUBMED   21840941
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wang,J., Sarkar,T.R., Zhou,M., Sharan,S., Ritt,D.A., Veenstra,T.D.,
            Morrison,D.K., Huang,A.M. and Sterneck,E.
  TITLE     CCAAT/enhancer binding protein delta (C/EBPdelta, CEBPD)-mediated
            nuclear import of FANCD2 by IPO4 augments cellular response to DNA
            damage
  JOURNAL   Proc Natl Acad Sci U S A 107 (37), 16131-16136 (2010)
   PUBMED   20805509
  REMARK    GeneRIF: report a function of IPO4 and nuclear import in the
            Fanconi anemia pathway of DNA repair
REFERENCE   4  (residues 1 to 1082)
  AUTHORS   Pradeepa,M.M., Manjunatha,S., Sathish,V., Agrawal,S. and Rao,M.R.
  TITLE     Involvement of importin-4 in the transport of transition protein 2
            into the spermatid nucleus
  JOURNAL   Mol Cell Biol 28 (13), 4331-4341 (2008)
   PUBMED   17682055
REFERENCE   5  (residues 1 to 1082)
  AUTHORS   Wesselkamper,S.C., McDowell,S.A., Medvedovic,M., Dalton,T.P.,
            Deshmukh,H.S., Sartor,M.A., Case,L.M., Henning,L.N., Borchers,M.T.,
            Tomlinson,C.R., Prows,D.R. and Leikauf,G.D.
  TITLE     The role of metallothionein in the pathogenesis of acute lung
            injury
  JOURNAL   Am J Respir Cell Mol Biol 34 (1), 73-82 (2006)
   PUBMED   16166738
  REMARK    GeneRIF: Metallothionein deficient mice have a marked decrease in
            Importin 4 transcripts during acute lung injury
REFERENCE   6  (residues 1 to 1082)
  AUTHORS   Corbo,J.C. and Cepko,C.L.
  TITLE     A hybrid photoreceptor expressing both rod and cone genes in a
            mouse model of enhanced S-cone syndrome
  JOURNAL   PLoS Genet 1 (2), e11 (2005)
   PUBMED   16110338
  REMARK    Erratum:[PLoS Genet. 2008 Jan;4(1):e18]
REFERENCE   7  (residues 1 to 1082)
  AUTHORS   Jakel,S., Mingot,J.M., Schwarzmaier,P., Hartmann,E. and Gorlich,D.
  TITLE     Importins fulfil a dual function as nuclear import receptors and
            cytoplasmic chaperones for exposed basic domains
  JOURNAL   EMBO J 21 (3), 377-386 (2002)
   PUBMED   11823430
REFERENCE   8  (residues 1 to 1082)
  AUTHORS   Chu,C.C. and Paul,W.E.
  TITLE     Expressed genes in interleukin-4 treated B cells identified by cDNA
            representational difference analysis
  JOURNAL   Mol Immunol 35 (8), 487-502 (1998)
   PUBMED   9798653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK030490.1 and AK147086.1.
            
            On Mar 27, 2002 this sequence version replaced NP_077229.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK147086.1, AK030490.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 28.19 cM"
     Protein         1..1082
                     /product="importin-4 isoform 1"
                     /note="importin 4a; imp4; ran-binding protein 4"
                     /calculated_mol_wt=119144
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q8TEX9; propagated from
                     UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          24..90
                     /region_name="IBN_N"
                     /note="Importin-beta N-terminal domain; smart00913"
                     /db_xref="CDD:197981"
     Region          348..385
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          <353..>620
                     /region_name="KAP95"
                     /note="Karyopherin (importin) beta [Intracellular
                     trafficking and secretion]; COG5215"
                     /db_xref="CDD:227540"
     Region          353..381
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(370..371,374,377..378,381,412..413,416,419..420,423,
                     456..457,460,463..464,498..499,502,505..506)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          390..427
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          394..424
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          431..471
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          435..464
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          475..513
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          477..507
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          896..933
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          901..929
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          937..975
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          942..972
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..1082
                     /gene="Ipo4"
                     /gene_synonym="8430408O15Rik; Imp4a; RanBP4"
                     /coded_by="NM_024267.7:87..3335"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS27121.1"
                     /db_xref="GeneID:75751"
                     /db_xref="MGI:MGI:1923001"
ORIGIN      
        1 mepagleqil kelllpdter irrateqlqt ilrdpaalpa lfdllatatd sqirqfaavl
       61 trrrlnnrwr rlapeqresl kslvltalqk etvhsvsvsl aqlsatifrk eglqgwpqfm
      121 nllqhsthss hspekevgll llsvvvssqp eafhahqhel lqllnetlsd vsfpgvlfys
      181 lrtltaiary vrpddvslar mlvpkvvtal rtlipldevk acealealde mletelpiin
      241 phlsevltfc levaknvalg eplrvrvlcc ltflvkvksk allknrlvpp llhalfplma
      301 aeppmgqldp edqdsddddl eiglmgetpk hfavqvvdml alhlppeklc phvmpmleea
      361 lrsedpyqrk agflvlavls dgagdhirqr llypllqivc kglddpsqiv rnaalfalgq
      421 fsenlqphis syseevmpll lsylksvpmg nthhlakacy alenfvenlg pkvqpylpel
      481 mecmlqplkn pskartkela vsaigaiata aqdsllpyfp timdllrefl ltghedfhlv
      541 qiqsletlgv laralgesmk plaeeccqlg lglcihiddp dvrrctyslf aalsglmgeg
      601 lgpylpqitt lmllslrste givpqydgis sfllfdddse aeeeeelmde dmeeegddse
      661 isgysvenaf fdekedtcta lgeismntcv aflpfmdatf devykllecp hmnvrksaye
      721 algqfccalh kasqrsssdp ssspvlqtsl arvmpaymqa vkvererpvv mavlesltgv
      781 lrtcgslalq ppgrlselcn vlkavlqkkt acqdaeeddd edddqaeyda mllehageai
      841 pvlaataggh afapffatfl plllcktkqs ctvaeksfav gtlaesiqgl gtasaqfvsr
      901 lfpvllnnar eadpevrsna ifglgvlaeh ggcpaqdhfp kllglllpll arerhdrvrd
      961 nicgalarvl maspvgktep qvlatllral plkedmeewl tighlfsflh qnnpeqvvdv
     1021 asellricsl ilpdnrippd tkaalllllt flakqhtdsf htalgslpnd kaqelqammg
     1081 lt
//
LOCUS       NP_036472                921 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear factor of activated T-cells, cytoplasmic 2 isoform B [Homo
            sapiens].
ACCESSION   NP_036472
VERSION     NP_036472.2
DBSOURCE    REFSEQ: accession NM_012340.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Xiao,Z.J., Wang,S.Q., Chen,J.J., Li,Y., Jiang,Y., Tin,V.P., Liu,J.,
            Hu,H., Wong,M.P., Pan,Y. and Yam,J.W.P.
  TITLE     The Dual Role of the NFATc2/galectin-9 Axis in Modulating
            Tumor-Initiating Cell Phenotypes and Immune Suppression in Lung
            Adenocarcinoma
  JOURNAL   Adv Sci (Weinh) 11 (20), e2306059 (2024)
   PUBMED   38528665
  REMARK    GeneRIF: The Dual Role of the NFATc2/galectin-9 Axis in Modulating
            Tumor-Initiating Cell Phenotypes and Immune Suppression in Lung
            Adenocarcinoma.
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Ge,L., Rui,Y., Wang,C., Wu,Y., Wang,H. and Wang,J.
  TITLE     The RNA m6A reader IGF2BP3 regulates NFAT1/IRF1 axis-mediated
            anti-tumor activity in gastric cancer
  JOURNAL   Cell Death Dis 15 (3), 192 (2024)
   PUBMED   38448411
  REMARK    GeneRIF: The RNA m[6]A reader IGF2BP3 regulates NFAT1/IRF1
            axis-mediated anti-tumor activity in gastric cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 921)
  AUTHORS   Liu,L., Li,L., Ding,Y., Kong,F., Mo,W., Ye,H. and Shen,D.
  TITLE     Report and literature review of four cases of EWSR1::NFATC2 round
            cell sarcoma
  JOURNAL   Diagn Pathol 19 (1), 19 (2024)
   PUBMED   38254207
  REMARK    GeneRIF: Report and literature review of four cases of
            EWSR1::NFATC2 round cell sarcoma.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 921)
  AUTHORS   Vittal,R., Walker,N.M., McLinden,A.P., Braeuer,R.R., Ke,F.,
            Fattahi,F., Combs,M.P., Misumi,K., Aoki,Y., Wheeler,D.S.,
            Wilke,C.A., Huang,S.K., Moore,B.B., Cao,P. and Lama,V.N.
  TITLE     Genetic deficiency of the transcription factor NFAT1 confers
            protection against fibrogenic responses independent of immune
            influx
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 326 (1), L39-L51 (2024)
   PUBMED   37933452
  REMARK    GeneRIF: Genetic deficiency of the transcription factor NFAT1
            confers protection against fibrogenic responses independent of
            immune influx.
REFERENCE   5  (residues 1 to 921)
  AUTHORS   Malsy,M., Graf,B., Bruendl,E., Maier-Stocker,C. and Bundscherer,A.
  TITLE     Effect of NFATc2- and Sp1-mediated TNFalpha Regulation on the
            Proliferation and Migration Behavior of Pancreatic Cancer Cells
  JOURNAL   Cancer Genomics Proteomics 20 (6suppl), 706-711 (2023)
   PUBMED   38035702
  REMARK    GeneRIF: Effect of NFATc2- and Sp1-mediated TNFalpha Regulation on
            the Proliferation and Migration Behavior of Pancreatic Cancer
            Cells.
REFERENCE   6  (residues 1 to 921)
  AUTHORS   Aramburu,J., Azzoni,L., Rao,A. and Perussia,B.
  TITLE     Activation and expression of the nuclear factors of activated T
            cells, NFATp and NFATc, in human natural killer cells: regulation
            upon CD16 ligand binding
  JOURNAL   J Exp Med 182 (3), 801-810 (1995)
   PUBMED   7650486
REFERENCE   7  (residues 1 to 921)
  AUTHORS   Auffray,C., Behar,G., Bois,F., Bouchier,C., Da Silva,C.,
            Devignes,M.D., Duprat,S., Houlgatte,R., Jumeau,M.N., Lamy,B. et al.
  TITLE     [IMAGE: molecular integration of the analysis of the human genome
            and its expression]
  JOURNAL   C R Acad Sci III 318 (2), 263-272 (1995)
   PUBMED   7757816
REFERENCE   8  (residues 1 to 921)
  AUTHORS   Li,X., Ho,S.N., Luna,J., Giacalone,J., Thomas,D.J., Timmerman,L.A.,
            Crabtree,G.R. and Francke,U.
  TITLE     Cloning and chromosomal localization of the human and murine genes
            for the T-cell transcription factors NFATc and NFATp
  JOURNAL   Cytogenet Cell Genet 68 (3-4), 185-191 (1995)
   PUBMED   7842733
REFERENCE   9  (residues 1 to 921)
  AUTHORS   Vacca,A., Farina,M., Maroder,M., Alesse,E., Screpanti,I., Frati,L.
            and Gulino,A.
  TITLE     Human immunodeficiency virus type-1 tat enhances interleukin-2
            promoter activity through synergism with phorbol ester and
            calcium-mediated activation of the NF-AT cis-regulatory motif
  JOURNAL   Biochem Biophys Res Commun 205 (1), 467-474 (1994)
   PUBMED   7999066
REFERENCE   10 (residues 1 to 921)
  AUTHORS   Ho,S., Timmerman,L., Northrop,J. and Crabtree,G.R.
  TITLE     Cloning and characterization of NF-ATc and NF-ATp: the cytoplasmic
            components of NF-AT
  JOURNAL   Adv Exp Med Biol 365, 167-173 (1994)
   PUBMED   7887301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from EU887576.1, EU887573.1,
            AL035682.16 and BE674599.1.
            
            On Jan 24, 2003 this sequence version replaced NP_036472.1.
            
            Summary: This gene is a member of the nuclear factor of activated T
            cells (NFAT) family. The product of this gene is a DNA-binding
            protein with a REL-homology region (RHR) and an NFAT-homology
            region (NHR). This protein is present in the cytosol and only
            translocates to the nucleus upon T cell receptor (TCR) stimulation,
            where it becomes a member of the nuclear factors of activated T
            cells transcription complex. This complex plays a central role in
            inducing gene transcription during the immune response. Alternate
            transcriptional splice variants encoding different isoforms have
            been characterized. [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (1) contains an alternate exon in
            the 3' end compared to variant 2, that causes a frameshift. The
            resulting isoform (B) has a shorter and distinct C-terminus
            compared to isoform C.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU887573.1, BC144074.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371564.8/ ENSP00000360619.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.2"
     Protein         1..921
                     /product="nuclear factor of activated T-cells, cytoplasmic
                     2 isoform B"
                     /note="nuclear factor of activated T-cells, preexisting
                     component; NFAT transcription complex, preexisting
                     component; nuclear factor of activated T-cells,
                     cytoplasmic 2; T cell transcription factor NFAT1; NFAT
                     pre-existing subunit; preexisting nuclear factor of
                     activated T-cells 2; NF-ATc2; nuclear factor of activated
                     T-cells, cytoplasmic, calcineurin-dependent 2"
                     /calculated_mol_wt=99654
     Region          1..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13469.2)"
     Region          <4..442
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Region          26..34
                     /region_name="9aaTAD"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13469.2)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Region          111..116
                     /region_name="Calcineurin-binding.
                     /evidence=ECO:0000269|PubMed:26248042"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13469.2)"
     Region          119..199
                     /region_name="Transactivation domain A (TAD-A)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13469.2)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Region          161..175
                     /region_name="Required for cytoplasmic retention of the
                     phosphorylated form. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13469.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Region          184..286
                     /region_name="3 X approximate SP repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13469.2)"
     Region          195..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13469.2)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Region          251..253
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13469.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60591; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Region          398..572
                     /region_name="RHD-n_NFAT"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor of activated T-cells (NFAT)
                     proteins; cd07881"
                     /db_xref="CDD:143641"
     Site            order(421,424,426..427,429..431,479,520,522..523,537..538,
                     540,571)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143641"
     Region          577..677
                     /region_name="IPT_NFAT"
                     /note="IPT domain of the NFAT family of transcription
                     factors. NFAT transcription complexes are a target of
                     calcineurin, a calcium dependent phosphatase, and activate
                     genes mainly involved in cell-cell-interaction; cd01178"
                     /db_xref="CDD:238583"
     Site            order(601,665)
                     /site_type="DNA binding"
                     /note="DNA binding sites [nucleotide binding]"
                     /db_xref="CDD:238583"
     Region          664..666
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13469.2)"
     Site            755
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Region          839..894
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13469.2)"
     Site            856
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13469.2)"
     CDS             1..921
                     /gene="NFATC2"
                     /gene_synonym="JCOSL; NFAT1; NFATP"
                     /coded_by="NM_012340.5:221..2986"
                     /note="isoform B is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33488.1"
                     /db_xref="GeneID:4773"
                     /db_xref="HGNC:HGNC:7776"
                     /db_xref="MIM:600490"
ORIGIN      
        1 mnaperqpqp dggdapghep ggspqdeldf silfdyeyln pneeepnahk vasppsgpay
       61 pddvldyglk pysplaslsg eppgrfgepd rvgpqkflsa akpagasgls prieitpshe
      121 liqavgplrm rdagllveqp plagvaaspr ftlpvpgfeg yreplclspa ssgssasfis
      181 dtfspytspc vspnnggpdd lcpqfqnipa hysprtspim sprtslaeds clgrhspvpr
      241 pasrssspga krrhscaeal valppgaspq rsrspspqps shvapqdhgs pagyppvags
      301 avimdalnsl atdspcgipp kmwktspdps pvsaapskag lprhiypave flgpceqger
      361 rnsapesill vpptwpkplv paipicsipv taslpplewp lssqsgsyel rievqpkphh
      421 rahyetegsr gavkaptggh pvvqlhgyme nkplglqifi gtaderilkp hafyqvhrit
      481 gktvtttsye kivgntkvle iplepknnmr atidcagilk lrnadielrk getdigrknt
      541 rvrlvfrvhi pessgrivsl qtasnpiecs qrsahelpmv erqdtdsclv yggqqmiltg
      601 qnftseskvv ftekttdgqq iwemeatvdk dksqpnmlfv eipeyrnkhi rtpvkvnfyv
      661 ingkrkrsqp qhftyhpvpa ikteptdeyd ptlicspthg glgsqpyypq hpmvaespsc
      721 lvatmapcqq frtglsspda ryqqqnpaav lyqrskslsp sllgyqqpal maaplslada
      781 hrsvlvhags qgqssallhp sptnqqaspv ihysptnqql rcgshqefqh imycenfapg
      841 ttrpgpppvs qgqrlspgsy ptviqqqnat sqraakngpp vsdqkevlpa gvtikqeqnl
      901 dqtylddeli dthlswiqni l
//
LOCUS       NP_001186224             640 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 549 isoform 1 [Homo sapiens].
ACCESSION   NP_001186224
VERSION     NP_001186224.2
DBSOURCE    REFSEQ: accession NM_001199295.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Zhao,Z. and Qin,X.
  TITLE     MicroRNA-708 targeting ZNF549 regulates colon adenocarcinoma
            development through PI3K/AKt pathway
  JOURNAL   Sci Rep 10 (1), 16729 (2020)
   PUBMED   33028966
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC003682.1.
            
            On Nov 23, 2018 this sequence version replaced NP_001186224.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060863.1, SRR1660809.82153.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376233.8/ ENSP00000365407.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..640
                     /product="zinc finger protein 549 isoform 1"
                     /calculated_mol_wt=74308
     Region          27..67
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          223..603
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          224..241
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          249..269
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          277..298
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          306..326
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          334..355
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          363..383
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          391..411
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(396,398,400,402..403,406..407,410,424,426,430..431,
                     434..435,438,452,454,456,458..459,462..463,466)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          419..439
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          447..467
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          475..495
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          503..523
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          531..551
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          559..579
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(564,566,568,570..571,574..575,578,592,594,598..599,
                     602..603,606,620,622,624,626..627,630..631,634)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          587..607
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          600..624
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          615..635
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..640
                     /gene="ZNF549"
                     /coded_by="NM_001199295.2:219..2141"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS56106.1"
                     /db_xref="GeneID:256051"
                     /db_xref="HGNC:HGNC:26632"
                     /db_xref="MIM:620720"
ORIGIN      
        1 maeaalvitp qipmvteefv kpsqghvtfe diavyfsqee wglldeaqrc lyhdvmlenf
       61 slmasvgclh gieaeeapse qtlsaqgvsq artpklgpsi pnahscemci lvmkdilyls
      121 ehqgtlpwqk pytsvasgkw fsfgsnlqqh qnqdsgekhi rkeessalll nsckiplsdn
      181 lfpckdvekd fptilgllqh qtthsrqeya hrsretfqqr rykceqvfne kvhvtehqrv
      241 htgekaykrr eygkslnsky lfvehqrthn aekpyvcnic gksflhkqtl vghqqrihtr
      301 ersyvciecg kslsskyslv ehqrthngek pyvcnvcgks frhkqtfvgh qqrihtgerp
      361 yvcmecgksf ihsydrirhq rvhtgegayq csecgksfiy kqslldhhri htgerpyeck
      421 ecgkafihkk rllehqriht gekpyvciic gksfirssdy mrhqrihtge rayecsdcgk
      481 afiskqtllk hhkihtrerp yecsecgkgf ylevkllqhq rihtreqlce cnecgkvfsh
      541 qkrllehqkv htgekpcecs ecgkcfrhrt sliqhqkvhs gerpynctac ekafiyknkl
      601 vehqrihtge kpyecgkcgk afnkryslvr hqkvhiteep
//
LOCUS       NP_036250                431 aa            linear   PRI 27-APR-2025
DEFINITION  nocturnin [Homo sapiens].
ACCESSION   NP_036250
VERSION     NP_036250.2
DBSOURCE    REFSEQ: accession NM_012118.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Abshire,E.T., Hughes,K.L., Diao,R., Pearce,S., Gopalakrishna,S.,
            Trievel,R.C., Rorbach,J., Freddolino,P.L. and Goldstrohm,A.C.
  TITLE     Differential processing and localization of human Nocturnin
            controls metabolism of mRNA and nicotinamide adenine dinucleotide
            cofactors
  JOURNAL   J Biol Chem 295 (44), 15112-15133 (2020)
   PUBMED   32839274
  REMARK    GeneRIF: Differential processing and localization of human
            Nocturnin controls metabolism of mRNA and nicotinamide adenine
            dinucleotide cofactors.
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Bracci,M., Copertaro,A., Ciarapica,V., Barbaresi,M., Esposito,S.,
            Albanesi,A., Valentino,M., Ledda,C., Rapisarda,V. and Santarelli,L.
  TITLE     NOCTURNIN Gene Diurnal Variation in Healthy Volunteers and
            Expression Levels in Shift Workers
  JOURNAL   Biomed Res Int 2019, 7582734 (2019)
   PUBMED   31467910
  REMARK    GeneRIF: Measuring NOCTURNIN expression levels in human peripheral
            blood lymphocytes can improve investigations on the relationship
            between changes in circadian rhythm and metabolic disorders. Shift
            workers show higher NOCTURNIN levels than daytime worker
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Estrella,M.A., Du,J., Chen,L., Rath,S., Prangley,E., Chitrakar,A.,
            Aoki,T., Schedl,P., Rabinowitz,J. and Korennykh,A.
  TITLE     The metabolites NADP+ and NADPH are the targets of the circadian
            protein Nocturnin (Curled)
  JOURNAL   Nat Commun 10 (1), 2367 (2019)
   PUBMED   31147539
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Li,R., Yue,J., Zhang,Y., Zhou,L., Hao,W., Yuan,J., Qiang,B.,
            Ding,J.M., Peng,X. and Cao,J.M.
  TITLE     CLOCK/BMAL1 regulates human nocturnin transcription through binding
            to the E-box of nocturnin promoter
  JOURNAL   Mol Cell Biochem 317 (1-2), 169-177 (2008)
   PUBMED   18587630
  REMARK    GeneRIF: The transcription of human nocturnin gene displayed
            circadian oscillations in Huh7 cells (a human hepatoma cell line)
            and was regulated by CLOCK/BMAL1 heterodimer via the E-box of
            nocturnin promoter.
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Nakamura,E.S., Koizumi,K., Kobayashi,M., Saitoh,Y., Arita,Y.,
            Nakayama,T., Sakurai,H., Yoshie,O. and Saiki,I.
  TITLE     RANKL-induced CCL22/macrophage-derived chemokine produced from
            osteoclasts potentially promotes the bone metastasis of lung cancer
            expressing its receptor CCR4
  JOURNAL   Clin Exp Metastasis 23 (1), 9-18 (2006)
   PUBMED   16821125
  REMARK    GeneRIF: A human lung cancer cell line SBC-5 that efficiently
            metastasized to bone when intravenously injected into SCID mice was
            found to express CCR4.
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Wang,Y., Osterbur,D.L., Megaw,P.L., Tosini,G., Fukuhara,C.,
            Green,C.B. and Besharse,J.C.
  TITLE     Rhythmic expression of Nocturnin mRNA in multiple tissues of the
            mouse
  JOURNAL   BMC Dev Biol 1, 9 (2001)
   PUBMED   11394964
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Dupressoir,A., Barbot,W., Loireau,M.P. and Heidmann,T.
  TITLE     Characterization of a mammalian gene related to the yeast CCR4
            general transcription factor and revealed by transposon insertion
  JOURNAL   J Biol Chem 274 (43), 31068-31075 (1999)
   PUBMED   10521507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY067201.1, BC113494.1 and
            AC093602.5.
            
            On May 27, 2003 this sequence version replaced NP_036250.1.
            
            Summary: The protein encoded by this gene is highly similar to
            Nocturnin, a gene identified as a circadian clock regulated gene in
            Xenopus laevis. This protein and Nocturnin protein share similarity
            with the C-terminal domain of a yeast transcription factor, carbon
            catabolite repression 4 (CCR4). The mRNA abundance of a similar
            gene in mouse has been shown to exhibit circadian rhythmicity,
            which suggests a role for this protein in clock function or as a
            circadian clock effector. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.329239.1, AF183961.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280614.4/ ENSP00000280614.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..431
                     /product="nocturnin"
                     /EC_number="3.1.3.108"
                     /note="CCR4-like (carbon catabolite repression 4,
                     S.cerevisiae); CCR4 protein homolog; circadian deadenylase
                     NOC; carbon catabolite repression 4-like protein; CCR4
                     carbon catabolite repression 4-like"
                     /calculated_mol_wt=48065
     Region          20..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK39.2)"
     Region          144..423
                     /region_name="Deadenylase_nocturnin"
                     /note="C-terminal deadenylase domain of nocturnin and
                     related domains; cd09096"
                     /db_xref="CDD:197330"
     Site            order(149,195,286,289,291,297,324,326,328,367,372,
                     376..377,414)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197330"
     Site            order(149,195,286,289,291,297,324,326,328,367,372,376,414)
                     /site_type="other"
                     /note="putative poly(A) RNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:197330"
     Site            order(149,195,286,324,326,377,413..414)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197330"
     Site            order(149,195,413)
                     /site_type="other"
                     /note="putative Mg binding site A [ion binding]"
                     /db_xref="CDD:197330"
     Site            order(286,326,414)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197330"
     Site            order(324,326,414)
                     /site_type="other"
                     /note="putative Mg binding site B [ion binding]"
                     /db_xref="CDD:197330"
     Region          343..353
                     /region_name="Interaction with PPARG.
                     /evidence=ECO:0000250|UniProtKB:O35710"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK39.2)"
     CDS             1..431
                     /gene="NOCT"
                     /gene_synonym="Ccr4c; CCR4L; CCRN4L; NOC"
                     /coded_by="NM_012118.4:202..1497"
                     /db_xref="CCDS:CCDS3743.1"
                     /db_xref="GeneID:25819"
                     /db_xref="HGNC:HGNC:14254"
                     /db_xref="MIM:608468"
ORIGIN      
        1 mfhsprrlcs allqrdapgl rrlpapglrr plsppaavpr pasprllaaa saasgaarsc
       61 srtvcsmgtg tsrlysalak tlnssaasqh peylvspdpe hlepidpkel leecravlht
      121 rpprfqrdfv dlrtdcpsth ppirvmqwni laqalgegkd nfvqcpveal kweerkclil
      181 eeilayqpdi lclqevdhyf dtfqpllsrl gyqgtffpkp wspcldvehn ngpdgcalff
      241 lqnrfklvns anirltamtl ktnqvaiaqt leckesgrqf ciavthlkar tgwerfrsaq
      301 gcdllqnlqn itqgakipli vcgdfnaept eevykhfass slnlnsaykl lsadgqsepp
      361 yttwkirtsg ecrhtldyiw yskhalnvrs aldllteeqi gpnrlpsfny psdhlslvcd
      421 fsfteesdgl s
//
LOCUS       NP_003491                681 aa            linear   PRI 27-APR-2025
DEFINITION  peroxisomal acyl-coenzyme A oxidase 2 [Homo sapiens].
ACCESSION   NP_003491
VERSION     NP_003491.1
DBSOURCE    REFSEQ: accession NM_003500.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Zhang,Q., Zhang,Y., Sun,S., Wang,K., Qian,J., Cui,Z., Tao,T. and
            Zhou,J.
  TITLE     ACOX2 is a prognostic marker and impedes the progression of
            hepatocellular carcinoma via PPARalpha pathway
  JOURNAL   Cell Death Dis 12 (1), 15 (2021)
   PUBMED   33414412
  REMARK    GeneRIF: ACOX2 is a prognostic marker and impedes the progression
            of hepatocellular carcinoma via PPARalpha pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 681)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 681)
  AUTHORS   Lisowska,M., Pietrucha,T. and Sakowicz,A.
  TITLE     Preeclampsia and Related Cardiovascular Risk: Common Genetic
            Background
  JOURNAL   Curr Hypertens Rep 20 (8), 71 (2018)
   PUBMED   29971632
  REMARK    GeneRIF: ACOX2, physiologically responsible for one of the stages
            in the degradation of branched-chain fatty acids and bile acid, may
            be a possible genetic risk factor linking Preeclampsia and Related
            Cardiovascular diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 681)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 681)
  AUTHORS   Moghrabi,N.N., Naylor,S.L., Van Veldhoven,P.P., Baumgart,E.,
            Dawson,D.B. and Bennett,M.J.
  TITLE     Assignment of the human peroxisomal branched-chain acyl-CoA oxidase
            gene to chromosome 3p21.1-p14.2 by rodent/human somatic cell
            hybridization
  JOURNAL   Biochem Biophys Res Commun 231 (3), 767-769 (1997)
   PUBMED   9070889
REFERENCE   7  (residues 1 to 681)
  AUTHORS   Baumgart,E., Vanhooren,J.C., Fransen,M., Mannaerts,G.P. and Van
            Veldhoven,P.P.
  TITLE     Mammalian peroxisomal acyl-CoA oxidases. III. Molecular
            characterization of human branched chain fatty acyl-CoA oxidase
  JOURNAL   Ann N Y Acad Sci 804, 678-679 (1996)
   PUBMED   8993592
REFERENCE   8  (residues 1 to 681)
  AUTHORS   Baumgart,E., Vanhooren,J.C., Fransen,M., Marynen,P., Puype,M.,
            Vandekerckhove,J., Leunissen,J.A., Fahimi,H.D., Mannaerts,G.P. and
            van Veldhoven,P.P.
  TITLE     Molecular characterization of the human peroxisomal branched-chain
            acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue
            distribution, and evidence for the absence of the protein in
            Zellweger syndrome
  JOURNAL   Proc Natl Acad Sci U S A 93 (24), 13748-13753 (1996)
   PUBMED   8943006
REFERENCE   9  (residues 1 to 681)
  AUTHORS   Vanhove,G.F., Van Veldhoven,P.P., Fransen,M., Denis,S.,
            Eyssen,H.J., Wanders,R.J. and Mannaerts,G.P.
  TITLE     The CoA esters of 2-methyl-branched chain fatty acids and of the
            bile acid intermediates di- and trihydroxycoprostanic acids are
            oxidized by one single peroxisomal branched chain acyl-CoA oxidase
            in human liver and kidney
  JOURNAL   J Biol Chem 268 (14), 10335-10344 (1993)
   PUBMED   8387517
REFERENCE   10 (residues 1 to 681)
  AUTHORS   Casteels,M., Schepers,L., Van Veldhoven,P.P., Eyssen,H.J. and
            Mannaerts,G.P.
  TITLE     Separate peroxisomal oxidases for fatty acyl-CoAs and
            trihydroxycoprostanoyl-CoA in human liver
  JOURNAL   J Lipid Res 31 (10), 1865-1872 (1990)
   PUBMED   2079609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG698950.1, BC047700.1 and
            AC116036.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The product of this gene belongs to the acyl-CoA oxidase
            family. It encodes the branched-chain acyl-CoA oxidase which is
            involved in the degradation of long branched fatty acids and bile
            acid intermediates in peroxisomes. Deficiency of this enzyme
            results in the accumulation of branched fatty acids and bile acid
            intermediates, and may lead to Zellweger syndrome, severe cognitive
            disability, and death in children. [provided by RefSeq, Mar 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.462859.1,
                                           SRR5189667.126401.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302819.10/ ENSP00000307697.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     Protein         1..681
                     /product="peroxisomal acyl-coenzyme A oxidase 2"
                     /EC_number="1.17.99.3"
                     /note="acyl-Coenzyme A oxidase 2, branched chain; THCA-CoA
                     oxidase; trihydroxycoprostanoyl-CoA oxidase; peroxisomal
                     branched chain acyl-CoA oxidase;
                     3-alpha,7-alpha,
                     12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase;
                     3-alpha,7-alpha,
                     12-alpha-trihydroxy-5-beta-cholestanoyl-CoA
                     24-hydroxylase; acyl-CoA oxidase 2, branched chain"
                     /calculated_mol_wt=76696
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97562; propagated from
                     UniProtKB/Swiss-Prot (Q99424.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99424.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99424.1)"
     Region          20..655
                     /region_name="ACAD"
                     /note="Acyl-CoA dehydrogenase; cl09933"
                     /db_xref="CDD:447864"
     Site            order(121,151,153,191,193,435..437,439,441)
                     /site_type="active"
                     /db_xref="CDD:173839"
     Region          679..681
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99424.1)"
     CDS             1..681
                     /gene="ACOX2"
                     /gene_synonym="BCOX; BRCACOX; BRCOX; CBAS6; THCCox"
                     /coded_by="NM_003500.4:164..2209"
                     /db_xref="CCDS:CCDS33775.1"
                     /db_xref="GeneID:8309"
                     /db_xref="HGNC:HGNC:120"
                     /db_xref="MIM:601641"
ORIGIN      
        1 mgspvhrvsl gdtwsrqmhp dieserymqs fdverltnil dggaqntalr rkvesiihsy
       61 pefsckdnyf mtqnerykaa mrrafhirli arrlgwledg relgyayral sgdvalnihr
      121 vfvralrslg seeqiakwdp lckniqiiat yaqtelghgt ylqgleteat ydaatqefvi
      181 hsptltatkw wpgdlgrsat halvqaqlic sgarrgmhaf ivpirslqdh tplpgiiigd
      241 igpkmdfdqt dngflqlnhv rvprenmlsr faqvlpdgty vklgtaqsny lpmvvvrvel
      301 lsgeilpilq kacviamrys virrqsrlrp sdpeakvldy qtqqqklfpq laisyafhfl
      361 avslleffqh sytailnqdf sflpelhals tgmkammsef ctqgaemcrr acgghgyskl
      421 sglpslvtkl sasctyegen tvlylqvarf lvksylqtqm spgstpqrsl spsvayltap
      481 dlarcpaqra adflcpelyt tawahvavrl ikdsvqhlqt ltqsgadqhe awnqttvihl
      541 qaakvhcyyv tvkgfteale klenepaiqq vlkrlcdlha ihgiltnsgd flhdaflsga
      601 qvdmartayl dllrlirkda illtdafdft dqclnsalgc ydgnvyerlf qwaqksptnt
      661 qenpayeeyi rpllqswrsk l
//
LOCUS       NP_001005285             320 aa            linear   PRI 27-APR-2025
DEFINITION  olfactory receptor 2AT4 isoform 1 [Homo sapiens].
ACCESSION   NP_001005285 XP_016873144
VERSION     NP_001005285.1
DBSOURCE    REFSEQ: accession NM_001005285.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Piccini,I., Cheret,J., Tsutsumi,M., Sakaguchi,S., Ponce,L.,
            Almeida,L., Funk,W., Kuckelhaus,M., Kajiya,K., Paus,R. and
            Bertolini,M.
  TITLE     Preliminary evidence that Merkel cells exert chemosensory functions
            in human epidermis
  JOURNAL   Exp Dermatol 32 (10), 1848-1855 (2023)
   PUBMED   37587642
  REMARK    GeneRIF: Preliminary evidence that Merkel cells exert chemosensory
            functions in human epidermis.
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Shi,J., Lu,D., Gu,R., Xu,Y., Pan,R., Bo,F. and Zhang,Y.
  TITLE     Identification of Key Biomarkers and Immune Infiltration in
            Sporadic Vestibular Schwannoma Basing Transcriptome-Wide Profiling
  JOURNAL   World Neurosurg 160, e591-e600 (2022)
   PUBMED   35092815
  REMARK    GeneRIF: Identification of Key Biomarkers and Immune Infiltration
            in Sporadic Vestibular Schwannoma Basing Transcriptome-Wide
            Profiling.
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Cheret,J., Bertolini,M., Ponce,L., Lehmann,J., Tsai,T., Alam,M.,
            Hatt,H. and Paus,R.
  TITLE     Olfactory receptor OR2AT4 regulates human hair growth
  JOURNAL   Nat Commun 9 (1), 3624 (2018)
   PUBMED   30228264
  REMARK    GeneRIF: Study shows that human hair follicles (HF) can engage in
            chemosensation and that the specific activation of OR2AT4 is
            required to sustain HF growth.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Busse,D., Kudella,P., Gruning,N.M., Gisselmann,G., Stander,S.,
            Luger,T., Jacobsen,F., Steinstrasser,L., Paus,R., Gkogkolou,P.,
            Bohm,M., Hatt,H. and Benecke,H.
  TITLE     A synthetic sandalwood odorant induces wound-healing processes in
            human keratinocytes via the olfactory receptor OR2AT4
  JOURNAL   J Invest Dermatol 134 (11), 2823-2832 (2014)
   PUBMED   24999593
  REMARK    GeneRIF: OR2AT4 is involved in human keratinocyte
            re-epithelialization during wound-healing processes
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Malnic,B., Godfrey,P.A. and Buck,L.B.
  TITLE     The human olfactory receptor gene family
  JOURNAL   Proc Natl Acad Sci U S A 101 (8), 2584-2589 (2004)
   PUBMED   14983052
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 May 4;101(18):7205]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001972.4 and AP003175.2.
            
            On May 8, 2019 this sequence version replaced XP_016873144.1.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.65986.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMN03267769
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..320
                     /product="olfactory receptor 2AT4 isoform 1"
                     /note="olfactory receptor OR11-265 pseudogene; olfactory
                     receptor 2AT4"
                     /calculated_mol_wt=35372
     Site            7
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A6NND4.1)"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NND4.1)"
     Region          45..299
                     /region_name="7tmA_OR"
                     /note="olfactory receptors, member of the class A family
                     of seven-transmembrane G protein-coupled receptors;
                     cd13954"
                     /db_xref="CDD:320092"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NND4.1)"
     Region          64..90
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320092"
     Site            order(86,89..90,102..107,109..110,113,158,160..164,200,
                     203..205,207..209,211..212,257,260..261,263..264,267,
                     273..274,276..278,281,284..285)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320092"
     Region          102..132
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320092"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NND4.1)"
     Site            146..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NND4.1)"
     Region          146..164
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320092"
     Region          200..230
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320092"
     Site            201..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NND4.1)"
     Region          237..267
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320092"
     Site            246..266
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NND4.1)"
     Region          274..299
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320092"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NND4.1)"
     CDS             1..320
                     /gene="OR2AT4"
                     /gene_synonym="OR11-265"
                     /coded_by="NM_001005285.2:719..1681"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31639.1"
                     /db_xref="GeneID:341152"
                     /db_xref="HGNC:HGNC:19620"
ORIGIN      
        1 mdatacnesv dgspvfyllg ipslpetffl pvffifllfy llilmgnali lvavvaepsl
       61 hkpmyfflin lstldilftt ttvpkmlslf llgdrflsfs scllqmylfq sftcseafil
      121 vvmaydryva ichplhypvl mnpqtnatla asawltalll pipavvrtsq maynsiayiy
      181 hcfcdhlavv qascsdttpq tlmgfciamv vsflplllvl lsyvhilasv lrisslegra
      241 kafstcsshl lvvgtyyssi aiayvayrad lpldfhimgn vvyailtpil npliytlrnr
      301 dvkaaitkim sqdpgcdrsi
//
LOCUS       NP_009165                186 aa            linear   PRI 27-APR-2025
DEFINITION  dynactin subunit 3 isoform 1 [Homo sapiens].
ACCESSION   NP_009165
VERSION     NP_009165.1
DBSOURCE    REFSEQ: accession NM_007234.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Su,X., Li,H., Chen,S. and Qin,C.
  TITLE     Study on the Prognostic Values of Dynactin Genes in Low-Grade
            Glioma
  JOURNAL   Technol Cancer Res Treat 20, 15330338211010143 (2021)
   PUBMED   33896271
  REMARK    GeneRIF: Study on the Prognostic Values of Dynactin Genes in
            Low-Grade Glioma.
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Kuzma-Kozakiewicz,M., Kazmierczak,B., Chudy,A., Gajewska,B. and
            Baranczyk-Kuzma,A.
  TITLE     Alteration of Motor Protein Expression Involved in Bidirectional
            Transport in Peripheral Blood Mononuclear Cells of Patients with
            Amyotrophic Lateral Sclerosis
  JOURNAL   Neurodegener Dis 16 (3-4), 235-244 (2016)
   PUBMED   26954557
  REMARK    GeneRIF: Study found that in peripheral blood mononuclear cells the
            median expression of KIFC3, KIF1B, and KIF5C was much lower than
            the expression of dynactin subunits DCTN1 and DCTN3, in both
            sporadic amyotrophic lateral sclerosis and healthy cases
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Mills,D.R. and Jackson,C.L.
  TITLE     Assignment of p22 dynactin light chain (DCTN3) to human chromosome
            region 9p13 by radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 92 (1-2), 166 (2001)
   PUBMED   11306820
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Karki,S., Tokito,M.K. and Holzbaur,E.L.
  TITLE     A dynactin subunit with a highly conserved cysteine-rich motif
            interacts directly with Arp1
  JOURNAL   J Biol Chem 275 (7), 4834-4839 (2000)
   PUBMED   10671518
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Karki,S., LaMonte,B. and Holzbaur,E.L.
  TITLE     Characterization of the p22 subunit of dynactin reveals the
            localization of cytoplasmic dynein and dynactin to the midbody of
            dividing cells
  JOURNAL   J Cell Biol 142 (4), 1023-1034 (1998)
   PUBMED   9722614
  REMARK    Erratum:[J Cell Biol 1998 Oct 19;143(2):following 560]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA212054.1, BC107697.1 and
            CN257020.1.
            
            Summary: This gene encodes the smallest subunit of dynactin, a
            macromolecular complex consisting of 10 subunits ranging in size
            from 22 to 150 kD. Dynactin binds to both microtubules and
            cytoplasmic dynein. It is involved in a diverse array of cellular
            functions, including ER-to-Golgi transport, the centripetal
            movement of lysosomes and endosomes, spindle formation,
            cytokinesis, chromosome movement, nuclear positioning, and
            axonogenesis. This subunit, like most other dynactin subunits,
            exists only as a part of the dynactin complex. It is primarily an
            alpha-helical protein with very little coiled coil, and binds
            directly to the largest subunit (p150) of dynactin. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.555144.1,
                                           SRR5189661.24228.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259632.12/ ENSP00000259632.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..186
                     /product="dynactin subunit 3 isoform 1"
                     /note="dynactin light chain; dynactin complex subunit 22
                     kDa subunit; dynactin 3 (p22)"
                     /calculated_mol_wt=20988
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O75935.1)"
     Region          10..170
                     /region_name="Dynactin_p22"
                     /note="Dynactin subunit p22; pfam07426"
                     /db_xref="CDD:462162"
     CDS             1..186
                     /gene="DCTN3"
                     /gene_synonym="DCTN-22; DCTN22"
                     /coded_by="NM_007234.5:32..592"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6560.1"
                     /db_xref="GeneID:11258"
                     /db_xref="HGNC:HGNC:2713"
                     /db_xref="MIM:607387"
ORIGIN      
        1 magltdlqrl qarveelerw vygpggargs rkvadglvkv qvalgnissk rervkilykk
       61 iedlikyldp eyidriaipd asklqfilae eqfilsqval leqvnalvpm ldsahikavp
      121 ehaarlqrla qihiqqqdqc veiteeskal leeynkttml lskqfvqwde llcqleaatq
      181 vkpaee
//
LOCUS       NP_001355612            1012 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein 26 isoform 1 [Mus musculus].
ACCESSION   NP_001355612
VERSION     NP_001355612.1
DBSOURCE    REFSEQ: accession NM_001368683.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Kogo,H., Kowa-Sugiyama,H., Yamada,K., Bolor,H., Tsutsumi,M.,
            Ohye,T., Inagaki,H., Taniguchi,M., Toda,T. and Kurahashi,H.
  TITLE     Screening of genes involved in chromosome segregation during
            meiosis I: toward the identification of genes responsible for
            infertility in humans
  JOURNAL   J Hum Genet 55 (5), 293-299 (2010)
   PUBMED   20339383
REFERENCE   4  (residues 1 to 1012)
  AUTHORS   Guo,G., Huss,M., Tong,G.Q., Wang,C., Li Sun,L., Clarke,N.D. and
            Robson,P.
  TITLE     Resolution of cell fate decisions revealed by single-cell gene
            expression analysis from zygote to blastocyst
  JOURNAL   Dev Cell 18 (4), 675-685 (2010)
   PUBMED   20412781
REFERENCE   5  (residues 1 to 1012)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   6  (residues 1 to 1012)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1012)
  AUTHORS   Peterson,K.A., King,B.L., Hagge-Greenberg,A., Roix,J.J., Bult,C.J.
            and O'Brien,T.P.
  TITLE     Functional and comparative genomic analysis of the piebald deletion
            region of mouse chromosome 14
  JOURNAL   Genomics 80 (2), 172-184 (2002)
   PUBMED   12160731
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113125.8 and AC146601.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 55.36 cM"
     Protein         1..1012
                     /product="RNA-binding protein 26 isoform 1"
                     /note="RNA-binding protein 26; cutaneous T-cell lymphoma
                     tumor antigen se70-2; protein expressed in male leptotene
                     and zygotene spermatocytes 393"
                     /calculated_mol_wt=114012
     Region          11..76
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          106..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          <294..314
                     /region_name="ZnF_C3H1"
                     /note="zinc finger; smart00356"
                     /db_xref="CDD:214632"
     Region          334..404
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          465..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T8P6; propagated from
                     UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Site            515
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T8P6; propagated from
                     UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          536..611
                     /region_name="RRM1_RBM26"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     RNA-binding protein 26 (RBM26); cd12516"
                     /db_xref="CDD:409938"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          647..667
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          <725..>846
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Region          858..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          891..962
                     /region_name="RRM2_RBM26_like"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     RNA-binding protein 26 (RBM26) and similar proteins;
                     cd12258"
                     /db_xref="CDD:409703"
     Region          970..1012
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     CDS             1..1012
                     /gene="Rbm26"
                     /gene_synonym="1700009P03Rik; C230097K14Rik; MLZ-393;
                     Pro1777; Se70-2"
                     /coded_by="NM_001368683.1:463..3501"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:74213"
                     /db_xref="MGI:MGI:1921463"
ORIGIN      
        1 mvskmiienf ealkswlskt lepicdadps alakyvlalv kkdksekelk alcidqldvf
       61 lqketqifve klfdavntks ylpppeqpss gslkvdflqh qekdikkeel tkeeerekkf
      121 srrlnhsppq sssryrdnrs rderkkddrs rkrdydrnpp rrdsyrdryn rrrgrsrsys
      181 rsrsrswske rlrdrdrdrs rtrsrsrtrs rerdlvkpky dldrtdplen nytpvssvsn
      241 issghypvpt lsstitviap thhgnnttes wsefhedqvd hnsyvrppmp kkrcrdydek
      301 gfcmrgdmcp fdhgsdpvvv edvnlpgmlp fpaqppvveg ppppglpppp piltpppvnl
      361 rppvpppgpl ppslppvtgp ppplpplqps gmdappnsat ssvptvvttg ihhqpppapp
      421 slftavfvlp dtydtdgynp eapsitntsr pmyrhrvhaq rpnligltsg dmdlpprekp
      481 pnkssmrivv dsesrkrtig sgepgvstkk twfdkpnfnr tnspgfqkkv qfgnentkle
      541 lrkvppelnn isklnehfsr fgtlvnlqva yngdpegali qfatyeeakk aissteavln
      601 nrfikvywhr egttqqlqtt spkviqplvq qpilpvvkqs vkerlgpvps attepaeaqs
      661 atselpqnvt klsvkdrlgf vskpsvsate kvlststglt ktvynpaalk aaqktlsvst
      721 pavdnneaqk kkqealklqq dvrkrkqeil ekhietqkml iskleknktm ksedkaeimk
      781 tleiltknit klkdevksts pgrclpksik tktqmqkell dteldlykkm qageevtelr
      841 rkytelqlea akrgilssgr grgihtrgrg tahgrgrgrg rgrgvpghav vdhrpralei
      901 saftesdred llphfaqyge iedcqiddas lhaiitfktr aeaeaaaihg arfkgqdlkl
      961 awnkpianms avdteeaepd eeefqeeslv ddsllqddde eeednesrsw rr
//
LOCUS       NP_068575                162 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-21 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_068575
VERSION     NP_068575.1
DBSOURCE    REFSEQ: accession NM_021803.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Shufang,M., Xiaojiao,H. and Yinhong,K.
  TITLE     Pro-inflammatory cytokine IL-21 correlates with the reactive oxygen
            species and 25-hydroxy vitamin D in rheumatoid arthritis patients
  JOURNAL   Immun Inflamm Dis 12 (7), e1308 (2024)
   PUBMED   39056553
  REMARK    GeneRIF: Pro-inflammatory cytokine IL-21 correlates with the
            reactive oxygen species and 25-hydroxy vitamin D in rheumatoid
            arthritis patients.
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Isvoranu,G. and Chiritoiu-Butnaru,M.
  TITLE     Therapeutic potential of interleukin-21 in cancer
  JOURNAL   Front Immunol 15, 1369743 (2024)
   PUBMED   38638431
  REMARK    GeneRIF: Therapeutic potential of interleukin-21 in cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Shbeer,A.M. and Ahmed Robadi,I.
  TITLE     The role of Interleukin-21 in autoimmune Diseases: Mechanisms,
            therapeutic Implications, and future directions
  JOURNAL   Cytokine 173, 156437 (2024)
   PUBMED   37972478
  REMARK    GeneRIF: The role of Interleukin-21 in autoimmune Diseases:
            Mechanisms, therapeutic Implications, and future directions.
            Review article
REFERENCE   4  (residues 1 to 162)
  AUTHORS   Cai,Y., Ji,H., Zhou,X., Zhao,K., Zhang,X., Pan,L. and Shi,R.
  TITLE     Interleukin-21 modulates balance between regulatory T cells and
            T-helper 17 cells in chronic hepatitis B virus infection
  JOURNAL   BMC Infect Dis 23 (1), 719 (2023)
   PUBMED   37875903
  REMARK    GeneRIF: Interleukin-21 modulates balance between regulatory T
            cells and T-helper 17 cells in chronic hepatitis B virus infection.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 162)
  AUTHORS   Yi,J.S., Cox,M.A. and Zajac,A.J.
  TITLE     Interleukin-21: a multifunctional regulator of immunity to
            infections
  JOURNAL   Microbes Infect 12 (14-15), 1111-1119 (2010)
   PUBMED   20817119
  REMARK    Review article
REFERENCE   6  (residues 1 to 162)
  AUTHORS   Strengell,M., Sareneva,T., Foster,D., Julkunen,I. and Matikainen,S.
  TITLE     IL-21 up-regulates the expression of genes associated with innate
            immunity and Th1 response
  JOURNAL   J Immunol 169 (7), 3600-3605 (2002)
   PUBMED   12244150
  REMARK    GeneRIF: IL-21 rapidly induces mRNA synthesis for IFN-gamma, T-bet,
            IL-2 receptor alpha, IL-12 receptor beta 2, IL-18 receptor, and
            myeloid differentiation factor 88, the genes that are important in
            activating innate immunity and Th1 response in NK and T cells.
REFERENCE   7  (residues 1 to 162)
  AUTHORS   Asao,H., Okuyama,C., Kumaki,S., Ishii,N., Tsuchiya,S., Foster,D.
            and Sugamura,K.
  TITLE     Cutting edge: the common gamma-chain is an indispensable subunit of
            the IL-21 receptor complex
  JOURNAL   J Immunol 167 (1), 1-5 (2001)
   PUBMED   11418623
REFERENCE   8  (residues 1 to 162)
  AUTHORS   Vosshenrich,C.A. and Di Santo,J.P.
  TITLE     Cytokines: IL-21 joins the gamma(c)-dependent network?
  JOURNAL   Curr Biol 11 (5), R175-R177 (2001)
   PUBMED   11267886
REFERENCE   9  (residues 1 to 162)
  AUTHORS   Parrish-Novak,J., Dillon,S.R., Nelson,A., Hammond,A., Sprecher,C.,
            Gross,J.A., Johnston,J., Madden,K., Xu,W., West,J., Schrader,S.,
            Burkhead,S., Heipel,M., Brandt,C., Kuijper,J.L., Kramer,J.,
            Conklin,D., Presnell,S.R., Berry,J., Shiota,F., Bort,S., Hambly,K.,
            Mudri,S., Clegg,C., Moore,M., Grant,F.J., Lofton-Day,C.,
            Gilbert,T., Rayond,F., Ching,A., Yao,L., Smith,D., Webster,P.,
            Whitmore,T., Maurer,M., Kaushansky,K., Holly,R.D. and Foster,D.
  TITLE     Interleukin 21 and its receptor are involved in NK cell expansion
            and regulation of lymphocyte function
  JOURNAL   Nature 408 (6808), 57-63 (2000)
   PUBMED   11081504
REFERENCE   10 (residues 1 to 162)
  AUTHORS   Flores,I., Casaseca,T., Martinez-A,C., Kanoh,H. and Merida,I.
  TITLE     Phosphatidic acid generation through interleukin 2 (IL-2)-induced
            alpha-diacylglycerol kinase activation is an essential step in
            IL-2-mediated lymphocyte proliferation
  JOURNAL   J Biol Chem 271 (17), 10334-10340 (1996)
   PUBMED   8626603
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC053545.5, AF254069.1,
            BC069124.1 and LC133256.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the common-gamma chain
            family of cytokines with immunoregulatory activity. The encoded
            protein plays a role in both the innate and adaptive immune
            responses by inducing the differentiation, proliferation and
            activity of multiple target cells including macrophages, natural
            killer cells, B cells and cytotoxic T cells. Dysregulation of this
            gene plays a role in multiple immune-mediated diseases including
            lupus, psoriasis and chronic inflammatory diseases. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: LC133256.1, BC069124.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000648588.1/ ENSP00000497915.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q27"
     Protein         1..162
                     /product="interleukin-21 isoform 1 precursor"
                     /calculated_mol_wt=15464
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3207
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBE4.3)"
     Region          105..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBE4.3)"
     CDS             1..162
                     /gene="IL21"
                     /gene_synonym="CVID11; IL-21; Za11"
                     /coded_by="NM_021803.4:56..544"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3727.1"
                     /db_xref="GeneID:59067"
                     /db_xref="HGNC:HGNC:6005"
                     /db_xref="MIM:605384"
ORIGIN      
        1 mrsspgnmer iviclmvifl gtlvhksssq gqdrhmirmr qlidivdqlk nyvndlvpef
       61 lpapedvetn cewsafscfq kaqlksantg nneriinvsi kklkrkppst nagrrqkhrl
      121 tcpscdsyek kppkeflerf ksllqkmihq hlssrthgse ds
//
LOCUS       NP_001356239             496 aa            linear   ROD 27-APR-2025
DEFINITION  serine/arginine-rich splicing factor 4 isoform a [Mus musculus].
ACCESSION   NP_001356239
VERSION     NP_001356239.1
DBSOURCE    REFSEQ: accession NM_001369310.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Larrasa-Alonso,J., Villalba-Orero,M., Marti-Gomez,C.,
            Ortiz-Sanchez,P., Lopez-Olaneta,M.M., Rey-Martin,M.A.,
            Sanchez-Cabo,F., McNicoll,F., Muller-McNicoll,M., Garcia-Pavia,P.
            and Lara-Pezzi,E.
  TITLE     The SRSF4-GAS5-Glucocorticoid Receptor Axis Regulates Ventricular
            Hypertrophy
  JOURNAL   Circ Res 129 (6), 669-683 (2021)
   PUBMED   34333993
  REMARK    GeneRIF: The SRSF4-GAS5-Glucocorticoid Receptor Axis Regulates
            Ventricular Hypertrophy.
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Guo,H., Li,Y., Luo,M., Lin,S., Chen,J., Ma,Q., Gu,Y., Jiang,Z. and
            Gui,Y.
  TITLE     Androgen receptor binding to an androgen-responsive element in the
            promoter of the Srsf4 gene inhibits its expression in mouse Sertoli
            cells
  JOURNAL   Mol Reprod Dev 82 (12), 976-985 (2015)
   PUBMED   26308373
  REMARK    GeneRIF: these results demonstrate that Srsf4 is a direct
            downstream target of the androgen receptor in mouse Sertoli cells.
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Manley,J.L. and Krainer,A.R.
  TITLE     A rational nomenclature for serine/arginine-rich protein splicing
            factors (SR proteins)
  JOURNAL   Genes Dev 24 (11), 1073-1074 (2010)
   PUBMED   20516191
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Guo,Y., Zhang,X., Huang,J., Zeng,Y., Liu,W., Geng,C., Li,K.W.,
            Yang,D., Wu,S., Wei,H., Han,Z., Qian,X., Jiang,Y. and He,F.
  TITLE     Relationships between hematopoiesis and hepatogenesis in the
            midtrimester fetal liver characterized by dynamic transcriptomic
            and proteomic profiles
  JOURNAL   PLoS One 4 (10), e7641 (2009)
   PUBMED   19865483
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Yomoda,J., Muraki,M., Kataoka,N., Hosoya,T., Suzuki,M., Hagiwara,M.
            and Kimura,H.
  TITLE     Combination of Clk family kinase and SRp75 modulates alternative
            splicing of Adenovirus E1A
  JOURNAL   Genes Cells 13 (3), 233-244 (2008)
   PUBMED   18298798
REFERENCE   9  (residues 1 to 496)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607088.26.
            
            Summary: The protein encoded by this gene is a member of the
            serine/arginine (SR)-rich family of pre-mRNA splicing factors,
            which constitute part of the spliceosome. Each of these factors
            contains an RNA recognition motif (RRM) for binding RNA and an RS
            domain for binding other proteins. The RS domain is rich in serine
            and arginine residues and facilitates interaction between different
            SR splicing factors. In addition to being critical for mRNA
            splicing, the SR proteins have also been shown to be involved in
            mRNA export from the nucleus and in translation. [provided by
            RefSeq, Sep 2010].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1-4 all encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.1872865.1,
                                           SRR11927932.3747209.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 64.53 cM"
     Protein         1..496
                     /product="serine/arginine-rich splicing factor 4 isoform
                     a"
                     /note="splicing factor, arginine/serine-rich 4 (SRp75);
                     serine/arginine-rich splicing factor 4"
                     /calculated_mol_wt=56325
     Region          <42..92
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          109..180
                     /region_name="RRM2_SRSF4_like"
                     /note="RNA recognition motif 2 (RRM2) found in
                     serine/arginine-rich splicing factor 4 (SRSF4) and similar
                     proteins; cd12600"
                     /db_xref="CDD:410012"
     Region          250..>361
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     CDS             1..496
                     /gene="Srsf4"
                     /gene_synonym="5730499P16Rik; MNCb-2616; Sfrs4; SRp75"
                     /coded_by="NM_001369310.1:702..2192"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:57317"
                     /db_xref="MGI:MGI:1890577"
ORIGIN      
        1 msecgngsph weskthillv laedshvhiq rkacgtvvgq rygfvefddl rdaddavyel
       61 ngkdlcgerv ivehargprr dgsygsgrsg ygyrrsgrdk ygpptrteyr livenlssrc
      121 swqdlkdymr qagevtyada hkgrknegvi efvsysdmkr alekldgtev ngrkirlved
      181 kpgsrrrrsy srsrshsrsr srsrhsrksr srsgsskssh sksrsrsrsg shsrsksrsr
      241 sqsrsrskke ksrspskdnk srsrsrspdk srskskdhae dklqnndsag kakshspsrh
      301 dsksrsrsqe rraeeerrrs vsrarsqeks rsqeksllks rsrsrskvgs rsrsrskdkr
      361 kgrkrsrdes rsrsrskser srkhsskrds kvssssskkk kdtdhsrsps rsvskereha
      421 kaesgqresr aegeseapnp eprarsrsts kskpnvpaes rsrsksaskt rsrskspsrs
      481 asrspsrsrs rshsrs
//
LOCUS       NP_997719                291 aa            linear   PRI 27-APR-2025
DEFINITION  EEF1A lysine methyltransferase 2 isoform 1 [Homo sapiens].
ACCESSION   NP_997719
VERSION     NP_997719.2
DBSOURCE    REFSEQ: accession NM_212554.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Shimazu,T., Barjau,J., Sohtome,Y., Sodeoka,M. and Shinkai,Y.
  TITLE     Selenium-based S-adenosylmethionine analog reveals the mammalian
            seven-beta-strand methyltransferase METTL10 to be an EF1A1 lysine
            methyltransferase
  JOURNAL   PLoS One 9 (8), e105394 (2014)
   PUBMED   25144183
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY048148.1, BC026167.1, AL832292.1, AK022354.1, AC068896.9 and
            AA776892.1.
            
            On Jan 26, 2005 this sequence version replaced NP_997719.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026167.1, SRR1803615.272093.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467150 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368836.7/ ENSP00000357829.2
            RefSeq Select criteria :: based on longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..291
                     /product="EEF1A lysine methyltransferase 2 isoform 1"
                     /note="methyltransferase-like protein 10; protein-lysine
                     N-methyltransferase METTL10; methyltransferase like 10;
                     eukaryotic translation elongation factor 1 alpha lysine
                     methyltransferase 2"
                     /calculated_mol_wt=31699
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JPI9.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q5JPI9.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5JPI9.3)"
     Region          80..219
                     /region_name="Methyltransf_31"
                     /note="Methyltransferase domain; pfam13847"
                     /db_xref="CDD:463998"
     CDS             1..291
                     /gene="EEF1AKMT2"
                     /gene_synonym="C10orf138; Efm4; METTL10"
                     /coded_by="NM_212554.4:55..930"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31307.1"
                     /db_xref="GeneID:399818"
                     /db_xref="HGNC:HGNC:33787"
                     /db_xref="MIM:617794"
ORIGIN      
        1 mssgadgggg aavaarsdkg spgedgfvps algtrehwda vyerelqtfr eygdtgeiwf
       61 geesmnrlir wmqkhkipld asvldigtgn gvflvelakf gfsnitgidy spsaiqlsgs
      121 iiekeglsni klkvedflnl stqlsgfhic idkgtfdais lnpdnaiekr kqyvkslsrv
      181 lkvkgfflit scnwtkeell nefsegwstv agfwltaalt swaqaifsts asrvggttgt
      241 hhhawiifvf laetrfchvv qaglellgss dsptwppkvl glyharpsla f
//
LOCUS       NP_065387               1005 aa            linear   PRI 27-APR-2025
DEFINITION  ephrin type-A receptor 8 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_065387
VERSION     NP_065387.1
DBSOURCE    REFSEQ: accession NM_020526.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Wang,G.H., Ni,K., Gu,C., Huang,J., Chen,J., Wang,X.D. and Ni,Q.
  TITLE     EphA8 inhibits cell apoptosis via AKT signaling and is associated
            with poor prognosis in breast cancer
  JOURNAL   Oncol Rep 46 (2) (2021)
   PUBMED   34278497
  REMARK    GeneRIF: EphA8 inhibits cell apoptosis via AKT signaling and is
            associated with poor prognosis in breast cancer.
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Wang,Y., Zhou,N., Li,P., Wu,H., Wang,Q., Gao,X., Wang,X. and
            Huang,J.
  TITLE     EphA8 acts as an oncogene and contributes to poor prognosis in
            gastric cancer via regulation of ADAM10
  JOURNAL   J Cell Physiol 234 (11), 20408-20419 (2019)
   PUBMED   31026069
  REMARK    GeneRIF: EphA8 knockdown also decreased expression of the protease
            ADAM10
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Liu,L., Wang,X. and Ge,W.
  TITLE     EphA8 is a Prognostic Factor for Oral Tongue Squamous Cell
            Carcinoma
  JOURNAL   Med Sci Monit 24, 7213-7222 (2018)
   PUBMED   30300334
  REMARK    GeneRIF: Q-PCR and IHC staining revealed that EphA8 was highly
            expressed in OTSCC tissues, especially in advanced stage OTSCC
            tissues. Kaplan-Meier curve showed that high EphA8 expression was
            significantly associated with poor prognosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1005)
  AUTHORS   Apellaniz-Ruiz,M., Tejero,H., Inglada-Perez,L., Sanchez-Barroso,L.,
            Gutierrez-Gutierrez,G., Calvo,I., Castelo,B., Redondo,A.,
            Garcia-Donas,J., Romero-Laorden,N., Sereno,M., Merino,M.,
            Curras-Freixes,M., Montero-Conde,C., Mancikova,V.,
            Avall-Lundqvist,E., Green,H., Al-Shahrour,F., Cascon,A., Robledo,M.
            and Rodriguez-Antona,C.
  TITLE     Targeted Sequencing Reveals Low-Frequency Variants in EPHA Genes as
            Markers of Paclitaxel-Induced Peripheral Neuropathy
  JOURNAL   Clin Cancer Res 23 (5), 1227-1235 (2017)
   PUBMED   27582484
  REMARK    GeneRIF: Gene-based analysis identified EPHA6 as the gene most
            significantly associated with paclitaxel-induced neuropathy...This
            first study sequencing EPHA genes revealed that low-frequency
            variants in EPHA6, EPHA5, and EPHA8 contribute to the
            susceptibility to paclitaxel-induced neuropathy
REFERENCE   5  (residues 1 to 1005)
  AUTHORS   Liu,X., Xu,Y., Jin,Q., Wang,W., Zhang,S., Wang,X., Zhang,Y., Xu,X.
            and Huang,J.
  TITLE     EphA8 is a prognostic marker for epithelial ovarian cancer
  JOURNAL   Oncotarget 7 (15), 20801-20809 (2016)
   PUBMED   26989075
  REMARK    GeneRIF: High EPHA8 expression is associated with epithelial
            ovarian cancer.
REFERENCE   6  (residues 1 to 1005)
  AUTHORS   .
  TITLE     Unified nomenclature for Eph family receptors and their ligands,
            the ephrins. Eph Nomenclature Committee
  JOURNAL   Cell 90 (3), 403-404 (1997)
   PUBMED   9267020
REFERENCE   7  (residues 1 to 1005)
  AUTHORS   Park,S., Frisen,J. and Barbacid,M.
  TITLE     Aberrant axonal projections in mice lacking EphA8 (Eek) tyrosine
            protein kinase receptors
  JOURNAL   EMBO J 16 (11), 3106-3114 (1997)
   PUBMED   9214628
REFERENCE   8  (residues 1 to 1005)
  AUTHORS   Park,S. and Sanchez,M.P.
  TITLE     The Eek receptor, a member of the Eph family of tyrosine protein
            kinases, can be activated by three different Eph family ligands
  JOURNAL   Oncogene 14 (5), 533-542 (1997)
   PUBMED   9053851
REFERENCE   9  (residues 1 to 1005)
  AUTHORS   Lemke,G.
  TITLE     A coherent nomenclature for Eph receptors and their ligands
  JOURNAL   Mol Cell Neurosci 9 (5-6), 331-332 (1997)
   PUBMED   9361271
REFERENCE   10 (residues 1 to 1005)
  AUTHORS   Chan,J. and Watt,V.M.
  TITLE     eek and erk, new members of the eph subclass of receptor
            protein-tyrosine kinases
  JOURNAL   Oncogene 6 (6), 1057-1061 (1991)
   PUBMED   1648701
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL035703.21, DR007053.1,
            BC072417.1 and AB040892.1.
            
            Summary: This gene encodes a member of the ephrin receptor
            subfamily of the protein-tyrosine kinase family. EPH and
            EPH-related receptors have been implicated in mediating
            developmental events, particularly in the nervous system. Receptors
            in the EPH subfamily typically have a single kinase domain and an
            extracellular region containing a Cys-rich domain and 2 fibronectin
            type III repeats. The ephrin receptors are divided into 2 groups
            based on the similarity of their extracellular domain sequences and
            their affinities for binding ephrin-A and ephrin-B ligands. The
            protein encoded by this gene functions as a receptor for ephrin A2,
            A3 and A5 and plays a role in short-range contact-mediated axonal
            guidance during development of the mammalian nervous system.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2158188
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000166244.8/ ENSP00000166244.3
            RefSeq Select criteria    :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1005
                     /product="ephrin type-A receptor 8 isoform 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="protein-tyrosine kinase; hydroxyaryl-protein
                     kinase; tyrosylprotein kinase; ephrin type-A receptor 8;
                     tyrosine-protein kinase receptor EEK; EPH- and ELK-related
                     tyrosine kinase; EPH-like kinase 3; EPH- and ELK-related
                     kinase"
                     /calculated_mol_wt=108398
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2623
     mat_peptide     28..1005
                     /product="Ephrin type-A receptor 8. /id=PRO_0000016822"
                     /note="propagated from UniProtKB/Swiss-Prot (P29322.2)"
                     /calculated_mol_wt=108398
     Region          31..203
                     /region_name="EphR_LBD"
                     /note="Ligand Binding Domain of Ephrin Receptors; cl02704"
                     /db_xref="CDD:470656"
     Site            order(43,55..58,60..61,66,68,71,104,106,154,162..164,
                     191..193,195)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198439"
     Region          <326..>519
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29322.2)"
     Site            407
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29322.2)"
     Site            432
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29322.2)"
     Region          439..524
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(440,504,519)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(520..521,523..524)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            543..563
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29322.2)"
     Region          <562..632
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          564..570
                     /region_name="Mediates interaction with ANKS1A and ANKS1B.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P29322.2)"
     Region          589..644
                     /region_name="Mediates interaction with PIK3CG and
                     required for endocytosis. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P29322.2)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O09127; propagated from
                     UniProtKB/Swiss-Prot (P29322.2)"
     Region          630..896
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(641,643..645,649,665,667,713..714,716,760,764..765,
                     767,778,797..801,810,844)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(641..645,649,665,667,713..716,719..720,764..765,767,
                     778)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            order(760,764,797..801,810,844)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            777..803
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Site            839
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O09127; propagated from
                     UniProtKB/Swiss-Prot (P29322.2)"
     Region          933..995
                     /region_name="SAM_EPH-A8"
                     /note="SAM domain of EPH-A8 subfamily of tyrosine kinase
                     receptors; cd09550"
                     /db_xref="CDD:188949"
     Site            order(947,980)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188949"
     Region          1003..1005
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P29322.2)"
     CDS             1..1005
                     /gene="EPHA8"
                     /gene_synonym="EEK; EK3; HEK3"
                     /coded_by="NM_020526.5:148..3165"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS225.1"
                     /db_xref="GeneID:2046"
                     /db_xref="HGNC:HGNC:3391"
                     /db_xref="MIM:176945"
ORIGIN      
        1 mapargrlpp alwvvtaaaa aatcvsaarg evnlldtsti hgdwgwltyp ahgwdsinev
       61 desfqpihty qvcnvmspnq nnwlrtswvp rdgarrvyae ikftlrdcns mpgvlgtcke
      121 tfnlyylesd rdlgastqes qflkidtiaa desftgadlg vrrlklntev rsvgplskrg
      181 fylafqdiga clailslriy ykkcpamvrn laafseavtg adssslvevr gqcvrhseer
      241 dtpkmycsae gewlvpigkc vcsagyeerr dacvacelgf yksapgdqlc arcpphshsa
      301 apaaqachcd lsyyraaldp pssactrpps apvnlissvn gtsvtlewap pldpggrsdi
      361 tynavcrrcp walsrceacg sgtrfvpqqt slvqasllva nllahmnysf wieavngvsd
      421 lspeprraav vnittnqaap sqvvvirqer agqtsvsllw qepeqpngii leyeikyyek
      481 dkemqsystl kavttratvs glkpgtryvf qvrartsagc grfsqameve tgkprprydt
      541 rtivwicltl itglvvllll lickkrhcgy skafqdsdee kmhyqngqap ppvflplhhp
      601 pgklpepqfy aephtyeepg ragrsftrei easrihieki igsgdsgevc ygrlrvpgqr
      661 dvpvaikalk agyterqrrd flseasimgq fdhpniirle gvvtrgrlam ivteymengs
      721 ldtflrthdg qftimqlvgm lrgvgagmry lsdlgyvhrd laarnvlvds nlvckvsdfg
      781 lsrvleddpd aaytttggki pirwtapeai afrtfssasd vwsfgvvmwe vlaygerpyw
      841 nmtnrdviss veegyrlpap mgcphalhql mldcwhkdra qrprfsqivs vldalirspe
      901 slratatvsr cpppafvrsc fdlrggsggg ggltvgdwld sirmgryrdh faaggysslg
      961 mvlrmnaqdv ralgitlmgh qkkilgsiqt mraqltstqg prrhl
//
LOCUS       NP_001355184             138 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 234 isoform 3 precursor [Mus musculus].
ACCESSION   NP_001355184
VERSION     NP_001355184.1
DBSOURCE    REFSEQ: accession NM_001368255.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Tang,T., Li,L., Tang,J., Li,Y., Lin,W.Y., Martin,F., Grant,D.,
            Solloway,M., Parker,L., Ye,W., Forrest,W., Ghilardi,N., Oravecz,T.,
            Platt,K.A., Rice,D.S., Hansen,G.M., Abuin,A., Eberhart,D.E.,
            Godowski,P., Holt,K.H., Peterson,A., Zambrowicz,B.P. and de
            Sauvage,F.J.
  TITLE     A mouse knockout library for secreted and transmembrane proteins
  JOURNAL   Nat Biotechnol 28 (7), 749-755 (2010)
   PUBMED   20562862
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL671759.10.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY277251.1, BY278522.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 63.26 cM"
     Protein         1..138
                     /product="transmembrane protein 234 isoform 3 precursor"
                     /calculated_mol_wt=12401
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2340
     Site            1..21
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R1E7.1)"
     Region          18..124
                     /region_name="TMEM234"
                     /note="Putative transmembrane family 234; pfam10639"
                     /db_xref="CDD:371174"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R1E7.1)"
     CDS             1..138
                     /gene="Tmem234"
                     /gene_synonym="1500002D11Rik; 2510006D16Rik;
                     4933407D05Rik"
                     /coded_by="NM_001368255.1:37..453"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:76799"
                     /db_xref="MGI:MGI:1924049"
ORIGIN      
        1 maaswgqvla lvlvaalwgg tqpllkrass gleqvrertw awqllqeika lfgnteylmp
       61 fllnqsgsll yyltlastdl tlavpicnsl aivftlivgk vlgediggkv agmvltitgi
      121 tvcitssvsk tqgqpshs
//
LOCUS       NP_000811                678 aa            linear   PRI 27-APR-2025
DEFINITION  growth arrest-specific protein 6 precursor [Homo sapiens].
ACCESSION   NP_000811 XP_947177 XP_950775 XP_950777 XP_950778
VERSION     NP_000811.1
DBSOURCE    REFSEQ: accession NM_000820.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Perez,F., Iribarren,M.L., Olexen,C.M., Ruera,C.N., Errasti,A.E.,
            Guzman,L., Garbi,L., Carrera Silva,E.A. and Chirdo,F.G.
  TITLE     Duodenal mucosa of untreated celiac disease patients has altered
            expression of the GAS6 and PROS1 and the negative regulator
            tyrosine kinase TAM receptors subfamily
  JOURNAL   Clin Immunol 263, 110202 (2024)
   PUBMED   38575045
  REMARK    GeneRIF: Duodenal mucosa of untreated celiac disease patients has
            altered expression of the GAS6 and PROS1 and the negative regulator
            tyrosine kinase TAM receptors subfamily.
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Baskol,G., Yetkin,M.O., Sevim,D.G., Guclu,K., Arda,H.,
            Saracoglu,H., Gahramanov,K. and Evereklioglu,C.
  TITLE     Serum GAS6, sAXL, IL-10, NO, and BCL-2 levels are decreased in
            patients with Behcet's disease
  JOURNAL   Indian J Ophthalmol 72 (Suppl 3), S468-S472 (2024)
   PUBMED   38648454
  REMARK    GeneRIF: Serum GAS6, sAXL, IL-10, NO, and BCL-2 levels are
            decreased in patients with Behcet's disease.
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Hayashi,M., Abe,K., Sugaya,T., Takahata,Y., Fujita,M., Takahashi,A.
            and Ohira,H.
  TITLE     Influence of serum Gas6 levels on prognosis in patients with
            hepatocellular carcinoma
  JOURNAL   Jpn J Clin Oncol 54 (1), 62-69 (2024)
   PUBMED   37801445
  REMARK    GeneRIF: Influence of serum Gas6 levels on prognosis in patients
            with hepatocellular carcinoma.
REFERENCE   4  (residues 1 to 678)
  AUTHORS   Cheng,Y., Yang,X., Wang,Y., Ding,Q., Huang,Y. and Zhang,C.
  TITLE     The role of the Gas6/TAM signal pathway in the LPS-induced
            pulmonary epithelial cells injury
  JOURNAL   Mol Immunol 163, 181-187 (2023)
   PUBMED   37820442
  REMARK    GeneRIF: The role of the Gas6/TAM signal pathway in the LPS-induced
            pulmonary epithelial cells injury.
REFERENCE   5  (residues 1 to 678)
  AUTHORS   Laurance,S., Lemarie,C.A. and Blostein,M.D.
  TITLE     Growth arrest-specific gene 6 (gas6) and vascular hemostasis
  JOURNAL   Adv Nutr 3 (2), 196-203 (2012)
   PUBMED   22516727
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 678)
  AUTHORS   Saccone,S., Marcandalli,P., Gostissa,M., Schneider,C. and Della
            Valle,G.
  TITLE     Assignment of the human GAS6 gene to chromosome 13q34 by
            fluorescence in situ hybridization
  JOURNAL   Genomics 30 (1), 129-131 (1995)
   PUBMED   8595896
REFERENCE   7  (residues 1 to 678)
  AUTHORS   Godowski,P.J., Mark,M.R., Chen,J., Sadick,M.D., Raab,H. and
            Hammonds,R.G.
  TITLE     Reevaluation of the roles of protein S and Gas6 as ligands for the
            receptor tyrosine kinase Rse/Tyro 3
  JOURNAL   Cell 82 (3), 355-358 (1995)
   PUBMED   7634325
REFERENCE   8  (residues 1 to 678)
  AUTHORS   Stitt,T.N., Conn,G., Goret,M., Lai,C., Bruno,J., Radzlejewski,C.,
            Mattsson,K., Fisher,J., Gies,D.R., Jones,P.F., Masiakowski,P.,
            Ryan,T.E., Tobkes,N.J., Chen,D.H., DiStefano,P.S., Long,G.L.,
            Basilico,C., Goldfarb,M.P., Lemke,G., Glass,D.J. and
            Yancopoulos,G.D.
  TITLE     The anticoagulation factor protein S and its relative, Gas6, are
            ligands for the Tyro 3/Axl family of receptor tyrosine kinases
  JOURNAL   Cell 80 (4), 661-670 (1995)
   PUBMED   7867073
REFERENCE   9  (residues 1 to 678)
  AUTHORS   Varnum,B.C., Young,C., Elliott,G., Garcia,A., Bartley,T.D.,
            Fridell,Y.W., Hunt,R.W., Trail,G., Clogston,C., Toso,R.J. et al.
  TITLE     Axl receptor tyrosine kinase stimulated by the vitamin K-dependent
            protein encoded by growth-arrest-specific gene 6
  JOURNAL   Nature 373 (6515), 623-626 (1995)
   PUBMED   7854420
REFERENCE   10 (residues 1 to 678)
  AUTHORS   Manfioletti,G., Brancolini,C., Avanzi,G. and Schneider,C.
  TITLE     The protein encoded by a growth arrest-specific gene (gas6) is a
            new member of the vitamin K-dependent proteins related to protein
            S, a negative coregulator in the blood coagulation cascade
  JOURNAL   Mol Cell Biol 13 (8), 4976-4985 (1993)
   PUBMED   8336730
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY038614.1, BC038984.1 and
            AA045119.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_947177.1, XP_950775.1, XP_950777.1, XP_950778.1.
            
            Summary: This gene encodes a gamma-carboxyglutamic acid
            (Gla)-containing protein thought to be involved in the stimulation
            of cell proliferation. This gene is frequently overexpressed in
            many cancers and has been implicated as an adverse prognostic
            marker. Elevated protein levels are additionally associated with a
            variety of disease states, including venous thromboembolic disease,
            systemic lupus erythematosus, chronic renal failure, and
            preeclampsia. [provided by RefSeq, Aug 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279841.6559.1, BC030708.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327773.7/ ENSP00000331831.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..678
                     /product="growth arrest-specific protein 6 precursor"
                     /note="AXL stimulatory factor; growth arrest-specific
                     protein 6; AXL receptor tyrosine kinase ligand"
                     /calculated_mol_wt=71915
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3029
     Region          53..92
                     /region_name="Gla"
                     /note="Vitamin K-dependent
                     carboxylation/gamma-carboxyglutamic (GLA) domain;
                     pfam00594"
                     /db_xref="CDD:459861"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (Q14393.3)"
     Region          160..195
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          197..>227
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(197,200,214)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          245..277
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          298..450
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Site            420
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16362042; propagated from
                     UniProtKB/Swiss-Prot (Q14393.3)"
     Region          513..644
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63772; propagated from
                     UniProtKB/Swiss-Prot (Q14393.3)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63772; propagated from
                     UniProtKB/Swiss-Prot (Q14393.3)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q63772; propagated from
                     UniProtKB/Swiss-Prot (Q14393.3)"
     CDS             1..678
                     /gene="GAS6"
                     /gene_synonym="AXLLG; AXSF"
                     /coded_by="NM_000820.4:157..2193"
                     /db_xref="CCDS:CCDS45072.1"
                     /db_xref="GeneID:2621"
                     /db_xref="HGNC:HGNC:4168"
                     /db_xref="MIM:600441"
ORIGIN      
        1 mapslspgpa alrrapqlll lllaaecala allpareatq flrprqrraf qvfeeakqgh
       61 lerecveelc sreearevfe ndpetdyfyp ryldcinkyg spytknsgfa tcvqnlpdqc
      121 tpnpcdrkgt qacqdlmgnf fclckagwgg rlcdkdvnec sqenggclqi chnkpgsfhc
      181 schsgfelss dgrtcqdide cadseacgea rcknlpgsys clcdegfays sqekacrdvd
      241 eclqgrceqv cvnspgsytc hcdgrgglkl sqdmdtcedi lpcvpfsvak svkslylgrm
      301 fsgtpvirlr fkrlqptrlv aefdfrtfdp egillfaggh qdstwivlal ragrlelqlr
      361 yngvgrvtss gpvinhgmwq tisveelarn lvikvnrdav mkiavagdlf qperglyhln
      421 ltvggipfhe kdlvqpinpr ldgcmrswnw lngedttiqe tvkvntrmqc fsvtergsfy
      481 pgsgfafysl dymrtpldvg testwevevv ahirpaadtg vlfalwapdl ravplsvalv
      541 dyhstkklkk qlvvlaveht alalmeikvc dgqehvvtvs lrdgeatlev dgtrgqsevs
      601 aaqlqerlav lerhlrspvl tfagglpdvp vtsapvtafy rgcmtlevnr rlldldeaay
      661 khsditahsc ppvepaaa
//
LOCUS       NP_694998                468 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 151A [Homo sapiens].
ACCESSION   NP_694998 XP_943939
VERSION     NP_694998.1
DBSOURCE    REFSEQ: accession NM_153266.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Huang,H.L., Zhang,Q.X., Huang,F., Long,X.Y., Song,Z., Xiao,B.,
            Li,G.L., Ma,C.Y. and Liu,D.
  TITLE     TMEM151A variants associated with paroxysmal kinesigenic dyskinesia
  JOURNAL   Hum Genet 142 (8), 1017-1028 (2023)
   PUBMED   36856871
  REMARK    GeneRIF: TMEM151A variants associated with paroxysmal kinesigenic
            dyskinesia.
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Mounir Alaoui,O., Charbonneau,P.F., Prin,P., Mongin,M., Choquer,M.,
            Damier,P., Riant,F. and Degos,B.
  TITLE     TMEM151A as an alternative to PRRT2 in paroxysmal kinesigenic
            dyskinesia: About three new cases
  JOURNAL   Parkinsonism Relat Disord 108, 105295 (2023)
   PUBMED   36724570
  REMARK    GeneRIF: TMEM151A as an alternative to PRRT2 in paroxysmal
            kinesigenic dyskinesia: About three new cases.
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Chen,Y.L., Chen,D.F., Li,H.F. and Wu,Z.Y.
  TITLE     Features Differ Between Paroxysmal Kinesigenic Dyskinesia Patients
            with PRRT2 and TMEM151A Variants
  JOURNAL   Mov Disord 37 (3), 608-613 (2022)
   PUBMED   35083789
  REMARK    GeneRIF: Features Differ Between Paroxysmal Kinesigenic Dyskinesia
            Patients with PRRT2 and TMEM151A Variants.
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Tian,W.T., Zhan,F.X., Liu,Z.H., Liu,Z., Liu,Q., Guo,X.N.,
            Zhou,Z.W., Wang,S.G., Liu,X.R., Jiang,H., Li,X.H., Zhao,G.H.,
            Li,H.Y., Tang,J.G., Bi,G.H., Zhong,P., Yin,X.M., Liu,T.T., Ni,R.L.,
            Zheng,H.R., Liu,X.L., Qian,X.H., Wu,J.Y., Cao,Y.W., Zhang,C.,
            Liu,S.H., Wu,Y.Y., Wang,Q.F., Xu,T., Hou,W.Z., Li,Z.Y., Ke,H.Y.,
            Zhu,Z.Y., Zheng,L., Wang,T., Rong,T.Y., Wu,L., Zhang,Y., Fang,K.,
            Wang,Z.H., Zhang,Y.K., Zhang,M., Zhao,Y.W., Tang,B.S., Luan,X.H.,
            Huang,X.J. and Cao,L.
  TITLE     TMEM151A Variants Cause Paroxysmal Kinesigenic Dyskinesia: A
            Large-Sample Study
  JOURNAL   Mov Disord 37 (3), 545-552 (2022)
   PUBMED   34820915
  REMARK    GeneRIF: TMEM151A Variants Cause Paroxysmal Kinesigenic Dyskinesia:
            A Large-Sample Study.
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Li,H.F., Chen,Y.L., Zhuang,L., Chen,D.F., Ke,H.Z., Luo,W.J.,
            Liu,G.L., Wu,S.N., Zhou,W.H., Xiong,Z.Q. and Wu,Z.Y.
  TITLE     TMEM151A variants cause paroxysmal kinesigenic dyskinesia
  JOURNAL   Cell Discov 7 (1), 83 (2021)
   PUBMED   34518509
  REMARK    Erratum:[Cell Discov. 2021 Oct 28;7(1):102. doi:
            10.1038/s41421-021-00345-3. PMID: 34711800]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 468)
  CONSRTM   Psychiatric GWAS Consortium Bipolar Disorder Working Group
  TITLE     Large-scale genome-wide association analysis of bipolar disorder
            identifies a new susceptibility locus near ODZ4
  JOURNAL   Nat Genet 43 (10), 977-983 (2011)
   PUBMED   21926972
  REMARK    Erratum:[Nat Genet. 2012 Sep;44(9):1072. Fullerton, Janice M
            [added]; Hyoun, Phil L [corrected to Lee, Phil H]; Meng, Fan Guo
            [corrected to Meng, Fan]]
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001107.5, DB477253.1, BC033898.2, BM727563.1 and BU732410.1.
            
            On Mar 4, 2006 this sequence version replaced XP_943939.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY155283.1, BC033898.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327259.5/ ENSP00000326244.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..468
                     /product="transmembrane protein 151A"
                     /note="transmembrane protein 151"
                     /calculated_mol_wt=51147
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4L1.1)"
     Region          26..423
                     /region_name="TMEM151"
                     /note="TMEM151 family; pfam14857"
                     /db_xref="CDD:464349"
     Site            45..65
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4L1.1)"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4L1.1)"
     Region          384..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4L1.1)"
     CDS             1..468
                     /gene="TMEM151A"
                     /gene_synonym="DYT36; EKD3; TMEM151"
                     /coded_by="NM_153266.4:121..1527"
                     /db_xref="CCDS:CCDS8133.1"
                     /db_xref="GeneID:256472"
                     /db_xref="HGNC:HGNC:28497"
                     /db_xref="MIM:620108"
ORIGIN      
        1 mpedgagdgg evpalipdge plreeqrplk qslgsslcre shwkcllltl lihacgavva
       61 wcrlatvprl vlgpeaalar gaggppptyp aspcsdgyly iplafvslly llylaecwhc
      121 hvrscqaprt dahtvlalir rlqqappcvw wkatsyhyvr rtrqitryrn gdaytttqvy
      181 heradsrtar gefdysahgv rdvskelvgl aehaatrlrf tkcfsfgsae aeasyltqra
      241 rffsanegld dylearegmh lkdvdfresl mvfadprspp wyarawvfwl vsaatlswpl
      301 rvvaaygtah vhyqveklfg asspppgavp sgpplsrvat vdftelewhi csnrqlvpsy
      361 seavvmgags gaylrgcqrc rrsvssnslp parpsgprlp fsrsrlslga ggratpgvfr
      421 slsggplgrr gedteplesp pcyedalyfp vlivhgdsgc qgdgqgal
//
LOCUS       NP_001350006            1241 aa            linear   ROD 27-APR-2025
DEFINITION  cordon-bleu protein-like 1 isoform 4 [Mus musculus].
ACCESSION   NP_001350006
VERSION     NP_001350006.1
DBSOURCE    REFSEQ: accession NM_001363077.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1241)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1241)
  AUTHORS   Lewandowski,J.P., Du,F., Zhang,S., Powell,M.B., Falkenstein,K.N.,
            Ji,H. and Vokes,S.A.
  TITLE     Spatiotemporal regulation of GLI target genes in the mammalian limb
            bud
  JOURNAL   Dev Biol 406 (1), 92-103 (2015)
   PUBMED   26238476
REFERENCE   3  (residues 1 to 1241)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   4  (residues 1 to 1241)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL929132.9, AL935171.9 and AL929129.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK037010.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1241
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 38.35 cM"
     Protein         1..1241
                     /product="cordon-bleu protein-like 1 isoform 4"
                     /note="cordon-bleu protein-like 1; cobl-related 1;
                     cobl-related protein 1"
                     /calculated_mol_wt=133243
     Region          72..138
                     /region_name="RBD"
                     /note="Raf-like Ras-binding domain; pfam02196"
                     /db_xref="CDD:460485"
     Region          156..234
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Region          <873..1144
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1190..1215
                     /region_name="WH2"
                     /note="Wiskott-Aldrich Syndrome Homology (WASP) region 2
                     (WH2 motif), and similar proteins; cl41728"
                     /db_xref="CDD:425359"
     Site            order(1194..1195,1197..1199,1201..1203,1211..1214)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409196"
     CDS             1..1241
                     /gene="Cobll1"
                     /gene_synonym="1810047P18Rik; Coblr1; D430044D16Rik"
                     /coded_by="NM_001363077.1:248..3973"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS89492.1"
                     /db_xref="GeneID:319876"
                     /db_xref="MGI:MGI:2442894"
ORIGIN      
        1 mdrsvpdplp rsaprtpamq pagsagrktk gkaplppaet kgtdvssaed pvestavvte
       61 qqdnmidkdi elsvvlpgdi lksttvhgsk pmmdllvflc aqyhlnpssh tidllsaeen
      121 likfkpntpi gmldvekvil kpksldkkkp tpiipektvr vvinfkktqk tivrvsphap
      181 lqdlapiics kcefdplhtv llkdyqaqep ldltkslndl glrelyamdi srescqishn
      241 pdivkekenk gifsffqrsk kkreqtasap atplvskhrp sftrsntisk pyisntlpsd
      301 apkkrraplp pmptsqgaaq gqerrascve rstsvddtdk ssseaimvrt gslqlsstsi
      361 gtsslkrtkr kapappsktp laqtdernsa mahglpledg iapdsmlels spegmstpeg
      421 slgpgflsqe qcavpkppde isegpgtpea avasltsgvs sdysleeide keelseaskd
      481 pagsisvksp diasastdmr itvekdpdsa lgisdgetsp sskgktqegr stegqgpyhp
      541 vvghignedr vsdsikdmkt lgpnqesvvq neimvcatst dyvknrpgkm ettiegegea
      601 lkkasdmetd rlsgspacrm dnvkssrenh ltaspgpdqk lnqpgvektk mqdaaiqatp
      661 argtfdgnhe vsnssdprad etvqtsdgsi saqhssaslq dsvnasrefr sqgtstyvqd
      721 rlpekepact ygnnvplspv dgsnknpaas ylknfplyrq dsnpkpkpsn eitreyipki
      781 gmttykivpp kslemakdwe seamgrkddq kmlpvgqrht ienmtetsmq tevpatskss
      841 qqpqpdlkpk pssgterhlh rtlssptgte tnppkaprvt tdtgtipfap nledinnile
      901 skfrsrasnp qakpssfflq mqkrasghyv tsaaaksvht apgpapkept ikevqrdpql
      961 speqhpssls erthsaplpn iskadddiiq kpaetspppv apkpmtlrae tspppvfpkp
     1021 mtlpaetspp pvfpkpmtlp aetslplvfp kpmtlraets pppvaakpva lpgsqgtsln
     1081 lktlktfgap rpysssgpsp falavvkrsq sfskacpesa segssalppa atqdekthtv
     1141 nkptvgsqhg dgdkqnnpvq nehssqvltp adgpsftlkr qssltfqssd pehvrqsllt
     1201 airsgeaaak lkrvtvpsnt isvngksgls qsmsidaqds r
//
LOCUS       NP_060064                199 aa            linear   PRI 27-APR-2025
DEFINITION  GTP-binding protein Di-Ras2 [Homo sapiens].
ACCESSION   NP_060064
VERSION     NP_060064.2
DBSOURCE    REFSEQ: accession NM_017594.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Hillmann,B., Zuberer,A., Obermeyer,L., Erb,M., Scheffler,K.,
            Nieratschker,V. and Ethofer,T.
  TITLE     ADHD patients with DIRAS2 risk allele need more thalamic activation
            during emotional face-voice recognition
  JOURNAL   Psychiatry Res 308, 114355 (2022)
   PUBMED   34990989
  REMARK    GeneRIF: ADHD patients with DIRAS2 risk allele need more thalamic
            activation during emotional face-voice recognition.
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Ying,K., Wang,C., Liu,S., Kuang,Y., Tao,Q. and Hu,X.
  TITLE     Diverse Ras-related GTPase DIRAS2, downregulated by PSMD2 in a
            proteasome-mediated way, inhibits colorectal cancer proliferation
            by blocking NF-kappaB signaling
  JOURNAL   Int J Biol Sci 18 (3), 1039-1050 (2022)
   PUBMED   35173535
  REMARK    GeneRIF: Diverse Ras-related GTPase DIRAS2, downregulated by PSMD2
            in a proteasome-mediated way, inhibits colorectal cancer
            proliferation by blocking NF-kappaB signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Rao,H., Li,X., Liu,M., Liu,J., Li,X., Xu,J., Li,L. and Gao,W.Q.
  TITLE     Di-Ras2 promotes renal cell carcinoma formation by activating the
            mitogen-activated protein kinase pathway in the absence of von
            Hippel-Lindau protein
  JOURNAL   Oncogene 39 (19), 3853-3866 (2020)
   PUBMED   32161311
  REMARK    GeneRIF: Di-Ras2 promotes renal cell carcinoma formation by
            activating the mitogen-activated protein kinase pathway in the
            absence of von Hippel-Lindau protein.
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Grunewald,L., Becker,N., Camphausen,A., O'Leary,A., Lesch,K.P.,
            Freudenberg,F. and Reif,A.
  TITLE     Expression of the ADHD candidate gene Diras2 in the brain
  JOURNAL   J Neural Transm (Vienna) 125 (6), 913-923 (2018)
   PUBMED   29488099
  REMARK    GeneRIF: Our findings support the idea of DIRAS2 as a candidate
            gene for attention-deficit/hyperactivity disorder
REFERENCE   6  (residues 1 to 199)
  AUTHORS   Reif,A., Nguyen,T.T., Weissflog,L., Jacob,C.P., Romanos,M.,
            Renner,T.J., Buttenschon,H.N., Kittel-Schneider,S., Gessner,A.,
            Weber,H., Neuner,M., Gross-Lesch,S., Zamzow,K., Kreiker,S.,
            Walitza,S., Meyer,J., Freitag,C.M., Bosch,R., Casas,M., Gomez,N.,
            Ribases,M., Bayes,M., Buitelaar,J.K., Kiemeney,L.A., Kooij,J.J.,
            Kan,C.C., Hoogman,M., Johansson,S., Jacobsen,K.K., Knappskog,P.M.,
            Fasmer,O.B., Asherson,P., Warnke,A., Grabe,H.J., Mahler,J.,
            Teumer,A., Volzke,H., Mors,O.N., Schafer,H., Ramos-Quiroga,J.A.,
            Cormand,B., Haavik,J., Franke,B. and Lesch,K.P.
  TITLE     DIRAS2 is associated with adult ADHD, related traits, and co-morbid
            disorders
  JOURNAL   Neuropsychopharmacology 36 (11), 2318-2327 (2011)
   PUBMED   21750579
  REMARK    GeneRIF: Four single nucleotide polymorphisms (SNPs) and two
            haplotype blocks in DIRAS2 show evidence of association with
            attention deficit/hyperactivity disorder (ADHD) in adults.
            Erratum:[Neuropsychopharmacology. 2012 Mar;37(4):1076]
REFERENCE   7  (residues 1 to 199)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 199)
  AUTHORS   Seshadri,S., DeStefano,A.L., Au,R., Massaro,J.M., Beiser,A.S.,
            Kelly-Hayes,M., Kase,C.S., D'Agostino,R.B. Sr., Decarli,C.,
            Atwood,L.D. and Wolf,P.A.
  TITLE     Genetic correlates of brain aging on MRI and cognitive test
            measures: a genome-wide association and linkage analysis in the
            Framingham Study
  JOURNAL   BMC Med Genet 8 Suppl 1 (Suppl 1), S15 (2007)
   PUBMED   17903297
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 199)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 199)
  AUTHORS   Kontani,K., Tada,M., Ogawa,T., Okai,T., Saito,K., Araki,Y. and
            Katada,T.
  TITLE     Di-Ras, a distinct subgroup of ras family GTPases with unique
            biochemical properties
  JOURNAL   J Biol Chem 277 (43), 41070-41078 (2002)
   PUBMED   12194967
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK122986.1, BP360709.1, CN365099.1 and AK124628.1.
            
            On Jul 8, 2002 this sequence version replaced NP_060064.1.
            
            Summary: DIRAS2 belongs to a distinct branch of the functionally
            diverse Ras (see HRAS; MIM 190020) superfamily of monomeric
            GTPases.[supplied by OMIM, Apr 2004].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.66327.1,
                                           SRR1660805.124933.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375765.5/ ENSP00000364919.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.2"
     Protein         1..199
                     /product="GTP-binding protein Di-Ras2"
                     /note="distinct subgroup of the Ras family member 2; DIRAS
                     family, GTP-binding RAS-like 2"
                     /calculated_mol_wt=22354
     mat_peptide     1..196
                     /product="GTP-binding protein Di-Ras2. /id=PRO_0000191650"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HU8.1)"
                     /calculated_mol_wt=22142
     Region          7..170
                     /region_name="ARHI_like"
                     /note="A Ras homolog member I (ARHI); cd04140"
                     /db_xref="CDD:206711"
     Site            14..21
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206711"
     Site            order(15..16,63..64)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206711"
     Site            order(17..22,32..34,36,39,121..122,124..125,151..153)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206711"
     Site            order(21..22,36,38,44..45,58..59,61,63..64,153)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206711"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5PR73; propagated from
                     UniProtKB/Swiss-Prot (Q96HU8.1)"
     Region          36..44
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HU8.1)"
     Site            order(37..38,42..45)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206711"
     Site            37..44
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206711"
     Site            39
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206711"
     Site            61..64
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206711"
     Site            order(63..76,78..81)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206711"
     Site            121..124
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206711"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5PR73; propagated from
                     UniProtKB/Swiss-Prot (Q96HU8.1)"
     Site            151..153
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206711"
     Site            196
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q96HU8.1)"
     CDS             1..199
                     /gene="DIRAS2"
                     /gene_synonym="Di-Ras2"
                     /coded_by="NM_017594.5:110..709"
                     /db_xref="CCDS:CCDS6687.1"
                     /db_xref="GeneID:54769"
                     /db_xref="HGNC:HGNC:19323"
                     /db_xref="MIM:607863"
ORIGIN      
        1 mpeqsndyrv avfgaggvgk sslvlrfvkg tfresyiptv edtyrqvisc dksictlqit
       61 dttgshqfpa mqrlsiskgh afilvysits rqsleelkpi yeqiceikgd vesipimlvg
      121 nkcdespsre vqsseaeala rtwkcafmet saklnhnvke lfqellnlek rrtvslqidg
      181 kkskqqkrke klkgkcvim
//
LOCUS       NP_058079                923 aa            linear   ROD 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 1 [Mus
            musculus].
ACCESSION   NP_058079
VERSION     NP_058079.2
DBSOURCE    REFSEQ: accession NM_016799.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Thoren,L.A., Norgaard,G.A., Weischenfeldt,J., Waage,J.,
            Jakobsen,J.S., Damgaard,I., Bergstrom,F.C., Blom,A.M., Borup,R.,
            Bisgaard,H.C. and Porse,B.T.
  TITLE     UPF2 is a critical regulator of liver development, function and
            regeneration
  JOURNAL   PLoS One 5 (7), e11650 (2010)
   PUBMED   20657840
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Combes,A.N., Lesieur,E., Harley,V.R., Sinclair,A.H., Little,M.H.,
            Wilhelm,D. and Koopman,P.
  TITLE     Three-dimensional visualization of testis cord morphogenesis, a
            novel tubulogenic mechanism in development
  JOURNAL   Dev Dyn 238 (5), 1033-1041 (2009)
   PUBMED   19334288
REFERENCE   3  (residues 1 to 923)
  AUTHORS   Hoffman,B.G., Zavaglia,B., Witzsche,J., Ruiz de Algara,T.,
            Beach,M., Hoodless,P.A., Jones,S.J., Marra,M.A. and Helgason,C.D.
  TITLE     Identification of transcripts with enriched expression in the
            developing and adult pancreas
  JOURNAL   Genome Biol 9 (6), R99 (2008)
   PUBMED   18554416
REFERENCE   4  (residues 1 to 923)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   5  (residues 1 to 923)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 923)
  AUTHORS   Cobellis,G., Nicolaus,G., Iovino,M., Romito,A., Marra,E.,
            Barbarisi,M., Sardiello,M., Di Giorgio,F.P., Iovino,N., Zollo,M.,
            Ballabio,A. and Cortese,R.
  TITLE     Tagging genes with cassette-exchange sites
  JOURNAL   Nucleic Acids Res 33 (4), e44 (2005)
   PUBMED   15741177
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 923)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 923)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 923)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
REFERENCE   10 (residues 1 to 923)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL627185.10 and AL627078.10.
            
            On Jul 25, 2008 this sequence version replaced NP_058079.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.28185.1,
                                           SRR9219382.167092.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164140 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 67.34 cM"
     Protein         1..923
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 1"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein;
                     plenty-of-prolines-101"
                     /calculated_mol_wt=104175
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          624..>821
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..923
                     /gene="Srrm1"
                     /gene_synonym="POP101; Srm160"
                     /coded_by="NM_016799.4:30..2801"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS38919.2"
                     /db_xref="GeneID:51796"
                     /db_xref="MGI:MGI:1858303"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkeks pelpepsvrm kdssvqeats
      241 tsdilkapkp epvpepkeps peknskkeke ktrprsrsrs ksrsrtrsrs pshtrprrrh
      301 rsrsrsyspr rrpsprrrps prrrtpprrm pppprhrrsr spgrrrrrss aslsgsssss
      361 sssrsrsppk kppkrtsspp rktrrlspsa spprrrhrps spatpppktr hsptpqqsnr
      421 trksrvsvsp grtsgkvtkh kgtekresps papkprkvel seseedkgsk maaadsvqqr
      481 rqyrrqnqqs ssdsgsssts ederpkrshv kngevgrrrr hspsrsasps prkrqketsp
      541 rmqmgkrwqs pvtkssrrrr spsppparrr rspspapppp pppppprrrr sptppprrrt
      601 psppprrrsp sprrysppiq rryspspppk rrtasppppp krraspsppp krrvshsppp
      661 kqrsptvtkr rspslsskhr kgsspgrstr earspqpnkr hspsprprap qtsspppvrr
      721 gasaspqgrq spspstrpir rvsrtpepkk ikkaaspspq svrrvsssrs vsgspepaak
      781 kppappspvq sqspstnwsp avpakkaksp tpslsparns dqegggkkkk kkkdkkhkkd
      841 kkhkkhkkhk kekavtiatp ataapaavsa atttsaqeep aaapeprket eseaeddnld
      901 dlerhlreka lrsmrkaqvs pqs
//
LOCUS       NP_001013002             317 aa            linear   PRI 27-APR-2025
DEFINITION  uncharacterized protein C16orf86 [Homo sapiens].
ACCESSION   NP_001013002 XP_370984
VERSION     NP_001013002.2
DBSOURCE    REFSEQ: accession NM_001012984.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010530.8, BC032064.1 and CA432406.1.
            
            On Feb 10, 2007 this sequence version replaced NP_001013002.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.657716.1,
                                           SRR3476690.902001.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000403458.9/ ENSP00000384117.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..317
                     /product="uncharacterized protein C16orf86"
                     /calculated_mol_wt=33380
     Region          1..184
                     /region_name="DUF4691"
                     /note="Domain of unknown function (DUF4691); pfam15762"
                     /db_xref="CDD:464853"
     Region          1..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZW13.2)"
     CDS             1..317
                     /gene="C16orf86"
                     /coded_by="NM_001012984.3:158..1111"
                     /db_xref="CCDS:CCDS32468.2"
                     /db_xref="GeneID:388284"
                     /db_xref="HGNC:HGNC:33755"
ORIGIN      
        1 masagaerrp gvqeatvvgq gqlteepgsa qtsecpvagd qflvpahear gtqsedqrpa
       61 gaaseselqe egpklgeerp kphagaleer gprpvvsivr prhgpkrkpv kslslpglra
      121 hlkaeaelpp klplqeeepe dsqsepspsa kqhkkakkrk slgapvlhav asmvsaplet
      181 lrlerkaqrl rplyqyvnyc npelnqagkg dgeaeveaea elapvpeegg veqlqallpl
      241 agelgpglal pcpsplvtpt halaplgeea geepgglpsl gvsdhkaevd kstqvdidkm
      301 lsvctaplvp plspqyk
//
LOCUS       NP_056036               1577 aa            linear   PRI 27-APR-2025
DEFINITION  dynamin-binding protein isoform a [Homo sapiens].
ACCESSION   NP_056036 XP_050742
VERSION     NP_056036.1
DBSOURCE    REFSEQ: accession NM_015221.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1577)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 1577)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1577)
  AUTHORS   Ouyang,C., Mu,J., Lu,Q., Li,J., Zhu,H., Wang,Q., Zou,M.H. and
            Xie,Z.
  TITLE     Autophagic degradation of KAT2A/GCN5 promotes directional migration
            of vascular smooth muscle cells by reducing TUBA/alpha-tubulin
            acetylation
  JOURNAL   Autophagy 16 (10), 1753-1770 (2020)
   PUBMED   31878840
  REMARK    GeneRIF: Autophagic degradation of KAT2A/GCN5 promotes directional
            migration of vascular smooth muscle cells by reducing
            TUBA/alpha-tubulin acetylation.
REFERENCE   4  (residues 1 to 1577)
  AUTHORS   Ansar,M., Chung,H.L., Taylor,R.L., Nazir,A., Imtiaz,S.,
            Sarwar,M.T., Manousopoulou,A., Makrythanasis,P., Saeed,S.,
            Falconnet,E., Guipponi,M., Pournaras,C.J., Ansari,M.A., Ranza,E.,
            Santoni,F.A., Ahmed,J., Shah,I., Gul,K., Black,G.C., Bellen,H.J.
            and Antonarakis,S.E.
  TITLE     Bi-allelic Loss-of-Function Variants in DNMBP Cause Infantile
            Cataracts
  JOURNAL   Am J Hum Genet 103 (4), 568-578 (2018)
   PUBMED   30290152
  REMARK    GeneRIF: DNMBP loss-of-function variants cause infantile-onset
            cataracts in humans.
REFERENCE   5  (residues 1 to 1577)
  AUTHORS   Tatjewski,M., Gruca,A., Plewczynski,D. and Grynberg,M.
  TITLE     The proline-rich region of glyceraldehyde-3-phosphate dehydrogenase
            from human sperm may bind SH3 domains, as revealed by a
            bioinformatic study of low-complexity protein segments
  JOURNAL   Mol Reprod Dev 83 (2), 144-148 (2016)
   PUBMED   26660717
REFERENCE   6  (residues 1 to 1577)
  AUTHORS   Minster,R.L., DeKosky,S.T. and Kamboh,M.I.
  TITLE     No association of dynamin binding protein (DNMBP) gene SNPs and
            Alzheimer's disease
  JOURNAL   Neurobiol Aging 29 (10), 1602-1604 (2008)
   PUBMED   17442457
  REMARK    GeneRIF: We observed no association of statistical significance in
            either the total sample or the APOE*4 non-carriers for any of the
            SNPs of Dynamin Binding Protein.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1577)
  AUTHORS   Otani,T., Ichii,T., Aono,S. and Takeichi,M.
  TITLE     Cdc42 GEF Tuba regulates the junctional configuration of simple
            epithelial cells
  JOURNAL   J Cell Biol 175 (1), 135-146 (2006)
   PUBMED   17015620
  REMARK    GeneRIF: Tuba controls the shaping of cell junctions through the
            local activation of Cdc42 and its effectors.
REFERENCE   8  (residues 1 to 1577)
  AUTHORS   Kuwano,R., Miyashita,A., Arai,H., Asada,T., Imagawa,M., Shoji,M.,
            Higuchi,S., Urakami,K., Kakita,A., Takahashi,H., Tsukie,T.,
            Toyabe,S., Akazawa,K., Kanazawa,I. and Ihara,Y.
  CONSRTM   Japanese Genetic Study Consortium for Alzeheimer's Disease
  TITLE     Dynamin-binding protein gene on chromosome 10q is associated with
            late-onset Alzheimer's disease
  JOURNAL   Hum Mol Genet 15 (13), 2170-2182 (2006)
   PUBMED   16740596
  REMARK    GeneRIF: Results confirmed DNMBP may be one of the susceptibility
            genes for Alzheimer's disease.
            GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   9  (residues 1 to 1577)
  AUTHORS   Cestra,G., Kwiatkowski,A., Salazar,M., Gertler,F. and De Camilli,P.
  TITLE     Tuba, a GEF for CDC42, links dynamin to actin regulatory proteins
  JOURNAL   Methods Enzymol 404, 537-545 (2005)
   PUBMED   16413298
REFERENCE   10 (residues 1 to 1577)
  AUTHORS   Salazar,M.A., Kwiatkowski,A.V., Pellegrini,L., Cestra,G.,
            Butler,M.H., Rossman,K.L., Serna,D.M., Sondek,J., Gertler,F.B. and
            De Camilli,P.
  TITLE     Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl
            homology domains, links dynamin to regulation of the actin
            cytoskeleton
  JOURNAL   J Biol Chem 278 (49), 49031-49043 (2003)
   PUBMED   14506234
  REMARK    GeneRIF: functions to bring together dynamin with actin regulatory
            proteins
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB481528.1, AL833283.1,
            AB023227.1 and AI023943.1.
            
            On Dec 18, 2003 this sequence version replaced XP_050742.5.
            
            Summary: This gene encodes a protein belonging to the guanine
            nucleotide exchange factor family, and which regulates the
            configuration of cell junctions. It contains multiple binding sites
            for dynamin and thus links dynamin to actin regulatory proteins.
            Polymorphisms in this gene have been linked to Alzheimer's disease
            in some populations, though there are conflicting reports of such
            linkages in other populations. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.29545.1, AL833283.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324109.9/ ENSP00000315659.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..1577
                     /product="dynamin-binding protein isoform a"
                     /note="scaffold protein TUBA"
                     /calculated_mol_wt=177217
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          6..56
                     /region_name="SH3_DNMBP_N1"
                     /note="First N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11794"
                     /db_xref="CDD:212728"
     Site            order(11,13,16,20,38..39,52,54..55)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212728"
     Region          70..123
                     /region_name="SH3_DNMBP_N2"
                     /note="Second N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11795"
                     /db_xref="CDD:212729"
     Site            order(75,77,80,84,102..103,117,119..120)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212729"
     Region          149..199
                     /region_name="SH3_DNMBP_N3"
                     /note="Third N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11796"
                     /db_xref="CDD:212730"
     Site            order(154,156,159,163,181..182,195,197..198)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212730"
     Region          211..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          247..296
                     /region_name="SH3_DNMBP_N4"
                     /note="Fourth N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11797"
                     /db_xref="CDD:212731"
     Site            order(252,254,257,261,279..280,293,295..296)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212731"
     Region          335..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          591..624
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          639..659
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          785..965
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(791,795,884,916..917,920..921,923..924,927..928,
                     931..932,935,961,965)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          1017..1208
                     /region_name="BAR_DNMBP"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin
                     Binding Protein; cd07589"
                     /db_xref="CDD:153273"
     Site            order(1029,1032..1033,1037,1039..1040,1043..1044,
                     1046..1047,1061..1062,1064..1065,1068..1069,1071..1072,
                     1075,1081,1084..1085,1169,1172..1173,1175,1180,1183..1184,
                     1186..1187,1190..1191,1194..1195,1197..1198,1201..1202,
                     1204..1205)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153273"
     Region          1289..1345
                     /region_name="SH3_DNMBP_C1"
                     /note="First C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11798"
                     /db_xref="CDD:212732"
     Site            order(1294,1296,1299,1303,1325..1326,1339,1341..1342)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212732"
     Region          1348..1487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          1517..1573
                     /region_name="SH3_DNMBP_C2"
                     /note="Second C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba, and similar domains;
                     cd12141"
                     /db_xref="CDD:213017"
     Site            order(1522,1524,1527,1531,1553..1554,1567,1569..1570)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213017"
     CDS             1..1577
                     /gene="DNMBP"
                     /gene_synonym="ARHGEF36; CTRCT48; TUBA"
                     /coded_by="NM_015221.4:121..4854"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7485.1"
                     /db_xref="GeneID:23268"
                     /db_xref="HGNC:HGNC:30373"
                     /db_xref="MIM:611282"
ORIGIN      
        1 meagsvvrai fdfcpsvsee lplfvgdiie vlavvdefwl lgkkedvtgq fpssfveivt
       61 ipslkegerl fvciceftsq eldnlplhrg dlvildgipt agwlqgrscw gargffpssc
      121 vrelclssqs rqwhsqsalf qipeysmgqa ralmglsaql deeldfregd vitiigvpep
      181 gwfegelegr rgifpegfve llgplrtvde svssgnqddc ivngevdtpv geeeigpded
      241 eeepgtygva lyrfqalepn eldfevgdki rilatledgw legslkgrtg ifpyrfvklc
      301 pdtrveetma lpqegslari petsldclen tlgveeqrhe tsdheaeepd ciiseaptsp
      361 lghltseydt drnsyqdedt aggpprspgv ewemplatds ptsdptevvn gissqpqvpf
      421 hpnlqksqyy stvggshphs eqypdllple artrdyaslp pkrmysqlkt lqkpvlplyr
      481 gssvsasrvv kprqsspqlh nlasytkkhh tssvysiser lemkpgpqaq glvmeaaths
      541 qgdgstdlds kltqqliefe kslagpgtep dkilrhfsim dfnsekdivr gsskliteqe
      601 lperrkalrp ppprpctpvs tsphllvdqn lkpapplvvr psrpaplpps aqqrtnavsp
      661 kllsrhrptc etlekegpgh mgrsldqtsp cplvlvriee merdldmysr aqeelnlmle
      721 ekqdessrae tledlkfces nieslnmelq qlremtllss qssslvapsg svsaenpeqr
      781 mlekrakvie ellqterdyi rdlemcieri mvpmqqaqvp nidfeglfgn mqmvikvskq
      841 llaaleisda vgpvflghrd elegtykiyc qnhdeaiall eiyekdekiq khlqdsladl
      901 kslynewgct nyinlgsfli kpvqrvmryp lllmellnst peshpdkvpl tnavlavkei
      961 nvnineykrr kdlvlkyrkg dedslmekis klnihsiikk snrvsshlkh ltgfapqikd
     1021 evfeeteknf rmqerliksf irdlslylqh iresacvkvv aavsmwdvcm erghrdleqf
     1081 ervhryisdq lftnfkerte rlvisplnql lsmftgphkl vqkrfdklld fyncteraek
     1141 lkdkktleel qsarnnyeal naqlldelpk fhqyaqglft ncvhgyaeah cdfvhqaleq
     1201 lkpllsllkv agregnliai fheehsrvlq qlqvftffpe slpatkkpfe rktidrqsar
     1261 kpllglpsym lqseelrasl laryppeklf qaernfnaaq dldvsllegd lvgvikkkdp
     1321 mgsqnrwlid ngvtkgfvys sflkpynprr shsdasvgsh sstesehgss sprfprqnsg
     1381 stltfnpssm avsftsgscq kqpqdasppp kecdqgtlsa slnpsnsess psrcpsdpds
     1441 tsqprsgdsa dvardvkqpt atprsyrnfr hpeivgysvp grngqsqdlv kgcartaqap
     1501 edrstepdgs eaegnqvyfa vytfkarnpn elsvsanqkl kilefkdvtg ntewwlaevn
     1561 gkkgyvpsny irkteyt
//
LOCUS       NP_060596                247 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 33 [Homo sapiens].
ACCESSION   NP_060596
VERSION     NP_060596.2
DBSOURCE    REFSEQ: accession NM_018126.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Liu,F., Ma,M., Gao,A., Ma,F., Ma,G., Liu,P., Jia,C., Wang,Y.,
            Donahue,K., Zhang,S., Ong,I.M., Keles,S., Li,L. and Xu,W.
  TITLE     PKM2-TMEM33 axis regulates lipid homeostasis in cancer cells by
            controlling SCAP stability
  JOURNAL   EMBO J 40 (22), e108065 (2021)
   PUBMED   34487377
  REMARK    GeneRIF: PKM2-TMEM33 axis regulates lipid homeostasis in cancer
            cells by controlling SCAP stability.
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Arhatte,M., Gunaratne,G.S., El Boustany,C., Kuo,I.Y., Moro,C.,
            Duprat,F., Plaisant,M., Duval,H., Li,D., Picard,N., Couvreux,A.,
            Duranton,C., Rubera,I., Pagnotta,S., Lacas-Gervais,S.,
            Ehrlich,B.E., Marchant,J.S., Savage,A.M., van Eeden,F.J.M.,
            Wilkinson,R.N., Demolombe,S., Honore,E. and Patel,A.
  TITLE     TMEM33 regulates intracellular calcium homeostasis in renal tubular
            epithelial cells
  JOURNAL   Nat Commun 10 (1), 2024 (2019)
   PUBMED   31048699
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Sokolina,K., Kittanakom,S., Snider,J., Kotlyar,M., Maurice,P.,
            Gandia,J., Benleulmi-Chaachoua,A., Tadagaki,K., Oishi,A., Wong,V.,
            Malty,R.H., Deineko,V., Aoki,H., Amin,S., Yao,Z., Morato,X.,
            Otasek,D., Kobayashi,H., Menendez,J., Auerbach,D., Angers,S.,
            Przulj,N., Bouvier,M., Babu,M., Ciruela,F., Jockers,R., Jurisica,I.
            and Stagljar,I.
  TITLE     Systematic protein-protein interaction mapping for clinically
            relevant human GPCRs
  JOURNAL   Mol Syst Biol 13 (3), 918 (2017)
   PUBMED   28298427
  REMARK    Erratum:[Mol Syst Biol. 2025 Feb;21(2):208-209. doi:
            10.1038/s44320-024-00080-3. PMID: 39762653]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Benleulmi-Chaachoua,A., Chen,L., Sokolina,K., Wong,V., Jurisica,I.,
            Emerit,M.B., Darmon,M., Espin,A., Stagljar,I., Tafelmeyer,P.,
            Zamponi,G.W., Delagrange,P., Maurice,P. and Jockers,R.
  TITLE     Protein interactome mining defines melatonin MT1 receptors as
            integral component of presynaptic protein complexes of neurons
  JOURNAL   J Pineal Res 60 (1), 95-108 (2016)
   PUBMED   26514267
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Sakabe,I., Hu,R., Jin,L., Clarke,R. and Kasid,U.N.
  TITLE     TMEM33: a new stress-inducible endoplasmic reticulum transmembrane
            protein and modulator of the unfolded protein response signaling
  JOURNAL   Breast Cancer Res Treat 153 (2), 285-297 (2015)
   PUBMED   26268696
  REMARK    GeneRIF: TMEM33 is a novel regulator of the PERK-eIE2alpha-ATF4 and
            IRE1-XBP1 axes of the UPR signaling.
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Urade,T., Yamamoto,Y., Zhang,X., Ku,Y. and Sakisaka,T.
  TITLE     Identification and characterization of TMEM33 as a
            reticulon-binding protein
  JOURNAL   Kobe J Med Sci 60 (3), E57-E65 (2014)
   PUBMED   25612671
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 247)
  AUTHORS   Daulat,A.M., Maurice,P., Froment,C., Guillaume,J.L., Broussard,C.,
            Monsarrat,B., Delagrange,P. and Jockers,R.
  TITLE     Purification and identification of G protein-coupled receptor
            protein complexes under native conditions
  JOURNAL   Mol Cell Proteomics 6 (5), 835-844 (2007)
   PUBMED   17215244
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000948.2 and AC106052.4.
            
            On Mar 6, 2009 this sequence version replaced NP_060596.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.89382.1, AY659966.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000504986.6/ ENSP00000422473.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p13"
     Protein         1..247
                     /product="transmembrane protein 33"
                     /calculated_mol_wt=27847
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P57088.2)"
     Region          9..245
                     /region_name="TMEM33_Pom33"
                     /note="Transmembrane protein 33/Nucleoporin POM33;
                     pfam03661"
                     /db_xref="CDD:461009"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57088.2)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57088.2)"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57088.2)"
     CDS             1..247
                     /gene="TMEM33"
                     /gene_synonym="1600019D15Rik; Pom33; SHINC-3; SHINC3"
                     /coded_by="NM_018126.3:57..800"
                     /db_xref="CCDS:CCDS3464.1"
                     /db_xref="GeneID:55161"
                     /db_xref="HGNC:HGNC:25541"
                     /db_xref="MIM:618515"
ORIGIN      
        1 madttpngpq gagavqfmmt nkldtamwls rlftvycsal fvlpllglhe aasfyqrall
       61 analtsalrl hqrlphfqls raflaqalle dschyllysl ifvnsypvtm sifpvllfsl
      121 lhaatytkkv ldargsnslp llrsvldkls anqqnilkfi acneiflmpa tvfmlfsgqg
      181 sllqpfiyyr fltlryssrr npycrtlfne lrivvehiim kpacplfvrr lclqsiafis
      241 rlaptvp
//
LOCUS       NP_689586                378 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 684 [Homo sapiens].
ACCESSION   NP_689586
VERSION     NP_689586.3
DBSOURCE    REFSEQ: accession NM_152373.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK094072.1, BC111463.1 and BG116229.1.
            
            On Dec 29, 2009 this sequence version replaced NP_689586.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK094072.1, SRR3476690.362201.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372699.8/ ENSP00000361784.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..378
                     /product="zinc finger protein 684"
                     /note="hypothetical protein MGC27466"
                     /calculated_mol_wt=43814
     Region          8..68
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          161..181
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <185..345
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          189..209
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(194,196,198,200..201,204..205,208,222,224,228..229,
                     232..233,236,250,252,254,256..257,260..261,264)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..321
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(306,308,310,312..313,316..317,320,334,336,340..341,
                     344..345,348,362,364,366,368..369,372..373,376)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          329..349
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          341..366
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..378
                     /gene="ZNF684"
                     /coded_by="NM_152373.4:176..1312"
                     /db_xref="CCDS:CCDS454.1"
                     /db_xref="GeneID:127396"
                     /db_xref="HGNC:HGNC:28418"
ORIGIN      
        1 misfqesvtf qdvavdftae ewqlldcaer tlywdvmlen yrnlisvgcp itktkvilkv
       61 eqgqepwmve ganphesspe sdyplvdepg khreskdnfl ksvlltfnki ltmerihhyn
      121 mstslnpmrk ksyksfekcl ppnldllkyn rsytvenaye csecgkafkk kfhfirhekn
      181 htrkkpfecn dcgkaysrka hlathqkihn gerpfvcndc gkafmhkaql vvhqrlhtge
      241 kpyecsqcgk tftwnssfnq hvkshtleks feckecgktf ryssslykhs rfhtgekpyq
      301 ciicgkafgn tsvlvthqri htgekpysci ecgkafikks hllrhqitht gekpyecnrc
      361 gkafsqksnl ivhqkiht
//
LOCUS       NP_001348523              79 aa            linear   ROD 27-APR-2025
DEFINITION  armadillo repeat-containing protein 7 isoform 2 [Mus musculus].
ACCESSION   NP_001348523 XP_017170068
VERSION     NP_001348523.1
DBSOURCE    REFSEQ: accession NM_001361594.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL645470.20.
            
            On Mar 29, 2018 this sequence version replaced XP_017170068.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF585735.1, FO718557.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 80.84 cM"
     Protein         1..79
                     /product="armadillo repeat-containing protein 7 isoform 2"
                     /note="armadillo repeat-containing protein 7"
                     /calculated_mol_wt=8900
     CDS             1..79
                     /gene="Armc7"
                     /gene_synonym="A630084C13"
                     /coded_by="NM_001361594.1:271..510"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:276905"
                     /db_xref="MGI:MGI:2679719"
ORIGIN      
        1 maqkpkidph vgrlgylqal vtefqetesq dakeqvlanl anfaydpgny qylrqlqvld
       61 lfldslseen etlikfaiv
//
LOCUS       NP_001356189             876 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 245 isoform 2 [Mus musculus].
ACCESSION   NP_001356189 XP_006537988
VERSION     NP_001356189.1
DBSOURCE    REFSEQ: accession NM_001369260.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 876)
  AUTHORS   Hoffman,B.G., Zavaglia,B., Witzsche,J., Ruiz de Algara,T.,
            Beach,M., Hoodless,P.A., Jones,S.J., Marra,M.A. and Helgason,C.D.
  TITLE     Identification of transcripts with enriched expression in the
            developing and adult pancreas
  JOURNAL   Genome Biol 9 (6), R99 (2008)
   PUBMED   18554416
REFERENCE   2  (residues 1 to 876)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX470220.11 and AL929577.9.
            
            On Mar 29, 2019 this sequence version replaced XP_006537988.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR10223970.6268.1,
                                           SRR10223971.4705.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..876
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 31.66 cM"
     Protein         1..876
                     /product="transmembrane protein 245 isoform 2"
                     /note="likely ortholog of H. sapiens chromosome 9 open
                     reading frame 5 (C9orf5); transmembrane 245"
                     /calculated_mol_wt=97227
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            56..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            181..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            237..257
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Region          289..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZXD8; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            377..397
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            457..477
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            548
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            572
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            623..643
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Region          <645..837
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
     Site            647..667
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            728..748
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            749..769
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            773..793
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            812..832
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AZA5.1)"
     Site            874
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H330; propagated from
                     UniProtKB/Swiss-Prot (B1AZA5.1)"
     CDS             1..876
                     /gene="Tmem245"
                     /gene_synonym="A630051L19Rik; D730040F13Rik"
                     /coded_by="NM_001369260.1:19..2649"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS89746.1"
                     /db_xref="GeneID:242474"
                     /db_xref="MGI:MGI:2445107"
ORIGIN      
        1 madrggpaea psprgsprpe sraprtvgpg etprtaalal rfdkpikqaf yntgavlfvc
       61 lccgaavlvy fileaflrpl lwavlcgtfl hpfkssltrl grlwlrrlhr ahtpivlaal
      121 llplcfadyg vealgeqalr rrrlllllga ggpllyglyc lgsylgvqvl lahagalicr
      181 gldyfsslwi wtlvvgyvlm vsfkwnastq rylravsipv wmillfhias lagswripvf
      241 lvivflmsvg tlyekqneke sagaelpgqv ismaastlan laisitgyes stedqpsdpp
      301 teptdkgepp palsasssss srsspsspsp tlgrqrpemg tflrkkktsd iyfvslvwai
      361 iavqlwlnlw ivqllpvpva vwiikklvih fgvvgflekr chawwqviec flkerqeala
      421 pwpiiglgkf llkvdsklwh wlnkkmiiwl ekmldkiisi fiifllvigt lllallltak
      481 vhqesvhmie vtsslinetl anhpewanwl peaqvvqral nsaannvyqy grewithklh
      541 kilgdkvnnt aviekqvlel wdrlyhswfv knvthsgrhk ghkmhvsrqn swlgdildwq
      601 diasfvheni etflsilesl wivmsrnvsl lfttvttllt ilfysgtall nfvlsliifl
      661 ttlfyllsss deyykpvkwv isltplsqpg pssniigqsv eeairgvfda slkmagfygl
      721 ytwlthtifg inivfipsal aailgavpfl gtywaavpav ldlwltqglg ckailllvfh
      781 llptyfvdta iysdisgggh pyltglavag gayylglega iigpillcil vvasniysam
      841 lvsptnsmpt pnqtpwpaqt qrtfrdised lkssvd
//
LOCUS       NP_001355354             213 aa            linear   ROD 27-APR-2025
DEFINITION  RNA polymerase I subunit H isoform 2 [Mus musculus].
ACCESSION   NP_001355354
VERSION     NP_001355354.1
DBSOURCE    REFSEQ: accession NM_001368425.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Friedel,R.H., Seisenberger,C., Kaloff,C. and Wurst,W.
  TITLE     EUCOMM--the European conditional mouse mutagenesis program
  JOURNAL   Brief Funct Genomic Proteomic 6 (3), 180-185 (2007)
   PUBMED   17967808
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CR956641.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.2072167.1,
                                           SRR5189685.36412.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 19.16 cM"
     Protein         1..213
                     /product="RNA polymerase I subunit H isoform 2"
                     /note="ZNRD1 antisense RNA 1; ZNRD1 antisense gene protein
                     1; T-complex testis-expressed protein 4; zinc ribbon
                     domain containing 1, antisense"
                     /calculated_mol_wt=25357
     Region          1..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R0E5.2)"
     CDS             1..213
                     /gene="Polr1has"
                     /gene_synonym="1700022C21Rik; Znrd1-as; Znrd1as"
                     /coded_by="NM_001368425.1:705..1346"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS89093.1"
                     /db_xref="GeneID:76416"
                     /db_xref="MGI:MGI:1923666"
ORIGIN      
        1 mvermkkdtg detktkvqee ppspsppppp pprrerqkqh ywvperekkq ierhihrtsh
       61 areftdkpwr qprlfsettl pkivleeesi pqaqkrrqah erellqikdh rermirgrel
      121 lqqrlkdril rkspsqiplp ekrdqvkkqk kefekvvayp lvqpsctsri kvdvlmeksq
      181 deedlstiik pfgrrflavp pflrtqigki kdl
//
LOCUS       NP_001026915             379 aa            linear   PRI 27-APR-2025
DEFINITION  RIB43A-like with coiled-coils protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001026915
VERSION     NP_001026915.1
DBSOURCE    REFSEQ: accession NM_001031745.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Froyen,G., Corbett,M., Vandewalle,J., Jarvela,I., Lawrence,O.,
            Meldrum,C., Bauters,M., Govaerts,K., Vandeleur,L., Van Esch,H.,
            Chelly,J., Sanlaville,D., van Bokhoven,H., Ropers,H.H.,
            Laumonnier,F., Ranieri,E., Schwartz,C.E., Abidi,F., Tarpey,P.S.,
            Futreal,P.A., Whibley,A., Raymond,F.L., Stratton,M.R., Fryns,J.P.,
            Scott,R., Peippo,M., Sipponen,M., Partington,M., Mowat,D.,
            Field,M., Hackett,A., Marynen,P., Turner,G. and Gecz,J.
  TITLE     Submicroscopic duplications of the hydroxysteroid dehydrogenase
            HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with
            mental retardation
  JOURNAL   Am J Hum Genet 82 (2), 432-443 (2008)
   PUBMED   18252223
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Sogayar,M.C., Camargo,A.A., Bettoni,F., Carraro,D.M., Pires,L.C.,
            Parmigiani,R.B., Ferreira,E.N., de Sa Moreira,E., do Rosario D de O
            Latorre,M., Simpson,A.J., Cruz,L.O., Degaki,T.L., Festa,F.,
            Massirer,K.B., Sogayar,M.C., Filho,F.C., Camargo,L.P., Cunha,M.A.,
            De Souza,S.J., Faria,M. Jr., Giuliatti,S., Kopp,L., de
            Oliveira,P.S., Paiva,P.B., Pereira,A.A., Pinheiro,D.G., Puga,R.D.,
            S de Souza,J.E., Albuquerque,D.M., Andrade,L.E., Baia,G.S.,
            Briones,M.R., Cavaleiro-Luna,A.M., Cerutti,J.M., Costa,F.F.,
            Costanzi-Strauss,E., Espreafico,E.M., Ferrasi,A.C., Ferro,E.S.,
            Fortes,M.A., Furchi,J.R., Giannella-Neto,D., Goldman,G.H.,
            Goldman,M.H., Gruber,A., Guimaraes,G.S., Hackel,C.,
            Henrique-Silva,F., Kimura,E.T., Leoni,S.G., Macedo,C., Malnic,B.,
            Manzini,B. CV, Marie,S.K., Martinez-Rossi,N.M., Menossi,M.,
            Miracca,E.C., Nagai,M.A., Nobrega,F.G., Nobrega,M.P.,
            Oba-Shinjo,S.M., Oliveira,M.K., Orabona,G.M., Otsuka,A.Y.,
            Paco-Larson,M.L., Paixao,B.M., Pandolfi,J.R., Pardini,M.I., Passos
            Bueno,M.R., Passos,G.A., Pesquero,J.B., Pessoa,J.G., Rahal,P.,
            Rainho,C.A., Reis,C.P., Ricca,T.I., Rodrigues,V., Rogatto,S.R.,
            Romano,C.M., Romeiro,J.G., Rossi,A., Sa,R.G., Sales,M.M.,
            Sant'Anna,S.C., Santarosa,P.L., Segato,F., Silva,W.A. Jr.,
            Silva,I.D., Silva,N.P., Soares-Costa,A., Sonati,M.F., Strauss,B.E.,
            Tajara,E.H., Valentini,S.R., Villanova,F.E., Ward,L.S. and
            Zanette,D.L.
  CONSRTM   Ludwig-FAPESP Transcript Finishing Initiative
  TITLE     A transcript finishing initiative for closing gaps in the human
            transcriptome
  JOURNAL   Genome Res 14 (7), 1413-1423 (2004)
   PUBMED   15197164
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK304179.1, BC036767.1, CA433728.1 and BF433577.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.161704.1,
                                           SRR5189667.145103.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375327.6/ ENSP00000364476.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..379
                     /product="RIB43A-like with coiled-coils protein 1 isoform
                     1"
                     /note="RIB43A-like with coiled-coils protein 1"
                     /calculated_mol_wt=43884
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N443.1)"
     Region          9..379
                     /region_name="RIB43A"
                     /note="pfam05914"
                     /db_xref="CDD:461780"
     CDS             1..379
                     /gene="RIBC1"
                     /gene_synonym="2610028I09Rik"
                     /coded_by="NM_001031745.5:222..1361"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35299.1"
                     /db_xref="GeneID:158787"
                     /db_xref="HGNC:HGNC:26537"
ORIGIN      
        1 mynikqstdt keaaaiearr nrekerqnrf fnvrnrvmgv dvqalnnqvg drkrreaaer
       61 skeaaygtsq vqydvvvqml ekeeadrtrq lakkvqefre qkqqlkngre fslwdpgqvw
      121 kglptylsys ntypgpaslq yfsgedldrd trlrmqqgqf rynlerqqqe qqqakvdeny
      181 tdalsnqlrl amdaqathla rleescraam mcamananka qaavqagrqr cerqreqkan
      241 laeiqhqsts dlltenpqva qhpmapyrvl pycwkgmtpe qqaairkeqe vqrskkqahr
      301 qaektldtew ksqtmssaqa vleleeqere lcavfqrglg sfnqqlaneq kaqqdylnsv
      361 iytnqptaqy hqqfntssr
//
LOCUS       NP_001289559             455 aa            linear   ROD 27-APR-2025
DEFINITION  oxysterol-binding protein 2 isoform 3 [Mus musculus].
ACCESSION   NP_001289559
VERSION     NP_001289559.1
DBSOURCE    REFSEQ: accession NM_001302630.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Ge,T., Yuan,L., Xu,L., Yang,F., Xu,W., Niu,C., Li,G., Zhou,H. and
            Zheng,Y.
  TITLE     Coiled-coil domain containing 159 is required for spermatid head
            and tail assembly in micedagger
  JOURNAL   Biol Reprod 110 (5), 877-894 (2024)
   PUBMED   38236177
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Udagawa,O., Ito,C., Ogonuki,N., Sato,H., Lee,S., Tripvanuntakul,P.,
            Ichi,I., Uchida,Y., Nishimura,T., Murakami,M., Ogura,A., Inoue,T.,
            Toshimori,K. and Arai,H.
  TITLE     Oligo-astheno-teratozoospermia in mice lacking ORP4, a
            sterol-binding protein in the OSBP-related protein family
  JOURNAL   Genes Cells 19 (1), 13-27 (2014)
   PUBMED   24245814
  REMARK    GeneRIF: ORP4 is essential for the postmeiotic differentiation of
            germ cells
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Anniss,A.M., Apostolopoulos,J., Dworkin,S., Purton,L.E. and
            Sparrow,R.L.
  TITLE     An oxysterol-binding protein family identified in the mouse
  JOURNAL   DNA Cell Biol 21 (8), 571-580 (2002)
   PUBMED   12215260
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CV784397.1, BC058602.1 and BC058356.1.
            
            Summary: The protein encoded by this gene belongs to the
            oxysterol-binding protein-related family of proteins, which are
            defined by a C-terminal sterol domain with a highly conserved
            EQVSHHPP motif. Oxysterols are oxygenated derivatives of
            cholesterol that are involved in mechanisms that include apoptosis,
            cholesterol homeostasis, lipid trafficking and cell
            differentiation. This protein is selectively expressed at high
            levels in the brain and testis. Within the testis, the mRNA is
            localized to postmeiotic germ cells, including spermatids and
            spermatozoa, but is not detectable in somatic cells. Mice
            homozygous mutant for a targeted deletion in this gene do not
            exhibit overt developmental phenotypes but are male sterile.
            Females display normal fertility. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2014].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC031794.1, SRR9219382.148547.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 2.6 cM"
     Protein         1..455
                     /product="oxysterol-binding protein 2 isoform 3"
                     /calculated_mol_wt=52049
     Region          66..444
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     CDS             1..455
                     /gene="Osbp2"
                     /gene_synonym="1700095P05Rik; C630001G20Rik; Gm244; ORP-4;
                     OSBPL1"
                     /coded_by="NM_001302630.2:387..1754"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS78912.1"
                     /db_xref="GeneID:74309"
                     /db_xref="MGI:MGI:1921559"
ORIGIN      
        1 medstsfitv vteakedrkp esgpgtttvd wtsadnvldg asfmpknsck vkrrvripdk
       61 pnyslnlwsi mkncigrels ripmpvnfne plsmlqrlte dleyhhlldk avnctssveq
      121 mclvaafsvs systtvhria kpfnpmlget feldrmedmg lrslceqvsh hppsaahhvf
      181 skhgwslwqe itiaskfrgk yisimplgai hlefqasgnh yvwrkststv hniivgklwi
      241 dqsgdieivn hktkdrcqlk fvpysyfske aarkvtgvvs dsqgkahyvl sgswddqmec
      301 skivhsspss dgrqktvyqt lpakllwrky plpenaenmy yfselaltln eqedgvaptd
      361 srlrpdqrlm ergrwdeant ekqrleekqr lsrrrrlesc tagcggeeek esdgyvplwf
      421 ekrldpltge macmykggyw eakekkdwhm cpnif
//
LOCUS       NP_001673               1220 aa            linear   PRI 27-APR-2025
DEFINITION  plasma membrane calcium-transporting ATPase 1 isoform 1b [Homo
            sapiens].
ACCESSION   NP_001673
VERSION     NP_001673.2
DBSOURCE    REFSEQ: accession NM_001682.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1220)
  AUTHORS   Kobayashi,Y., Yatsu,K., Haruna,A., Kawano,R., Ozawa,M., Haze,T.,
            Komiya,S., Suzuki,S., Ohki,Y., Fujiwara,A., Saka,S., Hirawa,N.,
            Toya,Y. and Tamura,K.
  TITLE     ATP2B1 gene polymorphisms associated with resistant hypertension in
            the Japanese population
  JOURNAL   J Clin Hypertens (Greenwich) 26 (4), 355-362 (2024)
   PUBMED   38430457
  REMARK    GeneRIF: ATP2B1 gene polymorphisms associated with resistant
            hypertension in the Japanese population.
REFERENCE   2  (residues 1 to 1220)
  AUTHORS   Gao,Y., Liu,Y., Jiang,Y., Qin,M., Guan,Z., Gao,Y. and Yang,Y.
  TITLE     Association between polymorphism and haplotype of ATP2B1 gene and
            skeletal fluorosis in Han population
  JOURNAL   Int J Environ Health Res 34 (3), 1410-1420 (2024)
   PUBMED   37211801
  REMARK    GeneRIF: Association between polymorphism and haplotype of ATP2B1
            gene and skeletal fluorosis in Han population.
REFERENCE   3  (residues 1 to 1220)
  AUTHORS   Berrocal,M. and Mata,A.M.
  TITLE     The Plasma Membrane Ca2+-ATPase, a Molecular Target for Tau-induced
            Cytosolic Calcium Dysregulation
  JOURNAL   Neuroscience 518, 112-118 (2023)
   PUBMED   35469971
  REMARK    GeneRIF: The Plasma Membrane Ca[2+]-ATPase, a Molecular Target for
            Tau-induced Cytosolic Calcium Dysregulation.
            Review article
REFERENCE   4  (residues 1 to 1220)
  AUTHORS   Yang,X., Lu,L., Wu,C. and Zhang,F.
  TITLE     ATP2B1-AS1 exacerbates sepsis-induced cell apoptosis and
            inflammation by regulating miR-23a-3p/TLR4 axis
  JOURNAL   Allergol Immunopathol (Madr) 51 (2), 17-26 (2023)
   PUBMED   36916084
  REMARK    GeneRIF: ATP2B1-AS1 exacerbates sepsis-induced cell apoptosis and
            inflammation by regulating miR-23a-3p/TLR4 axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1220)
  AUTHORS   Rahimi,M.J., Urban,N., Wegler,M., Sticht,H., Schaefer,M., Popp,B.,
            Gaunitz,F., Morleo,M., Nigro,V., Maitz,S., Mancini,G.M.S.,
            Ruivenkamp,C., Suk,E.K., Bartolomaeus,T., Merkenschlager,A.,
            Koboldt,D., Bartholomew,D., Stegmann,A.P.A., Sinnema,M.,
            Duynisveld,I., Salvarinova,R., Race,S., de Vries,B.B.A.,
            Trimouille,A., Naudion,S., Marom,D., Hamiel,U., Henig,N.,
            Demurger,F., Rahner,N., Bartels,E., Hamm,J.A., Putnam,A.M.,
            Person,R., Abou Jamra,R. and Oppermann,H.
  TITLE     De novo variants in ATP2B1 lead to neurodevelopmental delay
  JOURNAL   Am J Hum Genet 109 (5), 944-952 (2022)
   PUBMED   35358416
  REMARK    GeneRIF: De novo variants in ATP2B1 lead to neurodevelopmental
            delay.
REFERENCE   6  (residues 1 to 1220)
  AUTHORS   Kessler,F., Falchetto,R., Heim,R., Meili,R., Vorherr,T.,
            Strehler,E.E. and Carafoli,E.
  TITLE     Study of calmodulin binding to the alternatively spliced C-terminal
            domain of the plasma membrane Ca2+ pump
  JOURNAL   Biochemistry 31 (47), 11785-11792 (1992)
   PUBMED   1332771
REFERENCE   7  (residues 1 to 1220)
  AUTHORS   Wang,K.K., Wright,L.C., Machan,C.L., Allen,B.G., Conigrave,A.D. and
            Roufogalis,B.D.
  TITLE     Protein kinase C phosphorylates the carboxyl terminus of the plasma
            membrane Ca(2+)-ATPase from human erythrocytes
  JOURNAL   J Biol Chem 266 (14), 9078-9085 (1991)
   PUBMED   1827443
REFERENCE   8  (residues 1 to 1220)
  AUTHORS   Olson,S., Wang,M.G., Carafoli,E., Strehler,E.E. and McBride,O.W.
  TITLE     Localization of two genes encoding plasma membrane
            Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and
            12q21-23
  JOURNAL   Genomics 9 (4), 629-641 (1991)
   PUBMED   1674727
REFERENCE   9  (residues 1 to 1220)
  AUTHORS   Strehler,E.E., Strehler-Page,M.A., Vogel,G. and Carafoli,E.
  TITLE     mRNAs for plasma membrane calcium pump isoforms differing in their
            regulatory domain are generated by alternative splicing that
            involves two internal donor sites in a single exon
  JOURNAL   Proc Natl Acad Sci U S A 86 (18), 6908-6912 (1989)
   PUBMED   2528729
REFERENCE   10 (residues 1 to 1220)
  AUTHORS   James,P.H., Pruschy,M., Vorherr,T.E., Penniston,J.T. and
            Carafoli,E.
  TITLE     Primary structure of the cAMP-dependent phosphorylation site of the
            plasma membrane calcium pump
  JOURNAL   Biochemistry 28 (10), 4253-4258 (1989)
   PUBMED   2548572
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009522.11, AC068641.18 and
            AC025034.22.
            
            On Jun 4, 2004 this sequence version replaced NP_001673.1.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type primary ion transport ATPases characterized by the formation
            of an aspartyl phosphate intermediate during the reaction cycle.
            These enzymes remove bivalent calcium ions from eukaryotic cells
            against very large concentration gradients and play a critical role
            in intracellular calcium homeostasis. The mammalian plasma membrane
            calcium ATPase isoforms are encoded by at least four separate genes
            and the diversity of these enzymes is further increased by
            alternative splicing of transcripts. The expression of different
            isoforms and splice variants is regulated in a developmental,
            tissue- and cell type-specific manner, suggesting that these pumps
            are functionally adapted to the physiological needs of particular
            cells and tissues. This gene encodes the plasma membrane calcium
            ATPase isoform 1. Alternatively spliced transcript variants
            encoding different isoforms have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks a segment in the coding
            region, which leads to a frameshift, compared to variant 1. The
            resulting isoform (1b) contains a longer and distinct C-terminus
            compared to isoform 1a. Variants 2-5, 16, and 17 all encode the
            same isoform (1b).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1907733.1,
                                           SRR1803611.11819.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.33"
     Protein         1..1220
                     /product="plasma membrane calcium-transporting ATPase 1
                     isoform 1b"
                     /EC_number="7.2.2.10"
                     /note="plasma membrane calcium pump; ATPase, Ca++
                     transporting, plasma membrane 1; plasma membrane
                     calcium-transporting ATPase 1"
                     /calculated_mol_wt=134554
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Region          15..1064
                     /region_name="ATPase-IIB_Ca"
                     /note="plasma-membrane calcium-translocating P-type
                     ATPase; TIGR01517"
                     /db_xref="CDD:273668"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            155..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Region          297..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G5E829; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Site            367..386
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            419..439
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            856..876
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            883..903
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            928..948
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            972..991
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            1006..1027
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            1040..1060
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Region          1100..1117
                     /region_name="Calmodulin-binding subdomain A.
                     /evidence=ECO:0000305|PubMed:1332771"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Region          1103..1149
                     /region_name="ATP_Ca_trans_C"
                     /note="Plasma membrane calcium transporter ATPase C
                     terminal; pfam12424"
                     /db_xref="CDD:463575"
     Site            1116
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000269|PubMed:1827443; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Region          1118..1220
                     /region_name="Required for basolateral membrane targeting.
                     /evidence=ECO:0000250|UniProtKB:P11505"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            1140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11505; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Site            1155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Region          1160..1220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            1165
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Site            1182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P20020.4)"
     CDS             1..1220
                     /gene="ATP2B1"
                     /gene_synonym="MRD66; PMCA1; PMCA1kb"
                     /coded_by="NM_001682.3:370..4032"
                     /note="isoform 1b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9035.1"
                     /db_xref="GeneID:490"
                     /db_xref="HGNC:HGNC:814"
                     /db_xref="MIM:108731"
ORIGIN      
        1 mgdmannsva ysgvknslke anhdgdfgit laelralmel rstdalrkiq esygdvygic
       61 tklktspneg lsgnpadler reavfgknfi ppkkpktflq lvwealqdvt liileiaaiv
      121 slglsfyqpp egdnalcgev svgeeegege tgwiegaail lsvvcvvlvt afndwskekq
      181 frglqsrieq eqkftvirgg qviqipvadi tvgdiaqvky gdllpadgil iqgndlkide
      241 ssltgesdhv kksldkdpll lsgthvmegs grmvvtavgv nsqtgiiftl lgaggeeeek
      301 kdekkkekkn kkqdgaienr nkakaqdgaa memqplksee ggdgdekdkk kanlpkkeks
      361 vlqgkltkla vqigkagllm saitviilvl yfvidtfwvq krpwlaectp iyiqyfvkff
      421 iigvtvlvva vpeglplavt islaysvkkm mkdnnlvrhl dacetmgnat aicsdktgtl
      481 tmnrmtvvqa yinekhykkv pepeaippni lsylvtgisv ncaytskilp pekegglprh
      541 vgnktecall gllldlkrdy qdvrneipee alykvytfns vrksmstvlk nsdgsyrifs
      601 kgaseiilkk cfkilsange akvfrprdrd divktviepm aseglrticl afrdfpagep
      661 epewdnendi vtgltciavv giedpvrpev pdaikkcqra gitvrmvtgd nintaraiat
      721 kcgilhpged flclegkdfn rrirnekgei eqeridkiwp klrvlarssp tdkhtlvkgi
      781 idstvsdqrq vvavtgdgtn dgpalkkadv gfamgiagtd vakeasdiil tddnftsivk
      841 avmwgrnvyd siskflqfql tvnvvaviva ftgacitqds plkavqmlwv nlimdtlasl
      901 alatepptes lllrkpygrn kplisrtmmk nilghafyql vvvftllfag ekffdidsgr
      961 naplhappse hytivfntfv lmqlfneina rkihgernvf egifnnaifc tivlgtfvvq
     1021 iiivqfggkp fscselsieq wlwsiflgmg tllwgqlist iptsrlkflk eaghgtqkee
     1081 ipeeelaedv eeidhaerel rrgqilwfrg lnriqtqirv vnafrsslye glekpesrss
     1141 ihnfmthpef riedsephip liddtdaedd aptkrnsspp pspnknnnav dsgihltiem
     1201 nksatssspg splhsletsl
//
LOCUS       NP_002218               1154 aa            linear   PRI 27-APR-2025
DEFINITION  tyrosine-protein kinase JAK1 isoform 1 [Homo sapiens].
ACCESSION   NP_002218
VERSION     NP_002218.2
DBSOURCE    REFSEQ: accession NM_002227.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1154)
  AUTHORS   Horesh,M.E., Martin-Fernandez,M., Gruber,C., Buta,S., Le Voyer,T.,
            Puzenat,E., Lesmana,H., Wu,Y., Richardson,A., Stein,D., Hodeib,S.,
            Youssef,M., Kurowski,J.A., Feuille,E., Pedroza,L.A., Fuleihan,R.L.,
            Haseley,A., Hovnanian,A., Quartier,P., Rosain,J., Davis,G.,
            Mullan,D., Stewart,O., Patel,R., Lee,A.E., Rubinstein,R., Ewald,L.,
            Maheshwari,N., Rahming,V., Chinn,I.K., Lupski,J.R., Orange,J.S.,
            Sancho-Shimizu,V., Casanova,J.L., Abul-Husn,N.S., Itan,Y.,
            Milner,J.D., Bustamante,J. and Bogunovic,D.
  TITLE     Individuals with JAK1 variants are affected by syndromic features
            encompassing autoimmunity, atopy, colitis, and dermatitis
  JOURNAL   J Exp Med 221 (6) (2024)
   PUBMED   38563820
  REMARK    GeneRIF: Individuals with JAK1 variants are affected by syndromic
            features encompassing autoimmunity, atopy, colitis, and dermatitis.
            Erratum:[J Exp Med. 2024 Jun 3;221(6):e2023238704302024c. doi:
            10.1084/jem.2023238704302024c. PMID: 38709237]
REFERENCE   2  (residues 1 to 1154)
  AUTHORS   Shrestha,H., Radler,P.D., Dennaoui,R., Wicker,M.N., Rajbhandari,N.,
            Sun,Y., Peck,A.R., Vistisen,K., Triplett,A.A., Beydoun,R.,
            Sterneck,E., Saur,D., Rui,H. and Wagner,K.U.
  TITLE     The Janus kinase 1 is critical for pancreatic cancer initiation and
            progression
  JOURNAL   Cell Rep 43 (5), 114202 (2024)
   PUBMED   38733583
  REMARK    GeneRIF: The Janus kinase 1 is critical for pancreatic cancer
            initiation and progression.
REFERENCE   3  (residues 1 to 1154)
  AUTHORS   Yu,Z., Zhang,Q., Wei,S., Zhang,Y., Zhou,T., Zhang,Q., Shi,R.,
            Zinovkin,D., Pranjol,Z.I., Zhang,J. and Wang,H.
  TITLE     CD146+CAFs promote progression of endometrial cancer by inducing
            angiogenesis and vasculogenic mimicry via IL-10/JAK1/STAT3 pathway
  JOURNAL   Cell Commun Signal 22 (1), 170 (2024)
   PUBMED   38459564
  REMARK    GeneRIF: CD146[+]CAFs promote progression of endometrial cancer by
            inducing angiogenesis and vasculogenic mimicry via IL-10/JAK1/STAT3
            pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1154)
  AUTHORS   Cheng,B., Li,L., Luo,T., Wang,Q., Luo,Y., Bai,S., Li,K., Lai,Y. and
            Huang,H.
  TITLE     Single-cell deconvolution algorithms analysis unveils autocrine
            IL11-mediated resistance to docetaxel in prostate cancer via
            activation of the JAK1/STAT4 pathway
  JOURNAL   J Exp Clin Cancer Res 43 (1), 67 (2024)
   PUBMED   38429845
  REMARK    GeneRIF: Single-cell deconvolution algorithms analysis unveils
            autocrine IL11-mediated resistance to docetaxel in prostate cancer
            via activation of the JAK1/STAT4 pathway.
            Erratum:[J Exp Clin Cancer Res. 2024 Dec 28;43(1):333. doi:
            10.1186/s13046-024-03257-8. PMID: 39731134]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1154)
  AUTHORS   Huang,Q., Xiao,Y., Lan,T., Lu,Y., Huang,L. and Zheng,D.
  TITLE     WNT7A promotes tumorigenesis of head and neck squamous cell
            carcinoma via activating FZD7/JAK1/STAT3 signaling
  JOURNAL   Int J Oral Sci 16 (1), 7 (2024)
   PUBMED   38246919
  REMARK    GeneRIF: WNT7A promotes tumorigenesis of head and neck squamous
            cell carcinoma via activating FZD7/JAK1/STAT3 signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1154)
  AUTHORS   Johnston,J.A., Wang,L.M., Hanson,E.P., Sun,X.J., White,M.F.,
            Oakes,S.A., Pierce,J.H. and O'Shea,J.J.
  TITLE     Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of
            insulin receptor substrates 1 and 2 in T cells. Potential role of
            JAK kinases
  JOURNAL   J Biol Chem 270 (48), 28527-28530 (1995)
   PUBMED   7499365
REFERENCE   7  (residues 1 to 1154)
  AUTHORS   Velazquez,L., Fellous,M., Stark,G.R. and Pellegrini,S.
  TITLE     A protein tyrosine kinase in the interferon alpha/beta signaling
            pathway
  JOURNAL   Cell 70 (2), 313-322 (1992)
   PUBMED   1386289
REFERENCE   8  (residues 1 to 1154)
  AUTHORS   Howard,O.M., Dean,M., Young,H., Ramsburg,M., Turpin,J.A.,
            Michiel,D.F., Kelvin,D.J., Lee,L. and Farrar,W.L.
  TITLE     Characterization of a class 3 tyrosine kinase
  JOURNAL   Oncogene 7 (5), 895-900 (1992)
   PUBMED   1373877
REFERENCE   9  (residues 1 to 1154)
  AUTHORS   Pritchard,M.A., Baker,E., Callen,D.F., Sutherland,G.R. and
            Wilks,A.F.
  TITLE     Two members of the JAK family of protein tyrosine kinases map to
            chromosomes 1p31.3 and 9p24
  JOURNAL   Mamm Genome 3 (1), 36-38 (1992)
   PUBMED   1581631
REFERENCE   10 (residues 1 to 1154)
  AUTHORS   Wilks,A.F., Harpur,A.G., Kurban,R.R., Ralph,S.J., Zurcher,G. and
            Ziemiecki,A.
  TITLE     Two novel protein-tyrosine kinases, each with a second
            phosphotransferase-related catalytic domain, define a new class of
            protein kinase
  JOURNAL   Mol Cell Biol 11 (4), 2057-2065 (1991)
   PUBMED   1848670
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL606517.14, BC009079.1,
            AB209057.1 and AC093427.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 26, 2006 this sequence version replaced NP_002218.1.
            
            Summary: This gene encodes a membrane protein that is a member of a
            class of protein-tyrosine kinases (PTK) characterized by the
            presence of a second phosphotransferase-related domain immediately
            N-terminal to the PTK domain. The encoded kinase phosphorylates
            STAT proteins (signal transducers and activators of transcription)
            and plays a key role in interferon-alpha/beta, interferon-gamma,
            and cytokine signal transduction. This gene plays a crucial role in
            effecting the expression of genes that mediate inflammation,
            epithelial remodeling, and metastatic cancer progression. This gene
            is a key component of the interleukin-6 (IL-6)/JAK1/STAT3 immune
            and inflammation response and is a therapeutic target for
            alleviating cytokine storms. The kinase activity of this gene is
            directly inhibited by the suppressor of cytokine signalling 1
            (SOCS1) protein. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2020].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.1147.1,
                                           SRR11853561.958.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: relevant for COVID-19 treatment
            MANE Ensembl match     :: ENST00000342505.5/ ENSP00000343204.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..1154
                     /product="tyrosine-protein kinase JAK1 isoform 1"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase JAK1"
                     /calculated_mol_wt=133147
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P23458.2)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P23458.2)"
     Region          36..129
                     /region_name="FERM_F1"
                     /note="FERM F1 ubiquitin-like domain; pfam18379"
                     /db_xref="CDD:465733"
     Region          147..277
                     /region_name="FERM_F2"
                     /note="FERM F2 acyl-CoA binding protein-like domain;
                     pfam18377"
                     /db_xref="CDD:436450"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P23458.2)"
     Region          282..426
                     /region_name="FERM_C_JAK1"
                     /note="FERM domain C-lobe of Janus kinase 1; cd13332"
                     /db_xref="CDD:275412"
     Site            order(290,322,324,365)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:275412"
     Site            order(369,374..377,406,410,413..414)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:275412"
     Site            406..417
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:275412"
     Region          426..527
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(446,466,497,499)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198173"
     Site            order(498,525)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198173"
     Region          583..846
                     /region_name="PTK_Jak1_rpt1"
                     /note="Pseudokinase (repeat 1) domain of the Protein
                     Tyrosine Kinase, Janus kinase 1; cd05077"
                     /db_xref="CDD:270662"
     Region          870..1153
                     /region_name="PTKc_Jak1_rpt2"
                     /note="Catalytic (repeat 2) domain of the Protein Tyrosine
                     Kinase, Janus kinase 1; cd05079"
                     /db_xref="CDD:173644"
     Site            order(881..884,887..889,906,908,956..959,963,1003,
                     1007..1008,1010,1020..1021,1040..1044,1053,1101)
                     /site_type="active"
                     /db_xref="CDD:173644"
     Site            order(881..884,887..889,906,908,956..959,963,1007..1008,
                     1010,1020..1021)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173644"
     Site            order(1003,1007,1040..1044,1053,1101)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173644"
     Site            1020..1046
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173644"
     Site            1034
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:11909529; propagated from
                     UniProtKB/Swiss-Prot (P23458.2)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:11909529; propagated from
                     UniProtKB/Swiss-Prot (P23458.2)"
     CDS             1..1154
                     /gene="JAK1"
                     /gene_synonym="AIIDE; JAK1A; JAK1B; JTK3"
                     /coded_by="NM_002227.4:295..3759"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41346.1"
                     /db_xref="GeneID:3716"
                     /db_xref="HGNC:HGNC:6190"
                     /db_xref="MIM:147795"
ORIGIN      
        1 mqylnikedc namafcakmr sskktevnle apepgvevif ylsdreplrl gsgeytaeel
       61 ciraaqacri splchnlfal ydentklwya pnrtitvddk mslrlhyrmr fyftnwhgtn
      121 dneqsvwrhs pkkqkngyek kkipdatpll dassleylfa qgqydlvkcl apirdpkteq
      181 dghdienecl gmavlaishy ammkkmqlpe lpkdisykry ipetlnksir qrnlltrmri
      241 nnvfkdflke fnnkticdss vsthdlkvky latletltkh ygaeifetsm llissenemn
      301 wfhsndggnv lyyevmvtgn lgiqwrhkpn vvsvekeknk lkrkklenkh kkdeeknkir
      361 eewnnfsyfp eithivikes vvsinkqdnk kmelklsshe ealsfvslvd gyfrltadah
      421 hylctdvapp livhniqngc hgpicteyai nklrqegsee gmyvlrwsct dfdnilmtvt
      481 cfekseqvqg aqkqfknfqi evqkgryslh gsdrsfpslg dlmshlkkqi lrtdnisfml
      541 krccqpkpre isnllvatkk aqewqpvypm sqlsfdrilk kdlvqgehlg rgtrthiysg
      601 tlmdykddeg tseekkikvi lkvldpshrd islaffeaas mmrqvshkhi vylygvcvrd
      661 venimveefv eggpldlfmh rksdvlttpw kfkvakqlas alsyledkdl vhgnvctknl
      721 llaregidse cgpfiklsdp gipitvlsrq ecieripwia pecvedsknl svaadkwsfg
      781 ttlweicyng eiplkdktli ekerfyesrc rpvtpsckel adlmtrcmny dpnqrpffra
      841 imrdinklee qnpdivsekk patevdpthf ekrflkrird lgeghfgkve lcrydpegdn
      901 tgeqvavksl kpesggnhia dlkkeieilr nlyhenivky kgictedggn giklimeflp
      961 sgslkeylpk nknkinlkqq lkyavqickg mdylgsrqyv hrdlaarnvl vesehqvkig
     1021 dfgltkaiet dkeyytvkdd rdspvfwyap eclmqskfyi asdvwsfgvt lhelltycds
     1081 dsspmalflk migpthgqmt vtrlvntlke gkrlpcppnc pdevyqlmrk cwefqpsnrt
     1141 sfqnliegfe allk
//
LOCUS       NP_689706                420 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 362 [Homo sapiens].
ACCESSION   NP_689706
VERSION     NP_689706.2
DBSOURCE    REFSEQ: accession NM_152493.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Dias Neto,E., Correa,R.G., Verjovski-Almeida,S., Briones,M.R.,
            Nagai,M.A., da Silva,W. Jr., Zago,M.A., Bordin,S., Costa,F.F.,
            Goldman,G.H., Carvalho,A.F., Matsukuma,A., Baia,G.S., Simpson,D.H.,
            Brunstein,A., de Oliveira,P.S., Bucher,P., Jongeneel,C.V.,
            O'Hare,M.J., Soares,F., Brentani,R.R., Reis,L.F., de Souza,S.J. and
            Simpson,A.J.
  TITLE     Shotgun sequencing of the human transcriptome with ORF expressed
            sequence tags
  JOURNAL   Proc Natl Acad Sci U S A 97 (7), 3491-3496 (2000)
   PUBMED   10737800
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL513327.34, BX283663.1, AW204855.1, BF743001.1 and AF318356.1.
            
            On Dec 1, 2003 this sequence version replaced NP_689706.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.245816.1,
                                           SRR14038197.1184211.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000539719.6/ ENSP00000446335.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..420
                     /product="zinc finger protein 362"
                     /note="rotund homolog"
                     /calculated_mol_wt=45684
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T0B9.1)"
     Region          <27..>125
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          54..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T0B9.1)"
     Region          115..155
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T0B9.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5T0B9.1)"
     Region          178..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T0B9.1)"
     Region          229..249
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(229,232,245,249)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          241..266
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          255..277
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          257..277
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(257,260,273,277)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(262,264,266,268..269,272..273,276,290,292,296..297,
                     300..301,304,320,322,324,326..327,330..331,334)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          269..294
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          285..305
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <307..359
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          313..335
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          343..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          375..393
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5T0B9.1)"
     CDS             1..420
                     /gene="ZNF362"
                     /gene_synonym="lin-29; RN"
                     /coded_by="NM_152493.3:252..1514"
                     /db_xref="CCDS:CCDS377.1"
                     /db_xref="GeneID:149076"
                     /db_xref="HGNC:HGNC:18079"
ORIGIN      
        1 msrsspsgkg hsrmaeprfn npyfwppppt mpsqldnlvl inkikeqlma ekirpphlpp
       61 tsassqqpll vppapaessq avmslpklqq vpglhpqavp qpdvalharp atstvtglgl
      121 strtpsvsts essagagtgt gtstpstptt tsqsrliass ptlisgitsp plldsiktiq
      181 ghgllgppks ergrkkikae npggppvlvv pypilasget akegktyrck vcpltfftks
      241 emqihsksht eakphkcphc sksfanasyl aqhlrihlgv kpyhcsycdk sfrqlshlqq
      301 htrihtgdrp ykcphpgcek aftqlsnlqs hqrqhnkdkp ykcpncyray sdsaslqihl
      361 sahaikhaka yccsmcgray tsetylmkhm skhtvvehlv shhspqrtes pgipvrisli
//
LOCUS       NP_114104                490 aa            linear   PRI 27-APR-2025
DEFINITION  tektin-3 [Homo sapiens].
ACCESSION   NP_114104
VERSION     NP_114104.1
DBSOURCE    REFSEQ: accession NM_031898.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Liu,Y., Li,Y., Meng,L., Li,K., Gao,Y., Lv,M., Guo,R., Xu,Y.,
            Zhou,P., Wei,Z., He,X., Cao,Y., Wu,H., Tan,Y. and Hua,R.
  TITLE     Bi-allelic human TEKT3 mutations cause male infertility with
            oligoasthenoteratozoospermia owing to acrosomal hypoplasia and
            reduced progressive motility
  JOURNAL   Hum Mol Genet 32 (10), 1730-1740 (2023)
   PUBMED   36708031
  REMARK    GeneRIF: Bi-allelic human TEKT3 mutations cause male infertility
            with oligoasthenoteratozoospermia owing to acrosomal hypoplasia and
            reduced progressive motility.
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Gui,M., Croft,J.T., Zabeo,D., Acharya,V., Kollman,J.M.,
            Burgoyne,T., Hoog,J.L. and Brown,A.
  TITLE     SPACA9 is a lumenal protein of human ciliary singlet and doublet
            microtubules
  JOURNAL   Proc Natl Acad Sci U S A 119 (41), e2207605119 (2022)
   PUBMED   36191189
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 490)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 490)
  AUTHORS   Roy,A., Yan,W., Burns,K.H. and Matzuk,M.M.
  TITLE     Tektin3 encodes an evolutionarily conserved putative testicular
            microtubules-related protein expressed preferentially in male germ
            cells
  JOURNAL   Mol Reprod Dev 67 (3), 295-302 (2004)
   PUBMED   14735490
REFERENCE   9  (residues 1 to 490)
  AUTHORS   Inoue,K., Dewar,K., Katsanis,N., Reiter,L.T., Lander,E.S.,
            Devon,K.L., Wyman,D.W., Lupski,J.R. and Birren,B.
  TITLE     The 1.4-Mb CMT1A duplication/HNPP deletion genomic region reveals
            unique genome architectural features and provides insights into the
            recent evolution of new genes
  JOURNAL   Genome Res 11 (6), 1018-1033 (2001)
   PUBMED   11381029
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC031688.1 and AF334676.1.
            
            Summary: This gene product belongs to the tektin family of
            proteins. Tektins comprise a family of filament-forming proteins
            that are coassembled with tubulins to form ciliary and flagellar
            microtubules. The exact function of this gene is not known.
            [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.196785.1,
                                           SRR5189667.135257.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395930.6/ ENSP00000379263.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..490
                     /product="tektin-3"
                     /note="testicular microtubules-related protein"
                     /calculated_mol_wt=56505
     Site            7
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXF9.1)"
     Site            9
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXF9.1)"
     Site            10
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXF9.1)"
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXF9.1)"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXF9.1)"
     Region          99..481
                     /region_name="Tektin"
                     /note="Tektin family; pfam03148"
                     /db_xref="CDD:460827"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXF9.1)"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXF9.1)"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXF9.1)"
     Site            344
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXF9.1)"
     CDS             1..490
                     /gene="TEKT3"
                     /gene_synonym="SPGF81"
                     /coded_by="NM_031898.3:144..1616"
                     /db_xref="CCDS:CCDS11169.1"
                     /db_xref="GeneID:64518"
                     /db_xref="HGNC:HGNC:14293"
                     /db_xref="MIM:612683"
ORIGIN      
        1 mervgctltt tyahprptpt nflpaistma ssyrdrfphs nlthslslpw rpstyykvas
       61 nspsvapyct rsqrvsentm lpfvsnrttf ftrytpddwy rsnltnyqes ntsrhnsekl
      121 rvdtsrliqd kyqqtrktqa dttqnlgerv ndigfwksei iheldemige tnaltdvkkr
      181 leralmetea plqvareclf hrekrmgidl vhdeveaqll tevdtilccq ermklhldka
      241 iaqlaanras qhelekdlsd kqtayriddk chhlrntsdg vgyfrgverv datvsvpesw
      301 akftddnilr sqseraasak lrddienllv vtanemwnqf nkvnlsftnr iaetadaknk
      361 iqthlaktlq eifqtemtie sikkaikdkt aflkvaqtrl dertrrpnie lcrdmaqlrl
      421 vnevhevddt iqtlqqrlrd aedtlqslvh ikatleydla vkanslyidq ekcmsmrksy
      481 pntlrlvgfc
//
LOCUS       NP_001129284             221 aa            linear   PRI 27-APR-2025
DEFINITION  SIN3-HDAC complex-associated factor [Homo sapiens].
ACCESSION   NP_001129284
VERSION     NP_001129284.1
DBSOURCE    REFSEQ: accession NM_001135812.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Jhuang,Y.L., Yang,C.W., Tseng,Y.F., Hsu,C.L., Li,H.Y., Yuan,R.H.
            and Jeng,Y.M.
  TITLE     SIN3-HDAC complex-associated factor, a chromatin remodelling gene
            located in the 12p amplicon, is a potential germ cell
            tumour-specific oncogene
  JOURNAL   J Pathol 258 (4), 353-365 (2022)
   PUBMED   36056608
  REMARK    GeneRIF: SIN3-HDAC complex-associated factor, a chromatin
            remodelling gene located in the 12p amplicon, is a potential germ
            cell tumour-specific oncogene.
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Zhang,Y., Li,J.H., Yuan,Q.G. and Yang,W.B.
  TITLE     Restraint of FAM60A has a cancer-inhibiting role in pancreatic
            carcinoma via the effects on the Akt/GSK-3beta/beta-catenin
            signaling pathway
  JOURNAL   Environ Toxicol 37 (6), 1432-1444 (2022)
   PUBMED   35213078
  REMARK    GeneRIF: Restraint of FAM60A has a cancer-inhibiting role in
            pancreatic carcinoma via the effects on the
            Akt/GSK-3beta/beta-catenin signaling pathway.
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Sun,Y.H., Sun,X.W., Yang,L., Cheng,B. and Chen,Y.L.
  TITLE     [Research Progress of FAM60A in the Regulation of Cellular
            Function]
  JOURNAL   Zhongguo Yi Xue Ke Xue Yuan Xue Bao 43 (3), 469-474 (2021)
   PUBMED   34238425
  REMARK    GeneRIF: [Research Progress of FAM60A in the Regulation of Cellular
            Function].
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Joshi,P., Greco,T.M., Guise,A.J., Luo,Y., Yu,F., Nesvizhskii,A.I.
            and Cristea,I.M.
  TITLE     The functional interactome landscape of the human histone
            deacetylase family
  JOURNAL   Mol Syst Biol 9, 672 (2013)
   PUBMED   23752268
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Smith,K.T., Sardiu,M.E., Martin-Brown,S.A., Seidel,C.,
            Mushegian,A., Egidy,R., Florens,L., Washburn,M.P. and Workman,J.L.
  TITLE     Human family with sequence similarity 60 member A (FAM60A) protein:
            a new subunit of the Sin3 deacetylase complex
  JOURNAL   Mol Cell Proteomics 11 (12), 1815-1828 (2012)
   PUBMED   22984288
  REMARK    GeneRIF: studies reveal that loss of FAM60A or another component of
            the Sin3 complex, SDS3, leads to a change in cell morphology and an
            increase in cell migration
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Munoz,I.M., MacArtney,T., Sanchez-Pulido,L., Ponting,C.P., Rocha,S.
            and Rouse,J.
  TITLE     Family with sequence similarity 60A (FAM60A) protein is a cell
            cycle-fluctuating regulator of the SIN3-HDAC1 histone deacetylase
            complex
  JOURNAL   J Biol Chem 287 (39), 32346-32353 (2012)
   PUBMED   22865885
  REMARK    GeneRIF: Family with sequence similarity 60A (FAM60A) protein is a
            cell cycle-fluctuating regulator of the SIN3-HDAC1 histone
            deacetylase complex.
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA741767.1, AK026932.1, DR763430.1 and BC004462.1.
            
            Transcript Variant: This variant (3) lacks a segment in the 5' UTR,
            compared to variant 1. Variants 1, 2, and 3 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026932.1, AF212220.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337682.9/ ENSP00000337477.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.21"
     Protein         1..221
                     /product="SIN3-HDAC complex-associated factor"
                     /note="tera protein homolog; protein FAM60A; family with
                     sequence similarity 60 member A"
                     /calculated_mol_wt=24721
     Region          2..198
                     /region_name="FAM60A"
                     /note="Protein Family FAM60A; pfam15396"
                     /db_xref="CDD:464703"
     Region          112..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP50.1)"
     Region          201..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP50.1)"
     CDS             1..221
                     /gene="SINHCAF"
                     /gene_synonym="C12orf14; FAM60A; L4; TERA"
                     /coded_by="NM_001135812.2:148..813"
                     /db_xref="CCDS:CCDS8723.1"
                     /db_xref="GeneID:58516"
                     /db_xref="HGNC:HGNC:30702"
                     /db_xref="MIM:615027"
ORIGIN      
        1 mfgfhkpkmy rsiegccicr akssssrftd skryekdfqs cfglhetrsg dicnacvllv
       61 krwkklpags kknwnhvvda ragpslkttl kpkkvktlsg nriksnqisk lqkefkrhns
      121 dahsttssas paqspcysnq sddgsdtema sgsnrtpvfs fldltywkrq kiccgiiykg
      181 rfgevlidth lfkpccsnkk aaaekpeeqg peplpistqe w
//
LOCUS       NP_005117                579 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear receptor subfamily 1 group D member 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_005117 XP_945129
VERSION     NP_005117.3
DBSOURCE    REFSEQ: accession NM_005126.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Karuga,F.F., Jaromirska,J., Sochal,M., Bialasiewicz,P. and
            Gabryelska,A.
  TITLE     Association between glucose metabolism, the circadian cycle and
            hypoxia: Evaluation of the NPAS2 and Rev-Erb-alpha protein serum
            levels in obstructive sleep apnea patients - a pilot study
  JOURNAL   Dent Med Probl 61 (3), 465-469 (2024)
   PUBMED   38804230
  REMARK    GeneRIF: Association between glucose metabolism, the circadian
            cycle and hypoxia: Evaluation of the NPAS2 and Rev-Erb-alpha
            protein serum levels in obstructive sleep apnea patients - a pilot
            study.
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Cho,H., Yun,A., Kim,J., Park,E., Jung,J.W., Chung,S. and Son,G.H.
  TITLE     Functional Characterization of Circadian Nuclear Receptors
            REV-ERBalpha and REV-ERBbeta in Human Osteosarcoma Cell Cultures
  JOURNAL   Int J Mol Sci 25 (2), 770 (2024)
   PUBMED   38255844
  REMARK    GeneRIF: Functional Characterization of Circadian Nuclear Receptors
            REV-ERBalpha and REV-ERBbeta in Human Osteosarcoma Cell Cultures.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Hida,A., Iida,A., Ukai,M., Kadotani,H., Uchiyama,M., Ebisawa,T.,
            Inoue,Y., Kitamura,S. and Mishima,K.
  TITLE     Novel CLOCK and NR1D2 variants in 64 sighted Japanese individuals
            with non-24-hour sleep-wake rhythm disorder
  JOURNAL   Sleep 46 (6) (2023)
   PUBMED   36897197
  REMARK    GeneRIF: Novel CLOCK and NR1D2 variants in 64 sighted Japanese
            individuals with non-24-hour sleep-wake rhythm disorder.
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Mittal,N., Davis,C., McLean,P., Calla,J., Godinez-Macias,K.P.,
            Gardner,A., Healey,D., Orjuela-Sanchez,P., Ottilie,S., Chong,Y.,
            Gibson,C. and Winzeler,E.A.
  TITLE     Human nuclear hormone receptor activity contributes to malaria
            parasite liver stage development
  JOURNAL   Cell Chem Biol 30 (5), 486-498 (2023)
   PUBMED   37172592
  REMARK    GeneRIF: Human nuclear hormone receptor activity contributes to
            malaria parasite liver stage development.
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Raza,G.S., Sodum,N., Kaya,Y. and Herzig,K.H.
  TITLE     Role of Circadian Transcription Factor Rev-Erb in Metabolism and
            Tissue Fibrosis
  JOURNAL   Int J Mol Sci 23 (21), 12954 (2022)
   PUBMED   36361737
  REMARK    GeneRIF: Role of Circadian Transcription Factor Rev-Erb in
            Metabolism and Tissue Fibrosis.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Sauve,F., McBroom,L.D., Gallant,J., Moraitis,A.N., Labrie,F. and
            Giguere,V.
  TITLE     CIA, a novel estrogen receptor coactivator with a bifunctional
            nuclear receptor interacting determinant
  JOURNAL   Mol Cell Biol 21 (1), 343-353 (2001)
   PUBMED   11113208
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Koh,Y.S. and Moore,D.D.
  TITLE     Linkage of the nuclear hormone receptor genes NR1D2, THRB, and
            RARB: evidence for an ancient, large-scale duplication
  JOURNAL   Genomics 57 (2), 289-292 (1999)
   PUBMED   10198169
REFERENCE   8  (residues 1 to 579)
  AUTHORS   Burke,L.J., Downes,M., Laudet,V. and Muscat,G.E.
  TITLE     Identification and characterization of a novel corepressor
            interaction region in RVR and Rev-erbA alpha
  JOURNAL   Mol Endocrinol 12 (2), 248-262 (1998)
   PUBMED   9482666
REFERENCE   9  (residues 1 to 579)
  AUTHORS   Downes,M., Burke,L.J., Bailey,P.J. and Muscat,G.E.
  TITLE     Two receptor interaction domains in the corepressor, N-CoR/RIP13,
            are required for an efficient interaction with Rev-erbA alpha and
            RVR: physical association is dependent on the E region of the
            orphan receptors
  JOURNAL   Nucleic Acids Res 24 (22), 4379-4386 (1996)
   PUBMED   8948627
REFERENCE   10 (residues 1 to 579)
  AUTHORS   Dumas,B., Harding,H.P., Choi,H.S., Lehmann,K.A., Chung,M.,
            Lazar,M.A. and Moore,D.D.
  TITLE     A new orphan member of the nuclear hormone receptor superfamily
            closely related to Rev-Erb
  JOURNAL   Mol Endocrinol 8 (8), 996-1005 (1994)
   PUBMED   7997240
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR004486.1, D16815.1,
            AC124914.3 and CA412377.1.
            
            On Feb 26, 2009 this sequence version replaced NP_005117.2.
            
            Summary: This gene encodes a member of the nuclear hormone receptor
            family, specifically the NR1 subfamily of receptors. The encoded
            protein functions as a transcriptional repressor and may play a
            role in circadian rhythms and carbohydrate and lipid metabolism.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.192213.1, BC045613.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312521.9/ ENSP00000310006.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.2"
     Protein         1..579
                     /product="nuclear receptor subfamily 1 group D member 2
                     isoform 1"
                     /note="rev-erb-beta; rev-erba-alpha-related receptor;
                     rev-erb alpha-related receptor; orphan nuclear hormone
                     receptor BD73; V-erbA-related protein 1-related"
                     /calculated_mol_wt=64512
     Region          1..99
                     /region_name="Modulating"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14995.4)"
     Region          1..60
                     /region_name="Required for phosphorylation by CSNK1E and
                     cytoplasmic localization.
                     /evidence=ECO:0000250|UniProtKB:Q60674"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14995.4)"
     Region          13..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14995.4)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q14995.4)"
     Region          98..186
                     /region_name="NR_DBD_REV_ERB"
                     /note="DNA-binding domain of REV-ERB receptor-like is
                     composed of two C4-type zinc fingers; cd07166"
                     /db_xref="CDD:143540"
     Site            order(103,106,120,123,140,146,156,159)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143540"
     Site            order(112..115,121..122,124,126,128..129,153..154,157,160,
                     171,174..180)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143540"
     Site            162
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by KAT5.
                     /evidence=ECO:0000269|PubMed:17996965; propagated from
                     UniProtKB/Swiss-Prot (Q14995.4)"
     Site            163
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by KAT5.
                     /evidence=ECO:0000269|PubMed:17996965; propagated from
                     UniProtKB/Swiss-Prot (Q14995.4)"
     Site            order(171..172,176)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143540"
     Region          222..250
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14995.4)"
     Region          389..577
                     /region_name="NR_LBD_REV_ERB"
                     /note="The ligand binding domain of REV-ERB receptors,
                     members of the nuclear receptor superfamily; cd06940"
                     /db_xref="CDD:132738"
     Region          397..579
                     /region_name="Interaction with ZNHIT1.
                     /evidence=ECO:0000269|PubMed:17892483"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14995.4)"
     Site            order(402,405,409,413,443,446..447,450,454,482..483,486,
                     568,571..572,575)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132738"
     Site            order(492,515..517,526,529..530,551..552,555..556,
                     559..560,562..563,566..567)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:132738"
     CDS             1..579
                     /gene="NR1D2"
                     /gene_synonym="BD73; EAR-1R; REVERBB; REVERBbeta; RVR"
                     /coded_by="NM_005126.5:294..2033"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33718.1"
                     /db_xref="GeneID:9975"
                     /db_xref="HGNC:HGNC:7963"
                     /db_xref="MIM:602304"
ORIGIN      
        1 mevnaggvia yisssssass paschsegse nsfqsssssv psspnssnsd tngnpkngdl
       61 aniegilknd ridcsmktsk ssapgmtksh sgvtkfsgmv llckvcgdva sgfhygvhac
      121 egckgffrrs iqqniqykkc lknencsimr mnrnrcqqcr fkkclsvgms rdavrfgrip
      181 krekqrmlie mqsamktmmn sqfsghlqnd tlvehheqta lpaqeqlrpk pqleqeniks
      241 ssppssdfak eevigmvtra hkdtfmynqe qqensaesmq pqrgeripkn meqynlnhdh
      301 cgnglsshfp csesqqhlng qfkgrnimhy pnghaician ghcmnfsnay tqrvcdrvpi
      361 dgfsqnenkn sylcntggrm hlvcpmsksp yvdphksghe iweefsmsft pavkevvefa
      421 kripgfrdls qhdqvnllka gtfevlmvrf aslfdakert vtflsgkkys vddlhsmgag
      481 dllnsmfefs eklnalqlsd eemslftavv lvsadrsgie nvnsvealqe tliralrtli
      541 mknhpneasi ftklllklpd lrslnnmhse ellafkvhp
//
LOCUS       NP_001106997             614 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 276 isoform a [Homo sapiens].
ACCESSION   NP_001106997
VERSION     NP_001106997.1
DBSOURCE    REFSEQ: accession NM_001113525.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Ohta,S., Bukowski-Wills,J.C., Sanchez-Pulido,L., Alves Fde,L.,
            Wood,L., Chen,Z.A., Platani,M., Fischer,L., Hudson,D.F.,
            Ponting,C.P., Fukagawa,T., Earnshaw,W.C. and Rappsilber,J.
  TITLE     The protein composition of mitotic chromosomes determined using
            multiclassifier combinatorial proteomics
  JOURNAL   Cell 142 (5), 810-821 (2010)
   PUBMED   20813266
REFERENCE   5  (residues 1 to 614)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   6  (residues 1 to 614)
  AUTHORS   Wong,J.C.Y., Gokgoz,N., Alon,N., Andrulis,I.L. and Buchwald,M.
  TITLE     Cloning and mutation analysis of ZFP276 as a candidate tumor
            suppressor in breast cancer
  JOURNAL   J Hum Genet 48 (12), 668-671 (2003)
   PUBMED   14605947
REFERENCE   7  (residues 1 to 614)
  AUTHORS   Wong,J.C., Alon,N., Norga,K., Kruyt,F.A., Youssoufian,H. and
            Buchwald,M.
  TITLE     Cloning and analysis of the mouse Fanconi anemia group A cDNA and
            an overlapping penta zinc finger cDNA
  JOURNAL   Genomics 67 (3), 273-283 (2000)
   PUBMED   10936049
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010538.9, DA891371.1, BC110348.1, BC107603.1, AK096762.1,
            AF354756.1, BC105959.1, BQ432535.1, AK096004.1, BQ549716.1 and
            AI283548.1.
            
            Transcript Variant: This variant (a) encodes the longer isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.208620.1, BC110348.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000443381.7/ ENSP00000415836.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..614
                     /product="zinc finger protein 276 isoform a"
                     /note="zinc finger protein 477; zinc finger, AD-type; zinc
                     finger protein 276 homolog; centromere protein Z"
                     /calculated_mol_wt=67088
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N554.4)"
     Region          78..155
                     /region_name="zf-AD"
                     /note="Zinc-finger associated domain (zf-AD); pfam07776"
                     /db_xref="CDD:462262"
     Region          268..420
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N554.4)"
     Region          <434..519
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          470..490
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(474,476,478,480..481,484..485,489,503,505,509..510,
                     513..514,517,531,533,535,537..538,541..542,545)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          498..518
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          501..>580
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          501..546
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Site            order(503,509,536,545,555,562)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          526..546
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          556..577
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          556..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          583..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N554.4)"
     CDS             1..614
                     /gene="ZNF276"
                     /gene_synonym="CENP-Z; CENPZ; ZADT; ZFP276; ZNF477"
                     /coded_by="NM_001113525.2:105..1949"
                     /note="isoform a is encoded by transcript variant a"
                     /db_xref="CCDS:CCDS45554.1"
                     /db_xref="GeneID:92822"
                     /db_xref="HGNC:HGNC:23330"
                     /db_xref="MIM:608460"
ORIGIN      
        1 mkrdrlgrfl spgssrqcga sdggggvsrt rgrpslsggp rvdgatarra wgpvgscgda
       61 gedgadeaga gralamghcr lchgkfssrs lrsiserapg asmerpsaee rvlvrdfqrl
      121 lgvavrqdpt lspfvcksch aqfyqchsll ksflqrvnas pagrrkpcak vgaqpptgae
      181 egaclvdlit sspqclhglv gwvhghaasc galphlqrtl sseycgviqv vwgcdqghdy
      241 tmdtssscka flldsalavk wpwdketapr lpqhrgwnpg dapqtsqgrg tgtpvgaetk
      301 tlpstdvaqp psdsdavgpr sgfppqpslp lcrapgqlge kqlpsstsdd rvkdefsdls
      361 egdvlseden dkkqnaqssd esfepyperk vsgkkseske akkseeprir kkpgpkpgwk
      421 kklrcereel ptiykcpyqg ctavyrgadg mkkhikehhe evrerpcphp gcnkvfmidr
      481 ylqrhvklih tevrnyicde cgqtfkqrkh llvhqmrhsg akplqcevcg fqcrqraslk
      541 yhmtkhkaet eldfacdqcg rrfekahnln vhmsmvhplt qtqdkalple aepppgppsp
      601 svttegqavk pept
//
LOCUS       NP_056498                407 aa            linear   PRI 27-APR-2025
DEFINITION  arrestin domain-containing protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_056498
VERSION     NP_056498.1
DBSOURCE    REFSEQ: accession NM_015683.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Shea,F.F., Rowell,J.L., Li,Y., Chang,T.H. and Alvarez,C.E.
  TITLE     Mammalian alpha arrestins link activated seven transmembrane
            receptors to Nedd4 family e3 ubiquitin ligases and interact with
            beta arrestins
  JOURNAL   PLoS One 7 (12), e50557 (2012)
   PUBMED   23236378
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF193051.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022516.1, AF193051.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222250.5/ ENSP00000222250.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..407
                     /product="arrestin domain-containing protein 2 isoform 1"
                     /note="arrestin domain-containing protein 2"
                     /calculated_mol_wt=44248
     Region          9..158
                     /region_name="Arrestin_N"
                     /note="Arrestin (or S-antigen), N-terminal domain;
                     pfam00339"
                     /db_xref="CDD:425619"
     Region          181..307
                     /region_name="Arrestin_C"
                     /note="Arrestin (or S-antigen), C-terminal domain;
                     smart01017"
                     /db_xref="CDD:214976"
     CDS             1..407
                     /gene="ARRDC2"
                     /gene_synonym="CLONE24945; PP2703"
                     /coded_by="NM_015683.2:142..1365"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12370.1"
                     /db_xref="GeneID:27106"
                     /db_xref="HGNC:HGNC:25225"
ORIGIN      
        1 mlfdkvkafs vqldgatagv epvfsggqav agrvllelss aarvgalrlr argrahvhwt
       61 esrsagssta ytqsyserve vvshratlla pdtgetttlp pgrheflfsf qlpptlvtsf
      121 egkhgsvryc ikatlhrpwv parrarkvft viepvdintp allapqagar ekvarswycn
      181 rglvslsaki drkgytpgev ipvfaeidng strpvlpraa vvqtqtfmar garkqkravv
      241 aslagepvgp gqralwqgra lrippvgpsi lhcrvlhvdy alkvcvdipg tsklllelpl
      301 vigtiplhpf gsrsssvgsh asflldwrlg alperpeapp eysevvadte eaalgqspfp
      361 lpqdpdmsle gpffayiqef ryrppplyse edpnpllgdm rprcmtc
//
LOCUS       NP_037457                393 aa            linear   PRI 27-APR-2025
DEFINITION  cysteine protease ATG4B isoform a [Homo sapiens].
ACCESSION   NP_037457
VERSION     NP_037457.3
DBSOURCE    REFSEQ: accession NM_013325.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Torres,P., Rico-Rios,S., Ceron-Codorniu,M., Santacreu-Vilaseca,M.,
            Seoane-Miraz,D., Jad,Y., Ayala,V., Marino,G., Beltran,M.,
            Miralles,M.P., Andres-Benito,P., Fernandez-Irigoyen,J.,
            Santamaria,E., Lopez-Otin,C., Soler,R.M., Povedano,M., Ferrer,I.,
            Pamplona,R., Wood,M.J.A., Varela,M.A. and Portero-Otin,M.
  TITLE     TDP-43 regulates LC3ylation in neural tissue through ATG4B cryptic
            splicing inhibition
  JOURNAL   Acta Neuropathol 148 (1), 45 (2024)
   PUBMED   39305312
  REMARK    GeneRIF: TDP-43 regulates LC3ylation in neural tissue through ATG4B
            cryptic splicing inhibition.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Zhang,N., Shen,M.Y., Meng,Q.L., Sun,H.P., Fan,F.Y., Yi,H. and
            Yang,Y.J.
  TITLE     FAT1 inhibits AML autophagy and proliferation via downregulating
            ATG4B expression
  JOURNAL   Biochim Biophys Acta Gen Subj 1868 (1), 130519 (2024)
   PUBMED   37952564
  REMARK    GeneRIF: FAT1 inhibits AML autophagy and proliferation via
            downregulating ATG4B expression.
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Xie,W., Zhang,C., Wang,Z., Chen,H., Gu,T., Zhou,T., Wu,Y., Xia,F.,
            Li,M., Wang,J., Jiao,R., Cui,J. and Jin,S.
  TITLE     ATG4B antagonizes antiviral immunity by GABARAP-directed autophagic
            degradation of TBK1
  JOURNAL   Autophagy 19 (11), 2853-2868 (2023)
   PUBMED   37434364
  REMARK    GeneRIF: ATG4B antagonizes antiviral immunity by GABARAP-directed
            autophagic degradation of TBK1.
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Sathiyaseelan,P., Chittaranjan,S., Kalloger,S.E., Chan,J., Go,N.E.,
            Jardon,M.A., Ho,C.J., Hui,T., Xu,J., Chow,C., Gao,D., Johnson,F.D.,
            Lockwood,W.W., Morin,G.B., Renouf,D.J., Schaeffer,D.F. and
            Gorski,S.M.
  TITLE     Loss of ATG4B and ATG4A results in two-stage cell cycle defects in
            pancreatic ductal adenocarcinoma cells
  JOURNAL   J Cell Sci 136 (19) (2023)
   PUBMED   37701987
  REMARK    GeneRIF: Loss of ATG4B and ATG4A results in two-stage cell cycle
            defects in pancreatic ductal adenocarcinoma cells.
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Sugawara,K., Suzuki,N.N., Fujioka,Y., Mizushima,N., Ohsumi,Y. and
            Inagaki,F.
  TITLE     Structural basis for the specificity and catalysis of human Atg4B
            responsible for mammalian autophagy
  JOURNAL   J Biol Chem 280 (48), 40058-40065 (2005)
   PUBMED   16183633
  REMARK    GeneRIF: analysis of specificity and catalysis of HsAtg4B
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Tanida,I., Ueno,T. and Kominami,E.
  TITLE     Human light chain 3/MAP1LC3B is cleaved at its carboxyl-terminal
            Met121 to expose Gly120 for lipidation and targeting to
            autophagosomal membranes
  JOURNAL   J Biol Chem 279 (46), 47704-47710 (2004)
   PUBMED   15355958
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Tanida,I., Sou,Y.S., Ezaki,J., Minematsu-Ikeguchi,N., Ueno,T. and
            Kominami,E.
  TITLE     HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three
            human Atg8 homologues and delipidates microtubule-associated
            protein light chain 3- and GABAA receptor-associated
            protein-phospholipid conjugates
  JOURNAL   J Biol Chem 279 (35), 36268-36276 (2004)
   PUBMED   15187094
  REMARK    GeneRIF: HsAtg4B negatively regulates the localization of LC3 to a
            membrane compartment by delipidation
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Kabeya,Y., Mizushima,N., Yamamoto,A., Oshitani-Okamoto,S.,
            Ohsumi,Y. and Yoshimori,T.
  TITLE     LC3, GABARAP and GATE16 localize to autophagosomal membrane
            depending on form-II formation
  JOURNAL   J Cell Sci 117 (Pt 13), 2805-2812 (2004)
   PUBMED   15169837
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL080168.1, AK123425.1,
            AK125277.1 and BC000719.2.
            
            On May 12, 2004 this sequence version replaced NP_037457.2.
            
            Summary: Autophagy is the process by which endogenous proteins and
            damaged organelles are destroyed intracellularly. Autophagy is
            postulated to be essential for cell homeostasis and cell remodeling
            during differentiation, metamorphosis, non-apoptotic cell death,
            and aging. Reduced levels of autophagy have been described in some
            malignant tumors, and a role for autophagy in controlling the
            unregulated cell growth linked to cancer has been proposed. This
            gene encodes a member of the autophagin protein family. The encoded
            protein is also designated as a member of the C-54 family of
            cysteine proteases. Alternate transcriptional splice variants,
            encoding different isoforms, have been characterized. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the predominant transcript
            and it encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.449131.1,
                                           SRR1803614.152383.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000404914.8/ ENSP00000384259.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..393
                     /product="cysteine protease ATG4B isoform a"
                     /note="autophagin-1; cysteine protease ATG4B; hAPG4B;
                     AUT-like 1 cysteine endopeptidase; autophagy-related
                     protein 4 homolog B; autophagy-related cysteine
                     endopeptidase 1; APG4 autophagy 4 homolog B; ATG4
                     autophagy related 4 homolog B"
                     /calculated_mol_wt=44163
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.10,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4P1.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1 and PKB/AKT2.
                     /evidence=ECO:0000269|PubMed:29165041,
                     ECO:0000269|PubMed:30443548, ECO:0000269|PubMed:33607258;
                     propagated from UniProtKB/Swiss-Prot (Q9Y4P1.2)"
     Region          39..335
                     /region_name="Peptidase_C54"
                     /note="Peptidase family C54; pfam03416"
                     /db_xref="CDD:460915"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000269|PubMed:28821708; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4P1.2)"
     Region          363..391
                     /region_name="ATG4_LIR"
                     /note="ATG4, F-type LIR motif; pfam20166"
                     /db_xref="CDD:466317"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by STK26.
                     /evidence=ECO:0000269|PubMed:26378241,
                     ECO:0000269|PubMed:29232556, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4P1.2)"
     Region          388..391
                     /region_name="LIR. /evidence=ECO:0000269|PubMed:28287329"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4P1.2)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26378241; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4P1.2)"
     CDS             1..393
                     /gene="ATG4B"
                     /gene_synonym="APG4B; AUTL1; HsAPG4B"
                     /coded_by="NM_013325.5:23..1204"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46564.1"
                     /db_xref="GeneID:23192"
                     /db_xref="HGNC:HGNC:20790"
                     /db_xref="MIM:611338"
ORIGIN      
        1 mdaatltydt lrfaefedfp etsepvwilg rkysiftekd eilsdvasrl wftyrknfpa
       61 iggtgptsdt gwgcmlrcgq mifaqalvcr hlgrdwrwtq rkrqpdsyfs vlnafidrkd
      121 syysihqiaq mgvgegksig qwygpntvaq vlkklavfdt wsslavhiam dntvvmeeir
      181 rlcrtsvpca gatafpadsd rhcngfpaga evtnrpspwr plvlliplrl gltdineayv
      241 etlkhcfmmp qslgviggkp nsahyfigyv geeliyldph ttqpaveptd gcfipdesfh
      301 cqhppcrmsi aeldpsiavg ffckteddfn dwcqqvkkls llggalpmfe lvelqpshla
      361 cpdvlnlsld ssdverlerf fdsededfei lsl
//
LOCUS       NP_001355638             143 aa            linear   PRI 27-APR-2025
DEFINITION  core-binding factor subunit beta isoform 5 [Homo sapiens].
ACCESSION   NP_001355638 XP_016879301
VERSION     NP_001355638.1
DBSOURCE    REFSEQ: accession NM_001368709.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Beyltjens,T., Boudin,E., Revencu,N., Boeckx,N., Bertrand,M.,
            Schutz,L., Haack,T.B., Weber,A., Biliouri,E., Vinksel,M.,
            Zagozen,A., Peterlin,B., Pai,S., Telegrafi,A., Henderson,L.B.,
            Ells,C., Turner,L., Wuyts,W., Van Hul,W., Hendrickx,G. and
            Mortier,G.R.
  TITLE     Heterozygous pathogenic variants involving CBFB cause a new
            skeletal disorder resembling cleidocranial dysplasia
  JOURNAL   J Med Genet 60 (5), 498-504 (2023)
   PUBMED   36241386
  REMARK    GeneRIF: Heterozygous pathogenic variants involving CBFB cause a
            new skeletal disorder resembling cleidocranial dysplasia.
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Malik,N., Kim,Y.I., Yan,H., Tseng,Y.C., du Bois,W., Ayaz,G.,
            Tran,A.D., Vera-Ramirez,L., Yang,H., Michalowski,A.M., Kruhlak,M.,
            Lee,M., Hunter,K.W. and Huang,J.
  TITLE     Dysregulation of Mitochondrial Translation Caused by CBFB
            Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in
            Breast Cancer
  JOURNAL   Cancer Res 83 (8), 1280-1298 (2023)
   PUBMED   36799863
  REMARK    GeneRIF: Dysregulation of Mitochondrial Translation Caused by CBFB
            Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in
            Breast Cancer.
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Khan,A.S., Campbell,K.J., Cameron,E.R. and Blyth,K.
  TITLE     The RUNX/CBFbeta Complex in Breast Cancer: A Conundrum of Context
  JOURNAL   Cells 12 (4), 641 (2023)
   PUBMED   36831308
  REMARK    GeneRIF: The RUNX/CFBbeta Complex in Breast Cancer: A Conundrum of
            Context.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Jiang,Y., Chao,H.Y., Lu,X.Z., Wu,P. and Sun,X.C.
  TITLE     [Molecular Genetic Characteristics of Acute Myeloid Leukemia
            Patients with CBFbeta-MYH11 Positive]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1661-1667 (2022)
   PUBMED   36476886
  REMARK    GeneRIF: [Molecular Genetic Characteristics of Acute Myeloid
            Leukemia Patients with CBFbeta-MYH11 Positive].
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Zhao,C., Wang,S. and Wang,K.
  TITLE     Mutual exclusivity between the fusion gene CBFB::MYH11 and somatic
            mitochondrial mutations in acute myeloid leukaemia
  JOURNAL   Br J Haematol 199 (4), e25-e29 (2022)
   PUBMED   36039018
  REMARK    GeneRIF: Mutual exclusivity between the fusion gene CBFB::MYH11 and
            somatic mitochondrial mutations in acute myeloid leukaemia.
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Chiba,N., Watanabe,T., Nomura,S., Tanaka,Y., Minowa,M., Niki,M.,
            Kanamaru,R. and Satake,M.
  TITLE     Differentiation dependent expression and distinct subcellular
            localization of the protooncogene product, PEBP2beta/CBFbeta, in
            muscle development
  JOURNAL   Oncogene 14 (21), 2543-2552 (1997)
   PUBMED   9191054
REFERENCE   7  (residues 1 to 143)
  AUTHORS   Bae,S.C., Takahashi,E., Zhang,Y.W., Ogawa,E., Shigesada,K.,
            Namba,Y., Satake,M. and Ito,Y.
  TITLE     Cloning, mapping and expression of PEBP2 alpha C, a third gene
            encoding the mammalian Runt domain
  JOURNAL   Gene 159 (2), 245-248 (1995)
   PUBMED   7622058
REFERENCE   8  (residues 1 to 143)
  AUTHORS   Liu,P., Seidel,N., Bodine,D., Speck,N., Tarle,S. and Collins,F.S.
  TITLE     Acute myeloid leukemia with Inv (16) produces a chimeric
            transcription factor with a myosin heavy chain tail
  JOURNAL   Cold Spring Harb Symp Quant Biol 59, 547-553 (1994)
   PUBMED   7587111
REFERENCE   9  (residues 1 to 143)
  AUTHORS   Liu,P., Tarle,S.A., Hajra,A., Claxton,D.F., Marlton,P.,
            Freedman,M., Siciliano,M.J. and Collins,F.S.
  TITLE     Fusion between transcription factor CBF beta/PEBP2 beta and a
            myosin heavy chain in acute myeloid leukemia
  JOURNAL   Science 261 (5124), 1041-1044 (1993)
   PUBMED   8351518
REFERENCE   10 (residues 1 to 143)
  AUTHORS   Muller,C.W. and Schulz,G.E.
  TITLE     Structure of the complex of adenylate kinase from Escherichia coli
            with the inhibitor P1,P5-di(adenosine-5'-)pentaphosphate
  JOURNAL   J Mol Biol 202 (4), 909-912 (1988)
   PUBMED   2845103
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009084.9 and AC074143.5.
            
            On Feb 19, 2019 this sequence version replaced XP_016879301.1.
            
            Summary: The protein encoded by this gene is the beta subunit of a
            heterodimeric core-binding transcription factor belonging to the
            PEBP2/CBF transcription factor family which master-regulates a host
            of genes specific to hematopoiesis (e.g., RUNX1) and osteogenesis
            (e.g., RUNX2). The beta subunit is a non-DNA binding regulatory
            subunit; it allosterically enhances DNA binding by alpha subunit as
            the complex binds to the core site of various enhancers and
            promoters, including murine leukemia virus, polyomavirus enhancer,
            T-cell receptor enhancers and GM-CSF promoters. Alternative
            splicing generates two mRNA variants, each encoding a distinct
            carboxyl terminus. In some cases, a pericentric inversion of
            chromosome 16 [inv(16)(p13q22)] produces a chimeric transcript
            consisting of the N terminus of core-binding factor beta in a
            fusion with the C-terminal portion of the smooth muscle myosin
            heavy chain 11. This chromosomal rearrangement is associated with
            acute myeloid leukemia of the M4Eo subtype. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: Variants 5 and 6 encode isoforms that are the
            same length, but have distinct protein sequences.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3111405.1,
                                           SRR14038192.4125386.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..143
                     /product="core-binding factor subunit beta isoform 5"
                     /note="SL3/AKV core-binding factor beta subunit;
                     polyomavirus enhancer binding protein 2, beta subunit;
                     SL3-3 enhancer factor 1 beta subunit; CBF-beta; PEA2-beta;
                     PEBP2-beta; SL3-3 enhancer factor 1 subunit beta"
                     /calculated_mol_wt=16979
     Region          1..128
                     /region_name="CBF_beta"
                     /note="Core binding factor beta subunit; pfam02312"
                     /db_xref="CDD:396750"
     CDS             1..143
                     /gene="CBFB"
                     /gene_synonym="CLCD2; PEBP2B"
                     /coded_by="NM_001368709.1:260..691"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:865"
                     /db_xref="HGNC:HGNC:1539"
                     /db_xref="MIM:121360"
ORIGIN      
        1 mprvvpdqrs kfeneeffrk lsreceikyt gfrdrpheer qarfqnacrd grseivylka
       61 pmilngvcvi wkgwidlqrl dgmgclefde eraqqedala qqafeearrr trefedrdrs
      121 hreemevrvs qllavtgkkt trp
//
LOCUS       NP_001356421             273 aa            linear   PRI 27-APR-2025
DEFINITION  carabin isoform 3 [Homo sapiens].
ACCESSION   NP_001356421
VERSION     NP_001356421.1
DBSOURCE    REFSEQ: accession NM_001369492.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Qiao,H., Lv,R., Pang,Y., Yao,Z., Zhou,X., Zhu,W. and Zhou,W.
  TITLE     Weighted Gene Coexpression Network Analysis Identifies TBC1D10C as
            a New Prognostic Biomarker for Breast Cancer
  JOURNAL   Anal Cell Pathol (Amst) 2022, 5259187 (2022)
   PUBMED   35425695
  REMARK    GeneRIF: Weighted Gene Coexpression Network Analysis Identifies
            TBC1D10C as a New Prognostic Biomarker for Breast Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Jiang,W., Zhou,X., Li,Z., Liu,K., Wang,W., Tan,R., Cong,X.,
            Shan,J., Zhan,Y., Cui,Z., Jiang,L., Li,Q., Shen,S., Bai,M.,
            Cheng,Y., Li,B., Tan,M., Ma,D.K., Liu,J.O. and Dang,Y.
  TITLE     Prolyl 4-hydroxylase 2 promotes B-cell lymphoma progression via
            hydroxylation of Carabin
  JOURNAL   Blood 131 (12), 1325-1336 (2018)
   PUBMED   29437589
  REMARK    GeneRIF: identify prolyl 4-hydroxylase 2 (P4HA2) as a specific
            proline hydroxylase of Carabin. Carabin hydroxylation leads to its
            proteasomal degradation, thereby activating the Ras/extracellular
            signal-regulated kinase pathway and increasing B-cell lymphoma
            proliferation.
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Schickel,J.N., Pasquali,J.L., Soley,A., Knapp,A.M., Decossas,M.,
            Kern,A., Fauny,J.D., Marcellin,L., Korganow,A.S., Martin,T. and
            Soulas-Sprauel,P.
  TITLE     Carabin deficiency in B cells increases BCR-TLR9
            costimulation-induced autoimmunity
  JOURNAL   EMBO Mol Med 4 (12), 1261-1275 (2012)
   PUBMED   23109291
  REMARK    GeneRIF: Carabin as a new negative regulator of B-cell function,
            whose deficiency in B cells speeds up early B-cell responses
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Hsu,C., Morohashi,Y., Yoshimura,S., Manrique-Hoyos,N., Jung,S.,
            Lauterbach,M.A., Bakhti,M., Gronborg,M., Mobius,W., Rhee,J.,
            Barr,F.A. and Simons,M.
  TITLE     Regulation of exosome secretion by Rab35 and its GTPase-activating
            proteins TBC1D10A-C
  JOURNAL   J Cell Biol 189 (2), 223-232 (2010)
   PUBMED   20404108
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Datta,D., Contreras,A.G., Basu,A., Dormond,O., Flynn,E.,
            Briscoe,D.M. and Pal,S.
  TITLE     Calcineurin inhibitors activate the proto-oncogene Ras and promote
            protumorigenic signals in renal cancer cells
  JOURNAL   Cancer Res 69 (23), 8902-8909 (2009)
   PUBMED   19903851
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Fuchs,E., Haas,A.K., Spooner,R.A., Yoshimura,S., Lord,J.M. and
            Barr,F.A.
  TITLE     Specific Rab GTPase-activating proteins define the Shiga toxin and
            epidermal growth factor uptake pathways
  JOURNAL   J Cell Biol 177 (6), 1133-1143 (2007)
   PUBMED   17562788
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Pan,F., Sun,L., Kardian,D.B., Whartenby,K.A., Pardoll,D.M. and
            Liu,J.O.
  TITLE     Feedback inhibition of calcineurin and Ras by a dual inhibitory
            protein Carabin
  JOURNAL   Nature 445 (7126), 433-436 (2007)
   PUBMED   17230191
  REMARK    GeneRIF: Carabin is a negative feedback inhibitor of the
            calcineurin signalling pathway that also mediates crosstalk between
            calcineurin and Ras
            GeneRIF: Carabin inhibits calcineurin and Ras and was identified by
            a yeast-two-hybrid screen with calcineurin
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003419.3.
            
            Summary: The protein encoded by this gene has an N-terminal
            Rab-GTPase domain and a binding site at the C-terminus for
            calcineurin, and is an inhibitor of both the Ras signaling pathway
            and calcineurin, a phosphatase regulated by calcium and calmodulin.
            Genes encoding similar proteins are located on chromosomes 16 and
            22. Multiple transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, Jan 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.511142.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..273
                     /product="carabin isoform 3"
                     /calculated_mol_wt=28622
     Region          89..>159
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..273
                     /gene="TBC1D10C"
                     /gene_synonym="CARABIN; EPI64C"
                     /coded_by="NM_001369492.1:121..942"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:374403"
                     /db_xref="HGNC:HGNC:24702"
                     /db_xref="MIM:610831"
ORIGIN      
        1 maqalgedlv qppelqddss slgsdselsg pgpyrqadry gfiggssaep gpghppadli
       61 rqremkwvem tshwektmsr rykkvkmqcr kgipsalrar cwpllcgahv cqknspgtyq
      121 elaeapgdpq wmetigrdlh rqfplhemfv spqghgrpsg awcrsvrsts lgttgptwcq
      181 stvpcgadtg apgaghcraa rglpwppgdt gspsshppra aaggglhvtg aqrgavragp
      241 aagdqgpagp aarfragtpa patgpprrgp shl
//
LOCUS       NP_006263                 92 aa            linear   PRI 27-APR-2025
DEFINITION  protein S100-B [Homo sapiens].
ACCESSION   NP_006263
VERSION     NP_006263.1
DBSOURCE    REFSEQ: accession NM_006272.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Shi,H., Zhang,Y., Yang,Y., Zhang,H., Li,W., Zhong,Z. and Lv,L.
  TITLE     Serum S100B protein and white matter changes in schizophrenia
            before and after medication
  JOURNAL   Brain Res Bull 210, 110927 (2024)
   PUBMED   38485004
  REMARK    GeneRIF: Serum S100B protein and white matter changes in
            schizophrenia before and after medication.
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Yan,A.
  TITLE     Application value of serum S100B combined with glucose metabolism
            indexes in predicting adverse pregnancy outcomes of patients with
            severe preeclampsia
  JOURNAL   J Hum Hypertens 38 (3), 232-237 (2024)
   PUBMED   38160207
  REMARK    GeneRIF: Application value of serum S100B combined with glucose
            metabolism indexes in predicting adverse pregnancy outcomes of
            patients with severe preeclampsia.
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Michetti,F., Di Sante,G., Clementi,M.E., Valeriani,F.,
            Mandarano,M., Ria,F., Di Liddo,R., Rende,M. and Romano Spica,V.
  TITLE     The Multifaceted S100B Protein: A Role in Obesity and Diabetes?
  JOURNAL   Int J Mol Sci 25 (2), 776 (2024)
   PUBMED   38255850
  REMARK    GeneRIF: The Multifaceted S100B Protein: A Role in Obesity and
            Diabetes?
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Elhady,M.M., Adly,S.A., Elshebiny,H.A. and Moselhy,S.S.
  TITLE     Detection the severity of organophosphate intoxication using
            sensitive serum biomarkers S100B and amyloid beta (Abeta) in
            Egyptian subjects
  JOURNAL   Environ Sci Pollut Res Int 30 (48), 105194-105201 (2023)
   PUBMED   37713081
  REMARK    GeneRIF: Detection the severity of organophosphate intoxication
            using sensitive serum biomarkers S100B and amyloid beta (Abeta) in
            Egyptian subjects.
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Yue,P., Zhang,L. and Wang,B.
  TITLE     Effects of interventional vascular embolization at different timing
            on prognosis and serum S100 calcium-binding protein B level of
            patients with aneurysmal subarachnoid hemorrhage
  JOURNAL   Afr Health Sci 23 (3), 561-568 (2023)
   PUBMED   38357151
  REMARK    GeneRIF: Effects of interventional vascular embolization at
            different timing on prognosis and serum S100 calcium-binding
            protein B level of patients with aneurysmal subarachnoid
            hemorrhage.
REFERENCE   6  (residues 1 to 92)
  AUTHORS   Morii,K., Tanaka,R., Takahashi,Y., Minoshima,S., Fukuyama,R.,
            Shimizu,N. and Kuwano,R.
  TITLE     Structure and chromosome assignment of human S100 alpha and beta
            subunit genes
  JOURNAL   Biochem Biophys Res Commun 175 (1), 185-191 (1991)
   PUBMED   1998503
  REMARK    Erratum:[Biochem Biophys Res Commun 1991 Jun 14;177(2):894]
REFERENCE   7  (residues 1 to 92)
  AUTHORS   Allore,R.J., Friend,W.C., O'Hanlon,D., Neilson,K.M., Baumal,R.,
            Dunn,R.J. and Marks,A.
  TITLE     Cloning and expression of the human S100 beta gene
  JOURNAL   J Biol Chem 265 (26), 15537-15543 (1990)
   PUBMED   2394738
REFERENCE   8  (residues 1 to 92)
  AUTHORS   Duncan,A.M., Higgins,J., Dunn,R.J., Allore,R. and Marks,A.
  TITLE     Refined sublocalization of the human gene encoding the beta subunit
            of the S100 protein (S100B) and confirmation of a subtle t(9;21)
            translocation using in situ hybridization
  JOURNAL   Cytogenet Cell Genet 50 (4), 234-235 (1989)
   PUBMED   2530061
REFERENCE   9  (residues 1 to 92)
  AUTHORS   Baudier,J. and Cole,R.D.
  TITLE     Interactions between the microtubule-associated tau proteins and
            S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent
            protein kinase II
  JOURNAL   J Biol Chem 263 (12), 5876-5883 (1988)
   PUBMED   2833519
REFERENCE   10 (residues 1 to 92)
  AUTHORS   Allore,R., O'Hanlon,D., Price,R., Neilson,K., Willard,H.F.,
            Cox,D.R., Marks,A. and Dunn,R.J.
  TITLE     Gene encoding the beta subunit of S100 protein is on chromosome 21:
            implications for Down syndrome
  JOURNAL   Science 239 (4845), 1311-1313 (1988)
   PUBMED   2964086
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AA310307.1, BC001766.1,
            EB386131.1 and AP000339.2.
            
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21; however, this gene is
            located at 21q22.3. This protein may function in Neurite extension,
            proliferation of melanoma cells, stimulation of Ca2+ fluxes,
            inhibition of PKC-mediated phosphorylation, astrocytosis and axonal
            proliferation, and inhibition of microtubule assembly. Chromosomal
            rearrangements and altered expression of this gene have been
            implicated in several neurological, neoplastic, and other types of
            diseases, including Alzheimer's disease, Down's syndrome, epilepsy,
            amyotrophic lateral sclerosis, melanoma, and type I diabetes.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.311408.1,
                                           SRR1660807.308821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000291700.9/ ENSP00000291700.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..92
                     /product="protein S100-B"
                     /note="S100 calcium-binding protein, beta (neural); S-100
                     calcium-binding protein, beta chain; S-100 protein subunit
                     beta"
                     /calculated_mol_wt=10582
     Region          2..89
                     /region_name="S-100B"
                     /note="S-100B domain found in proteins similar to S100B.
                     S100B is a calcium-binding protein belonging to a large
                     S100 vertebrate-specific protein family within the EF-hand
                     superfamily of calcium-binding proteins. Note that the
                     S-100 hierarchy, to which this...; cd05027"
                     /db_xref="CDD:240154"
     Site            order(2..5,7..19,26,36,39..41,71..72,74..75,78..80,82..83,
                     87..89)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240154"
     Site            2
                     /site_type="blocked"
                     /note="Blocked amino end (Ser), alternate.
                     /evidence=ECO:0000269|PubMed:4031854; propagated from
                     UniProtKB/Swiss-Prot (P04271.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P02638; propagated from
                     UniProtKB/Swiss-Prot (P04271.2)"
     Site            order(19,22,24,27,32,62,64,66,68,73)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:240154"
     Region          19..32
                     /region_name="Calcium binding region"
     Site            order(43..48,50,52..53,56..57,80..81,84..85,87..88)
                     /site_type="other"
                     /note="NDR kinase binding site [polypeptide binding]"
                     /db_xref="CDD:240154"
     Site            order(47,49,53,56..57,60,72,77,80..81,84..85,87..88)
                     /site_type="active"
                     /note="TRTK-12 binding site [active]"
                     /db_xref="CDD:240154"
     Region          62..73
                     /region_name="Calcium binding region"
     CDS             1..92
                     /gene="S100B"
                     /gene_synonym="NEF; S100; S100-B; S100beta"
                     /coded_by="NM_006272.3:72..350"
                     /db_xref="CCDS:CCDS13736.1"
                     /db_xref="GeneID:6285"
                     /db_xref="HGNC:HGNC:10500"
                     /db_xref="MIM:176990"
ORIGIN      
        1 mselekamva lidvfhqysg regdkhklkk selkelinne lshfleeike qevvdkvmet
       61 ldndgdgecd fqefmafvam vttacheffe he
//
LOCUS       NP_766294               1028 aa            linear   ROD 27-APR-2025
DEFINITION  endosome/lysosome-associated apoptosis and autophagy regulator
            family member 2 isoform 1 precursor [Mus musculus].
ACCESSION   NP_766294
VERSION     NP_766294.2
DBSOURCE    REFSEQ: accession NM_172706.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Araki,T., Kusakabe,M. and Nishida,E.
  TITLE     A transmembrane protein EIG121L is required for epidermal
            differentiation during early embryonic development
  JOURNAL   J Biol Chem 286 (8), 6760-6768 (2011)
   PUBMED   21177533
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158121.12, AC157783.7 and AC157555.9.
            
            On Jul 23, 2006 this sequence version replaced NP_766294.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK133610.1, AK034358.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849387, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 3.69 cM"
     Protein         1..1028
                     /product="endosome/lysosome-associated apoptosis and
                     autophagy regulator family member 2 isoform 1 precursor"
                     /note="estrogen-induced gene 121-like protein; UPF0577
                     protein KIAA1324-like homolog"
                     /calculated_mol_wt=108488
     sig_peptide     1..47
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3UZV7.1)"
                     /calculated_mol_wt=5190
     mat_peptide     48..1028
                     /product="Endosome/lysosome-associated apoptosis and
                     autophagy regulator family member 2. /id=PRO_0000333799"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UZV7.1)"
                     /calculated_mol_wt=108488
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3UZV7.1)"
     Region          286..320
                     /region_name="Ephrin_rec_like"
                     /note="Tyrosine-protein kinase ephrin type A/B
                     receptor-like; pfam07699"
                     /db_xref="CDD:429604"
     Region          401..>431
                     /region_name="Ephrin_rec_like"
                     /note="Tyrosine-protein kinase ephrin type A/B
                     receptor-like; pfam07699"
                     /db_xref="CDD:429604"
     Site            404
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3UZV7.1)"
     Site            690
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3UZV7.1)"
     Site            929..949
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UZV7.1)"
     Site            1017
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A8MWY0; propagated from
                     UniProtKB/Swiss-Prot (Q3UZV7.1)"
     CDS             1..1028
                     /gene="Elapor2"
                     /gene_synonym="9330182L06Rik; Eig121l"
                     /coded_by="NM_172706.4:154..3240"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS19089.1"
                     /db_xref="GeneID:231014"
                     /db_xref="MGI:MGI:2443264"
ORIGIN      
        1 mllltlrrak grdrgrpagg prralslpws pawiccwala gcqavwagds sssgrplpac
       61 qekdyhfeyt ecdstgsrwr vaipnsavdc sglpdpvkgk ectfscasge ylemknqvcs
      121 kcvegtyslg sgikfdewde lpagfsnvat fmdtvvgpsd srpdgcnnss wlprgnyies
      181 nrddctvsli yavhlkksgy vffeyqyvdn niffeffiqn dqcqemdatt dkwvkltdng
      241 ewgshsvmlk sgtnilywrt tgilmgskav kpvlvkniti egvaytsecf pckpgtfsnk
      301 pgsfncqmcp rntysekgak ecirckedsq fseegasecv drppcttkdy fqihtpcdee
      361 gktqimykwi epkicredlt dairlppsge kkdcppcnpg fynngsssch pcppgtfsdg
      421 tkeckscpag tepalgfeyk wwnvlpanmk tscfnvgnsk cdgmngweva gdhirsgagg
      481 sdndylilnl hipgfkppts mtgatgselg ritfvfetlc sadcvlyfmv dinrkstnvv
      541 eswggtkekq aythvifkna tftftwafqr tnqgqdnrrf indvvkiysi tatnavdgva
      601 ascracalgs eqsasscvpc ppghyieket nqckecpadt ylsihqvygk eacipcgpgs
      661 kstqdhslcy sdcffyheke nqtlhydfrn lssvgslmng psftskgtky fhffnislcg
      721 hegrkmalct nnisdftvke mvtgsddytn lvgafvcqst iipseskgfr aalssqsiil
      781 admflgvtvd talqnvnike dmfpvspsqv pdvhffykss tattscingr stavkmrcnp
      841 mrpgagvisv pskcpagtcd gctfyflwes aeacplcteh dfheiegack rglqeilyvw
      901 nepkwcikgi slpekklstc etvdfwlkvg agvgaftavl lvaltcyfwk knqkleykys
      961 klvmttnske celpaadsca imegedneed vvysnkqsll gklkslatke kddhfesvql
     1021 kssrcpni
//
LOCUS       NP_001013404             203 aa            linear   ROD 27-APR-2025
DEFINITION  ras-like protein family member 10B isoform 1 [Mus musculus].
ACCESSION   NP_001013404 XP_205779 XP_907986 XP_912606 XP_925549
VERSION     NP_001013404.1
DBSOURCE    REFSEQ: accession NM_001013386.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Shigesawa,I., Nakamura,A., Yamauchi,Y., Kawata,S., Miyazaki,A.,
            Nomoto,H., Kameda,H., Terauchi,Y. and Atsumi,T.
  TITLE     Effects of glucokinase haploinsufficiency on the pancreatic
            beta-cell mass and function of long-term high-fat, high-sucrose
            diet-fed mice
  JOURNAL   J Diabetes Investig 15 (12), 1732-1742 (2024)
   PUBMED   39305123
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Rybkin,I.I., Kim,M.S., Bezprozvannaya,S., Qi,X., Richardson,J.A.,
            Plato,C.F., Hill,J.A., Bassel-Duby,R. and Olson,E.N.
  TITLE     Regulation of atrial natriuretic peptide secretion by a novel
            Ras-like protein
  JOURNAL   J Cell Biol 179 (3), 527-537 (2007)
   PUBMED   17984325
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL663096.16.
            
            On or before Dec 12, 2005 this sequence version replaced
            XP_205779.5, XP_907986.1, XP_912606.1, XP_925549.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK158941.1, SRR17784646.1293055.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384, SAMN00849390
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 50.3 cM"
     Protein         1..203
                     /product="ras-like protein family member 10B isoform 1"
                     /EC_number="3.6.5.2"
                     /note="ras-like protein family member 10B"
                     /calculated_mol_wt=23098
     Region          1..203
                     /region_name="Small GTPase-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
     mat_peptide     1..200
                     /product="Ras-like protein family member 10B.
                     /id=PRO_0000280801"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
                     /calculated_mol_wt=22914
     Region          5..203
                     /region_name="RRP22"
                     /note="Ras-related protein on chromosome 22 (RRP22)
                     family; cd04142"
                     /db_xref="CDD:133342"
     Site            11..18
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133342"
     Site            order(12..13,61..62)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133342"
     Site            order(13..19,59,62,128..129,131,159..160)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133342"
     Site            order(18..19,33,35,42..43,56..57,59,61..62,161)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133342"
     Region          33..42
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
     Site            order(34..35,40..43)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133342"
     Site            order(34..38,40..42)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133342"
     Site            36
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133342"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133342"
     Site            order(61..62,72..77,84..87)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133342"
     Site            128..131
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133342"
     Site            159..161
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133342"
     Site            200..203
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:133342"
     Site            200
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
     CDS             1..203
                     /gene="Rasl10b"
                     /gene_synonym="B230331P10Rik; Gm729; VTS58635"
                     /coded_by="NM_001013386.3:662..1273"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS25163.1"
                     /db_xref="GeneID:276952"
                     /db_xref="MGI:MGI:2685575"
ORIGIN      
        1 mvstyrvavl gargvgksai vrqflynefs evcvptttrr lylpavvmng hvhdlqildf
       61 ppisafpvnt lqewadaccr glrsvhayil vydiccfdsf eyvktirqqi letrvigtse
      121 tpiiivgnkr dlqrgrvipr wnvshlvrkt wkcgyvecsa kynwhilllf sellksvgca
      181 rckhvhaalr fqgalrrnrc aim
//
LOCUS       NP_001474                286 aa            linear   PRI 27-APR-2025
DEFINITION  protein NipSnap homolog 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001474
VERSION     NP_001474.1
DBSOURCE    REFSEQ: accession NM_001483.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Peng,J., Ma,K., Rong,H., Xiao,B., Zhu,J. and He,J.T.
  TITLE     Knockdown of GBAS regulates esophageal cancer cell viability and
            apoptosis
  JOURNAL   Mol Med Rep 24 (1) (2021)
   PUBMED   34036378
  REMARK    GeneRIF: Knockdown of GBAS regulates esophageal cancer cell
            viability and apoptosis.
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Princely Abudu,Y., Pankiv,S., Mathai,B.J., Hakon Lystad,A.,
            Bindesboll,C., Brenne,H.B., Yoke Wui Ng,M., Thiede,B., Yamamoto,A.,
            Mutugi Nthiga,T., Lamark,T., Esguerra,C.V., Johansen,T. and
            Simonsen,A.
  TITLE     NIPSNAP1 and NIPSNAP2 Act as 'Eat Me' Signals for Mitophagy
  JOURNAL   Dev Cell 49 (4), 509-525 (2019)
   PUBMED   30982665
  REMARK    GeneRIF: NIPSNAP1 and NIPSNAP2 have a redundant function in
            mitophagy and are predominantly expressed in different tissues.
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Hong,M.J., Lee,S.Y., Choi,J.E., Kang,H.G., Do,S.K., Lee,J.H.,
            Yoo,S.S., Lee,E.B., Seok,Y., Cho,S., Jheon,S., Lee,J., Cha,S.I.,
            Kim,C.H. and Park,J.Y.
  TITLE     Intronic variant of EGFR is associated with GBAS expression and
            survival outcome of early-stage non-small cell lung cancer
  JOURNAL   Thorac Cancer 9 (8), 916-923 (2018)
   PUBMED   29806744
  REMARK    GeneRIF: Results show that the rs9642391C>G variant, which is
            located in the intron region of EGFR, is associated with GBAS
            expression and survival outcomes in surgically resected early-stage
            non-small cell lung cancer patients.
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Yamamoto,S., Okamoto,T., Ogasawara,N., Hashimoto,S., Shiraishi,T.,
            Sato,T., Yamamoto,K., Tsutsumi,H., Takano,K., Himi,T., Itoh,H. and
            Yokota,S.I.
  TITLE     NIP-SNAP-1 and -2 mitochondrial proteins are maintained by heat
            shock protein 60
  JOURNAL   Biochem Biophys Res Commun 483 (3), 917-922 (2017)
   PUBMED   28011268
  REMARK    GeneRIF: NIP-SNAP-1 and -2 localized in the mitochondrial inner
            membrane space, whereas HSP60 localized in the matrix. Expression
            levels of NIP-SNAP-1 and -2 in cells were decreased by knockdown of
            HSP60, but not HSP10. The findings indicate that HSP60 promotes
            folding and maintains the stability of NIP-SNAP-1 and -2.
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Martherus,R.S., Sluiter,W., Timmer,E.D., VanHerle,S.J., Smeets,H.J.
            and Ayoubi,T.A.
  TITLE     Functional annotation of heart enriched mitochondrial genes GBAS
            and CHCHD10 through guilt by association
  JOURNAL   Biochem Biophys Res Commun 402 (2), 203-208 (2010)
   PUBMED   20888800
  REMARK    GeneRIF: CHCHD10 and GBAS are involved in oxidative
            phosphorylation.
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Seroussi,E., Pan,H.Q., Kedra,D., Roe,B.A. and Dumanski,J.P.
  TITLE     Characterization of the human NIPSNAP1 gene from 22q12: a member of
            a novel gene family
  JOURNAL   Gene 212 (1), 13-20 (1998)
   PUBMED   9661659
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Wang,X.Y., Smith,D.I., Liu,W. and James,C.D.
  TITLE     GBAS, a novel gene encoding a protein with tyrosine phosphorylation
            sites and a transmembrane domain, is co-amplified with EGFR
  JOURNAL   Genomics 49 (3), 448-451 (1998)
   PUBMED   9615231
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CX166452.1, BC030821.1 and
            BU753659.1.
            
            Summary: This gene encodes a member of the NipSnap family of
            proteins that may be involved in vesicular transport. The encoded
            protein is localized to mitochondria and plays a role in oxidative
            phosphorylation. A pseudogene of this gene is located on the long
            arm of chromosome 2. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene.
            [provided by RefSeq, Feb 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.62888.1,
                                           SRR3476690.323305.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000322090.8/
                                                  ENSP00000313050.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p11.2"
     Protein         1..286
                     /product="protein NipSnap homolog 2 isoform 1"
                     /note="4-nitrophenylphosphatase domain and non-neuronal
                     SNAP25-like 2; protein NipSnap homolog 2; glioblastoma
                     amplified sequence"
                     /calculated_mol_wt=33612
     Region          187..284
                     /region_name="NIPSNAP"
                     /note="pfam07978"
                     /db_xref="CDD:429767"
     CDS             1..286
                     /gene="NIPSNAP2"
                     /gene_synonym="GBAS"
                     /coded_by="NM_001483.3:26..886"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5521.1"
                     /db_xref="GeneID:2631"
                     /db_xref="HGNC:HGNC:4179"
                     /db_xref="MIM:603004"
ORIGIN      
        1 maarvlrarg aawaggllqr aapcsllprl rtwtsssnrs redswlkslf vrkvdprkda
       61 hsnllakket snlyklqfhn vkpecleayn kicqevlpki hedkhypctl vgtwntwyge
      121 qdqavhlwry eggypaltev mnklrenkef lefrkarsdm llsrknqlll efsfwnepvp
      181 rsgpniyelr syqlrpgtmi ewgnywarai rfrqdgneav ggffsqigql ymvhhlwayr
      241 dlqtredirn aawhkhgwee lvyytvpliq emesrimipl ktsplq
//
LOCUS       NP_003722                119 aa            linear   PRI 27-APR-2025
DEFINITION  microtubule nucleation factor SSNA1 [Homo sapiens].
ACCESSION   NP_003722
VERSION     NP_003722.2
DBSOURCE    REFSEQ: accession NM_003731.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Wu,L.W. and Hu,X.
  TITLE     SSNA1 Promotes Hepatocellular Carcinoma Metastasis Via STAT3/EMT
            Induction
  JOURNAL   Anticancer Res 43 (8), 3479-3486 (2023)
   PUBMED   37500134
  REMARK    GeneRIF: SSNA1 Promotes Hepatocellular Carcinoma Metastasis Via
            STAT3/EMT Induction.
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Lawrence,E.J., Arpag,G., Arnaiz,C. and Zanic,M.
  TITLE     SSNA1 stabilizes dynamic microtubules and detects microtubule
            damage
  JOURNAL   Elife 10, e67282 (2021)
   PUBMED   34970964
  REMARK    GeneRIF: SSNA1 stabilizes dynamic microtubules and detects
            microtubule damage.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   7  (residues 1 to 119)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
REFERENCE   8  (residues 1 to 119)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   9  (residues 1 to 119)
  AUTHORS   Ramos-Morales,F., Infante,C., Fedriani,C., Bornens,M. and Rios,R.M.
  TITLE     NA14 is a novel nuclear autoantigen with a coiled-coil domain
  JOURNAL   J Biol Chem 273 (3), 1634-1639 (1998)
   PUBMED   9430706
REFERENCE   10 (residues 1 to 119)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000864.1.
            
            On Jun 10, 2008 this sequence version replaced NP_003722.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.254204.1, BC000864.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322310.10/ ENSP00000313752.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..119
                     /product="microtubule nucleation factor SSNA1"
                     /note="Sjogren's syndrome nuclear autoantigen 1; sjoegren
                     syndrome nuclear autoantigen 1; Sjogren syndrome nuclear
                     autoantigen 1; nuclear autoantigen of 14 kDa"
                     /calculated_mol_wt=13465
     Region          <1..>100
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          2..32
                     /region_name="Important for localization to the
                     centrosome. /evidence=ECO:0000269|PubMed:25390646"
                     /note="propagated from UniProtKB/Swiss-Prot (O43805.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O43805.2)"
     CDS             1..119
                     /gene="SSNA1"
                     /gene_synonym="N14; NA-14; NA14"
                     /coded_by="NM_003731.3:52..411"
                     /db_xref="CCDS:CCDS7034.1"
                     /db_xref="GeneID:8636"
                     /db_xref="HGNC:HGNC:11321"
                     /db_xref="MIM:610882"
ORIGIN      
        1 mtqqgaalqn ynnelvkcie elcqkreelc rqiqeeedek qrlqnevrql teklarvnen
       61 larkiasrne fdrtiaetea aylkilessq tllsvlkrea gnltkatapd qkssggrds
//
LOCUS       NP_038476               1556 aa            linear   PRI 27-APR-2025
DEFINITION  bromodomain adjacent to zinc finger domain protein 1A isoform a
            [Homo sapiens].
ACCESSION   NP_038476
VERSION     NP_038476.2
DBSOURCE    REFSEQ: accession NM_013448.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1556)
  AUTHORS   Siddappa,M., Hussain,S., Wani,S.A., White,J., Tang,H., Gray,J.S.,
            Jafari,H., Wu,H.C., Long,M.D., Elhussin,I., Karanam,B., Wang,H.,
            Morgan,R., Hardiman,G., Adelani,I.B., Rotimi,S.O., Murphy,A.R.,
            Nonn,L., Davis,M.B., Kittles,R.A., Hughes Halbert,C.,
            Sucheston-Campbell,L.E., Yates,C. and Campbell,M.J.
  TITLE     African American Prostate Cancer Displays Quantitatively Distinct
            Vitamin D Receptor Cistrome-transcriptome Relationships Regulated
            by BAZ1A
  JOURNAL   Cancer Res Commun 3 (4), 621-639 (2023)
   PUBMED   37082578
  REMARK    GeneRIF: African American Prostate Cancer Displays Quantitatively
            Distinct Vitamin D Receptor Cistrome-transcriptome Relationships
            Regulated by BAZ1A.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1556)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1556)
  AUTHORS   Li,X., Ding,D., Yao,J., Zhou,B., Shen,T., Qi,Y., Ni,T. and Wei,G.
  TITLE     Chromatin remodeling factor BAZ1A regulates cellular senescence in
            both cancer and normal cells
  JOURNAL   Life Sci 229, 225-232 (2019)
   PUBMED   31085244
  REMARK    GeneRIF: results revealed chromatin remodeling modulator BAZ1A
            acting as a novel regulator of cellular senescence in both normal
            and cancer cells, indicating a new target for potential cancer
            treatment
REFERENCE   4  (residues 1 to 1556)
  AUTHORS   Oppikofer,M., Sagolla,M., Haley,B., Zhang,H.M., Kummerfeld,S.K.,
            Sudhamsu,J., Flynn,E.M., Bai,T., Zhang,J., Ciferri,C. and
            Cochran,A.G.
  TITLE     Non-canonical reader modules of BAZ1A promote recovery from DNA
            damage
  JOURNAL   Nat Commun 8 (1), 862 (2017)
   PUBMED   29021563
  REMARK    GeneRIF: promotes recovery after DNA damage, in part by recruiting
            SMARCA5 to damaged chromatin
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1556)
  AUTHORS   Sun,H., Damez-Werno,D.M., Scobie,K.N., Shao,N.Y., Dias,C.,
            Rabkin,J., Wright,K.N., Mouzon,E., Kabbaj,M., Neve,R., Turecki,G.,
            Shen,L. and Nestler,E.J.
  TITLE     Regulation of BAZ1A and nucleosome positioning in the nucleus
            accumbens in response to cocaine
  JOURNAL   Neuroscience 353, 1-6 (2017)
   PUBMED   28412501
  REMARK    GeneRIF: Results from the study suggest that acute cocaine exposure
            increased Baz1a expression in nucleus accumbens while repeated
            cocaine exposure produced the opposite effect. Findings implicate
            BAZ1A in molecular and behavioral plasticity to cocaine and offer
            new insight into the pathophysiology of cocaine addiction.
REFERENCE   6  (residues 1 to 1556)
  AUTHORS   Collins,N., Poot,R.A., Kukimoto,I., Garcia-Jimenez,C., Dellaire,G.
            and Varga-Weisz,P.D.
  TITLE     An ACF1-ISWI chromatin-remodeling complex is required for DNA
            replication through heterochromatin
  JOURNAL   Nat Genet 32 (4), 627-632 (2002)
   PUBMED   12434153
REFERENCE   7  (residues 1 to 1556)
  AUTHORS   Bozhenok,L., Wade,P.A. and Varga-Weisz,P.
  TITLE     WSTF-ISWI chromatin remodeling complex targets heterochromatic
            replication foci
  JOURNAL   EMBO J 21 (9), 2231-2241 (2002)
   PUBMED   11980720
  REMARK    Erratum:[EMBO J 2002 Jun 17;21(12):3212]
REFERENCE   8  (residues 1 to 1556)
  AUTHORS   Poot,R.A., Dellaire,G., Hulsmann,B.B., Grimaldi,M.A., Corona,D.F.,
            Becker,P.B., Bickmore,W.A. and Varga-Weisz,P.D.
  TITLE     HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1
            and two novel histone-fold proteins
  JOURNAL   EMBO J 19 (13), 3377-3387 (2000)
   PUBMED   10880450
REFERENCE   9  (residues 1 to 1556)
  AUTHORS   Bochar,D.A., Savard,J., Wang,W., Lafleur,D.W., Moore,P., Cote,J.
            and Shiekhattar,R.
  TITLE     A family of chromatin remodeling factors related to Williams
            syndrome transcription factor
  JOURNAL   Proc Natl Acad Sci U S A 97 (3), 1038-1043 (2000)
   PUBMED   10655480
REFERENCE   10 (residues 1 to 1556)
  AUTHORS   Jones,M.H., Hamana,N., Nezu,Ji. and Shimane,M.
  TITLE     A novel family of bromodomain genes
  JOURNAL   Genomics 63 (1), 40-45 (2000)
   PUBMED   10662543
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB032252.1, AF213467.1, AF221130.1, CB217757.1 and AL050089.1.
            
            On Jul 18, 2003 this sequence version replaced NP_038476.1.
            
            Summary: The BAZ1A gene encodes the accessory subunit of the
            ATP-dependent chromatin assembly factor (ACF), a member of the ISWI
            ('imitation switch') family of chromatin remodeling complexes
            (summarized by Racki et al., 2009 [PubMed 20033039]).[supplied by
            OMIM, Apr 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF213467.1, ERR3218370.553944.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360310.6/ ENSP00000353458.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1556
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1-q13.2"
     Protein         1..1556
                     /product="bromodomain adjacent to zinc finger domain
                     protein 1A isoform a"
                     /note="ATP-dependent chromatin remodeling protein;
                     bromodomain adjacent to zinc finger domain protein 1A;
                     hWALp1; CHRAC subunit ACF1; ATP-utilizing chromatin
                     assembly and remodeling factor 1; williams syndrome
                     transcription factor-related chromatin-remodeling factor
                     180"
                     /calculated_mol_wt=178572
     Region          1..133
                     /region_name="Required for interaction with NCOR1.
                     /evidence=ECO:0000269|PubMed:17519354"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Region          1..128
                     /region_name="Required for interaction with the
                     CHRAC1-POLE3 heterodimer. Required for interaction with
                     the CHRAC1-POLE3 heterodimer.
                     /evidence=ECO:0000269|PubMed:14759371"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Region          23..122
                     /region_name="WAC_Acf1_DNA_bd"
                     /note="ATP-utilizing chromatin assembly and remodelling
                     N-terminal; pfam10537"
                     /db_xref="CDD:463140"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Region          422..485
                     /region_name="DDT"
                     /note="domain in different transcription and chromosome
                     remodeling factors; smart00571"
                     /db_xref="CDD:214726"
     Region          590..635
                     /region_name="WHIM1"
                     /note="WSTF, HB1, Itc1p, MBD9 motif 1; pfam15612"
                     /db_xref="CDD:464774"
     Region          <645..788
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          662..754
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Region          667..933
                     /region_name="Required for interaction with SMARCA5 and
                     formation of the CHRAC ISWI chromatin remodeling complex.
                     /evidence=ECO:0000269|PubMed:12434153"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            731
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Region          800..926
                     /region_name="WSD"
                     /note="Williams-Beuren syndrome DDT (WSD), D-TOX E motif;
                     pfam15613"
                     /db_xref="CDD:464775"
     Region          841..877
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Region          941..966
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            960
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88379; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            961
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Region          1150..1195
                     /region_name="PHD_BAZ1A"
                     /note="PHD finger found in bromodomain adjacent to zinc
                     finger domain protein 1A (BAZ1A); cd15627"
                     /db_xref="CDD:277097"
     Site            order(1150,1162..1166,1170,1190)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277097"
     Region          1202..1376
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            1281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            1320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            1339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88379; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            1353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88379; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            1363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            1371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Region          1399..1431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            1402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            1413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Site            1417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NRL2.2)"
     Region          1423..1535
                     /region_name="Bromo_Acf1_like"
                     /note="Bromodomain; Acf1_like or BAZ1A_like subfamily.
                     Bromo adjacent to zinc finger 1A (BAZ1A) was identified as
                     a novel human bromodomain gene by cDNA library screening.
                     The Drosophila homologue, Acf1, is part of the CHRAC
                     (chromatin accessibility complex)...; cd05504"
                     /db_xref="CDD:99936"
     Site            order(1458,1463,1466,1505,1509,1515)
                     /site_type="other"
                     /note="putative acetyllysine binding site [chemical
                     binding]"
                     /db_xref="CDD:99936"
     Site            1547
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL2.2)"
     CDS             1..1556
                     /gene="BAZ1A"
                     /gene_synonym="ACF1; hACF1; WALp1; WCRF180"
                     /coded_by="NM_013448.3:282..4952"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9651.1"
                     /db_xref="GeneID:11177"
                     /db_xref="HGNC:HGNC:960"
                     /db_xref="MIM:605680"
ORIGIN      
        1 mpllhrkpfv rqkppadlrp deevfyckvt neifrhyddf fertilcnsl vwscavtgrp
       61 gltyqeales ekkarqnlqs fpepliipvl yltslthrsr lheicddifa yvkdryfvee
      121 tvevirnnga rlqcrilevl ppshqngfan ghvnsvdget iiisdsddse tqscsfqngk
      181 kkdaidpllf kykvqptkke lhesaivkat qisrrkhlfs rdklklflkq hcepqdgvik
      241 ikasslstyk iaeqdfsyff pddpptfifs panrrrgrpp krihisqedn vankqtlasy
      301 rskatkerdk llkqeemksl afekaklkre kadaleakkk ekedkekkre elkkiveeer
      361 lkkkeekerl kverekerek lreekrkyve ylkqwskpre dmecddlkel peptpvktrl
      421 ppeifgdalm vleflnafge lfdlqdefpd gvtlevleea lvgndsegpl cellffflta
      481 ifqaiaeeee evakeqltda dtkdlteald edadptksal savaslaaaw pqlhqgcslk
      541 sldldsctls eilrlhilas gadvtsanak yryqkrggfd atddacmelr lsnpslvkkl
      601 sstsvydltp gekmkilhal cgklltlvst rdfiedyvdi lrqakqefre lkaeqhrker
      661 eeaaarirkr keeklkeqeq kmkekqeklk edeqrnstad isigeeered fdtsieskdt
      721 eqkeldqdmv tededdpgsh krgrrgkrgq ngfkeftrqe qincvtrepl tadeeealkq
      781 ehqrkekell ekiqsaiact nifplgrdrm yrrywifpsi pglfieedys gltedmllpr
      841 pssfqnnvqs qdpqvstktg eplmsestsn idqgprdhsv qlpkpvhkpn rwcfyssceq
      901 ldqliealns rghresalke tllqeksric aqlarfseek fhfsdkpqpd skptysrgrs
      961 snaydpsqmc aekqlelrlr dflldiedri yqgtlgaikv tdrhiwrsal esgryellse
     1021 enkengiikt vnedveemei deqtkvivkd rllgiktetp stvstnastp qsvssvvhyl
     1081 amalfqieqg ierrflkapl dasdsgrsyk tvldrwresl lssaslsqvf lhlstldrsv
     1141 iwsksilnar ckicrkkgda enmvlcdgcd rghhtycvrp klktvpegdw fcpecrpkqr
     1201 srrlssrqrp slesdedved smggeddevd gdeeegqsee eeyeveqded dsqeeeevsl
     1261 pkrgrpqvrl pvktrgklss sfssrgqqqe pgrypsrsqq stpkttvssk tgrslrkins
     1321 apptetkslr iasrstrhsh gplqadvfve llsprrkrrg rksanntpen spnfpnfrvi
     1381 atksseqsrs vniasklslq eseskrrcrk rqspepspvt lgrrssgrqg gvhelsafeq
     1441 lvvelvrhdd swpflklvsk iqvpdyydii kkpialniir ekvnkceykl asefiddiel
     1501 mfsncfeynp rntseakagt rlqaffhiqa qklglhvtps nvdqvstppa akksri
//
LOCUS       NP_996777                636 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 790 [Homo sapiens].
ACCESSION   NP_996777 XP_371163
VERSION     NP_996777.2
DBSOURCE    REFSEQ: accession NM_206894.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Lamesch,P., Li,N., Milstein,S., Fan,C., Hao,T., Szabo,G., Hu,Z.,
            Venkatesan,K., Bethel,G., Martin,P., Rogers,J., Lawlor,S.,
            McLaren,S., Dricot,A., Borick,H., Cusick,M.E., Vandenhaute,J.,
            Dunham,I., Hill,D.E. and Vidal,M.
  TITLE     hORFeome v3.1: a resource of human open reading frames representing
            over 10,000 human genes
  JOURNAL   Genomics 89 (3), 307-315 (2007)
   PUBMED   17207965
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020928.7, AK297474.1 and BM473790.1.
            
            On Feb 8, 2007 this sequence version replaced NP_996777.1.
            
            Transcript Variant: This variant (1) represents a distinct first
            exon.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297474.1, SRR11853561.14830.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356725.9/ ENSP00000349161.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..636
                     /product="zinc finger protein 790"
                     /calculated_mol_wt=74441
     Region          5..64
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          145..164
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          172..192
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <183..361
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          201..220
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          228..248
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          256..276
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          284..304
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(289,291,293,295..296,299..300,303,317,319,323..324,
                     327..328,331,345,347,349,351..352,355..356,359)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          308..>575
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          312..332
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          340..360
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          368..388
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          396..416
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          424..444
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          452..472
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          480..500
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(485,487,489,491..492,495..496,499,513,515,519..520,
                     523..524,527,541,543,545,547..548,551..552,555)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          508..528
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          536..556
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          564..583
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..636
                     /gene="ZNF790"
                     /coded_by="NM_206894.4:125..2035"
                     /db_xref="CCDS:CCDS12496.1"
                     /db_xref="GeneID:388536"
                     /db_xref="HGNC:HGNC:33114"
ORIGIN      
        1 mahlmmfrdv avdfsqeewe cldleqrdly rdvmlenysn mvslgfciyq peafsllekg
       61 kepwkilrde trgpcpdmqs rcqtkkllpk ngifereiaq leimricknh sldclcfrgd
      121 wegntqfqtl qdnqeecfkq virtcekrpt fnqhtvfnlh qrlntgdkln efkelgkafi
      181 sgsdhtqhql ihtsekfcgd kecgntflpd seviqyqtvh tvkktyecke cgksfslrss
      241 ltghkrihtg ekpfkckdcg kafrfhsqls vhkrihtgek syeckecgka fscgsdltrh
      301 qrihtgekpy ecnecrkafs qrshlikhqr ihtgekpyec kecgkaftrg shltqhqrih
      361 tgekshecke cgkafirgsn laqhqnvhvg rkpykcekcg kayiwsshla rhqrihtgrk
      421 pyeckqcgkt ftwasylaqh ekihnerksy eckecgktfl hgsefnrhqk ihtgernyec
      481 kecgktffrg selnrhqkih tgkrpyecee cgkaflwgsq ltrhqrmhtg eepyvckecg
      541 ksfiwgsqlt rhkkihtdae pygckksshi fshhsyfteq kihnsanlce wtdygntfsh
      601 esnfaqhqni ytfeksyefk dfekafssss hfisll
//
LOCUS       NP_001355729            1556 aa            linear   ROD 27-APR-2025
DEFINITION  band 4.1-like protein 1 isoform f [Mus musculus].
ACCESSION   NP_001355729
VERSION     NP_001355729.1
DBSOURCE    REFSEQ: accession NM_001368800.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1556)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1556)
  AUTHORS   Wang,D., Zhang,L., Hu,A., Wang,Y., Liu,Y., Yang,J., Du,N., An,X.,
            Wu,C. and Liu,C.
  TITLE     Loss of 4.1N in epithelial ovarian cancer results in EMT and
            matrix-detached cell death resistance
  JOURNAL   Protein Cell 12 (2), 107-127 (2021)
   PUBMED   32448967
  REMARK    GeneRIF: Loss of 4.1N in epithelial ovarian cancer results in EMT
            and matrix-detached cell death resistance.
REFERENCE   3  (residues 1 to 1556)
  AUTHORS   Wang,H., Parra,M., Conboy,J.G., Hillyer,C.D., Mohandas,N. and An,X.
  TITLE     Selective effects of protein 4.1N deficiency on neuroendocrine and
            reproductive systems
  JOURNAL   Sci Rep 10 (1), 16947 (2020)
   PUBMED   33046791
  REMARK    GeneRIF: Selective effects of protein 4.1N deficiency on
            neuroendocrine and reproductive systems.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1556)
  AUTHORS   Zhang,X., Chen,M.H., Wu,X., Kodani,A., Fan,J., Doan,R., Ozawa,M.,
            Ma,J., Yoshida,N., Reiter,J.F., Black,D.L., Kharchenko,P.V.,
            Sharp,P.A. and Walsh,C.A.
  TITLE     Cell-Type-Specific Alternative Splicing Governs Cell Fate in the
            Developing Cerebral Cortex
  JOURNAL   Cell 166 (5), 1147-1162 (2016)
   PUBMED   27565344
REFERENCE   5  (residues 1 to 1556)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   6  (residues 1 to 1556)
  AUTHORS   Fukatsu,K., Bannai,H., Zhang,S., Nakamura,H., Inoue,T. and
            Mikoshiba,K.
  TITLE     Lateral diffusion of inositol 1,4,5-trisphosphate receptor type 1
            is regulated by actin filaments and 4.1N in neuronal dendrites
  JOURNAL   J Biol Chem 279 (47), 48976-48982 (2004)
   PUBMED   15364918
REFERENCE   7  (residues 1 to 1556)
  AUTHORS   Zhang,S., Mizutani,A., Hisatsune,C., Higo,T., Bannai,H.,
            Nakayama,T., Hattori,M. and Mikoshiba,K.
  TITLE     Protein 4.1N is required for translocation of inositol
            1,4,5-trisphosphate receptor type 1 to the basolateral membrane
            domain in polarized Madin-Darby canine kidney cells
  JOURNAL   J Biol Chem 278 (6), 4048-4056 (2003)
   PUBMED   12444087
REFERENCE   8  (residues 1 to 1556)
  AUTHORS   Walensky,L.D., Blackshaw,S., Liao,D., Watkins,C.C., Weier,H.U.,
            Parra,M., Huganir,R.L., Conboy,J.G., Mohandas,N. and Snyder,S.H.
  TITLE     A novel neuron-enriched homolog of the erythrocyte membrane
            cytoskeletal protein 4.1
  JOURNAL   J Neurosci 19 (15), 6457-6467 (1999)
   PUBMED   10414974
REFERENCE   9  (residues 1 to 1556)
  AUTHORS   Peters,L.L., Weier,H.U., Walensky,L.D., Snyder,S.H., Parra,M.,
            Mohandas,N. and Conboy,J.G.
  TITLE     Four paralogous protein 4.1 genes map to distinct chromosomes in
            mouse and human
  JOURNAL   Genomics 54 (2), 348-350 (1998)
   PUBMED   9828140
REFERENCE   10 (residues 1 to 1556)
  AUTHORS   Takeuchi,K., Kawashima,A., Nagafuchi,A. and Tsukita,S.
  TITLE     Structural diversity of band 4.1 superfamily members
  JOURNAL   J Cell Sci 107 (Pt 7), 1921-1928 (1994)
   PUBMED   7983158
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL928935.14 and AL929153.11.
            
            Transcript Variant: This variant (8) encodes the longest isoform
            (f).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164131,
                              SAMN01164132 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1556
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 77.39 cM"
     Protein         1..1556
                     /product="band 4.1-like protein 1 isoform f"
                     /note="band 4.1-like protein 1; neuronal protein 4.1;
                     erythrocyte protein band 4.1 like 1"
                     /calculated_mol_wt=169761
     Region          1..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          99..288
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          283..376
                     /region_name="FERM_C_4_1_family"
                     /note="FERM domain C-lobe of Protein 4.1 family; cd13184"
                     /db_xref="CDD:270005"
     Site            order(292,309,311,317)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270005"
     Site            order(321,326..329,364,368,371..372)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18034455; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            364..375
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          385..428
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTP0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          482..540
                     /region_name="Spectrin--actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          492..>523
                     /region_name="SAB"
                     /note="SAB domain; pfam04382"
                     /db_xref="CDD:461285"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4G0; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16452087,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2H5.2)"
     Region          1417..1542
                     /region_name="4_1_CTD"
                     /note="4.1 protein C-terminal domain (CTD); pfam05902"
                     /db_xref="CDD:461774"
     CDS             1..1556
                     /gene="Epb41l1"
                     /gene_synonym="4.1N; Epb4.1l1; mKIAA0338; NBL1"
                     /coded_by="NM_001368800.1:273..4943"
                     /note="isoform f is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS89573.1"
                     /db_xref="GeneID:13821"
                     /db_xref="MGI:MGI:103010"
ORIGIN      
        1 mttetgpdse vkkaqeetpq qpeaaaavtt pvtpaghshp etnsnekhlt qqdtrpaeqs
       61 ldmddkdyse adglserttp skaqkspqki akkfksaicr vtlldaseye cevekhgrgq
      121 vlfdlvcehl nllekdyfgl tycdadsqkn wldpskeikk qirsspwnfa ftvkfyppdp
      181 aqlteditry ylclqlradi itgrlpcsfv thallgsyav qaelgdydae ehvgnyvsel
      241 rfapnqtrel eerimelhkt yrgmtpgeae ihflenakkl smygvdlhha kdsegidiml
      301 gvcanglliy rdrlrinrfa wpkilkisyk rsnfyikirp geyeqfesti gfklpnhrsa
      361 krlwkvcieh htffrlvspe pppkgflvmg skfrysgrtq aqtrqasali drpapffers
      421 sskrytmsrs ldgefsrpas vsenhdagpd gdkreddaes ggrrseaeeg evrtptkike
      481 lkpeqettpr hkqefldkpe dvllkhqasi nelkrtlkep nsklihrdrd wdrerrlpss
      541 paspspkgtp ekasegsehw vliervytrp edlglltvpa tqreesgssl teiladgrls
      601 kvdilvdkfk vevateetvr aqrtstqqqg kmiaspegse tmreedaclr ggprdatraa
      661 gytstdklkl rntrvsngqt eshvelnkgl erpqtwgrlt aagvgpvqge vlspasdkgg
      721 lqsflldpaq tearadssde tdtsfaersf clnygkkdse dsllapslgd reehldappg
      781 dgtwlelaga htenwepkss dprasapgss qnkdeahmas saeeawsprd rgrpddlqgs
      841 avcqtleegw entqglegel aypvadvaed eaptsidwmg ktekksppar wkknppgggg
      901 gggggggggg ggggggggrv hldaqacall rtippcvrkp vrpdqasflp kekgavstha
      961 vepetedrea vtplpassgh tevlaatsls pvpprsgess esrgfirdqs pvilkyihlp
     1021 eespvhkdpq gerkappvas kkprvvpegt egpallglvl psgkletslq drdqggsqed
     1081 vsktsvanki rifethgaep crasqgevrt lpheppseas pgqveerskp rdlgfvqlqp
     1141 pgdlaspkvt cssvmplatq hygeatptts hqerctdpel vspdsgcett leeatgskag
     1201 daggedknsf grlapstpgk ggrlrfaspp glqraglreg seekvkpprp rapesdtgde
     1261 dqdqerdavf lkdnhlaier kcssitvsst ssleaevdft vigdyhggaf edfsrslpel
     1321 drdksdsete glvfardlkg pssqedesgg ledspdrgac stpempqfes vkaetmtvss
     1381 lairkkiepe amlqsrvsaa dstqvdggtp mvkdfmttpp cittetistt menslksgkg
     1441 aaamipgpqt vateirslsp iigkdvltst ygataetlst sttthvtktv kggfsetrie
     1501 kriiitgded vdqdqalala ikeaklqhpd mlvtkavvyr etdpspeerd kkpqes
//
LOCUS       NP_997235                525 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome P450 4V2 [Homo sapiens].
ACCESSION   NP_997235
VERSION     NP_997235.3
DBSOURCE    REFSEQ: accession NM_207352.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Huang,K., Ma,T., Li,Q., Zhong,Z., Zhou,Y., Zhang,W., Qin,T.,
            Tang,S., Zhong,J. and Lu,S.
  TITLE     CYP4V2 rs56413992 C > T was associated with the risk of coronary
            heart disease in the Chinese Han population: a case-control study
  JOURNAL   BMC Med Genomics 16 (1), 322 (2023)
   PUBMED   38066650
  REMARK    GeneRIF: CYP4V2 rs56413992 C > T was associated with the risk of
            coronary heart disease in the Chinese Han population: a
            case-control study.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Hanany,M., Yang,R.R., Lam,C.M., Beryozkin,A., Sundaresan,Y. and
            Sharon,D.
  TITLE     An In-Depth Single-Gene Worldwide Carrier Frequency and Genetic
            Prevalence Analysis of CYP4V2 as the Cause of Bietti Crystalline
            Dystrophy
  JOURNAL   Transl Vis Sci Technol 12 (2), 27 (2023)
   PUBMED   36795063
  REMARK    GeneRIF: An In-Depth Single-Gene Worldwide Carrier Frequency and
            Genetic Prevalence Analysis of CYP4V2 as the Cause of Bietti
            Crystalline Dystrophy.
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Triamchaisri,N., Toochinda,P. and Lawtrakul,L.
  TITLE     Structural Investigation of Beta-Cyclodextrin Complexes with
            Cannabidiol and Delta-9-Tetrahydrocannabinol in 1:1 and 2:1
            Host-Guest Stoichiometry: Molecular Docking and Density Functional
            Calculations
  JOURNAL   Int J Mol Sci 24 (2), 1525 (2023)
   PUBMED   36675035
  REMARK    GeneRIF: Structural Investigation of Beta-Cyclodextrin Complexes
            with Cannabidiol and Delta-9-Tetrahydrocannabinol in 1:1 and 2:1
            Host-Guest Stoichiometry: Molecular Docking and Density Functional
            Calculations.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Long,F., Wang,D., Su,Q., Zhang,Y., Li,J., Xia,S., Wang,H., Wu,Y.
            and Qu,Q.
  TITLE     CYP4 subfamily V member 2 (CYP4V2) polymorphisms were associated
            with ischemic stroke in Chinese Han population
  JOURNAL   BMC Med Genomics 15 (1), 246 (2022)
   PUBMED   36437455
  REMARK    GeneRIF: CYP4 subfamily V member 2 (CYP4V2) polymorphisms were
            associated with ischemic stroke in Chinese Han population.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Li,A., Jiao,X., Munier,F.L., Schorderet,D.F., Yao,W., Iwata,F.,
            Hayakawa,M., Kanai,A., Shy Chen,M., Alan Lewis,R., Heckenlively,J.,
            Weleber,R.G., Traboulsi,E.I., Zhang,Q., Xiao,X., Kaiser-Kupfer,M.,
            Sergeev,Y.V. and Hejtmancik,J.F.
  TITLE     Bietti crystalline corneoretinal dystrophy is caused by mutations
            in the novel gene CYP4V2
  JOURNAL   Am J Hum Genet 74 (5), 817-826 (2004)
   PUBMED   15042513
  REMARK    GeneRIF: Bietti crystalline corneoretinal dystrophy is caused by
            mutations in the novel gene CYP4V2
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   7  (residues 1 to 525)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 525)
  AUTHORS   Jiao,X., Munier,F.L., Iwata,F., Hayakawa,M., Kanai,A., Lee,J.,
            Schorderet,D.F., Chen,M.S., Kaiser-Kupfer,M. and Hejtmancik,J.F.
  TITLE     Genetic linkage of Bietti crystallin corneoretinal dystrophy to
            chromosome 4q35
  JOURNAL   Am J Hum Genet 67 (5), 1309-1313 (2000)
   PUBMED   11001583
REFERENCE   9  (residues 1 to 525)
  AUTHORS   Vargas,M., Mitchell,A., Yang,P. and Weleber,R.
  TITLE     Bietti Crystalline Dystrophy
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22497028
REFERENCE   10 (residues 1 to 525)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY422002.1, BC060857.1,
            AC110771.3 and AA918796.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 13, 2008 this sequence version replaced NP_997235.2.
            
            Summary: This gene encodes a member of the cytochrome P450
            hemethiolate protein superfamily which are involved in oxidizing
            various substrates in the metabolic pathway. It is implicated in
            the metabolism of fatty acid precursors into n-3 polyunsaturated
            fatty acids. Mutations in this gene result in Bietti crystalline
            corneoretinal dystrophy. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.282586.1,
                                           SRR1803614.32044.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378802.5/ ENSP00000368079.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q35.1-q35.2"
     Protein         1..525
                     /product="cytochrome P450 4V2"
                     /EC_number="1.14.14.79"
                     /EC_number="1.14.14.80"
                     /note="docosahexaenoic acid omega-hydroxylase CYP4V2;
                     cytochrome P450, family 4, subfamily V, polypeptide 2;
                     long-chain fatty acid omega-monooxygenase"
                     /calculated_mol_wt=60593
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZWL3.2)"
     Region          76..515
                     /region_name="CYP4V"
                     /note="cytochrome P450 family 4, subfamily V; cd20680"
                     /db_xref="CDD:410773"
     Site            order(118,135..136,143,147,154,326,329..330,333,394,398,
                     459..461,465..469,472..473,477)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410773"
     Site            order(136,328..329,333,397,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:410773"
     CDS             1..525
                     /gene="CYP4V2"
                     /gene_synonym="BCD; CYP4AH1"
                     /coded_by="NM_207352.4:258..1835"
                     /db_xref="CCDS:CCDS34119.1"
                     /db_xref="GeneID:285440"
                     /db_xref="HGNC:HGNC:23198"
                     /db_xref="MIM:608614"
ORIGIN      
        1 maglwlglvw qklllwgaas alslagaslv lsllqrvasy arkwqqmrpi ptvarayplv
       61 ghallmkpdg reffqqiiey teeyrhmpll klwvgpvpmv alynaenvev iltsskqidk
      121 ssmykflepw lglglltstg nkwrsrrkml tptfhftile dfldimneqa nilvkklekh
      181 inqeafncff yitlcaldii cetamgknig aqsnddseyv ravyrmsemi frrikmpwlw
      241 ldlwylmfke gwehkkslqi lhtftnsvia eranemnane dcrgdgrgsa psknkrrafl
      301 dlllsvtdde gnrlshedir eevdtfmfeg hdttaaainw slyllgsnpe vqkkvdheld
      361 dvfgksdrpa tvedlkklry lecviketlr lfpsvplfar svsedcevag yrvlkgteav
      421 iipyalhrdp ryfpnpeefq perffpenaq grhpyayvpf sagprncigq kfavmeekti
      481 lscilrhfwi esnqkreelg legqlilrps ngiwiklkrr nader
//
LOCUS       NP_001356016             372 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001356016 XP_016871780
VERSION     NP_001356016.1
DBSOURCE    REFSEQ: accession NM_001369087.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            On Mar 18, 2019 this sequence version replaced XP_016871780.1.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.198599.1,
                                           SRR1803612.173865.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..372
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 5"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=42098
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..321
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..372
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369087.1:104..1222"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilks fallprleyn daisahcnlc lpgssdspas asqvagitgv
      361 sdaysqslpg ks
//
LOCUS       NP_004798                411 aa            linear   PRI 27-APR-2025
DEFINITION  heparan-sulfate 6-O-sulfotransferase 1 [Homo sapiens].
ACCESSION   NP_004798
VERSION     NP_004798.3
DBSOURCE    REFSEQ: accession NM_004807.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Hu,S., Xia,C., Zou,H., Ren,W., Liu,L., Wang,L., Kang,Q., He,K.,
            Wang,T. and Zhang,X.
  TITLE     HS6ST1 overexpressed in cancer-associated fibroblast and inhibited
            cholangiocarcinoma progression
  JOURNAL   Dig Liver Dis 55 (8), 1114-1125 (2023)
   PUBMED   36586771
  REMARK    GeneRIF: HS6ST1 overexpressed in cancer-associated fibroblast and
            inhibited cholangiocarcinoma progression.
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Howard,S.R., Oleari,R., Poliandri,A., Chantzara,V., Fantin,A.,
            Ruiz-Babot,G., Metherell,L.A., Cabrera,C.P., Barnes,M.R.,
            Wehkalampi,K., Guasti,L., Ruhrberg,C., Cariboni,A. and Dunkel,L.
  TITLE     HS6ST1 Insufficiency Causes Self-Limited Delayed Puberty in
            Contrast With Other GnRH Deficiency Genes
  JOURNAL   J Clin Endocrinol Metab 103 (9), 3420-3429 (2018)
   PUBMED   29931354
  REMARK    GeneRIF: We have linked a deleterious mutation in HS6ST1 to
            familial self-limited delayed puberty and show that heterozygous
            Hs6st1 loss causes delayed puberty in mice. In this study, the
            observed overlap in potentially pathogenic mutations contributing
            to the phenotypes of self-limited delayed puberty and
            hypogonadotropic hypogonadism was limited to this one gene.
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Ushakov,V.S., Tsidulko,A.Y., de La Bourdonnaye,G., Kazanskaya,G.M.,
            Volkov,A.M., Kiselev,R.S., Kobozev,V.V., Kostromskaya,D.V.,
            Gaytan,A.S., Krivoshapkin,A.L., Aidagulova,S.V. and Grigorieva,E.V.
  TITLE     Heparan Sulfate Biosynthetic System Is Inhibited in Human Glioma
            Due to EXT1/2 and HS6ST1/2 Down-Regulation
  JOURNAL   Int J Mol Sci 18 (11), 2301 (2017)
   PUBMED   29104277
  REMARK    GeneRIF: RT-PCR analysis showed that the overall transcriptional
            activity of the main Heparan Sulfate biosynthesis-involved genes
            (EXT1, EXT2, NDST1, NDST2, GLCE, HS2ST1, HS3ST1, HS3ST2, HS6ST1,
            HS6ST2, SULF1, SULF2, HPSE) was decreased by 1.5-2-fold in Grade
            II-III glioma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Cole,C.L., Rushton,G., Jayson,G.C. and Avizienyte,E.
  TITLE     Ovarian cancer cell heparan sulfate 6-O-sulfotransferases regulate
            an angiogenic program induced by heparin-binding epidermal growth
            factor (EGF)-like growth factor/EGF receptor signaling
  JOURNAL   J Biol Chem 289 (15), 10488-10501 (2014)
   PUBMED   24563483
  REMARK    GeneRIF: HS6ST-1 and HS6ST-2 have roles in regulating the
            angiogenic program in ovarian cancer cells affecting HB-EGF
            signaling and subsequent expression of angiogenic cytokines by
            cancer cells
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Wu,J.H., Lemaitre,R.N., Manichaikul,A., Guan,W., Tanaka,T., Foy,M.,
            Kabagambe,E.K., Djousse,L., Siscovick,D., Fretts,A.M., Johnson,C.,
            King,I.B., Psaty,B.M., McKnight,B., Rich,S.S., Chen,Y.D.,
            Nettleton,J.A., Tang,W., Bandinelli,S., Jacobs,D.R. Jr.,
            Browning,B.L., Laurie,C.C., Gu,X., Tsai,M.Y., Steffen,L.M.,
            Ferrucci,L., Fornage,M. and Mozaffarian,D.
  TITLE     Genome-wide association study identifies novel loci associated with
            concentrations of four plasma phospholipid fatty acids in the de
            novo lipogenesis pathway: results from the Cohorts for Heart and
            Aging Research in Genomic Epidemiology (CHARGE) consortium
  JOURNAL   Circ Cardiovasc Genet 6 (2), 171-183 (2013)
   PUBMED   23362303
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Tornberg,J., Sykiotis,G.P., Keefe,K., Plummer,L., Hoang,X.,
            Hall,J.E., Quinton,R., Seminara,S.B., Hughes,V., Van Vliet,G., Van
            Uum,S., Crowley,W.F., Habuchi,H., Kimata,K., Pitteloud,N. and
            Bulow,H.E.
  TITLE     Heparan sulfate 6-O-sulfotransferase 1, a gene involved in
            extracellular sugar modifications, is mutated in patients with
            idiopathic hypogonadotrophic hypogonadism
  JOURNAL   Proc Natl Acad Sci U S A 108 (28), 11524-11529 (2011)
   PUBMED   21700882
  REMARK    GeneRIF: idiopathic hypogonadotrophic hypogonadism--associated
            HS6ST1 mutations display reduced activity in vitro and in vivo,
            suggesting that HS6ST1 and the complex modifications of
            extracellular sugars are critical for normal development
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Habuchi,H., Miyake,G., Nogami,K., Kuroiwa,A., Matsuda,Y.,
            Kusche-Gullberg,M., Habuchi,O., Tanaka,M. and Kimata,K.
  TITLE     Biosynthesis of heparan sulphate with diverse structures and
            functions: two alternatively spliced forms of human heparan
            sulphate 6-O-sulphotransferase-2 having different expression
            patterns and properties
  JOURNAL   Biochem J 371 (Pt 1), 131-142 (2003)
   PUBMED   12492399
  REMARK    GeneRIF: we have characterized HS6ST-2 and HS6ST-1 human isologues,
            including their chromosomal localizations,HS6STs could also
            transfer sulphate to N -sulphoglucosamine residues located at the
            non-reducing terminal of HS with high affinity.
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Habuchi,H., Kobayashi,M. and Kimata,K.
  TITLE     Molecular characterization and expression of heparan-sulfate
            6-sulfotransferase. Complete cDNA cloning in human and partial
            cloning in Chinese hamster ovary cells
  JOURNAL   J Biol Chem 273 (15), 9208-9213 (1998)
   PUBMED   9535912
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Balasubramanian,R. and Crowley,W.F. Jr.
  TITLE     Isolated Gonadotropin-Releasing Hormone (GnRH) Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301509
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC017079.5, DR005030.1,
            BP219645.1, CV569969.1, BC001196.1 and BC063521.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 11, 2007 this sequence version replaced NP_004798.2.
            
            Summary: The protein encoded by this gene is a member of the
            heparan sulfate biosynthetic enzyme family. Heparan sulfate
            biosynthetic enzymes are key components in generating a myriad of
            distinct heparan sulfate fine structures that carry out multiple
            biological activities. This enzyme is a type II integral membrane
            protein and is responsible for 6-O-sulfation of heparan sulfate.
            This enzyme does not share significant sequence similarity with
            other known sulfotransferases. A pseudogene located on chromosome 1
            has been found for this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB006179.1, BC096239.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259241.7/ ENSP00000259241.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..411
                     /product="heparan-sulfate 6-O-sulfotransferase 1"
                     /EC_number="2.8.2.-"
                     /note="heparan-sulfate 6-sulfotransferase; HS6ST-1"
                     /calculated_mol_wt=48095
     Site            18..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60243.5)"
     Region          85..351
                     /region_name="Sulfotransfer_2"
                     /note="Sulfotransferase family; pfam03567"
                     /db_xref="CDD:427369"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60243.5)"
     Site            320
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60243.5)"
     CDS             1..411
                     /gene="HS6ST1"
                     /gene_synonym="HH15; HS6ST"
                     /coded_by="NM_004807.3:306..1541"
                     /db_xref="CCDS:CCDS42748.1"
                     /db_xref="GeneID:9394"
                     /db_xref="HGNC:HGNC:5201"
                     /db_xref="MIM:604846"
ORIGIN      
        1 mrrrraggrt mveraskfvl vvagsvcfml ilyqyagpgl slgapggrap pddldlfptp
       61 dphyekkyyf pvrelerslr fdmkgddviv flhiqktggt tfgrhlvqnv rlevpcdcrp
      121 gqkkctcyrp nrretwlfsr fstgwscglh adwteltncv pgvldrrdsa alrtprkfyy
      181 itllrdpvsr ylsewrhvqr gatwktslhm cdgrtptpee lppcyegtdw sgctlqefmd
      241 cpynlannrq vrmladlslv gcynlsfipe gkraqllles akknlrgmaf fgltefqrkt
      301 qylfertfnl kfirpfmqyn straggvevd edtirrieel ndldmqlydy akdlfqqryq
      361 ykrqlerreq rlrsreerll hrakealpre dadepgrvpt edymshiiek w
//
LOCUS       NP_055692               1942 aa            linear   PRI 27-APR-2025
DEFINITION  probable helicase with zinc finger domain isoform 1 [Homo sapiens].
ACCESSION   NP_055692 XP_375485
VERSION     NP_055692.3
DBSOURCE    REFSEQ: accession NM_014877.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1942)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 1942)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1942)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 1942)
  AUTHORS   Maio,N., Singh,A., Uhrigshardt,H., Saxena,N., Tong,W.H. and
            Rouault,T.A.
  TITLE     Cochaperone binding to LYR motifs confers specificity of iron
            sulfur cluster delivery
  JOURNAL   Cell Metab 19 (3), 445-457 (2014)
   PUBMED   24606901
REFERENCE   5  (residues 1 to 1942)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 1942)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 1942)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1942)
  AUTHORS   Hamamoto,R., Furukawa,Y., Morita,M., Iimura,Y., Silva,F.P., Li,M.,
            Yagyu,R. and Nakamura,Y.
  TITLE     SMYD3 encodes a histone methyltransferase involved in the
            proliferation of cancer cells
  JOURNAL   Nat Cell Biol 6 (8), 731-740 (2004)
   PUBMED   15235609
REFERENCE   9  (residues 1 to 1942)
  AUTHORS   Nagai,H., Yabe,A., Mine,N., Mikami,I., Fujiwara,H., Terada,Y.,
            Hirano,A., Tsuneizumi,M., Yokota,T. and Emi,M.
  TITLE     Down-regulation in human cancers of DRHC, a novel helicase-like
            gene from 17q25.1 that inhibits cell growth
  JOURNAL   Cancer Lett 193 (1), 41-47 (2003)
   PUBMED   12691822
  REMARK    GeneRIF: Results suggest that loss of expression of DRHC may play a
            role in human carcinogenesis.
REFERENCE   10 (residues 1 to 1942)
  AUTHORS   Wagner,D.S., Gan,L. and Klein,W.H.
  TITLE     Identification of a differentially expressed RNA helicase by gene
            trapping
  JOURNAL   Biochem Biophys Res Commun 262 (3), 677-684 (1999)
   PUBMED   10471385
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007448.14 and AC005544.1.
            
            On Nov 23, 2018 this sequence version replaced NP_055692.2.
            
            Summary: HELZ is a member of the superfamily I class of RNA
            helicases. RNA helicases alter the conformation of RNA by unwinding
            double-stranded regions, thereby altering the biologic activity of
            the RNA molecule and regulating access to other proteins (Wagner et
            al., 1999 [PubMed 10471385]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.239143.1,
                                           SRR1660807.108853.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358691.10/ ENSP00000351524.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1942
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..1942
                     /product="probable helicase with zinc finger domain
                     isoform 1"
                     /note="helicase with zinc finger domain; probable helicase
                     with zinc finger domain; down-regulated in human cancers
                     protein"
                     /calculated_mol_wt=218840
     Region          181..205
                     /region_name="zf-CCCH"
                     /note="Zinc finger C-x8-C-x5-C-x3-H type (and similar);
                     pfam00642"
                     /db_xref="CDD:459885"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42694.2)"
     Region          641..867
                     /region_name="DEXXQc_HELZ"
                     /note="DEXXQ-box helicase domain of HELZ; cd18077"
                     /db_xref="CDD:350835"
     Site            order(646,671..676,825,866..867)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350835"
     Region          <765..1074
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
     Region          794..797
                     /region_name="DEAA box"
                     /note="propagated from UniProtKB/Swiss-Prot (P42694.2)"
     Region          1117..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42694.2)"
     Site            1163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42694.2)"
     Site            1245
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P42694.2)"
     Region          1246..1345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42694.2)"
     Region          1386..1429
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42694.2)"
     Region          1527..1552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42694.2)"
     Region          1608..1637
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42694.2)"
     Site            1614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42694.2)"
     Site            1645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42694.2)"
     Region          1729..1779
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42694.2)"
     Site            1738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42694.2)"
     Site            1741
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42694.2)"
     Site            1766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P42694.2)"
     Region          1792..1843
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42694.2)"
     Region          1870..1942
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42694.2)"
     CDS             1..1942
                     /gene="HELZ"
                     /gene_synonym="DHRC; DRHC; HUMORF5"
                     /coded_by="NM_014877.4:181..6009"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42374.1"
                     /db_xref="GeneID:9931"
                     /db_xref="HGNC:HGNC:16878"
                     /db_xref="MIM:606699"
ORIGIN      
        1 medrraeksc eqaceslkrq dyemalkhct eallslgqys madftgpcpl eierikiesl
       61 lyriasflql knyvqadedc rhvlgeglak gedafravlc cmqlkgklqp vstilakslt
      121 geslngmvtk dltrlktlls etetatsnal sgyhvedlde gscngwhfrp pprgitssee
      181 ytlckrfleq gicrygaqct sahsqeelae wqkryasrli klkqqnenkq lsgsymetli
      241 ekwmnslspe kvlseciegv kvehnpdlsv tvstkkshqt wtfaltckpa rmlyrvally
      301 dahrphfsii aisagdsttq vsqevpencq ewiggkmaqn gldhyvykvg iafnteifgt
      361 frqtivfdfg lepvlmqrvm idaastedle ylmhakqqlv ttakrwdsss ktiidfepne
      421 ttdlekslli ryqiplsadq lftqsvldks ltksnyqsrl hdllyieeia qykeiskfnl
      481 kvqlqilasf mltgvsggak yaqngqlfgr fkltetlsed tlagrlvmtk vnavyllpvp
      541 kqklvqtqgt kekvyeatie ektkeyiflr lsrecceeln lrpdcdtqve lqfqlnrlpl
      601 cemhyaldri kdngvlfpdi smtptipwsp nrqwdeqldp rlnakqkeav laittplaiq
      661 lppvliigpy gtgktftlaq avkhilqqqe trilicthsn saadlyikdy lhpyveagnp
      721 qarplrvyfr nrwvktvhpv vhqyclissa hstfqmpqke dilkhrvvvv tlntsqylcq
      781 ldlepgffth illdeaaqam ecetimplal atqntrivla gdhmqlspfv ysefarernl
      841 hvslldrlye hypaefpcri llcenyrshe aiinytself yegklmasgk qpahkdfypl
      901 tfftargedv qeknstafyn naevfevver veelrrkwpv awgklddgsi gvvtpyadqv
      961 friraelrkk rlsdvnverv lnvqgkqfrv lflstvrtrh tckhkqtpik kkeqlledst
     1021 edldygflsn ykllntaitr aqslvavvgd pialcsigrc rkfwerfial chensslhgi
     1081 tfeqikaqle alelkktyvl nplapefipr alrlqhsgst nkqqqsppkg kslhhtqndh
     1141 fqndgivqpn psvlignpir aytpppplgp hpnlgkspsp vqridphtgt silyvpavyg
     1201 gnvvmsvplp vpwtgyqgrf avdpriithq aamaynmnll qthgrgspip yglghhppvt
     1261 igqpqnqhqe kdqheqnrng ksdtnnsgpe inkirtpekk ptepkqvdle snpqnrspes
     1321 rpsvvypstk fprkdnlnpr hinlplpaph aqyaipnrhf hplpqlprpp fpipqqhtll
     1381 nqqqnnlpeq pnqippqpnq vvqqqsqlnq qpqqpppqls payqagpnna ffnsavahrp
     1441 qsppaeavip eqqpppmlqe ghsplraiaq pgpilpshln sfidenpsgl pigealdrih
     1501 gsvaletlrq qqarfqqwse hhaflsqgsa pyphhhhphl qhlpqpplgl hqppvradwk
     1561 ltssaedeve ttysrfqdli relshrdqse trelaemppp qsrllqyrqv qsrsppavps
     1621 ppsstdhssh fsnfndnsrd ievasnpafp qrlppqifns pfslpsehla ppplkylapd
     1681 gawtfanlqq nhlmgpgfpy glpplphrpp qnpfvqiqnh qhaigqepfh plssrtvsss
     1741 slpsleeyep rgpgrplyqr rissssvqpc seevstpqds laqckelqdh snqssfnfss
     1801 peswvnttss tpyqnipcng ssrtaqprel iappktvkpp edqlksenle vsssfnysvl
     1861 qhlgqfpplm pnkqiaesan ssspqssagg kpamsyasal rappkprppp eqakkssdpl
     1921 slfqelslgs ssgsngfysy fk
//
LOCUS       NP_000622                339 aa            linear   PRI 27-APR-2025
DEFINITION  neutrophil cytosol factor 4 isoform 1 [Homo sapiens].
ACCESSION   NP_000622
VERSION     NP_000622.2
DBSOURCE    REFSEQ: accession NM_000631.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Li,L., Mao,R., Yuan,S., Xie,Q., Meng,J., Gu,Y., Tan,S., Xu,X.,
            Gao,C., Liu,H., Ma,C., Man,S.M., Meng,X., Xu,T. and Qi,X.
  TITLE     NCF4 attenuates colorectal cancer progression by modulating
            inflammasome activation and immune surveillance
  JOURNAL   Nat Commun 15 (1), 5170 (2024)
   PUBMED   38886341
  REMARK    GeneRIF: NCF4 attenuates colorectal cancer progression by
            modulating inflammasome activation and immune surveillance.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Liu,X., Shi,Y., Liu,R., Song,K. and Chen,L.
  TITLE     Structure of human phagocyte NADPH oxidase in the activated state
  JOURNAL   Nature 627 (8002), 189-195 (2024)
   PUBMED   38355798
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Azarova,Y.E., Klyosova,E.Y., Ivakin,V.E., Churilin,M.I.,
            Kolomoets,I.I., Sunyaykina,O.A., Ragulina,V.A. and Polonikov,A.V.
  TITLE     Polymorphisms of the NCF4 Gene Increase the Risk of Chronic Heart
            Failure in Patients with Type 2 Diabetes Mellitus
  JOURNAL   Bull Exp Biol Med 176 (1), 77-81 (2023)
   PUBMED   38085396
  REMARK    GeneRIF: Polymorphisms of the NCF4 Gene Increase the Risk of
            Chronic Heart Failure in Patients with Type 2 Diabetes Mellitus.
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Chen,Y., He,F., Wang,R., Yao,M., Li,Y., Guo,D. and He,S.
  TITLE     NCF1/2/4 Are Prognostic Biomarkers Related to the Immune
            Infiltration of Kidney Renal Clear Cell Carcinoma
  JOURNAL   Biomed Res Int 2021, 5954036 (2021)
   PUBMED   34708124
  REMARK    GeneRIF: NCF1/2/4 Are Prognostic Biomarkers Related to the Immune
            Infiltration of Kidney Renal Clear Cell Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Zhang,T.P., Li,R., Huang,Q., Pan,H.F., Ye,D.Q. and Li,X.M.
  TITLE     Association of NCF2, NCF4, and CYBA Gene Polymorphisms with
            Rheumatoid Arthritis in a Chinese Population
  JOURNAL   J Immunol Res 2020, 8528976 (2020)
   PUBMED   33145364
  REMARK    GeneRIF: Association of NCF2, NCF4, and CYBA Gene Polymorphisms
            with Rheumatoid Arthritis in a Chinese Population.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Leto,T.L., Adams,A.G. and de Mendez,I.
  TITLE     Assembly of the phagocyte NADPH oxidase: binding of Src homology 3
            domains to proline-rich targets
  JOURNAL   Proc Natl Acad Sci U S A 91 (22), 10650-10654 (1994)
   PUBMED   7938008
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Tsunawaki,S., Mizunari,H., Nagata,M., Tatsuzawa,O. and Kuratsuji,T.
  TITLE     A novel cytosolic component, p40phox, of respiratory burst oxidase
            associates with p67phox and is absent in patients with chronic
            granulomatous disease who lack p67phox
  JOURNAL   Biochem Biophys Res Commun 199 (3), 1378-1387 (1994)
   PUBMED   8147882
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Wientjes,F.B., Hsuan,J.J., Totty,N.F. and Segal,A.W.
  TITLE     p40phox, a third cytosolic component of the activation complex of
            the NADPH oxidase to contain src homology 3 domains
  JOURNAL   Biochem J 296 (Pt 3) (Pt 3), 557-561 (1993)
   PUBMED   8280052
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Leiding,J.W. and Holland,S.M.
  TITLE     Chronic Granulomatous Disease
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22876374
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Jones,J.H.
  TITLE     The essence of operating room nursing. Paramedical personnel
  JOURNAL   Australas Nurses J 7 (1), 44-45 (1977)
   PUBMED   243433
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC002798.1, BX355636.2 and
            BU076892.1.
            
            On May 19, 2004 this sequence version replaced NP_000622.1.
            
            Summary: The protein encoded by this gene is a cytosolic regulatory
            component of the superoxide-producing phagocyte NADPH-oxidase, a
            multicomponent enzyme system important for host defense. This
            protein is preferentially expressed in cells of myeloid lineage. It
            interacts primarily with neutrophil cytosolic factor 2
            (NCF2/p67-phox) to form a complex with neutrophil cytosolic factor
            1 (NCF1/p47-phox), which further interacts with the small G protein
            RAC1 and translocates to the membrane upon cell stimulation. This
            complex then activates flavocytochrome b, the membrane-integrated
            catalytic core of the enzyme system. The PX domain of this protein
            can bind phospholipid products of the PI(3) kinase, which suggests
            its role in PI(3) kinase-mediated signaling events. The
            phosphorylation of this protein was found to negatively regulate
            the enzyme activity. Alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) lacks an internal coding
            segment compared to variant 2, which leads to a translation
            frameshift. The resulting isoform (1) has a distinct and shorter
            C-terminus, as compared to isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.936687.1,
                                           SRR3476690.958705.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248899.11/ ENSP00000248899.6
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..339
                     /product="neutrophil cytosol factor 4 isoform 1"
                     /note="neutrophil NADPH oxidase factor 4; neutrophil
                     cytosol factor 4; NCF-4; p40-phox; SH3 and PX
                     domain-containing protein 4; neutrophil cytosolic factor
                     4, 40kDa"
                     /calculated_mol_wt=38901
     Region          19..141
                     /region_name="PX_p40phox"
                     /note="The phosphoinositide binding Phox Homology domain
                     of the p40phox subunit of NADPH oxidase; cd06882"
                     /db_xref="CDD:132792"
     Site            order(33,35..36,38,60,138,141)
                     /site_type="other"
                     /note="PB1 domain interface [polypeptide binding]"
                     /db_xref="CDD:132792"
     Site            order(58..60,92..93,105)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132792"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:9804763; propagated from
                     UniProtKB/Swiss-Prot (Q15080.2)"
     Region          174..227
                     /region_name="SH3_p40phox"
                     /note="Src Homology 3 domain of the p40phox subunit of
                     NADPH oxidase; cd11869"
                     /db_xref="CDD:212802"
     Site            order(179..180,184,188,203..204,206..207,220,223)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212802"
     Site            order(200,213..214,216)
                     /site_type="other"
                     /note="PB1 domain interface [polypeptide binding]"
                     /db_xref="CDD:212802"
     Region          238..329
                     /region_name="PB1_P40"
                     /note="The PB1 domain is essential part of the p40 adaptor
                     protein which plays an important role in activating
                     phagocyte NADPH oxidase during phagocytosis. The PB1
                     domain is a modular domain mediating specific
                     protein-protein interaction which play a role in...;
                     cd06399"
                     /db_xref="CDD:99721"
     Site            order(257,265,273,320,322)
                     /site_type="active"
                     /note="hydrophobic pocket [active]"
                     /db_xref="CDD:99721"
     Site            order(289,291,293,302)
                     /site_type="other"
                     /note="PB1 interaction site [polypeptide binding]"
                     /db_xref="CDD:99721"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9804763; propagated from
                     UniProtKB/Swiss-Prot (Q15080.2)"
     CDS             1..339
                     /gene="NCF4"
                     /gene_synonym="CGD3; NCF; P40PHOX; SH3PXD4"
                     /coded_by="NM_000631.5:167..1186"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13934.1"
                     /db_xref="GeneID:4689"
                     /db_xref="HGNC:HGNC:7662"
                     /db_xref="MIM:601488"
ORIGIN      
        1 mavaqqlrae sdfeqlpddv aisaniadie ekrgftshfv fvievktkgg skyliyrryr
       61 qfhalqskle erfgpdskss alactlptlp akvyvgvkqe iaemripaln aymksllslp
      121 vwvlmdedvr iffyqspyds eqvpqalrrl rprtrkvksv spqgnsvdrm aapraealfd
      181 ftgnskleln fkagdvifll srinkdwleg tvrgatgifp lsfvkilkdf peeddptnwl
      241 rcyyyedtis tikdiaveed lsstpllkdl leltrrefqr edialnyrda egdlvrllsd
      301 edvalmvrqa rglpsqkrlf pwklhitqkd nyrvyntmp
//
LOCUS       NP_001010853             436 aa            linear   PRI 27-APR-2025
DEFINITION  xaa-Arg dipeptidase [Homo sapiens].
ACCESSION   NP_001010853 XP_072402
VERSION     NP_001010853.1
DBSOURCE    REFSEQ: accession NM_001010853.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Veiga-da-Cunha,M., Chevalier,N., Stroobant,V., Vertommen,D. and Van
            Schaftingen,E.
  TITLE     Metabolite proofreading in carnosine and homocarnosine synthesis:
            molecular identification of PM20D2 as beta-alanyl-lysine
            dipeptidase
  JOURNAL   J Biol Chem 289 (28), 19726-19736 (2014)
   PUBMED   24891507
  REMARK    GeneRIF: PM20D2 hydrolyzed beta-alanyl-lysine,
            beta-alanyl-ornithine, gamma-aminobutyryl-lysine, and
            gamma-aminobutyryl-ornithine as its best substrates.
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Shin,S.Y., Fauman,E.B., Petersen,A.K., Krumsiek,J., Santos,R.,
            Huang,J., Arnold,M., Erte,I., Forgetta,V., Yang,T.P., Walter,K.,
            Menni,C., Chen,L., Vasquez,L., Valdes,A.M., Hyde,C.L., Wang,V.,
            Ziemek,D., Roberts,P., Xi,L., Grundberg,E., Waldenberger,M.,
            Richards,J.B., Mohney,R.P., Milburn,M.V., John,S.L., Trimmer,J.,
            Theis,F.J., Overington,J.P., Suhre,K., Brosnan,M.J., Gieger,C.,
            Kastenmuller,G., Spector,T.D. and Soranzo,N.
  CONSRTM   Multiple Tissue Human Expression Resource (MuTHER) Consortium
  TITLE     An atlas of genetic influences on human blood metabolites
  JOURNAL   Nat Genet 46 (6), 543-550 (2014)
   PUBMED   24816252
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC035036.1, AK302464.1, AL353135.32 and AA503266.1.
            
            On Jan 26, 2005 this sequence version replaced XP_072402.7.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035036.1, SRR1660807.66389.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000275072.5/ ENSP00000275072.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q15"
     Protein         1..436
                     /product="xaa-Arg dipeptidase"
                     /EC_number="3.4.13.4"
                     /note="aminoacylase-1-like protein 2; I(2)-alanyl-lysine
                     dipeptidase; beta-alanyl-lysine dipeptidase; beta-Ala-Lys
                     dipeptidase"
                     /calculated_mol_wt=47645
     Region          31..406
                     /region_name="M20_ACY1L2-like"
                     /note="M20 Peptidase aminoacylase 1-like protein 2-like,
                     amidohydrolase subfamily; cd05672"
                     /db_xref="CDD:349921"
     CDS             1..436
                     /gene="PM20D2"
                     /gene_synonym="ACY1L2"
                     /coded_by="NM_001010853.3:91..1401"
                     /db_xref="CCDS:CCDS34499.1"
                     /db_xref="GeneID:135293"
                     /db_xref="HGNC:HGNC:21408"
                     /db_xref="MIM:615913"
ORIGIN      
        1 mrpggerpve ggacngrsel ellklrsaec ideaaerlga lsraiwsqpe layeehhahr
       61 vlthfferep paaswavqph yqlptafrae weppearaps atprplhlgf lceydalpgi
      121 ghacghnlia evgaaaalgv rgaleglprp pppvkvvvlg tpaeedgggk idlieagaft
      181 nldvvfmahp sqenaaylpd maehdvtvky ygkashsasy pweglnalda avlaynnlsv
      241 frqqmkptwr vhgiiknggv kpniipsyse liyyfrapsm kelqvltkka edcfraaala
      301 sgctveikgg ahdyynvlpn kslwkaymen grklgiefis edtmlngpsg stdfgnvsfv
      361 vpgihpyfhi gsnalnhteq yteaagsqea qfytlrtaka lamtaldvif kpellegire
      421 dfklklqeeq fvnave
//
LOCUS       NP_003204                434 aa            linear   PRI 27-APR-2025
DEFINITION  transcriptional enhancer factor TEF-3 isoform 1 [Homo sapiens].
ACCESSION   NP_003204
VERSION     NP_003204.2
DBSOURCE    REFSEQ: accession NM_003213.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Li,F., Wang,X., Zhang,J., Zhang,J., Jing,X., Jiang,Q., Zhou,J.,
            Cao,L., Peng,H., Tong,D. and Huang,C.
  TITLE     RBM8A, a new target of TEAD4, promotes breast cancer progression by
            regulating IGF1R and IRS-2
  JOURNAL   J Transl Med 22 (1), 823 (2024)
   PUBMED   39232805
  REMARK    GeneRIF: RBM8A, a new target of TEAD4, promotes breast cancer
            progression by regulating IGF1R and IRS-2.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Tan,K., Wang,J., Su,X., Zheng,Y. and Li,W.
  TITLE     KAT6A/YAP/TEAD4 pathway modulates osteoclastogenesis by regulating
            the RANKL/OPG ratio on the compression side during orthodontic
            tooth movement
  JOURNAL   Prog Orthod 25 (1), 29 (2024)
   PUBMED   39129034
  REMARK    GeneRIF: KAT6A/YAP/TEAD4 pathway modulates osteoclastogenesis by
            regulating the RANKL/OPG ratio on the compression side during
            orthodontic tooth movement.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Zhu,M., Meglicki,M., Lamba,A., Wang,P., Royer,C., Turner,K.,
            Jauhar,M.A., Jones,C., Child,T., Coward,K., Na,J. and
            Zernicka-Goetz,M.
  TITLE     Tead4 and Tfap2c generate bipotency and a bistable switch in
            totipotent embryos to promote robust lineage diversification
  JOURNAL   Nat Struct Mol Biol 31 (6), 964-976 (2024)
   PUBMED   38789684
  REMARK    GeneRIF: Tead4 and Tfap2c generate bipotency and a bistable switch
            in totipotent embryos to promote robust lineage diversification.
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Chan,S.W., Lim,C.J., Huang,C., Chong,Y.F., Gunaratne,H.J.,
            Hogue,K.A., Blackstock,W.P., Harvey,K.F. and Hong,W.
  TITLE     WW domain-mediated interaction with Wbp2 is important for the
            oncogenic property of TAZ
  JOURNAL   Oncogene 30 (5), 600-610 (2011)
   PUBMED   20972459
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Appukuttan,B., McFarland,T.J., Davies,M.H., Atchaneeyasakul,L.O.,
            Zhang,Y., Babra,B., Pan,Y., Rosenbaum,J.T., Acott,T., Powers,M.R.
            and Stout,J.T.
  TITLE     Identification of novel alternatively spliced isoforms of RTEF-1
            within human ocular vascular endothelial cells and murine retina
  JOURNAL   Invest Ophthalmol Vis Sci 48 (8), 3775-3782 (2007)
   PUBMED   17652751
  REMARK    GeneRIF: Novel RTEF-1 transcripts are present within human ocular
            vascular endothelial cells and mouse neural retina during normal
            and retinopathy of prematurity development, and alternatively
            spliced products are produced under hyperoxic and hypoxic
            conditions
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Vassilev,A., Kaneko,K.J., Shu,H., Zhao,Y. and DePamphilis,M.L.
  TITLE     TEAD/TEF transcription factors utilize the activation domain of
            YAP65, a Src/Yes-associated protein localized in the cytoplasm
  JOURNAL   Genes Dev 15 (10), 1229-1241 (2001)
   PUBMED   11358867
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Jacquemin,P., Depetris,D., Mattei,M.G., Martial,J.A. and
            Davidson,I.
  TITLE     Localization of human transcription factor TEF-4 and TEF-5 (TEAD2,
            TEAD3) genes to chromosomes 19q13.3 and 6p21.2 using fluorescence
            in situ hybridization and radiation hybrid analysis
  JOURNAL   Genomics 55 (1), 127-129 (1999)
   PUBMED   9889009
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Stewart,A.F., Richard,C.W. 3rd, Suzow,J., Stephan,D.,
            Weremowicz,S., Morton,C.C. and Adra,C.N.
  TITLE     Cloning of human RTEF-1, a transcriptional enhancer
            factor-1-related gene preferentially expressed in skeletal muscle:
            evidence for an ancient multigene family
  JOURNAL   Genomics 37 (1), 68-76 (1996)
   PUBMED   8921372
  REMARK    GeneRIF: The paper described several reasons to designate the
            putative translation initiation codon as the leucine (TTG) codon,
            which is 7 codons upstream from the isoleucine (ATT) codon.
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Jacquemin,P., Hwang,J.J., Martial,J.A., Dolle,P. and Davidson,I.
  TITLE     A novel family of developmentally regulated mammalian transcription
            factors containing the TEA/ATTS DNA binding domain
  JOURNAL   J Biol Chem 271 (36), 21775-21785 (1996)
   PUBMED   8702974
  REMARK    GeneRIF: The paper described that the ORF of TEF-3 initiates with
            an ATT codon encoding isoleucine.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA210894.1, BC015497.1 and
            U63824.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 20, 2004 this sequence version replaced NP_003204.1.
            
            Summary: This gene product is a member of the transcriptional
            enhancer factor (TEF) family of transcription factors, which
            contain the TEA/ATTS DNA-binding domain. It is preferentially
            expressed in the skeletal muscle, and binds to the M-CAT regulatory
            element found in promoters of muscle-specific genes to direct their
            gene expression. Alternatively spliced transcripts encoding
            distinct isoforms, some of which are translated through the use of
            a non-AUG (UUG) initiation codon, have been described for this
            gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1), and initiates translation from a non-AUG (UUG) codon.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U63824.1, BC015497.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match       :: ENST00000359864.8/ ENSP00000352926.3
            non-AUG initiation codon :: PMID: 8921372
            RefSeq Select criteria   :: based on conservation, expression,
                                        longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..434
                     /product="transcriptional enhancer factor TEF-3 isoform 1"
                     /note="transcriptional enhancer factor 3; transcription
                     factor 13-like 1; related transcription enhancer factor
                     1B; transcriptional enhancer factor TEF-3; transcriptional
                     enhancer factor 1-related; transcription factor RTEF-1;
                     TEA domain family member 4"
                     /calculated_mol_wt=48198
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15561.3)"
     Region          38..105
                     /region_name="TEA"
                     /note="TEA domain; smart00426"
                     /db_xref="CDD:128703"
     Region          188..215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15561.3)"
     Region          222..431
                     /region_name="YBD"
                     /note="YAP binding domain; pfam17725"
                     /db_xref="CDD:435993"
     CDS             1..434
                     /gene="TEAD4"
                     /gene_synonym="EFTR-2; hRTEF-1B; RTEF1; TCF13L1; TEF-3;
                     TEF3; TEFR-1"
                     /coded_by="NM_003213.4:208..1512"
                     /note="isoform 1 is encoded by transcript variant 1;
                     non-AUG (UUG) translation initiation codon"
                     /db_xref="CCDS:CCDS31729.1"
                     /db_xref="GeneID:7004"
                     /db_xref="HGNC:HGNC:11717"
                     /db_xref="MIM:601714"
ORIGIN      
        1 megtagtits newssptspe gstasggsqa ldkpidndae gvwspdieqs fqealaiypp
       61 cgrrkiilsd egkmygrnel iaryiklrtg ktrtrkqvss hiqvlarrka reiqaklkdq
      121 aakdkalqsm aamssaqiis atafhssmal argpgrpavs gfwqgalpgq agtshdvkpf
      181 sqqtyavqpp lplpgfespa gpapspsapp appwqgrsva ssklwmlefs afleqqqdpd
      241 tynkhlfvhi gqsspsysdp yleavdirqi ydkfpekkgg lkdlfergps nafflvkfwa
      301 dlntniedeg ssfygvssqy espenmiitc stkvcsfgkq vvekveteya ryenghysyr
      361 ihrsplceym infihklkhl pekymmnsvl enftilqvvt nrdtqetllc iayvfevsas
      421 ehgaqhhiyr lvke
//
LOCUS       NP_001354378            1860 aa            linear   PRI 27-APR-2025
DEFINITION  rho GTPase-activating protein 21 isoform c [Homo sapiens].
ACCESSION   NP_001354378
VERSION     NP_001354378.1
DBSOURCE    REFSEQ: accession NM_001367449.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1860)
  AUTHORS   Xie,Z., Liu,L., Fang,J., Zhong,X., Lin,J. and Chen,F.
  TITLE     [ARHGAP21 inhibits epithelial-mesenchymal transition by
            inactivating the WNT signaling pathway in non-small cell lung
            cancer]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 43 (8), 1322-1332 (2023)
   PUBMED   37712268
  REMARK    GeneRIF: [ARHGAP21 inhibits epithelial-mesenchymal transition by
            inactivating the WNT signaling pathway in non-small cell lung
            cancer].
REFERENCE   2  (residues 1 to 1860)
  AUTHORS   Lazarini,M., Assis-Mendonca,G.R., Machado-Neto,J.A.,
            Latuf-Filho,P., Bezerra,S.M., Vieira,K.P. and Saad,S.T.O.
  TITLE     Silencing of ARHGAP21, a Rho GTPase activating protein (RhoGAP),
            reduces the growth of prostate cancer xenografts in NOD/SCID mice
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1870 (4), 119439 (2023)
   PUBMED   36764390
  REMARK    GeneRIF: Silencing of ARHGAP21, a Rho GTPase activating protein
            (RhoGAP), reduces the growth of prostate cancer xenografts in
            NOD/SCID mice.
REFERENCE   3  (residues 1 to 1860)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1860)
  AUTHORS   Wang,Z., Wu,S., Wang,G., Yang,Z., Zhang,Y., Zhu,C. and Qin,X.
  TITLE     ARHGAP21 Is Involved in the Carcinogenic Mechanism of
            Cholangiocarcinoma: A Study Based on Bioinformatic Analyses and
            Experimental Validation
  JOURNAL   Medicina (Kaunas) 59 (1), 139 (2023)
   PUBMED   36676763
  REMARK    GeneRIF: ARHGAP21 Is Involved in the Carcinogenic Mechanism of
            Cholangiocarcinoma: A Study Based on Bioinformatic Analyses and
            Experimental Validation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1860)
  AUTHORS   Menetrey,J., Perderiset,M., Cicolari,J., Dubois,T., Elkhatib,N., El
            Khadali,F., Franco,M., Chavrier,P. and Houdusse,A.
  TITLE     Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi
            membranes
  JOURNAL   EMBO J 26 (7), 1953-1962 (2007)
   PUBMED   17347647
  REMARK    GeneRIF: The crystal structure of the activated GTP-bound form of
            ARF1 in a complex with the Arf-binding domain (ArfBD) of ARHGAP21
            at 2.1 A resolution, is presented.
REFERENCE   6  (residues 1 to 1860)
  AUTHORS   Benzinger,A., Muster,N., Koch,H.B., Yates,J.R. 3rd and Hermeking,H.
  TITLE     Targeted proteomic analysis of 14-3-3 sigma, a p53 effector
            commonly silenced in cancer
  JOURNAL   Mol Cell Proteomics 4 (6), 785-795 (2005)
   PUBMED   15778465
REFERENCE   7  (residues 1 to 1860)
  AUTHORS   Dubois,T., Paleotti,O., Mironov,A.A., Fraisier,V., Stradal,T.E., De
            Matteis,M.A., Franco,M. and Chavrier,P.
  TITLE     Golgi-localized GAP for Cdc42 functions downstream of ARF1 to
            control Arp2/3 complex and F-actin dynamics
  JOURNAL   Nat Cell Biol 7 (4), 353-364 (2005)
   PUBMED   15793564
  REMARK    GeneRIF: The ARHGAP10 protein is a novel Rho GTPase-activating
            protein (Rho-GAP) that is recruited to Golgi membranes through
            binding to GTP-ARF1.
REFERENCE   8  (residues 1 to 1860)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 1860)
  AUTHORS   Basseres,D.S., Tizzei,E.V., Duarte,A.A., Costa,F.F. and Saad,S.T.
  TITLE     ARHGAP10, a novel human gene coding for a potentially cytoskeletal
            Rho-GTPase activating protein
  JOURNAL   Biochem Biophys Res Commun 294 (3), 579-585 (2002)
   PUBMED   12056806
  REMARK    GeneRIF: ARHGAP10 gene is highly expressed in muscle and brain,
            which are highly differentiated tissues. It supports the hypothesis
            that ARHGAP10 is important for cell differentiation
REFERENCE   10 (residues 1 to 1860)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL355979.11 and AL392104.19.
            
            Summary: ARHGAP21 functions preferentially as a GTPase-activating
            protein (GAP) for CDC42 (MIM 116952) and regulates the ARP2/3
            complex (MIM 604221) and F-actin dynamics at the Golgi through
            control of CDC42 activity (Dubois et al., 2005 [PubMed
            15793564]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (7), as well as variant 8, encodes
            isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.258698.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..1860
                     /product="rho GTPase-activating protein 21 isoform c"
                     /note="rho GTPase-activating protein 21; Rho-GTPase
                     activating protein 10; rho GTPase-activating protein 10;
                     rho-type GTPase-activating protein 21"
                     /calculated_mol_wt=206335
     Region          <1..58
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          835..944
                     /region_name="PH_ARHGAP21-like"
                     /note="ARHGAP21 and related proteins pleckstrin homology
                     (PH) domain; cd01253"
                     /db_xref="CDD:269955"
     Site            order(835..852,857..883,885..917,919..942)
                     /site_type="other"
                     /note="ARF1 binding site [polypeptide binding]"
                     /db_xref="CDD:269955"
     Region          1046..1241
                     /region_name="RhoGAP_ARHGAP21"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain of ArhGAP21-like proteins. ArhGAP21
                     is a multi-domain protein, containing RhoGAP, PH and PDZ
                     domains, and is believed to play a role in the
                     organization of the cell-cell junction...; cd04395"
                     /db_xref="CDD:239860"
     Site            order(1086,1126,1130,1199,1202..1203,1227)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239860"
     Site            1086
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239860"
     CDS             1..1860
                     /gene="ARHGAP21"
                     /gene_synonym="ARHGAP10"
                     /coded_by="NM_001367449.1:786..6368"
                     /note="isoform c is encoded by transcript variant 7"
                     /db_xref="GeneID:57584"
                     /db_xref="HGNC:HGNC:23725"
                     /db_xref="MIM:609870"
ORIGIN      
        1 mdtifvkqvk eggpafeagl ctgdriikvn gesvigktys qvialiqnsd ttlelsvmpk
       61 dedilqvlqf tkdvtalays qdaylkgnea ysgnarnipe pppicypwlp sapsamaqpv
      121 eisppdssls kqqtstpvlt qpgrayrmei qvppsptdva ksntavcvcn esvrtvivps
      181 ekvvdllsnr nnhtgpshrt eevrygvseq tslktvsrtt spplsiptth lihqpagsrs
      241 lepsgillks gnysghsdgi sssrsqavea psvsvnhysp nshqhidwkn yktykeyidn
      301 rrlhigcrti qerldslraa sqsttdynqv vpnrttlqgr rrstshdrvp qsvqirqrsv
      361 sqerledsvl mkycprsasq galtspsvsf snhrtrswdy iegqdetlen vnsgtpipds
      421 ngekkqtykw sgfteqddrr gicerprqqe ihksfrgsnf tvapsvvnsd nrrmsgrgvg
      481 svsqfkkipp dlktlqsnrn fqttcgmslp rgisqdrspl vkvrsnslka psthvtkpsf
      541 sqksfvsikd qrpvnhlhqn sllnqqtwvr tdsapdqqve tgkspslsga sakpapqsse
      601 nagtsdlelp vsqrnqdlsl qeaeteqsdt ldnkeavilr ekppsgrqtp qplrhqsyil
      661 avndqetgsd ttcwlpndar revhikrmee rkasstsppg dslasipfid eptspsidhd
      721 iahipasavi sastsqvpsi atvppcltts aplirrqlsh dhesvgppsl daqpnskter
      781 sksydegldd yredaklsfk hvsslkgiki adsqksseds gsrkdsssev fsdaakegwl
      841 hfrplvtdkg krvggsirpw kqmyvvlrgh slylykdkre qttpseeeqp isvnaclidi
      901 sysetkrknv frlttsdcec lfqaedrddm lawiktiqes snlneedtgv tnrdlisrri
      961 keynnlmska eqlpktprqs lsirqtllga ksepktqsph spkeeserkl lskddtsppk
     1021 dkgtwrkgip simrktfekk ptatgtfgvr lddcppahtn ryiplivdic cklveergle
     1081 ytgiyrvpgn naaissmqee lnkgmadidi qddkwrdlnv issllksffr klpeplftnd
     1141 kyadfieanr kedpldrlkt lkrlihdlpe hhyetlkfls ahlktvaens eknkmeprnl
     1201 aivfgptlvr tsednmthmv thmpdqykiv etliqhhdwf fteegaeepl ttvqeestvd
     1261 sqpvpnidhl ltnigrtgvs pgdvsdsats dstkskgswg sgkdqysrel lvssifaaas
     1321 rkrkkpkeka qpsssedeld nvffkkenve qchndtkees kkesetlgrk qkiiiakens
     1381 trkdpsttkd ekislgkest pseepspphn skhnksptls crfailkesp rsllaqkssh
     1441 leetgsdsgt llstssqasl arfsmkksts petkhsefla nvstitsdys ttssatylts
     1501 ldssrlspev qsvaeskgde adderselis egrpvetdse sefpvfptal tserlfrgkl
     1561 qevtkssrrn segselscte gsltssldsr rqlfsshkli ecdtlsrkks arfksdsgsl
     1621 gdaknekeap sltkvfdvmk kgkstgsllt ptrgesekqe ptwktkiadr lklrprapad
     1681 dmfgvgnhkv naetakrksi rrrhtlgghr dateisvlnf wkvheqsger eselsavnrl
     1741 kpkcsaqdls isdwlarerl rtstsdlsrg eigdpqtenp streiattdt plslhcntgs
     1801 ssstlastnr pllsippqsp dqingesfqn vsknassaan aqphklsetp gskaefhpcl
//
LOCUS       NP_080606                266 aa            linear   ROD 27-APR-2025
DEFINITION  non-structural maintenance of chromosomes element 1 homolog isoform
            1 [Mus musculus].
ACCESSION   NP_080606
VERSION     NP_080606.3
DBSOURCE    REFSEQ: accession NM_026330.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Gong,M., Wang,Z., Liu,Y., Li,W., Ye,S., Zhu,J., Zhang,H., Wang,J.
            and He,K.
  TITLE     A transcriptomic analysis of Nsmce1 overexpression in mouse
            hippocampal neuronal cell by RNA sequencing
  JOURNAL   Funct Integr Genomics 20 (3), 459-470 (2020)
   PUBMED   31792732
  REMARK    GeneRIF: A transcriptomic analysis of Nsmce1 overexpression in
            mouse hippocampal neuronal cell by RNA sequencing.
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Hwang,G., Sun,F., O'Brien,M., Eppig,J.J., Handel,M.A. and
            Jordan,P.W.
  TITLE     SMC5/6 is required for the formation of segregation-competent
            bivalent chromosomes during meiosis I in mouse oocytes
  JOURNAL   Development 144 (9), 1648-1660 (2017)
   PUBMED   28302748
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Pryzhkova,M.V. and Jordan,P.W.
  TITLE     Conditional mutation of Smc5 in mouse embryonic stem cells perturbs
            condensin localization and mitotic progression
  JOURNAL   J Cell Sci 129 (8), 1619-1634 (2016)
   PUBMED   26919979
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Taniura,H., Tanabe,N., Bando,Y. and Arai,N.
  TITLE     Nse1 and Nse4, subunits of the Smc5-Smc6 complex, are involved in
            Dictyostelium development upon starvation
  JOURNAL   Dev Growth Differ 57 (6), 430-443 (2015)
   PUBMED   26036668
REFERENCE   7  (residues 1 to 266)
  AUTHORS   Gur,I., Fujiwara,K., Hasegawa,K. and Yoshikawa,K.
  TITLE     Necdin promotes ubiquitin-dependent degradation of PIAS1 SUMO E3
            ligase
  JOURNAL   PLoS One 9 (6), e99503 (2014)
   PUBMED   24911587
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 266)
  AUTHORS   Hoffman,B.G., Zavaglia,B., Witzsche,J., Ruiz de Algara,T.,
            Beach,M., Hoodless,P.A., Jones,S.J., Marra,M.A. and Helgason,C.D.
  TITLE     Identification of transcripts with enriched expression in the
            developing and adult pancreas
  JOURNAL   Genome Biol 9 (6), R99 (2008)
   PUBMED   18554416
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK011011.1 and BC049558.1.
            
            On Apr 4, 2019 this sequence version replaced NP_080606.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC049558.1, AK011011.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 68.87 cM"
     Protein         1..266
                     /product="non-structural maintenance of chromosomes
                     element 1 homolog isoform 1"
                     /EC_number="2.3.2.27"
                     /note="non-structural maintenance of chromosomes element 1
                     homolog; non-SMC element 1 homolog"
                     /calculated_mol_wt=30577
     Region          1..102
                     /region_name="Interaction with NSMCE3.
                     /evidence=ECO:0000250|UniProtKB:Q8WV22"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D720.1)"
     Region          16..175
                     /region_name="SMC_Nse1"
                     /note="Nse1 non-SMC component of SMC5-6 complex;
                     pfam07574"
                     /db_xref="CDD:462214"
     Region          189..235
                     /region_name="RING-CH-C4HC3_NSE1"
                     /note="RING-CH finger, H2 subclass (C4HC3-type), found in
                     non-structural maintenance of chromosomes (SMC) element 1
                     homolog (NSE1) and similar proteins; cd16493"
                     /db_xref="CDD:438156"
     Region          246..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D720.1)"
     CDS             1..266
                     /gene="Nsmce1"
                     /gene_synonym="2510027N19Rik"
                     /coded_by="NM_026330.4:43..843"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:67711"
                     /db_xref="MGI:MGI:1914961"
ORIGIN      
        1 mqgstrraga mtdvhrrflq llmthgvlee wevrrlqnhc yqvhdrnatv dkledfinni
       61 nsvleslyie ikkgvteddg rpiyalvnla ttsvskmatd faeneldlfr kalelivdse
      121 tgfasstnil nlvdqlkgkk mrkkeaeqvl qkfvqskwli ekegeftlhg railemeqfi
      181 resypdsvkm cnichglliq gqscetcgir mhlpcvakyf qsipephcph cndywphdip
      241 evynpekere agiskssrks lrtrqh
//
LOCUS       NP_002846                517 aa            linear   PRI 27-APR-2025
DEFINITION  nectin-1 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_002846
VERSION     NP_002846.3
DBSOURCE    REFSEQ: accession NM_002855.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Kite,J., Hill,M., Preston,N., Rubina,A., Kollnberger,S.,
            Wang,E.C.Y. and Elliott,G.
  TITLE     Downregulation of endogenous nectin1 in human keratinocytes by
            herpes simplex virus 1 glycoprotein D excludes superinfection but
            does not affect NK cell function
  JOURNAL   J Gen Virol 105 (3) (2024)
   PUBMED   38471041
  REMARK    GeneRIF: Downregulation of endogenous nectin1 in human
            keratinocytes by herpes simplex virus 1 glycoprotein D excludes
            superinfection but does not affect NK cell function.
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Park,J.W., Kang,G., Baek,S.H. and Kim,Y.H.
  TITLE     Genetic associations and parent-of-origin effects of PVRL1 in
            non-syndromic cleft lip with or without cleft palate across
            multiple ethnic populations
  JOURNAL   Epidemiol Health 46, e2024069 (2024)
   PUBMED   39139080
  REMARK    GeneRIF: Genetic associations and parent-of-origin effects of PVRL1
            in non-syndromic cleft lip with or without cleft palate across
            multiple ethnic populations.
REFERENCE   3  (residues 1 to 517)
  AUTHORS   De La Cruz,N.C., Mockel,M., Niehues,H., Rubsam,M., Malter,W.,
            Zinser,M., Krummenacher,C. and Knebel-Morsdorf,D.
  TITLE     Ex Vivo Infection of Human Skin Models with Herpes Simplex Virus 1:
            Accessibility of the Receptor Nectin-1 during Formation or
            Impairment of Epidermal Barriers Is Restricted by Tight Junctions
  JOURNAL   J Virol 97 (6), e0026223 (2023)
   PUBMED   37289055
  REMARK    GeneRIF: Ex Vivo Infection of Human Skin Models with Herpes Simplex
            Virus 1: Accessibility of the Receptor Nectin-1 during Formation or
            Impairment of Epidermal Barriers Is Restricted by Tight Junctions.
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Ablain,J., Al Mahi,A., Rothschild,H., Prasad,M., Aires,S., Yang,S.,
            Dokukin,M.E., Xu,S., Dang,M., Sokolov,I., Lian,C.G. and Zon,L.I.
  TITLE     Loss of NECTIN1 triggers melanoma dissemination upon local IGF1
            depletion
  JOURNAL   Nat Genet 54 (12), 1839-1852 (2022)
   PUBMED   36229674
  REMARK    GeneRIF: Loss of NECTIN1 triggers melanoma dissemination upon local
            IGF1 depletion.
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Kite,J., Russell,T., Jones,J. and Elliott,G.
  TITLE     Cell-to-cell transmission of HSV1 in human keratinocytes in the
            absence of the major entry receptor, nectin1
  JOURNAL   PLoS Pathog 17 (9), e1009631 (2021)
   PUBMED   34587223
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Krummenacher,C., Nicola,A.V., Whitbeck,J.C., Lou,H., Hou,W.,
            Lambris,J.D., Geraghty,R.J., Spear,P.G., Cohen,G.H. and
            Eisenberg,R.J.
  TITLE     Herpes simplex virus glycoprotein D can bind to poliovirus
            receptor-related protein 1 or herpesvirus entry mediator, two
            structurally unrelated mediators of virus entry
  JOURNAL   J Virol 72 (9), 7064-7074 (1998)
   PUBMED   9696799
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Geraghty,R.J., Krummenacher,C., Cohen,G.H., Eisenberg,R.J. and
            Spear,P.G.
  TITLE     Entry of alphaherpesviruses mediated by poliovirus receptor-related
            protein 1 and poliovirus receptor
  JOURNAL   Science 280 (5369), 1618-1620 (1998)
   PUBMED   9616127
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Lopez,M., Eberle,F., Mattei,M.G., Gabert,J., Birg,F., Bardin,F.,
            Maroc,C. and Dubreuil,P.
  TITLE     Complementary DNA characterization and chromosomal localization of
            a human gene related to the poliovirus receptor-encoding gene
  JOURNAL   Gene 155 (2), 261-265 (1995)
   PUBMED   7721102
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Bustos,T., Simosa,V., Pinto-Cisternas,J., Abramovits,W., Jolay,L.,
            Rodriguez,L., Fernandez,L. and Ramela,M.
  TITLE     Autosomal recessive ectodermal dysplasia: I. An undescribed
            dysplasia/malformation syndrome
  JOURNAL   Am J Med Genet 41 (4), 398-404 (1991)
   PUBMED   1776626
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Carritt,B. and Goldfarb,P.
  TITLE     A human chromosomal determinant for susceptibility to herpes
            simplex virus
  JOURNAL   Nature 264 (5586), 556-558 (1976)
   PUBMED   1034214
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003390.1, AI819997.1,
            BC104948.1, AP003393.1 and BC021976.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 17, 2004 this sequence version replaced NP_002846.2.
            
            Summary: This gene encodes an adhesion protein that plays a role in
            the organization of adherens junctions and tight junctions in
            epithelial and endothelial cells. The protein is a
            calcium(2+)-independent cell-cell adhesion molecule that belongs to
            the immunoglobulin superfamily and has 3 extracellular
            immunoglobulin-like loops, a single transmembrane domain (in some
            isoforms), and a cytoplasmic region. This protein acts as a
            receptor for glycoprotein D (gD) of herpes simplex viruses 1 and 2
            (HSV-1, HSV-2), and pseudorabies virus (PRV) and mediates viral
            entry into epithelial and neuronal cells. Mutations in this gene
            cause cleft lip and palate/ectodermal dysplasia 1 syndrome (CLPED1)
            as well as non-syndromic cleft lip with or without cleft palate
            (CL/P). Alternative splicing results in multiple transcript
            variants encoding proteins with distinct C-termini. [provided by
            RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest protein (isoform 1; also known
            as isoform Delta, alpha, or HveC).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF060231.1, BC104948.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267784 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264025.8/ ENSP00000264025.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..517
                     /product="nectin-1 isoform 1 precursor"
                     /note="nectin 1; poliovirus receptor-related 1
                     (herpesvirus entry mediator C); ectodermal dysplasia 4
                     (Margarita Island type); poliovirus receptor-like 1;
                     poliovirus receptor-related protein 1; herpesvirus Ig-like
                     receptor; herpes virus entry mediator C; herpes simplex
                     virus type 1 sensitivity"
                     /calculated_mol_wt=54061
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3116
     mat_peptide     31..517
                     /product="nectin-1 isoform 1"
                     /calculated_mol_wt=54061
     Region          31..143
                     /region_name="IgV_1_Nectin-1_like"
                     /note="First immunoglobulin variable (IgV) domain of
                     nectin-1, and similar domains; cd05886"
                     /db_xref="CDD:409469"
     Region          31..54
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409469"
     Region          31..35
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409469"
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Region          37..41
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409469"
     Site            order(45..52,62..70,77..89,107..113,118..132,135..143)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409469"
     Region          46..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409469"
     Region          55..62
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409469"
     Region          63..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409469"
     Region          64..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409469"
     Region          70..89
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409469"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21980294; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Region          79..84
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409469"
     Region          86..90
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409469"
     Region          90..128
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409469"
     Region          97..101
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409469"
     Region          106..113
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409469"
     Region          120..128
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409469"
     Region          129..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409469"
     Region          132..142
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409469"
     Region          133..143
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409469"
     Site            139
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21980294; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Region          146..243
                     /region_name="IgC1_2_Nectin-1_like"
                     /note="Second immunoglobulin (Ig) domain of nectin-1, and
                     similar domains; member of the C1-set of Ig superfamily
                     (IgSF) domains; cd05890"
                     /db_xref="CDD:143298"
     Region          146..152
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:143298"
     Region          168..175
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:143298"
     Region          180..186
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:143298"
     Region          188..190
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:143298"
     Region          191..199
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:143298"
     Site            202
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:21980294,
                     ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Region          205..213
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:143298"
     Region          223..230
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:143298"
     Region          234..240
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:143298"
     Region          247..333
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          265..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..283
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          282..299
                     /region_name="Interaction with FGFR.
                     /evidence=ECO:0000250|UniProtKB:Q9JKF6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15223.3)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Site            297
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Region          298..302
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Region          313..318
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          330..333
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            332
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Site            356..376
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15223.3)"
     Region          399..488
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15223.3)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKF6; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKF6; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKF6; propagated from
                     UniProtKB/Swiss-Prot (Q15223.3)"
     CDS             1..517
                     /gene="NECTIN1"
                     /gene_synonym="CD111; CLPED1; ED4; HIgR; HV1S; HVEC;
                     nectin-1; OFC7; PRR; PRR1; PVRL1; PVRR; PVRR1; SK-12"
                     /coded_by="NM_002855.5:648..2201"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8426.1"
                     /db_xref="GeneID:5818"
                     /db_xref="HGNC:HGNC:9706"
                     /db_xref="MIM:600644"
ORIGIN      
        1 marmglagaa grwwglalgl tafflpgvhs qvvqvndsmy gfigtdvvlh csfanplpsv
       61 kitqvtwqks tngskqnvai ynpsmgvsvl apyrervefl rpsftdgtir lsrleledeg
      121 vyicefatfp tgnresqlnl tvmakptnwi egtqavlrak kgqddkvlva tctsangkpp
      181 svvswetrlk geaeyqeirn pngtvtvisr yrlvpsreah qqslacivny hmdrfkeslt
      241 lnvqyepevt iegfdgnwyl qrmdvkltck adanppatey hwttlngslp kgveaqnrtl
      301 ffkgpinysl agtyiceatn pigtrsgqve vnitefpytp sppehgrrag pvptaiiggv
      361 agsillvliv vggivvalrr rrhtfkgdys tkkhvygngy skagipqhhp pmaqnlqypd
      421 dsddekkagp lggssyeeee eeeeggggge rkvggphpky dedakrpyft vdeaearqdg
      481 ygdrtlgyqy dpeqldlaen mvsqndgsfi skkewyv
//
LOCUS       NP_003120                574 aa            linear   PRI 27-APR-2025
DEFINITION  squalene monooxygenase [Homo sapiens].
ACCESSION   NP_003120
VERSION     NP_003120.2
DBSOURCE    REFSEQ: accession NM_003129.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Jun,S.Y., Yoon,H.R., Yoon,J.Y., Lee,J.J., Kim,J.Y., Kim,J.M. and
            Kim,N.S.
  TITLE     Age-related cholesterol and colorectal cancer progression:
            Validating squalene epoxidase for high-risk cases
  JOURNAL   Aging Cell 23 (7), e14152 (2024)
   PUBMED   38517197
  REMARK    GeneRIF: Age-related cholesterol and colorectal cancer progression:
            Validating squalene epoxidase for high-risk cases.
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Zhang,L., Cao,Z., Hong,Y., He,H., Chen,L., Yu,Z. and Gao,Y.
  TITLE     Squalene Epoxidase: Its Regulations and Links with Cancers
  JOURNAL   Int J Mol Sci 25 (7), 3874 (2024)
   PUBMED   38612682
  REMARK    GeneRIF: Squalene Epoxidase: Its Regulations and Links with
            Cancers.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Zhu,C., Fang,X., Liu,X., Jiang,C., Ren,W., Huang,W., Jiang,Y. and
            Wang,D.
  TITLE     Squalene monooxygenase facilitates bladder cancer development in
            part by regulating PCNA
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (3), 119681 (2024)
   PUBMED   38280406
  REMARK    GeneRIF: Squalene monooxygenase facilitates bladder cancer
            development in part by regulating PCNA.
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Wang,Y., Ma,X., Xu,E., Huang,Z., Yang,C., Zhu,K., Dong,Y. and
            Zhang,C.
  TITLE     Identifying squalene epoxidase as a metabolic vulnerability in
            high-risk osteosarcoma using an artificial intelligence-derived
            prognostic index
  JOURNAL   Clin Transl Med 14 (2), e1586 (2024)
   PUBMED   38372422
  REMARK    GeneRIF: Identifying squalene epoxidase as a metabolic
            vulnerability in high-risk osteosarcoma using an artificial
            intelligence-derived prognostic index.
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Ma,Y.C., Jin,S.J., Gu,G.J., Zhao,L.F. and Xu,S.T.
  TITLE     The expression of squalene epoxidase in human gastric cancer and
            its clinical significance
  JOURNAL   Indian J Pathol Microbiol 66 (4), 799-803 (2023)
   PUBMED   38084535
  REMARK    GeneRIF: The expression of squalene epoxidase in human gastric
            cancer and its clinical significance.
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Ma,J., Dempsey,A.A., Stamatiou,D., Marshall,K.W. and Liew,C.C.
  TITLE     Identifying leukocyte gene expression patterns associated with
            plasma lipid levels in human subjects
  JOURNAL   Atherosclerosis 191 (1), 63-72 (2007)
   PUBMED   16806233
REFERENCE   7  (residues 1 to 574)
  AUTHORS   Nagai,M., Sakakibara,J., Nakamura,Y., Gejyo,F. and Ono,T.
  TITLE     SREBP-2 and NF-Y are involved in the transcriptional regulation of
            squalene epoxidase
  JOURNAL   Biochem Biophys Res Commun 295 (1), 74-80 (2002)
   PUBMED   12083769
  REMARK    GeneRIF: functional promotor regions involved in transcription was
            determined
REFERENCE   8  (residues 1 to 574)
  AUTHORS   Laden,B.P., Tang,Y. and Porter,T.D.
  TITLE     Cloning, heterologous expression, and enzymological
            characterization of human squalene monooxygenase
  JOURNAL   Arch Biochem Biophys 374 (2), 381-388 (2000)
   PUBMED   10666321
REFERENCE   9  (residues 1 to 574)
  AUTHORS   Nagai,M., Sakakibara,J., Wakui,K., Fukushima,Y., Igarashi,S.,
            Tsuji,S., Arakawa,M. and Ono,T.
  TITLE     Localization of the squalene epoxidase gene (SQLE) to human
            chromosome region 8q24.1
  JOURNAL   Genomics 44 (1), 141-143 (1997)
   PUBMED   9286711
REFERENCE   10 (residues 1 to 574)
  AUTHORS   Nakamura,Y., Sakakibara,J., Izumi,T., Shibata,A. and Ono,T.
  TITLE     Transcriptional regulation of squalene epoxidase by sterols and
            inhibitors in HeLa cells
  JOURNAL   J Biol Chem 271 (14), 8053-8056 (1996)
   PUBMED   8626488
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG772453.1, BX647400.1,
            BX647605.1 and BC017033.1.
            
            On Apr 22, 2005 this sequence version replaced NP_003120.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647605.1, SRR1803616.235615.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265896.10/ ENSP00000265896.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..574
                     /product="squalene monooxygenase"
                     /EC_number="1.14.14.17"
                     /note="SE"
                     /calculated_mol_wt=63792
     Region          1..100
                     /region_name="Interaction with MARCHF6.
                     /evidence=ECO:0000269|PubMed:24449766"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14534.3)"
     Region          62..73
                     /region_name="Required for degradation in response to high
                     membrane cholesterol levels.
                     /evidence=ECO:0000269|PubMed:28972164"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14534.3)"
     Region          118..574
                     /region_name="Sufficient for enzyme activity.
                     /evidence=ECO:0000269|PubMed:10666321,
                     ECO:0000269|PubMed:30626872"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14534.3)"
     Region          122..>427
                     /region_name="PRK07045"
                     /note="putative monooxygenase; Reviewed"
                     /db_xref="CDD:136171"
     Site            195
                     /site_type="other"
                     /note="Important for enzyme activity.
                     /evidence=ECO:0000269|PubMed:30626872; propagated from
                     UniProtKB/Swiss-Prot (Q14534.3)"
     Region          277..548
                     /region_name="SE"
                     /note="Squalene epoxidase; pfam08491"
                     /db_xref="CDD:400679"
     Region          516..574
                     /region_name="Hydrophobic, mediates interaction with
                     membranes. /evidence=ECO:0000269|PubMed:30626872"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14534.3)"
     CDS             1..574
                     /gene="SQLE"
                     /coded_by="NM_003129.4:900..2624"
                     /db_xref="CCDS:CCDS47918.1"
                     /db_xref="GeneID:6713"
                     /db_xref="HGNC:HGNC:11279"
                     /db_xref="MIM:602019"
ORIGIN      
        1 mwtflgiatf tyfykkfgdf itlanrevll cvlvflslgl vlsyrcrhrn ggllgrqqsg
       61 sqfalfsdil sglpfigffw aksppesenk eqlearrrrk gtnisetsli gtaactstss
      121 qndpeviivg agvlgsalaa vlsrdgrkvt vierdlkepd rivgeflqpg gyhvlkdlgl
      181 gdtvegldaq vvngymihdq esksevqipy plsennqvqs grafhhgrfi mslrkaamae
      241 pnakfiegvv lqlleeddvv mgvqykdket gdikelhapl tvvadglfsk frkslvsnkv
      301 svsshfvgfl mknapqfkan haelilanps pvliyqisss etrvlvdirg emprnlreym
      361 vekiypqipd hlkepfleat dnshlrsmpa sflppssvkk rgvlllgday nmrhpltggg
      421 mtvafkdikl wrkllkgipd lyddaaifea kksfywarkt shsfvvnila qalyelfsat
      481 ddslhqlrka cflyfklgge cvagpvglls vlspnplvli ghffavaiya vyfcfksepw
      541 itkprallss gavlykacsv ifpliysemk ymvh
//
LOCUS       NP_001353347            1292 aa            linear   PRI 27-APR-2025
DEFINITION  histone-lysine N-methyltransferase SETDB1 isoform 4 [Homo sapiens].
ACCESSION   NP_001353347 XP_005245698
VERSION     NP_001353347.1
DBSOURCE    REFSEQ: accession NM_001366418.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1292)
  AUTHORS   Xia,K., Hui,Y., Zhang,L., Qiu,Q., Zhong,J., Chen,H., Liu,X.,
            Wang,L. and Chen,Z.
  TITLE     SETDB1 targeting SESN2 regulates mitochondrial damage and oxidative
            stress in renal ischemia-reperfusion injury
  JOURNAL   BMC Biol 22 (1), 246 (2024)
   PUBMED   39443993
  REMARK    GeneRIF: SETDB1 targeting SESN2 regulates mitochondrial damage and
            oxidative stress in renal ischemia-reperfusion injury.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1292)
  AUTHORS   Chang,Y.H., Yamamoto,K., Fujino,T., Wang,T.W., Sugimoto,E.,
            Zhang,W., Yabushita,T., Suzaki,K., Pietsch,E.C., Weir,B.A.,
            Crescenzo,R., Cowley,G.S., Attar,R., Philippar,U., Wunderlich,M.,
            Mizukawa,B., Zheng,Y., Enomoto,Y., Imai,Y., Kitamura,T. and
            Goyama,S.
  TITLE     SETDB1 suppresses NK cell-mediated immunosurveillance in acute
            myeloid leukemia with granulo-monocytic differentiation
  JOURNAL   Cell Rep 43 (8), 114536 (2024)
   PUBMED   39096901
REFERENCE   3  (residues 1 to 1292)
  AUTHORS   Kang,Y.K., Eom,J., Min,B. and Park,J.S.
  TITLE     SETDB1 deletion causes DNA demethylation and upregulation of
            multiple zinc-finger genes
  JOURNAL   Mol Biol Rep 51 (1), 778 (2024)
   PUBMED   38904842
  REMARK    GeneRIF: SETDB1 deletion causes DNA demethylation and upregulation
            of multiple zinc-finger genes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1292)
  AUTHORS   Yang,W., Wei,Y., Wang,T., Xu,Y., Jin,X., Qian,H., Yang,S. and He,S.
  TITLE     Cytoplasmic localization of SETDB1-induced Warburg effect via
            c-MYC-LDHA axis enhances migration and invasion in breast carcinoma
  JOURNAL   Int J Mol Med 53 (4) (2024)
   PUBMED   38426579
  REMARK    GeneRIF: Cytoplasmic localization of SETDB1-induced Warburg effect
            via c-MYC-LDHA axis enhances migration and invasion in breast
            carcinoma.
REFERENCE   5  (residues 1 to 1292)
  AUTHORS   Hao,Y., Bai,X.Y., Huo,F. and Chen,X.B.
  TITLE     [Downregulation of SETDB1 suppresses epithelial mesenchymal
            transition and invasion and metastasis in oral cancer via SOX7
            methylation]
  JOURNAL   Shanghai Kou Qiang Yi Xue 33 (1), 30-35 (2024)
   PUBMED   38583021
  REMARK    GeneRIF: [Downregulation of SETDB1 suppresses epithelial
            mesenchymal transition and invasion and metastasis in oral cancer
            via SOX7 methylation].
REFERENCE   6  (residues 1 to 1292)
  AUTHORS   Ayyanathan,K., Lechner,M.S., Bell,P., Maul,G.G., Schultz,D.C.,
            Yamada,Y., Tanaka,K., Torigoe,K. and Rauscher,F.J. 3rd.
  TITLE     Regulated recruitment of HP1 to a euchromatic gene induces
            mitotically heritable, epigenetic gene silencing: a mammalian cell
            culture model of gene variegation
  JOURNAL   Genes Dev 17 (15), 1855-1869 (2003)
   PUBMED   12869583
REFERENCE   7  (residues 1 to 1292)
  AUTHORS   Yang,L., Mei,Q., Zielinska-Kwiatkowska,A., Matsui,Y.,
            Blackburn,M.L., Benedetti,D., Krumm,A.A., Taborsky,G.J. Jr. and
            Chansky,H.A.
  TITLE     An ERG (ets-related gene)-associated histone methyltransferase
            interacts with histone deacetylases 1/2 and transcription
            co-repressors mSin3A/B
  JOURNAL   Biochem J 369 (Pt 3), 651-657 (2003)
   PUBMED   12398767
REFERENCE   8  (residues 1 to 1292)
  AUTHORS   Schultz,D.C., Ayyanathan,K., Negorev,D., Maul,G.G. and
            Rauscher,F.J. 3rd.
  TITLE     SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific
            methyltransferase that contributes to HP1-mediated silencing of
            euchromatic genes by KRAB zinc-finger proteins
  JOURNAL   Genes Dev 16 (8), 919-932 (2002)
   PUBMED   11959841
  REMARK    GeneRIF: Contributes to HP1-mediated silencing of euchromatic genes
            by KRAB zinc-finger proteins; KAP-1, SETDB1, H3-MeK9, and HP1 are
            enriched at promoter sequences of a euchromatic gene silenced by
            the KRAB-KAP-1 repression system
REFERENCE   9  (residues 1 to 1292)
  AUTHORS   Yang,L., Xia,L., Wu,D.Y., Wang,H., Chansky,H.A., Schubach,W.H.,
            Hickstein,D.D. and Zhang,Y.
  TITLE     Molecular cloning of ESET, a novel histone H3-specific
            methyltransferase that interacts with ERG transcription factor
  JOURNAL   Oncogene 21 (1), 148-152 (2002)
   PUBMED   11791185
REFERENCE   10 (residues 1 to 1292)
  AUTHORS   Harte,P.J., Wu,W., Carrasquillo,M.M. and Matera,A.G.
  TITLE     Assignment of a novel bifurcated SET domain gene, SETDB1, to human
            chromosome band 1q21 by in situ hybridization and radiation hybrids
  JOURNAL   Cytogenet Cell Genet 84 (1-2), 83-86 (1999)
   PUBMED   10343109
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590133.32.
            
            On Oct 4, 2018 this sequence version replaced XP_005245698.1.
            
            Summary: This gene encodes a histone methyltransferase which
            regulates histone methylation, gene silencing, and transcriptional
            repression. This gene has been identified as a target for treatment
            in Huntington Disease, given that gene silencing and transcription
            dysfunction likely play a role in the disease pathogenesis.
            Alternatively spliced transcript variants of this gene have been
            described.[provided by RefSeq, Jun 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.719197.1,
                                           SRR1660805.205466.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000692827.1/ ENSP00000509425.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..1292
                     /product="histone-lysine N-methyltransferase SETDB1
                     isoform 4"
                     /EC_number="2.1.1.366"
                     /note="ERG-associated protein with a SET domain, ESET;
                     histone-lysine N-methyltransferase, H3lysine-9 specific 4;
                     lysine N-methyltransferase 1E; histone-lysine
                     N-methyltransferase SETDB1; histone H3-K9
                     methyltransferase 4; tudor domain containing 21; SET
                     domain bifurcated 1"
                     /calculated_mol_wt=143128
     Region          108..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15047.1)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88974; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88974; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88974; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Region          193..250
                     /region_name="DUF5604"
                     /note="Domain of unknown function (DUF5604); pfam18300"
                     /db_xref="CDD:408109"
     Region          260..341
                     /region_name="Tudor_SETDB1_rpt1"
                     /note="first Tudor domain found in SET domain bifurcated 1
                     (SETDB1) and similar proteins; cd20382"
                     /db_xref="CDD:410453"
     Site            order(296,299..302)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410453"
     Region          348..401
                     /region_name="Tudor_SETDB1_rpt2"
                     /note="second Tudor domain found in SET domain bifurcated
                     1 (SETDB1) and similar proteins; cd21181"
                     /db_xref="CDD:410548"
     Site            order(357,360,386..389,392..394)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410548"
     Region          598..673
                     /region_name="MBD"
                     /note="Methyl-CpG binding domain; smart00391"
                     /db_xref="CDD:128673"
     Site            order(612,614,616,623,625,634,637,641)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238689"
     Region          675..>876
                     /region_name="SET_SETDB1"
                     /note="SET domain (including pre-SET and post-SET domains)
                     found in SET domain bifurcated 1 (SETDB1) and similar
                     proteins; cd10517"
                     /db_xref="CDD:380915"
     Region          869..1161
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15047.1)"
     Site            1026
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Site            1067
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Site            1171
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Site            1179
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15047.1)"
     Region          <1203..1292
                     /region_name="SET"
                     /note="SET (Su(var)3-9, Enhancer-of-zeste, Trithorax)
                     domain superfamily; cl40432"
                     /db_xref="CDD:394802"
     Site            order(1220..1225,1233..1235,1264..1267)
                     /site_type="active"
                     /db_xref="CDD:380915"
     CDS             1..1292
                     /gene="SETDB1"
                     /gene_synonym="ESET; H3-K9-HMTase4; KG1T; KMT1E; TDRD21"
                     /coded_by="NM_001366418.1:167..4045"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS91050.1"
                     /db_xref="GeneID:9869"
                     /db_xref="HGNC:HGNC:10761"
                     /db_xref="MIM:604396"
ORIGIN      
        1 msslpgcigl daatatvese eiaelqqavv eelgismeel rhfideelek mdcvqqrkkq
       61 laeletwviq kesevahvdq lfddasravt nceslvkdfy sklglqyrds ssedessrpt
      121 eiieipdedd dvlsidsgda gsrtpkdqkl reamaalrks aqdvqkfmda vnkksssqdl
      181 hkgtlsqmsg elskdgdliv smrilgkkrt ktwhkgtlia iqtvgpgkky kvkfdnkgks
      241 llsgnhiayd yhppadklyv gsrvvakykd gnqvwlyagi vaetpnvknk lrfliffddg
      301 yasyvtqsel ypicrplkkt wediediscr dfieeyvtay pnrpmvllks gqlikteweg
      361 twwksrveev dgslvrilfl ddkrcewiyr gstrlepmfs mktssasale kkqgqlrtrp
      421 nmgavrskgp vvqytqdltg tgtqfkpvep pqptappapp fppapplspq agdseslesq
      481 laqsrkqvak kstsfrpgsv gsghssptsp alsenvsggk pginqtyrsp lgstasapap
      541 salpappapp vfhgmlerap aepsyrapme klfylphvcs ytclsrvrpm rneqyrgknp
      601 llvpllydfr rmtarrrvnr kmgfhviykt pcglclrtmq eierylfetg cdflflemfc
      661 ldpyvlvdrk fqpykpfyyi lditygkedv plscvneidt tpppqvaysk eripgkgvfi
      721 ntgpeflvgc dckdgcrdks kcachqltiq atactpggqi npnsgyqykr leeclptgvy
      781 ecnkrckcdp nmctnrlvqh glqvrlqlfk tqnkgwgirc lddiakgsfv ciyagkiltd
      841 dfadkeglem gdeyfanldh iesvenfkeg yesdapcssd ssgvdlkdqe dgnsgtedpe
      901 esnddssddn fckdedfsts svwrsyatrr qtrgqkengl settskdshp pdlgpphipv
      961 ppsipvggcn ppsseetpkn kvaswlscns vseggfadsd shssfktneg gegraggsrm
     1021 eaekastsgl gikdegdikq akkedtddrn kmsvvtessr nygynpspvk peglrrppsk
     1081 tsmhqsrrlm asaqsnpddv ltlssstese gesgtsrkpt agqtsatavd sddiqtissg
     1141 segddfedkk nmtgpmkrqv avkstrgfal ksthgiaiks tnmasvdkge sapvrkntrq
     1201 fydgeescyi idaklegnlg rylnhscspn lfvqnvfvdt hdlrfpwvaf faskriragt
     1261 eltwdynyev gsvegkellc ccgaiecrgr ll
//
LOCUS       NP_004370                327 aa            linear   PRI 27-APR-2025
DEFINITION  cyclic AMP-responsive element-binding protein 1 isoform A [Homo
            sapiens].
ACCESSION   NP_004370
VERSION     NP_004370.1
DBSOURCE    REFSEQ: accession NM_004379.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   He,C., Zeng,Z., Yang,Y., Ye,S., Wu,Q., Liu,X., Liu,C., Zeng,W. and
            Liu,S.
  TITLE     Silencing of CircTRIM25/miR-138-5p/CREB1 axis promotes
            chondrogenesis in osteoarthritis
  JOURNAL   Autoimmunity 57 (1), 2361749 (2024)
   PUBMED   39007896
  REMARK    GeneRIF: Silencing of CircTRIM25/miR-138-5p/CREB1 axis promotes
            chondrogenesis in osteoarthritis.
            Erratum:[Autoimmunity. 2024 Dec;57(1):2435720. doi:
            10.1080/08916934.2024.2435720. PMID: 39621026]
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Aida,Y. and Kataoka,K.
  TITLE     CREB activates the MafA promoter through proximal E-boxes and a
            CCAAT motif in pancreatic beta-cells
  JOURNAL   J Mol Endocrinol 73 (3), e240023 (2024)
   PUBMED   39189982
  REMARK    GeneRIF: CREB activates the MafA promoter through proximal E-boxes
            and a CCAAT motif in pancreatic beta-cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Ismael,A., Robinette,A.J., Huric,L., Schuetz,J., Dona,K.,
            Benson,D., Cocucci,E. and Cottini,F.
  TITLE     CREB1 promotes expression of immune checkpoint HLA-E leading to
            immune escape in multiple myeloma
  JOURNAL   Leukemia 38 (8), 1777-1786 (2024)
   PUBMED   38902472
  REMARK    GeneRIF: CREB1 promotes expression of immune checkpoint HLA-E
            leading to immune escape in multiple myeloma.
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Pei,W., Yin,W., Yu,T., Zhang,X., Zhang,Q., Yang,X., Shi,C., Shen,W.
            and Liu,G.
  TITLE     Dual-Specificity Phosphatase 4 Promotes Malignant Features in
            Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation
  JOURNAL   Dig Dis Sci 69 (8), 2856-2874 (2024)
   PUBMED   38824257
  REMARK    GeneRIF: Dual-Specificity Phosphatase 4 Promotes Malignant Features
            in Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation.
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Ma,Y., Zong,H., Pan,P., Shang,H. and Yang,X.
  TITLE     The CREB1/WNK1 axis promotes the tumorigenesis of ovarian cancer
            via regulating HIF-1
  JOURNAL   Exp Cell Res 438 (1), 114006 (2024)
   PUBMED   38599542
  REMARK    GeneRIF: The CREB1/WNK1 axis promotes the tumorigenesis of ovarian
            cancer via regulating HIF-1.
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Meyer,T.E. and Habener,J.F.
  TITLE     Cyclic AMP response element binding protein CREB and modulator
            protein CREM are products of distinct genes
  JOURNAL   Nucleic Acids Res 20 (22), 6106 (1992)
   PUBMED   1461747
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Zhao,L.J. and Giam,C.Z.
  TITLE     Human T-cell lymphotropic virus type I (HTLV-I) transcriptional
            activator, Tax, enhances CREB binding to HTLV-I 21-base-pair
            repeats by protein-protein interaction
  JOURNAL   Proc Natl Acad Sci U S A 89 (15), 7070-7074 (1992)
   PUBMED   1386673
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Rehfuss,R.P., Walton,K.M., Loriaux,M.M. and Goodman,R.H.
  TITLE     The cAMP-regulated enhancer-binding protein ATF-1 activates
            transcription in response to cAMP-dependent protein kinase A
  JOURNAL   J Biol Chem 266 (28), 18431-18434 (1991)
   PUBMED   1655749
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Short,M.L., Manohar,C.F., Furtado,M.R., Ghadge,G.D., Wolinsky,S.M.,
            Thimmapaya,B. and Jungmann,R.A.
  TITLE     Nucleotide and derived amino-acid sequences of the CRE-binding
            proteins from rat C6 glioma and HeLa cells
  JOURNAL   Nucleic Acids Res 19 (15), 4290 (1991)
   PUBMED   1831258
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Waeber,G., Meyer,T.E., Hoeffler,J.P. and Habener,J.F.
  TITLE     Diversification of cyclic AMP-responsive enhancer binding
            proteins-generated by alternative exon splicing
  JOURNAL   Trans Assoc Am Physicians 103, 28-37 (1990)
   PUBMED   1966745
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC095407.1, AC079767.7 and
            BU154326.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a transcription factor that is a member
            of the leucine zipper family of DNA binding proteins. This protein
            binds as a homodimer to the cAMP-responsive element, an octameric
            palindrome. The protein is phosphorylated by several protein
            kinases, and induces transcription of genes in response to hormonal
            stimulation of the cAMP pathway. Alternate splicing of this gene
            results in several transcript variants encoding different isoforms.
            [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (1, also known as A) lacks an
            alternate in-frame exon compared to variant 2. The resulting
            isoform (A) has the same N- and C-termini but is shorter compared
            to isoform B.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.50553.1,
                                           SRR1660807.69906.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000353267.8/ ENSP00000236995.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..327
                     /product="cyclic AMP-responsive element-binding protein 1
                     isoform A"
                     /note="cAMP-response element-binding protein-1; active
                     transcription factor CREB; transactivator protein; cyclic
                     AMP-responsive element-binding protein 1; cyclic adenosine
                     3',5'-monophosphate response element-binding protein CREB;
                     cyclic adenosine 3',5'-monophosphate response element
                     binding protein"
                     /calculated_mol_wt=35005
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16220.3)"
     Region          94..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16220.3)"
     Region          99..137
                     /region_name="pKID"
                     /note="pKID domain; pfam02173"
                     /db_xref="CDD:396650"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK1, CaMK2, CaMK4, PKB/AKT1 or
                     PKB/AKT2, RPS6KA3, RPS6KA4, RPS6KA5, SGK1 and TSSK4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00312,
                     ECO:0000269|PubMed:15733869, ECO:0000269|PubMed:15964553,
                     ECO:0000269|PubMed:7608156, ECO:0000269|PubMed:8065343,
                     ECO:0000269|PubMed:9770464, ECO:0000269|PubMed:9829964;
                     propagated from UniProtKB/Swiss-Prot (P16220.3)"
     Region          125..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16220.3)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16220.3)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00312,
                     ECO:0000269|PubMed:20573984; propagated from
                     UniProtKB/Swiss-Prot (P16220.3)"
     Region          270..295
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P16220.3)"
     Region          271..325
                     /region_name="bZIP_CREB1"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 1 (CREB1) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14690"
                     /db_xref="CDD:269838"
     Region          272..324
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269838"
     Site            order(272,276,278..280,282..284,286..287,289..291)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269838"
     Site            order(290,293,297..298,300..301,304..305,307..308,311,
                     314..315,318..319,321..322)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269838"
     Region          297..318
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P16220.3)"
     Site            300
                     /site_type="other"
                     /note="Required for binding TORCs; propagated from
                     UniProtKB/Swiss-Prot (P16220.3)"
     CDS             1..327
                     /gene="CREB1"
                     /gene_synonym="CREB; CREB-1"
                     /coded_by="NM_004379.5:182..1165"
                     /note="isoform A is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2374.1"
                     /db_xref="GeneID:1385"
                     /db_xref="HGNC:HGNC:2345"
                     /db_xref="MIM:123810"
ORIGIN      
        1 mtmesgaenq qsgdaavtea enqqmtvqaq pqiatlaqvs mpaahatssa ptvtlvqlpn
       61 gqtvqvhgvi qaaqpsviqs pqvqtvqist iaesedsqes vdsvtdsqkr reilsrrpsy
      121 rkilndlssd apgvprieee kseeetsapa ittvtvptpi yqtssgqyia itqggaiqla
      181 nngtdgvqgl qtltmtnaaa tqpgttilqy aqttdgqqil vpsnqvvvqa asgdvqtyqi
      241 rtaptstiap gvvmasspal ptqpaeeaar krevrlmknr eaarecrrkk keyvkclenr
      301 vavlenqnkt lieelkalkd lychksd
//
LOCUS       NP_001350155             607 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor Sp2 isoform 3 [Mus musculus].
ACCESSION   NP_001350155 XP_006534584
VERSION     NP_001350155.1
DBSOURCE    REFSEQ: accession NM_001363226.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Johnson,C.A. and Ghashghaei,H.T.
  TITLE     Sp2 regulates late neurogenic but not early expansive divisions of
            neural stem cells underlying population growth in the mouse cortex
  JOURNAL   Development 147 (4) (2020)
   PUBMED   32001437
  REMARK    GeneRIF: there is a stage-specific requirement for Sp2 in neural
            stem and progenitor cells in the mouse cortex
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Norrie,J.L., Lupo,M.S., Xu,B., Al Diri,I., Valentine,M., Putnam,D.,
            Griffiths,L., Zhang,J., Johnson,D., Easton,J., Shao,Y., Honnell,V.,
            Frase,S., Miller,S., Stewart,V., Zhou,X., Chen,X. and Dyer,M.A.
  TITLE     Nucleome Dynamics during Retinal Development
  JOURNAL   Neuron 104 (3), 512-528 (2019)
   PUBMED   31493975
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Volkel,S., Stielow,B., Finkernagel,F., Berger,D., Stiewe,T.,
            Nist,A. and Suske,G.
  TITLE     Transcription factor Sp2 potentiates binding of the TALE
            homeoproteins Pbx1:Prep1 and the histone-fold domain protein Nf-y
            to composite genomic sites
  JOURNAL   J Biol Chem 293 (50), 19250-19262 (2018)
   PUBMED   30337366
  REMARK    GeneRIF: a mechanism by which the DNA binding-independent activity
            of Sp2 potentiates genomic loading of Pbx1:Prep1 and Nf-y to
            composite motifs present in many promoters of highly expressed
            genes
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Wegener,A., Kuspert,M., Sock,E., Philipsen,S., Suske,G. and
            Wegner,M.
  TITLE     Sp2 is the only glutamine-rich specificity protein with minor
            impact on development and differentiation in myelinating glia
  JOURNAL   J Neurochem 140 (2), 245-256 (2017)
   PUBMED   27889927
REFERENCE   5  (residues 1 to 607)
  AUTHORS   Zschemisch,N.H., Brusch,I., Hambusch,A.S. and Bleich,A.
  TITLE     Transcription Factor SP2 Enhanced the Expression of Cd14 in
            Colitis-Susceptible C3H/HeJBir
  JOURNAL   PLoS One 11 (5), e0155821 (2016)
   PUBMED   27191968
  REMARK    GeneRIF: SP2 as important factor responsible for higher Cd14
            expression and reduced IBD susceptibility mediated by the C3Bir
            allele.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 607)
  AUTHORS   Suske,G., Bruford,E. and Philipsen,S.
  TITLE     Mammalian SP/KLF transcription factors: bring in the family
  JOURNAL   Genomics 85 (5), 551-556 (2005)
   PUBMED   15820306
REFERENCE   7  (residues 1 to 607)
  AUTHORS   Moorefield,K.S., Fry,S.J. and Horowitz,J.M.
  TITLE     Sp2 DNA binding activity and trans-activation are negatively
            regulated in mammalian cells
  JOURNAL   J Biol Chem 279 (14), 13911-13924 (2004)
   PUBMED   14726517
REFERENCE   8  (residues 1 to 607)
  AUTHORS   Hammer,F., Compagnone,N.A., Vigne,J.L., Bair,S.R. and Mellon,S.H.
  TITLE     Transcriptional regulation of P450scc gene expression in the
            embryonic rodent nervous system
  JOURNAL   Endocrinology 145 (2), 901-912 (2004)
   PUBMED   14576192
REFERENCE   9  (residues 1 to 607)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 607)
  AUTHORS   Bakovic,M., Waite,K.A. and Vance,D.E.
  TITLE     Functional significance of Sp1, Sp2, and Sp3 transcription factors
            in regulation of the murine CTP:phosphocholine cytidylyltransferase
            alpha promoter
  JOURNAL   J Lipid Res 41 (4), 583-594 (2000)
   PUBMED   10744779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK080877.1 and AL596384.17.
            
            On May 12, 2018 this sequence version replaced XP_006534584.1.
            
            Summary: This gene encodes a member of the Sp subfamily of Sp/XKLF
            transcription factors. Sp family proteins are sequence-specific
            DNA-binding proteins characterized by an amino-terminal
            trans-activation domain and three carboxy-terminal zinc finger
            motifs. This protein contains the least conserved DNA-binding
            domain within the Sp subfamily of proteins, and its DNA sequence
            specificity differs from the other Sp proteins. The protein can act
            as a transcriptional activator or repressor, depending on the
            promoter and cell type. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK080877.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 60.17 cM"
     Protein         1..607
                     /product="transcription factor Sp2 isoform 3"
                     /note="transcription factor Sp2"
                     /calculated_mol_wt=64219
     Region          4..520
                     /region_name="SP2_N"
                     /note="N-terminal domain of transcription factor
                     Specificity Protein (SP) 2; cd22540"
                     /db_xref="CDD:411776"
     Region          524..543
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(528,530,532,534..535,538..539,542,558,560,564..565,
                     568..569,572,586,588,590,592..593,596..597,600)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          536..562
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          551..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          565..588
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          579..601
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          581..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..607
                     /gene="Sp2"
                     /gene_synonym="4930480I16Rik; mKIAA0048"
                     /coded_by="NM_001363226.1:87..1910"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS88237.1"
                     /db_xref="GeneID:78912"
                     /db_xref="MGI:MGI:1926162"
ORIGIN      
        1 msmaataavs psdylqpaaa ttqdsqpspl allaatcski gppaveaavt ppappqptpr
       61 klvpikpapl plspcknsfs ilsskgnilq iqgsqlstsy pggqfvfaiq nptlinkgsr
      121 snasiqyqvp qiqgnssqti qvqpsltnqi qvipgtnqai ttpstsghkp vpikpapvqk
      181 ssttttpvqs ganvvkltgg gsnmtltlpl nnlvntsdig gpaqlltesp ptplsktnkk
      241 arkkslpvsq psvavaeqve tvliettadn iiqagnnlli vqspgggqpa vvqqvqvvpp
      301 kaeqqqvvqi pqqalrvvqa asatlptvpq kpsqnfqiqt teptptqvyi rtpsgevqtv
      361 lvqdsppata attstvtcns palraphlsg tskkhsaail rkerplpkia pagsiislna
      421 aqlaaaaqam qtiningvqv qgvpvtitnt ggqqqltvqn vsgnnltisg lsptqiqlqm
      481 eqalageaqp gekrrrmact cpnckdgekr sgeqgkkkhv chipdcgktf rktsllrahv
      541 rlhtgerpfv cnwffcgkrf trsdelqrha rthtgdkrfe caqcqkrfmr sdhltkhykt
      601 hlgtkgl
//
LOCUS       NP_001356034             318 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 12 [Homo
            sapiens].
ACCESSION   NP_001356034
VERSION     NP_001356034.1
DBSOURCE    REFSEQ: accession NM_001369105.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.48188.1,
                                           SRR1803617.229409.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..318
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 12"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=36303
     Region          20..85
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(29,31..33,35..39,42..43,46..47,52..55)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          94..317
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..318
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369105.1:319..1275"
                     /note="isoform 12 is encoded by transcript variant 26"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mecadepcda yeveqtpqgf rstlrapsll ykhivgkrgd trkkiemetk tsisipkpgq
       61 dgeivitgqh rngvisartr idvlldtfrr kqpfthflaf flnevevqeg flrfqeevla
      121 kcsmdhgvds sifqnpkklh ltigmlvlls eeeiqqtcem lqqckeefin disggkplev
      181 emagieymnd dpgmvdvlya kvhmkdgsnr lqelvdrvle rfqasglivk ewnsvklhat
      241 vmntlfrkdp naegrynlyt aegkyifker esfdgrnilk lfenfyfgsl klnsihisqr
      301 ftvdsfgnya scgqidfs
//
LOCUS       NP_083958                436 aa            linear   ROD 27-APR-2025
DEFINITION  AMSH-like protease isoform 1 [Mus musculus].
ACCESSION   NP_083958
VERSION     NP_083958.3
DBSOURCE    REFSEQ: accession NM_029682.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Zhang,H., Wang,Z., Zhang,J., Li,Z., Liu,J., Yu,J., Zhao,Y., Guo,F.,
            Chen,W.D. and Wang,Y.D.
  TITLE     A MYC-STAMBPL1-TOE1 positive feedback loop mediates EGFR stability
            in hepatocellular carcinoma
  JOURNAL   Cell Rep 43 (10), 114812 (2024)
   PUBMED   39388352
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Lavorgna,A. and Harhaj,E.W.
  TITLE     An RNA interference screen identifies the Deubiquitinase STAMBPL1
            as a critical regulator of human T-cell leukemia virus type 1 tax
            nuclear export and NF-kappaB activation
  JOURNAL   J Virol 86 (6), 3357-3369 (2012)
   PUBMED   22258247
  REMARK    Erratum:[J Virol. 2012 May;86(9):5409]
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Kitajima,K., Matsumoto,K., Tahara,M., Takahashi,H., Nakamura,T. and
            Nakamura,T.
  TITLE     A newly identified AMSH-family protein is specifically expressed in
            haploid stages of testicular germ cells
  JOURNAL   Biochem Biophys Res Commun 309 (1), 135-142 (2003)
   PUBMED   12943674
  REMARK    GeneRIF: AMSH-FP is specifically expressed in haploid stages of
            testicular germ cells and has a functional role in spermiogenesis
            [AMSH-FP]
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Takahashi,H., Koshimizu,U. and Nakamura,T.
  TITLE     A novel transcript encoding truncated LIM kinase 2 is specifically
            expressed in male germ cells undergoing meiosis
  JOURNAL   Biochem Biophys Res Commun 249 (1), 138-145 (1998)
   PUBMED   9705845
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC165239.3, AB010121.1 and AC102285.7.
            
            On Nov 15, 2004 this sequence version replaced NP_083958.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB066211.1, BC023097.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 29.35 cM"
     Protein         1..436
                     /product="AMSH-like protease isoform 1"
                     /EC_number="3.1.2.15"
                     /note="AMSH-family protein; AMSH-like protease; AMSH-LP"
                     /calculated_mol_wt=49509
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q96FJ0; propagated from
                     UniProtKB/Swiss-Prot (Q76N33.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96FJ0; propagated from
                     UniProtKB/Swiss-Prot (Q76N33.1)"
     Region          28..132
                     /region_name="USP8_dimer"
                     /note="USP8 dimerization domain; pfam08969"
                     /db_xref="CDD:462647"
     Region          <101..>176
                     /region_name="HlpA"
                     /note="Periplasmic chaperone for outer membrane proteins,
                     Skp family [Cell wall/membrane/envelope biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG2825"
                     /db_xref="CDD:442073"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q76N33.1)"
     Region          266..436
                     /region_name="MPN_AMSH_like"
                     /note="Mov34/MPN/PAD-1 family; cd08066"
                     /db_xref="CDD:163697"
     Site            order(292,347,349,357,360)
                     /site_type="active"
                     /note="MPN+ (JAMM) motif [active]"
                     /db_xref="CDD:163697"
     Site            292
                     /site_type="other"
                     /note="Indirect zinc-binding.
                     /evidence=ECO:0000250|UniProtKB:Q96FJ0; propagated from
                     UniProtKB/Swiss-Prot (Q76N33.1)"
     Site            order(294..296,321..325,328..329,332,335,341..342,345,347,
                     349,357,359..360,362..363,366..367,369..370,407)
                     /site_type="other"
                     /note="Distal ubiquitin recognition interface [polypeptide
                     binding]"
                     /db_xref="CDD:163697"
     Site            order(321,349,352..353,355,357..358,407..409)
                     /site_type="active"
                     /note="Proximal ubiquitin recognition interface [active]"
                     /db_xref="CDD:163697"
     Region          347..360
                     /region_name="JAMM motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76N33.1)"
     Site            order(347,349,360)
                     /site_type="other"
                     /note="Zinc-binding site [ion binding]"
                     /db_xref="CDD:163697"
     CDS             1..436
                     /gene="Stambpl1"
                     /gene_synonym="1700095N21Rik; 8230401J17Rik; ALMalpha;
                     AMSH-FP"
                     /coded_by="NM_029682.5:454..1764"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS29756.1"
                     /db_xref="GeneID:76630"
                     /db_xref="MGI:MGI:1923880"
ORIGIN      
        1 meqpftvnsl kklaampdht dvslspeerv ralsklgcni sineditprr yfrsgvemer
       61 masvyleegn lenafvlynk fitlfveklp shrdyqqcav pekqdimkkl keiafprtde
      121 lktdllrkyn ieyqeylqsk nkykaeilkk lehqrlieae rqriaqmrqq qleseqflff
      181 edqlkkqela rgqirgqdsp vlseqtdgsa lscfsthqsn slrnafadhp hksdgsnfan
      241 ysppvnralk paatlsavqn lvveglrcvv lsrdlchkfl lladsntvrg ietcgilcgk
      301 lthneftith vvvpkqsagp dycdvenvee lfnvqdqhgl ltlgwihthp tqtaflssvd
      361 lhthcsyqlm lpeaiaivcs pkhkdtgifr ltnagmlevs tckkkgfhph tkdpklfsic
      421 shvlvkdikt tvldlr
//
LOCUS       NP_742024                478 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat and BTB/POZ domain-containing protein 1 isoform 2
            [Homo sapiens].
ACCESSION   NP_742024
VERSION     NP_742024.1
DBSOURCE    REFSEQ: accession NM_172027.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Kitamura,H., Ozono,E., Iwanaga,R., Bradford,A.P., Okuno,J.,
            Shimizu,E., Kurayoshi,K., Kugawa,K., Toh,H. and Ohtani,K.
  TITLE     Identification of novel target genes specifically activated by
            deregulated E2F in human normal fibroblasts
  JOURNAL   Genes Cells 20 (9), 739-757 (2015)
   PUBMED   26201719
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Koiwai,K., Maezawa,S., Hayano,T., Iitsuka,M. and Koiwai,O.
  TITLE     BPOZ-2 directly binds to eEF1A1 to promote eEF1A1 ubiquitylation
            and degradation and prevent translation
  JOURNAL   Genes Cells 13 (6), 593-607 (2008)
   PUBMED   18459963
  REMARK    GeneRIF: BPOZ-2 promoted eEF1A1 ubiquitylation and degradation,
            suggesting that eEF1A1 is a substrate of BPOZ-2.
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Maezawa,S., Hayano,T., Koiwai,K., Fukushima,R., Kouda,K., Kubota,T.
            and Koiwai,O.
  TITLE     Bood POZ containing gene type 2 is a human counterpart of yeast
            Btb3p and promotes the degradation of terminal
            deoxynucleotidyltransferase
  JOURNAL   Genes Cells 13 (5), 439-457 (2008)
   PUBMED   18429817
  REMARK    GeneRIF: Study showed that BPOZ-2 is a human counterpart of yeast
            Btb3p, which is a putative adaptor for Pcu3p-based ubiquitin
            ligase; BPOZ-2 bound to E3 ligase CUL3 in vitro and in vivo.
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Unoki,M. and Nakamura,Y.
  TITLE     Growth-suppressive effects of BPOZ and EGR2, two genes involved in
            the PTEN signaling pathway
  JOURNAL   Oncogene 20 (33), 4457-4465 (2001)
   PUBMED   11494141
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Dai,K.S., Wei,W. and Liew,C.C.
  TITLE     Molecular cloning and characterization of a novel human gene
            containing ankyrin repeat and double BTB/POZ domain
  JOURNAL   Biochem Biophys Res Commun 273 (3), 991-996 (2000)
   PUBMED   10891360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF664138.1, AB053325.1,
            AI337369.1 and BM671027.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein with an ankyrin repeat region
            and two BTB/POZ domains, which are thought to be involved in
            protein-protein interactions. Expression of this gene is activated
            by the phosphatase and tensin homolog, a tumor suppressor.
            Alternate splicing results in three transcript variants. [provided
            by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (2, also known as BPOZ type 2)
            encodes the longer isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1171313.1,
                                           SRR3476690.727347.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000232744.13/ ENSP00000232744.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.3"
     Protein         1..478
                     /product="ankyrin repeat and BTB/POZ domain-containing
                     protein 1 isoform 2"
                     /note="elongation factor 1A-binding protein; ankyrin
                     repeat and BTB (POZ) domain containing 1"
                     /calculated_mol_wt=53848
     Region          1..31
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969K4.1)"
     Region          <6..118
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          35..66
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          35..64
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969K4.1)"
     Region          97..214
                     /region_name="BTB1_POZ_ABTB1_BPOZ1"
                     /note="first BTB (Broad-Complex, Tramtrack and Bric a
                     brac)/POZ (poxvirus and zinc finger) domain found in
                     Ankyrin repeat and BTB/POZ domain-containing protein 1
                     (ABTB1); cd18295"
                     /db_xref="CDD:349604"
     Region          254..377
                     /region_name="BTB2_POZ_ABTB1_BPOZ1"
                     /note="second BTB (Broad-Complex, Tramtrack and Bric a
                     brac)/POZ (poxvirus and zinc finger) domain found in
                     Ankyrin repeat and BTB/POZ domain-containing protein 1
                     (ABTB1); cd18296"
                     /db_xref="CDD:349605"
     Region          376..447
                     /region_name="BACK_ABTB1_BPOZ"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     ankyrin repeat and BTB/POZ domain-containing protein 1
                     (ABTB1); cd18497"
                     /db_xref="CDD:350572"
     CDS             1..478
                     /gene="ABTB1"
                     /gene_synonym="BPOZ; BPOZ-2; BTB3; BTBD21; EF1ABP; PP2259"
                     /coded_by="NM_172027.3:75..1511"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3045.1"
                     /db_xref="GeneID:80325"
                     /db_xref="HGNC:HGNC:18275"
                     /db_xref="MIM:608308"
ORIGIN      
        1 mdtsdlfasc rkgdvgrvry lleqrdvevn vrdkwdstpl yyaclcghee lvlyllanga
       61 rceantfdge rclygalsdp irralrdykq vtascrrrdy yddflqrlle qgihsdvvfv
      121 vhgkpfrvhr cvlgarsayf anmldtkwkg ksvvvlrhpl inpvafgall qylytgrldi
      181 gvehvsdcer lakqcqlwdl lsdleakcek vsefvaskpg tcvkvltiep ppadprlred
      241 malladcalp pelrgdlwel pfpcpdgfns cpdicfrvag csflchkaff cgrsdyfral
      301 lddhfresee patsggppav tlhgispdvf thvlyymysd htelspeaay dvlsvadmyl
      361 lpglkrlcgr slaqmldedt vvgvwrvakl frlarledqc teymakviek lveredfvea
      421 vkeeaaavaa rqetdsiplv ddirfhvast vqtysaieea qqrlraledl lvsigldc
//
LOCUS       NP_001356863             643 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001356863 XP_016884498
VERSION     NP_001356863.1
DBSOURCE    REFSEQ: accession NM_001369934.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            On Apr 24, 2019 this sequence version replaced XP_016884498.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.141156.1,
                                           SRR1803615.268648.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..643
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 9"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=73067
     Region          355..394
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..643
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369934.1:359..2290"
                     /note="isoform 9 is encoded by transcript variant 17"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mqkrlhrsvf ltflrmsthk eskdhfisps afgeilynnf lfdipkildl cvlfgkgnsp
       61 llqkmignif tqqpsyysdl detlptilqv fsnilqhcgl qgdganttpq kleergrltp
      121 sdmpllelkd ivlylcdtct tlwafldifp lacqtfqkhd fcyrlasfye aaipemesai
      181 kkrrledskl lgdlwqrlsh srkklmeifh iilnqicllp ilesscdniq gfieeflqif
      241 ssllqekrfl rdydalfpva edisllqqas svldetrtay ilqavesawe gvdrrkatda
      301 kdpsvieepn gepngvtvta eavsqasshp enseeeecmg aaaavgpamc gveldslisq
      361 vkdllpdlge gfilacleyy hydpeqvinn ileerlaptl sqldrnldre mkpdptpllt
      421 srhnvfqnde fdvfsrdsvd lsrvhkgkst rkeentrsll ndkravaaqr qryeqysvvv
      481 eevplqpges lpyhsvyyed eyddtydgnq vgandadsdd elisrrpfti pqvlrtkvpr
      541 egqeedddde eddadeeapk pdhfvqdpav lrekaearrm aflakkgyrh dsstavagsp
      601 rghgqsrett qerrkkeank atranhnrrt madrkrskgm ips
//
LOCUS       NP_766044                368 aa            linear   ROD 27-APR-2025
DEFINITION  nuclease EXOG, mitochondrial isoform 1 precursor [Mus musculus].
ACCESSION   NP_766044
VERSION     NP_766044.1
DBSOURCE    REFSEQ: accession NM_172456.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Man,J.C.K., Mohan,R.A., Boogaard,M.V.D., Hilvering,C.R.E.,
            Jenkins,C., Wakker,V., Bianchi,V., Laat,W., Barnett,P.,
            Boukens,B.J. and Christoffels,V.M.
  TITLE     An enhancer cluster controls gene activity and topology of the
            SCN5A-SCN10A locus in vivo
  JOURNAL   Nat Commun 10 (1), 4943 (2019)
   PUBMED   31666509
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Szczesny,B., Brunyanszki,A., Olah,G., Mitra,S. and Szabo,C.
  TITLE     Opposing roles of mitochondrial and nuclear PARP1 in the regulation
            of mitochondrial and nuclear DNA integrity: implications for the
            regulation of mitochondrial function
  JOURNAL   Nucleic Acids Res 42 (21), 13161-13173 (2014)
   PUBMED   25378300
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC166052.5 and AC121922.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK162566.1, AK028887.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 71.33 cM"
     Protein         1..368
                     /product="nuclease EXOG, mitochondrial isoform 1
                     precursor"
                     /EC_number="3.1.30.-"
                     /note="endonuclease G-like 1; nuclease EXOG,
                     mitochondrial; endo G-like 1; endo/exonuclease (5'-3'),
                     endonuclease G-like"
                     /calculated_mol_wt=37043
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q8C163.1)"
                     /calculated_mol_wt=4359
     mat_peptide     42..368
                     /product="Nuclease EXOG, mitochondrial.
                     /id=PRO_0000342610"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8C163.1)"
                     /calculated_mol_wt=37043
     Region          77..287
                     /region_name="NUC"
                     /note="DNA/RNA non-specific endonuclease; smart00477"
                     /db_xref="CDD:214683"
     Site            order(137..138,140,171,179,183)
                     /site_type="active"
                     /db_xref="CDD:238043"
     Site            order(137..138,183)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238043"
     Site            171
                     /site_type="other"
                     /note="Mg2+ binding site [ion binding]"
                     /db_xref="CDD:238043"
     Region          302..350
                     /region_name="Exog_C"
                     /note="Endo/exonuclease (EXOG) C-terminal domain;
                     pfam18026"
                     /db_xref="CDD:465620"
     CDS             1..368
                     /gene="Exog"
                     /gene_synonym="Endogl1; Endogl2; Engl; ENGL-a; ENGL-B;
                     Engla; Englb"
                     /coded_by="NM_172456.4:29..1135"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS23616.1"
                     /db_xref="GeneID:208194"
                     /db_xref="MGI:MGI:2143333"
ORIGIN      
        1 maaksfasrl rdsrrflngf lagavvgaag agltalqffr rpdaesakla rqphesaeea
       61 vleqfgfpla gtetrrytnh alsydqakrv prwvlehisk dkiigdadrk hckfkpdpsv
      121 psafsalned yigsgwsrgh mapagnnkfs seamaetfyl snivpqnfdn nsgywnriem
      181 ycrelterfe dvwivsgplt lphtrndgtk tvsyqviged nvavpshlyk vilarrspes
      241 teplalgafv vpnkaigfqs qlsefqvslh dlekmsglvf fprldrsrdi rnicsvdtck
      301 llgfqeftly lstrkidgar svarlekvle alkssgvepd dyflsryekk leelkakeqk
      361 daqlekqs
//
LOCUS       NP_115784               1483 aa            linear   PRI 27-APR-2025
DEFINITION  tyrosine-protein kinase BAZ1B [Homo sapiens].
ACCESSION   NP_115784
VERSION     NP_115784.1
DBSOURCE    REFSEQ: accession NM_032408.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1483)
  AUTHORS   Salvati,A., Melone,V., Sellitto,A., Rizzo,F., Tarallo,R.,
            Nyman,T.A., Giurato,G., Nassa,G. and Weisz,A.
  TITLE     Combinatorial targeting of a chromatin complex comprising Dot1L,
            menin and the tyrosine kinase BAZ1B reveals a new therapeutic
            vulnerability of endocrine therapy-resistant breast cancer
  JOURNAL   Breast Cancer Res 24 (1), 52 (2022)
   PUBMED   35850772
  REMARK    GeneRIF: Combinatorial targeting of a chromatin complex comprising
            Dot1L, menin and the tyrosine kinase BAZ1B reveals a new
            therapeutic vulnerability of endocrine therapy-resistant breast
            cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1483)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1483)
  AUTHORS   Yang,L., Du,C., Chen,H. and Diao,Z.
  TITLE     Downregulation of Williams syndrome transcription factor (WSTF)
            suppresses glioblastoma cell growth and invasion by inhibiting
            PI3K/AKT signal pathway
  JOURNAL   Eur J Histochem 65 (4), 3255 (2021)
   PUBMED   34784707
  REMARK    GeneRIF: Downregulation of Williams syndrome transcription factor
            (WSTF) suppresses glioblastoma cell growth and invasion by
            inhibiting PI3K/AKT signal pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1483)
  AUTHORS   Jiang,D., Ren,C., Yang,L., Li,F., Yang,X., Zheng,Y., Ji,X. and
            Tian,Y.
  TITLE     Williams syndrome transcription factor promotes proliferation and
            invasion of cervical cancer cells by regulating PI3K/Akt signaling
            pathway
  JOURNAL   J Obstet Gynaecol Res 47 (7), 2433-2441 (2021)
   PUBMED   34028125
  REMARK    GeneRIF: Williams syndrome transcription factor promotes
            proliferation and invasion of cervical cancer cells by regulating
            PI3K/Akt signaling pathway.
REFERENCE   5  (residues 1 to 1483)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1483)
  AUTHORS   Bozhenok,L., Wade,P.A. and Varga-Weisz,P.
  TITLE     WSTF-ISWI chromatin remodeling complex targets heterochromatic
            replication foci
  JOURNAL   EMBO J 21 (9), 2231-2241 (2002)
   PUBMED   11980720
  REMARK    Erratum:[EMBO J 2002 Jun 17;21(12):3212]
REFERENCE   7  (residues 1 to 1483)
  AUTHORS   Pascual,J., Martinez-Yamout,M., Dyson,H.J. and Wright,P.E.
  TITLE     Structure of the PHD zinc finger from human Williams-Beuren
            syndrome transcription factor
  JOURNAL   J Mol Biol 304 (5), 723-729 (2000)
   PUBMED   11124022
REFERENCE   8  (residues 1 to 1483)
  AUTHORS   Jones,M.H., Hamana,N., Nezu,Ji. and Shimane,M.
  TITLE     A novel family of bromodomain genes
  JOURNAL   Genomics 63 (1), 40-45 (2000)
   PUBMED   10662543
REFERENCE   9  (residues 1 to 1483)
  AUTHORS   Lu,X., Meng,X., Morris,C.A. and Keating,M.T.
  TITLE     A novel human gene, WSTF, is deleted in Williams syndrome
  JOURNAL   Genomics 54 (2), 241-249 (1998)
   PUBMED   9828126
REFERENCE   10 (residues 1 to 1483)
  AUTHORS   Peoples,R.J., Cisco,M.J., Kaplan,P. and Francke,U.
  TITLE     Identification of the WBSCR9 gene, encoding a novel transcriptional
            regulator, in the Williams-Beuren syndrome deletion at 7q11.23
  JOURNAL   Cytogenet Cell Genet 82 (3-4), 238-246 (1998)
   PUBMED   9858827
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005089.3, DA739467.1,
            BC136520.1 and AF084479.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the bromodomain protein
            family. The bromodomain is a structural motif characteristic of
            proteins involved in chromatin-dependent regulation of
            transcription. This gene is deleted in Williams-Beuren syndrome, a
            developmental disorder caused by deletion of multiple genes at
            7q11.23. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.865389.1, AF084479.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000339594.9/ ENSP00000342434.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..1483
                     /product="tyrosine-protein kinase BAZ1B"
                     /EC_number="2.7.10.2"
                     /note="transcription factor WSTF; hWALp2; williams
                     syndrome transcription factor; williams-Beuren syndrome
                     chromosomal region 9 protein; williams-Beuren syndrome
                     chromosomal region 10 protein"
                     /calculated_mol_wt=170772
     Region          21..120
                     /region_name="WAC_Acf1_DNA_bd"
                     /note="ATP-utilizing chromatin assembly and remodelling
                     N-terminal; pfam10537"
                     /db_xref="CDD:463140"
     Region          145..212
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z277; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z277; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z277; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Region          207..213
                     /region_name="C motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Region          302..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Region          379..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Region          446..470
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Region          604..668
                     /region_name="DDT"
                     /note="domain in different transcription and chromosome
                     remodeling factors; smart00571"
                     /db_xref="CDD:214726"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            716
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Region          727..767
                     /region_name="WHIM1"
                     /note="WSTF, HB1, Itc1p, MBD9 motif 1; pfam15612"
                     /db_xref="CDD:464774"
     Region          <763..905
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          788..817
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Region          898..1025
                     /region_name="WSD"
                     /note="Williams-Beuren syndrome DDT (WSD), D-TOX E motif;
                     pfam15613"
                     /db_xref="CDD:464775"
     Site            947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Region          1186..1231
                     /region_name="PHD_BAZ1B"
                     /note="PHD finger found in bromodomain adjacent to zinc
                     finger domain protein 1B (BAZ1B); cd15628"
                     /db_xref="CDD:277098"
     Site            order(1186,1198..1202,1206,1226)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277098"
     Region          1237..1326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            1315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            1335
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z277; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            1342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Region          1344..1440
                     /region_name="Bromo_WSTF_like"
                     /note="Bromodomain; Williams syndrome transcription
                     factor-like subfamily (WSTF-like). The Williams-Beuren
                     syndrome deletion transcript 9 is a putative
                     transcriptional regulator. WSTF was found to play a role
                     in vitamin D-mediated transcription as part of two...;
                     cd05505"
                     /db_xref="CDD:99937"
     Site            order(1368,1373,1376,1415,1419,1425)
                     /site_type="other"
                     /note="putative acetyllysine binding site [chemical
                     binding]"
                     /db_xref="CDD:99937"
     Region          1455..1483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     Site            1468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UIG0.2)"
     CDS             1..1483
                     /gene="BAZ1B"
                     /gene_synonym="WBSCR10; WBSCR9; WSTF"
                     /coded_by="NM_032408.4:361..4812"
                     /db_xref="CCDS:CCDS5549.1"
                     /db_xref="GeneID:9031"
                     /db_xref="HGNC:HGNC:961"
                     /db_xref="MIM:605681"
ORIGIN      
        1 mapllgrkpf plvkplpgee plftiphtqe afrtreeyea rleryseriw tckstgssql
       61 thkeaweeeq evaellkeef pawyeklvle mvhhntasle klvdtawlei mtkyavgeec
      121 dfevgkekml kvkivkihpl ekvdeeatek ksdgacdsps sdkenssqia qdhqkketvv
      181 kedegrresi ndrarrsprk lptslkkger kwappkflph kydvklqned kiisnvpads
      241 lirterppnk eivryfirhn alragtgena pwvvedelvk kyslpskfsd flldpykymt
      301 lnpstkrknt gspdrkpskk sktdnsslss plnpklwchv hlkkslsgsp lkvknsknsk
      361 speehleemm kmmspnklht nfhipkkgpp akkpgkhsdk plkakgrskg ilngqkstgn
      421 skspkkglkt pktkmkqmtl ldmakgtqkm traprnsggt prtsskphkh lppaalhlia
      481 yykenkdred krsalscvis ktarllssed rarlpeelrs lvqkryelle hkkrwasmse
      541 eqrkeylkkk reelkkklke kakerrekem lerlekqkry edqeltgknl pafrlvdtpe
      601 glpntlfgdv amvveflscy sglllpdaqy pitavslmea lsadkggfly lnrvlvillq
      661 tllqdeiaed ygelgmklse ipltlhsvse lvrlclrrsd vqeesegsdt ddnkdsaafe
      721 dnevqdefle kletseffel tseeklqilt alchrilmty svqdhmetrq qmsaelwker
      781 lavlkeendk kraekqkrke meaknkengk venglgktdr kkeivkfepq vdteaedmis
      841 avksrrllai qakkereiqe remkvklerq aeeerirkhk aaaekafqeg iakaklvmrr
      901 tpigtdrnhn rywlfsdevp glfiekgwvh dsidyrfnhh ckdhtvsgde dycprskkan
      961 lgknasmntq hgtatevave tttpkqgqnl wflcdsqkel dellnclhpq giresqlker
     1021 lekryqdiih sihlarkpnl glkscdgnqe llnflrsdli evatrlqkgg lgyveetsef
     1081 earvislekl kdfgecvial qasvikkflq gfmapkqkrr klqsedsakt eevdeekkmv
     1141 eeakvasale kwktaireaq tfsrmhvllg mldacikwdm saenarckvc rkkgeddkli
     1201 lcdecnkafh lfclrpalye vpdgewqcpa cqpatarrns rgrnyteesa sedseddesd
     1261 eeeeeeeeee eeedyevagl rlrprktirg khsvippaar sgrrpgkkph strrsqpkap
     1321 pvddaevdel vlqtkrssrr qslelqkcee ilhkivkyrf swpfrepvtr deaedyydvi
     1381 thpmdfqtvq nkcscgsyrs vqefltdmkq vftnaevync rgshvlscmv kteqclvall
     1441 hkhlpghpyv rrkrkkfpdr laedegdsep eavgqsrgrr qkk
//
LOCUS       NP_038201                290 aa            linear   ROD 27-APR-2025
DEFINITION  sodium/potassium-transporting ATPase subunit beta-2 [Mus musculus].
ACCESSION   NP_038201
VERSION     NP_038201.1
DBSOURCE    REFSEQ: accession NM_013415.6
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Collin,G.B., Gogna,N., Chang,B., Damkham,N., Pinkney,J., Hyde,L.F.,
            Stone,L., Naggert,J.K., Nishina,P.M. and Krebs,M.P.
  TITLE     Mouse Models of Inherited Retinal Degeneration with Photoreceptor
            Cell Loss
  JOURNAL   Cells 9 (4), 931 (2020)
   PUBMED   32290105
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Litan,A., Li,Z., Tokhtaeva,E., Kelly,P., Vagin,O. and Langhans,S.A.
  TITLE     A Functional Interaction Between Na,K-ATPase beta2-Subunit/AMOG and
            NF2/Merlin Regulates Growth Factor Signaling in Cerebellar Granule
            Cells
  JOURNAL   Mol Neurobiol 56 (11), 7557-7571 (2019)
   PUBMED   31062247
  REMARK    GeneRIF: a functional link between the Na,K-ATPase beta2-subunit
            and Merlin/NF2 and suggest a role for the beta2-subunit in
            regulating cytoskeletal dynamics and Hippo/YAP signaling during
            neuronal differentiation, is reported.
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Buenaventura,D.F., Corseri,A. and Emerson,M.M.
  TITLE     Identification of Genes With Enriched Expression in Early
            Developing Mouse Cone Photoreceptors
  JOURNAL   Invest Ophthalmol Vis Sci 60 (8), 2787-2799 (2019)
   PUBMED   31260032
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Plossl,K., Straub,K., Schmid,V., Strunz,F., Wild,J., Merkl,R.,
            Weber,B.H.F. and Friedrich,U.
  TITLE     Identification of the retinoschisin-binding site on the retinal
            Na/K-ATPase
  JOURNAL   PLoS One 14 (5), e0216320 (2019)
   PUBMED   31048931
  REMARK    GeneRIF: These and previous results led us to suggest an
            induced-fit binding mechanism for the interaction between
            retinoschisin and the Na/K-ATPase, which is dependent on threonine
            240 in ATP1B2 allowing the accommodation of hyperflexible
            retinoschisin spikes by the associated protein-protein interaction
            patch on ATP1B2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Ding,B., Walton,J.P., Zhu,X. and Frisina,R.D.
  TITLE     Age-related changes in Na, K-ATPase expression, subunit isoform
            selection and assembly in the stria vascularis lateral wall of
            mouse cochlea
  JOURNAL   Hear Res 367, 59-73 (2018)
   PUBMED   30029086
  REMARK    GeneRIF: Functional selection and assembly of NKA subunit isoforms
            occurs in the cochlear stria vascularis lateral wall, which is
            disrupted and dysregulated with age.
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Shyjan,A.W., Canfield,V.A. and Levenson,R.
  TITLE     Evolution of the Na,K- and H,K-ATPase beta subunit gene family:
            structure of the murine Na,K-ATPase beta 2 subunit gene
  JOURNAL   Genomics 11 (2), 435-442 (1991)
   PUBMED   1663071
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hearne,C.M., McAleer,M.A., Love,J.M., Aitman,T.J., Cornall,R.J.,
            Ghosh,S., Knight,A.M., Prins,J.B. and Todd,J.A.
  TITLE     Additional microsatellite markers for mouse genome mapping
  JOURNAL   Mamm Genome 1 (4), 273-282 (1991)
   PUBMED   1794058
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Magyar,J.P. and Schachner,M.
  TITLE     Genomic structure of the adhesion molecule on glia (AMOG,
            Na/K-ATPase beta 2 subunit)
  JOURNAL   Nucleic Acids Res 18 (22), 6695-6696 (1990)
   PUBMED   1701244
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Hsieh,C.L., Cheng-Deutsch,A., Gloor,S., Schachner,M. and Francke,U.
  TITLE     Assignment of Amog (adhesion molecule on glia) gene to mouse
            chromosome 11 near Zfp-3 and Asgr-1,2 and to human chromosome 17
  JOURNAL   Somat Cell Mol Genet 16 (4), 401-405 (1990)
   PUBMED   1699290
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Gloor,S., Antonicek,H., Sweadner,K.J., Pagliusi,S., Frank,R.,
            Moos,M. and Schachner,M.
  TITLE     The adhesion molecule on glia (AMOG) is a homologue of the beta
            subunit of the Na,K-ATPase
  JOURNAL   J Cell Biol 110 (1), 165-174 (1990)
   PUBMED   1688561
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK141786.1, AK158321.1 and CX204070.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.233519.1,
                                           SRR1660815.278250.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849382, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 42.86 cM"
     Protein         1..290
                     /product="sodium/potassium-transporting ATPase subunit
                     beta-2"
                     /EC_number="7.2.2.13"
                     /note="glial cell adhesion molecule;
                     sodium/potassium-dependent ATPase subunit beta-2; adhesion
                     molecule in glia"
                     /calculated_mol_wt=33213
     Region          2..289
                     /region_name="Na_K_ATPase_bet"
                     /note="Sodium Potassium ATPase beta subunit; TIGR01107"
                     /db_xref="CDD:273446"
     Site            40..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14231.2)"
     Site            96
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14231.2)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P14231.2)"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14231.2)"
     Region          193..290
                     /region_name="immunoglobulin-like. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P14231.2)"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14231.2)"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14231.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14231.2)"
     Site            238
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P14231.2)"
     CDS             1..290
                     /gene="Atp1b2"
                     /gene_synonym="Amog; Atpb-2"
                     /coded_by="NM_013415.6:589..1461"
                     /db_xref="CCDS:CCDS24898.1"
                     /db_xref="GeneID:11932"
                     /db_xref="MGI:MGI:88109"
ORIGIN      
        1 mviqkekksc gqvveewkef vwnprthqfm grtgtswafi llfylvfygf ltamfsltmw
       61 vmlqtvsdht pkyqdrlatp glmirpkten ldvivnisdt eswgqhvqkl nkflepynds
      121 iqaqkndvcr pgryyeqpdn gvlnypkrac qfnrtqlgdc sgigdpthyg ystgqpcvfi
      181 kmnrvinfya ganqsmnvtc vgkrdedaen lghfvmfpan gsidlmyfpy ygkkfhvnyt
      241 qplvavkfln vtpnvevnve crinaaniat dderdkfagr vafklrinkt
//
LOCUS       NP_001185                889 aa            linear   PRI 27-APR-2025
DEFINITION  potassium/sodium hyperpolarization-activated cyclic
            nucleotide-gated channel 2 [Homo sapiens].
ACCESSION   NP_001185
VERSION     NP_001185.3
DBSOURCE    REFSEQ: accession NM_001194.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Pai,V.P. and Levin,M.
  TITLE     HCN2 channel-induced rescue of brain, eye, heart and gut
            teratogenesis caused by nicotine, ethanol and aberrant notch
            signalling
  JOURNAL   Wound Repair Regen 30 (6), 681-706 (2022)
   PUBMED   35662339
  REMARK    GeneRIF: HCN2 channel-induced rescue of brain, eye, heart and gut
            teratogenesis caused by nicotine, ethanol and aberrant notch
            signalling.
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Lin,W., Qin,J., Ni,G., Li,Y., Xie,H., Yu,J., Li,H., Sui,L., Guo,Q.,
            Fang,Z. and Zhou,L.
  TITLE     Downregulation of hyperpolarization-activated cyclic
            nucleotide-gated channels (HCN) in the hippocampus of patients with
            medial temporal lobe epilepsy and hippocampal sclerosis (MTLE-HS)
  JOURNAL   Hippocampus 30 (10), 1112-1126 (2020)
   PUBMED   32543742
  REMARK    GeneRIF: Downregulation of hyperpolarization-activated cyclic
            nucleotide-gated channels (HCN) in the hippocampus of patients with
            medial temporal lobe epilepsy and hippocampal sclerosis (MTLE-HS).
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Zhao,H., Wang,F., Tang,Y., Wang,X., Wang,T., Zhao,Q. and Huang,C.
  TITLE     HCN2 and TBX3 Reprogram Human-Induced Pluripotent Stem
            Cells-Derived Cardiomyocytes into Pacemaker-Like Cells
  JOURNAL   DNA Cell Biol 39 (2), 289-298 (2020)
   PUBMED   31916853
  REMARK    GeneRIF: overexpression of TBX3 and HCN2 could reprogram
            human-induced pluripotent stem cells-derived cardiomyocytes into
            pacemaker-like cells
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Thomas,M., Ranjith,G., Radhakrishnan,A. and Arun Anirudhan,V.
  TITLE     Effects of HCN2 Mutations on Dendritic Excitability and Synaptic
            Plasticity: A Computational Study
  JOURNAL   Neuroscience 423, 148-161 (2019)
   PUBMED   31682955
  REMARK    GeneRIF: Effects of HCN2 Mutations on Dendritic Excitability and
            Synaptic Plasticity: A Computational Study.
REFERENCE   5  (residues 1 to 889)
  AUTHORS   Li,M., Maljevic,S., Phillips,A.M., Petrovski,S., Hildebrand,M.S.,
            Burgess,R., Mount,T., Zara,F., Striano,P., Schubert,J., Thiele,H.,
            Nurnberg,P., Wong,M., Weisenberg,J.L., Thio,L.L., Lerche,H.,
            Scheffer,I.E., Berkovic,S.F., Petrou,S. and Reid,C.A.
  TITLE     Gain-of-function HCN2 variants in genetic epilepsy
  JOURNAL   Hum Mutat 39 (2), 202-209 (2018)
   PUBMED   29064616
  REMARK    GeneRIF: Data suggest that HCN2 variants can confer susceptibility
            to Genetic generalized epilepsy via a gain-of-function mechanism.
REFERENCE   6  (residues 1 to 889)
  AUTHORS   Vaccari,T., Moroni,A., Rocchi,M., Gorza,L., Bianchi,M.E.,
            Beltrame,M. and DiFrancesco,D.
  TITLE     The human gene coding for HCN2, a pacemaker channel of the heart
  JOURNAL   Biochim Biophys Acta 1446 (3), 419-425 (1999)
   PUBMED   10524219
REFERENCE   7  (residues 1 to 889)
  AUTHORS   Ludwig,A., Zong,X., Stieber,J., Hullin,R., Hofmann,F. and Biel,M.
  TITLE     Two pacemaker channels from human heart with profoundly different
            activation kinetics
  JOURNAL   EMBO J 18 (9), 2323-2329 (1999)
   PUBMED   10228147
REFERENCE   8  (residues 1 to 889)
  AUTHORS   Kleiderlein,J.J., Nisson,P.E., Jessee,J., Li,W.B., Becker,K.G.,
            Derby,M.L., Ross,C.A. and Margolis,R.L.
  TITLE     CCG repeats in cDNAs from human brain
  JOURNAL   Hum Genet 103 (6), 666-673 (1998)
   PUBMED   9921901
  REMARK    Erratum:[Hum Genet 1999 Jan;104(1):113]
REFERENCE   9  (residues 1 to 889)
  AUTHORS   Santoro,B., Liu,D.T., Yao,H., Bartsch,D., Kandel,E.R.,
            Siegelbaum,S.A. and Tibbs,G.R.
  TITLE     Identification of a gene encoding a hyperpolarization-activated
            pacemaker channel of brain
  JOURNAL   Cell 93 (5), 717-729 (1998)
   PUBMED   9630217
REFERENCE   10 (residues 1 to 889)
  AUTHORS   Santoro,B., Grant,S.G., Bartsch,D. and Kandel,E.R.
  TITLE     Interactive cloning with the SH3 domain of N-src identifies a new
            brain specific ion channel protein, with homology to eag and cyclic
            nucleotide-gated channels
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14815-14820 (1997)
   PUBMED   9405696
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005559.2, AJ012582.1,
            BC039619.1 and AF065164.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 16, 2007 this sequence version replaced NP_001185.2.
            
            Summary: The protein encoded by this gene is a
            hyperpolarization-activated cation channel involved in the
            generation of native pacemaker activity in the heart and in the
            brain. The encoded protein is activated by cAMP and can produce a
            fast, large current. Defects in this gene were noted as a possible
            cause of some forms of epilepsy. [provided by RefSeq, Jan 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ012582.1, AF065164.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000251287.3/ ENSP00000251287.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..889
                     /product="potassium/sodium hyperpolarization-activated
                     cyclic nucleotide-gated channel 2"
                     /note="brain cyclic nucleotide-gated channel 2;
                     hyperpolarization activated cyclic nucleotide gated
                     potassium channel 2"
                     /calculated_mol_wt=96820
     Region          1..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Region          <57..185
                     /region_name="PBP1"
                     /note="PAB1-binding protein, interacts with
                     poly(A)-binding protein [RNA processing and modification];
                     COG5180"
                     /db_xref="CDD:444064"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Region          150..>688
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Region          158..209
                     /region_name="Involved in subunit assembly.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKA9; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            216..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            241..261
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            289..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            370..390
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            407
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            441..461
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Region          544..652
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(608..609,618..620)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(640..642,646..648)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG/PRKG2.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Region          754..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            754
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKA9; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            756
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            779
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     CDS             1..889
                     /gene="HCN2"
                     /gene_synonym="BCNG-2; BCNG2; EIG17; FEB2; GEFSP11; HAC-1"
                     /coded_by="NM_001194.4:66..2735"
                     /db_xref="CCDS:CCDS12035.1"
                     /db_xref="GeneID:610"
                     /db_xref="HGNC:HGNC:4846"
                     /db_xref="MIM:602781"
ORIGIN      
        1 mdarggggrp gespgatpap gpppppppap pqqqpppppp papppgpgpa ppqhppraea
       61 lppeaadegg prgrlrsrds scgrpgtpga astakgspng ecgrgepqcs pagpegparg
      121 pkvsfscrga asgpapgpgp aeeagseeag pageprgsqa sfmqrqfgal lqpgvnkfsl
      181 rmfgsqkave reqervksag awiihpysdf rfywdftmll fmvgnliiip vgitffkdet
      241 tapwivfnvv sdtfflmdlv lnfrtgivie dnteiildpe kikkkylrtw fvvdfvssip
      301 vdyiflivek gidsevykta ralrivrftk ilsllrllrl srliryihqw eeifhmtydl
      361 asavmricnl ismmlllchw dgclqflvpm lqdfprncwv singmvnhsw selysfalfk
      421 amshmlcigy grqapesmtd iwltmlsmiv gatcyamfig hataliqsld ssrrqyqeky
      481 kqveqymsfh klpadfrqki hdyyehryqg kmfdedsilg elngplreei vnfncrklva
      541 smplfanadp nfvtamltkl kfevfqpgdy iiregtigkk myfiqhgvvs vltkgnkemk
      601 lsdgsyfgei clltrgrrta svradtycrl yslsvdnfne vleeypmmrr afetvaidrl
      661 drigkknsil lhkvqhdlns gvfnnqenai iqeivkydre mvqqaelgqr vglfpppppp
      721 pqvtsaiatl qqaaamsfcp qvarplvgpl algsprlvrr pppgpapaaa spgppppasp
      781 pgapasprap rtspygglpa aplagpalpa rrlsrasrpl sasqpslphg apgpaastrp
      841 assstprlgp tpaaraaaps pdrrdsaspg aaggldpqds arsrlssnl
//
LOCUS       NP_001120648             262 aa            linear   PRI 27-APR-2025
DEFINITION  protein maestro isoform d [Homo sapiens].
ACCESSION   NP_001120648
VERSION     NP_001120648.1
DBSOURCE    REFSEQ: accession NM_001127176.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Kenigsberg,S., Lima,P.D., Maghen,L., Wyse,B.A., Lackan,C.,
            Cheung,A.N., Tsang,B.K. and Librach,C.L.
  TITLE     The elusive MAESTRO gene: Its human reproductive tissue-specific
            expression pattern
  JOURNAL   PLoS One 12 (4), e0174873 (2017)
   PUBMED   28406912
  REMARK    GeneRIF: study also shows a punctate nuclear expression pattern and
            disperse cytoplasmic expression pattern of the MRO protein in human
            granulosa-cumulus cells and in testicular germ cells, which was
            later validated by western blotting
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
  REMARK    GeneRIF: The sequence and function of the related mouse gene are
            described.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Yanaihara,N., Kohno,T., Takakura,S., Takei,K., Otsuka,A.,
            Sunaga,N., Takahashi,M., Yamazaki,M., Tashiro,H., Fukuzumi,Y.,
            Fujimori,Y., Hagiwara,K., Tanaka,T. and Yokota,J.
  TITLE     Physical and transcriptional map of a 311-kb segment of chromosome
            18q21, a candidate lung tumor suppressor locus
  JOURNAL   Genomics 72 (2), 169-179 (2001)
   PUBMED   11401430
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015864.5.
            
            Summary: This gene is specifically transcribed in males before and
            after differentiation of testis, and the encoded protein may play
            an important role in a mammalian sex determination. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.146928.1,
                                           SRR1803613.213381.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..262
                     /product="protein maestro isoform d"
                     /note="beside the Ma29 deletion; protein maestro;
                     male-specific transcription in the developing reproductive
                     organs"
                     /calculated_mol_wt=29961
     CDS             1..262
                     /gene="MRO"
                     /gene_synonym="B29; C18orf3"
                     /coded_by="NM_001127176.3:102..890"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS45868.1"
                     /db_xref="GeneID:83876"
                     /db_xref="HGNC:HGNC:24121"
                     /db_xref="MIM:608080"
ORIGIN      
        1 mawgskgiqg wenlaesshl attressppe sgtgsgssrg srlqepqvsw klrfqkrepl
       61 knvffilaer ardpsakkrh mamrnlgtma yeapdkvrky kkivldllvy glydpvnlev
      121 ihesmktltv vlgkiqgkgl gsffiditlq trtllddend slrysafvlf gqlaafagrk
      181 wkkfftsqvk qtrdsllihl qdrnpqvaka ckttfqacsp ylklkeeysf qseedqrntk
      241 lyqqlshyhp eilqffyank il
//
LOCUS       NP_997158                 90 aa            linear   ROD 27-APR-2025
DEFINITION  barrier-to-autointegration factor-like protein [Mus musculus].
ACCESSION   NP_997158 XP_130486
VERSION     NP_997158.1
DBSOURCE    REFSEQ: accession NM_207275.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Huang,C., Gong,H., Mu,B., Lan,X., Yang,C., Tan,J., Liu,W., Zou,Y.,
            Li,L., Feng,B., He,X., Luo,Q. and Chen,Z.
  TITLE     BAF-L Modulates Histone-to-Protamine Transition during
            Spermiogenesis
  JOURNAL   Int J Mol Sci 23 (4), 1985 (2022)
   PUBMED   35216101
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Niu,C.M., Xia,M.M., Zhong,Y.N. and Zheng,Y.
  TITLE     Mus musculus Barrier-To-Autointegration Factor 2 (Banf2) is Not
            Essential for Spermatogenesis or Fertility
  JOURNAL   Cytogenet Genome Res 161 (3-4), 167-177 (2021)
   PUBMED   33951625
  REMARK    GeneRIF: Mus musculus Barrier-To-Autointegration Factor 2 (Banf2)
            is Not Essential for Spermatogenesis or Fertility.
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Lu,Y., Oura,S., Matsumura,T., Oji,A., Sakurai,N., Fujihara,Y.,
            Shimada,K., Miyata,H., Tobita,T., Noda,T., Castaneda,J.M.,
            Kiyozumi,D., Zhang,Q., Larasati,T., Young,S.A.M., Kodani,M.,
            Huddleston,C.A., Robertson,M.J., Coarfa,C., Isotani,A.,
            Aitken,R.J., Okabe,M., Matzuk,M.M., Garcia,T.X. and Ikawa,M.
  TITLE     CRISPR/Cas9-mediated genome editing reveals 30 testis-enriched
            genes dispensable for male fertility in micedagger
  JOURNAL   Biol Reprod 101 (2), 501-511 (2019)
   PUBMED   31201419
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Tifft,K.E., Segura-Totten,M., Lee,K.K. and Wilson,K.L.
  TITLE     Barrier-to-autointegration factor-like (BAF-L): a proposed
            regulator of BAF
  JOURNAL   Exp Cell Res 312 (4), 478-487 (2006)
   PUBMED   16337940
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL928891.20.
            
            On Aug 30, 2004 this sequence version replaced XP_130486.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK076863.1, AV266439.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 70.91 cM"
     Protein         1..90
                     /product="barrier-to-autointegration factor-like protein"
                     /note="likely ortholog of H. sapiens Chromosome 20 open
                     reading frame 179 (C20orf179); barrier to autointegration
                     factor 2"
                     /calculated_mol_wt=10136
     Region          4..89
                     /region_name="BAF"
                     /note="Barrier to autointegration factor; cl03803"
                     /db_xref="CDD:470880"
     CDS             1..90
                     /gene="Banf2"
                     /gene_synonym="4930517K23Rik; Baf-L; Baf-like; Gm115"
                     /coded_by="NM_207275.2:190..462"
                     /db_xref="CCDS:CCDS16813.1"
                     /db_xref="GeneID:403171"
                     /db_xref="MGI:MGI:2684961"
ORIGIN      
        1 mddmsprlra flsepigekd vawvdgisre lainlvtkgf nkayvllgqf llmhkneaef
       61 qrwiicccga tecearqsst clkewcscfl
//
LOCUS       NP_001346463             693 aa            linear   ROD 27-APR-2025
DEFINITION  TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 [Mus
            musculus].
ACCESSION   NP_001346463 XP_017169562
VERSION     NP_001346463.1
DBSOURCE    REFSEQ: accession NM_001359534.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Li,N., Yun,B., Zeng,L., Lv,Y., Zhou,Y., Fang,M., Li,S., Chen,Y.,
            Huang,E., Zhang,L., Jiang,Y., Zhang,H., Li,J. and Yuan,X.
  TITLE     The antisense lncRNA of TAB2 that prevents oxidative stress to
            enhance the follicular growth in mammals
  JOURNAL   Commun Biol 7 (1), 1246 (2024)
   PUBMED   39358475
  REMARK    GeneRIF: The antisense lncRNA of TAB2 that prevents oxidative
            stress to enhance the follicular growth in mammals.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Ali,T., Nguyen,H.M., Abbas,N., Takeuchi,O., Akira,S., Suzuki,T.,
            Matsuzaki,G. and Takaesu,G.
  TITLE     TAK1-binding protein 2 (TAB2) and TAB3 are redundantly required for
            TLR-induced cytokine production in macrophages
  JOURNAL   Int Immunol 36 (9), 439-450 (2024)
   PUBMED   38567483
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Yao,X., Dong,R., Hu,S., Liu,Z., Cui,J., Hu,F., Cheng,X., Wang,X.,
            Ma,T., Tian,S., Zhang,X.J., Hu,Y., Bai,L., Li,H. and Zhang,P.
  TITLE     Tripartite motif 38 alleviates the pathological process of
            NAFLD-NASH by promoting TAB2 degradation
  JOURNAL   J Lipid Res 64 (7), 100382 (2023)
   PUBMED   37116711
  REMARK    GeneRIF: Tripartite motif 38 alleviates the pathological process of
            NAFLD-NASH by promoting TAB2 degradation.
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Zhang,J., Cao,L., Gao,A., Ren,R., Yu,L., Li,Q., Liu,Y., Qi,W.,
            Hou,Y., Sui,W., Su,G., Zhang,Y., Zhang,C. and Zhang,M.
  TITLE     E3 ligase RNF99 negatively regulates TLR-mediated inflammatory
            immune response via K48-linked ubiquitination of TAB2
  JOURNAL   Cell Death Differ 30 (4), 966-978 (2023)
   PUBMED   36681779
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Yin,H., Guo,X., Chen,Y., Zeng,Y., Mo,X., Hong,S., He,H., Li,J.,
            Steinmetz,R. and Liu,Q.
  TITLE     TAB2 deficiency induces dilated cardiomyopathy by promoting
            RIPK1-dependent apoptosis and necroptosis
  JOURNAL   J Clin Invest 132 (4) (2022)
   PUBMED   34990405
  REMARK    GeneRIF: TAB2 deficiency induces dilated cardiomyopathy by
            promoting RIPK1-dependent apoptosis and necroptosis.
REFERENCE   6  (residues 1 to 693)
  AUTHORS   Orelio,C. and Dzierzak,E.
  TITLE     Identification of 2 novel genes developmentally regulated in the
            mouse aorta-gonad-mesonephros region
  JOURNAL   Blood 101 (6), 2246-2249 (2003)
   PUBMED   12433684
  REMARK    GeneRIF: the expression of mouse TAB2 in the E11 dorsal aorta
            endothelium suggests a role for mTAB2 in hematopoietic stem cell
            emergence and/or regulation
REFERENCE   7  (residues 1 to 693)
  AUTHORS   Sanjo,H., Takeda,K., Tsujimura,T., Ninomiya-Tsuji,J., Matsumoto,K.
            and Akira,S.
  TITLE     TAB2 is essential for prevention of apoptosis in fetal liver but
            not for interleukin-1 signaling
  JOURNAL   Mol Cell Biol 23 (4), 1231-1238 (2003)
   PUBMED   12556483
  REMARK    GeneRIF: TAB2 is essential for embryonic development through
            prevention of liver apoptosis but not for the IL-1
            receptor-mediated signaling pathway.
REFERENCE   8  (residues 1 to 693)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Hara,Y., Nagase,T.,
            Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: I. The complete nucleotide sequences of 100 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 9 (5), 179-188 (2002)
   PUBMED   12465718
REFERENCE   9  (residues 1 to 693)
  AUTHORS   Baek,S.H., Ohgi,K.A., Rose,D.W., Koo,E.H., Glass,C.K. and
            Rosenfeld,M.G.
  TITLE     Exchange of N-CoR corepressor and Tip60 coactivator complexes links
            gene expression by NF-kappaB and beta-amyloid precursor protein
  JOURNAL   Cell 110 (1), 55-67 (2002)
   PUBMED   12150997
REFERENCE   10 (residues 1 to 693)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092856.26, AY093701.1, CN532534.1 and AW492243.1.
            
            On Jan 13, 2018 this sequence version replaced XP_017169562.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660811.79088.1,
                                           SRR9219383.161150.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164135
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 2.56 cM"
     Protein         1..693
                     /product="TGF-beta-activated kinase 1 and MAP3K7-binding
                     protein 2"
                     /note="TGF-beta-activated kinase 1-binding protein 2;
                     mitogen-activated protein kinase kinase kinase
                     7-interacting protein 2; Tak1 binding protein 2"
                     /calculated_mol_wt=76311
     Region          9..50
                     /region_name="CUE_TAB2_TAB3"
                     /note="CUE domain found in the N-terminal of
                     TGF-beta-activated kinase 1 and MAP3K7-binding proteins
                     TAB2, TAB3 and similar proteins; cd14362"
                     /db_xref="CDD:270545"
     Region          90..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99K90.1)"
     Site            173
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q99K90.1)"
     Region          223..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99K90.1)"
     Region          330..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99K90.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYJ8; propagated from
                     UniProtKB/Swiss-Prot (Q99K90.1)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYJ8; propagated from
                     UniProtKB/Swiss-Prot (Q99K90.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYJ8; propagated from
                     UniProtKB/Swiss-Prot (Q99K90.1)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99K90.1)"
     Region          540..>619
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     Site            582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYJ8; propagated from
                     UniProtKB/Swiss-Prot (Q99K90.1)"
     Region          640..663
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99K90.1)"
     Region          667..690
                     /region_name="ZnF_RBZ"
                     /note="Zinc finger domain; smart00547"
                     /db_xref="CDD:197784"
     Region          668..687
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     Region          675..685
                     /region_name="Interaction with polyubiquitin.
                     /evidence=ECO:0000269|PubMed:19927120"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99K90.1)"
     CDS             1..693
                     /gene="Tab2"
                     /gene_synonym="1110030N06Rik; A530078N03Rik; Map3k7ip2;
                     mKIAA0733"
                     /coded_by="NM_001359534.1:749..2830"
                     /db_xref="CCDS:CCDS23691.1"
                     /db_xref="GeneID:68652"
                     /db_xref="MGI:MGI:1915902"
ORIGIN      
        1 maqgshqidf qvlhdlrqkf pevpevvvsr cmlqnnnnld accavlsqes trylygegdl
       61 nfsdesgisg lrnhmtslnl dlqsqnvyhh gregsrvngs rtlthsvsdg qlhggqsnne
      121 lfqqepqtap aqvpqgfnvf gmpstsgasn stphlgfhlg skgtsnlsqq tprfnpimvt
      181 lapniqtgrs tptslhihgv pppvlnspqg nsiyirpyit tpsgtarqtq qhsgwvsqfn
      241 pmnpqqayqp sqpgpwttyp asnplphtst qqpnqqghqt shvympissp ttpqpptihs
      301 sgssqssahs qyniqnistg prknqieikl eppqrnsssk lrssgprtas tsslvnsqtl
      361 nrnqptvyia asppntdemi srsqpkvyis anatagdeqg mrnqptlfis tnsgpsaasr
      421 nmsgqvsmgp afihhhppks rvlggnsats prvvvtqpnt kytfkitvsp nkppavspgv
      481 vsptfeltnl lnhpdhyvet eniqhltdpa lahvdrisea rklsmgsdda aytqallvhq
      541 karmerlqre lemqkkkldk lksevnemen nltrrrlkrs nsisqipsle emqqlrscnr
      601 qlqididclt keidlfqarg phfnpsaihn fydnigfvgp vppkpkdqrs tikapktqda
      661 edeegaqwnc tactflnhpa lirceqcemp rhf
//
LOCUS       NP_038464               1128 aa            linear   PRI 27-APR-2025
DEFINITION  nck-associated protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_038464
VERSION     NP_038464.1
DBSOURCE    REFSEQ: accession NM_013436.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1128)
  AUTHORS   Noh,M.Y., Kwon,M.S., Oh,K.W., Nahm,M., Park,J., Kim,Y.E., Ki,C.S.,
            Jin,H.K., Bae,J.S. and Kim,S.H.
  TITLE     Role of NCKAP1 in the Defective Phagocytic Function of
            Microglia-Like Cells Derived from Rapidly Progressing Sporadic ALS
  JOURNAL   Mol Neurobiol 60 (8), 4761-4777 (2023)
   PUBMED   37154887
  REMARK    GeneRIF: Role of NCKAP1 in the Defective Phagocytic Function of
            Microglia-Like Cells Derived from Rapidly Progressing Sporadic ALS.
REFERENCE   2  (residues 1 to 1128)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1128)
  AUTHORS   Fan,Z.X., Xi,W., Miao,X.Y., Li,L.Y. and Miao,G.Y.
  TITLE     Circ_NCKAP1 promotes skin basal cell carcinoma progression by
            sponging the miR-148b-5p/HSP90 axis
  JOURNAL   Eur Rev Med Pharmacol Sci 25 (17), 5355-5364 (2021)
   PUBMED   34533810
  REMARK    GeneRIF: Circ_NCKAP1 promotes skin basal cell carcinoma progression
            by sponging the miR-148b-5p/HSP90 axis.
REFERENCE   4  (residues 1 to 1128)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1128)
  AUTHORS   Wang,X., Jiang,W., Luo,S., Yang,X., Wang,C., Wang,B., Dang,Y.,
            Shen,Y. and Ma,D.K.
  TITLE     The C. elegans homolog of human panic-disorder risk gene TMEM132D
            orchestrates neuronal morphogenesis through the WAVE-regulatory
            complex
  JOURNAL   Mol Brain 14 (1), 54 (2021)
   PUBMED   33726789
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1128)
  AUTHORS   Witke,W., Podtelejnikov,A.V., Di Nardo,A., Sutherland,J.D.,
            Gurniak,C.B., Dotti,C. and Mann,M.
  TITLE     In mouse brain profilin I and profilin II associate with regulators
            of the endocytic pathway and actin assembly
  JOURNAL   EMBO J 17 (4), 967-976 (1998)
   PUBMED   9463375
REFERENCE   7  (residues 1 to 1128)
  AUTHORS   Kobayashi,K., Kuroda,S., Fukata,M., Nakamura,T., Nagase,T.,
            Nomura,N., Matsuura,Y., Yoshida-Kubomura,N., Iwamatsu,A. and
            Kaibuchi,K.
  TITLE     p140Sra-1 (specifically Rac1-associated protein) is a novel
            specific target for Rac1 small GTPase
  JOURNAL   J Biol Chem 273 (1), 291-295 (1998)
   PUBMED   9417078
REFERENCE   8  (residues 1 to 1128)
  AUTHORS   Matuoka,K., Miki,H., Takahashi,K. and Takenawa,T.
  TITLE     A novel ligand for an SH3 domain of the adaptor protein Nck bears
            an SH2 domain and nuclear signaling motifs
  JOURNAL   Biochem Biophys Res Commun 239 (2), 488-492 (1997)
   PUBMED   9344857
REFERENCE   9  (residues 1 to 1128)
  AUTHORS   Kitamura,Y., Kitamura,T., Sakaue,H., Maeda,T., Ueno,H., Nishio,S.,
            Ohno,S., Osada,Si., Sakaue,M., Ogawa,W. and Kasuga,M.
  TITLE     Interaction of Nck-associated protein 1 with activated GTP-binding
            protein Rac
  JOURNAL   Biochem J 322 (Pt 3) (Pt 3), 873-878 (1997)
   PUBMED   9148763
REFERENCE   10 (residues 1 to 1128)
  AUTHORS   Kitamura,T., Kitamura,Y., Yonezawa,K., Totty,N.F., Gout,I.,
            Hara,K., Waterfield,M.D., Sakaue,M., Ogawa,W. and Kasuga,M.
  TITLE     Molecular cloning of p125Nap1, a protein that associates with an
            SH3 domain of Nck
  JOURNAL   Biochem Biophys Res Commun 219 (2), 509-514 (1996)
   PUBMED   8605018
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB011159.1, BC015025.1, CA314471.1 and AC108514.3.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the shorter isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015025.1, AB014509.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361354.9/ ENSP00000355348.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.1"
     Protein         1..1128
                     /product="nck-associated protein 1 isoform 1"
                     /note="membrane-associated protein HEM-2; nck-associated
                     protein 1"
                     /calculated_mol_wt=128660
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2A7.1)"
     Region          13..1122
                     /region_name="Nckap1"
                     /note="Nck-associated protein 1; pfam09735"
                     /db_xref="CDD:462866"
     Region          640..665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2A7.1)"
     Site            995..1015
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2A7.1)"
     CDS             1..1128
                     /gene="NCKAP1"
                     /gene_synonym="HEM2; NAP1; NAP125; p125Nap1"
                     /coded_by="NM_013436.5:359..3745"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2287.1"
                     /db_xref="GeneID:10787"
                     /db_xref="HGNC:HGNC:7666"
                     /db_xref="MIM:604891"
ORIGIN      
        1 msrsvlqpsq qklaekltil ndrgvgmltr lynikkacgd pkakpsylid knlesavkfi
       61 vrkfpavetr nnnqqlaqlq kekseilknl alyyftfvdv mefkdhvcel lntidvcqvf
      121 fditvnfdlt knyldliity ttlmillsri eerkaiigly nyahemthga sdreyprlgq
      181 mivdyenplk kmmeefvphs kslsdalisl qmvyprrnls adqwrnaqll slisapstml
      241 npaqsdtmpc eylsldamek wiifgfilch gilntdatal nlwklalqss sclslfrdev
      301 fhihkaaedl fvnirgynkr indireckea avshagsmhr errkflrsal kelatvlsdq
      361 pgllgpkalf vfmalsfard eiiwllrhad nmpkksaddf idkhiaelif ymeelrahvr
      421 kygpvmqryy vqylsgfdav vlnelvqnls vcpedesiim ssfvntmtsl svkqvedgev
      481 fdfrgmrldw frlqaytsvs kaslgladhr elgkmmntii fhtkmvdslv emlvetsdls
      541 ifcfysrafe kmfqqclelp sqsrysiafp llcthfmsct helcpeerhh igdrslslcn
      601 mfldemakqa rnlitdicte qctlsdqllp khcaktisqa vnkkskkqtg kkgeperekp
      661 gvesmrknrl vvtnldklht alselcfsin yvpnmvvweh tftpreylts hleirftksi
      721 vgmtmynqat qeiakpsell tsvraymtvl qsienyvqid itrvfnnvll qqtqhldshg
      781 eptitslytn wyletllrqv snghiayfpa mkafvnlpte neltfnaeey sdisemrsls
      841 ellgpygmkf lseslmwhis sqvaelkklv venvdvltqm rtsfdkpdqm aalfkrlssv
      901 dsvlkrmtii gvilsfrsla qealrdvlsy hipflvssie dfkdhipret dmkvamnvye
      961 lssaaglpce idpalvvals sqksenispe eeykiacllm vfvavslptl asnvmsqysp
     1021 aieghcnnih clakainqia aalftihkgs iedrlkefla lasssllkig qetdktttrn
     1081 resvyllldm ivqespfltm dllescfpyv llrnayhavy kqsvtssa
//
LOCUS       NP_113603                508 aa            linear   PRI 27-APR-2025
DEFINITION  gasdermin-C [Homo sapiens].
ACCESSION   NP_113603
VERSION     NP_113603.1
DBSOURCE    REFSEQ: accession NM_031415.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Li,M., Jiang,Q., Liu,X., Han,L., Chen,S. and Xue,R.
  TITLE     The Pyroptosis-Related Signature Composed of GSDMC Predicts
            Prognosis and Contributes to Growth and Metastasis of
            Hepatocellular Carcinoma
  JOURNAL   Front Biosci (Landmark Ed) 28 (10), 235 (2023)
   PUBMED   37919059
  REMARK    GeneRIF: The Pyroptosis-Related Signature Composed of GSDMC
            Predicts Prognosis and Contributes to Growth and Metastasis of
            Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Yan,C., Niu,Y., Li,F., Zhao,W. and Ma,L.
  TITLE     System analysis based on the pyroptosis-related genes identifies
            GSDMC as a novel therapy target for pancreatic adenocarcinoma
  JOURNAL   J Transl Med 20 (1), 455 (2022)
   PUBMED   36199146
  REMARK    GeneRIF: System analysis based on the pyroptosis-related genes
            identifies GSDMC as a novel therapy target for pancreatic
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Cui,Y.Q., Meng,F., Zhan,W.L., Dai,Z.T. and Liao,X.
  TITLE     High Expression of GSDMC Is Associated with Poor Survival in Kidney
            Clear Cell Cancer
  JOURNAL   Biomed Res Int 2021, 5282894 (2021)
   PUBMED   34778452
  REMARK    GeneRIF: High Expression of GSDMC Is Associated with Poor Survival
            in Kidney Clear Cell Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Zhang,J.Y., Zhou,B., Sun,R.Y., Ai,Y.L., Cheng,K., Li,F.N.,
            Wang,B.R., Liu,F.J., Jiang,Z.H., Wang,W.J., Zhou,D., Chen,H.Z. and
            Wu,Q.
  TITLE     The metabolite alpha-KG induces GSDMC-dependent pyroptosis through
            death receptor 6-activated caspase-8
  JOURNAL   Cell Res 31 (9), 980-997 (2021)
   PUBMED   34012073
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Jiang,H., Moro,A., Liu,Y., Wang,J., Meng,D., Zhan,X. and Wei,Q.
  TITLE     Two GWAS-identified variants are associated with lumbar spinal
            stenosis and Gasdermin-C expression in Chinese population
  JOURNAL   Sci Rep 10 (1), 21069 (2020)
   PUBMED   33273635
  REMARK    GeneRIF: Two GWAS-identified variants are associated with lumbar
            spinal stenosis and Gasdermin-C expression in Chinese population.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Lango Allen,H., Estrada,K., Lettre,G., Berndt,S.I., Weedon,M.N.,
            Rivadeneira,F., Willer,C.J., Jackson,A.U., Vedantam,S.,
            Raychaudhuri,S., Ferreira,T., Wood,A.R., Weyant,R.J., Segre,A.V.,
            Speliotes,E.K., Wheeler,E., Soranzo,N., Park,J.H., Yang,J.,
            Gudbjartsson,D., Heard-Costa,N.L., Randall,J.C., Qi,L., Vernon
            Smith,A., Magi,R., Pastinen,T., Liang,L., Heid,I.M., Luan,J.,
            Thorleifsson,G., Winkler,T.W., Goddard,M.E., Sin Lo,K., Palmer,C.,
            Workalemahu,T., Aulchenko,Y.S., Johansson,A., Zillikens,M.C.,
            Feitosa,M.F., Esko,T., Johnson,T., Ketkar,S., Kraft,P., Mangino,M.,
            Prokopenko,I., Absher,D., Albrecht,E., Ernst,F., Glazer,N.L.,
            Hayward,C., Hottenga,J.J., Jacobs,K.B., Knowles,J.W., Kutalik,Z.,
            Monda,K.L., Polasek,O., Preuss,M., Rayner,N.W., Robertson,N.R.,
            Steinthorsdottir,V., Tyrer,J.P., Voight,B.F., Wiklund,F., Xu,J.,
            Zhao,J.H., Nyholt,D.R., Pellikka,N., Perola,M., Perry,J.R.,
            Surakka,I., Tammesoo,M.L., Altmaier,E.L., Amin,N., Aspelund,T.,
            Bhangale,T., Boucher,G., Chasman,D.I., Chen,C., Coin,L.,
            Cooper,M.N., Dixon,A.L., Gibson,Q., Grundberg,E., Hao,K., Juhani
            Junttila,M., Kaplan,L.M., Kettunen,J., Konig,I.R., Kwan,T.,
            Lawrence,R.W., Levinson,D.F., Lorentzon,M., McKnight,B.,
            Morris,A.P., Muller,M., Suh Ngwa,J., Purcell,S., Rafelt,S.,
            Salem,R.M., Salvi,E., Sanna,S., Shi,J., Sovio,U., Thompson,J.R.,
            Turchin,M.C., Vandenput,L., Verlaan,D.J., Vitart,V., White,C.C.,
            Ziegler,A., Almgren,P., Balmforth,A.J., Campbell,H., Citterio,L.,
            De Grandi,A., Dominiczak,A., Duan,J., Elliott,P., Elosua,R.,
            Eriksson,J.G., Freimer,N.B., Geus,E.J., Glorioso,N., Haiqing,S.,
            Hartikainen,A.L., Havulinna,A.S., Hicks,A.A., Hui,J., Igl,W.,
            Illig,T., Jula,A., Kajantie,E., Kilpelainen,T.O., Koiranen,M.,
            Kolcic,I., Koskinen,S., Kovacs,P., Laitinen,J., Liu,J., Lokki,M.L.,
            Marusic,A., Maschio,A., Meitinger,T., Mulas,A., Pare,G.,
            Parker,A.N., Peden,J.F., Petersmann,A., Pichler,I.,
            Pietilainen,K.H., Pouta,A., Ridderstrale,M., Rotter,J.I.,
            Sambrook,J.G., Sanders,A.R., Schmidt,C.O., Sinisalo,J., Smit,J.H.,
            Stringham,H.M., Bragi Walters,G., Widen,E., Wild,S.H.,
            Willemsen,G., Zagato,L., Zgaga,L., Zitting,P., Alavere,H.,
            Farrall,M., McArdle,W.L., Nelis,M., Peters,M.J., Ripatti,S., van
            Meurs,J.B., Aben,K.K., Ardlie,K.G., Beckmann,J.S., Beilby,J.P.,
            Bergman,R.N., Bergmann,S., Collins,F.S., Cusi,D., den Heijer,M.,
            Eiriksdottir,G., Gejman,P.V., Hall,A.S., Hamsten,A., Huikuri,H.V.,
            Iribarren,C., Kahonen,M., Kaprio,J., Kathiresan,S., Kiemeney,L.,
            Kocher,T., Launer,L.J., Lehtimaki,T., Melander,O., Mosley,T.H. Jr.,
            Musk,A.W., Nieminen,M.S., O'Donnell,C.J., Ohlsson,C., Oostra,B.,
            Palmer,L.J., Raitakari,O., Ridker,P.M., Rioux,J.D., Rissanen,A.,
            Rivolta,C., Schunkert,H., Shuldiner,A.R., Siscovick,D.S.,
            Stumvoll,M., Tonjes,A., Tuomilehto,J., van Ommen,G.J., Viikari,J.,
            Heath,A.C., Martin,N.G., Montgomery,G.W., Province,M.A., Kayser,M.,
            Arnold,A.M., Atwood,L.D., Boerwinkle,E., Chanock,S.J., Deloukas,P.,
            Gieger,C., Gronberg,H., Hall,P., Hattersley,A.T., Hengstenberg,C.,
            Hoffman,W., Lathrop,G.M., Salomaa,V., Schreiber,S., Uda,M.,
            Waterworth,D., Wright,A.F., Assimes,T.L., Barroso,I., Hofman,A.,
            Mohlke,K.L., Boomsma,D.I., Caulfield,M.J., Cupples,L.A.,
            Erdmann,J., Fox,C.S., Gudnason,V., Gyllensten,U., Harris,T.B.,
            Hayes,R.B., Jarvelin,M.R., Mooser,V., Munroe,P.B., Ouwehand,W.H.,
            Penninx,B.W., Pramstaller,P.P., Quertermous,T., Rudan,I.,
            Samani,N.J., Spector,T.D., Volzke,H., Watkins,H., Wilson,J.F.,
            Groop,L.C., Haritunians,T., Hu,F.B., Kaplan,R.C., Metspalu,A.,
            North,K.E., Schlessinger,D., Wareham,N.J., Hunter,D.J.,
            O'Connell,J.R., Strachan,D.P., Wichmann,H.E., Borecki,I.B., van
            Duijn,C.M., Schadt,E.E., Thorsteinsdottir,U., Peltonen,L.,
            Uitterlinden,A.G., Visscher,P.M., Chatterjee,N., Loos,R.J.,
            Boehnke,M., McCarthy,M.I., Ingelsson,E., Lindgren,C.M.,
            Abecasis,G.R., Stefansson,K., Frayling,T.M. and Hirschhorn,J.N.
  TITLE     Hundreds of variants clustered in genomic loci and biological
            pathways affect human height
  JOURNAL   Nature 467 (7317), 832-838 (2010)
   PUBMED   20881960
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Birnbaum,S., Ludwig,K.U., Reutter,H., Herms,S., Steffens,M.,
            Rubini,M., Baluardo,C., Ferrian,M., Almeida de Assis,N.,
            Alblas,M.A., Barth,S., Freudenberg,J., Lauster,C., Schmidt,G.,
            Scheer,M., Braumann,B., Berge,S.J., Reich,R.H., Schiefke,F.,
            Hemprich,A., Potzsch,S., Steegers-Theunissen,R.P., Potzsch,B.,
            Moebus,S., Horsthemke,B., Kramer,F.J., Wienker,T.F., Mossey,P.A.,
            Propping,P., Cichon,S., Hoffmann,P., Knapp,M., Nothen,M.M. and
            Mangold,E.
  TITLE     Key susceptibility locus for nonsyndromic cleft lip with or without
            cleft palate on chromosome 8q24
  JOURNAL   Nat Genet 41 (4), 473-477 (2009)
   PUBMED   19270707
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Saeki,N., Usui,T., Aoyagi,K., Kim,D.H., Sato,M., Mabuchi,T.,
            Yanagihara,K., Ogawa,K., Sakamoto,H., Yoshida,T. and Sasaki,H.
  TITLE     Distinctive expression and function of four GSDM family genes
            (GSDMA-D) in normal and malignant upper gastrointestinal epithelium
  JOURNAL   Genes Chromosomes Cancer 48 (3), 261-271 (2009)
   PUBMED   19051310
  REMARK    GeneRIF: Study investigated the expression pattern of the GSDM
            family genes in the upper gastrointestinal epithelium and cancers.
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Tamura,M., Tanaka,S., Fujii,T., Aoki,A., Komiyama,H., Ezawa,K.,
            Sumiyama,K., Sagai,T. and Shiroishi,T.
  TITLE     Members of a novel gene family, Gsdm, are expressed exclusively in
            the epithelium of the skin and gastrointestinal tract in a highly
            tissue-specific manner
  JOURNAL   Genomics 89 (5), 618-629 (2007)
   PUBMED   17350798
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Watabe,K., Ito,A., Asada,H., Endo,Y., Kobayashi,T., Nakamoto,K.,
            Itami,S., Takao,S., Shinomura,Y., Aikou,T., Yoshikawa,K.,
            Matsuzawa,Y., Kitamura,Y. and Nojima,H.
  TITLE     Structure, expression and chromosome mapping of MLZE, a novel gene
            which is preferentially expressed in metastatic melanoma cells
  JOURNAL   Jpn J Cancer Res 92 (2), 140-151 (2001)
   PUBMED   11223543
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB042405.1, DA437012.1 and BC063595.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB042405.1, BC035321.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000276708.9/ ENSP00000276708.4
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..508
                     /product="gasdermin-C"
                     /note="melanoma-derived leucine zipper, extra-nuclear
                     factor; melanoma-derived leucine zipper-containing
                     extranuclear factor"
                     /calculated_mol_wt=57561
     Region          1..257
                     /region_name="Triggers pyroptosis.
                     /evidence=ECO:0000269|PubMed:27281216"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYG8.3)"
     Region          4..240
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Site            240..241
                     /site_type="cleavage"
                     /note="Cleavage, by CASP8.
                     /evidence=ECO:0000269|PubMed:34012073; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG8.3)"
     Region          313..482
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     Site            365..366
                     /site_type="cleavage"
                     /note="Cleavage, by CASP8.
                     /evidence=ECO:0000305|PubMed:32929201; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG8.3)"
     CDS             1..508
                     /gene="GSDMC"
                     /gene_synonym="MLZE"
                     /coded_by="NM_031415.3:619..2145"
                     /db_xref="CCDS:CCDS6360.1"
                     /db_xref="GeneID:56169"
                     /db_xref="HGNC:HGNC:7151"
                     /db_xref="MIM:608384"
ORIGIN      
        1 mpsmlerisk nlvkeigskd ltpvkyllsa tklrqfvilr kkkdsrssfw eqsdyvpvef
       61 slndilepss svletvvtgp fhfsdimiqk hkadmgvnvg ievsvsgeas vdhgcslefq
      121 ivtipspnle dfqkrklldp epsflkecrr rgdnlyvvte avelinntvl ydsssvnilg
      181 kialwitygk gqgqgeslrv kkkaltlqkg mvmaykrkql vikekailis dddeqrtfqd
      241 eyeisemvgy caarsegllp sfhtisptlf nassndmklk pelfltqqfl sghlpkyeqv
      301 hilpvgriee pfwqnfkhlq eevfqkiktl aqlskdvqdv mfysilamlr drgalqdlmn
      361 mleldssghl dgpggailkk lqqdsnhawf npkdpilyll eaimvlsdfq hdllacsmek
      421 rillqqqelv rsilepnfry pwsipftlkp ellaplqseg laitygllee cglrmeldnp
      481 rstwdveakm plsalygtls llqqlaea
//
LOCUS       NP_660311                244 aa            linear   PRI 27-APR-2025
DEFINITION  serine-rich single-pass membrane protein 1 [Homo sapiens].
ACCESSION   NP_660311
VERSION     NP_660311.1
DBSOURCE    REFSEQ: accession NM_145268.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Nozawa,K., Zhang,Q., Miyata,H., Devlin,D.J., Yu,Z., Oura,S.,
            Koyano,T., Matsuyama,M., Ikawa,M. and Matzuk,M.M.
  TITLE     Knockout of serine-rich single-pass membrane protein 1 (Ssmem1)
            causes globozoospermia and sterility in male micedagger
  JOURNAL   Biol Reprod 103 (2), 244-253 (2020)
   PUBMED   32301969
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087071.2, BC017587.2 and AC024085.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017587.2, SRR5189667.359281.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297819.4/ ENSP00000297819.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q32.2"
     Protein         1..244
                     /product="serine-rich single-pass membrane protein 1"
                     /calculated_mol_wt=28036
     Region          1..243
                     /region_name="DUF4636"
                     /note="Domain of unknown function (DUF4636); pfam15468"
                     /db_xref="CDD:373871"
     Site            35..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWF3.1)"
     Region          65..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWF3.1)"
     Region          126..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWF3.1)"
     Region          210..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWF3.1)"
     CDS             1..244
                     /gene="SSMEM1"
                     /gene_synonym="C7orf45"
                     /coded_by="NM_145268.4:52..786"
                     /db_xref="CCDS:CCDS5816.1"
                     /db_xref="GeneID:136263"
                     /db_xref="HGNC:HGNC:29580"
ORIGIN      
        1 mgdlfslfwe vdpppipvnc aipnqdyecw kddscgtigs fllwyfvivf vlmffsrasv
       61 wmsedkkdeg sgtstsvrka sketsckrqs kdsawdpsqt mkkpkqnqlt pvtnsevalv
      121 naypeqrrar rqsqfnevnq nqhdsdttey gseesnseas swkesesehh pspdsikrrk
      181 maqrqrnlgs yqmserhclh ckalrtnewl ahhsrqkpsv tppmkrdsqe essisdinkk
      241 fskf
//
LOCUS       NP_057525               1036 aa            linear   PRI 27-APR-2025
DEFINITION  cysteine-rich motor neuron 1 protein precursor [Homo sapiens].
ACCESSION   NP_057525
VERSION     NP_057525.1
DBSOURCE    REFSEQ: accession NM_016441.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Dai,N., Ma,H. and Feng,Y.
  TITLE     Silencing of long non-coding RNA SDCBP2-AS1/microRNA-656-3p/CRIM1
            axis promotes ferroptosis of lung cancer cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (9), 189-194 (2023)
   PUBMED   37807311
  REMARK    GeneRIF: Silencing of long non-coding RNA
            SDCBP2-AS1/microRNA-656-3p/CRIM1 axis promotes ferroptosis of lung
            cancer cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Yu,F., Xing,J., Li,L. and Xiang,M.
  TITLE     CircCRIM1 mediates proliferation, migration, and invasion of
            trophoblast cell through regulating miR-942-5p/IL1RAP axis
  JOURNAL   Am J Reprod Immunol 90 (1), e13699 (2023)
   PUBMED   37382169
  REMARK    GeneRIF: CircCRIM1 mediates proliferation, migration, and invasion
            of trophoblast cell through regulating miR-942-5p/IL1RAP axis.
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Park,Y., Kim,H., Seo,H., Choi,J.Y., Ma,Y., Yun,S., Min,B.J.,
            Seo,M.E., Yoo,K.H., Kang,H.J., Im,H.J. and Kim,J.H.
  TITLE     Homozygote CRIM1 variant is associated with thiopurine-induced
            neutropenia in leukemic patients with both wildtype NUDT15 and TPMT
  JOURNAL   J Transl Med 18 (1), 265 (2020)
   PUBMED   32611418
  REMARK    GeneRIF: Homozygote CRIM1 variant is associated with
            thiopurine-induced neutropenia in leukemic patients with both
            wildtype NUDT15 and TPMT.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1036)
  AUTHORS   Maurizi,E., Schiroli,D., Atkinson,S.D., Mairs,L., Courtney,D.G.,
            O'Hagan,B., McGilligan,V.E., Pagnamenta,A.T., Taylor,J.C.,
            Vasquez,J.J.D., Illanes-Velarde,D.E., Goldsmith,D., Gouws,P.,
            Moore,J.E., Nesbit,M.A. and Moore,C.B.T.
  TITLE     A novel role for CRIM1 in the corneal response to UV and pterygium
            development
  JOURNAL   Exp Eye Res 179, 75-92 (2019)
   PUBMED   30365943
  REMARK    GeneRIF: We propose here a series of intracellular events where
            CRIM1 regulation of the ERK pathway prevents UV-induced cell
            proliferation and may play an important role in the in the
            pathogenesis of pterygium.
REFERENCE   5  (residues 1 to 1036)
  AUTHORS   Ogasawara,N., Kudo,T., Sato,M., Kawasaki,Y., Yonezawa,S.,
            Takahashi,S., Miyagi,Y., Natori,Y. and Sugiyama,A.
  TITLE     Reduction of Membrane Protein CRIM1 Decreases E-Cadherin and
            Increases Claudin-1 and MMPs, Enhancing the Migration and Invasion
            of Renal Carcinoma Cells
  JOURNAL   Biol Pharm Bull 41 (4), 604-611 (2018)
   PUBMED   29607933
  REMARK    GeneRIF: CRIM1 regulates the expression of several
            epithelial-mesenchymal transition (EMT) related factors and appears
            to play a role in suppressing migration and invasion through
            control of EMT.
REFERENCE   6  (residues 1 to 1036)
  AUTHORS   Polasek,O., Marusic,A., Rotim,K., Hayward,C., Vitart,V.,
            Huffman,J., Campbell,S., Jankovic,S., Boban,M., Biloglav,Z.,
            Kolcic,I., Krzelj,V., Terzic,J., Matec,L., Tometic,G., Nonkovic,D.,
            Nincevic,J., Pehlic,M., Zedelj,J., Velagic,V., Juricic,D.,
            Kirac,I., Belak Kovacevic,S., Wright,A.F., Campbell,H. and Rudan,I.
  TITLE     Genome-wide association study of anthropometric traits in Korcula
            Island, Croatia
  JOURNAL   Croat Med J 50 (1), 7-16 (2009)
   PUBMED   19260139
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 1036)
  AUTHORS   Wilkinson,L., Kolle,G., Wen,D., Piper,M., Scott,J. and Little,M.
  TITLE     CRIM1 regulates the rate of processing and delivery of bone
            morphogenetic proteins to the cell surface
  JOURNAL   J Biol Chem 278 (36), 34181-34188 (2003)
   PUBMED   12805376
  REMARK    GeneRIF: CRIM1 modulates BMP activity by affecting its processing
            and delivery to the cell surface
REFERENCE   8  (residues 1 to 1036)
  AUTHORS   Glienke,J., Sturz,A., Menrad,A. and Thierauch,K.H.
  TITLE     CRIM1 is involved in endothelial cell capillary formation in vitro
            and is expressed in blood vessels in vivo
  JOURNAL   Mech Dev 119 (2), 165-175 (2002)
   PUBMED   12464430
  REMARK    GeneRIF: CRIM1 has a role in capillary formation and maintenance
            during angiogenesis
REFERENCE   9  (residues 1 to 1036)
  AUTHORS   Georgas,K., Bowles,J., Yamada,T., Koopman,P. and Little,M.H.
  TITLE     Characterisation of Crim1 expression in the developing mouse
            urogenital tract reveals a sexually dimorphic gonadal expression
            pattern
  JOURNAL   Dev Dyn 219 (4), 582-587 (2000)
   PUBMED   11084657
REFERENCE   10 (residues 1 to 1036)
  AUTHORS   Kolle,G., Georgas,K., Holmes,G.P., Little,M.H. and Yamada,T.
  TITLE     CRIM1, a novel gene encoding a cysteine-rich repeat protein, is
            developmentally regulated and implicated in vertebrate CNS
            development and organogenesis
  JOURNAL   Mech Dev 90 (2), 181-193 (2000)
   PUBMED   10642437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009414.4, AB209139.1 and
            AF167706.1.
            
            Summary: This gene encodes a transmembrane protein containing six
            cysteine-rich repeat domains and an insulin-like growth
            factor-binding domain. The encoded protein may play a role in
            tissue development though interactions with members of the
            transforming growth factor beta family, such as bone morphogenetic
            proteins. [provided by RefSeq, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF167706.1, SRR1660809.144038.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280527.7/ ENSP00000280527.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.2"
     Protein         1..1036
                     /product="cysteine-rich motor neuron 1 protein precursor"
                     /note="cysteine-rich repeat-containing protein S52;
                     cysteine-rich motor neuron 1 protein; cysteine rich
                     transmembrane BMP regulator 1 (chordin-like)"
                     /calculated_mol_wt=110276
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3481
     mat_peptide     35..1036
                     /product="cysteine-rich motor neuron 1 protein"
                     /calculated_mol_wt=110276
     Region          39..90
                     /region_name="IGFBP"
                     /note="Insulin-like growth factor binding protein;
                     pfam00219"
                     /db_xref="CDD:459717"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV1.1)"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV1.1)"
     Region          314..316
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV1.1)"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV1.1)"
     Region          336..390
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Region          403..456
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Site            474
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV1.1)"
     Region          567..592
                     /region_name="Antistasin"
                     /note="Antistasin family; pfam02822"
                     /db_xref="CDD:460713"
     Region          612..662
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Region          683..734
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Site            746
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV1.1)"
     Region          758..808
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Region          819..873
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Region          907..1036
                     /region_name="CRIM1_C"
                     /note="Cysteine-rich motor neuron 1 protein C-terminal;
                     pfam19442"
                     /db_xref="CDD:437274"
     Site            940..960
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV1.1)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV1.1)"
     CDS             1..1036
                     /gene="CRIM1"
                     /gene_synonym="CRIM-1; S52"
                     /coded_by="NM_016441.3:516..3626"
                     /db_xref="CCDS:CCDS1783.1"
                     /db_xref="GeneID:51232"
                     /db_xref="HGNC:HGNC:2359"
                     /db_xref="MIM:606189"
ORIGIN      
        1 mylvagdrgl agcghllvsl lglllllars gtralvclpc deskceeprn cpgsivqgvc
       61 gccytcasqr nescggtfgi ygtcdrglrc virpplngds lteyeagvce denwtddqll
      121 gfkpcnenli agcniingkc ecntirtcsn pfefpsqdmc lsalkrieee kpdcskarce
      181 vqfsprcped svliegyapp geccplpsrc vcnpagclrk vcqpgnlnil vskasgkpge
      241 ccdlyeckpv fgvdcrtvec ppvqqtacpp dsyetqvrlt adgcctlptr ceclsglcgf
      301 pvcevgstpr ivsrgdgtpg kccdvfecvn dtkpacvfnn veyydgdmfr mdncrfcrcq
      361 ggvaicftaq cgeinceryy vpegeccpvc edpvypfnnp agcyanglil ahgdrwredd
      421 ctfcqcvnge rhcvatvcgq tctnpvkvpg eccpvceept iitvdppacg elsnctltgk
      481 dcingfkrdh ngcrtcqcin teelcserkq gctlncpfgf ltdaqnceic ecrprpkkcr
      541 piicdkycpl gllknkhgcd icrckkcpel scskicplgf qqdshgclic kcreasasag
      601 ppilsgtclt vdghhhknee swhdgcrecy clngremcal itcpvpacgn ptihpgqccp
      661 scaddfvvqk pelstpsich apggeyfveg etwnidsctq ctchsgrvlc etevcppllc
      721 qnpsrtqdsc cpqctdqpfr pslsrnnsvp nyckndegdi flaaeswkpd vctscicids
      781 viscfsescp svscerpvlr kgqccpycie dtipkkvvch fsgkayadee rwdldscthc
      841 yclqgqtlcs tvscpplpcv epinvegscc pmcpemyvpe ptnipiektn hrgevdlevp
      901 lwptpsendi vhlprdmghl qvdyrdnrlh psedssldsi asvvvpiiic lsiiiaflfi
      961 nqkkqwipll cwyrtptkps slnnqlvsvd ckkgtrvqvd ssqrmlriae pdarfsgfys
     1021 mqkqnhlqad nfyqtv
//
LOCUS       NP_001343262             668 aa            linear   ROD 27-APR-2025
DEFINITION  RAF proto-oncogene serine/threonine-protein kinase isoform 2 [Mus
            musculus].
ACCESSION   NP_001343262 XP_006505426
VERSION     NP_001343262.1
DBSOURCE    REFSEQ: accession NM_001356333.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Luo,X., Zhang,D., Zheng,J., Liu,H., Sun,L., Guo,H., Wang,L. and
            Cui,S.
  TITLE     Casein kinase 1alpha mediates estradiol secretion via CYP19A1
            expression in mouse ovarian granulosa cells
  JOURNAL   BMC Biol 22 (1), 176 (2024)
   PUBMED   39183304
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Liu,H., Niu,T., Qiu,G., Cui,S. and Zhang,D.
  TITLE     Taurine promotes insulin synthesis by enhancing Isl-1 expression
            through miR-7a/RAF1/ERK1/2 pathway
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (1), 23-35 (2024)
   PUBMED   38117455
  REMARK    GeneRIF: Taurine promotes insulin synthesis by enhancing Isl-1
            expression through miR-7a/RAF1/ERK1/2 pathway.
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Geng,W., Cao,M., Dong,K., An,J. and Gao,H.
  TITLE     SHOC2 mediates the drug-resistance of triple-negative breast cancer
            cells to everolimus
  JOURNAL   Cancer Biol Ther 24 (1), 2206362 (2023)
   PUBMED   37170083
  REMARK    GeneRIF: SHOC2 mediates the drug-resistance of triple-negative
            breast cancer cells to everolimus.
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Zhong,S. and Borlak,J.
  TITLE     Sex disparities in non-small cell lung cancer: mechanistic insights
            from a cRaf transgenic disease model
  JOURNAL   EBioMedicine 95, 104763 (2023)
   PUBMED   37625265
  REMARK    GeneRIF: Sex disparities in non-small cell lung cancer: mechanistic
            insights from a cRaf transgenic disease model.
REFERENCE   6  (residues 1 to 668)
  AUTHORS   Kyriakis,J.M., App,H., Zhang,X.F., Banerjee,P., Brautigan,D.L.,
            Rapp,U.R. and Avruch,J.
  TITLE     Raf-1 activates MAP kinase-kinase
  JOURNAL   Nature 358 (6385), 417-421 (1992)
   PUBMED   1322500
REFERENCE   7  (residues 1 to 668)
  AUTHORS   Ludwig,T., Ruther,U., Metzger,R., Copeland,N.G., Jenkins,N.A.,
            Lobel,P. and Hoflack,B.
  TITLE     Gene and pseudogene of the mouse cation-dependent mannose
            6-phosphate receptor. Genomic organization, expression, and
            chromosomal localization
  JOURNAL   J Biol Chem 267 (17), 12211-12219 (1992)
   PUBMED   1376319
REFERENCE   8  (residues 1 to 668)
  AUTHORS   Wilkie,T.M., Gilbert,D.J., Olsen,A.S., Chen,X.N., Amatruda,T.T.,
            Korenberg,J.R., Trask,B.J., de Jong,P., Reed,R.R., Simon,M.I. et
            al.
  TITLE     Evolution of the mammalian G protein alpha subunit multigene family
  JOURNAL   Nat Genet 1 (2), 85-91 (1992)
   PUBMED   1302014
  REMARK    Review article
REFERENCE   9  (residues 1 to 668)
  AUTHORS   Danciger,M., Chakraborti,A., Farber,D.B. and Kozak,C.A.
  TITLE     Localization of the gene for a third G protein beta-subunit to
            mouse chromosome 6 near Raf-1
  JOURNAL   Genomics 12 (4), 688-692 (1992)
   PUBMED   1572642
REFERENCE   10 (residues 1 to 668)
  AUTHORS   Moore,K.J., D'Amore-Bruno,M.A., Korfhagen,T.R., Glasser,S.W.,
            Whitsett,J.A., Jenkins,N.A. and Copeland,N.G.
  TITLE     Chromosomal localization of three pulmonary surfactant protein
            genes in the mouse
  JOURNAL   Genomics 12 (2), 388-393 (1992)
   PUBMED   1346779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC160032.7.
            
            On Sep 29, 2017 this sequence version replaced XP_006505426.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.61832.1,
                                           SRR7345562.1927795.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 53.62 cM"
     Protein         1..668
                     /product="RAF proto-oncogene serine/threonine-protein
                     kinase isoform 2"
                     /EC_number="2.7.11.1"
                     /note="murine sarcoma 3611 oncogene 1; RAF proto-oncogene
                     serine/threonine-protein kinase; proto-oncogene c-RAF;
                     Craf1 transforming"
                     /calculated_mol_wt=75020
     Region          55..131
                     /region_name="RBD_CRAF"
                     /note="Ras-binding domain (RBD) found in RAF
                     proto-oncogene serine/threonine-protein kinase RAF1/CRAF;
                     cd17135"
                     /db_xref="CDD:340655"
     Site            order(57,59,64..69,71,84,88..90)
                     /site_type="other"
                     /note="RBD_Raf-Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:340655"
     Site            order(57,64,66..69,84,87..90)
                     /site_type="other"
                     /note="putative RBD_Raf-KRas interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340655"
     Site            125
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:340655"
     Region          136..187
                     /region_name="C1_A_C-Raf"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma)
                     kinases, and similar proteins; cd20870"
                     /db_xref="CDD:410420"
     Region          356..638
                     /region_name="STKc_C-Raf"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; cd14149"
                     /db_xref="CDD:271051"
     Site            order(360,362,387,389..390,417..423,427..429,474,477..478,
                     481..482,498,500,627)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271051"
     Site            order(375..379,383,393,395,426,441..444,448,450,488,490,
                     492..493,495,506,509,527..530)
                     /site_type="active"
                     /db_xref="CDD:271051"
     Site            order(375..379,383,393,395,426,441..444,448,488,490,
                     492..493,495,506)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271051"
     Site            order(379,448,450,488,490,492,509,527..530)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271051"
     Site            505..530
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271051"
     CDS             1..668
                     /gene="Raf1"
                     /gene_synonym="6430402F14Rik; c-Raf; cRaf; Craf1;
                     D830050J10Rik; Raf-1; v-Raf"
                     /coded_by="NM_001356333.2:427..2433"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:110157"
                     /db_xref="MGI:MGI:97847"
ORIGIN      
        1 mehiqgawkt isngfglkda vfdgsscisp tivqqfgyqr rasddgkltd ssktsntirv
       61 flpnkqrtvv nvrngmslhd clmkalkvrg lqpeccavfr llqehkgkka rldwntdaas
      121 ligeelqvdf ldhvpltthn farktflkla fcdicqkfll ngfrcqtcgy kfhehcstkv
      181 ptmcvdwsni rqlllfpnst vgdsgvpapp sfpmrrmres vsrmpassqh rystphaftf
      241 ntsspssegs lsqrqrstst pnvhmvsttl hvdsrmiesn slnaspracs rrfclrgrda
      301 irshsesasp salssspnnl sptgwsqpkt pvpaqrerap gsgtqeknki rprgqrdssy
      361 yweieasevm lstrigsgsf gtvykgkwhg dvavkilkvv dptpeqlqaf rnevavlrkt
      421 rhvnillfmg ymtkdnlaiv tqwcegssly khlhvqetkf qmfqlidiar qtaqgmdylh
      481 akniihrdmk snniflhegl tvkigdfgla tvksrwsgsq qveqptgsvl wmapevirmq
      541 ddnpfsfqsd vysygivlye lmagelpyah innrdqiifm vgrgyaspdl srlykncpka
      601 mkrlvadcvk kvkeerplfp qilssiellq hslpkinrsa sepslhraah tedinactlt
      661 tsprlpvf
//
LOCUS       NP_002872                206 aa            linear   PRI 27-APR-2025
DEFINITION  ras-related protein Ral-B [Homo sapiens].
ACCESSION   NP_002872
VERSION     NP_002872.1
DBSOURCE    REFSEQ: accession NM_002881.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Yoshimachi,S., Shirakawa,R., Cao,M., Trinh,D.A., Gao,P., Sakata,N.,
            Miyazaki,K., Goto,K., Miura,T., Ariake,K., Maeda,S., Masuda,K.,
            Ishida,M., Ohtsuka,H., Unno,M. and Horiuchi,H.
  TITLE     Ral GTPase-activating protein regulates the malignancy of
            pancreatic ductal adenocarcinoma
  JOURNAL   Cancer Sci 112 (8), 3064-3073 (2021)
   PUBMED   34009715
  REMARK    GeneRIF: Ral GTPase-activating protein regulates the malignancy of
            pancreatic ductal adenocarcinoma.
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Wang,Y., Zheng,Y., Chen,Q., Dai,Y. and Li,T.
  TITLE     MicroRNA-139 inhibits pancreatic-cancer carcinogenesis by
            suppressing RalB via the Ral/RAC/PI3K pathway
  JOURNAL   Arch Biochem Biophys 704, 108719 (2021)
   PUBMED   33290747
  REMARK    GeneRIF: MicroRNA-139 inhibits pancreatic-cancer carcinogenesis by
            suppressing RalB via the Ral/RAC/PI3K pathway.
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Naszai,M., Bellec,K., Yu,Y., Roman-Fernandez,A., Sandilands,E.,
            Johansson,J., Campbell,A.D., Norman,J.C., Sansom,O.J., Bryant,D.M.
            and Cordero,J.B.
  TITLE     RAL GTPases mediate EGFR-driven intestinal stem cell proliferation
            and tumourigenesis
  JOURNAL   Elife 10, e63807 (2021)
   PUBMED   34096503
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Khawaja,H., Campbell,A., Roberts,J.Z., Javadi,A., O'Reilly,P.,
            McArt,D., Allen,W.L., Majkut,J., Rehm,M., Bardelli,A., Di
            Nicolantonio,F., Scott,C.J., Kennedy,R., Vitale,N., Harrison,T.,
            Sansom,O.J., Longley,D.B., Evergren,E. and Van Schaeybroeck,S.
  TITLE     RALB GTPase: a critical regulator of DR5 expression and TRAIL
            sensitivity in KRAS mutant colorectal cancer
  JOURNAL   Cell Death Dis 11 (10), 930 (2020)
   PUBMED   33122623
  REMARK    GeneRIF: RALB GTPase: a critical regulator of DR5 expression and
            TRAIL sensitivity in KRAS mutant colorectal cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Joneson,T. and Bar-Sagi,D.
  TITLE     Ras effectors and their role in mitogenesis and oncogenesis
  JOURNAL   J Mol Med (Berl) 75 (8), 587-593 (1997)
   PUBMED   9297626
  REMARK    Review article
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Jilkina,O. and Bhullar,R.P.
  TITLE     Generation of antibodies specific for the RalA and RalB GTP-binding
            proteins and determination of their concentration and distribution
            in human platelets
  JOURNAL   Biochim Biophys Acta 1314 (1-2), 157-166 (1996)
   PUBMED   8972729
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Jullien-Flores,V., Dorseuil,O., Romero,F., Letourneur,F.,
            Saragosti,S., Berger,R., Tavitian,A., Gacon,G. and Camonis,J.H.
  TITLE     Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with
            CDC42/Rac GTPase-activating protein activity
  JOURNAL   J Biol Chem 270 (38), 22473-22477 (1995)
   PUBMED   7673236
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Hsieh,C.L., Swaroop,A. and Francke,U.
  TITLE     Chromosomal localization and cDNA sequence of human ralB, a GTP
            binding protein
  JOURNAL   Somat Cell Mol Genet 16 (4), 407-410 (1990)
   PUBMED   2120779
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Chardin,P. and Tavitian,A.
  TITLE     Coding sequences of human ralA and ralB cDNAs
  JOURNAL   Nucleic Acids Res 17 (11), 4380 (1989)
   PUBMED   2662142
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ893549.1, AK127675.1,
            M35416.1 and BC018163.1.
            
            Summary: This gene encodes a GTP-binding protein that belongs to
            the small GTPase superfamily and Ras family of proteins.
            GTP-binding proteins mediate the transmembrane signaling initiated
            by the occupancy of certain cell surface receptors. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.321124.1,
                                           SRR3476690.805409.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000272519.10/ ENSP00000272519.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.2"
     Protein         1..206
                     /product="ras-related protein Ral-B"
                     /EC_number="3.6.5.2"
                     /note="RAS-like protein B; v-ral simian leukemia viral
                     oncogene homolog B (ras related; GTP binding protein); ras
                     related GTP binding protein B; RALB Ras like
                     proto-oncogene B"
                     /calculated_mol_wt=23277
     Region          15..178
                     /region_name="RalA_RalB"
                     /note="Ral (Ras-like) family containing highly homologous
                     RalA and RalB; cd04139"
                     /db_xref="CDD:206710"
     Site            21..28
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206710"
     Site            order(22..23,70..72,74..75,79,82,97,99,102..103,106..107,
                     110)
                     /site_type="active"
                     /note="GDI interaction site [active]"
                     /db_xref="CDD:206710"
     Site            order(23..29,39..40,46,71,128..129,131,158..159)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206710"
     Site            order(28..29,43,45,51..52,65..66,68,70..71,160)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206710"
     Site            order(36,38,47..52,56,60..61,161..164,166)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:206710"
     Region          43..51
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11234.1)"
     Site            44..51
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206710"
     Site            46
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206710"
     Site            68..71
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206710"
     Site            70..88
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206710"
     Site            128..131
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206710"
     Site            order(140..141,144,148,156)
                     /site_type="active"
                     /note="alternate GDI interaction site [active]"
                     /db_xref="CDD:206710"
     Site            158..160
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206710"
     Region          180..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11234.1)"
     Site            203
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P11234.1)"
     CDS             1..206
                     /gene="RALB"
                     /coded_by="NM_002881.3:177..797"
                     /db_xref="CCDS:CCDS2131.1"
                     /db_xref="GeneID:5899"
                     /db_xref="HGNC:HGNC:9840"
                     /db_xref="MIM:179551"
ORIGIN      
        1 maankskgqs slalhkvimv gsggvgksal tlqfmydefv edyeptkads yrkkvvldge
       61 evqidildta gqedyaaird nyfrsgegfl lvfsitehes ftataefreq ilrvkaeedk
      121 ipllvvgnks dleerrqvpv eearskaeew gvqyvetsak tranvdkvff dlmreirtkk
      181 msenkdkngk kssknkksfk erccll
//
LOCUS       NP_001357308             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357308 XP_016881649
VERSION     NP_001357308.1
DBSOURCE    REFSEQ: accession NM_001370379.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            On May 7, 2019 this sequence version replaced XP_016881649.1.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.51096.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370379.1:1515..3164"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_001275494             183 aa            linear   PRI 27-APR-2025
DEFINITION  proton-transporting V-type ATPase complex assembly regulator TMEM9
            isoform a precursor [Homo sapiens].
ACCESSION   NP_001275494
VERSION     NP_001275494.1
DBSOURCE    REFSEQ: accession NM_001288565.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Baek,S., Chang,J.W., Yoo,S.M., Choo,J., Jung,S., Nah,J. and
            Jung,Y.K.
  TITLE     TMEM9 activates Rab9-dependent alternative autophagy through
            interaction with Beclin1
  JOURNAL   Cell Mol Life Sci 81 (1), 322 (2024)
   PUBMED   39078420
  REMARK    GeneRIF: TMEM9 activates Rab9-dependent alternative autophagy
            through interaction with Beclin1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Wang,Z., Zhao,P., Tian,K., Qiao,Z., Dong,H., Li,J., Guan,Z., Su,H.,
            Song,Y. and Ma,X.
  TITLE     TMEM9 promotes lung adenocarcinoma progression via activating the
            MEK/ERK/STAT3 pathway to induce VEGF expression
  JOURNAL   Cell Death Dis 15 (4), 295 (2024)
   PUBMED   38664392
  REMARK    GeneRIF: TMEM9 promotes lung adenocarcinoma progression via
            activating the MEK/ERK/STAT3 pathway to induce VEGF expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Zhang,S., Lee,S.H., Nie,L., Huang,Y., Zou,G., Jung,Y.S., Jun,S.,
            Zhang,J., Lien,E.M., Chen,J. and Park,J.I.
  TITLE     Lysosomal TMEM9-LAMTOR4-controlled mTOR signaling integrity is
            required for mammary tumorigenesis
  JOURNAL   Cancer Commun (Lond) 43 (1), 159-163 (2023)
   PUBMED   36336962
  REMARK    GeneRIF: Lysosomal TMEM9-LAMTOR4-controlled mTOR signaling
            integrity is required for mammary tumorigenesis.
REFERENCE   4  (residues 1 to 183)
  AUTHORS   He,J., Bu,Y., Li,X., Zhang,X. and Ma,L.
  TITLE     Tumor-Promoting Properties of TMEM9A in Breast Cancer Progression
            via Activating the Wnt/beta-Catenin Signaling Pathway
  JOURNAL   Biol Pharm Bull 46 (1), 74-85 (2023)
   PUBMED   36596527
  REMARK    GeneRIF: Tumor-Promoting Properties of TMEM9A in Breast Cancer
            Progression via Activating the Wnt/beta-Catenin Signaling Pathway.
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Wei,W., Jiang,F., Liu,X.C. and Su,Q.
  TITLE     TMEM9 mediates IL-6 and IL-1beta secretion and is modulated by the
            Wnt pathway
  JOURNAL   Int Immunopharmacol 63, 253-260 (2018)
   PUBMED   30119033
  REMARK    GeneRIF: TMEM9 plays a significant role in TNF-alpha-enhanced
            cytokines (IL-6 and IL-1beta) secretion in LX-2 cells and that the
            canonical Wnt/beta-catenin signaling pathway is involved in the
            induction of these cytokine expressions.
REFERENCE   7  (residues 1 to 183)
  AUTHORS   Zhang,Y., Ran,Y., Xiong,Y., Zhong,Z.B., Wang,Z.H., Fan,X.L. and
            Ye,Q.F.
  TITLE     Effects of TMEM9 gene on cell progression in hepatocellular
            carcinoma by RNA interference
  JOURNAL   Oncol Rep 36 (1), 299-305 (2016)
   PUBMED   27220462
  REMARK    GeneRIF: TMEM9 knockdown by RNA interference resulted in G1 arrest.
REFERENCE   8  (residues 1 to 183)
  AUTHORS   Dodeller,F., Gottar,M., Huesken,D., Iourgenko,V. and Cenni,B.
  TITLE     The lysosomal transmembrane protein 9B regulates the activity of
            inflammatory signaling pathways
  JOURNAL   J Biol Chem 283 (31), 21487-21494 (2008)
   PUBMED   18541524
  REMARK    GeneRIF: TMEM9B is a key component of inflammatory signaling
            pathways and suggest that endosomal or lysosomal compartments
            regulate these pathways
REFERENCE   9  (residues 1 to 183)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 183)
  AUTHORS   Kveine,M., Tenstad,E., Dosen,G., Funderud,S. and Rian,E.
  TITLE     Characterization of the novel human transmembrane protein 9 (TMEM9)
            that localizes to lysosomes and late endosomes
  JOURNAL   Biochem Biophys Res Commun 297 (4), 912-917 (2002)
   PUBMED   12359240
  REMARK    GeneRIF: phylogenetically conserved, widely expressed transmembrane
            protein with a potential, but unknown function in intracellular
            transport that localizes to lysosomes and late endosomes
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA364005.1, DA160051.1, CX751563.1, AK091726.1, AK054883.1 and
            AI201238.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1-7 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1055858.1, AK091726.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367330.6/ ENSP00000356299.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..183
                     /product="proton-transporting V-type ATPase complex
                     assembly regulator TMEM9 isoform a precursor"
                     /note="dermal papilla-derived protein 4; v-ATPase assembly
                     regulator TMEM9; proton-transporting V-type ATPase complex
                     assembly regulator TMEM9"
                     /calculated_mol_wt=18568
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2024
     mat_peptide     21..183
                     /product="Proton-transporting V-type ATPase complex
                     assembly regulator TMEM9. /id=PRO_0000034374"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0T7.1)"
                     /calculated_mol_wt=18568
     Site            21
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9P0T7.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9P0T7.1)"
     Region          41..182
                     /region_name="Tmemb_9"
                     /note="TMEM9; pfam05434"
                     /db_xref="CDD:428471"
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9P0T7.1)"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0T7.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P0T7.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0T7.1)"
     CDS             1..183
                     /gene="TMEM9"
                     /gene_synonym="DERM4; TMEM9A"
                     /coded_by="NM_001288565.2:552..1103"
                     /note="isoform a precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS1408.1"
                     /db_xref="GeneID:252839"
                     /db_xref="HGNC:HGNC:18823"
                     /db_xref="MIM:616877"
ORIGIN      
        1 mkllslvavv gcllvppaea nkssedirck cicppyrnis ghiynqnvsq kdcnclhvve
       61 pmpvpghdve aycllcecry eerstttikv iiviylsvvg alllymaflm lvdplirkpd
      121 ayteqlhnee enedarsmaa aaaslggpra ntvlervega qqrwklqvqe qrktvfdrhk
      181 mls
//
LOCUS       NP_001123630            1136 aa            linear   PRI 27-APR-2025
DEFINITION  unconventional myosin-Ib isoform 1 [Homo sapiens].
ACCESSION   NP_001123630
VERSION     NP_001123630.1
DBSOURCE    REFSEQ: accession NM_001130158.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Li,Z., Qiu,X., He,Q., Fu,X., Ji,F. and Tian,X.
  TITLE     CCND1-associated ceRNA network reveal the critical pathway of
            TPRG1-AS1-hsa-miR-363-3p-MYO1B as a prognostic marker for head and
            neck squamous cell carcinoma
  JOURNAL   Sci Rep 13 (1), 11831 (2023)
   PUBMED   37481637
  REMARK    GeneRIF: CCND1-associated ceRNA network reveal the critical pathway
            of TPRG1-AS1-hsa-miR-363-3p-MYO1B as a prognostic marker for head
            and neck squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Sun,Z., Guo,X., Chen,H., Ling,J., Zhao,H., Chang,A. and Zhuo,X.
  TITLE     MYO1B as a prognostic biomarker and a therapeutic target in
            Arecoline-associated oral carcinoma
  JOURNAL   Mol Carcinog 62 (7), 920-939 (2023)
   PUBMED   37014156
  REMARK    GeneRIF: MYO1B as a prognostic biomarker and a therapeutic target
            in Arecoline-associated oral carcinoma.
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Yu,Y., Ren,Y., Li,Z., Li,Y., Li,Y., Zhang,Y., Gui,R., Cui,Y.,
            Qian,L. and Xiong,Y.
  TITLE     Myo1b Promotes Premature Endothelial Senescence and Dysfunction via
            Suppressing Autophagy: Implications for Vascular Aging
  JOURNAL   Oxid Med Cell Longev 2023, 4654083 (2023)
   PUBMED   36654782
  REMARK    GeneRIF: Myo1b Promotes Premature Endothelial Senescence and
            Dysfunction via Suppressing Autophagy: Implications for Vascular
            Aging.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1136)
  AUTHORS   Chen,Y.H., Xu,N.Z., Hong,C., Li,W.Q., Zhang,Y.Q., Yu,X.Y.,
            Huang,Y.L. and Zhou,J.Y.
  TITLE     Myo1b promotes tumor progression and angiogenesis by inhibiting
            autophagic degradation of HIF-1alpha in colorectal cancer
  JOURNAL   Cell Death Dis 13 (11), 939 (2022)
   PUBMED   36347835
  REMARK    GeneRIF: Myo1b promotes tumor progression and angiogenesis by
            inhibiting autophagic degradation of HIF-1alpha in colorectal
            cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1136)
  AUTHORS   Li,S.H., Qian,L., Chen,Y.H., Lu,H.I., Tsai,H.T., Lyu,H., Yang,R.
            and Chen,C.H.
  TITLE     Targeting MYO1B impairs tumorigenesis via inhibiting the
            SNAI2/cyclin D1 signaling in esophageal squamous cell carcinoma
  JOURNAL   J Cell Physiol 237 (9), 3671-3686 (2022)
   PUBMED   35861939
  REMARK    GeneRIF: Targeting MYO1B impairs tumorigenesis via inhibiting the
            SNAI2/cyclin D1 signaling in esophageal squamous cell carcinoma.
REFERENCE   6  (residues 1 to 1136)
  AUTHORS   Dumont,R.A., Zhao,Y.D., Holt,J.R., Bahler,M. and Gillespie,P.G.
  TITLE     Myosin-I isozymes in neonatal rodent auditory and vestibular
            epithelia
  JOURNAL   J Assoc Res Otolaryngol 3 (4), 375-389 (2002)
   PUBMED   12486594
  REMARK    GeneRIF: At apical surfaces of supporting cells that surround hair
            cells in auditory epithelia of postnatal rats. In vestibular
            epithelia, present in ring within apical pole of hair cell.
            Expression was prominent only immediately after birth.
REFERENCE   7  (residues 1 to 1136)
  AUTHORS   Tang,N. and Ostap,E.M.
  TITLE     Motor domain-dependent localization of myo1b (myr-1)
  JOURNAL   Curr Biol 11 (14), 1131-1135 (2001)
   PUBMED   11509238
REFERENCE   8  (residues 1 to 1136)
  AUTHORS   Ruppert,C., Godel,J., Muller,R.T., Kroschewski,R., Reinhard,J. and
            Bahler,M.
  TITLE     Localization of the rat myosin I molecules myr 1 and myr 2 and in
            vivo targeting of their tail domains
  JOURNAL   J Cell Sci 108 (Pt 12), 3775-3786 (1995)
   PUBMED   8719884
REFERENCE   9  (residues 1 to 1136)
  AUTHORS   Bement,W.M., Hasson,T., Wirth,J.A., Cheney,R.E. and Mooseker,M.S.
  TITLE     Identification and overlapping expression of multiple
            unconventional myosin genes in vertebrate cell types
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6549-6553 (1994)
   PUBMED   8022818
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11767. doi:
            10.1073/pnas.91.24.11767-c. PMID: 7972138]
REFERENCE   10 (residues 1 to 1136)
  AUTHORS   Ruppert,C., Kroschewski,R. and Bahler,M.
  TITLE     Identification, characterization and cloning of myr 1, a mammalian
            myosin-I
  JOURNAL   J Cell Biol 120 (6), 1393-1403 (1993)
   PUBMED   8449985
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB461518.1, BC060849.1, AB290176.1, AI751497.1, AJ001381.1,
            BF061446.1 and CA435949.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Both variants 1 and 3 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB290176.1, SRR1803614.146141.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392318.8/ ENSP00000376132.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.3"
     Protein         1..1136
                     /product="unconventional myosin-Ib isoform 1"
                     /note="myosin-I alpha; MYO1B variant protein;
                     unconventional myosin-Ib"
                     /calculated_mol_wt=131855
     Region          29..688
                     /region_name="MYSc_Myo1"
                     /note="class I myosin, motor domain; cd01378"
                     /db_xref="CDD:276829"
     Site            order(56..59,64,108..115,155..165,387..392)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276829"
     Site            order(56..59,64)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276829"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43795.3)"
     Site            108..115
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276829"
     Site            155..165
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276829"
     Site            387..392
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276829"
     Site            order(416..427,430..437,439)
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276829"
     Region          578..600
                     /region_name="Actin-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00782"
                     /note="propagated from UniProtKB/Swiss-Prot (O43795.3)"
     Site            620..630
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276829"
     Site            order(632..658,675..688)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276829"
     Region          749..771
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     Region          941..1118
                     /region_name="Myosin_TH1"
                     /note="Unconventional myosin tail, actin- and
                     lipid-binding; pfam06017"
                     /db_xref="CDD:461801"
     CDS             1..1136
                     /gene="MYO1B"
                     /gene_synonym="MMI-alpha; MMIa; MYH-1c; myr1"
                     /coded_by="NM_001130158.3:233..3643"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46477.1"
                     /db_xref="GeneID:4430"
                     /db_xref="HGNC:HGNC:7596"
                     /db_xref="MIM:606537"
ORIGIN      
        1 makmevktsl ldnmigvgdm vlleplneet finnlkkrfd hseiytyigs vvisvnpyrs
       61 lpiyspekve eyrnrnfyel sphifalsde ayrslrdqdk dqcilitges gagkteaskl
      121 vmsyvaavcg kgaevnqvke qllqsnpvle afgnaktvrn dnssrfgkym diefdfkgdp
      181 lggvisnyll eksrvvkqpr gernfhvfyq llsgaseell nklklerdfs rynylsldsa
      241 kvngvddaan frtvrnamqi vgfmdheaes vlavvaavlk lgniefkpes rvngldeski
      301 kdknelkeic eltgidqsvl erafsfrtve akqekvsttl nvaqayyard alaknlysrl
      361 fswlvnrine sikaqtkvrk kvmgvldiyg feifednsfe qfiinycnek lqqifieltl
      421 keeqeeyire diewthidyf nnaiicdlie nntngilaml deeclrpgtv tdetflekln
      481 qvcathqhfe srmskcsrfl ndtslphscf riqhyagkvl yqvegfvdkn ndllyrdlsq
      541 amwkashali kslfpegnpa kinlkrppta gsqfkasvat lmknlqtknp nyircikpnd
      601 kkaahifnea lvchqirylg llenvrvrra gyafrqayep clerykmlck qtwphwkgpa
      661 rsgvevlfne leipveeysf grskifirnp rtlfkledlr kqrledlatl iqkiyrgwkc
      721 rthfllmkks qiviaawyrr yaqqkryqqt kssalviqsy irgwkarkil relkhqkrck
      781 eavttiaayw hgtqarrelr rlkeearnkh aiaviwaywl gskarrelkr lkeearrkha
      841 vaviwaywlg lkvrreyrkf franagkkiy eftlqrivqk yflemknkmp slspidknwp
      901 srpylfldst hkelkrifhl wrckkyrdqf tdqqkliyee kleaselfkd kkalypssvg
      961 qpfqgaylei nknpkykklk daieekiiia evvnkinran gkstsrifll tnnnllladq
     1021 ksgqiksevp lvdvtkvsms sqndgffavh lkegseaask gdflfssdhl iematklyrt
     1081 tlsqtkqkln ieisdeflvq frqdkvcvkf iqgnqkngsv ptckrknnrl levavp
//
LOCUS       NP_002909                979 aa            linear   PRI 27-APR-2025
DEFINITION  MHC class II regulatory factor RFX1 [Homo sapiens].
ACCESSION   NP_002909
VERSION     NP_002909.4
DBSOURCE    REFSEQ: accession NM_002918.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 979)
  AUTHORS   Issac,J., Raveendran,P.S., Kunnummal,M., Angelin,M., Ravindran,S.,
            Basu,B. and Das,A.V.
  TITLE     RXR agonist, Bexarotene, effectively reduces drug resistance via
            regulation of RFX1 in embryonic carcinoma cells
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1870 (7), 119510 (2023)
   PUBMED   37301270
  REMARK    GeneRIF: RXR agonist, Bexarotene, effectively reduces drug
            resistance via regulation of RFX1 in embryonic carcinoma cells.
REFERENCE   2  (residues 1 to 979)
  AUTHORS   Chirichella,M., Bianchi,N., Dzafo,E., Foli,E., Gualdrini,F.,
            Kenyon,A., Natoli,G. and Monticelli,S.
  TITLE     RFX transcription factors control a miR-150/PDAP1 axis that
            restrains the proliferation of human T cells
  JOURNAL   PLoS Biol 20 (2), e3001538 (2022)
   PUBMED   35143476
  REMARK    GeneRIF: RFX transcription factors control a miR-150/PDAP1 axis
            that restrains the proliferation of human T cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 979)
  AUTHORS   Mizukawa,T., Nishida,T., Akashi,S., Kawata,K., Kikuchi,S.,
            Kawaki,H., Takigawa,M., Kamioka,H. and Kubota,S.
  TITLE     RFX1-mediated CCN3 induction that may support chondrocyte survival
            under starved conditions
  JOURNAL   J Cell Physiol 236 (10), 6884-6896 (2021)
   PUBMED   33655492
  REMARK    GeneRIF: RFX1-mediated CCN3 induction that may support chondrocyte
            survival under starved conditions.
REFERENCE   4  (residues 1 to 979)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 979)
  AUTHORS   Du,P., Gao,K., Cao,Y., Yang,S., Wang,Y., Guo,R., Zhao,M. and Jia,S.
  TITLE     RFX1 downregulation contributes to TLR4 overexpression in CD14+
            monocytes via epigenetic mechanisms in coronary artery disease
  JOURNAL   Clin Epigenetics 11 (1), 44 (2019)
   PUBMED   30857550
  REMARK    GeneRIF: Results show that RFX1 expression deficiency leads to the
            overexpression of TLR4 and the activation of CD14(+) monocytes in
            coronary artery disease (CAD) patients by regulating DNA
            methylation and histone modifications, which highlights the vital
            role of RFX1 in the pathogenesis of CAD.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 979)
  AUTHORS   Reith,W., Ucla,C., Barras,E., Gaud,A., Durand,B.,
            Herrero-Sanchez,C., Kobr,M. and Mach,B.
  TITLE     RFX1, a transactivator of hepatitis B virus enhancer I, belongs to
            a novel family of homodimeric and heterodimeric DNA-binding
            proteins
  JOURNAL   Mol Cell Biol 14 (2), 1230-1244 (1994)
   PUBMED   8289803
REFERENCE   7  (residues 1 to 979)
  AUTHORS   Safrany,G. and Perry,R.P.
  TITLE     Transcription factor RFX1 helps control the promoter of the mouse
            ribosomal protein-encoding gene rpL30 by binding to its alpha
            element
  JOURNAL   Gene 132 (2), 279-283 (1993)
   PUBMED   8224874
REFERENCE   8  (residues 1 to 979)
  AUTHORS   Herrero Sanchez,C., Reith,W., Silacci,P. and Mach,B.
  TITLE     The DNA-binding defect observed in major histocompatibility complex
            class II regulatory mutants concerns only one member of a family of
            complexes binding to the X boxes of class II promoters
  JOURNAL   Mol Cell Biol 12 (9), 4076-4083 (1992)
   PUBMED   1508204
REFERENCE   9  (residues 1 to 979)
  AUTHORS   Pugliatti,L., Derre,J., Berger,R., Ucla,C., Reith,W. and Mach,B.
  TITLE     The genes for MHC class II regulatory factors RFX1 and RFX2 are
            located on the short arm of chromosome 19
  JOURNAL   Genomics 13 (4), 1307-1310 (1992)
   PUBMED   1505960
REFERENCE   10 (residues 1 to 979)
  AUTHORS   Reith,W., Herrero-Sanchez,C., Kobr,M., Silacci,P., Berte,C.,
            Barras,E., Fey,S. and Mach,B.
  TITLE     MHC class II regulatory factor RFX has a novel DNA-binding domain
            and a functionally independent dimerization domain
  JOURNAL   Genes Dev 4 (9), 1528-1540 (1990)
   PUBMED   2253877
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK309824.1, AC020916.8,
            BC049826.1 and BM662273.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 4, 2009 this sequence version replaced NP_002909.3.
            
            Summary: This gene encodes a member of the regulatory factor X
            (RFX) family of transcription factors, which are characterized by a
            winged-helix DNA-binding domain. The encoded transcription factor
            contains an N-terminal activation domain and a C-terminal
            repression domain, and may activate or repress target gene
            expression depending on cellular context. This transcription factor
            has been shown to regulate a wide variety of genes involved in
            immunity and cancer, including the MHC class II genes and genes
            that may be involved in cancer progression. This gene exhibits
            altered expression in glioblastoma and the autoimmune disease
            systemic lupus erythematosis (SLE). [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC049826.1, SRR14038196.271947.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254325.9/ ENSP00000254325.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..979
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..979
                     /product="MHC class II regulatory factor RFX1"
                     /note="transcription factor RFX1; trans-acting regulatory
                     factor 1; enhancer factor C; MHC class II regulatory
                     factor RFX; regulatory factor X, 1 (influences HLA class
                     II expression)"
                     /calculated_mol_wt=104627
     Region          1..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22670.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22670.2)"
     Region          181..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22670.2)"
     Region          216..372
                     /region_name="RFX1_trans_act"
                     /note="RFX1 transcription activation region; pfam04589"
                     /db_xref="CDD:461362"
     Region          370..405
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22670.2)"
     Region          436..513
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     Region          744..979
                     /region_name="Necessary for dimerization"
                     /note="propagated from UniProtKB/Swiss-Prot (P22670.2)"
     Region          915..960
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22670.2)"
     Site            978
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P22670.2)"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P22670.2)"
     CDS             1..979
                     /gene="RFX1"
                     /gene_synonym="EFC; RFX"
                     /coded_by="NM_002918.5:271..3210"
                     /db_xref="CCDS:CCDS12301.1"
                     /db_xref="GeneID:5989"
                     /db_xref="HGNC:HGNC:9982"
                     /db_xref="MIM:600006"
ORIGIN      
        1 matqaytelq aapppsqppq appqaqpqpp pppppaapqp pqpptaaatp qpqyvtelqs
       61 pqpqaqppgg qkqyvtelpa vpapsqptga ptpspapqqy ivvtvsegam rasetvseas
      121 pgstasqtgv ptqvvqqvqg tqqrllvqts vqakpghvsp lqltniqvpq qalptqrlvv
      181 qsaapgskgg qvsltvhgtq qvhsppeqsp vqansssskt agaptgtvpq qlqvhgvqqs
      241 vpvtqersvv qatpqapkpg pvqpltvqgl qpvhvaqevq qlqqvpvphv yssqvqyveg
      301 gdasytasai rsstysypet plytqtasts yyeaagtatq vstpatsqav assgsmpmyv
      361 sgsqvvasst stgagasnss ggggsggggg gggggggggs gstggggsga gtyviqggym
      421 lgsasqsysh ttraspatvq wlldnyetae gvslprstly chyllhcqeq klepvnaasf
      481 gklirsvfmg lrtrrlgtrg nskyhyyglr ikasspllrl medqqhmamr gqpfsqkqrl
      541 kpiqkmegmt ngvavgqqps tglsdisaqv qqyqqfldas rslpdfteld lqgkvlpegv
      601 gpgdikafqv lyrehceaiv dvmvnlqftl vetlwktfwr ynlsqpseap plavhdeaek
      661 rlpkailvll skfepvlqwt khcdnvlyqg lveilipdvl rpipsaltqa irnfaksles
      721 wlthamvnip eemlrvkvaa agafaqtlrr ytslnhlaqa aravlqntaq inqmlsdlnr
      781 vdfanvqeqa swvcrcedrv vqrleqdfkv tlqqqnsleq waawldgvvs qvlkpyqgsa
      841 gfpkaaklfl lkwsfyssmv irdltlrsaa sfgsfhlirl lydeymyyli ehrvaqakge
      901 tpiavmgefa nlatslnpld pdkdeeeeee eesedelpqd islaaggesp algpetlepp
      961 aklartdarg lfvqalpss
//
LOCUS       NP_065704                761 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 287 isoform a [Homo sapiens].
ACCESSION   NP_065704
VERSION     NP_065704.2
DBSOURCE    REFSEQ: accession NM_020653.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Yang,R., Chen,L., Newman,S., Gandhi,K., Doho,G., Moreno,C.S.,
            Vertino,P.M., Bernal-Mizarchi,L., Lonial,S., Boise,L.H., Rossi,M.,
            Kowalski,J. and Qin,Z.S.
  TITLE     Integrated analysis of whole-genome paired-end and mate-pair
            sequencing data for identifying genomic structural variations in
            multiple myeloma
  JOURNAL   Cancer Inform 13 (Suppl 2), 49-53 (2014)
   PUBMED   25288879
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Dang,D.T., Pevsner,J. and Yang,V.W.
  TITLE     The biology of the mammalian Kruppel-like family of transcription
            factors
  JOURNAL   Int J Biochem Cell Biol 32 (11-12), 1103-1121 (2000)
   PUBMED   11137451
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA103127.1, BC057791.1 and
            AC127540.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 19, 2008 this sequence version replaced NP_065704.1.
            
            Summary: This gene encodes a member of the krueppel family of zinc
            finger proteins, suggesting a role as a transcription factor. Its
            specific function has not been determined. This gene is located
            near the Smith-Magenis syndrome region on chromosome 17. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1-4 all encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.199132.1,
                                           SRR1660803.43302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267768 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395825.4/ ENSP00000379169.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..761
                     /product="zinc finger protein 287 isoform a"
                     /note="zinc finger protein with KRAB and SCAN domains 13"
                     /calculated_mol_wt=88208
     Region          46..144
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          134..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBT7.2)"
     Region          170..227
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <364..419
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          370..390
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          398..418
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          422..755
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          426..446
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(431,433,435,437..438,441..442,445,459,461,465..466,
                     469..470,473,487,489,491,493..494,497..498,501)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          454..474
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          482..502
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          510..530
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          538..558
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          566..586
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(571,573,575,577..578,581..582,585,599,601,605..606,
                     609..610,613,627,629,631,633..634,637..638,641)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          594..614
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          622..642
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          650..670
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          678..698
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          706..726
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          734..754
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..761
                     /gene="ZNF287"
                     /gene_synonym="ZKSCAN13; ZSCAN45"
                     /coded_by="NM_020653.4:452..2737"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11179.2"
                     /db_xref="GeneID:57336"
                     /db_xref="HGNC:HGNC:13502"
ORIGIN      
        1 mlasskrmns ssrsqillrw ksdkaqsgpy nvekeiltsr flrdtetcrq nfrnfpypdl
       61 agprkalsql relclkwlrp eihskeqile llvleqflti lpgevrtwvk sqypesseea
      121 vtlvedltqi leeeapqnst lsqdtpeedp rgkhafqtgw lndlvtkesm tfkdvavdit
      181 qedwelmrpv qkelyktvtl qnywnmvslg ltvyrptvip ileepwmvik eilegpspew
      241 etkaqactpv edmskltkee thtikledsy dyddrlerrg kggfwkihtd ergfslksvl
      301 sqeydpteec lskydiyrnn fekhsnlivq fdtqldnkts vynegratfn hvsygivhrk
      361 ilpgekpykc nvcgkkfrky psllkhqsth akeksyecee cgkefrhiss liahqrmhtg
      421 ekpyechqcg kafsqrahlt ihqrihtgek pykcddcgkd fsqrahltih qrthtgekpy
      481 kclecgktfs hssslinhqr vhtgekpyic necgktfsqs thllqhqkih tgkkpykcne
      541 cwkvfsqsty lirhqrihsg ekcykcnecg kafahsstli qhqtthtgek syicnicgka
      601 fsqsanltqh hrthtgekpy kcsvcgkafs qsvhltqhqr ihngekpfkc nicgkayrqg
      661 anltqhqrih tgekpykcne cgkafiysss lnqhqrthtg erpykcnecd kdfsqrtcli
      721 qhqrihtgek pyacricgkt ftqstnliqh qrvhtgakhr n
//
LOCUS       NP_001351213             514 aa            linear   ROD 27-APR-2025
DEFINITION  synaptotagmin-16 isoform 5 [Mus musculus].
ACCESSION   NP_001351213
VERSION     NP_001351213.1
DBSOURCE    REFSEQ: accession NM_001364284.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Fukuda,M.
  TITLE     Molecular cloning, expression, and characterization of a novel
            class of synaptotagmin (Syt XIV) conserved from Drosophila to
            humans
  JOURNAL   J Biochem 133 (5), 641-649 (2003)
   PUBMED   12801916
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC161591.2 and AC158365.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660817.56122.1,
                                           SRR7345562.1632507.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 32.02 cM"
     Protein         1..514
                     /product="synaptotagmin-16 isoform 5"
                     /note="synaptotagmin-16; synaptotagmin 14-like protein;
                     synaptotagmin XIV-related protein"
                     /calculated_mol_wt=57379
     Region          219..342
                     /region_name="C2A_Synaptotagmin-14_16"
                     /note="C2A domain first repeat present in Synaptotagmins
                     14 and 16; cd08389"
                     /db_xref="CDD:176035"
     Region          375..512
                     /region_name="C2B_Synaptotagmin-14_16"
                     /note="C2 domain second repeat present in Synaptotagmins
                     14 and 16; cd08408"
                     /db_xref="CDD:176053"
     CDS             1..514
                     /gene="Syt16"
                     /gene_synonym="Strep14; Syt14l; syt14r"
                     /coded_by="NM_001364284.1:75..1619"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:238266"
                     /db_xref="MGI:MGI:2673872"
ORIGIN      
        1 matditpeai gflsaigvfv vllavlllfi nkklcsenlr ghpypeqrgk rkhsrdktgg
       61 htgtvnsfgd deepstsses dedvtkqfki svsrsqsfrs gvsekgktte leqkikckrl
      121 lcthqedsae gsacedldrt sqlsyseils yedrpisilp qspfesrnvr hhgpcrpemg
      181 mvrslgrpca dgvletetaf eqdgtslqvp hrllepiskc gdldvifeyr avtqkltvti
      241 vraqglpdkd rsgvnswqvh ivllpskkqr gktniqrgpn pvfkekvtft kleprdvasc
      301 avrfrlyaar kmtrermmge klfclshlhp egemkvtlvl eprsnlssge splspsvvsh
      361 sdsasstqsl shggvpellv glsynattgr lsvemikgsh frnlaanrap dtygklflln
      421 cvgqemsrck tsirrgqpnp vyketfvfqv alfqlsdvtl misiysrrtm krkemigwva
      481 lgqnssgeee qehweemkes kgqqtcrwht lles
//
LOCUS       NP_002470                224 aa            linear   PRI 27-APR-2025
DEFINITION  myogenin [Homo sapiens].
ACCESSION   NP_002470
VERSION     NP_002470.2
DBSOURCE    REFSEQ: accession NM_002479.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Gao,Q., Wang,P., Qiu,H., Qiu,B., Yi,W., Tu,W., Lin,B., Sun,D.,
            Zeng,R., Huang,M., Chen,J., Cen,J. and Zhuang,J.
  TITLE     Myogenin suppresses apoptosis induced by angiotensin II in human
            induced pluripotent stem cell-derived cardiomyocytes
  JOURNAL   Biochem Biophys Res Commun 552, 84-90 (2021)
   PUBMED   33743352
  REMARK    GeneRIF: Myogenin suppresses apoptosis induced by angiotensin II in
            human induced pluripotent stem cell-derived cardiomyocytes.
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Cooper,L.M., West,R.C., Hayes,C.S. and Waddell,D.S.
  TITLE     Dual-specificity phosphatase 29 is induced during neurogenic
            skeletal muscle atrophy and attenuates glucocorticoid receptor
            activity in muscle cell culture
  JOURNAL   Am J Physiol Cell Physiol 319 (2), C441-C454 (2020)
   PUBMED   32639872
  REMARK    GeneRIF: Dual-specificity phosphatase 29 is induced during
            neurogenic skeletal muscle atrophy and attenuates glucocorticoid
            receptor activity in muscle cell culture.
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Liu,Z., Zhang,X., Lei,H., Lam,N., Carter,S., Yockey,O., Xu,M.,
            Mendoza,A., Hernandez,E.R., Wei,J.S., Khan,J., Yohe,M.E.,
            Shern,J.F. and Thiele,C.J.
  TITLE     CASZ1 induces skeletal muscle and rhabdomyosarcoma differentiation
            through a feed-forward loop with MYOD and MYOG
  JOURNAL   Nat Commun 11 (1), 911 (2020)
   PUBMED   32060262
  REMARK    GeneRIF: CASZ1 plays a critical role in inducing skeletal
            myogenesis and co-operating to form a feed-forward loop with MYOD
            and MYOG that is critical for Embryonal rhabdomyosarcoma
            differentiation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Funk,W.D. and Wright,W.E.
  TITLE     Cyclic amplification and selection of targets for multicomponent
            complexes: myogenin interacts with factors recognizing binding
            sites for basic helix-loop-helix, nuclear factor 1,
            myocyte-specific enhancer-binding factor 2, and COMP1 factor
  JOURNAL   Proc Natl Acad Sci U S A 89 (20), 9484-9488 (1992)
   PUBMED   1329097
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Chakraborty,T., Martin,J.F. and Olson,E.N.
  TITLE     Analysis of the oligomerization of myogenin and E2A products in
            vivo using a two-hybrid assay system
  JOURNAL   J Biol Chem 267 (25), 17498-17501 (1992)
   PUBMED   1325437
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Salminen,A., Braun,T., Buchberger,A., Jurs,S., Winter,B. and
            Arnold,H.H.
  TITLE     Transcription of the muscle regulatory gene Myf4 is regulated by
            serum components, peptide growth factors and signaling pathways
            involving G proteins
  JOURNAL   J Cell Biol 115 (4), 905-917 (1991)
   PUBMED   1659574
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Lassar,A.B., Davis,R.L., Wright,W.E., Kadesch,T., Murre,C.,
            Voronova,A., Baltimore,D. and Weintraub,H.
  TITLE     Functional activity of myogenic HLH proteins requires
            hetero-oligomerization with E12/E47-like proteins in vivo
  JOURNAL   Cell 66 (2), 305-315 (1991)
   PUBMED   1649701
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Weintraub,H., Davis,R., Tapscott,S., Thayer,M., Krause,M.,
            Benezra,R., Blackwell,T.K., Turner,D., Rupp,R., Hollenberg,S. et
            al.
  TITLE     The myoD gene family: nodal point during specification of the
            muscle cell lineage
  JOURNAL   Science 251 (4995), 761-766 (1991)
   PUBMED   1846704
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC053899.1 and AC105940.2.
            
            On Feb 19, 2002 this sequence version replaced NP_002470.1.
            
            Summary: Myogenin is a muscle-specific transcription factor that
            can induce myogenesis in a variety of cell types in tissue culture.
            It is a member of a large family of proteins related by sequence
            homology, the helix-loop-helix (HLH) proteins. It is essential for
            the development of functional skeletal muscle. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053899.1, X17651.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000241651.5/ ENSP00000241651.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..224
                     /product="myogenin"
                     /note="myogenic factor 4; class C basic helix-loop-helix
                     protein 3"
                     /calculated_mol_wt=24906
     Region          1..86
                     /region_name="BASIC"
                     /note="Basic domain in HLH proteins of MYOD family;
                     smart00520"
                     /db_xref="CDD:128794"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2G.
                     /evidence=ECO:0000250|UniProtKB:P20428; propagated from
                     UniProtKB/Swiss-Prot (P15173.2)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2G.
                     /evidence=ECO:0000250|UniProtKB:P20428; propagated from
                     UniProtKB/Swiss-Prot (P15173.2)"
     Region          81..139
                     /region_name="bHLH_TS_MYOG_Myf4"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     myogenin (MYOG) and similar proteins; cd18935"
                     /db_xref="CDD:381505"
     Site            order(82..83,87,89..91,93,98,115..118)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381505"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CaMK2G.
                     /evidence=ECO:0000250|UniProtKB:P20428; propagated from
                     UniProtKB/Swiss-Prot (P15173.2)"
     Site            order(96..97,100..101,103..104,119,122,126,128..129,133,
                     135..136)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381505"
     CDS             1..224
                     /gene="MYOG"
                     /gene_synonym="bHLHc3; myf-4; MYF4"
                     /coded_by="NM_002479.6:52..726"
                     /db_xref="CCDS:CCDS1433.1"
                     /db_xref="GeneID:4656"
                     /db_xref="HGNC:HGNC:7612"
                     /db_xref="MIM:159980"
ORIGIN      
        1 melyetspyf yqeprfydge nylpvhlqgf eppgyertel tlspeapgpl edkglgtpeh
       61 cpgqclpwac kvckrksvsv drrraatlre krrlkkvnea fealkrstll npnqrlpkve
      121 ilrsaiqyie rlqallssln qeerdlryrg gggpqpgvps ecsshsascs pewgsalefs
      181 anpgdhllta dptdahnlhs ltsivdsitv edvsvafpde tmpn
//
LOCUS       NP_001917                100 aa            linear   PRI 27-APR-2025
DEFINITION  defensin-6 preproprotein [Homo sapiens].
ACCESSION   NP_001917
VERSION     NP_001917.1
DBSOURCE    REFSEQ: accession NM_001926.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Barthold,L., Heber,S., Schmidt,C.Q., Gradl,M., Weidinger,G.,
            Barth,H. and Fischer,S.
  TITLE     Human alpha-Defensin-6 Neutralizes Clostridioides difficile Toxins
            TcdA and TcdB by Direct Binding
  JOURNAL   Int J Mol Sci 23 (9), 4509 (2022)
   PUBMED   35562899
  REMARK    GeneRIF: Human alpha-Defensin-6 Neutralizes Clostridioides
            difficile Toxins TcdA and TcdB by Direct Binding.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Feng,S., Zhong,Z., Fan,J., Li,X., Shi,D. and Jiang,L.
  TITLE     Upregulated Expression of Intestinal Antimicrobial Peptide HD5
            Associated with Renal Function in IgA Nephropathy
  JOURNAL   Dis Markers 2020, 2078279 (2020)
   PUBMED   32089753
  REMARK    GeneRIF: Upregulated Expression of Intestinal Antimicrobial Peptide
            HD5 Associated with Renal Function in IgA Nephropathy.
            Erratum:[Dis Markers. 2022 Aug 17;2022:9797825. doi:
            10.1155/2022/9797825. PMID: 36033832]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 100)
  AUTHORS   Jeong,D., Kim,H., Kim,D., Ban,S., Oh,S., Ji,S., Kang,D., Lee,H.,
            Ahn,T.S., Kim,H.J., Bae,S.B., Lee,M.S., Kim,C.J., Kwon,H.Y. and
            Baek,M.J.
  TITLE     Defensin alpha 6 (DEFA6) is a prognostic marker in colorectal
            cancer
  JOURNAL   Cancer Biomark 24 (4), 485-495 (2019)
   PUBMED   30932884
  REMARK    GeneRIF: DEFA6 is associated with overall survival rate of CRC
            patients and thus an independent prognostic marker for CRC. These
            results suggest that DEFA6 plays an essential oncogenic role in CRC
            and serves a good therapeutic target for the disease.
REFERENCE   6  (residues 1 to 100)
  AUTHORS   Chu,H., Pazgier,M., Jung,G., Nuccio,S.P., Castillo,P.A., de
            Jong,M.F., Winter,M.G., Winter,S.E., Wehkamp,J., Shen,B.,
            Salzman,N.H., Underwood,M.A., Tsolis,R.M., Young,G.M., Lu,W.,
            Lehrer,R.I., Baumler,A.J. and Bevins,C.L.
  TITLE     Human alpha-defensin 6 promotes mucosal innate immunity through
            self-assembled peptide nanonets
  JOURNAL   Science 337 (6093), 477-481 (2012)
   PUBMED   22722251
  REMARK    GeneRIF: study reports that HD6 affords protection against invasion
            by enteric bacterial pathogens in vitro and in vivo; after
            stochastic binding to bacterial surface proteins, HD6 undergoes
            ordered self-assembly to form fibrils and nanonets that surround
            and entangle bacteria
REFERENCE   7  (residues 1 to 100)
  AUTHORS   Nam,M.J., Kee,M.K., Kuick,R. and Hanash,S.M.
  TITLE     Identification of defensin alpha6 as a potential biomarker in colon
            adenocarcinoma
  JOURNAL   J Biol Chem 280 (9), 8260-8265 (2005)
   PUBMED   15613481
  REMARK    GeneRIF: defensin alpha6 is highly expressed in colon cancer cell
            lines
REFERENCE   8  (residues 1 to 100)
  AUTHORS   Mallow,E.B., Harris,A., Salzman,N., Russell,J.P.,
            DeBerardinis,R.J., Ruchelli,E. and Bevins,C.L.
  TITLE     Human enteric defensins. Gene structure and developmental
            expression
  JOURNAL   J Biol Chem 271 (8), 4038-4045 (1996)
   PUBMED   8626737
REFERENCE   9  (residues 1 to 100)
  AUTHORS   Bevins,C.L., Jones,D.E., Dutra,A., Schaffzin,J. and Muenke,M.
  TITLE     Human enteric defensin genes: chromosomal map position and a model
            for possible evolutionary relationships
  JOURNAL   Genomics 31 (1), 95-106 (1996)
   PUBMED   8808285
REFERENCE   10 (residues 1 to 100)
  AUTHORS   Jones,D.E. and Bevins,C.L.
  TITLE     Defensin-6 mRNA in human Paneth cells: implications for
            antimicrobial peptides in host defense of the human bowel
  JOURNAL   FEBS Lett 315 (2), 187-192 (1993)
   PUBMED   8417977
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC069667.1 and BM855691.1.
            
            Summary: Defensins are a family of antimicrobial and cytotoxic
            peptides thought to be involved in host defense. They are abundant
            in the granules of neutrophils and also found in the epithelia of
            mucosal surfaces such as those of the intestine, respiratory tract,
            urinary tract, and vagina. Members of the defensin family are
            highly similar in protein sequence and distinguished by a conserved
            cysteine motif. Several alpha defensin genes appear to be clustered
            on chromosome 8. The protein encoded by this gene, defensin, alpha
            6, is highly expressed in the secretory granules of Paneth cells of
            the small intestine, and likely plays a role in host defense of
            human bowel. [provided by RefSeq, Oct 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY306549.1, HY151424.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000297436.3/
                                                  ENSP00000297436.2
            Protein has antimicrobial activity :: PMID: 22722251
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..100
                     /product="defensin-6 preproprotein"
                     /note="defensin-6; defensin, alpha 6, Paneth
                     cell-specific"
                     /calculated_mol_wt=8967
     Region          1..58
                     /region_name="Defensin_propep"
                     /note="Defensin propeptide; pfam00879"
                     /db_xref="CDD:459976"
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2027
     proprotein      20..100
                     /product="defensin-6 proprotein"
                     /calculated_mol_wt=8967
     mat_peptide     69..100
                     /product="defensin-6"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     22722251]"
                     /calculated_mol_wt=3714
     Region          72..99
                     /region_name="Defensin_1"
                     /note="Mammalian defensin; pfam00323"
                     /db_xref="CDD:425607"
     CDS             1..100
                     /gene="DEFA6"
                     /gene_synonym="DEF6; HD-6"
                     /coded_by="NM_001926.4:42..344"
                     /db_xref="CCDS:CCDS5960.1"
                     /db_xref="GeneID:1671"
                     /db_xref="HGNC:HGNC:2765"
                     /db_xref="MIM:600471"
ORIGIN      
        1 mrtltiltav llvalqakae plqaeddplq akayeadaqe qrgandqdfa vsfaedasss
       61 lralgstraf tchcrrscys teysygtctv mginhrfccl
//
LOCUS       NP_003684                830 aa            linear   PRI 27-APR-2025
DEFINITION  scavenger receptor class F member 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_003684
VERSION     NP_003684.2
DBSOURCE    REFSEQ: accession NM_003693.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Jorge,A.M., Lao,T., Kim,R., Licciardi,S., El Khoury,J.,
            Luster,A.D., Means,T.K. and Ramirez-Ortiz,Z.G.
  TITLE     SCARF1-Induced Efferocytosis Plays an Immunomodulatory Role in
            Humans, and Autoantibodies Targeting SCARF1 Are Produced in
            Patients with Systemic Lupus Erythematosus
  JOURNAL   J Immunol 208 (4), 955-967 (2022)
   PUBMED   35082161
  REMARK    GeneRIF: SCARF1-Induced Efferocytosis Plays an Immunomodulatory
            Role in Humans, and Autoantibodies Targeting SCARF1 Are Produced in
            Patients with Systemic Lupus Erythematosus.
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Zhang,R., Peng,X., Lin,J., Zhang,Y., Zhan,L., Tian,X., Yin,J. and
            Zhao,G.
  TITLE     The Role of SREC- in Innate Immunity to Aspergillus fumigatus
            Keratitis
  JOURNAL   Invest Ophthalmol Vis Sci 62 (9), 12 (2021)
   PUBMED   34236384
  REMARK    GeneRIF: The Role of SREC- in Innate Immunity to Aspergillus
            fumigatus Keratitis.
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 830)
  AUTHORS   Wicker-Planquart,C., Dufour,S., Tacnet-Delorme,P., Bally,I.,
            Delneste,Y., Frachet,P., Housset,D. and Thielens,N.M.
  TITLE     Molecular and Cellular Interactions of Scavenger Receptor SR-F1
            With Complement C1q Provide Insights Into Its Role in the Clearance
            of Apoptotic Cells
  JOURNAL   Front Immunol 11, 544 (2020)
   PUBMED   32296440
  REMARK    GeneRIF: Molecular and Cellular Interactions of Scavenger Receptor
            SR-F1 With Complement C1q Provide Insights Into Its Role in the
            Clearance of Apoptotic Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 830)
  AUTHORS   Calderwood,S.K., Mambula,S.S., Gray,P.J. Jr. and Theriault,J.R.
  TITLE     Extracellular heat shock proteins in cell signaling
  JOURNAL   FEBS Lett 581 (19), 3689-3694 (2007)
   PUBMED   17499247
  REMARK    Review article
REFERENCE   6  (residues 1 to 830)
  AUTHORS   Jeannin,P., Bottazzi,B., Sironi,M., Doni,A., Rusnati,M., Presta,M.,
            Maina,V., Magistrelli,G., Haeuw,J.F., Hoeffel,G., Thieblemont,N.,
            Corvaia,N., Garlanda,C., Delneste,Y. and Mantovani,A.
  TITLE     Complexity and complementarity of outer membrane protein A
            recognition by cellular and humoral innate immunity receptors
  JOURNAL   Immunity 22 (5), 551-560 (2005)
   PUBMED   15894273
REFERENCE   7  (residues 1 to 830)
  AUTHORS   Ishii,J., Adachi,H., Aoki,J., Koizumi,H., Tomita,S., Suzuki,T.,
            Tsujimoto,M., Inoue,K. and Arai,H.
  TITLE     SREC-II, a new member of the scavenger receptor type F family,
            trans-interacts with SREC-I through its extracellular domain
  JOURNAL   J Biol Chem 277 (42), 39696-39702 (2002)
   PUBMED   12154095
  REMARK    GeneRIF: SRECI binds to SRECII and has a similar tissue
            distribution pattern
REFERENCE   8  (residues 1 to 830)
  AUTHORS   Adachi,H. and Tsujimoto,M.
  TITLE     Characterization of the human gene encoding the scavenger receptor
            expressed by endothelial cell and its regulation by a novel
            transcription factor, endothelial zinc finger protein-2
  JOURNAL   J Biol Chem 277 (27), 24014-24021 (2002)
   PUBMED   11978792
  REMARK    GeneRIF: Characterization of the gene and its regulation by a novel
            transcription factor, endothelial zinc protein-2
REFERENCE   9  (residues 1 to 830)
  AUTHORS   Dhaliwal,B.S. and Steinbrecher,U.P.
  TITLE     Scavenger receptors and oxidized low density lipoproteins
  JOURNAL   Clin Chim Acta 286 (1-2), 191-205 (1999)
   PUBMED   10511292
  REMARK    Review article
REFERENCE   10 (residues 1 to 830)
  AUTHORS   Adachi,H., Tsujimoto,M., Arai,H. and Inoue,K.
  TITLE     Expression cloning of a novel scavenger receptor from human
            endothelial cells
  JOURNAL   J Biol Chem 272 (50), 31217-31220 (1997)
   PUBMED   9395444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK291810.1, AC130343.7 and
            CA434049.1.
            
            On Aug 12, 2003 this sequence version replaced NP_003684.1.
            
            Summary: The protein encoded by this gene is a scavenger receptor
            that is expressed in endothelial cells. It regulates the uptake of
            chemically modified low density lipoproteins, including acetylated
            low density lipoprotein (Ac-LDL), and it may be involved in
            atherogenesis. This gene is regulated by the transcription factors
            ZNF444/EZF-2 and SP1. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Apr 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291810.1, BC039735.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263071.9/ ENSP00000263071.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..830
                     /product="scavenger receptor class F member 1 isoform 1
                     precursor"
                     /note="acetyl LDL receptor; scavenger receptor expressed
                     by endothelial cells 1"
                     /calculated_mol_wt=85353
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2053
     mat_peptide     20..830
                     /product="Scavenger receptor class F member 1.
                     /id=PRO_0000007738"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14162.3)"
                     /calculated_mol_wt=85353
     Region          <111..202
                     /region_name="gliding_CglD"
                     /note="adventurous gliding motility lipoprotein CglD;
                     NF033765"
                     /db_xref="CDD:468178"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14162.3)"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14162.3)"
     Site            393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14162.3)"
     Site            422..442
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14162.3)"
     Region          516..539
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14162.3)"
     Region          <540..830
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          581..688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14162.3)"
     Site            589
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5ND28; propagated from
                     UniProtKB/Swiss-Prot (Q14162.3)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14162.3)"
     Region          715..830
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14162.3)"
     CDS             1..830
                     /gene="SCARF1"
                     /gene_synonym="SREC; SREC-I; SREC1"
                     /coded_by="NM_003693.4:36..2528"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS11007.1"
                     /db_xref="GeneID:8578"
                     /db_xref="HGNC:HGNC:16820"
                     /db_xref="MIM:607873"
ORIGIN      
        1 mglglllpll llwtrgtqgs eldpkgqhvc vasspsaelq ccagwrqkdq ectipicegp
       61 dacqkdevcv kpglcrckpg ffgahcssrc pgqywgpdcr escpchphgq cepatgacqc
      121 qadrwgarce fpcacgphgr cdpatgvchc epgwwsstcr rpcqcntaaa rceqatgacv
      181 ckpgwwgrrc sfrcnchgsp ceqdsgrcac rpgwwgpecq qqcecvrgrc saasgectcp
      241 pgfrgarcel pcpagshgvq cahscgrckh nepcspdtgs cescepgwng tqcqqpclpg
      301 tfgesceqqc phcrhgeace pdtghcqrcd pgwlgprced pcptgtfged cgstcptcvq
      361 gscdtvtgdc vcsagywgps cnascpagfh gnncsvpcec peglchpvsg scqpgsgsrd
      421 taliagslvp llllflglac cacccwaprs dlkdrpardg atvsrmklqv wgtltslgst
      481 lpcrslsshk lpwvtvshhd pevpfnhsfi eppsagwatd dsfssdpesg eadevpaycv
      541 ppqegmvpva qagsseasla agafpppeda stpfaiprts slarakrpsv sfaegtkfap
      601 qsrrssgels splrkpkrls rgaqsgpegr eaeestgpee aeapesfpaa aspgdsatgh
      661 rrpplggrtv aehveaiegs vqessgpvtt iymlagkprg segpvrsvfr hfgsfqkgqa
      721 eakvkraipk pprqalnrkk gspglasgsv gqspnsapka glpgatgpma vrpeeavrgl
      781 gagtessrra qepvsgcgsp eqdpqkqaee erqeepeyen vvpisrppep
//
LOCUS       NP_001342455             127 aa            linear   PRI 27-APR-2025
DEFINITION  EF-hand calcium-binding domain-containing protein 10 isoform 1
            [Homo sapiens].
ACCESSION   NP_001342455 XP_001719500 XP_001719502 XP_001723093 XP_001723095
            XP_001725578 XP_001725579 XP_001725859 XP_001725861
VERSION     NP_001342455.1
DBSOURCE    REFSEQ: accession NM_001355526.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Winham,S.J., Cuellar-Barboza,A.B., Oliveros,A., McElroy,S.L.,
            Crow,S., Colby,C., Choi,D.S., Chauhan,M., Frye,M. and
            Biernacka,J.M.
  TITLE     Genome-wide association study of bipolar disorder accounting for
            effect of body mass index identifies a new risk allele in TCF7L2
  JOURNAL   Mol Psychiatry 19 (9), 1010-1016 (2014)
   PUBMED   24322204
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC105284.1 and BE502251.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105284.1, SRR5189667.362273.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000480514.6/ ENSP00000418678.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..127
                     /product="EF-hand calcium-binding domain-containing
                     protein 10 isoform 1"
                     /note="EF-hand domain-containing protein; eF-hand
                     calcium-binding domain-containing protein 10"
                     /calculated_mol_wt=14590
     Region          7..53
                     /region_name="DD_EFCAB10"
                     /note="dimerization/docking (D/D) domain found in EF-hand
                     calcium-binding domain-containing protein 10 (EFCAB10) and
                     similar proteins; cd22976"
                     /db_xref="CDD:438545"
     CDS             1..127
                     /gene="EFCAB10"
                     /coded_by="NM_001355526.2:31..414"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS87537.1"
                     /db_xref="GeneID:100130771"
                     /db_xref="HGNC:HGNC:34531"
ORIGIN      
        1 metssrelqa aeylekhqik evvsyltsal lffrpekpke ylisllerlr iakvtgvafp
       61 ffmdnsniva mfemmdssgr gtisfvqyke alktlglcte dedlqddghk itldkfkeev
      121 nkrmkei
//
LOCUS       NP_065979               1215 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger SWIM domain-containing protein 6 [Homo sapiens].
ACCESSION   NP_065979 XP_001716206 XP_035299 XP_941366
VERSION     NP_065979.1
DBSOURCE    REFSEQ: accession NM_020928.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1215)
  AUTHORS   Cha,M.Y., Hong,Y.J., Choi,J.E., Kwon,T.S., Kim,I.J. and Hong,K.W.
  TITLE     Classification of early age facial growth pattern and
            identification of the genetic basis in two Korean populations
  JOURNAL   Sci Rep 12 (1), 13828 (2022)
   PUBMED   35970861
  REMARK    GeneRIF: Classification of early age facial growth pattern and
            identification of the genetic basis in two Korean populations.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1215)
  AUTHORS   Palmer,E.E., Kumar,R., Gordon,C.T., Shaw,M., Hubert,L., Carroll,R.,
            Rio,M., Murray,L., Leffler,M., Dudding-Byth,T., Oufadem,M.,
            Lalani,S.R., Lewis,A.M., Xia,F., Tam,A., Webster,R., Brammah,S.,
            Filippini,F., Pollard,J., Spies,J., Minoche,A.E., Cowley,M.J.,
            Risen,S., Powell-Hamilton,N.N., Tusi,J.E., Immken,L., Nagakura,H.,
            Bole-Feysot,C., Nitschke,P., Garrigue,A., de Saint Basile,G.,
            Kivuva,E., Scott,R.H., Rendon,A., Munnich,A., Newman,W., Kerr,B.,
            Besmond,C., Rosenfeld,J.A., Amiel,J., Field,M. and Gecz,J.
  CONSRTM   DDD Study
  TITLE     A Recurrent De Novo Nonsense Variant in ZSWIM6 Results in Severe
            Intellectual Disability without Frontonasal or Limb Malformations
  JOURNAL   Am J Hum Genet 101 (6), 995-1005 (2017)
   PUBMED   29198722
  REMARK    GeneRIF: This study builds support for a key role for ZSWIM6 in
            neuronal development and function, in addition to its putative
            roles in limb and craniofacial development, and provides a striking
            example of different variants in the same gene leading to distinct
            phenotypes.
REFERENCE   3  (residues 1 to 1215)
  AUTHORS   Twigg,S.R., Ousager,L.B., Miller,K.A., Zhou,Y., Elalaoui,S.C.,
            Sefiani,A., Bak,G.S., Hove,H., Hansen,L.K., Fagerberg,C.R.,
            Tajir,M. and Wilkie,A.O.
  TITLE     Acromelic frontonasal dysostosis and ZSWIM6 mutation: phenotypic
            spectrum and mosaicism
  JOURNAL   Clin Genet 90 (3), 270-275 (2016)
   PUBMED   26706854
  REMARK    GeneRIF: A single recurrent heterozygous missense substitution in
            ZSWIM6, encoding a protein of unknown function, was previously
            shown to underlie this disorder in four unrelated cases. Here we
            describe four additional individuals from three families,
            comprising two sporadic subjects (one of whom had no limb
            malformation) and a mildly affected female with a severely affected
            son
REFERENCE   4  (residues 1 to 1215)
  AUTHORS   Smith,J.D., Hing,A.V., Clarke,C.M., Johnson,N.M., Perez,F.A.,
            Park,S.S., Horst,J.A., Mecham,B., Maves,L., Nickerson,D.A. and
            Cunningham,M.L.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Exome sequencing identifies a recurrent de novo ZSWIM6 mutation
            associated with acromelic frontonasal dysostosis
  JOURNAL   Am J Hum Genet 95 (2), 235-240 (2014)
   PUBMED   25105228
  REMARK    GeneRIF: Exome sequencing of one trio and two unrelated probands
            revealed the same heterozygous variant (c.3487C>T [p.
            Arg1163Trp])associated with acromelic frontonasal dysostosis in a
            highly conserved protein domain of ZSWIM6; this variant has not
            been seen in the 1000 Genomes data, dbSNP, or the Exome Sequencing
            Project
REFERENCE   5  (residues 1 to 1215)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   6  (residues 1 to 1215)
  AUTHORS   Ripke,S., O'Dushlaine,C., Chambert,K., Moran,J.L., Kahler,A.K.,
            Akterin,S., Bergen,S.E., Collins,A.L., Crowley,J.J., Fromer,M.,
            Kim,Y., Lee,S.H., Magnusson,P.K., Sanchez,N., Stahl,E.A.,
            Williams,S., Wray,N.R., Xia,K., Bettella,F., Borglum,A.D.,
            Bulik-Sullivan,B.K., Cormican,P., Craddock,N., de Leeuw,C.,
            Durmishi,N., Gill,M., Golimbet,V., Hamshere,M.L., Holmans,P.,
            Hougaard,D.M., Kendler,K.S., Lin,K., Morris,D.W., Mors,O.,
            Mortensen,P.B., Neale,B.M., O'Neill,F.A., Owen,M.J.,
            Milovancevic,M.P., Posthuma,D., Powell,J., Richards,A.L.,
            Riley,B.P., Ruderfer,D., Rujescu,D., Sigurdsson,E., Silagadze,T.,
            Smit,A.B., Stefansson,H., Steinberg,S., Suvisaari,J., Tosato,S.,
            Verhage,M., Walters,J.T., Levinson,D.F., Gejman,P.V., Kendler,K.S.,
            Laurent,C., Mowry,B.J., O'Donovan,M.C., Owen,M.J., Pulver,A.E.,
            Riley,B.P., Schwab,S.G., Wildenauer,D.B., Dudbridge,F., Holmans,P.,
            Shi,J., Albus,M., Alexander,M., Campion,D., Cohen,D., Dikeos,D.,
            Duan,J., Eichhammer,P., Godard,S., Hansen,M., Lerer,F.B.,
            Liang,K.Y., Maier,W., Mallet,J., Nertney,D.A., Nestadt,G.,
            Norton,N., O'Neill,F.A., Papadimitriou,G.N., Ribble,R.,
            Sanders,A.R., Silverman,J.M., Walsh,D., Williams,N.M., Wormley,B.,
            Arranz,M.J., Bakker,S., Bender,S., Bramon,E., Collier,D.,
            Crespo-Facorro,B., Hall,J., Iyegbe,C., Jablensky,A., Kahn,R.S.,
            Kalaydjieva,L., Lawrie,S., Lewis,C.M., Lin,K., Linszen,D.H.,
            Mata,I., McIntosh,A., Murray,R.M., Ophoff,R.A., Powell,J.,
            Rujescu,D., Van Os,J., Walshe,M., Weisbrod,M., Wiersma,D.,
            Donnelly,P., Barroso,I., Blackwell,J.M., Bramon,E., Brown,M.A.,
            Casas,J.P., Corvin,A.P., Deloukas,P., Duncanson,A., Jankowski,J.,
            Markus,H.S., Mathew,C.G., Palmer,C.N., Plomin,R., Rautanen,A.,
            Sawcer,S.J., Trembath,R.C., Viswanathan,A.C., Wood,N.W.,
            Spencer,C.C., Band,G., Bellenguez,C., Freeman,C., Hellenthal,G.,
            Giannoulatou,E., Pirinen,M., Pearson,R.D., Strange,A., Su,Z.,
            Vukcevic,D., Donnelly,P., Langford,C., Hunt,S.E., Edkins,S.,
            Gwilliam,R., Blackburn,H., Bumpstead,S.J., Dronov,S., Gillman,M.,
            Gray,E., Hammond,N., Jayakumar,A., McCann,O.T., Liddle,J.,
            Potter,S.C., Ravindrarajah,R., Ricketts,M.,
            Tashakkori-Ghanbaria,A., Waller,M.J., Weston,P., Widaa,S.,
            Whittaker,P., Barroso,I., Deloukas,P., Mathew,C.G., Blackwell,J.M.,
            Brown,M.A., Corvin,A.P., McCarthy,M.I., Spencer,C.C., Bramon,E.,
            Corvin,A.P., O'Donovan,M.C., Stefansson,K., Scolnick,E.,
            Purcell,S., McCarroll,S.A., Sklar,P., Hultman,C.M. and
            Sullivan,P.F.
  CONSRTM   Multicenter Genetic Studies of Schizophrenia Consortium; Psychosis
            Endophenotypes International Consortium; Wellcome Trust Case
            Control Consortium 2
  TITLE     Genome-wide association analysis identifies 13 new risk loci for
            schizophrenia
  JOURNAL   Nat Genet 45 (10), 1150-1159 (2013)
   PUBMED   23974872
REFERENCE   7  (residues 1 to 1215)
  AUTHORS   Bergen,S.E., O'Dushlaine,C.T., Ripke,S., Lee,P.H., Ruderfer,D.M.,
            Akterin,S., Moran,J.L., Chambert,K.D., Handsaker,R.E., Backlund,L.,
            Osby,U., McCarroll,S., Landen,M., Scolnick,E.M., Magnusson,P.K.,
            Lichtenstein,P., Hultman,C.M., Purcell,S.M., Sklar,P. and
            Sullivan,P.F.
  TITLE     Genome-wide association study in a Swedish population yields
            support for greater CNV and MHC involvement in schizophrenia
            compared with bipolar disorder
  JOURNAL   Mol Psychiatry 17 (9), 880-886 (2012)
   PUBMED   22688191
REFERENCE   8  (residues 1 to 1215)
  AUTHORS   Kai,N., Iwase,K., Imai,K., Nakahira,E., Soma,M., Ohtsuka,S.,
            Yagi,T., Kobayashi,K., Koga,H., Takiguchi,M. and Yuasa,S.
  TITLE     Altered gene expression in the subdivisions of the amygdala of
            Fyn-deficient mice as revealed by laser capture microdissection and
            mKIAA cDNA array analysis
  JOURNAL   Brain Res 1073-1074, 60-70 (2006)
   PUBMED   16427614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC122718.2, AC008836.6,
            BF751445.1, BF750632.1, AA740254.1, AB046797.1 and AW136453.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Nov 1, 2008 this sequence version replaced
            XP_035299.7, XP_941366.1, XP_001716206.1.
            
            Summary: The protein encoded by this gene contains a zinc finger
            SWI2/SNF2 and MuDR (SWIM) domain. Proteins with SWIM domains have
            been found in a diverse number of species and are predicted to
            interact with DNA or proteins. Mutations in this gene result in
            acromelic frontonasal dysostosis. [provided by RefSeq, Apr 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by orthologous and paralogous data.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000252744.6/ ENSP00000252744.5
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.1"
     Protein         1..1215
                     /product="zinc finger SWIM domain-containing protein 6"
                     /note="zinc finger, SWIM domain containing 6"
                     /calculated_mol_wt=133340
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCJ5.2)"
     Region          133..161
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCJ5.2)"
     Region          207..>333
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
     CDS             1..1215
                     /gene="ZSWIM6"
                     /gene_synonym="AFND; NEDMAGA"
                     /coded_by="NM_020928.2:16..3663"
                     /db_xref="CCDS:CCDS47215.1"
                     /db_xref="GeneID:57688"
                     /db_xref="HGNC:HGNC:29316"
                     /db_xref="MIM:615951"
ORIGIN      
        1 maergqqppp akrlccrpgg ggggggssgg gggagggyss acrpgpragg aaaaaacggg
       61 aalgllppgk tqspeslldi aarrvaekwp fqrveerfer ipepvqrriv ywsfprsere
      121 icmyssfntg ggaaggpgdd sgggggaggg ggggsssspa atsaaatsaa aaaaaaaaaa
      181 aaaagagaps vgaagaadgg detrlpfrrg iallesgcvd nvlqvgfhls gtvtepaiqs
      241 epetvcnvai sfdrckitsv tcscgnkdif ycahvvalsl yrirkpdqvk lhlpisetlf
      301 qmnrdqlqkf vqylitvhht evlptaqkla deilsqnsei nqvhgapdpt agasiddenc
      361 whldeeqvqe qvklflsqgg yhgsgkqlnl lfakvremlk mrdsngarml tliteqfmad
      421 prlslwrqqg tamtdkyrql wdelgalwmc ivlnphckle qkaswlkqlk kwnsvdvcpw
      481 edgnhgselp nltnalpqga nanqdssnrp hrtvftraie acdlhwqdsh lqhiissdly
      541 tnycyhddte nslfdsrgwp lwhehvptac arvdalrshg yprealrlai aivntlrrqq
      601 qkqlemfrtq kkelphknit sitnlegwvg hpldpvgtlf sslmeacrid denlsgfsdf
      661 tenmgqcksl eyqhlpahkf leegesyltl avevaliglg qqrimpdgly tqekvcrnee
      721 qlisklqeie lddtlvkifr kqavflleag pysglgeiih resvpmhtfa kylftsllph
      781 daelaykial ramrllvles tapsgdltrp hhiasvvpnr yprwftlshi esqqcelast
      841 mltaakgdvr rletvlesiq knihssshif klaqdafkia tlmdslpdit llkvslelgl
      901 qvmrmtlstl nwrrremvrw lvtcatevgv yaldsimqtw ftlftpteat sivattvmsn
      961 stivrlhldc hqqeklassa rtlalqcamk dpqncalsal tlcekdhiaf etayqivlda
     1021 attgmsytql ftiarymehr gypmraykla tlamthlnls ynqdthpain dvlwacalsh
     1081 slgknelaai iplvvksvkc atvlsdilrr ctlttpgmvg lhgrrnsgkl msldkaplrq
     1141 lldatigayi ntthsrlthi sprhysefie flskaretfl mahdghiqft qfidnlkqiy
     1201 kgkkklmmlv rerfg
//
LOCUS       NP_067042                298 aa            linear   PRI 27-APR-2025
DEFINITION  junctional adhesion molecule B isoform 1 precursor [Homo sapiens].
ACCESSION   NP_067042
VERSION     NP_067042.1
DBSOURCE    REFSEQ: accession NM_021219.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Khojasteh,M., Soleimani,P., Ghasemi,A., Taghizadeh,P., Rohani,M.
            and Alavi,A.
  TITLE     JAM2 variants can be more common in primary familial brain
            calcification (PFBC) cases than those appear; may be due to a
            founder mutation
  JOURNAL   Neurol Sci 45 (8), 3829-3844 (2024)
   PUBMED   38441788
  REMARK    GeneRIF: JAM2 variants can be more common in primary familial brain
            calcification (PFBC) cases than those appear; may be due to a
            founder mutation.
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Dong,Y., Zhang,J., Xie,S., Di,S., Fan,B. and Gong,T.
  TITLE     JAM2 is a prognostic biomarker and inhibits proliferation,
            metastasis and epithelial-mesenchymal transition in lung
            adenocarcinoma
  JOURNAL   J Gene Med 26 (2), e3679 (2024)
   PUBMED   38404047
  REMARK    GeneRIF: JAM2 is a prognostic biomarker and inhibits proliferation,
            metastasis and epithelial-mesenchymal transition in lung
            adenocarcinoma.
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Peng,Y., Li,H., Fu,Y., Guo,S., Qu,C., Zhang,Y., Zong,B. and Liu,S.
  TITLE     JAM2 predicts a good prognosis and inhibits invasion and migration
            by suppressing EMT pathway in breast cancer
  JOURNAL   Int Immunopharmacol 103, 108430 (2022)
   PUBMED   34923424
  REMARK    GeneRIF: JAM2 predicts a good prognosis and inhibits invasion and
            migration by suppressing EMT pathway in breast cancer.
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Schottlaender,L.V., Abeti,R., Jaunmuktane,Z., Macmillan,C.,
            Chelban,V., O'Callaghan,B., McKinley,J., Maroofian,R.,
            Efthymiou,S., Athanasiou-Fragkouli,A., Forbes,R., Soutar,M.P.M.,
            Livingston,J.H., Kalmar,B., Swayne,O., Hotton,G., Pittman,A.,
            Mendes de Oliveira,J.R., de Grandis,M., Richard-Loendt,A.,
            Launchbury,F., Althonayan,J., McDonnell,G., Carr,A., Khan,S.,
            Beetz,C., Bisgin,A., Tug Bozdogan,S., Begtrup,A., Torti,E.,
            Greensmith,L., Giunti,P., Morrison,P.J., Brandner,S.,
            Aurrand-Lions,M. and Houlden,H.
  CONSRTM   SYNAPS Study Group
  TITLE     Bi-allelic JAM2 Variants Lead to Early-Onset Recessive Primary
            Familial Brain Calcification
  JOURNAL   Am J Hum Genet 106 (3), 412-421 (2020)
   PUBMED   32142645
  REMARK    GeneRIF: Along with JAM3 and OCLN, JAM2 is the third tight-junction
            gene in which bi-allelic variants are associated with brain
            calcification, suggesting that defective cell-to-cell adhesion and
            dysfunction of the movement of solutes through the paracellular
            spaces in the neurovascular unit is a key mechanism in CNS
            calcification
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Cen,Z., Chen,Y., Chen,S., Wang,H., Yang,D., Zhang,H., Wu,H.,
            Wang,L., Tang,S., Ye,J., Shen,J., Wang,H., Fu,F., Chen,X., Xie,F.,
            Liu,P., Xu,X., Cao,J., Cai,P., Pan,Q., Li,J., Yang,W., Shan,P.F.,
            Li,Y., Liu,J.Y., Zhang,B. and Luo,W.
  TITLE     Biallelic loss-of-function mutations in JAM2 cause primary familial
            brain calcification
  JOURNAL   Brain 143 (2), 491-502 (2020)
   PUBMED   31851307
  REMARK    GeneRIF: mutant JAM2 protein resulted in impaired cell-cell
            adhesion functions and reduced integrity of the neurovascular unit
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Liang,T.W., Chiu,H.H., Gurney,A., Sidle,A., Tumas,D.B., Schow,P.,
            Foster,J., Klassen,T., Dennis,K., DeMarco,R.A., Pham,T., Frantz,G.
            and Fong,S.
  TITLE     Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2
            interacts with T, NK, and dendritic cells through JAM 3
  JOURNAL   J Immunol 168 (4), 1618-1626 (2002)
   PUBMED   11823489
  REMARK    GeneRIF: role as an adhesive ligand for interacting with a variety
            of immune cell types
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Arrate,M.P., Rodriguez,J.M., Tran,T.M., Brock,T.A. and
            Cunningham,S.A.
  TITLE     Cloning of human junctional adhesion molecule 3 (JAM3) and its
            identification as the JAM2 counter-receptor
  JOURNAL   J Biol Chem 276 (49), 45826-45832 (2001)
   PUBMED   11590146
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Cunningham,S.A., Arrate,M.P., Rodriguez,J.M., Bjercke,R.J.,
            Vanderslice,P., Morris,A.P. and Brock,T.A.
  TITLE     A novel protein with homology to the junctional adhesion molecule.
            Characterization of leukocyte interactions
  JOURNAL   J Biol Chem 275 (44), 34750-34756 (2000)
   PUBMED   10945976
  REMARK    GeneRIF: Cloning and discovery as adhesion receptor for T cells
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Palmeri,D., van Zante,A., Huang,C.C., Hemmerich,S. and Rosen,S.D.
  TITLE     Vascular endothelial junction-associated molecule, a novel member
            of the immunoglobulin superfamily, is localized to intercellular
            boundaries of endothelial cells
  JOURNAL   J Biol Chem 275 (25), 19139-19145 (2000)
   PUBMED   10779521
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000223.1, BM921497.1,
            AY077698.1, AK294769.1, CX870550.1, AK056079.1, BG540412.1 and
            AI742752.1.
            
            Summary: This gene belongs to the immunoglobulin superfamily, and
            the junctional adhesion molecule (JAM) family. The protein encoded
            by this gene is a type I membrane protein that is localized at the
            tight junctions of both epithelial and endothelial cells. It acts
            as an adhesive ligand for interacting with a variety of immune cell
            types, and may play a role in lymphocyte homing to secondary
            lymphoid organs. Alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.160828.1,
                                           SRR1803614.52505.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000480456.6/ ENSP00000420419.1
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..298
                     /product="junctional adhesion molecule B isoform 1
                     precursor"
                     /note="vascular endothelial junction-associated molecule;
                     junctional adhesion molecule B; JAM-IT/VE-JAM; JAM-2"
                     /calculated_mol_wt=29885
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3340
     mat_peptide     29..298
                     /product="Junctional adhesion molecule B.
                     /id=PRO_0000015069"
                     /note="propagated from UniProtKB/Swiss-Prot (P57087.1)"
                     /calculated_mol_wt=29885
     Region          30..131
                     /region_name="IgV_1_JAM1-like"
                     /note="First Ig-like domain of Junctional adhesion
                     molecule-1 (JAM1)and similar domains; a member of the
                     V-set of IgSF domains; cd20946"
                     /db_xref="CDD:409538"
     Region          30..52
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409538"
     Region          30..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409538"
     Region          37..41
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409538"
     Region          44..53
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409538"
     Region          53..59
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409538"
     Region          59..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409538"
     Region          60..67
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409538"
     Region          70..83
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409538"
     Region          70..75
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409538"
     Region          77..79
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409538"
     Region          84..112
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409538"
     Region          86..90
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409538"
     Region          92..96
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409538"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P57087.1)"
     Region          105..113
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409538"
     Region          113..121
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409538"
     Region          121..130
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409538"
     Region          122..131
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409538"
     Region          137..232
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          151..155
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          165..169
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            187
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57087.1)"
     Region          197..201
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          211..216
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          225..228
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57087.1)"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57087.1)"
     CDS             1..298
                     /gene="JAM2"
                     /gene_synonym="C21orf43; CD322; IBGC8; JAM-B; JAMB;
                     PRO245; VE-JAM; VEJAM"
                     /coded_by="NM_021219.4:565..1461"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS42911.1"
                     /db_xref="GeneID:58494"
                     /db_xref="HGNC:HGNC:14686"
                     /db_xref="MIM:606870"
ORIGIN      
        1 marrsrhrll llllrylvva lgyhkaygfs apkdqqvvta veyqeailac ktpkktvssr
       61 lewkklgrsv sfvyyqqtlq gdfknraemi dfniriknvt rsdagkyrce vsapseqgqn
      121 leedtvtlev lvapavpsce vpssalsgtv velrcqdkeg npapeytwfk dgirllenpr
      181 lgsqstnssy tmntktgtlq fntvskldtg eyscearnsv gyrrcpgkrm qvddlnisgi
      241 iaavvvvalv isvcglgvcy aqrkgyfske tsfqksnsss kattmsendf khtksfii
//
LOCUS       NP_061174                639 aa            linear   PRI 27-APR-2025
DEFINITION  CTTNBP2 N-terminal-like protein [Homo sapiens].
ACCESSION   NP_061174
VERSION     NP_061174.1
DBSOURCE    REFSEQ: accession NM_018704.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 639)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 639)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   6  (residues 1 to 639)
  AUTHORS   Goudreault,M., D'Ambrosio,L.M., Kean,M.J., Mullin,M.J.,
            Larsen,B.G., Sanchez,A., Chaudhry,S., Chen,G.I., Sicheri,F.,
            Nesvizhskii,A.I., Aebersold,R., Raught,B. and Gingras,A.C.
  TITLE     A PP2A phosphatase high density interaction network identifies a
            novel striatin-interacting phosphatase and kinase complex linked to
            the cerebral cavernous malformation 3 (CCM3) protein
  JOURNAL   Mol Cell Proteomics 8 (1), 157-171 (2009)
   PUBMED   18782753
REFERENCE   7  (residues 1 to 639)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 639)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   9  (residues 1 to 639)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 639)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA238082.1, AL598321.1, DB236769.1, AL354760.11 and BE645464.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA834426.1, SRR1660803.227069.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000271277.11/ ENSP00000271277.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..639
                     /product="CTTNBP2 N-terminal-like protein"
                     /calculated_mol_wt=70027
     Region          5..188
                     /region_name="CortBP2"
                     /note="Cortactin-binding protein-2; pfam09727"
                     /db_xref="CDD:462860"
     Region          <100..>283
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Region          387..430
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Region          463..490
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Region          511..609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            590
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P2B4.2)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P2B4.2)"
     CDS             1..639
                     /gene="CTTNBP2NL"
                     /coded_by="NM_018704.3:193..2112"
                     /db_xref="CCDS:CCDS845.1"
                     /db_xref="GeneID:55917"
                     /db_xref="HGNC:HGNC:25330"
                     /db_xref="MIM:615100"
ORIGIN      
        1 mnleklskpe lltlfsileg eleardlvie alkaqhrdtf ieerygkyni sdplmalqrd
       61 fetlkekndg ekqpvctnpl silkvvmkqc knmqermlsq laaaesrhrk vildleeerq
      121 rhaqdtaegd dvtymleker erltqqlefe ksqvkkfeke qkklssqlee ersrhkqlss
      181 mlvleckkat nkaaeegqka gelslkleke ksrvskleee laaerkrglq teaqvekqls
      241 efdiereqlr aklnreenrt ktlkeemesl kkivkdleas hqhsspneql kkpvtvskgt
      301 ateplmlmsv fcqtesfpae rthgsniakm tntglpgpat paysyaktng hcdpeiqttr
      361 eltagnnven qvppreksva laqekpveng gcpvgietpv pmpsplsssg sslspsstas
      421 ssltsspcss pvltkrllgs sasspgyqss yqvginqrfh aarhkfqsqa dqdqqasglq
      481 sppsrdlspt lidnsaakql arntvtqvls rftsqqgpik pvspnsspfg tdyrnlanta
      541 nprgdtshsp tpgkvsspls plspgikspt ipraergnpp pippkkpglt pspsattplt
      601 kthsqaaslt taedlasscs sntvvangkd velllptss
//
LOCUS       NP_001393                462 aa            linear   PRI 27-APR-2025
DEFINITION  elongation factor 1-alpha 1 [Homo sapiens].
ACCESSION   NP_001393
VERSION     NP_001393.1
DBSOURCE    REFSEQ: accession NM_001402.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Wang,Y., Luan,T., Wang,L., Feng,D., Dong,Y., Li,S., Yang,H.,
            Chen,Y., Fei,Y., Lin,L., Pan,J., Zhong,Z. and Zhao,W.
  TITLE     N-Acetylcysteine Inhibits Coxsackievirus B3 Replication by
            Downregulating Eukaryotic Translation Elongation Factor 1 Alpha 1
  JOURNAL   Viruses 16 (9), 1503 (2024)
   PUBMED   39339978
  REMARK    GeneRIF: N-Acetylcysteine Inhibits Coxsackievirus B3 Replication by
            Downregulating Eukaryotic Translation Elongation Factor 1 Alpha 1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhao,J., Huo,Q., Zhang,J., Sun,K., Guo,J., Cheng,F., Hu,X. and
            Xu,Q.
  TITLE     UCHL3 promotes hepatocellular carcinoma progression by stabilizing
            EEF1A1 through deubiquitination
  JOURNAL   Biol Direct 19 (1), 53 (2024)
   PUBMED   38965582
  REMARK    GeneRIF: UCHL3 promotes hepatocellular carcinoma progression by
            stabilizing EEF1A1 through deubiquitination.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Wilson,R.B., Kozlov,A.M., Hatam Tehrani,H., Twumasi-Ankrah,J.S.,
            Chen,Y.J., Borrelli,M.J., Sawyez,C.G., Maini,S., Shepherd,T.G.,
            Cumming,R.C., Betts,D.H. and Borradaile,N.M.
  TITLE     Elongation factor 1A1 regulates metabolic substrate preference in
            mammalian cells
  JOURNAL   J Biol Chem 300 (3), 105684 (2024)
   PUBMED   38272231
  REMARK    GeneRIF: Elongation factor 1A1 regulates metabolic substrate
            preference in mammalian cells.
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Minoia,M., Quintana-Cordero,J., Jetzinger,K., Kotan,I.E.,
            Turnbull,K.J., Ciccarelli,M., Masser,A.E., Liebers,D., Gouarin,E.,
            Czech,M., Hauryliuk,V., Bukau,B., Kramer,G. and Andreasson,C.
  TITLE     Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A
            biogenesis
  JOURNAL   Nat Commun 15 (1), 1382 (2024)
   PUBMED   38360885
  REMARK    GeneRIF: Chp1 is a dedicated chaperone at the ribosome that
            safeguards eEF1A biogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Negrutskii,B.S., Porubleva,L.V., Malinowska,A., Novosylna,O.V.,
            Dadlez,M. and Knudsen,C.R.
  TITLE     Understanding functions of eEF1 translation elongation factors
            beyond translation. A proteomic approach
  JOURNAL   Adv Protein Chem Struct Biol 138, 67-99 (2024)
   PUBMED   38220433
  REMARK    GeneRIF: Understanding functions of eEF1 translation elongation
            factors beyond translation. A proteomic approach.
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Madsen,H.O., Poulsen,K., Dahl,O., Clark,B.F. and Hjorth,J.P.
  TITLE     Retropseudogenes constitute the major part of the human elongation
            factor 1 alpha gene family
  JOURNAL   Nucleic Acids Res 18 (6), 1513-1516 (1990)
   PUBMED   2183196
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Bec,G., Kerjan,P., Zha,X.D. and Waller,J.P.
  TITLE     Valyl-tRNA synthetase from rabbit liver. I. Purification as a
            heterotypic complex in association with elongation factor 1
  JOURNAL   J Biol Chem 264 (35), 21131-21137 (1989)
   PUBMED   2556394
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Whiteheart,S.W., Shenbagamurthi,P., Chen,L., Cotter,R.J. and
            Hart,G.W.
  TITLE     Murine elongation factor 1 alpha (EF-1 alpha) is
            posttranslationally modified by novel amide-linked
            ethanolamine-phosphoglycerol moieties. Addition of
            ethanolamine-phosphoglycerol to specific glutamic acid residues on
            EF-1 alpha
  JOURNAL   J Biol Chem 264 (24), 14334-14341 (1989)
   PUBMED   2569467
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Uetsuki,T., Naito,A., Nagata,S. and Kaziro,Y.
  TITLE     Isolation and characterization of the human chromosomal gene for
            polypeptide chain elongation factor-1 alpha
  JOURNAL   J Biol Chem 264 (10), 5791-5798 (1989)
   PUBMED   2564392
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Motorin,Yu.A., Wolfson,A.D., Orlovsky,A.F. and Gladilin,K.L.
  TITLE     Mammalian valyl-tRNA synthetase forms a complex with the first
            elongation factor
  JOURNAL   FEBS Lett 238 (2), 262-264 (1988)
   PUBMED   3169261
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC066893.1, AJ420488.1 and AL603910.6.
            
            Summary: This gene encodes an isoform of the alpha subunit of the
            elongation factor-1 complex, which is responsible for the enzymatic
            delivery of aminoacyl tRNAs to the ribosome. This isoform (alpha 1)
            is expressed in brain, placenta, lung, liver, kidney, and pancreas,
            and the other isoform (alpha 2) is expressed in brain, heart and
            skeletal muscle. This isoform is identified as an autoantigen in
            66% of patients with Felty syndrome. This gene has been found to
            have multiple copies on many chromosomes, some of which, if not
            all, represent different pseudogenes. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.28133.1,
                                           SRR1660807.43653.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309268.11/ ENSP00000339053.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..462
                     /product="elongation factor 1-alpha 1"
                     /note="cervical cancer suppressor 3; eukaryotic
                     translation elongation factor 1 alpha 1-like 14; leukocyte
                     receptor cluster (LRC) member 7; CTCL tumor antigen;
                     prostate tumor-inducing protein 1; EF1a-like protein;
                     glucocorticoid receptor AF-1 specific elongation factor;
                     elongation factor 1 alpha subunit; elongation factor Tu;
                     EF-1-alpha-1; eukaryotic elongation factor 1 A-1;
                     leukocyte receptor cluster member 7; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=50010
     Region          1..460
                     /region_name="PTZ00141"
                     /note="elongation factor 1- alpha; Provisional"
                     /db_xref="CDD:185474"
     Site            2
                     /site_type="methylation"
                     /note="N,N,N-trimethylglycine.
                     /evidence=ECO:0000269|PubMed:26545399,
                     ECO:0000269|PubMed:30143613; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Region          14..21
                     /region_name="G1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P68104.1)"
     Site            14..21
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206670"
     Site            order(15,17,21..22,25,28..29,76..77,95..96,119..120,169,
                     173)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206670"
     Site            order(17,19..22,153..154,156,194..196)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206670"
     Site            order(21,64,67..68,70,72,74..76,78,89,91,93..95,97,100)
                     /site_type="other"
                     /note="EF1Balpha binding site [polypeptide binding]"
                     /db_xref="CDD:206670"
     Site            36
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate, by EEF1AKMT4.
                     /evidence=ECO:0000269|PubMed:28520920;
                     N6,N6-dimethyllysine, alternate, by EEF1AKMT4.
                     /evidence=ECO:0000269|PubMed:28520920; N6-methyllysine,
                     alternate, by EEF1AKMT4.
                     /evidence=ECO:0000269|PubMed:28520920; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Site            55
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0000269|PubMed:30143613,
                     ECO:0000269|PubMed:30612740, ECO:0000269|Ref.7; propagated
                     from UniProtKB/Swiss-Prot (P68104.1)"
     Site            66..76
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206670"
     Region          70..74
                     /region_name="G2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P68104.1)"
     Site            72
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206670"
     Site            79
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by EEF1AKMT1.
                     /evidence=ECO:0000269|PubMed:26545399; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Region          91..94
                     /region_name="G3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P68104.1)"
     Site            91..94
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206670"
     Site            93..111
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206670"
     Region          153..156
                     /region_name="G4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P68104.1)"
     Site            153..156
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206670"
     Site            165
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate, by EEF1AKMT3.
                     /evidence=ECO:0000269|PubMed:28108655;
                     N6,N6-dimethyllysine, alternate, by EEF1AKMT3.
                     /evidence=ECO:0000269|PubMed:28108655, ECO:0000269|Ref.7;
                     N6-methyllysine, alternate, by EEF1AKMT3.
                     /evidence=ECO:0000269|PubMed:28108655; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Site            165
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P10126; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Site            172
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10126; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Region          194..196
                     /region_name="G5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P68104.1)"
     Site            194..196
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206670"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10126; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TGFBR1.
                     /evidence=ECO:0000269|PubMed:20832312; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="5-glutamyl glycerylphosphorylethanolamine.
                     /evidence=ECO:0000269|PubMed:2569467; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Site            318
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by EEF1AKMT2.
                     /evidence=ECO:0000269|PubMed:25144183; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Site            374
                     /site_type="phosphorylation"
                     /note="5-glutamyl glycerylphosphorylethanolamine.
                     /evidence=ECO:0000269|PubMed:2569467; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Site            392
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P10126; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PASK.
                     /evidence=ECO:0000269|PubMed:17595531; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     Site            439
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10126; propagated from
                     UniProtKB/Swiss-Prot (P68104.1)"
     CDS             1..462
                     /gene="EEF1A1"
                     /gene_synonym="CCS-3; CCS3; EE1A1; EEF-1; EEF1A; eEF1A-1;
                     EF-Tu; EF1A; EF1A1; EF1alpha1; GRAF-1EF; LENG7; PTI1"
                     /coded_by="NM_001402.6:64..1452"
                     /db_xref="CCDS:CCDS4980.1"
                     /db_xref="GeneID:1915"
                     /db_xref="HGNC:HGNC:3189"
                     /db_xref="MIM:130590"
ORIGIN      
        1 mgkekthini vvighvdsgk stttghliyk cggidkrtie kfekeaaemg kgsfkyawvl
       61 dklkaererg itidislwkf etskyyvtii dapghrdfik nmitgtsqad cavlivaagv
      121 gefeagiskn gqtrehalla ytlgvkqliv gvnkmdstep pysqkryeei vkevstyikk
      181 igynpdtvaf vpisgwngdn mlepsanmpw fkgwkvtrkd gnasgttlle aldcilpptr
      241 ptdkplrlpl qdvykiggig tvpvgrvetg vlkpgmvvtf apvnvttevk svemhheals
      301 ealpgdnvgf nvknvsvkdv rrgnvagdsk ndppmeaagf taqviilnhp gqisagyapv
      361 ldchtahiac kfaelkekid rrsgkkledg pkflksgdaa ivdmvpgkpm cvesfsdypp
      421 lgrfavrdmr qtvavgvika vdkkaagagk vtksaqkaqk ak
//
LOCUS       NP_848824                668 aa            linear   ROD 27-APR-2025
DEFINITION  RING finger protein 214 isoform 1 [Mus musculus].
ACCESSION   NP_848824
VERSION     NP_848824.1
DBSOURCE    REFSEQ: accession NM_178709.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Faghihi,M.A., Modarresi,F., Khalil,A.M., Wood,D.E., Sahagan,B.G.,
            Morgan,T.E., Finch,C.E., St Laurent,G. 3rd, Kenny,P.J. and
            Wahlestedt,C.
  TITLE     Expression of a noncoding RNA is elevated in Alzheimer's disease
            and drives rapid feed-forward regulation of beta-secretase
  JOURNAL   Nat Med 14 (7), 723-730 (2008)
   PUBMED   18587408
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Carninci,P., Waki,K., Shiraki,T., Konno,H., Shibata,K., Itoh,M.,
            Aizawa,K., Arakawa,T., Ishii,Y., Sasaki,D., Bono,H., Kondo,S.,
            Sugahara,Y., Saito,R., Osato,N., Fukuda,S., Sato,K., Watahiki,A.,
            Hirozane-Kishikawa,T., Nakamura,M., Shibata,Y., Yasunishi,A.,
            Kikuchi,N., Yoshiki,A., Kusakabe,M., Gustincich,S., Beisel,K.,
            Pavan,W., Aidinis,V., Nakagawara,A., Held,W.A., Iwata,H., Kono,T.,
            Nakauchi,H., Lyons,P., Wells,C., Hume,D.A., Fagiolini,M.,
            Hensch,T.K., Brinkmeier,M., Camper,S., Hirota,J., Mombaerts,P.,
            Muramatsu,M., Okazaki,Y., Kawai,J. and Hayashizaki,Y.
  TITLE     Targeting a complex transcriptome: the construction of the mouse
            full-length cDNA encyclopedia
  JOURNAL   Genome Res 13 (6B), 1273-1289 (2003)
   PUBMED   12819125
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC126804.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK051527.1, BC094247.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 25.26 cM"
     Protein         1..668
                     /product="RING finger protein 214 isoform 1"
                     /calculated_mol_wt=73494
     Region          1..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q8ND24; propagated from
                     UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8ND24; propagated from
                     UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8ND24; propagated from
                     UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8ND24; propagated from
                     UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Region          103..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Region          486..552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8ND24; propagated from
                     UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8ND24; propagated from
                     UniProtKB/Swiss-Prot (Q8BFU3.1)"
     Region          621..665
                     /region_name="RING-H2_RNF214"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 214 (RNF214) and similar proteins; cd16477"
                     /db_xref="CDD:438140"
     CDS             1..668
                     /gene="Rnf214"
                     /gene_synonym="D130054N24Rik"
                     /coded_by="NM_178709.5:568..2574"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS23136.1"
                     /db_xref="GeneID:235315"
                     /db_xref="MGI:MGI:2444451"
ORIGIN      
        1 maasevaglg agtpspsess alcasksdes lpdglspkds aqkqknlspp svssqmitke
       61 snrnahlehp eqnpgssvgd tsaaheevvg enlvatalcl sgngsqsdlk dltnpageeg
      121 dtslreslhp vtrslkagch skqlasgncs eekcpaasvl kegsrdagld llpvvppang
      181 vegvrvdqdd dqdssslkls qniavqtdfk tadsevntdq dieknldkmm tertllkery
      241 qevldkqrqv esqlqvqlkq lqqrreeemk nhqeilkaiq dvtikreetk kkiekekkef
      301 lqkeqdlkae ieklcekgrr evwemeldrl knqdgeinrn imeeterawk aeilslesrk
      361 ellvlkleea ekeaelhlty lkstpptlet vrskqewetr lngvrimkkn vrdqfnshiq
      421 lvrngaklss lpqiptptlp pppseadfml qvfqpspslt prmpfsigqv tmpmvmpsad
      481 prslsfpiln palsqssqps pplpgshgrn spglgslvsp hgphmppaas ippppglggi
      541 kassetprpq pvdklekile klltrfpqcn kaqmtnilqq iktarttmag ltmeeliqlv
      601 aarlaeherv asstqapptc klclmcqklv qpselhpmac thalhkecik fwaqtntndt
      661 cpfcptlk
//
LOCUS       NP_037477                380 aa            linear   PRI 27-APR-2025
DEFINITION  probable G-protein coupled receptor 132 isoform 1 [Homo sapiens].
ACCESSION   NP_037477
VERSION     NP_037477.1
DBSOURCE    REFSEQ: accession NM_013345.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Yi,C., He,J., Huang,D., Zhao,Y., Zhang,C., Ye,X., Huang,Y.,
            Nussinov,R., Zheng,J., Liu,M. and Lu,W.
  TITLE     Activation of orphan receptor GPR132 induces cell differentiation
            in acute myeloid leukemia
  JOURNAL   Cell Death Dis 13 (11), 1004 (2022)
   PUBMED   36437247
  REMARK    GeneRIF: Activation of orphan receptor GPR132 induces cell
            differentiation in acute myeloid leukemia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Li,Q., Feng,C., Li,L., Xu,G., Gu,H., Li,S., Li,D., Liu,M., Han,S.
            and Zheng,B.
  TITLE     Lipid Receptor G2A-Mediated Signal Pathway Plays a Critical Role in
            Inflammatory Response by Promoting Classical Macrophage Activation
  JOURNAL   J Immunol 206 (10), 2338-2352 (2021)
   PUBMED   33941654
  REMARK    GeneRIF: Lipid Receptor G2A-Mediated Signal Pathway Plays a
            Critical Role in Inflammatory Response by Promoting Classical
            Macrophage Activation.
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Klatt,W., Wallner,S., Brochhausen,C., Stolwijk,J.A. and Schreml,S.
  TITLE     Expression profiles of proton-sensing G-protein coupled receptors
            in common skin tumors
  JOURNAL   Sci Rep 10 (1), 15327 (2020)
   PUBMED   32948783
  REMARK    GeneRIF: Expression profiles of proton-sensing G-protein coupled
            receptors in common skin tumors.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Lahvic,J.L., Ammerman,M., Li,P., Blair,M.C., Stillman,E.R.,
            Fast,E.M., Robertson,A.L., Christodoulou,C., Perlin,J.R., Yang,S.,
            Chiang,N., Norris,P.C., Daily,M.L., Redfield,S.E., Chan,I.T.,
            Chatrizeh,M., Chase,M.E., Weis,O., Zhou,Y., Serhan,C.N. and
            Zon,L.I.
  TITLE     Specific oxylipins enhance vertebrate hematopoiesis via the
            receptor GPR132
  JOURNAL   Proc Natl Acad Sci U S A 115 (37), 9252-9257 (2018)
   PUBMED   30139917
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Ogawa,A., Obinata,H., Hattori,T., Kishi,M., Tatei,K., Ishikawa,O.
            and Izumi,T.
  TITLE     Identification and analysis of two splice variants of human G2A
            generated by alternative splicing
  JOURNAL   J Pharmacol Exp Ther 332 (2), 469-478 (2010)
   PUBMED   19855098
  REMARK    GeneRIF: we found an additional novel G2A variant (G2A-b) that is
            the major transcript with functional response to ligand stimulation
            as well as G2A-a, and succeeded in discriminating proton-sensing
            and oxidized fatty acid-sensing activities of G2A.
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Obinata,H., Hattori,T., Nakane,S., Tatei,K. and Izumi,T.
  TITLE     Identification of 9-hydroxyoctadecadienoic acid and other oxidized
            free fatty acids as ligands of the G protein-coupled receptor G2A
  JOURNAL   J Biol Chem 280 (49), 40676-40683 (2005)
   PUBMED   16236715
  REMARK    GeneRIF: results indicate that G protein-coupled receptor G2A is a
            receptor for 9-hydroxyoctadecadienoic acid (9-HODE) and other
            oxidized free fatty acids and is activated by oxidized free fatty
            acids
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Murakami,N., Yokomizo,T., Okuno,T. and Shimizu,T.
  TITLE     G2A is a proton-sensing G-protein-coupled receptor antagonized by
            lysophosphatidylcholine
  JOURNAL   J Biol Chem 279 (41), 42484-42491 (2004)
   PUBMED   15280385
  REMARK    GeneRIF: G2A is a proton-sensing G-protein-coupled receptor
            antagonized by lysophosphatidylcholine
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Rikitake,Y., Hirata,K., Yamashita,T., Iwai,K., Kobayashi,S.,
            Itoh,H., Ozaki,M., Ejiri,J., Shiomi,M., Inoue,N., Kawashima,S. and
            Yokoyama,M.
  TITLE     Expression of G2A, a receptor for lysophosphatidylcholine, by
            macrophages in murine, rabbit, and human atherosclerotic plaques
  JOURNAL   Arterioscler Thromb Vasc Biol 22 (12), 2049-2053 (2002)
   PUBMED   12482833
  REMARK    GeneRIF: In atherosclerotic plaques of human coronary arterial
            specimens, G2A is expressed by macrophages within the lipid-rich
            plaques, whereas no immunoreactivity of G2A is observed in fibrous
            plaques where macrophages do not exist.
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Le,L.Q., Kabarowski,J.H., Wong,S., Nguyen,K., Gambhir,S.S. and
            Witte,O.N.
  TITLE     Positron emission tomography imaging analysis of G2A as a negative
            modifier of lymphoid leukemogenesis initiated by the BCR-ABL
            oncogene
  JOURNAL   Cancer Cell 1 (4), 381-391 (2002)
   PUBMED   12086852
  REMARK    GeneRIF: G2A is a negative modifier of lymphoid leukemogenesis
            initiated by the BCR-ABL oncogene
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Weng,Z., Fluckiger,A.C., Nisitani,S., Wahl,M.I., Le,L.Q.,
            Hunter,C.A., Fernal,A.A., Le Beau,M.M. and Witte,O.N.
  TITLE     A DNA damage and stress inducible G protein-coupled receptor blocks
            cells in G2/M
  JOURNAL   Proc Natl Acad Sci U S A 95 (21), 12334-12339 (1998)
   PUBMED   9770487
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB465599.1 and AA714520.1.
            
            Summary: This gene encodes a member of the guanine
            nucleotide-binding protein (G protein)-coupled receptor (GPCR)
            superfamily. The receptors are seven-pass transmembrane proteins
            that respond to extracellular cues and activate intracellular
            signal transduction pathways. This protein was reported to be a
            receptor for lysophosphatidylcholine action, but PubMedID: 15653487
            retracts this finding and instead suggests this protein to be an
            effector of lysophosphatidylcholine action. This protein may have
            proton-sensing activity and may be a receptor for oxidized free
            fatty acids. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB465599.1, AF083955.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329797.8/ ENSP00000328818.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..380
                     /product="probable G-protein coupled receptor 132 isoform
                     1"
                     /note="G2 accumulation protein; probable G-protein coupled
                     receptor 132"
                     /calculated_mol_wt=42368
     Site            35
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UNW8.1)"
     Region          43..319
                     /region_name="7tmA_GPR132_G2A"
                     /note="proton-sensing G protein-coupled receptor 132,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15364"
                     /db_xref="CDD:320486"
     Region          43..70
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320486"
     Site            46..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNW8.1)"
     Region          77..102
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320486"
     Site            80..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNW8.1)"
     Site            order(98,101..102,115..120,122..123,126,171,173..177,196,
                     199..201,203..205,207..208,255,258..259,261..262,265,
                     286..287,289..291,294,297..298)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320486"
     Region          115..145
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320486"
     Site            117..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNW8.1)"
     Region          157..179
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320486"
     Site            159..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNW8.1)"
     Region          196..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320486"
     Site            198..220
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNW8.1)"
     Region          235..265
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320486"
     Site            247..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNW8.1)"
     Region          287..312
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320486"
     Site            289..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNW8.1)"
     CDS             1..380
                     /gene="GPR132"
                     /gene_synonym="G2A"
                     /coded_by="NM_013345.4:913..2055"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9997.1"
                     /db_xref="GeneID:29933"
                     /db_xref="HGNC:HGNC:17482"
                     /db_xref="MIM:606167"
ORIGIN      
        1 mcpmllkngy ngnatpvttt apwaslglsa ktcnnvsfee srivlvvvys avctlgvpan
       61 cltawlallq vlqgnvlavy llclalcell ytgtlplwvi yirnqhrwtl gllackvtay
      121 iffcniyvsi lflcciscdr fvavvyales rgrrrrrtai lisacifilv givhypvfqt
      181 edketcfdml qmdsriagyy yarftvgfai plsiiaftnh rifrsikqsm glsaaqkakv
      241 khsaiavvvi flvcfapyhl vllvkaaafs yyrgdrnamc gleerlytas vvflclstvn
      301 gvadpiiyvl atdhsrqevs rihkgwkews mktdvtrlth srdteelqsp valadhytfs
      361 rpvhppgspc pakrlieesc
//
LOCUS       NP_006399                175 aa            linear   PRI 27-APR-2025
DEFINITION  anterior gradient protein 2 homolog precursor [Homo sapiens].
ACCESSION   NP_006399
VERSION     NP_006399.1
DBSOURCE    REFSEQ: accession NM_006408.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Martisova,A., Faktor,J., Sosolikova,T., Klemesova,I., Kolarova,T.,
            Holcakova,J. and Hrstka,R.
  TITLE     Characterization of the AGR2-NPM3 axis uncovers the AGR2
            involvement in PD-L1 regulation in colorectal cancer
  JOURNAL   Sci Rep 14 (1), 21926 (2024)
   PUBMED   39300184
  REMARK    GeneRIF: Characterization of the AGR2-NPM3 axis uncovers the AGR2
            involvement in PD-L1 regulation in colorectal cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Wambach,M., Montani,M., Runz,J., Stephan,C., Jung,K., Moch,H.,
            Eberli,D., Bernhardt,M., Hommerding,O., Kreft,T., Cronauer,M.V.,
            Kremer,A., Mayr,T., Hauser,S. and Kristiansen,G.
  TITLE     Clinical implications of AGR2 in primary prostate cancer: Results
            from a large-scale study
  JOURNAL   APMIS 132 (4), 256-266 (2024)
   PUBMED   38288749
  REMARK    GeneRIF: Clinical implications of AGR2 in primary prostate cancer:
            Results from a large-scale study.
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Kosykh,A.V., Tereshina,M.B. and Gurskaya,N.G.
  TITLE     Potential Role of AGR2 for Mammalian Skin Wound Healing
  JOURNAL   Int J Mol Sci 24 (9), 7895 (2023)
   PUBMED   37175601
  REMARK    GeneRIF: Potential Role of AGR2 for Mammalian Skin Wound Healing.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Yan,T., Wang,H., Ma,X., Cao,J., Tong,Y., Guo,L. and Lu,R.
  TITLE     Clinical value of serum and tissue AGR2 for diagnosis and prognosis
            in epithelial ovarian cancer
  JOURNAL   Biomark Med 17 (6), 325-336 (2023)
   PUBMED   37284743
  REMARK    GeneRIF: Clinical value of serum and tissue AGR2 for diagnosis and
            prognosis in epithelial ovarian cancer.
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Adilay,H.U., Evran,S., Katar,S., Ozdemir,A., Kayhan,A.,
            Avcikurt,A.S., Gunaldi,O., Guclu,B. and Tanriverdi,O.
  TITLE     AGR2 Gene Expression in Glioblastoma: A Novel Molecular Potential
            Target for Diagnosis and Treatment
  JOURNAL   Turk Neurosurg 33 (2), 265-271 (2023)
   PUBMED   36622190
  REMARK    GeneRIF: AGR2 Gene Expression in Glioblastoma: A Novel Molecular
            Potential Target for Diagnosis and Treatment.
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Fletcher,G.C., Patel,S., Tyson,K., Adam,P.J., Schenker,M.,
            Loader,J.A., Daviet,L., Legrain,P., Parekh,R., Harris,A.L. and
            Terrett,J.A.
  TITLE     hAG-2 and hAG-3, human homologues of genes involved in
            differentiation, are associated with oestrogen receptor-positive
            breast tumours and interact with metastasis gene C4.4a and
            dystroglycan
  JOURNAL   Br J Cancer 88 (4), 579-585 (2003)
   PUBMED   12592373
  REMARK    GeneRIF: hAG-2 and hAG-3, human homologues of genes involved in
            differentiation, are associated with oestrogen receptor-positive
            breast tumours and interact with metastasis gene C4.4a and
            dystroglycan.
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Petek,E., Windpassinger,C., Egger,H., Kroisel,P.M. and Wagner,K.
  TITLE     Localization of the human anterior gradient-2 gene (AGR2) to
            chromosome band 7p21.3 by radiation hybrid mapping and
            fluorescencein situ hybridisation
  JOURNAL   Cytogenet Cell Genet 89 (3-4), 141-142 (2000)
   PUBMED   10965104
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Thompson,D.A. and Weigel,R.J.
  TITLE     hAG-2, the human homologue of the Xenopus laevis cement gland gene
            XAG-2, is coexpressed with estrogen receptor in breast cancer cell
            lines
  JOURNAL   Biochem Biophys Res Commun 251 (1), 111-116 (1998)
   PUBMED   9790916
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF088867.1 and AC073333.5.
            
            Summary: This gene encodes a member of the disulfide isomerase
            (PDI) family of endoplasmic reticulum (ER) proteins that catalyze
            protein folding and thiol-disulfide interchange reactions. The
            encoded protein has an N-terminal ER-signal sequence, a
            catalytically active thioredoxin domain, and a C-terminal
            ER-retention sequence. This protein plays a role in cell migration,
            cellular transformation and metastasis and is as a p53 inhibitor.
            As an ER-localized molecular chaperone, it plays a role in the
            folding, trafficking, and assembly of cysteine-rich transmembrane
            receptors and the cysteine-rich intestinal gylcoprotein mucin. This
            gene has been implicated in inflammatory bowel disease and cancer
            progression. [provided by RefSeq, Mar 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF115926.1, SRR5189667.313185.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2154405
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000419304.7/ ENSP00000391490.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.1"
     Protein         1..175
                     /product="anterior gradient protein 2 homolog precursor"
                     /note="protein disulfide isomerase family A, member 17;
                     anterior gradient protein 2 homolog; secreted cement gland
                     homolog; secreted cement gland protein XAG-2 homolog;
                     anterior gradient homolog 2; epididymis secretory protein
                     Li 116"
                     /calculated_mol_wt=17818
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2180
     mat_peptide     21..175
                     /product="Anterior gradient protein 2 homolog.
                     /id=PRO_0000001037"
                     /note="propagated from UniProtKB/Swiss-Prot (O95994.1)"
                     /calculated_mol_wt=17818
     Region          21..40
                     /region_name="Required to promote cell adhesion.
                     /evidence=ECO:0000269|PubMed:23274113"
                     /note="propagated from UniProtKB/Swiss-Prot (O95994.1)"
     Region          45..54
                     /region_name="Homodimer stabilization, interchain.
                     /evidence=ECO:0000269|PubMed:23274113,
                     ECO:0007744|PDB:2LNS"
                     /note="propagated from UniProtKB/Swiss-Prot (O95994.1)"
     Region          47..175
                     /region_name="AGR"
                     /note="Anterior Gradient (AGR) family; members of this
                     family are similar to secreted proteins encoded by the
                     cement gland-specific genes XAG-1 and XAG-2, expressed in
                     the anterior region of dorsal ectoderm of Xenopus. They
                     are implicated in the formation of...; cd02960"
                     /db_xref="CDD:239258"
     Region          60..67
                     /region_name="Homodimer stabilization, interchain.
                     /evidence=ECO:0000269|PubMed:23274113,
                     ECO:0007744|PDB:2LNS"
                     /note="propagated from UniProtKB/Swiss-Prot (O95994.1)"
     Site            order(81,84)
                     /site_type="active"
                     /note="putative catalytic residues [active]"
                     /db_xref="CDD:239258"
     CDS             1..175
                     /gene="AGR2"
                     /gene_synonym="AG-2; AG2; GOB-4; HAG-2; HEL-S-116; HPC8;
                     PDIA17; RIFTD; XAG-2"
                     /coded_by="NM_006408.4:73..600"
                     /db_xref="CCDS:CCDS5364.1"
                     /db_xref="GeneID:10551"
                     /db_xref="HGNC:HGNC:328"
                     /db_xref="MIM:606358"
ORIGIN      
        1 mekipvsafl llvalsytla rdttvkpgak kdtkdsrpkl pqtlsrgwgd qliwtqtyee
       61 alyksktsnk plmiihhlde cphsqalkkv faenkeiqkl aeqfvllnlv yettdkhlsp
      121 dgqyvprimf vdpsltvrad itgrysnrly ayepadtall ldnmkkalkl lktel
//
LOCUS       NP_001356024             357 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform b [Homo
            sapiens].
ACCESSION   NP_001356024
VERSION     NP_001356024.1
DBSOURCE    REFSEQ: accession NM_001369095.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 357)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 357)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.64255.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..357
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform b"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=41097
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..356
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..357
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369095.1:124..1197"
                     /note="isoform b is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS31219.1"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilkl fenfyfgslk lnsihisqrf tvdsfgnyas cgqidfs
//
LOCUS       NP_001128145             509 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear factor 1 A-type isoform 1 [Homo sapiens].
ACCESSION   NP_001128145
VERSION     NP_001128145.1
DBSOURCE    REFSEQ: accession NM_001134673.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Tauziede-Espariat,A., Lew-Derivry,L., Abbou,S., Metais,A.,
            Pierron,G., Reynaud,S., Masliah-Planchon,J., Mariet,C., Hasty,L.,
            Dangouloff-Ros,V., Boddaert,N., Csanyi,M., Aline-Fardin,A.,
            Lamaison,C., Chretien,F., Beccaria,K., Puget,S. and Varlet,P.
  TITLE     CNS erythroblastic sarcoma: a potential emerging pediatric tumor
            type characterized by NFIA::RUNX1T1/3 fusions
  JOURNAL   Acta Neuropathol Commun 12 (1), 12 (2024)
   PUBMED   38243303
  REMARK    GeneRIF: CNS erythroblastic sarcoma: a potential emerging pediatric
            tumor type characterized by NFIA::RUNX1T1/3 fusions.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Kong,S., Chen,T.X., Jia,X.L., Cheng,X.L., Zeng,M.L., Liang,J.Y.,
            He,X.H., Yin,J., Han,S., Liu,W.H., Fan,Y.T., Zhou,T., Liu,Y.M. and
            Peng,B.W.
  TITLE     Cell-specific NFIA upregulation promotes epileptogenesis by
            TRPV4-mediated astrocyte reactivity
  JOURNAL   J Neuroinflammation 20 (1), 247 (2023)
   PUBMED   37880726
  REMARK    GeneRIF: Cell-specific NFIA upregulation promotes epileptogenesis
            by TRPV4-mediated astrocyte reactivity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Lu,R., Tang,P., Zhang,D., Lin,S., Li,H., Feng,X., Sun,M. and
            Zhang,H.
  TITLE     SOX9/NFIA promotes human ovarian cancer metastasis through the
            Wnt/beta-catenin signaling pathway
  JOURNAL   Pathol Res Pract 248, 154602 (2023)
   PUBMED   37315400
  REMARK    GeneRIF: SOX9/NFIA promotes human ovarian cancer metastasis through
            the Wnt/beta-catenin signaling pathway.
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Santo,M., Rigoldi,L., Falcone,C., Tuccillo,M., Calabrese,M.,
            Martinez-Cerdeno,V. and Mallamaci,A.
  TITLE     Spatial control of astrogenesis progression by cortical
            arealization genes
  JOURNAL   Cereb Cortex 33 (6), 3107-3123 (2023)
   PUBMED   35818636
  REMARK    GeneRIF: Spatial control of astrogenesis progression by cortical
            arealization genes.
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Malczewska-Lenczowska,J., Orysiak,J., Majorczyk,E., Sitkowski,D.,
            Starczewski,M. and Zmijewski,P.
  TITLE     HIF-1alpha and NFIA-AS2 Polymorphisms as Potential Determinants of
            Total Hemoglobin Mass in Endurance Athletes
  JOURNAL   J Strength Cond Res 36 (6), 1596-1604 (2022)
   PUBMED   35622109
  REMARK    GeneRIF: HIF-1alpha and NFIA-AS2 Polymorphisms as Potential
            Determinants of Total Hemoglobin Mass in Endurance Athletes.
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Xu,H., Uno,J.K., Inouye,M., Collins,J.F. and Ghishan,F.K.
  TITLE     NF1 transcriptional factor(s) is required for basal promoter
            activation of the human intestinal NaPi-IIb cotransporter gene
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 288 (2), G175-G181 (2005)
   PUBMED   15458926
  REMARK    GeneRIF: Role in the expression mechanism of hNaPi-IIb gene
            transcription.
REFERENCE   7  (residues 1 to 509)
  AUTHORS   das Neves,L., Duchala,C.S., Tolentino-Silva,F., Haxhiu,M.A.,
            Colmenares,C., Macklin,W.B., Campbell,C.E., Butz,K.G. and
            Gronostajski,R.M.
  TITLE     Disruption of the murine nuclear factor I-A gene (Nfia) results in
            perinatal lethality, hydrocephalus, and agenesis of the corpus
            callosum
  JOURNAL   Proc Natl Acad Sci U S A 96 (21), 11946-11951 (1999)
   PUBMED   10518556
  REMARK    GeneRIF: Disruption of the Nfia gene in the mouse causes perinatal
            lethality, agenesis of the corpus callosum and hydrocephalus.
            Erratum:[Proc Natl Acad Sci U S A 2001 Mar 27;98(7):4276. Godinho F
            [corrected to Tolentino-Silva F]]
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Leahy,P., Crawford,D.R., Grossman,G., Gronostajski,R.M. and
            Hanson,R.W.
  TITLE     CREB binding protein coordinates the function of multiple
            transcription factors including nuclear factor I to regulate
            phosphoenolpyruvate carboxykinase (GTP) gene transcription
  JOURNAL   J Biol Chem 274 (13), 8813-8822 (1999)
   PUBMED   10085123
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Qian,F., Kruse,U., Lichter,P. and Sippel,A.E.
  TITLE     Chromosomal localization of the four genes (NFIA, B, C, and X) for
            the human transcription factor nuclear factor I by FISH
  JOURNAL   Genomics 28 (1), 66-73 (1995)
   PUBMED   7590749
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Senaratne,T.N. and Quintero-Rivera,F.
  TITLE     NFIA-Related Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31194316
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB037860.1, AL096888.30 and
            AA974652.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the NF1 (nuclear factor 1)
            family of transcription factors. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.200273.1,
                                           SRR1660809.95677.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000403491.8/ ENSP00000384523.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..509
                     /product="nuclear factor 1 A-type isoform 1"
                     /note="nuclear factor 1 A-type; TGGCA-binding protein;
                     CCAAT-box-binding transcription factor"
                     /calculated_mol_wt=55813
     Region          9..46
                     /region_name="NfI_DNAbd_pre-N"
                     /note="Nuclear factor I protein pre-N-terminus; pfam10524"
                     /db_xref="CDD:463134"
     Region          68..172
                     /region_name="MH1"
                     /note="MH1 domain; pfam03165"
                     /db_xref="CDD:460833"
     Region          189..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12857.2)"
     Region          214..501
                     /region_name="CTF_NFI"
                     /note="CTF/NF-I family transcription modulation region;
                     pfam00859"
                     /db_xref="CDD:459967"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q12857.2)"
     Region          259..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12857.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q12857.2)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q12857.2)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12857.2)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12857.2)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09414; propagated from
                     UniProtKB/Swiss-Prot (Q12857.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q12857.2)"
     Region          352..371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12857.2)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q12857.2)"
     Site            389
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q02780; propagated from
                     UniProtKB/Swiss-Prot (Q12857.2)"
     Region          394..402
                     /region_name="9aaTAD.
                     /evidence=ECO:0000269|PubMed:31375868"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12857.2)"
     Region          435..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12857.2)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12857.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12857.2)"
     CDS             1..509
                     /gene="NFIA"
                     /gene_synonym="BRMUTD; C1DELp32p31; CTF; DEL1P32P31;
                     NF-I/A; NF1-A; NFI-A; NFI-L"
                     /coded_by="NM_001134673.4:232..1761"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44156.1"
                     /db_xref="GeneID:4774"
                     /db_xref="HGNC:HGNC:7784"
                     /db_xref="MIM:600727"
ORIGIN      
        1 mysplcltqd efhpfieall phvrafaytw fnlqarkrky fkkhekrmsk eeeravkdel
       61 lsekpevkqk wasrllaklr kdirpeyred fvltvtgkkp pccvlsnpdq kgkmrridcl
      121 rqadkvwrld lvmvilfkgi plestdgerl vkspqcsnpg lcvqphhigv svkeldlyla
      181 yfvhaadssq sespsqpsda dikdqpengh lgfqdsfvts gvfsvtelvr vsqtpiaagt
      241 gpnfslsdle sssyysmspg amrrslpsts stsstkrlks vedemdspge epfytgqgrs
      301 pgsgsqssgw hevepgmpsp ttlkkseksg fsspspsqts slgtaftqhh rpvitgpras
      361 phatpstlhf ptspiiqqpg pyfshpairy hpqetlkefv qlvcpdagqq agqvgflnpn
      421 gssqgkvhnp flptpmlppp ppppmarpvp lpvpdtkppt tsteggaasp tsptystpst
      481 spanrfvsvg prdpsfvnip qqtqswylg
//
LOCUS       NP_570138                235 aa            linear   PRI 27-APR-2025
DEFINITION  regulator of G-protein signaling 18 [Homo sapiens].
ACCESSION   NP_570138
VERSION     NP_570138.1
DBSOURCE    REFSEQ: accession NM_130782.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Meng,Y., Qiu,S.Q., Wang,Q. and Zuo,J.L.
  TITLE     Regulator of G protein signalling 18 promotes osteocyte
            proliferation by activating the extracellular signal-regulated
            kinase signalling pathway
  JOURNAL   Int J Mol Med 53 (3) (2024)
   PUBMED   38214344
  REMARK    GeneRIF: Regulator of G protein signalling 18 promotes osteocyte
            proliferation by activating the extracellular signal-regulated
            kinase signalling pathway.
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Kim,J.O., Lee,K.O., Kim,H.W., Park,H.S., Kim,J., Sung,J.H., Oh,D.,
            Kim,O.J. and Kim,N.K.
  TITLE     Association between KCNQ2, TCF4 and RGS18 polymorphisms and silent
            brain infarction based on whole-exome sequencing
  JOURNAL   Mol Med Rep 21 (4), 1973-1983 (2020)
   PUBMED   32319632
  REMARK    GeneRIF: Association between KCNQ2, TCF4 and RGS18 polymorphisms
            and silent brain infarction based on wholeexome sequencing.
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Kim,K., Lee,J. and Ghil,S.
  TITLE     The regulators of G protein signaling RGS16 and RGS18 inhibit
            protease-activated receptor 2/Gi/o signaling through distinct
            interactions with Galpha in live cells
  JOURNAL   FEBS Lett 592 (18), 3126-3138 (2018)
   PUBMED   30117167
  REMARK    GeneRIF: Data show that bothregulator of G protein signaling (RGS16
            and RGS18) inhibit protease-activated receptor 2 (PAR2)/G-protein,
            Gi-Go subunits (Galphai/o) -mediated signaling.
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Gegenbauer,K., Elia,G., Blanco-Fernandez,A. and Smolenski,A.
  TITLE     Regulator of G-protein signaling 18 integrates activating and
            inhibitory signaling in platelets
  JOURNAL   Blood 119 (16), 3799-3807 (2012)
   PUBMED   22234696
  REMARK    GeneRIF: These findings indicate cross-talk between platelet
            activation and inhibition pathways at the level of RGS18 and Gq.
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Ma,P., Cierniewska,A., Signarvic,R., Cieslak,M., Kong,H.,
            Sinnamon,A.J., Neubig,R.R., Newman,D.K., Stalker,T.J. and
            Brass,L.F.
  TITLE     A newly identified complex of spinophilin and the tyrosine
            phosphatase, SHP-1, modulates platelet activation by regulating G
            protein-dependent signaling
  JOURNAL   Blood 119 (8), 1935-1945 (2012)
   PUBMED   22210881
  REMARK    GeneRIF: Data show that that SPL/RGS/SHP1 complexes are present in
            resting platelets where constitutive phosphorylation of SPL(Y398)
            creates an atypical binding site for SHP-1.
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Gagnon,A.W., Murray,D.L. and Leadley,R.J.
  TITLE     Cloning and characterization of a novel regulator of G protein
            signalling in human platelets
  JOURNAL   Cell Signal 14 (7), 595-606 (2002)
   PUBMED   11955952
  REMARK    GeneRIF: molecular cloning and characterization of RGS18 as a
            regulator of G protein signalling in human platelets
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Sierra,D.A., Gilbert,D.J., Householder,D., Grishin,N.V., Yu,K.,
            Ukidwe,P., Barker,S.A., He,W., Wensel,T.G., Otero,G., Brown,G.,
            Copeland,N.G., Jenkins,N.A. and Wilkie,T.M.
  TITLE     Evolution of the regulators of G-protein signaling multigene family
            in mouse and human
  JOURNAL   Genomics 79 (2), 177-185 (2002)
   PUBMED   11829488
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Yowe,D., Weich,N., Prabhudas,M., Poisson,L., Errada,P.,
            Kapeller,R., Yu,K., Faron,L., Shen,M., Cleary,J., Wilkie,T.M.,
            Gutierrez-Ramos,C. and Hodge,M.R.
  TITLE     RGS18 is a myeloerythroid lineage-specific regulator of
            G-protein-signalling molecule highly expressed in megakaryocytes
  JOURNAL   Biochem J 359 (Pt 1), 109-118 (2001)
   PUBMED   11563974
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Nagata,Y., Oda,M., Nakata,H., Shozaki,Y., Kozasa,T. and Todokoro,K.
  TITLE     A novel regulator of G-protein signaling bearing GAP activity for
            Galphai and Galphaq in megakaryocytes
  JOURNAL   Blood 97 (10), 3051-3060 (2001)
   PUBMED   11342430
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Park,I.K., Klug,C.A., Li,K., Jerabek,L., Li,L., Nanamori,M.,
            Neubig,R.R., Hood,L., Weissman,I.L. and Clarke,M.F.
  TITLE     Molecular cloning and characterization of a novel regulator of
            G-protein signaling from mouse hematopoietic stem cells
  JOURNAL   J Biol Chem 276 (2), 915-923 (2001)
   PUBMED   11042171
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AV715708.1, BC020632.1,
            AF268036.1 and AF076642.1.
            
            Summary: This gene encodes a member of the regulator of G-protein
            signaling family. This protein is contains a conserved, 120 amino
            acid motif called the RGS domain. The protein attenuates the
            signaling activity of G-proteins by binding to activated, GTP-bound
            G alpha subunits and acting as a GTPase activating protein (GAP),
            increasing the rate of conversion of the GTP to GDP. This
            hydrolysis allows the G alpha subunits to bind G beta/gamma subunit
            heterodimers, forming inactive G-protein heterotrimers, thereby
            terminating the signal. Alternate transcriptional splice variants
            of this gene have been observed but have not been thoroughly
            characterized. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF076642.1, AF268036.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367460.4/ ENSP00000356430.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q31.2"
     Protein         1..235
                     /product="regulator of G-protein signaling 18"
                     /note="regulator of G-protein signalling 18; regulator of
                     G-protein signalling 13"
                     /calculated_mol_wt=27451
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14645010; propagated from
                     UniProtKB/Swiss-Prot (Q9NS28.1)"
     Region          87..200
                     /region_name="RGS_RGS18"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS18 protein; cd08712"
                     /db_xref="CDD:188667"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99PG4; propagated from
                     UniProtKB/Swiss-Prot (Q9NS28.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99PG4; propagated from
                     UniProtKB/Swiss-Prot (Q9NS28.1)"
     CDS             1..235
                     /gene="RGS18"
                     /gene_synonym="RGS13"
                     /coded_by="NM_130782.3:177..884"
                     /db_xref="CCDS:CCDS1374.1"
                     /db_xref="GeneID:64407"
                     /db_xref="HGNC:HGNC:14261"
                     /db_xref="MIM:607192"
ORIGIN      
        1 mettllffsq inmceskekt ffklihgsgk eetskeakir akekrnrlsl lvqkpefhed
       61 trssrsghla ketrvspeea vkwgesfdkl lshrdgleaf trflktefse eniefwiace
      121 dfkkskgpqq ihlkakaiye kfiqtdapke vnldfhtkev itnsitqptl hsfdaaqsrv
      181 yqlmeqdsyt rflksdiyld lmegrpqrpt nlrrrsrsft cnefqdvqsd vaiwl
//
LOCUS       NP_056985                352 aa            linear   PRI 27-APR-2025
DEFINITION  NAD(P)H pyrophosphatase NUDT13, mitochondrial isoform a [Homo
            sapiens].
ACCESSION   NP_056985
VERSION     NP_056985.3
DBSOURCE    REFSEQ: accession NM_015901.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB035851.1, AL521667.3, BC046173.2 and AL050114.1.
            
            On Jul 26, 2004 this sequence version replaced NP_056985.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.170839.1,
                                           SRR5189667.202424.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357321.9/ ENSP00000349874.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..352
                     /product="NAD(P)H pyrophosphatase NUDT13, mitochondrial
                     isoform a"
                     /EC_number="3.6.1.22"
                     /note="nucleoside diphosphate-linked moiety X motif 13;
                     nudix motif 13; nudix (nucleoside diphosphate linked
                     moiety X)-type motif 13; NAD(P)H pyrophosphatase NUDT13,
                     mitochondrial"
                     /calculated_mol_wt=37176
     transit_peptide 1..20
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q86X67.3)"
                     /calculated_mol_wt=2530
     mat_peptide     21..352
                     /product="NAD(P)H pyrophosphatase NUDT13, mitochondrial.
                     /evidence=ECO:0000255. /id=PRO_0000057111"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X67.3)"
                     /calculated_mol_wt=37176
     Region          36..343
                     /region_name="NPY1"
                     /note="NADH pyrophosphatase NudC, Nudix superfamily
                     [Nucleotide transport and metabolism]; COG2816"
                     /db_xref="CDD:442065"
     Region          216..240
                     /region_name="Nudix box.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00794"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X67.3)"
     CDS             1..352
                     /gene="NUDT13"
                     /coded_by="NM_015901.6:123..1181"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31220.1"
                     /db_xref="GeneID:25961"
                     /db_xref="HGNC:HGNC:18827"
                     /db_xref="MIM:609233"
ORIGIN      
        1 mslycgiacr rkffwcyrll styvtktryl felkedddac kkaqqtgafy lfhslapllq
       61 tsahqylapr hsllelerll gkfgqdaqri edsvligcse qqeawfaldl gldssfsisa
      121 slhkpemete lkgsfielrk alfqlnarda sllstaqall rwhdahqfcs rsgqptkknv
      181 agskrvcpsn niiyypqmap vaitlvsdgt rcllarqssf pkgmysalag fcdigesvee
      241 tirrevaeev gleveslqyy asqhwpfpsg slmiachatv kpgqteiqvn lreletaawf
      301 shdevatalk rkgpytqqqn gtfpfwlppk laishqlike wvekqtcssl pa
//
LOCUS       NP_003206                631 aa            linear   PRI 27-APR-2025
DEFINITION  tyrosine-protein kinase Tec [Homo sapiens].
ACCESSION   NP_003206
VERSION     NP_003206.2
DBSOURCE    REFSEQ: accession NM_003215.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Yeung,S.F., Zhou,Y., Zou,W., Chan,W.L. and Ching,Y.P.
  TITLE     TEC kinase stabilizes PLK4 to promote liver cancer metastasis
  JOURNAL   Cancer Lett 524, 70-81 (2022)
   PUBMED   34637843
  REMARK    GeneRIF: TEC kinase stabilizes PLK4 to promote liver cancer
            metastasis.
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Afifiyan,N., Tillman,B., French,B.A., Sweeny,O., Masouminia,M.,
            Samadzadeh,S. and French,S.W.
  TITLE     The role of Tec kinase signaling pathways in the development of
            Mallory Denk Bodies in balloon cells in alcoholic hepatitis
  JOURNAL   Exp Mol Pathol 103 (2), 191-199 (2017)
   PUBMED   28935395
  REMARK    GeneRIF: High TEC expression is associated with the development of
            Mallory Denk Bodies in balloon cells in alcoholic hepatitis.
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Vanova,T., Konecna,Z., Zbonakova,Z., La Venuta,G., Zoufalova,K.,
            Jelinkova,S., Varecha,M., Rotrekl,V., Krejci,P., Nickel,W.,
            Dvorak,P. and Kunova Bosakova,M.
  TITLE     Tyrosine Kinase Expressed in Hepatocellular Carcinoma, TEC,
            Controls Pluripotency and Early Cell Fate Decisions of Human
            Pluripotent Stem Cells via Regulation of Fibroblast Growth Factor-2
            Secretion
  JOURNAL   Stem Cells 35 (9), 2050-2059 (2017)
   PUBMED   28631381
  REMARK    GeneRIF: TEC is yet another regulator of FGF2-mediated Human
            pluripotent stem cells pluripotency and differentiation.
REFERENCE   4  (residues 1 to 631)
  AUTHORS   La Venuta,G., Wegehingel,S., Sehr,P., Muller,H.M., Dimou,E.,
            Steringer,J.P., Grotwinkel,M., Hentze,N., Mayer,M.P., Will,D.W.,
            Uhrig,U., Lewis,J.D. and Nickel,W.
  TITLE     Small Molecule Inhibitors Targeting Tec Kinase Block Unconventional
            Secretion of Fibroblast Growth Factor 2
  JOURNAL   J Biol Chem 291 (34), 17787-17803 (2016)
   PUBMED   27382052
  REMARK    GeneRIF: using RNA interference, the identified compounds
            corroborate the role of Tec kinase in unconventional secretion of
            FGF2.
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Kleino,I., Jarviluoma,A., Hepojoki,J., Huovila,A.P. and Saksela,K.
  TITLE     Preferred SH3 domain partners of ADAM metalloproteases include
            shared and ADAM-specific SH3 interactions
  JOURNAL   PLoS One 10 (3), e0121301 (2015)
   PUBMED   25825872
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Mano,H., Yamashita,Y., Miyazato,A., Miura,Y. and Ozawa,K.
  TITLE     Tec protein-tyrosine kinase is an effector molecule of Lyn
            protein-tyrosine kinase
  JOURNAL   FASEB J 10 (5), 637-642 (1996)
   PUBMED   8621063
REFERENCE   7  (residues 1 to 631)
  AUTHORS   Machide,M., Mano,H. and Todokoro,K.
  TITLE     Interleukin 3 and erythropoietin induce association of Vav with Tec
            kinase through Tec homology domain
  JOURNAL   Oncogene 11 (4), 619-625 (1995)
   PUBMED   7651724
REFERENCE   8  (residues 1 to 631)
  AUTHORS   Tang,B., Mano,H., Yi,T. and Ihle,J.N.
  TITLE     Tec kinase associates with c-kit and is tyrosine phosphorylated and
            activated following stem cell factor binding
  JOURNAL   Mol Cell Biol 14 (12), 8432-8437 (1994)
   PUBMED   7526158
REFERENCE   9  (residues 1 to 631)
  AUTHORS   Sato,K., Mano,H., Ariyama,T., Inazawa,J., Yazaki,Y. and Hirai,H.
  TITLE     Molecular cloning and analysis of the human Tec protein-tyrosine
            kinase
  JOURNAL   Leukemia 8 (10), 1663-1672 (1994)
   PUBMED   7934162
REFERENCE   10 (residues 1 to 631)
  AUTHORS   Mano,H., Ishikawa,F., Nishida,J., Hirai,H. and Takaku,F.
  TITLE     A novel protein-tyrosine kinase, tec, is preferentially expressed
            in liver
  JOURNAL   Oncogene 5 (12), 1781-1786 (1990)
   PUBMED   2284097
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098873.3, BC101713.1 and
            AC079118.5.
            
            On Mar 14, 2007 this sequence version replaced NP_003206.1.
            
            Summary: The protein encoded by this gene belongs to the Tec family
            of non-receptor protein-tyrosine kinases containing a pleckstrin
            homology domain. Tec family kinases are involved in the
            intracellular signaling mechanisms of cytokine receptors,
            lymphocyte surface antigens, heterotrimeric G-protein coupled
            receptors, and integrin molecules. They are also key players in the
            regulation of the immune functions. Tec kinase is an integral
            component of T cell signaling and has a distinct role in T cell
            activation. This gene may be associated with myelodysplastic
            syndrome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143487.1, SRR14038197.1982769.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381501.8/ ENSP00000370912.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p12-p11"
     Protein         1..631
                     /product="tyrosine-protein kinase Tec"
                     /EC_number="2.7.10.2"
                     /calculated_mol_wt=73450
     Region          7..148
                     /region_name="PH_Btk"
                     /note="Bruton's tyrosine kinase pleckstrin homology (PH)
                     domain; cd01238"
                     /db_xref="CDD:269944"
     Site            order(9..10,28..30,43,94)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:269944"
     Site            order(13,15..16,18..19,25,29,51)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269944"
     Site            order(121,132..133,143)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:269944"
     Region          157..178
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42680.2)"
     Region          182..237
                     /region_name="SH3_Tec"
                     /note="Src Homology 3 domain of Tec (Tyrosine kinase
                     expressed in hepatocellular carcinoma); cd11905"
                     /db_xref="CDD:212838"
     Site            order(188,190,193,197,215..216,230,232..233)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212838"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12573241,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42680.2)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42680.2)"
     Region          240..346
                     /region_name="SH2_Tec_Itk"
                     /note="Src homology 2 (SH2) domain found in Tec protein,
                     IL2-inducible T-cell kinase (Itk); cd10396"
                     /db_xref="CDD:198259"
     Site            order(254,273)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198259"
     Site            order(329,337..338)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198259"
     Region          365..624
                     /region_name="PTKc_Tec_Rlk"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Tyrosine kinase expressed in hepatocellular carcinoma and
                     Resting lymphocyte kinase; cd05114"
                     /db_xref="CDD:270685"
     Site            order(376..377,384,396,398,417,440,442..446,448,489,493,
                     496,506..507,510,524..528,537,571)
                     /site_type="active"
                     /db_xref="CDD:270685"
     Site            order(376..377,384,396,398,417,440,442..446,448,493,496,
                     506..507,510)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270685"
     Site            order(489,493,524..528,537,571)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270685"
     Site            506..530
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270685"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis, LYN and JAK2.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P42680.2)"
     CDS             1..631
                     /gene="TEC"
                     /gene_synonym="PSCTK4"
                     /coded_by="NM_003215.3:133..2028"
                     /db_xref="CCDS:CCDS3481.1"
                     /db_xref="GeneID:7006"
                     /db_xref="HGNC:HGNC:11719"
                     /db_xref="MIM:600583"
ORIGIN      
        1 mnfntileei likrsqqkkk tsplnykerl fvltksmlty yegraekkyr kgfidvskik
       61 cveivknddg vipcqnkypf qvvhdantly ifapspqsrd lwvkklkeei knnnnimiky
      121 hpkfwtdgsy qccrqtekla pgcekynlfe ssirkalppa petkkrrppp pipleeedns
      181 eeivvamydf qaaeghdlrl ergqeylile kndvhwwrar dkygnegyip snyvtgkksn
      241 nldqyewycr nmnrskaeql lrsedkeggf mvrdssqpgl ytvslytkfg gegssgfrhy
      301 hiketttspk kyylaekhaf gsipeiieyh khnaaglvtr lrypvsvkgk napttagfsy
      361 ekweinpsel tfmrelgsgl fgvvrlgkwr aqykvaikai regamceedf ieeakvmmkl
      421 thpklvqlyg vctqqkpiyi vtefmergcl lnflrqrqgh fsrdvllsmc qdvcegmeyl
      481 ernsfihrdl aarnclvsea gvvkvsdfgm aryvlddqyt sssgakfpvk wcppevfnys
      541 rfssksdvws fgvlmwevft egrmpfekyt nyevvtmvtr ghrlyqpkla snyvyevmlr
      601 cwqekpegrp sfedllrtid elveceetfg r
//
LOCUS       NP_037469                194 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim22 [Homo
            sapiens].
ACCESSION   NP_037469
VERSION     NP_037469.2
DBSOURCE    REFSEQ: accession NM_013337.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Guo,L., Liu,J.J., Long,S.Y., Wang,P.Y., Li,S., Wang,J.L., Wei,X.F.,
            Li,J., Lei,L., Huang,A.L. and Hu,J.L.
  TITLE     TIM22 and TIM29 inhibit HBV replication by up-regulating SRSF1
            expression
  JOURNAL   J Med Virol 96 (2), e29439 (2024)
   PUBMED   38294104
  REMARK    GeneRIF: TIM22 and TIM29 inhibit HBV replication by up-regulating
            SRSF1 expression.
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Jackson,T.D., Hock,D.H., Fujihara,K.M., Palmer,C.S., Frazier,A.E.,
            Low,Y.C., Kang,Y., Ang,C.S., Clemons,N.J., Thorburn,D.R.,
            Stroud,D.A. and Stojanovski,D.
  TITLE     The TIM22 complex mediates the import of sideroflexins and is
            required for efficient mitochondrial one-carbon metabolism
  JOURNAL   Mol Biol Cell 32 (6), 475-491 (2021)
   PUBMED   33476211
  REMARK    GeneRIF: The TIM22 complex mediates the import of sideroflexins and
            is required for efficient mitochondrial one-carbon metabolism.
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Qi,L., Wang,Q., Guan,Z., Wu,Y., Shen,C., Hong,S., Cao,J., Zhang,X.,
            Yan,C. and Yin,P.
  TITLE     Cryo-EM structure of the human mitochondrial translocase TIM22
            complex
  JOURNAL   Cell Res 31 (3), 369-372 (2021)
   PUBMED   32901109
  REMARK    GeneRIF: Cryo-EM structure of the human mitochondrial translocase
            TIM22 complex.
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Valpadashi,A., Callegari,S., Linden,A., Neumann,P., Ficner,R.,
            Urlaub,H., Deckers,M. and Rehling,P.
  TITLE     Defining the architecture of the human TIM22 complex by chemical
            crosslinking
  JOURNAL   FEBS Lett 595 (2), 157-168 (2021)
   PUBMED   33125709
  REMARK    GeneRIF: Defining the architecture of the human TIM22 complex by
            chemical crosslinking.
REFERENCE   6  (residues 1 to 194)
  AUTHORS   Callegari,S., Richter,F., Chojnacka,K., Jans,D.C., Lorenzi,I.,
            Pacheu-Grau,D., Jakobs,S., Lenz,C., Urlaub,H., Dudek,J.,
            Chacinska,A. and Rehling,P.
  TITLE     TIM29 is a subunit of the human carrier translocase required for
            protein transport
  JOURNAL   FEBS Lett 590 (23), 4147-4158 (2016)
   PUBMED   27718247
REFERENCE   7  (residues 1 to 194)
  AUTHORS   Kang,Y., Baker,M.J., Liem,M., Louber,J., McKenzie,M., Atukorala,I.,
            Ang,C.S., Keerthikumar,S., Mathivanan,S. and Stojanovski,D.
  TITLE     Tim29 is a novel subunit of the human TIM22 translocase and is
            involved in complex assembly and stability
  JOURNAL   Elife 5, e17463 (2016)
   PUBMED   27554484
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 194)
  AUTHORS   Muhlenbein,N., Hofmann,S., Rothbauer,U. and Bauer,M.F.
  TITLE     Organization and function of the small Tim complexes acting along
            the import pathway of metabolite carriers into mammalian
            mitochondria
  JOURNAL   J Biol Chem 279 (14), 13540-13546 (2004)
   PUBMED   14726512
  REMARK    GeneRIF: in contrast to yeast, only a small fraction of
            Tim9-Tim10a-Tim10b complex is in a stable association with Tim22.
REFERENCE   9  (residues 1 to 194)
  AUTHORS   Kovermann,P., Truscott,K.N., Guiard,B., Rehling,P., Sepuri,N.B.,
            Muller,H., Jensen,R.E., Wagner,R. and Pfanner,N.
  TITLE     Tim22, the essential core of the mitochondrial protein insertion
            complex, forms a voltage-activated and signal-gated channel
  JOURNAL   Mol Cell 9 (2), 363-373 (2002)
   PUBMED   11864609
REFERENCE   10 (residues 1 to 194)
  AUTHORS   Bauer,M.F., Rothbauer,U., Muhlenbein,N., Smith,R.J., Gerbitz,K.,
            Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     The mitochondrial TIM22 preprotein translocase is highly conserved
            throughout the eukaryotic kingdom
  JOURNAL   FEBS Lett 464 (1-2), 41-47 (1999)
   PUBMED   10611480
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC002324.2, AI522232.1 and
            AC015884.15.
            
            On Dec 15, 2004 this sequence version replaced NP_037469.1.
            
            Summary: Multipass transmembrane proteins are brought into
            mitochondria and inserted into the mitochondrial inner membrane by
            way of the TIM22 complex. This complex has six subunits and is a
            twin-pore translocase. The protein encoded by this gene is a
            subunit of TIM22 and represents the voltage-activated and
            signal-gated channel. [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.162958.1,
                                           SRR1660807.72389.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000327158.5/
                                                  ENSP00000320236.2
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..194
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim22"
                     /note="testis-expressed sequence 4; translocase of inner
                     mitochondrial membrane 22 homolog; testis-expressed
                     protein 4"
                     /calculated_mol_wt=19900
     Region          69..184
                     /region_name="Tim17"
                     /note="Tim17/Tim22/Tim23/Pmp24 family; pfam02466"
                     /db_xref="CDD:460567"
     Site            74..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y584.2)"
     Site            123..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y584.2)"
     Site            170..190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y584.2)"
     CDS             1..194
                     /gene="TIMM22"
                     /gene_synonym="COXPD43; TEX4; TIM22"
                     /coded_by="NM_013337.4:15..599"
                     /db_xref="CCDS:CCDS32521.1"
                     /db_xref="GeneID:29928"
                     /db_xref="HGNC:HGNC:17317"
                     /db_xref="MIM:607251"
ORIGIN      
        1 maaaapnagg sapetagsae aplqyslllq ylvgdkrqpr llepgslggi pspakseeqk
       61 miekamesca fkaalacvgg fvlggafgvf tagidtnvgf dpkdpyrtpt akevlkdmgq
      121 rgmsyaknfa ivgamfscte cliesyrgts dwknsvisgc itggaigfra glkagaigcg
      181 gfaafsaaid yylr
//
LOCUS       NP_076950                737 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX50 [Homo sapiens].
ACCESSION   NP_076950
VERSION     NP_076950.1
DBSOURCE    REFSEQ: accession NM_024045.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Pallett,M.A., Lu,Y. and Smith,G.L.
  TITLE     DDX50 Is a Viral Restriction Factor That Enhances IRF3 Activation
  JOURNAL   Viruses 14 (2), 316 (2022)
   PUBMED   35215908
  REMARK    GeneRIF: DDX50 Is a Viral Restriction Factor That Enhances IRF3
            Activation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Han,P., Ye,W., Lv,X., Ma,H., Weng,D., Dong,Y., Cheng,L., Chen,H.,
            Zhang,L., Xu,Z., Lei,Y. and Zhang,F.
  TITLE     DDX50 inhibits the replication of dengue virus 2 by upregulating
            IFN-beta production
  JOURNAL   Arch Virol 162 (6), 1487-1494 (2017)
   PUBMED   28181036
  REMARK    GeneRIF: Results provide evidence that DDX50 negatively regulates
            DENV-2 replication during the early stages of infection by inducing
            IFN-beta production.
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 737)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 737)
  AUTHORS   Ohnishi,S., Paakkonen,K., Koshiba,S., Tochio,N., Sato,M.,
            Kobayashi,N., Harada,T., Watanabe,S., Muto,Y., Guntert,P.,
            Tanaka,A., Kigawa,T. and Yokoyama,S.
  TITLE     Solution structure of the GUCT domain from human RNA helicase II/Gu
            beta reveals the RRM fold, but implausible RNA interactions
  JOURNAL   Proteins 74 (1), 133-144 (2009)
   PUBMED   18615715
  REMARK    GeneRIF: Solution structure of the GUCT domain from human RNA
            helicase II/Gu beta reveals the RRM fold, but implausible RNA
            interactions.
REFERENCE   7  (residues 1 to 737)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   8  (residues 1 to 737)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 737)
  AUTHORS   Valdez,B.C., Yang,H., Hong,E. and Sequitin,A.M.
  TITLE     Genomic structure of newly identified paralogue of RNA helicase
            II/Gu: detection of pseudogenes and multiple alternatively spliced
            mRNAs
  JOURNAL   Gene 284 (1-2), 53-61 (2002)
   PUBMED   11891046
REFERENCE   10 (residues 1 to 737)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359844.15.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this DEAD box
            protein family are believed to be involved in embryogenesis,
            spermatogenesis, and cellular growth and division. This gene
            encodes a DEAD box enzyme that may be involved in ribosomal RNA
            synthesis or processing. This gene and DDX21, also called
            RH-II/GuA, have similar genomic structures and are in tandem
            orientation on chromosome 10, suggesting that the two genes arose
            by gene duplication in evolution. This gene has pseudogenes on
            chromosomes 2, 3 and 4. Alternative splicing of this gene generates
            multiple transcript variants, but the full length nature of all the
            other variants but one has not been defined. [provided by RefSeq,
            Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000272.1, SRR1803611.100878.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373585.8/ ENSP00000362687.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..737
                     /product="ATP-dependent RNA helicase DDX50"
                     /EC_number="3.6.4.13"
                     /note="RNA helicase II/Gu beta; nucleolar protein GU2;
                     DEAD box protein 50; malignant cell derived RNA helicase;
                     gu-beta; DEAD (Asp-Glu-Ala-Asp) box polypeptide 50;
                     DEAD-box helicase 50"
                     /calculated_mol_wt=82434
     Region          1..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ39.1)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ39.1)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BQ39.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ39.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ39.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ39.1)"
     Region          137..165
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ39.1)"
     Region          139..526
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ39.1)"
     Region          290..293
                     /region_name="DEVD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ39.1)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ39.1)"
     Region          568..659
                     /region_name="GUCT_RHII_Gualpha_beta"
                     /note="RNA-binding GUCT domain found in vertebrate RNA
                     helicase II/Gualpha (RH-II/Gualpha), RNA helicase
                     II/Gubeta (RH-II/Gubeta) and similar proteins; cd12936"
                     /db_xref="CDD:240593"
     Region          668..737
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ39.1)"
     CDS             1..737
                     /gene="DDX50"
                     /gene_synonym="GU2; GUB; mcdrh; RH-II/GuB"
                     /coded_by="NM_024045.2:71..2284"
                     /db_xref="CCDS:CCDS7283.1"
                     /db_xref="GeneID:79009"
                     /db_xref="HGNC:HGNC:17906"
                     /db_xref="MIM:610373"
ORIGIN      
        1 mpgkllwgdi meleaplees esqkkerqks drrksrhhyd sdeksetren gvtddldapk
       61 akkskmkekl ngdteegfnr lsdefskshk srrkdlpngd ideyekkskr vssldtsthk
      121 ssdnkleetl treqkegafs nfpiseetik llkgrgvtyl fpiqvktfgp vyegkdliaq
      181 artgtgktfs faiplierlq rnqetikksr spkvlvlapt relanqvakd fkditrklsv
      241 acfyggtsyq sqinhirngi dilvgtpgri kdhlqsgrld lsklrhvvld evdqmldlgf
      301 aeqvediihe syktdsednp qtllfsatcp qwvykvakky mksryeqvdl vgkmtqkaat
      361 tvehlaiqch wsqrpavigd vlqvysgseg raiifcetkk nvtemamnph ikqnaqclhg
      421 diaqsqreit lkgfregsfk vlvatnvaar gldipevdlv iqssppqdve syihrsgrtg
      481 ragrtgicic fyqprergql ryveqkagit fkrvgvpstm dlvksksmda irslasvsya
      541 avdffrpsaq rlieekgavd alaaalahis gassfeprsl itsdkgfvtm tlesleeiqd
      601 vscawkelnr klssnavsqi trmcllkgnm gvcfdvptte serlqaewhd sdwilsvpak
      661 lpeieeyydg ntssnsrqrs gwssgrsgrs grsggrsggr sgrqsrqgsr sgsrqdgrrr
      721 sgnrnrsrsg ghkrsfd
//
LOCUS       NP_660304                116 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit TIM14
            isoform 1 [Homo sapiens].
ACCESSION   NP_660304
VERSION     NP_660304.1
DBSOURCE    REFSEQ: accession NM_145261.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Janz,A., Walz,K., Cirnu,A., Surjanto,J., Urlaub,D., Leskien,M.,
            Kohlhaas,M., Nickel,A., Brand,T., Nose,N., Worsdorfer,P.,
            Wagner,N., Higuchi,T., Maack,C., Dudek,J., Lorenz,K., Klopocki,E.,
            Ergun,S., Duff,H.J. and Gerull,B.
  TITLE     Mutations in DNAJC19 cause altered mitochondrial structure and
            increased mitochondrial respiration in human iPSC-derived
            cardiomyocytes
  JOURNAL   Mol Metab 79, 101859 (2024)
   PUBMED   38142971
  REMARK    GeneRIF: Mutations in DNAJC19 cause altered mitochondrial structure
            and increased mitochondrial respiration in human iPSC-derived
            cardiomyocytes.
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Sinha,D., Srivastava,S. and D'Silva,P.
  TITLE     Functional Diversity of Human Mitochondrial J-proteins Is
            Independent of Their Association with the Inner Membrane
            Presequence Translocase
  JOURNAL   J Biol Chem 291 (33), 17345-17359 (2016)
   PUBMED   27330077
  REMARK    GeneRIF: Both DnaJC15 and DnaJC19 formed two distinct subcomplexes
            with Magmas at the import channel.
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Sinha,D., Joshi,N., Chittoor,B., Samji,P. and D'Silva,P.
  TITLE     Role of Magmas in protein transport and human mitochondria
            biogenesis
  JOURNAL   Hum Mol Genet 19 (7), 1248-1262 (2010)
   PUBMED   20053669
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Elsner,S., Simian,D., Iosefson,O., Marom,M. and Azem,A.
  TITLE     The mitochondrial protein translocation motor: structural
            conservation between the human and yeast Tim14/Pam18-Tim16/Pam16
            co-chaperones
  JOURNAL   Int J Mol Sci 10 (5), 2041-2053 (2009)
   PUBMED   19564938
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 116)
  AUTHORS   Sparkes,R., Patton,D. and Bernier,F.
  TITLE     Cardiac features of a novel autosomal recessive dilated
            cardiomyopathic syndrome due to defective importation of
            mitochondrial protein
  JOURNAL   Cardiol Young 17 (2), 215-217 (2007)
   PUBMED   17244376
  REMARK    GeneRIF: Dilated cardiomyopathy caused by homozygous mutations in a
            novel gene, DNAJC19, presumed to play a role in importation of
            mitochondrial proteins.
REFERENCE   8  (residues 1 to 116)
  AUTHORS   Davey,K.M., Parboosingh,J.S., McLeod,D.R., Chan,A., Casey,R.,
            Ferreira,P., Snyder,F.F., Bridge,P.J. and Bernier,F.P.
  TITLE     Mutation of DNAJC19, a human homologue of yeast inner mitochondrial
            membrane co-chaperones, causes DCMA syndrome, a novel autosomal
            recessive Barth syndrome-like condition
  JOURNAL   J Med Genet 43 (5), 385-393 (2006)
   PUBMED   16055927
  REMARK    GeneRIF: The association of dilated cardiomyopathy with ataxia
            (DCMA) syndrome with a segment of 3q26.33 and the identification of
            a splice mutation in a novel gene DNAJC19 in DCMA patients.
REFERENCE   9  (residues 1 to 116)
  AUTHORS   Mokranjac,D., Sichting,M., Neupert,W. and Hell,K.
  TITLE     Tim14, a novel key component of the import motor of the TIM23
            protein translocase of mitochondria
  JOURNAL   EMBO J 22 (19), 4945-4956 (2003)
   PUBMED   14517234
REFERENCE   10 (residues 1 to 116)
  AUTHORS   Bauer,M.F., Gempel,K., Reichert,A.S., Rappold,G.A., Lichtner,P.,
            Gerbitz,K.D., Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     Genetic and structural characterization of the human mitochondrial
            inner membrane translocase
  JOURNAL   J Mol Biol 289 (1), 69-82 (1999)
   PUBMED   10339406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA158066.1, BC073989.1 and
            AC008009.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is thought to be part of
            a complex involved in the ATP-dependent transport of transit
            peptide-containing proteins from the inner cell membrane to the
            mitochondrial matrix. Defects in this gene are a cause of
            3-methylglutaconic aciduria type 5 (MGA5), also known as dilated
            cardiomyopathy with ataxia (DCMA). Alternative splicing of this
            gene results in multiple transcript variants. Related pseudogenes
            have been identified on chromosomes 1, 2, 6, 10, 14 and 19.
            [provided by RefSeq, Jan 2012].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.131706.1,
                                           SRR1660807.98900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000382564.8/
                                                  ENSP00000372005.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.33"
     Protein         1..116
                     /product="mitochondrial import inner membrane translocase
                     subunit TIM14 isoform 1"
                     /note="homolog of yeast TIM14; mitochondrial import inner
                     membrane translocase subunit TIM14; DnaJ (Hsp40) homolog,
                     subfamily C, member 19; DnaJ-like protein subfamily C
                     member 19"
                     /calculated_mol_wt=10867
     transit_peptide 1..18
                     /inference="protein motif:SignalP:3.0"
                     /note="The cleavage site of the signal peptide has not
                     been experimentally determined."
                     /calculated_mol_wt=1650
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (Q96DA6.3)"
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DA6.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96DA6.3)"
     Region          <53..110
                     /region_name="DnaJ"
                     /note="DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock
                     protein 40) proteins are highly conserved and play crucial
                     roles in protein translation, folding, unfolding,
                     translocation, and degradation. They act primarily by
                     stimulating the ATPase activity of Hsp70s; cl02542"
                     /db_xref="CDD:413365"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96DA6.3)"
     CDS             1..116
                     /gene="DNAJC19"
                     /gene_synonym="PAM18; TIM14; TIMM14"
                     /coded_by="NM_145261.4:135..485"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33895.1"
                     /db_xref="GeneID:131118"
                     /db_xref="HGNC:HGNC:30528"
                     /db_xref="MIM:608977"
ORIGIN      
        1 mastvvavgl tiaaagfagr yvlqamkhme pqvkqvfqsl pksafsggyy rggfepkmtk
       61 reaalilgvs ptankgkird ahrrimllnh pdkggspyia akineakdll egqakk
//
LOCUS       NP_054836                275 aa            linear   PRI 27-APR-2025
DEFINITION  HUWE1-associated protein modifying stress responses 1 [Homo
            sapiens].
ACCESSION   NP_054836
VERSION     NP_054836.2
DBSOURCE    REFSEQ: accession NM_014117.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Monda,J.K., Ge,X., Hunkeler,M., Donovan,K.A., Ma,M.W., Jin,C.Y.,
            Leonard,M., Fischer,E.S. and Bennett,E.J.
  TITLE     HAPSTR1 localizes HUWE1 to the nucleus to limit stress signaling
            pathways
  JOURNAL   Cell Rep 42 (5), 112496 (2023)
   PUBMED   37167062
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Amici,D.R., Cingoz,H., Alasady,M.J., Alhayek,S., Phoumyvong,C.M.,
            Sahni,N., Yi,S.S. and Mendillo,M.L.
  TITLE     The HAPSTR2 retrogene buffers stress signaling and resilience in
            mammals
  JOURNAL   Nat Commun 14 (1), 152 (2023)
   PUBMED   36631436
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Amici,D.R., Ansel,D.J., Metz,K.A., Smith,R.S., Phoumyvong,C.M.,
            Gayatri,S., Chamera,T., Edwards,S.L., O'Hara,B.P., Srivastava,S.,
            Brockway,S., Takagishi,S.R., Cho,B.K., Goo,Y.A., Kelleher,N.L.,
            Ben-Sahra,I., Foltz,D.R., Li,J. and Mendillo,M.L.
  TITLE     C16orf72/HAPSTR1 is a molecular rheostat in an integrated network
            of stress response pathways
  JOURNAL   Proc Natl Acad Sci U S A 119 (27), e2111262119 (2022)
   PUBMED   35776542
  REMARK    GeneRIF: C16orf72/HAPSTR1 is a molecular rheostat in an integrated
            network of stress response pathways.
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Santos,G.A.D., Reis,S.T., Leite,K.R.M. and Srougi,M.
  TITLE     Telomere Attrition and p53 Response 1 (TAPR1): a new player in
            cancer biology?
  JOURNAL   Clinics (Sao Paulo) 76, e2997 (2021)
   PUBMED   34133663
  REMARK    GeneRIF: Telomere Attrition and p53 Response 1 (TAPR1): a new
            player in cancer biology?
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Benslimane,Y., Sanchez-Osuna,M., Coulombe-Huntington,J.,
            Bertomeu,T., Henry,D., Huard,C., Bonneil,E., Thibault,P., Tyers,M.
            and Harrington,L.
  TITLE     A novel p53 regulator, C16ORF72/TAPR1, buffers against telomerase
            inhibition
  JOURNAL   Aging Cell 20 (4), e13331 (2021)
   PUBMED   33660365
  REMARK    GeneRIF: A novel p53 regulator, C16ORF72/TAPR1, buffers against
            telomerase inhibition.
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 275)
  AUTHORS   McGue,M., Zhang,Y., Miller,M.B., Basu,S., Vrieze,S., Hicks,B.,
            Malone,S., Oetting,W.S. and Iacono,W.G.
  TITLE     A genome-wide association study of behavioral disinhibition
  JOURNAL   Behav Genet 43 (5), 363-373 (2013)
   PUBMED   23942779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087190.5.
            
            On Oct 29, 2003 this sequence version replaced NP_054836.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.180770.1,
                                           SRR1660803.200827.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327827.12/ ENSP00000331720.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.2"
     Protein         1..275
                     /product="HUWE1-associated protein modifying stress
                     responses 1"
                     /note="UPF0472 protein C16orf72; Telomere Attrition and
                     p53 Response 1; telomere attrition and p53 response 1
                     protein"
                     /calculated_mol_wt=30794
     Region          25..273
                     /region_name="DUF4588"
                     /note="Domain of unknown function (DUF4588); pfam15251"
                     /db_xref="CDD:464591"
     Region          32..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CZ0.1)"
     Region          80..152
                     /region_name="HUWE1-binding and HAPSTR1 oligomerization
                     (HBO) domain. /evidence=ECO:0000269|PubMed:35776542"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CZ0.1)"
     Region          155..181
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CZ0.1)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14CZ0.1)"
     Region          204..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CZ0.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14CZ0.1)"
     Region          250..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CZ0.1)"
     CDS             1..275
                     /gene="HAPSTR1"
                     /gene_synonym="C16orf72; PRO0149; TAPR1"
                     /coded_by="NM_014117.3:402..1229"
                     /db_xref="CCDS:CCDS10538.1"
                     /db_xref="GeneID:29035"
                     /db_xref="HGNC:HGNC:30103"
ORIGIN      
        1 meerkeegea eiqehgpehw fskwerqcla eaeqdeqlpp elqeeaaaaa qpehkqqklw
       61 hlfqnsatav aqlykdrvcq qpglslwvpf qnaatavtnl ykesvdthqr sfdigiqigy
      121 qrrnkdvlaw vkkrrrtirr edlisflcgk vppprnsrap prltvvspnr atstetsssv
      181 etdlqpfrea ialhglsgam asisvrsstp gspthvssgs nasrrrnglh dvdlntfise
      241 emalhldngg trkrtsaqcg dvitdspthk rnrmi
//
LOCUS       NP_002993                159 aa            linear   PRI 27-APR-2025
DEFINITION  succinate dehydrogenase [ubiquinone] cytochrome b small subunit,
            mitochondrial isoform a precursor [Homo sapiens].
ACCESSION   NP_002993
VERSION     NP_002993.1
DBSOURCE    REFSEQ: accession NM_003002.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Du,Z., Zhou,X., Lai,Y., Xu,J., Zhang,Y., Zhou,S., Feng,Z., Yu,L.,
            Tang,Y., Wang,W., Yu,L., Tian,C., Ran,T., Chen,H., Guddat,L.W.,
            Liu,F., Gao,Y., Rao,Z. and Gong,H.
  TITLE     Structure of the human respiratory complex II
  JOURNAL   Proc Natl Acad Sci U S A 120 (18), e2216713120 (2023)
   PUBMED   37098072
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Taieb,D., Wanna,G.B., Ahmad,M., Lussey-Lepoutre,C., Perrier,N.D.,
            Nolting,S., Amar,L., Timmers,H.J.L.M., Schwam,Z.G., Estrera,A.L.,
            Lim,M., Pollom,E.L., Vitzthum,L., Bourdeau,I., Casey,R.T.,
            Castinetti,F., Clifton-Bligh,R., Corssmit,E.P.M., de Krijger,R.R.,
            Del Rivero,J., Eisenhofer,G., Ghayee,H.K., Gimenez-Roqueplo,A.P.,
            Grossman,A., Imperiale,A., Jansen,J.C., Jha,A., Kerstens,M.N.,
            Kunst,H.P.M., Liu,J.K., Maher,E.R., Marchioni,D.,
            Mercado-Asis,L.B., Mete,O., Naruse,M., Nilubol,N.,
            Pandit-Taskar,N., Sebag,F., Tanabe,A., Widimsky,J., Meuter,L.,
            Lenders,J.W.M. and Pacak,K.
  TITLE     Clinical consensus guideline on the management of phaeochromocytoma
            and paraganglioma in patients harbouring germline SDHD pathogenic
            variants
  JOURNAL   Lancet Diabetes Endocrinol 11 (5), 345-361 (2023)
   PUBMED   37011647
  REMARK    GeneRIF: Clinical consensus guideline on the management of
            phaeochromocytoma and paraganglioma in patients harbouring germline
            SDHD pathogenic variants.
            Review article
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Baysal,B.E.
  TITLE     Mitochondrial complex II and genomic imprinting in inheritance of
            paraganglioma tumors
  JOURNAL   Biochim Biophys Acta 1827 (5), 573-577 (2013)
   PUBMED   23291190
  REMARK    GeneRIF: Studies indicate that mutations in the mitochondrial
            complex II structural subunit genes SDHB, SDHC and SDHD and the
            regulatory subunit gene SDHAF2 in many paraganglioma families.
            Review article
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Gimm,O., Armanios,M., Dziema,H., Neumann,H.P. and Eng,C.
  TITLE     Somatic and occult germ-line mutations in SDHD, a mitochondrial
            complex II gene, in nonfamilial pheochromocytoma
  JOURNAL   Cancer Res 60 (24), 6822-6825 (2000)
   PUBMED   11156372
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Baysal,B.E., Ferrell,R.E., Willett-Brozick,J.E., Lawrence,E.C.,
            Myssiorek,D., Bosch,A., van der Mey,A., Taschner,P.E.,
            Rubinstein,W.S., Myers,E.N., Richard,C.W. 3rd, Cornelisse,C.J.,
            Devilee,P. and Devlin,B.
  TITLE     Mutations in SDHD, a mitochondrial complex II gene, in hereditary
            paraganglioma
  JOURNAL   Science 287 (5454), 848-851 (2000)
   PUBMED   10657297
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Hirawake,H., Taniwaki,M., Tamura,A., Amino,H., Tomitsuka,E. and
            Kita,K.
  TITLE     Characterization of the human SDHD gene encoding the small subunit
            of cytochrome b (cybS) in mitochondrial succinate-ubiquinone
            oxidoreductase
  JOURNAL   Biochim Biophys Acta 1412 (3), 295-300 (1999)
   PUBMED   10482792
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Hirawake,H., Taniwaki,M., Tamura,A., Kojima,S. and Kita,K.
  TITLE     Cytochrome b in human complex II (succinate-ubiquinone
            oxidoreductase): cDNA cloning of the components in liver
            mitochondria and chromosome assignment of the genes for the large
            (SDHC) and small (SDHD) subunits to 1q21 and 11q23
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 132-138 (1997)
   PUBMED   9533030
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Mariman,E.C., van Beersum,S.E., Cremers,C.W., Struycken,P.M. and
            Ropers,H.H.
  TITLE     Fine mapping of a putatively imprinted gene for familial
            non-chromaffin paragangliomas to chromosome 11q13.1: evidence for
            genetic heterogeneity
  JOURNAL   Hum Genet 95 (1), 56-62 (1995)
   PUBMED   7814027
REFERENCE   9  (residues 1 to 159)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   10 (residues 1 to 159)
  AUTHORS   Heutink,P., van der Mey,A.G., Sandkuijl,L.A., van Gils,A.P.,
            Bardoel,A., Breedveld,G.J., van Vliet,M., van Ommen,G.J.,
            Cornelisse,C.J., Oostra,B.A. et al.
  TITLE     A gene subject to genomic imprinting and responsible for hereditary
            paragangliomas maps to chromosome 11q23-qter
  JOURNAL   Hum Mol Genet 1 (1), 7-10 (1992)
   PUBMED   1301144
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC015188.1, AI753083.1 and
            AP002007.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of complex II of the
            respiratory chain, which is responsible for the oxidation of
            succinate. The encoded protein is one of two integral membrane
            proteins anchoring the complex to the matrix side of the
            mitochondrial inner membrane. Mutations in this gene are associated
            with the formation of tumors, including hereditary paraganglioma.
            Transmission of disease occurs almost exclusively through the
            paternal allele, suggesting that this locus may be maternally
            imprinted. There are pseudogenes for this gene on chromosomes 1, 2,
            3, 7, and 18. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Feb 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.222484.1,
                                           SRR5189652.48039.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            imprinted gene                     :: PMID: 23291190
            MANE Ensembl match                 :: ENST00000375549.8/
                                                  ENSP00000364699.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.1"
     Protein         1..159
                     /product="succinate dehydrogenase [ubiquinone] cytochrome
                     b small subunit, mitochondrial isoform a precursor"
                     /note="succinate dehydrogenase [ubiquinone] cytochrome b
                     small subunit, mitochondrial; succinate-ubiquinone
                     reductase membrane anchor subunit; succinate-ubiquinone
                     oxidoreductase cytochrome b small subunit; succinate
                     dehydrogenase complex subunit D integral membrane protein;
                     malate dehydrogenase [quinone] cytochrome b small subunit"
                     /calculated_mol_wt=10889
     transit_peptide 1..56
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O14521.1)"
                     /calculated_mol_wt=6172
     mat_peptide     57..159
                     /product="Succinate dehydrogenase [ubiquinone] cytochrome
                     b small subunit, mitochondrial. /id=PRO_0000006487"
                     /note="propagated from UniProtKB/Swiss-Prot (O14521.1)"
                     /calculated_mol_wt=10889
     Region          60..158
                     /region_name="SQR_TypeC_CybS"
                     /note="SQR catalyzes the oxidation of succinate to
                     fumarate coupled to the reduction of quinone to quinol.
                     Eukaryotic SQRs reduce high potential quinones such as
                     ubiquinone. SQR is also called succinate dehydrogenase or
                     Complex II, and is part of the citric...; cd03496"
                     /db_xref="CDD:239576"
     Site            order(60,62..63,109,112..113,116)
                     /site_type="active"
                     /note="Iron-sulfur protein interface [active]"
                     /db_xref="CDD:239576"
     Site            64..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14521.1)"
     Site            order(70,113..114,135,138,141,146,152,157)
                     /site_type="other"
                     /note="CybL subunit interface [polypeptide binding]"
                     /db_xref="CDD:239576"
     Site            order(83..84,154,157)
                     /site_type="other"
                     /note="distal quinone binding site [chemical binding]"
                     /db_xref="CDD:239576"
     Site            91..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14521.1)"
     Site            order(102,106)
                     /site_type="other"
                     /note="proximal heme binding site [chemical binding]"
                     /db_xref="CDD:239576"
     Site            114
                     /site_type="other"
                     /note="proximal quinone binding site [chemical binding]"
                     /db_xref="CDD:239576"
     Site            123..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14521.1)"
     CDS             1..159
                     /gene="SDHD"
                     /gene_synonym="CBT1; CII-4; CWS3; cybS; MC2DN3; PGL; PGL1;
                     PPGL1; QPs3; SDH4"
                     /coded_by="NM_003002.4:36..515"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS31678.1"
                     /db_xref="GeneID:6392"
                     /db_xref="HGNC:HGNC:10683"
                     /db_xref="MIM:602690"
ORIGIN      
        1 mavlwrlsav cgalggrall lrtpvvrpah isaflqdrpi pewcgvqhih lspshhsgsk
       61 aaslhwtser vvsvlllgll paaylnpcsa mdyslaaalt lhghwglgqv vtdyvhgdal
      121 qkaakaglla lsaltfaglc yfnyhdvgic kavamlwkl
//
LOCUS       NP_001305814              82 aa            linear   PRI 27-APR-2025
DEFINITION  high mobility group nucleosome-binding domain-containing protein 3
            isoform f [Homo sapiens].
ACCESSION   NP_001305814
VERSION     NP_001305814.1
DBSOURCE    REFSEQ: accession NM_001318885.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Bian,Y., Li,J., Shen,H., Li,Y., Hou,Y., Huang,L., Song,G. and
            Qiao,C.
  TITLE     WTAP dysregulation-mediated HMGN3-m6A modification inhibited
            trophoblast invasion in early-onset preeclampsia
  JOURNAL   FASEB J 36 (12), e22617 (2022)
   PUBMED   36412513
  REMARK    GeneRIF: WTAP dysregulation-mediated HMGN3-m6A modification
            inhibited trophoblast invasion in early-onset preeclampsia.
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Sorin,S., Kubota,S., Hamidi,S., Yokomizo-Nakano,T.,
            Vaeteewoottacharn,K., Wongkham,S., Waraasawapati,S., Pairojkul,C.,
            Bai,J., Morii,M., Sheng,G., Sawanyawisuth,K. and Sashida,G.
  TITLE     HMGN3 represses transcription of epithelial regulators to promote
            migration of cholangiocarcinoma in a SNAI2-dependent manner
  JOURNAL   FASEB J 36 (7), e22345 (2022)
   PUBMED   35635715
  REMARK    GeneRIF: HMGN3 represses transcription of epithelial regulators to
            promote migration of cholangiocarcinoma in a SNAI2-dependent
            manner.
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Koh,M., Ahmad,I., Ko,Y., Zhang,Y., Martinez,T.F., Diedrich,J.K.,
            Chu,Q., Moresco,J.J., Erb,M.A., Saghatelian,A., Schultz,P.G. and
            Bollong,M.J.
  TITLE     A short ORF-encoded transcriptional regulator
  JOURNAL   Proc Natl Acad Sci U S A 118 (4) (2021)
   PUBMED   33468658
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Lei,S.F., Shen,H., Yang,T.L., Guo,Y., Dong,S.S., Xu,X.H.,
            Deng,F.Y., Tian,Q., Liu,Y.J., Liu,Y.Z., Li,J. and Deng,H.W.
  TITLE     Genome-wide association study identifies HMGN3 locus for spine bone
            size variation in Chinese
  JOURNAL   Hum Genet 131 (3), 463-469 (2012)
   PUBMED   21947420
  REMARK    GeneRIF: The SNPs in the region of HMGN3 gene formed a tightly
            combined haplotype block in both Chinese and Caucasians. The
            results suggest that the genomic region containing HMGN3 gene may
            be associated with spine BS in Chinese.
REFERENCE   5  (residues 1 to 82)
  AUTHORS   Ueda,T., Furusawa,T., Kurahashi,T., Tessarollo,L. and Bustin,M.
  TITLE     The nucleosome binding protein HMGN3 modulates the transcription
            profile of pancreatic beta cells and affects insulin secretion
  JOURNAL   Mol Cell Biol 29 (19), 5264-5276 (2009)
   PUBMED   19651901
  REMARK    GeneRIF: loss of HMGN3 impairs glucose-stimulated insulin secretion
            and leads to a diabetic phenotype.
REFERENCE   6  (residues 1 to 82)
  AUTHORS   West,K.L., Castellini,M.A., Duncan,M.K. and Bustin,M.
  TITLE     Chromosomal proteins HMGN3a and HMGN3b regulate the expression of
            glycine transporter 1
  JOURNAL   Mol Cell Biol 24 (9), 3747-3756 (2004)
   PUBMED   15082770
REFERENCE   7  (residues 1 to 82)
  AUTHORS   Leong,P.W., Liew,K., Lim,W. and Chow,V.T.
  TITLE     Differential display RT-PCR analysis of enterovirus-71-infected
            rhabdomyosarcoma cells reveals mRNA expression responses of
            multiple human genes with known and novel functions
  JOURNAL   Virology 295 (1), 147-159 (2002)
   PUBMED   12033773
REFERENCE   8  (residues 1 to 82)
  AUTHORS   West,K.L., Ito,Y., Birger,Y., Postnikov,Y., Shirakawa,H. and
            Bustin,M.
  TITLE     HMGN3a and HMGN3b, two protein isoforms with a tissue-specific
            expression pattern, expand the cellular repertoire of
            nucleosome-binding proteins
  JOURNAL   J Biol Chem 276 (28), 25959-25969 (2001)
   PUBMED   11356838
REFERENCE   9  (residues 1 to 82)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355796.11.
            
            Summary: The protein encoded by this gene binds thyroid hormone
            receptor beta in the presence of thyroid hormone. The encoded
            protein, a member of the HMGN protein family, is thought to reduce
            the compactness of the chromatin fiber in nucleosomes, thereby
            enhancing transcription from chromatin templates. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. There is a related pseudogene on chromosome 1.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (6) lacks an alternate in-frame
            exon in the 5' coding region compared to variant 1. The resulting
            isoform (f) is shorter than isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.263336.1, W19124.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267756, SAMN03267763
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..82
                     /product="high mobility group nucleosome-binding
                     domain-containing protein 3 isoform f"
                     /note="thyroid hormone receptor interacting protein 7;
                     high mobility group nucleosome-binding domain-containing
                     protein 3; TR-interacting protein 7"
                     /calculated_mol_wt=8719
     Region          3..77
                     /region_name="HMG17"
                     /note="domain in high mobilty group proteins HMG14 and HMG
                     17; smart00527"
                     /db_xref="CDD:197773"
     CDS             1..82
                     /gene="HMGN3"
                     /gene_synonym="PNAS-24; PNAS-25; TRIP7"
                     /coded_by="NM_001318885.2:123..371"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:9324"
                     /db_xref="HGNC:HGNC:12312"
                     /db_xref="MIM:604502"
ORIGIN      
        1 mpkrkptrrs arlsakpapp kpepkprkts akkepgakis rgakgkkeek qeagkegtap
       61 sengetkaee aqktesvdne ge
//
LOCUS       NP_000749                144 aa            linear   PRI 27-APR-2025
DEFINITION  granulocyte-macrophage colony-stimulating factor precursor [Homo
            sapiens].
ACCESSION   NP_000749
VERSION     NP_000749.2
DBSOURCE    REFSEQ: accession NM_000758.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Gan,Y., Zhou,H., Guo,Y., Huang,B., Liu,H., Wang,Z., Li,Z., Zhao,X.,
            Zhu,H., Han,Q., Ye,H., He,J., Wang,Q., Li,Z. and Sun,X.
  TITLE     A GITRL-mTORC1-GM-CSF Positive Loop Promotes Pathogenic Th17
            Response in Primary Sjogren Syndrome
  JOURNAL   Arthritis Rheumatol 76 (9), 1419-1430 (2024)
   PUBMED   38589318
  REMARK    GeneRIF: A GITRL-mTORC1-GM-CSF Positive Loop Promotes Pathogenic
            Th17 Response in Primary Sjogren Syndrome.
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Li,H., Cao,X., Gu,X., Dong,M., Huang,L., Mao,C., Xia,S., Yang,H.,
            Bao,X., Yang,Y. and Xu,Y.
  TITLE     GM-CSF Promotes the Development of Dysfunctional Vascular Networks
            in Moyamoya Disease
  JOURNAL   Neurosci Bull 40 (4), 451-465 (2024)
   PUBMED   38113014
  REMARK    GeneRIF: GM-CSF Promotes the Development of Dysfunctional Vascular
            Networks in Moyamoya Disease.
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Harber,K.J., Nguyen,T.A., Schomakers,B.V., Heister,D.A.F., de
            Vries,H.E., van Weeghel,M., Van den Bossche,J. and de
            Winther,M.P.J.
  TITLE     Adenine is an anti-inflammatory metabolite found to be more
            abundant in M-CSF over GM-CSF-differentiated human macrophages
  JOURNAL   Immunol Lett 265, 23-30 (2024)
   PUBMED   38142781
  REMARK    GeneRIF: Adenine is an anti-inflammatory metabolite found to be
            more abundant in M-CSF over GM-CSF-differentiated human
            macrophages.
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Rahmani,F., Brier,M.R., Gordon,B.A., McKay,N., Flores,S., Keefe,S.,
            Hornbeck,R., Ances,B., Joseph-Mathurin,N., Xiong,C., Wang,G.,
            Raji,C.A., Libre-Guerra,J.J., Perrin,R.J., McDade,E., Daniels,A.,
            Karch,C., Day,G.S., Brickman,A.M., Fulham,M., Jack,C.R. Jr., la La
            Fougere,C., Reischl,G., Schofield,P.R., Oh,H., Levin,J.,
            Voglein,J., Cash,D.M., Yakushev,I., Ikeuchi,T., Klunk,W.E.,
            Morris,J.C., Bateman,R.J. and Benzinger,T.L.S.
  CONSRTM   Dominantly Inherited Alzheimer Network (DIAN)
  TITLE     T1 and FLAIR signal intensities are related to tau pathology in
            dominantly inherited Alzheimer disease
  JOURNAL   Hum Brain Mapp 44 (18), 6375-6387 (2023)
   PUBMED   37867465
  REMARK    GeneRIF: T1 and FLAIR signal intensities are related to tau
            pathology in dominantly inherited Alzheimer disease.
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Martin,S.J., Brand-Arzamendi,K., Saab,G., Muccilli,A., Oh,J. and
            Schneider,R.
  TITLE     GM-CSF is a marker of compartmentalised intrathecal inflammation in
            multiple sclerosis
  JOURNAL   Mult Scler 29 (11-12), 1373-1382 (2023)
   PUBMED   37700482
  REMARK    GeneRIF: GM-CSF is a marker of compartmentalised intrathecal
            inflammation in multiple sclerosis.
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Walter,M.R., Cook,W.J., Ealick,S.E., Nagabhushan,T.L., Trotta,P.P.
            and Bugg,C.E.
  TITLE     Three-dimensional structure of recombinant human
            granulocyte-macrophage colony-stimulating factor
  JOURNAL   J Mol Biol 224 (4), 1075-1085 (1992)
   PUBMED   1569568
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Kaushansky,K., Lopez,J.A. and Brown,C.B.
  TITLE     Role of carbohydrate modification in the production and secretion
            of human granulocyte macrophage colony-stimulating factor in
            genetically engineered and normal mesenchymal cells
  JOURNAL   Biochemistry 31 (6), 1881-1886 (1992)
   PUBMED   1737041
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Diederichs,K., Boone,T. and Karplus,P.A.
  TITLE     Novel fold and putative receptor binding site of
            granulocyte-macrophage colony-stimulating factor
  JOURNAL   Science 254 (5039), 1779-1782 (1991)
   PUBMED   1837174
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Frolova,E.I., Dolganov,G.M., Mazo,I.A., Smirnov,D.V., Copeland,P.,
            Stewart,C., O'Brien,S.J. and Dean,M.
  TITLE     Linkage mapping of the human CSF2 and IL3 genes
  JOURNAL   Proc Natl Acad Sci U S A 88 (11), 4821-4824 (1991)
   PUBMED   1675789
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Hayashida,K., Kitamura,T., Gorman,D.M., Arai,K., Yokota,T. and
            Miyajima,A.
  TITLE     Molecular cloning of a second subunit of the receptor for human
            granulocyte-macrophage colony-stimulating factor (GM-CSF):
            reconstitution of a high-affinity GM-CSF receptor
  JOURNAL   Proc Natl Acad Sci U S A 87 (24), 9655-9659 (1990)
   PUBMED   1702217
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC034228.6, M11220.1 and
            BC108724.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 31, 2002 this sequence version replaced NP_000749.1.
            
            Summary: The protein encoded by this gene is a cytokine that
            controls the production, differentiation, and function of
            granulocytes and macrophages. The active form of the protein is
            found extracellularly as a homodimer. This gene has been localized
            to a cluster of related genes at chromosome region 5q31, which is
            known to be associated with interstitial deletions in the 5q-
            syndrome and acute myelogenous leukemia. Other genes in the cluster
            include those encoding interleukins 4, 5, and 13. This gene plays a
            role in promoting tissue inflammation. Elevated levels of
            cytokines, including the one produced by this gene, have been
            detected in SARS-CoV-2 infected patients that develop acute
            respiratory distress syndrome. Mice deficient in this gene or its
            receptor develop pulmonary alveolar proteinosis. [provided by
            RefSeq, Aug 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC108724.1, M11220.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in cytokine storm inflammatory
                                      response
            MANE Ensembl match     :: ENST00000296871.4/ ENSP00000296871.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..144
                     /product="granulocyte-macrophage colony-stimulating factor
                     precursor"
                     /note="sargramostim; molgramostin; molgramostim;
                     granulocyte macrophage-colony stimulating factor; colony
                     stimulating factor 2 (granulocyte-macrophage)"
                     /calculated_mol_wt=14478
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1835
     mat_peptide     18..144
                     /product="Granulocyte-macrophage colony-stimulating
                     factor. /id=PRO_0000005865"
                     /note="propagated from UniProtKB/Swiss-Prot (P04141.1)"
                     /calculated_mol_wt=14478
     Region          18..138
                     /region_name="CSF2"
                     /note="Granulocyte Macrophage Colony Stimulating Factor
                     (GM-CSF) is a member of the large family of polypeptide
                     growth factors called cytokines. It stimulates a wide
                     variety of hematopoietic and nonhematopoietic cell types
                     via binding to members of the cytokine...; cd00040"
                     /db_xref="CDD:238000"
     Site            22
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1737041; propagated from
                     UniProtKB/Swiss-Prot (P04141.1)"
     Site            24
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1737041; propagated from
                     UniProtKB/Swiss-Prot (P04141.1)"
     Site            26
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:1737041; propagated from
                     UniProtKB/Swiss-Prot (P04141.1)"
     Site            27
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine, partial.
                     /evidence=ECO:0000269|PubMed:1737041; propagated from
                     UniProtKB/Swiss-Prot (P04141.1)"
     Site            order(44,54)
                     /site_type="glycosylation"
                     /note="glycosylation sites [posttranslational
                     modification]"
                     /db_xref="CDD:238000"
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P04141.1)"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P04141.1)"
     CDS             1..144
                     /gene="CSF2"
                     /gene_synonym="CSF; GMCSF"
                     /coded_by="NM_000758.4:36..470"
                     /db_xref="CCDS:CCDS4150.1"
                     /db_xref="GeneID:1437"
                     /db_xref="HGNC:HGNC:2434"
                     /db_xref="MIM:138960"
ORIGIN      
        1 mwlqsllllg tvacsisapa rspspstqpw ehvnaiqear rllnlsrdta aemnetvevi
       61 semfdlqept clqtrlelyk qglrgsltkl kgpltmmash ykqhcpptpe tscatqiitf
      121 esfkenlkdf llvipfdcwe pvqe
//
LOCUS       NP_705740                143 aa            linear   ROD 27-APR-2025
DEFINITION  opalin [Mus musculus].
ACCESSION   NP_705740
VERSION     NP_705740.1
DBSOURCE    REFSEQ: accession NM_153520.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Yu,Z., Yang,Z., Ren,G., Wang,Y., Luo,X., Zhu,F., Yu,S., Jia,L.,
            Chen,M., Worley,P.F. and Xiao,B.
  TITLE     GATOR2 complex-mediated amino acid signaling regulates brain
            myelination
  JOURNAL   Proc Natl Acad Sci U S A 119 (3) (2022)
   PUBMED   35022234
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Hardt,R., Jordans,S., Winter,D., Gieselmann,V., Wang-Eckhardt,L.
            and Eckhardt,M.
  TITLE     Decreased turnover of the CNS myelin protein Opalin in a mouse
            model of hereditary spastic paraplegia 35
  JOURNAL   Hum Mol Genet 29 (22), 3616-3630 (2021)
   PUBMED   33215680
  REMARK    GeneRIF: Decreased turnover of the CNS myelin protein Opalin in a
            mouse model of hereditary spastic paraplegia 35.
REFERENCE   3  (residues 1 to 143)
  AUTHORS   de Faria,O. Jr., Dhaunchak,A.S., Kamen,Y., Roth,A.D., Kuhlmann,T.,
            Colman,D.R. and Kennedy,T.E.
  TITLE     TMEM10 Promotes Oligodendrocyte Differentiation and is Expressed by
            Oligodendrocytes in Human Remyelinating Multiple Sclerosis Plaques
  JOURNAL   Sci Rep 9 (1), 3606 (2019)
   PUBMED   30837646
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Yoshikawa,F., Sato,Y., Tohyama,K., Akagi,T., Furuse,T.,
            Sadakata,T., Tanaka,M., Shinoda,Y., Hashikawa,T., Itohara,S.,
            Sano,Y., Ghandour,M.S., Wakana,S. and Furuichi,T.
  TITLE     Mammalian-Specific Central Myelin Protein Opalin Is Redundant for
            Normal Myelination: Structural and Behavioral Assessments
  JOURNAL   PLoS One 11 (11), e0166732 (2016)
   PUBMED   27855200
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Xiao,J., Vemula,S.R., Xue,Y., Khan,M.M., Kuruvilla,K.P.,
            Marquez-Lona,E.M., Cobb,M.R. and LeDoux,M.S.
  TITLE     Motor phenotypes and molecular networks associated with germline
            deficiency of Ciz1
  JOURNAL   Exp Neurol 283 (Pt A), 110-120 (2016)
   PUBMED   27163549
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Yoshikawa,F., Sato,Y., Tohyama,K., Akagi,T., Hashikawa,T.,
            Nagakura-Takagi,Y., Sekine,Y., Morita,N., Baba,H., Suzuki,Y.,
            Sugano,S., Sato,A. and Furuichi,T.
  TITLE     Opalin, a transmembrane sialylglycoprotein located in the central
            nervous system myelin paranodal loop membrane
  JOURNAL   J Biol Chem 283 (30), 20830-20840 (2008)
   PUBMED   18490449
  REMARK    GeneRIF: highly sialylglycosylated Opalin has a role in an
            intermembranous function of the myelin paranodal loops in the
            central nervous system
REFERENCE   7  (residues 1 to 143)
  AUTHORS   Kippert,A., Trajkovic,K., Fitzner,D., Opitz,L. and Simons,M.
  TITLE     Identification of Tmem10/Opalin as a novel marker for
            oligodendrocytes using gene expression profiling
  JOURNAL   BMC Neurosci 9, 40 (2008)
   PUBMED   18439243
  REMARK    GeneRIF: Together, our results demonstrate that Tmem10 is a novel
            marker for in vitro generated oligodendrocytes.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 143)
  AUTHORS   Aruga,J., Yoshikawa,F., Nozaki,Y., Sakaki,Y., Toyoda,A. and
            Furuichi,T.
  TITLE     An oligodendrocyte enhancer in a phylogenetically conserved intron
            region of the mammalian myelin gene Opalin
  JOURNAL   J Neurochem 102 (5), 1533-1547 (2007)
   PUBMED   17442045
REFERENCE   9  (residues 1 to 143)
  AUTHORS   Montelius,A., Marmigere,F., Baudet,C., Aquino,J.B., Enerback,S. and
            Ernfors,P.
  TITLE     Emergence of the sensory nervous system as defined by Foxs1
            expression
  JOURNAL   Differentiation 75 (5), 404-417 (2007)
   PUBMED   17309606
REFERENCE   10 (residues 1 to 143)
  AUTHORS   Nobile,C., Hinzmann,B., Scannapieco,P., Siebert,R., Zimbello,R.,
            Perez-Tur,J., Sarafidou,T., Moschonas,N.K., French,L., Deloukas,P.,
            Ciccodicola,A., Gesk,S., Poza,J.J., Lo Nigro,C., Seri,M.,
            Schlegelberger,B., Rosenthal,A., Valle,G., Lopez de Munain,A.,
            Tassinari,C.A. and Michelucci,R.
  TITLE     Identification and characterization of a novel human brain-specific
            gene, homologous to S. scrofa tmp83.5, in the chromosome 10q24
            critical region for temporal lobe epilepsy and spastic paraplegia
  JOURNAL   Gene 282 (1-2), 87-94 (2002)
   PUBMED   11814680
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC121873.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK140031.1, BK000002.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02415132 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 34.36 cM"
     Protein         1..143
                     /product="opalin"
                     /note="transmembrane protein 10; transmembrane protein
                     TMP10"
                     /calculated_mol_wt=15702
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M750.1)"
     Site            6
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18490449; propagated from
                     UniProtKB/Swiss-Prot (Q7M750.1)"
     Site            12
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18490449; propagated from
                     UniProtKB/Swiss-Prot (Q7M750.1)"
     Site            14
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:18490449; propagated from
                     UniProtKB/Swiss-Prot (Q7M750.1)"
     Site            31..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M750.1)"
     Region          79..103
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M750.1)"
     Region          79..95
                     /region_name="Required for plasma membrane localization.
                     /evidence=ECO:0000269|PubMed:30837646"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M750.1)"
     CDS             1..143
                     /gene="Opalin"
                     /gene_synonym="Tmem10; Tmp10"
                     /coded_by="NM_153520.2:78..509"
                     /db_xref="CCDS:CCDS37985.1"
                     /db_xref="GeneID:226115"
                     /db_xref="MGI:MGI:2657025"
ORIGIN      
        1 msfslnftlp snttsspvvt sakatdcgps iglaagipsl latallvall ftliqrrrti
       61 ddepveetei pceiselydn pkisenprrs pthemnprgs qeghiyvktv sgseeplpdt
      121 yrppeelerr rglwwlvpsl sle
//
LOCUS       NP_002679                369 aa            linear   PRI 27-APR-2025
DEFINITION  septin-5 isoform 1 [Homo sapiens].
ACCESSION   NP_002679
VERSION     NP_002679.2
DBSOURCE    REFSEQ: accession NM_002688.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Marttinen,M., Ferreira,C.B., Paldanius,K.M.A., Takalo,M.,
            Natunen,T., Makinen,P., Leppanen,L., Leinonen,V., Tanigaki,K.,
            Kang,G., Hiroi,N., Soininen,H., Rilla,K., Haapasalo,A. and
            Hiltunen,M.
  TITLE     Presynaptic Vesicle Protein SEPTIN5 Regulates the Degradation of
            APP C-Terminal Fragments and the Levels of Abeta
  JOURNAL   Cells 9 (11), 2482 (2020)
   PUBMED   33203136
  REMARK    GeneRIF: Presynaptic Vesicle Protein SEPTIN5 Regulates the
            Degradation of APP C-Terminal Fragments and the Levels of Abeta.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Caltagarone,J., Rhodes,J., Honer,W.G. and Bowser,R.
  TITLE     Localization of a novel septin protein, hCDCrel-1, in neurons of
            human brain
  JOURNAL   Neuroreport 9 (12), 2907-2912 (1998)
   PUBMED   9760144
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Yagi,M., Zieger,B., Roth,G.J. and Ware,J.
  TITLE     Structure and expression of the human septin gene HCDCREL-1
  JOURNAL   Gene 212 (2), 229-236 (1998)
   PUBMED   9611266
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Hsu,S.C., Hazuka,C.D., Roth,R., Foletti,D.L., Heuser,J. and
            Scheller,R.H.
  TITLE     Subunit composition, protein interactions, and structures of the
            mammalian brain sec6/8 complex and septin filaments
  JOURNAL   Neuron 20 (6), 1111-1122 (1998)
   PUBMED   9655500
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Megonigal,M.D., Rappaport,E.F., Jones,D.H., Williams,T.M.,
            Lovett,B.D., Kelly,K.M., Lerou,P.H., Moulton,T., Budarf,M.L. and
            Felix,C.A.
  TITLE     t(11;22)(q23;q11.2) In acute myeloid leukemia of infant twins fuses
            MLL with hCDCrel, a cell division cycle gene in the genomic region
            of deletion in DiGeorge and velocardiofacial syndromes
  JOURNAL   Proc Natl Acad Sci U S A 95 (11), 6413-6418 (1998)
   PUBMED   9600980
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Aug 18;95(17):10344]
REFERENCE   9  (residues 1 to 369)
  AUTHORS   McKie,J.M., Sutherland,H.F., Harvey,E., Kim,U.J. and Scambler,P.J.
  TITLE     A human gene similar to Drosophila melanogaster peanut maps to the
            DiGeorge syndrome region of 22q11
  JOURNAL   Hum Genet 101 (1), 6-12 (1997)
   PUBMED   9385360
REFERENCE   10 (residues 1 to 369)
  AUTHORS   Zieger,B., Hashimoto,Y. and Ware,J.
  TITLE     Alternative expression of platelet glycoprotein Ib(beta) mRNA from
            an adjacent 5' gene with an imperfect polyadenylation signal
            sequence
  JOURNAL   J Clin Invest 99 (3), 520-525 (1997)
   PUBMED   9022087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC025261.1.
            
            On Aug 30, 2000 this sequence version replaced NP_002679.1.
            
            Summary: This gene is a member of the septin gene family of
            nucleotide binding proteins, originally described in yeast as cell
            division cycle regulatory proteins. Septins are highly conserved in
            yeast, Drosophila, and mouse and appear to regulate cytoskeletal
            organization. Disruption of septin function disturbs cytokinesis
            and results in large multinucleate or polyploid cells. This gene is
            mapped to 22q11, the region frequently deleted in DiGeorge and
            velocardiofacial syndromes. A translocation involving the MLL gene
            and this gene has also been reported in patients with acute myeloid
            leukemia. Alternative splicing results in multiple transcript
            variants. The presence of a non-consensus polyA signal (AACAAT) in
            this gene also results in read-through transcription into the
            downstream neighboring gene (GP1BB; platelet glycoprotein Ib),
            whereby larger, non-coding transcripts are produced. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025261.1, U74628.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000455784.7/ ENSP00000391311.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..369
                     /product="septin-5 isoform 1"
                     /EC_number="3.1.5.1"
                     /note="peanut-like 1; cell division control related
                     protein 1; platelet glycoprotein Ib beta chain"
                     /calculated_mol_wt=42646
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2Q6; propagated from
                     UniProtKB/Swiss-Prot (Q99719.1)"
     Region          42..313
                     /region_name="Septin"
                     /note="pfam00735"
                     /db_xref="CDD:395596"
     Region          51..58
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99719.1)"
     Site            51..58
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(53..59,108,111,189..190,192,248..249)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            83..91
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            85
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Region          108..111
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99719.1)"
     Site            108..111
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(110..145,146..155)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Site            168
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2Q6; propagated from
                     UniProtKB/Swiss-Prot (Q99719.1)"
     Region          189..192
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99719.1)"
     Site            189..192
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99719.1)"
     Site            248..250
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99719.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2Q6; propagated from
                     UniProtKB/Swiss-Prot (Q99719.1)"
     CDS             1..369
                     /gene="SEPTIN5"
                     /gene_synonym="CDCREL; CDCREL-1; CDCREL1; H5; HCDCREL-1;
                     PNUTL1; SEPT5; Septin-5"
                     /coded_by="NM_002688.6:87..1196"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13764.1"
                     /db_xref="GeneID:5413"
                     /db_xref="HGNC:HGNC:9164"
                     /db_xref="MIM:602724"
ORIGIN      
        1 mstglryksk latpedkqdi dkqyvgfatl pnqvhrksvk kgfdftlmva gesglgkstl
       61 vhslfltdly kdrkllsaee risqtveilk htvdieekgv klkltivdtp gfgdavnnte
      121 cwkpitdyvd qqfeqyfrde sglnrkniqd nrvhcclyfi spfghglrpv dvgfmkalhe
      181 kvnivpliak adclvpseir klkerireei dkfgihvyqf pecdsdeded fkqqdrelke
      241 sapfavigsn tvveakgqrv rgrlypwgiv evenqahcdf vklrnmlirt hmhdlkdvtc
      301 dvhyenyrah ciqqmtsklt qdsrmespip ilplptpdae teklirmkde elrrmqemlq
      361 rmkqqmqdq
//
LOCUS       NP_067037                329 aa            linear   PRI 27-APR-2025
DEFINITION  alpha/beta hydrolase domain-containing protein 17C [Homo sapiens].
ACCESSION   NP_067037 XP_051862 XP_942638
VERSION     NP_067037.1
DBSOURCE    REFSEQ: accession NM_021214.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Tortosa,E., Adolfs,Y., Fukata,M., Pasterkamp,R.J., Kapitein,L.C.
            and Hoogenraad,C.C.
  TITLE     Dynamic Palmitoylation Targets MAP6 to the Axon to Promote
            Microtubule Stabilization during Neuronal Polarization
  JOURNAL   Neuron 94 (4), 809-825 (2017)
   PUBMED   28521134
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Yokoi,N., Fukata,Y., Sekiya,A., Murakami,T., Kobayashi,K. and
            Fukata,M.
  TITLE     Identification of PSD-95 Depalmitoylating Enzymes
  JOURNAL   J Neurosci 36 (24), 6431-6444 (2016)
   PUBMED   27307232
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Lin,D.T. and Conibear,E.
  TITLE     ABHD17 proteins are novel protein depalmitoylases that regulate
            N-Ras palmitate turnover and subcellular localization
  JOURNAL   Elife 4, e11306 (2015)
   PUBMED   26701913
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Ovsyannikova,I.G., Kennedy,R.B., O'Byrne,M., Jacobson,R.M.,
            Pankratz,V.S. and Poland,G.A.
  TITLE     Genome-wide association study of antibody response to smallpox
            vaccine
  JOURNAL   Vaccine 30 (28), 4182-4189 (2012)
   PUBMED   22542470
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023302.9, BC059401.1 and AL390079.1.
            
            On or before Jul 25, 2007 this sequence version replaced
            XP_051862.6, XP_942638.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC059401.1, SRR1163655.259145.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258884.5/ ENSP00000258884.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..329
                     /product="alpha/beta hydrolase domain-containing protein
                     17C"
                     /EC_number="3.1.2.22"
                     /note="abhydrolase domain-containing protein FAM108C1;
                     abhydrolase domain-containing protein 17C; protein
                     ABHD17C; family with sequence similarity 108, member C1"
                     /calculated_mol_wt=35700
     Region          53..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCB6.2)"
     Region          108..326
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
     CDS             1..329
                     /gene="ABHD17C"
                     /gene_synonym="FAM108C1"
                     /coded_by="NM_021214.2:121..1110"
                     /db_xref="CCDS:CCDS45323.1"
                     /db_xref="GeneID:58489"
                     /db_xref="HGNC:HGNC:26925"
                     /db_xref="MIM:617944"
ORIGIN      
        1 mpepgprmng fslgelcwlf ccppcpsria aklaflppep tytvlapeqr gagasapapa
       61 qataaaaaaq papqqpeega gagpgacslh lseradwqys qreldavevf fsrtardnrl
      121 gcmfvrcaps srytllfshg navdlgqmcs fyiglgsrin cnifsydysg ygvssgkpse
      181 knlyadidaa wqalrtrygv speniilygq sigtvptvdl asryecaavi lhsplmsglr
      241 vafpdtrkty cfdafpsidk iskvtspvlv ihgtedevid fshglamyer cpraveplwv
      301 egaghndiel yaqylerlkq fishelpns
//
LOCUS       NP_001355350             506 aa            linear   ROD 27-APR-2025
DEFINITION  complement component C9 isoform 2 [Mus musculus].
ACCESSION   NP_001355350
VERSION     NP_001355350.1
DBSOURCE    REFSEQ: accession NM_001368421.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Roy,T.A., Bubier,J.A., Dickson,P.E., Wilcox,T.D., Ndukum,J.,
            Clark,J.W., Sukoff Rizzo,S.J., Crabbe,J.C., Denegre,J.M.,
            Svenson,K.L., Braun,R.E., Kumar,V., Murray,S.A., White,J.K.,
            Philip,V.M. and Chesler,E.J.
  TITLE     Discovery and validation of genes driving drug-intake and related
            behavioral traits in mice
  JOURNAL   Genes Brain Behav 23 (1), e12875 (2024)
   PUBMED   38164795
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Ueda,Y., Miwa,T., Ito,D., Kim,H., Sato,S., Gullipalli,D., Zhou,L.,
            Golla,M., Song,D., Dunaief,J.L., Palmer,M.B. and Song,W.C.
  TITLE     Differential contribution of C5aR and C5b-9 pathways to renal
            thrombic microangiopathy and macrovascular thrombosis in mice
            carrying an atypical hemolytic syndrome-related factor H mutation
  JOURNAL   Kidney Int 96 (1), 67-79 (2019)
   PUBMED   30910380
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Menny,A., Serna,M., Boyd,C.M., Gardner,S., Joseph,A.P.,
            Morgan,B.P., Topf,M., Brooks,N.J. and Bubeck,D.
  TITLE     CryoEM reveals how the complement membrane attack complex ruptures
            lipid bilayers
  JOURNAL   Nat Commun 9 (1), 5316 (2018)
   PUBMED   30552328
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Qiu,C., Huang,S., Park,J., Park,Y., Ko,Y.A., Seasock,M.J.,
            Bryer,J.S., Xu,X.X., Song,W.C., Palmer,M., Hill,J., Guarnieri,P.,
            Hawkins,J., Boustany-Kari,C.M., Pullen,S.S., Brown,C.D. and
            Susztak,K.
  TITLE     Renal compartment-specific genetic variation analyses identify new
            pathways in chronic kidney disease
  JOURNAL   Nat Med 24 (11), 1721-1731 (2018)
   PUBMED   30275566
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Fu,X., Ju,J., Lin,Z., Xiao,W., Li,X., Zhuang,B., Zhang,T., Ma,X.,
            Li,X., Ma,C., Su,W., Wang,Y., Qin,X. and Liang,S.
  TITLE     Target deletion of complement component 9 attenuates
            antibody-mediated hemolysis and lipopolysaccharide (LPS)-induced
            acute shock in mice
  JOURNAL   Sci Rep 6, 30239 (2016)
   PUBMED   27444648
  REMARK    GeneRIF: these results not only confirm the critical role of C5b-9
            in complement-mediated hemolysis and but also highlight the
            critical role of C5b-9 in inflammasome activation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   8  (residues 1 to 506)
  AUTHORS   Ghesquiere,B., Van Damme,J., Martens,L., Vandekerckhove,J. and
            Gevaert,K.
  TITLE     Proteome-wide characterization of N-glycosylation events by
            diagonal chromatography
  JOURNAL   J Proteome Res 5 (9), 2438-2447 (2006)
   PUBMED   16944957
REFERENCE   9  (residues 1 to 506)
  AUTHORS   Caetano,A.R., Lyons,L.A., Laughlin,T.F., O'Brien,S.J., Murray,J.D.
            and Bowling,A.T.
  TITLE     Equine synteny mapping of comparative anchor tagged sequences
            (CATS) from human Chromosome 5
  JOURNAL   Mamm Genome 10 (11), 1082-1084 (1999)
   PUBMED   10556427
REFERENCE   10 (residues 1 to 506)
  AUTHORS   Stanley,K.K. and Herz,J.
  TITLE     Topological mapping of complement component C9 by recombinant DNA
            techniques suggests a novel mechanism for its insertion into target
            membranes
  JOURNAL   EMBO J 6 (7), 1951-1957 (1987)
   PUBMED   2443347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC105324.11 and AC161196.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189682.83365.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849386, SAMN01164134
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 2.79 cM"
     Protein         1..506
                     /product="complement component C9 isoform 2"
                     /note="complement component C9"
                     /calculated_mol_wt=57306
     Region          1..50
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     Region          59..90
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(61,69,80..81)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(73,76,80,86..87)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            83..87
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          250..464
                     /region_name="MACPF"
                     /note="membrane-attack complex / perforin; smart00457"
                     /db_xref="CDD:214671"
     CDS             1..506
                     /gene="C9"
                     /coded_by="NM_001368421.1:342..1862"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:12279"
                     /db_xref="MGI:MGI:1098282"
ORIGIN      
        1 mspwsnwsec dpclkqrfrs rsilafgqfn gkscvdvlgd rqgceptqec eeiqencgnd
       61 fqcetgrcik rrllcngdnd cgdysdendc dddprtpcrd rvaeeselgl tagyginilg
      121 meplrtpfdn efynglcdrv rdektyyrkp wnvvsliyet kadksfrten ydehlevfka
      181 inrektsnfn adfalkfsat evpekgagev spaehsskpt nisakfkfsy fmgknfrrls
      241 syfsqskkmf vhlrgvvqlg rfvmrnrdvv lrstflddvk alptsyekge yfgfletygt
      301 hystsgslgg qyeivyvldk asmkekgvdl ndvkhclgfn mdlriplqdd lkdasvtasv
      361 nadgciktdn gktvnitrdn iiddvisfir ggtreqaill kekilrgdkt fdktdfanwa
      421 sslanapali sqrmspiynl iplkikdayi kkqnlekave dyidefstkr cypclnggti
      481 illdgqclcs cpmmfrgmac eihqki
//
LOCUS       NP_076422                235 aa            linear   PRI 27-APR-2025
DEFINITION  adenine nucleotide translocase lysine N-methyltransferase isoform 1
            [Homo sapiens].
ACCESSION   NP_076422
VERSION     NP_076422.1
DBSOURCE    REFSEQ: accession NM_023933.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Malecki,J.M., Willemen,H.L.D.M., Pinto,R., Ho,A.Y.Y., Moen,A.,
            Eijkelkamp,N. and Falnes,P.O.
  TITLE     Human FAM173A is a mitochondrial lysine-specific methyltransferase
            that targets adenine nucleotide translocase and affects
            mitochondrial respiration
  JOURNAL   J Biol Chem 294 (31), 11654-11664 (2019)
   PUBMED   31213526
  REMARK    GeneRIF: FAM173A is the long-sought mitochondrial lysine-specific
            methyltransferase responsible for adenine nucleotide translocase
            methylation at Lys-52, and point out the functional significance of
            Lys-52 methylation in adenine nucleotide translocase.
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Daniels,R.J., Peden,J.F., Lloyd,C., Horsley,S.W., Clark,K.,
            Tufarelli,C., Kearney,L., Buckle,V.J., Doggett,N.A., Flint,J. and
            Higgs,D.R.
  TITLE     Sequence, structure and pathology of the fully annotated terminal 2
            Mb of the short arm of human chromosome 16
  JOURNAL   Hum Mol Genet 10 (4), 339-352 (2001)
   PUBMED   11157797
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI597021.1, BC002624.2 and AI492179.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001181.1, BU632070.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000569529.6/ ENSP00000454380.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..235
                     /product="adenine nucleotide translocase lysine
                     N-methyltransferase isoform 1"
                     /note="protein FAM173A; protein N-lysine methyltransferase
                     FAM173A; family with sequence similarity 173 member A;
                     adenine nucleotide translocase lysine N-methyltransferase"
                     /calculated_mol_wt=24999
     Region          1..22
                     /region_name="N-terminal sequence (NTS).
                     /evidence=ECO:0000303|PubMed:31213526"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQD7.1)"
     Site            20..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQD7.1)"
     Region          43..77
                     /region_name="Methyltransferase (MTase).
                     /evidence=ECO:0000303|PubMed:31213526"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQD7.1)"
     Region          43..77
                     /region_name="Pre-methyltransferase (preMT).
                     /evidence=ECO:0000303|PubMed:31213526"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQD7.1)"
     Region          <74..>123
                     /region_name="COG2263"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:441864"
     Region          215..235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQD7.1)"
     CDS             1..235
                     /gene="ANTKMT"
                     /gene_synonym="ANT-KMT; C16orf24; FAM173A"
                     /coded_by="NM_023933.3:130..837"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10423.1"
                     /db_xref="GeneID:65990"
                     /db_xref="HGNC:HGNC:14152"
                     /db_xref="MIM:618566"
ORIGIN      
        1 meqddpveal telrerrlga lellqaaags glaayavwal llqpgfrrvp lrlqvpyvga
       61 sarqvehvls llrgrpgktv dlgsgdgriv laahrcglrp avgyelnpwl valarlhawr
      121 agcagsvcyr rkdlwkvslr dcrnvsvfla psvlplledk lrtelpagar vvsgrfplpt
      181 wqpvtavgeg ldrvwaydvp eggqageaas sripiqaapg pssapipggl isqas
//
LOCUS       NP_056009               1006 aa            linear   PRI 27-APR-2025
DEFINITION  unconventional myosin-Id isoform 1 [Homo sapiens].
ACCESSION   NP_056009 XP_050041
VERSION     NP_056009.1
DBSOURCE    REFSEQ: accession NM_015194.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Yuan,Z., Zhu,X., Xie,X., Wang,C., Gu,H., Yang,J., Fan,L., Xiang,R.,
            Yang,Y. and Tan,Z.
  TITLE     Identification of a novel MYO1D variant associated with laterality
            defects, congenital heart diseases, and sperm defects in humans
  JOURNAL   Front Med 18 (3), 558-564 (2024)
   PUBMED   38684630
  REMARK    GeneRIF: Identification of a novel MYO1D variant associated with
            laterality defects, congenital heart diseases, and sperm defects in
            humans.
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 1006)
  AUTHORS   Benesh,A.E., Fleming,J.T., Chiang,C., Carter,B.D. and Tyska,M.J.
  TITLE     Expression and localization of myosin-1d in the developing nervous
            system
  JOURNAL   Brain Res 1440, 9-22 (2012)
   PUBMED   22284616
REFERENCE   5  (residues 1 to 1006)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   6  (residues 1 to 1006)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   7  (residues 1 to 1006)
  AUTHORS   Hasson,T., Skowron,J.F., Gilbert,D.J., Avraham,K.B., Perry,W.L.,
            Bement,W.M., Anderson,B.L., Sherr,E.H., Chen,Z.Y., Greene,L.A.,
            Ward,D.C., Corey,D.P., Mooseker,M.S., Copeland,N.G. and
            Jenkins,N.A.
  TITLE     Mapping of unconventional myosins in mouse and human
  JOURNAL   Genomics 36 (3), 431-439 (1996)
   PUBMED   8884266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC030602.2, AB018270.2, AC007982.2 and BC030796.2.
            
            On Aug 30, 2004 this sequence version replaced XP_050041.7.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC146763.1, AB018270.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000318217.10/ ENSP00000324527.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..1006
                     /product="unconventional myosin-Id isoform 1"
                     /note="myosin-I gamma; unconventional myosin-Id; protein
                     phosphatase 1, regulatory subunit 108"
                     /calculated_mol_wt=116072
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.4;
                     propagated from UniProtKB/Swiss-Prot (O94832.2)"
     Region          24..682
                     /region_name="MYSc_Myo1"
                     /note="class I myosin, motor domain; cd01378"
                     /db_xref="CDD:276829"
     Site            order(50..53,58,102..109,151..161,383..388)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276829"
     Site            order(50..53,58)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276829"
     Site            102..109
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276829"
     Site            151..161
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276829"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O94832.2)"
     Site            383..388
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276829"
     Site            order(412..423,426..433,435)
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276829"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q5SYD0; propagated from
                     UniProtKB/Swiss-Prot (O94832.2)"
     Region          572..594
                     /region_name="Actin-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00782"
                     /note="propagated from UniProtKB/Swiss-Prot (O94832.2)"
     Site            614..624
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276829"
     Site            order(626..652,669..682)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276829"
     Region          803..996
                     /region_name="Myosin_TH1"
                     /note="Unconventional myosin tail, actin- and
                     lipid-binding; pfam06017"
                     /db_xref="CDD:461801"
     CDS             1..1006
                     /gene="MYO1D"
                     /gene_synonym="myr4; PPP1R108"
                     /coded_by="NM_015194.3:253..3273"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32615.1"
                     /db_xref="GeneID:4642"
                     /db_xref="HGNC:HGNC:7598"
                     /db_xref="MIM:606539"
ORIGIN      
        1 maeqeslefg kadfvlmdtv smpefmanlr lrfekgriyt figevvvsvn pykllniygr
       61 dtieqykgre lyerpphlfa iadaaykamk rrskdtcivi sgesgagkte askyimqyia
      121 aitnpsqrae vervknmllk sncvleafgn aktnrndnss rfgkymdinf dfkgdpiggh
      181 innylleksr vivqqpgers fhsfyqllqg gseqmlrslh lqkslssyny ihvgaqlkss
      241 indaaefrvv adamkvigfk peeiqtvyki laailhlgnl kfvvdgdtpl iengkvvsii
      301 aellstktdm vekallyrtv atgrdiidkq hteqeasygr dafakaiyer lfcwivtrin
      361 diievknydt tihgkntvig vldiygfeif dnnsfeqfci nycneklqql fiqlvlkqeq
      421 eeyqregipw khidyfnnqi ivdlveqqhk giiailddac mnvgkvtdem flealnsklg
      481 khahfssrkl casdkilefd rdfrirhyag dvvysvigfi dknkdtlfqd fkrlmynssn
      541 pvlknmwpeg klsitevtkr pltaatlfkn smialvdnla skepyyvrci kpndkkspqi
      601 fddercrhqv eylgllenvr vrragfafrq tyekflhryk miseftwpnh dlpsdkeavk
      661 kliercgfqd dvaygktkif irtprtlftl eelraqmlir ivlflqkvwr gtlarmrykr
      721 tkaaltiiry yrrykvksyi hevarrfhgv ktmrdygkhv kwpsppkvlr rfeealqtif
      781 nrwrasqlik sipasdlpqv rakvaaveml kgqradlglq rawegnylas kpdtpqtsgt
      841 fvpvanelkr kdkymnvlfs chvrkvnrfs kvedraifvt drhlykmdpt kqykvmktip
      901 lynltglsvs ngkdqlvvfh tkdnkdlivc lfskqpthes rigelvgvlv nhfksekrhl
      961 qvnvtnpvqc slhgkkctvs vetrlnqpqp dftknrsgfi lsvpgn
//
LOCUS       NP_055767                780 aa            linear   PRI 27-APR-2025
DEFINITION  bromo adjacent homology domain-containing 1 protein isoform a [Homo
            sapiens].
ACCESSION   NP_055767
VERSION     NP_055767.3
DBSOURCE    REFSEQ: accession NM_014952.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Yang,Z.Y., Yin,S.P., Ren,Q., Lu,D.W., Tang,T., Li,Y., Sun,Y.Z.,
            Mo,H.B., Yin,T.J., Yi,Z.Y., Zhu,J.P., Zhang,F. and Chen,H.
  TITLE     BAHD1 serves as a critical regulator of breast cancer cell
            proliferation and invasion
  JOURNAL   Breast Cancer 29 (3), 516-530 (2022)
   PUBMED   35048286
  REMARK    GeneRIF: BAHD1 serves as a critical regulator of breast cancer cell
            proliferation and invasion.
            Erratum:[Breast Cancer. 2022 Nov;29(6):1140. doi:
            10.1007/s12282-022-01402-9. PMID: 36112339]
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Fan,H., Guo,Y., Tsai,Y.H., Storey,A.J., Kim,A., Gong,W.,
            Edmondson,R.D., Mackintosh,S.G., Li,H., Byrum,S.D., Tackett,A.J.,
            Cai,L. and Wang,G.G.
  TITLE     A conserved BAH module within mammalian BAHD1 connects H3K27me3 to
            Polycomb gene silencing
  JOURNAL   Nucleic Acids Res 49 (8), 4441-4455 (2021)
   PUBMED   33823544
  REMARK    GeneRIF: A conserved BAH module within mammalian BAHD1 connects
            H3K27me3 to Polycomb gene silencing.
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Xu,P., Scott,D.C., Xu,B., Yao,Y., Feng,R., Cheng,L., Mayberry,K.,
            Wang,Y.D., Bi,W., Palmer,L.E., King,M.T., Wang,H., Li,Y., Fan,Y.,
            Alpi,A.F., Li,C., Peng,J., Papizan,J., Pruett-Miller,S.M.,
            Spallek,R., Bassermann,F., Cheng,Y., Schulman,B.A. and Weiss,M.J.
  TITLE     FBXO11-mediated proteolysis of BAHD1 relieves PRC2-dependent
            transcriptional repression in erythropoiesis
  JOURNAL   Blood 137 (2), 155-167 (2021)
   PUBMED   33156908
  REMARK    GeneRIF: FBXO11-mediated proteolysis of BAHD1 relieves
            PRC2-dependent transcriptional repression in erythropoiesis.
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Pourpre,R., Naudon,L., Meziane,H., Lakisic,G., Jouneau,L.,
            Varet,H., Legendre,R., Wendling,O., Selloum,M., Proux,C.,
            Coppee,J.Y., Herault,Y. and Bierne,H.
  TITLE     BAHD1 haploinsufficiency results in anxiety-like phenotypes in male
            mice
  JOURNAL   PLoS One 15 (5), e0232789 (2020)
   PUBMED   32407325
  REMARK    GeneRIF: The effect of partial BAHD1 deficiency on behavior was
            then evaluated on Bahd1 heterozygous male mice, which have no
            lethal or metabolic phenotypes. Bahd1+/- mice showed anxiety-like
            behavior and reduced prepulse inhibition (PPI) of the startle
            response.
            Erratum:[PLoS One. 2025 Mar 21;20(3):e0320947. doi:
            10.1371/journal.pone.0320947. PMID: 40117285]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Zhu,H., Wan,X., Li,J., Han,L., Bo,X., Chen,W., Lu,C., Shen,Z.,
            Xu,C., Chen,L., Yu,C. and Xu,G.
  TITLE     Computational Prediction and Validation of BAHD1 as a Novel
            Molecule for Ulcerative Colitis
  JOURNAL   Sci Rep 5, 12227 (2015)
   PUBMED   26183847
  REMARK    GeneRIF: computational approaches leveraging public gene expression
            data can be used to infer potential genes or proteins for diseases,
            and BAHD1 might act as an indispensable factor in regulating the
            cellular inflammatory response in UC.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Lebreton,A., Job,V., Ragon,M., Le Monnier,A., Dessen,A., Cossart,P.
            and Bierne,H.
  TITLE     Structural basis for the inhibition of the chromatin repressor
            BAHD1 by the bacterial nucleomodulin LntA
  JOURNAL   mBio 5 (1), e00775-e00713 (2014)
   PUBMED   24449750
  REMARK    GeneRIF: Authors identified a dilysine motif (K180/K181) in the
            elbow region of Listeria monocytogenes LntA and a central
            proline-rich region in human BAHD1 as crucial for the direct
            LntA-BAHD1 interaction.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Lebreton,A., Lakisic,G., Job,V., Fritsch,L., Tham,T.N., Camejo,A.,
            Mattei,P.J., Regnault,B., Nahori,M.A., Cabanes,D., Gautreau,A.,
            Ait-Si-Ali,S., Dessen,A., Cossart,P. and Bierne,H.
  TITLE     A bacterial protein targets the BAHD1 chromatin complex to
            stimulate type III interferon response
  JOURNAL   Science 331 (6022), 1319-1321 (2011)
   PUBMED   21252314
  REMARK    GeneRIF: findings show a Listeria virulence factor, lmo0438/lntA,
            could target the chromatin repressor BAHD1 in host cell nucleus to
            activate interferon-stimulated genes; LntA-BAHD1 interplay may
            modulate IFN-lambda-mediated immune response to control host
            colonization
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Bierne,H., Tham,T.N., Batsche,E., Dumay,A., Leguillou,M.,
            Kerneis-Golsteyn,S., Regnault,B., Seeler,J.S., Muchardt,C.,
            Feunteun,J. and Cossart,P.
  TITLE     Human BAHD1 promotes heterochromatic gene silencing
  JOURNAL   Proc Natl Acad Sci U S A 106 (33), 13826-13831 (2009)
   PUBMED   19666599
  REMARK    GeneRIF: BAHD1 acts as a silencer by recruiting at specific
            promoters a set of proteins that coordinate heterochromatin
            assembly
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC013356.8, HY041603.1, BC022782.2, AB023162.1 and BU740533.1.
            
            On Apr 3, 2007 this sequence version replaced NP_055767.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022782.2, SRR9304715.349738.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000416165.6/ ENSP00000396976.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1"
     Protein         1..780
                     /product="bromo adjacent homology domain-containing 1
                     protein isoform a"
                     /note="bromo adjacent homology domain-containing 1
                     protein; BAH domain-containing protein 1"
                     /calculated_mol_wt=84521
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBE0.2)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TBE0.2)"
     Region          78..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBE0.2)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TBE0.2)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TBE0.2)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8TBE0.2)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TBE0.2)"
     Region          320..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBE0.2)"
     Region          514..589
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBE0.2)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TBE0.2)"
     Region          623..733
                     /region_name="BAH_BAHCC1"
                     /note="BAH, or Bromo Adjacent Homology domain, as present
                     in mammalian BAHCC1 and similar proteins. BAHCC1 stands
                     for BAH domain and coiled-coil containing 1. BAH domains
                     are found in a variety of proteins playing roles in
                     transcriptional silencing and the...; cd04714"
                     /db_xref="CDD:240065"
     Region          731..751
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBE0.2)"
     CDS             1..780
                     /gene="BAHD1"
                     /coded_by="NM_014952.5:331..2673"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10058.1"
                     /db_xref="GeneID:22893"
                     /db_xref="HGNC:HGNC:29153"
                     /db_xref="MIM:613880"
ORIGIN      
        1 mthtrrkslp mlssgltgrr eplqmedsnm eqgvegvepg mpespghltg rrknyplrkr
       61 plvpekpkac kvlltrlenv agprsadead elppdlpkpp spapssedpg laqprkrrla
      121 slnaealnnl lleredtssl agtrrsragd phrsrdrdra tggwssskkr prlgdlgggs
      181 rdlspepapd egprrdgdpa pkrlaslnaa aflklsqere lplrlpraha evdgrstepp
      241 apkaprpkwp kvngknypka wqgassgeaa gppgwqgcpd epwpsatpcg psvqpshqpl
      301 skalesplgl rphlpllmgg qaalkpepgr pgeespapkq elhqpsfptp qlsplpmpgn
      361 padynglcvg peltalgsfy lycgqeglqc ggyspcpmlp egklspvaap heeglllaps
      421 svpsgtpfqh ppwgssrycs sedtgvngys icgvlplsvt hagttcggcp ykmpfaaegc
      481 rslgqlefpl peaghpaspa hpllgcpvps vppaaepvph lqtptsepqt varacpqsak
      541 ppsgsksglr tgsscrhtar skaarrpshp kqprvqrprp rrrrrrrtng wvpvgaacek
      601 avyvldepep airksyqave rhgetirvrd tvllksgprk tstpyvakis alwenpesge
      661 lmmsllwyyr pehlqggrsp smheplqnev fasrhqdqns vacieekcyv ltfaeycrfc
      721 amakrrgegl psrktalvpp sadystpphr tvpedtdpel vflcrhvydf rhgrilknpq
//
LOCUS       NP_003092                550 aa            linear   PRI 27-APR-2025
DEFINITION  sterol O-acyltransferase 1 isoform 1 [Homo sapiens].
ACCESSION   NP_003092
VERSION     NP_003092.4
DBSOURCE    REFSEQ: accession NM_003101.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Hong,Y., Abudukeremu,X., She,F. and Chen,Y.
  TITLE     SOAT1 in gallbladder cancer: Clinicopathological significance and
            avasimibe therapeutics
  JOURNAL   J Biochem Mol Toxicol 38 (6), e23733 (2024)
   PUBMED   38770938
  REMARK    GeneRIF: SOAT1 in gallbladder cancer: Clinicopathological
            significance and avasimibe therapeutics.
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Fu,R., Xue,W., Liang,J., Li,X., Zheng,J., Wang,L., Zhang,M. and
            Meng,J.
  TITLE     SOAT1 regulates cholesterol metabolism to induce EMT in
            hepatocellular carcinoma
  JOURNAL   Cell Death Dis 15 (5), 325 (2024)
   PUBMED   38724499
  REMARK    GeneRIF: SOAT1 regulates cholesterol metabolism to induce EMT in
            hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Farhat,N.Y., Alexander,D., McKee,K., Iben,J., Rodriguez-Gil,J.L.,
            Wassif,C.A., Cawley,N.X., Balch,W.E. and Porter,F.D.
  TITLE     Sterol O-Acyltransferase 1 (SOAT1): A Genetic Modifier of
            Niemann-Pick Disease, Type C1
  JOURNAL   Int J Mol Sci 25 (8), 4217 (2024)
   PUBMED   38673803
  REMARK    GeneRIF: Sterol O-Acyltransferase 1 (SOAT1): A Genetic Modifier of
            Niemann-Pick Disease, Type C1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Wang,Z., Wang,M., Zhang,M., Xu,K., Zhang,X., Xie,Y., Zhang,Y.,
            Chang,C., Li,X., Sun,A. and He,F.
  TITLE     High-affinity SOAT1 ligands remodeled cholesterol metabolism
            program to inhibit tumor growth
  JOURNAL   BMC Med 20 (1), 292 (2022)
   PUBMED   35941608
  REMARK    GeneRIF: High-affinity SOAT1 ligands remodeled cholesterol
            metabolism program to inhibit tumor growth.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Cases,S., Novak,S., Zheng,Y.W., Myers,H.M., Lear,S.R., Sande,E.,
            Welch,C.B., Lusis,A.J., Spencer,T.A., Krause,B.R., Erickson,S.K.
            and Farese,R.V. Jr.
  TITLE     ACAT-2, a second mammalian acyl-CoA:cholesterol acyltransferase.
            Its cloning, expression, and characterization
  JOURNAL   J Biol Chem 273 (41), 26755-26764 (1998)
   PUBMED   9756919
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Yang,H., Cromley,D., Wang,H., Billheimer,J.T. and Sturley,S.L.
  TITLE     Functional expression of a cDNA to human acyl-coenzyme
            A:cholesterol acyltransferase in yeast. Species-dependent substrate
            specificity and inhibitor sensitivity
  JOURNAL   J Biol Chem 272 (7), 3980-3985 (1997)
   PUBMED   9020103
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Chang,C.C., Noll,W.W., Nutile-McMenemy,N., Lindsay,E.A.,
            Baldini,A., Chang,W. and Chang,T.Y.
  TITLE     Localization of acyl coenzyme A:cholesterol acyltransferase gene to
            human chromosome 1q25
  JOURNAL   Somat Cell Mol Genet 20 (1), 71-74 (1994)
   PUBMED   8197480
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Chang,C.C., Huh,H.Y., Cadigan,K.M. and Chang,T.Y.
  TITLE     Molecular cloning and functional expression of human acyl-coenzyme
            A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary
            cells
  JOURNAL   J Biol Chem 268 (28), 20747-20755 (1993)
   PUBMED   8407899
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Cadigan,K.M., Chang,C.C. and Chang,T.Y.
  TITLE     Isolation of Chinese hamster ovary cell lines expressing human
            acyl-coenzyme A/cholesterol acyltransferase activity
  JOURNAL   J Cell Biol 108 (6), 2201-2210 (1989)
   PUBMED   2738092
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Cadigan,K.M., Heider,J.G. and Chang,T.Y.
  TITLE     Isolation and characterization of Chinese hamster ovary cell
            mutants deficient in acyl-coenzyme A:cholesterol acyltransferase
            activity
  JOURNAL   J Biol Chem 263 (1), 274-282 (1988)
   PUBMED   3335499
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC344271.1, BC028940.1,
            AL833625.1, AL451075.15 and BQ182606.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 1, 2004 this sequence version replaced NP_003092.3.
            
            Summary: The protein encoded by this gene belongs to the
            acyltransferase family. It is located in the endoplasmic reticulum,
            and catalyzes the formation of fatty acid-cholesterol esters. This
            gene has been implicated in the formation of beta-amyloid and
            atherosclerotic plaques by controlling the equilibrium between free
            cholesterol and cytoplasmic cholesteryl esters. Alternatively
            spliced transcript variants have been found for this gene.
            [provided by RefSeq, Nov 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.204046.1,
                                           SRR1660807.233547.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000367619.8/
                                                  ENSP00000356591.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..550
                     /product="sterol O-acyltransferase 1 isoform 1"
                     /EC_number="2.3.1.26"
                     /note="sterol O-acyltransferase (acyl-Coenzyme A:
                     cholesterol acyltransferase) 1; acyl-coenzyme
                     A:cholesterol acyltransferase 1"
                     /calculated_mol_wt=64604
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P35610.3)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35610.3)"
     Site            139..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     Region          171..520
                     /region_name="MBOAT"
                     /note="membrane-bound O-acyltransferase family; pfam03062"
                     /db_xref="CDD:427117"
     Site            181..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     Site            219..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     Site            253..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     Site            320..352
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     Site            370..395
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     Region          403..409
                     /region_name="FYXDWWN motif.
                     /evidence=ECO:0000303|PubMed:32433614"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     Site            444..468
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     Site            475..490
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     Site            497..528
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35610.3)"
     CDS             1..550
                     /gene="SOAT1"
                     /gene_synonym="ACACT; ACAT; ACAT-1; ACAT1; SOAT; STAT"
                     /coded_by="NM_003101.6:149..1801"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1330.1"
                     /db_xref="GeneID:6646"
                     /db_xref="HGNC:HGNC:11177"
                     /db_xref="MIM:102642"
ORIGIN      
        1 mvgeekmslr nrlsksrenp eededqrnpa kesletpsng ridikqliak kikltaeaee
       61 lkpffmkevg shfddfvtnl ieksasldng gcalttfsvl egeknnhrak dlrappeqgk
      121 ifiarrslld ellevdhirt iyhmfialli lfilstlvvd yidegrlvle fsllsyafgk
      181 fptvvwtwwi mflstfsvpy flfqhwatgy sksshplirs lfhgflfmif qigvlgfgpt
      241 yvvlaytlpp asrfiiifeq irfvmkahsf vrenvprvln sakeksstvp iptvnqylyf
      301 lfaptliyrd syprnptvrw gyvamkfaqv fgcffyvyyi ferlcaplfr nikqepfsar
      361 vlvlcvfnsi lpgvlilflt ffaflhcwln afaemlrfgd rmfykdwwns tsysnyyrtw
      421 nvvvhdwlyy yaykdflwff skrfksaaml avfavsavvh eyalavclsf fypvlfvlfm
      481 ffgmafnfiv ndsrkkpiwn vlmwtslflg ngvllcfysq ewyarqhcpl knptfldyvr
      541 prswtcryvf
//
LOCUS       NP_006654                828 aa            linear   PRI 27-APR-2025
DEFINITION  relA-associated inhibitor [Homo sapiens].
ACCESSION   NP_006654
VERSION     NP_006654.2
DBSOURCE    REFSEQ: accession NM_006663.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Tulbah,S., Alruwaili,N., Alhashem,A., Aljohany,A., Alhadeq,F.,
            Brotons,D.C.A., Alwadai,A. and Al-Hassnan,Z.N.
  TITLE     Variable phenotype of a null PPP1R13L allele in children with
            dilated cardiomyopathy
  JOURNAL   Am J Med Genet A 194 (1), 59-63 (2024)
   PUBMED   37698259
  REMARK    GeneRIF: Variable phenotype of a null PPP1R13L allele in children
            with dilated cardiomyopathy.
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Yin,J., Wang,C., Vogel,U., Ma,Y., Zhang,Y., Wang,H., Sun,Z. and
            Du,S.
  TITLE     Common variants of pro-inflammatory gene IL1B and interactions with
            PPP1R13L and POLR1G in relation to lung cancer among Northeast
            Chinese
  JOURNAL   Sci Rep 13 (1), 7352 (2023)
   PUBMED   37147350
  REMARK    GeneRIF: Common variants of pro-inflammatory gene IL1B and
            interactions with PPP1R13L and POLR1G in relation to lung cancer
            among Northeast Chinese.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Zhou,M., Dong,J., Huang,J., Ye,W., Zheng,Z., Huang,K., Pan,Y.,
            Cen,J., Liang,Y., Shu,G., Ye,S., Lu,X. and Zhang,J.
  TITLE     Chitosan-Gelatin-EGCG Nanoparticle-Meditated LncRNA TMEM44-AS1
            Silencing to Activate the P53 Signaling Pathway for the Synergistic
            Reversal of 5-FU Resistance in Gastric Cancer
  JOURNAL   Adv Sci (Weinh) 9 (22), e2105077 (2022)
   PUBMED   35717675
  REMARK    GeneRIF: Chitosan-Gelatin-EGCG Nanoparticle-Meditated LncRNA
            TMEM44-AS1 Silencing to Activate the P53 Signaling Pathway for the
            Synergistic Reversal of 5-FU Resistance in Gastric Cancer.
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Zhao,D., Zheng,S., Wang,X., Liu,H., Zhao,K., Li,L. and Hu,Y.
  TITLE     iASPP is essential for HIF-1alpha stabilization to promote
            angiogenesis and glycolysis via attenuating VHL-mediated protein
            degradation
  JOURNAL   Oncogene 41 (13), 1944-1958 (2022)
   PUBMED   35169254
  REMARK    GeneRIF: iASPP is essential for HIF-1alpha stabilization to promote
            angiogenesis and glycolysis via attenuating VHL-mediated protein
            degradation.
REFERENCE   5  (residues 1 to 828)
  AUTHORS   Yin,J., Hou,W., Vogel,U., Li,X., Ma,Y., Wang,C., Wang,H. and Sun,Z.
  TITLE     TP53 common variants and interaction with PPP1R13L and CD3EAP SNPs
            and lung cancer risk and smoking behavior in a Chinese population
  JOURNAL   Biomed J 45 (1), 169-178 (2022)
   PUBMED   35351459
  REMARK    GeneRIF: TP53 common variants and interaction with PPP1R13L and
            CD3EAP SNPs and lung cancer risk and smoking behavior in a Chinese
            population.
REFERENCE   6  (residues 1 to 828)
  AUTHORS   Slee,E.A., Gillotin,S., Bergamaschi,D., Royer,C., Llanos,S.,
            Ali,S., Jin,B., Trigiante,G. and Lu,X.
  TITLE     The N-terminus of a novel isoform of human iASPP is required for
            its cytoplasmic localization
  JOURNAL   Oncogene 23 (56), 9007-9016 (2004)
   PUBMED   15489900
REFERENCE   7  (residues 1 to 828)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   8  (residues 1 to 828)
  AUTHORS   Bergamaschi,D., Samuels,Y., O'Neil,N.J., Trigiante,G., Crook,T.,
            Hsieh,J.K., O'Connor,D.J., Zhong,S., Campargue,I., Tomlinson,M.L.,
            Kuwabara,P.E. and Lu,X.
  TITLE     iASPP oncoprotein is a key inhibitor of p53 conserved from worm to
            human
  JOURNAL   Nat Genet 33 (2), 162-167 (2003)
   PUBMED   12524540
REFERENCE   9  (residues 1 to 828)
  AUTHORS   Takada,N., Sanda,T., Okamoto,H., Yang,J.P., Asamitsu,K., Sarol,L.,
            Kimura,G., Uranishi,H., Tetsuka,T. and Okamoto,T.
  TITLE     RelA-associated inhibitor blocks transcription of human
            immunodeficiency virus type 1 by inhibiting NF-kappaB and Sp1
            actions
  JOURNAL   J Virol 76 (16), 8019-8030 (2002)
   PUBMED   12134007
  REMARK    GeneRIF: Effect of RAI on transcription and replication of human
            immunodeficiency virus type 1 (HIV-1).
REFERENCE   10 (residues 1 to 828)
  AUTHORS   Yang,J.P., Hori,M., Sanda,T. and Okamoto,T.
  TITLE     Identification of a novel inhibitor of nuclear factor-kappaB,
            RelA-associated inhibitor
  JOURNAL   J Biol Chem 274 (22), 15662-15670 (1999)
   PUBMED   10336463
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092309.3 and BC032298.1.
            
            On May 3, 2005 this sequence version replaced NP_006654.1.
            
            Summary: IASPP is one of the most evolutionarily conserved
            inhibitors of p53 (TP53; MIM 191170), whereas ASPP1 (MIM 606455)
            and ASPP2 (MIM 602143) are activators of p53.[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032298.1, SRR7346977.1137704.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360957.10/ ENSP00000354218.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..828
                     /product="relA-associated inhibitor"
                     /note="retinoic acid induced 4; NFkB interacting protein
                     1; inhibitor of apoptosis stimulating protein of p53;
                     protein iASPP; PPP1R13B-like protein; inhibitor of ASPP
                     protein; protein phosphatase 1, regulatory (inhibitor)
                     subunit 13 like"
                     /calculated_mol_wt=88960
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Region          45..267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Region          <75..507
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            137
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q5I1X5; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            142
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q5I1X5; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            144
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q5I1X5; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            160
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q5I1X5; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            167
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            180
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            205
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q5I1X5; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Region          286..371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Region          393..506
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Region          520..619
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Region          <605..>730
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          631..657
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(632..633,636..638,640..641,645,648,657,659,661,
                     665..666,669..671,673..674,678,681,690,692,694,698..699,
                     702..704,706..707,711,714)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          659..691
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Region          659..690
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          692..724
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUF5.4)"
     Region          692..721
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          761..817
                     /region_name="SH3_iASPP"
                     /note="Src Homology 3 (SH3) domain of Inhibitor of ASPP
                     protein (iASPP); cd11952"
                     /db_xref="CDD:212885"
     Site            order(769,772..773,775..776,794..795,797..798,809,811,813)
                     /site_type="other"
                     /note="p53 binding site [polypeptide binding]"
                     /db_xref="CDD:212885"
     CDS             1..828
                     /gene="PPP1R13L"
                     /gene_synonym="ARCME; CMAEA; IASPP; NKIP1; RAI; RAI4"
                     /coded_by="NM_006663.4:93..2579"
                     /db_xref="CCDS:CCDS33050.1"
                     /db_xref="GeneID:10848"
                     /db_xref="HGNC:HGNC:18838"
                     /db_xref="MIM:607463"
ORIGIN      
        1 mdseafqsar dfldmnfqsl amkhmdlkqm eldtaaakvd eltkqleslw sdspappgpq
       61 agppsrppry ssssipepfg srgsprkaat dgadtpfgrs esaptlhpys plspkgrpss
      121 prtplylqpd aygsldrats prprafdgag sslgrapspr pgpgplrqqg pptpfdflgr
      181 agsprgspla egpqaffper gpsprppata ydapasafgs sllgsggsaf applraqddl
      241 tlrrrppkaw nesdldvaye kkpsqtasye rldvfarpas pslqllpwre ssldglggtg
      301 kdnltsatlp rnykvsplas drrsdagsyr rslgsagpsg tlprswqpvs ripmppsspq
      361 prgaprqrpi plsmifklqn afwehgasra mlpgsplftr apppklqpqp qpqpqpqsqp
      421 qpqlppqpqt qpqtptpapq hpqqtwppvn egppkpptel epepeiegll tpvleagdvd
      481 egpvarplsp trlqpalppe aqsvpeleev arvlaeiprp lkrrgsmeqa pavalppthk
      541 kqyqqiisrl fhrhggpgpg gpepelspit egsearagpp apappapipp papsqssppe
      601 qpqsmemrsv lrkagsprka rrarlnplvl lldaaltgel evvqqavkem ndpsqpneeg
      661 italhnaicg anysivdfli taganvnspd shgwtplhca ascndtvicm alvqhgaaif
      721 attlsdgata fekcdpyreg yadcatylad veqsmglmns gavyalwdys aefgdelsfr
      781 egesvtvlrr dgpeetdwww aalhgqegyv prnyfglfpr vkpqrskv
//
LOCUS       NP_068777                488 aa            linear   PRI 27-APR-2025
DEFINITION  H2.0-like homeobox protein [Homo sapiens].
ACCESSION   NP_068777
VERSION     NP_068777.1
DBSOURCE    REFSEQ: accession NM_021958.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Nagel,S., Uphoff,C.C., Dirks,W.G., Pommerenke,C., Meyer,C. and
            Drexler,H.G.
  TITLE     Epstein-Barr virus (EBV) activates NKL homeobox gene HLX in DLBCL
  JOURNAL   PLoS One 14 (5), e0216898 (2019)
   PUBMED   31141539
  REMARK    GeneRIF: Epstein-Barr virus (EBV) activates NKL homeobox gene HLX
            in DLBCL.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Piragyte,I., Clapes,T., Polyzou,A., Klein Geltink,R.I.,
            Lefkopoulos,S., Yin,N., Cauchy,P., Curtis,J.D., Klaeyle,L.,
            Langa,X., Beckmann,C.C.A., Wlodarski,M.W., Muller,P., Van Essen,D.,
            Rambold,A., Kapp,F.G., Mione,M., Buescher,J.M., Pearce,E.L.,
            Polyzos,A. and Trompouki,E.
  TITLE     A metabolic interplay coordinated by HLX regulates myeloid
            differentiation and AML through partly overlapping pathways
  JOURNAL   Nat Commun 9 (1), 3090 (2018)
   PUBMED   30082823
  REMARK    GeneRIF: HLX has a role in coordinating metabolic interplay
            regulates myeloid differentiation both in zebrafish and human
            hematopoietic stem and progenitor cells and in acute myeloid
            leukemia through partly overlapping pathways
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Yuen,N., Brennecke,S.P., Umstad,M.P., Yong,H.E.J., Borg,A.J.,
            Rajaraman,G., Kalionis,B. and Murthi,P.
  TITLE     Expression of Homeobox Gene HLX and its Downstream Target Genes are
            Altered in Placentae From Discordant Twin Pregnancies
  JOURNAL   Twin Res Hum Genet 21 (1), 42-50 (2018)
   PUBMED   29212571
  REMARK    GeneRIF: An important association between HLX transcription factor
            expression and abnormal human placental development in discordant
            twin pregnancies.
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Farrell,S.A., Sodhi,S., Marshall,C.R., Guerin,A., Slavotinek,A.,
            Paton,T., Chong,K., Sirkin,W.L., Scherer,S.W., Berube-Simard,F.A.
            and Pilon,N.
  TITLE     HLX is a candidate gene for a pattern of anomalies associated with
            congenital diaphragmatic hernia, short bowel, and asplenia
  JOURNAL   Am J Med Genet A 173 (11), 3070-3074 (2017)
   PUBMED   28898547
  REMARK    GeneRIF: HLX is a homeobox transcription factor gene which is
            relatively conserved across species. Hlx homozygous null mice have
            a short bowel and reduced muscle cells in the diaphragm, closely
            resembling the anomalies in the two fetuses and we therefore
            suggest that the HLX mutation in this family could explain the
            fetal findings
REFERENCE   6  (residues 1 to 488)
  AUTHORS   Najfeld,V., Menninger,J., Ballard,S.G., Deguchi,Y., Ward,D.C. and
            Kehrl,J.H.
  TITLE     Two diverged human homeobox genes involved in the differentiation
            of human hematopoietic progenitors map to chromosome 1, bands
            q41-42.1
  JOURNAL   Genes Chromosomes Cancer 5 (4), 343-347 (1992)
   PUBMED   1283323
REFERENCE   7  (residues 1 to 488)
  AUTHORS   Deguchi,Y., Kirschenbaum,A. and Kehrl,J.H.
  TITLE     A diverged homeobox gene is involved in the proliferation and
            lineage commitment of human hematopoietic progenitors and highly
            expressed in acute myelogenous leukemia
  JOURNAL   Blood 79 (11), 2841-2848 (1992)
   PUBMED   1375114
REFERENCE   8  (residues 1 to 488)
  AUTHORS   Deguchi,Y., Thevenin,C. and Kehrl,J.H.
  TITLE     Stable expression of HB24, a diverged human homeobox gene, in T
            lymphocytes induces genes involved in T cell activation and growth
  JOURNAL   J Biol Chem 267 (12), 8222-8229 (1992)
   PUBMED   1349016
REFERENCE   9  (residues 1 to 488)
  AUTHORS   Deguchi,Y., Moroney,J.F., Wilson,G.L., Fox,C.H., Winter,H.S. and
            Kehrl,J.H.
  TITLE     Cloning of a human homeobox gene that resembles a diverged
            Drosophila homeobox gene and is expressed in activated lymphocytes
  JOURNAL   New Biol 3 (4), 353-363 (1991)
   PUBMED   1676597
REFERENCE   10 (residues 1 to 488)
  AUTHORS   Allen,J.D., Lints,T., Jenkins,N.A., Copeland,N.G., Strasser,A.,
            Harvey,R.P. and Adams,J.M.
  TITLE     Novel murine homeo box gene on chromosome 1 expressed in specific
            hematopoietic lineages and during embryogenesis
  JOURNAL   Genes Dev 5 (4), 509-520 (1991)
   PUBMED   1672660
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA951303.1 and BC033808.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127923.1, BC007294.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366903.8/ ENSP00000355870.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..488
                     /product="H2.0-like homeobox protein"
                     /note="H2.0-like homeo box-1; H2.0-like homeobox 1;
                     homeobox protein HB24; homeobox protein HLX1"
                     /calculated_mol_wt=50658
     Region          118..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14774.3)"
     Region          273..333
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          331..488
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14774.3)"
     CDS             1..488
                     /gene="HLX"
                     /gene_synonym="HB24; HLX1"
                     /coded_by="NM_021958.4:416..1882"
                     /db_xref="CCDS:CCDS1527.1"
                     /db_xref="GeneID:3142"
                     /db_xref="HGNC:HGNC:4978"
                     /db_xref="MIM:142995"
ORIGIN      
        1 mfaaglapfy asnfslwsaa ycssagpggc sfpldpaavk kpsfciadil hagvgdlgaa
       61 peglagasaa altahlgsvh phasfqaaar splrptpvva psevpagfpq rlsplsaayh
      121 hhhpqqqqqq qqpqqqqppp ppragalqpp asgtrvvpnp hhsgsapaps skdlkfgidr
      181 ilsaefdpkv kegntlrdlt slltggrpag vhlsglqpsa gqffasldpi neasailspl
      241 nsnprnsvqh qfqdtfpgpy avltkdtmpq tykrkrswsr avfsnlqrkg lekrfeiqky
      301 vtkpdrkqla amlgltdaqv kvwfqnrrmk wrhskeaqaq kdkdkeagek psggapaadg
      361 eqderspsrs egeaesessd sesldmapsd tertegsers lhqttvikap vtgalitass
      421 agsggssggg gnsfsfssas slsssstsag casslgggga sellpatqpt assapkspep
      481 aqgalgcl
//
LOCUS       NP_001349                795 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DHX15 [Homo sapiens].
ACCESSION   NP_001349
VERSION     NP_001349.2
DBSOURCE    REFSEQ: accession NM_001358.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Dostalkova,A., Krizova,I., Junkova,P., Rackova,J., Kapisheva,M.,
            Novotny,R., Danda,M., Zvonarova,K., Sinkovec,L., Vecerkova,K.,
            Bednarova,L., Ruml,T. and Rumlova,M.
  TITLE     Unveiling the DHX15-G-patch interplay in retroviral RNA packaging
  JOURNAL   Proc Natl Acad Sci U S A 121 (40), e2407990121 (2024)
   PUBMED   39320912
  REMARK    GeneRIF: Unveiling the DHX15-G-patch interplay in retroviral RNA
            packaging.
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Kanwal,N., Krogh,N., Memet,I., Lemus-Diaz,N., Thome,C.C.,
            Welp,L.M., Mizi,A., Hackert,P., Papantonis,A., Urlaub,H.,
            Nielsen,H., Bohnsack,K.E. and Bohnsack,M.T.
  TITLE     GPATCH4 regulates rRNA and snRNA 2'-O-methylation in both
            DHX15-dependent and DHX15-independent manners
  JOURNAL   Nucleic Acids Res 52 (4), 1953-1974 (2024)
   PUBMED   38113271
  REMARK    GeneRIF: GPATCH4 regulates rRNA and snRNA 2'-O-methylation in both
            DHX15-dependent and DHX15-independent manners.
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Feng,Q., Krick,K., Chu,J. and Burge,C.B.
  TITLE     Splicing quality control mediated by DHX15 and its G-patch
            activator SUGP1
  JOURNAL   Cell Rep 42 (10), 113223 (2023)
   PUBMED   37805921
  REMARK    GeneRIF: Splicing quality control mediated by DHX15 and its G-patch
            activator SUGP1.
REFERENCE   4  (residues 1 to 795)
  AUTHORS   Fan,L., Guo,X., Zhang,J., Wang,Y., Wang,J. and Li,Y.
  TITLE     Relationship between DHX15 expression and survival in colorectal
            cancer
  JOURNAL   Rev Esp Enferm Dig 115 (5), 234-240 (2023)
   PUBMED   36177832
  REMARK    GeneRIF: Relationship between DHX15 expression and survival in
            colorectal cancer.
REFERENCE   5  (residues 1 to 795)
  AUTHORS   Zhang,J., Huang,J., Xu,K., Xing,P., Huang,Y., Liu,Z., Tong,L. and
            Manley,J.L.
  TITLE     DHX15 is involved in SUGP1-mediated RNA missplicing by mutant SF3B1
            in cancer
  JOURNAL   Proc Natl Acad Sci U S A 119 (49), e2216712119 (2022)
   PUBMED   36459648
  REMARK    GeneRIF: DHX15 is involved in SUGP1-mediated RNA missplicing by
            mutant SF3B1 in cancer.
REFERENCE   6  (residues 1 to 795)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
REFERENCE   7  (residues 1 to 795)
  AUTHORS   Fouraux,M.A., Kolkman,M.J., Van der Heijden,A., De Jong,A.S., Van
            Venrooij,W.J. and Pruijn,G.J.
  TITLE     The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a
            putative DEAH-box RNA helicase
  JOURNAL   RNA 8 (11), 1428-1443 (2002)
   PUBMED   12458796
REFERENCE   8  (residues 1 to 795)
  AUTHORS   Luking,A., Stahl,U. and Schmidt,U.
  TITLE     The protein family of RNA helicases
  JOURNAL   Crit Rev Biochem Mol Biol 33 (4), 259-296 (1998)
   PUBMED   9747670
  REMARK    Review article
REFERENCE   9  (residues 1 to 795)
  AUTHORS   Imamura,O., Sugawara,M. and Furuichi,Y.
  TITLE     Cloning and characterization of a putative human RNA helicase gene
            of the DEAH-box protein family
  JOURNAL   Biochem Biophys Res Commun 240 (2), 335-340 (1997)
   PUBMED   9388478
REFERENCE   10 (residues 1 to 795)
  AUTHORS   Ono,Y., Ohno,M. and Shimura,Y.
  TITLE     Identification of a putative RNA helicase (HRH1), a human homolog
            of yeast Prp22
  JOURNAL   Mol Cell Biol 14 (11), 7611-7620 (1994)
   PUBMED   7935475
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU158645.1, BC035974.1 and
            AA771922.1.
            
            On Jul 1, 2005 this sequence version replaced NP_001349.1.
            
            Summary: The protein encoded by this gene is a putative
            ATP-dependent RNA helicase implicated in pre-mRNA splicing.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB001636.1, BC035974.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336812.5/ ENSP00000336741.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.2"
     Protein         1..795
                     /product="ATP-dependent RNA helicase DHX15"
                     /EC_number="3.6.4.13"
                     /note="DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 15;
                     putative pre-mRNA-splicing factor ATP-dependent RNA
                     helicase DHX15; RNA helicase 2; DEAD/H box-15; DEAH box
                     protein 15; ATP-dependent RNA helicase #46; DEAH
                     (Asp-Glu-Ala-His) box polypeptide 15; DEAH
                     (Asp-Glu-Ala-His) box helicase 15; splicing factor Prp43"
                     /calculated_mol_wt=90802
     Region          1..108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43143.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43143.2)"
     Region          136..>763
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
     Region          260..263
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (O43143.2)"
     Site            488
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O43143.2)"
     CDS             1..795
                     /gene="DHX15"
                     /gene_synonym="DBP1; DDX15; hPrp43; PRP43; PRPF43;
                     PrPp43p"
                     /coded_by="NM_001358.3:162..2549"
                     /db_xref="CCDS:CCDS33966.1"
                     /db_xref="GeneID:1665"
                     /db_xref="HGNC:HGNC:2738"
                     /db_xref="MIM:603403"
ORIGIN      
        1 mskrhrldlg edypsgkkra gtdgkdrdrd rdredrskdr drerdrgdre rerekekeke
       61 lrastnamli saglpplkas hsahsthsah sthsthsahs thaghaghts lpqcinpftn
      121 lphtpryydi lkkrlqlpvw eykdrftdil vrhqsfvlvg etgsgkttqi pqwcveymrs
      181 lpgpkrgvac tqprrvaams vaqrvademd vmlgqevgys irfedcssak tilkymtdgm
      241 llreamndpl lerygviild eahertlatd ilmgvlkevv rqrsdlkviv msatldagkf
      301 qiyfdncpll tipgrthpve ifytpeperd yleaairtvi qihmceeeeg dlllfltgqe
      361 eideackrik revddlgpev gdikiiplys tlppqqqqri feppppkkqn gaigrkvvvs
      421 tniaetslti dgvvfvidpg fakqkvynpr irvesllvta iskasaqqra gragrtrpgk
      481 cfrlytekay ktemqdntyp eilrsnlgsv vlqlkklgid dlvhfdfmdp papetlmral
      541 ellnylaaln ddgdltelgs mmaefpldpq lakmviascd yncsnevlsi tamlsvpqcf
      601 vrpteakkaa deakmrfahi dgdhltllnv yhafkqnhes vqwcydnfin yrslmsadnv
      661 rqqlsrimdr fnlprrstdf tsrdyyinir kalvtgyfmq vahlertghy ltvkdnqvvq
      721 lhpstvldhk pewvlynefv lttknyirtc tdikpewlvk iapqyydmsn fpqceakrql
      781 driiaklqsk eysqy
//
LOCUS       NP_065982                787 aa            linear   PRI 27-APR-2025
DEFINITION  E3 SUMO-protein ligase KIAA1586 isoform a [Homo sapiens].
ACCESSION   NP_065982 XP_166451
VERSION     NP_065982.1
DBSOURCE    REFSEQ: accession NM_020931.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Eisenhardt,N., Chaugule,V.K., Koidl,S., Droescher,M., Dogan,E.,
            Rettich,J., Sutinen,P., Imanishi,S.Y., Hofmann,K., Palvimo,J.J. and
            Pichler,A.
  TITLE     A new vertebrate SUMO enzyme family reveals insights into
            SUMO-chain assembly
  JOURNAL   Nat Struct Mol Biol 22 (12), 959-967 (2015)
   PUBMED   26524493
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC041125.1 and CN359914.1.
            
            On Nov 22, 2004 this sequence version replaced XP_166451.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.181122.1,
                                           SRR1660807.171359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370733.5/ ENSP00000359768.4
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.1"
     Protein         1..787
                     /product="E3 SUMO-protein ligase KIAA1586 isoform a"
                     /calculated_mol_wt=89542
     Region          1..223
                     /region_name="Sufficient for E3 SUMO-protein ligase
                     activity. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCI6.2)"
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCI6.2)"
     Region          30..37
                     /region_name="Interaction with SUMO2 1.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4E5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCI6.2)"
     Region          38..41
                     /region_name="PSRP. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCI6.2)"
     Region          42..50
                     /region_name="Interaction with SUMO2 2.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4E5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCI6.2)"
     Region          185..401
                     /region_name="DUF4371"
                     /note="Domain of unknown function (DUF4371); cl46273"
                     /db_xref="CDD:480613"
     CDS             1..787
                     /gene="KIAA1586"
                     /coded_by="NM_020931.4:64..2427"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34480.1"
                     /db_xref="GeneID:57691"
                     /db_xref="HGNC:HGNC:21360"
ORIGIN      
        1 mgdpgseiie svppagpeas esttdenedd iqfvsegpsr pvleyidlvc gddenpsayy
       61 sdilfpkmpk rqgdflhfln vkkvktdten nevsknhcrl skakephfey ieqpiieekp
      121 slsskkeidn lvlpdcwnek qafmfteqyk wleikegklg ckdcsavrhl gskaekhvhv
      181 skewiaylvt pngsnkttrq aslrkkireh dvskahgkiq dllkestnds icnlvhkqnn
      241 knidatvkvf ntvyslvkhn rplsdiegar elqekngevn clntrysatr iaehiakemk
      301 mkifkniiee nakiciiide astvskkttl viylqctiqs apapvmlfva lkelvstiae
      361 civntllttl ndcgftneyl kanliafcsd gantilgrks gvatkllenf peiiiwncln
      421 hrlqlsldds iseikqinhl kifidkiysi yhqpnknqtk llgtvakele teiikigrvm
      481 gprwaacslq aatavwhayp ilymhfshsy sglakrlani nflqdlalmi dileefsvls
      541 talqsrstni kkaqklikrt iralenlkig tgkyesqied liksdkfkdi pfnknnkfna
      601 lprsilldni iqhmnlrlls drnhedifny fdllepstwp yeeitspwia gektlfhlck
      661 ilkyevdlnd frefvnnnik snnvsiptti ykakkivsti ainsaeaerg fnlmniictr
      721 vrnsltidhv sdlmtinllg keladwdatp fvkswsncnh rlatdtrvrq kstkvfhenq
      781 laiwnlk
//
LOCUS       NP_659501                364 aa            linear   PRI 27-APR-2025
DEFINITION  SH3 and cysteine-rich domain-containing protein 3 isoform a [Homo
            sapiens].
ACCESSION   NP_659501
VERSION     NP_659501.1
DBSOURCE    REFSEQ: accession NM_145064.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Gromand,M., Gueguen,P., Perville,A., Ferroul,F., Morel,G.,
            Harouna,A., Doray,B., Urtizberea,J.A., Alessandri,J.L. and Robin,S.
  TITLE     STAC3 related congenital myopathy: A case series of seven Comorian
            patients
  JOURNAL   Eur J Med Genet 65 (10), 104598 (2022)
   PUBMED   36030003
  REMARK    GeneRIF: STAC3 related congenital myopathy: A case series of seven
            Comorian patients.
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Bi,X., Liu,J., Xu,S., Wang,Y. and Wu,X.
  TITLE     Testicular STAC3 regulates Leydig cell steroidogenesis through
            potentiating mitochondrial membrane potential and StAR processing
  JOURNAL   Cell Tissue Res 384 (1), 195-209 (2021)
   PUBMED   33409656
  REMARK    GeneRIF: Testicular STAC3 regulates Leydig cell steroidogenesis
            through potentiating mitochondrial membrane potential and StAR
            processing.
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 364)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Nelson,B.R., Wu,F., Liu,Y., Anderson,D.M., McAnally,J., Lin,W.,
            Cannon,S.C., Bassel-Duby,R. and Olson,E.N.
  TITLE     Skeletal muscle-specific T-tubule protein STAC3 mediates
            voltage-induced Ca2+ release and contractility
  JOURNAL   Proc Natl Acad Sci U S A 110 (29), 11881-11886 (2013)
   PUBMED   23818578
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Horstick,E.J., Linsley,J.W., Dowling,J.J., Hauser,M.A.,
            McDonald,K.K., Ashley-Koch,A., Saint-Amant,L., Satish,A., Cui,W.W.,
            Zhou,W., Sprague,S.M., Stamm,D.S., Powell,C.M., Speer,M.C.,
            Franzini-Armstrong,C., Hirata,H. and Kuwada,J.Y.
  TITLE     Stac3 is a component of the excitation-contraction coupling
            machinery and mutated in Native American myopathy
  JOURNAL   Nat Commun 4, 1952 (2013)
   PUBMED   23736855
  REMARK    GeneRIF: A mutation in human STAC3 is the genetic basis of the
            debilitating Native American myopathy.
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Webb,B.D., Manoli,I. and Jabs,E.W.
  TITLE     STAC3 Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31219695
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Rosenberg,H., Sambuughin,N., Riazi,S. and Dirksen,R.
  TITLE     Malignant Hyperthermia Susceptibility
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301325
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA896836.1, AK057013.1 and
            BU738507.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a component of the
            excitation-contraction coupling machinery of muscles. This protein
            is a member of the Stac gene family and contains an N-terminal
            cysteine-rich domain and two SH3 domains. Mutations in this gene
            are a cause of Native American myopathy. [provided by RefSeq, Nov
            2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK057013.1, ERR279851.2766.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000332782.7/ ENSP00000329200.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..364
                     /product="SH3 and cysteine-rich domain-containing protein
                     3 isoform a"
                     /note="SH3 and cysteine-rich domain-containing protein 3"
                     /calculated_mol_wt=41376
     Region          1..89
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MF2.1)"
     Region          85..143
                     /region_name="C1_Stac3"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in SH3 and cysteine-rich domain-containing protein 3
                     (Stac3) and similar proteins; cd20882"
                     /db_xref="CDD:410432"
     Region          147..243
                     /region_name="STAC2_u1"
                     /note="Unstructured on SH3 and cysteine-rich
                     domain-containing protein 2; pfam16664"
                     /db_xref="CDD:435497"
     Region          189..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MF2.1)"
     Region          251..303
                     /region_name="SH3_Stac3_1"
                     /note="First C-terminal Src homology 3 domain of SH3 and
                     cysteine-rich domain-containing protein 3 (Stac3);
                     cd11986"
                     /db_xref="CDD:212919"
     Site            order(256,258,261,265,283..284,297,299..300)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212919"
     Region          310..360
                     /region_name="SH3_Stac_2"
                     /note="Second C-terminal Src homology 3 domain of SH3 and
                     cysteine-rich domain-containing proteins 1 and 3; cd11834"
                     /db_xref="CDD:212768"
     Site            order(315,317,320,322,339..340,357,359..360)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212768"
     CDS             1..364
                     /gene="STAC3"
                     /gene_synonym="CMYO13; CMYP13; MYPBB; NAM"
                     /coded_by="NM_145064.3:197..1291"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8936.1"
                     /db_xref="GeneID:246329"
                     /db_xref="HGNC:HGNC:28423"
                     /db_xref="MIM:615521"
ORIGIN      
        1 mtekevlesp kpsfpaetrq sglqrlkqll rkgstgtkem elppepqang eavgagggpi
       61 yyiyeeeeee eeeeeepppe ppklvndkph kfkdhffkkp kfcdvcarmi vlnnkfglrc
      121 kncktniheh cqsyvemqrc fgkippgfhr ayssplysnq qyacvkdlsa anrndpvfet
      181 lrtgvimank erkkgqadkk npvaammeee pesarpeegk pqdgnpegdk kaekktpddk
      241 hkqpgfqqsh yfvalyrfka lekddldfpp gekitvidds neewwrgkig ekvgffppnf
      301 iirvragerv hrvtrsfvgn reigqitlkk dqivvqkgde aggyvkvytg rkvglfptdf
      361 leei
//
LOCUS       NP_065777                704 aa            linear   PRI 27-APR-2025
DEFINITION  neurolysin, mitochondrial [Homo sapiens].
ACCESSION   NP_065777
VERSION     NP_065777.1
DBSOURCE    REFSEQ: accession NM_020726.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Shi,K., Bagchi,S., Bickel,J., Esfahani,S.H., Yin,L., Cheng,T.,
            Karamyan,V.T. and Aihara,H.
  TITLE     Structural basis of divergent substrate recognition and inhibition
            of human neurolysin
  JOURNAL   Sci Rep 14 (1), 18420 (2024)
   PUBMED   39117724
  REMARK    GeneRIF: Structural basis of divergent substrate recognition and
            inhibition of human neurolysin.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Mirali,S., Botham,A., Voisin,V., Xu,C., St-Germain,J., Sharon,D.,
            Hoff,F.W., Qiu,Y., Hurren,R., Gronda,M., Jitkova,Y., Nachmias,B.,
            MacLean,N., Wang,X., Arruda,A., Minden,M.D., Horton,T.M.,
            Kornblau,S.M., Chan,S.M., Bader,G.D., Raught,B. and Schimmer,A.D.
  TITLE     The mitochondrial peptidase, neurolysin, regulates respiratory
            chain supercomplex formation and is necessary for AML viability
  JOURNAL   Sci Transl Med 12 (538) (2020)
   PUBMED   32269163
  REMARK    GeneRIF: The mitochondrial peptidase, neurolysin, regulates
            respiratory chain supercomplex formation and is necessary for AML
            viability.
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Teixeira,P.F., Masuyer,G., Pinho,C.M., Branca,R.M.M., Kmiec,B.,
            Wallin,C., Warmlander,S.K.T.S., Berntsson,R.P., Ankarcrona,M.,
            Graslund,A., Lehtio,J., Stenmark,P. and Glaser,E.
  TITLE     Mechanism of Peptide Binding and Cleavage by the Human
            Mitochondrial Peptidase Neurolysin
  JOURNAL   J Mol Biol 430 (3), 348-362 (2018)
   PUBMED   29183787
  REMARK    GeneRIF: The crystal structure of human neurolysin(E475Q) in
            complex with the products of neurotensin cleavage at 2.7A revealed
            a closed conformation with an internal cavity that restricts
            substrate length and highlighted the mechanism of enzyme
            opening/closing that is necessary for substrate binding and
            catalytic activity.
REFERENCE   5  (residues 1 to 704)
  AUTHORS   Norman,M.U., Reeve,S.B., Dive,V., Smith,A.I. and Lew,R.A.
  TITLE     Endopeptidases 3.4.24.15 and 24.16 in endothelial cells: potential
            role in vasoactive peptide metabolism
  JOURNAL   Am J Physiol Heart Circ Physiol 284 (6), H1978-H1984 (2003)
   PUBMED   12609826
REFERENCE   6  (residues 1 to 704)
  AUTHORS   Garrido,P.A., Vandenbulcke,F., Ramjaun,A.R., Vincent,B.,
            Checler,F., Ferro,E. and Beaudet,A.
  TITLE     Confocal microscopy reveals thimet oligopeptidase (EC 3.4.24.15)
            and neurolysin (EC 3.4.24.16) in the classical secretory pathway
  JOURNAL   DNA Cell Biol 18 (4), 323-331 (1999)
   PUBMED   10235115
REFERENCE   7  (residues 1 to 704)
  AUTHORS   Rioli,V., Kato,A., Portaro,F.C., Cury,G.K., te Kaat,K., Vincent,B.,
            Checler,F., Camargo,A.C., Glucksman,M.J., Roberts,J.L., Hirose,S.
            and Ferro,E.S.
  TITLE     Neuropeptide specificity and inhibition of recombinant isoforms of
            the endopeptidase 3.4.24.16 family: comparison with the related
            recombinant endopeptidase 3.4.24.15
  JOURNAL   Biochem Biophys Res Commun 250 (1), 5-11 (1998)
   PUBMED   9735321
REFERENCE   8  (residues 1 to 704)
  AUTHORS   Krause,D.R., Piva,T.J., Brown,S.B. and Ellem,K.A.
  TITLE     Characterization and localization of mitochondrial oligopeptidase
            (MOP) (EC 3.4.24.16) activity in the human cervical adenocarcinoma
            cell line HeLa
  JOURNAL   J Cell Biochem 66 (3), 297-308 (1997)
   PUBMED   9257187
REFERENCE   9  (residues 1 to 704)
  AUTHORS   Vincent,B., Dauch,P., Vincent,J.P. and Checler,F.
  TITLE     Stably transfected human cells overexpressing rat brain
            endopeptidase 3.4.24.16: biochemical characterization of the
            activity and expression of soluble and membrane-associated
            counterparts
  JOURNAL   J Neurochem 68 (2), 837-845 (1997)
   PUBMED   9003076
REFERENCE   10 (residues 1 to 704)
  AUTHORS   Vincent,B., Vincent,J.P. and Checler,F.
  TITLE     Purification and characterization of human endopeptidase 3.4.24.16.
            Comparison with the porcine counterpart indicates a unique cleavage
            site on neurotensin
  JOURNAL   Brain Res 709 (1), 51-58 (1996)
   PUBMED   8869556
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB992921.1, AJ300837.1,
            AC016643.6 and CA441264.1.
            
            Summary: This gene encodes a member of the metallopeptidase M3
            protein family that cleaves neurotensin at the Pro10-Tyr11 bond,
            leading to the formation of neurotensin(1-10) and
            neurotensin(11-13). The encoded protein is likely involved in the
            termination of the neurotensinergic signal in the central nervous
            system and in the gastrointestinal tract.[provided by RefSeq, Jun
            2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB033052.2, SRR1803615.18418.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000380985.10/
                                                  ENSP00000370372.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..704
                     /product="neurolysin, mitochondrial"
                     /EC_number="3.4.24.16"
                     /note="endopeptidase 24.16; neurotensin endopeptidase;
                     angiotensin binding protein; microsomal endopeptidase;
                     mitochondrial oligopeptidase M; neurolysin
                     (metallopeptidase M3 family)"
                     /calculated_mol_wt=80521
     Region          58..696
                     /region_name="M3A_TOP"
                     /note="Peptidase M3 thimet oligopeptidase (TOP), also
                     includes neurolysin; cd06455"
                     /db_xref="CDD:341050"
     Site            order(497..498,501,526,624,629..630,632..633,636)
                     /site_type="active"
                     /db_xref="CDD:341050"
     Site            664
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BYT8.1)"
     CDS             1..704
                     /gene="NLN"
                     /gene_synonym="AGTBP; EP24.16; MEP; MOP"
                     /coded_by="NM_020726.5:170..2284"
                     /db_xref="CCDS:CCDS3989.1"
                     /db_xref="GeneID:57486"
                     /db_xref="HGNC:HGNC:16058"
                     /db_xref="MIM:611530"
ORIGIN      
        1 miarcllavr slrrvggsri llrmtlgrev msplqamssy tvagrnvlrw dlspeqiktr
       61 teelivqtkq vydavgmlgi eevtyenclq aladvevkyi vertmldfpq hvssdkevra
      121 asteadkrls rfdiemsmrg diferivhlq etcdlgkikp earryleksi kmgkrnglhl
      181 peqvqneiks mkkrmselci dfnknlnedd tflvfskael galpddfids lektdddkyk
      241 itlkyphyfp vmkkccipet rrrmemafnt rckeentiil qqllplrtkv akllgystha
      301 dfvlemntak stsrvtafld dlsqklkplg eaerefilnl kkkeckdrgf eydgkinawd
      361 lyyymtqtee lkysidqefl keyfpievvt egllntyqel lglsfeqmtd ahvwnksvtl
      421 ytvkdkatge vlgqfyldly pregkynhaa cfglqpgcll pdgsrmmava alvvnfsqpv
      481 agrpsllrhd evrtyfhefg hvmhqicaqt dfarfsgtnv etdfvevpsq mlenwvwdvd
      541 slrrlskhyk dgspiaddll eklvasrlvn tglltlrqiv lskvdqslht ntsldaasey
      601 akycseilgv aatpgtnmpa tfghlaggyd gqyygylwse vfsmdmfysc fkkegimnpe
      661 vgmkyrnlil kpggsldgmd mlhnflkrep nqkaflmsrg lhap
//
LOCUS       NP_065755                834 aa            linear   PRI 27-APR-2025
DEFINITION  striatin-interacting protein 2 isoform a [Homo sapiens].
ACCESSION   NP_065755 XP_045907 XP_379923
VERSION     NP_065755.1
DBSOURCE    REFSEQ: accession NM_020704.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Pan,J., Zhang,Y., He,L., Wu,Y., Xiao,W., Zhang,J. and Xu,Y.
  TITLE     STRIP2 is regulated by the transcription factor Sp1 and promotes
            lung adenocarcinoma progression via activating the
            PI3K/AKT/mTOR/MYC signaling pathway
  JOURNAL   Genomics 116 (5), 110923 (2024)
   PUBMED   39191354
  REMARK    GeneRIF: STRIP2 is regulated by the transcription factor Sp1 and
            promotes lung adenocarcinoma progression via activating the
            PI3K/AKT/mTOR/MYC signaling pathway.
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Zhang,X., Chen,Q., He,Y., Shi,Q., Yin,C., Xie,Y., Yu,H., Bao,Y.,
            Wang,X., Tang,C. and Dong,Z.
  TITLE     STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent
  JOURNAL   J Exp Clin Cancer Res 42 (1), 19 (2023)
   PUBMED   36639675
  REMARK    GeneRIF: STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Qiu,L.M., Sun,Y.H., Chen,T.T., Chen,J.J. and Ma,H.T.
  TITLE     STRIP2, a member of the striatin-interacting phosphatase and kinase
            complex, is implicated in lung adenocarcinoma cell growth and
            migration
  JOURNAL   FEBS Open Bio 10 (3), 351-361 (2020)
   PUBMED   31901223
  REMARK    GeneRIF: STRIP2, a member of the striatin-interacting phosphatase
            and kinase complex, is implicated in lung adenocarcinoma cell
            growth and migration.
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Suryavanshi,N., Furmston,J. and Ridley,A.J.
  TITLE     The STRIPAK complex components FAM40A and FAM40B regulate
            endothelial cell contractility via ROCKs
  JOURNAL   BMC Cell Biol 19 (1), 26 (2018)
   PUBMED   30509168
  REMARK    GeneRIF: These results demonstrate the importance of the FAM40
            proteins for endothelial cell physiology, and suggest that they act
            as part of the CCM3-containing STRIPAK complex.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 834)
  AUTHORS   Eden,M., Meder,B., Volkers,M., Poomvanicha,M., Domes,K.,
            Branchereau,M., Marck,P., Will,R., Bernt,A., Rangrez,A., Busch,M.,
            Hrabe de Angelis,M., Heymes,C., Rottbauer,W., Most,P., Hofmann,F.
            and Frey,N.
  CONSRTM   German Mouse Clinic Consortium
  TITLE     Myoscape controls cardiac calcium cycling and contractility via
            regulation of L-type calcium channel surface expression
  JOURNAL   Nat Commun 7, 11317 (2016)
   PUBMED   27122098
  REMARK    GeneRIF: Data indicate that a cardiac protein named
            Myoscape/FAM40B/STRIP2, which directly interacts with the L-type
            calcium channel CaV1.2.
            Erratum:[Nat Commun. 2016 May 26;7:11835. doi: 10.1038/ncomms11835.
            PMID: 27225593]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 834)
  AUTHORS   Lisa-Santamaria,P., Jimenez,A. and Revuelta,J.L.
  TITLE     The protein factor-arrest 11 (Far11) is essential for the toxicity
            of human caspase-10 in yeast and participates in the regulation of
            autophagy and the DNA damage signaling
  JOURNAL   J Biol Chem 287 (35), 29636-29647 (2012)
   PUBMED   22782902
REFERENCE   7  (residues 1 to 834)
  AUTHORS   Pracheil,T., Thornton,J. and Liu,Z.
  TITLE     TORC2 signaling is antagonized by protein phosphatase 2A and the
            Far complex in Saccharomyces cerevisiae
  JOURNAL   Genetics 190 (4), 1325-1339 (2012)
   PUBMED   22298706
REFERENCE   8  (residues 1 to 834)
  AUTHORS   Bai,S.W., Herrera-Abreu,M.T., Rohn,J.L., Racine,V., Tajadura,V.,
            Suryavanshi,N., Bechtel,S., Wiemann,S., Baum,B. and Ridley,A.J.
  TITLE     Identification and characterization of a set of conserved and new
            regulators of cytoskeletal organization, cell morphology and
            migration
  JOURNAL   BMC Biol 9, 54 (2011)
   PUBMED   21834987
  REMARK    Erratum:[BMC Biol. 2024 Oct 10;22(1):228. doi:
            10.1186/s12915-024-02036-3. PMID: 39390519]
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 834)
  AUTHORS   Goudreault,M., D'Ambrosio,L.M., Kean,M.J., Mullin,M.J.,
            Larsen,B.G., Sanchez,A., Chaudhry,S., Chen,G.I., Sicheri,F.,
            Nesvizhskii,A.I., Aebersold,R., Raught,B. and Gingras,A.C.
  TITLE     A PP2A phosphatase high density interaction network identifies a
            novel striatin-interacting phosphatase and kinase complex linked to
            the cerebral cavernous malformation 3 (CCM3) protein
  JOURNAL   Mol Cell Proteomics 8 (1), 157-171 (2009)
   PUBMED   18782753
REFERENCE   10 (residues 1 to 834)
  AUTHORS   Kemp,H.A. and Sprague,G.F. Jr.
  TITLE     Far3 and five interacting proteins prevent premature recovery from
            pheromone arrest in the budding yeast Saccharomyces cerevisiae
  JOURNAL   Mol Cell Biol 23 (5), 1750-1763 (2003)
   PUBMED   12588993
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009244.25, DA409007.1 and AB032996.1.
            
            On or before Nov 22, 2004 this sequence version replaced
            XP_379923.2, XP_045907.4.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB032996.1, SRR1803612.238534.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000249344.7/ ENSP00000249344.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q32.1"
     Protein         1..834
                     /product="striatin-interacting protein 2 isoform a"
                     /note="homolog of yeast FAR11 protein 2; protein FAM40B;
                     family with sequence similarity 40, member B; FAR11 factor
                     arrest 11 homolog B"
                     /calculated_mol_wt=95229
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Region          49..291
                     /region_name="N1221"
                     /note="N1221-like protein; pfam07923"
                     /db_xref="CDD:429737"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Region          321..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Region          360..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Region          456..779
                     /region_name="DUF3402"
                     /note="Domain of unknown function (DUF3402); pfam11882"
                     /db_xref="CDD:463384"
     CDS             1..834
                     /gene="STRIP2"
                     /gene_synonym="FAM40B; FAR11B"
                     /coded_by="NM_020704.3:42..2546"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34752.1"
                     /db_xref="GeneID:57464"
                     /db_xref="HGNC:HGNC:22209"
                     /db_xref="MIM:617919"
ORIGIN      
        1 medpaapgtg gppangngng ggkgkqaapk greafrsqrr esegsvdcpt lefeygdadg
       61 haaelselys ytenleftnn rrcfeedfkt qvqgkewlel eedaqkayim glldrlevvs
      121 rerrlkvara vlylaqgtfg ecdsevdvlh wsryncflly qmgtfstfle llhmeidnsq
      181 acssalrkpa vsiadstelr vllsvmylmv enirleretd pcgwrtaret frtelsfsmh
      241 neepfalllf smvtkfcsgl aphfpikkvl lllwkvvmft lggfehlqtl kvqkraelgl
      301 pplaedsiqv vksmraaspp sytldlgesq lapppsklrg rrgsrrqllt kqdsldiyne
      361 rdlfkteepa teeeeesagd gertldgeld lleqdplvpp ppsqaplsae rvafpkglpw
      421 apkvrqkdie hflemsrnkf igftlgqdtd tlvglprpih esvktlkqhk yisiadvqik
      481 neeelekcpm slgeevvpet pceilyqgml yslpqymial lkillaaapt skaktdsini
      541 ladvlpeemp itvlqsmklg idvnrhkeii vksistllll llkhfklnhi yqfeyvsqhl
      601 vfanciplil kffnqnilsy itaknsisvl dypcctiqdl peltteslea gdnsqfcwrn
      661 lfscinllrl lnkltkwkhs rtmmlvvfks apilkralkv kqamlqlyvl kllklqtkyl
      721 grqwrksnmk tmsaiyqkvr hrmnddwayg ndidarpwdf qaeectlran ieafnsrryd
      781 rpqdsefspv dnclqsvlgq rldlpedfhy syelwlerev fsqpicweel lqnh
//
LOCUS       NP_001184223             684 aa            linear   PRI 27-APR-2025
DEFINITION  dihydropyrimidinase-related protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001184223
VERSION     NP_001184223.1
DBSOURCE    REFSEQ: accession NM_001197294.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Liang,P.I., Lai,H.Y., Chan,T.C., Li,W.M., Hsing,C.H., Huang,S.K.,
            Hsieh,K.L., Tseng,W.H., Chen,T.J., Li,W.S., Chen,H.D., Kuo,Y.H. and
            Li,C.F.
  TITLE     Upregulation of dihydropyrimidinase-like 3 (DPYSL3) protein
            predicts poor prognosis in urothelial carcinoma
  JOURNAL   BMC Cancer 23 (1), 599 (2023)
   PUBMED   37380971
  REMARK    GeneRIF: Upregulation of dihydropyrimidinase-like 3 (DPYSL3)
            protein predicts poor prognosis in urothelial carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Park,S.Y., Kim,J.T., Park,E.S., Hwang,Y.S., Yoon,H.R., Baek,K.E.,
            Jung,H., Yoon,S.R., Kim,B.Y., Cho,H.J. and Lee,H.G.
  TITLE     Collapsin response mediator protein 4 enhances the radiosensitivity
            of colon cancer cells through calcium-mediated cell signaling
  JOURNAL   Oncol Rep 45 (4) (2021)
   PUBMED   33655336
  REMARK    GeneRIF: Collapsin response mediator protein 4 enhances the
            radiosensitivity of colon cancer cells through calciummediated cell
            signaling.
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 684)
  AUTHORS   Tsai,Y.M., Wu,K.L., Chang,Y.Y., Hung,J.Y., Chang,W.A., Chang,C.Y.,
            Jian,S.F., Tsai,P.H., Huang,Y.C., Chong,I.W. and Hsu,Y.L.
  TITLE     Upregulation of Thr/Tyr kinase Increases the Cancer Progression by
            Neurotensin and Dihydropyrimidinase-Like 3 in Lung Cancer
  JOURNAL   Int J Mol Sci 21 (5), 1640 (2020)
   PUBMED   32121246
  REMARK    GeneRIF: Upregulation of Thr/Tyr kinase Increases the Cancer
            Progression by Neurotensin and Dihydropyrimidinase-Like 3 in Lung
            Cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Matsuo,T., Stauffer,J.K., Walker,R.L., Meltzer,P. and Thiele,C.J.
  TITLE     Structure and promoter analysis of the human unc-33-like
            phosphoprotein gene. E-box required for maximal expression in
            neuroblastoma and myoblasts
  JOURNAL   J Biol Chem 275 (22), 16560-16568 (2000)
   PUBMED   10748015
  REMARK    Erratum:[J Biol Chem 2000 Aug 11;275(32):25052-3]
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Inagaki,H., Kato,Y., Hamajima,N., Nonaka,M., Sasaki,M. and
            Eimoto,T.
  TITLE     Differential expression of dihydropyrimidinase-related protein
            genes in developing and adult enteric nervous system
  JOURNAL   Histochem Cell Biol 113 (1), 37-41 (2000)
   PUBMED   10664068
REFERENCE   8  (residues 1 to 684)
  AUTHORS   Gaetano,C., Matsuo,T. and Thiele,C.J.
  TITLE     Identification and characterization of a retinoic acid-regulated
            human homologue of the unc-33-like phosphoprotein gene (hUlip) from
            neuroblastoma cells
  JOURNAL   J Biol Chem 272 (18), 12195-12201 (1997)
   PUBMED   9115293
REFERENCE   9  (residues 1 to 684)
  AUTHORS   Hamajima,N., Matsuda,K., Sakata,S., Tamaki,N., Sasaki,M. and
            Nonaka,M.
  TITLE     A novel gene family defined by human dihydropyrimidinase and three
            related proteins with differential tissue distribution
  JOURNAL   Gene 180 (1-2), 157-163 (1996)
   PUBMED   8973361
REFERENCE   10 (residues 1 to 684)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011373.4, BC077077.1, D78014.1 and CA424493.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC077077.1, SRR1803612.105721.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000343218.10/ ENSP00000343690.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..684
                     /product="dihydropyrimidinase-related protein 3 isoform 1"
                     /note="dihydropyrimidinase-related protein 3; collapsin
                     response mediator protein 4 long; unc-33-like
                     phosphoprotein 1; testicular secretory protein Li 7"
                     /calculated_mol_wt=73780
     Region          131..585
                     /region_name="D-hydantoinase"
                     /note="TIGR02033"
                     /db_xref="CDD:273937"
     Site            order(142..143,145,158..159,294,315,318,321,344,348,352,
                     355,382..383,385..386,504,509,514)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238639"
     Site            order(187,189,279,312,368,446)
                     /site_type="active"
                     /db_xref="CDD:238639"
     CDS             1..684
                     /gene="DPYSL3"
                     /gene_synonym="CRMP-4; CRMP4; DRP-3; DRP3; LCRMP; ULIP;
                     ULIP-1"
                     /coded_by="NM_001197294.2:211..2265"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS56387.1"
                     /db_xref="GeneID:1809"
                     /db_xref="HGNC:HGNC:3015"
                     /db_xref="MIM:601168"
ORIGIN      
        1 masgrrgwds sheddlpvyl arpgttdqvp rqkyggmfcn vegafesktl dfdalsvgqr
       61 gaktprsgqg sdrgsgsrpg iegdtprrgq greesrepap aspapagvei rsatgkevlq
      121 nlgpkdksdr llikggrivn ddqsfyadiy medglikqig dnlivpggvk tieangkmvi
      181 pggidvhthf qmpykgmttv ddffqgtkaa laggttmiid hvvpepessl teayekwrew
      241 adgksccdya lhvdithwnd svkqevqnli kdkgvnsfmv ymaykdlyqv sntelyeift
      301 clgelgaiaq vhaengdiia qeqtrmlemg itgpeghvls rpeeleaeav fraitiasqt
      361 ncplyvtkvm sksaadlisq arkkgnvvfg epitaslgid gthywsknwa kaaafvtspp
      421 lspdpttpdy insllasgdl qlsgsahctf staqkaigkd nftaipegtn gveermsviw
      481 dkavatgkmd enqfvavtst naakifnlyp rkgrisvgsd sdlviwdpda vkivsaknhq
      541 saaeynifeg melrgaplvv icqgkimled gnlhvtqgag rfipcspfsd yvykrikarr
      601 kmadlhavpr gmydgpvfdl tttpkggtpa gsargsptrp nppvrnlhqs gfslsgtqvd
      661 egvrsaskri vappggrsni tsls
//
LOCUS       NP_631903                205 aa            linear   PRI 27-APR-2025
DEFINITION  stAR-related lipid transfer protein 4 isoform a [Homo sapiens].
ACCESSION   NP_631903
VERSION     NP_631903.1
DBSOURCE    REFSEQ: accession NM_139164.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Yahya,N.A., King,S.R., Shi,B., Shaaban,A., Whitfield,N.E., Yan,C.,
            Kordus,R.J., Whitman-Elia,G.F. and LaVoie,H.A.
  TITLE     Differential regulation of STARD1, STARD4 and STARD6 in the human
            ovary
  JOURNAL   J Endocrinol 262 (2), e230385 (2024)
   PUBMED   38829257
  REMARK    GeneRIF: Differential regulation of STARD1, STARD4 and STARD6 in
            the human ovary.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Talandashti,R., van Ek,L., Gehin,C., Xue,D., Moqadam,M., Gavin,A.C.
            and Reuter,N.
  TITLE     Membrane specificity of the human cholesterol transfer protein
            STARD4
  JOURNAL   J Mol Biol 436 (11), 168572 (2024)
   PUBMED   38615744
  REMARK    GeneRIF: Membrane specificity of the human cholesterol transfer
            protein STARD4.
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Yue,X., Kong,Y., Zhang,Y., Sun,M., Liu,S., Wu,Z., Gao,L., Liang,X.
            and Ma,C.
  TITLE     SREBF2-STARD4 axis confers sorafenib resistance in hepatocellular
            carcinoma by regulating mitochondrial cholesterol homeostasis
  JOURNAL   Cancer Sci 114 (2), 477-489 (2023)
   PUBMED   35642354
  REMARK    GeneRIF: SREBF2-STARD4 axis confers sorafenib resistance in
            hepatocellular carcinoma by regulating mitochondrial cholesterol
            homeostasis.
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Huang,T., Shan,R., Zhang,M., Li,L., Huang,J., Liu,B. and Zhou,W.
  TITLE     [Steroidogenic acute regulatory protein-related lipid transfer 4
            (StarD4) promotes breast cancer cell proliferation and its
            mechanism]
  JOURNAL   Sheng Wu Yi Xue Gong Cheng Xue Za Zhi 38 (6), 1118-1125 (2021)
   PUBMED   34970895
  REMARK    GeneRIF: [Steroidogenic acute regulatory protein-related lipid
            transfer 4 (StarD4) promotes breast cancer cell proliferation and
            its mechanism].
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Zhang,M., Xiang,Z., Wang,F., Shan,R., Li,L., Chen,J., Liu,B.A.,
            Huang,J., Sun,L.Q. and Zhou,W.B.
  TITLE     STARD4 promotes breast cancer cell malignancy
  JOURNAL   Oncol Rep 44 (6), 2487-2502 (2020)
   PUBMED   33125124
  REMARK    GeneRIF: STARD4 promotes breast cancer cell malignancy.
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Rodriguez-Agudo,D., Ren,S., Wong,E., Marques,D., Redford,K.,
            Gil,G., Hylemon,P. and Pandak,W.M.
  TITLE     Intracellular cholesterol transporter StarD4 binds free cholesterol
            and increases cholesteryl ester formation
  JOURNAL   J Lipid Res 49 (7), 1409-1419 (2008)
   PUBMED   18403318
  REMARK    GeneRIF: StarD4 plays an important role as a directional
            cholesterol transporter in the maintenance of cellular cholesterol
            homeostasis
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Yamada,S., Yamaguchi,T., Hosoda,A., Iwawaki,T. and Kohno,K.
  TITLE     Regulation of human STARD4 gene expression under endoplasmic
            reticulum stress
  JOURNAL   Biochem Biophys Res Commun 343 (4), 1079-1085 (2006)
   PUBMED   16579971
  REMARK    GeneRIF: Induction of STARD4 depended on both transcription factor
            ATF6 and an ERSE-like element in its promoter.
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Soccio,R.E., Adams,R.M., Maxwell,K.N. and Breslow,J.L.
  TITLE     Differential gene regulation of StarD4 and StarD5 cholesterol
            transfer proteins. Activation of StarD4 by sterol regulatory
            element-binding protein-2 and StarD5 by endoplasmic reticulum
            stress
  JOURNAL   J Biol Chem 280 (19), 19410-19418 (2005)
   PUBMED   15760897
  REMARK    GeneRIF: StarD4 is regulated by sterols via SREBP-2, and StarD5 is
            activated by ER stress cholesterol metabolism; they serve different
            functions
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Soccio,R.E., Adams,R.M., Romanowski,M.J., Sehayek,E., Burley,S.K.
            and Breslow,J.L.
  TITLE     The cholesterol-regulated StarD4 gene encodes a StAR-related lipid
            transfer protein with two closely related homologues, StarD5 and
            StarD6
  JOURNAL   Proc Natl Acad Sci U S A 99 (10), 6943-6948 (2002)
   PUBMED   12011452
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB475661.1, AK054566.1, AK125317.1, BI091150.1, AK026207.1 and
            BU607573.1.
            
            Summary: Cholesterol homeostasis is regulated, at least in part, by
            sterol regulatory element (SRE)-binding proteins (e.g., SREBP1; MIM
            184756) and by liver X receptors (e.g., LXRA; MIM 602423). Upon
            sterol depletion, LXRs are inactive and SREBPs are cleaved, after
            which they bind promoter SREs and activate genes involved in
            cholesterol biosynthesis and uptake. Sterol transport is mediated
            by vesicles or by soluble protein carriers, such as steroidogenic
            acute regulatory protein (STAR; MIM 600617). STAR is homologous to
            a family of proteins containing a 200- to 210-amino acid
            STAR-related lipid transfer (START) domain, including STARD4
            (Soccio et al., 2002 [PubMed 12011452]).[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Both variants 1 and 2 encode isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP281046.1, SRR1660803.157181.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296632.8/ ENSP00000296632.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.1"
     Protein         1..205
                     /product="stAR-related lipid transfer protein 4 isoform a"
                     /note="START domain containing 4, sterol regulated;
                     stAR-related lipid transfer protein 4; START
                     domain-containing protein 4; StAR-related lipid transfer
                     (START) domain containing 4"
                     /calculated_mol_wt=23386
     Region          5..205
                     /region_name="SRPBCC"
                     /note="START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC)
                     ligand-binding domain superfamily; cl14643"
                     /db_xref="CDD:472699"
     Site            order(53,55,57,66..68,70..71,86,97,99,101,103,118,120,122,
                     131,133,152..153,155,157,169,171,173,175,186..190,
                     192..193,196..198,201)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
     CDS             1..205
                     /gene="STARD4"
                     /coded_by="NM_139164.3:161..778"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4104.1"
                     /db_xref="GeneID:134429"
                     /db_xref="HGNC:HGNC:18058"
                     /db_xref="MIM:607049"
ORIGIN      
        1 meglsdvasf atklkntliq yhsieedkwr vakktkdvtv wrkpseefng ylykaqgvid
       61 dlvysiidhi rpgpcrldwd slmtsldile nfeenccvmr yttagqlwni isprefvdfs
      121 ytvgykegll scgisldwde krpefvrgyn hpcgwfcvpl kdnpnqsllt gyiqtdlrgm
      181 ipqsavdtam astltnfygd lrkal
//
LOCUS       NP_066010               1232 aa            linear   PRI 27-APR-2025
DEFINITION  anoctamin-8 [Homo sapiens].
ACCESSION   NP_066010 XP_050644
VERSION     NP_066010.1
DBSOURCE    REFSEQ: accession NM_020959.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1232)
  AUTHORS   Liu,X., Lai,H., Zeng,X., Xin,S., Nie,L., Liang,Z., Wu,M., Chen,Y.,
            Zheng,J. and Zou,Y.
  TITLE     Whole-exome sequencing reveals ANO8 as a genetic risk factor for
            intrahepatic cholestasis of pregnancy
  JOURNAL   BMC Pregnancy Childbirth 20 (1), 544 (2020)
   PUBMED   32942997
  REMARK    GeneRIF: Whole-exome sequencing reveals ANO8 as a genetic risk
            factor for intrahepatic cholestasis of pregnancy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1232)
  AUTHORS   Jha,A., Chung,W.Y., Vachel,L., Maleth,J., Lake,S., Zhang,G.,
            Ahuja,M. and Muallem,S.
  TITLE     Anoctamin 8 tethers endoplasmic reticulum and plasma membrane for
            assembly of Ca2+ signaling complexes at the ER/PM compartment
  JOURNAL   EMBO J 38 (12) (2019)
   PUBMED   31061173
  REMARK    GeneRIF: Anoctamin 8 (ANO8) as a key tether in the formation of the
            Endoplasmic reticulum/Plasma membrane (ER/PM) junctions that is
            essential for STIM1-STIM1 interaction and STIM1-Orai1 interaction
            and channel activation at a ER/PM PI(4,5)P2-rich compartment. Ano8
            assembles all core Calcium signaling proteins.
REFERENCE   3  (residues 1 to 1232)
  AUTHORS   Pedemonte,N. and Galietta,L.J.
  TITLE     Structure and function of TMEM16 proteins (anoctamins)
  JOURNAL   Physiol Rev 94 (2), 419-459 (2014)
   PUBMED   24692353
  REMARK    Review article
REFERENCE   4  (residues 1 to 1232)
  AUTHORS   Okada,Y., Wu,D., Trynka,G., Raj,T., Terao,C., Ikari,K., Kochi,Y.,
            Ohmura,K., Suzuki,A., Yoshida,S., Graham,R.R., Manoharan,A.,
            Ortmann,W., Bhangale,T., Denny,J.C., Carroll,R.J., Eyler,A.E.,
            Greenberg,J.D., Kremer,J.M., Pappas,D.A., Jiang,L., Yin,J., Ye,L.,
            Su,D.F., Yang,J., Xie,G., Keystone,E., Westra,H.J., Esko,T.,
            Metspalu,A., Zhou,X., Gupta,N., Mirel,D., Stahl,E.A., Diogo,D.,
            Cui,J., Liao,K., Guo,M.H., Myouzen,K., Kawaguchi,T., Coenen,M.J.,
            van Riel,P.L., van de Laar,M.A., Guchelaar,H.J., Huizinga,T.W.,
            Dieude,P., Mariette,X., Bridges,S.L. Jr., Zhernakova,A., Toes,R.E.,
            Tak,P.P., Miceli-Richard,C., Bang,S.Y., Lee,H.S., Martin,J.,
            Gonzalez-Gay,M.A., Rodriguez-Rodriguez,L., Rantapaa-Dahlqvist,S.,
            Arlestig,L., Choi,H.K., Kamatani,Y., Galan,P., Lathrop,M., Eyre,S.,
            Bowes,J., Barton,A., de Vries,N., Moreland,L.W., Criswell,L.A.,
            Karlson,E.W., Taniguchi,A., Yamada,R., Kubo,M., Liu,J.S., Bae,S.C.,
            Worthington,J., Padyukov,L., Klareskog,L., Gregersen,P.K.,
            Raychaudhuri,S., Stranger,B.E., De Jager,P.L., Franke,L.,
            Visscher,P.M., Brown,M.A., Yamanaka,H., Mimori,T., Takahashi,A.,
            Xu,H., Behrens,T.W., Siminovitch,K.A., Momohara,S., Matsuda,F.,
            Yamamoto,K. and Plenge,R.M.
  CONSRTM   RACI consortium; GARNET consortium
  TITLE     Genetics of rheumatoid arthritis contributes to biology and drug
            discovery
  JOURNAL   Nature 506 (7488), 376-381 (2014)
   PUBMED   24390342
REFERENCE   5  (residues 1 to 1232)
  AUTHORS   Tian,Y., Schreiber,R. and Kunzelmann,K.
  TITLE     Anoctamins are a family of Ca2+-activated Cl- channels
  JOURNAL   J Cell Sci 125 (Pt 21), 4991-4998 (2012)
   PUBMED   22946059
REFERENCE   6  (residues 1 to 1232)
  AUTHORS   Scudieri,P., Sondo,E., Ferrera,L. and Galietta,L.J.
  TITLE     The anoctamin family: TMEM16A and TMEM16B as calcium-activated
            chloride channels
  JOURNAL   Exp Physiol 97 (2), 177-183 (2012)
   PUBMED   21984732
REFERENCE   7  (residues 1 to 1232)
  AUTHORS   Ousingsawat,J., Kongsuphol,P., Schreiber,R. and Kunzelmann,K.
  TITLE     CFTR and TMEM16A are separate but functionally related Cl- channels
  JOURNAL   Cell Physiol Biochem 28 (4), 715-724 (2011)
   PUBMED   22178883
REFERENCE   8  (residues 1 to 1232)
  AUTHORS   Hartzell,H.C., Yu,K., Xiao,Q., Chien,L.T. and Qu,Z.
  TITLE     Anoctamin/TMEM16 family members are Ca2+-activated Cl- channels
  JOURNAL   J Physiol 587 (Pt 10), 2127-2139 (2009)
   PUBMED   19015192
  REMARK    Review article
REFERENCE   9  (residues 1 to 1232)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of TMEM16H gene in silico
  JOURNAL   Int J Mol Med 15 (2), 353-358 (2005)
   PUBMED   15647853
  REMARK    GeneRIF: Human TMEM16H gene, consisting of 18 exons, is located at
            human chromosome 19p13.11.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010463.6, AB046843.2 and AI860149.1.
            
            On Nov 22, 2004 this sequence version replaced XP_050644.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB046843.2, ERR4352441.67869.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000159087.7/ ENSP00000159087.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1232
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1232
                     /product="anoctamin-8"
                     /note="transmembrane protein 16H"
                     /calculated_mol_wt=135904
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Region          237..>497
                     /region_name="Anoctamin"
                     /note="Calcium-activated chloride channel; pfam04547"
                     /db_xref="CDD:461349"
     Site            245..265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            282..302
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PB70; propagated from
                     UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            357..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            401..421
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            438..458
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Region          524..650
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PB70; propagated from
                     UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Region          681..728
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Region          <717..877
                     /region_name="Anoctamin"
                     /note="Calcium-activated chloride channel; pfam04547"
                     /db_xref="CDD:461349"
     Site            751..771
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            801
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            808..828
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            842..862
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Region          888..970
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Region          <940..>1120
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          997..1152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Site            1020
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q6PB70;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q6PB70; propagated from
                     UniProtKB/Swiss-Prot (Q9HCE9.3)"
     Region          1174..1232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE9.3)"
     CDS             1..1232
                     /gene="ANO8"
                     /gene_synonym="KIAA1623; TMEM16H"
                     /coded_by="NM_020959.3:186..3884"
                     /db_xref="CCDS:CCDS32949.1"
                     /db_xref="GeneID:57719"
                     /db_xref="HGNC:HGNC:29329"
                     /db_xref="MIM:610216"
ORIGIN      
        1 maeaasgagg tslegergkr pppegepaap asgvldklfg krllqagryl vshkawmktv
       61 ptencdvlmt fpdttddhtl lwllnhirvg ipelivqvrh hrhtrayaff vtatyesllr
      121 gadelglrka vkaefgggtr gfsceedfiy enveselrff tsqerqsiir fwlqnlrakq
      181 gealhnvrfl edqpiipela argiiqqvfp vheqrilnrl mkswvqavce nqplddicdy
      241 fgvkiamyfa wlgfytsamv ypavfgsvly tfteadqtsr dvscvvfalf nviwstlfle
      301 ewkrrgaela ykwgtldspg eaveeprpqf rgvrrispit raeefyyppw krllfqllvs
      361 lplclaclvc vfllmlgcfq lqelvlsvkg lprlarflpk vmlallvsvs aegykklaiw
      421 lndmenyrle sayekhliik vvlfqfvnsy lslfyigfyl kdmerlkeml atllitrqfl
      481 qnvrevlqph lyrrlgrgel glravwelar allgllslrr paprrlepqa degggggsgg
      541 ggrrclsggc gapeeeeeaa lverrrageg geegdgppgg keededdeee edeeeeedee
      601 egeegglldc glrlkkvsfa ergagrrrpg pspealleeg sptmvekgle pgvftlaeed
      661 deaegapgsp ereppailfr raggegrdqg pdggpdpepg snsdstrrqr rqnrsswidp
      721 peeehspqlt qaelescmkk yedtfqdyqe mfvqfgyvvl fssafplaal calvnnliei
      781 rsdafklctg lqrpfgqrve sigqwqkvme amgvlaivvn cyligqcgql qrlfpwlspe
      841 aaivsvvvle hfalllkyli hvaipdipgw vaeemakley qrreafkrhe rqaqhryqqq
      901 qrrrreeeer qrhaehharr ehdsggreea raegsgldpa tssekasaka kgstagghgp
      961 erpkrpgsll apnnvmklkq iiplqgkfls sgatsslaaa gagattrppp aqsptgsdtr
     1021 lpaflsfkfl kspetrrdse rshsppkafh agklfpfggt raepgsngag gqarpdgtps
     1081 sgssrvqrsg pvdealaeel eaprpeeegs gtalapvgap alrtrrsrsp appppmplpr
     1141 pptppagcwq wdgpwgcgge gaaprqalaa aecppcamag pppapqplpg dasfyslppp
     1201 plpptsdple tpapspspsp spqavcwpsg wh
//
LOCUS       NP_001356451             488 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM39 isoform 2 [Homo sapiens].
ACCESSION   NP_001356451
VERSION     NP_001356451.1
DBSOURCE    REFSEQ: accession NM_001369522.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Ogura,T., Azuma,K., Takeiwa,T., Sato,J., Kinowaki,K., Ikeda,K.,
            Kawabata,H. and Inoue,S.
  TITLE     TRIM39 is a poor prognostic factor for patients with estrogen
            receptor-positive breast cancer and promotes cell cycle progression
  JOURNAL   Pathol Int 72 (2), 96-106 (2022)
   PUBMED   35174936
  REMARK    GeneRIF: TRIM39 is a poor prognostic factor for patients with
            estrogen receptor-positive breast cancer and promotes cell cycle
            progression.
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Hu,J., Ding,X., Tian,S., Chu,Y., Liu,Z., Li,Y., Li,X., Wang,G.,
            Wang,L. and Wang,Z.
  TITLE     TRIM39 deficiency inhibits tumor progression and autophagic flux in
            colorectal cancer via suppressing the activity of Rab7
  JOURNAL   Cell Death Dis 12 (4), 391 (2021)
   PUBMED   33846303
  REMARK    GeneRIF: TRIM39 deficiency inhibits tumor progression and
            autophagic flux in colorectal cancer via suppressing the activity
            of Rab7.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Ning,L., Ko,J.M., Yu,V.Z., Ng,H.Y., Chan,C.K., Tao,L., Lam,S.Y.,
            Leong,M.M., Ngan,R.K., Kwong,D.L., Lee,A.W., Ng,W.T., Cheng,A.,
            Tung,S., Lee,V.H., Lam,K.O., Kwan,C.K., Li,W.S., Yau,S., Bei,J.X.
            and Lung,M.L.
  TITLE     Nasopharyngeal carcinoma MHC region deep sequencing identifies HLA
            and novel non-HLA TRIM31 and TRIM39 loci
  JOURNAL   Commun Biol 3 (1), 759 (2020)
   PUBMED   33311639
  REMARK    GeneRIF: Nasopharyngeal carcinoma MHC region deep sequencing
            identifies HLA and novel non-HLA TRIM31 and TRIM39 loci.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 488)
  AUTHORS   Roberts,J.D. Jr., Chiche,J.D., Kolpa,E.M., Bloch,D.B. and
            Bloch,K.D.
  TITLE     cGMP-dependent protein kinase I interacts with TRIM39R, a novel
            Rpp21 domain-containing TRIM protein
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 293 (4), L903-L912 (2007)
   PUBMED   17601797
REFERENCE   7  (residues 1 to 488)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   8  (residues 1 to 488)
  AUTHORS   Tao,W.A., Wollscheid,B., O'Brien,R., Eng,J.K., Li,X.J.,
            Bodenmiller,B., Watts,J.D., Hood,L. and Aebersold,R.
  TITLE     Quantitative phosphoproteome analysis using a dendrimer conjugation
            chemistry and tandem mass spectrometry
  JOURNAL   Nat Methods 2 (8), 591-598 (2005)
   PUBMED   16094384
REFERENCE   9  (residues 1 to 488)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   10 (residues 1 to 488)
  AUTHORS   Orimo,A., Yamagishi,T., Tominaga,N., Yamauchi,Y., Hishinuma,T.,
            Okada,K., Suzuki,M., Sato,M., Nogi,Y., Suzuki,H., Inoue,S.,
            Yoshimura,K., Shimizu,Y. and Muramatsu,M.
  TITLE     Molecular cloning of testis-abundant finger Protein/Ring finger
            protein 23 (RNF23), a novel RING-B box-coiled coil-B30.2 protein on
            the class I region of the human MHC
  JOURNAL   Biochem Biophys Res Commun 276 (1), 45-51 (2000)
   PUBMED   11006080
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662795.5.
            
            Summary: The protein encoded by this gene is a member of the
            tripartite motif (TRIM) family. The TRIM motif includes three
            zinc-binding domains, a RING, a B-box type 1 and a B-box type 2,
            and a coiled-coil region. The function of this protein has not been
            identified. This gene lies within the major histocompatibility
            complex class I region on chromosome 6. Alternate splicing results
            in two transcript variants encoding different isoforms. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.170972.1,
                                           SRR1660803.206526.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..488
                     /product="E3 ubiquitin-protein ligase TRIM39 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 23; testis-abundant finger
                     protein; tripartite motif-containing protein 39; E3
                     ubiquitin-protein ligase TRIM39; RING-type E3 ubiquitin
                     transferase TRIM39"
                     /calculated_mol_wt=56244
     Region          22..82
                     /region_name="RING-HC_TRIM7-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins, TRIM7, TRIM11 and TRIM27, and
                     similar proteins; cd16594"
                     /db_xref="CDD:438256"
     Region          103..146
                     /region_name="Bbox2_TRIM39-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins TRIM39, TRIM58 and similar
                     proteins; cd19780"
                     /db_xref="CDD:380838"
     Region          149..>270
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          305..483
                     /region_name="SPRY_PRY_TRIM39"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     39 (TRIM39) and TRIM39-like; cd13745"
                     /db_xref="CDD:293979"
     CDS             1..488
                     /gene="TRIM39"
                     /gene_synonym="RNF23; TFP; TRIM39B"
                     /coded_by="NM_001369522.1:580..2046"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS34378.1"
                     /db_xref="GeneID:56658"
                     /db_xref="HGNC:HGNC:10065"
                     /db_xref="MIM:605700"
ORIGIN      
        1 maetslleag asaastaaal enlqveascs vcleylkepv iiecghnfck acitrwwedl
       61 erdfpcpvcr ktsryrslrp nrqlgsmvei akqlqavkrk irdeslcpqh healslfcye
      121 dqeavclica ishthrahtv vplddatqey keklqkclep leqklqeitr cksseekkpg
      181 elkrlvesrr qqilrefeel hrrldeeqqv llsrleeeeq dilqrlrena ahlgdkrrdl
      241 ahlaaevegk clqsgfemlk dvkstlekce kvktmevtsv sieleknfsn fprqyfalrk
      301 ilkqliadvt ldpetahpnl vlsedrksvk fvetrlrdlp dtprrftfyp cvlategfts
      361 grhywevevg dkthwavgvc rdsvsrkgel tplpetgywr vrlwngdkya atttpftplh
      421 ikvkpkrvgi fldyeagtls fynvtdrshi ytftdtftek lwplfypgir agrknaaplt
      481 irpptdwe
//
LOCUS       NP_003899                333 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 2 subunit 2 isoform 1
            [Homo sapiens].
ACCESSION   NP_003899
VERSION     NP_003899.2
DBSOURCE    REFSEQ: accession NM_003908.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Fatalska,A., Hodgson,G., Freund,S.M.V., Maslen,S.L., Morgan,T.,
            Thorkelsson,S.R., van Slegtenhorst,M., Lorenz,S., Andreeva,A.,
            Kaat,L.D. and Bertolotti,A.
  TITLE     Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit
            PPP1R15B
  JOURNAL   Mol Cell 84 (3), 506-521 (2024)
   PUBMED   38159565
  REMARK    GeneRIF: Recruitment of trimeric eIF2 by phosphatase non-catalytic
            subunit PPP1R15B.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Zhang,J., Li,S., Zhang,L., Xu,J., Song,M., Shao,T., Huang,Z. and
            Li,Y.
  TITLE     RBP EIF2S2 Promotes Tumorigenesis and Progression by Regulating
            MYC-Mediated Inhibition via FHIT-Related Enhancers
  JOURNAL   Mol Ther 28 (4), 1105-1118 (2020)
   PUBMED   32059763
  REMARK    GeneRIF: RBP EIF2S2 Promotes Tumorigenesis and Progression by
            Regulating MYC-Mediated Inhibition via FHIT-Related Enhancers.
            Erratum:[Mol Ther. 2021 Feb 3;29(2):886. doi:
            10.1016/j.ymthe.2020.12.020. PMID: 33341125]
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Das,S., Maiti,T., Das,K. and Maitra,U.
  TITLE     Specific interaction of eukaryotic translation initiation factor 5
            (eIF5) with the beta-subunit of eIF2
  JOURNAL   J Biol Chem 272 (50), 31712-31718 (1997)
   PUBMED   9395514
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Brand,S.R., Kobayashi,R. and Mathews,M.B.
  TITLE     The Tat protein of human immunodeficiency virus type 1 is a
            substrate and inhibitor of the interferon-induced, virally
            activated protein kinase, PKR
  JOURNAL   J Biol Chem 272 (13), 8388-8395 (1997)
   PUBMED   9079663
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Welsh,G.I., Price,N.T., Bladergroen,B.A., Bloomberg,G. and
            Proud,C.G.
  TITLE     Identification of novel phosphorylation sites in the beta-subunit
            of translation initiation factor eIF-2
  JOURNAL   Biochem Biophys Res Commun 201 (3), 1279-1288 (1994)
   PUBMED   8024572
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Pathak,V.K., Nielsen,P.J., Trachsel,H. and Hershey,J.W.
  TITLE     Structure of the beta subunit of translational initiation factor
            eIF-2
  JOURNAL   Cell 54 (5), 633-639 (1988)
   PUBMED   3044606
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Safer,B., Adams,S.L., Anderson,W.F. and Merrick,W.C.
  TITLE     Binding of MET-TRNAf and GTP to homogeneous initiation factor MP
  JOURNAL   J Biol Chem 250 (23), 9076-9082 (1975)
   PUBMED   1104615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC000461.2, AL031668.23 and CA436754.1.
            
            On Apr 14, 2003 this sequence version replaced NP_003899.1.
            
            Summary: Eukaryotic translation initiation factor 2 (EIF-2)
            functions in the early steps of protein synthesis by forming a
            ternary complex with GTP and initiator tRNA and binding to a 40S
            ribosomal subunit. EIF-2 is composed of three subunits, alpha,
            beta, and gamma, with the protein encoded by this gene representing
            the beta subunit. The beta subunit catalyzes the exchange of GDP
            for GTP, which recycles the EIF-2 complex for another round of
            initiation. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Oct
            2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.96523.1,
                                           SRR1660803.162664.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374980.3/ ENSP00000364119.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..333
                     /product="eukaryotic translation initiation factor 2
                     subunit 2 isoform 1"
                     /note="eukaryotic translation initiation factor 2 subunit
                     2; protein phosphatase 1, regulatory subunit 67;
                     eukaryotic translation initiation factor 2, subunit 2
                     beta, 38kDa; eIF2-beta"
                     /calculated_mol_wt=38257
     Region          1..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Region          139..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Region          199..308
                     /region_name="eIF2B_5"
                     /note="domain present in translation initiation factor
                     eIF2B and eIF5; smart00653"
                     /db_xref="CDD:214764"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41035; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            293
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     CDS             1..333
                     /gene="EIF2S2"
                     /gene_synonym="eIF-2-beta; EIF2; EIF2B; EIF2beta; PPP1R67"
                     /coded_by="NM_003908.5:134..1135"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13231.1"
                     /db_xref="GeneID:8894"
                     /db_xref="HGNC:HGNC:3266"
                     /db_xref="MIM:603908"
ORIGIN      
        1 msgdemifdp tmskkkkkkk kpfmldeegd tqteetqpse tkevepepte dkdleadeed
       61 trkkdasddl ddlnffnqkk kkkktkkifd ideaeegvkd lkiesdvqep tepeddldim
      121 lgnkkkkkkn vkfpdedeil ekdealeded nkkddgisfs nqtgpawags erdytyeell
      181 nrvfnimrek npdmvagekr kfvmkppqvv rvgtkktsfv nftdickllh rqpkhllafl
      241 laelgtsgsi dgnnqlvikg rfqqkqienv lrryikeyvt chtcrspdti lqkdtrlyfl
      301 qcetchsrcs vasiktgfqa vtgkraqlra kan
//
LOCUS       NP_002452                400 aa            linear   PRI 27-APR-2025
DEFINITION  diphosphomevalonate decarboxylase [Homo sapiens].
ACCESSION   NP_002452
VERSION     NP_002452.1
DBSOURCE    REFSEQ: accession NM_002461.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Bharadwaj,T., Schrauwen,I., Rehman,S., Liaqat,K., Acharya,A.,
            Giese,A.P.J., Nouel-Saied,L.M., Nasir,A., Everard,J.L.,
            Pollock,L.M., Zhu,S., Bamshad,M.J., Nickerson,D.A., Ali,R.H.,
            Ullah,A., Wali,A., Ali,G., Santos-Cortez,R.L.P., Ahmed,Z.M.,
            McDermott,B.M. Jr., Ansar,M., Riazuddin,S., Ahmad,W. and Leal,S.M.
  TITLE     ADAMTS1, MPDZ, MVD, and SEZ6: candidate genes for autosomal
            recessive nonsyndromic hearing impairment
  JOURNAL   Eur J Hum Genet 30 (1), 22-33 (2022)
   PUBMED   34135477
  REMARK    GeneRIF: ADAMTS1, MPDZ, MVD, and SEZ6: candidate genes for
            autosomal recessive nonsyndromic hearing impairment.
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Saleva-Stateva,M., Technau-Hafsi,K., Frommherz,L., Gruninger,G.,
            Jagle,S., Dourmishev,L., Miteva,L., Fischer,J. and Has,C.
  TITLE     Recurrent MVD mutation in European patients with disseminated
            porokeratosis
  JOURNAL   Br J Dermatol 184 (2), 347-348 (2021)
   PUBMED   32767669
  REMARK    GeneRIF: Recurrent MVD mutation in European patients with
            disseminated porokeratosis.
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Kubo,A., Sasaki,T., Suzuki,H., Shiohama,A., Aoki,S., Sato,S.,
            Fujita,H., Ono,N., Umegaki-Arao,N., Kawai,T., Nakabayashi,K.,
            Hata,K., Yamada,D., Matsubara,Y., Kosaki,K. and Amagai,M.
  TITLE     Clonal Expansion of Second-Hit Cells with Somatic Recombinations or
            C>T Transitions Form Porokeratosis in MVD or MVK Mutant
            Heterozygotes
  JOURNAL   J Invest Dermatol 139 (12), 2458-2466 (2019)
   PUBMED   31207227
  REMARK    GeneRIF: Patients with disseminated superficial actinic
            porokeratosis (DSAP) and linear porokeratosis (LP) exhibit
            monoallelic germline mutations in genes encoding mevalonate pathway
            enzymes, such as MVD or MVK
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Wadhwa,R., Yaguchi,T., Hasan,M.K., Taira,K. and Kaul,S.C.
  TITLE     Mortalin-MPD (mevalonate pyrophosphate decarboxylase) interactions
            and their role in control of cellular proliferation
  JOURNAL   Biochem Biophys Res Commun 302 (4), 735-742 (2003)
   PUBMED   12646231
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Hogenboom,S., Romeijn,G.J., Houten,S.M., Baes,M., Wanders,R.J. and
            Waterham,H.R.
  TITLE     Absence of functional peroxisomes does not lead to deficiency of
            enzymes involved in cholesterol biosynthesis
  JOURNAL   J Lipid Res 43 (1), 90-98 (2002)
   PUBMED   11792727
REFERENCE   8  (residues 1 to 400)
  AUTHORS   Cuthbert,J.A. and Lipsky,P.E.
  TITLE     Regulation of proliferation and Ras localization in transformed
            cells by products of mevalonate metabolism
  JOURNAL   Cancer Res 57 (16), 3498-3505 (1997)
   PUBMED   9270019
REFERENCE   9  (residues 1 to 400)
  AUTHORS   Ku,E.C.
  TITLE     Regulation of fatty acid biosynthesis by intermediates of the
            cholesterol biosynthetic pathway
  JOURNAL   Biochem Biophys Res Commun 225 (1), 173-179 (1996)
   PUBMED   8769113
REFERENCE   10 (residues 1 to 400)
  AUTHORS   Toth,M.J. and Huwyler,L.
  TITLE     Molecular cloning and expression of the cDNAs encoding human and
            yeast mevalonate pyrophosphate decarboxylase
  JOURNAL   J Biol Chem 271 (14), 7895-7898 (1996)
   PUBMED   8626466
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC000011.2, HY026498.1,
            AC116552.2 and U49260.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The enzyme mevalonate pyrophosphate decarboxylase
            catalyzes the conversion of mevalonate pyrophosphate into
            isopentenyl pyrophosphate in one of the early steps in cholesterol
            biosynthesis. It decarboxylates and dehydrates its substrate while
            hydrolyzing ATP. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U49260.1, BC000011.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301012.8/ ENSP00000301012.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.2"
     Protein         1..400
                     /product="diphosphomevalonate decarboxylase"
                     /EC_number="4.1.1.33"
                     /note="mevalonate pyrophosphate decarboxylase; mevalonate
                     (diphospho) decarboxylase"
                     /calculated_mol_wt=43274
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P53602.1)"
     Region          10..337
                     /region_name="MDD_C"
                     /note="Mevalonate 5-diphosphate decarboxylase C-terminal
                     domain; cl28577"
                     /db_xref="CDD:475042"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P53602.1)"
     CDS             1..400
                     /gene="MVD"
                     /gene_synonym="FP17780; MDDase; MPD; POROK7"
                     /coded_by="NM_002461.3:12..1214"
                     /db_xref="CCDS:CCDS10968.1"
                     /db_xref="GeneID:4597"
                     /db_xref="HGNC:HGNC:7529"
                     /db_xref="MIM:603236"
ORIGIN      
        1 masekplaav tctapvniav ikywgkrdee lvlpinssls vtlhqdqlkt tttaviskdf
       61 tedriwlngr eedvgqprlq aclreircla rkrrnsrdgd plpsslsckv hvasvnnfpt
      121 aaglassaag yaclaytlar vygvesdlse varrgsgsac rslyggfvew qmgeqadgkd
      181 siarqvapes hwpelrvlil vvsaekkltg stvgmrasve tspllrfrae svvparmaem
      241 arcirerdfp sfaqltmkds nqfhatcldt fppisylnai swriihlvhr fnahhgdtkv
      301 aytfdagpna viftlddtva efvaavwhgf ppgsngdtfl kglqvrpapl saelqaalam
      361 eptpggvkyi ivtqvgpgpq ilddpcahll gpdglpkpaa
//
LOCUS       NP_001093115             122 aa            linear   PRI 27-APR-2025
DEFINITION  ribosomal protein eL22-like isoform 1 [Homo sapiens].
ACCESSION   NP_001093115 XP_001132475 XP_001132707
VERSION     NP_001093115.1
DBSOURCE    REFSEQ: accession NM_001099645.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Yi,X., Zhang,C., Liu,B., Gao,G., Tang,Y., Lu,Y., Pan,Z., Wang,G.
            and Feng,W.
  TITLE     Ribosomal protein L22-like1 promotes prostate cancer progression by
            activating PI3K/Akt/mTOR signalling pathway
  JOURNAL   J Cell Mol Med 27 (3), 403-411 (2023)
   PUBMED   36625246
  REMARK    GeneRIF: Ribosomal protein L22-like1 promotes prostate cancer
            progression by activating PI3K/Akt/mTOR signalling pathway.
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Rao,S., Peri,S., Hoffmann,J., Cai,K.Q., Harris,B., Rhodes,M.,
            Connolly,D.C., Testa,J.R. and Wiest,D.L.
  TITLE     RPL22L1 induction in colorectal cancer is associated with poor
            prognosis and 5-FU resistance
  JOURNAL   PLoS One 14 (10), e0222392 (2019)
   PUBMED   31581233
  REMARK    GeneRIF: RPL22L1 might be a prognostic marker in colorectal cancer
            and predict 5-Fluorouracil responsiveness.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Matoba,R., Okubo,K., Hori,N., Fukushima,A. and Matsubara,K.
  TITLE     The addition of 5'-coding information to a 3'-directed cDNA library
            improves analysis of gene expression
  JOURNAL   Gene 146 (2), 199-207 (1994)
   PUBMED   8076819
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC062731.1, AC061708.17 and CA449264.1.
            
            On or before Jul 26, 2007 this sequence version replaced
            XP_001132707.1, XP_001132475.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.167320.1,
                                           SRR1660809.144861.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149876, SAMN03267778
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295830.13/ ENSP00000346080.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..122
                     /product="ribosomal protein eL22-like isoform 1"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L22-like 1; large ribosomal
                     subunit protein eL22-like 1; ribosomal protein eL22-like"
                     /calculated_mol_wt=14475
     Region          16..114
                     /region_name="Ribosomal_L22e"
                     /note="Ribosomal L22e protein family; pfam01776"
                     /db_xref="CDD:460321"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6P5R6.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6P5R6.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P5R6.2)"
     CDS             1..122
                     /gene="RPL22L1"
                     /coded_by="NM_001099645.2:29..397"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46955.1"
                     /db_xref="GeneID:200916"
                     /db_xref="HGNC:HGNC:27610"
ORIGIN      
        1 mapqkdrkpk rstwrfnldl thpvedgifd sgnfeqflre kvkvngktgn lgnvvhierf
       61 knkitvvsek qfskrylkyl tkkylkknnl rdwlrvvasd ketyelryfq isqdedeses
      121 ed
//
LOCUS       NP_057213                406 aa            linear   PRI 27-APR-2025
DEFINITION  COP9 signalosome complex subunit 4 isoform 1 [Homo sapiens].
ACCESSION   NP_057213
VERSION     NP_057213.2
DBSOURCE    REFSEQ: accession NM_016129.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Bech-Otschir,D., Kraft,R., Huang,X., Henklein,P., Kapelari,B.,
            Pollmann,C. and Dubiel,W.
  TITLE     COP9 signalosome-specific phosphorylation targets p53 to
            degradation by the ubiquitin system
  JOURNAL   EMBO J 20 (7), 1630-1639 (2001)
   PUBMED   11285227
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Cohen,H., Azriel,A., Cohen,T., Meraro,D., Hashmueli,S.,
            Bech-Otschir,D., Kraft,R., Dubiel,W. and Levi,B.Z.
  TITLE     Interaction between interferon consensus sequence-binding protein
            and COP9/signalosome subunit CSN2 (Trip15). A possible link between
            interferon regulatory factor signaling and the COP9/signalosome
  JOURNAL   J Biol Chem 275 (50), 39081-39089 (2000)
   PUBMED   10991940
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Naumann,M., Bech-Otschir,D., Huang,X., Ferrell,K. and Dubiel,W.
  TITLE     COP9 signalosome-directed c-Jun activation/stabilization is
            independent of JNK
  JOURNAL   J Biol Chem 274 (50), 35297-35300 (1999)
   PUBMED   10585392
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK001148.1, BC004302.1 and
            BC009292.2.
            
            On Nov 18, 2003 this sequence version replaced NP_057213.1.
            
            Summary: This gene encodes one of eight subunits composing COP9
            signalosome, a highly conserved protein complex that functions as
            an important regulator in multiple signaling pathways. The
            structure and function of COP9 signalosome is similar to that of
            the 19S regulatory particle of 26S proteasome. COP9 signalosome has
            been shown to interact with SCF-type E3 ubiquitin ligases and act
            as a positive regulator of E3 ubiquitin ligases. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (1) encodes isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005665.1, SRR3476690.835033.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264389.7/ ENSP00000264389.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..406
                     /product="COP9 signalosome complex subunit 4 isoform 1"
                     /note="COP9 signalosome complex subunit 4; signalosome
                     subunit 4; JAB1-containing signalosome subunit 4; COP9
                     constitutive photomorphogenic homolog subunit 4; COP9
                     constitutive photomorphogenic-like protein subunit 4;
                     testis tissue sperm-binding protein Li 42a"
                     /calculated_mol_wt=46138
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:18850735,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9BT78.1)"
     Site            25
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BT78.1)"
     Region          <71..377
                     /region_name="RPN5"
                     /note="26S proteasome regulatory complex component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5071"
                     /db_xref="CDD:227403"
     Region          264..362
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     Region          365..406
                     /region_name="CSN4_RPN5_eIF3a"
                     /note="CSN4/RPN5/eIF3a helix turn helix domain; pfam18420"
                     /db_xref="CDD:375846"
     CDS             1..406
                     /gene="COPS4"
                     /gene_synonym="CSN4; SGN4"
                     /coded_by="NM_016129.3:43..1263"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3600.1"
                     /db_xref="GeneID:51138"
                     /db_xref="HGNC:HGNC:16702"
                     /db_xref="MIM:616008"
ORIGIN      
        1 maaavrqdla qlmnssgshk dlagkyrqil ekaiqlsgae qlealkafve amvnenvslv
       61 isrqlltdfc thlpnlpdst akeiyhftle kiqprvisfe eqvasirqhl asiyekeedw
      121 rnaaqvlvgi pletgqkqyn vdykletylk iarlyleddd pvqaeayinr asllqnestn
      181 eqlqihykvc yarvldyrrk fieaaqryne lsyktivhes erlealkhal hctilasagq
      241 qrsrmlatlf kdercqqlaa ygilekmyld riirgnqlqe faamlmphqk attadgssil
      301 draviehnll sasklynnit feelgallei paakaekias qmitegrmng fidqidgivh
      361 fetrealptw dkqiqslcfq vnnllekisq tapewtaqam eaqmaq
//
LOCUS       NP_001295065             148 aa            linear   PRI 27-APR-2025
DEFINITION  protein archease isoform 3 [Homo sapiens].
ACCESSION   NP_001295065 XP_005270858
VERSION     NP_001295065.1
DBSOURCE    REFSEQ: accession NM_001308136.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Mason,C.C., Khorashad,J.S., Tantravahi,S.K., Kelley,T.W.,
            Zabriskie,M.S., Yan,D., Pomicter,A.D., Reynolds,K.R., Eiring,A.M.,
            Kronenberg,Z., Sherman,R.L., Tyner,J.W., Dalley,B.K., Dao,K.H.,
            Yandell,M., Druker,B.J., Gotlib,J., O'Hare,T. and Deininger,M.W.
  TITLE     Age-related mutations and chronic myelomonocytic leukemia
  JOURNAL   Leukemia 30 (4), 906-913 (2016)
   PUBMED   26648538
  REMARK    GeneRIF: ARCH mutation is associated with chronic myelomonocytic
            leukemia.
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Jurkin,J., Henkel,T., Nielsen,A.F., Minnich,M., Popow,J.,
            Kaufmann,T., Heindl,K., Hoffmann,T., Busslinger,M. and Martinez,J.
  TITLE     The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA
            and controls antibody secretion in plasma cells
  JOURNAL   EMBO J 33 (24), 2922-2936 (2014)
   PUBMED   25378478
  REMARK    GeneRIF: RTCB, the catalytic subunit of the tRNA ligase complex,
            and its co-factor archease mediate XBP1 mRNA splicing both in vitro
            and in vivo.
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Popow,J., Jurkin,J., Schleiffer,A. and Martinez,J.
  TITLE     Analysis of orthologous groups reveals archease and DDX1 as tRNA
            splicing factors
  JOURNAL   Nature 511 (7507), 104-107 (2014)
   PUBMED   24870230
  REMARK    GeneRIF: archease (also called ZBTB8OS), a protein of unknown
            function, is required for full activity of the human tRNA ligase
            complex and, in cooperation with DDX1, facilitates the formation of
            an RTCB-guanylate intermediate central to mammalian RNA ligation
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Popow,J., Englert,M., Weitzer,S., Schleiffer,A., Mierzwa,B.,
            Mechtler,K., Trowitzsch,S., Will,C.L., Luhrmann,R., Soll,D. and
            Martinez,J.
  TITLE     HSPC117 is the essential subunit of a human tRNA splicing ligase
            complex
  JOURNAL   Science 331 (6018), 760-764 (2011)
   PUBMED   21311021
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 148)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2 and AL033529.25.
            
            On Apr 28, 2015 this sequence version replaced XP_005270858.1.
            
            Transcript Variant: This variant (3) lacks an exon in the 3' coding
            region, which results in a frameshift and an early stop codon,
            compared to variant 1. The encoded isoform (3) is shorter and has a
            distinct C-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.654545.1,
                                           SRR5189667.297107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2153733
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..148
                     /product="protein archease isoform 3"
                     /note="protein archease; archease-like protein; archease
                     (ARCH); zinc finger and BTB domain-containing opposite
                     strand protein 8"
                     /calculated_mol_wt=16763
     Region          43..>136
                     /region_name="Archease"
                     /note="Archease protein family (MTH1598/TM1083);
                     pfam01951"
                     /db_xref="CDD:426527"
     CDS             1..148
                     /gene="ZBTB8OS"
                     /gene_synonym="ARCH; ARCH2"
                     /coded_by="NM_001308136.2:368..814"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:339487"
                     /db_xref="HGNC:HGNC:24094"
                     /db_xref="MIM:615891"
ORIGIN      
        1 mkggsrvsnp avmaqeeedv rdynlteeqk aikakyppvn rkyeyldhta dvqlhawgdt
       61 leeafeqcam amfgymtdtg tveplqtvev etqgddlqsl lfhfldewly kfsadeffip
      121 rvgrrifivq apsgnrsqsn nifsnagl
//
LOCUS       NP_001349142             565 aa            linear   ROD 27-APR-2025
DEFINITION  kelch repeat and BTB domain-containing protein 2 isoform b [Mus
            musculus].
ACCESSION   NP_001349142 XP_006505911
VERSION     NP_001349142.1
DBSOURCE    REFSEQ: accession NM_001362213.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Ding,J., Gao,W., Yang,H., Duan,L., Sun,D., Liu,L., Qu,X., Yu,H.,
            Xu,B., Zhao,S., Wang,L. and Chai,J.
  TITLE     KBTBD2 promotes proliferation and migration of gastric cancer via
            activating EGFR signaling pathway
  JOURNAL   Pathol Res Pract 254, 155095 (2024)
   PUBMED   38237399
  REMARK    GeneRIF: KBTBD2 promotes proliferation and migration of gastric
            cancer via activating EGFR signaling pathway.
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Zhang,Z., Gallagher,T., Scherer,P.E. and Beutler,B.
  TITLE     Tissue-specific disruption of Kbtbd2 uncovers adipocyte-intrinsic
            and -extrinsic features of the teeny lipodystrophy syndrome
  JOURNAL   Proc Natl Acad Sci U S A 117 (21), 11829-11835 (2020)
   PUBMED   32381739
  REMARK    GeneRIF: Tissue-specific disruption of Kbtbd2 uncovers
            adipocyte-intrinsic and -extrinsic features of the teeny
            lipodystrophy syndrome.
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Dai,K., Huang,Y., Chen,Z., Sun,X., Yang,L. and Jiang,Y.
  TITLE     Kbtbd2 inhibits the cytotoxic activity of immortalized NK cells
            through down-regulating mTOR signaling in a mouse hepatocellular
            carcinoma model
  JOURNAL   Eur J Immunol 48 (4), 683-695 (2018)
   PUBMED   29331106
  REMARK    GeneRIF: This investigation indicates that Kbtbd2 is an inhibitory
            molecule for the tumoricidal activity of KIL C.2 Natural killer
            cells and perhaps intratumoral Natural killer cells.
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Zhang,Z., Turer,E., Li,X., Zhan,X., Choi,M., Tang,M., Press,A.,
            Smith,S.R., Divoux,A., Moresco,E.M. and Beutler,B.
  TITLE     Insulin resistance and diabetes caused by genetic or diet-induced
            KBTBD2 deficiency in mice
  JOURNAL   Proc Natl Acad Sci U S A 113 (42), E6418-E6426 (2016)
   PUBMED   27708159
  REMARK    GeneRIF: KBTBD2 is an essential regulator of the insulin-signaling
            pathway, modulating insulin sensitivity by limiting p85alpha
            abundance.
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Wang,T., Zhan,X., Bu,C.H., Lyon,S., Pratt,D., Hildebrand,S.,
            Choi,J.H., Zhang,Z., Zeng,M., Wang,K.W., Turer,E., Chen,Z.,
            Zhang,D., Yue,T., Wang,Y., Shi,H., Wang,J., Sun,L., SoRelle,J.,
            McAlpine,W., Hutchins,N., Zhan,X., Fina,M., Gobert,R., Quan,J.,
            Kreutzer,M., Arnett,S., Hawkins,K., Leach,A., Tate,C., Daniel,C.,
            Reyna,C., Prince,L., Davis,S., Purrington,J., Bearden,R.,
            Weatherly,J., White,D., Russell,J., Sun,Q., Tang,M., Li,X.,
            Scott,L., Moresco,E.M., McInerney,G.M., Karlsson Hedestam,G.B.,
            Xie,Y. and Beutler,B.
  TITLE     Real-time resolution of point mutations that cause phenovariance in
            mice
  JOURNAL   Proc Natl Acad Sci U S A 112 (5), E440-E449 (2015)
   PUBMED   25605905
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC115003.18.
            
            On Apr 10, 2018 this sequence version replaced XP_006505911.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660811.217453.1,
                                           SRR10662774.3801209.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 27.73 cM"
     Protein         1..565
                     /product="kelch repeat and BTB domain-containing protein 2
                     isoform b"
                     /note="BTB and kelch domain containing 1; kelch repeat and
                     BTB domain-containing protein 2"
                     /calculated_mol_wt=64379
     Region          <1..79
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Region          27..458
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          70..165
                     /region_name="BACK_KBTBD2"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch repeat and BTB domain-containing protein 2 (KBTBD2);
                     cd18479"
                     /db_xref="CDD:350554"
     Region          252..308
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          316..357
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          361..398
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          401..458
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          461..510
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..565
                     /gene="Kbtbd2"
                     /gene_synonym="Bklhd1; mKIAA1489"
                     /coded_by="NM_001362213.1:360..2057"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="GeneID:210973"
                     /db_xref="MGI:MGI:2384811"
ORIGIN      
        1 mfmsglsesk qthvhlrnvd aaalqmiiay aytgnlavnd stveqlyeta cflqvedvlq
       61 rcreylikki naencvrlls fadlfsceel kqsakrmveh kftavyrqea fmqlshdlli
      121 dilssdnlnv ekeetvreaa mlwleyntes rsqylssvls qiridalsev tqrawfqglp
      181 pndksvvvqg lyksmpkffk prlgmtkeem mifieassen pcslyssvcy spqaekvykl
      241 csppadlhkv gtvvtpdndi yiaggqvplk ntktnhskts klqtafrtvn cfywfdaqqn
      301 twfpktpmlf vrvkpslvcc egyiyaiggd svggelnrrt verydtekde wtmvsplpca
      361 wqwsaavvvh dciyvmtlnl mycyfprsds wvemamrqts rsfasaaafg dkifyigglh
      421 iatnsgirlp sgtvdgssvt veiydvnkne wkmaanipak rysdpcvrav visnslcvfm
      481 rethlnerak yvtyqydlel drwslrqhis ervlwdlgrd frctvgklyp scleespwkp
      541 ptylfspdgt eefeldgemv alppv
//
LOCUS       NP_001355068             281 aa            linear   PRI 27-APR-2025
DEFINITION  unconventional myosin-VI isoform 6 [Homo sapiens].
ACCESSION   NP_001355068
VERSION     NP_001355068.1
DBSOURCE    REFSEQ: accession NM_001368139.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Zheng,S., Hong,Z., Tan,Y., Wang,Y., Li,J., Zhang,Z., Feng,T.,
            Hong,Z., Lin,G. and Ye,D.
  TITLE     MYO6 contributes to tumor progression and enzalutamide resistance
            in castration-resistant prostate cancer by activating the focal
            adhesion signaling pathway
  JOURNAL   Cell Commun Signal 22 (1), 517 (2024)
   PUBMED   39449086
  REMARK    GeneRIF: MYO6 contributes to tumor progression and enzalutamide
            resistance in castration-resistant prostate cancer by activating
            the focal adhesion signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Raghuvanshi,R., Panda,K.C., Ray,C.S. and Ramchander,P.V.
  TITLE     Targeted Next-Generation Sequencing Analysis Reveals a Novel
            Genetic Variant in MYO6 Gene in an Indian Family with Postlingual
            Nonsyndromic Hearing Loss
  JOURNAL   Genet Test Mol Biomarkers 28 (8), 328-336 (2024)
   PUBMED   39019031
  REMARK    GeneRIF: Targeted Next-Generation Sequencing Analysis Reveals a
            Novel Genetic Variant in MYO6 Gene in an Indian Family with
            Postlingual Nonsyndromic Hearing Loss.
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Canon,L., Kikuti,C., Planelles-Herrero,V.J., Lin,T., Mayeux,F.,
            Sirkia,H., Lee,Y.I., Heidsieck,L., Velikovsky,L., David,A., Liu,X.,
            Moussaoui,D., Forest,E., Hook,P., Petersen,K.J., Morgan,T.E., Di
            Cicco,A., Sires-Campos,J., Derivery,E., Levy,D., Delevoye,C.,
            Sweeney,H.L. and Houdusse,A.
  TITLE     How myosin VI traps its off-state, is activated and dimerizes
  JOURNAL   Nat Commun 14 (1), 6732 (2023)
   PUBMED   37872146
  REMARK    GeneRIF: How myosin VI traps its off-state, is activated and
            dimerizes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Yang,A., Liu,X., Liu,P., Feng,Y., Liu,H., Gao,S., Huo,L., Han,X.,
            Wang,J. and Kong,W.
  TITLE     LncRNA UCA1 promotes development of gastric cancer via the
            miR-145/MYO6 axis
  JOURNAL   Cell Mol Biol Lett 26 (1), 33 (2021)
   PUBMED   34238213
  REMARK    GeneRIF: LncRNA UCA1 promotes development of gastric cancer via the
            miR-145/MYO6 axis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Avraham,K.B., Hasson,T., Sobe,T., Balsara,B., Testa,J.R.,
            Skvorak,A.B., Morton,C.C., Copeland,N.G. and Jenkins,N.A.
  TITLE     Characterization of unconventional MYO6, the human homologue of the
            gene responsible for deafness in Snell's waltzer mice
  JOURNAL   Hum Mol Genet 6 (8), 1225-1231 (1997)
   PUBMED   9259267
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Avraham,K.B., Hasson,T., Steel,K.P., Kingsley,D.M., Russell,L.B.,
            Mooseker,M.S., Copeland,N.G. and Jenkins,N.A.
  TITLE     The mouse Snell's waltzer deafness gene encodes an unconventional
            myosin required for structural integrity of inner ear hair cells
  JOURNAL   Nat Genet 11 (4), 369-375 (1995)
   PUBMED   7493015
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Hasson,T. and Mooseker,M.S.
  TITLE     Porcine myosin-VI: characterization of a new mammalian
            unconventional myosin
  JOURNAL   J Cell Biol 127 (2), 425-440 (1994)
   PUBMED   7929586
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Bement,W.M., Hasson,T., Wirth,J.A., Cheney,R.E. and Mooseker,M.S.
  TITLE     Identification and overlapping expression of multiple
            unconventional myosin genes in vertebrate cell types
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6549-6553 (1994)
   PUBMED   8022818
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11767. doi:
            10.1073/pnas.91.24.11767-c. PMID: 7972138]
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109897.30 and AL136093.8.
            
            Summary: This gene encodes a reverse-direction motor protein that
            moves toward the minus end of actin filaments and plays a role in
            intracellular vesicle and organelle transport. The protein consists
            of a motor domain containing an ATP- and an actin-binding site and
            a globular tail which interacts with other proteins. This protein
            maintains the structural integrity of inner ear hair cells and
            mutations in this gene cause non-syndromic autosomal dominant and
            recessive hearing loss. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms. [provided by
            RefSeq, Jul 2014].
            
            Transcript Variant: This variant (6), as well as variant 7, encodes
            isoform 6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.188092.1,
                                           SRR1660807.418212.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968540,
                                           SAMEA2163459 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..281
                     /product="unconventional myosin-VI isoform 6"
                     /note="unconventional myosin-6; unconventional myosin-VI"
                     /calculated_mol_wt=31610
     Region          71..>263
                     /region_name="Motor_domain"
                     /note="Myosin and Kinesin motor domain; cl22853"
                     /db_xref="CDD:473979"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     CDS             1..281
                     /gene="MYO6"
                     /gene_synonym="DFNA22; DFNB37"
                     /coded_by="NM_001368139.1:351..1196"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:4646"
                     /db_xref="HGNC:HGNC:7605"
                     /db_xref="MIM:600970"
ORIGIN      
        1 medgkpvwap hptdgfqmgn ivdigpdslt ieplnqkgkt flalinqvfp aeedskkdve
       61 dncslmylne atllhnikvr yskdriytyv aniliavnpy fdipkiysse aiksyqgksl
      121 gtrpphvfai adkafrdmkv lkmsqsiivs gesgagkten tkfvlrylte sygtgqdidd
      181 riveanplle afgnaktvrn nnssrfgkfv eihfnekssv vggfvshyll eksricvqgk
      241 eernyhifyr lcagasedir eklhlsspdn frvgqkkrnf i
//
LOCUS       NP_065747                154 aa            linear   PRI 27-APR-2025
DEFINITION  uncharacterized protein KIAA1143 isoform 1 [Homo sapiens].
ACCESSION   NP_065747
VERSION     NP_065747.1
DBSOURCE    REFSEQ: accession NM_020696.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA192476.1, BC008468.1, AC098649.2 and BU741967.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA443587.1, SRR1660803.152736.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMN03267771 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296121.6/ ENSP00000296121.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..154
                     /product="uncharacterized protein KIAA1143 isoform 1"
                     /calculated_mol_wt=17334
     Region          5..150
                     /region_name="DUF4604"
                     /note="Domain of unknown function (DUF4604); pfam15377"
                     /db_xref="CDD:464685"
     Region          23..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AT1.2)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96AT1.2)"
     Region          79..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AT1.2)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96AT1.2)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96AT1.2)"
     CDS             1..154
                     /gene="KIAA1143"
                     /coded_by="NM_020696.4:18..482"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2721.1"
                     /db_xref="GeneID:57456"
                     /db_xref="HGNC:HGNC:29198"
ORIGIN      
        1 mskrnqvsyv rpaepaflar fkervgyreg ptvetkriqp qppdedgdhs dkedeqpqvv
       61 vlkkgdlsve evmkikaeik aakadeeptp adgriiyrkp vkhpsdekys gltasskkkk
      121 pnedevnqds vkknsqkqik nssllsfdne dene
//
LOCUS       NP_000569                550 aa            linear   PRI 27-APR-2025
DEFINITION  natural resistance-associated macrophage protein 1 [Homo sapiens].
ACCESSION   NP_000569
VERSION     NP_000569.3
DBSOURCE    REFSEQ: accession NM_000578.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Wu,D., Zhou,Y., Shi,X., Yi,X., Sheng,Z., Fan,L., Ge,J., Cheng,W.,
            Zhou,W., He,H. and Fu,D.
  TITLE     SLC11A1 promotes kidney renal clear cell carcinoma (KIRC)
            progression by remodeling the tumor microenvironment
  JOURNAL   Toxicol Appl Pharmacol 487, 116975 (2024)
   PUBMED   38762191
  REMARK    GeneRIF: SLC11A1 promotes kidney renal clear cell carcinoma (KIRC)
            progression by remodeling the tumor microenvironment.
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Antony,B.S., Nagarajan,C., Devaraj,D.V. and Subbaraj,G.K.
  TITLE     A Systemic Review and Meta-analysis on Natural
            Resistance-associated Macrophage Protein 1 (3'-Untranslated Region)
            and Nucleotide-binding Oligomerization Domain-2 (rs8057341)
            Polymorphisms and Leprosy Susceptibility in Asian and Caucasian
            Populations
  JOURNAL   Int J Mycobacteriol 13 (2), 115-125 (2024)
   PUBMED   38916380
  REMARK    GeneRIF: A Systemic Review and Meta-analysis on Natural
            Resistance-associated Macrophage Protein 1 (3'-Untranslated Region)
            and Nucleotide-binding Oligomerization Domain-2 (rs8057341)
            Polymorphisms and Leprosy Susceptibility in Asian and Caucasian
            Populations.
            Review article
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Meng,C., Chen,G., Wen,D., Dong,L., Cui,X., Jing,X., Cui,J., Gao,Y.,
            Liu,Y., Bu,H. and Wu,C.
  TITLE     The expression of Nramp1 modulates the uptake of Mycobacterium
            tuberculosis by macrophages through alternating inflammatory
            responses
  JOURNAL   Tuberculosis (Edinb) 143, 102414 (2023)
   PUBMED   37820457
  REMARK    GeneRIF: The expression of Nramp1 modulates the uptake of
            Mycobacterium tuberculosis by macrophages through alternating
            inflammatory responses.
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Pauline,R., Devaraj,D.V., Sivasubramanian,J., Velmurugan,S.,
            Stephen,S.B., Yasam,S.K., Kulanthaivel,L. and Subbaraj,G.K.
  TITLE     Systemic assessment of solute carrier family 11-member A1
            (rs17235409) gene polymorphism and Mycobacterium Tuberculosis Risk
            in Asian and caucasian population: A comprehensive updated
            meta-analysis
  JOURNAL   Int J Mycobacteriol 12 (4), 467-477 (2023)
   PUBMED   38149545
  REMARK    GeneRIF: Systemic assessment of solute carrier family 11-member A1
            (rs17235409) gene polymorphism and Mycobacterium Tuberculosis Risk
            in Asian and caucasian population: A comprehensive updated
            meta-analysis.
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Waworuntu,W., Tanoerahardjo,F.S., Mallongi,A., Ahmad,A., Amin,M.,
            Djaharuddin,I., Bukhari,A., Tabri,N.A., Bahar,B., Hidayah,N.,
            Halik,H. and Massi,M.N.
  TITLE     Serum iron levels in tuberculosis patients and household contacts
            and its association with natural resistance-associated macrophage
            protein 1 polymorphism and expression
  JOURNAL   Clin Respir J 17 (9), 893-904 (2023)
   PUBMED   37607533
  REMARK    GeneRIF: Serum iron levels in tuberculosis patients and household
            contacts and its association with natural resistance-associated
            macrophage protein 1 polymorphism and expression.
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Liu,J., Fujiwara,T.M., Buu,N.T., Sanchez,F.O., Cellier,M.,
            Paradis,A.J., Frappier,D., Skamene,E., Gros,P., Morgan,K. et al.
  TITLE     Identification of polymorphisms and sequence variants in the human
            homologue of the mouse natural resistance-associated macrophage
            protein gene
  JOURNAL   Am J Hum Genet 56 (4), 845-853 (1995)
   PUBMED   7717395
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Blackwell,J.M., Barton,C.H., White,J.K., Searle,S., Baker,A.M.,
            Williams,H. and Shaw,M.A.
  TITLE     Genomic organization and sequence of the human NRAMP gene:
            identification and mapping of a promoter region polymorphism
  JOURNAL   Mol Med 1 (2), 194-205 (1995)
   PUBMED   8529098
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Kishi,F.
  TITLE     Isolation and characterization of human Nramp cDNA
  JOURNAL   Biochem Biophys Res Commun 204 (3), 1074-1080 (1994)
   PUBMED   7980580
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Cellier,M., Govoni,G., Vidal,S., Kwan,T., Groulx,N., Liu,J.,
            Sanchez,F., Skamene,E., Schurr,E. and Gros,P.
  TITLE     Human natural resistance-associated macrophage protein: cDNA
            cloning, chromosomal mapping, genomic organization, and
            tissue-specific expression
  JOURNAL   J Exp Med 180 (5), 1741-1752 (1994)
   PUBMED   7964458
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Vidal,S.M., Malo,D., Vogan,K., Skamene,E. and Gros,P.
  TITLE     Natural resistance to infection with intracellular parasites:
            isolation of a candidate for Bcg
  JOURNAL   Cell 73 (3), 469-485 (1993)
   PUBMED   8490962
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB284801.1, L32185.1,
            AC021016.5 and CA307182.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 19, 2006 this sequence version replaced NP_000569.2.
            
            Summary: This gene is a member of the solute carrier family 11
            (proton-coupled divalent metal ion transporters) family and encodes
            a multi-pass membrane protein. The protein functions as a divalent
            transition metal (iron and manganese) transporter involved in iron
            metabolism and host resistance to certain pathogens. Mutations in
            this gene have been associated with susceptibility to infectious
            diseases such as tuberculosis and leprosy, and inflammatory
            diseases such as rheumatoid arthritis and Crohn disease.
            Alternatively spliced variants that encode different protein
            isoforms have been described but the full-length nature of only one
            has been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.36007.1, D50402.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000233202.11/ ENSP00000233202.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..550
                     /product="natural resistance-associated macrophage protein
                     1"
                     /note="solute carrier family 11 (sodium/phosphate
                     symporters), member 1; NRAMP 1; solute carrier family 11
                     (proton-coupled divalent metal ion transporters), member
                     1; solute carrier family 11 (proton-coupled divalent metal
                     ion transporter), member 1; Leishmaniasis resistance"
                     /calculated_mol_wt=59741
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Region          56..456
                     /region_name="nramp"
                     /note="NRAMP (natural resistance-associated macrophage
                     protein) metal ion transporters; TIGR01197"
                     /db_xref="CDD:162246"
     Site            59..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            86..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            143..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            168..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            241..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            288..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49279.1)"
     Site            338
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49279.1)"
     Site            350..369
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            401..418
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            430..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            467..488
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     Site            497..516
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49279.1)"
     CDS             1..550
                     /gene="SLC11A1"
                     /gene_synonym="LSH; NRAMP; NRAMP1"
                     /coded_by="NM_000578.4:97..1749"
                     /db_xref="CCDS:CCDS2415.1"
                     /db_xref="GeneID:6556"
                     /db_xref="HGNC:HGNC:10907"
                     /db_xref="MIM:600266"
ORIGIN      
        1 mtgdkgpqrl sgssygsiss ptsptspgpq qappretyls ekipipdtkp gtfslrklwa
       61 ftgpgflmsi afldpgnies dlqagavagf kllwvllwat vlgllcqrla arlgvvtgkd
      121 lgevchlyyp kvprtvlwlt ielaivgsdm qevigtaiaf nllsagripl wggvlitivd
      181 tffflfldny glrkleaffg llitimaltf gyeyvvarpe qgallrglfl pscpgcghpe
      241 llqavgivga iimphniylh salvksreid rarradirea nmyflieati alsvsfiinl
      301 fvmavfgqaf yqktnqaafn icansslhdy akifpmnnat vavdiyqggv ilgclfgpaa
      361 lyiwaiglla agqsstmtgt yagqfvmegf lrlrwsrfar vlltrscail ptvlvavfrd
      421 lrdlsglndl lnvlqslllp favlpiltft smptlmqefa ngllnkvvts simvlvcain
      481 lyfvvsylps lphpayfgla allaaaylgl stylvwtccl ahgatflahs shhhflygll
      541 eedqkgetsg
//
LOCUS       NP_032724                284 aa            linear   ROD 27-APR-2025
DEFINITION  protein NipSnap homolog 1 [Mus musculus].
ACCESSION   NP_032724
VERSION     NP_032724.1
DBSOURCE    REFSEQ: accession NM_008698.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Liu,Y., Qu,Y., Cheng,C., Tsai,P.Y., Edwards,K., Xue,S., Pandit,S.,
            Eguchi,S., Sanghera,N. and Barrow,J.J.
  TITLE     Nipsnap1-A regulatory factor required for long-term maintenance of
            non-shivering thermogenesis
  JOURNAL   Mol Metab 75, 101770 (2023)
   PUBMED   37423391
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Princely Abudu,Y., Pankiv,S., Mathai,B.J., Hakon Lystad,A.,
            Bindesboll,C., Brenne,H.B., Yoke Wui Ng,M., Thiede,B., Yamamoto,A.,
            Mutugi Nthiga,T., Lamark,T., Esguerra,C.V., Johansen,T. and
            Simonsen,A.
  TITLE     NIPSNAP1 and NIPSNAP2 Act as 'Eat Me' Signals for Mitophagy
  JOURNAL   Dev Cell 49 (4), 509-525 (2019)
   PUBMED   30982665
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Okuda-Ashitaka,E., Minami,T., Tsubouchi,S., Kiyonari,H.,
            Iwamatsu,A., Noda,T., Handa,H. and Ito,S.
  TITLE     Identification of NIPSNAP1 as a nocistatin-interacting protein
            involving pain transmission
  JOURNAL   J Biol Chem 287 (13), 10403-10413 (2012)
   PUBMED   22311985
  REMARK    GeneRIF: NIPSNAP1 is an interacting molecule of NST and plays a
            crucial role in pain transmission.
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Tummala,H., Li,X. and Homayouni,R.
  TITLE     Interaction of a novel mitochondrial protein,
            4-nitrophenylphosphatase domain and non-neuronal SNAP25-like
            protein homolog 1 (NIPSNAP1), with the amyloid precursor protein
            family
  JOURNAL   Eur J Neurosci 31 (11), 1926-1934 (2010)
   PUBMED   20497468
  REMARK    GeneRIF: Data suggest that amyloid precursor proteins may affect
            mitochondrial function through a direct interaction with NIPSNAP1
            as well as with other mitochondrial proteins.
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Qiu,Y., Cavelier,L., Chiu,S., Yang,X., Rubin,E. and Cheng,J.F.
  TITLE     Human and mouse ABCA1 comparative sequencing and transgenesis
            studies revealing novel regulatory sequences
  JOURNAL   Genomics 73 (1), 66-76 (2001)
   PUBMED   11352567
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Wertz,K. and Herrmann,B.G.
  TITLE     Large-scale screen for genes involved in gonad development
  JOURNAL   Mech Dev 98 (1-2), 51-70 (2000)
   PUBMED   11044607
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Seroussi,E., Pan,H.Q., Kedra,D., Roe,B.A. and Dumanski,J.P.
  TITLE     Characterization of the human NIPSNAP1 gene from 22q12: a member of
            a novel gene family
  JOURNAL   Gene 212 (1), 13-20 (1998)
   PUBMED   9661659
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY712531.1, AK031804.1, AK013140.1 and BP771057.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ001260.1, AK013140.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 3.07 cM"
     Protein         1..284
                     /product="protein NipSnap homolog 1"
                     /note="4-nitrophenylphosphatase domain and non-neuronal
                     SNAP25-like protein homolog 1"
                     /calculated_mol_wt=29593
     transit_peptide 1..35
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O55125.1)"
                     /calculated_mol_wt=3789
     Region          2..15
                     /region_name="SIFI-degron.
                     /evidence=ECO:0000250|UniProtKB:Q9BPW8"
                     /note="propagated from UniProtKB/Swiss-Prot (O55125.1)"
     mat_peptide     36..284
                     /product="Protein NipSnap homolog 1.
                     /evidence=ECO:0000255. /id=PRO_0000221147"
                     /note="propagated from UniProtKB/Swiss-Prot (O55125.1)"
                     /calculated_mol_wt=29593
     Site            65
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (O55125.1)"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (O55125.1)"
     Site            73
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (O55125.1)"
     Site            80
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (O55125.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BPW8; propagated from
                     UniProtKB/Swiss-Prot (O55125.1)"
     Site            143
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (O55125.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (O55125.1)"
     Region          185..282
                     /region_name="NIPSNAP"
                     /note="pfam07978"
                     /db_xref="CDD:429767"
     Site            191
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (O55125.1)"
     Site            193
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (O55125.1)"
     Site            279
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (O55125.1)"
     CDS             1..284
                     /gene="Nipsnap1"
                     /coded_by="NM_008698.3:56..910"
                     /db_xref="CCDS:CCDS24392.1"
                     /db_xref="GeneID:18082"
                     /db_xref="MGI:MGI:1278344"
ORIGIN      
        1 maprlciisa aarrlftkpr pragdlaaag avrfyskdse gswfrslfvh kvdprkdahs
       61 tllskketsn lykiqfhnvk pecldaynsl teavlpklhl dedypcslvg nwntwygeqd
      121 qavhlwrfsg gypalmdcmn klknnkeyle frkerskmll srrnqlllef sfwnepqpra
      181 gpniyelrty klkpgtmiew gnnwaraiky rqenqeavgg ffsqigelyv vhhlwaykdl
      241 qsreetrnaa wrkrgwdenv yytvplvrhm esrimiplki splq
//
LOCUS       NP_001348970             559 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 17 [Mus musculus].
ACCESSION   NP_001348970
VERSION     NP_001348970.1
DBSOURCE    REFSEQ: accession NM_001362041.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 559)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 559)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 559)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..559
                     /product="cAMP-regulated phosphoprotein 21 isoform 17"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=59554
     Region          <5..35
                     /region_name="SUZ"
                     /note="SUZ domain; pfam12752"
                     /db_xref="CDD:463689"
     Region          305..>534
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..559
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362041.1:1354..3033"
                     /note="isoform 17 is encoded by transcript variant 51"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mnrmhpfrdd rrsksieere eeyqrvreri fahdsvcsqe slfldnrahr dssgrtsgsr
       61 qsssetelrw pdhqrawsst dsdssnrnlk ptmtktasfg gitvltrgds tsstrsagkl
      121 sktgsessss agssgslsrt hpqstaltss vaagspgcma ysengmggqv ppsstsyill
      181 plesatgipp gsillnphtg qpfvnpdgtp aiynppgsqq tlrgtvggqp qqppqqqpsp
      241 qpqqqvqasq pqmagplvtq svqslqpssq svqypavsfp pqhllpmspt qhfplreela
      301 aqfsqlsmsr qssgdtpepp sgtvypasll pqtaqpqsyv itsagqqlst ggfsdsgppi
      361 sqqvlqapps pqgfvqqppp aqmsvyyyps gqyptstsqq yrplasvqys aqrsqqipqt
      421 tqqagyqpvl sgqqgfqgmm gvqqsahsqg vmssqqgapv hgvmvsyptm ssyqvpmtqg
      481 sqavpqqtyq ppimlpsqag qgslpatgmp vycnvtppnp qnnlrlmgph cpsstvpvms
      541 ascrtncgnv snagwqvkf
//
LOCUS       NP_057280                960 aa            linear   PRI 27-APR-2025
DEFINITION  probable RNA-binding protein 19 [Homo sapiens].
ACCESSION   NP_057280 NP_055667 XP_947767 XP_951306 XP_951307 XP_951308
VERSION     NP_057280.2
DBSOURCE    REFSEQ: accession NM_016196.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 960)
  AUTHORS   Xie,T., Deng,L., Mei,P., Zhou,Y., Wang,B., Zhang,J., Lin,J.,
            Wei,Y., Zhang,X. and Xu,R.
  TITLE     Genome-wide association study combining pathway analysis for
            typical sporadic amyotrophic lateral sclerosis in Chinese Han
            populations
  JOURNAL   Neurobiol Aging 35 (7), 1778 (2014)
   PUBMED   24529757
REFERENCE   2  (residues 1 to 960)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 960)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 960)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 960)
  AUTHORS   Lorenzen,J.A., Bonacci,B.B., Palmer,R.E., Wells,C., Zhang,J.,
            Haber,D.A., Goldstein,A.M. and Mayer,A.N.
  TITLE     Rbm19 is a nucleolar protein expressed in crypt/progenitor cells of
            the intestinal epithelium
  JOURNAL   Gene Expr Patterns 6 (1), 45-56 (2005)
   PUBMED   16027046
REFERENCE   6  (residues 1 to 960)
  AUTHORS   Mayer,A.N. and Fishman,M.C.
  TITLE     Nil per os encodes a conserved RNA recognition motif protein
            required for morphogenesis and cytodifferentiation of digestive
            organs in zebrafish
  JOURNAL   Development 130 (17), 3917-3928 (2003)
   PUBMED   12874115
  REMARK    GeneRIF: Primarily a zebrafish paper but shows an alignment of
            human RBM19
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB096676.1, AL117547.1,
            AC090669.9 and AC009731.6.
            
            On Apr 10, 2009 this sequence version replaced NP_057280.1.
            
            Summary: This gene encodes a nucleolar protein that contains six
            RNA-binding motifs. The encoded protein may be involved in
            regulating ribosome biogenesis. Multiple alternatively spliced
            variants, encoding the same protein, have been identified.[provided
            by RefSeq, Apr 2009].
            
            Transcript Variant: This variant (2) differs in the 3' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL117547.1, SRR1803611.237233.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261741.10/ ENSP00000261741.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..960
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.13-q24.21"
     Protein         1..960
                     /product="probable RNA-binding protein 19"
                     /calculated_mol_wt=107201
     Region          2..77
                     /region_name="RRM1_RBM19"
                     /note="RNA recognition motif 1 (RRM1) found in RNA-binding
                     protein 19 (RBM19) and similar proteins; cd12564"
                     /db_xref="CDD:409980"
     Region          85..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4C8.3)"
     Region          149..294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4C8.3)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C8.3)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C8.3)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C8.3)"
     Region          294..365
                     /region_name="RRM2_RMB19"
                     /note="RNA recognition motif 2 (RRM2) found in RNA-binding
                     protein 19 (RBM19) and similar proteins; cd12502"
                     /db_xref="CDD:409925"
     Region          400..478
                     /region_name="RRM3_RBM19"
                     /note="RNA recognition motif 3 (RRM3) found in RNA-binding
                     protein 19 (RBM19) and similar proteins; cd12567"
                     /db_xref="CDD:409983"
     Region          491..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4C8.3)"
     Region          587..658
                     /region_name="RRM4_RBM19"
                     /note="RNA recognition motif 4 (RRM4) found in RNA-binding
                     protein 19 (RBM19) and similar proteins; cd12569"
                     /db_xref="CDD:409984"
     Region          667..729
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4C8.3)"
     Region          730..809
                     /region_name="RRM5_RBM19_like"
                     /note="RNA recognition motif 5 (RRM5) found in RNA-binding
                     protein 19 (RBM19 or RBD-1) and similar proteins; cd12318"
                     /db_xref="CDD:409757"
     Region          832..910
                     /region_name="RRM6_RBM19"
                     /note="RNA recognition motif 6 (RRM6) found in RNA-binding
                     protein 19 (RBM19) and similar proteins; cd12571"
                     /db_xref="CDD:409985"
     Site            936
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C8.3)"
     Site            949
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C8.3)"
     Site            951
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C8.3)"
     CDS             1..960
                     /gene="RBM19"
                     /gene_synonym="Mrd1"
                     /coded_by="NM_016196.4:99..2981"
                     /db_xref="CCDS:CCDS9172.1"
                     /db_xref="GeneID:9904"
                     /db_xref="HGNC:HGNC:29098"
                     /db_xref="MIM:616444"
ORIGIN      
        1 msrlivknlp ngmkeerfrq lfaafgtltd cslkftkdgk frkfgfigfk seeeaqkaqk
       61 hfnksfidts ritvefcksf gdpakpraws khaqkpsqpk qppkdsttpe ikkdekkkkv
      121 agqleklked tefqeflsvh qrraqaatwa ndgldaepsk gkskpasdyl nfdsdsgqes
      181 eeegagedle eeaslepkaa vqkelsdmdy lkskmvkags sssseeeese deavhcdegs
      241 eaeeedssat pvlqerdskg agqeqgmpag kkrppearae tekpanqkep ttchtvklrg
      301 apfnvteknv meflaplkpv airivrnahg nktgyifvdf sneeevkqal kcnreymggr
      361 yievfreknv pttkgapknt tkswqgrilg eneeeedlae sgrlfvrnlp ytsteedlek
      421 lfskygplse lhypidsltk kpkgfafitf mfpehavkay sevdgqvfqg rmlhvlpsti
      481 kkeasedasa lgsssykkkk eaqdkansas shnwntlfmg pnavadaiaq kynatksqvf
      541 dhetkgsvav rvalgetqlv qevrrflidn gvsldsfsqa aaersktvil vknlpagtla
      601 aqlqetfghf gslgrvllpe ggitaivefl eplearkafr hlayskfhhv plylewapvg
      661 vfsstapqkk klqdtpsepm ekdpaepetv pdgetpeden pteegadnss akmeeeeeee
      721 eeeeeslpgc tlfiknlnfd tteeklkevf skvgtvkscs iskkknkagv llsmgfgfve
      781 yrkpeqaqka lkqlqghvvd ghklevrise ratkpavtla rkkqvprkqt tskilvrnip
      841 fqahsreire lfstfgelkt vrlpkkmtgt gthrgfgfvd fltkqdakra fnalchsthl
      901 ygrrlvlewa dsevtlqalr rktaahfhep pkkkrsvvld eileqlegsd sdseeqtlql
//
LOCUS       NP_001357379             426 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 577 isoform b [Homo sapiens].
ACCESSION   NP_001357379 XP_016882876
VERSION     NP_001357379.1
DBSOURCE    REFSEQ: accession NM_001370450.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Lorenzo,P.M., Izquierdo,A.G., Diaz-Lagares,A., Carreira,M.C.,
            Macias-Gonzalez,M., Sandoval,J., Cueva,J., Lopez-Lopez,R.,
            Casanueva,F.F. and Crujeiras,A.B.
  TITLE     ZNF577 Methylation Levels in Leukocytes From Women With Breast
            Cancer Is Modulated by Adiposity, Menopausal State, and the
            Mediterranean Diet
  JOURNAL   Front Endocrinol (Lausanne) 11, 245 (2020)
   PUBMED   32390948
  REMARK    GeneRIF: ZNF577 Methylation Levels in Leukocytes From Women With
            Breast Cancer Is Modulated by Adiposity, Menopausal State, and the
            Mediterranean Diet.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK093036.1, AL832871.1, AK291812.1, AK289479.1, AI004737.1 and
            AC074141.3.
            
            On May 8, 2019 this sequence version replaced XP_016882876.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.70575.1,
                                           SRR1803615.159654.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2162568
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..426
                     /product="zinc finger protein 577 isoform b"
                     /calculated_mol_wt=48239
     Region          25..83
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          97..>158
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          101..121
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          129..149
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <135..340
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          157..177
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(162,164,166,168..169,172..173,176,190,192,196..197,
                     200..201,204,218,220,222,224..225,228..229,232)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          185..205
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          213..233
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          241..261
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(246,248,250,252..253,256..257,260,274,276,280..281,
                     284..285,288,302,304,306,308..309,312..313,316)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          269..289
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          297..317
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..426
                     /gene="ZNF577"
                     /coded_by="NM_001370450.1:1350..2630"
                     /note="isoform b is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS46160.1"
                     /db_xref="GeneID:84765"
                     /db_xref="HGNC:HGNC:28673"
ORIGIN      
        1 mknativmsv rreqgsssge gslsfedvav gftreewqfl dqsqkvlyke vmlenyinlv
       61 sigyrgtkpd slfkleqgep pgiaegaahs qicpggkphe csvcgrafsr kaqliqhqrt
      121 ergekphgcg ecgktfmrki qltehqrtht gekphecsec gkafsrksql mvhqrthtge
      181 kpyrcskcgk afsrkcrlnr hqrshtgekl ygcsvcgkaf sqkayltahq rlhtgdkpyk
      241 csdcgrtfyf ksdltrhqri htgekpyecs ecekafrsks kliqhqrtht gerpyscrec
      301 gkafahmsvl ikhekthire tainsltvek pssrshtsly mseliqeqkt vntvpiemps
      361 sgtppllnks erlvgrnvvi veqpfprnqa fvvnqefeqr isltnevnva psvinyilyl
      421 tdivse
//
LOCUS       NP_114032                825 aa            linear   PRI 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein U isoform a [Homo sapiens].
ACCESSION   NP_114032
VERSION     NP_114032.2
DBSOURCE    REFSEQ: accession NM_031844.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Lee,F.F.Y., Harris,C. and Alper,S.
  TITLE     RNA Binding Proteins that Mediate LPS-induced Alternative Splicing
            of the MyD88 Innate Immune Regulator
  JOURNAL   J Mol Biol 436 (8), 168497 (2024)
   PUBMED   38369277
  REMARK    GeneRIF: RNA Binding Proteins that Mediate LPS-induced Alternative
            Splicing of the MyD88 Innate Immune Regulator.
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Wu,X., Cao,C., Li,Z., Xie,Y., Zhang,S., Sun,W. and Guo,J.
  TITLE     Circular RNA CircSLC22A23 Promotes Gastric Cancer Progression by
            Activating HNRNPU Expression
  JOURNAL   Dig Dis Sci 69 (4), 1200-1213 (2024)
   PUBMED   38400886
  REMARK    GeneRIF: Circular RNA CircSLC22A23 Promotes Gastric Cancer
            Progression by Activating HNRNPU Expression.
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Wang,X., Xu,J., Li,Q., Zhang,Y., Lin,Z., Zhai,X., Wang,F.,
            Huang,J., Gao,Q., Wen,J., Li,L., Feng,Y., Luo,H., Li,Q., Liu,X.,
            Li,J., Zhao,F., Zhang,L., Niu,T., Sun,C. and Zheng,Y.
  TITLE     RNA-binding protein hnRNPU regulates multiple myeloma resistance to
            selinexor
  JOURNAL   Cancer Lett 580, 216486 (2024)
   PUBMED   37984724
  REMARK    GeneRIF: RNA-binding protein hnRNPU regulates multiple myeloma
            resistance to selinexor.
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Liu,W., Fang,S., Yang,Z., Ma,J., Tan,Y., Chen,Y., Zhang,K., Liu,K.
            and Gu,W.
  TITLE     ITGA9-AS1 up-regulates ITGA9 by targeting miR-4765 and recruiting
            HNRNPU to affect the proliferation and apoptosis of non-small cell
            lung cancer cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (14), 22-28 (2023)
   PUBMED   38279497
  REMARK    GeneRIF: ITGA9-AS1 up-regulates ITGA9 by targeting miR-4765 and
            recruiting HNRNPU to affect the proliferation and apoptosis of
            non-small cell lung cancer cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Li,H., Jiao,W., Song,J., Wang,J., Chen,G., Li,D., Wang,X., Bao,B.,
            Du,X., Cheng,Y., Yang,C., Tong,Q. and Zheng,L.
  TITLE     circ-hnRNPU inhibits NONO-mediated c-Myc transactivation and mRNA
            stabilization essential for glycosylation and cancer progression
  JOURNAL   J Exp Clin Cancer Res 42 (1), 313 (2023)
   PUBMED   37993881
  REMARK    GeneRIF: circ-hnRNPU inhibits NONO-mediated c-Myc transactivation
            and mRNA stabilization essential for glycosylation and cancer
            progression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Barel,M., Balbo,M., Gauffre,A. and Frade,R.
  TITLE     Binding sites of the Epstein-Barr virus and C3d receptor (CR2,
            CD21) for its three intracellular ligands, the p53
            anti-oncoprotein, the p68 calcium binding protein and the nuclear
            p120 ribonucleoprotein
  JOURNAL   Mol Immunol 32 (6), 389-397 (1995)
   PUBMED   7753047
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Sidorenko,S.P., Law,C.L., Chandran,K.A. and Clark,E.A.
  TITLE     Human spleen tyrosine kinase p72Syk associates with the Src-family
            kinase p53/56Lyn and a 120-kDa phosphoprotein
  JOURNAL   Proc Natl Acad Sci U S A 92 (2), 359-363 (1995)
   PUBMED   7831290
REFERENCE   8  (residues 1 to 825)
  AUTHORS   Fackelmayer,F.O. and Richter,A.
  TITLE     hnRNP-U/SAF-A is encoded by two differentially polyadenylated mRNAs
            in human cells
  JOURNAL   Biochim Biophys Acta 1217 (2), 232-234 (1994)
   PUBMED   7509195
REFERENCE   9  (residues 1 to 825)
  AUTHORS   Balasubramanian,M.
  TITLE     HNRNPU-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35274911
REFERENCE   10 (residues 1 to 825)
  AUTHORS   Kiledjian,M. and Dreyfuss,G.
  TITLE     Primary structure and binding activity of the hnRNP U protein:
            binding RNA through RGG box
  JOURNAL   EMBO J 11 (7), 2655-2664 (1992)
   PUBMED   1628625
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323046.3, AF068846.1,
            BC024767.1, BC015782.1 and AK095525.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 6, 2005 this sequence version replaced NP_114032.1.
            
            Summary: This gene encodes a member of a family of proteins that
            bind nucleic acids and function in the formation of
            ribonucleoprotein complexes in the nucleus with heterogeneous
            nuclear RNA (hnRNA). The encoded protein has affinity for both RNA
            and DNA, and binds scaffold-attached region (SAR) DNA. Mutations in
            this gene have been associated with epileptic encephalopathy, early
            infantile, 54. A pseudogene of this gene has been identified on
            chromosome 14. [provided by RefSeq, Jun 2017].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3396444.1,
                                           SRR14038197.1276289.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000640218.2/ ENSP00000491215.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..825
                     /product="heterogeneous nuclear ribonucleoprotein U
                     isoform a"
                     /note="p120 nuclear protein; heterogeneous nuclear
                     ribonucleoprotein U (scaffold attachment factor A);
                     nuclear p120 ribonucleoprotein; HNRNPU antisense RNA 1"
                     /calculated_mol_wt=90454
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine, partial.
                     /evidence=ECO:0000269|Ref.7, ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q00839.6)"
     Region          8..42
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Site            17
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Region          41..281
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00839.6)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:25986610,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q00839.6)"
     Site            100..101
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000269|PubMed:10671544,
                     ECO:0000269|PubMed:9405365; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            186
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            215
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q00839.6)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Region          288..463
                     /region_name="SPRY_hnRNP"
                     /note="SPRY domain in heterogeneous nuclear
                     ribonucleoprotein U-like (hnRNP) protein 1; cd12884"
                     /db_xref="CDD:293942"
     Site            352
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Region          488..672
                     /region_name="ATPase domain.
                     /evidence=ECO:0000269|PubMed:28622508"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00839.6)"
     Region          499..643
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
     Site            516
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            524
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            551
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            565
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            582
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Region          611..626
                     /region_name="Actin-binding.
                     /evidence=ECO:0000269|PubMed:15711563"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00839.6)"
     Site            635
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Region          671..749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00839.6)"
     Site            702
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Region          714..739
                     /region_name="RNA-binding RGG-box.
                     /evidence=ECO:0000269|PubMed:14608463,
                     ECO:0000269|PubMed:1628625"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00839.6)"
     Site            715
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            720
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            727
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            733
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            739
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; Dimethylated
                     arginine, in A2780 ovarian carcinoma cell line.
                     /evidence=ECO:0000269|Ref.8; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (Q00839.6)"
     Site            755
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Site            762
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     Region          769..799
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00839.6)"
     Site            814
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00839.6)"
     CDS             1..825
                     /gene="HNRNPU"
                     /gene_synonym="DEE54; EIEE54; GRIP120; hnRNP U;
                     HNRNPU-AS1; HNRPU; pp120; SAF-A; SAFA; U21.1"
                     /coded_by="NM_031844.3:237..2714"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41479.1"
                     /db_xref="GeneID:3192"
                     /db_xref="HGNC:HGNC:5048"
                     /db_xref="MIM:602869"
ORIGIN      
        1 mssspvnvkk lkvselkeel kkrrlsdkgl kaelmerlqa alddeeaggr pamepgngsl
       61 dlggdsagrs gagleqeaaa ggdeeeeeee eeeegisald gdqmelgeen gaagaadsgp
      121 meeeeaased engddqgfqe gedelgdeee gagdenghge qqpqppatqq qqpqqqrgaa
      181 keaagkssgp tslfavtvap pgarqgqqqa ggkkkaeggg gggrpgapaa gdgkteqkgg
      241 dkkrgvkrpr edhgrgyfey ieenkysrak spqppveeed ehfddtvvcl dtyncdlhfk
      301 isrdrlsass ltmesfaflw aggrasygvs kgkvcfemkv tekipvrhly tkdidihevr
      361 igwslttsgm llgeeefsyg yslkgiktcn cetedygekf dendvitcfa nfesdevels
      421 yakngqdlgv afkiskevla grplfphvlc hncavefnfg qkekpyfpip eeytfiqnvp
      481 ledrvrgpkg peekkdcevv mmiglpgagk ttwvtkhaae npgkynilgt ntimdkmmva
      541 gfkkqmadtg klntllqrap qclgkfieia arkkrnfild qtnvsaaaqr rkmclfagfq
      601 rkavvvcpkd edykqrtqkk aevegkdlpe havlkmkgnf tlpevaecfd eityvelqke
      661 eaqklleqyk eeskkalppe kkqntgskks nknksgknqf nrggghrgrg gfnmrggnfr
      721 ggapgnrggy nrrgnmpqrg gggggsggig ypyprapvfp grgsysnrgn ynrggmpnrg
      781 nynqnfrgrg nnrgyknqsq gynqwqqgqf wgqkpwsqhy hqgyy
//
LOCUS       NP_001353495             821 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001353495 XP_016855515
VERSION     NP_001353495.1
DBSOURCE    REFSEQ: accession NM_001366566.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 821)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 821)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 821)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 821)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 821)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855515.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.37790.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..821
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 4"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=92527
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <523..>657
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..821
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366566.1:405..2870"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels eseedkggkm aaadsvqqrr qyrrqnqqss sdsgssssse
      421 derpkrshvk ngevgrrrrh spsrsaspsp rkrqketspr grrrrspspp ptrrrrspsp
      481 appprrrrtp tppprrrtps ppprrrspsp rrysppiqrr yspspppkrr taspppppkr
      541 raspspppkr rvshspppkq rsspvtkrrs pslsskhrkg sspsrstrea rspqpnkrhs
      601 psprprapqt ssspppvrrg assspqrrqs pspstrpirr vsrtpepkki kkaaspspqs
      661 vrrvsssrsv sgspepaakk ppappspvqs qspstnwspa vpvkkakspt pspspprnsd
      721 qegggkkkkk kkdkkhkkdk khkkhkkhkk ekavaaaaaa avtpaaiaaa tttlaqeepv
      781 aapepkkete seaednlddl ekhlrekalr smrkaqvspq s
//
LOCUS       NP_006834                328 aa            linear   PRI 27-APR-2025
DEFINITION  L-serine dehydratase/L-threonine deaminase [Homo sapiens].
ACCESSION   NP_006834
VERSION     NP_006834.2
DBSOURCE    REFSEQ: accession NM_006843.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Wang,Y. and Tatakis,D.N.
  TITLE     Human gingiva transcriptome during wound healing
  JOURNAL   J Clin Periodontol 44 (4), 394-402 (2017)
   PUBMED   28005267
  REMARK    GeneRIF: SDS expression is significantly upregulated in human
            masticatory mucosa during wound healing
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Wang,C.Y., Ku,S.C., Lee,C.C. and Wang,A.H.
  TITLE     Modulating the function of human serine racemase and human serine
            dehydratase by protein engineering
  JOURNAL   Protein Eng Des Sel 25 (11), 741-749 (2012)
   PUBMED   23112234
  REMARK    GeneRIF: S84A serine racemase mutant behaved like serine
            dehydratase, whereas A65S serine dehydratase mutant acquired an
            additional function of using D-serine as a substrate.
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Yamada,T., Komoto,J., Kasuya,T., Takata,Y., Ogawa,H., Mori,H. and
            Takusagawa,F.
  TITLE     A catalytic mechanism that explains a low catalytic activity of
            serine dehydratase like-1 from human cancer cells: crystal
            structure and site-directed mutagenesis studies
  JOURNAL   Biochim Biophys Acta 1780 (5), 809-818 (2008)
   PUBMED   18342636
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Szaflik,J.P., Majsterek,I., Kowalski,M., Rusin,P., Sobczuk,A.,
            Borucka,A.I., Szaflik,J. and Blasiak,J.
  TITLE     Association between sorbitol dehydrogenase gene polymorphisms and
            type 2 diabetic retinopathy
  JOURNAL   Exp Eye Res 86 (4), 647-652 (2008)
   PUBMED   18289528
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Ogawa,H., Gomi,T., Konishi,K., Date,T., Nakashima,H., Nose,K.,
            Matsuda,Y., Peraino,C., Pitot,H.C. and Fujioka,M.
  TITLE     Human liver serine dehydratase. cDNA cloning and sequence homology
            with hydroxyamino acid dehydratases from other sources
  JOURNAL   J Biol Chem 264 (27), 15818-15823 (1989)
   PUBMED   2674117
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Akopov,M.A., Kagan,Z.C., Berezov,T.T. and Filiptsev,P.Ia.
  TITLE     [Kinetic and allosteric properties of L-threonine-L-serine
            dehydratase from human liver]
  JOURNAL   Biokhimiia 44 (2), 282-292 (1979)
   PUBMED   435568
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Akopov,M.A., Kagan,Z.S., Berezov,T.T. and Filiptsev,P.Ia.
  TITLE     [Detection and properties of L-threonine-L-serine dehydratase in
            human liver]
  JOURNAL   Biokhimiia 43 (10), 1860-1872 (1978)
   PUBMED   31199
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Kitagawa,T. and Pitot,H.C.
  TITLE     The regulation of serine dehydratase and glucose-6-phosphatase in
            hyperplastic nodules of rat liver during diethylnitrosamine and
            N-2-fluorenylacetamide feeding
  JOURNAL   Cancer Res 35 (4), 1075-1084 (1975)
   PUBMED   163697
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Kitagawa,T. and Pitot,H.C.
  TITLE     Immunohistochemical demonstration of serine dehydratase in rat
            liver
  JOURNAL   Am J Pathol 78 (2), 309-318 (1975)
   PUBMED   163593
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG534053.1, BC020750.1,
            BG566257.1, J05037.1 and BU740747.1.
            
            On Aug 7, 2003 this sequence version replaced NP_006834.1.
            
            Summary: This gene encodes one of three enzymes that are involved
            in metabolizing serine and glycine. L-serine dehydratase converts
            L-serine to pyruvate and ammonia and requires pyridoxal phosphate
            as a cofactor. The encoded protein can also metabolize threonine to
            NH4+ and 2-ketobutyrate. The encoded protein is found predominantly
            in the liver. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.600160.1,
                                           SRR5189664.1638.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257549.9/ ENSP00000257549.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.13"
     Protein         1..328
                     /product="L-serine dehydratase/L-threonine deaminase"
                     /EC_number="4.3.1.17"
                     /EC_number="4.3.1.19"
                     /note="L-serine deaminase; L-serine dehydratase; L-serine
                     ammonia-lyase; TDH; L-threonine dehydratase; hepatic
                     serine dehydratase"
                     /calculated_mol_wt=34494
     Region          10..320
                     /region_name="L-Ser-dehyd"
                     /note="Serine dehydratase is a pyridoxal phosphate
                     (PLP)-dependent enzyme which catalyzes the conversion of
                     L-, D-serine, or L-threonine to pyruvate/ketobutyrate and
                     ammonia; cd06448"
                     /db_xref="CDD:107209"
     Site            order(41,67,168..172)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107209"
     Site            41
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107209"
     CDS             1..328
                     /gene="SDS"
                     /gene_synonym="hSDH; SDH"
                     /coded_by="NM_006843.3:123..1109"
                     /db_xref="CCDS:CCDS9169.1"
                     /db_xref="GeneID:10993"
                     /db_xref="HGNC:HGNC:10691"
                     /db_xref="MIM:182128"
ORIGIN      
        1 mmsgeplhvk tpirdsmals kmagtsvylk mdsaqpsgsf kirgighfck rwakqgcahf
       61 vcssagnagm aaayaarqlg vpativvpst tpaltierlk negatvkvvg elldeafela
      121 kalaknnpgw vyippfddpl iweghasivk elketlwekp gaialsvggg gllcgvvqgl
      181 qevgwgdvpv iametfgahs fhaattagkl vslpkitsva kalgvktvga qalklfqehp
      241 ifsevisdqe avaaiekfvd dekilvepac gaalaavysh viqklqlegn lrtplpslvv
      301 ivcggsnisl aqlralkeql gmtnrlpk
//
LOCUS       NP_861447                942 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear receptor coactivator 7 isoform 1 [Homo sapiens].
ACCESSION   NP_861447
VERSION     NP_861447.3
DBSOURCE    REFSEQ: accession NM_181782.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Wang,L., Wei,Z., Wu,Y., Hu,X., Zhou,L., Zhao,M., Sun,A., Shao,G.,
            Yang,W. and Lin,Q.
  TITLE     Nuclear receptor coactivator 7 (NCOA7) protects cancer cells from
            oxidative damage through its ERbd domain
  JOURNAL   Cell Signal 124, 111382 (2024)
   PUBMED   39243920
  REMARK    GeneRIF: Nuclear receptor coactivator 7 (NCOA7) protects cancer
            cells from oxidative damage through its ERbd domain.
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Guo,J., Ke,S., Chen,Q., Zhou,J., Guo,J. and Qiu,T.
  TITLE     NCOA7 Regulates Growth and Metastasis of Clear Cell Renal Cell
            Carcinoma via MAPK/ERK Signaling Pathway
  JOURNAL   Int J Mol Sci 24 (14), 11584 (2023)
   PUBMED   37511343
  REMARK    GeneRIF: NCOA7 Regulates Growth and Metastasis of Clear Cell Renal
            Cell Carcinoma via MAPK/ERK Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   4  (residues 1 to 942)
  AUTHORS   Khan,H., Winstone,H., Jimenez-Guardeno,J.M., Graham,C.,
            Doores,K.J., Goujon,C., Matthews,D.A., Davidson,A.D., Rihn,S.J.,
            Palmarini,M., Neil,S.J.D. and Malim,M.H.
  TITLE     TMPRSS2 promotes SARS-CoV-2 evasion from NCOA7-mediated restriction
  JOURNAL   PLoS Pathog 17 (11), e1009820 (2021)
   PUBMED   34807954
  REMARK    GeneRIF: TMPRSS2 promotes SARS-CoV-2 evasion from NCOA7-mediated
            restriction.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 942)
  AUTHORS   Arnaud-Arnould,M., Tauziet,M., Moncorge,O., Goujon,C. and Blaise,M.
  TITLE     Crystal structure of the TLDc domain of human NCOA7-AS
  JOURNAL   Acta Crystallogr F Struct Biol Commun 77 (Pt 8), 230-237 (2021)
   PUBMED   34341188
  REMARK    GeneRIF: Crystal structure of the TLDc domain of human NCOA7-AS.
REFERENCE   6  (residues 1 to 942)
  AUTHORS   Rushing,S.R. and Denison,M.S.
  TITLE     The silencing mediator of retinoic acid and thyroid hormone
            receptors can interact with the aryl hydrocarbon (Ah) receptor but
            fails to repress Ah receptor-dependent gene expression
  JOURNAL   Arch Biochem Biophys 403 (2), 189-201 (2002)
   PUBMED   12139968
REFERENCE   7  (residues 1 to 942)
  AUTHORS   Shao,W., Halachmi,S. and Brown,M.
  TITLE     ERAP140, a conserved tissue-specific nuclear receptor coactivator
  JOURNAL   Mol Cell Biol 22 (10), 3358-3372 (2002)
   PUBMED   11971969
  REMARK    GeneRIF: ERAP140 may represent a distinct class of nuclear receptor
            coactivators.  ERAP140 is recruited by estrogen-bound ER alpha to
            the promoter region of endogenous ER alpha target genes in a cyclic
            pattern similar to that of other coactivators.
REFERENCE   8  (residues 1 to 942)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 942)
  AUTHORS   Nguyen,T.A., Hoivik,D., Lee,J.E. and Safe,S.
  TITLE     Interactions of nuclear receptor coactivator/corepressor proteins
            with the aryl hydrocarbon receptor complex
  JOURNAL   Arch Biochem Biophys 367 (2), 250-257 (1999)
   PUBMED   10395741
REFERENCE   10 (residues 1 to 942)
  AUTHORS   Halachmi,S., Marden,E., Martin,G., MacKay,H., Abbondanza,C. and
            Brown,M.
  TITLE     Estrogen receptor-associated proteins: possible mediators of
            hormone-induced transcription
  JOURNAL   Science 264 (5164), 1455-1458 (1994)
   PUBMED   8197458
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA770225.1, BC137094.1, AK294558.1, BX537385.1, AL834442.1 and
            AL035689.26.
            
            On Mar 27, 2008 this sequence version replaced NP_861447.2.
            
            Transcript Variant: This variant (1) and variants 3 and 4 encode
            the same longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX537385.1, SRR1660807.23561.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392477.7/ ENSP00000376269.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31-q22.32"
     Protein         1..942
                     /product="nuclear receptor coactivator 7 isoform 1"
                     /note="estrogen receptor associated protein 140 kDa;
                     putative protein product of Nbla00052; putative protein
                     product of Nbla10993; estrogen nuclear receptor
                     coactivator 1; 140 kDa estrogen receptor-associated
                     protein; TBC/LysM-associated domain containing 4"
                     /calculated_mol_wt=106031
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI08.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Region          11..158
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Region          161..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI08.2)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6DFV7; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Region          324..416
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI08.2)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Site            500
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6DFV7; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI08.2)"
     Region          780..942
                     /region_name="TLDc"
                     /note="domain in TBC and LysM domain containing proteins;
                     smart00584"
                     /db_xref="CDD:214733"
     CDS             1..942
                     /gene="NCOA7"
                     /gene_synonym="dJ187J11.3; ERAP140; ESNA1; Nbla00052;
                     Nbla10993; NCOA7-AS; TLDC4"
                     /coded_by="NM_181782.5:173..3001"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5132.1"
                     /db_xref="GeneID:135112"
                     /db_xref="HGNC:HGNC:21081"
                     /db_xref="MIM:609752"
ORIGIN      
        1 mdtkeekker kqsyfarlkk kkqakqnaet asavatrtht gkednntvvl epdkcniave
       61 eeymtdekkk rksnqlkeir rtelkryysi ddnqnkthdk kekkmvvqkp hgtmeytagn
      121 qdtlnsialk fnitpnklve lnklfthtiv pgqvlfvpda nspsstlrls ssspgatvsp
      181 sssdaeydkl pdadlarkal kpiervlsst seedepgvvk flkmncryft dgkgvvggvm
      241 ivtpnnimfd phksdplvie ngceeyglic pmeevvsial yndishmkik dalpsdlpqd
      301 lcplyrpgew edlasekdin pfskfksink ekrqqngeki mtsdsrpivp lekstghtpt
      361 kpsgssvsek lkkldssret shgsptvtkl skepsdtssa festakenfl gedddfvdle
      421 elssqtgggm hkkdtlkecl sldpeerkka esqinnsave mqvqsalafl gtendvelkg
      481 aldletcekq dimpevdkqs gspesrvent lnihedldkv klieyyltkn kegpqvsenl
      541 qktelsdgks iepggiditl ssslsqagdp itegnkepdk twvkkgeplp vklnsstean
      601 vikealdssl estldnscqg aqmdnksevq lwllkriqvp iedilpskee ksktppmflc
      661 ikvgkpmrks fathtaamvq qygkrrkqpe ywfavprerv dhlytffvqw spdvygkdak
      721 eqgfvvveke elnmidnffs epttksweii tveeakrrks tcsyyedede evlpvlrphs
      781 allenmhieq larrlparvq gypwrlayst lehgtslktl yrksasldsp vllvikdmdn
      841 qifgayathp fkfsdhyygt getflytfsp hfkvfkwsge nsyfingdis slelgggggr
      901 fglwldadly hgrsnscstf nndilskked fivqdlevwa fd
//
LOCUS       NP_057326                261 aa            linear   PRI 27-APR-2025
DEFINITION  endomucin isoform 1 precursor [Homo sapiens].
ACCESSION   NP_057326
VERSION     NP_057326.2
DBSOURCE    REFSEQ: accession NM_016242.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Brookins,E., Serrano,S.E., Hyder,Z., Yacu,G.S., Finer,G. and
            Thomson,B.R.
  TITLE     Non-endothelial expression of endomucin in the mouse and human
            choroid
  JOURNAL   Exp Eye Res 247, 110054 (2024)
   PUBMED   39153592
  REMARK    GeneRIF: Non-endothelial expression of endomucin in the mouse and
            human choroid.
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Cano,I., Wild,M., Gupta,U., Chaudhary,S., Ng,Y.S.E.,
            Saint-Geniez,M., D'Amore,P.A. and Hu,Z.
  TITLE     Endomucin selectively regulates vascular endothelial growth factor
            receptor-2 endocytosis through its interaction with AP2
  JOURNAL   Cell Commun Signal 22 (1), 225 (2024)
   PUBMED   38605348
  REMARK    GeneRIF: Endomucin selectively regulates vascular endothelial
            growth factor receptor-2 endocytosis through its interaction with
            AP2.
            Erratum:[Cell Commun Signal. 2024 Jun 6;22(1):311. doi:
            10.1186/s12964-024-01696-6. PMID: 38844932]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Wang,S., Jin,J., Chen,J. and Lou,W.
  TITLE     MUC14-Related ncRNA-mRNA Network in Breast Cancer
  JOURNAL   Genes (Basel) 12 (11), 1677 (2021)
   PUBMED   34828282
  REMARK    GeneRIF: MUC14-Related ncRNA-mRNA Network in Breast Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Hu,Z., Cano,I., Saez-Torres,K.L., LeBlanc,M.E., Saint-Geniez,M.,
            Ng,Y.S., Argueso,P. and D'Amore,P.A.
  TITLE     Elements of the Endomucin Extracellular Domain Essential for
            VEGF-Induced VEGFR2 Activity
  JOURNAL   Cells 9 (6), 1413 (2020)
   PUBMED   32517158
  REMARK    GeneRIF: Elements of the Endomucin Extracellular Domain Essential
            for VEGF-Induced VEGFR2 Activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Kanda,H., Tanaka,T., Matsumoto,M., Umemoto,E., Ebisuno,Y.,
            Kinoshita,M., Noda,M., Kannagi,R., Hirata,T., Murai,T., Fukuda,M.
            and Miyasaka,M.
  TITLE     Endomucin, a sialomucin expressed in high endothelial venules,
            supports L-selectin-mediated rolling
  JOURNAL   Int Immunol 16 (9), 1265-1274 (2004)
   PUBMED   15249540
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Kuhn,A., Brachtendorf,G., Kurth,F., Sonntag,M., Samulowitz,U.,
            Metze,D. and Vestweber,D.
  TITLE     Expression of endomucin, a novel endothelial sialomucin, in normal
            and diseased human skin
  JOURNAL   J Invest Dermatol 119 (6), 1388-1393 (2002)
   PUBMED   12485444
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Samulowitz,U., Kuhn,A., Brachtendorf,G., Nawroth,R., Braun,A.,
            Bankfalvi,A., Bocker,W. and Vestweber,D.
  TITLE     Human endomucin: distribution pattern, expression on high
            endothelial venules, and decoration with the MECA-79 epitope
  JOURNAL   Am J Pathol 160 (5), 1669-1681 (2002)
   PUBMED   12000719
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Liu,C., Shao,Z.M., Zhang,L., Beatty,P., Sartippour,M., Lane,T.,
            Livingston,E. and Nguyen,M.
  TITLE     Human endomucin is an endothelial marker
  JOURNAL   Biochem Biophys Res Commun 288 (1), 129-136 (2001)
   PUBMED   11594763
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Kinoshita,M., Nakamura,T., Ihara,M., Haraguchi,T., Hiraoka,Y.,
            Tashiro,K. and Noda,M.
  TITLE     Identification of human endomucin-1 and -2 as membrane-bound
            O-sialoglycoproteins with anti-adhesive activity
  JOURNAL   FEBS Lett 499 (1-2), 121-126 (2001)
   PUBMED   11418125
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK313504.1, AK291831.1, AC097459.3 and AL133118.1.
            
            On Apr 8, 2002 this sequence version replaced NP_057326.1.
            
            Summary: EMCN is a mucin-like sialoglycoprotein that interferes
            with the assembly of focal adhesion complexes and inhibits
            interaction between cells and the extracellular matrix (Kinoshita
            et al., 2001 [PubMed 11418125]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF205940.1, SRR1803615.175378.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296420.9/ ENSP00000296420.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..261
                     /product="endomucin isoform 1 precursor"
                     /note="endomucin-2; MUC-14; mucin-14; gastric cancer
                     antigen Ga34"
                     /calculated_mol_wt=25463
     Region          1..261
                     /region_name="Endomucin"
                     /note="pfam07010"
                     /db_xref="CDD:429246"
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2007
     mat_peptide     19..261
                     /product="Endomucin. /id=PRO_0000019290"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULC0.2)"
                     /calculated_mol_wt=25463
     Site            19
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULC0.2)"
     Site            28
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULC0.2)"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULC0.2)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULC0.2)"
     Region          118..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULC0.2)"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULC0.2)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULC0.2)"
     Site            191..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULC0.2)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0H2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULC0.2)"
     CDS             1..261
                     /gene="EMCN"
                     /gene_synonym="EMCN2; MUC14"
                     /coded_by="NM_016242.4:109..894"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3655.1"
                     /db_xref="GeneID:51705"
                     /db_xref="HGNC:HGNC:16041"
                     /db_xref="MIM:608350"
ORIGIN      
        1 mellqvtilf llpsicssns tgvleaanns lvvtttkpsi ttpnteslqk nvvtpttgtt
       61 pkgtitnell kmslmstatf ltskdeglka tttdvrknds iisnvtvtsv tlpnavstlq
      121 sskpktetqs siktteipgs vlqpdaspsk tgtltsipvt ipentsqsqv igteggknas
      181 tsatsrsyss iilpvviali vitlsvfvlv glyrmcwkad pgtpengndq pqsdkesvkl
      241 ltvktishes gehsaqgktk n
//
LOCUS       NP_000963                266 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein eL8 [Homo sapiens].
ACCESSION   NP_000963
VERSION     NP_000963.1
DBSOURCE    REFSEQ: accession NM_000972.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Khatter,H., Myasnikov,A.G., Natchiar,S.K. and Klaholz,B.P.
  TITLE     Structure of the human 80S ribosome
  JOURNAL   Nature 520 (7549), 640-645 (2015)
   PUBMED   25901680
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Burris,T.P., Nawaz,Z., Tsai,M.J. and O'Malley,B.W.
  TITLE     A nuclear hormone receptor-associated protein that inhibits
            transactivation by the thyroid hormone and retinoic acid receptors
  JOURNAL   Proc Natl Acad Sci U S A 92 (21), 9525-9529 (1995)
   PUBMED   7568167
REFERENCE   7  (residues 1 to 266)
  AUTHORS   Colombo,P., Yon,J. and Fried,M.
  TITLE     The organization and expression of the human L7a ribosomal protein
            gene
  JOURNAL   Biochim Biophys Acta 1129 (1), 93-95 (1991)
   PUBMED   1756182
REFERENCE   8  (residues 1 to 266)
  AUTHORS   Ben-Ishai,R., Scharf,R., Sharon,R. and Kapten,I.
  TITLE     A human cellular sequence implicated in trk oncogene activation is
            DNA damage inducible
  JOURNAL   Proc Natl Acad Sci U S A 87 (16), 6039-6043 (1990)
   PUBMED   1696715
REFERENCE   9  (residues 1 to 266)
  AUTHORS   Ziemiecki,A., Muller,R.G., Fu,X.C., Hynes,N.E. and Kozma,S.
  TITLE     Oncogenic activation of the human trk proto-oncogene by
            recombination with the ribosomal large subunit protein L7a
  JOURNAL   EMBO J 9 (1), 191-196 (1990)
   PUBMED   2403926
REFERENCE   10 (residues 1 to 266)
  AUTHORS   Kozma,S.C., Redmond,S.M., Fu,X.C., Saurer,S.M., Groner,B. and
            Hynes,N.E.
  TITLE     Activation of the receptor kinase domain of the trk oncogene by
            recombination with two different cellular sequences
  JOURNAL   EMBO J 7 (1), 147-154 (1988)
   PUBMED   2966065
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AL772161.10 and AL593848.15.
            
            Summary: Cytoplasmic ribosomes, organelles that catalyze protein
            synthesis, consist of a small 40S subunit and a large 60S subunit.
            Together these subunits are composed of 4 RNA species and
            approximately 80 structurally distinct proteins. This gene encodes
            a ribosomal protein that is a component of the 60S subunit. The
            protein belongs to the L7AE family of ribosomal proteins. It can
            interact with a subclass of nuclear hormone receptors, including
            thyroid hormone receptor, and inhibit their ability to
            transactivate by preventing their binding to their DNA response
            elements. This gene is included in the surfeit gene cluster, a
            group of very tightly linked genes that do not share sequence
            similarity. It is co-transcribed with the U24, U36a, U36b, and U36c
            small nucleolar RNA genes, which are located in its second, fifth,
            fourth, and sixth introns, respectively. This gene rearranges with
            the trk proto-oncogene to form the chimeric oncogene trk-2h, which
            encodes an oncoprotein consisting of the N terminus of ribosomal
            protein L7a fused to the receptor tyrosine kinase domain of trk. As
            is typical for genes encoding ribosomal proteins, there are
            multiple processed pseudogenes of this gene dispersed through the
            genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.152640.1,
                                           SRR5189655.22992.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323345.11/ ENSP00000361076.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2"
     Protein         1..266
                     /product="large ribosomal subunit protein eL8"
                     /note="surfeit 3; surfeit locus protein 3; PLA-X
                     polypeptide; 60S ribosomal protein L7a; thyroid hormone
                     receptor uncoupling protein"
                     /calculated_mol_wt=29865
     Region          16..266
                     /region_name="SNU13"
                     /note="U4/U6.U5 small nuclear ribonucleoprotein SNU13;
                     cl42391"
                     /db_xref="CDD:455736"
     Site            34
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62424.2)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62424.2)"
     Site            order(141,144..145,148,163,165..166,168..169,172)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:411046"
     Site            217
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62424.2)"
     CDS             1..266
                     /gene="RPL7A"
                     /gene_synonym="eL8; L7A; SURF3; TRUP"
                     /coded_by="NM_000972.3:27..827"
                     /db_xref="CCDS:CCDS6965.1"
                     /db_xref="GeneID:6130"
                     /db_xref="HGNC:HGNC:10364"
                     /db_xref="MIM:185640"
ORIGIN      
        1 mpkgkkakgk kvapapavvk kqeakkvvnp lfekrpknfg igqdiqpkrd ltrfvkwpry
       61 irlqrqrail ykrlkvppai nqftqaldrq tatqllklah kyrpetkqek kqrllaraek
      121 kaagkgdvpt krppvlragv ntvttlvenk kaqlvviahd vdpielvvfl palcrkmgvp
      181 yciikgkarl grlvhrktct tvaftqvnse dkgalaklve airtnyndry deirrhwggn
      241 vlgpksvari aklekakake latklg
//
LOCUS       NP_055263                709 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 16 [Homo sapiens].
ACCESSION   NP_055263
VERSION     NP_055263.2
DBSOURCE    REFSEQ: accession NM_014448.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Yu,B., Xu,L., Chen,L., Wang,Y., Jiang,H., Wang,Y., Yan,Y., Luo,S.
            and Zhai,Z.
  TITLE     FYN is required for ARHGEF16 to promote proliferation and migration
            in colon cancer cells
  JOURNAL   Cell Death Dis 11 (8), 652 (2020)
   PUBMED   32811808
  REMARK    GeneRIF: FYN is required for ARHGEF16 to promote proliferation and
            migration in colon cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Muller,P.M., Rademacher,J., Bagshaw,R.D., Wortmann,C., Barth,C.,
            van Unen,J., Alp,K.M., Giudice,G., Eccles,R.L., Heinrich,L.E.,
            Pascual-Vargas,P., Sanchez-Castro,M., Brandenburg,L., Mbamalu,G.,
            Tucholska,M., Spatt,L., Czajkowski,M.T., Welke,R.W., Zhang,S.,
            Nguyen,V., Rrustemi,T., Trnka,P., Freitag,K., Larsen,B., Popp,O.,
            Mertins,P., Gingras,A.C., Roth,F.P., Colwill,K., Bakal,C.,
            Pertz,O., Pawson,T., Petsalaki,E. and Rocks,O.
  TITLE     Systems analysis of RhoGEF and RhoGAP regulatory proteins reveals
            spatially organized RAC1 signalling from integrin adhesions
  JOURNAL   Nat Cell Biol 22 (4), 498-511 (2020)
   PUBMED   32203420
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Benzinger,A., Muster,N., Koch,H.B., Yates,J.R. 3rd and Hermeking,H.
  TITLE     Targeted proteomic analysis of 14-3-3 sigma, a p53 effector
            commonly silenced in cancer
  JOURNAL   Mol Cell Proteomics 4 (6), 785-795 (2005)
   PUBMED   15778465
REFERENCE   7  (residues 1 to 709)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   8  (residues 1 to 709)
  AUTHORS   Rabizadeh,S. and Bredesen,D.E.
  TITLE     Ten years on: mediation of cell death by the common neurotrophin
            receptor p75(NTR)
  JOURNAL   Cytokine Growth Factor Rev 14 (3-4), 225-239 (2003)
   PUBMED   12787561
  REMARK    Review article
REFERENCE   9  (residues 1 to 709)
  AUTHORS   Salehi,A.H., Xanthoudakis,S. and Barker,P.A.
  TITLE     NRAGE, a p75 neurotrophin receptor-interacting protein, induces
            caspase activation and cell death through a JNK-dependent
            mitochondrial pathway
  JOURNAL   J Biol Chem 277 (50), 48043-48050 (2002)
   PUBMED   12376548
REFERENCE   10 (residues 1 to 709)
  AUTHORS   Harrington,A.W., Kim,J.Y. and Yoon,S.O.
  TITLE     Activation of Rac GTPase by p75 is necessary for c-jun N-terminal
            kinase-mediated apoptosis
  JOURNAL   J Neurosci 22 (1), 156-166 (2002)
   PUBMED   11756498
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL512413.23.
            
            On Dec 20, 2007 this sequence version replaced NP_055263.1.
            
            Summary: Although the specific function of this protein is not
            known yet, it is thought to be involved in protein-protein and
            protein-lipid interactions. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK095984.1, SRR9304717.512506.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378378.9/ ENSP00000367629.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.32"
     Protein         1..709
                     /product="rho guanine nucleotide exchange factor 16"
                     /note="Rho guanine exchange factor (GEF) 16; ephexin-4;
                     Rho guanine nucleotide exchange factor (GEF) 16; ephexin4"
                     /calculated_mol_wt=79974
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5VV41.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5VV41.1)"
     Region          22..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV41.1)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5VV41.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5VV41.1)"
     Region          114..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV41.1)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VV41.1)"
     Region          180..246
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV41.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VV41.1)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5VV41.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3U5C8; propagated from
                     UniProtKB/Swiss-Prot (Q5VV41.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5VV41.1)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5VV41.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5VV41.1)"
     Region          275..481
                     /region_name="Required for RHOG activation and mediates
                     interaction with EPHA2.
                     /evidence=ECO:0000269|PubMed:20679435"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV41.1)"
     Region          288..466
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          489..622
                     /region_name="PH_ephexin"
                     /note="Ephexin Pleckstrin homology (PH) domain; cd01221"
                     /db_xref="CDD:269929"
     Region          633..686
                     /region_name="SH3_ARHGEF16_26"
                     /note="Src homology 3 domain of the Rho guanine nucleotide
                     exchange factors ARHGEF16 and ARHGEF26; cd11938"
                     /db_xref="CDD:212871"
     Site            order(638,640,643,647,664..665,680,682..683)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212871"
     Region          707..709
                     /region_name="PDZ-binding motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV41.1)"
     CDS             1..709
                     /gene="ARHGEF16"
                     /gene_synonym="GEF16; NBR"
                     /coded_by="NM_014448.4:167..2296"
                     /db_xref="CCDS:CCDS46.2"
                     /db_xref="GeneID:27237"
                     /db_xref="HGNC:HGNC:15515"
                     /db_xref="MIM:618871"
ORIGIN      
        1 maqrhsdssl eekllghrfh selrldaggn pasglpmvrg sprvrddaaf qpqvpappqp
       61 rppgheepwp ivlstespaa lklgtqqlip kslavaskak tparhqsfga avlsreaarr
      121 dpkllpapsf slddmdvdkd pggmlrrnlr nqsyraamkg lgkpggqgda iqlspklqal
      181 aeepsqphtr spaknkktlg rkrghkgsfk ddpqlyqeiq erglntsqes dddildesss
      241 pegtqkvdat ivvksyrpaq vtwsqlpevv elgildqlst eerkrqeamf eiltsefsyq
      301 hslsilveef lqskelratv tqmehhhlfs nildvlgasq rffedleqrh kaqvlvedis
      361 dileehaekh fhpyiaycsn evyqqrtlqk lissnaafre alreierrpa cgglpmlsfl
      421 ilpmqrvtrl pllmdtlclk tqghseryka asralkaisk lvrqcnegah rmermeqmyt
      481 lhtqldfskv kslplisasr wllkrgelfl veetglfrki asrptcylfl fndvlvvtkk
      541 kseesymvqd yaqmnhiqve kiepselplp gggnrsssvp hpfqvtllrn segrqeqlll
      601 ssdsasdrar wivalthser qwqglsskgd lpqveitkaf fakqadevtl qqadvvlvlq
      661 qedgwlyger lrdgetgwfp edfarfitsr vavegnvrrm erlrvetdv
//
LOCUS       NP_003793               1938 aa            linear   PRI 27-APR-2025
DEFINITION  myosin-13 [Homo sapiens].
ACCESSION   NP_003793
VERSION     NP_003793.2
DBSOURCE    REFSEQ: accession NM_003802.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1938)
  AUTHORS   Schiaffino,S., Hughes,S.M., Murgia,M. and Reggiani,C.
  TITLE     MYH13, a superfast myosin expressed in extraocular, laryngeal and
            syringeal muscles
  JOURNAL   J Physiol 602 (3), 427-443 (2024)
   PUBMED   38160435
  REMARK    GeneRIF: MYH13, a superfast myosin expressed in extraocular,
            laryngeal and syringeal muscles.
REFERENCE   2  (residues 1 to 1938)
  AUTHORS   Chen,Z., Zhao,T.J., Li,J., Gao,Y.S., Meng,F.G., Yan,Y.B. and
            Zhou,H.M.
  TITLE     Slow skeletal muscle myosin-binding protein-C (MyBPC1) mediates
            recruitment of muscle-type creatine kinase (CK) to myosin
  JOURNAL   Biochem J 436 (2), 437-445 (2011)
   PUBMED   21426302
  REMARK    GeneRIF: Domain-mapping experiments indicated that muscle-type
            creatine kinase binds to the C-terminal domains of MyBPC1, which is
            also the binding site of myosin.
REFERENCE   3  (residues 1 to 1938)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 1938)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 1938)
  AUTHORS   Schjeide,B.M., McQueen,M.B., Mullin,K., DiVito,J., Hogan,M.F.,
            Parkinson,M., Hooli,B., Lange,C., Blacker,D., Tanzi,R.E. and
            Bertram,L.
  TITLE     Assessment of Alzheimer's disease case-control associations using
            family-based methods
  JOURNAL   Neurogenetics 10 (1), 19-25 (2009)
   PUBMED   18830724
  REMARK    GeneRIF: Meta-analysis of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 1938)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   7  (residues 1 to 1938)
  AUTHORS   Schachat,F. and Briggs,M.M.
  TITLE     Phylogenetic implications of the superfast myosin in extraocular
            muscles
  JOURNAL   J Exp Biol 205 (Pt 15), 2189-2201 (2002)
   PUBMED   12110653
  REMARK    GeneRIF: phylogenic imlications in extraocular muscles (REVIEW)
REFERENCE   8  (residues 1 to 1938)
  AUTHORS   Weiss,A., Schiaffino,S. and Leinwand,L.A.
  TITLE     Comparative sequence analysis of the complete human sarcomeric
            myosin heavy chain family: implications for functional diversity
  JOURNAL   J Mol Biol 290 (1), 61-75 (1999)
   PUBMED   10388558
REFERENCE   9  (residues 1 to 1938)
  AUTHORS   Weiss,A., McDonough,D., Wertman,B., Acakpo-Satchivi,L.,
            Montgomery,K., Kucherlapati,R., Leinwand,L. and Krauter,K.
  TITLE     Organization of human and mouse skeletal myosin heavy chain gene
            clusters is highly conserved
  JOURNAL   Proc Natl Acad Sci U S A 96 (6), 2958-2963 (1999)
   PUBMED   10077619
REFERENCE   10 (residues 1 to 1938)
  AUTHORS   Winters,L.M., Briggs,M.M. and Schachat,F.
  TITLE     The human extraocular muscle myosin heavy chain gene (MYH13) maps
            to the cluster of fast and developmental myosin genes on chromosome
            17
  JOURNAL   Genomics 54 (1), 188-189 (1998)
   PUBMED   9806854
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005291.1 and AF111782.2.
            
            On Jul 22, 2006 this sequence version replaced NP_003793.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF111782.2 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252172.9/ ENSP00000252172.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1938
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..1938
                     /product="myosin-13"
                     /note="myosin, heavy polypeptide 13, skeletal muscle;
                     extraocular muscle myosin heavy chain; extraocular myosin
                     heavy chain; myosin heavy chain, skeletal muscle,
                     extraocular; superfast myosin; myosin heavy chain,
                     skeletal muscle, laryngeal; myosin, heavy chain 13,
                     skeletal muscle"
                     /calculated_mol_wt=223475
     Region          33..77
                     /region_name="Myosin_N"
                     /note="Myosin N-terminal SH3-like domain; pfam02736"
                     /db_xref="CDD:460670"
     Region          100..770
                     /region_name="MYSc_Myh13"
                     /note="class II myosin heavy chain 13, motor domain;
                     cd14923"
                     /db_xref="CDD:276887"
     Site            order(127..135,179..186,235..245,463..468)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276887"
     Site            127..135
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276887"
     Site            130
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q9UKX3.2)"
     Site            179..186
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276887"
     Site            235..245
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276887"
     Site            463..468
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276887"
     Site            order(492..503,506..515)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276887"
     Region          659..681
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX3.2)"
     Site            701..710
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276887"
     Site            713..770
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276887"
     Region          761..775
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX3.2)"
     Region          850..1927
                     /region_name="Myosin_tail_1"
                     /note="Myosin tail; pfam01576"
                     /db_xref="CDD:460256"
     Region          1917..1938
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX3.2)"
     CDS             1..1938
                     /gene="MYH13"
                     /gene_synonym="MyHC-eo; MyHC-IIL"
                     /coded_by="NM_003802.3:92..5908"
                     /db_xref="CCDS:CCDS45613.1"
                     /db_xref="GeneID:8735"
                     /db_xref="HGNC:HGNC:7571"
                     /db_xref="MIM:603487"
ORIGIN      
        1 mssdaemaif geaapylrkp ekerieaqnr pfdskkacfv adnkemyvkg miqtrendkv
       61 ivktlddrml tlnndqvfpm nppkfdkied mammthlhep avlynlkery aawmiytysg
      121 lfcvtvnpyk wlpvykpevv aayrgkkrqe apphifsisd nayqfmltdr dnqsilitge
      181 sgagktvntk rviqyfatia vtgdkkketq pgkmqgtled qiiqanplle afgnaktvrn
      241 dnssrfgkfi rihfgatgkl asadietyll eksrvtfqls sersyhifyq imsnkkpeli
      301 dlllistnpf dfpfvsqgev tvasiddsee llatdnaidi lgfsseekvg iykltgavmh
      361 ygnmkfkqkq reeqaepdgt evadkagylm glnsaemlkg lccprvkvgn eyvtkgqnvq
      421 qvtnsvgala kavyekmflw mvtrinqqld tkqprqyfig vldiagfeif dfnsleqlci
      481 nftneklqqf fnhhmfvleq eeykkegiew efidfgmdla acieliekpm gifsileeec
      541 mfpkatdtsf knklydqhlg ksnnfqkpkp akgkaeahfs lvhyagtvdy niagwldknk
      601 dplnetvvgl yqksslklls flfsnyagae tgdsggskkg gkkkgssfqt vsavfrenln
      661 klmtnlrsth phfvrclipn etktpgvmdh ylvmhqlrcn gvlegiricr kgfpsrilya
      721 dfkqryriln asaipegqfi dsknasekll nsidvdreqf rfgntkvffk agllglleem
      781 rdeklvtlmt stqavcrgyl mrvefkkmme rrdsifciqy nirsfmnvkh wpwmnlffki
      841 kpllksaeae kematmkedf ertkeelars earrkeleek mvsllqeknd lqlqvqsete
      901 nlmdaeerce glikskille akvkelterl eeeeemnsel vakkrnledk csslkrdidd
      961 leltltkvek ekhatenkvk nlseemtale eniskltkek kslqeahqqt lddlqveedk
     1021 vnglikinak leqqtddleg sleqekklra dlerakrkle gdlkmsqesi mdlendkqqi
     1081 eeklkkkefe lsqlqakidd eqvhslqfqk kikelqarie eleeeieaeh tlrakiekqr
     1141 sdlareleei serleeasga tsaqiemnkk reaefqkmrr dleeatlqhe ataatlrkkq
     1201 adsvaelgeq idnlqrvkqk lekekselkm eiddmasnie alsksksnie rtcrtvedqf
     1261 seikakdeqq tqlihdlnmq karlqtqnge lshrveekes lisqltkskq altqqleelk
     1321 rqmeeetkak namahalqss rhdcdllreq yeeeqeakae lqralskans evaqwrtkye
     1381 tdaiqrteel eeakkklaqr lqeaeentet anskcaslek tkqrlqgeve dlmrdlersh
     1441 tacatldkkq rnfdkvlaew kqkldesqae leaaqkesrs lstelfkmrn ayeevvdqle
     1501 tlrrenknlq eeisdlteqi aetgknlqea ektkklveqe ksdlqvalee vegslehees
     1561 kilrvqlels qvkseldrkv iekdeeieql krnsqraaea lqsvldaeir srndalrlkk
     1621 kmegdlneme iqlghsnrqm aetqkhlrtv qgqlkdsqlh lddalrsned lkeqlaiver
     1681 rngllleele emkvaleqte rtrrlseqel ldasdrvqll hsqntslint kkkleadiaq
     1741 cqaevensiq esrnaeekak kaitdaamma eelkkeqdts ahlermkknl eqtvkdlqhr
     1801 ldeaeqlalk ggkkqiqkle nrvrelenel dveqkrgaea lkgahkyerk vkemtyqaee
     1861 dhknilrlqd lvdklqakvk sykrqaeeae eqantqlsrc rrvqheleea aeradiaesq
     1921 vnklraksrd vgsqkmee
//
LOCUS       NP_733466                388 aa            linear   PRI 27-APR-2025
DEFINITION  regulator of G-protein signaling 20 isoform a [Homo sapiens].
ACCESSION   NP_733466
VERSION     NP_733466.1
DBSOURCE    REFSEQ: accession NM_170587.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Li,G., Wang,M., Ren,L., Li,H., Liu,Q., Ouyang,Y., He,L. and Li,F.
  TITLE     Regulator of G protein signaling 20 promotes proliferation and
            migration in bladder cancer via NF-kappaB signaling
  JOURNAL   Biomed Pharmacother 117, 109112 (2019)
   PUBMED   31212130
  REMARK    GeneRIF: RGS20 acted as an oncogene in bladder cancer.
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Sierra,D.A., Gilbert,D.J., Householder,D., Grishin,N.V., Yu,K.,
            Ukidwe,P., Barker,S.A., He,W., Wensel,T.G., Otero,G., Brown,G.,
            Copeland,N.G., Jenkins,N.A. and Wilkie,T.M.
  TITLE     Evolution of the regulators of G-protein signaling multigene family
            in mouse and human
  JOURNAL   Genomics 79 (2), 177-185 (2002)
   PUBMED   11829488
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Barker,S.A., Wang,J., Sierra,D.A. and Ross,E.M.
  TITLE     RGSZ1 and Ret RGS: two of several splice variants from the gene
            RGS20
  JOURNAL   Genomics 78 (3), 223-229 (2001)
   PUBMED   11735229
REFERENCE   8  (residues 1 to 388)
  AUTHORS   Chatterjee,T.K. and Fisher,R.A.
  TITLE     Cytoplasmic, nuclear, and golgi localization of RGS proteins.
            Evidence for N-terminal and RGS domain sequences as intracellular
            targeting motifs
  JOURNAL   J Biol Chem 275 (31), 24013-24021 (2000)
   PUBMED   10791963
REFERENCE   9  (residues 1 to 388)
  AUTHORS   Wang,J., Ducret,A., Tu,Y., Kozasa,T., Aebersold,R. and Ross,E.M.
  TITLE     RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane
            association, regulation by Galphaz phosphorylation, and
            relationship to a Gz gtpase-activating protein subfamily
  JOURNAL   J Biol Chem 273 (40), 26014-26025 (1998)
   PUBMED   9748280
REFERENCE   10 (residues 1 to 388)
  AUTHORS   Glick,J.L., Meigs,T.E., Miron,A. and Casey,P.J.
  TITLE     RGSZ1, a Gz-selective regulator of G protein signaling whose action
            is sensitive to the phosphorylation state of Gzalpha
  JOURNAL   J Biol Chem 273 (40), 26008-26013 (1998)
   PUBMED   9748279
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113194.8, AY046538.1 and AC100821.2.
            
            Summary: The protein encoded by this gene belongs to the family of
            regulator of G protein signaling (RGS) proteins, which are
            regulatory and structural components of G protein-coupled receptor
            complexes. RGS proteins inhibit signal transduction by increasing
            the GTPase activity of G protein alpha subunits, thereby driving
            them into their inactive GDP-bound forms. This protein selectively
            binds to G(z)-alpha and G(alpha)-i2 subunits, and regulates their
            signaling activities. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY046538.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.23"
     Protein         1..388
                     /product="regulator of G-protein signaling 20 isoform a"
                     /note="regulator of G-protein signalling 20; regulator of
                     G-protein signaling Z1; gz-selective GTPase-activating
                     protein; regulator of Gz-selective protein signaling 1"
                     /calculated_mol_wt=43561
     Region          138..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O76081.4)"
     Region          221..376
                     /region_name="RGS_RGS20"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS20 protein; cd08746"
                     /db_xref="CDD:188700"
     Site            order(284,288,291,327..328,356,359)
                     /site_type="other"
                     /note="putative G-alpha interaction site"
                     /db_xref="CDD:188700"
     CDS             1..388
                     /gene="RGS20"
                     /gene_synonym="g(z)GAP; gz-GAP; RGSZ1; ZGAP1"
                     /coded_by="NM_170587.4:106..1272"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6155.1"
                     /db_xref="GeneID:8601"
                     /db_xref="HGNC:HGNC:14600"
                     /db_xref="MIM:607193"
ORIGIN      
        1 mpqlsqdnqe clqkhfsrps iwtqflplfr aqryntdihq itenegdlra vpdiksfppa
       61 qlpdspaapk lfgllsspls slarffshll rrpppeaprr rldfspllpa lpaarlsrgh
      121 eelpgrlsll lgaalalpgr psggrplrpp hpvakpreed atagqsspmp qmgsermemr
      181 krqmpaaqdt pgaapgqpga gsrgsnaccf cwccccscsc ltvrnqedqr ptiashelra
      241 dlptweespa ptleevnawa qsfdklmvtp agrnafrefl rtefseenml fwmaceelkk
      301 eankniieek ariiyedyis ilspkevsld srvrevinrn mvepsqhifd daqlqiytlm
      361 hrdsyprfmn savykdllqs lseksiea
//
LOCUS       NP_001014450              72 aa            linear   PRI 27-APR-2025
DEFINITION  small proline-rich protein 2F [Homo sapiens].
ACCESSION   NP_001014450
VERSION     NP_001014450.1
DBSOURCE    REFSEQ: accession NM_001014450.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Wang,Y., Anderson,E.P. and Tatakis,D.N.
  TITLE     Whole transcriptome analysis of smoker palatal mucosa identifies
            multiple downregulated innate immunity genes
  JOURNAL   J Periodontol 91 (6), 756-766 (2020)
   PUBMED   31682009
  REMARK    GeneRIF: SPRR2F expression is significantly downregulated in
            healthy palatal mucosa of smokers
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Kainu,K., Kivinen,K., Zucchelli,M., Suomela,S., Kere,J., Inerot,A.,
            Baker,B.S., Powles,A.V., Fry,L., Samuelsson,L. and
            Saarialho-Kere,U.
  TITLE     Association of psoriasis to PGLYRP and SPRR genes at PSORS4 locus
            on 1q shows heterogeneity between Finnish, Swedish and Irish
            families
  JOURNAL   Exp Dermatol 18 (2), 109-115 (2009)
   PUBMED   18643845
  REMARK    GeneRIF: Association of psoriasis to PGLYRP and SPRR genes at
            PSORS4 locus on 1q shows heterogeneity between Finnish, Swedish and
            Irish families.
REFERENCE   3  (residues 1 to 72)
  AUTHORS   Hong,S.H., Nah,H.Y., Lee,J.Y., Lee,Y.J., Lee,J.W., Gye,M.C.,
            Kim,C.H., Kang,B.M. and Kim,M.K.
  TITLE     Estrogen regulates the expression of the small proline-rich 2 gene
            family in the mouse uterus
  JOURNAL   Mol Cells 17 (3), 477-484 (2004)
   PUBMED   15232223
REFERENCE   4  (residues 1 to 72)
  AUTHORS   Cabral,A., Voskamp,P., Cleton-Jansen,A.M., South,A., Nizetic,D. and
            Backendorf,C.
  TITLE     Structural organization and regulation of the small proline-rich
            family of cornified envelope precursors suggest a role in adaptive
            barrier function
  JOURNAL   J Biol Chem 276 (22), 19231-19237 (2001)
   PUBMED   11279051
REFERENCE   5  (residues 1 to 72)
  AUTHORS   Song,H.J., Poy,G., Darwiche,N., Lichti,U., Kuroki,T., Steinert,P.M.
            and Kartasova,T.
  TITLE     Mouse Sprr2 genes: a clustered family of genes showing differential
            expression in epithelial tissues
  JOURNAL   Genomics 55 (1), 28-42 (1999)
   PUBMED   9888996
REFERENCE   6  (residues 1 to 72)
  AUTHORS   Davodeau,F., Houde,I., Boulot,G., Romagne,F., Necker,A., Canavo,N.,
            Peyrat,M.A., Hallet,M.M., Vie,H., Jacques,Y. et al.
  TITLE     Secretion of disulfide-linked human T-cell receptor gamma delta
            heterodimers
  JOURNAL   J Biol Chem 268 (21), 15455-15460 (1993)
   PUBMED   8340374
REFERENCE   7  (residues 1 to 72)
  AUTHORS   Gibbs,S., Fijneman,R., Wiegant,J., van Kessel,A.G., van De Putte,P.
            and Backendorf,C.
  TITLE     Molecular characterization and evolution of the SPRR family of
            keratinocyte differentiation markers encoding small proline-rich
            proteins
  JOURNAL   Genomics 16 (3), 630-637 (1993)
   PUBMED   8325635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139417.9, AF333956.1 and AI051688.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279873.4562.1, ERR279829.4815.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000468739.2/ ENSP00000418193.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..72
                     /product="small proline-rich protein 2F"
                     /note="SPR-2F"
                     /calculated_mol_wt=7674
     Region          21..47
                     /region_name="3 X 9 AA tandem repeats of
                     [PS]-K-C-P-[EQ]-[PS]-C-P-P"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RM1.1)"
     Region          53..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RM1.1)"
     CDS             1..72
                     /gene="SPRR2F"
                     /coded_by="NM_001014450.3:63..281"
                     /db_xref="CCDS:CCDS30867.1"
                     /db_xref="GeneID:6705"
                     /db_xref="HGNC:HGNC:11266"
                     /db_xref="MIM:617589"
ORIGIN      
        1 msyqqqqckq pcqpppvcpa pkcpepcppp kcpepcppsk cpqscppqqc qqkcppvtps
       61 ppcqpkcppk sk
//
LOCUS       NP_008882                800 aa            linear   PRI 27-APR-2025
DEFINITION  transcription initiation factor TFIID subunit 5 isoform 1 [Homo
            sapiens].
ACCESSION   NP_008882
VERSION     NP_008882.2
DBSOURCE    REFSEQ: accession NM_006951.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Gupta,K., Watson,A.A., Baptista,T., Scheer,E., Chambers,A.L.,
            Koehler,C., Zou,J., Obong-Ebong,I., Kandiah,E., Temblador,A.,
            Round,A., Forest,E., Man,P., Bieniossek,C., Laue,E.D., Lemke,E.A.,
            Rappsilber,J., Robinson,C.V., Devys,D., Tora,L. and Berger,I.
  TITLE     Architecture of TAF11/TAF13/TBP complex suggests novel regulation
            properties of general transcription factor TFIID
  JOURNAL   Elife 6, e30395 (2017)
   PUBMED   29111974
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Louder,R.K., He,Y., Lopez-Blanco,J.R., Fang,J., Chacon,P. and
            Nogales,E.
  TITLE     Structure of promoter-bound TFIID and model of human pre-initiation
            complex assembly
  JOURNAL   Nature 531 (7596), 604-609 (2016)
   PUBMED   27007846
  REMARK    Erratum:[Nature. 2016 Aug 4;536(7614):112. doi:
            10.1038/nature17984. PMID: 27096372]
REFERENCE   4  (residues 1 to 800)
  AUTHORS   Ba,X., Bacsi,A., Luo,J., Aguilera-Aguirre,L., Zeng,X., Radak,Z.,
            Brasier,A.R. and Boldogh,I.
  TITLE     8-oxoguanine DNA glycosylase-1 augments proinflammatory gene
            expression by facilitating the recruitment of site-specific
            transcription factors
  JOURNAL   J Immunol 192 (5), 2384-2394 (2014)
   PUBMED   24489103
  REMARK    GeneRIF: results show that nonproductive binding of OGG1 to 8-oxoG
            in promoter sequences could be an epigenetic mechanism to modulate
            gene expression for a prompt innate immune response.
REFERENCE   5  (residues 1 to 800)
  AUTHORS   Bieniossek,C., Papai,G., Schaffitzel,C., Garzoni,F., Chaillet,M.,
            Scheer,E., Papadopoulos,P., Tora,L., Schultz,P. and Berger,I.
  TITLE     The architecture of human general transcription factor TFIID core
            complex
  JOURNAL   Nature 493 (7434), 699-702 (2013)
   PUBMED   23292512
REFERENCE   6  (residues 1 to 800)
  AUTHORS   Bhattacharya,S., Takada,S. and Jacobson,R.H.
  TITLE     Structural analysis and dimerization potential of the human TAF5
            subunit of TFIID
  JOURNAL   Proc Natl Acad Sci U S A 104 (4), 1189-1194 (2007)
   PUBMED   17227857
  REMARK    GeneRIF: TAF5 protein demonstrates the ability of the N-terminal
            half of the TAF5 gene to form a flexible, extended dimer, a key
            property required for the assembly of the TFIID complex
REFERENCE   7  (residues 1 to 800)
  AUTHORS   Tanese,N., Saluja,D., Vassallo,M.F., Chen,J.L. and Admon,A.
  TITLE     Molecular cloning and analysis of two subunits of the human TFIID
            complex: hTAFII130 and hTAFII100
  JOURNAL   Proc Natl Acad Sci U S A 93 (24), 13611-13616 (1996)
   PUBMED   8942982
REFERENCE   8  (residues 1 to 800)
  AUTHORS   Zhou,Q. and Sharp,P.A.
  TITLE     Novel mechanism and factor for regulation by HIV-1 Tat
  JOURNAL   EMBO J 14 (2), 321-328 (1995)
   PUBMED   7835343
REFERENCE   9  (residues 1 to 800)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 800)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X95525.1, BC052268.1,
            BG290312.1 and AW136916.1.
            
            On May 22, 2002 this sequence version replaced NP_008882.1.
            
            Summary: Initiation of transcription by RNA polymerase II requires
            the activities of more than 70 polypeptides. The protein that
            coordinates these activities is transcription factor IID (TFIID),
            which binds to the core promoter to position the polymerase
            properly, serves as the scaffold for assembly of the remainder of
            the transcription complex, and acts as a channel for regulatory
            signals. TFIID is composed of the TATA-binding protein (TBP) and a
            group of evolutionarily conserved proteins known as TBP-associated
            factors or TAFs. TAFs may participate in basal transcription, serve
            as coactivators, function in promoter recognition or modify general
            transcription factors (GTFs) to facilitate complex assembly and
            transcription initiation. This gene encodes an integral subunit of
            TFIID associated with all transcriptionally competent forms of that
            complex. This subunit interacts strongly with two TFIID subunits
            that show similarity to histones H3 and H4, and it may participate
            in forming a nucleosome-like core in the TFIID complex. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.276184.1, BC052268.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369839.4/ ENSP00000358854.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.33"
     Protein         1..800
                     /product="transcription initiation factor TFIID subunit 5
                     isoform 1"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, D, 100kD; TATA box binding protein
                     (TBP)-associated factor 2D; transcription initiation
                     factor TFIID 100 kD subunit; transcription initiation
                     factor TFIID subunit 5; transcription initiation factor
                     TFIID 100 kDa subunit; TAF5 RNA polymerase II, TATA box
                     binding protein (TBP)-associated factor, 100kDa"
                     /calculated_mol_wt=86699
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15542.3)"
     Region          153..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15542.3)"
     Region          194..340
                     /region_name="NTD2, involved in homo-dimerization, also
                     involved in TFIID-TFIIF contacts in the RNA Pol II
                     pre-initiation complex (PIC).
                     /evidence=ECO:0000303|PubMed:33795473,
                     ECO:0007744|PDB:2NXP"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15542.3)"
     Region          208..337
                     /region_name="TFIID_NTD2"
                     /note="WD40 associated region in TFIID subunit, NTD2
                     domain; pfam04494"
                     /db_xref="CDD:461330"
     Site            order(234..235,275,304..308,340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:176269"
     Site            order(274,277..278)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:176269"
     Region          384..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15542.3)"
     Region          <456..740
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          468..507
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15542.3)"
     Region          473..541
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          541..580
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15542.3)"
     Region          547..583
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          583..624
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15542.3)"
     Region          588..624
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          625..666
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15542.3)"
     Region          631..666
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          667..706
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15542.3)"
     Region          672..708
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          709..748
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15542.3)"
     Region          714..756
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..800
                     /gene="TAF5"
                     /gene_synonym="TAF(II)100; TAF2D; TAFII-100; TAFII100"
                     /coded_by="NM_006951.5:15..2417"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7547.1"
                     /db_xref="GeneID:6877"
                     /db_xref="HGNC:HGNC:11539"
                     /db_xref="MIM:601787"
ORIGIN      
        1 maalaeeqte vavklepegp ptllppqagd gagegsggtt nngpnggggn vaassstggd
       61 ggtpkptvav saaapagaap vpaaapdaga phdrqtllav lqflrqsklr eaeealrrea
      121 glleeavags gapgevdsag aevtsallsr vtasapgpaa pdppgtgasg atvvsgsasg
      181 paapgkvgsv avedqpdvsa vlsaynqqgd ptmyeeyysg lkhfiecsld chraelsqlf
      241 yplfvhmyle lvynqhenea ksffekfhgd qecyyqddlr vlssltkkeh mkgnetmldf
      301 rtskfvlris rdsyqllkrh lqekqnnqiw nivqehlyid ifdgmprskq qidamvgsla
      361 geakreanks kvffgllkep eievpldded eegeneegkp kkkkpkkdsi gskskkqdpn
      421 appqnriplp elkdsdkldk imnmkettkr vrlgpdclps icfytflnay qgltavdvtd
      481 dssliaggfa dstvrvwsvt pkklrsvkqa sdlslidkes ddvlerimde ktaselkily
      541 ghsgpvygas fspdrnylls ssedgtvrlw slqtftclvg ykghnypvwd tqfspygyyf
      601 vsgghdrvar lwatdhyqpl rifaghladv nctrfhpnsn yvatgsadrt vrlwdvlngn
      661 cvriftghkg pihsltfspn grflatgatd grvllwdigh glmvgelkgh tdtvcslrfs
      721 rdgeilasgs mdntvrlwda ikafedletd dfttatghin lpensqelll gtymtkstpv
      781 vhlhftrrnl vlaagayspq
//
LOCUS       NP_001069080             256 aa            linear   MAM 27-APR-2025
DEFINITION  calsenilin [Bos taurus].
ACCESSION   NP_001069080 XP_590980
VERSION     NP_001069080.1
DBSOURCE    REFSEQ: accession NM_001075612.2
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC118417.1.
            
            On Oct 4, 2006 this sequence version replaced XP_590980.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC118417.1, SRR5571254.4452.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03145412, SAMN03145419
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="11"
                     /map="11"
                     /breed="Hereford"
     Protein         1..256
                     /product="calsenilin"
                     /note="kv channel-interacting protein 3; A-type potassium
                     channel modulatory protein 3; Kv channel interacting
                     protein 3, calsenilin"
                     /calculated_mol_wt=29315
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17QD9.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JM47; propagated from
                     UniProtKB/Swiss-Prot (Q17QD9.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXT8; propagated from
                     UniProtKB/Swiss-Prot (Q17QD9.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W7; propagated from
                     UniProtKB/Swiss-Prot (Q17QD9.1)"
     Region          107..241
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          243..256
                     /region_name="Interaction with KCND2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17QD9.1)"
     CDS             1..256
                     /gene="KCNIP3"
                     /gene_synonym="KChIP3"
                     /coded_by="NM_001075612.2:74..844"
                     /db_xref="BGD:BT28508"
                     /db_xref="GeneID:513316"
                     /db_xref="VGNC:VGNC:102823"
ORIGIN      
        1 mqrakevmkv sdgsllgepg rtplskkegv kwqrprltrq almrcclvkw ilssaapqgs
       61 yssdselels avrhqpegld qlqaqtkftk kelqslyrgf knecptglvd edtfkliysq
      121 ffpqgdatty ahflfnafda dgngairfed fvvglsillr gtvheklkwa fnlydinkdg
      181 yitkeemlai mksiydmmgr htypilreda plehverffq kmdrnqdgvv tidefletcq
      241 kdenimssmq lfenvi
//
LOCUS       NP_001010915             232 aa            linear   PRI 27-APR-2025
DEFINITION  very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 4 isoform 1
            [Homo sapiens].
ACCESSION   NP_001010915 XP_376819
VERSION     NP_001010915.2
DBSOURCE    REFSEQ: accession NM_001010915.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Jo,Y.S., Kim,M.S., Yoo,N.J. and Lee,S.H.
  TITLE     Inactivating Frameshift Mutations of HACD4 and TCP10L Tumor
            Suppressor Genes in Colorectal and Gastric Cancers
  JOURNAL   Pathol Oncol Res 26 (1), 583-584 (2020)
   PUBMED   29532408
  REMARK    GeneRIF: Inactivating Frameshift Mutations of HACD4 and TCP10L
            Tumor Suppressor Genes in Colorectal and Gastric Cancers.
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Zivotic,I., Djuric,T., Stankovic,A., Ivancevic,I., Koncar,I.,
            Milasinovic,D., Stankovic,G., Alavantic,D. and Zivkovic,M.
  TITLE     The HACD4 haplotype as a risk factor for atherosclerosis in males
  JOURNAL   Gene 641, 35-40 (2018)
   PUBMED   29031776
  REMARK    GeneRIF: association of HACD4 haplotypes with atherosclerotic
            phenotypes connotes a further validation and replication in larger
            cohorts as well as functional studies to enlighten the potential
            mechanism of its action in pathophysiology of atherosclerosis.
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Zhu,S., Wang,Z., Zhang,Z., Wang,J., Li,Y., Yao,L., Mei,Q. and
            Zhang,W.
  TITLE     PTPLAD2 is a tumor suppressor in esophageal squamous cell
            carcinogenesis
  JOURNAL   FEBS Lett 588 (6), 981-989 (2014)
   PUBMED   24530685
  REMARK    GeneRIF: PTPLAD2 is a potential tumor suppressor and prognostic
            indicator that reduces STAT3 phosphorylation.
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Cheng,C.Y., Schache,M., Ikram,M.K., Young,T.L., Guggenheim,J.A.,
            Vitart,V., MacGregor,S., Verhoeven,V.J., Barathi,V.A., Liao,J.,
            Hysi,P.G., Bailey-Wilson,J.E., St Pourcain,B., Kemp,J.P.,
            McMahon,G., Timpson,N.J., Evans,D.M., Montgomery,G.W., Mishra,A.,
            Wang,Y.X., Wang,J.J., Rochtchina,E., Polasek,O., Wright,A.F.,
            Amin,N., van Leeuwen,E.M., Wilson,J.F., Pennell,C.E., van
            Duijn,C.M., de Jong,P.T., Vingerling,J.R., Zhou,X., Chen,P., Li,R.,
            Tay,W.T., Zheng,Y., Chew,M., Burdon,K.P., Craig,J.E., Iyengar,S.K.,
            Igo,R.P. Jr., Lass,J.H. Jr., Chew,E.Y., Haller,T., Mihailov,E.,
            Metspalu,A., Wedenoja,J., Simpson,C.L., Wojciechowski,R., Hohn,R.,
            Mirshahi,A., Zeller,T., Pfeiffer,N., Lackner,K.J., Bettecken,T.,
            Meitinger,T., Oexle,K., Pirastu,M., Portas,L., Nag,A.,
            Williams,K.M., Yonova-Doing,E., Klein,R., Klein,B.E.,
            Hosseini,S.M., Paterson,A.D., Makela,K.M., Lehtimaki,T.,
            Kahonen,M., Raitakari,O., Yoshimura,N., Matsuda,F., Chen,L.J.,
            Pang,C.P., Yip,S.P., Yap,M.K., Meguro,A., Mizuki,N., Inoko,H.,
            Foster,P.J., Zhao,J.H., Vithana,E., Tai,E.S., Fan,Q., Xu,L.,
            Campbell,H., Fleck,B., Rudan,I., Aung,T., Hofman,A.,
            Uitterlinden,A.G., Bencic,G., Khor,C.C., Forward,H., Parssinen,O.,
            Mitchell,P., Rivadeneira,F., Hewitt,A.W., Williams,C., Oostra,B.A.,
            Teo,Y.Y., Hammond,C.J., Stambolian,D., Mackey,D.A., Klaver,C.C.,
            Wong,T.Y., Saw,S.M. and Baird,P.N.
  CONSRTM   Consortium for Refractive Error and Myopia; Fuchs' Genetics
            Multi-Center Study Group; Wellcome Trust Case Control Consortium 2;
            Diabetes Control and Complications Trial/Epidemiology of Diabetes
            Interventions, and Complications Research Group
  TITLE     Nine loci for ocular axial length identified through genome-wide
            association studies, including shared loci with refractive error
  JOURNAL   Am J Hum Genet 93 (2), 264-277 (2013)
   PUBMED   24144296
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Ikeda,M., Kanao,Y., Yamanaka,M., Sakuraba,H., Mizutani,Y.,
            Igarashi,Y. and Kihara,A.
  TITLE     Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases
            involved in very long-chain fatty acid synthesis
  JOURNAL   FEBS Lett 582 (16), 2435-2440 (2008)
   PUBMED   18554506
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY118500.1, BX648779.1, BC114215.1 and AL662879.5.
            
            On May 23, 2007 this sequence version replaced NP_001010915.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.149241.1,
                                           SRR1803617.120925.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000495827.3/ ENSP00000419503.1
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.3"
     Protein         1..232
                     /product="very-long-chain (3R)-3-hydroxyacyl-CoA
                     dehydratase 4 isoform 1"
                     /EC_number="4.2.1.134"
                     /note="protein tyrosine phosphatase-like protein PTPLAD2;
                     very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein]
                     dehydratase 4; very-long-chain (3R)-3-hydroxyacyl-CoA
                     dehydratase 4; protein tyrosine phosphatase-like A domain
                     containing 2; protein-tyrosine phosphatase-like A
                     domain-containing protein 2"
                     /calculated_mol_wt=27389
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWC8.1)"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWC8.1)"
     Region          65..223
                     /region_name="PTPLA"
                     /note="Protein tyrosine phosphatase-like protein, PTPLA;
                     pfam04387"
                     /db_xref="CDD:461286"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWC8.1)"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWC8.1)"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWC8.1)"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWC8.1)"
     CDS             1..232
                     /gene="HACD4"
                     /gene_synonym="PTPLAD2"
                     /coded_by="NM_001010915.5:51..749"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43791.1"
                     /db_xref="GeneID:401494"
                     /db_xref="HGNC:HGNC:20920"
                     /db_xref="MIM:615941"
ORIGIN      
        1 mgplalpawl qpryrknayl fiyyliqfcg hswiftnmtv rffsfgkdsm vdtfyaiglv
       61 mrlcqsvsll ellhiyvgie snhllprflq lteriiilfv vitsqeevqe kyvvcvlfvf
      121 wnlldmvryt ysmlsvigis yavltwlsqt lwmpiyplcv laeafaiyqs lpyfesfgty
      181 stklpfdlsi yfpyvlkiyl mmlfigmyft yshlyserrd ilgifpikkk km
//
LOCUS       NP_057556                139 aa            linear   PRI 27-APR-2025
DEFINITION  GSK3B-interacting protein [Homo sapiens].
ACCESSION   NP_057556
VERSION     NP_057556.2
DBSOURCE    REFSEQ: accession NM_016472.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Cheng,Y.W., Chen,Y.Y., Lin,C.J., Lieu,A.S., Tsai,H.P. and Kwan,A.L.
  TITLE     High expression of GSKIP is associated with poor prognosis in
            meningioma
  JOURNAL   Medicine (Baltimore) 101 (50), e32209 (2022)
   PUBMED   36550871
  REMARK    GeneRIF: High expression of GSKIP is associated with poor prognosis
            in meningioma.
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Sakai,S.S., Hasegawa,A., Ishimura,R., Tamura,N., Kageyama,S.,
            Komatsu-Hirota,S., Abe,M., Ling,Y., Okuda,S., Funayama,M.,
            Kikkawa,M., Miura,Y., Sakimura,K., Narita,I., Waguri,S., Shimizu,R.
            and Komatsu,M.
  TITLE     Loss of Atg2b and Gskip Impairs the Maintenance of the
            Hematopoietic Stem Cell Pool Size
  JOURNAL   Mol Cell Biol 42 (1), e0002421 (2022)
   PUBMED   34748402
  REMARK    GeneRIF: Loss of Atg2b and Gskip Impairs the Maintenance of the
            Hematopoietic Stem Cell Pool Size.
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Pegliasco,J., Hirsch,P., Marzac,C., Isnard,F., Meniane,J.C.,
            Deswarte,C., Pellet,P., Lemaitre,C., Leroy,G., Rabadan Moraes,G.,
            Guermouche,H., Schmaltz-Panneau,B., Pasquier,F., Colas,C.,
            Benusiglio,P.R., Bera,O., Bourhis,J.H., Brissot,E., Caron,O.,
            Chraibi,S., Cony-Makhoul,P., Delaunay-Darivon,C., Lapusan,S., de
            Fontbrune,F.S., Fuseau,P., Najman,A., Vainchenker,W.,
            Delhommeau,F., Micol,J.B., Plo,I. and Bellanne-Chantelot,C.
  TITLE     Germline ATG2B/GSKIP-containing 14q32 duplication predisposes to
            early clonal hematopoiesis leading to myeloid neoplasms
  JOURNAL   Leukemia 36 (1), 126-137 (2022)
   PUBMED   34172895
  REMARK    GeneRIF: Germline ATG2B/GSKIP-containing 14q32 duplication
            predisposes to early clonal hematopoiesis leading to myeloid
            neoplasms.
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Pilot-Storck,F., Chopin,E., Rual,J.F., Baudot,A., Dobrokhotov,P.,
            Robinson-Rechavi,M., Brun,C., Cusick,M.E., Hill,D.E., Schaeffer,L.,
            Vidal,M. and Goillot,E.
  TITLE     Interactome mapping of the phosphatidylinositol 3-kinase-mammalian
            target of rapamycin pathway identifies deformed epidermal
            autoregulatory factor-1 as a new glycogen synthase kinase-3
            interactor
  JOURNAL   Mol Cell Proteomics 9 (7), 1578-1593 (2010)
   PUBMED   20368287
REFERENCE   7  (residues 1 to 139)
  AUTHORS   Howng,S.L., Hwang,C.C., Hsu,C.Y., Hsu,M.Y., Teng,C.Y., Chou,C.H.,
            Lee,M.F., Wu,C.H., Chiou,S.J., Lieu,A.S., Loh,J.K., Yang,C.N.,
            Lin,C.S. and Hong,Y.R.
  TITLE     Involvement of the residues of GSKIP, AxinGID, and FRATtide in
            their binding with GSK3beta to unravel a novel C-terminal
            scaffold-binding region
  JOURNAL   Mol Cell Biochem 339 (1-2), 23-33 (2010)
   PUBMED   20043192
REFERENCE   8  (residues 1 to 139)
  AUTHORS   Hundsrucker,C., Skroblin,P., Christian,F., Zenn,H.M., Popara,V.,
            Joshi,M., Eichhorst,J., Wiesner,B., Herberg,F.W., Reif,B.,
            Rosenthal,W. and Klussmann,E.
  TITLE     Glycogen synthase kinase 3beta interaction protein functions as an
            A-kinase anchoring protein
  JOURNAL   J Biol Chem 285 (8), 5507-5521 (2010)
   PUBMED   20007971
REFERENCE   9  (residues 1 to 139)
  AUTHORS   Lin,C.C., Chou,C.H., Howng,S.L., Hsu,C.Y., Hwang,C.C., Wang,C.,
            Hsu,C.M. and Hong,Y.R.
  TITLE     GSKIP, an inhibitor of GSK3beta, mediates the
            N-cadherin/beta-catenin pool in the differentiation of SH-SY5Y
            cells
  JOURNAL   J Cell Biochem 108 (6), 1325-1336 (2009)
   PUBMED   19830702
REFERENCE   10 (residues 1 to 139)
  AUTHORS   Chou,H.Y., Howng,S.L., Cheng,T.S., Hsiao,Y.L., Lieu,A.S., Loh,J.K.,
            Hwang,S.L., Lin,C.C., Hsu,C.M., Wang,C., Lee,C.I., Lu,P.J.,
            Chou,C.K., Huang,C.Y. and Hong,Y.R.
  TITLE     GSKIP is homologous to the Axin GSK3beta interaction domain and
            functions as a negative regulator of GSK3beta
  JOURNAL   Biochemistry 45 (38), 11379-11389 (2006)
   PUBMED   16981698
  REMARK    GeneRIF: GSKIP is a naturally occurring protein that is homologous
            with the GSK3beta interaction domain of Axin and is able to
            negatively regulate GSK3beta of the Wnt signaling pathway.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359240.4.
            
            On Mar 30, 2005 this sequence version replaced NP_057556.1.
            
            Summary: This gene encodes a protein that is involved as a negative
            regulator of GSK3-beta in the Wnt signaling pathway. The encoded
            protein may play a role in the retinoic acid signaling pathway by
            regulating the functional interactions between GSK3-beta,
            beta-catenin and cyclin D1, and it regulates the
            beta-catenin/N-cadherin pool. The encoded protein contains a
            GSK3-beta interacting domain (GID) in its C-terminus, which is
            similar to the GID of Axin. The protein also contains an
            evolutionarily conserved RII-binding domain, which facilitates
            binding with protein kinase-A and GSK3-beta, enabling its role as
            an A-kinase anchoring protein. Alternatively spliced transcript
            variants have been observed for this gene. [provided by RefSeq, Dec
            2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3 and 4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000796.1, SRR1660805.148365.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000555181.6/ ENSP00000450420.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.2"
     Protein         1..139
                     /product="GSK3B-interacting protein"
                     /note="GSK3-beta interaction protein"
                     /calculated_mol_wt=15517
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0R6.2)"
     Region          33..133
                     /region_name="GSKIP_dom"
                     /note="GSKIP domain; pfam05303"
                     /db_xref="CDD:398795"
     Region          41..45
                     /region_name="Required for PRKAR2A interaction,
                     contributes to a protective effect against
                     H(2)O(2)-induced apoptosis.
                     /evidence=ECO:0000269|PubMed:25920809"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0R6.2)"
     Region          115..139
                     /region_name="Interaction with GSK3B and acts as a GSK3B
                     inhibitor. /evidence=ECO:0000269|PubMed:16981698"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0R6.2)"
     Site            130
                     /site_type="other"
                     /note="Required for GSK3B interaction, contributes to a
                     protective effect against H(2)O(2)-induced apoptosis.
                     /evidence=ECO:0000269|PubMed:16981698,
                     ECO:0000269|PubMed:25920809, ECO:0000269|PubMed:27484798;
                     propagated from UniProtKB/Swiss-Prot (Q9P0R6.2)"
     CDS             1..139
                     /gene="GSKIP"
                     /gene_synonym="C14orf129; HSPC210"
                     /coded_by="NM_016472.5:146..565"
                     /db_xref="CCDS:CCDS32153.1"
                     /db_xref="GeneID:51527"
                     /db_xref="HGNC:HGNC:20343"
                     /db_xref="MIM:616605"
ORIGIN      
        1 metdcnpmel ssmsgfeegs elngfegtdm kdmrleaeav vndvlfavnn mfvskslrca
       61 ddvayinvet kernryclel teaglkvvgy afdqvddhlq tpyhetvysl ldtlspayre
      121 afgnallqrl ealkrdgqs
//
LOCUS       NP_990644                408 aa            linear   VRT 27-APR-2025
DEFINITION  thyroid hormone receptor alpha [Gallus gallus].
ACCESSION   NP_990644 XP_015155046 XP_429297
VERSION     NP_990644.1
DBSOURCE    REFSEQ: accession NM_205313.2
KEYWORDS    RefSeq.
SOURCE      Gallus gallus (chicken)
  ORGANISM  Gallus gallus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
            Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
            Phasianidae; Phasianinae; Gallus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Tang,H., Finn,R.D. and Thomas,P.D.
  TITLE     TreeGrafter: phylogenetic tree-based annotation of proteins with
            Gene Ontology terms and other annotations
  JOURNAL   Bioinformatics 35 (3), 518-520 (2019)
   PUBMED   30032202
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Putcha,B.D., Wright,E., Brunzelle,J.S. and Fernandez,E.J.
  TITLE     Structural basis for negative cooperativity within agonist-bound
            TR:RXR heterodimers
  JOURNAL   Proc Natl Acad Sci U S A 109 (16), 6084-6087 (2012)
   PUBMED   22474364
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Burge,S., Kelly,E., Lonsdale,D., Mutowo-Muellenet,P., McAnulla,C.,
            Mitchell,A., Sangrador-Vegas,A., Yong,S.Y., Mulder,N. and Hunter,S.
  TITLE     Manual GO annotation of predictive protein signatures: the InterPro
            approach to GO curation
  JOURNAL   Database (Oxford) 2012, bar068 (2012)
   PUBMED   22301074
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Lassova,L., Niu,Z., Golden,E.B., Cohen,A.J. and Adams,S.L.
  TITLE     Thyroid hormone treatment of cultured chondrocytes mimics in vivo
            stimulation of collagen X mRNA by increasing BMP 4 expression
  JOURNAL   J Cell Physiol 219 (3), 595-605 (2009)
   PUBMED   19170125
REFERENCE   5  (residues 1 to 408)
  CONSRTM   International Chicken Genome Sequencing Consortium
  TITLE     Sequence and comparative analysis of the chicken genome provide
            unique perspectives on vertebrate evolution
  JOURNAL   Nature 432 (7018), 695-716 (2004)
   PUBMED   15592404
  REMARK    Erratum:[Nature. 2005 Feb 17;433(7027):777]
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Zhang,X.K., Hoffmann,B., Tran,P.B., Graupner,G. and Pfahl,M.
  TITLE     Retinoid X receptor is an auxiliary protein for thyroid hormone and
            retinoic acid receptors
  JOURNAL   Nature 355 (6359), 441-446 (1992)
   PUBMED   1310350
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Glineur,C., Bailly,M. and Ghysdael,J.
  TITLE     The c-erbA alpha-encoded thyroid hormone receptor is phosphorylated
            in its amino terminal domain by casein kinase II
  JOURNAL   Oncogene 4 (10), 1247-1254 (1989)
   PUBMED   2552374
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Zahraoui,A. and Cuny,G.
  TITLE     Nucleotide sequence of the chicken proto-oncogene c-erbA
            corresponding to domain 1 of v-erbA
  JOURNAL   Eur J Biochem 166 (1), 63-69 (1987)
   PUBMED   3036525
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Sap,J., Munoz,A., Damm,K., Goldberg,Y., Ghysdael,J., Leutz,A.,
            Beug,H. and Vennstrom,B.
  TITLE     The c-erb-A protein is a high-affinity receptor for thyroid hormone
  JOURNAL   Nature 324 (6098), 635-640 (1986)
   PUBMED   2879242
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AADN05000735.1.
            
            On or before Jan 17, 2016 this sequence version replaced
            XP_015155046.1, XP_429297.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns
                              SAMEA103992432, SAMEA103992453 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Gallus gallus"
                     /db_xref="taxon:9031"
                     /chromosome="27"
                     /map="27"
                     /breed="Red Jungle Fowl"
     Protein         1..408
                     /product="thyroid hormone receptor alpha"
                     /note="c-erb-A protein; thyroid hormone receptor beta;
                     nuclear receptor subfamily 1 group A member 1; thyroid
                     hormone receptor, alpha (erythroblastic leukemia viral
                     (v-erb-a) oncogene homolog, avian)"
                     /calculated_mol_wt=46626
     Region          1..50
                     /region_name="Modulating"
                     /note="propagated from UniProtKB/Swiss-Prot (P04625.1)"
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04625.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:2552374; propagated from
                     UniProtKB/Swiss-Prot (P04625.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2903825; propagated from
                     UniProtKB/Swiss-Prot (P04625.1)"
     Region          50..136
                     /region_name="NR_DBD_TR"
                     /note="DNA-binding domain of thyroid hormone receptors
                     (TRs) is composed of two C4-type zinc fingers; cd06961"
                     /db_xref="CDD:143519"
     Site            order(51,54,68,71,89,95,105,108)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143519"
     Site            order(61..63,69..70,72,74,76..77,80,102..103,106,109,
                     122..124,129,132..133,135..136)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143519"
     Site            order(61,64,119,121..122)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:143519"
     Region          160..402
                     /region_name="NR_LBD_TR"
                     /note="The ligand binding domain of thyroid hormone
                     receptor, a members of a superfamily of nuclear receptors;
                     cd06935"
                     /db_xref="CDD:132733"
     Site            order(213,216..217,219..220,223,226,254,257,261,273..275,
                     285,288,290,297,379,386,399)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132733"
     Site            order(225,228,232,242,246,249,397..398,401)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132733"
     Site            order(292,337,367,370..371,374,377..378,380..381)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132733"
     CDS             1..408
                     /gene="THRA"
                     /gene_synonym="NR1A1"
                     /coded_by="NM_205313.2:288..1514"
                     /db_xref="CGNC:155"
                     /db_xref="GeneID:396251"
ORIGIN      
        1 meqkpstldp lsepedtrwl dgkrkrkssq clvkssmsgy ipsyldkdeq cvvcgdkatg
       61 yhyrcitceg ckgffrrtiq knlhptysck ydgccvidki trnqcqlcrf kkcisvgmam
      121 dlvlddskrv akrklieenr errrkeemik slqhrpspsa eewelihvvt eahrstnaqg
      181 shwkqkrkfl pedigqspma smpdgdkvdl eafseftkii tpaitrvvdf akklpmfsel
      241 pcedqiillk gccmeimslr aavrydpese tltlsgemav kreqlknggl gvvsdaifdl
      301 gkslsafnld dtevallqav llmssdrtgl icvdkiekcq etyllafehy inyrkhniph
      361 fwpkllmkvt dlrmigacha srflhmkvec ptelfpplfl evfedqev
//
LOCUS       NP_001135783             297 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 169 [Homo sapiens].
ACCESSION   NP_001135783
VERSION     NP_001135783.1
DBSOURCE    REFSEQ: accession NM_001142311.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Hersh,C.P., Pillai,S.G., Zhu,G., Lomas,D.A., Bakke,P., Gulsvik,A.,
            DeMeo,D.L., Klanderman,B.J., Lazarus,R., Litonjua,A.A., Sparrow,D.,
            Reilly,J.J., Agusti,A., Calverley,P.M., Donner,C.F., Levy,R.D.,
            Make,B.J., Pare,P.D., Rennard,S.I., Vestbo,J., Wouters,E.F.,
            Scholand,M.B., Coon,H., Hoidal,J. and Silverman,E.K.
  TITLE     Multistudy fine mapping of chromosome 2q identifies XRCC5 as a
            chronic obstructive pulmonary disease susceptibility gene
  JOURNAL   Am J Respir Crit Care Med 182 (5), 605-613 (2010)
   PUBMED   20463177
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC008604.1, AK091582.1 and AW291087.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All variants (1-4) encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB146976.1, SRR3476690.430119.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000437356.7/ ENSP00000401305.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..297
                     /product="transmembrane protein 169"
                     /calculated_mol_wt=33480
     Region          1..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HH4.1)"
     Region          147..277
                     /region_name="TMEM169"
                     /note="TMEM169 protein family; pfam15052"
                     /db_xref="CDD:464471"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HH4.1)"
     Site            211..231
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HH4.1)"
     CDS             1..297
                     /gene="TMEM169"
                     /coded_by="NM_001142311.2:188..1081"
                     /db_xref="CCDS:CCDS2401.1"
                     /db_xref="GeneID:92691"
                     /db_xref="HGNC:HGNC:25130"
ORIGIN      
        1 meeptavegq vqlpsphqgs lrkavaaala ldgestmghr kkkrkesrpe siiiyrsdne
       61 ktdeepgese ggdqpkeeeg ddfldypvdd dmwnlpldsr yvtltgtitr gkkkgqmvdi
      121 hvtltekelq eltkpkessr ettpegrmac qmgadrgphv vlwtliclpv vfilsfvvsf
      181 yygtitwyni flvyneertf whkisycpcl vlfypvlima masslglyaa vvqlswswea
      241 wwqaardmek gfcgwlcskl gledcspysi vellesdnis stlsnkdpiq evetstv
//
LOCUS       NP_085133                788 aa            linear   PRI 27-APR-2025
DEFINITION  protein HID1 [Homo sapiens].
ACCESSION   NP_085133
VERSION     NP_085133.1
DBSOURCE    REFSEQ: accession NM_030630.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   Schanzer,A., Achleitner,M.T., Trumbach,D., Hubert,L., Munnich,A.,
            Ahlemeyer,B., AlAbdulrahim,M.M., Greif,P.A., Vosberg,S., Hummer,B.,
            Feichtinger,R.G., Mayr,J.A., Wortmann,S.B., Aichner,H.,
            Rudnik-Schoneborn,S., Ruiz,A., Gabau,E., Sanchez,J.P., Ellard,S.,
            Homfray,T., Stals,K.L., Wurst,W., Neubauer,B.A., Acker,T.,
            Bohlander,S.K., Asensio,C., Besmond,C., Alkuraya,F.S.,
            AlSayed,M.D., Hahn,A. and Weber,A.
  TITLE     Mutations in HID1 Cause Syndromic Infantile Encephalopathy and
            Hypopituitarism
  JOURNAL   Ann Neurol 90 (1), 143-158 (2021)
   PUBMED   33999436
  REMARK    GeneRIF: Mutations in HID1 Cause Syndromic Infantile Encephalopathy
            and Hypopituitarism.
REFERENCE   2  (residues 1 to 788)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 788)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 788)
  AUTHORS   Hummer,B.H., de Leeuw,N.F., Burns,C., Chen,L., Joens,M.S.,
            Hosford,B., Fitzpatrick,J.A.J. and Asensio,C.S.
  TITLE     HID-1 controls formation of large dense core vesicles by
            influencing cargo sorting and trans-Golgi network acidification
  JOURNAL   Mol Biol Cell 28 (26), 3870-3880 (2017)
   PUBMED   29074564
  REMARK    GeneRIF: Authors propose that HID-1 influences early steps in LDCV
            formation by controlling dense core formation at the TGN.
REFERENCE   5  (residues 1 to 788)
  AUTHORS   Fong,K.W., Leung,J.W., Li,Y., Wang,W., Feng,L., Ma,W., Liu,D.,
            Songyang,Z. and Chen,J.
  TITLE     MTR120/KIAA1383, a novel microtubule-associated protein, promotes
            microtubule stability and ensures cytokinesis
  JOURNAL   J Cell Sci 126 (Pt 3), 825-837 (2013)
   PUBMED   23264731
REFERENCE   6  (residues 1 to 788)
  AUTHORS   Wang,L., Zhan,Y., Song,E., Yu,Y., Jiu,Y., Du,W., Lu,J., Liu,P.,
            Xu,P. and Xu,T.
  TITLE     HID-1 is a peripheral membrane protein primarily associated with
            the medial- and trans- Golgi apparatus
  JOURNAL   Protein Cell 2 (1), 74-85 (2011)
   PUBMED   21337012
  REMARK    GeneRIF: mammalian HID-1 localized to the medial- and trans- Golgi
            apparatus as well as the cytosol.
REFERENCE   7  (residues 1 to 788)
  AUTHORS   Pilot-Storck,F., Chopin,E., Rual,J.F., Baudot,A., Dobrokhotov,P.,
            Robinson-Rechavi,M., Brun,C., Cusick,M.E., Hill,D.E., Schaeffer,L.,
            Vidal,M. and Goillot,E.
  TITLE     Interactome mapping of the phosphatidylinositol 3-kinase-mammalian
            target of rapamycin pathway identifies deformed epidermal
            autoregulatory factor-1 as a new glycogen synthase kinase-3
            interactor
  JOURNAL   Mol Cell Proteomics 9 (7), 1578-1593 (2010)
   PUBMED   20368287
REFERENCE   8  (residues 1 to 788)
  AUTHORS   Harada,H., Nagai,H., Tsuneizumi,M., Mikami,I., Sugano,S. and Emi,M.
  TITLE     Identification of DMC1, a novel gene in the TOC region on 17q25.1
            that shows loss of expression in multiple human cancers
  JOURNAL   J Hum Genet 46 (2), 90-95 (2001)
   PUBMED   11281419
REFERENCE   9  (residues 1 to 788)
  AUTHORS   Masson,J.Y., Davies,A.A., Hajibagheri,N., Van Dyck,E., Benson,F.E.,
            Stasiak,A.Z., Stasiak,A. and West,S.C.
  TITLE     The meiosis-specific recombinase hDmc1 forms ring structures and
            interacts with hRad51
  JOURNAL   EMBO J 18 (22), 6552-6560 (1999)
   PUBMED   10562567
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA336027.1, BC035372.1, BX496609.1, AC087651.19 and BC032219.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.239215.1,
                                           SRR1803617.151698.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000425042.7/ ENSP00000413520.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..788
                     /product="protein HID1"
                     /note="downregulated in multiple cancer 1; down-regulated
                     in multiple cancers 1; UPF0663 transmembrane protein
                     C17orf28; protein hid-1 homolog; HID1 domain-containing
                     protein"
                     /calculated_mol_wt=88614
     Region          1..785
                     /region_name="Hid1"
                     /note="High-temperature-induced dauer-formation protein;
                     pfam12722"
                     /db_xref="CDD:463680"
     Region          297..316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IV36.1)"
     Region          571..681
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IV36.1)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IV36.1)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1F6; propagated from
                     UniProtKB/Swiss-Prot (Q8IV36.1)"
     CDS             1..788
                     /gene="HID1"
                     /gene_synonym="17orf28; C17orf28; DEE105; DMC1; HID-1"
                     /coded_by="NM_030630.3:104..2470"
                     /db_xref="CCDS:CCDS32726.1"
                     /db_xref="GeneID:283987"
                     /db_xref="HGNC:HGNC:15736"
                     /db_xref="MIM:605752"
ORIGIN      
        1 mgstdsklnf rkaviqlttk tqpveatdda fwdqfwadta tsvqdvfalv paaeiravre
       61 espsnlatlc ykaveklvqg aesgchseke kqivlncsrl ltrvlpyife dpdwrgffws
      121 tvpgagrggq geeddeharp laeslllaia dllfcpdftv qshrrstvds aedvhsldsc
      181 eyiweagvgf ahspqpnyih dmnrmellkl lltcfseamy lppapesgst npwvqffcst
      241 enrhalplft sllntvcayd pvgygipynh llfsdyrepl veeaaqvliv tldhdsassa
      301 sptvdgtttg tamddadppg penlfvnyls rihreedfqf ilkgiarlls npllqtylpn
      361 stkkiqfhqe llvlfwklcd fnkkflffvl kssdvldilv pilfflndar adqsrvglmh
      421 igvfilllls gernfgvrln kpysirvpmd ipvftgthad llivvfhkii tsghqrlqpl
      481 fdclltivvn vspylkslsm vtankllhll eafsttwflf saaqnhhlvf fllevfnnii
      541 qyqfdgnsnl vyaiirkrsi fhqlanlptd pptihkalqr rrrtpeplsr tgsqegtsme
      601 gsrpaapaep gtlktslvat pgidklteks qvsedgtlrs lepepqqsle dgspakgeps
      661 qawreqrrps tssasgqwsp tpewvlswks klplqtimrl lqvlvpqvek icidkgltde
      721 seilrflqhg tlvgllpvph pilirkyqan sgtamwfrty mwgviylrnv dppvwydtdv
      781 klfeiqrv
//
LOCUS       NP_009123               1047 aa            linear   PRI 27-APR-2025
DEFINITION  FACT complex subunit SPT16 [Homo sapiens].
ACCESSION   NP_009123
VERSION     NP_009123.1
DBSOURCE    REFSEQ: accession NM_007192.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Li,Y. and Huang,H.
  TITLE     Structural basis for H2A-H2B recognitions by human Spt16
  JOURNAL   Biochem Biophys Res Commun 651, 85-91 (2023)
   PUBMED   36801613
  REMARK    GeneRIF: Structural basis for H2A-H2B recognitions by human Spt16.
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Ma,M., Zhang,X., Zheng,Y., Lu,S., Pan,X., Mao,X., Pan,H.,
            Chung,H.L., Wang,H., Guo,H. and Bellen,H.J.
  TITLE     The fly homolog of SUPT16H, a gene associated with
            neurodevelopmental disorders, is required in a cell-autonomous
            fashion for cell survival
  JOURNAL   Hum Mol Genet 32 (6), 984-997 (2023)
   PUBMED   36255738
  REMARK    GeneRIF: The fly homolog of SUPT16H, a gene associated with
            neurodevelopmental disorders, is required in a cell-autonomous
            fashion for cell survival.
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wang,J., Wang,Z., Dai,L., Zhu,X., Guan,X., Wang,J., Li,J.,
            Zhang,M., Bai,Y. and Guo,H.
  TITLE     Supt16 Haploinsufficiency Impairs PI3K/AKT/mTOR/Autophagy Pathway
            in Human Pluripotent Stem Cells Derived Neural Stem Cells
  JOURNAL   Int J Mol Sci 24 (3), 3035 (2023)
   PUBMED   36769360
  REMARK    GeneRIF: Supt16 Haploinsufficiency Impairs PI3K/AKT/mTOR/Autophagy
            Pathway in Human Pluripotent Stem Cells Derived Neural Stem Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1047)
  AUTHORS   McCauley,M.J., Morse,M., Becker,N., Hu,Q., Botuyan,M.V.,
            Navarrete,E., Huo,R., Muthurajan,U.M., Rouzina,I., Luger,K.,
            Mer,G., Maher,L.J. 3rd and Williams,M.C.
  TITLE     Human FACT subunits coordinate to catalyze both disassembly and
            reassembly of nucleosomes
  JOURNAL   Cell Rep 41 (13), 111858 (2022)
   PUBMED   36577379
  REMARK    GeneRIF: Human FACT subunits coordinate to catalyze both
            disassembly and reassembly of nucleosomes.
REFERENCE   5  (residues 1 to 1047)
  AUTHORS   Zhou,D., Wu,Z., Park,J.G., Fiches,G.N., Li,T.W., Ma,Q., Huang,H.,
            Biswas,A., Martinez-Sobrido,L., Santoso,N.G. and Zhu,J.
  TITLE     FACT subunit SUPT16H associates with BRD4 and contributes to
            silencing of interferon signaling
  JOURNAL   Nucleic Acids Res 50 (15), 8700-8718 (2022)
   PUBMED   35904816
  REMARK    GeneRIF: FACT subunit SUPT16H associates with BRD4 and contributes
            to silencing of interferon signaling.
REFERENCE   6  (residues 1 to 1047)
  AUTHORS   Wada,T., Orphanides,G., Hasegawa,J., Kim,D.K., Shima,D.,
            Yamaguchi,Y., Fukuda,A., Hisatake,K., Oh,S., Reinberg,D. and
            Handa,H.
  TITLE     FACT relieves DSIF/NELF-mediated inhibition of transcriptional
            elongation and reveals functional differences between P-TEFb and
            TFIIH
  JOURNAL   Mol Cell 5 (6), 1067-1072 (2000)
   PUBMED   10912001
REFERENCE   7  (residues 1 to 1047)
  AUTHORS   Kang,S.W., Kuzuhara,T. and Horikoshi,M.
  TITLE     Functional interaction of general transcription initiation factor
            TFIIE with general chromatin factor SPT16/CDC68
  JOURNAL   Genes Cells 5 (4), 251-263 (2000)
   PUBMED   10792464
REFERENCE   8  (residues 1 to 1047)
  AUTHORS   Orphanides,G., Wu,W.H., Lane,W.S., Hampsey,M. and Reinberg,D.
  TITLE     The chromatin-specific transcription elongation factor FACT
            comprises human SPT16 and SSRP1 proteins
  JOURNAL   Nature 400 (6741), 284-288 (1999)
   PUBMED   10421373
REFERENCE   9  (residues 1 to 1047)
  AUTHORS   LeRoy,G., Orphanides,G., Lane,W.S. and Reinberg,D.
  TITLE     Requirement of RSF and FACT for transcription of chromatin
            templates in vitro
  JOURNAL   Science 282 (5395), 1900-1904 (1998)
   PUBMED   9836642
REFERENCE   10 (residues 1 to 1047)
  AUTHORS   Orphanides,G., LeRoy,G., Chang,C.H., Luse,D.S. and Reinberg,D.
  TITLE     FACT, a factor that facilitates transcript elongation through
            nucleosomes
  JOURNAL   Cell 92 (1), 105-116 (1998)
   PUBMED   9489704
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK024072.1, AK001719.1,
            BC014046.2, BP872403.1 and AL135744.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Transcription of protein-coding genes can be reconstituted
            on naked DNA with only the general transcription factors and RNA
            polymerase II. However, this minimal system cannot transcribe DNA
            packaged into chromatin, indicating that accessory factors may
            facilitate access to DNA. One such factor, FACT (facilitates
            chromatin transcription), interacts specifically with histones
            H2A/H2B to effect nucleosome disassembly and transcription
            elongation. FACT is composed of an 80 kDa subunit and a 140 kDa
            subunit; this gene encodes the 140 kDa subunit. [provided by
            RefSeq, Feb 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.7420079.1,
                                           SRR11853567.8739.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216297.7/ ENSP00000216297.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..1047
                     /product="FACT complex subunit SPT16"
                     /note="facilitates chromatin remodeling 140 kDa subunit;
                     hSPT16; FACT 140 kDa subunit; facilitates chromatin
                     transcription complex subunit SPT16; chromatin-specific
                     transcription elongation factor 140 kDa subunit;
                     suppressor of Ty 16 homolog"
                     /calculated_mol_wt=119783
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.3,
                     ECO:0000269|Ref.4, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Region          5..1001
                     /region_name="COG5406"
                     /note="Nucleosome binding factor SPN, SPT16 subunit
                     [Transcription, Replication, recombination and repair,
                     Chromatin structure and dynamics]"
                     /db_xref="CDD:227693"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            196
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            223
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Region          492..518
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            513
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            732
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            786
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            904
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Region          918..1047
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            982
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            986
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     Site            1015
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5B9.1)"
     CDS             1..1047
                     /gene="SUPT16H"
                     /gene_synonym="CDC68; FACTP140; NEDDFAC; SPT16;
                     SPT16/CDC68"
                     /coded_by="NM_007192.4:93..3236"
                     /db_xref="CCDS:CCDS9569.1"
                     /db_xref="GeneID:11198"
                     /db_xref="HGNC:HGNC:11465"
                     /db_xref="MIM:605012"
ORIGIN      
        1 mavtldkday yrrvkrlysn wrkgedeyan vdaivvsvgv deeivyakst alqtwlfgye
       61 ltdtimvfcd dkiifmaskk kveflkqian tkgnenanga paitllirek nesnkssfdk
      121 mieaikeskn gkkigvfskd kfpgefmksw ndclnkegfd kidisavvay tiavkedgel
      181 nlmkkaasit sevfnkffke rvmeivdade kvrhsklaes vekaieekky lagadpstve
      241 mcyppiiqsg gnynlkfsvv sdknhmhfga itcamgirfk sycsnlvrtl mvdpsqevqe
      301 nynfllqlqe ellkelrhgv kicdvynavm dvvkkqkpel lnkitknlgf gmgiefregs
      361 lvinsknqyk lkkgmvfsin lgfsdltnke gkkpeektya lfigdtvlvd edgpatvlts
      421 vkkkvknvgi flknedeeee eeekdeaedl lgrgsraall tertrnemta eekrrahqke
      481 laaqlneeak rrlteqkgeq qiqkarksnv syknpslmpk ephiremkiy idkkyetvim
      541 pvfgiatpfh iatiknisms vegdytylri nfycpgsalg rnegnifpnp eatfvkeity
      601 rasnikapge qtvpalnlqn afriikevqk ryktreaeek ekegivkqds lvinlnrsnp
      661 klkdlyirpn iaqkrmqgsl eahvngfrft svrgdkvdil ynnikhalfq pcdgemiivl
      721 hfhlknaimf gkkrhtdvqf ytevgeittd lgkhqhmhdr ddlyaeqmer emrhklktaf
      781 knfiekveal tkeelefevp frdlgfngap yrstcllqpt ssalvnatew ppfvvtldev
      841 elihfervqf hlknfdmviv ykdyskkvtm inaipvasld pikewlnscd lkytegvqsl
      901 nwtkimktiv ddpegffeqg gwsflepege gsdaeegdse seiedetfnp seddyeeeee
      961 dsdedyssea eesdyskesl gseeesgkdw deleeearka dresryeeee eqsrsmsrkr
     1021 kasvhssgrg snrgsrhssa ppkkkrk
//
LOCUS       NP_067653                376 aa            linear   PRI 27-APR-2025
DEFINITION  MYG1 exonuclease precursor [Homo sapiens].
ACCESSION   NP_067653
VERSION     NP_067653.4
DBSOURCE    REFSEQ: accession NM_021640.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Chen,J., Duan,S., Wang,Y., Ling,Y., Hou,X., Zhang,S., Liu,X.,
            Long,X., Lan,J., Zhou,M., Xu,H., Zheng,H. and Zhou,J.
  TITLE     MYG1 drives glycolysis and colorectal cancer development through
            nuclear-mitochondrial collaboration
  JOURNAL   Nat Commun 15 (1), 4969 (2024)
   PUBMED   38862489
  REMARK    GeneRIF: MYG1 drives glycolysis and colorectal cancer development
            through nuclear-mitochondrial collaboration.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Grover,R., Burse,S.A., Shankrit,S., Aggarwal,A., Kirty,K.,
            Narta,K., Srivastav,R., Ray,A.K., Malik,G., Vats,A., Motiani,R.K.,
            Thukral,L., Roy,S.S., Bhattacharya,S., Sharma,R., Natarajan,K.,
            Mukerji,M., Pandey,R., Gokhale,R.S. and Natarajan,V.T.
  TITLE     Myg1 exonuclease couples the nuclear and mitochondrial
            translational programs through RNA processing
  JOURNAL   Nucleic Acids Res 47 (11), 5852-5866 (2019)
   PUBMED   31081026
  REMARK    GeneRIF: analysis of the widely conserved dually localized protein
            Myg1 shows that it has a role as a 3'-5' RNA exonuclease
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Dwivedi,M., Laddha,N.C. and Begum,R.
  TITLE     Correlation of increased MYG1 expression and its promoter
            polymorphism with disease progression and higher susceptibility in
            vitiligo patients
  JOURNAL   J Dermatol Sci 71 (3), 195-202 (2013)
   PUBMED   23706493
  REMARK    GeneRIF: Significant increase in MYG1 mRNA expression was observed
            in vitiligo patients compared to controls. The MYG1 mRNA expression
            was increased in patients with active and generalized vitiligo as
            compared to stable and localized vitiligo.
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Philips,M.A., Kingo,K., Karelson,M., Ratsep,R., Aunin,E.,
            Reimann,E., Reemann,P., Porosaar,O., Vikesa,J., Nielsen,F.C.,
            Vasar,E., Silm,H. and Koks,S.
  TITLE     Promoter polymorphism -119C/G in MYG1 (C12orf10) gene is related to
            vitiligo susceptibility and Arg4Gln affects mitochondrial entrance
            of Myg1
  JOURNAL   BMC Med Genet 11, 56 (2010)
   PUBMED   20377893
  REMARK    GeneRIF: Both MYG1 promoter polymorphism and Arg4Gln polymorphism
            in the mitochondrial signal of Myg1 have an impact on the
            regulation of the MYG1 gene and promoter polymorphism is related
            with suspectibility for actively progressing vitiligo.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Philips,M.A., Vikesa,J., Luuk,H., Jonson,L., Lillevali,K.,
            Rehfeld,J.F., Vasar,E., Koks,S. and Nielsen,F.C.
  TITLE     Characterization of MYG1 gene and protein: subcellular distribution
            and function
  JOURNAL   Biol Cell 101 (6), 361-373 (2009)
   PUBMED   19014353
  REMARK    GeneRIF: Human and mouse MYG1 is ubiquitously expressed, with the
            highest level in the testis.
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Kingo,K., Philips,M.A., Aunin,E., Luuk,H., Karelson,M., Ratsep,R.,
            Silm,H., Vasar,E. and Koks,S.
  TITLE     MYG1, novel melanocyte related gene, has elevated expression in
            vitiligo
  JOURNAL   J Dermatol Sci 44 (2), 119-122 (2006)
   PUBMED   16996721
  REMARK    GeneRIF: demonstrates possible role of MYG1 in vitiligo
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073611.29.
            
            On Nov 23, 2018 this sequence version replaced NP_067653.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.78169.1,
                                           SRR5189667.119582.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267103.10/ ENSP00000267103.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..376
                     /product="MYG1 exonuclease precursor"
                     /note="melanocyte related; UPF0160 protein MYG1,
                     mitochondrial; melanocyte proliferating gene 1"
                     /calculated_mol_wt=37113
     transit_peptide 1..47
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9HB07.4)"
                     /calculated_mol_wt=5355
     Region          46..366
                     /region_name="UPF0160"
                     /note="Uncharacterized protein family (UPF0160);
                     pfam03690"
                     /db_xref="CDD:461014"
     mat_peptide     48..376
                     /product="MYG1 exonuclease. /id=PRO_0000213483"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB07.4)"
                     /calculated_mol_wt=37113
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HB07.4)"
     Site            267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9HB07.4)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JK81; propagated from
                     UniProtKB/Swiss-Prot (Q9HB07.4)"
     CDS             1..376
                     /gene="MYG1"
                     /gene_synonym="C12orf10; Gamm1; MST024; MSTP024; MYG"
                     /coded_by="NM_021640.4:44..1174"
                     /db_xref="CCDS:CCDS31810.1"
                     /db_xref="GeneID:60314"
                     /db_xref="HGNC:HGNC:17590"
                     /db_xref="MIM:611366"
ORIGIN      
        1 mghqflrgll tlllpppply trhrmlgpes vpppkrsrsk lmapprigth ngtfhcdeal
       61 acallrllpe yrdaeivrtr dpeklascdi vvdvggeydp rrhrydhhqr sftetmssls
      121 pgkpwqtkls sagliylhfg hkllaqllgt seedsmvgtl ydkmyenfve evdavdngis
      181 qwaegeprya ltttlsarva rlnptwnhpd qdteagfkra mdlvqeeflq rldfyqhswl
      241 paralveeal aqrfqvdpsg eivelakgac pwkehlyhle sglsppvaif fviytdqagq
      301 wriqcvpkep hsfqsrlplp epwrglrdea ldqvsgipgc ifvhasgftg ghhtregals
      361 maratlaqrs ylpqis
//
LOCUS       NP_004066                586 aa            linear   PRI 27-APR-2025
DEFINITION  cryptochrome-1 isoform d [Homo sapiens].
ACCESSION   NP_004066
VERSION     NP_004066.1
DBSOURCE    REFSEQ: accession NM_004075.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Ma,J., Chen,S., Liu,J., Liao,Y., Li,L., Wang,C.C., Song,S.,
            Feng,R., Hu,H. and Quan,S.
  TITLE     Cryptochrome 1 regulates ovarian granulosa cell senescence through
            NCOA4-mediated ferritinophagy
  JOURNAL   Free Radic Biol Med 217, 1-14 (2024)
   PUBMED   38522484
  REMARK    GeneRIF: Cryptochrome 1 regulates ovarian granulosa cell senescence
            through NCOA4-mediated ferritinophagy.
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Chiou,Y.Y., Lee,C.Y., Yang,H.W., Cheng,W.C. and Ji,K.D.
  TITLE     Circadian modulation of glucose utilization via CRY1-mediated
            repression of Pdk1 expression
  JOURNAL   J Biol Chem 300 (2), 105637 (2024)
   PUBMED   38199564
  REMARK    GeneRIF: Circadian modulation of glucose utilization via
            CRY1-mediated repression of Pdk1 expression.
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Liu,D., Xie,Z., Gu,P., Li,X., Zhang,Y., Wang,X., Chen,Z., Deng,S.,
            Shu,Y. and Li,J.D.
  TITLE     Cry1Delta11 mutation induces ADHD-like symptoms through hyperactive
            dopamine D1 receptor signaling
  JOURNAL   JCI Insight 8 (16), e170434 (2023)
   PUBMED   37606043
  REMARK    GeneRIF: Cry1Delta11 mutation induces ADHD-like symptoms through
            hyperactive dopamine D1 receptor signaling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Sancar,A.
  TITLE     Regulation of the mammalian circadian clock by cryptochrome
  JOURNAL   J Biol Chem 279 (33), 34079-34082 (2004)
   PUBMED   15123698
  REMARK    Review article
REFERENCE   5  (residues 1 to 586)
  AUTHORS   van der Horst,G.T., Muijtjens,M., Kobayashi,K., Takano,R.,
            Kanno,S., Takao,M., de Wit,J., Verkerk,A., Eker,A.P., van
            Leenen,D., Buijs,R., Bootsma,D., Hoeijmakers,J.H. and Yasui,A.
  TITLE     Mammalian Cry1 and Cry2 are essential for maintenance of circadian
            rhythms
  JOURNAL   Nature 398 (6728), 627-630 (1999)
   PUBMED   10217146
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Kobayashi,K., Kanno,S., Smit,B., van der Horst,G.T., Takao,M. and
            Yasui,A.
  TITLE     Characterization of photolyase/blue-light receptor homologs in
            mouse and human cells
  JOURNAL   Nucleic Acids Res 26 (22), 5086-5092 (1998)
   PUBMED   9801304
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Zhao,S. and Sancar,A.
  TITLE     Human blue-light photoreceptor hCRY2 specifically interacts with
            protein serine/threonine phosphatase 5 and modulates its activity
  JOURNAL   Photochem Photobiol 66 (5), 727-731 (1997)
   PUBMED   9383998
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Hsu,D.S., Zhao,X., Zhao,S., Kazantsev,A., Wang,R.P., Todo,T.,
            Wei,Y.F. and Sancar,A.
  TITLE     Putative human blue-light photoreceptors hCRY1 and hCRY2 are
            flavoproteins
  JOURNAL   Biochemistry 35 (44), 13871-13877 (1996)
   PUBMED   8909283
REFERENCE   9  (residues 1 to 586)
  AUTHORS   van der Spek,P.J., Kobayashi,K., Bootsma,D., Takao,M., Eker,A.P.
            and Yasui,A.
  TITLE     Cloning, tissue expression, and mapping of a human photolyase
            homolog with similarity to plant blue-light receptors
  JOURNAL   Genomics 37 (2), 177-182 (1996)
   PUBMED   8921389
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Todo,T., Ryo,H., Yamamoto,K., Toh,H., Inui,T., Ayaki,H., Nomura,T.
            and Ikenaga,M.
  TITLE     Similarity among the Drosophila (6-4)photolyase, a human photolyase
            homolog, and the DNA photolyase-blue-light photoreceptor family
  JOURNAL   Science 272 (5258), 109-112 (1996)
   PUBMED   8600518
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB454192.1, BJ993835.1,
            AK290552.1 and BC017466.1.
            
            Summary: This gene encodes a flavin adenine dinucleotide-binding
            protein that is a key component of the circadian core oscillator
            complex, which regulates the circadian clock. This gene is
            upregulated by CLOCK/ARNTL heterodimers but then represses this
            upregulation in a feedback loop using PER/CRY heterodimers to
            interact with CLOCK/ARNTL. Polymorphisms in this gene have been
            associated with altered sleep patterns. The encoded protein is
            widely conserved across plants and animals. Loss of the related
            gene in mouse results in a shortened circadian cycle in complete
            darkness. [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D83702.1, BC017466.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2147920
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000008527.10/ ENSP00000008527.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..586
                     /product="cryptochrome-1 isoform d"
                     /note="cryptochrome-1; cryptochrome 1 (photolyase-like);
                     cryptochrome circadian clock 1"
                     /calculated_mol_wt=66264
     Region          5..487
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
     Region          50..54
                     /region_name="LIR 1.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:P97784; propagated from
                     UniProtKB/Swiss-Prot (Q16526.1)"
     Region          82..87
                     /region_name="LIR 2.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          151..156
                     /region_name="LIR 3.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK.
                     /evidence=ECO:0000250|UniProtKB:P97784; propagated from
                     UniProtKB/Swiss-Prot (Q16526.1)"
     Region          255..260
                     /region_name="LIR 4.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          271..276
                     /region_name="LIR 5.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:P97784; propagated from
                     UniProtKB/Swiss-Prot (Q16526.1)"
     Region          285..290
                     /region_name="LIR 6.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          335..339
                     /region_name="LIR 7.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          371..470
                     /region_name="Required for inhibition of
                     CLOCK-BMAL1-mediated transcription.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          379..384
                     /region_name="LIR 8.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          395..400
                     /region_name="LIR 9.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          411..416
                     /region_name="LIR 10.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          430..435
                     /region_name="LIR 11.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          471..493
                     /region_name="Interaction with TIMELESS.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          486..491
                     /region_name="LIR 12.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          492..497
                     /region_name="LIR 13.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Region          552..586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16526.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97784; propagated from
                     UniProtKB/Swiss-Prot (Q16526.1)"
     CDS             1..586
                     /gene="CRY1"
                     /gene_synonym="DSPD; PHLL1"
                     /coded_by="NM_004075.5:589..2349"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS9112.1"
                     /db_xref="GeneID:1407"
                     /db_xref="HGNC:HGNC:2384"
                     /db_xref="MIM:601933"
ORIGIN      
        1 mgvnavhwfr kglrlhdnpa lkeciqgadt ircvyildpw fagssnvgin rwrfllqcle
       61 dldanlrkln srlfvirgqp advfprlfke wnitklsiey dsepfgkerd aaikklatea
      121 gvevivrish tlydldkiie lnggqpplty krfqtliskm epleipveti tseviekctt
      181 plsddhdeky gvpsleelgf dtdglssavw pggetealtr lerhlerkaw vanferprmn
      241 ansllasptg lspylrfgcl scrlfyfklt dlykkvkkns spplslygql lwreffytaa
      301 tnnprfdkme gnpicvqipw dknpealakw aegrtgfpwi daimtqlrqe gwihhlarha
      361 vacfltrgdl wisweegmkv feellldadw sinagswmwl scssffqqff hcycpvgfgr
      421 rtdpngdyir rylpvlrgfp akyiydpwna pegiqkvakc ligvnypkpm vnhaeasrln
      481 iermkqiyqq lsryrglgll asvpsnpngn ggfmgysaen ipgcsssgsc sqgsgilhya
      541 hgdsqqthll kqgrssmgtg lsggkrpsqe edtqsigpkv qrqstn
//
LOCUS       NP_006007                197 aa            linear   PRI 27-APR-2025
DEFINITION  sialomucin core protein 24 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_006007
VERSION     NP_006007.2
DBSOURCE    REFSEQ: accession NM_006016.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Liu,J., Knopp,K.A., Rackaityte,E., Wang,C.Y., Laurie,M.T.,
            Sunshine,S., Puschnik,A.S. and DeRisi,J.L.
  TITLE     Genome-Wide Knockout Screen Identifies Human Sialomucin CD164 as an
            Essential Entry Factor for Lymphocytic Choriomeningitis Virus
  JOURNAL   mBio 13 (3), e0020522 (2022)
   PUBMED   35502904
  REMARK    GeneRIF: Genome-Wide Knockout Screen Identifies Human Sialomucin
            CD164 as an Essential Entry Factor for Lymphocytic Choriomeningitis
            Virus.
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Ozieblo,D., Lee,S.Y., Leja,M.L., Sarosiak,A., Baldyga,N.,
            Skarzynski,H., Kim,Y., Han,J.H., Yoo,H.S., Park,M.H., Choi,B.Y. and
            Oldak,M.
  TITLE     Update on CD164 and LMX1A genes to strengthen their causative role
            in autosomal dominant hearing loss
  JOURNAL   Hum Genet 141 (3-4), 445-453 (2022)
   PUBMED   35254497
  REMARK    GeneRIF: Update on CD164 and LMX1A genes to strengthen their
            causative role in autosomal dominant hearing loss.
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Bakkers,M.J.G., Moon-Walker,A., Herlo,R., Brusic,V., Stubbs,S.H.,
            Hastie,K.M., Saphire,E.O., Kirchhausen,T.L. and Whelan,S.P.J.
  TITLE     CD164 is a host factor for lymphocytic choriomeningitis virus entry
  JOURNAL   Proc Natl Acad Sci U S A 119 (10), e2119676119 (2022)
   PUBMED   35235462
  REMARK    GeneRIF: CD164 is a host factor for lymphocytic choriomeningitis
            virus entry.
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Zhang,X.W., Li,S.L., Zhang,D., Sun,X.L. and Zhai,H.J.
  TITLE     RP11-619L19.2 promotes colon cancer development by regulating the
            miR-1271-5p/CD164 axis
  JOURNAL   Oncol Rep 44 (6), 2419-2428 (2020)
   PUBMED   33125110
  REMARK    GeneRIF: RP11619L19.2 promotes colon cancer development by
            regulating the miR12715p/CD164 axis.
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Zhang,L., Wang,Y. and Su,H.
  TITLE     Long non-coding RNA LINC00152/miR-613/CD164 axis regulates cell
            proliferation, apoptosis, migration and invasion in glioma via
            PI3K/AKT pathway
  JOURNAL   Neoplasma 67 (4), 762-772 (2020)
   PUBMED   32726126
  REMARK    GeneRIF: Long non-coding RNA LINC00152/miR-613/CD164 axis regulates
            cell proliferation, apoptosis, migration and invasion in glioma via
            PI3K/AKT pathway.
REFERENCE   6  (residues 1 to 197)
  AUTHORS   Doyonnas,R., Yi-Hsin Chan,J., Butler,L.H., Rappold,I.,
            Lee-Prudhoe,J.E., Zannettino,A.C., Simmons,P.J., Buhring,H.J.,
            Levesque,J.P. and Watt,S.M.
  TITLE     CD164 monoclonal antibodies that block hemopoietic progenitor cell
            adhesion and proliferation interact with the first mucin domain of
            the CD164 receptor
  JOURNAL   J Immunol 165 (2), 840-851 (2000)
   PUBMED   10878358
REFERENCE   7  (residues 1 to 197)
  AUTHORS   Kurosawa,N., Kanemitsu,Y., Matsui,T., Shimada,K., Ishihama,H. and
            Muramatsu,T.
  TITLE     Genomic analysis of a murine cell-surface sialomucin, MGC-24/CD164
  JOURNAL   Eur J Biochem 265 (1), 466-472 (1999)
   PUBMED   10491205
REFERENCE   8  (residues 1 to 197)
  AUTHORS   Zannettino,A.C., Buhring,H.J., Niutta,S., Watt,S.M., Benton,M.A.
            and Simmons,P.J.
  TITLE     The sialomucin CD164 (MGC-24v) is an adhesive glycoprotein
            expressed by human hematopoietic progenitors and bone marrow
            stromal cells that serves as a potent negative regulator of
            hematopoiesis
  JOURNAL   Blood 92 (8), 2613-2628 (1998)
   PUBMED   9763543
REFERENCE   9  (residues 1 to 197)
  AUTHORS   Watt,S.M., Buhring,H.J., Rappold,I., Chan,J.Y., Lee-Prudhoe,J.,
            Jones,T., Zannettino,A.C., Simmons,P.J., Doyonnas,R., Sheer,D. and
            Butler,L.H.
  TITLE     CD164, a novel sialomucin on CD34(+) and erythroid subsets, is
            located on human chromosome 6q21
  JOURNAL   Blood 92 (3), 849-866 (1998)
   PUBMED   9680353
REFERENCE   10 (residues 1 to 197)
  AUTHORS   Masuzawa,Y., Miyauchi,T., Hamanoue,M., Ando,S., Yoshida,J.,
            Takao,S., Shimazu,H., Adachi,M. and Muramatsu,T.
  TITLE     A novel core protein as well as polymorphic epithelial mucin carry
            peanut agglutinin binding sites in human gastric carcinoma cells:
            sequence analysis and examination of gene expression
  JOURNAL   J Biochem 112 (5), 609-615 (1992)
   PUBMED   1478919
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359711.18.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_006007.1.
            
            Summary: This gene encodes a transmembrane sialomucin and cell
            adhesion molecule that regulates the proliferation, adhesion and
            migration of hematopoietic progenitor cells. The encoded protein
            also interacts with the C-X-C chemokine receptor type 4 and may
            regulate muscle development. Elevated expression of this gene has
            been observed in human patients with Sezary syndrome, a type of
            blood cancer, and a mutation in this gene may be associated with
            impaired hearing. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.888542.1,
                                           SRR1803616.179464.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03568911 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310786.10/ ENSP00000309376.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..197
                     /product="sialomucin core protein 24 isoform 1 precursor"
                     /note="CD164 antigen, sialomucin; sialomucin core protein
                     24; multi-glycosylated core protein 24"
                     /calculated_mol_wt=18484
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2451
     mat_peptide     24..197
                     /product="Sialomucin core protein 24. /id=PRO_0000019292"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04900.2)"
                     /calculated_mol_wt=18484
     Site            26
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            32
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Region          60..197
                     /region_name="MGC-24"
                     /note="Multi-glycosylated core protein 24 (MGC-24),
                     sialomucin; pfam05283"
                     /db_xref="CDD:461610"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Region          118..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04900.2)"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            142
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04900.2)"
     Site            163..183
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04900.2)"
     Region          191..197
                     /region_name="Required for endosomal and lysosomal
                     localization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04900.2)"
     CDS             1..197
                     /gene="CD164"
                     /gene_synonym="DFNA66; endolyn; MGC-24; MGC-24v; MUC-24"
                     /coded_by="NM_006016.6:90..683"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS5073.1"
                     /db_xref="GeneID:8763"
                     /db_xref="HGNC:HGNC:1632"
                     /db_xref="MIM:603356"
ORIGIN      
        1 msrlsrsllw aatclgvlcv lsadknttqh pnvttlapis nvtsapvtsl plvttpapet
       61 cegrnscvsc fnvsvvnttc fwieckdesy cshnstvsdc qvgnttdfcs vstatpvpta
      121 nstakptvqp spsttsktvt tsgttnntvt ptsqpvrkst fdaasfiggi vlvlgvqavi
      181 fflykfcksk ernyhtl
//
LOCUS       NP_005725               1215 aa            linear   PRI 27-APR-2025
DEFINITION  homeodomain-interacting protein kinase 3 isoform 1 [Homo sapiens].
ACCESSION   NP_005725
VERSION     NP_005725.3
DBSOURCE    REFSEQ: accession NM_005734.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1215)
  AUTHORS   Wu,Y., Huang,J., Liu,L., Zhang,X., Zhang,W. and Li,Q.
  TITLE     CircHIPK3/miR-124 affects angiogenesis in early-onset preeclampsia
            via CPT1A-mediated fatty acid oxidation
  JOURNAL   J Mol Med (Berl) 102 (8), 1037-1049 (2024)
   PUBMED   38904677
  REMARK    GeneRIF: CircHIPK3/miR-124 affects angiogenesis in early-onset
            preeclampsia via CPT1A-mediated fatty acid oxidation.
REFERENCE   2  (residues 1 to 1215)
  AUTHORS   Wu,Q.N., Qi,J., Liu,Z.K., Luo,X.J., Yu,K., Lu,Y.X., Wang,Y.,
            Jin,Y., Liu,J., Huang,L.Y., Zeng,Z.L., Zheng,Y., Xu,R.H. and
            Liu,Z.X.
  TITLE     HIPK3 maintains sensitivity to platinum drugs and prevents disease
            progression in gastric cancer
  JOURNAL   Cancer Lett 584, 216643 (2024)
   PUBMED   38246220
  REMARK    GeneRIF: HIPK3 maintains sensitivity to platinum drugs and prevents
            disease progression in gastric cancer.
REFERENCE   3  (residues 1 to 1215)
  AUTHORS   Mon,A.M., Intuyod,K., Klungsaeng,S., Jusakul,A., Pongking,T.,
            Lert-Itthiporn,W., Luvira,V., Pairojkul,C., Plengsuriyakarn,T.,
            Na-Bangchang,K., Pinlaor,S. and Pinlaor,P.
  TITLE     Overexpression of microRNA-205-5p promotes cholangiocarcinoma
            growth by reducing expression of homeodomain-interacting protein
            kinase 3
  JOURNAL   Sci Rep 13 (1), 22444 (2023)
   PUBMED   38105269
  REMARK    GeneRIF: Overexpression of microRNA-205-5p promotes
            cholangiocarcinoma growth by reducing expression of
            homeodomain-interacting protein kinase 3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1215)
  AUTHORS   Feng,S., Qi,Y., Xiao,Z., Chen,H., Liu,S., Luo,H., Wu,H. and
            Zhang,W.
  TITLE     CircHIPK3 relieves vascular calcification via mediating
            SIRT1/PGC-1alpha/MFN2 pathway by interacting with FUS
  JOURNAL   BMC Cardiovasc Disord 23 (1), 583 (2023)
   PUBMED   38012555
  REMARK    GeneRIF: CircHIPK3 relieves vascular calcification via mediating
            SIRT1/PGC-1alpha/MFN2 pathway by interacting with FUS.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1215)
  AUTHORS   Jiang,J., Gao,H., Zhou,W., Cai,H., Liao,L. and Wang,C.
  TITLE     Circular RNA HIPK3 facilitates ferroptosis in gestational diabetes
            mellitus by regulating glutathione peroxidase 4 DNA methylation
  JOURNAL   J Gene Med 25 (9), e3526 (2023)
   PUBMED   37253602
  REMARK    GeneRIF: Circular RNA HIPK3 facilitates ferroptosis in gestational
            diabetes mellitus by regulating glutathione peroxidase 4 DNA
            methylation.
REFERENCE   6  (residues 1 to 1215)
  AUTHORS   Scaffidi,C., Volkland,J., Blomberg,I., Hoffmann,I., Krammer,P.H.
            and Peter,M.E.
  TITLE     Phosphorylation of FADD/ MORT1 at serine 194 and association with a
            70-kDa cell cycle-regulated protein kinase
  JOURNAL   J Immunol 164 (3), 1236-1242 (2000)
   PUBMED   10640736
REFERENCE   7  (residues 1 to 1215)
  AUTHORS   Nupponen,N.N. and Visakorpi,T.
  TITLE     Assignment of the protein kinase homolog of YAK1 (HIPK3) to human
            chromosome band 11p13 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 87 (1-2), 102-103 (1999)
   PUBMED   10640824
REFERENCE   8  (residues 1 to 1215)
  AUTHORS   Kim,Y.H., Choi,C.Y., Lee,S.J., Conti,M.A. and Kim,Y.
  TITLE     Homeodomain-interacting protein kinases, a novel family of
            co-repressors for homeodomain transcription factors
  JOURNAL   J Biol Chem 273 (40), 25875-25879 (1998)
   PUBMED   9748262
REFERENCE   9  (residues 1 to 1215)
  AUTHORS   Moilanen,A.M., Karvonen,U., Poukka,H., Janne,O.A. and Palvimo,J.J.
  TITLE     Activation of androgen receptor function by a novel nuclear protein
            kinase
  JOURNAL   Mol Biol Cell 9 (9), 2527-2543 (1998)
   PUBMED   9725910
REFERENCE   10 (residues 1 to 1215)
  AUTHORS   Begley,D.A., Berkenpas,M.B., Sampson,K.E. and Abraham,I.
  TITLE     Identification and sequence of human PKY, a putative kinase with
            increased expression in multidrug-resistant cells, with homology to
            yeast protein kinase Yak1
  JOURNAL   Gene 200 (1-2), 35-43 (1997)
   PUBMED   9373137
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY053621.1, DR000092.1, Y09306.1, AF004849.1, AL122015.17 and
            BX117467.1.
            
            On Sep 19, 2006 this sequence version replaced NP_005725.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.144149.1,
                                           SRR1660809.112552.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303296.9/ ENSP00000304226.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..1215
                     /product="homeodomain-interacting protein kinase 3 isoform
                     1"
                     /EC_number="2.7.11.1"
                     /note="ANPK; FIST; homolog of protein kinase YAK1;
                     fas-interacting serine/threonine-protein kinase; androgen
                     receptor-interacting nuclear protein kinase"
                     /calculated_mol_wt=133613
     Region          196..525
                     /region_name="STKc_HIPK3"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Homeodomain-Interacting Protein Kinase 3; cd14229"
                     /db_xref="CDD:271131"
     Site            order(203..207,211,224,226,240,259,275..278,281,283..284,
                     322,324,326..327,329,344,347,357,359..362,364,401)
                     /site_type="active"
                     /db_xref="CDD:271131"
     Site            order(203..207,211,224,226,259,275..278,281,322,324,
                     326..327,329,344)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271131"
     Site            order(240,283,322,324,347,357,359..362,364,401)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271131"
     Site            343..364
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271131"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERH7; propagated from
                     UniProtKB/Swiss-Prot (Q9H422.1)"
     Region          767..944
                     /region_name="Interaction with AR. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H422.1)"
     Region          796..891
                     /region_name="Interaction with FAS. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H422.1)"
     Region          <814..1021
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          855..1011
                     /region_name="Required for localization to nuclear
                     speckles. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H422.1)"
     Region          866..918
                     /region_name="SUMO interaction motifs (SIM), required for
                     nuclear localization and kinase activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H422.1)"
     Region          870..880
                     /region_name="Interaction with UBL1.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H422.1)"
     Region          912..987
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H422.1)"
     CDS             1..1215
                     /gene="HIPK3"
                     /gene_synonym="DYRK6; FIST3; PKY; YAK1"
                     /coded_by="NM_005734.5:512..4159"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7884.1"
                     /db_xref="GeneID:10114"
                     /db_xref="HGNC:HGNC:4915"
                     /db_xref="MIM:604424"
ORIGIN      
        1 masqvlvypp yvyqtqssaf csvkklkvep sscvfqerny prtyvngrnf gnshpptkgs
       61 afqtkipfnr prghnfslqt savvlkntag atkviaaqaq qahvqapqig awrnrlhfle
      121 gpqrcglkrk seeldnhssa mqivdelsil pamlqtnmgn pvtvvtattg skqncttgeg
      181 dyqlvqhevl csmkntyevl dflgrgtfgq vvkcwkrgtn eivaikilkn hpsyarqgqi
      241 evsilarlst enadeynfvr ayecfqhrnh tclvfemleq nlydflkqnk fsplplkvir
      301 pilqqvatal kklkslglih adlkpeniml vdpvrqpyrv kvidfgsash vsktvcstyl
      361 qsryyrapei ilglpfceai dmwslgcvia elflgwplyp galeydqiry isqtqglpge
      421 qllnvgtkst rffcketdms hsgwrlktle eheaetgmks kearkyifns lddvahvntv
      481 mdlegsdlla ekadrrefvs llkkmllida dlritpaetl nhpfvnmkhl ldfphsnhvk
      541 scfhimdick shlnscdtnn hnktsllrpv assstatlta nftkigtlrs qalttsahsv
      601 vhhgiplqag taqfgcgdaf qqtliicppa iqgipathgk ptsysirvdn tvplvtqapa
      661 vqplqirpgv lsqtwsgrtq qmlvpawqqv tplapatttl tsesvagshr lgdwgkmisc
      721 snhynsvmpq plltnqitls apqpvsvgia hvvwpqpatt kknkqcqnrg ilvklmewep
      781 greeinafsw snslqntnip hsafispkii ngkdveevsc ietqdnqnse gearnccets
      841 irqdsdssvs dkqrqtiiia dspspavsvi tissdtdeee tsqrhslrec kgsldceacq
      901 stlnidrmcs lsspdstlst sssgqsspsp ckrpnsmsde eqesscdtvd gsptsdssgh
      961 dspfaestfv edthentelv ssadtetkpa vcsvvvppve lenglnadeh mantdsicqp
     1021 likgrsapgr lnqpsavgtr qqkltsafqq qhlnfsqvqh fgsghqewng nfghrrqqay
     1081 iptsvtsnpf tlshgspnht avhahlagnt hlggqptllp ypssatlssa apvahllasp
     1141 ctsrpmlqhp tynishpsgi vhqvpvglnp rllpsptihq tqykpifpph syiaaspayt
     1201 gfplsptkls qypym
//
LOCUS       NP_001295067             110 aa            linear   PRI 27-APR-2025
DEFINITION  protein archease isoform 5 [Homo sapiens].
ACCESSION   NP_001295067 XP_011539641
VERSION     NP_001295067.1
DBSOURCE    REFSEQ: accession NM_001308138.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Mason,C.C., Khorashad,J.S., Tantravahi,S.K., Kelley,T.W.,
            Zabriskie,M.S., Yan,D., Pomicter,A.D., Reynolds,K.R., Eiring,A.M.,
            Kronenberg,Z., Sherman,R.L., Tyner,J.W., Dalley,B.K., Dao,K.H.,
            Yandell,M., Druker,B.J., Gotlib,J., O'Hare,T. and Deininger,M.W.
  TITLE     Age-related mutations and chronic myelomonocytic leukemia
  JOURNAL   Leukemia 30 (4), 906-913 (2016)
   PUBMED   26648538
  REMARK    GeneRIF: ARCH mutation is associated with chronic myelomonocytic
            leukemia.
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Jurkin,J., Henkel,T., Nielsen,A.F., Minnich,M., Popow,J.,
            Kaufmann,T., Heindl,K., Hoffmann,T., Busslinger,M. and Martinez,J.
  TITLE     The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA
            and controls antibody secretion in plasma cells
  JOURNAL   EMBO J 33 (24), 2922-2936 (2014)
   PUBMED   25378478
  REMARK    GeneRIF: RTCB, the catalytic subunit of the tRNA ligase complex,
            and its co-factor archease mediate XBP1 mRNA splicing both in vitro
            and in vivo.
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Popow,J., Jurkin,J., Schleiffer,A. and Martinez,J.
  TITLE     Analysis of orthologous groups reveals archease and DDX1 as tRNA
            splicing factors
  JOURNAL   Nature 511 (7507), 104-107 (2014)
   PUBMED   24870230
  REMARK    GeneRIF: archease (also called ZBTB8OS), a protein of unknown
            function, is required for full activity of the human tRNA ligase
            complex and, in cooperation with DDX1, facilitates the formation of
            an RTCB-guanylate intermediate central to mammalian RNA ligation
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Popow,J., Englert,M., Weitzer,S., Schleiffer,A., Mierzwa,B.,
            Mechtler,K., Trowitzsch,S., Will,C.L., Luhrmann,R., Soll,D. and
            Martinez,J.
  TITLE     HSPC117 is the essential subunit of a human tRNA splicing ligase
            complex
  JOURNAL   Science 331 (6018), 760-764 (2011)
   PUBMED   21311021
REFERENCE   7  (residues 1 to 110)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 110)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2 and AL033529.25.
            
            On Apr 28, 2015 this sequence version replaced XP_011539641.1.
            
            Transcript Variant: This variant (5) has multiple differences in
            the coding region compared to variant 1. This variant represents
            translation initiation at a downstream start codon compared to
            variant 1; the 5'-most initiation codon, as used in variant 1, is
            associated with a truncated ORF that would render the transcript a
            candidate for nonsense-mediated decay (NMD). Leaky scanning may
            allow translation initiation at the downstream start codon to
            encode an isoform (5) that has a shorter N-terminus, compared to
            isoform 1. Variants 5, 6, 7, and 8 all encode the same isoform (5).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.499751.1, DT220608.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..110
                     /product="protein archease isoform 5"
                     /note="protein archease; archease-like protein; archease
                     (ARCH); zinc finger and BTB domain-containing opposite
                     strand protein 8"
                     /calculated_mol_wt=12646
     Region          1..110
                     /region_name="Archease"
                     /note="Archease protein family (MTH1598/TM1083);
                     pfam01951"
                     /db_xref="CDD:426527"
     CDS             1..110
                     /gene="ZBTB8OS"
                     /gene_synonym="ARCH; ARCH2"
                     /coded_by="NM_001308138.2:619..951"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS76134.1"
                     /db_xref="GeneID:339487"
                     /db_xref="HGNC:HGNC:24094"
                     /db_xref="MIM:615891"
ORIGIN      
        1 mamfgymtdt gtveplqtve vetqgddlqs llfhfldewl ykfsadeffi prevkvlsid
       61 qrnfklrsig wgeefslskh pqgtevkait ysamqvynee npevfviidi
//
LOCUS       NP_065883               1237 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 687 [Homo sapiens].
ACCESSION   NP_065883
VERSION     NP_065883.1
DBSOURCE    REFSEQ: accession NM_020832.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1237)
  AUTHORS   Li,J., Li,S., Xing,X., Liu,N., Lai,S., Liao,D. and Li,J.
  TITLE     FTO-mediated ZNF687 accelerates tumor growth, metastasis, and
            angiogenesis in colorectal cancer through the Wnt/beta-catenin
            pathway
  JOURNAL   Biotechnol Appl Biochem 71 (2), 245-255 (2024)
   PUBMED   37983718
  REMARK    GeneRIF: FTO-mediated ZNF687 accelerates tumor growth, metastasis,
            and angiogenesis in colorectal cancer through the Wnt/beta-catenin
            pathway.
REFERENCE   2  (residues 1 to 1237)
  AUTHORS   Li,M., Liu,Z., Hou,Z., Wang,X., Shi,H., Li,Y., Xiao,X., Tang,Z.,
            Yang,J., Luo,Y., Zhang,M. and Chen,M.
  TITLE     Oncogenic zinc finger protein ZNF687 accelerates lung
            adenocarcinoma cell proliferation and tumor progression by
            activating the PI3K/AKT signaling pathway
  JOURNAL   Thorac Cancer 14 (14), 1223-1238 (2023)
   PUBMED   36944484
  REMARK    GeneRIF: Oncogenic zinc finger protein ZNF687 accelerates lung
            adenocarcinoma cell proliferation and tumor progression by
            activating the PI3K/AKT signaling pathway.
REFERENCE   3  (residues 1 to 1237)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   4  (residues 1 to 1237)
  AUTHORS   Scotto di Carlo,F., Pazzaglia,L., Mumm,S., Benassi,M.S., De
            Chiara,A., Franchi,A., Parafioriti,A., Righi,A., Esposito,T.,
            Whyte,M.P. and Gianfrancesco,F.
  TITLE     ZNF687 Mutations in an Extended Cohort of Neoplastic
            Transformations in Paget's Disease of Bone: Implications for
            Clinical Pathology
  JOURNAL   J Bone Miner Res 35 (10), 1974-1980 (2020)
   PUBMED   32106343
  REMARK    GeneRIF: ZNF687 Mutations in an Extended Cohort of Neoplastic
            Transformations in Paget's Disease of Bone: Implications for
            Clinical Pathology.
REFERENCE   5  (residues 1 to 1237)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1237)
  AUTHORS   Divisato,G., Formicola,D., Esposito,T., Merlotti,D., Pazzaglia,L.,
            Del Fattore,A., Siris,E., Orcel,P., Brown,J.P., Nuti,R.,
            Strazzullo,P., Benassi,M.S., Cancela,M.L., Michou,L., Rendina,D.,
            Gennari,L. and Gianfrancesco,F.
  TITLE     ZNF687 Mutations in Severe Paget Disease of Bone Associated with
            Giant Cell Tumor
  JOURNAL   Am J Hum Genet 98 (2), 275-286 (2016)
   PUBMED   26849110
  REMARK    GeneRIF: ZNF687 Expression increased in paget disease of bone
            Affected Individuals.
REFERENCE   7  (residues 1 to 1237)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   8  (residues 1 to 1237)
  AUTHORS   Denoeud,F., Kapranov,P., Ucla,C., Frankish,A., Castelo,R.,
            Drenkow,J., Lagarde,J., Alioto,T., Manzano,C., Chrast,J., Dike,S.,
            Wyss,C., Henrichsen,C.N., Holroyd,N., Dickson,M.C., Taylor,R.,
            Hance,Z., Foissac,S., Myers,R.M., Rogers,J., Hubbard,T., Harrow,J.,
            Guigo,R., Gingeras,T.R., Antonarakis,S.E. and Reymond,A.
  TITLE     Prominent use of distal 5' transcription start sites and discovery
            of a large number of additional exons in ENCODE regions
  JOURNAL   Genome Res 17 (6), 746-759 (2007)
   PUBMED   17567994
REFERENCE   9  (residues 1 to 1237)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 1237)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391069.11, AB037862.1,
            BC032463.1 and CR749307.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes C2H2 zinc finger protein. The encoded
            protein may play a role in bone differentiation and development.
            Mutations in this gene are the cause of Paget disease of bone-6.
            Alternate splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All three variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032463.1, SRR7346977.2102064.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336715.11/ ENSP00000336620.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..1237
                     /product="zinc finger protein 687"
                     /calculated_mol_wt=129398
     Region          1..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Region          <54..294
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          96..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2D7; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Region          707..727
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(712,714,716,718..719,722..723,726,740,742,745..746,
                     749..750,756,771,773,775,777..778,781..782,785)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          735..757
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          766..785
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          794..815
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          795..877
                     /region_name="zf-C2H2_8"
                     /note="C2H2-type zinc ribbon; pfam15909"
                     /db_xref="CDD:464935"
     Region          829..850
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          860..881
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          880..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Region          965..985
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(970,972,974,976..977,980..981,984,1000,1002,
                     1006..1007,1010..1011,1014,1032,1035,1037,1039..1040,
                     1043..1044)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          995..1016
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1025..1045
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1051..1121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1057
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1060
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2D7; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1082
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1083
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1101
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2D7; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Region          1133..1159
                     /region_name="zf-C2H2_11"
                     /note="zinc-finger C2H2-type; pfam16622"
                     /db_xref="CDD:465205"
     Region          1159..1195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2D7; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     Site            1211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N1G0.1)"
     CDS             1..1237
                     /gene="ZNF687"
                     /gene_synonym="PDB6"
                     /coded_by="NM_020832.3:115..3828"
                     /db_xref="CCDS:CCDS992.1"
                     /db_xref="GeneID:57592"
                     /db_xref="HGNC:HGNC:29277"
                     /db_xref="MIM:610568"
ORIGIN      
        1 mgdmktpdfd dllaafdipd idaneaihsg peenegpggp gkpepgvgse sedtaaasag
       61 dgpgvpaqas dhglpppdis vvsvivkntv cpeqsealag gsagdgaqaa gvtkegpvgp
      121 hrmqngfgsp epslpgtphs pappsggtwk ekgmegktpl dlfahfgpep gdhsdplpps
      181 apsptregal tpppfpssfe laqengpgmq ppvsspplga lkqescsphh pqvlaqqgsg
      241 sspkatdipa saspppvagv pffkqspghq splaspkvpv cqplkeeddd egpvdksspg
      301 spqspssgae aadedsndsp assssrplkv riktiktscg nitrtvtqvp sdpdppapla
      361 egaflaeasl lklspatpts egpkvvsvql gdgtrlkgtv lpvatiqnas tamlmaasva
      421 rkavvlpggt atspkmiakn vlglvpqalp kadgraglgt ggqkvngasv vmvqpsktat
      481 gpstgggtvi srtqsslvea fnkilnsknl lpayrpnlsp paeaglalpp tgyrclecgd
      541 afslekslar hydrrsmrie vtcnhcarrl vffnkcslll harehkdkgl vmqcshlvmr
      601 pvaldqmvgq pditpllpva vppvsgplal palgkgegai tssaittvaa eapvlplste
      661 ppaapatsay tcfrclecke qcrdkagmaa hfqqlgppap gatsnvcptc pmmlpnrcsf
      721 sahqrmhknr pphvcpecgg nflqanfqth lreaclhvsr rvgyrcpscs vvfggvnsik
      781 shiqtshcev fhkcpicpma fksgpsahah lysqhpsfqt qqakliykca mcdtvfthkp
      841 llsshfdqhl lpqrvsvfkc pscpllfaqk rtmlehlknt hqsgrleeta gkgaggallt
      901 pktepeelav sqggaapate essssseeee vpsspepprp akrprrelgs kglkgggggp
      961 ggwtcglchs wfperdeyva hmkkehgksv kkfpcrlcer sfcsapslrr hvrvnhegik
     1021 rvypcrycte gkrtfssrli lekhvqvrhg lqlgaqspgr gttlargssa raqgpgrkrr
     1081 qssdscseep dsttppaksp rggpgsgghg plryrsssst eqslmmglrv edgaqqcldc
     1141 glcfaspgsl srhrfishkk rrgvgkasal glgdgeeeap psrsdpdggd splpasggpl
     1201 tckvcgkscd splnlkthfr thgmafirar qgavgdn
//
LOCUS       NP_006806                201 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane emp24 domain-containing protein 2 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_006806
VERSION     NP_006806.1
DBSOURCE    REFSEQ: accession NM_006815.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Sun,C., Zhang,Y., Wang,Z., Chen,J., Zhang,J. and Gu,Y.
  TITLE     TMED2 promotes glioma tumorigenesis by being involved in EGFR
            recycling transport
  JOURNAL   Int J Biol Macromol 262 (Pt 2), 130055 (2024)
   PUBMED   38354922
  REMARK    GeneRIF: TMED2 promotes glioma tumorigenesis by being involved in
            EGFR recycling transport.
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Liang,C., Zhang,H.Y., Wang,Y.Q., Yang,L.A., Du,Y.S., Luo,Y.,
            Zhang,T.C. and Xu,Y.
  TITLE     TMED2 Induces Cisplatin Resistance in Breast Cancer via Targeting
            the KEAP1-Nrf2 Pathway
  JOURNAL   Curr Med Sci 43 (5), 1023-1032 (2023)
   PUBMED   37615927
  REMARK    GeneRIF: TMED2 Induces Cisplatin Resistance in Breast Cancer via
            Targeting the KEAP1-Nrf2 Pathway.
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Xu,H., Lin,X., Li,Z., He,X., Li,Y., Qiu,L., Lu,L., Liu,B., Zhan,M.
            and He,K.
  TITLE     VIRMA facilitates intrahepatic cholangiocarcinoma progression
            through epigenetic augmentation of TMED2 and PARD3B mRNA
            stabilization
  JOURNAL   J Gastroenterol 58 (9), 925-944 (2023)
   PUBMED   37391589
  REMARK    GeneRIF: VIRMA facilitates intrahepatic cholangiocarcinoma
            progression through epigenetic augmentation of TMED2 and PARD3B
            mRNA stabilization.
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Feng,L., Cheng,P., Feng,Z. and Zhang,X.
  TITLE     Transmembrane p24 trafficking protein 2 regulates inflammation
            through the TLR4/NF-kappaB signaling pathway in lung adenocarcinoma
  JOURNAL   World J Surg Oncol 20 (1), 32 (2022)
   PUBMED   35135563
  REMARK    GeneRIF: Transmembrane p24 trafficking protein 2 regulates
            inflammation through the TLR4/NF-kappaB signaling pathway in lung
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Goldberg,J.
  TITLE     Decoding of sorting signals by coatomer through a GTPase switch in
            the COPI coat complex
  JOURNAL   Cell 100 (6), 671-679 (2000)
   PUBMED   10761932
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Fullekrug,J., Suganuma,T., Tang,B.L., Hong,W., Storrie,B. and
            Nilsson,T.
  TITLE     Localization and recycling of gp27 (hp24gamma3): complex formation
            with other p24 family members
  JOURNAL   Mol Biol Cell 10 (6), 1939-1955 (1999)
   PUBMED   10359607
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Gommel,D., Orci,L., Emig,E.M., Hannah,M.J., Ravazzola,M.,
            Nickel,W., Helms,J.B., Wieland,F.T. and Sohn,K.
  TITLE     p24 and p23, the major transmembrane proteins of COPI-coated
            transport vesicles, form hetero-oligomeric complexes and cycle
            between the organelles of the early secretory pathway
  JOURNAL   FEBS Lett 447 (2-3), 179-185 (1999)
   PUBMED   10214941
REFERENCE   9  (residues 1 to 201)
  AUTHORS   Fiedler,K., Veit,M., Stamnes,M.A. and Rothman,J.E.
  TITLE     Bimodal interaction of coatomer with the p24 family of putative
            cargo receptors
  JOURNAL   Science 273 (5280), 1396-1399 (1996)
   PUBMED   8703076
REFERENCE   10 (residues 1 to 201)
  AUTHORS   Blum,R., Feick,P., Puype,M., Vandekerckhove,J., Klengel,R.,
            Nastainczyk,W. and Schulz,I.
  TITLE     Tmp21 and p24A, two type I proteins enriched in pancreatic
            microsomal membranes, are members of a protein family involved in
            vesicular trafficking
  JOURNAL   J Biol Chem 271 (29), 17183-17189 (1996)
   PUBMED   8663407
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC055713.29, BI086507.1 and BC025957.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.972817.1,
                                           SRR1660805.248900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262225.8/ ENSP00000262225.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..201
                     /product="transmembrane emp24 domain-containing protein 2
                     isoform 1 precursor"
                     /note="coated vesicle membrane protein; membrane protein
                     p24A; p24 family protein beta-1; transmembrane emp24
                     domain trafficking protein 2"
                     /calculated_mol_wt=20781
     Region          1..181
                     /region_name="Interaction with F2RL1.
                     /evidence=ECO:0000269|PubMed:17693410"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1999
     Region          20..196
                     /region_name="EMP24_GP25L"
                     /note="emp24/gp25L/p24 family/GOLD; pfam01105"
                     /db_xref="CDD:426051"
     mat_peptide     21..201
                     /product="Transmembrane emp24 domain-containing protein 2.
                     /id=PRO_0000010381"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
                     /calculated_mol_wt=20781
     Region          118..157
                     /region_name="Required for TMED10 and TMED2 cis-Golgi
                     network localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
     Site            169..189
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
     Region          194..201
                     /region_name="COPI vesicle coat-binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
     Region          194..195
                     /region_name="COPII vesicle coat-binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
     CDS             1..201
                     /gene="TMED2"
                     /gene_synonym="p24; P24A; p24b1; p24beta1; RNP24"
                     /coded_by="NM_006815.4:86..691"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9250.1"
                     /db_xref="GeneID:10959"
                     /db_xref="HGNC:HGNC:16996"
                     /db_xref="MIM:619642"
ORIGIN      
        1 mvtlaellvl laallatvsg yfvsidahae ecffervtsg tkmglifeva eggfldidve
       61 itgpdnkgiy kgdressgky tfaahmdgty kfcfsnrmst mtpkivmfti digeapkgqd
      121 meteahqnkl eeminelava mtavkheqey mevrerihra indntnsrvv lwsffealvl
      181 vamtlgqiyy lkrffevrrv v
//
LOCUS       NP_001357426            1382 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-binding cassette sub-family C member 11 isoform a [Homo
            sapiens].
ACCESSION   NP_001357426 XP_016879284
VERSION     NP_001357426.1
DBSOURCE    REFSEQ: accession NM_001370497.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1382)
  AUTHORS   Toyoda,Y., Matsuo,H. and Takada,T.
  TITLE     Functional characterization of variants in human ABCC11, an
            axillary osmidrosis risk factor
  JOURNAL   Hum Cell 37 (4), 1070-1079 (2024)
   PUBMED   38750405
  REMARK    GeneRIF: Functional characterization of variants in human ABCC11,
            an axillary osmidrosis risk factor.
REFERENCE   2  (residues 1 to 1382)
  AUTHORS   Kutsuwada,Y., Yokota,K., Yoshida,K., Tsuda,H., Watanabe,K.,
            Matsumoto,A. and Iwamoto,S.
  TITLE     Association of HLA-DPB1, NLRP10, OVOL1, and ABCC11 with the
            axillary microbiome in a Japanese population
  JOURNAL   J Dermatol Sci 105 (2), 98-104 (2022)
   PUBMED   35078690
  REMARK    GeneRIF: Association of HLA-DPB1, NLRP10, OVOL1, and ABCC11 with
            the axillary microbiome in a Japanese population.
REFERENCE   3  (residues 1 to 1382)
  AUTHORS   Matsumoto,H., Sasai,H., Kawamoto,N., Katsuyama,M., Minamiyama,M.,
            Kuru,S., Fukao,T. and Ohnishi,H.
  CONSRTM   SMON research group members
  TITLE     Founder genetic variants of ABCC4 and ABCC11 in the Japanese
            population are not associated with the development of subacute
            myelo-optico-neuropathy (SMON)
  JOURNAL   Mol Genet Genomic Med 10 (1), e1845 (2022)
   PUBMED   34951141
  REMARK    GeneRIF: Founder genetic variants of ABCC4 and ABCC11 in the
            Japanese population are not associated with the development of
            subacute myelo-optico-neuropathy (SMON).
REFERENCE   4  (residues 1 to 1382)
  AUTHORS   Hara,S., Kusunoki,T., Nakagawa,H., Toyoda,Y., Nojiri,S., Kamiya,K.,
            Furukawa,M., Takata,Y., Okada,H., Anzai,T., Matsumoto,F. and
            Ikeda,K.
  TITLE     Association Between Earwax-Determinant Genotypes and Acquired
            Middle Ear Cholesteatoma in a Japanese Population
  JOURNAL   Otolaryngol Head Neck Surg 166 (1), 139-145 (2022)
   PUBMED   33722103
  REMARK    GeneRIF: Association Between Earwax-Determinant Genotypes and
            Acquired Middle Ear Cholesteatoma in a Japanese Population.
REFERENCE   5  (residues 1 to 1382)
  AUTHORS   Wang,Y., Li,J., Huang,J., Wu,C., Li,L. and Gong,P.
  TITLE     Mutation differences in circulating tumor DNAs from non-small cell
            lung cancer patients between Uygur and Han populations
  JOURNAL   Medicine (Baltimore) 100 (4), e24159 (2021)
   PUBMED   33530206
  REMARK    GeneRIF: Mutation differences in circulating tumor DNAs from
            non-small cell lung cancer patients between Uygur and Han
            populations.
REFERENCE   6  (residues 1 to 1382)
  AUTHORS   Lai,L. and Tan,T.M.
  TITLE     Role of glutathione in the multidrug resistance protein 4
            (MRP4/ABCC4)-mediated efflux of cAMP and resistance to purine
            analogues
  JOURNAL   Biochem J 361 (Pt 3), 497-503 (2002)
   PUBMED   11802779
REFERENCE   7  (residues 1 to 1382)
  AUTHORS   Yabuuchi,H., Shimizu,H., Takayanagi,S. and Ishikawa,T.
  TITLE     Multiple splicing variants of two new human ATP-binding cassette
            transporters, ABCC11 and ABCC12
  JOURNAL   Biochem Biophys Res Commun 288 (4), 933-939 (2001)
   PUBMED   11688999
  REMARK    GeneRIF: alternative splice variants and gene expression
REFERENCE   8  (residues 1 to 1382)
  AUTHORS   Bera,T.K., Lee,S., Salvatore,G., Lee,B. and Pastan,I.
  TITLE     MRP8, a new member of ABC transporter superfamily, identified by
            EST database mining and gene prediction program, is highly
            expressed in breast cancer
  JOURNAL   Mol Med 7 (8), 509-516 (2001)
   PUBMED   11591886
REFERENCE   9  (residues 1 to 1382)
  AUTHORS   Tammur,J., Prades,C., Arnould,I., Rzhetsky,A., Hutchinson,A.,
            Adachi,M., Schuetz,J.D., Swoboda,K.J., Ptacek,L.J., Rosier,M.,
            Dean,M. and Allikmets,R.
  TITLE     Two new genes from the human ATP-binding cassette transporter
            superfamily, ABCC11 and ABCC12, tandemly duplicated on chromosome
            16q12
  JOURNAL   Gene 273 (1), 89-96 (2001)
   PUBMED   11483364
REFERENCE   10 (residues 1 to 1382)
  AUTHORS   Dean,M., Rzhetsky,A. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Genome Res 11 (7), 1156-1166 (2001)
   PUBMED   11435397
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007600.6 and AC096996.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 9, 2019 this sequence version replaced XP_016879284.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This ABC
            full transporter is a member of the MRP subfamily which is involved
            in multi-drug resistance. The product of this gene participates in
            physiological processes involving bile acids, conjugated steroids,
            and cyclic nucleotides. In addition, a SNP in this gene is
            responsible for determination of human earwax type. This gene and
            family member ABCC12 are determined to be derived by duplication
            and are both localized to chromosome 16q12.1. Multiple
            alternatively spliced transcript variants have been described for
            this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF352582.1, SRR7346977.2318316.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356608.7/ ENSP00000349017.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.1"
     Protein         1..1382
                     /product="ATP-binding cassette sub-family C member 11
                     isoform a"
                     /EC_number="7.6.2.2"
                     /EC_number="7.6.2.3"
                     /note="multi-resistance protein 8; ATP-binding cassette
                     transporter MRP8; ATP-binding cassette protein C11;
                     ATP-binding cassette transporter sub-family C member 11;
                     ATP-binding cassette sub-family C member 11; multidrug
                     resistance-associated protein 8; ATP-binding cassette,
                     sub-family C (CFTR/MRP), member 11"
                     /calculated_mol_wt=154171
     Region          85..1371
                     /region_name="PLN03130"
                     /note="ABC transporter C family member; Provisional"
                     /db_xref="CDD:215595"
     Site            164..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            195..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            271..291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            297..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            418..438
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Region          504..523
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            807..827
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            838
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:19383836;
                     propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            844
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:19383836;
                     propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            864..884
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            931..951
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            952..972
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            1050..1070
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     Site            1075..1095
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J66.1)"
     CDS             1..1382
                     /gene="ABCC11"
                     /gene_synonym="EWWD; MRP8; WW"
                     /coded_by="NM_001370497.1:245..4393"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS10732.1"
                     /db_xref="GeneID:85320"
                     /db_xref="HGNC:HGNC:14639"
                     /db_xref="MIM:607040"
ORIGIN      
        1 mtrkrtywvp nssgglvnrg idigddmvsg liyktytlqd gpwsqqernp eapgraavpp
       61 wgkydaalrt mipfrpkprf papqpldnag lfsyltvswl tplmiqslrs rldentippl
      121 svhdasdknv qrlhrlweee vsrrgiekas vllvmlrfqr trlifdallg icfciasvlg
      181 piliipkile yseeqlgnvv hgvglcfalf lsecvkslsf ssswiinqrt airfraavss
      241 fafekliqfk svihitsgea isfftgdvny lfegvcygpl vlitcaslvi csissyfiig
      301 ytafiailcy llvfplavfm trmavkaqhh tsevsdqrir vtsevltcik likmytwekp
      361 fakiiedlrr kerkllekcg lvqsltsitl fiiptvatav wvlihtslkl kltasmafsm
      421 laslnllrls vffvpiavkg ltnsksavmr fkkfflqesp vfyvqtlqdp skalvfeeat
      481 lswqqtcpgi vngalelern ghasegmtrp rdalgpeeeg nslgpelhki nlvvskgmml
      541 gvcgntgsgk ssllsailee mhllegsvgv qgslayvpqq awivsgnire nilmggaydk
      601 arylqvlhcc slnrdlellp fgdmteiger glnlsggqkq rislaravys drqiyllddp
      661 lsavdahvgk hifeecikkt lrgktvvlvt hqlqylefcg qiillengki cengthselm
      721 qkkgkyaqli qkmhkeatsd mlqdtakiae kpkvesqala tsleeslngn avpehqltqe
      781 eemeegslsw rvyhhyiqaa ggymvsciif ffvvlivflt ifsfwwlsyw leqgsgtnss
      841 resngtmadl gniadnpqls fyqlvyglna lllicvgvcs sgiftkvtrk astalhnklf
      901 nkvfrcpmsf fdtipigrll ncfagdleql dqllpifseq flvlslmvia vllivsvlsp
      961 yillmgaiim vicfiyymmf kkaigvfkrl enysrsplfs hilnslqgls sihvygkted
     1021 fisqfkrltd aqnnylllfl sstrwmalrl eimtnlvtla valfvafgis stpysfkvma
     1081 vnivlqlass fqatarigle teaqftaver ilqymkmcvs eaplhmegts cpqgwpqhge
     1141 iifqdyhmky rdntptvlhg inltirghev vgivgrtgsg ksslgmalfr lvepmagril
     1201 idgvdicsig ledlrsklsv ipqdpvllsg tirfnldpfd rhtdqqiwda lertfltkai
     1261 skfpkklhtd vvenggnfsv gerqllciar avlrnskiil ideatasidm etdtliqrti
     1321 reafqgctvl viahrvttvl ncdhilvmgn gkvvefdrpe vlrkkpgslf aalmatatss
     1381 lr
//
LOCUS       NP_001347558             357 aa            linear   ROD 27-APR-2025
DEFINITION  hsp70-binding protein 1 [Mus musculus].
ACCESSION   NP_001347558 XP_006540351
VERSION     NP_001347558.1
DBSOURCE    REFSEQ: accession NM_001360629.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Zhao,T., Hong,Y., Yin,P., Li,S. and Li,X.J.
  TITLE     Differential HspBP1 expression accounts for the greater
            vulnerability of neurons than astrocytes to misfolded proteins
  JOURNAL   Proc Natl Acad Sci U S A 114 (37), E7803-E7811 (2017)
   PUBMED   28847953
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Rogon,C., Ulbricht,A., Hesse,M., Alberti,S., Vijayaraj,P., Best,D.,
            Adams,I.R., Magin,T.M., Fleischmann,B.K. and Hohfeld,J.
  TITLE     HSP70-binding protein HSPBP1 regulates chaperone expression at a
            posttranslational level and is essential for spermatogenesis
  JOURNAL   Mol Biol Cell 25 (15), 2260-2271 (2014)
   PUBMED   24899640
  REMARK    GeneRIF: Male HSPBP1knockout mice are sterile because of impaired
            meiosis and massive apoptosis of spermatocytes.
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Miller,J.A., Nathanson,J., Franjic,D., Shim,S., Dalley,R.A.,
            Shapouri,S., Smith,K.A., Sunkin,S.M., Bernard,A., Bennett,J.L.,
            Lee,C.K., Hawrylycz,M.J., Jones,A.R., Amaral,D.G., Sestan,N.,
            Gage,F.H. and Lein,E.S.
  TITLE     Conserved molecular signatures of neurogenesis in the hippocampal
            subgranular zone of rodents and primates
  JOURNAL   Development 140 (22), 4633-4644 (2013)
   PUBMED   24154525
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Kettern,N., Rogon,C., Limmer,A., Schild,H. and Hohfeld,J.
  TITLE     The Hsc/Hsp70 co-chaperone network controls antigen aggregation and
            presentation during maturation of professional antigen presenting
            cells
  JOURNAL   PLoS One 6 (1), e16398 (2011)
   PUBMED   21283720
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Zhang,C., Xu,Z., He,X.R., Michael,L.H. and Patterson,C.
  TITLE     CHIP, a cochaperone/ubiquitin ligase that regulates protein quality
            control, is required for maximal cardioprotection after myocardial
            infarction in mice
  JOURNAL   Am J Physiol Heart Circ Physiol 288 (6), H2836-H2842 (2005)
   PUBMED   15665051
  REMARK    GeneRIF: Provides a critical cardioprotective effect in the setting
            of ischemia-reperfusion injury due in part to increased apoptosis
            in cardiac cells.
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC161197.9.
            
            On Feb 8, 2018 this sequence version replaced XP_006540351.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK088469.1, SRR7652917.751946.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164141 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 2.69 cM"
     Protein         1..357
                     /product="hsp70-binding protein 1"
                     /note="hsp70-interacting protein 1; heat shock
                     protein-binding protein 1; SPA) binding protein,
                     cytoplasmic cochaperone 1"
                     /calculated_mol_wt=39036
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P31.1)"
     Region          43..137
                     /region_name="Fes1"
                     /note="Nucleotide exchange factor Fes1; pfam08609"
                     /db_xref="CDD:462534"
     Site            order(119,123,127,161,165,169,203,208,212)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          130..172
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P31.1)"
     Region          135..172
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          175..215
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P31.1)"
     Region          178..213
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          218..257
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P31.1)"
     Region          231..255
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          260..299
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P31.1)"
     Region          263..299
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99P31.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NZL4; propagated from
                     UniProtKB/Swiss-Prot (Q99P31.1)"
     CDS             1..357
                     /gene="Hspbp1"
                     /gene_synonym="1500019G21Rik"
                     /coded_by="NM_001360629.1:180..1253"
                     /db_xref="CCDS:CCDS20740.1"
                     /db_xref="GeneID:66245"
                     /db_xref="MGI:MGI:1913495"
ORIGIN      
        1 madkgsggsr lplalppasq gcssggsgss aggsgnprpp rnlqgllqma itagsqepdp
       61 ppepmseerr qwlqeamsaa frgqreeveq mknclrvlsq atpamageae latdqqereg
      121 alelladlce nmdnaadfcq lsgmhllvgr yleagaaglr wraaqligtc sqnvaaiqeq
      181 vlglgalrkl lrlldrdscd tvrvkalfai sclvreqeag llqflrldgf svlmramqqq
      241 vqklkvksaf llqnllvghp ehkgtlcsmg mvqqlvalvr tehspfhehv lgalcslvtd
      301 fpqgvrecre pelgleellr hrcqllqqre eyqeelefce kllqtcfssp tddsmdr
//
LOCUS       NP_060328                301 aa            linear   PRI 27-APR-2025
DEFINITION  TIMELESS-interacting protein isoform 1 [Homo sapiens].
ACCESSION   NP_060328
VERSION     NP_060328.3
DBSOURCE    REFSEQ: accession NM_017858.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Arai,H., Xiao,Y., Millstein,J., Wang,J., Battaglin,F.,
            Kawanishi,N., Jayachandran,P., Soni,S., Zhang,W., Mancao,C.,
            Salhia,B., Mumenthaler,S.M., Parikh,A.R. and Lenz,H.J.
  TITLE     Germline polymorphisms in genes maintaining the replication fork
            predict the efficacy of oxaliplatin and irinotecan in patients with
            metastatic colorectal cancer
  JOURNAL   Br J Cancer 126 (1), 72-78 (2022)
   PUBMED   34689170
  REMARK    GeneRIF: Germline polymorphisms in genes maintaining the
            replication fork predict the efficacy of oxaliplatin and irinotecan
            in patients with metastatic colorectal cancer.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Lerner,L.K., Holzer,S., Kilkenny,M.L., Svikovic,S., Murat,P.,
            Schiavone,D., Eldridge,C.B., Bittleston,A., Maman,J.D., Branzei,D.,
            Stott,K., Pellegrini,L. and Sale,J.E.
  TITLE     Timeless couples G-quadruplex detection with processing by DDX11
            helicase during DNA replication
  JOURNAL   EMBO J 39 (18), e104185 (2020)
   PUBMED   32705708
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Gotter,A.L., Suppa,C. and Emanuel,B.S.
  TITLE     Mammalian TIMELESS and Tipin are evolutionarily conserved
            replication fork-associated factors
  JOURNAL   J Mol Biol 366 (1), 36-52 (2007)
   PUBMED   17141802
  REMARK    GeneRIF: TIM and Tipin are functional orthologs of their
            replisome-associated yeast counterparts capable of coordinating
            replication with genotoxic stress responses, and distinguishes
            mammalian TIM from the circadian-specific paralogs.
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Yoshizawa-Sugata,N. and Masai,H.
  TITLE     Human Tim/Timeless-interacting protein, Tipin, is required for
            efficient progression of S phase and DNA replication checkpoint
  JOURNAL   J Biol Chem 282 (4), 2729-2740 (2007)
   PUBMED   17102137
  REMARK    GeneRIF: Tipin is a checkpoint mediator that cooperates with Tim
            and may regulate the nuclear relocation of Claspin in response to
            replication checkpoint
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Chou,D.M. and Elledge,S.J.
  TITLE     Tipin and Timeless form a mutually protective complex required for
            genotoxic stress resistance and checkpoint function
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18143-18147 (2006)
   PUBMED   17116885
  REMARK    GeneRIF: observation explains the similar checkpoint phenotypes
            observed in both Tipin- and Timeless-depleted cells
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Gotter,A.L.
  TITLE     Tipin, a novel timeless-interacting protein, is developmentally
            co-expressed with timeless and disrupts its self-association
  JOURNAL   J Mol Biol 331 (1), 167-176 (2003)
   PUBMED   12875843
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            On Nov 23, 2018 this sequence version replaced NP_060328.2.
            
            Summary: The protein encoded by this gene is part of the replisome
            complex, a group of proteins that support DNA replication. It binds
            TIM, which is involved in circadian rhythm regulation, and aids in
            protecting cells against DNA damage and stress. Two pseudogenes and
            two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, Jul 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR12921934.2502533.1,
                                           SRR14038197.56315.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261881.9/ ENSP00000261881.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..301
                     /product="TIMELESS-interacting protein isoform 1"
                     /note="timeless-interacting protein; CSM3 homolog"
                     /calculated_mol_wt=34424
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Region          66..148
                     /region_name="Swi3"
                     /note="Replication Fork Protection Component Swi3;
                     pfam07962"
                     /db_xref="CDD:462324"
     Region          67..143
                     /region_name="Interaction with TIMELESS.
                     /evidence=ECO:0000269|PubMed:23359676"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Region          240..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     CDS             1..301
                     /gene="TIPIN"
                     /coded_by="NM_017858.3:56..961"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10215.1"
                     /db_xref="GeneID:54962"
                     /db_xref="HGNC:HGNC:30750"
                     /db_xref="MIM:610716"
ORIGIN      
        1 mlepqengvi dlpdyehved etfppfpppa sperqdgegt epdeesgnga pvrvppkrtv
       61 krnipkldaq rliserglpa lrhvfdkakf kgkgheaedl kmlirhmehw ahrlfpklqf
      121 edfidrveyl gskkevqtcl krirldlpil hedfvsnnde vaennehdvt steldpfltn
      181 lsesemfase lsrslteeqq qriernkqla lerrqaklls nsqtlgndml mntprahtve
      241 evntdedqke esnglnedil dnpcndaian tlneeetlld qsfknvqqql datsrnitea
      301 r
//
LOCUS       NP_001934               1118 aa            linear   PRI 27-APR-2025
DEFINITION  desmoglein-2 preproprotein [Homo sapiens].
ACCESSION   NP_001934
VERSION     NP_001934.2
DBSOURCE    REFSEQ: accession NM_001943.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Zhang,G., Chen,Z., Wang,Y., Huang,A., Nie,F., Gao,L., Wang,Y. and
            Ren,F.
  TITLE     Up-regulated DSG2 promotes tumor growth and reduces immune
            infiltration in cervical cancer
  JOURNAL   Pathol Res Pract 262, 155554 (2024)
   PUBMED   39226803
  REMARK    GeneRIF: Up-regulated DSG2 promotes tumor growth and reduces immune
            infiltration in cervical cancer.
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Zhang,B., Wu,Y., Zhou,C., Xie,J., Zhang,Y., Yang,X., Xiao,J.,
            Wang,D.W., Shan,C., Zhou,X., Xiang,Y. and Yang,B.
  TITLE     Hyperactivation of ATF4/TGF-beta1 signaling contributes to the
            progressive cardiac fibrosis in Arrhythmogenic cardiomyopathy
            caused by DSG2 Variant
  JOURNAL   BMC Med 22 (1), 361 (2024)
   PUBMED   39227800
  REMARK    GeneRIF: Hyperactivation of ATF4/TGF-beta1 signaling contributes to
            the progressive cardiac fibrosis in Arrhythmogenic cardiomyopathy
            caused by DSG2 Variant.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Han,J.Y., Che,N., Mo,J., Zhang,D.F., Liang,X.H., Dong,X.Y.,
            Zhao,X.L. and Sun,B.C.
  TITLE     Desmoglein 2 and desmocollin 2 depletions promote malignancy
            through distinct mechanisms in triple-negative and luminal breast
            cancer
  JOURNAL   BMC Cancer 24 (1), 532 (2024)
   PUBMED   38671389
  REMARK    GeneRIF: Desmoglein 2 and desmocollin 2 depletions promote
            malignancy through distinct mechanisms in triple-negative and
            luminal breast cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1118)
  AUTHORS   Amagai,M. and Stanley,J.R.
  TITLE     Desmoglein as a target in skin disease and beyond
  JOURNAL   J Invest Dermatol 132 (3 Pt 2), 776-784 (2012)
   PUBMED   22189787
  REMARK    GeneRIF: Desmoglein 2, expressed earliest among the four isoforms
            in development, was found to be mutated in arrythmogenic right
            ventricular cardiomyopathy and is a receptor for a subset of
            adenoviruses that cause respiratory and urinary tract infections.
            Review article
REFERENCE   5  (residues 1 to 1118)
  AUTHORS   Simrak,D., Cowley,C.M., Buxton,R.S. and Arnemann,J.
  TITLE     Tandem arrangement of the closely linked desmoglein genes on human
            chromosome 18
  JOURNAL   Genomics 25 (2), 591-594 (1995)
   PUBMED   7790000
REFERENCE   6  (residues 1 to 1118)
  AUTHORS   Schafer,S., Koch,P.J. and Franke,W.W.
  TITLE     Identification of the ubiquitous human desmoglein, Dsg2, and the
            expression catalogue of the desmoglein subfamily of desmosomal
            cadherins
  JOURNAL   Exp Cell Res 211 (2), 391-399 (1994)
   PUBMED   8143788
REFERENCE   7  (residues 1 to 1118)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 1118)
  AUTHORS   McNally,E., MacLeod,H. and Dellefave-Castillo,L.
  TITLE     Arrhythmogenic Right Ventricular Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301310
REFERENCE   9  (residues 1 to 1118)
  AUTHORS   Arnemann,J., Spurr,N.K., Magee,A.I. and Buxton,R.S.
  TITLE     The human gene (DSG2) coding for HDGC, a second member of the
            desmoglein subfamily of the desmosomal cadherins, is, like DSG1
            coding for desmoglein DGI, assigned to chromosome 18
  JOURNAL   Genomics 13 (2), 484-486 (1992)
   PUBMED   1612610
REFERENCE   10 (residues 1 to 1118)
  AUTHORS   Koch,P.J., Goldschmidt,M.D., Walsh,M.J., Zimbelmann,R. and
            Franke,W.W.
  TITLE     Complete amino acid sequence of the epidermal desmoglein precursor
            polypeptide and identification of a second type of desmoglein gene
  JOURNAL   Eur J Cell Biol 55 (2), 200-208 (1991)
   PUBMED   1935985
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY268349.1, DC417739.1,
            BC099657.3, CN395083.1, BC022413.1, DR158777.1, BC014581.1 and
            BQ023247.1.
            
            On Oct 24, 2006 this sequence version replaced NP_001934.1.
            
            Summary: This gene encodes a member of the desmoglein family and
            cadherin cell adhesion molecule superfamily of proteins.
            Desmogleins are calcium-binding transmembrane glycoprotein
            components of desmosomes, cell-cell junctions between epithelial,
            myocardial, and other cell types. The encoded preproprotein is
            proteolytically processed to generate the mature glycoprotein. This
            gene is present in a gene cluster with other desmoglein gene family
            members on chromosome 18. Mutations in this gene have been
            associated with arrhythmogenic right ventricular dysplasia,
            familial, 10. [provided by RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK308408.1, Z26317.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261590.13/ ENSP00000261590.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..1118
                     /product="desmoglein-2 preproprotein"
                     /note="cadherin family member 5"
                     /calculated_mol_wt=119890
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2423
     mat_peptide     50..1118
                     /product="Desmoglein-2. /id=PRO_0000003846"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14126.2)"
                     /calculated_mol_wt=116752
     Region          62..155
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(62..63,118,120,151,153..154)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            112
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Region          163..268
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(170..171,228,230,264,266..267)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            182
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973;
                     propagated from UniProtKB/Swiss-Prot (Q14126.2)"
     Region          281..377
                     /region_name="CA_like"
                     /note="Cadherin repeat-like domain; cl46864"
                     /db_xref="CDD:481204"
     Site            309
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Region          392..495
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(399..400,454,456,491,493..494)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            462
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Site            514
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Site            610..634
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14126.2)"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Site            703
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Site            723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Site            804
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Site            806
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Site            815
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Region          881..912
                     /region_name="Desmoglein repeat 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14126.2)"
     Region          913..942
                     /region_name="Desmoglein repeat 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14126.2)"
     Site            922
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     Region          943..968
                     /region_name="Desmoglein repeat 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14126.2)"
     Region          969..992
                     /region_name="Desmoglein repeat 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14126.2)"
     Region          993..1021
                     /region_name="Desmoglein repeat 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14126.2)"
     Region          1022..1051
                     /region_name="Desmoglein repeat 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14126.2)"
     Region          1068..1118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14126.2)"
     Site            1118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14126.2)"
     CDS             1..1118
                     /gene="DSG2"
                     /gene_synonym="CDHF5; HDGC"
                     /coded_by="NM_001943.5:76..3432"
                     /db_xref="CCDS:CCDS42423.1"
                     /db_xref="GeneID:1829"
                     /db_xref="HGNC:HGNC:3049"
                     /db_xref="MIM:125671"
ORIGIN      
        1 marspgraya lllllicfnv gsglhlqvls trnenkllpk hphlvrqkra witapvalre
       61 gedlskknpi akihsdlaee rglkitykyt gkgiteppfg ifvfnkdtge lnvtsildre
      121 etpfflltgy aldargnnve kplelrikvl dindnepvft qdvfvgsvee lsaahtlvmk
      181 inatdadepn tlnskisyri vslepayppv fylnkdtgei yttsvtldre ehssytltve
      241 ardgngevtd kpvkqaqvqi rildvndnip vvenkvlegm veenqvnvev trikvfdade
      301 igsdnwlanf tfasgneggy fhietdaqtn egivtlikev dyeemknldf svivankaaf
      361 hksirskykp tpipikvkvk nvkegihfks svisiyvses mdrsskgqii gnfqafdedt
      421 glpaharyvk ledrdnwisv dsvtseikla klpdfesryv qngtytvkiv aisedyprkt
      481 itgtvlinve dindncptli epvqtichda eyvnvtaedl dghpnsgpfs fsvidkppgm
      541 aekwkiarqe stsvllqqse kklgrseiqf lisdnqgfsc pekqvltltv ceclhgsgcr
      601 eaqhdsyvgl gpaaialmil aflllllvpl lllmchcgkg akgftpipgt iemlhpwnne
      661 gappedkvvp sflpvdqggs lvgrngvggm akeatmkgss sasivkgqhe msemdgrwee
      721 hrsllsgrat qftgatgaim ttettktara tgasrdmaga qaaavalnee flrnyftdka
      781 asyteedenh takdcllvys qeeteslnas igccsfiege lddrflddlg lkfktlaevc
      841 lgqkidinke ieqrqkpate tsmntashsl ceqtmvnsen tyssgssfpv pkslqeanae
      901 kvtqeivter svssrqaqkv atplpdpmas rnviatetsy vtgstmpptt vilgpsqpqs
      961 livtervyap astlvdqpya negtvvvter viqphgggsn plegtqhlqd vpyvmvrere
     1021 sflapssgvq ptlampniav gqnvtvterv lapastlqss yqiptensmt arnttvsgag
     1081 vpgplpdfgl eesghsnsti ttsstrvtkh stvqhsys
//
LOCUS       NP_115695                188 aa            linear   PRI 27-APR-2025
DEFINITION  protease-associated domain-containing protein 1 precursor [Homo
            sapiens].
ACCESSION   NP_115695
VERSION     NP_115695.1
DBSOURCE    REFSEQ: accession NM_032319.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Zhou,Y.B., Liu,F., Zhu,Z.D., Zhu,H., Zhang,X., Wang,Z.Q., Liu,J.H.
            and Han,Z.G.
  TITLE     N-glycosylation is required for efficient secretion of a novel
            human secreted glycoprotein, hPAP21
  JOURNAL   FEBS Lett 576 (3), 401-407 (2004)
   PUBMED   15498570
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM556790.1 and BC005069.1.
            
            Transcript Variant: This variant (1) represents the longer,
            protein-coding variant.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.50309.1,
                                           SRR3476690.947677.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258083.3/ ENSP00000258083.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.2"
     Protein         1..188
                     /product="protease-associated domain-containing protein 1
                     precursor"
                     /note="protease-associated domain-containing glycoprotein
                     21 kDa; protease-associated domain-containing protein of
                     21 kDa; protease-associated domain-containing protein 1"
                     /calculated_mol_wt=18929
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2132
     mat_peptide     22..188
                     /product="Protease-associated domain-containing protein 1.
                     /id=PRO_0000022001"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSG0.1)"
                     /calculated_mol_wt=18929
     Region          51..168
                     /region_name="PA_hPAP21_like"
                     /note="Protease-associated domain containing proteins like
                     the human secreted glycoprotein hPAP21 (human
                     protease-associated domain-containing protein, 21kDa).
                     This group contains various PA domain-containing proteins
                     similar to hPAP21. Complex N-glycosylation...; cd02127"
                     /db_xref="CDD:239042"
     Site            121
                     /site_type="other"
                     /note="Not glycosylated. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (Q9BSG0.1)"
     Site            126..128
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:239042"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15498570; propagated from
                     UniProtKB/Swiss-Prot (Q9BSG0.1)"
     CDS             1..188
                     /gene="PRADC1"
                     /gene_synonym="C2orf7; PAP21"
                     /coded_by="NM_032319.3:80..646"
                     /db_xref="CCDS:CCDS1924.1"
                     /db_xref="GeneID:84279"
                     /db_xref="HGNC:HGNC:16047"
                     /db_xref="MIM:619674"
ORIGIN      
        1 mvpgaagwcc lvlwlpacva ahgfrihdyl yfqvlspgdi ryiftatpak dfggifhtry
       61 eqihlvpaep peacgelsng ffiqdqialv erggcsflsk trvvqehggr aviisdnavd
      121 ndsfyvemiq dstqrtadip alfllgrdgy mirrsleqhg lpwaiisipv nvtsiptfel
      181 lqppwtfw
//
LOCUS       NP_689763                729 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase SH3RF2 [Homo sapiens].
ACCESSION   NP_689763
VERSION     NP_689763.4
DBSOURCE    REFSEQ: accession NM_152550.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Gong,T.T., Liu,F.H., Xiao,Q., Li,Y.Z., Wei,Y.F., Xu,H.L., Cao,F.,
            Sun,M.L., Jiang,F.L., Tao,T., Ma,Q.P., Qin,X., Song,Y., Gao,S.,
            Wu,L., Zhao,Y.H., Huang,D.H. and Wu,Q.J.
  TITLE     SH3RF2 contributes to cisplatin resistance in ovarian cancer cells
            by promoting RBPMS degradation
  JOURNAL   Commun Biol 7 (1), 67 (2024)
   PUBMED   38195842
  REMARK    GeneRIF: SH3RF2 contributes to cisplatin resistance in ovarian
            cancer cells by promoting RBPMS degradation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Yang,X., Sun,D., Xiang,H., Wang,S., Huang,Y., Li,L., Cheng,X.,
            Liu,H., Hu,F., Cheng,Y., Ma,T., Hu,M., Tian,H., Tian,S., Zhou,Y.,
            Zhang,P., Zhang,X.J., Ji,Y.X., Hu,Y., Li,H. and She,Z.G.
  TITLE     Hepatocyte SH3RF2 Deficiency Is a Key Aggravator for NAFLD
  JOURNAL   Hepatology 74 (3), 1319-1338 (2021)
   PUBMED   33894019
  REMARK    GeneRIF: Hepatocyte SH3RF2 Deficiency Is a Key Aggravator for
            NAFLD.
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Chen,H., Zhou,J., Jiao,L., Song,J., Zhong,H., Zhao,Z., Meng,Z.,
            Lu,X., Chen,X., Zhang,W. and Ying,B.
  TITLE     Assessing the role of SH3RF1 and SH3RF2 polymorphisms in
            susceptibility to tuberculosis: A case-control study in the Han
            Chinese population
  JOURNAL   Microb Pathog 152, 104567 (2021)
   PUBMED   33129950
  REMARK    GeneRIF: Assessing the role of SH3RF1 and SH3RF2 polymorphisms in
            susceptibility to tuberculosis: A case-control study in the Han
            Chinese population.
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 729)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 729)
  AUTHORS   Wilhelm,M., Kukekov,N.V., Schmit,T.L., Biagas,K.V., Sproul,A.A.,
            Gire,S., Maes,M.E., Xu,Z. and Greene,L.A.
  TITLE     Sh3rf2/POSHER protein promotes cell survival by ring-mediated
            proteasomal degradation of the c-Jun N-terminal kinase scaffold
            POSH (Plenty of SH3s) protein
  JOURNAL   J Biol Chem 287 (3), 2247-2256 (2012)
   PUBMED   22128169
REFERENCE   7  (residues 1 to 729)
  AUTHORS   Esteves,S.L., Domingues,S.C., da Cruz e Silva,O.A., Fardilha,M. and
            da Cruz e Silva,E.F.
  TITLE     Protein phosphatase 1alpha interacting proteins in the human brain
  JOURNAL   OMICS 16 (1-2), 3-17 (2012)
   PUBMED   22321011
REFERENCE   8  (residues 1 to 729)
  AUTHORS   Chen,C.Y., Lai,N.S., Yang,J.J., Huang,H.L., Hung,W.C., Li,C.,
            Lin,T.H. and Huang,H.B.
  TITLE     FLJ23654 encodes a heart protein phosphatase 1-binding protein
            (Hepp1)
  JOURNAL   Biochem Biophys Res Commun 391 (1), 698-702 (2010)
   PUBMED   19945436
  REMARK    GeneRIF: the novel protein heart protein phosphatase 1-binding
            protein (Hepp1), encoded by FLJ23654, was identified.Hepp1 can play
            a role in cardiac functions by working in concert with PP1.
REFERENCE   9  (residues 1 to 729)
  AUTHORS   Voss,M., Lettau,M. and Janssen,O.
  TITLE     Identification of SH3 domain interaction partners of human FasL
            (CD178) by phage display screening
  JOURNAL   BMC Immunol 10, 53 (2009)
   PUBMED   19807924
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 729)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011359.5, AC005351.1, AC005216.1 and AC091887.3.
            
            On Nov 23, 2018 this sequence version replaced NP_689763.3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK074234.1, SRR1803617.280437.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359120.9/ ENSP00000352028.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..729
                     /product="E3 ubiquitin-protein ligase SH3RF2"
                     /EC_number="2.3.2.27"
                     /note="putative E3 ubiquitin-protein ligase SH3RF2; RING
                     finger protein 158; SH3 domain-containing RING finger
                     protein 2; heart protein phosphatase 1-binding protein;
                     protein phosphatase 1 regulatory subunit 39;
                     POSH-eliminating RING protein; phosphatase 1 binding
                     protein; RING-type E3 ubiquitin transferase SH3RF2"
                     /calculated_mol_wt=79189
     Region          11..55
                     /region_name="RING-HC_SH3RF2"
                     /note="RING finger, HC subclass, found in SH3
                     domain-containing RING finger protein 2 (SH3RF2) and
                     similar proteins; cd16749"
                     /db_xref="CDD:438407"
     Region          78..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEC5.3)"
     Region          128..181
                     /region_name="SH3_SH3RF2_1"
                     /note="First Src Homology 3 domain of SH3 domain
                     containing ring finger 2; cd11929"
                     /db_xref="CDD:212862"
     Site            order(134,136,139,143,161..162,175,177..178)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212862"
     Region          191..247
                     /region_name="SH3_SH3RF2_2"
                     /note="Second Src Homology 3 domain of SH3 domain
                     containing ring finger 2; cd11932"
                     /db_xref="CDD:212865"
     Site            order(196,198,201,211,229..230,243,245..246)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212865"
     Region          258..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEC5.3)"
     Region          370..459
                     /region_name="Interaction with PAK4.
                     /evidence=ECO:0000269|PubMed:24130170"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEC5.3)"
     Region          384..438
                     /region_name="SH3_SH3RF2_3"
                     /note="Third Src Homology 3 domain of SH3 domain
                     containing ring finger 2; cd11784"
                     /db_xref="CDD:212718"
     Site            order(389,391,394,398,416..417,432,434..435)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212718"
     Region          497..526
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEC5.3)"
     Region          610..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEC5.3)"
     Region          641..646
                     /region_name="Interaction with PPP1CA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEC5.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q498M5; propagated from
                     UniProtKB/Swiss-Prot (Q8TEC5.3)"
     CDS             1..729
                     /gene="SH3RF2"
                     /gene_synonym="HEPP1; POSHER; PPP1R39; RNF158"
                     /coded_by="NM_152550.4:224..2413"
                     /db_xref="CCDS:CCDS4280.1"
                     /db_xref="GeneID:153769"
                     /db_xref="HGNC:HGNC:26299"
                     /db_xref="MIM:613377"
ORIGIN      
        1 mddltlldll ecpvcfekld vtakvlpcqh tfckpclqrv fkahkelrcp ecrtpvfsni
       61 ealpanlllv rlldgvrsgq ssgrggsfrr pgtmtlqdgr ksrtnprrlq aspfrlvpnv
      121 rihmdgvpra kalcnyrgqn pgdlrfnkgd iillrrqlde nwyqgeingi sgnfpassve
      181 vikqlpqppp lcralynfdl rgkdksenqd cltflkddii tvisrvdenw aegklgdkvg
      241 ifpilfvepn ltarhllekn kgrqssrtkn lslvssssrg ntstlrrgpg srrkvpgqfs
      301 ittalntlnr mvhspsgrhm veistpvlis ssnpsvitqp mekadvpssc vgqvstyhpa
      361 pvspghstav vslpgsqqhl sanmfvalhs ysahgpdeld lqkgegvrvl gkcqdgwlrg
      421 vslvtgrvgi fpnnyvipif rktssfpdsr spglyttwtl stssvssqgs isegdprqsr
      481 pfksvfvpta ivnpvrstag pgtlgqgslr kgrssmrkng slqrplqsgi ptlvvgslrr
      541 sptmvlrpqq fqfyqpqgip sspsavvvem gskpaltgep altcisrgse awihsaassl
      601 imedkeipik seplpkppas appsilvkpe nsrngiekqv ktvrfqnysp pptkhytshp
      661 tsgkpeqpat lkasqpeaas lgpemtvlfa hrsgchsgqq tdlrrksalg kattlvstas
      721 gtqtvfpsk
//
LOCUS       NP_115829                609 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 527 [Homo sapiens].
ACCESSION   NP_115829 XP_951045
VERSION     NP_115829.1
DBSOURCE    REFSEQ: accession NM_032453.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Gulkovskyi,R.V., Chernushyn,S.Y., Kravchenko,S.A. and Livshits,L.A.
  TITLE     ZNF527 GENE rs386809049 ANALYSIS IN POPULATION OF UKRAINE
  JOURNAL   Tsitol Genet 49 (4), 35-39 (2015)
   PUBMED   26419067
  REMARK    GeneRIF: A high polymorphic ZNF527 allele frequency implies that
            rs386809049 polymorphism in ZNF527 gene cannot be the major cause
            of intellectual disability in the Ukrainian population.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008806.4 and DC341389.1.
            
            On Jun 21, 2007 this sequence version replaced XP_951045.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.26349.1,
                                           SRR1803613.111019.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000436120.7/ ENSP00000390179.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..609
                     /product="zinc finger protein 527"
                     /calculated_mol_wt=70771
     Region          14..74
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          222..240
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          252..268
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          277..296
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          304..324
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <328..490
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          332..352
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          360..380
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(365,367,369,371..372,375..376,379,393,395,399..400,
                     403..404,407,421,423,425,427..428,431..432,435)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          388..408
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          416..436
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          444..464
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          472..492
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          485..508
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          500..520
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          516..537
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          528..548
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(533,535,537,539..540,543..544,547,561,563,567..568,
                     571..572,575,589,591,593,595..596,599..600,603)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          540..563
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          556..576
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          568..593
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          584..604
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..609
                     /gene="ZNF527"
                     /coded_by="NM_032453.2:170..1999"
                     /db_xref="CCDS:CCDS42559.1"
                     /db_xref="GeneID:84503"
                     /db_xref="HGNC:HGNC:29385"
ORIGIN      
        1 mavglckams qglvtfrdva ldfsqeewew lkpsqkdlyr dvmlenyrnl vwlglsiskp
       61 nmislleqgk epwmverkms qghcadwesw ceieelspkw fidedeisqe mvmerlashg
      121 lecssfreaw kykgefelhq gnaerhfmqv tavkeistgk rdnefsnsgr siplksvflt
      181 qqkvptiqqv hkfdiydklf pqnsviieyk rlhaekesli gneceefnqs tylskdigip
      241 pgekpyeshd fskllsfhsl ftqhqtthfg klphgydecg dafscysfft qpqrihsgek
      301 pyacndcgka fshdfflseh qrthigekpy eckecnkafr qsahlaqhqr ihtgekpfac
      361 necgkafsry aflvehqrih tgekpyecke cnkafrqsah lnqhqrihtg ekpyecnqcg
      421 kafsrrialt lhqrihtgek pfkcsecgkt fgyrshlnqh qrihtgekpy ecikcgkffr
      481 tdsqlnrhhr ihtgerpfec skcgkafsda lvlihhkrsh agekpyecnk cgkafscgsy
      541 lnqhqrihtg ekpyecsecg kafhqilslr lhqrihagek pykcnecgnn fscvsalrrh
      601 qrihnretl
//
LOCUS       NP_001135758            1091 aa            linear   PRI 27-APR-2025
DEFINITION  structural maintenance of chromosomes protein 6 [Homo sapiens].
ACCESSION   NP_001135758
VERSION     NP_001135758.1
DBSOURCE    REFSEQ: accession NM_001142286.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Diman,A., Panis,G., Castrogiovanni,C., Prados,J., Baechler,B. and
            Strubin,M.
  TITLE     Human Smc5/6 recognises transcription-generated positive DNA
            supercoils
  JOURNAL   Nat Commun 15 (1), 7805 (2024)
   PUBMED   39242537
  REMARK    GeneRIF: Human Smc5/6 recognises transcription-generated positive
            DNA supercoils.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Fingerman,D.F., O'Leary,D.R., Hansen,A.R., Tran,T., Harris,B.R.,
            DeWeerd,R.A., Hayer,K.E., Fan,J., Chen,E., Tennakoon,M., Meroni,A.,
            Szeto,J.H., Devenport,J., LaVigne,D., Weitzman,M.D., Shalem,O.,
            Bednarski,J., Vindigni,A., Zhao,X. and Green,A.M.
  TITLE     The SMC5/6 complex prevents genotoxicity upon APOBEC3A-mediated
            replication stress
  JOURNAL   EMBO J 43 (15), 3240-3255 (2024)
   PUBMED   38886582
  REMARK    GeneRIF: The SMC5/6 complex prevents genotoxicity upon
            APOBEC3A-mediated replication stress.
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Roy,S., Adhikary,H. and D'Amours,D.
  TITLE     The SMC5/6 complex: folding chromosomes back into shape when
            genomes take a break
  JOURNAL   Nucleic Acids Res 52 (5), 2112-2129 (2024)
   PUBMED   38375830
  REMARK    GeneRIF: The SMC5/6 complex: folding chromosomes back into shape
            when genomes take a break.
            Review article
REFERENCE   4  (residues 1 to 1091)
  AUTHORS   Irwan,I.D., Bogerd,H.P. and Cullen,B.R.
  TITLE     Epigenetic silencing by the SMC5/6 complex mediates HIV-1 latency
  JOURNAL   Nat Microbiol 7 (12), 2101-2113 (2022)
   PUBMED   36376394
  REMARK    GeneRIF: Epigenetic silencing by the SMC5/6 complex mediates HIV-1
            latency.
REFERENCE   5  (residues 1 to 1091)
  AUTHORS   Oravcova,M., Nie,M., Zilio,N., Maeda,S., Jami-Alahmadi,Y.,
            Lazzerini-Denchi,E., Wohlschlegel,J.A., Ulrich,H.D., Otomo,T. and
            Boddy,M.N.
  TITLE     The Nse5/6-like SIMC1-SLF2 complex localizes SMC5/6 to viral
            replication centers
  JOURNAL   Elife 11, e79676 (2022)
   PUBMED   36373674
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1091)
  AUTHORS   Potts,P.R. and Yu,H.
  TITLE     Human MMS21/NSE2 is a SUMO ligase required for DNA repair
  JOURNAL   Mol Cell Biol 25 (16), 7021-7032 (2005)
   PUBMED   16055714
  REMARK    GeneRIF: the human SMC5/6 complex and the SUMO ligase activity of
            hMMS21 are required for the prevention of DNA damage-induced
            apoptosis by facilitating DNA repair in human cells
REFERENCE   7  (residues 1 to 1091)
  AUTHORS   Sergeant,J., Taylor,E., Palecek,J., Fousteri,M., Andrews,E.A.,
            Sweeney,S., Shinagawa,H., Watts,F.Z. and Lehmann,A.R.
  TITLE     Composition and architecture of the Schizosaccharomyces pombe Rad18
            (Smc5-6) complex
  JOURNAL   Mol Cell Biol 25 (1), 172-184 (2005)
   PUBMED   15601840
REFERENCE   8  (residues 1 to 1091)
  AUTHORS   Harvey,S.H., Sheedy,D.M., Cuddihy,A.R. and O'Connell,M.J.
  TITLE     Coordination of DNA damage responses via the Smc5/Smc6 complex
  JOURNAL   Mol Cell Biol 24 (2), 662-674 (2004)
   PUBMED   14701739
REFERENCE   9  (residues 1 to 1091)
  AUTHORS   Taylor,E.M., Moghraby,J.S., Lees,J.H., Smit,B., Moens,P.B. and
            Lehmann,A.R.
  TITLE     Characterization of a novel human SMC heterodimer homologous to the
            Schizosaccharomyces pombe Rad18/Spr18 complex
  JOURNAL   Mol Biol Cell 12 (6), 1583-1594 (2001)
   PUBMED   11408570
REFERENCE   10 (residues 1 to 1091)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB451629.1, AL136544.1, BC039828.1, AL832979.1 and CD369665.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136544.1, SRR1660803.160497.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000448223.7/ ENSP00000404092.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.2"
     Protein         1..1091
                     /product="structural maintenance of chromosomes protein 6"
                     /note="SMC protein 6; SMC6 structural maintenance of
                     chromosomes 6-like 1"
                     /calculated_mol_wt=126195
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB8.2)"
     Region          48..>204
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            76..83
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213179"
     Site            188..191
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213179"
     Region          <215..1049
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          452..659
                     /region_name="Flexible hinge"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB8.2)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96SB8.2)"
     Region          806..828
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB8.2)"
     Region          <977..1075
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            987..996
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213179"
     Site            1011..1016
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213179"
     Site            1019..1022
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213179"
     Site            1046..1052
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213179"
     Region          1072..1091
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB8.2)"
     CDS             1..1091
                     /gene="SMC6"
                     /gene_synonym="hSMC6; SMC-6; SMC6L1"
                     /coded_by="NM_001142286.2:278..3553"
                     /db_xref="CCDS:CCDS1690.1"
                     /db_xref="GeneID:79677"
                     /db_xref="HGNC:HGNC:20466"
                     /db_xref="MIM:609387"
ORIGIN      
        1 makrkeenfs spknakrprq eeledfdkdg dedeckgttl taaevgiies ihlknfmchs
       61 mlgpfkfgsn vnfvvgnngs gksavltali vglggravat nrgsslkgfv kdgqnsadis
      121 itlrnrgdda fkasvygnsi liqqhisidg srsyklksat gsvvstrkee liaildhfni
      181 qvdnpvsvlt qemskqflqs knegdkykff mkatqleqmk edysyimetk ertkeqihqg
      241 eerltelkrq cvekeerfqs iaglstmktn leslkhemaw avvneiekql nairdnikig
      301 edraarldrk meeqqvrlne aeqkykdiqd klekiseetn arapecmalk advvakkray
      361 neaevlynrs lneykalkkd deqlckriee lkkstdqsle perlerqkki swlkervkaf
      421 qnqensvnqe ieqfqqaiek dkeehgkikr eeldvkhals ynqrqlkelk dsktdrlkrf
      481 gpnvpallea iddayrqghf tykpvgplga cihlrdpela laiesclkgl lqaycchnha
      541 dervlqalmk rfylpgtsrp piivsefrne iydvrhraay hpdfptvlta leidnavvan
      601 slidmrgiet vlliknnsva ravmqsqkpp kncreaftad gdqvfagryy ssentrpkfl
      661 srdvdseisd lenevenkta qilnlqqhls alekdikhne ellkrcqlhy kelkmkirkn
      721 iseireleni eehqsvdiat ledeaqenks kmkmveehme qqkenmehlk slkieaenky
      781 daikfkinql seladplkde lnladsevdn qkrgkrhyee kqkehldtln kkkreldmke
      841 keleekmsqa rqicperiev eksasildke inrlrqkiqa ehashgdree imrqyqeare
      901 tyldldskvr tlkkfikllg eimehrfkty qqfrrcltlr cklyfdnlls qraycgkmnf
      961 dhknetlsis vqpgegnkaa fndmralsgg ersfstvcfi lslwsiaesp frcldefdvy
     1021 mdmvnrriam dlilkmadsq rfrqfilltp qsmsslpssk lirilrmsdp ergqttlpfr
     1081 pvtqeedddq r
//
LOCUS       NP_055976                203 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-ribosylation factor-like protein 6-interacting protein 1
            isoform 1 [Homo sapiens].
ACCESSION   NP_055976
VERSION     NP_055976.1
DBSOURCE    REFSEQ: accession NM_015161.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Byrne,D.J., Garcia-Pardo,M.E., Cole,N.B., Batnasan,B., Heneghan,S.,
            Sohail,A., Blackstone,C. and O'Sullivan,N.C.
  TITLE     Liver X receptor-agonist treatment rescues degeneration in a
            Drosophila model of hereditary spastic paraplegia
  JOURNAL   Acta Neuropathol Commun 10 (1), 40 (2022)
   PUBMED   35346366
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 203)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 203)
  AUTHORS   Lui,H.M., Chen,J., Wang,L. and Naumovski,L.
  TITLE     ARMER, apoptotic regulator in the membrane of the endoplasmic
            reticulum, a novel inhibitor of apoptosis
  JOURNAL   Mol Cancer Res 1 (7), 508-518 (2003)
   PUBMED   12754298
  REMARK    GeneRIF: novel endoplasmic reticulum integral membrane protein
            which protects cells by inhibiting caspase-9 activity and reveal a
            possible role for ARMER in cell survival
REFERENCE   9  (residues 1 to 203)
  AUTHORS   Pettersson,M., Bessonova,M., Gu,H.F., Groop,L.C. and Jonsson,J.I.
  TITLE     Characterization, chromosomal localization, and expression during
            hematopoietic differentiation of the gene encoding Arl6ip,
            ADP-ribosylation-like factor-6 interacting protein (ARL6)
  JOURNAL   Genomics 68 (3), 351-354 (2000)
   PUBMED   10995579
REFERENCE   10 (residues 1 to 203)
  AUTHORS   Ingley,E., Williams,J.H., Walker,C.E., Tsai,S., Colley,S.,
            Sayer,M.S., Tilbrook,P.A., Sarna,M., Beaumont,J.G. and Klinken,S.P.
  TITLE     A novel ADP-ribosylation like factor (ARL-6), interacts with the
            protein-conducting channel SEC61beta subunit
  JOURNAL   FEBS Lett 459 (1), 69-74 (1999)
   PUBMED   10508919
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC406882.1 and BC010281.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to the ARL6ip family and encodes a
            transmembrane protein that is predominantly localized to
            intracytoplasmic membranes. It is highly expressed in early myeloid
            progenitor cells and thought to be involved in protein transport,
            membrane trafficking, or cell signaling during hematopoietic
            maturation. Mutations in this gene are associated with spastic
            paraplegia 61 (SPG61). Alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1135795.1,
                                           SRR3476690.254845.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267779 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304414.12/ ENSP00000306788.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..203
                     /product="ADP-ribosylation factor-like protein
                     6-interacting protein 1 isoform 1"
                     /note="ADP-ribosylation factor-like 6 interacting protein
                     1; ADP-ribosylation factor GTPase 6 interacting protein 1;
                     ADP ribosylation factor like GTPase 6 interacting protein
                     1; ARF like GTPase 6 interacting protein 1; apoptotic
                     regulator in the membrane of the endoplasmic reticulum;
                     ADP-ribosylation factor-like protein 6-interacting protein
                     1; aip-1; ARL-6-interacting protein 1"
                     /calculated_mol_wt=23232
     Region          34..200
                     /region_name="Arl6IP1"
                     /note="ADP-ribosylation factor-like protein 6-interacting
                     protein 1; cd22559"
                     /db_xref="CDD:411698"
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15041.2)"
     Site            66..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15041.2)"
     Site            134..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15041.2)"
     CDS             1..203
                     /gene="ARL6IP1"
                     /gene_synonym="AIP1; ARL6IP; ARMER; SPG61"
                     /coded_by="NM_015161.3:84..695"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10572.1"
                     /db_xref="GeneID:23204"
                     /db_xref="HGNC:HGNC:697"
                     /db_xref="MIM:607669"
ORIGIN      
        1 maegdnrstn llaaetasle eqlqgwgevm lmadkvlrwe rawfppaimg vvslvfliiy
       61 yldpsvlsgv scfvmflcla dylvpilapr ifgsnkwtte qqqrfheics nlvktrrrav
      121 gwwkrlftlk eekpkmyfmt mivslaavaw vgqqvhnlll tylivtslll lpglnqhgii
      181 lkyigmakre inkllkqkek kne
//
LOCUS       NP_060060                977 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger CCCH domain-containing protein 7B [Homo sapiens].
ACCESSION   NP_060060 NP_079289
VERSION     NP_060060.3
DBSOURCE    REFSEQ: accession NM_017590.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Hoang,L.N., Aneja,A., Conlon,N., Delair,D.F., Middha,S.,
            Benayed,R., Hensley,M.L., Park,K.J., Hollmann,T.J., Hameed,M.R.,
            Antonescu,C.R., Soslow,R.A. and Chiang,S.
  TITLE     Novel High-grade Endometrial Stromal Sarcoma: A Morphologic
            Mimicker of Myxoid Leiomyosarcoma
  JOURNAL   Am J Surg Pathol 41 (1), 12-24 (2017)
   PUBMED   27631520
  REMARK    GeneRIF: we find that ESS with ZC3H7B-BCOR fusion constitutes a
            novel type of high-grade endometrial stromal sarcoma and shares
            significant morphologic overlap with myxoid leiomyosarcoma.
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Specht,K., Zhang,L., Sung,Y.S., Nucci,M., Dry,S., Vaiyapuri,S.,
            Richter,G.H., Fletcher,C.D. and Antonescu,C.R.
  TITLE     Novel BCOR-MAML3 and ZC3H7B-BCOR Gene Fusions in Undifferentiated
            Small Blue Round Cell Sarcomas
  JOURNAL   Am J Surg Pathol 40 (4), 433-442 (2016)
   PUBMED   26752546
  REMARK    GeneRIF: The present study further expands the genetic spectrum of
            small blue round cell tumors, with 2 novel fusions, BCOR-MAML3 and
            ZC3H7B-BCOR, identified
REFERENCE   4  (residues 1 to 977)
  AUTHORS   Antonescu,C.R., Sung,Y.S., Chen,C.L., Zhang,L., Chen,H.W.,
            Singer,S., Agaram,N.P., Sboner,A. and Fletcher,C.D.
  TITLE     Novel ZC3H7B-BCOR, MEAF6-PHF1, and EPC1-PHF1 fusions in ossifying
            fibromyxoid tumors--molecular characterization shows genetic
            overlap with endometrial stromal sarcoma
  JOURNAL   Genes Chromosomes Cancer 53 (2), 183-193 (2014)
   PUBMED   24285434
  REMARK    GeneRIF: ZC3H7B-BCOR and MEAF6-PHF1 fusions occurred predominantly
            in S100 protein-negative and malignant ossifying fibromyxoid
            tumors.
REFERENCE   5  (residues 1 to 977)
  AUTHORS   Panagopoulos,I., Thorsen,J., Gorunova,L., Haugom,L.,
            Bjerkehagen,B., Davidson,B., Heim,S. and Micci,F.
  TITLE     Fusion of the ZC3H7B and BCOR genes in endometrial stromal sarcomas
            carrying an X;22-translocation
  JOURNAL   Genes Chromosomes Cancer 52 (7), 610-618 (2013)
   PUBMED   23580382
  REMARK    GeneRIF: Reverse transciptase-PCR with the ZC3H7B forward and BCOR
            reverse primer combinations confirmed the presence of a ZC3H7-BCOR
            chimeric transcript in both ESS carrying a der(22)t(X;22) but not
            in a control ESS with t(1;6) and the MEAF6-PHF1 fusion.
REFERENCE   6  (residues 1 to 977)
  AUTHORS   Harb,M., Becker,M.M., Vitour,D., Baron,C.H., Vende,P., Brown,S.C.,
            Bolte,S., Arold,S.T. and Poncet,D.
  TITLE     Nuclear localization of cytoplasmic poly(A)-binding protein upon
            rotavirus infection involves the interaction of NSP3 with eIF4G and
            RoXaN
  JOURNAL   J Virol 82 (22), 11283-11293 (2008)
   PUBMED   18799579
  REMARK    GeneRIF: nuclear localization of PABP-C1 not only is dependent on
            the capacity of rotavirus NSP3 to interact with eIF4G but also
            requires the interaction of NSP3 with a specific region in RoXaN
REFERENCE   7  (residues 1 to 977)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 977)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   9  (residues 1 to 977)
  AUTHORS   Vitour,D., Lindenbaum,P., Vende,P., Becker,M.M. and Poncet,D.
  TITLE     RoXaN, a novel cellular protein containing TPR, LD, and zinc finger
            motifs, forms a ternary complex with eukaryotic initiation factor
            4G and rotavirus NSP3
  JOURNAL   J Virol 78 (8), 3851-3862 (2004)
   PUBMED   15047801
  REMARK    GeneRIF: RoXaN is capable of interacting with NSP3 and eIF4G I in
            vivo and during rotavirus infection. Domains of interaction were
            mapped.
REFERENCE   10 (residues 1 to 977)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL035659.22.
            
            On or before Jan 23, 2003 this sequence version replaced
            NP_079289.1, NP_060060.2.
            
            Summary: This gene encodes a protein that contains a
            tetratricopeptide repeat domain. The encoded protein also interacts
            with the rotavirus non-structural protein NSP3. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC152558.1, BC098378.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000352645.5/ ENSP00000345793.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..977
                     /product="zinc finger CCCH domain-containing protein 7B"
                     /note="ubiquitous tetratricopeptide containing protein
                     RoXaN; rotavirus X protein associated with NSP3; Rotavirus
                     'X' associated non-structural protein; rotavirus
                     'X'-associated non-structural protein"
                     /calculated_mol_wt=109727
     Region          1..27
                     /region_name="TPR 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGR2.2)"
     Region          18..>162
                     /region_name="3a0801s09"
                     /note="mitochondrial precursor proteins import receptor
                     (72 kDa mitochondrial outermembrane protein)
                     (mitochondrial import receptor for the ADP/ATP carrier)
                     (translocase of outermembrane tom70); TIGR00990"
                     /db_xref="CDD:273380"
     Region          36..69
                     /region_name="TPR 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGR2.2)"
     Region          39..64
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(40..41,44..45,47,83,86..87,90..91,93..94,117,
                     120..121,124..125,128)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          69..111
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          82..115
                     /region_name="TPR 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGR2.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UGR2.2)"
     Region          248..256
                     /region_name="LD motif, interaction with NSP3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGR2.2)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UGR2.2)"
     Region          365..403
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGR2.2)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UGR2.2)"
     Region          844..867
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          844..866
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          890..913
                     /region_name="zf-CCCH"
                     /note="Zinc finger C-x8-C-x5-C-x3-H type (and similar);
                     pfam00642"
                     /db_xref="CDD:459885"
     CDS             1..977
                     /gene="ZC3H7B"
                     /gene_synonym="RoXaN; ROXAN1"
                     /coded_by="NM_017590.6:255..3188"
                     /db_xref="CCDS:CCDS14013.1"
                     /db_xref="GeneID:23264"
                     /db_xref="HGNC:HGNC:30869"
                     /db_xref="MIM:618206"
ORIGIN      
        1 merqkrkadi ekglqfiqst lplkqeeyea fllklvqnlf aegndlfrek dykqalvqym
       61 eglnvadyaa sdqvalprel lcklhvnraa cyftmglyek aledsekalg ldsesiralf
      121 rkaralnelg rhkeayecss rcslalphde svtqlgqela qklglrvrka ykrpqeletf
      181 sllsngtaag vadqgtsngl gsiddietdc yvdprgspal lpstptmplf phvldllapl
      241 dssrtlpstd slddfsdgdv fgpeldtlld slslvqggls gsgvpselpq lipvfpggtp
      301 llppvvggsi pvssplppas fglvmdpskk laasvldald ppgptldpld llpysetrld
      361 aldsfgstrg sldkpdsfme etnsqdhrpp sgaqkpapsp epcmpntall iknplaathe
      421 fkqacqlcyp ktgpragdyt yreglehkck rdillgrlrs sedqtwkrir prptktsfvg
      481 syylckdmin kqdckygdnc tfayhqeeid vwteerkgtl nrdllfdplg gvkrgsltia
      541 kllkehqgif tflceicfds kpriiskgtk dspsvcsnla akhsfynnkc lvhivrstsl
      601 kyskirqfqe hfqfdvcrhe vrygclreds chfahsfiel kvwllqqysg mthedivqes
      661 kkywqqmeah agkasssmga prthgpstfd lqmkfvcgqc wrngqvvepd kdlkycsaka
      721 rhcwtkerrv llvmskakrk wvsvrplpsi rnfpqqydlc ihaqngrkcq yvgncsfahs
      781 peerdmwtfm kenkildmqq tydmwlkkhn pgkpgegtpi ssregekqiq mptdyadimm
      841 gyhcwlcgkn snskkqwqqh iqsekhkekv ftsdsdasgw afrfpmgefr lcdrlqkgka
      901 cpdgdkcrca hgqeelnewl drrevlkqkl akarkdmllc prdddfgkyn fllqedgdla
      961 gatpeapaaa atattge
//
LOCUS       NP_001354778             254 aa            linear   PRI 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 10 [Homo sapiens].
ACCESSION   NP_001354778
VERSION     NP_001354778.1
DBSOURCE    REFSEQ: accession NM_001367849.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Lu,J., Li,H., Zhang,H., Lin,Z., Xu,C., Xu,X., Hu,L., Luan,Z.,
            Lou,Y. and Tang,S.
  TITLE     The distal arthrogryposis-linked p.R63C variant promotes the
            stability and nuclear accumulation of TNNT3
  JOURNAL   J Clin Lab Anal 35 (12), e24089 (2021)
   PUBMED   34766372
  REMARK    GeneRIF: The distal arthrogryposis-linked p.R63C variant promotes
            the stability and nuclear accumulation of TNNT3.
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Nunez Lopez,Y.O., Messi,M.L., Pratley,R.E., Zhang,T. and Delbono,O.
  TITLE     Troponin T3 associates with DNA consensus sequence that overlaps
            with p53 binding motifs
  JOURNAL   Exp Gerontol 108, 35-40 (2018)
   PUBMED   29596868
  REMARK    GeneRIF: The TnT3 appears to contribute to age-related sarcopenia
            and possibly other age-related deficiencies such as muscle insulin
            resistance and beta cell dysfunction by interacting with
            TnT3-binding sequences in the promoter area of p53-related genes,
            among others, and consequently modulating the transcriptional
            regulation of these target genes.
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Wei,B. and Jin,J.P.
  TITLE     TNNT1, TNNT2, and TNNT3: Isoform genes, regulation, and
            structure-function relationships
  JOURNAL   Gene 582 (1), 1-13 (2016)
   PUBMED   26774798
  REMARK    GeneRIF: Three homologous genes have evolved in vertebrates to
            encode three muscle type-specific TnT isoforms: TNNT1 for slow
            skeletal muscle TnT, TNNT2 for cardiac muscle TnT, and TNNT3 for
            fast skeletal muscle TnT.
            Review article
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Vorster,A.A., Beighton,P. and Ramesar,R.S.
  TITLE     Digitotalar dysmorphism: Molecular elucidation
  JOURNAL   S Afr Med J 106 (3), 253-255 (2016)
   PUBMED   26915936
  REMARK    GeneRIF: The presence of the p.(Arg63His) missense mutation at
            position 63 of TNNT3 was confirmed through direct cycle sequencing
            of genomic DNA in six affected South African family members for
            whom DNA had been archived.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Lindstrom,S., Thompson,D.J., Paterson,A.D., Li,J., Gierach,G.L.,
            Scott,C., Stone,J., Douglas,J.A., dos-Santos-Silva,I.,
            Fernandez-Navarro,P., Verghase,J., Smith,P., Brown,J., Luben,R.,
            Wareham,N.J., Loos,R.J., Heit,J.A., Pankratz,V.S., Norman,A.,
            Goode,E.L., Cunningham,J.M., deAndrade,M., Vierkant,R.A., Czene,K.,
            Fasching,P.A., Baglietto,L., Southey,M.C., Giles,G.G., Shah,K.P.,
            Chan,H.P., Helvie,M.A., Beck,A.H., Knoblauch,N.W., Hazra,A.,
            Hunter,D.J., Kraft,P., Pollan,M., Figueroa,J.D., Couch,F.J.,
            Hopper,J.L., Hall,P., Easton,D.F., Boyd,N.F., Vachon,C.M. and
            Tamimi,R.M.
  TITLE     Genome-wide association study identifies multiple loci associated
            with both mammographic density and breast cancer risk
  JOURNAL   Nat Commun 5, 5303 (2014)
   PUBMED   25342443
  REMARK    Erratum:[Nat Commun. 2015 Sep 09;6:8358. doi: 10.1038/ncomms9358.
            PMID: 26349435]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Stefancsik,R., Randall,J.D., Mao,C. and Sarkar,S.
  TITLE     Structure and sequence of the human fast skeletal troponin T
            (TNNT3) gene: insight into the evolution of the gene and the origin
            of the developmentally regulated isoforms
  JOURNAL   Comp Funct Genomics 4 (6), 609-625 (2003)
   PUBMED   18629027
  REMARK    Erratum:[Comp Funct Genomics. 2004;5(2):205]
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Briggs,M.M., Maready,M., Schmidt,J.M. and Schachat,F.
  TITLE     Identification of a fetal exon in the human fast troponin T gene
  JOURNAL   FEBS Lett 350 (1), 37-40 (1994)
   PUBMED   8062920
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Wu,Q.L., Jha,P.K., Raychowdhury,M.K., Du,Y., Leavis,P.C. and
            Sarkar,S.
  TITLE     Isolation and characterization of human fast skeletal beta troponin
            T cDNA: comparative sequence analysis of isoforms and insight into
            the evolution of members of a multigene family
  JOURNAL   DNA Cell Biol 13 (3), 217-233 (1994)
   PUBMED   8172653
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Chong,P.C. and Hodges,R.S.
  TITLE     Photochemical cross-linking between rabbit skeletal troponin
            subunits. Troponin I-troponin T interactions
  JOURNAL   J Biol Chem 257 (19), 11667-11672 (1982)
   PUBMED   7118902
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC051649.21.
            
            Summary: The binding of Ca(2+) to the trimeric troponin complex
            initiates the process of muscle contraction. Increased Ca(2+)
            concentrations produce a conformational change in the troponin
            complex that is transmitted to tropomyosin dimers situated along
            actin filaments. The altered conformation permits increased
            interaction between a myosin head and an actin filament which,
            ultimately, produces a muscle contraction. The troponin complex has
            protein subunits C, I, and T. Subunit C binds Ca(2+) and subunit I
            binds to actin and inhibits actin-myosin interaction. Subunit T
            binds the troponin complex to the tropomyosin complex and is also
            required for Ca(2+)-mediated activation of actomyosin ATPase
            activity. There are 3 different troponin T genes that encode
            tissue-specific isoforms of subunit T for fast skeletal-, slow
            skeletal-, and cardiac-muscle. This gene encodes fast skeletal
            troponin T protein; also known as troponin T type 3. Alternative
            splicing results in multiple transcript variants encoding
            additional distinct troponin T type 3 isoforms. A developmentally
            regulated switch between fetal/neonatal and adult troponin T type 3
            isoforms occurs. Additional splice variants have been described but
            their biological validity has not been established. Mutations in
            this gene may cause distal arthrogryposis multiplex congenita type
            2B (DA2B). [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.320060.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..254
                     /product="troponin T, fast skeletal muscle isoform 10"
                     /note="troponin T, fast skeletal muscle; troponin T type 3
                     (skeletal, fast)"
                     /calculated_mol_wt=29809
     Region          58..194
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..254
                     /gene="TNNT3"
                     /gene_synonym="beta-TnTF; DA2B2; TNTF"
                     /coded_by="NM_001367849.1:45..809"
                     /note="isoform 10 is encoded by transcript variant 14"
                     /db_xref="GeneID:7140"
                     /db_xref="HGNC:HGNC:11950"
                     /db_xref="MIM:600692"
ORIGIN      
        1 msdeeveqve eeaqeeaaev heedtaeeda eeekprpklt apkipegekv dfddiqkkrq
       61 nkdlmelqal idshfearkk eeeelvalke riekrraera eqqriraeke rerqnrlaee
      121 karreeedak rraeddlkkk kalssmgany ssylakadqk rgkkqtarem kkkilaerrk
      181 plnidhlged klrdkakelw etlhqleidk fefgeklkrq kydittlrsr idqaqkhskk
      241 agtpakgkvg grwk
//
LOCUS       NP_001353385             304 aa            linear   PRI 27-APR-2025
DEFINITION  rab GTPase-activating protein 1-like isoform Q [Homo sapiens].
ACCESSION   NP_001353385
VERSION     NP_001353385.1
DBSOURCE    REFSEQ: accession NM_001366456.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Anttila,V., Winsvold,B.S., Gormley,P., Kurth,T., Bettella,F.,
            McMahon,G., Kallela,M., Malik,R., de Vries,B., Terwindt,G.,
            Medland,S.E., Todt,U., McArdle,W.L., Quaye,L., Koiranen,M.,
            Ikram,M.A., Lehtimaki,T., Stam,A.H., Ligthart,L., Wedenoja,J.,
            Dunham,I., Neale,B.M., Palta,P., Hamalainen,E., Schurks,M.,
            Rose,L.M., Buring,J.E., Ridker,P.M., Steinberg,S., Stefansson,H.,
            Jakobsson,F., Lawlor,D.A., Evans,D.M., Ring,S.M., Farkkila,M.,
            Artto,V., Kaunisto,M.A., Freilinger,T., Schoenen,J., Frants,R.R.,
            Pelzer,N., Weller,C.M., Zielman,R., Heath,A.C., Madden,P.A.F.,
            Montgomery,G.W., Martin,N.G., Borck,G., Gobel,H., Heinze,A.,
            Heinze-Kuhn,K., Williams,F.M.K., Hartikainen,A.L., Pouta,A., van
            den Ende,J., Uitterlinden,A.G., Hofman,A., Amin,N., Hottenga,J.J.,
            Vink,J.M., Heikkila,K., Alexander,M., Muller-Myhsok,B.,
            Schreiber,S., Meitinger,T., Wichmann,H.E., Aromaa,A.,
            Eriksson,J.G., Traynor,B., Trabzuni,D., Rossin,E., Lage,K.,
            Jacobs,S.B.R., Gibbs,J.R., Birney,E., Kaprio,J., Penninx,B.W.,
            Boomsma,D.I., van Duijn,C., Raitakari,O., Jarvelin,M.R.,
            Zwart,J.A., Cherkas,L., Strachan,D.P., Kubisch,C., Ferrari,M.D.,
            van den Maagdenberg,A.M.J.M., Dichgans,M., Wessman,M., Smith,G.D.,
            Stefansson,K., Daly,M.J., Nyholt,D.R., Chasman,D. and Palotie,A.
  CONSRTM   North American Brain Expression Consortium; UK Brain Expression
            Consortium
  TITLE     Genome-wide meta-analysis identifies new susceptibility loci for
            migraine
  JOURNAL   Nat Genet 45 (8), 912-917 (2013)
   PUBMED   23793025
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Kim,J.H., Jung,S.H., Bae,J.S., Lee,H.S., Yim,S.H., Park,S.Y.,
            Bang,S.Y., Hu,H.J., Shin,H.D., Bae,S.C. and Chung,Y.J.
  TITLE     Deletion variants of RABGAP1L, 10q21.3, and C4 are associated with
            the risk of systemic lupus erythematosus in Korean women
  JOURNAL   Arthritis Rheum 65 (4), 1055-1063 (2013)
   PUBMED   23335107
  REMARK    GeneRIF: Deletion variants of RABGAP1L were found to be
            significantly associated with SLE in Korean women.
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL161671.25 and Z99127.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.210919.1,
                                           SRR1803615.113610.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1"
     Protein         1..304
                     /product="rab GTPase-activating protein 1-like isoform Q"
                     /note="TBC1 domain family, member 18; expressed in
                     hematopoietic cells, heart, liver (HLL); rab
                     GTPase-activating protein 1-like"
                     /calculated_mol_wt=35164
     CDS             1..304
                     /gene="RABGAP1L"
                     /gene_synonym="HHL; TBC1D18"
                     /coded_by="NM_001366456.1:596..1510"
                     /note="isoform Q is encoded by transcript variant 20"
                     /db_xref="GeneID:9910"
                     /db_xref="HGNC:HGNC:24663"
                     /db_xref="MIM:609238"
ORIGIN      
        1 meegvpcpap aakltppvkk sqdmhdersk lvneyacrvl ellgmghrlf vprllatske
       61 dllqadfega lkffrvqlpk ryraeenarr lmeqacnikv ptkklkkyek eyqtmresql
      121 qqedpmdryk renrrlqeas mrleqenddl ahelvtskia lrndldqaed kadvlnkell
      181 ltkqrlvete eekrkqeeet aqlkevfrkq lekaeyeikk ttaiiaeykq icsqlstrle
      241 kqqaaskeel evvkelehqr galmneiqaa knswfsktln siktatgtqp lqpapvtqpp
      301 kest
//
LOCUS       NP_001073982             545 aa            linear   PRI 27-APR-2025
DEFINITION  carboxypeptidase N subunit 2 precursor [Homo sapiens].
ACCESSION   NP_001073982 XP_930891
VERSION     NP_001073982.3
DBSOURCE    REFSEQ: accession NM_001080513.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Cui,R., Zhang,P. and Li,Y.
  TITLE     Role of Carboxypeptidase N Invasion and Migration in Breast Cancer
  JOURNAL   Anticancer Agents Med Chem 16 (9), 1198-1202 (2016)
   PUBMED   26860443
  REMARK    GeneRIF: Real-time PCR and western blotting show the following CPN2
            expression: minimal in MDA-MB-468 cells but obvious in MDA-MB-231
            and MCF7 cells. MDA-MB-231 breast cancer cell lines were selected
            for the control group and CPN2 was knocked out for the experimental
            group.
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Grilo,A., Saez-Rosas,M.P., Santos-Morano,J., Sanchez,E.,
            Moreno-Rey,C., Real,L.M., Ramirez-Lorca,R. and Saez,M.E.
  TITLE     Identification of genetic factors associated with susceptibility to
            angiotensin-converting enzyme inhibitors-induced cough
  JOURNAL   Pharmacogenet Genomics 21 (1), 10-17 (2011)
   PUBMED   21052031
  REMARK    GeneRIF: Observational study of gene-disease association, gene-gene
            interaction, gene-environment interaction, and pharmacogenomic /
            toxicogenomic. (HuGE Navigator)
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Liu,T., Qian,W.J., Gritsenko,M.A., Camp,D.G. 2nd, Monroe,M.E.,
            Moore,R.J. and Smith,R.D.
  TITLE     Human plasma N-glycoproteome analysis by immunoaffinity
            subtraction, hydrazide chemistry, and mass spectrometry
  JOURNAL   J Proteome Res 4 (6), 2070-2080 (2005)
   PUBMED   16335952
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Bunkenborg,J., Pilch,B.J., Podtelejnikov,A.V. and Wisniewski,J.R.
  TITLE     Screening for N-glycosylated proteins by liquid chromatography mass
            spectrometry
  JOURNAL   Proteomics 4 (2), 454-465 (2004)
   PUBMED   14760718
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Riley,D.A., Tan,F., Miletich,D.J. and Skidgel,R.A.
  TITLE     Chromosomal localization of the genes for human carboxypeptidase D
            (CPD) and the active 50-kilodalton subunit of human
            carboxypeptidase N (CPN1)
  JOURNAL   Genomics 50 (1), 105-108 (1998)
   PUBMED   9628828
REFERENCE   7  (residues 1 to 545)
  AUTHORS   Tan,F., Weerasinghe,D.K., Skidgel,R.A., Tamei,H., Kaul,R.K.,
            Roninson,I.B., Schilling,J.W. and Erdos,E.G.
  TITLE     The deduced protein sequence of the human carboxypeptidase N high
            molecular weight subunit reveals the presence of leucine-rich
            tandem repeats
  JOURNAL   J Biol Chem 265 (1), 13-19 (1990)
   PUBMED   2378615
  REMARK    Erratum:[J Biol Chem 1990 Jul 25;265(21):12749]
REFERENCE   8  (residues 1 to 545)
  AUTHORS   Skidgel,R.A., Bennett,C.D., Schilling,J.W., Tan,F.L.,
            Weerasinghe,D.K. and Erdos,E.G.
  TITLE     Amino acid sequence of the N-terminus and selected tryptic peptides
            of the active subunit of human plasma carboxypeptidase N:
            comparison with other carboxypeptidases
  JOURNAL   Biochem Biophys Res Commun 154 (3), 1323-1329 (1988)
   PUBMED   3408501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC174158.3.
            
            On May 15, 2014 this sequence version replaced NP_001073982.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042334.1, BI762653.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2159080
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323830.4/ ENSP00000319464.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..545
                     /product="carboxypeptidase N subunit 2 precursor"
                     /EC_number="3.4.17.3"
                     /note="carboxypeptidase N, polypeptide 2, 83kD;
                     carboxypeptidase N large subunit; carboxypeptidase N 83
                     kDa chain; carboxypeptidase N regulatory subunit"
                     /calculated_mol_wt=58227
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2348
     Region          21..53
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     mat_peptide     22..545
                     /product="Carboxypeptidase N subunit 2.
                     /id=PRO_0000020989"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
                     /calculated_mol_wt=58227
     Region          30..53
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22792.3)"
     Region          75..98
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          95..419
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          98..119
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          99..122
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22792.3)"
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22792.3)"
     Region          122..143
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          123..146
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          146..167
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          147..170
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          170..191
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          171..194
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          194..215
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          195..218
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          218..239
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          219..242
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            228
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P22792.3)"
     Region          242..263
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          243..266
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          266..287
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Site            266
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22792.3)"
     Region          267..290
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          290..311
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          291..314
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          314..335
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          315..338
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          338..359
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          339..359
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718; propagated from
                     UniProtKB/Swiss-Prot (P22792.3)"
     Site            359
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718; propagated from
                     UniProtKB/Swiss-Prot (P22792.3)"
     Region          362..383
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P22792.3)"
     Region          363..382
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          387..399
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          395..446
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Site            518
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P22792.3)"
     CDS             1..545
                     /gene="CPN2"
                     /gene_synonym="ACBP"
                     /coded_by="NM_001080513.4:91..1728"
                     /db_xref="CCDS:CCDS33920.1"
                     /db_xref="GeneID:1370"
                     /db_xref="HGNC:HGNC:2313"
                     /db_xref="MIM:603104"
ORIGIN      
        1 mlpgawllwt sllllarpaq pcpmgcdcfv qevfcsdeel atvpldippy tkniifvets
       61 fttletrafg snpnltkvvf lntqlcqfrp dafgglprle dlevtgssfl nlstnifsnl
      121 tslgkltlnf nmlealpegl fqhlaalesl hlqgnqlqal prrlfqplth lktlnlaqnl
      181 laqlpeelfh pltslqtlkl snnalsglpq gvfgklgslq elfldsnnis elppqvfsql
      241 fclerlwlqr naithlplsi faslgnltfl slqwnmlrvl paglfahtpc lvglslthnq
      301 letvaegtfa hlsnlrslml synaithlpa gifrdleelv klylgsnnlt alhpalfqnl
      361 sklellslsk nqlttlpegi fdtnynlfnl alhgnpwqcd chlaylfnwl qqytdrllni
      421 qtycagpayl kgqvvpalne kqlvcpvtrd hlgfqvtwpd eskaggswdl avqeraarsq
      481 ctysnpegtv vlacdqaqcr wlnvqlspqq gslglqynas qewdlrsscg slrltvsiea
      541 raagp
//
LOCUS       NP_060034               2551 aa            linear   PRI 27-APR-2025
DEFINITION  stabilin-2 precursor [Homo sapiens].
ACCESSION   NP_060034
VERSION     NP_060034.9
DBSOURCE    REFSEQ: accession NM_017564.10
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2551)
  AUTHORS   Yu,W., Srivastava,R., Srivastava,S., Ma,Y., Shankar,S. and
            Srivastava,R.K.
  TITLE     Oncogenic Role of SATB2 In Vitro: Regulator of Pluripotency,
            Self-Renewal, and Epithelial-Mesenchymal Transition in Prostate
            Cancer
  JOURNAL   Cells 13 (11), 962 (2024)
   PUBMED   38891096
  REMARK    GeneRIF: Oncogenic Role of SATB2 In Vitro: Regulator of
            Pluripotency, Self-Renewal, and Epithelial-Mesenchymal Transition
            in Prostate Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2551)
  AUTHORS   Jo,H.S. and Kim,H.J.
  TITLE     Stabilin-2 mediated apoptotic cell phagocytosis induces
            interleukin-10 expression by p38 and Pbx1 signaling
  JOURNAL   Cell Biochem Biophys 82 (2), 919-925 (2024)
   PUBMED   38480573
  REMARK    GeneRIF: Stabilin-2 mediated apoptotic cell phagocytosis induces
            interleukin-10 expression by p38 and Pbx1 signaling.
REFERENCE   3  (residues 1 to 2551)
  AUTHORS   Li,J., Zeng,Q., Lin,J., Huang,H. and Chen,L.
  TITLE     Loss of SATB2 and CDX2 expression is associated with DNA mismatch
            repair protein deficiency and BRAF mutation in colorectal cancer
  JOURNAL   Med Mol Morphol 57 (1), 1-10 (2024)
   PUBMED   37583001
  REMARK    GeneRIF: Loss of SATB2 and CDX2 expression is associated with DNA
            mismatch repair protein deficiency and BRAF mutation in colorectal
            cancer.
REFERENCE   4  (residues 1 to 2551)
  AUTHORS   Holte,C., Szafranska,K., Kruse,L., Simon-Santamaria,J., Li,R.,
            Svistounov,D. and McCourt,P.
  TITLE     Highly oxidized albumin is cleared by liver sinusoidal endothelial
            cells via the receptors stabilin-1 and -2
  JOURNAL   Sci Rep 13 (1), 19121 (2023)
   PUBMED   37926735
  REMARK    GeneRIF: Highly oxidized albumin is cleared by liver sinusoidal
            endothelial cells via the receptors stabilin-1 and -2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2551)
  AUTHORS   Xin,T., Li,Q., Bai,R., Zhang,T., Zhou,Y., Zhang,Y., Han,B. and
            Yang,R.
  TITLE     A novel mutation of SATB2 inhibits odontogenesis of human dental
            pulp stem cells through Wnt/beta-catenin signaling pathway
  JOURNAL   Stem Cell Res Ther 12 (1), 595 (2021)
   PUBMED   34863303
  REMARK    GeneRIF: A novel mutation of SATB2 inhibits odontogenesis of human
            dental pulp stem cells through Wnt/beta-catenin signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2551)
  AUTHORS   Smedsrod,B., Johansson,S. and Goerdt,S.
  TITLE     Shooting HARE
  JOURNAL   Glycobiology 13 (5), 11G-12G (2003)
   PUBMED   12751488
REFERENCE   7  (residues 1 to 2551)
  AUTHORS   Zhou,B., McGary,C.T., Weigel,J.A., Saxena,A. and Weigel,P.H.
  TITLE     Purification and molecular identification of the human hyaluronan
            receptor for endocytosis
  JOURNAL   Glycobiology 13 (5), 339-349 (2003)
   PUBMED   12626425
  REMARK    GeneRIF: amino acid sequence of 190-kDa protein composed of 1416
            amino acids and alignment with rat sequence
REFERENCE   8  (residues 1 to 2551)
  AUTHORS   Tamura,Y., Adachi,H., Osuga,J., Ohashi,K., Yahagi,N., Sekiya,M.,
            Okazaki,H., Tomita,S., Iizuka,Y., Shimano,H., Nagai,R., Kimura,S.,
            Tsujimoto,M. and Ishibashi,S.
  TITLE     FEEL-1 and FEEL-2 are endocytic receptors for advanced glycation
            end products
  JOURNAL   J Biol Chem 278 (15), 12613-12617 (2003)
   PUBMED   12473645
REFERENCE   9  (residues 1 to 2551)
  AUTHORS   Adachi,H. and Tsujimoto,M.
  TITLE     FEEL-1, a novel scavenger receptor with in vitro bacteria-binding
            and angiogenesis-modulating activities
  JOURNAL   J Biol Chem 277 (37), 34264-34270 (2002)
   PUBMED   12077138
REFERENCE   10 (residues 1 to 2551)
  AUTHORS   Politz,O., Gratchev,A., McCourt,P.A., Schledzewski,K., Guillot,P.,
            Johansson,S., Svineng,G., Franke,P., Kannicht,C., Kzhyshkowska,J.,
            Longati,P., Velten,F.W., Johansson,S. and Goerdt,S.
  TITLE     Stabilin-1 and -2 constitute a novel family of fasciclin-like
            hyaluronan receptor homologues
  JOURNAL   Biochem J 362 (Pt 1), 155-164 (2002)
   PUBMED   11829752
  REMARK    GeneRIF: code for homologous transmembrane proteins featuring seven
            fasciclin-like adhesion domains, 18-20 epidermal-growth-factor
            domains, one X-link domain and three to six B-(X(7))-B
            hyaluronan-binding motifs
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC084364.20 and AY311388.1.
            
            On Mar 24, 2005 this sequence version replaced NP_060034.8.
            
            Summary: This gene encodes a large, transmembrane receptor protein
            which may function in angiogenesis, lymphocyte homing, cell
            adhesion, or receptor scavenging. The protein contains 7 fasciclin,
            15 epidermal growth factor (EGF)-like, and 2 laminin-type EGF-like
            domains as well as a C-type lectin-like hyaluronan-binding Link
            module. The protein is primarily expressed on sinusoidal
            endothelial cells of liver, spleen, and lymph node. The receptor
            has been shown to bind and endocytose ligands such as hyaluronan,
            low density lipoprotein, Gram-positive and Gram-negative bacteria,
            and advanced glycosylation end products. Supporting its possible
            role as a scavenger receptor, the protein has been shown to cycle
            between the plasma membrane and lysosomes. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY311388.1, AJ295695.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000388887.7/ ENSP00000373539.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..2551
                     /product="stabilin-2 precursor"
                     /note="hyaluronic acid receptor for endocytosis; FAS1
                     EGF-like and X-link domain containing adhesion molecule-2;
                     fasciclin egf-like, laminin-type egf-like, and link
                     domain-containing scavenger receptor-2; CD44-like
                     precursor FELL; hepatic hyaluronan clearance receptor;
                     hyaluronan receptor for endocytosis"
                     /calculated_mol_wt=274799
     sig_peptide     1..19
                     /calculated_mol_wt=2209
     mat_peptide     20..2551
                     /product="stabilin-2"
                     /calculated_mol_wt=274799
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          246..275
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Region          326..361
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          382..505
                     /region_name="Fasciclin"
                     /note="Fasciclin domain; pfam02469"
                     /db_xref="CDD:396845"
     Site            449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          526..654
                     /region_name="Fasciclin"
                     /note="Fasciclin domain; pfam02469"
                     /db_xref="CDD:396845"
     Site            619
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            720
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            761
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          837..865
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Site            847
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          876..908
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Region          920..951
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Site            925
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          957..993
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Region          1009..1129
                     /region_name="Fasciclin"
                     /note="Fasciclin domain; pfam02469"
                     /db_xref="CDD:396845"
     Site            1016
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            1028
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            1100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     mat_peptide     1136..2551
                     /product="190 kDa form stabilin-2"
                     /exception="alternative processing"
                     /calculated_mol_wt=154043
     Region          1148..1265
                     /region_name="Fasciclin"
                     /note="Fasciclin domain; pfam02469"
                     /db_xref="CDD:396845"
     Site            1247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            1275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            1367
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            1429
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          1437..1469
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Site            1437
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            1465
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          1475..1511
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Region          1517..1553
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Region          1559..1595
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Site            1573
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          1617..1726
                     /region_name="Fasciclin"
                     /note="Fasciclin domain; pfam02469"
                     /db_xref="CDD:396845"
     Site            1679
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            1743
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          1752..1882
                     /region_name="Fasciclin"
                     /note="Fasciclin domain; pfam02469"
                     /db_xref="CDD:396845"
     Site            1993
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            2064
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          2086..2121
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Region          2127..2164
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Region          2198..2290
                     /region_name="Link_domain_TSG_6_like"
                     /note="This is the extracellular link domain of the type
                     found in human TSG-6. The link domain is a hyaluronan
                     (HA)-binding domain. TSG-6 is the protein product of tumor
                     necrosis factor-stimulated gene-6. TSG-6 is up-regulated
                     in inflammatory lesions and in the...; cd03515"
                     /db_xref="CDD:239592"
     Site            order(2208..2209,2256,2267,2275)
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239592"
     Site            2280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            2296
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            2336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          2356..2449
                     /region_name="FAS1"
                     /note="Four repeated domains in the Fasciclin I family of
                     proteins, present in many other contexts; smart00554"
                     /db_xref="CDD:214719"
     Site            2368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            2382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            2393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            2459..2479
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Site            2497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          2504..2514
                     /region_name="Interaction with TMSB4X.
                     /evidence=ECO:0000269|PubMed:18519035"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     Region          2512..2551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWQ8.3)"
     CDS             1..2551
                     /gene="STAB2"
                     /gene_synonym="FEEL2; FELE-2; FELL2; FEX2; HARE; SCARH1"
                     /coded_by="NM_017564.10:205..7860"
                     /db_xref="CCDS:CCDS31888.1"
                     /db_xref="GeneID:55576"
                     /db_xref="HGNC:HGNC:18629"
                     /db_xref="MIM:608561"
ORIGIN      
        1 mmlqhlvifc lglvvqnfcs paettgqarr cdrkslltir tecrscalnl gvkcpdgytm
       61 itsgsvgvrd crytfevrty slslpgcrhi crkdylqprc cpgrwgpdci ecpggagspc
      121 ngrgscaegm egngtcscqe gfggtacetc addnlfgpsc ssvcncvhgv cnsgldgdgt
      181 cecysaytgp kcdkpipeca allcpensrc spstedenkl eckclpnyrg dgkycdpinp
      241 clrkichpha hctylgpnrh sctcqegyrg dgqvclpvdp cqinfgncpt kstvckydgp
      301 gqshceckeh yqnfvpgvgc smtdicksdn pchrnanctt vapgrtecic qkgyvgdglt
      361 cygnimerlr elnteprgkw qgrltsfisl ldkayawpls klgpftvllp tdkglkgfnv
      421 nellvdnkaa qyfvklhiia gqmnieymnn tdmfytltgk sgeifnsdkd nqiklklhgg
      481 kkkvkiiqgd iiasngllhi ldramdklep tfesnneqti mtmlqprysk frslleetnl
      541 ghaldedgvg gpytifvpnn ealnnmkdgt ldyllspegs rkllelvryh ivpftqleva
      601 tlistphirs manqliqfnt tdngqiland vameeieita kngriytltg vlippsivpi
      661 lphrcdetkr emklgtcvsc slvywsrcpa nseptalfth rcvysgrfgs lksgcarycn
      721 atvkipkcck gfygpdcnqc pggfsnpcsg ngqcadslgg ngtciceegf qgsqcqfcsd
      781 pnkygprcnk kclcvhgtcn nridsdgacl tgtcrdgsag rlcdkqtsac gpyvqfchih
      841 atceysngta scickagyeg dgtlcsemdp ctgltpggcs rnaeciktgt gthtcvcqqg
      901 wtgngrdcse inncllpsag gchdnascly vgpgqnecec kkgfrgngid cepitscleq
      961 tgkchplasc qstssgvwsc vcqegyegdg flcygnaave lsflseaaif nrwinnaslq
     1021 ptlsatsnlt vlvpsqqate dmdqdeksfw lsqsnipali kyhmllgtyr vadlqtlsss
     1081 dmlatslqgn flhlakvdgn itiegasivd gdnaatngvi hiinkvlvpq rrltgslpnl
     1141 lmrleqmpdy sifrgyiiqy nlanaieaad aytvfapnnn aienyirekk vlsleedvlr
     1201 yhvvleekll kndlhngmhr etmlgfsyfl sfflhndqly vneapinytn vatdkgvihg
     1261 lgkvleiqkn rcdnndttii rgrcrtcsse ltcpfgtksl gnekrrciyt syfmgrrtlf
     1321 igcqpkcvrt vitreccagf fgpqcqpcpg naqnvcfgng icldgvngtg vcecgegfsg
     1381 tacetctegk ygihcdqacs cvhgrcnqgp lgdgscdcdv gwrgvhcdna ttedncngtc
     1441 htsancltns dgtasckcaa gfqgngtict ainaceisng gcsakadckr ttpgrrvctc
     1501 kagytgdgiv cleinpclen hggcdknaec tqtgpnqaac nclpaytgdg kvctlinvcl
     1561 tknggcsefa icnhtgqver tctckpnyig dgftcrgsiy qelpknpkts qyffqlqehf
     1621 vkdlvgpgpf tvfaplsaaf deearvkdwd kyglmpqvlr yhvvachqll lenlklisna
     1681 tslqgepivi svsqstvyin nkakiissdi istngivhii dkllspknll itpkdnsgri
     1741 lqnlttlatn ngyikfsnli qdsgllsvit dpihtpvtlf wptdqalhal paeqqdflfn
     1801 qdnkdklkey lkfhvirdak vlavdlptst awktlqgsel svkcgagrdi gdlflngqtc
     1861 rivqrellfd lgvaygidcl lidptlggrc dtfttfdasg ecgscvntps cprwskpkgv
     1921 kqkclynlpf krnlegcrer cslviqiprc ckgyfgrdcq acpggpdapc nnrgvcldqy
     1981 satgeckcnt gfngtacemc wpgrfgpdcl pcgcsdhgqc ddgitgsgqc lcetgwtgps
     2041 cdtqavlpav ctppcsahat ckenntcecn ldyegdgitc tvvdfckqdn ggcakvarcs
     2101 qkgtkvscsc qkgykgdghs cteidpcadg lnggchehat ckmtgpgkhk ceckshyvgd
     2161 glncepeqlp idrclqdngq chadakcvdl hfqdttvgvf hlrsplgqyk ltfdkareac
     2221 aneaatmaty nqlsyaqkak yhlcsagwle tgrvayptaf asqncgsgvv givdygprpn
     2281 ksemwdvfcy rmkdvnctck vgyvgdgfsc sgnllqvlms fpsltnflte vlaysnssar
     2341 graflehltd lsirgtlfvp qnsglgenet lsgrdiehhl anvsmffynd lvngttlqtr
     2401 lgskllitas qdplqptetr fvdgrailqw difasngiih visrplkapp apvtlthtgl
     2461 gagiffaiil vtgavalaay syfrinrrti gfqhfeseed invaalgkqq penisnplye
     2521 sttsappeps ydpftdseer qlegndplrt l
//
LOCUS       NP_004413                736 aa            linear   PRI 27-APR-2025
DEFINITION  segment polarity protein dishevelled homolog DVL-2 [Homo sapiens].
ACCESSION   NP_004413
VERSION     NP_004413.1
DBSOURCE    REFSEQ: accession NM_004422.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Omble,A., Mahajan,S., Bhoite,A. and Kulkarni,K.
  TITLE     Dishevelled2 activates WGEF via its interaction with a unique
            internal peptide motif of the GEF
  JOURNAL   Commun Biol 7 (1), 543 (2024)
   PUBMED   38714795
  REMARK    GeneRIF: Dishevelled2 activates WGEF via its interaction with a
            unique internal peptide motif of the GEF.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 736)
  AUTHORS   He,R., Chen,Y., Qian,C., Hu,Y., Huang,X. and Tao,R.
  TITLE     Dishevelled segment polarity protein 2 promotes gastric cancer
            progression through Wnt/beta-catenin pathway
  JOURNAL   Tissue Cell 82, 102119 (2023)
   PUBMED   37257286
  REMARK    GeneRIF: Dishevelled segment polarity protein 2 promotes gastric
            cancer progression through Wnt/beta-catenin pathway.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Demirci,U., Orenay-Boyacioglu,S., Kasap,E., Gerceker,E., Bilgic,F.,
            Yuceyar,H., Yildirim,H., Baykan,A.R., Ellidokuz,E.B. and Korkmaz,M.
  TITLE     Overexpressions of RHOA, CSNK1A1, DVL2, FZD8, and LRP5 genes
            enhance gastric cancer development in the presence of Helicobacter
            pylori
  JOURNAL   Arab J Gastroenterol 24 (2), 91-97 (2023)
   PUBMED   36720664
  REMARK    GeneRIF: Overexpressions of RHOA, CSNK1A1, DVL2, FZD8, and LRP5
            genes enhance gastric cancer development in the presence of
            Helicobacter pylori.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Shen,J., Zha,Q., Yang,Q.H., Zhou,Y.Q., Liang,X., Chen,Y.J.,
            Qi,G.X., Zhang,X.J., Yao,W.B., Gao,X.D. and Chen,S.
  TITLE     Inhibiting von Hippel-Lindau protein-mediated Dishevelled
            ubiquitination protects against experimental parkinsonism
  JOURNAL   Acta Pharmacol Sin 44 (5), 940-953 (2023)
   PUBMED   36357669
  REMARK    GeneRIF: Inhibiting von Hippel-Lindau protein-mediated Dishevelled
            ubiquitination protects against experimental parkinsonism.
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Kang,K., Shi,Q., Wang,X. and Chen,Y.G.
  TITLE     Dishevelled phase separation promotes Wnt signalosome assembly and
            destruction complex disassembly
  JOURNAL   J Cell Biol 221 (12) (2022)
   PUBMED   36342472
  REMARK    GeneRIF: Dishevelled phase separation promotes Wnt signalosome
            assembly and destruction complex disassembly.
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Strovel,E.T., Wu,D. and Sussman,D.J.
  TITLE     Protein phosphatase 2Calpha dephosphorylates axin and activates
            LEF-1-dependent transcription
  JOURNAL   J Biol Chem 275 (4), 2399-2403 (2000)
   PUBMED   10644691
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Semenov,M.V. and Snyder,M.
  TITLE     Human dishevelled genes constitute a DHR-containing multigene
            family
  JOURNAL   Genomics 42 (2), 302-310 (1997)
   PUBMED   9192851
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Klingensmith,J., Yang,Y., Axelrod,J.D., Beier,D.R., Perrimon,N. and
            Sussman,D.J.
  TITLE     Conservation of dishevelled structure and function between flies
            and mice: isolation and characterization of Dvl2
  JOURNAL   Mech Dev 58 (1-2), 15-26 (1996)
   PUBMED   8887313
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Pizzuti,A., Amati,F., Calabrese,G., Mari,A., Colosimo,A.,
            Silani,V., Giardino,L., Ratti,A., Penso,D., Calza,L., Palka,G.,
            Scarlato,G., Novelli,G. and Dallapiccola,B.
  TITLE     cDNA characterization and chromosomal mapping of two human
            homologues of the Drosophila dishevelled polarity gene
  JOURNAL   Hum Mol Genet 5 (7), 953-958 (1996)
   PUBMED   8817329
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Greco,T.L., Sussman,D.J. and Camper,S.A.
  TITLE     Dishevelled-2 maps to human chromosome 17 and distal to Wnt3a and
            vestigial tail (vt) on mouse chromosome 11
  JOURNAL   Mamm Genome 7 (6), 475-476 (1996)
   PUBMED   8662242
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG716400.1, CB994349.1,
            BC014844.1 and AK026019.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the dishevelled (dsh)
            protein family. The vertebrate dsh proteins have approximately 40%
            amino acid sequence similarity with Drosophila dsh. This gene
            encodes a 90-kD protein that undergoes posttranslational
            phosphorylation to form a 95-kD cytoplasmic protein, which may play
            a role in the signal transduction pathway mediated by multiple Wnt
            proteins. The mechanisms of dishevelled function in Wnt signaling
            are likely to be conserved among metazoans. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014844.1, SRR1660803.149730.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000005340.10/ ENSP00000005340.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..736
                     /product="segment polarity protein dishevelled homolog
                     DVL-2"
                     /note="dishevelled 2 (homologous to Drosophila dsh);
                     dishevelled, dsh homolog 2"
                     /calculated_mol_wt=78817
     Region          13..93
                     /region_name="DAX"
                     /note="Domain present in Dishevelled and axin; smart00021"
                     /db_xref="CDD:197474"
     Region          92..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14641.1)"
     Region          125..263
                     /region_name="Dishevelled"
                     /note="Dishevelled specific domain; pfam02377"
                     /db_xref="CDD:460544"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O14641.1)"
     Region          250..355
                     /region_name="Required for interaction with FOXK2.
                     /evidence=ECO:0000269|PubMed:25805136"
                     /note="propagated from UniProtKB/Swiss-Prot (O14641.1)"
     Region          267..353
                     /region_name="PDZ_Dishevelled-like"
                     /note="PDZ domain of segment polarity protein dishevelled
                     homolog DVL1, DVL2, DVL3, and related domains; cd06717"
                     /db_xref="CDD:467201"
     Site            order(277..283,297,300,330,334,337..338)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467201"
     Region          424..507
                     /region_name="DEP_dishevelled"
                     /note="DEP (Dishevelled, Egl-10, and Pleckstrin) domain
                     found in dishevelled-like proteins. Dishevelled-like
                     proteins play a key role in the transduction of the Wnt
                     signal from the cell surface to the nucleus, which in turn
                     is an important regulatory pathway...; cd04438"
                     /db_xref="CDD:239885"
     Region          515..726
                     /region_name="Dsh_C"
                     /note="Segment polarity protein dishevelled (Dsh) C
                     terminal; pfam12316"
                     /db_xref="CDD:463531"
     Region          558..675
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14641.1)"
     CDS             1..736
                     /gene="DVL2"
                     /coded_by="NM_004422.3:256..2466"
                     /db_xref="CCDS:CCDS11091.1"
                     /db_xref="GeneID:1856"
                     /db_xref="HGNC:HGNC:3086"
                     /db_xref="MIM:602151"
ORIGIN      
        1 magsstgggg vgetkviyhl deeetpylvk ipvpaeritl gdfksvlqrp agakyffksm
       61 dqdfgvvkee isddnarlpc fngrvvswlv ssdnpqpema ppvheprael appapplppl
      121 ppertsgigd srppsfhpnv ssshenlepe tetesvvslr rerprrrdss ehgagghrtg
      181 gpsrlerhla gyessstlmt selestslgd sdeedtmsrf sssteqssas rllkrhrrrr
      241 kqrpprlert ssfssvtdst mslniitvtl nmekynflgi sivgqsnerg dggiyigsim
      301 kggavaadgr iepgdmllqv ndmnfenmsn ddavrvlrdi vhkpgpivlt vakcwdpspq
      361 ayftlprnep iqpidpaawv shsaaltgtf paypgsssms titsgsslpd gcegrglsvh
      421 tdmasvtkam aapesglevr drmwlkitip naflgsdvvd wlyhhvegfp errearkyas
      481 gllkaglirh tvnkitfseq cyyvfgdlsg gcesylvnls lndndgssga sdqdtlaplp
      541 gatpwpllpt fsyqypaphp yspqpppyhe lssytygggs assqhsegsr ssgstrsdgg
      601 agrtgrpeer apesksgsgs esepssrggs lrrggeasgt sdggpppsrg stggapnlra
      661 hpglhpygpp pgmalpynpm mvvmmppppp pvppavqppg appvrdlgsv ppeltasrqs
      721 fhmamgnpse ffvdvm
//
LOCUS       NP_066015               2579 aa            linear   PRI 27-APR-2025
DEFINITION  ectopic P granules protein 5 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_066015 XP_038864
VERSION     NP_066015.2
DBSOURCE    REFSEQ: accession NM_020964.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2579)
  AUTHORS   Vansenne,F., Fock,J.M., Stolte-Dijkstra,I., Meiners,L.C., van den
            Boogaard,M.H., Jaeger,B., Boven,L., Vos,Y.J., Sinke,R.J. and
            Verbeek,D.S.
  TITLE     Phenotypic expansion of EGP5-related Vici syndrome: 15 Dutch
            patients carrying a founder variant
  JOURNAL   Eur J Paediatr Neurol 41, 91-98 (2022)
   PUBMED   36410285
  REMARK    GeneRIF: Phenotypic expansion of EGP5-related Vici syndrome: 15
            Dutch patients carrying a founder variant.
REFERENCE   2  (residues 1 to 2579)
  AUTHORS   Schwertz,H., Rowley,J.W., Portier,I., Middleton,E.A., Tolley,N.D.,
            Campbell,R.A., Eustes,A.S., Chen,K. and Rondina,M.T.
  TITLE     Human platelets display dysregulated sepsis-associated autophagy,
            induced by altered LC3 protein-protein interaction of the
            Vici-protein EPG5
  JOURNAL   Autophagy 18 (7), 1534-1550 (2022)
   PUBMED   34689707
  REMARK    GeneRIF: Human platelets display dysregulated sepsis-associated
            autophagy, induced by altered LC3 protein-protein interaction of
            the Vici-protein EPG5.
REFERENCE   3  (residues 1 to 2579)
  AUTHORS   Rafei,M.A., Harikrishna,B., Al Thihli,K., Al-Mujaini,A.S. and
            Ganesh,A.
  TITLE     Ophthalmic findings as clues for early diagnosis of Vici syndrome
            in a neonate
  JOURNAL   Ophthalmic Genet 42 (6), 780-783 (2021)
   PUBMED   34264147
  REMARK    GeneRIF: Ophthalmic findings as clues for early diagnosis of Vici
            syndrome in a neonate.
REFERENCE   4  (residues 1 to 2579)
  AUTHORS   Nam,S.E., Cheung,Y.W.S., Nguyen,T.N., Gong,M., Chan,S., Lazarou,M.
            and Yip,C.K.
  TITLE     Insights on autophagosome-lysosome tethering from structural and
            biochemical characterization of human autophagy factor EPG5
  JOURNAL   Commun Biol 4 (1), 291 (2021)
   PUBMED   33674710
  REMARK    GeneRIF: Insights on autophagosome-lysosome tethering from
            structural and biochemical characterization of human autophagy
            factor EPG5.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2579)
  AUTHORS   Ehmke,N., Parvaneh,N., Krawitz,P., Ashrafi,M.R., Karimi,P.,
            Mehdizadeh,M., Kruger,U., Hecht,J., Mundlos,S. and Robinson,P.N.
  TITLE     First description of a patient with Vici syndrome due to a mutation
            affecting the penultimate exon of EPG5 and review of the literature
  JOURNAL   Am J Med Genet A 164A (12), 3170-3175 (2014)
   PUBMED   25331754
  REMARK    GeneRIF: A mutation affecting the penultimate exon of EPG5 and
            presenting with typical clinical manifestations of Vici syndrome.
            Review article
REFERENCE   6  (residues 1 to 2579)
  AUTHORS   Cullup,T., Dionisi-Vici,C., Kho,A.L., Yau,S., Mohammed,S.,
            Gautel,M. and Jungbluth,H.
  TITLE     Clinical utility gene card for: Vici Syndrome
  JOURNAL   Eur J Hum Genet 22 (3) (2014)
   PUBMED   23838600
REFERENCE   7  (residues 1 to 2579)
  AUTHORS   Cullup,T., Kho,A.L., Dionisi-Vici,C., Brandmeier,B., Smith,F.,
            Urry,Z., Simpson,M.A., Yau,S., Bertini,E., McClelland,V.,
            Al-Owain,M., Koelker,S., Koerner,C., Hoffmann,G.F., Wijburg,F.A.,
            ten Hoedt,A.E., Rogers,R.C., Manchester,D., Miyata,R., Hayashi,M.,
            Said,E., Soler,D., Kroisel,P.M., Windpassinger,C., Filloux,F.M.,
            Al-Kaabi,S., Hertecant,J., Del Campo,M., Buk,S., Bodi,I.,
            Goebel,H.H., Sewry,C.A., Abbs,S., Mohammed,S., Josifova,D.,
            Gautel,M. and Jungbluth,H.
  TITLE     Recessive mutations in EPG5 cause Vici syndrome, a multisystem
            disorder with defective autophagy
  JOURNAL   Nat Genet 45 (1), 83-87 (2013)
   PUBMED   23222957
  REMARK    GeneRIF: Recessive mutations in EPG5 cause Vici syndrome, a
            multisystem disorder with defective autophagy.
REFERENCE   8  (residues 1 to 2579)
  AUTHORS   Tian,Y., Li,Z., Hu,W., Ren,H., Tian,E., Zhao,Y., Lu,Q., Huang,X.,
            Yang,P., Li,X., Wang,X., Kovacs,A.L., Yu,L. and Zhang,H.
  TITLE     C. elegans screen identifies autophagy genes specific to
            multicellular organisms
  JOURNAL   Cell 141 (6), 1042-1055 (2010)
   PUBMED   20550938
REFERENCE   9  (residues 1 to 2579)
  AUTHORS   Halama,N., Grauling-Halama,S.A., Beder,A. and Jager,D.
  TITLE     Comparative integromics on the breast cancer-associated gene
            KIAA1632: clues to a cancer antigen domain
  JOURNAL   Int J Oncol 31 (1), 205-210 (2007)
   PUBMED   17549423
  REMARK    GeneRIF: We characterized the KIAA1632 gene by computational
            methods: detailed investigation of the genomic structure, protein
            prediction, identification of orthologs in other species and
            phylogenetic analysis.
REFERENCE   10 (residues 1 to 2579)
  AUTHORS   Dafsari,H.S., Ebrahimi-Fakhari,D., Saffari,A., Deneubourg,C.,
            Fanto,M. and Jungbluth,H.
  TITLE     EPG5-Related Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36228046
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB065073.1, AB046852.1,
            AC090355.9, AK023817.1, DB235183.1, BC003695.1, AC087685.9 and
            BM680107.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 22, 2006 this sequence version replaced NP_066015.1.
            
            Summary: This gene encodes a large coiled coil domain-containing
            protein that functions in autophagy during starvation conditions.
            Mutations in this gene cause Vici syndrome. [provided by RefSeq,
            Aug 2015].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            CCDS Note: The coding region has been updated to include additional
            exons at both the 5' and 3' ends, resulting in an extension of both
            the N- and C-termini. There are no full-length human transcripts
            representing this gene, but the update is supported by available
            overlapping partial transcripts, by conservation data, and by data
            included in PMID:17549423.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000282041.11/ ENSP00000282041.4
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2579
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.3-q21.1"
     Protein         1..2579
                     /product="ectopic P granules protein 5 homolog isoform 1"
                     /note="ectopic P-granules autophagy protein 5 homolog"
                     /calculated_mol_wt=292351
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE0.2)"
     Region          92..132
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE0.2)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCE0.2)"
     Region          535..564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE0.2)"
     CDS             1..2579
                     /gene="EPG5"
                     /gene_synonym="HEEW1; KIAA1632; VICIS"
                     /coded_by="NM_020964.3:91..7830"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11926.2"
                     /db_xref="GeneID:57724"
                     /db_xref="HGNC:HGNC:29331"
                     /db_xref="MIM:615068"
ORIGIN      
        1 maeavkpqrr akakasrtkt kekkkyetpq reessevslp ktsreqeips lacefkgdhl
       61 kvvtdsqlqd dasgqnesem fdvpltslti sneesltcnt eppkeggear pcvgdsavtp
      121 kvhpgdnvgt kvetpknfte veenmsvqgg lsesapqsnf sytqpameni qvretqnske
      181 dkqglvcsse vpqnvglqss cpakhgfqtp rvkklypqlp aeiageapal vavkpllrse
      241 rlypelpsql elvpftkeql kilepgswle nvesyleefd smahqdrhef yelllnysrc
      301 rkqlllaeae lltltsdcqn aksrlwqfke eqmsvqgica dqvkvfsyhr yqrvemnena
      361 lvelkklfda ksehlhqtla lhsytsvlsr lqvesyiyal lsssavlrss aihqqgrask
      421 qtesipsdlc qlkecisvlf mftrrvnedt qfhddillwl qklvsvlqrv gcpgdhlfll
      481 nhilrcpagv skwavpfiqi kvlhnpsgvf hfmqslallm spvknraefm chmkpserkp
      541 sssgpgsgtw tlvdeggeed edpetswill neddlvtila qfpfhelfqh llgfkakgdy
      601 lpettrpqem mkifafansl vellavglet fnraryrqfv krigymirmt lgyvsdhwaq
      661 yvshnqgsgl aqqpysmekl qvefdelflr avlhvlkakr lgiwlfmsem pfgtlsvqml
      721 wklfylmhqv esenlqqlss slqpaqckqq lqdpehftnf ekclssmnss eeicllttfa
      781 qmaqarrtnv dedfikiivl eiyevsyvtl stretfskvg rellgtitav hpeiisvlld
      841 rvqetidqvg mvslylfkel plylwqpsas eiavirdwll nynltvvknk lacvilegln
      901 wgfakqatlh ldqavhaeva lmvleayqky laqkpyagil sesmkqvsyl asivrygetp
      961 etsfnqwawn lilrlklhkn dygiqpncpa vpfsvtvpdm tesptfhpll kavkagmpig
     1021 cylalsmtav ghsiekfcae gipllgilvq srhlrtvvhv ldkilplfyp cqyyllkneq
     1081 flshlllflh ldsgvpqgvt qqvthkvaqh ltgashgdnv kllnsmiqah isvstqpnev
     1141 gpvavlefwv qalisqhlwy reqpilflmd hlckaafqlm qedciqklly qqhknalgyh
     1201 cdrsllsslv swivagnitp sfveglatpt qvwfawtvln mesifeedsq lrrviegelv
     1261 insaftpdqa lkkaqtqlkl pivpslqrll iyrwahqalv tpsdhpllpl iwqkffllyl
     1321 hrpgpqyglp idgcigrrff qspahinllk emkrrlteva dfhhaaskal rvpaegsegl
     1381 peshsgtpgy ltspelhkel vrlfnvyilw ledenfqkgd tyipslpkhy dihrlakvmq
     1441 nqqdlwmeyl nmeriyhefq etvglwtqak leshstpcsl svqldftdpl lakervlsnl
     1501 rkheapqppl alhptkppvp vissavllsq kdatqlvctd lnllqqqart aalresqqva
     1561 ldgelldtmp kqyvnreeqt tlhlecrgss gkkcqgaavv tvqfegmhkn eaisqqlhvl
     1621 rkevkqlqae aakppslniv eaavhaenli talvnayklq ptpgiqkvgi slfftivdyv
     1681 sdetqrhppt rqfftsciei lgqvfisgik secrkvleti lknsrlcsll spfftpnaap
     1741 aefiqlyeqv vkflsednsd mifmlltkfd lkqwlsatkp plsdrtrlle sihlaltawg
     1801 lepdedilmp fnlfckhwty lllyqfpdqy sdilrllmqs saeqllspec wkatlralgc
     1861 capscqqgaa stegavlpss sdallsdkqv metiqwlsdf fyklrlskmd fksfglfskw
     1921 spymadvktf lgylvkrlid lemtclaqdp tasrktvlks lhsviiqlfk pwilvledne
     1981 ssqqrhypwl esdtvvassi vqlftdcids lhesfkdkll pgdagalwlh lmhyceacta
     2041 pkmpefilya fhstyrklpw kdlhpdqmlm eaffkvergs pkscflflgs vlcevnwvsv
     2101 lsdawnssph petrsmivcl lfmmillake vqlvdqtdsp llsllgqtss lswhlvdivs
     2161 yqsvlsyfss hyppsiilak esyaelimkl lkvsaglsip tdsqkhldav pkcqafthqm
     2221 vqflstleqn gkitlavleq emskllddii vfnppdmdsq trhmalsslf mevlmmmnna
     2281 tiptaeflrg sirtwigqkm hglvvlpllt aacqslasvr hmaetteaci tayfkespln
     2341 qnsgwgpilv slqvpeltme eflqecltlg syltlyvyll qclnseqtlr nemkvllils
     2401 kwleqvypss veeeaklflw whqvlqlsli qteqndsvlt esvirilllv qsrqnlvaee
     2461 rlssgilgai gfgrksplsn rfrvvarsma aflsvqvpme dqirlrpgse lhltpkaqqa
     2521 lnalesmass kqyveyqdqi lqatqfirhp ghclqdgksf lallvnclyp evhyldhir
//
LOCUS       NP_001355203             106 aa            linear   ROD 27-APR-2025
DEFINITION  small membrane A-kinase anchor protein [Mus musculus].
ACCESSION   NP_001355203 XP_011236868
VERSION     NP_001355203.1
DBSOURCE    REFSEQ: accession NM_001368274.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Shalom-Barak,T., Zhang,X., Chu,T., Timothy Schaiff,W., Reddy,J.K.,
            Xu,J., Sadovsky,Y. and Barak,Y.
  TITLE     Placental PPARgamma regulates spatiotemporally diverse genes and a
            unique metabolic network
  JOURNAL   Dev Biol 372 (1), 143-155 (2012)
   PUBMED   22967998
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Thiagarajan,R.D., Georgas,K.M., Rumballe,B.A., Lesieur,E.,
            Chiu,H.S., Taylor,D., Tang,D.T., Grimmond,S.M. and Little,M.H.
  TITLE     Identification of anchor genes during kidney development defines
            ontological relationships, molecular subcompartments and regulatory
            pathways
  JOURNAL   PLoS One 6 (2), e17286 (2011)
   PUBMED   21386911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Lin,Q., Donahue,S.L., Moore-Jarrett,T., Cao,S., Osipovich,A.B. and
            Ruley,H.E.
  TITLE     Mutagenesis of diploid mammalian genes by gene entrapment
  JOURNAL   Nucleic Acids Res 34 (20), e139 (2006)
   PUBMED   17062627
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU961456.1 and AC129337.4.
            
            On Feb 2, 2019 this sequence version replaced XP_011236868.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU961456.1, CN833178.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 26.99 cM"
     Protein         1..106
                     /product="small membrane A-kinase anchor protein"
                     /note="UPF0733 protein C2orf88 homolog; small membrane
                     AKAP"
                     /calculated_mol_wt=11795
     Region          1..100
                     /region_name="SmAKAP"
                     /note="Small membrane A-kinase anchor protein; pfam15127"
                     /db_xref="CDD:464517"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CPS8.1)"
     Region          62..85
                     /region_name="PKA-RI-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CPS8.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BSF0; propagated from
                     UniProtKB/Swiss-Prot (Q9CPS8.1)"
     CDS             1..106
                     /gene="1700019D03Rik"
                     /gene_synonym="2410136C24Rik; smAKAP"
                     /coded_by="NM_001368274.1:275..595"
                     /db_xref="CCDS:CCDS14949.1"
                     /db_xref="GeneID:67080"
                     /db_xref="MGI:MGI:1914330"
ORIGIN      
        1 mgcmksketf pfpttldidk lheseeafip ddssqyrtps pgeqqqvqev kklpepgavi
       61 galilefadr laseivedal qqwaceniqy ynipyieseg sdttin
//
LOCUS       NP_004934                674 aa            linear   PRI 27-APR-2025
DEFINITION  dystrophia myotonica WD repeat-containing protein [Homo sapiens].
ACCESSION   NP_004934 XP_496318
VERSION     NP_004934.1
DBSOURCE    REFSEQ: accession NM_004943.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Olazabal-Herrero,A., Bilbao-Arribas,M., Carlevaris,O., Sendino,M.,
            Varela-Martinez,E., Jugo,B.M., Berra,E. and Rodriguez,J.A.
  TITLE     The dystrophia myotonica WD repeat-containing protein DMWD and
            WDR20 differentially regulate USP12 deubiquitinase
  JOURNAL   FEBS J 288 (20), 5943-5963 (2021)
   PUBMED   33844468
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Santoro,M., Masciullo,M., Silvestri,G., Novelli,G. and Botta,A.
  TITLE     Myotonic dystrophy type 1: role of CCG, CTC and CGG interruptions
            within DMPK alleles in the pathogenesis and molecular diagnosis
  JOURNAL   Clin Genet 92 (4), 355-364 (2017)
   PUBMED   27991661
  REMARK    Review article
REFERENCE   3  (residues 1 to 674)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   4  (residues 1 to 674)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   5  (residues 1 to 674)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   6  (residues 1 to 674)
  AUTHORS   Groenen,P. and Wieringa,B.
  TITLE     Expanding complexity in myotonic dystrophy
  JOURNAL   Bioessays 20 (11), 901-912 (1998)
   PUBMED   9872056
  REMARK    Review article
REFERENCE   7  (residues 1 to 674)
  AUTHORS   Jansen,G., Bachner,D., Coerwinkel,M., Wormskamp,N., Hameister,H.
            and Wieringa,B.
  TITLE     Structural organization and developmental expression pattern of the
            mouse WD-repeat gene DMR-N9 immediately upstream of the myotonic
            dystrophy locus
  JOURNAL   Hum Mol Genet 4 (5), 843-852 (1995)
   PUBMED   7633444
REFERENCE   8  (residues 1 to 674)
  AUTHORS   Shaw,D.J., McCurrach,M., Rundle,S.A., Harley,H.G., Crow,S.R.,
            Sohn,R., Thirion,J.P., Hamshere,M.G., Buckler,A.J., Harper,P.S. et
            al.
  TITLE     Genomic organization and transcriptional units at the myotonic
            dystrophy locus
  JOURNAL   Genomics 18 (3), 673-679 (1993)
   PUBMED   7905855
REFERENCE   9  (residues 1 to 674)
  AUTHORS   Mahadevan,M.S., Amemiya,C., Jansen,G., Sabourin,L., Baird,S.,
            Neville,C.E., Wormskamp,N., Segers,B., Batzer,M., Lamerdin,J. et
            al.
  TITLE     Structure and genomic sequence of the myotonic dystrophy (DM
            kinase) gene
  JOURNAL   Hum Mol Genet 2 (3), 299-304 (1993)
   PUBMED   8499920
REFERENCE   10 (residues 1 to 674)
  AUTHORS   Jansen,G., Mahadevan,M., Amemiya,C., Wormskamp,N., Segers,B.,
            Hendriks,W., O'Hoy,K., Baird,S., Sabourin,L., Lennon,G. et al.
  TITLE     Characterization of the myotonic dystrophy region predicts multiple
            protein isoform-encoding mRNAs
  JOURNAL   Nat Genet 1 (4), 261-266 (1992)
   PUBMED   1302022
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011530.6, BM922103.1, L19267.1, BG106514.1, BC019266.1,
            CD106470.1, BX283745.1, BC041034.1 and BQ189202.1.
            
            On Apr 29, 2005 this sequence version replaced XP_496318.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L19267.1, ERR3218378.45696.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270223.7/ ENSP00000270223.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..674
                     /product="dystrophia myotonica WD repeat-containing
                     protein"
                     /note="protein 59; dystrophia myotonica-containing WD
                     repeat motif protein; dystrophia myotonica, WD repeat
                     containing"
                     /calculated_mol_wt=70307
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q09019.3)"
     Region          31..92
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Region          103..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Region          211..251
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Region          217..282
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <276..378
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          282..321
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Region          287..322
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          324..363
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Region          330..363
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          366..409
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Region          384..419
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Region          413..453
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Region          456..516
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q09019.3)"
     Region          532..573
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Site            551
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q08274; propagated from
                     UniProtKB/Swiss-Prot (Q09019.3)"
     Region          601..638
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     Region          637..674
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09019.3)"
     CDS             1..674
                     /gene="DMWD"
                     /gene_synonym="D19S593E; DMR-N9; DMRN9; gene59"
                     /coded_by="NM_004943.2:90..2114"
                     /db_xref="CCDS:CCDS33054.1"
                     /db_xref="GeneID:1762"
                     /db_xref="HGNC:HGNC:2936"
                     /db_xref="MIM:609857"
ORIGIN      
        1 maaggaeggs gpgaamgdca eiksqfrtre gfykllpgdg aarrsgpasa qtpvppqppq
       61 pppgpasasg pgaagpassp ppagpgpgpa lpavrlslvr lgepdsagag eppatpaglg
      121 sggdrvcfnl grelyfypgc crrgsqrsid lnkpidkriy kgtqptchdf nqftaateti
      181 sllvgfsagq vqyldlikkd tsklfneerl idktkvtylk wlpeseslfl ashasghlyl
      241 ynvshpcasa ppqysllkqg egfsvyaaks kaprnplakw avgegplnef afspdgrhla
      301 cvsqdgclrv fhfdsmllrg lmksyfggll cvcwspdgry vvtggeddlv tvwsftegrv
      361 varghghksw vnavafdpyt traeeaataa gadgersgee eeeepeaagt gsaggaplsp
      421 lpkagsityr fgsagqdtqf clwdltedvl yphpplartr tlpgtpgttp paasssrgge
      481 pgpgplprsl srsnslphpa gggkaggpgv aaepgtpfsi grfatltlqe rrdrgaekeh
      541 kryhslgnis rggsggsgsg gekpsgpvpr srldpakvlg talcprihev plleplvckk
      601 iaqerltvll fledciitac qeglictwar pgkaftdeet eaqtgegswp rspsksvveg
      661 issqpgnsps gtvv
//
LOCUS       NP_003097                317 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor SOX-2 [Homo sapiens].
ACCESSION   NP_003097
VERSION     NP_003097.1
DBSOURCE    REFSEQ: accession NM_003106.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Schaefer,T., Mittal,N., Wang,H., Ataman,M., Candido,S.,
            Lotscher,J., Velychko,S., Tintignac,L., Bock,T., Borsch,A.,
            Bassler,J., Rao,T.N., Zmajkovic,J., Roffeis,S., Loliger,J.,
            Jacob,F., Dumlin,A., Schurch,C., Schmidt,A., Skoda,R.C.,
            Wymann,M.P., Hess,C., Scholer,H.R., Zaehres,H., Hurt,E., Zavolan,M.
            and Lengerke,C.
  TITLE     Nuclear and cytosolic fractions of SOX2 synergize as
            transcriptional and translational co-regulators of cell fate
  JOURNAL   Cell Rep 43 (10), 114807 (2024)
   PUBMED   39368083
  REMARK    GeneRIF: Nuclear and cytosolic fractions of SOX2 synergize as
            transcriptional and translational co-regulators of cell fate.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Ormsbee Golden,B.D., Gonzalez,D.V., Yochum,G.S., Coulter,D.W. and
            Rizzino,A.
  TITLE     SOX2 represses c-MYC transcription by altering the co-activator
            landscape of the c-MYC super-enhancer and promoter regions
  JOURNAL   J Biol Chem 300 (9), 107642 (2024)
   PUBMED   39122009
  REMARK    GeneRIF: SOX2 represses c-MYC transcription by altering the
            co-activator landscape of the c-MYC super-enhancer and promoter
            regions.
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Kainulainen,K., Niskanen,E.A., Kinnunen,J., Maki-Mantila,K.,
            Hartikainen,K., Paakinaho,V., Malinen,M., Ketola,K. and
            Pasonen-Seppanen,S.
  TITLE     Secreted factors from M1 macrophages drive prostate cancer stem
            cell plasticity by upregulating NANOG, SOX2, and CD44 through
            NFkappaB-signaling
  JOURNAL   Oncoimmunology 13 (1), 2393442 (2024)
   PUBMED   39175947
  REMARK    GeneRIF: Secreted factors from M1 macrophages drive prostate cancer
            stem cell plasticity by upregulating NANOG, SOX2, and CD44 through
            NFkappaB-signaling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Silveira,A.C.J., Guimaraes,L.S., VON Held,R., Silva,E.B.D.,
            Silveira,F.M., Oliveira Neto,Z.C., Scariot,R., Winckler,C.,
            Kuchler,E.C., Brancher,J.A., Antunes,L.A.A. and Antunes,L.S.
  TITLE     Do SOD2 and SOD3 gene polymorphisms impact the oral health-related
            quality of life in Para athletes?
  JOURNAL   Braz Oral Res 38, e074 (2024)
   PUBMED   39109770
  REMARK    GeneRIF: Do SOD2 and SOD3 gene polymorphisms impact the oral
            health-related quality of life in Para athletes?
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Helland,R., Berglund,G.I., Otlewski,J., Apostoluk,W.,
            Andersen,O.A., Willassen,N.P. and Smalas,A.O.
  TITLE     High-resolution structures of three new trypsin-squash-inhibitor
            complexes: a detailed comparison with other trypsins and their
            complexes
  JOURNAL   Acta Crystallogr D Biol Crystallogr 55 (Pt 1), 139-148 (1999)
   PUBMED   10089404
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Yuan,H., Corbi,N., Basilico,C. and Dailey,L.
  TITLE     Developmental-specific activity of the FGF-4 enhancer requires the
            synergistic action of Sox2 and Oct-3
  JOURNAL   Genes Dev 9 (21), 2635-2645 (1995)
   PUBMED   7590241
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Stevanovic,M., Zuffardi,O., Collignon,J., Lovell-Badge,R. and
            Goodfellow,P.
  TITLE     The cDNA sequence and chromosomal location of the human SOX2 gene
  JOURNAL   Mamm Genome 5 (10), 640-642 (1994)
   PUBMED   7849401
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Scott,D.A.
  TITLE     Esophageal Atresia / Tracheoesophageal Fistula Overview - RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301753
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Williamson,K.A., Yates,T.M. and FitzPatrick,D.R.
  TITLE     SOX2 Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301477
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF305585.1, DA388996.1,
            BC013923.2, AC117415.7 and CN430685.1.
            
            Summary: This intronless gene encodes a member of the SRY-related
            HMG-box (SOX) family of transcription factors involved in the
            regulation of embryonic development and in the determination of
            cell fate. The product of this gene is required for stem-cell
            maintenance in the central nervous system, and also regulates gene
            expression in the stomach. Mutations in this gene have been
            associated with optic nerve hypoplasia and with syndromic
            microphthalmia, a severe form of structural eye malformation. This
            gene lies within an intron of another gene called SOX2 overlapping
            transcript (SOX2OT). [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR3476690.293043.1,
                                        SRR3476690.254255.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325404.3/ ENSP00000323588.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.33"
     Protein         1..317
                     /product="transcription factor SOX-2"
                     /note="transcription factor SOX2; SRY-related HMG-box gene
                     2; sex determining region Y-box 2; SRY (sex determining
                     region Y)-box 2; SRY-box 2"
                     /calculated_mol_wt=34179
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48431.1)"
     Region          39..118
                     /region_name="HMG-box_SoxB"
                     /note="high mobility group (HMG)-box found in group B
                     SRY-related high-mobility group (HMG) box (Sox)
                     transcription factors; cd01388"
                     /db_xref="CDD:438790"
     Site            order(40,42..43,45..49,53,56..57,64..69,72..73,76,79..80,
                     87,98,110..115)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438790"
     Site            42
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:29358331; propagated from
                     UniProtKB/Swiss-Prot (P48431.1)"
     Region          110..200
                     /region_name="SOXp"
                     /note="SOX transcription factor; pfam12336"
                     /db_xref="CDD:463537"
     Site            117
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:29358331; propagated from
                     UniProtKB/Swiss-Prot (P48431.1)"
     Region          243..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48431.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P48431.1)"
     Region          272..280
                     /region_name="9aaTAD.
                     /evidence=ECO:0000250|UniProtKB:P41225"
                     /note="propagated from UniProtKB/Swiss-Prot (P48431.1)"
     Region          297..317
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48431.1)"
     CDS             1..317
                     /gene="SOX2"
                     /gene_synonym="ANOP3; MCOPS3"
                     /coded_by="NM_003106.4:437..1390"
                     /db_xref="CCDS:CCDS3239.1"
                     /db_xref="GeneID:6657"
                     /db_xref="HGNC:HGNC:11195"
                     /db_xref="MIM:184429"
ORIGIN      
        1 mynmmetelk ppgpqqtsgg gggnstaaaa ggnqknspdr vkrpmnafmv wsrgqrrkma
       61 qenpkmhnse iskrlgaewk llsetekrpf ideakrlral hmkehpdyky rprrktktlm
      121 kkdkytlpgg llapggnsma sgvgvgaglg agvnqrmdsy ahmngwsngs ysmmqdqlgy
      181 pqhpglnahg aaqmqpmhry dvsalqynsm tssqtymngs ptysmsysqq gtpgmalgsm
      241 gsvvkseass sppvvtsssh srapcqagdl rdmismylpg aevpepaaps rlhmsqhyqs
      301 gpvpgtaing tlplshm
//
LOCUS       NP_001349896             257 aa            linear   ROD 27-APR-2025
DEFINITION  7-methylguanosine phosphate-specific 5'-nucleotidase isoform 4 [Mus
            musculus].
ACCESSION   NP_001349896
VERSION     NP_001349896.1
DBSOURCE    REFSEQ: accession NM_001362967.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590968.8, AK011707.1 and BE944684.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY710934.1, ERR3363658.820459.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164137
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 63.47 cM"
     Protein         1..257
                     /product="7-methylguanosine phosphate-specific
                     5'-nucleotidase isoform 4"
                     /EC_number="3.1.3.5"
                     /EC_number="3.1.3.91"
                     /note="cytosolic 5'-nucleotidase III-like protein;
                     cN-III-like protein; 5'-nucleotidase, cytosolic III-like;
                     cytosolic 5'-nucleotidase 3B; 7-methylguanosine
                     phosphate-specific 5'-nucleotidase; 7-methylguanosine
                     nucleotidase; N(7)-methylguanylate 5'-phosphatase"
                     /calculated_mol_wt=29595
     Region          1..246
                     /region_name="UMPH-1"
                     /note="Pyrimidine 5'-nucleotidase (UMPH-1); pfam05822"
                     /db_xref="CDD:310424"
     Site            order(1..2,17,38,42,45,62..63,66,113..115,159,162,
                     186..187,190..191)
                     /site_type="active"
                     /db_xref="CDD:319807"
     CDS             1..257
                     /gene="Nt5c3b"
                     /gene_synonym="2610037D24Rik; C330027I04Rik; Nt5c3l"
                     /coded_by="NM_001362967.1:190..963"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS88253.1"
                     /db_xref="GeneID:68106"
                     /db_xref="MGI:MGI:1915356"
ORIGIN      
        1 mtlsrfayng qrcpsshnil dnskiisedc rkeltelfhh yypieidphr tikeklphmv
       61 qwwskahsll cqqriqkvqi aqvvgestam lregyktffd tlyqnniplf ifsagigdil
      121 eeiirqmkvf hpnihivsny mdfsedgflk gfkgqlihty nknssvcens syfqqlqnkt
      181 niillgdsig dltmadgvpg vqnilkigfl ndkveerrer ymdsydivle kdetldvvng
      241 llrhilyqgd cvelqgs
//
LOCUS       NP_001349879            1399 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear receptor coactivator 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001349879
VERSION     NP_001349879.1
DBSOURCE    REFSEQ: accession NM_001362950.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1399)
  AUTHORS   Tong,Z., Zhang,Y., Guo,P., Wang,W., Chen,Q., Jin,J., Liu,S., Yu,C.,
            Mo,P., Zhang,L. and Huang,J.
  TITLE     Steroid receptor coactivator 1 promotes human hepatocellular
            carcinoma invasiveness through enhancing MMP-9
  JOURNAL   J Cell Mol Med 28 (7), e18171 (2024)
   PUBMED   38506084
  REMARK    GeneRIF: Steroid receptor coactivator 1 promotes human
            hepatocellular carcinoma invasiveness through enhancing MMP-9.
REFERENCE   2  (residues 1 to 1399)
  AUTHORS   Kurdi,M., Fadul,M.M., Addas,B.M.J., Faizo,E., Alkhayyat,S.,
            Bamaga,A.K., Alsinani,T., Katib,Y., Okal,F., Maghrabi,Y.,
            Sabbagh,A.J., Moshref,R., Albalawi,S., Alkhotani,A., Halawa,T.F.,
            Mulla,N., Hakamy,S. and Baeesa,S.
  TITLE     Dynamic interplay between corticosteroid treatment and the role of
            SRC-1 gene dysregulation in the progression of WHO-Grade 4
            Astrocytoma
  JOURNAL   J Neurooncol 163 (3), 693-705 (2023)
   PUBMED   37402091
  REMARK    GeneRIF: Dynamic interplay between corticosteroid treatment and the
            role of SRC-1 gene dysregulation in the progression of WHO-Grade 4
            Astrocytoma.
REFERENCE   3  (residues 1 to 1399)
  AUTHORS   Cacciottolo,T.M., Henning,E., Keogh,J.M., Bel Lassen,P., Lawler,K.,
            Bounds,R., Ahmed,R., Perdikari,A., Mendes de Oliveira,E., Smith,M.,
            Godfrey,E.M., Johnson,E., Hodson,L., Clement,K., van der
            Klaauw,A.A. and Farooqi,I.S.
  TITLE     Obesity Due to Steroid Receptor Coactivator-1 Deficiency Is
            Associated With Endocrine and Metabolic Abnormalities
  JOURNAL   J Clin Endocrinol Metab 107 (6), e2532-e2544 (2022)
   PUBMED   35137184
  REMARK    GeneRIF: Obesity Due to Steroid Receptor Coactivator-1 Deficiency
            Is Associated With Endocrine and Metabolic Abnormalities.
REFERENCE   4  (residues 1 to 1399)
  AUTHORS   Guo,P., Chen,Q., Peng,K., Xie,J., Liu,J., Ren,W., Tong,Z., Li,M.,
            Xu,J., Zhang,Y., Yu,C. and Mo,P.
  TITLE     Nuclear receptor coactivator SRC-1 promotes colorectal cancer
            progression through enhancing GLI2-mediated Hedgehog signaling
  JOURNAL   Oncogene 41 (20), 2846-2859 (2022)
   PUBMED   35418691
  REMARK    GeneRIF: Nuclear receptor coactivator SRC-1 promotes colorectal
            cancer progression through enhancing GLI2-mediated Hedgehog
            signaling.
REFERENCE   5  (residues 1 to 1399)
  AUTHORS   Dermawan,J.K., Azzato,E.M., Jebastin Thangaiah,J.,
            Gjorgova-Gjeorgievski,S., Rubin,B.P., Folpe,A.L., Agaimy,A. and
            Fritchie,K.J.
  TITLE     PRRX1-NCOA1-rearranged fibroblastic tumour: a clinicopathological,
            immunohistochemical and molecular genetic study of six cases of a
            potentially under-recognised, distinctive mesenchymal tumour
  JOURNAL   Histopathology 79 (6), 997-1003 (2021)
   PUBMED   34272753
  REMARK    GeneRIF: PRRX1-NCOA1-rearranged fibroblastic tumour: a
            clinicopathological, immunohistochemical and molecular genetic
            study of six cases of a potentially under-recognised, distinctive
            mesenchymal tumour.
REFERENCE   6  (residues 1 to 1399)
  AUTHORS   Jeyakumar,M., Tanen,M.R. and Bagchi,M.K.
  TITLE     Analysis of the functional role of steroid receptor coactivator-1
            in ligand-induced transactivation by thyroid hormone receptor
  JOURNAL   Mol Endocrinol 11 (6), 755-767 (1997)
   PUBMED   9171239
REFERENCE   7  (residues 1 to 1399)
  AUTHORS   Takeshita,A., Yen,P.M., Misiti,S., Cardona,G.R., Liu,Y. and
            Chin,W.W.
  TITLE     Molecular cloning and properties of a full-length putative thyroid
            hormone receptor coactivator
  JOURNAL   Endocrinology 137 (8), 3594-3597 (1996)
   PUBMED   8754792
REFERENCE   8  (residues 1 to 1399)
  AUTHORS   Kamei,Y., Xu,L., Heinzel,T., Torchia,J., Kurokawa,R., Gloss,B.,
            Lin,S.C., Heyman,R.A., Rose,D.W., Glass,C.K. and Rosenfeld,M.G.
  TITLE     A CBP integrator complex mediates transcriptional activation and
            AP-1 inhibition by nuclear receptors
  JOURNAL   Cell 85 (3), 403-414 (1996)
   PUBMED   8616895
REFERENCE   9  (residues 1 to 1399)
  AUTHORS   Zhu,Y., Qi,C., Calandra,C., Rao,M.S. and Reddy,J.K.
  TITLE     Cloning and identification of mouse steroid receptor coactivator-1
            (mSRC-1), as a coactivator of peroxisome proliferator-activated
            receptor gamma
  JOURNAL   Gene Expr 6 (3), 185-195 (1996)
   PUBMED   9041124
REFERENCE   10 (residues 1 to 1399)
  AUTHORS   Onate,S.A., Tsai,S.Y., Tsai,M.J. and O'Malley,B.W.
  TITLE     Sequence and characterization of a coactivator for the steroid
            hormone receptor superfamily
  JOURNAL   Science 270 (5240), 1354-1357 (1995)
   PUBMED   7481822
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093798.3 and AC013459.9.
            
            Summary: The protein encoded by this gene acts as a transcriptional
            coactivator for steroid and nuclear hormone receptors. It is a
            member of the p160/steroid receptor coactivator (SRC) family and
            like other family members has histone acetyltransferase activity
            and contains a nuclear localization signal, as well as bHLH and PAS
            domains. The product of this gene binds nuclear receptors directly
            and stimulates the transcriptional activities in a
            hormone-dependent fashion. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3436612.1,
                                           SRR14038196.1515404.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..1399
                     /product="nuclear receptor coactivator 1 isoform 2"
                     /EC_number="2.3.1.48"
                     /note="steroid receptor coactivator-1; Hin-2 protein;
                     renal carcinoma antigen NY-REN-52; class E basic
                     helix-loop-helix protein 74"
                     /calculated_mol_wt=152254
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Region          27..87
                     /region_name="bHLH-PAS_NCoA1_SRC1"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in nuclear receptor coactivator 1 (NCoA-1)
                     and similar proteins; cd18948"
                     /db_xref="CDD:381518"
     Site            order(27..29,33,35..36,40,65..66)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381518"
     Site            order(38..39,42..43,45..46,67,70,74,76..77,81,83)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381518"
     Region          46..50
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          83..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          112..116
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          120..213
                     /region_name="PAS"
                     /note="PAS domain; PAS motifs appear in archaea,
                     eubacteria and eukarya. Probably the most surprising
                     identification of a PAS domain was that in EAG-like
                     K+-channels. PAS domains have been found to bind ligands,
                     and to act as sensors for light and oxygen in...; cd00130"
                     /db_xref="CDD:238075"
     Site            order(136,140,146,159..162,192)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(156,160,168,172..173,199,201)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          259..370
                     /region_name="PAS_11"
                     /note="PAS domain; pfam14598"
                     /db_xref="CDD:464214"
     Region          361..567
                     /region_name="Interaction with STAT3.
                     /evidence=ECO:0000269|PubMed:11773079"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          368..443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10660621,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10660621,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          457..477
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          468..590
                     /region_name="NCOA_u2"
                     /note="Unstructured region on nuclear receptor coactivator
                     protein; pfam16665"
                     /db_xref="CDD:465223"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10660621; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70365; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Region          561..585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10660621; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Region          597..626
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          629..708
                     /region_name="SRC-1"
                     /note="Steroid receptor coactivator; pfam08832"
                     /db_xref="CDD:462615"
     Region          633..637
                     /region_name="LXXLL motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          662..723
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          690..694
                     /region_name="LXXLL motif 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Region          741..818
                     /region_name="DUF4927"
                     /note="Domain of unknown function (DUF4927); pfam16279"
                     /db_xref="CDD:465083"
     Region          749..753
                     /region_name="LXXLL motif 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          781..988
                     /region_name="Interaction with CREBBP"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Site            867..868
                     /site_type="other"
                     /note="Breakpoint for translocation to form PAX3-NCOA1
                     oncogene; propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          913..917
                     /region_name="LXXLL motif 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          924..969
                     /region_name="Nuc_rec_co-act"
                     /note="Nuclear receptor coactivator; pfam08815"
                     /db_xref="CDD:462608"
     Region          974..>1309
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10660621; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Site            1073
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P70365; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Site            1091
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P70365; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Site            1124
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P70365; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Site            1131
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P70365; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Region          1143..1188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15788.3)"
     Region          1149..1205
                     /region_name="DUF1518"
                     /note="Nuclear receptor coactivator, DUF1518; pfam07469"
                     /db_xref="CDD:462174"
     Site            1179
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:10660621; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Site            1185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10660621; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     Region          1212..1268
                     /region_name="DUF1518"
                     /note="Nuclear receptor coactivator, DUF1518; pfam07469"
                     /db_xref="CDD:462174"
     Site            1372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15788.3)"
     CDS             1..1399
                     /gene="NCOA1"
                     /gene_synonym="bHLHe42; bHLHe74; F-SRC-1; KAT13A; RIP160;
                     SRC1"
                     /coded_by="NM_001362950.1:745..4944"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS1713.1"
                     /db_xref="GeneID:8648"
                     /db_xref="HGNC:HGNC:7668"
                     /db_xref="MIM:602691"
ORIGIN      
        1 msglgdsssd panpdshkrk gspcdtlass tekrrreqen kyleelaell sanisdidsl
       61 svkpdkckil kktvdqiqlm krmeqekstt dddvqksdis sssqgvieke slgpllleal
      121 dgfffvvnce grivfvsenv tsylgynqee lmntsvysil hvgdhaefvk nllpkslvng
      181 vpwpqeatrr nshtfncrml ihppdepgte nqeacqryev mqcftvsqpk siqedgedfq
      241 scliciarrl prppaitgve sfmtkqdttg kiisidtssl raagrtgwed lvrkciyaff
      301 qpqgrepsya rqlfqevmtr gtasspsyrf ilndgtmlsa htkcklcypq spdmqpfimg
      361 ihiidrehsg lspqddtnsg msiprvnpsv npsispahgv arsstlppsn snmvstrinr
      421 qqssdlhsss hsnssnsqgs fgcspgsqiv anvalnqgqa ssqssnpsln lnnspmegtg
      481 islaqfmspr rqvtsglatr prmpnnsfpp nistlsspvg mtssacnnnn rsysnipvts
      541 lqgmnegpnn svgfsasspv lrqmssqnsp srlniqpaka eskdnkeias ilnemiqsdn
      601 sssdgkplds gllhnndrls dgdskysqts hklvqllttt aeqqlrhadi dtsckdvlsc
      661 tgtsnsasan ssggscpssh sslterhkil hrllqegsps dittlsvepd kkdsastsvs
      721 vtgqvqgnss ikleldaskk keskdhqllr ylldkdekdl rstpnlsldd vkvkvekkeq
      781 mdpcntnptp mtkptpeeik leaqsqftad ldqfdqllpt lekaaqlpgl cetdrmdgav
      841 tsvtikseil paslqsatar ptsrlnrlpe leleaidnqf gqpgtgdqip wtnntvtain
      901 qsksedqcis sqldellcpp ttvegrndek alleqlvsfl sgkdetelae ldralgidkl
      961 vqgggldvls erfppqqatp plimeerpnl ysqpysspsp tanlpspfqg mvrqkpslgt
     1021 mpvqvtpprg afspgmgmqp rqtlnrppaa pnqlrlqlqq rlqgqqqlih qnrqailnqf
     1081 aatapvginm rsgmqqqitp qpplnaqmla qrqrelysqq hrqrqliqqq ramlmrqqsf
     1141 gnnlppssgl pvqmgnprlp qgapqqfpyp pnygtnpgtp pastspfsql aanpeaslan
     1201 rnsmvsrgmt gniggqfgtg inpqmqqnvf qypgagmvpq geanfapsls pgssmvpmpi
     1261 pppqssllqq tppasgyqsp dmkawqqgai gnnnvfsqav qnqptpaqpg vynnmsitvs
     1321 maggntnvqn mnpmmaqmqm sslqmpgmnt vcpeqindpa lrhtglycnq lsstdllkte
     1381 adgtqdkkte effsvvttd
//
LOCUS       NP_001354901            1932 aa            linear   PRI 27-APR-2025
DEFINITION  autophagy-related protein 2 homolog A isoform 3 [Homo sapiens].
ACCESSION   NP_001354901 XP_005273906
VERSION     NP_001354901.1
DBSOURCE    REFSEQ: accession NM_001367972.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1932)
  AUTHORS   Wang,Y., Dahmane,S., Ti,R., Mai,X., Zhu,L., Carlson,L.A. and
            Stjepanovic,G.
  TITLE     Structural basis for lipid transfer by the ATG2A-ATG9A complex
  JOURNAL   Nat Struct Mol Biol 32 (1), 35-47 (2025)
   PUBMED   39174844
REFERENCE   2  (residues 1 to 1932)
  AUTHORS   Chu,F., Wu,P., Mu,M., Hu,S. and Niu,C.
  TITLE     MGCG regulates glioblastoma tumorigenicity via hnRNPK/ATG2A and
            promotes autophagy
  JOURNAL   Cell Death Dis 14 (7), 443 (2023)
   PUBMED   37460467
  REMARK    GeneRIF: MGCG regulates glioblastoma tumorigenicity via
            hnRNPK/ATG2A and promotes autophagy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1932)
  AUTHORS   Broadbent,D.G., Barnaba,C., Perez,G.I. and Schmidt,J.C.
  TITLE     Quantitative analysis of autophagy reveals the role of ATG9 and
            ATG2 in autophagosome formation
  JOURNAL   J Cell Biol 222 (7) (2023)
   PUBMED   37115157
  REMARK    GeneRIF: Quantitative analysis of autophagy reveals the role of
            ATG9 and ATG2 in autophagosome formation.
REFERENCE   4  (residues 1 to 1932)
  AUTHORS   Ghanbarpour,A., Valverde,D.P., Melia,T.J. and Reinisch,K.M.
  TITLE     A model for a partnership of lipid transfer proteins and
            scramblases in membrane expansion and organelle biogenesis
  JOURNAL   Proc Natl Acad Sci U S A 118 (16) (2021)
   PUBMED   33850023
  REMARK    GeneRIF: A model for a partnership of lipid transfer proteins and
            scramblases in membrane expansion and organelle biogenesis.
REFERENCE   5  (residues 1 to 1932)
  AUTHORS   Li,Q., Ni,Y., Zhang,L., Jiang,R., Xu,J., Yang,H., Hu,Y., Qiu,J.,
            Pu,L., Tang,J. and Wang,X.
  TITLE     HIF-1alpha-induced expression of m6A reader YTHDF1 drives
            hypoxia-induced autophagy and malignancy of hepatocellular
            carcinoma by promoting ATG2A and ATG14 translation
  JOURNAL   Signal Transduct Target Ther 6 (1), 76 (2021)
   PUBMED   33619246
  REMARK    GeneRIF: HIF-1alpha-induced expression of m6A reader YTHDF1 drives
            hypoxia-induced autophagy and malignancy of hepatocellular
            carcinoma by promoting ATG2A and ATG14 translation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1932)
  AUTHORS   Yamada,Y., Sakuma,J., Takeuchi,I., Yasukochi,Y., Kato,K., Oguri,M.,
            Fujimaki,T., Horibe,H., Muramatsu,M., Sawabe,M., Fujiwara,Y.,
            Taniguchi,Y., Obuchi,S., Kawai,H., Shinkai,S., Mori,S., Arai,T. and
            Tanaka,M.
  TITLE     Identification of C21orf59 and ATG2A as novel determinants of renal
            function-related traits in Japanese by exome-wide association
            studies
  JOURNAL   Oncotarget 8 (28), 45259-45273 (2017)
   PUBMED   28410202
  REMARK    GeneRIF: Among polymorphisms identified in the present study,
            rs76974938 [C/T (D67N)] of C21orf59 and rs188780113 [G/A (R478C)]
            of ATG2A may be novel determinants of estimated glomerular
            filtration rate and chronic kidney disease or of the serum
            concentration of uric acid, respectively.
REFERENCE   7  (residues 1 to 1932)
  AUTHORS   Pfisterer,S.G., Bakula,D., Frickey,T., Cezanne,A., Brigger,D.,
            Tschan,M.P., Robenek,H. and Proikas-Cezanne,T.
  TITLE     Lipid droplet and early autophagosomal membrane targeting of Atg2A
            and Atg14L in human tumor cells
  JOURNAL   J Lipid Res 55 (7), 1267-1278 (2014)
   PUBMED   24776541
  REMARK    GeneRIF: These data provide evidence for additional roles of Atg2A
            and Atg14L in the formation of early autophagosomal membranes and
            also in lipid metabolism.
REFERENCE   8  (residues 1 to 1932)
  AUTHORS   Velikkakath,A.K., Nishimura,T., Oita,E., Ishihara,N. and
            Mizushima,N.
  TITLE     Mammalian Atg2 proteins are essential for autophagosome formation
            and important for regulation of size and distribution of lipid
            droplets
  JOURNAL   Mol Biol Cell 23 (5), 896-909 (2012)
   PUBMED   22219374
  REMARK    GeneRIF: Depletion of both Atg2A and Atg2B causes clustering of
            enlarged lipid droplets in an autophagy-independent manner. These
            data suggest that mammalian Atg2 proteins function both in
            autophagosome formation and regulation of lipid droplet morphology
            and dispersion.
REFERENCE   9  (residues 1 to 1932)
  AUTHORS   Romanyuk,D., Polak,A., Maleszewska,A., Sienko,M., Grynberg,M. and
            Zoladek,T.
  TITLE     Human hAtg2A protein expressed in yeast is recruited to
            preautophagosomal structure but does not complement autophagy
            defects of atg2Delta strain
  JOURNAL   Acta Biochim Pol 58 (3), 365-374 (2011)
   PUBMED   21887408
  REMARK    GeneRIF: human hAtg2A can not function in autophagy in yeast,
            however, it is recruited to the preautophagosomal structure
REFERENCE   10 (residues 1 to 1932)
  AUTHORS   Guru,S.C., Agarwal,S.K., Manickam,P., Olufemi,S.E., Crabtree,J.S.,
            Weisemann,J.M., Kester,M.B., Kim,Y.S., Wang,Y., Emmert-Buck,M.R.,
            Liotta,L.A., Spiegel,A.M., Boguski,M.S., Roe,B.A., Collins,F.S.,
            Marx,S.J., Burns,L. and Chandrasekharappa,S.C.
  TITLE     A transcript map for the 2.8-Mb region containing the multiple
            endocrine neoplasia type 1 locus
  JOURNAL   Genome Res 7 (7), 725-735 (1997)
   PUBMED   9253601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001187.5.
            
            On Jan 4, 2019 this sequence version replaced XP_005273906.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1932
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..1932
                     /product="autophagy-related protein 2 homolog A isoform 3"
                     /note="autophagy-related protein 2 homolog A; ATG2
                     autophagy related 2 homolog A; bridge-like lipid transfer
                     protein family member 4A"
                     /calculated_mol_wt=212095
     Region          14..>108
                     /region_name="Chorein_N"
                     /note="N-terminal region of Chorein or VPS13; pfam12624"
                     /db_xref="CDD:463646"
     Site            765
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Site            878
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P4T0; propagated from
                     UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P4T0; propagated from
                     UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P4T0; propagated from
                     UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Site            1260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P4T0; propagated from
                     UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Site            1295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Site            1303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Region          1309..1353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Region          1352..1398
                     /region_name="WIPI-interacting.
                     /evidence=ECO:0000269|PubMed:32483132"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Site            1396
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Region          1432..1470
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Region          1608..1651
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAZ0.3)"
     Region          1833..1926
                     /region_name="ATG_C"
                     /note="Autophagy-related protein C terminal domain;
                     pfam09333"
                     /db_xref="CDD:462761"
     CDS             1..1932
                     /gene="ATG2A"
                     /gene_synonym="BLTP4A"
                     /coded_by="NM_001367972.1:75..5873"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:23130"
                     /db_xref="HGNC:HGNC:29028"
                     /db_xref="MIM:616225"
ORIGIN      
        1 msrwlwpwsn cvkervcryl lhhylghffq ehlsldqlsl dlykgsvalr dihleiwsvn
       61 evlesmespl elvegfvgsi evavpwaall tdhctvrvsg lqltlqprrg papgaadsqs
      121 wascmttslq laqeclrdgl pepseppqpl eglemfaqti etvlrrikvt fldtvvrveh
      181 spgdgergva vevrvqrley cdeavrdpsq appvdvhqpp aflhkllqla gvrlhyeelp
      241 aqeeppeppl qigscsgyme lmvklkqnea fpgpklevag qlgslhlllt prqlqqlqel
      301 lsavsltdhe gladklnksr plgaedlwli eqdlnqqlqa gavaeplspd pltnpllnld
      361 ntdlffsmag ltssvasals elslsdvdla ssvrsdmasr rlsaqahpag kmapnplldt
      421 mrpdsllkmt lggvtltllq tsapssgppd lathfftefd atkdgpfgsr dfhhlrprfq
      481 racpcshvrl tgtavqlswe lrtgsrgrrt tsmevhfgql evleclwprg tsepeyteil
      541 tfpgtlgsqa sarpcahlrh tqilrrvpks rprrsvachc hselaldlan fqadvelgal
      601 drlaallrla tvpaeppagl lteplpameq qtvfrlsapr atlrlrfpia dlrpepdpwa
      661 gqavraeqlr lelsepqfrs elssgpgppv pthleltcsd lhgiyedggk ppvpclrvsk
      721 aldpkstgrk yflpqvvvtv npqssstqwe vapekgeele lsvespcelr epepspfssk
      781 rtmyeteemv ipgdpeemrt fqsrtlalsr cslevilpsv hiflpskevy esiynrinnd
      841 llmwepadll ptpdpaaqps gfpgpsgfwh dsfkmcksaf kldsdsdded ahffsvgasg
      901 gpqaaapeap slhlqstfst lvtvlkgrit alcetkdegg krleavhgel vldmehgtlf
      961 svsqycgqpg lgyfcleaek atlyhraavd dyplpshldl psfappaqla ptiypseegv
     1021 tergasgrkg qgrgphmlst avrihldphk nvkeflvtlr lhkatlrhym alpeqswhsq
     1081 llefldvldd pvlgylpptv itilhthlfs csvdyrplyl pvrvlitaet ftlssniimd
     1141 tstfllrfil ddsalylsdk cevetldlrr dyvcvldvdl lelviktwkg stegklsqpl
     1201 felrcsnnvv hvhscadsca llvnllqyvm stgdlhpppr ppspteiagq kvqlsespas
     1261 lpscppveta linqrdlada lldterslre laqpsgghlp qaspisvylf pgersgappp
     1321 sppvggpags lgscseeked ereeegdgdt ldsdefcild apglgipprd gepvvtqlhp
     1381 gpivvrdgyf srpigstdll rapahfpvps trvvlrevsl vwhlyggrdf gphpghrart
     1441 glsgprssps rcsgpnrpqn swrtqggsgr qhhvlmeiql skvsfqhevy paepatgpaa
     1501 psqeleerpl srqvfivqel evrdrlassq inkflylhts ermprrahsn mltikalhva
     1561 pttnlggpec clrvslmplr lnvdqdalff lkdfftslva ginpvvpget saearpetra
     1621 qpssplegqa egvettgsqe apggghspsp pdqqpiyfre frftsevpiw ldyhgkhvtm
     1681 dqvgtfagll iglaqlncse lklkrlccrh gllgvdkvlg yalnewlqdi rknqlpgllg
     1741 gvgpmhsvvq lfqgfrdllw lpieqyrkdg rlmrglqrga asfgsstasa alelsnrlvq
     1801 aiqataetvy dilspaapvs rslqdkrsar rlrrgqqpad lregvakayd tvregildta
     1861 qticdvasrg heqkgltgav ggvirqlppt vvkplilate atssllggmr nqivpdahkd
     1921 halkwrsdsa qd
//
LOCUS       NP_001353281             220 aa            linear   PRI 27-APR-2025
DEFINITION  androgen-induced gene 1 protein isoform n [Homo sapiens].
ACCESSION   NP_001353281
VERSION     NP_001353281.1
DBSOURCE    REFSEQ: accession NM_001366352.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Nakada-Tsukui,K., Sekizuka,T., Sato-Ebine,E., Escueta-de Cadiz,A.,
            Ji,D.D., Tomii,K., Kuroda,M. and Nozaki,T.
  TITLE     AIG1 affects in vitro and in vivo virulence in clinical isolates of
            Entamoeba histolytica
  JOURNAL   PLoS Pathog 14 (3), e1006882 (2018)
   PUBMED   29554130
  REMARK    GeneRIF: High AIG1 expression is associated with virulence in
            clinical isolates of Entamoeba histolytica.
            Erratum:[PLoS Pathog. 2018 May 31;14(5):e1007091. doi:
            10.1371/journal.ppat.1007091. PMID: 29851996]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Parsons,W.H., Kolar,M.J., Kamat,S.S., Cognetta,A.B. 3rd,
            Hulce,J.J., Saez,E., Kahn,B.B., Saghatelian,A. and Cravatt,B.F.
  TITLE     AIG1 and ADTRP are atypical integral membrane hydrolases that
            degrade bioactive FAHFAs
  JOURNAL   Nat Chem Biol 12 (5), 367-372 (2016)
   PUBMED   27018888
  REMARK    GeneRIF: These results indicate that AIG1 and ADTRP are founding
            members of an evolutionarily conserved class of transmembrane
            threonine hydrolases involved in bioactive lipid metabolism.
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 220)
  AUTHORS   Wu,G., Sun,M., Zhang,W. and Huo,K.
  TITLE     AIG1 is a novel Pirh2-interacting protein that activates the NFAT
            signaling pathway
  JOURNAL   Front Biosci (Elite Ed) 3 (3), 834-842 (2011)
   PUBMED   21622095
  REMARK    GeneRIF: identified a novel Pirh2-interacting protein, AIG1, by
            yeast two-hybrid screening and confirmed its interaction with p53
            both in vitro and in vivo
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 220)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   8  (residues 1 to 220)
  AUTHORS   Seo,J., Kim,J. and Kim,M.
  TITLE     Cloning of androgen-inducible gene 1 (AIG1) from human dermal
            papilla cells
  JOURNAL   Mol Cells 11 (1), 35-40 (2001)
   PUBMED   11266118
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL023581.1, AL391726.8 and AL136116.11.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.27777.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.2"
     Protein         1..220
                     /product="androgen-induced gene 1 protein isoform n"
                     /note="androgen-induced gene 1 protein; FAHFA hydrolase
                     AIG1; fatty acid esters of hydroxy fatty acids hydrolase
                     AIG1"
                     /calculated_mol_wt=25191
     Region          36..>157
                     /region_name="Far-17a_AIG1"
                     /note="FAR-17a/AIG1-like protein; pfam04750"
                     /db_xref="CDD:428104"
     CDS             1..220
                     /gene="AIG1"
                     /gene_synonym="AIG-1; dJ95L4.1"
                     /coded_by="NM_001366352.1:183..845"
                     /note="isoform n is encoded by transcript variant 14"
                     /db_xref="GeneID:51390"
                     /db_xref="HGNC:HGNC:21607"
                     /db_xref="MIM:608514"
ORIGIN      
        1 mtkvtkemtt rrlpgrgrqw rasanrarpv qvlrmaills ycsilcnyka iempshqtyg
       61 gswkfltfid lviqavffgi cvltdlssll trgsgnqeqe rqlkklislr dwmlavlafp
      121 vgvfvvavfw iiyaydremi ypklldnfip gwlnhgmgvl gascnwhvgv pfpgthwprs
      181 qnhllwvynh lnelpvpagr sseqlylgyt ekygrrerka
//
LOCUS       NP_733800                330 aa            linear   PRI 27-APR-2025
DEFINITION  G-protein coupled bile acid receptor 1 [Homo sapiens].
ACCESSION   NP_733800
VERSION     NP_733800.1
DBSOURCE    REFSEQ: accession NM_170699.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Zhuang,L., Jia,N., Zhang,L., Zhang,Q., Antwi,S.O., Sartorius,K.,
            Wu,K., Sun,D., Xi,D. and Lu,Y.
  TITLE     Gpbar-1/cAMP/PKA signaling mitigates macrophage-mediated acute
            cholestatic liver injury via antagonizing NLRP3-ASC inflammasome
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (6), 167266 (2024)
   PUBMED   38806072
  REMARK    GeneRIF: Gpbar-1/cAMP/PKA signaling mitigates macrophage-mediated
            acute cholestatic liver injury via antagonizing NLRP3-ASC
            inflammasome.
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Vanden Brink,H., Vandeputte,D., Brito,I.L., Ronnekleiv,O.K.,
            Roberson,M.S. and Lomniczi,A.
  TITLE     Changes in the Bile Acid Pool and Timing of Female Puberty:
            Potential Novel Role of Hypothalamic TGR5
  JOURNAL   Endocrinology 165 (9) (2024)
   PUBMED   39082696
  REMARK    GeneRIF: Changes in the Bile Acid Pool and Timing of Female
            Puberty: Potential Novel Role of Hypothalamic TGR5.
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Li,C., Wang,L., Xie,W., Chen,E., Chen,Y., Li,H., Can,D., Lei,A.,
            Wang,Y. and Zhang,J.
  TITLE     TGR5 deficiency in excitatory neurons ameliorates Alzheimer's
            pathology by regulating APP processing
  JOURNAL   Sci Adv 10 (26), eado1855 (2024)
   PUBMED   38941459
  REMARK    GeneRIF: TGR5 deficiency in excitatory neurons ameliorates
            Alzheimer's pathology by regulating APP processing.
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Buchynskyi,M., Oksenych,V., Kamyshna,I., Vorobets,I., Halabitska,I.
            and Kamyshnyi,O.
  TITLE     Modulatory Roles of AHR, FFAR2, FXR, and TGR5 Gene Expression in
            Metabolic-Associated Fatty Liver Disease and COVID-19 Outcomes
  JOURNAL   Viruses 16 (6), 985 (2024)
   PUBMED   38932276
  REMARK    GeneRIF: Modulatory Roles of AHR, FFAR2, FXR, and TGR5 Gene
            Expression in Metabolic-Associated Fatty Liver Disease and COVID-19
            Outcomes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Zhan,K., Wu,H., Xu,Y., Rao,K., Zheng,H., Qin,S., Yang,Y., Jia,R.,
            Chen,W. and Huang,S.
  TITLE     The function of the gut microbiota-bile acid-TGR5 axis in
            diarrhea-predominant irritable bowel syndrome
  JOURNAL   mSystems 9 (3), e0129923 (2024)
   PUBMED   38329942
  REMARK    GeneRIF: The function of the gut microbiota-bile acid-TGR5 axis in
            diarrhea-predominant irritable bowel syndrome.
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Watanabe,M., Houten,S.M., Mataki,C., Christoffolete,M.A., Kim,B.W.,
            Sato,H., Messaddeq,N., Harney,J.W., Ezaki,O., Kodama,T.,
            Schoonjans,K., Bianco,A.C. and Auwerx,J.
  TITLE     Bile acids induce energy expenditure by promoting intracellular
            thyroid hormone activation
  JOURNAL   Nature 439 (7075), 484-489 (2006)
   PUBMED   16400329
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Kawamata,Y., Fujii,R., Hosoya,M., Harada,M., Yoshida,H., Miwa,M.,
            Fukusumi,S., Habata,Y., Itoh,T., Shintani,Y., Hinuma,S.,
            Fujisawa,Y. and Fujino,M.
  TITLE     A G protein-coupled receptor responsive to bile acids
  JOURNAL   J Biol Chem 278 (11), 9435-9440 (2003)
   PUBMED   12524422
  REMARK    GeneRIF: TGR5 is implicated in the suppression of macrophage
            functions by bile acids
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Maruyama,T., Miyamoto,Y., Nakamura,T., Tamai,Y., Okada,H.,
            Sugiyama,E., Nakamura,T., Itadani,H. and Tanaka,K.
  TITLE     Identification of membrane-type receptor for bile acids (M-BAR)
  JOURNAL   Biochem Biophys Res Commun 298 (5), 714-719 (2002)
   PUBMED   12419312
  REMARK    GeneRIF: Expression of BG37 was detected in various specific
            tissues, suggesting its physiological role.
REFERENCE   9  (residues 1 to 330)
  AUTHORS   Feldman,D.S., Zamah,A.M., Pierce,K.L., Miller,W.E., Kelly,F.,
            Rapacciuolo,A., Rockman,H.A., Koch,W.J. and Luttrell,L.M.
  TITLE     Selective inhibition of heterotrimeric Gs signaling. Targeting the
            receptor-G protein interface using a peptide minigene encoding the
            Galpha(s) carboxyl terminus
  JOURNAL   J Biol Chem 277 (32), 28631-28640 (2002)
   PUBMED   12036966
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Takeda,S., Kadowaki,S., Haga,T., Takaesu,H. and Mitaku,S.
  TITLE     Identification of G protein-coupled receptor genes from the human
            genome sequence
  JOURNAL   FEBS Lett 520 (1-3), 97-101 (2002)
   PUBMED   12044878
  REMARK    Erratum:[FEBS Lett 2002 Jul 17;523(1-3):257]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK122660.1, BC033625.1 and
            AC021016.5.
            
            Summary: This gene encodes a member of the G protein-coupled
            receptor (GPCR) superfamily. This enzyme functions as a cell
            surface receptor for bile acids. Treatment of cells expressing this
            GPCR with bile acids induces the production of intracellular cAMP,
            activation of a MAP kinase signaling pathway, and internalization
            of the receptor. The receptor is implicated in the suppression of
            macrophage functions and regulation of energy homeostasis by bile
            acids. Alternative splicing results in multiple transcript variants
            encoding the same protein. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033625.1, BX365038.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000519574.2/ ENSP00000430202.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..330
                     /product="G-protein coupled bile acid receptor 1"
                     /note="G-protein coupled bile acid receptor BG37; membrane
                     bile acid receptor; membrane-type receptor for bile acids;
                     G-protein coupled receptor GPCR19"
                     /calculated_mol_wt=35117
     Site            4
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDU6.1)"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDU6.1)"
     Region          28..284
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          51..72
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320571"
     Site            51..71
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDU6.1)"
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDU6.1)"
     Region          86..108
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320571"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDU6.1)"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDU6.1)"
     Region          126..142
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320571"
     Region          162..185
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320571"
     Site            166..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDU6.1)"
     Region          223..245
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320571"
     Site            229..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDU6.1)"
     Region          259..284
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320571"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDU6.1)"
     Region          309..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDU6.1)"
     CDS             1..330
                     /gene="GPBAR1"
                     /gene_synonym="BG37; GPCR19; GPR131; M-BAR; TGR5"
                     /coded_by="NM_170699.3:248..1240"
                     /db_xref="CCDS:CCDS46515.1"
                     /db_xref="GeneID:151306"
                     /db_xref="HGNC:HGNC:19680"
                     /db_xref="MIM:610147"
ORIGIN      
        1 mtpnstgevp spipkgalgl slalasliit anlllalgia wdrrlrsppa gcfflsllla
       61 glltglalpt lpglwnqsrr gywscllvyl apnfsflsll anlllvhger ymavlrplqp
      121 pgsirlalll twagpllfas lpalgwnhwt pgancssqai fpapylylev yglllpavga
      181 aaflsvrvla tahrqlqdic rleravcrde psalaraltw rqaraqagam llfglcwgpy
      241 vatlllsvla yeqrpplgpg tllsllslgs asaaavpvam glgdqrytap wraaaqrclq
      301 glwgrasrds pgpsiayhps sqssvdldln
//
LOCUS       NP_001350571             271 aa            linear   PRI 27-APR-2025
DEFINITION  BTB/POZ domain-containing protein KCTD11 isoform l [Homo sapiens].
ACCESSION   NP_001350571
VERSION     NP_001350571.1
DBSOURCE    REFSEQ: accession NM_001363642.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Lospinoso Severini,L., Loricchio,E., Navacci,S., Basili,I.,
            Alfonsi,R., Bernardi,F., Moretti,M., Conenna,M., Cucinotta,A.,
            Coni,S., Petroni,M., De Smaele,E., Giannini,G., Maroder,M.,
            Canettieri,G., Mastronuzzi,A., Guardavaccaro,D., Ayrault,O.,
            Infante,P., Bufalieri,F. and Di Marcotullio,L.
  TITLE     SALL4 is a CRL3REN/KCTD11 substrate that drives Sonic
            Hedgehog-dependent medulloblastoma
  JOURNAL   Cell Death Differ 31 (2), 170-187 (2024)
   PUBMED   38062245
  REMARK    GeneRIF: SALL4 is a CRL3[REN/KCTD11] substrate that drives Sonic
            Hedgehog-dependent medulloblastoma.
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Yang,M., Han,Y.M., Han,Q., Rong,X.Z., Liu,X.F. and Ln,X.Y.
  TITLE     KCTD11 inhibits progression of lung cancer by binding to
            beta-catenin to regulate the activity of the Wnt and Hippo pathways
  JOURNAL   J Cell Mol Med 25 (19), 9411-9426 (2021)
   PUBMED   34453479
  REMARK    GeneRIF: KCTD11 inhibits progression of lung cancer by binding to
            beta-catenin to regulate the activity of the Wnt and Hippo
            pathways.
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Smaldone,G., Pirone,L., Pedone,E., Marlovits,T., Vitagliano,L. and
            Ciccarelli,L.
  TITLE     The BTB domains of the potassium channel tetramerization domain
            proteins prevalently assume pentameric states
  JOURNAL   FEBS Lett 590 (11), 1663-1671 (2016)
   PUBMED   27152988
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Zazzeroni,F., Nicosia,D., Tessitore,A., Gallo,R., Verzella,D.,
            Fischietti,M., Vecchiotti,D., Ventura,L., Capece,D., Gulino,A. and
            Alesse,E.
  TITLE     KCTD11 tumor suppressor gene expression is reduced in prostate
            adenocarcinoma
  JOURNAL   Biomed Res Int 2014, 380398 (2014)
   PUBMED   25045667
  REMARK    GeneRIF: Our study demonstrates and supports that KCTD11, as well
            as negatively regulated downstream effectors belonging to Hh
            signaling, plays a role in prostate cancer pathogenesis.
REFERENCE   5  (residues 1 to 271)
  AUTHORS   De Smaele,E., Di Marcotullio,L., Moretti,M., Pelloni,M.,
            Occhione,M.A., Infante,P., Cucchi,D., Greco,A., Pietrosanti,L.,
            Todorovic,J., Coni,S., Canettieri,G., Ferretti,E., Bei,R.,
            Maroder,M., Screpanti,I. and Gulino,A.
  TITLE     Identification and characterization of KCASH2 and KCASH3, 2 novel
            Cullin3 adaptors suppressing histone deacetylase and Hedgehog
            activity in medulloblastoma
  JOURNAL   Neoplasia 13 (4), 374-385 (2011)
   PUBMED   21472142
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Correale,S., Pirone,L., Di Marcotullio,L., De Smaele,E., Greco,A.,
            Mazza,D., Moretti,M., Alterio,V., Vitagliano,L., Di Gaetano,S.,
            Gulino,A. and Pedone,E.M.
  TITLE     Molecular organization of the cullin E3 ligase adaptor KCTD11
  JOURNAL   Biochimie 93 (4), 715-724 (2011)
   PUBMED   21237243
  REMARK    GeneRIF: the protein is expressed in two alternative variants: a
            short previously characterized form (sKCTD11) composed by 232 amino
            acids and a longer variant (lKCTD11) which contains an N-terminal
            extension of 39 residues.
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Mancarelli,M.M., Zazzeroni,F., Ciccocioppo,L., Capece,D., Po,A.,
            Murgo,S., Di Camillo,R., Rinaldi,C., Ferretti,E., Gulino,A. and
            Alesse,E.
  TITLE     The tumor suppressor gene KCTD11REN is regulated by Sp1 and
            methylation and its expression is reduced in tumors
  JOURNAL   Mol Cancer 9, 172 (2010)
   PUBMED   20591193
  REMARK    GeneRIF: findings identify KCTD11 as a widely down-regulated gene
            in human cancers, and provide a basis to understand how its
            expression might be deregulated in tumor cells
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Di Marcotullio,L., Ferretti,E., De Smaele,E., Argenti,B.,
            Mincione,C., Zazzeroni,F., Gallo,R., Masuelli,L., Napolitano,M.,
            Maroder,M., Modesti,A., Giangaspero,F., Screpanti,I., Alesse,E. and
            Gulino,A.
  TITLE     REN(KCTD11) is a suppressor of Hedgehog signaling and is deleted in
            human medulloblastoma
  JOURNAL   Proc Natl Acad Sci U S A 101 (29), 10833-10838 (2004)
   PUBMED   15249678
  REMARK    GeneRIF: Results identify REN(KCTD11) as a suppressor of Hedgehog
            signaling and suggest that its inactivation might lead to a
            deregulation of the tumor-promoting Hedgehog pathway in
            medulloblastoma.
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Gallo,R., Zazzeroni,F., Alesse,E., Mincione,C., Borello,U.,
            Buanne,P., D'Eugenio,R., Mackay,A.R., Argenti,B., Gradini,R.,
            Russo,M.A., Maroder,M., Cossu,G., Frati,L., Screpanti,I. and
            Gulino,A.
  TITLE     REN: a novel, developmentally regulated gene that promotes neural
            cell differentiation
  JOURNAL   J Cell Biol 158 (4), 731-740 (2002)
   PUBMED   12186855
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026954.14.
            
            Transcript Variant: This variant (1b) initiates translation at an
            upstream AUU alternate start codon and encodes an isoform (l) with
            a longer N-terminus compared to isoform s. This isoform is
            suggested by experimental data in PMID:21237243.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match       :: ENST00000333751.8/ ENSP00000328352.5
            non-AUG initiation codon :: PMID: 21237243
            RefSeq Select criteria   :: based on manual assertion,
                                        conservation, expression, longest
                                        protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..271
                     /product="BTB/POZ domain-containing protein KCTD11 isoform
                     l"
                     /EC_number="2.3.2.27"
                     /note="BTB/POZ domain-containing protein KCTD11; retinoic
                     acid, EGF, NGF induced gene protein; RING-type E3
                     ubiquitin transferase subunit KCTD11; potassium channel
                     tetramerization domain-containing protein 11"
                     /calculated_mol_wt=29744
     Region          17..104
                     /region_name="BTB_POZ_KCTD11"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     channel tetramerization domain-containing protein KCTD11;
                     cd18370"
                     /db_xref="CDD:349679"
     Region          40
                     /region_name="alternative AUG start codon"
     Region          127..271
                     /region_name="KCTD11_21_C"
                     /note="BTB/POZ domain-containing protein KCTD11/21
                     C-terminus; pfam19329"
                     /db_xref="CDD:466043"
     CDS             1..271
                     /gene="KCTD11"
                     /gene_synonym="C17orf36; KCASH1; REN; REN/KCTD11"
                     /coded_by="NM_001363642.1:665..1480"
                     /exception="alternative start codon"
                     /note="isoform l is encoded by transcript variant 1b;
                     non-AUG (AUU) translation initiation codon"
                     /db_xref="CCDS:CCDS92247.1"
                     /db_xref="GeneID:147040"
                     /db_xref="HGNC:HGNC:21302"
                     /db_xref="MIM:609848"
ORIGIN      
        1 mspppvpssp psfggpvtln vggtlysttl etltrfpdsm lgamfragtp mppnlnsqgg
       61 ghyfidrdgk afrhilnflr lgrldlprgy getallraea dfyqirplld alreleasqg
      121 tpaptaallh advdvsprlv hfsarrgphh yelssvqvdt franlfctds eclgalrarf
      181 gvasgdraeg sphfhlewap rpvelpevey grlglqplwt ggpgerrevv gtpsfleevl
      241 rvalehgfrl dsvfpdpedl lnsrslrfvr h
//
LOCUS       NP_083837                338 aa            linear   ROD 27-APR-2025
DEFINITION  NEDD4 family-interacting protein 2 [Mus musculus].
ACCESSION   NP_083837 XP_001005690
VERSION     NP_083837.2
DBSOURCE    REFSEQ: accession NM_029561.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Gorla,M., Santiago,C., Chaudhari,K., Layman,A.A.K., Oliver,P.M. and
            Bashaw,G.J.
  TITLE     Ndfip Proteins Target Robo Receptors for Degradation and Allow
            Commissural Axons to Cross the Midline in the Developing Spinal
            Cord
  JOURNAL   Cell Rep 26 (12), 3298-3312 (2019)
   PUBMED   30893602
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Trimpert,C., Wesche,D., de Groot,T., Pimentel Rodriguez,M.M.,
            Wong,V., van den Berg,D.T.M., Cheval,L., Ariza,C.A., Doucet,A.,
            Stagljar,I. and Deen,P.M.T.
  TITLE     NDFIP allows NEDD4/NEDD4L-induced AQP2 ubiquitination and
            degradation
  JOURNAL   PLoS One 12 (9), e0183774 (2017)
   PUBMED   28931009
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   5  (residues 1 to 338)
  AUTHORS   O'Leary,C.E., Riling,C.R., Spruce,L.A., Ding,H., Kumar,S., Deng,G.,
            Liu,Y., Seeholzer,S.H. and Oliver,P.M.
  TITLE     Ndfip-mediated degradation of Jak1 tunes cytokine signalling to
            limit expansion of CD4+ effector T cells
  JOURNAL   Nat Commun 7, 11226 (2016)
   PUBMED   27088444
  REMARK    GeneRIF: Data indicate thar Janus kinase 1 (Jak1) degradation is
            dependent on Nedd4 family interacting proteins Ndfip1/Ndfip2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Foot,N.J., Dalton,H.E., Shearwin-Whyatt,L.M., Dorstyn,L., Tan,S.S.,
            Yang,B. and Kumar,S.
  TITLE     Regulation of the divalent metal ion transporter DMT1 and iron
            homeostasis by a ubiquitin-dependent mechanism involving Ndfips and
            WWP2
  JOURNAL   Blood 112 (10), 4268-4275 (2008)
   PUBMED   18776082
  REMARK    GeneRIF: DMT1 interacts with 2 WW domain-interacting proteins,
            Ndfip1 and Ndfip2. This promotes DMT1 ubiquitination and
            degradation by WWP2.
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Shearwin-Whyatt,L.M., Brown,D.L., Wylie,F.G., Stow,J.L. and
            Kumar,S.
  TITLE     N4WBP5A (Ndfip2), a Nedd4-interacting protein, localizes to
            multivesicular bodies and the Golgi, and has a potential role in
            protein trafficking
  JOURNAL   J Cell Sci 117 (Pt 16), 3679-3689 (2004)
   PUBMED   15252135
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Konstas,A.A., Shearwin-Whyatt,L.M., Fotia,A.B., Degger,B.,
            Riccardi,D., Cook,D.I., Korbmacher,C. and Kumar,S.
  TITLE     Regulation of the epithelial sodium channel by N4WBP5A, a novel
            Nedd4/Nedd4-2-interacting protein
  JOURNAL   J Biol Chem 277 (33), 29406-29416 (2002)
   PUBMED   12050153
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Harvey,K.F., Shearwin-Whyatt,L.M., Fotia,A., Parton,R.G. and
            Kumar,S.
  TITLE     N4WBP5, a potential target for ubiquitination by the Nedd4 family
            of proteins, is a novel Golgi-associated protein
  JOURNAL   J Biol Chem 277 (11), 9307-9317 (2002)
   PUBMED   11748237
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC141878.4.
            
            On Jul 9, 2010 this sequence version replaced NP_083837.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC071237.1, AK132235.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 55.64 cM"
     Protein         1..338
                     /product="NEDD4 family-interacting protein 2"
                     /note="NEDD4 WW domain-binding protein 5A"
                     /calculated_mol_wt=36409
     Region          105..338
                     /region_name="NDFIP2"
                     /note="NEDD4 family-interacting protein 2; cd22306"
                     /db_xref="CDD:412070"
     CDS             1..338
                     /gene="Ndfip2"
                     /gene_synonym="0710001O20Rik; 2810436B12Rik;
                     9130207N19Rik; mKIAA1165; N4wbp5a"
                     /coded_by="NM_029561.5:51..1067"
                     /db_xref="CCDS:CCDS49560.2"
                     /db_xref="GeneID:76273"
                     /db_xref="MGI:MGI:1923523"
ORIGIN      
        1 mgrrrsqrac asapsmlssa rgspelrrrs asdaelsaga egatgseaap pgdlggrtrg
       61 ggrgsaaaaa ttstreaega errgdtpark pdpeagrmdh hqlgtgryqv lhneednses
      121 saveqpstss laaptveaaa sapaldpdsp ppyssitvea pttsdtdvys efypvpppys
      181 vatslptyde aekakaaala aaaadapqrn qeedctprdd fsdveqlrvg ndgifmlaff
      241 mafifnwlgf clsfcitnti agrygaicgf glslikwili vrfsdyftgy fngqywlwwi
      301 flvlglllff rgfvnylkvr nmsesmaaah rtryffll
//
LOCUS       NP_776464                765 aa            linear   MAM 27-APR-2025
DEFINITION  dipeptidyl peptidase 4 [Bos taurus].
ACCESSION   NP_776464
VERSION     NP_776464.1
DBSOURCE    REFSEQ: accession NM_174039.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Antonyan,A.A., Sharoyan,S.G., Mardanyan,S.S. and Galoyan,A.A.
  TITLE     Proline-rich cytokine from neurosecretory granules: a new natural
            substrate for dipeptidyl peptidase IV
  JOURNAL   Neurochem Res 36 (1), 34-38 (2011)
   PUBMED   20838887
  REMARK    GeneRIF: Results describe a proline-rich cytokine from
            neurosecretory granules that represents a new natural substrate for
            Dipeptidyl Peptidase IV (DPPIV).
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Sharoyan,S.G., Antonyan,A.A., Mardanyan,S.S., Lupidi,G.,
            Cuccioloni,M., Angeletti,M. and Cristalli,G.
  TITLE     Complex of dipeptidyl peptidase II with adenosine deaminase
  JOURNAL   Biochemistry (Mosc) 73 (8), 943-949 (2008)
   PUBMED   18774942
  REMARK    GeneRIF: Data demonstrate that dipeptidyl peptidase II can form a
            complex with adenosine deaminase, but with one order of magnitude
            higher dissociation constant than that of DPPIV.
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Dubois,V., Lambeir,A.M., Van der Veken,P., Augustyns,K.,
            Creemers,J., Chen,X., Scharpe,S. and De Meester,I.
  TITLE     Purification and characterization of dipeptidyl peptidase IV-like
            enzymes from bovine testes
  JOURNAL   Front Biosci 13, 3558-3568 (2008)
   PUBMED   18508455
  REMARK    GeneRIF: This and other dipeptidyl peptidases can be isolated from
            bovine testes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 765)
  AUTHORS   Lee,S.U., Park,Y.H., Davis,W.C., Hamilton,J., Naessens,J. and
            Bohach,G.A.
  TITLE     Molecular characterization of bovine CD26 upregulated by a
            staphylococcal superantigen
  JOURNAL   Immunogenetics 54 (3), 216-220 (2002)
   PUBMED   12073152
REFERENCE   6  (residues 1 to 765)
  AUTHORS   Gliddon,D.R. and Howard,C.J.
  TITLE     CD26 is expressed on a restricted subpopulation of dendritic cells
            in vivo
  JOURNAL   Eur J Immunol 32 (5), 1472-1481 (2002)
   PUBMED   11981836
REFERENCE   7  (residues 1 to 765)
  AUTHORS   Lee,S.U., Ferens,W., Davis,W.C., Hamilton,M.J., Park,Y.H.,
            Fox,L.K., Naessens,J. and Bohach,G.A.
  TITLE     Identity of activation molecule 3 on superantigen-stimulated bovine
            cells is CD26
  JOURNAL   Infect Immun 69 (11), 7190-7193 (2001)
   PUBMED   11598101
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF461806.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF461806.1, BC102523.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03145413, SAMN03145414
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="2"
                     /map="2"
     Protein         1..765
                     /product="dipeptidyl peptidase 4"
                     /EC_number="3.4.14.5"
                     /note="dipeptidylpeptidase IV (CD26, adenosine deaminase
                     complexing protein 2); dipeptidyl peptidase IV; activation
                     molecule 3; T-cell activation antigen CD26;
                     dipeptidyl-peptidase 4 (CD26, adenosine deaminase
                     complexing protein 2)"
                     /calculated_mol_wt=88239
     Site            7..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P81425.3)"
     Region          37..57
                     /region_name="DPPIV_rep"
                     /note="Dipeptidyl peptidase IV (DPP IV) low complexity
                     region; pfam18811"
                     /db_xref="CDD:465875"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     Site            91
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     Region          107..477
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Site            149
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     Site            218
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     Site            228
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     Site            320
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     Site            392
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     Site            495
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     Region          558..762
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     Site            684
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P81425.3)"
     CDS             1..765
                     /gene="DPP4"
                     /gene_synonym="ACT3; ADCP-I; CD26; DPPIV; WC10"
                     /coded_by="NM_174039.3:328..2625"
                     /db_xref="GeneID:281122"
                     /db_xref="VGNC:VGNC:106715"
ORIGIN      
        1 mktpwkvllg llaiaalvtv itvpvvlltk gndastdsrr tytladylkn tfrmkfynlr
       61 wvsdheylyk qennillfna eygnssifle nstfdefghs indysvspdr qyilfeynyv
      121 kqwrhsytas ydiydlnkrq liteeripnn tqwitwssvg hklayvwnnd iyvknepnsp
      181 sqritwtgkk dviyngitdw vyeeevfsay salwwspnst flayaqfndt evplieysfy
      241 sdeslqypkt vkipypkaga vnptikffvv nisslspnin atsqqivppg svligdhylc
      301 dvtwvteeri slqwlrriqn ysimdicdyd rstgrwissv grqhieistt gwvgrfrpae
      361 phftsdgnsf ykiisneegy khichfqtdk rnctfitkga wevigiealt sdylyyisne
      421 ykgmpgarnl ykiqlndytk vtclscelnp drcqyysvsf sqeakyyqlr csgpglplyt
      481 lhnsnndkel rvlennsdld qvlqdvqmps kkldfihlhg tkfwyqmilp phfdkskkyp
      541 lllevyagpc sqkadaifrl nwatylaste niivasfdgr gsgyqgdkim hainrrlgtf
      601 evedqieatr qfskmgfvdd kriaiwgwsy ggyvtsmvlg agsgvfkcgi avapvskwey
      661 ydsvyterym glptpednld syrnstvmsr aenfkqveyl lihgtaddnv hfqqsaqisk
      721 alvdagvdfq smwytdedhg iasstahqhi ythmshflkq cfsll
//
LOCUS       NP_058607                464 aa            linear   ROD 27-APR-2025
DEFINITION  sushi-repeat-containing protein SRPX isoform 1 precursor [Mus
            musculus].
ACCESSION   NP_058607 XP_911985 XP_925207 XP_925212
VERSION     NP_058607.1
DBSOURCE    REFSEQ: accession NM_016911.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Inoue,Y., Ueda,M., Tasaki,M., Takeshima,A., Nagatoshi,A.,
            Masuda,T., Misumi,Y., Kosaka,T., Nomura,T., Mizukami,M.,
            Matsumoto,S., Yamashita,T., Takahashi,H., Kakita,A. and Ando,Y.
  TITLE     Sushi repeat-containing protein 1: a novel disease-associated
            molecule in cerebral amyloid angiopathy
  JOURNAL   Acta Neuropathol 134 (4), 605-617 (2017)
   PUBMED   28478503
  REMARK    GeneRIF: SRPX1 co-accumulated with Abeta deposits in cerebral blood
            vessels of all autopsied cases with severe cerebral amyloid
            angiopathy (CAA); no SRPX1 co-accumulated with Abeta deposits in
            senile plaques. Furthermore, we demonstrated that both Abeta40 and
            Abeta42 bound to SRPX1 in vitro and enhanced SRPX1 expression in
            primary cultures of cerebrovascular smooth muscle cells. SRPX1
            enhanced caspase activity induced by Abeta40.
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Tambe,Y., Hasebe,M., Kim,C.J., Yamamoto,A. and Inoue,H.
  TITLE     The drs tumor suppressor regulates glucose metabolism via lactate
            dehydrogenase-B
  JOURNAL   Mol Carcinog 55 (1), 52-63 (2016)
   PUBMED   25620379
  REMARK    GeneRIF: drs regulates glucose metabolism via LDH-B. Downregulating
            drs may contribute to the Warburg effect, which is closely
            associated with malignant progression of cancer cells.
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Tambe,Y., Okuyama,N., Nakagawa,T., Muramoto,A., Hasebe,M., Chano,T.
            and Inoue,H.
  TITLE     Suppression of viral replication by drs tumor suppressor via mTOR
            dependent pathway
  JOURNAL   Cancer Lett 314 (1), 82-91 (2012)
   PUBMED   21983129
  REMARK    GeneRIF: Drs suppresses viral replication via mTOR-dependent
            pathway.
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Tambe,Y., Yamamoto,A., Isono,T., Chano,T., Fukuda,M. and Inoue,H.
  TITLE     The drs tumor suppressor is involved in the maturation process of
            autophagy induced by low serum
  JOURNAL   Cancer Lett 283 (1), 74-83 (2009)
   PUBMED   19368996
  REMARK    GeneRIF: drs is involved in the maturation process of autophagy
            from autophagosomes to autolysosomes
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Tambe,Y., Yoshioka-Yamashita,A., Mukaisho,K., Haraguchi,S.,
            Chano,T., Isono,T., Kawai,T., Suzuki,Y., Kushima,R., Hattori,T.,
            Goto,M., Yamada,S., Kiso,M., Saga,Y. and Inoue,H.
  TITLE     Tumor prone phenotype of mice deficient in a novel
            apoptosis-inducing gene, drs
  JOURNAL   Carcinogenesis 28 (4), 777-784 (2007)
   PUBMED   17088259
  REMARK    GeneRIF: Tumor prone phenotype of mice deficient in a novel
            apoptosis-inducing gene, drs
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Kawai,T., Suzuki,Y., Yamashita,A. and Inoue,H.
  TITLE     Isolation of a novel mouse variant of the drs tumor suppressor gene
  JOURNAL   Cancer Lett 183 (1), 79-86 (2002)
   PUBMED   12049817
  REMARK    GeneRIF: Isolation of a novel variant of the tumor suppressor gene
            (mDRS-2)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX005236.16.
            
            On or before Dec 7, 2005 this sequence version replaced
            XP_925207.1, XP_925212.1, XP_911985.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK034696.1, BC022572.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134, SAMN01164137
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="X"
                     /map="X 4.62 cM"
     Protein         1..464
                     /product="sushi-repeat-containing protein SRPX isoform 1
                     precursor"
                     /note="sushi-repeat-containing protein, X-chromosome;
                     sushi-repeat-containing protein SRPX"
                     /calculated_mol_wt=48419
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3173
     mat_peptide     31..464
                     /product="Sushi-repeat-containing protein SRPX.
                     /id=PRO_0000022417"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R0M3.1)"
                     /calculated_mol_wt=48419
     Site            34
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P78539; propagated from
                     UniProtKB/Swiss-Prot (Q9R0M3.1)"
     Region          <53..175
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          120..175
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(130,148)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          175..257
                     /region_name="HYR"
                     /note="HYR domain; pfam02494"
                     /db_xref="CDD:460572"
     Region          262..317
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(272,291)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          332..451
                     /region_name="DUF4174"
                     /note="Domain of unknown function (DUF4174); pfam13778"
                     /db_xref="CDD:463980"
     CDS             1..464
                     /gene="Srpx"
                     /gene_synonym="drs; drs-1; DRS-1; drs-2; DRS-2"
                     /coded_by="NM_016911.5:101..1495"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS30013.1"
                     /db_xref="GeneID:51795"
                     /db_xref="MGI:MGI:1858306"
ORIGIN      
        1 mgspglrpel llpqvlplll allhvlpsqg fpgsgdsple ddgvwyshsl ykdtpwcspi
       61 kvkygdvycr appggyykta lgtrcdircr kgyelhgssq licqsnkrws dkvickqkrc
      121 ptltmpangg fkcvdgayfn srceyycspg ytlkgertvt cmdnkawsgr pascvdlepp
      181 rikcpsvker iaepnkltvr vswespegrd tadgiltdvi lkglppgsnf pegdhkieyt
      241 vydraenkgt ckfrvkvrvr rcgklnapen gymkcssdgd nygatcefsc iggyelqgsp
      301 arvcqsnlaw sgtepscaam nvnvgvrtaa alldqfyekr rllivstpta rnllyrlqlg
      361 mlqqaqcgld lrhvtvvelv gvfptligri rakimppala lqlrlllrip lysfsmvvvd
      421 khgmdkeryv slvtpmalfn lidtfplrke emilqaemgq tcnv
//
LOCUS       NP_001265441            1101 aa            linear   PRI 27-APR-2025
DEFINITION  AP-3 complex subunit beta-2 isoform 1 [Homo sapiens].
ACCESSION   NP_001265441
VERSION     NP_001265441.1
DBSOURCE    REFSEQ: accession NM_001278512.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Dilber,C., Yucel,G. and Sahin,Y.
  TITLE     Novel homozygous AP3B2 mutations in four individuals with
            developmental and epileptic encephalopathy: A rare clinical entity
  JOURNAL   Clin Neurol Neurosurg 223, 107509 (2022)
   PUBMED   36356440
  REMARK    GeneRIF: Novel homozygous AP3B2 mutations in four individuals with
            developmental and epileptic encephalopathy: A rare clinical entity.
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Yang,F., Jing,F., Li,Y., Kong,S., Zhang,S., Huo,Y., Huang,X. and
            Yu,S.
  TITLE     Plasma lncRNA LOC338963 and mRNA AP3B2 are upregulated in
            paraneoplastic Lambert-Eaton myasthenic syndrome
  JOURNAL   Muscle Nerve 66 (2), 216-222 (2022)
   PUBMED   35508598
  REMARK    GeneRIF: Plasma lncRNA LOC338963 and mRNA AP3B2 are upregulated in
            paraneoplastic Lambert-Eaton myasthenic syndrome.
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Ueda,K., Ogawa,S., Matsuda,K., Hasegawa,Y., Nishi,E., Yanagi,K.,
            Kaname,T., Yamamoto,T. and Okamoto,N.
  TITLE     Blended phenotype of combination of HERC2 and AP3B2 deficiency and
            Angelman syndrome caused by paternal isodisomy of chromosome 15
  JOURNAL   Am J Med Genet A 185 (10), 3092-3098 (2021)
   PUBMED   34042275
  REMARK    GeneRIF: Blended phenotype of combination of HERC2 and AP3B2
            deficiency and Angelman syndrome caused by paternal isodisomy of
            chromosome 15.
REFERENCE   4  (residues 1 to 1101)
  AUTHORS   Honorat,J.A., Lopez-Chiriboga,A.S., Kryzer,T.J., Komorowski,L.,
            Scharf,M., Hinson,S.R., Lennon,V.A., Pittock,S.J., Klein,C.J. and
            McKeon,A.
  TITLE     Autoimmune gait disturbance accompanying adaptor protein-3B2-IgG
  JOURNAL   Neurology 93 (10), e954-e963 (2019)
   PUBMED   31371564
  REMARK    GeneRIF: The AP3B2 antigen was identified in sera and cerebrospinal
            fluid of patients with sensory or cerebellar ataxia.
            Erratum:[Neurology. 2019 Oct 1;93(14):647. doi:
            10.1212/WNL.0000000000008232. PMID: 31467253]
REFERENCE   5  (residues 1 to 1101)
  AUTHORS   Assoum,M., Philippe,C., Isidor,B., Perrin,L., Makrythanasis,P.,
            Sondheimer,N., Paris,C., Douglas,J., Lesca,G., Antonarakis,S.,
            Hamamy,H., Jouan,T., Duffourd,Y., Auvin,S., Saunier,A., Begtrup,A.,
            Nowak,C., Chatron,N., Ville,D., Mireskandari,K., Milani,P.,
            Jonveaux,P., Lemeur,G., Milh,M., Amamoto,M., Kato,M., Nakashima,M.,
            Miyake,N., Matsumoto,N., Masri,A., Thauvin-Robinet,C.,
            Riviere,J.B., Faivre,L. and Thevenon,J.
  TITLE     Autosomal-Recessive Mutations in AP3B2, Adaptor-Related Protein
            Complex 3 Beta 2 Subunit, Cause an Early-Onset Epileptic
            Encephalopathy with Optic Atrophy
  JOURNAL   Am J Hum Genet 99 (6), 1368-1376 (2016)
   PUBMED   27889060
  REMARK    GeneRIF: Autosomal-Recessive Mutations in AP3B2, Adaptor-Related
            Protein Complex 3 Beta 2 Subunit, Cause an Early-Onset Epileptic
            Encephalopathy with Optic Atrophy.
REFERENCE   6  (residues 1 to 1101)
  AUTHORS   Dell'Angelica,E.C., Klumperman,J., Stoorvogel,W. and
            Bonifacino,J.S.
  TITLE     Association of the AP-3 adaptor complex with clathrin
  JOURNAL   Science 280 (5362), 431-434 (1998)
   PUBMED   9545220
REFERENCE   7  (residues 1 to 1101)
  AUTHORS   Simpson,F., Peden,A.A., Christopoulou,L. and Robinson,M.S.
  TITLE     Characterization of the adaptor-related protein complex, AP-3
  JOURNAL   J Cell Biol 137 (4), 835-845 (1997)
   PUBMED   9151686
REFERENCE   8  (residues 1 to 1101)
  AUTHORS   Dell'Angelica,E.C., Ohno,H., Ooi,C.E., Rabinovich,E., Roche,K.W.
            and Bonifacino,J.S.
  TITLE     AP-3: an adaptor-like protein complex with ubiquitous expression
  JOURNAL   EMBO J 16 (5), 917-928 (1997)
   PUBMED   9118953
REFERENCE   9  (residues 1 to 1101)
  AUTHORS   Newman,L.S., McKeever,M.O., Okano,H.J. and Darnell,R.B.
  TITLE     Beta-NAP, a cerebellar degeneration antigen, is a neuron-specific
            vesicle coat protein
  JOURNAL   Cell 82 (5), 773-783 (1995)
   PUBMED   7671305
REFERENCE   10 (residues 1 to 1101)
  AUTHORS   Darnell,R.B., Furneaux,H.M. and Posner,J.B.
  TITLE     Antiserum from a patient with cerebellar degeneration identifies a
            novel protein in Purkinje cells, cortical neurons, and
            neuroectodermal tumors
  JOURNAL   J Neurosci 11 (5), 1224-1230 (1991)
   PUBMED   1851215
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ777385.1, BC143346.1 and
            AF022152.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Adaptor protein complex 3 (AP-3 complex) is a
            heterotrimeric protein complex involved in the formation of
            clathrin-coated synaptic vesicles. The protein encoded by this gene
            represents the beta subunit of the neuron-specific AP-3 complex and
            was first identified as the target antigen in human paraneoplastic
            neurologic disorders. The encoded subunit binds clathrin and is
            phosphorylated by a casein kinase-like protein, which mediates
            synaptic vesicle coat assembly. Defects in this gene are a cause of
            early-onset epileptic encephalopathy. [provided by RefSeq, Feb
            2017].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143346.1, SRR1803614.23017.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000535359.6/ ENSP00000440984.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..1101
                     /product="AP-3 complex subunit beta-2 isoform 1"
                     /note="Neuronal adaptin-like protein, beta-subunit; AP-3
                     complex subunit beta-2; beta-3B-adaptin; adaptor protein
                     complex AP-3 subunit beta-2; neuron-specific vesicle coat
                     protein beta-NAP; clathrin assembly protein complex 3
                     beta-2 large chain; adaptor related protein complex 3 beta
                     2 subunit"
                     /calculated_mol_wt=121058
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13367.2)"
     Region          34..590
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          111..139
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          145..173
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          182..208
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          272..295
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13367.2)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13367.2)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JME5; propagated from
                     UniProtKB/Swiss-Prot (Q13367.2)"
     Region          685..821
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13367.2)"
     Region          822..966
                     /region_name="AP3B1_C"
                     /note="Clathrin-adaptor complex-3 beta-1 subunit
                     C-terminal; pfam14796"
                     /db_xref="CDD:464319"
     CDS             1..1101
                     /gene="AP3B2"
                     /gene_synonym="DEE48; EIEE48; NAPTB"
                     /coded_by="NM_001278512.2:170..3475"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS61737.1"
                     /db_xref="GeneID:8120"
                     /db_xref="HGNC:HGNC:567"
                     /db_xref="MIM:602166"
ORIGIN      
        1 msaapaysed kggsagpgep eyghdpasgg ifssdykrhd dlkemldtnk dslkleamkr
       61 ivamiargkn asdlfpavvk nvacknievk klvyvylvry aeeqqdlall sistfqrglk
      121 dpnqlirasa lrvlssirvp iivpimmlai keaasdmspy vrktaahaip klysldsdqk
      181 dqlieviekl ladkttlvag svvmafeevc peridlihkn yrklcnllid veewgqvvii
      241 smltryartq flsptqnesl leenaekafy gseedeakga gseetaaaaa psrkpyvmdp
      301 dhrlllrntk pllqsrsaav vmavaqlyfh lapkaevgvi akalvrllrs hsevqyvvlq
      361 nvatmsikrr gmfepylksf yirstdptqi kilklevltn lanetniptv lrefqtyirs
      421 mdkdfvaati qaigrcatni grvrdtclng lvqllsnrde lvvaesvvvi kkllqmqpaq
      481 hgeiikhlak ltdniqvpma rasilwlige ycehvpriap dvlrkmaksf taeedivklq
      541 vinlaaklyl tnskqtkllt qyvlslakyd qnydirdrar ftrqlivpse qggalsrhak
      601 klflapkpap vlessfkdrd hfqlgslshl lnakatgyqe lpdwpeeapd psvrnveeed
      661 lsliethvgl lgeytevpew tkcsnrekrk ekekpfysds egesgptesa dsdpeseses
      721 dsksssesgs gesssesdne dqdedeekgr gseseqseed gkrktkkkvp erkgeasssd
      781 egsdssssss esemtsesee eqlepaswsr ktppssksap atkeislldl edftppsvqp
      841 vsppaivsts laadlegltl tdstlvpsll spvsgvgrqe llhrvagegl avdytfsrqp
      901 fsgdphmvsv hihfsnssdt pikglhvgtp klpagisiqe fpeieslapg esatavmgin
      961 fcdstqaanf qlctqtrqfy vsiqppvgel mapvfmsene fkkeqgklmg mneiteklml
     1021 pdtcrsdhiv vqkvtatanl grvpcgtsde yrfagrtltg gslvlltlda rpagaaqltv
     1081 nsekmvigtm lvkdviqalt q
//
LOCUS       NP_001078880             442 aa            linear   PRI 27-APR-2025
DEFINITION  NAD kinase 2, mitochondrial isoform 1 [Homo sapiens].
ACCESSION   NP_001078880
VERSION     NP_001078880.1
DBSOURCE    REFSEQ: accession NM_001085411.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Kim,H., Fu,Z., Yang,Z., Song,Z., Shamsa,E.H., Yumnamcha,T., Sun,S.,
            Liu,W., Ibrahim,A.S., Qi,N.R., Zhang,R. and Zhang,K.
  TITLE     The mitochondrial NAD kinase functions as a major metabolic
            regulator upon increased energy demand
  JOURNAL   Mol Metab 64, 101562 (2022)
   PUBMED   35944895
  REMARK    GeneRIF: The mitochondrial NAD kinase functions as a major
            metabolic regulator upon increased energy demand.
            GeneRIF: Deleting MNADK (NADK2) in mice reduced fat oxidation upon
            energy demand triggered by endurance exercise or fasting. NADK2 is
            a major metabolic regulator upon increased energy demand.
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Mary,C., Soflaee,M.H., Kesavan,R., Gelin,M., Brown,H.,
            Zacharias,G., Mathews,T.P., Lemoff,A., Lionne,C., Labesse,G. and
            Hoxhaj,G.
  TITLE     Crystal structure of human NADK2 reveals a dimeric organization and
            active site occlusion by lysine acetylation
  JOURNAL   Mol Cell 82 (17), 3299-3311 (2022)
   PUBMED   35868311
  REMARK    GeneRIF: Crystal structure of human NADK2 reveals a dimeric
            organization and active site occlusion by lysine acetylation.
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Zhu,J., Schworer,S., Berisa,M., Kyung,Y.J., Ryu,K.W., Yi,J.,
            Jiang,X., Cross,J.R. and Thompson,C.B.
  TITLE     Mitochondrial NADP(H) generation is essential for proline
            biosynthesis
  JOURNAL   Science 372 (6545), 968-972 (2021)
   PUBMED   33888598
  REMARK    GeneRIF: Mitochondrial NADP(H) generation is essential for proline
            biosynthesis.
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Pomerantz,D.J., Ferdinandusse,S., Cogan,J., Cooper,D.N.,
            Reimschisel,T., Robertson,A., Bican,A., McGregor,T., Gauthier,J.,
            Millington,D.S., Andrae,J.L.W., Tschannen,M.R., Helbling,D.C.,
            Demos,W.M., Denis,S., Wanders,R.J.A., Newman,J.N., Hamid,R. and
            Phillips,J.A. 3rd.
  CONSRTM   Collaborators of UDN
  TITLE     Clinical heterogeneity of mitochondrial NAD kinase deficiency
            caused by a NADK2 start loss variant
  JOURNAL   Am J Med Genet A 176 (3), 692-698 (2018)
   PUBMED   29388319
  REMARK    GeneRIF: Our findings also clarify the mechanism underlying NADK2
            deficiency and suggest that this disease should be ruled out in
            cases of hyperlysinemia, especially those with visual loss, and
            neurological phenotypes.
            Review article
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Tort,F., Ugarteburu,O., Torres,M.A., Garcia-Villoria,J., Giros,M.,
            Ruiz,A. and Ribes,A.
  TITLE     Lysine Restriction and Pyridoxal Phosphate Administration in a
            NADK2 Patient
  JOURNAL   Pediatrics 138 (5) (2016)
   PUBMED   27940755
  REMARK    GeneRIF: The use of whole exome sequencing has allowed us to
            identify a new homozygous mutation in NADK2, leading to a premature
            stop codon and absence of protein. To our knowledge this is the
            second reported individual with mutations in NADK2.
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Houten,S.M., Denis,S., Te Brinke,H., Jongejan,A., van Kampen,A.H.,
            Bradley,E.J., Baas,F., Hennekam,R.C., Millington,D.S., Young,S.P.,
            Frazier,D.M., Gucsavas-Calikoglu,M. and Wanders,R.J.
  TITLE     Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes
            dienoyl-CoA reductase deficiency with hyperlysinemia
  JOURNAL   Hum Mol Genet 23 (18), 5009-5016 (2014)
   PUBMED   24847004
  REMARK    GeneRIF: An autosomal recessive defect in NADK2 causes
            mitochondrial NADPH deficiency with secondary deficiencies in
            several mitochondrial processes including polyunsaturated fatty
            acid oxidation and lysine degradation.
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Zhang,R.
  TITLE     MNADK, a novel liver-enriched mitochondrion-localized NAD kinase
  JOURNAL   Biol Open 2 (4), 432-438 (2013)
   PUBMED   23616928
  REMARK    GeneRIF: MNADK is localized to mitochondria in Hep G2 cells, and a
            recombinant MNADK showed NAD kinase activity. MNADK is abundant in
            mitochondrion-rich tissues, such as liver. MNADK expression was
            suppressed in human liver tumors. Identification of MNADK
            immediately suggests a model in which NADK and MNADK are
            responsible for de novo synthesis of NADP(+) in cytosol and
            mitochondria, respectively.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Ohashi,K., Kawai,S. and Murata,K.
  TITLE     Identification and characterization of a human mitochondrial NAD
            kinase
  JOURNAL   Nat Commun 3, 1248 (2012)
   PUBMED   23212377
  REMARK    GeneRIF: exhibits NAD kinase activity, utilizing ATP or inorganic
            polyphosphate, and is localized in mitochondria of HEK293A cells
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008807.10, AI377881.1,
            BC062567.1, BX648388.1, BM990433.1 and HY336341.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a mitochondrial kinase that catalyzes
            the phosphorylation of NAD to yield NADP. Mutations in this gene
            result in 2,4-dienoyl-CoA reductase deficiency. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Oct 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.33485.1,
                                           SRR1803613.280195.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162895, SAMEA2467148
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000381937.9/
                                                  ENSP00000371362.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..442
                     /product="NAD kinase 2, mitochondrial isoform 1"
                     /EC_number="2.7.1.23"
                     /note="NAD kinase domain-containing protein 1,
                     mitochondrial"
                     /calculated_mol_wt=43328
     transit_peptide 1..62
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q4G0N4.2)"
                     /calculated_mol_wt=6123
     Region          24..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G0N4.2)"
     mat_peptide     63..442
                     /product="NAD kinase 2, mitochondrial. /id=PRO_0000296292"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G0N4.2)"
                     /calculated_mol_wt=43328
     Site            76
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C5H8; propagated from
                     UniProtKB/Swiss-Prot (Q4G0N4.2)"
     Region          96..>318
                     /region_name="DAGK_cat"
                     /note="Diacylglycerol kinase catalytic domain; cl01255"
                     /db_xref="CDD:445337"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q4G0N4.2)"
     Site            317
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C5H8; propagated from
                     UniProtKB/Swiss-Prot (Q4G0N4.2)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q4G0N4.2)"
     Site            397
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C5H8; propagated from
                     UniProtKB/Swiss-Prot (Q4G0N4.2)"
     CDS             1..442
                     /gene="NADK2"
                     /gene_synonym="C5orf33; DECRD; MNADK; NADKD1"
                     /coded_by="NM_001085411.3:128..1456"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47197.1"
                     /db_xref="GeneID:133686"
                     /db_xref="HGNC:HGNC:26404"
                     /db_xref="MIM:615787"
ORIGIN      
        1 mtcyrgfllg sccrvaggra aalrgpgagg paarprlggd gggrrhlgqg qprelagcgs
       61 radggfrpsr vvvvakttry efeqqryrya elseedlkql lalkgssysg llerhhihtk
      121 nvehiidslr negievrlvk rreydeetvr wadaviaagg dgtmllaask vldrlkpvig
      181 vntdperseg hlclpvryth sfpealqkfy rgefrwlwrq rirlylegtg inpvpvdlhe
      241 qqlslnqhnr alnierahde rseasgpqll pvralnevfi geslssrasy yeisvddgpw
      301 ekqkssglnl ctgtgskaws fninrvatqa vedvlniakr qgnlslplnr elvekvtney
      361 nesllyspee pkilfsirep ianrvfsssr qrcfsskvcv rsrcwdacmv vdggtsfefn
      421 dgaiasmmin kedelrtvll eq
//
LOCUS       NP_001356469             477 aa            linear   PRI 27-APR-2025
DEFINITION  BDNF/NT-3 growth factors receptor isoform b precursor [Homo
            sapiens].
ACCESSION   NP_001356469
VERSION     NP_001356469.1
DBSOURCE    REFSEQ: accession NM_001369540.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Gupta,R., Dittmeier,M., Wohlleben,G., Nickl,V., Bischler,T.,
            Luzak,V., Wegat,V., Doll,D., Sodmann,A., Bady,E., Langlhofer,G.,
            Wachter,B., Havlicek,S., Gupta,J., Horn,E., Luningschror,P.,
            Villmann,C., Polat,B., Wischhusen,J., Monoranu,C.M., Kuper,J. and
            Blum,R.
  TITLE     Atypical cellular responses mediated by intracellular constitutive
            active TrkB (NTRK2) kinase domains and a solely intracellular
            NTRK2-fusion oncogene
  JOURNAL   Cancer Gene Ther 31 (9), 1357-1379 (2024)
   PUBMED   39039193
  REMARK    GeneRIF: Atypical cellular responses mediated by intracellular
            constitutive active TrkB (NTRK2) kinase domains and a solely
            intracellular NTRK2-fusion oncogene.
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X., Zhang,Y., Yan,H., Yu,H., Zhang,D., Mattay,V.S., Tan,H.Y.
            and Yue,W.
  TITLE     Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2
  JOURNAL   BMC Med 22 (1), 146 (2024)
   PUBMED   38561734
  REMARK    GeneRIF: Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Ikhlef,L., Yassine,M., Chandouri,B., Riviere,L., Naves,T.,
            Dmytruk,N., Gachard,N., Jauberteau,M.O. and Gallet,P.F.
  TITLE     Targeting the NTSR2/TrkB oncogenic pathway in chronic lymphocytic
            leukemia
  JOURNAL   Sci Rep 14 (1), 6084 (2024)
   PUBMED   38480783
  REMARK    GeneRIF: Targeting the NTSR2/TrkB oncogenic pathway in chronic
            lymphocytic leukemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Wang,Y., Liang,J., Xu,B., Yang,J., Wu,Z. and Cheng,L.
  TITLE     TrkB/BDNF signaling pathway and its small molecular agonists in CNS
            injury
  JOURNAL   Life Sci 336, 122282 (2024)
   PUBMED   38008209
  REMARK    GeneRIF: TrkB/BDNF signaling pathway and its small molecular
            agonists in CNS injury.
            Review article
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Luberg,K., Wong,J., Weickert,C.S. and Timmusk,T.
  TITLE     Human TrkB gene: novel alternative transcripts, protein isoforms
            and expression pattern in the prefrontal cerebral cortex during
            postnatal development
  JOURNAL   J Neurochem 113 (4), 952-964 (2010)
   PUBMED   20193039
  REMARK    GeneRIF: Identification of 36 potential TrkB protein isoforms
            suggests high complexity in the synthesis, regulation and function
            of this important neurotrophin receptor emphasizing the need for
            further study of these novel TrkB variants.
REFERENCE   6  (residues 1 to 477)
  AUTHORS   Stoilov,P., Castren,E. and Stamm,S.
  TITLE     Analysis of the human TrkB gene genomic organization reveals novel
            TrkB isoforms, unusual gene length, and splicing mechanism
  JOURNAL   Biochem Biophys Res Commun 290 (3), 1054-1065 (2002)
   PUBMED   11798182
  REMARK    GeneRIF: analysis of TrkB gene reveals novel gene length and
            splicing mechanism
REFERENCE   7  (residues 1 to 477)
  AUTHORS   Haniu,M., Talvenheimo,J., Le,J., Katta,V., Welcher,A. and
            Rohde,M.F.
  TITLE     Extracellular domain of neurotrophin receptor trkB: disulfide
            structure, N-glycosylation sites, and ligand binding
  JOURNAL   Arch Biochem Biophys 322 (1), 256-264 (1995)
   PUBMED   7574684
REFERENCE   8  (residues 1 to 477)
  AUTHORS   Nakagawara,A., Liu,X.G., Ikegaki,N., White,P.S., Yamashiro,D.J.,
            Nycum,L.M., Biegel,J.A. and Brodeur,G.M.
  TITLE     Cloning and chromosomal localization of the human TRK-B tyrosine
            kinase receptor gene (NTRK2)
  JOURNAL   Genomics 25 (2), 538-546 (1995)
   PUBMED   7789988
REFERENCE   9  (residues 1 to 477)
  AUTHORS   Squinto,S.P., Stitt,T.N., Aldrich,T.H., Davis,S., Blanco,S.M.,
            RadzieJewski,C., Glass,D.J., Masiakowski,P., Furth,M.E.,
            Valenzuela,D.M., Distefano,P.S. and Yancopoulos,G.D.
  TITLE     trkB encodes a functional receptor for brain-derived neurotrophic
            factor and neurotrophin-3 but not nerve growth factor
  JOURNAL   Cell 65 (5), 885-893 (1991)
   PUBMED   1710174
REFERENCE   10 (residues 1 to 477)
  AUTHORS   Soppet,D., Escandon,E., Maragos,J., Middlemas,D.S., Reid,S.W.,
            Blair,J., Burton,L.E., Stanton,B.R., Kaplan,D.R., Hunter,T.,
            Nikolics,K. and Parada,L.F.
  TITLE     The neurotrophic factors brain-derived neurotrophic factor and
            neurotrophin-3 are ligands for the trkB tyrosine kinase receptor
  JOURNAL   Cell 65 (5), 895-903 (1991)
   PUBMED   1645620
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390777.13.
            
            Summary: This gene encodes a member of the neurotrophic tyrosine
            receptor kinase (NTRK) family. This kinase is a membrane-bound
            receptor that, upon neurotrophin binding, phosphorylates itself and
            members of the MAPK pathway. Signalling through this kinase leads
            to cell differentiation. Mutations in this gene have been
            associated with obesity and mood disorders. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (p), as well as variants b, o, and
            q-w, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.199242.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465404
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..477
                     /product="BDNF/NT-3 growth factors receptor isoform b
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="BDNF/NT-3 growth factors receptor; tyrosine kinase
                     receptor B; BDNF-tropomyosine receptor kinase B;
                     tropomyosin-related kinase B; neurotrophic tyrosine kinase
                     receptor type 2"
                     /calculated_mol_wt=49372
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3697
     Region          31..60
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; pfam01462"
                     /db_xref="CDD:396168"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          92..150
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          92..113
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          96..116
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          116..137
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Region          117..139
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          140..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          151..195
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          205..283
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          214..218
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          227..230
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          245..252
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            254
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          262..268
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          276..279
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          286..379
                     /region_name="IgI_TrkB_d5"
                     /note="Fifth domain (immunoglobulin-like) of Trk receptor
                     TrkB; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05855"
                     /db_xref="CDD:409441"
     Region          286..294
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409441"
     Region          295..298
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409441"
     Region          301..309
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409441"
     Site            310
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409441"
     Region          312..319
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409441"
     Region          322..325
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409441"
     Site            325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          330..335
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409441"
     Site            order(335,349..350,353)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:409441"
     Site            338
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          341..349
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409441"
     Region          357..365
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409441"
     Region          368..376
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409441"
     Site            412
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Site            431..454
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Region          455..466
                     /region_name="Interaction with MAPK8IP3/JIP3.
                     /evidence=ECO:0000250|UniProtKB:Q63604"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     CDS             1..477
                     /gene="NTRK2"
                     /gene_synonym="DEE58; EIEE58; GP145-TrkB; OBHD; trk-B;
                     TRKB"
                     /coded_by="NM_001369540.1:474..1907"
                     /note="isoform b precursor is encoded by transcript
                     variant p"
                     /db_xref="CCDS:CCDS35053.1"
                     /db_xref="GeneID:4915"
                     /db_xref="HGNC:HGNC:8032"
                     /db_xref="MIM:600456"
ORIGIN      
        1 msswirwhgp amarlwgfcw lvvgfwraaf acptsckcsa sriwcsdpsp givafprlep
       61 nsvdpenite ifianqkrle iineddveay vglrnltivd sglkfvahka flknsnlqhi
      121 nftrnkltsl srkhfrhldl selilvgnpf tcscdimwik tlqeaksspd tqdlyclnes
      181 skniplanlq ipncglpsan laapnltvee gksitlscsv agdpvpnmyw dvgnlvskhm
      241 netshtqgsl ritnissdds gkqiscvaen lvgedqdsvn ltvhfaptit flesptsdhh
      301 wcipftvkgn pkpalqwfyn gailneskyi ctkihvtnht eyhgclqldn pthmnngdyt
      361 liakneygkd ekqisahfmg wpgiddganp nypdviyedy gtaandigdt tnrsneipst
      421 dvtdktgreh lsvyavvvia svvgfcllvm lfllklarhs kfgmkgfvlf hkipldg
//
LOCUS       NP_001355185             139 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 234 isoform 2 precursor [Mus musculus].
ACCESSION   NP_001355185
VERSION     NP_001355185.1
DBSOURCE    REFSEQ: accession NM_001368256.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Tang,T., Li,L., Tang,J., Li,Y., Lin,W.Y., Martin,F., Grant,D.,
            Solloway,M., Parker,L., Ye,W., Forrest,W., Ghilardi,N., Oravecz,T.,
            Platt,K.A., Rice,D.S., Hansen,G.M., Abuin,A., Eberhart,D.E.,
            Godowski,P., Holt,K.H., Peterson,A., Zambrowicz,B.P. and de
            Sauvage,F.J.
  TITLE     A mouse knockout library for secreted and transmembrane proteins
  JOURNAL   Nat Biotechnol 28 (7), 749-755 (2010)
   PUBMED   20562862
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL671759.10.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3463742.1, BY264863.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 63.26 cM"
     Protein         1..139
                     /product="transmembrane protein 234 isoform 2 precursor"
                     /calculated_mol_wt=12472
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2340
     Site            1..21
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R1E7.1)"
     Region          18..125
                     /region_name="TMEM234"
                     /note="Putative transmembrane family 234; pfam10639"
                     /db_xref="CDD:371174"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R1E7.1)"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R1E7.1)"
     CDS             1..139
                     /gene="Tmem234"
                     /gene_synonym="1500002D11Rik; 2510006D16Rik;
                     4933407D05Rik"
                     /coded_by="NM_001368256.1:37..456"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:76799"
                     /db_xref="MGI:MGI:1924049"
ORIGIN      
        1 maaswgqvla lvlvaalwgg tqpllkrass gleqvrertw awqllqeika lfgnteylmp
       61 fllnqsgsll yyltlastdl tlavpicnsl aivftlivgk vlgediggka vagmvltitg
      121 itvcitssvs ktqgqpshs
//
LOCUS       NP_872310                265 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 270 [Homo sapiens].
ACCESSION   NP_872310
VERSION     NP_872310.2
DBSOURCE    REFSEQ: accession NM_182504.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Osborne,L.R., Martindale,D., Scherer,S.W., Shi,X.M., Huizenga,J.,
            Heng,H.H., Costa,T., Pober,B., Lew,L., Brinkman,J., Rommens,J.,
            Koop,B. and Tsui,L.C.
  TITLE     Identification of genes from a 500-kb region at 7q11.23 that is
            commonly deleted in Williams syndrome patients
  JOURNAL   Genomics 36 (2), 328-336 (1996)
   PUBMED   8812460
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY372053.1 and AC093168.3.
            
            On Jul 24, 2007 this sequence version replaced NP_872310.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY372053.1, SRR5189667.251548.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000320531.3/ ENSP00000316775.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..265
                     /product="transmembrane protein 270"
                     /note="Williams-Beuren syndrome critical region 28;
                     williams-Beuren syndrome chromosomal region 28 protein;
                     Williams-Beuren syndrome chromosome region 28"
                     /calculated_mol_wt=29302
     Region          1..265
                     /region_name="WBS28"
                     /note="Williams-Beuren syndrome chromosomal region 28
                     protein homolog; pfam15164"
                     /db_xref="CDD:464540"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UE05.2)"
     Site            130..150
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UE05.2)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UE05.2)"
     Region          229..265
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UE05.2)"
     CDS             1..265
                     /gene="TMEM270"
                     /gene_synonym="WBSCR28"
                     /coded_by="NM_182504.4:37..834"
                     /db_xref="CCDS:CCDS43597.1"
                     /db_xref="GeneID:135886"
                     /db_xref="HGNC:HGNC:23018"
                     /db_xref="MIM:612547"
ORIGIN      
        1 mealppvrss llgillqvtr lsvllvqnrd hlynflllki nlfnhwvsgl aqeargscnw
       61 qahlplgaaa cplgqalwag laliqvpvwl vlqgprlmwa gmwgstkglg lallsaweql
      121 glsvaiwtdl flsclhglml valllvvvtw rvcqkshcfr lgrqlskalq vncvvrkllv
      181 qlrrlywwve tmtaltswhl aylitwttcl ashllqaafe httqlaeaqe vepqevsgss
      241 llpslsassd sesgtvlpeq etpre
//
LOCUS       NP_932140                480 aa            linear   ROD 27-APR-2025
DEFINITION  REST corepressor 1 [Mus musculus].
ACCESSION   NP_932140 XP_006515823 XP_127140
VERSION     NP_932140.2
DBSOURCE    REFSEQ: accession NM_198023.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Ramirez,M., Badayeva,Y., Yeung,J., Wu,J., Abdalla-Wyse,A., Yang,E.,
            Trost,B., Scherer,S.W. and Goldowitz,D.
  CONSRTM   FANTOM 5 Consortium
  TITLE     Temporal analysis of enhancers during mouse cerebellar development
            reveals dynamic and novel regulatory functions
  JOURNAL   Elife 11, e74207 (2022)
   PUBMED   35942939
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Xiong,Y., Wang,L., Di Giorgio,E., Akimova,T., Beier,U.H., Han,R.,
            Trevisanut,M., Kalin,J.H., Cole,P.A. and Hancock,W.W.
  TITLE     Inhibiting the coregulator CoREST impairs Foxp3+ Treg function and
            promotes antitumor immunity
  JOURNAL   J Clin Invest 130 (4), 1830-1842 (2020)
   PUBMED   31917688
  REMARK    GeneRIF: Inhibiting the coregulator CoREST impairs Foxp3+ Treg
            function and promotes antitumor immunity.
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Zhang,C., Leng,F., Saxena,L., Hoang,N., Yu,J., Alejo,S., Lee,L.,
            Qi,D., Lu,F., Sun,H. and Zhang,H.
  TITLE     Proteolysis of methylated SOX2 protein is regulated by L3MBTL3 and
            CRL4DCAF5 ubiquitin ligase
  JOURNAL   J Biol Chem 294 (2), 476-489 (2019)
   PUBMED   30442713
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Elsen,G.E., Bedogni,F., Hodge,R.D., Bammler,T.K., MacDonald,J.W.,
            Lindtner,S., Rubenstein,J.L.R. and Hevner,R.F.
  TITLE     The Epigenetic Factor Landscape of Developing Neocortex Is
            Regulated by Transcription Factors Pax6--> Tbr2--> Tbr1
  JOURNAL   Front Neurosci 12, 571 (2018)
   PUBMED   30186101
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Hara,Y., Nagase,T.,
            Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: I. The complete nucleotide sequences of 100 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 9 (5), 179-188 (2002)
   PUBMED   12465718
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Grimes,J.A., Nielsen,S.J., Battaglioli,E., Miska,E.A., Speh,J.C.,
            Berry,D.L., Atouf,F., Holdener,B.C., Mandel,G. and Kouzarides,T.
  TITLE     The co-repressor mSin3A is a functional component of the
            REST-CoREST repressor complex
  JOURNAL   J Biol Chem 275 (13), 9461-9467 (2000)
   PUBMED   10734093
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Ko,M.S., Threat,T.A., Wang,X., Horton,J.H., Cui,Y., Wang,X.,
            Pryor,E., Paris,J., Wells-Smith,J., Kitchen,J.R., Rowe,L.B.,
            Eppig,J., Satoh,T., Brant,L., Fujiwara,H., Yotsumoto,S. and
            Nakashima,H.
  TITLE     Genome-wide mapping of unselected transcripts from extraembryonic
            tissue of 7.5-day mouse embryos reveals enrichment in the t-complex
            and under-representation on the X chromosome
  JOURNAL   Hum Mol Genet 7 (12), 1967-1978 (1998)
   PUBMED   9811942
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Lan,Y., Jiang,R., Shawber,C., Weinmaster,G. and Gridley,T.
  TITLE     The Jagged2 gene maps to chromosome 12 and is a candidate for the
            lgl and sm mutations
  JOURNAL   Mamm Genome 8 (11), 875-876 (1997)
   PUBMED   9341252
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC153152.5 and AC122023.3.
            
            On or before Mar 7, 2019 this sequence version replaced
            XP_006515823.1, NP_932140.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042731.1, SRR7652917.393784.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 60.93 cM"
     Protein         1..480
                     /product="REST corepressor 1"
                     /calculated_mol_wt=52584
     Region          1..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFE3.3)"
     Region          72..251
                     /region_name="Interaction with HDAC1.
                     /evidence=ECO:0000250|UniProtKB:Q9UKL0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFE3.3)"
     Region          99..152
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKL0; propagated from
                     UniProtKB/Swiss-Prot (Q8CFE3.3)"
     Region          188..232
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cl21498"
                     /db_xref="CDD:473887"
     Site            order(189,218..219,221..222,224..226,228..230)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          238..308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFE3.3)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (Q8CFE3.3)"
     Region          290..378
                     /region_name="Interaction with KDM1A.
                     /evidence=ECO:0000250|UniProtKB:Q9UKL0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFE3.3)"
     Region          379..422
                     /region_name="Myb_DNA-binding"
                     /note="Myb-like DNA-binding domain; pfam00249"
                     /db_xref="CDD:459731"
     Region          436..466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFE3.3)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CFE3.3)"
     CDS             1..480
                     /gene="Rcor1"
                     /gene_synonym="5730409O11; 6720480E22Rik; D12Wsu95e;
                     mKIAA0071; Rocr1"
                     /coded_by="NM_198023.3:240..1682"
                     /db_xref="CCDS:CCDS49179.2"
                     /db_xref="GeneID:217864"
                     /db_xref="MGI:MGI:106340"
ORIGIN      
        1 mpamvekgpe vsgkrrgrnt aasaasaaas aasaaasaaa sagtasasaa aaasaaaapn
       61 ngqnkslaaa apngnsgsns weegssgsss deehggggmr vgpqyqaavp dfdpaklarr
      121 sqerdnlgml vwspnqslse akldeyiaia kekhgynmeq algmlfwhkh nieksladlp
      181 nftpfpdewt vedkvlfeqa fsfhgktfhr iqqmlpdksi aslvkfyysw kktrtktsvm
      241 drharkqkre reesedelee tngsnpvdie idpnkeskke vpptetvpqv kkekhstqak
      301 nrakrkppkg mflsqedvea vsanataatt vlrqldmelv sikrqiqnik qtnsalkekl
      361 dggiepyrlp eviqkcnarw tteeqllavq airkygrdfq aisdvignks vvqvknffvn
      421 yrrrfnidev lqeweaehgk detngpanqk pvkspessik ipeeedeaas vldvryasas
//
LOCUS       NP_005052                407 aa            linear   PRI 27-APR-2025
DEFINITION  ribosomal protein uL3-like [Homo sapiens].
ACCESSION   NP_005052
VERSION     NP_005052.1
DBSOURCE    REFSEQ: accession NM_005061.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Bajpai,A.K., Gu,Q., Orgil,B.O., Alberson,N.R., Towbin,J.A.,
            Martinez,H.R., Lu,L. and Purevjav,E.
  TITLE     Exploring the Regulation and Function of Rpl3l in the Development
            of Early-Onset Dilated Cardiomyopathy and Congestive Heart Failure
            Using Systems Genetics Approach
  JOURNAL   Genes (Basel) 15 (1), 53 (2023)
   PUBMED   38254943
  REMARK    GeneRIF: Exploring the Regulation and Function of Rpl3l in the
            Development of Early-Onset Dilated Cardiomyopathy and Congestive
            Heart Failure Using Systems Genetics Approach.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Casabonne,D., Reina,O., Benavente,Y., Becker,N., Maynadie,M.,
            Foretova,L., Cocco,P., Gonzalez-Neira,A., Nieters,A., Boffetta,P.,
            Middeldorp,J.M. and de Sanjose,S.
  TITLE     Single nucleotide polymorphisms of matrix metalloproteinase 9
            (MMP9) and tumor protein 73 (TP73) interact with Epstein-Barr virus
            in chronic lymphocytic leukemia: results from the European
            case-control study EpiLymph
  JOURNAL   Haematologica 96 (2), 323-327 (2011)
   PUBMED   21048031
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Kapp,L.D. and Lorsch,J.R.
  TITLE     The molecular mechanics of eukaryotic translation
  JOURNAL   Annu Rev Biochem 73, 657-704 (2004)
   PUBMED   15189156
  REMARK    Review article
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Mazumder,B., Sampath,P., Seshadri,V., Maitra,R.K., DiCorleto,P.E.
            and Fox,P.L.
  TITLE     Regulated release of L13a from the 60S ribosomal subunit as a
            mechanism of transcript-specific translational control
  JOURNAL   Cell 115 (2), 187-198 (2003)
   PUBMED   14567916
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Daniels,R.J., Peden,J.F., Lloyd,C., Horsley,S.W., Clark,K.,
            Tufarelli,C., Kearney,L., Buckle,V.J., Doggett,N.A., Flint,J. and
            Higgs,D.R.
  TITLE     Sequence, structure and pathology of the fully annotated terminal 2
            Mb of the short arm of human chromosome 16
  JOURNAL   Hum Mol Genet 10 (4), 339-352 (2001)
   PUBMED   11157797
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Van Raay,T.J., Connors,T.D., Klinger,K.W., Landes,G.M. and
            Burn,T.C.
  TITLE     A novel ribosomal protein L3-like gene (RPL3L) maps to the
            autosomal dominant polycystic kidney disease gene region
  JOURNAL   Genomics 37 (2), 172-176 (1996)
   PUBMED   8921388
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Burn,T.C., Connors,T.D., Van Raay,T.J., Dackowski,W.R.,
            Millholland,J.M., Klinger,K.W. and Landes,G.M.
  TITLE     Generation of a transcriptional map for a 700-kb region surrounding
            the polycystic kidney disease type 1 (PKD1) and tuberous sclerosis
            type 2 (TSC2) disease genes on human chromosome 16p3.3
  JOURNAL   Genome Res 6 (6), 525-537 (1996)
   PUBMED   8828041
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005363.1.
            
            Summary: This gene encodes a protein that shares sequence
            similarity with ribosomal protein L3. The protein belongs to the
            L3P family of ribosomal proteins. Unlike the ubiquitous expression
            of ribosomal protein genes, this gene has a tissue-specific pattern
            of expression, with the highest levels of expression in skeletal
            muscle and heart. It is not currently known whether the encoded
            protein is a functional ribosomal protein or whether it has evolved
            a function that is independent of the ribosome. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050413.1, SRR5189655.26801.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA1970526 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268661.8/ ENSP00000268661.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..407
                     /product="ribosomal protein uL3-like"
                     /note="60S ribosomal protein L3-like; large ribosomal
                     subunit protein uL3-like"
                     /calculated_mol_wt=46165
     Region          1..398
                     /region_name="PTZ00103"
                     /note="60S ribosomal protein L3; Provisional"
                     /db_xref="CDD:240267"
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92901.3)"
     Region          387..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92901.3)"
     CDS             1..407
                     /gene="RPL3L"
                     /gene_synonym="CMD2D"
                     /coded_by="NM_005061.3:59..1282"
                     /db_xref="CCDS:CCDS10450.1"
                     /db_xref="GeneID:6123"
                     /db_xref="HGNC:HGNC:10351"
                     /db_xref="MIM:617416"
ORIGIN      
        1 mshrkfsapr hghlgflphk rshrhrgkvk twprddpsqp vhltaflgyk agmthtlrev
       61 hrpglkiskr eeveavtive tpplvvvgvv gyvatprglr sfktifaehl sdecrrrfyk
      121 dwhkskkkaf tkackrwrdt dgkkqlqkdf aamkkyckvi rvivhtqmkl lpfrqkkahi
      181 meiqlnggtv aekvawaqar lekqvpvhsv fsqsevidvi avtkgrgvkg vtsrwhtkkl
      241 prkthkglrk vacigawhpa rvgcsiarag qkgyhhrtel nkkifrigrg phmedgklvk
      301 nnastsydvt aksitplggf phygevnndf vmlkgciagt kkrvitlrks llvhhsrqav
      361 enielkfidt tskfghgrfq taqekrafmg pqkkhleket petsgdl
//
LOCUS       NP_078848                552 aa            linear   PRI 27-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 14 isoform 1 [Homo
            sapiens].
ACCESSION   NP_078848
VERSION     NP_078848.2
DBSOURCE    REFSEQ: accession NM_024572.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Zhan,S., Qiu,M., Wei,X., Wei,J., Qin,L., Jiang,B., Wen,Q., Chen,P.,
            Lin,Q., Wei,X., Zhou,Z., Jiang,Y., Liang,X., Li,R., Liu,Y. and
            Yu,H.
  TITLE     Potentially functional genetic variants in ferroptosis-related
            CREB3 and GALNT14 genes predict survival of hepatitis B
            virus-related hepatocellular carcinoma
  JOURNAL   Cancer Med 13 (1), e6848 (2024)
   PUBMED   38151984
  REMARK    GeneRIF: Potentially functional genetic variants in
            ferroptosis-related CREB3 and GALNT14 genes predict survival of
            hepatitis B virus-related hepatocellular carcinoma.
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Chu,Y.D., Fan,T.C., Lai,M.W. and Yeh,C.T.
  TITLE     GALNT14-mediated O-glycosylation on PHB2 serine-161 enhances cell
            growth, migration and drug resistance by activating IGF1R cascade
            in hepatoma cells
  JOURNAL   Cell Death Dis 13 (11), 956 (2022)
   PUBMED   36376274
  REMARK    GeneRIF: GALNT14-mediated O-glycosylation on PHB2 serine-161
            enhances cell growth, migration and drug resistance by activating
            IGF1R cascade in hepatoma cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Li,H.W., Liu,M.B., Jiang,X., Song,T., Feng,S.X., Wu,J.Y., Deng,P.F.
            and Wang,X.Y.
  TITLE     GALNT14 regulates ferroptosis and apoptosis of ovarian cancer
            through the EGFR/mTOR pathway
  JOURNAL   Future Oncol 18 (2), 149-161 (2022)
   PUBMED   34643088
  REMARK    GeneRIF: GALNT14 regulates ferroptosis and apoptosis of ovarian
            cancer through the EGFR/mTOR pathway.
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Yu,Y., Wang,Z., Zheng,Q. and Li,J.
  TITLE     GALNT2/14 overexpression correlate with prognosis and methylation:
            potential therapeutic targets for lung adenocarcinoma
  JOURNAL   Gene 790, 145689 (2021)
   PUBMED   33964375
  REMARK    GeneRIF: GALNT2/14 overexpression correlate with prognosis and
            methylation: potential therapeutic targets for lung adenocarcinoma.
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Lin,W.R. and Yeh,C.T.
  TITLE     GALNT14: An Emerging Marker Capable of Predicting Therapeutic
            Outcomes in Multiple Cancers
  JOURNAL   Int J Mol Sci 21 (4), 1491 (2020)
   PUBMED   32098271
  REMARK    GeneRIF: GALNT14: An Emerging Marker Capable of Predicting
            Therapeutic Outcomes in Multiple Cancers.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Wu,C., Guo,X., Wang,W., Wang,Y., Shan,Y., Zhang,B., Song,W., Ma,S.,
            Ge,J., Deng,H. and Zhu,M.
  TITLE     N-Acetylgalactosaminyltransferase-14 as a potential biomarker for
            breast cancer by immunohistochemistry
  JOURNAL   BMC Cancer 10, 123 (2010)
   PUBMED   20356418
  REMARK    GeneRIF: Results provide evidence that GalNAc-T14 may be a
            potential biomarker for breast cancer by immunohistochemistry.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Stern,H.M., Padilla,M., Wagner,K., Amler,L. and Ashkenazi,A.
  TITLE     Development of immunohistochemistry assays to assess GALNT14 and
            FUT3/6 in clinical trials of dulanermin and drozitumab
  JOURNAL   Clin Cancer Res 16 (5), 1587-1596 (2010)
   PUBMED   20179215
  REMARK    GeneRIF: GALNT14 and FUT3/6 H-scores were significantly higher in
            non-small cell lung cancer cell lines sensitive to dulanermin and
            drozitumab versus resistant cell lines
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Wu,C., Shan,Y., Liu,X., Song,W., Wang,J., Zou,M., Wang,M. and Xu,D.
  TITLE     GalNAc-T14 may be involved in regulating the apoptotic action of
            IGFBP-3
  JOURNAL   J Biosci 34 (3), 389-395 (2009)
   PUBMED   19805900
  REMARK    GeneRIF: GALNT14 may be involved in regulating the apoptotic action
            of IGFBP-3.
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Wu,C., Yao,G., Zou,M., Chen,G., Wang,M., Liu,J., Wang,J. and Xu,D.
  TITLE     N-Acetylgalactosaminyltransferase 14, a novel insulin-like growth
            factor binding protein-3 binding partner
  JOURNAL   Biochem Biophys Res Commun 357 (2), 360-365 (2007)
   PUBMED   17434446
  REMARK    GeneRIF: The role of GalNAc-T14 as an intracellular mediator of the
            effects of IGFBP-3 need to be verified in future studies.
REFERENCE   10 (residues 1 to 552)
  AUTHORS   Wang,H., Tachibana,K., Zhang,Y., Iwasaki,H., Kameyama,A., Cheng,L.,
            Guo,Jm., Hiruma,T., Togayachi,A., Kudo,T., Kikuchi,N. and
            Narimatsu,H.
  TITLE     Cloning and characterization of a novel UDP-GalNAc:polypeptide
            N-acetylgalactosaminyltransferase, pp-GalNAc-T14
  JOURNAL   Biochem Biophys Res Commun 300 (3), 738-744 (2003)
   PUBMED   12507512
  REMARK    GeneRIF: cloning and characterization; results provide evidence
            that pp-GalNAc-T14 is a new member of the pp-GalNAc-T family and
            suggest that it may be involved in the O-glycosylation in kidney
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC010659.1 and AY358758.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2005 this sequence version replaced NP_078848.1.
            
            Summary: This gene encodes a Golgi protein which is a member of the
            polypeptide N-acetylgalactosaminyltransferase (ppGalNAc-Ts) protein
            family. These enzymes catalyze the transfer of
            N-acetyl-D-galactosamine (GalNAc) to the hydroxyl groups on serines
            and threonines in target peptides. The encoded protein has been
            shown to transfer GalNAc to large proteins like mucins. Alterations
            in this gene may play a role in cancer progression and response to
            chemotherapy. [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358758.1, BC010659.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000349752.10/ ENSP00000288988.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.1"
     Protein         1..552
                     /product="polypeptide N-acetylgalactosaminyltransferase 14
                     isoform 1"
                     /EC_number="2.4.1.41"
                     /note="UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase T10; polypeptide
                     N-acetylgalactosaminyltransferase 15; pp-GaNTase 14;
                     polypeptide GalNAc transferase 14; protein-UDP
                     acetylgalactosaminyltransferase 14; UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase 14;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 14 (GalNAc-T14)"
                     /calculated_mol_wt=64190
     Site            7..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FL9.1)"
     Region          110..215
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FL9.1)"
     Region          114..408
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(118..120,122,151,176,179,183,199..201,282..283,
                     305..306,308,333,336,341)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(199,201,333)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          274..336
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FL9.1)"
     Region          413..552
                     /region_name="beta-trefoil_Ricin_GALNT14"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide N-acetylgalactosaminyltransferase 14
                     (GALNT14) and similar proteins; cd23478"
                     /db_xref="CDD:467356"
     Site            order(432..435,445,447,450,459..460)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467356"
     Site            order(478..481,489,491,494,499..500)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467356"
     Site            order(519..522,534,536,539,544..545)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467356"
     CDS             1..552
                     /gene="GALNT14"
                     /gene_synonym="GalNac-T10; GalNac-T14; GALNT15"
                     /coded_by="NM_024572.4:355..2013"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1773.2"
                     /db_xref="GeneID:79623"
                     /db_xref="HGNC:HGNC:22946"
                     /db_xref="MIM:608225"
ORIGIN      
        1 mrrltrrlvl pvfgvlwitv llffwvtkrk levptgpevq tpkpsdadwd dlwdqfderr
       61 ylnakkwrvg ddpyklyafn qreserissn raipdtrhlr ctllvyctdl pptsiiitfh
      121 nearstllrt irsvlnrtpt hlireiilvd dfsndpddck qliklpkvkc lrnnerqglv
      181 rsrirgadia qgttltflds hcevnrdwlq pllhrvkedy trvvcpvidi inldtftyie
      241 saselrggfd wslhfqweql speqkarrld ptepirtpii agglfvidka wfdylgkydm
      301 dmdiwggenf eisfrvwmcg gsleivpcsr vghvfrkkhp yvfpdgnant yikntkrtae
      361 vwmdeykqyy yaarpfaler pfgnvesrld lrknlrcqsf kwyleniype lsipkessiq
      421 kgnirqrqkc lesqrqnnqe tpnlklspca kvkgedaksq vwaftytqqi lqeelclsvi
      481 tlfpgapvvl vlckngddrq qwtktgshie hiashlcldt dmfgdgteng keivvnpces
      541 slmsqhwdmv ss
//
LOCUS       NP_001120646             196 aa            linear   PRI 27-APR-2025
DEFINITION  protein maestro isoform b [Homo sapiens].
ACCESSION   NP_001120646
VERSION     NP_001120646.1
DBSOURCE    REFSEQ: accession NM_001127174.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Kenigsberg,S., Lima,P.D., Maghen,L., Wyse,B.A., Lackan,C.,
            Cheung,A.N., Tsang,B.K. and Librach,C.L.
  TITLE     The elusive MAESTRO gene: Its human reproductive tissue-specific
            expression pattern
  JOURNAL   PLoS One 12 (4), e0174873 (2017)
   PUBMED   28406912
  REMARK    GeneRIF: study also shows a punctate nuclear expression pattern and
            disperse cytoplasmic expression pattern of the MRO protein in human
            granulosa-cumulus cells and in testicular germ cells, which was
            later validated by western blotting
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
  REMARK    GeneRIF: The sequence and function of the related mouse gene are
            described.
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Yanaihara,N., Kohno,T., Takakura,S., Takei,K., Otsuka,A.,
            Sunaga,N., Takahashi,M., Yamazaki,M., Tashiro,H., Fukuzumi,Y.,
            Fujimori,Y., Hagiwara,K., Tanaka,T. and Yokota,J.
  TITLE     Physical and transcriptional map of a 311-kb segment of chromosome
            18q21, a candidate lung tumor suppressor locus
  JOURNAL   Genomics 72 (2), 169-179 (2001)
   PUBMED   11401430
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015864.5.
            
            Summary: This gene is specifically transcribed in males before and
            after differentiation of testis, and the encoded protein may play
            an important role in a mammalian sex determination. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX114686.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..196
                     /product="protein maestro isoform b"
                     /note="beside the Ma29 deletion; protein maestro;
                     male-specific transcription in the developing reproductive
                     organs"
                     /calculated_mol_wt=22885
     CDS             1..196
                     /gene="MRO"
                     /gene_synonym="B29; C18orf3"
                     /coded_by="NM_001127174.3:77..667"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45869.1"
                     /db_xref="GeneID:83876"
                     /db_xref="HGNC:HGNC:24121"
                     /db_xref="MIM:608080"
ORIGIN      
        1 mdqrqrrilg qplsiptsqp kqkrtsmisf fskvswklrf qkreplknvf filaerardp
       61 sakkrhmamr nlgtmayeap dkvrkykkiv ldllvyglyd pvnlevihes mktltvvlgk
      121 iqgkglgsff iditlqtrtl lddackttfq acspylklke eysfqseedq rntklyqqls
      181 hyhpeilqff yankil
//
LOCUS       NP_006485                548 aa            linear   PRI 27-APR-2025
DEFINITION  ETS domain-containing transcription factor ERF isoform 1 [Homo
            sapiens].
ACCESSION   NP_006485
VERSION     NP_006485.2
DBSOURCE    REFSEQ: accession NM_006494.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Dentici,M.L., Niceta,M., Lepri,F.R., Mancini,C., Priolo,M.,
            Bonnard,A.A., Cappelletti,C., Leoni,C., Ciolfi,A., Pizzi,S.,
            Cordeddu,V., Rossi,C., Ferilli,M., Mucciolo,M., Colona,V.L.,
            Fauth,C., Bellini,M., Biasucci,G., Sinibaldi,L., Briuglia,S.,
            Gazzin,A., Carli,D., Memo,L., Trevisson,E., Schiavariello,C.,
            Luca,M., Novelli,A., Michot,C., Sweertvaegher,A., Germanaud,D.,
            Scarano,E., De Luca,A., Zampino,G., Zenker,M., Mussa,A.,
            Dallapiccola,B., Cave,H., Digilio,M.C. and Tartaglia,M.
  TITLE     Loss-of-function variants in ERF are associated with a Noonan
            syndrome-like phenotype with or without craniosynostosis
  JOURNAL   Eur J Hum Genet 32 (8), 954-963 (2024)
   PUBMED   38824261
  REMARK    GeneRIF: Loss-of-function variants in ERF are associated with a
            Noonan syndrome-like phenotype with or without craniosynostosis.
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Bao,X., Gao,Y., Wang,Z., Ye,Y., Chen,D., Zuo,Y., Zhao,C. and Xu,X.
  TITLE     Activation of gamma-globin expression by LncRNA-mediated ERF
            promoter hypermethylation in beta-thalassemia
  JOURNAL   Clin Epigenetics 16 (1), 12 (2024)
   PUBMED   38218889
  REMARK    GeneRIF: Activation of gamma-globin expression by LncRNA-mediated
            ERF promoter hypermethylation in beta-thalassemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Gupta,N., Song,H., Wu,W., Ponce,R.K., Lin,Y.K., Kim,J.W.,
            Small,E.J., Feng,F.Y., Huang,F.W. and Okimoto,R.A.
  TITLE     The CIC-ERF co-deletion underlies fusion-independent activation of
            ETS family member, ETV1, to drive prostate cancer progression
  JOURNAL   Elife 11, e77072 (2022)
   PUBMED   36383412
  REMARK    GeneRIF: The CIC-ERF co-deletion underlies fusion-independent
            activation of ETS family member, ETV1, to drive prostate cancer
            progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Care,H., Luscombe,C., Wall,S.A., Dalton,L., Johnson,D. and
            Wilkie,A.O.M.
  TITLE     Cognitive, Behavioural, Speech, Language and Developmental Outcomes
            Associated with Pathogenic Variants in the ERF Gene
  JOURNAL   J Craniofac Surg 33 (6), 1847-1852 (2022)
   PUBMED   35761471
  REMARK    GeneRIF: Cognitive, Behavioural, Speech, Language and Developmental
            Outcomes Associated with Pathogenic Variants in the ERF Gene.
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Singh,R., Cohen,A.S.A., Poulton,C., Hjortshoj,T.D.,
            Akahira-Azuma,M., Mendiratta,G., Khan,W.A., Azmanov,D.N.,
            Woodward,K.J., Kirchhoff,M., Shi,L., Edelmann,L., Baynam,G.,
            Scott,S.A. and Jabs,E.W.
  TITLE     Deletion of ERF and CIC causes abnormal skull morphology and global
            developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 7 (3), a005991 (2021)
   PUBMED   34117072
  REMARK    GeneRIF: Deletion of ERF and CIC causes abnormal skull morphology
            and global developmental delay.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Dintilhac,A. and Bernues,J.
  TITLE     HMGB1 interacts with many apparently unrelated proteins by
            recognizing short amino acid sequences
  JOURNAL   J Biol Chem 277 (9), 7021-7028 (2002)
   PUBMED   11748221
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Le Gallic,L., Sgouras,D., Beal,G. Jr. and Mavrothalassitis,G.
  TITLE     Transcriptional repressor ERF is a Ras/mitogen-activated protein
            kinase target that regulates cellular proliferation
  JOURNAL   Mol Cell Biol 19 (6), 4121-4133 (1999)
   PUBMED   10330152
REFERENCE   8  (residues 1 to 548)
  AUTHORS   de Castro,C.M., Rabe,S.M., Langdon,S.D., Fleenor,D.E.,
            Slentz-Kesler,K., Ahmed,M.N., Qumsiyeh,M.B. and Kaufman,R.E.
  TITLE     Genomic structure and chromosomal localization of the novel ETS
            factor, PE-2 (ERF)
  JOURNAL   Genomics 42 (2), 227-235 (1997)
   PUBMED   9192842
REFERENCE   9  (residues 1 to 548)
  AUTHORS   Liu,D., Pavlopoulos,E., Modi,W., Moschonas,N. and
            Mavrothalassitis,G.
  TITLE     ERF: genomic organization, chromosomal localization and promoter
            analysis of the human and mouse genes
  JOURNAL   Oncogene 14 (12), 1445-1451 (1997)
   PUBMED   9136988
REFERENCE   10 (residues 1 to 548)
  AUTHORS   Sgouras,D.N., Athanasiou,M.A., Beal,G.J. Jr., Fisher,R.J.,
            Blair,D.G. and Mavrothalassitis,G.J.
  TITLE     ERF: an ETS domain protein with strong transcriptional repressor
            activity, can suppress ets-associated tumorigenesis and is
            regulated by phosphorylation during cell cycle and mitogenic
            stimulation
  JOURNAL   EMBO J 14 (19), 4781-4793 (1995)
   PUBMED   7588608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC371332.1, U15655.1,
            BC022231.1 and AW005463.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 17, 2007 this sequence version replaced NP_006485.1.
            
            Summary: ETS2 is a transcription factor and protooncogene involved
            in development, apoptosis, and the regulation of telomerase. The
            protein encoded by this gene binds to the ETS2 promoter and is a
            strong repressor of ETS2 transcription. Several transcript variants
            encoding two different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U15655.1, BC022231.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152798, SAMEA2156099
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222329.9/ ENSP00000222329.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..548
                     /product="ETS domain-containing transcription factor ERF
                     isoform 1"
                     /note="ETS domain-containing transcription factor ERF"
                     /calculated_mol_wt=58572
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Region          26..111
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     Region          <126..383
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          130..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50548.2)"
     Region          184..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50548.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Region          280..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50548.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P50548.2)"
     Region          342..478
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50548.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Region          492..548
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50548.2)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:7588608,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50548.2)"
     CDS             1..548
                     /gene="ERF"
                     /gene_synonym="CHYTS; CRS4; PE-2; PE2"
                     /coded_by="NM_006494.4:130..1776"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12600.1"
                     /db_xref="GeneID:2077"
                     /db_xref="HGNC:HGNC:3444"
                     /db_xref="MIM:611888"
ORIGIN      
        1 mktpadtgfa fpdwaykpes spgsrqiqlw hfilellrke eyqgviawqg dygefvikdp
       61 devarlwgvr kckpqmnydk lsralryyyn krilhktkgk rftykfnfnk lvlvnypfid
      121 vglaggavpq sappvpsggs hfrfppstps evlsptedpr sppacsssss slfsavvarr
      181 lgrgsvsdcs dgtseleepl gedprarppg ppdlgafrgp plarlphdpg vfrvyprprg
      241 gpeplspfpv splagpgsll ppqlspalpm tpthlaytps ptlspmypsg gggpsgsggg
      301 shfsfspedm krylqahtqs vynyhlspra flhypglvvp qpqrpdkcpl ppmapetppv
      361 pssassssss ssspfkfklq ppplgrrqra agekavagad ksggsaggla egagalappp
      421 pppqikvepi segeseevev tdisdedeed gevfktprap pappkpepge apgasqcmpl
      481 klrfkrrwse dcrleggggp aggfedeged kkvrgegpge aggpltprrv ssdlqhataq
      541 lslehrds
//
LOCUS       NP_001353150             833 aa            linear   PRI 27-APR-2025
DEFINITION  disks large homolog 1 isoform 14 [Homo sapiens].
ACCESSION   NP_001353150
VERSION     NP_001353150.1
DBSOURCE    REFSEQ: accession NM_001366221.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   4  (residues 1 to 833)
  AUTHORS   Veljacic Viskovic,D., Lozic,M., Vukoja,M., Soljic,V., Vukojevic,K.,
            Glavina Durdov,M., Filipovic,N. and Lozic,B.
  TITLE     Spatio-Temporal Expression Pattern of CAKUT Candidate Genes DLG1
            and KIF12 during Human Kidney Development
  JOURNAL   Biomolecules 13 (2), 340 (2023)
   PUBMED   36830709
  REMARK    GeneRIF: Spatio-Temporal Expression Pattern of CAKUT Candidate
            Genes DLG1 and KIF12 during Human Kidney Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 833)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 833)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 833)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 833)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 833)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 833)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.46022.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..833
                     /product="disks large homolog 1 isoform 14"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=91734
     Region          <105..140
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          139..227
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(150..156,173,176,206,210,213..214)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          236..320
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(245..251,268,271,301,305,308..309)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          321..382
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          380..470
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(392..398,409,412,442,446,449..450)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          499..565
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(504,526..527,548)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(507,509,512,521,539..540,559,561..562)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          642..820
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..833
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366221.1:65..2566"
                     /note="isoform 14 is encoded by transcript variant 29"
                     /db_xref="CCDS:CCDS93448.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mnyifgnntl lysrgsrggn tssshgsagp kqkhwakkgs sdelqaepep srwqqivaff
       61 trrhsfidci svatsstqpt eavlpspptv pvipvlpvpa entvilptip qanpppvlvn
      121 tdsletptyv ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga
      181 aaqdgrlrvn dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli
      241 kgpkglgfsi aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt
      301 heeavtalkn tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas
      361 paryspvska vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls
      421 gelrkgdrii svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq
      481 mmnssissgs gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew
      541 wqarqvtpdg esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt
      601 snasdsessy lilitdeygc skggqeeyvl syepvnqqev nytrpviilg pmkdrinddl
      661 isefpdkfgs cvphttrpkr dyevdgrdyh fvtsreqmek diqehkfiea gqynnhlygt
      721 svqsvrevae kgkhcildvs gnaikrlqia qlypisifik pksmenimem nkrlteeqar
      781 ktferamkle qeftehftai vqgdtlediy nqvkqiieeq sgsyiwvpak ekl
//
LOCUS       NP_001019316             855 aa            linear   ROD 27-APR-2025
DEFINITION  cytosolic phospholipase A2 zeta isoform 1 [Mus musculus].
ACCESSION   NP_001019316 XP_195168
VERSION     NP_001019316.1
DBSOURCE    REFSEQ: accession NM_001024145.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Yun,B., Lee,H., Ghosh,M., Cravatt,B.F., Hsu,K.L., Bonventre,J.V.,
            Ewing,H., Gelb,M.H. and Leslie,C.C.
  TITLE     Serine hydrolase inhibitors block necrotic cell death by preventing
            calcium overload of the mitochondria and permeability transition
            pore formation
  JOURNAL   J Biol Chem 289 (3), 1491-1504 (2014)
   PUBMED   24297180
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Ghosh,M., Loper,R., Ghomashchi,F., Tucker,D.E., Bonventre,J.V.,
            Gelb,M.H. and Leslie,C.C.
  TITLE     Function, activity, and membrane targeting of cytosolic
            phospholipase A(2)zeta in mouse lung fibroblasts
  JOURNAL   J Biol Chem 282 (16), 11676-11686 (2007)
   PUBMED   17293613
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Ohto,T., Uozumi,N., Hirabayashi,T. and Shimizu,T.
  TITLE     Identification of novel cytosolic phospholipase A(2)s, murine
            cPLA(2){delta}, {epsilon}, and {zeta}, which form a gene cluster
            with cPLA(2){beta}
  JOURNAL   J Biol Chem 280 (26), 24576-24583 (2005)
   PUBMED   15866882
  REMARK    GeneRIF: murine cytosolic phospholipases A2 delta, epsilon, and
            zeta form a gene cluster with cPLA(2)beta
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL844608.18.
            
            On Jun 19, 2005 this sequence version replaced XP_195168.5.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB195278.1, DQ904008.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 60.31 cM"
     Protein         1..855
                     /product="cytosolic phospholipase A2 zeta isoform 1"
                     /EC_number="3.1.1.4"
                     /note="cytosolic phospholipase A2 zeta; cPLA2-zeta"
                     /calculated_mol_wt=96234
     Region          46..162
                     /region_name="C2_cPLA2"
                     /note="C2 domain present in cytosolic PhosphoLipase A2
                     (cPLA2); cd04036"
                     /db_xref="CDD:176001"
     Site            order(63,66,88,116,118)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176001"
     Region          181..301
                     /region_name="cPLA2_C2"
                     /note="Cytosolic phospholipases A2 C2-domain; pfam18695"
                     /db_xref="CDD:465834"
     Region          300..848
                     /region_name="Patatin_and_cPLA2"
                     /note="Patatins and Phospholipases; cl11396"
                     /db_xref="CDD:416256"
     Site            order(362..363,365,393,685)
                     /site_type="active"
                     /db_xref="CDD:132836"
     Site            391..395
                     /site_type="other"
                     /note="nucleophile elbow"
                     /db_xref="CDD:132836"
     CDS             1..855
                     /gene="Pla2g4f"
                     /gene_synonym="4732472I07Rik; Gm647; Pla2zeta"
                     /coded_by="NM_001024145.3:110..2677"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS16618.1"
                     /db_xref="GeneID:271844"
                     /db_xref="MGI:MGI:2685493"
ORIGIN      
        1 mpwtlqpkwl agkglpllga illrktekse pqwkhrrqet hpyydlqvkv lrarniqhtd
       61 klskadcyvr lwlptasvsp sqtrtvvnss dpewnetfpy qihgavknvl elalydedvl
      121 dsdnvfsilf dtstlqlgqp ctknftrqqd pkeleveftl eksqtpasev vtngvlvahp
      181 clriqgtvtg dktaslgelg srqiqlavpg ayekpqplqp tsepglpvnf tfhvnpvlsp
      241 klhiklqeql qvfhsgpsde leaqtskmdk asillsslpl neeltklvdl eegqqvslrm
      301 kadmsssgdl dlrlgfdlcd geqefldkrk qvaskalqrv mglsealhcd qvpvvavlgs
      361 gggtramtsl ygslaglqel glldavtyls gvsgsswcis tlyrdpswsq kalqgpikya
      421 servcsskig mlspkqfeyy srekrawesr ghsmsftdlw gliieyflnq eenpaklsdq
      481 qetvsqgqnp ypiyasinvh knisgddfae wceftpyevg fpkygayvpt elfgseffmg
      541 rllhfwpepr icylqgmwgs afaaslyeif lklgglslsf ldwhrgsvsv tddwpklrkq
      601 dptrlptrlf tpmssfsqav ldiftsritc aqtfnftrgl cmykdytark dfvvsedawh
      661 shnygypdac pnqltpmkdf lslvdggfai nspfplvlqp qravdlivsf dyslegpfev
      721 lqvtekycrd rgipfpriev dpkdsedpre cylfaeaedp cspivlhfpl vnrtfrthla
      781 pgverqtaee kafgdfiing pdtaygmmdf tyepkefdrl vtlsrynvln nketirhalq
      841 laldrrrqag grvgg
//
LOCUS       NP_775859               1326 aa            linear   PRI 27-APR-2025
DEFINITION  immunoglobulin superfamily member 22 [Homo sapiens].
ACCESSION   NP_775859
VERSION     NP_775859.4
DBSOURCE    REFSEQ: accession NM_173588.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1326)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC103974.6.
            
            On Jan 3, 2019 this sequence version replaced NP_775859.3.
            
            Transcript Variant: This variant (1) represents the protein-coding
            transcript.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1968189
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000513874.6/ ENSP00000421191.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..1326
                     /product="immunoglobulin superfamily member 22"
                     /calculated_mol_wt=147864
     Region          67..157
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          84..88
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          97..101
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          123..127
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          137..142
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          150..153
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          190..223
                     /region_name="THB"
                     /note="Tri-helix bundle domain; pfam18362"
                     /db_xref="CDD:465725"
     Region          235..323
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          265..269
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          293..297
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          307..312
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          316..319
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          329..414
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          357..361
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          384..388
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          398..403
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          420..492
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          436..440
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          448..452
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          473..477
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          487..492
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          521..597
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          543..547
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          568..572
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          582..587
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          617..697
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          625..629
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409406"
     Region          638..642
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409406"
     Region          663..667
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409406"
     Region          677..682
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409406"
     Region          690..693
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409406"
     Region          <727..1160
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          1213..1302
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          1230..1234
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1243..1247
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1268..1272
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1282..1287
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1295..1298
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..1326
                     /gene="IGSF22"
                     /gene_synonym="IGFN2"
                     /coded_by="NM_173588.4:149..4129"
                     /db_xref="CCDS:CCDS41625.2"
                     /db_xref="GeneID:283284"
                     /db_xref="HGNC:HGNC:26750"
ORIGIN      
        1 mttihsrqml qehvsmefss stthvqtfsq ttkivgeevv rrksssivef fslvtrssni
       61 pagdsvpefv ekpqpvtape gdkavfrarv qgnakphisw kresgipike sakifydsin
      121 kehvlklepl tsddsdnykc iasndhadai ytvsllvteg qekmdfkkml kkrappapkk
      181 kqkkvaneke mleilskvpk kdfekvcmey gftdfrgllr klkemkkkve veairilkpl
      241 edketkvdtt vvfdcimelk dpnvkmiwik gteplriqys lgkydvkqmg tkymlvisnv
      301 nmndagiysl svgdkrmsae ltvldeplkf lgemkpvkvt erqtavfeir lskkepnfvw
      361 kfngkelkrd dkyeitvsed glthtlkikd arlsdsgefs aeagnlvqka qltvdripik
      421 fvsnlknvrv kersraclec eltskdvtlr wkkdgqllmh gtkysmnheg kraeliieda
      481 qlsdggeytv vamqdgdpte yystaivtve erlatvksgm sdvhaatgsp aelcvvlnde
      541 kvegvwlkdg keitdlpgmq ivkqgavhkl ifpsmgpehe gkytfrakgt eseasvfiad
      601 pptidpsvle alaahaitvk vghtahikvp frgkplpkvt wykdgmevte eervsmerge
      661 dqalltisnc vredsglill klkndhgsat atlhlsvldr pkppqgrvef lelsgscvhm
      721 kwkapkdngg rpvtqfiver ravgkkswik igevdgkvtn fstnkveegk ayqfrilavn
      781 segvsdplet eevfagnpie ppgfasqpqv tdvtkeavti twnaptqdgg apvlgyiver
      841 rkkgsnlwvp vnkdpiqgtk ctvdglledt eyefrviavn kagpgqpsvp sssvvakdpv
      901 kppglvqdlh vsdssnssis lawrepaegd ppsgyilemr aedtkewskc tkipisgtcy
      961 tvgglierqk yffriravne agvgepveld kgvrampppa apkfdlsarl kshmvvragt
     1021 alcihaafsg spppdviwqk dgvptkgret itksknhsqf linstkrsds gvyrillqne
     1081 fgearydihv rvadfprppt nlrlfeevpn tvtltwnhsp dvqedgeahy iimkrdasta
     1141 twytaaervf snkytvtgll pgrkyyfrvv arneigdsep ldsrdtwlin kdqiqdlsak
     1201 lkpyekkdwr haprfvtplk phtvlrgqdc tmtcaflgnp rptvtlykgd vnitanskfw
     1261 ynstsgvctl viptctlkds gdysvlvene lgkdrssctl tvydkddksv vasiteslqk
     1321 kskhlm
//
LOCUS       NP_001036158             190 aa            linear   PRI 27-APR-2025
DEFINITION  protein shisa-like-2A [Homo sapiens].
ACCESSION   NP_001036158
VERSION     NP_001036158.1
DBSOURCE    REFSEQ: accession NM_001042693.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     Unexpected diversity in Shisa-like proteins suggests the importance
            of their roles as transmembrane adaptors
  JOURNAL   Cell Signal 24 (3), 758-769 (2012)
   PUBMED   22120523
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL356976.30, AK128236.1, AY358621.1 and BG192125.1.
            
            Transcript Variant: This variant (1) encodes the supported protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279847.971.1, AY358621.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000517870.2/ ENSP00000429726.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..190
                     /product="protein shisa-like-2A"
                     /note="membrane protein FAM159A; family with sequence
                     similarity 159 member A"
                     /calculated_mol_wt=20175
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWV7.2)"
     Site            70..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWV7.2)"
     CDS             1..190
                     /gene="SHISAL2A"
                     /gene_synonym="FAM159A; PRO7171; WWLS2783"
                     /coded_by="NM_001042693.3:327..899"
                     /db_xref="CCDS:CCDS41336.1"
                     /db_xref="GeneID:348378"
                     /db_xref="HGNC:HGNC:28757"
                     /db_xref="MIM:620218"
ORIGIN      
        1 msgactsyvs aeqevvrgfs cprpggeaaa vfccgfrdhk yccddphsff pyehsymwwl
       61 sigaliglsv aavvllafiv tacvlcylfi sskphtkldl glslqtagpe evspdcqgvn
      121 tgmaaevpkv splqqsyscl npqlesnegq avnskrllhh cfmatvttsd ipgspeeasv
      181 pnpdlcgpvp
//
LOCUS       NP_001291288            5654 aa            linear   PRI 27-APR-2025
DEFINITION  mucin-5AC precursor [Homo sapiens].
ACCESSION   NP_001291288
VERSION     NP_001291288.1
DBSOURCE    REFSEQ: accession NM_001304359.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 5654)
  AUTHORS   Wu,X., Du,F., Zhang,A., Zhang,G., Xu,R. and Du,X.
  TITLE     KDELR2 is necessary for chronic obstructive pulmonary disease
            airway Mucin5AC hypersecretion via an IRE1alpha/XBP-1s-dependent
            mechanism
  JOURNAL   J Cell Mol Med 28 (19), e70125 (2024)
   PUBMED   39365189
  REMARK    GeneRIF: KDELR2 is necessary for chronic obstructive pulmonary
            disease airway Mucin5AC hypersecretion via an
            IRE1alpha/XBP-1s-dependent mechanism.
REFERENCE   2  (residues 1 to 5654)
  AUTHORS   Sabo,M.C., Thuong,N.T.T., Chang,X., Ardiansyah,E., Tram,T.T.B.,
            Hai,H.T., Nghia,H.D.T., Bang,N.D., Dian,S., Ganiem,A.R.,
            Shaporifar,S., Kumar,V., Li,Z., Hibberd,M., Khor,C.C.,
            Thwaites,G.E., Heemskerk,D., van Laarhoven,A., van Crevel,R.,
            Dunstan,S.J. and Shah,J.A.
  TITLE     MUC5AC Genetic Variation Is Associated With Tuberculous Meningitis
            Cerebral Spinal Fluid Cytokine Responses and Mortality
  JOURNAL   J Infect Dis 228 (3), 343-352 (2023)
   PUBMED   36823694
  REMARK    GeneRIF: MUC5AC Genetic Variation Is Associated With Tuberculous
            Meningitis Cerebral Spinal Fluid Cytokine Responses and Mortality.
REFERENCE   3  (residues 1 to 5654)
  AUTHORS   Khorasani,A.M., Mohammadi,B., Saghafi,M.R., Mohammadi,S.,
            Ghaffari,S., Mirsadraee,M. and Khakzad,M.R.
  TITLE     The association between MUC5AC and MUC5B genes expression and
            remodeling progression in severe neutrophilic asthma: A direct
            relationship
  JOURNAL   Respir Med 213, 107260 (2023)
   PUBMED   37146737
  REMARK    GeneRIF: The association between MUC5AC and MUC5B genes expression
            and remodeling progression in severe neutrophilic asthma: A direct
            relationship.
REFERENCE   4  (residues 1 to 5654)
  AUTHORS   Manne,A., Kasi,A., Esnakula,A.K. and Paluri,R.K.
  TITLE     Predictive Value of MUC5AC Signature in Pancreatic Ductal
            Adenocarcinoma: A Hypothesis Based on Preclinical Evidence
  JOURNAL   Int J Mol Sci 24 (9), 8087 (2023)
   PUBMED   37175794
  REMARK    GeneRIF: Predictive Value of MUC5AC Signature in Pancreatic Ductal
            Adenocarcinoma: A Hypothesis Based on Preclinical Evidence.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 5654)
  AUTHORS   Baumlin,N., Silswal,N., Dennis,J.S., Niloy,A.J., Kim,M.D. and
            Salathe,M.
  TITLE     Nebulized Menthol Impairs Mucociliary Clearance via TRPM8 and
            MUC5AC/MUC5B in Primary Airway Epithelial Cells
  JOURNAL   Int J Mol Sci 24 (2), 1694 (2023)
   PUBMED   36675209
  REMARK    GeneRIF: Nebulized Menthol Impairs Mucociliary Clearance via TRPM8
            and MUC5AC/MUC5B in Primary Airway Epithelial Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 5654)
  AUTHORS   Debailleul,V., Laine,A., Huet,G., Mathon,P., d'Hooghe,M.C.,
            Aubert,J.P. and Porchet,N.
  TITLE     Human mucin genes MUC2, MUC3, MUC4, MUC5AC, MUC5B, and MUC6 express
            stable and extremely large mRNAs and exhibit a variable length
            polymorphism. An improved method to analyze large mRNAs
  JOURNAL   J Biol Chem 273 (2), 881-890 (1998)
   PUBMED   9422745
REFERENCE   7  (residues 1 to 5654)
  AUTHORS   Ho,S.B., Roberton,A.M., Shekels,L.L., Lyftogt,C.T., Niehans,G.A.
            and Toribara,N.W.
  TITLE     Expression cloning of gastric mucin complementary DNA and
            localization of mucin gene expression
  JOURNAL   Gastroenterology 109 (3), 735-747 (1995)
   PUBMED   7657101
REFERENCE   8  (residues 1 to 5654)
  AUTHORS   Lesuffleur,T., Roche,F., Hill,A.S., Lacasa,M., Fox,M.,
            Swallow,D.M., Zweibaum,A. and Real,F.X.
  TITLE     Characterization of a mucin cDNA clone isolated from HT-29
            mucus-secreting cells. The 3' end of MUC5AC?
  JOURNAL   J Biol Chem 270 (23), 13665-13673 (1995)
   PUBMED   7775418
REFERENCE   9  (residues 1 to 5654)
  AUTHORS   Guyonnet Duperat,V., Audie,J.P., Debailleul,V., Laine,A.,
            Buisine,M.P., Galiegue-Zouitina,S., Pigny,P., Degand,P.,
            Aubert,J.P. and Porchet,N.
  TITLE     Characterization of the human mucin gene MUC5AC: a consensus
            cysteine-rich domain for 11p15 mucin genes?
  JOURNAL   Biochem J 305 (Pt 1) (Pt 1), 211-219 (1995)
   PUBMED   7826332
REFERENCE   10 (residues 1 to 5654)
  AUTHORS   Meezaman,D., Charles,P., Daskal,E., Polymeropoulos,M.H.,
            Martin,B.M. and Rose,M.C.
  TITLE     Cloning and analysis of cDNA encoding a major airway glycoprotein,
            human tracheobronchial mucin (MUC5)
  JOURNAL   J Biol Chem 269 (17), 12932-12939 (1994)
   PUBMED   7513696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF015521.1, AJ298317.1, FP326773.16, KC800812.1, AJ001402.1,
            Z48314.1 and BC033831.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2142586,
                              SAMEA2154405 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: PMID: 9422745
            MANE Ensembl match        :: ENST00000621226.2/ ENSP00000485659.1
            RefSeq Select criteria    :: based on single protein-coding
                                         transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..5654
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..5654
                     /product="mucin-5AC precursor"
                     /note="mucin 5, subtypes A and C,
                     tracheobronchial/gastric; tracheobronchial mucin; gastric
                     mucin; major airway glycoprotein; lewis B blood group
                     antigen; mucin-5 subtype AC, tracheobronchial; mucin 5AC,
                     oligomeric mucus/gel-forming pseudogene"
                     /calculated_mol_wt=582674
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
                     /calculated_mol_wt=2918
     Region          27..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     mat_peptide     28..5654
                     /product="Mucin-5AC. /evidence=ECO:0000255.
                     /id=PRO_0000158957"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
                     /calculated_mol_wt=582674
     Region          74..216
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Site            205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Site            258
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Region          265..334
                     /region_name="C8"
                     /note="C8 domain; pfam08742"
                     /db_xref="CDD:462584"
     Region          338..394
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(347,351,364,368)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            415
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Region          423..587
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Site            524
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Region          624..694
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Region          704..761
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(713,717,731,735)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          802..863
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(811,823,834,839)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          892..1051
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Region          1088..1162
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Site            1308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Region          <1335..1576
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1336..1377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          1383..4731
                     /region_name="9 X Cys-rich subdomain repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          1389..1475
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            1389
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          1483..1575
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          1584..1670
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            1584
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          1688..1733
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          1749..1840
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            1749
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          1849..1948
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          1957..2043
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            1957
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          2059..2110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          2122..2213
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            2122
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan.
                     /evidence=ECO:0000269|PubMed:14718370; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Region          2224..3214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          2257..3200
                     /region_name="107 X 8 AA approximate tandem repeats of
                     T-T-S-T-T-S-A-P"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Site            2395
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            2405
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            2451
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            2461
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            2531
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            2541
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            2571
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            2581
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            2699
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            2709
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            2883
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            2893
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            2979
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            2989
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            3067
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            3077
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Region          3228..3319
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            3228
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          3329..3515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          3363..3498
                     /region_name="17 X 8 AA approximate tandem repeats of
                     T-T-S-T-T-S-A-P"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          3526..3617
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            3526
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          3628..3951
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          3661..3931
                     /region_name="34 X 8 AA approximate tandem repeats of
                     T-T-S-T-T-S-A-P"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Site            3774
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Region          3959..4050
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            3959
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          4060..4625
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          4093..4595
                     /region_name="58 X 8 AA approximate tandem repeats of
                     T-T-S-T-T-S-A-P"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Site            4224
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            4234
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            4296
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            4306
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            4320
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            4330
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            4376
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            4386
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            4440
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            4450
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            4480
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            4490
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            4512
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            4522
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Site            4568
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            4578
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine.
                     /evidence=ECO:0000269|PubMed:25939779,
                     ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP; propagated
                     from UniProtKB/Swiss-Prot (P98088.4)"
     Region          4633..4724
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            4633
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Region          4830..4849
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     Site            4869
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Region          4911..5079
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Site            4926..4927
                     /site_type="cleavage"
                     /note="Cleavage; propagated from UniProtKB/Swiss-Prot
                     (P98088.4)"
     Site            4942
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Site            5057
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Site            5093
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Region          5146..5205
                     /region_name="C8"
                     /note="C8 domain; pfam08742"
                     /db_xref="CDD:462584"
     Site            5236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Site            5347
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Site            5377
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Site            5386
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Site            5455
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Site            5528
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Region          5534..5616
                     /region_name="CT"
                     /note="C-terminal cystine knot-like domain (CTCK);
                     smart00041"
                     /db_xref="CDD:214482"
     Site            5591
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P98088.4)"
     Region          5622..5654
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98088.4)"
     CDS             1..5654
                     /gene="MUC5AC"
                     /gene_synonym="leB; MUC5; mucin; TBM"
                     /coded_by="NM_001304359.2:48..17012"
                     /db_xref="CCDS:CCDS76369.1"
                     /db_xref="GeneID:4586"
                     /db_xref="HGNC:HGNC:7515"
                     /db_xref="MIM:158373"
ORIGIN      
        1 msvgrrklal lwalalalac trhtghaqdg ssessykhhp alspiargps gvplrgatvf
       61 pslrtipvvr asnpahngrv cstwgsfhyk tfdgdvfrfp glcnyvfseh cgaayedfni
      121 qlrrsqesaa ptlsrvlmkv dgvviqltkg svlvnghpvl lpfsqsgvli qqsssytkve
      181 arlglvlmwn hddsllleld tkyanktcgl cgdfngmpvv sellshntkl tpmefgnlqk
      241 mddptdqcqd pvpepprncs tgfgiceell hgqlfsgcva lvdvgsylea crqdlcfced
      301 tdllscvcht laeysrqcth agglpqdwrg pdfcpqkcpn nmqyhecrsp cadtcsnqeh
      361 sracedhcva gcfcpegtvl ddigqtgcvp vskcacvyng aayapgatys tdctnctcsg
      421 grwscqevpc pgtcsvlgga hfstfdgkqy tvhgdcsyvl tkpcdssaft vlaelrrcgl
      481 tdsetclksv tlsldgaqtv vvikasgevf lnqiytqlpi saanvtifrp stffiiaqts
      541 lglqlnlqlv ptmqlfmqla pklrgqtcgl cgnfnsiqad dfrtlsgvve ataaaffntf
      601 ktqaacpnir nsfedpcsls venekyaqhw csqltdadgp fgrchaavkp gtyysncmfd
      661 tcncersedc lcaalssyvh acaakgvqlg gwrdgvctkp mttcpksmty hyhvstcqpt
      721 crslsegdit csvgfipvdg cicpkgtfld dtgkcvqasn cpcyhrgsmi pngesvhdsg
      781 aictcthgkl sciggqapap vcaapmvffd crnatpgdtg agcqkschtl dmtcyspqcv
      841 pgcvcpdglv adgeggcita edcpcvhnea syragqtirv gcntctcdsr mwrctddpcl
      901 atcavygdgh yltfdgqsys fngdceytlv qnhcggkdst qdsfrvvten vpcgttgttc
      961 skaikiflgg felklshgkv evigtdesqe vpytirqmgi ylvvdtdigl vllwdkktsi
     1021 finlspefkg rvcglcgnfd diavndfatr srsvvgdvle fgnswklsps cpdalapkdp
     1081 ctanpfrksw aqkqcsilhg ptfaachahv eparyyeacv ndacacdsgg dcecfctava
     1141 ayaqachevg lcvswrtpsi cplfcdyynp egqcewhyqp cgvpclrtcr nprgdclrdv
     1201 rglegcypkc ppeapifded kmqcvatcpt pplpprchvh gksyrpgavv psdkncqscl
     1261 ctergvecty kaeacvctyn gqrfhpgdvi yhttdgtggc isarcgangt ierrvypcsp
     1321 ttpvppttfs fstpplvvss thtpsngpss ahtgppssaw pttagtsprt rlptasaslp
     1381 pvcgekclws pwmdvsrpgr gtdsgdfdtl enlrahgyrv cesprsvecr aedapgvplr
     1441 algqrvqcsp dvgltcrnre qasglcynyq irvqcctplp cstssspaqt tppttsktte
     1501 trasgssaps stpgtvslst arttpapgta tsvkktfstp spppvpatst ssmsttapgt
     1561 svvsskptpt epstssclqe lctwtewidg sypapgingg dfdtfqnlrd egytfcespr
     1621 svqcraesfp ntpladlgqd vicshtegli clnknqlppi cynyeiriqc cetvnvcrdi
     1681 trlpktvatt rptphptgaq tqttftthmp sasteqptat srggptatsv tqgthttlvt
     1741 rnchprctwt kwfdvdfpsp gphggdkety nniirsgeki crrpeeitrl qcrakshpev
     1801 siehlgqvvq csreeglvcr nqdqqgpfkm clnyevrvlc cetprgchmt stpgstsssp
     1861 aqttpsttsk ttetqasgss apsstpgtvs lstarttpap gtatsvkktf stpspppvpa
     1921 tstssmstta pgtsvvsskp tptepstssc lqelctwtew idgsypapgi nggdfdtfqn
     1981 lrdegytfce sprsvqcrae sfpntpladl gqdvicshte gliclnknql ppicynyeir
     2041 iqccetvnvc rditrppktv attrptphpt gaqtqttftt hmpsasteqp tatsrggpta
     2101 tsvtqgthtt pvtrnchprc twttwfdvdf pspgphggdk etynniirsg ekicrrpeei
     2161 trlqcraksh pevsiehlgq vvqcsreegl vcrnqdqqgp fkmclnyevr vlccetpkgc
     2221 pvtstpvtap stpsgratsp tqstsswqks rtttlvttst tstpqtstty ahttsttsap
     2281 tarttsaptt rttsaspast tsgpgntpsp vpttstisap ttsitsaptt sttsaptsst
     2341 tsgpgttpsp vpttsitsap ttsttsaptt sttsartsst tsatttsris gpettpspvp
     2401 ttsttsattt sttsapttst tsaptsstts spqtsttsap ttsttsgpgt tpspvpttst
     2461 tsapttrtts apkssttsaa ttsttsgpet tprpvpttst tsspttstts apttsttsas
     2521 ttsttsgagt tpspvpttst tsapttstts apissttsat ttsttsgpgt tpspvpttst
     2581 tsapttstts gpgttpsavp ttsitsaptt stnsapisst tsatttsris gpettpspvp
     2641 tasttsastt sttsgpgttp spvpttstis vpttsttsas ttsttsastt sttsgpgttp
     2701 spvpttstts apttsttsap ttstisaptt sttsatttst tsaptprrts apttstisas
     2761 ttsttsattt sttsatttst isapttsttl spttsttstt itsttsapis sttstpqtst
     2821 tsapttstts gpgttsspvp ttsttsaptt sttsapttrt tsvptsstts tattsttsgp
     2881 gttpspvptt sttsapttrt tsapttstts apttsttsap tssttsattt stisvpttst
     2941 tsvpgttpsp vpttstisvp ttsttsastt sttsgpgttp spvpttstts apttsttsap
     3001 ttstisaptt stpsapttst tlapttstts apttsttstp tssttsspqt sttsasttsi
     3061 tsgpgttpsp vpttsttsap ttsttsaatt stisapttst tsapttstts astasktsgl
     3121 gttpspiptt sttsppttst tsastaskts gpgttpspvp ttstifaprt sttsasttst
     3181 tpgpgttpsp vpttstasvs ktstshvsis ktthsqpvtr dchlrctwtk wfdidfpspg
     3241 phggdketyn niirsgekic rrpeeitrlq craeshpevs iehlgqvvqc sreeglvcrn
     3301 qdqqgpfkmc lnyevrvlcc etpkgcpvts tpvtapstps gratsptqst sswqksrttt
     3361 lvttsttstp qtsttsaptt sttsapttst tsapttstts tpqtsissap tssttsapts
     3421 stisarttsi isapttstts spttsttsat ttsttsapts sttstpqtsk tsaatsstts
     3481 gsgttpspvt ttstasvskt stshvsvskt thsqpvtrdc hprctwtkwf dvdfpspgph
     3541 ggdketynni irsgekicrr peeitrlqcr akshpevsie hlgqvvqcsr eeglvcrnqd
     3601 qqgpfkmcln yevrvlccet pkgcpvtsts vtapstpsgr atsptqstss wqksrtttlv
     3661 tssitsttqt sttsapttst tpasipstts apttsttsap ttsttsaptt sttstpqttt
     3721 ssaptsstts apttstisap ttstisaptt sttsaptast tsaptstssa pttnttsapt
     3781 tsttsapits tisapttstt stpqtstiss pttsttstpq tsttssptts ttsapttstt
     3841 sapttsttst pqtsissapt ssttsaptas tisapttstt sfhttsttsp ptsstsstpq
     3901 tsktsaatss ttsgsgttps pvpttstasv sktstshvsv sktthsqpvt rdchprctwt
     3961 kwfdvdfpsp gphggdkety nniirsgeki crrpeeitrl qcraeshpev siehlgqvvq
     4021 csreeglvcr nqdqqgpfkm clnyevrvlc cetpkgcpvt stpvtapstp sgratsptqs
     4081 tsswqksrtt tlvttsttst pqtsttsapt tstipastps ttsapttstt sapttsttsa
     4141 pthrttsgpt tsttlaptts ttsapttstn sapttstisa sttstisapt tstissptss
     4201 ttstpqtskt saatssttsg sgttpspvpt tsttsastts ttsapttstt sgpgttpspv
     4261 pststtsaat tsttsapttr ttsaptssmt sgpgttpspv pttsttsapt tsttsgpgtt
     4321 pspvpttstt sapitsttsg pgstpspvpt tsttsaptts ttsastastt sgpgttpspv
     4381 pttsttsapt trttsastas ttsgpgstps pvpttsttsa pttrttpast asttsgpgtt
     4441 pspvpttstt sasttstisl pttsttsapi tsmtsgpgtt pspvpttstt sapttsttsa
     4501 stasttsgpg ttpspvptts ttsapttstt sastasttsg pgtslspvpt tsttsaptts
     4561 ttsgpgttps pvpttsttsa pttsttsgpg ttpspvptts ttpvsktsts hlsvsktths
     4621 qpvtsdchpl cawtkwfdvd fpspgphggd ketynniirs gekicrrpee itrlqcraes
     4681 hpevniehlg qvvqcsreeg lvcrnqdqqg pfkmclnyev rvlccetprg cpvtsvtpyg
     4741 tsptnalyps lstsmvsasv astsvasssv asssvaystq tcfcnvadrl ypagstiyrh
     4801 rdlaghcyya lcsqdcqvvr gvdsdcpstt lppapatsps istsepvtel gcpnavpprk
     4861 kgetwatpnc seatcegnnv islrprtcpr vekptcangy pavkvadqdg cchhyqcqcv
     4921 csgwgdphyi tfdgtyytfl dnctyvlvqq ivpvyghfrv lvdnyfcgae dglscprsii
     4981 leyhqdrvvl trkpvhgvmt neiifnnkvv spgfrkngiv vsrigvkmya tipelgvqvm
     5041 fsglifsvev pfskfannte gqcgtctndr kdecrtprgt vvascsemsg lwnvsipdqp
     5101 achrphptpt tvgpttvgst tvgpttvgst tvgpttppap clpspicqli lskvfepcht
     5161 vippllfyeg cvfdrchmtd ldvvcsslel yaalcashdi cidwrgrtgh mcpftcpadk
     5221 vyqpcgpsnp sycygndsas lgalpeagpi tegcfcpegm tlfstsaqvc vptgcprclg
     5281 phgepvkvgh tvgmdcqect ceaatwtltc rpklcplppa cplpgfvpvp aapqagqccp
     5341 qyscacntsr cpapvgcpeg araiptyqeg accpvqncsw tvcsingtly qpgavvsssl
     5401 cetcrcelpg gppsdafvvs cetqicnthc pvgfeyqeqs gqccgtcvqv acvtntsksp
     5461 ahlfypgetw sdagnhcvth qcekhqdglv vvttkkacpp lscsldearm skdgccrfcp
     5521 pppppyqnqs tcavyhrsli iqqqgcssse pvrlaycrgn cgdsssmysl egntvehrcq
     5581 ccqelrtslr nvtlhctdgs srafsyteve ecgcmgrrcp apgdtqhsee aepepsqeae
     5641 sgswergvpv spmh
//
LOCUS       NP_689934                331 aa            linear   PRI 27-APR-2025
DEFINITION  docking protein 6 [Homo sapiens].
ACCESSION   NP_689934
VERSION     NP_689934.2
DBSOURCE    REFSEQ: accession NM_152721.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lan,C., Wu,Y., Wang,N., Luo,Y., Zhao,J., Zheng,Y., Zhang,Y.,
            Huang,L., Zhu,Y., Lu,L., Zhong,W., Zeng,J. and Xia,H.
  TITLE     Association between ABHD1 and DOK6 polymorphisms and susceptibility
            to Hirschsprung disease in Southern Chinese children
  JOURNAL   J Cell Mol Med 25 (20), 9609-9616 (2021)
   PUBMED   34545688
  REMARK    GeneRIF: Association between ABHD1 and DOK6 polymorphisms and
            susceptibility to Hirschsprung disease in Southern Chinese
            children.
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Li,Wq., Shi,L., You,Yg., Gong,Yh., Yin,B., Yuan,Jg. and Peng,Xz.
  TITLE     Downstream of tyrosine kinase/docking protein 6, as a novel
            substrate of tropomyosin-related kinase C receptor, is involved in
            neurotrophin 3-mediated neurite outgrowth in mouse cortex neurons
  JOURNAL   BMC Biol 8, 86 (2010)
   PUBMED   20565848
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Hsu,Y.H., Zillikens,M.C., Wilson,S.G., Farber,C.R., Demissie,S.,
            Soranzo,N., Bianchi,E.N., Grundberg,E., Liang,L., Richards,J.B.,
            Estrada,K., Zhou,Y., van Nas,A., Moffatt,M.F., Zhai,G., Hofman,A.,
            van Meurs,J.B., Pols,H.A., Price,R.I., Nilsson,O., Pastinen,T.,
            Cupples,L.A., Lusis,A.J., Schadt,E.E., Ferrari,S.,
            Uitterlinden,A.G., Rivadeneira,F., Spector,T.D., Karasik,D. and
            Kiel,D.P.
  TITLE     An integration of genome-wide association study and gene expression
            profiling to prioritize the discovery of novel susceptibility Loci
            for osteoporosis-related traits
  JOURNAL   PLoS Genet 6 (6), e1000977 (2010)
   PUBMED   20548944
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Kurotsuchi,A., Murakumo,Y., Jijiwa,M., Kurokawa,K., Itoh,Y.,
            Kodama,Y., Kato,T., Enomoto,A., Asai,N., Terasaki,H. and
            Takahashi,M.
  TITLE     Analysis of DOK-6 function in downstream signaling of RET in human
            neuroblastoma cells
  JOURNAL   Cancer Sci 101 (5), 1147-1155 (2010)
   PUBMED   20210798
  REMARK    GeneRIF: DOK-6 is involved in RET signaling with less influence
            when compared with DOK-1, DOK-4, and SHC.
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Jones,R.B., Gordus,A., Krall,J.A. and MacBeath,G.
  TITLE     A quantitative protein interaction network for the ErbB receptors
            using protein microarrays
  JOURNAL   Nature 439 (7073), 168-174 (2006)
   PUBMED   16273093
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Crowder,R.J., Enomoto,H., Yang,M., Johnson,E.M. Jr. and
            Milbrandt,J.
  TITLE     Dok-6, a Novel p62 Dok family member, promotes Ret-mediated neurite
            outgrowth
  JOURNAL   J Biol Chem 279 (40), 42072-42081 (2004)
   PUBMED   15286081
  REMARK    GeneRIF: Dok-6 binds to the phosphorylated Ret Tyr(1062) residue
            resulting in phosphorylation of tyrosine residue(s) located within
            the unique C terminus of Dok-6 predominantly through a
            Src-dependent mechanism
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026585.9, DB480182.1, AY599248.1, BC008583.1, BX280184.1,
            BC019045.2 and AC090231.7.
            
            On May 24, 2004 this sequence version replaced NP_689934.1.
            
            Summary: DOK6 is a member of the DOK (see DOK1; MIM 602919) family
            of intracellular adaptors that play a role in the RET (MIM 164761)
            signaling cascade (Crowder et al., 2004 [PubMed
            15286081]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.154678.1,
                                           SRR1803612.137908.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382713.10/ ENSP00000372160.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q22.2"
     Protein         1..331
                     /product="docking protein 6"
                     /note="downstream of tyrosine kinase 6"
                     /calculated_mol_wt=38187
     Region          9..113
                     /region_name="PH_DOK4_DOK5_DOK6"
                     /note="Pleckstrin homology (PH) domain of Downstream of
                     tyrosine kinase 4, 5, and 6 proteins; cd14678"
                     /db_xref="CDD:270197"
     Region          133..235
                     /region_name="PTB_DOK4_DOK5_DOK6"
                     /note="Downstream of tyrosine kinase 4, 5, and 6 proteins
                     phosphotyrosine-binding domain (PTBi); cd13164"
                     /db_xref="CDD:241318"
     Site            order(184..189,195,199..200,210,223)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:241318"
     Region          263..273
                     /region_name="DKFBH motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PKX4.1)"
     Region          293..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PKX4.1)"
     CDS             1..331
                     /gene="DOK6"
                     /gene_synonym="DOK5L; HsT3226"
                     /coded_by="NM_152721.6:358..1353"
                     /db_xref="CCDS:CCDS32841.1"
                     /db_xref="GeneID:220164"
                     /db_xref="HGNC:HGNC:28301"
                     /db_xref="MIM:611402"
ORIGIN      
        1 masnfndivk qgyvkirsrk lgifrrcwlv fkkasskgpr rlekfpdeka ayfrnfhkvt
       61 elhniknitr lpretkkhav aiifhdetsk tfaceselea eewckhlcme clgtrlndis
      121 lgepdllaag vqreqnerfn vylmptpnld iygectmqit heniylwdih nakvklvmwp
      181 lsslrrygrd stwftfesgr mcdtgeglft fqtregemiy qkvhsatlai aeqherlmle
      241 meqkarlqts ltepmtlsks islprsaywh hitrqnsvge iyslqghgfg sskmsraqtf
      301 psyapeqsee aqqplsrsss ygfsysssli q
//
LOCUS       NP_001353512             683 aa            linear   PRI 27-APR-2025
DEFINITION  protein O-mannosyl-transferase TMTC3 isoform 5 [Homo sapiens].
ACCESSION   NP_001353512
VERSION     NP_001353512.1
DBSOURCE    REFSEQ: accession NM_001366583.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Yuan,H., Zhao,Z., Guo,Z., Ma,L., Han,J. and Song,Y.
  TITLE     A Novel ER Stress Mediator TMTC3 Promotes Squamous Cell Carcinoma
            Progression by Activating GRP78/PERK Signaling Pathway
  JOURNAL   Int J Biol Sci 18 (13), 4853-4868 (2022)
   PUBMED   35982901
  REMARK    GeneRIF: A Novel ER Stress Mediator TMTC3 Promotes Squamous Cell
            Carcinoma Progression by Activating GRP78/PERK Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Biyik,I., Kalkan,U. and Simsek,S.
  TITLE     The deep infiltrating endometriosis tissue has lower T-cadherin,
            E-cadherin, progesterone receptor and oestrogen receptor than
            endometrioma tissue
  JOURNAL   Taiwan J Obstet Gynecol 60 (6), 1059-1065 (2021)
   PUBMED   34794738
  REMARK    GeneRIF: The deep infiltrating endometriosis tissue has lower
            T-cadherin, E-cadherin, progesterone receptor and oestrogen
            receptor than endometrioma tissue.
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Eisenhaber,B., Sinha,S., Jadalanki,C.K., Shitov,V.A., Tan,Q.W.,
            Sirota,F.L. and Eisenhaber,F.
  TITLE     Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4,
            new O-mannosyltransferases from the GT-C/PMT clan, are rationalized
            as ligand binding sites
  JOURNAL   Biol Direct 16 (1), 4 (2021)
   PUBMED   33436046
  REMARK    GeneRIF: Conserved sequence motifs in human TMTC1, TMTC2, TMTC3,
            and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are
            rationalized as ligand binding sites.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Larsen,I.S.B., Narimatsu,Y., Joshi,H.J., Siukstaite,L.,
            Harrison,O.J., Brasch,J., Goodman,K.M., Hansen,L., Shapiro,L.,
            Honig,B., Vakhrushev,S.Y., Clausen,H. and Halim,A.
  TITLE     Discovery of an O-mannosylation pathway selectively serving
            cadherins and protocadherins
  JOURNAL   Proc Natl Acad Sci U S A 114 (42), 11163-11168 (2017)
   PUBMED   28973932
  REMARK    GeneRIF: O-mannosylation pathway dedicated to cadherins/
            protocadherins orchestrated by the four TMTC1-4 genes
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Jerber,J., Zaki,M.S., Al-Aama,J.Y., Rosti,R.O., Ben-Omran,T.,
            Dikoglu,E., Silhavy,J.L., Caglar,C., Musaev,D., Albrecht,B.,
            Campbell,K.P., Willer,T., Almuriekhi,M., Caglayan,A.O., Vajsar,J.,
            Bilguvar,K., Ogur,G., Abou Jamra,R., Gunel,M. and Gleeson,J.G.
  TITLE     Biallelic Mutations in TMTC3, Encoding a Transmembrane and
            TPR-Containing Protein, Lead to Cobblestone Lissencephaly
  JOURNAL   Am J Hum Genet 99 (5), 1181-1189 (2016)
   PUBMED   27773428
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Goldstein,J.I., Jarskog,L.F., Hilliard,C., Alfirevic,A., Duncan,L.,
            Fourches,D., Huang,H., Lek,M., Neale,B.M., Ripke,S., Shianna,K.,
            Szatkiewicz,J.P., Tropsha,A., van den Oord,E.J., Cascorbi,I.,
            Dettling,M., Gazit,E., Goff,D.C., Holden,A.L., Kelly,D.L.,
            Malhotra,A.K., Nielsen,J., Pirmohamed,M., Rujescu,D., Werge,T.,
            Levy,D.L., Josiassen,R.C., Kennedy,J.L., Lieberman,J.A., Daly,M.J.
            and Sullivan,P.F.
  TITLE     Clozapine-induced agranulocytosis is associated with rare HLA-DQB1
            and HLA-B alleles
  JOURNAL   Nat Commun 5, 4757 (2014)
   PUBMED   25187353
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Yun,E.J. and Vu,T.H.
  TITLE     mSmile is necessary for bronchial smooth muscle and alveolar
            myofibroblast development
  JOURNAL   Anat Rec (Hoboken) 295 (1), 167-176 (2012)
   PUBMED   21956870
  REMARK    GeneRIF: SMILE is a novel transgene specifying both bronchial
            smooth muscle and lung alveolar myofibroblast lineages,
            contributing to the understanding of the biological control of the
            development of these cells.
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Racape,M., Duong Van Huyen,J.P., Danger,R., Giral,M., Bleicher,F.,
            Foucher,Y., Pallier,A., Pilet,P., Tafelmeyer,P., Ashton-Chess,J.,
            Dugast,E., Pettre,S., Charreau,B., Soulillou,J.P. and Brouard,S.
  TITLE     The involvement of SMILE/TMTC3 in endoplasmic reticulum stress
            response
  JOURNAL   PLoS One 6 (5), e19321 (2011)
   PUBMED   21603654
  REMARK    GeneRIF: that SMILE is involved in the endoplasmic reticulum stress
            response, by modulating proteasome activity and XBP-1 transcript
            expression. This function of SMILE may influence immune cell
            behavior in the context of transplantation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091516.8, AC087865.8 and
            AC127901.6.
            
            Summary: This gene encodes a protein that belongs to the
            transmembrane and tetratricopeptide repeat-containing protein
            family. [provided by RefSeq, May 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.77095.1,
                                           DRR138512.526422.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2467147
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.32"
     Protein         1..683
                     /product="protein O-mannosyl-transferase TMTC3 isoform 5"
                     /EC_number="2.4.1.109"
                     /note="transmembrane and TPR repeat-containing protein 3;
                     protein O-mannosyl-transferase TMTC3; transmembrane and
                     tetratricopeptide repeat containing 3"
                     /calculated_mol_wt=78158
     Region          27..100
                     /region_name="TMTC_DUF1736"
                     /note="Protein O-mannosyl-transferase TMTC, DUF1736;
                     pfam08409"
                     /db_xref="CDD:462468"
     Region          208..437
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          215..243
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          248..292
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          299..326
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(301..302,305,307,309,333,336..337,340..341,343..344,
                     367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          313..568
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          331..361
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          366..394
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          437..465
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          470..500
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          505..534
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          540..568
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..683
                     /gene="TMTC3"
                     /gene_synonym="LIS8; SMILE"
                     /coded_by="NM_001366583.1:467..2518"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:160418"
                     /db_xref="HGNC:HGNC:26899"
                     /db_xref="MIM:617218"
ORIGIN      
        1 mlqtlvkliv lmfstlllvv irvqviqsql pvftrfdnpa avsptptrql tfnyllpvna
       61 wlllnpselc cdwtmgtipl ieslldirnl atftffcflg mlgvfsirys gdssktvlma
      121 lclmalpfip asnlffpvgf vvaervlyvp smgfcilvah gwqkistksv fkklswicls
      181 mvilthslkt fhrnwdwese ytlfmsalkv nknnaklwnn vghalenekn feralkyflq
      241 athvqpddig ahmnvgrtyk nlnrtkeaee symmakslmp qiipgkkyaa riapnhlnvy
      301 inlanliran esrleeadql yrqaismrpd fkqayisrge lllkmnkplk akeaylkale
      361 ldrnnadlwy nlaivhielk epnealknfn ralelnpkhk lalfnsaivm qesgevklrp
      421 earkrllsyi neepldangy fnlgmlamdd kkdneaeiwm kkaiklqadf rsalfnlall
      481 ysqtakelka lpileellry ypdhikglil kgdilmnqkk dilgakkcfe rilemdpsnv
      541 qgkhnlcvvy feekdllkae rclletlala pheeyiqrhl nivrdkisss sfiepifpts
      601 kissvegkki ptesvkeirg esrqtqivkt sdnksqsksn kqlgkngdee tphkttkdik
      661 eiekkrvaal krleeieril nge
//
LOCUS       NP_000734                505 aa            linear   PRI 27-APR-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-3 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_000734
VERSION     NP_000734.2
DBSOURCE    REFSEQ: accession NM_000743.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Chmielowiec,K., Chmielowiec,J., Stronska-Pluta,A., Trybek,G.,
            Smiarowska,M., Suchanecka,A., Wozniak,G., Jaron,A. and Grzywacz,A.
  TITLE     Association of Polymorphism CHRNA5 and CHRNA3 Gene in People
            Addicted to Nicotine
  JOURNAL   Int J Environ Res Public Health 19 (17), 10478 (2022)
   PUBMED   36078193
  REMARK    GeneRIF: Association of Polymorphism CHRNA5 and CHRNA3 Gene in
            People Addicted to Nicotine.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Kitazaki,Y., Ikawa,M., Kishitani,T., Kamisawa,T., Nakane,S.,
            Nakamoto,Y. and Hamano,T.
  TITLE     Progressive Encephalomyelitis with Rigidity and Myoclonus
            (PERM)-like Symptoms Associated with Anti-ganglionic Acetylcholine
            Receptor Antibodies
  JOURNAL   Intern Med 60 (14), 2307-2313 (2021)
   PUBMED   33583893
  REMARK    GeneRIF: Progressive Encephalomyelitis with Rigidity and Myoclonus
            (PERM)-like Symptoms Associated with Anti-ganglionic Acetylcholine
            Receptor Antibodies.
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Shibao,C.A., Joos,K., Phillips,J.A. 3rd, Cogan,J., Newman,J.H.,
            Hamid,R., Meiler,J., Capra,J., Sheehan,J., Vetrini,F., Yang,Y.,
            Black,B., Diedrich,A., Roberston,D. and Biaggioni,I.
  TITLE     Familial Autonomic Ganglionopathy Caused by Rare CHRNA3 Genetic
            Variants
  JOURNAL   Neurology 97 (2), e145-e155 (2021)
   PUBMED   33947782
  REMARK    GeneRIF: Familial Autonomic Ganglionopathy Caused by Rare CHRNA3
            Genetic Variants.
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Yi,X., Li,W., Wang,Y., Chen,X., Ye,F., Sun,G. and Chen,J.
  TITLE     The relationship between CHRNA5/A3/B4 gene cluster polymorphisms
            and lung cancer risk: An updated meta-analysis and systematic
            review
  JOURNAL   Medicine (Baltimore) 100 (6), e24355 (2021)
   PUBMED   33578531
  REMARK    GeneRIF: The relationship between CHRNA5/A3/B4 gene cluster
            polymorphisms and lung cancer risk: An updated meta-analysis and
            systematic review.
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Elliott,K.J., Ellis,S.B., Berckhan,K.J., Urrutia,A.,
            Chavez-Noriega,L.E., Johnson,E.C., Velicelebi,G. and Harpold,M.M.
  TITLE     Comparative structure of human neuronal alpha 2-alpha 7 and beta
            2-beta 4 nicotinic acetylcholine receptor subunits and functional
            expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and
            beta 4 subunits
  JOURNAL   J Mol Neurosci 7 (3), 217-228 (1996)
   PUBMED   8906617
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Raimondi,E., Rubboli,F., Moralli,D., Chini,B., Fornasari,D.,
            Tarroni,P., De Carli,L. and Clementi,F.
  TITLE     Chromosomal localization and physical linkage of the genes encoding
            the human alpha 3, alpha 5, and beta 4 neuronal nicotinic receptor
            subunits
  JOURNAL   Genomics 12 (4), 849-850 (1992)
   PUBMED   1572664
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Eng,C.M., Kozak,C.A., Beaudet,A.L. and Zoghbi,H.Y.
  TITLE     Mapping of multiple subunits of the neuronal nicotinic
            acetylcholine receptor to chromosome 15 in man and chromosome 9 in
            mouse
  JOURNAL   Genomics 9 (2), 278-282 (1991)
   PUBMED   2004777
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Mihovilovic,M. and Roses,A.D.
  TITLE     Expression of mRNAs in human thymus coding for the alpha 3 subunit
            of a neuronal acetylcholine receptor
  JOURNAL   Exp Neurol 111 (2), 175-180 (1991)
   PUBMED   1989896
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Papke,R.L. and Heinemann,S.F.
  TITLE     The role of the beta 4-subunit in determining the kinetic
            properties of rat neuronal nicotinic acetylcholine alpha
            3-receptors
  JOURNAL   J Physiol 440, 95-112 (1991)
   PUBMED   1725184
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Fornasari,D., Chini,B., Tarroni,P. and Clementi,F.
  TITLE     Molecular cloning of human neuronal nicotinic receptor alpha
            3-subunit
  JOURNAL   Neurosci Lett 111 (3), 351-356 (1990)
   PUBMED   2336208
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC006114.1, BC002996.1,
            AC027228.16, BM666615.1 and AI833126.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_000734.1.
            
            Summary: This locus encodes a member of the nicotinic acetylcholine
            receptor family of proteins. Members of this family of proteins
            form pentameric complexes comprised of both alpha and beta
            subunits. This locus encodes an alpha-type subunit, as it contains
            characteristic adjacent cysteine residues. The encoded protein is a
            ligand-gated ion channel that likely plays a role in
            neurotransmission. Polymorphisms in this gene have been associated
            with an increased risk of smoking initiation and an increased
            susceptibility to lung cancer. Alternatively spliced transcript
            variants have been described. [provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098443.1, SRR1660805.149200.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            MANE Ensembl match               :: ENST00000326828.6/
                                                ENSP00000315602.5
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..505
                     /product="neuronal acetylcholine receptor subunit alpha-3
                     isoform 1 precursor"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     3; neuronal nicotinic acetylcholine receptor, alpha3
                     subunit; cholinergic receptor, nicotinic, alpha 3
                     (neuronal); cholinergic receptor, nicotinic alpha 3"
                     /calculated_mol_wt=54306
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3193
     Region          30..496
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     mat_peptide     32..505
                     /product="Neuronal acetylcholine receptor subunit alpha-3.
                     /id=PRO_0000000346"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
                     /calculated_mol_wt=54306
     Region          35..241
                     /region_name="LGIC_ECD_nAChR_A3"
                     /note="extracellular domain of nicotinic acetylcholine
                     receptor subunit alpha 3 (CHRNA3); cd19016"
                     /db_xref="CDD:349817"
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Site            order(70,72,78..79,86,108,110,119..120,122,124..125,129,
                     131..132,136..138,140,150,152,154,158,180,240)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349817"
     Region          159..173
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349817"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Site            251..266
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     Site            269..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     Site            308..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04757; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04757; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Site            475..493
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     CDS             1..505
                     /gene="CHRNA3"
                     /gene_synonym="BAIPRCK; LNCR2; NACHRA3; PAOD2"
                     /coded_by="NM_000743.5:203..1720"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10305.1"
                     /db_xref="GeneID:1136"
                     /db_xref="HGNC:HGNC:1957"
                     /db_xref="MIM:118503"
ORIGIN      
        1 mgsgplslpl alspprllll lllsllpvar aseaehrlfe rlfedyneii rpvanvsdpv
       61 iihfevsmsq lvkvdevnqi metnlwlkqi wndyklkwnp sdyggaefmr vpaqkiwkpd
      121 ivlynnavgd fqvddktkal lkytgevtwi ppaifkssck idvtyfpfdy qnctmkfgsw
      181 sydkakidlv ligssmnlkd ywesgewaii kapgykhdik yncceeiypd ityslyirrl
      241 plfytinlii pcllisfltv lvfylpsdcg ekvtlcisvl lsltvfllvi tetipstslv
      301 ipligeyllf tmifvtlsiv itvfvlnvhy rtptthtmps wvktvflnll prvmfmtrpt
      361 snegnaqkpr plygaelsnl ncfsraeskg ckegypcqdg mcgychhrri kisnfsanlt
      421 rssssesvda vlslsalspe ikeaiqsvky iaenmkaqne akeiqddwky vamvidrifl
      481 wvftlvcilg taglflqplm areda
//
LOCUS       NP_035632                269 aa            linear   ROD 27-APR-2025
DEFINITION  syntaxin-3 isoform C [Mus musculus].
ACCESSION   NP_035632
VERSION     NP_035632.1
DBSOURCE    REFSEQ: accession NM_011502.4
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Chatterjee,R., Nair,A.V., Singh,A., Mehta,N., Setty,S.R.G. and
            Chakravortty,D.
  TITLE     Syntaxin 3 SPI-2 dependent crosstalk facilitates the division of
            Salmonella containing vacuole
  JOURNAL   Traffic 24 (7), 270-283 (2023)
   PUBMED   37114883
  REMARK    GeneRIF: Syntaxin 3 SPI-2 dependent crosstalk facilitates the
            division of Salmonella containing vacuole.
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Kakakhel,M., Tebbe,L., Makia,M.S., Conley,S.M., Sherry,D.M.,
            Al-Ubaidi,M.R. and Naash,M.I.
  TITLE     Syntaxin 3 is essential for photoreceptor outer segment protein
            trafficking and survival
  JOURNAL   Proc Natl Acad Sci U S A 117 (34), 20615-20624 (2020)
   PUBMED   32778589
  REMARK    GeneRIF: Syntaxin 3 is essential for photoreceptor outer segment
            protein trafficking and survival.
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Jurado,S.
  TITLE     The dendritic SNARE fusion machinery involved in AMPARs insertion
            during long-term potentiation
  JOURNAL   Front Cell Neurosci 8, 407 (2014)
   PUBMED   25565955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Lehtonen,S., Riento,K., Olkkonen,V.M. and Lehtonen,E.
  TITLE     Syntaxin 3 and Munc-18-2 in epithelial cells during kidney
            development
  JOURNAL   Kidney Int 56 (3), 815-826 (1999)
   PUBMED   10469351
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Gerst,J.E.
  TITLE     SNAREs and SNARE regulators in membrane fusion and exocytosis
  JOURNAL   Cell Mol Life Sci 55 (5), 707-734 (1999)
   PUBMED   10379359
  REMARK    Review article
REFERENCE   8  (residues 1 to 269)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 269)
  AUTHORS   Riento,K., Jantti,J., Jansson,S., Hielm,S., Lehtonen,E.,
            Ehnholm,C., Keranen,S. and Olkkonen,V.M.
  TITLE     A sec1-related vesicle-transport protein that is expressed
            predominantly in epithelial cells
  JOURNAL   Eur J Biochem 239 (3), 638-646 (1996)
   PUBMED   8774707
REFERENCE   10 (residues 1 to 269)
  AUTHORS   Ibaraki,K., Horikawa,H.P., Morita,T., Mori,H., Sakimura,K.,
            Mishina,M., Saisu,H. and Abe,T.
  TITLE     Identification of four different forms of syntaxin 3
  JOURNAL   Biochem Biophys Res Commun 211 (3), 997-1005 (1995)
   PUBMED   7598732
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC126266.3, BC056949.1 and BC024844.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D29799.1, SRR7974084.16377.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 8.52 cM"
     Protein         1..269
                     /product="syntaxin-3 isoform C"
                     /calculated_mol_wt=30803
     Region          54..208
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          176..242
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(204,211,214)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            207
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     CDS             1..269
                     /gene="Stx3"
                     /gene_synonym="Syn-3"
                     /coded_by="NM_011502.4:683..1492"
                     /note="isoform C is encoded by transcript variant C"
                     /db_xref="CCDS:CCDS29612.1"
                     /db_xref="GeneID:20908"
                     /db_xref="MGI:MGI:103077"
ORIGIN      
        1 mkdrleqlka kqltqdddtd eveiaidnta fmdeffsenf hgilsyllrl sshetkddle
       61 qltteikkra nnvrnklksm ekhieedevr ssadlrirks qhsvlsrkfv evmtkyneaq
      121 vdfrerskgr iqrqleitgk kttdeeleem lesgnpaift sgiidsqisk qalseiegrh
      181 kdivrlessi kelhdmfmdi amlvenqgam idriennmdq svgfverava dtkkavkyqs
      241 earrkkimim icciilaiil astiggifa
//
LOCUS       NP_001510                677 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor IIIB 90 kDa subunit isoform 1 [Homo sapiens].
ACCESSION   NP_001510
VERSION     NP_001510.2
DBSOURCE    REFSEQ: accession NM_001519.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Wang,J., Chen,Q., Wang,X., Zhao,S., Deng,H., Guo,B., Zhang,C.,
            Song,X., Deng,W., Zhang,T. and Ni,H.
  TITLE     TFIIB-related factor 1 is a nucleolar protein that promotes RNA
            polymerase I-directed transcription and tumour cell growth
  JOURNAL   Hum Mol Genet 32 (1), 104-121 (2023)
   PUBMED   35925837
  REMARK    GeneRIF: TFIIB-related factor 1 is a nucleolar protein that
            promotes RNA polymerase I-directed transcription and tumour cell
            growth.
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Zhao,X., Lan,Y., Miao,J., Li,G., Sun,W., Qiu,X., Zhu,S. and Zhu,Z.
  TITLE     A novel BRF1 mutation in two middle-aged siblings with
            cerebellofaciodental syndrome
  JOURNAL   Chin Med J (Engl) 135 (19), 2375-2377 (2022)
   PUBMED   34935685
  REMARK    GeneRIF: A novel BRF1 mutation in two middle-aged siblings with
            cerebellofaciodental syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Guillon,J., Coquelet,H., Leman,G., Toutain,B., Petit,C., Henry,C.,
            Boissard,A., Guette,C. and Coqueret,O.
  TITLE     tRNA biogenesis and specific aminoacyl-tRNA synthetases regulate
            senescence stability under the control of mTOR
  JOURNAL   PLoS Genet 17 (12), e1009953 (2021)
   PUBMED   34928935
  REMARK    GeneRIF: tRNA biogenesis and specific aminoacyl-tRNA synthetases
            regulate senescence stability under the control of mTOR.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Anuraga,G., Tang,W.C., Phan,N.N., Ta,H.D.K., Liu,Y.H., Wu,Y.F.,
            Lee,K.H. and Wang,C.Y.
  TITLE     Comprehensive Analysis of Prognostic and Genetic Signatures for
            General Transcription Factor III (GTF3) in Clinical Colorectal
            Cancer Patients Using Bioinformatics Approaches
  JOURNAL   Curr Issues Mol Biol 43 (1), 2-20 (2021)
   PUBMED   33925358
  REMARK    GeneRIF: Comprehensive Analysis of Prognostic and Genetic
            Signatures for General Transcription Factor III (GTF3) in Clinical
            Colorectal Cancer Patients Using Bioinformatics Approaches.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Chu,W.M., Wang,Z., Roeder,R.G. and Schmid,C.W.
  TITLE     RNA polymerase III transcription repressed by Rb through its
            interactions with TFIIIB and TFIIIC2
  JOURNAL   J Biol Chem 272 (23), 14755-14761 (1997)
   PUBMED   9169441
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     Three human RNA polymerase III-specific subunits form a subcomplex
            with a selective function in specific transcription initiation
  JOURNAL   Genes Dev 11 (10), 1315-1326 (1997)
   PUBMED   9171375
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Chesnokov,I., Chu,W.M., Botchan,M.R. and Schmid,C.W.
  TITLE     p53 inhibits RNA polymerase III-directed transcription in a
            promoter-dependent manner
  JOURNAL   Mol Cell Biol 16 (12), 7084-7088 (1996)
   PUBMED   8943363
REFERENCE   9  (residues 1 to 677)
  AUTHORS   Mital,R., Kobayashi,R. and Hernandez,N.
  TITLE     RNA polymerase III transcription from the human U6 and adenovirus
            type 2 VAI promoters has different requirements for human BRF, a
            subunit of human TFIIIB
  JOURNAL   Mol Cell Biol 16 (12), 7031-7042 (1996)
   PUBMED   8943358
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     Structure and function of a human transcription factor TFIIIB
            subunit that is evolutionarily conserved and contains both TFIIB-
            and high-mobility-group protein 2-related domains
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7026-7030 (1995)
   PUBMED   7624363
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL512355.6, BX440529.2,
            BC016743.2, U75276.1 and BC071637.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 31, 2002 this sequence version replaced NP_001510.1.
            
            Summary: This gene encodes one of the three subunits of the RNA
            polymerase III transcription factor complex. This complex plays a
            central role in transcription initiation by RNA polymerase III on
            genes encoding tRNA, 5S rRNA, and other small structural RNAs. The
            gene product belongs to the TF2B family. Several alternatively
            spliced variants encoding different isoforms, that function at
            different promoters transcribed by RNA polymerase III, have been
            identified. [provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U28838.1, U75276.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000547530.7/ ENSP00000448387.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..677
                     /product="transcription factor IIIB 90 kDa subunit isoform
                     1"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase III, GTF3B subunit 2; TBP - associated
                     factor, RNA polymerase III, 90kD; BRF1 RNA polymerase III
                     transcription initiation factor subunit; B - related
                     factor 1; TATA box binding protein (TBP)-associated factor
                     3C; general transcription factor IIIB, 90kD subunit;
                     transcription factor IIIB 90 kDa subunit; BRF1, RNA
                     polymerase III transcription initiation factor 90 kDa
                     subunit; BRF1 homolog, subunit of RNA polymerase III
                     transcription initiation factor IIIB; epididymis secretory
                     sperm binding protein Li 76p"
                     /calculated_mol_wt=73709
     Region          4..45
                     /region_name="TF_Zn_Ribbon"
                     /note="TFIIB zinc-binding; pfam08271"
                     /db_xref="CDD:400527"
     Region          84..174
                     /region_name="CYCLIN_TFIIIB90_rpt1"
                     /note="first cyclin box found in transcription factor IIIB
                     90 kDa subunit (TFIIIB90) and similar proteins; cd20553"
                     /db_xref="CDD:410256"
     Site            order(85,124..127,161,165,168..169)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410256"
     Region          91..172
                     /region_name="Repetitive region"
                     /note="1; propagated from UniProtKB/Swiss-Prot (Q92994.1)"
     Region          179..270
                     /region_name="CYCLIN_TFIIIB90_rpt2"
                     /note="second cyclin box found in transcription factor
                     IIIB 90 kDa subunit (TFIIIB90) and similar proteins;
                     cd20554"
                     /db_xref="CDD:410257"
     Region          185..269
                     /region_name="Repetitive region"
                     /note="2; propagated from UniProtKB/Swiss-Prot (Q92994.1)"
     Site            order(222..224,255..256,258..259)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410257"
     Region          340..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92994.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92994.1)"
     Region          385..413
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92994.1)"
     Region          450..546
                     /region_name="BRF1"
                     /note="Brf1-like TBP-binding domain; pfam07741"
                     /db_xref="CDD:462250"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92994.1)"
     Region          501..521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92994.1)"
     Region          544..653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92994.1)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92994.1)"
     CDS             1..677
                     /gene="BRF1"
                     /gene_synonym="BRF; BRF-1; CFDS; GTF3B; hBRF; HEL-S-76p;
                     TAF3B2; TAF3C; TAFIII90; TF3B90; TFIIIB90"
                     /coded_by="NM_001519.4:373..2406"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10001.1"
                     /db_xref="GeneID:2972"
                     /db_xref="HGNC:HGNC:11551"
                     /db_xref="MIM:604902"
ORIGIN      
        1 mtgrvcrgcg gtdieldaar gdavctacgs vledniivse vqfvessggg ssavgqfvsl
       61 dgagktptlg ggfhvnlgke sraqtlqngr rhihhlgnql qlnqhcldta fnffkmavsr
      121 hltrgrkmah viaaclylvc rtegtphmll dlsdllqvnv yvlgktflll arelcinapa
      181 idpclyiprf ahllefgekn hevsmtalrl lqrmkrdwmh tgrrpsglcg aallvaarmh
      241 dfrrtvkevi svvkvcestl rkrltefedt ptsqltidef mkidleeecd ppsytagqrk
      301 lrmkqleqvl skkleevege issyqdaiei elensrpkak gglaslakdg stedtasslc
      361 geedtedeel eaaashlnkd lyrellggap gsseaagspe wggrppalgs lldplptaas
      421 lgisdsirec issqssdpkd asgdgeldls giddleidry ilnesearvk aelwmrenae
      481 ylreqrekea riakekelgi ykehkpkksc krrepiqast areaiekmle qkkisskiny
      541 svlrglssag ggsphredaq pehsasarkl srrrtpasrs gadpvtsvgk rlrplvstqp
      601 akkvatgeal lpssptlgae parpqavlve sgpvsyhade eadeeepdee dgepcvsalq
      661 mmgsndygcd gdeddgy
//
LOCUS       NP_002952                101 aa            linear   PRI 27-APR-2025
DEFINITION  protein S100-A4 [Homo sapiens].
ACCESSION   NP_002952
VERSION     NP_002952.1
DBSOURCE    REFSEQ: accession NM_002961.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Ren,W. and Ouyang,L.
  TITLE     Long noncoding RNA VPS9D1-AS1 promotes the progression of
            endometrial cancer via regulation of the miR-187-3p/S100A4 axis
  JOURNAL   Environ Toxicol 39 (9), 4447-4458 (2024)
   PUBMED   38953363
  REMARK    GeneRIF: Long noncoding RNA VPS9D1-AS1 promotes the progression of
            endometrial cancer via regulation of the miR-187-3p/S100A4 axis.
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Tan,X., He,Y., Yu,P., Deng,Y., Xie,Z., Guo,J., Hou,Q., Li,P.,
            Lin,X., Ouyang,S., Ma,W., Xie,Y., Guo,Z., Chen,D., Zhang,Z.,
            Zhu,Y., Huang,F., Zhao,Z., Zhang,C., Guo,Z., Chen,X., Peng,T.,
            Li,L. and Xie,W.
  TITLE     The dual role of FSP1 in programmed cell death: resisting
            ferroptosis in the cell membrane and promoting necroptosis in the
            nucleus of THP-1 cells
  JOURNAL   Mol Med 30 (1), 102 (2024)
   PUBMED   39009982
  REMARK    GeneRIF: The dual role of FSP1 in programmed cell death: resisting
            ferroptosis in the cell membrane and promoting necroptosis in the
            nucleus of THP-1 cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Hua,D., Zhou,X.X., Wang,Q., Sun,C.Y., Shi,C.J., Luo,W.J.,
            Jiang,Z.D. and Yu,S.Z.
  TITLE     [SRSF2 promotes glioblastoma cell proliferation by inducing
            alternative splicing of FSP1 and inhibiting ferroptosis]
  JOURNAL   Zhonghua Bing Li Xue Za Zhi 53 (5), 430-438 (2024)
   PUBMED   38678322
  REMARK    GeneRIF: [SRSF2 promotes glioblastoma cell proliferation by
            inducing alternative splicing of FSP1 and inhibiting ferroptosis].
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Zhou,X., Zhao,J., Yan,T., Ye,D., Wang,Y., Zhou,B., Liu,D., Wang,X.,
            Zheng,W., Zheng,B., Qian,F., Li,Y., Li,D. and Fang,L.
  TITLE     ANXA9 facilitates S100A4 and promotes breast cancer progression
            through modulating STAT3 pathway
  JOURNAL   Cell Death Dis 15 (4), 260 (2024)
   PUBMED   38609357
  REMARK    GeneRIF: ANXA9 facilitates S100A4 and promotes breast cancer
            progression through modulating STAT3 pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Yang,L., Liu,J., Yin,J., Li,Y., Liu,J., Liu,D., Wang,Z.,
            DiSanto,M.E., Zhang,W. and Zhang,X.
  TITLE     S100A4 modulates cell proliferation, apoptosis and fibrosis in the
            hyperplastic prostate
  JOURNAL   Int J Biochem Cell Biol 169, 106551 (2024)
   PUBMED   38360265
  REMARK    GeneRIF: S100A4 modulates cell proliferation, apoptosis and
            fibrosis in the hyperplastic prostate.
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Ambartsumian,N., Tarabykina,S., Grigorian,M., Tulchinsky,E.,
            Hulgaard,E., Georgiev,G. and Lukanidin,E.
  TITLE     Characterization of two splice variants of metastasis-associated
            human mts1 gene
  JOURNAL   Gene 159 (1), 125-130 (1995)
   PUBMED   7607566
REFERENCE   7  (residues 1 to 101)
  AUTHORS   Tomida,Y., Terasawa,M., Kobayashi,R. and Hidaka,H.
  TITLE     Calcyclin and calvasculin exist in human platelets
  JOURNAL   Biochem Biophys Res Commun 189 (3), 1310-1316 (1992)
   PUBMED   1482346
REFERENCE   8  (residues 1 to 101)
  AUTHORS   Engelkamp,D., Schafer,B.W., Erne,P. and Heizmann,C.W.
  TITLE     S100 alpha, CAPL, and CACY: molecular cloning and expression
            analysis of three calcium-binding proteins from human heart
  JOURNAL   Biochemistry 31 (42), 10258-10264 (1992)
   PUBMED   1384693
REFERENCE   9  (residues 1 to 101)
  AUTHORS   Tulchinsky,E., Ford,H.L., Kramerov,D., Reshetnyak,E., Grigorian,M.,
            Zain,S. and Lukanidin,E.
  TITLE     Transcriptional analysis of the mts1 gene with specific reference
            to 5' flanking sequences
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 9146-9150 (1992)
   PUBMED   1329089
REFERENCE   10 (residues 1 to 101)
  AUTHORS   Stoler,A. and Bouck,N.
  TITLE     Identification of a single chromosome in the normal human genome
            essential for suppression of hamster cell transformation
  JOURNAL   Proc Natl Acad Sci U S A 82 (2), 570-574 (1985)
   PUBMED   3155863
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX470102.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21. This protein may function
            in motility, invasion, and tubulin polymerization. Chromosomal
            rearrangements and altered expression of this gene have been
            implicated in tumor metastasis. Multiple alternatively spliced
            variants, encoding the same protein, have been identified.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) has an alternate 5' UTR,
            compared to variant 2. Both variants 1 and 2 encode the same
            isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB106939.1, AK292083.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368716.9/ ENSP00000357705.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..101
                     /product="protein S100-A4"
                     /note="fibroblast-specific protein-1; metastasin 1; S100
                     calcium-binding protein A4 (calcium protein, calvasculin,
                     metastasin, murine placental homolog); malignant
                     transformation suppression 1; leukemia multidrug
                     resistance associated protein; protein Mts1; placental
                     calcium-binding protein; calcium placental protein"
                     /calculated_mol_wt=11597
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P35466; propagated from
                     UniProtKB/Swiss-Prot (P26447.1)"
     Region          4..90
                     /region_name="S-100"
                     /note="S-100 domain, which represents the largest family
                     within the superfamily of proteins carrying the Ca-binding
                     EF-hand motif. Note that this S-100 hierarchy contains
                     only S-100 EF-hand domains, other EF-hands have been
                     modeled separately. S100 proteins are...; cd00213"
                     /db_xref="CDD:238131"
     Site            order(4..20,26..28,37..38,40..42,70..73,75..76,78..81,
                     83..90)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238131"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P26447.1)"
     Site            order(20,25,28,33..34,63,65,67,69,71,74)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238131"
     Region          20..33
                     /region_name="Calcium binding region"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P26447.1)"
     Region          63..74
                     /region_name="Calcium binding region"
     CDS             1..101
                     /gene="S100A4"
                     /gene_synonym="18A2; 42A; CAPL; FSP1; MTS1; P9KA; PEL98"
                     /coded_by="NM_002961.3:70..375"
                     /db_xref="CCDS:CCDS1042.1"
                     /db_xref="GeneID:6275"
                     /db_xref="HGNC:HGNC:10494"
                     /db_xref="MIM:114210"
ORIGIN      
        1 macplekald vmvstfhkys gkegdkfkln kselkelltr elpsflgkrt deaafqklms
       61 nldsnrdnev dfqeycvfls ciammcneff egfpdkqprk k
//
LOCUS       NP_003713                680 aa            linear   PRI 27-APR-2025
DEFINITION  tumor protein 63 isoform 1 [Homo sapiens].
ACCESSION   NP_003713
VERSION     NP_003713.3
DBSOURCE    REFSEQ: accession NM_003722.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Zhang,Y., Karagiannis,D., Liu,H., Lin,M., Fang,Y., Jiang,M.,
            Chen,X., Suresh,S., Huang,H., She,J., Shi,F., Liu,J., Luo,D.,
            Angel,J.C., Lin,G., Yang,P., El-Rifai,W., Zaika,A., Oro,A.E.,
            Liu,K., Rustgi,A.K., Wang,T.C., Lu,C. and Que,J.
  TITLE     Epigenetic regulation of p63 blocks squamous-to-neuroendocrine
            transdifferentiation in esophageal development and malignancy
  JOURNAL   Sci Adv 10 (41), eadq0479 (2024)
   PUBMED   39383220
  REMARK    GeneRIF: Epigenetic regulation of p63 blocks
            squamous-to-neuroendocrine transdifferentiation in esophageal
            development and malignancy.
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Zhao,J., Williams,M.D., Hernandez,M., Kuang,G., Goldberg,H.,
            Fan,J., Ning,J., Ferrarotto,R. and Esmaeli,B.
  TITLE     Prognostic Impact of Notch1 Intracellular Domain, P63, and c-MYC in
            Lacrimal Gland Adenoid Cystic Carcinoma
  JOURNAL   Invest Ophthalmol Vis Sci 65 (11), 4 (2024)
   PUBMED   39230995
  REMARK    GeneRIF: Prognostic Impact of Notch1 Intracellular Domain, P63, and
            c-MYC in Lacrimal Gland Adenoid Cystic Carcinoma.
REFERENCE   3  (residues 1 to 680)
  AUTHORS   Chen,Z., Cai,H., Ye,W., Wu,J., Liu,J., Xie,Y., Feng,S., Jin,Y.,
            Lv,Y., Ye,H., Cai,C. and Cai,G.
  TITLE     TP63 transcriptionally regulates SLC7A5 to suppress ferroptosis in
            head and neck squamous cell carcinoma
  JOURNAL   Front Immunol 15, 1445472 (2024)
   PUBMED   39234254
  REMARK    GeneRIF: TP63 transcriptionally regulates SLC7A5 to suppress
            ferroptosis in head and neck squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 680)
  AUTHORS   Rouleau,M., Medawar,A., Hamon,L., Shivtiel,S., Wolchinsky,Z.,
            Zhou,H., De Rosa,L., Candi,E., de la Forest Divonne,S.,
            Mikkola,M.L., van Bokhoven,H., Missero,C., Melino,G., Puceat,M. and
            Aberdam,D.
  TITLE     TAp63 is important for cardiac differentiation of embryonic stem
            cells and heart development
  JOURNAL   Stem Cells 29 (11), 1672-1683 (2011)
   PUBMED   21898690
REFERENCE   5  (residues 1 to 680)
  AUTHORS   Liu,M. and Eiden,M.V.
  TITLE     Role of human endogenous retroviral long terminal repeats (LTRs) in
            maintaining the integrity of the human germ line
  JOURNAL   Viruses 3 (6), 901-905 (2011)
   PUBMED   21994760
REFERENCE   6  (residues 1 to 680)
  AUTHORS   Beyer,U., Moll-Rocek,J., Moll,U.M. and Dobbelstein,M.
  TITLE     Endogenous retrovirus drives hitherto unknown proapoptotic p63
            isoforms in the male germ line of humans and great apes
  JOURNAL   Proc Natl Acad Sci U S A 108 (9), 3624-3629 (2011)
   PUBMED   21300884
  REMARK    GeneRIF: Human p63 transcripts with unique 5'-ends derived from
            incorporated exons upstream of the currently mapped TP63 gene, were
            identified.
REFERENCE   7  (residues 1 to 680)
  AUTHORS   Crum,C.P. and McKeon,F.D.
  TITLE     p63 in epithelial survival, germ cell surveillance, and neoplasia
  JOURNAL   Annu Rev Pathol 5, 349-371 (2010)
   PUBMED   20078223
  REMARK    Review article
REFERENCE   8  (residues 1 to 680)
  AUTHORS   Bian,J. and Sun,Y.
  TITLE     p53CP, a putative p53 competing protein that specifically binds to
            the consensus p53 DNA binding sites: a third member of the p53
            family?
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14753-14758 (1997)
   PUBMED   9405685
REFERENCE   9  (residues 1 to 680)
  AUTHORS   Robinson,A., Gibbins,J., Rodriguez-Linares,B., Finan,P.M.,
            Wilson,L., Kellie,S., Findell,P. and Watson,S.P.
  TITLE     Characterization of Grb2-binding proteins in human platelets
            activated by Fc gamma RIIA cross-linking
  JOURNAL   Blood 88 (2), 522-530 (1996)
   PUBMED   8695800
REFERENCE   10 (residues 1 to 680)
  AUTHORS   Sutton,V.R. and van Bokhoven,H.
  TITLE     TP63-Related Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20556892
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078809.9, BC039815.1 and
            AC063939.15.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 9, 2003 this sequence version replaced NP_003713.2.
            
            Summary: This gene encodes a member of the p53 family of
            transcription factors. The functional domains of p53 family
            proteins include an N-terminal transactivation domain, a central
            DNA-binding domain and an oligomerization domain. Alternative
            splicing of this gene and the use of alternative promoters results
            in multiple transcript variants encoding different isoforms that
            vary in their functional properties. These isoforms function during
            skin development and maintenance, adult stem/progenitor cell
            regulation, heart development and premature aging. Some isoforms
            have been found to protect the germline by eliminating oocytes or
            testicular germ cells that have suffered DNA damage. Mutations in
            this gene are associated with ectodermal dysplasia, and cleft
            lip/palate syndrome 3 (EEC3); split-hand/foot malformation 4
            (SHFM4); ankyloblepharon-ectodermal defects-cleft lip/palate; ADULT
            syndrome (acro-dermato-ungual-lacrimal-tooth); limb-mammary
            syndrome; Rap-Hodgkin syndrome (RHS); and orofacial cleft 8.
            [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (1) is the longest transcript and
            encodes the longest isoform (1, also known as TAp63alpha, TA-alpha,
            KET, and p51B). This isoform is expressed in female germ cells and
            acts to protect the germline by eliminating oocytes that have
            suffered DNA damage.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC039815.1, Y16961.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2158800
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264731.8/ ENSP00000264731.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q28"
     Protein         1..680
                     /product="tumor protein 63 isoform 1"
                     /note="tumor protein p53-competing protein; amplified in
                     squamous cell carcinoma; chronic ulcerative stomatitis
                     protein; transformation-related protein 63; keratinocyte
                     transcription factor KET; tumor protein 63"
                     /calculated_mol_wt=76655
     Region          1..107
                     /region_name="Transcription activation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3D4.1)"
     Region          123..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3D4.1)"
     Region          177..358
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Site            order(244,247,308,312)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(245..247,249)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            order(309,311,318,343,345..347,350)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          351..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3D4.1)"
     Region          352..388
                     /region_name="Interaction with HIPK2.
                     /evidence=ECO:0000269|PubMed:11925430"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3D4.1)"
     Region          391..431
                     /region_name="P53_tetramer"
                     /note="P53 tetramerization motif; pfam07710"
                     /db_xref="CDD:462238"
     Region          394..443
                     /region_name="Oligomerization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3D4.1)"
     Region          435..472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3D4.1)"
     Region          543..607
                     /region_name="SAM_tumor-p63"
                     /note="SAM domain of tumor-p63 proteins; cd09572"
                     /db_xref="CDD:188971"
     Region          610..680
                     /region_name="Transactivation inhibition"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3D4.1)"
     CDS             1..680
                     /gene="TP63"
                     /gene_synonym="AIS; B(p51A); B(p51B); EEC3; KET; LMS; NBP;
                     OFC8; p40; p51; p53CP; p63; p73H; p73L; RHS; SHFM4;
                     TP53CP; TP53L; TP73L"
                     /coded_by="NM_003722.5:128..2170"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3293.1"
                     /db_xref="GeneID:8626"
                     /db_xref="HGNC:HGNC:15979"
                     /db_xref="MIM:603273"
ORIGIN      
        1 mnfetsrcat lqycpdpyiq rfvetpahfs wkesyyrstm sqstqtnefl spevfqhiwd
       61 fleqpicsvq pidlnfvdep sedgatnkie ismdcirmqd sdlsdpmwpq ytnlgllnsm
      121 dqqiqngsss tspyntdhaq nsvtapspya qpsstfdals pspaipsntd ypgphsfdvs
      181 fqqsstaksa twtystelkk lycqiaktcp iqikvmtppp qgavirampv ykkaehvtev
      241 vkrcpnhels refnegqiap pshlirvegn shaqyvedpi tgrqsvlvpy eppqvgteft
      301 tvlynfmcns scvggmnrrp iliivtletr dgqvlgrrcf earicacpgr drkadedsir
      361 kqqvsdstkn gdgtkrpfrq nthgiqmtsi kkrrspddel lylpvrgret yemllkikes
      421 lelmqylpqh tietyrqqqq qqhqhllqkq tsiqspssyg nsspplnkmn smnklpsvsq
      481 linpqqrnal tpttipdgmg anipmmgthm pmagdmngls ptqalpppls mpstshctpp
      541 ppyptdcsiv sflarlgcss cldyfttqgl ttiyqiehys mddlaslkip eqfrhaiwkg
      601 ildhrqlhef sspshllrtp ssastvsvgs setrgervid avrftlrqti sfpprdewnd
      661 fnfdmdarrn kqqrikeege
//
LOCUS       NP_660149                747 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 47 isoform 2 [Homo
            sapiens].
ACCESSION   NP_660149
VERSION     NP_660149.2
DBSOURCE    REFSEQ: accession NM_145166.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Ward,S.K., Wadley,A., Tsai,C.A., Benke,P.J., Emrick,L., Fisher,K.,
            Houck,K.M., Dai,H., Guillen Sacoto,M.J., Craigen,W., Glaser,K.,
            Murdock,D.R., Rohena,L., Diderich,K.E.M., Bruggenwirth,H.T.,
            Lee,B., Bacino,C., Burrage,L.C. and Rosenfeld,J.A.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     De novo missense variants in ZBTB47 are associated with
            developmental delays, hypotonia, seizures, gait abnormalities, and
            variable movement abnormalities
  JOURNAL   Am J Med Genet A 194 (1), 17-30 (2024)
   PUBMED   37743782
  REMARK    GeneRIF: De novo missense variants in ZBTB47 are associated with
            developmental delays, hypotonia, seizures, gait abnormalities, and
            variable movement abnormalities.
            Erratum:[Am J Med Genet A. 2024 Jun;194(6):e63558. doi:
            10.1002/ajmg.a.63558. PMID: 38327012]
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Kumar,R., Cheney,K.M., Neilsen,P.M., Schulz,R.B. and Callen,D.F.
  TITLE     CBFA2T3-ZNF651, like CBFA2T3-ZNF652, functions as a transcriptional
            corepressor complex
  JOURNAL   FEBS Lett 584 (5), 859-864 (2010)
   PUBMED   20116376
  REMARK    GeneRIF: Data show that ZNF651 is a ZNF652 paralogue that shares a
            common DNA binding sequence with ZNF652 and represses target gene
            expression through the formation of a CBFA2T3-ZNF651 corepressor
            complex.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006059.3, AK127065.1, AB033016.1 and BF509106.1.
            
            On Oct 31, 2009 this sequence version replaced NP_660149.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968832 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000232974.11/ ENSP00000232974.6
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.1"
     Protein         1..747
                     /product="zinc finger and BTB domain-containing protein 47
                     isoform 2"
                     /note="zinc finger protein 651; zinc finger and BTB
                     domain-containing protein 47"
                     /calculated_mol_wt=82630
     Region          1..115
                     /region_name="BTB_POZ_ZBTB47_ZNF651"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 47 (ZBTB47); cd18231"
                     /db_xref="CDD:349540"
     Region          243..424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UFB7.3)"
     Region          <422..496
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          438..459
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          465..484
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          492..512
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          534..559
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          550..570
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <572..655
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          578..598
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(583,585,587,589..590,593..594,597,611,613,617..618,
                     621..622,625,639,641,643,645..646,649..650,653)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          606..626
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          630..>701
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          634..654
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          662..678
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          694..747
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UFB7.3)"
     CDS             1..747
                     /gene="ZBTB47"
                     /gene_synonym="ZNF651"
                     /coded_by="NM_145166.4:269..2512"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS46805.2"
                     /db_xref="GeneID:92999"
                     /db_xref="HGNC:HGNC:26955"
                     /db_xref="MIM:619969"
ORIGIN      
        1 mgrlneqrlf qpdlcdvdlv lvpqrsvfpa hkgvlaaysq ffhslftqnk qlqrvelsle
       61 alapgglqqi lnfiytskll vnaanvhevl saasllqmad iaascqelld arslgppgpg
      121 tvalaqpaas ctpaappyyc dikqeadtpg lpkiyaregp dpysvrvedg agtaggtvpa
      181 tigpaqpffk eekeggveea ggppaslckl eggeeleeel ggsgtysrre qsqiivevnl
      241 nnqtlhvstg pegkpgagps patvvlgred glqrhsdeee eddeeeeeee eeeegggsgr
      301 eeeeeeeggs qgeeeeeeed ghseqeeeee eeeeegpseq dqesseeeeg eegeaggkqg
      361 prgsrssrad ppphshmatr srenarrrgt pepeeagrrg gkrpkpppgv asasargppa
      421 tdglgakvkl eekqhhpcqk cprvfnnrwy lekhmnvths rmqicdqcgk rflleselll
      481 hrqtdcerni qcvtcgkafk klwslhehnk ivhgyaekkf sceicekkfy tmahvrkhmv
      541 ahtkdmpftc etcgksfkrs mslkvhslqh sgekpfrcen cnerfqykyq lrshmsihig
      601 hkqfmcqwcg kdfnmkqyfd ehmkthtgek pyiceicgks ftsrpnmkrh rrthtgekpy
      661 pcdvcgqrfr fsnmlkahke kcfrvshtla gdgvpaapgl pptqpqahal pllpglpqtl
      721 pppphlpppp plfpttaspg grmnann
//
LOCUS       NP_996738               1146 aa            linear   ROD 27-APR-2025
DEFINITION  transforming acidic coiled-coil-containing protein 2 isoform a [Mus
            musculus].
ACCESSION   NP_996738 XP_355948
VERSION     NP_996738.2
DBSOURCE    REFSEQ: accession NM_206856.4
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1146)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1146)
  AUTHORS   Mallampalli,R.K., Li,X., Jang,J.H., Kaminski,T., Hoji,A., Coon,T.,
            Chandra,D., Welty,S., Teng,Y., Sembrat,J., Rojas,M., Zhao,Y.,
            Lafyatis,R., Zou,C., Sciurba,F., Sundd,P., Lan,L. and Nyunoya,T.
  TITLE     Cigarette smoke exposure enhances transforming acidic
            coiled-coil-containing protein 2 turnover and thereby promotes
            emphysema
  JOURNAL   JCI Insight 5 (2), 125895 (2020)
   PUBMED   31996486
  REMARK    GeneRIF: Cigarette smoke exposure enhances transforming acidic
            coiled-coil-containing protein 2 turnover and thereby promotes
            emphysema.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1146)
  AUTHORS   Ray,J.P., Staron,M.M., Shyer,J.A., Ho,P.C., Marshall,H.D.,
            Gray,S.M., Laidlaw,B.J., Araki,K., Ahmed,R., Kaech,S.M. and
            Craft,J.
  TITLE     The Interleukin-2-mTORc1 Kinase Axis Defines the Signaling,
            Differentiation, and Metabolism of T Helper 1 and Follicular B
            Helper T Cells
  JOURNAL   Immunity 43 (4), 690-702 (2015)
   PUBMED   26410627
REFERENCE   4  (residues 1 to 1146)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1146)
  AUTHORS   Tei,S., Saitoh,N., Funahara,T., Iida,S., Nakatsu,Y., Kinoshita,K.,
            Kinoshita,Y., Saya,H. and Nakao,M.
  TITLE     Simian virus 40 large T antigen targets the microtubule-stabilizing
            protein TACC2
  JOURNAL   J Cell Sci 122 (Pt 17), 3190-3198 (2009)
   PUBMED   19671663
REFERENCE   6  (residues 1 to 1146)
  AUTHORS   Schuendeln,M.M., Piekorz,R.P., Wichmann,C., Lee,Y., McKinnon,P.J.,
            Boyd,K., Takahashi,Y. and Ihle,J.N.
  TITLE     The centrosomal, putative tumor suppressor protein TACC2 is
            dispensable for normal development, and deficiency does not lead to
            cancer
  JOURNAL   Mol Cell Biol 24 (14), 6403-6409 (2004)
   PUBMED   15226440
  REMARK    GeneRIF: Results suggest that TACC2 is not required for mouse
            development and normal cell proliferation and is not a tumor
            suppressor protein.
REFERENCE   7  (residues 1 to 1146)
  AUTHORS   Still,I.H., Vettaikkorumakankauv,A.K., DiMatteo,A. and Liang,P.
  TITLE     Structure-function evolution of the transforming acidic coiled coil
            genes revealed by analysis of phylogenetically diverse organisms
  JOURNAL   BMC Evol Biol 4, 16 (2004)
   PUBMED   15207008
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1146)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 1146)
  AUTHORS   Piekorz,R.P., Hoffmeyer,A., Duntsch,C.D., McKay,C., Nakajima,H.,
            Sexl,V., Snyder,L., Rehg,J. and Ihle,J.N.
  TITLE     The centrosomal protein TACC3 is essential for hematopoietic stem
            cell function and genetically interfaces with p53-regulated
            apoptosis
  JOURNAL   EMBO J 21 (4), 653-664 (2002)
   PUBMED   11847113
REFERENCE   10 (residues 1 to 1146)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC175034.1 and AC145294.4.
            
            On Sep 22, 2004 this sequence version replaced NP_996738.1.
            
            Summary: This gene encodes a member of the transforming, acidic
            coiled-coil (TACC) family of proteins. Members of this family are
            centrosomal proteins that interact with microtubules and tubulin.
            TACC proteins are thought to be involved in centrosome/mitotic
            spindle dynamics and gene regulation. Alternative splicing of this
            gene results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849375,
                              SAMN01164133 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1146
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 73.19 cM"
     Protein         1..1146
                     /product="transforming acidic coiled-coil-containing
                     protein 2 isoform a"
                     /calculated_mol_wt=123800
     Region          293..>404
                     /region_name="PRK13335"
                     /note="superantigen-like protein SSL3; Reviewed"
                     /db_xref="CDD:139494"
     Region          <639..896
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          940..1140
                     /region_name="TACC_C"
                     /note="Transforming acidic coiled-coil-containing protein
                     (TACC), C-terminal; pfam05010"
                     /db_xref="CDD:461517"
     CDS             1..1146
                     /gene="Tacc2"
                     /gene_synonym="mKIAA4180"
                     /coded_by="NM_206856.4:47..3487"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS21904.1"
                     /db_xref="GeneID:57752"
                     /db_xref="MGI:MGI:1928899"
ORIGIN      
        1 mgnenstsdh qrtssvqspr slqppgksqs lqkqqgdlpg scagsipgtd dviqpaapvd
       61 pghppladss hhgdavssvs thltvqsasp saaraspapl apehtasaps aagpgvevtp
      121 taspqhlakn eprssdseea fetpesttpv kappappppp pevtpepevi dppapeepgc
      181 iseppvvvpd gprssesveg spfrpshsss avfdedkpia ssgtynldfd sielvdnfqs
      241 lepcsadskg qeckvstrrk stesvppsks tlsrslslqa sdfdgascpg speagtlttd
      301 acgtgsnsas stlkrtkktr ppslkkkqat kkptetppvk etqqepgees pvpseehlap
      361 etktesatpe gagctlsddt plespavpta tcpltlesae dvsplvsggg rvqnsppvgr
      421 ksvplttase avevtlsdsg gqedlpakgl svrlefdyse dkgswesqqe napptkkigk
      481 kpvakmplrr pkmkktpekl dntpaspprs ptepsdtpia kgtytfdidk wddpnfnpfs
      541 stskmqespk lsqqsynfdp daceesldpf kassktpssp skspasfeip astteadgdg
      601 lnkpakkkkt plktmvedvm svcslfdtfr vkkspkrspl sdppsqdptp aatpeapsai
      661 stvvhatdee klavtsqkwt cmtvdldadk qdfpqpsdls nfvnetkfns pseeldyrns
      721 yeieymeklg sslpqdddtp kkqalylmfd tpqespvksp pvrmsdsptp csgssfedte
      781 alvnaatklq hpvarglpss qepllqvpek psqkeleama lgtpaeaiei tapegafasa
      841 dtllsrlahp aslcgalgyl epdlaeknpp vfaqklqeel efavmrieal klarqialas
      901 rsrqdtkrea ahppdvsisk talysrigst evekppgllf qqpdldsalq varaeviake
      961 revsewrdky eesrrevvem rkivaeyekt iaqmiedeqr eksishqtvq qlvlekeqal
     1021 adlnsveksl adlfrryekm kevlegfrkn eevlkkcaqe ylsrvkkeeq ryqalkvhae
     1081 ekldranaei aqvrgkaqqe qaayqaslrk eqlrvdaler tleqknkeie eltkicdeli
     1141 akmgks
//
LOCUS       NP_055645                712 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 39 [Homo sapiens].
ACCESSION   NP_055645 XP_374985
VERSION     NP_055645.1
DBSOURCE    REFSEQ: accession NM_014830.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026120.33, AK292468.1 and BC152461.1.
            
            On Nov 26, 2004 this sequence version replaced XP_374985.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.88238.1,
                                           SRR1660805.154259.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119, SAMN03267765
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300101.3/ ENSP00000300101.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..712
                     /product="zinc finger and BTB domain-containing protein
                     39"
                     /calculated_mol_wt=78870
     Region          4..126
                     /region_name="BTB_POZ_ZBTB39"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 39 (ZBTB39); cd18224"
                     /db_xref="CDD:349533"
     Region          129..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15060.1)"
     Region          176..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15060.1)"
     Region          236..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15060.1)"
     Region          345..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(350,352,354,356..357,360,362,365,379,381,385..386,
                     389..390,393,407,409,411,413..414,417..418)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          374..394
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          402..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          453..474
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          482..502
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          510..530
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          540..560
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          607..627
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(612,614,616,618..619,622..623,626,640,642,646..647,
                     650..651,654,669,671..672,678..679,682)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          619..642
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          621..>668
                     /region_name="C1"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     superfamily; cl00040"
                     /db_xref="CDD:412127"
     Region          635..655
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          663..683
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..712
                     /gene="ZBTB39"
                     /gene_synonym="ZNF922"
                     /coded_by="NM_014830.3:187..2325"
                     /db_xref="CCDS:CCDS31839.1"
                     /db_xref="GeneID:9880"
                     /db_xref="HGNC:HGNC:29014"
                     /db_xref="MIM:619384"
ORIGIN      
        1 mgmriklqst nhpnnllkel nkcrlsetmc dvtivvgsrs fpahkavlac aagyfqnlfl
       61 ntgldaarty vvdfitpanf ekvlsfvyts elftdlinvg viyevaerlg medllqachs
      121 tfpdlestar akpltstses hsgtlscpsa epahplgelr gggdylgadr nyvlpsdagg
      181 sykeeeknva sdanhslhlp qppppppkte dhdtpapfts ipsmmtqpll gtvstgiqts
      241 tsscqpykvq sngdfsknsf ltpdnavdit tgtnsclsns ehskdpgfgq mdelqledlg
      301 dddlqfedpa edigtteevi elsddsedel afgendnren kampcqvckk vlepniqlir
      361 qhardhvdll tgnckvceth fqdrnsrvth vlshigiflf scdmcetkff tqwqltlhrr
      421 dgifenniiv hpndplpgkl glfsgaaspe lkcaacgkvl akdfhvvrgh ildhlnlkgq
      481 acsvcdqrhl nlcslmwhtl shlgisvfsc svcansfvdw hllekhmavh qsledalfhc
      541 rlcsqsfkse aayryhvsqh kcnsgldarp gfglqhpalq krklpaeefl geelalqgqp
      601 gnskysckvc gkrfahtsef nyhrrihtge kpyqckvchk ffrgrstikc hlkthsgalm
      661 yrctvcghys stlnlmskhv gvhkgslppd ftieqtfmyi ihskeadknp ds
//
LOCUS       NP_932332                184 aa            linear   PRI 27-APR-2025
DEFINITION  glucosamine 6-phosphate N-acetyltransferase [Homo sapiens].
ACCESSION   NP_932332
VERSION     NP_932332.1
DBSOURCE    REFSEQ: accession NM_198066.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Hu,H., Wang,Z.W., Hu,S., Xiang,Y., Deng,Y., Wan,F.J., Zhang,T.C.,
            Yang,Z.Y. and Liao,X.H.
  TITLE     GNPNAT1 promotes the stemness of breast cancer and serves as a
            potential prognostic biomarker
  JOURNAL   Oncol Rep 50 (2) (2023)
   PUBMED   37387422
  REMARK    GeneRIF: GNPNAT1 promotes the stemness of breast cancer and serves
            as a potential prognostic biomarker.
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Yuan,R., Zhang,Y., Wang,Y., Chen,H., Zhang,R., Hu,Z., Chai,C. and
            Chen,T.
  TITLE     GNPNAT1 is a potential biomarker correlated with immune
            infiltration and immunotherapy outcome in breast cancer
  JOURNAL   Front Immunol 14, 1152678 (2023)
   PUBMED   37215111
  REMARK    GeneRIF: GNPNAT1 is a potential biomarker correlated with immune
            infiltration and immunotherapy outcome in breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Zhang,S., Zhang,H., Li,H., Guo,J., Wang,J. and Zhang,L.
  TITLE     Potential role of glucosamine-phosphate N-acetyltransferase 1 in
            the development of lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 13 (5), 7430-7453 (2021)
   PUBMED   33686019
  REMARK    GeneRIF: Potential role of glucosamine-phosphate
            N-acetyltransferase 1 in the development of lung adenocarcinoma.
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Zheng,X., Li,Y., Ma,C., Zhang,J., Zhang,Y., Fu,Z. and Luo,H.
  TITLE     Independent Prognostic Potential of GNPNAT1 in Lung Adenocarcinoma
  JOURNAL   Biomed Res Int 2020, 8851437 (2020)
   PUBMED   33178836
  REMARK    GeneRIF: Independent Prognostic Potential of GNPNAT1 in Lung
            Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Brockhausen,I., Nair,D.G., Chen,M., Yang,X., Allingham,J.S.,
            Szarek,W.A. and Anastassiades,T.
  TITLE     Human acetyl-CoA:glucosamine-6-phosphate N-acetyltransferase 1 has
            a relaxed donor specificity and transfers acyl groups up to four
            carbons in length
  JOURNAL   Biochem Cell Biol 94 (2), 197-204 (2016)
   PUBMED   26935656
  REMARK    GeneRIF: The Glucosamine-6-phosphate N-acetyltransferase1 (GNA1)
            catalyses the transfer of an acetyl group from acetyl coenzyme A to
            glucosamine-6-phosphate to form N-acetylglucosamine-6-phosphate
            which is an essential intermediate in UDP-GlcNAc biosynthesis.
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Eeles,R.A., Olama,A.A., Benlloch,S., Saunders,E.J.,
            Leongamornlert,D.A., Tymrakiewicz,M., Ghoussaini,M., Luccarini,C.,
            Dennis,J., Jugurnauth-Little,S., Dadaev,T., Neal,D.E., Hamdy,F.C.,
            Donovan,J.L., Muir,K., Giles,G.G., Severi,G., Wiklund,F.,
            Gronberg,H., Haiman,C.A., Schumacher,F., Henderson,B.E., Le
            Marchand,L., Lindstrom,S., Kraft,P., Hunter,D.J., Gapstur,S.,
            Chanock,S.J., Berndt,S.I., Albanes,D., Andriole,G., Schleutker,J.,
            Weischer,M., Canzian,F., Riboli,E., Key,T.J., Travis,R.C.,
            Campa,D., Ingles,S.A., John,E.M., Hayes,R.B., Pharoah,P.D.,
            Pashayan,N., Khaw,K.T., Stanford,J.L., Ostrander,E.A.,
            Signorello,L.B., Thibodeau,S.N., Schaid,D., Maier,C., Vogel,W.,
            Kibel,A.S., Cybulski,C., Lubinski,J., Cannon-Albright,L.,
            Brenner,H., Park,J.Y., Kaneva,R., Batra,J., Spurdle,A.B.,
            Clements,J.A., Teixeira,M.R., Dicks,E., Lee,A., Dunning,A.M.,
            Baynes,C., Conroy,D., Maranian,M.J., Ahmed,S., Govindasami,K.,
            Guy,M., Wilkinson,R.A., Sawyer,E.J., Morgan,A., Dearnaley,D.P.,
            Horwich,A., Huddart,R.A., Khoo,V.S., Parker,C.C., Van As,N.J.,
            Woodhouse,C.J., Thompson,A., Dudderidge,T., Ogden,C., Cooper,C.S.,
            Lophatananon,A., Cox,A., Southey,M.C., Hopper,J.L., English,D.R.,
            Aly,M., Adolfsson,J., Xu,J., Zheng,S.L., Yeager,M., Kaaks,R.,
            Diver,W.R., Gaudet,M.M., Stern,M.C., Corral,R., Joshi,A.D.,
            Shahabi,A., Wahlfors,T., Tammela,T.L., Auvinen,A., Virtamo,J.,
            Klarskov,P., Nordestgaard,B.G., Roder,M.A., Nielsen,S.F.,
            Bojesen,S.E., Siddiq,A., Fitzgerald,L.M., Kolb,S., Kwon,E.M.,
            Karyadi,D.M., Blot,W.J., Zheng,W., Cai,Q., McDonnell,S.K.,
            Rinckleb,A.E., Drake,B., Colditz,G., Wokolorczyk,D.,
            Stephenson,R.A., Teerlink,C., Muller,H., Rothenbacher,D.,
            Sellers,T.A., Lin,H.Y., Slavov,C., Mitev,V., Lose,F.,
            Srinivasan,S., Maia,S., Paulo,P., Lange,E., Cooney,K.A.,
            Antoniou,A.C., Vincent,D., Bacot,F., Tessier,D.C., Kote-Jarai,Z.
            and Easton,D.F.
  CONSRTM   COGS-Cancer Research UK GWAS-ELLIPSE (part of GAME-ON) Initiative;
            Australian Prostate Cancer Bioresource; UK Genetic Prostate Cancer
            Study Collaborators/British Association of Urological Surgeons'
            Section of Oncology; UK ProtecT (Prostate testing for cancer and
            Treatment) Study Collaborators; PRACTICAL (Prostate Cancer
            Association Group to Investigate Cancer-Associated Alterations in
            the Genome) Consortium
  TITLE     Identification of 23 new prostate cancer susceptibility loci using
            the iCOGS custom genotyping array
  JOURNAL   Nat Genet 45 (4), 385-391 (2013)
   PUBMED   23535732
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Wang,J., Liu,X., Liang,Y.H., Li,L.F. and Su,X.D.
  TITLE     Acceptor substrate binding revealed by crystal structure of human
            glucosamine-6-phosphate N-acetyltransferase 1
  JOURNAL   FEBS Lett 582 (20), 2973-2978 (2008)
   PUBMED   18675810
  REMARK    GeneRIF: Crystal structures of human GNA1, including apo GNA1, the
            GNA1-GlcN6P complex and an E156A mutant were reported.
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Vessal,M. and Jaberi-Pour,M.
  TITLE     Partial purification and kinetic properties of three different
            D-glucosamine 6-P:N-acetyltransferase forms from human placenta
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 121 (4), 379-384 (1998)
   PUBMED   9972309
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG717628.1, AK090577.1, AL139317.5 and CA435370.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.455389.1,
                                           SRR1803613.44163.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216410.8/ ENSP00000216410.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.1"
     Protein         1..184
                     /product="glucosamine 6-phosphate N-acetyltransferase"
                     /EC_number="2.3.1.4"
                     /note="phosphoglucosamine acetylase; phosphoglucosamine
                     transacetylase"
                     /calculated_mol_wt=20618
     Region          36..174
                     /region_name="N-Acyltransferase superfamily: Various
                     enyzmes that characteristicly catalyze the transfer of an
                     acyl group to a substrate"
                     /note="NAT (N-Acyltransferase) is a large superfamily of
                     enzymes that mostly catalyze the transfer of an acyl group
                     to a substrate and are implicated in a variety of
                     functions, from bacterial antibiotic resistance to
                     circadian rhythms in mammals. Members...; cl17182"
                     /db_xref="CDD:473072"
     CDS             1..184
                     /gene="GNPNAT1"
                     /gene_synonym="GNA1; GNPNAT; Gpnat1; RHZDAN"
                     /coded_by="NM_198066.4:195..749"
                     /db_xref="CCDS:CCDS9712.1"
                     /db_xref="GeneID:64841"
                     /db_xref="HGNC:HGNC:19980"
                     /db_xref="MIM:616510"
ORIGIN      
        1 mkpdetpmfd psllkevdws qntatfspai spthpgeglv lrplctadln rgffkvlgql
       61 tetgvvspeq fmksfehmkk sgdyyvtvve dvtlgqivat atliiehkfi hscakrgrve
      121 dvvvsdecrg kqlgklllst ltllskklnc ykitleclpq nvgfykkfgy tvseenymcr
      181 rflk
//
LOCUS       NP_000092                195 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome b-245 light chain [Homo sapiens].
ACCESSION   NP_000092
VERSION     NP_000092.2
DBSOURCE    REFSEQ: accession NM_000101.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Zhang,R., Liu,S., Tan,P., Guo,Z., Hou,H., Liu,S., Li,H. and Wang,X.
  TITLE     Effect of the CYBA C242T Polymorphism on Preeclampsia Pathogenesis
            in the Chinese Population
  JOURNAL   Biochem Genet 62 (3), 1675-1689 (2024)
   PUBMED   37665479
  REMARK    GeneRIF: Effect of the CYBA C242T Polymorphism on Preeclampsia
            Pathogenesis in the Chinese Population.
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Liu,X., Shi,Y., Liu,R., Song,K. and Chen,L.
  TITLE     Structure of human phagocyte NADPH oxidase in the activated state
  JOURNAL   Nature 627 (8002), 189-195 (2024)
   PUBMED   38355798
  REMARK    GeneRIF: Structure of human phagocyte NADPH oxidase in the
            activated state.
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Chang,C.F., Huang,S.P., Hsueh,Y.M., Chen,P.L., Lee,C.H., Geng,J.H.,
            Huang,C.Y. and Bao,B.Y.
  TITLE     CYBA as a Potential Biomarker for Renal Cell Carcinoma: Evidence
            from an Integrated Genetic Analysis
  JOURNAL   Cancer Genomics Proteomics 20 (5), 469-475 (2023)
   PUBMED   37643785
  REMARK    GeneRIF: CYBA as a Potential Biomarker for Renal Cell Carcinoma:
            Evidence from an Integrated Genetic Analysis.
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Tornell,A., Lagerstrom,N., Mossberg,N., Kiffin,R., Farman,H.,
            Lycke,J., Andersen,O., Axelsson,M., Hellstrand,K. and Martner,A.
  TITLE     CYBA allelic variants are associated with severity and recovery in
            Guillain-Barre syndrome
  JOURNAL   J Peripher Nerv Syst 28 (3), 407-414 (2023)
   PUBMED   37288802
  REMARK    GeneRIF: CYBA allelic variants are associated with severity and
            recovery in Guillain-Barre syndrome.
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Tlili,A., Pintard,C., Hurtado-Nedelec,M., Liu,D., Marzaioli,V.,
            Thieblemont,N., Dang,P.M. and El-Benna,J.
  TITLE     ROCK2 interacts with p22phox to phosphorylate p47phox and to
            control NADPH oxidase activation in human monocytes
  JOURNAL   Proc Natl Acad Sci U S A 120 (3), e2209184120 (2023)
   PUBMED   36626553
  REMARK    GeneRIF: ROCK2 interacts with p22phox to phosphorylate p47phox and
            to control NADPH oxidase activation in human monocytes.
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Leiding,J.W. and Holland,S.M.
  TITLE     Chronic Granulomatous Disease
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22876374
REFERENCE   7  (residues 1 to 195)
  AUTHORS   de Boer,M., de Klein,A., Hossle,J.P., Seger,R., Corbeel,L.,
            Weening,R.S. and Roos,D.
  TITLE     Cytochrome b558-negative, autosomal recessive chronic granulomatous
            disease: two new mutations in the cytochrome b558 light chain of
            the NADPH oxidase (p22-phox)
  JOURNAL   Am J Hum Genet 51 (5), 1127-1135 (1992)
   PUBMED   1415254
REFERENCE   8  (residues 1 to 195)
  AUTHORS   Dinauer,M.C., Pierce,E.A., Erickson,R.W., Muhlebach,T.J.,
            Messner,H., Orkin,S.H., Seger,R.A. and Curnutte,J.T.
  TITLE     Point mutation in the cytoplasmic domain of the neutrophil p22-phox
            cytochrome b subunit is associated with a nonfunctional NADPH
            oxidase and chronic granulomatous disease
  JOURNAL   Proc Natl Acad Sci U S A 88 (24), 11231-11235 (1991)
   PUBMED   1763037
REFERENCE   9  (residues 1 to 195)
  AUTHORS   Bu-Ghanim,H.N., Casimir,C.M., Povey,S. and Segal,A.W.
  TITLE     The alpha subunit of cytochrome b-245 mapped to chromosome 16
  JOURNAL   Genomics 8 (3), 568-570 (1990)
   PUBMED   2286377
REFERENCE   10 (residues 1 to 195)
  AUTHORS   Dinauer,M.C., Pierce,E.A., Bruns,G.A., Curnutte,J.T. and Orkin,S.H.
  TITLE     Human neutrophil cytochrome b light chain (p22-phox). Gene
            structure, chromosomal location, and mutations in
            cytochrome-negative autosomal recessive chronic granulomatous
            disease
  JOURNAL   J Clin Invest 86 (5), 1729-1737 (1990)
   PUBMED   2243141
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116552.2.
            
            On Jul 1, 2005 this sequence version replaced NP_000092.1.
            
            Summary: Cytochrome b is comprised of a light chain (alpha) and a
            heavy chain (beta). This gene encodes the light, alpha subunit
            which has been proposed as a primary component of the microbicidal
            oxidase system of phagocytes. Mutations in this gene are associated
            with autosomal recessive chronic granulomatous disease (CGD), that
            is characterized by the failure of activated phagocytes to generate
            superoxide, which is important for the microbicidal activity of
            these cells. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CA311054.1, CA311071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261623.8/ ENSP00000261623.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.2"
     Protein         1..195
                     /product="cytochrome b-245 light chain"
                     /note="cytochrome b, alpha polypeptide; cytochrome b light
                     chain; flavocytochrome b-558 alpha polypeptide; cytochrome
                     b(558) alpha-subunit; p22phox; cytochrome b-245, alpha
                     polypeptide; p22 phagocyte B-cytochrome; cytochrome b(558)
                     alpha chain; cytochrome b558 subunit alpha; neutrophil
                     cytochrome b 22 kDa polypeptide; superoxide-generating
                     NADPH oxidase light chain subunit"
                     /calculated_mol_wt=20881
     Region          2..193
                     /region_name="Cytochrom_B558a"
                     /note="Cytochrome Cytochrome b558 alpha-subunit;
                     pfam05038"
                     /db_xref="CDD:461532"
     Site            8..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13498.3)"
     Site            36..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13498.3)"
     Site            87..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13498.3)"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13498.3)"
     Region          134..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13498.3)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19948736,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P13498.3)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61462; propagated from
                     UniProtKB/Swiss-Prot (P13498.3)"
     CDS             1..195
                     /gene="CYBA"
                     /gene_synonym="CGD4; p22-PHOX"
                     /coded_by="NM_000101.4:41..628"
                     /db_xref="CCDS:CCDS32504.1"
                     /db_xref="GeneID:1535"
                     /db_xref="HGNC:HGNC:2577"
                     /db_xref="MIM:608508"
ORIGIN      
        1 mgqiewamwa neqalasgli litggivata grftqwyfga ysivagvfvc lleyprgkrk
       61 kgstmerwgq kymtavvklf gpftrnyyvr avlhlllsvp agfllatilg taclaiasgi
      121 yllaavrgeq wtpiepkpre rpqiggtikq ppsnppprpp aearkkpsee eaavaaggpp
      181 ggpqvnpipv tdevv
//
LOCUS       NP_001350630             459 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger C3HC-type protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001350630 XP_016867776
VERSION     NP_001350630.1
DBSOURCE    REFSEQ: accession NM_001363701.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Gunkel,P., Iino,H., Krull,S. and Cordes,V.C.
  TITLE     ZC3HC1 Is a Novel Inherent Component of the Nuclear Basket,
            Resident in a State of Reciprocal Dependence with TPR
  JOURNAL   Cells 10 (8), 1937 (2021)
   PUBMED   34440706
  REMARK    GeneRIF: ZC3HC1 Is a Novel Inherent Component of the Nuclear
            Basket, Resident in a State of Reciprocal Dependence with TPR.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Jafaripour,S., Sasanejad,P., Dadgarmoghaddam,M. and Sadr-Nabavi,A.
  TITLE     ADAMTS7 and ZC3HC1 Share Genetic Predisposition to Coronary Artery
            Disease and Large Artery Ischemic Stroke
  JOURNAL   Crit Rev Eukaryot Gene Expr 29 (4), 351-361 (2019)
   PUBMED   31679296
  REMARK    GeneRIF: Data show that common variants in A disintegrin and
            metalloproteinase with thrombospondin motifs 7 protein (ADAMTS7)
            and zinc finger, C3HC-type containing 1 protein (ZC3HC1) genes
            contribute to an increased risk for both coronary artery disease
            (CAD) and large artery ischemic stroke (LA atherosclerotic) IS.
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Dichgans,M., Malik,R., Konig,I.R., Rosand,J., Clarke,R.,
            Gretarsdottir,S., Thorleifsson,G., Mitchell,B.D., Assimes,T.L.,
            Levi,C., O'Donnell,C.J., Fornage,M., Thorsteinsdottir,U.,
            Psaty,B.M., Hengstenberg,C., Seshadri,S., Erdmann,J., Bis,J.C.,
            Peters,A., Boncoraglio,G.B., Marz,W., Meschia,J.F., Kathiresan,S.,
            Ikram,M.A., McPherson,R., Stefansson,K., Sudlow,C., Reilly,M.P.,
            Thompson,J.R., Sharma,P., Hopewell,J.C., Chambers,J.C., Watkins,H.,
            Rothwell,P.M., Roberts,R., Markus,H.S., Samani,N.J., Farrall,M. and
            Schunkert,H.
  CONSRTM   METASTROKE Consortium; CARDIoGRAM Consortium; C4D Consortium;
            International Stroke Genetics Consortium
  TITLE     Shared genetic susceptibility to ischemic stroke and coronary
            artery disease: a genome-wide analysis of common variants
  JOURNAL   Stroke 45 (1), 24-36 (2014)
   PUBMED   24262325
  REMARK    Review article
REFERENCE   6  (residues 1 to 459)
  AUTHORS   Lopez-Mejias,R., Genre,F., Garcia-Bermudez,M., Corrales,A.,
            Gonzalez-Juanatey,C., Llorca,J., Miranda-Filloy,J.A.,
            Rueda-Gotor,J., Blanco,R., Castaneda,S., Martin,J. and
            Gonzalez-Gay,M.A.
  TITLE     The ZC3HC1 rs11556924 polymorphism is associated with increased
            carotid intima-media thickness in patients with rheumatoid
            arthritis
  JOURNAL   Arthritis Res Ther 15 (5), R152 (2013)
   PUBMED   24286297
  REMARK    GeneRIF: Results indicate that ZC3HC1 rs11556924 polymorphism is
            associated with subclinical atherosclerosis in rheumatoid
            arthritis.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 459)
  AUTHORS   Illert,A.L., Zech,M., Moll,C., Albers,C., Kreutmair,S., Peschel,C.,
            Bassermann,F. and Duyster,J.
  TITLE     Extracellular signal-regulated kinase 2 (ERK2) mediates
            phosphorylation and inactivation of nuclear interaction partner of
            anaplastic lymphoma kinase (NIPA) at G2/M
  JOURNAL   J Biol Chem 287 (45), 37997-38005 (2012)
   PUBMED   22955283
  REMARK    GeneRIF: Data show that cell cycle-dependent phosphorylation of
            nuclear interaction partner of anaplastic lymphoma kinase (NIPA)is
            mediated by extracellular signal-regulated kinase 2 (ERK2).
REFERENCE   8  (residues 1 to 459)
  AUTHORS   Klitzing,Cv., Huss,R., Illert,A.L., Froschl,A., Wotzel,S.,
            Peschel,C., Bassermann,F. and Duyster,J.
  TITLE     APC/C(Cdh1)-mediated degradation of the F-box protein NIPA is
            regulated by its association with Skp1
  JOURNAL   PLoS One 6 (12), e28998 (2011)
   PUBMED   22205987
  REMARK    GeneRIF: phosphorylated NIPA is degraded in late mitosis in an
            APC/C(Cdh1)-dependent manner
REFERENCE   9  (residues 1 to 459)
  AUTHORS   Bassermann,F., von Klitzing,C., Munch,S., Bai,R.Y., Kawaguchi,H.,
            Morris,S.W., Peschel,C. and Duyster,J.
  TITLE     NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic
            entry
  JOURNAL   Cell 122 (1), 45-57 (2005)
   PUBMED   16009132
  REMARK    GeneRIF: The NIPA protein is a human F-box-containing protein that
            defines an SCF-type E3 ligase (SCF(NIPA)) controlling mitotic
            entry.
REFERENCE   10 (residues 1 to 459)
  AUTHORS   Ouyang,T., Bai,R.Y., Bassermann,F., von Klitzing,C., Klumpen,S.,
            Miething,C., Morris,S.W., Peschel,C. and Duyster,J.
  TITLE     Identification and characterization of a nuclear interacting
            partner of anaplastic lymphoma kinase (NIPA)
  JOURNAL   J Biol Chem 278 (32), 30028-30036 (2003)
   PUBMED   12748172
  REMARK    GeneRIF: NIPA has an antiapoptotic role in NPM-ALK-mediated
            signaling events
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087071.2 and AC073320.8.
            
            On May 29, 2018 this sequence version replaced XP_016867776.1.
            
            Summary: This gene encodes an F-box-containing protein that is a
            component of an SCF-type E3 ubiquitin ligase complex that regulates
            the onset of cell division. The G2/M transition in the cell cycle
            requires the interaction of the proteins cyclin B1 and
            cyclin-dependent kinase 1. The activated ubiquitin ligase complex
            targets the protein cyclin B1 for degradation, preventing this
            transition to mitosis. [provided by RefSeq, Aug 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.211665.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q32.2"
     Protein         1..459
                     /product="zinc finger C3HC-type protein 1 isoform 4"
                     /note="nuclear interacting partner of anaplastic lymphoma
                     kinase (ALK); nuclear-interacting partner of ALK;
                     hematopoietic stem/progenitor cell protein 216"
                     /calculated_mol_wt=50431
     Region          73..201
                     /region_name="zf-C3HC"
                     /note="C3HC zinc finger-like; pfam07967"
                     /db_xref="CDD:429759"
     Region          <376..423
                     /region_name="Rsm1"
                     /note="Rsm1-like; pfam08600"
                     /db_xref="CDD:369989"
     CDS             1..459
                     /gene="ZC3HC1"
                     /gene_synonym="HSPC216; NIPA"
                     /coded_by="NM_001363701.1:20..1399"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS87546.1"
                     /db_xref="GeneID:51530"
                     /db_xref="HGNC:HGNC:29913"
                     /db_xref="MIM:619746"
ORIGIN      
        1 maapcegqaf avgveknwga vvrspegtpq kirqlidegi apeeggvdak dtsatsqsvn
       61 gspqaeqpsl estskeaffs rvetfsslkw agkpfelspl vcakygwvtv ecdmlkcssc
      121 qaflcaslqp afdfdrykqr caelkkalct ahekfcfwpd spspdrfgml pldepailvs
      181 efldrfqslc hldlqlpslr pedlktmclt edkislllhl ledeldhrtd erkttiklgs
      241 diqvhvtaci lsvcgwacss pipglegrpe rlplvpespr rmmtrsqdat fspgseqaek
      301 spgpivsrtr swdssspvdr pepeaasptt rtrpvtrsmg tgdtpglevp ssplrkakra
      361 rlcsssssdt ssrsffdpts qhrdwcpwvn itlgkesren ggtepdasap aepgwkavlt
      421 illahkqssq paetdsmsls eksrkvfrif rqweslcsc
//
LOCUS       NP_110379                556 aa            linear   PRI 27-APR-2025
DEFINITION  T-complex protein 1 subunit alpha isoform a [Homo sapiens].
ACCESSION   NP_110379
VERSION     NP_110379.2
DBSOURCE    REFSEQ: accession NM_030752.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Zhang,M., Xie,Z., Tan,Y., Wu,Y., Wang,M., Zhang,P., Yuan,Y. and
            Li,J.
  TITLE     METTL14-mediated N6-methyladenosine modification of TCP1 mRNA
            promotes acute myeloid leukemia progression
  JOURNAL   Cell Signal 122, 111304 (2024)
   PUBMED   39033992
  REMARK    GeneRIF: METTL14-mediated N6-methyladenosine modification of TCP1
            mRNA promotes acute myeloid leukemia progression.
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Chen,X.F., Chen,X.L. and Chen,Y.Z.
  TITLE     [The Effect of TCP1 Expression on the Proliferation and the
            Accumulation of Intracellular Drug of HL60/A and HL60 Cell and Its
            Mechanism]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 32 (1), 71-77 (2024)
   PUBMED   38387902
  REMARK    GeneRIF: [The Effect of TCP1 Expression on the Proliferation and
            the Accumulation of Intracellular Drug of HL60/A and HL60 Cell and
            Its Mechanism].
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Zhong,X.L., Qian,B.P., Huang,J.C., Zhao,S.Z., Li,Y. and Qiu,Y.
  TITLE     Low expression of TCP1 (T-Complex 1) and PSMC1 (Proteasome 26S
            subunit, ATPase 1) in heterotopic ossification during ankylosing
            spondylitis
  JOURNAL   Bioengineered 12 (1), 7459-7469 (2021)
   PUBMED   34612770
  REMARK    GeneRIF: Low expression of TCP1 (T-Complex 1) and PSMC1 (Proteasome
            26S subunit, ATPase 1) in heterotopic ossification during
            ankylosing spondylitis.
REFERENCE   5  (residues 1 to 556)
  AUTHORS   Weng,H., Feng,X., Lan,Y. and Zheng,Z.
  TITLE     TCP1 regulates PI3K/AKT/mTOR signaling pathway to promote
            proliferation of ovarian cancer cells
  JOURNAL   J Ovarian Res 14 (1), 82 (2021)
   PUBMED   34162426
  REMARK    GeneRIF: TCP1 regulates PI3K/AKT/mTOR signaling pathway to promote
            proliferation of ovarian cancer cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 556)
  AUTHORS   Lewis,V.A., Hynes,G.M., Zheng,D., Saibil,H. and Willison,K.
  TITLE     T-complex polypeptide-1 is a subunit of a heteromeric particle in
            the eukaryotic cytosol
  JOURNAL   Nature 358 (6383), 249-252 (1992)
   PUBMED   1630492
REFERENCE   7  (residues 1 to 556)
  AUTHORS   Yaffe,M.B., Farr,G.W., Miklos,D., Horwich,A.L., Sternlicht,M.L. and
            Sternlicht,H.
  TITLE     TCP1 complex is a molecular chaperone in tubulin biogenesis
  JOURNAL   Nature 358 (6383), 245-248 (1992)
   PUBMED   1630491
  REMARK    GeneRIF: a paper describing a pathway in which this gene product
            functions
REFERENCE   8  (residues 1 to 556)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   9  (residues 1 to 556)
  AUTHORS   Blanche,H., Wright,L.G., Vergnaud,G., de Gouyon,B., Lauthier,V.,
            Silver,L.M., Dausset,J., Cann,H.M. and Spielman,R.S.
  TITLE     Genetic mapping of three human homologues of murine t-complex genes
            localizes TCP10 to 6q27, 15 cM distal to TCP1 and PLG
  JOURNAL   Genomics 12 (4), 826-828 (1992)
   PUBMED   1572657
REFERENCE   10 (residues 1 to 556)
  AUTHORS   Ursic,D. and Culbertson,M.R.
  TITLE     The yeast homolog to mouse Tcp-1 affects microtubule-mediated
            processes
  JOURNAL   Mol Cell Biol 11 (5), 2629-2640 (1991)
   PUBMED   1901944
  REMARK    GeneRIF: a paper describing a pathway in which this gene product
            functions
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM827784.1, BC000665.1,
            BM697304.1 and AA810047.1.
            
            On Jan 15, 2005 this sequence version replaced NP_110379.1.
            
            Summary: The protein encoded by this gene is a molecular chaperone
            that is a member of the chaperonin containing TCP1 complex (CCT),
            also known as the TCP1 ring complex (TRiC). This complex consists
            of two identical stacked rings, each containing eight different
            proteins. Unfolded polypeptides enter the central cavity of the
            complex and are folded in an ATP-dependent manner. The complex
            folds various proteins, including actin and tubulin. Alternate
            transcriptional splice variants of this gene, encoding different
            isoforms, have been characterized. In addition, three pseudogenes
            that appear to be derived from this gene have been found. [provided
            by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1102035.1,
                                           SRR1660809.200873.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321394.12/ ENSP00000317334.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..556
                     /product="T-complex protein 1 subunit alpha isoform a"
                     /note="T-complex protein 1, alpha subunit; tailless
                     complex polypeptide 1; T-complex protein 1 subunit alpha;
                     t-complex 1 protein; chaperonin containing T-complex
                     polypeptide 1 subunit 1"
                     /calculated_mol_wt=60213
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P17987.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P17987.1)"
     Region          9..535
                     /region_name="TCP1_alpha"
                     /note="TCP-1 (CTT or eukaryotic type II) chaperonin
                     family, alpha subunit. Chaperonins are involved in
                     productive folding of proteins. They share a common
                     general morphology, a double toroid of 2 stacked rings. In
                     contrast to bacterial group I chaperonins...; cd03335"
                     /db_xref="CDD:239451"
     Site            order(9,13,41..44,46,64,66,70,74,77,382,526..532)
                     /site_type="other"
                     /note="ring oligomerisation interface [polypeptide
                     binding]"
                     /db_xref="CDD:239451"
     Site            order(36..38,88,92,154,394,412,452,503,505)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239451"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P17987.1)"
     Site            199
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P17987.1)"
     Site            400
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P17987.1)"
     Site            order(432,450,459,461..462,465)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239451"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P17987.1)"
     Site            494
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11983; propagated from
                     UniProtKB/Swiss-Prot (P17987.1)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P17987.1)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P17987.1)"
     CDS             1..556
                     /gene="TCP1"
                     /gene_synonym="CCT-alpha; CCT1; CCTa; D6S230E; IDDPMGS;
                     TCP-1-alpha"
                     /coded_by="NM_030752.3:135..1805"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5269.1"
                     /db_xref="GeneID:6950"
                     /db_xref="HGNC:HGNC:11655"
                     /db_xref="MIM:186980"
ORIGIN      
        1 megplsvfgd rstgetirsq nvmaaasian ivksslgpvg ldkmlvddig dvtitndgat
       61 ilkllevehp aakvlcelad lqdkevgdgt tsvviiaael lknadelvkq kihptsvisg
      121 yrlackeavr yinenlivnt delgrdclin aaktsmsski igingdffan mvvdavlaik
      181 ytdirgqpry pvnsvnilka hgrsqmesml isgyalncvv gsqgmpkriv nakiacldfs
      241 lqktkmklgv qvvitdpekl dqirqresdi tkeriqkila tganvilttg giddmclkyf
      301 veagamavrr vlkrdlkria kasgatilst lanlegeetf eaamlgqaee vvqericdde
      361 lilikntkar tsasiilrga ndfmcdemer slhdalcvvk rvlesksvvp gggaveaals
      421 iylenyatsm gsreqlaiae farsllvipn tlavnaaqds tdlvaklraf hneaqvnper
      481 knlkwigldl sngkprdnkq agvfeptivk vkslkfatea aitilriddl iklhpeskdd
      541 khgsyedavh sgalnd
//
LOCUS       NP_478123                376 aa            linear   PRI 27-APR-2025
DEFINITION  DNA repair protein RAD51 homolog 3 isoform 1 [Homo sapiens].
ACCESSION   NP_478123
VERSION     NP_478123.1
DBSOURCE    REFSEQ: accession NM_058216.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Rein,H.L. and Bernstein,K.A.
  TITLE     Variants in the first methionine of RAD51C are homologous
            recombination proficient due to an alternative start site
  JOURNAL   DNA Repair (Amst) 135, 103644 (2024)
   PUBMED   38330859
  REMARK    GeneRIF: Variants in the first methionine of RAD51C are homologous
            recombination proficient due to an alternative start site.
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Longo,M.A., Roy,S., Chen,Y., Tomaszowski,K.H., Arvai,A.S.,
            Pepper,J.T., Boisvert,R.A., Kunnimalaiyaan,S., Keshvani,C.,
            Schild,D., Bacolla,A., Williams,G.J., Tainer,J.A. and Schlacher,K.
  TITLE     RAD51C-XRCC3 structure and cancer patient mutations define DNA
            replication roles
  JOURNAL   Nat Commun 14 (1), 4445 (2023)
   PUBMED   37488098
  REMARK    GeneRIF: RAD51C-XRCC3 structure and cancer patient mutations define
            DNA replication roles.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Vaz,F., Hanenberg,H., Schuster,B., Barker,K., Wiek,C., Erven,V.,
            Neveling,K., Endt,D., Kesterton,I., Autore,F., Fraternali,F.,
            Freund,M., Hartmann,L., Grimwade,D., Roberts,R.G., Schaal,H.,
            Mohammed,S., Rahman,N., Schindler,D. and Mathew,C.G.
  TITLE     Mutation of the RAD51C gene in a Fanconi anemia-like disorder
  JOURNAL   Nat Genet 42 (5), 406-409 (2010)
   PUBMED   20400963
  REMARK    GeneRIF: biallelic germline mutations in a RAD51 paralog are
            associated with an FA-like syndrome [case report]
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Liu,Y., Masson,J.Y., Shah,R., O'Regan,P. and West,S.C.
  TITLE     RAD51C is required for Holliday junction processing in mammalian
            cells
  JOURNAL   Science 303 (5655), 243-246 (2004)
   PUBMED   14716019
  REMARK    GeneRIF: concluded that the RAD51 paralogs are involved in Holliday
            junction processing in human cells
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Kurumizaka,H., Ikawa,S., Nakada,M., Eda,K., Kagawa,W., Takata,M.,
            Takeda,S., Yokoyama,S. and Shibata,T.
  TITLE     Homologous-pairing activity of the human DNA-repair proteins
            Xrcc3.Rad51C
  JOURNAL   Proc Natl Acad Sci U S A 98 (10), 5538-5543 (2001)
   PUBMED   11331762
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Wu,G.J., Sinclair,C.S., Paape,J., Ingle,J.N., Roche,P.C.,
            James,C.D. and Couch,F.J.
  TITLE     17q23 amplifications in breast cancer involve the PAT1, RAD51C,
            PS6K, and SIGma1B genes
  JOURNAL   Cancer Res 60 (19), 5371-5375 (2000)
   PUBMED   11034073
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Barlund,M., Monni,O., Kononen,J., Cornelison,R., Torhorst,J.,
            Sauter,G., Kallioniemi,O.L.L.I.-P. and Kallioniemi,A.
  TITLE     Multiple genes at 17q23 undergo amplification and overexpression in
            breast cancer
  JOURNAL   Cancer Res 60 (19), 5340-5344 (2000)
   PUBMED   11034067
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Dosanjh,M.K., Collins,D.W., Fan,W., Lennon,G.G., Albala,J.S.,
            Shen,Z. and Schild,D.
  TITLE     Isolation and characterization of RAD51C, a new human member of the
            RAD51 family of related genes
  JOURNAL   Nucleic Acids Res 26 (5), 1179-1184 (1998)
   PUBMED   9469824
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Mehta,P.A. and Ebens,C.
  TITLE     Fanconi Anemia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301575
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF029669.1, CB243543.1 and
            AC025521.21.
            
            Summary: This gene is a member of the RAD51 family. RAD51 family
            members are highly similar to bacterial RecA and Saccharomyces
            cerevisiae Rad51 and are known to be involved in the homologous
            recombination and repair of DNA. This protein can interact with
            other RAD51 paralogs and is reported to be important for Holliday
            junction resolution. Mutations in this gene are associated with
            Fanconi anemia-like syndrome. This gene is one of four localized to
            a region of chromosome 17q23 where amplification occurs frequently
            in breast tumors. Overexpression of the four genes during
            amplification has been observed and suggests a possible role in
            tumor progression. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) is the longest transcript and
            encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF029669.1, SRR1803617.474.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337432.9/ ENSP00000336701.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q22"
     Protein         1..376
                     /product="DNA repair protein RAD51 homolog 3 isoform 1"
                     /note="yeast RAD51 homolog 3; DNA repair protein RAD51
                     homolog 3; RAD51-like protein 2"
                     /calculated_mol_wt=42059
     Region          1..126
                     /region_name="Required for Holliday junction resolution
                     activity"
                     /note="propagated from UniProtKB/Swiss-Prot (O43502.1)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43502.1)"
     Region          79..136
                     /region_name="Interaction with RAD51B, RAD51D and XRCC3.
                     /evidence=ECO:0000269|PubMed:14704354"
                     /note="propagated from UniProtKB/Swiss-Prot (O43502.1)"
     Region          118..330
                     /region_name="Rad51C"
                     /note="RAD51C recombinase; cd19492"
                     /db_xref="CDD:410900"
     Site            order(128..133,161,242,285,317)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:410900"
     Region          366..370
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43502.1)"
     CDS             1..376
                     /gene="RAD51C"
                     /gene_synonym="BROVCA3; FANCO; R51H3; RAD51L2"
                     /coded_by="NM_058216.3:43..1173"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11611.1"
                     /db_xref="GeneID:5889"
                     /db_xref="HGNC:HGNC:9820"
                     /db_xref="MIM:602774"
ORIGIN      
        1 mrgktfrfem qrdlvsfpls pavrvklvsa gfqtaeelle vkpselskev giskaealet
       61 lqiirreclt nkpryagtse shkkctalel leqehtqgfi itfcsalddi lgggvplmkt
      121 teicgapgvg ktqlcmqlav dvqipecfgg vageavfidt egsfmvdrvv dlataciqhl
      181 qliaekhkge ehrkaledft ldnilshiyy frcrdytell aqvyllpdfl sehskvrlvi
      241 vdgiafpfrh dlddlslrtr llnglaqqmi slannhrlav iltnqmttki drnqallvpa
      301 lgeswghaat irlifhwdrk qrlatlyksp sqkectvlfq ikpqgfrdtv vtsacslqte
      361 gslstrkrsr dpeeel
//
LOCUS       NP_001356531             531 aa            linear   PRI 27-APR-2025
DEFINITION  suppressor of tumorigenicity 7 protein isoform 6 [Homo sapiens].
ACCESSION   NP_001356531
VERSION     NP_001356531.1
DBSOURCE    REFSEQ: accession NM_001369602.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Liu,H., Lu,W., He,H., Wu,J., Zhang,C., Gong,H. and Yang,C.
  TITLE     Inflammation-dependent overexpression of c-Myc enhances CRL4DCAF4
            E3 ligase activity and promotes ubiquitination of ST7 in
            colitis-associated cancer
  JOURNAL   J Pathol 248 (4), 464-475 (2019)
   PUBMED   30945288
  REMARK    GeneRIF: Inflammation-dependent overexpression of c-Myc enhances
            CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7
            in colitis-associated cancer.
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yan,F., Alinari,L., Lustberg,M.E., Martin,L.K.,
            Cordero-Nieves,H.M., Banasavadi-Siddegowda,Y., Virk,S.,
            Barnholtz-Sloan,J., Bell,E.H., Wojton,J., Jacob,N.K.,
            Chakravarti,A., Nowicki,M.O., Wu,X., Lapalombella,R., Datta,J.,
            Yu,B., Gordon,K., Haseley,A., Patton,J.T., Smith,P.L., Ryu,J.,
            Zhang,X., Mo,X., Marcucci,G., Nuovo,G., Kwon,C.H., Byrd,J.C.,
            Chiocca,E.A., Li,C., Sif,S., Jacob,S., Lawler,S., Kaur,B. and
            Baiocchi,R.A.
  TITLE     Genetic validation of the protein arginine methyltransferase PRMT5
            as a candidate therapeutic target in glioblastoma
  JOURNAL   Cancer Res 74 (6), 1752-1765 (2014)
   PUBMED   24453002
  REMARK    GeneRIF: The tumor suppressor ST7 is a key gene silenced by PRMT5.
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Hu,L., Wu,C., Zhao,X., Heist,R., Su,L., Zhao,Y., Han,B., Cao,S.,
            Chu,M., Dai,J., Dong,J., Shu,Y., Xu,L., Chen,Y., Wang,Y., Lu,F.,
            Jiang,Y., Yu,D., Chen,H., Tan,W., Ma,H., Chen,J., Jin,G., Wu,T.,
            Lu,D., Christiani,D.C., Lin,D., Hu,Z. and Shen,H.
  TITLE     Genome-wide association study of prognosis in advanced non-small
            cell lung cancer patients receiving platinum-based chemotherapy
  JOURNAL   Clin Cancer Res 18 (19), 5507-5514 (2012)
   PUBMED   22872573
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Zenklusen,J.C., Rodriguez,L.V., LaCava,M., Wang,Z., Goldstein,L.S.
            and Conti,C.J.
  TITLE     Novel susceptibility locus for mouse hepatomas: evidence for a
            conserved tumor suppressor gene
  JOURNAL   Genome Res 6 (11), 1070-1076 (1996)
   PUBMED   8938430
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Zenklusen,J.C., Weitzel,J.N., Ball,H.G. and Conti,C.J.
  TITLE     Allelic loss at 7q31.1 in human primary ovarian carcinomas suggests
            the existence of a tumor suppressor gene
  JOURNAL   Oncogene 11 (2), 359-363 (1995)
   PUBMED   7624150
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Zenklusen,J.C., Thompson,J.C., Troncoso,P., Kagan,J. and Conti,C.J.
  TITLE     Loss of heterozygosity in human primary prostate carcinomas: a
            possible tumor suppressor gene at 7q31.1
  JOURNAL   Cancer Res 54 (24), 6370-6373 (1994)
   PUBMED   7987830
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Zenklusen,J.C., Bieche,I., Lidereau,R. and Conti,C.J.
  TITLE     (C-A)n microsatellite repeat D7S522 is the most commonly deleted
            region in human primary breast cancer
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12155-12158 (1994)
   PUBMED   7991599
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Ogata,T., Ayusawa,D., Namba,M., Takahashi,E., Oshimura,M. and
            Oishi,M.
  TITLE     Chromosome 7 suppresses indefinite division of nontumorigenic
            immortalized human fibroblast cell lines KMST-6 and SUSM-1
  JOURNAL   Mol Cell Biol 13 (10), 6036-6043 (1993)
   PUBMED   8105370
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106873.3, AC002542.1 and
            AC003987.1.
            
            Summary: The gene for this product maps to a region on chromosome 7
            identified as an autism-susceptibility locus. Mutation screening of
            the entire coding region in autistic individuals failed to identify
            phenotype-specific variants, suggesting that coding mutations for
            this gene are unlikely to be involved in the etiology of autism.
            The function of this gene product has not been determined.
            Transcript variants encoding different isoforms of this protein
            have been described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297861.1, SRR1163655.623429.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.2"
     Protein         1..531
                     /product="suppressor of tumorigenicity 7 protein isoform
                     6"
                     /note="family with sequence similarity 4, subfamily A,
                     member 1; suppression of tumorigenicity 7 (breast);
                     suppressor of tumorigenicity 7 protein"
                     /calculated_mol_wt=60568
     Region          5..530
                     /region_name="ST7"
                     /note="ST7 protein; pfam04184"
                     /db_xref="CDD:461214"
     CDS             1..531
                     /gene="ST7"
                     /gene_synonym="ETS7q; FAM4A; FAM4A1; HELG; RAY1; SEN4;
                     TSG7"
                     /coded_by="NM_001369602.1:91..1686"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS94183.1"
                     /db_xref="GeneID:7982"
                     /db_xref="HGNC:HGNC:11351"
                     /db_xref="MIM:600833"
ORIGIN      
        1 mdytvsmfln tltpkfyval tgtsslisgl ilifewwyfr kygtsfieqv svshlrpllg
       61 gvdnnssnns nssngdsdsn rqsvseckvw rnplnlfrga eynrytwvtg repltyydmn
      121 lsaqdhqtff tcdsdhlrpa daimqkawre rnpqarisaa healeineir srvevplias
      181 stiweikllp kcatayilla eeeattiaea eklfkqalka gdgcyrrsqq lqhhgsqyea
      241 qhrrdtnvlv yikrrlamca rrlgrtreav kmmrdlmkef pllsmfnihe nlleallelq
      301 ayadvqavla kyddislpks aticytaall karavsdkfs peaasrrgls taemnaveai
      361 hravefnphv pkyllemksl ilppehilkr gdseaiayaf fhlahwkrve galnllhctw
      421 egtfrmipyp lekghlfypy pictetadre llpsfhevsv ypkkelpffi lftaglcsft
      481 amlallthqf pelmgvfaka flstlfapln fvmekvesil psslwhqltr i
//
LOCUS       NP_659073                532 aa            linear   ROD 27-APR-2025
DEFINITION  telomerase Cajal body protein 1 [Mus musculus].
ACCESSION   NP_659073
VERSION     NP_659073.1
DBSOURCE    REFSEQ: accession NM_144824.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Guo,T., Han,X., He,J., Feng,J., Jing,J., Janeckova,E., Lei,J.,
            Ho,T.V., Xu,J. and Chai,Y.
  TITLE     KDM6B interacts with TFDP1 to activate P53 signaling in regulating
            mouse palatogenesis
  JOURNAL   Elife 11, e74595 (2022)
   PUBMED   35212626
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Chen,L., Roake,C.M., Freund,A., Batista,P.J., Tian,S., Yin,Y.A.,
            Gajera,C.R., Lin,S., Lee,B., Pech,M.F., Venteicher,A.S., Das,R.,
            Chang,H.Y. and Artandi,S.E.
  TITLE     An Activity Switch in Human Telomerase Based on RNA Conformation
            and Shaped by TCAB1
  JOURNAL   Cell 174 (1), 218-230 (2018)
   PUBMED   29804836
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Kannan,M., Bayam,E., Wagner,C., Rinaldi,B., Kretz,P.F., Tilly,P.,
            Roos,M., McGillewie,L., Bar,S., Minocha,S., Chevalier,C., Po,C.,
            Chelly,J., Mandel,J.L., Borgatti,R., Piton,A., Kinnear,C., Loos,B.,
            Adams,D.J., Herault,Y., Collins,S.C., Friant,S., Godin,J.D. and
            Yalcin,B.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     WD40-repeat 47, a microtubule-associated protein, is essential for
            brain development and autophagy
  JOURNAL   Proc Natl Acad Sci U S A 114 (44), E9308-E9317 (2017)
   PUBMED   29078390
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Sun,Y., Yang,C., Chen,J., Song,X., Li,Z., Duan,M., Li,J., Hu,X.,
            Wu,K., Yan,G., Yang,C., Liu,J., Tan,W. and Ye,M.
  TITLE     Overexpression of WDR79 in non-small cell lung cancer is linked to
            tumour progression
  JOURNAL   J Cell Mol Med 20 (4), 698-709 (2016)
   PUBMED   26849396
  REMARK    GeneRIF: Overexpression of WDR79 in non-small cell lung cancer is
            linked to tumor progression.
REFERENCE   7  (residues 1 to 532)
  AUTHORS   Mahmoudi,S., Henriksson,S., Corcoran,M., Mendez-Vidal,C.,
            Wiman,K.G. and Farnebo,M.
  TITLE     Wrap53, a natural p53 antisense transcript required for p53
            induction upon DNA damage
  JOURNAL   Mol Cell 33 (4), 462-471 (2009)
   PUBMED   19250907
  REMARK    Erratum:[Mol Cell. 2016 Dec 1;64(5):1009. doi:
            10.1016/j.molcel.2016.11.027. PMID: 27912092]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL731687.13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021790.1, AK145219.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 42.81 cM"
     Protein         1..532
                     /product="telomerase Cajal body protein 1"
                     /note="WD repeat-containing protein 79; WD40
                     repeat-containing protein encoded by RNA antisense to p53;
                     WD repeat domain 79; WD repeat containing, antisense to
                     TP53; WD repeat-containing protein WRAP53; WD40
                     repeat-containing protein antisense to TP53 gene homolog"
                     /calculated_mol_wt=58020
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q8VC51.1)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          80..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          151..190
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          159..204
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <161..466
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          206..251
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          211..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          256..297
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          264..303
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          307..348
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          313..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          349..389
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          354..394
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          395..434
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          402..442
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q8VC51.1)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q8VC51.1)"
     Region          510..532
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC51.1)"
     CDS             1..532
                     /gene="Wrap53"
                     /gene_synonym="Wdr79"
                     /coded_by="NM_144824.3:198..1796"
                     /db_xref="CCDS:CCDS24897.1"
                     /db_xref="GeneID:216853"
                     /db_xref="MGI:MGI:2384933"
ORIGIN      
        1 mktseerlla pdslppdlap apvpqgspae kntdfepvpp pcggddqpql atdpvaslvv
       61 sqelqqgdsv plevefntss elspgieeqd vsehaslpge etnlpelesg eategvseer
      121 aevdegdtfw tysfsqvpry lsgswsefst rsenflkgck wapdgscilt nsadnvlriy
      181 nlppelyseq eqvdyaemvp vlrmvegdti ydycwyslms stqpdtsyva sssrenpihi
      241 wdaftgelra sfraynhlde ltaahslcfs pdgsqlfcgf nrtvrvfsts rpgrdcevra
      301 tfakkqgqsg iisciafsps qplyacgsyg rtiglyawdd gsplallggh qggithlcfh
      361 pdgnlffsga rkdaellcwd lrqpghllws lsrevttnqr iyfdldpsgq flvsgntsgv
      421 vsvwdisgal sddsklepvv tflpqkdctn gvslhptlpl latasgqrvf peptnsgdeg
      481 elelelplls lchahpecql qlwwcgggpd psspvddqde kgqrrteavg ms
//
LOCUS       NP_001356612             496 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 53 isoform c [Homo
            sapiens].
ACCESSION   NP_001356612 XP_005264626
VERSION     NP_001356612.1
DBSOURCE    REFSEQ: accession NM_001369683.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Kim,S. and Jang,C.Y.
  TITLE     ANKRD53 interacts with DDA3 and regulates chromosome integrity
            during mitosis
  JOURNAL   Biochem Biophys Res Commun 470 (3), 484-491 (2016)
   PUBMED   26820536
  REMARK    GeneRIF: Thus, ANKRD53 is recruited to the mitotic spindle by DDA3
            and acts as a regulator of spindle dynamics and cytokinesis.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007040.2.
            
            On Apr 15, 2019 this sequence version replaced XP_005264626.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2145245 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..496
                     /product="ankyrin repeat domain-containing protein 53
                     isoform c"
                     /note="ankyrin repeat domain-containing protein 53"
                     /calculated_mol_wt=55870
     Region          <66..278
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          106..137
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(107,111..112,115..117,119..120,124,127,137,139,141,
                     145..146,149..151,157..158,162,165,174,176,178,182..183,
                     186..188,190..191,195,198,207)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          139..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          176..207
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..496
                     /gene="ANKRD53"
                     /coded_by="NM_001369683.1:202..1692"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92774.1"
                     /db_xref="GeneID:79998"
                     /db_xref="HGNC:HGNC:25691"
                     /db_xref="MIM:617009"
ORIGIN      
        1 masagstarr agsgswhser gegrgarpqp tpsgsmqqan kvslkatwtd aeskqpspsk
       61 esdqtaidqt aigsyyqlfa aavgnvewlr fclnqslrei ptddkgftai hfaaqwgkla
      121 clqvlveeyk fpvdlltnns qtplhlvihr dnttvalpci yyllekgadl naqtcngstp
      181 lhlaardgll dcvkvlvqsg anvhaqdamg ykpidfckiw nhracarflk damwkkdkkd
      241 faremtkmkm fksqltlmeh nylieyqkeh kilreaairk wlhgklhpgh slvsntkqar
      301 atalsktpeq resqrsrsfh psvdarlqci pqptempkpi yrkptvkrpt mwnvsnnpar
      361 ppttqishsq girlgvhpdp tpehdfssfl evrpdghgga rlhtvdghwv apvprlpfev
      421 llrmlyprvw pyrmkvpqgf ypismrevpr krhlgdntfw tdtlamnlrd tfdeaflaav
      481 rshqglptlp spqtnp
//
LOCUS       NP_001354484             117 aa            linear   PRI 27-APR-2025
DEFINITION  oxidized purine nucleoside triphosphate hydrolase isoform 3 [Homo
            sapiens].
ACCESSION   NP_001354484
VERSION     NP_001354484.1
DBSOURCE    REFSEQ: accession NM_001367555.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Xu,W., Zhang,Y., Su,Y., Li,L., Yang,X., Wang,L. and Gao,H.
  TITLE     USP9X regulates the proliferation, survival, migration and invasion
            of gastric cancer cells by stabilizing MTH1
  JOURNAL   BMC Gastroenterol 24 (1), 239 (2024)
   PUBMED   39075342
  REMARK    GeneRIF: USP9X regulates the proliferation, survival, migration and
            invasion of gastric cancer cells by stabilizing MTH1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Lau,H.C., Yuan,X., Huang,H., Zhang,M., Hsueh,C.Y. and Gong,H.
  TITLE     Fusobacterium nucleatum facilitates proliferation and autophagy by
            activating miR-361-3p/NUDT1 axis through oxidative stress in
            hypopharyngeal squamous cell carcinoma
  JOURNAL   BMC Cancer 23 (1), 990 (2023)
   PUBMED   37848855
  REMARK    GeneRIF: Fusobacterium nucleatum facilitates proliferation and
            autophagy by activating miR-361-3p/NUDT1 axis through oxidative
            stress in hypopharyngeal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Nakamura,T., Koga-Ogawa,Y., Fujimiya,K., Chirifu,M., Goto,M.,
            Ikemizu,S., Nakabeppu,Y. and Yamagata,Y.
  TITLE     Protonation states of Asp residues in the human Nudix hydrolase
            MTH1 contribute to its broad substrate recognition
  JOURNAL   FEBS Lett 597 (13), 1770-1778 (2023)
   PUBMED   36914375
  REMARK    GeneRIF: Protonation states of Asp residues in the human Nudix
            hydrolase MTH1 contribute to its broad substrate recognition.
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Zhang,J., Liu,R., Mo,L., Liu,C. and Jiang,J.
  TITLE     miR-4478 Accelerates Nucleus Pulposus Cells Apoptosis Induced by
            Oxidative Stress by Targeting MTH1
  JOURNAL   Spine (Phila Pa 1976) 48 (5), E54-E69 (2023)
   PUBMED   36130054
  REMARK    GeneRIF: miR-4478 Accelerates Nucleus Pulposus Cells Apoptosis
            Induced by Oxidative Stress by Targeting MTH1.
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Li,J., Wang,Z.H., Dang,Y.M., Li,D.N., Liu,Z., Dai,D.P. and Cai,J.P.
  TITLE     MTH1 suppression enhances the stemness of MCF7 through upregulation
            of STAT3
  JOURNAL   Free Radic Biol Med 188, 447-458 (2022)
   PUBMED   35809767
  REMARK    GeneRIF: MTH1 suppression enhances the stemness of MCF7 through
            upregulation of STAT3.
REFERENCE   6  (residues 1 to 117)
  AUTHORS   Oda,H., Taketomi,A., Maruyama,R., Itoh,R., Nishioka,K.,
            Yakushiji,H., Suzuki,T., Sekiguchi,M. and Nakabeppu,Y.
  TITLE     Multi-forms of human MTH1 polypeptides produced by alternative
            translation initiation and single nucleotide polymorphism
  JOURNAL   Nucleic Acids Res 27 (22), 4335-4343 (1999)
   PUBMED   10536140
REFERENCE   7  (residues 1 to 117)
  AUTHORS   Kang,D., Nishida,J., Iyama,A., Nakabeppu,Y., Furuichi,M.,
            Fujiwara,T., Sekiguchi,M. and Takeshige,K.
  TITLE     Intracellular localization of 8-oxo-dGTPase in human cells, with
            special reference to the role of the enzyme in mitochondria
  JOURNAL   J Biol Chem 270 (24), 14659-14665 (1995)
   PUBMED   7782328
REFERENCE   8  (residues 1 to 117)
  AUTHORS   Furuichi,M., Yoshida,M.C., Oda,H., Tajiri,T., Nakabeppu,Y.,
            Tsuzuki,T. and Sekiguchi,M.
  TITLE     Genomic structure and chromosome location of the human mutT
            homologue gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to
            C:G transversion
  JOURNAL   Genomics 24 (3), 485-490 (1994)
   PUBMED   7713500
REFERENCE   9  (residues 1 to 117)
  AUTHORS   Ponnambalam,S., Jackson,A.P., LeBeau,M.M., Pravtcheva,D.,
            Ruddle,F.H., Alibert,C. and Parham,P.
  TITLE     Chromosomal location and some structural features of human clathrin
            light-chain genes (CLTA and CLTB)
  JOURNAL   Genomics 24 (3), 440-444 (1994)
   PUBMED   7713494
REFERENCE   10 (residues 1 to 117)
  AUTHORS   Sakumi,K., Furuichi,M., Tsuzuki,T., Kakuma,T., Kawabata,S., Maki,H.
            and Sekiguchi,M.
  TITLE     Cloning and expression of cDNA for a human enzyme that hydrolyzes
            8-oxo-dGTP, a mutagenic substrate for DNA synthesis
  JOURNAL   J Biol Chem 268 (31), 23524-23530 (1993)
   PUBMED   8226881
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004971.3.
            
            Summary: Misincorporation of oxidized nucleoside triphosphates into
            DNA/RNA during replication and transcription can cause mutations
            that may result in carcinogenesis or neurodegeneration. The protein
            encoded by this gene is an enzyme that hydrolyzes oxidized purine
            nucleoside triphosphates, such as 8-oxo-dGTP, 8-oxo-dATP,
            2-hydroxy-dATP, and 2-hydroxy rATP, to monophosphates, thereby
            preventing misincorporation. The encoded protein is localized
            mainly in the cytoplasm, with some in the mitochondria, suggesting
            that it is involved in the sanitization of nucleotide pools both
            for nuclear and mitochondrial genomes. Several alternatively
            spliced transcript variants, some of which encode distinct
            isoforms, have been identified. Additional variants have been
            observed, but their full-length natures have not been determined. A
            rare single-nucleotide polymorphism that results in the production
            of an additional, longer isoform (p26) has been described.
            [provided by RefSeq, Dec 2018].
            
            Transcript Variant: This variant (7), as well as variant 6, encodes
            isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2149398 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..117
                     /product="oxidized purine nucleoside triphosphate
                     hydrolase isoform 3"
                     /EC_number="3.6.1.56"
                     /note="8-oxo-7,8-dihydrodeoxyguanosine triphosphatase;
                     8-oxo-dGTPase; 7,8-dihydro-8-oxoguanine triphosphatase;
                     8-oxo-7,8-dihydroguanosine triphosphatase; mutT human
                     homolog 1; nudix motif 1; nucleoside diphosphate-linked
                     moiety X-type motif 1; nudix (nucleoside diphosphate
                     linked moiety X)-type motif 1; nucleoside
                     diphosphate-linked moiety X motif 1; 2-hydroxy-dATP
                     diphosphatase; methylated purine nucleoside triphosphate
                     hydrolase; oxidized purine nucleoside triphosphate
                     hydrolase"
                     /calculated_mol_wt=12688
     Region          5..>99
                     /region_name="NUDIX_MTH1_Nudt1"
                     /note="MutT homolog-1 (MTH1); cd03427"
                     /db_xref="CDD:467533"
     Region          37..58
                     /region_name="Nudix box.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00794"
                     /note="propagated from UniProtKB/Swiss-Prot (P36639.4)"
     CDS             1..117
                     /gene="NUDT1"
                     /gene_synonym="MTH1"
                     /coded_by="NM_001367555.1:44..397"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="GeneID:4521"
                     /db_xref="HGNC:HGNC:8048"
                     /db_xref="MIM:600312"
ORIGIN      
        1 mgasrlytlv lvlqpqrvll gmkkrgfgag rwngfggkvq egetiedgar relqeesglt
       61 vdalhkvgqi vfefvgepel mdvhvfctds iqgtpvesdv etgfhrvsqd gldllts
//
LOCUS       NP_598419                783 aa            linear   ROD 27-APR-2025
DEFINITION  general transcription and DNA repair factor IIH
            helicase/translocase subunit XPB [Mus musculus].
ACCESSION   NP_598419
VERSION     NP_598419.1
DBSOURCE    REFSEQ: accession NM_133658.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Mourgues,S., Gautier,V., Lagarou,A., Bordier,C., Mourcet,A.,
            Slingerland,J., Kaddoum,L., Coin,F., Vermeulen,W., Gonzales de
            Peredo,A., Monsarrat,B., Mari,P.O. and Giglia-Mari,G.
  TITLE     ELL, a novel TFIIH partner, is involved in transcription restart
            after DNA repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (44), 17927-17932 (2013)
   PUBMED   24127601
REFERENCE   3  (residues 1 to 783)
  AUTHORS   Nonnekens,J., Perez-Fernandez,J., Theil,A.F., Gadal,O., Bonnart,C.
            and Giglia-Mari,G.
  TITLE     Mutations in TFIIH causing trichothiodystrophy are responsible for
            defects in ribosomal RNA production and processing
  JOURNAL   Hum Mol Genet 22 (14), 2881-2893 (2013)
   PUBMED   23562818
REFERENCE   4  (residues 1 to 783)
  AUTHORS   Laugel-Haushalter,V., Langer,A., Marrie,J., Fraulob,V.,
            Schuhbaur,B., Koch-Phillips,M., Dolle,P. and Bloch-Zupan,A.
  TITLE     From the transcription of genes involved in ectodermal dysplasias
            to the understanding of associated dental anomalies
  JOURNAL   Mol Syndromol 3 (4), 158-168 (2012)
   PUBMED   23239958
REFERENCE   5  (residues 1 to 783)
  AUTHORS   Godon,C., Mourgues,S., Nonnekens,J., Mourcet,A., Coin,F.,
            Vermeulen,W., Mari,P.O. and Giglia-Mari,G.
  TITLE     Generation of DNA single-strand displacement by compromised
            nucleotide excision repair
  JOURNAL   EMBO J 31 (17), 3550-3563 (2012)
   PUBMED   22863773
REFERENCE   6  (residues 1 to 783)
  AUTHORS   Binato,R., Alvarez Martinez,C.E., Pizzatti,L., Robert,B. and
            Abdelhay,E.
  TITLE     SMAD 8 binding to mice Msx1 basal promoter is required for
            transcriptional activation
  JOURNAL   Biochem J 393 (Pt 1), 141-150 (2006)
   PUBMED   16101586
REFERENCE   7  (residues 1 to 783)
  AUTHORS   Le May,N., Dubaele,S., Proietti De Santis,L., Billecocq,A.,
            Bouloy,M. and Egly,J.M.
  TITLE     TFIIH transcription factor, a target for the Rift Valley
            hemorrhagic fever virus
  JOURNAL   Cell 116 (4), 541-550 (2004)
   PUBMED   14980221
REFERENCE   8  (residues 1 to 783)
  AUTHORS   De Graeve,F., Bahr,A., Chatton,B. and Kedinger,C.
  TITLE     A murine ATFa-associated factor with transcriptional repressing
            activity
  JOURNAL   Oncogene 19 (14), 1807-1819 (2000)
   PUBMED   10777215
REFERENCE   9  (residues 1 to 783)
  AUTHORS   Hubank,M. and Mayne,L.
  TITLE     Expression of the excision repair gene, ERCC3 (excision repair
            cross-complementing), during mouse development
  JOURNAL   Brain Res Dev Brain Res 81 (1), 66-76 (1994)
   PUBMED   7805288
REFERENCE   10 (residues 1 to 783)
  AUTHORS   Weeda,G., Ma,L., van Ham,R.C., Bootsma,D., van der Eb,A.J. and
            Hoeijmakers,J.H.
  TITLE     Characterization of the mouse homolog of the XPBC/ERCC-3 gene
            implicated in xeroderma pigmentosum and Cockayne's syndrome
  JOURNAL   Carcinogenesis 12 (12), 2361-2368 (1991)
   PUBMED   1747940
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY273530.1, S71186.1 and BC022956.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK151188.1, AK152347.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849377, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 17.97 cM"
     Protein         1..783
                     /product="general transcription and DNA repair factor IIH
                     helicase/translocase subunit XPB"
                     /EC_number="5.6.2.4"
                     /note="TFIIH basal transcription factor complex helicase
                     XPB subunit; xeroderma pigmentosum group B-complementing
                     protein; TFIIH 89 kDa subunit; DNA excision repair protein
                     ERCC-3; DNA repair protein complementing XP-B cells; basic
                     transcription factor 2 89 kDa subunit; general
                     transcription and DNA repair factor IIH helicase subunit
                     XPB; DNA 3'-5' helicase/translocase XPB"
                     /calculated_mol_wt=88996
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49135.1)"
     Region          6..18
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P49135.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4G005; propagated from
                     UniProtKB/Swiss-Prot (P49135.1)"
     Region          60..780
                     /region_name="rad25"
                     /note="DNA repair helicase rad25; TIGR00603"
                     /db_xref="CDD:273168"
     Region          442..445
                     /region_name="DEVH box"
                     /note="propagated from UniProtKB/Swiss-Prot (P49135.1)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19447; propagated from
                     UniProtKB/Swiss-Prot (P49135.1)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P19447; propagated from
                     UniProtKB/Swiss-Prot (P49135.1)"
     CDS             1..783
                     /gene="Ercc3"
                     /gene_synonym="BTF2 p89; Ercc-3; XPB"
                     /coded_by="NM_133658.2:68..2419"
                     /db_xref="CCDS:CCDS29118.1"
                     /db_xref="GeneID:13872"
                     /db_xref="MGI:MGI:95414"
ORIGIN      
        1 mgkrdrvdrd kkkskkrqye eeeededdip gnesqeavps aagkqvdess tkvdeygakd
       61 yrqqmplkgd htsrplwvap dghifleafs pvykyaqdfl vaiaepvcrp thvheyklta
      121 yslyaavsvg lqtsditeyl rklsktgvpd giiqfiklct vsygkvklvl khnryfvess
      181 hpdviqhllq dpvirecrlr naegeateli tetftsksai sktaaegsgg pstsqgvdaq
      241 atsdipkdlf dfyeqmdkde eeeeetqtvs fevkqemiee lqkrcicley pllaeydfrn
      301 dtlnpdinid lkptavlrpy qekslrkmfg ngrarsgviv lpcgagkslv gvtaactvrk
      361 rclvlgnsav sveqwkaqfk mwstiddsqi crftsdakdk pigcsvaist ysmlghttkr
      421 sweaervmew lktqewglmi ldevhtipar mfrrvltivq ahcklgltat lvreddkivd
      481 lnfligpkly eanwmelqnn gyiakvqcae vwcpmspefy reyvaiktkk rillytmnpn
      541 kfracqflik fherrndkii vfadnvfalk eyairlnkpy iygptsqger mqilqnfkhn
      601 pkintifisk vgdtsfdlpe anvliqissh ggsrrqeaqr lgrvlrakkg mvaeeynaff
      661 yslvsqdtqe maystkrqrf lvdqgysfkv itklagmeee elafstkeeq qqllqkvlaa
      721 tdldaeeevv agefgsrsgq asrrcgtmss lsgaddtvym eyhssrskas skhvhplfkr
      781 frk
//
LOCUS       NP_705806                323 aa            linear   ROD 27-APR-2025
DEFINITION  magnesium transporter NIPA1 [Mus musculus].
ACCESSION   NP_705806
VERSION     NP_705806.1
DBSOURCE    REFSEQ: accession NM_153578.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Adissu,H.A., Estabel,J., Sunter,D., Tuck,E., Hooks,Y.,
            Carragher,D.M., Clarke,K., Karp,N.A., Newbigging,S., Jones,N.,
            Morikawa,L., White,J.K. and McKerlie,C.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Histopathology reveals correlative and unique phenotypes in a
            high-throughput mouse phenotyping screen
  JOURNAL   Dis Model Mech 7 (5), 515-524 (2014)
   PUBMED   24652767
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Botzolakis,E.J., Zhao,J., Gurba,K.N., Macdonald,R.L. and Hedera,P.
  TITLE     The effect of HSP-causing mutations in SPG3A and NIPA1 on the
            assembly, trafficking, and interaction between atlastin-1 and NIPA1
  JOURNAL   Mol Cell Neurosci 46 (1), 122-135 (2011)
   PUBMED   20816793
REFERENCE   5  (residues 1 to 323)
  AUTHORS   van der Zwaag,B., Staal,W.G., Hochstenbach,R., Poot,M.,
            Spierenburg,H.A., de Jonge,M.V., Verbeek,N.E., van 't Slot,R., van
            Es,M.A., Staal,F.J., Freitag,C.M., Buizer-Voskamp,J.E., Nelen,M.R.,
            van den Berg,L.H., van Amstel,H.K., van Engeland,H. and
            Burbach,J.P.
  TITLE     A co-segregating microduplication of chromosome 15q11.2 pinpoints
            two risk genes for autism spectrum disorder
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 153B (4), 960-966 (2010)
   PUBMED   20029941
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Zhao,J., Matthies,D.S., Botzolakis,E.J., Macdonald,R.L.,
            Blakely,R.D. and Hedera,P.
  TITLE     Hereditary spastic paraplegia-associated mutations in the NIPA1
            gene and its Caenorhabditis elegans homolog trigger neural
            degeneration in vitro and in vivo through a gain-of-function
            mechanism
  JOURNAL   J Neurosci 28 (51), 13938-13951 (2008)
   PUBMED   19091982
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Goytain,A., Hines,R.M., El-Husseini,A. and Quamme,G.A.
  TITLE     NIPA1(SPG6), the basis for autosomal dominant form of hereditary
            spastic paraplegia, encodes a functional Mg2+ transporter
  JOURNAL   J Biol Chem 282 (11), 8060-8068 (2007)
   PUBMED   17166836
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Chai,J.H., Locke,D.P., Greally,J.M., Knoll,J.H., Ohta,T., Dunai,J.,
            Yavor,A., Eichler,E.E. and Nicholls,R.D.
  TITLE     Identification of four highly conserved genes between breakpoint
            hotspots BP1 and BP2 of the Prader-Willi/Angelman syndromes
            deletion region that have undergone evolutionary transposition
            mediated by flanking duplicons
  JOURNAL   Am J Hum Genet 73 (4), 898-925 (2003)
   PUBMED   14508708
  REMARK    GeneRIF: indentification on mouse chromosome 7C
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC102121.7.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC055828.1, AY098645.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02415126 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 33.42 cM"
     Protein         1..323
                     /product="magnesium transporter NIPA1"
                     /note="non-imprinted in Prader-Willi/Angelman syndrome
                     region protein 1 homolog; spastic paraplegia 6 homolog"
                     /calculated_mol_wt=33974
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BHK1.1)"
     Region          25..307
                     /region_name="EamA"
                     /note="EamA-like transporter family; cl23754"
                     /db_xref="CDD:474045"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BHK1.1)"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BHK1.1)"
     Site            112..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BHK1.1)"
     Site            154..174
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BHK1.1)"
     Site            178..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BHK1.1)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BHK1.1)"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BHK1.1)"
     Site            285..305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BHK1.1)"
     CDS             1..323
                     /gene="Nipa1"
                     /gene_synonym="1110027G09Rik; A830014A18Rik; FSP3; Spg6"
                     /coded_by="NM_153578.3:33..1004"
                     /db_xref="CCDS:CCDS21317.1"
                     /db_xref="GeneID:233280"
                     /db_xref="MGI:MGI:2442058"
ORIGIN      
        1 mgtaaaaaaa gegargpspa avslglgvav vsslvngstf vlqkkgivra krrgtsyltd
       61 ivwwagtiam avgqignfla ytavptvlvt plgalgvpfg silasyllke klnilgklgc
      121 llscagsvvl iihspksesv ttqaeleekl tnpvfvgylc ivllmlllli fwiapahgpt
      181 nimvyisics llgsftvpst kgiglaaqdi lhnnpssqra lclclvllav lgcsiivqfr
      241 yinkalecfd ssvfgaiyyv vfttlvllas ailfrewsnv glvdflgmac gfttvsvgiv
      301 liqvfkefnf nlgemnksnm ktd
//
LOCUS       NP_666346                131 aa            linear   ROD 27-APR-2025
DEFINITION  ER membrane protein complex subunit 5 [Mus musculus].
ACCESSION   NP_666346
VERSION     NP_666346.1
DBSOURCE    REFSEQ: accession NM_146234.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Guna,A., Volkmar,N., Christianson,J.C. and Hegde,R.S.
  TITLE     The ER membrane protein complex is a transmembrane domain insertase
  JOURNAL   Science 359 (6374), 470-473 (2018)
   PUBMED   29242231
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Spierings,D.C., McGoldrick,D., Hamilton-Easton,A.M., Neale,G.,
            Murchison,E.P., Hannon,G.J., Green,D.R. and Withoff,S.
  TITLE     Ordered progression of stage-specific miRNA profiles in the mouse
            B2 B-cell lineage
  JOURNAL   Blood 117 (20), 5340-5349 (2011)
   PUBMED   21403133
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Kozomara,A. and Griffiths-Jones,S.
  TITLE     miRBase: integrating microRNA annotation and deep-sequencing data
  JOURNAL   Nucleic Acids Res 39 (Database issue), D152-D157 (2011)
   PUBMED   21037258
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Goytain,A. and Quamme,G.A.
  TITLE     Identification and characterization of a novel family of membrane
            magnesium transporters, MMgT1 and MMgT2
  JOURNAL   Am J Physiol Cell Physiol 294 (2), C495-C502 (2008)
   PUBMED   18057121
  REMARK    GeneRIF: These experiments suggest that MMgT proteins may provide
            regulated pathways for Mg(2+) transport in the Golgi and post-Golgi
            organelles of epithelium-derived cells.(MMgT1 PROTEIN, MOUSE)
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Bailey,P.J., Klos,J.M., Andersson,E., Karlen,M., Kallstrom,M.,
            Ponjavic,J., Muhr,J., Lenhard,B., Sandelin,A. and Ericson,J.
  TITLE     A global genomic transcriptional code associated with CNS-expressed
            genes
  JOURNAL   Exp Cell Res 312 (16), 3108-3119 (2006)
   PUBMED   16919269
REFERENCE   6  (residues 1 to 131)
  AUTHORS   Taniwaki,T., Haruna,K., Nakamura,H., Sekimoto,T., Oike,Y.,
            Imaizumi,T., Saito,F., Muta,M., Soejima,Y., Utoh,A., Nakagata,N.,
            Araki,M., Yamamura,K. and Araki,K.
  TITLE     Characterization of an exchangeable gene trap using pU-17 carrying
            a stop codon-beta geo cassette
  JOURNAL   Dev Growth Differ 47 (3), 163-172 (2005)
   PUBMED   15840001
REFERENCE   7  (residues 1 to 131)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC048362.14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK036253.1, AK049689.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="X"
                     /map="X 30.06 cM"
     Protein         1..131
                     /product="ER membrane protein complex subunit 5"
                     /note="transmembrane protein 32"
                     /calculated_mol_wt=14546
     Site            4..22
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K273.1)"
     Region          29..>61
                     /region_name="MMgT"
                     /note="Membrane magnesium transporter; pfam10270"
                     /db_xref="CDD:431186"
     Site            44..63
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K273.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8K273.1)"
     CDS             1..131
                     /gene="Mmgt1"
                     /gene_synonym="9630048L06Rik; Emc5; mir-5116; Mir5116;
                     Tmem32"
                     /coded_by="NM_146234.4:82..477"
                     /db_xref="CCDS:CCDS30147.1"
                     /db_xref="GeneID:236792"
                     /db_xref="MGI:MGI:2384305"
ORIGIN      
        1 mapslwkglv gvglfalaha afsaaqhrsy mrltekedes lpidivlqtl lafavtcygi
       61 vhiagefkdm datselknkt fdtlrnhpsf yvfnhrgrvl frpsdatnss nldalssnts
      121 lklrkfdslr r
//
LOCUS       NP_000610                166 aa            linear   PRI 27-APR-2025
DEFINITION  interferon gamma precursor [Homo sapiens].
ACCESSION   NP_000610
VERSION     NP_000610.2
DBSOURCE    REFSEQ: accession NM_000619.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Lin,C.I., Wang,Y.W., Su,K.Y. and Chuang,Y.H.
  TITLE     Interleukin-37 exacerbates liver inflammation and promotes
            IFN-gamma production in NK cells
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113086 (2024)
   PUBMED   39260304
  REMARK    GeneRIF: Interleukin-37 exacerbates liver inflammation and promotes
            IFN-gamma production in NK cells.
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Wang,S., Cheng,T., Chen,X., Zeng,C., Qin,W. and Xu,Y.
  TITLE     IFN-gamma induces acute graft-versus-host disease by promoting
            HMGB1-mediated nuclear-to-cytoplasm translocation and autophagic
            degradation of p53
  JOURNAL   Clin Sci (Lond) 138 (20), 1287-1304 (2024)
   PUBMED   39312196
  REMARK    GeneRIF: IFN-gamma induces acute graft-versus-host disease by
            promoting HMGB1-mediated nuclear-to-cytoplasm translocation and
            autophagic degradation of p53.
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Hanin,A., Comi,M., Sumida,T.S. and Hafler,D.A.
  TITLE     Cholesterol promotes IFNG mRNA expression in CD4+ effector/memory
            cells by SGK1 activation
  JOURNAL   Life Sci Alliance 7 (12), e202402890 (2024)
   PUBMED   39366761
  REMARK    GeneRIF: Cholesterol promotes IFNG mRNA expression in CD4[+]
            effector/memory cells by SGK1 activation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Hautala,N.M., Joensuu,M., Paakkola,T., Glumoff,V., Kettunen,K.,
            Saarela,J., Siiskonen,M., Chen,Z., Pylkas,K. and Hautala,T.
  TITLE     Recurrent ocular toxoplasmosis is associated with interferon-gamma
            deficiency possibly due to genetic origin
  JOURNAL   BMJ Open Ophthalmol 9 (1), e001769 (2024)
   PUBMED   39277179
  REMARK    GeneRIF: Recurrent ocular toxoplasmosis is associated with
            interferon-gamma deficiency possibly due to genetic origin.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Walter,M.R., Windsor,W.T., Nagabhushan,T.L., Lundell,D.J.,
            Lunn,C.A., Zauodny,P.J. and Narula,S.K.
  TITLE     Crystal structure of a complex between interferon-gamma and its
            soluble high-affinity receptor
  JOURNAL   Nature 376 (6537), 230-235 (1995)
   PUBMED   7617032
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Emilie,D., Maillot,M.C., Nicolas,J.F., Fior,R. and Galanaud,P.
  TITLE     Antagonistic effect of interferon-gamma on tat-induced
            transactivation of HIV long terminal repeat
  JOURNAL   J Biol Chem 267 (29), 20565-20570 (1992)
   PUBMED   1400376
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Grzesiek,S., Dobeli,H., Gentz,R., Garotta,G., Labhardt,A.M. and
            Bax,A.
  TITLE     1H, 13C, and 15N NMR backbone assignments and secondary structure
            of human interferon-gamma
  JOURNAL   Biochemistry 31 (35), 8180-8190 (1992)
   PUBMED   1525157
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Slodowski,O., Bohm,J., Schone,B. and Otto,B.
  TITLE     Carboxy-terminal truncated rhuIFN-gamma with a substitution of
            Gln133 or Ser132 to leucine leads to higher biological activity
            than in the wild type
  JOURNAL   Eur J Biochem 202 (3), 1133-1140 (1991)
   PUBMED   1662603
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Gray,P.W. and Goeddel,D.V.
  TITLE     Structure of the human immune interferon gene
  JOURNAL   Nature 298 (5877), 859-863 (1982)
   PUBMED   6180322
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Devos,R., Cheroutre,H., Taya,Y., Degrave,W., Van Heuverswyn,H. and
            Fiers,W.
  TITLE     Molecular cloning of human immune interferon cDNA and its
            expression in eukaryotic cells
  JOURNAL   Nucleic Acids Res 10 (8), 2487-2501 (1982)
   PUBMED   6176945
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC070256.1, V00543.1 and
            AC007458.14.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 22, 2004 this sequence version replaced NP_000610.1.
            
            Summary: This gene encodes a soluble cytokine that is a member of
            the type II interferon class. The encoded protein is secreted by
            cells of both the innate and adaptive immune systems. The active
            protein is a homodimer that binds to the interferon gamma receptor
            which triggers a cellular response to viral and microbial
            infections. Mutations in this gene are associated with an increased
            susceptibility to viral, bacterial and parasitic infections and to
            several autoimmune diseases. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070256.1, SRR1163655.241293.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in cytokine storm inflammatory
                                      response
            MANE Ensembl match     :: ENST00000229135.4/ ENSP00000229135.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..166
                     /product="interferon gamma precursor"
                     /note="IFN-gamma; immune interferon"
                     /calculated_mol_wt=16776
     sig_peptide     1..23
                     /note="/evidence=ECO:0000269|PubMed:3109913,
                     ECO:0000269|PubMed:6427223; propagated from
                     UniProtKB/Swiss-Prot (P01579.1)"
                     /calculated_mol_wt=2590
     Region          15..152
                     /region_name="IFN-gamma"
                     /note="Interferon gamma; pfam00714"
                     /db_xref="CDD:395581"
     mat_peptide     24..161
                     /product="Interferon gamma. /id=PRO_0000016444"
                     /note="propagated from UniProtKB/Swiss-Prot (P01579.1)"
                     /calculated_mol_wt=16178
     Site            24
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:3109913,
                     ECO:0000269|PubMed:6427223; propagated from
                     UniProtKB/Swiss-Prot (P01579.1)"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:6427223; propagated from
                     UniProtKB/Swiss-Prot (P01579.1)"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, in dimeric form.
                     /evidence=ECO:0000269|PubMed:6427223; propagated from
                     UniProtKB/Swiss-Prot (P01579.1)"
     Region          147..166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01579.1)"
     CDS             1..166
                     /gene="IFNG"
                     /gene_synonym="IFG; IFI; IMD69"
                     /coded_by="NM_000619.3:126..626"
                     /db_xref="CCDS:CCDS8980.1"
                     /db_xref="GeneID:3458"
                     /db_xref="HGNC:HGNC:5438"
                     /db_xref="MIM:147570"
ORIGIN      
        1 mkytsyilaf qlcivlgslg cycqdpyvke aenlkkyfna ghsdvadngt lflgilknwk
       61 eesdrkimqs qivsfyfklf knfkddqsiq ksvetikedm nvkffnsnkk krddfekltn
      121 ysvtdlnvqr kaiheliqvm aelspaaktg krkrsqmlfr grrasq
//
LOCUS       NP_006408                444 aa            linear   PRI 27-APR-2025
DEFINITION  interferon-induced protein 44 [Homo sapiens].
ACCESSION   NP_006408
VERSION     NP_006408.3
DBSOURCE    REFSEQ: accession NM_006417.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Elsayed Ramadan Genena,S., Hamouda,M.A.F., Salama,N.M.,
            Zahran,E.S., Abdel Latif,A.A. and Dawood,A.A.
  TITLE     Interferon-induced protein 44 (IFI44) and interferon regulatory
            factor 4 (IRF4) gene expression in rheumatoid arthritis
  JOURNAL   J Immunoassay Immunochem 45 (5), 432-451 (2024)
   PUBMED   39051937
  REMARK    GeneRIF: Interferon-induced protein 44 (IFI44) and interferon
            regulatory factor 4 (IRF4) gene expression in rheumatoid arthritis.
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Rupa,D., Chuang,H.W., Hu,C.E., Su,W.M., Wu,S.R., Lee,H.S. and
            Yuan,T.C.
  TITLE     ACSL4 upregulates IFI44 and IFI44L expression and promotes the
            proliferation and invasiveness of head and neck squamous cell
            carcinoma cells
  JOURNAL   Cancer Sci 115 (9), 3026-3040 (2024)
   PUBMED   38989827
  REMARK    GeneRIF: ACSL4 upregulates IFI44 and IFI44L expression and promotes
            the proliferation and invasiveness of head and neck squamous cell
            carcinoma cells.
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Zheng,Q., Wang,D., Lin,R., Lv,Q. and Wang,W.
  TITLE     IFI44 is an immune evasion biomarker for SARS-CoV-2 and
            Staphylococcus aureus infection in patients with RA
  JOURNAL   Front Immunol 13, 1013322 (2022)
   PUBMED   36189314
  REMARK    GeneRIF: IFI44 is an immune evasion biomarker for SARS-CoV-2 and
            Staphylococcus aureus infection in patients with RA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Busse,D.C., Habgood-Coote,D., Clare,S., Brandt,C., Bassano,I.,
            Kaforou,M., Herberg,J., Levin,M., Eleouet,J.F., Kellam,P. and
            Tregoning,J.S.
  TITLE     Interferon-Induced Protein 44 and Interferon-Induced Protein
            44-Like Restrict Replication of Respiratory Syncytial Virus
  JOURNAL   J Virol 94 (18), e00297-20 (2020)
   PUBMED   32611756
  REMARK    GeneRIF: Interferon-Induced Protein 44 and Interferon-Induced
            Protein 44-Like Restrict Replication of Respiratory Syncytial
            Virus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Mailaparambil,B., Jochum,J., Forster,J., Heinze,J., Krueger,M. and
            Heinzmann,A.
  TITLE     Polymorphisms of interferons and their receptors in the genetics of
            severe RSV-associated diseases
  JOURNAL   Arch Virol 153 (11), 2133-2137 (2008)
   PUBMED   18953482
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Hallen,L.C., Burki,Y., Ebeling,M., Broger,C., Siegrist,F.,
            Oroszlan-Szovik,K., Bohrmann,B., Certa,U. and Foser,S.
  TITLE     Antiproliferative activity of the human IFN-alpha-inducible protein
            IFI44
  JOURNAL   J Interferon Cytokine Res 27 (8), 675-680 (2007)
   PUBMED   17784819
  REMARK    GeneRIF: Binds and depletes intracellular GTP, abolishing
            extracellular signal-regulated kinase (ERK) signaling and resulting
            finally in cell cycle arrest.
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Hwang,Y., Chen,E.Y., Gu,Z.J., Chuang,W.L., Yu,M.L., Lai,M.Y.,
            Chao,Y.C., Lee,C.M., Wang,J.H., Dai,C.Y., Shian-Jy Bey,M.,
            Liao,Y.T., Chen,P.J. and Chen,D.S.
  TITLE     Genetic predisposition of responsiveness to therapy for chronic
            hepatitis C
  JOURNAL   Pharmacogenomics 7 (5), 697-709 (2006)
   PUBMED   16886895
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Izmailova,E., Bertley,F.M., Huang,Q., Makori,N., Miller,C.J.,
            Young,R.A. and Aldovini,A.
  TITLE     HIV-1 Tat reprograms immature dendritic cells to express
            chemoattractants for activated T cells and macrophages
  JOURNAL   Nat Med 9 (2), 191-197 (2003)
   PUBMED   12539042
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Kitamura,A., Takahashi,K., Okajima,A. and Kitamura,N.
  TITLE     Induction of the human gene for p44, a hepatitis-C-associated
            microtubular aggregate protein, by interferon-alpha/beta
  JOURNAL   Eur J Biochem 224 (3), 877-883 (1994)
   PUBMED   7925411
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC300799.1, DN994910.1, BC022870.1 and CA426666.1.
            
            On Feb 1, 2008 this sequence version replaced NP_006408.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.312280.1,
                                           SRR3476690.188286.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370747.9/ ENSP00000359783.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..444
                     /product="interferon-induced protein 44"
                     /note="interferon-induced, hepatitis C-associated
                     microtubular aggregate protein (44kD);
                     microtubule-associated protein 44; TBC/LysM-associated
                     domain containing 5"
                     /calculated_mol_wt=50360
     Region          26..>70
                     /region_name="TLD"
                     /note="cl02144"
                     /db_xref="CDD:445683"
     CDS             1..444
                     /gene="IFI44"
                     /gene_synonym="MTAP44; p44; TLDC5"
                     /coded_by="NM_006417.5:86..1420"
                     /db_xref="CCDS:CCDS688.1"
                     /db_xref="GeneID:10561"
                     /db_xref="HGNC:HGNC:16938"
                     /db_xref="MIM:610468"
ORIGIN      
        1 mavttrltwl hekilqnhfg gkrlsllykg svhgfrngvl ldrccnqgpt ltviysedhi
       61 igayaeesyq egkyasiilf alqdtkisew klglctpetl fccdvtkyns ptnfqidgrn
      121 rkvimdlktm enlglaqnct isiqdyevfr cedslderki kgvielrksl lsalrtyepy
      181 gslvqqiril llgpigagks sffnsvrsvf qghvthqalv gtnttgisek yrtysirdgk
      241 dgkylpfilc dslglsekeg glcrddifyi lngnirdryq fnpmesikln hhdyidspsl
      301 kdrihcvafv fdassiqyfs sqmivkikri rrelvnagvv hvallthvds mdlitkgdli
      361 eiercepvrs kleevqrklg falsdisvvs nysseweldp vkdvlilsal rrmlwaaddf
      421 ledlpfeqig nlreeiinca qgkk
//
LOCUS       NP_690047                140 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 18 isoform 1 [Homo sapiens].
ACCESSION   NP_690047
VERSION     NP_690047.2
DBSOURCE    REFSEQ: accession NM_152834.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Chermon,D. and Birk,R.
  TITLE     Drinking Habits and Physical Activity Interact and Attenuate
            Obesity Predisposition of TMEM18 Polymorphisms Carriers
  JOURNAL   Nutrients 15 (2), 266 (2023)
   PUBMED   36678137
  REMARK    GeneRIF: Drinking Habits and Physical Activity Interact and
            Attenuate Obesity Predisposition of TMEM18 Polymorphisms Carriers.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Landgraf,K., Kloting,N., Gericke,M., Maixner,N., Guiu-Jurado,E.,
            Scholz,M., Witte,A.V., Beyer,F., Schwartze,J.T., Lacher,M.,
            Villringer,A., Kovacs,P., Rudich,A., Bluher,M., Kiess,W. and
            Korner,A.
  TITLE     The Obesity-Susceptibility Gene TMEM18 Promotes Adipogenesis
            through Activation of PPARG
  JOURNAL   Cell Rep 33 (3), 108295 (2020)
   PUBMED   33086065
  REMARK    GeneRIF: The Obesity-Susceptibility Gene TMEM18 Promotes
            Adipogenesis through Activation of PPARG.
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Rana,S. and Sultana,A.
  TITLE     Association of the Variant rs7561317 Downstream of the TMEM18 Gene
            with Overweight/Obesity and Related Anthropometric Traits in a
            Sample of Pakistani Population
  JOURNAL   Biochem Genet 58 (2), 257-278 (2020)
   PUBMED   31628562
  REMARK    GeneRIF: Association of the Variant rs7561317 Downstream of the
            TMEM18 Gene with Overweight/Obesity and Related Anthropometric
            Traits in a Sample of Pakistani Population.
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Kang,J., Guan,R.C., Zhao,Y. and Chen,Y.
  TITLE     Obesity-related loci in TMEM18, CDKAL1 and FAIM2 are associated
            with obesity and type 2 diabetes in Chinese Han patients
  JOURNAL   BMC Med Genet 21 (1), 65 (2020)
   PUBMED   32228543
  REMARK    GeneRIF: Loci near TMEM18 (rs6548238), CDKAL1 (rs7754840), and
            FAIM2 (rs7138803) may be associated with obesity-related
            indicators, and loci near TMEM18 (rs6548238) and FAIM2 (rs7138803)
            may increase susceptibility of concurrent type 2 diabetes
            associated with obesity.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Renstrom,F., Payne,F., Nordstrom,A., Brito,E.C., Rolandsson,O.,
            Hallmans,G., Barroso,I., Nordstrom,P. and Franks,P.W.
  CONSRTM   GIANT Consortium
  TITLE     Replication and extension of genome-wide association study results
            for obesity in 4923 adults from northern Sweden
  JOURNAL   Hum Mol Genet 18 (8), 1489-1496 (2009)
   PUBMED   19164386
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Willer,C.J., Speliotes,E.K., Loos,R.J., Li,S., Lindgren,C.M.,
            Heid,I.M., Berndt,S.I., Elliott,A.L., Jackson,A.U., Lamina,C.,
            Lettre,G., Lim,N., Lyon,H.N., McCarroll,S.A., Papadakis,K., Qi,L.,
            Randall,J.C., Roccasecca,R.M., Sanna,S., Scheet,P., Weedon,M.N.,
            Wheeler,E., Zhao,J.H., Jacobs,L.C., Prokopenko,I., Soranzo,N.,
            Tanaka,T., Timpson,N.J., Almgren,P., Bennett,A., Bergman,R.N.,
            Bingham,S.A., Bonnycastle,L.L., Brown,M., Burtt,N.P., Chines,P.,
            Coin,L., Collins,F.S., Connell,J.M., Cooper,C., Smith,G.D.,
            Dennison,E.M., Deodhar,P., Elliott,P., Erdos,M.R., Estrada,K.,
            Evans,D.M., Gianniny,L., Gieger,C., Gillson,C.J., Guiducci,C.,
            Hackett,R., Hadley,D., Hall,A.S., Havulinna,A.S., Hebebrand,J.,
            Hofman,A., Isomaa,B., Jacobs,K.B., Johnson,T., Jousilahti,P.,
            Jovanovic,Z., Khaw,K.T., Kraft,P., Kuokkanen,M., Kuusisto,J.,
            Laitinen,J., Lakatta,E.G., Luan,J., Luben,R.N., Mangino,M.,
            McArdle,W.L., Meitinger,T., Mulas,A., Munroe,P.B., Narisu,N.,
            Ness,A.R., Northstone,K., O'Rahilly,S., Purmann,C., Rees,M.G.,
            Ridderstrale,M., Ring,S.M., Rivadeneira,F., Ruokonen,A.,
            Sandhu,M.S., Saramies,J., Scott,L.J., Scuteri,A., Silander,K.,
            Sims,M.A., Song,K., Stephens,J., Stevens,S., Stringham,H.M.,
            Tung,Y.C., Valle,T.T., Van Duijn,C.M., Vimaleswaran,K.S.,
            Vollenweider,P., Waeber,G., Wallace,C., Watanabe,R.M.,
            Waterworth,D.M., Watkins,N., Witteman,J.C., Zeggini,E., Zhai,G.,
            Zillikens,M.C., Altshuler,D., Caulfield,M.J., Chanock,S.J.,
            Farooqi,I.S., Ferrucci,L., Guralnik,J.M., Hattersley,A.T., Hu,F.B.,
            Jarvelin,M.R., Laakso,M., Mooser,V., Ong,K.K., Ouwehand,W.H.,
            Salomaa,V., Samani,N.J., Spector,T.D., Tuomi,T., Tuomilehto,J.,
            Uda,M., Uitterlinden,A.G., Wareham,N.J., Deloukas,P.,
            Frayling,T.M., Groop,L.C., Hayes,R.B., Hunter,D.J., Mohlke,K.L.,
            Peltonen,L., Schlessinger,D., Strachan,D.P., Wichmann,H.E.,
            McCarthy,M.I., Boehnke,M., Barroso,I., Abecasis,G.R. and
            Hirschhorn,J.N.
  CONSRTM   Wellcome Trust Case Control Consortium; Genetic Investigation of
            ANthropometric Traits Consortium
  TITLE     Six new loci associated with body mass index highlight a neuronal
            influence on body weight regulation
  JOURNAL   Nat Genet 41 (1), 25-34 (2009)
   PUBMED   19079261
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Thorleifsson,G., Walters,G.B., Gudbjartsson,D.F.,
            Steinthorsdottir,V., Sulem,P., Helgadottir,A., Styrkarsdottir,U.,
            Gretarsdottir,S., Thorlacius,S., Jonsdottir,I., Jonsdottir,T.,
            Olafsdottir,E.J., Olafsdottir,G.H., Jonsson,T., Jonsson,F.,
            Borch-Johnsen,K., Hansen,T., Andersen,G., Jorgensen,T.,
            Lauritzen,T., Aben,K.K., Verbeek,A.L., Roeleveld,N., Kampman,E.,
            Yanek,L.R., Becker,L.C., Tryggvadottir,L., Rafnar,T., Becker,D.M.,
            Gulcher,J., Kiemeney,L.A., Pedersen,O., Kong,A.,
            Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Genome-wide association yields new sequence variants at seven loci
            that associate with measures of obesity
  JOURNAL   Nat Genet 41 (1), 18-24 (2009)
   PUBMED   19079260
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Jurvansuu,J., Zhao,Y., Leung,D.S., Boulaire,J., Yu,Y.H., Ahmed,S.
            and Wang,S.
  TITLE     Transmembrane protein 18 enhances the tropism of neural stem cells
            for glioma cells
  JOURNAL   Cancer Res 68 (12), 4614-4622 (2008)
   PUBMED   18559506
  REMARK    GeneRIF: Overexpression of TMEM18 is associated with glioma
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL137269.1, CK826537.1, DN601654.1, FN163096.1, AC092159.4 and
            AI272939.1.
            
            On Jan 2, 2004 this sequence version replaced NP_690047.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM762047.1, SRR1803612.15009.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281017.8/ ENSP00000281017.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.3"
     Protein         1..140
                     /product="transmembrane protein 18 isoform 1"
                     /calculated_mol_wt=16134
     Region          16..127
                     /region_name="TMEM18"
                     /note="Transmembrane protein 18; pfam14770"
                     /db_xref="CDD:405460"
     Site            26..46
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B42.2)"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B42.2)"
     Site            92..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B42.2)"
     Region          113..140
                     /region_name="DNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B42.2)"
     Region          130..138
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B42.2)"
     CDS             1..140
                     /gene="TMEM18"
                     /gene_synonym="lncND"
                     /coded_by="NM_152834.4:62..484"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33141.1"
                     /db_xref="GeneID:129787"
                     /db_xref="HGNC:HGNC:25257"
                     /db_xref="MIM:613220"
ORIGIN      
        1 mpsafsvssf pvsipavltq tdwtepwlmg latfhalcvl ltclssrsyr lqighflclv
       61 ilvycaeyin eaaamnwrlf skyqyfdsrg mfisivfsap llvnamiivv mwvwktlnvm
      121 tdlknaqerr kekkrrrked
//
LOCUS       NP_666300                283 aa            linear   ROD 27-APR-2025
DEFINITION  BTB/POZ domain-containing protein KCTD15 [Mus musculus].
ACCESSION   NP_666300
VERSION     NP_666300.1
DBSOURCE    REFSEQ: accession NM_146188.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Raymundo,J.R., Zhang,H., Smaldone,G., Zhu,W., Daly,K.E.,
            Glennon,B.J., Pecoraro,G., Salvatore,M., Devine,W.A., Lo,C.W.,
            Vitagliano,L. and Marneros,A.G.
  TITLE     KCTD1/KCTD15 complexes control ectodermal and neural crest cell
            functions, and their impairment causes aplasia cutis
  JOURNAL   J Clin Invest 134 (4), e174138 (2023)
   PUBMED   38113115
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Smaldone,G., Pirone,L., Capolupo,A., Vitagliano,L., Monti,M.C., Di
            Gaetano,S. and Pedone,E.
  TITLE     The essential player in adipogenesis GRP78 is a novel KCTD15
            interactor
  JOURNAL   Int J Biol Macromol 115, 469-475 (2018)
   PUBMED   29665387
  REMARK    GeneRIF: the physiological role played by the complex KCTD15-GRP78
            in the adipogenesis
REFERENCE   4  (residues 1 to 283)
  AUTHORS   West,D.B., Engelhard,E.K., Adkisson,M., Nava,A.J., Kirov,J.V.,
            Cipollone,A., Willis,B., Rapp,J., de Jong,P.J. and Lloyd,K.C.
  TITLE     Transcriptome Analysis of Targeted Mouse Mutations Reveals the
            Topography of Local Changes in Gene Expression
  JOURNAL   PLoS Genet 12 (2), e1005691 (2016)
   PUBMED   26839965
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Williams,M.J., Goergen,P., Rajendran,J., Zheleznyakova,G.,
            Hagglund,M.G., Perland,E., Bagchi,S., Kalogeropoulou,A., Khan,Z.,
            Fredriksson,R. and Schioth,H.B.
  TITLE     Obesity-linked homologues TfAP-2 and Twz establish meal frequency
            in Drosophila melanogaster
  JOURNAL   PLoS Genet 10 (9), e1004499 (2014)
   PUBMED   25187989
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Zarelli,V.E. and Dawid,I.B.
  TITLE     The BTB-containing protein Kctd15 is SUMOylated in vivo
  JOURNAL   PLoS One 8 (9), e75016 (2013)
   PUBMED   24086424
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Bailey,P.J., Klos,J.M., Andersson,E., Karlen,M., Kallstrom,M.,
            Ponjavic,J., Muhr,J., Lenhard,B., Sandelin,A. and Ericson,J.
  TITLE     A global genomic transcriptional code associated with CNS-expressed
            genes
  JOURNAL   Exp Cell Res 312 (16), 3108-3119 (2006)
   PUBMED   16919269
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX649462.9, BC031749.1 and AW124009.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC031749.1, SRR1660813.81623.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134, SAMN01164138
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 20.41 cM"
     Protein         1..283
                     /product="BTB/POZ domain-containing protein KCTD15"
                     /note="potassium channel tetramerization domain-containing
                     protein 15"
                     /calculated_mol_wt=31755
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K0E1.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96SI1; propagated from
                     UniProtKB/Swiss-Prot (Q8K0E1.1)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8K0E1.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8K0E1.1)"
     Region          55..153
                     /region_name="BTB_POZ_KCTD15"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     channel tetramerization domain-containing protein 15
                     (KCTD15); cd18388"
                     /db_xref="CDD:349696"
     Site            order(55,57,59,61,63..64,66..70,73,93,95,98,100,102,
                     104..106,108,111,115,118..119,121,123,125..127,129..130,
                     133,136,139)
                     /site_type="other"
                     /note="putative pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349696"
     CDS             1..283
                     /gene="Kctd15"
                     /coded_by="NM_146188.2:377..1228"
                     /db_xref="CCDS:CCDS21141.1"
                     /db_xref="GeneID:233107"
                     /db_xref="MGI:MGI:2385276"
ORIGIN      
        1 mphrkerpsg sslnahgssg taeggnmsrl sltrspvspl aaqgiplpaq ltkanapvhi
       61 dvgghmytss latltkypds risrlfngte pivldslkqh yfidrdgeif ryilsflrts
      121 klllpddfkd fnllyeeary yqlqpmvrel erwqqdqeqr rrsracdclv vrvtpdlger
      181 ialsgekali eevfpetgdv mcnsvnagwn qdpthvirfp lngycrlnsv qvlerlfqrg
      241 fsvaascggg vdssqfseyv lcreerrpqp tptavrikqe pld
//
LOCUS       NP_001350063             226 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF167 isoform 2 [Mus musculus].
ACCESSION   NP_001350063 XP_006534257
VERSION     NP_001350063.1
DBSOURCE    REFSEQ: accession NM_001363134.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Lussier,M.P., Herring,B.E., Nasu-Nishimura,Y., Neutzner,A.,
            Karbowski,M., Youle,R.J., Nicoll,R.A. and Roche,K.W.
  TITLE     Ubiquitin ligase RNF167 regulates AMPA receptor-mediated synaptic
            transmission
  JOURNAL   Proc Natl Acad Sci U S A 109 (47), 19426-19431 (2012)
   PUBMED   23129617
  REMARK    GeneRIF: RNF167 is a selective regulator of AMPAR-mediated
            neurotransmission.
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Taher,L., Collette,N.M., Murugesh,D., Maxwell,E., Ovcharenko,I. and
            Loots,G.G.
  TITLE     Global gene expression analysis of murine limb development
  JOURNAL   PLoS One 6 (12), e28358 (2011)
   PUBMED   22174793
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL596117.19 and AI840160.1.
            
            On May 9, 2018 this sequence version replaced XP_006534257.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189682.83740.1,
                                           SRR7652917.118488.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 43.21 cM"
     Protein         1..226
                     /product="E3 ubiquitin-protein ligase RNF167 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF167; novel PA domain
                     and C3HC4 type zinc finger (RING finger) containing
                     protein; RING-type E3 ubiquitin transferase RNF167"
                     /calculated_mol_wt=25230
     Region          <1..49
                     /region_name="PA"
                     /note="Protease-associated (PA) domain. The PA domain is
                     an insert domain in a diverse fraction of proteases. The
                     significance of the PA domain to many of the proteins in
                     which it is inserted is undetermined. It may be a
                     protein-protein interaction domain. At...; cl28883"
                     /db_xref="CDD:333703"
     Region          107..152
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(109,112,127,129,132,135,147,150)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438111"
     CDS             1..226
                     /gene="Rnf167"
                     /gene_synonym="0610010G05Rik; 5730408C10Rik"
                     /coded_by="NM_001363134.1:946..1626"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:70510"
                     /db_xref="MGI:MGI:1917760"
ORIGIN      
        1 mvwnseeiqq qiwipsvfig ersaeylral fvyekgarvl lvpdnsfplg yylipftgiv
       61 gllvlamgtv livrciqhrk rlqrnrltke qlkqipthdy qkgdeydvca icldeyedgd
      121 klrvlpcaha yhsrcvdpwl tqtrktcpic kqpvhrgpgd eeqeeetqeq eegdegeprd
      181 qpasewtpll gssptlptsf gslapaplvf pgpstdpspp ssaala
//
LOCUS       NP_004721                437 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic peptide chain release factor subunit 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_004721
VERSION     NP_004721.1
DBSOURCE    REFSEQ: accession NM_004730.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Shuvalov,A., Klishin,A., Biziaev,N., Shuvalova,E. and Alkalaeva,E.
  TITLE     Functional Activity of Isoform 2 of Human eRF1
  JOURNAL   Int J Mol Sci 25 (14), 7997 (2024)
   PUBMED   39063238
  REMARK    GeneRIF: Functional Activity of Isoform 2 of Human eRF1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Oltion,K., Carelli,J.D., Yang,T., See,S.K., Wang,H.Y., Kampmann,M.
            and Taunton,J.
  TITLE     An E3 ligase network engages GCN1 to promote the degradation of
            translation factors on stalled ribosomes
  JOURNAL   Cell 186 (2), 346-362 (2023)
   PUBMED   36638793
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Song,H., Mugnier,P., Das,A.K., Webb,H.M., Evans,D.R., Tuite,M.F.,
            Hemmings,B.A. and Barford,D.
  TITLE     The crystal structure of human eukaryotic release factor
            eRF1--mechanism of stop codon recognition and peptidyl-tRNA
            hydrolysis
  JOURNAL   Cell 100 (3), 311-321 (2000)
   PUBMED   10676813
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Guenet,L., Henry,C., Toutain,B., Dubourg,C., Le Gall,J.Y., David,V.
            and Le Treut,A.
  TITLE     Eukaryotic translation termination factor gene (ETF1/eRF1) maps at
            D5S500 in a commonly deleted region of chromosome 5q31 in malignant
            myeloid diseases
  JOURNAL   Cytogenet Cell Genet 88 (1-2), 82-86 (2000)
   PUBMED   10773672
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Hansen,L.L., Jakobsen,C.G. and Justesen,J.
  TITLE     Assignment of the human translation termination factor 1 (ETF1) to
            5q31.1 and of the proximal marker D5S1995 by radiation hybrid
            mapping
  JOURNAL   Cytogenet Cell Genet 87 (3-4), 256-257 (1999)
   PUBMED   10702684
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Chauvel,B., Dorval,I., Fergelot,P., Pichon,L., Giffon,T.,
            Gicquel,I., Le Gall,J.Y. and David,V.
  TITLE     A human homologue to the yeast omnipotent suppressor 45 maps 100 kb
            centromeric to HLA-A
  JOURNAL   Immunogenetics 41 (6), 380-382 (1995)
   PUBMED   7759135
REFERENCE   8  (residues 1 to 437)
  AUTHORS   Frolova,L., Le Goff,X., Rasmussen,H.H., Cheperegin,S., Drugeon,G.,
            Kress,M., Arman,I., Haenni,A.L., Celis,J.E., Philippe,M. et al.
  TITLE     A highly conserved eukaryotic protein family possessing properties
            of polypeptide chain release factor
  JOURNAL   Nature 372 (6507), 701-703 (1994)
   PUBMED   7990965
REFERENCE   9  (residues 1 to 437)
  AUTHORS   Grenett,H.E., Bounelis,P. and Fuller,G.M.
  TITLE     Identification of a human cDNA with high homology to yeast
            omnipotent suppressor 45
  JOURNAL   Gene 110 (2), 239-243 (1992)
   PUBMED   1537561
REFERENCE   10 (residues 1 to 437)
  AUTHORS   Grenett,H.E., Eipers,P.G., Kidd,V.J., Bounelis,P. and Fuller,G.M.
  TITLE     Chromosomal localization of a human cDNA containing a DIDS binding
            domain and demonstrating high homology to yeast omnipotent
            suppressor 45
  JOURNAL   Somat Cell Mol Genet 18 (1), 97-102 (1992)
   PUBMED   1546371
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB060174.1, AK312510.1,
            U90176.1, AC113403.4 and AW131045.1.
            
            Summary: This gene encodes a class-1 polypeptide chain release
            factor. The encoded protein plays an essential role in directing
            termination of mRNA translation from the termination codons UAA,
            UAG and UGA. This protein is a component of the SURF complex which
            promotes degradation of prematurely terminated mRNAs via the
            mechanism of nonsense-mediated mRNA decay (NMD). Alternate splicing
            results in multiple transcript variants. Pseudogenes of this gene
            are found on chromosomes 6, 7, and X. [provided by RefSeq, Aug
            2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.171475.1,
                                           SRR1660807.125552.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360541.10/ ENSP00000353741.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.2"
     Protein         1..437
                     /product="eukaryotic peptide chain release factor subunit
                     1 isoform 1"
                     /note="polypeptide chain release factor 1; sup45 (yeast
                     omnipotent suppressor 45) homolog-like 1; eukaryotic
                     peptide chain release factor subunit 1; protein Cl1"
                     /calculated_mol_wt=48900
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P62495.3)"
     Region          13..417
                     /region_name="aRF1/eRF1"
                     /note="peptide chain release factor 1, archaeal and
                     eukaryotic forms; TIGR03676"
                     /db_xref="CDD:274719"
     Region          61..64
                     /region_name="NIKS motif, plays an important role in
                     translational termination.
                     /evidence=ECO:0000305|PubMed:24486019"
                     /note="propagated from UniProtKB/Swiss-Prot (P62495.3)"
     Site            185
                     /site_type="methylation"
                     /note="N5-methylglutamine.
                     /evidence=ECO:0000269|PubMed:18539146,
                     ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:26797129;
                     propagated from UniProtKB/Swiss-Prot (P62495.3)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62495.3)"
     CDS             1..437
                     /gene="ETF1"
                     /gene_synonym="D5S1995; ERF; ERF1; RF1; SUP45L1; TB3-1"
                     /coded_by="NM_004730.4:159..1472"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4207.1"
                     /db_xref="GeneID:2107"
                     /db_xref="HGNC:HGNC:3477"
                     /db_xref="MIM:600285"
ORIGIN      
        1 maddpsaadr nveiwkikkl iksleaargn gtsmisliip pkdqisrvak mladefgtas
       61 niksrvnrls vlgaitsvqq rlklynkvpp nglvvycgti vteegkekkv nidfepfkpi
      121 ntslylcdnk fhtealtall sddskfgfiv idgsgalfgt lqgntrevlh kftvdlpkkh
      181 grggqsalrf arlrmekrhn yvrkvaetav qlfisgdkvn vaglvlagsa dfktelsqsd
      241 mfdqrlqskv lklvdisygg engfnqaiel stevlsnvkf iqekkligry fdeisqdtgk
      301 ycfgvedtlk alemgaveil ivyenldimr yvlhcqgtee ekilyltpeq ekdkshftdk
      361 etgqehelie smpllewfan nykkfgatle ivtdksqegs qfvkgfggig gilryrvdfq
      421 gmeyqggdde ffdlddy
//
LOCUS       NP_003712                260 aa            linear   PRI 27-APR-2025
DEFINITION  DNA-binding protein RFXANK isoform a [Homo sapiens].
ACCESSION   NP_003712
VERSION     NP_003712.1
DBSOURCE    REFSEQ: accession NM_003721.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Mousavi Khorshidi,M.S., Seeleuthner,Y., Chavoshzadeh,Z., Behfar,M.,
            Hamidieh,A.A., Alimadadi,H., Sherkat,R., Momen,T., Behniafard,N.,
            Eskandarzadeh,S., Mansouri,M., Behnam,M., Mahdavi,M., Heydarazad
            Zadeh,M., Shokri,M., Alizadeh,F., Movahedi,M., Momenilandi,M.,
            Keramatipour,M., Casanova,J.L., Cobat,A., Abel,L., Shahrooei,M. and
            Parvaneh,N.
  TITLE     Clinical, Immunological, and Genetic Findings in Iranian Patients
            with MHC-II Deficiency: Confirmation of c.162delG RFXANK Founder
            Mutation in the Iranian Population
  JOURNAL   J Clin Immunol 43 (8), 1941-1952 (2023)
   PUBMED   37584719
  REMARK    GeneRIF: Clinical, Immunological, and Genetic Findings in Iranian
            Patients with MHC-II Deficiency: Confirmation of c.162delG RFXANK
            Founder Mutation in the Iranian Population.
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Abolnezhadian,F., Saeedi-Boroujeni,A. and Iranparast,S.
  TITLE     MHC Class II Deficiency with Normal CD4+ T Cell Counts: A Case
            Report
  JOURNAL   Iran J Allergy Asthma Immunol 17 (6), 594-600 (2018)
   PUBMED   30644704
  REMARK    GeneRIF: this study reports an 8 month-old girl with MHC class II
            deficiency with a novel homozygous mutation in RFXANK gene and
            normal CD4+ T cell counts, diagnosed by whole exome sequencing and
            negative HLA-DR proteins on peripheral blood mononuclear cell in
            flow cytometry
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Forsberg,J., Li,X., Akpinar,B., Salvatori,R., Ott,M.,
            Zhivotovsky,B. and Olsson,M.
  TITLE     A caspase-2-RFXANK interaction and its implication for MHC class II
            expression
  JOURNAL   Cell Death Dis 9 (2), 80 (2018)
   PUBMED   29362422
  REMARK    GeneRIF: these data identify a novel caspase-2-interacting factor,
            RFXANK, and indicate a potential non-apoptotic role for the enzyme
            in the control of MHC class II gene regulation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Nagarajan,U.M., Peijnenburg,A., Gobin,S.J., Boss,J.M. and van den
            elsen,P.J.
  TITLE     Novel mutations within the RFX-B gene and partial rescue of MHC and
            related genes through exogenous class II transactivator in
            RFX-B-deficient cells
  JOURNAL   J Immunol 164 (7), 3666-3674 (2000)
   PUBMED   10725724
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Wiszniewski,W., Fondaneche,M.C., Lambert,N., Masternak,K.,
            Picard,C., Notarangelo,L., Schwartz,K., Bal,J., Reith,W.,
            Alcaide,C., de Saint Basile,G., Fischer,A. and
            Lisowska-Grospierre,B.
  TITLE     Founder effect for a 26-bp deletion in the RFXANK gene in North
            African major histocompatibility complex class II-deficient
            patients belonging to complementation group B
  JOURNAL   Immunogenetics 51 (4-5), 261-267 (2000)
   PUBMED   10803838
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Lin,J.H., Makris,A., McMahon,C., Bear,S.E., Patriotis,C.,
            Prasad,V.R., Brent,R., Golemis,E.A. and Tsichlis,P.N.
  TITLE     The ankyrin repeat-containing adaptor protein Tvl-1 is a novel
            substrate and regulator of Raf-1
  JOURNAL   J Biol Chem 274 (21), 14706-14715 (1999)
   PUBMED   10329666
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Nagarajan,U.M., Louis-Plence,P., DeSandro,A., Nilsen,R., Bushey,A.
            and Boss,J.M.
  TITLE     RFX-B is the gene responsible for the most common cause of the bare
            lymphocyte syndrome, an MHC class II immunodeficiency
  JOURNAL   Immunity 10 (2), 153-162 (1999)
   PUBMED   10072068
  REMARK    Erratum:[Immunity 1999 Mar;10(3):399]
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Masternak,K., Barras,E., Zufferey,M., Conrad,B., Corthals,G.,
            Aebersold,R., Sanchez,J.C., Hochstrasser,D.F., Mach,B. and Reith,W.
  TITLE     A gene encoding a novel RFX-associated transactivator is mutated in
            the majority of MHC class II deficiency patients
  JOURNAL   Nat Genet 20 (3), 273-277 (1998)
   PUBMED   9806546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM682278.1, AF094760.1 and
            AW411190.1.
            
            Summary: Major histocompatibility (MHC) class II molecules are
            transmembrane proteins that have a central role in development and
            control of the immune system. The protein encoded by this gene,
            along with regulatory factor X-associated protein and regulatory
            factor-5, forms a complex that binds to the X box motif of certain
            MHC class II gene promoters and activates their transcription. Once
            bound to the promoter, this complex associates with the
            non-DNA-binding factor MHC class II transactivator, which controls
            the cell type specificity and inducibility of MHC class II gene
            expression. This protein contains ankyrin repeats involved in
            protein-protein interactions. Mutations in this gene have been
            linked to bare lymphocyte syndrome type II, complementation group
            B. Multiple alternatively spliced transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.928654.1, AF094760.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303088.9/ ENSP00000305071.2
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..260
                     /product="DNA-binding protein RFXANK isoform a"
                     /note="ankyrin repeat-containing regulatory factor
                     X-associated protein; regulatory factor X subunit B;
                     RFX-Bdelta4; DNA-binding protein RFXANK; ankyrin repeat
                     family A protein 1"
                     /calculated_mol_wt=27971
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          89..118
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          <94..249
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          94..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(123,125,129..130,133..135,137..138,142,145,154,156,
                     158,162..163,166..168,170..171,175,178,187,189,191,
                     195..196,199..201,203..204,208,211)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          123..154
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          123..152
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          156..187
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          156..185
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          189..218
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          189..217
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          222..251
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     CDS             1..260
                     /gene="RFXANK"
                     /gene_synonym="ANKRA1; BLS; F14150_1; MHC2D2; RFX-B"
                     /coded_by="NM_003721.4:447..1229"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12395.1"
                     /db_xref="GeneID:8625"
                     /db_xref="HGNC:HGNC:9987"
                     /db_xref="MIM:603200"
ORIGIN      
        1 meltqpaedl iqtqqtpase lgdpedpgee aadgsdtvvl slfpctpepv npepdasvss
       61 pqagsslkhs ttltnrqrgn evsalpatld slsihqlaaq geldqlkehl rkgdnlvnkp
      121 dergftpliw asafgeietv rfllewgadp hilakeresa lslastggyt divglllerd
      181 vdiniydwng gtpllyavrg nhvkcveall argadlttea dsgytpmdla valgyrkvqq
      241 vienhilklf qsnlvpadpe
//
LOCUS       NP_065892                889 aa            linear   PRI 27-APR-2025
DEFINITION  oxysterol-binding protein-related protein 8 isoform a [Homo
            sapiens].
ACCESSION   NP_065892
VERSION     NP_065892.1
DBSOURCE    REFSEQ: accession NM_020841.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Li,J., Cui,J., Li,Z., Fu,X., Li,J., Li,H., Wang,S. and Zhang,M.
  TITLE     ORP8 induces apoptosis by releasing cytochrome c from mitochondria
            in non-small cell lung cancer
  JOURNAL   Oncol Rep 43 (5), 1516-1524 (2020)
   PUBMED   32323800
  REMARK    GeneRIF: ORP8 induces apoptosis by releasing cytochrome c from
            mitochondria in nonsmall cell lung cancer.
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Pulli,I., Lassila,T., Pan,G., Yan,D., Olkkonen,V.M. and
            Tornquist,K.
  TITLE     Oxysterol-binding protein related-proteins (ORPs) 5 and 8 regulate
            calcium signaling at specific cell compartments
  JOURNAL   Cell Calcium 72, 62-69 (2018)
   PUBMED   29748134
  REMARK    GeneRIF: ORP5/8 regulate Ca(2+) signaling at specific membrane
            contact sites foci.
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Sohn,M., Korzeniowski,M., Zewe,J.P., Wills,R.C., Hammond,G.R.V.,
            Humpolickova,J., Vrzal,L., Chalupska,D., Veverka,V., Fairn,G.D.,
            Boura,E. and Balla,T.
  TITLE     PI(4,5)P2 controls plasma membrane PI4P and PS levels via ORP5/8
            recruitment to ER-PM contact sites
  JOURNAL   J Cell Biol 217 (5), 1797-1813 (2018)
   PUBMED   29472386
  REMARK    GeneRIF: ORP5/8 recruitment to the plasma membrane occurs through
            interactions with the N-terminal Pleckstrin homology domains and
            adjacent basic residues of ORP5/8 with both phosphatidylinositol
            4-phosphate and Phosphatidylinositol 4,5-bisphosphate.
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Lee,M. and Fairn,G.D.
  TITLE     Both the PH domain and N-terminal region of oxysterol-binding
            protein related protein 8S are required for localization to PM-ER
            contact sites
  JOURNAL   Biochem Biophys Res Commun 496 (4), 1088-1094 (2018)
   PUBMED   29409900
  REMARK    GeneRIF: Examination of a series of deletion constructs
            demonstrated that both the N-terminal polybasic region and the PH
            domain are required for proper targeting of the short splice
            variant ORP8S to the PM-ER contact site in Chinese hamster ovary
            cells.
REFERENCE   5  (residues 1 to 889)
  AUTHORS   Ghai,R., Du,X., Wang,H., Dong,J., Ferguson,C., Brown,A.J.,
            Parton,R.G., Wu,J.W. and Yang,H.
  TITLE     ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate
            (PtdIns(4,5)P 2) and regulate its level at the plasma membrane
  JOURNAL   Nat Commun 8 (1), 757 (2017)
   PUBMED   28970484
  REMARK    GeneRIF: ORP5/8 are endoplasmic reticulum (ER) membrane proteins
            implicated in lipid trafficking that localize to ER-plasma membrane
            (PM) contacts and maintain membrane homeostasis. Here the authors
            show that PtdIns(4,5)P 2 plays a critical role in the targeting and
            function of ORP5/8 at the PM.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 889)
  AUTHORS   Yan,D., Mayranpaa,M.I., Wong,J., Perttila,J., Lehto,M.,
            Jauhiainen,M., Kovanen,P.T., Ehnholm,C., Brown,A.J. and
            Olkkonen,V.M.
  TITLE     OSBP-related protein 8 (ORP8) suppresses ABCA1 expression and
            cholesterol efflux from macrophages
  JOURNAL   J Biol Chem 283 (1), 332-340 (2008)
   PUBMED   17991739
  REMARK    GeneRIF: Data identify ORP8 as a negative regulator of ABCA1
            expression and macrophage cholesterol efflux. ORP8 may, thus,
            modulate the development of atherosclerosis.
REFERENCE   7  (residues 1 to 889)
  AUTHORS   Suchanek,M., Hynynen,R., Wohlfahrt,G., Lehto,M., Johansson,M.,
            Saarinen,H., Radzikowska,A., Thiele,C. and Olkkonen,V.M.
  TITLE     The mammalian oxysterol-binding protein-related proteins (ORPs)
            bind 25-hydroxycholesterol in an evolutionarily conserved pocket
  JOURNAL   Biochem J 405 (3), 473-480 (2007)
   PUBMED   17428193
REFERENCE   8  (residues 1 to 889)
  AUTHORS   Ma,J., Dempsey,A.A., Stamatiou,D., Marshall,K.W. and Liew,C.C.
  TITLE     Identifying leukocyte gene expression patterns associated with
            plasma lipid levels in human subjects
  JOURNAL   Atherosclerosis 191 (1), 63-72 (2007)
   PUBMED   16806233
REFERENCE   9  (residues 1 to 889)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 889)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF392452.1 and AL832876.1.
            
            Summary: This gene encodes a member of a family of proteins
            containing an N-terminal pleckstrin homology domain and a highly
            conserved C-terminal oxysterol-binding protein-like sterol-binding
            domain. It binds mutliple lipid-containing molecules, including
            phosphatidylserine, phosphatidylinositol 4-phosphate (PI4P) and
            oxysterol, and promotes their exchange between the endoplasmic
            reticulum and the plasma membrane. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB040884.3, AF392452.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261183.8/ ENSP00000261183.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..889
                     /product="oxysterol-binding protein-related protein 8
                     isoform a"
                     /note="oxysterol-binding protein-related protein 8;
                     OSBP-related protein 8"
                     /calculated_mol_wt=101065
     Region          1..129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Region          142..271
                     /region_name="PH_OPR5_ORP8"
                     /note="Human Oxysterol binding protein related proteins 5
                     and 8 Pleckstrin homology (PH) domain; cd13286"
                     /db_xref="CDD:270103"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Region          322..399
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Region          407..753
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     Region          771..823
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            807
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BZF1.3)"
     Site            871..888
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZF1.3)"
     CDS             1..889
                     /gene="OSBPL8"
                     /gene_synonym="MST120; MSTP120; ORP8; OSBP10"
                     /coded_by="NM_020841.5:443..3112"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31862.1"
                     /db_xref="GeneID:114882"
                     /db_xref="HGNC:HGNC:16396"
                     /db_xref="MIM:606736"
ORIGIN      
        1 meggladgep drtsllgdsk dvlgpstvva nsdesqlltp gkmsqrqgke ayptptkdlh
       61 qpslspasph sqgfergked isqnkdessl smsksksesk lyngsekdss tsskltkkes
      121 lkvqkknyre ekkratkell stitdpsviv madwlkirgt lkswtklwcv lkpgvlliyk
      181 tqkngqwvgt vllnaceiie rpskkdgfcf klfhpleqsi wavkgpkgea vgsitqplps
      241 syliiratse sdgrcwmdal elalkcssll krtmiregke hdlsvssdst hvtfygllra
      301 nnlhsgdnfq lndseierqh fkdqdmysdk sdkendqehd esdnevmgks eesdtdtser
      361 qddsyiepep veplkettyt eqsheelgea geasqtetvs eenksliwtl lkqvrpgmdl
      421 skvvlptfil eprsfldkls dyyyhadfls eaaleenpyf rlkkvvkwyl sgfykkpkgl
      481 kkpynpilge tfrclwihpr tnsktfyiae qvshhppisa fyvsnrkdgf clsgsilaks
      541 kfygnslsai legearltfl nrgedyvmtm pyahckgily gtmtlelggt vnitcqktgy
      601 sailefklkp flgssdcvnq isgklklgke vlatleghwd sevfitdkkt dnsevfwnpt
      661 pdikqwrlir htvkfeeqgd feseklwqrv trainakdqt eatqekyvle eaqrqaardr
      721 ktkneewsck lfeldpltge whykfadtrp wdplndmiqf ekdgviqtkv khrtpmvsvp
      781 kmkhkptrqq kkvakgyssp epdiqdssgs eaqsvkpstr rkkgielgdi qssiesikqt
      841 qeeikrnima lrnhlvsstp atdyflqqkd yfiifllill qviinfmfk
//
LOCUS       NP_620688               1095 aa            linear   PRI 27-APR-2025
DEFINITION  A disintegrin and metalloproteinase with thrombospondin motifs 17
            preproprotein [Homo sapiens].
ACCESSION   NP_620688
VERSION     NP_620688.2
DBSOURCE    REFSEQ: accession NM_139057.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Guo,D., Liu,L., Yang,F., Young,C.A., Zheng,D. and Jin,G.
  TITLE     Characteristics and genotype-phenotype correlations in ADAMTS17
            mutation-related Weill-Marchesani syndrome
  JOURNAL   Exp Eye Res 234, 109606 (2023)
   PUBMED   37506754
  REMARK    GeneRIF: Characteristics and genotype-phenotype correlations in
            ADAMTS17 mutation-related Weill-Marchesani syndrome.
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Han,P., Jiang,F. and Zhang,L.
  TITLE     The role of ADAMTS6 and ADAMTS17 polymorphisms in susceptibility to
            lumbar disc herniation in Chinese Han population
  JOURNAL   Eur Spine J 32 (4), 1106-1114 (2023)
   PUBMED   36810712
  REMARK    GeneRIF: The role of ADAMTS6 and ADAMTS17 polymorphisms in
            susceptibility to lumbar disc herniation in Chinese Han population.
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Taniguchi,Y., Akune,T., Nishida,N., Omori,G., Ha,K., Ueno,K.,
            Saito,T., Oichi,T., Koike,A., Mabuchi,A., Oka,H., Muraki,S.,
            Oshima,Y., Kawaguchi,H., Nakamura,K., Tokunaga,K., Tanaka,S. and
            Yoshimura,N.
  TITLE     A common variant rs2054564 in ADAMST17 is associated with
            susceptibility to lumbar spondylosis
  JOURNAL   Sci Rep 13 (1), 4900 (2023)
   PUBMED   36966180
  REMARK    GeneRIF: A common variant rs2054564 in ADAMST17 is associated with
            susceptibility to lumbar spondylosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1095)
  AUTHORS   Evans,D.R., Green,J.S., Fahiminiya,S., Majewski,J., Fernandez,B.A.,
            Deardorff,M.A., Johnson,G.J., Whelan,J.H., Hubmacher,D., Apte,S.S.
            and Woods,M.O.
  CONSRTM   Care4Rare Canada Consortium
  TITLE     A novel pathogenic missense ADAMTS17 variant that impairs secretion
            causes Weill-Marchesani Syndrome with variably dysmorphic hand
            features
  JOURNAL   Sci Rep 10 (1), 10827 (2020)
   PUBMED   32616716
  REMARK    GeneRIF: A novel pathogenic missense ADAMTS17 variant that impairs
            secretion causes Weill-Marchesani Syndrome with variably dysmorphic
            hand features.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1095)
  AUTHORS   Karoulias,S.Z., Beyens,A., Balic,Z., Symoens,S., Vandersteen,A.,
            Rideout,A.L., Dickinson,J., Callewaert,B. and Hubmacher,D.
  TITLE     A novel ADAMTS17 variant that causes Weill-Marchesani syndrome 4
            alters fibrillin-1 and collagen type I deposition in the
            extracellular matrix
  JOURNAL   Matrix Biol 88, 1-18 (2020)
   PUBMED   31726086
  REMARK    GeneRIF: A novel ADAMTS17 variant that causes Weill-Marchesani
            syndrome 4 alters fibrillin-1 and collagen type I deposition in the
            extracellular matrix.
REFERENCE   6  (residues 1 to 1095)
  AUTHORS   Morales,J., Al-Sharif,L., Khalil,D.S., Shinwari,J.M., Bavi,P.,
            Al-Mahrouqi,R.A., Al-Rajhi,A., Alkuraya,F.S., Meyer,B.F. and Al
            Tassan,N.
  TITLE     Homozygous mutations in ADAMTS10 and ADAMTS17 cause lenticular
            myopia, ectopia lentis, glaucoma, spherophakia, and short stature
  JOURNAL   Am J Hum Genet 85 (5), 558-568 (2009)
   PUBMED   19836009
  REMARK    GeneRIF: Homozygous mutation in ADAMTS17 causes lenticular myopia,
            ectopia lentis, glaucoma, spheropakia, and short stature.
REFERENCE   7  (residues 1 to 1095)
  AUTHORS   Sovio,U., Bennett,A.J., Millwood,I.Y., Molitor,J., O'Reilly,P.F.,
            Timpson,N.J., Kaakinen,M., Laitinen,J., Haukka,J., Pillas,D.,
            Tzoulaki,I., Molitor,J., Hoggart,C., Coin,L.J., Whittaker,J.,
            Pouta,A., Hartikainen,A.L., Freimer,N.B., Widen,E., Peltonen,L.,
            Elliott,P., McCarthy,M.I. and Jarvelin,M.R.
  TITLE     Genetic determinants of height growth assessed longitudinally from
            infancy to adulthood in the northern Finland birth cohort 1966
  JOURNAL   PLoS Genet 5 (3), e1000409 (2009)
   PUBMED   19266077
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1095)
  AUTHORS   Gudbjartsson,D.F., Walters,G.B., Thorleifsson,G., Stefansson,H.,
            Halldorsson,B.V., Zusmanovich,P., Sulem,P., Thorlacius,S.,
            Gylfason,A., Steinberg,S., Helgadottir,A., Ingason,A.,
            Steinthorsdottir,V., Olafsdottir,E.J., Olafsdottir,G.H.,
            Jonsson,T., Borch-Johnsen,K., Hansen,T., Andersen,G., Jorgensen,T.,
            Pedersen,O., Aben,K.K., Witjes,J.A., Swinkels,D.W., den Heijer,M.,
            Franke,B., Verbeek,A.L., Becker,D.M., Yanek,L.R., Becker,L.C.,
            Tryggvadottir,L., Rafnar,T., Gulcher,J., Kiemeney,L.A., Kong,A.,
            Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Many sequence variants affecting diversity of adult human height
  JOURNAL   Nat Genet 40 (5), 609-615 (2008)
   PUBMED   18391951
REFERENCE   9  (residues 1 to 1095)
  AUTHORS   Cal,S., Obaya,A.J., Llamazares,M., Garabaya,C., Quesada,V. and
            Lopez-Otin,C.
  TITLE     Cloning, expression analysis, and structural characterization of
            seven novel human ADAMTSs, a family of metalloproteinases with
            disintegrin and thrombospondin-1 domains
  JOURNAL   Gene 283 (1-2), 49-62 (2002)
   PUBMED   11867212
REFERENCE   10 (residues 1 to 1095)
  AUTHORS   Marzin,P., Cormier-Daire,V. and Tsilou,E.
  TITLE     Weill-Marchesani Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301293
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB279404.1, AJ315735.1,
            AC113187.6 and AC084855.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 20, 2006 this sequence version replaced NP_620688.1.
            
            Summary: This gene encodes a member of the ADAMTS (a disintegrin
            and metalloproteinase with thrombospondin motifs) protein family.
            ADAMTS family members share several distinct protein modules,
            including a propeptide region, a metalloproteinase domain, a
            disintegrin-like domain, and a thrombospondin type 1 (TS) motif.
            Individual members of this family differ in the number of
            C-terminal TS motifs, and some have unique C-terminal domains. The
            encoded preproprotein is proteolytically processed to generate the
            mature protein, which may promote breast cancer cell growth and
            survival. Mutations in this gene are associated with a
            Weill-Marchesani-like syndrome, which is characterized by
            lenticular myopia, ectopia lentis, glaucoma, spherophakia, and
            short stature. [provided by RefSeq, May 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ315735.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268070.9/ ENSP00000268070.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.3"
     Protein         1..1095
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 17 preproprotein"
                     /note="a disintegrin-like and metalloprotease (reprolysin
                     type) with thrombospondin type 1 motif, 17; a disintegrin
                     and metalloproteinase with thrombospondin motifs 17"
                     /calculated_mol_wt=118202
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2944
     Region          50..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TE56.2)"
     Region          <81..180
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TE56.2)"
     Region          199..206
                     /region_name="Cysteine switch. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TE56.2)"
     mat_peptide     224..1095
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 17. /id=PRO_0000029199"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TE56.2)"
                     /calculated_mol_wt=96524
     Region          232..449
                     /region_name="ZnMc_ADAMTS_like"
                     /note="Zinc-dependent metalloprotease, ADAMTS_like
                     subgroup. ADAMs (A Disintegrin And Metalloprotease) are
                     glycoproteins, which play roles in cell signaling, cell
                     fusion, and cell-cell interactions. This particular
                     subfamily represents domain architectures that...;
                     cd04273"
                     /db_xref="CDD:239801"
     Site            order(389..390,393,399)
                     /site_type="active"
                     /db_xref="CDD:239801"
     Region          466..533
                     /region_name="ADAMTS_CR_2"
                     /note="ADAMTS cysteine-rich domain 2; pfam17771"
                     /db_xref="CDD:465496"
     Site            483
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TE56.2)"
     Region          546..598
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          <630..699
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Region          702..779
                     /region_name="Spacer"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TE56.2)"
     Region          <713..783
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Site            785
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TE56.2)"
     Site            790
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TE56.2)"
     Region          809..861
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            832
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TE56.2)"
     Site            839
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TE56.2)"
     Region          865..921
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            894
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TE56.2)"
     Region          925..967
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          976..1023
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     CDS             1..1095
                     /gene="ADAMTS17"
                     /gene_synonym="WMS4"
                     /coded_by="NM_139057.4:77..3364"
                     /db_xref="CCDS:CCDS10383.1"
                     /db_xref="GeneID:170691"
                     /db_xref="HGNC:HGNC:17109"
                     /db_xref="MIM:607511"
ORIGIN      
        1 mcdgallppl vlpvllllvw gldpgtavgd aaadvevvlp wrvrpddvhl pplpaapgpr
       61 rrrrprtppa aprarpgera lllhlpafgr dlylqlrrdl rflsrgfeve eagaarrrgr
      121 paelcfysgr vlghpgslvs lsacgaaggl vgliqlgqeq vliqplnnsq gpfsgrehli
      181 rrkwsltpsp saeaqrpeql ckvltekkkp twgrpsrdwr errnairlts ehtvetlvva
      241 dadmvqyhga eaaqrfiltv mnmvynmfqh qslgikiniq vtklvllrqr paklsighhg
      301 erslesfchw qneeyggary lgnnqvpggk ddpplvdaav fvtrtdfcvh kdepcdtvgi
      361 aylggvcsak rkcvlaedng lnlaftiahe lghnlgmnhd ddhsscagrs himsgewvkg
      421 rnpsdlswss csrddlenfl kskvstcllv tdprsqhtvr lphklpgmhy saneqcqilf
      481 gmnatfcrnm ehlmcaglwc lvegdtsckt kldppldgte cgadkwcrag ecvsktpipe
      541 hvdgdwspwg awsmcsrtcg tgarfrqrkc dnpppgpggt hcpgasveha vcenlpcpkg
      601 lpsfrdqqcq ahdrlspkkk glltavvvdd kpcelycspl gkespllvad rvldgtpcgp
      661 yetdlcvhgk cqkigcdgii gsaakedrcg vcsgdgktch lvkgdfshar gtalkdsgkg
      721 sinsdwkiel pgefqiagtt vryvrrglwe kisakgptkl plhlmvllfh dqdygihyey
      781 tvpvnrtaen qsepekpqds lfiwthsgwe gcsvqcggge rrtivsctri vnktttlvnd
      841 sdcpqasrpe pqvrrcnlhp cqsrwvagpw spcsatcekg fqhrevtcvy qlqngthvat
      901 rplycpgprp aavqscegqd clsiweasew sqcsascgkg vwkrtvactn sqgkcdastr
      961 praeeacedy sgcyewktgd wstcsstcgk glqsrvvqcm hkvtgrhgse cpalskpapy
     1021 rqcyqevcnd rinantitsp rlaaltykct rdqwtvycrv ireknlcqdm rwyqrccqtc
     1081 rdfyankmrq pppns
//
LOCUS       NP_057654                377 aa            linear   PRI 27-APR-2025
DEFINITION  endoplasmic reticulum-Golgi intermediate compartment protein 2
            [Homo sapiens].
ACCESSION   NP_057654
VERSION     NP_057654.2
DBSOURCE    REFSEQ: accession NM_016570.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Yoo,W., Cho,E.B., Kim,S. and Yoon,J.B.
  TITLE     The E3 ubiquitin ligase MARCH2 regulates ERGIC3-dependent
            trafficking of secretory proteins
  JOURNAL   J Biol Chem 294 (28), 10900-10912 (2019)
   PUBMED   31142615
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Yu,J., Chia,J., Canning,C.A., Jones,C.M., Bard,F.A. and
            Virshup,D.M.
  TITLE     WLS retrograde transport to the endoplasmic reticulum during Wnt
            secretion
  JOURNAL   Dev Cell 29 (3), 277-291 (2014)
   PUBMED   24768165
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Kwok,S.C., Kumar,S. and Dai,G.
  TITLE     Characterization of a variant of ERGIC2 transcript
  JOURNAL   DNA Cell Biol 33 (2), 73-78 (2014)
   PUBMED   24303950
  REMARK    GeneRIF: A variant of ERGIC2 with four coding bases deleted has an
            abrogated function as a transport shuttle, but does continue to
            upregulate the heme oxygenase 1 gene, suggesting that it may be
            involved in the oxidative stress pathway.
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Yang,Y.F., Chou,M.Y., Fan,C.Y., Chen,S.F., Lyu,P.C., Liu,C.C. and
            Tseng,T.L.
  TITLE     The possible interaction of CDA14 and protein elongation factor
            1alpha
  JOURNAL   Biochim Biophys Acta 1784 (2), 312-318 (2008)
   PUBMED   17980171
  REMARK    GeneRIF: CDA14 participated in the elongation factor 1alpha
            regulated mechanisms
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Kwok,S.C., Liu,X., Mangel,P. and Daskal,I.
  TITLE     PTX1(ERGIC2)-VP22 fusion protein upregulates interferon-beta in
            prostate cancer cell line PC-3
  JOURNAL   DNA Cell Biol 25 (9), 523-529 (2006)
   PUBMED   16989575
  REMARK    GeneRIF: Ectopic expression of a partial sequence of PTX1 (Met84 -
            Leu225) as a VP22-fusion protein in prostate cancer cell line,
            PC-3, induced cellular senescence.
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Breuza,L., Halbeisen,R., Jeno,P., Otte,S., Barlowe,C., Hong,W. and
            Hauri,H.P.
  TITLE     Proteomics of endoplasmic reticulum-Golgi intermediate compartment
            (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies
            ERGIC-32, a new cycling protein that interacts with human Erv46
  JOURNAL   J Biol Chem 279 (45), 47242-47253 (2004)
   PUBMED   15308636
  REMARK    GeneRIF: ERGIC-32 functions as a modulator of the hErv41-hErv46
            complex by stabilizing hErv46
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Liu,X., Daskal,I. and Kwok,S.C.
  TITLE     Effects of PTX1 expression on growth and tumorigenicity of the
            prostate cancer cell line PC-3
  JOURNAL   DNA Cell Biol 22 (7), 469-474 (2003)
   PUBMED   12932305
  REMARK    GeneRIF: may play an important role in the growth and
            tumorigenicity of PC-3 prostate tumor cells
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Kwok,S.C., Liu,X. and Daskal,I.
  TITLE     Molecular cloning, expression, localization, and gene organization
            of PTX1, a human nuclear protein that is downregulated in prostate
            cancer
  JOURNAL   DNA Cell Biol 20 (6), 349-357 (2001)
   PUBMED   11445006
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF681475.1, BC000887.1, AL834128.2, BU675240.1 and AC009318.11.
            
            On Aug 4, 2004 this sequence version replaced NP_057654.1.
            
            Summary: ERGIC2, or PTX1, is a ubiquitously expressed nuclear
            protein that is downregulated in prostate carcinoma (Kwok et al.,
            2001 [PubMed 11445006]).[supplied by OMIM, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.452088.1, AL834128.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360150.9/ ENSP00000353270.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.22"
     Protein         1..377
                     /product="endoplasmic reticulum-Golgi intermediate
                     compartment protein 2"
                     /note="CD14 protein"
                     /calculated_mol_wt=42418
     Region          13..95
                     /region_name="ERGIC_N"
                     /note="Endoplasmic Reticulum-Golgi Intermediate
                     Compartment (ERGIC); pfam13850"
                     /db_xref="CDD:464000"
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RQ1.2)"
     Region          <170..332
                     /region_name="COPIIcoated_ERV"
                     /note="Endoplasmic reticulum vesicle transporter;
                     pfam07970"
                     /db_xref="CDD:462327"
     Site            320..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RQ1.2)"
     CDS             1..377
                     /gene="ERGIC2"
                     /gene_synonym="cd002; CDA14; Erv41; PTX1"
                     /coded_by="NM_016570.3:96..1229"
                     /db_xref="CCDS:CCDS41765.1"
                     /db_xref="GeneID:51290"
                     /db_xref="HGNC:HGNC:30208"
                     /db_xref="MIM:612236"
ORIGIN      
        1 mrrlnrkktl slvkeldafp kvpesyvets asggtvslia fttmalltim efsvyqdtwm
       61 kyeyevdkdf ssklrinidi tvamkcqyvg advldlaetm vasadglvye ptvfdlspqq
      121 kewqrmlqli qsrlqeehsl qdvifksafk ststalppre ddssqspnac rihghlyvnk
      181 vagnfhitvg kaiphprgha hlaalvnhes ynfshridhl sfgelvpaii npldgtekia
      241 idhnqmfqyf itvvptklht ykisadthqf svtereriin haagshgvsg ifmkydlssl
      301 mvtvteehmp fwqffvrlcg ivggifsttg mlhgigkfiv eiiccrfrlg sykpvnsvpf
      361 edghtdnhlp llennth
//
LOCUS       NP_001356340             299 aa            linear   PRI 27-APR-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 4 [Homo sapiens].
ACCESSION   NP_001356340
VERSION     NP_001356340.1
DBSOURCE    REFSEQ: accession NM_001369411.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
            Review article
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Du,P., Li,G., Wu,L. and Huang,M.
  TITLE     Perspectives of ERCC1 in early-stage and advanced cervical cancer:
            From experiments to clinical applications
  JOURNAL   Front Immunol 13, 1065379 (2023)
   PUBMED   36713431
  REMARK    GeneRIF: Perspectives of ERCC1 in early-stage and advanced cervical
            cancer: From experiments to clinical applications.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 299)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 299)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 299)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 299)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139353.3.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR736697.1, BX097972.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..299
                     /product="DNA excision repair protein ERCC-1 isoform 4"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=32863
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          235..261
                     /region_name="HHH"
                     /note="Helix-hairpin-helix motif; pfam00633"
                     /db_xref="CDD:425789"
     CDS             1..299
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369411.1:155..1054"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrsleqli
      241 aasredlalc pglgpqkvra lgknprswgk erapnkhnlr pqsfkvkkep ktrhsgfrl
//
LOCUS       NP_079497                250 aa            linear   PRI 27-APR-2025
DEFINITION  Kv channel-interacting protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_079497
VERSION     NP_079497.2
DBSOURCE    REFSEQ: accession NM_025221.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Mosley,J.D., Shaffer,C.M., Van Driest,S.L., Weeke,P.E., Wells,Q.S.,
            Karnes,J.H., Velez Edwards,D.R., Wei,W.Q., Teixeira,P.L.,
            Bastarache,L., Crawford,D.C., Li,R., Manolio,T.A., Bottinger,E.P.,
            McCarty,C.A., Linneman,J.G., Brilliant,M.H., Pacheco,J.A.,
            Thompson,W., Chisholm,R.L., Jarvik,G.P., Crosslin,D.R.,
            Carrell,D.S., Baldwin,E., Ralston,J., Larson,E.B., Grafton,J.,
            Scrol,A., Jouni,H., Kullo,I.J., Tromp,G., Borthwick,K.M.,
            Kuivaniemi,H., Carey,D.J., Ritchie,M.D., Bradford,Y., Verma,S.S.,
            Chute,C.G., Veluchamy,A., Siddiqui,M.K., Palmer,C.N., Doney,A.,
            MahmoudPour,S.H., Maitland-van der Zee,A.H., Morris,A.D.,
            Denny,J.C. and Roden,D.M.
  TITLE     A genome-wide association study identifies variants in KCNIP4
            associated with ACE inhibitor-induced cough
  JOURNAL   Pharmacogenomics J 16 (3), 231-237 (2016)
   PUBMED   26169577
  REMARK    GeneRIF: Results indicate that SNPs in KCNIP4 may modulate ACE
            inhibitor-induced cough risk.
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Kitazawa,M., Kubo,Y. and Nakajo,K.
  TITLE     The stoichiometry and biophysical properties of the Kv4 potassium
            channel complex with K+ channel-interacting protein (KChIP)
            subunits are variable, depending on the relative expression level
  JOURNAL   J Biol Chem 289 (25), 17597-17609 (2014)
   PUBMED   24811166
  REMARK    GeneRIF: Subunit counting by single-molecule imaging revealed that
            the bound number of KChIP4 in each Kv4.2.KChIP4 complex was
            dependent on the expression level of KChIP4.
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Tang,Y.Q., Liang,P., Zhou,J., Lu,Y., Lei,L., Bian,X. and Wang,K.
  TITLE     Auxiliary KChIP4a suppresses A-type K+ current through endoplasmic
            reticulum (ER) retention and promoting closed-state inactivation of
            Kv4 channels
  JOURNAL   J Biol Chem 288 (21), 14727-14741 (2013)
   PUBMED   23576435
  REMARK    GeneRIF: KChIP4a suppresses A-type Kv4 current via ER retention and
            enhancement of Kv4 closed-state inactivation.
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Bonne,A., Vreede,L., Kuiper,R.P., Bodmer,D., Jansen,C., Eleveld,M.,
            van Erp,F., Arkesteijn,G., Hoogerbrugge,N., van Ravenswaaij,C.,
            Schoenmakers,E.F. and Geurts van Kessel,A.
  TITLE     Mapping of constitutional translocation breakpoints in renal cell
            cancer patients: identification of KCNIP4 as a candidate gene
  JOURNAL   Cancer Genet Cytogenet 179 (1), 11-18 (2007)
   PUBMED   17981209
  REMARK    GeneRIF: Mutation of KCNIP4 is associated with renal cell
            carcinoma.
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Chen,C.P., Lee,L. and Chang,L.S.
  TITLE     Effects of metal-binding properties of human Kv channel-interacting
            proteins on their molecular structure and binding with Kv4.2
            channel
  JOURNAL   Protein J 25 (5), 345-351 (2006)
   PUBMED   16951992
  REMARK    GeneRIF: The conformational change with metal-bound KChIP4.1 is
            crucial for its interaction with Kv channel but not for KChIP2.2,
            and that the Mg2+- and Ca2+-binding properties of KChIP2.2 and
            KChIP4.1 have different effects on their molecular structure.
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Pruunsild,P. and Timmusk,T.
  TITLE     Structure, alternative splicing, and expression of the human and
            mouse KCNIP gene family
  JOURNAL   Genomics 86 (5), 581-593 (2005)
   PUBMED   16112838
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Morohashi,Y., Hatano,N., Ohya,S., Takikawa,R., Watabiki,T.,
            Takasugi,N., Imaizumi,Y., Tomita,T. and Iwatsubo,T.
  TITLE     Molecular cloning and characterization of CALP/KChIP4, a novel
            EF-hand protein interacting with presenilin 2 and voltage-gated
            potassium channel subunit Kv4
  JOURNAL   J Biol Chem 277 (17), 14965-14975 (2002)
   PUBMED   11847232
  REMARK    GeneRIF: cloning and investigation of interaction with presenilin 2
            and voltage-gated potassium channel subunit Kv4
REFERENCE   10 (residues 1 to 250)
  AUTHORS   Holmqvist,M.H., Cao,J., Hernandez-Pineda,R., Jacobson,M.D.,
            Carroll,K.I., Sung,M.A., Betty,M., Ge,P., Gilbride,K.J.,
            Brown,M.E., Jurman,M.E., Lawson,D., Silos-Santiago,I., Xie,Y.,
            Covarrubias,M., Rhodes,K.J., Distefano,P.S. and An,W.F.
  TITLE     Elimination of fast inactivation in Kv4 A-type potassium channels
            by an auxiliary subunit domain
  JOURNAL   Proc Natl Acad Sci U S A 99 (2), 1035-1040 (2002)
   PUBMED   11805342
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113606.3, BI596848.1,
            AF367023.1, BC032520.2, AC097505.2, AC104065.3 and BX648990.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 5, 2002 this sequence version replaced NP_079497.1.
            
            Summary: This gene encodes a member of the family of voltage-gated
            potassium (Kv) channel-interacting proteins (KCNIPs), which belong
            to the recoverin branch of the EF-hand superfamily. Members of the
            KCNIP family are small calcium binding proteins. They all have
            EF-hand-like domains, and differ from each other in the N-terminus.
            They are integral subunit components of native Kv4 channel
            complexes. They may regulate A-type currents, and hence neuronal
            excitability, in response to changes in intracellular calcium. This
            protein member also interacts with presenilin. Multiple
            alternatively spliced transcript variants encoding distinct
            isoforms have been identified for this gene. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1, also known as KCHIP4.1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.271330.1,
                                           SRR1803611.185942.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382152.7/ ENSP00000371587.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.31-p15.2"
     Protein         1..250
                     /product="Kv channel-interacting protein 4 isoform 1"
                     /note="calsenilin-like protein; a-type potassium channel
                     modulatory protein 4; Kv channel interacting protein 4"
                     /calculated_mol_wt=28598
     Region          2..44
                     /region_name="KIS. /evidence=ECO:0000250|UniProtKB:Q6PHZ8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PIL6.1)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ8; propagated from
                     UniProtKB/Swiss-Prot (Q6PIL6.1)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ8; propagated from
                     UniProtKB/Swiss-Prot (Q6PIL6.1)"
     Region          99..146
                     /region_name="EF-hand_8"
                     /note="EF-hand domain pair; pfam13833"
                     /db_xref="CDD:404678"
     Region          <128..235
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          237..250
                     /region_name="Interaction with KCND2.
                     /evidence=ECO:0000250|UniProtKB:Q8R426"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PIL6.1)"
     CDS             1..250
                     /gene="KCNIP4"
                     /gene_synonym="CALP; KCHIP4"
                     /coded_by="NM_025221.6:142..894"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43216.1"
                     /db_xref="GeneID:80333"
                     /db_xref="HGNC:HGNC:30083"
                     /db_xref="MIM:608182"
ORIGIN      
        1 mnvrrvesis aqleeasstg gflyaqnstk rsikerlmkl lpcsaaktss paiqnsvede
       61 lematvrhrp ealelleaqs kftkkelqil yrgfknecps gvvneetfke iysqffpqgd
      121 sttyahflfn afdtdhngav sfedfikgls illrgtvqek lnwafnlydi nkdgyitkee
      181 mldimkaiyd mmgkctypvl kedaprqhve tffqkmdknk dgvvtidefi escqkdenim
      241 rsmqlfenvi
//
LOCUS       NP_776873                184 aa            linear   MAM 27-APR-2025
DEFINITION  ras-related protein Rap-1A [Bos taurus].
ACCESSION   NP_776873
VERSION     NP_776873.1
DBSOURCE    REFSEQ: accession NM_174448.5
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Glading,A., Han,J., Stockton,R.A. and Ginsberg,M.H.
  TITLE     KRIT-1/CCM1 is a Rap1 effector that regulates endothelial cell cell
            junctions
  JOURNAL   J Cell Biol 179 (2), 247-254 (2007)
   PUBMED   17954608
  REMARK    GeneRIF: Rap1 increases KRIT-1 targeting to endothelial cell-cell
            junctions where it suppresses stress fibers and stabilizes
            junctional integrity.
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Smith,T.P., Grosse,W.M., Freking,B.A., Roberts,A.J., Stone,R.T.,
            Casas,E., Wray,J.E., White,J., Cho,J., Fahrenkrug,S.C.,
            Bennett,G.L., Heaton,M.P., Laegreid,W.W., Rohrer,G.A.,
            Chitko-McKown,C.G., Pertea,G., Holt,I., Karamycheva,S., Liang,F.,
            Quackenbush,J. and Keele,J.W.
  TITLE     Sequence evaluation of four pooled-tissue normalized bovine cDNA
            libraries and construction of a gene index for cattle
  JOURNAL   Genome Res 11 (4), 626-630 (2001)
   PUBMED   11282978
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Kawata,M., Kawahara,Y., Sunako,M., Araki,S., Koide,M., Tsuda,T.,
            Fukuzaki,H. and Takai,Y.
  TITLE     The molecular heterogeneity of the smg-21/Krev-1/rap1 proteins, a
            GTP-binding protein having the same effector domain as ras p21s, in
            bovine aortic smooth muscle membranes
  JOURNAL   Oncogene 6 (5), 841-848 (1991)
   PUBMED   1646988
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Kawata,M., Matsui,Y., Kondo,J., Hishida,T., Teranishi,Y. and
            Takai,Y.
  TITLE     A novel small molecular weight GTP-binding protein with the same
            putative effector domain as the ras proteins in bovine brain
            membranes. Purification, determination of primary structure, and
            characterization
  JOURNAL   J Biol Chem 263 (35), 18965-18971 (1988)
   PUBMED   3143720
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000003.1.
            
            Sequence Note: This RefSeq record was created from transcripts of
            different breeds because no single transcript from the same breed
            was available for the full length of the gene. The extent of this
            transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5571255.11784.1,
                                           SRR5721698.8484.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN03145458,
                                           SAMN03145491 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="3"
                     /map="3"
                     /breed="Hereford"
     Protein         1..184
                     /product="ras-related protein Rap-1A"
                     /EC_number="3.6.5.2"
                     /note="GTP-binding protein smg p21A"
                     /calculated_mol_wt=20856
     mat_peptide     1..181
                     /product="Ras-related protein Rap-1A. /id=PRO_0000030197"
                     /note="propagated from UniProtKB/Swiss-Prot (P62833.1)"
                     /calculated_mol_wt=20648
     Region          3..167
                     /region_name="Rap1"
                     /note="Rap1 family GTPase consists of Rap1a and Rap1b
                     isoforms; cd04175"
                     /db_xref="CDD:133375"
     Site            10..17
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133375"
     Site            order(11..12,59..60)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133375"
     Site            order(12..18,28..30,32,34..35,60,116..117,119,147..149)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133375"
     Site            order(17..18,32,34,40..41,54..55,57,59..60,149)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133375"
     Site            order(25,31,33,36..41)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:133375"
     Region          32..40
                     /region_name="Effector region. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P62833.1)"
     Site            33..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133375"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133375"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133375"
     Site            59..77
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133375"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133375"
     Site            147..149
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133375"
     Site            181
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P62834; propagated from
                     UniProtKB/Swiss-Prot (P62833.1)"
     CDS             1..184
                     /gene="RAP1A"
                     /coded_by="NM_174448.5:153..707"
                     /db_xref="BGD:BT12135"
                     /db_xref="GeneID:282031"
                     /db_xref="VGNC:VGNC:33715"
ORIGIN      
        1 mreyklvvlg sggvgksalt vqfvqgifve kydptiedsy rkqvevdcqq cmleildtag
       61 teqftamrdl ymkngqgfal vysitaqstf ndlqdlreqi lrvkdtedvp milvgnkcdl
      121 edervvgkeq gqnlarqwcn caflessaks kinvneifyd lvrqinrktp vekkkpkkks
      181 clll
//
LOCUS       NP_116294                401 aa            linear   PRI 27-APR-2025
DEFINITION  splicing factor 45 [Homo sapiens].
ACCESSION   NP_116294 NP_006441
VERSION     NP_116294.1
DBSOURCE    REFSEQ: accession NM_032905.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Fukumura,K., Sperotto,L., Seuss,S., Kang,H.S., Yoshimoto,R.,
            Sattler,M. and Mayeda,A.
  TITLE     SAP30BP interacts with RBM17/SPF45 to promote splicing in a subset
            of human short introns
  JOURNAL   Cell Rep 42 (12), 113534 (2023)
   PUBMED   38065098
  REMARK    GeneRIF: SAP30BP interacts with RBM17/SPF45 to promote splicing in
            a subset of human short introns.
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Fu,Y., Bai,C., Wang,S., Chen,D., Zhang,P., Wei,H., Rong,F.,
            Zhang,C., Chen,S. and Wang,Z.
  TITLE     AKT1 phosphorylates RBM17 to promote Sox2 transcription by
            modulating alternative splicing of FOXM1 to enhance cancer stem
            cell properties in colorectal cancer cells
  JOURNAL   FASEB J 37 (1), e22707 (2023)
   PUBMED   36520054
  REMARK    GeneRIF: AKT1 phosphorylates RBM17 to promote Sox2 transcription by
            modulating alternative splicing of FOXM1 to enhance cancer stem
            cell properties in colorectal cancer cells.
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Liu,L., Vujovic,A., Deshpande,N.P., Sathe,S., Anande,G.,
            Chen,H.T.T., Xu,J., Minden,M.D., Yeo,G.W., Unnikrishnan,A.,
            Hope,K.J. and Lu,Y.
  TITLE     The splicing factor RBM17 drives leukemic stem cell maintenance by
            evading nonsense-mediated decay of pro-leukemic factors
  JOURNAL   Nat Commun 13 (1), 3833 (2022)
   PUBMED   35781533
  REMARK    GeneRIF: The splicing factor RBM17 drives leukemic stem cell
            maintenance by evading nonsense-mediated decay of pro-leukemic
            factors.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Perry,W.L. 3rd, Shepard,R.L., Sampath,J., Yaden,B., Chin,W.W.,
            Iversen,P.W., Jin,S., Lesoon,A., O'Brien,K.A., Peek,V.L., Rolfe,M.,
            Shyjan,A., Tighe,M., Williamson,M., Krishnan,V., Moore,R.E. and
            Dantzig,A.H.
  TITLE     Human splicing factor SPF45 (RBM17) confers broad multidrug
            resistance to anticancer drugs when overexpressed--a phenotype
            partially reversed by selective estrogen receptor modulators
  JOURNAL   Cancer Res 65 (15), 6593-6600 (2005)
   PUBMED   16061639
  REMARK    GeneRIF: Resistance to various chemotherapeutics resulting from
            stable transfection of RBM17 (SPF45) in A2780 ovarian carcinoma
            cells may be due to effects of SPF45 on transcription and splicing
            of ERbeta-regulated genes.
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Sampath,J., Long,P.R., Shepard,R.L., Xia,X., Devanarayan,V.,
            Sandusky,G.E., Perry,W.L. 3rd, Dantzig,A.H., Williamson,M.,
            Rolfe,M. and Moore,R.E.
  TITLE     Human SPF45, a splicing factor, has limited expression in normal
            tissues, is overexpressed in many tumors, and can confer a
            multidrug-resistant phenotype to cells
  JOURNAL   Am J Pathol 163 (5), 1781-1790 (2003)
   PUBMED   14578179
  REMARK    GeneRIF: overexpression of SPF45 in HeLa, a cervical carcinoma cell
            line, resulted in drug resistance to doxorubicin and vincristine
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Graveley,B.R.
  TITLE     Sex, AGility, and the regulation of alternative splicing
  JOURNAL   Cell 109 (4), 409-412 (2002)
   PUBMED   12086596
  REMARK    Review article
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Lallena,M.J., Chalmers,K.J., Llamazares,S., Lamond,A.I. and
            Valcarcel,J.
  TITLE     Splicing regulation at the second catalytic step by Sex-lethal
            involves 3' splice site recognition by SPF45
  JOURNAL   Cell 109 (3), 285-296 (2002)
   PUBMED   12015979
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CV570433.1, AF542550.1,
            CN291330.1, AL157395.17 and AA905075.1.
            
            On Jan 13, 2003 this sequence version replaced NP_006441.1.
            
            Summary: This gene encodes an RNA binding protein. The encoded
            protein is part of the spliceosome complex and functions in the
            second catalytic step of mRNA splicing. Alternatively spliced
            transcript variants have been described. Related pseudogenes exist
            on chromosomes 9 and 15. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.162318.1, AF542550.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379888.9/ ENSP00000369218.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p15.1"
     Protein         1..401
                     /product="splicing factor 45"
                     /note="splicing factor 45kDa; 45 kDa-splicing factor"
                     /calculated_mol_wt=44831
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            41
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8JZX4; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Region          57..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Region          114..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96I25.1)"
     Region          235..279
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Region          303..397
                     /region_name="RRM_UHM_SPF45"
                     /note="RNA recognition motif (RRM) found in UHM domain of
                     45 kDa-splicing factor (SPF45) and similar proteins;
                     cd12647"
                     /db_xref="CDD:410051"
     CDS             1..401
                     /gene="RBM17"
                     /gene_synonym="SPF45"
                     /coded_by="NM_032905.5:179..1384"
                     /db_xref="CCDS:CCDS7077.1"
                     /db_xref="GeneID:84991"
                     /db_xref="HGNC:HGNC:16944"
                     /db_xref="MIM:606935"
ORIGIN      
        1 mslyddlgve tsdsktegws knfkllqsql qvkkaaltqa ksqrtkqstv lapvidlkrg
       61 gssddrqivd tpphvaaglk dpvpsgfsag evlipladey dpmfpndyek vvkrqreerq
      121 rqrelerqke ieerekrrkd rheasgfarr pdpdsdeded yererrkrsm ggaaiappts
      181 lvekdkelpr dfpyeedsrp rsqsskaaip ppvyeeqdrp rsptgpsnsf lanmggtvah
      241 kimqkygfre gqglgkheqg lstalsvekt skrggkiivg datekdaskk sdsnplteil
      301 kcptkvvllr nmvgagevde dlevetkeec ekygkvgkcv ifeipgapdd eavriflefe
      361 rvesaikavv dlngryfggr vvkacfynld kfrvldlaeq v
//
LOCUS       NP_758872                989 aa            linear   PRI 27-APR-2025
DEFINITION  voltage-gated delayed rectifier potassium channel KCNH1 isoform 1
            [Homo sapiens].
ACCESSION   NP_758872
VERSION     NP_758872.1
DBSOURCE    REFSEQ: accession NM_172362.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Wu,R., Li,X., Meng,Z., Li,P., He,Z. and Liang,L.
  TITLE     Phenotypic and genetic analysis of children with unexplained
            neurodevelopmental delay and neurodevelopmental comorbidities in a
            Chinese cohort using trio-based whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 205 (2024)
   PUBMED   38764027
  REMARK    GeneRIF: Phenotypic and genetic analysis of children with
            unexplained neurodevelopmental delay and neurodevelopmental
            comorbidities in a Chinese cohort using trio-based whole-exome
            sequencing.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Tian,M.Q., Li,R.K., Yang,F., Shu,X.M., Li,J., Chen,J., Peng,L.Y.,
            Yu,X.H. and Yang,C.J.
  TITLE     Phenotypic expansion of KCNH1-associated disorders to include
            isolated epilepsy and its associations with genotypes and molecular
            sub-regional locations
  JOURNAL   CNS Neurosci Ther 29 (1), 270-281 (2023)
   PUBMED   36285361
  REMARK    GeneRIF: Phenotypic expansion of KCNH1-associated disorders to
            include isolated epilepsy and its associations with genotypes and
            molecular sub-regional locations.
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Napoli,G., Panzironi,N., Traversa,A., Catalanotto,C., Pace,V.,
            Petrizzelli,F., Giovannetti,A., Lazzari,S., Cogoni,C.,
            Tartaglia,M., Carella,M., Mazza,T., Pizzuti,A., Parisi,C. and
            Caputo,V.
  TITLE     Potassium Channel KCNH1 Activating Variants Cause Altered
            Functional and Morphological Ciliogenesis
  JOURNAL   Mol Neurobiol 59 (8), 4825-4838 (2022)
   PUBMED   35639255
  REMARK    GeneRIF: Potassium Channel KCNH1 Activating Variants Cause Altered
            Functional and Morphological Ciliogenesis.
REFERENCE   4  (residues 1 to 989)
  AUTHORS   Jones,D.K.
  TITLE     Hysteretic hERG channel gating current recorded at physiological
            temperature
  JOURNAL   Sci Rep 12 (1), 5950 (2022)
   PUBMED   35396394
  REMARK    GeneRIF: Hysteretic hERG channel gating current recorded at
            physiological temperature.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 989)
  AUTHORS   Toplak,Z., Merzel,F., Pardo,L.A., Peterlin Masic,L. and Tomasic,T.
  TITLE     Molecular Dynamics-Derived Pharmacophore Model Explaining the
            Nonselective Aspect of KV10.1 Pore Blockers
  JOURNAL   Int J Mol Sci 22 (16), 8999 (2021)
   PUBMED   34445705
  REMARK    GeneRIF: Molecular Dynamics-Derived Pharmacophore Model Explaining
            the Nonselective Aspect of KV10.1 Pore Blockers.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 989)
  AUTHORS   Schonherr,R., Lober,K. and Heinemann,S.H.
  TITLE     Inhibition of human ether a go-go potassium channels by
            Ca(2+)/calmodulin
  JOURNAL   EMBO J 19 (13), 3263-3271 (2000)
   PUBMED   10880439
REFERENCE   7  (residues 1 to 989)
  AUTHORS   Pardo,L.A., del Camino,D., Sanchez,A., Alves,F., Bruggemann,A.,
            Beckh,S. and Stuhmer,W.
  TITLE     Oncogenic potential of EAG K(+) channels
  JOURNAL   EMBO J 18 (20), 5540-5547 (1999)
   PUBMED   10523298
REFERENCE   8  (residues 1 to 989)
  AUTHORS   Hoshi,N., Takahashi,H., Shahidullah,M., Yokoyama,S. and
            Higashida,H.
  TITLE     KCR1, a membrane protein that facilitates functional expression of
            non-inactivating K+ currents associates with rat EAG
            voltage-dependent K+ channels
  JOURNAL   J Biol Chem 273 (36), 23080-23085 (1998)
   PUBMED   9722534
REFERENCE   9  (residues 1 to 989)
  AUTHORS   Occhiodoro,T., Bernheim,L., Liu,J.H., Bijlenga,P., Sinnreich,M.,
            Bader,C.R. and Fischer-Lougheed,J.
  TITLE     Cloning of a human ether-a-go-go potassium channel expressed in
            myoblasts at the onset of fusion
  JOURNAL   FEBS Lett 434 (1-2), 177-182 (1998)
   PUBMED   9738473
REFERENCE   10 (residues 1 to 989)
  AUTHORS   Warmke,J.W. and Ganetzky,B.
  TITLE     A family of potassium channel genes related to eag in Drosophila
            and mammals
  JOURNAL   Proc Natl Acad Sci U S A 91 (8), 3438-3442 (1994)
   PUBMED   8159766
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092017.2, AJ001366.1,
            AF078742.1 and AC096636.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Voltage-gated potassium (Kv) channels represent the most
            complex class of voltage-gated ion channels from both functional
            and structural standpoints. Their diverse functions include
            regulating neurotransmitter release, heart rate, insulin secretion,
            neuronal excitability, epithelial electrolyte transport, smooth
            muscle contraction, and cell volume. This gene encodes a member of
            the potassium channel, voltage-gated, subfamily H. This member is a
            pore-forming (alpha) subunit of a voltage-gated non-inactivating
            delayed rectifier potassium channel. It is activated at the onset
            of myoblast differentiation. The gene is highly expressed in brain
            and in myoblasts. Overexpression of the gene may confer a growth
            advantage to cancer cells and favor tumor cell proliferation.
            Alternative splicing of this gene results in two transcript
            variants encoding distinct isoforms. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1), also known as eagB, encodes
            the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF078742.1, SRR1803612.181704.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000271751.10/ ENSP00000271751.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.2"
     Protein         1..989
                     /product="voltage-gated delayed rectifier potassium
                     channel KCNH1 isoform 1"
                     /note="ether-a-go-go, Drosophila, homolog of;
                     ether-a-go-go potassium channel 1; EAG channel 1;
                     voltage-gated potassium channel subunit Kv10.1; potassium
                     channel, voltage gated eag related subfamily H, member 1;
                     potassium voltage-gated channel, subfamily H
                     (eag-related), member 1; voltage-gated delayed rectifier
                     potassium channel KCNH1; ether-a-go-go 1"
                     /calculated_mol_wt=111292
     Region          41..135
                     /region_name="PAS_9"
                     /note="PAS domain; pfam13426"
                     /db_xref="CDD:463873"
     Region          151..162
                     /region_name="Required for phosphatidylinositol
                     bisphosphate binding.
                     /evidence=ECO:0000269|PubMed:27005320"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Region          220..>647
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Site            221..241
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Site            291..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Site            346..368
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Site            378..399
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Site            415
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95259.1)"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95259.1)"
     Region          463..468
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:Q63472"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Site            478..498
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Region          608..>712
                     /region_name="PRK11753"
                     /note="cAMP-activated global transcriptional regulator
                     CRP"
                     /db_xref="CDD:236969"
     Region          673..770
                     /region_name="Calmodulin-binding.
                     /evidence=ECO:0000269|PubMed:10880439"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Region          699..701
                     /region_name="Interaction with cyclic nucleotide-binding
                     pocket. /evidence=ECO:0000250|UniProtKB:Q60603"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Region          855..886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Region          924..964
                     /region_name="CAD (involved in subunit assembly).
                     /evidence=ECO:0000250|UniProtKB:Q63472"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Region          962..989
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95259.1)"
     Site            974
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60603; propagated from
                     UniProtKB/Swiss-Prot (O95259.1)"
     Site            978
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60603; propagated from
                     UniProtKB/Swiss-Prot (O95259.1)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60603; propagated from
                     UniProtKB/Swiss-Prot (O95259.1)"
     CDS             1..989
                     /gene="KCNH1"
                     /gene_synonym="EAG; EAG1; h-eag; hEAG; hEAG1; K(V)10.1;
                     Kv10.1; TMBTS; ZLS1"
                     /coded_by="NM_172362.3:204..3173"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1496.1"
                     /db_xref="GeneID:3756"
                     /db_xref="HGNC:HGNC:6250"
                     /db_xref="MIM:603305"
ORIGIN      
        1 mtmaggrrgl vapqntflen ivrrsndtnf vlgnaqivdw pivysndgfc klsgyhraev
       61 mqksstcsfm ygeltdkdti ekvrqtfeny emnsfeilmy kknrtpvwff vkiapirneq
      121 dkvvlflctf sditafkqpi eddsckgwgk farltralts srgvlqqlap svqkgenvhk
      181 hsrlaevlql gsdilpqykq eapktpphii lhycvfkttw dwiililtfy tailvpynvs
      241 fktrqnnvaw lvvdsivdvi flvdivlnfh ttfvgpagev isdpklirmn ylktwfvidl
      301 lsclpydvin afenvdevsa fmgdpgkigf adqipppleg resqgisslf sslkvvrllr
      361 lgrvarkldh yieygaavlv llvcvfglaa hwmaciwysi gdyeifdedt ktirnnswly
      421 qlamdigtpy qfngsgsgkw eggpsknsvy isslyftmts ltsvgfgnia pstdiekifa
      481 vaimmigsll yatifgnvtt ifqqmyantn ryhemlnsvr dflklyqvpk glservmdyi
      541 vstwsmsrgi dtekvlqicp kdmradicvh lnrkvfkehp afrlasdgcl ralamefqtv
      601 hcapgdliyh agesvdslcf vvsgsleviq ddevvailgk gdvfgdvfwk eatlaqscan
      661 vraltycdlh vikrdalqkv lefytafshs fsrnliltyn lrkrivfrki sdvkreeeer
      721 mkrkneapli lppdhpvrrl fqrfrqqkea rlaaerggrd lddldvekgn vltehasanh
      781 slvkasvvtv respatpvsf qaastsgvpd haklqapgse clgpkggggd cakrkswarf
      841 kdacgksedw nkvskaesme tlpertkasg eatlkktdsc dsgitksdlr ldnvgearsp
      901 qdrspilaev khsfypipeq tlqatvlevr helkedikal nakmtniekq lseilrilts
      961 rrssqspqel feisrpqspe serdifgas
//
LOCUS       NP_689857                 94 aa            linear   PRI 27-APR-2025
DEFINITION  protein FAM24B precursor [Homo sapiens].
ACCESSION   NP_689857 XP_001131369
VERSION     NP_689857.2
DBSOURCE    REFSEQ: accession NM_152644.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB410280.1, BG490871.1, AV762334.2, BC031343.1 and AC073585.8.
            
            On or before Oct 11, 2006 this sequence version replaced
            XP_001131369.1, NP_689857.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the supported protein. Both variants 1 and 2
            encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV762334.2, SRR1803614.244408.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368898.8/ ENSP00000357894.3
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..94
                     /product="protein FAM24B precursor"
                     /note="protein FAM24B"
                     /calculated_mol_wt=8073
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N5W8.2)"
                     /calculated_mol_wt=2092
     mat_peptide     22..94
                     /product="Protein FAM24B. /id=PRO_0000021224"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5W8.2)"
                     /calculated_mol_wt=8073
     Region          22..94
                     /region_name="FAM24"
                     /note="FAM24 family; pfam15193"
                     /db_xref="CDD:464556"
     CDS             1..94
                     /gene="FAM24B"
                     /coded_by="NM_152644.3:275..559"
                     /db_xref="CCDS:CCDS31303.1"
                     /db_xref="GeneID:196792"
                     /db_xref="HGNC:HGNC:23475"
ORIGIN      
        1 mpviaggila allllivvvl clyfkihnal kaakepeava vknhnpdkvw waknsqakti
       61 atescpalqc cegyrmcasf dslppcccdi negl
//
LOCUS       NP_061889                525 aa            linear   PRI 27-APR-2025
DEFINITION  keratin, type I cytoskeletal 24 [Homo sapiens].
ACCESSION   NP_061889
VERSION     NP_061889.2
DBSOURCE    REFSEQ: accession NM_019016.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Gul,D., Habtemichael,N., Dietrich,D., Dietrich,J., Gosswein,D.,
            Khamis,A., Deuss,E., Kunzel,J., Schneider,G., Strieth,S. and
            Stauber,R.H.
  TITLE     Identification of cytokeratin24 as a tumor suppressor for the
            management of head and neck cancer
  JOURNAL   Biol Chem 403 (8-9), 869-890 (2021)
   PUBMED   34450690
  REMARK    GeneRIF: Identification of cytokeratin24 as a tumor suppressor for
            the management of head and neck cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Shibata,N., Ishida,H., Kiyokawa,E., Singh,D.P., Sasaki,H. and
            Kubo,E.
  TITLE     Relative gene expression analysis of human pterygium tissues and UV
            radiation-evoked gene expression patterns in corneal and
            conjunctival cells
  JOURNAL   Exp Eye Res 199, 108194 (2020)
   PUBMED   32822701
  REMARK    GeneRIF: Relative gene expression analysis of human pterygium
            tissues and UV radiation-evoked gene expression patterns in corneal
            and conjunctival cells.
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Klar,A.S., Michalak,K., Bottcher-Haberzeth,S., Reichmann,E.,
            Meuli,M. and Biedermann,T.
  TITLE     The expression pattern of keratin 24 in tissue-engineered
            dermo-epidermal human skin substitutes in an in vivo model
  JOURNAL   Pediatr Surg Int 34 (2), 237-244 (2018)
   PUBMED   29039047
  REMARK    GeneRIF: the keratinocyte differentiation marker Keratin 24 is
            expressed in our dermo-epidermal skin substitutes in a normal
            pattern. This highlights that our bio-engineered skin analogs
            mature and reach homeostasis in an in vivo assay.
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Min,M., Chen,X.B., Wang,P., Landeck,L., Chen,J.Q., Li,W., Cai,S.Q.,
            Zheng,M. and Man,X.Y.
  TITLE     Role of keratin 24 in human epidermal keratinocytes
  JOURNAL   PLoS One 12 (3), e0174626 (2017)
   PUBMED   28362807
  REMARK    GeneRIF: K24 may be suggested as a potential differentiation marker
            and anti-proliferative factor in the epidermis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Hong,Y., Ho,K.S., Eu,K.W. and Cheah,P.Y.
  TITLE     A susceptibility gene set for early onset colorectal cancer that
            integrates diverse signaling pathways: implication for
            tumorigenesis
  JOURNAL   Clin Cancer Res 13 (4), 1107-1114 (2007)
   PUBMED   17317818
REFERENCE   7  (residues 1 to 525)
  AUTHORS   Schweizer,J., Bowden,P.E., Coulombe,P.A., Langbein,L., Lane,E.B.,
            Magin,T.M., Maltais,L., Omary,M.B., Parry,D.A., Rogers,M.A. and
            Wright,M.W.
  TITLE     New consensus nomenclature for mammalian keratins
  JOURNAL   J Cell Biol 174 (2), 169-174 (2006)
   PUBMED   16831889
REFERENCE   8  (residues 1 to 525)
  AUTHORS   Sprecher,E., Itin,P., Whittock,N.V., McGrath,J.A., Meyer,R.,
            DiGiovanna,J.J., Bale,S.J., Uitto,J. and Richard,G.
  TITLE     Refined mapping of Naegeli-Franceschetti- Jadassohn syndrome to a 6
            cM interval on chromosome 17q11.2-q21 and investigation of
            candidate genes
  JOURNAL   J Invest Dermatol 119 (3), 692-698 (2002)
   PUBMED   12230514
  REMARK    GeneRIF: KRT24 encodes a new keratin protein that bears high
            similarity to the type I keratins and displays a unique expression
            profile; sequence aberrations were not found in
            Naegeli-Franceschetti-Jadassohn syndrome
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090283.7, AK000268.1 and
            BC111968.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 25, 2008 this sequence version replaced NP_061889.1.
            
            Summary: This gene encodes a member of the type I (acidic) keratin
            family, which belongs to the superfamily of intermediate filament
            (IF) proteins. Keratins are heteropolymeric structural proteins
            which form the intermediate filament. These filaments, along with
            actin microfilaments and microtubules, compose the cytoskeleton of
            epithelial cells. The type I keratin genes are clustered in a
            region of chromosome 17q12-q21. [provided by RefSeq, Jun 2009].
            
            Transcript Variant: This variant (1, coding) represents the allele
            encoded by the GRCh38 reference genome and encodes isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000268.1, BC111968.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264651.3/ ENSP00000264651.2
            polymorphic pseudogene :: based on alignments, homology
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..525
                     /product="keratin, type I cytoskeletal 24"
                     /note="cytokeratin-24; type I keratin-24; keratin 24, type
                     I"
                     /calculated_mol_wt=54956
     Region          1..139
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M2I5.1)"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M2I5.1)"
     Region          140..452
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          140..175
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M2I5.1)"
     Region          176..198
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M2I5.1)"
     Region          199..290
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M2I5.1)"
     Region          291..313
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M2I5.1)"
     Region          314..452
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M2I5.1)"
     Region          453..525
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M2I5.1)"
     Region          459..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M2I5.1)"
     CDS             1..525
                     /gene="KRT24"
                     /gene_synonym="CK-24; K24; KA24"
                     /coded_by="NM_019016.3:60..1637"
                     /db_xref="CCDS:CCDS11372.1"
                     /db_xref="GeneID:192666"
                     /db_xref="HGNC:HGNC:18527"
                     /db_xref="MIM:607742"
ORIGIN      
        1 mscssrasss raggsssarv saggssfssg srcglggssa qgfrggassc slsggssgaf
       61 ggsfgggfgs csvgggfgga sgsgtgfggg ssfggvsgfg rgsgfcgssr fssgatggfy
      121 sygggmgggv gdgglfsgge kqtmqnlndr lanyldkvra leeantdlen kikewydkyg
      181 pgsgdggsgr dyskyysiie dlrnqiiaat venagiilhi dnarlaaddf rlkyenelcl
      241 rqsveading lrkvlddltm trsdlemqie sfteelaylr knheeemknm qgssggevtv
      301 emnaapgtdl tkllndmraq yeelaeqnrr eaeerfnkqs aslqaqistd agaatsakne
      361 itelkrtlqa leielqsqla mksslegtla dteagyvaql seiqtqisal eeeicqiwge
      421 tkcqnaeykq lldiktrlev eietyrrlld gegggssfae fggrnsgsvn mgsrdlvsgd
      481 srsgscsgqg rdssktrvtk tiveelvdgk vvssqvssis evkvk
//
LOCUS       NP_060941                426 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger CCCH domain-containing protein 15 [Homo sapiens].
ACCESSION   NP_060941
VERSION     NP_060941.2
DBSOURCE    REFSEQ: accession NM_018471.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Hou,J., Xu,M., Gu,H., Pei,D., Liu,Y., Huang,P., Chang,H. and Cui,H.
  TITLE     ZC3H15 promotes glioblastoma progression through regulating EGFR
            stability
  JOURNAL   Cell Death Dis 13 (1), 55 (2022)
   PUBMED   35027542
  REMARK    GeneRIF: ZC3H15 promotes glioblastoma progression through
            regulating EGFR stability.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Li,Q., Hou,J., Guo,C., Zhang,Y., Liu,L., Hu,H., Shi,S., Ji,Y.,
            Guo,L., Shi,Y., Liu,Y. and Cui,H.
  TITLE     ZC3H15 Correlates with a Poor Prognosis and Tumor Progression in
            Melanoma
  JOURNAL   Biomed Res Int 2021, 8305299 (2021)
   PUBMED   34988227
  REMARK    GeneRIF: ZC3H15 Correlates with a Poor Prognosis and Tumor
            Progression in Melanoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Capalbo,G., Muller-Kuller,T., Dietrich,U., Hoelzer,D., Ottmann,O.G.
            and Scheuring,U.J.
  TITLE     Inhibition of X4-tropic HIV type 1 replication by knockdown of the
            cellular protein LEREPO4
  JOURNAL   AIDS Res Hum Retroviruses 26 (10), 1155-1161 (2010)
   PUBMED   20925576
  REMARK    GeneRIF: down-regulation of LEREPO4 expression caused a significant
            inhibition of HIV replication
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Ishikawa,K., Akiyama,T., Ito,K., Semba,K. and Inoue,J.
  TITLE     Independent stabilizations of polysomal Drg1/Dfrp1 complex and
            non-polysomal Drg2/Dfrp2 complex in mammalian cells
  JOURNAL   Biochem Biophys Res Commun 390 (3), 552-556 (2009)
   PUBMED   19819225
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Gregory,R.C., Lord,K.A., Panek,L.B., Gaines,P., Dillon,S.B. and
            Wojchowski,D.M.
  TITLE     Subtraction cloning and initial characterization of novel
            epo-immediate response genes
  JOURNAL   Cytokine 12 (7), 845-857 (2000)
   PUBMED   10880228
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL040058.1 and BC021102.1.
            
            On Nov 19, 2006 this sequence version replaced NP_060941.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.288403.1, AF289586.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337859.11/ ENSP00000338788.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.1"
     Protein         1..426
                     /product="zinc finger CCCH domain-containing protein 15"
                     /note="DRG family-regulatory protein 1; likely ortholog of
                     mouse immediate early response erythropoietin 4"
                     /calculated_mol_wt=48472
     Region          1..325
                     /region_name="COG5252"
                     /note="Uncharacterized conserved protein, contains
                     CCCH-type Zn-finger protein [General function prediction
                     only]"
                     /db_xref="CDD:227577"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Region          53..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WU90.1)"
     Region          236..260
                     /region_name="Required for interaction with DRG1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Region          299..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Region          358..411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WU90.1)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     CDS             1..426
                     /gene="ZC3H15"
                     /gene_synonym="DFRP1; HT010; LEREPO4; MSTP012"
                     /coded_by="NM_018471.3:124..1404"
                     /db_xref="CCDS:CCDS42791.1"
                     /db_xref="GeneID:55854"
                     /db_xref="HGNC:HGNC:29528"
                     /db_xref="MIM:619704"
ORIGIN      
        1 mppkkqaqag gskkaeqkkk ekiiedktfg lknkkgakqq kfikavthqv kfgqqnprqv
       61 aqseaekklk kddkkkelqe lnelfkpvva aqkiskgadp ksvvcaffkq gqctkgdkck
      121 fshdltlerk cekrsvyida rdeelekdtm dnwdekklee vvnkkhgeae kkkpktqivc
      181 khfleaienn kygwfwvcpg ggdicmyrha lppgfvlkkd kkkeekedei sledlierer
      241 salgpnvtki tlesflawkk rkrqekidkl eqdmerrkad fkagkalvis grevfefrpe
      301 lvndddeead dtrytqgtgg devddsvsvn didlslyipr dvdetgitva slerfstyts
      361 dkdenklsea sggraenger sdleednere gtengaidav pvdenlftge dldeleeeln
      421 tldlee
//
LOCUS       NP_940871                161 aa            linear   PRI 27-APR-2025
DEFINITION  MORN repeat-containing protein 5 isoform a [Homo sapiens].
ACCESSION   NP_940871 XP_171204
VERSION     NP_940871.2
DBSOURCE    REFSEQ: accession NM_198469.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Argos,M., Tong,L., Pierce,B.L., Rakibuz-Zaman,M., Ahmed,A.,
            Islam,T., Rahman,M., Paul-Brutus,R., Rahaman,R., Roy,S.,
            Jasmine,F., Kibriya,M.G. and Ahsan,H.
  TITLE     Genome-wide association study of smoking behaviours among
            Bangladeshi adults
  JOURNAL   J Med Genet 51 (5), 327-333 (2014)
   PUBMED   24665060
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Letra,A., Menezes,R., Govil,M., Fonseca,R.F., McHenry,T.,
            Granjeiro,J.M., Castilla,E.E., Orioli,I.M., Marazita,M.L. and
            Vieira,A.R.
  TITLE     Follow-up association studies of chromosome region 9q and
            nonsyndromic cleft lip/palate
  JOURNAL   Am J Med Genet A 152A (7), 1701-1710 (2010)
   PUBMED   20583170
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY011325.1, BC133690.1, AK128877.1 and AI560944.1.
            
            On Feb 11, 2009 this sequence version replaced NP_940871.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.288970.1,
                                           SRR5189667.48927.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373764.8/ ENSP00000362869.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.2"
     Protein         1..161
                     /product="MORN repeat-containing protein 5 isoform a"
                     /note="MORN repeat-containing protein 5"
                     /calculated_mol_wt=18600
     Region          <5..76
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          8..30
                     /region_name="MORN 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VZ52.1)"
     Region          31..53
                     /region_name="MORN 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VZ52.1)"
     Region          54..75
                     /region_name="MORN 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VZ52.1)"
     CDS             1..161
                     /gene="MORN5"
                     /gene_synonym="C9orf113; C9orf18"
                     /coded_by="NM_198469.4:66..551"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6836.1"
                     /db_xref="GeneID:254956"
                     /db_xref="HGNC:HGNC:17841"
                     /db_xref="MIM:619837"
ORIGIN      
        1 meytgskyig eyvdgrmegk akyilpteti yvgemkdgmf hgegtlyfps gsqydaiwen
       61 glaikgtytf sdglhydekn whycdgydrr fyteilnglk pagmaqltnm dpprkipkgy
      121 ydcgdgfynp vtrvvkdyrn rflrnaddde hewitrtcrk g
//
LOCUS       NP_597709                739 aa            linear   PRI 27-APR-2025
DEFINITION  ribonucleoprotein PTB-binding 1 isoform 1 [Homo sapiens].
ACCESSION   NP_597709 XP_058946
VERSION     NP_597709.3
DBSOURCE    REFSEQ: accession NM_133452.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Wedler,A., Bley,N., Glass,M., Muller,S., Rausch,A., Lederer,M.,
            Urbainski,J., Schian,L., Obika,K.B., Simon,T., Peters,L.M.,
            Misiak,C., Fuchs,T., Kohn,M., Jacob,R., Gutschner,T., Ihling,C.,
            Sinz,A. and Huttelmaier,S.
  TITLE     RAVER1 hinders lethal EMT and modulates miR/RISC activity by the
            control of alternative splicing
  JOURNAL   Nucleic Acids Res 52 (7), 3971-3988 (2024)
   PUBMED   38300787
  REMARK    GeneRIF: RAVER1 hinders lethal EMT and modulates miR/RISC activity
            by the control of alternative splicing.
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Fink-Baldauf,I.M., Stuart,W.D., Brewington,J.J., Guo,M. and
            Maeda,Y.
  TITLE     CRISPRi links COVID-19 GWAS loci to LZTFL1 and RAVER1
  JOURNAL   EBioMedicine 75, 103806 (2022)
   PUBMED   34998241
  REMARK    GeneRIF: CRISPRi links COVID-19 GWAS loci to LZTFL1 and RAVER1.
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 739)
  CONSRTM   COVID-19 Host Genetics Initiative
  TITLE     Mapping the human genetic architecture of COVID-19
  JOURNAL   Nature 600 (7889), 472-477 (2021)
   PUBMED   34237774
REFERENCE   5  (residues 1 to 739)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 739)
  AUTHORS   Miyasaka,T., Morita,M., Ito,K., Suzuki,T., Fukuda,H., Takeda,S.,
            Inoue,J., Semba,K. and Yamamoto,T.
  TITLE     Interaction of antiproliferative protein Tob with the CCR4-NOT
            deadenylase complex
  JOURNAL   Cancer Sci 99 (4), 755-761 (2008)
   PUBMED   18377426
REFERENCE   7  (residues 1 to 739)
  AUTHORS   Romanelli,M.G., Lorenzi,P., Avesani,F. and Morandi,C.
  TITLE     Functional characterization of the ribonucleoprotein, PTB-binding
            1/Raver1 promoter region
  JOURNAL   Gene 405 (1-2), 79-87 (2007)
   PUBMED   17931803
  REMARK    GeneRIF: Raver1 gene promoter region shares common features of
            ubiquitously expressed gene with the interacting splicing regulator
            PTB
REFERENCE   8  (residues 1 to 739)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 739)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 739)
  AUTHORS   Huttelmaier,S., Illenberger,S., Grosheva,I., Rudiger,M.,
            Singer,R.H. and Jockusch,B.M.
  TITLE     Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and
            microfilament attachment proteins
  JOURNAL   J Cell Biol 155 (5), 775-786 (2001)
   PUBMED   11724819
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB446023.1, BX401103.2, BC037565.1 and CR746909.1.
            
            On Sep 25, 2018 this sequence version replaced NP_597709.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2099020.1,
                                           SRR7346977.1448016.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: locus in the vicinity of
                                      disease-associated variant(s)
            MANE Ensembl match     :: ENST00000617231.5/ ENSP00000482277.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..739
                     /product="ribonucleoprotein PTB-binding 1 isoform 1"
                     /note="protein raver-1"
                     /calculated_mol_wt=77713
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY67.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IY67.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IY67.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IY67.1)"
     Region          45..60
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY67.1)"
     Region          59..129
                     /region_name="RRM1_RAVER1"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     ribonucleoprotein PTB-binding 1 (raver-1); cd12663"
                     /db_xref="CDD:410064"
     Site            order(67..69,91..93,117,119..121)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410064"
     Region          133..209
                     /region_name="RRM2_RAVER1"
                     /note="RNA recognition motif 2 (RRM2) found found in
                     vertebrate ribonucleoprotein PTB-binding 1 (raver-1);
                     cd12665"
                     /db_xref="CDD:410066"
     Region          219..306
                     /region_name="RRM3_RAVER1"
                     /note="RNA recognition motif 3 (RRM3) found in vertebrate
                     ribonucleoprotein PTB-binding 1 (raver-1); cd12667"
                     /db_xref="CDD:410068"
     Region          307..395
                     /region_name="Interaction with PTBP1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY67.1)"
     Region          <364..635
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          391..474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY67.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IY67.1)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IY67.1)"
     CDS             1..739
                     /gene="RAVER1"
                     /coded_by="NM_133452.3:23..2242"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45960.2"
                     /db_xref="GeneID:125950"
                     /db_xref="HGNC:HGNC:30296"
                     /db_xref="MIM:609950"
ORIGIN      
        1 maadvsvthr pplspksgae veagdaaerr apeeelppld peeirkrleh terqfrnrrk
       61 ilirglpgdv tnqevhdlls dyelkycfvd kykgtafvtl lngeqaeaai nafhqsrlre
      121 relsvqlqpt dallcvanlp psltqqqfee lvrpfgsler cflvysertg qskgygfaey
      181 mkkdsaarak sdllgkplgp rtlyvhwtda gqltpallhs rclcvdrlpp gfndvdalcr
      241 alsavhsptf cqlacgqdgq lkgfavleye taemaeeaqq qadglslggs hlrvsfcapg
      301 ppgrsmlaal iaaqatalnr gkgllpepni lqllnnlgps aslqlllnpl lhgsaggkqg
      361 llgappampl lngpalstal lqlalqtqgq kkpgilgdsp lgalqpgaqp anpllgelpa
      421 ggglppelpp rrgkpppllp svlgpaggdr ealglgppaa qltpppapvg lrgsglrglq
      481 kdsgplptpp gvsllgeppk dyriplnpyl nlhsllpasn lagkeargwg gagrsrrpae
      541 gpptnppapg ggsssskafq lksrllspls sarlppepgl sdsysfdyps dmgprrlfsh
      601 prepalgphg psrhkmsppp sgfgerssgg sgggplshfy sgsptsyfts glqaglkqsh
      661 lskaigsspl gsgegllgls pgpnghshll ktplggqkrs fahllpspep spegsyvgqh
      721 sqglgghyad sylkrkrif
//
LOCUS       NP_001910                302 aa            linear   PRI 27-APR-2025
DEFINITION  enoyl-CoA delta isomerase 1, mitochondrial isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001910
VERSION     NP_001910.2
DBSOURCE    REFSEQ: accession NM_001919.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Bramhecha,Y.M., Guerard,K.P., Audet-Walsh,E., Rouzbeh,S.,
            Kassem,O., Pernet,E., Scarlata,E., Hamel,L., Brimo,F.,
            Divangahi,M., Aprikian,A.G., Chevalier,S., Giguere,V. and
            Lapointe,J.
  TITLE     Fatty acid oxidation enzyme Delta3, Delta2-enoyl-CoA isomerase 1
            (ECI1) drives aggressive tumor phenotype and predicts poor clinical
            outcome in prostate cancer patients
  JOURNAL   Oncogene 41 (20), 2798-2810 (2022)
   PUBMED   35411033
  REMARK    GeneRIF: Fatty acid oxidation enzyme Delta3, Delta2-enoyl-CoA
            isomerase 1 (ECI1) drives aggressive tumor phenotype and predicts
            poor clinical outcome in prostate cancer patients.
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Rasmussen,A.L., Diamond,D.L., McDermott,J.E., Gao,X., Metz,T.O.,
            Matzke,M.M., Carter,V.S., Belisle,S.E., Korth,M.J., Waters,K.M.,
            Smith,R.D. and Katze,M.G.
  TITLE     Systems virology identifies a mitochondrial fatty acid oxidation
            enzyme, dodecenoyl coenzyme A delta isomerase, required for
            hepatitis C virus replication and likely pathogenesis
  JOURNAL   J Virol 85 (22), 11646-11654 (2011)
   PUBMED   21917952
  REMARK    GeneRIF: Hepatitis C virus growth and RNA replication in hepatoma
            cell lines stably expressing coenzyme A delta isomerase
            (DCI)-targeting short hairpin RNA (shRNA) were abrogated,
            indicating that DCI is required for productive infection.
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Partanen,S.T., Novikov,D.K., Popov,A.N., Mursula,A.M.,
            Hiltunen,J.K. and Wierenga,R.K.
  TITLE     The 1.3 A crystal structure of human mitochondrial
            Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for
            the fatty acyl group
  JOURNAL   J Mol Biol 342 (4), 1197-1208 (2004)
   PUBMED   15351645
  REMARK    GeneRIF: determination of structure and mode of binding for fatty
            acyl group
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Takahashi,Y., Hirata,Y., Burstein,Y. and Listowsky,I.
  TITLE     Delta 3, delta 2-enoyl-CoA isomerase is the protein that copurifies
            with human glutathione S-transferases from S-hexylglutathione
            affinity matrices
  JOURNAL   Biochem J 304 (Pt 3) (Pt 3), 849-852 (1994)
   PUBMED   7818490
REFERENCE   8  (residues 1 to 302)
  AUTHORS   Janssen,U., Fink,T., Lichter,P. and Stoffel,W.
  TITLE     Human mitochondrial 3,2-trans-enoyl-CoA isomerase (DCI): gene
            structure and localization to chromosome 16p13.3
  JOURNAL   Genomics 23 (1), 223-228 (1994)
   PUBMED   7829074
REFERENCE   9  (residues 1 to 302)
  AUTHORS   Kilponen,J.M., Hayrinen,H.M., Rehn,M. and Hiltunen,J.K.
  TITLE     cDNA cloning and amino acid sequence of human mitochondrial delta 3
            delta 2-enoyl-CoA isomerase: comparison of the human enzyme with
            its rat counterpart, mitochondrial short-chain isomerase
  JOURNAL   Biochem J 300 (Pt 1) (Pt 1), 1-5 (1994)
   PUBMED   8198519
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK291127.1, BQ773923.1 and
            AC009065.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 13, 2005 this sequence version replaced NP_001910.1.
            
            Summary: This gene encodes a member of the hydratase/isomerase
            superfamily. The protein encoded is a key mitochondrial enzyme
            involved in beta-oxidation of unsaturated fatty acids. It catalyzes
            the transformation of 3-cis and 3-trans-enoyl-CoA esters arising
            during the stepwise degradation of cis-, mono-, and polyunsaturated
            fatty acids to the 2-trans-enoyl-CoA intermediates. Alternatively
            spliced transcript variants have been described. [provided by
            RefSeq, May 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.616007.1, AK291127.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152568 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000301729.9/
                                                  ENSP00000301729.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..302
                     /product="enoyl-CoA delta isomerase 1, mitochondrial
                     isoform 1 precursor"
                     /EC_number="5.3.3.8"
                     /note="dodecenoyl-Coenzyme A delta isomerase (3,2
                     trans-enoyl-Coenzyme A isomerase); dodecenoyl-CoA delta
                     isomerase (3,2 trans-enoyl-CoA isomerase); D3,D2-enoyl-CoA
                     isomerase; acetylene-allene isomerase; 3,2-trans-enoyl-CoA
                     isomerase, mitochondrial; enoyl-CoA delta isomerase 1,
                     mitochondrial; delta(3),Delta(2)-enoyl-CoA isomerase;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=28736
     transit_peptide 1..41
                     /calculated_mol_wt=4098
     mat_peptide     42..302
                     /product="enoyl-CoA delta isomerase 1, mitochondrial
                     isoform 1"
                     /calculated_mol_wt=28736
     Region          52..298
                     /region_name="ECH_1"
                     /note="Enoyl-CoA hydratase/isomerase; pfam00378"
                     /db_xref="CDD:395302"
     Site            61
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P42125; propagated from
                     UniProtKB/Swiss-Prot (P42126.1)"
     Site            order(67,69,102,106..110,149,151..153,177..178,181)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:119339"
     Site            89
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P42126.1)"
     Site            order(108,153)
                     /site_type="active"
                     /note="oxyanion hole (OAH) forming residues [active]"
                     /db_xref="CDD:119339"
     Site            order(133,141,162..165,179..182,188,190..192,194..195,
                     200..201,203..204,206..207,210,221,224,239,242..243)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:119339"
     Site            178
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000305|PubMed:15351645; propagated from
                     UniProtKB/Swiss-Prot (P42126.1)"
     Site            283
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P42125; propagated from
                     UniProtKB/Swiss-Prot (P42126.1)"
     CDS             1..302
                     /gene="ECI1"
                     /gene_synonym="DCI"
                     /coded_by="NM_001919.4:22..930"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10464.1"
                     /db_xref="GeneID:1632"
                     /db_xref="HGNC:HGNC:2703"
                     /db_xref="MIM:600305"
ORIGIN      
        1 malvasvrvp arvllragar lpgaalgrte raagggdgar rfgsqrvlve pdagagvavm
       61 kfknppvnsl slefltelvi sleklendks frgviltsdr pgvfsagldl temcgrspah
      121 yagywkavqe lwlrlyqsnl vlvsaingac paggclvalt cdyriladnp ryciglnetq
      181 lgiiapfwlk dtlentighr aaeralqlgl lfppaealqv givdqvvpee qvqstalsai
      241 aqwmaipdha rqltkammrk atasrlvtqr dadvqnfvsf iskdsiqksl qmylerlkee
      301 kg
//
LOCUS       NP_001139283             801 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor SOX-6 isoform b [Homo sapiens].
ACCESSION   NP_001139283
VERSION     NP_001139283.1
DBSOURCE    REFSEQ: accession NM_001145811.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Lu,M.Y., Fang,C.Y., Hsieh,P.L., Chao,S.C., Liao,Y.W., Ohiro,Y.,
            Yu,C.C. and Ho,D.C.
  TITLE     MIAT promotes myofibroblastic activities and transformation in oral
            submucous fibrosis through sponging the miR-342-3p/SOX6 axis
  JOURNAL   Aging (Albany NY) 16 (19), 12909-12927 (2024)
   PUBMED   39379100
  REMARK    GeneRIF: MIAT promotes myofibroblastic activities and
            transformation in oral submucous fibrosis through sponging the
            miR-342-3p/SOX6 axis.
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Li,M., Niu,M., Fan,X., Chen,F., Cao,H., Liu,Q., Gan,S., Yue,P. and
            Gao,J.
  TITLE     LncRNA MIR181A2HG inhibits keratinocytes proliferation through
            miR-223-3p/SOX6 axis
  JOURNAL   Aging (Albany NY) 16 (11), 9846-9858 (2024)
   PUBMED   38848163
  REMARK    GeneRIF: LncRNA MIR181A2HG inhibits keratinocytes proliferation
            through miR-223-3p/SOX6 axis.
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Pastori,V., Zambanini,G., Citterio,E., Weiss,T., Nakamura,Y.,
            Cantu,C. and Ronchi,A.E.
  TITLE     Transcriptional repression of the oncofetal LIN28B gene by the
            transcription factor SOX6
  JOURNAL   Sci Rep 14 (1), 10287 (2024)
   PUBMED   38704454
  REMARK    GeneRIF: Transcriptional repression of the oncofetal LIN28B gene by
            the transcription factor SOX6.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Zheng,H., Liu,M., Shi,S., Huang,H., Yang,X., Luo,Z., Song,Y.,
            Xu,Q., Li,T., Xue,L., Lu,F. and Wang,J.
  TITLE     MAP4K4 and WT1 mediate SOX6-induced cellular senescence by
            synergistically activating the ATF2-TGFbeta2-Smad2/3 signaling
            pathway in cervical cancer
  JOURNAL   Mol Oncol 18 (5), 1327-1346 (2024)
   PUBMED   38383842
  REMARK    GeneRIF: MAP4K4 and WT1 mediate SOX6-induced cellular senescence by
            synergistically activating the ATF2-TGFbeta2-Smad2/3 signaling
            pathway in cervical cancer.
REFERENCE   5  (residues 1 to 801)
  AUTHORS   Li,S. and Wang,Y.
  TITLE     Regulatory mechanism of DDX5 in ox-LDL-induced endothelial cell
            injury through the miR-640/SOX6 axis
  JOURNAL   Clin Hemorheol Microcirc 88 (2), 157-170 (2024)
   PUBMED   39093065
  REMARK    GeneRIF: Regulatory mechanism of DDX5 in ox-LDL-induced endothelial
            cell injury through the miR-640/SOX6 axis.
REFERENCE   6  (residues 1 to 801)
  AUTHORS   Ueda,R., Iizuka,Y., Yoshida,K., Kawase,T., Kawakami,Y. and Toda,M.
  TITLE     Identification of a human glioma antigen, SOX6, recognized by
            patients' sera
  JOURNAL   Oncogene 23 (7), 1420-1427 (2004)
   PUBMED   14691456
REFERENCE   7  (residues 1 to 801)
  AUTHORS   Cohen-Barak,O., Hagiwara,N., Arlt,M.F., Horton,J.P. and
            Brilliant,M.H.
  TITLE     Cloning, characterization and chromosome mapping of the human SOX6
            gene
  JOURNAL   Gene 265 (1-2), 157-164 (2001)
   PUBMED   11255018
REFERENCE   8  (residues 1 to 801)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 801)
  AUTHORS   Hagiwara,N., Klewer,S.E., Samson,R.A., Erickson,D.T., Lyon,M.F. and
            Brilliant,M.H.
  TITLE     Sox6 is a candidate gene for p100H myopathy, heart block, and
            sudden neonatal death
  JOURNAL   Proc Natl Acad Sci U S A 97 (8), 4180-4185 (2000)
   PUBMED   10760285
REFERENCE   10 (residues 1 to 801)
  AUTHORS   Denny,P., Swift,S., Brand,N., Dabhade,N., Barton,P. and Ashworth,A.
  TITLE     A conserved family of genes related to the testis determining gene,
            SRY
  JOURNAL   Nucleic Acids Res 20 (11), 2887 (1992)
   PUBMED   1614875
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027016.4, AC013595.11,
            AC068405.5, AC103794.2 and AC009869.7.
            
            Summary: This gene encodes a member of the D subfamily of sex
            determining region y-related transcription factors that are
            characterized by a conserved DNA-binding domain termed the high
            mobility group box and by their ability to bind the minor groove of
            DNA. The encoded protein is a transcriptional activator that is
            required for normal development of the central nervous system,
            chondrogenesis and maintenance of cardiac and skeletal muscle
            cells. The encoded protein interacts with other family members to
            cooperatively activate gene expression. Alternative splicing
            results in multiple transcript variants.[provided by RefSeq, Mar
            2009].
            
            Transcript Variant: This variant (3) has multiple differences in
            the coding region, compared to variant 1. The encoded isoform (3)
            is shorter than isoform 1. Variants 1 and 3 both encode the same
            isoform (b).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037866.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.2"
     Protein         1..801
                     /product="transcription factor SOX-6 isoform b"
                     /note="SRY-box containing gene 6; transcription factor
                     SOX-6; SRY-box 6; SRY (sex determining region Y)-box 6"
                     /calculated_mol_wt=88857
     Region          592..669
                     /region_name="HMG-box_EGL13-like"
                     /note="high mobility group (HMG)-box found in
                     Caenorhabditis elegans protein egg laying defective 13
                     (EGL-13) and similar proteins; cd22042"
                     /db_xref="CDD:438848"
     Site            order(593,595..596,598..599,601..602,606,609,613,620..622,
                     625..626,629,632..633,651,661,663..666)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438848"
     CDS             1..801
                     /gene="SOX6"
                     /gene_synonym="HSSOX6; SOXD; TOLCAS"
                     /coded_by="NM_001145811.2:164..2569"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53604.1"
                     /db_xref="GeneID:55553"
                     /db_xref="HGNC:HGNC:16421"
                     /db_xref="MIM:607257"
ORIGIN      
        1 msskqatspf acaadgedam tqdltsreke egsdqhvash lplhpimhnk phseelptlv
       61 stiqqdadwd svlssqqrme sennklcsly sfrntstsph kpdegsrdre imtsvtfgtp
      121 errkgsladv vdtlkqkkle emtrteqeds scmekllskd wkekmerlnt sellgeikgt
      181 peslaekerq lstmitqlis lreqllaahd eqkklaasqi ekqrqqmdla rqqqeqiarq
      241 qqqllqqqhk inllqqqiqv qghmpplmip ifphdqrtla aaaaaqqgfl fppgitykpg
      301 dnypvqfips tmaaaaasgl splqlqqlya aqlasmqvsp gakmpstpqp pntagtvspt
      361 giknekrgts pvtqvkdeaa aqplnlssrp ktaepvkspt sptqnlfpas ktspvnlpnk
      421 ssipspiggs lgrgsslgkw ksqhqeetye ldilsslnsp alfgdqdtvm kaiqearkmr
      481 eqiqreqqqq qphgvdgkls sinnmglnsc rnekertrfe nlgpqltgks nedgklgpgv
      541 idltrpedae gskamngsaa klqqyycwpt ggatvaearv yrdargrass ephikrpmna
      601 fmvwakderr kilqafpdmh nsniskilgs rwksmsnqek qpyyeeqarl skihlekypn
      661 ykykprpkrt civdgkklri geykqlmrsr rqemrqfftv gqqpqipitt gtgvvypgai
      721 tmatttpspq mtsdcsstsa spepslpviq stygmktdgg slagneming edememyddy
      781 eddpksdyss eneapeavsa n
//
LOCUS       NP_847884                403 aa            linear   PRI 27-APR-2025
DEFINITION  RILP-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_847884 XP_351878
VERSION     NP_847884.2
DBSOURCE    REFSEQ: accession NM_178314.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Yang,X., Zhang,D., Shen,S., Li,P., Li,M., Niu,J., Ma,D., Xu,D.,
            Li,S., Guo,X., Wang,Z., Zhao,Y., Ren,H., Ling,C., Wang,Y., Fan,Y.,
            Shen,J., Zhu,Y., Wang,D., Cui,L., Chen,L., Shi,C. and Dai,Y.
  TITLE     A large pedigree study confirmed the CGG repeat expansion of RILPL1
            Is associated with oculopharyngodistal myopathy
  JOURNAL   BMC Med Genomics 16 (1), 253 (2023)
   PUBMED   37864208
  REMARK    GeneRIF: A large pedigree study confirmed the CGG repeat expansion
            of RILPL1 Is associated with oculopharyngodistal myopathy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Yu,J., Shan,J., Yu,M., Di,L., Xie,Z., Zhang,W., Lv,H., Meng,L.,
            Zheng,Y., Zhao,Y., Gang,Q., Guo,X., Wang,Y., Xi,J., Zhu,W., Da,Y.,
            Hong,D., Yuan,Y., Yan,C., Wang,Z. and Deng,J.
  TITLE     The CGG repeat expansion in RILPL1 is associated with
            oculopharyngodistal myopathy type 4
  JOURNAL   Am J Hum Genet 109 (3), 533-541 (2022)
   PUBMED   35148830
  REMARK    GeneRIF: The CGG repeat expansion in RILPL1 is associated with
            oculopharyngodistal myopathy type 4.
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Lara Ordonez,A.J., Fernandez,B., Fdez,E., Romo-Lozano,M.,
            Madero-Perez,J., Lobbestael,E., Baekelandt,V., Aiastui,A., Lopez de
            Munain,A., Melrose,H.L., Civiero,L. and Hilfiker,S.
  TITLE     RAB8, RAB10 and RILPL1 contribute to both LRRK2 kinase-mediated
            centrosomal cohesion and ciliogenesis deficits
  JOURNAL   Hum Mol Genet 28 (21), 3552-3568 (2019)
   PUBMED   31428781
  REMARK    GeneRIF: Pathogenic LRRK2 causes the centrosomal accumulation not
            only of phosho-RAB8 but also of phospho-RAB10, and the effects on
            centrosomal cohesion are dependent on RAB8, RAB10 and RILPL1.
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Steger,M., Diez,F., Dhekne,H.S., Lis,P., Nirujogi,R.S., Karayel,O.,
            Tonelli,F., Martinez,T.N., Lorentzen,E., Pfeffer,S.R., Alessi,D.R.
            and Mann,M.
  TITLE     Systematic proteomic analysis of LRRK2-mediated Rab GTPase
            phosphorylation establishes a connection to ciliogenesis
  JOURNAL   Elife 6, e31012 (2017)
   PUBMED   29125462
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Gonzalez,M.C., Romero,J.M., Ingaramo,M.C., Munoz Sosa,C.J.,
            Curtino,J.A. and Carrizo,M.E.
  TITLE     Enhancement by GOSPEL protein of GAPDH aggregation induced by
            nitric oxide donor and its inhibition by NAD(.)
  JOURNAL   FEBS Lett 590 (14), 2210-2220 (2016)
   PUBMED   27282776
  REMARK    GeneRIF: NAD(+) inhibited both GAPDH aggregation and co-aggregation
            with GOSPEL, a hitherto undescribed effect of the coenzyme against
            the consequences of oxidative stress.
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Schaub,J.R. and Stearns,T.
  TITLE     The Rilp-like proteins Rilpl1 and Rilpl2 regulate ciliary membrane
            content
  JOURNAL   Mol Biol Cell 24 (4), 453-464 (2013)
   PUBMED   23264467
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Sen,N., Hara,M.R., Ahmad,A.S., Cascio,M.B., Kamiya,A., Ehmsen,J.T.,
            Agrawal,N., Hester,L., Dore,S., Snyder,S.H. and Sawa,A.
  TITLE     GOSPEL: a neuroprotective protein that binds to GAPDH upon
            S-nitrosylation
  JOURNAL   Neuron 63 (1), 81-91 (2009)
   PUBMED   19607794
  REMARK    Erratum:[Neuron. 2009 Sep 10;63(5):709. Aggrawal, Nishant
            [corrected to Agrawal, Nishant]]
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Wang,T., Wong,K.K. and Hong,W.
  TITLE     A unique region of RILP distinguishes it from its related proteins
            in its regulation of lysosomal morphology and interaction with Rab7
            and Rab34
  JOURNAL   Mol Biol Cell 15 (2), 815-826 (2004)
   PUBMED   14668488
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC055713.29, BX359997.2, BC089444.1, BX281699.1, BC080626.1 and
            AC145423.8.
            
            On Aug 7, 2008 this sequence version replaced NP_847884.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089444.1, SRR1803613.19534.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376874.9/ ENSP00000366070.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..403
                     /product="RILP-like protein 1 isoform 1"
                     /note="RILP-like protein 1; GAPDH competitor of SIAH
                     protein enhances life"
                     /calculated_mol_wt=46977
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZUQ0; propagated from
                     UniProtKB/Swiss-Prot (Q5EBL4.1)"
     Region          27..175
                     /region_name="Jnk-SapK_ap_N"
                     /note="JNK_SAPK-associated protein-1; pfam09744"
                     /db_xref="CDD:462875"
     Region          <96..319
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          254..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EBL4.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5EBL4.1)"
     Region          295..357
                     /region_name="RILP"
                     /note="Rab interacting lysosomal protein; pfam11461"
                     /db_xref="CDD:463282"
     Region          327..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EBL4.1)"
     Region          384..403
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EBL4.1)"
     CDS             1..403
                     /gene="RILPL1"
                     /gene_synonym="GOSPEL; OPDM4; RLP1"
                     /coded_by="NM_178314.5:238..1449"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45006.1"
                     /db_xref="GeneID:353116"
                     /db_xref="HGNC:HGNC:26814"
                     /db_xref="MIM:614092"
ORIGIN      
        1 meeergsala aesaleknva eltvmdvydi aslvghefer vidqhgceai arlmpkvvrv
       61 leilevlvsr hhvapeldel rleldrlrle rmdriekerk hqkelelved vwrgeaqdll
      121 sqiaqlqeen kqlmtnlshk dvnfseeefq khegmserer qvmkklkevv dkqrdeirak
      181 drelglkned vealqqqqtr lmkinhdlrh rvtvveaqgk alieqkvele adlqtkeqem
      241 gslraelgkl rerlqgehsq ngeeepetep vgeesisdae kvamdlkdpn rprftlqelr
      301 dvlhernelk skvfllqeel ayykseemee enripqpppi ahprtspqpe sgikrlfsff
      361 srdkkrlant qrnvhiqesf gqwanthrdd gyteqgqeal qhl
//
LOCUS       NP_001028793             496 aa            linear   ROD 27-APR-2025
DEFINITION  myotilin [Mus musculus].
ACCESSION   NP_001028793 NP_067459 XP_899274 XP_906449 XP_919012 XP_928070
VERSION     NP_001028793.1
DBSOURCE    REFSEQ: accession NM_001033621.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Pathak,P., Blech-Hermoni,Y., Subedi,K., Mpamugo,J.,
            Obeng-Nyarko,C., Ohman,R., Molloy,I., Kates,M., Hale,J.,
            Stauffer,S., Sharan,S.K. and Mankodi,A.
  TITLE     Myopathy associated LDB3 mutation causes Z-disc disassembly and
            protein aggregation through PKCalpha and TSC2-mTOR downregulation
  JOURNAL   Commun Biol 4 (1), 355 (2021)
   PUBMED   33742095
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Chen,J.Q., Mori,H., Cardiff,R.D., Trott,J.F., Hovey,R.C.,
            Hubbard,N.E., Engelberg,J.A., Tepper,C.G., Willis,B.J., Khan,I.H.,
            Ravindran,R.K., Chan,S.R., Schreiber,R.D. and Borowsky,A.D.
  TITLE     Abnormal Mammary Development in 129:STAT1-Null Mice is
            Stroma-Dependent
  JOURNAL   PLoS One 10 (6), e0129895 (2015)
   PUBMED   26075897
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Zhou,H., Wan,B., Grubisic,I., Kaplan,T. and Tjian,R.
  TITLE     TAF7L modulates brown adipose tissue formation
  JOURNAL   Elife 3, e02811 (2014)
   PUBMED   24876128
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 496)
  AUTHORS   von Nandelstadh,P., Ismail,M., Gardin,C., Suila,H., Zara,I.,
            Belgrano,A., Valle,G., Carpen,O. and Faulkner,G.
  TITLE     A class III PDZ binding motif in the myotilin and FATZ families
            binds enigma family proteins: a common link for Z-disc myopathies
  JOURNAL   Mol Cell Biol 29 (3), 822-834 (2009)
   PUBMED   19047374
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Ochala,J., Carpen,O. and Larsson,L.
  TITLE     Maintenance of muscle mass, fiber size, and contractile function in
            mice lacking the Z-disc protein myotilin
  JOURNAL   Ups J Med Sci 114 (4), 235-241 (2009)
   PUBMED   19878039
  REMARK    GeneRIF: Myotilin does not have a significant influence on muscle
            mass, muscle fiber size, or regulation of muscle contraction.
            Alternatively, compensatory over-expressions of other elements may
            compensate for the lack of myotilin.
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Potthoff,M.J., Arnold,M.A., McAnally,J., Richardson,J.A.,
            Bassel-Duby,R. and Olson,E.N.
  TITLE     Regulation of skeletal muscle sarcomere integrity and postnatal
            muscle function by Mef2c
  JOURNAL   Mol Cell Biol 27 (23), 8143-8151 (2007)
   PUBMED   17875930
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Moza,M., Mologni,L., Trokovic,R., Faulkner,G., Partanen,J. and
            Carpen,O.
  TITLE     Targeted deletion of the muscular dystrophy gene myotilin does not
            perturb muscle structure or function in mice
  JOURNAL   Mol Cell Biol 27 (1), 244-252 (2007)
   PUBMED   17074808
  REMARK    GeneRIF: either myotilin does not participate in muscle development
            and basal function maintenance or other proteins serve as
            structural and functional compensatory molecules when myotilin is
            absent
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Mologni,L., Moza,M., Lalowski,M.M. and Carpen,O.
  TITLE     Characterization of mouse myotilin and its promoter
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1001-1009 (2005)
   PUBMED   15752755
  REMARK    GeneRIF: features suggest an important role for myotilin in
            sarcomere organization.
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Mologni,L., Salmikangas,P., Fougerousse,F., Beckmann,J.S. and
            Carpen,O.
  TITLE     Developmental expression of myotilin, a gene mutated in limb-girdle
            muscular dystrophy type 1A
  JOURNAL   Mech Dev 103 (1-2), 121-125 (2001)
   PUBMED   11335118
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Hauser,M.A., Horrigan,S.K., Salmikangas,P., Torian,U.M.,
            Viles,K.D., Dancel,R., Tim,R.W., Taivainen,A., Bartoloni,L.,
            Gilchrist,J.M., Stajich,J.M., Gaskell,P.C., Gilbert,J.R.,
            Vance,J.M., Pericak-Vance,M.A., Carpen,O., Westbrook,C.A. and
            Speer,M.C.
  TITLE     Myotilin is mutated in limb girdle muscular dystrophy 1A
  JOURNAL   Hum Mol Genet 9 (14), 2141-2147 (2000)
   PUBMED   10958653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132130.3.
            
            On or before May 12, 2006 this sequence version replaced
            NP_067459.1, XP_899274.1, XP_906449.1, XP_919012.1, XP_928070.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064052.1, AK017447.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 23.74 cM"
     Protein         1..496
                     /product="myotilin"
                     /note="titin immunoglobulin domain protein; myofibrillar
                     titin-like Ig domains protein"
                     /calculated_mol_wt=55185
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIF9.1)"
     Site            20
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9JIF9.1)"
     Region          78..149
                     /region_name="Necessary for interaction with ACTN1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIF9.1)"
     Region          202..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIF9.1)"
     Region          213..496
                     /region_name="Necessary for interaction with ACTA1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIF9.1)"
     Region          213..491
                     /region_name="Necessary for interaction with FLNC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIF9.1)"
     Region          248..338
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          265..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          278..282
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          304..308
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          318..323
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..334
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          347..438
                     /region_name="IgI_Myotilin_C"
                     /note="C-terminal immunoglobulin (Ig)-like domain of
                     myotilin; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05892"
                     /db_xref="CDD:409473"
     Region          347..350
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409473"
     Region          353..358
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409473"
     Region          363..370
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409473"
     Region          377..383
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409473"
     Region          384..387
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409473"
     Region          394..400
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409473"
     Region          403..413
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409473"
     Region          417..425
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409473"
     Region          427..438
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409473"
     CDS             1..496
                     /gene="Myot"
                     /gene_synonym="5530402I04Rik; Ttid"
                     /coded_by="NM_001033621.4:275..1765"
                     /db_xref="CCDS:CCDS29228.1"
                     /db_xref="GeneID:58916"
                     /db_xref="MGI:MGI:1889800"
ORIGIN      
        1 mfnyerpkhf iqpqnpcgsr lqppgpevsg fpsqtkqssi viqprqcteq rfsasstvss
       61 hitvsssayp apqqlagpnp gqkvtatynq spasflssil psqpdycnsk ipstvdsnyq
      121 qssvnqpvna mssqaanarp tpktpdheiq gskealiqdl erklkckdtl lhngnqrlty
      181 eekmarrllg pqnaaavfqa qnsdvqdspq hnpeqarlhv ptsqvrsrss sraeandqda
      241 iqekfypprf iqvpenmsie egrfcrmdfk vsglpapdvs wylngrpvqs delhkmivse
      301 kgfhslifev vrasdagpya cvarnragea tftvqldvla kehkrapmfi fkpqskkvfe
      361 getvklecqi saipppklfw krnnemvqfn tdrislyhdn agrvtllikd vnkkdagwyt
      421 vsavneagvt tcntrldvta rpiqtlpapk qlrvrptfsk ylalngrgld vkqafnpege
      481 fqrlaaqsgl yeseel
//
LOCUS       NP_653254                587 aa            linear   PRI 27-APR-2025
DEFINITION  nucleus accumbens-associated protein 2 [Homo sapiens].
ACCESSION   NP_653254
VERSION     NP_653254.1
DBSOURCE    REFSEQ: accession NM_144653.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Penning,A., Snoeck,S., Garritsen,O., Tosoni,G., Hof,A., de Boer,F.,
            van Hasenbroek,J., Zhang,L., Thrupp,N., Craessaerts,K., Fiers,M.
            and Salta,E.
  TITLE     NACC2, a molecular effector of miR-132 regulation at the interface
            between adult neurogenesis and Alzheimer's disease
  JOURNAL   Sci Rep 14 (1), 21163 (2024)
   PUBMED   39256511
  REMARK    GeneRIF: NACC2, a molecular effector of miR-132 regulation at the
            interface between adult neurogenesis and Alzheimer's disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Wang,X.Z., Chen,L., Sun,H., Li,X.Q., Wang,H., Zhang,X.P., Sun,J.B.
            and Wang,H.Y.
  TITLE     MiR-199a-3p promotes repair of myocardial infarction by targeting
            NACC2
  JOURNAL   Int J Clin Exp Pathol 16 (3), 57-66 (2023)
   PUBMED   37033393
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Xuan,C., Wang,Q., Han,X., Duan,Y., Li,L., Shi,L., Wang,Y., Shan,L.,
            Yao,Z. and Shang,Y.
  TITLE     RBB, a novel transcription repressor, represses the transcription
            of HDM2 oncogene
  JOURNAL   Oncogene 32 (32), 3711-3721 (2013)
   PUBMED   22926524
  REMARK    GeneRIF: RBB is a novel transcriptional repressor and an important
            regulator of p53 pathway.
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   6  (residues 1 to 587)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL138781.13, BM791117.1, BC015649.2 and AL355574.27.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3900986.1,
                                           SRR14038193.2457454.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000277554.4/ ENSP00000277554.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..587
                     /product="nucleus accumbens-associated protein 2"
                     /note="BEN domain containing 9; BTB (POZ) domain
                     containing 14A; NACC family member 2, BEN and BTB (POZ)
                     domain containing; BTB/POZ domain-containing protein 14A;
                     transcription repressor with a BTB domain and a BEN
                     domain; repressor with BTB domain and BEN domain"
                     /calculated_mol_wt=62706
     Region          1..131
                     /region_name="BTB_POZ_BTBD14A_NAC2"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in nucleus
                     accumbens-associated protein 2 (NAC-2); cd18289"
                     /db_xref="CDD:349598"
     Region          240..272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BF6.1)"
     Region          373..450
                     /region_name="BEN"
                     /note="The BEN domain is found in diverse animal proteins;
                     smart01025"
                     /db_xref="CDD:214981"
     Region          542..587
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BF6.1)"
     CDS             1..587
                     /gene="NACC2"
                     /gene_synonym="BEND9; BTBD14; BTBD14A; BTBD31; NAC-2; RBB"
                     /coded_by="NM_144653.5:161..1924"
                     /db_xref="CCDS:CCDS6993.1"
                     /db_xref="GeneID:138151"
                     /db_xref="HGNC:HGNC:23846"
                     /db_xref="MIM:615786"
ORIGIN      
        1 msqmlhieip nfgntvlgcl neqrllglyc dvsivvkgqa fkahravlaa sslyfrdlfs
       61 gnsksafelp gsvppacfqq ilsfcytgrl tmtaseqlvv mytagflqiq hivergtdlm
      121 fkvssphcds qtaviedags epqspcnqlq paaaaaapyv vspsvpipll trvkheamel
      181 ppagpglapk rpletgprdg vavaagaava agtaplklpr vsyygvpsla tlipgiqqmp
      241 ypqgertspg asslpttdsp tsyhneedee ddeaydtmve eqygqmyika sgsyavqekp
      301 epvplesrsc vlirrdlval paslisqigy rchpklyseg dpgeklelva gsgvyitrgq
      361 lmnchlcagv khkvllrrll atffdrntla nscgtgirss tsdpsrkpld srvlnavkly
      421 cqnfapsfke semnviaadm ctnarrvrkr wlpkiksmlp egvemyrtvm gsaaasvpld
      481 pefppaaaqv feqriyaerr gdaativalr tdavnvdlsa aanpafdage evdgagsviq
      541 evaapeplpa dgqsppqpfe qggggpsrpq tpaaaarrpe gtyagtl
//
LOCUS       NP_065912                514 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_065912
VERSION     NP_065912.1
DBSOURCE    REFSEQ: accession NM_020861.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Kambe,G., Kobayashi,M., Ishikita,H., Koyasu,S., Hammond,E.M. and
            Harada,H.
  TITLE     ZBTB7A forms a heterodimer with ZBTB2 and inhibits ZBTB2
            homodimerization required for full activation of HIF-1
  JOURNAL   Biochem Biophys Res Commun 733, 150604 (2024)
   PUBMED   39197198
  REMARK    GeneRIF: ZBTB7A forms a heterodimer with ZBTB2 and inhibits ZBTB2
            homodimerization required for full activation of HIF-1.
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Qi,C., Zhang,L. and Wang,W.
  TITLE     The novel circ_0004674/miR-139-5p/ZBTB2 regulatory cascade inhibits
            the development of oral squamous cell carcinoma
  JOURNAL   Head Neck 46 (7), 1671-1682 (2024)
   PUBMED   38665011
  REMARK    GeneRIF: The novel circ_0004674/miR-139-5p/ZBTB2 regulatory cascade
            inhibits the development of oral squamous cell carcinoma.
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Chow,C.C.T., Kobayashi,M., Kambe,G. and Harada,H.
  TITLE     ZBTB2 is Recruited to a Specific Subset of HIF-1 Target Loci to
            Facilitate Full Gene Expression Under Hypoxia
  JOURNAL   J Mol Biol 435 (15), 168162 (2023)
   PUBMED   37257772
  REMARK    GeneRIF: ZBTB2 is Recruited to a Specific Subset of HIF-1 Target
            Loci to Facilitate Full Gene Expression Under Hypoxia.
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Koyasu,S., Horita,S., Saito,K., Kobayashi,M., Ishikita,H.,
            Chow,C.C., Kambe,G., Nishikawa,S., Menju,T., Morinibu,A.,
            Okochi,Y., Tabuchi,Y., Onodera,Y., Takeda,N., Date,H.,
            Semenza,G.L., Hammond,E.M. and Harada,H.
  TITLE     ZBTB2 links p53 deficiency to HIF-1-mediated hypoxia signaling to
            promote cancer aggressiveness
  JOURNAL   EMBO Rep 24 (1), e54042 (2023)
   PUBMED   36341521
  REMARK    GeneRIF: ZBTB2 links p53 deficiency to HIF-1-mediated hypoxia
            signaling to promote cancer aggressiveness.
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Lafaye,C., Barbier,E., Miscioscia,A., Saint-Pierre,C., Kraut,A.,
            Coute,Y., Plo,I., Gasparutto,D., Ravanat,J.L. and Breton,J.
  TITLE     DNA binding of the p21 repressor ZBTB2 is inhibited by cytosine
            hydroxymethylation
  JOURNAL   Biochem Biophys Res Commun 446 (1), 341-346 (2014)
   PUBMED   24607898
  REMARK    GeneRIF: ZBTB2 being considered as a multifunctional cell
            proliferation activator, notably through p21 repression, this work
            points out new epigenetic processes potentially involved in
            carcinogenesis.
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Kim,D.H., Lee,S.T., Won,H.H., Kim,S., Kim,M.J., Kim,H.J., Kim,S.H.,
            Kim,J.W., Kim,H.J., Kim,Y.K., Sohn,S.K., Moon,J.H., Jung,C.W. and
            Lipton,J.H.
  TITLE     A genome-wide association study identifies novel loci associated
            with susceptibility to chronic myeloid leukemia
  JOURNAL   Blood 117 (25), 6906-6911 (2011)
   PUBMED   21540461
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Jeon,B.N., Choi,W.I., Yu,M.Y., Yoon,A.R., Kim,M.H., Yun,C.O. and
            Hur,M.W.
  TITLE     ZBTB2, a novel master regulator of the p53 pathway
  JOURNAL   J Biol Chem 284 (27), 17935-17946 (2009)
   PUBMED   19380588
  REMARK    GeneRIF: ZBTB2 is a potential proto-oncogenic master control gene
            of the p53 pathway and, in particular, is a potent transcription
            repressor of the cell cycle arrest gene p21 by inhibiting p53 and
            Sp1
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Jung,S.Y., Malovannaya,A., Wei,J., O'Malley,B.W. and Qin,J.
  TITLE     Proteomic analysis of steady-state nuclear hormone receptor
            coactivator complexes
  JOURNAL   Mol Endocrinol 19 (10), 2451-2465 (2005)
   PUBMED   16051665
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK291942.1 and BC020172.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020172.1, SRR3476690.882953.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325144.5/ ENSP00000323183.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.1"
     Protein         1..514
                     /product="zinc finger and BTB domain-containing protein 2"
                     /calculated_mol_wt=57206
     Region          3..117
                     /region_name="BTB_POZ_ZBTB2"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 2 (ZBTB2); cd18193"
                     /db_xref="CDD:349502"
     Region          149..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N680.1)"
     Region          254..276
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          256..276
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N680.1)"
     Region          363..385
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          365..385
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(370,372,374,376..377,380..381,384,397,399,403..404,
                     407..408,442,455,457,459,461..462,465..466)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          377..399
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          392..443
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          450..466
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..514
                     /gene="ZBTB2"
                     /gene_synonym="ZNF437"
                     /coded_by="NM_020861.3:153..1697"
                     /db_xref="CCDS:CCDS5231.1"
                     /db_xref="GeneID:57621"
                     /db_xref="HGNC:HGNC:20868"
                     /db_xref="MIM:616595"
ORIGIN      
        1 mdlanhglil lqqlnaqref gflcdctvai gdvyfkahks vlasfsnyfk mlfvhqtsec
       61 vrlkptdiqp difsyllhlm ytgkmapqli dpvrleqgik flhaypliqe aslasqgafs
      121 hpdqvfplas slygiqiadh qlrqatkias apeklgrdpr pqtsrisqeq vpeasqlsql
      181 tsnlaqvnrt nmtpsdplqt slspelvstp vpppppgeet nleasssdeq pasltiahvk
      241 psimkrngsf pkyyachlcg rrftlrsslr ehlqihtgvp ftssqqgesr vpltlcsnaa
      301 dlgkdamevp eagmisdsel qhisdspiid gqqqsetppp sdiadidnle qadqerevkr
      361 rkyecticgr kfiqkshwre hmyihtgkpf kcstcdksfc ranqaarhvc lnqsidtytm
      421 vdkqtlelct feegsqmdnm lvqtnkpykc nlcdktfstp nevvkhscqn qnsdvfalde
      481 grsillgsgd sevtepdhpv lasikkeqet vlld
//
LOCUS       NP_001182149             546 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 783 [Homo sapiens].
ACCESSION   NP_001182149
VERSION     NP_001182149.1
DBSOURCE    REFSEQ: accession NM_001195220.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 546)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004890.2.
            
            Transcript Variant: This variant (1) represents the protein-coding
            transcript.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence because no single transcript was available for the
            full length of the gene. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.442946.1,
                                           SRR1660805.346092.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000434415.6/ ENSP00000410890.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..546
                     /product="zinc finger protein 783"
                     /note="protein ZNF783; zinc finger family member 783"
                     /calculated_mol_wt=60883
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZMS7.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6ZMS7.2)"
     Region          143..202
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          218..270
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZMS7.2)"
     Region          291..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZMS7.2)"
     Region          349..371
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          351..371
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          372..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZMS7.2)"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(443,445,447,449..450,453..454,457,473,475,479..480,
                     483..484,487,501,503,505,507..508,511..512,515)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          468..488
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          468..488
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          480..505
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          496..516
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          527..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZMS7.2)"
     CDS             1..546
                     /gene="ZNF783"
                     /coded_by="NM_001195220.2:139..1779"
                     /db_xref="CCDS:CCDS56519.1"
                     /db_xref="GeneID:100289678"
                     /db_xref="HGNC:HGNC:27222"
ORIGIN      
        1 maeaapardp etdkhtedqs pstplpqpaa eknsylyste itlwtvvaai qalekkvdsc
       61 ltrlltlegr tgtaekklad cektavefgn qlegkwavlg tllqeygllq rrlenvenll
      121 rnrnfwilrl ppgskgeapk vpvtfddvav yfselewgkl edwqkelykh vmrgnyetlv
      181 sldyaiskpd iltriergee pcldrwgqek gnevevgrpr mmgtglppyp ehltsplspa
      241 qeelkegqap kqqqdsearv apagpeaggg vaikteaqse demtperlfl gvsrgqtecr
      301 iprgprnrpg gpsrhqaqgm prvrageprp pgasgetprv lsrrrqrafp cpdcgqsfrl
      361 kinltihqrt hveegrqeap grsptscgds qamlepgevv vpgpvirwlp eepegrrsva
      421 ggralvgrrp aaskmyhcse clrffqqrks lllhqrlhtg ngqgwpacpy cgkafrrpsd
      481 lfrhqrihtg erpyqcpqcg rtfnrnhhla vhmqthargq vgphfpaapa rhgslplpwp
      541 srkeeg
//
LOCUS       NP_002088                365 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor IIIA [Homo sapiens].
ACCESSION   NP_002088 XP_001715675 XP_001717003 XP_001717693
VERSION     NP_002088.2
DBSOURCE    REFSEQ: accession NM_002097.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Anuraga,G., Tang,W.C., Phan,N.N., Ta,H.D.K., Liu,Y.H., Wu,Y.F.,
            Lee,K.H. and Wang,C.Y.
  TITLE     Comprehensive Analysis of Prognostic and Genetic Signatures for
            General Transcription Factor III (GTF3) in Clinical Colorectal
            Cancer Patients Using Bioinformatics Approaches
  JOURNAL   Curr Issues Mol Biol 43 (1), 2-20 (2021)
   PUBMED   33925358
  REMARK    GeneRIF: Comprehensive Analysis of Prognostic and Genetic
            Signatures for General Transcription Factor III (GTF3) in Clinical
            Colorectal Cancer Patients Using Bioinformatics Approaches.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Sloan,K.E., Bohnsack,M.T. and Watkins,N.J.
  TITLE     The 5S RNP couples p53 homeostasis to ribosome biogenesis and
            nucleolar stress
  JOURNAL   Cell Rep 5 (1), 237-247 (2013)
   PUBMED   24120868
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Speliotes,E.K., Willer,C.J., Berndt,S.I., Monda,K.L.,
            Thorleifsson,G., Jackson,A.U., Lango Allen,H., Lindgren,C.M.,
            Luan,J., Magi,R., Randall,J.C., Vedantam,S., Winkler,T.W., Qi,L.,
            Workalemahu,T., Heid,I.M., Steinthorsdottir,V., Stringham,H.M.,
            Weedon,M.N., Wheeler,E., Wood,A.R., Ferreira,T., Weyant,R.J.,
            Segre,A.V., Estrada,K., Liang,L., Nemesh,J., Park,J.H.,
            Gustafsson,S., Kilpelainen,T.O., Yang,J., Bouatia-Naji,N., Esko,T.,
            Feitosa,M.F., Kutalik,Z., Mangino,M., Raychaudhuri,S., Scherag,A.,
            Smith,A.V., Welch,R., Zhao,J.H., Aben,K.K., Absher,D.M., Amin,N.,
            Dixon,A.L., Fisher,E., Glazer,N.L., Goddard,M.E., Heard-Costa,N.L.,
            Hoesel,V., Hottenga,J.J., Johansson,A., Johnson,T., Ketkar,S.,
            Lamina,C., Li,S., Moffatt,M.F., Myers,R.H., Narisu,N., Perry,J.R.,
            Peters,M.J., Preuss,M., Ripatti,S., Rivadeneira,F., Sandholt,C.,
            Scott,L.J., Timpson,N.J., Tyrer,J.P., van Wingerden,S.,
            Watanabe,R.M., White,C.C., Wiklund,F., Barlassina,C., Chasman,D.I.,
            Cooper,M.N., Jansson,J.O., Lawrence,R.W., Pellikka,N.,
            Prokopenko,I., Shi,J., Thiering,E., Alavere,H., Alibrandi,M.T.,
            Almgren,P., Arnold,A.M., Aspelund,T., Atwood,L.D., Balkau,B.,
            Balmforth,A.J., Bennett,A.J., Ben-Shlomo,Y., Bergman,R.N.,
            Bergmann,S., Biebermann,H., Blakemore,A.I., Boes,T.,
            Bonnycastle,L.L., Bornstein,S.R., Brown,M.J., Buchanan,T.A.,
            Busonero,F., Campbell,H., Cappuccio,F.P., Cavalcanti-Proenca,C.,
            Chen,Y.D., Chen,C.M., Chines,P.S., Clarke,R., Coin,L., Connell,J.,
            Day,I.N., den Heijer,M., Duan,J., Ebrahim,S., Elliott,P.,
            Elosua,R., Eiriksdottir,G., Erdos,M.R., Eriksson,J.G.,
            Facheris,M.F., Felix,S.B., Fischer-Posovszky,P., Folsom,A.R.,
            Friedrich,N., Freimer,N.B., Fu,M., Gaget,S., Gejman,P.V.,
            Geus,E.J., Gieger,C., Gjesing,A.P., Goel,A., Goyette,P.,
            Grallert,H., Grassler,J., Greenawalt,D.M., Groves,C.J.,
            Gudnason,V., Guiducci,C., Hartikainen,A.L., Hassanali,N.,
            Hall,A.S., Havulinna,A.S., Hayward,C., Heath,A.C., Hengstenberg,C.,
            Hicks,A.A., Hinney,A., Hofman,A., Homuth,G., Hui,J., Igl,W.,
            Iribarren,C., Isomaa,B., Jacobs,K.B., Jarick,I., Jewell,E.,
            John,U., Jorgensen,T., Jousilahti,P., Jula,A., Kaakinen,M.,
            Kajantie,E., Kaplan,L.M., Kathiresan,S., Kettunen,J., Kinnunen,L.,
            Knowles,J.W., Kolcic,I., Konig,I.R., Koskinen,S., Kovacs,P.,
            Kuusisto,J., Kraft,P., Kvaloy,K., Laitinen,J., Lantieri,O.,
            Lanzani,C., Launer,L.J., Lecoeur,C., Lehtimaki,T., Lettre,G.,
            Liu,J., Lokki,M.L., Lorentzon,M., Luben,R.N., Ludwig,B.,
            Manunta,P., Marek,D., Marre,M., Martin,N.G., McArdle,W.L.,
            McCarthy,A., McKnight,B., Meitinger,T., Melander,O., Meyre,D.,
            Midthjell,K., Montgomery,G.W., Morken,M.A., Morris,A.P., Mulic,R.,
            Ngwa,J.S., Nelis,M., Neville,M.J., Nyholt,D.R., O'Donnell,C.J.,
            O'Rahilly,S., Ong,K.K., Oostra,B., Pare,G., Parker,A.N., Perola,M.,
            Pichler,I., Pietilainen,K.H., Platou,C.G., Polasek,O., Pouta,A.,
            Rafelt,S., Raitakari,O., Rayner,N.W., Ridderstrale,M., Rief,W.,
            Ruokonen,A., Robertson,N.R., Rzehak,P., Salomaa,V., Sanders,A.R.,
            Sandhu,M.S., Sanna,S., Saramies,J., Savolainen,M.J., Scherag,S.,
            Schipf,S., Schreiber,S., Schunkert,H., Silander,K., Sinisalo,J.,
            Siscovick,D.S., Smit,J.H., Soranzo,N., Sovio,U., Stephens,J.,
            Surakka,I., Swift,A.J., Tammesoo,M.L., Tardif,J.C.,
            Teder-Laving,M., Teslovich,T.M., Thompson,J.R., Thomson,B.,
            Tonjes,A., Tuomi,T., van Meurs,J.B., van Ommen,G.J., Vatin,V.,
            Viikari,J., Visvikis-Siest,S., Vitart,V., Vogel,C.I., Voight,B.F.,
            Waite,L.L., Wallaschofski,H., Walters,G.B., Widen,E., Wiegand,S.,
            Wild,S.H., Willemsen,G., Witte,D.R., Witteman,J.C., Xu,J.,
            Zhang,Q., Zgaga,L., Ziegler,A., Zitting,P., Beilby,J.P.,
            Farooqi,I.S., Hebebrand,J., Huikuri,H.V., James,A.L., Kahonen,M.,
            Levinson,D.F., Macciardi,F., Nieminen,M.S., Ohlsson,C.,
            Palmer,L.J., Ridker,P.M., Stumvoll,M., Beckmann,J.S., Boeing,H.,
            Boerwinkle,E., Boomsma,D.I., Caulfield,M.J., Chanock,S.J.,
            Collins,F.S., Cupples,L.A., Smith,G.D., Erdmann,J., Froguel,P.,
            Gronberg,H., Gyllensten,U., Hall,P., Hansen,T., Harris,T.B.,
            Hattersley,A.T., Hayes,R.B., Heinrich,J., Hu,F.B., Hveem,K.,
            Illig,T., Jarvelin,M.R., Kaprio,J., Karpe,F., Khaw,K.T.,
            Kiemeney,L.A., Krude,H., Laakso,M., Lawlor,D.A., Metspalu,A.,
            Munroe,P.B., Ouwehand,W.H., Pedersen,O., Penninx,B.W., Peters,A.,
            Pramstaller,P.P., Quertermous,T., Reinehr,T., Rissanen,A.,
            Rudan,I., Samani,N.J., Schwarz,P.E., Shuldiner,A.R., Spector,T.D.,
            Tuomilehto,J., Uda,M., Uitterlinden,A., Valle,T.T., Wabitsch,M.,
            Waeber,G., Wareham,N.J., Watkins,H., Wilson,J.F., Wright,A.F.,
            Zillikens,M.C., Chatterjee,N., McCarroll,S.A., Purcell,S.,
            Schadt,E.E., Visscher,P.M., Assimes,T.L., Borecki,I.B.,
            Deloukas,P., Fox,C.S., Groop,L.C., Haritunians,T., Hunter,D.J.,
            Kaplan,R.C., Mohlke,K.L., O'Connell,J.R., Peltonen,L.,
            Schlessinger,D., Strachan,D.P., van Duijn,C.M., Wichmann,H.E.,
            Frayling,T.M., Thorsteinsdottir,U., Abecasis,G.R., Barroso,I.,
            Boehnke,M., Stefansson,K., North,K.E., McCarthy,M.I.,
            Hirschhorn,J.N., Ingelsson,E. and Loos,R.J.
  CONSRTM   MAGIC; Procardis Consortium
  TITLE     Association analyses of 249,796 individuals reveal 18 new loci
            associated with body mass index
  JOURNAL   Nat Genet 42 (11), 937-948 (2010)
   PUBMED   20935630
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Weser,S., Riemann,J., Seifart,K.H. and Meissner,W.
  TITLE     Assembly and isolation of intermediate steps of transcription
            complexes formed on the human 5S rRNA gene
  JOURNAL   Nucleic Acids Res 31 (9), 2408-2416 (2003)
   PUBMED   12711686
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Fridell,R.A., Fischer,U., Luhrmann,R., Meyer,B.E., Meinkoth,J.L.,
            Malim,M.H. and Cullen,B.R.
  TITLE     Amphibian transcription factor IIIA proteins contain a sequence
            element functionally equivalent to the nuclear export signal of
            human immunodeficiency virus type 1 Rev
  JOURNAL   Proc Natl Acad Sci U S A 93 (7), 2936-2940 (1996)
   PUBMED   8610146
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Drew,P.D., Nagle,J.W., Canning,R.D., Ozato,K., Biddison,W.E. and
            Becker,K.G.
  TITLE     Cloning and expression analysis of a human cDNA homologous to
            Xenopus TFIIIA
  JOURNAL   Gene 159 (2), 215-218 (1995)
   PUBMED   7622052
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Arakawa,H., Nagase,H., Hayashi,N., Ogawa,M., Nagata,M.,
            Fujiwara,T., Takahashi,E., Shin,S. and Nakamura,Y.
  TITLE     Molecular cloning, characterization, and chromosomal mapping of a
            novel human gene (GTF3A) that is highly homologous to Xenopus
            transcription factor IIIA
  JOURNAL   Cytogenet Cell Genet 70 (3-4), 235-238 (1995)
   PUBMED   7789179
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Moorefield,B. and Roeder,R.G.
  TITLE     Purification and characterization of human transcription factor
            IIIA
  JOURNAL   J Biol Chem 269 (33), 20857-20865 (1994)
   PUBMED   8063702
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Seifart,K.H., Wang,L., Waldschmidt,R., Jahn,D. and Wingender,E.
  TITLE     Purification of human transcription factor IIIA and its interaction
            with a chemically synthesized gene encoding human 5 S rRNA
  JOURNAL   J Biol Chem 264 (3), 1702-1709 (1989)
   PUBMED   2912980
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D32257.1, BP254755.1, U20272.1,
            AW627732.1 and AL137059.20.
            
            On or before Mar 29, 2008 this sequence version replaced
            XP_001717003.1, XP_001715675.1, XP_001717693.1, NP_002088.1.
            
            Summary: The product of this gene is a zinc finger protein with
            nine Cis[2]-His[2] zinc finger domains. It functions as an RNA
            polymerase III transcription factor to induce transcription of the
            5S rRNA genes. The protein binds to a 50 bp internal promoter in
            the 5S genes called the internal control region (ICR), and
            nucleates formation of a stable preinitiation complex. This complex
            recruits the TFIIIC and TFIIIB transcription factors and RNA
            polymerase III to form the complete transcription complex. The
            protein is thought to be translated using a non-AUG translation
            initiation site in mammals based on sequence analysis, protein
            homology, and the size of the purified protein. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.289034.1,
                                           SRR3476690.656735.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match       :: ENST00000381140.10/ ENSP00000370532.5
            non-AUG initiation codon :: inferred from conservation
            RefSeq Select criteria   :: based on single protein-coding
                                        transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.2"
     Protein         1..365
                     /product="transcription factor IIIA"
                     /calculated_mol_wt=41384
     Region          42..64
                     /region_name="zinc finger"
     Region          45..64
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(49,51,53,55..56,59..60,63,79,81,85..86,89..90,93,
                     109,111,113,115..116,119..120)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <64..187
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          72..94
                     /region_name="zinc finger"
     Region          72..94
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          102..125
                     /region_name="zinc finger"
     Region          102..120
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          134..156
                     /region_name="zinc finger"
     Region          137..156
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(141,143,145,147..148,151..152,155,171,173,177..178,
                     181..182,185,224,226,228,230..231,234..235,238)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          164..186
                     /region_name="zinc finger"
     Region          164..186
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          191..213
                     /region_name="zinc finger"
     Region          219..239
                     /region_name="zinc finger"
     Region          219..239
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          246..271
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          248..271
                     /region_name="zinc finger"
     Region          279..301
                     /region_name="zinc finger"
     Region          279..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..365
                     /gene="GTF3A"
                     /gene_synonym="AP2; TFIIIA"
                     /coded_by="NM_002097.3:120..1217"
                     /note="non-AUG (CUG) translation initiation codon"
                     /db_xref="CCDS:CCDS45019.1"
                     /db_xref="GeneID:2971"
                     /db_xref="HGNC:HGNC:4662"
                     /db_xref="MIM:600860"
ORIGIN      
        1 mdppavvaes vssltiadaf iaagessapt pprpalprrf icsfpdcsan yskawkldah
       61 lckhtgerpf vcdyegcgka firdyhlsrh ilthtgekpf vcaangcdqk fntksnlkkh
      121 ferkhenqqk qyicsfedck ktfkkhqqlk ihqcqhtnep lfkctqegcg khfaspsklk
      181 rhakahegyv cqkgcsfvak twtellkhvr ethkeeilce vcrktfkrkd ylkqhmktha
      241 perdvcrcpr egcgrtyttv fnlqshilsf heesrpfvce hagcgktfam kqsltrhavv
      301 hdpdkkkmkl kvkksrekrs lashlsgyip pkrkqgqgls lcqngespnc vedkmlstva
      361 vltlg
//
LOCUS       NP_001347742              89 aa            linear   ROD 27-APR-2025
DEFINITION  ergosterol biosynthetic protein 28 homolog isoform 2 [Mus
            musculus].
ACCESSION   NP_001347742
VERSION     NP_001347742.1
DBSOURCE    REFSEQ: accession NM_001360813.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Easterday,M.C., Dougherty,J.D., Jackson,R.L., Ou,J., Nakano,I.,
            Paucar,A.A., Roobini,B., Dianati,M., Irvin,D.K., Weissman,I.L.,
            Terskikh,A.V., Geschwind,D.H. and Kornblum,H.I.
  TITLE     Neural progenitor genes. Germinal zone expression and analysis of
            genetic overlap in stem cell populations
  JOURNAL   Dev Biol 264 (2), 309-322 (2003)
   PUBMED   14651920
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Nelson,P.S., Pritchard,C., Abbott,D. and Clegg,N.
  TITLE     The human (PEDB) and mouse (mPEDB) Prostate Expression Databases
  JOURNAL   Nucleic Acids Res 30 (1), 218-220 (2002)
   PUBMED   11752298
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Ottolenghi,C., Daizadeh,I., Ju,A., Kossida,S., Renault,G.,
            Jacquet,M., Fellous,A., Gilbert,W. and Veitia,R.
  TITLE     The genomic structure of c14orf1 is conserved across eukarya
  JOURNAL   Mamm Genome 11 (9), 786-788 (2000)
   PUBMED   10967139
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138303.4, BE656456.1 and AI851047.1.
            
            Transcript Variant: This variant (4) uses an alternate 3' terminal
            exon, compared to variant 1. The encoded isoform (2) is shorter and
            has a distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF906466.1, CJ070716.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 39.81 cM"
     Protein         1..89
                     /product="ergosterol biosynthetic protein 28 homolog
                     isoform 2"
                     /note="probable ergosterol biosynthetic protein 28;
                     c14orf1-like protein; ergosterol biosynthetic protein 28
                     homolog"
                     /calculated_mol_wt=10260
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERY9.1)"
     Region          8..>75
                     /region_name="Erg28"
                     /note="Erg28 like protein; pfam03694"
                     /db_xref="CDD:461015"
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERY9.1)"
     CDS             1..89
                     /gene="Erg28"
                     /gene_synonym="0610007P14Rik; 1190004E09Rik; ORF11"
                     /coded_by="NM_001360813.1:452..721"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:58520"
                     /db_xref="MGI:MGI:1915571"
ORIGIN      
        1 msrflnvlrs wlvmvsiiam gntlqsfrdh tflyeklytg kpnlvnglqa rtfgiwtlls
       61 svirclcaid ihnktyvrer rplvsvcwq
//
LOCUS       NP_005223                976 aa            linear   PRI 27-APR-2025
DEFINITION  ephrin type-A receptor 1 precursor [Homo sapiens].
ACCESSION   NP_005223
VERSION     NP_005223.4
DBSOURCE    REFSEQ: accession NM_005232.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Owens,H.A., Thorburn,L.E., Walsby,E., Moon,O.R., Rizkallah,P.,
            Sherwani,S., Tinsley,C.L., Rogers,L., Cerutti,C., Ridley,A.J.,
            Williams,J., Knauper,V. and Ager,A.
  TITLE     Alzheimer's disease-associated P460L variant of EphA1 dysregulates
            receptor activity and blood-brain barrier function
  JOURNAL   Alzheimers Dement 20 (3), 2016-2033 (2024)
   PUBMED   38184788
  REMARK    GeneRIF: Alzheimer's disease-associated P460L variant of EphA1
            dysregulates receptor activity and blood-brain barrier function.
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Shin,J.M., Han,M.S., Park,J.H., Lee,S.H., Kim,T.H. and Lee,S.H.
  TITLE     The EphA1 and EphA2 Signaling Modulates the Epithelial Permeability
            in Human Sinonasal Epithelial Cells and the Rhinovirus Infection
            Induces Epithelial Barrier Dysfunction via EphA2 Receptor Signaling
  JOURNAL   Int J Mol Sci 24 (4), 3629 (2023)
   PUBMED   36835041
  REMARK    GeneRIF: The EphA1 and EphA2 Signaling Modulates the Epithelial
            Permeability in Human Sinonasal Epithelial Cells and the Rhinovirus
            Infection Induces Epithelial Barrier Dysfunction via EphA2 Receptor
            Signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 976)
  AUTHORS   LaCombe,R., Cecchini,A., Seibert,M. and Cornelison,D.
  TITLE     EphA1 receptor tyrosine kinase is localized to the nucleus in
            rhabdomyosarcoma from multiple species
  JOURNAL   Biol Open 11 (10) (2022)
   PUBMED   36214254
  REMARK    GeneRIF: EphA1 receptor tyrosine kinase is localized to the nucleus
            in rhabdomyosarcoma from multiple species.
REFERENCE   4  (residues 1 to 976)
  AUTHORS   Dai,B.Q. and Zhang,X.
  TITLE     SOCS2 affects the proliferation, migration and invasion of
            nasopharyngeal carcinoma cells via regulating EphA1
  JOURNAL   Neoplasma 67 (4), 794-801 (2020)
   PUBMED   32266818
  REMARK    GeneRIF: SOCS2 affects the proliferation, migration and invasion of
            nasopharyngeal carcinoma cells via regulating EphA1.
REFERENCE   5  (residues 1 to 976)
  AUTHORS   Nagare,R.P., Sneha,S., Sidhanth,C., Roopa,S., Murhekar,K.,
            Shirley,S., Swaminathan,R., Sridevi,V. and Ganesan,T.S.
  TITLE     Expression of cancer stem cell markers CD24, EPHA1 and CD9 and
            their correlation with clinical outcome in epithelial ovarian
            tumours
  JOURNAL   Cancer Biomark 28 (3), 397-408 (2020)
   PUBMED   32224528
  REMARK    GeneRIF: Expression of cancer stem cell markers CD24, EPHA1 and CD9
            and their correlation with clinical outcome in epithelial ovarian
            tumours.
REFERENCE   6  (residues 1 to 976)
  AUTHORS   Holder,N. and Klein,R.
  TITLE     Eph receptors and ephrins: effectors of morphogenesis
  JOURNAL   Development 126 (10), 2033-2044 (1999)
   PUBMED   10207129
  REMARK    Review article
REFERENCE   7  (residues 1 to 976)
  AUTHORS   Zhou,R.
  TITLE     The Eph family receptors and ligands
  JOURNAL   Pharmacol Ther 77 (3), 151-181 (1998)
   PUBMED   9576626
  REMARK    Review article
REFERENCE   8  (residues 1 to 976)
  AUTHORS   Flanagan,J.G. and Vanderhaeghen,P.
  TITLE     The ephrins and Eph receptors in neural development
  JOURNAL   Annu Rev Neurosci 21, 309-345 (1998)
   PUBMED   9530499
  REMARK    Review article
REFERENCE   9  (residues 1 to 976)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   10 (residues 1 to 976)
  AUTHORS   Hirai,H., Maru,Y., Hagiwara,K., Nishida,J. and Takaku,F.
  TITLE     A novel putative tyrosine kinase receptor encoded by the eph gene
  JOURNAL   Science 238 (4834), 1717-1720 (1987)
   PUBMED   2825356
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC130291.1, EU826605.1,
            CN289901.1 and AI057542.1.
            
            On Jan 24, 2009 this sequence version replaced NP_005223.3.
            
            Summary: This gene belongs to the ephrin receptor subfamily of the
            protein-tyrosine kinase family. EPH and EPH-related receptors have
            been implicated in mediating developmental events, particularly in
            the nervous system. Receptors in the EPH subfamily typically have a
            single kinase domain and an extracellular region containing a
            Cys-rich domain and 2 fibronectin type III repeats. The ephrin
            receptors are divided into 2 groups based on the similarity of
            their extracellular domain sequences and their affinities for
            binding ephrin-A and ephrin-B ligands. This gene is expressed in
            some human cancer cell lines and has been implicated in
            carcinogenesis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290351.1, M18391.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000275815.4/ ENSP00000275815.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q34-q35"
     Protein         1..976
                     /product="ephrin type-A receptor 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="erythropoietin-producing hepatoma amplified
                     sequence; ephrin type-A receptor 1; tyrosine-protein
                     kinase receptor EPH; oncogene EPH; eph tyrosine kinase 1;
                     hEpha1; erythropoietin-producing hepatoma receptor"
                     /calculated_mol_wt=105445
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2700
     Region          27..203
                     /region_name="EphR_LBD_A1"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 1;
                     cd10479"
                     /db_xref="CDD:198447"
     Site            order(52,54..58,64..65,67,69,102,104,109..110,154,
                     158..159,162..164,191..193,195)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198447"
     Site            order(333,411,430)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          334..431
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            414
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21709.4)"
     Site            order(431..432,434..435)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          453..535
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(524..525,527..528)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            548..568
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21709.4)"
     Region          <586..621
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21709.4)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21709.4)"
     Region          619..884
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(630..633,636,638,654,656,686,702..705,749,753..754,
                     756,766..767)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            781
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21709.4)"
     Site            906
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P21709.4)"
     Site            910
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P21709.4)"
     Region          912..974
                     /region_name="SAM_EPH-A1"
                     /note="SAM domain of EPH-A1 subfamily of tyrosine kinase
                     receptors; cd09542"
                     /db_xref="CDD:188941"
     Site            order(930,963)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188941"
     Site            930
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21709.4)"
     Region          974..976
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P21709.4)"
     CDS             1..976
                     /gene="EPHA1"
                     /gene_synonym="EPH; EPHT; EPHT1"
                     /coded_by="NM_005232.5:52..2982"
                     /db_xref="CCDS:CCDS5884.1"
                     /db_xref="GeneID:2041"
                     /db_xref="HGNC:HGNC:3385"
                     /db_xref="MIM:179610"
ORIGIN      
        1 merrwplglg lvlllcaplp pgarakevtl mdtskaqgel gwlldppkdg wseqqqilng
       61 tplymyqdcp mqgrrdtdhw lrsnwiyrge easrvhvelq ftvrdcksfp ggagplgcke
      121 tfnllymesd qdvgiqlrrp lfqkvttvaa dqsftirdlv sgsvklnver cslgrltrrg
      181 lylafhnpga cvalvsvrvf yqrcpetlng laqfpdtlpg paglvevagt clpharaspr
      241 psgaprmhcs pdgewlvpvg rchcepgyee ggsgeacvac psgsyrmdmd tphcltcpqq
      301 staesegati ctcesghyra pgegpqvact gppsaprnls fsasgtqlsl rweppadtgg
      361 rqdvrysvrc sqcqgtaqdg gpcqpcgvgv hfspgarglt tpavhvngle pyanytfnve
      421 aqngvsglgs sghastsvsi smghaeslsg lslrlvkkep rqleltwags rprspganlt
      481 yelhvlnqde eryqmvlepr vlltelqpdt tyivrvrmlt plgpgpfspd hefrtsppvs
      541 rgltggeiva vifglllgaa lllgilvfrs rraqrqrqqr qrdratdvdr edklwlkpyv
      601 dlqayedpaq galdftreld pawlmvdtvi gegefgevyr gtlrlpsqdc ktvaiktlkd
      661 tspggqwwnf lreatimgqf shphilhleg vvtkrkpimi itefmengal daflreredq
      721 lvpgqlvaml qgiasgmnyl snhnyvhrdl aarnilvnqn lcckvsdfgl trllddfdgt
      781 yetqggkipi rwtapeaiah rifttasdvw sfgivmwevl sfgdkpygem snqevmksie
      841 dgyrlpppvd cpaplyelmk ncwaydrarr phfqklqahl eqllanphsl rtianfdprm
      901 tlrlpslsgs dgipyrtvse wlesirmkry ilhfhsagld tmecvlelta edltqmgitl
      961 pghqkrilcs iqgfkd
//
LOCUS       NP_001106795             123 aa            linear   PRI 27-APR-2025
DEFINITION  CST complex subunit TEN1 [Homo sapiens].
ACCESSION   NP_001106795
VERSION     NP_001106795.2
DBSOURCE    REFSEQ: accession NM_001113324.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Takai,H., Aria,V., Borges,P., Yeeles,J.T.P. and de Lange,T.
  TITLE     CST-polymerase alpha-primase solves a second telomere
            end-replication problem
  JOURNAL   Nature 627 (8004), 664-670 (2024)
   PUBMED   38418884
  REMARK    GeneRIF: CST-polymerase alpha-primase solves a second telomere
            end-replication problem.
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Zaug,A.J., Goodrich,K.J., Song,J.J., Sullivan,A.E. and Cech,T.R.
  TITLE     Reconstitution of a telomeric replicon organized by CST
  JOURNAL   Nature 608 (7924), 819-825 (2022)
   PUBMED   35831508
  REMARK    GeneRIF: Reconstitution of a telomeric replicon organized by CST.
REFERENCE   3  (residues 1 to 123)
  AUTHORS   He,Q., Lin,X., Chavez,B.L., Agrawal,S., Lusk,B.L. and Lim,C.J.
  TITLE     Structures of the human CST-Polalpha-primase complex bound to
            telomere templates
  JOURNAL   Nature 608 (7924), 826-832 (2022)
   PUBMED   35830881
  REMARK    GeneRIF: Structures of the human CST-Polalpha-primase complex bound
            to telomere templates.
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Dos Santos,G.A., Viana,N.I., Pimenta,R., de Camargo,J.A.,
            Guimaraes,V.R., Romao,P., Candido,P., Ghazarian,V., Reis,S.T.,
            Leite,K.R.M. and Srougi,M.
  TITLE     Pan-cancer analysis reveals that CTC1-STN1-TEN1 (CST) complex may
            have a key position in oncology
  JOURNAL   Cancer Genet 262-263, 80-90 (2022)
   PUBMED   35134616
  REMARK    GeneRIF: Pan-cancer analysis reveals that CTC1-STN1-TEN1 (CST)
            complex may have a key position in oncology.
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Kasbek,C., Wang,F. and Price,C.M.
  TITLE     Human TEN1 maintains telomere integrity and functions in
            genome-wide replication restart
  JOURNAL   J Biol Chem 288 (42), 30139-30150 (2013)
   PUBMED   24025336
  REMARK    GeneRIF: TEN1 likely functions in conjunction with CTC1 and STN1 at
            the telomere and elsewhere in the genome.
REFERENCE   7  (residues 1 to 123)
  AUTHORS   Chen,L.Y. and Lingner,J.
  TITLE     CST for the grand finale of telomere replication
  JOURNAL   Nucleus 4 (4), 277-282 (2013)
   PUBMED   23851344
  REMARK    GeneRIF: The mammalian CST (CTC1-STN1-TEN1) complex is directly
            involved at several stages of telomere end formation and CST seems
            to play critical roles in coordinating telomerase elongation and
            fill-in synthesis to complete telomere replication.
REFERENCE   8  (residues 1 to 123)
  AUTHORS   Bryan,C., Rice,C., Harkisheimer,M., Schultz,D.C. and Skordalakes,E.
  TITLE     Structure of the human telomeric Stn1-Ten1 capping complex
  JOURNAL   PLoS One 8 (6), e66756 (2013)
   PUBMED   23826127
  REMARK    GeneRIF: data indicate that hTen1 is critical for the telomeric
            function of hCST, both in telomere protection and downregulation of
            telomerase function
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 123)
  AUTHORS   Chen,L.Y., Redon,S. and Lingner,J.
  TITLE     The human CST complex is a terminator of telomerase activity
  JOURNAL   Nature 488 (7412), 540-544 (2012)
   PUBMED   22763445
  REMARK    GeneRIF: the human CST (CTC1, STN1 and TEN1) complex, previously
            implicated in telomere protection and DNA metabolism, inhibits
            telomerase activity through primer sequestration and physical
            interaction with the protection of telomeres 1 (POT1)-TPP1
            telomerase processivity factor
REFERENCE   10 (residues 1 to 123)
  AUTHORS   Miyake,Y., Nakamura,M., Nabetani,A., Shimamura,S., Tamura,M.,
            Yonehara,S., Saito,M. and Ishikawa,F.
  TITLE     RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded
            DNA and protects telomeres independently of the Pot1 pathway
  JOURNAL   Mol Cell 36 (2), 193-206 (2009)
   PUBMED   19854130
  REMARK    GeneRIF: Ctc1-Stn1-Ten1 is a replication protein A (RPA)-like
            complex that is not directly involved in conventional DNA
            replication at forks but plays a role in DNA metabolism frequently
            required by telomeres.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC047782.1.
            
            On Jan 22, 2011 this sequence version replaced NP_001106795.1.
            
            Summary: C17ORF106, or TEN1, appears to function in a
            telomere-associated complex with STN1 (OBFC1; MIM 613128) and CTC1
            (C17ORF68; MIM 613129) (Miyake et al., 2009 [PubMed
            19854130]).[supplied by OMIM, Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047782.1, SRR1163655.70280.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397640.6/ ENSP00000380762.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..123
                     /product="CST complex subunit TEN1"
                     /note="telomeric pathways in association with Stn1, number
                     1; protein telomeric pathways with STN1 homolog; telomere
                     length regulation protein TEN1 homolog; TEN1 telomerase
                     capping complex subunit homolog; TEN1, CST complex
                     subunit"
                     /calculated_mol_wt=13725
     Region          3..119
                     /region_name="Ten1_2"
                     /note="Telomere-capping, CST complex subunit; pfam15490"
                     /db_xref="CDD:464745"
     CDS             1..123
                     /gene="TEN1"
                     /gene_synonym="C17orf106"
                     /coded_by="NM_001113324.3:279..650"
                     /db_xref="CCDS:CCDS45780.2"
                     /db_xref="GeneID:100134934"
                     /db_xref="HGNC:HGNC:37242"
                     /db_xref="MIM:613130"
ORIGIN      
        1 mmlpkpgtyy lpwevsagqv pdgstlrtfg rlclydmiqs rvtlmaqhgs dqhqvlvctk
       61 lvepfhaqvg slyivlgelq hqqdrgsvvk arvltcvegm nlplleqair eqrlykqerg
      121 gsq
//
LOCUS       NP_006579                302 aa            linear   PRI 27-APR-2025
DEFINITION  sulfotransferase 1C4 isoform 1 [Homo sapiens].
ACCESSION   NP_006579
VERSION     NP_006579.2
DBSOURCE    REFSEQ: accession NM_006588.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Jiang,L., Xu,F., Li,C., Liu,T., Zhao,Q., Liu,Y., Zhao,Y., Li,Y.,
            Zhang,Z., Tang,X. and Zhang,J.
  TITLE     Sulfotransferase 1C2 promotes hepatocellular carcinoma progression
            by enhancing glycolysis and fatty acid metabolism
  JOURNAL   Cancer Med 12 (9), 10738-10754 (2023)
   PUBMED   36880364
  REMARK    GeneRIF: Sulfotransferase 1C2 promotes hepatocellular carcinoma
            progression by enhancing glycolysis and fatty acid metabolism.
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Mei,X., Gohal,S.A., Zhou,C.Y. and Liu,M.C.
  TITLE     Sulfation of hyperoside by the human cytosolic sulfotransferases
            (SULTs): impact of genetic polymorphisms on hyperoside-sulfating
            activity of SULT1C4 allozymes
  JOURNAL   J Asian Nat Prod Res 25 (1), 75-84 (2023)
   PUBMED   35249434
  REMARK    GeneRIF: Sulfation of hyperoside by the human cytosolic
            sulfotransferases (SULTs): impact of genetic polymorphisms on
            hyperoside-sulfating activity of SULT1C4 allozymes.
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Dubaisi,S., Fang,H., Caruso,J.A., Gaedigk,R., Vyhlidal,C.A.,
            Kocarek,T.A. and Runge-Morris,M.
  TITLE     Developmental Expression of SULT1C4 Transcript Variants in Human
            Liver: Implications for Discordance Between SULT1C4 mRNA and
            Protein Levels
  JOURNAL   Drug Metab Dispos 48 (6), 515-520 (2020)
   PUBMED   32303576
  REMARK    GeneRIF: Developmental Expression of SULT1C4 Transcript Variants in
            Human Liver: Implications for Discordance Between SULT1C4 mRNA and
            Protein Levels.
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Guidry,A.L., Tibbs,Z.E., Runge-Morris,M. and Falany,C.N.
  TITLE     Expression, purification and characterization of human cytosolic
            sulfotransferase (SULT) 1C4
  JOURNAL   Horm Mol Biol Clin Investig 29 (1), 27-36 (2017)
   PUBMED   28222028
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Luo,L., Zhou,C., Hui,Y., Kurogi,K., Sakakibara,Y., Suiko,M. and
            Liu,M.C.
  TITLE     Human cytosolic sulfotransferase SULT1C4 mediates the sulfation of
            doxorubicin and epirubicin
  JOURNAL   Drug Metab Pharmacokinet 31 (2), 163-166 (2016)
   PUBMED   26948952
  REMARK    GeneRIF: The current study aimed to identify the human cytosolic
            sulfotransferase(s) that is(are) capable of sulfating doxorubicin
            and its analog epirubicin, and to verify whether sulfation of
            doxorubicin and epirubicin may occur under metabolic conditions.
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Glatt,H.
  TITLE     Sulfotransferases in the bioactivation of xenobiotics
  JOURNAL   Chem Biol Interact 129 (1-2), 141-170 (2000)
   PUBMED   11154739
  REMARK    Review article
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Freimuth,R.R., Raftogianis,R.B., Wood,T.C., Moon,E., Kim,U.J.,
            Xu,J., Siciliano,M.J. and Weinshilboum,R.M.
  TITLE     Human sulfotransferases SULT1C1 and SULT1C2: cDNA characterization,
            gene cloning, and chromosomal localization
  JOURNAL   Genomics 65 (2), 157-165 (2000)
   PUBMED   10783263
REFERENCE   8  (residues 1 to 302)
  AUTHORS   Glatt,H., Engelke,C.E., Pabel,U., Teubner,W., Jones,A.L.,
            Coughtrie,M.W., Andrae,U., Falany,C.N. and Meinl,W.
  TITLE     Sulfotransferases: genetics and role in toxicology
  JOURNAL   Toxicol Lett 112-113, 341-348 (2000)
   PUBMED   10720750
  REMARK    Review article
REFERENCE   9  (residues 1 to 302)
  AUTHORS   Sakakibara,Y., Yanagisawa,K., Katafuchi,J., Ringer,D.P., Takami,Y.,
            Nakayama,T., Suiko,M. and Liu,M.C.
  TITLE     Molecular cloning, expression, and characterization of novel human
            SULT1C sulfotransferases that catalyze the sulfonation of
            N-hydroxy-2-acetylaminofluorene
  JOURNAL   J Biol Chem 273 (51), 33929-33935 (1998)
   PUBMED   9852044
REFERENCE   10 (residues 1 to 302)
  AUTHORS   Weinshilboum,R.M., Otterness,D.M., Aksoy,I.A., Wood,T.C., Her,C.
            and Raftogianis,R.B.
  TITLE     Sulfation and sulfotransferases 1: Sulfotransferase molecular
            biology: cDNAs and genes
  JOURNAL   FASEB J 11 (1), 3-14 (1997)
   PUBMED   9034160
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068941.7 and BC125043.1.
            
            On Mar 4, 2003 this sequence version replaced NP_006579.1.
            
            Summary: Sulfotransferase enzymes catalyze the sulfate conjugation
            of many hormones, neurotransmitters, drugs, and xenobiotic
            compounds. These cytosolic enzymes are different in their tissue
            distributions and substrate specificities. The gene structure
            (number and length of exons) is similar among family members. This
            gene encodes a protein that belongs to the SULT1 subfamily,
            responsible for transferring a sulfo moiety from PAPS to
            phenol-containing compounds. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments, including
            RNA-seq data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.264815.1,
                                           SRR1803616.413212.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000272452.7/ ENSP00000272452.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.3"
     Protein         1..302
                     /product="sulfotransferase 1C4 isoform 1"
                     /EC_number="2.8.2.1"
                     /note="sulfotransferase family, cytosolic, 1C, member C2;
                     sulfotransferase family, cytosolic, 1C, member 2;
                     sulfotransferase 1C4; sulfotransferase 1C2; ST1C4;
                     SULT1C#2; sulfotransferase family, cytosolic, 1C, member
                     4"
                     /calculated_mol_wt=35389
     Region          45..294
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; pfam00685"
                     /db_xref="CDD:425820"
     CDS             1..302
                     /gene="SULT1C4"
                     /gene_synonym="SULT1C; SULT1C2"
                     /coded_by="NM_006588.4:385..1293"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2077.1"
                     /db_xref="GeneID:27233"
                     /db_xref="HGNC:HGNC:11457"
                     /db_xref="MIM:608357"
ORIGIN      
        1 malhdmedft fdgtkrlsvn yvkgilqptd tcdiwdkiwn fqakpddlli stypkagttw
       61 tqeiveliqn egdvekskra pthqrfpfle mkipslgsgl eqahampspr ilkthlpfhl
      121 lppslleknc kiiyvarnpk dnmvsyyhfq rmnkalpapg tweeyfetfl agkvcwgswh
      181 ehvkgwweak dkhrilylfy edmkknpkhe iqklaefigk klddkvldki vhytsfdvmk
      241 qnpmanyssi paeimdhsis pfmrkgavgd wkkhftvaqn erfdedykkk mtdtrltfhf
      301 qf
//
LOCUS       NP_000603                180 aa            linear   PRI 27-APR-2025
DEFINITION  insulin-like growth factor 2 isoform 1 preproprotein [Homo
            sapiens].
ACCESSION   NP_000603
VERSION     NP_000603.1
DBSOURCE    REFSEQ: accession NM_000612.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Li,X., Huang,L., Liu,B., Zhang,Z., Zhou,G., Guo,Z., Song,J. and
            Wang,X.
  TITLE     Cyclic negative pressure promotes chondrocyte growth: Association
            of IGF-2 with EGR-1
  JOURNAL   Biomol Biomed 24 (6), 1761-1775 (2024)
   PUBMED   38912889
  REMARK    GeneRIF: Cyclic negative pressure promotes chondrocyte growth:
            Association of IGF-2 with EGR-1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Vos,S., Van den Bergh,B.R.H., Martens,D.S., Bijnens,E., Shkedy,Z.,
            Kindermans,H., Platzer,M., Schwab,M. and Nawrot,T.S.
  TITLE     Maternal perceived stress and green spaces during pregnancy are
            associated with adult offspring gene (NR3C1 and IGF2/H19)
            methylation patterns in adulthood: A pilot study
  JOURNAL   Psychoneuroendocrinology 167, 107088 (2024)
   PUBMED   38924829
  REMARK    GeneRIF: Maternal perceived stress and green spaces during
            pregnancy are associated with adult offspring gene (NR3C1 and
            IGF2/H19) methylation patterns in adulthood: A pilot study.
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Mirbahari,S.N., Fatemi,N., Savabkar,S., Chaleshi,V., Zali,N.,
            Taleghani,M.Y., Mirzaei,E., Rejali,L., Moghadam,P.K. and
            Mojarad,E.N.
  TITLE     Unmasking early colorectal cancer clues: in silico and in vitro
            investigation of downregulated IGF2, SOCS1, MLH1, and CACNA1G in
            SSA polyps
  JOURNAL   Mol Biol Rep 51 (1), 764 (2024)
   PUBMED   38874740
  REMARK    GeneRIF: Unmasking early colorectal cancer clues: in silico and in
            vitro investigation of downregulated IGF2, SOCS1, MLH1, and CACNA1G
            in SSA polyps.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Rainier,S., Johnson,L.A., Dobry,C.J., Ping,A.J., Grundy,P.E. and
            Feinberg,A.P.
  TITLE     Relaxation of imprinted genes in human cancer
  JOURNAL   Nature 362 (6422), 747-749 (1993)
   PUBMED   8385745
  REMARK    GeneRIF: IGF2 gene is imprinted, with expression from only the
            paternal allele.
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Shuman,C., Kalish,J.M. and Weksberg,R.
  TITLE     Beckwith-Wiedemann Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301568
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Saal,H.M., Harbison,M.D. and Netchine,I.
  TITLE     Silver-Russell Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301499
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Daimon,M., Johnson,T.R., Ilan,J. and Ilan,J.
  TITLE     The third IGF-II promoter specifies transcription of three
            transcripts out of five in human placenta
  JOURNAL   Mol Reprod Dev 33 (4), 413-417 (1992)
   PUBMED   1282023
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Sussenbach,J.S., Steenbergh,P.H. and Holthuizen,P.
  TITLE     Structure and expression of the human insulin-like growth factor
            genes
  JOURNAL   Growth Regul 2 (1), 1-9 (1992)
   PUBMED   1486331
  REMARK    Review article
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Rinderknecht,E. and Humbel,R.E.
  TITLE     Primary structure of human insulin-like growth factor II
  JOURNAL   FEBS Lett 89 (2), 283-286 (1978)
   PUBMED   658418
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC132217.15, BC053318.1,
            M17426.1, AK025719.1, BC073756.1 and BQ014465.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the insulin family of
            polypeptide growth factors, which are involved in development and
            growth. It is an imprinted gene, expressed only from the paternal
            allele, and epigenetic changes at this locus are associated with
            Wilms tumour, Beckwith-Wiedemann syndrome, rhabdomyosarcoma, and
            Silver-Russell syndrome. A read-through INS-IGF2 gene exists, whose
            5' region overlaps the INS gene and the 3' region overlaps this
            gene. Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Oct
            2010].
            
            Transcript Variant: This variant (1) represents the most
            predominant transcript. Variants 1, 2, 4 and 5 encode the same
            isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.895793.1,
                                           SRR14038192.1386562.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene         :: PMID: 8385745
            MANE Ensembl match     :: ENST00000416167.7/ ENSP00000414497.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..180
                     /product="insulin-like growth factor 2 isoform 1
                     preproprotein"
                     /note="insulin-like growth factor type 2; insulin-like
                     growth factor 2 (somatomedin A); T3M-11-derived growth
                     factor; preptin"
                     /calculated_mol_wt=17640
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2518
     proprotein      25..180
                     /product="insulin-like growth factor II isoform 1
                     proprotein"
                     /calculated_mol_wt=17640
     mat_peptide     25..91
                     /product="Insulin-like growth factor 2.
                     /id=PRO_0000015717"
                     /note="propagated from UniProtKB/Swiss-Prot (P01344.1)"
                     /calculated_mol_wt=7476
     Region          25..52
                     /region_name="B"
                     /note="propagated from UniProtKB/Swiss-Prot (P01344.1)"
     mat_peptide     26..91
                     /product="Insulin-like growth factor II Ala-25 Del.
                     /id=PRO_0000015718"
                     /note="propagated from UniProtKB/Swiss-Prot (P01344.1)"
                     /calculated_mol_wt=7404
     Region          28..91
                     /region_name="IlGF"
                     /note="insulin_like growth factors; specific to
                     vertebrates. Members include a number of peptides
                     including insulin-like growth factors I and II, which play
                     a variety of roles in controlling processes such as
                     growth, differentiation, and reproduction. On a...;
                     cd04368"
                     /db_xref="CDD:239834"
     Site            order(30,39,47..51)
                     /site_type="active"
                     /note="IGFBP binding surface [active]"
                     /db_xref="CDD:239834"
     Site            order(48,50..51,67)
                     /site_type="active"
                     /note="type 1 IGF- and insulin-receptor binding surface
                     [active]"
                     /db_xref="CDD:239834"
     Site            48
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000269|PubMed:28873464; propagated from
                     UniProtKB/Swiss-Prot (P01344.1)"
     Region          53..64
                     /region_name="C"
                     /note="propagated from UniProtKB/Swiss-Prot (P01344.1)"
     Site            58
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000269|PubMed:28873464; propagated from
                     UniProtKB/Swiss-Prot (P01344.1)"
     Site            61
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000269|PubMed:28873464; propagated from
                     UniProtKB/Swiss-Prot (P01344.1)"
     Site            62
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000269|PubMed:28873464; propagated from
                     UniProtKB/Swiss-Prot (P01344.1)"
     Region          65..85
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (P01344.1)"
     Site            order(72..74,78..79)
                     /site_type="active"
                     /note="type 2 IGF-receptor binding surface [active]"
                     /db_xref="CDD:239834"
     Region          86..91
                     /region_name="D"
                     /note="propagated from UniProtKB/Swiss-Prot (P01344.1)"
     mat_peptide     92..180
                     /product="E peptide"
                     /calculated_mol_wt=10183
     mat_peptide     93..126
                     /product="Preptin. /id=PRO_0000370376"
                     /note="propagated from UniProtKB/Swiss-Prot (P01344.1)"
                     /calculated_mol_wt=4030
     Site            96
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:22171320,
                     ECO:0000269|PubMed:23234360; propagated from
                     UniProtKB/Swiss-Prot (P01344.1)"
     Site            99
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1569071,
                     ECO:0000269|PubMed:22171320; propagated from
                     UniProtKB/Swiss-Prot (P01344.1)"
     Region          112..166
                     /region_name="IGF2_C"
                     /note="Insulin-like growth factor II E-peptide; pfam08365"
                     /db_xref="CDD:462445"
     Region          161..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01344.1)"
     Site            163
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19838169,
                     ECO:0000269|PubMed:22171320; propagated from
                     UniProtKB/Swiss-Prot (P01344.1)"
     CDS             1..180
                     /gene="IGF2"
                     /gene_synonym="C11orf43; GRDF; IGF-II; PP9974; SRS3"
                     /coded_by="NM_000612.6:1168..1710"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS7728.1"
                     /db_xref="GeneID:3481"
                     /db_xref="HGNC:HGNC:5466"
                     /db_xref="MIM:147470"
ORIGIN      
        1 mgipmgksml vlltflafas cciaayrpse tlcggelvdt lqfvcgdrgf yfsrpasrvs
       61 rrsrgiveec cfrscdlall etycatpaks erdvstpptv lpdnfprypv gkffqydtwk
      121 qstqrlrrgl pallrarrgh vlakeleafr eakrhrplia lptqdpahgg appemasnrk
//
LOCUS       NP_001129628             953 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 507 [Homo sapiens].
ACCESSION   NP_001129628
VERSION     NP_001129628.1
DBSOURCE    REFSEQ: accession NM_001136156.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Creamer,K.M., Larsen,E.C. and Lawrence,J.B.
  TITLE     ZNF146/OZF and ZNF507 target LINE-1 sequences
  JOURNAL   G3 (Bethesda) 12 (3) (2022)
   PUBMED   35100360
  REMARK    GeneRIF: ZNF146/OZF and ZNF507 target LINE-1 sequences.
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Kwon,W., Choi,S.K., Kim,D., Kim,H.G., Park,J.K., Han,J.E.,
            Cho,G.J., Yun,S., Yu,W., Han,S.H., Ha,Y.S., Lee,J.N., Kwon,T.G.,
            Cho,D.H., Yi,J.K., Kim,M.O., Ryoo,Z.Y. and Park,S.
  TITLE     ZNF507 affects TGF-beta signaling via TGFBR1 and MAP3K8 activation
            in the progression of prostate cancer to an aggressive state
  JOURNAL   J Exp Clin Cancer Res 40 (1), 291 (2021)
   PUBMED   34537073
  REMARK    GeneRIF: ZNF507 affects TGF-beta signaling via TGFBR1 and MAP3K8
            activation in the progression of prostate cancer to an aggressive
            state.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB165165.1, AL713775.1, BX640881.1, AC007773.1, BU681879.1 and
            CK820221.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.117234.1,
                                           SRR1803611.187557.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355898.6/ ENSP00000348162.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..953
                     /product="zinc finger protein 507"
                     /calculated_mol_wt=105636
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TCN5.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TCN5.2)"
     Region          470..489
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCN5.2)"
     Region          643..663
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(648,650,652,654..655,658..659,662,676,678,682..683,
                     686..687,690,704,706,708,710..711,714..715)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          671..691
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          699..717
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          760..780
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          788..808
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          831..888
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCN5.2)"
     CDS             1..953
                     /gene="ZNF507"
                     /gene_synonym="Zfp507"
                     /coded_by="NM_001136156.2:271..3132"
                     /db_xref="CCDS:CCDS32985.1"
                     /db_xref="GeneID:22847"
                     /db_xref="HGNC:HGNC:23783"
                     /db_xref="MIM:620567"
ORIGIN      
        1 meesssvaml vpdigeqeai ltaesiisps leideqrktk pdplihviqk lskiveneks
       61 qkclligkkr prssaathsl etqelceipa kviqspaadt rraemsqtnf tpdtlaqneg
      121 kamsyqcslc kflsssfsvl kdhikqhgqq nevilmcsec hitsrsqeel eahvvndhdn
      181 danihtqska qqcvspsssl crktternet ipdipvsvdn lqthtvqtas vaemgrrkwy
      241 ayeqygmyrc lfcsytcgqq rmlkthawkh agevdcsypi feneneplgl ldssaaaapg
      301 gvdavviaig eselsihngp svqvqicsse qlsssspleq saergvhlsq svtldpneee
      361 mlevisdaee nlipdsllts aqkiissspn kkghvnvive rlpsaeetls qkrflmntem
      421 eegkdlslte aqigregmdd vyradkctvd iggliigwss sekkdelmnk glatdenapp
      481 grrrtnsesl rlhslaaeal vtmpiraael tranlghygd inlldpdtsq rqvdstlaay
      541 skmmsplkns sdgltslnqs nstlvalpeg rqelsdgqvk tgismslltv ieklrertdq
      601 nasdddilke lqdnaqcqpn sdtslsgnnv veyipnaerp yrcrlchyts gnkgyikqhl
      661 rvhrqrqpyq cpicehiadn skdleshmih hcktriyqck qceesfhyks qlrnhereqh
      721 slpdtlsiat sneprissdt adgkcvqegn kssvqkqyrc dvcdytstty vgvrnhrrih
      781 nsdkpyrcsl cgyvcshpps lkshmwkhas dqnynyeqvn kaindaisqs grvlgkspgk
      841 tqlksseesa dpvtgssena vssselmsqt psevlgtnen eklsptsnts yslekissla
      901 ppsmeycvll fcccicgfes tskenlldhm kehegeivni ilnkdhntal ntn
//
LOCUS       NP_001968                957 aa            linear   PRI 27-APR-2025
DEFINITION  glutamyl aminopeptidase isoform 1 [Homo sapiens].
ACCESSION   NP_001968
VERSION     NP_001968.3
DBSOURCE    REFSEQ: accession NM_001977.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 957)
  AUTHORS   Huang,W., Chen,A.C.H., Wei,X., Fong,S.W., Yeung,W.S.B. and Lee,Y.L.
  TITLE     Uncovering the role of TET2-mediated ENPEP activation in
            trophoblast cell fate determination
  JOURNAL   Cell Mol Life Sci 81 (1), 270 (2024)
   PUBMED   38886218
  REMARK    GeneRIF: Uncovering the role of TET2-mediated ENPEP activation in
            trophoblast cell fate determination.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 957)
  AUTHORS   Valverde,A., Dunys,J., Lorivel,T., Debayle,D., Gay,A.S.,
            Lacas-Gervais,S., Roques,B.P., Chami,M. and Checler,F.
  TITLE     Aminopeptidase A contributes to biochemical, anatomical and
            cognitive defects in Alzheimer's disease (AD) mouse model and is
            increased at early stage in sporadic AD brain
  JOURNAL   Acta Neuropathol 141 (6), 823-839 (2021)
   PUBMED   33881611
  REMARK    GeneRIF: Aminopeptidase A contributes to biochemical, anatomical
            and cognitive defects in Alzheimer's disease (AD) mouse model and
            is increased at early stage in sporadic AD brain.
REFERENCE   3  (residues 1 to 957)
  AUTHORS   Aung,M., Konoshita,T., Moodley,J., Naicker,T., Connolly,C.,
            Khaliq,O.P. and Gathiram,P.
  TITLE     Aminopeptidase A (ENPEP) gene polymorphisms and preeclampsia:
            Descriptive analysis
  JOURNAL   Eur J Obstet Gynecol Reprod Biol 258, 70-74 (2021)
   PUBMED   33421813
  REMARK    GeneRIF: Aminopeptidase A (ENPEP) gene polymorphisms and
            preeclampsia: Descriptive analysis.
REFERENCE   4  (residues 1 to 957)
  AUTHORS   Qi,F., Qian,S., Zhang,S. and Zhang,Z.
  TITLE     Single cell RNA sequencing of 13 human tissues identify cell types
            and receptors of human coronaviruses
  JOURNAL   Biochem Biophys Res Commun 526 (1), 135-140 (2020)
   PUBMED   32199615
REFERENCE   5  (residues 1 to 957)
  AUTHORS   Chuang,H.Y., Jiang,J.K., Yang,M.H., Wang,H.W., Li,M.C., Tsai,C.Y.,
            Jhang,Y.Y. and Huang,J.C.
  TITLE     Aminopeptidase A initiates tumorigenesis and enhances tumor cell
            stemness via TWIST1 upregulation in colorectal cancer
  JOURNAL   Oncotarget 8 (13), 21266-21280 (2017)
   PUBMED   28177885
  REMARK    GeneRIF: We suggest that APA enzymatic activity affects tumor
            initiation and cancer malignancy in a TWIST-dependent manner
REFERENCE   6  (residues 1 to 957)
  AUTHORS   Malinauskas,M., Wallenius,V., Fandriks,L. and Casselbrant,A.
  TITLE     Local expression of AP/AngIV/IRAP and effect of AngIV on
            glucose-induced epithelial transport in human jejunal mucosa
  JOURNAL   J Renin Angiotensin Aldosterone Syst 16 (4), 1101-1108 (2015)
   PUBMED   26311161
  REMARK    GeneRIF: The substrate Angiotensin II, the enzymes
            aminopeptidases-A, B, M as well as IRAP were detected in the
            jejunal mucosa.
REFERENCE   7  (residues 1 to 957)
  AUTHORS   Li,L., Wang,J. and Cooper,M.D.
  TITLE     cDNA cloning and expression of human glutamyl aminopeptidase
            (aminopeptidase A)
  JOURNAL   Genomics 17 (3), 657-664 (1993)
   PUBMED   8244382
REFERENCE   8  (residues 1 to 957)
  AUTHORS   Nanus,D.M., Engelstein,D., Gastl,G.A., Gluck,L., Vidal,M.J.,
            Morrison,M., Finstad,C.L., Bander,N.H. and Albino,A.P.
  TITLE     Molecular cloning of the human kidney differentiation antigen
            gp160: human aminopeptidase A
  JOURNAL   Proc Natl Acad Sci U S A 90 (15), 7069-7073 (1993)
   PUBMED   8346219
REFERENCE   9  (residues 1 to 957)
  AUTHORS   Stefanovic,V., Vlahovic,P., Ardaillou,N. and Ardaillou,R.
  TITLE     Receptor-mediated induction of aminopeptidase A (APA) of human
            glomerular epithelial cells (HGEC) by glucocorticoids
  JOURNAL   FEBS Lett 294 (3), 171-174 (1991)
   PUBMED   1756856
REFERENCE   10 (residues 1 to 957)
  AUTHORS   Nanus,D.M., Pfeffer,L.M., Bander,N.H., Bahri,S. and Albino,A.P.
  TITLE     Antiproliferative and antitumor effects of alpha-interferon in
            renal cell carcinomas: correlation with the expression of a
            kidney-associated differentiation glycoprotein
  JOURNAL   Cancer Res 50 (14), 4190-4194 (1990)
   PUBMED   2364374
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC094770.1, AC098798.4,
            BG400415.1, AL568777.3, AI640493.1 and AC017068.7.
            
            On Mar 15, 2007 this sequence version replaced NP_001968.2.
            
            Summary: The ENPEP gene encodes glutamyl aminopeptidase, a type II
            integral membrane protein with an extracellular zinc-binding
            domain. This protein can upregulate blood pressure by cleaving the
            N-terminal aspartate from angiotensin II, and can regulate blood
            vessel formation and enhance tumorigenesis in some tissues. Along
            with ANPEP and DPP4, ENPEP was found to be a candidate co-receptor
            for the coronavirus SARS-CoV-2, which causes COVID-19. [provided by
            RefSeq, Apr 2020].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AM888273.1, AM888274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265162.10/ ENSP00000265162.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..957
                     /product="glutamyl aminopeptidase isoform 1"
                     /EC_number="3.4.11.7"
                     /note="EAP; AP-A; aminopeptidase A; differentiation
                     antigen gp160"
                     /calculated_mol_wt=109114
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07075.3)"
     Region          44..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07075.3)"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, atypical.
                     /evidence=ECO:0000269|PubMed:23888046,
                     ECO:0007744|PDB:4KX7; propagated from UniProtKB/Swiss-Prot
                     (Q07075.3)"
     Region          100..540
                     /region_name="M1_APN-Q_like"
                     /note="Peptidase M1 aminopeptidase N catalytic domain
                     family which includes aminopeptidase N (APN),
                     aminopeptidase Q (APQ), tricorn interacting factor F3, and
                     endoplasmic reticulum aminopeptidase 1 (ERAP1); cd09601"
                     /db_xref="CDD:341064"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q07075.3)"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23888046,
                     ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8,
                     ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
                     ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC,
                     ECO:0007744|PDB:4KXD; propagated from UniProtKB/Swiss-Prot
                     (Q07075.3)"
     Site            order(221,223,357..360,393..394,397,416,420,474,479)
                     /site_type="active"
                     /db_xref="CDD:341064"
     Site            221
                     /site_type="other"
                     /note="Binds calcium which modulates its enzyme activity.
                     /evidence=ECO:0000269|PubMed:23888046; propagated from
                     UniProtKB/Swiss-Prot (Q07075.3)"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7,
                     ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9,
                     ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB,
                     ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD; propagated
                     from UniProtKB/Swiss-Prot (Q07075.3)"
     Site            340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23888046,
                     ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9,
                     ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB,
                     ECO:0007744|PDB:4KXC; propagated from UniProtKB/Swiss-Prot
                     (Q07075.3)"
     Site            479
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000269|PubMed:23888046,
                     ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
                     ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC,
                     ECO:0007744|PDB:4KXD; propagated from UniProtKB/Swiss-Prot
                     (Q07075.3)"
     Site            554
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23888046,
                     ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8,
                     ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
                     ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD; propagated
                     from UniProtKB/Swiss-Prot (Q07075.3)"
     Site            589
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07075.3)"
     Site            597
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23888046,
                     ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KXD; propagated
                     from UniProtKB/Swiss-Prot (Q07075.3)"
     Site            607
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q07075.3)"
     Region          616..934
                     /region_name="ERAP1_C"
                     /note="ERAP1-like C-terminal domain; pfam11838"
                     /db_xref="CDD:463368"
     Site            678
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23888046,
                     ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8,
                     ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
                     ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC,
                     ECO:0007744|PDB:4KXD; propagated from UniProtKB/Swiss-Prot
                     (Q07075.3)"
     Site            763
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7,
                     ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9,
                     ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB,
                     ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD; propagated
                     from UniProtKB/Swiss-Prot (Q07075.3)"
     Site            773
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q07075.3)"
     Site            801
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23888046,
                     ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8,
                     ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
                     ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC,
                     ECO:0007744|PDB:4KXD; propagated from UniProtKB/Swiss-Prot
                     (Q07075.3)"
     Site            828
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23888046,
                     ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8,
                     ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA,
                     ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC,
                     ECO:0007744|PDB:4KXD; propagated from UniProtKB/Swiss-Prot
                     (Q07075.3)"
     CDS             1..957
                     /gene="ENPEP"
                     /gene_synonym="APA; CD249; gp160"
                     /coded_by="NM_001977.4:261..3134"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3691.1"
                     /db_xref="GeneID:2028"
                     /db_xref="HGNC:HGNC:3355"
                     /db_xref="MIM:138297"
ORIGIN      
        1 mnfaeregsk ryciqtkhva ilcavvvgvg livglavglt rscdssgdgg pgtapapshl
       61 psstaspsgp paqdqdicpa sedesgqwkn frlpdfvnpv hydlhvkpll eedtytgtvs
      121 isinlsaptr ylwlhlretr itrlpelkrp sgdqvqvrrc feykkqeyvv veaeeeltps
      181 sgdglylltm efagwlngsl vgfyrttyte ngqvksivat dheptdarks fpcfdepnkk
      241 atytisithp keygalsnmp vakeesvddk wtrttfeksv pmstylvcfa vhqfdsvkri
      301 snsgkpltiy vqpeqkhtae yaanitksvf dyfeeyfamn yslpkldkia ipdfgtgame
      361 nwglityret nllydpkesa ssnqqrvatv vahelvhqwf gnivtmdwwe dlwlnegfas
      421 ffeflgvnha etdwqmrdqm lledvlpvqe ddslmsshpi ivtvttpdei tsvfdgisys
      481 kgssilrmle dwikpenfqk gcqmylekyq fknaktsdfw aaleeasrlp vkevmdtwtr
      541 qmgypvlnvn gvknitqkrf lldpranpsq ppsdlgytwn ipvkwtedni tssvlfnrse
      601 kegitlnssn psgnaflkin pdhigfyrvn yevatwdsia talslnhktf ssadraslid
      661 dafalaraql ldykvalnlt kylkreenfl pwqrvisavt yiismfeddk elypmieeyf
      721 qgqvkpiads lgwndagdhv tkllrssvlg fackmgdrea lnnasslfeq wlngtvslpv
      781 nlrllvyryg mqnsgneisw nytleqyqkt slaqekekll yglasvknvt llsryldllk
      841 dtnliktqdv ftviryisyn sygknmawnw iqlnwdylvn rytlnnrnlg rivtiaepfn
      901 telqlwqmes ffakypqaga gekpreqvle tvknniewlk qhrntirewf fnllesg
//
LOCUS       NP_001035202            1945 aa            linear   PRI 27-APR-2025
DEFINITION  myosin-11 isoform SM2B [Homo sapiens].
ACCESSION   NP_001035202
VERSION     NP_001035202.1
DBSOURCE    REFSEQ: accession NM_001040113.2
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1945)
  AUTHORS   Wei,X., Ma,Y., Xie,B., Gui,C., Shi,M., Wei,X., Huang,Y., Fan,X.,
            Wei,Q., Huang,Q., Deng,L., Zhang,C., Deng,X., Gui,B. and Chen,Y.
  TITLE     Complex genotype-phenotype correlation of MYH11: new insights from
            monozygotic twins with highly variable expressivity and outcomes
  JOURNAL   BMC Med Genomics 17 (1), 135 (2024)
   PUBMED   38773466
  REMARK    GeneRIF: Complex genotype-phenotype correlation of MYH11: new
            insights from monozygotic twins with highly variable expressivity
            and outcomes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1945)
  AUTHORS   Billon,C., Piccoli,G.B., de Sainte Agathe,J.M., Stoeva,R.,
            Derive,N., Heidet,L., Berrebi,D., Bruneval,P., Jeunemaitre,X. and
            Hureaux,M.
  TITLE     Genome-wide analysis identifies MYH11 compound heterozygous
            variants leading to visceral myopathy corresponding to late-onset
            form of megacystis-microcolon-intestinal hypoperistalsis syndrome
  JOURNAL   Mol Genet Genomics 299 (1), 44 (2024)
   PUBMED   38625590
  REMARK    GeneRIF: Genome-wide analysis identifies MYH11 compound
            heterozygous variants leading to visceral myopathy corresponding to
            late-onset form of megacystis-microcolon-intestinal hypoperistalsis
            syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1945)
  AUTHORS   Pan,M., Tan,X., Sun,T., Zhu,W., Liu,H., Liu,Q. and Dong,H.
  TITLE     A harmful MYH11 variant detected in a family with thoracic aortic
            dissection and patent ductus arteriosus
  JOURNAL   Forensic Sci Med Pathol 20 (1), 212-218 (2024)
   PUBMED   37306888
  REMARK    GeneRIF: A harmful MYH11 variant detected in a family with thoracic
            aortic dissection and patent ductus arteriosus.
REFERENCE   4  (residues 1 to 1945)
  AUTHORS   Jiang,Y., Chao,H.Y., Lu,X.Z., Wu,P. and Sun,X.C.
  TITLE     [Molecular Genetic Characteristics of Acute Myeloid Leukemia
            Patients with CBFbeta-MYH11 Positive]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1661-1667 (2022)
   PUBMED   36476886
  REMARK    GeneRIF: [Molecular Genetic Characteristics of Acute Myeloid
            Leukemia Patients with CBFbeta-MYH11 Positive].
REFERENCE   5  (residues 1 to 1945)
  AUTHORS   Aikawa,M., Sivam,P.N., Kuro-o,M., Kimura,K., Nakahara,K.,
            Takewaki,S., Ueda,M., Yamaguchi,H., Yazaki,Y., Periasamy,M. et al.
  TITLE     Human smooth muscle myosin heavy chain isoforms as molecular
            markers for vascular development and atherosclerosis
  JOURNAL   Circ Res 73 (6), 1000-1012 (1993)
   PUBMED   7916668
REFERENCE   6  (residues 1 to 1945)
  AUTHORS   van der Reijden,B.A., Dauwerse,J.G., Wessels,J.W., Beverstock,G.C.,
            Hagemeijer,A., van Ommen,G.J. and Breuning,M.H.
  TITLE     A gene for a myosin peptide is disrupted by the inv(16)(p13q22) in
            acute nonlymphocytic leukemia M4Eo
  JOURNAL   Blood 82 (10), 2948-2952 (1993)
   PUBMED   8219185
REFERENCE   7  (residues 1 to 1945)
  AUTHORS   Deng,Z., Liu,P., Marlton,P., Claxton,D.F., Lane,S., Callen,D.F.,
            Collins,F.S. and Siciliano,M.J.
  TITLE     Smooth muscle myosin heavy chain locus (MYH11) maps to
            16p13.13-p13.12 and establishes a new region of conserved synteny
            between human 16p and mouse 16
  JOURNAL   Genomics 18 (1), 156-159 (1993)
   PUBMED   8276405
REFERENCE   8  (residues 1 to 1945)
  AUTHORS   Matsuoka,R., Yoshida,M.C., Furutani,Y., Imamura,S., Kanda,N.,
            Yanagisawa,M., Masaki,T. and Takao,A.
  TITLE     Human smooth muscle myosin heavy chain gene mapped to chromosomal
            region 16q12
  JOURNAL   Am J Med Genet 46 (1), 61-67 (1993)
   PUBMED   7684189
REFERENCE   9  (residues 1 to 1945)
  AUTHORS   Ambartsumyan,L.
  TITLE     Megacystis-Microcolon-Intestinal Hypoperistalsis Syndrome Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31070878
REFERENCE   10 (residues 1 to 1945)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX489788.1, AY520817.1,
            BC104906.1 and AA552189.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a smooth muscle myosin
            belonging to the myosin heavy chain family. The gene product is a
            subunit of a hexameric protein that consists of two heavy chain
            subunits and two pairs of non-identical light chain subunits. It
            functions as a major contractile protein, converting chemical
            energy into mechanical energy through the hydrolysis of ATP. A
            chromosomal rearrangement involving this gene is associated with
            acute myeloid leukemia of the M4Eo subtype. Mutations in this gene
            are associated with visceral myopathy,
            megacystis-microcolon-intestinal hypoperistalsis syndrome 2, and
            familial thoracic aortic aneurysm 4. [provided by RefSeq, May
            2022].
            
            Transcript Variant: This variant (SM2B) represents the longer
            transcript. It encodes the isoform SM2B.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY520817.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match :: ENST00000452625.7/ ENSP00000407821.2
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1945
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.11"
     Protein         1..1945
                     /product="myosin-11 isoform SM2B"
                     /note="myosin, heavy polypeptide 11, smooth muscle;
                     myosin, heavy chain 11, smooth muscle; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=224198
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Region          31..76
                     /region_name="Myosin_N"
                     /note="Myosin N-terminal SH3-like domain; pfam02736"
                     /db_xref="CDD:460670"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z406; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Region          99..778
                     /region_name="MYSc_class_II"
                     /note="class II myosins, motor domain; cd01377"
                     /db_xref="CDD:276951"
     Site            order(126..134,178..185,238..248,466..471)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276951"
     Site            126..134
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276951"
     Site            129
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Site            178..185
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276951"
     Site            238..248
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276951"
     Site            466..471
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276951"
     Site            495..518
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276951"
     Region          668..690
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Site            710..719
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276951"
     Site            order(722..738,767..778)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276951"
     Region          769..783
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Region          855..1935
                     /region_name="Myosin_tail_1"
                     /note="Myosin tail; pfam01576"
                     /db_xref="CDD:460256"
     Region          865..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Site            1184
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z406; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            1691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63862; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            1729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63862; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Region          1751..1807
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     CDS             1..1945
                     /gene="MYH11"
                     /gene_synonym="AAT4; FAA4; SMHC; SMMHC; SMMS-1; VSCM2"
                     /coded_by="NM_001040113.2:106..5943"
                     /note="isoform SM2B is encoded by transcript variant SM2B"
                     /db_xref="CCDS:CCDS45424.1"
                     /db_xref="GeneID:4629"
                     /db_xref="HGNC:HGNC:7569"
                     /db_xref="MIM:160745"
ORIGIN      
        1 maqkgqlsdd ekflfvdknf inspvaqadw aakrlvwvps ekqgfeaasi keekgdevvv
       61 elvengkkvt vgkddiqkmn ppkfskvedm aeltclneas vlhnlreryf sgliytysgl
      121 fcvvvnpykh lpiysekivd mykgkkrhem pphiyaiadt ayrsmlqdre dqsilctges
      181 gagktentkk viqylavvas shkgkkdtsi tqgpsfayge lekqllqanp ileafgnakt
      241 vkndnssrfg kfirinfdvt gyivganiet ylleksrair qardertfhi fyymiagake
      301 kmrsdllleg fnnytflsng fvpipaaqdd emfqetveam aimgfseeeq lsilkvvssv
      361 lqlgnivfkk erntdqasmp dntaaqkvch lmginvtdft rsiltprikv grdvvqkaqt
      421 keqadfavea lakatyerlf rwiltrvnka ldkthrqgas flgildiagf eifevnsfeq
      481 lcinytnekl qqlfnhtmfi leqeeyqreg iewnfidfgl dlqpcielie rpnnppgvla
      541 lldeecwfpk atdksfvekl cteqgshpkf qkpkqlkdkt efsiihyagk vdynasawlt
      601 knmdplndnv tsllnassdk fvadlwkdvd rivgldqmak mtesslpsas ktkkgmfrtv
      661 gqlykeqlgk lmttlrnttp nfvrciipnh ekrsgkldaf lvleqlrcng vlegiricrq
      721 gfpnrivfqe frqryeilaa naipkgfmdg kqacilmika leldpnlyri gqskiffrtg
      781 vlahleeerd lkitdvimaf qamcrgylar kafakrqqql tamkviqrnc aaylklrnwq
      841 wwrlftkvkp llqvtrqeee mqakedelqk tkerqqkaen elkeleqkhs qlteeknllq
      901 eqlqaetely aeaeemrvrl aakkqeleei lhemearlee eedrgqqlqa erkkmaqqml
      961 dleeqleeee aarqklqlek vtaeakikkl edeilvmddq nnklskerkl leerisdltt
     1021 nlaeeeekak nltklknkhe smiselevrl kkeeksrqel eklkrklegd asdfheqiad
     1081 lqaqiaelkm qlakkeeelq aalarlddei aqknnalkki releghisdl qedldseraa
     1141 rnkaekqkrd lgeelealkt eledtldsta tqqelrakre qevtvlkkal deetrsheaq
     1201 vqemrqkhaq aveelteqle qfkrakanld knkqtleken adlagelrvl gqakqevehk
     1261 kkkleaqvqe lqskcsdger araelndkvh klqnevesvt gmlneaegka iklakdvasl
     1321 ssqlqdtqel lqeetrqkln vstklrqlee ernslqdqld eemeakqnle rhistlniql
     1381 sdskkklqdf astvealeeg kkrfqkeien ltqqyeekaa aydklektkn rlqqelddlv
     1441 vdldnqrqlv snlekkqrkf dqllaeekni sskyaderdr aeaeareket kalslarale
     1501 ealeakeele rtnkmlkaem edlvsskddv gknvheleks kraletqmee mktqleeled
     1561 elqatedakl rlevnmqalk gqferdlqar deqneekrrq lqrqlheyet elederkqra
     1621 laaaakkkle gdlkdlelqa dsaikgreea ikqlrklqaq mkdfqreled arasrdeifa
     1681 takenekkak sleadlmqlq edlaaaerar kqadlekeel aeelasslsg rnalqdekrr
     1741 leariaqlee eleeeqgnme amsdrvrkat qqaeqlsnel aterstaqkn esarqqlerq
     1801 nkelrsklhe megavkskfk stiaaleaki aqleeqveqe arekqaatks lkqkdkklke
     1861 illqvederk maeqykeqae kgnarvkqlk rqleeaeees qrinanrrkl qreldeates
     1921 neamgrevna lksklrgppp qetsq
//
LOCUS       NP_005782                681 aa            linear   PRI 27-APR-2025
DEFINITION  U3 small nucleolar ribonucleoprotein protein MPP10 [Homo sapiens].
ACCESSION   NP_005782
VERSION     NP_005782.1
DBSOURCE    REFSEQ: accession NM_005791.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 681)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   4  (residues 1 to 681)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 681)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   6  (residues 1 to 681)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   7  (residues 1 to 681)
  AUTHORS   Granneman,S., Gallagher,J.E., Vogelzangs,J., Horstman,W., van
            Venrooij,W.J., Baserga,S.J. and Pruijn,G.J.
  TITLE     The human Imp3 and Imp4 proteins form a ternary complex with
            hMpp10, which only interacts with the U3 snoRNA in 60-80S
            ribonucleoprotein complexes
  JOURNAL   Nucleic Acids Res 31 (7), 1877-1887 (2003)
   PUBMED   12655004
REFERENCE   8  (residues 1 to 681)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 681)
  AUTHORS   Westendorf,J.M., Konstantinov,K.N., Wormsley,S., Shu,M.D.,
            Matsumoto-Taniura,N., Pirollet,F., Klier,F.G., Gerace,L. and
            Baserga,S.J.
  TITLE     M phase phosphoprotein 10 is a human U3 small nucleolar
            ribonucleoprotein component
  JOURNAL   Mol Biol Cell 9 (2), 437-449 (1998)
   PUBMED   9450966
REFERENCE   10 (residues 1 to 681)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC126389.1 and BC041084.1.
            
            Summary: This gene encodes a protein that is phosphorylated during
            mitosis. The protein localizes to the nucleolus during interphase
            and to the chromosomes during M phase. The protein associates with
            the U3 small nucleolar ribonucleoprotein 60-80S complexes and may
            be involved in pre-rRNA processing. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.151375.1,
                                           SRR1660803.210472.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000244230.7/ ENSP00000244230.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..681
                     /product="U3 small nucleolar ribonucleoprotein protein
                     MPP10"
                     /note="m phase phosphoprotein 10; protein phosphatase 1,
                     regulatory subunit 106; U3 small nucleolar
                     ribonucleoprotein"
                     /calculated_mol_wt=78733
     Region          25..573
                     /region_name="Mpp10"
                     /note="Mpp10 protein; pfam04006"
                     /db_xref="CDD:461128"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00566.2)"
     Region          105..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00566.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O00566.2)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O00566.2)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00566.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00566.2)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00566.2)"
     Region          216..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00566.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O00566.2)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O00566.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O00566.2)"
     Region          558..606
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00566.2)"
     Site            609
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O00566.2)"
     Region          660..681
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00566.2)"
     CDS             1..681
                     /gene="MPHOSPH10"
                     /gene_synonym="CT90; MPP10; MPP10P; PPP1R106"
                     /coded_by="NM_005791.3:33..2078"
                     /db_xref="CCDS:CCDS1916.1"
                     /db_xref="GeneID:10199"
                     /db_xref="HGNC:HGNC:7213"
                     /db_xref="MIM:605503"
ORIGIN      
        1 mapqvwrrrt lercltevgk atgrpecflt iqeglaskft sltkvlydfn kilengrihg
       61 splqklvien fddeqiwqql elqnepilqy fqnavsetin dedisllpes eeqereedgs
      121 eieaddkedl edleeeevsd mgnddpemge raenssksdl rkspvfsded sdldfdiskl
      181 eqqskvqnkg qgkpreksiv ddkffklsem eaylenieke eerkddndee eedidffedi
      241 dsdedegglf gskklksgks srnlkykdff dpvesdedit nvhddeldsn keddeiaeee
      301 aeelsisetd edddlqened nkqhkeslkr vtfalpddae tedtgvlnvk knsdevkssf
      361 ekrqekmnek iaslekelle kkpwqlqgev taqkrpensl leetlhfdha vrmapvitee
      421 ttlqlediik qrirdqawdd vvrkekpked ayeykkrltl dheksklsla eiyeqeyikl
      481 nqqktaeeen pehveiqkmm dslflkldal snfhfipkpp vpeikvvsnl paitmeevap
      541 vsvsdaalla peeikeknka gdiktaaekt atdkkrerrk kkyqkrmkik ekekrrklle
      601 kssvdqagky sktvaseklk qltktgkasf ikdegkdkal kssqaffskl qdqvkmqind
      661 akktekkkkk rqdisvhklk l
//
LOCUS       NP_001355303             164 aa            linear   ROD 27-APR-2025
DEFINITION  RING finger protein 122 isoform 2 [Mus musculus].
ACCESSION   NP_001355303 XP_006509252
VERSION     NP_001355303.1
DBSOURCE    REFSEQ: accession NM_001368374.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Wang,W., Jiang,M., Liu,S., Zhang,S., Liu,W., Ma,Y., Zhang,L.,
            Zhang,J. and Cao,X.
  TITLE     RNF122 suppresses antiviral type I interferon production by
            targeting RIG-I CARDs to mediate RIG-I degradation
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9581-9586 (2016)
   PUBMED   27506794
  REMARK    GeneRIF: RNF122 suppresses antiviral type I interferon production
            by targeting RIG-I caspase activation and recruitment domains to
            mediate RIG-I degradation.
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC109163.16.
            
            On Feb 8, 2019 this sequence version replaced XP_006509252.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR17784650.1326190.1,
                                           SRR13422601.157336.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 17.97 cM"
     Protein         1..164
                     /product="RING finger protein 122 isoform 2"
                     /note="ring finger protein 122 homolog"
                     /calculated_mol_wt=18064
     Region          101..146
                     /region_name="RING-H2_RNF122"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 122 (RNF122) and similar proteins; cd16676"
                     /db_xref="CDD:438338"
     Site            order(102,105,120,122,125,128,139,142)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:438338"
     CDS             1..164
                     /gene="Rnf122"
                     /gene_synonym="1110063C11Rik"
                     /coded_by="NM_001368374.1:69..563"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:68867"
                     /db_xref="MGI:MGI:1916117"
ORIGIN      
        1 magrrrllav eegpvgpegc fcglglvstn kscsmppisf qdlplniymv ifgtgifvfm
       61 lslifccyfi sklrnqaqse rygykevvlk gdakklqlyg tcavcledfk gkdelgvlpc
      121 qhafhrkclv kwlevrcvcp mcnkpiagpt etsqsigill delv
//
LOCUS       NP_001350003             854 aa            linear   ROD 27-APR-2025
DEFINITION  cytosolic phospholipase A2 zeta isoform 3 [Mus musculus].
ACCESSION   NP_001350003 XP_006499713
VERSION     NP_001350003.1
DBSOURCE    REFSEQ: accession NM_001363074.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Yun,B., Lee,H., Ghosh,M., Cravatt,B.F., Hsu,K.L., Bonventre,J.V.,
            Ewing,H., Gelb,M.H. and Leslie,C.C.
  TITLE     Serine hydrolase inhibitors block necrotic cell death by preventing
            calcium overload of the mitochondria and permeability transition
            pore formation
  JOURNAL   J Biol Chem 289 (3), 1491-1504 (2014)
   PUBMED   24297180
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Ghosh,M., Loper,R., Ghomashchi,F., Tucker,D.E., Bonventre,J.V.,
            Gelb,M.H. and Leslie,C.C.
  TITLE     Function, activity, and membrane targeting of cytosolic
            phospholipase A(2)zeta in mouse lung fibroblasts
  JOURNAL   J Biol Chem 282 (16), 11676-11686 (2007)
   PUBMED   17293613
REFERENCE   3  (residues 1 to 854)
  AUTHORS   Ohto,T., Uozumi,N., Hirabayashi,T. and Shimizu,T.
  TITLE     Identification of novel cytosolic phospholipase A(2)s, murine
            cPLA(2){delta}, {epsilon}, and {zeta}, which form a gene cluster
            with cPLA(2){beta}
  JOURNAL   J Biol Chem 280 (26), 24576-24583 (2005)
   PUBMED   15866882
  REMARK    GeneRIF: murine cytosolic phospholipases A2 delta, epsilon, and
            zeta form a gene cluster with cPLA(2)beta
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL844608.18.
            
            On May 5, 2018 this sequence version replaced XP_006499713.1.
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice junction compared to variant 1. The resulting isoform (3)
            has the same N- and C-termini but is 1 aa shorter compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC145426.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 60.31 cM"
     Protein         1..854
                     /product="cytosolic phospholipase A2 zeta isoform 3"
                     /EC_number="3.1.1.4"
                     /note="cytosolic phospholipase A2 zeta; cPLA2-zeta"
                     /calculated_mol_wt=96106
     Region          45..161
                     /region_name="C2_cPLA2"
                     /note="C2 domain present in cytosolic PhosphoLipase A2
                     (cPLA2); cd04036"
                     /db_xref="CDD:176001"
     Site            order(62,65,87,115,117)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176001"
     Region          180..300
                     /region_name="cPLA2_C2"
                     /note="Cytosolic phospholipases A2 C2-domain; pfam18695"
                     /db_xref="CDD:465834"
     Region          299..847
                     /region_name="Patatin_and_cPLA2"
                     /note="Patatins and Phospholipases; cl11396"
                     /db_xref="CDD:416256"
     Site            order(361..362,364,392,684)
                     /site_type="active"
                     /db_xref="CDD:132836"
     Site            390..394
                     /site_type="other"
                     /note="nucleophile elbow"
                     /db_xref="CDD:132836"
     CDS             1..854
                     /gene="Pla2g4f"
                     /gene_synonym="4732472I07Rik; Gm647; Pla2zeta"
                     /coded_by="NM_001363074.1:110..2674"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:271844"
                     /db_xref="MGI:MGI:2685493"
ORIGIN      
        1 mpwtlqpkwl agkglpllga illrktekse pqwkhrreth pyydlqvkvl rarniqhtdk
       61 lskadcyvrl wlptasvsps qtrtvvnssd pewnetfpyq ihgavknvle lalydedvld
      121 sdnvfsilfd tstlqlgqpc tknftrqqdp keleveftle ksqtpasevv tngvlvahpc
      181 lriqgtvtgd ktaslgelgs rqiqlavpga yekpqplqpt sepglpvnft fhvnpvlspk
      241 lhiklqeqlq vfhsgpsdel eaqtskmdka sillsslpln eeltklvdle egqqvslrmk
      301 admsssgdld lrlgfdlcdg eqefldkrkq vaskalqrvm glsealhcdq vpvvavlgsg
      361 ggtramtsly gslaglqelg lldavtylsg vsgsswcist lyrdpswsqk alqgpikyas
      421 ervcsskigm lspkqfeyys rekrawesrg hsmsftdlwg liieyflnqe enpaklsdqq
      481 etvsqgqnpy piyasinvhk nisgddfaew ceftpyevgf pkygayvpte lfgseffmgr
      541 llhfwpepri cylqgmwgsa faaslyeifl klgglslsfl dwhrgsvsvt ddwpklrkqd
      601 ptrlptrlft pmssfsqavl diftsritca qtfnftrglc mykdytarkd fvvsedawhs
      661 hnygypdacp nqltpmkdfl slvdggfain spfplvlqpq ravdlivsfd yslegpfevl
      721 qvtekycrdr gipfprievd pkdsedprec ylfaeaedpc spivlhfplv nrtfrthlap
      781 gverqtaeek afgdfiingp dtaygmmdft yepkefdrlv tlsrynvlnn ketirhalql
      841 aldrrrqagg rvgg
//
LOCUS       NP_057134                192 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein uL11m isoform a [Homo sapiens].
ACCESSION   NP_057134
VERSION     NP_057134.1
DBSOURCE    REFSEQ: accession NM_016050.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Jager,S., Cimermancic,P., Gulbahce,N., Johnson,J.R., McGovern,K.E.,
            Clarke,S.C., Shales,M., Mercenne,G., Pache,L., Li,K., Hernandez,H.,
            Jang,G.M., Roth,S.L., Akiva,E., Marlett,J., Stephens,M., D'Orso,I.,
            Fernandes,J., Fahey,M., Mahon,C., O'Donoghue,A.J., Todorovic,A.,
            Morris,J.H., Maltby,D.A., Alber,T., Cagney,G., Bushman,F.D.,
            Young,J.A., Chanda,S.K., Sundquist,W.I., Kortemme,T.,
            Hernandez,R.D., Craik,C.S., Burlingame,A., Sali,A., Frankel,A.D.
            and Krogan,N.J.
  TITLE     Global landscape of HIV-human protein complexes
  JOURNAL   Nature 481 (7381), 365-370 (2011)
   PUBMED   22190034
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Han,M.J., Cimen,H., Miller-Lee,J.L., Koc,H. and Koc,E.C.
  TITLE     Purification of human mitochondrial ribosomal L7/L12 stalk proteins
            and reconstitution of functional hybrid ribosomes in Escherichia
            coli
  JOURNAL   Protein Expr Purif 78 (1), 48-54 (2011)
   PUBMED   21453772
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Structural compensation for the deficit of rRNA with proteins in
            the mammalian mitochondrial ribosome. Systematic analysis of
            protein components of the large ribosomal subunit from mammalian
            mitochondria
  JOURNAL   J Biol Chem 276 (24), 21724-21736 (2001)
   PUBMED   11279069
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU597133.1, AK290084.1,
            AL519939.3 and BU678208.1.
            
            Summary: This nuclear gene encodes a 39S subunit component of the
            mitochondial ribosome. Alternative splicing results in multiple
            transcript variants. Pseudogenes for this gene are found on
            chromosomes 5 and 12. [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290084.1, SRR14038196.170939.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000310999.11/
                                                  ENSP00000308897.7
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..192
                     /product="large ribosomal subunit protein uL11m isoform a"
                     /note="39S ribosomal protein L11, mitochondrial;
                     mitochondrial large ribosomal subunit protein uL11m"
                     /calculated_mol_wt=20552
     Region          20..155
                     /region_name="Ribosomal_L11"
                     /note="Ribosomal protein L11. Ribosomal protein L11,
                     together with proteins L10 and L7/L12, and 23S rRNA, form
                     the L7/L12 stalk on the surface of the large subunit of
                     the ribosome. The homologous eukaryotic cytoplasmic
                     protein is also called 60S ribosomal...; cd00349"
                     /db_xref="CDD:100101"
     Site            order(21,41,86..88,92,99,124,133..135,139,142..143,
                     146..147,149..151)
                     /site_type="other"
                     /note="23S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:100101"
     Site            order(21,69,71..74,78,80..81,125..126,133..134)
                     /site_type="other"
                     /note="L7/L12 interface [polypeptide binding]"
                     /db_xref="CDD:100101"
     Site            order(37,41)
                     /site_type="active"
                     /note="putative thiostrepton binding site [active]"
                     /db_xref="CDD:100101"
     Site            order(105,108)
                     /site_type="other"
                     /note="L25 interface [polypeptide binding]"
                     /db_xref="CDD:100101"
     CDS             1..192
                     /gene="MRPL11"
                     /gene_synonym="CGI-113; L11MT; MRP-L11; uL11m"
                     /coded_by="NM_016050.5:95..673"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8139.1"
                     /db_xref="GeneID:65003"
                     /db_xref="HGNC:HGNC:14042"
                     /db_xref="MIM:611826"
ORIGIN      
        1 msklgraarg lrkpevggvi raivraglam pgpplgpvlg qrgvsinqfc kefnertkdi
       61 kegiplptki lvkpdrtfei kigqptvsyf lkaaagiekg arqtgkevag lvtlkhvyei
      121 arikaqdeaf alqdvplssv vrsiigsars lgirvvkdls seelaafqke raiflaaqke
      181 adlaaqeeaa kk
//
LOCUS       NP_001096647             701 aa            linear   ROD 27-APR-2025
DEFINITION  actin-binding LIM protein 1 isoform 2 [Mus musculus].
ACCESSION   NP_001096647
VERSION     NP_001096647.1
DBSOURCE    REFSEQ: accession NM_001103177.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Chen,X., Liu,Y., Xu,C., Ba,L., Liu,Z., Li,X., Huang,J., Simpson,E.,
            Gao,H., Cao,D., Sheng,W., Qi,H., Ji,H., Sanderson,M., Cai,C.L.,
            Li,X., Yang,L., Na,J., Yamamura,K., Liu,Y., Huang,G., Shou,W. and
            Sun,N.
  TITLE     QKI is a critical pre-mRNA alternative splicing regulator of
            cardiac myofibrillogenesis and contractile function
  JOURNAL   Nat Commun 12 (1), 89 (2021)
   PUBMED   33397958
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Jin,S.H., Kim,H., Gu,D.R., Park,K.H., Lee,Y.R., Choi,Y. and
            Lee,S.H.
  TITLE     Actin-binding LIM protein 1 regulates receptor activator of
            NF-kappaB ligand-mediated osteoclast differentiation and motility
  JOURNAL   BMB Rep 51 (7), 356-361 (2018)
   PUBMED   29921413
  REMARK    GeneRIF: ABLIM1 is associated with the regulation of preosteoclast
            motility via the PI3K/Akt/Rac1 pathway during RANKL-mediated
            osteoclastogenesis.
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Zhang,Q., Huang,R., Ye,Y., Guo,X., Lu,J., Zhu,F., Gong,X.,
            Zhang,Q., Yan,J., Luo,L., Zhuang,S., Chen,Y., Zhao,X., Evans,S.M.,
            Jiang,C., Liang,X. and Sun,Y.
  TITLE     Temporal requirements for ISL1 in sympathetic neuron proliferation,
            differentiation, and diversification
  JOURNAL   Cell Death Dis 9 (2), 247 (2018)
   PUBMED   29445148
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 701)
  AUTHORS   Narahara,H., Sakai,E., Yamaguchi,Y., Narahara,S., Iwatake,M.,
            Okamoto,K., Yoshida,N. and Tsukuba,T.
  TITLE     Actin binding LIM 1 (abLIM1) negatively controls osteoclastogenesis
            by regulating cell migration and fusion
  JOURNAL   J Cell Physiol 234 (1), 486-499 (2018)
   PUBMED   29904924
  REMARK    GeneRIF: abLIM1 regulated the localization of tubulin, migration,
            and fusion in osteoclasts. Thus, these results indicate that abLIM1
            negatively controls osteoclast differentiation by regulating cell
            migration and fusion mediated via actin formation.
REFERENCE   6  (residues 1 to 701)
  AUTHORS   Erkman,L., Yates,P.A., McLaughlin,T., McEvilly,R.J., Whisenhunt,T.,
            O'Connell,S.M., Krones,A.I., Kirby,M.A., Rapaport,D.H.,
            Bermingham,J.R., O'Leary,D.D. and Rosenfeld,M.G.
  TITLE     A POU domain transcription factor-dependent program regulates axon
            pathfinding in the vertebrate visual system
  JOURNAL   Neuron 28 (3), 779-792 (2000)
   PUBMED   11163266
REFERENCE   7  (residues 1 to 701)
  AUTHORS   Suriyapperuma,S.P., Lozovatsky,L., Ciciotte,S.L., Peters,L.L. and
            Gilligan,D.M.
  TITLE     The mouse adducin gene family: alternative splicing and chromosomal
            localization
  JOURNAL   Mamm Genome 11 (1), 16-23 (2000)
   PUBMED   10602987
REFERENCE   8  (residues 1 to 701)
  AUTHORS   Kim,H.J., Noben-Trauth,K. and Morell,R.J.
  TITLE     Tectorin-beta (Tectb) maps to mouse chromosome 19
  JOURNAL   Genomics 53 (3), 419-420 (1998)
   PUBMED   9799617
REFERENCE   9  (residues 1 to 701)
  AUTHORS   Kim,A.C., Peters,L.L., Knoll,J.H., Van Huffel,C., Ciciotte,S.L.,
            Kleyn,P.W. and Chishti,A.H.
  TITLE     Limatin (LIMAB1), an actin-binding LIM protein, maps to mouse
            chromosome 19 and human chromosome 10q25, a region frequently
            deleted in human cancers
  JOURNAL   Genomics 46 (2), 291-293 (1997)
   PUBMED   9417918
REFERENCE   10 (residues 1 to 701)
  AUTHORS   Roof,D.J., Hayes,A., Adamian,M., Chishti,A.H. and Li,T.
  TITLE     Molecular characterization of abLIM, a novel actin-binding and
            double zinc finger protein
  JOURNAL   J Cell Biol 138 (3), 575-588 (1997)
   PUBMED   9245787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC102655.7, AW060969.1, AF404775.1, AC161518.3 and BE994737.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and lacks three alternate in-frame
            exons inthe 3' coding region, compared to variant 1. It initiates
            translation at an alternate start codon. The encoded isoform (2,
            also known as abLIM-m) has a distinct N-terminus and is shorter
            than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF404775.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 52.09 cM"
     Protein         1..701
                     /product="actin-binding LIM protein 1 isoform 2"
                     /note="actin-binding double zinc finger protein;
                     actin-binding LIM protein family member 1"
                     /calculated_mol_wt=78830
     Region          23..74
                     /region_name="LIM1_abLIM"
                     /note="The first LIM domain of actin binding LIM (abLIM)
                     proteins; cd09327"
                     /db_xref="CDD:188713"
     Site            order(23,26,43,46,49,52,70,73)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188713"
     Region          79..134
                     /region_name="LIM2_abLIM"
                     /note="The second LIM domain on actin binding LIM (abLIM)
                     proteins; cd09328"
                     /db_xref="CDD:188714"
     Site            order(82,85,102,105,108,111,130,133)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188714"
     Region          150..201
                     /region_name="LIM3_abLIM"
                     /note="The third LIM domain of actin binding LIM (abLIM)
                     proteins; cd09329"
                     /db_xref="CDD:188715"
     Site            order(150,153,171,174,177,180,197,200)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188715"
     Region          209..264
                     /region_name="LIM4_abLIM"
                     /note="The fourth LIM domain of actin binding LIM (abLIM)
                     proteins; cd09330"
                     /db_xref="CDD:188716"
     Site            order(209,212,229,232,235,238,257,260)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188716"
     Region          273..651
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          666..701
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..701
                     /gene="Ablim1"
                     /gene_synonym="2210411C18Rik; 2610209L21Rik;
                     4833406P10Rik; 9330196J19Rik; Limab1; mKIAA0059"
                     /coded_by="NM_001103177.3:318..2423"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS50479.1"
                     /db_xref="GeneID:226251"
                     /db_xref="MGI:MGI:1194500"
ORIGIN      
        1 mvkekvahpq dphhssekpv ihchkcgepc kgevlrvqtk hfhikcftck vcgcdlaqgg
       61 ffikngdylc tldyqrmygt rchgcgefve gevvtalgkt yhpncfacti ckrpfppgdr
      121 vtfngrdclc qlcaqpmsss pkeascssnc agcgrdikng qallaldkqw hlgcfkcksc
      181 gkvltgeyis kdgspycekd yqglfgvkce achqfitgkv leagdkhyhp scarcsrcnq
      241 mftegeemyl qgstvwhpdc kqstkteekl rptrtssesi ysrpgssipg spghtiyakv
      301 dneildykdl aaipkvkaiy dierpdlity epfytsgyed kqerqslges prtlsptpsa
      361 egyqdvrdrm ihrstsqgsi nspvysrhsy tpttsrspqh fhrpgnepss grnsplpyrp
      421 dsrpltptya qapkhfhvpd qginiyrkpp iykqhaalaa qskasediik fskfpaaqap
      481 dpneipkiet dhwpgppsla avgtdprrrs sgreedeeel lrrrqlqeeq lmklnsglgq
      541 lilkeemeke sreraslasr ydsplhsash apssktsslp gygknglhrp vstdfaqyns
      601 ygdisggvrd yqtlpdghmp avrmdrgvsm pnmlepkifp yemlmvtnrg rnkilrdvdr
      661 trlerhlape vfweifgmsi qefdklplwr rndmkkkakl f
//
LOCUS       NP_001709                513 aa            linear   PRI 27-APR-2025
DEFINITION  bone morphogenetic protein 6 preproprotein [Homo sapiens].
ACCESSION   NP_001709
VERSION     NP_001709.1
DBSOURCE    REFSEQ: accession NM_001718.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Arcanjo,G.S., Souza,M.B., Domingos,I.F., Pereira-Martins,D.A.,
            Falcao,D.A., Batista,J.V., Hatzlhofer,B.L., Diniz,M.V., Silva,A.P.,
            Guarana,W.L., Hazin,M.F., Araujo,A.S., Cunha,A.F., Saad,S.O.,
            Costa,F.F., Lucena-Araujo,A.R. and Bezerra,M.A.C.
  TITLE     BMP6 and VDR gene polymorphisms are associated with osteonecrosis
            in a sickle cell anaemia cohort
  JOURNAL   Br J Haematol 204 (4), 1507-1514 (2024)
   PUBMED   38323352
  REMARK    GeneRIF: BMP6 and VDR gene polymorphisms are associated with
            osteonecrosis in a sickle cell anaemia cohort.
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Xin,X., Chang,H.M., Leung,P.C.K., Dong,L., Li,J., Lian,F. and Wu,H.
  TITLE     Bone morphogenetic protein 6 induces downregulation of pentraxin 3
            expression in human granulosa lutein cells in women with polycystic
            ovary syndrome
  JOURNAL   J Assist Reprod Genet 41 (1), 31-48 (2024)
   PUBMED   37930517
  REMARK    GeneRIF: Bone morphogenetic protein 6 induces downregulation of
            pentraxin 3 expression in human granulosa lutein cells in women
            with polycystic ovary syndrome.
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Tang,H., Li,J., Li,J.K., He,S.H., Xiang,G., Rong,R., Liang,Z.T. and
            Zhang,H.Q.
  TITLE     BMP6 participates in the pathogenesis of adolescent idiopathic
            scoliosis by regulating osteopenia
  JOURNAL   J Cell Physiol 238 (11), 2586-2599 (2023)
   PUBMED   37795636
  REMARK    GeneRIF: BMP6 participates in the pathogenesis of adolescent
            idiopathic scoliosis by regulating osteopenia.
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Novak,R., Ahmad,Y.A., Timaner,M., Bitman-Lotan,E.,
            Oknin-Vaisman,A., Horwitz,R., Hartmann,O., Reissland,M., Buck,V.,
            Rosenfeldt,M., Nikomarov,D., Diefenbacher,M.E., Shaked,Y. and
            Orian,A.
  TITLE     RNF4 RGMb BMP6 axis required for osteogenic differentiation and
            cancer cell survival
  JOURNAL   Cell Death Dis 13 (9), 820 (2022)
   PUBMED   36153321
  REMARK    GeneRIF: RNF4~RGMb~BMP6 axis required for osteogenic
            differentiation and cancer cell survival.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Wang,R.N., Green,J., Wang,Z., Deng,Y., Qiao,M., Peabody,M.,
            Zhang,Q., Ye,J., Yan,Z., Denduluri,S., Idowu,O., Li,M., Shen,C.,
            Hu,A., Haydon,R.C., Kang,R., Mok,J., Lee,M.J., Luu,H.L. and
            Shi,L.L.
  TITLE     Bone Morphogenetic Protein (BMP) signaling in development and human
            diseases
  JOURNAL   Genes Dis 1 (1), 87-105 (2014)
   PUBMED   25401122
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Tamada,H., Kitazawa,R., Gohji,K., Kamidono,S., Maeda,S. and
            Kitazawa,S.
  TITLE     Molecular cloning and analysis of the 5'-flanking region of the
            human bone morphogenetic protein-6 (BMP-6)
  JOURNAL   Biochim Biophys Acta 1395 (3), 247-251 (1998)
   PUBMED   9512655
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Schluesener,H.J. and Meyermann,R.
  TITLE     Immunolocalization of BMP-6, a novel TGF-beta-related cytokine, in
            normal and atherosclerotic smooth muscle cells
  JOURNAL   Atherosclerosis 113 (2), 153-156 (1995)
   PUBMED   7605353
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Hahn,G.V., Cohen,R.B., Wozney,J.M., Levitz,C.L., Shore,E.M.,
            Zasloff,M.A. and Kaplan,F.S.
  TITLE     A bone morphogenetic protein subfamily: chromosomal localization of
            human genes for BMP5, BMP6, and BMP7
  JOURNAL   Genomics 14 (3), 759-762 (1992)
   PUBMED   1427904
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Sauermann,U., Meyermann,R. and Schluesener,H.J.
  TITLE     Cloning of a novel TGF-beta related cytokine, the vgr, from rat
            brain: cloning of and comparison to homologous human cytokines
  JOURNAL   J Neurosci Res 33 (1), 142-147 (1992)
   PUBMED   1453478
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Celeste,A.J., Iannazzi,J.A., Taylor,R.C., Hewick,R.M., Rosen,V.,
            Wang,E.A. and Wozney,J.M.
  TITLE     Identification of transforming growth factor beta family members
            present in bone-inductive protein purified from bovine bone
  JOURNAL   Proc Natl Acad Sci U S A 87 (24), 9843-9847 (1990)
   PUBMED   2263636
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK300628.1, AL135778.9,
            BF732376.1, M60315.1, BC099624.1, AL133541.21 and AA700487.1.
            
            Summary: This gene encodes a secreted ligand of the TGF-beta
            (transforming growth factor-beta) superfamily of proteins. Ligands
            of this family bind various TGF-beta receptors leading to
            recruitment and activation of SMAD family transcription factors
            that regulate gene expression. The encoded preproprotein is
            proteolytically processed to generate each subunit of the
            disulfide-linked homodimer. This protein regulates a wide range of
            biological processes including iron homeostasis, fat and bone
            development, and ovulation. Differential expression of this gene
            may be associated with progression of breast and prostate cancer.
            Mutations in this gene may be associated with iron overload in
            human patients. [provided by RefSeq, Jul 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M60315.1, SRR1803611.262077.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283147.7/ ENSP00000283147.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
     Protein         1..513
                     /product="bone morphogenetic protein 6 preproprotein"
                     /note="vegetal related growth factor (TGFB-related);
                     VG-1-R; VG-1-related protein"
                     /calculated_mol_wt=54824
     sig_peptide     1..20
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22004.1)"
                     /calculated_mol_wt=2420
     Region          38..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22004.1)"
     Region          65..362
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; pfam00688"
                     /db_xref="CDD:459906"
     Region          89..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22004.1)"
     Region          145..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22004.1)"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22004.1)"
     Site            269
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22004.1)"
     Region          373..398
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22004.1)"
     mat_peptide     375..513
                     /product="Bone morphogenetic protein 6.
                     /id=PRO_0000033871"
                     /note="propagated from UniProtKB/Swiss-Prot (P22004.1)"
                     /calculated_mol_wt=15675
     Site            386
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22004.1)"
     Site            404
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22004.1)"
     Region          411..513
                     /region_name="TGF_beta_BMP6"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in bone morphogenetic protein 6 (BMP-6) and
                     similar proteins; cd19396"
                     /db_xref="CDD:381666"
     Site            order(417,423,436,438..440,457..458,461..462,464,468,472,
                     474,477..480,503..505,507,513)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381666"
     Site            454
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:18070108;
                     propagated from UniProtKB/Swiss-Prot (P22004.1)"
     CDS             1..513
                     /gene="BMP6"
                     /gene_synonym="IO; VGR; VGR1"
                     /coded_by="NM_001718.6:858..2399"
                     /db_xref="CCDS:CCDS4503.1"
                     /db_xref="GeneID:654"
                     /db_xref="HGNC:HGNC:1073"
                     /db_xref="MIM:112266"
ORIGIN      
        1 mpglgrraqw lcwwwgllcs ccgppplrpp lpaaaaaaag gqllgdggsp grteqpppsp
       61 qsssgflyrr lktqekremq keilsvlglp hrprplhglq qpqppalrqq eeqqqqqqlp
      121 rgepppgrlk saplfmldly nalsadnded gasegerqqs wpheaasssq rrqpppgaah
      181 plnrksllap gsgsggaspl tsaqdsafln dadmvmsfvn lveydkefsp rqrhhkefkf
      241 nlsqipegev vtaaefriyk dcvmgsfknq tflisiyqvl qehqhrdsdl flldtrvvwa
      301 seegwlefdi tatsnlwvvt pqhnmglqls vvtrdgvhvh praaglvgrd gpydkqpfmv
      361 affkvsevhv rttrsassrr rqqsrnrstq sqdvarvssa sdynsselkt acrkhelyvs
      421 fqdlgwqdwi iapkgyaany cdgecsfpln ahmnatnhai vqtlvhlmnp eyvpkpccap
      481 tklnaisvly fddnsnvilk kyrnmvvrac gch
//
LOCUS       NP_001406                472 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 2 subunit 3 [Homo
            sapiens].
ACCESSION   NP_001406
VERSION     NP_001406.1
DBSOURCE    REFSEQ: accession NM_001415.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Cardenal Peralta,C., Vandroux,P., Neumann-Arnold,L., Panvert,M.,
            Fagart,J., Seufert,W., Mechulam,Y. and Schmitt,E.
  TITLE     Binding of human Cdc123 to eIF2gamma
  JOURNAL   J Struct Biol 215 (3), 108006 (2023)
   PUBMED   37507029
  REMARK    GeneRIF: Binding of human Cdc123 to eIF2gamma.
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Ivanova,N., Serzhanova,V., Demina,N., Guseva,D. and Skoblov,M.
  TITLE     mRNA analysis revealed a novel pathogenic EIF2S3 variant causing
            MEHMO syndrome
  JOURNAL   Eur J Med Genet 65 (2), 104421 (2022)
   PUBMED   34999262
  REMARK    GeneRIF: mRNA analysis revealed a novel pathogenic EIF2S3 variant
            causing MEHMO syndrome.
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Lu,J., Chen,S., Tan,H., Huang,Z., Li,B., Liu,L., Chen,Y., Zeng,X.,
            Zou,Y. and Xu,L.
  TITLE     Eukaryotic initiation factor-2, gamma subunit, suppresses
            proliferation and regulates the cell cycle via the MAPK/ERK
            signaling pathway in acute myeloid leukemia
  JOURNAL   J Cancer Res Clin Oncol 147 (11), 3157-3168 (2021)
   PUBMED   34232382
  REMARK    GeneRIF: Eukaryotic initiation factor-2, gamma subunit, suppresses
            proliferation and regulates the cell cycle via the MAPK/ERK
            signaling pathway in acute myeloid leukemia.
REFERENCE   5  (residues 1 to 472)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 472)
  AUTHORS   Ehrmann,I.E., Ellis,P.S., Mazeyrat,S., Duthie,S., Brockdorff,N.,
            Mattei,M.G., Gavin,M.A., Affara,N.A., Brown,G.M., Simpson,E.,
            Mitchell,M.J. and Scott,D.M.
  TITLE     Characterization of genes encoding translation initiation factor
            eIF-2gamma in mouse and human: sex chromosome localization, escape
            from X-inactivation and evolution
  JOURNAL   Hum Mol Genet 7 (11), 1725-1737 (1998)
   PUBMED   9736774
REFERENCE   7  (residues 1 to 472)
  AUTHORS   Brand,S.R., Kobayashi,R. and Mathews,M.B.
  TITLE     The Tat protein of human immunodeficiency virus type 1 is a
            substrate and inhibitor of the interferon-induced, virally
            activated protein kinase, PKR
  JOURNAL   J Biol Chem 272 (13), 8388-8395 (1997)
   PUBMED   9079663
REFERENCE   8  (residues 1 to 472)
  AUTHORS   Gaspar,N.J., Kinzy,T.G., Scherer,B.J., Humbelin,M., Hershey,J.W.
            and Merrick,W.C.
  TITLE     Translation initiation factor eIF-2. Cloning and expression of the
            human cDNA encoding the gamma-subunit
  JOURNAL   J Biol Chem 269 (5), 3415-3422 (1994)
   PUBMED   8106381
REFERENCE   9  (residues 1 to 472)
  AUTHORS   Ray,M.K., Chakraborty,A., Datta,B., Chattopadhyay,A., Saha,D.,
            Bose,A., Kinzy,T.G., Wu,S., Hileman,R.E., Merrick,W.C. et al.
  TITLE     Characteristics of the eukaryotic initiation factor 2 associated
            67-kDa polypeptide
  JOURNAL   Biochemistry 32 (19), 5151-5159 (1993)
   PUBMED   8098621
REFERENCE   10 (residues 1 to 472)
  AUTHORS   Safer,B., Adams,S.L., Anderson,W.F. and Merrick,W.C.
  TITLE     Binding of MET-TRNAf and GTP to homogeneous initiation factor MP
  JOURNAL   J Biol Chem 250 (23), 9076-9082 (1975)
   PUBMED   1104615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC019906.1, BC011945.1, AI133612.1, BF435665.1 and
            CB150474.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is the largest subunit of
            a heterotrimeric GTP-binding protein involved in the recruitment of
            methionyl-tRNA(i) to the 40 S ribosomal subunit. [provided by
            RefSeq, Jan 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.218577.1,
                                           SRR1660807.237157.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253039.9/ ENSP00000253039.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.11"
     Protein         1..472
                     /product="eukaryotic translation initiation factor 2
                     subunit 3"
                     /EC_number="3.6.5.3"
                     /note="eukaryotic translation initiation factor 2G;
                     eIF-2gX; eIF2-gamma X; eIF-2-gamma X; eukaryotic
                     translation initiation factor 2 subunit gamma X;
                     eukaryotic translation initiation factor 2, subunit 3
                     gamma, 52kDa; mental retardation, epileptic seizures,
                     hypogonadism and -genitalism, microcephaly and obesity
                     syndrome"
                     /calculated_mol_wt=50979
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine, partial.
                     /evidence=ECO:0000269|Ref.8; propagated from
                     UniProtKB/Swiss-Prot (P41091.3)"
     Region          13..466
                     /region_name="PTZ00327"
                     /note="eukaryotic translation initiation factor 2 gamma
                     subunit; Provisional"
                     /db_xref="CDD:240362"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0N1; propagated from
                     UniProtKB/Swiss-Prot (P41091.3)"
     Region          48..55
                     /region_name="G1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     Region          76..80
                     /region_name="G2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     Region          134..137
                     /region_name="G3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     Region          190..193
                     /region_name="G4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     Region          225..227
                     /region_name="G5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     Region          457..469
                     /region_name="Interacts with CDC123.
                     /evidence=ECO:0000305|PubMed:35031321"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     CDS             1..472
                     /gene="EIF2S3"
                     /gene_synonym="eIF-2gA; EIF2; EIF2G; EIF2gamma; eIF2gX;
                     MEHMO; MRXSBRK"
                     /coded_by="NM_001415.4:14..1432"
                     /db_xref="CCDS:CCDS14210.1"
                     /db_xref="GeneID:1968"
                     /db_xref="HGNC:HGNC:3267"
                     /db_xref="MIM:300161"
ORIGIN      
        1 maggeagvtl gqphlsrqdl ttldvtkltp lshevisrqa tinigtighv ahgkstvvka
       61 isgvhtvrfk nelernitik lgyanakiyk lddpscprpe cyrscgsstp defptdipgt
      121 kgnfklvrhv sfvdcpghdi lmatmlngaa vmdaalllia gnescpqpqt sehlaaieim
      181 klkhililqn kidlvkesqa keqyeqilaf vqgtvaegap iipisaqlky nievvceyiv
      241 kkipvpprdf tseprlivir sfdvnkpgce vddlkggvag gsilkgvlkv gqeievrpgi
      301 vskdsegklm ckpifskivs lfaehndlqy aapggligvg tkidptlcra drmvgqvlga
      361 vgalpeifte leisyfllrr llgvrtegdk kaakvqklsk nevlmvnigs lstggrvsav
      421 kadlgkivlt npvctevgek ialsrrvekh wrligwgqir rgvtikptvd dd
//
LOCUS       NP_005659                359 aa            linear   PRI 27-APR-2025
DEFINITION  CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase isoform a
            precursor [Homo sapiens].
ACCESSION   NP_005659
VERSION     NP_005659.1
DBSOURCE    REFSEQ: accession NM_005668.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Hatanaka,R., Hane,M., Hayakawa,K., Morishita,S., Ohno,S.,
            Yamaguchi,Y., Wu,D., Kitajima,K. and Sato,C.
  TITLE     Identification of a buried beta-strand as a novel disease-related
            motif in the human polysialyltransferases
  JOURNAL   J Biol Chem 300 (1), 105564 (2024)
   PUBMED   38103644
  REMARK    GeneRIF: Identification of a buried beta-strand as a novel
            disease-related motif in the human polysialyltransferases.
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Mori,A., Hane,M., Niimi,Y., Kitajima,K. and Sato,C.
  TITLE     Different properties of polysialic acids synthesized by the
            polysialyltransferases ST8SIA2 and ST8SIA4
  JOURNAL   Glycobiology 27 (9), 834-846 (2017)
   PUBMED   28810663
  REMARK    GeneRIF: Different properties of polysialic acids synthesized by
            the polysialyltransferases ST8SIA2 and ST8SIA4 have been described.
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Ma,W., Zhao,X., Liang,L., Wang,G., Li,Y., Miao,X. and Zhao,Y.
  TITLE     miR-146a and miR-146b promote proliferation, migration and invasion
            of follicular thyroid carcinoma via inhibition of ST8SIA4
  JOURNAL   Oncotarget 8 (17), 28028-28041 (2017)
   PUBMED   28427206
  REMARK    GeneRIF: our results demonstrate that miR-146a and miR-146b promote
            proliferation, migration and invasion of FTC via inhibition of
            ST8SIA4.
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Bhide,G.P., Prehna,G., Ramirez,B.E. and Colley,K.J.
  TITLE     The Polybasic Region of the Polysialyltransferase ST8Sia-IV Binds
            Directly to the Neural Cell Adhesion Molecule, NCAM
  JOURNAL   Biochemistry 56 (10), 1504-1517 (2017)
   PUBMED   28233978
  REMARK    GeneRIF: The polybasic region of the polysialyltransferase
            ST8Sia-IV binds directly to NCAM.
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Ma,X., Dong,W., Su,Z., Zhao,L., Miao,Y., Li,N., Zhou,H. and Jia,L.
  TITLE     Functional roles of sialylation in breast cancer progression
            through miR-26a/26b targeting ST8SIA4
  JOURNAL   Cell Death Dis 7 (12), e2561 (2016)
   PUBMED   28032858
  REMARK    GeneRIF: changes in the glycosylation patterns and sialylation
            levels may be useful markers of the progression of breast cancer,
            as well as miR-26a/26b may be widely involved in the regulation of
            sialylation machinery by targeting ST8SIA4.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Close,B.E. and Colley,K.J.
  TITLE     In vivo autopolysialylation and localization of the
            polysialyltransferases PST and STX
  JOURNAL   J Biol Chem 273 (51), 34586-34593 (1998)
   PUBMED   9852130
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Angata,K., Suzuki,M. and Fukuda,M.
  TITLE     Differential and cooperative polysialylation of the neural cell
            adhesion molecule by two polysialyltransferases, PST and STX
  JOURNAL   J Biol Chem 273 (43), 28524-28532 (1998)
   PUBMED   9774483
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Angata,K., Nakayama,J., Fredette,B., Chong,K., Ranscht,B. and
            Fukuda,M.
  TITLE     Human STX polysialyltransferase forms the embryonic form of the
            neural cell adhesion molecule. Tissue-specific expression, neurite
            outgrowth, and chromosomal localization in comparison with another
            polysialyltransferase, PST
  JOURNAL   J Biol Chem 272 (11), 7182-7190 (1997)
   PUBMED   9054414
REFERENCE   9  (residues 1 to 359)
  AUTHORS   Nakayama,J., Fukuda,M.N., Fredette,B., Ranscht,B. and Fukuda,M.
  TITLE     Expression cloning of a human polysialyltransferase that forms the
            polysialylated neural cell adhesion molecule present in embryonic
            brain
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7031-7035 (1995)
   PUBMED   7624364
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Eckhardt,M., Muhlenhoff,M., Bethe,A., Koopman,J., Frosch,M. and
            Gerardy-Schahn,R.
  TITLE     Molecular characterization of eukaryotic polysialyltransferase-1
  JOURNAL   Nature 373 (6516), 715-718 (1995)
   PUBMED   7854457
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA862968.1, AK292872.1,
            AC117530.2 and AA836260.1.
            
            Summary: The protein encoded by this gene catalyzes the
            polycondensation of alpha-2,8-linked sialic acid required for the
            synthesis of polysialic acid, a modulator of the adhesive
            properties of neural cell adhesion molecule (NCAM1). The encoded
            protein, which is a member of glycosyltransferase family 29, is a
            type II membrane protein that may be present in the Golgi
            apparatus. Two transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.144379.1,
                                           SRR1660803.80785.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000231461.10/ ENSP00000231461.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q21.1"
     Protein         1..359
                     /product="CMP-N-acetylneuraminate-poly-alpha-2,
                     8-sialyltransferase isoform a precursor"
                     /EC_number="2.4.99.-"
                     /note="sialyltransferase 8 (alpha-2,
                     8-polysialytransferase) D;
                     CMP-N-acetylneuraminate-poly-alpha-2,8-sialyl transferase;
                     polysialyltransferase-1; alpha-2,8-sialyltransferase 8D;
                     CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase;
                     sialytransferase St8Sia IV; sialyltransferase St8Sia IV;
                     ST8 alpha-N-acetylneuraminate alpha-2,8-sialyltransferase
                     4"
                     /calculated_mol_wt=37972
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3341
     Site            8..20
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92187.1)"
     mat_peptide     27..359
                     /product="CMP-N-acetylneuraminate-poly-alpha-2,
                     8-sialyltransferase isoform a"
                     /calculated_mol_wt=38128
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92187.1)"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:11279095; propagated from
                     UniProtKB/Swiss-Prot (Q92187.1)"
     Region          76..353
                     /region_name="GT29_ST8SIA4"
                     /note="alpha-N-acetylneuraminide
                     alpha-2,8-sialyltransferase 4; cd23988"
                     /db_xref="CDD:467716"
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92187.1)"
     Site            order(146..148,169..170,191,279..281,299..300,313..315,
                     331)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:467716"
     Site            204
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92187.1)"
     Site            219
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92187.1)"
     CDS             1..359
                     /gene="ST8SIA4"
                     /gene_synonym="PST; PST1; SIAT8-D; SIAT8D; ST8SIA-IV;
                     ST8SiaIV"
                     /coded_by="NM_005668.6:328..1407"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4091.1"
                     /db_xref="GeneID:7903"
                     /db_xref="HGNC:HGNC:10871"
                     /db_xref="MIM:602547"
ORIGIN      
        1 mrsirkrwti ctislllify ktkeiartee hqetqligdg elslsrslvn ssdkiirkag
       61 ssifqhnveg wkinsslvle irknilrfld aerdvsvvks sfkpgdvihy vldrrrtlni
      121 shdlhsllpe vspmknrrfk tcavvgnsgi lldsecgkei dshnfvircn lapvvefaad
      181 vgtksdfitm npsvvqrafg gfrnesdrek fvhrlsmlnd svlwipafmv kggekhvewv
      241 nalilknklk vrtaypslrl ihavrgywlt nkvpikrpst gllmytlatr fcdeihlygf
      301 wpfpkdlngk avkyhyyddl kyryfsnasp hrmplefktl nvlhnrgalk lttgkcvkq
//
LOCUS       NP_078919                456 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger C2HC domain-containing protein 1C isoform a [Homo
            sapiens].
ACCESSION   NP_078919
VERSION     NP_078919.2
DBSOURCE    REFSEQ: accession NM_024643.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Qiao,Y., Shao,T., Chen,Y., Chen,J., Sun,X. and Chen,X.
  TITLE     Screening of candidate genes at GLC3B and GLC3C loci in Chinese
            primary congenital glaucoma patients with targeted next generation
            sequencing
  JOURNAL   Ophthalmic Genet 44 (2), 133-138 (2023)
   PUBMED   36193031
  REMARK    GeneRIF: Screening of candidate genes at GLC3B and GLC3C loci in
            Chinese primary congenital glaucoma patients with targeted next
            generation sequencing.
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY031397.1, AK026746.1, AL049780.4 and AK223359.1.
            
            On Jun 22, 2006 this sequence version replaced NP_078919.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.95260.1,
                                           SRR1660803.70129.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000524913.3/ ENSP00000435550.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..456
                     /product="zinc finger C2HC domain-containing protein 1C
                     isoform a"
                     /note="protein FAM164C; family with sequence similarity
                     164, member C; zinc finger C2HC domain-containing protein
                     1C"
                     /calculated_mol_wt=51527
     Region          16..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53FD0.3)"
     Region          85..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53FD0.3)"
     Region          336..388
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53FD0.3)"
     Region          387..410
                     /region_name="zf-C2HC_2"
                     /note="zinc-finger of a C2HC-type; pfam13913"
                     /db_xref="CDD:464037"
     CDS             1..456
                     /gene="ZC2HC1C"
                     /gene_synonym="C14orf140; FAM164C"
                     /coded_by="NM_024643.4:129..1499"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41972.1"
                     /db_xref="GeneID:79696"
                     /db_xref="HGNC:HGNC:20354"
ORIGIN      
        1 maglqrlash lpvgvmlphn tteapgphsa kqdsyeqgds sqqslkghlr nnfqkqllsn
       61 kelildkvyt hpkwntqtka rsysyphctg isqqdpesds qgqgnglfys sgpqswypka
      121 nnqdfipftk krvgvdrafp lkpmvhrksc stgeagtdgd hnvyprppep refssrnfgv
      181 rnqgnfsvvg tvlaatqaek avanfdrtew vqirrleaag esleeeirrk qillrgklkk
      241 teeelrriqt qkeqakenen gelqkiilpr srvkgnksnt mykpifspef efeeefsrdr
      301 redetwgrsq qnsgpfqfsd yriqrlkrer lvasnnkird pvsepsvekf sppsetpvga
      361 lqgsarnssl smapdssgss gsieepqlge cshcgrkfls frlerhsnic srmrgskrkv
      421 fdssrarakg teleqylnwk gpasakaepp qksnwr
//
LOCUS       NP_001356702             558 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger imprinted 2 isoform a [Homo sapiens].
ACCESSION   NP_001356702
VERSION     NP_001356702.1
DBSOURCE    REFSEQ: accession NM_001369773.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Kim,J., Bergmann,A., Lucas,S., Stone,R. and Stubbs,L.
  TITLE     Lineage-specific imprinting and evolution of the zinc-finger gene
            ZIM2
  JOURNAL   Genomics 84 (1), 47-58 (2004)
   PUBMED   15203203
  REMARK    GeneRIF: ZIM2 gene, like the co-transcribed PEG3 gene, is imprinted
            in human, with preferential expression from the paternal allele.
            The imprinting status of ZIM2 is not conserved among mammals.
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Kim,J., Bergmann,A. and Stubbs,L.
  TITLE     Exon sharing of a novel human zinc-finger gene, ZIM2, and
            paternally expressed gene 3 (PEG3)
  JOURNAL   Genomics 64 (1), 114-118 (2000)
   PUBMED   10708526
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006115.1.
            
            Summary: In human, ZIM2 and PEG3 (GeneID:5178) are two distinct
            genes that share a set of 5' exons and have a common promoter, and
            both genes are paternally expressed. Alternative splicing events
            connect the shared exons either with the remaining 4 exons unique
            to ZIM2, or with the remaining 2 exons unique to PEG3. This is in
            contrast to mouse and cow, where ZIM2 and PEG3 genes do not share
            exons in common, and the imprinting status of ZIM2 is also not
            conserved amongst mammals. Additional 5' alternatively spliced
            transcripts encoding the same protein have been found for the human
            ZIM2 gene. [provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (7), as well as variants 8 and 13,
            encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.635606.1,
                                           SRR5189664.160525.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 15203203
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..558
                     /product="zinc finger imprinted 2 isoform a"
                     /note="zinc finger protein 656"
                     /calculated_mol_wt=64386
     Region          207..263
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          361..381
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          373..396
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          389..409
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          445..465
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(450,452,454,456..457,460..461,464,504,506,510..511,
                     514..515,518,532,534,536,538..539,542..543,546)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          497..519
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          499..519
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          511..534
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          525..547
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          527..547
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..558
                     /gene="ZIM2"
                     /gene_synonym="ZNF656"
                     /coded_by="NM_001369773.1:383..2059"
                     /note="isoform a is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS92697.1"
                     /db_xref="GeneID:23619"
                     /db_xref="HGNC:HGNC:12875"
ORIGIN      
        1 myqpeddnns dvtsdddmtr nrresspphs vhsfsgdrdw drrgrsrdme prdrwshtrn
       61 prsrmpprdl slpvvaktsf emdreddrds rayesrsqda esyqnvvdla edrkphntiq
      121 dnmenyrkll slgvqlaedd ghshmtqghs srskrsayps tsrgflaqds vpaekrntem
      181 ldnlpsagsq fpdfkhlgtf lvfeelvtfe dvlvdfspee lsslsaaqrn lyrevmleny
      241 rnlvslghqf skpdiisrle eeesyametd srhtvicqge shddplephq gnqeklltpi
      301 tmndpktltp ersygsdefe rssnlskqsk dplgkdpqeg tapgictspq sasqenkhnr
      361 cefckrtfst qvalrrheri htgkkpyeck qcaeafylmp hlnrhqkths grktsgcneg
      421 rkpsvqcanl cervrihsqe dyfecfqcgk aflqnvhllq hlkaheaarv lppglshskt
      481 yliryqrkhd yvgeracqcc dcgrvfsrns yliqhyrtht qerpyqcqlc gkcfgrpsyl
      541 tqhyqlhsqe ktvecdhc
//
LOCUS       NP_001350                335 aa            linear   PRI 27-APR-2025
DEFINITION  2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial
            isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001350
VERSION     NP_001350.1
DBSOURCE    REFSEQ: accession NM_001359.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Guo,S., Jiang,H., Deng,Y., Dong,Y., Yin,A., Wang,Q., Lan,Q.,
            Zhang,Y. and Xu,C.
  TITLE     Reduced 2,4-dienoyl-CoA reductase 1 is served as an unfavorable
            biomarker and is related to immune infiltration in cervical cancer
  JOURNAL   J Obstet Gynaecol Res 49 (10), 2475-2486 (2023)
   PUBMED   37497824
  REMARK    GeneRIF: Reduced 2,4-dienoyl-CoA reductase 1 is served as an
            unfavorable biomarker and is related to immune infiltration in
            cervical cancer.
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Zhou,H., Zhang,J., Yan,Z., Qu,M., Zhang,G., Han,J., Wang,F.,
            Sun,K., Wang,L. and Yang,X.
  TITLE     DECR1 directly activates HSL to promote lipolysis in cervical
            cancer cells
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1867 (3), 159090 (2022)
   PUBMED   34896618
  REMARK    GeneRIF: DECR1 directly activates HSL to promote lipolysis in
            cervical cancer cells.
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Fang,J., Sheng,R. and Qin,Z.H.
  TITLE     NADPH Oxidases in the Central Nervous System: Regional and Cellular
            Localization and the Possible Link to Brain Diseases
  JOURNAL   Antioxid Redox Signal 35 (12), 951-973 (2021)
   PUBMED   34293949
  REMARK    GeneRIF: NADPH Oxidases in the Central Nervous System: Regional and
            Cellular Localization and the Possible Link to Brain Diseases.
            Review article
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Santos,C.G.M., Rolim-Filho,N.G., Domingues,C.A.,
            Dornelas-Ribeiro,M., King,J.L., Budowle,B., Moura-Neto,R.S. and
            Silva,R.
  TITLE     Association of whole mtDNA, an NADPH G11914A variant, and
            haplogroups with high physical performance in an elite military
            troop
  JOURNAL   Braz J Med Biol Res 54 (6), e10317 (2021)
   PUBMED   33909855
  REMARK    GeneRIF: Association of whole mtDNA, an NADPH G11914A variant, and
            haplogroups with high physical performance in an elite military
            troop.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Koivuranta,K.T., Hakkola,E.H. and Hiltunen,J.K.
  TITLE     Isolation and characterization of cDNA for human 120 kDa
            mitochondrial 2,4-dienoyl-coenzyme A reductase
  JOURNAL   Biochem J 304 (Pt 3) (Pt 3), 787-792 (1994)
   PUBMED   7818482
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Luo,M.J., Smeland,T.E., Shoukry,K. and Schulz,H.
  TITLE     Delta 3,5, delta 2,4-dienoyl-CoA isomerase from rat liver
            mitochondria. Purification and characterization of a new enzyme
            involved in the beta-oxidation of unsaturated fatty acids
  JOURNAL   J Biol Chem 269 (4), 2384-2388 (1994)
   PUBMED   8300563
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Smeland,T.E., Nada,M., Cuebas,D. and Schulz,H.
  TITLE     NADPH-dependent beta-oxidation of unsaturated fatty acids with
            double bonds extending from odd-numbered carbon atoms
  JOURNAL   Proc Natl Acad Sci U S A 89 (15), 6673-6677 (1992)
   PUBMED   1495956
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Nishimaki-Mogami,T., Tanaka,A., Minegishi,K. and Takahashi,A.
  TITLE     Effect of sorbic acid feeding on peroxisomes and sorboyl-CoA
            metabolizing enzymes in mouse liver. Selective induction of
            2,4-dienoyl-CoA hydratase
  JOURNAL   Biochem Pharmacol 42 (2), 239-246 (1991)
   PUBMED   1859445
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Dommes,V., Baumgart,C. and Kunau,W.H.
  TITLE     Degradation of unsaturated fatty acids in peroxisomes. Existence of
            a 2,4-dienoyl-CoA reductase pathway
  JOURNAL   J Biol Chem 256 (16), 8259-8262 (1981)
   PUBMED   7263650
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC105080.1, H98841.1,
            CR737790.1, CB104585.1, AC004612.1 and AA725334.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.270996.1,
                                           SRR1660809.40469.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000220764.7/
                                                  ENSP00000220764.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.3"
     Protein         1..335
                     /product="2,4-dienoyl-CoA reductase
                     [(3E)-enoyl-CoA-producing], mitochondrial isoform 1
                     precursor"
                     /EC_number="1.3.1.124"
                     /note="4-enoyl-CoA reductase; 2,4-dienoyl-CoA reductase,
                     mitochondrial; short chain dehydrogenase/reductase family
                     18C member 1; 2,4-dienoyl-CoA reductase 1, mitochondrial;
                     2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing],
                     mitochondrial"
                     /calculated_mol_wt=32150
     transit_peptide 1..34
                     /note="Mitochondrion.
                     /evidence=ECO:0000305|PubMed:7818482; propagated from
                     UniProtKB/Swiss-Prot (Q16698.1)"
                     /calculated_mol_wt=3936
     mat_peptide     35..335
                     /product="2,4-dienoyl-CoA reductase
                     [(3E)-enoyl-CoA-producing], mitochondrial.
                     /id=PRO_0000031965"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16698.1)"
                     /calculated_mol_wt=32150
     Site            42
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ62; propagated from
                     UniProtKB/Swiss-Prot (Q16698.1)"
     Site            49
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ62; propagated from
                     UniProtKB/Swiss-Prot (Q16698.1)"
     Region          57..303
                     /region_name="TER_DECR_SDR_a"
                     /note="Trans-2-enoyl-CoA reductase (TER) and
                     2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR;
                     cd05369"
                     /db_xref="CDD:187627"
     Site            order(66,69..71,90..92,116..119,144..146,167,195..197,214,
                     240..243,245)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16698.1)"
     Site            order(91,119,146..149,157,159..160,163,197,199,210,242)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ62; propagated from
                     UniProtKB/Swiss-Prot (Q16698.1)"
     Site            order(121,152..154,156..158,161..162,165,169..170,
                     173..174,177,181,184,189,199,203..206,208,211..212,
                     215..216,219..220,222..229,231,242,266..268,270..272,276,
                     279..280,283,288,290..295,297..303)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
     Site            order(148,199,210,214)
                     /site_type="active"
                     /db_xref="CDD:187627"
     Site            order(152..154,156,161..162,165,170,173..174,203..206,208,
                     211..212,215..216,219..220,223,226..227)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
     Site            230
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q16698.1)"
     Site            244
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ62; propagated from
                     UniProtKB/Swiss-Prot (Q16698.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ62; propagated from
                     UniProtKB/Swiss-Prot (Q16698.1)"
     Site            319
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ62; propagated from
                     UniProtKB/Swiss-Prot (Q16698.1)"
     CDS             1..335
                     /gene="DECR1"
                     /gene_synonym="DECR; NADPH; SDR18C1"
                     /coded_by="NM_001359.2:17..1024"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS6250.1"
                     /db_xref="GeneID:1666"
                     /db_xref="HGNC:HGNC:2753"
                     /db_xref="MIM:222745"
ORIGIN      
        1 mklparvfft lgsrlpcgla prrffsygtk ilyqntealq skffsplqka mlppnsfqgk
       61 vafitgggtg lgkgmttlls slgaqcvias rkmdvlkata eqissqtgnk vhaiqcdvrd
      121 pdmvqntvse likvaghpni vinnaagnfi spterlspna wktitdivln gtafvtleig
      181 kqlikaqkga aflsittiya etgsgfvvps asakagveam skslaaewgk ygmrfnviqp
      241 gpiktkgafs rldptgtfek emigripcgr lgtveelanl aaflcsdyas wingavikfd
      301 ggeevlisge fndlrkvtke qwdtieelir ktkgs
//
LOCUS       NP_001350707             275 aa            linear   PRI 27-APR-2025
DEFINITION  synaptogyrin-2 isoform 3 [Homo sapiens].
ACCESSION   NP_001350707 XP_005257849
VERSION     NP_001350707.1
DBSOURCE    REFSEQ: accession NM_001363778.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Liu,C., Qu,Z., Zhao,H., Wang,P., Zhan,C. and Zhang,Y.
  TITLE     Pan-cancer analysis of SYNGR2 with a focus on clinical implications
            and immune landscape in liver hepatocellular carcinoma
  JOURNAL   BMC Bioinformatics 24 (1), 192 (2023)
   PUBMED   37170221
  REMARK    GeneRIF: Pan-cancer analysis of SYNGR2 with a focus on clinical
            implications and immune landscape in liver hepatocellular
            carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Sun,Q., Qi,X., Zhang,Y., Wu,X., Liang,M., Li,C., Li,D.,
            Cardona,C.J. and Xing,Z.
  TITLE     Synaptogyrin-2 Promotes Replication of a Novel Tick-borne
            Bunyavirus through Interacting with Viral Nonstructural Protein NSs
  JOURNAL   J Biol Chem 291 (31), 16138-16149 (2016)
   PUBMED   27226560
  REMARK    GeneRIF: synaptogyrin-2 is essential to promoting the formation of
            the IBs to become virus factories for viral RNA replication through
            its interaction with NSs. These findings unveil the function of
            synaptogyrin-2 as an enhancer in viral infection.
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Kedra,D., Pan,H.Q., Seroussi,E., Fransson,I., Guilbaud,C.,
            Collins,J.E., Dunham,I., Blennow,E., Roe,B.A., Piehl,F. and
            Dumanski,J.P.
  TITLE     Characterization of the human synaptogyrin gene family
  JOURNAL   Hum Genet 103 (2), 131-141 (1998)
   PUBMED   9760194
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Janz,R. and Sudhof,T.C.
  TITLE     Cellugyrin, a novel ubiquitous form of synaptogyrin that is
            phosphorylated by pp60c-src
  JOURNAL   J Biol Chem 273 (5), 2851-2857 (1998)
   PUBMED   9446595
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021593.15 and BC105992.1.
            
            On Jun 3, 2018 this sequence version replaced XP_005257849.1.
            
            Summary: This gene encodes an integral membrane protein containing
            four transmembrane regions and a C-terminal cytoplasmic tail that
            is tyrosine phosphorylated. The exact function of this protein is
            unclear, but studies of a similar rat protein suggest that it may
            play a role in regulating membrane traffic in non-neuronal cells.
            The gene belongs to the synaptogyrin gene family. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Feb 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.792593.1,
                                           SRR3476690.1140746.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..275
                     /product="synaptogyrin-2 isoform 3"
                     /note="cellugyrin"
                     /calculated_mol_wt=30244
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (O43760.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43760.1)"
     Region          20..161
                     /region_name="MARVEL"
                     /note="Membrane-associating domain; pfam01284"
                     /db_xref="CDD:366555"
     Site            26..46
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43760.1)"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43760.1)"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43760.1)"
     CDS             1..275
                     /gene="SYNGR2"
                     /coded_by="NM_001363778.1:73..900"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS86641.1"
                     /db_xref="GeneID:9144"
                     /db_xref="HGNC:HGNC:11499"
                     /db_xref="MIM:603926"
ORIGIN      
        1 mesgaygaak aggsfdlrrf ltqpqvvara vclvfalivf sciygegysn aheskqmycv
       61 fnrnedacry gsaigvlafl asafflvvda yfpqisnatd rkylvigdll fsalwtflwf
      121 vgfcfltnqw avtnpkdvlv gadsvraait fsffsifswv gwpgagswvk ggggwgpppt
      181 ctllcspcrv cwppwptsat rlawttssri tltplrtptl ptpptqvhlw tttnshpspr
      241 trrppratsr plcterrlaw eggqrgpspl pwtfp
//
LOCUS       NP_001161                342 aa            linear   PRI 27-APR-2025
DEFINITION  aquaporin-7 isoform 1 [Homo sapiens].
ACCESSION   NP_001161
VERSION     NP_001161.1
DBSOURCE    REFSEQ: accession NM_001170.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Liu,J., Xia,Z., Peng,S., Xia,J., Xu,R., Wang,X., Li,F. and Zhu,W.
  TITLE     The Important Role of Aquaglyceroporin 7 in Health and Disease
  JOURNAL   Biomolecules 14 (10), 1228 (2024)
   PUBMED   39456161
  REMARK    GeneRIF: The Important Role of Aquaglyceroporin 7 in Health and
            Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Ribeiro,J.C., Bernardino,R.L., Goncalves,A., Barros,A.,
            Calamita,G., Alves,M.G. and Oliveira,P.F.
  TITLE     Aquaporin-7-Mediated Glycerol Permeability Is Linked to Human Sperm
            Motility in Asthenozoospermia and during Sperm Capacitation
  JOURNAL   Cells 12 (15), 2003 (2023)
   PUBMED   37566082
  REMARK    GeneRIF: Aquaporin-7-Mediated Glycerol Permeability Is Linked to
            Human Sperm Motility in Asthenozoospermia and during Sperm
            Capacitation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Huang,P., Venskutonyte,R., Prasad,R.B., Ardalani,H., de Mare,S.W.,
            Fan,X., Li,P., Spegel,P., Yan,N., Gourdon,P., Artner,I. and
            Lindkvist-Petersson,K.
  TITLE     Cryo-EM structure supports a role of AQP7 as a junction protein
  JOURNAL   Nat Commun 14 (1), 600 (2023)
   PUBMED   36737436
  REMARK    GeneRIF: Cryo-EM structure supports a role of AQP7 as a junction
            protein.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Plaza,A., Merino,B. and Ruiz-Gayo,M.
  TITLE     Cholecystokinin promotes functional expression of the aquaglycerol
            channel aquaporin 7 in adipocytes
  JOURNAL   Br J Pharmacol 179 (16), 4092-4106 (2022)
   PUBMED   35366004
  REMARK    GeneRIF: Cholecystokinin promotes functional expression of the
            aquaglycerol channel aquaporin 7 in adipocytes.
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Kondo,H., Shimomura,I., Kishida,K., Kuriyama,H., Makino,Y.,
            Nishizawa,H., Matsuda,M., Maeda,N., Nagaretani,H., Kihara,S.,
            Kurachi,Y., Nakamura,T., Funahashi,T. and Matsuzawa,Y.
  TITLE     Human aquaporin adipose (AQPap) gene. Genomic structure, promoter
            analysis and functional mutation
  JOURNAL   Eur J Biochem 269 (7), 1814-1826 (2002)
   PUBMED   11952783
  REMARK    GeneRIF: determination of genomic structure, promotor analysis and
            functional mutation
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Ishibashi,K., Yamauchi,K., Kageyama,Y., Saito-Ohara,F., Ikeuchi,T.,
            Marumo,F. and Sasaki,S.
  TITLE     Molecular characterization of human Aquaporin-7 gene and its
            chromosomal mapping
  JOURNAL   Biochim Biophys Acta 1399 (1), 62-66 (1998)
   PUBMED   9714739
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Ishibashi,K., Kuwahara,M., Gu,Y., Kageyama,Y., Tohsaka,A.,
            Suzuki,F., Marumo,F. and Sasaki,S.
  TITLE     Cloning and functional expression of a new water channel abundantly
            expressed in the testis permeable to water, glycerol, and urea
  JOURNAL   J Biol Chem 272 (33), 20782-20786 (1997)
   PUBMED   9252401
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Raina,S., Preston,G.M., Guggino,W.B. and Agre,P.
  TITLE     Molecular cloning and characterization of an aquaporin cDNA from
            salivary, lacrimal, and respiratory tissues
  JOURNAL   J Biol Chem 270 (4), 1908-1912 (1995)
   PUBMED   7530250
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC306826.1, AB006190.1,
            DQ786216.1 and AL356218.22.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the aquaporin family of
            water-selective membrane channels. The encoded protein localizes to
            the plasma membrane and allows movement of water, glycerol and urea
            across cell membranes. This gene is highly expressed in the adipose
            tissue where the encoded protein facilitates efflux of glycerol. In
            the proximal straight tubules of kidney, the encoded protein is
            localized to the apical membrane and prevents excretion of glycerol
            into urine. The encoded protein is present in spermatids, as well
            as in the testicular and epididymal spermatozoa suggesting an
            important role in late spermatogenesis. Alternative splicing of
            this gene results in multiple transcript variants encoding
            different isoforms. This gene is located adjacent to a related
            aquaporin gene on chromosome 9. Multiple pseudogenes of this gene
            have been identified. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Variants 1 and 8 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.19154.1,
                                           SRR5189655.46040.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297988.6/ ENSP00000297988.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..342
                     /product="aquaporin-7 isoform 1"
                     /note="aquaporin adipose; aquaglyceroporin-7"
                     /calculated_mol_wt=37101
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56403; propagated from
                     UniProtKB/Swiss-Prot (O14520.1)"
     Region          31..280
                     /region_name="MIP"
                     /note="Major intrinsic protein (MIP) superfamily. Members
                     of the MIP superfamily function as membrane channels that
                     selectively transport water, small neutral molecules, and
                     ions out of and between cells. The channel proteins share
                     a common fold: the N-terminal...; cl00200"
                     /db_xref="CDD:444743"
     Site            37..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14520.1)"
     Site            68..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14520.1)"
     Site            order(74,92..94,222..223,226,229)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            74
                     /site_type="other"
                     /note="Selectivity filter.
                     /evidence=ECO:0000305|PubMed:36737436; propagated from
                     UniProtKB/Swiss-Prot (O14520.1)"
     Site            order(94..96,226..228)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     Region          94..96
                     /region_name="NPA 1.
                     /evidence=ECO:0000305|PubMed:36737436"
                     /note="propagated from UniProtKB/Swiss-Prot (O14520.1)"
     Site            112..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14520.1)"
     Site            135
                     /site_type="other"
                     /note="Important for permeability to glycerol.
                     /evidence=ECO:0000269|PubMed:30423801; propagated from
                     UniProtKB/Swiss-Prot (O14520.1)"
     Site            171..188
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14520.1)"
     Site            201..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14520.1)"
     Site            223
                     /site_type="other"
                     /note="Selectivity filter.
                     /evidence=ECO:0000305|PubMed:36737436; propagated from
                     UniProtKB/Swiss-Prot (O14520.1)"
     Region          226..228
                     /region_name="NPA 2.
                     /evidence=ECO:0000305|PubMed:36737436"
                     /note="propagated from UniProtKB/Swiss-Prot (O14520.1)"
     Site            229
                     /site_type="other"
                     /note="Selectivity filter.
                     /evidence=ECO:0000305|PubMed:36737436; propagated from
                     UniProtKB/Swiss-Prot (O14520.1)"
     Site            254..275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14520.1)"
     CDS             1..342
                     /gene="AQP7"
                     /gene_synonym="AQP7L; AQPap; GLYCQTL"
                     /coded_by="NM_001170.3:222..1250"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6541.1"
                     /db_xref="GeneID:364"
                     /db_xref="HGNC:HGNC:640"
                     /db_xref="MIM:602974"
ORIGIN      
        1 mvqasghrrs trgskmvsws viakiqeilq rkmvreflae fmstyvmmvf glgsvahmvl
       61 nkkygsylgv nlgfgfgvtm gvhvagrisg ahmnaavtfa ncalgrvpwr kfpvyvlgqf
      121 lgsflaaati yslfytailh fsggqlmvtg pvatagifat ylpdhmtlwr gflneawltg
      181 mlqlclfait dqennpalpg tealvigilv viigvslgmn tgyainpsrd lppriftfia
      241 gwgkqvfsng enwwwvpvva pllgaylggi iylvfigsti preplkleds vayedhgitv
      301 lpkmgshept ispltpvsvs panrssvhpa pplhesmale hf
//
LOCUS       NP_937791                756 aa            linear   PRI 27-APR-2025
DEFINITION  inactive carboxypeptidase-like protein X2 precursor [Homo sapiens].
ACCESSION   NP_937791 XP_058409
VERSION     NP_937791.2
DBSOURCE    REFSEQ: accession NM_198148.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Grabowski,K., Herlan,L., Witten,A., Qadri,F., Eisenreich,A.,
            Lindner,D., Schadlich,M., Schulz,A., Subrova,J., Mhatre,K.N.,
            Primessnig,U., Plehm,R., van Linthout,S., Escher,F., Bader,M.,
            Stoll,M., Westermann,D., Heinzel,F.R. and Kreutz,R.
  TITLE     Cpxm2 as a novel candidate for cardiac hypertrophy and failure in
            hypertension
  JOURNAL   Hypertens Res 45 (2), 292-307 (2022)
   PUBMED   34916661
  REMARK    GeneRIF: Cpxm2 as a novel candidate for cardiac hypertrophy and
            failure in hypertension.
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Zhao,X., Li,R., Wang,Q., Wu,M. and Wang,Y.
  TITLE     Overexpression of carboxypeptidase X M14 family member 2 predicts
            an unfavorable prognosis and promotes proliferation and migration
            of osteosarcoma
  JOURNAL   Diagn Pathol 14 (1), 118 (2019)
   PUBMED   31651348
  REMARK    GeneRIF: imply an active role for Carboxypeptidase X, M14 family
            member 2 in promoting tumor aggressiveness via epithelial to
            mesenchymal transition (EMT) modulation in osteosarcoma
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Niu,G., Yang,Y., Ren,J., Song,T., Hu,Z., Chen,L., Hong,R., Xia,J.,
            Ke,C. and Wang,X.
  TITLE     Overexpression of CPXM2 predicts an unfavorable prognosis and
            promotes the proliferation and migration of gastric cancer
  JOURNAL   Oncol Rep 42 (4), 1283-1294 (2019)
   PUBMED   31364750
  REMARK    GeneRIF: Results imply an active role for CPXM2 in promoting tumor
            aggressiveness via epithelial to mesenchymal transition (EMT)
            modulation in GCs.
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Gil-Varea,E., Urcelay,E., Vilarino-Guell,C., Costa,C., Midaglia,L.,
            Matesanz,F., Rodriguez-Antiguedad,A., Oksenberg,J.,
            Espino-Paisan,L., Dessa Sadovnick,A., Saiz,A., Villar,L.M.,
            Garcia-Merino,J.A., Ramio-Torrenta,L., Trivino,J.C., Quintana,E.,
            Robles,R., Sanchez-Lopez,A., Arroyo,R., Alvarez-Cermeno,J.C.,
            Vidal-Jordana,A., Malhotra,S., Fissolo,N., Montalban,X. and
            Comabella,M.
  TITLE     Exome sequencing study in patients with multiple sclerosis reveals
            variants associated with disease course
  JOURNAL   J Neuroinflammation 15 (1), 265 (2018)
   PUBMED   30217166
  REMARK    GeneRIF: The Genetic variants located in CPXM2 have the potential
            to modulate disease course in MS patients and may be used as
            disease activity biomarkers to identify patients with divergent
            disease courses.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 756)
  AUTHORS   Chen,Y.C., Hsiao,C.J., Jung,C.C., Hu,H.H., Chen,J.H., Lee,W.C.,
            Chiou,J.M., Chen,T.F., Sun,Y., Wen,L.L., Yip,P.K., Chu,Y.M.,
            Chen,C.J. and Yang,H.I.
  TITLE     Performance Metrics for Selecting Single Nucleotide Polymorphisms
            in Late-onset Alzheimer's Disease
  JOURNAL   Sci Rep 6, 36155 (2016)
   PUBMED   27805002
  REMARK    GeneRIF: Performance metrics were used to select SNPs in stage 1,
            which were then genotyped to another dataset (stage 2). Four SNPs
            (CPXM2 rs2362967, APOC1 rs4420638, ZNF521 rs7230380, and
            rs12965520) were identified for LOAD by both traditional P-values
            (without correcting for multiple tests) and performance metrics.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 756)
  AUTHORS   Julia,A., Domenech,E., Chaparro,M., Garcia-Sanchez,V., Gomollon,F.,
            Panes,J., Manosa,M., Barreiro-De Acosta,M., Gutierrez,A.,
            Garcia-Planella,E., Aguas,M., Munoz,F., Esteve,M., Mendoza,J.L.,
            Vera,M., Marquez,L., Tortosa,R., Lopez-Lasanta,M., Alonso,A.,
            Gelpi,J.L., Garcia-Montero,A.C., Bertranpetit,J., Absher,D.,
            Myers,R.M., Gisbert,J.P. and Marsal,S.
  TITLE     A genome-wide association study identifies a novel locus at 6q22.1
            associated with ulcerative colitis
  JOURNAL   Hum Mol Genet 23 (25), 6927-6934 (2014)
   PUBMED   25082827
REFERENCE   7  (residues 1 to 756)
  AUTHORS   Siedlinski,M., Cho,M.H., Bakke,P., Gulsvik,A., Lomas,D.A.,
            Anderson,W., Kong,X., Rennard,S.I., Beaty,T.H., Hokanson,J.E.,
            Crapo,J.D. and Silverman,E.K.
  CONSRTM   COPDGene Investigators; ECLIPSE Investigators
  TITLE     Genome-wide association study of smoking behaviours in patients
            with COPD
  JOURNAL   Thorax 66 (10), 894-902 (2011)
   PUBMED   21685187
REFERENCE   8  (residues 1 to 756)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 756)
  AUTHORS   Xin,X., Day,R., Dong,W., Lei,Y. and Fricker,L.D.
  TITLE     Identification of mouse CPX-2, a novel member of the
            metallocarboxypeptidase gene family: cDNA cloning, mRNA
            distribution, and protein expression and characterization
  JOURNAL   DNA Cell Biol 17 (10), 897-909 (1998)
   PUBMED   9809751
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY358565.1 and AC009987.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 9, 2009 this sequence version replaced NP_937791.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.69107.1, AY358565.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000241305.4/ ENSP00000241305.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..756
                     /product="inactive carboxypeptidase-like protein X2
                     precursor"
                     /note="4632435C11Rik; carboxypeptidase-like protein X2;
                     carboxypeptidase Hlo; inactive carboxypeptidase-like
                     protein X2; cytosolic carboxypeptidase; carboxypeptidase X
                     (M14 family), member 2"
                     /calculated_mol_wt=83538
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2351
     mat_peptide     26..756
                     /product="Inactive carboxypeptidase-like protein X2.
                     /id=PRO_0000004409"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N436.3)"
                     /calculated_mol_wt=83538
     Region          <48..103
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          51..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N436.3)"
     Region          137..292
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            order(185,213,220)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            231
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N436.3)"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N436.3)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N436.3)"
     Region          318..639
                     /region_name="M14_CPX_like"
                     /note="Peptidase M14 carboxypeptidase subfamily N/E-like;
                     Carboxypeptidase X subgroup; cd03869"
                     /db_xref="CDD:349441"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N436.3)"
     Site            order(379,382,444,453..454,517..518,524,528,584,588,590,
                     610)
                     /site_type="active"
                     /db_xref="CDD:349441"
     Site            491
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N436.3)"
     Region          643..718
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cd11308"
                     /db_xref="CDD:200604"
     CDS             1..756
                     /gene="CPXM2"
                     /gene_synonym="CPX2; UNQ676"
                     /coded_by="NM_198148.3:149..2419"
                     /db_xref="CCDS:CCDS7637.1"
                     /db_xref="GeneID:119587"
                     /db_xref="HGNC:HGNC:26977"
                     /db_xref="MIM:617348"
ORIGIN      
        1 msrpgtatpa lalvllavtl agvgaqgaal edpdyygqei wsrepyyarp epeletfspp
       61 lpagpgeewe rrpqeprppk ratkpkkapk reksapeppp pgkhsnkkvm rtkssekaan
      121 ddhsvrvare dvrescpplg letlkitdfq lhastvkryg lgahrgrlni qaginendfy
      181 dgawcagrnd lqqwievdar rltrftgvit qgrnslwlsd wvtsykvmvs ndshtwvtvk
      241 ngsgdmifeg nsekeipvln elpvpmvary irinpqswfd ngsicmrmei lgcplpdpnn
      301 yyhrrnemtt tddldfkhhn ykemrqlmkv vnemcpnitr iynigkshqg lklyaveisd
      361 hpgehevgep efhyiagahg nevlgrelll llvqfvcqey larnarivhl veetrihvlp
      421 slnpdgyeka yeggselggw slgrwthdgi dinnnfpdln tllweaedrq nvprkvpnhy
      481 iaipewflse natvaaetra viawmekipf vlggnlqgge lvvaypydlv rspwktqeht
      541 ptpddhvfrw laysyasthr lmtdarrrvc htedfqkeeg tvngaswhtv agslndfsyl
      601 htncfelsiy vgcdkyphes qlpeewennr eslivfmeqv hrgikglvrd shgkgipnai
      661 isveginhdi rtandgdywr llnpgeyvvt akaegftast kncmvgydmg atrcdftlsk
      721 tnmarireim ekfgkqpvsl parrlklrgq krrqrg
//
LOCUS       NP_597731                923 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 721 [Homo sapiens].
ACCESSION   NP_597731 XP_496681
VERSION     NP_597731.2
DBSOURCE    REFSEQ: accession NM_133474.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Kimura,K., Wakamatsu,A., Suzuki,Y., Ota,T., Nishikawa,T.,
            Yamashita,R., Yamamoto,J., Sekine,M., Tsuritani,K., Wakaguri,H.,
            Ishii,S., Sugiyama,T., Saito,K., Isono,Y., Irie,R., Kushida,N.,
            Yoneyama,T., Otsuka,R., Kanda,K., Yokoi,T., Kondo,H., Wagatsuma,M.,
            Murakawa,K., Ishida,S., Ishibashi,T., Takahashi-Fujii,A.,
            Tanase,T., Nagai,K., Kikuchi,H., Nakai,K., Isogai,T. and Sugano,S.
  TITLE     Diversification of transcriptional modulation: large-scale
            identification and characterization of putative alternative
            promoters of human genes
  JOURNAL   Genome Res 16 (1), 55-65 (2006)
   PUBMED   16344560
REFERENCE   3  (residues 1 to 923)
  AUTHORS   Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R.,
            Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H.,
            Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T.,
            Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y.,
            Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M.,
            Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H.,
            Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T.,
            Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K.,
            Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H.,
            Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M.,
            Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S.,
            Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A.,
            Hara,H., Tanase,T.O., Nomura,Y., Togiya,S., Komai,F., Hara,R.,
            Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A.,
            Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T.,
            Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S.,
            Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H.,
            Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T.,
            Sugiyama,A., Takemoto,M., Kawakami,B., Yamazaki,M., Watanabe,K.,
            Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M.,
            Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y.,
            Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N.,
            Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T.,
            Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K.,
            Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T.,
            Oyama,M., Hata,H., Watanabe,M., Komatsu,T., Mizushima-Sugano,J.,
            Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K.,
            Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R.,
            Nakai,K., Yada,T., Nakamura,Y., Ohara,O., Isogai,T. and Sugano,S.
  TITLE     Complete sequencing and characterization of 21,243 full-length
            human cDNAs
  JOURNAL   Nat Genet 36 (1), 40-45 (2004)
   PUBMED   14702039
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY075884.1, DA309597.1, AC092574.2 and AI223001.1.
            
            On Dec 8, 2006 this sequence version replaced NP_597731.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.136791.1, DA309597.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152798 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000511833.3/ ENSP00000428878.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..923
                     /product="zinc finger protein 721"
                     /calculated_mol_wt=106358
     Region          111..131
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          139..159
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          151..176
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          <161..241
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          167..187
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          218..608
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          223..243
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          251..271
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          279..299
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(284,286,288,290..291,294..295,298,312,314,318..319,
                     322..323,326,340,342,344,346..347,350..351,354)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          307..327
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          335..355
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          363..383
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          391..411
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          442..885
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          447..467
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          475..495
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          503..523
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(508,510,512,514..515,518..519,522,536,538,542..543,
                     546..547,550,564,566,568,570..571,574..575,578)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          531..551
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          559..579
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          587..607
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          615..634
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          643..663
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          671..691
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          699..719
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          755..775
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(760,762,764,766..767,770..771,774,788,790,794..795,
                     798..799,802,816,818,820,822..823,826..827,830)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          783..803
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          811..831
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          839..859
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          867..887
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          895..915
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..923
                     /gene="ZNF721"
                     /coded_by="NM_133474.4:195..2966"
                     /db_xref="CCDS:CCDS46991.1"
                     /db_xref="GeneID:170960"
                     /db_xref="HGNC:HGNC:29425"
ORIGIN      
        1 mlenyrnlvs lamcshftqd flpvqgieds fhklilrrye kcghdnlqlr kgcksmnvck
       61 vqkgvyngin kclsntqski fqcnarvkvf skfansnkdk trhtgekhfk cnecgksfqk
      121 fsdltqhkgi hagekpytce ergkdfgwyt dlnqhkkiht gekpykceec gkafnrstnl
      181 tahkrihnre kaytgedrdr afgwstnlne ykkihtgdkp ykckecgkaf mhsshlnkhe
      241 kihtgekpyk ckecgkviss sssfakhkri htgekpfkcl ecgkafnist tltkhrriht
      301 gekpytcevc gkafrqsanl yvhrrihtge kpytcgecgk tfrqsanlyv hrrihtgekp
      361 ykcedcgkaf grytalnqhk kihtgekpyk ceecgkafns stnltahkri htrekpytce
      421 drgrafglst nlneykkiht gdkpykckec gkafihslhl nkhekihtgk kpykckqcgk
      481 vitssssfak hkrihtgekp feclecgkaf tssttltkhr rihtgekpyt cevcgkafrq
      541 sailyvhrri htgekpytce ecgktfrqsa nlyvhrriht gekpykceec gkafgrytdl
      601 nqhkkihtge klykceecgk dfvwytdlnq qkkiytgekp ykceecgkaf apstdlnqht
      661 kiltgeqsyk ceecgkafgw sialnqhkki htgekpykce ecgkafsrsr nltthrrvht
      721 rekpykcedr grsfgwstnl neykkihtgd klykckecgk vfkqsshlnr hekihtgkkp
      781 ykckecgkvi tssssfakhk rihtgekpfk clecgkafts sttltkhrri htgekpytce
      841 ecgkafrqsa ilyvhrriht gekpytcgec gktfrqsanl yahkkihtge kpytcgdcgk
      901 tfrqsanlya hkkihtgdkt iqv
//
LOCUS       NP_940684                254 aa            linear   PRI 27-APR-2025
DEFINITION  very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 isoform b
            [Homo sapiens].
ACCESSION   NP_940684
VERSION     NP_940684.1
DBSOURCE    REFSEQ: accession NM_198402.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Zhou,Y., Lv,R., Ye,R.D., Ren,R. and Yu,L.
  TITLE     The 3-hydroxyacyl-CoA dehydratase 1/2 form complex with
            trans-2-enoyl-CoA reductase involved in substrates transfer in very
            long chain fatty acid elongation
  JOURNAL   Biochem Biophys Res Commun 704, 149588 (2024)
   PUBMED   38422897
  REMARK    GeneRIF: The 3-hydroxyacyl-CoA dehydratase 1/2 form complex with
            trans-2-enoyl-CoA reductase involved in substrates transfer in very
            long chain fatty acid elongation.
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Sawai,M., Uchida,Y., Ohno,Y., Miyamoto,M., Nishioka,C., Itohara,S.,
            Sassa,T. and Kihara,A.
  TITLE     The 3-hydroxyacyl-CoA dehydratases HACD1 and HACD2 exhibit
            functional redundancy and are active in a wide range of fatty acid
            elongation pathways
  JOURNAL   J Biol Chem 292 (37), 15538-15551 (2017)
   PUBMED   28784662
  REMARK    GeneRIF: Mutations in HACD1 can result in myopathies in humans;
            knockout mice lacking Hacd1 develop myopathic phenotypes. Data
            (including data from studies using knockout mice and cultured cells
            from knockout mice) suggest that HACD1 and HACD2 exhibit
            overlapping substrate specificities and thus appear to represent
            redundant activities in skeletal muscle.
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Ikeda,M., Kanao,Y., Yamanaka,M., Sakuraba,H., Mizutani,Y.,
            Igarashi,Y. and Kihara,A.
  TITLE     Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases
            involved in very long-chain fatty acid synthesis
  JOURNAL   FEBS Lett 582 (16), 2435-2440 (2008)
   PUBMED   18554506
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Wang,B., Pelletier,J., Massaad,M.J., Herscovics,A. and Shore,G.C.
  TITLE     The yeast split-ubiquitin membrane protein two-hybrid screen
            identifies BAP31 as a regulator of the turnover of endoplasmic
            reticulum-associated protein tyrosine phosphatase-like B
  JOURNAL   Mol Cell Biol 24 (7), 2767-2778 (2004)
   PUBMED   15024066
  REMARK    GeneRIF: Data describe a novel human member of the protein tyrosine
            phosphatase-like B (PTPLB) family, an integral protein of the
            endoplasmic reticulum membrane, as a BAP31-interacting protein.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY191814.1.
            
            Summary: The protein encoded by this gene can catalyze the third
            step (dehydration) in the conversion of long chain fatty acids to
            very long chain fatty acids. The encoded protein localizes to the
            endoplasmic reticulum membrane. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (b) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY191814.1, BC049369.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159080 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000383657.10/ ENSP00000373153.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.1"
     Protein         1..254
                     /product="very-long-chain (3R)-3-hydroxyacyl-CoA
                     dehydratase 2 isoform b"
                     /EC_number="4.2.1.134"
                     /note="protein-tyrosine phosphatase-like member B;
                     very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein]
                     dehydratase 2; very-long-chain (3R)-3-hydroxyacyl-CoA
                     dehydratase 2; protein tyrosine phosphatase-like (proline
                     instead of catalytic arginine), member b"
                     /calculated_mol_wt=28237
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:25732826,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6Y1H2.1)"
     Region          11..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1H2.1)"
     Site            42..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1H2.1)"
     Site            80..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1H2.1)"
     Region          85..245
                     /region_name="PTPLA"
                     /note="Protein tyrosine phosphatase-like protein, PTPLA;
                     pfam04387"
                     /db_xref="CDD:461286"
     Site            108..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1H2.1)"
     Site            131..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1H2.1)"
     Site            170..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1H2.1)"
     Region          198..214
                     /region_name="May be involved in interaction with TECR.
                     /evidence=ECO:0000269|PubMed:38422897"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1H2.1)"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Y1H2.1)"
     Site            218..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1H2.1)"
     CDS             1..254
                     /gene="HACD2"
                     /gene_synonym="PTPLB"
                     /coded_by="NM_198402.5:27..791"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS46895.1"
                     /db_xref="GeneID:201562"
                     /db_xref="HGNC:HGNC:9640"
                     /db_xref="MIM:615939"
ORIGIN      
        1 maavaataaa kgngggggra gagdasgtrk kkgpgplata ylviynvvmt agwlviavgl
       61 vraylakgsy hslyysiekp lkffqtgall eilhcaigiv pssvvltsfq vmsrvfliwa
      121 vthsvkevqs edsvllfvia wtiteiirys fytfsllnhl pylikwaryt lfivlypmgv
      181 sgelltiyaa lpfvrqagly sislpnkynf sfdyyaflil imisyipifp qlyfhmihqr
      241 rkilshteeh kkfe
//
LOCUS       NP_000700                445 aa            linear   PRI 27-APR-2025
DEFINITION  2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial isoform
            1 precursor [Homo sapiens].
ACCESSION   NP_000700
VERSION     NP_000700.1
DBSOURCE    REFSEQ: accession NM_000709.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Yang,J., Xiu,J., Sun,Y., Liu,F., Shang,X. and Li,G.
  TITLE     Three novel mutations of the BCKDHA, BCKDHB and DBT genes in
            Chinese children with maple syrup urine disease
  JOURNAL   J Pediatr Endocrinol Metab 35 (3), 303-312 (2021)
   PUBMED   34883003
  REMARK    GeneRIF: Three novel mutations of the BCKDHA, BCKDHB and DBT genes
            in Chinese children with maple syrup urine disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Vargas-Morales,J.M., Guizar-Heredia,R., Mendez-Garcia,A.L.,
            Palacios-Gonzalez,B., Schcolnik-Cabrera,A., Granados,O.,
            Lopez-Barradas,A.M., Vazquez-Manjarrez,N., Medina-Vera,I.,
            Aguilar-Lopez,M., Tovar-Palacio,C., Ordaz-Nava,G.,
            Rocha-Viggiano,A.K., Medina-Cerda,E., Torres,N., Ordovas,J.M.,
            Tovar,A.R., Guevara-Cruz,M. and Noriega,L.G.
  TITLE     Association of BCAT2 and BCKDH polymorphisms with clinical,
            anthropometric and biochemical parameters in young adults
  JOURNAL   Nutr Metab Cardiovasc Dis 31 (11), 3210-3218 (2021)
   PUBMED   34511290
  REMARK    GeneRIF: Association of BCAT2 and BCKDH polymorphisms with
            clinical, anthropometric and biochemical parameters in young
            adults.
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Fernandez-Lainez,C., Alaez-Verson,C., Ibarra-Gonzalez,I.,
            Enriquez-Flores,S., Carrillo-Sanchez,K., Flores-Lagunes,L.,
            Guillen-Lopez,S., Belmont-Martinez,L. and Vela-Amieva,M.
  TITLE     In silico prediction of the pathogenic effect of a novel variant of
            BCKDHA leading to classical maple syrup urine disease identified
            using clinical exome sequencing
  JOURNAL   Clin Chim Acta 483, 33-38 (2018)
   PUBMED   29673582
  REMARK    GeneRIF: pathogenic effect of a novel variant of BCKDHA leading to
            classical maple syrup urine disease
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Strauss,K.A., Puffenberger,E.G. and Carson,V.J.
  TITLE     Maple Syrup Urine Disease
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301495
REFERENCE   7  (residues 1 to 445)
  AUTHORS   McKean,M.C., Winkeler,K.A. and Danner,D.J.
  TITLE     Nucleotide sequence of the 5' end including the initiation codon of
            cDNA for the E1 alpha subunit of the human branched chain
            alpha-ketoacid dehydrogenase complex
  JOURNAL   Biochim Biophys Acta 1171 (1), 109-112 (1992)
   PUBMED   1420356
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Mitsubuchi,H., Matsuda,I., Nobukuni,Y., Heidenreich,R., Indo,Y.,
            Endo,F., Mallee,J. and Segal,S.
  TITLE     Gene analysis of Mennonite maple syrup urine disease kindred using
            primer-specified restriction map modification
  JOURNAL   J Inherit Metab Dis 15 (2), 181-187 (1992)
   PUBMED   1356170
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Dariush,N., Fisher,C.W., Cox,R.P. and Chuang,D.T.
  TITLE     Structure of the gene encoding the entire mature E1 alpha subunit
            of human branched-chain alpha-keto acid dehydrogenase complex
            (1991) FEBS Letters 284, 34-38
  JOURNAL   FEBS Lett 291 (2), 376-377 (1991)
   PUBMED   1682165
  REMARK    Correction to:[FEBS Lett. 1991 Jun 17;284(1):34-8. doi:
            10.1016/0014-5793(91)80755-r. PMID: 2060625]
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Eisenstein,R.S., Hoganson,G., Miller,R.H. and Harper,A.E.
  TITLE     Altered phosphorylation state of branched-chain 2-oxo acid
            dehydrogenase in a branched-chain acyltransferase deficient human
            fibroblast cell line
  JOURNAL   J Inherit Metab Dis 14 (1), 37-44 (1991)
   PUBMED   1861457
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC023983.1, AK298188.1 and
            BQ018849.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The branched-chain alpha-keto acid (BCAA) dehydrogenase
            (BCKD) complex is an innter mitochondrial enzyme complex that
            catalyzes the second major step in the catabolism of the
            branched-chain amino acids leucine, isoleucine, and valine. The
            BCKD complex consists of three catalytic components: a
            heterotetrameric (alpha2-beta2) branched-chain alpha-keto acid
            decarboxylase (E1), a dihydrolipoyl transacylase (E2), and a
            dihydrolipoamide dehydrogenase (E3). This gene encodes the alpha
            subunit of the decarboxylase (E1) component. Mutations in this gene
            result in maple syrup urine disease, type IA. Multiple transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC023983.1, SRR3476690.198658.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000269980.7/
                                                  ENSP00000269980.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..445
                     /product="2-oxoisovalerate dehydrogenase subunit alpha,
                     mitochondrial isoform 1 precursor"
                     /EC_number="1.2.4.4"
                     /note="2-oxoisovalerate dehydrogenase (lipoamide);
                     2-oxoisovalerate dehydrogenase subunit alpha,
                     mitochondrial; branched-chain alpha-keto acid
                     dehydrogenase E1 component alpha chain; BCKDH E1-alpha;
                     branched chain keto acid dehydrogenase E1 alpha protein;
                     branched chain keto acid dehydrogenase E1, alpha
                     polypeptide"
                     /calculated_mol_wt=45513
     transit_peptide 1..45
                     /calculated_mol_wt=4976
     Region          33..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12694.2)"
     mat_peptide     46..445
                     /product="2-oxoisovalerate dehydrogenase subunit alpha,
                     mitochondrial isoform 1"
                     /calculated_mol_wt=45513
     Region          80..429
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by BCKDK.
                     /evidence=ECO:0000269|PubMed:19411760,
                     ECO:0000269|PubMed:22589535; propagated from
                     UniProtKB/Swiss-Prot (P12694.2)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P50136; propagated from
                     UniProtKB/Swiss-Prot (P12694.2)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50136; propagated from
                     UniProtKB/Swiss-Prot (P12694.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50136; propagated from
                     UniProtKB/Swiss-Prot (P12694.2)"
     Site            356
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P50136; propagated from
                     UniProtKB/Swiss-Prot (P12694.2)"
     CDS             1..445
                     /gene="BCKDHA"
                     /gene_synonym="BCKDE1A; MSU; MSUD1; MSUD1A; OVD1A"
                     /coded_by="NM_000709.4:11..1348"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12581.1"
                     /db_xref="GeneID:593"
                     /db_xref="HGNC:HGNC:986"
                     /db_xref="MIM:608348"
ORIGIN      
        1 mavaiaaarv wrlnrglsqa allllrqpga rglarshppr qqqqfssldd kpqfpgasae
       61 fidklefiqp nvisgipiyr vmdrqgqiin psedphlpke kvlklyksmt llntmdrily
      121 esqrqgrisf ymtnygeegt hvgsaaaldn tdlvfgqyre agvlmyrdyp lelfmaqcyg
      181 nisdlgkgrq mpvhygcker hfvtisspla tqipqavgaa yaakrananr vvicyfgega
      241 asegdahagf nfaatlecpi iffcrnngya istptseqyr gdgiaargpg ygimsirvdg
      301 ndvfavynat kearrravae nqpflieamt yrighhstsd dssayrsvde vnywdkqdhp
      361 isrlrhylls qgwwdeeqek awrkqsrrkv meafeqaerk pkpnpnllfs dvyqempaql
      421 rkqqeslarh lqtygehypl dhfdk
//
LOCUS       NP_000747                196 aa            linear   PRI 27-APR-2025
DEFINITION  corticoliberin preproprotein [Homo sapiens].
ACCESSION   NP_000747
VERSION     NP_000747.1
DBSOURCE    REFSEQ: accession NM_000756.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Zhu,C. and Li,S.
  TITLE     Role of CRH in colitis and colitis-associated cancer: a combinative
            result of central and peripheral effects?
  JOURNAL   Front Endocrinol (Lausanne) 15, 1363748 (2024)
   PUBMED   38616821
  REMARK    GeneRIF: Role of CRH in colitis and colitis-associated cancer: a
            combinative result of central and peripheral effects?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Zhu,C. and Li,S.
  TITLE     The peripheral corticotropin releasing factor family's role in
            vasculitis
  JOURNAL   Vascul Pharmacol 154, 107275 (2024)
   PUBMED   38184094
  REMARK    GeneRIF: The peripheral corticotropin releasing factor family's
            role in vasculitis.
            Review article
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Qing,L., Xiong,P., Lu,Y., Jiang,H. and Nie,S.
  TITLE     Sex-dependent association of DNA methylation in the coding region
            of the corticotropin-releasing hormone gene and schizophrenia
            spectrum disorder
  JOURNAL   Ann Hum Biol 50 (1), 1-8 (2023)
   PUBMED   37401376
  REMARK    GeneRIF: Sex-dependent association of DNA methylation in the coding
            region of the corticotropin-releasing hormone gene and
            schizophrenia spectrum disorder.
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Contoreggi,C.
  TITLE     Corticotropin releasing hormone and imaging, rethinking the stress
            axis
  JOURNAL   Nucl Med Biol 42 (4), 323-339 (2015)
   PUBMED   25573209
  REMARK    Review article
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Kurahashi,H. and Hirose,S.
  TITLE     Autosomal Dominant Sleep-Related Hypermotor (Hyperkinetic) Epilepsy
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301348
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Vamvakopoulos,N.C., Karl,M., Mayol,V., Gomez,T., Stratakis,C.A.,
            Margioris,A. and Chrousos,G.P.
  TITLE     Structural analysis of the regulatory region of the human
            corticotropin releasing hormone gene
  JOURNAL   FEBS Lett 267 (1), 1-5 (1990)
   PUBMED   2365075
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Robinson,B.G., D'Angio,L.A. Jr., Pasieka,K.B. and Majzoub,J.A.
  TITLE     Preprocorticotropin releasing hormone: cDNA sequence and in vitro
            processing
  JOURNAL   Mol Cell Endocrinol 61 (2), 175-180 (1989)
   PUBMED   2783917
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Sasaki,A., Tempst,P., Liotta,A.S., Margioris,A.N., Hood,L.E.,
            Kent,S.B., Sato,S., Shinkawa,O., Yoshinaga,K. and Krieger,D.T.
  TITLE     Isolation and characterization of a corticotropin-releasing
            hormone-like peptide from human placenta
  JOURNAL   J Clin Endocrinol Metab 67 (4), 768-773 (1988)
   PUBMED   3262120
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Arbiser,J.L., Morton,C.C., Bruns,G.A. and Majzoub,J.A.
  TITLE     Human corticotropin releasing hormone gene is located on the long
            arm of chromosome 8
  JOURNAL   Cytogenet Cell Genet 47 (3), 113-116 (1988)
   PUBMED   3259914
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Shibahara,S., Morimoto,Y., Furutani,Y., Notake,M., Takahashi,H.,
            Shimizu,S., Horikawa,S. and Numa,S.
  TITLE     Isolation and sequence analysis of the human
            corticotropin-releasing factor precursor gene
  JOURNAL   EMBO J 2 (5), 775-779 (1983)
   PUBMED   6605851
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK075431.1 and AC090195.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the corticotropin-releasing
            factor family. The encoded preproprotein is proteolytically
            processed to generate the mature neuropeptide hormone. In response
            to stress, this hormone is secreted by the paraventricular nucleus
            (PVN) of the hypothalamus, binds to corticotropin releasing hormone
            receptors and stimulates the release of adrenocorticotropic hormone
            from the pituitary gland. Marked reduction in this protein has been
            observed in association with Alzheimer's disease. Autosomal
            recessive hypothalamic corticotropin deficiency has multiple and
            potentially fatal metabolic consequences including hypoglycemia and
            hepatitis. In addition to production in the hypothalamus, this
            protein is also synthesized in peripheral tissues, such as T
            lymphocytes, and is highly expressed in the placenta. In the
            placenta it is a marker that determines the length of gestation and
            the timing of parturition and delivery. A rapid increase in
            circulating levels of the hormone occurs at the onset of
            parturition, suggesting that, in addition to its metabolic
            functions, this protein may act as a trigger for parturition.
            [provided by RefSeq, Nov 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG573303.1, AK075431.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000276571.5/ ENSP00000276571.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..196
                     /product="corticoliberin preproprotein"
                     /note="corticotropin-releasing factor; corticoliberin"
                     /calculated_mol_wt=18937
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2503
     Region          32..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06850.1)"
     Region          85..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06850.1)"
     Region          136..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06850.1)"
     mat_peptide     154..194
                     /product="Corticoliberin. /id=PRO_0000006213"
                     /note="propagated from UniProtKB/Swiss-Prot (P06850.1)"
                     /calculated_mol_wt=4759
     Region          157..194
                     /region_name="CRF"
                     /note="Corticotropin-releasing factor family; pfam00473"
                     /db_xref="CDD:425703"
     Site            194
                     /site_type="amidation"
                     /note="Isoleucine amide.
                     /evidence=ECO:0000269|PubMed:6605851; propagated from
                     UniProtKB/Swiss-Prot (P06850.1)"
     CDS             1..196
                     /gene="CRH"
                     /gene_synonym="CRF; CRH1"
                     /coded_by="NM_000756.4:187..777"
                     /db_xref="CCDS:CCDS6188.1"
                     /db_xref="GeneID:1392"
                     /db_xref="HGNC:HGNC:2355"
                     /db_xref="MIM:122560"
ORIGIN      
        1 mrlpllvsag vllvallpcp pcrallsrgp vpgarqapqh pqpldffqpp pqseqpqqpq
       61 arpvllrmge eyflrlgnln kspaaplspa ssllaggsgs rpspeqatan ffrvllqqll
      121 lprrsldspa alaergarna lgghqeaper errseeppis ldltfhllre vlemaraeql
      181 aqqahsnrkl meiigk
//
LOCUS       NP_003587                370 aa            linear   PRI 27-APR-2025
DEFINITION  protein-tyrosine sulfotransferase 1 [Homo sapiens].
ACCESSION   NP_003587
VERSION     NP_003587.1
DBSOURCE    REFSEQ: accession NM_003596.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Tanaka,S., Nishiyori,T., Kojo,H., Otsubo,R., Tsuruta,M., Kurogi,K.,
            Liu,M.C., Suiko,M., Sakakibara,Y. and Kakuta,Y.
  TITLE     Structural basis for the broad substrate specificity of the human
            tyrosylprotein sulfotransferase-1
  JOURNAL   Sci Rep 7 (1), 8776 (2017)
   PUBMED   28821720
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Jiang,Z., Zhu,J., Ma,Y., Hong,C., Xiao,S. and Jin,L.
  TITLE     Tyrosylprotein sulfotransferase 1 expression is negatively
            correlated with c-Met and lymph node metastasis in human lung
            cancer
  JOURNAL   Mol Med Rep 12 (4), 5217-5222 (2015)
   PUBMED   26238632
  REMARK    GeneRIF: TPST1 was significantly negatively correlated with the
            expression of cMet in lung cancer and may be a negative prognostic
            biomarker of lung cancer.
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Kim,J.G., Chae,Y.S., Lee,S.J., Kang,B.W., Park,J.Y., Lee,E.J.,
            Jeon,H.S., Park,J.S. and Choi,G.S.
  TITLE     Genetic variation in microRNA-binding site and prognosis of
            patients with colorectal cancer
  JOURNAL   J Cancer Res Clin Oncol 141 (1), 35-41 (2015)
   PUBMED   25079514
  REMARK    GeneRIF: TPST1 rs3757417T>G polymorphisms are associated with
            colorectal cancer.
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Xu,J., Deng,X., Tang,M., Li,L., Xiao,L., Yang,L., Zhong,J.,
            Bode,A.M., Dong,Z., Tao,Y. and Cao,Y.
  TITLE     Tyrosylprotein sulfotransferase-1 and tyrosine sulfation of
            chemokine receptor 4 are induced by Epstein-Barr virus encoded
            latent membrane protein 1 and associated with the metastatic
            potential of human nasopharyngeal carcinoma
  JOURNAL   PLoS One 8 (3), e56114 (2013)
   PUBMED   23472069
  REMARK    GeneRIF: up-regulation of TPST-1 and tyrosine sulfation of CXCR4 by
            LMP1 might be a potential mechanism contributing to nasopharyngeal
            carcinoma metastasis
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Saito,A., Kawamoto,M. and Kamatani,N.
  TITLE     Association study between single-nucleotide polymorphisms in 199
            drug-related genes and commonly measured quantitative traits of 752
            healthy Japanese subjects
  JOURNAL   J Hum Genet 54 (6), 317-323 (2009)
   PUBMED   19343046
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Goettsch,S., Goettsch,W., Morawietz,H. and Bayer,P.
  TITLE     Shear stress mediates tyrosylprotein sulfotransferase isoform shift
            in human endothelial cells
  JOURNAL   Biochem Biophys Res Commun 294 (3), 541-546 (2002)
   PUBMED   12056800
  REMARK    GeneRIF: Shear stress-dependent downregulation of TPST1 in human
            endothelium involves protein kinase C
            Erratum:[Biochem Biophys Res Commun 2002 Jul 26;295(4):1033]
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Popovic,M., Goobie,S., Morrison,J., Ellis,L., Ehtesham,N.,
            Richards,N., Boocock,G., Durie,P.R. and Rommens,J.M.
  TITLE     Fine mapping of the locus for Shwachman-Diamond syndrome at 7q11,
            identification of shared disease haplotypes, and exclusion of TPST1
            as a candidate gene
  JOURNAL   Eur J Hum Genet 10 (4), 250-258 (2002)
   PUBMED   12032733
  REMARK    GeneRIF: results exclude TPST1 as the causative gene for
            Shwachman-Diamond syndrome
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Ouyang,Y.B. and Moore,K.L.
  TITLE     Molecular cloning and expression of human and mouse tyrosylprotein
            sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue
            in Caenorhabditis elegans
  JOURNAL   J Biol Chem 273 (38), 24770-24774 (1998)
   PUBMED   9733778
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Ouyang,Yb., Lane,W.S. and Moore,K.L.
  TITLE     Tyrosylprotein sulfotransferase: purification and molecular cloning
            of an enzyme that catalyzes tyrosine O-sulfation, a common
            posttranslational modification of eukaryotic proteins
  JOURNAL   Proc Natl Acad Sci U S A 95 (6), 2896-2901 (1998)
   PUBMED   9501187
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Marchese,P., Murata,M., Mazzucato,M., Pradella,P., De Marco,L.,
            Ware,J. and Ruggeri,Z.M.
  TITLE     Identification of three tyrosine residues of glycoprotein Ib alpha
            with distinct roles in von Willebrand factor and alpha-thrombin
            binding
  JOURNAL   J Biol Chem 270 (16), 9571-9578 (1995)
   PUBMED   7721887
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC013188.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013188.1, SRR1803616.185557.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304842.6/ ENSP00000302413.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..370
                     /product="protein-tyrosine sulfotransferase 1"
                     /EC_number="2.8.2.20"
                     /note="TPST-1; transport and golgi organization 13 homolog
                     A"
                     /calculated_mol_wt=42057
     Site            9..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60507.1)"
     Site            60
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16859706; propagated from
                     UniProtKB/Swiss-Prot (O60507.1)"
     Region          72..261
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
     Region          102..106
                     /region_name="Interaction with peptide substrate.
                     /evidence=ECO:0000269|PubMed:28821720"
                     /note="propagated from UniProtKB/Swiss-Prot (O60507.1)"
     Site            159
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:O60704; propagated from
                     UniProtKB/Swiss-Prot (O60507.1)"
     Site            262
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16859706; propagated from
                     UniProtKB/Swiss-Prot (O60507.1)"
     Site            286
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:O60704; propagated from
                     UniProtKB/Swiss-Prot (O60507.1)"
     CDS             1..370
                     /gene="TPST1"
                     /gene_synonym="TANGO13A"
                     /coded_by="NM_003596.4:291..1403"
                     /db_xref="CCDS:CCDS5533.1"
                     /db_xref="GeneID:8460"
                     /db_xref="HGNC:HGNC:12020"
                     /db_xref="MIM:603125"
ORIGIN      
        1 mvgklkqnll laclvissvt vfylgqhame chhrieersq pvklestrtt vrtgldlkan
       61 ktfayhkdmp lifiggvprs gttlmramld ahpdircgee trviprilal kqmwsrsske
      121 kirldeagvt devldsamqa flleiivkhg epapylcnkd pfalksltyl srlfpnakfl
      181 lmvrdgrasv hsmisrkvti agfdlnsyrd cltkwnraie tmynqcmevg ykkcmlvhye
      241 qlvlhperwm rtllkflqip wnhsvlhhee migkaggvsl skverstdqv ikpvnvgals
      301 kwvgkippdv lqdmaviapm laklgydpya nppnygkpdp kiientrrvy kgefqlpdfl
      361 kekpqteqve
//
LOCUS       NP_001034454             170 aa            linear   ROD 27-APR-2025
DEFINITION  myelin-associated oligodendrocyte basic protein isoform b [Mus
            musculus].
ACCESSION   NP_001034454
VERSION     NP_001034454.1
DBSOURCE    REFSEQ: accession NM_001039365.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Yu,Z., Yang,Z., Ren,G., Wang,Y., Luo,X., Zhu,F., Yu,S., Jia,L.,
            Chen,M., Worley,P.F. and Xiao,B.
  TITLE     GATOR2 complex-mediated amino acid signaling regulates brain
            myelination
  JOURNAL   Proc Natl Acad Sci U S A 119 (3) (2022)
   PUBMED   35022234
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Kennedy,A.J., Rahn,E.J., Paulukaitis,B.S., Savell,K.E.,
            Kordasiewicz,H.B., Wang,J., Lewis,J.W., Posey,J., Strange,S.K.,
            Guzman-Karlsson,M.C., Phillips,S.E., Decker,K., Motley,S.T.,
            Swayze,E.E., Ecker,D.J., Michael,T.P., Day,J.J. and Sweatt,J.D.
  TITLE     Tcf4 Regulates Synaptic Plasticity, DNA Methylation, and Memory
            Function
  JOURNAL   Cell Rep 16 (10), 2666-2685 (2016)
   PUBMED   27568567
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Maloney,S.E., Khangura,E. and Dougherty,J.D.
  TITLE     The RNA-binding protein Celf6 is highly expressed in diencephalic
            nuclei and neuromodulatory cell populations of the mouse brain
  JOURNAL   Brain Struct Funct 221 (4), 1809-1831 (2016)
   PUBMED   25682262
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Schafer,I., Muller,C., Luhmann,H.J. and White,R.
  TITLE     MOBP levels are regulated by Fyn kinase and affect the
            morphological differentiation of oligodendrocytes
  JOURNAL   J Cell Sci 129 (5), 930-942 (2016)
   PUBMED   26801084
  REMARK    GeneRIF: MOBP synthesis is stimulated by Fyn activity.
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Mardaryev,A.N., Liu,B., Rapisarda,V., Poterlowicz,K.,
            Malashchuk,I., Rudolf,J., Sharov,A.A., Jahoda,C.A., Fessing,M.Y.,
            Benitah,S.A., Xu,G.L. and Botchkarev,V.A.
  TITLE     Cbx4 maintains the epithelial lineage identity and cell
            proliferation in the developing stratified epithelium
  JOURNAL   J Cell Biol 212 (1), 77-89 (2016)
   PUBMED   26711500
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Montague,P., Barrie,J.A., Thomson,C.E., Kirkham,D., McCallion,A.S.,
            Davies,R.W., Kennedy,P.G. and Griffths,I.R.
  TITLE     Cytoskeletal and nuclear localization of myelin oligodendrocytic
            basic protein isoforms
  JOURNAL   Eur J Neurosci 10 (4), 1321-1328 (1998)
   PUBMED   9749786
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Holz,A., Frank,M., Copeland,N.G., Gilbert,D.J., Jenkins,N.A. and
            Schwab,M.E.
  TITLE     Chromosomal localization of the myelin-associated oligodendrocytic
            basic protein and expression in the genetically linked neurological
            mouse mutants ducky and tippy
  JOURNAL   J Neurochem 69 (5), 1801-1809 (1997)
   PUBMED   9349522
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Montague,P., Dickinson,P.J., McCallion,A.S., Stewart,G.J.,
            Savioz,A., Davies,R.W., Kennedy,P.G. and Griffiths,I.R.
  TITLE     Developmental expression of the murine Mobp gene
  JOURNAL   J Neurosci Res 49 (2), 133-143 (1997)
   PUBMED   9272636
REFERENCE   9  (residues 1 to 170)
  AUTHORS   McCallion,A.S., Guenet,J.L., Montague,P., Griffiths,I.R., Savioz,A.
            and Davies,R.W.
  TITLE     The mouse gene (Mobp) encoding myelin-associated oligodendrocytic
            basic protein maps to distal chromosome 9
  JOURNAL   Mamm Genome 7 (11), 847-849 (1996)
   PUBMED   8875894
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Holz,A., Schaeren-Wiemers,N., Schaefer,C., Pott,U., Colello,R.J.
            and Schwab,M.E.
  TITLE     Molecular and developmental characterization of novel cDNAs of the
            myelin-associated/oligodendrocytic basic protein
  JOURNAL   J Neurosci 16 (2), 467-477 (1996)
   PUBMED   8551331
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK140055.1 and AI839250.1.
            
            Transcript Variant: This variant (3) uses an alternate 3' terminal
            exon compared to variant 1. The resulting protein (isoform b) is
            longer and has a distinct C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC048492.1, AK140055.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 71.41 cM"
     Protein         1..170
                     /product="myelin-associated oligodendrocyte basic protein
                     isoform b"
                     /note="myelin-associated oligodendrocyte basic protein"
                     /calculated_mol_wt=19066
     Region          <1..68
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          69..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D2P8.1)"
     Region          <79..>165
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9D2P8.1)"
     Region          93..115
                     /region_name="3 X 9 AA approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D2P8.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63327; propagated from
                     UniProtKB/Swiss-Prot (Q9D2P8.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63327; propagated from
                     UniProtKB/Swiss-Prot (Q9D2P8.1)"
     CDS             1..170
                     /gene="Mobp"
                     /gene_synonym="MOBP155; MOBP170; MOBP69; MOBP73; MOBP81"
                     /coded_by="NM_001039365.3:140..652"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS23626.1"
                     /db_xref="GeneID:17433"
                     /db_xref="MGI:MGI:108511"
ORIGIN      
        1 msqkmakegp rlsknqkfse hfsihccppf tflnskreiv drkysicksg cfyqkkeedw
       61 iccacqktsr ratspqrpkh qpaaspvvvr appakpkspl mpakprsppr pakprspsrt
      121 erqprprpev rpppakqkpp qkskqparss plrgpgtsrg gsptraprfw
//
LOCUS       NP_055989                939 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger RNA-binding protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_055989 XP_001130130 XP_001130674
VERSION     NP_055989.1
DBSOURCE    REFSEQ: accession NM_015174.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 939)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093078.3, DA333602.1, AC004598.1, AB029009.1 and AC005777.1.
            
            On or before Mar 15, 2007 this sequence version replaced
            XP_001130130.1, XP_001130674.1.
            
            Transcript Variant: This variant (1) is a longer transcript and
            encodes the full-length protein (isoform 1).
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1968540, SAMEA1968968
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262961.9/ ENSP00000262961.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..939
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..939
                     /product="zinc finger RNA-binding protein 2 isoform 1"
                     /calculated_mol_wt=101200
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR6.3)"
     Region          <6..211
                     /region_name="PHA02732"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:165099"
     Region          116..185
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR6.3)"
     Region          217..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR6.3)"
     Region          271..300
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          273..295
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(280..282,284..285,289,294,326,329..333,335..336)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          289..314
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR6.3)"
     Region          318..350
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          321..343
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          <356..>457
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          360..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR6.3)"
     Region          401..449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR6.3)"
     Region          467..498
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          470..492
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          <516..549
                     /region_name="ARGLU"
                     /note="Arginine and glutamate-rich 1; pfam15346"
                     /db_xref="CDD:405931"
     Region          545..590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR6.3)"
     Region          652..904
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Region          906..939
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR6.3)"
     CDS             1..939
                     /gene="ZFR2"
                     /gene_synonym="KIAA1086"
                     /coded_by="NM_015174.2:22..2841"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45921.1"
                     /db_xref="GeneID:23217"
                     /db_xref="HGNC:HGNC:29189"
                     /db_xref="MIM:619284"
ORIGIN      
        1 matsqyfdfa qgggpqysaq pptlplptvg asytaqptpg mdpavnpafp paapagyggy
       61 qphsgqdfay gsrpqepvpt attmatyqds ysygqsaaar syedrpyfqs aalqsgrmta
      121 adsgqpgtqe acgqpsphgs hshaqppqqa pivesgqpas tlssgytypt atgvqpessa
      181 sivtsyppps ynptctayta psypnydasv ysaaspfypp aqpppppgpp qqlppppapa
      241 gsgssprads kpplpsklpr pkagprqlql hycdickisc agpqtyrehl ggqkhrkkea
      301 aqktgvqpng sprgvqaqlh cdlcavsctg adayaahirg skhqkvfklh aklgkpiptl
      361 epalatespp gaeakptspt gpsvcassrp alakrpvask alcegppepq aagcrpqwgk
      421 paqpklegpg aptqggskea pagcsdaqpv gpeyveevfs degrvlrfhc klcecsfndl
      481 nakdlhvrgr rhrlqyrkkv npdlpiatep ssrarkvlee rmrkqrhlae erleqlrrwh
      541 aerrrleeep pqdvpphapp dwaqpllmgr pespasaplq pgrrpassdd rhvmckhati
      601 ypteqellav qravshaera lklvsdtlae edrgrreeeg dkrssvapqt rvlkgvmrvg
      661 ilakglllrg drnvrlallc sekpthsllr riaqqlprql qmvtedeyev ssdpeanivi
      721 ssceeprmqv tisvtsplmr edpstdpgve epqadagdvl spkkclesla alrharwfqa
      781 rasglqpcvi virvlrdlcr rvptwgalpa wamellveka vssaagplgp gdavrrvlec
      841 vatgtlltdg pglqdpcerd qtdalepmtl qeredvtasa qhalrmlafr qthkvlgmdl
      901 lpprhrlgar frkrqrgpge geegagekkr grrggeglv
//
LOCUS       NP_006521                227 aa            linear   PRI 27-APR-2025
DEFINITION  YEATS domain-containing protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_006521
VERSION     NP_006521.1
DBSOURCE    REFSEQ: accession NM_006530.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Han,S., Cao,C., Liu,R., Yuan,Y., Pan,L., Xu,M., Hu,C., Zhang,X.,
            Li,M. and Zhang,X.
  TITLE     GAS41 mediates proliferation and GEM chemoresistance via H2A.Z.2
            and Notch1 in pancreatic cancer
  JOURNAL   Cell Oncol (Dordr) 45 (3), 429-446 (2022)
   PUBMED   35503594
  REMARK    GeneRIF: GAS41 mediates proliferation and GEM chemoresistance via
            H2A.Z.2 and Notch1 in pancreatic cancer.
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Cho,H.J., Li,H., Linhares,B.M., Kim,E., Ndoj,J., Miao,H.,
            Grembecka,J. and Cierpicki,T.
  TITLE     GAS41 Recognizes Diacetylated Histone H3 through a Bivalent Binding
            Mode
  JOURNAL   ACS Chem Biol 13 (9), 2739-2746 (2018)
   PUBMED   30071723
  REMARK    GeneRIF: This study determined the crystal structure of the GAS41
            YEATS domain with H3K23acK27ac to visualize the molecular basis of
            diacetylated histone binding. The results suggest a unique binding
            mode in which full-length GAS41 is a reader of diacetylated
            histones.
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Wang,Y., Jin,J., Chung,M.W.H., Feng,L., Sun,H. and Hao,Q.
  TITLE     Identification of the YEATS domain of GAS41 as a pH-dependent
            reader of histone succinylation
  JOURNAL   Proc Natl Acad Sci U S A 115 (10), 2365-2370 (2018)
   PUBMED   29463709
  REMARK    GeneRIF: Cellular and structural studies revealed that GAS41 is a
            histone lysine succinylation reader owing to a protonated histidine
            residue located inside the pocket.
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Debernardi,S., Bassini,A., Jones,L.K., Chaplin,T., Linder,B., de
            Bruijn,D.R., Meese,E. and Young,B.D.
  TITLE     The MLL fusion partner AF10 binds GAS41, a protein that interacts
            with the human SWI/SNF complex
  JOURNAL   Blood 99 (1), 275-281 (2002)
   PUBMED   11756182
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Munnia,A., Schutz,N., Romeike,B.F., Maldener,E., Glass,B., Maas,R.,
            Nastainczyk,W., Feiden,W., Fischer,U. and Meese,E.
  TITLE     Expression, cellular distribution and protein binding of the glioma
            amplified sequence (GAS41), a highly conserved putative
            transcription factor
  JOURNAL   Oncogene 20 (35), 4853-4863 (2001)
   PUBMED   11521196
REFERENCE   8  (residues 1 to 227)
  AUTHORS   Harborth,J., Weber,K. and Osborn,M.
  TITLE     GAS41, a highly conserved protein in eukaryotic nuclei, binds to
            NuMA
  JOURNAL   J Biol Chem 275 (41), 31979-31985 (2000)
   PUBMED   10913114
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Fischer,U., Heckel,D., Michel,A., Janka,M., Hulsebos,T. and
            Meese,E.
  TITLE     Cloning of a novel transcription factor-like gene amplified in
            human glioma including astrocytoma grade I
  JOURNAL   Hum Mol Genet 6 (11), 1817-1822 (1997)
   PUBMED   9302258
REFERENCE   10 (residues 1 to 227)
  AUTHORS   Gracia,E., Fischer,U., elKahloun,A., Trent,J.M., Meese,E. and
            Meltzer,P.S.
  TITLE     Isolation of genes amplified in human cancers by microdissection
            mediated cDNA capture
  JOURNAL   Hum Mol Genet 5 (5), 595-600 (1996)
   PUBMED   8733125
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN915967.1, U61384.1,
            AC117502.4 and CK820576.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is found in the nucleoli.
            It has high sequence homology to human MLLT1, and yeast and human
            MLLT3 proteins. Both MLLT1 and MLLT3 proteins belong to a class of
            transcription factors, indicating that the encoded protein might
            also represent a transcription factor. This protein is thought to
            be required for RNA transcription. This gene has been shown to be
            amplified in tumors. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.203888.1,
                                           SRR3476690.836038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247843.7/ ENSP00000247843.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..227
                     /product="YEATS domain-containing protein 4 isoform 1"
                     /note="NuMA binding protein 1; nuBI1; glioma-amplified
                     sequence 41"
                     /calculated_mol_wt=26368
     Region          19..155
                     /region_name="YEATS_GAS41_like"
                     /note="YEATS domain found in YEATS domain-containing
                     protein 4 and similar proteins; cd16909"
                     /db_xref="CDD:341128"
     Site            73
                     /site_type="other"
                     /note="Interacts with diacetylated histone H3.
                     /evidence=ECO:0000269|PubMed:29900004,
                     ECO:0000269|PubMed:30071723, ECO:0007744|PDB:5VNB,
                     ECO:0007744|PDB:5XTZ; propagated from UniProtKB/Swiss-Prot
                     (O95619.1)"
     Region          93..97
                     /region_name="Diacetylated histone H3 binding.
                     /evidence=ECO:0000269|PubMed:29900004,
                     ECO:0000269|PubMed:30071723, ECO:0007744|PDB:5VNB,
                     ECO:0007744|PDB:5XTZ"
                     /note="propagated from UniProtKB/Swiss-Prot (O95619.1)"
     Region          163..227
                     /region_name="Interaction with MLLT10.
                     /evidence=ECO:0000269|PubMed:11756182"
                     /note="propagated from UniProtKB/Swiss-Prot (O95619.1)"
     Region          168..227
                     /region_name="Interaction with TACC1.
                     /evidence=ECO:0000269|PubMed:11903063"
                     /note="propagated from UniProtKB/Swiss-Prot (O95619.1)"
     CDS             1..227
                     /gene="YEATS4"
                     /gene_synonym="4930573H17Rik; B230215M10Rik; GAS41;
                     NUBI-1; YAF9"
                     /coded_by="NM_006530.4:231..914"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8990.1"
                     /db_xref="GeneID:8089"
                     /db_xref="HGNC:HGNC:24859"
                     /db_xref="MIM:602116"
ORIGIN      
        1 mfkrmaefgp dsggrvkgvt ivkpivygnv aryfgkkree dghthqwtvy vkpyrnedms
       61 ayvkkiqfkl hesygnplrv vtkppyeite tgwgefeiii kiffidpner pvtlyhllkl
      121 fqsdtnamlg kktvvsefyd emifqdptam mqqllttsrq ltlgaykhet efaelevktr
      181 ekleaakkkt sfeiaelker lkasretinc lkneirklee ddqakdi
//
LOCUS       NP_002217               1238 aa            linear   PRI 27-APR-2025
DEFINITION  protein jagged-2 isoform a precursor [Homo sapiens].
ACCESSION   NP_002217
VERSION     NP_002217.3
DBSOURCE    REFSEQ: accession NM_002226.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1238)
  AUTHORS   Dofash,L., Lyengar,K., Pereira,N., Parmar,J., Folland,C., Laing,N.,
            Kang,P.B., Cairns,A., Lynch,M., Davis,M. and Ravenscroft,G.
  TITLE     Three novel missense variants in two families with JAG2-associated
            limb-girdle muscular dystrophy
  JOURNAL   Neuromuscul Disord 42, 36-42 (2024)
   PUBMED   39121631
  REMARK    GeneRIF: Three novel missense variants in two families with
            JAG2-associated limb-girdle muscular dystrophy.
REFERENCE   2  (residues 1 to 1238)
  AUTHORS   Huang,H., Jiang,Y., Liu,J., Luo,D., Yuan,J., Mu,R., Yu,X., Sun,D.,
            Lin,J., Chen,Q., Li,X., Jiang,M., Xu,J., Chu,B., Yin,C., Zhang,L.,
            Ye,Y., Cao,B., Wang,Q. and Zhang,Y.
  TITLE     Jag1/2 maintain esophageal homeostasis and suppress foregut
            tumorigenesis by restricting the basal progenitor cell pool
  JOURNAL   Nat Commun 15 (1), 4124 (2024)
   PUBMED   38750026
  REMARK    GeneRIF: Jag1/2 maintain esophageal homeostasis and suppress
            foregut tumorigenesis by restricting the basal progenitor cell
            pool.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1238)
  AUTHORS   Mandula,J.K., Sierra-Mondragon,R.A., Jimenez,R.V., Chang,D.,
            Mohamed,E., Chang,S., Vazquez-Martinez,J.A., Cao,Y., Anadon,C.M.,
            Lee,S.B., Das,S., Rocha-Munguba,L., Pham,V.M., Li,R., Tarhini,A.A.,
            Furqan,M., Dalton,W., Churchman,M., Moran-Segura,C.M., Nguyen,J.,
            Perez,B., Kojetin,D.J., Obermayer,A., Yu,X., Chen,A., Shaw,T.I.,
            Conejo-Garcia,J.R. and Rodriguez,P.C.
  TITLE     Jagged2 targeting in lung cancer activates anti-tumor immunity via
            Notch-induced functional reprogramming of tumor-associated
            macrophages
  JOURNAL   Immunity 57 (5), 1124-1140 (2024)
   PUBMED   38636522
  REMARK    GeneRIF: Jagged2 targeting in lung cancer activates anti-tumor
            immunity via Notch-induced functional reprogramming of
            tumor-associated macrophages.
REFERENCE   4  (residues 1 to 1238)
  AUTHORS   Islam,S.S., Al-Mohanna,F.H., Yousef,I.M., Al-Badawi,I.A. and
            Aboussekhra,A.
  TITLE     Ovarian tumor cell-derived JAGGED2 promotes omental metastasis
            through stimulating the Notch signaling pathway in the mesothelial
            cells
  JOURNAL   Cell Death Dis 15 (4), 247 (2024)
   PUBMED   38575576
  REMARK    GeneRIF: Ovarian tumor cell-derived JAGGED2 promotes omental
            metastasis through stimulating the Notch signaling pathway in the
            mesothelial cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1238)
  AUTHORS   Deng,Y., Madan,A., Banta,A.B., Friedman,C., Trask,B.J., Hood,L. and
            Li,L.
  TITLE     Characterization, chromosomal localization, and the complete 30-kb
            DNA sequence of the human Jagged2 (JAG2) gene
  JOURNAL   Genomics 63 (1), 133-138 (2000)
   PUBMED   10662552
REFERENCE   6  (residues 1 to 1238)
  AUTHORS   Felli,M.P., Maroder,M., Mitsiadis,T.A., Campese,A.F., Bellavia,D.,
            Vacca,A., Mann,R.S., Frati,L., Lendahl,U., Gulino,A. and
            Screpanti,I.
  TITLE     Expression pattern of notch1, 2 and 3 and Jagged1 and 2 in lymphoid
            and stromal thymus components: distinct ligand-receptor
            interactions in intrathymic T cell development
  JOURNAL   Int Immunol 11 (7), 1017-1025 (1999)
   PUBMED   10383933
REFERENCE   7  (residues 1 to 1238)
  AUTHORS   Gray,G.E., Mann,R.S., Mitsiadis,E., Henrique,D., Carcangiu,M.L.,
            Banks,A., Leiman,J., Ward,D., Ish-Horowitz,D. and
            Artavanis-Tsakonas,S.
  TITLE     Human ligands of the Notch receptor
  JOURNAL   Am J Pathol 154 (3), 785-794 (1999)
   PUBMED   10079256
REFERENCE   8  (residues 1 to 1238)
  AUTHORS   Valsecchi,C., Ghezzi,C., Ballabio,A. and Rugarli,E.I.
  TITLE     JAGGED2: a putative Notch ligand expressed in the apical ectodermal
            ridge and in sites of epithelial-mesenchymal interactions
  JOURNAL   Mech Dev 69 (1-2), 203-207 (1997)
   PUBMED   9486542
REFERENCE   9  (residues 1 to 1238)
  AUTHORS   Luo,B., Aster,J.C., Hasserjian,R.P., Kuo,F. and Sklar,J.
  TITLE     Isolation and functional analysis of a cDNA for human Jagged2, a
            gene encoding a ligand for the Notch1 receptor
  JOURNAL   Mol Cell Biol 17 (10), 6057-6067 (1997)
   PUBMED   9315665
REFERENCE   10 (residues 1 to 1238)
  AUTHORS   Shawber,C., Boulter,J., Lindsell,C.E. and Weinmaster,G.
  TITLE     Jagged2: a serrate-like gene expressed during rat embryogenesis
  JOURNAL   Dev Biol 180 (1), 370-376 (1996)
   PUBMED   8948600
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF029778.1, AL512356.6,
            U69180.1, AF003521.1, AJ712299.1, BX105691.1, AA775404.1 and
            AI276672.1.
            
            On Jul 8, 2002 this sequence version replaced NP_002217.2.
            
            Summary: The Notch signaling pathway is an intercellular signaling
            mechanism that is essential for proper embryonic development.
            Members of the Notch gene family encode transmembrane receptors
            that are critical for various cell fate decisions. The protein
            encoded by this gene is one of several ligands that activate Notch
            and related receptors. Two transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF029778.1, AF020201.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331782.8/ ENSP00000328169.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..1238
                     /product="protein jagged-2 isoform a precursor"
                     /note="protein jagged-2; jagged 2"
                     /calculated_mol_wt=130697
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2688
     mat_peptide     24..1238
                     /product="Protein jagged-2. /id=PRO_0000007629"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y219.3)"
                     /calculated_mol_wt=130697
     Region          28..196
                     /region_name="MNNL"
                     /note="N terminus of Notch ligand C2-like domain;
                     pfam07657"
                     /db_xref="CDD:462222"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y219.3)"
     Region          178..240
                     /region_name="DSL"
                     /note="delta serrate ligand; smart00051"
                     /db_xref="CDD:128366"
     Region          307..345
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(307,310,325)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          351..381
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          385..421
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(385,388,402)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          423..458
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(423,426,440)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          461..496
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(461,464,477)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          500..534
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          536..571
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(536,539,553)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            570
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y219.3)"
     Site            619
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y219.3)"
     Region          636..671
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(636,639,653)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          676..709
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          716..746
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Site            752
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y219.3)"
     Region          757..787
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          789..824
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(789,792,806)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          827..863
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(827,830,844)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          872..943
                     /region_name="VWC_out"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00215"
                     /db_xref="CDD:214565"
     Site            1058
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y219.3)"
     Site            1081..1101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y219.3)"
     Region          1114..1139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y219.3)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y219.3)"
     Region          1156..1238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y219.3)"
     CDS             1..1238
                     /gene="JAG2"
                     /gene_synonym="HJ2; LGMDR27; SER2"
                     /coded_by="NM_002226.5:357..4073"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9998.1"
                     /db_xref="GeneID:3714"
                     /db_xref="HGNC:HGNC:6189"
                     /db_xref="MIM:602570"
ORIGIN      
        1 mraqgrgrlp rrlllllalw vqaarpmgyf elqlsalrnv ngellsgacc dgdgrttrag
       61 gcghdecdty vrvclkeyqa kvtptgpcsy ghgatpvlgg nsfylppaga agdrararar
      121 aggdqdpglv vipfqfawpr sftliveawd wdndttpnee lliervshag minpedrwks
      181 lhfsghvahl elqirvrcde nyysatcnkf crprndffgh ytcdqygnka cmdgwmgkec
      241 keavckqgcn llhggctvpg ecrcsygwqg rfcdecvpyp gcvhgscvep wqcncetnwg
      301 gllcdkdlny cgshhpctng gtcinaepdq yrctcpdgys grncekaeha ctsnpcangg
      361 schevpsgfe chcpsgwsgp tcaldideca snpcaaggtc vdqvdgfeci cpeqwvgatc
      421 qldanecegk pclnafsckn liggyycdci pgwkginchi nvndcrgqcq hggtckdlvn
      481 gyqcvcprgf ggrhcelerd ecasspchsg glcedladgf hchcpqgfsg plcevdvdlc
      541 epspcrngar cynlegdyyc acpddfggkn csvprepcpg gacrvidgcg sdagpgmpgt
      601 aasgvcgphg rcvsqpggnf scicdsgftg tycheniddc lgqpcrnggt cidevdafrc
      661 fcpsgwegel cdtnpndclp dpchsrgrcy dlvndfycac ddgwkgktch srefqcdayt
      721 csnggtcyds gdtfrcacpp gwkgstcava knssclpnpc vnggtcvgsg asfscicrdg
      781 wegrtcthnt ndcnplpcyn ggicvdgvnw frcecapgfa gpdcrinide cqsspcayga
      841 tcvdeingyr cscppgragp rcqevigfgr scwsrgtpfp hgsswvedcn scrcldgrrd
      901 cskvwcgwkp cllagqpeal saqcplgqrc lekapgqclr ppceawgecg aeeppstpcl
      961 prsghldnnc arltlhfnrd hvpqgttvga icsgirslpa travardrll vllcdrassg
     1021 asavevavsf spardlpdss liqgaahaiv aaitqrgnss lllavtevkv etvvtggsst
     1081 gllvpvlcga fsvlwlacvv lcvwwtrkrr kerersrlpr eesannqwap lnpirnpier
     1141 pgghkdvlyq cknftppprr adealpgpag haavredeed edlgrgeeds leaekflshk
     1201 ftkdpgrspg rpahwasgpk vdnravrsin earyagke
//
LOCUS       NP_001271165            1539 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger FYVE domain-containing protein 16 isoform a [Homo
            sapiens].
ACCESSION   NP_001271165 XP_005248688
VERSION     NP_001271165.2
DBSOURCE    REFSEQ: accession NM_001284236.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1539)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 1539)
  AUTHORS   Liu,X., Salokas,K., Tamene,F., Jiu,Y., Weldatsadik,R.G., Ohman,T.
            and Varjosalo,M.
  TITLE     An AP-MS- and BioID-compatible MAC-tag enables comprehensive
            mapping of protein interactions and subcellular localizations
  JOURNAL   Nat Commun 9 (1), 1188 (2018)
   PUBMED   29568061
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1539)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 1539)
  AUTHORS   Shi,W., Chang,C., Nie,S., Xie,S., Wan,M. and Cao,X.
  TITLE     Endofin acts as a Smad anchor for receptor activation in BMP
            signaling
  JOURNAL   J Cell Sci 120 (Pt 7), 1216-1224 (2007)
   PUBMED   17356069
REFERENCE   5  (residues 1 to 1539)
  AUTHORS   Chen,Y.G., Wang,Z., Ma,J., Zhang,L. and Lu,Z.
  TITLE     Endofin, a FYVE domain protein, interacts with Smad4 and
            facilitates transforming growth factor-beta signaling
  JOURNAL   J Biol Chem 282 (13), 9688-9695 (2007)
   PUBMED   17272273
  REMARK    GeneRIF: Facilitates TGF-beta signaling as a scaffold protein to
            promote the R-Smad-Smad4 complex formation by bringing Smad4 to the
            proximity of the receptor complex.
REFERENCE   6  (residues 1 to 1539)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   7  (residues 1 to 1539)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
REFERENCE   8  (residues 1 to 1539)
  AUTHORS   Seet,L.F., Liu,N., Hanson,B.J. and Hong,W.
  TITLE     Endofin recruits TOM1 to endosomes
  JOURNAL   J Biol Chem 279 (6), 4670-4679 (2004)
   PUBMED   14613930
  REMARK    GeneRIF: marked recruitment of TOM1 to endosomes was observed in
            cells overexpressing endofin or its carboxyl-terminal fragment
REFERENCE   9  (residues 1 to 1539)
  AUTHORS   Seet,L.F. and Hong,W.
  TITLE     Endofin, an endosomal FYVE domain protein
  JOURNAL   J Biol Chem 276 (45), 42445-42454 (2001)
   PUBMED   11546807
REFERENCE   10 (residues 1 to 1539)
  AUTHORS   Xu,Y., Hortsman,H., Seet,L., Wong,S.H. and Hong,W.
  TITLE     SNX3 regulates endosomal function through its PX-domain-mediated
            interaction with PtdIns(3)P
  JOURNAL   Nat Cell Biol 3 (7), 658-666 (2001)
   PUBMED   11433298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008771.4.
            
            On Nov 22, 2018 this sequence version replaced NP_001271165.1.
            
            Summary: This gene encodes an endosomal protein that belongs to the
            FYVE zinc finger family of proteins. The encoded protein is thought
            to regulate membrane trafficking in the endosome. This protein
            functions as a scaffold protein in the transforming growth
            factor-beta signaling pathway and is involved in positive and
            negative feedback regulation of the bone morphogenetic protein
            signaling pathway. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 ,3 and 5 encode the same protein
            (isoform a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR933621.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000505560.5/ ENSP00000426848.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..1539
                     /product="zinc finger FYVE domain-containing protein 16
                     isoform a"
                     /note="endosome-associated FYVE-domain protein; protein
                     phosphatase 1, regulatory subunit 69; zinc finger FYVE
                     domain-containing protein 16; zinc finger, FYVE domain
                     containing 16"
                     /calculated_mol_wt=168773
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80U44; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Region          469..491
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Region          640..678
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Region          738..804
                     /region_name="FYVE_endofin"
                     /note="FYVE domain found in endofin and similar proteins;
                     cd15729"
                     /db_xref="CDD:277268"
     Site            order(744,747,765..770,772..773,795..797)
                     /site_type="other"
                     /note="putative phosphatidylinositol 3-phosphate binding
                     site [chemical binding]"
                     /db_xref="CDD:277268"
     Site            815
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Region          816..850
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Site            845
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Region          884..907
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80U44; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Site            939
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Site            946
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3T8.3)"
     Region          1167..1515
                     /region_name="DUF3480"
                     /note="Domain of unknown function (DUF3480); pfam11979"
                     /db_xref="CDD:463419"
     CDS             1..1539
                     /gene="ZFYVE16"
                     /gene_synonym="PPP1R69"
                     /coded_by="NM_001284236.3:184..4803"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS4050.1"
                     /db_xref="GeneID:9765"
                     /db_xref="HGNC:HGNC:20756"
                     /db_xref="MIM:608880"
ORIGIN      
        1 mdsyfkaavs dldkllddfe qnpdeqdylq dvqnaydsnh csvsselass qrtsllpkdq
       61 ecvnscasse tsygtnessl nektlkglts iqneknvtgl dllssvdggt sdeiqplymg
      121 rcskpicdli sdmgnlvhat nseedikkll pddfksnads ligldlssvs dtpcvsstdh
      181 dsdtvreqqn disselqnre iggikelgik vdttlsdsyn ysgtenlkdk kifnqlesiv
      241 dfnmssaltr qsskmfhakd klqhksqpcg llkdvglvke evdvavitaa eclkeegkts
      301 altcslpkne dlclndsnsr denfklpdfs fqedktvikq saqedsksld lkdndviqds
      361 ssalhvsskd vpsslsclpa sgsmcgslie skargdflpq hehkdniqda vtiheeiqns
      421 vvlggepfke ndllkqekck sillqslieg medrkidpdq tviraesldg gdtsstvves
      481 qeglsgthvp essdccegfi ntfssndmdg qdldyfnide gaksgplisd aeldaflteq
      541 ylqttniksf eenvndsksq mnqidmkgld dgninniyfn aeagaigesh giniiceivd
      601 kqntiengls lgekstipvq qglptsksei tnqlsvsdin sqsvggarpk qlfslpsrtr
      661 sskdlnkpdv pdtiesepst adtvvpitca idstadpqvs fnsnyidies nseggssfvt
      721 anedsvpent ckeglvlgqk qptwvpdsea pncmncqvkf tftkrrhhcr acgkvfcgvc
      781 cnrkcklqyl ekearvcvvc yetiskaqaf ermmsptgsn lksnhsdect tvqppqenqt
      841 ssipspatlp vsalkqpgve glcskeqkrv wfadgilpng evadttklss gskrcsedfs
      901 plspdvpmtv ntvdhshstt vekpnnetgd itrneiiqsp isqvpsvekl smntgneglp
      961 tsgsftlddd vfaeteepss ptgvlvnsnl piasisdyrl lcdinkyvcn kisllpnded
     1021 slppllvasg ekgsvpvvee hpsheqiill legesfhpvt fvlnanllvn vkfifyssdk
     1081 ywyfstnglh glgqaeiiil llclpnedti pkdifrlfit iykdalkgky ienldnitft
     1141 esflsskdhg gflfitptfq klddlslpsn pflcgiliqk leipwakvfp mrlmlrlgae
     1201 ykaypaplts irgrkplfge ightimnllv dlrnyqytlh nidqllihme mgkscikipr
     1261 kkysdvmkvl nssnehvisi gasfsteads hlvciqndgi yetqansatg hprkvtgasf
     1321 vvfngalkts sgflakssiv edglmvqitp etmnglrlal reqkdfkitc gkvdavdlre
     1381 yvdicwvdae ekgnkgviss vdgislqgfp sekikleadf etdekivkct evfyflkdqd
     1441 lsilstsyqf akeiamacsa alcphlktlk sngmnkiglr vsidtdmvef qagsegqllp
     1501 qhylndldsa lipvihggts nsslpleiel vffiiehlf
//
LOCUS       NP_001352748            1868 aa            linear   PRI 27-APR-2025
DEFINITION  myotubularin-related protein 5 isoform 2 [Homo sapiens].
ACCESSION   NP_001352748
VERSION     NP_001352748.1
DBSOURCE    REFSEQ: accession NM_001365819.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1868)
  AUTHORS   Khamse,S., Alizadeh,S., Bernhart,S.H., Afshar,H., Delbari,A. and
            Ohadi,M.
  TITLE     A (GCC) repeat in SBF1 reveals a novel biological phenomenon in
            human and links to late onset neurocognitive disorder
  JOURNAL   Sci Rep 12 (1), 15480 (2022)
   PUBMED   36104480
  REMARK    GeneRIF: A (GCC) repeat in SBF1 reveals a novel biological
            phenomenon in human and links to late onset neurocognitive
            disorder.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1868)
  AUTHORS   Gang,Q., Bettencourt,C., Holton,J., Lovejoy,C., Chelban,V.,
            Oconnor,E., Yuan,Y., Reilly,M.M., Hanna,M. and Houlden,H.
  TITLE     A novel frameshift deletion in autosomal recessive SBF1-related
            syndromic neuropathy with necklace fibres
  JOURNAL   J Neurol 267 (9), 2705-2712 (2020)
   PUBMED   32444983
  REMARK    GeneRIF: A novel frameshift deletion in autosomal recessive
            SBF1-related syndromic neuropathy with necklace fibres.
REFERENCE   3  (residues 1 to 1868)
  AUTHORS   Flusser,H., Halperin,D., Kadir,R., Shorer,Z., Shelef,I. and
            Birk,O.S.
  TITLE     Novel SBF1 splice-site null mutation broadens the clinical spectrum
            of Charcot-Marie-Tooth type 4B3 disease
  JOURNAL   Clin Genet 94 (5), 473-479 (2018)
   PUBMED   30039846
  REMARK    GeneRIF: The novel SBF1 null mutation highlights distinct severe
            phenotypic manifestations, broadening the clinical spectrum of
            SBF1-related neuropathies: cerebellar and pyramidal signs evident
            in the first months of life with peripheral polyneuropathy emerging
            only toward the end of the first decade, together with unique MRI
            findings.
REFERENCE   4  (residues 1 to 1868)
  AUTHORS   Manole,A., Horga,A., Gamez,J., Raguer,N., Salvado,M., San
            Millan,B., Navarro,C., Pittmann,A., Reilly,M.M. and Houlden,H.
  TITLE     SBF1 mutations associated with autosomal recessive axonal
            neuropathy with cranial nerve involvement
  JOURNAL   Neurogenetics 18 (1), 63-67 (2017)
   PUBMED   28005197
  REMARK    GeneRIF: Novel sequence variants in SBF1 (c.1168C>G and
            c.2209_2210del) as the potential causative mutations in two
            siblings with severe axonal neuropathy, hearing loss, facial
            weakness and bulbar features.
REFERENCE   5  (residues 1 to 1868)
  AUTHORS   Zhu,M.H., Ji,S.L., Zhang,C.Y., Cui,L., Xiong,L. and Zheng,H.L.
  TITLE     DNA microarray reveals ZNF195 and SBF1 are potential biomarkers for
            gemcitabine sensitivity in head and neck squamous cell carcinoma
            cell lines
  JOURNAL   Int J Clin Exp Pathol 7 (4), 1514-1523 (2014)
   PUBMED   24817947
  REMARK    GeneRIF: ZNF195 and SBF1 are potential biomarkers for gemcitabine
            sensitivity in head and neck squamous cell carcinoma cell lines.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1868)
  AUTHORS   Firestein,R. and Cleary,M.L.
  TITLE     Pseudo-phosphatase Sbf1 contains an N-terminal GEF homology domain
            that modulates its growth regulatory properties
  JOURNAL   J Cell Sci 114 (Pt 16), 2921-2927 (2001)
   PUBMED   11686296
REFERENCE   7  (residues 1 to 1868)
  AUTHORS   Firestein,R., Cui,X., Huie,P. and Cleary,M.L.
  TITLE     Set domain-dependent regulation of transcriptional silencing and
            growth control by SUV39H1, a mammalian ortholog of Drosophila
            Su(var)3-9
  JOURNAL   Mol Cell Biol 20 (13), 4900-4909 (2000)
   PUBMED   10848615
REFERENCE   8  (residues 1 to 1868)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A., Tentler,D., Kretz,C.,
            Dahl,N. and Mandel,J.L.
  TITLE     Characterization of the myotubularin dual specificity phosphatase
            gene family from yeast to human
  JOURNAL   Hum Mol Genet 7 (11), 1703-1712 (1998)
   PUBMED   9736772
  REMARK    GeneRIF: SBF1 (MTMR5) belongs to the myotubularin family of
            phosphoinositides phosphatases-like
REFERENCE   9  (residues 1 to 1868)
  AUTHORS   Cui,X., De Vivo,I., Slany,R., Miyamoto,A., Firestein,R. and
            Cleary,M.L.
  TITLE     Association of SET domain and myotubularin-related proteins
            modulates growth control
  JOURNAL   Nat Genet 18 (4), 331-337 (1998)
   PUBMED   9537414
REFERENCE   10 (residues 1 to 1868)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 4 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301641
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL096767.14.
            
            Summary: This gene encodes a member of the protein-tyrosine
            phosphatase family. However, the encoded protein does not appear to
            be a catalytically active phosphatase because it lacks several
            amino acids in the catalytic pocket. This protein contains a
            Guanine nucleotide exchange factor (GEF) domain which is necessary
            for its role in growth and differentiation. Mutations in this gene
            have been associated with Charcot-Marie-Tooth disease 4B3.
            Pseudogenes of this gene have been defined on chromosomes 1 and 8.
            [provided by RefSeq, Dec 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1868
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..1868
                     /product="myotubularin-related protein 5 isoform 2"
                     /note="myotubularin-related protein 5; DENN/MADD domain
                     containing 7A; inactive phosphatidylinositol 3-phosphatase
                     5"
                     /calculated_mol_wt=208313
     Region          1..86
                     /region_name="uDENN"
                     /note="Domain always found upstream of DENN domain, found
                     in a variety of signalling proteins; smart00800"
                     /db_xref="CDD:214824"
     Region          91..123
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95248.4)"
     Region          130..311
                     /region_name="DENN"
                     /note="Domain found in a variety of signalling proteins,
                     always encircled by uDENN and dDENN; smart00799"
                     /db_xref="CDD:214823"
     Region          365..433
                     /region_name="dDENN"
                     /note="Domain always found downstream of DENN domain,
                     found in a variety of signalling proteins; smart00801"
                     /db_xref="CDD:129037"
     Region          543..765
                     /region_name="SBF2"
                     /note="Myotubularin protein; pfam12335"
                     /db_xref="CDD:463536"
     Region          894..1012
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          1067..1116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95248.4)"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95248.4)"
     Site            1138
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O95248.4)"
     Region          1151..1497
                     /region_name="PTP-MTMR5"
                     /note="protein tyrosine phosphatase-like pseudophosphatase
                     domain of myotubularin related phosphoinositide
                     phosphatase 5; cd14588"
                     /db_xref="CDD:350436"
     Site            1223
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O95248.4)"
     Region          1268..1318
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95248.4)"
     Region          1606..1631
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95248.4)"
     Region          1723..1757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95248.4)"
     Site            1747
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95248.4)"
     Region          1761..1866
                     /region_name="PH_Sbf1_hMTMR5"
                     /note="Set binding factor 1 (also called Human MTMR5)
                     Pleckstrin Homology (PH) domain; cd01235"
                     /db_xref="CDD:269941"
     CDS             1..1868
                     /gene="SBF1"
                     /gene_synonym="CMT4B3; DENND7A; MTMR5"
                     /coded_by="NM_001365819.1:196..5802"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93186.1"
                     /db_xref="GeneID:6305"
                     /db_xref="HGNC:HGNC:10542"
                     /db_xref="MIM:603560"
ORIGIN      
        1 marladyfvl vafgphprgs gegqgqilqr fpekdwednp fpqgielfcq psgwqlcper
       61 npptffvavl tdinserhyc acltfwepae psqqettrve datereeegd eggqthlspt
      121 apapsaqlfa pktlvlvsrl dhtevfrnsl gliyaihveg lnvclenvig nlltctvpla
      181 ggsqrtislg agdrqviqtp ladslpvsrc svallfrqlg itnvlslfca altehkvlfl
      241 srsyqrlada crgllallfp lrysftyvpi lpaqllevls tptpfiigvn aafqaetqel
      301 ldvivadldg gtvtipecvh ipplpeplqs qthsvlsmvl dpeleladla fpppttstss
      361 lkmqdkelra vflrlfaqll qgyrwclhvv rihpepvirf hkaaflgqrg lveddflmkv
      421 legmafagfv sergvpyrpt dlfdelvahe varmradenh pqrvlrhvqe laeqlyknen
      481 pypavamhkv qrpgesshlr rvprpfprld egtvqwivdq aaakmqgapp avkaerrttv
      541 psgppmtail ercsglhvns arrlevvrnc isyvfegkml eakkllpavl ralkgraarr
      601 claqelhlhv qqnravldhq qfdfvvrmmn cclqdctsld ehgiaaallp lvtafcrkls
      661 pgvtqfaysc vqehvvwstp qfweamfygd vqthiralyl eptedlapaq evgeapsqed
      721 ersaldvase qrrlwptlsr ekqqelvqke estvfsqaih yanrmsylll pldssksrll
      781 reraglgdle sasnslvtns magsvaesyd tesgfedaet cdvagavvrf inrfvdkvct
      841 esgvtsdhlk glhvmvpdiv qmhietleav qresrrlppi qkpkllrprl lpgeecvldg
      901 lrvyllpdgr eegaggsagg pallpaegav flttyrvift gmptdplvge qvvvrsfpva
      961 altkekrisv qtpvdqllqd glqlrsctfq llkmafdeev gsdsaelfrk qlhklryppd
     1021 iratfaftlg sahtpgrppr vtkdkgpslr tlsrnlvkna kktigrqhvt rkkynppswe
     1081 hrgqpppedq edeisvseel epstltpssa lkpsdrmtms slveraccrd yqrlglgtls
     1141 sslsraksep frispvnrmy aicrsypgll ivpqsvqdna lqrvsrcyrq nrfpvvcwrs
     1201 grskavllrs gglhgkgvvg lfkaqnapsp gqsqadsssl eqekylqavv ssmpryadas
     1261 grntlsgfss ahmgshgkwg svrtsgrssg lgtdvgsrla grdalappqa nggppdpgfl
     1321 rpqraalyil gdkaqlkgvr sdplqqwelv pievfearqv kasfkkllka cvpgcpaaep
     1381 spasflrsle dsewliqihk llqvsvlvve lldsgssvlv gledgwditt qvvslvqlls
     1441 dpfyrtlegf rllvekewls fghrfshrga htlagqssgf tpvflqfldc vhqvhlqfpm
     1501 efefsqfylk flgyhhvsrr frtflldsdy erielgllye ekgerrgqvp crsvweyvdr
     1561 lskrtpvfhn ymyapedaev lrpysnvsnl kvwdfyteet laegppydwe laqgppeppe
     1621 eersdggapq srrrvvwpcy dscpraqpda isrlleelqr letelgqpae rwkdtwdrvk
     1681 aaqrlegrpd grgtpssllv staphhrrsl gvylqegpvg stlslsldsd qssgsttsgs
     1741 rqaarrstst lysqfqtaes enrsyegtly kkgafmkpwk arwfvldktk hqlryydhrv
     1801 dteckgvidl aeveavapgt ptmgapktvd ekaffdvktt rrvynfcaqd vpsaqqwvdr
     1861 iqsclsda
//
LOCUS       NP_001351330             710 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger CCCH domain-containing protein 14 isoform f [Mus
            musculus].
ACCESSION   NP_001351330 XP_017170723
VERSION     NP_001351330.1
DBSOURCE    REFSEQ: accession NM_001364401.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Li,Q., Yang,G., Ren,B., Liu,X., Tang,L.Q., Shi,Q., Shan,G. and
            Wang,X.
  TITLE     ZC3H14 facilitates backsplicing by binding to exon-intron boundary
            and 3' UTR
  JOURNAL   Mol Cell 84 (22), 4314-4333 (2024)
   PUBMED   39461343
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Corgiat,E.B., List,S.M., Rounds,J.C., Corbett,A.H. and Moberg,K.H.
  TITLE     The RNA-binding protein Nab2 regulates the proteome of the
            developing Drosophila brain
  JOURNAL   J Biol Chem 297 (1), 100877 (2021)
   PUBMED   34139237
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Wheeler,J.M., McMillan,P., Strovas,T.J., Liachko,N.F.,
            Amlie-Wolf,A., Kow,R.L., Klein,R.L., Szot,P., Robinson,L.,
            Guthrie,C., Saxton,A., Kanaan,N.M., Raskind,M., Peskind,E.,
            Trojanowski,J.Q., Lee,V.M.Y., Wang,L.S., Keene,C.D., Bird,T.,
            Schellenberg,G.D. and Kraemer,B.
  TITLE     Activity of the poly(A) binding protein MSUT2 determines
            susceptibility to pathological tau in the mammalian brain
  JOURNAL   Sci Transl Med 11 (523) (2019)
   PUBMED   31852801
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Rha,J., Jones,S.K., Fidler,J., Banerjee,A., Leung,S.W.,
            Morris,K.J., Wong,J.C., Inglis,G.A.S., Shapiro,L., Deng,Q.,
            Cutler,A.A., Hanif,A.M., Pardue,M.T., Schaffer,A., Seyfried,N.T.,
            Moberg,K.H., Bassell,G.J., Escayg,A., Garcia,P.S. and Corbett,A.H.
  TITLE     The RNA-binding protein, ZC3H14, is required for proper poly(A)
            tail length control, expression of synaptic proteins, and brain
            function in mice
  JOURNAL   Hum Mol Genet 26 (19), 3663-3681 (2017)
   PUBMED   28666327
  REMARK    GeneRIF: Among the proteins increased in the hippocampi of
            Zc3h14Deltaex13/Deltaex13 mice compared to control are key synaptic
            proteins including CaMK2a. This newly generated mouse serves as a
            tool to study the function of ZC3H14 in vivo.
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Watanabe,K., Takebayashi,H., Bepari,A.K., Esumi,S., Yanagawa,Y. and
            Tamamaki,N.
  TITLE     Dpy19l1, a multi-transmembrane protein, regulates the radial
            migration of glutamatergic neurons in the developing cerebral
            cortex
  JOURNAL   Development 138 (22), 4979-4990 (2011)
   PUBMED   22028030
  REMARK    Erratum:[Development. 2012 Mar;139(6):1225]
REFERENCE   8  (residues 1 to 710)
  AUTHORS   Pak,C., Garshasbi,M., Kahrizi,K., Gross,C., Apponi,L.H., Noto,J.J.,
            Kelly,S.M., Leung,S.W., Tzschach,A., Behjati,F., Abedini,S.S.,
            Mohseni,M., Jensen,L.R., Hu,H., Huang,B., Stahley,S.N., Liu,G.,
            Williams,K.R., Burdick,S., Feng,Y., Sanyal,S., Bassell,G.J.,
            Ropers,H.H., Najmabadi,H., Corbett,A.H., Moberg,K.H. and Kuss,A.W.
  TITLE     Mutation of the conserved polyadenosine RNA binding protein,
            ZC3H14/dNab2, impairs neural function in Drosophila and humans
  JOURNAL   Proc Natl Acad Sci U S A 108 (30), 12390-12395 (2011)
   PUBMED   21734151
REFERENCE   9  (residues 1 to 710)
  AUTHORS   Leung,S.W., Apponi,L.H., Cornejo,O.E., Kitchen,C.M.,
            Valentini,S.R., Pavlath,G.K., Dunham,C.M. and Corbett,A.H.
  TITLE     Splice variants of the human ZC3H14 gene generate multiple isoforms
            of a zinc finger polyadenosine RNA binding protein
  JOURNAL   Gene 439 (1-2), 71-78 (2009)
   PUBMED   19303045
REFERENCE   10 (residues 1 to 710)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC159193.2.
            
            On Jun 15, 2018 this sequence version replaced XP_017170723.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.646275.1,
                                           SRR7345562.2599451.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849378, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 49.88 cM"
     Protein         1..710
                     /product="zinc finger CCCH domain-containing protein 14
                     isoform f"
                     /note="zinc finger CCCH domain-containing protein 14"
                     /calculated_mol_wt=79377
     Region          576..593
                     /region_name="zf-CCCH_2"
                     /note="RNA-binding, Nab2-type zinc finger; pfam14608"
                     /db_xref="CDD:464217"
     Region          596..614
                     /region_name="zf-CCCH_2"
                     /note="RNA-binding, Nab2-type zinc finger; pfam14608"
                     /db_xref="CDD:464217"
     Region          655..672
                     /region_name="zf-CCCH_2"
                     /note="RNA-binding, Nab2-type zinc finger; pfam14608"
                     /db_xref="CDD:464217"
     CDS             1..710
                     /gene="Zc3h14"
                     /gene_synonym="1010001P15Rik; 1700016A15Rik;
                     2700069A02Rik"
                     /coded_by="NM_001364401.1:156..2288"
                     /note="isoform f is encoded by transcript variant 7"
                     /db_xref="GeneID:75553"
                     /db_xref="MGI:MGI:1919824"
ORIGIN      
        1 meigteisrk irsaikgklq elgayvdeel pdyimvmvan kksqdqmted lslflgnnti
       61 rftvwlhgvl dklrsvttep sslkspdasi fdshvpsnks sfsrgderrh eaavpplavs
      121 ssrpekrdsr vstssqeqks tnvrhsyddg astrlmstvk plrepapsed vidikpepdd
      181 lidedlnfvq enplsqkkpt vtltygssrp sieiyrppas rnadtgthln rlqlhpqqss
      241 ahaakqldvq ssqvseagrl ceppvlssve dtyspffrnn ldkmsieden frkrklpvvs
      301 svvkvkrfsh dgeeeeeded ygtrigslss svsvpakper rpslppskqa nknlilkais
      361 eaqesvtktt nysavpqkqt lpvaprtrts qeellaemvq gqnraprisp pvkeeeakgd
      421 ntgksqdyyd mesmvhadtr sfilkkpkls eeivvtpnqd sgmktadalr vlsghlmqtr
      481 dlvqpdkpas pkfivtldgv psppgymsdq eeemcfegmk pvnqtsasnk glrgllhpqq
      541 lhllsrqled pdgsfsnaem tdlsvaqkpe kllerckywp ackngdecvy hhpispckaf
      601 pnckfaekcl fvhpnckydt kctkadcpft hmsrrasilt pkpvsspaps sngqlcryfp
      661 ackkmecpfy hpkhcrfntq ctrpdctfyh ptitvpprha lkwirpqsse
//
LOCUS       NP_976051                 78 aa            linear   PRI 27-APR-2025
DEFINITION  small integral membrane protein 10-like protein 2A [Homo sapiens].
ACCESSION   NP_976051 XP_001127817 XP_001129116 XP_001721235
VERSION     NP_976051.1
DBSOURCE    REFSEQ: accession NM_203306.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Ji,B., Huang,Y., Gu,T., Zhang,L., Li,G. and Zhang,C.
  TITLE     Potential diagnostic and prognostic value of plasma long noncoding
            RNA LINC00086 and miR-214 expression in gastric cancer
  JOURNAL   Cancer Biomark 24 (2), 249-255 (2019)
   PUBMED   30689553
  REMARK    GeneRIF: Plasma long noncoding RNA LINC00086 expression is
            significantly lower in gastric cancer (GC) patients than in normal
            individuals. GC patients with low LINC00086 expression are likely
            to have larger tumors, lymphatic metastasis, larger TNM stage, and
            higher carcinoembryonic antigen and carbohydrate antigen 19-9
            levels. GC patients with low LINC00086 expression show lower
            survival rates.
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Guo,J., Ma,J., Zhao,G., Li,G., Fu,Y., Luo,Y. and Gui,R.
  TITLE     Long Noncoding RNA LINC0086 Functions as a Tumor Suppressor in
            Nasopharyngeal Carcinoma by Targeting miR-214
  JOURNAL   Oncol Res 25 (7), 1189-1197 (2017)
   PUBMED   28245169
  REMARK    GeneRIF: tumor-suppressive role of LINC0086 in NPC. Low expression
            of LINC0086 is associated with a poor prognosis of NPC patients.
            Upregulation of LINC0086 significantly inhibited NPC cancer cell
            growth and caused apoptosis in vitro and in vivo by targeting
            miR-214.
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Leveille,N., Melo,C.A., Rooijers,K., Diaz-Lagares,A., Melo,S.A.,
            Korkmaz,G., Lopes,R., Moqadam,F.A., Maia,A.R., Wijchers,P.J.,
            Geeven,G., den Boer,M.L., Kalluri,R., de Laat,W., Esteller,M. and
            Agami,R.
  TITLE     Genome-wide profiling of p53-regulated enhancer RNAs uncovers a
            subset of enhancers controlled by a lncRNA
  JOURNAL   Nat Commun 6, 6520 (2015)
   PUBMED   25813522
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL450472.14.
            
            Summary: This gene encodes a highly conserved small protein that
            contains a conserved motif (DUF4560) and may function as an
            integral membrane protein. This transcript was also shown to
            associate with enhancer chromatin and therefore may also function
            as an RNA to regulate enhancers. [provided by RefSeq, Jan 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030620.1, BM547891.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000417443.3/ ENSP00000488643.1
            NMD candidate          :: translation inferred from conservation
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.3"
     Protein         1..78
                     /product="small integral membrane protein 10-like protein
                     2A"
                     /note="long intergenic non-protein coding RNA 86; lncRNA
                     activator of enhancer domains; Small integral membrane
                     protein 10-like protein 2B"
                     /calculated_mol_wt=8258
     Region          21..77
                     /region_name="DUF4560"
                     /note="Domain of unknown function (DUF4560); pfam15118"
                     /db_xref="CDD:434473"
     CDS             1..78
                     /gene="SMIM10L2A"
                     /gene_synonym="LED; LINC00086; LINC00087; LINC0086;
                     NCRNA00086; NCRNA00087; SMIM10L2B"
                     /coded_by="NM_203306.3:189..425"
                     /db_xref="GeneID:399668"
                     /db_xref="HGNC:HGNC:34499"
ORIGIN      
        1 maasaalsaa aaaaalsgla vrlsrsaaar gsygafckgl trtlltffdl awrlrmnfpy
       61 fyivasvmln vrlqvrie
//
LOCUS       NP_001012772             347 aa            linear   PRI 27-APR-2025
DEFINITION  NHL repeat-containing protein 3 isoform a precursor [Homo sapiens].
ACCESSION   NP_001012772 XP_370722
VERSION     NP_001012772.1
DBSOURCE    REFSEQ: accession NM_001012754.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC140877.1, AL445590.4 and
            CR749318.1.
            
            On Mar 14, 2005 this sequence version replaced XP_370722.2.
            
            Summary: This gene encodes a protein containing NCL-1, HT2A and
            Lin-41 (NHL) family repeats. Mammalian NHL-repeat containing
            proteins may be involved in a variety of enzymatic processes,
            including protein modification through ubiquitination.
            Alternatively spliced transcript variants have been observed for
            this gene. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX648122.1, SRR1803613.60954.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379600.8/ ENSP00000368920.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q13.3"
     Protein         1..347
                     /product="NHL repeat-containing protein 3 isoform a
                     precursor"
                     /note="NHL repeat-containing protein 3"
                     /calculated_mol_wt=35451
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5JS37.1)"
                     /calculated_mol_wt=2849
     mat_peptide     26..347
                     /product="NHL repeat-containing protein 3.
                     /id=PRO_0000317194"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JS37.1)"
                     /calculated_mol_wt=35451
     Site            32
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5JS37.1)"
     Region          47..93
                     /region_name="NHL 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JS37.1)"
     Region          66..336
                     /region_name="NHL"
                     /note="NHL repeat unit of beta-propeller proteins;
                     cl18310"
                     /db_xref="CDD:302697"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5JS37.1)"
     Region          107..153
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          150..196
                     /region_name="NHL 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JS37.1)"
     Region          166..205
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          200..243
                     /region_name="NHL 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JS37.1)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5JS37.1)"
     Region          213..250
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          258..295
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5JS37.1)"
     Region          294..338
                     /region_name="NHL 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JS37.1)"
     Region          308..335
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     CDS             1..347
                     /gene="NHLRC3"
                     /coded_by="NM_001012754.4:185..1228"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS31961.1"
                     /db_xref="GeneID:387921"
                     /db_xref="HGNC:HGNC:33751"
ORIGIN      
        1 marfwvcvag agfflaflvl hsrfcgspvl rnftfavswr tekilyrldv gwpkhpeyft
       61 gttfcvavds lnglvyigqr gdnipkilvf tedgyflraw nytvdtphgi faastlyeqs
      121 vwitdvgsgf fghtvkkyss fgdlvqvlgt pgkkgtslnp lqfdnpaely vedtgdiyiv
      181 dgdgglnnrl iklsqdfmil wlhgengtgp akfniphsvt ldsagrvwva drgnkriqvf
      241 dkdtgewlga wnncfteegp ssvrftpdgk ylivaqlnls rlsvvaappv gsigecsvis
      301 tiqladqvlp hllevdrktg avyvaeigak qvqkyvplns yvpsfgs
//
LOCUS       NP_001350306             355 aa            linear   PRI 27-APR-2025
DEFINITION  sugar phosphate exchanger 3 isoform 8 [Homo sapiens].
ACCESSION   NP_001350306 XP_024302742
VERSION     NP_001350306.1
DBSOURCE    REFSEQ: accession NM_001363377.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Yu,Z., Surface,L.E., Park,C.Y., Horlbeck,M.A., Wyant,G.A.,
            Abu-Remaileh,M., Peterson,T.R., Sabatini,D.M., Weissman,J.S. and
            O'Shea,E.K.
  TITLE     Identification of a transporter complex responsible for the
            cytosolic entry of nitrogen-containing bisphosphonates
  JOURNAL   Elife 7, e36620 (2018)
   PUBMED   29745899
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Palmieri,M., Impey,S., Kang,H., di Ronza,A., Pelz,C., Sardiello,M.
            and Ballabio,A.
  TITLE     Characterization of the CLEAR network reveals an integrated control
            of cellular clearance pathways
  JOURNAL   Hum Mol Genet 20 (19), 3852-3866 (2011)
   PUBMED   21752829
  REMARK    GeneRIF: SLC37A3 protein localizes in lysosomes in HeLa cells
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Pan,C.J., Chen,S.Y., Jun,H.S., Lin,S.R., Mansfield,B.C. and
            Chou,J.Y.
  TITLE     SLC37A1 and SLC37A2 are phosphate-linked, glucose-6-phosphate
            antiporters
  JOURNAL   PLoS One 6 (9), e23157 (2011)
   PUBMED   21949678
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Bartoloni,L. and Antonarakis,S.E.
  TITLE     The human sugar-phosphate/phosphate exchanger family SLC37
  JOURNAL   Pflugers Arch 447 (5), 780-783 (2004)
   PUBMED   12811562
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093087.3.
            
            On May 17, 2018 this sequence version replaced XP_024302742.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.135429.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..355
                     /product="sugar phosphate exchanger 3 isoform 8"
                     /note="sugar phosphate exchanger 3; solute carrier family
                     37 (glycerol-3-phosphate transporter), member 3;
                     sugar-phosphate exchange protein 3"
                     /calculated_mol_wt=39271
     Site            16..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Region          20..>286
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            177..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     CDS             1..355
                     /gene="SLC37A3"
                     /gene_synonym="SPX3"
                     /coded_by="NM_001363377.1:186..1253"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:84255"
                     /db_xref="HGNC:HGNC:20651"
                     /db_xref="MIM:619137"
ORIGIN      
        1 mawpnvfqrg sllsqfshhh vvvflltffs ysllhasrkt fsnvkvsise qwtpsafnts
       61 velpveiwss nhlfpsaeka tlflgtldti flfsyavglf isgivgdrln lrwvlsfgmc
      121 ssalvvfvfg altewlrfyn kwlycclwiv ngllqstgwp cvvavmgnwf gkagrgvvfg
      181 lwsacasvgn ilgaclassv lqygyeysla yaclklvnys fffwlpfyls nnfgwkeaea
      241 dklsiwydvg giivfsvsdp gqarmdvgfl lfhshdklyn cvylainseg nilsraketg
      301 shiegvtgar etertmsats gplglrvcpn lglsrsssli ldcqaslnta shlrc
//
LOCUS       NP_689986                142 aa            linear   PRI 27-APR-2025
DEFINITION  dynein light chain Tctex-type protein 2B isoform 2 [Homo sapiens].
ACCESSION   NP_689986 XP_941477
VERSION     NP_689986.2
DBSOURCE    REFSEQ: accession NM_152773.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Hamada,Y., Tsurumi,Y., Nozaki,S., Katoh,Y. and Nakayama,K.
  TITLE     Interaction of WDR60 intermediate chain with TCTEX1D2 light chain
            of the dynein-2 complex is crucial for ciliary protein trafficking
  JOURNAL   Mol Biol Cell 29 (13), 1628-1639 (2018)
   PUBMED   29742051
  REMARK    GeneRIF: WDR60 plays a major role and TCTEX1D2 plays an auxiliary
            role in the dynein-2 complex to mediate retrograde ciliary protein
            trafficking.
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Schmidts,M., Hou,Y., Cortes,C.R., Mans,D.A., Huber,C., Boldt,K.,
            Patel,M., van Reeuwijk,J., Plaza,J.M., van Beersum,S.E., Yap,Z.M.,
            Letteboer,S.J., Taylor,S.P., Herridge,W., Johnson,C.A.,
            Scambler,P.J., Ueffing,M., Kayserili,H., Krakow,D., King,S.M.,
            Beales,P.L., Al-Gazali,L., Wicking,C., Cormier-Daire,V.,
            Roepman,R., Mitchison,H.M. and Witman,G.B.
  CONSRTM   UK10K
  TITLE     TCTEX1D2 mutations underlie Jeune asphyxiating thoracic dystrophy
            with impaired retrograde intraflagellar transport
  JOURNAL   Nat Commun 6, 7074 (2015)
   PUBMED   26044572
  REMARK    GeneRIF: integral component of the evolutionarily conserved
            retrograde intraflagellar transport machinery
            Erratum:[Nat Commun. 2016 Mar 29;7:11270. doi: 10.1038/ncomms11270.
            PMID: 27021811]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Gholkar,A.A., Senese,S., Lo,Y.C., Capri,J., Deardorff,W.J.,
            Dharmarajan,H., Contreras,E., Hodara,E., Whitelegge,J.P.,
            Jackson,P.K. and Torres,J.Z.
  TITLE     Tctex1d2 associates with short-rib polydactyly syndrome proteins
            and is required for ciliogenesis
  JOURNAL   Cell Cycle 14 (7), 1116-1125 (2015)
   PUBMED   25830415
  REMARK    GeneRIF: Tctex1d2 is a novel dynein light chain important for
            trafficking to the cilium and potentially retrograde intraflagellar
            transport.
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Asante,D., Stevenson,N.L. and Stephens,D.J.
  TITLE     Subunit composition of the human cytoplasmic dynein-2 complex
  JOURNAL   J Cell Sci 127 (Pt 21), 4774-4787 (2014)
   PUBMED   25205765
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC021177.2, BM548106.1 and
            BM983853.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 1, 2009 this sequence version replaced NP_689986.1.
            
            Summary: Dyneins are a group of microtubule-activated ATPases that
            function as molecular motors. They are divided into two subgroups
            of axonemal and cytoplasmic dyneins. The cytoplasmic dyneins
            function in intracellular motility, including retrograde axonal
            transport, protein sorting, organelle movement, and spindle
            dynamics. Molecules of conventional cytoplasmic dynein are
            comprised of 2 heavy chain polypeptides and a number of
            intermediate and light chains. This gene encodes a subunit of the
            human cytoplasmic dynein-2 complex. Mutations in this gene are
            associated with short-rib thoracic dysplasia 17 with or without
            polydactyly. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, May 2017].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.542246.1,
                                           SRR1163657.100823.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325318.10/ ENSP00000324323.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..142
                     /product="dynein light chain Tctex-type protein 2B isoform
                     2"
                     /note="tctex1 domain-containing protein 2; Tctex1 domain
                     containing 2; dynein light chain Tctex-type protein 2B"
                     /calculated_mol_wt=15991
     Region          38..141
                     /region_name="DLC-like_TCTEX1D2"
                     /note="dynein light chain (DLC)-like domain found in
                     Tctex1 domain-containing protein 2 (TCTEX1D2) and similar
                     proteins; cd21459"
                     /db_xref="CDD:412007"
     CDS             1..142
                     /gene="DYNLT2B"
                     /gene_synonym="SRTD17; TCTEX1D2"
                     /coded_by="NM_152773.5:89..517"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33929.1"
                     /db_xref="GeneID:255758"
                     /db_xref="HGNC:HGNC:28482"
                     /db_xref="MIM:617353"
ORIGIN      
        1 matsigvsfs vgdgvpeaek nagepentyi lrpvfqqrfr psvvkdciha vlkeelanae
       61 yspeempqlt khlsenikdk lkemgfdryk mvvqvvigeq rgegvfmasr cfwdadtdny
      121 thdvfmndsl fcvvaafgcf yy
//
LOCUS       NP_653233                229 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 182 isoform a precursor [Homo sapiens].
ACCESSION   NP_653233
VERSION     NP_653233.5
DBSOURCE    REFSEQ: accession NM_144632.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Ma,M., Lee,J.H. and Kim,M.
  TITLE     Identification of a TMEM182 rs141764639 polymorphism associated
            with central obesity by regulating tumor necrosis factor-alpha in a
            Korean population
  JOURNAL   J Diabetes Complications 34 (12), 107732 (2020)
   PUBMED   32938560
  REMARK    GeneRIF: Identification of a TMEM182 rs141764639 polymorphism
            associated with central obesity by regulating tumor necrosis
            factor-alpha in a Korean population.
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Hsing,E.W., Shiah,S.G., Peng,H.Y., Chen,Y.W., Chuu,C.P.,
            Hsiao,J.R., Lyu,P.C. and Chang,J.Y.
  TITLE     TNF-alpha-induced miR-450a mediates TMEM182 expression to promote
            oral squamous cell carcinoma motility
  JOURNAL   PLoS One 14 (3), e0213463 (2019)
   PUBMED   30893332
  REMARK    GeneRIF: Tumor necrosis factor alpha (TNF-alpha)-mediated
            expression of TMEM182 was regulated by miR-450a induction in oral
            squamous cell carcinoma. MiR-450a-reduced cellular adhesion was
            abolished by TMEM182 restoration.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Kim,Y.K., Kim,Y., Hwang,M.Y., Shimokawa,K., Won,S., Kato,N.,
            Tabara,Y., Yokota,M., Han,B.G., Lee,J.H. and Kim,B.J.
  TITLE     Identification of a genetic variant at 2q12.1 associated with blood
            pressure in East Asians by genome-wide scan including
            gene-environment interactions
  JOURNAL   BMC Med Genet 15, 65 (2014)
   PUBMED   24903457
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Lauc,G., Huffman,J.E., Pucic,M., Zgaga,L., Adamczyk,B., Muzinic,A.,
            Novokmet,M., Polasek,O., Gornik,O., Kristic,J., Keser,T.,
            Vitart,V., Scheijen,B., Uh,H.W., Molokhia,M., Patrick,A.L.,
            McKeigue,P., Kolcic,I., Lukic,I.K., Swann,O., van Leeuwen,F.N.,
            Ruhaak,L.R., Houwing-Duistermaat,J.J., Slagboom,P.E., Beekman,M.,
            de Craen,A.J., Deelder,A.M., Zeng,Q., Wang,W., Hastie,N.D.,
            Gyllensten,U., Wilson,J.F., Wuhrer,M., Wright,A.F., Rudd,P.M.,
            Hayward,C., Aulchenko,Y., Campbell,H. and Rudan,I.
  TITLE     Loci associated with N-glycosylation of human immunoglobulin G show
            pleiotropy with autoimmune diseases and haematological cancers
  JOURNAL   PLoS Genet 9 (1), e1003225 (2013)
   PUBMED   23382691
REFERENCE   8  (residues 1 to 229)
  AUTHORS   Wu,Y. and Smas,C.M.
  TITLE     Expression and regulation of transcript for the novel transmembrane
            protein Tmem182 in the adipocyte and muscle lineage
  JOURNAL   BMC Res Notes 1, 85 (2008)
   PUBMED   18803820
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 229)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007251.4.
            
            On Nov 23, 2018 this sequence version replaced NP_653233.4.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR936735.1, AK129862.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000412401.3/ ENSP00000394178.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.1"
     Protein         1..229
                     /product="transmembrane protein 182 isoform a precursor"
                     /calculated_mol_wt=23126
     sig_peptide     1..26
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6ZP80.2)"
                     /calculated_mol_wt=2771
     Region          15..220
                     /region_name="Claudin_2"
                     /note="PMP-22/EMP/MP20/Claudin tight junction; pfam13903"
                     /db_xref="CDD:372799"
     mat_peptide     27..229
                     /product="Transmembrane protein 182. /id=PRO_0000290226"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZP80.2)"
                     /calculated_mol_wt=23126
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6ZP80.2)"
     Region          49..59
                     /region_name="Interaction with ITGB1.
                     /evidence=ECO:0000250|UniProtKB:A0A1D5NY17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZP80.2)"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6ZP80.2)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZP80.2)"
     Site            154..174
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZP80.2)"
     Site            201..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZP80.2)"
     CDS             1..229
                     /gene="TMEM182"
                     /coded_by="NM_144632.5:188..877"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2064.1"
                     /db_xref="GeneID:130827"
                     /db_xref="HGNC:HGNC:26391"
ORIGIN      
        1 mrlniaiffg alfgalgvll flvafgsdyw llatevgrcs geknienvtf hhegffwrcw
       61 fngiveends niwkfwytnq ppskncthay lspypfmrge hnstsydsav iyrgfwavlm
      121 llgvvavvia sfliicaapf ashflykagg gsyiaagilf slvvmlyviw vqavadmesy
      181 rnmkmkdcld ftpsvlygws fflapagiff sllagllflv vgwhiqihh
//
LOCUS       NP_002192                181 aa            linear   PRI 27-APR-2025
DEFINITION  interferon-stimulated gene 20 kDa protein isoform a [Homo sapiens].
ACCESSION   NP_002192
VERSION     NP_002192.2
DBSOURCE    REFSEQ: accession NM_002201.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Du,H., Sun,J., Wang,X., Zhao,L., Liu,X., Zhang,C., Wang,F. and
            Wu,J.
  TITLE     FOSL2-mediated transcription of ISG20 induces M2 polarization of
            macrophages and enhances tumorigenic ability of glioblastoma cells
  JOURNAL   J Neurooncol 169 (3), 659-670 (2024)
   PUBMED   39073688
  REMARK    GeneRIF: FOSL2-mediated transcription of ISG20 induces M2
            polarization of macrophages and enhances tumorigenic ability of
            glioblastoma cells.
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Wang,Y., Suo,J., Wang,Z., Ran,K., Tian,Y., Han,W., Liu,Y. and
            Peng,X.
  TITLE     The PTPRZ1-MET/STAT3/ISG20 axis in glioma stem-like cells modulates
            tumor-associated macrophage polarization
  JOURNAL   Cell Signal 120, 111191 (2024)
   PUBMED   38685521
  REMARK    GeneRIF: The PTPRZ1-MET/STAT3/ISG20 axis in glioma stem-like cells
            modulates tumor-associated macrophage polarization.
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Karasawa,T., Sato,R., Imaizumi,T., Fujita,M., Aizawa,T.,
            Tsugawa,K., Mattinzoli,D., Kawaguchi,S., Seya,K., Terui,K., Joh,K.
            and Tanaka,H.
  TITLE     Expression of interferon-stimulated gene 20 (ISG20), an antiviral
            effector protein, in glomerular endothelial cells: possible
            involvement of ISG20 in lupus nephritis
  JOURNAL   Ren Fail 45 (1), 2224890 (2023)
   PUBMED   37340981
  REMARK    GeneRIF: Expression of interferon-stimulated gene 20 (ISG20), an
            antiviral effector protein, in glomerular endothelial cells:
            possible involvement of ISG20 in lupus nephritis.
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Luo,H., Zhu,Y., Guo,B., Ruan,Z., Liu,Z., Fan,Z. and Zhao,S.
  TITLE     Causal relationships between CD25 on immune cells and hip
            osteoarthritis
  JOURNAL   Front Immunol 14, 1247710 (2023)
   PUBMED   37731506
  REMARK    GeneRIF: Causal relationships between CD25 on immune cells and hip
            osteoarthritis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Chen,Z., Yin,M., Jia,H., Chen,Q. and Zhang,H.
  TITLE     ISG20 stimulates anti-tumor immunity via a double-stranded
            RNA-induced interferon response in ovarian cancer
  JOURNAL   Front Immunol 14, 1176103 (2023)
   PUBMED   37342328
  REMARK    GeneRIF: ISG20 stimulates anti-tumor immunity via a double-stranded
            RNA-induced interferon response in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Izmailova,E., Bertley,F.M., Huang,Q., Makori,N., Miller,C.J.,
            Young,R.A. and Aldovini,A.
  TITLE     HIV-1 Tat reprograms immature dendritic cells to express
            chemoattractants for activated T cells and macrophages
  JOURNAL   Nat Med 9 (2), 191-197 (2003)
   PUBMED   12539042
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Nguyen,L.H., Espert,L., Mechti,N. and Wilson,D.M. 3rd.
  TITLE     The human interferon- and estrogen-regulated ISG20/HEM45 gene
            product degrades single-stranded RNA and DNA in vitro
  JOURNAL   Biochemistry 40 (24), 7174-7179 (2001)
   PUBMED   11401564
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Pentecost,B.T.
  TITLE     Expression and estrogen regulation of the HEM45 MRNA in human tumor
            lines and in the rat uterus
  JOURNAL   J Steroid Biochem Mol Biol 64 (1-2), 25-33 (1998)
   PUBMED   9569007
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Gongora,C., David,G., Pintard,L., Tissot,C., Hua,T.D., Dejean,A.
            and Mechti,N.
  TITLE     Molecular cloning of a new interferon-induced PML nuclear
            body-associated protein
  JOURNAL   J Biol Chem 272 (31), 19457-19463 (1997)
   PUBMED   9235947
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Mattei,M.G., Tissot,C., Gongora,C. and Mechti,N.
  TITLE     Assignment of ISG20 encoding a new interferon-induced PML nuclear
            body-associated protein, to chromosome 15q26 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 286-287 (1997)
   PUBMED   9605874
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG759382.1, BC007922.2, BX339191.2, AK307769.1 and AC104259.14.
            
            On Feb 3, 2000 this sequence version replaced NP_002192.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1, 2, and 3 all encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.154782.1,
                                           SRR1660809.129679.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306072.10/ ENSP00000306565.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..181
                     /product="interferon-stimulated gene 20 kDa protein
                     isoform a"
                     /EC_number="3.1.13.1"
                     /note="interferon-stimulated gene 20 kDa protein;
                     estrogen-regulated transcript 45 protein; promyelocytic
                     leukemia nuclear body-associated protein ISG20; interferon
                     stimulated exonuclease gene 20kDa"
                     /calculated_mol_wt=20232
     Region          8..163
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Site            order(11..14,89..90,92..94,154)
                     /site_type="active"
                     /db_xref="CDD:176647"
     Site            order(11,13,94,154)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176647"
     Site            order(12..14,89..90,92..93,154)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176647"
     CDS             1..181
                     /gene="ISG20"
                     /gene_synonym="CD25; HEM45"
                     /coded_by="NM_002201.6:86..631"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10345.1"
                     /db_xref="GeneID:3669"
                     /db_xref="HGNC:HGNC:6130"
                     /db_xref="MIM:604533"
ORIGIN      
        1 magsrevvam dcemvglgph resglarcsl vnvhgavlyd kfirpegeit dyrtrvsgvt
       61 pqhmvgatpf avarleilql lkgklvvghd lkhdfqalke dmsgytiydt stdrllwrea
      121 kldhcrrvsl rvlserllhk siqnsllghs svedaratme lyqisqrira rrglprlavs
      181 d
//
LOCUS       NP_705835                639 aa            linear   PRI 27-APR-2025
DEFINITION  CREB3 regulatory factor isoform 1 [Homo sapiens].
ACCESSION   NP_705835
VERSION     NP_705835.2
DBSOURCE    REFSEQ: accession NM_153607.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Amitrano,F., Krishnan,M., Murphy,R., Okesene-Gafa,K.A.M., Ji,M.,
            Thompson,J.M.D., Taylor,R.S., Merriman,T.R., Rush,E., McCowan,M.,
            McCowan,L.M.E. and McKinlay,C.J.D.
  TITLE     The impact of CREBRF rs373863828 Pacific-variant on infant body
            composition
  JOURNAL   Sci Rep 14 (1), 8825 (2024)
   PUBMED   38627436
  REMARK    GeneRIF: The impact of CREBRF rs373863828 Pacific-variant on infant
            body composition.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Wu,Z.H., Li,F.F., Ruan,L.L., Feng,Q., Zhang,S., Li,Z.H., Otoo,A.,
            Tang,J., Fu,L.J., Liu,T.H. and Ding,Y.B.
  TITLE     miR-181d-5p, which is upregulated in fetal growth restriction
            placentas, inhibits trophoblast fusion via CREBRF
  JOURNAL   J Assist Reprod Genet 40 (11), 2725-2737 (2023)
   PUBMED   37610607
  REMARK    GeneRIF: miR-181d-5p, which is upregulated in fetal growth
            restriction placentas, inhibits trophoblast fusion via CREBRF.
            Erratum:[J Assist Reprod Genet. 2024 Jan;41(1):231. doi:
            10.1007/s10815-023-02970-1. PMID: 37856054]
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Zhang,J.Z., Heinsberg,L.W., Krishnan,M., Hawley,N.L., Major,T.J.,
            Carlson,J.C., Harre Hindmarsh,J., Watson,H., Qasim,M., Stamp,L.K.,
            Dalbeth,N., Murphy,R., Sun,G., Cheng,H., Naseri,T., Reupena,M.S.,
            Kershaw,E.E., Deka,R., McGarvey,S.T., Minster,R.L., Merriman,T.R.
            and Weeks,D.E.
  TITLE     Multivariate analysis of a missense variant in CREBRF reveals
            associations with measures of adiposity in people of Polynesian
            ancestries
  JOURNAL   Genet Epidemiol 47 (1), 105-118 (2023)
   PUBMED   36352773
  REMARK    GeneRIF: Multivariate analysis of a missense variant in CREBRF
            reveals associations with measures of adiposity in people of
            Polynesian ancestries.
REFERENCE   4  (residues 1 to 639)
  AUTHORS   Hawley,N.L., Duckham,R.L., Carlson,J.C., Naseri,T., Reupena,M.S.,
            Lameko,V., Pomer,A., Wetzel,A., Selu,M., Lupematisila,V., Unasa,F.,
            Vesi,L., Fatu,T., Unasa,S., Faasalele-Savusa,K., Rivara,A.C.,
            Russell,E., Delany,J.P., Viali,S., Kershaw,E.E., Minster,R.L.,
            Weeks,D.E. and McGarvey,S.T.
  TITLE     The protective effect of rs373863828 on type 2 diabetes does not
            operate through a body composition pathway in adult Samoans
  JOURNAL   Obesity (Silver Spring) 30 (12), 2468-2476 (2022)
   PUBMED   36284436
  REMARK    GeneRIF: The protective effect of rs373863828 on type 2 diabetes
            does not operate through a body composition pathway in adult
            Samoans.
REFERENCE   5  (residues 1 to 639)
  AUTHORS   Fu,H., Hawley,N.L., Carlson,J.C., Russell,E.M., Pomer,A., Cheng,H.,
            Naseri,T., Reupena,M.S., Deka,R., Choy,C.C., McGarvey,S.T.,
            Minster,R.L. and Weeks,D.E.
  TITLE     The missense variant, rs373863828, in CREBRF plays a role in
            longitudinal changes in body mass index in Samoans
  JOURNAL   Obes Res Clin Pract 16 (3), 220-227 (2022)
   PUBMED   35606300
  REMARK    GeneRIF: The missense variant, rs373863828, in CREBRF plays a role
            in longitudinal changes in body mass index in Samoans.
REFERENCE   6  (residues 1 to 639)
  AUTHORS   Xue,H., Zhang,J., Guo,X., Wang,J., Li,J., Gao,X., Guo,X., Li,T.,
            Xu,S., Zhang,P., Liu,Q. and Li,G.
  TITLE     CREBRF is a potent tumor suppressor of glioblastoma by blocking
            hypoxia-induced autophagy via the CREB3/ATG5 pathway
  JOURNAL   Int J Oncol 49 (2), 519-528 (2016)
   PUBMED   27278737
  REMARK    GeneRIF: Findings provide new insight into the molecular mechanisms
            underlying hypoxia-induced glioblastoma cell autophagy and indicate
            that the hypoxia/CREBRF/CREB3/ATG5 pathway plays a central role in
            malignant glioma progression.
REFERENCE   7  (residues 1 to 639)
  AUTHORS   Martyn,A.C., Choleris,E., Gillis,D.J., Armstrong,J.N., Amor,T.R.,
            McCluggage,A.R., Turner,P.V., Liang,G., Cai,K. and Lu,R.
  TITLE     Luman/CREB3 recruitment factor regulates glucocorticoid receptor
            activity and is essential for prolactin-mediated maternal instinct
  JOURNAL   Mol Cell Biol 32 (24), 5140-5150 (2012)
   PUBMED   23071095
REFERENCE   8  (residues 1 to 639)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 639)
  AUTHORS   Audas,T.E., Li,Y., Liang,G. and Lu,R.
  TITLE     A novel protein, Luman/CREB3 recruitment factor, inhibits Luman
            activation of the unfolded protein response
  JOURNAL   Mol Cell Biol 28 (12), 3952-3966 (2008)
   PUBMED   18391022
REFERENCE   10 (residues 1 to 639)
  AUTHORS   Liang,G., Audas,T.E., Li,Y., Cockram,G.P., Dean,J.D., Martyn,A.C.,
            Kokame,K. and Lu,R.
  TITLE     Luman/CREB3 induces transcription of the endoplasmic reticulum (ER)
            stress response protein Herp through an ER stress response element
  JOURNAL   Mol Cell Biol 26 (21), 7999-8010 (2006)
   PUBMED   16940180
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX647768.1, AY139008.1 and AC008378.6.
            
            On Dec 8, 2009 this sequence version replaced NP_705835.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.32056.1,
                                           SRR1660803.167214.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296953.6/ ENSP00000296953.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.1"
     Protein         1..639
                     /product="CREB3 regulatory factor isoform 1"
                     /note="luman-recruiting factor; adult retina protein;
                     UPF0474 protein C5orf41; luman/CREB3 recruitment factor;
                     luman recruitment factor"
                     /calculated_mol_wt=72018
     Region          302..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUR6.2)"
     Region          523..532
                     /region_name="Basic motif. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUR6.2)"
     Region          525..>563
                     /region_name="bZIP_AUREO-like"
                     /note="Basic leucine zipper (bZIP) domain of blue light
                     (BL) receptor aureochrome (AUREO) and similar bZIP
                     domains; cd14809"
                     /db_xref="CDD:269871"
     Site            order(528,530..532,534..539,541..543)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269871"
     Region          533..540
                     /region_name="Leucine-zipper. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUR6.2)"
     CDS             1..639
                     /gene="CREBRF"
                     /gene_synonym="C5orf41; LRF"
                     /coded_by="NM_153607.3:320..2239"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34293.1"
                     /db_xref="GeneID:153222"
                     /db_xref="HGNC:HGNC:24050"
                     /db_xref="MIM:617109"
ORIGIN      
        1 mpqpsvsgmd ppfgdafrsh tfseqtlmst dllanssdpd fmyeldremn yqqnprdnfl
       61 sledckdien lesftdvldn egaltsnweq wdtycedltk ytkltscdiw gtkevdylgl
      121 ddfsspyqde evisktptla qlnsedsqsv sdslyypdsl fsvkqnplps sfpgkkitsr
      181 aaapvcsskt lqaevplsdc vqkaskptss tqimvktnmy hnekvnfhve ckdyvkkakv
      241 kinpvqqsrp llsqihtdaa kentcycgav akrqekkgme plqghatpal pfketqelll
      301 splpqegpgs laagesssls astsvsdssq kkeehnyslf vsdnlgeqpt kcspeedeed
      361 eedvddedhd egfgsehels eneeeeeeee dyeddkdddi sdtfsepgye ndsvedlkev
      421 tsissrkrgk rryfweyseq ltpsqqerml rpsewnrdtl psnmyqkngl hhgkyavkks
      481 rrtdvedltp npkkllqign elrklnkvis dltpvselpl tarprsrkek nklasracrl
      541 kkkaqyeank vklwglntey dnllfvinsi kqeivnrvqn prdergpnmg qkleilikdt
      601 lglpvagqts efvnqvlekt aegnptgglv glriptskv
//
LOCUS       NP_035288                416 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-dependent protein kinase type II-beta regulatory subunit
            isoform 1 [Mus musculus].
ACCESSION   NP_035288 XP_126885
VERSION     NP_035288.2
DBSOURCE    REFSEQ: accession NM_011158.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Wang,B., Zhao,M., Su,Z., Jin,B., Yang,X., Zhang,C., Guo,B., Li,J.,
            Hong,W., Liu,J., Zhao,Y., Hou,Y., Lai,F., Zhang,W., Qin,L.,
            Zhang,W., Luo,J. and Zheng,R.
  TITLE     RIIbeta-PKA in GABAergic Neurons of Dorsal Median Hypothalamus
            Governs White Adipose Browning
  JOURNAL   Adv Sci (Weinh) 10 (5), e2205173 (2023)
   PUBMED   36529950
  REMARK    GeneRIF: RIIbeta-PKA in GABAergic Neurons of Dorsal Median
            Hypothalamus Governs White Adipose Browning.
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Zhang,J., Zhang,C., Chen,X., Wang,B., Ma,W., Yang,Y., Zheng,R. and
            Huang,Z.
  TITLE     PKA-RIIbeta autophosphorylation modulates PKA activity and seizure
            phenotypes in mice
  JOURNAL   Commun Biol 4 (1), 263 (2021)
   PUBMED   33649504
  REMARK    GeneRIF: PKA-RIIbeta autophosphorylation modulates PKA activity and
            seizure phenotypes in mice.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Yoon,H., Jang,H., Kim,E.Y., Moon,S., Lee,S., Cho,M., Cho,H.J.,
            Ko,J.J., Chang,E.M., Lee,K.A. and Choi,Y.
  TITLE     Knockdown of PRKAR2B Results in the Failure of Oocyte Maturation
  JOURNAL   Cell Physiol Biochem 45 (5), 2009-2020 (2018)
   PUBMED   29518769
  REMARK    GeneRIF: RNAi-mediated Prkar2b suppression resulted in MI-stage
            arrest during oocyte development, and these oocytes exhibited
            abnormal spindle formation and chromosome aggregation.
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Berthon,A., Faucz,F.R., Espiard,S., Drougat,L., Bertherat,J. and
            Stratakis,C.A.
  TITLE     Age-dependent effects of Armc5 haploinsufficiency on adrenocortical
            function
  JOURNAL   Hum Mol Genet 26 (18), 3495-3507 (2017)
   PUBMED   28911199
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Greene,R.M., Lloyd,M.R., Uberti,M., Nugent,P. and Pisano,M.M.
  TITLE     Patterns of cyclic AMP-dependent protein kinase gene expression
            during ontogeny of the murine palate
  JOURNAL   J Cell Physiol 163 (3), 431-440 (1995)
   PUBMED   7775586
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Brandon,E.P., Gerhold,K.A., Qi,M., McKnight,G.S. and Idzerda,R.L.
  TITLE     Derivation of novel embryonic stem cell lines and targeting of
            cyclic AMP-dependent protein kinase genes
  JOURNAL   Recent Prog Horm Res 50, 403-408 (1995)
   PUBMED   7740174
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Luo,Z., Singh,I.S., Fujihira,T. and Erlichman,J.
  TITLE     Characterization of a minimal promoter element required for
            transcription of the mouse type II beta regulatory subunit (RII
            beta) of cAMP-dependent protein kinase
  JOURNAL   J Biol Chem 267 (34), 24738-24747 (1992)
   PUBMED   1332964
REFERENCE   9  (residues 1 to 416)
  AUTHORS   Singh,I.S., Luo,Z.J., Eng,A. and Erlichman,J.
  TITLE     Molecular cloning and characterization of the promoter region of
            the mouse regulatory subunit RII beta of type II cAMP-dependent
            protein kinase
  JOURNAL   Biochem Biophys Res Commun 178 (1), 221-226 (1991)
   PUBMED   2069562
REFERENCE   10 (residues 1 to 416)
  AUTHORS   Cadd,G. and McKnight,G.S.
  TITLE     Distinct patterns of cAMP-dependent protein kinase gene expression
            in mouse brain
  JOURNAL   Neuron 3 (1), 71-79 (1989)
   PUBMED   2619996
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK135621.1, AK138963.1, CJ238090.1 and CT010463.9.
            
            On or before Mar 23, 2004 this sequence version replaced
            XP_126885.1, NP_035288.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK138963.1, AK041013.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 13.74 cM"
     Protein         1..416
                     /product="cAMP-dependent protein kinase type II-beta
                     regulatory subunit isoform 1"
                     /EC_number="2.7.11.1"
                     /note="cAMP-dependent protein kinase type II-beta
                     regulatory subunit"
                     /calculated_mol_wt=46036
     Region          1..151
                     /region_name="Dimerization and phosphorylation"
                     /note="propagated from UniProtKB/Swiss-Prot (P31324.3)"
     Region          3..45
                     /region_name="DD_RIIbeta_PKA"
                     /note="dimerization/docking (D/D) domain of the Type II
                     beta Regulatory subunit of cAMP-dependent protein kinase;
                     cd12104"
                     /db_xref="CDD:438525"
     Site            order(5..7,9,12..13,16..17,20..21,24,27..30,32..33,36..37,
                     39..40)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:438525"
     Site            order(5,9..10,13..14,17..18,21..22)
                     /site_type="other"
                     /note="putative AKAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:438525"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P31324.3)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31323; propagated from
                     UniProtKB/Swiss-Prot (P31324.3)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087,
                     ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P31324.3)"
     Region          152..265
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(220..221,230..232)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(252..254,258..260)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          274..394
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(349..350,359..361)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(381..383,387..389)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     CDS             1..416
                     /gene="Prkar2b"
                     /gene_synonym="Pkarb2; PKARIIbeta; RII(beta)"
                     /coded_by="NM_011158.4:196..1446"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS25869.1"
                     /db_xref="GeneID:19088"
                     /db_xref="MGI:MGI:97760"
ORIGIN      
        1 msieipaglt ellqgftvev lrhqpadlle falqhftrlq qenerkgaar fghegrtwgd
       61 agaaagggip skgvnfaeep mrsdsengee eeaaeagafn apvinrftrr asvcaeaynp
      121 deeeddaesr iihpktddqr nrlqeackdi llfknldpeq msqvldamfe klvkegehvi
      181 dqgddgdnfy vidrgtfdiy vkcdgvgrcv gnydnrgsfg elalmyntpr aatitatspg
      241 alwgldrvtf rriivknnak krkmyesfie slpflkslev serlkvvdvi gtkvyndgeq
      301 iiaqgdlads ffivesgevk itmkrkgkse veengaveia rcfrgqyfge lalvtnkpra
      361 asahaigtvk clamdvqafe rllgpcmeim krniatyeeq lvalfgtnmd ivepta
//
LOCUS       NP_002513                432 aa            linear   PRI 27-APR-2025
DEFINITION  neuronal pentraxin-1 precursor [Homo sapiens].
ACCESSION   NP_002513 XP_946350
VERSION     NP_002513.2
DBSOURCE    REFSEQ: accession NM_002522.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Sun,Y., Xie,L., Ren,X., Ran,L., He,H., Kong,F., Yang,S. and
            Zhang,M.
  TITLE     miR-148a-3p regulates proliferation and apoptosis of idiopathic
            gingival fibroma by targeting NPTX1
  JOURNAL   Oral Dis 30 (4), 2136-2149 (2024)
   PUBMED   37357360
  REMARK    GeneRIF: miR-148a-3p regulates proliferation and apoptosis of
            idiopathic gingival fibroma by targeting NPTX1.
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Warth Perez Arias,C.C., Silbern,I., Caldi Gomes,L., Wartmann,H.,
            Dambeck,V., Fanz,J., Neuenroth,L., Bahr,M., Outeiro,T.F., Bonn,S.,
            Stadelmann-Nessler,C., Rizzoli,S.O., Lenz,C., Urlaub,H. and
            Lingor,P.
  TITLE     Proteomic analysis of the human hippocampus identifies neuronal
            pentraxin 1 (NPTX1) as synapto-axonal target in late-stage
            Parkinson's disease
  JOURNAL   J Neurochem 166 (5), 862-874 (2023)
   PUBMED   37515330
  REMARK    GeneRIF: Proteomic analysis of the human hippocampus identifies
            neuronal pentraxin 1 (NPTX1) as synapto-axonal target in late-stage
            Parkinson's disease.
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Coutelier,M., Jacoupy,M., Janer,A., Renaud,F., Auger,N.,
            Saripella,G.V., Ancien,F., Pucci,F., Rooman,M., Gilis,D.,
            Lariviere,R., Sgarioto,N., Valter,R., Guillot-Noel,L., Le Ber,I.,
            Sayah,S., Charles,P., Numann,A., Pauly,M.G., Helmchen,C.,
            Deininger,N., Haack,T.B., Brais,B., Brice,A., Tregouet,D.A., El
            Hachimi,K.H., Shoubridge,E.A., Durr,A. and Stevanin,G.
  TITLE     NPTX1 mutations trigger endoplasmic reticulum stress and cause
            autosomal dominant cerebellar ataxia
  JOURNAL   Brain 145 (4), 1519-1534 (2022)
   PUBMED   34788392
  REMARK    GeneRIF: NPTX1 mutations trigger endoplasmic reticulum stress and
            cause autosomal dominant cerebellar ataxia.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Vial,R., Poitevin,S., McKay,N., Burtey,S. and Cerini,C.
  TITLE     Tryptophan Metabolites Regulate Neuropentraxin 1 Expression in
            Endothelial Cells
  JOURNAL   Int J Mol Sci 23 (4), 2369 (2022)
   PUBMED   35216489
  REMARK    GeneRIF: Tryptophan Metabolites Regulate Neuropentraxin 1
            Expression in Endothelial Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Ye,R.Y., Kuang,X.Y., Shao,N., Wang,S.M. and Lin,Y.
  TITLE     Downregulation of NPTX1 induces cell cycle progression through
            Wnt/beta-catenin signaling in breast cancer
  JOURNAL   J Biol Regul Homeost Agents 35 (3), 1177-1183 (2021)
   PUBMED   34212686
  REMARK    GeneRIF: Downregulation of NPTX1 induces cell cycle progression
            through Wnt/beta-catenin signaling in breast cancer.
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Guzeloglu-Kayisli,O., Basar,M., Shapiro,J.P., Semerci,N.,
            Huang,J.S., Schatz,F., Lockwood,C.J. and Kayisli,U.A.
  TITLE     Long-acting progestin-only contraceptives enhance human endometrial
            stromal cell expressed neuronal pentraxin-1 and reactive oxygen
            species to promote endothelial cell apoptosis
  JOURNAL   J Clin Endocrinol Metab 99 (10), E1957-E1966 (2014)
   PUBMED   25029423
  REMARK    GeneRIF: Long acting progestin contraceptive-enhanced NPTX1
            secretion and reactive oxygen species generation in endometrial
            stromal cells impair endometrial endothelial cells survival
            resulting in a loss in vascular integrity.
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Abad,M.A., Enguita,M., DeGregorio-Rocasolano,N., Ferrer,I. and
            Trullas,R.
  TITLE     Neuronal pentraxin 1 contributes to the neuronal damage evoked by
            amyloid-beta and is overexpressed in dystrophic neurites in
            Alzheimer's brain
  JOURNAL   J Neurosci 26 (49), 12735-12747 (2006)
   PUBMED   17151277
  REMARK    GeneRIF: Neuronal pentraxin 1 transgene is a key factor for the
            synapse loss, the neurite damage, and the apoptotic neuronal death
            evoked by amyloid-beta protein, which regulates NP1 expression.
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Poulsen,T.T., Pedersen,N., Perin,M.S., Hansen,C.K. and Poulsen,H.S.
  TITLE     Specific sensitivity of small cell lung cancer cell lines to the
            snake venom toxin taipoxin
  JOURNAL   Lung Cancer 50 (3), 329-337 (2005)
   PUBMED   16115696
  REMARK    GeneRIF: The purpose of the present study was to assess the toxic
            effect of taipoxin in SCLC-cell lines and to determine if toxicity
            correlates to NPR and NP1 and NP2 expression levels.
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Kirkpatrick,L.L., Matzuk,M.M., Dodds,D.C. and Perin,M.S.
  TITLE     Biochemical interactions of the neuronal pentraxins. Neuronal
            pentraxin (NP) receptor binds to taipoxin and taipoxin-associated
            calcium-binding protein 49 via NP1 and NP2
  JOURNAL   J Biol Chem 275 (23), 17786-17792 (2000)
   PUBMED   10748068
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Omeis,I.A., Hsu,Y.C. and Perin,M.S.
  TITLE     Mouse and human neuronal pentraxin 1 (NPTX1): conservation, genomic
            structure, and chromosomal localization
  JOURNAL   Genomics 36 (3), 543-545 (1996)
   PUBMED   8884281
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC120024.22, AK127335.1 and
            DA188847.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_946350.1, NP_002513.1.
            
            Summary: NPTX1 is a member of the neuronal pentraxin gene family.
            Neuronal pentraxin 1 is similar to the rat NP1 gene which encodes a
            binding protein for the snake venom toxin taipoxin. Human NPTX1
            mRNA is exclusively localized to the nervous system. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127335.1, U61849.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306773.5/ ENSP00000307549.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..432
                     /product="neuronal pentraxin-1 precursor"
                     /note="NP-I; neuronal pentraxin I"
                     /calculated_mol_wt=45040
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2101
     mat_peptide     23..432
                     /product="neuronal pentraxin-1"
                     /calculated_mol_wt=45040
     Region          90..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15818.2)"
     Region          <120..>216
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
     Site            154
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15818.2)"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15818.2)"
     Region          222..428
                     /region_name="PTX"
                     /note="Pentraxin / C-reactive protein / pentaxin family;
                     smart00159"
                     /db_xref="CDD:128463"
     Site            order(280,358,360,367,370)
                     /site_type="active"
                     /note="calcium mediated ligand binding site [active]"
                     /db_xref="CDD:238086"
     Site            order(320,337,375,423)
                     /site_type="active"
                     /note="intermolecular salt bridges [active]"
                     /db_xref="CDD:238086"
     CDS             1..432
                     /gene="NPTX1"
                     /gene_synonym="NP1; SCA50"
                     /coded_by="NM_002522.4:162..1460"
                     /db_xref="CCDS:CCDS32762.1"
                     /db_xref="GeneID:4884"
                     /db_xref="HGNC:HGNC:7952"
                     /db_xref="MIM:602367"
ORIGIN      
        1 mpagraartc allalcllga gaqdfgptrf ictsvpvdad mcaasvaagg aeelrssvlq
       61 lretvlqqke tilsqketir eltaklgrce sqstldpgag earagggrkq pgsgkntmgd
      121 lsrtpaaetl sqlgqtlqsl ktrlenleqy srlnsssqtn slkdllqski delerqvlsr
      181 vntleegkgg prndteervk ietaltslhq riselekgqk dnrpgdkfql tfplrtnymy
      241 akvkkslpem yaftvcmwlk ssatpgvgtp fsyavpgqan elvliewgnn pmeilindkv
      301 aklpfvindg kwhhicvtwt trdgvweayq dgtqggsgen lapyhpikpq gvlvlgqeqd
      361 tlgggfdatq afvgelahfn iwdrkltpge vynlatcstk alsgnviawa eshieiygga
      421 tkwtfeacrq in
//
LOCUS       NP_055085                487 aa            linear   PRI 27-APR-2025
DEFINITION  B(0,+)-type amino acid transporter 1 [Homo sapiens].
ACCESSION   NP_055085
VERSION     NP_055085.1
DBSOURCE    REFSEQ: accession NM_014270.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Wu,C.W., Badreddine,J., Chang,J., Huang,Y.M., Kim,F.J., Wild,T.,
            Tsai,A.C., Meeks,N., Donalisio Da Silva,R., Molina,W.R. and
            Schumacher,F.R.
  TITLE     Population genetics analysis of SLC3A1 and SLC7A9 revealed the
            etiology of cystine stone may be more than what our current genetic
            knowledge can explain
  JOURNAL   Urolithiasis 51 (1), 101 (2023)
   PUBMED   37561200
  REMARK    GeneRIF: Population genetics analysis of SLC3A1 and SLC7A9 revealed
            the etiology of cystine stone may be more than what our current
            genetic knowledge can explain.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Lee,B., Lee,S.Y., Han,D.H. and Park,H.D.
  TITLE     Interpretation of SLC3A1 and SLC7A9 variants in cystinuria
            patients: The significance of the PM3 criterion and protein
            stability
  JOURNAL   Urolithiasis 51 (1), 94 (2023)
   PUBMED   37439839
  REMARK    GeneRIF: Interpretation of SLC3A1 and SLC7A9 variants in cystinuria
            patients: The significance of the PM3 criterion and protein
            stability.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Baba,H., Kanda,M., Sawaki,K., Nakamura,S., Ueda,S., Shimizu,D.,
            Koike,M., Kodera,Y. and Fujii,T.
  TITLE     SLC7A9 as a Potential Biomarker for Lymph Node Metastasis of
            Esophageal Squamous Cell Carcinoma
  JOURNAL   Ann Surg Oncol 29 (4), 2699-2709 (2022)
   PUBMED   34773193
  REMARK    GeneRIF: SLC7A9 as a Potential Biomarker for Lymph Node Metastasis
            of Esophageal Squamous Cell Carcinoma.
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Tkaczyk,M., Gadomska-Prokop,K., Zaluska-Lesniewska,I., Musial,K.,
            Zawadzki,J., Jobs,K., Porowski,T., Rogowska-Kalisz,A., Jander,A.,
            Kirolos,M., Halinski,A., Krzemien,A., Sobieszczanska-Drozdziel,A.,
            Zachwieja,K., Beck,B.B., Sikora,P. and Zaniew,M.
  TITLE     Clinical profile of a Polish cohort of children and young adults
            with cystinuria
  JOURNAL   Ren Fail 43 (1), 62-70 (2021)
   PUBMED   33349102
  REMARK    GeneRIF: Clinical profile of a Polish cohort of children and young
            adults with cystinuria.
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Wu,D., Grund,T.N., Welsch,S., Mills,D.J., Michel,M., Safarian,S.
            and Michel,H.
  TITLE     Structural basis for amino acid exchange by a human heteromeric
            amino acid transporter
  JOURNAL   Proc Natl Acad Sci U S A 117 (35), 21281-21287 (2020)
   PUBMED   32817565
  REMARK    GeneRIF: Structural basis for amino acid exchange by a human
            heteromeric amino acid transporter.
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Pfeiffer,R., Loffing,J., Rossier,G., Bauch,C., Meier,C.,
            Eggermann,T., Loffing-Cueni,D., Kuhn,L.C. and Verrey,F.
  TITLE     Luminal heterodimeric amino acid transporter defective in
            cystinuria
  JOURNAL   Mol Biol Cell 10 (12), 4135-4147 (1999)
   PUBMED   10588648
REFERENCE   7  (residues 1 to 487)
  AUTHORS   Feliubadalo,L., Font,M., Purroy,J., Rousaud,F., Estivill,X.,
            Nunes,V., Golomb,E., Centola,M., Aksentijevich,I., Kreiss,Y.,
            Goldman,B., Pras,M., Kastner,D.L., Pras,E., Gasparini,P.,
            Bisceglia,L., Beccia,E., Gallucci,M., de Sanctis,L., Ponzone,A.,
            Rizzoni,G.F., Zelante,L., Bassi,M.T., George,A.L. Jr., Manzoni,M.,
            De Grandi,A., Riboni,M., Endsley,J.K., Ballabio,A., Borsani,G.,
            Reig,N., Fernandez,E., Estevez,R., Pineda,M., Torrents,D.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  CONSRTM   International Cystinuria Consortium
  TITLE     Non-type I cystinuria caused by mutations in SLC7A9, encoding a
            subunit (bo,+AT) of rBAT
  JOURNAL   Nat Genet 23 (1), 52-57 (1999)
   PUBMED   10471498
REFERENCE   8  (residues 1 to 487)
  AUTHORS   Wartenfeld,R., Golomb,E., Katz,G., Bale,S.J., Goldman,B., Pras,M.,
            Kastner,D.L. and Pras,E.
  TITLE     Molecular analysis of cystinuria in Libyan Jews: exclusion of the
            SLC3A1 gene and mapping of a new locus on 19q
  JOURNAL   Am J Hum Genet 60 (3), 617-624 (1997)
   PUBMED   9042922
REFERENCE   9  (residues 1 to 487)
  AUTHORS   Bisceglia,L., Calonge,M.J., Totaro,A., Feliubadalo,L.,
            Melchionda,S., Garcia,J., Testar,X., Gallucci,M., Ponzone,A.,
            Zelante,L., Zorzano,A., Estivill,X., Gasparini,P., Nunes,V. and
            Palacin,M.
  TITLE     Localization, by linkage analysis, of the cystinuria type III gene
            to chromosome 19q13.1
  JOURNAL   Am J Hum Genet 60 (3), 611-616 (1997)
   PUBMED   9042921
REFERENCE   10 (residues 1 to 487)
  AUTHORS   Chillaron,J., Estevez,R., Mora,C., Wagner,C.A., Suessbrich,H.,
            Lang,F., Gelpi,J.L., Testar,X., Busch,A.E., Zorzano,A. and
            Palacin,M.
  TITLE     Obligatory amino acid exchange via systems bo,+-like and y+L-like.
            A tertiary active transport mechanism for renal reabsorption of
            cystine and dibasic amino acids
  JOURNAL   J Biol Chem 271 (30), 17761-17770 (1996)
   PUBMED   8663357
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP276659.1, AK026446.1 and
            BC017962.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that belongs to a family of
            light subunits of amino acid transporters. This protein plays a
            role in the high-affinity and sodium-independent transport of
            cystine and neutral and dibasic amino acids, and appears to
            function in the reabsorption of cystine in the kidney tubule.
            Mutations in this gene cause non-type I cystinuria, a disease that
            leads to cystine stones in the urinary system due to impaired
            transport of cystine and dibasic amino acids. Alternate transcript
            variants, which encode the same protein, have been found for this
            gene. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026446.1, BC017962.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000023064.9/ ENSP00000023064.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..487
                     /product="B(0,+)-type amino acid transporter 1"
                     /note="solute carrier family 7 (cationic amino acid
                     transporter, y+ system), member 9; glycoprotein-associated
                     amino acid transporter b0,+AT1; b(0,+)AT; cystinuria type
                     3; solute carrier family 7 (glycoprotein-associated amino
                     acid transporter light chain, bo,+ system), member 9;
                     solute carrier family 7 (amino acid transporter light
                     chain, bo,+ system), member 9"
                     /calculated_mol_wt=53351
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P82252; propagated from
                     UniProtKB/Swiss-Prot (P82251.1)"
     Region          26..484
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     Site            32..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            111..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            148..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            170..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            252..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            303..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            352..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            435..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     CDS             1..487
                     /gene="SLC7A9"
                     /gene_synonym="BAT1; CSNU3"
                     /coded_by="NM_014270.5:194..1657"
                     /db_xref="CCDS:CCDS12425.1"
                     /db_xref="GeneID:11136"
                     /db_xref="HGNC:HGNC:11067"
                     /db_xref="MIM:604144"
ORIGIN      
        1 mgdtglrkrr edeksiqsqe pkttslqkel glisgisiiv gtiigsgifv spksvlsnte
       61 avgpcliiwa acgvlatlga lcfaelgtmi tksggeypyl meaygpipay lfswaslivi
      121 kptsfaiicl sfseyvcapf yvgckppqiv vkclaaaail fistvnslsv rlgsyvqnif
      181 taaklvivai iiisglvlla qgntknfdns fegaqlsvga islafynglw aydgwnqlny
      241 iteelrnpyr nlplaiiigi plvtacyilm nvsyftvmta tellqsqava vtfgdrvlyp
      301 aswivplfva fstigaangt cftagrliyv agreghmlkv lsyisvrrlt papaiifygi
      361 iatiyiipgd inslvnyfsf aawlfyglti lglivmrftr kelerpikvp vvipvlmtli
      421 svflvlapii skptweylyc vlfilsgllf yflfvhykfg waqkiskpit mhlqmlmevv
      481 ppeedpe
//
LOCUS       NP_077017                 83 aa            linear   PRI 27-APR-2025
DEFINITION  bublin coiled-coil protein [Homo sapiens].
ACCESSION   NP_077017
VERSION     NP_077017.1
DBSOURCE    REFSEQ: accession NM_024112.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Chen,X., Zhang,H. and Xiao,B.
  TITLE     C9orf16 represents the aberrant genetic programs and drives the
            progression of PDAC
  JOURNAL   BMC Cancer 22 (1), 1102 (2022)
   PUBMED   36307773
  REMARK    GeneRIF: C9orf16 represents the aberrant genetic programs and
            drives the progression of PDAC.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Morimoto,E., Tsuboyama,K. and Tomari,Y.
  TITLE     Fusion with heat-resistant obscure (Hero) proteins have the
            potential to improve the molecular property of recombinant proteins
  JOURNAL   PLoS One 17 (6), e0270097 (2022)
   PUBMED   35714106
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Remmelzwaal,S., Geisler,F., Stucchi,R., van der Horst,S.,
            Pasolli,M., Kroll,J.R., Jarosinska,O.D., Akhmanova,A.,
            Richardson,C.A., Altelaar,M., Leube,R.E., Ramalho,J.J. and Boxem,M.
  TITLE     BBLN-1 is essential for intermediate filament organization and
            apical membrane morphology
  JOURNAL   Curr Biol 31 (11), 2334-2346 (2021)
   PUBMED   33857431
REFERENCE   5  (residues 1 to 83)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 83)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   7  (residues 1 to 83)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   8  (residues 1 to 83)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 83)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 83)
  AUTHORS   Gilley,J. and Fried,M.
  TITLE     Extensive gene order differences within regions of conserved
            synteny between the Fugu and human genomes: implications for
            chromosomal evolution and the cloning of disease genes
  JOURNAL   Hum Mol Genet 8 (7), 1313-1320 (1999)
   PUBMED   10369878
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB493059.1 and BC001857.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM550794.1, SRR1163655.129104.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372994.2/ ENSP00000362085.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..83
                     /product="bublin coiled-coil protein"
                     /note="UPF0184 protein C9orf16"
                     /calculated_mol_wt=8923
     Region          1..83
                     /region_name="UPF0184"
                     /note="Uncharacterized protein family (UPF0184);
                     pfam03670"
                     /db_xref="CDD:112485"
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUW7.1)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9BUW7.1)"
     CDS             1..83
                     /gene="BBLN"
                     /gene_synonym="C9orf16; EST00098; Hero9"
                     /coded_by="NM_024112.4:144..395"
                     /db_xref="CCDS:CCDS6893.1"
                     /db_xref="GeneID:79095"
                     /db_xref="HGNC:HGNC:17823"
ORIGIN      
        1 msgpngdlgm pveagaegee dgfgeaeyaa insmldqins cldhleeknd hlharlqell
       61 esnrqtrlef qqqlgeapsd asp
//
LOCUS       NP_001350082             922 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 31 isoform 9 [Homo sapiens].
ACCESSION   NP_001350082 XP_016869476
VERSION     NP_001350082.1
DBSOURCE    REFSEQ: accession NM_001363153.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 922)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 922)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 922)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100873.2.
            
            On May 9, 2018 this sequence version replaced XP_016869476.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..922
                     /product="TBC1 domain family member 31 isoform 9"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=106653
     Region          44..340
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          46..81
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          86..123
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          130..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          215..253
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          261..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          309..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          462..605
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <624..>913
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     CDS             1..922
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001363153.1:64..2832"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
ORIGIN      
        1 mqstdlgnke sgkiwhrkps patrdgiivn iihntsdyhp kvlrflnvaf dgtgdcliag
       61 dhqgniyvfd lhgnrfnlvq rtaqactala fnlrrksefl valadysikc fdtvtkelvs
      121 wmrghessvf sisvhasgky aittssdtaq lwdldtfqrk rklnirqsvg iqkvfflpls
      181 ntilscfkdn sifawecdtl fckyqlpapp esssilykvf avtrdgrila aggksnhlhl
      241 wclearqlfr iiqmptkvra irhleflpds fdagsnqvlg vlsqdgimrf inmqtckllf
      301 eigsldegis ssaisphgry iasimengsl niysvqaltq einkpppplv kviedlpknk
      361 lsssdlkmkv tsgrvqqpak sreskmqtri lkqdltgdfe skknelpdgl nkkrlqillk
      421 gygeyptkyr mfiwrsllql penhtafstl idkgthvafl nlqkkypiks rkllrvlqrt
      481 lsalahwsvi fsdtpylpll afpfvklfqn nqlicfevia tliinwcqhw feyfpnppin
      541 ilsmienvla fhdkellqhf idhditsqly awplletvfs evltreewlk lfdnifsnhp
      601 sfllmtvvay nicsrtplls cnlkddfetv edmqakvdqq rvedeawyqk qellrkaeet
      661 rremllqeee kmiqqrqrla avkrelkvke mhlqdaarrr flklqqdqqe melrrlddei
      721 grkvymrdre iaatardlem rqlelesqkr lyeknltenq ealakemrad adayrrkvdl
      781 eehmfhklie agetqsqktq kwkeaegkef rlrsakkasa lsdasrkwfl kqeinaaveh
      841 aenpchkeep rfqneqdssc lprtsqlnds semdpstqis lnrravewdt tgqnlikkvr
      901 nlrqrltara rhrcqtphll aa
//
LOCUS       NP_066285                414 aa            linear   PRI 27-APR-2025
DEFINITION  COUP transcription factor 2 isoform a [Homo sapiens].
ACCESSION   NP_066285
VERSION     NP_066285.1
DBSOURCE    REFSEQ: accession NM_021005.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Ganapathi,M., Matsuoka,L.S., March,M., Li,D., Brokamp,E.,
            Benito-Sanz,S., White,S.M., Lachlan,K., Ahimaz,P., Sewda,A.,
            Bastarache,L., Thomas-Wilson,A., Stoler,J.M., Bramswig,N.C.,
            Baptista,J., Stals,K., Demurger,F., Cogne,B., Isidor,B.,
            Bedeschi,M.F., Peron,A., Amiel,J., Zackai,E., Schacht,J.P.,
            Iglesias,A.D., Morton,J., Schmetz,A., Seidel,V., Lucia,S.,
            Baskin,S.M., Thiffault,I., Cogan,J.D., Gordon,C.T., Chung,W.K.,
            Bowdin,S. and Bhoj,E.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     Heterozygous rare variants in NR2F2 cause a recognizable multiple
            congenital anomaly syndrome with developmental delays
  JOURNAL   Eur J Hum Genet 31 (10), 1117-1124 (2023)
   PUBMED   37500725
  REMARK    GeneRIF: Heterozygous rare variants in NR2F2 cause a recognizable
            multiple congenital anomaly syndrome with developmental delays.
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Dougherty,E.J., Chen,L.Y., Awad,K.S., Ferreyra,G.A.,
            Demirkale,C.Y., Keshavarz,A., Gairhe,S., Johnston,K.A., Hicks,M.E.,
            Sandler,A.B., Curran,C.S., Krack,J.M., Ding,Y., Suffredini,A.F.,
            Solomon,M.A., Elinoff,J.M. and Danner,R.L.
  TITLE     Inflammation and DKK1-induced AKT activation contribute to
            endothelial dysfunction following NR2F2 loss
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 324 (6), L783-L798 (2023)
   PUBMED   37039367
  REMARK    GeneRIF: Inflammation and DKK1-induced AKT activation contribute to
            endothelial dysfunction following NR2F2 loss.
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Davalos,V., Lovell,C.D., Von Itter,R., Dolgalev,I., Agrawal,P.,
            Baptiste,G., Kahler,D.J., Sokolova,E., Moran,S., Pique,L.,
            Vega-Saenz de Miera,E., Fontanals-Cirera,B., Karz,A., Tsirigos,A.,
            Yun,C., Darvishian,F., Etchevers,H.C., Osman,I., Esteller,M.,
            Schober,M. and Hernando,E.
  TITLE     An epigenetic switch controls an alternative NR2F2 isoform that
            unleashes a metastatic program in melanoma
  JOURNAL   Nat Commun 14 (1), 1867 (2023)
   PUBMED   37015919
  REMARK    GeneRIF: An epigenetic switch controls an alternative NR2F2 isoform
            that unleashes a metastatic program in melanoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Di-Luoffo,M., Pierre,K.J., Robert,N.M., Girard,M.J. and
            Tremblay,J.J.
  TITLE     The nuclear receptors SF1 and COUP-TFII cooperate on the Insl3
            promoter in Leydig cells
  JOURNAL   Reproduction 164 (2), 31-40 (2022)
   PUBMED   35666805
  REMARK    GeneRIF: The nuclear receptors SF1 and COUP-TFII cooperate on the
            Insl3 promoter in Leydig cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Li,W., Zhang,Z., Li,Y. and Wang,Z.
  TITLE     Abnormal hsa_circ_0003948 expression affects chronic periodontitis
            development by regulating miR-144-3p/NR2F2/PTEN signaling
  JOURNAL   J Periodontal Res 57 (2), 316-323 (2022)
   PUBMED   34910830
  REMARK    GeneRIF: Abnormal hsa_circ_0003948 expression affects chronic
            periodontitis development by regulating miR-144-3p/NR2F2/PTEN
            signaling.
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Qiu,Y., Krishnan,V., Zeng,Z., Gilbert,D.J., Copeland,N.G.,
            Gibson,L., Yang-Feng,T., Jenkins,N.A., Tsai,M.J. and Tsai,S.Y.
  TITLE     Isolation, characterization, and chromosomal localization of mouse
            and human COUP-TF I and II genes
  JOURNAL   Genomics 29 (1), 240-246 (1995)
   PUBMED   8530078
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Mietus-Snyder,M., Sladek,F.M., Ginsburg,G.S., Kuo,C.F.,
            Ladias,J.A., Darnell,J.E. Jr. and Karathanasis,S.K.
  TITLE     Antagonism between apolipoprotein AI regulatory protein 1,
            Ear3/COUP-TF, and hepatocyte nuclear factor 4 modulates
            apolipoprotein CIII gene expression in liver and intestinal cells
  JOURNAL   Mol Cell Biol 12 (4), 1708-1718 (1992)
   PUBMED   1312668
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Ladias,J.A. and Karathanasis,S.K.
  TITLE     Regulation of the apolipoprotein AI gene by ARP-1, a novel member
            of the steroid receptor superfamily
  JOURNAL   Science 251 (4993), 561-565 (1991)
   PUBMED   1899293
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Wang,L.H., Ing,N.H., Tsai,S.Y., O'Malley,B.W. and Tsai,M.J.
  TITLE     The COUP-TFs compose a family of functionally related transcription
            factors
  JOURNAL   Gene Expr 1 (3), 207-216 (1991)
   PUBMED   1820218
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016251.9 and BC042897.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the steroid thyroid hormone
            superfamily of nuclear receptors. The encoded protein is a ligand
            inducible transcription factor that is involved in the regulation
            of many different genes. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M62760.1, SRR1660809.174579.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394166.8/ ENSP00000377721.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.2"
     Protein         1..414
                     /product="COUP transcription factor 2 isoform a"
                     /note="ADP-ribosylation factor related protein 1; chicken
                     ovalbumin upstream promoter transcription factor 2;
                     chicken ovalbumin upstream promoter-transcription factor
                     I; COUP transcription factor II; apolipoprotein AI
                     regulatory protein 1; apolipoprotein A-I regulatory
                     protein 1"
                     /calculated_mol_wt=45440
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24468.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P24468.1)"
     Region          79..151
                     /region_name="NR_DBD_COUP_TF"
                     /note="DNA-binding domain of chicken ovalbumin upstream
                     promoter transcription factors (COUP-TFs) is composed of
                     two C4-type zinc fingers; cd06958"
                     /db_xref="CDD:143516"
     Site            order(79,82,96,99,115,121,131,134)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143516"
     Site            order(88..91,97..98,100,102,105,108,116,128..129,132,135,
                     146)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143516"
     Region          117..414
                     /region_name="Interaction with ZFPM2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P24468.1)"
     Region          177..411
                     /region_name="NR_LBD_COUP-TF"
                     /note="Ligand binding domain of chicken ovalbumin upstream
                     promoter transcription factors, a member of the nuclear
                     receptor family; cd06948"
                     /db_xref="CDD:132746"
     Site            order(211..212,216,250,254,257,271,292)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:132746"
     Site            order(221,224,228,233,238..239,241..242,245..246)
                     /site_type="active"
                     /note="putative coactivator recognition site [active]"
                     /db_xref="CDD:132746"
     Region          337..414
                     /region_name="Important for dimerization"
                     /note="propagated from UniProtKB/Swiss-Prot (P24468.1)"
     CDS             1..414
                     /gene="NR2F2"
                     /gene_synonym="ARP-1; ARP1; CHTD4; COUPTF2; COUPTFB;
                     COUPTFII; NF-E3; SRXX5; SVP40; TFCOUP2"
                     /coded_by="NM_021005.4:1407..2651"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10375.1"
                     /db_xref="GeneID:7026"
                     /db_xref="HGNC:HGNC:7976"
                     /db_xref="MIM:107773"
ORIGIN      
        1 mamvvstwrd pqdevpgsqg sqasqappvp gpppgaphtp qtpgqggpas tpaqtaaggq
       61 ggpggpgsdk qqqqqhiecv vcgdkssgkh ygqftcegck sffkrsvrrn lsytcranrn
      121 cpidqhhrnq cqycrlkkcl kvgmrreavq rgrmpptqpt hgqfaltngd plnchsylsg
      181 yislllraep yptsrfgsqc mqpnnimgie nicelaarml fsavewarni pffpdlqitd
      241 qvallrltws elfvlnaaqc smplhvapll aaaglhaspm sadrvvafmd hirifqeqve
      301 klkalhvdsa eysclkaivl ftsdacglsd vahveslqek sqcaleeyvr sqypnqptrf
      361 gklllrlpsl rtvsssvieq lffvrlvgkt pietlirdml lsgssfnwpy maiq
//
LOCUS       NP_001018855             778 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 749 isoform 1 [Homo sapiens].
ACCESSION   NP_001018855 XP_371200
VERSION     NP_001018855.2
DBSOURCE    REFSEQ: accession NM_001023561.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Tsuritani,K., Irie,T., Yamashita,R., Sakakibara,Y., Wakaguri,H.,
            Kanai,A., Mizushima-Sugano,J., Sugano,S., Nakai,K. and Suzuki,Y.
  TITLE     Distinct class of putative 'non-conserved' promoters in humans:
            comparative studies of alternative promoters of human and mouse
            genes
  JOURNAL   Genome Res 17 (7), 1005-1014 (2007)
   PUBMED   17567985
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP872084.1, DB099619.1, AK122794.1 and AC004076.1.
            
            On May 2, 2007 this sequence version replaced NP_001018855.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.250227.1,
                                           SRR1660809.203047.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334181.5/ ENSP00000333980.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..778
                     /product="zinc finger protein 749 isoform 1"
                     /calculated_mol_wt=90234
     Region          7..48
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          202..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          258..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          295..689
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          356..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          384..404
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(389,391,393,395..396,399..400,403,417,419,423..424,
                     427..428,431,445,447,449,451..452,455..456,459)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          412..432
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          440..460
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            466
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O43361.2)"
     Region          485..505
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          513..533
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            539
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O43361.2)"
     Region          558..578
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          586..606
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(591,593,595,597..598,601..602,605,619,621,625..626,
                     629..630,633,647,649,651,653..654,657..658,661)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          614..634
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          642..662
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          670..689
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          698..718
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          727..745
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          753..773
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..778
                     /gene="ZNF749"
                     /coded_by="NM_001023561.4:255..2591"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33132.2"
                     /db_xref="GeneID:388567"
                     /db_xref="HGNC:HGNC:32783"
ORIGIN      
        1 mnltedcmvf edvaiyfsqe ewgilndaqr hlhsnvmlen fallssvgcw hgakdeevps
       61 kqcvsvrvlq vtipkpalst lkaqpckmcs silkdilhla ehdgthpeqg lytcaaehdl
      121 hqkeqirekl trsdewrpsf vnhsahvger nftctqggkd ftassdllqq qvlnsgwkly
      181 rdtqdgeafq geqndfnssq ggkdfchqhg lfehqkthng erpyefsecg elfrynsnli
      241 kyqqnhager pyegteygkt firksnlvqh qkihsegfls krsdpiehqe ilsrptpyec
      301 tqcgkafltq ahlvghqkth tgeqpyecnk cgkffmynsk lirhqkvhtg erryecsecg
      361 klfmdsftlg rhqrvhtger pfecsicgkf fshrstlnmh qrvhagkrly kcsecgkafs
      421 lkhnvvqhlk ihtgerpyec tecekafvrk shlvqhqkih tdafskrsdl iqhkridirp
      481 rpytcsecgk afltqahlvg hqkihtgerp yectqcakaf vrkshlvqhe kihtdafskr
      541 sdliqhkrid lrprpyvcse cgkafltqah ldghqkiqtg erryecnecg kffldsyklv
      601 ihqrihtgek pykcskcgkf fryrctlsrh qkvhtgerpy ecsecgkffr dsykliihqr
      661 vhtgekpyec sncgkflryr stfikhhkvc tgekphecsk crelfrtkss liihqqshtg
      721 espfklrecg kdfnkcntgq rqkthtgers yecgesskvf kynsslikhq iihtgkrp
//
LOCUS       NP_001508                462 aa            linear   PRI 27-APR-2025
DEFINITION  general transcription factor IIH subunit 4 [Homo sapiens].
ACCESSION   NP_001508 XP_378195
VERSION     NP_001508.1
DBSOURCE    REFSEQ: accession NM_001517.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Hoag,A., Duan,M. and Mao,P.
  TITLE     The role of Transcription Factor IIH complex in nucleotide excision
            repair
  JOURNAL   Environ Mol Mutagen 65 Suppl 1 (Suppl 1), 72-81 (2024)
   PUBMED   37545038
  REMARK    GeneRIF: The role of Transcription Factor IIH complex in nucleotide
            excision repair.
            Review article
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Porter,L.F., Saptarshi,N., Fang,Y., Rathi,S., den Hollander,A.I.,
            de Jong,E.K., Clark,S.J., Bishop,P.N., Olsen,T.W., Liloglou,T.,
            Chavali,V.R.M. and Paraoan,L.
  TITLE     Whole-genome methylation profiling of the retinal pigment
            epithelium of individuals with age-related macular degeneration
            reveals differential methylation of the SKI, GTF2H4, and TNXB genes
  JOURNAL   Clin Epigenetics 11 (1), 6 (2019)
   PUBMED   30642396
  REMARK    GeneRIF: Data demonstrates gene expression changes in
            differentially methylated GTF2H4 gene in patients with age-related
            macular degeneration.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Zhou,Q. and Sharp,P.A.
  TITLE     Tat-SF1: cofactor for stimulation of transcriptional elongation by
            HIV-1 Tat
  JOURNAL   Science 274 (5287), 605-610 (1996)
   PUBMED   8849451
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Drapkin,R., Le Roy,G., Cho,H., Akoulitchev,S. and Reinberg,D.
  TITLE     Human cyclin-dependent kinase-activating kinase exists in three
            distinct complexes
  JOURNAL   Proc Natl Acad Sci U S A 93 (13), 6488-6493 (1996)
   PUBMED   8692842
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Blau,J., Xiao,H., McCracken,S., O'Hare,P., Greenblatt,J. and
            Bentley,D.
  TITLE     Three functional classes of transcriptional activation domain
  JOURNAL   Mol Cell Biol 16 (5), 2044-2055 (1996)
   PUBMED   8628270
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI460355.1, BC004935.1 and AL669830.9.
            
            On Oct 18, 2004 this sequence version replaced XP_378195.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.84695.1, BC004935.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259895.9/ ENSP00000259895.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..462
                     /product="general transcription factor IIH subunit 4"
                     /note="TFIIH basal transcription factor complex p52
                     subunit; BTF2 p52; basic transcription factor 2 52 kDa
                     subunit; general transcription factor IIH polypeptide 4;
                     general transcription factor IIH, polypeptide 4, 52kDa"
                     /calculated_mol_wt=52055
     Region          18..460
                     /region_name="tfb2"
                     /note="Transcription factor tfb2; TIGR00625"
                     /db_xref="CDD:273180"
     CDS             1..462
                     /gene="GTF2H4"
                     /gene_synonym="P52; TFB2; TFIIH"
                     /coded_by="NM_001517.5:201..1589"
                     /db_xref="CCDS:CCDS34386.1"
                     /db_xref="GeneID:2968"
                     /db_xref="HGNC:HGNC:4658"
                     /db_xref="MIM:601760"
ORIGIN      
        1 mestpsrgln rvhlqcrnlq eflgglspgv ldrlyghpat clavfrelps laknwvmrml
       61 fleqplpqaa valwvkkefs kaqeestgll sglriwhtql lpgglqglil npifrqnlri
      121 allgggkaws ddtsqlgpdk hardvpsldk yaeerwevvl hfmvgspsaa vsqdlaqlls
      181 qaglmkstep geppcitsag fqfllldtpa qlwyfmlqyl qtaqsrgmdl veilsflfql
      241 sfstlgkdys vegmsdslln flqhlrefgl vfqrkrksrr yyptrlainl ssgvsgaggt
      301 vhqpgfivve tnyrlyayte selqialial fsemlyrfpn mvvaqvtres vqqaiasgit
      361 aqqiihflrt rahpvmlkqt pvlpptitdq irlwelerdr lrftegvlyn qflsqvdfel
      421 llaharelgv lvfensakrl mvvtpaghsd vkrfwkrqkh ss
//
LOCUS       NP_004543                106 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 [Homo
            sapiens].
ACCESSION   NP_004543
VERSION     NP_004543.1
DBSOURCE    REFSEQ: accession NM_004552.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Salscheider,S.L., Gerlich,S., Cabrera-Orefice,A., Peker,E.,
            Rothemann,R.A., Murschall,L.M., Finger,Y., Szczepanowska,K.,
            Ahmadi,Z.A., Guerrero-Castillo,S., Erdogan,A., Becker,M., Ali,M.,
            Habich,M., Petrungaro,C., Burdina,N., Schwarz,G., Klussmann,M.,
            Neundorf,I., Stroud,D.A., Ryan,M.T., Trifunovic,A., Brandt,U. and
            Riemer,J.
  TITLE     AIFM1 is a component of the mitochondrial disulfide relay that
            drives complex I assembly through efficient import of NDUFS5
  JOURNAL   EMBO J 41 (17), e110784 (2022)
   PUBMED   35859387
  REMARK    GeneRIF: AIFM1 is a component of the mitochondrial disulfide relay
            that drives complex I assembly through efficient import of NDUFS5.
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Iwahana,T., Okada,S., Kanda,M., Oshima,M., Iwama,A., Matsumiya,G.
            and Kobayashi,Y.
  TITLE     Novel myocardial markers GADD45G and NDUFS5 identified by
            RNA-sequencing predicts left ventricular reverse remodeling in
            advanced non-ischemic heart failure: a retrospective cohort study
  JOURNAL   BMC Cardiovasc Disord 20 (1), 116 (2020)
   PUBMED   32138671
  REMARK    GeneRIF: Novel myocardial markers GADD45G and NDUFS5 identified by
            RNA-sequencing predicts left ventricular reverse remodeling in
            advanced non-ischemic heart failure: a retrospective cohort study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Triepels,R.H., Hanson,B.J., van den Heuvel,L.P., Sundell,L.,
            Marusich,M.F., Smeitink,J.A. and Capaldi,R.A.
  TITLE     Human complex I defects can be resolved by monoclonal antibody
            analysis into distinct subunit assembly patterns
  JOURNAL   J Biol Chem 276 (12), 8892-8897 (2001)
   PUBMED   11112787
REFERENCE   7  (residues 1 to 106)
  AUTHORS   Loeffen,J., Smeets,R., Smeitink,J., Triepels,R., Sengers,R.,
            Trijbels,F. and van den Heuvel,L.
  TITLE     The human NADH: ubiquinone oxidoreductase NDUFS5 (15 kDa) subunit:
            cDNA cloning, chromosomal localization, tissue distribution and the
            absence of mutations in isolated complex I-deficient patients
  JOURNAL   J Inherit Metab Dis 22 (1), 19-28 (1999)
   PUBMED   10070614
REFERENCE   8  (residues 1 to 106)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   9  (residues 1 to 106)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
REFERENCE   10 (residues 1 to 106)
  AUTHORS   Emahazion,T., Beskow,A., Gyllensten,U. and Brookes,A.J.
  TITLE     Intron based radiation hybrid mapping of 15 complex I genes of the
            human electron transport chain
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 115-119 (1998)
   PUBMED   9763677
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL606465.21, BC093057.1 and
            AI244607.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the NADH dehydrogenase
            (ubiquinone) iron-sulfur protein family. The encoded protein is a
            subunit of the NADH:ubiquinone oxidoreductase (complex I), the
            first enzyme complex in the electron transport chain located in the
            inner mitochondrial membrane. Alternative splicing results in
            multiple transcript variants and pseudogenes have been identified
            on chromosomes 1, 4 and 17. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF047434.1, SRR1163658.204720.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000372969.8/
                                                  ENSP00000362060.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..106
                     /product="NADH dehydrogenase [ubiquinone] iron-sulfur
                     protein 5"
                     /EC_number="7.1.1.2"
                     /note="CI-15 kDa; NADH:ubiquinone oxidoreductase 15 kDa IP
                     subunit; complex I-15 kDa; NADH dehydrogenase (ubiquinone)
                     Fe-S protein 5, 15kDa (NADH-coenzyme Q reductase)"
                     /calculated_mol_wt=12386
     Region          1..96
                     /region_name="Ndufs5"
                     /note="NADH:ubiquinone oxidoreductase, NDUFS5-15kDa;
                     pfam10200"
                     /db_xref="CDD:431131"
     Region          33..43
                     /region_name="Cx9C motif 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (O43920.3)"
     Region          56..66
                     /region_name="Cx9C motif 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (O43920.3)"
     Region          84..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43920.3)"
     CDS             1..106
                     /gene="NDUFS5"
                     /gene_synonym="CI-15k; CI15K"
                     /coded_by="NM_004552.3:56..376"
                     /db_xref="CCDS:CCDS434.1"
                     /db_xref="GeneID:4725"
                     /db_xref="HGNC:HGNC:7712"
                     /db_xref="MIM:603847"
ORIGIN      
        1 mpfldiqkrf glnidrwlti qsgeqpykma grchafekew iecahgigyt raekeckiey
       61 ddfvecllrq ktmrragtir kqrdklikeg kytppphhig kgeprp
//
LOCUS       NP_001028485             181 aa            linear   ROD 27-APR-2025
DEFINITION  28 kDa heat- and acid-stable phosphoprotein [Mus musculus].
ACCESSION   NP_001028485 XP_891612 XP_922437
VERSION     NP_001028485.1
DBSOURCE    REFSEQ: accession NM_001033313.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Delgado-Benito,V., Berruezo-Llacuna,M., Altwasser,R., Winkler,W.,
            Sundaravinayagam,D., Balasubramanian,S., Caganova,M., Graf,R.,
            Rahjouei,A., Henke,M.T., Driesner,M., Keller,L., Prigione,A.,
            Janz,M., Akalin,A. and Di Virgilio,M.
  TITLE     PDGFA-associated protein 1 protects mature B lymphocytes from
            stress-induced cell death and promotes antibody gene
            diversification
  JOURNAL   J Exp Med 217 (10) (2020)
   PUBMED   32609329
  REMARK    GeneRIF: PDGFA-associated protein 1 protects mature B lymphocytes
            from stress-induced cell death and promotes antibody gene
            diversification.
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Saba,L., Bhave,S.V., Grahame,N., Bice,P., Lapadat,R., Belknap,J.,
            Hoffman,P.L. and Tabakoff,B.
  TITLE     Candidate genes and their regulatory elements: alcohol preference
            and tolerance
  JOURNAL   Mamm Genome 17 (6), 669-688 (2006)
   PUBMED   16783646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC110556.15.
            
            On or before Jan 12, 2006 this sequence version replaced
            XP_922437.1, XP_891612.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK147170.1, FO716593.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849382, SAMN00849386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 85.04 cM"
     Protein         1..181
                     /product="28 kDa heat- and acid-stable phosphoprotein"
                     /note="PDGF-associated protein"
                     /calculated_mol_wt=20474
     Region          1..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13442; propagated from
                     UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13442; propagated from
                     UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:18630941,
                     ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:18630941,
                     ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Region          85..149
                     /region_name="PP28"
                     /note="Casein kinase substrate phosphoprotein PP28;
                     pfam10252"
                     /db_xref="CDD:463025"
     Site            126
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13442; propagated from
                     UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Site            132
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13442; propagated from
                     UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Region          151..181
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Site            164
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13442; propagated from
                     UniProtKB/Swiss-Prot (Q3UHX2.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13442; propagated from
                     UniProtKB/Swiss-Prot (Q3UHX2.1)"
     CDS             1..181
                     /gene="Pdap1"
                     /gene_synonym="HASPP28; PAP; PAP1"
                     /coded_by="NM_001033313.4:47..592"
                     /db_xref="CCDS:CCDS39384.1"
                     /db_xref="GeneID:231887"
                     /db_xref="MGI:MGI:2448536"
ORIGIN      
        1 mpkggrkggh kgrvrqytsp eeidaqlqae kqkaneedeq eeggdgasgd pkkekkslds
       61 desededddy qqkrkgvegl idienpnrva qttkkvtqld ldgpkelsrr ereeiekqka
      121 kerymkmhla gkteqakadl arlaiirkqr eeaarkkeee rkakddatls gkrmqslsln
      181 k
//
LOCUS       NP_001347577             193 aa            linear   ROD 27-APR-2025
DEFINITION  tubulin-folding cofactor B isoform 2 [Mus musculus].
ACCESSION   NP_001347577 XP_011248974
VERSION     NP_001347577.1
DBSOURCE    REFSEQ: accession NM_001360648.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Kuh,G.F., Stockmann,M., Meyer-Ohlendorf,M., Linta,L., Proepper,C.,
            Ludolph,A.C., Bockmann,J., Boeckers,T.M. and Liebau,S.
  TITLE     Tubulin-binding cofactor B is a direct interaction partner of the
            dynactin subunit p150(Glued)
  JOURNAL   Cell Tissue Res 350 (1), 13-26 (2012)
   PUBMED   22777741
  REMARK    GeneRIF: Overexpression of TBCB leads to the decreased localization
            of p150 to the microtubule network that might result in a
            functional modulation of this protein complex.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Lo,J.C., Jamsai,D., O'Connor,A.E., Borg,C., Clark,B.J.,
            Whisstock,J.C., Field,M.C., Adams,V., Ishikawa,T., Aitken,R.J.,
            Whittle,B., Goodnow,C.C., Ormandy,C.J. and O'Bryan,M.K.
  TITLE     RAB-like 2 has an essential role in male fertility, sperm
            intra-flagellar transport, and tail assembly
  JOURNAL   PLoS Genet 8 (10), e1002969 (2012)
   PUBMED   23055941
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Ganay,T., Boizot,A., Burrer,R., Chauvin,J.P. and Bomont,P.
  TITLE     Sensory-motor deficits and neurofilament disorganization in
            gigaxonin-null mice
  JOURNAL   Mol Neurodegener 6, 25 (2011)
   PUBMED   21486449
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Wen,H.L., Lin,Y.T., Ting,C.H., Lin-Chao,S., Li,H. and Hsieh-Li,H.M.
  TITLE     Stathmin, a microtubule-destabilizing protein, is dysregulated in
            spinal muscular atrophy
  JOURNAL   Hum Mol Genet 19 (9), 1766-1778 (2010)
   PUBMED   20176735
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Lopez-Fanarraga,M., Carranza,G., Bellido,J., Kortazar,D.,
            Villegas,J.C. and Zabala,J.C.
  TITLE     Tubulin cofactor B plays a role in the neuronal growth cone
  JOURNAL   J Neurochem 100 (6), 1680-1687 (2007)
   PUBMED   17217416
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Kortazar,D., Fanarraga,M.L., Carranza,G., Bellido,J.,
            Villegas,J.C., Avila,J. and Zabala,J.C.
  TITLE     Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer
            dissociation
  JOURNAL   Exp Cell Res 313 (3), 425-436 (2007)
   PUBMED   17184771
  REMARK    GeneRIF: We show that TBCB overexpression depolymerizes
            microtubules. We found that this function is based on the ability
            of TBCB to form a binary complex with TBCE that greatly enhances
            the efficiency of this cofactor to dissociate tubulin in vivo and
            in vitro.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC149067.3.
            
            On Feb 8, 2018 this sequence version replaced XP_011248974.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2) is
            shorter at the N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.539730.1,
                                           SRR7345562.2742243.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN01164134
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 17.33 cM"
     Protein         1..193
                     /product="tubulin-folding cofactor B isoform 2"
                     /note="cytoskeleton-associated protein 1; tubulin-specific
                     chaperone B; cytoskeleton-associated protein CKAPI"
                     /calculated_mol_wt=21714
     Region          <1..38
                     /region_name="Ubl_TBCB"
                     /note="ubiquitin-like (Ubl) domain found in
                     tubulin-folding cofactor B (TBCB) and similar proteins;
                     cd01789"
                     /db_xref="CDD:340487"
     Region          110..178
                     /region_name="CAP_GLY"
                     /note="CAP-Gly domain; pfam01302"
                     /db_xref="CDD:460154"
     CDS             1..193
                     /gene="Tbcb"
                     /gene_synonym="2410007D12Rik; CG22; Ckap1; CKAPI"
                     /coded_by="NM_001360648.1:74..655"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:66411"
                     /db_xref="MGI:MGI:1913661"
ORIGIN      
        1 melelygadd kfyskldqed allgsypvdd gcrihvidhs gvrlgeyedv skvekyeisp
       61 eayerrqntv rsfmkrsklg pyneelraqq eaeaaqrlse ekaqasaisv gsrcevrapd
      121 hslrrgtvmy vgltdfkpgy wvgvrydepl gkndgsvngk ryfecqakyg afvkpsavtv
      181 gdfpeedygl dem
//
LOCUS       NP_005860                472 aa            linear   PRI 27-APR-2025
DEFINITION  spliceosome-associated protein CWC27 homolog isoform 1 [Homo
            sapiens].
ACCESSION   NP_005860
VERSION     NP_005860.2
DBSOURCE    REFSEQ: accession NM_005869.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Yassin,S.H., Henderson,R., Lenberg,J., Murillo,V., Murdock,D.R.,
            Friedman,J., Jones,M.C., Wigby,K. and Borooah,S.
  TITLE     Further delineation of the CWC27-associated spliceosomeopathy: Case
            report and review of the literature
  JOURNAL   Am J Med Genet A 191 (5), 1378-1383 (2023)
   PUBMED   36718996
  REMARK    GeneRIF: Further delineation of the CWC27-associated
            spliceosomeopathy: Case report and review of the literature.
            Review article
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Busetto,V., Barbosa,I., Basquin,J., Marquenet,E., Hocq,R.,
            Hennion,M., Paternina,J.A., Namane,A., Conti,E., Bensaude,O. and Le
            Hir,H.
  TITLE     Structural and functional insights into CWC27/CWC22 heterodimer
            linking the exon junction complex to spliceosomes
  JOURNAL   Nucleic Acids Res 48 (10), 5670-5683 (2020)
   PUBMED   32329775
  REMARK    GeneRIF: Structural and functional insights into CWC27/CWC22
            heterodimer linking the exon junction complex to spliceosomes.
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   5  (residues 1 to 472)
  AUTHORS   Xu,M., Xie,Y.A., Abouzeid,H., Gordon,C.T., Fiorentino,A., Sun,Z.,
            Lehman,A., Osman,I.S., Dharmat,R., Riveiro-Alvarez,R.,
            Bapst-Wicht,L., Babino,D., Arno,G., Busetto,V., Zhao,L., Li,H.,
            Lopez-Martinez,M.A., Azevedo,L.F., Hubert,L., Pontikos,N.,
            Eblimit,A., Lorda-Sanchez,I., Kheir,V., Plagnol,V., Oufadem,M.,
            Soens,Z.T., Yang,L., Bole-Feysot,C., Pfundt,R., Allaman-Pillet,N.,
            Nitschke,P., Cheetham,M.E., Lyonnet,S., Agrawal,S.A., Li,H.,
            Pinton,G., Michaelides,M., Besmond,C., Li,Y., Yuan,Z., von
            Lintig,J., Webster,A.R., Le Hir,H., Stoilov,P., Amiel,J.,
            Hardcastle,A.J., Ayuso,C., Sui,R., Chen,R., Allikmets,R. and
            Schorderet,D.F.
  CONSRTM   UK Inherited Retinal Dystrophy Consortium
  TITLE     Mutations in the Spliceosome Component CWC27 Cause Retinal
            Degeneration with or without Additional Developmental Anomalies
  JOURNAL   Am J Hum Genet 100 (4), 592-604 (2017)
   PUBMED   28285769
  REMARK    GeneRIF: By whole-exome sequencing, recessive protein-truncating
            mutations in CWC27 were found in seven unrelated families that show
            a range of clinical phenotypes, including retinal degeneration,
            brachydactyly, craniofacial abnormalities, short stature, and
            neurologic defects.
REFERENCE   6  (residues 1 to 472)
  AUTHORS   Wang,M., Li,Z., Chu,H., Lv,Q., Ye,D., Ding,Q., Xu,C., Guo,J.,
            Du,M., Chen,J., Song,Z., Yin,C., Qin,C., Gu,C., Zhu,Y., Xia,G.,
            Liu,F., Zhang,Z., Yuan,L., Fu,G., Hu,Z., Tong,N., Shen,J., Liu,K.,
            Sun,J., Sun,Y., Li,J., Li,X., Shen,H., Xu,J., Shi,Y. and Zhang,Z.
  TITLE     Genome-Wide Association Study of Bladder Cancer in a Chinese Cohort
            Reveals a New Susceptibility Locus at 5q12.3
  JOURNAL   Cancer Res 76 (11), 3277-3284 (2016)
   PUBMED   27206850
  REMARK    GeneRIF: CWC27 overexpression is associated with Bladder Cancer.
REFERENCE   7  (residues 1 to 472)
  AUTHORS   Ulrich,A. and Wahl,M.C.
  TITLE     Structure and evolution of the spliceosomal peptidyl-prolyl
            cis-trans isomerase Cwc27
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 12), 3110-3123 (2014)
   PUBMED   25478830
  REMARK    GeneRIF: The crystal structure of a relatively protease-resistant
            N-terminal fragment of human Cwc27 containing the cyclophilin-type
            peptidyl-prolyl cis-trans isomerase domain was determined at 2.0 A
            resolution.
REFERENCE   8  (residues 1 to 472)
  AUTHORS   Davis,T.L., Walker,J.R., Campagna-Slater,V., Finerty,P.J.,
            Paramanathan,R., Bernstein,G., MacKenzie,F., Tempel,W., Ouyang,H.,
            Lee,W.H., Eisenmesser,E.Z. and Dhe-Paganon,S.
  TITLE     Structural and biochemical characterization of the human
            cyclophilin family of peptidyl-prolyl isomerases
  JOURNAL   PLoS Biol 8 (7), e1000439 (2010)
   PUBMED   20676357
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 472)
  AUTHORS   Fabrizio,P., Dannenberg,J., Dube,P., Kastner,B., Stark,H.,
            Urlaub,H. and Luhrmann,R.
  TITLE     The evolutionarily conserved core design of the catalytic
            activation step of the yeast spliceosome
  JOURNAL   Mol Cell 36 (4), 593-608 (2009)
   PUBMED   19941820
REFERENCE   10 (residues 1 to 472)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX647971.1, BC012117.1, AK225105.1 and BG193598.1.
            
            On May 13, 2005 this sequence version replaced NP_005860.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.259211.1,
                                           SRR1660807.139360.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381070.8/ ENSP00000370460.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..472
                     /product="spliceosome-associated protein CWC27 homolog
                     isoform 1"
                     /EC_number="5.2.1.8"
                     /note="serologically defined colon cancer antigen 10;
                     peptidyl-prolyl cis-trans isomerase SDCCAG10;
                     peptidyl-prolyl cis-trans isomerase CWC27 homolog; PPIase
                     SDCCAG10; antigen NY-CO-10; PPIase CWC27; probable
                     inactive peptidyl-prolyl cis-trans isomerase CWC27
                     homolog; spliceosome-associated protein CWC27 homolog;
                     CWC27 spliceosome associated protein homolog"
                     /calculated_mol_wt=53716
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     Region          8..178
                     /region_name="cyclophilin_CeCYP16-like"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerase) (PPIase) domain similar to Caenorhabditis
                     elegans cyclophilin 16. C. elegans CeCYP-16, compared to
                     the archetypal cyclophilin Human cyclophilin A has, a
                     reduced peptidylprolyl cis- trans isomerase...; cd01925"
                     /db_xref="CDD:238906"
     Site            order(55..56,61,112,114,122)
                     /site_type="active"
                     /db_xref="CDD:238906"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     Site            201
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     Region          206..386
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UX04.1)"
     Region          <302..>472
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5XIB2; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     Region          376..428
                     /region_name="CWC27_CTD"
                     /note="C-terminal domain of spliceosome-associated protein
                     CWC27 and similar proteins; cd22288"
                     /db_xref="CDD:412084"
     Site            order(380,382,384..389,391..393,395..397,400,406,412..414,
                     416..419,421..426)
                     /site_type="other"
                     /note="CWC27 binding site [polypeptide binding]"
                     /db_xref="CDD:412084"
     Region          398..472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UX04.1)"
     CDS             1..472
                     /gene="CWC27"
                     /gene_synonym="NY-CO-10; RPSKA; SDCCAG-10; SDCCAG10"
                     /coded_by="NM_005869.4:218..1636"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3982.2"
                     /db_xref="GeneID:10283"
                     /db_xref="HGNC:HGNC:10664"
                     /db_xref="MIM:617170"
ORIGIN      
        1 msniyiqepp tngkvllktt agdidielws keapkacrnf iqlcleayyd ntifhrvvpg
       61 fivqggdptg tgsggesiyg apfkdefhsr lrfnrrglva managshdng sqffftlgra
      121 delnnkhtif gkvtgdtvyn mlrlsevdid dderphnphk ikscevlfnp fddiipreik
      181 rlkkekpeee vkklkpkgtk nfsllsfgee aeeeeeevnr vsqsmkgksk sshdllkddp
      241 hlssvpvves ekgdapdlvd dgedesaehd eyidgdeknl mreriakklk kdtsanvksa
      301 gegevekksv srseelrkea rqlkrellaa kqkkvenaak qaekrseeee appdgavaey
      361 rrekqkyeal rkqqskkgts redqtlalln qfkskltqai aetpendipe teveddegwm
      421 shvlqfedks rkvkdasmqd sdtfeiydpr npvnkrrree skklmrekke rr
//
LOCUS       NP_001354863            1209 aa            linear   PRI 27-APR-2025
DEFINITION  phospholipid-transporting ATPase ID isoform c [Homo sapiens].
ACCESSION   NP_001354863
VERSION     NP_001354863.1
DBSOURCE    REFSEQ: accession NM_001367934.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1209)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   2  (residues 1 to 1209)
  AUTHORS   Takatsu,H., Tanaka,G., Segawa,K., Suzuki,J., Nagata,S., Nakayama,K.
            and Shin,H.W.
  TITLE     Phospholipid flippase activities and substrate specificities of
            human type IV P-type ATPases localized to the plasma membrane
  JOURNAL   J Biol Chem 289 (48), 33543-33556 (2014)
   PUBMED   25315773
  REMARK    Erratum:[J Biol Chem. 2016 Oct 7;291(41):21421. doi:
            10.1074/jbc.A114.593012. PMID: 27825076]
REFERENCE   3  (residues 1 to 1209)
  AUTHORS   Bryde,S., Hennrich,H., Verhulst,P.M., Devaux,P.F., Lenoir,G. and
            Holthuis,J.C.
  TITLE     CDC50 proteins are critical components of the human class-1
            P4-ATPase transport machinery
  JOURNAL   J Biol Chem 285 (52), 40562-40572 (2010)
   PUBMED   20961850
REFERENCE   4  (residues 1 to 1209)
  AUTHORS   van der Velden,L.M., Wichers,C.G., van Breevoort,A.E.,
            Coleman,J.A., Molday,R.S., Berger,R., Klomp,L.W. and van de
            Graaf,S.F.
  TITLE     Heteromeric interactions required for abundance and subcellular
            localization of human CDC50 proteins and class 1 P4-ATPases
  JOURNAL   J Biol Chem 285 (51), 40088-40096 (2010)
   PUBMED   20947505
REFERENCE   5  (residues 1 to 1209)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 1209)
  AUTHORS   Paulusma,C.C. and Oude Elferink,R.P.
  TITLE     The type 4 subfamily of P-type ATPases, putative aminophospholipid
            translocases with a role in human disease
  JOURNAL   Biochim Biophys Acta 1741 (1-2), 11-24 (2005)
   PUBMED   15919184
  REMARK    Review article
REFERENCE   7  (residues 1 to 1209)
  AUTHORS   Kuhlbrandt,W.
  TITLE     Biology, structure and mechanism of P-type ATPases
  JOURNAL   Nat Rev Mol Cell Biol 5 (4), 282-295 (2004)
   PUBMED   15071553
  REMARK    Review article
REFERENCE   8  (residues 1 to 1209)
  AUTHORS   Harris,M.J. and Arias,I.M.
  TITLE     FIC1, a P-type ATPase linked to cholestatic liver disease, has
            homologues (ATP8B2 and ATP8B3) expressed throughout the body
  JOURNAL   Biochim Biophys Acta 1633 (2), 127-131 (2003)
   PUBMED   12880872
REFERENCE   9  (residues 1 to 1209)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1209)
  AUTHORS   Abbott,W.M., Mellor,A., Edwards,Y. and Feizi,T.
  TITLE     Soluble bovine galactose-binding lectin. cDNA cloning reveals the
            complete amino acid sequence and an antigenic relationship with the
            major encephalitogenic domain of myelin basic protein
  JOURNAL   Biochem J 259 (1), 283-290 (1989)
   PUBMED   2470348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162591.16.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of
            aminophospholipid-transporting ATPases. The aminophospholipid
            translocases transport phosphatidylserine and
            phosphatidylethanolamine from one side of a bilayer to another.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.216292.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..1209
                     /product="phospholipid-transporting ATPase ID isoform c"
                     /EC_number="7.6.2.1"
                     /note="phospholipid-transporting ATPase ID; probable
                     phospholipid-transporting ATPase ID; ATPase, class I, type
                     8B, member 2; P4-ATPase flippase complex alpha subunit
                     ATP8B2; 36/8-9 fusion protein with epitope for anti-lectin
                     antibody; ATPase, aminophospholipid transporter, class I,
                     type 8B, member 2"
                     /calculated_mol_wt=137310
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Region          50..991
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            65..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            93..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            296..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            347..368
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            order(411..413,556,579..581,646,693..695,807,810,813,833,
                     836)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            411..417
                     /site_type="other"
                     /note="P-type ATPase signature motif"
                     /db_xref="CDD:319770"
     Site            411
                     /site_type="phosphorylation"
                     /note="phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:319770"
     Site            890..910
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            923..942
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            973..994
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            1009..1031
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            1038..1058
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            1079..1103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            1175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P98198.2)"
     Region          1181..1209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     CDS             1..1209
                     /gene="ATP8B2"
                     /gene_synonym="ATPID"
                     /coded_by="NM_001367934.1:191..3820"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91062.1"
                     /db_xref="GeneID:57198"
                     /db_xref="HGNC:HGNC:13534"
                     /db_xref="MIM:605867"
ORIGIN      
        1 mtvpkempek waraqappsw srkkpswgte eerrarandr eynekfqyas nciktskyni
       61 ltflpvnlfe qfqevantyf lfllilqlip qisslswftt ivplvlvlti tavkdatddy
      121 frhksdnqvn nrqsqvling ilqqeqwmnv cvgdiiklen nqfvaadlll lsssephglc
      181 yietaeldge tnmkvrqaip vtselgdisk lakfdgevic eppnnkldkf sgtlywkenk
      241 fplsnqnmll rgcvlrntew cfglvifagp dtklmqnsgr tkfkrtsidr lmntlvlwif
      301 gflvcmgvil aignaiwehe vgmrfqvylp wdeavdsaff sgflsfwsyi iilntvvpis
      361 lyvsvevirl ghsyfinwdk kmfcmkkrtp aeartttlne elgqveyifs dktgtltqni
      421 mvfnkcsing hsygdvfdvl ghkaelgerp epvdfsfnpl adkkflfwdp slleavkigd
      481 phtheffrll slchtvmsee knegelyyka qspdegalvt aarnfgfvfr srtpktitvh
      541 emgtaityql laildfnnir krmsvivrnp egkirlyckg adtilldrlh hstqellntt
      601 mdhlneyage glrtlvlayk dldeeyyeew aerrlqasla qdsredrlas iyeevennmm
      661 llgataiedk lqqgvpetia lltlanikiw vltgdkqeta vnigysckml tddmtevfiv
      721 tghtvlevre elrkarekmm dssrsvgngf tyqdklsssk ltsvleavag eyalvinghs
      781 lahaleadme lefletacac kaviccrvtp lqkaqvvelv kkykkavtla igdgandvsm
      841 iktahigvgi sgqegiqavl asdysfsqfk flqrlllvhg rwsylrmckf lcyffyknfa
      901 ftmvhfwfgf fcgfsaqtvy dqyfitlyni vytslpvlam gvfdqdvpeq rsmeypklye
      961 pgqlnllfnk refficiaqg iytsvlmffi pygvfadatr ddgtqladyq sfavtvatsl
     1021 vivvsvqigl dtgywtainh ffiwgslavy failfamhsn glfdmfpnqf rfvgnaqntl
     1081 aqptvwltiv lttvvcimpv vafrflrlnl kpdlsdtvry tqlvrkkqka qhrcmrrvgr
     1141 tgsrrsgyaf shqegfgeli msgknmrlss lalssfttrs ssswieslrr kksdsassps
     1201 ggadkplkg
//
LOCUS       NP_001091742             520 aa            linear   PRI 27-APR-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, cytoplasmic isoform 1 [Homo
            sapiens].
ACCESSION   NP_001091742
VERSION     NP_001091742.1
DBSOURCE    REFSEQ: accession NM_001098272.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zhang,M., Du,G., Xie,L., Xu,Y. and Chen,W.
  TITLE     Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction
  JOURNAL   Elife 13, 97267 (2024)
   PUBMED   39235443
  REMARK    GeneRIF: Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Chen,L., Huang,D., Huang,Z., Liu,X., He,M., Luo,M., Tang,Z.,
            Tan,G., Guo,Q. and Xiong,H.
  TITLE     Decreased HMGCS1 inhibits proliferation and inflammatory response
            of keratinocytes and ameliorates imiquimod-induced psoriasis via
            the STAT3/IL-23 axis
  JOURNAL   Int Immunopharmacol 133, 112033 (2024)
   PUBMED   38608446
  REMARK    GeneRIF: Decreased HMGCS1 inhibits proliferation and inflammatory
            response of keratinocytes and ameliorates imiquimod-induced
            psoriasis via the STAT3/IL-23 axis.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Zhou,R., Qiu,L., Zhou,L., Geng,R., Yang,S. and Wu,J.
  TITLE     P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression
  JOURNAL   Cell Signal 105, 110609 (2023)
   PUBMED   36702290
  REMARK    GeneRIF: P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Shi,S.J., Han,D.H., Zhang,J.L., Li,Y., Yang,A.G. and Zhang,R.
  TITLE     VIM-AS1 promotes proliferation and drives enzalutamide resistance
            in prostate cancer via IGF2BP2-mediated HMGCS1 mRNA stabilization
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36734275
  REMARK    GeneRIF: VIMAS1 promotes proliferation and drives enzalutamide
            resistance in prostate cancer via IGF2BP2mediated HMGCS1 mRNA
            stabilization.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Russ,A.P., Ruzicka,V., Maerz,W., Appelhans,H. and Gross,W.
  TITLE     Amplification and direct sequencing of a cDNA encoding human
            cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochim Biophys Acta 1132 (3), 329-331 (1992)
   PUBMED   1358203
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Gil,G., Smith,J.R., Goldstein,J.L. and Brown,M.S.
  TITLE     Optional exon in the 5'-untranslated region of
            3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved
            sequence and splicing pattern in humans and hamsters
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1863-1866 (1987)
   PUBMED   3470763
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Mehrabian,M., Callaway,K.A., Clarke,C.F., Tanaka,R.D.,
            Greenspan,M., Lusis,A.J., Sparkes,R.S., Mohandas,T., Edmond,J.,
            Fogelman,A.M. et al.
  TITLE     Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A
            synthase and the chromosomal localization of the human gene
  JOURNAL   J Biol Chem 261 (34), 16249-16255 (1986)
   PUBMED   2877984
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Leonard,S., Arbogast,D., Geyer,D., Jones,C. and Sinensky,M.
  TITLE     Localization of the gene encoding
            3-hydroxy-3-methylglutaryl-coenzyme A synthase to human chromosome
            5
  JOURNAL   Proc Natl Acad Sci U S A 83 (7), 2187-2189 (1986)
   PUBMED   2870496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK315593.1 and AC114947.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.216745.1,
                                           SRR1803615.11048.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325110.11/ ENSP00000322706.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..520
                     /product="hydroxymethylglutaryl-CoA synthase, cytoplasmic
                     isoform 1"
                     /EC_number="2.3.3.10"
                     /note="3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
                     synthase; 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1
                     (soluble); hydroxymethylglutaryl-CoA synthase,
                     cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA synthase 1
                     (soluble)"
                     /calculated_mol_wt=57163
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          13..469
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     Site            46
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          492..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01581.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     CDS             1..520
                     /gene="HMGCS1"
                     /gene_synonym="HMGCS"
                     /coded_by="NM_001098272.3:127..1689"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34154.1"
                     /db_xref="GeneID:3157"
                     /db_xref="HGNC:HGNC:5007"
                     /db_xref="MIM:142940"
ORIGIN      
        1 mpgslplnae acwpkdvgiv aleiyfpsqy vdqaelekyd gvdagkytig lgqakmgfct
       61 dredinslcm tvvqnlmern nlsydcigrl evgtetiidk sksvktnlmq lfeesgntdi
      121 egidttnacy ggtaavfnav nwiessswdg ryalvvagdi avyatgnarp tggvgavall
      181 igpnaplife rglrgthmqh aydfykpdml seypivdgkl siqcylsald rcysvyckki
      241 haqwqkegnd kdftlndfgf mifhspyckl vqkslarmll ndflndqnrd knsiysglea
      301 fgdvkledty fdrdvekafm kasselfsqk tkasllvsnq ngnmytssvy gslasvlaqy
      361 spqqlagkri gvfsygsgla atlyslkvtq datpgsaldk itaslcdlks rldsrtgvap
      421 dvfaenmklr edthhlvnyi pqgsidslfe gtwylvrvde khrrtyarrp tpnddtldeg
      481 vglvhsniat ehipspakkv prlpataaep eaavisngeh
//
LOCUS       NP_065947                879 aa            linear   PRI 27-APR-2025
DEFINITION  oxysterol-binding protein-related protein 5 isoform a [Homo
            sapiens].
ACCESSION   NP_065947
VERSION     NP_065947.1
DBSOURCE    REFSEQ: accession NM_020896.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 879)
  AUTHORS   Wu,Y., Min,L., Zhang,P., Zhang,L., Xu,Y., Li,D., Zheng,M., Pei,D.
            and Wang,Q.
  TITLE     ORP5 promotes migration and invasion of cervical cancer cells by
            inhibiting endoplasmic reticulum stress
  JOURNAL   Cell Stress Chaperones 28 (4), 395-407 (2023)
   PUBMED   37314629
  REMARK    GeneRIF: ORP5 promotes migration and invasion of cervical cancer
            cells by inhibiting endoplasmic reticulum stress.
REFERENCE   2  (residues 1 to 879)
  AUTHORS   Santos,N.C., Girik,V. and Nunes-Hasler,P.
  TITLE     ORP5 and ORP8: Sterol Sensors and Phospholipid Transfer Proteins at
            Membrane Contact Sites?
  JOURNAL   Biomolecules 10 (6), 928 (2020)
   PUBMED   32570981
  REMARK    GeneRIF: ORP5 and ORP8: Sterol Sensors and Phospholipid Transfer
            Proteins at Membrane Contact Sites?
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 879)
  AUTHORS   Sandhu,J., Li,S., Fairall,L., Pfisterer,S.G., Gurnett,J.E.,
            Xiao,X., Weston,T.A., Vashi,D., Ferrari,A., Orozco,J.L.,
            Hartman,C.L., Strugatsky,D., Lee,S.D., He,C., Hong,C., Jiang,H.,
            Bentolila,L.A., Gatta,A.T., Levine,T.P., Ferng,A., Lee,R.,
            Ford,D.A., Young,S.G., Ikonen,E., Schwabe,J.W.R. and Tontonoz,P.
  TITLE     Aster Proteins Facilitate Nonvesicular Plasma Membrane to ER
            Cholesterol Transport in Mammalian Cells
  JOURNAL   Cell 175 (2), 514-529 (2018)
   PUBMED   30220461
REFERENCE   4  (residues 1 to 879)
  AUTHORS   Pulli,I., Lassila,T., Pan,G., Yan,D., Olkkonen,V.M. and
            Tornquist,K.
  TITLE     Oxysterol-binding protein related-proteins (ORPs) 5 and 8 regulate
            calcium signaling at specific cell compartments
  JOURNAL   Cell Calcium 72, 62-69 (2018)
   PUBMED   29748134
  REMARK    GeneRIF: ORP5/8 regulate Ca(2+) signaling at specific membrane
            contact sites foci.
REFERENCE   5  (residues 1 to 879)
  AUTHORS   Sohn,M., Korzeniowski,M., Zewe,J.P., Wills,R.C., Hammond,G.R.V.,
            Humpolickova,J., Vrzal,L., Chalupska,D., Veverka,V., Fairn,G.D.,
            Boura,E. and Balla,T.
  TITLE     PI(4,5)P2 controls plasma membrane PI4P and PS levels via ORP5/8
            recruitment to ER-PM contact sites
  JOURNAL   J Cell Biol 217 (5), 1797-1813 (2018)
   PUBMED   29472386
  REMARK    GeneRIF: ORP5/8 recruitment to the plasma membrane occurs through
            interactions with the N-terminal Pleckstrin homology domains and
            adjacent basic residues of ORP5/8 with both phosphatidylinositol
            4-phosphate and Phosphatidylinositol 4,5-bisphosphate.
REFERENCE   6  (residues 1 to 879)
  AUTHORS   Ma,J., Dempsey,A.A., Stamatiou,D., Marshall,K.W. and Liew,C.C.
  TITLE     Identifying leukocyte gene expression patterns associated with
            plasma lipid levels in human subjects
  JOURNAL   Atherosclerosis 191 (1), 63-72 (2007)
   PUBMED   16806233
REFERENCE   7  (residues 1 to 879)
  AUTHORS   Higashimoto,K., Soejima,H., Yatsuki,H., Joh,K., Uchiyama,M.,
            Obata,Y., Ono,R., Wang,Y., Xin,Z., Zhu,X., Masuko,S., Ishino,F.,
            Hatada,I., Jinno,Y., Iwasaka,T., Katsuki,T. and Mukai,T.
  TITLE     Characterization and imprinting status of OBPH1/Obph1 gene:
            implications for an extended imprinting domain in human and mouse
  JOURNAL   Genomics 80 (6), 575-584 (2002)
   PUBMED   12504849
  REMARK    GeneRIF: OBPH1/Obph1 gene is imprinted, with preferential
            expression from the maternal allele in human and mouse.
REFERENCE   8  (residues 1 to 879)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   9  (residues 1 to 879)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
REFERENCE   10 (residues 1 to 879)
  AUTHORS   Laitinen,S., Olkkonen,V.M., Ehnholm,C. and Ikonen,E.
  TITLE     Family of human oxysterol binding protein (OSBP) homologues. A
            novel member implicated in brain sterol metabolism
  JOURNAL   J Lipid Res 40 (12), 2204-2211 (1999)
   PUBMED   10588946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC400863.1, BC039579.1,
            AC108448.12 and AL136918.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors
            that play a key role in the maintenance of cholesterol balance in
            the body. Most members contain an N-terminal pleckstrin homology
            domain and a highly conserved C-terminal OSBP-like sterol-binding
            domain. This gene has been shown to be imprinted, with preferential
            expression from the maternal allele only in placenta. Transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a). Isoform a has a pleckstrin homology domain and a
            sterol-binding domain.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056510.1, AB074006.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene         :: PMID: 12504849
            MANE Ensembl match     :: ENST00000263650.12/ ENSP00000263650.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..879
                     /product="oxysterol-binding protein-related protein 5
                     isoform a"
                     /note="oxysterol-binding protein-related protein 5;
                     OSBP-related protein 5; oxysterol-binding protein
                     homologue 1; ORP-5; oxysterol-binding protein homolog 1"
                     /calculated_mol_wt=98486
     Region          1..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0X9.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ER64; propagated from
                     UniProtKB/Swiss-Prot (Q9H0X9.1)"
     Region          120..248
                     /region_name="PH_OPR5_ORP8"
                     /note="Human Oxysterol binding protein related proteins 5
                     and 8 Pleckstrin homology (PH) domain; cd13286"
                     /db_xref="CDD:270103"
     Region          254..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0X9.1)"
     Region          374..717
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     Region          742..806
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0X9.1)"
     Site            747
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H0X9.1)"
     Site            860..878
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0X9.1)"
     CDS             1..879
                     /gene="OSBPL5"
                     /gene_synonym="OBPH1; ORP5"
                     /coded_by="NM_020896.4:117..2756"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31344.1"
                     /db_xref="GeneID:114879"
                     /db_xref="HGNC:HGNC:16392"
                     /db_xref="MIM:606733"
ORIGIN      
        1 mkeeaflrrr fslcppsstp qkvdprkltr nlllsgdnel yplspgkdme pngpslprde
       61 gpptpssatk vppaeyrlcn gsdkecvspt arvtkketlk aqkenyrqek kratrqllsa
      121 ltdpsvvima dslkirgtlk swtklwcvlk pgvlliyktp kvgqwvgtvl lhccelierp
      181 skkdgfcfkl fhpldqsvwa vkgpkgesvg sitqplpssy lifraasesd grcwldalel
      241 alrcssllrl gtckpgrdge pgtspdasps slcglpasat vhpdqdlfpl ngsslendaf
      301 sdkserenpe esdtetqdhs rktesgsdqs etpgapvrrg ttyveqvqee lgelgeasqv
      361 etvseenksl mwtllkqlrp gmdlsrvvlp tfvleprsfl nklsdyyyha dllsraavee
      421 daysrmklvl rwylsgfykk pkgikkpynp ilgetfrccw fhpqtdsrtf yiaeqvshhp
      481 pvsafhvsnr kdgfcisgsi taksrfygns lsalldgkat ltflnraedy tltmpyahck
      541 gilygtmtle lggkvtieca knnfqaqlef klkpffggst sinqisgkit sgeevlasls
      601 ghwdrdvfik eegsgssalf wtpsgevrrq rlrqhtvple eqteleserl wqhvtraisk
      661 gdqhratqek faleeaqrqr arerqeslmp wkpqlfhldp itqewhyrye dhspwdplkd
      721 iaqfeqdgil rtlqqeavar qttflgspgp rhersgpdqr lrkasdqpsg hsqatessgs
      781 tpescpelsd eeqdgdfvpg gespcprcrk earrlqalhe ailsireaqq elhrhlsaml
      841 sstaraaqap tpgllqsprs wfllcvflac qlfinhilk
//
LOCUS       NP_004273                211 aa            linear   PRI 27-APR-2025
DEFINITION  BAG family molecular chaperone regulator 2 [Homo sapiens].
ACCESSION   NP_004273
VERSION     NP_004273.1
DBSOURCE    REFSEQ: accession NM_004282.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Lauer,S.M., Omar,M.H., Golkowski,M.G., Kenerson,H.L., Lee,K.S.,
            Pascual,B.C., Lim,H.C., Forbush,K., Smith,F.D., Gordan,J.D.,
            Ong,S.E., Yeung,R.S. and Scott,J.D.
  TITLE     Recruitment of BAG2 to DNAJ-PKAc scaffolds promotes cell survival
            and resistance to drug-induced apoptosis in fibrolamellar carcinoma
  JOURNAL   Cell Rep 43 (2), 113678 (2024)
   PUBMED   38236773
  REMARK    GeneRIF: Recruitment of BAG2 to DNAJ-PKAc scaffolds promotes cell
            survival and resistance to drug-induced apoptosis in fibrolamellar
            carcinoma.
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Iglesias-Martinez,L.F., Rauch,N., Wynne,K., McCann,B., Kolch,W. and
            Rauch,J.
  TITLE     Interactome dynamics of RAF1-BRAF kinase monomers and dimers
  JOURNAL   Sci Data 10 (1), 203 (2023)
   PUBMED   37045861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Huang,X., Shi,D., Zou,X., Wu,X., Huang,S., Kong,L., Yang,M.,
            Xiao,Y., Chen,B., Chen,X., Ouyang,Y., Song,L., Jian,Y. and Lin,C.
  TITLE     BAG2 drives chemoresistance of breast cancer by exacerbating mutant
            p53 aggregate
  JOURNAL   Theranostics 13 (1), 339-354 (2023)
   PUBMED   36593950
  REMARK    GeneRIF: BAG2 drives chemoresistance of breast cancer by
            exacerbating mutant p53 aggregate.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Lima,R.S., Carrettiero,D.C. and Ferrari,M.F.R.
  TITLE     BAG2 prevents Tau hyperphosphorylation and increases p62/SQSTM1 in
            cell models of neurodegeneration
  JOURNAL   Mol Biol Rep 49 (8), 7623-7635 (2022)
   PUBMED   35612780
  REMARK    GeneRIF: BAG2 prevents Tau hyperphosphorylation and increases
            p62/SQSTM1 in cell models of neurodegeneration.
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Tu,R., Kang,W., Kang,Y., Chen,Z., Zhang,P., Xiong,X., Ma,J.,
            Du,R.L. and Zhang,C.
  TITLE     c-MYC-USP49-BAG2 axis promotes proliferation and chemoresistance of
            colorectal cancer cells in vitro
  JOURNAL   Biochem Biophys Res Commun 607, 117-123 (2022)
   PUBMED   35367823
  REMARK    GeneRIF: c-MYC-USP49-BAG2 axis promotes proliferation and
            chemoresistance of colorectal cancer cells in vitro.
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Dai,Q., Qian,S.B., Li,H.H., McDonough,H., Borchers,C., Huang,D.,
            Takayama,S., Younger,J.M., Ren,H.Y., Cyr,D.M. and Patterson,C.
  TITLE     Regulation of the cytoplasmic quality control protein degradation
            pathway by BAG2
  JOURNAL   J Biol Chem 280 (46), 38673-38681 (2005)
   PUBMED   16169850
  REMARK    GeneRIF: BAG2 binds to the carboxyl terminus of Hsp70-interacting
            protein (CHIP) and provides a cochaperone-dependent regulatory
            mechanism for preventing unregulated ubiquitylation of misfolded
            proteins by CHIP
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Ueda,K., Kosako,H., Fukui,Y. and Hattori,S.
  TITLE     Proteomic identification of Bcl2-associated athanogene 2 as a novel
            MAPK-activated protein kinase 2 substrate
  JOURNAL   J Biol Chem 279 (40), 41815-41821 (2004)
   PUBMED   15271996
  REMARK    GeneRIF: BAG2 was directly phosphorylated at serine 20 in vitro by
            MAPKAPK2 and MAPKAP2 is also required for phosphorylation of BAG2
            in vivo.
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Takayama,S., Xie,Z. and Reed,J.C.
  TITLE     An evolutionarily conserved family of Hsp70/Hsc70 molecular
            chaperone regulators
  JOURNAL   J Biol Chem 274 (2), 781-786 (1999)
   PUBMED   9873016
REFERENCE   10 (residues 1 to 211)
  AUTHORS   Halse,R., Rochford,J.J., McCormack,J.G., Vandenheede,J.R.,
            Hemmings,B.A. and Yeaman,S.J.
  TITLE     Control of glycogen synthesis in cultured human muscle cells
  JOURNAL   J Biol Chem 274 (2), 776-780 (1999)
   PUBMED   9873015
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA874388.1, AL136311.7,
            AL050287.1, CA442969.1 and AL031321.1.
            
            Summary: BAG proteins compete with Hip for binding to the
            Hsc70/Hsp70 ATPase domain and promote substrate release. All the
            BAG proteins have an approximately 45-amino acid BAG domain near
            the C terminus but differ markedly in their N-terminal regions. The
            predicted BAG2 protein contains 211 amino acids. The BAG domains of
            BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase
            domain in vitro and in mammalian cells. All 3 proteins bind with
            high affinity to the ATPase domain of Hsc70 and inhibit its
            chaperone activity in a Hip-repressible manner. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.250176.1,
                                           SRR1803617.34704.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370693.5/ ENSP00000359727.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.1"
     Protein         1..211
                     /product="BAG family molecular chaperone regulator 2"
                     /note="dJ417I1.2 (BAG-family molecular chaperone regulator
                     2); bcl-2-associated athanogene 2; BCL2 associated
                     athanogene 2"
                     /calculated_mol_wt=23641
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O95816.1)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O95816.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95816.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95816.1)"
     Region          109..189
                     /region_name="BAG"
                     /note="BAG domains, present in regulator of Hsp70
                     proteins; smart00264"
                     /db_xref="CDD:214591"
     CDS             1..211
                     /gene="BAG2"
                     /gene_synonym="BAG-2; dJ417I1.2"
                     /coded_by="NM_004282.4:373..1008"
                     /db_xref="CCDS:CCDS4961.1"
                     /db_xref="GeneID:9532"
                     /db_xref="HGNC:HGNC:938"
                     /db_xref="MIM:603882"
ORIGIN      
        1 maqakinaka negrfcrsss madrssrlle sldqlelrve alreaatave qekeillemi
       61 hsiqnsqdmr qisdgereel nltanrlmgr tltvevsvet irnpqqqesl khatriidev
      121 vnkflddlgn akshlmslys acssevphgp vdqkfqsivi gcaledqkki krrletllrn
      181 iensdkaikl lehskgagsk tlqqnaesrf n
//
LOCUS       NP_001007545             172 aa            linear   PRI 27-APR-2025
DEFINITION  regulator of hemoglobinization and erythroid cell expansion protein
            [Homo sapiens].
ACCESSION   NP_001007545 XP_496432
VERSION     NP_001007545.1
DBSOURCE    REFSEQ: accession NM_001007544.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Franke,K., Bal,G., Li,Z., Zuberbier,T. and Babina,M.
  TITLE     Clorfl86/RHEX Is a Negative Regulator of SCF/KIT Signaling in Human
            Skin Mast Cells
  JOURNAL   Cells 12 (9), 1306 (2023)
   PUBMED   37174705
  REMARK    GeneRIF: Clorfl86/RHEX Is a Negative Regulator of SCF/KIT Signaling
            in Human Skin Mast Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Verma,R., Su,S., McCrann,D.J., Green,J.M., Leu,K., Young,P.R.,
            Schatz,P.J., Silva,J.C., Stokes,M.P. and Wojchowski,D.M.
  TITLE     RHEX, a novel regulator of human erythroid progenitor cell
            expansion and erythroblast development
  JOURNAL   J Exp Med 211 (9), 1715-1722 (2014)
   PUBMED   25092874
  REMARK    GeneRIF: RHEX(C1orf186) comprises a new EPO/EPOR target and
            regulator of erythroid cell expansion that additionally acts to
            support late-stage erythroblast development
            Erratum:[J Exp Med. 2015 Jun 1;212(6):971. doi:
            10.1084/jem.2013062404242015c. PMID: 25941257]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC071785.1, AK122631.1 and AI683243.1.
            
            On Nov 29, 2004 this sequence version replaced XP_496432.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC071785.1, SRR5189667.201948.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331555.10/ ENSP00000356093.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..172
                     /product="regulator of hemoglobinization and erythroid
                     cell expansion protein"
                     /note="uncharacterized protein C1orf186; regulator of
                     human erythroid cell expansion protein"
                     /calculated_mol_wt=19274
     Region          7..172
                     /region_name="DUF4692"
                     /note="Regulator of human erythroid cell expansion (RHEX);
                     pfam15763"
                     /db_xref="CDD:434917"
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZWK4.1)"
     Region          52..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZWK4.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:25092874; propagated from
                     UniProtKB/Swiss-Prot (Q6ZWK4.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:25092874; propagated from
                     UniProtKB/Swiss-Prot (Q6ZWK4.1)"
     CDS             1..172
                     /gene="RHEX"
                     /gene_synonym="C1orf186"
                     /coded_by="NM_001007544.4:190..708"
                     /db_xref="CCDS:CCDS73014.1"
                     /db_xref="GeneID:440712"
                     /db_xref="HGNC:HGNC:25341"
                     /db_xref="MIM:616088"
ORIGIN      
        1 mltevmevwh glviavvslf lqacfltain yllsrhmahk seqilkaasl qvprpspghh
       61 hppavkemke tqterdipms dslyrhdsdt psdsldsscs sppacqated vdytqvvfsd
      121 pgelkndspl dyenikeitd yvnvnperhk psfwyfvnpa lsepaeydqv am
//
LOCUS       NP_001355605             213 aa            linear   ROD 27-APR-2025
DEFINITION  unconventional myosin-Ih isoform 2 [Mus musculus].
ACCESSION   NP_001355605
VERSION     NP_001355605.1
DBSOURCE    REFSEQ: accession NM_001368676.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Dumont,R.A., Zhao,Y.D., Holt,J.R., Bahler,M. and Gillespie,P.G.
  TITLE     Myosin-I isozymes in neonatal rodent auditory and vestibular
            epithelia
  JOURNAL   J Assoc Res Otolaryngol 3 (4), 375-389 (2002)
   PUBMED   12486594
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC127255.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144867.1, SRR17253014.3035241.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849384
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 55.99 cM"
     Protein         1..213
                     /product="unconventional myosin-Ih isoform 2"
                     /note="myosin-Ih; unconventional myosin-Ih"
                     /calculated_mol_wt=23879
     Region          25..206
                     /region_name="Myosin_TH1"
                     /note="Unconventional myosin tail, actin- and
                     lipid-binding; pfam06017"
                     /db_xref="CDD:461801"
     CDS             1..213
                     /gene="Myo1h"
                     /gene_synonym="4631401O15Rik"
                     /coded_by="NM_001368676.1:381..1022"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS89974.1"
                     /db_xref="GeneID:231646"
                     /db_xref="MGI:MGI:1914674"
ORIGIN      
        1 mctrnlvrky crgisaerka mmqqkvvtse ifrgkkegya eslnqlfags rldesninpk
       61 vlqllgseki qygvpvikyd rkgfkarqrq llltqrsayl velskvkqki eyaavrgvst
      121 sslsdgilvi hispadkqqk gdvilqcehi fevatklaml irkehtvrvv qgslqfyvsp
      181 gregtivfet geedqvykdk ngqlrvvsag kkt
//
LOCUS       NP_689568                693 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 441 [Homo sapiens].
ACCESSION   NP_689568
VERSION     NP_689568.2
DBSOURCE    REFSEQ: accession NM_152355.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB250168.1, AC008543.9 and BX649086.1.
            
            On Jun 27, 2008 this sequence version replaced NP_689568.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB250168.1, SRR1803617.39867.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357901.5/ ENSP00000350576.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..693
                     /product="zinc finger protein 441"
                     /calculated_mol_wt=80005
     Region          3..44
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          143..163
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          171..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          222..634
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          227..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(287,289,291,293..294,297..298,301,315,317,321..322,
                     325..326,329,343,345,347,349..350,353..354,357)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          395..413
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          421..441
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(426,428,430,432..433,436..437,440,454,456,460..461,
                     464..465,468,482,484,486,488..489,492..493,496)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          449..469
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          477..497
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          505..525
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(510,512,514,516..517,520..521,524,538,540,544..545,
                     548..549,552,566,568,570,572..573,576..577,580)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          533..553
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          561..581
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          589..609
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(594,596,598,600..601,604..605,608,622,624,628..629,
                     632..633,636,650,652,654,656..657,660..661,664)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          617..637
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          645..665
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          673..693
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..693
                     /gene="ZNF441"
                     /coded_by="NM_152355.3:195..2276"
                     /db_xref="CCDS:CCDS12266.2"
                     /db_xref="GeneID:126068"
                     /db_xref="HGNC:HGNC:20875"
ORIGIN      
        1 mdsvafedva inftceewal lgpsqkslyr dvmqetirnl dcigmiwqnh dieedqykdl
       61 rrnlrchmve raceikdnsq cggpftqtqd sivnekipgv dpwessectd vlmgrsslnc
      121 yvrvdsehkp ceyqeygekp ythtqcgtaf syqpcfqihe rpqhgkklyd ckecasfssl
      181 enlqrhmaah hgdgprickl cgnafiwpsl fhmlrrthte ekpyeyeqcs tafpaysstl
      241 rherthsgek pyqckqcgka fscscytqly erthtgeqsy eckqcgkafy hlgsfqrhmi
      301 vhtgdgphkc kicgkgflsp ssvrrhkrth tgekpyecky cgkafsdctg frrhmithtg
      361 dgphkckvcg kafdspslcr rhetthtgek pykcecgkaf sdfyyfrnhe tthtgekpyk
      421 ckqcgkafic ctylqiheri htgerpykck qcgkafrssn yirvhektht gekpyeckqc
      481 gkalshlksf qrhmimhtgd gphkckicgk sfdspssfrr herihtgerp ykcklcgkgf
      541 rsssyiqlhe rthtgekpyg cqqcgkalsd lssfrrhmit htgngphkck icgkgfdyps
      601 svqrhertht gekpyeckec gkafshssyl rihervhtge kpykckecgk pfhcpsafhk
      661 herthsmekp ykckecgeaf hcissfhkhe mth
//
LOCUS       NP_001348495             203 aa            linear   ROD 27-APR-2025
DEFINITION  ras-like protein family member 10B isoform 1 [Mus musculus].
ACCESSION   NP_001348495 XP_006533549
VERSION     NP_001348495.1
DBSOURCE    REFSEQ: accession NM_001361566.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Shigesawa,I., Nakamura,A., Yamauchi,Y., Kawata,S., Miyazaki,A.,
            Nomoto,H., Kameda,H., Terauchi,Y. and Atsumi,T.
  TITLE     Effects of glucokinase haploinsufficiency on the pancreatic
            beta-cell mass and function of long-term high-fat, high-sucrose
            diet-fed mice
  JOURNAL   J Diabetes Investig 15 (12), 1732-1742 (2024)
   PUBMED   39305123
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Rybkin,I.I., Kim,M.S., Bezprozvannaya,S., Qi,X., Richardson,J.A.,
            Plato,C.F., Hill,J.A., Bassel-Duby,R. and Olson,E.N.
  TITLE     Regulation of atrial natriuretic peptide secretion by a novel
            Ras-like protein
  JOURNAL   J Cell Biol 179 (3), 527-537 (2007)
   PUBMED   17984325
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY277818.1, BC116407.2, AK045997.1, AK158941.1 and AW456843.1.
            
            On Mar 29, 2018 this sequence version replaced XP_006533549.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.1854392.1,
                                           SRR7974084.22835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849379
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 50.3 cM"
     Protein         1..203
                     /product="ras-like protein family member 10B isoform 1"
                     /EC_number="3.6.5.2"
                     /note="ras-like protein family member 10B"
                     /calculated_mol_wt=23098
     Region          1..203
                     /region_name="Small GTPase-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
     mat_peptide     1..200
                     /product="Ras-like protein family member 10B.
                     /id=PRO_0000280801"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
                     /calculated_mol_wt=22914
     Region          5..203
                     /region_name="RRP22"
                     /note="Ras-related protein on chromosome 22 (RRP22)
                     family; cd04142"
                     /db_xref="CDD:133342"
     Site            11..18
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133342"
     Site            order(12..13,61..62)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133342"
     Site            order(13..19,59,62,128..129,131,159..160)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133342"
     Site            order(18..19,33,35,42..43,56..57,59,61..62,161)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133342"
     Region          33..42
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
     Site            order(34..35,40..43)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133342"
     Site            order(34..38,40..42)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133342"
     Site            36
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133342"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133342"
     Site            order(61..62,72..77,84..87)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133342"
     Site            128..131
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133342"
     Site            159..161
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133342"
     Site            200..203
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:133342"
     Site            200
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
     CDS             1..203
                     /gene="Rasl10b"
                     /gene_synonym="B230331P10Rik; Gm729; VTS58635"
                     /coded_by="NM_001361566.1:381..992"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS25163.1"
                     /db_xref="GeneID:276952"
                     /db_xref="MGI:MGI:2685575"
ORIGIN      
        1 mvstyrvavl gargvgksai vrqflynefs evcvptttrr lylpavvmng hvhdlqildf
       61 ppisafpvnt lqewadaccr glrsvhayil vydiccfdsf eyvktirqqi letrvigtse
      121 tpiiivgnkr dlqrgrvipr wnvshlvrkt wkcgyvecsa kynwhilllf sellksvgca
      181 rckhvhaalr fqgalrrnrc aim
//
LOCUS       NP_003625                284 aa            linear   PRI 27-APR-2025
DEFINITION  protein NipSnap homolog 1 isoform 1 [Homo sapiens].
ACCESSION   NP_003625
VERSION     NP_003625.2
DBSOURCE    REFSEQ: accession NM_003634.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Pei,H., Dai,Y., Yu,Y., Tang,J., Cao,Z., Zhang,Y., Li,B., Nie,J.,
            Hei,T.K. and Zhou,G.
  TITLE     The Tumorigenic Effect of lncRNA AFAP1-AS1 is Mediated by
            Translated Peptide ATMLP Under the Control of m6 A Methylation
  JOURNAL   Adv Sci (Weinh) 10 (13), e2300314 (2023)
   PUBMED   36871154
  REMARK    GeneRIF: The Tumorigenic Effect of lncRNA AFAP1-AS1 is Mediated by
            Translated Peptide ATMLP Under the Control of m[6] A Methylation.
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Princely Abudu,Y., Pankiv,S., Mathai,B.J., Hakon Lystad,A.,
            Bindesboll,C., Brenne,H.B., Yoke Wui Ng,M., Thiede,B., Yamamoto,A.,
            Mutugi Nthiga,T., Lamark,T., Esguerra,C.V., Johansen,T. and
            Simonsen,A.
  TITLE     NIPSNAP1 and NIPSNAP2 Act as 'Eat Me' Signals for Mitophagy
  JOURNAL   Dev Cell 49 (4), 509-525 (2019)
   PUBMED   30982665
  REMARK    GeneRIF: NIPSNAP1 and NIPSNAP2 have a redundant function in
            mitophagy and are predominantly expressed in different tissues.
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Okuda-Ashitaka,E., Minami,T., Tsubouchi,S., Kiyonari,H.,
            Iwamatsu,A., Noda,T., Handa,H. and Ito,S.
  TITLE     Identification of NIPSNAP1 as a nocistatin-interacting protein
            involving pain transmission
  JOURNAL   J Biol Chem 287 (13), 10403-10413 (2012)
   PUBMED   22311985
  REMARK    GeneRIF: NIPSNAP1 is an interacting molecule of NST and plays a
            crucial role in pain transmission.
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Schoeber,J.P., Topala,C.N., Lee,K.P., Lambers,T.T., Ricard,G., van
            der Kemp,A.W., Huynen,M.A., Hoenderop,J.G. and Bindels,R.J.
  TITLE     Identification of Nipsnap1 as a novel auxiliary protein inhibiting
            TRPV6 activity
  JOURNAL   Pflugers Arch 457 (1), 91-101 (2008)
   PUBMED   18392847
  REMARK    GeneRIF: This study presents the first physiological function of
            mouse Nipsnap1 as an associated protein inhibiting transient
            receptor potential vanilloid channel 6 activity that possibly
            exerts its effect directly at the plasma membrane.
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Satoh,K., Takeuchi,M., Oda,Y., Deguchi-Tawarada,M., Sakamoto,Y.,
            Matsubara,K., Nagasu,T. and Takai,Y.
  TITLE     Identification of activity-regulated proteins in the postsynaptic
            density fraction
  JOURNAL   Genes Cells 7 (2), 187-197 (2002)
   PUBMED   11895482
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Seroussi,E., Pan,H.Q., Kedra,D., Roe,B.A. and Dumanski,J.P.
  TITLE     Characterization of the human NIPSNAP1 gene from 22q12: a member of
            a novel gene family
  JOURNAL   Gene 212 (1), 13-20 (1998)
   PUBMED   9661659
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and BC006473.1.
            
            On Jun 29, 2008 this sequence version replaced NP_003625.1.
            
            Summary: This gene encodes a member of the NipSnap family of
            proteins that may be involved in vesicular transport. A similar
            protein in mice inhibits the calcium channel TRPV6, and is also
            localized to the inner mitochondrial membrane where it may play a
            role in mitochondrial DNA maintenance. A pseudogene of this gene is
            located on the short arm of chromosome 17. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Feb 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC002371.2, SRR1803611.228575.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216121.12/ ENSP00000216121.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..284
                     /product="protein NipSnap homolog 1 isoform 1"
                     /note="4-nitrophenylphosphatase domain and non-neuronal
                     SNAP25-like 1; protein NipSnap homolog 1"
                     /calculated_mol_wt=33179
     Region          2..15
                     /region_name="SIFI-degron.
                     /evidence=ECO:0000269|PubMed:38297121"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPW8.1)"
     Site            65
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O55125; propagated from
                     UniProtKB/Swiss-Prot (Q9BPW8.1)"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O55125; propagated from
                     UniProtKB/Swiss-Prot (Q9BPW8.1)"
     Site            73
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O55125; propagated from
                     UniProtKB/Swiss-Prot (Q9BPW8.1)"
     Site            80
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O55125; propagated from
                     UniProtKB/Swiss-Prot (Q9BPW8.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BPW8.1)"
     Site            143
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O55125; propagated from
                     UniProtKB/Swiss-Prot (Q9BPW8.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BPW8.1)"
     Region          185..282
                     /region_name="NIPSNAP"
                     /note="pfam07978"
                     /db_xref="CDD:429767"
     Site            191
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O55125; propagated from
                     UniProtKB/Swiss-Prot (Q9BPW8.1)"
     Site            193
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O55125; propagated from
                     UniProtKB/Swiss-Prot (Q9BPW8.1)"
     Site            279
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O55125; propagated from
                     UniProtKB/Swiss-Prot (Q9BPW8.1)"
     CDS             1..284
                     /gene="NIPSNAP1"
                     /coded_by="NM_003634.4:32..886"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13860.1"
                     /db_xref="GeneID:8508"
                     /db_xref="HGNC:HGNC:7827"
                     /db_xref="MIM:603249"
ORIGIN      
        1 maprlcsisv tarrllggpg pragdvasaa aarfyskdne gswfrslfvh kvdprkdahs
       61 tllskketsn lykiqfhnvk peyldaynsl teavlpklhl dedypcslvg nwntwygeqd
      121 qavhlwrfsg gypalmdcmn klknnkeyle frrersqmll srrnqlllef sfwnepqprm
      181 gpniyelrty klkpgtmiew gnnwaraiky rqenqeavgg ffsqigelyv vhhlwaykdl
      241 qsreetrnaa wrkrgwdenv yytvplvrhm esrimiplki splq
//
LOCUS       NP_001351482             381 aa            linear   ROD 27-APR-2025
DEFINITION  ELMO domain-containing protein 3 [Mus musculus].
ACCESSION   NP_001351482 XP_006506022
VERSION     NP_001351482.1
DBSOURCE    REFSEQ: accession NM_001364553.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Turn,R.E., Hu,Y., Dewees,S.I., Devi,N., East,M.P., Hardin,K.R.,
            Khatib,T., Linnert,J., Wolfrum,U., Lim,M.J., Casanova,J.E.,
            Caspary,T. and Kahn,R.A.
  TITLE     The ARF GAPs ELMOD1 and ELMOD3 act at the Golgi and cilia to
            regulate ciliogenesis and ciliary protein traffic
  JOURNAL   Mol Biol Cell 33 (2), ar13 (2022)
   PUBMED   34818063
  REMARK    GeneRIF: The ARF GAPs ELMOD1 and ELMOD3 act at the Golgi and cilia
            to regulate ciliogenesis and ciliary protein traffic.
            Erratum:[Mol Biol Cell. 2022 Jun 1;33(7):cor1. doi:
            10.1091/mbc.E21-09-0443_corr. PMID: 35612986]
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Li,W., Feng,Y., Chen,A., Li,T., Huang,S., Liu,J., Liu,X., Liu,Y.,
            Gao,J., Yan,D., Sun,J., Mei,L., Liu,X. and Ling,J.
  TITLE     Elmod3 knockout leads to progressive hearing loss and abnormalities
            in cochlear hair cell stereocilia
  JOURNAL   Hum Mol Genet 28 (24), 4103-4112 (2019)
   PUBMED   31628468
  REMARK    GeneRIF: Finding associates Elmod3 deficiencies with stereocilia
            dysmorphologies and reveals that they might play roles in the actin
            cytoskeleton dynamics in cochlear hair cells, and thus relate to
            hearing impairment.
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Gineste,C., De Winter,J.M., Kohl,C., Witt,C.C., Giannesini,B.,
            Brohm,K., Le Fur,Y., Gretz,N., Vilmen,C., Pecchi,E., Jubeau,M.,
            Cozzone,P.J., Stienen,G.J., Granzier,H., Labeit,S.,
            Ottenheijm,C.A., Bendahan,D. and Gondin,J.
  TITLE     In vivo and in vitro investigations of heterozygous nebulin
            knock-out mice disclose a mild skeletal muscle phenotype
  JOURNAL   Neuromuscul Disord 23 (4), 357-369 (2013)
   PUBMED   23375831
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Sevajol,M., Reiser,J.B., Chouquet,A., Perard,J., Ayala,I., Gans,P.,
            Kleman,J.P. and Housset,D.
  TITLE     The C-terminal polyproline-containing region of ELMO contributes to
            an increase in the life-time of the ELMO-DOCK complex
  JOURNAL   Biochimie 94 (3), 823-828 (2012)
   PUBMED   22177965
  REMARK    GeneRIF: The data demonstrate the ability of the SH3 domain of
            DOCK180 to interact with ELMO1, regardless of the presence of the
            polyproline-containing C-terminal end.
REFERENCE   7  (residues 1 to 381)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125039.4, AK049155.1, AK084010.1 and BE944793.1.
            
            On Jun 22, 2018 this sequence version replaced XP_006506022.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.200474.1,
                                           SRR13422597.642579.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 32.27 cM"
     Protein         1..381
                     /product="ELMO domain-containing protein 3"
                     /note="RNA binding motif and ELMO domain 1; RNA-binding
                     motif and ELMO domain-containing protein 1"
                     /calculated_mol_wt=42528
     Region          154..313
                     /region_name="ELMO_CED12"
                     /note="ELMO/CED-12 family; pfam04727"
                     /db_xref="CDD:461411"
     CDS             1..381
                     /gene="Elmod3"
                     /gene_synonym="C330008I15Rik; Rbed1; RBM29"
                     /coded_by="NM_001364553.1:373..1518"
                     /db_xref="CCDS:CCDS20243.1"
                     /db_xref="GeneID:232089"
                     /db_xref="MGI:MGI:2445168"
ORIGIN      
        1 msetscsffi ekefqdgqle nvsaglsssy kdkgalmafr gipiseltnh gilqaltaet
       61 ngwqpgvvse evlraqeewe vvdtihpdie sgvhcqqpgq lisfnealeh fqsvdlssfk
      121 kriqptiqrt glaalrhclf gppklhqglr eerdlvltia qcgldsqnpt hgrvlqtiyk
      181 kltgskfdca lhgdhwedlg fqganpatdl rgagflallh llylvmdskt flmaqeifrl
      241 shhhiqqfpf clmsvnitri aiqalreecl srecnrrqkv ipvvnsfyaa tflhlarvwr
      301 tqqktildsg fvlkdleala kkspkrllkt lddylaqvsk gqtslleahk rpgsqgphsr
      361 dltftgvcdl qshsfesagl i
//
LOCUS       NP_001356014             394 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001356014 XP_024303798
VERSION     NP_001356014.1
DBSOURCE    REFSEQ: accession NM_001369085.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            On Mar 18, 2019 this sequence version replaced XP_024303798.1.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.115802.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..394
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 3"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=44482
     Region          81..146
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(90,92..94,96..100,103..104,107..108,113..116)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          155..343
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..394
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369085.1:282..1466"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mmkypgtwpc qgiigisfge svmevlrpql iridgrnyrk npvqeqtyqh eedeedfyqg
       61 smecadepcd ayeveqtpqg frstlrapsl lykhivgkrg dtrkkiemet ktsisipkpg
      121 qdgeivitgq hrngvisart ridvlldtfr rkqpfthfla fflnevevqe gflrfqeevl
      181 akcsmdhgvd ssifqnpkkl hltigmlvll seeeiqqtce mlqqckeefi ndisggkple
      241 vemagieymn ddpgmvdvly akvhmkdgsn rlqelvdrvl erfqasgliv kewnsvklha
      301 tvmntlfrkd pnaegrynly taegkyifke resfdgrnil ksfallprle yndaisahcn
      361 lclpgssdsp asasqvagit gvsdaysqsl pgks
//
LOCUS       NP_004177                785 aa            linear   PRI 27-APR-2025
DEFINITION  semaphorin-3F isoform 1 precursor [Homo sapiens].
ACCESSION   NP_004177
VERSION     NP_004177.3
DBSOURCE    REFSEQ: accession NM_004186.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Moragas,N., Fernandez-Nogueira,P., Recalde-Percaz,L., Inman,J.L.,
            Lopez-Plana,A., Bergholtz,H., Noguera-Castells,A., Del Burgo,P.J.,
            Chen,X., Sorlie,T., Gascon,P., Bragado,P., Bissell,M., Carbo,N. and
            Fuster,G.
  TITLE     The SEMA3F-NRP1/NRP2 axis is a key factor in the acquisition of
            invasive traits in in situ breast ductal carcinoma
  JOURNAL   Breast Cancer Res 26 (1), 122 (2024)
   PUBMED   39138514
  REMARK    GeneRIF: The SEMA3F-NRP1/NRP2 axis is a key factor in the
            acquisition of invasive traits in in situ breast ductal carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Li,Q., Ma,N., Li,X., Yang,C., Zhang,W., Xiong,J., Zhu,L., Li,J.,
            Wen,Q., Gao,L., Yang,C., Rao,L., Gao,L., Zhang,X. and Rao,J.
  TITLE     Reverse effect of Semaphorin-3F on rituximab resistance in diffuse
            large B-cell lymphoma via the Hippo pathway
  JOURNAL   Chin Med J (Engl) 136 (12), 1448-1458 (2023)
   PUBMED   37114652
  REMARK    GeneRIF: Reverse effect of Semaphorin-3F on rituximab resistance in
            diffuse large B-cell lymphoma via the Hippo pathway.
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Duncan,B.W., Mohan,V., Wade,S.D., Truong,Y., Kampov-Polevoi,A.,
            Temple,B.R. and Maness,P.F.
  TITLE     Semaphorin3F Drives Dendritic Spine Pruning Through Rho-GTPase
            Signaling
  JOURNAL   Mol Neurobiol 58 (8), 3817-3834 (2021)
   PUBMED   33856648
  REMARK    GeneRIF: Semaphorin3F Drives Dendritic Spine Pruning Through
            Rho-GTPase Signaling.
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Halabi,R., Watterston,C., Hehr,C.L., Mori-Kreiner,R., Childs,S.J.
            and McFarlane,S.
  TITLE     Semaphorin 3fa Controls Ocular Vascularization From the Embryo
            Through to the Adult
  JOURNAL   Invest Ophthalmol Vis Sci 62 (2), 21 (2021)
   PUBMED   33595613
  REMARK    GeneRIF: Semaphorin 3fa Controls Ocular Vascularization From the
            Embryo Through to the Adult.
REFERENCE   5  (residues 1 to 785)
  AUTHORS   Xie,Z., Li,T., Huang,B., Liu,S., Zhang,L. and Zhang,Q.
  TITLE     Semaphorin 3F Serves as a Tumor Suppressor in Esophageal Squamous
            Cell Carcinoma and is Associated With Lymph Node Metastasis in
            Disease Progression
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928117 (2020)
   PUBMED   32441221
  REMARK    GeneRIF: Semaphorin 3F Serves as a Tumor Suppressor in Esophageal
            Squamous Cell Carcinoma and is Associated With Lymph Node
            Metastasis in Disease Progression.
REFERENCE   6  (residues 1 to 785)
  AUTHORS   Sekido,Y., Bader,S., Latif,F., Chen,J.Y., Duh,F.M., Wei,M.H.,
            Albanesi,J.P., Lee,C.C., Lerman,M.I. and Minna,J.D.
  TITLE     Human semaphorins A(V) and IV reside in the 3p21.3 small cell lung
            cancer deletion region and demonstrate distinct expression patterns
  JOURNAL   Proc Natl Acad Sci U S A 93 (9), 4120-4125 (1996)
   PUBMED   8633026
REFERENCE   7  (residues 1 to 785)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   8  (residues 1 to 785)
  AUTHORS   Goshima,Y., Nakamura,F., Strittmatter,P. and Strittmatter,S.M.
  TITLE     Collapsin-induced growth cone collapse mediated by an intracellular
            protein related to UNC-33
  JOURNAL   Nature 376 (6540), 509-514 (1995)
   PUBMED   7637782
REFERENCE   9  (residues 1 to 785)
  AUTHORS   Kolodkin,A.L., Matthes,D.J. and Goodman,C.S.
  TITLE     The semaphorin genes encode a family of transmembrane and secreted
            growth cone guidance molecules
  JOURNAL   Cell 75 (7), 1389-1399 (1993)
   PUBMED   8269517
REFERENCE   10 (residues 1 to 785)
  AUTHORS   Luo,Y., Raible,D. and Raper,J.A.
  TITLE     Collapsin: a protein in brain that induces the collapse and
            paralysis of neuronal growth cones
  JOURNAL   Cell 75 (2), 217-227 (1993)
   PUBMED   8402908
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104450.2, BF058597.1,
            BC042914.1, AA378582.1 and CB240860.1.
            
            On May 16, 2008 this sequence version replaced NP_004177.2.
            
            Summary: This gene encodes a member of the semaphorin III family of
            secreted signaling proteins that are involved in axon guidance
            during neuronal development. The encoded protein contains an
            N-terminal Sema domain, an immunoglobulin loop and a C-terminal
            basic domain. This gene is expressed by the endothelial cells where
            it was found to act in an autocrine fashion to induce apoptosis,
            inhibit cell proliferation and survival, and function as an
            anti-tumorigenic agent. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042914.1, U33920.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000002829.8/ ENSP00000002829.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..785
                     /product="semaphorin-3F isoform 1 precursor"
                     /note="sema domain, immunoglobulin domain (Ig), short
                     basic domain, secreted, 3F; semaphorin III/F; semaphorin
                     IV; sema domain, immunoglobulin domain (Ig), short basic
                     domain, secreted, (semaphorin) 3F"
                     /calculated_mol_wt=86488
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1912
     mat_peptide     19..785
                     /product="Semaphorin-3F. /id=PRO_0000032320"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13275.2)"
                     /calculated_mol_wt=86488
     Region          48..548
                     /region_name="Sema_3F"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 3F (Sema3F); cd11254"
                     /db_xref="CDD:200515"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13275.2)"
     Site            order(105..108,198..199,203,224,226..227,234,244,247..248,
                     250,255,284,307..311,313,429,433,436)
                     /site_type="other"
                     /note="putative plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200515"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13275.2)"
     Site            order(285..287,290..292,326,329..330,332,334,338,361..368,
                     394..397,442,457)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200515"
     Region          547..584
                     /region_name="PSI"
                     /note="domain found in Plexins, Semaphorins and Integrins;
                     smart00423"
                     /db_xref="CDD:214655"
     Region          608..697
                     /region_name="Ig_Sema3"
                     /note="Immunoglobulin (Ig)-like domain of class III
                     semaphorin Sema3; cd05871"
                     /db_xref="CDD:409455"
     Region          608..614
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409455"
     Region          619..627
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409455"
     Site            order(621,666)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409455"
     Region          633..639
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409455"
     Region          641..644
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409455"
     Region          654..658
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409455"
     Region          661..668
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409455"
     Region          674..683
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409455"
     Region          686..697
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409455"
     Region          752..785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13275.2)"
     CDS             1..785
                     /gene="SEMA3F"
                     /gene_synonym="SEMA-IV; SEMA4; SEMAK"
                     /coded_by="NM_004186.5:290..2647"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2811.1"
                     /db_xref="GeneID:6405"
                     /db_xref="HGNC:HGNC:10728"
                     /db_xref="MIM:601124"
ORIGIN      
        1 mlvaglllwa slltgawpsf ptqdhlpatp rvrlsfkelk atgtahffnf llnttdyril
       61 lkdedhdrmy vgskdyvlsl dlhdinrepl iihwaaspqr ieecvlsgkd vngecgnfvr
      121 liqpwnrthl yvcgtgaynp mctyvnrgrr aqatpwtqtq avrgrgsrat dgalrpmpta
      181 prqdyifyle perlesgkgk cpydpkldta salineelya gvyidfmgtd aaifrtlgkq
      241 tamrtdqyns rwlndpsfih aelipdsaer nddklyfffr ersaeapqsp avyarigric
      301 lnddgghccl vnkwstflka rlvcsvpged giethfdelq dvfvqqtqdv rnpviyavft
      361 ssgsvfrgsa vcvysmadir mvfngpfahk egpnyqwmpf sgkmpyprpg tcpggtftps
      421 mkstkdypde vinfmrshpl myqavyplqr rplvvrtgap yrlttiavdq vdaadgryev
      481 lflgtdrgtv qkvivlpkdd qeleelmlee vevfkdpapv ktmtisskrq qlyvasavgv
      541 thlslhrcqa ygaacadccl ardpycawdg qacsrytass krrsrrqdvr hgnpirqcrg
      601 fnsnanknav esvqygvags aaflecqprs pqatvkwlfq rdpgdrrrei raedrflrte
      661 qglllralql sdrglyscta tennfkhvvt rvqlhvlgrd avhaalfppl smsappppga
      721 gpptppyqel aqllaqpevg lihqycqgyw rhvppsprea pgaprspepq dqkkprnrrh
      781 hppdt
//
LOCUS       NP_612400                376 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 183A isoform 1 [Homo sapiens].
ACCESSION   NP_612400
VERSION     NP_612400.3
DBSOURCE    REFSEQ: accession NM_138391.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Hubel,P., Urban,C., Bergant,V., Schneider,W.M., Knauer,B.,
            Stukalov,A., Scaturro,P., Mann,A., Brunotte,L., Hoffmann,H.H.,
            Schoggins,J.W., Schwemmle,M., Mann,M., Rice,C.M. and Pichlmair,A.
  TITLE     A protein-interaction network of interferon-stimulated genes
            extends the innate immune system landscape
  JOURNAL   Nat Immunol 20 (4), 493-502 (2019)
   PUBMED   30833792
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Davidsson,J., Andersson,A., Paulsson,K., Heidenblad,M.,
            Isaksson,M., Borg,A., Heldrup,J., Behrendtz,M., Panagopoulos,I.,
            Fioretos,T. and Johansson,B.
  TITLE     Tiling resolution array comparative genomic hybridization,
            expression and methylation analyses of dup(1q) in Burkitt lymphomas
            and pediatric high hyperdiploid acute lymphoblastic leukemias
            reveal clustered near-centromeric breakpoints and overexpression of
            genes in 1q22-32.3
  JOURNAL   Hum Mol Genet 16 (18), 2215-2225 (2007)
   PUBMED   17613536
  REMARK    GeneRIF: B4GALT3, DAP3, RGS16, TMEM183A and UCK2--were
            significantly overexpressed in dup(1q)-positive ALLs compared with
            high hyperdiploid ALLs without dup(1q).
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Yu,H., Jiang,H., Zhou,Q., Yang,J., Cun,Y., Su,B., Xiao,C. and
            Wang,W.
  TITLE     Origination and evolution of a human-specific transmembrane protein
            gene, c1orf37-dup
  JOURNAL   Hum Mol Genet 15 (11), 1870-1875 (2006)
   PUBMED   16644869
  REMARK    GeneRIF: c1orf37-dup encodes a novel transmembrane protein in
            humans which potentially endows new properties to cell surface
            interactions
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC364887.1, AK291426.1 and AC096632.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 5, 2006 this sequence version replaced NP_612400.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.19854.1,
                                           SRR1803617.140748.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367242.4/ ENSP00000356211.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..376
                     /product="transmembrane protein 183A isoform 1"
                     /calculated_mol_wt=42695
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXX5.2)"
     Region          100..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXX5.2)"
     Site            300..320
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXX5.2)"
     CDS             1..376
                     /gene="TMEM183A"
                     /gene_synonym="C1orf37"
                     /coded_by="NM_138391.6:93..1223"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1432.1"
                     /db_xref="GeneID:92703"
                     /db_xref="HGNC:HGNC:20173"
ORIGIN      
        1 margpgplgr prpdtvampk rgkrlkfrah dacsgrvtva dyansdpavv rsgrvkkava
       61 navqqevksl cgleasqvpa eealsgagep cdiidssdem daqeesiher tvsrkkkskr
      121 hkeeldgagg eeypmdiwll lasyirpedi vnfslickna wtvtctaafw trlyrrhytl
      181 daslplrlrp esmeklrclr acvirslyhm yepfaarisk npaipestps tlknskcllf
      241 wcrkivgnrq epmwefnfkf kkqsprlksk ctgglqppvq yedvhtnpdq dccllqvttl
      301 nfifipivmg miftlftinv stdmrhhrvr lvfqdspvhg grklrseqgv qvildpvhsv
      361 rlfdwwhpqy pfslra
//
LOCUS       NP_620175                106 aa            linear   PRI 27-APR-2025
DEFINITION  HIG1 domain family member 2A, mitochondrial [Homo sapiens].
ACCESSION   NP_620175
VERSION     NP_620175.1
DBSOURCE    REFSEQ: accession NM_138820.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Salazar,C., Barros,M., Elorza,A.A. and Ruiz,L.M.
  TITLE     Dynamic Distribution of HIG2A between the Mitochondria and the
            Nucleus in Response to Hypoxia and Oxidative Stress
  JOURNAL   Int J Mol Sci 23 (1), 389 (2021)
   PUBMED   35008815
  REMARK    GeneRIF: Dynamic Distribution of HIG2A between the Mitochondria and
            the Nucleus in Response to Hypoxia and Oxidative Stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Hock,D.H., Reljic,B., Ang,C.S., Muellner-Wong,L., Mountford,H.S.,
            Compton,A.G., Ryan,M.T., Thorburn,D.R. and Stroud,D.A.
  TITLE     HIGD2A is Required for Assembly of the COX3 Module of Human
            Mitochondrial Complex IV
  JOURNAL   Mol Cell Proteomics 19 (7), 1145-1160 (2020)
   PUBMED   32317297
  REMARK    GeneRIF: HIGD2A is Required for Assembly of the COX3 Module of
            Human Mitochondrial Complex IV.
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Salazar,C., Yanez,O., Elorza,A.A., Cortes,N., Garcia-Beltran,O.,
            Tiznado,W. and Ruiz,L.M.
  TITLE     Biosystem Analysis of the Hypoxia Inducible Domain Family Member
            2A: Implications in Cancer Biology
  JOURNAL   Genes (Basel) 11 (2), 206 (2020)
   PUBMED   32085461
  REMARK    GeneRIF: Biosystem Analysis of the Hypoxia Inducible Domain Family
            Member 2A: Implications in Cancer Biology.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Vukotic,M., Oeljeklaus,S., Wiese,S., Vogtle,F.N., Meisinger,C.,
            Meyer,H.E., Zieseniss,A., Katschinski,D.M., Jans,D.C., Jakobs,S.,
            Warscheid,B., Rehling,P. and Deckers,M.
  TITLE     Rcf1 mediates cytochrome oxidase assembly and respirasome
            formation, revealing heterogeneity of the enzyme complex
  JOURNAL   Cell Metab 15 (3), 336-347 (2012)
   PUBMED   22342701
REFERENCE   6  (residues 1 to 106)
  AUTHORS   An,H.J., Shin,H., Jo,S.G., Kim,Y.J., Lee,J.O., Paik,S.G. and Lee,H.
  TITLE     The survival effect of mitochondrial Higd-1a is associated with
            suppression of cytochrome C release and prevention of caspase
            activation
  JOURNAL   Biochim Biophys Acta 1813 (12), 2088-2098 (2011)
   PUBMED   21856340
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AW473735.1, BC007502.2 and
            BQ671009.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            cytochrome c oxidase complex (complex IV), which is the terminal
            enzyme in the mitochondrial respiratory chain. The encoded protein
            is an inner mitochondrial membrane protein and is a functional
            ortholog of the yeast respiratory supercomplex factor 1 (Rcf1). In
            mouse, the orthologous protein enhances cell survival under
            conditions of hypoxia. [provided by RefSeq, Sep 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.144105.1,
                                           SRR5189667.258213.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 22342701; reported by
                                                  MitoCarta
            MANE Ensembl match                 :: ENST00000274787.3/
                                                  ENSP00000274787.2
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..106
                     /product="HIG1 domain family member 2A, mitochondrial"
                     /note="HIG1 domain family, member 2A; RCF1 homolog B"
                     /calculated_mol_wt=11397
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9BW72.1)"
     Region          45..96
                     /region_name="HIG_1_N"
                     /note="Hypoxia induced protein conserved region;
                     pfam04588"
                     /db_xref="CDD:461361"
     Site            47..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BW72.1)"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BW72.1)"
     CDS             1..106
                     /gene="HIGD2A"
                     /gene_synonym="HIG2A; RCF1b"
                     /coded_by="NM_138820.4:70..390"
                     /db_xref="CCDS:CCDS4401.1"
                     /db_xref="GeneID:192286"
                     /db_xref="HGNC:HGNC:28311"
                     /db_xref="MIM:620788"
ORIGIN      
        1 matpgpvipe vpfepskppv ieglsptvyr npesfkekfv rktrenpvvp igclataaal
       61 tyglysfhrg nsqrsqlmmr triaaqgftv aaillglavt amksrp
//
LOCUS       NP_003426                427 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 134 [Homo sapiens].
ACCESSION   NP_003426 XP_005276731 XP_006726851 XP_011507178
VERSION     NP_003426.3
DBSOURCE    REFSEQ: accession NM_003435.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA098572.1, BC113410.1, BC042636.1 and AC003682.1.
            
            On or before Mar 22, 2015 this sequence version replaced
            XP_011507178.1, XP_006726851.1, XP_005276731.1, NP_003426.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.32972.1,
                                           SRR1803616.82301.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396161.10/ ENSP00000379464.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..427
                     /product="zinc finger protein 134"
                     /note="zinc finger protein 134 (clone pHZ-15)"
                     /calculated_mol_wt=48349
     Region          52..72
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(57,59,61,63..64,67..68,71,85,87..89,91..92,96)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          80..98
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          178..198
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(183,185,187,189..190,193..194,197,211,213,217..218,
                     221..222,225,239,241,243,245..246,249..250,253)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <202..358
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          206..226
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          234..254
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          262..282
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          290..310
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          318..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          346..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(351,353,355,357..358,361..362,365,379,381,385..386,
                     389..390,393,407,409,411,413..414,417..418,421)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          374..394
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          386..410
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          402..422
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..427
                     /gene="ZNF134"
                     /gene_synonym="pHZ-15"
                     /coded_by="NM_003435.5:320..1603"
                     /db_xref="CCDS:CCDS42638.1"
                     /db_xref="GeneID:7693"
                     /db_xref="HGNC:HGNC:12918"
                     /db_xref="MIM:604076"
ORIGIN      
        1 mtlvtaggaw tgpgcwhevk deessseqsi siavshvnts kaglpaqtal pcdicgpilk
       61 dilhldehqg thhglklhtc gacgrqfwfs anlhqyqkcy sieqplrrdk seasivknct
      121 vskephpsek pftckeeqkn fqatlggcqq kaihskrkth rstesgdafh geqmhykcse
      181 cgkafsrkdt lvqhqrihsg ekpyecsecg kafsrkatlv qhqrihtger pyecsecgkt
      241 fsrkdnltqh krihtgempy kcnecgkyfs hhsnlivhqr vhngarpykc sdcgkvfrhk
      301 stlvqhesih tgenpydcsd cgksfghkyt likhqrihte skpfeciecg kffsrssdyi
      361 ahqrvhtger pfvcskcgkd firtshlvrh qrvhtgerpy ecsecgkays lsshlnrhqk
      421 vhtagrl
//
LOCUS       NP_001353383             242 aa            linear   PRI 27-APR-2025
DEFINITION  rab GTPase-activating protein 1-like isoform O [Homo sapiens].
ACCESSION   NP_001353383 XP_016858488
VERSION     NP_001353383.1
DBSOURCE    REFSEQ: accession NM_001366454.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Anttila,V., Winsvold,B.S., Gormley,P., Kurth,T., Bettella,F.,
            McMahon,G., Kallela,M., Malik,R., de Vries,B., Terwindt,G.,
            Medland,S.E., Todt,U., McArdle,W.L., Quaye,L., Koiranen,M.,
            Ikram,M.A., Lehtimaki,T., Stam,A.H., Ligthart,L., Wedenoja,J.,
            Dunham,I., Neale,B.M., Palta,P., Hamalainen,E., Schurks,M.,
            Rose,L.M., Buring,J.E., Ridker,P.M., Steinberg,S., Stefansson,H.,
            Jakobsson,F., Lawlor,D.A., Evans,D.M., Ring,S.M., Farkkila,M.,
            Artto,V., Kaunisto,M.A., Freilinger,T., Schoenen,J., Frants,R.R.,
            Pelzer,N., Weller,C.M., Zielman,R., Heath,A.C., Madden,P.A.F.,
            Montgomery,G.W., Martin,N.G., Borck,G., Gobel,H., Heinze,A.,
            Heinze-Kuhn,K., Williams,F.M.K., Hartikainen,A.L., Pouta,A., van
            den Ende,J., Uitterlinden,A.G., Hofman,A., Amin,N., Hottenga,J.J.,
            Vink,J.M., Heikkila,K., Alexander,M., Muller-Myhsok,B.,
            Schreiber,S., Meitinger,T., Wichmann,H.E., Aromaa,A.,
            Eriksson,J.G., Traynor,B., Trabzuni,D., Rossin,E., Lage,K.,
            Jacobs,S.B.R., Gibbs,J.R., Birney,E., Kaprio,J., Penninx,B.W.,
            Boomsma,D.I., van Duijn,C., Raitakari,O., Jarvelin,M.R.,
            Zwart,J.A., Cherkas,L., Strachan,D.P., Kubisch,C., Ferrari,M.D.,
            van den Maagdenberg,A.M.J.M., Dichgans,M., Wessman,M., Smith,G.D.,
            Stefansson,K., Daly,M.J., Nyholt,D.R., Chasman,D. and Palotie,A.
  CONSRTM   North American Brain Expression Consortium; UK Brain Expression
            Consortium
  TITLE     Genome-wide meta-analysis identifies new susceptibility loci for
            migraine
  JOURNAL   Nat Genet 45 (8), 912-917 (2013)
   PUBMED   23793025
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Kim,J.H., Jung,S.H., Bae,J.S., Lee,H.S., Yim,S.H., Park,S.Y.,
            Bang,S.Y., Hu,H.J., Shin,H.D., Bae,S.C. and Chung,Y.J.
  TITLE     Deletion variants of RABGAP1L, 10q21.3, and C4 are associated with
            the risk of systemic lupus erythematosus in Korean women
  JOURNAL   Arthritis Rheum 65 (4), 1055-1063 (2013)
   PUBMED   23335107
  REMARK    GeneRIF: Deletion variants of RABGAP1L were found to be
            significantly associated with SLE in Korean women.
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL161671.25, AL008735.2 and Z99127.2.
            
            On Oct 5, 2018 this sequence version replaced XP_016858488.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.26509.1,
                                           SRR3476690.630703.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1"
     Protein         1..242
                     /product="rab GTPase-activating protein 1-like isoform O"
                     /note="TBC1 domain family, member 18; expressed in
                     hematopoietic cells, heart, liver (HLL); rab
                     GTPase-activating protein 1-like"
                     /calculated_mol_wt=28067
     CDS             1..242
                     /gene="RABGAP1L"
                     /gene_synonym="HHL; TBC1D18"
                     /coded_by="NM_001366454.1:996..1724"
                     /note="isoform O is encoded by transcript variant 18"
                     /db_xref="GeneID:9910"
                     /db_xref="HGNC:HGNC:24663"
                     /db_xref="MIM:609238"
ORIGIN      
        1 mmeeisimva ydahvfsqlh dedfltslva iskprsmvpt kklkkyekey qtmresqlqq
       61 edpmdrykre nrrlqeasmr leqenddlah elvtskialr ndldqaedka dvlnkelllt
      121 kqrlveteee krkqeeetaq lkevfrkqle kaeyeikktt aiiaeykqic sqlstrlekq
      181 qaaskeelev vkelehqrga lmneiqaakn swfsktlnsi ktatgtqplq papvtqppke
      241 st
//
LOCUS       NP_001346574             460 aa            linear   ROD 27-APR-2025
DEFINITION  rab-3A-interacting protein isoform 1 [Mus musculus].
ACCESSION   NP_001346574 XP_006513608
VERSION     NP_001346574.1
DBSOURCE    REFSEQ: accession NM_001359645.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Li,L., Li,J. and Yuan,L.
  TITLE     A direct interaction between CENTLEIN and RABIN8 is required for
            primary cilium formation
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (9), 1434-1444 (2023)
   PUBMED   37475549
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Walia,V., Cuenca,A., Vetter,M., Insinna,C., Perera,S., Lu,Q.,
            Ritt,D.A., Semler,E., Specht,S., Stauffer,J., Morrison,D.K.,
            Lorentzen,E. and Westlake,C.J.
  TITLE     Akt Regulates a Rab11-Effector Switch Required for Ciliogenesis
  JOURNAL   Dev Cell 50 (2), 229-246 (2019)
   PUBMED   31204173
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Vetter,M., Stehle,R., Basquin,C. and Lorentzen,E.
  TITLE     Structure of Rab11-FIP3-Rabin8 reveals simultaneous binding of FIP3
            and Rabin8 effectors to Rab11
  JOURNAL   Nat Struct Mol Biol 22 (9), 695-702 (2015)
   PUBMED   26258637
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   7  (residues 1 to 460)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   8  (residues 1 to 460)
  AUTHORS   Taniwaki,T., Haruna,K., Nakamura,H., Sekimoto,T., Oike,Y.,
            Imaizumi,T., Saito,F., Muta,M., Soejima,Y., Utoh,A., Nakagata,N.,
            Araki,M., Yamamura,K. and Araki,K.
  TITLE     Characterization of an exchangeable gene trap using pU-17 carrying
            a stop codon-beta geo cassette
  JOURNAL   Dev Growth Differ 47 (3), 163-172 (2005)
   PUBMED   15840001
REFERENCE   9  (residues 1 to 460)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
REFERENCE   10 (residues 1 to 460)
  AUTHORS   Yoshida,M., Yagi,T., Furuta,Y., Takayanagi,K., Kominami,R.,
            Takeda,N., Tokunaga,T., Chiba,J., Ikawa,Y. and Aizawa,S.
  TITLE     A new strategy of gene trapping in ES cells using 3'RACE
  JOURNAL   Transgenic Res 4 (4), 277-287 (1995)
   PUBMED   7655516
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY059863.1, AK152122.1, AA980340.1, AK045783.1 and BM938945.1.
            
            On Jan 13, 2018 this sequence version replaced XP_006513608.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK152122.1, SRR13422597.786782.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 64.96 cM"
     Protein         1..460
                     /product="rab-3A-interacting protein isoform 1"
                     /note="gene trap PAT 12; rab-3A-interacting protein;
                     rabin-3; SSX2-interacting protein; rab3A-interacting
                     protein"
                     /calculated_mol_wt=50764
     Region          <87..226
                     /region_name="Cast"
                     /note="RIM-binding protein of the cytomatrix active zone;
                     pfam10174"
                     /db_xref="CDD:431111"
     Region          173..241
                     /region_name="Sec2p"
                     /note="GDP/GTP exchange factor Sec2p; pfam06428"
                     /db_xref="CDD:428938"
     Region          266..458
                     /region_name="Rab11BD_RAB3IP"
                     /note="Rab11 binding domain of Rab-3A-interacting protein
                     (RAB3IP); cd21068"
                     /db_xref="CDD:411032"
     Site            order(351..357,412,415..416,419,423,428..432)
                     /site_type="other"
                     /note="Rab11 binding site [polypeptide binding]"
                     /db_xref="CDD:411032"
     CDS             1..460
                     /gene="Rab3ip"
                     /gene_synonym="B230311A06; Gtpat12; Rabin3"
                     /coded_by="NM_001359645.1:225..1607"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS88090.1"
                     /db_xref="GeneID:216363"
                     /db_xref="MGI:MGI:105933"
ORIGIN      
        1 mandplegfh evnlasptsp dllgvcdpgt qeqttspsvi yrphpstlca aplqanaldl
       61 sdlptqpvys sprhfncaev snisahapdp assvpsavas gltkltsrkd scnaereflq
      121 gatiteasag nddifglstd slsrlrspsv levrekgyer lkeelakaqr elklkdeece
      181 rlskvrdqlg qeleeltasl feeahkmvre anvkqataek qlkeaqgkid vlqaevaalk
      241 tlvlssspts ptqeplaaak tpfkrghtrn kstssamggs hqdlsviqpi vkdckeadls
      301 lynefrswkd eptmdrtcpf ldkiyqedif pcltfaksel asavleaven ntlsiepvgl
      361 qpirfvkasa vecggpkkca ltgqskpcrh rirlgdsscc yyispfcryr itsvcnffty
      421 iryiqqglvk qqdvdqmfwe vmqlrkemsl aklgyfkeel
//
LOCUS       NP_055401                714 aa            linear   PRI 27-APR-2025
DEFINITION  hormonally up-regulated neu tumor-associated kinase [Homo sapiens].
ACCESSION   NP_055401
VERSION     NP_055401.1
DBSOURCE    REFSEQ: accession NM_014586.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Jiang,S., Han,X., Liu,T., He,Y., Zhao,Z., Liu,T., Cheng,S.,
            Zhang,J., Duan,L., Liu,Y., Cheng,T., Liu,Y., Ye,Q. and Gao,S.
  TITLE     HUNK inhibits cargo uptake and lysosomal traffic in the caveolar
            pathway via the AGAP3/ARF6
  JOURNAL   Sci Bull (Beijing) 69 (2), 173-178 (2024)
   PUBMED   38071109
  REMARK    GeneRIF: HUNK inhibits cargo uptake and lysosomal traffic in the
            caveolar pathway via the AGAP3/ARF6.
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Han,X., Jiang,S., Gu,Y., Ding,L., Zhao,E., Cao,D., Wang,X., Wen,Y.,
            Pan,Y., Yan,X., Duan,L., Sun,M., Zhou,T., Liu,Y., Hu,H., Ye,Q. and
            Gao,S.
  TITLE     HUNK inhibits epithelial-mesenchymal transition of CRC via direct
            phosphorylation of GEF-H1 and activating RhoA/LIMK-1/CFL-1
  JOURNAL   Cell Death Dis 14 (5), 327 (2023)
   PUBMED   37193711
  REMARK    GeneRIF: HUNK inhibits epithelial-mesenchymal transition of CRC via
            direct phosphorylation of GEF-H1 and activating RhoA/LIMK-1/CFL-1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 714)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Williams,C.B., Phelps-Polirer,K., Dingle,I.P., Williams,C.J.,
            Rhett,M.J., Eblen,S.T., Armeson,K., Hill,E.G. and Yeh,E.S.
  TITLE     HUNK phosphorylates EGFR to regulate breast cancer metastasis
  JOURNAL   Oncogene 39 (5), 1112-1124 (2020)
   PUBMED   31597954
  REMARK    GeneRIF: HUNK phosphorylates EGFR to regulate breast cancer
            metastasis.
            Erratum:[Oncogene. 2021 May;40(20):3635-3636. doi:
            10.1038/s41388-021-01797-3. PMID: 33958726]
REFERENCE   5  (residues 1 to 714)
  AUTHORS   Zambrano,J.N., Eblen,S.T., Abt,M., Rhett,J.M., Muise-Helmericks,R.
            and Yeh,E.S.
  TITLE     HUNK Phosphorylates Rubicon to Support Autophagy
  JOURNAL   Int J Mol Sci 20 (22), 5813 (2019)
   PUBMED   31752345
  REMARK    GeneRIF: Rubicon as a novel substrate of HUNK.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 714)
  AUTHORS   Wertheim,G.B., Yang,T.W., Pan,T.C., Ramne,A., Liu,Z., Gardner,H.P.,
            Dugan,K.D., Kristel,P., Kreike,B., van de Vijver,M.J.,
            Cardiff,R.D., Reynolds,C. and Chodosh,L.A.
  TITLE     The Snf1-related kinase, Hunk, is essential for mammary tumor
            metastasis
  JOURNAL   Proc Natl Acad Sci U S A 106 (37), 15855-15860 (2009)
   PUBMED   19717424
  REMARK    GeneRIF: a gene expression signature that distinguishes Hunk-wild
            type from Hunk-deficient tumors predicts clinical outcome in women
            with breast cancer
REFERENCE   7  (residues 1 to 714)
  AUTHORS   Vasilescu,J., Zweitzig,D.R., Denis,N.J., Smith,J.C., Ethier,M.,
            Haines,D.S. and Figeys,D.
  TITLE     The proteomic reactor facilitates the analysis of affinity-purified
            proteins by mass spectrometry: application for identifying
            ubiquitinated proteins in human cells
  JOURNAL   J Proteome Res 6 (1), 298-305 (2007)
   PUBMED   17203973
REFERENCE   8  (residues 1 to 714)
  AUTHORS   Korobko,I.V., Zavalishina,L.E., Kiselev,S.L., Raikhlin,N.T. and
            Frank,G.A.
  TITLE     [Proteinkinase MAK-V/Hunk as a possible dianostic and prognostic
            marker of human breast carcinoma]
  JOURNAL   Arkh Patol 66 (5), 6-9 (2004)
   PUBMED   15575376
  REMARK    GeneRIF: Overproduction of MAK-V/Hunk in human breast cancer may be
            used fore more precise molecular typing.
REFERENCE   9  (residues 1 to 714)
  AUTHORS   Korobko,I.V., Korobko,E.V. and Kiselev,S.L.
  TITLE     The MAK-V protein kinase regulates endocytosis in mouse
  JOURNAL   Mol Gen Genet 264 (4), 411-418 (2000)
   PUBMED   11129044
REFERENCE   10 (residues 1 to 714)
  AUTHORS   Gardner,H.P., Wertheim,G.B., Ha,S.I., Copeland,N.G., Gilbert,D.J.,
            Jenkins,N.A., Marquis,S.T. and Chodosh,L.A.
  TITLE     Cloning and characterization of Hunk, a novel mammalian
            SNF1-related protein kinase
  JOURNAL   Genomics 63 (1), 46-59 (2000)
   PUBMED   10662544
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP000256.1 and AJ271722.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ271722.1, SRR1660807.109709.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270112.7/ ENSP00000270112.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..714
                     /product="hormonally up-regulated neu tumor-associated
                     kinase"
                     /EC_number="2.7.11.1"
                     /note="hormonally upregulated neu tumor-associated kinase;
                     hormonally upregulated Neu-associated kinase;
                     serine/threonine protein kinase MAK-V; B19"
                     /calculated_mol_wt=79555
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P57058.1)"
     Region          58..320
                     /region_name="STKc_HUNK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Hormonally up-regulated Neu-associated kinase (also called
                     MAK-V); cd14070"
                     /db_xref="CDD:270972"
     Site            order(68..72,76,89,91,124,140..143,147,149..150,152,
                     185..186,188,190..191,193,203..204,207,223..228,230,
                     259..262,264)
                     /site_type="active"
                     /db_xref="CDD:270972"
     Site            order(68..71,76,89,91,124,140..143,147,190..191,193,
                     203..204)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270972"
     Site            order(147,149..150,152,186,188,190,207,223..228,230,
                     259..262,264)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270972"
     Site            order(203..218,220..228)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270972"
     Region          437..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P57058.1)"
     Region          518..552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P57058.1)"
     Region          590..615
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P57058.1)"
     CDS             1..714
                     /gene="HUNK"
                     /coded_by="NM_014586.2:656..2800"
                     /db_xref="CCDS:CCDS13610.1"
                     /db_xref="GeneID:30811"
                     /db_xref="HGNC:HGNC:13326"
                     /db_xref="MIM:606532"
ORIGIN      
        1 mpaaagdgll gepaapgggg gaedaarpaa acegsflpaw vsgvprerlr dfqhhkrvgn
       61 yligsrklge gsfakvregl hvltgekvai kvidkkrakk dtyvtknlrr egqiqqmirh
      121 pnitqlldil etensyylvm elcpggnlmh kiyekkrlee searryirql isavehlhra
      181 gvvhrdlkie nllldednni klidfglsnc agilgysdpf stqcgspaya apellarkky
      241 gpkidvwsig vnmyamltgt lpftvepfsl ralyqkmvdk emnplptqls tgaisflrsl
      301 lepdpvkrpn iqqalanrwl nenytgkvpc nvtypnrisl edlspsvvlh mteklgykns
      361 dvintvlsnr achilaiyfl lnkkleryls gksdiqdslc yktrlyqiek yrapkesyea
      421 sldtwtrdle fhavqdkkpk eqekrgdflh rpfskkldkn lpshkqpsgs lmtqiqntka
      481 llkdrkasks sfpdkdsfgc rnifrktsds ncvasssmef ipvppprtpr ivkkpephqp
      541 gpgstgiphk edplmldmvr sfesvdrddh vevlspshhy rilnspvsla rrnssertls
      601 pglpsgsmsp lhtplhptlv sfahedknsp pkeeglccpp pvpsngpmqp lgspncvksr
      661 grfpmmgigq mlrkrhqslq psadrpleas lpplqplapv nlafdmadgv ktqc
//
LOCUS       NP_001352176             486 aa            linear   PRI 27-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 3
            [Homo sapiens].
ACCESSION   NP_001352176
VERSION     NP_001352176.1
DBSOURCE    REFSEQ: accession NM_001365247.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Zhang,S., Huang,J., Lan,Z., Xiao,Y., Liao,Y., Basnet,S., Huang,P.,
            Li,Y., Yan,J., Sheng,Y., Zhou,W., Liu,Q., Tan,H., Tan,Y., Yuan,L.,
            Wang,L., Dai,L., Zhang,W. and Du,C.
  TITLE     CPEB1 Controls NRF2 Proteostasis and Ferroptosis Susceptibility in
            Pancreatic Cancer
  JOURNAL   Int J Biol Sci 20 (8), 3156-3172 (2024)
   PUBMED   38904009
  REMARK    GeneRIF: CPEB1 Controls NRF2 Proteostasis and Ferroptosis
            Susceptibility in Pancreatic Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Pico,S., Parras,A., Santos-Galindo,M., Pose-Utrilla,J., Castro,M.,
            Fraga,E., Hernandez,I.H., Elorza,A., Anta,H., Wang,N.,
            Marti-Sanchez,L., Belloc,E., Garcia-Esparcia,P., Garrido,J.J.,
            Ferrer,I., Macias-Garcia,D., Mir,P., Artuch,R., Perez,B.,
            Hernandez,F., Navarro,P., Lopez-Sendon,J.L., Iglesias,T.,
            Yang,X.W., Mendez,R. and Lucas,J.J.
  TITLE     CPEB alteration and aberrant transcriptome-polyadenylation lead to
            a treatable SLC19A3 deficiency in Huntington's disease
  JOURNAL   Sci Transl Med 13 (613), eabe7104 (2021)
   PUBMED   34586830
  REMARK    GeneRIF: CPEB alteration and aberrant transcriptome-polyadenylation
            lead to a treatable SLC19A3 deficiency in Huntington's disease.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Shao,K., Pu,W., Zhang,J., Guo,S., Qian,F., Glurich,I., Jin,Q.,
            Ma,Y., Ju,S., Zhang,Z. and Ding,W.
  TITLE     DNA hypermethylation contributes to colorectal cancer metastasis by
            regulating the binding of CEBPB and TFCP2 to the CPEB1 promoter
  JOURNAL   Clin Epigenetics 13 (1), 89 (2021)
   PUBMED   33892791
  REMARK    GeneRIF: DNA hypermethylation contributes to colorectal cancer
            metastasis by regulating the binding of CEBPB and TFCP2 to the
            CPEB1 promoter.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Sovijit,W., Sovijit,W., Ishii,Y., Kambe,J., Fujita,T., Watanabe,G.,
            Yamaguchi,H. and Nagaoka,K.
  TITLE     Estrogen promotes increased breast cancer cell proliferation and
            migration through downregulation of CPEB1 expression
  JOURNAL   Biochem Biophys Res Commun 534, 871-876 (2021)
   PUBMED   33162033
  REMARK    GeneRIF: Estrogen promotes increased breast cancer cell
            proliferation and migration through downregulation of CPEB1
            expression.
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Jiao,W., Zhao,S., Liu,R., Guo,T. and Qin,Y.
  TITLE     CPEB1 deletion is not a common explanation for premature ovarian
            insufficiency in a Chinese cohort
  JOURNAL   J Ovarian Res 13 (1), 49 (2020)
   PUBMED   32354341
  REMARK    GeneRIF: CPEB1 deletion is not a common explanation for premature
            ovarian insufficiency in a Chinese cohort.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Hagele,S., Kuhn,U., Boning,M. and Katschinski,D.M.
  TITLE     Cytoplasmic polyadenylation-element-binding protein (CPEB)1 and 2
            bind to the HIF-1alpha mRNA 3'-UTR and modulate HIF-1alpha protein
            expression
  JOURNAL   Biochem J 417 (1), 235-246 (2009)
   PUBMED   18752464
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Sasayama,T., Marumoto,T., Kunitoku,N., Zhang,D., Tamaki,N.,
            Kohmura,E., Saya,H. and Hirota,T.
  TITLE     Over-expression of Aurora-A targets cytoplasmic polyadenylation
            element binding protein and promotes mRNA polyadenylation of Cdk1
            and cyclin B1
  JOURNAL   Genes Cells 10 (7), 627-638 (2005)
   PUBMED   15966895
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Wilczynska,A., Aigueperse,C., Kress,M., Dautry,F. and Weil,D.
  TITLE     The translational regulator CPEB1 provides a link between dcp1
            bodies and stress granules
  JOURNAL   J Cell Sci 118 (Pt 5), 981-992 (2005)
   PUBMED   15731006
  REMARK    GeneRIF: CPEB1 has a role in compartmentalization of mRNA
            metabolism in the cytoplasm, between dcp1 bodies and stress
            granules
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Mendez,R. and Richter,J.D.
  TITLE     Translational control by CPEB: a means to the end
  JOURNAL   Nat Rev Mol Cell Biol 2 (7), 521-529 (2001)
   PUBMED   11433366
  REMARK    Review article
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Welk,J.F., Charlesworth,A., Smith,G.D. and MacNicol,A.M.
  TITLE     Identification and characterization of the gene encoding human
            cytoplasmic polyadenylation element binding protein
  JOURNAL   Gene 263 (1-2), 113-120 (2001)
   PUBMED   11223249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105339.9, AC110291.7 and
            AC245033.2.
            
            Summary: This gene encodes a member of the cytoplasmic
            polyadenylation element binding protein family. This highly
            conserved protein binds to a specific RNA sequence, called the
            cytoplasmic polyadenylation element, found in the 3' untranslated
            region of some mRNAs. The encoded protein functions in both the
            cytoplasm and the nucleus. It is involved in the regulation of mRNA
            translation, as well as processing of the 3' untranslated region,
            and may play a role in cell proliferation and tumorigenesis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.132385.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..486
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 3"
                     /note="CPE-binding protein 1"
                     /calculated_mol_wt=53504
     Region          <1..232
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          234..336
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          347..430
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          424..479
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..486
                     /gene="CPEB1"
                     /gene_synonym="CPE-BP1; CPEB; CPEB-1; h-CPEB; hCPEB-1"
                     /coded_by="NM_001365247.1:383..1843"
                     /note="isoform 3 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS45330.2"
                     /db_xref="GeneID:64506"
                     /db_xref="HGNC:HGNC:21744"
                     /db_xref="MIM:607342"
ORIGIN      
        1 mlfptsaqes srglpdandl clglqslslt gwdrpwstqd sdssaqssth svlsmlhnpl
       61 gnvlgkppls flpldplgsd lvdkfpapsv rgsrldtrpi ldsrssspsd sdtsgfssgs
      121 dhlsdlissl rispplpfls lsgggprdpl kmgvgsrmdq eqaalaavtp sptsaskrwp
      181 gasvwpswdl leapkdpfsi erearlhrqa aavneatctw sgqlpprnyk npiysckvfl
      241 ggvpwditea glvntfrvfg slsvewpgkd gkhprcppkg yvylvfelek svrsllqacs
      301 hdplspdgls eyyfkmssrr mrckevqvip wvladsnfvr spsqrldpsr tvfvgalhgm
      361 lnaealaail ndlfggvvya gidtdkhkyp igsgrvtfnn qrsylkavsa afveikttkf
      421 tkkvqidpyl edslchicss qpgpffcrdq vcfkyfcrsc whwrhsmegl rhhsplmrnq
      481 knrdss
//
LOCUS       NP_001018025             107 aa            linear   PRI 27-APR-2025
DEFINITION  protein p13 MTCP-1 [Homo sapiens].
ACCESSION   NP_001018025
VERSION     NP_001018025.1
DBSOURCE    REFSEQ: accession NM_001018025.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Walker,J.S., Hing,Z.A., Sher,S., Cronin,J., Williams,K.,
            Harrington,B., Skinner,J.N., Cempre,C.B., Gregory,C.T., Pan,A.,
            Yano,M., Beaver,L.P., Walker,B.R., Labanowska,J.M., Heerema,N.A.,
            Mrozek,K., Woyach,J.A., Ruppert,A.S., Lehman,A., Ozer,H.G.,
            Coppola,V., Yan,P., Byrd,J.C., Blachly,J.S. and Lapalombella,R.
  TITLE     Rare t(X;14)(q28;q32) translocation reveals link between MTCP1 and
            chronic lymphocytic leukemia
  JOURNAL   Nat Commun 12 (1), 6338 (2021)
   PUBMED   34732719
  REMARK    GeneRIF: Rare t(X;14)(q28;q32) translocation reveals link between
            MTCP1 and chronic lymphocytic leukemia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Wang,L., McDonnell,S.K., Hebbring,S.J., Cunningham,J.M., St
            Sauver,J., Cerhan,J.R., Isaya,G., Schaid,D.J. and Thibodeau,S.N.
  TITLE     Polymorphisms in mitochondrial genes and prostate cancer risk
  JOURNAL   Cancer Epidemiol Biomarkers Prev 17 (12), 3558-3566 (2008)
   PUBMED   19064571
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Joiner,M., Le Toriellec,E., Despouy,G. and Stern,M.H.
  TITLE     The MTCP1 oncogene modifies T-cell homeostasis before
            leukemogenesis in transgenic mice
  JOURNAL   Leukemia 21 (2), 362-366 (2007)
   PUBMED   17136114
  REMARK    GeneRIF: Transgenic mice overexpressing MTCP1 develop leukemias
            with a CD8 central memory phenotype in most cases.
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Laine,J., Kunstle,G., Obata,T. and Noguchi,M.
  TITLE     Differential regulation of Akt kinase isoforms by the members of
            the TCL1 oncogene family
  JOURNAL   J Biol Chem 277 (5), 3743-3751 (2002)
   PUBMED   11707444
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Laine,J., Kunstle,G., Obata,T., Sha,M. and Noguchi,M.
  TITLE     The protooncogene TCL1 is an Akt kinase coactivator
  JOURNAL   Mol Cell 6 (2), 395-407 (2000)
   PUBMED   10983986
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Madani,A., Choukroun,V., Soulier,J., Cacheux,V., Claisse,J.F.,
            Valensi,F., Daliphard,S., Cazin,B., Levy,V., Leblond,V.,
            Daniel,M.T., Sigaux,F. and Stern,M.H.
  TITLE     Expression of p13MTCP1 is restricted to mature T-cell
            proliferations with t(X;14) translocations
  JOURNAL   Blood 87 (5), 1923-1927 (1996)
   PUBMED   8634440
REFERENCE   7  (residues 1 to 107)
  AUTHORS   Thick,J., Mak,Y.F., Metcalfe,J., Beatty,D. and Taylor,A.M.
  TITLE     A gene on chromosome Xq28 associated with T-cell prolymphocytic
            leukemia in two patients with ataxia telangiectasia
  JOURNAL   Leukemia 8 (4), 564-573 (1994)
   PUBMED   8152252
REFERENCE   8  (residues 1 to 107)
  AUTHORS   Fisch,P., Forster,A., Sherrington,P.D., Dyer,M.J. and Rabbitts,T.H.
  TITLE     The chromosomal translocation t(X;14)(q28;q11) in T-cell
            pro-lymphocytic leukaemia breaks within one gene and activates
            another
  JOURNAL   Oncogene 8 (12), 3271-3276 (1993)
   PUBMED   8247530
REFERENCE   9  (residues 1 to 107)
  AUTHORS   Stern,M.H., Soulier,J., Rosenzwajg,M., Nakahara,K., Canki-Klain,N.,
            Aurias,A., Sigaux,F. and Kirsch,I.R.
  TITLE     MTCP-1: a novel gene on the human chromosome Xq28 translocated to
            the T cell receptor alpha/delta locus in mature T cell
            proliferations
  JOURNAL   Oncogene 8 (9), 2475-2483 (1993)
   PUBMED   8361760
REFERENCE   10 (residues 1 to 107)
  AUTHORS   Kenwrick,S., Levinson,B., Taylor,S., Shapiro,A. and Gitschier,J.
  TITLE     Isolation and sequence of two genes associated with a CpG island 5'
            of the factor VIII gene
  JOURNAL   Hum Mol Genet 1 (3), 179-186 (1992)
   PUBMED   1303175
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX470111.4, AW976554.1 and
            AA744518.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene was identified by involvement in some t(X;14)
            translocations associated with mature T-cell proliferations. This
            region has a complex gene structure, with a common promoter and 5'
            exon spliced to two different sets of 3' exons that encode two
            different proteins. This gene represents the upstream 13 kDa
            protein that is a member of the TCL1 family. This protein may be
            involved in leukemogenesis. [provided by RefSeq, Mar 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX341834.2, ERR3218371.393469.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000369476.8/
                                                  ENSP00000358488.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..107
                     /product="protein p13 MTCP-1"
                     /note="mature T-cell proliferation-1 type B1; MTCP-1 type
                     B1; TCL1 family AKT coactivator C"
                     /calculated_mol_wt=12469
     Region          6..105
                     /region_name="TCL1_MTCP1"
                     /note="TCL1/MTCP1 family; pfam01840"
                     /db_xref="CDD:460358"
     CDS             1..107
                     /gene="MTCP1"
                     /gene_synonym="P13MTCP1; p8MTCP1; TCL1C"
                     /coded_by="NM_001018025.4:491..814"
                     /db_xref="CCDS:CCDS44027.1"
                     /db_xref="GeneID:4515"
                     /db_xref="HGNC:HGNC:7423"
                     /db_xref="MIM:300116"
ORIGIN      
        1 magedvgapp dhlwvhqegi yrdeyqrtwv avveeetsfl rarvqqiqvp lgdaarpshl
       61 ltsqlplmwq lypeerymdn nsrlwqiqhh lmvrgvqell lkllpdd
//
LOCUS       NP_081330                128 aa            linear   ROD 27-APR-2025
DEFINITION  cystatin-12 precursor [Mus musculus].
ACCESSION   NP_081330 XP_130487 XP_923248
VERSION     NP_081330.2
DBSOURCE    REFSEQ: accession NM_027054.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Do,H.Q., Hewetson,A., Borcik,C.G., Hastert,M.C., Whelly,S.,
            Wylie,B.J., Sutton,R.B. and Cornwall,G.A.
  TITLE     Cross-seeding between the functional amyloidogenic CRES and CRES3
            family members and their regulation of Abeta assembly
  JOURNAL   J Biol Chem 296, 100250 (2021)
   PUBMED   33384380
  REMARK    GeneRIF: Cross-seeding between the functional amyloidogenic CRES
            and CRES3 family members and their regulation of Abeta assembly.
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Frygelius,J., Oscarson,M., Nordqvist,K., Wedell,A. and Tohonen,V.
  TITLE     The reproductive tissue specific cystatin subgroup of genes:
            expression during gonadal development in wildtype and testatin
            knockout animals
  JOURNAL   Sex Dev 1 (6), 363-372 (2007)
   PUBMED   18391548
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Li,Y., Putnam-Lawson,C.A., Knapp-Hoch,H., Friel,P.J., Mitchell,D.,
            Hively,R. and Griswold,M.D.
  TITLE     Immunolocalization and regulation of cystatin 12 in mouse testis
            and epididymis
  JOURNAL   Biol Reprod 73 (5), 872-880 (2005)
   PUBMED   15972886
  REMARK    GeneRIF: CST12 protein may play a specialized role during
            spermatogenesis and sperm maturation
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Hsia,N. and Cornwall,G.A.
  TITLE     Cres2 and Cres3: new members of the cystatin-related epididymal
            spermatogenic subgroup of family 2 cystatins
  JOURNAL   Endocrinology 144 (3), 909-915 (2003)
   PUBMED   12586767
  REMARK    GeneRIF: CRES2 and CRES3 represent new members of a subgroup of
            cystatin family 2 proteins that likely carry out tissue-specific
            functions distinct from that of typical cystatins CRES2, CRES3]
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Cornwall,G.A. and Hsia,N.
  TITLE     A new subgroup of the family 2 cystatins
  JOURNAL   Mol Cell Endocrinol 200 (1-2), 1-8 (2003)
   PUBMED   12644294
  REMARK    Review article
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Li,Y., Friel,P.J., Robinson,M.O., McLean,D.J. and Griswold,M.D.
  TITLE     Identification and characterization of testis- and
            epididymis-specific genes: cystatin SC and cystatin TE-1
  JOURNAL   Biol Reprod 67 (6), 1872-1880 (2002)
   PUBMED   12444065
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC119432.2, AK005670.1 and AF440737.2.
            
            On Feb 15, 2019 this sequence version replaced NP_081330.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF440737.2, CA463760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 73.55 cM"
     Protein         1..128
                     /product="cystatin-12 precursor"
                     /note="cystatin-related epididymal spermatogenic protein
                     3; cystatin TE-1; cystatin-related gene expressed in
                     testis and epididymis"
                     /calculated_mol_wt=12722
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9DAN8.1)"
                     /calculated_mol_wt=2332
     mat_peptide     22..128
                     /product="Cystatin-12. /id=PRO_0000285791"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DAN8.1)"
                     /calculated_mol_wt=12722
     Region          23..126
                     /region_name="CY"
                     /note="Cystatin-like domain; Cystatins are a family of
                     cysteine protease inhibitors that occur mainly as single
                     domain proteins. However some extracellular proteins such
                     as kininogen, His-rich glycoprotein and fetuin also
                     contain these domains; cl09238"
                     /db_xref="CDD:447698"
     Site            122
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9DAN8.1)"
     CDS             1..128
                     /gene="Cst12"
                     /gene_synonym="1700006F03Rik; CRES3"
                     /coded_by="NM_027054.2:36..422"
                     /db_xref="CCDS:CCDS50737.2"
                     /db_xref="GeneID:69362"
                     /db_xref="MGI:MGI:1916612"
ORIGIN      
        1 mlwksvlsva livlgihdcs fkfleidkne eefaisvehv vfhfnenqdd dfaykflrvr
       61 rslrqkytlk ylvdlemgrt lcgkydedid ncplqegpge rkvrctyive teawvtkfti
      121 lnstcvqt
//
LOCUS       NP_001354464             425 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 28 [Homo sapiens].
ACCESSION   NP_001354464
VERSION     NP_001354464.1
DBSOURCE    REFSEQ: accession NM_001367535.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.821490.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..425
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 28"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=47365
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     CDS             1..425
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367535.1:95..1372"
                     /note="isoform 28 is encoded by transcript variant 28"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk pqsnnknslv spaqepaplq tamepqttvv
      361 hnatdgikgs tescnttted edlkarclkd gapgteqppl qacspsllsa pqpcenrrsl
      421 rlqns
//
LOCUS       NP_653299               1001 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 35 isoform 1 [Homo
            sapiens].
ACCESSION   NP_653299
VERSION     NP_653299.4
DBSOURCE    REFSEQ: accession NM_144698.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Wang,Y., Peng,M., Zhong,Y., Xiong,W., Zhu,L. and Jin,X.
  TITLE     The E3 ligase RBCK1 reduces the sensitivity of ccRCC to sunitinib
            through the ANKRD35-MITD1-ANXA1 axis
  JOURNAL   Oncogene 42 (13), 952-966 (2023)
   PUBMED   36732658
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Ruiz-Arenas,C., Caceres,A., Lopez,M., Pelegri-Siso,D., Gonzalez,J.
            and Gonzalez,J.R.
  TITLE     Identifying chromosomal subpopulations based on their recombination
            histories advances the study of the genetic basis of phenotypic
            traits
  JOURNAL   Genome Res 30 (12), 1802-1814 (2020)
   PUBMED   33203765
  REMARK    GeneRIF: Identifying chromosomal subpopulations based on their
            recombination histories advances the study of the genetic basis of
            phenotypic traits.
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA399526.1, BC101618.1, AK294308.1, AC243547.1 and HY327286.1.
            
            On Jul 23, 2013 this sequence version replaced NP_653299.3.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.134397.1, AK091120.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355594.9/ ENSP00000347802.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.1"
     Protein         1..1001
                     /product="ankyrin repeat domain-containing protein 35
                     isoform 1"
                     /note="ankyrin repeat domain-containing protein 35"
                     /calculated_mol_wt=109806
     Region          24..242
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          24..51
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(53,55,59..60,63..65,67..68,72,75,84,86,88,92..93,
                     96..98,100..101,105,108,117,119,121,125..126,129..131,
                     133..134,138,141,150)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          53..84
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          53..82
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N283.3)"
     Region          86..117
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          86..115
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N283.3)"
     Region          119..150
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          119..148
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N283.3)"
     Region          152..183
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          152..181
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N283.3)"
     Region          185..216
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          185..214
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N283.3)"
     Region          218..247
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N283.3)"
     Region          256..296
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N283.3)"
     Region          <301..>960
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          352..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N283.3)"
     Region          559..601
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N283.3)"
     Region          879..902
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N283.3)"
     CDS             1..1001
                     /gene="ANKRD35"
                     /coded_by="NM_144698.5:109..3114"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS72867.1"
                     /db_xref="GeneID:148741"
                     /db_xref="HGNC:HGNC:26323"
ORIGIN      
        1 mkrifscsst qvaverwnrh dqklleavhr gdvgrvaala srksarptkl dsngqspfhl
       61 aaskgltecl tillangadi nsknedgsta lhlatiscqp qcvkvllqhg anedavdaen
      121 rsplhwaass gcassvlllc dheafldvld ndgrtplmia slgghaaics qllqrgarvn
      181 vtdkndksal ilacekgsae vaelllshga dagavdstgh dalhyalhtq dkalwrhlqq
      241 alsrrrrggq rlvqhpdlas qaspsepqag sppksswrae peeeqeeked edpcseewrw
      301 kyeeerrkvv rleqelvqkt eecktqaaay ldlenqireq aqelgvllsw eprasgkqgs
      361 slrpggdgme qgcpkdllae stqelkkqqq aaatvnpvla pkkaedsapg kiqyevhgrs
      421 qpeeqgppqs pasetirkat gqqlttngaq tfgpdhadql pagqkessqv lgvepggtva
      481 epvgpaamnq lllqlreela avwrekdaar galsrpvmeg algtpraeaa aaawekmear
      541 lervlarlew akaglqvkpe vpsqesrega lkaapgsikq deekekrvpg aqgeplgalg
      601 gekalgglak gqlekemsvl rlsnsnllee lgelgrerqr lqrelqslsq rlqrefvpkp
      661 qaqvqlqqlr qsvglltnel amekeatekl rkllasqssg lrglwdclpa dlvgersaqs
      721 kaaesleelr acistlvdrh reaqqvlarl qeenqqlrgs lspcrepgts lkapaspqva
      781 aleqdlgkle eelravqatm sgksqeigkl kqllyqatee vaelrareaa slrqhektrg
      841 slvaqaqawg qelkalleky ntacrevgrl reavaeerrr sgdlaaqaae qerqasemrg
      901 rseqfektae llkekmehli gacrdkeaki kellkkleql seevlairge narlalqlqd
      961 sqknheeiis tyrnhllnaa rgymehevyn illqilsmee e
//
LOCUS       NP_001356780             827 aa            linear   VRT 27-APR-2025
DEFINITION  outer dense fiber protein 2 isoform 2 [Xenopus laevis].
ACCESSION   NP_001356780
VERSION     NP_001356780.1
DBSOURCE    REFSEQ: accession NM_001369851.1
KEYWORDS    RefSeq.
SOURCE      Xenopus laevis (African clawed frog)
  ORGANISM  Xenopus laevis
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae;
            Xenopus; Xenopus.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Klein,S.L., Strausberg,R.L., Wagner,L., Pontius,J., Clifton,S.W.
            and Richardson,P.
  TITLE     Genetic and genomic tools for Xenopus research: The NIH Xenopus
            initiative
  JOURNAL   Dev Dyn 225 (4), 384-391 (2002)
   PUBMED   12454917
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC087396.1, BX843128.1 and BQ731573.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed/partial sample support SAMD00012418,
                              SAMD00012419 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Xenopus laevis"
                     /db_xref="taxon:8355"
                     /chromosome="8L"
                     /map="8L"
     Protein         1..827
                     /product="outer dense fiber protein 2 isoform 2"
                     /note="outer dense fiber protein 2; cenexin; outer dense
                     fiber of sperm tails protein 2"
                     /calculated_mol_wt=96270
     Region          1..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQ23.1)"
     Region          <94..786
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          339..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQ23.1)"
     CDS             1..827
                     /gene="odf2.L"
                     /gene_synonym="odf2"
                     /coded_by="NM_001369851.1:107..2590"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:496006"
                     /db_xref="Xenbase:XB-GENE-977569"
ORIGIN      
        1 mknrspsppl hvhvdestpv hvhikkssrp paktqqgakl kkkgmgnlrr satvktkvpw
       61 ippgksslrd aglkweglth rlditppdte rmfsalrmsd lstdeeemkr skmnsyeeki
      121 atlmsemgtl khelelqkre kylgkceeql aaskrlleaq qeelaevsqe lvetenenvw
      181 lkrsldriqe ekglsilqkq qlqeekahll aklleaetdg aeaakqvtll sdtiqrlkhe
      241 krmtstdinl ltrqkelllq klntfedtnr slrtllreqh rqetetyrlm eqkemllkkl
      301 sdadtekmhl qlklheqeek vedllaqlkt ekdlsktase vsksiestka hlqgqlrtre
      361 aennrlsvqi rnlerneahq keeivklmeq ltelkqkvds ekealkksvr aqkqraerse
      421 etlemlnrql vgndselaka lssaetwrsr ynklmkessq heeevavlsn rlkgllgesh
      481 gieergrler dslleklhqq ttentclrle heklkasltt veeklslaqs evqqlknslr
      541 qyeglvdtyk eqlqksrqea nsislqlems ekenkniked mnleleqmrr kfqnrlsele
      601 hlpeilkste ldlqechqql rsyeqkssel sstisdlrtr meqqgdkmes trdryqsave
      661 enkhlvmkle elerrledas tqnrellqav akrdesmhqn qqrldektre csalarqlea
      721 aiedsrrqvd qtrervtske rvtqskildl etqlsktkte lnqfrrskdd aerrfqsrlq
      781 dlkdrleqse stnrsmqnyv qflkssyanv fgdatlsssp irprtpl
//
LOCUS       NP_001013650             463 aa            linear   PRI 27-APR-2025
DEFINITION  DDB1- and CUL4-associated factor 12-like protein 2 [Homo sapiens].
ACCESSION   NP_001013650 XP_293387
VERSION     NP_001013650.1
DBSOURCE    REFSEQ: accession NM_001013628.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
  REMARK    GeneRIF: Functionally characterizes other DDB1- and CUL4-associated
            factors, including the DCAF12 factor which most closely resembles
            the product of this gene.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445072.17, BC136674.1 and
            AY726580.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 30, 2005 this sequence version replaced XP_293387.1.
            
            Summary: This gene encodes a member of the WD repeat protein
            family. WD repeats are minimally conserved regions of approximately
            40 amino acids typically bracketed by Gly-His and Trp-Asp (GH-WD),
            which may facilitate formation of heterotrimeric or multi-protein
            complexes. Members of this family are involved in a variety of
            cellular processes, including cell cycle progression, signal
            transduction, apoptosis, and gene regulation. This gene appears to
            represent an intronless retrocopy of a related multi-exon gene
            located on chromosome 9. However, the CDS of this intronless gene
            remains intact, it is conserved in other mammalian species, it is
            known to be transcribed, and it is therefore thought to encode a
            functional protein. [provided by RefSeq, May 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR1803612.100109.1, SRR1660809.50847.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360028.4/ ENSP00000353128.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..463
                     /product="DDB1- and CUL4-associated factor 12-like protein
                     2"
                     /note="WD repeat-containing protein 40C"
                     /calculated_mol_wt=50672
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VW00.1)"
     Region          89..137
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VW00.1)"
     Region          100..145
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <109..293
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          138..184
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VW00.1)"
     Region          153..192
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          185..252
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VW00.1)"
     Region          197..228
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          230..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          253..297
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VW00.1)"
     Region          265..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          298..341
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VW00.1)"
     Region          310..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          342..401
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VW00.1)"
     Region          402..445
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VW00.1)"
     CDS             1..463
                     /gene="DCAF12L2"
                     /gene_synonym="WDR40C"
                     /coded_by="NM_001013628.3:366..1757"
                     /db_xref="CCDS:CCDS43991.1"
                     /db_xref="GeneID:340578"
                     /db_xref="HGNC:HGNC:32950"
ORIGIN      
        1 maqqqtgsrk rkapaveaga gssssqglaa adgegpllpk kqkrpatrrr lvhylkgrev
       61 gargpaglqg fegelrgyav qrlpellter qldlgtlnkv fasqwlnarq vvcgtkcntl
      121 fvvdvqsghi triplmrdke aglaqahqgc gihaielnps ktllatggen pnslaiyqlp
      181 tldplclgdr hghkdwifav awlsdtvavs gsrdgtvalw rmdpdmfngs iawhsevglp
      241 vyahirprdv eaiprastnp snrkvralaf sgknqelgav sldgyfhlwk arstlsrlls
      301 irlpycrenv cltycdelsl yavgsqshvs fldprqrqqn irplcsregg tgvrslsfyq
      361 hiitvgtghg sllfydiraq kfleerasss ldsmpgpagr klklacgrgw lnqddvwvny
      421 fggmgefpna lythcynwpe mklfvaggpl psglhgnyag lws
//
LOCUS       NP_001275731             889 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear factor of activated T-cells, cytoplasmic 4 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001275731
VERSION     NP_001275731.1
DBSOURCE    REFSEQ: accession NM_001288802.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Yu,S., Sun,Z., Ju,T., Liu,Y., Mei,Z., Wang,C., Qu,Z., Li,N., Wu,F.,
            Liu,K., Lu,M., Huang,M., Pang,X., Jia,Y., Li,Y., Zhang,Y., Dou,S.,
            Jiang,J., Dong,X., Huang,C., Li,W., Zhang,Y., Yuan,Y., Yang,B. and
            Du,W.
  TITLE     The m7G Methyltransferase Mettl1 Drives Cardiac Hypertrophy by
            Regulating SRSF9-Mediated Splicing of NFATc4
  JOURNAL   Adv Sci (Weinh) 11 (29), e2308769 (2024)
   PUBMED   38810124
  REMARK    GeneRIF: The m7G Methyltransferase Mettl1 Drives Cardiac
            Hypertrophy by Regulating SRSF9-Mediated Splicing of NFATc4.
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Zhang,X., Lei,F., Wang,X.M., Deng,K.Q., Ji,Y.X., Zhang,Y., Li,H.,
            Zhang,X.D., Lu,Z. and Zhang,P.
  TITLE     NULP1 Alleviates Cardiac Hypertrophy by Suppressing NFAT3
            Transcriptional Activity
  JOURNAL   J Am Heart Assoc 9 (16), e016419 (2020)
   PUBMED   32805187
  REMARK    GeneRIF: NULP1 Alleviates Cardiac Hypertrophy by Suppressing NFAT3
            Transcriptional Activity.
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Cole,A.J., Iyengar,M., Panesso-Gomez,S., O'Hayer,P., Chan,D.,
            Delgoffe,G.M., Aird,K.M., Yoon,E., Bai,S. and Buckanovich,R.J.
  TITLE     NFATC4 promotes quiescence and chemotherapy resistance in ovarian
            cancer
  JOURNAL   JCI Insight 5 (7), 131486 (2020)
   PUBMED   32182216
  REMARK    GeneRIF: NFATC4 promotes quiescence and chemotherapy resistance in
            ovarian cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 889)
  AUTHORS   Kaminuma,O., Kitamura,N., Nishito,Y., Nemoto,S., Tatsumi,H.,
            Mori,A. and Hiroi,T.
  TITLE     Downregulation of NFAT3 Due to Lack of T-Box Transcription Factor
            TBX5 Is Crucial for Cytokine Expression in T Cells
  JOURNAL   J Immunol 200 (1), 92-100 (2018)
   PUBMED   29180489
  REMARK    GeneRIF: TBX5 deficiency-mediated downregulation of NFAT3 is
            crucial for the high cytokine-producing activity of T cells
REFERENCE   6  (residues 1 to 889)
  AUTHORS   Molkentin,J.D., Lu,J.R., Antos,C.L., Markham,B., Richardson,J.,
            Robbins,J., Grant,S.R. and Olson,E.N.
  TITLE     A calcineurin-dependent transcriptional pathway for cardiac
            hypertrophy
  JOURNAL   Cell 93 (2), 215-228 (1998)
   PUBMED   9568714
REFERENCE   7  (residues 1 to 889)
  AUTHORS   Aramburu,J., Garcia-Cozar,F., Raghavan,A., Okamura,H., Rao,A. and
            Hogan,P.G.
  TITLE     Selective inhibition of NFAT activation by a peptide spanning the
            calcineurin targeting site of NFAT
  JOURNAL   Mol Cell 1 (5), 627-637 (1998)
   PUBMED   9660947
REFERENCE   8  (residues 1 to 889)
  AUTHORS   Rao,A., Luo,C. and Hogan,P.G.
  TITLE     Transcription factors of the NFAT family: regulation and function
  JOURNAL   Annu Rev Immunol 15, 707-747 (1997)
   PUBMED   9143705
  REMARK    Review article
REFERENCE   9  (residues 1 to 889)
  AUTHORS   Hoey,T., Sun,Y.L., Williamson,K. and Xu,X.
  TITLE     Isolation of two new members of the NF-AT gene family and
            functional characterization of the NF-AT proteins
  JOURNAL   Immunity 2 (5), 461-472 (1995)
   PUBMED   7749981
REFERENCE   10 (residues 1 to 889)
  AUTHORS   Vacca,A., Farina,M., Maroder,M., Alesse,E., Screpanti,I., Frati,L.
            and Gulino,A.
  TITLE     Human immunodeficiency virus type-1 tat enhances interleukin-2
            promoter activity through synergism with phorbol ester and
            calcium-mediated activation of the NF-AT cis-regulatory motif
  JOURNAL   Biochem Biophys Res Commun 205 (1), 467-474 (1994)
   PUBMED   7999066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL096870.5, AK310433.1,
            EU887634.1 and BC053855.1.
            
            Summary: This gene encodes a member of the nuclear factor of
            activated T cells (NFAT) protein family. The encoded protein is
            part of a DNA-binding transcription complex. This complex consists
            of at least two components: a preexisting cytosolic component that
            translocates to the nucleus upon T cell receptor stimulation and an
            inducible nuclear component. NFAT proteins are activated by the
            calmodulin-dependent phosphatase, calcineurin. The encoded protein
            plays a role in the inducible expression of cytokine genes in T
            cells, especially in the induction of interleukin-2 and
            interleukin-4. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU887646.1, AK310433.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..889
                     /product="nuclear factor of activated T-cells, cytoplasmic
                     4 isoform 6"
                     /note="nuclear factor of activated T-cells, cytoplasmic 4;
                     T-cell transcription factor NFAT3; nuclear factor of
                     activated T-cells, cytoplasmic, calcineurin-dependent 4"
                     /calculated_mol_wt=93848
     Region          <202..401
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          395..568
                     /region_name="RHD-n_NFAT"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor of activated T-cells (NFAT)
                     proteins; cd07881"
                     /db_xref="CDD:143641"
     Site            order(418,421,423..424,426..428,475,516,518..519,533..534,
                     536,567)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143641"
     Region          573..673
                     /region_name="IPT_NFAT"
                     /note="IPT domain of the NFAT family of transcription
                     factors. NFAT transcription complexes are a target of
                     calcineurin, a calcium dependent phosphatase, and activate
                     genes mainly involved in cell-cell-interaction; cd01178"
                     /db_xref="CDD:238583"
     Site            order(597,661)
                     /site_type="DNA binding"
                     /note="DNA binding sites [nucleotide binding]"
                     /db_xref="CDD:238583"
     CDS             1..889
                     /gene="NFATC4"
                     /gene_synonym="NF-AT3; NF-ATC4; NFAT3"
                     /coded_by="NM_001288802.2:316..2985"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS73625.1"
                     /db_xref="GeneID:4776"
                     /db_xref="HGNC:HGNC:7778"
                     /db_xref="MIM:602699"
ORIGIN      
        1 mpasissifp gptlllscgs eeldsedapp ccrlalgepp pygaapigip rpppprpgmh
       61 sppprpapsp gtwesqpars vrlggpggga ggagggrvle cpsiritsis ptpeppaale
      121 dnpdawgdgs prdypppegf ggyreaggqg ggaffspspg ssslsswsff sdasdeaaly
      181 aacdevesel neaasrfglg splpsprasp rpwtpedpws lygpspggrg pedswlllsa
      241 pgptpasprp aspcgkrrys ssgtpssasp alsrrgslge egsepppppp lplardpgsp
      301 gpfdyvgapp aesipqktrr tsseqavalp rseepascng klplgaeesv appggsrkev
      361 agmdylavps plawskarig ghspifrtsa lppldwplps qyeqlelrie vqprahhrah
      421 yetegsrgav kaapgghpvv kllgysekpl tlqmfigtad ernlrphafy qvhritgkmv
      481 atasyeavvs gtkvlemtll pennmaanid cagilklrns dielrkgetd igrkntrvrl
      541 vfrvhvpqgg gkvvsvqaas vpiecsqrsa qelpqveays psacsvrgge elvltgsnfl
      601 pdskvvfier gpdgklqwee eatvnrlqsn evtltltvpe ysnkrvsrpv qvyfyvsngr
      661 rkrsptqsfr flpvickeep lpdsslrgfp sasatpfgtd mdfspprppy psyphedpac
      721 etpylsegfg ygmpplypqt gpppsyrpgl rmfpetrgtt gcaqppavsf lprpfpsdpy
      781 ggrgssfslg lpfsppapfr ppplpasppl egpfpsqsdv hplpaegynk vgpgygpgeg
      841 apeqeksrgg yssgfrdsvp iqgitleegg cgtggcecec vqeialhvc
//
LOCUS       NP_000159               1580 aa            linear   PRI 27-APR-2025
DEFINITION  transcriptional activator GLI3 [Homo sapiens].
ACCESSION   NP_000159
VERSION     NP_000159.3
DBSOURCE    REFSEQ: accession NM_000168.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1580)
  AUTHORS   Wang,R.Y., Xiong,Q., Chang,S.H., Jin,J.Y., Xiang,R., Zeng,L. and
            Yu,F.
  TITLE     Identification of truncated variants in GLI family zinc finger 3
            (GLI3) associated with polydactyly
  JOURNAL   J Orthop Surg Res 19 (1), 449 (2024)
   PUBMED   39080720
  REMARK    GeneRIF: Identification of truncated variants in GLI family zinc
            finger 3 (GLI3) associated with polydactyly.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1580)
  AUTHORS   Yoshida,S., Kawamura,A., Aoki,K., Wiriyasermkul,P., Sugimoto,S.,
            Tomiyoshi,J., Tajima,A., Ishida,Y., Katoh,Y., Tsukada,T.,
            Tsuneoka,Y., Yamada,K., Nagamori,S., Nakayama,K. and Yoshida,K.
  TITLE     Positive regulation of Hedgehog signaling via phosphorylation of
            GLI2/GLI3 by DYRK2 kinase
  JOURNAL   Proc Natl Acad Sci U S A 121 (28), e2320070121 (2024)
   PUBMED   38968120
  REMARK    GeneRIF: Positive regulation of Hedgehog signaling via
            phosphorylation of GLI2/GLI3 by DYRK2 kinase.
REFERENCE   3  (residues 1 to 1580)
  AUTHORS   Nguyen,T.N., Tran,G.S., Hoang,H.D. and Nguyen,L.G.
  TITLE     A novel missense variant located within the zinc finger domain of
            the GLI3 gene was identified in a Vietnamese pedigree with index
            finger polydactyly
  JOURNAL   Mol Genet Genomic Med 12 (6), e2468 (2024)
   PUBMED   38864382
  REMARK    GeneRIF: A novel missense variant located within the zinc finger
            domain of the GLI3 gene was identified in a Vietnamese pedigree
            with index finger polydactyly.
REFERENCE   4  (residues 1 to 1580)
  AUTHORS   Pagnamenta,A.T., Yu,J., Evans,J., Twiss,P., Offiah,A.C., Wafik,M.,
            Mehta,S.G., Javaid,M.K., Smithson,S.F. and Taylor,J.C.
  CONSRTM   Genomics England Research Consortium; Musculoskeletal GeCIP MDT
  TITLE     Conclusion of diagnostic odysseys due to inversions disrupting GLI3
            and FBN1
  JOURNAL   J Med Genet 60 (5), 505-510 (2023)
   PUBMED   36411030
  REMARK    GeneRIF: Conclusion of diagnostic odysseys due to inversions
            disrupting GLI3 and FBN1.
REFERENCE   5  (residues 1 to 1580)
  AUTHORS   Scott,D.A.
  TITLE     Esophageal Atresia / Tracheoesophageal Fistula Overview - RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301753
REFERENCE   6  (residues 1 to 1580)
  AUTHORS   Biesecker,L.G.
  TITLE     GLI3-Related Pallister-Hall Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301638
REFERENCE   7  (residues 1 to 1580)
  AUTHORS   Biesecker,L.G. and Johnston,J.J.
  TITLE     Greig Cephalopolysyndactyly Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301619
REFERENCE   8  (residues 1 to 1580)
  AUTHORS   Pettigrew,A.L., Greenberg,F., Caskey,C.T. and Ledbetter,D.H.
  TITLE     Greig syndrome associated with an interstitial deletion of 7p:
            confirmation of the localization of Greig syndrome to 7p13
  JOURNAL   Hum Genet 87 (4), 452-456 (1991)
   PUBMED   1879832
REFERENCE   9  (residues 1 to 1580)
  AUTHORS   Ruppert,J.M., Vogelstein,B., Arheden,K. and Kinzler,K.W.
  TITLE     GLI3 encodes a 190-kilodalton protein with multiple regions of GLI
            similarity
  JOURNAL   Mol Cell Biol 10 (10), 5408-5415 (1990)
   PUBMED   2118997
REFERENCE   10 (residues 1 to 1580)
  AUTHORS   Ruppert,J.M., Kinzler,K.W., Wong,A.J., Bigner,S.H., Kao,F.T.,
            Law,M.L., Seuanez,H.N., O'Brien,S.J. and Vogelstein,B.
  TITLE     The GLI-Kruppel family of human genes
  JOURNAL   Mol Cell Biol 8 (8), 3104-3113 (1988)
   PUBMED   2850480
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005158.3, AI863961.1,
            BC113616.1, AA330409.1, DA713549.1, AC005028.2 and BI497308.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 14, 2006 this sequence version replaced NP_000159.2.
            
            Summary: This gene encodes a protein which belongs to the C2H2-type
            zinc finger proteins subclass of the Gli family. They are
            characterized as DNA-binding transcription factors and are
            mediators of Sonic hedgehog (Shh) signaling. The protein encoded by
            this gene localizes in the cytoplasm and activates patched
            Drosophila homolog (PTCH) gene expression. It is also thought to
            play a role during embryogenesis. Mutations in this gene have been
            associated with several diseases, including Greig
            cephalopolysyndactyly syndrome, Pallister-Hall syndrome, preaxial
            polydactyly type IV, and postaxial polydactyly types A1 and B.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2192517.1,
                                           SRR14038194.3922560.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395925.8/ ENSP00000379258.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1580
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.1"
     Protein         1..1580
                     /product="transcriptional activator GLI3"
                     /note="zinc finger protein GLI3; glioma-associated
                     oncogene family zinc finger 3; GLI-Kruppel family member
                     GLI3; oncogene GLI3"
                     /calculated_mol_wt=169733
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10071.6)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P10071.6)"
     Site            175
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61602; propagated from
                     UniProtKB/Swiss-Prot (P10071.6)"
     Region          368..475
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10071.6)"
     Site            order(525,527,529,531..532,535..536,539,555,557,561..562,
                     565..566,569,585,587,589,591..592,595..596,600)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <542..632
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          548..570
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          578..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          609..630
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          620..728
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10071.6)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P10071.6)"
     Region          745..845
                     /region_name="Mediates interaction with DZIP1.
                     /evidence=ECO:0000250|UniProtKB:Q61602"
                     /note="propagated from UniProtKB/Swiss-Prot (P10071.6)"
     Site            849
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10693759; propagated from
                     UniProtKB/Swiss-Prot (P10071.6)"
     Region          863..918
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10071.6)"
     Site            865
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10693759; propagated from
                     UniProtKB/Swiss-Prot (P10071.6)"
     Site            877
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10693759; propagated from
                     UniProtKB/Swiss-Prot (P10071.6)"
     Site            907
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10693759; propagated from
                     UniProtKB/Swiss-Prot (P10071.6)"
     Site            980
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10693759; propagated from
                     UniProtKB/Swiss-Prot (P10071.6)"
     Region          981..1042
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10071.6)"
     Site            1006
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10693759; propagated from
                     UniProtKB/Swiss-Prot (P10071.6)"
     CDS             1..1580
                     /gene="GLI3"
                     /gene_synonym="ACLS; GCPS; GLI3-190; GLI3FL; PAP-A; PAPA;
                     PAPA1; PAPB; PHS; PPDIV"
                     /coded_by="NM_000168.6:282..5024"
                     /db_xref="CCDS:CCDS5465.1"
                     /db_xref="GeneID:2737"
                     /db_xref="HGNC:HGNC:4319"
                     /db_xref="MIM:165240"
ORIGIN      
        1 meaqshsstt tekkkvensi vkcstrtdvs ekavasstts nedespgqty hrerrnaitm
       61 qpqnvqglsk vseepstssd eraslikkei hgslphvaep svpyrgtvfa mdprngymep
      121 hyhpphlfpa fhppvpidar hhegryhydp spipplhmts alsssptypd lpfirisphr
      181 nptaasespf spphpyinpy mdyirslhss pslsmisatr glsptdapha gvspaeyyhq
      241 malltgqrsp yadiipsaat agtgaihmey lhamdstrfs sprlsarpsr krtlsispls
      301 dhsfdlqtmi rtspnslvti lnnsrssssa sgsyghlsas aispalsfty ssapvslhmh
      361 qqilsrqqsl gsafghsppl ihpaptfptq rpipgiptvl npvqvssgps essqnkptse
      421 savsstgdpm hnkrskikpd edlpspgarg qqeqpegttl vkeegdkdes kqepeviyet
      481 nchwegcare fdtqeqlvhh inndhihgek kefvcrwldc sreqkpfkaq ymlvvhmrrh
      541 tgekphkctf egctkaysrl enlkthlrsh tgekpyvceh egcnkafsna sdrakhqnrt
      601 hsnekpyvck ipgctkrytd psslrkhvkt vhgpeahvtk kqrgdihprp ppprdsgshs
      661 qsrspgrptq galgeqqdls nttskreecl qvktvkaekp mtsqpspggq sscssqqspi
      721 snysnsglel pltdggsigd lsaidetpim dstistatta lalqarrnpa gtkwmehvkl
      781 erlkqvngmf prlnpilppk apavsplign gtqsnntcsl ggpmtllpgr sdlsgvdvtm
      841 lnmlnrrdss astissayls srrssgispc fssrrsseas qaegrpqnvs vadsydpist
      901 dasrrsseas qsdglpslls ltpaqqyrlk akyaaatggp pptplpnmer mslktrlall
      961 gdalepgval ppvhaprrcs dggahgygrr hlqphdapgh gvrrasdpvr tgseglalpr
     1021 vprfsslssc nppamatsae krslvlqnyt rpeggqsrnf hsspcppsit envtlesltm
     1081 dadanlnded flpddvvqyl nsqnqagyeq hfpsalpdds kvphgpgdfd apglpdshag
     1141 qqfhaleqpc pegsktdlpi qwnevssgsa dlsssklkcg prpavpqtra fgfcngmvvh
     1201 pqnplrsgpa ggyqtlgens npyggpehlm lhnspgsgts gnafheqpck apqygnclnr
     1261 qpvapgaldg acgagiqask lkstpmqgsg gqlnfglpva pnesagsmvn gmqnqdpvgq
     1321 gylahqllgd smqhpgagrp gqqmlgqisa tshiniyqgp esclpgahgm gsqpsslavv
     1381 rgyqpcasfg gsrrqamprd slalqsgqls dtsqtcrvng ikmemkgqph plcsnlqnys
     1441 gqfydqtvgf sqqdtkagsf sisdascllq gtsaknsell spganqvtst vdsldshdle
     1501 gvqidfdaii ddgdhsslms galspsiiqn lshsssrltt praslpfpal smsttnmaig
     1561 dmsslltsla eeskflavmq
//
LOCUS       NP_001138632             284 aa            linear   PRI 27-APR-2025
DEFINITION  tropomyosin alpha-4 chain isoform Tpm4.1cy [Homo sapiens].
ACCESSION   NP_001138632
VERSION     NP_001138632.1
DBSOURCE    REFSEQ: accession NM_001145160.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Yan,J., Xie,B., Tian,Y., An,W., Peng,Z., Liu,Z., Li,J. and Li,L.
  TITLE     MicroRNA-5195-3p mediated malignant biological behaviour of
            insulin-resistant liver cancer cells via SOX9 and TPM4
  JOURNAL   BMC Cancer 23 (1), 557 (2023)
   PUBMED   37328795
  REMARK    GeneRIF: MicroRNA-5195-3p mediated malignant biological behaviour
            of insulin-resistant liver cancer cells via SOX9 and TPM4.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Guo,Q., Zhao,L., Yan,N., Li,Y., Guo,C., Dang,S., Shen,X., Han,J.
            and Luo,Y.
  TITLE     Integrated pan-cancer analysis and experimental verification of the
            roles of tropomyosin 4 in gastric cancer
  JOURNAL   Front Immunol 14, 1148056 (2023)
   PUBMED   36993958
  REMARK    GeneRIF: Integrated pan-cancer analysis and experimental
            verification of the roles of tropomyosin 4 in gastric cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Luo,A., Lan,X., Qiu,Q., Zhou,Q., Li,J., Wu,M., Liu,P., Zhang,H.,
            Lu,B., Lu,Y. and Lu,W.
  TITLE     LncRNA SFTA1P promotes cervical cancer progression by interaction
            with PTBP1 to facilitate TPM4 mRNA degradation
  JOURNAL   Cell Death Dis 13 (11), 936 (2022)
   PUBMED   36344495
  REMARK    GeneRIF: LncRNA SFTA1P promotes cervical cancer progression by
            interaction with PTBP1 to facilitate TPM4 mRNA degradation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Marin-Quilez,A., Vuelta,E., Diaz-Ajenjo,L., Fernandez-Infante,C.,
            Garcia-Tunon,I., Benito,R., Palma-Barqueros,V.,
            Hernandez-Rivas,J.M., Gonzalez-Porras,J.R., Rivera,J. and
            Bastida,J.M.
  TITLE     A novel nonsense variant in TPM4 caused dominant
            macrothrombocytopenia, mild bleeding tendency and disrupted
            cytoskeleton remodeling
  JOURNAL   J Thromb Haemost 20 (5), 1248-1255 (2022)
   PUBMED   35170221
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Stapley,R.J., Poulter,N.S., Khan,A.O., Smith,C.W., Bignell,P.,
            Fratter,C., Lester,W., Lowe,G. and Morgan,N.V.
  CONSRTM   UK GAPP Study Group
  TITLE     Rare missense variants in Tropomyosin-4 (TPM4) are associated with
            platelet dysfunction, cytoskeletal defects, and excessive bleeding
  JOURNAL   J Thromb Haemost 20 (2), 478-485 (2022)
   PUBMED   34758189
  REMARK    GeneRIF: Rare missense variants in Tropomyosin-4 (TPM4) are
            associated with platelet dysfunction, cytoskeletal defects, and
            excessive bleeding.
            Erratum:[J Thromb Haemost. 2022 Jun;20(6):1511. doi:
            10.1111/jth.15719. PMID: 35596517]
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Crabos,M., Yamakado,T., Heizmann,C.W., Cerletti,N., Buhler,F.R. and
            Erne,P.
  TITLE     The calcium binding protein tropomyosin in human platelets and
            cardiac tissue: elevation in hypertensive cardiac hypertrophy
  JOURNAL   Eur J Clin Invest 21 (5), 472-478 (1991)
   PUBMED   1836432
REFERENCE   9  (residues 1 to 284)
  AUTHORS   MacLeod,A.R., Talbot,K., Smillie,L.B. and Houlker,C.
  TITLE     Characterization of a cDNA defining a gene family encoding TM30p1,
            a human fibroblast tropomyosin
  JOURNAL   J Mol Biol 194 (1), 1-10 (1987)
   PUBMED   3612796
REFERENCE   10 (residues 1 to 284)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK023385.1 and AC008894.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins involved in the contractile system of
            striated and smooth muscles and the cytoskeleton of non-muscle
            cells. Tropomyosins are dimers of coiled-coil proteins that
            polymerize end-to-end along the major groove in most actin
            filaments. They provide stability to the filaments and regulate
            access of other actin-binding proteins. In muscle cells, they
            regulate muscle contraction by controlling the binding of myosin
            heads to the actin filament. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2009].
            
            Transcript Variant: This variant (Tpm4.1, also known as variant 1)
            encodes the longest isoform (Tpm4.1cy, also known as isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.83329.1,
                                           SRR3476690.71877.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12-p13.11"
     Protein         1..284
                     /product="tropomyosin alpha-4 chain isoform Tpm4.1cy"
                     /note="tropomyosin alpha-4 chain; TM30p1; epididymis
                     secretory protein Li 108"
                     /calculated_mol_wt=32592
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="TPM4"
                     /gene_synonym="BDPLT25; HEL-S-108"
                     /coded_by="NM_001145160.2:88..942"
                     /note="isoform Tpm4.1cy is encoded by transcript variant
                     2"
                     /db_xref="CCDS:CCDS46007.1"
                     /db_xref="GeneID:7171"
                     /db_xref="HGNC:HGNC:12013"
                     /db_xref="MIM:600317"
ORIGIN      
        1 meaikkkmqm lkldkenaid raeqaeadkk aaedkckqve eelthlqkkl kgtedeldky
       61 sedlkdaqek leltekkasd aegdvaalnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi enramkdeek meiqemqlke akhiaeeadr kyeevarklv ilegelerae
      181 eraevselkc gdleeelknv tnnlksleaa sekysekedk yeeeikllsd klkeaetrae
      241 faertvakle ktiddleekl aqakeenvgl hqtldqtlne lnci
//
LOCUS       NP_808587                200 aa            linear   ROD 27-APR-2025
DEFINITION  transcription elongation factor A protein-like 5 [Mus musculus].
ACCESSION   NP_808587 XP_284745
VERSION     NP_808587.1
DBSOURCE    REFSEQ: accession NM_177919.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Sawada,A., Yamamoto,T. and Sato,T.
  TITLE     Tceal5 and Tceal7 Function in C2C12 Myogenic Differentiation via
            Exosomes in Fetal Bovine Serum
  JOURNAL   Int J Mol Sci 23 (4), 2036 (2022)
   PUBMED   35216152
  REMARK    GeneRIF: Tceal5 and Tceal7 Function in C2C12 Myogenic
            Differentiation via Exosomes in Fetal Bovine Serum.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Navas-Perez,E., Vicente-Garcia,C., Mirra,S., Burguera,D.,
            Fernandez-Castillo,N., Ferran,J.L., Lopez-Mayorga,M.,
            Alaiz-Noya,M., Suarez-Pereira,I., Anton-Galindo,E., Ulloa,F.,
            Herrera-Ubeda,C., Cusco,P., Falcon-Moya,R., Rodriguez-Moreno,A.,
            D'Aniello,S., Cormand,B., Marfany,G., Soriano,E., Carrion,A.M.,
            Carvajal,J.J. and Garcia-Fernandez,J.
  TITLE     Characterization of an eutherian gene cluster generated after
            transposon domestication identifies Bex3 as relevant for advanced
            neurological functions
  JOURNAL   Genome Biol 21 (1), 267 (2020)
   PUBMED   33100228
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Gergics,P., Christian,H.C., Choo,M.S., Ajmal,A. and Camper,S.A.
  TITLE     Gene Expression in Mouse Thyrotrope Adenoma: Transcription
            Elongation Factor Stimulates Proliferation
  JOURNAL   Endocrinology 157 (9), 3631-3646 (2016)
   PUBMED   27580811
  REMARK    GeneRIF: sufficient to increase the growth rate of pituitary
            progenitors, suggesting a role as a proto-oncogene
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY245586.1, AK032140.1 and BE991033.1.
            
            On Aug 30, 2004 this sequence version replaced XP_284745.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.4869209.1,
                                           SRR7345562.3471595.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849378, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="X"
                     /map="X 57.4 cM"
     Protein         1..200
                     /product="transcription elongation factor A protein-like
                     5"
                     /note="TCEA-like protein 5; transcription elongation
                     factor S-II protein-like 5"
                     /calculated_mol_wt=21907
     Region          1..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CCT4.1)"
     Region          <6..>151
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          80..174
                     /region_name="BEX"
                     /note="Brain expressed X-linked like family; pfam04538"
                     /db_xref="CDD:461346"
     CDS             1..200
                     /gene="Tceal5"
                     /gene_synonym="6430401A05Rik"
                     /coded_by="NM_177919.3:213..815"
                     /db_xref="CCDS:CCDS30416.1"
                     /db_xref="GeneID:331532"
                     /db_xref="MGI:MGI:3036236"
ORIGIN      
        1 mekfykeneg kpenkgraed egsteeggka dedksdaegk parqgkleve ggpgeqaqqk
       61 gegkpekqgk sdgegkrqge skpdsqaksa searaaekrp aedyvprkak rktdrgtdds
      121 pknsqedlqd rhvsseemmr ecadmtraqe elrkrqkmgg fhwvprdaqd alvprgqrgv
      181 rgvrggggrg qkdledapfv
//
LOCUS       NP_001138531             148 aa            linear   PRI 27-APR-2025
DEFINITION  IQ domain-containing protein F5 [Homo sapiens].
ACCESSION   NP_001138531 XP_001723415 XP_371643 XP_947645
VERSION     NP_001138531.1
DBSOURCE    REFSEQ: accession NM_001145059.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Xie,T., Deng,L., Mei,P., Zhou,Y., Wang,B., Zhang,J., Lin,J.,
            Wei,Y., Zhang,X. and Xu,R.
  TITLE     Genome-wide association study combining pathway analysis for
            typical sporadic amyotrophic lateral sclerosis in Chinese Han
            populations
  JOURNAL   Neurobiol Aging 35 (7), 1778 (2014)
   PUBMED   24529757
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Muzny,D.M., Scherer,S.E., Kaul,R., Wang,J., Yu,J., Sudbrak,R.,
            Buhay,C.J., Chen,R., Cree,A., Ding,Y., Dugan-Rocha,S., Gill,R.,
            Gunaratne,P., Harris,R.A., Hawes,A.C., Hernandez,J., Hodgson,A.V.,
            Hume,J., Jackson,A., Khan,Z.M., Kovar-Smith,C., Lewis,L.R.,
            Lozado,R.J., Metzker,M.L., Milosavljevic,A., Miner,G.R.,
            Morgan,M.B., Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z.,
            Steffen,D., Wei,S., Wheeler,D.A., Wright,M.W., Worley,K.C.,
            Yuan,Y., Zhang,Z., Adams,C.Q., Ansari-Lari,M.A., Ayele,M.,
            Brown,M.J., Chen,G., Chen,Z., Clendenning,J.,
            Clerc-Blankenburg,K.P., Chen,R., Chen,Z., Davis,C., Delgado,O.,
            Dinh,H.H., Dong,W., Draper,H., Ernst,S., Fu,G.,
            Gonzalez-Garay,M.L., Garcia,D.K., Gillett,W., Gu,J., Hao,B.,
            Haugen,E., Havlak,P., He,X., Hennig,S., Hu,S., Huang,W.,
            Jackson,L.R., Jacob,L.S., Kelly,S.H., Kube,M., Levy,R., Li,Z.,
            Liu,B., Liu,J., Liu,W., Lu,J., Maheshwari,M., Nguyen,B.V.,
            Okwuonu,G.O., Palmeiri,A., Pasternak,S., Perez,L.M., Phelps,K.A.,
            Plopper,F.J., Qiang,B., Raymond,C., Rodriguez,R.,
            Saenphimmachak,C., Santibanez,J., Shen,H., Shen,Y., Subramanian,S.,
            Tabor,P.E., Verduzco,D., Waldron,L., Wang,J., Wang,J., Wang,Q.,
            Williams,G.A., Wong,G.K., Yao,Z., Zhang,J., Zhang,X., Zhao,G.,
            Zhou,J., Zhou,Y., Nelson,D., Lehrach,H., Reinhardt,R., Naylor,S.L.,
            Yang,H., Olson,M., Weinstock,G. and Gibbs,R.A.
  TITLE     The DNA sequence, annotation and analysis of human chromosome 3
  JOURNAL   Nature 440 (7088), 1194-1198 (2006)
   PUBMED   16641997
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC097636.2, BX106781.1 and AW138546.1.
            
            On or before Feb 9, 2009 this sequence version replaced
            XP_947645.1, XP_001723415.1, XP_371643.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX106781.1, SRR5189667.312543.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000446461.2/ ENSP00000394653.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..148
                     /product="IQ domain-containing protein F5"
                     /calculated_mol_wt=17917
     Region          4..>29
                     /region_name="IQCG-IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing G and D
                     (IQCG and IQCD); cl49618"
                     /db_xref="CDD:483958"
     CDS             1..148
                     /gene="IQCF5"
                     /coded_by="NM_001145059.2:71..517"
                     /db_xref="CCDS:CCDS46838.1"
                     /db_xref="GeneID:389124"
                     /db_xref="HGNC:HGNC:35159"
ORIGIN      
        1 mgpeektimt ersaavfiqa wwrgmlvrrt llhaalrawi iqcwwrqvle kllakrrrmv
       61 lefyvqqewa avrlqswvrm wcvrqrycrl lnavriiqvy wrwhschsrv fieghyelke
      121 nqlniqleis lglqackvqq ciplplke
//
LOCUS       NP_612358                393 aa            linear   PRI 27-APR-2025
DEFINITION  tumor protein p53-inducible protein 13 isoform a precursor [Homo
            sapiens].
ACCESSION   NP_612358
VERSION     NP_612358.3
DBSOURCE    REFSEQ: accession NM_138349.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Hata,T., Ogawa,T., Yokoyama,T.A., Fukushige,S., Horii,A. and
            Furukawa,T.
  TITLE     DSCP1, a novel TP53-inducible gene, is upregulated by strong
            genotoxic stresses and its overexpression inhibits tumor cell
            growth in vitro
  JOURNAL   Int J Oncol 24 (3), 513-520 (2004)
   PUBMED   14767535
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL551604.3 and BC001593.2.
            
            On Sep 15, 2006 this sequence version replaced NP_612358.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.557732.1, AB110209.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301057.8/ ENSP00000301057.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..393
                     /product="tumor protein p53-inducible protein 13 isoform a
                     precursor"
                     /note="damage-stimulated cytoplasmic protein 1"
                     /calculated_mol_wt=39502
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2754
     mat_peptide     28..393
                     /product="Tumor protein p53-inducible protein 13.
                     /id=PRO_0000333824"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBR0.1)"
                     /calculated_mol_wt=39502
     Region          184..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBR0.1)"
     Site            310..330
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBR0.1)"
     Region          366..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBR0.1)"
     CDS             1..393
                     /gene="TP53I13"
                     /gene_synonym="DSCP1"
                     /coded_by="NM_138349.4:59..1240"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS42289.1"
                     /db_xref="GeneID:90313"
                     /db_xref="HGNC:HGNC:25102"
ORIGIN      
        1 mappppspql lllaalarll gpsevmagpa eeagahcpes lwplppqvsp rvtytrvspg
       61 qaedvtflyh pcahpwlklq lallayacma npsltpdfsl tqdrplvlta wglalemawv
      121 epawaahwlm rrrrrkqrkk kawiycesls gpapseptpg rgrlcrrgcv qalalafalr
      181 swrppgtevt sqgprqpsss gakrrrlraa lgpqptrsal rfpsaspgsl kakqsmagip
      241 gresnapsvp tvsllpgapg gnassrteaq vpngqgspgg cvcssqaspa praaappraa
      301 rgptprteea awaamaltfl lvlltlatlc trlhrnfrrg esiywgptad sqdtvaavlk
      361 rrllqpsrrv krsrrrpllp ptpdsgpege sse
//
LOCUS       NP_008840               1237 aa            linear   PRI 27-APR-2025
DEFINITION  ras-specific guanine nucleotide-releasing factor 2 [Homo sapiens].
ACCESSION   NP_008840 XP_027943
VERSION     NP_008840.1
DBSOURCE    REFSEQ: accession NM_006909.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1237)
  AUTHORS   Lin,Q., Qiu,M., Wei,X., Xiang,Z., Zhou,Z., Ji,I., Liang,X.,
            Zhou,X., Wen,Q., Liu,Y. and Yu,H.
  TITLE     Genetic variants of SOS2, MAP2K1 and RASGRF2 in the RAS pathway
            genes predict survival of HBV-related hepatocellular carcinoma
            patients
  JOURNAL   Arch Toxicol 97 (6), 1599-1611 (2023)
   PUBMED   37029817
  REMARK    GeneRIF: Genetic variants of SOS2, MAP2K1 and RASGRF2 in the RAS
            pathway genes predict survival of HBV-related hepatocellular
            carcinoma patients.
REFERENCE   2  (residues 1 to 1237)
  AUTHORS   Korolkova,O.Y., Widatalla,S.E., Whalen,D.S., Nangami,G.N.,
            Abimbola,A., Williams,S.D., Beasley,H.K., Reisenbichler,E.,
            Washington,M.K., Ochieng,J., Mayer,I.A., Lehmann,B.D. and
            Sakwe,A.M.
  TITLE     Reciprocal expression of Annexin A6 and RasGRF2 discriminates
            rapidly growing from invasive triple negative breast cancer subsets
  JOURNAL   PLoS One 15 (4), e0231711 (2020)
   PUBMED   32298357
  REMARK    GeneRIF: AnxA6 may be a reliable biomarker for distant relapse-free
            survival and response of triple negative breast cancer (TNBC)
            patients to chemotherapy, and that the reciprocal expression of
            AnxA6 and GRF2 can reliably delineate TNBCs into rapidly growing
            and invasive subsets which may be more relevant for subset-specific
            therapeutic interventions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1237)
  AUTHORS   Lu,P., Chen,J., Yan,L., Yang,L., Zhang,L., Dai,J., Hao,Z., Bai,T.,
            Xi,Y., Li,Y., Kang,Z., Xv,J., Sun,G. and Yang,T.
  TITLE     RasGRF2 promotes migration and invasion of colorectal cancer cells
            by modulating expression of MMP9 through Src/Akt/NF-kappaB pathway
  JOURNAL   Cancer Biol Ther 20 (4), 435-443 (2019)
   PUBMED   30359168
  REMARK    GeneRIF: High RASGRF2 expression is associated with migration and
            invasion of colorectal cancer.
REFERENCE   4  (residues 1 to 1237)
  AUTHORS   Karamitros,T., Hurst,T., Marchi,E., Karamichali,E.,
            Georgopoulou,U., Mentis,A., Riepsaame,J., Lin,A., Paraskevis,D.,
            Hatzakis,A., McLauchlan,J., Katzourakis,A. and Magiorkinis,G.
  TITLE     Human Endogenous Retrovirus-K HML-2 integration within RASGRF2 is
            associated with intravenous drug abuse and modulates transcription
            in a cell-line model
  JOURNAL   Proc Natl Acad Sci U S A 115 (41), 10434-10439 (2018)
   PUBMED   30249655
  REMARK    GeneRIF: RASGRF2-int is significantly associated with drug
            addiction.
REFERENCE   5  (residues 1 to 1237)
  AUTHORS   Novo-Veleiro,I., Cieza-Borrella,C., Pastor,I., Chamorro,A.J.,
            Laso,F.J., Gonzalez-Sarmiento,R. and Marcos,M.
  TITLE     A Single Nucleotide Polymorphism in the RASGRF2 Gene Is Associated
            with Alcoholic Liver Cirrhosis in Men
  JOURNAL   PLoS One 11 (12), e0168685 (2016)
   PUBMED   27992614
  REMARK    GeneRIF: this genetic association study represents the first to
            show an association of the RASGRF2 G>A (rs26907) polymorphism with
            Alcoholic Liver Cirrhosis in men, particularly in the subgroup of
            patients with alcohol dependence. The findings suggest the
            potential relevance of the RAS gene family in alcoholism and
            Alcoholic Liver Cirrhosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1237)
  AUTHORS   Harrington,A.W., Kim,J.Y. and Yoon,S.O.
  TITLE     Activation of Rac GTPase by p75 is necessary for c-jun N-terminal
            kinase-mediated apoptosis
  JOURNAL   J Neurosci 22 (1), 156-166 (2002)
   PUBMED   11756498
REFERENCE   7  (residues 1 to 1237)
  AUTHORS   Anborgh,P.H., Qian,X., Papageorge,A.G., Vass,W.C., DeClue,J.E. and
            Lowy,D.R.
  TITLE     Ras-specific exchange factor GRF: oligomerization through its Dbl
            homology domain and calcium-dependent activation of Raf
  JOURNAL   Mol Cell Biol 19 (7), 4611-4622 (1999)
   PUBMED   10373510
REFERENCE   8  (residues 1 to 1237)
  AUTHORS   Fan,W.T., Koch,C.A., de Hoog,C.L., Fam,N.P. and Moran,M.F.
  TITLE     The exchange factor Ras-GRF2 activates Ras-dependent and
            Rac-dependent mitogen-activated protein kinase pathways
  JOURNAL   Curr Biol 8 (16), 935-938 (1998)
   PUBMED   9707409
REFERENCE   9  (residues 1 to 1237)
  AUTHORS   Fam,N.P., Fan,W.T., Wang,Z., Zhang,L.J., Chen,H. and Moran,M.F.
  TITLE     Cloning and characterization of Ras-GRF2, a novel guanine
            nucleotide exchange factor for Ras
  JOURNAL   Mol Cell Biol 17 (3), 1396-1406 (1997)
   PUBMED   9032266
REFERENCE   10 (residues 1 to 1237)
  AUTHORS   Fam,N.P., Zhang,L.J., Rommens,J.M., Beatty,B.G. and Moran,M.F.
  TITLE     Mapping of the Ras-GRF2 gene (GRF2) to mouse chromosome 13C3-D1 and
            human chromosome 5q13, near the Ras-GAP gene
  JOURNAL   Genomics 39 (1), 118-120 (1997)
   PUBMED   9027497
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026427.4, BC136296.1,
            DA219722.1, DA230428.1, BX502901.1, BU430075.1, CR749239.1 and
            BC041953.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 18, 2003 this sequence version replaced XP_027943.2.
            
            Summary: RAS GTPases cycle between an inactive GDP-bound state and
            an active GTP-bound state. This gene encodes a calcium-regulated
            nucleotide exchange factor activating both RAS and RAS-related
            protein, RAC1, through the exchange of bound GDP for GTP, thereby,
            coordinating the signaling of distinct mitogen-activated protein
            kinase pathways. [provided by RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.174237.1,
                                           SRR1803614.86111.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265080.9/ ENSP00000265080.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..1237
                     /product="ras-specific guanine nucleotide-releasing factor
                     2"
                     /note="ras guanine nucleotide exchange factor 2"
                     /calculated_mol_wt=140634
     Region          19..158
                     /region_name="PH_RasGRF1_2"
                     /note="Ras-specific guanine nucleotide-releasing factors 1
                     and 2 Pleckstrin homology (PH) domain; cd13261"
                     /db_xref="CDD:270081"
     Region          247..428
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; smart00325"
                     /db_xref="CDD:214619"
     Site            order(250,254,351,378..379,382..383,385..386,389..390,
                     393..394,397,423)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          480..588
                     /region_name="PH"
                     /note="Pleckstrin homology domain; smart00233"
                     /db_xref="CDD:214574"
     Region          638..>686
                     /region_name="RasGEF_N"
                     /note="RasGEF N-terminal motif; pfam00618"
                     /db_xref="CDD:459873"
     Region          710..809
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14827.2)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70392; propagated from
                     UniProtKB/Swiss-Prot (O14827.2)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70392; propagated from
                     UniProtKB/Swiss-Prot (O14827.2)"
     Site            737
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5.
                     /evidence=ECO:0000269|PubMed:15128856; propagated from
                     UniProtKB/Swiss-Prot (O14827.2)"
     Region          744..752
                     /region_name="Regulates proteasomal degradation.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O14827.2)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O14827.2)"
     Region          829..873
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14827.2)"
     Site            848
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70392; propagated from
                     UniProtKB/Swiss-Prot (O14827.2)"
     Site            852
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70392; propagated from
                     UniProtKB/Swiss-Prot (O14827.2)"
     Region          <901..972
                     /region_name="REM"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     GTPases; N-terminal domain (RasGef_N), also called REM
                     domain (Ras exchanger motif). This domain is common in
                     nucleotide exchange factors for Ras-like small GTPases and
                     is typically found immediately...; cl02520"
                     /db_xref="CDD:470601"
     Site            972
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70392; propagated from
                     UniProtKB/Swiss-Prot (O14827.2)"
     Region          998..1234
                     /region_name="RasGEF"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     small GTPases; smart00147"
                     /db_xref="CDD:214539"
     Site            order(1031..1033,1043..1044,1046..1048,1050..1051,
                     1054..1055,1058,1091,1094..1095,1097..1099,1101..1104,
                     1106..1107,1127,1130,1135..1137,1140,1153..1155,
                     1158..1160,1162..1164,1166..1169,1184,1188,1222,
                     1225..1226)
                     /site_type="other"
                     /note="Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:238087"
     Region          1099..1128
                     /region_name="Responsible of the affinity for farnesylated
                     versus geranylgeranylated Ras. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O14827.2)"
     CDS             1..1237
                     /gene="RASGRF2"
                     /gene_synonym="GRF2; RAS-GRF2"
                     /coded_by="NM_006909.3:377..4090"
                     /db_xref="CCDS:CCDS4052.1"
                     /db_xref="GeneID:5924"
                     /db_xref="HGNC:HGNC:9876"
                     /db_xref="MIM:606614"
ORIGIN      
        1 mqksvryneg halylaflar kegtkrgfls kktaeasrwh ekwfalyqnv lfyfegeqsc
       61 rpagmylleg cscertpapp ragagqggvr daldkqyyft vlfghegqkp lelrceeeqd
      121 gkewmeaihq asyadilier evlmqkyihl vqivetekia anqlrhqled qdteierlks
      181 eiialnktke rmrpyqsnqe dedpdikkik kvqsfmrgwl crrkwktivq dyicsphaes
      241 mrkrnqivft mveaeseyvh qlyilvngfl rplrmaassk kppishddvs siflnsetim
      301 flheifhqgl karianwptl iladlfdill pmlniyqefv rnhqyslqvl anckqnrdfd
      361 kllkqyeanp acegrmletf ltypmfqipr yiitlhella htphehverk slefakskle
      421 elsrvmhdev sdtenirknl aiermivegc dilldtsqtf irqgsliqvp svergklskv
      481 rlgslslkke gerqcflftk hflictrssg gklhllktgg vlslidctli eepdasddds
      541 kgsgqvfghl dfkivveppd aaaftvvlla psrqekaawm sdisqcvdni rcnglmtivf
      601 eenskvtvph miksdarlhk ddtdicfskt lnsckvpqir yasverller ltdlrflsid
      661 flntflhtyr ifttaavvlg klsdiykrpf tsipvrslel ffatsqnnrg ehlvdgkspr
      721 lcrkfssppp lavsrtsspv rarklsltsp lnskigaldl ttsssptttt qspaasppph
      781 tgqipldlsr glsspeqspg tveenvdnpr vdlcnklkrs iqkavlesap adragvessp
      841 aadttelspc rspstprhlr yrqpggqtad nahcsvspas afaiataaag hgsppgfnnt
      901 ertcdkefii rrtatnrvln vlrhwvskha qdfelnnelk mnvlnlleev lrdpdllpqe
      961 rkaaanilra lsqddqddih lklediiqmt dcmkaecfes lsamelaeqi tlldhvifrs
     1021 ipyeeflgqg wmkldknert pyimktsqhf ndmsnlvasq imnyadvssr anaiekwvav
     1081 adicrclhny ngvleitsal nrsaiyrlkk twakvskqtk almdklqktv ssegrfknlr
     1141 etlkncnppa vpylgmyltd lafieegtpn fteeglvnfs kmrmishiir eirqfqqtsy
     1201 ridhqpkvaq ylldkdliid edtlyelslk ieprlpa
//
LOCUS       NP_065189                196 aa            linear   PRI 27-APR-2025
DEFINITION  SPRY domain-containing protein 7 isoform 1 [Homo sapiens].
ACCESSION   NP_065189
VERSION     NP_065189.1
DBSOURCE    REFSEQ: accession NM_020456.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Montero-Calle,A., Jimenez de Ocana,S., Benavente-Naranjo,R.,
            Rejas-Gonzalez,R., Bartolome,R.A., Martinez-Useros,J., Sanz,R.,
            Dziakova,J., Fernandez-Acenero,M.J., Mendiola,M., Casal,J.I.,
            Pelaez-Garcia,A. and Barderas,R.
  TITLE     Functional Proteomics Characterization of the Role of SPRYD7 in
            Colorectal Cancer Progression and Metastasis
  JOURNAL   Cells 12 (21), 2548 (2023)
   PUBMED   37947626
  REMARK    GeneRIF: Functional Proteomics Characterization of the Role of
            SPRYD7 in Colorectal Cancer Progression and Metastasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Mertens,D., Wolf,S., Schroeter,P., Schaffner,C., Dohner,H.,
            Stilgenbauer,S. and Lichter,P.
  TITLE     Down-regulation of candidate tumor suppressor genes within
            chromosome band 13q14.3 is independent of the DNA methylation
            pattern in B-cell chronic lymphocytic leukemia
  JOURNAL   Blood 99 (11), 4116-4121 (2002)
   PUBMED   12010815
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Tiazhelova,T.V., Ivanov,D.V., Makeeva,N.V., Kapanadze,B.I.,
            Nikitin,E.A., Semov,A.B., Sangfeldt,O., Grander,D., Vorob'ev,A.I.,
            Einhorn,S., Iankovskii,N.K. and Baranova,A.V.
  TITLE     [Transcription map of the 13q14 region, frequently deleted in
            B-cell chronic lymphocytic leukemia patients]
  JOURNAL   Genetika 37 (11), 1530-1537 (2001)
   PUBMED   11771308
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Mabuchi,H., Fujii,H., Calin,G., Alder,H., Negrini,M., Rassenti,L.,
            Kipps,T.J., Bullrich,F. and Croce,C.M.
  TITLE     Cloning and characterization of CLLD6, CLLD7, and CLLD8, novel
            candidate genes for leukemogenesis at chromosome 13q14, a region
            commonly deleted in B-cell chronic lymphocytic leukemia
  JOURNAL   Cancer Res 61 (7), 2870-2877 (2001)
   PUBMED   11306461
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN992366.1, AF055016.1, BC022519.1, AF334405.1 and BM684781.1.
            
            Transcript Variant: This variant (1) encodes the predicted full
            length protein isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF334405.1, SRR3476690.587712.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361840.8/ ENSP00000354774.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..196
                     /product="SPRY domain-containing protein 7 isoform 1"
                     /note="chronic lymphocytic leukemia deletion region gene 6
                     protein; CLL deletion region gene 6 protein; SPRY
                     domain-containing protein 7; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=21535
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q5W111.2)"
     Region          35..196
                     /region_name="SPRYD7"
                     /note="SPRY domain-containing protein 7; cd12880"
                     /db_xref="CDD:293938"
     CDS             1..196
                     /gene="SPRYD7"
                     /gene_synonym="C13orf1; CLLD6"
                     /coded_by="NM_020456.4:106..696"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9422.1"
                     /db_xref="GeneID:57213"
                     /db_xref="HGNC:HGNC:14297"
                     /db_xref="MIM:607866"
ORIGIN      
        1 matsvlcclr ccrdggtghi plkempavql dtqhmgtdvv ivkngrricg tggclasapl
       61 hqnksyfefk iqstgiwgig vatqkvnlnq iplgrdmhsl vmrndgalyh nneeknrlpa
      121 nslpqegdvv gitydhveln vylngknmhc pasgirgtvy pvvyvddsai ldcqfsefyh
      181 tpppgfekil feqqif
//
LOCUS       NP_001269251             300 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF212B [Homo sapiens].
ACCESSION   NP_001269251 XP_003118966 XP_003119614 XP_003960596
VERSION     NP_001269251.1
DBSOURCE    REFSEQ: accession NM_001282322.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Gershoni,M., Braun,T., Hauser,R., Barda,S., Lehavi,O., Malcov,M.,
            Frumkin,T., Kalma,Y., Pietrokovski,S., Arama,E. and Kleiman,S.E.
  TITLE     A pathogenic variant in the uncharacterized RNF212B gene results in
            severe aneuploidy male infertility and repeated IVF failure
  JOURNAL   HGG Adv 4 (3), 100189 (2023)
   PUBMED   37124137
  REMARK    GeneRIF: A pathogenic variant in the uncharacterized RNF212B gene
            results in severe aneuploidy male infertility and repeated IVF
            failure.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL049829.4.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_003119614.2, XP_003960596.2, XP_003118966.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000430154.7/ ENSP00000397830.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..300
                     /product="E3 ubiquitin-protein ligase RNF212B"
                     /EC_number="2.3.2.27"
                     /note="RING finger protein C14orf164-like"
                     /calculated_mol_wt=33439
     Region          4..40
                     /region_name="RING-HC_RNF212B"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 212B (RNF212B) and similar proteins; cd16747"
                     /db_xref="CDD:438405"
     Region          94..151
                     /region_name="SlyX"
                     /note="pfam04102"
                     /db_xref="CDD:461173"
     Region          141..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A8MTL3.1)"
     CDS             1..300
                     /gene="RNF212B"
                     /gene_synonym="C14orf164"
                     /coded_by="NM_001282322.3:122..1024"
                     /db_xref="CCDS:CCDS61401.1"
                     /db_xref="GeneID:100507650"
                     /db_xref="HGNC:HGNC:20438"
                     /db_xref="MIM:621020"
ORIGIN      
        1 mdwfhcnqcf rkdgahffvt scghifckkc vtlekcavcg tackhlalsd nlkpqekmff
       61 kspvetalqy fshisqvwsf qkkqtdllia fykhritkle tamqeaqqal vsqdkelsvl
      121 rkengelkkf lailkespsr yqgsrsitpr pvgitspsqs vtprpsfqhs sqvvsrsssa
      181 esipyreagf gslgqggrgl qgrrtprdsy netpspasth slsyrtssas sgqgifsfrp
      241 spnghsghtr vltpnnfaqr estttleslp sfqlpvlqtl yqqrrhmglp sgreawttsr
//
LOCUS       NP_114131                343 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 120A isoform 1 [Homo sapiens].
ACCESSION   NP_114131
VERSION     NP_114131.1
DBSOURCE    REFSEQ: accession NM_031925.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Liu,X., Zhang,R., Fatehi,M., Wang,Y., Long,W., Tian,R., Deng,X.,
            Weng,Z., Xu,Q., Light,P.E., Tang,J. and Chen,X.Z.
  TITLE     Regulation of PKD2 channel function by TACAN
  JOURNAL   J Physiol 601 (1), 83-98 (2023)
   PUBMED   36420836
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Chen,X., Wang,Y., Li,Y., Lu,X., Chen,J., Li,M., Wen,T., Liu,N.,
            Chang,S., Zhang,X., Yang,X. and Shen,Y.
  TITLE     Cryo-EM structure of the human TACAN in a closed state
  JOURNAL   Cell Rep 38 (9), 110445 (2022)
   PUBMED   35235791
  REMARK    GeneRIF: Cryo-EM structure of the human TACAN in a closed state.
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Li,S., Qian,N., Jiang,C., Zu,W., Liang,A., Li,M., Elledge,S.J. and
            Tan,X.
  TITLE     Gain-of-function genetic screening identifies the antiviral
            function of TMEM120A via STING activation
  JOURNAL   Nat Commun 13 (1), 105 (2022)
   PUBMED   35013224
  REMARK    GeneRIF: Gain-of-function genetic screening identifies the
            antiviral function of TMEM120A via STING activation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Ke,M., Yu,Y., Zhao,C., Lai,S., Su,Q., Yuan,W., Yang,L., Deng,D.,
            Wu,K., Zeng,W., Geng,J., Wu,J. and Yan,Z.
  TITLE     Cryo-EM structures of human TMEM120A and TMEM120B
  JOURNAL   Cell Discov 7 (1), 77 (2021)
   PUBMED   34465718
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Rong,Y., Jiang,J., Gao,Y., Guo,J., Song,D., Liu,W., Zhang,M.,
            Zhao,Y., Xiao,B. and Liu,Z.
  TITLE     TMEM120A contains a specific coenzyme A-binding site and might not
            mediate poking- or stretch-induced channel activities in cells
  JOURNAL   Elife 10, e71474 (2021)
   PUBMED   34409941
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Beaulieu-Laroche,L., Christin,M., Donoghue,A., Agosti,F.,
            Yousefpour,N., Petitjean,H., Davidova,A., Stanton,C., Khan,U.,
            Dietz,C., Faure,E., Fatima,T., MacPherson,A.,
            Mouchbahani-Constance,S., Bisson,D.G., Haglund,L., Ouellet,J.A.,
            Stone,L.S., Samson,J., Smith,M.J., Ask,K., Ribeiro-da-Silva,A.,
            Blunck,R., Poole,K., Bourinet,E. and Sharif-Naeini,R.
  TITLE     TACAN Is an Ion Channel Involved in Sensing Mechanical Pain
  JOURNAL   Cell 180 (5), 956-967 (2020)
   PUBMED   32084332
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Batrakou,D.G., de Las Heras,J.I., Czapiewski,R., Mouras,R. and
            Schirmer,E.C.
  TITLE     TMEM120A and B: Nuclear Envelope Transmembrane Proteins Important
            for Adipocyte Differentiation
  JOURNAL   PLoS One 10 (5), e0127712 (2015)
   PUBMED   26024229
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Cornelis,M.C., Byrne,E.M., Esko,T., Nalls,M.A., Ganna,A.,
            Paynter,N., Monda,K.L., Amin,N., Fischer,K., Renstrom,F.,
            Ngwa,J.S., Huikari,V., Cavadino,A., Nolte,I.M., Teumer,A., Yu,K.,
            Marques-Vidal,P., Rawal,R., Manichaikul,A., Wojczynski,M.K.,
            Vink,J.M., Zhao,J.H., Burlutsky,G., Lahti,J., Mikkila,V.,
            Lemaitre,R.N., Eriksson,J., Musani,S.K., Tanaka,T., Geller,F.,
            Luan,J., Hui,J., Magi,R., Dimitriou,M., Garcia,M.E., Ho,W.K.,
            Wright,M.J., Rose,L.M., Magnusson,P.K., Pedersen,N.L., Couper,D.,
            Oostra,B.A., Hofman,A., Ikram,M.A., Tiemeier,H.W.,
            Uitterlinden,A.G., van Rooij,F.J., Barroso,I., Johansson,I.,
            Xue,L., Kaakinen,M., Milani,L., Power,C., Snieder,H., Stolk,R.P.,
            Baumeister,S.E., Biffar,R., Gu,F., Bastardot,F., Kutalik,Z.,
            Jacobs,D.R. Jr., Forouhi,N.G., Mihailov,E., Lind,L., Lindgren,C.,
            Michaelsson,K., Morris,A., Jensen,M., Khaw,K.T., Luben,R.N.,
            Wang,J.J., Mannisto,S., Perala,M.M., Kahonen,M., Lehtimaki,T.,
            Viikari,J., Mozaffarian,D., Mukamal,K., Psaty,B.M., Doring,A.,
            Heath,A.C., Montgomery,G.W., Dahmen,N., Carithers,T., Tucker,K.L.,
            Ferrucci,L., Boyd,H.A., Melbye,M., Treur,J.L., Mellstrom,D.,
            Hottenga,J.J., Prokopenko,I., Tonjes,A., Deloukas,P., Kanoni,S.,
            Lorentzon,M., Houston,D.K., Liu,Y., Danesh,J., Rasheed,A.,
            Mason,M.A., Zonderman,A.B., Franke,L., Kristal,B.S.,
            Karjalainen,J., Reed,D.R., Westra,H.J., Evans,M.K., Saleheen,D.,
            Harris,T.B., Dedoussis,G., Curhan,G., Stumvoll,M., Beilby,J.,
            Pasquale,L.R., Feenstra,B., Bandinelli,S., Ordovas,J.M., Chan,A.T.,
            Peters,U., Ohlsson,C., Gieger,C., Martin,N.G., Waldenberger,M.,
            Siscovick,D.S., Raitakari,O., Eriksson,J.G., Mitchell,P.,
            Hunter,D.J., Kraft,P., Rimm,E.B., Boomsma,D.I., Borecki,I.B.,
            Loos,R.J., Wareham,N.J., Vollenweider,P., Caporaso,N., Grabe,H.J.,
            Neuhouser,M.L., Wolffenbuttel,B.H., Hu,F.B., Hypponen,E.,
            Jarvelin,M.R., Cupples,L.A., Franks,P.W., Ridker,P.M., van
            Duijn,C.M., Heiss,G., Metspalu,A., North,K.E., Ingelsson,E.,
            Nettleton,J.A., van Dam,R.M. and Chasman,D.I.
  CONSRTM   Coffee and Caffeine Genetics Consortium; International Parkinson's
            Disease Genomics Consortium (IPDGC); North American Brain
            Expression Consortium (NABEC); UK Brain Expression Consortium
            (UKBEC)
  TITLE     Genome-wide meta-analysis identifies six novel loci associated with
            habitual coffee consumption
  JOURNAL   Mol Psychiatry 20 (5), 647-656 (2015)
   PUBMED   25288136
  REMARK    Review article
REFERENCE   10 (residues 1 to 343)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC051850.1, AF327923.1, CX869634.1 and AC006330.5.
            
            Transcript Variant: This variant (1) represents the longer
            transcript but encodes the shorter isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.152716.1, BC051850.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000493111.7/ ENSP00000473983.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..343
                     /product="transmembrane protein 120A isoform 1"
                     /note="transmembrane protein induced by tumor necrosis
                     factor alpha; ion channel TACAN"
                     /calculated_mol_wt=40479
     Region          13..336
                     /region_name="TMPIT"
                     /note="TMPIT-like protein; pfam07851"
                     /db_xref="CDD:462288"
     Site            133..152
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ8.1)"
     Site            159..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ8.1)"
     Site            191..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ8.1)"
     Site            219..240
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ8.1)"
     Site            271..294
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ8.1)"
     Site            305..330
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ8.1)"
     CDS             1..343
                     /gene="TMEM120A"
                     /gene_synonym="NET29; TACAN; TMPIT"
                     /coded_by="NM_031925.3:26..1057"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS64688.1"
                     /db_xref="GeneID:83862"
                     /db_xref="HGNC:HGNC:21697"
                     /db_xref="MIM:616550"
ORIGIN      
        1 mqppppgplg dclrdwedlq qdfqniqeth rlyrlkleel tklqnnctss itrqkkrlqe
       61 lalalkkckp slpaeaegaa qelenqmker qglffdmeay lpkknglyls lvlgnvnvtl
      121 lskqakfayk deyekfklyl tiililisft crfllnsrvt daafnfllvw yyctltires
      181 ilinngsrik gwwvfhhyvs tflsgvmltw pdglmyqkfr nqflsfsmyq sfvqflqyyy
      241 qsgclyrlra lgerhtmdlt vegfqswmwr gltfllpflf fghfwqlfna ltlfnlaqdp
      301 qckewqvlmc gfpflllflg nffttlrvvh hkfhsqrhgs kkd
//
LOCUS       NP_068594                384 aa            linear   PRI 27-APR-2025
DEFINITION  DNA dC->dU-editing enzyme APOBEC-3G isoform 1 [Homo sapiens].
ACCESSION   NP_068594
VERSION     NP_068594.1
DBSOURCE    REFSEQ: accession NM_021822.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Belbacha,I., Bensghir,R., Filali Marhoum,K., Laboudi,M.,
            Hajoutt,K., Elharti,E., Sadki,K. and Oumzil,H.
  TITLE     Prevalence of HBsAg among Moroccan HIV-1 infected patients and
            APOBEC3G variant frequencies in HIV-1/HBV co-infection
  JOURNAL   J Infect Dev Ctries 18 (5), 779-786 (2024)
   PUBMED   38865405
  REMARK    GeneRIF: Prevalence of HBsAg among Moroccan HIV-1 infected patients
            and APOBEC3G variant frequencies in HIV-1/HBV co-infection.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Shandilya,S.M., Nalam,M.N., Nalivaika,E.A., Gross,P.J.,
            Valesano,J.C., Shindo,K., Li,M., Munson,M., Royer,W.E., Harjes,E.,
            Kono,T., Matsuo,H., Harris,R.S., Somasundaran,M. and Schiffer,C.A.
  TITLE     Crystal structure of the APOBEC3G catalytic domain reveals
            potential oligomerization interfaces
  JOURNAL   Structure 18 (1), 28-38 (2010)
   PUBMED   20152150
  REMARK    GeneRIF: crystal structure of the catalytically active C-terminal
            domain of APOBEC3G was determined to 2.25 A.
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Furukawa,A., Nagata,T., Matsugami,A., Habu,Y., Sugiyama,R.,
            Hayashi,F., Kobayashi,N., Yokoyama,S., Takaku,H. and Katahira,M.
  TITLE     Structure, interaction and real-time monitoring of the enzymatic
            reaction of wild-type APOBEC3G
  JOURNAL   EMBO J 28 (4), 440-451 (2009)
   PUBMED   19153609
  REMARK    GeneRIF: analysis of the enzymatic reaction of wild-type APOBEC3G
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Stenglein,M.D., Matsuo,H. and Harris,R.S.
  TITLE     Two regions within the amino-terminal half of APOBEC3G cooperate to
            determine cytoplasmic localization
  JOURNAL   J Virol 82 (19), 9591-9599 (2008)
   PUBMED   18667511
  REMARK    GeneRIF: two regions of APOBEC3G combine to mediate an
            intermolecular interaction that controls subcellular localization
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Gooch,B.D. and Cullen,B.R.
  TITLE     Functional domain organization of human APOBEC3G
  JOURNAL   Virology 379 (1), 118-124 (2008)
   PUBMED   18639915
  REMARK    GeneRIF: Here, the authors demonstrate that the ability to bind to
            Gag and package into HIV-1 virions is entirely contained within the
            amino-terminal half of A3G.
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Zhang,K.L., Mangeat,B., Ortiz,M., Zoete,V., Trono,D., Telenti,A.
            and Michielin,O.
  TITLE     Model structure of human APOBEC3G
  JOURNAL   PLoS One 2 (4), e378 (2007)
   PUBMED   17440614
  REMARK    GeneRIF: structure model identifies a cluster of residues important
            for packaging of APOBEC3G into virions, and may serve to guide
            functional analysis of APOBEC3G
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Chelico,L., Pham,P., Calabrese,P. and Goodman,M.F.
  TITLE     APOBEC3G DNA deaminase acts processively 3' --> 5' on
            single-stranded DNA
  JOURNAL   Nat Struct Mol Biol 13 (5), 392-399 (2006)
   PUBMED   16622407
  REMARK    GeneRIF: G --> A mutational gradient generated in viral genomic DNA
            in vivo could result from an intrinsic processive directional
            attack by APOBEC3G on single-stranded cDNA
REFERENCE   8  (residues 1 to 384)
  AUTHORS   An,P., Bleiber,G., Duggal,P., Nelson,G., May,M., Mangeat,B.,
            Alobwede,I., Trono,D., Vlahov,D., Donfield,S., Goedert,J.J.,
            Phair,J., Buchbinder,S., O'Brien,S.J., Telenti,A. and Winkler,C.A.
  TITLE     APOBEC3G genetic variants and their influence on the progression to
            AIDS
  JOURNAL   J Virol 78 (20), 11070-11076 (2004)
   PUBMED   15452227
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Li,J., Potash,M.J. and Volsky,D.J.
  TITLE     Functional domains of APOBEC3G required for antiviral activity
  JOURNAL   J Cell Biochem 92 (3), 560-572 (2004)
   PUBMED   15156567
  REMARK    GeneRIF: APOBEC3G inhibits HIV-1 infection through interference
            with reverse transcription.
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Wedekind,J.E., Dance,G.S., Sowden,M.P. and Smith,H.C.
  TITLE     Messenger RNA editing in mammals: new members of the APOBEC family
            seeking roles in the family business
  JOURNAL   Trends Genet 19 (4), 207-216 (2003)
   PUBMED   12683974
  REMARK    Review article
            Erratum:[Trends Genet. 2003 Jul;19(7):369]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL022318.2, AL078641.2 and
            BC009683.1.
            
            Summary: This gene is a member of the cytidine deaminase gene
            family. It is one of seven related genes or pseudogenes found in a
            cluster, thought to result from gene duplication, on chromosome 22.
            Members of the cluster encode proteins that are structurally and
            functionally related to the C to U RNA-editing cytidine deaminase
            APOBEC1. The protein encoded by this gene catalyzes site-specific
            deamination of both RNA and single-stranded DNA. The encoded
            protein has been found to be a specific inhibitor of human
            immunodeficiency virus-1 (HIV-1) infectivity. [provided by RefSeq,
            Mar 2017].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF182420.1, SRR1163658.137014.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000407997.4/ ENSP00000385057.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..384
                     /product="DNA dC->dU-editing enzyme APOBEC-3G isoform 1"
                     /EC_number="3.5.4.38"
                     /note="phorbolin-like protein MDS019; deoxycytidine
                     deaminase; apolipoprotein B editing enzyme catalytic
                     polypeptide-like 3G; apolipoprotein B mRNA-editing enzyme
                     catalytic polypeptide 3G; apolipoprotein B mRNA editing
                     enzyme, catalytic polypeptide-like 3G; DNA dC->dU-editing
                     enzyme APOBEC-3G; DNA dC->dU editing enzyme;
                     APOBEC-related protein 9; APOBEC-related cytidine
                     deaminase; apolipoprotein B mRNA editing enzyme cytidine
                     deaminase"
                     /calculated_mol_wt=46277
     Region          1..60
                     /region_name="Essential for cytoplasmic localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC16.1)"
     Region          12..194
                     /region_name="APOBEC2"
                     /note="pfam18772"
                     /db_xref="CDD:465863"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000269|PubMed:18836454,
                     ECO:0000269|PubMed:21659520; propagated from
                     UniProtKB/Swiss-Prot (Q9HC16.1)"
     Region          195..379
                     /region_name="NAD2"
                     /note="Novel AID APOBEC clade 2; pfam18782"
                     /db_xref="CDD:436733"
     Region          209..336
                     /region_name="Necessary for homooligomerization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC16.1)"
     Region          213..215
                     /region_name="Interaction with DNA. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC16.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA and CAMK2.
                     /evidence=ECO:0000269|PubMed:21659520; propagated from
                     UniProtKB/Swiss-Prot (Q9HC16.1)"
     Site            244
                     /site_type="other"
                     /note="Interaction with DNA. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q9HC16.1)"
     Region          313..320
                     /region_name="Interaction with DNA. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC16.1)"
     CDS             1..384
                     /gene="APOBEC3G"
                     /gene_synonym="A3G; ARCD; ARP-9; ARP9; bK150C2.7; CEM-15;
                     CEM15; dJ494G10.1; MDS019"
                     /coded_by="NM_021822.4:88..1242"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13984.1"
                     /db_xref="GeneID:60489"
                     /db_xref="HGNC:HGNC:17357"
                     /db_xref="MIM:607113"
ORIGIN      
        1 mkphfrntve rmyrdtfsyn fynrpilsrr ntvwlcyevk tkgpsrppld akifrgqvys
       61 elkyhpemrf fhwfskwrkl hrdqeyevtw yiswspctkc trdmatflae dpkvtltifv
      121 arlyyfwdpd yqealrslcq krdgpratmk imnydefqhc wskfvysqre lfepwnnlpk
      181 yyillhimlg eilrhsmdpp tftfnfnnep wvrgrhetyl cyevermhnd twvllnqrrg
      241 flcnqaphkh gflegrhael cfldvipfwk ldldqdyrvt cftswspcfs caqemakfis
      301 knkhvslcif tariyddqgr cqeglrtlae agakisimty sefkhcwdtf vdhqgcpfqp
      361 wdgldehsqd lsgrlrailq nqen
//
LOCUS       NP_001312                193 aa            linear   PRI 27-APR-2025
DEFINITION  cysteine and glycine-rich protein 2 isoform b [Homo sapiens].
ACCESSION   NP_001312
VERSION     NP_001312.1
DBSOURCE    REFSEQ: accession NM_001321.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Hayashi,K., Labios,R.J., Morita,T., Ashimori,A., Aoki,R., Mikuni,M.
            and Kimura,K.
  TITLE     Significance of the p38MAPK-CRP2 axis in myofibroblastic phenotypic
            transition
  JOURNAL   Cell Struct Funct 48 (2), 199-210 (2023)
   PUBMED   37899269
  REMARK    GeneRIF: Significance of the p38MAPK-CRP2 axis in myofibroblastic
            phenotypic transition.
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Hayashi,K., Horoiwa,S., Mori,K., Miyata,H., Labios,R.J., Morita,T.,
            Kobayashi,Y., Yamashiro,C., Higashijima,F., Yoshimoto,T., Kimura,K.
            and Nakagawa,Y.
  TITLE     Role of CRP2-MRTF interaction in functions of myofibroblasts
  JOURNAL   Cell Struct Funct 48 (1), 83-98 (2023)
   PUBMED   37164693
  REMARK    GeneRIF: Role of CRP2-MRTF interaction in functions of
            myofibroblasts.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Chen,L., Long,X., Duan,S., Liu,X., Chen,J., Lan,J., Liu,X.,
            Huang,W., Geng,J. and Zhou,J.
  TITLE     CSRP2 suppresses colorectal cancer progression via p130Cas/Rac1
            axis-meditated ERK, PAK, and HIPPO signaling pathways
  JOURNAL   Theranostics 10 (24), 11063-11079 (2020)
   PUBMED   33042270
  REMARK    GeneRIF: CSRP2 suppresses colorectal cancer progression via
            p130Cas/Rac1 axis-meditated ERK, PAK, and HIPPO signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Hoffmann,C., Mao,X., Brown-Clay,J., Moreau,F., Al Absi,A.,
            Wurzer,H., Sousa,B., Schmitt,F., Berchem,G., Janji,B. and Thomas,C.
  TITLE     Hypoxia promotes breast cancer cell invasion through
            HIF-1alpha-mediated up-regulation of the invadopodial actin
            bundling protein CSRP2
  JOURNAL   Sci Rep 8 (1), 10191 (2018)
   PUBMED   29976963
  REMARK    GeneRIF: Study showed that CSRP2, an invadopodial actin bundling
            protein, is upregulated by hypoxia in various breast cancer cell
            lines, as well as in pre-clinical and clinical breast tumor
            specimens and functionally characterized two hypoxia responsive
            elements within the proximal promoter of CSRP2 gene which are
            targeted by hypoxia-inducible factor-1 (HIF-1) and required for
            promoter transactivation in response to hypoxia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Weiskirchen,R. and Gressner,A.M.
  TITLE     The cysteine- and glycine-rich LIM domain protein CRP2 specifically
            interacts with a novel human protein (CRP2BP)
  JOURNAL   Biochem Biophys Res Commun 274 (3), 655-663 (2000)
   PUBMED   10924333
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Weiskirchen,R., Erdel,M., Utermann,G. and Bister,K.
  TITLE     Cloning, structural analysis, and chromosomal localization of the
            human CSRP2 gene encoding the LIM domain protein CRP2
  JOURNAL   Genomics 44 (1), 83-93 (1997)
   PUBMED   9286703
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Jain,M.K., Fujita,K.P., Hsieh,C.M., Endege,W.O., Sibinga,N.E.,
            Yet,S.F., Kashiki,S., Lee,W.S., Perrella,M.A., Haber,E. and
            Lee,M.E.
  TITLE     Molecular cloning and characterization of SmLIM, a developmentally
            regulated LIM protein preferentially expressed in aortic smooth
            muscle cells
  JOURNAL   J Biol Chem 271 (17), 10194-10199 (1996)
   PUBMED   8626582
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Karim,M.A., Ohta,K., Egashira,M., Jinno,Y., Niikawa,N., Matsuda,I.
            and Indo,Y.
  TITLE     Human ESP1/CRP2, a member of the LIM domain protein family:
            characterization of the cDNA and assignment of the gene locus to
            chromosome 14q32.3
  JOURNAL   Genomics 31 (2), 167-176 (1996)
   PUBMED   8824798
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Weiskirchen,R., Pino,J.D., Macalma,T., Bister,K. and Beckerle,M.C.
  TITLE     The cysteine-rich protein family of highly related LIM domain
            proteins
  JOURNAL   J Biol Chem 270 (48), 28946-28954 (1995)
   PUBMED   7499425
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX461295.2, BC000992.2 and
            AC124784.4.
            
            Summary: CSRP2 is a member of the CSRP family of genes, encoding a
            group of LIM domain proteins, which may be involved in regulatory
            processes important for development and cellular differentiation.
            CRP2 contains two copies of the cysteine-rich amino acid sequence
            motif (LIM) with putative zinc-binding activity, and may be
            involved in regulating ordered cell growth. Other genes in the
            family include CSRP1 and CSRP3. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) encodes isoform b. Variants
            1-5 all encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.172419.1,
                                           SRR5189652.173068.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311083.10/ ENSP00000310901.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..193
                     /product="cysteine and glycine-rich protein 2 isoform b"
                     /note="LIM domain only 5, smooth muscle; LMO-5;
                     cysteine-rich protein 2; LIM domain only protein 5; smooth
                     muscle cell LIM protein; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=20823
     Region          9..63
                     /region_name="LIM1_CRP2"
                     /note="The first LIM domain of Cysteine Rich Protein 2
                     (CRP2); cd09480"
                     /db_xref="CDD:188864"
     Site            order(10,13,31,34,37,40,58,61)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188864"
     Region          64..69
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16527.3)"
     Site            112
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P97314; propagated from
                     UniProtKB/Swiss-Prot (Q16527.3)"
     Region          119..172
                     /region_name="LIM2_CRP2"
                     /note="The second LIM domain of Cysteine Rich Protein 2
                     (CRP2); cd09840"
                     /db_xref="CDD:188871"
     Site            order(119,122,140,143,146,149,167,170)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188871"
     Site            131
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P21291; propagated from
                     UniProtKB/Swiss-Prot (Q16527.3)"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P97315; propagated from
                     UniProtKB/Swiss-Prot (Q16527.3)"
     Site            161
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P97315; propagated from
                     UniProtKB/Swiss-Prot (Q16527.3)"
     CDS             1..193
                     /gene="CSRP2"
                     /gene_synonym="CRP2; LMO5; SmLIM"
                     /coded_by="NM_001321.3:84..665"
                     /note="isoform b is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9015.1"
                     /db_xref="GeneID:1466"
                     /db_xref="HGNC:HGNC:2470"
                     /db_xref="MIM:601871"
ORIGIN      
        1 mpvwgggnkc gacgrtvyha eevqcdgrsf hrccflcmvc rknldsttva ihdeeiycks
       61 cygkkygpkg ygygqgagtl nmdrgerlgi kpesvqphrp ttnpntskfa qkyggaekcs
      121 rcgdsvyaae kiigagkpwh kncfrcakcg kslesttlte kegeiyckgc yaknfgpkgf
      181 gygqgagalv haq
//
LOCUS       NP_001347762             520 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 45 [Mus musculus].
ACCESSION   NP_001347762 XP_006539865
VERSION     NP_001347762.1
DBSOURCE    REFSEQ: accession NM_001360833.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Medeiros de Araujo,J.A., Barao,S., Mateos-White,I., Espinosa,A.,
            Costa,M.R., Gil-Sanz,C. and Muller,U.
  TITLE     ZBTB20 is crucial for the specification of a subset of callosal
            projection neurons and astrocytes in the mammalian neocortex
  JOURNAL   Development 148 (16) (2021)
   PUBMED   34351428
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Tang,F., Barbacioru,C., Nordman,E., Bao,S., Lee,C., Wang,X.,
            Tuch,B.B., Heard,E., Lao,K. and Surani,M.A.
  TITLE     Deterministic and stochastic allele specific gene expression in
            single mouse blastomeres
  JOURNAL   PLoS One 6 (6), e21208 (2011)
   PUBMED   21731673
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Sodersten,E., Lilja,T. and Hermanson,O.
  TITLE     The novel BTB/POZ and zinc finger factor Zbtb45 is essential for
            proper glial differentiation of neural and oligodendrocyte
            progenitor cells
  JOURNAL   Cell Cycle 9 (24), 4866-4875 (2010)
   PUBMED   21131782
  REMARK    GeneRIF: Data suggest that Zbtb45 is a novel regulator of glial
            differentiation.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Lin,Q., Donahue,S.L., Moore-Jarrett,T., Cao,S., Osipovich,A.B. and
            Ruley,H.E.
  TITLE     Mutagenesis of diploid mammalian genes by gene entrapment
  JOURNAL   Nucleic Acids Res 34 (20), e139 (2006)
   PUBMED   17062627
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC121301.8 and BC094359.1.
            
            On Feb 15, 2018 this sequence version replaced XP_006539865.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK154877.1, AK155880.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849389, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 7.72 cM"
     Protein         1..520
                     /product="zinc finger and BTB domain-containing protein
                     45"
                     /note="zinc finger protein 499"
                     /calculated_mol_wt=54881
     Region          15..126
                     /region_name="BTB_POZ_ZBTB45"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 45 (ZBTB45); cd18229"
                     /db_xref="CDD:349538"
     Region          182..272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KG4.1)"
     Region          337..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KG4.1)"
     Region          412..434
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          414..434
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(419,421,423,425..426,429..430,433,447,449,453..454,
                     457..458,461,475,477,479,481..482,485..486,489)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          442..462
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          454..479
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          468..490
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          470..490
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..520
                     /gene="Zbtb45"
                     /gene_synonym="Gm157; Zfp499"
                     /coded_by="NM_001360833.1:218..1780"
                     /db_xref="CCDS:CCDS20822.1"
                     /db_xref="GeneID:232879"
                     /db_xref="MGI:MGI:2685003"
ORIGIN      
        1 maateavhhi hlqnfsrsll etlngqrlgg hfcdvtvrir easlrahrcv laagspffqd
       61 klllghseir vppvvpaqtv rqlveflysg slvvaqgeal qvltaasvlr iqtvidectq
      121 iiararvpnt papaplpppv ppplapaqlr hrlrhllaar ppghpnaahs rkqrqparlq
      181 lpappapika egpdaepalt aapedrgeed ddeetdeetd aeegeggggg pgegqappaf
      241 pdcaggfltt aadsaredpp astgitdygg agrdflrgtg vtedvfpdsy vsawheessg
      301 gpescpvets appdcalagp rptgvktpgp pvalfpfhlg apgppaptpp tpsgpapapp
      361 ptfyptlqpd aapsaqlget qavpaapaaq ataisgtpvr apggqgaeqp ayecshcrkt
      421 fssrknytkh mfihsgekph qcavcwrsfs lrdyllkhmv thtgvrafqc avcakrftqk
      481 sslnvhmrth rperapcpac gkvfshrall erhlaahpap
//
LOCUS       NP_054752                244 aa            linear   PRI 27-APR-2025
DEFINITION  thiol S-methyltransferase TMT1A precursor [Homo sapiens].
ACCESSION   NP_054752
VERSION     NP_054752.3
DBSOURCE    REFSEQ: accession NM_014033.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Robey,R.W., Fitzsimmons,C.M., Guiblet,W.M., Frye,W.J.E., Gonzalez
            Dalmasy,J.M., Wang,L., Russell,D.A., Huff,L.M., Perciaccante,A.J.,
            Ali-Rahmani,F., Lipsey,C.C., Wade,H.M., Mitchell,A.V.,
            Maligireddy,S.S., Terrero,D., Butcher,D., Edmondson,E.F.,
            Jenkins,L.M., Nikitina,T., Zhurkin,V.B., Tiwari,A.K.,
            Piscopio,A.D., Totah,R.A., Bates,S.E., Arda,H.E., Gottesman,M.M.
            and Batista,P.J.
  TITLE     The Methyltransferases METTL7A and METTL7B Confer Resistance to
            Thiol-Based Histone Deacetylase Inhibitors
  JOURNAL   Mol Cancer Ther 23 (4), 464-477 (2024)
   PUBMED   38151817
  REMARK    GeneRIF: The Methyltransferases METTL7A and METTL7B Confer
            Resistance to Thiol-Based Histone Deacetylase Inhibitors.
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Zhang,D., Zou,T., Liu,Q., Chen,J., Xiao,M., Zheng,A., Zhang,Z.,
            Du,F., Dai,Y., Xiang,S., Wu,X., Li,M., Chen,Y., Zhao,Y., Shen,J.,
            Chen,G. and Xiao,Z.
  TITLE     Transcriptomic characterization revealed that METTL7A inhibits
            melanoma progression via the p53 signaling pathway and
            immunomodulatory pathway
  JOURNAL   PeerJ 11, e15799 (2023)
   PUBMED   37547717
  REMARK    GeneRIF: Transcriptomic characterization revealed that METTL7A
            inhibits melanoma progression via the p53 signaling pathway and
            immunomodulatory pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Russell,D.A., Chau,M.K., Shi,Y., Levasseur,I.N., Maldonato,B.J. and
            Totah,R.A.
  TITLE     METTL7A (TMT1A) and METTL7B (TMT1B) Are Responsible for Alkyl
            S-Thiol Methyl Transferase Activity in Liver
  JOURNAL   Drug Metab Dispos 51 (8), 1024-1034 (2023)
   PUBMED   37137720
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Vera-Montecinos,A., Galiano-Landeira,J., Roldan,M.,
            Vidal-Domenech,F., Claro,E. and Ramos,B.
  TITLE     A Novel Localization of METTL7A in Bergmann Glial Cells in Human
            Cerebellum
  JOURNAL   Int J Mol Sci 24 (9), 8405 (2023)
   PUBMED   37176112
  REMARK    GeneRIF: A Novel Localization of METTL7A in Bergmann Glial Cells in
            Human Cerebellum.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Wang,Z., He,J., Bach,D.H., Huang,Y.H., Li,Z., Liu,H., Lin,P. and
            Yang,J.
  TITLE     Induction of m6A methylation in adipocyte exosomal LncRNAs mediates
            myeloma drug resistance
  JOURNAL   J Exp Clin Cancer Res 41 (1), 4 (2022)
   PUBMED   34980213
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Zhou,S., Shen,Y., Zheng,M., Wang,L., Che,R., Hu,W. and Li,P.
  TITLE     DNA methylation of METTL7A gene body regulates its transcriptional
            level in thyroid cancer
  JOURNAL   Oncotarget 8 (21), 34652-34660 (2017)
   PUBMED   28416772
  REMARK    GeneRIF: Results revealed that the methylation level of METTL7A was
            downregulated in thyroid cancer, and determined the methylation
            level of one CpG site at the exon of the METTL7A gene body impacted
            the transcriptional activity.
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Park,E.M., Lim,Y.S., Ahn,B.Y. and Hwang,S.B.
  TITLE     AAM-B Interacts with Nonstructural 4B and Regulates Hepatitis C
            Virus Propagation
  JOURNAL   PLoS One 10 (7), e0132839 (2015)
   PUBMED   26185986
  REMARK    GeneRIF: AAM-B is predominantly localized in lipid droplets and may
            be involved in recruitment of NS4B protein in the proximity of
            lipid droplets.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 244)
  AUTHORS   Zehmer,J.K., Bartz,R., Bisel,B., Liu,P., Seemann,J. and
            Anderson,R.G.
  TITLE     Targeting sequences of UBXD8 and AAM-B reveal that the ER has a
            direct role in the emergence and regression of lipid droplets
  JOURNAL   J Cell Sci 122 (Pt 20), 3694-3702 (2009)
   PUBMED   19773358
REFERENCE   9  (residues 1 to 244)
  AUTHORS   Zehmer,J.K., Bartz,R., Liu,P. and Anderson,R.G.
  TITLE     Identification of a novel N-terminal hydrophobic sequence that
            targets proteins to lipid droplets
  JOURNAL   J Cell Sci 121 (11), 1852-1860 (2008)
   PUBMED   18477614
REFERENCE   10 (residues 1 to 244)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM805242.1, AY358797.1 and AC008121.43.
            
            On Mar 3, 2006 this sequence version replaced NP_054752.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225689.1, SRR1803617.98158.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000332160.5/ ENSP00000331787.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..244
                     /product="thiol S-methyltransferase TMT1A precursor"
                     /EC_number="2.1.1.348"
                     /EC_number="2.1.1.9"
                     /note="methyltransferase-like protein 7A; protein AAM-B;
                     putative methyltransferase-like protein 7A;
                     methyltransferase like 7A; methyltransferase TMT1A;
                     N6-adenosine-methyltransferase TMT1A; thiol
                     S-methyltransferase TMT1A"
                     /calculated_mol_wt=24849
     sig_peptide     1..29
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H8H3.1)"
                     /calculated_mol_wt=3488
     Region          1..28
                     /region_name="Targeting to lipid droplets.
                     /evidence=ECO:0000269|PubMed:18477614"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8H3.1)"
     mat_peptide     30..244
                     /product="Thiol S-methyltransferase TMT1A.
                     /id=PRO_0000251921"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8H3.1)"
                     /calculated_mol_wt=24849
     Region          75..172
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
     CDS             1..244
                     /gene="TMT1A"
                     /gene_synonym="AAM-B; AAMB; METTL7A"
                     /coded_by="NM_014033.4:25..759"
                     /db_xref="CCDS:CCDS8804.1"
                     /db_xref="GeneID:25840"
                     /db_xref="HGNC:HGNC:24550"
                     /db_xref="MIM:618338"
ORIGIN      
        1 meltifilrl aiyiltfply llnflglwsw ickkwfpyfl vrftviyneq maskkrelfs
       61 nlqefagpsg klsllevgcg tganfkfypp gcrvtcidpn pnfekfliks iaenrhlqfe
      121 rfvvaagenm hqvadgsvdv vvctlvlcsv knqerilrev crvlrpggaf yfmehvaaec
      181 stwnyfwqqv ldpawhllfd gcnltreswk alerasfskl klqhiqapls welvrphiyg
      241 yavk
//
LOCUS       NP_001028632             753 aa            linear   ROD 27-APR-2025
DEFINITION  dynein regulatory complex protein 1 [Mus musculus].
ACCESSION   NP_001028632 XP_355721 XP_913444
VERSION     NP_001028632.1
DBSOURCE    REFSEQ: accession NM_001033460.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Zhang,J., He,X., Wu,H., Zhang,X., Yang,S., Liu,C., Liu,S., Hua,R.,
            Zhou,S., Zhao,S., Hu,F., Zhang,J., Liu,W., Cheng,H., Gao,Y.,
            Zhang,F., Cao,Y. and Liu,M.
  TITLE     Loss of DRC1 function leads to multiple morphological abnormalities
            of the sperm flagella and male infertility in human and mouse
  JOURNAL   Hum Mol Genet 30 (21), 1996-2011 (2021)
   PUBMED   34169321
  REMARK    GeneRIF: Loss of DRC1 function leads to multiple morphological
            abnormalities of the sperm flagella and male infertility in human
            and mouse.
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Stauber,M., Weidemann,M., Dittrich-Breiholz,O., Lobschat,K.,
            Alten,L., Mai,M., Beckers,A., Kracht,M. and Gossler,A.
  TITLE     Identification of FOXJ1 effectors during ciliogenesis in the foetal
            respiratory epithelium and embryonic left-right organiser of the
            mouse
  JOURNAL   Dev Biol 423 (2), 170-188 (2017)
   PUBMED   27914912
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Burnicka-Turek,O., Steimle,J.D., Huang,W., Felker,L., Kamp,A.,
            Kweon,J., Peterson,M., Reeves,R.H., Maslen,C.L., Gruber,P.J.,
            Yang,X.H., Shendure,J. and Moskowitz,I.P.
  TITLE     Cilia gene mutations cause atrioventricular septal defects by
            multiple mechanisms
  JOURNAL   Hum Mol Genet 25 (14), 3011-3028 (2016)
   PUBMED   27340223
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Navarro,N. and Maga,A.M.
  TITLE     Does 3D Phenotyping Yield Substantial Insights in the Genetics of
            the Mouse Mandible Shape?
  JOURNAL   G3 (Bethesda) 6 (5), 1153-1163 (2016)
   PUBMED   26921296
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Li,Y., Klena,N.T., Gabriel,G.C., Liu,X., Kim,A.J., Lemke,K.,
            Chen,Y., Chatterjee,B., Devine,W., Damerla,R.R., Chang,C., Yagi,H.,
            San Agustin,J.T., Thahir,M., Anderton,S., Lawhead,C., Vescovi,A.,
            Pratt,H., Morgan,J., Haynes,L., Smith,C.L., Eppig,J.T.,
            Reinholdt,L., Francis,R., Leatherbury,L., Ganapathiraju,M.K.,
            Tobita,K., Pazour,G.J. and Lo,C.W.
  TITLE     Global genetic analysis in mice unveils central role for cilia in
            congenital heart disease
  JOURNAL   Nature 521 (7553), 520-524 (2015)
   PUBMED   25807483
REFERENCE   7  (residues 1 to 753)
  AUTHORS   McClintock,T.S., Glasser,C.E., Bose,S.C. and Bergman,D.A.
  TITLE     Tissue expression patterns identify mouse cilia genes
  JOURNAL   Physiol Genomics 32 (2), 198-206 (2008)
   PUBMED   17971504
  REMARK    GeneRIF: Gm1060 is most abundantly expressed in tissues rich in
            highly ciliated cells, such as olfactory sensory neurons, and is
            predicted to be important to cilia.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC241618.4 and AC242405.4.
            
            On or before Jan 26, 2006 this sequence version replaced
            XP_913444.1, XP_355721.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK140154.1, BC150863.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384, SAMN00849387
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 16.42 cM"
     Protein         1..753
                     /product="dynein regulatory complex protein 1"
                     /note="coiled-coil domain-containing protein 164;
                     coiled-coil domain containing 164"
                     /calculated_mol_wt=88377
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3USS3.1)"
     Region          <33..>277
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          55..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3USS3.1)"
     Region          99..200
                     /region_name="NYD-SP28"
                     /note="Sperm tail; pfam14772"
                     /db_xref="CDD:464307"
     Region          587..628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3USS3.1)"
     Region          673..732
                     /region_name="NYD-SP28_assoc"
                     /note="Sperm tail C-terminal domain; pfam14775"
                     /db_xref="CDD:464309"
     CDS             1..753
                     /gene="Drc1"
                     /gene_synonym="b2b1654Clo; Ccdc164; Gm1060"
                     /coded_by="NM_001033460.4:60..2321"
                     /db_xref="CCDS:CCDS84857.1"
                     /db_xref="GeneID:381738"
                     /db_xref="MGI:MGI:2685906"
ORIGIN      
        1 mnpsgtigvl eqngeehlat pilgpsvhsd npqeriqarr lriaarqear rrealgeyld
       61 gkkeseeeqs ksykqkeesr lkltklllcg telvtniqva advreihrrv eeeetkrqrl
      121 eklenevkts qdkfdeitak weegrrkrip qelwemlnsq qvhcaelied knklanelqq
      181 elkikddqyv kdlkkqsedi tlilermeeq vknvmknfrq elihiekafe serqellssn
      241 kkkweralqa hnakeleylt nrmkkvedye kqlnkqrvwd ceeyntikik leqdvqileq
      301 qlqqmkatyq lnqekleynf qvlkkrdees tviksqqkrk lnrlhdvvnn lrtkytkqir
      361 qfqddnqslt sdykrlvtqf kdlqkalrhf iiideekfre iwlmneaeak elaqrafdvd
      421 riihsqhlgl pwnmpdlwfl nnvgpislqq qksvtqilee lllqtedeat eaamsededy
      481 mdlpnqisak tttkvlmllc desgfliesk llsllhplek secyllrlda ifsalaiede
      541 ddlyklvnff lryrahrlss aqasssihsn vertslmsal erlslmsqtd kgsmvsksdq
      601 epteqedeqe gdnaslssre leeqedlssp rfihpndvlk ileafvtglk kpkdaqpvlk
      661 lkketrdnsk dteyweslaa vipffkqnlw dalykaleky ylvlterakl lmenesleqq
      721 naemqsllqq ylqakvntel qipptqgfrm psk
//
LOCUS       NP_032654                935 aa            linear   ROD 27-APR-2025
DEFINITION  DNA mismatch repair protein Msh2 [Mus musculus].
ACCESSION   NP_032654
VERSION     NP_032654.1
DBSOURCE    REFSEQ: accession NM_008628.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 935)
  AUTHORS   Wang,N., Zhang,S., Langfelder,P., Ramanathan,L., Gao,F.,
            Plascencia,M., Vaca,R., Gu,X., Deng,L., Dionisio,L.E., Vu,H.,
            Maciejewski,E., Ernst,J., Prasad,B.C., Vogt,T.F., Horvath,S.,
            Aaronson,J.S., Rosinski,J. and Yang,X.W.
  TITLE     Distinct mismatch-repair complex genes set neuronal CAG-repeat
            expansion rate to drive selective pathogenesis in HD mice
  JOURNAL   Cell 188 (6), 1524-1544 (2025)
   PUBMED   39938516
REFERENCE   2  (residues 1 to 935)
  AUTHORS   Bowen,C.M., Duzagac,F., Martel-Martel,A., Reyes-Uribe,L.,
            Zaheer,M., Thompson,J., Deng,N., Sinha,R., Mazumdar,S.,
            Taggart,M.W., Jain,A.K., Tosti,E., Edelmann,W., Sinha,K.M. and
            Vilar,E.
  TITLE     Inhibition of histone methyltransferase EZH2 for immune
            interception of colorectal cancer in Lynch syndrome
  JOURNAL   JCI Insight 10 (6), e177545 (2025)
   PUBMED   39946195
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 935)
  AUTHORS   Ghobashi,A.H., Lanzloth,R., Ladaika,C.A., Masood,A. and
            O'Hagan,H.M.
  TITLE     Single-Cell Profiling Reveals the Impact of Genetic Alterations on
            the Differentiation of Inflammation-Induced Murine Colon Tumors
  JOURNAL   Cancers (Basel) 16 (11), 2040 (2024)
   PUBMED   38893159
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 935)
  AUTHORS   Mandula,J.K., Sierra-Mondragon,R.A., Jimenez,R.V., Chang,D.,
            Mohamed,E., Chang,S., Vazquez-Martinez,J.A., Cao,Y., Anadon,C.M.,
            Lee,S.B., Das,S., Rocha-Munguba,L., Pham,V.M., Li,R., Tarhini,A.A.,
            Furqan,M., Dalton,W., Churchman,M., Moran-Segura,C.M., Nguyen,J.,
            Perez,B., Kojetin,D.J., Obermayer,A., Yu,X., Chen,A., Shaw,T.I.,
            Conejo-Garcia,J.R. and Rodriguez,P.C.
  TITLE     Jagged2 targeting in lung cancer activates anti-tumor immunity via
            Notch-induced functional reprogramming of tumor-associated
            macrophages
  JOURNAL   Immunity 57 (5), 1124-1140 (2024)
   PUBMED   38636522
REFERENCE   5  (residues 1 to 935)
  AUTHORS   Song,Y., Kerr,T.D., Sanders,C., Dai,L., Baxter,S.S., Somerville,B.,
            Baugher,R.N., Mellott,S.D., Young,T.B., Lawhorn,H.E., Plona,T.M.,
            Xu,B., Wei,L., Hu,Q., Liu,S., Hutson,A., Karim,B., Burkett,S.,
            Difilippantonio,S., Pinto,L., Gebert,J., Kloor,M., Lipkin,S.M.,
            Sei,S. and Shoemaker,R.H.
  TITLE     Organoids and metastatic orthotopic mouse model for mismatch
            repair-deficient colorectal cancer
  JOURNAL   Front Oncol 13, 1223915 (2023)
   PUBMED   37746286
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 935)
  AUTHORS   Reitmair,A.H., Schmits,R., Ewel,A., Bapat,B., Redston,M., Mitri,A.,
            Waterhouse,P., Mittrucker,H.W., Wakeham,A., Liu,B. et al.
  TITLE     MSH2 deficient mice are viable and susceptible to lymphoid tumours
  JOURNAL   Nat Genet 11 (1), 64-70 (1995)
   PUBMED   7550317
REFERENCE   7  (residues 1 to 935)
  AUTHORS   de Wind,N., Dekker,M., Berns,A., Radman,M. and te Riele,H.
  TITLE     Inactivation of the mouse Msh2 gene results in mismatch repair
            deficiency, methylation tolerance, hyperrecombination, and
            predisposition to cancer
  JOURNAL   Cell 82 (2), 321-330 (1995)
   PUBMED   7628020
REFERENCE   8  (residues 1 to 935)
  AUTHORS   Varlet,I., Pallard,C., Radman,M., Moreau,J. and de Wind,N.
  TITLE     Cloning and expression of the Xenopus and mouse Msh2 DNA mismatch
            repair genes
  JOURNAL   Nucleic Acids Res 22 (25), 5723-5728 (1994)
   PUBMED   7838728
REFERENCE   9  (residues 1 to 935)
  AUTHORS   Kolodner,R.D., Hall,N.R., Lipford,J., Kane,M.F., Rao,M.R.,
            Morrison,P., Wirth,L., Finan,P.J., Burn,J. and Chapman,P.
  TITLE     Structure of the human MSH2 locus and analysis of two Muir-Torre
            kindreds for msh2 mutations
  JOURNAL   Genomics 24 (3), 516-526 (1994)
   PUBMED   7713503
  REMARK    Erratum:[Genomics 1995 Aug 10;28(3):613]
REFERENCE   10 (residues 1 to 935)
  AUTHORS   Fishel,R., Lescoe,M.K., Rao,M.R., Copeland,N.G., Jenkins,N.A.,
            Garber,J., Kane,M. and Kolodner,R.
  TITLE     The human mutator gene homolog MSH2 and its association with
            hereditary nonpolyposis colon cancer
  JOURNAL   Cell 75 (5), 1027-1038 (1993)
   PUBMED   8252616
  REMARK    Erratum:[Cell. 1994 Apr 8;77(1):1 p following 166. PMID: 8156592]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC163652.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047117.1, X81143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..935
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 57.87 cM"
     Protein         1..935
                     /product="DNA mismatch repair protein Msh2"
                     /note="mutS protein homolog 2"
                     /calculated_mol_wt=104021
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P43246; propagated from
                     UniProtKB/Swiss-Prot (P43247.1)"
     Region          18..132
                     /region_name="MutS_I"
                     /note="MutS domain I; pfam01624"
                     /db_xref="CDD:426350"
     Region          152..853
                     /region_name="MutS"
                     /note="DNA mismatch repair ATPase MutS [Replication,
                     recombination and repair]; COG0249"
                     /db_xref="CDD:440019"
     Site            567
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P43247.1)"
     Region          601..671
                     /region_name="Interaction with EXO1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P43247.1)"
     Site            845
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P43246; propagated from
                     UniProtKB/Swiss-Prot (P43247.1)"
     Site            847
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P43246; propagated from
                     UniProtKB/Swiss-Prot (P43247.1)"
     Site            871
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P43246; propagated from
                     UniProtKB/Swiss-Prot (P43247.1)"
     Site            892
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P43246; propagated from
                     UniProtKB/Swiss-Prot (P43247.1)"
     Site            921
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43246; propagated from
                     UniProtKB/Swiss-Prot (P43247.1)"
     CDS             1..935
                     /gene="Msh2"
                     /coded_by="NM_008628.3:65..2872"
                     /db_xref="CCDS:CCDS29019.1"
                     /db_xref="GeneID:17685"
                     /db_xref="MGI:MGI:101816"
ORIGIN      
        1 mavqpketlq legaaeagfv rffegmpekp sttvrlfdrg dfytahgeda llaarevfkt
       61 qgvikymgpa gsktlqsvvl skmnfesfvk dlllvrqyrv evyknkagnk askenewyla
      121 fkaspgnlsq fedilfgnnd msasvgvmgi kmavvdgqrh vgvgyvdstq rklglcefpe
      181 ndqfsnleal liqigpkecv lpggettgdm gklrqviqrg giliterkra dfstkdiyqd
      241 lnrllkgkkg eqinsaalpe menqvavssl savikflell sddsnfgqfe latfdfsqym
      301 kldmaavral nlfqgsvedt tgsqslaall nkcktaqgqr lvnqwikqpl mdrnrieerl
      361 nlveafveds elrqslqedl lrrfpdlnrl akkfqrqaan lqdcyrlyqg inqlpsviqa
      421 lekyegrhqa lllavfvtpl idlrsdfskf qemiettldm dqvenheflv kpsfdpnlse
      481 lrevmdglek kmqstlinaa rglgldpgkq ikldssaqfg yyfrvtckee kvlrnnknfs
      541 tvdiqkngvk ftnselssln eeytknkgey eeaqdaivke ivnissgyve pmqtlndvla
      601 hldaivsfah vsnaapvpyv rpvilekgkg riilkasrha cvevqdevaf ipndvhfekd
      661 kqmfhiitgp nmggkstyir qtgvivlmaq igcfvpcesa evsivdcila rvgagdsqlk
      721 gvstfmaeml etasilrsat kdsliiidel grgtstydgf glawaisdyi atkigafcmf
      781 athfheltal anqiptvnnl hvtaltteet ltmlyqvkkg vcdqsfgihv aelanfprhv
      841 iacakqkale leefqnigts lgcdeaepaa krrclereqg ekiileflsk vkqvpftams
      901 eesisaklkq lkaevvaknn sfvneiisri kapap
//
LOCUS       NP_036575                509 aa            linear   PRI 27-APR-2025
DEFINITION  sperm-associated antigen 6 isoform 1 [Homo sapiens].
ACCESSION   NP_036575
VERSION     NP_036575.1
DBSOURCE    REFSEQ: accession NM_012443.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Zhao,B., Yin,J., Ding,L., Luo,J., Luo,J., Mu,J., Pan,S., Du,J.,
            Zhong,Y., Zhang,L. and Liu,L.
  TITLE     SPAG6 regulates cell proliferation and apoptosis via TGF-beta/Smad
            signal pathway in adult B-cell acute lymphoblastic leukemia
  JOURNAL   Int J Hematol 119 (2), 119-129 (2024)
   PUBMED   38147275
  REMARK    GeneRIF: SPAG6 regulates cell proliferation and apoptosis via
            TGF-beta/Smad signal pathway in adult B-cell acute lymphoblastic
            leukemia.
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Mu,J., Yuan,P., Luo,J., Chen,Y., Tian,Y., Ding,L., Zhao,B.,
            Wang,X., Wang,B. and Liu,L.
  TITLE     Upregulated SPAG6 promotes acute myeloid leukemia progression
            through MYO1D that regulates the EGFR family expression
  JOURNAL   Blood Adv 6 (18), 5379-5394 (2022)
   PUBMED   35667090
  REMARK    GeneRIF: Upregulated SPAG6 promotes acute myeloid leukemia
            progression through MYO1D that regulates the EGFR family
            expression.
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Xu,C., Tang,D., Shao,Z., Geng,H., Gao,Y., Li,K., Tan,Q., Wang,G.,
            Wang,C., Wu,H., Li,G., Lv,M., He,X. and Cao,Y.
  TITLE     Homozygous SPAG6 variants can induce nonsyndromic
            asthenoteratozoospermia with severe MMAF
  JOURNAL   Reprod Biol Endocrinol 20 (1), 41 (2022)
   PUBMED   35232447
  REMARK    GeneRIF: Homozygous SPAG6 variants can induce nonsyndromic
            asthenoteratozoospermia with severe MMAF.
            Erratum:[Reprod Biol Endocrinol. 2022 Apr 29;20(1):74. doi:
            10.1186/s12958-022-00939-w. PMID: 35488345]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Skou,A.S., Juul-Dam,K.L., Hansen,M., Lausen,B., Stratmann,S.,
            Holmfeldt,L., Aggerholm,A., Nyvold,C.G., Ommen,H.B. and Hasle,H.
  TITLE     Measurable Residual Disease Monitoring of SPAG6, ST18, PRAME, and
            XAGE1A Expression in Peripheral Blood May Detect Imminent Relapse
            in Childhood Acute Myeloid Leukemia
  JOURNAL   J Mol Diagn 23 (12), 1787-1799 (2021)
   PUBMED   34600138
  REMARK    GeneRIF: Measurable Residual Disease Monitoring of SPAG6, ST18,
            PRAME, and XAGE1A Expression in Peripheral Blood May Detect
            Imminent Relapse in Childhood Acute Myeloid Leukemia.
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Zhang,R., Zhu,H., Yuan,Y., Wang,Y. and Tian,Z.
  TITLE     SPAG6 promotes cell proliferation and inhibits apoptosis through
            the PTEN/PI3K/AKT pathway in Burkitt lymphoma
  JOURNAL   Oncol Rep 44 (5), 2021-2030 (2020)
   PUBMED   33000212
  REMARK    GeneRIF: SPAG6 promotes cell proliferation and inhibits apoptosis
            through the PTEN/PI3K/AKT pathway in Burkitt lymphoma.
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Sapiro,R., Kostetskii,I., Olds-Clarke,P., Gerton,G.L., Radice,G.L.
            and Strauss,I.I.I. JF.
  TITLE     Male infertility, impaired sperm motility, and hydrocephalus in
            mice deficient in sperm-associated antigen 6
  JOURNAL   Mol Cell Biol 22 (17), 6298-6305 (2002)
   PUBMED   12167721
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Neilson,L.I., Schneider,P.A., Van Deerlin,P.G., Kiriakidou,M.,
            Driscoll,D.A., Pellegrini,M.C., Millinder,S., Yamamoto,K.K.,
            French,C.K. and Strauss,J.F. 3rd.
  TITLE     cDNA cloning and characterization of a human sperm antigen (SPAG6)
            with homology to the product of the Chlamydomonas PF16 locus
  JOURNAL   Genomics 60 (3), 272-280 (1999)
   PUBMED   10493827
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Diekman,A.B. and Herr,J.C.
  TITLE     Sperm antigens and their use in the development of an
            immunocontraceptive
  JOURNAL   Am J Reprod Immunol 37 (1), 111-117 (1997)
   PUBMED   9138444
  REMARK    Review article
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Smith,E.F. and Lefebvre,P.A.
  TITLE     The role of central apparatus components in flagellar motility and
            microtubule assembly
  JOURNAL   Cell Motil Cytoskeleton 38 (1), 1-8 (1997)
   PUBMED   9295136
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB025758.1, AF079363.1 and
            BC030585.2.
            
            Summary: The correlation of anti-sperm antibodies with cases of
            unexplained infertility implicates a role for these antibodies in
            blocking fertilization. Improved diagnosis and treatment of
            immunologic infertility, as well as identification of proteins for
            targeted contraception, are dependent on the identification and
            characterization of relevant sperm antigens. The protein expressed
            by this gene is recognized by anti-sperm antibodies from an
            infertile man. This protein localizes to the tail of permeabilized
            human sperm and contains eight contiguous armadillo repeats, a
            motif known to mediate protein-protein interactions. Studies in
            mice suggest that this protein is involved in sperm flagellar
            motility and maintenance of the structural integrity of mature
            sperm. Several transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL080136.1, AF079363.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376624.8/ ENSP00000365811.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2"
     Protein         1..509
                     /product="sperm-associated antigen 6 isoform 1"
                     /note="sperm flagellar protein; axoneme central apparatus
                     protein; protein PF16 homolog; testicular tissue protein
                     Li 176"
                     /calculated_mol_wt=55345
     Region          31..70
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75602.1)"
     Region          37..68
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          73..112
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75602.1)"
     Region          78..110
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          112..>423
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          115..154
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75602.1)"
     Region          120..152
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(143,147,151,185,189,193,227,231)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          157..196
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75602.1)"
     Region          160..196
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          199..238
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O75602.1)"
     Region          202..234
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          241..280
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O75602.1)"
     Region          244..278
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          289..325
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          325..365
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O75602.1)"
     Region          335..369
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          368..409
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O75602.1)"
     Region          378..406
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..509
                     /gene="SPAG6"
                     /gene_synonym="CFAP194; CT141; FAP194; pf16; Repro-SA-1"
                     /coded_by="NM_012443.4:117..1646"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7139.1"
                     /db_xref="GeneID:9576"
                     /db_xref="HGNC:HGNC:11215"
                     /db_xref="MIM:605730"
ORIGIN      
        1 msqrqvlqvf eqyqkartqf vqmvaelatr pqnietlqna gvmsllrtll ldvvptiqqt
       61 aalalgrlan ynddlaeavv kcdilpqlvy slaeqnrfyk kaaafvlrav gkhspqlaqa
      121 ivdcgaldtl vicledfdpg vkeaaawalr yiarhnaels qavvdagavp llvlciqepe
      181 ialkriaasa lsdiakhspe laqtvvdaga vahlaqmiln pdaklkhqil salsqvskhs
      241 vdlaemvvea eifpvvltcl kdkdeyvkkn astlireiak htpelsqlvv naggvaavid
      301 cigsckgntr lpgimmlgyv aahsenlama viiskgvpql svclseeped hikaaaawal
      361 gqigrhtpeh aravavtntl pvllslymst essedlqvks kkaiknilqk ctylpalepf
      421 lydappnilk hvvgqfskvl phdskarrlf vtsgglkkvq eikaepgsll qeyinsinsc
      481 ypeeivryys pgysdtllqr vdsyqplnn
//
LOCUS       NP_001041523              70 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein eL38 [Mus musculus].
ACCESSION   NP_001041523 XP_006534072
VERSION     NP_001041523.1
DBSOURCE    REFSEQ: accession NM_001048058.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Shi,L., Hu,H., Sun,P., Li,Z., Ji,L., Liu,S. and Zhang,J.
  TITLE     RPL38 knockdown inhibits the inflammation and apoptosis in
            chondrocytes through regulating METTL3-mediated SOCS2 m6A
            modification in osteoarthritis
  JOURNAL   Inflamm Res 71 (7-8), 977-989 (2022)
   PUBMED   35596790
  REMARK    GeneRIF: RPL38 knockdown inhibits the inflammation and apoptosis in
            chondrocytes through regulating METTL3-mediated SOCS2 m6A
            modification in osteoarthritis.
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Zhao,Q., Yan,S., Lu,J., Parker,D.J., Wu,H., Sun,Q., Crossman,D.K.,
            Liu,S., Wang,Q., Sesaki,H., Mitra,K., Liu,K. and Jiao,K.
  TITLE     Drp1 regulates transcription of ribosomal protein genes in
            embryonic hearts
  JOURNAL   J Cell Sci 135 (4) (2022)
   PUBMED   35099001
REFERENCE   4  (residues 1 to 70)
  AUTHORS   Khatter,H., Myasnikov,A.G., Natchiar,S.K. and Klaholz,B.P.
  TITLE     Structure of the human 80S ribosome
  JOURNAL   Nature 520 (7549), 640-645 (2015)
   PUBMED   25901680
REFERENCE   5  (residues 1 to 70)
  AUTHORS   Distler,U., Schmeisser,M.J., Pelosi,A., Reim,D., Kuharev,J.,
            Weiczner,R., Baumgart,J., Boeckers,T.M., Nitsch,R., Vogt,J. and
            Tenzer,S.
  TITLE     In-depth protein profiling of the postsynaptic density from mouse
            hippocampus using data-independent acquisition proteomics
  JOURNAL   Proteomics 14 (21-22), 2607-2613 (2014)
   PUBMED   25211037
REFERENCE   6  (residues 1 to 70)
  AUTHORS   Noben-Trauth,K. and Latoche,J.R.
  TITLE     Ectopic mineralization in the middle ear and chronic otitis media
            with effusion caused by RPL38 deficiency in the Tail-short (Ts)
            mouse
  JOURNAL   J Biol Chem 286 (4), 3079-3093 (2011)
   PUBMED   21062742
  REMARK    GeneRIF: Ectopic mineralization in the middle ear and chronic
            otitis media with effusion caused by RPL38 deficiency in the
            Tail-short (Ts) mouse.
REFERENCE   7  (residues 1 to 70)
  AUTHORS   Center,E.M., Marcus,N.M. and Wilson,D.B.
  TITLE     Abnormal development of the notochord and perinotochordal sheath in
            duplicitas posterior, patch and tail-short mice
  JOURNAL   Histol Histopathol 3 (4), 405-412 (1988)
   PUBMED   2980249
REFERENCE   8  (residues 1 to 70)
  AUTHORS   Munke,M., Cox,D.R., Jackson,I.J., Hogan,B.L. and Francke,U.
  TITLE     The murine Hox-2 cluster of homeo box containing genes maps distal
            on chromosome 11 near the tail-short (Ts) locus
  JOURNAL   Cytogenet Cell Genet 42 (4), 236-240 (1986)
   PUBMED   2875852
REFERENCE   9  (residues 1 to 70)
  AUTHORS   Brotherton,T.W., Chui,D.H., McFarland,E.C. and Russell,E.S.
  TITLE     Fetal erythropoiesis and hemoglobin ontogeny in tail-short (Ts/+)
            mutant mice
  JOURNAL   Blood 54 (3), 673-683 (1979)
   PUBMED   465735
REFERENCE   10 (residues 1 to 70)
  AUTHORS   Johnson,D.R.
  TITLE     The interfrontal bone and mutant genes in the mouse
  JOURNAL   J Anat 121 (Pt 3), 507-513 (1976)
   PUBMED   1018005
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL645484.14 and BE448083.1.
            
            On May 3, 2018 this sequence version replaced XP_006534072.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BE448083.1, AV507225.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 79.82 cM"
     Protein         1..70
                     /product="large ribosomal subunit protein eL38"
                     /note="60S ribosomal protein L38"
                     /calculated_mol_wt=8073
     Region          2..68
                     /region_name="Ribosomal_L38e"
                     /note="Ribosomal L38e protein family; pfam01781"
                     /db_xref="CDD:460326"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P63173; propagated from
                     UniProtKB/Swiss-Prot (Q9JJI8.3)"
     Site            67
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63173; propagated from
                     UniProtKB/Swiss-Prot (Q9JJI8.3)"
     CDS             1..70
                     /gene="Rpl38"
                     /gene_synonym="0610025G13Rik; Rbt; Ts; Tss"
                     /coded_by="NM_001048058.2:138..350"
                     /db_xref="CCDS:CCDS36365.1"
                     /db_xref="GeneID:67671"
                     /db_xref="MGI:MGI:1914921"
ORIGIN      
        1 mprkieeikd flltarrkda ksvkikknkd nvkfkvrcsr ylytlvitdk ekaeklkqsl
       61 ppglavkdlk
//
LOCUS       NP_001354475             565 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 39 [Homo sapiens].
ACCESSION   NP_001354475 XP_005270254
VERSION     NP_001354475.1
DBSOURCE    REFSEQ: accession NM_001367546.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_005270254.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.633099.1,
                                           SRR3476690.930512.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..565
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 39"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=62706
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          433..560
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..565
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367546.1:95..1792"
                     /note="isoform 39 is encoded by transcript variant 39"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmepqttvvh natdgikgst escntttede dlkaaplrtg ngssvpegrs srdrtapsag
      421 mqpqpslcss amrkqeiiki teqlieainn gdfeaytkic dpgltsfepe algnlvegmd
      481 fhkfyfenll sknskpihtt ilnphvhvig edaaciayir ltqyidgqgr prtsqseetr
      541 vwhrrdgkwl nvhyhcsgap aaplq
//
LOCUS       NP_056295                549 aa            linear   PRI 27-APR-2025
DEFINITION  nectin-3 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_056295
VERSION     NP_056295.1
DBSOURCE    REFSEQ: accession NM_015480.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Hirabayashi,K., Tajiri,T., Bosch,D.E., Morimachi,M., Miyaoka,M.,
            Inomoto,C., Nakamura,N. and Yeh,M.M.
  TITLE     Loss of nectin-3 expression as a marker of tumor aggressiveness in
            pancreatic neuroendocrine tumor
  JOURNAL   Pathol Int 70 (2), 84-91 (2020)
   PUBMED   31855317
  REMARK    GeneRIF: Loss of nectin-3 expression as a marker of tumor
            aggressiveness in pancreatic neuroendocrine tumor.
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Lachke,S.A., Higgins,A.W., Inagaki,M., Saadi,I., Xi,Q., Long,M.,
            Quade,B.J., Talkowski,M.E., Gusella,J.F., Fujimoto,A.,
            Robinson,M.L., Yang,Y., Duong,Q.T., Shapira,I., Motro,B.,
            Miyoshi,J., Takai,Y., Morton,C.C. and Maas,R.L.
  TITLE     The cell adhesion gene PVRL3 is associated with congenital ocular
            defects
  JOURNAL   Hum Genet 131 (2), 235-250 (2012)
   PUBMED   21769484
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Reymond,N., Fabre,S., Lecocq,E., Adelaide,J., Dubreuil,P. and
            Lopez,M.
  TITLE     Nectin4/PRR4, a new afadin-associated member of the nectin family
            that trans-interacts with nectin1/PRR1 through V domain interaction
  JOURNAL   J Biol Chem 276 (46), 43205-43215 (2001)
   PUBMED   11544254
REFERENCE   7  (residues 1 to 549)
  AUTHORS   Reymond,N., Borg,J.P., Lecocq,E., Adelaide,J., Campadelli-Fiume,G.,
            Dubreuil,P. and Lopez,M.
  TITLE     Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family
            that interacts with afadin
  JOURNAL   Gene 255 (2), 347-355 (2000)
   PUBMED   11024295
REFERENCE   8  (residues 1 to 549)
  AUTHORS   Satoh-Horikawa,K., Nakanishi,H., Takahashi,K., Miyahara,M.,
            Nishimura,M., Tachibana,K., Mizoguchi,A. and Takai,Y.
  TITLE     Nectin-3, a new member of immunoglobulin-like cell adhesion
            molecules that shows homophilic and heterophilic cell-cell adhesion
            activities
  JOURNAL   J Biol Chem 275 (14), 10291-10299 (2000)
   PUBMED   10744716
REFERENCE   9  (residues 1 to 549)
  AUTHORS   Takahashi,K., Nakanishi,H., Miyahara,M., Mandai,K., Satoh,K.,
            Satoh,A., Nishioka,H., Aoki,J., Nomoto,A., Mizoguchi,A. and
            Takai,Y.
  TITLE     Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited
            to cadherin-based adherens junctions through interaction with
            Afadin, a PDZ domain-containing protein
  JOURNAL   J Cell Biol 145 (3), 539-549 (1999)
   PUBMED   10225955
REFERENCE   10 (residues 1 to 549)
  AUTHORS   Lopez,M., Aoubala,M., Jordier,F., Isnardon,D., Gomez,S. and
            Dubreuil,P.
  TITLE     The human poliovirus receptor related 2 protein is a new
            hematopoietic/endothelial homophilic adhesion molecule
  JOURNAL   Blood 92 (12), 4602-4611 (1998)
   PUBMED   9845526
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI464010.1, AF282874.1,
            AC137833.3 and AA555086.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the nectin family of
            proteins, which function as adhesion molecules at adherens
            junctions. This family member interacts with other nectin-like
            proteins and with afadin, a filamentous actin-binding protein
            involved in the regulation of directional motility, cell
            proliferation and survival. This gene plays a role in ocular
            development involving the ciliary body. Mutations in this gene are
            believed to result in congenital ocular defects. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.100385.1, AF282874.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000485303.6/ ENSP00000418070.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.13"
     Protein         1..549
                     /product="nectin-3 isoform 1 precursor"
                     /note="nectin 3; poliovirus receptor-related protein 3;
                     poliovirus receptor-related 3"
                     /calculated_mol_wt=55201
     sig_peptide     1..57
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
                     /calculated_mol_wt=5820
     mat_peptide     58..549
                     /product="Nectin-3. /id=PRO_0000226372"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS3.1)"
                     /calculated_mol_wt=55201
     Region          58..167
                     /region_name="IgV_1_Nectin-3_like"
                     /note="First immunoglobulin variable (IgV) domain of
                     nectin-3 (also known as poliovirus receptor related
                     protein 3), and similar domains; cd05887"
                     /db_xref="CDD:409470"
     Region          58..81
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409470"
     Region          58..62
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409470"
     Region          64..68
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409470"
     Site            order(72..79,86..94,101..113,131..137,142..156,159..167)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409470"
     Region          73..81
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409470"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          82..86
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409470"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          87..93
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409470"
     Region          88..93
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409470"
     Region          94..113
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409470"
     Region          103..108
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409470"
     Region          110..114
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409470"
     Region          114..152
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409470"
     Region          121..125
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409470"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          130..137
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409470"
     Region          144..152
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409470"
     Region          153..156
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409470"
     Region          156..166
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409470"
     Region          157..167
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409470"
     Region          170..265
                     /region_name="IgC1_2_Nectin-3-4_like"
                     /note="Second immunoglobulin (Ig) domain of nectin-3 and
                     nectin-4 (poliovirus receptor related protein 4), and
                     similar domains; member of the C1-set of Ig superfamily
                     (IgSF) domains; cd07704"
                     /db_xref="CDD:409501"
     Region          170..176
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409501"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          189..196
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409501"
     Region          201..207
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409501"
     Region          209..211
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409501"
     Region          213..220
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409501"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          225..233
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409501"
     Region          243..250
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409501"
     Region          256..262
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409501"
     Region          269..355
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          287..291
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..305
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          320..325
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          335..340
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          350..353
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          404..432
                     /region_name="TM_EGFR-like"
                     /note="Transmembrane domain of the Epidermal Growth Factor
                     Receptor family of Protein Tyrosine Kinases; cd12087"
                     /db_xref="CDD:213052"
     Site            order(404..405,408..409,411..413,415..416,419)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:213052"
     Site            405..425
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS3.1)"
     CDS             1..549
                     /gene="NECTIN3"
                     /gene_synonym="CD113; CDW113; NECTIN-3; PPR3; PRR3; PVRL3;
                     PVRR3"
                     /coded_by="NM_015480.3:203..1852"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2957.1"
                     /db_xref="GeneID:25945"
                     /db_xref="HGNC:HGNC:17664"
                     /db_xref="MIM:607147"
ORIGIN      
        1 martlrpspl cpgggkaqls sasllgagll lqpptpppll lllfplllfs rlcgalagpi
       61 ivephvtavw gknvslkcli evnetitqis wekihgkssq tvavhhpqyg fsvqgeyqgr
      121 vlfknyslnd atitlhnigf sdsgkyicka vtfplgnaqs sttvtvlvep tvslikgpds
      181 lidggnetva aiciaatgkp vahidwegdl gemestttsf pnetatiisq yklfptrfar
      241 grritcvvkh palekdirys fildiqyape vsvtgydgnw fvgrkgvnlk cnadanpppf
      301 ksvwsrldgq wpdgllasdn tlhfvhpltf nysgvyickv tnslgqrsdq kviyisdppt
      361 tttlqptiqw hpstadiedl atepkklpfp lstlatikdd tiatiiasvv ggalfivlvs
      421 vlagifcyrr rrtfrgdyfa knyippsdmq kesqidvlqq deldsypdsv kkenknpvnn
      481 lirkdyleep ektqwnnven lnrferpmdy yedlkmgmkf vsdehydene ddlvshvdgs
      541 visrrewyv
//
LOCUS       NP_001357490            1460 aa            linear   PRI 27-APR-2025
DEFINITION  DNA-binding protein RFX7 isoform 1 [Homo sapiens].
ACCESSION   NP_001357490
VERSION     NP_001357490.1
DBSOURCE    REFSEQ: accession NM_001370561.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1460)
  AUTHORS   Coronel,L., Riege,K., Schwab,K., Forste,S., Hackes,D., Semerau,L.,
            Bernhart,S.H., Siebert,R., Hoffmann,S. and Fischer,M.
  TITLE     Transcription factor RFX7 governs a tumor suppressor network in
            response to p53 and stress
  JOURNAL   Nucleic Acids Res 49 (13), 7437-7456 (2021)
   PUBMED   34197623
  REMARK    GeneRIF: Transcription factor RFX7 governs a tumor suppressor
            network in response to p53 and stress.
REFERENCE   2  (residues 1 to 1460)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1460)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   4  (residues 1 to 1460)
  AUTHORS   Castro,W., Chelbi,S.T., Niogret,C., Ramon-Barros,C., Welten,S.P.M.,
            Osterheld,K., Wang,H., Rota,G., Morgado,L., Vivier,E., Raeber,M.E.,
            Boyman,O., Delorenzi,M., Barras,D., Ho,P.C., Oxenius,A. and
            Guarda,G.
  TITLE     The transcription factor Rfx7 limits metabolism of NK cells and
            promotes their maintenance and immunity
  JOURNAL   Nat Immunol 19 (8), 809-820 (2018)
   PUBMED   29967452
REFERENCE   5  (residues 1 to 1460)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   6  (residues 1 to 1460)
  AUTHORS   Berndt,S.I., Skibola,C.F., Joseph,V., Camp,N.J., Nieters,A.,
            Wang,Z., Cozen,W., Monnereau,A., Wang,S.S., Kelly,R.S., Lan,Q.,
            Teras,L.R., Chatterjee,N., Chung,C.C., Yeager,M.,
            Brooks-Wilson,A.R., Hartge,P., Purdue,M.P., Birmann,B.M.,
            Armstrong,B.K., Cocco,P., Zhang,Y., Severi,G.,
            Zeleniuch-Jacquotte,A., Lawrence,C., Burdette,L., Yuenger,J.,
            Hutchinson,A., Jacobs,K.B., Call,T.G., Shanafelt,T.D., Novak,A.J.,
            Kay,N.E., Liebow,M., Wang,A.H., Smedby,K.E., Adami,H.O., Melbye,M.,
            Glimelius,B., Chang,E.T., Glenn,M., Curtin,K.,
            Cannon-Albright,L.A., Jones,B., Diver,W.R., Link,B.K., Weiner,G.J.,
            Conde,L., Bracci,P.M., Riby,J., Holly,E.A., Smith,M.T.,
            Jackson,R.D., Tinker,L.F., Benavente,Y., Becker,N., Boffetta,P.,
            Brennan,P., Foretova,L., Maynadie,M., McKay,J., Staines,A.,
            Rabe,K.G., Achenbach,S.J., Vachon,C.M., Goldin,L.R., Strom,S.S.,
            Lanasa,M.C., Spector,L.G., Leis,J.F., Cunningham,J.M.,
            Weinberg,J.B., Morrison,V.A., Caporaso,N.E., Norman,A.D.,
            Linet,M.S., De Roos,A.J., Morton,L.M., Severson,R.K., Riboli,E.,
            Vineis,P., Kaaks,R., Trichopoulos,D., Masala,G., Weiderpass,E.,
            Chirlaque,M.D., Vermeulen,R.C., Travis,R.C., Giles,G.G.,
            Albanes,D., Virtamo,J., Weinstein,S., Clavel,J., Zheng,T.,
            Holford,T.R., Offit,K., Zelenetz,A., Klein,R.J., Spinelli,J.J.,
            Bertrand,K.A., Laden,F., Giovannucci,E., Kraft,P., Kricker,A.,
            Turner,J., Vajdic,C.M., Ennas,M.G., Ferri,G.M., Miligi,L.,
            Liang,L., Sampson,J., Crouch,S., Park,J.H., North,K.E., Cox,A.,
            Snowden,J.A., Wright,J., Carracedo,A., Lopez-Otin,C., Bea,S.,
            Salaverria,I., Martin-Garcia,D., Campo,E., Fraumeni,J.F. Jr., de
            Sanjose,S., Hjalgrim,H., Cerhan,J.R., Chanock,S.J., Rothman,N. and
            Slager,S.L.
  TITLE     Genome-wide association study identifies multiple risk loci for
            chronic lymphocytic leukemia
  JOURNAL   Nat Genet 45 (8), 868-876 (2013)
   PUBMED   23770605
REFERENCE   7  (residues 1 to 1460)
  AUTHORS   Crowther-Swanepoel,D., Broderick,P., Di Bernardo,M.C.,
            Dobbins,S.E., Torres,M., Mansouri,M., Ruiz-Ponte,C., Enjuanes,A.,
            Rosenquist,R., Carracedo,A., Jurlander,J., Campo,E., Juliusson,G.,
            Montserrat,E., Smedby,K.E., Dyer,M.J., Matutes,E., Dearden,C.,
            Sunter,N.J., Hall,A.G., Mainou-Fowler,T., Jackson,G.H.,
            Summerfield,G., Harris,R.J., Pettitt,A.R., Allsup,D.J.,
            Bailey,J.R., Pratt,G., Pepper,C., Fegan,C., Parker,A., Oscier,D.,
            Allan,J.M., Catovsky,D. and Houlston,R.S.
  TITLE     Common variants at 2q37.3, 8q24.21, 15q21.3 and 16q24.1 influence
            chronic lymphocytic leukemia risk
  JOURNAL   Nat Genet 42 (2), 132-136 (2010)
   PUBMED   20062064
REFERENCE   8  (residues 1 to 1460)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 1460)
  AUTHORS   Aftab,S., Semenec,L., Chu,J.S. and Chen,N.
  TITLE     Identification and characterization of novel human tissue-specific
            RFX transcription factors
  JOURNAL   BMC Evol Biol 8, 226 (2008)
   PUBMED   18673564
  REMARK    GeneRIF: RFX7 is a winged helix transcription factor expressed
            ubiquitously in all tissues examined, especially brain tissue.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1460)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068726.5, AC084783.2 and KF456052.1.
            
            Summary: RFX7 is a member of the regulatory factor X (RFX) family
            of transcription factors (see RFX1, MIM 600006) (Aftab et al., 2008
            [PubMed 18673564]).[supplied by OMIM, Mar 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803616.239107.1, SRR1803611.169829.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..1460
                     /product="DNA-binding protein RFX7 isoform 1"
                     /note="regulatory factor X domain containing 2;
                     DNA-binding protein RFX7; regulatory factor X
                     domain-containing protein 2; regulatory factor X, 7"
                     /calculated_mol_wt=157221
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          43..100
                     /region_name="RFX5_N"
                     /note="RFX5 N-terminal domain; pfam18326"
                     /db_xref="CDD:375753"
     Region          105..183
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     Region          188..193
                     /region_name="PxLPxI/L motif, mediates interaction with
                     ANKRA2 and RFXANK. /evidence=ECO:0000269|PubMed:25752541,
                     ECO:0000312|PDB:6MEW"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          <258..568
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          308..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          404..428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          468..>745
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          481..585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          632..715
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            704
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          917..1015
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            988
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            1329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     CDS             1..1460
                     /gene="RFX7"
                     /gene_synonym="MRD71; RFXDC2"
                     /coded_by="NM_001370561.1:575..4957"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS92005.1"
                     /db_xref="GeneID:64864"
                     /db_xref="HGNC:HGNC:25777"
                     /db_xref="MIM:612660"
ORIGIN      
        1 maeeqqqppp qqpdahqqlp psapnsgval palvpglpgt easalqhkik nsicktvqsk
       61 vdcilqevek ftdleklyly lqlpsglsng eksdqnamss sraqqmhafs wirntleehp
      121 etslpkqevy deyksycdnl gyhplsaadf gkimknvfpn mkarrlgtrg kskycysglr
      181 kkafvhmptl pnldfhktgd glegaepsgq lqnideevis sacrlvcewa qkvlsqpfdt
      241 vlelarflvk shyigtksma altvmaaapa gmkgitqpsa fiptaesnsf qpqvktlpsp
      301 idakqqlqrk iqkkqqeqkl qsplpgesaa kksesatsng vtnlpngnps ilspqpigiv
      361 vaavpspipv qrtrqlvtsp spmsssdgkv lplnvqvvtq hmqsvkqapk tpqnvpaspg
      421 gdrsarhryp qilpkpants altirspttv lftsspikta vvpashmssl nvvkmttisl
      481 tpsnsntplk hsasvssatg tteesrsvpq ikngsvvslq spgsrsssag gtsavevkve
      541 petssdehpv qcqensdeak apqtpsallg qksntdgalq kpsnegviei katkvcdqrt
      601 kcksrcneml pgtstgnnqs titlsvasqn ltftsssspp ngdsinkdpk lctksprkrl
      661 sstlqetqvp pvkkpiveql saatiegqkq gsvkkdqkvp hsgktegsta gaqipskvsv
      721 nvsshiganq plnssalvis dsaleqqttp ssspdikvkl egsvflldsd sksvgsfnpn
      781 gwqqitkdse fisasceqqq disvmtipeh sdindleksv welegmpqdt ysqqlhsqiq
      841 esslnqiqah ssdqlplqse lkefepsvsq tnesyfpfdd eltqdsivee lvlmeqqmsm
      901 nnshsygncl gmtlqsqsvt pgapmsshts sthfyhpihs ngtpihtptp tptptptptp
      961 tptptsemia gsqslsresp csrlaqttpv dsalgssrht pigtphsncs ssvppspvec
     1021 rnpfaftpis ssmayhdasi vssspvkpmq rpmathpdkt klewmnngys gvgnssvsgh
     1081 gilpsyqelv edrfrkphaf avpgqsyqsq srhhdthfgr ltpvspvqhq gatvnntnkq
     1141 egfavpapld nkgtnssass nfrcrsvspa vhrqrnlsgs tlypvsnipr snvtpfgspv
     1201 tpevhvftnv htdacannia qrsqsvpltv mmqtafpnal qkqanskkit nvllskldsd
     1261 nddavrglgm nnlpsnytar mnltqileps tvfpsanpqn midsstsvye fqtpsyltks
     1321 nstgqinfsp gdnqaqseig eqqldfnstv kdllsgdslq tnqqlvgqga sdltntasdf
     1381 ssdirlssel sgsindlntl dpnllfdpgr qqgqddeatl eelkndplfq qicsesmnsm
     1441 tssgfewies kdhptvemlg
//
LOCUS       NP_116277               1860 aa            linear   PRI 27-APR-2025
DEFINITION  collagen alpha-1(XXVII) chain preproprotein [Homo sapiens].
ACCESSION   NP_116277
VERSION     NP_116277.2
DBSOURCE    REFSEQ: accession NM_032888.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1860)
  AUTHORS   Satoh,C., Kondoh,T., Shimizu,H., Kinoshita,A., Mishima,H.,
            Nishimura,G., Miyazaki,M., Okano,K., Kumai,Y. and Yoshiura,K.I.
  TITLE     Brothers with novel compound heterozygous mutations in COL27A1
            causing dental and genital abnormalities
  JOURNAL   Eur J Med Genet 64 (2), 104125 (2021)
   PUBMED   33359165
  REMARK    GeneRIF: Brothers with novel compound heterozygous mutations in
            COL27A1 causing dental and genital abnormalities.
REFERENCE   2  (residues 1 to 1860)
  AUTHORS   Gonzaga-Jauregui,C., Yesil,G., Nistala,H., Gezdirici,A., Bayram,Y.,
            Nannuru,K.C., Pehlivan,D., Yuan,B., Jimenez,J., Sahin,Y.,
            Paine,I.S., Akdemir,Z.C., Rajamani,S., Staples,J., Dronzek,J.,
            Howell,K., Fatih,J.M., Smaldone,S., Schlesinger,A.E., Ramirez,N.,
            Cornier,A.S., Kelly,M.A., Haber,R., Chim,S.M., Nieman,K., Wu,N.,
            Walls,J., Poueymirou,W., Siao,C.J., Sutton,V.R., Williams,M.S.,
            Posey,J.E., Gibbs,R.A., Carlo,S., Tegay,D.H., Economides,A.N. and
            Lupski,J.R.
  CONSRTM   Baylor-Hopkins Center for Mendelian Genetics, Regeneron Genetics
            Center
  TITLE     Functional biology of the Steel syndrome founder allele and
            evidence for clan genomics derivation of COL27A1 pathogenic alleles
            worldwide
  JOURNAL   Eur J Hum Genet 28 (9), 1243-1264 (2020)
   PUBMED   32376988
  REMARK    GeneRIF: Functional biology of the Steel syndrome founder allele
            and evidence for clan genomics derivation of COL27A1 pathogenic
            alleles worldwide.
REFERENCE   3  (residues 1 to 1860)
  AUTHORS   Evie,Kritioti., Athina,Theodosiou., Nayia,Nicolaou.,
            Angelos,Alexandrou., Ioannis,Papaevripidou., Elisavet,Efstathiou.,
            Violetta,Christophidou.-Anastasiadou., Carolina,Sismani. and
            Tanteles,G.A.
  TITLE     First reported case of Steel syndrome in the European population: A
            novel homozygous mutation in COL27A1 and review of the literature
  JOURNAL   Eur J Med Genet 63 (7), 103939 (2020)
   PUBMED   32360765
  REMARK    GeneRIF: First reported case of Steel syndrome in the European
            population: A novel homozygous mutation in COL27A1 and review of
            the literature.
            Review article
REFERENCE   4  (residues 1 to 1860)
  AUTHORS   Amlie-Wolf,L., Moyer-Harasink,S., Carr,A.M., Giampietro,P.,
            Schneider,A. and Simon,M.
  TITLE     Three new patients with Steel syndrome and a Puerto Rican specific
            COL27A1 mutation
  JOURNAL   Am J Med Genet A 182 (4), 798-803 (2020)
   PUBMED   31903681
  REMARK    GeneRIF: Three new patients with Steel syndrome and a Puerto Rican
            specific COL27A1 mutation.
REFERENCE   5  (residues 1 to 1860)
  AUTHORS   Meng,W., Adams,M.J., Palmer,C.N.A., Shi,J., Auton,A., Ryan,K.A.,
            Jordan,J.M., Mitchell,B.D., Jackson,R.D., Yau,M.S., McIntosh,A.M.
            and Smith,B.H.
  CONSRTM   23andMe Research Team
  TITLE     Genome-wide association study of knee pain identifies associations
            with GDF5 and COL27A1 in UK Biobank
  JOURNAL   Commun Biol 2, 321 (2019)
   PUBMED   31482140
  REMARK    GeneRIF: two loci in or near GDF5 and COL27A1 that are associated
            with knee pain, were identified.
            Erratum:[Commun Biol. 2020 Mar 26;3(1):149. doi:
            10.1038/s42003-020-0880-x. PMID: 32218487]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1860)
  AUTHORS   Vieira,A.R., McHenry,T.G., Daack-Hirsch,S., Murray,J.C. and
            Marazita,M.L.
  TITLE     Candidate gene/loci studies in cleft lip/palate and dental
            anomalies finds novel susceptibility genes for clefts
  JOURNAL   Genet Med 10 (9), 668-674 (2008)
   PUBMED   18978678
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1860)
  AUTHORS   Gudbjartsson,D.F., Walters,G.B., Thorleifsson,G., Stefansson,H.,
            Halldorsson,B.V., Zusmanovich,P., Sulem,P., Thorlacius,S.,
            Gylfason,A., Steinberg,S., Helgadottir,A., Ingason,A.,
            Steinthorsdottir,V., Olafsdottir,E.J., Olafsdottir,G.H.,
            Jonsson,T., Borch-Johnsen,K., Hansen,T., Andersen,G., Jorgensen,T.,
            Pedersen,O., Aben,K.K., Witjes,J.A., Swinkels,D.W., den Heijer,M.,
            Franke,B., Verbeek,A.L., Becker,D.M., Yanek,L.R., Becker,L.C.,
            Tryggvadottir,L., Rafnar,T., Gulcher,J., Kiemeney,L.A., Kong,A.,
            Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Many sequence variants affecting diversity of adult human height
  JOURNAL   Nat Genet 40 (5), 609-615 (2008)
   PUBMED   18391951
REFERENCE   8  (residues 1 to 1860)
  AUTHORS   Jenkins,E., Moss,J.B., Pace,J.M. and Bridgewater,L.C.
  TITLE     The new collagen gene COL27A1 contains SOX9-responsive enhancer
            elements
  JOURNAL   Matrix Biol 24 (3), 177-184 (2005)
   PUBMED   15922909
  REMARK    GeneRIF: SOX9 may play an important role in the transcriptional
            activation of the newest collagen gene, COL27A1.
REFERENCE   9  (residues 1 to 1860)
  AUTHORS   Boot-Handford,R.P., Tuckwell,D.S., Plumb,D.A., Rock,C.F. and
            Poulsom,R.
  TITLE     A novel and highly conserved collagen (pro(alpha)1(XXVII)) with a
            unique expression pattern and unusual molecular characteristics
            establishes a new clade within the vertebrate fibrillar collagen
            family
  JOURNAL   J Biol Chem 278 (33), 31067-31077 (2003)
   PUBMED   12766169
  REMARK    GeneRIF: type XXVII collagen has unusual molecular features such as
            no minor helical domain, a major helical domain that is short and
            interrupted, and a short chain selection sequence within the NC1
            domain
REFERENCE   10 (residues 1 to 1860)
  AUTHORS   Pace,J.M., Corrado,M., Missero,C. and Byers,P.H.
  TITLE     Identification, characterization and expression analysis of a new
            fibrillar collagen gene, COL27A1
  JOURNAL   Matrix Biol 22 (1), 3-14 (2003)
   PUBMED   12714037
  REMARK    GeneRIF: molecular cloning
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445543.20, BU076480.1,
            BC035728.1, AY149237.1, AL356796.16 and AI808820.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 22, 2003 this sequence version replaced NP_116277.1.
            
            Summary: This gene encodes a member of the fibrillar collagen
            family, and plays a role during the calcification of cartilage and
            the transition of cartilage to bone. The encoded protein product is
            a preproprotein. It includes an N-terminal signal peptide, which is
            followed by an N-terminal propetide, mature peptide and a
            C-terminal propeptide. The N-terminal propeptide contains
            thrombospondin N-terminal-like and laminin G-like domains. The
            mature peptide is a major triple-helical region. The C-terminal
            propeptide, also known as COLFI domain, plays crucial roles in
            tissue growth and repair. Mutations in this gene cause Steel
            syndrome. Alternatively spliced transcript variants have been
            found, but the full-length nature of some variants has not been
            determined. [provided by RefSeq, Sep 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY149237.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356083.8/ ENSP00000348385.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..1860
                     /product="collagen alpha-1(XXVII) chain preproprotein"
                     /note="collagen alpha-1(XXVII) chain; collagen, type
                     XXVII, alpha 1"
                     /calculated_mol_wt=182957
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3955
     proprotein      42..1860
                     /product="collagen alpha-1(XXVII) chain proprotein"
                     /calculated_mol_wt=182957
     Region          45..220
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cl22861"
                     /db_xref="CDD:473984"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZC6.1)"
     Region          <274..605
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          278..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC6.1)"
     mat_peptide     625..1621
                     /product="Collagen alpha-1(XXVII) chain.
                     /id=PRO_5000089163"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC6.1)"
                     /calculated_mol_wt=94791
     Region          625..1618
                     /region_name="Triple-helical region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC6.1)"
     Region          625..772
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC6.1)"
     Region          <709..>989
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          851..1625
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC6.1)"
     Region          <974..>1249
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1183..>1449
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1369..>1598
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1661..1859
                     /region_name="COLFI"
                     /note="Fibrillar collagen C-terminal domain; cl02436"
                     /db_xref="CDD:470578"
     Site            1769
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZC6.1)"
     CDS             1..1860
                     /gene="COL27A1"
                     /gene_synonym="STLS"
                     /coded_by="NM_032888.4:415..5997"
                     /db_xref="CCDS:CCDS6802.1"
                     /db_xref="GeneID:85301"
                     /db_xref="HGNC:HGNC:22986"
                     /db_xref="MIM:608461"
ORIGIN      
        1 mgagsargar gtaaaaaarg ggflfswilv sfachlastq gapedvdilq rlglswtkag
       61 spappgvipf qsgfiftqra rlqaptgtvi paalgtelal vlslcshrvn haflfavrsq
      121 krklqlglqf lpgktvvhlg srrsvafdld mhdgrwhhla lelrgrtvtl vtacgqrrvp
      181 vllpfhrdpa ldpggsflfg kmnphavqfe galcqfsiyp vtqvahnyct hlrkqcgqad
      241 tyqsplgplf sqdsgrpftf qsdlallgle nlttatpalg slpagrgprg tvapatptkp
      301 qrtsptnphq hmavggpaqt pllpaklsas naldpmlpas vggstrtprp aaaqpsqkit
      361 atkipkslpt kpsapstsiv piksphptqk tapssftksa lptqkqvppt srpvparvsr
      421 paekpiqrnp gmprppppst rplppttsss kkpiptlart eakitshask pasartsthk
      481 pppftalsss paptpgstrs trppatmvpp tsgtstprta pavptpgsap tgskkpigse
      541 askkagpkss prkpvplrpg kaardvplsd lttrpsprqp qpsqqttpal vlapaqflss
      601 sprptssgys ifhlagstpf pllmgppgpk gdcglpgppg lpglpgipga rgprgppgpy
      661 gnpglpgppg akgqkgdpgl spgkahdgak gdmglpglsg npgppgrkgh kgypgpaghp
      721 geqgqpgpeg spgakgypgr qglpgpvgdp gpkgsrgyig lpglfglpgs dgerglpgvp
      781 gkrgkmgmpg fpgvfgergp pgldgnpgel glpgppgvpg ligdlgvlgp igypgpkgmk
      841 glmgsvgepg lkgdkgeqgv pgvsgdpgfq gdkgsqglpg fpgargkpgp lgkvgdkgsi
      901 gfpgppgpeg fpgdigppgd ngpegmkgkp garglpgprg qlgpegdegp mgppgapgle
      961 gqpgrkgfpg rpgldgvkge pgdpgrpgpv geqgfmgfig lvgepgivge kgdrgmmgpp
     1021 gvpgpkgsmg hpgmpggmgt pgepgpqgpp gsrgppgmrg akgrrgprgp dgpageqgsr
     1081 glkgppgpqg rpgrpgqqgv agerghlgsr gfpgipgpsg ppgtkglpge pgpqgpqgpi
     1141 gppgemgpkg ppgavgepgl pgeagmkgdl gplgtpgeqg ligqrgepgl egdsgpmgpd
     1201 glkgdrgdpg pdgehgekgq eglmgedgpp gppgvtgvrg pegksgkqge kgrtgakgak
     1261 gyqgqlgemg vpgdpgppgt pgpkgsrgsl gptgapgrmg aqgepglagy dghkgivgpl
     1321 gppgpkgekg eqgedgkaeg ppgppgdrgp vgdrgdrgep gdpgypgqeg vqglrgkpgq
     1381 qgqpghpgpr gwpgpkgskg aegpkgkqgk agapgrrgvq glqglpgprg vvgrqglegi
     1441 agpdglpgrd gqagqqgeqg ddgdpgpmgp agkrgnpgva glpgaqgppg fkgesglpgq
     1501 lgppgkrgte grtglpgnqg epgskgqpgd sgemgfpgma glfgpkgppg digfkgiqgp
     1561 rgppglmgke givgplgilg psglpgpkgd kgsrgdwglq gprgppgprg rpgppgppgg
     1621 piqlqqddlg aafqtwmdts galrpesysy pdrlvldqgg eifktlhyls nliqsiktpl
     1681 gtkenparvc rdlmdceqkm vdgtywvdpn lgcssdtiev scnfthggqt clkpitaskv
     1741 efaisrvqmn flhllssevt qhitihclnm tvwqegtgqt pakqavrfra wngqifeagg
     1801 qfrpevsmdg ckvqdgrwhq tlftfrtqdp qqlpiisvdn lppassgkqy rlevgpacfl
//
LOCUS       NP_055685               1239 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 40 isoform a [Homo
            sapiens].
ACCESSION   NP_055685
VERSION     NP_055685.3
DBSOURCE    REFSEQ: accession NM_014870.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1239)
  AUTHORS   Zhou,M., Cui,Y., Zuo,S., Peng,Q., Liu,Y., Li,X., Yang,Y., He,Q.,
            Yu,X., Zhou,J., He,Z. and He,Q.
  TITLE     ZBTB40 is a telomere-associated protein and protects telomeres in
            human ALT cells
  JOURNAL   J Biol Chem 299 (9), 105053 (2023)
   PUBMED   37454741
  REMARK    GeneRIF: ZBTB40 is a telomere-associated protein and protects
            telomeres in human ALT cells.
REFERENCE   2  (residues 1 to 1239)
  AUTHORS   Cushing,K.C., Chen,Y., Du,X., Chen,V., Kuppa,A., Higgins,P. and
            Speliotes,E.K.
  TITLE     Risk Variants in or Near ZBTB40 AND NFATC1 Increase the Risk of
            Both IBD and Adverse Bone Health Outcomes Highlighting Common
            Genetic Underpinnings Across Both Diseases
  JOURNAL   Inflamm Bowel Dis 29 (6), 938-945 (2023)
   PUBMED   36680554
  REMARK    GeneRIF: Risk Variants in or Near ZBTB40 AND NFATC1 Increase the
            Risk of Both IBD and Adverse Bone Health Outcomes Highlighting
            Common Genetic Underpinnings Across Both Diseases.
REFERENCE   3  (residues 1 to 1239)
  AUTHORS   Doolittle,M.L., Calabrese,G.M., Mesner,L.D., Godfrey,D.A.,
            Maynard,R.D., Ackert-Bicknell,C.L. and Farber,C.R.
  TITLE     Genetic analysis of osteoblast activity identifies Zbtb40 as a
            regulator of osteoblast activity and bone mass
  JOURNAL   PLoS Genet 16 (6), e1008805 (2020)
   PUBMED   32497039
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1239)
  AUTHORS   Hu,Y., Lao,L., Mao,J., Jin,W., Luo,H., Charpentier,T., Qi,S.,
            Peng,J., Hu,B., Marcinkiewicz,M.M., Lamarre,A. and Wu,J.
  TITLE     Armc5 deletion causes developmental defects and compromises T-cell
            immune responses
  JOURNAL   Nat Commun 8, 13834 (2017)
   PUBMED   28169274
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1239)
  AUTHORS   Zhang,L., Choi,H.J., Estrada,K., Leo,P.J., Li,J., Pei,Y.F.,
            Zhang,Y., Lin,Y., Shen,H., Liu,Y.Z., Liu,Y., Zhao,Y., Zhang,J.G.,
            Tian,Q., Wang,Y.P., Han,Y., Ran,S., Hai,R., Zhu,X.Z., Wu,S.,
            Yan,H., Liu,X., Yang,T.L., Guo,Y., Zhang,F., Guo,Y.F., Chen,Y.,
            Chen,X., Tan,L., Zhang,L., Deng,F.Y., Deng,H., Rivadeneira,F.,
            Duncan,E.L., Lee,J.Y., Han,B.G., Cho,N.H., Nicholson,G.C.,
            McCloskey,E., Eastell,R., Prince,R.L., Eisman,J.A., Jones,G.,
            Reid,I.R., Sambrook,P.N., Dennison,E.M., Danoy,P.,
            Yerges-Armstrong,L.M., Streeten,E.A., Hu,T., Xiang,S.,
            Papasian,C.J., Brown,M.A., Shin,C.S., Uitterlinden,A.G. and
            Deng,H.W.
  TITLE     Multistage genome-wide association meta-analyses identified two new
            loci for bone mineral density
  JOURNAL   Hum Mol Genet 23 (7), 1923-1933 (2014)
   PUBMED   24249740
REFERENCE   6  (residues 1 to 1239)
  AUTHORS   Liu,J.M., Zhang,M.J., Zhao,L., Cui,B., Li,Z.B., Zhao,H.Y.,
            Sun,L.H., Tao,B., Li,M. and Ning,G.
  TITLE     Analysis of recently identified osteoporosis susceptibility genes
            in Han Chinese women
  JOURNAL   J Clin Endocrinol Metab 95 (9), E112-E120 (2010)
   PUBMED   20554715
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1239)
  AUTHORS   Rivadeneira,F., Styrkarsdottir,U., Estrada,K., Halldorsson,B.V.,
            Hsu,Y.H., Richards,J.B., Zillikens,M.C., Kavvoura,F.K., Amin,N.,
            Aulchenko,Y.S., Cupples,L.A., Deloukas,P., Demissie,S.,
            Grundberg,E., Hofman,A., Kong,A., Karasik,D., van Meurs,J.B.,
            Oostra,B., Pastinen,T., Pols,H.A., Sigurdsson,G., Soranzo,N.,
            Thorleifsson,G., Thorsteinsdottir,U., Williams,F.M., Wilson,S.G.,
            Zhou,Y., Ralston,S.H., van Duijn,C.M., Spector,T., Kiel,D.P.,
            Stefansson,K., Ioannidis,J.P. and Uitterlinden,A.G.
  CONSRTM   Genetic Factors for Osteoporosis (GEFOS) Consortium
  TITLE     Twenty bone-mineral-density loci identified by large-scale
            meta-analysis of genome-wide association studies
  JOURNAL   Nat Genet 41 (11), 1199-1206 (2009)
   PUBMED   19801982
REFERENCE   8  (residues 1 to 1239)
  AUTHORS   Styrkarsdottir,U., Halldorsson,B.V., Gretarsdottir,S.,
            Gudbjartsson,D.F., Walters,G.B., Ingvarsson,T., Jonsdottir,T.,
            Saemundsdottir,J., Center,J.R., Nguyen,T.V., Bagger,Y.,
            Gulcher,J.R., Eisman,J.A., Christiansen,C., Sigurdsson,G., Kong,A.,
            Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Multiple genetic loci for bone mineral density and fractures
  JOURNAL   N Engl J Med 358 (22), 2355-2365 (2008)
   PUBMED   18445777
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1239)
  AUTHORS   Matsuoka,S., Ballif,B.A., Smogorzewska,A., McDonald,E.R. 3rd,
            Hurov,K.E., Luo,J., Bakalarski,C.E., Zhao,Z., Solimini,N.,
            Lerenthal,Y., Shiloh,Y., Gygi,S.P. and Elledge,S.J.
  TITLE     ATM and ATR substrate analysis reveals extensive protein networks
            responsive to DNA damage
  JOURNAL   Science 316 (5828), 1160-1166 (2007)
   PUBMED   17525332
REFERENCE   10 (residues 1 to 1239)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA787818.1, BC114607.1, DA248977.1 and AL035703.21.
            
            On Apr 3, 2007 this sequence version replaced NP_055685.2.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.215422.1,
                                           SRR1803612.220868.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375647.5/ ENSP00000364798.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1239
                     /product="zinc finger and BTB domain-containing protein 40
                     isoform a"
                     /note="zinc finger and BTB domain-containing protein 40"
                     /calculated_mol_wt=137988
     Region          1..116
                     /region_name="BTB_POZ_ZBTB40"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 40 (ZBTB40); cd18225"
                     /db_xref="CDD:349534"
     Region          130..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUA8.4)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NUA8.4)"
     Region          687..732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUA8.4)"
     Site            703
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q9NUA8.4)"
     Region          768..789
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          779..801
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUA8.4)"
     Region          <794..970
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          809..830
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          838..858
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(843,845,847,849..850,853..854,857,871,873,877,907,
                     910..911,914,928,930,932,934..935,938..939,942)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          866..915
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <917..1031
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          923..942
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          952..970
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          <1001..1069
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          1008..1028
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1048..1066
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1077..1098
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1082,1084,1086,1088..1089,1092..1093,1096,1111,1113,
                     1117..1118,1121..1122,1125,1142,1144,1146,1148..1149,
                     1152..1153)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1106..1127
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1137..1154
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1239
                     /gene="ZBTB40"
                     /gene_synonym="ZNF923"
                     /coded_by="NM_014870.4:224..3943"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS224.1"
                     /db_xref="GeneID:9923"
                     /db_xref="HGNC:HGNC:29045"
                     /db_xref="MIM:612106"
ORIGIN      
        1 melpnysrql lqqlytlcke qqfcdctisi gtiyfrahkl vlaaasllfk tlldntdtis
       61 idasvvspee falllemmyt gklpvgkhnf skiisladsl qmfdvavsck nlltslvncs
      121 vqgqvvrdvs apssetfrke pekpqveils segagephss pelaatpggp vkaeteeaah
      181 svsqemsvns ptaqesqrna etpaetptta eacspspavq tfseakktst epgcerkhyq
      241 lnfllenegv fsdalmvtqd vlkklemcse ikgpqkemiv kcfegegghs afqrilgkvr
      301 eesldvqtvv sllrlyqysn pavktalldr kpedvdtvqp kgsteegktl svlllehked
      361 liqcvtqlrp imesletake efltgtekrv ilnccegrtp ketienllhr mteektltae
      421 glvkllqavk ttfpnlglll eklqksatlp sttvqpspdd ygtellrryh enlseiftdn
      481 qillkmishm tslapgerev meklvkrdsg sggfnslisa vlekqtlsat aiwqlllvvq
      541 etktcpldll meeirrepga daffravttp ehatletilr hnqlileaiq qkieyklfts
      601 eeehlaetvk eilsipseta speaslravl srameksvpa ieichllcsv hksfpglqpv
      661 mqelayigvl tkedgeketw kvsnkfhlea nnkedekaak edsqpgeqnd qgetgslpgq
      721 qekeasaspd pakksficka cdksfhfycr lkvhmkrcrv akskqvqcke csetkdskke
      781 ldkhqleahg aggepdapkk kkkrlpvtcd lcgrefahas gmqyhklteh fdekpfscee
      841 cgakfaanst lknhlrlhtg drpfmckhcl mtftqasala yhtkkkhseg kmyacqycda
      901 vfaqsielsr hvrthtgdkp yvcrdcgkgf rqanglsihl htfhniedpy dckkcrmsfp
      961 tlqdhrkhih evhskeyhpc ptcgkifsap smlerhvvth vggkpfscgi cnkayqqlsg
     1021 lwyhnrthhp dvfaaqnhrs skfsslqcss cdktfpntie hkkhikaeha dmkfhecdqc
     1081 kelfptpall qvhvkcqhsg sqpfrclyca atfrfpgalq hhvttehfkq settfpcelc
     1141 gelftsqaql dshlesehpk vmstetqaaa sqmaqviqtp epvapteqvi tleetqlags
     1201 qvfvtlpdsq asqasselva vtvedlldgt vtlicgeak
//
LOCUS       NP_006067                481 aa            linear   PRI 27-APR-2025
DEFINITION  arf-GAP domain and FG repeat-containing protein 2 [Homo sapiens].
ACCESSION   NP_006067
VERSION     NP_006067.3
DBSOURCE    REFSEQ: accession NM_006076.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Doria,M., Salcini,A.E., Colombo,E., Parslow,T.G., Pelicci,P.G. and
            Di Fiore,P.P.
  TITLE     The eps15 homology (EH) domain-based interaction between eps15 and
            hrb connects the molecular machinery of endocytosis to that of
            nucleocytosolic transport
  JOURNAL   J Cell Biol 147 (7), 1379-1384 (1999)
   PUBMED   10613896
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Glockner,G., Scherer,S., Schattevoy,R., Boright,A., Weber,J.,
            Tsui,L.C. and Rosenthal,A.
  TITLE     Large-scale sequencing of two regions in human chromosome 7q22:
            analysis of 650 kb of genomic sequence around the EPO and CUTL1
            loci reveals 17 genes
  JOURNAL   Genome Res 8 (10), 1060-1073 (1998)
   PUBMED   9799793
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Salcini,A.E., Confalonieri,S., Doria,M., Santolini,E., Tassi,E.,
            Minenkova,O., Cesareni,G., Pelicci,P.G. and Di Fiore,P.P.
  TITLE     Binding specificity and in vivo targets of the EH domain, a novel
            protein-protein interaction module
  JOURNAL   Genes Dev 11 (17), 2239-2249 (1997)
   PUBMED   9303539
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Wong,W.T., Schumacher,C., Salcini,A.E., Romano,A., Castagnino,P.,
            Pelicci,P.G. and Di Fiore,P.P.
  TITLE     A protein-binding domain, EH, identified in the receptor tyrosine
            kinase substrate Eps15 and conserved in evolution
  JOURNAL   Proc Natl Acad Sci U S A 92 (21), 9530-9534 (1995)
   PUBMED   7568168
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC069281.6, BF310674.1,
            AK314954.1, BC017329.2, AK090744.1 and BC047227.1.
            
            On Apr 13, 2006 this sequence version replaced NP_006067.2.
            
            Summary: This gene is a member of the HIV-1 Rev binding protein
            (HRB) family and encodes a protein with one Arf-GAP zinc finger
            domain, several phe-gly (FG) motifs, and four asn-pro-phe (NPF)
            motifs. This protein interacts with Eps15 homology (EH) domains and
            plays a role in the Rev export pathway, which mediates the
            nucleocytoplasmic transfer of proteins and RNAs. Alternatively
            spliced transcript variants have been described, but their
            biological validity has not been determined. [provided by RefSeq,
            Feb 2013].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.162403.1,
                                           SRR3476690.1060030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300176.9/ ENSP00000300176.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..481
                     /product="arf-GAP domain and FG repeat-containing protein
                     2"
                     /note="Rev/Rex activation domain binding protein-related;
                     arf-GAP domain and FG repeats-containing protein 2;
                     nucleoporin; HIV-1 Rev-binding protein-like protein;
                     rev/Rex activation domain-binding protein related"
                     /calculated_mol_wt=48832
     Region          30..146
                     /region_name="ArfGap_AGFG2"
                     /note="ArfGAP domain of AGFG2 (ArfGAP domain and FG
                     repeat-containing protein 2); cd17903"
                     /db_xref="CDD:350090"
     Site            order(47,50,67,70,75)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350090"
     Site            order(47,50,67,70)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350090"
     Region          <146..479
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          150..220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95081.2)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95081.2)"
     Region          271..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95081.2)"
     Region          431..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95081.2)"
     CDS             1..481
                     /gene="AGFG2"
                     /gene_synonym="HRBL; RABR"
                     /coded_by="NM_006076.5:145..1590"
                     /db_xref="CCDS:CCDS5697.1"
                     /db_xref="GeneID:3268"
                     /db_xref="HGNC:HGNC:5177"
                     /db_xref="MIM:604019"
ORIGIN      
        1 mvmaakkgpg pgggvsggka eaeaasevwc rrvrelggcs qagnrhcfec aqrgvtyvdi
       61 tvgsfvcttc sgllrglnpp hrvksismtt ftepevvflq srgnevcrki wlglfdarts
      121 lvpdsrdpqk vkeflqekye kkrwyvppdq vkgptytkgs astpvqgsip egkplrtllg
      181 dpapslsvaa stssqpvsqs hartsqarst qppphssvkk astdlladig gdpfaapqma
      241 pafaafpafg gqtpsqggfa nfdafssgps ssvfgslppa gqasfqaqpt pagssqgtpf
      301 gatplapasq pnsladvgsf lgpgvpaagv psslfgmagq vpplqsvtmg ggggsstgla
      361 fgaftnpfta paaqsplpst npfqpnglap gpgfgmssag pgfpqavppt gafassfpap
      421 lfppqtplvq qqngssfgdl gsaklgqrpl sqpagistnp fmtgpssspf askppttnpf
      481 l
//
LOCUS       NP_954993                571 aa            linear   PRI 27-APR-2025
DEFINITION  isthmin-2 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_954993
VERSION     NP_954993.1
DBSOURCE    REFSEQ: accession NM_199296.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Rossi,V., Beffagna,G., Rampazzo,A., Bauce,B. and Danieli,G.A.
  TITLE     TAIL1: an isthmin-like gene, containing type 1
            thrombospondin-repeat and AMOP domain, mapped to ARVD1 critical
            region
  JOURNAL   Gene 335, 101-108 (2004)
   PUBMED   15194193
  REMARK    GeneRIF: TAIL1 gene is located on chromosome 14q24.3 within ARVD1
            (arrhythmogenic right ventricular dysplasia/cardiomyopathy, type 1)
            critical region; preliminary evidence suggests that it is expressed
            in several tissues, showing multiple alternative splicing.
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Bork,P.
  TITLE     The modular architecture of a new family of growth regulators
            related to connective tissue growth factor
  JOURNAL   FEBS Lett 327 (2), 125-130 (1993)
   PUBMED   7687569
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB025298.1, BX248277.1,
            AJ583024.1 and BC033140.1.
            
            Summary: The protein encoded by this gene contains a type 1
            thrombospondin domain, which is present in thrombospondin, a number
            of proteins involved in the complement pathway, as well as in
            extracellular matrix proteins. Two alternatively spliced transcript
            variants encoding distinct isoforms have been observed. [provided
            by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749863.1, AK075445.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342219.9/ ENSP00000341490.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..571
                     /product="isthmin-2 isoform 1 precursor"
                     /note="thrombospondin, type I, domain containing 3;
                     thrombospondin and AMOP containing isthmin-like 1;
                     thrombospondin type-1 domain-containing protein 3;
                     thrombospondin and AMOP domain-containing isthmin-like
                     protein 1; isthmin 2 homolog"
                     /calculated_mol_wt=61188
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2736
     Region          30..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6H9L7.1)"
     Region          116..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6H9L7.1)"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6H9L7.1)"
     Region          257..294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6H9L7.1)"
     Site            300
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6H9L7.1)"
     Region          331..371
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            392
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6H9L7.1)"
     Region          396..559
                     /region_name="AMOP"
                     /note="Adhesion-associated domain present in MUC4 and
                     other proteins; smart00723"
                     /db_xref="CDD:128962"
     CDS             1..571
                     /gene="ISM2"
                     /gene_synonym="TAIL1; THSD3"
                     /coded_by="NM_199296.3:24..1739"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9864.1"
                     /db_xref="GeneID:145501"
                     /db_xref="HGNC:HGNC:23176"
                     /db_xref="MIM:612684"
ORIGIN      
        1 mralrdragl llcvlllaal leaalglpvk kprlrgprpg sltrlaevsa spdprplkee
       61 eeapllprth lqaephqhgc wtvtepaamt pgnatpprtp evtplrlelq klpglanttl
      121 stpnpdtqas aspdprplre eeearllprt hlqaelhqhg cwtvtepaal tpgnatpprt
      181 qevtplllel qklpelvhat lstpnpdnqv tikvvedpqa evsidllaep snpppqdtls
      241 wlpalwsflw gdykgeekdr apgekgeeke ededypsedi egedqedkee deeeqalwfn
      301 gttdnwdqgw lapgdwvfkd svsydyepqk ewspwspcsg ncstgkqqrt rpcgygctat
      361 etrtcdlpsc pgtedkdtlg lpseewklla rnatdmhdqd vdscekwlnc ksdflikyls
      421 qmlrdlpscp caypleamds pvslqdehqg rsfrwrdasg prerldiyqp tarfclrsml
      481 sgesstlaaq hccydedsrl ltrgkgagmp nlistdfspk lhfkfdttpw ilckgdwsrl
      541 havlppnngr actdnpleee ylaqlqeake y
//
LOCUS       NP_056470                751 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 337 [Homo sapiens].
ACCESSION   NP_056470
VERSION     NP_056470.1
DBSOURCE    REFSEQ: accession NM_015655.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP201424.1, AK291235.1, BC021298.2, AL031673.19 and BX113975.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a zinc finger domain containing protein.
            The function of this protein has yet to be determined. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Mar 2014].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.268215.1,
                                           SRR3476690.163167.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252979.6/ ENSP00000252979.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.21"
     Protein         1..751
                     /product="zinc finger protein 337"
                     /calculated_mol_wt=86744
     Region          12..71
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          101..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3M9.2)"
     Region          182..202
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(182,185,198,202)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          210..230
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(210,213,226,230)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          234..626
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          238..258
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(238,241,254,258)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          266..286
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          294..314
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(294,297,310,314)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          322..342
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(322,325,338,342)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          350..370
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(350,353,366,370)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(355,357,359,361..362,365..366,369,383,385,389..390,
                     393..394,397,411,413,415,417..418,421..422,425)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          378..398
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          406..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          434..454
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          462..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          490..510
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(518,521,534,538)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(574,577,590,594)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          602..622
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(602,605,618,622)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(607,609,611,613..614,617..618,621,635,637,641..642,
                     645..646,649,663,665,667,669..670,673..674,678)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          630..650
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          658..679
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          687..707
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          699..724
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          715..735
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..751
                     /gene="ZNF337"
                     /coded_by="NM_015655.4:145..2400"
                     /db_xref="CCDS:CCDS13174.1"
                     /db_xref="GeneID:26152"
                     /db_xref="HGNC:HGNC:15809"
ORIGIN      
        1 mgpqgarrqa flafgdvtvd ftqkewrlls paqralyrev tlenyshlvs lgilhskpel
       61 irrleqgevp wgeerrrrpg pcagiyaehv lrpknlglah qrqqqlqfsd qsfqsdtaeg
      121 qekekstkpm afsspplrha vssrrrnsvv eiessqgqre npteidkvlk giensrwgaf
      181 kcaergqdfs rkmmviihkk ahsrqklftc rechqgfrde salllhqnth tgeksyvcsv
      241 cgrgfslkan llrhqrthsg ekpflckvcg rgytsksylt vherthtgek pyecqecgrr
      301 fndkssynkh lkahsgekpf vckecgrgyt nksyfvvhkr ihsgekpyrc qecgrgfsnk
      361 shlithqrth sgekpfacrq ckqsfsvkgs llrhqrthsg ekpfvckdce rsfsqkstlv
      421 yhqrthsgek pfvcrecgqg fiqkstlvkh qithseekpf vckdcgrgfi qkstftlhqr
      481 thseekpygc recgrrfrdk ssynkhlrah lgekrffcrd cgrgftlkpn ltihqrthsg
      541 ekpfmckqce ksfslkanll rhqwthsger pfnckdcgrg filkstllfh qkthsgekpf
      601 icsecgqgfi wksnlvkhql ahsgkqpfvc kecgrgfnwk gnllthqrth sgekpfvcnv
      661 cgqgfswkrs ltrhhwrihs kekpfvcqec krgytsksdl tvherihtge rpyecqecgr
      721 kfsnksyysk hlkrhlrekr fctgsvgeas s
//
LOCUS       NP_008964                196 aa            linear   PRI 27-APR-2025
DEFINITION  protein RER1 [Homo sapiens].
ACCESSION   NP_008964
VERSION     NP_008964.3
DBSOURCE    REFSEQ: accession NM_007033.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Chen,S., Zhang,J., Chen,J., Wang,Y., Zhou,S., Huang,L., Bai,Y.,
            Peng,C., Shen,B., Chen,H. and Tian,Y.
  TITLE     RER1 enhances carcinogenesis and stemness of pancreatic cancer
            under hypoxic environment
  JOURNAL   J Exp Clin Cancer Res 38 (1), 15 (2019)
   PUBMED   30630537
  REMARK    GeneRIF: The present study has demonstrated that RER1 enhances the
            progression of PC through promoting cell proliferation, migration
            and aggressiveness.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Hara,T., Maejima,I., Akuzawa,T., Hirai,R., Kobayashi,H.,
            Tsukamoto,S., Tsunoda,M., Ono,A., Yamakoshi,S., Oikawa,S. and
            Sato,K.
  TITLE     Rer1-mediated quality control system is required for neural stem
            cell maintenance during cerebral cortex development
  JOURNAL   PLoS Genet 14 (9), e1007647 (2018)
   PUBMED   30260951
  REMARK    GeneRIF: Study in knockout mice and genetically modified human HAP1
            cell line suggests that Rer1 maintains Notch signaling by
            maintaining sufficient expression of the gamma-secretase complex on
            the cell surface and regulating neural stem cell maintenance during
            cerebral cortex development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Park,H.J., Ryu,D., Parmar,M., Giasson,B.I. and McFarland,N.R.
  TITLE     The ER retention protein RER1 promotes alpha-synuclein degradation
            via the proteasome
  JOURNAL   PLoS One 12 (9), e0184262 (2017)
   PUBMED   28877262
  REMARK    GeneRIF: RER1 is a novel and potential important mediator of
            elevated alphaSyn levels
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Hara,T., Hashimoto,Y., Akuzawa,T., Hirai,R., Kobayashi,H. and
            Sato,K.
  TITLE     Rer1 and calnexin regulate endoplasmic reticulum retention of a
            peripheral myelin protein 22 mutant that causes type 1A
            Charcot-Marie-Tooth disease
  JOURNAL   Sci Rep 4, 6992 (2014)
   PUBMED   25385046
  REMARK    GeneRIF: Charcot-Marie-Tooth disease-related PMP22 is trapped in
            the endoplasmic reticulum by calnexin-dependent retention and
            Rer1-mediated early Golgi retrieval systems and partly degraded by
            the Hrd1-mediated endoplasmic reticulum-associated degradation
            system.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Jurisch-Yaksi,N., Rose,A.J., Lu,H., Raemaekers,T., Munck,S.,
            Baatsen,P., Baert,V., Vermeire,W., Scales,S.J., Verleyen,D.,
            Vandepoel,R., Tylzanowski,P., Yaksi,E., de Ravel,T., Yost,H.J.,
            Froyen,G., Arrington,C.B. and Annaert,W.
  TITLE     Rer1p maintains ciliary length and signaling by regulating
            gamma-secretase activity and Foxj1a levels
  JOURNAL   J Cell Biol 200 (6), 709-720 (2013)
   PUBMED   23479743
  REMARK    GeneRIF: Rer1p depletion reduced ciliary length and function by
            increasing gamma-secretase complex assembly and activity and,
            consequently, enhancing Notch signaling as well as reducing Foxj1a
            expression.
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Tanabe,C., Maeda,T., Zou,K., Liu,J., Liu,S., Nakajima,T. and
            Komano,H.
  TITLE     The ubiquitin ligase synoviolin up-regulates amyloid beta
            production by targeting a negative regulator of gamma-secretase,
            Rer1, for degradation
  JOURNAL   J Biol Chem 287 (53), 44203-44211 (2012)
   PUBMED   23129766
  REMARK    GeneRIF: Synoviolin up-regulates amyloid beta production by
            targeting a negative regulator of gamma-secretase, Rer1, for
            degradation.
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Park,H.J., Shabashvili,D., Nekorchuk,M.D., Shyqyriu,E., Jung,J.I.,
            Ladd,T.B., Moore,B.D., Felsenstein,K.M., Golde,T.E. and Kim,S.H.
  TITLE     Retention in endoplasmic reticulum 1 (RER1) modulates amyloid-beta
            (Abeta) production by altering trafficking of gamma-secretase and
            amyloid precursor protein (APP)
  JOURNAL   J Biol Chem 287 (48), 40629-40640 (2012)
   PUBMED   23043097
  REMARK    GeneRIF: RER1 modulates amyloid-beta production by altering
            trafficking of gamma-secretase and amyloid precursor protein.
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Kaether,C., Scheuermann,J., Fassler,M., Zilow,S., Shirotani,K.,
            Valkova,C., Novak,B., Kacmar,S., Steiner,H. and Haass,C.
  TITLE     Endoplasmic reticulum retention of the gamma-secretase complex
            component Pen2 by Rer1
  JOURNAL   EMBO Rep 8 (8), 743-748 (2007)
   PUBMED   17668005
  REMARK    GeneRIF: Downregulation of Rer1 leads to increased surface
            localization of Pen2, whereas overexpression of Rer1 stabilizes
            unassembled Pen2. Rer1 is the first identified interaction partner
            of mammalian transmembrane-based retention/retrieval signals.
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Fullekrug,J., Boehm,J., Rottger,S., Nilsson,T., Mieskes,G. and
            Schmitt,H.D.
  TITLE     Human Rer1 is localized to the Golgi apparatus and complements the
            deletion of the homologous Rer1 protein of Saccharomyces cerevisiae
  JOURNAL   Eur J Cell Biol 74 (1), 31-40 (1997)
   PUBMED   9309388
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA409924.1, BC004965.1,
            AL513477.21 and BM682824.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 28, 2006 this sequence version replaced NP_008964.2.
            
            Summary: The protein encoded by this gene is a multi-pass membrane
            protein that is localized to the golgi apparatus. It is involved in
            the retention of endoplasmic reticulum (ER) membrane proteins in
            the ER and retrieval of ER membrane proteins from the early Golgi
            compartment to facilitate gamma-secretase complex assembly.
            [provided by RefSeq, Oct 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.211887.1,
                                           SRR1803615.42637.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000605895.6/ ENSP00000475168.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.32"
     Protein         1..196
                     /product="protein RER1"
                     /note="RER1 retention in endoplasmic reticulum 1 homolog"
                     /calculated_mol_wt=22827
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:25489052,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (O15258.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15258.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O15258.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15258.1)"
     Region          20..184
                     /region_name="Rer1"
                     /note="Rer1 family; pfam03248"
                     /db_xref="CDD:460860"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15258.1)"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15258.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O15258.1)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15258.1)"
     CDS             1..196
                     /gene="RER1"
                     /coded_by="NM_007033.5:126..716"
                     /db_xref="CCDS:CCDS41232.1"
                     /db_xref="GeneID:11079"
                     /db_xref="HGNC:HGNC:30309"
                     /db_xref="MIM:620048"
ORIGIN      
        1 msegdsvges vhgkpsvvyr fftrlgqiyq swldkstpyt avrwvvtlgl sfvymirvyl
       61 lqgwyivtya lgiyhlnlfi aflspkvdps lmedsddgps lptkqneefr pfirrlpefk
      121 fwhaatkgil vamvctffda fnvpvfwpil vmyfimlfci tmkrqikhmi kyryipfthg
      181 krryrgkeda gkafas
//
LOCUS       NP_000430                753 aa            linear   PRI 27-APR-2025
DEFINITION  neuroendocrine convertase 1 isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_000430
VERSION     NP_000430.3
DBSOURCE    REFSEQ: accession NM_000439.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Manco,L., Albuquerque,D., Aranda,B., Rodrigues,D.,
            Machado-Rodrigues,A.M. and Padez,C.
  TITLE     Differential sex-association between PCSK1 polymorphisms and
            obesity risk in Portuguese children
  JOURNAL   Am J Hum Biol 36 (5), e24023 (2024)
   PUBMED   38009939
  REMARK    GeneRIF: Differential sex-association between PCSK1 polymorphisms
            and obesity risk in Portuguese children.
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Guijo,B., Argente,J. and Martos-Moreno,G.A.
  TITLE     The N221D variant in PCSK1 is highly prevalent in childhood obesity
            and can influence the metabolic profile
  JOURNAL   J Pediatr Endocrinol Metab 36 (12), 1140-1145 (2023)
   PUBMED   37877373
  REMARK    GeneRIF: The N221D variant in PCSK1 is highly prevalent in
            childhood obesity and can influence the metabolic profile.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Velazquez-Roman,J., Angulo-Zamudio,U.A., Leon-Sicairos,N.,
            Flores-Villasenor,H., Benitez-Baez,M., Espinoza-Salomon,A.,
            Karam-Leon,A., Villamil-Ramirez,H., Canizales-Quinteros,S.,
            Macias-Kauffer,L., Monroy-Higuera,J., Acosta-Smith,E. and
            Canizalez-Roman,A.
  TITLE     Association of PCSK1 and PPARG1 Allelic Variants with Obesity and
            Metabolic Syndrome in Mexican Adults
  JOURNAL   Genes (Basel) 14 (9), 1775 (2023)
   PUBMED   37761915
  REMARK    GeneRIF: Association of PCSK1 and PPARG1 Allelic Variants with
            Obesity and Metabolic Syndrome in Mexican Adults.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Shah,B.P., Sleiman,P.M., Mc Donald,J., Moeller,I.H. and Kleyn,P.
  TITLE     Functional characterization of all missense variants in LEPR,
            PCSK1, and POMC genes arising from single-nucleotide variants
  JOURNAL   Expert Rev Endocrinol Metab 18 (2), 209-219 (2023)
   PUBMED   36864747
  REMARK    GeneRIF: Functional characterization of all missense variants in
            LEPR, PCSK1, and POMC genes arising from single-nucleotide
            variants.
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Folon,L., Baron,M., Toussaint,B., Vaillant,E., Boissel,M.,
            Scherrer,V., Loiselle,H., Leloire,A., Badreddine,A., Balkau,B.,
            Charpentier,G., Franc,S., Marre,M., Aboulouard,S., Salzet,M.,
            Canouil,M., Derhourhi,M., Froguel,P. and Bonnefond,A.
  TITLE     Contribution of heterozygous PCSK1 variants to obesity and
            implications for precision medicine: a case-control study
  JOURNAL   Lancet Diabetes Endocrinol 11 (3), 182-190 (2023)
   PUBMED   36822744
  REMARK    GeneRIF: Contribution of heterozygous PCSK1 variants to obesity and
            implications for precision medicine: a case-control study.
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Benjannet,S., Reudelhuber,T., Mercure,C., Rondeau,N., Chretien,M.
            and Seidah,N.G.
  TITLE     Proprotein conversion is determined by a multiplicity of factors
            including convertase processing, substrate specificity, and
            intracellular environment. Cell type-specific processing of human
            prorenin by the convertase PC1
  JOURNAL   J Biol Chem 267 (16), 11417-11423 (1992)
   PUBMED   1597471
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Seidah,N.G., Hamelin,J., Gaspar,A.M., Day,R. and Chretien,M.
  TITLE     The cDNA sequence of the human pro-hormone and pro-protein
            convertase PC1
  JOURNAL   DNA Cell Biol 11 (4), 283-289 (1992)
   PUBMED   1605851
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Creemers,J.W., Roebroek,A.J. and Van de Ven,W.J.
  TITLE     Expression in human lung tumor cells of the proprotein processing
            enzyme PC1/PC3. Cloning and primary sequence of a 5 kb cDNA
  JOURNAL   FEBS Lett 300 (1), 82-88 (1992)
   PUBMED   1547893
REFERENCE   9  (residues 1 to 753)
  AUTHORS   Seidah,N.G., Mattei,M.G., Gaspar,L., Benjannet,S., Mbikay,M. and
            Chretien,M.
  TITLE     Chromosomal assignments of the genes for neuroendocrine convertase
            PC1 (NEC1) to human 5q15-21, neuroendocrine convertase PC2 (NEC2)
            to human 20p11.1-11.2, and furin (mouse 7[D1-E2] region)
  JOURNAL   Genomics 11 (1), 103-107 (1991)
   PUBMED   1765368
REFERENCE   10 (residues 1 to 753)
  AUTHORS   Sanke,T., Bell,G.I., Sample,C., Rubenstein,A.H. and Steiner,D.F.
  TITLE     An islet amyloid peptide is derived from an 89-amino acid precursor
            by proteolytic processing
  JOURNAL   J Biol Chem 263 (33), 17243-17246 (1988)
   PUBMED   3053705
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA192592.1, X64810.1 and
            AC008951.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 28, 2002 this sequence version replaced NP_000430.2.
            
            Summary: This gene encodes a member of the subtilisin-like
            proprotein convertase family, which includes proteases that process
            protein and peptide precursors trafficking through regulated or
            constitutive branches of the secretory pathway. The encoded protein
            undergoes an initial autocatalytic processing event in the ER to
            generate a heterodimer which exits the ER and sorts to subcellular
            compartments where a second autocatalytic even takes place and the
            catalytic activity is acquired. The protease is packaged into and
            activated in dense core secretory granules and expressed in the
            neuroendocrine system and brain. This gene encodes one of the seven
            basic amino acid-specific members which cleave their substrates at
            single or paired basic residues. It functions in the proteolytic
            activation of polypeptide hormones and neuropeptides precursors.
            Mutations in this gene have been associated with susceptibility to
            obesity and proprotein convertase 1/3 deficiency. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene [provided by RefSeq, Jan 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.27882.1,
                                           SRR1660803.86657.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311106.8/ ENSP00000308024.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q15"
     Protein         1..753
                     /product="neuroendocrine convertase 1 isoform 1
                     preproprotein"
                     /EC_number="3.4.21.93"
                     /note="prohormone convertase 3; prohormone convertase 1;
                     neuroendocrine convertase 1; proprotein convertase 1/3"
                     /calculated_mol_wt=81092
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29120.2)"
                     /calculated_mol_wt=3078
     proprotein      28..753
                     /product="neuroendocrine convertase 1 isoform 1
                     proprotein"
                     /calculated_mol_wt=81092
     Region          34..110
                     /region_name="S8_pro-domain"
                     /note="Peptidase S8 pro-domain; pfam16470"
                     /db_xref="CDD:465126"
     mat_peptide     111..753
                     /product="neuroendocrine convertase 1 isoform 1"
                     /calculated_mol_wt=71376
     Region          121..415
                     /region_name="Peptidases_S8_Protein_convertases_Kexins_Fur
                     in-lik"
                     /note="Peptidase S8 family domain in Protein convertases;
                     cd04059"
                     /db_xref="CDD:173789"
     Site            order(123,176,222)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173789"
     Site            order(167..168,203,208,250,268,278,309,320,382)
                     /site_type="active"
                     /db_xref="CDD:173789"
     Site            order(167,208,382)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173789"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29120.2)"
     Site            order(315,345)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173789"
     Site            order(323,325,328,330)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:173789"
     Site            401
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29120.2)"
     Region          504..591
                     /region_name="P_proprotein"
                     /note="Proprotein convertase P-domain; pfam01483"
                     /db_xref="CDD:460225"
     Region          596..662
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29120.2)"
     Site            632
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:23234360; propagated from
                     UniProtKB/Swiss-Prot (P29120.2)"
     Region          713..751
                     /region_name="Proho_convert"
                     /note="Prohormone convertase enzyme; pfam12177"
                     /db_xref="CDD:463483"
     CDS             1..753
                     /gene="PCSK1"
                     /gene_synonym="BMIQ12; NEC1; PC1; PC1/3; PC3; SPC3"
                     /coded_by="NM_000439.5:207..2468"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4081.1"
                     /db_xref="GeneID:5122"
                     /db_xref="HGNC:HGNC:8743"
                     /db_xref="MIM:162150"
ORIGIN      
        1 merrawslqc tafvlfcawc alnsakakrq fvnewaaeip ggpeaasaia eelgydllgq
       61 igslenhylf khknhprrsr rsafhitkrl sdddrviwae qqyekerskr salrdsalnl
      121 fndpmwnqqw ylqdtrmtaa lpkldlhvip vwqkgitgkg vvitvlddgl ewnhtdiyan
      181 ydpeasydfn dndhdpfpry dptnenkhgt rcageiamqa nnhkcgvgva ynskvggirm
      241 ldgivtdaie assigfnpgh vdiysaswgp nddgktvegp grlaqkafey gvkqgrqgkg
      301 sifvwasgng grqgdncdcd gytdsiytis issasqqgls pwyaekcsst latsyssgdy
      361 tdqritsadl hndctethtg tsasaplaag ifalaleanp nltwrdmqhl vvwtseydpl
      421 annpgwkkng aglmvnsrfg fgllnakalv dladprtwrs vpekkecvvk dndfepralk
      481 angeviieip tracegqena ikslehvqfe atieysrrgd lhvtltsaag tstvllaere
      541 rdtspngfkn wdfmsvhtwg enpigtwtlr itdmsgriqn egrivnwkli lhgtssqpeh
      601 mkqprvytsy ntvqndrrgv ekmvdpgeeq ptqenpkent lvskspssss vggrrdelee
      661 gapsqamlrl lqsafsknsp pkqspkksps aklnipyenf yealeklnkp sqlkdsedsl
      721 yndyvdvfyn tkpykhrddr llqalvdiln een
//
LOCUS       NP_001354271             115 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 142 isoform 4 [Homo sapiens].
ACCESSION   NP_001354271
VERSION     NP_001354271.1
DBSOURCE    REFSEQ: accession NM_001367342.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Mir,A., Song,Y., Lee,H., Montazer-Zohouri,M., Reisi,M. and
            Tabatabaiefar,M.A.
  TITLE     A deleterious frameshift insertion mutation in the ZNF142 gene
            leads to intellectual developmental disorder with impaired speech
            in three affected siblings: Clinical features and literature review
  JOURNAL   Mol Genet Genomic Med 11 (12), e2261 (2023)
   PUBMED   37496384
  REMARK    GeneRIF: A deleterious frameshift insertion mutation in the ZNF142
            gene leads to intellectual developmental disorder with impaired
            speech in three affected siblings: Clinical features and literature
            review.
            Review article
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Christensen,M.B., Levy,A.M., Mohammadi,N.A., Niceta,M.,
            Kaiyrzhanov,R., Dentici,M.L., Al Alam,C., Alesi,V., Benoit,V.,
            Bhatia,K.P., Bierhals,T., Bosselmann,C.M., Buratti,J.,
            Callewaert,B., Ceulemans,B., Charles,P., De Wachter,M.,
            Dehghani,M., D'haenens,E., Doco-Fenzy,M., Gessner,M., Gobert,C.,
            Guliyeva,U., Haack,T.B., Hammer,T.B., Heinrich,T., Hempel,M.,
            Herget,T., Hoffmann,U., Horvath,J., Houlden,H., Keren,B.,
            Kresge,C., Kumps,C., Lederer,D., Lermine,A., Magrinelli,F.,
            Maroofian,R., Vahidi Mehrjardi,M.Y., Moudi,M., Muller,A.J.,
            Oostra,A.J., Pletcher,B.A., Ros-Pardo,D., Samarasekera,S.,
            Tartaglia,M., Van Schil,K., Vogt,J., Wassmer,E., Winkelmann,J.,
            Zaki,M.S., Zech,M., Lerche,H., Radio,F.C., Gomez-Puertas,P.,
            Moller,R.S. and Tumer,Z.
  TITLE     Biallelic variants in ZNF142 lead to a syndromic neurodevelopmental
            disorder
  JOURNAL   Clin Genet 102 (2), 98-109 (2022)
   PUBMED   35616059
  REMARK    GeneRIF: Biallelic variants in ZNF142 lead to a syndromic
            neurodevelopmental disorder.
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Kamal,N., Khamirani,H.J., Mohammadi,S., Dastgheib,S.A.,
            Dianatpour,M. and Tabei,S.M.B.
  TITLE     ZNF142 mutation causes neurodevelopmental disorder with speech
            impairment and seizures: Novel variants and literature review
  JOURNAL   Eur J Med Genet 65 (7), 104522 (2022)
   PUBMED   35618198
  REMARK    GeneRIF: ZNF142 mutation causes neurodevelopmental disorder with
            speech impairment and seizures: Novel variants and literature
            review.
            Review article
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Kameyama,S., Mizuguchi,T., Fukuda,H., Moey,L.H., Keng,W.T.,
            Okamoto,N., Tsuchida,N., Uchiyama,Y., Koshimizu,E., Hamanaka,K.,
            Fujita,A., Miyatake,S. and Matsumoto,N.
  TITLE     Biallelic null variants in ZNF142 cause global developmental delay
            with familial epilepsy and dysmorphic features
  JOURNAL   J Hum Genet 67 (3), 169-173 (2022)
   PUBMED   34531528
  REMARK    GeneRIF: Biallelic null variants in ZNF142 cause global
            developmental delay with familial epilepsy and dysmorphic features.
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Ahmeti,K.B., Ajroud-Driss,S., Al-Chalabi,A., Andersen,P.M.,
            Armstrong,J., Birve,A., Blauw,H.M., Brown,R.H., Bruijn,L., Chen,W.,
            Chio,A., Comeau,M.C., Cronin,S., Diekstra,F.P., Soraya Gkazi,A.,
            Glass,J.D., Grab,J.D., Groen,E.J., Haines,J.L., Hardiman,O.,
            Heller,S., Huang,J., Hung,W.Y., Jaworski,J.M., Jones,A., Khan,H.,
            Landers,J.E., Langefeld,C.D., Leigh,P.N., Marion,M.C.,
            McLaughlin,R.L., Meininger,V., Melki,J., Miller,J.W., Mora,G.,
            Pericak-Vance,M.A., Rampersaud,E., Robberecht,W., Russell,L.P.,
            Salachas,F., Saris,C.G., Shatunov,A., Shaw,C.E., Siddique,N.,
            Siddique,T., Smith,B.N., Sufit,R., Topp,S., Traynor,B.J., Vance,C.,
            van Damme,P., van den Berg,L.H., van Es,M.A., van Vught,P.W.,
            Veldink,J.H., Yang,Y. and Zheng,J.G.
  CONSRTM   ITALSGEN consortium; ALSGEN Consortium
  TITLE     Age of onset of amyotrophic lateral sclerosis is modulated by a
            locus on 1p34.1
  JOURNAL   Neurobiol Aging 34 (1), 357 (2013)
   PUBMED   22959728
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079810.4 and AC012510.8.
            
            Summary: The protein encoded by this gene belongs to the Kruppel
            family of C2H2-type zinc finger proteins. It contains 31 C2H2-type
            zinc fingers and may be involved in transcriptional regulation.
            Alternatively spliced transcript variants have been found for this
            gene. [provided by RefSeq, Jan 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.139761.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..115
                     /product="zinc finger protein 142 isoform 4"
                     /note="zinc finger protein 142 (clone pHZ-49)"
                     /calculated_mol_wt=11607
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52746.4)"
     CDS             1..115
                     /gene="ZNF142"
                     /gene_synonym="HA4654; NEDISHM; pHZ-49"
                     /coded_by="NM_001367342.1:543..890"
                     /note="isoform 4 is encoded by transcript variant 10"
                     /db_xref="GeneID:7701"
                     /db_xref="HGNC:HGNC:12927"
                     /db_xref="MIM:604083"
ORIGIN      
        1 mtdplldsqp asstgemdgl cpelllippp lsnrgilgpv qspcpsrdpa piptepgcll
       61 veatateegp gnmeiivetv agtltpgapg etpgtntvas rpvgqaalrf clgyf
//
LOCUS       NP_001186253             742 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 615 isoform 1 [Homo sapiens].
ACCESSION   NP_001186253
VERSION     NP_001186253.1
DBSOURCE    REFSEQ: accession NM_001199324.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Kimura,K., Wakamatsu,A., Suzuki,Y., Ota,T., Nishikawa,T.,
            Yamashita,R., Yamamoto,J., Sekine,M., Tsuritani,K., Wakaguri,H.,
            Ishii,S., Sugiyama,T., Saito,K., Isono,Y., Irie,R., Kushida,N.,
            Yoneyama,T., Otsuka,R., Kanda,K., Yokoi,T., Kondo,H., Wagatsuma,M.,
            Murakawa,K., Ishida,S., Ishibashi,T., Takahashi-Fujii,A.,
            Tanase,T., Nagai,K., Kikuchi,H., Nakai,K., Isogai,T. and Sugano,S.
  TITLE     Diversification of transcriptional modulation: large-scale
            identification and characterization of putative alternative
            promoters of human genes
  JOURNAL   Genome Res 16 (1), 55-65 (2006)
   PUBMED   16344560
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA095942.1, BC112961.1, BC053884.1, BX647556.1 and AC011460.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.85780.1,
                                           SRR1660803.134500.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000598071.6/ ENSP00000471041.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..742
                     /product="zinc finger protein 615 isoform 1"
                     /calculated_mol_wt=84502
     Region          8..68
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <95..425
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..321
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(306,308,310,312..313,316..317,320,334,336,340..341,
                     344..345,348,362,364,366,368..369,372..373,376)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          325..729
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          329..349
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          385..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(418,420,422,424..425,428..429,432,446,448,452..453,
                     456..457,460,474,476,478,480..481,484..485,488)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          525..545
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          553..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(558,560,562,564..565,568..569,572,586,588,592..593,
                     596..597,600,614,616,618,620..621,624..625,628)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          581..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          609..629
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          637..657
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          665..685
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(670,672,674,676..677,680..681,684,698,700,704..705,
                     708..709,712,726,728,730,732..733,736..737,740)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          693..713
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          721..741
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..742
                     /gene="ZNF615"
                     /coded_by="NM_001199324.2:299..2527"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS59418.1"
                     /db_xref="GeneID:284370"
                     /db_xref="HGNC:HGNC:24740"
ORIGIN      
        1 mmqaqesltl edvavdftwe ewqflspaqk dlyrdvmlen ysnlvavgyq askpdalskl
       61 ergeetctte deiysricsd sggasggaya eirkiddplq hhlqnqsiqk svkqcheqnm
      121 fgnivnqnkg hfllkqdcdt fdlhekplks nlsfenqkrs sglknsaefn rdgkslfhan
      181 hkqfytemkf paiakpinks qfikqqrthn ienahvcsec gkaflklsqf idhqrvhtge
      241 kphvcsmcgk afsrksrlmd hqrthtelkh yectecdktf lkksqlnihq kthmggkpyt
      301 csqcgkafik kcrliyhqrt htgekphgcs vcgkafstkf sltthqktht gekpyicsec
      361 gkgfiekrrl tahhrthtge kpficnkcgk gftlknslit hqqthtgekl ytcsecgkgf
      421 smkhclmvhq rthtgekpyk cnecgkgfal ksplirhqrt htgekpyvct ecrkgftmks
      481 dlivhqrtht aekpyicndc gkgftvksrl ivhqrthtge kpyvcgecgk gfpakirlmg
      541 hqrthtgekp yicnecgkgf tekshlnvhr rthtgekpyv csecgkgltg ksmliahqrt
      601 htgekpyicn ecgkgftmks tlsihqqtht gekpykcnec dktfrkktcl iqhqrfhtgk
      661 tsfactecgk fslrkndlit hqrihtgekp ykcsdcgkaf ttksglnvhq rkhtgerpyg
      721 csdcgkafah lsilvkhrri hr
//
LOCUS       NP_004218                399 aa            linear   PRI 27-APR-2025
DEFINITION  cytohesin-3 isoform a [Homo sapiens].
ACCESSION   NP_004218
VERSION     NP_004218.1
DBSOURCE    REFSEQ: accession NM_004227.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Fu,Y., Li,J., Feng,M.X., Yang,X.M., Wang,Y.H., Zhang,Y.L., Qin,W.,
            Xia,Q. and Zhang,Z.G.
  TITLE     Cytohesin-3 is upregulated in hepatocellular carcinoma and
            contributes to tumor growth and vascular invasion
  JOURNAL   Int J Clin Exp Pathol 7 (5), 2123-2132 (2014)
   PUBMED   24966920
  REMARK    GeneRIF: Cytohesin-3 was upregulated in hepatocellular carcinoma
            tissues, correlating with overall survival/relapse-free survival
            and tumor size/vascular invasion.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Malaby,A.W., van den Berg,B. and Lambright,D.G.
  TITLE     Structural basis for membrane recruitment and allosteric activation
            of cytohesin family Arf GTPase exchange factors
  JOURNAL   Proc Natl Acad Sci U S A 110 (35), 14213-14218 (2013)
   PUBMED   23940353
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Nevrivy,D.J., Peterson,V.J., Avram,D., Ishmael,J.E., Hansen,S.G.,
            Dowell,P., Hruby,D.E., Dawson,M.I. and Leid,M.
  TITLE     Interaction of GRASP, a protein encoded by a novel retinoic
            acid-induced gene, with members of the cytohesin family of guanine
            nucleotide exchange factors
  JOURNAL   J Biol Chem 275 (22), 16827-16836 (2000)
   PUBMED   10828067
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Ogasawara,M., Kim,S.C., Adamik,R., Togawa,A., Ferrans,V.J.,
            Takeda,K., Kirby,M., Moss,J. and Vaughan,M.
  TITLE     Similarities in function and gene structure of cytohesin-4 and
            cytohesin-1, guanine nucleotide-exchange proteins for
            ADP-ribosylation factors
  JOURNAL   J Biol Chem 275 (5), 3221-3230 (2000)
   PUBMED   10652308
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Venkateswarlu,K., Gunn-Moore,F., Oatey,P.B., Tavare,J.M. and
            Cullen,P.J.
  TITLE     Nerve growth factor- and epidermal growth factor-stimulated
            translocation of the ADP-ribosylation factor-exchange factor GRP1
            to the plasma membrane of PC12 cells requires activation of
            phosphatidylinositol 3-kinase and the GRP1 pleckstrin homology
            domain
  JOURNAL   Biochem J 335 (Pt 1) (Pt 1), 139-146 (1998)
   PUBMED   9742223
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Franco,M., Boretto,J., Robineau,S., Monier,S., Goud,B., Chardin,P.
            and Chavrier,P.
  TITLE     ARNO3, a Sec7-domain guanine nucleotide exchange factor for ADP
            ribosylation factor 1, is involved in the control of Golgi
            structure and function
  JOURNAL   Proc Natl Acad Sci U S A 95 (17), 9926-9931 (1998)
   PUBMED   9707577
REFERENCE   10 (residues 1 to 399)
  AUTHORS   Klarlund,J.K., Guilherme,A., Holik,J.J., Virbasius,J.V., Chawla,A.
            and Czech,M.P.
  TITLE     Signaling by phosphoinositide-3,4,5-trisphosphate through proteins
            containing pleckstrin and Sec7 homology domains
  JOURNAL   Science 275 (5308), 1927-1930 (1997)
   PUBMED   9072969
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009412.6, CB988199.1,
            AJ223957.1, BG620295.1 and BC028717.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the PSCD (pleckstrin
            homology, Sec7 and coiled-coil domains) family. PSCD family members
            have identical structural organization that consists of an
            N-terminal coiled-coil motif, a central Sec7 domain, and a
            C-terminal pleckstrin homology (PH) domain. The coiled-coil motif
            is involved in homodimerization, the Sec7 domain contains
            guanine-nucleotide exchange protein (GEP) activity, and the PH
            domain interacts with phospholipids and is responsible for
            association of PSCDs with membranes. Members of this family appear
            to mediate the regulation of protein sorting and membrane
            trafficking. This encoded protein is involved in the control of
            Golgi structure and function, and it may have a physiological role
            in regulating ADP-ribosylation factor protein 6 (ARF) functions, in
            addition to acting on ARF1. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028717.1, SRR1803616.73428.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000350796.8/ ENSP00000297044.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..399
                     /product="cytohesin-3 isoform a"
                     /note="pleckstrin homology, Sec7 and coiled-coil domains
                     3; ARF nucleotide-binding site opener 3; general receptor
                     of phosphoinositides 1; PH, SEC7 and coiled-coil
                     domain-containing protein 3"
                     /calculated_mol_wt=46161
     Region          66..248
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          263..382
                     /region_name="PH_GRP1-like"
                     /note="General Receptor for Phosphoinositides-1-like
                     Pleckstrin homology (PH) domain; cd01252"
                     /db_xref="CDD:269954"
     Site            order(263,290,292,294,304,307,309,340..342,344,347..352,
                     382)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:269954"
     Site            order(273,276,280,282,284,295,305,343,354..355)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269954"
     Region          391..399
                     /region_name="C-terminal autoinhibitory region.
                     /evidence=ECO:0000269|PubMed:23940353"
                     /note="propagated from UniProtKB/Swiss-Prot (O43739.2)"
     CDS             1..399
                     /gene="CYTH3"
                     /gene_synonym="ARNO3; cytohesin-3; GRP1; PSCD3"
                     /coded_by="NM_004227.4:118..1317"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5346.1"
                     /db_xref="GeneID:9265"
                     /db_xref="HGNC:HGNC:9504"
                     /db_xref="MIM:605081"
ORIGIN      
        1 mdedgggegg gvpedlslee reelldirrr kkeliddier lkyeiaevmt eidnltsvee
       61 skttqrnkqi amgrkkfnmd pkkgiqflie ndllqssped vaqflykgeg lnktvigdyl
      121 gerdefnikv lqafvelhef adlnlvqalr qflwsfrlpg eaqkidrmme afasryclcn
      181 pgvfqstdtc yvlsfaiiml ntslhnhnvr dkptaerfia mnrgineggd lpeellrnly
      241 esiknepfki peddgndlth tffnpdregw llklggrvkt wkrrwfiltd nclyyfeytt
      301 dkeprgiipl enlsireved prkpncfely npshkgqvik ackteadgrv vegnhvvyri
      361 sapspeekee wmksikasis rdpfydmlat rkrriankk
//
LOCUS       NP_001135                643 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase AMFR isoform c [Homo sapiens].
ACCESSION   NP_001135
VERSION     NP_001135.3
DBSOURCE    REFSEQ: accession NM_001144.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Deng,R., Medico-Salsench,E., Nikoncuk,A., Ramakrishnan,R.,
            Lanko,K., Kuhn,N.A., van der Linde,H.C., Lor-Zade,S.,
            Albuainain,F., Shi,Y., Yousefi,S., Capo,I., van den Herik,E.M., van
            Slegtenhorst,M., van Minkelen,R., Geeven,G., Mulder,M.T.,
            Ruijter,G.J.G., Lutjohann,D., Jacobs,E.H., Houlden,H.,
            Pagnamenta,A.T., Metcalfe,K., Jackson,A., Banka,S., De Simone,L.,
            Schwaede,A., Kuntz,N., Palculict,T.B., Abbas,S., Umair,M.,
            AlMuhaizea,M., Colak,D., AlQudairy,H., Alsagob,M., Pereira,C.,
            Trunzo,R., Karageorgou,V., Bertoli-Avella,A.M., Bauer,P.,
            Bouman,A., Hoefsloot,L.H., van Ham,T.J., Issa,M., Zaki,M.S.,
            Gleeson,J.G., Willemsen,R., Kaya,N., Arold,S.T., Maroofian,R.,
            Sanderson,L.E. and Barakat,T.S.
  TITLE     AMFR dysfunction causes autosomal recessive spastic paraplegia in
            human that is amenable to statin treatment in a preclinical model
  JOURNAL   Acta Neuropathol 146 (2), 353-368 (2023)
   PUBMED   37119330
  REMARK    GeneRIF: AMFR dysfunction causes autosomal recessive spastic
            paraplegia in human that is amenable to statin treatment in a
            preclinical model.
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Xu,J., Ma,H., Wang,Q. and Zhang,H.
  TITLE     Expression of autocrine motility factor receptor (AMFR) in human
            breast and lung invasive micropapillary carcinomas
  JOURNAL   Int J Exp Pathol 104 (1), 43-51 (2023)
   PUBMED   36576071
  REMARK    GeneRIF: Expression of autocrine motility factor receptor (AMFR) in
            human breast and lung invasive micropapillary carcinomas.
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Zhang,H., Wei,R., Yang,X., Xu,L., Jiang,H., Li,M., Jiang,H.,
            Zhang,H., Chen,Z., Qian,F. and Sun,L.
  TITLE     AMFR drives allergic asthma development by promoting alveolar
            macrophage-derived GM-CSF production
  JOURNAL   J Exp Med 219 (5) (2022)
   PUBMED   35333296
  REMARK    GeneRIF: AMFR drives allergic asthma development by promoting
            alveolar macrophage-derived GM-CSF production.
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Zheng,S., Zhao,D., Hou,G., Zhao,S., Zhang,W., Wang,X., Li,L.,
            Lin,L., Tang,T.S. and Hu,Y.
  TITLE     iASPP suppresses Gp78-mediated TMCO1 degradation to maintain Ca2+
            homeostasis and control tumor growth and drug resistance
  JOURNAL   Proc Natl Acad Sci U S A 119 (6) (2022)
   PUBMED   35121659
  REMARK    GeneRIF: iASPP suppresses Gp78-mediated TMCO1 degradation to
            maintain Ca(2+) homeostasis and control tumor growth and drug
            resistance.
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Mookherjee,D., Das,S., Mukherjee,R., Bera,M., Jana,S.C.,
            Chakrabarti,S. and Chakrabarti,O.
  TITLE     RETREG1/FAM134B mediated autophagosomal degradation of AMFR/GP78
            and OPA1 -a dual organellar turnover mechanism
  JOURNAL   Autophagy 17 (7), 1729-1752 (2021)
   PUBMED   32559118
  REMARK    GeneRIF: RETREG1/FAM134B mediated autophagosomal degradation of
            AMFR/GP78 and OPA1 -a dual organellar turnover mechanism.
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Luo,Y., Long,J.M., Lu,C., Chan,S.L., Spangler,E.L., Mascarucci,P.,
            Raz,A., Longo,D.L., Mattson,M.P., Ingram,D.K. and Weng,N.P.
  TITLE     A link between maze learning and hippocampal expression of
            neuroleukin and its receptor gp78
  JOURNAL   J Neurochem 80 (2), 354-361 (2002)
   PUBMED   11902125
  REMARK    GeneRIF: hippocampal expression of NLK and its receptor gp78 is
            associated with maze learning in rats.
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Fang,S., Ferrone,M., Yang,C., Jensen,J.P., Tiwari,S. and
            Weissman,A.M.
  TITLE     The tumor autocrine motility factor receptor, gp78, is a ubiquitin
            protein ligase implicated in degradation from the endoplasmic
            reticulum
  JOURNAL   Proc Natl Acad Sci U S A 98 (25), 14422-14427 (2001)
   PUBMED   11724934
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Shimizu,K., Tani,M., Watanabe,H., Nagamachi,Y., Niinaka,Y.,
            Shiroishi,T., Ohwada,S., Raz,A. and Yokota,J.
  TITLE     The autocrine motility factor receptor gene encodes a novel type of
            seven transmembrane protein
  JOURNAL   FEBS Lett 456 (2), 295-300 (1999)
   PUBMED   10456327
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Huang,B., Xie,Y. and Raz,A.
  TITLE     Identification of an upstream region that controls the
            transcription of the human autocrine motility factor receptor
  JOURNAL   Biochem Biophys Res Commun 212 (3), 727-742 (1995)
   PUBMED   7626106
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Watanabe,H., Carmi,P., Hogan,V., Raz,T., Silletti,S., Nabi,I.R. and
            Raz,A.
  TITLE     Purification of human tumor cell autocrine motility factor and
            molecular cloning of its receptor
  JOURNAL   J Biol Chem 266 (20), 13442-13448 (1991)
   PUBMED   1649192
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092140.4, BC069197.1,
            BX345849.2, CA748782.1, AC009102.10, BX409690.2 and AA767223.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 22, 2002 this sequence version replaced NP_001135.2.
            
            Summary: This locus encodes a glycosylated transmembrane receptor.
            Its ligand, autocrine motility factor, is a tumor
            motility-stimulating protein secreted by tumor cells. The encoded
            receptor is also a member of the E3 ubiquitin ligase family of
            proteins. It catalyzes ubiquitination and endoplasmic
            reticulum-associated degradation of specific proteins. [provided by
            RefSeq, Feb 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.88703.1,
                                           SRR1803617.150525.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000290649.10/ ENSP00000290649.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..643
                     /product="E3 ubiquitin-protein ligase AMFR isoform c"
                     /EC_number="2.3.2.36"
                     /note="RING finger protein 45; E3 ubiquitin-protein ligase
                     AMFR; RING-type E3 ubiquitin transferase AMFR"
                     /calculated_mol_wt=72865
     Region          39..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Region          86..>382
                     /region_name="HRD1"
                     /note="HRD ubiquitin ligase complex, ER membrane component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5243"
                     /db_xref="CDD:227568"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Site            276..296
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Region          339..382
                     /region_name="RING-H2_AMFR"
                     /note="RING finger, H2 subclass, found in autocrine
                     motility factor receptor (AMFR) and similar proteins;
                     cd16455"
                     /db_xref="CDD:438119"
     Site            order(342..346,367..368,371..372,376..377,379)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438119"
     Site            429..449
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Region          458..498
                     /region_name="CUE_AMFR"
                     /note="CUE domain found in autocrine motility factor
                     receptor (AMFR) and similar proteins; cd14421"
                     /db_xref="CDD:270604"
     Region          504..579
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Region          575..600
                     /region_name="G2BR"
                     /note="E3 gp78 Ube2g2-binding region (G2BR); pfam18442"
                     /db_xref="CDD:375868"
     Region          596..624
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     Region          622..640
                     /region_name="VCP/p97-interacting motif (VIM).
                     /evidence=ECO:0000269|PubMed:21914798"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV5.2)"
     CDS             1..643
                     /gene="AMFR"
                     /gene_synonym="GP78; RNF45; SPG89"
                     /coded_by="NM_001144.6:219..2150"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS10758.1"
                     /db_xref="GeneID:267"
                     /db_xref="HGNC:HGNC:463"
                     /db_xref="MIM:603243"
ORIGIN      
        1 mpllflerfp wpslrtytgl sglallgtii sayralsqpe agpgepdqlt aslqpeppap
       61 arpsaggpra rdvaqyllsd slfvwvlvnt accvlmlvak liqcivfgpl rvserqhlkd
      121 kfwnfifykf ififgvlnvq tveevvmwcl wfaglvflhl mvqlckdrfe ylsfspttpm
      181 sshgrvlsll vamllsccgl aavcsitgyt hgmhtlafma aesllvtvrt ahvilryvih
      241 lwdlnhegtw egkgtyvyyt dfvmeltlls ldlmhhihml lfgniwlsma slvifmqlry
      301 lfhevqrrir rhknylrvvg nmearfavat peelavnndd caicwdsmqa arklpcghlf
      361 hnsclrswle qdtscptcrm slniadnnrv reehqgenld enlvpvaaae grprlnqhnh
      421 ffhfdgsria swlpsfsvev mhttnilgit qasnsqlnam ahqiqemfpq vpyhlvlqdl
      481 qltrsveitt dnilegriqv pfptqrsdsi rpalnspver pssdqeeget saqtervpld
      541 lsprleetld fgevevepse vedfeargsr fsksaderqr mlvqrkdell qqarkrflnk
      601 sseddaases flpsegassd pvtlrrrmla aaaerrlqkq qts
//
LOCUS       NP_001347638             336 aa            linear   ROD 27-APR-2025
DEFINITION  apoptosis-enhancing nuclease isoform 1 [Mus musculus].
ACCESSION   NP_001347638 XP_006541200
VERSION     NP_001347638.1
DBSOURCE    REFSEQ: accession NM_001360709.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Bizen,N., Bepari,A.K., Zhou,L., Abe,M., Sakimura,K., Ono,K. and
            Takebayashi,H.
  TITLE     Ddx20, an Olig2 binding factor, governs the survival of neural and
            oligodendrocyte progenitor cells via proper Mdm2 splicing and p53
            suppression
  JOURNAL   Cell Death Differ 29 (5), 1028-1041 (2022)
   PUBMED   34974536
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Tiu,G.C., Kerr,C.H., Forester,C.M., Krishnarao,P.S.,
            Rosenblatt,H.D., Raj,N., Lantz,T.C., Zhulyn,O., Bowen,M.E.,
            Shokat,L., Attardi,L.D., Ruggero,D. and Barna,M.
  TITLE     A p53-dependent translational program directs tissue-selective
            phenotypes in a model of ribosomopathies
  JOURNAL   Dev Cell 56 (14), 2089-2102 (2021)
   PUBMED   34242585
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Ulmke,P.A., Xie,Y., Sokpor,G., Pham,L., Shomroni,O., Berulava,T.,
            Rosenbusch,J., Basu,U., Fischer,A., Nguyen,H.P., Staiger,J.F. and
            Tuoc,T.
  TITLE     Post-transcriptional regulation by the exosome complex is required
            for cell survival and forebrain development via repression of P53
            signaling
  JOURNAL   Development 148 (3) (2021)
   PUBMED   33462115
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CX211663.1, AC138376.11 and AK031972.1.
            
            On Feb 9, 2018 this sequence version replaced XP_006541200.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1 and 3 both encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3512191.1,
                                           SRR11927936.1278225.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849376
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 44.83 cM"
     Protein         1..336
                     /product="apoptosis-enhancing nuclease isoform 1"
                     /EC_number="3.1.-.-"
                     /note="interferon stimulated exonuclease gene 20-like 1;
                     interferon-stimulated 20 kDa exonuclease-like 1"
                     /calculated_mol_wt=37178
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZI9.1)"
     Region          25..33
                     /region_name="Nucleolar localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZI9.1)"
     Region          56..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZI9.1)"
     Region          110..266
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Site            order(113..116,192..193,195..197,257)
                     /site_type="active"
                     /db_xref="CDD:99852"
     Site            order(113,115,197,257)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99852"
     Site            order(114..116,192..193,195..196,257)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99852"
     Region          164..187
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZI9.1)"
     Region          276..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZI9.1)"
     CDS             1..336
                     /gene="Aen"
                     /gene_synonym="2700083B06Rik; Isg20l1"
                     /coded_by="NM_001360709.1:209..1219"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS39988.2"
                     /db_xref="GeneID:68048"
                     /db_xref="MGI:MGI:1915298"
ORIGIN      
        1 mvagevpest qcpsltslnt kdvvrrrhkr rsrqhqrfma rkallqeqel lstapgpglc
       61 llpspsqmpa vteasdsrrq rpkarsgsng lcskksvpre aprpgpikcv aidcemvgtg
      121 pqgrvselar csvvsysgdv lydkyirpem pivdyrtrws gitrqhmhka ipfqvaqkei
      181 lkllkgkvvv ghalhndfqa lkyvhprsqt rdttyvpnll sqpsslirtr vslkdlalnl
      241 lhkkiqvghq ghssvedamt amelyqlvev qweqqvassa qapaedrgpd sstdveqymd
      301 dqywpedltq stgaetnggp drqegeegqg arsapp
//
LOCUS       NP_777597                586 aa            linear   PRI 27-APR-2025
DEFINITION  transcription elongation regulator 1-like protein [Homo sapiens].
ACCESSION   NP_777597
VERSION     NP_777597.2
DBSOURCE    REFSEQ: accession NM_174937.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Chen,G., Bentley,A., Adeyemo,A., Shriner,D., Zhou,J., Doumatey,A.,
            Huang,H., Ramos,E., Erdos,M., Gerry,N., Herbert,A., Christman,M.
            and Rotimi,C.
  TITLE     Genome-wide association study identifies novel loci association
            with fasting insulin and insulin resistance in African Americans
  JOURNAL   Hum Mol Genet 21 (20), 4530-4536 (2012)
   PUBMED   22791750
  REMARK    GeneRIF: TCERG1L is associated with plasma adiponectin, a key
            modulator of obesity, inflammation, IR and diabetes.
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Service,S.K., Verweij,K.J., Lahti,J., Congdon,E., Ekelund,J.,
            Hintsanen,M., Raikkonen,K., Lehtimaki,T., Kahonen,M., Widen,E.,
            Taanila,A., Veijola,J., Heath,A.C., Madden,P.A., Montgomery,G.W.,
            Sabatti,C., Jarvelin,M.R., Palotie,A., Raitakari,O., Viikari,J.,
            Martin,N.G., Eriksson,J.G., Keltikangas-Jarvinen,L., Wray,N.R. and
            Freimer,N.B.
  TITLE     A genome-wide meta-analysis of association studies of Cloninger's
            Temperament Scales
  JOURNAL   Transl Psychiatry 2 (5), e116 (2012)
   PUBMED   22832960
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Kenny,E.E., Pe'er,I., Karban,A., Ozelius,L., Mitchell,A.A.,
            Ng,S.M., Erazo,M., Ostrer,H., Abraham,C., Abreu,M.T., Atzmon,G.,
            Barzilai,N., Brant,S.R., Bressman,S., Burns,E.R., Chowers,Y.,
            Clark,L.N., Darvasi,A., Doheny,D., Duerr,R.H., Eliakim,R.,
            Giladi,N., Gregersen,P.K., Hakonarson,H., Jones,M.R., Marder,K.,
            McGovern,D.P., Mulle,J., Orr-Urtreger,A., Proctor,D.D., Pulver,A.,
            Rotter,J.I., Silverberg,M.S., Ullman,T., Warren,S.T., Waterman,M.,
            Zhang,W., Bergman,A., Mayer,L., Katz,S., Desnick,R.J., Cho,J.H. and
            Peter,I.
  TITLE     A genome-wide scan of Ashkenazi Jewish Crohn's disease suggests
            novel susceptibility loci
  JOURNAL   PLoS Genet 8 (3), e1002559 (2012)
   PUBMED   22412388
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Sim,X., Ong,R.T., Suo,C., Tay,W.T., Liu,J., Ng,D.P., Boehnke,M.,
            Chia,K.S., Wong,T.Y., Seielstad,M., Teo,Y.Y. and Tai,E.S.
  TITLE     Transferability of type 2 diabetes implicated loci in multi-ethnic
            cohorts from Southeast Asia
  JOURNAL   PLoS Genet 7 (4), e1001363 (2011)
   PUBMED   21490949
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Neale,B.M., Medland,S., Ripke,S., Anney,R.J., Asherson,P.,
            Buitelaar,J., Franke,B., Gill,M., Kent,L., Holmans,P.,
            Middleton,F., Thapar,A., Lesch,K.P., Faraone,S.V., Daly,M.,
            Nguyen,T.T., Schafer,H., Steinhausen,H.C., Reif,A., Renner,T.J.,
            Romanos,M., Romanos,J., Warnke,A., Walitza,S., Freitag,C.,
            Meyer,J., Palmason,H., Rothenberger,A., Hawi,Z., Sergeant,J.,
            Roeyers,H., Mick,E. and Biederman,J.
  CONSRTM   IMAGE II Consortium Group
  TITLE     Case-control genome-wide association study of
            attention-deficit/hyperactivity disorder
  JOURNAL   J Am Acad Child Adolesc Psychiatry 49 (9), 906-920 (2010)
   PUBMED   20732627
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC042951.1, BC101535.1, BM689725.1 and AL390203.29.
            
            On Jun 8, 2007 this sequence version replaced NP_777597.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042951.1, SRR14038197.1477997.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368642.4/ ENSP00000357631.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.3"
     Protein         1..586
                     /product="transcription elongation regulator 1-like
                     protein"
                     /note="5730476P14Rik"
                     /calculated_mol_wt=65529
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWI1.2)"
     Region          281..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWI1.2)"
     Region          344..>584
                     /region_name="PRP40"
                     /note="Splicing factor [RNA processing and modification];
                     COG5104"
                     /db_xref="CDD:227435"
     Region          378..448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWI1.2)"
     Region          452..500
                     /region_name="FF"
                     /note="FF domain; pfam01846"
                     /db_xref="CDD:426471"
     Region          519..567
                     /region_name="FF"
                     /note="FF domain; pfam01846"
                     /db_xref="CDD:426471"
     CDS             1..586
                     /gene="TCERG1L"
                     /coded_by="NM_174937.4:87..1847"
                     /db_xref="CCDS:CCDS7662.2"
                     /db_xref="GeneID:256536"
                     /db_xref="HGNC:HGNC:23533"
                     /db_xref="MIM:620498"
ORIGIN      
        1 mqagarfqrr rrqlqqqqpr rrqpllwpmd aeppppppwv wmvpgsagll rlsagvvvpp
       61 vllasapppa apllpglpgw papsepvlpl lplpsapdsa aaaaahpfpa lhgqwlfggh
      121 spslglppss tvelvpvfph lcpsalatpi gkswidkrip nckiffnnsf aldstwihpe
      181 esrffhghek prllanqvav slsrpapasr plptvvlapq pipggchnsl kvtsspaiai
      241 ataaaaamvs vdpenlrgps pssvqprhfl tlapikiplr tspvsdtrte rgrvarppal
      301 mlraqksrdg dkedkepppm lgggedstar gnrpvastpv pgspwcvvwt gddrvfffnp
      361 tmhlsvwekp mdlkdrgdln riiedpphkr kleapatdns dgsssednre dqdvktkrnr
      421 tegcgspkpe eakredkgtr tpppqillpl eervthfrdm llergvsafs twekelhkiv
      481 fdprylllns eerkqifeqf vktrikeeyk ekksklllak eefkkllees kvsprttfke
      541 faekygrdqr frlvqkrkdq ehffnqfili lkkrdkenrl rlrkmr
//
LOCUS       NP_000033                345 aa            linear   PRI 27-APR-2025
DEFINITION  beta-2-glycoprotein 1 precursor [Homo sapiens].
ACCESSION   NP_000033
VERSION     NP_000033.2
DBSOURCE    REFSEQ: accession NM_000042.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   He,X., Zhang,J., Huang,M., Wang,J., Yang,S., Yu,X., Xu,Y. and
            Yang,W.
  TITLE     Serum apolipoprotein H determines ferroptosis resistance by
            modulating cellular lipid composition
  JOURNAL   Cell Death Dis 15 (10), 718 (2024)
   PUBMED   39353906
  REMARK    GeneRIF: Serum apolipoprotein H determines ferroptosis resistance
            by modulating cellular lipid composition.
            Erratum:[Cell Death Dis. 2024 Dec 3;15(12):875. doi:
            10.1038/s41419-024-07181-9. PMID: 39627207]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Yu,Z., Xiao,C., Liu,R., Pi,D., Jin,B., Zou,Z. and Xu,F.
  TITLE     The protective effect of apolipoprotein H in paediatric sepsis
  JOURNAL   Crit Care 28 (1), 36 (2024)
   PUBMED   38291524
  REMARK    GeneRIF: The protective effect of apolipoprotein H in paediatric
            sepsis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Liu,Y., Zhao,Y., Liu,Q., Li,B., Daniel,P.V., Chen,B. and Wu,Z.
  TITLE     Effects of apolipoprotein H downregulation on lipid metabolism,
            fatty liver disease, and gut microbiota dysbiosis
  JOURNAL   J Lipid Res 65 (1), 100483 (2024)
   PUBMED   38101620
  REMARK    GeneRIF: Effects of apolipoprotein H downregulation on lipid
            metabolism, fatty liver disease, and gut microbiota dysbiosis.
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Deng,X., Sang,Q., Zhang,R., Mu,J. and Bao,S.
  TITLE     The association of APOH and NCF1 polymorphisms on susceptibility to
            recurrent pregnancy loss in women with antiphospholipid syndrome
  JOURNAL   J Assist Reprod Genet 40 (7), 1703-1712 (2023)
   PUBMED   37243946
  REMARK    GeneRIF: The association of APOH and NCF1 polymorphisms on
            susceptibility to recurrent pregnancy loss in women with
            antiphospholipid syndrome.
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Kumar,S., Chinnaraj,M., Planer,W., Zuo,X., Macor,P., Tedesco,F. and
            Pozzi,N.
  TITLE     An allosteric redox switch in domain V of beta2-glycoprotein I
            controls membrane binding and anti-domain I autoantibody
            recognition
  JOURNAL   J Biol Chem 297 (2), 100890 (2021)
   PUBMED   34197876
  REMARK    GeneRIF: An allosteric redox switch in domain V of
            beta2-glycoprotein I controls membrane binding and anti-domain I
            autoantibody recognition.
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Steinkasserer,A., Barlow,P.N., Willis,A.C., Kertesz,Z.,
            Campbell,I.D., Sim,R.B. and Norman,D.G.
  TITLE     Activity, disulphide mapping and structural modelling of the fifth
            domain of human beta 2-glycoprotein I
  JOURNAL   FEBS Lett 313 (2), 193-197 (1992)
   PUBMED   1426288
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Matsuura,E., Igarashi,Y., Fujimoto,M., Ichikawa,K., Suzuki,T.,
            Sumida,T., Yasuda,T. and Koike,T.
  TITLE     Heterogeneity of anticardiolipin antibodies defined by the
            anticardiolipin cofactor
  JOURNAL   J Immunol 148 (12), 3885-3891 (1992)
   PUBMED   1602135
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Steinkasserer,A., Cockburn,D.J., Black,D.M., Boyd,Y., Solomon,E.
            and Sim,R.B.
  TITLE     Assignment of apolipoprotein H (APOH: beta-2-glycoprotein I) to
            human chromosome 17q23----qter; determination of the major
            expression site
  JOURNAL   Cytogenet Cell Genet 60 (1), 31-33 (1992)
   PUBMED   1582254
REFERENCE   9  (residues 1 to 345)
  AUTHORS   Day,J.R., O'Hara,P.J., Grant,F.J., Lofton-Day,C., Berkaw,M.N.,
            Werner,P. and Arnaud,P.
  TITLE     Molecular cloning and sequence analysis of the cDNA encoding human
            apolipoprotein H (beta 2-glycoprotein I)
  JOURNAL   Int J Clin Lab Res 21 (3), 256-263 (1992)
   PUBMED   1339416
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Polz,E. and Kostner,G.M.
  TITLE     The binding of beta 2-glycoprotein-I to human serum lipoproteins:
            distribution among density fractions
  JOURNAL   FEBS Lett 102 (1), 183-186 (1979)
   PUBMED   222615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG566874.1 and BC026283.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 24, 2007 this sequence version replaced NP_000033.1.
            
            Summary: Apolipoprotein H, also known as beta-2-glycoprotein I, is
            a component of circulating plasma lipoproteins. It has been
            implicated in a variety of physiologic pathways including
            lipoprotein metabolism, coagulation, hemostasis, and the production
            of antiphospholipid autoantibodies. APOH may be a required cofactor
            for anionic phospholipid binding by the antiphospholipid
            autoantibodies found in sera of many patients with lupus and
            primary antiphospholipid syndrome (APS). The anti-beta (2)
            glycoprotein I antibodies from APS patients, mediate inhibition of
            activated protein C which has anticoagulant properties. Because
            beta-2-GPI is the main autoantigen in patients with APS, the
            disruption of this pathway by autoantibodies may be an important
            mechanism for thrombosis in patients with APS.[provided by RefSeq,
            Dec 2019].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X57847.1, M62839.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2162895
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000205948.11/ ENSP00000205948.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..345
                     /product="beta-2-glycoprotein 1 precursor"
                     /note="beta-2-glycoprotein 1; beta(2)GPI; APC inhibitor;
                     anticardiolipin cofactor; activated protein C-binding
                     protein; B2GPI; apo-H; apolipoprotein H
                     (beta-2-glycoprotein I); epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=36255
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2062
     mat_peptide     20..345
                     /product="beta-2-glycoprotein 1"
                     /calculated_mol_wt=36255
     Site            33
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P17690; propagated from
                     UniProtKB/Swiss-Prot (P02749.3)"
     Region          41..260
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Site            149
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine; propagated from
                     UniProtKB/Swiss-Prot (P02749.3)"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
                     ECO:0000269|PubMed:6587378; propagated from
                     UniProtKB/Swiss-Prot (P02749.3)"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:6587378; propagated from
                     UniProtKB/Swiss-Prot (P02749.3)"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:6587378; propagated from
                     UniProtKB/Swiss-Prot (P02749.3)"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15084671,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6587378;
                     propagated from UniProtKB/Swiss-Prot (P02749.3)"
     Region          261..345
                     /region_name="Sushi_2"
                     /note="Beta-2-glycoprotein-1 fifth domain; pfam09014"
                     /db_xref="CDD:430371"
     Region          263..345
                     /region_name="Sushi-like"
                     /note="propagated from UniProtKB/Swiss-Prot (P02749.3)"
     CDS             1..345
                     /gene="APOH"
                     /gene_synonym="B2G1; B2GP1; BG"
                     /coded_by="NM_000042.3:37..1074"
                     /db_xref="CCDS:CCDS11663.1"
                     /db_xref="GeneID:350"
                     /db_xref="HGNC:HGNC:616"
                     /db_xref="MIM:138700"
ORIGIN      
        1 mispvlilfs sflchvaiag rtcpkpddlp fstvvplktf yepgeeitys ckpgyvsrgg
       61 mrkficpltg lwpintlkct prvcpfagil engavryttf eypntisfsc ntgfylngad
      121 sakcteegkw spelpvcapi icpppsiptf atlrvykpsa gnnslyrdta vfeclpqham
      181 fgndtitctt hgnwtklpec revkcpfpsr pdngfvnypa kptlyykdka tfgchdgysl
      241 dgpeeiectk lgnwsampsc kasckvpvkk atvvyqgerv kiqekfkngm lhgdkvsffc
      301 knkekkcsyt edaqcidgti evpkcfkehs slafwktdas dvkpc
//
LOCUS       NP_056263                203 aa            linear   PRI 27-APR-2025
DEFINITION  protein DPCD isoform 2 [Homo sapiens].
ACCESSION   NP_056263
VERSION     NP_056263.1
DBSOURCE    REFSEQ: accession NM_015448.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Dos Santos Morais,R., Santo,P.E., Ley,M., Schelcher,C., Abel,Y.,
            Plassart,L., Desligniere,E., Chagot,M.E., Quinternet,M.,
            Paiva,A.C.F., Hessmann,S., Morellet,N., M F Sousa,P.,
            Vandermoere,F., Bertrand,E., Charpentier,B., Bandeiras,T.M.,
            Plisson-Chastang,C., Verheggen,C., Cianferani,S. and Manival,X.
  TITLE     Deciphering cellular and molecular determinants of human DPCD
            protein in complex with RUVBL1/RUVBL2 AAA-ATPases
  JOURNAL   J Mol Biol 434 (19), 167760 (2022)
   PUBMED   35901867
  REMARK    GeneRIF: Deciphering cellular and molecular determinants of human
            DPCD protein in complex with RUVBL1/RUVBL2 AAA-ATPases.
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 203)
  AUTHORS   Zariwala,M., O'Neal,W.K., Noone,P.G., Leigh,M.W., Knowles,M.R. and
            Ostrowski,L.E.
  TITLE     Investigation of the possible role of a novel gene, DPCD, in
            primary ciliary dyskinesia
  JOURNAL   Am J Respir Cell Mol Biol 30 (4), 428-434 (2004)
   PUBMED   14630615
  REMARK    GeneRIF: a novel candidate gene for primary ciliary dyskinesia
            GeneRIF: The mouse homolog of this gene (named Dpcd, for Deleted in
            a mouse model of Primary Ciliary Dyskinesia) appears to be
            responsible for an inner arm defect in cilia.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY030728.1, BC001082.2 and
            BX361465.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene in mouse encodes a protein that may be involved
            in the generation and maintenance of ciliated cells. In mouse,
            expression of this gene increases during ciliated cell
            differentiation, and disruption of this gene has been linked to
            primary ciliary dyskinesia. [provided by RefSeq, Jul 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.501815.1,
                                           SRR5189667.321523.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370151.9/ ENSP00000359170.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..203
                     /product="protein DPCD isoform 2"
                     /note="protein DPCD; deleted in a mouse model of primary
                     ciliary dyskinesia; RP11-529I10.4"
                     /calculated_mol_wt=23109
     Region          6..194
                     /region_name="DPCD"
                     /note="DPCD protein family; pfam14913"
                     /db_xref="CDD:464369"
     CDS             1..203
                     /gene="DPCD"
                     /coded_by="NM_015448.3:17..628"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7514.1"
                     /db_xref="GeneID:25911"
                     /db_xref="HGNC:HGNC:24542"
                     /db_xref="MIM:616467"
ORIGIN      
        1 mavtgwlesl rtaqktallq dgrrkvhylf pdgkemaeey dektsellvr kwrvksalga
       61 mgqwqlevgd paplgagnlg pelikesnan pifmrkdtkm sfqwrirnlp ypkdvysvsv
      121 dqkerciivr ttnkkyykkf sipdldrhql plddallsfa hanctliisy qkpkevvvae
      181 selqkelkkv ktahsndgdc ktq
//
LOCUS       NP_001356532             508 aa            linear   PRI 27-APR-2025
DEFINITION  suppressor of tumorigenicity 7 protein isoform 7 [Homo sapiens].
ACCESSION   NP_001356532
VERSION     NP_001356532.1
DBSOURCE    REFSEQ: accession NM_001369603.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Liu,H., Lu,W., He,H., Wu,J., Zhang,C., Gong,H. and Yang,C.
  TITLE     Inflammation-dependent overexpression of c-Myc enhances CRL4DCAF4
            E3 ligase activity and promotes ubiquitination of ST7 in
            colitis-associated cancer
  JOURNAL   J Pathol 248 (4), 464-475 (2019)
   PUBMED   30945288
  REMARK    GeneRIF: Inflammation-dependent overexpression of c-Myc enhances
            CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7
            in colitis-associated cancer.
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Yan,F., Alinari,L., Lustberg,M.E., Martin,L.K.,
            Cordero-Nieves,H.M., Banasavadi-Siddegowda,Y., Virk,S.,
            Barnholtz-Sloan,J., Bell,E.H., Wojton,J., Jacob,N.K.,
            Chakravarti,A., Nowicki,M.O., Wu,X., Lapalombella,R., Datta,J.,
            Yu,B., Gordon,K., Haseley,A., Patton,J.T., Smith,P.L., Ryu,J.,
            Zhang,X., Mo,X., Marcucci,G., Nuovo,G., Kwon,C.H., Byrd,J.C.,
            Chiocca,E.A., Li,C., Sif,S., Jacob,S., Lawler,S., Kaur,B. and
            Baiocchi,R.A.
  TITLE     Genetic validation of the protein arginine methyltransferase PRMT5
            as a candidate therapeutic target in glioblastoma
  JOURNAL   Cancer Res 74 (6), 1752-1765 (2014)
   PUBMED   24453002
  REMARK    GeneRIF: The tumor suppressor ST7 is a key gene silenced by PRMT5.
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Hu,L., Wu,C., Zhao,X., Heist,R., Su,L., Zhao,Y., Han,B., Cao,S.,
            Chu,M., Dai,J., Dong,J., Shu,Y., Xu,L., Chen,Y., Wang,Y., Lu,F.,
            Jiang,Y., Yu,D., Chen,H., Tan,W., Ma,H., Chen,J., Jin,G., Wu,T.,
            Lu,D., Christiani,D.C., Lin,D., Hu,Z. and Shen,H.
  TITLE     Genome-wide association study of prognosis in advanced non-small
            cell lung cancer patients receiving platinum-based chemotherapy
  JOURNAL   Clin Cancer Res 18 (19), 5507-5514 (2012)
   PUBMED   22872573
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Zenklusen,J.C., Rodriguez,L.V., LaCava,M., Wang,Z., Goldstein,L.S.
            and Conti,C.J.
  TITLE     Novel susceptibility locus for mouse hepatomas: evidence for a
            conserved tumor suppressor gene
  JOURNAL   Genome Res 6 (11), 1070-1076 (1996)
   PUBMED   8938430
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Zenklusen,J.C., Weitzel,J.N., Ball,H.G. and Conti,C.J.
  TITLE     Allelic loss at 7q31.1 in human primary ovarian carcinomas suggests
            the existence of a tumor suppressor gene
  JOURNAL   Oncogene 11 (2), 359-363 (1995)
   PUBMED   7624150
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Zenklusen,J.C., Thompson,J.C., Troncoso,P., Kagan,J. and Conti,C.J.
  TITLE     Loss of heterozygosity in human primary prostate carcinomas: a
            possible tumor suppressor gene at 7q31.1
  JOURNAL   Cancer Res 54 (24), 6370-6373 (1994)
   PUBMED   7987830
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Zenklusen,J.C., Bieche,I., Lidereau,R. and Conti,C.J.
  TITLE     (C-A)n microsatellite repeat D7S522 is the most commonly deleted
            region in human primary breast cancer
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12155-12158 (1994)
   PUBMED   7991599
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Ogata,T., Ayusawa,D., Namba,M., Takahashi,E., Oshimura,M. and
            Oishi,M.
  TITLE     Chromosome 7 suppresses indefinite division of nontumorigenic
            immortalized human fibroblast cell lines KMST-6 and SUSM-1
  JOURNAL   Mol Cell Biol 13 (10), 6036-6043 (1993)
   PUBMED   8105370
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106873.3, AC002542.1 and
            AC003987.1.
            
            Summary: The gene for this product maps to a region on chromosome 7
            identified as an autism-susceptibility locus. Mutation screening of
            the entire coding region in autistic individuals failed to identify
            phenotype-specific variants, suggesting that coding mutations for
            this gene are unlikely to be involved in the etiology of autism.
            The function of this gene product has not been determined.
            Transcript variants encoding different isoforms of this protein
            have been described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.159532.1,
                                           SRR1163658.406551.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.2"
     Protein         1..508
                     /product="suppressor of tumorigenicity 7 protein isoform
                     7"
                     /note="family with sequence similarity 4, subfamily A,
                     member 1; suppression of tumorigenicity 7 (breast);
                     suppressor of tumorigenicity 7 protein"
                     /calculated_mol_wt=57937
     Region          5..507
                     /region_name="ST7"
                     /note="ST7 protein; pfam04184"
                     /db_xref="CDD:461214"
     CDS             1..508
                     /gene="ST7"
                     /gene_synonym="ETS7q; FAM4A; FAM4A1; HELG; RAY1; SEN4;
                     TSG7"
                     /coded_by="NM_001369603.1:91..1617"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS94184.1"
                     /db_xref="GeneID:7982"
                     /db_xref="HGNC:HGNC:11351"
                     /db_xref="MIM:600833"
ORIGIN      
        1 mdytvsmfln tltpkfyval tgtsslisgl ilifewwyfr kygtsfieqv svshlrpllg
       61 gvdnnssnns nssngdsdsn rqsvseckvw rnplnlfrga eynrytwvtg repltyydmn
      121 lsaqdhqtff tcdsdhlrpa daimqkawre rnpqarisaa healeineca tayillaeee
      181 attiaeaekl fkqalkagdg cyrrsqqlqh hgsqyeaqhr rdtnvlvyik rrlamcarrl
      241 grtreavkmm rdlmkefpll smfnihenll eallelqaya dvqavlakyd dislpksati
      301 cytaallkar avsdkfspea asrrglstae mnaveaihra vefnphvpky llemkslilp
      361 pehilkrgds eaiayaffhl ahwkrvegal nllhctwegt frmipyplek ghlfypypic
      421 tetadrellp sfhevsvypk kelpffilft aglcsftaml allthqfpel mgvfakafls
      481 tlfaplnfvm ekvesilpss lwhqltri
//
LOCUS       NP_055415                535 aa            linear   PRI 27-APR-2025
DEFINITION  EH domain-containing protein 3 [Homo sapiens].
ACCESSION   NP_055415
VERSION     NP_055415.1
DBSOURCE    REFSEQ: accession NM_014600.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Amessou,M., Ebrahim,A.S., Dilly,A., Joseph,M., Tabolina,M.,
            Chukkapalli,S., Meroueh,L., Syed,J.T., Liddane,A., Lang,S.L.,
            Al-Katib,A. and Kandouz,M.
  TITLE     Spatio-temporal regulation of EGFR signaling by the Eps15 homology
            domain-containing protein 3 (EHD3)
  JOURNAL   Oncotarget 7 (48), 79203-79216 (2016)
   PUBMED   27811356
  REMARK    GeneRIF: Data provide evidence that EHD3 might undergo its tumor
            suppressor functions at least in part through promoting the sorting
            of activated EGFR to the lysosomal degradative compartment and
            spatio-temporal regulation of EGFR signaling via ERK and AKT.
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Naslavsky,N., Rahajeng,J., Sharma,M., Jovic,M. and Caplan,S.
  TITLE     Interactions between EHD proteins and Rab11-FIP2: a role for EHD3
            in early endosomal transport
  JOURNAL   Mol Biol Cell 17 (1), 163-177 (2006)
   PUBMED   16251358
  REMARK    GeneRIF: presented herein promote a coordinated role for EHD
            proteins and Rab11-FIP2 in mediating endocytic recycling and
            provide evidence for the function of EHD3 in early endosome to
            endocytic recycling compartment transport
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Naslavsky,N., Boehm,M., Backlund,P.S. Jr. and Caplan,S.
  TITLE     Rabenosyn-5 and EHD1 interact and sequentially regulate protein
            recycling to the plasma membrane
  JOURNAL   Mol Biol Cell 15 (5), 2410-2422 (2004)
   PUBMED   15020713
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
REFERENCE   8  (residues 1 to 535)
  AUTHORS   Galperin,E., Benjamin,S., Rapaport,D., Rotem-Yehudar,R.,
            Tolchinsky,S. and Horowitz,M.
  TITLE     EHD3: a protein that resides in recycling tubular and vesicular
            membrane structures and interacts with EHD1
  JOURNAL   Traffic 3 (8), 575-589 (2002)
   PUBMED   12121420
  REMARK    GeneRIF: EHD3: a protein that resides in recycling tubular and
            vesicular membrane structures and interacts with EHD1.
REFERENCE   9  (residues 1 to 535)
  AUTHORS   Rotem-Yehudar,R., Galperin,E. and Horowitz,M.
  TITLE     Association of insulin-like growth factor 1 receptor with EHD1 and
            SNAP29
  JOURNAL   J Biol Chem 276 (35), 33054-33060 (2001)
   PUBMED   11423532
REFERENCE   10 (residues 1 to 535)
  AUTHORS   Pohl,U., Smith,J.S., Tachibana,I., Ueki,K., Lee,H.K., Ramaswamy,S.,
            Wu,Q., Mohrenweiser,H.W., Jenkins,R.B. and Louis,D.N.
  TITLE     EHD2, EHD3, and EHD4 encode novel members of a highly conserved
            family of EH domain-containing proteins
  JOURNAL   Genomics 63 (2), 255-262 (2000)
   PUBMED   10673336
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK316006.1, DA196836.1, BC033100.1, AF214736.1 and AL121657.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.27274.1,
                                           SRR1803615.35683.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322054.10/ ENSP00000327116.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.1"
     Protein         1..535
                     /product="EH domain-containing protein 3"
                     /note="PAST homolog 3"
                     /calculated_mol_wt=60756
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:12665801; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN3.2)"
     Region          <37..56
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Region          60..300
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Region          65..72
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN3.2)"
     Site            65..72
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(70..73,153,220,222,256..258)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Region          91..92
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN3.2)"
     Site            94
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            98..100
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Region          153..156
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN3.2)"
     Site            153..156
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(155..156,183..184)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Region          219..222
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN3.2)"
     Site            219..222
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Region          243
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN3.2)"
     Site            256..258
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     Region          288..394
                     /region_name="DUF5600"
                     /note="Domain of unknown function (DUF5600); pfam18150"
                     /db_xref="CDD:465667"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R491; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN3.2)"
     Region          438..531
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXY6; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN3.2)"
     CDS             1..535
                     /gene="EHD3"
                     /gene_synonym="PAST3"
                     /coded_by="NM_014600.3:471..2078"
                     /db_xref="CCDS:CCDS1774.1"
                     /db_xref="GeneID:30845"
                     /db_xref="HGNC:HGNC:3244"
                     /db_xref="MIM:605891"
ORIGIN      
        1 mfswlgtddr rrkdpevfqt vseglkklyk skllpleehy rfhefhspal edadfdnkpm
       61 vllvgqystg kttfirylle qdfpgmrigp epttdsfiav mqgdmegiip gnalvvdpkk
      121 pfrklnafgn aflnrfvcaq lpnpvlesis vidtpgilsg ekqrisrgyd faavlewfae
      181 rvdriillfd ahkldisdef sevikalknh edkmrvvlnk adqietqqlm rvygalmwsl
      241 gkivntpevi rvyigsfwsh pllipdnrkl feaeeqdlfr diqslprnaa lrklndlikr
      301 arlakvhayi isslkkemps vfgkdnkkke lvnnlaeiyg rierehqisp gdfpnlkrmq
      361 dqlqaqdfsk fqplksklle vvddmlahdi aqlmvlvrqe esqrpiqmvk ggafegtlhg
      421 pfghgygega gegiddaewv vardkpmyde ifytlspvdg kitganakke mvrsklpnsv
      481 lgkiwkladi dkdgmlddde falanhlikv kleghelpne lpahllppsk rkvae
//
LOCUS       NP_006704                127 aa            linear   PRI 27-APR-2025
DEFINITION  activated RNA polymerase II transcriptional coactivator p15 [Homo
            sapiens].
ACCESSION   NP_006704
VERSION     NP_006704.3
DBSOURCE    REFSEQ: accession NM_006713.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Zhao,T., He,X., Liang,X., Kellum,A.H. Jr., Tang,F., Yin,J., Guo,S.,
            Wang,Y., Gao,Z. and Wang,Y.
  TITLE     HMGB3 and SUB1 Bind to and Facilitate the Repair of N2-Alkylguanine
            Lesions in DNA
  JOURNAL   J Am Chem Soc 146 (32), 22553-22562 (2024)
   PUBMED   39101269
  REMARK    GeneRIF: HMGB3 and SUB1 Bind to and Facilitate the Repair of
            N[2]-Alkylguanine Lesions in DNA.
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Yan,B., Luo,P., Qiu,H., Wang,J., Xiong,Q., Hu,W., Wang,F., Liu,G.,
            Zhi,Y., Fang,Q., Shi,C. and Li,W.
  TITLE     PC4 promotes bladder cancer progression and stemness by directly
            interacting with Sp1 to transcriptionally activate the
            Wnt5a/beta-catenin pathway
  JOURNAL   Pathol Res Pract 259, 155369 (2024)
   PUBMED   38820928
  REMARK    GeneRIF: PC4 promotes bladder cancer progression and stemness by
            directly interacting with Sp1 to transcriptionally activate the
            Wnt5a/beta-catenin pathway.
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Wang,H., Chen,W., Wang,Y., Gao,Y., Zhang,Z., Mi,S., Wang,L. and
            Xue,M.
  TITLE     SUB1 promotes colorectal cancer metastasis by activating NF-kappaB
            signaling via UBR5-mediated ubiquitination of UBXN1
  JOURNAL   Sci China Life Sci 67 (6), 1199-1211 (2024)
   PUBMED   38240906
  REMARK    GeneRIF: SUB1 promotes colorectal cancer metastasis by activating
            NF-kappaB signaling via UBR5-mediated ubiquitination of UBXN1.
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Pan,Q., Luo,P., Hu,K., Qiu,Y., Liu,G., Dai,S., Cui,B., Yin,D. and
            Shi,C.
  TITLE     Periodic changes of cyclin D1 mRNA stability are regulated by PC4
            modifications in the cell cycle
  JOURNAL   J Cell Biol 223 (3) (2024)
   PUBMED   38349334
  REMARK    GeneRIF: Periodic changes of cyclin D1 mRNA stability are regulated
            by PC4 modifications in the cell cycle.
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Mustafi,P., Hu,M., Kumari,S., Das,C., Li,G. and Kundu,T.K.
  TITLE     Phosphorylation-dependent association of human chromatin protein
            PC4 to linker histone H1 regulates genome organization and
            transcription
  JOURNAL   Nucleic Acids Res 50 (11), 6116-6136 (2022)
   PUBMED   35670677
  REMARK    GeneRIF: Phosphorylation-dependent association of human chromatin
            protein PC4 to linker histone H1 regulates genome organization and
            transcription.
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Brandsen,J., Werten,S., van der Vliet,P.C., Meisterernst,M.,
            Kroon,J. and Gros,P.
  TITLE     C-terminal domain of transcription cofactor PC4 reveals dimeric
            ssDNA binding site
  JOURNAL   Nat Struct Biol 4 (11), 900-903 (1997)
   PUBMED   9360603
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Kaiser,K., Stelzer,G. and Meisterernst,M.
  TITLE     The coactivator p15 (PC4) initiates transcriptional activation
            during TFIIA-TFIID-promoter complex formation
  JOURNAL   EMBO J 14 (14), 3520-3527 (1995)
   PUBMED   7628453
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Ge,H., Zhao,Y., Chait,B.T. and Roeder,R.G.
  TITLE     Phosphorylation negatively regulates the function of coactivator
            PC4
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12691-12695 (1994)
   PUBMED   7809103
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Kretzschmar,M., Kaiser,K., Lottspeich,F. and Meisterernst,M.
  TITLE     A novel mediator of class II gene transcription with homology to
            viral immediate-early transcriptional regulators
  JOURNAL   Cell 78 (3), 525-534 (1994)
   PUBMED   8062392
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Ge,H. and Roeder,R.G.
  TITLE     Purification, cloning, and characterization of a human coactivator,
            PC4, that mediates transcriptional activation of class II genes
  JOURNAL   Cell 78 (3), 513-523 (1994)
   PUBMED   8062391
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX472106.1, BC010537.1, BC071655.1 and AC074134.3.
            
            On Dec 12, 2008 this sequence version replaced NP_006704.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC071655.1, SRR1660807.205718.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265073.9/ ENSP00000265073.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.3"
     Protein         1..127
                     /product="activated RNA polymerase II transcriptional
                     coactivator p15"
                     /note="activated RNA polymerase II transcription cofactor
                     4; positive cofactor 4; SUB1 homolog, transcriptional
                     regulator"
                     /calculated_mol_wt=14264
     Region          1..64
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53999.3)"
     Region          2..50
                     /region_name="Regulatory"
                     /note="propagated from UniProtKB/Swiss-Prot (P53999.3)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16689930; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16689930,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16689930,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16689930,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16689930,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            50..51
                     /site_type="cleavage"
                     /note="Cleavage; propagated from UniProtKB/Swiss-Prot
                     (P53999.3)"
     Site            53
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11031; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Region          64..115
                     /region_name="PC4"
                     /note="Transcriptional Coactivator p15 (PC4); pfam02229"
                     /db_xref="CDD:460501"
     Site            68
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P53999.3)"
     Region          77..101
                     /region_name="Interaction with ssDNA"
                     /note="propagated from UniProtKB/Swiss-Prot (P53999.3)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P53999.3)"
     CDS             1..127
                     /gene="SUB1"
                     /gene_synonym="p14; P15; PC4"
                     /coded_by="NM_006713.4:71..454"
                     /db_xref="CCDS:CCDS3897.1"
                     /db_xref="GeneID:10923"
                     /db_xref="HGNC:HGNC:19985"
                     /db_xref="MIM:600503"
ORIGIN      
        1 mpkskelvss sssgsdsdse vdkklkrkkq vapekpvkkq ktgetsrals sskqssssrd
       61 dnmfqigkmr yvsvrdfkgk vlidireywm dpegemkpgr kgislnpeqw sqlkeqisdi
      121 ddavrkl
//
LOCUS       NP_000856                365 aa            linear   PRI 27-APR-2025
DEFINITION  5-hydroxytryptamine receptor 1E [Homo sapiens].
ACCESSION   NP_000856
VERSION     NP_000856.1
DBSOURCE    REFSEQ: accession NM_000865.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Tan,Y., Xu,P., Huang,S., Yang,G., Zhou,F., He,X., Ma,H., Xu,H.E.
            and Jiang,Y.
  TITLE     Structural insights into the ligand binding and Gi coupling of
            serotonin receptor 5-HT5A
  JOURNAL   Cell Discov 8 (1), 50 (2022)
   PUBMED   35610220
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Sharma,V.K., Yang,X., Kim,S.K., Mafi,A., Saiz-Sanchez,D.,
            Villanueva-Anguita,P., Xiao,L., Inoue,A., Goddard,W.A. 3rd and
            Loh,Y.P.
  TITLE     Novel interaction between neurotrophic
            factor-alpha1/carboxypeptidase E and serotonin receptor, 5-HTR1E,
            protects human neurons against oxidative/neuroexcitotoxic stress
            via beta-arrestin/ERK signaling
  JOURNAL   Cell Mol Life Sci 79 (1), 24 (2021)
   PUBMED   34966948
  REMARK    GeneRIF: Novel interaction between neurotrophic
            factor-alpha1/carboxypeptidase E and serotonin receptor, 5-HTR1E,
            protects human neurons against oxidative/neuroexcitotoxic stress
            via beta-arrestin/ERK signaling.
            Erratum:[Cell Mol Life Sci. 2023 Feb 20;80(3):65. doi:
            10.1007/s00018-023-04711-0. PMID: 36808009]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Qin,X., Li,J., Wang,S., Lv,J., Luan,F., Liu,Y., Chen,Y., Chen,X.,
            Zhao,Y., Zhu,J., Piao,Y., Zhang,W., Shi,Y., Xiang,R., Qu,P. and
            Wang,L.
  TITLE     Serotonin/HTR1E signaling blocks chronic stress-promoted
            progression of ovarian cancer
  JOURNAL   Theranostics 11 (14), 6950-6965 (2021)
   PUBMED   34093864
  REMARK    GeneRIF: Serotonin/HTR1E signaling blocks chronic stress-promoted
            progression of ovarian cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Xu,P., Huang,S., Zhang,H., Mao,C., Zhou,X.E., Cheng,X., Simon,I.A.,
            Shen,D.D., Yen,H.Y., Robinson,C.V., Harpsoe,K., Svensson,B.,
            Guo,J., Jiang,H., Gloriam,D.E., Melcher,K., Jiang,Y., Zhang,Y. and
            Xu,H.E.
  TITLE     Structural insights into the lipid and ligand regulation of
            serotonin receptors
  JOURNAL   Nature 592 (7854), 469-473 (2021)
   PUBMED   33762731
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Levy,F.O., Holtgreve-Grez,H., Tasken,K., Solberg,R., Ried,T. and
            Gudermann,T.
  TITLE     Assignment of the gene encoding the 5-HT1E serotonin receptor (S31)
            (locus HTR1E) to human chromosome 6q14-q15
  JOURNAL   Genomics 22 (3), 637-640 (1994)
   PUBMED   8001977
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Zgombick,J.M., Schechter,L.E., Macchi,M., Hartig,P.R.,
            Branchek,T.A. and Weinshank,R.L.
  TITLE     Human gene S31 encodes the pharmacologically defined serotonin
            5-hydroxytryptamine1E receptor
  JOURNAL   Mol Pharmacol 42 (2), 180-185 (1992)
   PUBMED   1513320
REFERENCE   8  (residues 1 to 365)
  AUTHORS   McAllister,G., Charlesworth,A., Snodin,C., Beer,M.S., Noble,A.J.,
            Middlemiss,D.N., Iversen,L.L. and Whiting,P.
  TITLE     Molecular cloning of a serotonin receptor from human brain (5HT1E):
            a fifth 5HT1-like subtype
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5517-5521 (1992)
   PUBMED   1608964
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Levy,F.O., Gudermann,T., Birnbaumer,M., Kaumann,A.J. and
            Birnbaumer,L.
  TITLE     Molecular cloning of a human gene (S31) encoding a novel serotonin
            receptor mediating inhibition of adenylyl cyclase
  JOURNAL   FEBS Lett 296 (2), 201-206 (1992)
   PUBMED   1733778
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Itoh,H., Toyama,R., Kozasa,T., Tsukamoto,T., Matsuoka,M. and
            Kaziro,Y.
  TITLE     Presence of three distinct molecular species of Gi protein alpha
            subunit. Structure of rat cDNAs and human genomic DNAs
  JOURNAL   J Biol Chem 263 (14), 6656-6664 (1988)
   PUBMED   2834384
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL521170.3, AL157777.5, BC069751.1 and M91467.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.49482.1,
                                           SRR1660805.202329.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305344.7/ ENSP00000307766.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..365
                     /product="5-hydroxytryptamine receptor 1E"
                     /note="S31; 5-HT-1E; serotonin receptor 1E;
                     5-hydroxytryptamine (serotonin) receptor 1E, G
                     protein-coupled"
                     /calculated_mol_wt=41551
     Site            2
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28566.1)"
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28566.1)"
     Site            22..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28566.1)"
     Region          23..355
                     /region_name="7tmA_5-HT1E"
                     /note="serotonin receptor subtype 1E, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15335"
                     /db_xref="CDD:320457"
     Region          24..50
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320457"
     Region          57..83
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320457"
     Site            60..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28566.1)"
     Site            93..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28566.1)"
     Region          95..125
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320457"
     Site            order(98..99,102..103,106..107,173,186,190,304,307..308,
                     314,323,326..327,330,334)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320457"
     Region          119..121
                     /region_name="DRY motif, important for ligand-induced
                     conformation changes.
                     /evidence=ECO:0000250|UniProtKB:P41595"
                     /note="propagated from UniProtKB/Swiss-Prot (P28566.1)"
     Region          137..159
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320457"
     Site            139..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28566.1)"
     Region          179..208
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320457"
     Site            180..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28566.1)"
     Region          284..314
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320457"
     Site            292..316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28566.1)"
     Region          323..348
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320457"
     Site            323..345
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28566.1)"
     Region          340..344
                     /region_name="NPxxY motif, important for ligand-induced
                     conformation changes and signaling.
                     /evidence=ECO:0000250|UniProtKB:P41595"
                     /note="propagated from UniProtKB/Swiss-Prot (P28566.1)"
     CDS             1..365
                     /gene="HTR1E"
                     /gene_synonym="5-HT1E"
                     /coded_by="NM_000865.3:482..1579"
                     /db_xref="CCDS:CCDS5006.1"
                     /db_xref="GeneID:3354"
                     /db_xref="HGNC:HGNC:5291"
                     /db_xref="MIM:182132"
ORIGIN      
        1 mnitncttea smairpktit ekmlicmtlv vittlttlln lavimaigtt kklhqpanyl
       61 icslavtdll vavlvmplsi iyivmdrwkl gyflcevwls vdmtcctcsi lhlcvialdr
      121 ywaitnaiey arkrtakraa lmiltvwtis ifismpplfw rshrrlsppp sqctiqhdhv
      181 iytiystlga fyipltlili lyyriyhaak slyqkrgssr hlsnrstdsq nsfasckltq
      241 tfcvsdfsts dpttefekfh asirippfdn dldhpgerqq isstrerkaa rilglilgaf
      301 ilswlpffik elivglsiyt vssevadflt wlgyvnslin pllytsfned fklafkklir
      361 creht
//
LOCUS       NP_940959                357 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding protein 43 [Homo sapiens].
ACCESSION   NP_940959 XP_351504
VERSION     NP_940959.1
DBSOURCE    REFSEQ: accession NM_198557.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Feng,H., Liu,J., Qiu,Y., Liu,Y., Saiyin,H., Liang,X., Zheng,F.,
            Wang,Y., Jiang,D., Wang,Y., Yu,L., Su,W., Shen,S. and Wu,J.
  TITLE     RNA-binding motif protein 43 (RBM43) suppresses hepatocellular
            carcinoma progression through modulation of cyclin B1 expression
  JOURNAL   Oncogene 39 (33), 5495-5506 (2020)
   PUBMED   32632220
  REMARK    GeneRIF: RNA-binding motif protein 43 (RBM43) suppresses
            hepatocellular carcinoma progression through modulation of cyclin
            B1 expression.
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Albertsen,H.M., Chettier,R., Farrington,P. and Ward,K.
  TITLE     Genome-wide association study link novel loci to endometriosis
  JOURNAL   PLoS One 8 (3), e58257 (2013)
   PUBMED   23472165
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Palmer,N.D., McDonough,C.W., Hicks,P.J., Roh,B.H., Wing,M.R.,
            An,S.S., Hester,J.M., Cooke,J.N., Bostrom,M.A., Rudock,M.E.,
            Talbert,M.E., Lewis,J.P., Ferrara,A., Lu,L., Ziegler,J.T.,
            Sale,M.M., Divers,J., Shriner,D., Adeyemo,A., Rotimi,C.N., Ng,M.C.,
            Langefeld,C.D., Freedman,B.I., Bowden,D.W., Voight,B.F.,
            Scott,L.J., Steinthorsdottir,V., Morris,A.P., Dina,C., Welch,R.P.,
            Zeggini,E., Huth,C., Aulchenko,Y.S., Thorleifsson,G.,
            McCulloch,L.J., Ferreira,T., Grallert,H., Amin,N., Wu,G.,
            Willer,C.J., Raychaudhuri,S., McCarroll,S.A., Langenberg,C.,
            Hofmann,O.M., Dupuis,J., Qi,L., Segre,A.V., van Hoek,M.,
            Navarro,P., Ardlie,K., Balkau,B., Benediktsson,R., Bennett,A.J.,
            Blagieva,R., Boerwinkle,E., Bonnycastle,L.L., Bostrom,K.B.,
            Bravenboer,B., Bumpstead,S., Burtt,N.P., Charpentier,G.,
            Chines,P.S., Cornelis,M., Couper,D.J., Crawford,G., Doney,A.S.,
            Elliott,K.S., Elliott,A.L., Erdos,M.R., Fox,C.S., Franklin,C.S.,
            Ganser,M., Gieger,C., Grarup,N., Green,T., Griffin,S., Groves,C.J.,
            Guiducci,C., Hadjadj,S., Hassanali,N., Herder,C., Isomaa,B.,
            Jackson,A.U., Johnson,P.R., Jorgensen,T., Kao,W.H., Klopp,N.,
            Kong,A., Kraft,P., Kuusisto,J., Lauritzen,T., Li,M., Lieverse,A.,
            Lindgren,C.M., Lyssenko,V., Marre,M., Meitinger,T., Midthjell,K.,
            Morken,M.A., Narisu,N., Nilsson,P., Owen,K.R., Payne,F.,
            Perry,J.R., Petersen,A.K., Platou,C., Proenca,C., Prokopenko,I.,
            Rathmann,W., Rayner,N.W., Robertson,N.R., Rocheleau,G., Roden,M.,
            Sampson,M.J., Saxena,R., Shields,B.M., Shrader,P., Sigurdsson,G.,
            Sparso,T., Strassburger,K., Stringham,H.M., Sun,Q., Swift,A.J.,
            Thorand,B., Tichet,J., Tuomi,T., van Dam,R.M., van Haeften,T.W.,
            van Herpt,T., van Vliet-Ostaptchouk,J.V., Walters,G.B.,
            Weedon,M.N., Wijmenga,C., Witteman,J., Bergman,R.N., Cauchi,S.,
            Collins,F.S., Gloyn,A.L., Gyllensten,U., Hansen,T., Hide,W.A.,
            Hitman,G.A., Hofman,A., Hunter,D.J., Hveem,K., Laakso,M.,
            Mohlke,K.L., Morris,A.D., Palmer,C.N., Pramstaller,P.P., Rudan,I.,
            Sijbrands,E., Stein,L.D., Tuomilehto,J., Uitterlinden,A.,
            Walker,M., Wareham,N.J., Watanabe,R.M., Abecasis,G.R., Boehm,B.O.,
            Campbell,H., Daly,M.J., Hattersley,A.T., Hu,F.B., Meigs,J.B.,
            Pankow,J.S., Pedersen,O., Wichmann,H.E., Barroso,I., Florez,J.C.,
            Frayling,T.M., Groop,L., Sladek,R., Thorsteinsdottir,U.,
            Wilson,J.F., Illig,T., Froguel,P., van Duijn,C.M., Stefansson,K.,
            Altshuler,D., Boehnke,M., McCarthy,M.I., Soranzo,N., Wheeler,E.,
            Glazer,N.L., Bouatia-Naji,N., Magi,R., Randall,J., Johnson,T.,
            Elliott,P., Rybin,D., Henneman,P., Dehghan,A., Hottenga,J.J.,
            Song,K., Goel,A., Egan,J.M., Lajunen,T., Doney,A., Kanoni,S.,
            Cavalcanti-Proenca,C., Kumari,M., Timpson,N.J., Zabena,C.,
            Ingelsson,E., An,P., O'Connell,J., Luan,J., Elliott,A.,
            McCarroll,S.A., Roccasecca,R.M., Pattou,F., Sethupathy,P.,
            Ariyurek,Y., Barter,P., Beilby,J.P., Ben-Shlomo,Y., Bergmann,S.,
            Bochud,M., Bonnefond,A., Borch-Johnsen,K., Bottcher,Y., Brunner,E.,
            Bumpstead,S.J., Chen,Y.D., Chines,P., Clarke,R., Coin,L.J.,
            Cooper,M.N., Crisponi,L., Day,I.N., de Geus,E.J., Delplanque,J.,
            Fedson,A.C., Fischer-Rosinsky,A., Forouhi,N.G., Frants,R.,
            Franzosi,M.G., Galan,P., Goodarzi,M.O., Graessler,J., Grundy,S.,
            Gwilliam,R., Hallmans,G., Hammond,N., Han,X., Hartikainen,A.L.,
            Hayward,C., Heath,S.C., Hercberg,S., Hicks,A.A., Hillman,D.R.,
            Hingorani,A.D., Hui,J., Hung,J., Jula,A., Kaakinen,M., Kaprio,J.,
            Kesaniemi,Y.A., Kivimaki,M., Knight,B., Koskinen,S., Kovacs,P.,
            Kyvik,K.O., Lathrop,G.M., Lawlor,D.A., Le Bacquer,O., Lecoeur,C.,
            Li,Y., Mahley,R., Mangino,M., Manning,A.K., Martinez-Larrad,M.T.,
            McAteer,J.B., McPherson,R., Meisinger,C., Melzer,D., Meyre,D.,
            Mitchell,B.D., Mukherjee,S., Naitza,S., Neville,M.J., Oostra,B.A.,
            Orru,M., Pakyz,R., Paolisso,G., Pattaro,C., Pearson,D., Peden,J.F.,
            Pedersen,N.L., Perola,M., Pfeiffer,A.F., Pichler,I., Polasek,O.,
            Posthuma,D., Potter,S.C., Pouta,A., Province,M.A., Psaty,B.M.,
            Rayner,N.W., Rice,K., Ripatti,S., Rivadeneira,F., Rolandsson,O.,
            Sandbaek,A., Sandhu,M., Sanna,S., Sayer,A.A., Scheet,P.,
            Seedorf,U., Sharp,S.J., Shields,B., Sijbrands,E.J., Silveira,A.,
            Simpson,L., Singleton,A., Smith,N.L., Sovio,U., Swift,A.,
            Syddall,H., Syvanen,A.C., Tanaka,T., Tonjes,A., Uitterlinden,A.G.,
            van Dijk,K.W., Varma,D., Visvikis-Siest,S., Vitart,V.,
            Vogelzangs,N., Waeber,G., Wagner,P.J., Walley,A., Ward,K.L.,
            Watkins,H., Wild,S.H., Willemsen,G., Witteman,J.C., Yarnell,J.W.,
            Zelenika,D., Zethelius,B., Zhai,G., Zhao,J.H., Zillikens,M.C.,
            Borecki,I.B., Loos,R.J., Meneton,P., Magnusson,P.K., Nathan,D.M.,
            Williams,G.H., Silander,K., Salomaa,V., Smith,G.D., Bornstein,S.R.,
            Schwarz,P., Spranger,J., Karpe,F., Shuldiner,A.R., Cooper,C.,
            Dedoussis,G.V., Serrano-Rios,M., Lind,L., Palmer,L.J., Franks,P.W.,
            Ebrahim,S., Marmot,M., Kao,W.H., Pramstaller,P.P., Wright,A.F.,
            Stumvoll,M., Hamsten,A., Buchanan,T.A., Valle,T.T., Rotter,J.I.,
            Siscovick,D.S., Penninx,B.W., Boomsma,D.I., Deloukas,P.,
            Spector,T.D., Ferrucci,L., Cao,A., Scuteri,A., Schlessinger,D.,
            Uda,M., Ruokonen,A., Jarvelin,M.R., Waterworth,D.M.,
            Vollenweider,P., Peltonen,L., Mooser,V. and Sladek,R.
  CONSRTM   DIAGRAM Consortium; MAGIC Investigators
  TITLE     A genome-wide association search for type 2 diabetes genes in
            African Americans
  JOURNAL   PLoS One 7 (1), e29202 (2012)
   PUBMED   22238593
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX337439.2, DA658209.1, BC136411.1 and AC018731.5.
            
            On Dec 17, 2003 this sequence version replaced XP_351504.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127552.1, BC136410.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331426.6/ ENSP00000331211.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..357
                     /product="RNA-binding protein 43"
                     /calculated_mol_wt=40535
     Region          15..93
                     /region_name="RRM_RBM43"
                     /note="RNA recognition motif in vertebrate RNA-binding
                     protein 43 (RBM43); cd12546"
                     /db_xref="CDD:409962"
     CDS             1..357
                     /gene="RBM43"
                     /gene_synonym="C2orf38"
                     /coded_by="NM_198557.3:137..1210"
                     /db_xref="CCDS:CCDS2191.1"
                     /db_xref="GeneID:375287"
                     /db_xref="HGNC:HGNC:24790"
ORIGIN      
        1 masvlnvkes kapertvvva glpvdlfsdq llavlvkshf qdikneggdv edviyptrtk
       61 gvayvifkek kvaenvirqk khwlarktrh aeltvslrvs hfgdkifssv naildlsvfg
      121 kevtletlvk dlkkkipsls fsplkpngri svegsflavk rlresllara csllekdrnf
      181 tseerkwnrq npqrnlqrsn nslasvrtlv petarsgeml vldtdvflyl khkcgsyest
      241 lkkfhilsqe kvdgeittic lksiqvgsqp nnakhvkeli eewshalylk lrketfileg
      301 kenrekrmik raceqlssry levlinlyrt hidiigsssd tylfkkgvmk ligqkvs
//
LOCUS       NP_006342                452 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit TIM44 [Homo
            sapiens].
ACCESSION   NP_006342
VERSION     NP_006342.2
DBSOURCE    REFSEQ: accession NM_006351.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Zhang,L., Shi,X., Zhang,L., Mi,Y., Zuo,L. and Gao,S.
  TITLE     A first-in-class TIMM44 blocker inhibits bladder cancer cell growth
  JOURNAL   Cell Death Dis 15 (3), 204 (2024)
   PUBMED   38467612
  REMARK    GeneRIF: A first-in-class TIMM44 blocker inhibits bladder cancer
            cell growth.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Ma,Z.R., Li,H.P., Cai,S.Z., Du,S.Y., Chen,X., Yao,J., Cao,X.,
            Zhen,Y.F. and Wang,Q.
  TITLE     The mitochondrial protein TIMM44 is required for angiogenesis in
            vitro and in vivo
  JOURNAL   Cell Death Dis 14 (5), 307 (2023)
   PUBMED   37147302
  REMARK    GeneRIF: The mitochondrial protein TIMM44 is required for
            angiogenesis in vitro and in vivo.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Guo,Y.Z., Chen,G., Huang,M., Wang,Y., Liu,Y.Y., Jiang,Q., Cao,C.
            and Liu,F.
  TITLE     TIMM44 is a potential therapeutic target of human glioma
  JOURNAL   Theranostics 12 (17), 7586-7602 (2022)
   PUBMED   36438483
  REMARK    GeneRIF: TIMM44 is a potential therapeutic target of human glioma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Yu,X., Li,Y., Ding,Y., Zhang,H., Ding,N. and Lu,M.
  TITLE     HuR Promotes Ovarian Cancer Cell Proliferation by Regulating TIMM44
            mRNA Stability
  JOURNAL   Cell Biochem Biophys 78 (4), 447-453 (2020)
   PUBMED   32901414
  REMARK    GeneRIF: HuR Promotes Ovarian Cancer Cell Proliferation by
            Regulating TIMM44 mRNA Stability.
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Yuryev,A. and Wennogle,L.P.
  TITLE     Novel raf kinase protein-protein interactions found by an
            exhaustive yeast two-hybrid analysis
  JOURNAL   Genomics 81 (2), 112-125 (2003)
   PUBMED   12620389
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Yuryev,A., Ono,M., Goff,S.A., Macaluso,F. and Wennogle,L.P.
  TITLE     Isoform-specific localization of A-RAF in mitochondria
  JOURNAL   Mol Cell Biol 20 (13), 4870-4878 (2000)
   PUBMED   10848612
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Moro,F., Sirrenberg,C., Schneider,H.C., Neupert,W. and Brunner,M.
  TITLE     The TIM17.23 preprotein translocase of mitochondria: composition
            and function in protein transport into the matrix
  JOURNAL   EMBO J 18 (13), 3667-3675 (1999)
   PUBMED   10393182
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Bauer,M.F., Gempel,K., Reichert,A.S., Rappold,G.A., Lichtner,P.,
            Gerbitz,K.D., Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     Genetic and structural characterization of the human mitochondrial
            inner membrane translocase
  JOURNAL   J Mol Biol 289 (1), 69-82 (1999)
   PUBMED   10339406
REFERENCE   10 (residues 1 to 452)
  AUTHORS   Abbott,W.M., Mellor,A., Edwards,Y. and Feizi,T.
  TITLE     Soluble bovine galactose-binding lectin. cDNA cloning reveals the
            complete amino acid sequence and an antigenic relationship with the
            major encephalitogenic domain of myelin basic protein
  JOURNAL   Biochem J 259 (1), 283-290 (1989)
   PUBMED   2470348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK289634.1, BC033628.1 and
            AC010336.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 14, 2003 this sequence version replaced NP_006342.1.
            
            Summary: This gene encodes a peripheral membrane protein associated
            with the mitochondrial inner membrane translocase, which functions
            in the import of proteins across the mitochondrial inner membrane
            and into the mitochondrial matrix. The encoded protein mediates
            binding of mitochondrial heat shock protein 70 to the translocase
            of inner mitochondrial membrane 23 (TIM23) complex. Expression of
            this gene is upregulated in kidney in a mouse model of diabetes. A
            mutation in this gene is associated with familial oncocytic thyroid
            carcinoma. [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.259519.1,
                                           SRR3476690.415820.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000270538.8/
                                                  ENSP00000270538.2
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..452
                     /product="mitochondrial import inner membrane translocase
                     subunit TIM44"
                     /note="translocase of inner mitochondrial membrane 44
                     homolog"
                     /calculated_mol_wt=51225
     Region          65..442
                     /region_name="3a0801s03tim44"
                     /note="mitochondrial import inner membrane, translocase
                     subunit; TIGR00984"
                     /db_xref="CDD:130057"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43615.2)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43615.2)"
     CDS             1..452
                     /gene="TIMM44"
                     /gene_synonym="TIM44"
                     /coded_by="NM_006351.4:16..1374"
                     /db_xref="CCDS:CCDS12192.1"
                     /db_xref="GeneID:10469"
                     /db_xref="HGNC:HGNC:17316"
                     /db_xref="MIM:605058"
ORIGIN      
        1 maaaalrsgw crcprrclgs giqflsshnl phgstyqmrr pggelplsks yssgnrkgfl
       61 sglldnvkqe laknkemkes ikkfrdearr leesdvlqea rrkyktiese tvrtsevlrk
      121 klgeltgtvk eslhevsksd lgrkikegve eaaktakqsa esvskggekl grtaafrals
      181 qgvesvkkei ddsvlgqtgp yrrpqrlrkr tefagdkfke ekvfepneea lgvvlhkdsk
      241 wyqqwkdfke nnvvfnrffe mkmkydesdn afirasralt dkvtdllggl fsktemsevl
      301 teilrvdpaf dkdrflkqce ndiipnvlea misgeldilk dwcyeatysq lahpiqqaka
      361 lglqfhsril didnvdlamg kmmeqgpvli itfqaqlvmv vrnpkgevve gdpdkvlrml
      421 yvwalcrdqd elnpyaawrl ldisassteq il
//
LOCUS       NP_056349                903 aa            linear   PRI 27-APR-2025
DEFINITION  ZZ-type zinc finger-containing protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_056349
VERSION     NP_056349.1
DBSOURCE    REFSEQ: accession NM_015534.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Lo Conte,M., Lucchino,V., Scalise,S., Zannino,C., Valente,D.,
            Rossignoli,G., Murfuni,M.S., Cicconetti,C., Scaramuzzino,L.,
            Matassa,D.S., Procopio,A., Martello,G., Cuda,G. and Parrotta,E.I.
  TITLE     Unraveling the impact of ZZZ3 on the mTOR/ribosome pathway in human
            embryonic stem cells homeostasis
  JOURNAL   Stem Cell Reports 19 (5), 729-743 (2024)
   PUBMED   38701777
  REMARK    GeneRIF: Unraveling the impact of ZZZ3 on the mTOR/ribosome pathway
            in human embryonic stem cells homeostasis.
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Mi,W., Zhang,Y., Lyu,J., Wang,X., Tong,Q., Peng,D., Xue,Y.,
            Tencer,A.H., Wen,H., Li,W., Kutateladze,T.G. and Shi,X.
  TITLE     The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated
            histone acetylation and gene activation
  JOURNAL   Nat Commun 9 (1), 3759 (2018)
   PUBMED   30217978
  REMARK    GeneRIF: Study identifies the ZZ domain of ZZZ3 as a histone H3
            reader that is required for the ATAC complex-mediated maintenance
            of histone acetylation and gene activation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Orpinell,M., Fournier,M., Riss,A., Nagy,Z., Krebs,A.R., Frontini,M.
            and Tora,L.
  TITLE     The ATAC acetyl transferase complex controls mitotic progression by
            targeting non-histone substrates
  JOURNAL   EMBO J 29 (14), 2381-2394 (2010)
   PUBMED   20562830
REFERENCE   7  (residues 1 to 903)
  AUTHORS   Nagy,Z., Riss,A., Fujiyama,S., Krebs,A., Orpinell,M., Jansen,P.,
            Cohen,A., Stunnenberg,H.G., Kato,S. and Tora,L.
  TITLE     The metazoan ATAC and SAGA coactivator HAT complexes regulate
            different sets of inducible target genes
  JOURNAL   Cell Mol Life Sci 67 (4), 611-628 (2010)
   PUBMED   19936620
REFERENCE   8  (residues 1 to 903)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 903)
  AUTHORS   Guelman,S., Kozuka,K., Mao,Y., Pham,V., Solloway,M.J., Wang,J.,
            Wu,J., Lill,J.R. and Zha,J.
  TITLE     The double-histone-acetyltransferase complex ATAC is essential for
            mammalian development
  JOURNAL   Mol Cell Biol 29 (5), 1176-1188 (2009)
   PUBMED   19103755
REFERENCE   10 (residues 1 to 903)
  AUTHORS   Guelman,S., Suganuma,T., Florens,L., Swanson,S.K., Kiesecker,C.L.,
            Kusch,T., Anderson,S., Yates,J.R. 3rd, Washburn,M.P., Abmayr,S.M.
            and Workman,J.L.
  TITLE     Host cell factor and an uncharacterized SANT domain protein are
            stable components of ATAC, a novel dAda2A/dGcn5-containing histone
            acetyltransferase complex in Drosophila
  JOURNAL   Mol Cell Biol 26 (3), 871-882 (2006)
   PUBMED   16428443
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX641001.1, AC093575.2, BX640658.1 and CA448091.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX641001.1, SRR1803614.222290.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370801.8/ ENSP00000359837.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..903
                     /product="ZZ-type zinc finger-containing protein 3 isoform
                     1"
                     /note="zinc finger, ZZ domain containing 3; ATAC component
                     1 homolog; ZZ-type zinc finger-containing protein 3"
                     /calculated_mol_wt=101892
     Region          1..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Region          297..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Region          373..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Site            394
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6KAQ7; propagated from
                     UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Region          602..636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Region          655..703
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cd00167"
                     /db_xref="CDD:238096"
     Site            order(655,690..691,693..694,696..698,700..702)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Site            701
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8IYH5.1)"
     Region          821..872
                     /region_name="ZZ_ZZZ3"
                     /note="Zinc finger, ZZ type. Zinc finger present in ZZZ3
                     (ZZ finger containing 3) and related proteins. The ZZ
                     motif coordinates two zinc ions and most likely
                     participates in ligand binding or molecular scaffolding;
                     cd02341"
                     /db_xref="CDD:239081"
     Site            order(823,826,838,841,853,856,863,867)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239081"
     Site            order(823,826,853,856)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239081"
     Site            order(824,835,837,849,851)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239081"
     Site            order(836,857,869,872)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239081"
     Site            order(838,841,863,867)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239081"
     CDS             1..903
                     /gene="ZZZ3"
                     /gene_synonym="ATAC1"
                     /coded_by="NM_015534.6:477..3188"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS677.1"
                     /db_xref="GeneID:26009"
                     /db_xref="HGNC:HGNC:24523"
                     /db_xref="MIM:619892"
ORIGIN      
        1 maasrstrvt rstvglngld esfcgrtlrn rsiahpeeis snsqvrsrsp kkrpepvpiq
       61 kgnnngrttd lkqqstresw vsprkrglss sekdnierqa iencerrqte pvspvlkrik
      121 rclrseapns seedspiksd kesveqrstv vdndadfqgt kracrclild dcekreikkv
      181 nvseegplns avveeitgyl avngvddsds avincddcqp dgntkqnsig syvlqeksva
      241 engdtdtqts mfldsrkeds yidhkvpctd sqvqvkledh kivtaclpve hvnqlttepa
      301 tgpfsetqss lrdseeevdv vgdssaskeq ckentnneld tslesmpasg epepspvldc
      361 vsaqmmslse pqehrytlrt sprraaptrg sptknsspyr engqfeennl spnetnatvs
      421 dnvsqsptnp geisqnekgi ccdsqnngse gvskppsear lnighlpsak esasqhitee
      481 edddpdvyyf esdhvalkhn kdyqrllqti avleaqrsqa vqdleslgrh qrealknpig
      541 fveklqkkad iglpypqrvv qlpeivwdqy thslgnfere fknrkrhtrr vklvfdkvgl
      601 parpkspldp kkdgeslsys mlplsdgpeg sssrpqmirg rlcddtkpet fnqlwtveeq
      661 kkleqlliky ppeevesrrw qkiadelgnr takqvasrvq kyfikltkag ipvpgrtpnl
      721 yiyskkssts rrqhplnkhl fkpstfmtsh eppvymdedd drscfhshmn tavedasdde
      781 sipimyrnlp eykellqfkk lkkqklqqmq aesgfvqhvg fkcdncgiep iqgvrwhcqd
      841 cppemsldfc dscsdclhet dihkedhqle piyrsetfld rdycvsqgts ynyldpnyfp
      901 anr
//
LOCUS       NP_653273               1139 aa            linear   PRI 27-APR-2025
DEFINITION  otoancorin isoform 1 precursor [Homo sapiens].
ACCESSION   NP_653273 XP_001126535 XP_011544049
VERSION     NP_653273.3
DBSOURCE    REFSEQ: accession NM_144672.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Yang,J.Y., Wang,Q.Q., Han,M.Y., Huang,S.S., Kang,D.Y., Zhang,X.,
            Yang,S.Y., Dai,P. and Yuan,Y.Y.
  TITLE     [Phenotype-genotype analysis of the autosomal recessive hereditary
            hearing loss caused by OTOA variations]
  JOURNAL   Zhonghua Er Bi Yan Hou Tou Jing Wai Ke Za Zhi 58 (5), 460-469
            (2023)
   PUBMED   37114731
  REMARK    GeneRIF: [Phenotype-genotype analysis of the autosomal recessive
            hereditary hearing loss caused by OTOA variations].
REFERENCE   2  (residues 1 to 1139)
  AUTHORS   Laurent,S., Gehrig,C., Nouspikel,T., Amr,S.S., Oza,A., Murphy,E.,
            Vannier,A., Bena,F.S., Carminho-Rodrigues,M.T., Blouin,J.L., Cao
            Van,H., Abramowicz,M., Paoloni-Giacobino,A. and Guipponi,M.
  TITLE     Molecular characterization of pathogenic OTOA gene conversions in
            hearing loss patients
  JOURNAL   Hum Mutat 42 (4), 373-377 (2021)
   PUBMED   33492714
  REMARK    GeneRIF: Molecular characterization of pathogenic OTOA gene
            conversions in hearing loss patients.
REFERENCE   3  (residues 1 to 1139)
  AUTHORS   Zhang,L., Tian,W. and Zhou,B.
  TITLE     Polymorphisms in Neuronal Growth Regulator 1 and Otoancorin
            Alternate the Susceptibility to Lung Cancer in Chinese Nonsmoking
            Females
  JOURNAL   DNA Cell Biol 39 (9), 1657-1663 (2020)
   PUBMED   32552051
  REMARK    GeneRIF: Polymorphisms in Neuronal Growth Regulator 1 and
            Otoancorin Alternate the Susceptibility to Lung Cancer in Chinese
            Nonsmoking Females.
REFERENCE   4  (residues 1 to 1139)
  AUTHORS   Kim,B.J., Kim,D.K., Han,J.H., Oh,J., Kim,A.R., Lee,C., Kim,N.K.,
            Park,H.R., Kim,M.Y., Lee,S., Lee,S., Oh,D.Y., Park,W.Y., Park,S.
            and Choi,B.Y.
  TITLE     Clarification of glycosylphosphatidylinositol anchorage of
            OTOANCORIN and human OTOA variants associated with deafness
  JOURNAL   Hum Mutat 40 (5), 525-531 (2019)
   PUBMED   30740825
  REMARK    GeneRIF: the results of this reverse translational study confirmed
            GPI-anchorage of OTOA and showed that downstream sequences from the
            589th amino acid are critical for GPI-anchorage.
REFERENCE   5  (residues 1 to 1139)
  AUTHORS   He,L., Pang,X., Liu,H., Chai,Y., Wu,H. and Yang,T.
  TITLE     Targeted next-generation sequencing and parental genotyping in
            sporadic Chinese Han deaf patients
  JOURNAL   Clin Genet 93 (4), 899-904 (2018)
   PUBMED   29178603
  REMARK    GeneRIF: non-segregation of an OTOA p.Gln293Arg variant led to the
            discovery of a genomic microdeletion of OTOA on the opposite allele
            by copy number variation analysis. Overall, 13 pairs of recessive
            candidate variants were deemed causative in 13 patients.
REFERENCE   6  (residues 1 to 1139)
  AUTHORS   Lee,K., Chiu,I., Santos-Cortez,R.L., Basit,S., Khan,S., Azeem,Z.,
            Andrade,P.B., Kim,S.S., Ahmad,W. and Leal,S.M.
  TITLE     Novel OTOA mutations cause autosomal recessive non-syndromic
            hearing impairment in Pakistani families
  JOURNAL   Clin Genet 84 (3), 294-296 (2013)
   PUBMED   23173898
  REMARK    GeneRIF: A description of two novel OTOA mutations that were
            discovered in three consanguineous Pakistani families segregating
            autosomal recessive non-syndromic hearing impairment.
REFERENCE   7  (residues 1 to 1139)
  AUTHORS   Shahin,H., Walsh,T., Rayyan,A.A., Lee,M.K., Higgins,J., Dickel,D.,
            Lewis,K., Thompson,J., Baker,C., Nord,A.S., Stray,S., Gurwitz,D.,
            Avraham,K.B., King,M.C. and Kanaan,M.
  TITLE     Five novel loci for inherited hearing loss mapped by SNP-based
            homozygosity profiles in Palestinian families
  JOURNAL   Eur J Hum Genet 18 (4), 407-413 (2010)
   PUBMED   19888295
  REMARK    GeneRIF: Large deletions in OTOA gene is associated with hearing
            loss.
REFERENCE   8  (residues 1 to 1139)
  AUTHORS   Hofmann,O., Caballero,O.L., Stevenson,B.J., Chen,Y.T., Cohen,T.,
            Chua,R., Maher,C.A., Panji,S., Schaefer,U., Kruger,A.,
            Lehvaslaiho,M., Carninci,P., Hayashizaki,Y., Jongeneel,C.V.,
            Simpson,A.J., Old,L.J. and Hide,W.
  TITLE     Genome-wide analysis of cancer/testis gene expression
  JOURNAL   Proc Natl Acad Sci U S A 105 (51), 20422-20427 (2008)
   PUBMED   19088187
REFERENCE   9  (residues 1 to 1139)
  AUTHORS   Zwaenepoel,I., Mustapha,M., Leibovici,M., Verpy,E., Goodyear,R.,
            Liu,X.Z., Nouaille,S., Nance,W.E., Kanaan,M., Avraham,K.B.,
            Tekaia,F., Loiselet,J., Lathrop,M., Richardson,G. and Petit,C.
  TITLE     Otoancorin, an inner ear protein restricted to the interface
            between the apical surface of sensory epithelia and their overlying
            acellular gels, is defective in autosomal recessive deafness DFNB22
  JOURNAL   Proc Natl Acad Sci U S A 99 (9), 6240-6245 (2002)
   PUBMED   11972037
REFERENCE   10 (residues 1 to 1139)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092719.3, BK000099.1 and
            BC038458.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Aug 25, 2018 this sequence version replaced
            XP_011544049.1, XP_001126535.1, NP_653273.2.
            
            Summary: The protein encoded by this gene is specifically expressed
            in the inner ear, and is located at the interface between the
            apical surface of the inner ear sensory epithelia and their
            overlying acellular gels. It is prposed that this protein is
            involved in the attachment of the inner ear acellular gels to the
            apical surface of the underlying nonsensory cells. Mutations in
            this gene are associated with autosomal recessive deafness type 22
            (DFNB22). Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.61793.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159764, SAMN03267755
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000646100.2/ ENSP00000496564.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..1139
                     /product="otoancorin isoform 1 precursor"
                     /note="cancer/testis antigen 108"
                     /calculated_mol_wt=124380
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2492
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Site            211
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Site            244
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Site            321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Site            384
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Site            446
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Site            530
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Region          562..>949
                     /region_name="Mesothelin"
                     /note="Pre-pro-megakaryocyte potentiating factor precursor
                     (Mesothelin); pfam06060"
                     /db_xref="CDD:368727"
     Site            798
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Site            897
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Site            960
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7RTW8.1)"
     Region          1095..1114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTW8.1)"
     CDS             1..1139
                     /gene="OTOA"
                     /gene_synonym="CT108; DFNB22"
                     /coded_by="NM_144672.4:270..3689"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10600.2"
                     /db_xref="GeneID:146183"
                     /db_xref="HGNC:HGNC:16378"
                     /db_xref="MIM:607038"
ORIGIN      
        1 msqepttysl flflflshgv ssytvpnsrq dlhpllqnma eeiidgsyln alldliqfqs
       61 shvwtddlsh rvlaylnsrn vaftipslqa avenhleqrl hqpqklledl rktdaqqfrt
      121 amkclledkk dgldlkdiii dlgeireral qspgvnrslf litlercfqm lnslecveil
      181 gkvlrgssgs flqpditerl prdlredafk nlsavfkdly dktsahsqra lyswmtgilq
      241 tssnatddsa swvsaehlwv lgrymvhlsf eeitkispie iglfisydna tkqldmvydi
      301 tpelaqafle risssnfnmr ntstihrlgl lvcfyndlel ldatvaqvll yqmikcshlr
      361 gfqagvqklk aelldiamen qtlnetlgsl sdavvgltys qleslspeav hgaistlnqv
      421 sgwaksqvii lsakylahek vlsfynvsqm gallagvstq afcsmkrkdi sqvlrsavsq
      481 yvsdlspaqq qgilskmvqa edtapgivei qgaffkevsl fdlrrqpgfn stvlkdkelg
      541 rsqalflyel llkttrrpee llsagqlvkg vtcshidams tdfflahfqd fqnnfallsp
      601 yqvnclawky wevsrlsmpp fllaalpary lasvpasqcv pflislgksw ldslvldshk
      661 ktsvlrkvqq clddsiadey tvdimgnllc hlpaaiidrg isprawatal hglrdcpdln
      721 peqkaavrlk llgqyglpqh wtaettkdlg pflvlfsgde lssiatkfpe illqaaskma
      781 rtlptkeflw avfqsvrnss dkipsydpmp gchgvvapss ddifklaean acwaledlrc
      841 meedtfirtv ellgavqgfs rpqlmtlkek aiqvwdmpsy wrehhivslg rialalnese
      901 leqldlssid tvaslswqte wtpgqaesil qgylddsgys iqdlksfhlv glgatlcain
      961 iteiplikis efrvvvarig tllcsthvla efkrkaevvf gdptewtssv lqelgtiaag
     1021 ltkaelrmld kdlmpyfqps aikclpdeif kelsaeqias lgpenaaavt haqrrrlspl
     1081 qlqslqqald gakthswqda pasagptrts ssrspagalq swglwlgcpl lvlmakllw
//
LOCUS       NP_003417                644 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 74 isoform a [Homo sapiens].
ACCESSION   NP_003417
VERSION     NP_003417.2
DBSOURCE    REFSEQ: accession NM_003426.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Germain-Desprez,D., Bazinet,M., Bouvier,M. and Aubry,M.
  TITLE     Oligomerization of transcriptional intermediary factor 1 regulators
            and interaction with ZNF74 nuclear matrix protein revealed by
            bioluminescence resonance energy transfer in living cells
  JOURNAL   J Biol Chem 278 (25), 22367-22373 (2003)
   PUBMED   12684500
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Takase,K., Ohtsuki,T., Migita,O., Toru,M., Inada,T.,
            Yamakawa-Kobayashi,K. and Arinami,T.
  TITLE     Association of ZNF74 gene genotypes with age-at-onset of
            schizophrenia
  JOURNAL   Schizophr Res 52 (3), 161-165 (2001)
   PUBMED   11705709
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Cote,F., Boisvert,F.M., Grondin,B., Bazinet,M., Goodyer,C.G.,
            Bazett-Jones,D.P. and Aubry,M.
  TITLE     Alternative promoter usage and splicing of ZNF74 multifinger gene
            produce protein isoforms with a different repressor activity and
            nuclear partitioning
  JOURNAL   DNA Cell Biol 20 (3), 159-173 (2001)
   PUBMED   11313019
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Ravassard,P., Cote,F., Grondin,B., Bazinet,M., Mallet,J. and
            Aubry,M.
  TITLE     ZNF74, a gene deleted in DiGeorge syndrome, is expressed in human
            neural crest-derived tissues and foregut endoderm epithelia
  JOURNAL   Genomics 62 (1), 82-85 (1999)
   PUBMED   10585771
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Grondin,B., Cote,F., Bazinet,M., Vincent,M. and Aubry,M.
  TITLE     Direct interaction of the KRAB/Cys2-His2 zinc finger protein ZNF74
            with a hyperphosphorylated form of the RNA polymerase II largest
            subunit
  JOURNAL   J Biol Chem 272 (44), 27877-27885 (1997)
   PUBMED   9346935
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Grondin,B., Bazinet,M. and Aubry,M.
  TITLE     The KRAB zinc finger gene ZNF74 encodes an RNA-binding protein
            tightly associated with the nuclear matrix
  JOURNAL   J Biol Chem 271 (26), 15458-15467 (1996)
   PUBMED   8663113
REFERENCE   7  (residues 1 to 644)
  AUTHORS   Aubry,M., Demczuk,S., Desmaze,C., Aikem,M., Aurias,A., Julien,J.P.
            and Rouleau,G.A.
  TITLE     Isolation of a zinc finger gene consistently deleted in DiGeorge
            syndrome
  JOURNAL   Hum Mol Genet 2 (10), 1583-1587 (1993)
   PUBMED   8268910
REFERENCE   8  (residues 1 to 644)
  AUTHORS   Aubry,M., Marineau,C., Zhang,F.R., Zahed,L., Figlewicz,D.,
            Delattre,O., Thomas,G., de Jong,P.J., Julien,J.P. and Rouleau,G.A.
  TITLE     Cloning of six new genes with zinc finger motifs mapping to short
            and long arms of human acrocentric chromosome 22 (p and q11.2)
  JOURNAL   Genomics 13 (3), 641-648 (1992)
   PUBMED   1639391
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA791304.1, BC013395.2, BC056902.1, AC007731.16 and BG912037.1.
            
            On Oct 31, 2006 this sequence version replaced NP_003417.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Both variants 1 and 3 encode isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.86723.1,
                                           SRR1803612.113983.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000400451.7/ ENSP00000383301.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..644
                     /product="zinc finger protein 74 isoform a"
                     /note="zinc finger protein 520"
                     /calculated_mol_wt=72076
     Region          43..103
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <248..395
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          250..270
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          278..298
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          306..326
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(311,313,315,317..318,321..322,325,339,341,345..346,
                     349..350,353,367,369,371,373..374,377..378,381)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <331..511
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          334..354
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          362..382
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          390..410
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          418..438
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          446..466
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          474..494
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(479,481,483,485..486,489..490,493,507,509,513..514,
                     517..518,521,535,537,539,541..542,545..546,549)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          502..522
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          514..539
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          530..550
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          558..578
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..644
                     /gene="ZNF74"
                     /gene_synonym="COS52; hZNF7; ZFP520; ZNF520"
                     /coded_by="NM_003426.4:479..2413"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42982.1"
                     /db_xref="GeneID:7625"
                     /db_xref="HGNC:HGNC:13144"
                     /db_xref="MIM:194548"
ORIGIN      
        1 meipapepek talssqdpal slkenledis gwglpearsk esvsfkdvav dftqeewgql
       61 dspqralyrd vmlenyqnll algpplhkpd vishlergee pwsmqrevpr gpcpewelka
      121 vpsqqqgick eepaqepime rplggaqawg rqagalqrsq aapwapapam vwdvpveefp
      181 lrcplfaqqr vpeggplldt rknvqategr tkaparlcag enastpsepe kfpqvrrqrg
      241 agagegefvc gecgkafrqs ssltlhrrwh srekaykcde cgkaftwstn llehrrihtg
      301 ekpffcgecg kafschssln vhqrihtger pykcsaceka fscssllsmh lrvhtgekpy
      361 rcgecgkafn qrthltrhhr ihtgekpyqc gscgkaftch ssltvhekih sgdkpfkcsd
      421 cekafnsrsr ltlhqrthtg ekpfkcadcg kgfschayll vhrrihsgek pfkcnecgka
      481 fsshaylivh rrihtgekpf dcsqcwkafs chsslivhqr ihtgekpykc secgrafsqn
      541 hclikhqkih sgeksfkcek cgemfnwssh ltehqrlhse gkplaiqfnk hllstyyvpg
      601 sllgagdagl rdvdpidald vakllcvvpp ragrnfslgs kprn
//
LOCUS       NP_113627                388 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor SOX-7 [Homo sapiens].
ACCESSION   NP_113627
VERSION     NP_113627.1
DBSOURCE    REFSEQ: accession NM_031439.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Zhang,J., Zhang,W., Liu,J., Liu,Y., Jiang,Y., Ainiwaer,A., Chen,H.,
            Gu,Z., Chen,H., Mao,S., Guo,Y., Xu,T., Xu,Y., Wu,Y., Yao,X. and
            Yan,Y.
  TITLE     SOX7 inhibits the malignant progression of bladder cancer via the
            DNMT3B/CYGB axis
  JOURNAL   Mol Biomed 5 (1), 36 (2024)
   PUBMED   39227479
  REMARK    GeneRIF: SOX7 inhibits the malignant progression of bladder cancer
            via the DNMT3B/CYGB axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Liu,Y., Wang,X., Wang,Z., Gao,X., Xu,H., Gao,Y. and Niu,J.
  TITLE     System analysis based on weighted gene co-expression analysis
            identifies SOX7 as a novel regulator of hepatic stellate cell
            activation and liver fibrosis
  JOURNAL   FASEB J 38 (15), e23495 (2024)
   PUBMED   39126242
  REMARK    GeneRIF: System analysis based on weighted gene co-expression
            analysis identifies SOX7 as a novel regulator of hepatic stellate
            cell activation and liver fibrosis.
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Hao,Y., Bai,X.Y., Huo,F. and Chen,X.B.
  TITLE     [Downregulation of SETDB1 suppresses epithelial mesenchymal
            transition and invasion and metastasis in oral cancer via SOX7
            methylation]
  JOURNAL   Shanghai Kou Qiang Yi Xue 33 (1), 30-35 (2024)
   PUBMED   38583021
  REMARK    GeneRIF: [Downregulation of SETDB1 suppresses epithelial
            mesenchymal transition and invasion and metastasis in oral cancer
            via SOX7 methylation].
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Chiang,I.K.N., Graus,M.S., Kirschnick,N., Davidson,T., Luu,W.,
            Harwood,R., Jiang,K., Li,B., Wong,Y.Y., Moustaqil,M., Lesieur,E.,
            Skoczylas,R., Kouskoff,V., Kazenwadel,J., Arriola-Martinez,L.,
            Sierecki,E., Gambin,Y., Alitalo,K., Kiefer,F., Harvey,N.L. and
            Francois,M.
  TITLE     The blood vasculature instructs lymphatic patterning in a
            SOX7-dependent manner
  JOURNAL   EMBO J 42 (5), e109032 (2023)
   PUBMED   36715213
  REMARK    GeneRIF: The blood vasculature instructs lymphatic patterning in a
            SOX7-dependent manner.
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Chen,Q., Xi,X., Ma,J., Wang,X., Xia,Y., Wang,X., Deng,Y. and Li,Y.
  TITLE     The mechanism by which crocetin regulates the lncRNA
            NEAT1/miR-125b-5p/SOX7 molecular axis to inhibit high
            glucose-induced diabetic retinopathy
  JOURNAL   Exp Eye Res 222, 109157 (2022)
   PUBMED   35718188
  REMARK    GeneRIF: The mechanism by which crocetin regulates the lncRNA
            NEAT1/miR-125b-5p/SOX7 molecular axis to inhibit high
            glucose-induced diabetic retinopathy.
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Zhang,Y., Huang,S., Dong,W., Li,L., Feng,Y., Pan,L., Han,Z.,
            Wang,X., Ren,G., Su,D., Huang,B. and Lu,J.
  TITLE     SOX7, down-regulated in colorectal cancer, induces apoptosis and
            inhibits proliferation of colorectal cancer cells
  JOURNAL   Cancer Lett 277 (1), 29-37 (2009)
   PUBMED   19108950
  REMARK    GeneRIF: SOX7, down-regulated in colorectal cancer, induces
            apoptosis and inhibits proliferation of colorectal cancer cells.
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Semb,H.
  TITLE     Expandable endodermal progenitors: new tools to explore endoderm
            and its derivatives
  JOURNAL   Cell Stem Cell 3 (4), 355-356 (2008)
   PUBMED   18940723
  REMARK    GeneRIF: stable expression induces a stable expandable extra
            embryonic endoderm phenotype in hESCs
REFERENCE   8  (residues 1 to 388)
  AUTHORS   Guo,L., Zhong,D., Lau,S., Liu,X., Dong,X.Y., Sun,X., Yang,V.W.,
            Vertino,P.M., Moreno,C.S., Varma,V., Dong,J.T. and Zhou,W.
  TITLE     Sox7 Is an independent checkpoint for beta-catenin function in
            prostate and colon epithelial cells
  JOURNAL   Mol Cancer Res 6 (9), 1421-1430 (2008)
   PUBMED   18819930
  REMARK    GeneRIF: Sox7 is a tumor suppressor that functions as an
            independent checkpoint for beta-catenin transcriptional activity.
            Inactivation of Sox7 could promote the development of a majority of
            colorectal tumors and approximately half of prostate tumors.
REFERENCE   9  (residues 1 to 388)
  AUTHORS   Seguin,C.A., Draper,J.S., Nagy,A. and Rossant,J.
  TITLE     Establishment of endoderm progenitors by SOX transcription factor
            expression in human embryonic stem cells
  JOURNAL   Cell Stem Cell 3 (2), 182-195 (2008)
   PUBMED   18682240
  REMARK    GeneRIF: stable endoderm progenitors can be established from human
            ES cells by constitutive expression of SOX7 producing
            extraembryonic endoderm progenitors
REFERENCE   10 (residues 1 to 388)
  AUTHORS   Takash,W., Canizares,J., Bonneaud,N., Poulat,F., Mattei,M.G.,
            Jay,P. and Berta,P.
  TITLE     SOX7 transcription factor: sequence, chromosomal localisation,
            expression, transactivation and interference with Wnt signalling
  JOURNAL   Nucleic Acids Res 29 (21), 4274-4283 (2001)
   PUBMED   11691915
  REMARK    GeneRIF: gene expression, chromosome mapping, transactivation,
            interference with Wnt signaling
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY089489.1, BC004299.1 and
            AC105001.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the SOX (SRY-related
            HMG-box) family of transcription factors involved in the regulation
            of embryonic development and in the determination of the cell fate.
            The encoded protein may act as a transcriptional regulator after
            forming a protein complex with other proteins. The protein may play
            a role in tumorigenesis. A similar protein in mice is involved in
            the regulation of the wingless-type MMTV integration site family
            (Wnt) pathway. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA888228.1, SRR1660807.89138.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304501.2/ ENSP00000301921.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..388
                     /product="transcription factor SOX-7"
                     /note="SRY (sex determining region Y)-box 7; SRY-box 7"
                     /calculated_mol_wt=42066
     Region          20..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT81.1)"
     Region          34..121
                     /region_name="HMG-box_SoxF_SOX7"
                     /note="high mobility group (HMG)-box found in sex
                     determining region Y (SRY)-box 7 (SOX7) and similar
                     proteins; cd22046"
                     /db_xref="CDD:438849"
     Site            order(46..47,49..50,52..53,57,60,71..73,76..77,80,83,
                     113..114,116..118)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438849"
     Region          140..197
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT81.1)"
     Region          <198..230
                     /region_name="Sox17_18_mid"
                     /note="Sox 17/18 central domain; pfam12067"
                     /db_xref="CDD:463454"
     CDS             1..388
                     /gene="SOX7"
                     /coded_by="NM_031439.4:79..1245"
                     /db_xref="CCDS:CCDS5977.1"
                     /db_xref="GeneID:83595"
                     /db_xref="HGNC:HGNC:18196"
                     /db_xref="MIM:612202"
ORIGIN      
        1 masllgaypw peglecpald aelsdgqspp avprppgdkg sesrirrpmn afmvwakder
       61 krlavqnpdl hnaelskmlg kswkaltlsq krpyvdeaer lrlqhmqdyp nykyrprrkk
      121 qakrlckrvd pgfllsslsr dqnalpekrs gsrgalgeke drgeyspgta lpslrgcyhe
      181 gpaggggggt pssvdtypyg lptppemspl dvlepeqtff sspcqeehgh prriphlpgh
      241 pyspeyapsp lhcshplgsl algqspgvsm mspvpgcpps payyspatyh plhsnlqahl
      301 gqlspppehp gfdaldqlsq vellgdmdrn efdqylntpg hpdsatgama lsghvpvsqv
      361 tptgptetsl isvladatat yynsysvs
//
LOCUS       NP_543150                329 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat and SOCS box protein 5 isoform 1 [Homo sapiens].
ACCESSION   NP_543150
VERSION     NP_543150.1
DBSOURCE    REFSEQ: accession NM_080874.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Liu,P., Verhaar,A.P. and Peppelenbosch,M.P.
  TITLE     Signaling Size: Ankyrin and SOCS Box-Containing ASB E3 Ligases in
            Action
  JOURNAL   Trends Biochem Sci 44 (1), 64-74 (2019)
   PUBMED   30446376
  REMARK    Review article
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kile,B.T., Schulman,B.A., Alexander,W.S., Nicola,N.A., Martin,H.M.
            and Hilton,D.J.
  TITLE     The SOCS box: a tale of destruction and degradation
  JOURNAL   Trends Biochem Sci 27 (5), 235-241 (2002)
   PUBMED   12076535
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX647857.1 and AC093605.3.
            
            Summary: The protein encoded by this gene is a member of the
            ankyrin repeat and SOCS box-containing (ASB) family of proteins.
            They contain ankyrin repeat sequence and SOCS box domain. The SOCS
            box serves to couple suppressor of cytokine signalling (SOCS)
            proteins and their binding partners with the elongin B and C
            complex, possibly targeting them for degradation. Multiple
            alternatively spliced transcript variants have been described for
            this gene but their full length sequences are not known. [provided
            by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647857.1, AK096441.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159368 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296525.7/ ENSP00000296525.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q34.2"
     Protein         1..329
                     /product="ankyrin repeat and SOCS box protein 5 isoform 1"
                     /note="SOCS box protein ASB-5; ankyrin repeat and SOCS box
                     protein 5"
                     /calculated_mol_wt=36210
     Region          35..284
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          69..98
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWX0.1)"
     Site            order(71,75..76,79..81,83..84,88,91,100,102,104,108..109,
                     112..114,116..117,121,124,133,135,137,141..142,145..147,
                     149..150,154,157)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          71..100
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          102..133
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          102..131
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWX0.1)"
     Region          135..164
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWX0.1)"
     Region          135..160
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          167..196
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWX0.1)"
     Region          170..198
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(173..174,177..179,181..182,186,189,198,200,202,
                     206..207,210..212,214..215,219,222,230,232,234,238..239,
                     242..244,246..247,251,254,263)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          200..230
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          200..229
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWX0.1)"
     Region          232..263
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          232..261
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWX0.1)"
     Region          288..329
                     /region_name="SOCS_ASB5"
                     /note="SOCS (suppressors of cytokine signaling) box of
                     ASB5-like proteins. ASB family members have a C-terminal
                     SOCS box and an N-terminal ankyrin-related sequence. ASB5
                     has been implicated in the initiation of arteriogenesis.
                     The general function of the SOCS...; cd03724"
                     /db_xref="CDD:239694"
     Site            order(289..294,300,310,316,321)
                     /site_type="other"
                     /note="putative elongin B/C interaction [polypeptide
                     binding]"
                     /db_xref="CDD:239694"
     CDS             1..329
                     /gene="ASB5"
                     /gene_synonym="ASB-5"
                     /coded_by="NM_080874.4:115..1104"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3827.1"
                     /db_xref="GeneID:140458"
                     /db_xref="HGNC:HGNC:17180"
                     /db_xref="MIM:615050"
ORIGIN      
        1 msvleenrpf aqqlsnvyft ilslfcfklf vkislailsh fyivkgnrke aariaaefyg
       61 vtqgqgswad rsplheaasq grllalrtll sqgynvnavt ldhvtplhea clgdhvacar
      121 tlleaganvn aitidgvtpl fnacsqgsps caellleyga kaqlesclps ptheaaskgh
      181 hecldilisw gidvdqeiph lgtplyvacm sqqfhciwkl lyagadvqkg kywdtplhaa
      241 aqqssteivn lllefgadin akntellrpi dvatsssmve rillqheatp sslyqlcrlc
      301 irsyigkprl hlipqlqlpt llknflqyr
//
LOCUS       NP_001003681             601 aa            linear   PRI 27-APR-2025
DEFINITION  HMG domain-containing protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001003681
VERSION     NP_001003681.1
DBSOURCE    REFSEQ: accession NM_001003681.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Frankel,B.M., Cachia,D., Patel,S.J. and Das,A.
  TITLE     Analysis of the P53N a Novel Protein Encoded on Chromosome
            22q12.1-12.3 in Glioblastomas and Ependymomas Specimens
  JOURNAL   J Mol Neurosci 71 (8), 1714-1722 (2021)
   PUBMED   33595778
  REMARK    GeneRIF: Analysis of the P(53N) a Novel Protein Encoded on
            Chromosome 22q12.1-12.3 in Glioblastomas and Ependymomas Specimens.
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Salati,S., Zini,R., Nuzzo,S., Guglielmelli,P., Pennucci,V.,
            Prudente,Z., Ruberti,S., Rontauroli,S., Norfo,R., Bianchi,E.,
            Bogani,C., Rotunno,G., Fanelli,T., Mannarelli,C., Rosti,V.,
            Salmoiraghi,S., Pietra,D., Ferrari,S., Barosi,G., Rambaldi,A.,
            Cazzola,M., Bicciato,S., Tagliafico,E., Vannucchi,A.M. and
            Manfredini,R.
  CONSRTM   AGIMM (AIRC Gruppo Italiano Malattie Mieloproliferative)
            investigators
  TITLE     Integrative analysis of copy number and gene expression data
            suggests novel pathogenetic mechanisms in primary myelofibrosis
  JOURNAL   Int J Cancer 138 (7), 1657-1669 (2016)
   PUBMED   26547506
  REMARK    GeneRIF: These results highlight a previously un-reported role of
            HMGXB4 in the hematopoietic system and transcriptional imbalances
            of HMGXB4 could contribute to the aberrant expansion of the
            megakaryocytic lineage in primary myelofibrosis patients
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Vermeulen,M., Eberl,H.C., Matarese,F., Marks,H., Denissov,S.,
            Butter,F., Lee,K.K., Olsen,J.V., Hyman,A.A., Stunnenberg,H.G. and
            Mann,M.
  TITLE     Quantitative interaction proteomics and genome-wide profiling of
            epigenetic histone marks and their readers
  JOURNAL   Cell 142 (6), 967-980 (2010)
   PUBMED   20850016
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Potash,J.B., Buervenich,S., Cox,N.J., Zandi,P.P., Akula,N.,
            Steele,J., Rathe,J.A., Avramopoulos,D., Detera-Wadleigh,S.D.,
            Gershon,E.S., DePaulo,J.R. Jr., Feinberg,A.P. and McMahon,F.J.
  CONSRTM   NIMH Genetics Initiative Bipolar Disorder Consortium
  TITLE     Gene-based SNP mapping of a psychotic bipolar affective disorder
            linkage region on 22q12.3: association with HMG2L1 and TOM1
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 147B (1), 59-67 (2008)
   PUBMED   17671966
  REMARK    GeneRIF: high-mobility group protein 2-like 1 and SNP mapping of a
            psychotic bipolar affective disorder linkage region on 22q12.3
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Nery,F.C., Rui,E., Kuniyoshi,T.M. and Kobarg,J.
  TITLE     Evidence for the interaction of the regulatory protein Ki-1/57 with
            p53 and its interacting proteins
  JOURNAL   Biochem Biophys Res Commun 341 (3), 847-855 (2006)
   PUBMED   16455055
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   9  (residues 1 to 601)
  AUTHORS   Collins,J.E., Goward,M.E., Cole,C.G., Smink,L.J., Huckle,E.J.,
            Knowles,S., Bye,J.M., Beare,D.M. and Dunham,I.
  TITLE     Reevaluating human gene annotation: a second-generation analysis of
            chromosome 22
  JOURNAL   Genome Res 13 (1), 27-36 (2003)
   PUBMED   12529303
REFERENCE   10 (residues 1 to 601)
  AUTHORS   Seroussi,E., Kedra,D., Kost-Alimova,M., Sandberg-Nordqvist,A.C.,
            Fransson,I., Jacobs,J.F., Fu,Y., Pan,H.Q., Roe,B.A., Imreh,S. and
            Dumanski,J.P.
  TITLE     TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1
            and encode proteins similar to the endosomal proteins HGS and STAM
  JOURNAL   Genomics 57 (3), 380-388 (1999)
   PUBMED   10329004
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DW452042.1, BC052624.1,
            BC040447.1 and AI471703.1.
            
            Summary: High mobility group (HMG) proteins are nonhistone
            chromosomal proteins. See HMG2 (MIM 163906) for additional
            information on HMG proteins.[supplied by OMIM, Nov 2010].
            
            Transcript Variant: This variant (1) encodes the longer protein
            (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.238083.1,
                                           SRR1803614.81990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216106.6/ ENSP00000216106.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..601
                     /product="HMG domain-containing protein 4 isoform 1"
                     /note="HMG domain-containing protein 4; HMG box-containing
                     protein 4; high mobility group protein 2-like 1; HMG box
                     domain containing 4"
                     /calculated_mol_wt=65581
     Region          51..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGU5.2)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UGU5.2)"
     Region          110..232
                     /region_name="DUF4171"
                     /note="Domain of unknown function (DUF4171); pfam13775"
                     /db_xref="CDD:463979"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UGU5.2)"
     Region          407..467
                     /region_name="HMG-box_HMGXB4"
                     /note="high mobility group (HMG)-box found in HMG
                     domain-containing protein 4 (HMGXB4) and similar proteins;
                     cd21982"
                     /db_xref="CDD:438798"
     Site            order(408..409,411..415,418..419,426,438..439,442,
                     445..446,453,457,460,464,467)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438798"
     Region          473..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGU5.2)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UGU5.2)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UGU5.2)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UGU5.2)"
     CDS             1..601
                     /gene="HMGXB4"
                     /gene_synonym="HMG2L1; HMGBCG; P53N; THC211630"
                     /coded_by="NM_001003681.3:134..1939"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33641.1"
                     /db_xref="GeneID:10042"
                     /db_xref="HGNC:HGNC:5003"
                     /db_xref="MIM:604702"
ORIGIN      
        1 mayddsvkke dcfdgdhtfe diglaagrsq rekkrsykdf lreeeeiaaq vrnsskkklk
       61 dselyflgtd thkkkrkhss ddyyygdiss lessqkkkkk sspqstdtam dllkaitspl
      121 aagskpskkt gekssgsssh seskkehhrk kvsgssgelp ledggshksk kmkplyvnte
      181 tltlrepdgl kmklilspke kgsssvdees fqypsqqatv kksskksard eqgalllghe
      241 lqsflktark khksssdahs spgpegcgsd asqfaeshsa nldlsglepi lvesdsssgg
      301 eleagelvid dsyreikkkk kskkskkkkd kekhkekrhs kskrslglsa vpvgevtvts
      361 gpppsipyag aaapplplpg lhtdghsekk kkkeekdker ergekpkkkn msayqvfcke
      421 yrvtivadhp gidfgelskk laevwkqlpe kdkliwkqka qylqhkqnka eattvkrkas
      481 ssegsmkvka ssvgvlspqk ksppttmllp aspakapete pidvaahlql lgeslsligh
      541 rlqetegmva vsgslsvlld siicalgpla clttqlpeln gcpkqvlsnt ldniayimpg
      601 l
//
LOCUS       NP_056275                859 aa            linear   PRI 27-APR-2025
DEFINITION  rab effector MyRIP isoform a [Homo sapiens].
ACCESSION   NP_056275 XP_947129 XP_950737
VERSION     NP_056275.2
DBSOURCE    REFSEQ: accession NM_015460.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Conte,I.L., Hellen,N., Bierings,R., Mashanov,G.I., Manneville,J.B.,
            Kiskin,N.I., Hannah,M.J., Molloy,J.E. and Carter,T.
  TITLE     Interaction between MyRIP and the actin cytoskeleton regulates
            Weibel-Palade body trafficking and exocytosis
  JOURNAL   J Cell Sci 129 (3), 592-603 (2016)
   PUBMED   26675235
  REMARK    GeneRIF: The role of MyRIP in Ca(2+)-driven exocytosis requires
            both MyoVa- and actin-binding potential.
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Huet,S., Fanget,I., Jouannot,O., Meireles,P., Zeiske,T.,
            Larochette,N., Darchen,F. and Desnos,C.
  TITLE     Myrip couples the capture of secretory granules by the actin-rich
            cell cortex and their attachment to the plasma membrane
  JOURNAL   J Neurosci 32 (7), 2564-2577 (2012)
   PUBMED   22396429
  REMARK    GeneRIF: Myrip couples the retention of secretory granules in the
            cell cortex, their transport to the plasma membrane, and their
            attachment to the plasma membrane, thus promoting secretion.
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Rojo Pulido,I., Nightingale,T.D., Darchen,F., Seabra,M.C.,
            Cutler,D.F. and Gerke,V.
  TITLE     Myosin Va acts in concert with Rab27a and MyRIP to regulate acute
            von-Willebrand factor release from endothelial cells
  JOURNAL   Traffic 12 (10), 1371-1382 (2011)
   PUBMED   21740491
  REMARK    GeneRIF: A Rab27a/MyRIP/myosin Va complex is involved in linking
            von-Willebrand factor (Vwf) to the peripheral actin cytoskeleton of
            endothelial cells to allow full maturation and prevent premature
            secretion of vWF.
REFERENCE   5  (residues 1 to 859)
  AUTHORS   Kopplin,L.J., Igo,R.P. Jr., Wang,Y., Sivakumaran,T.A.,
            Hagstrom,S.A., Peachey,N.S., Francis,P.J., Klein,M.L.,
            SanGiovanni,J.P., Chew,E.Y., Pauer,G.J., Sturgill,G.M., Joshi,T.,
            Tian,L., Xi,Q., Henning,A.K., Lee,K.E., Klein,R., Klein,B.E. and
            Iyengar,S.K.
  TITLE     Genome-wide association identifies SKIV2L and MYRIP as protective
            factors for age-related macular degeneration
  JOURNAL   Genes Immun 11 (8), 609-621 (2010)
   PUBMED   20861866
  REMARK    GeneRIF: A new potentially protective effect was identified at
            rs2679798 in MYRIP.
            GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   6  (residues 1 to 859)
  AUTHORS   Goehring,A.S., Pedroja,B.S., Hinke,S.A., Langeberg,L.K. and
            Scott,J.D.
  TITLE     MyRIP anchors protein kinase A to the exocyst complex
  JOURNAL   J Biol Chem 282 (45), 33155-33167 (2007)
   PUBMED   17827149
REFERENCE   7  (residues 1 to 859)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   8  (residues 1 to 859)
  AUTHORS   Waselle,L., Coppola,T., Fukuda,M., Iezzi,M., El-Amraoui,A.,
            Petit,C. and Regazzi,R.
  TITLE     Involvement of the Rab27 binding protein Slac2c/MyRIP in insulin
            exocytosis
  JOURNAL   Mol Biol Cell 14 (10), 4103-4113 (2003)
   PUBMED   14517322
  REMARK    GeneRIF: Slac2c/MyRIP is part of a complex mediating the
            interaction of secretory granules with cortical actin cytoskeleton
REFERENCE   9  (residues 1 to 859)
  AUTHORS   Fukuda,M. and Kuroda,T.S.
  TITLE     Slac2-c (synaptotagmin-like protein homologue lacking C2
            domains-c), a novel linker protein that interacts with Rab27,
            myosin Va/VIIa, and actin
  JOURNAL   J Biol Chem 277 (45), 43096-43103 (2002)
   PUBMED   12221080
  REMARK    GeneRIF: Slac2-c/MyRIP contains an N-terminal Slp homology domain
            (SHD) and functions as a linker protein that interacts with myosin
            Rab27A/B, VIIa/Va, and actin.
REFERENCE   10 (residues 1 to 859)
  AUTHORS   El-Amraoui,A., Schonn,J.S., Kussel-Andermann,P., Blanchard,S.,
            Desnos,C., Henry,J.P., Wolfrum,U., Darchen,F. and Petit,C.
  TITLE     MyRIP, a novel Rab effector, enables myosin VIIa recruitment to
            retinal melanosomes
  JOURNAL   EMBO Rep 3 (5), 463-470 (2002)
   PUBMED   11964381
  REMARK    GeneRIF: a molecular complex composed of Rab27A, MyRIP and myosin
            VIIa bridges retinal melanosomes to the actin cytoskeleton and
            thereby mediates the local trafficking of these organelles
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104163.2, CF138044.1, BC092512.1, AB083783.1 and AK125334.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_947129.1, XP_950737.1, NP_056275.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a). Both variants 1 and
            2 encode isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092512.1, SRR1660805.196895.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302541.11/ ENSP00000301972.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.1"
     Protein         1..859
                     /product="rab effector MyRIP isoform a"
                     /note="synaptotagmin-like protein homologue lacking C2
                     domains-c; rab effector MYRIP; exophilin-8; Slp homologue
                     lacking C2 domains; slp homolog lacking C2 domains c;
                     myosin-VIIa- and Rab-interacting protein;
                     synaptotagmin-like protein lacking C2 domains C"
                     /calculated_mol_wt=95576
     Region          8..125
                     /region_name="FYVE_2"
                     /note="FYVE-type zinc finger; pfam02318"
                     /db_xref="CDD:426716"
     Region          143..560
                     /region_name="Myosin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW9.2)"
     Region          152..859
                     /region_name="Rab_eff_C"
                     /note="Rab effector MyRIP/melanophilin C-terminus;
                     pfam04698"
                     /db_xref="CDD:461398"
     Region          193..209
                     /region_name="PKA-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW9.2)"
     Region          232..248
                     /region_name="Negative regulation of PKA-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW9.2)"
     Region          251..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW9.2)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K3I4; propagated from
                     UniProtKB/Swiss-Prot (Q8NFW9.2)"
     Region          302..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW9.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TNY7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFW9.2)"
     Region          386..629
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW9.2)"
     Region          495..856
                     /region_name="Actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW9.2)"
     Region          783..812
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW9.2)"
     CDS             1..859
                     /gene="MYRIP"
                     /gene_synonym="SLAC2-C; SLAC2C"
                     /coded_by="NM_015460.4:339..2918"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2689.1"
                     /db_xref="GeneID:25924"
                     /db_xref="HGNC:HGNC:19156"
                     /db_xref="MIM:611790"
ORIGIN      
        1 mgrkldlsgl tddetehvlq vvqrdfnlrk keeerlselk qkldeegskc silskhqqfv
       61 ehccmrccsp ftflvntkrq cgdckfnvck sccsyqkhek awvccvcqqa rllraqslew
      121 fynnvksrfk rfgsakvlkn lyrkhrlesg acfdilggsl fesnlenegs isgsdstfyr
      181 qseghsvmdt lavalrvaee aieeaiskae aygdsldkqn easylrdhke elteelatti
      241 lqkiirkqks kseqqveeep gwphpqscst kvadegtsas pggyrapaal wrsqsafsit
      301 geealktppv eapsrqprdq gqhpraesal pswksvdrld etnlapvlqs pdgnwvalkd
      361 gappptrlla kpksgtfqal evassvasay demgsdseed fdwsealskl cprsralprn
      421 pqpqptqaqs sdqgpiaasp ssalspnpea mcsdsetssa gssrevghqa rlswlqrkap
      481 rnpaaekmrl hgeldvnfnp qlasretsds sepeeaphtt drrarrwrra rlgseepske
      541 psspsaqlrd ldthqvsddl setdisnear dpqtltdtte ekrrnrlyel amkmsekets
      601 sgedqesepk tesenqkesl ssednsqsvq eelkkkfsav slcnistevl kvinateeli
      661 agstgpwesp qvppdrqkgm fprgtdqvrl deqltsleen vylaagtvyg letqlteled
      721 aarcihsgtd ethladledq vataaaqvhh aelqisdies risaltiagl niapcvrftr
      781 rrdqkqrtqv qtidtsrqqr rklpappvka ekietssvtt iktfnhnfil qgsstnrtke
      841 rkgttkdlme palesavmy
//
LOCUS       NP_001356241             416 aa            linear   ROD 27-APR-2025
DEFINITION  serine/arginine-rich splicing factor 4 isoform c [Mus musculus].
ACCESSION   NP_001356241
VERSION     NP_001356241.1
DBSOURCE    REFSEQ: accession NM_001369312.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Larrasa-Alonso,J., Villalba-Orero,M., Marti-Gomez,C.,
            Ortiz-Sanchez,P., Lopez-Olaneta,M.M., Rey-Martin,M.A.,
            Sanchez-Cabo,F., McNicoll,F., Muller-McNicoll,M., Garcia-Pavia,P.
            and Lara-Pezzi,E.
  TITLE     The SRSF4-GAS5-Glucocorticoid Receptor Axis Regulates Ventricular
            Hypertrophy
  JOURNAL   Circ Res 129 (6), 669-683 (2021)
   PUBMED   34333993
  REMARK    GeneRIF: The SRSF4-GAS5-Glucocorticoid Receptor Axis Regulates
            Ventricular Hypertrophy.
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Guo,H., Li,Y., Luo,M., Lin,S., Chen,J., Ma,Q., Gu,Y., Jiang,Z. and
            Gui,Y.
  TITLE     Androgen receptor binding to an androgen-responsive element in the
            promoter of the Srsf4 gene inhibits its expression in mouse Sertoli
            cells
  JOURNAL   Mol Reprod Dev 82 (12), 976-985 (2015)
   PUBMED   26308373
  REMARK    GeneRIF: these results demonstrate that Srsf4 is a direct
            downstream target of the androgen receptor in mouse Sertoli cells.
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Manley,J.L. and Krainer,A.R.
  TITLE     A rational nomenclature for serine/arginine-rich protein splicing
            factors (SR proteins)
  JOURNAL   Genes Dev 24 (11), 1073-1074 (2010)
   PUBMED   20516191
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Guo,Y., Zhang,X., Huang,J., Zeng,Y., Liu,W., Geng,C., Li,K.W.,
            Yang,D., Wu,S., Wei,H., Han,Z., Qian,X., Jiang,Y. and He,F.
  TITLE     Relationships between hematopoiesis and hepatogenesis in the
            midtrimester fetal liver characterized by dynamic transcriptomic
            and proteomic profiles
  JOURNAL   PLoS One 4 (10), e7641 (2009)
   PUBMED   19865483
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Yomoda,J., Muraki,M., Kataoka,N., Hosoya,T., Suzuki,M., Hagiwara,M.
            and Kimura,H.
  TITLE     Combination of Clk family kinase and SRp75 modulates alternative
            splicing of Adenovirus E1A
  JOURNAL   Genes Cells 13 (3), 233-244 (2008)
   PUBMED   18298798
REFERENCE   9  (residues 1 to 416)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 416)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607088.26.
            
            Summary: The protein encoded by this gene is a member of the
            serine/arginine (SR)-rich family of pre-mRNA splicing factors,
            which constitute part of the spliceosome. Each of these factors
            contains an RNA recognition motif (RRM) for binding RNA and an RS
            domain for binding other proteins. The RS domain is rich in serine
            and arginine residues and facilitates interaction between different
            SR splicing factors. In addition to being critical for mRNA
            splicing, the SR proteins have also been shown to be involved in
            mRNA export from the nucleus and in translation. [provided by
            RefSeq, Sep 2010].
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (c)
            has a shorter and distinct N-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3403565.1,
                                           SRR13422600.514519.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849382, SAMN00849387
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 64.53 cM"
     Protein         1..416
                     /product="serine/arginine-rich splicing factor 4 isoform
                     c"
                     /note="splicing factor, arginine/serine-rich 4 (SRp75);
                     serine/arginine-rich splicing factor 4"
                     /calculated_mol_wt=47572
     Region          29..100
                     /region_name="RRM2_SRSF4_like"
                     /note="RNA recognition motif 2 (RRM2) found in
                     serine/arginine-rich splicing factor 4 (SRSF4) and similar
                     proteins; cd12600"
                     /db_xref="CDD:410012"
     Region          170..>281
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     CDS             1..416
                     /gene="Srsf4"
                     /gene_synonym="5730499P16Rik; MNCb-2616; Sfrs4; SRp75"
                     /coded_by="NM_001369312.1:438..1688"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="GeneID:57317"
                     /db_xref="MGI:MGI:1890577"
ORIGIN      
        1 myfsilfkgg ygyrrsgrdk ygpptrteyr livenlssrc swqdlkdymr qagevtyada
       61 hkgrknegvi efvsysdmkr alekldgtev ngrkirlved kpgsrrrrsy srsrshsrsr
      121 srsrhsrksr srsgsskssh sksrsrsrsg shsrsksrsr sqsrsrskke ksrspskdnk
      181 srsrsrspdk srskskdhae dklqnndsag kakshspsrh dsksrsrsqe rraeeerrrs
      241 vsrarsqeks rsqeksllks rsrsrskvgs rsrsrskdkr kgrkrsrdes rsrsrskser
      301 srkhsskrds kvssssskkk kdtdhsrsps rsvskereha kaesgqresr aegeseapnp
      361 eprarsrsts kskpnvpaes rsrsksaskt rsrskspsrs asrspsrsrs rshsrs
//
LOCUS       NP_666372                153 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane inner ear expressed protein precursor [Mus musculus].
ACCESSION   NP_666372
VERSION     NP_666372.1
DBSOURCE    REFSEQ: accession NM_146260.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Wang,P., Miller,K.K., He,E., Dhawan,S.S., Cunningham,C.L. and
            Grillet,N.
  TITLE     LOXHD1 is indispensable for maintaining TMC1 auditory
            mechanosensitive channels at the site of force transmission
  JOURNAL   Nat Commun 15 (1), 7865 (2024)
   PUBMED   39256406
  REMARK    Erratum:[Nat Commun. 2024 Oct 15;15(1):8878. doi:
            10.1038/s41467-024-52972-5. PMID: 39406713]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Jiang,Q., Zou,W., Li,S., Qiu,X., Zhu,L., Kang,L. and Muller,U.
  TITLE     Sequence variations and accessory proteins adapt TMC functions to
            distinct sensory modalities
  JOURNAL   Neuron 112 (17), 2922-2937 (2024)
   PUBMED   38986620
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Krey,J.F., Chatterjee,P., Halford,J., Cunningham,C.L., Perrin,B.J.
            and Barr-Gillespie,P.G.
  TITLE     Control of stereocilia length during development of hair bundles
  JOURNAL   PLoS Biol 21 (4), e3001964 (2023)
   PUBMED   37011103
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Ji,Y.R., Tona,Y., Wafa,T., Christman,M.E., Tourney,E.D., Jiang,T.,
            Ohta,S., Cheng,H., Fitzgerald,T., Fritzsch,B., Jones,S.M.,
            Cullen,K.E. and Wu,D.K.
  TITLE     Function of bidirectional sensitivity in the otolith organs
            established by transcription factor Emx2
  JOURNAL   Nat Commun 13 (1), 6330 (2022)
   PUBMED   36280667
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Cho,K.I., Suh,J.G., Lee,J.W., Hong,S.H., Kang,T.C., Oh,Y.S. and
            Ryoo,Z.Y.
  TITLE     The circling mouse (C57BL/6J-cir) has a 40-kilobase genomic
            deletion that includes the transmembrane inner ear (tmie) gene
  JOURNAL   Comp Med 56 (6), 476-481 (2006)
   PUBMED   17219777
  REMARK    GeneRIF: characterized the circling mutation as a 40-kilobase
            deletion that includes the transmembrane inner ear (tmie) gene
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Jones,S.M., Johnson,K.R., Yu,H., Erway,L.C., Alagramam,K.N.,
            Pollak,N. and Jones,T.A.
  TITLE     A quantitative survey of gravity receptor function in mutant mouse
            strains
  JOURNAL   J Assoc Res Otolaryngol 6 (4), 297-310 (2005)
   PUBMED   16235133
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Mitchem,K.L., Hibbard,E., Beyer,L.A., Bosom,K., Dootz,G.A.,
            Dolan,D.F., Johnson,K.R., Raphael,Y. and Kohrman,D.C.
  TITLE     Mutation of the novel gene Tmie results in sensory cell defects in
            the inner ear of spinner, a mouse model of human hearing loss DFNB6
  JOURNAL   Hum Mol Genet 11 (16), 1887-1898 (2002)
   PUBMED   12140191
  REMARK    GeneRIF: Mutation of the novel gene Tmie results in sensory cell
            defects in the inner ear of spinner, a mouse model of human hearing
            loss DFNB6.
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Vargas,G.A., Fantino,E., George-Nascimento,C., Gargus,J.J. and
            Haigler,H.T.
  TITLE     Reduced epidermal growth factor receptor expression in hypohidrotic
            ectodermal dysplasia and Tabby mice
  JOURNAL   J Clin Invest 97 (11), 2426-2432 (1996)
   PUBMED   8647934
REFERENCE   10 (residues 1 to 153)
  AUTHORS   DEOL,M.S. and ROBINS,M.W.
  TITLE     The spinner mouse
  JOURNAL   J Hered 53, 133-136 (1962)
   PUBMED   14027064
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC139378.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK030341.1, AF481143.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 60.79 cM"
     Protein         1..153
                     /product="transmembrane inner ear expressed protein
                     precursor"
                     /note="transmembrane inner ear expressed protein; spinner"
                     /calculated_mol_wt=14392
     sig_peptide     1..28
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8K467.1)"
                     /calculated_mol_wt=2653
     mat_peptide     29..153
                     /product="Transmembrane inner ear expressed protein.
                     /id=PRO_0000022556"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K467.1)"
                     /calculated_mol_wt=14392
     Region          47..132
                     /region_name="TMIE"
                     /note="TMIE protein; pfam16038"
                     /db_xref="CDD:464987"
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K467.1)"
     CDS             1..153
                     /gene="Tmie"
                     /gene_synonym="5131400L21Rik; Mm.87012; sr"
                     /coded_by="NM_146260.3:1152..1613"
                     /db_xref="CCDS:CCDS23578.1"
                     /db_xref="GeneID:20776"
                     /db_xref="MGI:MGI:2159400"
ORIGIN      
        1 magrqhgsgr lwalggaalg aclagvatql vepstappkp kpppltketv vfwdmrlwhv
       61 vgifslfvls iiitlccvfn crvprtrkei earylqrkaa kmytdkletv pplnelteip
      121 gedkkkkkkd svdtvaikve edekneakkk gek
//
LOCUS       NP_981942                266 aa            linear   PRI 27-APR-2025
DEFINITION  metallo-beta-lactamase domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_981942 XP_171171 XP_379899
VERSION     NP_981942.1
DBSOURCE    REFSEQ: accession NM_203397.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Pettinati,I., Grzechnik,P., Ribeiro de Almeida,C., Brem,J.,
            McDonough,M.A., Dhir,S., Proudfoot,N.J. and Schofield,C.J.
  TITLE     Biosynthesis of histone messenger RNA employs a specific 3' end
            endonuclease
  JOURNAL   Elife 7, e39865 (2018)
   PUBMED   30507380
  REMARK    GeneRIF: The cellular, genetic, biochemical, substrate selectivity,
            and crystallographic studies have been reported providing evidence
            that endoribonuclease, MBLAC1, is selective for 3' processing of
            replication-dependent histone pre-mRNA during the S-phase of the
            cell cycle.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC031288.1, BQ441096.1, AW772344.1 and AW449216.1.
            
            On or before May 5, 2005 this sequence version replaced
            XP_171171.1, XP_379899.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.940953.1, BC031288.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398075.4/ ENSP00000381150.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..266
                     /product="metallo-beta-lactamase domain-containing protein
                     1"
                     /EC_number="3.-.-.-"
                     /note="endoribonuclease MBLAC1"
                     /calculated_mol_wt=27071
     Region          20..236
                     /region_name="MBLAC1-like_MBL-fold"
                     /note="uncharacterized human metallo-beta-lactamase
                     domain-containing protein 1 and related proteins; MBL-fold
                     metallo hydrolase domain; cd07711"
                     /db_xref="CDD:293797"
     Region          48..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4D2B0.1)"
     Site            order(114,116,118..119,169..170,192,231)
                     /site_type="active"
                     /db_xref="CDD:293797"
     Region          229..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4D2B0.1)"
     CDS             1..266
                     /gene="MBLAC1"
                     /coded_by="NM_203397.3:127..927"
                     /db_xref="CCDS:CCDS43620.1"
                     /db_xref="GeneID:255374"
                     /db_xref="HGNC:HGNC:22180"
                     /db_xref="MIM:620906"
ORIGIN      
        1 mrteplcgas pllvpgdpys vvvllqgyae pegvgdavra dgsvtlvlpq trgpasshre
       61 sprgsggaea aleeaargpi lvdtggpwar eallgalagq gvapgdvtlv vgthghsdhi
      121 gnlglfpgaa llvshdfclp ggrylphglg egqplrlgpg levwatpghg gqrdvsvvva
      181 gtalgtvvva gdvferdgde dswqalsedp aaqersrkrv lvvadvvvpg hgppfrvlre
      241 asqpeteggg nsqqepvvgd eepalh
//
LOCUS       NP_005369                464 aa            linear   PRI 27-APR-2025
DEFINITION  N-myc proto-oncogene protein isoform 1 [Homo sapiens].
ACCESSION   NP_005369
VERSION     NP_005369.2
DBSOURCE    REFSEQ: accession NM_005378.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Vempuluru,V.S., Maniar,A., Bakal,K. and Kaliki,S.
  TITLE     Role of MYCN in retinoblastoma: A review of current literature
  JOURNAL   Surv Ophthalmol 69 (5), 697-706 (2024)
   PUBMED   38796108
  REMARK    GeneRIF: Role of MYCN in retinoblastoma: A review of current
            literature.
            Review article
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Sundaramoorthy,S., Colombo,D.F., Sanalkumar,R., Broye,L., Balmas
            Bourloud,K., Boulay,G., Cironi,L., Stamenkovic,I., Renella,R.,
            Kuttler,F., Turcatti,G., Rivera,M.N., Muhlethaler-Mottet,A.,
            Bardet,A.F. and Riggi,N.
  TITLE     Preclinical spheroid models identify BMX as a therapeutic target
            for metastatic MYCN nonamplified neuroblastoma
  JOURNAL   JCI Insight 9 (14), e169647 (2024)
   PUBMED   39133652
  REMARK    GeneRIF: Preclinical spheroid models identify BMX as a therapeutic
            target for metastatic MYCN nonamplified neuroblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Murray,J.E., Valli,E., Milazzo,G., Mayoh,C., Gifford,A.J.,
            Fletcher,J.I., Xue,C., Jayatilleke,N., Salehzadeh,F., Gamble,L.D.,
            Rouaen,J.R.C., Carter,D.R., Forgham,H., Sekyere,E.O., Keating,J.,
            Eden,G., Allan,S., Alfred,S., Kusuma,F.K., Clark,A., Webber,H.,
            Russell,A.J., de Weck,A., Kile,B.T., Santulli,M., De Rosa,P.,
            Fleuren,E.D.G., Gao,W., Wilkinson-White,L., Low,J.K.K.,
            Mackay,J.P., Marshall,G.M., Hilton,D.J., Giorgi,F.M., Koster,J.,
            Perini,G., Haber,M. and Norris,M.D.
  TITLE     The transcriptional co-repressor Runx1t1 is essential for
            MYCN-driven neuroblastoma tumorigenesis
  JOURNAL   Nat Commun 15 (1), 5585 (2024)
   PUBMED   38992040
  REMARK    GeneRIF: The transcriptional co-repressor Runx1t1 is essential for
            MYCN-driven neuroblastoma tumorigenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Besancon,R., Valsesia-Wittmann,S., Locher,C., Delloye-Bourgeois,C.,
            Furhman,L., Tutrone,G., Bertrand,C., Jallas,A.C., Garin,E. and
            Puisieux,A.
  TITLE     Upstream ORF affects MYCN translation depending on exon 1b
            alternative splicing
  JOURNAL   BMC Cancer 9, 445 (2009)
   PUBMED   20017904
  REMARK    GeneRIF: Existence of upstream ORF in MYCN transcripts leads to a
            new level of MYCN regulation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Marcelis,C.L.M. and de Brouwer,A.P.M.
  TITLE     Feingold Syndrome 1
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301770
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Scott,D.A.
  TITLE     Esophageal Atresia / Tracheoesophageal Fistula Overview - RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301753
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Hagiwara,T., Nakaya,K., Nakamura,Y., Nakajima,H., Nishimura,S. and
            Taya,Y.
  TITLE     Specific phosphorylation of the acidic central region of the N-myc
            protein by casein kinase II
  JOURNAL   Eur J Biochem 209 (3), 945-950 (1992)
   PUBMED   1425701
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Armstrong,B.C. and Krystal,G.W.
  TITLE     Isolation and characterization of complementary DNA for N-cym, a
            gene encoded by the DNA strand opposite to N-myc
  JOURNAL   Cell Growth Differ 3 (6), 385-390 (1992)
   PUBMED   1419902
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Fougerousse,F., Meloni,R., Roudaut,C. and Beckmann,J.S.
  TITLE     Dinucleotide repeat polymorphism at the human hemoglobin alpha-1
            pseudo-gene (HBAP1)
  JOURNAL   Nucleic Acids Res 20 (5), 1165 (1992)
   PUBMED   1549498
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Stanton,L.W. and Bishop,J.M.
  TITLE     Alternative processing of RNA transcribed from NMYC
  JOURNAL   Mol Cell Biol 7 (12), 4266-4272 (1987)
   PUBMED   3437890
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010145.10 and BC002712.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_005369.1.
            
            Summary: This gene is a member of the MYC family and encodes a
            protein with a basic helix-loop-helix (bHLH) domain. This protein
            is located in the nucleus and must dimerize with another bHLH
            protein in order to bind DNA. Amplification of this gene is
            associated with a variety of tumors, most notably neuroblastomas.
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jun 2014].
            
            Transcript Variant: This variant (2) lacks segment 1b in the 5'
            region, compared to variant 1. This variant includes two open
            reading frames; the isoform 1 represented by this RefSeq is
            translated from the downstream open reading frame. This transcript
            and variant 1 encode the same isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC002712.2, BT007384.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281043.4/ ENSP00000281043.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.3"
     Protein         1..464
                     /product="N-myc proto-oncogene protein isoform 1"
                     /note="neuroblastoma MYC oncogene; N-myc proto-oncogene
                     protein; oncogene NMYC; neuroblastoma-derived v-myc avian
                     myelocytomatosis viral related oncogene; class E basic
                     helix-loop-helix protein 37; v-myc avian myelocytomatosis
                     viral oncogene neuroblastoma derived homolog"
                     /calculated_mol_wt=49430
     Region          10..372
                     /region_name="Myc_N"
                     /note="Myc amino-terminal region; pfam01056"
                     /db_xref="CDD:460045"
     Region          19..47
                     /region_name="Interaction with AURKA.
                     /evidence=ECO:0000269|PubMed:27837025"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:30573562; propagated from
                     UniProtKB/Swiss-Prot (P04198.2)"
     Region          61..89
                     /region_name="Interaction with AURKA and FBXW7.
                     /evidence=ECO:0000269|PubMed:27837025"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          76..84
                     /region_name="9aaTAD.
                     /evidence=ECO:0000269|PubMed:34342803"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          129..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          196..294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:1425701; propagated from
                     UniProtKB/Swiss-Prot (P04198.2)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:1425701; propagated from
                     UniProtKB/Swiss-Prot (P04198.2)"
     Region          334..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          378..464
                     /region_name="bHLHzip_N-Myc_like"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in N-Myc and similar proteins; cd11456"
                     /db_xref="CDD:381462"
     Site            order(378,382..383,386..387,389..391,393..394,398,
                     418..419)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381462"
     Site            order(397,400..401,403..404,407,420,423..424,427,429..431,
                     433..434,436..437,440,443..444,447..448,450..452,454..455,
                     457..464)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381462"
     Site            order(397,400..401,403..404,407,420,423..424,427,429..431,
                     433..434,436..437,440,443..444,447..448,450..451,454,
                     457..458,461..462,464)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381462"
     Region          433..454
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     CDS             1..464
                     /gene="MYCN"
                     /gene_synonym="bHLHe37; FGLDS1; MODED; MPAPA; MYCNsORF;
                     MYCNsPEP; N-myc; NMYC; ODED"
                     /coded_by="NM_005378.6:312..1706"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1687.1"
                     /db_xref="GeneID:4613"
                     /db_xref="HGNC:HGNC:7559"
                     /db_xref="MIM:164840"
ORIGIN      
        1 mpscststmp gmicknpdle fdslqpcfyp deddfyfggp dstppgediw kkfellptpp
       61 lspsrgfaeh sseppswvte mllenelwgs paeedafglg glggltpnpv ilqdcmwsgf
      121 sareklerav seklqhgrgp ptagstaqsp gagaaspagr ghggaagagr agaalpaela
      181 hpaaecvdpa vvfpfpvnkr epapvpaapa sapaagpava sgagiaapag apgvapprpg
      241 grqtsggdhk alstsgedtl sdsddeddee edeeeeidvv tvekrrsssn tkavttftit
      301 vrpknaalgp graqsselil krclpihqqh nyaapspyve sedappqkki kseasprplk
      361 svippkaksl sprnsdseds errrnhnile rqrrndlrss fltlrdhvpe lvknekaakv
      421 vilkkateyv hslqaeehql llekeklqar qqqllkkieh artc
//
LOCUS       NP_115536               1212 aa            linear   PRI 27-APR-2025
DEFINITION  dermatan-sulfate epimerase-like protein precursor [Homo sapiens].
ACCESSION   NP_115536
VERSION     NP_115536.2
DBSOURCE    REFSEQ: accession NM_032160.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1212)
  AUTHORS   Sung,Y.J., de las Fuentes,L., Schwander,K.L., Simino,J. and
            Rao,D.C.
  TITLE     Gene-smoking interactions identify several novel blood pressure
            loci in the Framingham Heart Study
  JOURNAL   Am J Hypertens 28 (3), 343-354 (2015)
   PUBMED   25189868
REFERENCE   2  (residues 1 to 1212)
  AUTHORS   Shi,J., Potash,J.B., Knowles,J.A., Weissman,M.M., Coryell,W.,
            Scheftner,W.A., Lawson,W.B., DePaulo,J.R. Jr., Gejman,P.V.,
            Sanders,A.R., Johnson,J.K., Adams,P., Chaudhury,S., Jancic,D.,
            Evgrafov,O., Zvinyatskovskiy,A., Ertman,N., Gladis,M., Neimanas,K.,
            Goodell,M., Hale,N., Ney,N., Verma,R., Mirel,D., Holmans,P. and
            Levinson,D.F.
  TITLE     Genome-wide association study of recurrent early-onset major
            depressive disorder
  JOURNAL   Mol Psychiatry 16 (2), 193-201 (2011)
   PUBMED   20125088
REFERENCE   3  (residues 1 to 1212)
  AUTHORS   Zayed,H., Chao,R., Moshrefi,A., Lopezjimenez,N., Delaney,A.,
            Chen,J., Shaw,G.M. and Slavotinek,A.M.
  TITLE     A maternally inherited chromosome 18q22.1 deletion in a male with
            late-presenting diaphragmatic hernia and microphthalmia-evaluation
            of DSEL as a candidate gene for the diaphragmatic defect
  JOURNAL   Am J Med Genet A 152A (4), 916-923 (2010)
   PUBMED   20358601
  REMARK    GeneRIF: DSEL was selected for study in 125 patients with
            diaphragmatic hernias, as it is involved in the synthesis of
            decorin, a protein that is required for normal collagen formation
            and that is upregulated during myogenesis.
REFERENCE   4  (residues 1 to 1212)
  AUTHORS   Need,A.C., Attix,D.K., McEvoy,J.M., Cirulli,E.T., Linney,K.L.,
            Hunt,P., Ge,D., Heinzen,E.L., Maia,J.M., Shianna,K.V., Weale,M.E.,
            Cherkas,L.F., Clement,G., Spector,T.D., Gibson,G. and
            Goldstein,D.B.
  TITLE     A genome-wide study of common SNPs and CNVs in cognitive
            performance in the CANTAB
  JOURNAL   Hum Mol Genet 18 (23), 4650-4661 (2009)
   PUBMED   19734545
REFERENCE   5  (residues 1 to 1212)
  AUTHORS   Pacheco,B., Malmstrom,A. and Maccarana,M.
  TITLE     Two dermatan sulfate epimerases form iduronic acid domains in
            dermatan sulfate
  JOURNAL   J Biol Chem 284 (15), 9788-9795 (2009)
   PUBMED   19188366
REFERENCE   6  (residues 1 to 1212)
  AUTHORS   Maccarana,M., Olander,B., Malmstrom,J., Tiedemann,K., Aebersold,R.,
            Lindahl,U., Li,J.P. and Malmstrom,A.
  TITLE     Biosynthesis of dermatan sulfate: chondroitin-glucuronate
            C5-epimerase is identical to SART2
  JOURNAL   J Biol Chem 281 (17), 11560-11568 (2006)
   PUBMED   16505484
REFERENCE   7  (residues 1 to 1212)
  AUTHORS   Goossens,D., Van Gestel,S., Claes,S., De Rijk,P., Souery,D.,
            Massat,I., Van den Bossche,D., Backhovens,H., Mendlewicz,J., Van
            Broeckhoven,C. and Del-Favero,J.
  TITLE     A novel CpG-associated brain-expressed candidate gene for
            chromosome 18q-linked bipolar disorder
  JOURNAL   Mol Psychiatry 8 (1), 83-89 (2003)
   PUBMED   12556911
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AV656576.1 and AC110597.7.
            
            On Nov 16, 2018 this sequence version replaced NP_115536.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.252380.1,
                                           SRR1803617.93174.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467143, SAMEA2467144
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000310045.9/
                                                ENSP00000310565.8
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1212
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q22.1"
     Protein         1..1212
                     /product="dermatan-sulfate epimerase-like protein
                     precursor"
                     /EC_number="5.1.3.19"
                     /note="NCAG1; dermatan-sulfate epimerase-like protein"
                     /calculated_mol_wt=136981
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2275
     mat_peptide     21..1212
                     /product="Dermatan-sulfate epimerase-like protein.
                     /id=PRO_0000278288"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZU8.2)"
                     /calculated_mol_wt=136981
     Site            28
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZU8.2)"
     Site            666
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZU8.2)"
     Site            688
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZU8.2)"
     Site            709
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZU8.2)"
     Site            764..784
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZU8.2)"
     Site            803..823
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZU8.2)"
     Site            874
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZU8.2)"
     CDS             1..1212
                     /gene="DSEL"
                     /gene_synonym="C18orf4; DE-epi2"
                     /coded_by="NM_032160.3:1245..4883"
                     /db_xref="CCDS:CCDS11995.2"
                     /db_xref="GeneID:92126"
                     /db_xref="HGNC:HGNC:18144"
                     /db_xref="MIM:611125"
ORIGIN      
        1 malmftghll flallmfafs tfeesvsnys ewavftddid qfktqkvqdf rpnqklkksm
       61 lhpslyfdag eiqamrqksr ashlhlfrai rsavtvmlsn ptyylpppkh adfaakwnei
      121 ygnnlpplal ycllcpedkv afefvleymd rmvgykdwlv enapgdevpi ghsltgfata
      181 fdflynlldn hrrqkyleki wviteemyey skvrswgkql lhnhqatnmi alltgalvtg
      241 vdkgskaniw kqavvdvmek tmfllnhivd gsldegvayg sytaksvtqy vflaqrhfni
      301 nnldnnwlkm hfwfyyatll pgfqrtvgia dsnynwfygp esqlvfldkf ilkngagnwl
      361 aqqirkhrpk dgpmvpstaq rwstlhteyi wydpqltpqp padygtakih tfpnwgvvty
      421 gaglpntqtn tfvsfksgkl ggravydivh fqpyswidgw rsfnpghehp dqnsftfapn
      481 gqvfvsealy gpklshlnnv lvfapspssq cnkpwegqlg ecaqwlkwtg eevgdaagei
      541 itasqhgemv fvsgeavsay ssamrlksvy rallllnsqt llvvdhierq edspinsvsa
      601 ffhnldidfk yipykfmnry ngammdvwda hykmfwfdhh gnspmasiqe aeqaaefkkr
      661 wtqfvnvtfq meptitriay vfygpyinvs scrfidssnp glqislnvnn tehvvsivtd
      721 yhnlktrfny lgfggfasva dqgqitrfgl gtqaivkpvr hdriifpfgf kfniavglil
      781 cislviltfq wrfylsfrkl mrwililvia lwfielldvw stcsqpicak wtrteaegsk
      841 kslsseghhm dlpdvvitsl pgsgaeilkq lffnssdfly irvptayidi peteleidsf
      901 vdacewkvsd irsghfrllr gwlqslvqdt klhlqnihlh epnrgklaqy famnkdkkrk
      961 fkrreslpeq rsqmkgafdr daeyiralrr hlvyypsarp vlslssgswt lklhffqevl
     1021 gasmralyiv rdprawiysm lynskpslys lknvpehlak lfkieggkgk cnlnsgyafe
     1081 yeplrkelsk sksnavslls hlwlantaaa lrintdllpt syqlvkfedi vhfpqktter
     1141 ifaflgipls paslnqilfa tstnlfylpy egeisptntn vwkqnlprde iklienicwt
     1201 lmdrlgypkf md
//
LOCUS       NP_000763                490 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome P450 2C18 isoform 1 [Homo sapiens].
ACCESSION   NP_000763
VERSION     NP_000763.1
DBSOURCE    REFSEQ: accession NM_000772.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Braten,L.S., Haslemo,T., Jukic,M.M., Ivanov,M.,
            Ingelman-Sundberg,M., Molden,E. and Kringen,M.K.
  TITLE     A Novel CYP2C-Haplotype Associated With Ultrarapid Metabolism of
            Escitalopram
  JOURNAL   Clin Pharmacol Ther 110 (3), 786-793 (2021)
   PUBMED   33759177
  REMARK    GeneRIF: A Novel CYP2C-Haplotype Associated With Ultrarapid
            Metabolism of Escitalopram.
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Perera,M.A., Cavallari,L.H., Limdi,N.A., Gamazon,E.R.,
            Konkashbaev,A., Daneshjou,R., Pluzhnikov,A., Crawford,D.C.,
            Wang,J., Liu,N., Tatonetti,N., Bourgeois,S., Takahashi,H.,
            Bradford,Y., Burkley,B.M., Desnick,R.J., Halperin,J.L.,
            Khalifa,S.I., Langaee,T.Y., Lubitz,S.A., Nutescu,E.A., Oetjens,M.,
            Shahin,M.H., Patel,S.R., Sagreiya,H., Tector,M., Weck,K.E.,
            Rieder,M.J., Scott,S.A., Wu,A.H., Burmester,J.K., Wadelius,M.,
            Deloukas,P., Wagner,M.J., Mushiroda,T., Kubo,M., Roden,D.M.,
            Cox,N.J., Altman,R.B., Klein,T.E., Nakamura,Y. and Johnson,J.A.
  TITLE     Genetic variants associated with warfarin dose in African-American
            individuals: a genome-wide association study
  JOURNAL   Lancet 382 (9894), 790-796 (2013)
   PUBMED   23755828
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Flachsbart,F., Ufer,M., Kleindorp,R., Nikolaus,S., Schreiber,S. and
            Nebel,A.
  TITLE     Genetic variation in the CYP2C monooxygenase enzyme subfamily shows
            no association with longevity in a German population
  JOURNAL   J Gerontol A Biol Sci Med Sci 66 (11), 1186-1191 (2011)
   PUBMED   21798861
  REMARK    GeneRIF: These results suggest that there is no notable influence
            of sequence variation in the CYP2C genes on longevity in the
            examined German population
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Howard,T.D., Hsu,F.C., Grzywacz,J.G., Chen,H., Quandt,S.A.,
            Vallejos,Q.M., Whalley,L.E., Cui,W., Padilla,S. and Arcury,T.A.
  TITLE     Evaluation of candidate genes for cholinesterase activity in
            farmworkers exposed to organophosphorus pesticides: association of
            single nucleotide polymorphisms in BCHE
  JOURNAL   Environ Health Perspect 118 (10), 1395-1399 (2010)
   PUBMED   20529763
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Liu,C.Y., Wu,M.C., Chen,F., Ter-Minassian,M., Asomaning,K.,
            Zhai,R., Wang,Z., Su,L., Heist,R.S., Kulke,M.H., Lin,X., Liu,G. and
            Christiani,D.C.
  TITLE     A Large-scale genetic association study of esophageal
            adenocarcinoma risk
  JOURNAL   Carcinogenesis 31 (7), 1259-1263 (2010)
   PUBMED   20453000
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Goldstein,J.A. and de Morais,S.M.
  TITLE     Biochemistry and molecular biology of the human CYP2C subfamily
  JOURNAL   Pharmacogenetics 4 (6), 285-299 (1994)
   PUBMED   7704034
  REMARK    Review article
REFERENCE   8  (residues 1 to 490)
  AUTHORS   Ged,C. and Beaune,P.
  TITLE     Partial sequence and polymerase chain reaction-mediated analysis of
            expression of the human CYP2C18 gene
  JOURNAL   Pharmacogenetics 2 (3), 109-115 (1992)
   PUBMED   1306110
REFERENCE   9  (residues 1 to 490)
  AUTHORS   Furuya,H., Meyer,U.A., Gelboin,H.V. and Gonzalez,F.J.
  TITLE     Polymerase chain reaction-directed identification, cloning, and
            quantification of human CYP2C18 mRNA
  JOURNAL   Mol Pharmacol 40 (3), 375-382 (1991)
   PUBMED   1896026
REFERENCE   10 (residues 1 to 490)
  AUTHORS   Romkes,M., Faletto,M.B., Blaisdell,J.A., Raucy,J.L. and
            Goldstein,J.A.
  TITLE     Cloning and expression of complementary DNAs for multiple members
            of the human cytochrome P450IIC subfamily
  JOURNAL   Biochemistry 30 (13), 3247-3255 (1991)
   PUBMED   2009263
  REMARK    Erratum:[Biochemistry. 1993 Feb 9;32(5):1390. doi:
            10.1021/bi00056a025. PMID: 8095407]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M61856.1, BX538127.1 and
            M61853.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This protein localizes to the endoplasmic reticulum but its
            specific substrate has not yet been determined. The gene is located
            within a cluster of cytochrome P450 genes on chromosome 10q24. An
            additional gene, CYP2C17, was once thought to exist; however,
            CYP2C17 is now considered an artefact based on a chimera of CYP2C18
            and CYP2C19. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M61853.1, M61856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000285979.11/ ENSP00000285979.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.33"
     Protein         1..490
                     /product="cytochrome P450 2C18 isoform 1"
                     /EC_number="1.14.14.1"
                     /note="microsomal monooxygenase; flavoprotein-linked
                     monooxygenase; cytochrome P450, subfamily IIC (mephenytoin
                     4-hydroxylase), polypeptide 18; cytochrome P450, subfamily
                     IIC (mephenytoin 4-hydroxylase), polypeptide 17;
                     cytochrome P450 2C18; (S)-mephenytoin hydroxylase
                     associated cytochrome P450; unspecific monooxygenase;
                     CYPIIC18; cytochrome P450-6B/29C; cytochrome P450, family
                     2, subfamily C, polypeptide 18"
                     /calculated_mol_wt=55580
     Region          61..485
                     /region_name="CYP2C-like"
                     /note="cytochrome P450 family 2, subfamily C, and similar
                     cytochrome P450s; cd20665"
                     /db_xref="CDD:410758"
     Site            order(97,112..113,120,124,294,297..298,301..302,305,356,
                     361..362,365..366,368,427..429,433,435..437,441,444)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410758"
     Site            order(108,113..114,204..205,208,214,233,237,240,292..293,
                     296..297,300..301,362,366,476..477)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410758"
     CDS             1..490
                     /gene="CYP2C18"
                     /gene_synonym="CPCI; CYP2C; CYP2C17; P450-6B/29C;
                     P450IIC17"
                     /coded_by="NM_000772.3:92..1564"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7435.1"
                     /db_xref="GeneID:1562"
                     /db_xref="HGNC:HGNC:2620"
                     /db_xref="MIM:601131"
ORIGIN      
        1 mdpavalvlc lsclfllslw rqssgrgrlp sgptplpiig nilqldvkdm sksltnfskv
       61 ygpvftvyfg lkpivvlhgy eavkealidh geefsgrgsf pvaekvnkgl gilfsngkrw
      121 keirrfclmt lrnfgmgkrs iedrvqeear clveelrktn aspcdptfil gcapcnvics
      181 vifhdrfdyk dqrflnlmek fnenlrilss pwiqvcnnfp alidylpgsh nkiaenfayi
      241 ksyvlerike hqesldmnsa rdfidcflik meqekhnqqs eftvesliat vtdmfgagte
      301 ttsttlrygl llllkypevt akvqeeiecv vgrnrspcmq drshmpytda vvheiqryid
      361 llptnlphav tcdvkfknyl ipkgttiits ltsvlhndke fpnpemfdpg hfldksgnfk
      421 ksdyfmpfsa gkrmcmgegl armelflflt tilqnfnlks qvdpkdidit pianafgrvp
      481 plyqlcfipv
//
LOCUS       NP_073153               1944 aa            linear   PRI 27-APR-2025
DEFINITION  anaphase-promoting complex subunit 1 [Homo sapiens].
ACCESSION   NP_073153 XP_943596
VERSION     NP_073153.1
DBSOURCE    REFSEQ: accession NM_022662.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1944)
  AUTHORS   Mann,G., Sulkshane,P., Sadhu,P., Ziv,T., Glickman,M.H. and Brik,A.
  TITLE     Antibody for Serine 65 Phosphorylated Ubiquitin Identifies
            PLK1-Mediated Phosphorylation of Mitotic Proteins and APC1
  JOURNAL   Molecules 27 (15), 4867 (2022)
   PUBMED   35956818
  REMARK    GeneRIF: Antibody for Serine 65 Phosphorylated Ubiquitin Identifies
            PLK1-Mediated Phosphorylation of Mitotic Proteins and APC1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1944)
  AUTHORS   Liess,A.K.L., Kucerova,A., Schweimer,K., Schlesinger,D., Dybkov,O.,
            Urlaub,H., Mansfeld,J. and Lorenz,S.
  TITLE     Dimerization regulates the human APC/C-associated
            ubiquitin-conjugating enzyme UBE2S
  JOURNAL   Sci Signal 13 (654) (2020)
   PUBMED   33082289
  REMARK    GeneRIF: Dimerization regulates the human APC/C-associated
            ubiquitin-conjugating enzyme UBE2S.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1944)
  AUTHORS   Ajeawung,N.F., Nguyen,T.T.M., Lu,L., Kucharski,T.J., Rousseau,J.,
            Molidperee,S., Atienza,J., Gamache,I., Jin,W., Plon,S.E., Lee,B.H.,
            Teodoro,J.G., Wang,L.L. and Campeau,P.M.
  TITLE     Mutations in ANAPC1, Encoding a Scaffold Subunit of the
            Anaphase-Promoting Complex, Cause Rothmund-Thomson Syndrome Type 1
  JOURNAL   Am J Hum Genet 105 (3), 625-630 (2019)
   PUBMED   31303264
  REMARK    GeneRIF: Fibroblast studies showed that the intronic mutation
            causes the activation of a 95 bp pseudoexon, leading to mRNAs with
            premature termination codons and nonsense-mediated decay, decreased
            ANAPC1 protein levels, and prolongation of interphase
REFERENCE   4  (residues 1 to 1944)
  AUTHORS   Ivarsdottir,E.V., Benonisdottir,S., Thorleifsson,G., Sulem,P.,
            Oddsson,A., Styrkarsdottir,U., Kristmundsdottir,S.,
            Arnadottir,G.A., Thorgeirsson,G., Jonsdottir,I., Zoega,G.M.,
            Thorsteinsdottir,U., Gudbjartsson,D.F., Jonasson,F., Holm,H. and
            Stefansson,K.
  TITLE     Sequence variation at ANAPC1 accounts for 24% of the variability in
            corneal endothelial cell density
  JOURNAL   Nat Commun 10 (1), 1284 (2019)
   PUBMED   30894546
  REMARK    GeneRIF: Sequence variation at ANAPC1 accounts for 24% of the
            variability in corneal endothelial cell density.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1944)
  AUTHORS   Watson,E.R., Brown,N.G., Peters,J.M., Stark,H. and Schulman,B.A.
  TITLE     Posing the APC/C E3 Ubiquitin Ligase to Orchestrate Cell Division
  JOURNAL   Trends Cell Biol 29 (2), 117-134 (2019)
   PUBMED   30482618
  REMARK    GeneRIF: The anaphase promoting complex/cyclosome (APC/C) E3 ligase
            is not simply an interaction hub, but a dynamic, multifunctional
            molecular machine whose structure is remodeled by binding partners
            to achieve temporal ubiquitylation regulating cell division
            [Review].
            Review article
REFERENCE   6  (residues 1 to 1944)
  AUTHORS   Kramer,E.R., Scheuringer,N., Podtelejnikov,A.V., Mann,M. and
            Peters,J.M.
  TITLE     Mitotic regulation of the APC activator proteins CDC20 and CDH1
  JOURNAL   Mol Biol Cell 11 (5), 1555-1569 (2000)
   PUBMED   10793135
REFERENCE   7  (residues 1 to 1944)
  AUTHORS   Lukas,C., Sorensen,C.S., Kramer,E., Santoni-Rugiu,E., Lindeneg,C.,
            Peters,J.M., Bartek,J. and Lukas,J.
  TITLE     Accumulation of cyclin B1 requires E2F and cyclin-A-dependent
            rearrangement of the anaphase-promoting complex
  JOURNAL   Nature 401 (6755), 815-818 (1999)
   PUBMED   10548110
REFERENCE   8  (residues 1 to 1944)
  AUTHORS   Gieffers,C., Peters,B.H., Kramer,E.R., Dotti,C.G. and Peters,J.M.
  TITLE     Expression of the CDH1-associated form of the anaphase-promoting
            complex in postmitotic neurons
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11317-11322 (1999)
   PUBMED   10500174
REFERENCE   9  (residues 1 to 1944)
  AUTHORS   Grossberger,R., Gieffers,C., Zachariae,W., Podtelejnikov,A.V.,
            Schleiffer,A., Nasmyth,K., Mann,M. and Peters,J.M.
  TITLE     Characterization of the DOC1/APC10 subunit of the yeast and the
            human anaphase-promoting complex
  JOURNAL   J Biol Chem 274 (20), 14500-14507 (1999)
   PUBMED   10318877
REFERENCE   10 (residues 1 to 1944)
  AUTHORS   Wang,L.L. and Plon,S.E.
  TITLE     Rothmund-Thomson Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301415
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104651.2 and AC093166.6.
            
            On Mar 4, 2006 this sequence version replaced XP_943596.1.
            
            Summary: This gene encodes a subunit of the anaphase-promoting
            complex. This complex is an E3 ubiquitin ligase that regulates
            progression through the metaphase to anaphase portion of the cell
            cycle by ubiquitinating proteins which targets them for
            degradation. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1049856.1,
                                           SRR14038193.2038024.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341068.8/ ENSP00000339109.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1944
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..1944
                     /product="anaphase-promoting complex subunit 1"
                     /note="anaphase-promoting complex 1 (meiotic checkpoint
                     regulator); cyclosome subunit 1; mitotic checkpoint
                     regulator; testis-specific gene 24 protein"
                     /calculated_mol_wt=216370
     Region          1..136
                     /region_name="Apc1_N"
                     /note="Anaphase-promoting complex subunit 1 N-terminal;
                     pfam19521"
                     /db_xref="CDD:437353"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Region          151..359
                     /region_name="ANAPC1"
                     /note="Anaphase-promoting complex subunit 1 WD40
                     beta-propeller domain; pfam12859"
                     /db_xref="CDD:463732"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Region          305..343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Region          373..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Region          615..985
                     /region_name="Apc1_MidN"
                     /note="Anaphase-promoting complex subunit 1 middle domain;
                     pfam20518"
                     /db_xref="CDD:466667"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Site            916
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Region          994..1016
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Region          1297..1325
                     /region_name="PC 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Region          1366..1404
                     /region_name="PC 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Region          1467..1501
                     /region_name="PC 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Region          1467..1501
                     /region_name="PC_rep"
                     /note="Proteasome/cyclosome repeat; pfam01851"
                     /db_xref="CDD:460361"
     Region          1520..1552
                     /region_name="PC 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1A4.1)"
     Region          1739..1895
                     /region_name="APC1_C"
                     /note="Anaphase-promoting complex sub unit 1 C-terminal
                     domain; pfam18122"
                     /db_xref="CDD:465659"
     CDS             1..1944
                     /gene="ANAPC1"
                     /gene_synonym="APC1; MCPR; TSG24"
                     /coded_by="NM_022662.4:277..6111"
                     /db_xref="CCDS:CCDS2093.1"
                     /db_xref="GeneID:64682"
                     /db_xref="HGNC:HGNC:19988"
                     /db_xref="MIM:608473"
ORIGIN      
        1 msnfyeertt miaardlqef vpfgrdhckh hpnalnlqlr qlqpaselws sdgaaglvgs
       61 lqevtihekq keswqlrkgv seigedvdyd eelyvagnmv iwskgsksqa lavykaftvd
      121 spvqqalwcd fiisqdksek ayssnevekc icilqsscin mhsiegkdyi aslpfqvanv
      181 wptkygllfe rsasshevpp gspreplptm fsmlhpldei tplvcksgsl fgssrvqyvv
      241 dhamkivfln tdpsivmtyd avqnvhsvwt lrrvkseeen vvlkfseqgg tpqnvatsss
      301 ltahlrslsk gdspvtspfq nyssihsqsr stsspslhsr spsisnmaal srahspalgv
      361 hsfsgvqrfn isshnqspkr hsishspnsn sngsflapet epivpelcid hlwtetitni
      421 reknsqaskv fitsdlcgqk flcflvesql qlrcvkfqes ndktqlifgs vtnipakdaa
      481 pvekidtmlv legsgnlvly tgvvrvgkvf ipglpapslt msntmprpst pldgvstpkp
      541 lskllgslde vvllspvpel rdssklhdsl ynedctfqql gtyihsirdp vhnrvtlels
      601 ngsmvritip eiatselvqt clqaikfilp keiavqmlvk wynvhsapgg psyhsewnlf
      661 vtclmnmmgy ntdrlawtrn fdfegslspv iapkkarpse tgsdddweyl lnsdyhqnve
      721 shllnrslcl spseasqmkd edfsqnlsld sstllfthip aiffvlhlvy eelklntlmg
      781 egicslvell vqlardlklg pyvdhyyrdy ptlvrttgqv ctidpgqtgf mhhpsfftse
      841 ppsiyqwvss clkgegmppy pylpgicers rlvvlsialy ilgdeslvsd essqyltrit
      901 iapqklqveq eenrfsfrhs tsvsslaerl vvwmtnvgft lrdletlpfg ialpirdaiy
      961 hcreqpasdw peavclligr qdlskqaceg nlpkgksvls sdvpsgtete eeddgmndmn
     1021 hevmsliwse dlrvqdvrrl lqsahpvrvn vvqypelsdh efieekenrl lqlcqrtmal
     1081 pvgrgmftlf syhpvptepl pipklnltgr apprnttvdl nsgnidvppn mtswasfhng
     1141 vaaglkiapa sqidsawivy nkpkhaelan eyagflmalg lnghltklat lnihdyltkg
     1201 hemtsiglll gvsaaklgtm dmsitrllsi hipallppts teldvphnvq vaavvgiglv
     1261 yqgtahrhta evllaeigrp pgpemeyctd resyslaagl algmvclghg snligmsdln
     1321 vpeqlyqymv gghrrfqtgm hrekhkspsy qikegdtinv dvtcpgatla lamiylktnn
     1381 rsiadwlrap dtmylldfvk peflllrtla rclilwddil pnskwvdsnv pqiirensis
     1441 lseielpcse dlnletlsqa hvyiiagacl slgfrfagse nlsafnclhk fakdfmtyls
     1501 apnasvtgph nletclsvvl lslamvmags gnlkvlqlcr flhmktggem nygfhlahhm
     1561 algllflggg ryslstsnss iaallcalyp hfpahstdnr yhlqalrhly vlaaeprllv
     1621 pvdvdtntpc yallevtykg tqwyeqtkee lmaptllpel hllkqikvkg prywellidl
     1681 skgtqhlksi lskdgvlyvk lragqlsyke dpmgwqslla qtvanrnsea rafkpetisa
     1741 ftsdpallsf aeyfckptvn mgqkqeildl fssvlyecvt qetpemlpay iamdqairrl
     1801 grremsetse lwqiklvlef fssrshqerl qnhpkrglfm nseflpvvkc tidntldqwl
     1861 qvggdmcvha ylsgqplees qlsmlacflv yhsvpapqhl ppiglegsts faellfkfkq
     1921 lkmpvrallr laplllgnpq pmvm
//
LOCUS       NP_060807                327 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 444 isoform 1 [Homo sapiens].
ACCESSION   NP_060807
VERSION     NP_060807.2
DBSOURCE    REFSEQ: accession NM_018337.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Brandal,P., Panagopoulos,I., Bjerkehagen,B. and Heim,S.
  TITLE     t(19;22)(q13;q12) Translocation leading to the novel fusion gene
            EWSR1-ZNF444 in soft tissue myoepithelial carcinoma
  JOURNAL   Genes Chromosomes Cancer 48 (12), 1051-1056 (2009)
   PUBMED   19760602
  REMARK    GeneRIF: t(19;22)(q13;q12) Translocation leading to the novel
            fusion gene EWSR1-ZNF444 is associated with soft tissue
            myoepithelial carcinoma.
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Adachi,H. and Tsujimoto,M.
  TITLE     Characterization of the human gene encoding the scavenger receptor
            expressed by endothelial cell and its regulation by a novel
            transcription factor, endothelial zinc finger protein-2
  JOURNAL   J Biol Chem 277 (27), 24014-24021 (2002)
   PUBMED   11978792
  REMARK    GeneRIF: regulates the human gene encoding the scavenger receptor
            expressed by endothelial cells
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI823582.1 and AL834130.1.
            
            On Oct 7, 2003 this sequence version replaced NP_060807.1.
            
            Summary: This gene encodes a zinc finger protein which activates
            transcription of a scavenger receptor gene involved in the
            degradation of acetylated low density lipoprotein (Ac-LDL) (PMID:
            11978792). This gene is located in a cluster of zinc finger genes
            on chromosome 19 at q13.4. A pseudogene of this gene is located on
            chromosome 15. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Dec
            2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL834130.1, SRR3476690.46629.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337080.8/ ENSP00000338860.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..327
                     /product="zinc finger protein 444 isoform 1"
                     /note="endothelial zinc finger protein 2; zinc finger and
                     SCAN domain-containing protein 17"
                     /calculated_mol_wt=35073
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N0Y2.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N0Y2.1)"
     Region          21..98
                     /region_name="SCAN"
                     /note="SCAN domain; pfam02023"
                     /db_xref="CDD:460417"
     Region          101..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N0Y2.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N0Y2.1)"
     Region          <126..>226
                     /region_name="KREPA"
                     /note="Kinetoplastid RNA Editing Protein A (KREPA);
                     cl49620"
                     /db_xref="CDD:483960"
     Region          <179..>280
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          181..201
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(186,188,190,192..193,196..197,200,214,216,220..221,
                     224..225,228,257,259,261,263..264,267..268,271)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          209..229
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          220..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N0Y2.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N0Y2.1)"
     Region          252..272
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          278..300
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          280..300
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          305..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N0Y2.1)"
     CDS             1..327
                     /gene="ZNF444"
                     /gene_synonym="EZF-2; EZF2; ZSCAN17"
                     /coded_by="NM_018337.4:268..1251"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12939.1"
                     /db_xref="GeneID:55311"
                     /db_xref="HGNC:HGNC:16052"
                     /db_xref="MIM:607874"
ORIGIN      
        1 mevavpvkqe aeglaldspw hrfrrfhlgd apgprealgl lralcrdwlr pevhtkeqml
       61 ellvleqfls alpadtqawv csrqpqsgee avalleelwg paaspdgssa trvpqdvtqg
      121 pgatggkeds gmiplagtap gaegpapgds qavrpykqep sspplapglp aflaapgtts
      181 cpecgktslk pahllrhrqs hsgekphacp ecgkafrrke hlrrhrdthp gspgspgpal
      241 rplparekph accecgktfy wrehlvrhrk thsgarpfac wecgkgfgrr ehvlrhqrih
      301 graaasaqga vapgpdgggp fppwplg
//
LOCUS       NP_001186132            1321 aa            linear   ROD 27-APR-2025
DEFINITION  C-Jun-amino-terminal kinase-interacting protein 4 isoform 5 [Mus
            musculus].
ACCESSION   NP_001186132
VERSION     NP_001186132.1
DBSOURCE    REFSEQ: accession NM_001199203.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1321)
  AUTHORS   Tian,M., Zhang,L., Zhang,M., Qiao,L., Xu,B., Li,C., Liu,S.,
            Song,Y., Wei,Z., Wang,Y. and Wang,H.
  TITLE     JLP/Foxk1/N-cadherin axis fosters a partial epithelial-mesenchymal
            transition state in epithelial tubular cells
  JOURNAL   iScience 26 (4), 106396 (2023)
   PUBMED   37013185
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1321)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1321)
  AUTHORS   Mohan,R.A., Bosada,F.M., van Weerd,J.H., van Duijvenboden,K.,
            Wang,J., Mommersteeg,M.T.M., Hooijkaas,I.B., Wakker,V., de Gier-de
            Vries,C., Coronel,R., Boink,G.J.J., Bakkers,J., Barnett,P.,
            Boukens,B.J. and Christoffels,V.M.
  TITLE     T-box transcription factor 3 governs a transcriptional program for
            the function of the mouse atrioventricular conduction system
  JOURNAL   Proc Natl Acad Sci U S A 117 (31), 18617-18626 (2020)
   PUBMED   32675240
REFERENCE   4  (residues 1 to 1321)
  AUTHORS   Hanata,N., Shoda,H., Hatano,H., Nagafuchi,Y., Komai,T., Okamura,T.,
            Suzuki,A., Gunarta,I.K., Yoshioka,K., Yamamoto,K. and Fujio,K.
  TITLE     Peptidylarginine Deiminase 4 Promotes the Renal Infiltration of
            Neutrophils and Exacerbates the TLR7 Agonist-Induced Lupus Mice
  JOURNAL   Front Immunol 11, 1095 (2020)
   PUBMED   32655553
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1321)
  AUTHORS   Yan,Q., Zhu,K., Zhang,L., Fu,Q., Chen,Z., Liu,S., Fu,D.,
            Nakazato,R., Yoshioka,K., Diao,B., Ding,G., Li,X. and Wang,H.
  TITLE     A negative feedback loop between JNK-associated leucine zipper
            protein and TGF-beta1 regulates kidney fibrosis
  JOURNAL   Commun Biol 3 (1), 288 (2020)
   PUBMED   32504044
  REMARK    GeneRIF: A negative feedback loop between JNK-associated leucine
            zipper protein and TGF-beta1 regulates kidney fibrosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1321)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   7  (residues 1 to 1321)
  AUTHORS   Kelkar,N., Delmotte,M.H., Weston,C.R., Barrett,T., Sheppard,B.J.,
            Flavell,R.A. and Davis,R.J.
  TITLE     Morphogenesis of the telencephalic commissure requires scaffold
            protein JNK-interacting protein 3 (JIP3)
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 9843-9848 (2003)
   PUBMED   12897243
REFERENCE   8  (residues 1 to 1321)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 1321)
  AUTHORS   Lee,C.M., Onesime,D., Reddy,C.D., Dhanasekaran,N. and Reddy,E.P.
  TITLE     JLP: A scaffolding protein that tethers JNK/p38MAPK signaling
            modules and transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14189-14194 (2002)
   PUBMED   12391307
  REMARK    GeneRIF: describe a protein, JLP, which acts as a scaffolding
            protein to bring mitogen-activated protein kinases and their target
            transcription factors together for the execution of specific
            signaling pathways
REFERENCE   10 (residues 1 to 1321)
  AUTHORS   Bowman,A.B., Kamal,A., Ritchings,B.W., Philp,A.V., McGrail,M.,
            Gindhart,J.G. and Goldstein,L.S.
  TITLE     Kinesin-dependent axonal transport is mediated by the sunday driver
            (SYD) protein
  JOURNAL   Cell 103 (4), 583-594 (2000)
   PUBMED   11106729
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK161623.1, AB047782.1, AL662838.12, AK147431.1 and CO044222.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB047782.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1321
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 58.9 cM"
     Protein         1..1321
                     /product="C-Jun-amino-terminal kinase-interacting protein
                     4 isoform 5"
                     /note="JNK-interacting protein 4; C-jun-amino-terminal
                     kinase-interacting protein 4; JNK-interacting leucine
                     zipper; JNK/SAPK-associated protein 2; JNK-associated
                     leucine-zipper protein; mitogen-activated protein kinase
                     8-interacting protein 4"
                     /calculated_mol_wt=146105
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          24..178
                     /region_name="Jnk-SapK_ap_N"
                     /note="JNK_SAPK-associated protein-1; pfam09744"
                     /db_xref="CDD:462875"
     Region          <66..>549
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          203..308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          322..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          406..474
                     /region_name="JIP_LZII"
                     /note="JNK-interacting protein leucine zipper II;
                     pfam16471"
                     /db_xref="CDD:465127"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          473..500
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          563..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            586
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          853..883
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          954..>1172
                     /region_name="WD40_2"
                     /note="WD40 repeated domain; pfam19056"
                     /db_xref="CDD:465964"
     Site            1188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     Region          1239..1267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A65.2)"
     Site            1264
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60271; propagated from
                     UniProtKB/Swiss-Prot (Q58A65.2)"
     CDS             1..1321
                     /gene="Spag9"
                     /gene_synonym="3110018C07Rik; 4733401I23Rik;
                     4831406C20Rik; JIP-4; Jip4; JLP; JSAP2; JSAP2a; Mapk8ip4;
                     syd1"
                     /coded_by="NM_001199203.2:181..4146"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:70834"
                     /db_xref="MGI:MGI:1918084"
ORIGIN      
        1 meledgvvyq eepggsgavm servsglags iyreferlig rydeevvkel mplvvavlen
       61 ldsvfaqdqe hqvelellrd dneqlitqye rekalrkhae ekfiefedsq eqekkdlqtr
      121 veslesqtrq lelkaknyad qisrleerea elkkeynalh qrhtemihny mehlertklh
      181 qlsgsdqlea tahsrirker pislgifplp agdglltpdt qkggetpgse qwkfqelsqp
      241 rshtslkvsh speplkaveq edelsdisqg gskattpast ansdvsaipp dtpskedneg
      301 fvkgtdtsnk seiskhievq vaqetrnvst esgeneekse vqaiiestpe ldmdkdlsgy
      361 kgsstptkgi enkafdrnte slfeelssag sgligdvdeg adllgmgrev enlilentql
      421 letknalnvv kndliakvde ltcekdvlqg eleavkqakl kledknrele eelrkaraea
      481 edarqkakdd ddsdiptaqr krftrvemar vlmernqyke rlmelqeavr wtemirasre
      541 npamqekkrs siwqffsrlf ssssnatkkp eppvnlkyna ptshvtpsvk krsstlsqlp
      601 gdkskafdfl seeteaslas rreqkreqyr qvkahvqked grvqafgwsl pqkykqvang
      661 qgetkmknlp vpvylrplde kdasmklwca vgvnlsggkt rdggsvvgas vfykdiagld
      721 tegskqrsas qssldkldqe lkeqqkefkn qeelssqvwi ctsthsttkv iiidavqpgn
      781 ildsftvcns hvlciasvpg aretdypage elsesgqvdk aslcgsmtsn ssaemdsllg
      841 gitvvgcste gltgaatsps tngaspviek ppemetense vdeniptaee ateategnag
      901 stedtvdisq pgvytehvft dplgvqiped lspvfqssnd sdvykdqisv lpneqdlare
      961 eaqkmssllp tmwlgaqngc lyvhssvaqw rkclhsiklk dsilsivhvk givlvaladg
     1021 tlaifhrgvd gqwdlsnyhl ldlgrphhsi rcmtvvhdkv wcgyrnkiyv vqpkamkiek
     1081 sfdahprkes qvrqlawvgd gvwvsirlds tlrlyhahty qhlqdvdiep yvskmlgtgk
     1141 lgfsfvrita lmvscnrlwv gtgngviisi pltetnktsg tpgnrpgsvi rvygdensdk
     1201 vtpgtfipyc smahaqlcfh ghrdavkffv avpgqvispq sssggadlta dkagssaqep
     1261 ssqtplksml visggegyid frmgdegges ellgedlple psvtkaersh livwqvmcgn
     1321 e
//
LOCUS       NP_006861                165 aa            linear   PRI 27-APR-2025
DEFINITION  destrin isoform a [Homo sapiens].
ACCESSION   NP_006861
VERSION     NP_006861.1
DBSOURCE    REFSEQ: accession NM_006870.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Wen,R., Zhou,L., Jiang,S., Fan,H., Zheng,K., Yu,Y., Gao,X., Hao,L.,
            Lou,Z., Yu,G., Yang,F. and Zhang,W.
  TITLE     DSTN Hypomethylation Promotes Radiotherapy Resistance of Rectal
            Cancer by Activating the Wnt/beta-Catenin Signaling Pathway
  JOURNAL   Int J Radiat Oncol Biol Phys 117 (1), 198-210 (2023)
   PUBMED   37019366
  REMARK    GeneRIF: DSTN Hypomethylation Promotes Radiotherapy Resistance of
            Rectal Cancer by Activating the Wnt/beta-Catenin Signaling Pathway.
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Liao,K.A., Rangarajan,K.V., Bai,X., Taylor,J.M. and Mack,C.P.
  TITLE     The actin depolymerizing factor destrin serves as a negative
            feedback inhibitor of smooth muscle cell differentiation
  JOURNAL   Am J Physiol Heart Circ Physiol 321 (5), H893-H904 (2021)
   PUBMED   34559579
  REMARK    GeneRIF: The actin depolymerizing factor destrin serves as a
            negative feedback inhibitor of smooth muscle cell differentiation.
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Ullo,M.F. and Logue,J.S.
  TITLE     ADF and cofilin-1 collaborate to promote cortical actin flow and
            the leader bleb-based migration of confined cells
  JOURNAL   Elife 10, e67856 (2021)
   PUBMED   34169836
  REMARK    GeneRIF: ADF and cofilin-1 collaborate to promote cortical actin
            flow and the leader bleb-based migration of confined cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Toshima,J., Toshima,J.Y., Takeuchi,K., Mori,R. and Mizuno,K.
  TITLE     Cofilin phosphorylation and actin reorganization activities of
            testicular protein kinase 2 and its predominant expression in
            testicular Sertoli cells
  JOURNAL   J Biol Chem 276 (33), 31449-31458 (2001)
   PUBMED   11418599
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Hatanaka,H., Ogura,K., Moriyama,K., Ichikawa,S., Yahara,I. and
            Inagaki,F.
  TITLE     Tertiary structure of destrin and structural similarity between two
            actin-regulating protein families
  JOURNAL   Cell 85 (7), 1047-1055 (1996)
   PUBMED   8674111
REFERENCE   8  (residues 1 to 165)
  AUTHORS   Agnew,B.J., Minamide,L.S. and Bamburg,J.R.
  TITLE     Reactivation of phosphorylated actin depolymerizing factor and
            identification of the regulatory site
  JOURNAL   J Biol Chem 270 (29), 17582-17587 (1995)
   PUBMED   7615564
REFERENCE   9  (residues 1 to 165)
  AUTHORS   Hawkins,M., Pope,B., Maciver,S.K. and Weeds,A.G.
  TITLE     Human actin depolymerizing factor mediates a pH-sensitive
            destruction of actin filaments
  JOURNAL   Biochemistry 32 (38), 9985-9993 (1993)
   PUBMED   8399167
REFERENCE   10 (residues 1 to 165)
  AUTHORS   Moriyama,K., Nishida,E., Yonezawa,N., Sakai,H., Matsumoto,S.,
            Iida,K. and Yahara,I.
  TITLE     Destrin, a mammalian actin-depolymerizing protein, is closely
            related to cofilin. Cloning and expression of porcine brain destrin
            cDNA
  JOURNAL   J Biol Chem 265 (10), 5768-5773 (1990)
   PUBMED   2156828
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC009477.2, S65738.1,
            AI597935.1 and AL132765.38.
            
            Summary: The product of this gene belongs to the actin-binding
            proteins ADF family. This family of proteins is responsible for
            enhancing the turnover rate of actin in vivo. This gene encodes the
            actin depolymerizing protein that severs actin filaments (F-actin)
            and binds to actin monomers (G-actin). Two transcript variants
            encoding distinct isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript, but encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.145469.1,
                                           SRR1803615.81795.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000246069.12/ ENSP00000246069.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.1"
     Protein         1..165
                     /product="destrin isoform a"
                     /note="bA462D18.2 (destrin (actin depolymerizing factor
                     ADF) (ACTDP)); actin-depolymerizing factor; epididymis
                     luminal protein 32; epididymis secretory sperm binding
                     protein"
                     /calculated_mol_wt=18375
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P60981.3)"
     Region          3..152
                     /region_name="ADF_cofilin_like"
                     /note="Cofilin, Destrin, and related actin depolymerizing
                     factors; cd11286"
                     /db_xref="CDD:200442"
     Site            3..4
                     /site_type="other"
                     /note="putative G-actin interface [polypeptide binding]"
                     /db_xref="CDD:200442"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P60981.3)"
     Site            19
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P60981.3)"
     Region          30..34
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P60981.3)"
     Site            order(96,98,112,139,142)
                     /site_type="other"
                     /note="putative F-actin interface [polypeptide binding]"
                     /db_xref="CDD:200442"
     CDS             1..165
                     /gene="DSTN"
                     /gene_synonym="ACTDP; ADF; bA462D18.2; HEL32"
                     /coded_by="NM_006870.4:135..632"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13127.1"
                     /db_xref="GeneID:11034"
                     /db_xref="HGNC:HGNC:15750"
                     /db_xref="MIM:609114"
ORIGIN      
        1 masgvqvade vcrifydmkv rkcstpeeik krkkavifcl sadkkciive egkeilvgdv
       61 gvtitdpfkh fvgmlpekdc ryalydasfe tkesrkeelm fflwapelap lkskmiyass
      121 kdaikkkfqg ikhecqangp edlnraciae klggslivaf egcpv
//
LOCUS       NP_082174                722 aa            linear   ROD 27-APR-2025
DEFINITION  protein Aster-A isoform 2 [Mus musculus].
ACCESSION   NP_082174
VERSION     NP_082174.3
DBSOURCE    REFSEQ: accession NM_027898.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Ferrari,A., He,C., Kennelly,J.P., Sandhu,J., Xiao,X., Chi,X.,
            Jiang,H., Young,S.G. and Tontonoz,P.
  TITLE     Aster Proteins Regulate the Accessible Cholesterol Pool in the
            Plasma Membrane
  JOURNAL   Mol Cell Biol 40 (19), e00255-20 (2020)
   PUBMED   32719109
  REMARK    GeneRIF: Aster Proteins Regulate the Accessible Cholesterol Pool in
            the Plasma Membrane.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Nakano,Y., Wiechert,S. and Banfi,B.
  TITLE     Overlapping Activities of Two Neuronal Splicing Factors Switch the
            GABA Effect from Excitatory to Inhibitory by Regulating REST
  JOURNAL   Cell Rep 27 (3), 860-871 (2019)
   PUBMED   30995482
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Sandhu,J., Li,S., Fairall,L., Pfisterer,S.G., Gurnett,J.E.,
            Xiao,X., Weston,T.A., Vashi,D., Ferrari,A., Orozco,J.L.,
            Hartman,C.L., Strugatsky,D., Lee,S.D., He,C., Hong,C., Jiang,H.,
            Bentolila,L.A., Gatta,A.T., Levine,T.P., Ferng,A., Lee,R.,
            Ford,D.A., Young,S.G., Ikonen,E., Schwabe,J.W.R. and Tontonoz,P.
  TITLE     Aster Proteins Facilitate Nonvesicular Plasma Membrane to ER
            Cholesterol Transport in Mammalian Cells
  JOURNAL   Cell 175 (2), 514-529 (2018)
   PUBMED   30220461
REFERENCE   5  (residues 1 to 722)
  AUTHORS   Pan,J., Mor,G., Ju,W., Zhong,J., Luo,X., Aldo,P.B., Zhong,M.,
            Yu,Y., Jenkins,E.C., Brown,W.T. and Zhong,N.
  TITLE     Viral Infection-Induced Differential Expression of LncRNAs
            Associated with Collagen in Mouse Placentas and Amniotic Sacs
  JOURNAL   Am J Reprod Immunol 74 (3), 237-257 (2015)
   PUBMED   26073538
REFERENCE   6  (residues 1 to 722)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   7  (residues 1 to 722)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158993.2.
            
            On Dec 12, 2006 this sequence version replaced NP_082174.2.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK154821.1, AK150032.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 19.3 cM"
     Protein         1..722
                     /product="protein Aster-A isoform 2"
                     /note="GRAM domain-containing protein 1A; protein Aster-A"
                     /calculated_mol_wt=80568
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEF1.2)"
     Region          104..197
                     /region_name="PH-GRAM_GRAMDC"
                     /note="GRAM domain-containing protein (GRAMDC) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13220"
                     /db_xref="CDD:275406"
     Region          256..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEF1.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8VEF1.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8VEF1.2)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8VEF1.2)"
     Region          372..520
                     /region_name="VASt"
                     /note="VAD1 Analog of StAR-related lipid transfer domain;
                     pfam16016"
                     /db_xref="CDD:464975"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96CP6; propagated from
                     UniProtKB/Swiss-Prot (Q8VEF1.2)"
     Region          561..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEF1.2)"
     Site            609..629
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEF1.2)"
     CDS             1..722
                     /gene="Gramd1a"
                     /gene_synonym="1300003M23Rik; D7Bwg0611e"
                     /coded_by="NM_027898.4:269..2437"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS52189.1"
                     /db_xref="GeneID:52857"
                     /db_xref="MGI:MGI:105490"
ORIGIN      
        1 mfdttphsgr sspssspslr krlqllppir pppasepepg tmvekgsdss seksgvsgtl
       61 stqslgsrnf irnskkmqsw ysmlcptykq rnedfrklfs klpeaerliv dyscalqrei
      121 llqgrlylse nwicfysnif rwettisiql kevtclkkek taklipnaiq ictesekhff
      181 tsfgardrcf llifrlwqna llektlspre lwhlvhqcyg selgltsede dyvcplqlng
      241 lgspkevgdv ialsdispsg aadhsqepsp vgsrrgrvtp nlsrassdad hgaeedkeeq
      301 tdgldasssq tvtpvaepls septppdgpt sslgpldlls reelltdtsn sssstgeegd
      361 laallpdlsg rllinsvfhm gaerlqqmlf sdspflqgfl qqrkftdvtl spwssdskch
      421 qrrvltytip isnqlgpksa svvetqtlfr rgpqaggcvv dsevltqgip yqdyfytahr
      481 ycilglarnk arlrvsseir yrkqpwslvk slieknswsg iedyfhhldr elakaeklsl
      541 eeggkdtrgl lsglrrrkrp lswrghrdgp qhpdpdpctq tsmhtsgsls srfsepsvdq
      601 gpgagipsal vlisivlivl ialnallfyr lwslertaht feswhslala kgkfpqtate
      661 waeilalqkh fhsvevhkwr qilrasvell demkfslekl hqgitvpdpp ldtqpqpdds
      721 fp
//
LOCUS       NP_705899                553 aa            linear   PRI 27-APR-2025
DEFINITION  copine-9 isoform 1 [Homo sapiens].
ACCESSION   NP_705899
VERSION     NP_705899.2
DBSOURCE    REFSEQ: accession NM_153635.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Zhu,P., Qian,T., Si,C., Liu,Y., Cui,L., Huang,W., Fu,L., Deng,C.
            and Zeng,T.
  TITLE     High expression of CPNE5 and CPNE9 predicts positive prognosis in
            multiple myeloma
  JOURNAL   Cancer Biomark 31 (1), 77-85 (2021)
   PUBMED   33780365
  REMARK    GeneRIF: High expression of CPNE5 and CPNE9 predicts positive
            prognosis in multiple myeloma.
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Yoo,J.C., Lim,Ty., Park,J.S., Hah,Y.S., Park,N., Hong,S.G.,
            Park,J.Y. and Yoon,T.J.
  TITLE     SYT14L, especially its C2 domain, is involved in regulating
            melanocyte differentiation
  JOURNAL   J Dermatol Sci 72 (3), 246-251 (2013)
   PUBMED   23999003
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Pieragostino,D., Agnifili,L., Fasanella,V., D'Aguanno,S.,
            Mastropasqua,R., Di Ilio,C., Sacchetta,P., Urbani,A. and Del
            Boccio,P.
  TITLE     Shotgun proteomics reveals specific modulated protein patterns in
            tears of patients with primary open angle glaucoma naive to therapy
  JOURNAL   Mol Biosyst 9 (6), 1108-1116 (2013)
   PUBMED   23580065
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Liu,T., Qian,W.J., Gritsenko,M.A., Camp,D.G. 2nd, Monroe,M.E.,
            Moore,R.J. and Smith,R.D.
  TITLE     Human plasma N-glycoproteome analysis by immunoaffinity
            subtraction, hydrazide chemistry, and mass spectrometry
  JOURNAL   J Proteome Res 4 (6), 2070-2080 (2005)
   PUBMED   16335952
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Xie,H., Diber,A., Pollock,S., Nemzer,S., Safer,H., Meloon,B.,
            Olson,A., Hwang,J.J., Endress,G.A., Savitsky,K. and Gill-More,R.
  TITLE     Bridging expressed sequence alignments through targeted cDNA
            sequencing
  JOURNAL   Genomics 83 (4), 572-576 (2004)
   PUBMED   15028280
REFERENCE   8  (residues 1 to 553)
  AUTHORS   Creutz,C.E., Tomsig,J.L., Snyder,S.L., Gautier,M.C., Skouri,F.,
            Beisson,J. and Cohen,J.
  TITLE     The copines, a novel class of C2 domain-containing,
            calcium-dependent, phospholipid-binding proteins conserved from
            Paramecium to humans
  JOURNAL   J Biol Chem 273 (3), 1393-1402 (1998)
   PUBMED   9430674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM545574.1, BX453546.2, BU101942.1 and CA307982.1.
            
            On Feb 23, 2006 this sequence version replaced NP_705899.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.110338.1,
                                           SRR3476690.899559.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000383832.8/ ENSP00000373343.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..553
                     /product="copine-9 isoform 1"
                     /note="copine-like protein; copine-9; copine IX; copine
                     family member IX"
                     /calculated_mol_wt=61733
     Region          14..135
                     /region_name="C2A_Copine"
                     /note="C2 domain first repeat in Copine; cd04048"
                     /db_xref="CDD:176013"
     Site            order(29,35,89,91,101)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176013"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q8IYJ1.3)"
     Region          148..259
                     /region_name="C2B_Copine"
                     /note="C2 domain second repeat in Copine; cd04047"
                     /db_xref="CDD:176012"
     Site            order(163,169,225,227,233)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176012"
     Region          269..525
                     /region_name="vWA_copine_like"
                     /note="VWA Copine: Copines are phospholipid-binding
                     proteins originally identified in paramecium. They are
                     found in human and orthologues have been found in C.
                     elegans and Arabidopsis Thaliana. None have been found in
                     D. Melanogaster or S. Cereviciae; cd01459"
                     /db_xref="CDD:238736"
     Site            order(305,307,309,403,433)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238736"
     Region          531..553
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYJ1.3)"
     CDS             1..553
                     /gene="CPNE9"
                     /coded_by="NM_153635.3:165..1826"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2574.2"
                     /db_xref="GeneID:151835"
                     /db_xref="HGNC:HGNC:24336"
ORIGIN      
        1 mslggasers vpatkieitv scrnlldldt fsksdpmvvl ytqsrasqew refgrtevid
       61 ntlnpdfvrk fvldyffeek qnlrfdvynv dsktniskpk dflgqaflal geviggqgsr
      121 vertltgvpg kkcgtillta eelsncrdia tmqlcankld kkdffgksdp flvfyrsned
      181 gtftichkte vvkntlnpvw qpfsipvral cngdydrtvk idvydwdrdg shdfigeftt
      241 syrelskaqn qftvyevlnp rkkckkkkyv nsgtvtllsf svdseftfvd yikggtqlnf
      301 tvaidftasn gnplqptslh ymspyqlsay amalkavgei iqdydsdklf paygfgaklp
      361 pegrishqfp lnnndedpnc agiegvlesy fqslrtvqly gptyfapvin qvaraaakis
      421 dgsqyyvlli itdgvisdmt qtkeaivsas slpmsiiivg vgpamfeame eldgddvrvs
      481 srgryaerdi vqfvpfrdyv drsgnqvlsm arlakdvlae ipeqllsymr trdiqprppp
      541 panpspipap eqp
//
LOCUS       NP_982276                107 aa            linear   PRI 27-APR-2025
DEFINITION  serine-rich and transmembrane domain-containing protein 1 [Homo
            sapiens].
ACCESSION   NP_982276 XP_378410
VERSION     NP_982276.2
DBSOURCE    REFSEQ: accession NM_203451.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC036540.2, BI544475.1, AL136160.18, CA392022.1 and DC425828.1.
            
            On Aug 15, 2007 this sequence version replaced NP_982276.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.68081.1,
                                           SRR1660807.120578.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315190.4/ ENSP00000325776.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q13.3"
     Protein         1..107
                     /product="serine-rich and transmembrane domain-containing
                     protein 1"
                     /calculated_mol_wt=11327
     Region          11..106
                     /region_name="SRTM1"
                     /note="Serine-rich and transmembrane domain-containing
                     protein 1; pfam15872"
                     /db_xref="CDD:318153"
     Site            43..63
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A2A2V5.1)"
     CDS             1..107
                     /gene="SERTM1"
                     /gene_synonym="C13orf36"
                     /coded_by="NM_203451.3:339..662"
                     /db_xref="CCDS:CCDS9358.1"
                     /db_xref="GeneID:400120"
                     /db_xref="HGNC:HGNC:33792"
ORIGIN      
        1 msepdtssgf sgsvengtfl elfptslsts vdpssghlsn vyiyvsifls llafllllli
       61 ialqrlknii sssssypeyp sdagssftnl evcsissqrs tfsnlss
//
LOCUS       NP_000190                502 aa            linear   PRI 27-APR-2025
DEFINITION  N-sulphoglucosamine sulphohydrolase isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_000190
VERSION     NP_000190.1
DBSOURCE    REFSEQ: accession NM_000199.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Yi,F., Hong,X., Kumar,A.B., Zong,C., Boons,G.J., Scott,C.R.,
            Turecek,F., Robinson,B.H. and Gelb,M.H.
  TITLE     Detection of mucopolysaccharidosis III-A (Sanfilippo Syndrome-A) in
            dried blood spots (DBS) by tandem mass spectrometry
  JOURNAL   Mol Genet Metab 125 (1-2), 59-63 (2018)
   PUBMED   30006231
  REMARK    GeneRIF: Sulfamidase activity in 238 random newborns was well
            elevated compared to the range of activities measured in dried
            blood spots from 8 patients previously confirmed to have
            mucopolysaccharidosis III-A.
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Truxal,K.V., Fu,H., McCarty,D.M., McNally,K.A., Kunkler,K.L.,
            Zumberge,N.A., Martin,L., Aylward,S.C., Alfano,L.N., Berry,K.M.,
            Lowes,L.P., Corridore,M., McKee,C., McBride,K.L. and Flanigan,K.M.
  TITLE     A prospective one-year natural history study of
            mucopolysaccharidosis types IIIA and IIIB: Implications for
            clinical trial design
  JOURNAL   Mol Genet Metab 119 (3), 239-248 (2016)
   PUBMED   27590925
  REMARK    GeneRIF: CSF enzyme activity levels for either SGSH (in MPS IIIA
            subjects) or NAGLU (in MPS IIIB) significantly differed from normal
            controls. Several other behavioral or functional measures were
            found to be uninformative in this population, including timed
            functional motor tests.
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Wilkin,J., Kerr,N.C., Byrd,K.W., Ward,J.C. and Iannaccone,A.
  TITLE     Characterization of a Case of Pigmentary Retinopathy in Sanfilippo
            Syndrome Type IIIA Associated with Compound Heterozygous Mutations
            in the SGSH Gene
  JOURNAL   Ophthalmic Genet 37 (2), 217-227 (2016)
   PUBMED   26331342
  REMARK    GeneRIF: We have identified ocular features of a patient with
            Sanfilippo syndrome type IIIA harboring a novel SGHS mutation that
            were not previously known to occur in this disease - namely, a
            progressive retinopathy with distinctive features, cystic macular
            changes responsive to carbonic anhydrase inhibitors, and complex
            electroretinographic abnormalities consistent with postreceptoral
            dysfunction.
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Duncan,F.J., Naughton,B.J., Zaraspe,K., Murrey,D.A., Meadows,A.S.,
            Clark,K.R., Newsom,D.E., White,P., Fu,H. and McCarty,D.M.
  TITLE     Broad functional correction of molecular impairments by systemic
            delivery of scAAVrh74-hSGSH gene delivery in MPS IIIA mice
  JOURNAL   Mol Ther 23 (4), 638-647 (2015)
   PUBMED   25592334
  REMARK    GeneRIF: results demonstrate that a single systemic scAAVrh74-hSGSH
            delivery mediated efficient restoration of SGSH activity and
            resulted in a near complete correction of MPS IIIA molecular
            pathology
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Blanch,L., Weber,B., Guo,X.H., Scott,H.S. and Hopwood,J.J.
  TITLE     Molecular defects in Sanfilippo syndrome type A
  JOURNAL   Hum Mol Genet 6 (5), 787-791 (1997)
   PUBMED   9158154
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Karageorgos,L.E., Guo,X.H., Blanch,L., Weber,B., Anson,D.S.,
            Scott,H.S. and Hopwood,J.J.
  TITLE     Structure and sequence of the human sulphamidase gene
  JOURNAL   DNA Res 3 (4), 269-271 (1996)
   PUBMED   8946167
REFERENCE   8  (residues 1 to 502)
  AUTHORS   Scott,H.S., Blanch,L., Guo,X.H., Freeman,C., Orsborn,A., Baker,E.,
            Sutherland,G.R., Morris,C.P. and Hopwood,J.J.
  TITLE     Cloning of the sulphamidase gene and identification of mutations in
            Sanfilippo A syndrome
  JOURNAL   Nat Genet 11 (4), 465-467 (1995)
   PUBMED   7493035
REFERENCE   9  (residues 1 to 502)
  AUTHORS   Wagner,V.F. and Northrup,H.
  TITLE     Mucopolysaccharidosis Type III
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31536183
REFERENCE   10 (residues 1 to 502)
  AUTHORS   van de Kamp,J.J., Niermeijer,M.F., von Figura,K. and Giesberts,M.A.
  TITLE     Genetic heterogeneity and clinical variability in the Sanfilippo
            syndrome (types A, B, and C)
  JOURNAL   Clin Genet 20 (2), 152-160 (1981)
   PUBMED   6796310
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC319407.1, U30894.1,
            BU685248.1 and BP198470.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the enzyme sulfamidase; one of several
            enzymes involved in the lysosomal degradation of heparan sulfate.
            Mutations in this gene are associated with the lysosomal storage
            disease mucopolysaccaridosis IIIA, also known as Sanfilippo
            syndrome A, which results from impaired degradation of heparan
            sulfate. Transcripts of varying sizes have been reported but their
            biological validity has not been determined. [provided by RefSeq,
            Jun 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.229971.1, BC047318.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326317.11/ ENSP00000314606.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..502
                     /product="N-sulphoglucosamine sulphohydrolase isoform 1
                     precursor"
                     /EC_number="3.10.1.1"
                     /note="heparan sulfate sulfatase; sulfoglucosamine
                     sulfamidase; sulphamidase; mucopolysaccharidosis type
                     IIIA"
                     /calculated_mol_wt=54680
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2034
     mat_peptide     21..502
                     /product="N-sulphoglucosamine sulphohydrolase.
                     /id=PRO_0000033433"
                     /note="propagated from UniProtKB/Swiss-Prot (P51688.1)"
                     /calculated_mol_wt=54680
     Region          24..472
                     /region_name="SGSH"
                     /note="N-sulfoglucosamine sulfohydrolase (SGSH;
                     sulfamidase); cd16027"
                     /db_xref="CDD:293751"
     Site            order(31..32,70,123,125,181,273..274)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293751"
     Site            order(31..32,70,123,125,181,274)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293751"
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24816101,
                     ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV; propagated
                     from UniProtKB/Swiss-Prot (P51688.1)"
     Site            142
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51688.1)"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:24816101,
                     ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV; propagated
                     from UniProtKB/Swiss-Prot (P51688.1)"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX,
                     ECO:0007744|PDB:4MIV; propagated from UniProtKB/Swiss-Prot
                     (P51688.1)"
     Site            order(367,390..391)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293751"
     Site            413
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX,
                     ECO:0007744|PDB:4MIV; propagated from UniProtKB/Swiss-Prot
                     (P51688.1)"
     CDS             1..502
                     /gene="SGSH"
                     /gene_synonym="HSS; MPS3A; SFMD"
                     /coded_by="NM_000199.5:21..1529"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS11770.1"
                     /db_xref="GeneID:6448"
                     /db_xref="HGNC:HGNC:10818"
                     /db_xref="MIM:605270"
ORIGIN      
        1 mscpvpacca lllvlglcra rprnalllla ddggfesgay nnsaiatphl dalarrsllf
       61 rnaftsvssc spsraslltg lpqhqngmyg lhqdvhhfns fdkvrslpll lsqagvrtgi
      121 igkkhvgpet vypfdfayte engsvlqvgr nitrikllvr kflqtqddrp fflyvafhdp
      181 hrcghsqpqy gtfcekfgng esgmgripdw tpqaydpldv lvpyfvpntp aaradlaaqy
      241 ttvgrmdqgv glvlqelrda gvlndtlvif tsdngipfps grtnlywpgt aepllvsspe
      301 hpkrwgqvse ayvslldltp tildwfsipy psyaifgskt ihltgrsllp aleaeplwat
      361 vfgsqshhev tmsypmrsvq hrhfrlvhnl nfkmpfpidq dfyvsptfqd llnrttagqp
      421 tgwykdlrhy yyrarwelyd rsrdphetqn latdprfaql lemlrdqlak wqwethdpwv
      481 capdgvleek lspqcqplhn el
//
LOCUS       NP_075526                313 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat family A protein 2 [Homo sapiens].
ACCESSION   NP_075526
VERSION     NP_075526.1
DBSOURCE    REFSEQ: accession NM_023039.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Nie,J., Xu,C., Jin,J., Aka,J.A., Tempel,W., Nguyen,V., You,L.,
            Weist,R., Min,J., Pawson,T. and Yang,X.J.
  TITLE     Ankyrin repeats of ANKRA2 recognize a PxLPxL motif on the 3M
            syndrome protein CCDC8
  JOURNAL   Structure 23 (4), 700-712 (2015)
   PUBMED   25752541
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Xu,C., Jin,J., Bian,C., Lam,R., Tian,R., Weist,R., You,L., Nie,J.,
            Bochkarev,A., Tempel,W., Tan,C.S., Wasney,G.A., Vedadi,M.,
            Gish,G.D., Arrowsmith,C.H., Pawson,T., Yang,X.J. and Min,J.
  TITLE     Sequence-specific recognition of a PxLPxI/L motif by an ankyrin
            repeat tumbler lock
  JOURNAL   Sci Signal 5 (226), ra39 (2012)
   PUBMED   22649097
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Vaz Meirelles,G., Ferreira Lanza,D.C., da Silva,J.C., Santana
            Bernachi,J., Paes Leme,A.F. and Kobarg,J.
  TITLE     Characterization of hNek6 interactome reveals an important role for
            its short N-terminal domain and colocalization with proteins at the
            centrosome
  JOURNAL   J Proteome Res 9 (12), 6298-6316 (2010)
   PUBMED   20873783
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Wang,A.H., Gregoire,S., Zika,E., Xiao,L., Li,C.S., Li,H.,
            Wright,K.L., Ting,J.P. and Yang,X.J.
  TITLE     Identification of the ankyrin repeat proteins ANKRA and RFXANK as
            novel partners of class IIa histone deacetylases
  JOURNAL   J Biol Chem 280 (32), 29117-29127 (2005)
   PUBMED   15964851
  REMARK    GeneRIF: ANKRA, RFXANK, and CIITA are novel targets of class IIa
            HDACs which may deacetylases play a role in regulating MHCII
            expression
REFERENCE   8  (residues 1 to 313)
  AUTHORS   Rader,K., Orlando,R.A., Lou,X. and Farquhar,M.G.
  TITLE     Characterization of ANKRA, a novel ankyrin repeat protein that
            interacts with the cytoplasmic domain of megalin
  JOURNAL   J Am Soc Nephrol 11 (12), 2167-2178 (2000)
   PUBMED   11095640
REFERENCE   9  (residues 1 to 313)
  AUTHORS   Rader,K., Boyer,A.D., Farquhar,M.G. and Arden,K.C.
  TITLE     Assignment of ankyrin repeat, family A (RFXANK-like) 2 (ANKRA2) to
            human chromosome 5q12-->q13 by radiation hybrid mapping and somatic
            cell hybrid PCR
  JOURNAL   Cytogenet Cell Genet 89 (3-4), 164-165 (2000)
   PUBMED   10965114
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL558295.3, BC012917.1, DB543368.1 and AC010279.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.106596.1,
                                           SRR3476690.56682.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296785.8/ ENSP00000296785.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.2"
     Protein         1..313
                     /product="ankyrin repeat family A protein 2"
                     /note="RFXANK-like protein 2; ankyrin repeat, family A
                     (RFXANK-like), 2"
                     /calculated_mol_wt=34141
     Region          <93..207
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Region          144..179
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          148..180
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9E1.1)"
     Region          <169..313
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(181,183,187..188,191..193,195..196,200,203,212,214,
                     216,220..221,224..226,228..229,233,236,245,247,249,
                     253..254,257..259,261..262,266,269)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          181..213
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9E1.1)"
     Region          181..212
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          214..246
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9E1.1)"
     Region          214..245
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          247..279
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9E1.1)"
     Region          247..277
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          280..313
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9E1.1)"
     CDS             1..313
                     /gene="ANKRA2"
                     /gene_synonym="ANKRA"
                     /coded_by="NM_023039.5:613..1554"
                     /db_xref="CCDS:CCDS4020.1"
                     /db_xref="GeneID:57763"
                     /db_xref="HGNC:HGNC:13208"
                     /db_xref="MIM:605787"
ORIGIN      
        1 mdtstnldig aqliveecps tysltgmpdi kiehpldpns eegsaqgvam gmkfilpnrf
       61 dmnvcsrfvk slneedskni qdqvnsdlev asvlfkaecn ihtspspgiq vrhvytpstt
      121 khfspikqst tltnkhrgne vsttpllans lsvhqlaaqg emlylatrie qenvinhtde
      181 egftplmwaa ahgqiavvef llqngadpql lgkgresals lacskgytdi vkmlldcgvd
      241 vneydwnggt pllyavhgnh vkcvkmlles gadptietds gynsmdlava lgyrsvqqvi
      301 eshllkllqn ike
//
LOCUS       NP_003492                700 aa            linear   PRI 27-APR-2025
DEFINITION  peroxisomal acyl-coenzyme A oxidase 3 isoform a [Homo sapiens].
ACCESSION   NP_003492
VERSION     NP_003492.2
DBSOURCE    REFSEQ: accession NM_003501.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Kim,J.T., Won,S.Y., Kang,K., Kim,S.H., Park,M.S., Choi,K.H.,
            Nam,T.S., Denis,S.W., Ferdinandusse,S., Lee,J.E., Choi,S.Y. and
            Kim,M.K.
  TITLE     ACOX3 Dysfunction as a Potential Cause of Recurrent Spontaneous
            Vasospasm of Internal Carotid Artery
  JOURNAL   Transl Stroke Res 11 (5), 1041-1051 (2020)
   PUBMED   31975215
  REMARK    GeneRIF: ACOX3 Dysfunction as a Potential Cause of Recurrent
            Spontaneous Vasospasm of Internal Carotid Artery.
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Wade,R., Di Bernardo,M.C., Richards,S., Rossi,D.,
            Crowther-Swanepoel,D., Gaidano,G., Oscier,D.G., Catovsky,D. and
            Houlston,R.S.
  TITLE     Association between single nucleotide polymorphism-genotype and
            outcome of patients with chronic lymphocytic leukemia in a
            randomized chemotherapy trial
  JOURNAL   Haematologica 96 (10), 1496-1503 (2011)
   PUBMED   21659360
REFERENCE   3  (residues 1 to 700)
  AUTHORS   Shimada,M., Miyagawa,T., Kawashima,M., Tanaka,S., Honda,Y.,
            Honda,M. and Tokunaga,K.
  TITLE     An approach based on a genome-wide association study reveals
            candidate loci for narcolepsy
  JOURNAL   Hum Genet 128 (4), 433-441 (2010)
   PUBMED   20677014
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 700)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 700)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   6  (residues 1 to 700)
  AUTHORS   Zha,S., Ferdinandusse,S., Hicks,J.L., Denis,S., Dunn,T.A.,
            Wanders,R.J., Luo,J., De Marzo,A.M. and Isaacs,W.B.
  TITLE     Peroxisomal branched chain fatty acid beta-oxidation pathway is
            upregulated in prostate cancer
  JOURNAL   Prostate 63 (4), 316-323 (2005)
   PUBMED   15599942
  REMARK    GeneRIF: ACOX3, which is expressed at extremely low level in other
            human organs studied including the liver, might contribute
            significantly to peroxisomal branched chain fatty acid
            beta-oxidation in human prostate tissue and some prostate cancer
            cell lines
REFERENCE   7  (residues 1 to 700)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   8  (residues 1 to 700)
  AUTHORS   Vanhooren,J.C., Marynen,P., Mannaerts,G.P. and Van Veldhoven,P.P.
  TITLE     Evidence for the existence of a pristanoyl-CoA oxidase gene in man
  JOURNAL   Biochem J 325 (Pt 3) (Pt 3), 593-599 (1997)
   PUBMED   9271077
REFERENCE   9  (residues 1 to 700)
  AUTHORS   Baumgart,E., Vanhooren,J.C., Fransen,M., Mannaerts,G.P. and Van
            Veldhoven,P.P.
  TITLE     Mammalian peroxisomal acyl-CoA oxidases. III. Molecular
            characterization of human branched chain fatty acyl-CoA oxidase
  JOURNAL   Ann N Y Acad Sci 804, 678-679 (1996)
   PUBMED   8993592
REFERENCE   10 (residues 1 to 700)
  AUTHORS   Vanhove,G.F., Van Veldhoven,P.P., Fransen,M., Denis,S.,
            Eyssen,H.J., Wanders,R.J. and Mannaerts,G.P.
  TITLE     The CoA esters of 2-methyl-branched chain fatty acids and of the
            bile acid intermediates di- and trihydroxycoprostanic acids are
            oxidized by one single peroxisomal branched chain acyl-CoA oxidase
            in human liver and kidney
  JOURNAL   J Biol Chem 268 (14), 10335-10344 (1993)
   PUBMED   8387517
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA949869.1, BC017053.1, Y11411.1 and CA306669.1.
            
            On Aug 17, 2007 this sequence version replaced NP_003492.1.
            
            Summary: Acyl-Coenzyme A oxidase 3 also know as pristanoyl -CoA
            oxidase (ACOX3)is involved in the desaturation of 2-methyl branched
            fatty acids in peroxisomes.  Unlike the rat homolog, the human gene
            is expressed in very low amounts in liver such that its mRNA was
            undetectable by routine Northern-blot analysis or its product by
            immunoblotting or by enzyme activity measurements.  However the
            human cDNA encoding a 700 amino acid protein with a peroxisomal
            targeting C-terminal tripeptide S-K-L was isolated and is thought
            to be expressed under special conditions such as specific
            developmental stages or in a tissue specific manner in tissues that
            have not yet been examined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.175740.1,
                                           SRR1803612.206263.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356406.10/ ENSP00000348775.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.1"
     Protein         1..700
                     /product="peroxisomal acyl-coenzyme A oxidase 3 isoform a"
                     /EC_number="1.3.3.6"
                     /note="acyl-Coenzyme A oxidase 3, pristanoyl; peroxisomal
                     acyl-coenzyme A oxidase 3; BRCACox; pristanoyl-CoA
                     oxidase; branched-chain acyl-CoA oxidase"
                     /calculated_mol_wt=77498
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O15254.2)"
     Region          19..672
                     /region_name="AXO"
                     /note="Peroxisomal acyl-CoA oxidase; cd01150"
                     /db_xref="CDD:173839"
     Site            order(75..76,80,84,161..166,168,195..196,202..203,231,
                     245..250,252..253,333,335,343,348..350,355,420,423,
                     428..429,431,433,441..442,445,455,544,548..549,551..552,
                     663,669..670)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:173839"
     Site            order(127,156..159,196..198,253,303,311,431,450..451)
                     /site_type="active"
                     /db_xref="CDD:173839"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (O15254.2)"
     Site            451
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:173839"
     Site            467
                     /site_type="active"
                     /note="end of homology with other ACAD's [active]"
                     /db_xref="CDD:173839"
     Region          698..700
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000250|UniProtKB:Q63448"
                     /note="propagated from UniProtKB/Swiss-Prot (O15254.2)"
     CDS             1..700
                     /gene="ACOX3"
                     /coded_by="NM_003501.3:91..2193"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3401.1"
                     /db_xref="GeneID:8310"
                     /db_xref="HGNC:HGNC:121"
                     /db_xref="MIM:603402"
ORIGIN      
        1 mastveggdt allpefprgp ldayrarasf swkelalfte gegmlrfkkt ifsalendpl
       61 farspgadls lekyrelnfl rckrifeydf lsvedmfksp lkvpaliqcl gmydsslaak
      121 yllhslvfgs avyssgserh ltyiqkifrm eifgcfalte lshgsntkai rttahydpat
      181 eefiihspdf eaakfwvgnm gktathavvf aklcvpgdqc hglhpfivqi rdpktllpmp
      241 gvmvgdigkk lgqngldngf amfhkvrvpr qsllnrmgdv tpegtyvspf kdvrqrfgas
      301 lgslssgrvs ivslailnlk lavaialrfs atrrqfgpte eeeipvleyp mqqwrllpyl
      361 aavyaldhfs kslfldlvel qrglasgdrs arqaelgrei halasaskpl aswttqqgiq
      421 ecreacgghg ylamnrlgvl rddndpncty egdnnillqq tsnyllglla hqvhdgacfr
      481 splksvdfld aypgildqkf evssvadcld savalaaykw lvcyllrety qklnqekrsg
      541 ssdfearnkc qvshgrplal afveltvvqr fhehvhqpsv ppslravlgr lsalyalwsl
      601 srhaallyrg gyfsgeqage vlesavlalc sqlkddaval vdviappdfv ldspigradg
      661 elyknlwgav lqeskvlera swwpefsvnk pvigslkskl
//
LOCUS       NP_001138748             610 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger Y-chromosomal protein isoform 3 [Homo sapiens].
ACCESSION   NP_001138748
VERSION     NP_001138748.1
DBSOURCE    REFSEQ: accession NM_001145276.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Ni,W., Perez,A.A., Schreiner,S., Nicolet,C.M. and Farnham,P.J.
  TITLE     Characterization of the ZFX family of transcription factors that
            bind downstream of the start site of CpG island promoters
  JOURNAL   Nucleic Acids Res 48 (11), 5986-6000 (2020)
   PUBMED   32406922
  REMARK    GeneRIF: Characterization of the ZFX family of transcription
            factors that bind downstream of the start site of CpG island
            promoters.
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Decarpentrie,F., Vernet,N., Mahadevaiah,S.K., Longepied,G.,
            Streichemberger,E., Aknin-Seifer,I., Ojarikre,O.A., Burgoyne,P.S.,
            Metzler-Guillemain,C. and Mitchell,M.J.
  TITLE     Human and mouse ZFY genes produce a conserved testis-specific
            transcript encoding a zinc finger protein with a short acidic
            domain and modified transactivation potential
  JOURNAL   Hum Mol Genet 21 (12), 2631-2645 (2012)
   PUBMED   22407129
  REMARK    GeneRIF: Studies identified a major testis-specific ZFY transcript
            that encodes a protein with the same short acidic domain.
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Tricoli,J.V. and Bracken,R.B.
  TITLE     ZFY gene expression and retention in human prostate adenocarcinoma
  JOURNAL   Genes Chromosomes Cancer 6 (2), 65-72 (1993)
   PUBMED   7680890
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Kochoyan,M., Keutmann,H.T. and Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            refinement of the NMR structure of an even finger by selective
            deuterium labeling and implications for DNA recognition
  JOURNAL   Biochemistry 30 (29), 7063-7072 (1991)
   PUBMED   1854720
REFERENCE   8  (residues 1 to 610)
  AUTHORS   North,M., Sargent,C., O'Brien,J., Taylor,K., Wolfe,J., Affara,N.A.
            and Ferguson-Smith,M.A.
  TITLE     Comparison of ZFY and ZFX gene structure and analysis of
            alternative 3' untranslated regions of ZFY
  JOURNAL   Nucleic Acids Res 19 (10), 2579-2586 (1991)
   PUBMED   2041734
REFERENCE   9  (residues 1 to 610)
  AUTHORS   Kochoyan,M., Havel,T.F., Nguyen,D.T., Dahl,C.E., Keutmann,H.T. and
            Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            2D NMR structure of an even finger and implications for
            'jumping-linker' DNA recognition
  JOURNAL   Biochemistry 30 (14), 3371-3386 (1991)
   PUBMED   1849423
REFERENCE   10 (residues 1 to 610)
  AUTHORS   Palmer,M.S., Berta,P., Sinclair,A.H., Pym,B. and Goodfellow,P.N.
  TITLE     Comparison of human ZFY and ZFX transcripts
  JOURNAL   Proc Natl Acad Sci U S A 87 (5), 1681-1685 (1990)
   PUBMED   2308929
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006157.2.
            
            Summary: This gene encodes a zinc finger-containing protein that
            may function as a transcription factor. This gene was once a
            candidate gene for the testis-determining factor (TDF) and was
            erroneously referred to as TDF. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301061.1, SRR1803614.85942.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yp11.2"
     Protein         1..610
                     /product="zinc finger Y-chromosomal protein isoform 3"
                     /note="zinc finger Y-chromosomal protein"
                     /calculated_mol_wt=69777
     Region          <22..215
                     /region_name="Zfx_Zfy_act"
                     /note="Zfx / Zfy transcription activation region;
                     pfam04704"
                     /db_xref="CDD:461400"
     Region          <226..401
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          <232..>254
                     /region_name="ROS_MUCR"
                     /note="ROS/MUCR transcriptional regulator protein;
                     cl19880"
                     /db_xref="CDD:473244"
     Region          232..252
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(232,235,248,252)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          263..287
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          295..315
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(295,298,311,315)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(300,302,304,306..307,310..311,314,360,362,366..367,
                     370..371,374,388,390,392,394..395,398..399,402)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          348..>485
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          355..375
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          383..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          412..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          526..546
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(526,529,542,546)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(531,533,535,537..538,541..542,545,559,561,565..566,
                     569..570,574,588,590,592,594..595,598..599,602)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          538..562
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          554..575
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          583..603
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..610
                     /gene="ZFY"
                     /gene_synonym="ZNF911"
                     /coded_by="NM_001145276.2:95..1927"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS48200.1"
                     /db_xref="GeneID:7544"
                     /db_xref="HGNC:HGNC:12870"
                     /db_xref="MIM:490000"
ORIGIN      
        1 mdedefelqp qepnsffdgi vddagkiehd gstgvtidae semdpckvds tcpevikvyi
       61 fkadpgeddl ggtvdivese pendhgvell dqnssirvpr ekmvymtvnd sqqededlnv
      121 aeiadevyme vivgeedaav aaaaaavheq qidedemktf vpiawaaayg nnsdgienrn
      181 gtasallhid esaglgrlak qkpkkkrrpd srqyqtaiii gpdghpltvy pcmicgkkfk
      241 srgflkrhmk nhpehlakkk yhctdcdytt nkkislhnhl eshkltskae kaiecdecgk
      301 hfshagalft hkmvhkekga nkmhkckfce yetaeqglln rhllavhskn fphicvecgk
      361 gfrhpselrk hmrihtgekp yqcqyceyrs adssnlkthi ktkhskempf kcdiclltfs
      421 dtkevqqhtl vhqeskthqc lhcdhkssns sdlkrhvisv htkdyphkce mcekgfhrps
      481 elkkhvavhk gkkmhqcrhc dfkiadpfvl srhilsvhtk dlpfrckrcr kgfrqqnelk
      541 khmkthsgrk vyqceyceys ttdasgfkrh visihtkdyp hrceyckkgf rrpseknqhi
      601 mrhhkevglp
//
LOCUS       NP_005495                386 aa            linear   PRI 27-APR-2025
DEFINITION  branched-chain-amino-acid aminotransferase, cytosolic isoform 1
            [Homo sapiens].
ACCESSION   NP_005495
VERSION     NP_005495.2
DBSOURCE    REFSEQ: accession NM_005504.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Kang,Y.J., Song,W., Lee,S.J., Choi,S.A., Chae,S., Yoon,B.R.,
            Kim,H.Y., Lee,J.H., Kim,C., Cho,J.Y., Kim,H.J. and Lee,W.W.
  TITLE     Inhibition of BCAT1-mediated cytosolic leucine metabolism regulates
            Th17 responses via the mTORC1-HIF1alpha pathway
  JOURNAL   Exp Mol Med 56 (8), 1776-1790 (2024)
   PUBMED   39085353
  REMARK    GeneRIF: Inhibition of BCAT1-mediated cytosolic leucine metabolism
            regulates Th17 responses via the mTORC1-HIF1alpha pathway.
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Wang,W., Li,Y., Tang,L., Shi,Y., Li,W., Zou,L., Zhang,L., Cheng,Y.,
            Yuan,Z., Zhu,F. and Duan,Q.
  TITLE     Cross-talk between BCKDK-mediated phosphorylation and
            STUB1-dependent ubiquitination degradation of BCAT1 promotes GBM
            progression
  JOURNAL   Cancer Lett 591, 216849 (2024)
   PUBMED   38621458
  REMARK    GeneRIF: Cross-talk between BCKDK-mediated phosphorylation and
            STUB1-dependent ubiquitination degradation of BCAT1 promotes GBM
            progression.
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Pan,J., Wang,Y., Huang,S., Mao,S., Ling,Q., Li,C., Li,F., Yu,M.,
            Huang,X., Huang,J., Lv,Y., Li,X., Ye,W., Wang,H., Wang,J. and
            Jin,J.
  TITLE     High expression of BCAT1 sensitizes AML cells to PARP inhibitor by
            suppressing DNA damage response
  JOURNAL   J Mol Med (Berl) 102 (3), 415-433 (2024)
   PUBMED   38340163
  REMARK    GeneRIF: High expression of BCAT1 sensitizes AML cells to PARP
            inhibitor by suppressing DNA damage response.
REFERENCE   4  (residues 1 to 386)
  AUTHORS   You,H., Song,G., Xu,Z., Chen,S., Shen,W., Liu,H., Deng,B., Li,J.
            and Huang,G.
  TITLE     HuR promotes castration-resistant prostate cancer progression by
            altering ERK5 activation via posttranscriptional regulation of
            BCAT1
  JOURNAL   J Transl Med 22 (1), 178 (2024)
   PUBMED   38369471
  REMARK    GeneRIF: HuR promotes castration-resistant prostate cancer
            progression by altering ERK5 activation via posttranscriptional
            regulation of BCAT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Zheng,J., Liu,Y., Wang,J., Shi,J., Li,L., Jiang,X. and Tao,L.
  TITLE     Integrated single-cell and bulk characterization of branched chain
            amino acid metabolism-related key gene BCAT1 and association with
            prognosis and immunogenicity of clear cell renal cell carcinoma
  JOURNAL   Aging (Albany NY) 16 (3), 2715-2735 (2024)
   PUBMED   38309289
  REMARK    GeneRIF: Integrated single-cell and bulk characterization of
            branched chain amino acid metabolism-related key gene BCAT1 and
            association with prognosis and immunogenicity of clear cell renal
            cell carcinoma.
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Eden,A. and Benvenisty,N.
  TITLE     Involvement of branched-chain amino acid aminotransferase
            (Bcat1/Eca39) in apoptosis
  JOURNAL   FEBS Lett 457 (2), 255-261 (1999)
   PUBMED   10471790
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Ben-Yosef,T., Eden,A. and Benvenisty,N.
  TITLE     Characterization of murine BCAT genes: Bcat1, a c-Myc target, and
            its homolog, Bcat2
  JOURNAL   Mamm Genome 9 (7), 595-597 (1998)
   PUBMED   9657861
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Bledsoe,R.K., Dawson,P.A. and Hutson,S.M.
  TITLE     Cloning of the rat and human mitochondrial branched chain
            aminotransferases (BCATm)
  JOURNAL   Biochim Biophys Acta 1339 (1), 9-13 (1997)
   PUBMED   9165094
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Schuldiner,O., Eden,A., Ben-Yosef,T., Yanuka,O., Simchen,G. and
            Benvenisty,N.
  TITLE     ECA39, a conserved gene regulated by c-Myc in mice, is involved in
            G1/S cell cycle regulation in yeast
  JOURNAL   Proc Natl Acad Sci U S A 93 (14), 7143-7148 (1996)
   PUBMED   8692959
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Naylor,S.L. and Shows,T.B.
  TITLE     Branched-chain aminotransferase deficiency in Chinese hamster cells
            complemented by two independent genes on human chromosomes 12 and
            19
  JOURNAL   Somatic Cell Genet 6 (5), 641-652 (1980)
   PUBMED   6933702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK056255.1, BX474651.1,
            AC023796.22 and BU618839.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 5, 2003 this sequence version replaced NP_005495.1.
            
            Summary: This gene encodes the cytosolic form of the enzyme
            branched-chain amino acid transaminase. This enzyme catalyzes the
            reversible transamination of branched-chain alpha-keto acids to
            branched-chain L-amino acids essential for cell growth. Two
            different clinical disorders have been attributed to a defect of
            branched-chain amino acid transamination: hypervalinemia and
            hyperleucine-isoleucinemia. As there is also a gene encoding a
            mitochondrial form of this enzyme, mutations in either gene may
            contribute to these disorders. Alternatively spliced transcript
            variants have been described. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647122.1, SRR1660809.157590.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261192.12/ ENSP00000261192.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..386
                     /product="branched-chain-amino-acid aminotransferase,
                     cytosolic isoform 1"
                     /EC_number="2.6.1.42"
                     /note="branched chain aminotransferase 1, cytosolic;
                     placental protein 18; branched chain amino-acid
                     transaminase 1, cytosolic"
                     /calculated_mol_wt=42835
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P54687.3)"
     Region          32..378
                     /region_name="PRK13357"
                     /note="branched-chain amino acid aminotransferase;
                     Provisional"
                     /db_xref="CDD:237363"
     CDS             1..386
                     /gene="BCAT1"
                     /gene_synonym="BCATC; BCT1; ECA39; MECA39; PNAS121; PP18"
                     /coded_by="NM_005504.7:170..1330"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44845.1"
                     /db_xref="GeneID:586"
                     /db_xref="HGNC:HGNC:976"
                     /db_xref="MIM:113520"
ORIGIN      
        1 mkdcsngcsa ectgeggske vvgtfkakdl ivtpatilke kpdpnnlvfg tvftdhmltv
       61 ewssefgwek phikplqnls lhpgssalhy avelfeglka frgvdnkirl fqpnlnmdrm
      121 yrsavratlp vfdkeellec iqqlvkldqe wvpystsasl yirptfigte pslgvkkptk
      181 allfvllspv gpyfssgtfn pvslwanpky vrawkggtgd ckmggnygss lfaqceavdn
      241 gcqqvlwlyg edhqitevgt mnlflywine dgeeelatpp ldgiilpgvt rrcildlahq
      301 wgefkvsery ltmddlttal egnrvremfg sgtacvvcpv sdilykgeti hiptmengpk
      361 lasrilsklt diqygreesd wtivls
//
LOCUS       NP_078915                402 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 322 [Homo sapiens].
ACCESSION   NP_078915
VERSION     NP_078915.2
DBSOURCE    REFSEQ: accession NM_024639.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Huang,S.H., Hsieh,H.C., Shieh,J.M., Su,W.C. and Wang,Y.C.
  TITLE     Downregulation of microRNA-326 enhances ZNF322A expression,
            transcriptional activity and tumorigenic effects in lung cancer
  JOURNAL   Biofactors 50 (1), 214-227 (2024)
   PUBMED   37647209
  REMARK    GeneRIF: Downregulation of microRNA-326 enhances ZNF322A
            expression, transcriptional activity and tumorigenic effects in
            lung cancer.
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Lin,C.C., Kuo,I.Y., Wu,L.T., Kuan,W.H., Liao,S.Y., Jen,J.,
            Yang,Y.E., Tang,C.W., Chen,Y.R. and Wang,Y.C.
  TITLE     Dysregulated Kras/YY1/ZNF322A/Shh transcriptional axis enhances
            neo-angiogenesis to promote lung cancer progression
  JOURNAL   Theranostics 10 (22), 10001-10015 (2020)
   PUBMED   32929330
  REMARK    GeneRIF: Dysregulated Kras/YY1/ZNF322A/Shh transcriptional axis
            enhances neo-angiogenesis to promote lung cancer progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Cheung,C.H.Y., Hsu,C.L., Lin,T.Y., Chen,W.T., Wang,Y.C., Huang,H.C.
            and Juan,H.F.
  TITLE     ZNF322A-mediated protein phosphorylation induces autophagosome
            formation through modulation of IRS1-AKT glucose uptake and
            HSP-elicited UPR in lung cancer
  JOURNAL   J Biomed Sci 27 (1), 75 (2020)
   PUBMED   32576196
  REMARK    GeneRIF: ZNF322A-mediated protein phosphorylation induces
            autophagosome formation through modulation of IRS1-AKT glucose
            uptake and HSP-elicited UPR in lung cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Liao,S.Y., Kuo,I.Y., Chen,Y.T., Liao,P.C., Liu,Y.F., Wu,H.Y.,
            Lai,W.W. and Wang,Y.C.
  TITLE     AKT-mediated phosphorylation enhances protein stability and
            transcription activity of ZNF322A to promote lung cancer
            progression
  JOURNAL   Oncogene 38 (41), 6723-6736 (2019)
   PUBMED   31399647
  REMARK    GeneRIF: results reveal a new mechanism of AKT signaling in
            promoting ZNF322A protein stability and transcriptional activity in
            lung cancer cell, xenograft, and clinical models
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Jen,J., Liu,C.Y., Chen,Y.T., Wu,L.T., Shieh,Y.C., Lai,W.W. and
            Wang,Y.C.
  TITLE     Oncogenic zinc finger protein ZNF322A promotes stem cell-like
            properties in lung cancer through transcriptional suppression of
            c-Myc expression
  JOURNAL   Cell Death Differ 26 (7), 1283-1298 (2019)
   PUBMED   30258097
  REMARK    GeneRIF: The ZNF322A-centered transcriptome promotes lung
            tumorigenesis and ZNF322A acts as a transcription suppressor of
            c-Myc to maintain lung cancer stem cell-like properties by shifting
            metabolism towards oxidative phosphorylation.
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Liao,S.Y., Chiang,C.W., Hsu,C.H., Chen,Y.T., Jen,J., Juan,H.F.,
            Lai,W.W. and Wang,Y.C.
  TITLE     CK1delta/GSK3beta/FBXW7alpha axis promotes degradation of the
            ZNF322A oncoprotein to suppress lung cancer progression
  JOURNAL   Oncogene 36 (41), 5722-5733 (2017)
   PUBMED   28581525
  REMARK    GeneRIF: Our results reveal a new mechanism of ZNF322A oncoprotein
            destruction regulated by the CK1delta/GSK3beta/FBXW7a axis.
            Deregulation of this signaling axis results in ZNF322A
            overexpression and promotes cancer progression
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Jen,J., Lin,L.L., Chen,H.T., Liao,S.Y., Lo,F.Y., Tang,Y.A.,
            Su,W.C., Salgia,R., Hsu,C.L., Huang,H.C., Juan,H.F. and Wang,Y.C.
  TITLE     Oncoprotein ZNF322A transcriptionally deregulates alpha-adducin,
            cyclin D1 and p53 to promote tumor growth and metastasis in lung
            cancer
  JOURNAL   Oncogene 35 (18), 2357-2369 (2016)
   PUBMED   26279304
  REMARK    GeneRIF: ZNF322A overexpression transcriptionally dysregulates
            genes involved in cell growth and motility therefore contributes to
            lung tumorigenesis and poor prognosis
            Erratum:[Oncogene. 2017 Aug;36(31):4526. doi: 10.1038/onc.2017.77.
            PMID: 28368404]
REFERENCE   8  (residues 1 to 402)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 402)
  AUTHORS   Li,Y., Wang,Y., Zhang,C., Yuan,W., Wang,J., Zhu,C., Chen,L.,
            Huang,W., Zeng,W., Wu,X. and Liu,M.
  TITLE     ZNF322, a novel human C2H2 Kruppel-like zinc-finger protein,
            regulates transcriptional activation in MAPK signaling pathways
  JOURNAL   Biochem Biophys Res Commun 325 (4), 1383-1392 (2004)
   PUBMED   15555580
  REMARK    GeneRIF: These results suggest that ZNF322 is a member of the
            zinc-finger transcription factor family and may act as a positive
            regulator in gene transcription mediated by the MAPK signaling
            pathways.
REFERENCE   10 (residues 1 to 402)
  AUTHORS   Fortna,A., Kim,Y., MacLaren,E., Marshall,K., Hahn,G., Meltesen,L.,
            Brenton,M., Hink,R., Burgers,S., Hernandez-Boussard,T.,
            Karimpour-Fard,A., Glueck,D., McGavran,L., Berry,R., Pollack,J. and
            Sikela,J.M.
  TITLE     Lineage-specific gene duplication and loss in human and great ape
            evolution
  JOURNAL   PLoS Biol 2 (7), E207 (2004)
   PUBMED   15252450
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX474628.1, AK290038.1 and AL513548.8.
            
            On Jan 2, 2004 this sequence version replaced NP_078915.1.
            
            Summary: ZNF322A is a member of the zinc-finger transcription
            factor family and may regulate transcriptional activation in MAPK
            (see MAPK1; MIM 176948) signaling pathways (Li et al., 2004 [PubMed
            15555580]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3 and 4 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.241668.1,
                                           SRR1803615.87429.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000415922.7/ ENSP00000418897.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.2"
     Protein         1..402
                     /product="zinc finger protein 322"
                     /note="HLA complex group 12; zinc finger protein 489; zinc
                     finger protein 388; zinc finger protein 322A"
                     /calculated_mol_wt=46810
     Region          45..65
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <69..219
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          73..93
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          101..121
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          129..149
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(134,136,138,140..141,144..145,148,162,164,168..169,
                     172..173,176,190,192,194,196..197,200..201,204)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          157..177
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          185..205
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <207..291
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          213..233
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          241..261
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          269..289
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          295..315
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          353..373
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6U7Q0.2)"
     CDS             1..402
                     /gene="ZNF322"
                     /gene_synonym="HCG12; ZNF322A; ZNF388; ZNF489"
                     /coded_by="NM_024639.5:641..1849"
                     /db_xref="CCDS:CCDS4617.1"
                     /db_xref="GeneID:79692"
                     /db_xref="HGNC:HGNC:23640"
                     /db_xref="MIM:610847"
ORIGIN      
        1 mytseekcnq rtqkrkiynv cprkgkkifi hmheiiqidg hiyqcleckq nfcenlalim
       61 certhtgekp ykcdmcektf vqssdltshq rihnyekpyk cskceksfwh hlalsghqrt
      121 hagkkfytcd icgknfgqss dllvhqrsht gekpylcsec dkcfsrstnl irhrrthtge
      181 kpfkclecek afsgksdlis hqrthtgerp ykcnkceksy rhrsafivhk rvhtgekpyk
      241 cgacekcfgq ksdlivhqrv htgekpykcl ecmrsftrsa nlirhqatht htfkcleyek
      301 sfncssdliv hqrihmeekp hqwsacesgf llgmdfvaqq kmrtqteelh ykytvcdksf
      361 hqssallqhq tvhigekpfv cnvsekglel spphaseasq ms
//
LOCUS       NP_056083               2243 aa            linear   PRI 27-APR-2025
DEFINITION  dnaJ homolog subfamily C member 13 isoform 2 [Homo sapiens].
ACCESSION   NP_056083 XP_039828
VERSION     NP_056083.3
DBSOURCE    REFSEQ: accession NM_015268.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2243)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 2243)
  AUTHORS   Saini,P., Rudakou,U., Yu,E., Ruskey,J.A., Asayesh,F., Laurent,S.B.,
            Spiegelman,D., Fahn,S., Waters,C., Monchi,O., Dauvilliers,Y.,
            Dupre,N., Greenbaum,L., Hassin-Baer,S., Espay,A.J., Rouleau,G.A.,
            Alcalay,R.N., Fon,E.A., Postuma,R.B. and Gan-Or,Z.
  TITLE     Association study of DNAJC13, UCHL1, HTRA2, GIGYF2, and EIF4G1 with
            Parkinson's disease
  JOURNAL   Neurobiol Aging 100, 119 (2021)
   PUBMED   33239198
  REMARK    GeneRIF: Association study of DNAJC13, UCHL1, HTRA2, GIGYF2, and
            EIF4G1 with Parkinson's disease.
REFERENCE   3  (residues 1 to 2243)
  AUTHORS   Besemer,A.S., Maus,J., Ax,M.D.A., Stein,A., Vo,S., Freese,C.,
            Nalbach,K., von Hilchen,C., Pfalzgraf,I.F., Koziollek-Drechsler,I.,
            Silva,B., Huesmann,H., Boukhallouk,F., Florin,L., Kern,A., Behl,C.
            and Clement,A.M.
  TITLE     Receptor-mediated endocytosis 8 (RME-8)/DNAJC13 is a novel positive
            modulator of autophagy and stabilizes cellular protein homeostasis
  JOURNAL   Cell Mol Life Sci 78 (2), 645-660 (2021)
   PUBMED   32322926
  REMARK    GeneRIF: Receptor-mediated endocytosis 8 (RME-8)/DNAJC13 is a novel
            positive modulator of autophagy and stabilizes cellular protein
            homeostasis.
REFERENCE   4  (residues 1 to 2243)
  AUTHORS   Follett,J., Fox,J.D., Gustavsson,E.K., Kadgien,C., Munsie,L.N.,
            Cao,L.P., Tatarnikov,I., Milnerwood,A.J. and Farrer,M.J.
  TITLE     DNAJC13 p.Asn855Ser, implicated in familial parkinsonism, alters
            membrane dynamics of sorting nexin 1
  JOURNAL   Neurosci Lett 706, 114-122 (2019)
   PUBMED   31082451
REFERENCE   5  (residues 1 to 2243)
  AUTHORS   Gagliardi,M., Annesi,G., Procopio,R., Morelli,M., Iannello,G.,
            Bonapace,G., Mancini,M., Nicoletti,G. and Quattrone,A.
  TITLE     DNAJC13 mutation screening in patients with Parkinson's disease
            from South Italy
  JOURNAL   Parkinsonism Relat Disord 55, 134-137 (2018)
   PUBMED   29887357
  REMARK    GeneRIF: This study showed the DNAJC13 mutation screening in
            patients with Parkinson's disease.
REFERENCE   6  (residues 1 to 2243)
  AUTHORS   Girard,M., Poupon,V., Blondeau,F. and McPherson,P.S.
  TITLE     The DnaJ-domain protein RME-8 functions in endosomal trafficking
  JOURNAL   J Biol Chem 280 (48), 40135-40143 (2005)
   PUBMED   16179350
  REMARK    GeneRIF: RME-8 functions in intracellular trafficking and provides
            the first evidence of a functional role for a DnaJ domain-bearing
            co-chaperone on endosomes
REFERENCE   7  (residues 1 to 2243)
  AUTHORS   Foster,L.J., Zeemann,P.A., Li,C., Mann,M., Jensen,O.N. and
            Kassem,M.
  TITLE     Differential expression profiling of membrane proteins by
            quantitative proteomics in a human mesenchymal stem cell line
            undergoing osteoblast differentiation
  JOURNAL   Stem Cells 23 (9), 1367-1377 (2005)
   PUBMED   16210410
REFERENCE   8  (residues 1 to 2243)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 2243)
  AUTHORS   Chang,H.C., Hull,M. and Mellman,I.
  TITLE     The J-domain protein Rme-8 interacts with Hsc70 to control
            clathrin-dependent endocytosis in Drosophila
  JOURNAL   J Cell Biol 164 (7), 1055-1064 (2004)
   PUBMED   15051737
REFERENCE   10 (residues 1 to 2243)
  AUTHORS   Volz,A., Melkaoui,R., Hildebrandt,F. and Omran,H.
  TITLE     Candidate gene analysis of KIAA0678 encoding a DnaJ-like protein
            for adolescent nephronophthisis and Senior-Loken syndrome type 3
  JOURNAL   Cytogenet Genome Res 97 (3-4), 163-166 (2002)
   PUBMED   12438707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020633.3, AY779857.1 and
            AI189887.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 17, 2006 this sequence version replaced NP_056083.2.
            
            Summary: This gene encodes a member of the Dnaj protein family
            whose members act as co-chaperones of a partner heat-shock protein
            by binding to the latter and stimulating ATP hydrolysis. The
            encoded protein associates with the heat-shock protein Hsc70 and
            plays a role in clathrin-mediated endocytosis. It may also be
            involved in post-endocytic transport mechanisms via its
            associations with other proteins, including the sorting nexin SNX1.
            Mutations in this gene are associated with Parkinson's disease.
            [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. It encodes
            isoform 2, which is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.120148.1,
                                           SRR1803613.137071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260818.11/ ENSP00000260818.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.1"
     Protein         1..2243
                     /product="dnaJ homolog subfamily C member 13 isoform 2"
                     /note="dnaJ homolog subfamily C member 13; DnaJ
                     domain-containing protein RME-8; required for
                     receptor-mediated endocytosis 8; DnaJ (Hsp40) homolog,
                     subfamily C, member 13"
                     /calculated_mol_wt=254285
     Region          1..453
                     /region_name="Involved in membrane association.
                     /evidence=ECO:0000269|PubMed:18256511"
                     /note="propagated from UniProtKB/Swiss-Prot (O75165.5)"
     Region          12..831
                     /region_name="RME-8_N"
                     /note="DNAJ protein RME-8 N-terminal; pfam19432"
                     /db_xref="CDD:466078"
     Site            84
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75165.5)"
     Region          976..1026
                     /region_name="GYF_2"
                     /note="GYF domain 2; pfam14237"
                     /db_xref="CDD:464112"
     Region          1301..1354
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(1332..1334,1340,1343..1344,1347..1348)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     CDS             1..2243
                     /gene="DNAJC13"
                     /gene_synonym="PARK21; RME8"
                     /coded_by="NM_015268.4:273..7004"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33857.1"
                     /db_xref="GeneID:23317"
                     /db_xref="HGNC:HGNC:30343"
                     /db_xref="MIM:614334"
ORIGIN      
        1 mniirenkdl acfyttkhsw rgkykrvfsv gthaittynp ntlevtnqwp ygdicsispv
       61 gkgqgtefnl tfrkgsgkks etlkfstehr telltealrf rtdfsegkit grryncykhh
      121 wsdsrkpvil evtpggfdqi npatnrvlcs ydyrniegfv dlsdyqggfc ilyggfsrlh
      181 lfaseqreei iksaidhagn yigislrirk eplefeqyln lrfgkystde sitslaefvv
      241 qkisprhsep vkrvlaltet clverdpaty niatlkplge vfalvcdsen pqlftiefik
      301 gqvrkysste rdsllaslld gvrasgnrdv cvkmtpthkg qrwgllsmpv deeveslhlr
      361 flatppngnf adavfrfnan isysgvlhav tqdglfsenk eklinnaita llsqegdvva
      421 snaelesqfq avrrlvaska gflaftqlpk frerlgvkvv kalkrsnngi ihaavdmlca
      481 lmcpmhddyd lrqeqlnkas llsskkflen llekfnshvd hgtgalviss lldfltfalc
      541 apysettegq qfdmllemva sngrtlfklf qhpsmaiikg aglvmkaiie egdkeiatkm
      601 qelalsegal prhlhtamft issdqrmltn rqlsrhlvgl wtadnatatn llkrilppgl
      661 laylessdlv pekdadrmhv rdnvkiamdq ygkfnkvpew qrlagkaake vekfakekvd
      721 lvlmhwrdrm giaqkeninq kpvvlrkrrq rikieanwdl fyyrfgqdha rsnliwnfkt
      781 reelkdtles emrafnidre lgsanviswn hhefevkyec laeeikigdy ylrllleede
      841 neesgsikrs yeffnelyhr flltpkvnmk clclqalaiv ygrcheeigp ftdtryiigm
      901 lerctdkler drlilflnkl ilnkknvkdl mdsngirilv dlltlahlhv sratvplqsn
      961 vieaapdmkr esekewyfgn adkersgpyg fhemqelwtk gmlnaktrcw aqgmdgwrpl
     1021 qsipqlkwcl lasgqavlne tdlatlilnm litmcgyfps rdqdnaiirp lpkvkrllsd
     1081 stclphiiql lltfdpilve kvaillyhim qdnpqlprly lsgvfffimm ytgsnvlpva
     1141 rflkythtkq afkseetkgq difqrsilgh ilpeamvcyl enyepekfse iflgefdtpe
     1201 aiwssemrrl miekiaahla dftprlqsnt ralyqycpip iinypqlene lfcniyylkq
     1261 lcdtlrfpdw pikdpvkllk dtldawkkev ekkppmmsid dayevlnlpq gqgphdeski
     1321 rkayfrlaqk yhpdknpegr dmfekvnkay eflctksaki vdgpdpenii lilktqsilf
     1381 nrhkedlqpy kyagypmlir titmetsddl lfskespllp aatelafhtv ncsalnaeel
     1441 rrenglevlq eafsrcvavl traskpsdms vqvcgyiskc ysvaaqfeec rekitempsi
     1501 ikdlcrvlyf gksiprvaal gvecvssfav dfwlqthlfq agilwyllgf lfnydytlee
     1561 sgiqkseetn qqevanslak lsvhalsrlg gylaeeqatp enptirksla gmltpyvark
     1621 lavasvteil kmlnsntesp yliwnnstra elleflesqq enmikkgdcd ktygsefvys
     1681 dhakelivge ifvrvynevp tfqlevpkaf aaslldyigs qaqylhtfma ithaakvese
     1741 qhgdrlprve malealrnvi kynpgsesec ighfklifsl lrvhgagqvq qlalevvniv
     1801 tsnqdcvnni aesmvlssll allhslpssr qlvletlyal tsstkiikea makgaliyll
     1861 dmfcnsthpq vraqtaelfa kmtadkligp kvritlmkfl psvfmdamrd npeaavhife
     1921 gthenpeliw ndnsrdkvst tvremmlehf knqqdnpean wklpedfavv fgeaegelav
     1981 ggvflrifia qpawvlrkpr efliallekl telleknnph getletltma tvclfsaqpq
     2041 ladqvpplgh lpkviqamnh rnnaipksai rvihalsene lcvramasle tigplmngmk
     2101 kradtvglac eainrmfqke qselvaqalk adlvpyllkl legiglenld spaatkaqiv
     2161 kalkamtrsl qygeqvneil crssvwsafk dqkhdlfise sqtagyltgp gvagyltagt
     2221 stsvmsnlpp pvdheagdlg yqt
//
LOCUS       NP_149038                512 aa            linear   PRI 27-APR-2025
DEFINITION  mucin-13 precursor [Homo sapiens].
ACCESSION   NP_149038 NP_060118
VERSION     NP_149038.3
DBSOURCE    REFSEQ: accession NM_033049.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Kang,Q., Tingting,W., Bingzi,D., Hao,Z., Yuwei,X., Chuandong,S. and
            Chengzhan,Z.
  TITLE     GCNT3 regulated MUC13 to promote the development of hepatocellular
            carcinoma through the GSK3beta/beta-catenin pathway
  JOURNAL   Dig Liver Dis 56 (9), 1572-1581 (2024)
   PUBMED   38369410
  REMARK    GeneRIF: GCNT3 regulated MUC13 to promote the development of
            hepatocellular carcinoma through the GSK3beta/beta-catenin pathway.
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Segui-Perez,C., Stapels,D.A.C., Ma,Z., Su,J., Passchier,E.,
            Westendorp,B., Wubbolts,R.W., Wu,W., van Putten,J.P.M. and
            Strijbis,K.
  TITLE     MUC13 negatively regulates tight junction proteins and intestinal
            epithelial barrier integrity via protein kinase C
  JOURNAL   J Cell Sci 137 (5) (2024)
   PUBMED   38345099
  REMARK    GeneRIF: MUC13 negatively regulates tight junction proteins and
            intestinal epithelial barrier integrity via protein kinase C.
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Doxtater,K., Tripathi,M.K., Sekhri,R., Hafeez,B.B., Khan,S.,
            Zafar,N., Behrman,S.W., Yallapu,M.M., Jaggi,M. and Chauhan,S.C.
  TITLE     MUC13 drives cancer aggressiveness and metastasis through the
            YAP1-dependent pathway
  JOURNAL   Life Sci Alliance 6 (12), e202301975 (2023)
   PUBMED   37793774
  REMARK    GeneRIF: MUC13 drives cancer aggressiveness and metastasis through
            the YAP1-dependent pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Cai,T., Peng,B., Hu,J. and He,Y.
  TITLE     Long noncoding RNA BBOX1-AS1 promotes the progression of gastric
            cancer by regulating the miR-361-3p/Mucin 13 signaling axis
  JOURNAL   Bioengineered 13 (5), 13407-13421 (2022)
   PUBMED   36700475
  REMARK    GeneRIF: Long noncoding RNA BBOX1-AS1 promotes the progression of
            gastric cancer by regulating the miR-361-3p/Mucin 13 signaling
            axis.
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Gupta,B.K., Maher,D.M., Ebeling,M.C., Sundram,V., Koch,M.D.,
            Lynch,D.W., Bohlmeyer,T., Watanabe,A., Aburatani,H., Puumala,S.E.,
            Jaggi,M. and Chauhan,S.C.
  TITLE     Increased expression and aberrant localization of mucin 13 in
            metastatic colon cancer
  JOURNAL   J Histochem Cytochem 60 (11), 822-831 (2012)
   PUBMED   22914648
  REMARK    GeneRIF: Metastatic colon cancer and liver metastasis tissue
            samples demonstrated significantly (p<0.05) higher cytoplasmic and
            nuclear MUC13 expression compared with non-metastatic colon cancer
            and adjacent normal colon samples.
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Chauhan,S.C., Ebeling,M.C., Maher,D.M., Koch,M.D., Watanabe,A.,
            Aburatani,H., Lio,Y. and Jaggi,M.
  TITLE     MUC13 mucin augments pancreatic tumorigenesis
  JOURNAL   Mol Cancer Ther 11 (1), 24-33 (2012)
   PUBMED   22027689
  REMARK    GeneRIF: MUC13 overexpression caused a significant increase in cell
            motility, invasion, proliferation, and anchorage-dependent or
            -independent clonogenicity while decreasing cell-cell and
            cell-substratum adhesion in pancreatic cancer.
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Maher,D.M., Gupta,B.K., Nagata,S., Jaggi,M. and Chauhan,S.C.
  TITLE     Mucin 13: structure, function, and potential roles in cancer
            pathogenesis
  JOURNAL   Mol Cancer Res 9 (5), 531-537 (2011)
   PUBMED   21450906
  REMARK    GeneRIF: The various functional domains of MUC13 may confer
            oncogenic potential to MUC13
            Review article
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Samuels,T.L., Handler,E., Syring,M.L., Pajewski,N.M., Blumin,J.H.,
            Kerschner,J.E. and Johnston,N.
  TITLE     Mucin gene expression in human laryngeal epithelia: effect of
            laryngopharyngeal reflux
  JOURNAL   Ann Otol Rhinol Laryngol 117 (9), 688-695 (2008)
   PUBMED   18834073
  REMARK    GeneRIF: Reflux laryngitis is associated with down-regulation of
            mucin gene expression.
REFERENCE   9  (residues 1 to 512)
  AUTHORS   Shimamura,T., Ito,H., Shibahara,J., Watanabe,A., Hippo,Y.,
            Taniguchi,H., Chen,Y., Kashima,T., Ohtomo,T., Tanioka,F.,
            Iwanari,H., Kodama,T., Kazui,T., Sugimura,H., Fukayama,M. and
            Aburatani,H.
  TITLE     Overexpression of MUC13 is associated with intestinal-type gastric
            cancer
  JOURNAL   Cancer Sci 96 (5), 265-273 (2005)
   PUBMED   15904467
  REMARK    GeneRIF: MUC13 is a good differentiation marker for
            gastrointestinal mucosa
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Williams,S.J., Wreschner,D.H., Tran,M., Eyre,H.J., Sutherland,G.R.
            and McGuckin,M.A.
  TITLE     Muc13, a novel human cell surface mucin expressed by epithelial and
            hemopoietic cells
  JOURNAL   J Biol Chem 276 (21), 18327-18336 (2001)
   PUBMED   11278439
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA428072.1, AB035807.1, AK000070.1 and AF286113.1.
            
            On Oct 15, 2010 this sequence version replaced NP_149038.2.
            
            Summary: Epithelial mucins, such as MUC13, are a family of secreted
            and cell surface glycoproteins expressed by ductal and glandular
            epithelial tissues (Williams et al., 2001 [PubMed
            11278439]).[supplied by OMIM, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB035807.1, AY358831.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144835, SAMEA2161836
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000616727.4/ ENSP00000485028.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.2"
     Protein         1..512
                     /product="mucin-13 precursor"
                     /note="down-regulated in colon cancer 1; mucin 13,
                     epithelial transmembrane; mucin-13"
                     /calculated_mol_wt=52700
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1922
     Region          2..>122
                     /region_name="PRK11907"
                     /note="bifunctional 2',3'-cyclic-nucleotide
                     2'-phosphodiesterase/3'-nucleotidase"
                     /db_xref="CDD:237019"
     mat_peptide     19..512
                     /product="Mucin-13. /id=PRO_0000019284"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3R2.3)"
                     /calculated_mol_wt=52700
     Region          22..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3R2.3)"
     Region          133..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3R2.3)"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3R2.3)"
     Site            169
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3R2.3)"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3R2.3)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3R2.3)"
     Region          214..314
                     /region_name="SEA"
                     /note="SEA domain; pfam01390"
                     /db_xref="CDD:460188"
     Site            284
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3R2.3)"
     Site            332
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3R2.3)"
     Site            422..442
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3R2.3)"
     Region          493..512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3R2.3)"
     CDS             1..512
                     /gene="MUC13"
                     /gene_synonym="DRCC1; MUC-13"
                     /coded_by="NM_033049.4:40..1578"
                     /db_xref="CCDS:CCDS33839.2"
                     /db_xref="GeneID:56667"
                     /db_xref="HGNC:HGNC:7511"
                     /db_xref="MIM:612181"
ORIGIN      
        1 mkaiihltll allsvntatn qgnsadavtt tetatsgptv aaadttetnf petasttant
       61 psfptatspa ppiisthsss tiptpappii sthssstipi ptaadsestt nvnslatsdi
      121 itasspndgl itmvpsetqs nnemsptted nqssgpptgt alletstlns tgpsnpcqdd
      181 pcadnslcvk lhntsfclcl egyyynsstc kkgkvfpgki svtvsetfdp eekhsmayqd
      241 lhseitslfk dvfgtsvygq tviltvstsl sprsemradd kfvnvtivti laettsdnek
      301 tvtekinkai rssssnflny dltlrcdyyg cnqtaddcln glacdcksdl qrpnpqspfc
      361 vasslkcpda cnaqhkqcli kksggapeca cvpgyqedan gncqkcafgy sgldckdkfq
      421 liltivgtia givilsmiia livtarsnnk tkhieeenli dedfqnlklr stgftnlgae
      481 gsvfpkvrit asrdsqmqnp ysrhssmprp dy
//
LOCUS       NP_067347                309 aa            linear   ROD 27-APR-2025
DEFINITION  SERTA domain-containing protein 2 isoform 1 [Mus musculus].
ACCESSION   NP_067347
VERSION     NP_067347.2
DBSOURCE    REFSEQ: accession NM_021372.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Chen,C., Deng,Y., Hu,X., Ren,H., Zhu,J., Fu,S., Xie,J. and Peng,Y.
  TITLE     miR-128-3p regulates 3T3-L1 adipogenesis and lipolysis by targeting
            Pparg and Sertad2
  JOURNAL   J Physiol Biochem 74 (3), 381-393 (2018)
   PUBMED   29654510
  REMARK    GeneRIF: Data suggest that expression of microRNA-128-3p is
            down-regulated during adipogenesis; an abundance of microRNA-128-3p
            appears to down-regulate adipogenesis and up-regulate lipolysis in
            adipocytes by targeting expression of Pparg (peroxisome
            proliferator-activated receptor gamma) and Sertad2 (SERTA
            domain-containing protein-2).
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Qiang,G., Whang Kong,H., Gil,V. and Liew,C.W.
  TITLE     Transcription regulator TRIP-Br2 mediates ER stress-induced brown
            adipocytes dysfunction
  JOURNAL   Sci Rep 7, 40215 (2017)
   PUBMED   28067333
  REMARK    GeneRIF: Study demonstrates a role for TRIP-Br2 in endoplasmic
            reticulum stress-induced brown adipose tissue (BAT) dysfunction,
            and inhibiting TRIP-Br2 could be a potential approach for
            counteracting obesity-induced BAT dysfunction.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Qiang,G., Kong,H.W., Fang,D., McCann,M., Yang,X., Du,G., Bluher,M.,
            Zhu,J. and Liew,C.W.
  TITLE     The obesity-induced transcriptional regulator TRIP-Br2 mediates
            visceral fat endoplasmic reticulum stress-induced inflammation
  JOURNAL   Nat Commun 7, 11378 (2016)
   PUBMED   27109496
  REMARK    GeneRIF: Transcription factor GATA3 is responsible for the ER
            stress-induced TRIP-Br2 expression in visceral fat.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Thompson,C.L., Ng,L., Menon,V., Martinez,S., Lee,C.K.,
            Glattfelder,K., Sunkin,S.M., Henry,A., Lau,C., Dang,C.,
            Garcia-Lopez,R., Martinez-Ferre,A., Pombero,A., Rubenstein,J.L.R.,
            Wakeman,W.B., Hohmann,J., Dee,N., Sodt,A.J., Young,R., Smith,K.,
            Nguyen,T.N., Kidney,J., Kuan,L., Jeromin,A., Kaykas,A., Miller,J.,
            Page,D., Orta,G., Bernard,A., Riley,Z., Smith,S., Wohnoutka,P.,
            Hawrylycz,M.J., Puelles,L. and Jones,A.R.
  TITLE     A high-resolution spatiotemporal atlas of gene expression of the
            developing mouse brain
  JOURNAL   Neuron 83 (2), 309-323 (2014)
   PUBMED   24952961
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Peng,Y., Zhao,S., Song,L., Wang,M. and Jiao,K.
  TITLE     Sertad1 encodes a novel transcriptional co-activator of SMAD1 in
            mouse embryonic hearts
  JOURNAL   Biochem Biophys Res Commun 441 (4), 751-756 (2013)
   PUBMED   24211589
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Sim,K.G., Cheong,J.K. and Hsu,S.I.
  TITLE     The TRIP-Br family of transcriptional regulators is essential for
            the execution of cyclin E-mediated cell cycle progression
  JOURNAL   Cell Cycle 5 (10), 1111-1115 (2006)
   PUBMED   16721052
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Watanabe-Fukunaga,R., Iida,S., Shimizu,Y., Nagata,S. and
            Fukunaga,R.
  TITLE     SEI family of nuclear factors regulates p53-dependent
            transcriptional activation
  JOURNAL   Genes Cells 10 (8), 851-860 (2005)
   PUBMED   16098148
REFERENCE   8  (residues 1 to 309)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
REFERENCE   9  (residues 1 to 309)
  AUTHORS   Fuchs,S., Resch,K., Thiel,C., Ulbrich,M., Platzer,M., Jockusch,H.
            and Schmitt-John,T.
  TITLE     Comparative transcription map of the wobbler critical region on
            mouse chromosome 11 and the homologous region on human chromosome
            2p13-14
  JOURNAL   BMC Genet 3, 14 (2002)
   PUBMED   12174196
REFERENCE   10 (residues 1 to 309)
  AUTHORS   Hsu,S.I., Yang,C.M., Sim,K.G., Hentschel,D.M., O'Leary,E. and
            Bonventre,J.V.
  TITLE     TRIP-Br: a novel family of PHD zinc finger- and
            bromodomain-interacting proteins that regulate the transcriptional
            activity of E2F-1/DP-1
  JOURNAL   EMBO J 20 (9), 2273-2285 (2001)
   PUBMED   11331592
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK147674.1, AK142268.1 and AL663115.11.
            
            On Jan 6, 2006 this sequence version replaced NP_067347.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB041541.1, SRR9219382.73762.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 13.03 cM"
     Protein         1..309
                     /product="SERTA domain-containing protein 2 isoform 1"
                     /note="SERTA domain-containing protein 2; PHD zinc finger-
                     and bromodomain-interacting protein 2; transcriptional
                     regulator interacting with the PHD-bromodomain 2"
                     /calculated_mol_wt=33181
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJG5.2)"
     Region          40..75
                     /region_name="SERTA"
                     /note="SERTA motif; pfam06031"
                     /db_xref="CDD:461806"
     Region          79..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJG5.2)"
     Region          175..220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJG5.2)"
     Region          230..306
                     /region_name="Required for transactivation activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJG5.2)"
     Region          233..238
                     /region_name="Nuclear export signal (NES).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJG5.2)"
     CDS             1..309
                     /gene="Sertad2"
                     /gene_synonym="Kiaa0127; mKIAA0127; MNCb-1504; SEI-2;
                     Sei2; TRIP-Br2"
                     /coded_by="NM_021372.3:600..1529"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS24458.1"
                     /db_xref="GeneID:58172"
                     /db_xref="MGI:MGI:1931026"
ORIGIN      
        1 mlgkggkrkf dehedglegk ivspsdgpsr vsytlqrqti fnislmklyn hrpltepslq
       61 ktvlinnmlr riqeelkqeg slrpaftpss qpsnslsdsy qeapppaphp cdlgsttple
      121 acltpaslle ddnddtfctl qavhpaaptr lssaalpaek dsfssaldei eelcptstst
      181 eaahtaapeg pkgtssessv qkpegpeegr tddsrfmdsl pgnfeittst gfltdltldd
      241 ilfadidtsm ydfdpctsas gtaskmapvs addllktlap ysnqpvapsq pfkmdlteld
      301 himevlvgs
//
LOCUS       NP_001356869             643 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001356869
VERSION     NP_001356869.1
DBSOURCE    REFSEQ: accession NM_001369940.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.5596.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..643
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 9"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=73067
     Region          355..394
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..643
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369940.1:483..2414"
                     /note="isoform 9 is encoded by transcript variant 23"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mqkrlhrsvf ltflrmsthk eskdhfisps afgeilynnf lfdipkildl cvlfgkgnsp
       61 llqkmignif tqqpsyysdl detlptilqv fsnilqhcgl qgdganttpq kleergrltp
      121 sdmpllelkd ivlylcdtct tlwafldifp lacqtfqkhd fcyrlasfye aaipemesai
      181 kkrrledskl lgdlwqrlsh srkklmeifh iilnqicllp ilesscdniq gfieeflqif
      241 ssllqekrfl rdydalfpva edisllqqas svldetrtay ilqavesawe gvdrrkatda
      301 kdpsvieepn gepngvtvta eavsqasshp enseeeecmg aaaavgpamc gveldslisq
      361 vkdllpdlge gfilacleyy hydpeqvinn ileerlaptl sqldrnldre mkpdptpllt
      421 srhnvfqnde fdvfsrdsvd lsrvhkgkst rkeentrsll ndkravaaqr qryeqysvvv
      481 eevplqpges lpyhsvyyed eyddtydgnq vgandadsdd elisrrpfti pqvlrtkvpr
      541 egqeedddde eddadeeapk pdhfvqdpav lrekaearrm aflakkgyrh dsstavagsp
      601 rghgqsrett qerrkkeank atranhnrrt madrkrskgm ips
//
LOCUS       NP_001355963             495 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 9 isoform 4 [Homo sapiens].
ACCESSION   NP_001355963 XP_016884856
VERSION     NP_001355963.1
DBSOURCE    REFSEQ: accession NM_001369034.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Ma,X., Yan,W., Xu,P., Ma,L., Zan,Y., Huang,L., Wang,G., Liu,L. and
            Hui,W.
  TITLE     LncRNA-p21 suppresses cell proliferation and induces apoptosis in
            gastric cancer by sponging miR-514b-3p and up-regulating ARHGEF9
            expression
  JOURNAL   Biol Chem 403 (10), 945-958 (2022)
   PUBMED   35947460
  REMARK    GeneRIF: LncRNA-p21 suppresses cell proliferation and induces
            apoptosis in gastric cancer by sponging miR-514b-3p and
            up-regulating ARHGEF9 expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Yang,H., Liao,H., Gan,S., Xiao,T. and Wu,L.
  TITLE     ARHGEF9 gene variant leads to developmental and epileptic
            encephalopathy: Genotypic phenotype analysis and treatment
            exploration
  JOURNAL   Mol Genet Genomic Med 10 (7), e1967 (2022)
   PUBMED   35638461
  REMARK    GeneRIF: ARHGEF9 gene variant leads to developmental and epileptic
            encephalopathy: Genotypic phenotype analysis and treatment
            exploration.
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Hines,D.J., Contreras,A., Garcia,B., Barker,J.S., Boren,A.J.,
            Moufawad El Achkar,C., Moss,S.J. and Hines,R.M.
  TITLE     Human ARHGEF9 intellectual disability syndrome is phenocopied by a
            mutation that disrupts collybistin binding to the GABAA receptor
            alpha2 subunit
  JOURNAL   Mol Psychiatry 27 (3), 1729-1741 (2022)
   PUBMED   35169261
  REMARK    GeneRIF: Human ARHGEF9 intellectual disability syndrome is
            phenocopied by a mutation that disrupts collybistin binding to the
            GABAA receptor alpha2 subunit.
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Ghesh,L., Besnard,T., Nizon,M., Trochu,E., Landeau-Trottier,G.,
            Breheret,F., Thauvin-Robinet,C., Bruel,A.L., Kuentz,P., Coubes,C.,
            Cuisset,L., Mignot,C., Keren,B., Bezieau,S. and Cogne,B.
  TITLE     Loss-of-function variants in ARHGEF9 are associated with an
            X-linked intellectual disability dominant disorder
  JOURNAL   Hum Mutat 42 (5), 498-505 (2021)
   PUBMED   33600053
  REMARK    GeneRIF: Loss-of-function variants in ARHGEF9 are associated with
            an X-linked intellectual disability dominant disorder.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Scala,M., Zonneveld-Huijssoon,E., Brienza,M., Mecarelli,O., van der
            Hout,A.H., Zambrelli,E., Turner,K., Zara,F., Peron,A., Vignoli,A.
            and Striano,P.
  TITLE     De novo ARHGEF9 missense variants associated with
            neurodevelopmental disorder in females: expanding the genotypic and
            phenotypic spectrum of ARHGEF9 disease in females
  JOURNAL   Neurogenetics 22 (1), 87-94 (2021)
   PUBMED   32939676
  REMARK    GeneRIF: De novo ARHGEF9 missense variants associated with
            neurodevelopmental disorder in females: expanding the genotypic and
            phenotypic spectrum of ARHGEF9 disease in females.
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Harrington,A.W., Kim,J.Y. and Yoon,S.O.
  TITLE     Activation of Rac GTPase by p75 is necessary for c-jun N-terminal
            kinase-mediated apoptosis
  JOURNAL   J Neurosci 22 (1), 156-166 (2002)
   PUBMED   11756498
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Grosskreutz,Y., Hermann,A., Kins,S., Fuhrmann,J.C., Betz,H. and
            Kneussel,M.
  TITLE     Identification of a gephyrin-binding motif in the GDP/GTP exchange
            factor collybistin
  JOURNAL   Biol Chem 382 (10), 1455-1462 (2001)
   PUBMED   11727829
  REMARK    GeneRIF: Here we identified residues critical for interaction with
            gephyrin in the linker region between the SH3 and the DH domains of
            collybistin.
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Kins,S., Betz,H. and Kirsch,J.
  TITLE     Collybistin, a newly identified brain-specific GEF, induces
            submembrane clustering of gephyrin
  JOURNAL   Nat Neurosci 3 (1), 22-29 (2000)
   PUBMED   10607391
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Reid,T., Bathoorn,A., Ahmadian,M.R. and Collard,J.G.
  TITLE     Identification and characterization of hPEM-2, a guanine nucleotide
            exchange factor specific for Cdc42
  JOURNAL   J Biol Chem 274 (47), 33587-33593 (1999)
   PUBMED   10559246
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Balint,B. and Thomas,R.
  TITLE     Hereditary Hyperekplexia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL451106.9, AL355142.11 and
            AL391277.16.
            
            On Mar 14, 2019 this sequence version replaced XP_016884856.1.
            
            Summary: The protein encoded by this gene is a Rho-like GTPase that
            switches between the active (GTP-bound) state and inactive
            (GDP-bound) state to regulate CDC42 and other genes. This
            brain-specific protein also acts as an adaptor protein for the
            recruitment of gephyrin and together these proteins facilitate
            receceptor recruitement in GABAnergic and glycinergic synapses.
            Defects in this gene are the cause of startle disease with epilepsy
            (STHEE), also known as hyperekplexia with epilepsy, as well as
            several other types of cognitive disability. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.30822.1,
                                           SRR1803611.265620.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq11.1"
     Protein         1..495
                     /product="rho guanine nucleotide exchange factor 9 isoform
                     4"
                     /note="hPEM-2 collybistin; rho guanine nucleotide exchange
                     factor 9; PEM-2 homolog; rac/Cdc42 guanine nucleotide
                     exchange factor 9; Cdc42 guanine nucleotide exchange
                     factor (GEF) 9"
                     /calculated_mol_wt=58611
     Region          <1..47
                     /region_name="SH3_ARHGEF9"
                     /note="Src homology 3 domain of the Rho guanine nucleotide
                     exchange factor ARHGEF9; cd11975"
                     /db_xref="CDD:212908"
     Region          86..265
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; smart00325"
                     /db_xref="CDD:214619"
     Site            order(89,93,188,215..216,219..220,222..223,226..227,
                     230..231,234,260,264)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          270..409
                     /region_name="PH_Collybistin_ASEF"
                     /note="Collybistin/APC-stimulated guanine nucleotide
                     exchange factor pleckstrin homology (PH) domain; cd01224"
                     /db_xref="CDD:269931"
     CDS             1..495
                     /gene="ARHGEF9"
                     /gene_synonym="COLLYBISTIN; DEE8; EIEE8; HPEM-2; PEM-2;
                     PEM2"
                     /coded_by="NM_001369034.1:620..2107"
                     /note="isoform 4 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS83477.1"
                     /db_xref="GeneID:23229"
                     /db_xref="HGNC:HGNC:14561"
                     /db_xref="MIM:300429"
ORIGIN      
        1 manrelafka gdvikvldas nkdwwwgqid deegwfpasf vrlwvnqede veegpsdvqn
       61 ghldpnsdcl clgrplqnrd qmranvinei msterhyikh lkdicegylk qcrkrrdmfs
      121 deqlkvifgn iediyrfqmg fvrdlekqyn nddphlseig pcflehqdgf wiyseycnnh
      181 ldacmelskl mkdsryqhff eacrllqqmi diaidgfllt pvqkickypl qlaellkyta
      241 qdhsdyryva aalavmrnvt qqinerkrrl enidkiaqwq asvldweged ildrsseliy
      301 tgemawiyqp ygrnqqrvff lfdhqmvlck kdlirrdily ykgridmdky evvdiedgrd
      361 ddfnvsmkna fklhnketee ihlffakkle ekirwlrafr eerkmvqede kigfeisenq
      421 krqaamtvrk vpkqkgvnsa rsvppsyppp qdplnhgqyl vpdgiaqsqv feftepkrsq
      481 spfwqnfsrl tpfkk
//
LOCUS       NP_061041                418 aa            linear   PRI 27-APR-2025
DEFINITION  STE20-related kinase adapter protein beta isoform 1 [Homo sapiens].
ACCESSION   NP_061041
VERSION     NP_061041.2
DBSOURCE    REFSEQ: accession NM_018571.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Blandin,G., Marchand,S., Charton,K., Daniele,N., Gicquel,E.,
            Boucheteil,J.B., Bentaib,A., Barrault,L., Stockholm,D., Bartoli,M.
            and Richard,I.
  TITLE     A human skeletal muscle interactome centered on proteins involved
            in muscular dystrophies: LGMD interactome
  JOURNAL   Skelet Muscle 3 (1), 3 (2013)
   PUBMED   23414517
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Boudeau,J., Baas,A.F., Deak,M., Morrice,N.A., Kieloch,A.,
            Schutkowski,M., Prescott,A.R., Clevers,H.C. and Alessi,D.R.
  TITLE     MO25alpha/beta interact with STRADalpha/beta enhancing their
            ability to bind, activate and localize LKB1 in the cytoplasm
  JOURNAL   EMBO J 22 (19), 5102-5114 (2003)
   PUBMED   14517248
REFERENCE   8  (residues 1 to 418)
  AUTHORS   Hawley,S.A., Boudeau,J., Reid,J.L., Mustard,K.J., Udd,L.,
            Makela,T.P., Alessi,D.R. and Hardie,D.G.
  TITLE     Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and
            MO25 alpha/beta are upstream kinases in the AMP-activated protein
            kinase cascade
  JOURNAL   J Biol 2 (4), 28 (2003)
   PUBMED   14511394
REFERENCE   9  (residues 1 to 418)
  AUTHORS   Sanna,M.G., da Silva Correia,J., Luo,Y., Chuang,B., Paulson,L.M.,
            Nguyen,B., Deveraux,Q.L. and Ulevitch,R.J.
  TITLE     ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated
            activation of JNK1 and protection against apoptosis
  JOURNAL   J Biol Chem 277 (34), 30454-30462 (2002)
   PUBMED   12048196
  REMARK    GeneRIF: a novel XIAP-interacting protein that acts as a co-factor
            enhancing XIAP-mediated activation of JNK1 and the
            caspase-independent protection of XIAP against apoptosis
REFERENCE   10 (residues 1 to 418)
  AUTHORS   Hadano,S., Yanagisawa,Y., Skaug,J., Fichter,K., Nasir,J.,
            Martindale,D., Koop,B.F., Scherer,S.W., Nicholson,D.W.,
            Rouleau,G.A., Ikeda,J. and Hayden,M.R.
  TITLE     Cloning and characterization of three novel genes, ALS2CR1,
            ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis
            (ALS2) critical region at chromosome 2q33-q34: candidate genes for
            ALS2
  JOURNAL   Genomics 71 (2), 200-213 (2001)
   PUBMED   11161814
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007282.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 21, 2001 this sequence version replaced NP_061041.1.
            
            Summary: This gene encodes a protein that belongs to the
            serine/threonine protein kinase STE20 subfamily. One of the active
            site residues in the protein kinase domain of this protein is
            altered, and it is thus a pseudokinase. This protein is a component
            of a complex involved in the activation of serine/threonine kinase
            11, a master kinase that regulates cell polarity and
            energy-generating metabolism. This complex regulates the relocation
            of this kinase from the nucleus to the cytoplasm, and it is
            essential for G1 cell cycle arrest mediated by this kinase. The
            protein encoded by this gene can also interact with the X
            chromosome-linked inhibitor of apoptosis protein, and this
            interaction enhances the anti-apoptotic activity of this protein
            via the JNK1 signal transduction pathway. Two pseudogenes, located
            on chromosomes 1 and 7, have been found for this gene.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, May
            2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.130218.1,
                                           SRR1803615.39799.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000194530.8/ ENSP00000194530.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..418
                     /product="STE20-related kinase adapter protein beta
                     isoform 1"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 2; STRAD beta; pseudokinase
                     ALS2CR2; ILP-interacting protein ILPIPA; STE20-related
                     kinase adaptor beta; amyotrophic lateral sclerosis 2
                     chromosomal region candidate gene 2 protein"
                     /calculated_mol_wt=46895
     Region          59..386
                     /region_name="PK_STRAD_beta"
                     /note="Pseudokinase domain of STE20-related kinase adapter
                     protein beta; cd08226"
                     /db_xref="CDD:270864"
     Site            order(64..68,72,74,87,89,136..139,143,146,188..189,191,
                     204)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270864"
     Site            order(93..94,96..98,105,108..109,112..113,115,125..127,
                     129..130,132,174,178,212..213)
                     /site_type="other"
                     /note="MO25 interaction site [polypeptide binding]"
                     /db_xref="CDD:270864"
     Site            order(99,220,222,227,230,239..243,273..278)
                     /site_type="other"
                     /note="LKB1 interaction site [polypeptide binding]"
                     /db_xref="CDD:270864"
     CDS             1..418
                     /gene="STRADB"
                     /gene_synonym="ALS2CR2; CALS-21; ILPIP; ILPIPA; PAPK;
                     PRO1038"
                     /coded_by="NM_018571.6:295..1551"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2348.1"
                     /db_xref="GeneID:55437"
                     /db_xref="HGNC:HGNC:13205"
                     /db_xref="MIM:607333"
ORIGIN      
        1 mslldcfcts rtqveslrpe kqsetsihqy lvdeptlsws rpstrasevl cstnvshyel
       61 qveigrgfdn ltsvhlarht ptgtlvtiki tnlencneer lkalqkavil shffrhpnit
      121 tywtvftvgs wlwvispfma ygsasqllrt yfpegmsetl irnilfgavr glnylhqngc
      181 ihrsikashi lisgdglvtl sglshlhslv khgqrhravy dfpqfstsvq pwlspellrq
      241 dlhgynvksd iysvgitace lasgqvpfqd mhrtqmllqk lkgppyspld isifpqsesr
      301 mknsqsgvds gigesvlvss gthtvnsdrl htpssktfsp affslvqlcl qqdpekrpsa
      361 ssllshvffk qmkeesqdsi lsllppaynk psislppvlp wtepecdfpd ekdsywef
//
LOCUS       NP_997400               1691 aa            linear   PRI 27-APR-2025
DEFINITION  ADAMTS-like protein 3 isoform a precursor [Homo sapiens].
ACCESSION   NP_997400
VERSION     NP_997400.2
DBSOURCE    REFSEQ: accession NM_207517.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1691)
  AUTHORS   Zhou,X., Li,R., Jing,R., Zuo,B. and Zheng,Q.
  TITLE     Genome-wide CRISPR knockout screens identify ADAMTSL3 and PTEN
            genes as suppressors of HCC proliferation and metastasis,
            respectively
  JOURNAL   J Cancer Res Clin Oncol 146 (6), 1509-1521 (2020)
   PUBMED   32266537
  REMARK    GeneRIF: knocking out either the ADAMTSL3 or PTEN genes promoted
            either the proliferation or metastasis of hepatocellular carcinoma
            cells, respectively
REFERENCE   2  (residues 1 to 1691)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1691)
  AUTHORS   Jambaljav,B., Tanaka,D., Nagashima,K., Harashima,S.I., Harada,N.,
            Harada,T., Fujiwara,Y., Wang,Y., Liu,Y., Tabara,Y., Matsuda,F.,
            Koizumi,A. and Inagaki,N.
  TITLE     Whole-exome sequencing in a Japanese family with highly aggregated
            diabetes identifies a candidate susceptibility mutation in ADAMTSL3
  JOURNAL   Diabetes Res Clin Pract 135, 143-149 (2018)
   PUBMED   29162515
  REMARK    GeneRIF: A137T in ADAMTSL3 may be a susceptibility mutation for
            diabetes.
REFERENCE   4  (residues 1 to 1691)
  AUTHORS   He,M., Xu,M., Zhang,B., Liang,J., Chen,P., Lee,J.Y., Johnson,T.A.,
            Li,H., Yang,X., Dai,J., Liang,L., Gui,L., Qi,Q., Huang,J., Li,Y.,
            Adair,L.S., Aung,T., Cai,Q., Cheng,C.Y., Cho,M.C., Cho,Y.S.,
            Chu,M., Cui,B., Gao,Y.T., Go,M.J., Gu,D., Gu,W., Guo,H., Hao,Y.,
            Hong,J., Hu,Z., Hu,Y., Huang,J., Hwang,J.Y., Ikram,M.K., Jin,G.,
            Kang,D.H., Khor,C.C., Kim,B.J., Kim,H.T., Kubo,M., Lee,J., Lee,J.,
            Lee,N.R., Li,R., Li,J., Liu,J., Longe,J., Lu,W., Lu,X., Miao,X.,
            Okada,Y., Ong,R.T., Qiu,G., Seielstad,M., Sim,X., Song,H.,
            Takeuchi,F., Tanaka,T., Taylor,P.R., Wang,L., Wang,W., Wang,Y.,
            Wu,C., Wu,Y., Xiang,Y.B., Yamamoto,K., Yang,H., Liao,M., Yokota,M.,
            Young,T., Zhang,X., Kato,N., Wang,Q.K., Zheng,W., Hu,F.B., Lin,D.,
            Shen,H., Teo,Y.Y., Mo,Z., Wong,T.Y., Lin,X., Mohlke,K.L., Ning,G.,
            Tsunoda,T., Han,B.G., Shu,X.O., Tai,E.S., Wu,T. and Qi,L.
  TITLE     Meta-analysis of genome-wide association studies of adult height in
            East Asians identifies 17 novel loci
  JOURNAL   Hum Mol Genet 24 (6), 1791-1800 (2015)
   PUBMED   25429064
REFERENCE   5  (residues 1 to 1691)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   6  (residues 1 to 1691)
  AUTHORS   Weedon,M.N., Lango,H., Lindgren,C.M., Wallace,C., Evans,D.M.,
            Mangino,M., Freathy,R.M., Perry,J.R., Stevens,S., Hall,A.S.,
            Samani,N.J., Shields,B., Prokopenko,I., Farrall,M., Dominiczak,A.,
            Johnson,T., Bergmann,S., Beckmann,J.S., Vollenweider,P.,
            Waterworth,D.M., Mooser,V., Palmer,C.N., Morris,A.D.,
            Ouwehand,W.H., Zhao,J.H., Li,S., Loos,R.J., Barroso,I.,
            Deloukas,P., Sandhu,M.S., Wheeler,E., Soranzo,N., Inouye,M.,
            Wareham,N.J., Caulfield,M., Munroe,P.B., Hattersley,A.T.,
            McCarthy,M.I. and Frayling,T.M.
  CONSRTM   Diabetes Genetics Initiative; Wellcome Trust Case Control
            Consortium; Cambridge GEM Consortium
  TITLE     Genome-wide association analysis identifies 20 loci that influence
            adult height
  JOURNAL   Nat Genet 40 (5), 575-583 (2008)
   PUBMED   18391952
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 1691)
  AUTHORS   Gudbjartsson,D.F., Walters,G.B., Thorleifsson,G., Stefansson,H.,
            Halldorsson,B.V., Zusmanovich,P., Sulem,P., Thorlacius,S.,
            Gylfason,A., Steinberg,S., Helgadottir,A., Ingason,A.,
            Steinthorsdottir,V., Olafsdottir,E.J., Olafsdottir,G.H.,
            Jonsson,T., Borch-Johnsen,K., Hansen,T., Andersen,G., Jorgensen,T.,
            Pedersen,O., Aben,K.K., Witjes,J.A., Swinkels,D.W., den Heijer,M.,
            Franke,B., Verbeek,A.L., Becker,D.M., Yanek,L.R., Becker,L.C.,
            Tryggvadottir,L., Rafnar,T., Gulcher,J., Kiemeney,L.A., Kong,A.,
            Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Many sequence variants affecting diversity of adult human height
  JOURNAL   Nat Genet 40 (5), 609-615 (2008)
   PUBMED   18391951
REFERENCE   8  (residues 1 to 1691)
  AUTHORS   Lettre,G., Jackson,A.U., Gieger,C., Schumacher,F.R., Berndt,S.I.,
            Sanna,S., Eyheramendy,S., Voight,B.F., Butler,J.L., Guiducci,C.,
            Illig,T., Hackett,R., Heid,I.M., Jacobs,K.B., Lyssenko,V., Uda,M.,
            Boehnke,M., Chanock,S.J., Groop,L.C., Hu,F.B., Isomaa,B., Kraft,P.,
            Peltonen,L., Salomaa,V., Schlessinger,D., Hunter,D.J., Hayes,R.B.,
            Abecasis,G.R., Wichmann,H.E., Mohlke,K.L. and Hirschhorn,J.N.
  CONSRTM   Diabetes Genetics Initiative; FUSION; KORA; Prostate, Lung
            Colorectal and Ovarian Cancer Screening Trial; Nurses' Health
            Study; SardiNIA
  TITLE     Identification of ten loci associated with height highlights new
            biological pathways in human growth
  JOURNAL   Nat Genet 40 (5), 584-591 (2008)
   PUBMED   18391950
REFERENCE   9  (residues 1 to 1691)
  AUTHORS   Koo,B.H., Hurskainen,T., Mielke,K., Aung,P.P., Casey,G.,
            Autio-Harmainen,H. and Apte,S.S.
  TITLE     ADAMTSL3/punctin-2, a gene frequently mutated in colorectal tumors,
            is widely expressed in normal and malignant epithelial cells,
            vascular endothelial cells and other cell types, and its mRNA is
            reduced in colon cancer
  JOURNAL   Int J Cancer 121 (8), 1710-1716 (2007)
   PUBMED   17597111
  REMARK    GeneRIF: ADAMTSL3 is expressed in numerous tissues, suggesting a
            broader regulatory role than in colorectal epithelium alone, and
            that colorectal cancer has both structural mutations as well as
            decreased expression of ADAMTSL3.
REFERENCE   10 (residues 1 to 1691)
  AUTHORS   Hall,N.G., Klenotic,P., Anand-Apte,B. and Apte,S.S.
  TITLE     ADAMTSL-3/punctin-2, a novel glycoprotein in extracellular matrix
            related to the ADAMTS family of metalloproteases
  JOURNAL   Matrix Biol 22 (6), 501-510 (2003)
   PUBMED   14667842
  REMARK    GeneRIF: Highest expression of ADAMTSL3 was found in liver, kidney,
            heart and skeletal muscle.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF237652.1, BC128389.1, AC116157.4 and AC027807.6.
            
            On Apr 13, 2007 this sequence version replaced NP_997400.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128389.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000286744.10/ ENSP00000286744.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1691
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..1691
                     /product="ADAMTS-like protein 3 isoform a precursor"
                     /note="a disintegrin-like and metalloprotease domain with
                     thrombospondin type I motifs-like 3; punctin-2;
                     ADAMTS-like protein 3"
                     /calculated_mol_wt=185735
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2976
     mat_peptide     27..1691
                     /product="ADAMTS-like protein 3 isoform a"
                     /calculated_mol_wt=185735
     Region          78..124
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          129..227
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Site            293
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          343..401
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          422..479
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          482..534
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          570..625
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          648..703
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            681
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          707..759
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          763..819
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            797
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          825..880
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            915
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Site            927
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          <929..993
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          930..934
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          943..947
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          965..969
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          979..984
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          988..991
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            1102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          1146..1184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82987.4)"
     Site            1191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          1211..1276
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          1211..1215
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1224..1228
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1246..1250
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1260..1265
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            1292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          1293..1383
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            1316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          1317..1321
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1330..1334
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            1330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Site            1343
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Site            1349
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          1350..1354
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            1356
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          1364..1369
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1377..1380
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1428..1483
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            1432
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          1487..1544
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            1516
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Site            1574
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Site            1591
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P82987.4)"
     Region          1601..1655
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1659..1689
                     /region_name="PLAC"
                     /note="PLAC (protease and lacunin) domain; pfam08686"
                     /db_xref="CDD:462560"
     CDS             1..1691
                     /gene="ADAMTSL3"
                     /gene_synonym="ADAMTSL-3"
                     /coded_by="NM_207517.3:188..5263"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10326.1"
                     /db_xref="GeneID:57188"
                     /db_xref="HGNC:HGNC:14633"
                     /db_xref="MIM:609199"
ORIGIN      
        1 maswtspwwv ligmvfmhsp lpqttaeksp gayflpefal spqgsfledt tgeqfltyry
       61 ddqtsrntrs dedkdgnwda wgdwsdcsrt cgggasyslr rcltgrnceg qniryktcsn
      121 hdcppdaedf raqqcsaynd vqyqghyyew lpryndpaap calkchaqgq nlvvelapkv
      181 ldgtrcntds ldmcisgicq avgcdrqlgs nakedncgvc agdgstcrlv rgqskshvsp
      241 ekreenviav plgsrsvrit vkgpahlfie sktlqgskge hsfnspgvfl venttvefqr
      301 gserqtfkip gplmadfifk trytaakdsv vqfffyqpis hqwrqtdffp ctvtcgggyq
      361 lnsaecvdir lkrvvpdhyc hyypenvkpk pklkecsmdp cpssdgfkei mpydhfqplp
      421 rwehnpwtac svscgggiqr rsfvcveesm hgeilqveew kcmyapkpkv mqtcnlfdcp
      481 kwiamewsqc tvtcgrglry rvvlcinhrg ehvggcnpql klhikeecvi pipcykpkek
      541 spveaklpwl kqaqeleetr iateeptfip epwsacsttc gpgvqvrevk crvlltftqt
      601 etelpeeece gpklpterpc lleacdespa sreldiplpe dsettydwey agftpctatc
      661 vgghqeaiav clhiqtqqtv ndslcdmvhr ppamsqacnt epcpprwhvg swgpcsatcg
      721 vgiqtrdvyc lhpgetpapp eecrdekpha lqacnqfdcp pgwhieewqq csrtcgggtq
      781 nrrvtcrqll tdgsflnlsd elcqgpkass hkscartdcp phlavgdwsk csvscgvgiq
      841 rrkqvcqrla akgrriplse mmcrdlpglp lvrscqmpec skiksemktk lgeqgpqils
      901 vqrvyiqtre ekrinltigs rayllpntsv iikcpvrrfq ksliqwekdg rclqnskrlg
      961 itksgslkih glaapdigvy rciagsaqet vvlkligtdn rliarpalre pmreypgmdh
     1021 seanslgvtw hkmrqmwnnk ndlyldddhi snqpflrall ghcsnsagst nswelknkqf
     1081 eaavkqgays mdtaqfdeli rnmsqlmetg evsddlasql iyqlvaelak aqpthmqwrg
     1141 iqeetppaaq lrgetgsvsq sshaknsgkl tfkpkgpvlm rqsqppsisf nktinsrign
     1201 tvyitkrtev inilcdlitp seatytwtkd gtllqpsvki ildgtgkiqi qnptrkeqgi
     1261 yecsvanhlg sdvesssvly aeapvilsve rnitkpehnh lsvvvggive aalganvtir
     1321 cpvkgvpqpn itwlkrggsl sgnvsllfng slllqnvsle negtyvciat nalgkavats
     1381 vlhllerrwp esrivflqgh kkyilqatnt rtnsndptge pppqepfwep gnwshcsatc
     1441 ghlgariqrp qcvmangqev sealcdhlqk plagfepcni rdcparwfts vwsqcsvscg
     1501 egyhsrqvtc krtkangtvq vvspracapk drplgrkpcf ghpcvqwepg nrcpgrcmgr
     1561 avrmqqrhta cqhnssdsnc ddrkrptlrr nctsgacdvc whtgpwkpct aacgrgfqsr
     1621 kvdcihtrsc kpvakrhcvq kkkpiswrhc lgpscdrdct dtthycmfvk hlnlcsldry
     1681 kqrccqscqe g
//
LOCUS       NP_115727                306 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein mL45 isoform 1 [Homo sapiens].
ACCESSION   NP_115727 XP_941633
VERSION     NP_115727.5
DBSOURCE    REFSEQ: accession NM_032351.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Itoh,Y., Andrell,J., Choi,A., Richter,U., Maiti,P., Best,R.B.,
            Barrientos,A., Battersby,B.J. and Amunts,A.
  TITLE     Mechanism of membrane-tethered mitochondrial protein synthesis
  JOURNAL   Science 371 (6531), 846-849 (2021)
   PUBMED   33602856
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 306)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 306)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 306)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   10 (residues 1 to 306)
  AUTHORS   Koc,E.C., Burkhart,W., Blackburn,K., Moyer,M.B., Schlatzer,D.M.,
            Moseley,A. and Spremulli,L.L.
  TITLE     The large subunit of the mammalian mitochondrial ribosome. Analysis
            of the complement of ribosomal proteins present
  JOURNAL   J Biol Chem 276 (47), 43958-43969 (2001)
   PUBMED   11551941
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK293605.1 and BC006235.2.
            
            On May 10, 2014 this sequence version replaced NP_115727.4.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein. Alternative
            splicing results in multiple transcript variants. Pseudogenes
            corresponding to this gene are found on chromosomes 2p and 17q.
            [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK172741.1, SRR5189661.101169.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 11551941; reported by
                                                  MitoCarta
            MANE Ensembl match                 :: ENST00000613675.5/
                                                  ENSP00000484903.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..306
                     /product="large ribosomal subunit protein mL45 isoform 1"
                     /note="39S ribosomal protein L45, mitochondrial;
                     mitochondrial large ribosomal subunit protein mL45"
                     /calculated_mol_wt=35160
     Region          121..262
                     /region_name="Tim44"
                     /note="Tim44 is an essential component of the machinery
                     that mediates the translocation of nuclear-encoded
                     proteins across the mitochondrial inner membrane;
                     smart00978"
                     /db_xref="CDD:214950"
     Region          287..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRJ2.2)"
     CDS             1..306
                     /gene="MRPL45"
                     /gene_synonym="L45mt; Mba1; mL45; MRP-L45"
                     /coded_by="NM_032351.6:17..937"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11326.1"
                     /db_xref="GeneID:84311"
                     /db_xref="HGNC:HGNC:16651"
                     /db_xref="MIM:611850"
ORIGIN      
        1 maapipqgfs clsrflgwws rqpvlvtqsa aivpvrtkkr ftppiyqpkf ktekefmqha
       61 rkaglvippe ksdrsihlac tagifdayvp pegdarissl skeglierte rmkktmasqv
      121 sirrikdyda nfkikdfpek akdifieahl clnnsdhdrl htlvtehcfp dmtwdikykt
      181 vrwsfvesle pshvvqvrcs smmnqgnvyg qitvrmhtrq tlaiydrfgr lmygqedvpk
      241 dvleyvvfek qltnpygswr mhtkivppwa ppkqpilktv mipgpqlkpe eeyeeaqgea
      301 qkpqla
//
LOCUS       NP_005505                362 aa            linear   PRI 27-APR-2025
DEFINITION  major histocompatibility complex, class I, B precursor [Homo
            sapiens].
ACCESSION   NP_005505
VERSION     NP_005505.2
DBSOURCE    REFSEQ: accession NM_005514.8
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Adechina,A.P., Assogba,Y.P., Tchiakpe,E. and Yessoufou,A.
  TITLE     Human leukocyte antigen HLA-B*57:01 status in HIV-1 patients
            developing hypersensitivity reactions in Benin: a pilot study
  JOURNAL   BMC Res Notes 17 (1), 208 (2024)
   PUBMED   39075611
  REMARK    GeneRIF: Human leukocyte antigen HLA-B*57:01 status in HIV-1
            patients developing hypersensitivity reactions in Benin: a pilot
            study.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Kouniaki,D., Kitsiou,V. and Tsirogianni,A.
  TITLE     Characterisation of the novel HLA-B*38:01:01:18 allele by
            next-generation sequencing
  JOURNAL   HLA 103 (6), e15573 (2024)
   PUBMED   38923829
  REMARK    GeneRIF: Characterisation of the novel HLA-B*38:01:01:18 allele by
            next-generation sequencing.
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Dos Santos Angeli,R., Ribeiro,A.L., Kohem,C.L., Xavier,R.M. and
            Monticielo,O.A.
  TITLE     Comparative study of two laboratory techniques for the detection of
            HLA-B27 in patients with axial spondyloarthritis: a cross-sectional
            analysis
  JOURNAL   Adv Rheumatol 64 (1), 42 (2024)
   PUBMED   38783377
  REMARK    GeneRIF: Comparative study of two laboratory techniques for the
            detection of HLA-B27 in patients with axial spondyloarthritis: a
            cross-sectional analysis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Hu,G.F., Meng,L.B., Li,J., Xu,J., Xu,H.X. and Liu,D.P.
  TITLE     HLA-B and TIMP1 as hub genes of the ventricular remodeling caused
            by hypertension
  JOURNAL   Aging (Albany NY) 16 (9), 8260-8278 (2024)
   PUBMED   38728374
  REMARK    GeneRIF: HLA-B and TIMP1 as hub genes of the ventricular remodeling
            caused by hypertension.
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Kohansal Vajari,M., Ehsan,M., Ghiasi,S., Fooladi,S., Karami,N.,
            Hassanshahi,G. and Fatemi,A.
  TITLE     Human Leukocyte Antigen Alleles (HLA-A, HLA-B, and HLA-DRB1) are
            associated with Acute Lymphoblastic Leukemia (ALL) : A Case-Control
            Study in a Sample of Iranian Population
  JOURNAL   Asian Pac J Cancer Prev 25 (5), 1507-1513 (2024)
   PUBMED   38809622
  REMARK    GeneRIF: Human Leukocyte Antigen Alleles (HLA-A, HLA-B, and
            HLA-DRB1) are associated with Acute Lymphoblastic Leukemia (ALL) :
            A Case-Control Study in a Sample of Iranian Population.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Higgins,C.M., Lund,T., Shipley,M.E., Ebringer,A.,
            Sadowska-Wroblewska,M. and Craig,R.K.
  TITLE     Ankylosing spondylitis and HLA-B27: restriction fragment length
            polymorphism and sequencing of an HLA-B27 allele from a patient
            with ankylosing spondylitis
  JOURNAL   Ann Rheum Dis 51 (7), 855-862 (1992)
   PUBMED   1352961
  REMARK    Erratum:[Ann Rheum Dis 1993 Jan;52(1):88]
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Belich,M.P., Madrigal,J.A., Hildebrand,W.H., Zemmour,J.,
            Williams,R.C., Luz,R., Petzl-Erler,M.L. and Parham,P.
  TITLE     Unusual HLA-B alleles in two tribes of Brazilian Indians
  JOURNAL   Nature 357 (6376), 326-329 (1992)
   PUBMED   1317015
REFERENCE   8  (residues 1 to 362)
  AUTHORS   Orr,H.T., Lopez de Castro,J.A., Lancet,D. and Strominger,J.L.
  TITLE     Complete amino acid sequence of a papain-solubilized human
            histocompatibility antigen, HLA-B7. 2. Sequence determination and
            search for homologies
  JOURNAL   Biochemistry 18 (25), 5711-5720 (1979)
   PUBMED   518865
REFERENCE   9  (residues 1 to 362)
  AUTHORS   Parham,P., Alpert,B.N., Orr,H.T. and Strominger,J.L.
  TITLE     Carbohydrate moiety of HLA antigens. Antigenic properties and amino
            acid sequences around the site of glycosylation
  JOURNAL   J Biol Chem 252 (21), 7555-7567 (1977)
   PUBMED   72068
REFERENCE   10 (residues 1 to 362)
  AUTHORS   Peterson,P.A., Rask,L., Sege,K., Klareskog,L., Anundi,H. and
            Ostberg,L.
  TITLE     Evolutionary relationship between immunoglobulins and
            transplantation antigens
  JOURNAL   Proc Natl Acad Sci U S A 72 (4), 1612-1616 (1975)
   PUBMED   1055432
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC345094.1, U29057.1 and
            AW273181.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 28, 2001 this sequence version replaced NP_005505.1.
            
            Summary: HLA-B belongs to the HLA class I heavy chain paralogues.
            This class I molecule is a heterodimer consisting of a heavy chain
            and a light chain (beta-2 microglobulin). The heavy chain is
            anchored in the membrane. Class I molecules play a central role in
            the immune system by presenting peptides derived from the
            endoplasmic reticulum lumen. They are expressed in nearly all
            cells. The heavy chain is approximately 45 kDa and its gene
            contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3
            encode the alpha1 and alpha2 domains, which both bind the peptide,
            exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane
            region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms
            within exon 2 and exon 3 are responsible for the peptide binding
            specificity of each class one molecule. Typing for these
            polymorphisms is routinely done for bone marrow and kidney
            transplantation. Hundreds of HLA-B alleles have been described.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK130166.1, SRR3476690.120666.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000412585.7/ ENSP00000399168.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..362
                     /product="major histocompatibility complex, class I, B
                     precursor"
                     /note="HLA class I histocompatibility antigen, B alpha
                     chain; MHC HLA-B cell surface glycoprotein; MHC class I
                     antigen HLA-B heavy chain; MHC HLA-B transmembrane
                     glycoprotein; MHC class I antigen SHCHA; leukocyte antigen
                     class I-B; MHC class I molecule; MHC class 1 antigen; HLA
                     class I antigen HLA-B; MHC class I antigen HLA-B alpha
                     chain"
                     /calculated_mol_wt=37893
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2585
     Region          3..11
                     /region_name="VL9 epitope.
                     /evidence=ECO:0000269|PubMed:37264229"
                     /note="propagated from UniProtKB/Swiss-Prot (P01889.3)"
     mat_peptide     25..362
                     /product="major histocompatibility complex, class I, B"
                     /calculated_mol_wt=37893
     Region          25..203
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; pfam00129"
                     /db_xref="CDD:395078"
     Region          25..114
                     /region_name="Alpha-1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P01889.3)"
     Region          101..107
                     /region_name="Bw6 motif.
                     /evidence=ECO:0000269|PubMed:25480565"
                     /note="propagated from UniProtKB/Swiss-Prot (P01889.3)"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P01889.3)"
     Region          115..206
                     /region_name="Alpha-2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P01889.3)"
     Region          204..300
                     /region_name="IgC1_MHC_Ia_HLA-B"
                     /note="Class Ia major histocompatibility complex (MHC)
                     immunoglobulin domain of human leukocyte antigen (HLA) B
                     and similar proteins; member of the C1-set of Ig
                     superfamily (IgSF) domains; cd21026"
                     /db_xref="CDD:409617"
     Region          207..298
                     /region_name="Alpha-3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P01889.3)"
     Region          208..216
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409617"
     Site            order(216,226,228,230,255..256,258..261,266,268)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409617"
     Region          224..233
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409617"
     Region          237..243
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409617"
     Region          245..248
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409617"
     Region          252..260
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409617"
     Region          263..273
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409617"
     Region          280..287
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409617"
     Region          293..298
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409617"
     Region          299..309
                     /region_name="Connecting peptide. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P01889.3)"
     Site            310..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P01889.3)"
     Region          337..362
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01889.3)"
     Region          <346..362
                     /region_name="MHC_I_C"
                     /note="MHC_I C-terminus; pfam06623"
                     /db_xref="CDD:461964"
     CDS             1..362
                     /gene="HLA-B"
                     /gene_synonym="AS; B-4901; HLAB"
                     /coded_by="NM_005514.8:22..1110"
                     /db_xref="CCDS:CCDS34394.1"
                     /db_xref="GeneID:3106"
                     /db_xref="HGNC:HGNC:4932"
                     /db_xref="MIM:142830"
ORIGIN      
        1 mlvmaprtvl lllsaalalt etwagshsmr yfytsvsrpg rgeprfisvg yvddtqfvrf
       61 dsdaaspree prapwieqeg peywdrntqi ykaqaqtdre slrnlrgyyn qseagshtlq
      121 smygcdvgpd grllrghdqy aydgkdyial nedlrswtaa dtaaqitqrk weaareaeqr
      181 raylegecve wlrrylengk dkleradppk thvthhpisd heatlrcwal gfypaeitlt
      241 wqrdgedqtq dtelvetrpa gdrtfqkwaa vvvpsgeeqr ytchvqhegl pkpltlrwep
      301 ssqstvpivg ivaglavlav vvigavvaav mcrrkssggk ggsysqaacs dsaqgsdvsl
      361 ta
//
LOCUS       NP_443730                327 aa            linear   PRI 27-APR-2025
DEFINITION  guanine nucleotide-binding protein subunit beta-like protein 1
            [Homo sapiens].
ACCESSION   NP_443730 NP_066992 NP_071891
VERSION     NP_443730.1
DBSOURCE    REFSEQ: accession NM_053004.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Huang,M., Yao,F., Nie,L., Wang,C., Su,D., Zhang,H., Li,S., Tang,M.,
            Feng,X., Yu,B., Chen,Z., Wang,S., Yin,L., Mou,L., Hart,T. and
            Chen,J.
  TITLE     FACS-based genome-wide CRISPR screens define key regulators of DNA
            damage signaling pathways
  JOURNAL   Mol Cell 83 (15), 2810-2828 (2023)
   PUBMED   37541219
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Wang,Y.Y., Hsu,S.H., Tsai,H.Y. and Cheng,M.C.
  TITLE     Sequencing of the coding regions of GNBIL on chromosome 22q11.2 as
            a risk gene of schizophrenia
  JOURNAL   Psychiatry Res 300, 113943 (2021)
   PUBMED   33932639
  REMARK    GeneRIF: Sequencing of the coding regions of GNBIL on chromosome
            22q11.2 as a risk gene of schizophrenia.
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Sun,Y., Tao,Y., Wang,J. and Saffen,D.
  TITLE     The schizophrenia/bipolar disorder candidate gene GNB1L is
            regulated in human temporal cortex by a cis-acting element located
            within the 3'-region
  JOURNAL   Neurosci Bull 31 (1), 43-52 (2015)
   PUBMED   24831436
  REMARK    GeneRIF: mRNA expression results implies that the GNB1L
            high-expression allele is the risk allele for schizophrenia and
            bipolar disorder in the Han Chinese population.
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Li,Y., Zhao,Q., Wang,T., Liu,J., Li,J., Li,T., Zeng,Z., Feng,G.,
            He,L. and Shi,Y.
  TITLE     Association study between GNB1L and three major mental disorders in
            Chinese Han populations
  JOURNAL   Psychiatry Res 187 (3), 457-459 (2011)
   PUBMED   20538345
  REMARK    GeneRIF: The results of this study suggested that GNB1L is linked
            with bipolar disorder and schizophrenia and not with major
            depressive disorder.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Dorr,M., Schmidt,C.O., Spielhagen,T., Bornhorst,A., Hentschel,K.,
            Franz,C., Empen,K., Kocher,T., Diehl,S.R., Kroemer,H.K., Volzke,H.,
            Ewert,R., Felix,S.B. and Rosskopf,D.
  TITLE     beta-blocker therapy and heart rate control during exercise testing
            in the general population: role of a common G-protein beta-3
            subunit variant
  JOURNAL   Pharmacogenomics 11 (9), 1209-1221 (2010)
   PUBMED   20860462
  REMARK    GeneRIF: Beta-blocker therapy and heart rate control during
            exercise testing in the general population: role of GNB1L variant.
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Sarbassov,D.D., Ali,S.M., Kim,D.H., Guertin,D.A., Latek,R.R.,
            Erdjument-Bromage,H., Tempst,P. and Sabatini,D.M.
  TITLE     Rictor, a novel binding partner of mTOR, defines a
            rapamycin-insensitive and raptor-independent pathway that regulates
            the cytoskeleton
  JOURNAL   Curr Biol 14 (14), 1296-1302 (2004)
   PUBMED   15268862
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Funke,B., Pandita,R.K. and Morrow,B.E.
  TITLE     Isolation and characterization of a novel gene containing WD40
            repeats from the region deleted in velo-cardio-facial/DiGeorge
            syndrome on chromosome 22q11
  JOURNAL   Genomics 73 (3), 264-271 (2001)
   PUBMED   11350118
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Hirosawa,M., Nagase,T., Murahashi,Y., Kikuno,R. and Ohara,O.
  TITLE     Identification of novel transcribed sequences on human chromosome
            22 by expressed sequence tag mapping
  JOURNAL   DNA Res 8 (1), 1-9 (2001)
   PUBMED   11258795
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Gong,L., Liu,M., Jen,J. and Yeh,E.T.
  TITLE     GNB1L, a gene deleted in the critical region for DiGeorge syndrome
            on 22q11, encodes a G-protein beta-subunit-like polypeptide
  JOURNAL   Biochim Biophys Acta 1494 (1-2), 185-188 (2000)
   PUBMED   11072084
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY007378.1, CA425124.1, AC000089.1 and AC000091.1.
            
            On Dec 19, 2001 this sequence version replaced NP_071891.1.
            
            Summary: This gene encodes a G-protein beta-subunit-like
            polypeptide which is a member of the WD repeat protein family. WD
            repeats are minimally conserved regions of approximately 40 amino
            acids typically bracketed by gly-his and trp-asp (GH-WD), which may
            facilitate formation of heterotrimeric or multiprotein complexes.
            Members of this family are involved in a variety of cellular
            processes, including cell cycle progression, signal transduction,
            apoptosis, and gene regulation. This protein contains 6 WD repeats
            and is highly expressed in the heart. The gene maps to the region
            on chromosome 22q11, which is deleted in DiGeorge syndrome,
            trisomic in derivative 22 syndrome and tetrasomic in cat-eye
            syndrome. Therefore, this gene may contribute to the etiology of
            those disorders. Transcripts from this gene share exons with some
            transcripts from the C22orf29 gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF301895.1, AY007378.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329517.11/ ENSP00000331313.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..327
                     /product="guanine nucleotide-binding protein subunit
                     beta-like protein 1"
                     /note="G-protein beta subunit-like protein; guanine
                     nucleotide binding protein beta-subunit-like polypeptide;
                     guanine nucleotide binding protein (G protein), beta
                     polypeptide 1-like; WD repeat-containing protein 14; g
                     protein subunit beta-like protein 1; WD40
                     repeat-containing protein deleted in VCFS"
                     /calculated_mol_wt=35487
     Region          <15..323
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          16..54
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYB4.2)"
     Region          58..97
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYB4.2)"
     Region          70..110
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          103..145
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYB4.2)"
     Region          115..155
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          153..195
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYB4.2)"
     Region          164..205
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          200..237
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYB4.2)"
     Region          211..248
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          242..282
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYB4.2)"
     Region          255..296
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          286..323
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYB4.2)"
     Region          298..321
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..327
                     /gene="GNB1L"
                     /gene_synonym="DGCRK3; FKSG1; GY2; WDR14; WDVCF"
                     /coded_by="NM_053004.3:173..1156"
                     /db_xref="CCDS:CCDS13768.1"
                     /db_xref="GeneID:54584"
                     /db_xref="HGNC:HGNC:4397"
                     /db_xref="MIM:610778"
ORIGIN      
        1 mtapcppppp dpqfvlrgtq spvhalhfce gaqaqgrpll fsgsqsglvh iwslqtrrav
       61 ttldghggqc vtwlqtlpqg rqllsqgrdl klclwdlaeg rsavvdsvcl esvgfcrssi
      121 laggqprwtl avpgrgsdev qilempskts vcalkpkada klgmpmclrl wqadcssrpl
      181 llagyedgsv vlwdvseqkv csriacheep vmdldfdsqk argisgsagk alavwsldwq
      241 qalqvrgthe ltnpgiaevt irpdrkilat agwdhrirvf hwrtmqplav lafhsaavqc
      301 vaftadglla agskdqrisl wslypra
//
LOCUS       NP_001035350             766 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein kinase DCLK2 isoform a [Homo sapiens].
ACCESSION   NP_001035350
VERSION     NP_001035350.2
DBSOURCE    REFSEQ: accession NM_001040260.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Hu,L., Zhang,Y., Guo,L., Zhong,H., Xie,L., Zhou,J., Liao,C.,
            Yao,H., Fang,J., Liu,H., Zhang,C., Zhang,H., Zhu,X., Luo,M., von
            Kriegsheim,A., Li,B., Luo,W., Zhang,X., Chen,X., Mendell,J.T.,
            Xu,L., Kapur,P., Baldwin,A.S., Brugarolas,J. and Zhang,Q.
  TITLE     Kinome-wide siRNA screen identifies a DCLK2-TBK1 oncogenic
            signaling axis in clear cell renal cell carcinoma
  JOURNAL   Mol Cell 84 (4), 776-790 (2024)
   PUBMED   38211588
  REMARK    GeneRIF: Kinome-wide siRNA screen identifies a DCLK2-TBK1 oncogenic
            signaling axis in clear cell renal cell carcinoma.
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Song,J., Merrill,R.A., Usachev,A.Y. and Strack,S.
  TITLE     The X-linked intellectual disability gene product and E3 ubiquitin
            ligase KLHL15 degrades doublecortin proteins to constrain neuronal
            dendritogenesis
  JOURNAL   J Biol Chem 296, 100082 (2021)
   PUBMED   33199366
REFERENCE   4  (residues 1 to 766)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 766)
  AUTHORS   Nawabi,H., Belin,S., Cartoni,R., Williams,P.R., Wang,C.,
            Latremoliere,A., Wang,X., Zhu,J., Taub,D.G., Fu,X., Yu,B., Gu,X.,
            Woolf,C.J., Liu,J.S., Gabel,C.V., Steen,J.A. and He,Z.
  TITLE     Doublecortin-Like Kinases Promote Neuronal Survival and Induce
            Growth Cone Reformation via Distinct Mechanisms
  JOURNAL   Neuron 88 (4), 704-719 (2015)
   PUBMED   26526391
REFERENCE   6  (residues 1 to 766)
  AUTHORS   Kerjan,G., Koizumi,H., Han,E.B., Dube,C.M., Djakovic,S.N.,
            Patrick,G.N., Baram,T.Z., Heinemann,S.F. and Gleeson,J.G.
  TITLE     Mice lacking doublecortin and doublecortin-like kinase 2 display
            altered hippocampal neuronal maturation and spontaneous seizures
  JOURNAL   Proc Natl Acad Sci U S A 106 (16), 6766-6771 (2009)
   PUBMED   19342486
REFERENCE   7  (residues 1 to 766)
  AUTHORS   Gorelik,A., Sapir,T. and Reiner,O.
  TITLE     Gene trapping: an antibody-dependent approach for verifying
            integration in your favorite gene
  JOURNAL   Cell Mol Biol Lett 13 (4), 614-620 (2008)
   PUBMED   18618084
REFERENCE   8  (residues 1 to 766)
  AUTHORS   Tuy,F.P., Saillour,Y., Kappeler,C., Chelly,J. and Francis,F.
  TITLE     Alternative transcripts of Dclk1 and Dclk2 and their expression in
            doublecortin knockout mice
  JOURNAL   Dev Neurosci 30 (1-3), 171-186 (2008)
   PUBMED   18075264
REFERENCE   9  (residues 1 to 766)
  AUTHORS   Reiner,O., Coquelle,F.M., Peter,B., Levy,T., Kaplan,A., Sapir,T.,
            Orr,I., Barkai,N., Eichele,G. and Bergmann,S.
  TITLE     The evolving doublecortin (DCX) superfamily
  JOURNAL   BMC Genomics 7, 188 (2006)
   PUBMED   16869982
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 766)
  AUTHORS   Edelman,A.M., Kim,W.Y., Higgins,D., Goldstein,E.G., Oberdoerster,M.
            and Sigurdson,W.
  TITLE     Doublecortin kinase-2, a novel doublecortin-related protein kinase
            associated with terminal segments of axons and dendrites
  JOURNAL   J Biol Chem 280 (9), 8531-8543 (2005)
   PUBMED   15611072
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB209181.1, DA122884.1,
            AC093748.3 and AI419589.1.
            
            On Sep 1, 2007 this sequence version replaced NP_001035350.1.
            
            Summary: This gene encodes a member of the protein kinase
            superfamily and the doublecortin family. The protein encoded by
            this gene contains two N-terminal doublecortin domains, which bind
            microtubules and regulate microtubule polymerization, a C-terminal
            serine/threonine protein kinase domain, which shows substantial
            homology to Ca2+/calmodulin-dependent protein kinase, and a
            serine/proline-rich domain in between the doublecortin and the
            protein kinase domains, which mediates multiple protein-protein
            interactions. The microtubule-polymerizing activity of the encoded
            protein is independent of its protein kinase activity. Mouse
            studies show that the DCX gene, another family member, and this
            gene share function in the establishment of hippocampal
            organization and that their absence results in a severe epileptic
            phenotype and lethality, as described in human patients with
            lissencephaly. Multiple alternatively spliced transcript variants
            have been identified. [provided by RefSeq, Sep 2010].
            
            Transcript Variant: This variant (1) is known as exon-5-lacking
            transcript (PMIDs:15611072 and 18075264). It lacks an in-frame
            coding exon in the 5' region, as compared to variant 2. The
            resulting isoform (a) lacks an internal segment, as compared to
            isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB209181.1, SRR7346977.2549475.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296550.12/ ENSP00000296550.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.23-q31.3"
     Protein         1..766
                     /product="serine/threonine-protein kinase DCLK2 isoform a"
                     /EC_number="2.7.11.1"
                     /note="doublecortin and CaM kinase-like 2;
                     serine/threonine-protein kinase DCLK2; CaMK-like CREB
                     regulatory kinase 2; doublecortin-like and CAM kinase-like
                     2; doublecortin domain-containing protein 3B"
                     /calculated_mol_wt=83475
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N568.4)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N568.4)"
     Region          70..154
                     /region_name="DCX1_DCLK2"
                     /note="Dublecortin-like domain 1 found in
                     doublecortin-like kinase 2 (DCLK2); cd17141"
                     /db_xref="CDD:340661"
     Site            order(70,81..83,89,94..95,97,105,113..115,117..118,121,
                     148)
                     /site_type="other"
                     /note="putative tubulin binding site [polypeptide
                     binding]"
                     /db_xref="CDD:340661"
     Site            order(85,130)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340661"
     Region          193..276
                     /region_name="DCX2"
                     /note="Dublecortin-like domain 2; cd17069"
                     /db_xref="CDD:340589"
     Site            order(195,206..208,214,219..220,222,230,239..240,243,270)
                     /site_type="other"
                     /note="putative DCX-stabilized microtubules [polypeptide
                     binding]"
                     /db_xref="CDD:340589"
     Site            order(210,251)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340589"
     Region          300..378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N568.4)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N568.4)"
     Region          392..650
                     /region_name="STKc_DCKL2"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Doublecortin-like kinase 2 (also called Doublecortin-like
                     and CAM kinase-like 2); cd14184"
                     /db_xref="CDD:271086"
     Site            order(400..404,408,421,423,453,469..472,476,478,514..515,
                     517,519..520,522,536..537,540,552..556,558)
                     /site_type="active"
                     /db_xref="CDD:271086"
     Site            order(400..403,408,421,423,453,469..472,476,519..520,522,
                     536..537)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271086"
     Site            order(404,476,478,514..515,517,519,540,552..556,558)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271086"
     Site            536..556
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271086"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5MPA9; propagated from
                     UniProtKB/Swiss-Prot (Q8N568.4)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5MPA9; propagated from
                     UniProtKB/Swiss-Prot (Q8N568.4)"
     Region          707..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N568.4)"
     CDS             1..766
                     /gene="DCLK2"
                     /gene_synonym="CL2; CLICK-II; CLICK2; CLIK2; DCAMKL2;
                     DCDC3; DCDC3B; DCK2"
                     /coded_by="NM_001040260.4:584..2884"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34076.1"
                     /db_xref="GeneID:166614"
                     /db_xref="HGNC:HGNC:19002"
                     /db_xref="MIM:613166"
ORIGIN      
        1 mastrsiele hfeerdkrpr pgsrrgapss sggssssgpk gnglipspah sahcsfyrtr
       61 tlqalssekk akkarfyrng dryfkglvfa issdrfrsfd allieltrsl sdnvnlpqgv
      121 rtiytidgsr kvtsldelle gesyvcasne pfrkvdytkn inpnwsvnik ggtsralaaa
      181 ssvksevkes kdfikpklvt virsgvkprk avrillnkkt ahsfeqvltd iteaikldsg
      241 vvkrlctldg kqvtclqdff gdddvfiacg pekfryaqdd fvldhsecrv lkssysrssa
      301 vkysgskspg psrrskspas vngtpssqls tpkstkssss sptspgsfrg lkqisahgrs
      361 ssnvnggpel drcispegvn gnrcsesstl lekykigkvi gdgnfavvke cidrstgkef
      421 alkiidkakc cgkehliene vsilrrvkhp niimlveeme tatelflvme lvkggdlfda
      481 itsstkyter dgsamvynla nalrylhgls ivhrdikpen llvceypdgt kslklgdfgl
      541 atvvegplyt vcgtptyvap eiiaetgygl kvdiwaagvi tyillcgfpp frsennlqed
      601 lfdqilagkl efpapywdni tdsakelisq mlqvnvearc tagqilshpw vsddasqenn
      661 mqaevtgklk qhfnnalpkq nstttgvsvi mntaldkegq ifcskhcqds grpgmepisp
      721 vppsveeipv pgeavpaptp pesptphppp aapggeragt wrrhrd
//
LOCUS       NP_061135                648 aa            linear   PRI 27-APR-2025
DEFINITION  probable ATP-dependent RNA helicase DDX43 [Homo sapiens].
ACCESSION   NP_061135
VERSION     NP_061135.2
DBSOURCE    REFSEQ: accession NM_018665.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Tabatabaei,T., Rezvany,M.R., Ghasemi,B., Vafaei,F., Zadeh,M.K.,
            Zaker,F. and Salmaninejad,A.
  TITLE     Effect of DNMT3A R882H Hot Spot Mutations on DDX43 Promoter
            Methylation in Acute Myeloid Leukemia
  JOURNAL   Biomed Res Int 2024, 9625043 (2024)
   PUBMED   38807916
  REMARK    GeneRIF: Effect of DNMT3A R882H Hot Spot Mutations on DDX43
            Promoter Methylation in Acute Myeloid Leukemia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Amer,N.N., Khairat,R., Hammad,A.M. and Kamel,M.M.
  TITLE     DDX43 mRNA expression and protein levels in relation to
            clinicopathological profile of breast cancer
  JOURNAL   PLoS One 18 (5), e0284455 (2023)
   PUBMED   37200388
  REMARK    GeneRIF: DDX43 mRNA expression and protein levels in relation to
            clinicopathological profile of breast cancer.
            Erratum:[PLoS One. 2024 Dec 26;19(12):e0316591. doi:
            10.1371/journal.pone.0316591. PMID: 39724251]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Wu,H., Zhai,L.T., Chen,P.Y. and Xi,X.G.
  TITLE     DDX43 prefers single strand substrate and its full binding activity
            requires physical connection of all domains
  JOURNAL   Biochem Biophys Res Commun 520 (3), 594-599 (2019)
   PUBMED   31623828
  REMARK    GeneRIF: DDX43 prefers single-strand DNA or RNA with length longer
            than 12nt and much prefers guanosine than the other three
            nucleotides. Achievement of the full binding affinity of protein to
            substrate needs the existence of all domains, and they must be
            connected. The absence of either of them or the disjunction can
            result in a decreased binding affinity to substrates, approximately
            reduced 10-fold.
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Mathieu,M.G., Linley,A.J., Reeder,S.P., Badoual,C., Tartour,E.,
            Rees,R.C. and McArdle,S.E.
  TITLE     HAGE, a cancer/testis antigen expressed at the protein level in a
            variety of cancers
  JOURNAL   Cancer Immun 10, 2 (2010)
   PUBMED   20058853
  REMARK    GeneRIF: HAGE protein expression was confirmed in 75% (12/16) of
            carcinomas as compared to normal tissues
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Mathieu,M.G., Knights,A.J., Pawelec,G., Riley,C.L., Wernet,D.,
            Lemonnier,F.A., Straten,P.T., Mueller,L., Rees,R.C. and
            McArdle,S.E.
  TITLE     HAGE, a cancer/testis antigen with potential for melanoma
            immunotherapy: identification of several MHC class I/II
            HAGE-derived immunogenic peptides
  JOURNAL   Cancer Immunol Immunother 56 (12), 1885-1895 (2007)
   PUBMED   17487488
  REMARK    GeneRIF: HAGE is a cancer/testis antigen with potential for
            melanoma immunotherapy
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Nagel,H., Laskawi,R., Eiffert,H. and Schlott,T.
  TITLE     Analysis of the tumour suppressor genes, FHIT and WT-1, and the
            tumour rejection genes, BAGE, GAGE-1/2, HAGE, MAGE-1, and MAGE-3,
            in benign and malignant neoplasms of the salivary glands
  JOURNAL   Mol Pathol 56 (4), 226-231 (2003)
   PUBMED   12890744
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Martelange,V., De Smet,C., De Plaen,E., Lurquin,C. and Boon,T.
  TITLE     Identification on a human sarcoma of two new genes with
            tumor-specific expression
  JOURNAL   Cancer Res 60 (14), 3848-3855 (2000)
   PUBMED   10919659
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA453913.1, BX646425.1,
            BC066938.1 and BQ020439.1.
            
            On Jan 31, 2009 this sequence version replaced NP_061135.1.
            
            Summary:  The protein encoded by this gene is an ATP-dependent RNA
            helicase in the DEAD-box family and displays tumor-specific
            expression. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ278110.1, SRR1660809.217720.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370336.5/ ENSP00000359361.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..648
                     /product="probable ATP-dependent RNA helicase DDX43"
                     /EC_number="3.6.4.13"
                     /note="cancer/testis antigen 13; DEAD-box protein 43;
                     helical antigen; DEAD box protein HAGE; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 43"
                     /calculated_mol_wt=72713
     Region          1..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXZ2.2)"
     Region          69..134
                     /region_name="KH-I_DDX43_DDX53"
                     /note="type I K homology (KH) RNA-binding domain found in
                     DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53)
                     and similar proteins; cd22430"
                     /db_xref="CDD:411858"
     Site            order(77,79..81,83..87,90..91,94..95,100..103)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411858"
     Region          171..631
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          242..270
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXZ2.2)"
     Site            order(262,264..266,269,288..294,331,335)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350716"
     Region          396..399
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXZ2.2)"
     Region          628..648
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXZ2.2)"
     CDS             1..648
                     /gene="DDX43"
                     /gene_synonym="CT13; HAGE"
                     /coded_by="NM_018665.3:79..2025"
                     /db_xref="CCDS:CCDS4977.1"
                     /db_xref="GeneID:55510"
                     /db_xref="HGNC:HGNC:18677"
                     /db_xref="MIM:606286"
ORIGIN      
        1 mshhggapka stwvvasrrs stvsraperr paeelnrtgp egysvgrggr wrgtsrppea
       61 vaagheelpl cfalkshfvg avigrggski kniqsttntt iqiiqeqpes lvkifgskam
      121 qtkakavidn fvkkleenyn secgidtafq psvgkdgstd nnvvagdrpl idwdqireeg
      181 lkwqktkwad lppikknfyk estatsamsk veadswrken fnitwddlkd gekrpipnpt
      241 ctfddafqcy pevmenikka gfqkptpiqs qawpivlqgi dligvaqtgt gktlcylmpg
      301 fihlvlqpsl kgqrnrpgml vltptrelal qvegecckys ykglrsvcvy gggnrdeqie
      361 elkkgvdiii atpgrlndlq msnfvnlkni tylvldeadk mldmgfepqi mkilldvrpd
      421 rqtvmtsatw phsvhrlaqs ylkepmivyv gtldlvavss vkqniivtte eekwshmqtf
      481 lqsmsstdkv ivfvsrkava dhlssdlilg nisveslhgd reqrdrekal enfktgkvri
      541 liatdlasrg ldvhdvthvy nfdfprniee yvhrigrtgr agrtgvsitt ltrndwrvas
      601 elinileran qsipeelvsm aerfkahqqk remerkmerp qgrpkkfh
//
LOCUS       NP_055059               1211 aa            linear   PRI 27-APR-2025
DEFINITION  A disintegrin and metalloproteinase with thrombospondin motifs 2
            isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_055059
VERSION     NP_055059.2
DBSOURCE    REFSEQ: accession NM_014244.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Carter,E.P., Yoneten,K.K., Gavara,N., Tyler,E.J., Gauthier,V.,
            Murray,E.R., Ten Dijke,P., Cameron,A.J., Pearce,O. and Grose,R.P.
  TITLE     Opposing roles for ADAMTS2 and ADAMTS14 in myofibroblast
            differentiation and function
  JOURNAL   J Pathol 262 (1), 90-104 (2024)
   PUBMED   37929635
  REMARK    GeneRIF: Opposing roles for ADAMTS2 and ADAMTS14 in myofibroblast
            differentiation and function.
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Earley,E.J., Kelly,S., Fang,F., Alencar,C.S., Rodrigues,D.O.W.,
            Soares Cruz,D.T., Flanagan,J.M., Ware,R.E., Zhang,X., Gordeuk,V.,
            Gladwin,M., Zhang,Y., Nouraie,M., Nekhai,S., Sabino,E., Custer,B.,
            Dinardo,C. and Page,G.P.
  CONSRTM   International Component of the NHLBI Recipient Epidemiology and
            Donor Evaluation Study (REDS-III) and the NHLBI Trans-Omics for
            Precision Medicine (TOPMed) Consortium
  TITLE     Genome-wide association study of early ischaemic stroke risk in
            Brazilian individuals with sickle cell disease implicates ADAMTS2
            and CDK18 and uncovers novel loci
  JOURNAL   Br J Haematol 201 (2), 343-352 (2023)
   PUBMED   36602125
  REMARK    GeneRIF: Genome-wide association study of early ischaemic stroke
            risk in Brazilian individuals with sickle cell disease implicates
            ADAMTS2 and CDK18 and uncovers novel loci.
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Zhang,Y., Li,J., Ji,Y., Cheng,Y. and Fu,X.
  TITLE     Mutations in the TBX15-ADAMTS2 pathway associate with a novel soft
            palate dysplasia
  JOURNAL   Hum Mutat 43 (12), 2102-2115 (2022)
   PUBMED   36124393
  REMARK    GeneRIF: Mutations in the TBX15-ADAMTS2 pathway associate with a
            novel soft palate dysplasia.
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Witten,A., Ruhle,F., de Witt,M., Barysenka,A., Stach,M., Junker,R.,
            Nowak-Gottl,U. and Stoll,M.
  TITLE     ADAMTS12, a new candidate gene for pediatric stroke
  JOURNAL   PLoS One 15 (8), e0237928 (2020)
   PUBMED   32817637
  REMARK    GeneRIF: ADAMTS12, a new candidate gene for pediatric stroke.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Bekhouche,M. and Colige,A.
  TITLE     The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology
  JOURNAL   Matrix Biol 44-46, 46-53 (2015)
   PUBMED   25863161
  REMARK    GeneRIF: Data indicate that ADAMTS2 and 3 cleave the
            amino-propeptide of fibrillar collagens and regulate blood vessels
            homeostasis and lymphangiogenesis. Also, ADAMTS2 deficiency leads
            to the dermatosparactic type of Ehlers-Danlos syndrome. [review]
            Review article
REFERENCE   6  (residues 1 to 1211)
  AUTHORS   Colige,A., Ruggiero,F., Vandenberghe,I., Dubail,J., Kesteloot,F.,
            Van Beeumen,J., Beschin,A., Brys,L., Lapiere,C.M. and Nusgens,B.
  TITLE     Domains and maturation processes that regulate the activity of
            ADAMTS-2, a metalloproteinase cleaving the aminopropeptide of
            fibrillar procollagens types I-III and V
  JOURNAL   J Biol Chem 280 (41), 34397-34408 (2005)
   PUBMED   16046392
  REMARK    GeneRIF: Determination of the processing, activity and cleavage
            specificity of the bovine ADAMTS2 protein.
REFERENCE   7  (residues 1 to 1211)
  AUTHORS   Hurskainen,T.L., Hirohata,S., Seldin,M.F. and Apte,S.S.
  TITLE     ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of
            zinc metalloproteases. General features and genomic distribution of
            the ADAM-TS family
  JOURNAL   J Biol Chem 274 (36), 25555-25563 (1999)
   PUBMED   10464288
REFERENCE   8  (residues 1 to 1211)
  AUTHORS   Colige,A., Sieron,A.L., Li,S.W., Schwarze,U., Petty,E.,
            Wertelecki,W., Wilcox,W., Krakow,D., Cohn,D.H., Reardon,W.,
            Byers,P.H., Lapiere,C.M., Prockop,D.J. and Nusgens,B.V.
  TITLE     Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis
            are caused by mutations in the procollagen I N-proteinase gene
  JOURNAL   Am J Hum Genet 65 (2), 308-317 (1999)
   PUBMED   10417273
REFERENCE   9  (residues 1 to 1211)
  AUTHORS   Tang,B.L. and Hong,W.
  TITLE     ADAMTS: a novel family of proteases with an ADAM protease domain
            and thrombospondin 1 repeats
  JOURNAL   FEBS Lett 445 (2-3), 223-225 (1999)
   PUBMED   10094461
  REMARK    Review article
REFERENCE   10 (residues 1 to 1211)
  AUTHORS   Reardon,W., Winter,R.M., Smith,L.T., Lake,B.D., Rossiter,M. and
            Baraitser,M.
  TITLE     The natural history of human dermatosparaxis (Ehlers-Danlos
            syndrome type VIIC)
  JOURNAL   Clin Dysmorphol 4 (1), 1-11 (1995)
   PUBMED   7735500
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC109479.3, DA928965.1,
            AJ003125.1, AC008544.7, AC010216.8 and CA445758.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 28, 2006 this sequence version replaced NP_055059.1.
            
            Summary: This gene encodes a member of the ADAMTS (a disintegrin
            and metalloproteinase with thrombospondin motifs) protein family.
            Members of the family share several distinct protein modules,
            including a propeptide region, a metalloproteinase domain, a
            disintegrin-like domain, and a thrombospondin type 1 (TS) motif.
            Individual members of this family differ in the number of
            C-terminal TS motifs, and some have unique C-terminal domains. The
            encoded preproprotein is proteolytically processed to generate the
            mature procollagen N-proteinase. This proteinase excises the
            N-propeptide of the fibrillar procollagens types I-III and type V.
            Mutations in this gene cause Ehlers-Danlos syndrome type VIIC, a
            recessively inherited connective-tissue disorder. Alternative
            splicing results in multiple transcript variants, at least one of
            which encodes an isoform that is proteolytically processed.
            [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ003125.1, DRR138522.934417.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000251582.12/ ENSP00000251582.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..1211
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 2 isoform 1 preproprotein"
                     /EC_number="3.4.24.14"
                     /note="procollagen I N-proteinase; a disintegrin-like and
                     metalloprotease (reprolysin type) with thrombospondin type
                     1 motif, 2; a disintegrin and metalloproteinase with
                     thrombospondin motifs 2; procollagen N-endopeptidase;
                     procollagen I/II amino propeptide-processing enzyme"
                     /calculated_mol_wt=131715
     sig_peptide     1..29
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95450.2)"
                     /calculated_mol_wt=3059
     Region          91..212
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Site            112
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95450.2)"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95450.2)"
     mat_peptide     254..1211
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 2. /id=PRO_0000029159"
                     /note="propagated from UniProtKB/Swiss-Prot (O95450.2)"
                     /calculated_mol_wt=108323
     Region          266..467
                     /region_name="ZnMc_ADAMTS_like"
                     /note="Zinc-dependent metalloprotease, ADAMTS_like
                     subgroup. ADAMs (A Disintegrin And Metalloprotease) are
                     glycoproteins, which play roles in cell signaling, cell
                     fusion, and cell-cell interactions. This particular
                     subfamily represents domain architectures that...;
                     cd04273"
                     /db_xref="CDD:239801"
     Site            order(408..409,412,418)
                     /site_type="active"
                     /db_xref="CDD:239801"
     Region          482..551
                     /region_name="ADAMTS_CR_2"
                     /note="ADAMTS cysteine-rich domain 2; pfam17771"
                     /db_xref="CDD:465496"
     Region          564..616
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          621..722
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Region          691..693
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95450.2)"
     Region          723..851
                     /region_name="Spacer"
                     /note="propagated from UniProtKB/Swiss-Prot (O95450.2)"
     Region          724..837
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Region          858..913
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          918..975
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            949
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95450.2)"
     Region          979..1028
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            993
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95450.2)"
     Site            1031
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95450.2)"
     Site            1098
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95450.2)"
     Site            1145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95450.2)"
     Site            1150
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95450.2)"
     Region          1170..1191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95450.2)"
     CDS             1..1211
                     /gene="ADAMTS2"
                     /gene_synonym="ADAM-TS2; ADAMTS-2; ADAMTS-3; EDSDERMS;
                     NPI; PC I-NP; PCI-NP; PCINP; PCPNI; PNPI"
                     /coded_by="NM_014244.5:134..3769"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4444.1"
                     /db_xref="GeneID:9509"
                     /db_xref="HGNC:HGNC:218"
                     /db_xref="MIM:604539"
ORIGIN      
        1 mdppagaarr llcpalllll lllpppllpp ppppanarla aaadppggpl ghgaerilav
       61 pvrtdaqgrl vshvvsaats ragvrarraa pvrtpsfpgg neeepgshlf ynvtvfgrdl
      121 hlrlrpnarl vapgatmewq gekgttrvep llgsclyvgd vaglaeassv alsncdglag
      181 lirmeeeeff ieplekglaa qeaeqgrvhv vyrrpptspp lggpqaldtg asldsldsls
      241 ralgvleeha nssrrrarrh aadddyniev llgvddsvvq fhgkehvqky lltlmnivne
      301 iyhdeslgah invvlvriil lsygksmsli eignpsqsle nvcrwaylqq kpdtghdeyh
      361 dhaifltrqd fgpsgmqgya pvtgmchpvr sctlnhedgf ssafvvahet ghvlgmehdg
      421 qgnrcgdevr lgsimaplvq aafhrfhwsr csqqelsryl hsydcllddp fahdwpalpq
      481 lpglhysmne qcrfdfglgy mmctafrtfd pckqlwcshp dnpyfcktkk gppldgtmca
      541 pgkhcfkghc iwltpdilkr dgswgawspf gscsrtcgtg vkfrtrqcdn phpanggrtc
      601 sglaydfqlc srqdcpdsla dfreeqcrqw dlyfehgdaq hhwlphehrd akerchlyce
      661 sretgevvsm krmvhdgtrc sykdafslcv rgdcrkvgcd gvigsskqed kcgvcggdns
      721 hckvvkgtft rspkkhgyik mfeipagarh lliqevdats hhlavknlet gkfilneend
      781 vdassktfia mgveweyrde dgretlqtmg plhgtitvlv ipvgdtrvsl tykymiheds
      841 lnvddnnvle edsvvyewal kkwspcskpc gggsqftkyg crrrldhkmv hrgfcaalsk
      901 pkairracnp qecsqpvwvt gewepcsqtc grtgmqvrsv rciqplhdnt trsvhakhcn
      961 darpesrrac srelcpgrwr agpwsqcsvt cgngtqerpv lcrtaddsfg icqeerpeta
     1021 rtcrlgpcpr nisdpskksy vvqwlsrpdp dspirkissk ghcqgdksif crmevlsryc
     1081 sipgynklcc kscnlynnlt nvegrieppp gkhndidvfm ptlpvptvam evrpspstpl
     1141 evplnasstn atedhpetna vdepykihgl edevqppnli prrpspyekt rnqriqelid
     1201 emrkkemlgk f
//
LOCUS       NP_001348615             802 aa            linear   ROD 27-APR-2025
DEFINITION  diacylglycerol kinase beta isoform 1 [Mus musculus].
ACCESSION   NP_001348615 XP_006515132
VERSION     NP_001348615.1
DBSOURCE    REFSEQ: accession NM_001361686.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Cesari,E., Farini,D., Medici,V., Ehrmann,I., Guerra,M., Testa,E.,
            Naro,C., Geloso,M.C., Pagliarini,V., La Barbera,L., D'Amelio,M.,
            Orsini,T., Vecchioli,S.F., Tamagnone,L., Fort,P., Viscomi,M.T.,
            Elliott,D.J. and Sette,C.
  TITLE     Differential expression of paralog RNA binding proteins establishes
            a dynamic splicing program required for normal cerebral cortex
            development
  JOURNAL   Nucleic Acids Res 52 (8), 4167-4184 (2024)
   PUBMED   38324473
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Veerakumar,A., Yung,A.R., Liu,Y. and Krasnow,M.A.
  TITLE     Molecularly defined circuits for cardiovascular and cardiopulmonary
            control
  JOURNAL   Nature 606 (7915), 739-746 (2022)
   PUBMED   35650438
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Kakefuda,K., Ishisaka,M., Tsuruma,K., Shimazawa,M. and Hara,H.
  TITLE     Memantine, an NMDA receptor antagonist, improves working memory
            deficits in DGKbeta knockout mice
  JOURNAL   Neurosci Lett 630, 228-232 (2016)
   PUBMED   27495014
  REMARK    GeneRIF: Memantine, an NMDA receptor antagonist, improves working
            memory deficits in Diacylglycerol kinase (DGK) beta knockout mice.
            These findings may support the hypothesis that DGKbeta has a
            pivotal role in cognitive function.
REFERENCE   5  (residues 1 to 802)
  AUTHORS   Hozumi,Y., Kakefuda,K., Yamasaki,M., Watanabe,M., Hara,H. and
            Goto,K.
  TITLE     Involvement of diacylglycerol kinase beta in the spine formation at
            distal dendrites of striatal medium spiny neurons
  JOURNAL   Brain Res 1594, 36-45 (2015)
   PUBMED   25446448
  REMARK    GeneRIF: These findings suggest that DGKbeta regulates the spine
            formation at distal dendrites in medium spiny neurons
REFERENCE   6  (residues 1 to 802)
  AUTHORS   Shirai,Y., Kouzuki,T., Kakefuda,K., Moriguchi,S., Oyagi,A.,
            Horie,K., Morita,S.Y., Shimazawa,M., Fukunaga,K., Takeda,J.,
            Saito,N. and Hara,H.
  TITLE     Essential role of neuron-enriched diacylglycerol kinase (DGK),
            DGKbeta in neurite spine formation, contributing to cognitive
            function
  JOURNAL   PLoS One 5 (7), e11602 (2010)
   PUBMED   20657643
  REMARK    GeneRIF: Results demonstrate that membrane-localized DGKbeta
            regulates spine formation by regulation of lipids, contributing to
            the maintenance of neural networks in synaptic transmission of
            cognitive processes including memory.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 802)
  AUTHORS   Crotty,T., Cai,J., Sakane,F., Taketomi,A., Prescott,S.M. and
            Topham,M.K.
  TITLE     Diacylglycerol kinase delta regulates protein kinase C and
            epidermal growth factor receptor signaling
  JOURNAL   Proc Natl Acad Sci U S A 103 (42), 15485-15490 (2006)
   PUBMED   17021016
REFERENCE   8  (residues 1 to 802)
  AUTHORS   Keng,V.W., Yae,K., Hayakawa,T., Mizuno,S., Uno,Y., Yusa,K.,
            Kokubu,C., Kinoshita,T., Akagi,K., Jenkins,N.A., Copeland,N.G.,
            Horie,K. and Takeda,J.
  TITLE     Region-specific saturation germline mutagenesis in mice using the
            Sleeping Beauty transposon system
  JOURNAL   Nat Methods 2 (10), 763-769 (2005)
   PUBMED   16179923
REFERENCE   9  (residues 1 to 802)
  AUTHORS   Horie,K., Yusa,K., Yae,K., Odajima,J., Fischer,S.E., Keng,V.W.,
            Hayakawa,T., Mizuno,S., Kondoh,G., Ijiri,T., Matsuda,Y.,
            Plasterk,R.H. and Takeda,J.
  TITLE     Characterization of Sleeping Beauty transposition and its
            application to genetic screening in mice
  JOURNAL   Mol Cell Biol 23 (24), 9189-9207 (2003)
   PUBMED   14645530
REFERENCE   10 (residues 1 to 802)
  AUTHORS   Cipres,A., Carrasco,S., Merino,E., Diaz,E., Krishna,U.M.,
            Falck,J.R., Martinez-A,C. and Merida,I.
  TITLE     Regulation of diacylglycerol kinase alpha by phosphoinositide
            3-kinase lipid products
  JOURNAL   J Biol Chem 278 (37), 35629-35635 (2003)
   PUBMED   12832407
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CT025577.11, AC157494.2, AC141479.3, AC116471.8, AC157821.2,
            AC166996.1 and CT009742.12.
            
            On Mar 29, 2018 this sequence version replaced XP_006515132.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660811.117584.1,
                                           SRR9219382.230924.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 17.11 cM"
     Protein         1..802
                     /product="diacylglycerol kinase beta isoform 1"
                     /EC_number="2.7.1.107"
                     /note="DAG kinase beta; diglyceride kinase beta"
                     /calculated_mol_wt=90141
     Region          6..148
                     /region_name="DAG_kinase_N"
                     /note="Diacylglycerol kinase N-terminus; pfam14513"
                     /db_xref="CDD:464196"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NS52.2)"
     Region          152..221
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cd00051"
                     /db_xref="CDD:238008"
     Site            order(161,163,165,172,206,208,210,217)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238008"
     Region          237..302
                     /region_name="C1_DGKbeta_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase beta (DAG kinase
                     beta) and similar proteins; cd20845"
                     /db_xref="CDD:410395"
     Site            order(249..255,263..267,270)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410395"
     Region          307..365
                     /region_name="C1_DGKbeta_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase beta (DAG kinase
                     beta) and similar proteins; cd20891"
                     /db_xref="CDD:410441"
     Site            order(314..318,326..330,334)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410441"
     Region          384..416
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NS52.2)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NS52.2)"
     Region          438..559
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          580..760
                     /region_name="DAGKa"
                     /note="Diacylglycerol kinase accessory domain (presumed);
                     smart00045"
                     /db_xref="CDD:214486"
     Region          671..696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NS52.2)"
     Region          771..802
                     /region_name="Required for association with membranes and
                     function in neurite spine formation.
                     /evidence=ECO:0000269|PubMed:20657643"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NS52.2)"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NS52.2)"
     CDS             1..802
                     /gene="Dgkb"
                     /gene_synonym="6430574F24; 90kda; C630029D13Rik; DAGK2;
                     DGK; DGK-beta; mKIAA0718"
                     /coded_by="NM_001361686.1:625..3033"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:217480"
                     /db_xref="MGI:MGI:2442474"
ORIGIN      
        1 mtnqekwahl spsefsqlqk yaeystkklk dvleefhgng vlakynpegk qdilnqtidf
       61 egfklfmktf leaelpddft ahlfmsfsnk fphsspnvks kpallsgglr mnkgaitppr
      121 sspantcspe vihlkdivcy lsllergrpe dklefmfrly dtdgngflds seleniigqm
      181 mhvaeylewd vtelnpilhe mmeeidydrd gtvsleewiq ggmttipllv llglennvkd
      241 dgqhvwrlkh fnkpaycnlc lnmligvgkq glccsfckyt vhercvarap psciktyvks
      301 kkntdvmhhy wvegncptkc dkchktvkcy qgltglhcvw cqttlhnkca shlkpecdcg
      361 plkdhilppt ticpvvltmp sagasvpeer qstakkekss sqqpnkatdk nkmqransvt
      421 mdgqglqitp vpgthpllvf vnpksggkqg eriyrkfqyl lnprqvysls gngpmpglhf
      481 frdvpdfrvl acggdgtvgw ildciekanv vkhppvailp lgtgndlarc lrwgggyege
      541 nlmkilkdie ssteimldrw kfevtpndkd ekgdpvpysi innyfsigvd asiahrfhim
      601 rekhpekfns rmknkfwyfe fgtsetfsat ckklhesvei ecdgvqidli nislegiail
      661 nipsmhggsn lwgeskkkrs hrriekkgsd krptltdake lkfasqdlsd qllevvgleg
      721 amemgqiytg lksagrrlaq cssvvirtsk slpmqidgep wmqtpctiki thknqapmlm
      781 gpppktglfc slikrtrnrs ke
//
LOCUS       NP_001924                453 aa            linear   PRI 27-APR-2025
DEFINITION  dihydrolipoyllysine-residue succinyltransferase component of
            2-oxoglutarate dehydrogenase complex, mitochondrial isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001924
VERSION     NP_001924.2
DBSOURCE    REFSEQ: accession NM_001933.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Anderson,N.M., Qin,X., Finan,J.M., Lam,A., Athoe,J., Missiaen,R.,
            Skuli,N., Kennedy,A., Saini,A.S., Tao,T., Zhu,S., Nissim,I.,
            Look,A.T., Qing,G., Simon,M.C. and Feng,H.
  TITLE     Metabolic Enzyme DLST Promotes Tumor Aggression and Reveals a
            Vulnerability to OXPHOS Inhibition in High-Risk Neuroblastoma
  JOURNAL   Cancer Res 81 (17), 4417-4430 (2021)
   PUBMED   34233924
  REMARK    GeneRIF: Metabolic Enzyme DLST Promotes Tumor Aggression and
            Reveals a Vulnerability to OXPHOS Inhibition in High-Risk
            Neuroblastoma.
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Buffet,A., Zhang,J., Rebel,H., Corssmit,E.P.M., Jansen,J.C.,
            Hensen,E.F., Bovee,J.V.M.G., Morini,A., Gimenez-Roqueplo,A.P.,
            Hes,F.J., Devilee,P., Favier,J. and Bayley,J.P.
  TITLE     Germline DLST Variants Promote Epigenetic Modifications in
            Pheochromocytoma-Paraganglioma
  JOURNAL   J Clin Endocrinol Metab 106 (2), 459-471 (2021)
   PUBMED   33180916
  REMARK    GeneRIF: Germline DLST Variants Promote Epigenetic Modifications in
            Pheochromocytoma-Paraganglioma.
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Remacha,L., Pirman,D., Mahoney,C.E., Coloma,J., Calsina,B.,
            Curras-Freixes,M., Leton,R., Torres-Perez,R., Richter,S., Pita,G.,
            Herraez,B., Cianchetta,G., Honrado,E., Maestre,L., Urioste,M.,
            Aller,J., Garcia-Uriarte,O., Galvez,M.A., Luque,R.M., Lahera,M.,
            Moreno-Rengel,C., Eisenhofer,G., Montero-Conde,C.,
            Rodriguez-Antona,C., Llorca,O., Smolen,G.A., Robledo,M. and
            Cascon,A.
  TITLE     Recurrent Germline DLST Mutations in Individuals with Multiple
            Pheochromocytomas and Paragangliomas
  JOURNAL   Am J Hum Genet 104 (4), 651-664 (2019)
   PUBMED   30929736
  REMARK    GeneRIF: five germline variants affecting DLST in eight unrelated
            individuals were identified; all except one were diagnosed with
            multiple pheochromocytomas and paragangliomas
            Erratum:[Am J Hum Genet. 2019 May 2;104(5):1008-1010. doi:
            10.1016/j.ajhg.2019.04.010. PMID: 31051110]
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Chuang,D.T., Fisher,C.W., Lau,K.S., Griffin,T.A., Wynn,R.M. and
            Cox,R.P.
  TITLE     Maple syrup urine disease: domain structure, mutations and exon
            skipping in the dihydrolipoyl transacylase (E2) component of the
            branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   Mol Biol Med 8 (1), 49-63 (1991)
   PUBMED   1943690
REFERENCE   7  (residues 1 to 453)
  AUTHORS   Reed,L.J. and Hackert,M.L.
  TITLE     Structure-function relationships in dihydrolipoamide
            acyltransferases
  JOURNAL   J Biol Chem 265 (16), 8971-8974 (1990)
   PUBMED   2188967
  REMARK    Review article
REFERENCE   8  (residues 1 to 453)
  AUTHORS   Fregeau,D.R., Prindiville,T., Coppel,R.L., Kaplan,M., Dickson,E.R.
            and Gershwin,M.E.
  TITLE     Inhibition of alpha-ketoglutarate dehydrogenase activity by a
            distinct population of autoantibodies recognizing dihydrolipoamide
            succinyltransferase in primary biliary cirrhosis
  JOURNAL   Hepatology 11 (6), 975-981 (1990)
   PUBMED   2365294
REFERENCE   9  (residues 1 to 453)
  AUTHORS   Ono,K., Hakozaki,M., Kimura,A. and Kochi,H.
  TITLE     Purification, resolution, and reconstitution of rat liver
            branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   J Biochem 101 (1), 19-27 (1987)
   PUBMED   3571202
REFERENCE   10 (residues 1 to 453)
  AUTHORS   Kochi,H., Seino,H. and Ono,K.
  TITLE     Inhibition of glycine oxidation by pyruvate, alpha-ketoglutarate,
            and branched-chain alpha-keto acids in rat liver mitochondria:
            presence of interaction between the glycine cleavage system and
            alpha-keto acid dehydrogenase complexes
  JOURNAL   Arch Biochem Biophys 249 (2), 263-272 (1986)
   PUBMED   3753002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK289414.1, CX163292.1,
            CN422511.1, BM929953.1 and AI087261.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_001924.1.
            
            Summary: This gene encodes a mitochondrial protein that belongs to
            the 2-oxoacid dehydrogenase family. This protein is one of the
            three components (the E2 component) of the 2-oxoglutarate
            dehydrogenase complex that catalyzes the overall conversion of
            2-oxoglutarate to succinyl-CoA and CO(2). Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000302.2, SRR3476690.920610.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000334220.9/
                                                  ENSP00000335304.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..453
                     /product="dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial isoform 1 precursor"
                     /EC_number="2.3.1.61"
                     /note="dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial; E2K; OGDC-E2; dihydrolipoamide
                     S-succinyltransferase (E2 component of 2-oxo-glutarate
                     complex)"
                     /calculated_mol_wt=41390
     transit_peptide 1..67
                     /calculated_mol_wt=7384
     mat_peptide     68..453
                     /product="dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial isoform 1"
                     /calculated_mol_wt=41390
     Region          71..453
                     /region_name="sucB"
                     /note="2-oxoglutarate dehydrogenase complex
                     dihydrolipoamide succinyltransferase (E2 component);
                     TIGR01347"
                     /db_xref="CDD:273565"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Region          152..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36957.4)"
     Site            154
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Site            267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Site            272
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Site            277
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Site            307
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     CDS             1..453
                     /gene="DLST"
                     /gene_synonym="DLTS; KGD2; PGL7; PPGL7"
                     /coded_by="NM_001933.5:39..1400"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9833.1"
                     /db_xref="GeneID:1743"
                     /db_xref="HGNC:HGNC:2911"
                     /db_xref="MIM:126063"
ORIGIN      
        1 mlsrsrcvsr afsrslsafq kgncplgrrs lpgvslcqgp gypnsrkvvi nnsvfsvrff
       61 rttavckddl vtvktpafae svtegdvrwe kavgdtvaed evvceietdk tsvqvpspan
      121 gvieallvpd ggkveggtpl ftlrktgaap akakpaeapa aaapkaepta aavpppaapi
      181 ptqmppvpsp sqppsgkpvs avkptvappl aepgagkglr sehrekmnrm rqriaqrlke
      241 aqntcamltt fneidmsniq emrarhkeaf lkkhnlklgf msafvkasaf alqeqpvvna
      301 viddttkevv yrdyidisva vatprglvvp virnveamnf adiertitel gekarknela
      361 iedmdggtft isnggvfgsl fgtpiinppq sailgmhgif drpvaiggkv evrpmmyval
      421 tydhrlidgr eavtflrkik aavedprvll ldl
//
LOCUS       NP_001189367            1238 aa            linear   PRI 27-APR-2025
DEFINITION  erythroid differentiation-related factor 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001189367
VERSION     NP_001189367.1
DBSOURCE    REFSEQ: accession NM_001202438.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1238)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 1238)
  AUTHORS   Wang,D., Li,Y. and Shen,B.
  TITLE     A novel erythroid differentiation related gene EDRF1 upregulating
            globin gene expression in HEL cells
  JOURNAL   Chin Med J (Engl) 115 (11), 1701-1705 (2002)
   PUBMED   12609092
  REMARK    GeneRIF: EDRF1 regulated alpha- and gamma-globin gene synthesis by
            modulating DNA-binding activity of GATA-1 transcription factor.
REFERENCE   3  (residues 1 to 1238)
  AUTHORS   Wang,D., Ma,S., Wang,S. and Shen,B.
  TITLE     Antisense EDRF1 gene inhibited GATA-1 transcription factor
            DNA-binding activity in K562 cells
  JOURNAL   Sci China C Life Sci 45 (3), 289-297 (2002)
   PUBMED   18759052
REFERENCE   4  (residues 1 to 1238)
  AUTHORS   Wang,D., Li,Y. and Shen,B.
  TITLE     Initial function analysis of a novel erythroid differentiation
            related gene EDRF1
  JOURNAL   Sci China C Life Sci 44 (5), 489-496 (2001)
   PUBMED   18726394
REFERENCE   5  (residues 1 to 1238)
  AUTHORS   Wang,X., Wang,D., Chen,X., Hu,M., Wang,J., Li,Y., Guo,N. and
            Shen,B.
  TITLE     cDNA cloning and function analysis of two novel erythroid
            differentiation related genes
  JOURNAL   Sci China C Life Sci 44 (1), 99-105 (2001)
   PUBMED   18763094
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC026172.1, BC107479.1 and
            AL050102.1.
            
            Summary: This gene may play a role in erythroid cell
            differentiation. The encoded protein inhibits DNA binding of the
            erythroid transcription factor GATA-1 and may regulate the
            expression of alpha-globin and gamma-globin. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Feb
            2014].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.189997.1,
                                           SRR1660805.125095.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356792.9/ ENSP00000349244.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.2"
     Protein         1..1238
                     /product="erythroid differentiation-related factor 1
                     isoform 1"
                     /note="erythroid differentiation-related factor 1"
                     /calculated_mol_wt=138398
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T1.1)"
     Region          220..268
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T1.1)"
     Region          517..561
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T1.1)"
     Region          620..647
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T1.1)"
     Region          693..726
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T1.1)"
     Region          914..953
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T1.1)"
     CDS             1..1238
                     /gene="EDRF1"
                     /gene_synonym="C10orf137"
                     /coded_by="NM_001202438.2:100..3816"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS55733.1"
                     /db_xref="GeneID:26098"
                     /db_xref="HGNC:HGNC:24640"
                     /db_xref="MIM:620463"
ORIGIN      
        1 mgdakeagae gppagaaarg glsllsqges eessaqgsal flggnevksr avvkyssapp
       61 rtafarleek tdlklppanw lresaklgpa gttilgnskk skpfssfgma ydfidsvgnd
      121 vdvvsdseni kkllkipysk shvsmavhri grtllldeld iqelfmrssq tgdwtwlkef
      181 yqrlidqkwq rkkkskehwy qkailskfly ysingdgaaq pvsstaeqqe ssssdqtnds
      241 egaswpapfe mpssvsedps assqgseple psyivghvas apkeqnlitl fndgehsqgl
      301 kndfvrnilw tfedihmlvg snmpifgggr ypavslrlrd nnkpinvltg idywldnlic
      361 nvpelvmcfh vngivqkyem ikteeipnle nsnfstkvik diaqnilsfl ksnctkeght
      421 ywlfkasgsd ivklydlttl ceetedkyqn pftmpvaill ykvacnmmmk knqnkkhygt
      481 irtlllnclk lldksrhpqi iasanymlse lfqldepkke ensesplnen sdesyseeee
      541 empdsdengs ystssdpsdd skavaiiksv gelsvpekyk sihqirpsca fpvchdteer
      601 crlvlsyvle glksvdssik kesdlpaadp stpiplkyed essrggpegl ekqmalfldk
      661 mgslqkgnys sqsgmipgsw qhkmklqlil ksskayyvls daamslqkyg ralryiklal
      721 qshdtycclc tnmlsevllf lsqyltlcgd iqlmlaqnan nraahleefh yqtkedqeil
      781 hslhresscq gfawatdlst dlesqlsvsc kcyeaaneil qfsdlksqnp ehyvqvlkrm
      841 gnirneigvf ymnqaaalqs erlvsksvsa aeqqlwkksf scfekgihnf esiedatnaa
      901 lllcntgrlm ricaqahcga gdelkrefsp eeglyynkai dyylkalrsl gtrdihpavw
      961 dsvnwelstt yftmatlqqd yaplsrkaqe qiekevseam mkslkycdvd svsarqplcq
     1021 yraatihhrl asmyhsclrn qvgdehlrkq hrvladlhys kaaklfqllk dapcellrvq
     1081 lervafaefq mtsqnsnvgk lktlsgaldi mvrtehafql iqkelieefg qpksgdaaaa
     1141 adaspslnre evmkllsife srlsflllqs ikllsstkkk tsnnieddti lktnkhiysq
     1201 llratankta tllerinviv hllgqlaags aassnavq
//
LOCUS       NP_001351252             644 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 1 isoform 2 [Mus
            musculus].
ACCESSION   NP_001351252 XP_006515960
VERSION     NP_001351252.1
DBSOURCE    REFSEQ: accession NM_001364323.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Medeiros de Araujo,J.A., Barao,S., Mateos-White,I., Espinosa,A.,
            Costa,M.R., Gil-Sanz,C. and Muller,U.
  TITLE     ZBTB20 is crucial for the specification of a subset of callosal
            projection neurons and astrocytes in the mammalian neocortex
  JOURNAL   Development 148 (16) (2021)
   PUBMED   34351428
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Wang,J.H., Shi,C.W., Lu,Y.Y., Zeng,Y., Cheng,M.Y., Wang,R.Y.,
            Sun,Y., Jiang,Y.L., Yang,W.T., Zhao,D.D., Huang,H.B., Ye,L.P.,
            Cao,X., Yang,G.L. and Wang,C.F.
  TITLE     MicroRNA and circRNA Expression Analysis in a Zbtb1 Gene Knockout
            Monoclonal EL4 Cell Line
  JOURNAL   Front Cell Infect Microbiol 11, 706919 (2021)
   PUBMED   34290994
  REMARK    GeneRIF: MicroRNA and circRNA Expression Analysis in a Zbtb1 Gene
            Knockout Monoclonal EL4 Cell Line.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Zhang,X., Lu,Y., Cao,X., Zhen,T. and Kovalovsky,D.
  TITLE     Zbtb1 prevents default myeloid differentiation of lymphoid-primed
            multipotent progenitors
  JOURNAL   Oncotarget 7 (37), 58768-58778 (2016)
   PUBMED   27542215
  REMARK    GeneRIF: these results show that Zbtb1 expression prevents
            activation of a default myeloid program in LMPP cells, ensuring the
            generation of lymphoid cells
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Cao,X., Lu,Y., Zhang,X. and Kovalovsky,D.
  TITLE     Zbtb1 Safeguards Genome Integrity and Prevents p53-Mediated
            Apoptosis in Proliferating Lymphoid Progenitors
  JOURNAL   J Immunol 197 (4), 1199-1211 (2016)
   PUBMED   27402700
  REMARK    GeneRIF: these results indicate that Zbtb1 prevents DNA damage in
            replicating immune progenitors, allowing the generation of B cells,
            T cells, and myeloid cells.
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Oeschger,F.M., Wang,W.Z., Lee,S., Garcia-Moreno,F., Goffinet,A.M.,
            Arbones,M.L., Rakic,S. and Molnar,Z.
  TITLE     Gene expression analysis of the embryonic subplate
  JOURNAL   Cereb Cortex 22 (6), 1343-1359 (2012)
   PUBMED   21862448
REFERENCE   7  (residues 1 to 644)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   8  (residues 1 to 644)
  AUTHORS   Zhang,D., Harry,G.J., Blackshear,P.J. and Zeldin,D.C.
  TITLE     G-protein pathway suppressor 2 (GPS2) interacts with the regulatory
            factor X4 variant 3 (RFX4_v3) and functions as a transcriptional
            co-activator
  JOURNAL   J Biol Chem 283 (13), 8580-8590 (2008)
   PUBMED   18218630
REFERENCE   9  (residues 1 to 644)
  AUTHORS   Millien,G., Beane,J., Lenburg,M., Tsao,P.N., Lu,J., Spira,A. and
            Ramirez,M.I.
  TITLE     Characterization of the mid-foregut transcriptome identifies genes
            regulated during lung bud induction
  JOURNAL   Gene Expr Patterns 8 (2), 124-139 (2008)
   PUBMED   18023262
REFERENCE   10 (residues 1 to 644)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC124453.3.
            
            On Jun 14, 2018 this sequence version replaced XP_006515960.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660825.123917.1,
                                           SRR11927934.59490.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849379
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 33.73 cM"
     Protein         1..644
                     /product="zinc finger and BTB domain-containing protein 1
                     isoform 2"
                     /note="zinc finger and BTB domain-containing protein 1;
                     brain specific protein 2"
                     /calculated_mol_wt=73444
     Region          3..116
                     /region_name="BTB_POZ_ZBTB1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 1 (ZBTB1); cd18192"
                     /db_xref="CDD:349501"
     Region          270..319
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91VL9.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q91VL9.1)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q91VL9.1)"
     Region          536..574
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(536,539,552,574)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(541,543,545,547..548,551..552,573,585,587,591..592,
                     595..596,599,613,615,617,619..620,623..624,627)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          580..600
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          608..628
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..644
                     /gene="Zbtb1"
                     /gene_synonym="9430077A12; Bsg2; C430003J21Rik"
                     /coded_by="NM_001364323.1:228..2162"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:268564"
                     /db_xref="MGI:MGI:2442326"
ORIGIN      
        1 makpshssyv lqqlnnqrew gflcdcciai ddiyfqahka vlaacssyfr mffmnhqhst
       61 aqlnlsnmki saecfdlilq fmylgkimta pssfeqfkva mnylqlynvp dclediqdad
      121 cssskcsssa ssrqsskmif gvrmyedtva rngneanrwc aepsstvntp hhrepeeesl
      181 qlanfpeplf dvckkssvsk lstpkervsr rfgrsftcds cgfgfscekl ldehvltctn
      241 rhsyqnttra yhrivdirdg kdsnikaela ekdssktfsa qpdkyredan qapddsastt
      301 gsrkstveag iageeksrat etkriiikme pedipaddmk dfniikvtek dcnestdnde
      361 ledepeepfy ryyveedvgi kksgrktlkp rmsisvderg glenmrppnn tspiqedaen
      421 ascelcglti teedlsshyl akhienicac gkcgqilvkg rqlqehaqrc gepqdltmng
      481 lgnadekmdm eenpdeqsei rdmfvemldd frdnhyqins iqkkqlfkhs acpfrcpncg
      541 qrfetenlvv ehmsscldqd mfkgaimeen erdhrrkhfc nlcgkgfyqr chlrehytvh
      601 tkekqfvcqt cgkqflrerq lrlhndmhkg masgavgpsk plek
//
LOCUS       NP_037494                706 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 225 [Homo sapiens].
ACCESSION   NP_037494
VERSION     NP_037494.2
DBSOURCE    REFSEQ: accession NM_013362.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Shannon,M., Hamilton,A.T., Gordon,L., Branscomb,E. and Stubbs,L.
  TITLE     Differential expansion of zinc-finger transcription factor loci in
            homologous human and mouse gene clusters
  JOURNAL   Genome Res 13 (6A), 1097-1110 (2003)
   PUBMED   12743021
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EG328378.1, AK223477.1, BQ373092.1, AC021092.1 and BU633034.1.
            
            On Jul 14, 2006 this sequence version replaced NP_037494.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA337224.1, SRR1803611.63785.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262894.11/ ENSP00000262894.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..706
                     /product="zinc finger protein 225"
                     /calculated_mol_wt=82341
     Region          8..67
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          153..170
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          178..198
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(183,185,187,189..190,193..194,197,211,213,217..218,
                     221..222,225,239,241,243,245..246,249..250,253)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          202..634
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          206..226
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          234..254
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          262..282
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          290..310
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          318..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(323,325,327,329..330,333..334,337,351,353,357..358,
                     361..362,365,379,381,383,385..386,389..390,393)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          346..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          374..394
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          402..422
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          430..450
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          458..478
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(463,465,467,469..470,473..474,477,491,493,497..498,
                     501..502,505,519,521,523,525..526,529..530,533)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          486..506
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          514..534
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          542..562
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          570..590
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          598..618
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          626..646
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          654..672
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..706
                     /gene="ZNF225"
                     /coded_by="NM_013362.4:240..2360"
                     /db_xref="CCDS:CCDS46100.1"
                     /db_xref="GeneID:7768"
                     /db_xref="HGNC:HGNC:13018"
ORIGIN      
        1 mttlkeavtf kdvavvftee elrlldlaqr klyrevmlen frnllsvghq slhrdtfhfl
       61 keekfwmmet atqregnlgg kiqmemetvs esgtheglfs hqtweqissd ltrfqdsmvn
      121 sfqfskqddm pcqvdaglsi ihvrqkpseg rtckksfsdv svldlhqqlq srekshtcde
      181 cgksfcyssa lrihqrvhmg eklyncdvcg kefnqsshlq ihqrihtgek pfkceqcgkg
      241 fsrrsglyvh rklhtgvkph icekcgkafi hdsqlqehqr ihtgekpfkc diccksfrsr
      301 anlnrhsmvh mrekpfrcdt cgksfglksa lnshrmvhtg ekrykceecg krfiyrqdly
      361 khqidhtgek pynckecgks frwasglsrh vrvhsgettf kceecgkgfy tnsqryshqr
      421 ahsgekpyrc eecgkgykrr ldldfhqrvh rgekpyncke cgksfgwasc llnhqrihsg
      481 ekpfkceecg krftqnsqly thrrvhsgek pfkceecgkr ftqnsqlysh rrvhtgvkpy
      541 kceecgkgfn skfnldmhqr vhtgerpync kecgksfsra ssilnhkrlh gdekpfkcee
      601 cgkrftensq lhshqrvhtg ekpykcekcg ksfrwasthl thqrlhsrek llqcedcgks
      661 ivhssclkdq qrdqsgekts kcedcgkryk rrlnldtlls lflndt
//
LOCUS       NP_076438                235 aa            linear   PRI 27-APR-2025
DEFINITION  motile sperm domain-containing protein 3 isoform a [Homo sapiens].
ACCESSION   NP_076438
VERSION     NP_076438.1
DBSOURCE    REFSEQ: accession NM_023948.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Cabukusta,B., Berlin,I., van Elsland,D.M., Forkink,I., Spits,M., de
            Jong,A.W.M., Akkermans,J.J.L.L., Wijdeven,R.H.M., Janssen,G.M.C.,
            van Veelen,P.A. and Neefjes,J.
  TITLE     Human VAPome Analysis Reveals MOSPD1 and MOSPD3 as Membrane Contact
            Site Proteins Interacting with FFAT-Related FFNT Motifs
  JOURNAL   Cell Rep 33 (10), 108475 (2020)
   PUBMED   33296653
  REMARK    GeneRIF: Human VAPome Analysis Reveals MOSPD1 and MOSPD3 as
            Membrane Contact Site Proteins Interacting with FFAT-Related FFNT
            Motifs.
            Erratum:[Cell Rep. 2023 Jul 25;42(7):112849. doi:
            10.1016/j.celrep.2023.112849. PMID: 37440407]
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Pall,G.S., Wallis,J., Axton,R., Brownstein,D.G., Gautier,P.,
            Buerger,K., Mulford,C., Mullins,J.J. and Forrester,L.M.
  TITLE     A novel transmembrane MSP-containing protein that plays a role in
            right ventricle development
  JOURNAL   Genomics 84 (6), 1051-1059 (2004)
   PUBMED   15533722
  REMARK    GeneRIF: Deletion fo the Mospd3 locus is mutagenic and breeding to
            homozygosity results in a characteristic right ventricle defect and
            neonatal lethality in 50% of mice.
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Glockner,G., Scherer,S., Schattevoy,R., Boright,A., Weber,J.,
            Tsui,L.C. and Rosenthal,A.
  TITLE     Large-scale sequencing of two regions in human chromosome 7q22:
            analysis of 650 kb of genomic sequence around the EPO and CUTL1
            loci reveals 17 genes
  JOURNAL   Genome Res 8 (10), 1060-1073 (1998)
   PUBMED   9799793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC011653.2.
            
            Summary: This gene encodes a multi-pass membrane protein with a
            major sperm protein (MSP) domain. The deletion of a similar mouse
            gene is associated with defective cardiac development and neonatal
            lethality. Alternate transcriptional splice variants, encoding
            different isoforms, have been described. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1, 2 and 3
            encode the same isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011653.2, SRR3476690.1014050.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393950.7/ ENSP00000377522.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..235
                     /product="motile sperm domain-containing protein 3 isoform
                     a"
                     /note="motile sperm domain-containing protein 3"
                     /calculated_mol_wt=25388
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75425.1)"
     Region          41..133
                     /region_name="Motile_Sperm"
                     /note="MSP (Major sperm protein) domain; pfam00635"
                     /db_xref="CDD:459882"
     Region          143..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75425.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75425.1)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75425.1)"
     CDS             1..235
                     /gene="MOSPD3"
                     /gene_synonym="CDS3; NET30"
                     /coded_by="NM_023948.5:253..960"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5701.1"
                     /db_xref="GeneID:64598"
                     /db_xref="HGNC:HGNC:25078"
                     /db_xref="MIM:609125"
ORIGIN      
        1 mrrgapqdqe lvgpgppgrg srgappplgp vvpvlvfppd lvfradqrsg prqlltlynp
       61 tgtalrfrvl ctapakytvf daegyvkpqs cidivirhva pipshydvqd rfrielseeg
      121 aegrvvgrkd itsilrapay plelqgqpdp aprpgppagt ppptarhfqe hprqqlatss
      181 fllflltgiv svaflllplp delgsqlpqv lhvslgqklv aayvlglltm vflrt
//
LOCUS       NP_055445               1267 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 592 [Homo sapiens].
ACCESSION   NP_055445 XP_375247
VERSION     NP_055445.2
DBSOURCE    REFSEQ: accession NM_014630.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1267)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 1267)
  AUTHORS   Kamboh,M.I., Barmada,M.M., Demirci,F.Y., Minster,R.L.,
            Carrasquillo,M.M., Pankratz,V.S., Younkin,S.G., Saykin,A.J.,
            Sweet,R.A., Feingold,E., DeKosky,S.T. and Lopez,O.L.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     Genome-wide association analysis of age-at-onset in Alzheimer's
            disease
  JOURNAL   Mol Psychiatry 17 (12), 1340-1346 (2012)
   PUBMED   22005931
REFERENCE   3  (residues 1 to 1267)
  AUTHORS   Nicolas,E., Poitelon,Y., Chouery,E., Salem,N., Levy,N.,
            Megarbane,A. and Delague,V.
  TITLE     CAMOS, a nonprogressive, autosomal recessive, congenital cerebellar
            ataxia, is caused by a mutant zinc-finger protein, ZNF592
  JOURNAL   Eur J Hum Genet 18 (10), 1107-1113 (2010)
   PUBMED   20531441
  REMARK    GeneRIF: ZNF592 is idenified as the gene responsible for Cerebellar
            Ataxia with Mental retardation, Optic atrophy and Skin
            abnormalities, a rare, nonprogressive, cerebellar ataxia syndrome.
REFERENCE   4  (residues 1 to 1267)
  AUTHORS   Huang,J., Zheng,D.L., Qin,F.S., Cheng,N., Chen,H., Wan,B.B.,
            Wang,Y.P., Xiao,H.S. and Han,Z.G.
  TITLE     Genetic and epigenetic silencing of SCARA5 may contribute to human
            hepatocellular carcinoma by activating FAK signaling
  JOURNAL   J Clin Invest 120 (1), 223-241 (2010)
   PUBMED   20038795
  REMARK    GeneRIF: plasma membrane protein SCARA5 can contribute to human
            hepatocellular carcinoma (HCC) tumorigenesis and metastasis via
            activation of the FAK signaling pathway.
REFERENCE   5  (residues 1 to 1267)
  AUTHORS   Delague,V., Bareil,C., Bouvagnet,P., Salem,N., Chouery,E.,
            Loiselet,J., Megarbane,A. and Claustres,M.
  TITLE     A new autosomal recessive non-progressive congenital cerebellar
            ataxia associated with mental retardation, optic atrophy, and skin
            abnormalities (CAMOS) maps to chromosome 15q24-q26 in a large
            consanguineous Lebanese Druze Family
  JOURNAL   Neurogenetics 4 (1), 23-27 (2002)
   PUBMED   12030328
REFERENCE   6  (residues 1 to 1267)
  AUTHORS   Megarbane,A., Delague,V., Ruchoux,M.M., Rizkallah,E., Maurage,C.A.,
            Viollet,L., Rouaix-Emery,N. and Urtizberea,A.
  TITLE     New autosomal recessive cerebellar ataxia disorder in a large
            inbred Lebanese family
  JOURNAL   Am J Med Genet 101 (2), 135-141 (2001)
   PUBMED   11391656
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D86966.1, BQ217254.1,
            BG757479.1, AC012291.11 and AA835974.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 13, 2006 this sequence version replaced NP_055445.1.
            
            Summary: This gene is thought to play a role in a complex
            developmental pathway and the regulation of genes involved in
            cerebellar development. Mutations in this gene have been associated
            with autosomal recessive spinocerebellar ataxia. [provided by
            RefSeq, Jan 2011].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.157051.1,
                                           SRR1660809.70814.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000560079.7/ ENSP00000452877.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.3"
     Protein         1..1267
                     /product="zinc finger protein 592"
                     /calculated_mol_wt=137398
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92610.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92610.2)"
     Region          124..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92610.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q92610.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92610.2)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92610.2)"
     Region          <160..454
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          205..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92610.2)"
     Region          295..488
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92610.2)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92610.2)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92610.2)"
     Region          673..696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92610.2)"
     Site            689
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92610.2)"
     Site            691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92610.2)"
     Region          742..762
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(747,749,751,753..754,757..758,761,776,780..781,
                     784..785,816,834,836,838,840..841,844..845)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          770..817
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          829..845
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          918..970
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92610.2)"
     Region          985..1006
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          1015..1036
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1045..1065
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            1089
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92610.2)"
     Region          1151..1177
                     /region_name="zf-C2H2_11"
                     /note="zinc-finger C2H2-type; pfam16622"
                     /db_xref="CDD:465205"
     Region          1195..1267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92610.2)"
     Site            1205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BHZ4; propagated from
                     UniProtKB/Swiss-Prot (Q92610.2)"
     Site            1250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q92610.2)"
     CDS             1..1267
                     /gene="ZNF592"
                     /gene_synonym="CAMOS; SCAR5"
                     /coded_by="NM_014630.3:332..4135"
                     /db_xref="CCDS:CCDS32317.1"
                     /db_xref="GeneID:9640"
                     /db_xref="HGNC:HGNC:28986"
                     /db_xref="MIM:613624"
ORIGIN      
        1 mgdmktpdfd dllaafdipd ptsldakeai qtpseenesp lkppgicmde svslshsgsa
       61 pdvpavsviv kntsrqesfe aekdhitpsl lhngfrgsdl ppdphncgkf dstfmngdsa
      121 rsfpgklepp kseplptfnq fspisspepe dpikdngfgi kpkhsdsyfp pplgcgavgg
      181 pvlealakfp vpelhmfdhf ckkepkpepl plgsqqeheq sgqntvephk dpdatrffge
      241 alefnshpsn sigeskglar elgtcssvpp rqrlkpahsk lsscvaalva lqakrvasvt
      301 kedqpghtkd lsgptkessk gspkmpkspk sprspleatr ksikpsdspr sicsdssskg
      361 spsvaasspp aipkvrikti ktssgeikrt vtrilpdpdd pskspvgspl gsaiaeapse
      421 mpgdevpvee hfpeagtnsg spqgarkgde smtkasdsss pscssgprvp kgaapgsqtg
      481 kkqqstalqa stlapanllp kavhlanlnl vphsvaasvt akssvqrrsq pqltqmsvpl
      541 vhqvkkaapl ivevfnkvlh ssnpvplyap nlsppadsri hvpasgyccl ecgdafalek
      601 slsqhygrrs vhievlctlc sktllffnkc sllrhardhk skglvmqcsq llvkpisadq
      661 mfvsapvnst apaapapsss pkhgltsgsa sppppalply pdpvrlirys ikclechkqm
      721 rdymvlaahf qrtteetegl tcqvcqmllp nqcsfcahqr ihahkspycc pecgvlcrsa
      781 yfqthvkenc lhyarkvgyr cihcgvvhlt lallkshiqe rhcqvfhkca fcpmafktas
      841 stadhsatqh ptqphrpsql iykcscemvf nkkrhiqqhf yqnvsktqvg vfkcpecpll
      901 fvqkpelmqh vksthgvprn vdelsslqss adtsssrpgs rvpteppats vaarssslps
      961 grwgrpeahr rvearprlrn tgwtcqecqe wvpdresyvs hmkkshgrtl krypcrqceq
     1021 sfhtpnslrk hirnnhdtvk kfytcgycte dspsfprpsl leshislmhg irnpdlsqts
     1081 kvkppgghsp qvnhlkrpvs gvgdapgtsn gatvsstkrh kslfqcakcs fatdsglefq
     1141 shipqhqvds staqcllcgl cytsasslsr hlfivhkvrd qeeeeeeeaa aaemavevae
     1201 peegsgeevp metrenglee cageplsadp earrllgpap eddgghndhs qpqasqdqds
     1261 htlspqv
//
LOCUS       NP_006621                700 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 234 [Homo sapiens].
ACCESSION   NP_006621
VERSION     NP_006621.1
DBSOURCE    REFSEQ: accession NM_006630.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Shannon,M., Hamilton,A.T., Gordon,L., Branscomb,E. and Stubbs,L.
  TITLE     Differential expansion of zinc-finger transcription factor loci in
            homologous human and mouse gene clusters
  JOURNAL   Genome Res 13 (6A), 1097-1110 (2003)
   PUBMED   12743021
REFERENCE   3  (residues 1 to 700)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC021092.1, AK314064.1, AK289843.1 and AC138470.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.239303.1,
                                           SRR1803617.75103.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000426739.7/ ENSP00000400878.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..700
                     /product="zinc finger protein 234"
                     /note="zinc finger protein 269; C2-H2 type zinc finger
                     protein; Homo sapiens zinc finger 234; zinc finger protein
                     234, partial sequence; zinc finger protein 4; zinc finger
                     protein HZF4"
                     /calculated_mol_wt=80429
     Region          8..65
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          91..147
                     /region_name="KRNB"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14588.3)"
     Region          <101..306
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          150..170
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          178..198
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          202..>251
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          203..231
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          206..226
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(211,217,224,230,233,240)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          234..254
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          234..251
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          258..672
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          262..282
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(267,269,271,273..274,277..278,281,295,297,301..302,
                     305..306,309,323,325,327,329..330,333..334,337)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          290..310
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          318..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          346..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          374..394
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          402..422
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          430..450
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          458..478
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          486..506
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(491,493,495,497..498,501..502,505,519,521,525..526,
                     529..530,533,547,549,551,553..554,557..558,561)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          514..534
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          542..562
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          570..590
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          598..618
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(603,605,607,609..610,613..614,617,631,633,637..638,
                     641..642,645,659,661,663,665..666,669..670,673)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          626..646
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          654..674
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..700
                     /gene="ZNF234"
                     /gene_synonym="HZF4; ZNF269"
                     /coded_by="NM_006630.3:311..2413"
                     /db_xref="CCDS:CCDS46101.1"
                     /db_xref="GeneID:10780"
                     /db_xref="HGNC:HGNC:13027"
                     /db_xref="MIM:604750"
ORIGIN      
        1 mttfkegltf kdvavvftee elglldpvqr nlyqdvmlen frnllsvghh pfkhdvflle
       61 kekkldimkt atqrkgksad kiqsevetvp eagrheelyw gqiwkqiasd likyedsmis
      121 isrfprqgdl scqvraglyt thtgqkfyqc deykksftdv fnfdlhqqlh sgekshtcde
      181 cgksfcyisa lhihqrvhmg ekcykcdvcg kefsqsshlq thqrvhtvek pfkcvecgkg
      241 fsrrstltvh cklhsgekpy nceecgrafi hashlqehqr ihtgekpfkc dtcgknfrrr
      301 salnnhcmvh tgekpykced cgkcftcssn lrihqrvhtg ekpykceecg kcfiqpsqfq
      361 ahrrihtgek pyvckvcgkg fiysssfqah qgvhtgekpy kcnecgksfr mkihyqvhlv
      421 vhtgekpykc evcgkafrqs sylkihlkah svqkpfkcee cgqgfnqssr lqihqlihtg
      481 ekpykceecg kgfsrradlk ihcrihtgek pynceecgkv fsqashllth qrvhsgekpf
      541 kceecgksfs rsahlqahqk vhtgekpykc gecgkgfkws lnldmhqrvh tgekpytcge
      601 cgkhfsqass lqlhqsvhtg ekpykcdvcg kvfsrssqlq yhrrvhtgek pykceicgkr
      661 fswrsnlvsh hkihaagtfy endensknir elseggsstr
//
LOCUS       NP_004277                669 aa            linear   PRI 27-APR-2025
DEFINITION  GTP-binding protein 1 [Homo sapiens].
ACCESSION   NP_004277 NP_054746
VERSION     NP_004277.2
DBSOURCE    REFSEQ: accession NM_004286.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Salpietro,V., Maroofian,R., Zaki,M.S., Wangen,J., Ciolfi,A.,
            Barresi,S., Efthymiou,S., Lamaze,A., Aughey,G.N., Al Mutairi,F.,
            Rad,A., Rocca,C., Cali,E., Accogli,A., Zara,F., Striano,P.,
            Mojarrad,M., Tariq,H., Giacopuzzi,E., Taylor,J.C., Oprea,G.,
            Skrahina,V., Rehman,K.U., Abd Elmaksoud,M., Bassiony,M., El
            Said,H.G., Abdel-Hamid,M.S., Al Shalan,M., Seo,G., Kim,S., Lee,H.,
            Khang,R., Issa,M.Y., Elbendary,H.M., Rafat,K., Marinakis,N.M.,
            Traeger-Synodinos,J., Ververi,A., Sourmpi,M., Eslahi,A., Khadivi
            Zand,F., Beiraghi Toosi,M., Babaei,M., Jackson,A.,
            Bertoli-Avella,A., Pagnamenta,A.T., Niceta,M., Battini,R.,
            Corsello,A., Leoni,C., Chiarelli,F., Dallapiccola,B., Faqeih,E.A.,
            Tallur,K.K., Alfadhel,M., Alobeid,E., Maddirevula,S., Mankad,K.,
            Banka,S., Ghayoor-Karimiani,E., Tartaglia,M., Chung,W.K., Green,R.,
            Alkuraya,F.S., Jepson,J.E.C. and Houlden,H.
  CONSRTM   SYNAPS Study Group
  TITLE     Bi-allelic genetic variants in the translational GTPases GTPBP1 and
            GTPBP2 cause a distinct identical neurodevelopmental syndrome
  JOURNAL   Am J Hum Genet 111 (1), 200-210 (2024)
   PUBMED   38118446
  REMARK    GeneRIF: Bi-allelic genetic variants in the translational GTPases
            GTPBP1 and GTPBP2 cause a distinct identical neurodevelopmental
            syndrome.
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Zinoviev,A., Goyal,A., Jindal,S., LaCava,J., Komar,A.A.,
            Rodnina,M.V., Hellen,C.U.T. and Pestova,T.V.
  TITLE     Functions of unconventional mammalian translational GTPases GTPBP1
            and GTPBP2
  JOURNAL   Genes Dev 32 (17-18), 1226-1241 (2018)
   PUBMED   30108131
  REMARK    GeneRIF: GTPBP1 possesses eEF1A-like elongation activity,
            delivering cognate aminoacyl-transfer RNA to the ribosomal A site
            in a GTP-dependent manner. It also stimulates exosomal degradation
            of mRNAs in elongation complexes.
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 669)
  AUTHORS   Senju,S., Iyama,K., Kudo,H., Aizawa,S. and Nishimura,Y.
  TITLE     Immunocytochemical analyses and targeted gene disruption of GTPBP1
  JOURNAL   Mol Cell Biol 20 (17), 6195-6200 (2000)
   PUBMED   10938096
REFERENCE   7  (residues 1 to 669)
  AUTHORS   Kudo,H., Senju,S., Mitsuya,H. and Nishimura,Y.
  TITLE     Mouse and human GTPBP2, newly identified members of the GP-1 family
            of GTPase
  JOURNAL   Biochem Biophys Res Commun 272 (2), 456-465 (2000)
   PUBMED   10833435
REFERENCE   8  (residues 1 to 669)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   9  (residues 1 to 669)
  AUTHORS   Goretzki,L. and Mueller,B.M.
  TITLE     Low-density-lipoprotein-receptor-related protein (LRP) interacts
            with a GTP-binding protein
  JOURNAL   Biochem J 336 (Pt 2) (Pt 2), 381-386 (1998)
   PUBMED   9820815
REFERENCE   10 (residues 1 to 669)
  AUTHORS   Senju,S. and Nishimura,Y.
  TITLE     Identification of human and mouse GP-1, a putative member of a
            novel G-protein family
  JOURNAL   Biochem Biophys Res Commun 231 (2), 360-364 (1997)
   PUBMED   9070279
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF001482.1, BC014075.1,
            AK095950.1, BC016030.1 and BC001701.2.
            
            On Nov 18, 2005 this sequence version replaced NP_004277.1.
            
            Summary: This gene is upregulated by interferon-gamma and encodes a
            protein that is a member of the AGP11/GTPBP1 family of GTP-binding
            proteins. A structurally similar protein has been found in mouse,
            where disruption of the gene for that protein had no observable
            phenotype. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.199191.1,
                                           SRR1660807.264517.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216044.10/ ENSP00000216044.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..669
                     /product="GTP-binding protein 1"
                     /note="G-protein 1"
                     /calculated_mol_wt=72323
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00178.3)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08582; propagated from
                     UniProtKB/Swiss-Prot (O00178.3)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08582; propagated from
                     UniProtKB/Swiss-Prot (O00178.3)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00178.3)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08582; propagated from
                     UniProtKB/Swiss-Prot (O00178.3)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O00178.3)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00178.3)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00178.3)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00178.3)"
     Region          77..574
                     /region_name="GTPBP1"
                     /note="GTPase [General function prediction only]; COG5258"
                     /db_xref="CDD:444076"
     Region          167..174
                     /region_name="G1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (O00178.3)"
     Region          206..210
                     /region_name="G2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (O00178.3)"
     Region          252..255
                     /region_name="G3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (O00178.3)"
     Region          308..311
                     /region_name="G4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (O00178.3)"
     Region          366..368
                     /region_name="G5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (O00178.3)"
     Region          573..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00178.3)"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00178.3)"
     CDS             1..669
                     /gene="GTPBP1"
                     /gene_synonym="GP-1; GP1; HSPC018; NEDFET1"
                     /coded_by="NM_004286.5:13..2022"
                     /db_xref="CCDS:CCDS13977.2"
                     /db_xref="GeneID:9567"
                     /db_xref="HGNC:HGNC:4669"
                     /db_xref="MIM:602245"
ORIGIN      
        1 matersrsam dspvpasmfa pepsspgaar aaaaaarlhg gfdsdcsedg ealngepeld
       61 ltsklvlvsp tseqydsllr qmwermdegc getiyvigqg sdgteyglse admeasyatv
      121 ksmaeqiead villrerqea ggrvrdylvr krvgdndfle vrvavvgnvd agkstllgvl
      181 thgeldngrg farqklfrhk heiesgrtss vgndilgfds egnvvnkpds hggslewtki
      241 cekstkvitf idlaghekyl kttvfgmtgh lpdfcmlmvg snagivgmtk ehlglalaln
      301 vpvfvvvtki dmcpanilqe tlkllqrllk spgcrkipvl vqskddvivt asnfssermc
      361 pifqisnvtg enldllkmfl nllsprtsyr eeepaefqid dtysvpgvgt vvsgttlrgl
      421 iklndtlllg pdplgnflsi avksihrkrm pvkevrggqt asfalkkikr ssirkgmvmv
      481 sprlnpqasw efeaeilvlh hpttispryq amvhcgsirq tatilsmdkd clrtgdkatv
      541 hfrfiktpey lhidqrlvfr egrtkavgti tkllqttnns pmnskpqqik mqstkkgplt
      601 krdeggpsgg pavgapppgd eassvgagqp aassnlqpqp kpssggrrrg gqrhkvksqg
      661 acvtpasgc
//
LOCUS       NP_001629                326 aa            linear   PRI 27-APR-2025
DEFINITION  apolipoprotein F preproprotein [Homo sapiens].
ACCESSION   NP_001629
VERSION     NP_001629.1
DBSOURCE    REFSEQ: accession NM_001638.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Shi,X., Feng,D., Li,D., Han,P., Yang,L. and Wei,W.
  TITLE     A pan-cancer analysis of the oncogenic and immunological roles of
            apolipoprotein F (APOF) in human cancer
  JOURNAL   Eur J Med Res 28 (1), 190 (2023)
   PUBMED   37312170
  REMARK    GeneRIF: A pan-cancer analysis of the oncogenic and immunological
            roles of apolipoprotein F (APOF) in human cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Deprince,A., Hennuyer,N., Kooijman,S., Pronk,A.C.M., Bauge,E.,
            Lienard,V., Verrijken,A., Dirinck,E., Vonghia,L., Woitrain,E.,
            Kloosterhuis,N.J., Marez,E., Jacquemain,P., Wolters,J.C.,
            Lalloyer,F., Eberle,D., Quemener,S., Vallez,E., Tailleux,A.,
            Kouach,M., Goossens,J.F., Raverdy,V., Derudas,B., Kuivenhoven,J.A.,
            Croyal,M., van de Sluis,B., Francque,S., Pattou,F., Rensen,P.C.N.,
            Staels,B. and Haas,J.T.
  TITLE     Apolipoprotein F is reduced in humans with steatosis and controls
            plasma triglyceride-rich lipoprotein metabolism
  JOURNAL   Hepatology 77 (4), 1287-1302 (2023)
   PUBMED   35735979
  REMARK    GeneRIF: Apolipoprotein F is reduced in humans with steatosis and
            controls plasma triglyceride-rich lipoprotein metabolism.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Morton,R.E. and Mihna,D.
  TITLE     Apolipoprotein F concentration, activity, and the properties of LDL
            controlling ApoF activation in hyperlipidemic plasma
  JOURNAL   J Lipid Res 63 (2), 100166 (2022)
   PUBMED   35016907
  REMARK    GeneRIF: Apolipoprotein F concentration, activity, and the
            properties of LDL controlling ApoF activation in hyperlipidemic
            plasma.
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Kumar,A., Gangadharan,B., Cobbold,J., Thursz,M. and Zitzmann,N.
  TITLE     Absolute quantitation of disease protein biomarkers in a single
            LC-MS acquisition using apolipoprotein F as an example
  JOURNAL   Sci Rep 7 (1), 12072 (2017)
   PUBMED   28935895
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Paromov,V.M. and Morton,R.E.
  TITLE     Lipid transfer inhibitor protein defines the participation of high
            density lipoprotein subfractions in lipid transfer reactions
            mediated by cholesterol ester transfer protein (CETP)
  JOURNAL   J Biol Chem 278 (42), 40859-40866 (2003)
   PUBMED   12907677
  REMARK    GeneRIF: LTIP tailors CETP-mediated remodeling of HDL3 and HDL2
            particles in subclass-specific ways, strongly implicating it as a
            regulator of HDL metabolism
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Wang,X., Driscoll,D.M. and Morton,R.E.
  TITLE     Molecular cloning and expression of lipid transfer inhibitor
            protein reveals its identity with apolipoprotein F
  JOURNAL   J Biol Chem 274 (3), 1814-1820 (1999)
   PUBMED   9880564
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Day,J.R., Albers,J.J., Gilbert,T.L., Whitmore,T.E., McConathy,W.J.
            and Wolfbauer,G.
  TITLE     Purification and molecular cloning of human apolipoprotein F
  JOURNAL   Biochem Biophys Res Commun 203 (2), 1146-1151 (1994)
   PUBMED   8093033
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Koren,E., McConathy,W.J. and Alaupovic,P.
  TITLE     Isolation and characterization of simple and complex lipoproteins
            containing apolipoprotein F from human plasma
  JOURNAL   Biochemistry 21 (21), 5347-5351 (1982)
   PUBMED   6816269
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Olofsson,S.O., McConathy,W.J. and Alaupovic,P.
  TITLE     Isolation and partial characterization of a new acidic
            apolipoprotein (apolipoprotein F) from high density lipoproteins of
            human plasma
  JOURNAL   Biochemistry 17 (6), 1032-1036 (1978)
   PUBMED   204339
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC025574.19.
            
            Summary: The product of this gene is one of the minor
            apolipoproteins found in plasma. This protein forms complexes with
            lipoproteins and may be involved in transport and/or esterification
            of cholesterol. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.61956.1,
                                           SRR5189664.103843.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2145122
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000398189.4/
                                                ENSP00000381250.3
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..326
                     /product="apolipoprotein F preproprotein"
                     /note="lipid transfer inhibitor protein"
                     /calculated_mol_wt=31500
     sig_peptide     1..35
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13790.2)"
                     /calculated_mol_wt=3918
     proprotein      36..326
                     /product="apolipoprotein F proprotein"
                     /calculated_mol_wt=31500
     Region          62..260
                     /region_name="Apolipo_F"
                     /note="Apolipoprotein F; pfam15148"
                     /db_xref="CDD:464532"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13790.2)"
     mat_peptide     165..326
                     /product="Apolipoprotein F. /id=PRO_0000002052"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13790.2)"
                     /calculated_mol_wt=17425
     Site            274
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:22171320; propagated from
                     UniProtKB/Swiss-Prot (Q13790.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:28935895,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13790.2)"
     CDS             1..326
                     /gene="APOF"
                     /gene_synonym="Apo-F; LTIP"
                     /coded_by="NM_001638.4:113..1093"
                     /db_xref="CCDS:CCDS44923.1"
                     /db_xref="GeneID:319"
                     /db_xref="HGNC:HGNC:615"
                     /db_xref="MIM:107760"
ORIGIN      
        1 mtglcgysap dmrglrlimi pvelllcyll lhpvdatsyg kqtnvlmhfp lslesqtpss
       61 dplscqflhp kslpgfshma plpkflvsla lrnaleeagc qadvwalqlq lyrqggvnat
      121 qvliqhlrgl qkgrsternv svealasalq llareqqstg rvgrslpted cenekeqavh
      181 nvvqllpgvg tfynlgtaly yatqnclgka rergrdgaid lgydllmtma gmsggpmgla
      241 isaalkpalr sgvqqliqyy qdqkdanisq pettkeglra isdvsdleet ttlasfisev
      301 vssapywgwa iiksydldpg agslei
//
LOCUS       NP_080125                111 aa            linear   ROD 27-APR-2025
DEFINITION  distal membrane-arm assembly complex protein 1 [Mus musculus].
ACCESSION   NP_080125
VERSION     NP_080125.1
DBSOURCE    REFSEQ: accession NM_025849.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY074394.1, AK013937.1 and DV644498.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB193938.1, BC022621.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 36.66 cM"
     Protein         1..111
                     /product="distal membrane-arm assembly complex protein 1"
                     /note="transmembrane protein C9orf123 homolog;
                     transmembrane protein 261"
                     /calculated_mol_wt=11213
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQ00.1)"
     Region          46..91
                     /region_name="DUF4536"
                     /note="Domain of unknown function (DUF4536); pfam15055"
                     /db_xref="CDD:464474"
     Site            51..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQ00.1)"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQ00.1)"
     CDS             1..111
                     /gene="Dmac1"
                     /gene_synonym="1700027K24Rik; 3110001D03Rik; Tmem261"
                     /coded_by="NM_025849.4:42..377"
                     /db_xref="CCDS:CCDS18288.1"
                     /db_xref="GeneID:66928"
                     /db_xref="MGI:MGI:1914178"
ORIGIN      
        1 mgssfsgste fsapapptvs tavpanppak savpaspard pelktcwscr vlsgstlfga
       61 gtyvylvarr plkqgippgp gtvlqmvigi siacwgvvvl vdpkgkshpv i
//
LOCUS       NP_003008                164 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine-rich splicing factor 3 [Homo sapiens].
ACCESSION   NP_003008
VERSION     NP_003008.1
DBSOURCE    REFSEQ: accession NM_003017.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Zhang,L., Zhang,H., Tang,Y., Dai,C. and Zheng,J.
  TITLE     SRSF3 suppresses RCC tumorigenesis and progression via regulating
            SP4 alternative splicing
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119841 (2024)
   PUBMED   39222664
  REMARK    GeneRIF: SRSF3 suppresses RCC tumorigenesis and progression via
            regulating SP4 alternative splicing.
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Gao,H., Rocha,K.C.E., Jin,Z., Kumar,D., Zhang,D., Wang,K., Das,M.,
            Farrell,A., Truong,T., Tekin,Y., Jung,H.S., Kempf,J.,
            Webster,N.J.G. and Ying,W.
  TITLE     Restoring SRSF3 in Kupffer cells attenuates obesity-related insulin
            resistance
  JOURNAL   Hepatology 80 (2), 363-375 (2024)
   PUBMED   38456794
  REMARK    GeneRIF: Restoring SRSF3 in Kupffer cells attenuates
            obesity-related insulin resistance.
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Sue,S.H., Liu,S.T. and Huang,S.M.
  TITLE     Factors affecting the expression and stability of full-length and
            truncated SRSF3 proteins in human cancer cells
  JOURNAL   Sci Rep 14 (1), 14397 (2024)
   PUBMED   38909100
  REMARK    GeneRIF: Factors affecting the expression and stability of
            full-length and truncated SRSF3 proteins in human cancer cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 164)
  AUTHORS   More,D.A., Singh,N., Mishra,R., Muralidharan,H.P., Gopinath,K.S.,
            Gopal,C. and Kumar,A.
  TITLE     Intronic miR-6741-3p targets the oncogene SRSF3: Implications for
            oral squamous cell carcinoma pathogenesis
  JOURNAL   PLoS One 19 (5), e0296565 (2024)
   PUBMED   38781195
  REMARK    GeneRIF: Intronic miR-6741-3p targets the oncogene SRSF3:
            Implications for oral squamous cell carcinoma pathogenesis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Caceres,J.F., Screaton,G.R. and Krainer,A.R.
  TITLE     A specific subset of SR proteins shuttles continuously between the
            nucleus and the cytoplasm
  JOURNAL   Genes Dev 12 (1), 55-66 (1998)
   PUBMED   9420331
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Gui,J.F., Lane,W.S. and Fu,X.D.
  TITLE     A serine kinase regulates intracellular localization of splicing
            factors in the cell cycle
  JOURNAL   Nature 369 (6482), 678-682 (1994)
   PUBMED   8208298
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Zahler,A.M., Lane,W.S., Stolk,J.A. and Roth,M.B.
  TITLE     SR proteins: a conserved family of pre-mRNA splicing factors
  JOURNAL   Genes Dev 6 (5), 837-847 (1992)
   PUBMED   1577277
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Ayane,M., Preuss,U., Kohler,G. and Nielsen,P.J.
  TITLE     A differentially expressed murine RNA encoding a protein with
            similarities to two types of nucleic acid binding motifs
  JOURNAL   Nucleic Acids Res 19 (6), 1273-1278 (1991)
   PUBMED   2030943
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z85986.1.
            
            Summary: The protein encoded by this gene is a member of the
            serine/arginine (SR)-rich family of pre-mRNA splicing factors,
            which constitute part of the spliceosome. Each of these factors
            contains an RNA recognition motif (RRM) for binding RNA and an RS
            domain for binding other proteins. The RS domain is rich in serine
            and arginine residues and facilitates interaction between different
            SR splicing factors. In addition to being critical for mRNA
            splicing, the SR proteins have also been shown to be involved in
            mRNA export from the nucleus and in translation. Two transcript
            variants, one protein-coding and the other non-coding, have been
            found for this gene. [provided by RefSeq, Sep 2010].
            
            Transcript Variant: This variant (1) is the protein-coding variant.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.150012.1,
                                           SRR1803614.13020.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373715.11/ ENSP00000362820.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31-p21.2"
     Protein         1..164
                     /product="serine/arginine-rich splicing factor 3"
                     /note="splicing factor, arginine/serine-rich 3; splicing
                     factor, arginine/serine-rich, 20-kD; pre-mRNA-splicing
                     factor SRP20; pre-mRNA splicing factor SRp20; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=19198
     Region          1..90
                     /region_name="Sufficient for interaction with NXF1 and
                     SRSP. /evidence=ECO:0000269|PubMed:12667464,
                     ECO:0000269|PubMed:17036044, ECO:0000269|PubMed:32440474"
                     /note="propagated from UniProtKB/Swiss-Prot (P84103.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P84103.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P84103.1)"
     Region          6..86
                     /region_name="RRM_SRSF3"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     serine/arginine-rich splicing factor 3 (SRSF3); cd12645"
                     /db_xref="CDD:241089"
     Site            23
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P84103.1)"
     Site            order(40,42..44,46,48,50,81,83)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:241089"
     Region          81..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84103.1)"
     Region          119..164
                     /region_name="2 X approximate repeats, basic"
                     /note="propagated from UniProtKB/Swiss-Prot (P84103.1)"
     CDS             1..164
                     /gene="SRSF3"
                     /gene_synonym="SFRS3; SRp20"
                     /coded_by="NM_003017.5:123..617"
                     /db_xref="CCDS:CCDS4823.1"
                     /db_xref="GeneID:6428"
                     /db_xref="HGNC:HGNC:10785"
                     /db_xref="MIM:603364"
ORIGIN      
        1 mhrdscpldc kvyvgnlgnn gnkteleraf gyygplrsvw varnppgfaf vefedprdaa
       61 davreldgrt lcgcrvrvel sngekrsrnr gpppswgrrp rddyrrrspp prrrsprrrs
      121 fsrsrsrsls rdrrrersls rernhkpsrs fsrsrsrsrs nerk
//
LOCUS       NP_004379                385 aa            linear   PRI 27-APR-2025
DEFINITION  di-N-acetylchitobiase precursor [Homo sapiens].
ACCESSION   NP_004379
VERSION     NP_004379.1
DBSOURCE    REFSEQ: accession NM_004388.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Olszewski,S., Olszewska,E., Popko,J., Poskrobko,E., Sierakowski,S.
            and Zwierz,K.
  TITLE     Fibroblast-Like Synovial Cells in Rheumatoid Arthritis--the Impact
            of Infliximab on Hexosaminidase Activity
  JOURNAL   Adv Clin Exp Med 24 (5), 807-813 (2015)
   PUBMED   26768631
  REMARK    GeneRIF: Data indicate that infliximab changes the concentration of
            hexosaminidase (N-acetyl-beta-glucosaminidase; HEX) activity
            depending on the drug dose and time of administration.
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Aronson,N.N. and Halloran,B.A.
  TITLE     Optimum substrate size and specific anomer requirements for the
            reducing-end glycoside hydrolase di-N-acetylchitobiase
  JOURNAL   Biosci Biotechnol Biochem 70 (6), 1537-1541 (2006)
   PUBMED   16794344
  REMARK    GeneRIF: biochemical behavior of di-N-acetylchitobiase indicates it
            has three subsites, -2, -1, +1, in which the reducing-end trimer of
            any sized chitooligosaccharide is bound. The +1 site is specific
            for an alpha-anomer.
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Hutchinson,T., Dwivedi,K., Rastogi,A., Prasad,R. and Pereira,B.M.
  TITLE     N-acetyl beta-D-glucosaminidase is not attached to human sperm
            membranes through the glycosylphosphatidyl inositol (GPI)-anchor
  JOURNAL   Asian J Androl 4 (1), 27-33 (2002)
   PUBMED   11907625
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Liu,B., Ahmad,W. and Aronson,N.N. Jr.
  TITLE     Structure of the human gene for lysosomal di-N-acetylchitobiase
  JOURNAL   Glycobiology 9 (6), 589-593 (1999)
   PUBMED   10336991
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Ahmad,W., Li,S., Chen,H., Tuck-Muller,C.M., Pittler,S.J. and
            Aronson,N.N. Jr.
  TITLE     Lysosomal chitobiase (CTB) and the G-protein gamma 5 subunit (GNG5)
            genes co-localize to human chromosome 1p22
  JOURNAL   Cytogenet Cell Genet 71 (1), 44-46 (1995)
   PUBMED   7606925
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Fisher,K.J. and Aronson,N.N. Jr.
  TITLE     Cloning and expression of the cDNA sequence encoding the lysosomal
            glycosidase di-N-acetylchitobiase
  JOURNAL   J Biol Chem 267 (27), 19607-19616 (1992)
   PUBMED   1527079
REFERENCE   8  (residues 1 to 385)
  AUTHORS   Fisher,K.J. and Aronson,N.N. Jr.
  TITLE     Characterization of the cDNA and genomic sequence of a G protein
            gamma subunit (gamma 5)
  JOURNAL   Mol Cell Biol 12 (4), 1585-1591 (1992)
   PUBMED   1549114
REFERENCE   9  (residues 1 to 385)
  AUTHORS   Aronson,N.N. Jr. and Kuranda,M.J.
  TITLE     Lysosomal degradation of Asn-linked glycoproteins
  JOURNAL   FASEB J 3 (14), 2615-2622 (1989)
   PUBMED   2531691
  REMARK    Review article
REFERENCE   10 (residues 1 to 385)
  AUTHORS   Aronson,N.N. Jr., Backes,M. and Kuranda,M.J.
  TITLE     Rat liver chitobiase: purification, properties, and role in the
            lysosomal degradation of Asn-linked glycoproteins
  JOURNAL   Arch Biochem Biophys 272 (2), 290-300 (1989)
   PUBMED   2751306
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC126335.1, BC065191.1, AI339601.1 and AL359762.24.
            
            Summary: Chitobiase is a lysosomal glycosidase involved in
            degradation of asparagine-linked oligosaccharides on glycoproteins
            (Aronson and Kuranda, 1989 [PubMed 2531691]).[supplied by OMIM, Nov
            2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298703.1, SRR1660809.252331.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370630.6/ ENSP00000359664.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.3"
     Protein         1..385
                     /product="di-N-acetylchitobiase precursor"
                     /EC_number="3.2.1.-"
                     /note="di-N-acetylchitobiase; chitobiase, di-N-acetyl-"
                     /calculated_mol_wt=39756
     sig_peptide     1..38
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4022
     mat_peptide     39..385
                     /product="Di-N-acetylchitobiase. /id=PRO_0000011961"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01459.1)"
                     /calculated_mol_wt=39756
     Region          39..378
                     /region_name="GH18_chitobiase"
                     /note="Chitobiase (also known as di-N-acetylchitobiase) is
                     a lysosomal glycosidase that hydrolyzes the reducing-end
                     N-acetylglucosamine from the chitobiose core of
                     oligosaccharides during the ordered degradation of
                     asparagine-linked glycoproteins in eukaryotes; cd02875"
                     /db_xref="CDD:119354"
     Site            order(48,75,139,141,143,209..210,254,354)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:119354"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01459.1)"
     Site            228
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01459.1)"
     Site            262
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01459.1)"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q01459.1)"
     CDS             1..385
                     /gene="CTBS"
                     /gene_synonym="CTB"
                     /coded_by="NM_004388.3:26..1183"
                     /db_xref="CCDS:CCDS698.1"
                     /db_xref="GeneID:1486"
                     /db_xref="HGNC:HGNC:2496"
                     /db_xref="MIM:600873"
ORIGIN      
        1 msrpqlrrwr lvssppsgvp glallallal lalrlaagtd cpcpepelcr pirhhpdfev
       61 fvfdvgqktw ksydwsqitt vatfgkydse lmcyahskga rvvlkgdvsl kdiidpafra
      121 swiaqklnla ktqymdgini dieqevncls peydaltalv kettdsfhre iegsqvtfdv
      181 awspknidrr cynytgiada cdflfvmsyd eqsqiwseci aaanapynqt ltgyndyikm
      241 sinpkklvmg vpwygydytc lnlsedhvct iakvpfrgap csdaagrqvp yktimkqins
      301 sisgnlwdkd qrapyynykd paghfhqvwy dnpqsislka tyiqnyrlrg igmwnancld
      361 ysgdavakqq teemwevlkp kllqr
//
LOCUS       NP_008978                334 aa            linear   PRI 27-APR-2025
DEFINITION  butyrophilin subfamily 3 member A2 isoform a precursor [Homo
            sapiens].
ACCESSION   NP_008978
VERSION     NP_008978.2
DBSOURCE    REFSEQ: accession NM_007047.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Vantourout,P., Laing,A., Woodward,M.J., Zlatareva,I., Apolonia,L.,
            Jones,A.W., Snijders,A.P., Malim,M.H. and Hayday,A.C.
  TITLE     Heteromeric interactions regulate butyrophilin (BTN) and BTN-like
            molecules governing gammadelta T cell biology
  JOURNAL   Proc Natl Acad Sci U S A 115 (5), 1039-1044 (2018)
   PUBMED   29339503
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Horsburgh,S., Ciechomska,M. and O'Reilly,S.
  TITLE     CpG-specific methylation at rheumatoid arthritis diagnosis as a
            marker of treatment response
  JOURNAL   Epigenomics 9 (5), 595-597 (2017)
   PUBMED   28447857
  REMARK    GeneRIF: CpG-specific DNA methylation of ADAMTSL2 and BTN3A2 at
            rheumatoid arthritis diagnosis can serve as a marker of treatment
            response.
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Viken,M.K., Blomhoff,A., Olsson,M., Akselsen,H.E., Pociot,F.,
            Nerup,J., Kockum,I., Cambon-Thomsen,A., Thorsby,E., Undlien,D.E.
            and Lie,B.A.
  TITLE     Reproducible association with type 1 diabetes in the extended class
            I region of the major histocompatibility complex
  JOURNAL   Genes Immun 10 (4), 323-333 (2009)
   PUBMED   19295542
  REMARK    GeneRIF: our results identify PRSS16 and BTN3A2, two genes thought
            to play important roles in regulating the immune response, as
            potentially novel susceptibility genes for Type I Deabetes.
            GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Cavaletto,M., Giuffrida,M.G., Fortunato,D., Gardano,L.,
            Dellavalle,G., Napolitano,L., Giunta,C., Bertino,E., Fabris,C. and
            Conti,A.
  TITLE     A proteomic approach to evaluate the butyrophilin gene family
            expression in human milk fat globule membrane
  JOURNAL   Proteomics 2 (7), 850-856 (2002)
   PUBMED   12124930
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Rhodes,D.A., Stammers,M., Malcherek,G., Beck,S. and Trowsdale,J.
  TITLE     The cluster of BTN genes in the extended major histocompatibility
            complex
  JOURNAL   Genomics 71 (3), 351-362 (2001)
   PUBMED   11170752
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Ruddy,D.A., Kronmal,G.S., Lee,V.K., Mintier,G.A., Quintana,L.,
            Domingo,R. Jr., Meyer,N.C., Irrinki,A., McClelland,E.E., Fullan,A.,
            Mapa,F.A., Moore,T., Thomas,W., Loeb,D.B., Harmon,C.,
            Tsuchihashi,Z., Wolff,R.K., Schatzman,R.C. and Feder,J.N.
  TITLE     A 1.1-Mb transcript map of the hereditary hemochromatosis locus
  JOURNAL   Genome Res 7 (5), 441-456 (1997)
   PUBMED   9149941
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Tazi-Ahnini,R., Henry,J., Offer,C., Bouissou-Bouchouata,C.,
            Mather,I.H. and Pontarotti,P.
  TITLE     Cloning, localization, and structure of new members of the
            butyrophilin gene family in the juxta-telomeric region of the major
            histocompatibility complex
  JOURNAL   Immunogenetics 47 (1), 55-63 (1997)
   PUBMED   9382921
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD705662.1, AK290880.1,
            BC020214.1 and AL021917.4.
            
            On Sep 23, 2003 this sequence version replaced NP_008978.1.
            
            Summary: This gene encodes a member of the immunoglobulin
            superfamily, which resides in the juxta-telomeric region of the
            major histocompatability class 1 locus and is clustered with the
            other family members on chromosome 6. The encoded protein may be
            involved in the adaptive immune response. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1-3 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U90546.1, SRR1803614.239473.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377708.7/ ENSP00000366937.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.2"
     Protein         1..334
                     /product="butyrophilin subfamily 3 member A2 isoform a
                     precursor"
                     /note="butyrophilin protein"
                     /calculated_mol_wt=33284
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3162
     mat_peptide     30..334
                     /product="Butyrophilin subfamily 3 member A2.
                     /id=PRO_0000014533"
                     /note="propagated from UniProtKB/Swiss-Prot (P78410.2)"
                     /calculated_mol_wt=33284
     Region          31..144
                     /region_name="IgV_MOG_like"
                     /note="Immunoglobulin (Ig)-like domain of myelin
                     oligodendrocyte glycoprotein (MOG); cd05713"
                     /db_xref="CDD:409378"
     Region          31..54
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409378"
     Region          32..36
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409378"
     Region          39..43
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409378"
     Region          46..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409378"
     Region          55..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409378"
     Site            order(61..62,81,92,129..130,132..133,135..136)
                     /site_type="other"
                     /note="Fab binding site [polypeptide binding]"
                     /db_xref="CDD:409378"
     Region          63..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409378"
     Region          64..68
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409378"
     Region          69..87
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409378"
     Region          73..81
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409378"
     Region          82..85
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409378"
     Region          89..129
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409378"
     Region          96..101
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409378"
     Region          107..115
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409378"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78410.2)"
     Region          122..130
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409378"
     Region          130..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409378"
     Region          132..144
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409378"
     Region          133..144
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409378"
     Region          151..228
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          162..166
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          176..180
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          206..210
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          217..222
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P78410.2)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78410.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78410.2)"
     CDS             1..334
                     /gene="BTN3A2"
                     /gene_synonym="BT3.2; BTF4; BTN3.2; CD277"
                     /coded_by="NM_007047.5:222..1226"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4605.1"
                     /db_xref="GeneID:11118"
                     /db_xref="HGNC:HGNC:1139"
                     /db_xref="MIM:613594"
ORIGIN      
        1 mkmasslafl llnfhvslll vqlltpcsaq fsvlgpsgpi lamvgedadl pchlfptmsa
       61 etmelkwvss slrqvvnvya dgkevedrqs apyrgrtsil rdgitagkaa lrihnvtasd
      121 sgkylcyfqd gdfyekalve lkvaalgsnl hvevkgyedg gihlecrstg wypqpqiqws
      181 nakgenipav eapvvadgvg lyevaasvim rggsgegvsc iirnsllgle ktasisiadp
      241 ffrsaqpwia alagtlpill lllagasyfl wrqqkeital sseieseqem kemgyaater
      301 eislreslqe elkrkkiqyl trgeesssdt nksa
//
LOCUS       NP_001186127             699 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 23 isoform 1 [Homo sapiens].
ACCESSION   NP_001186127
VERSION     NP_001186127.1
DBSOURCE    REFSEQ: accession NM_001199198.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Zhao,L., Deng,H., Yang,Q., Tang,Y., Zhao,J., Li,P., Zhang,S.,
            Yong,X., Li,T., Billadeau,D.D. and Jia,D.
  TITLE     FAM91A1-TBC1D23 complex structure reveals human genetic variations
            susceptible for PCH
  JOURNAL   Proc Natl Acad Sci U S A 120 (45), e2309910120 (2023)
   PUBMED   37903274
  REMARK    GeneRIF: FAM91A1-TBC1D23 complex structure reveals human genetic
            variations susceptible for PCH.
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Zhang,Y., Su,H., Wudu,M., Ren,H., Xu,Y., Zhang,Q., Jiang,J.,
            Wang,Q., Jiang,X., Zhang,B., Liu,Z., Zou,Z. and Qiu,X.
  TITLE     TBC1 domain family member 23 interacts with Ras-related protein
            Rab-11A to promote poor prognosis of non-small-cell lung cancer via
            beta1-integrin
  JOURNAL   J Cell Mol Med 25 (18), 8821-8835 (2021)
   PUBMED   34363324
  REMARK    GeneRIF: TBC1 domain family member 23 interacts with Ras-related
            protein Rab-11A to promote poor prognosis of non-small-cell lung
            cancer via beta1-integrin.
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 699)
  AUTHORS   Liu,D., Yang,F., Liu,Z., Wang,J., Huang,W., Meng,W.,
            Billadeau,D.D., Sun,Q., Mo,X. and Jia,D.
  TITLE     Structure of TBC1D23 N-terminus reveals a novel role for rhodanese
            domain
  JOURNAL   PLoS Biol 18 (5), e3000746 (2020)
   PUBMED   32453802
  REMARK    GeneRIF: rhodanese domain packs against the TBC domain and forms
            part of the platform to interact with golgin-97/245
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 699)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 699)
  AUTHORS   Marin-Valencia,I., Gerondopoulos,A., Zaki,M.S., Ben-Omran,T.,
            Almureikhi,M., Demir,E., Guemez-Gamboa,A., Gregor,A., Issa,M.Y.,
            Appelhof,B., Roosing,S., Musaev,D., Rosti,B., Wirth,S., Stanley,V.,
            Baas,F., Barr,F.A. and Gleeson,J.G.
  TITLE     Homozygous Mutations in TBC1D23 Lead to a Non-degenerative Form of
            Pontocerebellar Hypoplasia
  JOURNAL   Am J Hum Genet 101 (3), 441-450 (2017)
   PUBMED   28823706
  REMARK    GeneRIF: Homozygous Mutations in TBC1D23 gene are associated with
            Non-degenerative Form of Pontocerebellar Hypoplasia.
REFERENCE   7  (residues 1 to 699)
  AUTHORS   Cheng,C.Y., Schache,M., Ikram,M.K., Young,T.L., Guggenheim,J.A.,
            Vitart,V., MacGregor,S., Verhoeven,V.J., Barathi,V.A., Liao,J.,
            Hysi,P.G., Bailey-Wilson,J.E., St Pourcain,B., Kemp,J.P.,
            McMahon,G., Timpson,N.J., Evans,D.M., Montgomery,G.W., Mishra,A.,
            Wang,Y.X., Wang,J.J., Rochtchina,E., Polasek,O., Wright,A.F.,
            Amin,N., van Leeuwen,E.M., Wilson,J.F., Pennell,C.E., van
            Duijn,C.M., de Jong,P.T., Vingerling,J.R., Zhou,X., Chen,P., Li,R.,
            Tay,W.T., Zheng,Y., Chew,M., Burdon,K.P., Craig,J.E., Iyengar,S.K.,
            Igo,R.P. Jr., Lass,J.H. Jr., Chew,E.Y., Haller,T., Mihailov,E.,
            Metspalu,A., Wedenoja,J., Simpson,C.L., Wojciechowski,R., Hohn,R.,
            Mirshahi,A., Zeller,T., Pfeiffer,N., Lackner,K.J., Bettecken,T.,
            Meitinger,T., Oexle,K., Pirastu,M., Portas,L., Nag,A.,
            Williams,K.M., Yonova-Doing,E., Klein,R., Klein,B.E.,
            Hosseini,S.M., Paterson,A.D., Makela,K.M., Lehtimaki,T.,
            Kahonen,M., Raitakari,O., Yoshimura,N., Matsuda,F., Chen,L.J.,
            Pang,C.P., Yip,S.P., Yap,M.K., Meguro,A., Mizuki,N., Inoko,H.,
            Foster,P.J., Zhao,J.H., Vithana,E., Tai,E.S., Fan,Q., Xu,L.,
            Campbell,H., Fleck,B., Rudan,I., Aung,T., Hofman,A.,
            Uitterlinden,A.G., Bencic,G., Khor,C.C., Forward,H., Parssinen,O.,
            Mitchell,P., Rivadeneira,F., Hewitt,A.W., Williams,C., Oostra,B.A.,
            Teo,Y.Y., Hammond,C.J., Stambolian,D., Mackey,D.A., Klaver,C.C.,
            Wong,T.Y., Saw,S.M. and Baird,P.N.
  CONSRTM   Consortium for Refractive Error and Myopia; Fuchs' Genetics
            Multi-Center Study Group; Wellcome Trust Case Control Consortium 2;
            Diabetes Control and Complications Trial/Epidemiology of Diabetes
            Interventions, and Complications Research Group
  TITLE     Nine loci for ocular axial length identified through genome-wide
            association studies, including shared loci with refractive error
  JOURNAL   Am J Hum Genet 93 (2), 264-277 (2013)
   PUBMED   24144296
REFERENCE   8  (residues 1 to 699)
  AUTHORS   De Arras,L., Yang,I.V., Lackford,B., Riches,D.W., Prekeris,R.,
            Freedman,J.H., Schwartz,D.A. and Alper,S.
  TITLE     Spatiotemporal inhibition of innate immunity signaling by the
            Tbc1d23 RAB-GAP
  JOURNAL   J Immunol 188 (6), 2905-2913 (2012)
   PUBMED   22312129
REFERENCE   9  (residues 1 to 699)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   10 (residues 1 to 699)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA801258.1 and BC020955.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020955.1, SRR1660809.202292.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394144.9/ ENSP00000377700.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q12.1-q12.2"
     Protein         1..699
                     /product="TBC1 domain family member 23 isoform 1"
                     /note="HCV nonstructural protein 4A-transactivated protein
                     1; HCV non-structural protein 4A-transactivated protein 1"
                     /calculated_mol_wt=78191
     Region          79..246
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; pfam00566"
                     /db_xref="CDD:459855"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NUY8.3)"
     Region          340..>384
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Site            401
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238089"
     Region          451..675
                     /region_name="TBC1D23_C"
                     /note="TBC1 domain family member 23 C-terminal; pfam19430"
                     /db_xref="CDD:437262"
     Region          459..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUY8.3)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K0F1; propagated from
                     UniProtKB/Swiss-Prot (Q9NUY8.3)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NUY8.3)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NUY8.3)"
     Region          514..699
                     /region_name="May mediate the interaction with WASHC1.
                     /evidence=ECO:0000250|UniProtKB:Q8K0F1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUY8.3)"
     Region          514..573
                     /region_name="May mediate the interaction with C17orf75,
                     FAM91A1 and WDR11. /evidence=ECO:0000250|UniProtKB:Q8K0F1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUY8.3)"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NUY8.3)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NUY8.3)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NUY8.3)"
     Region          574..699
                     /region_name="May mediate the interaction with FKBP15 and
                     WASHC2, required for endosome to Golgi trafficking.
                     /evidence=ECO:0000250|UniProtKB:Q8K0F1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUY8.3)"
     CDS             1..699
                     /gene="TBC1D23"
                     /gene_synonym="NS4ATP1; PCH11"
                     /coded_by="NM_001199198.3:28..2127"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS56265.1"
                     /db_xref="GeneID:55773"
                     /db_xref="HGNC:HGNC:25622"
                     /db_xref="MIM:617687"
ORIGIN      
        1 maegedvppl ptssgdgwek dleealeagg cdletlrnii qgrplpadlr akvwkialnv
       61 agkgdslasw dgildlpeqn tihkdclqfi dqlsvpeeka aellldiesv itfycksrni
      121 kystslswih llkplvhlql prsdlyncfy aimnkyiprd csqkgrpfhl frlliqyhep
      181 elcsyldtkk itpdsyalnw lgslfacycs tevtqaiwdg ylqqadpffi yflmliilvn
      241 akeviltqes dskeevikfl entpsslnie diedlfslaq yycsktpasf rkdnhhlfgs
      301 tllgikddda dlsqalclai svseilqanq lqgegvrffv vdcrpaeqyn aghlstafhl
      361 dsdlmlqnps efaqsvksll eaqkqsiesg siaggehlcf mgsgreeedm ymnmvlahfl
      421 qknkeyvsia sggfmalqqh ladinvdgpe ngyghwiast sgsrssinsv dgespngssd
      481 rgmkslvnkm tvalktksvn vrekvisfie ntstpvdrms fnlpwpdrsc terhvsssdr
      541 vgkpyrgvkp vfsigdeeey dtdeidsssm sdddrkevvn iqtwinkpdv khhfpckevk
      601 esghmfpshl lvtathmycl reivsrkgla yiqsrqalns vvkitskkkh pelitfkygn
      661 ssasgieila ierylipnag datkaikqqi mkvldales
//
LOCUS       NP_075620                329 aa            linear   ROD 27-APR-2025
DEFINITION  CAAX prenyl protease 2 isoform b [Mus musculus].
ACCESSION   NP_075620
VERSION     NP_075620.1
DBSOURCE    REFSEQ: accession NM_023131.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Karlsson,C., Akula,M.K., Staffas,A., Cisowski,J., Sayin,V.I.,
            Ibrahim,M.X., Lindahl,P. and Bergo,M.O.
  TITLE     Knockout of the RAS endoprotease RCE1 accelerates myeloid leukemia
            by downregulating GADD45b
  JOURNAL   Leukemia 35 (2), 606-609 (2021)
   PUBMED   32398789
  REMARK    GeneRIF: Knockout of the RAS endoprotease RCE1 accelerates myeloid
            leukemia by downregulating GADD45b.
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Yao,H., Chen,X., Kashif,M., Wang,T., Ibrahim,M.X., Tuksammel,E.,
            Revechon,G., Eriksson,M., Wiel,C. and Bergo,M.O.
  TITLE     Targeting RAS-converting enzyme 1 overcomes senescence and improves
            progeria-like phenotypes of ZMPSTE24 deficiency
  JOURNAL   Aging Cell 19 (8), e13200 (2020)
   PUBMED   32910507
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Collin,G.B., Gogna,N., Chang,B., Damkham,N., Pinkney,J., Hyde,L.F.,
            Stone,L., Naggert,J.K., Nishina,P.M. and Krebs,M.P.
  TITLE     Mouse Models of Inherited Retinal Degeneration with Photoreceptor
            Cell Loss
  JOURNAL   Cells 9 (4), 931 (2020)
   PUBMED   32290105
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Jaworski,J., Govender,U., McFarlane,C., de la Vega,M., Greene,M.K.,
            Rawlings,N.D., Johnston,J.A., Scott,C.J. and Burrows,J.F.
  TITLE     A novel RCE1 isoform is required for H-Ras plasma membrane
            localization and is regulated by USP17
  JOURNAL   Biochem J 457 (2), 289-300 (2014)
   PUBMED   24134311
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Christiansen,J.R., Kolandaivelu,S., Bergo,M.O. and Ramamurthy,V.
  TITLE     RAS-converting enzyme 1-mediated endoproteolysis is required for
            trafficking of rod phosphodiesterase 6 to photoreceptor outer
            segments
  JOURNAL   Proc Natl Acad Sci U S A 108 (21), 8862-8866 (2011)
   PUBMED   21555557
  REMARK    GeneRIF: RCE1 is essential for the intracellular trafficking of
            PDE6 and survival of photoreceptor cells.
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Aiyagari,A.L., Taylor,B.R., Aurora,V., Young,S.G. and Shannon,K.M.
  TITLE     Hematologic effects of inactivating the Ras processing enzyme Rce1
  JOURNAL   Blood 101 (6), 2250-2252 (2003)
   PUBMED   12433685
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Bergo,M.O., Gavino,B., Ross,J., Schmidt,W.K., Hong,C.,
            Kendall,L.V., Mohr,A., Meta,M., Genant,H., Jiang,Y., Wisner,E.R.,
            Van Bruggen,N., Carano,R.A., Michaelis,S., Griffey,S.M. and
            Young,S.G.
  TITLE     Zmpste24 deficiency in mice causes spontaneous bone fractures,
            muscle weakness, and a prelamin A processing defect
  JOURNAL   Proc Natl Acad Sci U S A 99 (20), 13049-13054 (2002)
   PUBMED   12235369
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Bergo,M.O., Ambroziak,P., Gregory,C., George,A., Otto,J.C., Kim,E.,
            Nagase,H., Casey,P.J., Balmain,A. and Young,S.G.
  TITLE     Absence of the CAAX endoprotease Rce1: effects on cell growth and
            transformation
  JOURNAL   Mol Cell Biol 22 (1), 171-181 (2002)
   PUBMED   11739732
REFERENCE   9  (residues 1 to 329)
  AUTHORS   Kim,E., Ambroziak,P., Otto,J.C., Taylor,B., Ashby,M., Shannon,K.,
            Casey,P.J. and Young,S.G.
  TITLE     Disruption of the mouse Rce1 gene results in defective Ras
            processing and mislocalization of Ras within cells
  JOURNAL   J Biol Chem 274 (13), 8383-8390 (1999)
   PUBMED   10085069
REFERENCE   10 (residues 1 to 329)
  AUTHORS   Dode,L., De Greef,C., Mountian,I., Attard,M., Town,M.M.,
            Casteels,R. and Wuytack,F.
  TITLE     Structure of the human sarco/endoplasmic reticulum Ca2+-ATPase 3
            gene. Promoter analysis and alternative splicing of the SERCA3
            pre-mRNA
  JOURNAL   J Biol Chem 273 (22), 13982-13994 (1998)
   PUBMED   9593748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC128739.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK012946.1, SRR7345562.1286077.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 4.07 cM"
     Protein         1..329
                     /product="CAAX prenyl protease 2 isoform b"
                     /EC_number="3.4.26.1"
                     /note="CAAX prenyl protease 2; FACE-2; prenyl
                     protein-specific endoprotease 2; farnesylated
                     proteins-converting enzyme 2; RCE1 homolog, prenyl protein
                     peptidase; Ras and a-factor-converting enzyme 1 homolog"
                     /calculated_mol_wt=35736
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y256; propagated from
                     UniProtKB/Swiss-Prot (P57791.1)"
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57791.1)"
     Site            75..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57791.1)"
     Site            112..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57791.1)"
     Region          164..267
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
     Site            193..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57791.1)"
     Site            226..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57791.1)"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57791.1)"
     Site            261
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:Q6LZY8; propagated from
                     UniProtKB/Swiss-Prot (P57791.1)"
     Site            265
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:Q6LZY8; propagated from
                     UniProtKB/Swiss-Prot (P57791.1)"
     Site            282..302
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57791.1)"
     CDS             1..329
                     /gene="Rce1"
                     /gene_synonym="D19Ertd283e; D19Ertd98e"
                     /coded_by="NM_023131.2:29..1018"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS29432.1"
                     /db_xref="GeneID:19671"
                     /db_xref="MGI:MGI:1336895"
ORIGIN      
        1 maalggdglr llsvsrperq pesaalsgpg sglccwvsvf scfslacsyv gslyvwksel
       61 prdhpavikr rstsvlvvss lsplcvllwr eltgiqpgts lltlmgfrle gifpaallpl
      121 lltmilflgp lmqlsmdcpc dltdglkvvl aprswarclt dmrwlrnqvi aplteelvfr
      181 acmlpmlapc tglgpavftc plffgvahfh hiieqlrfrq ssvgsifvsa afqfsytavf
      241 gaytaflfir tghligpvlc hsfcnymgfp avcaalehpq kwpllagyal gvglfllllq
      301 pltdpklygs lplcmllert gasetllcs
//
LOCUS       NP_033343                108 aa            linear   ROD 27-APR-2025
DEFINITION  T-cell acute lymphocytic leukemia protein 2 homolog [Mus musculus].
ACCESSION   NP_033343
VERSION     NP_033343.1
DBSOURCE    REFSEQ: accession NM_009317.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Tran,H.N., Nguyen,Q.H. and Jeong,Y.
  TITLE     Dbx1 is a dorsal midbrain-specific determinant of GABAergic neuron
            fate and regulates differentiation of the dorsal midbrain into the
            inferior and superior colliculi
  JOURNAL   Front Cell Dev Biol 12, 1336308 (2024)
   PUBMED   38344749
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Puelles,L. and Hidalgo-Sanchez,M.
  TITLE     The Midbrain Preisthmus: A Poorly Known Effect of the Isthmic
            Organizer
  JOURNAL   Int J Mol Sci 24 (11), 9769 (2023)
   PUBMED   37298722
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Kirjavainen,A., Singh,P., Lahti,L., Seja,P., Lelkes,Z.,
            Makkonen,A., Kilpinen,S., Ono,Y., Salminen,M., Aitta-Aho,T.,
            Stenberg,T., Molchanova,S., Achim,K. and Partanen,J.
  TITLE     Gata2, Nkx2-2 and Skor2 form a transcription factor network
            regulating development of a midbrain GABAergic neuron subtype with
            characteristics of REM-sleep regulatory neurons
  JOURNAL   Development 149 (14) (2022)
   PUBMED   35815619
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Su-Feher,L., Rubin,A.N., Silberberg,S.N., Catta-Preta,R., Lim,K.J.,
            Ypsilanti,A.R., Zdilar,I., McGinnis,C.S., McKinsey,G.L.,
            Rubino,T.E. Jr., Hawrylycz,M.J., Thompson,C., Gartner,Z.J.,
            Puelles,L., Zeng,H., Rubenstein,J.L.R. and Nord,A.S.
  TITLE     Single cell enhancer activity distinguishes GABAergic and
            cholinergic lineages in embryonic mouse basal ganglia
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2108760119 (2022)
   PUBMED   35377797
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Zhang,S., Ramsay,E.S. and Mock,B.A.
  TITLE     Cdkn2a, the cyclin-dependent kinase inhibitor encoding p16INK4a and
            p19ARF, is a candidate for the plasmacytoma susceptibility locus,
            Pctr1
  JOURNAL   Proc Natl Acad Sci U S A 95 (5), 2429-2434 (1998)
   PUBMED   9482902
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Yasui,K., Zhang,S.C., Uemura,M., Aizawa,S. and Ueki,T.
  TITLE     Expression of a twist-related gene, Bbtwist, during the development
            of a lancelet species and its relation to cephalochordate anterior
            structures
  JOURNAL   Dev Biol 195 (1), 49-59 (1998)
   PUBMED   9520323
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Pilz,A., Woodward,K., Povey,S. and Abbott,C.
  TITLE     Comparative mapping of 50 human chromosome 9 loci in the laboratory
            mouse
  JOURNAL   Genomics 25 (1), 139-149 (1995)
   PUBMED   7774911
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Baer,R.
  TITLE     TAL1, TAL2 and LYL1: a family of basic helix-loop-helix proteins
            implicated in T cell acute leukaemia
  JOURNAL   Semin Cancer Biol 4 (6), 341-347 (1993)
   PUBMED   8142619
  REMARK    Review article
REFERENCE   10 (residues 1 to 108)
  AUTHORS   Xia,Y., Brown,L., Yang,C.Y., Tsan,J.T., Siciliano,M.J., Espinosa,R.
            3rd, Le Beau,M.M. and Baer,R.J.
  TITLE     TAL2, a helix-loop-helix gene activated by the (7;9)(q34;q32)
            translocation in human T-cell leukemia
  JOURNAL   Proc Natl Acad Sci U S A 88 (24), 11416-11420 (1991)
   PUBMED   1763056
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL844585.11.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK018448.1, BC110625.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 28.75 cM"
     Protein         1..108
                     /product="T-cell acute lymphocytic leukemia protein 2
                     homolog"
                     /note="TAL-2"
                     /calculated_mol_wt=12184
     Region          2..62
                     /region_name="bHLH_SF"
                     /note="basic Helix Loop Helix (bHLH) domain superfamily;
                     cl00081"
                     /db_xref="CDD:469605"
     Site            order(11..12,14,19,39..40)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381392"
     Site            order(17..18,21..22,24..25,29,40..41,44..45,48,50..51,
                     54..55)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381392"
     Region          76..108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62282.1)"
     CDS             1..108
                     /gene="Tal2"
                     /gene_synonym="bHLHa19"
                     /coded_by="NM_009317.4:84..410"
                     /db_xref="CCDS:CCDS18192.1"
                     /db_xref="GeneID:21350"
                     /db_xref="MGI:MGI:99540"
ORIGIN      
        1 mtrkiftntr erwrqqsvnn afaklrklip thppdkklsk netlrlamry inflvkvlge
       61 qslhqtgvaa qgnilglfpp ktrlpdeddr tllndyrvps pgpshgap
//
LOCUS       NP_036523                335 aa            linear   PRI 27-APR-2025
DEFINITION  SAM pointed domain-containing Ets transcription factor isoform 1
            [Homo sapiens].
ACCESSION   NP_036523
VERSION     NP_036523.1
DBSOURCE    REFSEQ: accession NM_012391.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Vatanmakanian,M., Steffan,J.J., Koul,S., Ochoa,A.C.,
            Chaturvedi,L.S. and Koul,H.K.
  TITLE     Regulation of SPDEF expression by DNA methylation in advanced
            prostate cancer
  JOURNAL   Front Endocrinol (Lausanne) 14, 1156120 (2023)
   PUBMED   37900138
  REMARK    GeneRIF: Regulation of SPDEF expression by DNA methylation in
            advanced prostate cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Hou,Y., Zheng,S., Zou,F., Wang,D., Da,H., Zhou,Y., Fan,X., Liu,J.,
            Zhao,H., He,J., Li,H., Sun,X. and Liu,Y.
  TITLE     Lactobacillus rhamnosus 76 alleviates airway inflammation in
            ovalbumin-allergic mice and improves mucus secretion by
            down-regulating STAT6/SPDEF pathway
  JOURNAL   Immunobiology 228 (5), 152712 (2023)
   PUBMED   37515878
  REMARK    GeneRIF: Lactobacillus rhamnosus 76 alleviates airway inflammation
            in ovalbumin-allergic mice and improves mucus secretion by
            down-regulating STAT6/SPDEF pathway.
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Li,J., Wan,X., Xie,D., Yuan,H., Pei,Q., Luo,Y., Chen,Y., Xian,J.
            and Ye,T.
  TITLE     SPDEF enhances cancer stem cell-like properties and tumorigenesis
            through directly promoting GALNT7 transcription in luminal breast
            cancer
  JOURNAL   Cell Death Dis 14 (8), 569 (2023)
   PUBMED   37633945
  REMARK    GeneRIF: SPDEF enhances cancer stem cell-like properties and
            tumorigenesis through directly promoting GALNT7 transcription in
            luminal breast cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Bao,K.C. and Wang,F.F.
  TITLE     The role of SPDEF in cancer: promoter or suppressor
  JOURNAL   Neoplasma 69 (6), 1270-1276 (2022)
   PUBMED   35951453
  REMARK    GeneRIF: The role of SPDEF in cancer: promoter or suppressor.
            Review article
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Wang,Y., Ren,X., Li,W., Cao,R., Liu,S., Jiang,L., Cheng,B. and
            Xia,J.
  TITLE     SPDEF suppresses head and neck squamous cell carcinoma progression
            by transcriptionally activating NR4A1
  JOURNAL   Int J Oral Sci 13 (1), 33 (2021)
   PUBMED   34667150
  REMARK    GeneRIF: SPDEF suppresses head and neck squamous cell carcinoma
            progression by transcriptionally activating NR4A1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Thompson,H.G., Harris,J.W., Wold,B.J., Lin,F. and Brody,J.P.
  TITLE     p62 overexpression in breast tumors and regulation by
            prostate-derived Ets factor in breast cancer cells
  JOURNAL   Oncogene 22 (15), 2322-2333 (2003)
   PUBMED   12700667
  REMARK    GeneRIF: PDEF upregulates p62 promoter activity at 2 sites. PSI
            downregulates PDEF-induced p62 promoter activation through one of
            these sites.
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Chen,H., Nandi,A.K., Li,X. and Bieberich,C.J.
  TITLE     NKX-3.1 interacts with prostate-derived Ets factor and regulates
            the activity of the PSA promoter
  JOURNAL   Cancer Res 62 (2), 338-340 (2002)
   PUBMED   11809674
  REMARK    GeneRIF: NKX-3.1 interacts with prostate-derived Ets factor and
            regulates the activity of the PSA promoter.
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Oettgen,P., Finger,E., Sun,Z., Akbarali,Y., Thamrongsak,U.,
            Boltax,J., Grall,F., Dube,A., Weiss,A., Brown,L., Quinn,G., Kas,K.,
            Endress,G., Kunsch,C. and Libermann,T.A.
  TITLE     PDEF, a novel prostate epithelium-specific ets transcription
            factor, interacts with the androgen receptor and activates
            prostate-specific antigen gene expression
  JOURNAL   J Biol Chem 275 (2), 1216-1225 (2000)
   PUBMED   10625666
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Yamada,N., Tamai,Y., Miyamoto,H. and Nozaki,M.
  TITLE     Cloning and expression of the mouse Pse gene encoding a novel Ets
            family member
  JOURNAL   Gene 241 (2), 267-274 (2000)
   PUBMED   10675039
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Johannessen,J.V. and Finseth,I.
  TITLE     Electron micrographs in five minutes
  JOURNAL   Ultrastruct Pathol 4 (1), 97-100 (1983)
   PUBMED   6857767
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301543.1 and BC021299.2.
            
            Summary: The protein encoded by this gene belongs to the ETS family
            of transcription factors. It is highly expressed in the prostate
            epithelial cells, and functions as an androgen-independent
            transactivator of prostate-specific antigen (PSA) promoter. Higher
            expression of this protein has also been reported in brain, breast,
            lung and ovarian tumors, compared to the corresponding normal
            tissues, and it shows better tumor-association than other
            cancer-associated molecules, making it a more suitable target for
            developing specific cancer therapies. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Nov 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021299.2, AF071538.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374037.8/ ENSP00000363149.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..335
                     /product="SAM pointed domain-containing Ets transcription
                     factor isoform 1"
                     /note="prostate epithelium-specific Ets transcription
                     factor; SAM pointed domain-containing Ets transcription
                     factor; prostate-specific Ets; prostate-derived Ets
                     factor"
                     /calculated_mol_wt=37387
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95238.1)"
     Region          75..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95238.1)"
     Region          134..214
                     /region_name="SAM_PNT-PDEF-like"
                     /note="Sterile alpha motif (SAM)/Pointed domain of
                     prostate-derived ETS factor; cd08532"
                     /db_xref="CDD:188878"
     Region          248..334
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..335
                     /gene="SPDEF"
                     /gene_synonym="bA375E1.3; PDEF"
                     /coded_by="NM_012391.3:431..1438"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4794.1"
                     /db_xref="GeneID:25803"
                     /db_xref="HGNC:HGNC:17257"
                     /db_xref="MIM:608144"
ORIGIN      
        1 mgsaspglss vspshlllpp dtvsrtglek aaagavgler rdwspsppat peqglsafyl
       61 syfdmlyped sswaakapga ssreeppeep eqcpvidsqa pagsldlvpg gltleehsle
      121 qvqsmvvgev lkdietackl lnitadpmdw spsnvqkwll wtehqyrlpp mgkafqelag
      181 kelcamseeq frqrsplggd vlhahldiwk saawmkerts pgaihycast seeswtdsev
      241 dsscsgqpih lwqflkelll kphsygrfir wlnkekgifk iedsaqvarl wgirknrpam
      301 nydklsrsir qyykkgiirk pdisqrlvyq fvhpi
//
LOCUS       NP_001077434             561 aa            linear   PRI 27-APR-2025
DEFINITION  tudor and KH domain-containing protein isoform a [Homo sapiens].
ACCESSION   NP_001077434
VERSION     NP_001077434.1
DBSOURCE    REFSEQ: accession NM_001083965.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Amiri-Yekta,A., Sen,S., Hazane-Puch,F., Tebbakh,C.,
            Roux-Buisson,N., Cazin,C., Thierry-Mieg,N., Bouras,A., Mohammad
            Ali,S.G., Hosseini,S.H., Goodarzian,M., Gourabi,H., Ray,P.F. and
            Kherraf,Z.E.
  TITLE     Whole genome sequencing identifies a homozygous splicing variant in
            TDRKH segregating with non-obstructive azoospermia in an Iranian
            family
  JOURNAL   Clin Genet 106 (5), 625-631 (2024)
   PUBMED   38956960
  REMARK    GeneRIF: Whole genome sequencing identifies a homozygous splicing
            variant in TDRKH segregating with non-obstructive azoospermia in an
            Iranian family.
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Miura,S., Kosaka,K., Nomura,T., Nagata,S., Shimojo,T., Morikawa,T.,
            Fujioka,R., Harada,M., Taniwaki,T. and Shibata,H.
  TITLE     TDRKH is a candidate gene for an autosomal dominant distal
            hereditary motor neuropathy
  JOURNAL   Eur J Med Genet 62 (12), 103594 (2019)
   PUBMED   30503856
  REMARK    GeneRIF: TDRKH missense mutation segregates with dominant distal
            hereditary motor neuropathy in a four generation pedigree.
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Zhang,H., Liu,K., Izumi,N., Huang,H., Ding,D., Ni,Z., Sidhu,S.S.,
            Chen,C., Tomari,Y. and Min,J.
  TITLE     Structural basis for arginine methylation-independent recognition
            of PIWIL1 by TDRD2
  JOURNAL   Proc Natl Acad Sci U S A 114 (47), 12483-12488 (2017)
   PUBMED   29118143
  REMARK    GeneRIF: Unlike most other Tudor domains TDRD2 preferentially
            recognizes an unmethylated arginine-rich sequence from PIWIL1.
REFERENCE   7  (residues 1 to 561)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 561)
  AUTHORS   Cote,J. and Richard,S.
  TITLE     Tudor domains bind symmetrical dimethylated arginines
  JOURNAL   J Biol Chem 280 (31), 28476-28483 (2005)
   PUBMED   15955813
  REMARK    GeneRIF: Tudor domain proteins interact with arginine-glycine-rich
            motifs in a methylarginine-dependent manner.
REFERENCE   9  (residues 1 to 561)
  AUTHORS   Lamb,F.S., Barna,T.J., Goud,C., Marenholz,I., Mischke,D. and
            Schutte,B.C.
  TITLE     Complex RNA processing of TDRKH, a novel gene encoding the putative
            RNA-binding tudor and KH domains
  JOURNAL   Gene 246 (1-2), 209-218 (2000)
   PUBMED   10767542
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA796638.1, AF227192.1, AL589765.19, AK226092.1 and BC022467.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1, 2, and 3
            all encode isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF227192.1, SRR1803613.89652.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368824.8/ ENSP00000357815.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..561
                     /product="tudor and KH domain-containing protein isoform
                     a"
                     /note="putative RNA binding protein; tudor domain
                     containing 2; tudor and KH domain-containing protein;
                     tudor domain-containing protein 2"
                     /calculated_mol_wt=61915
     Region          49..119
                     /region_name="KH-I_TDRKH_rpt1"
                     /note="first type I K homology (KH) RNA-binding domain
                     found in tudor and KH domain-containing protein (TDRKH)
                     and similar proteins; cd22428"
                     /db_xref="CDD:411856"
     Site            order(62,64..66,68..72,75..76,79..80,85..88)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411856"
     Region          124..205
                     /region_name="KH-I_TDRKH_rpt2"
                     /note="second type I K homology (KH) RNA-binding domain
                     found in tudor and KH domain-containing protein (TDRKH)
                     and similar proteins; cd22429"
                     /db_xref="CDD:411857"
     Site            order(134,136..138,140..144,147..148,151..152,157..160)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411857"
     Region          219..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2W6.2)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2W6.2)"
     Region          328..420
                     /region_name="Tudor_TDRD2"
                     /note="Tudor domain found in Tudor domain-containing
                     protein 2 (TDRD2) and similar proteins; cd20412"
                     /db_xref="CDD:410483"
     Site            order(364,371,388,391,393)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410483"
     CDS             1..561
                     /gene="TDRKH"
                     /gene_synonym="TDRD2"
                     /coded_by="NM_001083965.2:149..1834"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41394.1"
                     /db_xref="GeneID:11022"
                     /db_xref="HGNC:HGNC:11713"
                     /db_xref="MIM:609501"
ORIGIN      
        1 mstertswts lstiqkialg lgipasatva yilyrryres reerltfvge ddieiemrvp
       61 qeavkliigr qganikqlrk qtgaridvdt edvgdervll isgfpvqvck akaaihqilt
      121 entpvseqls vpqrsvgrii grggetirsi ckasgakitc dkesegtlll srlikisgtq
      181 kevaaakhli lekvsedeel rkriahsaet rvprkqpisv rredmtepgg agepalwknt
      241 sssmeptapl vtpppkgggd mavvvskegs wekpsddsfq kseaqaipem pmfeipspdf
      301 sfhadeylev yvsasehpnh fwiqivgsrs lqldklvnem tqhyensvpe dltvhvgdiv
      361 aaplptngsw yrarvlgtle ngnldlyfvd fgdngdcplk dlralrsdfl slpfqaiecs
      421 lariapsgdq weeealdefd rlthcadwkp lvakissyvq tgistwpkiy lydtsngkkl
      481 diglelvhkg yaielpedie enravpdmlk dmatetdasl stlltetkks sgeithtlsc
      541 lslseaasms gddnleddyl l
//
LOCUS       NP_001289936             285 aa            linear   PRI 27-APR-2025
DEFINITION  putative hydrolase DDAH2 [Homo sapiens].
ACCESSION   NP_001289936
VERSION     NP_001289936.1
DBSOURCE    REFSEQ: accession NM_001303007.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Mendes,F.S., Luizon,M.R., Lopes,A.C.D.S., Pereira,D.A.,
            Evangelista,F.C.G., Godoi,L.C., Dusse,L.M. and Alpoim,P.N.
  TITLE     Early and late-onset preeclampsia: effects of DDAH2 polymorphisms
            on ADMA levels and association with DDAH2 haplotypes
  JOURNAL   Rev Bras Ginecol Obstet 46 (2024)
   PUBMED   38765527
  REMARK    GeneRIF: Early and late-onset preeclampsia: effects of DDAH2
            polymorphisms on ADMA levels and association with DDAH2 haplotypes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Ragavan,V.N., Nair,P.C., Jarzebska,N., Angom,R.S., Ruta,L.,
            Bianconi,E., Grottelli,S., Tararova,N.D., Ryazanskiy,D.,
            Lentz,S.R., Tommasi,S., Martens-Lobenhoffer,J., Suzuki-Yamamoto,T.,
            Kimoto,M., Rubets,E., Chau,S., Chen,Y., Hu,X., Bernhardt,N.,
            Spieth,P.M., Weiss,N., Bornstein,S.R., Mukhopadhyay,D.,
            Bode-Boger,S.M., Maas,R., Wang,Y., Macchiarulo,A., Mangoni,A.A.,
            Cellini,B. and Rodionov,R.N.
  TITLE     A multicentric consortium study demonstrates that dimethylarginine
            dimethylaminohydrolase 2 is not a dimethylarginine
            dimethylaminohydrolase
  JOURNAL   Nat Commun 14 (1), 3392 (2023)
   PUBMED   37296100
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Kozlova,A.A., Vaganova,A.N., Rodionov,R.N., Gainetdinov,R.R. and
            Bernhardt,N.
  TITLE     Assessment of DDAH1 and DDAH2 Contributions to Psychiatric
            Disorders via In Silico Methods
  JOURNAL   Int J Mol Sci 23 (19), 11902 (2022)
   PUBMED   36233204
  REMARK    GeneRIF: Assessment of DDAH1 and DDAH2 Contributions to Psychiatric
            Disorders via In Silico Methods.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Faramarzi,E., Aftabi,Y., Ansarin,K., Somi,M.H., Gilani,N. and
            Seyedrezazadeh,E.
  TITLE     Polymorphism (-499C/G) in DDAH2 promoter may act as a protective
            factor for metabolic syndrome: A case-control study in Azar-Cohort
            population
  JOURNAL   Arch Endocrinol Metab 65 (4), 443-449 (2021)
   PUBMED   34283907
  REMARK    GeneRIF: Polymorphism (-499C/G) in DDAH2 promoter may act as a
            protective factor for metabolic syndrome: A case-control study in
            Azar-Cohort population.
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Cillero-Pastor,B., Mateos,J., Fernandez-Lopez,C., Oreiro,N.,
            Ruiz-Romero,C. and Blanco,F.J.
  TITLE     Dimethylarginine dimethylaminohydrolase 2, a newly identified
            mitochondrial protein modulating nitric oxide synthesis in normal
            human chondrocytes
  JOURNAL   Arthritis Rheum 64 (1), 204-212 (2012)
   PUBMED   21898353
  REMARK    GeneRIF: DDAH-2 could play an important role in IL-1beta-induced NO
            production and in osteoarthritis pathogenesis.
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Birdsey,G.M., Leiper,J.M. and Vallance,P.
  TITLE     Intracellular localization of dimethylarginine
            dimethylaminohydrolase overexpressed in an endothelial cell line
  JOURNAL   Acta Physiol Scand 168 (1), 73-79 (2000)
   PUBMED   10691782
REFERENCE   8  (residues 1 to 285)
  AUTHORS   Leiper,J.M., Santa Maria,J., Chubb,A., MacAllister,R.J.,
            Charles,I.G., Whitley,G.S. and Vallance,P.
  TITLE     Identification of two human dimethylarginine
            dimethylaminohydrolases with distinct tissue distributions and
            homology with microbial arginine deiminases
  JOURNAL   Biochem J 343 Pt 1 (Pt 1), 209-214 (1999)
   PUBMED   10493931
REFERENCE   9  (residues 1 to 285)
  AUTHORS   Ribas,G., Neville,M., Wixon,J.L., Cheng,J. and Campbell,R.D.
  TITLE     Genes encoding three new members of the leukocyte antigen 6
            superfamily and a novel member of Ig superfamily, together with
            genes encoding the regulatory nuclear chloride ion channel protein
            (hRNCC) and an N omega-N omega-dimethylarginine
            dimethylaminohydrolase homologue, are found in a 30-kb segment of
            the MHC class III region
  JOURNAL   J Immunol 163 (1), 278-287 (1999)
   PUBMED   10384126
REFERENCE   10 (residues 1 to 285)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK026191.1.
            
            Summary: This gene encodes a dimethylarginine
            dimethylaminohydrolase. The encoded enzyme functions in nitric
            oxide generation by regulating the cellular concentrations of
            methylarginines, which in turn inhibit nitric oxide synthase
            activity. The protein may be localized to the mitochondria.
            Alternative splicing resulting in multiple transcript variants.
            [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026191.1, SRR1163658.234091.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 21898353
            MANE Ensembl match                 :: ENST00000375789.7/
                                                  ENSP00000364945.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..285
                     /product="putative hydrolase DDAH2"
                     /EC_number="3.5.3.18"
                     /note="dimethylarginine dimethylaminohydrolase II;
                     n(G),N(G)-dimethylarginine dimethylaminohydrolase 2;
                     S-phase protein; dimethylargininase-2; epididymis
                     secretory protein Li 277; testis tissue sperm-binding
                     protein Li 54e; inactive dimethylarginine
                     dimethylaminohydrolase 2; inactive
                     N(G),N(G)-dimethylarginine dimethylaminohydrolase 2"
                     /calculated_mol_wt=29513
     Region          <63..>172
                     /region_name="DdaH"
                     /note="N-Dimethylarginine dimethylaminohydrolase [Amino
                     acid transport and metabolism]; COG1834"
                     /db_xref="CDD:441439"
     CDS             1..285
                     /gene="DDAH2"
                     /gene_synonym="DDAH; DDAHII; G6a; HEL-S-277; NG30"
                     /coded_by="NM_001303007.2:139..996"
                     /db_xref="CCDS:CCDS4718.1"
                     /db_xref="GeneID:23564"
                     /db_xref="HGNC:HGNC:2716"
                     /db_xref="MIM:604744"
ORIGIN      
        1 mgtpgeglgr cshalirgvp eslasgegag aglpaldlak aqrehgvlgg klrqrlglql
       61 lelppeeslp lgpllgdtav iqgdtalitr pwsparrpev dgvrkalqdl glriveigde
      121 natldgtdvl ftgreffvgl skwtnhrgae ivadtfrdfa vstvpvsgps hlrglcgmgg
      181 prtvvagssd aaqkavrama vltdhpyasl tlpddaaadc lflrpglpgv ppfllhrggg
      241 dlpnsqealq klsdvtlvpv scselekaga glsslclvls trphs
//
LOCUS       NP_001350609             376 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 584 isoform 3 [Homo sapiens].
ACCESSION   NP_001350609 XP_024307182
VERSION     NP_001350609.1
DBSOURCE    REFSEQ: accession NM_001363680.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Khakpour,G., Noruzinia,M., Izadi,P., Karami,F., Ahmadvand,M.,
            Heshmat,R., Amoli,M.M. and Tavakkoly-Bazzaz,J.
  TITLE     Methylomics of breast cancer: Seeking epimarkers in peripheral
            blood of young subjects
  JOURNAL   Tumour Biol 39 (3), 1010428317695040 (2017)
   PUBMED   28349825
  REMARK    GeneRIF: total of 1799 differentially methylated regions were
            identified including SLC6A3, Rab40C, ZNF584, and FOXD3 whose
            significant methylation differences were confirmed in breast cancer
            patients through quantitative real-time polymerase chain
            reaction.Methylation of those aforementioned genes in white blood
            cells of our young patients may highlight their potential as early
            epimarkers
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB062261.1, BX333264.2, BC033149.1 and AK290068.1.
            
            On May 29, 2018 this sequence version replaced XP_024307182.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.273497.1,
                                           SRR1660803.88440.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..376
                     /product="zinc finger protein 584 isoform 3"
                     /calculated_mol_wt=43052
     Region          116..136
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <144..329
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          171..191
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(176,178,180,182..183,186..187,190,204,206,210..211,
                     214..215,218,232,234,236,238..239,242..243,246)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          199..219
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          227..247
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          255..275
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          283..303
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          311..331
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          339..359
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..376
                     /gene="ZNF584"
                     /coded_by="NM_001363680.1:570..1700"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS86814.1"
                     /db_xref="GeneID:201514"
                     /db_xref="HGNC:HGNC:27318"
ORIGIN      
        1 mlenfalvss lglapsrspv ftqleddeqs wvpswvdvtp vsraearrgf gldglcrved
       61 erahpehlks yrviqhqdth segkprrhte hgaafppgss cgqqqevhva eklfkcsdcg
      121 kvflkafall dhlithseer pfrcptgrsa fkksahinpr kihtgetahv cnecgkafsy
      181 psklrkhqkv htgikpfkcs dcgktfnrkd alvlhqriht gerpyecskc gktfsvlstl
      241 irhrkvhige rpyectecgk ffkynnsfil hqrvhtgerp feckqcgkgy vtrsglyqhw
      301 kvhtgerpye cslcgktftt rsyrnrhqqf hteersyect ecgkafkhss tllqhkkvht
      361 perrqedrah gkvvsc
//
LOCUS       NP_079333                529 aa            linear   PRI 27-APR-2025
DEFINITION  basal body-orientation factor 1 [Homo sapiens].
ACCESSION   NP_079333
VERSION     NP_079333.2
DBSOURCE    REFSEQ: accession NM_025057.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Chien,Y.H., Werner,M.E., Stubbs,J., Joens,M.S., Li,J., Chien,S.,
            Fitzpatrick,J.A., Mitchell,B.J. and Kintner,C.
  TITLE     Bbof1 is required to maintain cilia orientation
  JOURNAL   Development 140 (16), 3468-3477 (2013)
   PUBMED   23900544
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005484.2, DB484577.1, DB493409.1, BC044808.1, BC104979.1,
            AK026842.1 and AL834487.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 31, 2008 this sequence version replaced NP_079333.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC044808.1, SRR1803611.222344.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394009.5/ ENSP00000377577.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..529
                     /product="basal body-orientation factor 1"
                     /note="coiled-coil domain-containing protein 176;
                     coiled-coil domain containing 176"
                     /calculated_mol_wt=61856
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND07.3)"
     Region          77..270
                     /region_name="DUF4515"
                     /note="Domain of unknown function (DUF4515); pfam14988"
                     /db_xref="CDD:405647"
     CDS             1..529
                     /gene="BBOF1"
                     /gene_synonym="C14orf45; CCDC176; FBB10"
                     /coded_by="NM_025057.3:131..1720"
                     /db_xref="CCDS:CCDS32119.2"
                     /db_xref="GeneID:80127"
                     /db_xref="HGNC:HGNC:19855"
                     /db_xref="MIM:620496"
ORIGIN      
        1 mpskgkdkkk gkskgkdtkk liktdesvvd rakanaslwe arlevtelsr ikyrdtsril
       61 aksnedlkkk qckmekdims vlsylkkqdq ekdnmieklk qqlnetkeka qeekdkleqk
      121 ytrqineleg qfhqkakeig mihtelkavr qfqkrkiqve relddlkenl rnterihqet
      181 lrrlesrffe ekhrleqeae kkiimlaera hheaivqlnd agrnvfkend ylqkalayhl
      241 ketdalqkns qklqeshtll lhqkeindll vkekimqlvq qrsqiqtlqk kvvnletals
      301 ymtkefesev lklqqhamie nqagqveidk lqhllqmkdr emnrvkklak nilderteve
      361 rffldalhqv kqqilisrkh ykqiaqaafn lkmraactgr teypkirtfd grehstnsvn
      421 qdlleaekwt hiegnvdigd ltweqkekvl rllfakmngc psrkynqssr ppvpdyvvsd
      481 sgetkefgde sklqdkifit qqiaisdssg evvlptipke pqesdtgtf
//
LOCUS       NP_001353863            1111 aa            linear   PRI 27-APR-2025
DEFINITION  regulator of G-protein signaling protein-like isoform 2 [Homo
            sapiens].
ACCESSION   NP_001353863 XP_005245194
VERSION     NP_001353863.1
DBSOURCE    REFSEQ: accession NM_001366934.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Wiechec,E., Overgaard,J., Kjeldsen,E. and Hansen,L.L.
  TITLE     Chromosome 1q25.3 copy number alterations in primary breast cancers
            detected by multiplex ligation-dependent probe amplification and
            allelic imbalance assays and its comparison with fluorescent in
            situ hybridization assays
  JOURNAL   Cell Oncol (Dordr) 36 (2), 113-120 (2013)
   PUBMED   23248035
  REMARK    GeneRIF: Data indicate that multiplex ligation-dependent probe
            amplification (MLPA) probes (Fig. 2) corresponding to the RGSL2,
            RGSL1 and RGS16 genes showed 64.5 % tumour samples with copy number
            gains and 5 % tumour samples with copy number losses.
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Wiechec,E., Wiuf,C., Overgaard,J. and Hansen,L.L.
  TITLE     High-resolution melting analysis for mutation screening of RGSL1,
            RGS16, and RGS8 in breast cancer
  JOURNAL   Cancer Epidemiol Biomarkers Prev 20 (2), 397-407 (2011)
   PUBMED   21135262
  REMARK    GeneRIF: Missense mutations in RGSL1 gene is associated with breast
            cancer.
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Shulman,J.M., Chibnik,L.B., Aubin,C., Schneider,J.A., Bennett,D.A.
            and De Jager,P.L.
  TITLE     Intermediate phenotypes identify divergent pathways to Alzheimer's
            disease
  JOURNAL   PLoS One 5 (6), e11244 (2010)
   PUBMED   20574532
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1111)
  AUTHORS   Wiechec,E., Overgaard,J. and Hansen,L.L.
  TITLE     A fragile site within the HPC1 region at 1q25.3 affecting RGS16,
            RGSL1, and RGSL2 in human breast carcinomas
  JOURNAL   Genes Chromosomes Cancer 47 (9), 766-780 (2008)
   PUBMED   18521847
  REMARK    GeneRIF: A detailed mapping of the breakpoints revealed intragenic
            microdeletions affecting the coding regions of RGSL2, RGSL1.
REFERENCE   5  (residues 1 to 1111)
  AUTHORS   Silva,A.P., Salim,A.C., Bulgarelli,A., de Souza,J.E., Osorio,E.,
            Caballero,O.L., Iseli,C., Stevenson,B.J., Jongeneel,C.V., de
            Souza,S.J., Simpson,A.J. and Camargo,A.A.
  TITLE     Identification of 9 novel transcripts and two RGSL genes within the
            hereditary prostate cancer region (HPC1) at 1q25
  JOURNAL   Gene 310, 49-57 (2003)
   PUBMED   12801632
REFERENCE   6  (residues 1 to 1111)
  AUTHORS   Tosetti,P., Parente,V., Taglietti,V., Dunlap,K. and Toselli,M.
  TITLE     Chick RGS2L demonstrates concentration-dependent selectivity for
            pertussis toxin-sensitive and -insensitive pathways that inhibit
            L-type Ca2+ channels
  JOURNAL   J Physiol 549 (Pt 1), 157-169 (2003)
   PUBMED   12651916
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139344.24 and AL138776.10.
            
            On Oct 26, 2018 this sequence version replaced XP_005245194.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            NMD candidate             :: translation inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.3"
     Protein         1..1111
                     /product="regulator of G-protein signaling protein-like
                     isoform 2"
                     /note="regulator of G-protein signaling like 2; regulator
                     of G-protein signaling protein-like"
                     /calculated_mol_wt=129708
     Region          685..864
                     /region_name="RGS-like_2"
                     /note="Uncharacterized Regulator of G protein Signaling
                     (RGS) domain subfamily, child 2; cd08728"
                     /db_xref="CDD:188683"
     Region          911..1015
                     /region_name="RGS"
                     /note="Regulator of G protein signaling (RGS) domain
                     superfamily; cl02565"
                     /db_xref="CDD:470619"
     CDS             1..1111
                     /gene="RGSL1"
                     /gene_synonym="RGSL; RGSL2"
                     /coded_by="NM_001366934.1:21..3356"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:353299"
                     /db_xref="HGNC:HGNC:18636"
                     /db_xref="MIM:611012"
ORIGIN      
        1 mssaeiigst nliilledev fadffntfls lpvfgqtpfy tvensqwslw peipcnliak
       61 ykglltwlek crlpffcktn lcfhyilcqe fisfikspeg akmmrwkkad qwllqkcigg
      121 vrgmwrfysy ltgsageelv dfwilaenil sidemdlevr dyylslllml rathlqegsr
      181 vvtlcnmnik sllnlsiwhp nqsttrreil shmqkvalfk lqsywlpnfy thtkmtmake
      241 eachglmqey etrlysvcyt higglplnms ikkchhfqkr yssrkakrkm wqlvdpdsws
      301 lemdlkpdai gmplqetcpq ekvviqmpsl kmassketri sslekdmhya kissmenkak
      361 shlhmeapfe tkvsthlrtv ipivnhsskm tiqkaikqsf slgyihlalc adacagnpfr
      421 dhlkklnlkv eiqlldlwqd lqhflsvlln nkkngnaifr hllgdricel ylneqigpcl
      481 plksqtiqgl kellpsgdvi pwipkaqkei ckmlspwyde fldeedywfl lfttqnrfis
      541 srqhkrefig keenillykr iqqslelsqa ladmkemdyr qwrkiatedl kqggslqvel
      601 tspvfltdit kmsfeelcyk npkmaiqkis ddykiyceka pkidfkmeii ketktvsrsn
      661 rkmsllkrtl vrkpsmrprn ltevllntqh leffreflke rkakiplqfl tavqkisiet
      721 nekickslie nviktffqgq lspeemlqcd apiikeiasm rhvttstllt lqghvmksie
      781 ekwfkdyqdl fpphhqevev qsevqissrk pskivstylq esqkkgwmrm isfirsfcky
      841 rrfmlnpskr qefedylhqe mqnskenftt ahntsgrsap pstnvrsadq engeitlvkr
      901 rifghriitv nfaindlyff semekfndlv ssahmlqvnr aynendvilm rskmniiqkl
      961 flnsdippkl rvnvpefqkd ailaaitegy ldrsvfhgai msvfpvvmyf wkrfcfwkat
     1021 rsylqyrgkk fkdrksppks tdkypfssgg dnailrftll rgiewlqpqr eaissvqnss
     1081 sskltqprlv vsamqlhpvq gqklsyikke k
//
LOCUS       NP_001356022             357 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform b [Homo
            sapiens].
ACCESSION   NP_001356022 XP_006717936
VERSION     NP_001356022.1
DBSOURCE    REFSEQ: accession NM_001369093.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 357)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 357)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            On Mar 18, 2019 this sequence version replaced XP_006717936.1.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.50014.1,
                                           SRR1803617.163826.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..357
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform b"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=41097
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..356
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..357
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369093.1:209..1282"
                     /note="isoform b is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS31219.1"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilkl fenfyfgslk lnsihisqrf tvdsfgnyas cgqidfs
//
LOCUS       NP_001350799             348 aa            linear   PRI 27-APR-2025
DEFINITION  muscleblind-like protein 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001350799 XP_016861923
VERSION     NP_001350799.1
DBSOURCE    REFSEQ: accession NM_001363870.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Aoki,Y., Yanaizu,M., Ohki,A., Nishimiya,K. and Kino,Y.
  TITLE     CUG repeat RNA-dependent proteasomal degradation of MBNL1 in a
            cellular model of myotonic dystrophy type 1
  JOURNAL   Biochem Biophys Res Commun 733, 150729 (2024)
   PUBMED   39326259
  REMARK    GeneRIF: CUG repeat RNA-dependent proteasomal degradation of MBNL1
            in a cellular model of myotonic dystrophy type 1.
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Piasecka,A., Szczesniak,M.W., Sekrecki,M., Kajdasz,A.,
            Sznajder,L.J., Baud,A. and Sobczak,K.
  TITLE     MBNL splicing factors regulate the microtranscriptome of skeletal
            muscles
  JOURNAL   Nucleic Acids Res 52 (19), 12055-12073 (2024)
   PUBMED   39258536
  REMARK    GeneRIF: MBNL splicing factors regulate the microtranscriptome of
            skeletal muscles.
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Wang,H.F., Zhou,X.F., Zhang,Q.M., Wu,J.Q., Hou,J.H., Xu,X.L.,
            Li,X.M. and Liu,Y.L.
  TITLE     Involvement of circRNA Regulators MBNL1 and QKI in the Progression
            of Esophageal Squamous Cell Carcinoma
  JOURNAL   Cancer Control 31, 10732748241257142 (2024)
   PUBMED   38769028
  REMARK    GeneRIF: Involvement of circRNA Regulators MBNL1 and QKI in the
            Progression of Esophageal Squamous Cell Carcinoma.
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Yang,Y., Lee,G.C., Nakagaki-Silva,E., Huang,Y., Peacey,M.,
            Partridge,R., Gooding,C. and Smith,C.W.J.
  TITLE     Cell-type specific regulator RBPMS switches alternative splicing
            via higher-order oligomerization and heterotypic interactions with
            other splicing regulators
  JOURNAL   Nucleic Acids Res 51 (18), 9961-9982 (2023)
   PUBMED   37548402
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Tahraoui-Bories,J., Merien,A., Gonzalez-Barriga,A., Laine,J.,
            Leteur,C., Polveche,H., Carteron,A., De Lamotte,J.D., Nicoleau,C.,
            Polentes,J., Jarrige,M., Gomes-Pereira,M., Ventre,E., Poydenot,P.,
            Furling,D., Schaeffer,L., Legay,C. and Martinat,C.
  TITLE     MBNL-dependent impaired development within the neuromuscular system
            in myotonic dystrophy type 1
  JOURNAL   Neuropathol Appl Neurobiol 49 (1), e12876 (2023)
   PUBMED   36575942
  REMARK    GeneRIF: MBNL-dependent impaired development within the
            neuromuscular system in myotonic dystrophy type 1.
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Kino,Y., Mori,D., Oma,Y., Takeshita,Y., Sasagawa,N. and Ishiura,S.
  TITLE     Muscleblind protein, MBNL1/EXP, binds specifically to CHHG repeats
  JOURNAL   Hum Mol Genet 13 (5), 495-507 (2004)
   PUBMED   14722159
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Fardaei,M., Rogers,M.T., Thorpe,H.M., Larkin,K., Hamshere,M.G.,
            Harper,P.S. and Brook,J.D.
  TITLE     Three proteins, MBNL, MBLL and MBXL, co-localize in vivo with
            nuclear foci of expanded-repeat transcripts in DM1 and DM2 cells
  JOURNAL   Hum Mol Genet 11 (7), 805-814 (2002)
   PUBMED   11929853
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Mankodi,A., Urbinati,C.R., Yuan,Q.P., Moxley,R.T., Sansone,V.,
            Krym,M., Henderson,D., Schalling,M., Swanson,M.S. and Thornton,C.A.
  TITLE     Muscleblind localizes to nuclear foci of aberrant RNA in myotonic
            dystrophy types 1 and 2
  JOURNAL   Hum Mol Genet 10 (19), 2165-2170 (2001)
   PUBMED   11590133
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Fardaei,M., Larkin,K., Brook,J.D. and Hamshere,M.G.
  TITLE     In vivo co-localisation of MBNL protein with DMPK expanded-repeat
            transcripts
  JOURNAL   Nucleic Acids Res 29 (13), 2766-2771 (2001)
   PUBMED   11433021
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Miller,J.W., Urbinati,C.R., Teng-Umnuay,P., Stenberg,M.G.,
            Byrne,B.J., Thornton,C.A. and Swanson,M.S.
  TITLE     Recruitment of human muscleblind proteins to (CUG)(n) expansions
            associated with myotonic dystrophy
  JOURNAL   EMBO J 19 (17), 4439-4448 (2000)
   PUBMED   10970838
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106722.5 and AC026347.17.
            
            On Jun 3, 2018 this sequence version replaced XP_016861923.1.
            
            Summary: This gene encodes a member of the muscleblind protein
            family which was initially described in Drosophila melanogaster.
            The encoded protein is a C3H-type zinc finger protein that
            modulates alternative splicing of pre-mRNAs. Muscleblind proteins
            bind specifically to expanded dsCUG RNA but not to normal size CUG
            repeats and may thereby play a role in the pathophysiology of
            myotonic dystrophy. Mice lacking this gene exhibited muscle
            abnormalities and cataracts. Several alternatively spliced
            transcript variants have been described but the full-length natures
            of only some have been determined. The different isoforms are
            thought to have different binding specificities and/or splicing
            activities. [provided by RefSeq, Sep 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.55706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.1-q25.2"
     Protein         1..348
                     /product="muscleblind-like protein 1 isoform 9"
                     /note="triplet-expansion RNA-binding protein;
                     muscleblind-like"
                     /calculated_mol_wt=37768
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NR56.2)"
     Region          181..205
                     /region_name="ZnF_C3H1"
                     /note="zinc finger; smart00356"
                     /db_xref="CDD:214632"
     CDS             1..348
                     /gene="MBNL1"
                     /gene_synonym="EXP; MBNL"
                     /coded_by="NM_001363870.1:1031..2077"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS87156.1"
                     /db_xref="GeneID:4154"
                     /db_xref="HGNC:HGNC:6923"
                     /db_xref="MIM:606516"
ORIGIN      
        1 mavsvtpird tkwltlevcr efqrgtcsrp dteckfahps kscqvengrv iacfdslkgr
       61 csrenckylh ppphlktqle ingrnnliqq knmamlaqqm qlanammpga plqpvpmfsv
      121 apslatnasa aafnpylgpv spslvpaeil ptapmlvtgn pgvpvpaaaa aaaqklmrtd
      181 rlevcreyqr gncnrgendc rfahpadstm idtndntvtv cmdyikgrcs rekckyfhpp
      241 ahlqakikaa qyqvnqaaaa qaaataaamt qsavkslkrp leatfdlgip qavlpplpkr
      301 palektngat avfntgifqy qqalanmqlq qhtaflppdt hnicrtsd
//
LOCUS       NP_059982                443 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial enolase superfamily member 1 isoform rTSbeta [Homo
            sapiens].
ACCESSION   NP_059982
VERSION     NP_059982.2
DBSOURCE    REFSEQ: accession NM_017512.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Arjmandi,K., Ameli,F., Salahshourifar,I., Esfandbod,M. and Irani,S.
  TITLE     Evaluation of TS and ENOSF1 Variants as a Biomarker in Response to
            Neoadjuvant Chemotherapy based on 5FU in Gastric Cancer Patients
  JOURNAL   Asian Pac J Cancer Prev 23 (9), 2983-2989 (2022)
   PUBMED   36172660
  REMARK    GeneRIF: Evaluation of TS and ENOSF1 Variants as a Biomarker in
            Response to Neoadjuvant Chemotherapy based on 5FU in Gastric Cancer
            Patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Hamzic,S., Kummer,D., Froehlich,T.K., Joerger,M., Aebi,S.,
            Palles,C., Thomlinson,I., Meulendijks,D., Schellens,J.H.M.,
            Garcia-Gonzalez,X., Lopez-Fernandez,L.A., Amstutz,U. and
            Largiader,C.R.
  TITLE     Evaluating the role of ENOSF1 and TYMS variants as predictors in
            fluoropyrimidine-related toxicities: An IPD meta-analysis
  JOURNAL   Pharmacol Res 152, 104594 (2020)
   PUBMED   31838077
  REMARK    GeneRIF: Evaluating the role of ENOSF1 and TYMS variants as
            predictors in fluoropyrimidine-related toxicities: An IPD
            meta-analysis.
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Giusti,B., Sestini,I., Saracini,C., Sticchi,E., Bolli,P., Magi,A.,
            Gori,A.M., Marcucci,R., Gensini,G.F. and Abbate,R.
  TITLE     High-throughput multiplex single-nucleotide polymorphism (SNP)
            analysis in genes involved in methionine metabolism
  JOURNAL   Biochem Genet 46 (7-8), 406-423 (2008)
   PUBMED   18427977
  REMARK    GeneRIF: Observational study of genetic testing. (HuGE Navigator)
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Liang,P., Nair,J.R., Song,L., McGuire,J.J. and Dolnick,B.J.
  TITLE     Comparative genomic analysis reveals a novel mitochondrial isoform
            of human rTS protein and unusual phylogenetic distribution of the
            rTS gene
  JOURNAL   BMC Genomics 6, 125 (2005)
   PUBMED   16162288
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Dolnick,B.J., Angelino,N.J., Dolnick,R. and Sufrin,J.R.
  TITLE     A novel function for the rTS gene
  JOURNAL   Cancer Biol Ther 2 (4), 364-369 (2003)
   PUBMED   14508106
REFERENCE   7  (residues 1 to 443)
  AUTHORS   Chu,J. and Dolnick,B.J.
  TITLE     Natural antisense (rTSalpha) RNA induces site-specific cleavage of
            thymidylate synthase mRNA
  JOURNAL   Biochim Biophys Acta 1587 (2-3), 183-193 (2002)
   PUBMED   12084460
  REMARK    Review article
REFERENCE   8  (residues 1 to 443)
  AUTHORS   Dolnick,B.J., Lu,K., Yin,M.B. and Rustum,Y.M.
  TITLE     Recent advances in the study of rTS proteins. rTS expression during
            growth and in response to thymidylate synthase inhibitors in human
            tumor cells
  JOURNAL   Adv Enzyme Regul 37, 95-109 (1997)
   PUBMED   9381988
REFERENCE   9  (residues 1 to 443)
  AUTHORS   Dolnick,B.J. and Black,A.R.
  TITLE     Alternate splicing of the rTS gene product and its overexpression
            in a 5-fluorouracil-resistant cell line
  JOURNAL   Cancer Res 56 (14), 3207-3210 (1996)
   PUBMED   8764108
REFERENCE   10 (residues 1 to 443)
  AUTHORS   Dolnick,B.J.
  TITLE     Cloning and characterization of a naturally occurring antisense RNA
            to human thymidylate synthase mRNA
  JOURNAL   Nucleic Acids Res 21 (8), 1747-1752 (1993)
   PUBMED   8493092
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC001285.1 and AP001178.4.
            
            On Feb 1, 2005 this sequence version replaced NP_059982.1.
            
            Summary: This gene can encode a mitochondrial enzyme that is
            thought to convert L-fuconate to 2-keto-3-deoxy-L-fuconate. This
            locus was originally identified as the source of antisense RNAs of
            the adjacent thymidylate synthase gene. Splice variants at this
            locus may contain an alternate 3' exon that is complementary to the
            3'UTR and terminal intron of the thymidylate synthase (TS) RNA and
            may downregulate TS expression. [provided by RefSeq, Aug 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.31929.1,
                                           SRR5189658.169064.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 16162288
            MANE Ensembl match                 :: ENST00000647584.2/
                                                  ENSP00000497230.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.32"
     Protein         1..443
                     /product="mitochondrial enolase superfamily member 1
                     isoform rTSbeta"
                     /EC_number="4.2.1.68"
                     /note="antisense RNA to thymidylate synthase;
                     mitochondrial enolase superfamily member 1; L-fuconate
                     dehydratase"
                     /calculated_mol_wt=49656
     Region          4..419
                     /region_name="rTSbeta_L-fuconate_dehydratase"
                     /note="Human rTS beta is encoded by the rTS gene which,
                     through alternative RNA splicing, also encodes rTS alpha
                     whose mRNA is complementary to thymidylate synthase mRNA.
                     rTS beta expression is associated with the production of
                     small molecules that appear to...; cd03324"
                     /db_xref="CDD:239440"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15994970; propagated from
                     UniProtKB/Swiss-Prot (Q7L5Y1.1)"
     Site            order(190,220,222,250,274,276,305,328,355,386)
                     /site_type="active"
                     /note="putative active site pocket [active]"
                     /db_xref="CDD:239440"
     Site            order(250,276,305)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:239440"
     CDS             1..443
                     /gene="ENOSF1"
                     /gene_synonym="FUCD; RTS; TYMSAS"
                     /coded_by="NM_017512.7:44..1375"
                     /note="isoform rTSbeta is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11822.1"
                     /db_xref="GeneID:55556"
                     /db_xref="HGNC:HGNC:30365"
                     /db_xref="MIM:607427"
ORIGIN      
        1 mvrgrisrls vrdvrfptsl gghgadamht dpdysaayvv ietdaedgik gcgitftlgk
       61 gtevvvcavn alahhvlnkd lkdivgdfrg fyrqltsdgq lrwigpekgv vhlataavln
      121 avwdlwakqe gkpvwkllvd mdprmlvsci dfryitdvlt eedaleilqk gqigkkerek
      181 qmlaqgypay ttscawlgys ddtlkqlcaq alkdgwtrfk vkvgadlqdd mrrcqiirdm
      241 igpektlmmd anqrwdvpea vewmsklakf kplwieepts pddilghati skalvplgig
      301 iatgeqchnr vifkqllqak alqflqidsc rlgsvnenls vllmakkfei pvcphaggvg
      361 lcelvqhlii fdyisvsasl enrvceyvdh lhehfkypvm iqrasymppk dpgystemke
      421 esvkkhqypd gevwkkllpa qen
//
LOCUS       NP_757386                645 aa            linear   PRI 27-APR-2025
DEFINITION  SURP and G-patch domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_757386
VERSION     NP_757386.2
DBSOURCE    REFSEQ: accession NM_172231.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Feng,Q., Krick,K., Chu,J. and Burge,C.B.
  TITLE     Splicing quality control mediated by DHX15 and its G-patch
            activator SUGP1
  JOURNAL   Cell Rep 42 (10), 113223 (2023)
   PUBMED   37805921
  REMARK    GeneRIF: Splicing quality control mediated by DHX15 and its G-patch
            activator SUGP1.
REFERENCE   3  (residues 1 to 645)
  AUTHORS   Zhang,J., Huang,J., Xu,K., Xing,P., Huang,Y., Liu,Z., Tong,L. and
            Manley,J.L.
  TITLE     DHX15 is involved in SUGP1-mediated RNA missplicing by mutant SF3B1
            in cancer
  JOURNAL   Proc Natl Acad Sci U S A 119 (49), e2216712119 (2022)
   PUBMED   36459648
  REMARK    GeneRIF: DHX15 is involved in SUGP1-mediated RNA missplicing by
            mutant SF3B1 in cancer.
REFERENCE   4  (residues 1 to 645)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 645)
  AUTHORS   Alsafadi,S., Dayot,S., Tarin,M., Houy,A., Bellanger,D.,
            Cornella,M., Wassef,M., Waterfall,J.J., Lehnert,E., Roman-Roman,S.,
            Stern,M.H. and Popova,T.
  TITLE     Genetic alterations of SUGP1 mimic mutant-SF3B1 splice pattern in
            lung adenocarcinoma and other cancers
  JOURNAL   Oncogene 40 (1), 85-96 (2021)
   PUBMED   33057152
  REMARK    GeneRIF: Genetic alterations of SUGP1 mimic mutant-SF3B1 splice
            pattern in lung adenocarcinoma and other cancers.
REFERENCE   6  (residues 1 to 645)
  AUTHORS   Kathiresan,S., Willer,C.J., Peloso,G.M., Demissie,S., Musunuru,K.,
            Schadt,E.E., Kaplan,L., Bennett,D., Li,Y., Tanaka,T., Voight,B.F.,
            Bonnycastle,L.L., Jackson,A.U., Crawford,G., Surti,A., Guiducci,C.,
            Burtt,N.P., Parish,S., Clarke,R., Zelenika,D., Kubalanza,K.A.,
            Morken,M.A., Scott,L.J., Stringham,H.M., Galan,P., Swift,A.J.,
            Kuusisto,J., Bergman,R.N., Sundvall,J., Laakso,M., Ferrucci,L.,
            Scheet,P., Sanna,S., Uda,M., Yang,Q., Lunetta,K.L., Dupuis,J., de
            Bakker,P.I., O'Donnell,C.J., Chambers,J.C., Kooner,J.S.,
            Hercberg,S., Meneton,P., Lakatta,E.G., Scuteri,A., Schlessinger,D.,
            Tuomilehto,J., Collins,F.S., Groop,L., Altshuler,D., Collins,R.,
            Lathrop,G.M., Melander,O., Salomaa,V., Peltonen,L.,
            Orho-Melander,M., Ordovas,J.M., Boehnke,M., Abecasis,G.R.,
            Mohlke,K.L. and Cupples,L.A.
  TITLE     Common variants at 30 loci contribute to polygenic dyslipidemia
  JOURNAL   Nat Genet 41 (1), 56-65 (2009)
   PUBMED   19060906
REFERENCE   7  (residues 1 to 645)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 645)
  AUTHORS   Sampson,N.D. and Hewitt,J.E.
  TITLE     SF4 and SFRS14, two related putative splicing factors on human
            chromosome 19p13.11
  JOURNAL   Gene 305 (1), 91-100 (2003)
   PUBMED   12594045
REFERENCE   9  (residues 1 to 645)
  AUTHORS   Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R.
  TITLE     Comprehensive proteomic analysis of the human spliceosome
  JOURNAL   Nature 419 (6903), 182-185 (2002)
   PUBMED   12226669
REFERENCE   10 (residues 1 to 645)
  AUTHORS   Rappsilber,J., Ryder,U., Lamond,A.I. and Mann,M.
  TITLE     Large-scale proteomic analysis of the human spliceosome
  JOURNAL   Genome Res 12 (8), 1231-1245 (2002)
   PUBMED   12176931
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC363162.1, AY072917.1 and AC003967.2.
            
            On Aug 7, 2003 this sequence version replaced NP_757386.1.
            
            Summary: SF4 is a member of the SURP family of splicing
            factors.[supplied by OMIM, Sep 2003].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC142988.1, AK292085.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247001.10/ ENSP00000247001.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..645
                     /product="SURP and G-patch domain-containing protein 1"
                     /note="splicing factor 4; RNA-binding protein RBP"
                     /calculated_mol_wt=72340
     Region          49..78
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Region          97..123
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Region          150..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Region          190..241
                     /region_name="Surp"
                     /note="Surp module; pfam01805"
                     /db_xref="CDD:460339"
     Region          191..233
                     /region_name="SURP motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Region          265..316
                     /region_name="Surp"
                     /note="Surp module; pfam01805"
                     /db_xref="CDD:460339"
     Region          266..309
                     /region_name="SURP motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Region          319..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Region          380..386
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     Region          560..606
                     /region_name="G_patch"
                     /note="glycine rich nucleic binding domain; smart00443"
                     /db_xref="CDD:197727"
     Region          582..607
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWZ8.2)"
     CDS             1..645
                     /gene="SUGP1"
                     /gene_synonym="F23858; RBP; SF4"
                     /coded_by="NM_172231.4:14..1951"
                     /db_xref="CCDS:CCDS12399.1"
                     /db_xref="GeneID:57794"
                     /db_xref="HGNC:HGNC:18643"
                     /db_xref="MIM:607992"
ORIGIN      
        1 mslkmdnrdv agkanrwfgv appksgkmnm nilhqeelia qkkreieakm eqkakqnqva
       61 spqpphpgei tnahnsscis nkfandgsfl qqflklqkaq tstdaptsap sappstptps
      121 agkrsllisr rtglglaslp gpvksyshak qlpvahrpsv fqspdedeee dyeqwleikv
      181 sppegaetrk vieklarfva eggpelekva medykdnpaf aflhdknsre flyyrkkvae
      241 irkeaqksqa asqkvspped eevknlaekl arfiadggpe vetialqnnr enqafsflye
      301 pnsqgykyyr qkleefrkak asstgsftap dpglkrkspp ealsgslppa ttcpasstpa
      361 ptiipapaap gkpasaatvk rkrksrwgpe edkvelppae lvqrdvdasp splsvqdlkg
      421 lgyekgkpvg lvgvtelsda qkkqlkeqqe mqqmydmimq hkramqdmql lwekavqqhq
      481 hgydsdeevd selgtwehql rrmemdktre waeqltkmgr gkhfigdflp pdelekfmet
      541 fkalkegrep dyseykefkl tvenigyqml mkmgwkegeg lgsegqgikn pvnkgtttvd
      601 gagfgidrpa elskeddeye afrkrmmlay rfrpnplnnp rrpyy
//
LOCUS       NP_035039                381 aa            linear   ROD 27-APR-2025
DEFINITION  NF-kappa-B inhibitor-like protein 1 isoform 1 [Mus musculus].
ACCESSION   NP_035039 XP_001000143
VERSION     NP_035039.1
DBSOURCE    REFSEQ: accession NM_010909.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 381)
  AUTHORS   McIntyre,R.E., Nicod,J., Robles-Espinoza,C.D., Maciejowski,J.,
            Cai,N., Hill,J., Verstraten,R., Iyer,V., Rust,A.G., Balmus,G.,
            Mott,R., Flint,J. and Adams,D.J.
  TITLE     A Genome-Wide Association Study for Regulators of Micronucleus
            Formation in Mice
  JOURNAL   G3 (Bethesda) 6 (8), 2343-2354 (2016)
   PUBMED   27233670
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Chiba,T., Miyashita,K., Sugoh,T., Warita,T., Inoko,H., Kimura,M.
            and Sato,T.
  TITLE     IkappaBL, a novel member of the nuclear IkappaB family, inhibits
            inflammatory cytokine expression
  JOURNAL   FEBS Lett 585 (22), 3577-3581 (2011)
   PUBMED   22024480
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Chiba,T., Matsuzaka,Y., Warita,T., Sugoh,T., Miyashita,K.,
            Tajima,A., Nakamura,M., Inoko,H., Sato,T. and Kimura,M.
  TITLE     NFKBIL1 confers resistance to experimental autoimmune arthritis
            through the regulation of dendritic cell functions
  JOURNAL   Scand J Immunol 73 (5), 478-485 (2011)
   PUBMED   21284685
  REMARK    GeneRIF: NFKBIL-1 affects the pathogenesis of rheumatoid arthritis
            at least in part by the regulation of dendritic cell functions.
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Allcock,R.J., Martin,A.M. and Price,P.
  TITLE     The mouse as a model for the effects of MHC genes on human disease
  JOURNAL   Immunol Today 21 (7), 328-332 (2000)
   PUBMED   10871872
  REMARK    Review article
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Handel-Fernandez,M.E., Kurimoto,I., Streilein,J.W. and Vincek,V.
  TITLE     Genetic mapping and physical cloning of UVB susceptibility region
            in mice
  JOURNAL   J Invest Dermatol 113 (2), 224-229 (1999)
   PUBMED   10469308
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Hotfilder,M., Baxendale,S., Cross,M.A. and Sablitzky,F.
  TITLE     Def-2, -3, -6 and -8, novel mouse genes differentially expressed in
            the haemopoietic system
  JOURNAL   Br J Haematol 106 (2), 335-344 (1999)
   PUBMED   10460589
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Handel-Fernandez,M.E. and Vincek,V.
  TITLE     Sequence analysis and expression of a mouse homolog of human
            IkappaBL gene
  JOURNAL   Biochim Biophys Acta 1444 (2), 306-310 (1999)
   PUBMED   10023090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CR974444.18.
            
            On May 4, 2006 this sequence version replaced XP_001000143.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF095902.1, BC013269.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849387,
                                           SAMN01164134 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 18.6 cM"
     Protein         1..381
                     /product="NF-kappa-B inhibitor-like protein 1 isoform 1"
                     /note="NF-kappa-B inhibitor-like protein 1; I-kappa-B-like
                     protein; inhibitor of kappa B-like protein"
                     /calculated_mol_wt=43071
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88995.1)"
     Region          <44..>139
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          64..93
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O88995.1)"
     Region          65..96
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          97..134
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O88995.1)"
     Region          132..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88995.1)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBC1; propagated from
                     UniProtKB/Swiss-Prot (O88995.1)"
     Region          186..298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88995.1)"
     CDS             1..381
                     /gene="Nfkbil1"
                     /gene_synonym="Def-7; ikappaBL; IKBL"
                     /coded_by="NM_010909.5:81..1226"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS28693.1"
                     /db_xref="GeneID:18038"
                     /db_xref="MGI:MGI:1340031"
ORIGIN      
        1 msnpspqape eeastsvcrp qscsmasasr rhrrerrfrr ylsagrlvra qallqrhpgl
       61 dvdagqpppl hracarhdap alclllrlga dpahqdrhgd talhaaarqg pdaytdfflp
      121 llsrcpsamg iknkdgetpg qilgwgppwd saeeeedeev skerewrqkl qgeledewqe
      181 vigrfeddas rdtqepesfs awserlareh aqkqrqqlea egscrpprae gsshswrqhe
      241 eeqrlfrera rakekelces rarraqeaqr dkgpepprag praehprgae rgslwrfgdv
      301 pwpcpgggdp eamaaalvar gppleeqgal krylrvqqvr whpdrflqrf rsqietwelg
      361 rvmgavtals qalnrhaeal k
//
LOCUS       NP_001348219             857 aa            linear   ROD 27-APR-2025
DEFINITION  transportin-3 isoform 3 [Mus musculus].
ACCESSION   NP_001348219 XP_017177139
VERSION     NP_001348219.1
DBSOURCE    REFSEQ: accession NM_001361290.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Iwanami,N., Richter,A.S., Sikora,K. and Boehm,T.
  TITLE     Tnpo3 controls splicing of the pre-mRNA encoding the canonical TCR
            alpha chain of iNKT cells
  JOURNAL   Nat Commun 14 (1), 3645 (2023)
   PUBMED   37339974
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 857)
  AUTHORS   Bayer,M., Boller,S., Ramamoothy,S., Zolotarev,N., Cauchy,P.,
            Iwanami,N., Mittler,G., Boehm,T. and Grosschedl,R.
  TITLE     Tnpo3 enables EBF1 function in conditions of antagonistic Notch
            signaling
  JOURNAL   Genes Dev 36 (15-16), 901-915 (2022)
   PUBMED   36167471
  REMARK    GeneRIF: Tnpo3 enables EBF1 function in conditions of antagonistic
            Notch signaling.
REFERENCE   3  (residues 1 to 857)
  AUTHORS   Costa,R., Rodia,M.T., Zini,N., Pegoraro,V., Marozzo,R., Capanni,C.,
            Angelini,C., Lattanzi,G., Santi,S. and Cenacchi,G.
  TITLE     Morphological study of TNPO3 and SRSF1 interaction during
            myogenesis by combining confocal, structured illumination and
            electron microscopy analysis
  JOURNAL   Mol Cell Biochem 476 (4), 1797-1811 (2021)
   PUBMED   33452620
  REMARK    GeneRIF: Morphological study of TNPO3 and SRSF1 interaction during
            myogenesis by combining confocal, structured illumination and
            electron microscopy analysis.
REFERENCE   4  (residues 1 to 857)
  AUTHORS   Iwanami,N., Sikora,K., Richter,A.S., Monnich,M., Guerri,L.,
            Soza-Ried,C., Lawir,D.F., Mateos,F., Hess,I., O'Meara,C.P.,
            Schorpp,M. and Boehm,T.
  TITLE     Forward Genetic Screens in Zebrafish Identify Pre-mRNA-Processing
            Pathways Regulating Early T Cell Development
  JOURNAL   Cell Rep 17 (9), 2259-2270 (2016)
   PUBMED   27880902
REFERENCE   5  (residues 1 to 857)
  AUTHORS   Cerasoli,D.M., Riley,M.P., Shih,F.F. and Caton,A.J.
  TITLE     Genetic basis for T cell recognition of a major histocompatibility
            complex class II-restricted neo-self peptide
  JOURNAL   J Exp Med 182 (5), 1327-1336 (1995)
   PUBMED   7595203
REFERENCE   6  (residues 1 to 857)
  AUTHORS   Stenzel-Poore,M.P. and Rittenberg,M.B.
  TITLE     Clonal diversity, somatic mutation, and immune memory to
            phosphocholine-keyhole limpet hemocyanin
  JOURNAL   J Immunol 143 (12), 4123-4133 (1989)
   PUBMED   2512351
REFERENCE   7  (residues 1 to 857)
  AUTHORS   Blier,P.R. and Bothwell,A.
  TITLE     A limited number of B cell lineages generates the heterogeneity of
            a secondary immune response
  JOURNAL   J Immunol 139 (12), 3996-4006 (1987)
   PUBMED   3500977
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079276.4.
            
            On Mar 17, 2018 this sequence version replaced XP_017177139.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR9219382.167564.1,
                                           SRR1660817.72120.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 12.36 cM"
     Protein         1..857
                     /product="transportin-3 isoform 3"
                     /note="transportin-SR"
                     /calculated_mol_wt=96506
     Region          55..183
                     /region_name="Xpo1"
                     /note="Exportin 1-like protein; pfam08389"
                     /db_xref="CDD:462459"
     CDS             1..857
                     /gene="Tnpo3"
                     /gene_synonym="5730544L10Rik; C430013M08Rik; D6Ertd313e;
                     mKIAA4133; Trn-SR"
                     /coded_by="NM_001361290.1:722..3295"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:320938"
                     /db_xref="MGI:MGI:1196412"
ORIGIN      
        1 mkmkiqtsfy elptdshasl rdsllthiqn lkdlspvivt qlalaiadla lqmpswkgcv
       61 qtlvekysnd vtslpfllei ltvlpeevhs rslriganrr teiiedlafy sstvvsllmt
      121 cvekagtdek mlmkvfrclg swfnlgvlds nfmannklla llfevlqqdk tssnlheaas
      181 dcvcsalyai envetnlpla mqlfqgvltl etayhmavar edldkvlnyc riftelcetf
      241 lekivctpgq glgdlrtlel llicaghpqy evveisfnfw yrlgehlykt ndevihsifk
      301 ayiqrllhal arhcqlepdh egvpeetddf gefrmrvsdl vkdlifligs mecfaqlyst
      361 lkegnppwev teavlfimaa iaksvdpenn ptlvevlegv vhlpetvhta vrytsielvg
      421 emsevvdrnp qfldpvlgyl mkglcekpla saaakaihni csvcrdhmaq hfnglleiah
      481 sldsfmlspe aavgllkgta lvlarlpldk iteclselcs vqvmalkkll sqepsngiss
      541 dptvfldrla vifrhtnpiv engqthpcqk viqeiwpvls etlnkhradn riverccrcl
      601 rfavrcvgkg saallqplvt qmvnvyhvhq hscflylgsi lvdeygmeeg crqglldmlq
      661 alciptfqll eqqnglqnhp dtvddlfrla trfiqrspvt llrsqvvipi lqwaiasttl
      721 dhrdanssvm rflrdlihtg vandheedfe lrkeligqvm sqlgqqlvsq llhtccfclp
      781 pytlpdvaev lweimqvdrp tfcrwlensl kglpkettvg avtvthkqlt dfhkqvtsae
      841 eckqvcwalr dftrlfr
//
LOCUS       NP_997226                703 aa            linear   PRI 27-APR-2025
DEFINITION  RING finger protein 214 isoform 1 [Homo sapiens].
ACCESSION   NP_997226
VERSION     NP_997226.2
DBSOURCE    REFSEQ: accession NM_207343.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Schurks,M., Buring,J.E., Ridker,P.M., Chasman,D.I. and Kurth,T.
  TITLE     Genetic determinants of cardiovascular events among women with
            migraine: a genome-wide association study
  JOURNAL   PLoS One 6 (7), e22106 (2011)
   PUBMED   21779381
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC423629.1, AK298923.1, BX111206.1 and AP000892.4.
            
            On Oct 17, 2006 this sequence version replaced NP_997226.1.
            
            Transcript Variant: This variant (2) has an alternate 5' UTR exon,
            compared to variant 1. Both variants 1 and 2 encode the same
            isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.135675.1,
                                           SRR1660807.69395.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300650.9/ ENSP00000300650.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..703
                     /product="RING finger protein 214 isoform 1"
                     /calculated_mol_wt=77537
     Region          1..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND24.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8ND24.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8ND24.2)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8ND24.2)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8ND24.2)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8ND24.2)"
     Region          104..134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND24.2)"
     Region          146..197
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND24.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8ND24.2)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BFU3; propagated from
                     UniProtKB/Swiss-Prot (Q8ND24.2)"
     Region          486..552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND24.2)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8ND24.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8ND24.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8ND24.2)"
     Region          656..700
                     /region_name="RING-H2_RNF214"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 214 (RNF214) and similar proteins; cd16477"
                     /db_xref="CDD:438140"
     CDS             1..703
                     /gene="RNF214"
                     /coded_by="NM_207343.4:63..2174"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41720.1"
                     /db_xref="GeneID:257160"
                     /db_xref="HGNC:HGNC:25335"
ORIGIN      
        1 maasevagvv anapsppess slcasksdeg lpdglstkds aqkqknspll svssqtitke
       61 nnrnvhlehs eqnpgssagd tsaahqvvlg enliatalcl sgsgsqsdlk dvastageeg
      121 dtslreslhp vtrslkagch tkqlasrncs eekspqtsil kegnrdtsld frpvvspang
      181 vegvrvdqdd dqdssslkls qniavqtdfk tadsevntdq dieknldkmm tertllkery
      241 qevldkqrqv enqlqvqlkq lqqrreeemk nhqeilkaiq dvtikreetk kkiekekkef
      301 lqkeqdlkae ieklcekgrr evwemeldrl knqdgeinrn imeeterawk aeilslesrk
      361 ellvlkleea ekeaelhlty lkstpptlet vrskqewetr lngvrimkkn vrdqfnshiq
      421 lvrngaklss lpqiptptlp pppsetdfml qvfqpspsla prmpfsigqv tmpmvmpsad
      481 prslsfpiln palsqpsqps splpgshgrn spglgslvsp hgphmppaas ippppglggv
      541 kasaetprpq pvdklekile klltrfpqcn kaqmtnilqq iktarttmag ltmeeliqlv
      601 aarlaeherv aastqplgri ralfpaplaq istpmflpsa qvsypgrssh apatcklclm
      661 cqklvqpsel hpmacthvlh kecikfwaqt ntndtcpfcp tlk
//
LOCUS       NP_080301                217 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger CCHC-type and RNA-binding motif-containing protein 1
            isoform 1 [Mus musculus].
ACCESSION   NP_080301
VERSION     NP_080301.1
DBSOURCE    REFSEQ: accession NM_026025.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Horiuchi,K., Perez-Cerezales,S., Papasaikas,P., Ramos-Ibeas,P.,
            Lopez-Cardona,A.P., Laguna-Barraza,R., Fonseca Balvis,N.,
            Pericuesta,E., Fernandez-Gonzalez,R., Planells,B., Viera,A.,
            Suja,J.A., Ross,P.J., Alen,F., Orio,L., Rodriguez de Fonseca,F.,
            Pintado,B., Valcarcel,J. and Gutierrez-Adan,A.
  TITLE     Impaired Spermatogenesis, Muscle, and Erythrocyte Function in U12
            Intron Splicing-Defective Zrsr1 Mutant Mice
  JOURNAL   Cell Rep 23 (1), 143-155 (2018)
   PUBMED   29617656
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Wang,H., Gao,M.X., Li,L., Wang,B., Hori,N. and Sato,K.
  TITLE     Isolation, expression, and characterization of the human ZCRB1 gene
            mapped to 12q12
  JOURNAL   Genomics 89 (1), 59-69 (2007)
   PUBMED   16959469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC126556.4, AK012852.1 and AI666574.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB095989.1, AK012852.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 47.53 cM"
     Protein         1..217
                     /product="zinc finger CCHC-type and RNA-binding
                     motif-containing protein 1 isoform 1"
                     /note="zinc finger CCHC-type and RNA-binding
                     motif-containing protein 1; U11/U12 snRNP 31 kDa protein;
                     U11/U12 small nuclear ribonucleoprotein 31 kDa protein"
                     /calculated_mol_wt=24452
     Region          9..84
                     /region_name="RRM_ZCRB1"
                     /note="RNA recognition motif (RRM) found in Zinc finger
                     CCHC-type and RNA-binding motif-containing protein 1
                     (ZCRB1) and similar proteins; cd12393"
                     /db_xref="CDD:409827"
     Region          <97..123
                     /region_name="PTZ00368"
                     /note="universal minicircle sequence binding protein
                     (UMSBP); Provisional"
                     /db_xref="CDD:173561"
     Region          120..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZ96.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CZ96.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CZ96.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CZ96.1)"
     CDS             1..217
                     /gene="Zcrb1"
                     /gene_synonym="2700088M22Rik; Madp-1"
                     /coded_by="NM_026025.3:175..828"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS27766.1"
                     /db_xref="GeneID:67197"
                     /db_xref="MGI:MGI:1914447"
ORIGIN      
        1 msgglapsks tvyvsnlpfs ltnndlyrif skygkvvkvt imkdkdtrks kgvafilfld
       61 kdsalnctra innkqlfgrv ikasiaidng raaefirrrn yfdkskcyec gesghlsyac
      121 pknmlgerep pkkkekkkkr klpepeeeie evevseeege dpaldslsqa iafqqakiee
      181 eqskwrpnpg gpstsddsrr prikksayfs deeelsd
//
LOCUS       NP_037453                465 aa            linear   PRI 27-APR-2025
DEFINITION  sorting nexin-8 [Homo sapiens].
ACCESSION   NP_037453
VERSION     NP_037453.1
DBSOURCE    REFSEQ: accession NM_013321.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Li,X., Xiang,C., Zhu,S., Guo,J., Liu,C., Wang,A., Cao,J., Lu,Y.,
            Neculai,D., Xu,P. and Feng,X.H.
  TITLE     SNX8 enables lysosome reformation and reverses lysosomal storage
            disorder
  JOURNAL   Nat Commun 15 (1), 2553 (2024)
   PUBMED   38519472
  REMARK    GeneRIF: SNX8 enables lysosome reformation and reverses lysosomal
            storage disorder.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Hu,Y., He,W., Huang,Y., Xiang,H., Guo,J., Che,Y., Cheng,X., Hu,F.,
            Hu,M., Ma,T., Yu,J., Tian,H., Tian,S., Ji,Y.X., Zhang,P., She,Z.G.,
            Zhang,X.J., Huang,Z., Yang,J. and Li,H.
  TITLE     Fatty Acid Synthase-Suppressor Screening Identifies Sorting Nexin 8
            as a Therapeutic Target for NAFLD
  JOURNAL   Hepatology 74 (5), 2508-2525 (2021)
   PUBMED   34231239
  REMARK    GeneRIF: Fatty Acid Synthase-Suppressor Screening Identifies
            Sorting Nexin 8 as a Therapeutic Target for NAFLD.
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Suzuki,S.W., Oishi,A., Nikulin,N., Jorgensen,J.R., Baile,M.G. and
            Emr,S.D.
  TITLE     A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive
            endosomal recycling
  JOURNAL   Elife 10, e69883 (2021)
   PUBMED   34524084
  REMARK    GeneRIF: A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1
            drive endosomal recycling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Wei,J., Guo,W., Lian,H., Yang,Q., Lin,H., Li,S. and Shu,H.B.
  TITLE     SNX8 mediates IFNgamma-triggered noncanonical signaling pathway and
            host defense against Listeria monocytogenes
  JOURNAL   Proc Natl Acad Sci U S A 114 (49), 13000-13005 (2017)
   PUBMED   29180417
  REMARK    GeneRIF: SNX8 mediates IFNG-triggered non-canonical signaling
            pathway and host defense against Listeria monocytogenes.
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Wang,K.S., Liu,X.F. and Aragam,N.
  TITLE     A genome-wide meta-analysis identifies novel loci associated with
            schizophrenia and bipolar disorder
  JOURNAL   Schizophr Res 124 (1-3), 192-199 (2010)
   PUBMED   20889312
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Dyve,A.B., Bergan,J., Utskarpen,A. and Sandvig,K.
  TITLE     Sorting nexin 8 regulates endosome-to-Golgi transport
  JOURNAL   Biochem Biophys Res Commun 390 (1), 109-114 (2009)
   PUBMED   19782049
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC021565.1, AC004971.3 and AL713633.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021565.1, AK074544.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222990.8/ ENSP00000222990.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..465
                     /product="sorting nexin-8"
                     /calculated_mol_wt=52438
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5X2.1)"
     Region          75..178
                     /region_name="PX_SNX8_Mvp1p_like"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 8 and yeast Mvp1p; cd06866"
                     /db_xref="CDD:132776"
     Site            order(109..111,135..136,148)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132776"
     Region          195..440
                     /region_name="BAR_SNX8"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Sorting
                     Nexin 8; cd07597"
                     /db_xref="CDD:153281"
     Site            order(217,220..221,225,227..228,231..232,234..235,
                     252..253,255..256,259..260,262..263,266,295,298..299,401,
                     404..405,407,412,415..416,418..419,422..423,426..427,
                     429..430,433..434,436..437)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153281"
     Site            order(217,220..221,225,227..228,231,234..235,252..253,
                     255..256,259,262..263,266,295,401,404..405,407,412,
                     415..416,418..420,422..423,426..427,429..430,434,436..437)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153281"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5X2.1)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5X2.1)"
     CDS             1..465
                     /gene="SNX8"
                     /gene_synonym="Mvp1"
                     /coded_by="NM_013321.4:21..1418"
                     /db_xref="CCDS:CCDS5331.1"
                     /db_xref="GeneID:29886"
                     /db_xref="HGNC:HGNC:14972"
                     /db_xref="MIM:614905"
ORIGIN      
        1 mtgramdplp aaavgaaaea eadeeadppa sdlptpqaie pqaivqqvpa psrmqmpqgn
       61 plllshtlqe llardtvqve lipekkglfl khveyevssq rfkssvyrry ndfvvfqeml
      121 lhkfpyrmvp alppkrmlga drefiearrr alkrfvnlva rhplfsedvv lklflsfsgs
      181 dvqnklkesa qcvgdeflnc klatrakdfl padiqaqfai srelirniyn sfhklrdrae
      241 riasraidna adllifgkel saigsdttpl pswaalnsst wgslkqalkg lsvefallad
      301 kaaqqgkqee ndvveklnlf ldllqsykdl cerhekgvlh khqralhkys lmkrqmmsat
      361 aqnrepesve qlesriveqe naiqtmelrn yfslyclhqe tqlihvylpl tshilrafvn
      421 sqiqghkems kvwndlrpkl sclfagphst ltppcspped glcph
//
LOCUS       NP_004858                263 aa            linear   PRI 27-APR-2025
DEFINITION  integral membrane protein 2A isoform 1 [Homo sapiens].
ACCESSION   NP_004858
VERSION     NP_004858.1
DBSOURCE    REFSEQ: accession NM_004867.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Cho,W.K., Baek,I.C., Kim,S.E., Kim,M., Kim,T.G. and Suh,B.K.
  TITLE     Association of ITM2A rs1751094 polymorphism on X chromosome in
            Korean pediatric patients with autoimmune thyroid disease
  JOURNAL   Immun Inflamm Dis 11 (3), e800 (2023)
   PUBMED   36988246
  REMARK    GeneRIF: Association of ITM2A rs1751094 polymorphism on X
            chromosome in Korean pediatric patients with autoimmune thyroid
            disease.
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Zhao,N.Q., Pan,C.Y., Zhang,T.Z., Liu,P., Hu,T.Z., Shang,Q., Luo,H.,
            Fang,Q. and Wang,J.S.
  TITLE     [Study on the Relationship between Integrin 2A and Drug Resistance
            in Chronic Myeloid Leukemia]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 31 (1), 8-16 (2023)
   PUBMED   36765470
  REMARK    GeneRIF: [Study on the Relationship between Integrin 2A and Drug
            Resistance in Chronic Myeloid Leukemia].
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Morales-Alcala,C.C., Georgiou,I.C., Timmis,A.J. and Riobo-Del
            Galdo,N.A.
  TITLE     Integral Membrane Protein 2A Is a Negative Regulator of Canonical
            and Non-Canonical Hedgehog Signalling
  JOURNAL   Cells 10 (8), 2003 (2021)
   PUBMED   34440772
  REMARK    GeneRIF: Integral Membrane Protein 2A Is a Negative Regulator of
            Canonical and Non-Canonical Hedgehog Signalling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Lari,A., Gholami Pourbadie,H., Jafari,M., Sharifi-Zarchi,A.,
            Akhtari,M., Nejatbakhsh Samimi,L., Jamshidi,A. and Mahmoudi,M.
  TITLE     Downregulation of ITM2A Gene Expression in Macrophages of Patients
            with Ankylosing Spondylitis
  JOURNAL   Int Arch Allergy Immunol 182 (11), 1113-1121 (2021)
   PUBMED   34161951
  REMARK    GeneRIF: Downregulation of ITM2A Gene Expression in Macrophages of
            Patients with Ankylosing Spondylitis.
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Cho,W.K., Shin,H.R., Lee,N.Y., Kim,S.K., Ahn,M.B., Baek,I.C.,
            Kim,T.G. and Suh,B.K.
  TITLE     GPR174 and ITM2A Gene Polymorphisms rs3827440 and rs5912838 on the
            X chromosome in Korean Children with Autoimmune Thyroid Disease
  JOURNAL   Genes (Basel) 11 (8), 858 (2020)
   PUBMED   32727090
  REMARK    GeneRIF: GPR174 and ITM2A Gene Polymorphisms rs3827440 and
            rs5912838 on the X chromosome in Korean Children with Autoimmune
            Thyroid Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Kirchner,J. and Bevan,M.J.
  TITLE     ITM2A is induced during thymocyte selection and T cell activation
            and causes downregulation of CD8 when overexpressed in CD4(+)CD8(+)
            double positive thymocytes
  JOURNAL   J Exp Med 190 (2), 217-228 (1999)
   PUBMED   10432285
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Pittois,K., Wauters,J., Bossuyt,P., Deleersnijder,W. and
            Merregaert,J.
  TITLE     Genomic organization and chromosomal localization of the Itm2a gene
  JOURNAL   Mamm Genome 10 (1), 54-56 (1999)
   PUBMED   9892734
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
REFERENCE   9  (residues 1 to 263)
  AUTHORS   Deleersnijder,W., Hong,G., Cortvrindt,R., Poirier,C.,
            Tylzanowski,P., Pittois,K., Van Marck,E. and Merregaert,J.
  TITLE     Isolation of markers for chondro-osteogenic differentiation using
            cDNA library subtraction. Molecular cloning and characterization of
            a gene belonging to a novel multigene family of integral membrane
            proteins
  JOURNAL   J Biol Chem 271 (32), 19475-19482 (1996)
   PUBMED   8702637
REFERENCE   10 (residues 1 to 263)
  AUTHORS   Prashar,Y. and Weissman,S.M.
  TITLE     Analysis of differential gene expression by display of 3' end
            restriction fragments of cDNAs
  JOURNAL   Proc Natl Acad Sci U S A 93 (2), 659-663 (1996)
   PUBMED   8570611
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA365726.1, BC040437.1,
            BM561934.1 and AY359051.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a type II membrane protein that belongs
            to the ITM2 family. Studies in mouse suggest that it may be
            involved in osteo- and chondrogenic differentiation. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034485.1, SRR3476690.1175785.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373298.7/ ENSP00000362395.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq21.1"
     Protein         1..263
                     /product="integral membrane protein 2A isoform 1"
                     /note="BRICHOS domain containing 2A"
                     /calculated_mol_wt=29610
     Site            54..74
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43736.2)"
     Region          133..225
                     /region_name="BRICHOS"
                     /note="The BRICHOS domain is found in a variety of
                     proteins implicated in dementia, respiratory distress and
                     cancer; smart01039"
                     /db_xref="CDD:198107"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43736.2)"
     CDS             1..263
                     /gene="ITM2A"
                     /gene_synonym="BRICD2A; E25A"
                     /coded_by="NM_004867.5:120..911"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14444.1"
                     /db_xref="GeneID:9452"
                     /db_xref="HGNC:HGNC:6173"
                     /db_xref="MIM:300222"
ORIGIN      
        1 mvkiafntpt avqkeearqd veallsrtvr tqiltgkelr vatqekegss grcmltllgl
       61 sfilaglivg gaciykyfmp kstiyrgemc ffdsedpans lrggepnflp vteeadired
      121 dniaiidvpv psfsdsdpaa iihdfekgmt ayldlllgnc ylmplntsiv mppknlvelf
      181 gklasgrylp qtyvvredlv aveeirdvsn lgifiyqlcn nrksfrlrrr dlllgfnkra
      241 idkcwkirhf pnefivetki cqe
//
LOCUS       NP_001093143             100 aa            linear   PRI 27-APR-2025
DEFINITION  ribosomal biogenesis factor isoform 1 [Homo sapiens].
ACCESSION   NP_001093143
VERSION     NP_001093143.1
DBSOURCE    REFSEQ: accession NM_001099673.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Badertscher,L., Wild,T., Montellese,C., Alexander,L.T., Bammert,L.,
            Sarazova,M., Stebler,M., Csucs,G., Mayer,T.U., Zamboni,N., Zemp,I.,
            Horvath,P. and Kutay,U.
  TITLE     Genome-wide RNAi Screening Identifies Protein Modules Required for
            40S Subunit Synthesis in Human Cells
  JOURNAL   Cell Rep 13 (12), 2879-2891 (2015)
   PUBMED   26711351
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Tafforeau,L., Zorbas,C., Langhendries,J.L., Mullineux,S.T.,
            Stamatopoulou,V., Mullier,R., Wacheul,L. and Lafontaine,D.L.
  TITLE     The complexity of human ribosome biogenesis revealed by systematic
            nucleolar screening of Pre-rRNA processing factors
  JOURNAL   Mol Cell 51 (4), 539-551 (2013)
   PUBMED   23973377
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   5  (residues 1 to 100)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   6  (residues 1 to 100)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 100)
  AUTHORS   Kumar,S., Connor,J.R., Dodds,R.A., Halsey,W., Van Horn,M., Mao,J.,
            Sathe,G., Mui,P., Agarwal,P., Badger,A.M., Lee,J.C., Gowen,M. and
            Lark,M.W.
  TITLE     Identification and initial characterization of 5000 expressed
            sequenced tags (ESTs) each from adult human normal and
            osteoarthritic cartilage cDNA libraries
  JOURNAL   Osteoarthritis Cartilage 9 (7), 641-653 (2001)
   PUBMED   11597177
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC055092.1 and AC011773.9.
            
            Transcript Variant: This variant (4) differs in the 5' UTR,
            compared to variant 1. Variants 1-4 encode the same isoform (1).
            
            CCDS Note: The coding region was updated to include a 6-nt
            insertion found in the GRCh38 reference genome assembly and in
            aligning transcripts, resulting in two extra amino acids in the
            protein C-terminus.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.570162.1,
                                           SRR1660807.422880.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2150385, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000619594.5/ ENSP00000484492.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..100
                     /product="ribosomal biogenesis factor isoform 1"
                     /note="uncharacterized protein C8orf59; ribosome
                     biogenesis factor identified in screen"
                     /calculated_mol_wt=11325
     Region          1..100
                     /region_name="DUF4665"
                     /note="Domain of unknown function (DUF4665); pfam15679"
                     /db_xref="CDD:464797"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N0T1.4)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N0T1.4)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N0T1.4)"
     CDS             1..100
                     /gene="RBIS"
                     /gene_synonym="C8orf59"
                     /coded_by="NM_001099673.3:73..375"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55255.1"
                     /db_xref="GeneID:401466"
                     /db_xref="HGNC:HGNC:32235"
ORIGIN      
        1 maknklrgpk srnvfhiasq knfkaknkak pvttnlkkin imneekvnrv nkafvnvqke
       61 lahfaksisl eplqkelipq qrheskpvnv deatrlmall
//
LOCUS       NP_115699                394 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 79 [Homo sapiens].
ACCESSION   NP_115699
VERSION     NP_115699.1
DBSOURCE    REFSEQ: accession NM_032323.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Zhang,W., Fan,C., Yi,Z., Du,T., Wang,N., Tian,W., Pan,Q., Ma,X. and
            Wang,Z.
  TITLE     TMEM79 Ameliorates Cerebral Ischemia/Reperfusion Injury Through
            Regulating Inflammation and Oxidative Stress via the Nrf2/NLRP3
            Pathway
  JOURNAL   Immunol Invest 53 (6), 872-890 (2024)
   PUBMED   38809063
  REMARK    GeneRIF: TMEM79 Ameliorates Cerebral Ischemia/Reperfusion Injury
            Through Regulating Inflammation and Oxidative Stress via the
            Nrf2/NLRP3 Pathway.
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Wang,Y., Jin,Q., Zhang,S. and Wang,Y.
  TITLE     Overexpression of TMEM79 combined with SMG5 is related to
            prognosis, tumor immune infiltration and drug sensitivity in
            hepatocellular carcinoma
  JOURNAL   Eur J Med Res 28 (1), 490 (2023)
   PUBMED   37936239
  REMARK    GeneRIF: Overexpression of TMEM79 combined with SMG5 is related to
            prognosis, tumor immune infiltration and drug sensitivity in
            hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Elias,P.M. and Wakefield,J.S.
  TITLE     Mechanisms of abnormal lamellar body secretion and the
            dysfunctional skin barrier in patients with atopic dermatitis
  JOURNAL   J Allergy Clin Immunol 134 (4), 781-791 (2014)
   PUBMED   25131691
  REMARK    Review article
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Chen,P., Takeuchi,F., Lee,J.Y., Li,H., Wu,J.Y., Liang,J., Long,J.,
            Tabara,Y., Goodarzi,M.O., Pereira,M.A., Kim,Y.J., Go,M.J.,
            Stram,D.O., Vithana,E., Khor,C.C., Liu,J., Liao,J., Ye,X., Wang,Y.,
            Lu,L., Young,T.L., Lee,J., Thai,A.C., Cheng,C.Y., van Dam,R.M.,
            Friedlander,Y., Heng,C.K., Koh,W.P., Chen,C.H., Chang,L.C.,
            Pan,W.H., Qi,Q., Isono,M., Zheng,W., Cai,Q., Gao,Y., Yamamoto,K.,
            Ohnaka,K., Takayanagi,R., Kita,Y., Ueshima,H., Hsiung,C.A., Cui,J.,
            Sheu,W.H., Rotter,J.I., Chen,Y.D., Hsu,C., Okada,Y., Kubo,M.,
            Takahashi,A., Tanaka,T., van Rooij,F.J., Ganesh,S.K., Huang,J.,
            Huang,T., Yuan,J., Hwang,J.Y., Gross,M.D., Assimes,T.L., Miki,T.,
            Shu,X.O., Qi,L., Chen,Y.T., Lin,X., Aung,T., Wong,T.Y., Teo,Y.Y.,
            Kim,B.J., Kato,N. and Tai,E.S.
  CONSRTM   CHARGE Hematology Working Group
  TITLE     Multiple nonglycemic genomic loci are newly associated with blood
            level of glycated hemoglobin in East Asians
  JOURNAL   Diabetes 63 (7), 2551-2562 (2014)
   PUBMED   24647736
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Saunders,S.P., Goh,C.S., Brown,S.J., Palmer,C.N., Porter,R.M.,
            Cole,C., Campbell,L.E., Gierlinski,M., Barton,G.J., Schneider,G.,
            Balmain,A., Prescott,A.R., Weidinger,S., Baurecht,H., Kabesch,M.,
            Gieger,C., Lee,Y.A., Tavendale,R., Mukhopadhyay,S., Turner,S.W.,
            Madhok,V.B., Sullivan,F.M., Relton,C., Burn,J., Meggitt,S.,
            Smith,C.H., Allen,M.A., Barker,J.N., Reynolds,N.J., Cordell,H.J.,
            Irvine,A.D., McLean,W.H., Sandilands,A. and Fallon,P.G.
  TITLE     Tmem79/Matt is the matted mouse gene and is a predisposing gene for
            atopic dermatitis in human subjects
  JOURNAL   J Allergy Clin Immunol 132 (5), 1121-1129 (2013)
   PUBMED   24084074
  REMARK    GeneRIF: Tmem79/Matt is the matted mouse gene and is a predisposing
            gene for atopic dermatitis in human subjects.
            Erratum:[J Allergy Clin Immunol. 2015 Dec;136(6):1710. doi:
            10.1016/j.jaci.2015.10.002. PMID: 28843836]
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Kamatani,Y., Matsuda,K., Okada,Y., Kubo,M., Hosono,N., Daigo,Y.,
            Nakamura,Y. and Kamatani,N.
  TITLE     Genome-wide association study of hematological and biochemical
            traits in a Japanese population
  JOURNAL   Nat Genet 42 (3), 210-215 (2010)
   PUBMED   20139978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK315767.1, BC005094.1 and BF448444.1.
            
            Transcript Variant: This variant (1) encodes a 394aa protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279842.990.1, AK315767.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000405535.3/ ENSP00000384748.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..394
                     /product="transmembrane protein 79"
                     /note="mattrin"
                     /calculated_mol_wt=43389
     Region          1..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSE2.1)"
     Site            204..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSE2.1)"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSE2.1)"
     Site            283..303
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSE2.1)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSE2.1)"
     Site            343..363
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSE2.1)"
     CDS             1..394
                     /gene="TMEM79"
                     /gene_synonym="MATT"
                     /coded_by="NM_032323.3:126..1310"
                     /db_xref="CCDS:CCDS1138.1"
                     /db_xref="GeneID:84283"
                     /db_xref="HGNC:HGNC:28196"
                     /db_xref="MIM:615531"
ORIGIN      
        1 mteqetlall evkrsdspek sspqalvpng rqpegeggae spgaeslrvg ssagsptaie
       61 gaedgldstv seaatlpwgt gpqpsapfpd ppgwrdiepe ppesepltkl eelpeddanl
      121 lpekaarafv pidlqcierq pqedlivrce agegecrtfm pprvthpdpt erkwaeavvr
      181 ppgcscggcg scgdrewlra vasvgaalil fpcllygaya flpfdvprlp tmssrliytl
      241 rcgvfatfpi vlgilvygls llcfsalrpf geprreveih rryvaqsvql filyffnlav
      301 lstylpqdtl kllplltglf avsrliywlt favgrsfrgf gygltflpll smlmwnlyym
      361 fvvepermlt atesrldypd harsasdyrp rpwg
//
LOCUS       NP_996846                294 aa            linear   PRI 27-APR-2025
DEFINITION  retinoic acid receptor responder protein 1 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_996846
VERSION     NP_996846.1
DBSOURCE    REFSEQ: accession NM_206963.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Feng,Y., Sun,Z., Fu,J., Zhong,F., Zhang,W., Wei,C., Chen,A.,
            Liu,B.C., He,J.C. and Lee,K.
  TITLE     Podocyte-derived soluble RARRES1 drives kidney disease progression
            through direct podocyte and proximal tubular injury
  JOURNAL   Kidney Int 106 (1), 50-66 (2024)
   PUBMED   38697478
  REMARK    GeneRIF: Podocyte-derived soluble RARRES1 drives kidney disease
            progression through direct podocyte and proximal tubular injury.
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Wang,C.H., Tzeng,I.S., Wang,L.K., Wu,C.C., Chen,M.L., Kuo,C.Y.,
            Shyu,R.Y. and Tsai,F.M.
  TITLE     Tazarotene-induced Gene 1 Induces Melanoma Cell Death by Triggering
            Endoplasmic Reticulum Stress Response
  JOURNAL   Front Biosci (Landmark Ed) 29 (6), 233 (2024)
   PUBMED   38940043
  REMARK    GeneRIF: Tazarotene-induced Gene 1 Induces Melanoma Cell Death by
            Triggering Endoplasmic Reticulum Stress Response.
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Liu,M., Bai,R., Zhang,G., Liu,X., Wang,Z., He,K., Gan,X., Zhou,X.,
            Yin,P., Zheng,Y. and Wang,G.
  TITLE     RARRES1 identified by comprehensive bioinformatic analysis and
            experimental validation as a promising biomarker in Skin Cutaneous
            Melanoma
  JOURNAL   Sci Rep 14 (1), 14113 (2024)
   PUBMED   38898266
  REMARK    GeneRIF: RARRES1 identified by comprehensive bioinformatic analysis
            and experimental validation as a promising biomarker in Skin
            Cutaneous Melanoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Zhang,H., Mulya,A., Nieuwoudt,S., Vandanmagsar,B., McDowell,R.,
            Heintz,E.C., Zunica,E.R.M., Collier,J.J., Bozadjieva-Kramer,N.,
            Seeley,R.J., Axelrod,C.L. and Kirwan,J.P.
  TITLE     GDF15 Mediates the Effect of Skeletal Muscle Contraction on
            Glucose-Stimulated Insulin Secretion
  JOURNAL   Diabetes 72 (8), 1070-1082 (2023)
   PUBMED   37224335
  REMARK    GeneRIF: GDF15 Mediates the Effect of Skeletal Muscle Contraction
            on Glucose-Stimulated Insulin Secretion.
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Wang,C.H., Wang,L.K., Wu,C.C., Chen,M.L., Kuo,C.Y., Shyu,R.Y. and
            Tsai,F.M.
  TITLE     TIG1 Inhibits the mTOR Signaling Pathway in Malignant Melanoma
            Through the VAC14 Protein
  JOURNAL   Anticancer Res 43 (6), 2635-2643 (2023)
   PUBMED   37247911
  REMARK    GeneRIF: TIG1 Inhibits the mTOR Signaling Pathway in Malignant
            Melanoma Through the VAC14 Protein.
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Youssef,E.M., Chen,X.Q., Higuchi,E., Kondo,Y., Garcia-Manero,G.,
            Lotan,R. and Issa,J.P.
  TITLE     Hypermethylation and silencing of the putative tumor suppressor
            Tazarotene-induced gene 1 in human cancers
  JOURNAL   Cancer Res 64 (7), 2411-2417 (2004)
   PUBMED   15059893
  REMARK    GeneRIF: Silencing of TIG1 promoter by hypermethylation is common
            in human cancers and may contribute to the loss of retinoic acid
            responsiveness in some neoplastic cells.
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Zhang,J., Liu,L. and Pfeifer,G.P.
  TITLE     Methylation of the retinoid response gene TIG1 in prostate cancer
            correlates with methylation of the retinoic acid receptor beta gene
  JOURNAL   Oncogene 23 (12), 2241-2249 (2004)
   PUBMED   14691453
REFERENCE   8  (residues 1 to 294)
  AUTHORS   Jing,C., El-Ghany,M.A., Beesley,C., Foster,C.S., Rudland,P.S.,
            Smith,P. and Ke,Y.
  TITLE     Tazarotene-induced gene 1 (TIG1) expression in prostate carcinomas
            and its relationship to tumorigenicity
  JOURNAL   J Natl Cancer Inst 94 (7), 482-490 (2002)
   PUBMED   11929948
REFERENCE   9  (residues 1 to 294)
  AUTHORS   Duvic,M., Nagpal,S., Asano,A.T. and Chandraratna,R.A.
  TITLE     Molecular mechanisms of tazarotene action in psoriasis
  JOURNAL   J Am Acad Dermatol 37 (2 Pt 3), S18-S24 (1997)
   PUBMED   9270552
  REMARK    Review article
REFERENCE   10 (residues 1 to 294)
  AUTHORS   Nagpal,S., Patel,S., Asano,A.T., Johnson,A.T., Duvic,M. and
            Chandraratna,R.A.
  TITLE     Tazarotene-induced gene 1 (TIG1), a novel retinoic acid
            receptor-responsive gene in skin
  JOURNAL   J Invest Dermatol 106 (2), 269-274 (1996)
   PUBMED   8601727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM919188.1, AK130079.1,
            BC029640.1 and AC080013.17.
            
            Summary: This gene was identified as a retinoid acid (RA)
            receptor-responsive gene. It encodes a type 1 membrane protein. The
            expression of this gene is upregulated by tazarotene as well as by
            retinoic acid receptors. The expression of this gene is found to be
            downregulated in prostate cancer, which is caused by the
            methylation of its promoter and CpG island. Alternatively spliced
            transcript variant encoding distinct isoforms have been observed.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. It encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK130079.1, BC029640.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000237696.10/ ENSP00000237696.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.32"
     Protein         1..294
                     /product="retinoic acid receptor responder protein 1
                     isoform 1 precursor"
                     /note="latexin-like; phorbol ester-induced gene 1 protein;
                     retinoic acid receptor responder protein 1; RAR-responsive
                     protein TIG1; retinoic acid receptor responder (tazarotene
                     induced) 1; tazarotene-induced gene 1 protein"
                     /calculated_mol_wt=29252
     sig_peptide     1..38
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4051
     Site            21..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49788.2)"
     Site            40
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:27399812,
                     ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717;
                     propagated from UniProtKB/Swiss-Prot (P49788.2)"
     Region          52..274
                     /region_name="Latexin"
                     /note="pfam06907"
                     /db_xref="CDD:462036"
     Region          273..294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49788.2)"
     CDS             1..294
                     /gene="RARRES1"
                     /gene_synonym="LXNL; PERG-1; TIG1"
                     /coded_by="NM_206963.2:43..927"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3184.1"
                     /db_xref="GeneID:5918"
                     /db_xref="HGNC:HGNC:9867"
                     /db_xref="MIM:605090"
ORIGIN      
        1 mqprrqrlpa pwsgprgprp tapllallll lapvaapags gdpddpgqpq dagvprrllq
       61 qaaraalhff nfrsgspsal rvlaevqegr awinpkegck vhvvfstery npesllqege
      121 grlgkcsarv ffknqkprpt invtctrlie kkkrqqedyl lykqmkqlkn pleivsipdn
      181 hghidpslrl iwdlaflgss yvmwemttqv shyylaqlts vrqwktnddt idfdytvllh
      241 elstqeiipc rihlvwypgk plkvkyhcqe lqtpeeasgt eegsavvpte lsnf
//
LOCUS       NP_861441                483 aa            linear   PRI 27-APR-2025
DEFINITION  proton-coupled amino acid transporter 2 [Homo sapiens].
ACCESSION   NP_861441
VERSION     NP_861441.2
DBSOURCE    REFSEQ: accession NM_181776.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Shi,J., Lu,D., Gu,R., Xu,Y., Pan,R., Bo,F. and Zhang,Y.
  TITLE     Identification of Key Biomarkers and Immune Infiltration in
            Sporadic Vestibular Schwannoma Basing Transcriptome-Wide Profiling
  JOURNAL   World Neurosurg 160, e591-e600 (2022)
   PUBMED   35092815
  REMARK    GeneRIF: Identification of Key Biomarkers and Immune Infiltration
            in Sporadic Vestibular Schwannoma Basing Transcriptome-Wide
            Profiling.
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Ussar,S., Lee,K.Y., Dankel,S.N., Boucher,J., Haering,M.F.,
            Kleinridders,A., Thomou,T., Xue,R., Macotela,Y., Cypess,A.M.,
            Tseng,Y.H., Mellgren,G. and Kahn,C.R.
  TITLE     ASC-1, PAT2, and P2RX5 are cell surface markers for white, beige,
            and brown adipocytes
  JOURNAL   Sci Transl Med 6 (247), 247ra103 (2014)
   PUBMED   25080478
  REMARK    GeneRIF: The amino acid transporter PAT2 and the purinergic
            receptor P2RX5 are cell surface markers expressed in classical
            brown and beige adipocytes.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Schioth,H.B., Roshanbin,S., Hagglund,M.G. and Fredriksson,R.
  TITLE     Evolutionary origin of amino acid transporter families SLC32, SLC36
            and SLC38 and physiological, pathological and therapeutic aspects
  JOURNAL   Mol Aspects Med 34 (2-3), 571-585 (2013)
   PUBMED   23506890
  REMARK    Review article
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Koskinen,L.L., Einarsdottir,E., Korponay-Szabo,I.R., Kurppa,K.,
            Kaukinen,K., Sistonen,P., Pocsai,Z., Szeles,G., Adany,R., Maki,M.,
            Kere,J. and Saavalainen,P.
  TITLE     Fine mapping of the CELIAC2 locus on chromosome 5q31-q33 in the
            Finnish and Hungarian populations
  JOURNAL   Tissue Antigens 74 (5), 408-416 (2009)
   PUBMED   19845895
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Broer,S., Bailey,C.G., Kowalczuk,S., Ng,C., Vanslambrouck,J.M.,
            Rodgers,H., Auray-Blais,C., Cavanaugh,J.A., Broer,A. and Rasko,J.E.
  TITLE     Iminoglycinuria and hyperglycinuria are discrete human phenotypes
            resulting from complex mutations in proline and glycine
            transporters
  JOURNAL   J Clin Invest 118 (12), 3881-3892 (2008)
   PUBMED   19033659
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Broer,S.
  TITLE     Amino acid transport across mammalian intestinal and renal
            epithelia
  JOURNAL   Physiol Rev 88 (1), 249-286 (2008)
   PUBMED   18195088
  REMARK    Review article
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Bermingham,J.R. Jr. and Pennington,J.
  TITLE     Organization and expression of the SLC36 cluster of amino acid
            transporter genes
  JOURNAL   Mamm Genome 15 (2), 114-125 (2004)
   PUBMED   15058382
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Rubio-Aliaga,I., Boll,M., Vogt Weisenhorn,D.M., Foltz,M., Kottra,G.
            and Daniel,H.
  TITLE     The proton/amino acid cotransporter PAT2 is expressed in neurons
            with a different subcellular localization than its paralog PAT1
  JOURNAL   J Biol Chem 279 (4), 2754-2760 (2004)
   PUBMED   14600155
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Boll,M., Foltz,M., Rubio-Aliaga,I. and Daniel,H.
  TITLE     A cluster of proton/amino acid transporter genes in the human and
            mouse genomes
  JOURNAL   Genomics 82 (1), 47-56 (2003)
   PUBMED   12809675
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Boll,M., Foltz,M., Rubio-Aliaga,I., Kottra,G. and Daniel,H.
  TITLE     Functional characterization of two novel mammalian electrogenic
            proton-dependent amino acid cotransporters
  JOURNAL   J Biol Chem 277 (25), 22966-22973 (2002)
   PUBMED   11959859
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC362112.1, BC101101.1,
            AC008385.7 and AY162214.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 3, 2009 this sequence version replaced NP_861441.1.
            
            Summary: This gene encodes a pH-dependent proton-coupled amino acid
            transporter that belongs to the amino acid auxin permease 1 protein
            family. The encoded protein primarily transports small amino acids
            such as glycine, alanine and proline. Mutations in this gene are
            associated with iminoglycinuria and hyperglycinuria. [provided by
            RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY162214.1, BC101101.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335244.9/ ENSP00000334223.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..483
                     /product="proton-coupled amino acid transporter 2"
                     /note="tramdorin-1; solute carrier family 36 (proton/amino
                     acid symporter), member 2; transmembrane domain rich
                     protein 1"
                     /calculated_mol_wt=53085
     Region          26..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Region          52..463
                     /region_name="SLC5-6-like_sbd"
                     /note="Solute carrier families 5 and 6-like; solute
                     binding domain; cl00456"
                     /db_xref="CDD:444915"
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Site            198..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Site            223..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Site            265..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Site            297..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Site            350..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Site            380..400
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Site            405..425
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     Site            438..458
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q495M3.1)"
     CDS             1..483
                     /gene="SLC36A2"
                     /gene_synonym="PAT2; TRAMD1"
                     /coded_by="NM_181776.3:100..1551"
                     /db_xref="CCDS:CCDS4315.1"
                     /db_xref="GeneID:153201"
                     /db_xref="HGNC:HGNC:18762"
                     /db_xref="MIM:608331"
ORIGIN      
        1 msvtkstegp qgavaikldl msppesakkl enkdstflde spsesaglkk tkgitvfqal
       61 ihlvkgnmgt gilglplavk nagilmgpls llvmgfiach cmhilvkcaq rfckrlnkpf
      121 mdygdtvmhg leanpnawlq nhahwgrhiv sffliitqlg fccvyivfla dnlkqvveav
      181 nsttnncysn etviltptmd srlymlsflp flvllvlirn lriltifsml anismlvslv
      241 iiiqyitqei pdpsrlplva swktyplffg taifsfesig vvlplenkmk narhfpails
      301 lgmsivtsly igmaalgylr fgddikasis lnlpncwlyq svkllyiagi lctyalqfyv
      361 paeiiipfai srvstrwalp ldlsirlvmv cltcllaili prldlvislv gsvsgtalal
      421 iippllevtt fysegmsplt ifkdalisil gfvgfvvgty qaldellkse dshpfsnstt
      481 fvr
//
LOCUS       NP_001136402             524 aa            linear   PRI 27-APR-2025
DEFINITION  apoptosis inhibitor 5 isoform a [Homo sapiens].
ACCESSION   NP_001136402
VERSION     NP_001136402.1
DBSOURCE    REFSEQ: accession NM_001142930.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Kuttanamkuzhi,A., Panda,D., Malaviya,R., Gaidhani,G. and Lahiri,M.
  TITLE     Altered expression of anti-apoptotic protein Api5 affects breast
            tumorigenesis
  JOURNAL   BMC Cancer 23 (1), 374 (2023)
   PUBMED   37095445
  REMARK    GeneRIF: Altered expression of anti-apoptotic protein Api5 affects
            breast tumorigenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Matsuzawa-Ishimoto,Y., Yao,X., Koide,A., Ueberheide,B.M.,
            Axelrad,J.E., Reis,B.S., Parsa,R., Neil,J.A., Devlin,J.C.,
            Rudensky,E., Dewan,M.Z., Cammer,M., Blumberg,R.S., Ding,Y.,
            Ruggles,K.V., Mucida,D., Koide,S. and Cadwell,K.
  TITLE     The gammadelta IEL effector API5 masks genetic susceptibility to
            Paneth cell death
  JOURNAL   Nature 610 (7932), 547-554 (2022)
   PUBMED   36198790
  REMARK    GeneRIF: The gammadelta IEL effector API5 masks genetic
            susceptibility to Paneth cell death.
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Deng,T., Hu,B., Wang,X., Yan,Y., Zhou,J., Lin,L., Xu,Y., Zheng,X.
            and Zhou,J.
  TITLE     DeSUMOylation of Apoptosis Inhibitor 5 by Avibirnavirus VP3
            Supports Virus Replication
  JOURNAL   mBio 12 (4), e0198521 (2021)
   PUBMED   34372697
  REMARK    GeneRIF: DeSUMOylation of Apoptosis Inhibitor 5 by Avibirnavirus
            VP3 Supports Virus Replication.
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Sharma,V.K. and Lahiri,M.
  TITLE     Interplay between p300 and HDAC1 regulate acetylation and stability
            of Api5 to regulate cell proliferation
  JOURNAL   Sci Rep 11 (1), 16427 (2021)
   PUBMED   34385547
  REMARK    GeneRIF: Interplay between p300 and HDAC1 regulate acetylation and
            stability of Api5 to regulate cell proliferation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Li,Z., Hu,C.Y., Mo,B.Q., Xu,J.D. and Zhao,Y.
  TITLE     [Effect of beta-carotene on gene expression of breast cancer cells]
  JOURNAL   Ai Zheng 22 (4), 380-384 (2003)
   PUBMED   12703993
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Van den Berghe,L., Laurell,H., Huez,I., Zanibellato,C., Prats,H.
            and Bugler,B.
  TITLE     FIF [fibroblast growth factor-2 (FGF-2)-interacting-factor], a
            nuclear putatively antiapoptotic factor, interacts specifically
            with FGF-2
  JOURNAL   Mol Endocrinol 14 (11), 1709-1724 (2000)
   PUBMED   11075807
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Kim,J.W., Cho,H.S., Kim,J.H., Hur,S.Y., Kim,T.E., Lee,J.M.,
            Kim,I.K. and Namkoong,S.E.
  TITLE     AAC-11 overexpression induces invasion and protects cervical cancer
            cells from apoptosis
  JOURNAL   Lab Invest 80 (4), 587-594 (2000)
   PUBMED   10780674
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Gianfrancesco,F., Esposito,T., Ciccodicola,A., D'Esposito,M.,
            Mazzarella,R., D'Urso,M. and Forabosco,A.
  TITLE     Molecular cloning and fine mapping of API5L1, a novel human gene
            strongly related to an antiapoptotic gene
  JOURNAL   Cytogenet Cell Genet 84 (3-4), 164-166 (1999)
   PUBMED   10393420
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Tewari,M., Yu,M., Ross,B., Dean,C., Giordano,A. and Rubin,R.
  TITLE     AAC-11, a novel cDNA that inhibits apoptosis after growth factor
            withdrawal
  JOURNAL   Cancer Res 57 (18), 4063-4069 (1997)
   PUBMED   9307294
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087276.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an apoptosis inhibitory protein whose
            expression prevents apoptosis after growth factor deprivation. This
            protein suppresses the transcription factor E2F1-induced apoptosis
            and also interacts with, and negatively regulates Acinus, a nuclear
            factor involved in apoptotic DNA fragmentation. Its depletion
            enhances the cytotoxic action of the chemotherapeutic drugs.
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Aug
            2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.57111.1,
                                           SRR1803615.23605.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000531273.6/ ENSP00000431391.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p12"
     Protein         1..524
                     /product="apoptosis inhibitor 5 isoform a"
                     /note="fibroblast growth factor 2-interacting factor 2;
                     migration-inducing protein MIG8; FIF; antiapoptosis clone
                     11 protein; cell migration-inducing gene 8 protein"
                     /calculated_mol_wt=58874
     Region          2..360
                     /region_name="ARM-like and Heat-like helical repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZZ5.3)"
     Region          4..497
                     /region_name="API5"
                     /note="Apoptosis inhibitory protein 5 (API5); pfam05918"
                     /db_xref="CDD:428672"
     Region          63..91
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          97..139
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            251
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:22334682; propagated from
                     UniProtKB/Swiss-Prot (Q9BZZ5.3)"
     Region          370..391
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZZ5.3)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BZZ5.3)"
     Region          452..524
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZZ5.3)"
     Region          454..475
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:22334682"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZZ5.3)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BZZ5.3)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BZZ5.3)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35841; propagated from
                     UniProtKB/Swiss-Prot (Q9BZZ5.3)"
     Site            500
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9BZZ5.3)"
     CDS             1..524
                     /gene="API5"
                     /gene_synonym="AAC-11; AAC11"
                     /coded_by="NM_001142930.2:133..1707"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44572.1"
                     /db_xref="GeneID:8539"
                     /db_xref="HGNC:HGNC:594"
                     /db_xref="MIM:609774"
ORIGIN      
        1 mptveelyrn ygiladateq vgqhkdayqv ildgvkggtk ekrlaaqfip kffkhfpela
       61 dsainaqldl cededvsirr qaikelpqfa tgenlprvad iltqllqtdd saefnlvnna
      121 llsifkmdak gtlgglfsqi lqgedivrer aikflstklk tlpdevltke veeliltesk
      181 kvledvtgee fvlfmkilsg lkslqtvsgr qqlvelvaeq adleqtfnps dpdcvdrllq
      241 ctrqavplfs knvhstrfvt yfceqvlpnl gtlttpvegl diqlevlkll aemssfcgdm
      301 ekletnlrkl fdklleympl ppeeaengen agneepklqf syvecllysf hqlgrklpdf
      361 ltaklnaekl kdfkirlqyf arglqvyirq lrlalqgktg ealkteenki kvvalkitnn
      421 invlikdlfh ippsykstvt lswkpvqkve igqkrasedt tsgsppkkss agpkrdarqi
      481 ynppsgkyss nlgnfnyeqr gafrgsrggr gwgtrgnrsr grly
//
LOCUS       NP_115853                243 aa            linear   PRI 27-APR-2025
DEFINITION  linker for activation of T-cells family member 2 [Homo sapiens].
ACCESSION   NP_115853 NP_071323
VERSION     NP_115853.2
DBSOURCE    REFSEQ: accession NM_032464.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Crocco,P., Dato,S., La Grotta,R., Passarino,G. and Rose,G.
  TITLE     Evidence for a relationship between genetic polymorphisms of the
            L-DOPA transporter LAT2/4F2hc and risk of hypertension in the
            context of chronic kidney disease
  JOURNAL   BMC Med Genomics 17 (1), 163 (2024)
   PUBMED   38890684
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Narbona-Sanchez,I., Perez-Linaza,A., Serrano-Garcia,I.,
            Vico-Barranco,I., Fernandez-Aguilar,L.M., Poveda-Diaz,J.L., Sanchez
            Del Pino,M.J., Medina-Varo,F., Arbulo-Echevarria,M.M. and Aguado,E.
  TITLE     Expression of Non-T Cell Activation Linker (NTAL) in Jurkat Cells
            Negatively Regulates TCR Signaling: Potential Role in Rheumatoid
            Arthritis
  JOURNAL   Int J Mol Sci 24 (5), 4574 (2023)
   PUBMED   36902005
  REMARK    GeneRIF: Expression of Non-T Cell Activation Linker (NTAL) in
            Jurkat Cells Negatively Regulates TCR Signaling: Potential Role in
            Rheumatoid Arthritis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Zaugg,J., Huang,X., Ziegler,F., Rubin,M., Graff,J., Muller,J.,
            Moser-Hassig,R., Powell,T., Gertsch,J., Altmann,K.H. and
            Albrecht,C.
  TITLE     Small molecule inhibitors provide insights into the relevance of
            LAT1 and LAT2 in materno-foetal amino acid transport
  JOURNAL   J Cell Mol Med 24 (21), 12681-12693 (2020)
   PUBMED   33001560
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Kantipudi,S., Jeckelmann,J.M., Ucurum,Z., Bosshart,P.D. and
            Fotiadis,D.
  TITLE     The Heavy Chain 4F2hc Modulates the Substrate Affinity and
            Specificity of the Light Chains LAT1 and LAT2
  JOURNAL   Int J Mol Sci 21 (20), 7573 (2020)
   PUBMED   33066406
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Thome,C.H., Ferreira,G.A., Pereira-Martins,D.A., Dos Santos,G.A.,
            Ortiz,C.A., de Souza,L.E.B., Sobral,L.M., Silva,C.L.A.,
            Scheucher,P.S., Gil,C.D., Leopoldino,A.M., Silveira,D.R.A.,
            Coelho-Silva,J.L., Traina,F., Koury,L.C., Melo,R.A.M.,
            Bittencourt,R., Pagnano,K., Pasquini,R., Nunes,E.C., Fagundes,E.M.,
            Gloria,A.B.F., Kerbauy,F.R., Chauffaille,M.L., Keating,A.,
            Tallman,M.S., Ribeiro,R.C., Dillon,R., Ganser,A., Lowenberg,B.,
            Valk,P., Lo-Coco,F., Sanz,M.A., Berliner,N., Faca,V.M. and
            Rego,E.M.
  TITLE     NTAL is associated with treatment outcome, cell proliferation and
            differentiation in acute promyelocytic leukemia
  JOURNAL   Sci Rep 10 (1), 10315 (2020)
   PUBMED   32587277
  REMARK    GeneRIF: NTAL is associated with treatment outcome, cell
            proliferation and differentiation in acute promyelocytic leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Brdicka,T., Imrich,M., Angelisova,P., Brdickova,N., Horvath,O.,
            Spicka,J., Hilgert,I., Luskova,P., Draber,P., Novak,P., Engels,N.,
            Wienands,J., Simeoni,L., Osterreicher,J., Aguado,E., Malissen,M.,
            Schraven,B. and Horejsi,V.
  TITLE     Non-T cell activation linker (NTAL): a transmembrane adaptor
            protein involved in immunoreceptor signaling
  JOURNAL   J Exp Med 196 (12), 1617-1626 (2002)
   PUBMED   12486104
  REMARK    GeneRIF: data show that NTAL (non-T cell activation linker) appears
            to be a structural and possibly also functional homologue of LAT
            (linker for activation of T cells)in non-T cells [non-T cell
            activation linker]
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Martindale,D.W., Wilson,M.D., Wang,D., Burke,R.D., Chen,X.,
            Duronio,V. and Koop,B.F.
  TITLE     Comparative genomic sequence analysis of the Williams syndrome
            region (LIMK1-RFC2) of human chromosome 7q11.23
  JOURNAL   Mamm Genome 11 (10), 890-898 (2000)
   PUBMED   11003705
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Doyle,J.L., DeSilva,U., Miller,W. and Green,E.D.
  TITLE     Divergent human and mouse orthologs of a novel gene
            (WBSCR15/Wbscr15) reside within the genomic interval commonly
            deleted in Williams syndrome
  JOURNAL   Cytogenet Cell Genet 90 (3-4), 285-290 (2000)
   PUBMED   11124535
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Perez Jurado,L.A., Peoples,R., Kaplan,P., Hamel,B.C. and Francke,U.
  TITLE     Molecular definition of the chromosome 7 deletion in Williams
            syndrome and parent-of-origin effects on growth
  JOURNAL   Am J Hum Genet 59 (4), 781-792 (1996)
   PUBMED   8808592
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Osborne,L.R., Martindale,D., Scherer,S.W., Shi,X.M., Huizenga,J.,
            Heng,H.H., Costa,T., Pober,B., Lew,L., Brinkman,J., Rommens,J.,
            Koop,B. and Tsui,L.C.
  TITLE     Identification of genes from a 500-kb region at 7q11.23 that is
            commonly deleted in Williams syndrome patients
  JOURNAL   Genomics 36 (2), 328-336 (1996)
   PUBMED   8812460
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM468969.1, BC001609.1 and
            AI492348.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Dec 4, 2006 this sequence version replaced
            NP_071323.1, NP_115853.1.
            
            Summary: This gene is one of the contiguous genes at 7q11.23
            commonly deleted in Williams syndrome, a multisystem developmental
            disorder. This gene consists of at least 14 exons, and its
            alternative splicing generates 3 transcript variants, all encoding
            the same protein. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All three variants encode the same protein.
            
            CCDS Note: The coding region has been updated to represent an
            alternate splice pattern, resulting in an alternate and longer
            C-terminus that is better supported by available transcript and
            conservation data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF252611.1, SRR3476690.44670.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000460943.6/ ENSP00000420494.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..243
                     /product="linker for activation of T-cells family member
                     2"
                     /note="Williams-Beuren syndrome chromosomal region 5
                     protein; Williams-Beuren syndrome chromosomal region 15
                     protein; non-T-cell activation linker; linker for
                     activation of B-cells; membrane-associated adapter
                     molecule; linker for activation of T cells, transmembrane
                     adaptor 2"
                     /calculated_mol_wt=26419
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZY6.1)"
     Region          28..238
                     /region_name="LAT2"
                     /note="Linker for activation of T-cells family member 2;
                     pfam15703"
                     /db_xref="CDD:464812"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q9GZY6.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHL0; propagated from
                     UniProtKB/Swiss-Prot (Q9GZY6.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHL0; propagated from
                     UniProtKB/Swiss-Prot (Q9GZY6.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHL0; propagated from
                     UniProtKB/Swiss-Prot (Q9GZY6.1)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:12486104,
                     ECO:0000305|PubMed:14722116; propagated from
                     UniProtKB/Swiss-Prot (Q9GZY6.1)"
     Region          174..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZY6.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:12486104,
                     ECO:0000305|PubMed:14722116; propagated from
                     UniProtKB/Swiss-Prot (Q9GZY6.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:12486104,
                     ECO:0000269|PubMed:14722116; propagated from
                     UniProtKB/Swiss-Prot (Q9GZY6.1)"
     CDS             1..243
                     /gene="LAT2"
                     /gene_synonym="HSPC046; LAB; NTAL; WBSCR15; WBSCR5; WSCR5"
                     /coded_by="NM_032464.3:302..1033"
                     /db_xref="CCDS:CCDS5566.2"
                     /db_xref="GeneID:7462"
                     /db_xref="HGNC:HGNC:12749"
                     /db_xref="MIM:605719"
ORIGIN      
        1 mssgtellwp gaallvllgv aaslcvrcsr pgakrsekiy qqrslredqq sftgsrtysl
       61 vgqawpgpla dmaptrkdkl lqfypsledp assryqnfsk gsrhgseeay idpiameyyn
      121 wgrfskpped ddansyenvl ickqkttetg aqqegigglc rgdlslslal ktgptsglcp
      181 saspeedees edyqnsasih qwresrkvmg qlqreaspgp vgspdeedge pdyvngevaa
      241 tea
//
LOCUS       NP_073617                391 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein transferase RMND5A [Homo sapiens].
ACCESSION   NP_073617
VERSION     NP_073617.1
DBSOURCE    REFSEQ: accession NM_022780.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Gottemukkala,K.V., Chrustowicz,J., Sherpa,D., Sepic,S., Vu,D.T.,
            Karayel,O., Papadopoulou,E.C., Gross,A., Schorpp,K., von Gronau,S.,
            Hadian,K., Murray,P.J., Mann,M., Schulman,B.A. and Alpi,A.F.
  TITLE     Non-canonical substrate recognition by the human WDR26-CTLH E3
            ligase regulates prodrug metabolism
  JOURNAL   Mol Cell 84 (10), 1948-1963 (2024)
   PUBMED   38759627
  REMARK    GeneRIF: Non-canonical substrate recognition by the human
            WDR26-CTLH E3 ligase regulates prodrug metabolism.
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Deng,X., Ma,J., Zhou,W., Yuan,Y., Wang,B. and Meng,X.
  TITLE     GID2 Interacts With CDKN3 and Regulates Pancreatic Cancer Growth
            and Apoptosis
  JOURNAL   Lab Invest 103 (6), 100122 (2023)
   PUBMED   36828188
  REMARK    GeneRIF: GID2 Interacts With CDKN3 and Regulates Pancreatic Cancer
            Growth and Apoptosis.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Li,J., Chen,Y., Qin,X., Wen,J., Ding,H., Xia,W., Li,S., Su,X.,
            Wang,W., Li,H., Zhao,Q., Fang,T., Qu,L. and Shao,N.
  TITLE     MiR-138 downregulates miRNA processing in HeLa cells by targeting
            RMND5A and decreasing Exportin-5 stability
  JOURNAL   Nucleic Acids Res 42 (1), 458-474 (2014)
   PUBMED   24057215
  REMARK    GeneRIF: The study identifies a miR-138-RMND5A-Exportin-5 as a
            previously unknown miRNA processing regulatory pathway in HeLa
            cells.
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Vogel,T.W., Manjila,S. and Cohen,A.R.
  TITLE     Novel neurodevelopmental disorder in the case of a giant
            occipitoparietal meningoencephalocele
  JOURNAL   J Neurosurg Pediatr 10 (1), 25-29 (2012)
   PUBMED   22681319
  REMARK    GeneRIF: Duplications of this region involving RMND5A, whose
            product contains a C-terminal to lis homology (LisH) domain, have
            not previously been associated with a defined phenotype but may
            present insight into encephalocele formation.
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Kobayashi,N., Yang,J., Ueda,A., Suzuki,T., Tomaru,K., Takeno,M.,
            Okuda,K. and Ishigatsubo,Y.
  TITLE     RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat
            proteins ARMC8alpha and ARMC8beta are components of the CTLH
            complex
  JOURNAL   Gene 396 (2), 236-247 (2007)
   PUBMED   17467196
  REMARK    GeneRIF: RanBPM, ARMC8alpha, ARMC8beta, Muskelin, p48EMLP, and
            p44CTLH form complexes in cells.
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Bowzard,J.B., Cheng,D., Peng,J. and Kahn,R.A.
  TITLE     ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs
  JOURNAL   J Biol Chem 282 (24), 17568-17580 (2007)
   PUBMED   17452337
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK023972.1, BC047668.1, BC012165.1, AC064848.5 and BU620245.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.90910.1,
                                           SRR1660805.158266.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283632.5/ ENSP00000283632.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..391
                     /product="E3 ubiquitin-protein transferase RMND5A"
                     /EC_number="2.3.2.27"
                     /note="C-terminal to LisH motif, 44 kDa; protein RMD5
                     homolog A; GID complex subunit 2 homolog A; 44-kD protein
                     coding for CTLH motif"
                     /calculated_mol_wt=43862
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H871.1)"
     Region          17..391
                     /region_name="COG5109"
                     /note="Uncharacterized conserved protein, contains RING
                     Zn-finger [General function prediction only]"
                     /db_xref="CDD:227440"
     Region          153..297
                     /region_name="CTLH"
                     /note="CTLH/CRA C-terminal to LisH motif domain;
                     pfam10607"
                     /db_xref="CDD:402305"
     CDS             1..391
                     /gene="RMND5A"
                     /gene_synonym="CTLH; GID2; GID2A; p44CTLH; RMD5"
                     /coded_by="NM_022780.4:378..1553"
                     /db_xref="CCDS:CCDS1991.1"
                     /db_xref="GeneID:64795"
                     /db_xref="HGNC:HGNC:25850"
                     /db_xref="MIM:618964"
ORIGIN      
        1 mdqcvtvere lekvlhkfsg ygqlcergle elidytgglk heilqshgqd aelsgtlslv
       61 ltqcckrikd tvqklasdhk dihssvsrvg kaidknfdsd issvgidgcw qadsqrllne
      121 vmvehffrqg mldvaeelcq esglsvdpsq kepfvelnri lealkvrvlr palewavsnr
      181 emliaqnssl efklhrlyfi sllmggttnq realqyaknf qpfalnhqkd iqvlmgslvy
      241 lrqgienspy vhlldanqwa dicdiftrda callglsves plsvsfsagc valpalinik
      301 avieqrqctg vwnqkdelpi evdlgkkcwy hsifacpilr qqttdnnppm klvcghiisr
      361 dalnkmfngs klkcpycpme qspgdakqif f
//
LOCUS       NP_115787                148 aa            linear   PRI 27-APR-2025
DEFINITION  augurin precursor [Homo sapiens].
ACCESSION   NP_115787
VERSION     NP_115787.1
DBSOURCE    REFSEQ: accession NM_032411.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Xie,Z., Li,W., Ai,J., Xie,J. and Zhang,X.
  TITLE     C2orf40 inhibits metastasis and regulates chemo-resistance and
            radio-resistance of nasopharyngeal carcinoma cells by influencing
            cell cycle and activating the PI3K/AKT/mTOR signaling pathway
  JOURNAL   J Transl Med 20 (1), 264 (2022)
   PUBMED   35676661
  REMARK    GeneRIF: C2orf40 inhibits metastasis and regulates chemo-resistance
            and radio-resistance of nasopharyngeal carcinoma cells by
            influencing cell cycle and activating the PI3K/AKT/mTOR signaling
            pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Huo,H., Yang,S., Wu,H., Sun,Y., Zhao,R., Ye,R., Yan,D., Shi,X. and
            Yang,J.
  TITLE     Brain endothelial cells-derived extracellular vesicles
            overexpressing ECRG4 inhibit glioma proliferation through
            suppressing inflammation and angiogenesis
  JOURNAL   J Tissue Eng Regen Med 15 (12), 1162-1171 (2021)
   PUBMED   34551201
  REMARK    GeneRIF: Brain endothelial cells-derived extracellular vesicles
            overexpressing ECRG4 inhibit glioma proliferation through
            suppressing inflammation and angiogenesis.
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Chen,L., Tang,H., Liu,G., Xiao,S., Liang,D., Ma,J., Yang,Y.,
            Luo,H., Zhu,Y., Xie,F., Cheng,X., Chi,J. and Wu,X.
  TITLE     MicroRNA-196b promotes gastric cancer progression by targeting
            ECRG4
  JOURNAL   Anticancer Drugs 32 (2), 127-137 (2021)
   PUBMED   33417325
  REMARK    GeneRIF: MicroRNA-196b promotes gastric cancer progression by
            targeting ECRG4.
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Li,L.W., Yu,X.Y., Yang,Y., Zhang,C.P., Guo,L.P. and Lu,S.H.
  TITLE     Expression of esophageal cancer related gene 4 (ECRG4), a novel
            tumor suppressor gene, in esophageal cancer and its inhibitory
            effect on the tumor growth in vitro and in vivo
  JOURNAL   Int J Cancer 125 (7), 1505-1513 (2009)
   PUBMED   19521989
  REMARK    GeneRIF: The restoration of ECRG4 expression in ESCC cells
            inhibited cell proliferation, colony formation, cell cycle
            progression and tumor growth in vivo. ECRG4 is a novel candidate
            tumor suppressor gene in ESCC.
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Mori,Y., Ishiguro,H., Kuwabara,Y., Kimura,M., Mitsui,A.,
            Kurehara,H., Mori,R., Tomoda,K., Ogawa,R., Katada,T., Harata,K. and
            Fujii,Y.
  TITLE     Expression of ECRG4 is an independent prognostic factor for poor
            survival in patients with esophageal squamous cell carcinoma
  JOURNAL   Oncol Rep 18 (4), 981-985 (2007)
   PUBMED   17786363
  REMARK    GeneRIF: Significantly lower expression of esophageal
            cancer-related gene 4 is associated with esophageal squamous cell
            carcinoma
REFERENCE   8  (residues 1 to 148)
  AUTHORS   Mirabeau,O., Perlas,E., Severini,C., Audero,E., Gascuel,O.,
            Possenti,R., Birney,E., Rosenthal,N. and Gross,C.
  TITLE     Identification of novel peptide hormones in the human proteome by
            hidden Markov model screening
  JOURNAL   Genome Res 17 (3), 320-327 (2007)
   PUBMED   17284679
REFERENCE   9  (residues 1 to 148)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 148)
  AUTHORS   Yue,C.M., Deng,D.J., Bi,M.X., Guo,L.P. and Lu,S.H.
  TITLE     Expression of ECRG4, a novel esophageal cancer-related gene,
            downregulated by CpG island hypermethylation in human esophageal
            squamous cell carcinoma
  JOURNAL   World J Gastroenterol 9 (6), 1174-1178 (2003)
   PUBMED   12800218
  REMARK    GeneRIF: Inactivation of ECRG 4 gene by hypermethylation is a
            frequent molecular event in esophageal squamous cell carcinoma and
            may be involved in the carcinogenesis of this cancer.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF325503.1 and BC021742.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021742.1, ERR279855.2782.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000238044.8/ ENSP00000238044.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.2"
     Protein         1..148
                     /product="augurin precursor"
                     /note="esophageal cancer related gene 4 protein; augurin"
                     /calculated_mol_wt=14211
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2991
     Region          32..148
                     /region_name="Augurin"
                     /note="Oesophageal cancer-related gene 4; pfam15187"
                     /db_xref="CDD:464552"
     mat_peptide     71..132
                     /product="Augurin. /id=PRO_0000250514"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1Z8.1)"
                     /calculated_mol_wt=7876
     CDS             1..148
                     /gene="ECRG4"
                     /gene_synonym="C2orf40"
                     /coded_by="NM_032411.3:78..524"
                     /db_xref="CCDS:CCDS2072.1"
                     /db_xref="GeneID:84417"
                     /db_xref="HGNC:HGNC:24642"
                     /db_xref="MIM:611752"
ORIGIN      
        1 maasparpav laltglalll llcwgpggis gnklklmlqk reapvptktk vavdenkake
       61 flgslkrqkr qlwdrtrpev qqwyqqflym gfdeakfedd itywlnrdrn gheyygdyyq
      121 rhydedsaig prspygfrhg asvnyddy
//
LOCUS       NP_001355205             106 aa            linear   ROD 27-APR-2025
DEFINITION  small membrane A-kinase anchor protein [Mus musculus].
ACCESSION   NP_001355205
VERSION     NP_001355205.1
DBSOURCE    REFSEQ: accession NM_001368276.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Shalom-Barak,T., Zhang,X., Chu,T., Timothy Schaiff,W., Reddy,J.K.,
            Xu,J., Sadovsky,Y. and Barak,Y.
  TITLE     Placental PPARgamma regulates spatiotemporally diverse genes and a
            unique metabolic network
  JOURNAL   Dev Biol 372 (1), 143-155 (2012)
   PUBMED   22967998
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Thiagarajan,R.D., Georgas,K.M., Rumballe,B.A., Lesieur,E.,
            Chiu,H.S., Taylor,D., Tang,D.T., Grimmond,S.M. and Little,M.H.
  TITLE     Identification of anchor genes during kidney development defines
            ontological relationships, molecular subcompartments and regulatory
            pathways
  JOURNAL   PLoS One 6 (2), e17286 (2011)
   PUBMED   21386911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Lin,Q., Donahue,S.L., Moore-Jarrett,T., Cao,S., Osipovich,A.B. and
            Ruley,H.E.
  TITLE     Mutagenesis of diploid mammalian genes by gene entrapment
  JOURNAL   Nucleic Acids Res 34 (20), e139 (2006)
   PUBMED   17062627
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC129337.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CN833581.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 26.99 cM"
     Protein         1..106
                     /product="small membrane A-kinase anchor protein"
                     /note="UPF0733 protein C2orf88 homolog; small membrane
                     AKAP"
                     /calculated_mol_wt=11795
     Region          1..100
                     /region_name="SmAKAP"
                     /note="Small membrane A-kinase anchor protein; pfam15127"
                     /db_xref="CDD:464517"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CPS8.1)"
     Region          62..85
                     /region_name="PKA-RI-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CPS8.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BSF0; propagated from
                     UniProtKB/Swiss-Prot (Q9CPS8.1)"
     CDS             1..106
                     /gene="1700019D03Rik"
                     /gene_synonym="2410136C24Rik; smAKAP"
                     /coded_by="NM_001368276.1:334..654"
                     /db_xref="CCDS:CCDS14949.1"
                     /db_xref="GeneID:67080"
                     /db_xref="MGI:MGI:1914330"
ORIGIN      
        1 mgcmksketf pfpttldidk lheseeafip ddssqyrtps pgeqqqvqev kklpepgavi
       61 galilefadr laseivedal qqwaceniqy ynipyieseg sdttin
//
LOCUS       NP_004307                236 aa            linear   PRI 27-APR-2025
DEFINITION  achaete-scute homolog 1 [Homo sapiens].
ACCESSION   NP_004307
VERSION     NP_004307.2
DBSOURCE    REFSEQ: accession NM_004316.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Zhang,H., Zong,R., Wu,H., Jiang,J., Liu,C. and Liu,S.
  TITLE     Transcription factor ASCL1 targets SLC6A13 to inhibit the
            progression of hepatocellular carcinoma via the
            glycine-inflammasome signaling
  JOURNAL   Biomol Biomed 24 (6), 1606-1619 (2024)
   PUBMED   38780447
  REMARK    GeneRIF: Transcription factor ASCL1 targets SLC6A13 to inhibit the
            progression of hepatocellular carcinoma via the
            glycine-inflammasome signaling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Malbos,M., Wakeling,E., Gautier,T., Boespflug-Tanguy,O., Busby,L.,
            Taylor-Miller,T., Dudoignon,B., Bokov,P., Govin,J., Grisval,M.,
            Rega,A., Mourot De Rougemont,M.G., Aubriot-Lorton,M.H.,
            Darmency,V., Bensignor,C., Houzel,A., Huet,F., Denomme-Pichon,A.S.,
            Delanne,J., Tran Mau-Them,F., Bruel,A.L., Safraou,H., Nambot,S.,
            Garde,A., Philippe,C., Duffourd,Y., Vitobello,A., Faivre,L. and
            Thauvin-Robinet,C.
  TITLE     Further description of two individuals with de novo p.(Glu127Lys)
            missense variant in the ASCL1 gene
  JOURNAL   Clin Genet 105 (5), 555-560 (2024)
   PUBMED   38287449
  REMARK    GeneRIF: Further description of two individuals with de novo
            p.(Glu127Lys) missense variant in the ASCL1 gene.
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Li,Y., Yang,X., Geng,C., Liu,Y., Tang,T., Zhang,L., Liu,F.,
            Zhang,M., Hao,J. and Ma,L.
  TITLE     Identification of molecular subtypes based on chromatin
            regulator-related genes and experimental verification of the role
            of ASCL1 in conferring chemotherapy resistance to breast cancer
  JOURNAL   Front Immunol 15, 1390261 (2024)
   PUBMED   38726001
  REMARK    GeneRIF: Identification of molecular subtypes based on chromatin
            regulator-related genes and experimental verification of the role
            of ASCL1 in conferring chemotherapy resistance to breast cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Wohlschlegel,J., Finkbeiner,C., Hoffer,D., Kierney,F., Prieve,A.,
            Murry,A.D., Haugan,A.K., Ortuno-Lizaran,I., Rieke,F., Golden,S.A.
            and Reh,T.A.
  TITLE     ASCL1 induces neurogenesis in human Muller glia
  JOURNAL   Stem Cell Reports 18 (12), 2400-2417 (2023)
   PUBMED   38039971
  REMARK    GeneRIF: ASCL1 induces neurogenesis in human Muller glia.
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Abashkin,D.A., Karpov,D.S., Kurishev,A.O., Marilovtseva,E.V. and
            Golimbet,V.E.
  TITLE     ASCL1 Is Involved in the Pathogenesis of Schizophrenia by
            Regulation of Genes Related to Cell Proliferation, Neuronal
            Signature Formation, and Neuroplasticity
  JOURNAL   Int J Mol Sci 24 (21), 15746 (2023)
   PUBMED   37958729
  REMARK    GeneRIF: ASCL1 Is Involved in the Pathogenesis of Schizophrenia by
            Regulation of Genes Related to Cell Proliferation, Neuronal
            Signature Formation, and Neuroplasticity.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Chen,H., Biel,M.A., Borges,M.W., Thiagalingam,A., Nelkin,B.D.,
            Baylin,S.B. and Ball,D.W.
  TITLE     Tissue-specific expression of human achaete-scute homologue-1 in
            neuroendocrine tumors: transcriptional regulation by dual
            inhibitory regions
  JOURNAL   Cell Growth Differ 8 (6), 677-686 (1997)
   PUBMED   9186001
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Borges,M., Linnoila,R.I., van de Velde,H.J., Chen,H., Nelkin,B.D.,
            Mabry,M., Baylin,S.B. and Ball,D.W.
  TITLE     An achaete-scute homologue essential for neuroendocrine
            differentiation in the lung
  JOURNAL   Nature 386 (6627), 852-855 (1997)
   PUBMED   9126746
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Mao,Z. and Nadal-Ginard,B.
  TITLE     Functional and physical interactions between mammalian
            achaete-scute homolog 1 and myocyte enhancer factor 2A
  JOURNAL   J Biol Chem 271 (24), 14371-14375 (1996)
   PUBMED   8662987
REFERENCE   9  (residues 1 to 236)
  AUTHORS   Renault,B., Lieman,J., Ward,D., Krauter,K. and Kucherlapati,R.
  TITLE     Localization of the human achaete-scute homolog gene (ASCL1) distal
            to phenylalanine hydroxylase (PAH) and proximal to tumor rejection
            antigen (TRA1) on chromosome 12q22-q23
  JOURNAL   Genomics 30 (1), 81-83 (1995)
   PUBMED   8595908
REFERENCE   10 (residues 1 to 236)
  AUTHORS   Ball,D.W., Azzoli,C.G., Baylin,S.B., Chi,D., Dou,S.,
            Donis-Keller,H., Cumaraswamy,A., Borges,M. and Nelkin,B.D.
  TITLE     Identification of a human achaete-scute homolog highly expressed in
            neuroendocrine tumors
  JOURNAL   Proc Natl Acad Sci U S A 90 (12), 5648-5652 (1993)
   PUBMED   8390674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA005289.1, BC004425.1,
            CF454566.1, AC026108.29 and AW071836.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 15, 2004 this sequence version replaced NP_004307.1.
            
            Summary: This gene encodes a member of the basic helix-loop-helix
            (BHLH) family of transcription factors. The protein activates
            transcription by binding to the E box (5'-CANNTG-3'). Dimerization
            with other BHLH proteins is required for efficient DNA binding.
            This protein plays a role in the neuronal commitment and
            differentiation and in the generation of olfactory and autonomic
            neurons. Mutations in this gene may contribute to the congenital
            central hypoventilation syndrome (CCHS) phenotype in rare cases.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001638.2, L08424.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000266744.4/ ENSP00000266744.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.2"
     Protein         1..236
                     /product="achaete-scute homolog 1"
                     /note="achaete scute protein; ASH-1; class A basic
                     helix-loop-helix protein 46; achaete-scute complex-like 1;
                     achaete-scute complex homolog 1"
                     /calculated_mol_wt=25323
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50553.2)"
     Region          42..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50553.2)"
     Region          115..185
                     /region_name="bHLH_TS_ASCL1_Mash1"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     achaete-scute-like protein 1 (ASCL-1) and similar
                     proteins; cd19742"
                     /db_xref="CDD:381585"
     Site            order(120,124,126..128,130,135,153..156)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381585"
     Site            order(133..134,137..138,140..141,157,160,164,166..167,171,
                     173..174)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381585"
     Site            156
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q02067; propagated from
                     UniProtKB/Swiss-Prot (P50553.2)"
     CDS             1..236
                     /gene="ASCL1"
                     /gene_synonym="ASH1; bHLHa46; HASH1; MASH1"
                     /coded_by="NM_004316.4:572..1282"
                     /db_xref="CCDS:CCDS31886.1"
                     /db_xref="GeneID:429"
                     /db_xref="HGNC:HGNC:738"
                     /db_xref="MIM:100790"
ORIGIN      
        1 messakmesg gagqqpqpqp qqpflppaac ffataaaaaa aaaaaaaqsa qqqqqqqqqq
       61 qqapqlrpaa dgqpsggghk sapkqvkrqr ssspelmrck rrlnfsgfgy slpqqqpaav
      121 arrnerernr vklvnlgfat lrehvpngaa nkkmskvetl rsaveyiral qqlldehdav
      181 saafqagvls ptispnysnd lnsmagspvs syssdegsyd plspeeqell dftnwf
//
LOCUS       NP_003112                262 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor Spi-B isoform 1 [Homo sapiens].
ACCESSION   NP_003112
VERSION     NP_003112.2
DBSOURCE    REFSEQ: accession NM_003121.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Ling,B., Ye,G., Qin,C., Liao,X., Yang,R., Su,L. and Qi,G.
  TITLE     IGSF10 inhibits the metastasis of lung adenocarcinoma via the
            Spi-B/Integrin-beta1 signaling pathway
  JOURNAL   J Biochem Mol Toxicol 38 (4), e23693 (2024)
   PUBMED   38622980
  REMARK    GeneRIF: IGSF10 inhibits the metastasis of lung adenocarcinoma via
            the Spi-B/Integrin-beta1 signaling pathway.
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Gu,W., Qi,G. and Chen,L.
  TITLE     SPIB Knockdown Inhibits the Immune Escape of Ovarian Cancer Cells
            by Reducing PD-L1 (CD274) Expression and Inactivating the JAK/STAT
            Pathway
  JOURNAL   Iran J Immunol 20 (3), 335-347 (2023)
   PUBMED   37452634
  REMARK    GeneRIF: SPIB Knockdown Inhibits the Immune Escape of Ovarian
            Cancer Cells by Reducing PD-L1 (CD274) Expression and Inactivating
            the JAK/STAT Pathway.
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Wu,F., Tian,F., Qin,C., Qin,X., Zeng,W., Liu,X., Chen,C. and Lin,Y.
  TITLE     Peroxiredoxin2 regulates trophoblast proliferation and migration
            through SPIB-HDAC2 pathway
  JOURNAL   Exp Cell Res 422 (1), 113428 (2023)
   PUBMED   36400181
  REMARK    GeneRIF: Peroxiredoxin2 regulates trophoblast proliferation and
            migration through SPIB-HDAC2 pathway.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Ding,M., Li,Q., Tan,X., Zhang,L., Tan,J. and Zheng,L.
  TITLE     Comprehensive pan-cancer analysis reveals the prognostic value and
            immunological role of SPIB
  JOURNAL   Aging (Albany NY) 14 (15), 6338-6357 (2022)
   PUBMED   35969172
  REMARK    GeneRIF: Comprehensive pan-cancer analysis reveals the prognostic
            value and immunological role of SPIB.
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Mohsin,M., Singh,P., Khan,S., Verma,A.K., Jha,R., Alsahli,M.A.,
            Rahmani,A.H., Almatroodi,S.A., Alrumaihi,F., Kaprwan,N., Dev,K.,
            Dohare,R. and Syed,M.A.
  TITLE     Integrated transcriptomic and regulatory network analyses uncovers
            the role of let-7b-5p, SPIB, and HLA-DPB1 in sepsis
  JOURNAL   Sci Rep 12 (1), 11963 (2022)
   PUBMED   35831411
  REMARK    GeneRIF: Integrated transcriptomic and regulatory network analyses
            uncovers the role of let-7b-5p, SPIB, and HLA-DPB1 in sepsis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Yamamoto,H., Kihara-Negishi,F., Yamada,T., Suzuki,M., Nakano,T. and
            Oikawa,T.
  TITLE     Interaction between the hematopoietic Ets transcription factor
            Spi-B and the coactivator CREB-binding protein associated with
            negative cross-talk with c-Myb
  JOURNAL   Cell Growth Differ 13 (2), 69-75 (2002)
   PUBMED   11864910
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Nagy,M., Chapuis,B. and Matthes,T.
  TITLE     Expression of transcription factors Pu.1, Spi-B, Blimp-1, BSAP and
            oct-2 in normal human plasma cells and in multiple myeloma cells
  JOURNAL   Br J Haematol 116 (2), 429-435 (2002)
   PUBMED   11841448
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Rao,S., Matsumura,A., Yoon,J. and Simon,M.C.
  TITLE     SPI-B activates transcription via a unique proline, serine, and
            threonine domain and exhibits DNA binding affinity differences from
            PU.1
  JOURNAL   J Biol Chem 274 (16), 11115-11124 (1999)
   PUBMED   10196196
REFERENCE   9  (residues 1 to 262)
  AUTHORS   Ray-Gallet,D., Tavitian,A. and Moreau-Gachelin,F.
  TITLE     An alternatively spliced isoform of the Spi-B transcription factor
  JOURNAL   Biochem Biophys Res Commun 223 (2), 257-263 (1996)
   PUBMED   8670269
REFERENCE   10 (residues 1 to 262)
  AUTHORS   Ray,D., Bosselut,R., Ghysdael,J., Mattei,M.G., Tavitian,A. and
            Moreau-Gachelin,F.
  TITLE     Characterization of Spi-B, a transcription factor related to the
            putative oncoprotein Spi-1/PU.1
  JOURNAL   Mol Cell Biol 12 (10), 4297-4304 (1992)
   PUBMED   1406622
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020909.9.
            
            On Mar 26, 2005 this sequence version replaced NP_003112.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            activator that binds to the PU-box (5'-GAGGAA-3') and acts as a
            lymphoid-specific enhancer. Four transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225720.1, AK225225.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000595883.6/ ENSP00000471921.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..262
                     /product="transcription factor Spi-B isoform 1"
                     /note="transcription factor Spi-B; Spi-B transcription
                     factor (Spi-1/PU.1 related)"
                     /calculated_mol_wt=28687
     Region          1..31
                     /region_name="TAD1 (Acidic).
                     /evidence=ECO:0000269|PubMed:10196196"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01892.1)"
     Region          41..61
                     /region_name="TAD2. /evidence=ECO:0000269|PubMed:10196196"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01892.1)"
     Region          140..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01892.1)"
     Region          168..256
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..262
                     /gene="SPIB"
                     /gene_synonym="SPI-B"
                     /coded_by="NM_003121.5:26..814"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33080.1"
                     /db_xref="GeneID:6689"
                     /db_xref="HGNC:HGNC:11242"
                     /db_xref="MIM:606802"
ORIGIN      
        1 mlaleaaqld gphfsclypd gvfydldsck hssypdsega pdslwdwtva ppvpatpyea
       61 fdpaaaafsh pqaaqlcyep ptyspagnle lapsleapgp glpayptenf asqtlvppay
      121 apypspvlse eedlpldspa levsdsesde alvagpegkg seagtrkklr lyqfllgllt
      181 rgdmrecvww vepgagvfqf sskhkellar rwgqqkgnrk rmtyqklara lrnyaktgei
      241 rkvkrkltyq fdsallpavr ra
//
LOCUS       NP_001350794             893 aa            linear   PRI 27-APR-2025
DEFINITION  disks large homolog 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001350794 XP_016861298
VERSION     NP_001350794.1
DBSOURCE    REFSEQ: accession NM_001363865.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Veljacic Viskovic,D., Lozic,M., Vukoja,M., Soljic,V., Vukojevic,K.,
            Glavina Durdov,M., Filipovic,N. and Lozic,B.
  TITLE     Spatio-Temporal Expression Pattern of CAKUT Candidate Genes DLG1
            and KIF12 during Human Kidney Development
  JOURNAL   Biomolecules 13 (2), 340 (2023)
   PUBMED   36830709
  REMARK    GeneRIF: Spatio-Temporal Expression Pattern of CAKUT Candidate
            Genes DLG1 and KIF12 during Human Kidney Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 893)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Jun 3, 2018 this sequence version replaced XP_016861298.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.24389.1,
                                           SRR14372079.332688.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..893
                     /product="disks large homolog 1 isoform 6"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=99811
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          702..880
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..893
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001363865.1:227..2908"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS87192.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgqsfnd krkknlfsrk fpfyknkdqs
      661 eqetsdadqh vtsnasdses syrgqeeyvl syepvnqqev nytrpviilg pmkdrinddl
      721 isefpdkfgs cvphttrpkr dyevdgrdyh fvtsreqmek diqehkfiea gqynnhlygt
      781 svqsvrevae kgkhcildvs gnaikrlqia qlypisifik pksmenimem nkrlteeqar
      841 ktferamkle qeftehftai vqgdtlediy nqvkqiieeq sgsyiwvpak ekl
//
LOCUS       NP_057407               1024 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ISG15--protein ligase HERC5 [Homo sapiens].
ACCESSION   NP_057407
VERSION     NP_057407.2
DBSOURCE    REFSEQ: accession NM_016323.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Schneegans,S., Loptien,J., Mojzisch,A., Loreth,D., Kretz,O.,
            Raschdorf,C., Hanssen,A., Gocke,A., Siebels,B., Gunasekaran,K.,
            Ding,Y., Oliveira-Ferrer,L., Brylka,L., Schinke,T., Schluter,H.,
            Paatero,I., Voss,H., Werner,S., Pantel,K. and Wikman,H.
  TITLE     HERC5 downregulation in non-small cell lung cancer is associated
            with altered energy metabolism and metastasis
  JOURNAL   J Exp Clin Cancer Res 43 (1), 110 (2024)
   PUBMED   38605423
  REMARK    GeneRIF: HERC5 downregulation in non-small cell lung cancer is
            associated with altered energy metabolism and metastasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Qin,Y., Meng,X., Wang,M., Liang,W., Xu,R., Chen,J., Song,H., Fu,Y.,
            Li,J., Gao,C., Jia,M., Zhao,C. and Zhao,W.
  TITLE     Posttranslational ISGylation of NLRP3 by HERC enzymes facilitates
            inflammasome activation in models of inflammation
  JOURNAL   J Clin Invest 133 (20), e161935 (2023)
   PUBMED   37651190
  REMARK    GeneRIF: Posttranslational ISGylation of NLRP3 by HERC enzymes
            facilitates inflammasome activation in models of inflammation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Du,X., Sheng,J., Chen,Y., He,S., Yang,Y., Huang,Y., Fu,Y., Lie,L.,
            Han,Z., Zhu,B., Liu,H., Wen,Q., Zhou,X., Zhou,C., Hu,S. and Ma,L.
  TITLE     The E3 ligase HERC5 promotes antimycobacterial responses in
            macrophages by ISGylating the phosphatase PTEN
  JOURNAL   Sci Signal 16 (788), eabm1756 (2023)
   PUBMED   37279284
  REMARK    GeneRIF: The E3 ligase HERC5 promotes antimycobacterial responses
            in macrophages by ISGylating the phosphatase PTEN.
REFERENCE   4  (residues 1 to 1024)
  AUTHORS   Liu,C., Li,L., Hou,G., Lu,Y., Gao,M. and Zhang,L.
  TITLE     HERC5/IFI16/p53 signaling mediates breast cancer cell proliferation
            and migration
  JOURNAL   Life Sci 303, 120692 (2022)
   PUBMED   35671810
  REMARK    GeneRIF: HERC5/IFI16/p53 signaling mediates breast cancer cell
            proliferation and migration.
REFERENCE   5  (residues 1 to 1024)
  AUTHORS   Bawono,R.G., Abe,T., Qu,M., Kuroki,D., Deng,L., Matsui,C., Ryo,A.,
            Suzuki,T., Matsuura,Y., Sugiyama,M., Mizokami,M., Shimotohno,K. and
            Shoji,I.
  TITLE     HERC5 E3 ligase mediates ISGylation of hepatitis B virus X protein
            to promote viral replication
  JOURNAL   J Gen Virol 102 (10) (2021)
   PUBMED   34661519
  REMARK    GeneRIF: HERC5 E3 ligase mediates ISGylation of hepatitis B virus X
            protein to promote viral replication.
REFERENCE   6  (residues 1 to 1024)
  AUTHORS   Wong,J.J., Pung,Y.F., Sze,N.S. and Chin,K.C.
  TITLE     HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates
            type I IFN-induced ISGylation of protein targets
  JOURNAL   Proc Natl Acad Sci U S A 103 (28), 10735-10740 (2006)
   PUBMED   16815975
  REMARK    GeneRIF: HERC5/Ceb1 is involved in the conjugation of ISG15 to
            cellular proteins.
REFERENCE   7  (residues 1 to 1024)
  AUTHORS   Dastur,A., Beaudenon,S., Kelley,M., Krug,R.M. and Huibregtse,J.M.
  TITLE     Herc5, an interferon-induced HECT E3 enzyme, is required for
            conjugation of ISG15 in human cells
  JOURNAL   J Biol Chem 281 (7), 4334-4338 (2006)
   PUBMED   16407192
REFERENCE   8  (residues 1 to 1024)
  AUTHORS   Hochrainer,K., Mayer,H., Baranyi,U., Binder,B., Lipp,J. and
            Kroismayr,R.
  TITLE     The human HERC family of ubiquitin ligases: novel members, genomic
            organization, expression profiling, and evolutionary aspects
  JOURNAL   Genomics 85 (2), 153-164 (2005)
   PUBMED   15676274
REFERENCE   9  (residues 1 to 1024)
  AUTHORS   Kroismayr,R., Baranyi,U., Stehlik,C., Dorfleutner,A., Binder,B.R.
            and Lipp,J.
  TITLE     HERC5, a HECT E3 ubiquitin ligase tightly regulated in LPS
            activated endothelial cells
  JOURNAL   J Cell Sci 117 (Pt 20), 4749-4756 (2004)
   PUBMED   15331633
  REMARK    GeneRIF: Data show that HERC5, a functionally active HECT ubiquitin
            ligase, exhibits a tightly controlled cytosolic level under
            inflammatory conditions in endothelial cells.
REFERENCE   10 (residues 1 to 1024)
  AUTHORS   Mitsui,K., Nakanishi,M., Ohtsuka,S., Norwood,T.H., Okabayashi,K.,
            Miyamoto,C., Tanaka,K., Yoshimura,A. and Ohtsubo,M.
  TITLE     A novel human gene encoding HECT domain and RCC1-like repeats
            interacts with cyclins and is potentially regulated by the tumor
            suppressor proteins
  JOURNAL   Biochem Biophys Res Commun 266 (1), 115-122 (1999)
   PUBMED   10581175
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY337518.1, BC140716.1,
            AK302142.1, AC083829.5 and AI336946.1.
            
            On Jul 28, 2006 this sequence version replaced NP_057407.1.
            
            Summary: This gene is a member of the HERC family of ubiquitin
            ligases and encodes a protein with a HECT domain and five RCC1
            repeats. Pro-inflammatory cytokines upregulate expression of this
            gene in endothelial cells. The protein localizes to the cytoplasm
            and perinuclear region and functions as an interferon-induced E3
            protein ligase that mediates ISGylation of protein targets. The
            protein also acts as a modulator of the antiviral immune response.
            The gene lies in a cluster of HERC family genes on chromosome 4.
            [provided by RefSeq, Aug 2021].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.122484.1, AY337518.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000264350.8/ ENSP00000264350.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.1"
     Protein         1..1024
                     /product="E3 ISG15--protein ligase HERC5"
                     /note="probable E3 ubiquitin-protein ligase HERC5; HECT
                     domain and RCC1-like domain-containing protein 5;
                     cyclin-E-binding protein 1; hect domain and RLD 5"
                     /calculated_mol_wt=116722
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UII4.2)"
     Region          96..155
                     /region_name="RCC1 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UII4.2)"
     Region          <140..346
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          156..208
                     /region_name="RCC1 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UII4.2)"
     Region          209..260
                     /region_name="RCC1 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UII4.2)"
     Region          262..312
                     /region_name="RCC1 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UII4.2)"
     Region          314..364
                     /region_name="RCC1 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UII4.2)"
     Region          681..1024
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(687,717,728,785,958,988..989,992..996,1016,1023)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(813,816..817,819..820,823,828,830,834..835,837,842,
                     847,864,868)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..1024
                     /gene="HERC5"
                     /gene_synonym="CEB1; CEBP1"
                     /coded_by="NM_016323.4:152..3226"
                     /db_xref="CCDS:CCDS3630.1"
                     /db_xref="GeneID:51191"
                     /db_xref="HGNC:HGNC:24368"
                     /db_xref="MIM:608242"
ORIGIN      
        1 merrsrrksr rngrstagka aatqpakspg aqlwlfpsaa glhrallrrv evtrqlccsp
       61 grlavlergg agvqvhqlla gsggartpkc iklgknmkih svdqgaehml ilssdgkpfe
      121 ydnysmkhlr fesilqekki iqitcgdyhs lalskggelf awgqnlhgql gvgrkfpstt
      181 tpqivehlag vplaqisage ahsmalsmsg niyswgknec gqlglghtes kddpsliegl
      241 dnqkvefvac ggshsalltq dgllftfgag khgqlghnst qnelrpclva elvgyrvtqi
      301 acgrwhtlay vsdlgkvfsf gsgkdgqlgn ggtrdqlmpl pvkvssseel kleshtseke
      361 limiaggnqs illwikkens yvnlkrtipt lnegtvkrwi advetkrwqs tkreiqeifs
      421 spacltgsfl rkrrttemmp vyldlnkarn ifkeltqkdw itnmittclk dnllkrlpfh
      481 sppqealeif fllpecpmmh isnnweslvv pfakvvckms dqsslvleey watlqestfs
      541 klvqmfktav icqldywdes aeengnvqal lemlkklhrv nqvkcqlpes ifqvdellhr
      601 lnffvevcrr ylwkmtvdas envqccvifs hfpfifnnls kikllhtdtl lkieskkhka
      661 ylrsaaieee resefalrpt fdltvrrnhl iedvlnqlsq fenedlrkel wvsfsgeigy
      721 dlggvkkeff yclfaemiqp eygmfmypeg ascmwfpvkp kfekkryfff gvlcglslfn
      781 cnvanlpfpl alfkklldqm psledlkels pdlgknlqtl lddegdnfee vfyihfnvhw
      841 drndtnlipn gssitvnqtn krdyvskyin yifndsvkav yeefrrgfyk mcdediiklf
      901 hpeelkdviv gntdydwktf eknaryepgy nsshptivmf wkafhkltle ekkkflvflt
      961 gtdrlqmkdl nnmkitfccp eswnerdpir altcfsvlfl pkystmetve ealqeainnn
     1021 rgfg
//
LOCUS       NP_071748                414 aa            linear   PRI 27-APR-2025
DEFINITION  tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
            isoform 1 [Homo sapiens].
ACCESSION   NP_071748
VERSION     NP_071748.2
DBSOURCE    REFSEQ: accession NM_022353.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Zhou,J.B., Wang,Y., Zeng,Q.Y., Meng,S.X., Wang,E.D. and Zhou,X.L.
  TITLE     Molecular basis for t6A modification in human mitochondria
  JOURNAL   Nucleic Acids Res 48 (6), 3181-3194 (2020)
   PUBMED   32047918
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Lin,H., Miyauchi,K., Harada,T., Okita,R., Takeshita,E., Komaki,H.,
            Fujioka,K., Yagasaki,H., Goto,Y.I., Yanaka,K., Nakagawa,S.,
            Sakaguchi,Y. and Suzuki,T.
  TITLE     CO2-sensitive tRNA modification associated with human mitochondrial
            disease
  JOURNAL   Nat Commun 9 (1), 1875 (2018)
   PUBMED   29760464
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Liao,M., Shi,J., Huang,L., Gao,Y., Tan,A., Wu,C., Lu,Z., Yang,X.,
            Zhang,S., Hu,Y., Qin,X., Li,J., Chen,G., Xu,J., Mo,Z. and Zhang,H.
  TITLE     Genome-wide association study identifies variants in PMS1
            associated with serum ferritin in a Chinese population
  JOURNAL   PLoS One 9 (8), e105844 (2014)
   PUBMED   25162662
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Oberto,J., Breuil,N., Hecker,A., Farina,F., Brochier-Armanet,C.,
            Culetto,E. and Forterre,P.
  TITLE     Qri7/OSGEPL, the mitochondrial version of the universal Kae1/YgjD
            protein, is essential for mitochondrial genome maintenance
  JOURNAL   Nucleic Acids Res 37 (16), 5343-5352 (2009)
   PUBMED   19578062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC013468.12 and BC011904.2.
            
            On Oct 28, 2006 this sequence version replaced NP_071748.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011904.2, SRR11853565.17331.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264151.10/ ENSP00000264151.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..414
                     /product="tRNA N6-adenosine threonylcarbamoyltransferase,
                     mitochondrial isoform 1"
                     /EC_number="2.3.1.234"
                     /note="putative sialoglycoprotease type 2; OSGEP-like
                     protein 1; probable O-sialoglycoprotein endopeptidase 2;
                     tRNA threonylcarbamoyladenosine biosynthesis protein
                     OSGEPL1; probable tRNA threonylcarbamoyladenosine
                     biosynthesis protein OSGEPL1; O-sialoglycoprotein
                     endopeptidase-like protein 1; tRNA N6-adenosine
                     threonylcarbamoyltransferase, mitochondrial; t(6)A37
                     threonylcarbamoyladenosine biosynthesis protein OSGEPL1;
                     probable tRNA N6-adenosine threonylcarbamoyltransferase,
                     mitochondrial; t(6)A synthase;
                     N6-L-threonylcarbamoyladenine synthase"
                     /calculated_mol_wt=41635
     transit_peptide 1..29
                     /note="Mitochondrion.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03179; propagated from
                     UniProtKB/Swiss-Prot (Q9H4B0.2)"
                     /calculated_mol_wt=3506
     mat_peptide     30..414
                     /product="tRNA N6-adenosine threonylcarbamoyltransferase,
                     mitochondrial. /id=PRO_0000307778"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4B0.2)"
                     /calculated_mol_wt=41635
     Region          39..373
                     /region_name="ASKHA_NBD_OSGEPL1_QRI7_euk"
                     /note="nucleotide-binding domain (NBD) of
                     O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1)
                     and similar proteins from eukayotes; cd24134"
                     /db_xref="CDD:466984"
     Site            74
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32047918; propagated from
                     UniProtKB/Swiss-Prot (Q9H4B0.2)"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32047918; propagated from
                     UniProtKB/Swiss-Prot (Q9H4B0.2)"
     Site            203
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32047918; propagated from
                     UniProtKB/Swiss-Prot (Q9H4B0.2)"
     Site            230
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32047918; propagated from
                     UniProtKB/Swiss-Prot (Q9H4B0.2)"
     Site            240
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32047918; propagated from
                     UniProtKB/Swiss-Prot (Q9H4B0.2)"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32047918; propagated from
                     UniProtKB/Swiss-Prot (Q9H4B0.2)"
     CDS             1..414
                     /gene="OSGEPL1"
                     /gene_synonym="OSGEPL; Qri7"
                     /coded_by="NM_022353.3:129..1373"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46472.1"
                     /db_xref="GeneID:64172"
                     /db_xref="HGNC:HGNC:23075"
                     /db_xref="MIM:619634"
ORIGIN      
        1 mliltktagv ffkpskrkvy eflrsfnfhp gtlflhkivl gietscddta aavvdetgnv
       61 lgeaihsqte vhlktggivp paaqqlhren iqrivqeals asgvspsdls aiattikpgl
      121 alslgvglsf slqlvgqlkk pfipihhmea haltirltnk vefpflvlli sgghcllalv
      181 qgvsdflllg ksldiapgdm ldkvarrlsl ikhpecstms ggkaiehlak qgnrfhfdik
      241 pplhhakncd fsftglqhvt dkiimkkeke egiekgqils saadiaatvq htmachlvkr
      301 thrailfckq rdllpqnnav lvasggvasn fyirraleil tnatqctllc ppprlctdng
      361 imiawngier lraglgilhd iegiryepkc plgvdiskev geasikvpql kmei
//
LOCUS       NP_055506               1485 aa            linear   PRI 27-APR-2025
DEFINITION  RNA helicase aquarius [Homo sapiens].
ACCESSION   NP_055506 XP_029045
VERSION     NP_055506.1
DBSOURCE    REFSEQ: accession NM_014691.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1485)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 1485)
  AUTHORS   Song,C., Yan,H., Wang,H., Zhang,Y., Cao,H., Wan,Y., Kong,L.,
            Chen,S., Xu,H., Pan,B., Zhang,J., Fan,G., Xin,H., Liang,Z., Jia,W.
            and Tian,X.L.
  TITLE     AQR is a novel type 2 diabetes-associated gene that regulates
            signaling pathways critical for glucose metabolism
  JOURNAL   J Genet Genomics 45 (2), 111-120 (2018)
   PUBMED   29502958
  REMARK    GeneRIF: Our study suggests that AQR is a novel type 2
            diabetes-associated gene that regulates signaling pathways critical
            for glucose metabolism.
REFERENCE   3  (residues 1 to 1485)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 1485)
  AUTHORS   Zhang,X., Yan,C., Hang,J., Finci,L.I., Lei,J. and Shi,Y.
  TITLE     An Atomic Structure of the Human Spliceosome
  JOURNAL   Cell 169 (5), 918-929 (2017)
   PUBMED   28502770
REFERENCE   5  (residues 1 to 1485)
  AUTHORS   Bertram,K., Agafonov,D.E., Liu,W.T., Dybkov,O., Will,C.L.,
            Hartmuth,K., Urlaub,H., Kastner,B., Stark,H. and Luhrmann,R.
  TITLE     Cryo-EM structure of a human spliceosome activated for step 2 of
            splicing
  JOURNAL   Nature 542 (7641), 318-323 (2017)
   PUBMED   28076346
REFERENCE   6  (residues 1 to 1485)
  AUTHORS   Silva,L.K., Blanton,R.E., Parrado,A.R., Melo,P.S., Morato,V.G.,
            Reis,E.A., Dias,J.P., Castro,J.M., Vasconcelos,P.F., Goddard,K.A.,
            Barreto,M.L., Reis,M.G. and Teixeira,M.G.
  TITLE     Dengue hemorrhagic fever is associated with polymorphisms in JAK1
  JOURNAL   Eur J Hum Genet 18 (11), 1221-1227 (2010)
   PUBMED   20588308
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1485)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 1485)
  AUTHORS   Hirose,T., Ideue,T., Nagai,M., Hagiwara,M., Shu,M.D. and
            Steitz,J.A.
  TITLE     A spliceosomal intron binding protein, IBP160, links
            position-dependent assembly of intron-encoded box C/D snoRNP to
            pre-mRNA splicing
  JOURNAL   Mol Cell 23 (5), 673-684 (2006)
   PUBMED   16949364
REFERENCE   9  (residues 1 to 1485)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 1485)
  AUTHORS   Sam,M., Wurst,W., Kluppel,M., Jin,O., Heng,H. and Bernstein,A.
  TITLE     Aquarius, a novel gene isolated by gene trapping with an
            RNA-dependent RNA polymerase motif
  JOURNAL   Dev Dyn 212 (2), 304-317 (1998)
   PUBMED   9626505
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018868.4.
            
            On Dec 18, 2003 this sequence version replaced XP_029045.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.51066.1,
                                           SRR1660807.30390.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000156471.10/ ENSP00000156471.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..1485
                     /product="RNA helicase aquarius"
                     /EC_number="3.6.4.13"
                     /note="functional spliceosome-associated protein 164;
                     intron-binding protein aquarius; intron-binding protein of
                     160 kDa; aquarius homolog"
                     /calculated_mol_wt=171165
     Region          1..416
                     /region_name="Helical region with structural similarity to
                     ARM repeat domains. /evidence=ECO:0000269|PubMed:25599396"
                     /note="propagated from UniProtKB/Swiss-Prot (O60306.4)"
     Region          18..802
                     /region_name="Aquarius_N"
                     /note="Intron-binding protein aquarius N-terminus;
                     pfam16399"
                     /db_xref="CDD:435319"
     Region          417..1485
                     /region_name="Required for assembly of the IB complex.
                     /evidence=ECO:0000269|PubMed:25599396"
                     /note="propagated from UniProtKB/Swiss-Prot (O60306.4)"
     Region          797..1152
                     /region_name="EEXXQc_AQR"
                     /note="EEXXQ-box helicase domain of AQR; cd17935"
                     /db_xref="CDD:350693"
     Site            order(800..803,806,825..831,861,1137..1138)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350693"
     Site            1051
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60306.4)"
     Region          1140..1323
                     /region_name="SF1_C_Upf1"
                     /note="C-terminal helicase domain of Upf1-like family
                     helicases; cd18808"
                     /db_xref="CDD:350195"
     Site            order(1229..1231,1259,1261..1262,1277)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350195"
     Site            order(1265,1267,1296)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350195"
     Region          1419..1485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60306.4)"
     CDS             1..1485
                     /gene="AQR"
                     /gene_synonym="fSAP164; IBP160"
                     /coded_by="NM_014691.3:130..4587"
                     /db_xref="CCDS:CCDS42013.1"
                     /db_xref="GeneID:9716"
                     /db_xref="HGNC:HGNC:29513"
                     /db_xref="MIM:610548"
ORIGIN      
        1 maapaqpkki vaptvsqina efvtqlacky waphikkksp fdikviediy ekeivksrfa
       61 irkimllefs qylenylwmn yspevsskay lmsiccmvne kfrenvpawe ifkkkpdhfp
      121 fffkhilkaa laetdgefsl heqtvlllfl dhcfnslevd lirsqvqqli slpmwmglql
      181 arlelelkkt pklrkfwnli kkndekmdpe areqayqerr flsqliqkfi svlksvplse
      241 pvtmdkvhyc erfielmidl eallptrrwf ntilddshll vhcylsnlvr reedghlfsq
      301 lldmlkfytg feindqtgna ltenemttih ydritslqra afahfpelyd falsnvaevd
      361 treslvkffg plssntlhqv asylcllptl pknedttfdk efllellvsr herrisqiqq
      421 lnqmplypte kiiwdenivp teyysgegcl alpklnlqfl tlhdyllrnf nlfrlestye
      481 irqdiedsvs rmkpwqseyg gvvfggwarm aqpivaftvv evakpnigen wptrvradvt
      541 inlnvrdhik deweglrkhd vcflitvrpt kpygtkfdrr rpfieqvglv yvrgceiqgm
      601 lddkgrvied gpeprpnlrg esrtfrvfld pnqyqqdmtn tiqngaedvy etfniimrrk
      661 pkennfkavl etirnlmntd cvvpdwlhdi ilgygdpssa hyskmpnqia tldfndtfls
      721 iehlkasfpg hnvkvtvedp alqippfrit fpvrsgkgkk rkdadveded teeaktlive
      781 phvipnrgpy pynqpkrnti qfthtqieai ragmqpgltm vvgppgtgkt dvavqiisni
      841 yhnfpeqrtl ivthsnqaln qlfekimald iderhllrlg hgeeeletek dfsrygrvny
      901 vlarrielle evkrlqkslg vpgdasytce tagyfflyqv msrweeyisk vknkgstlpd
      961 vtevstffpf heyfanapqp ifkgrsyeed meiaegcfrh ikkiftqlee frasellrsg
     1021 ldrskyllvk eakiiamtct haalkrhdlv klgfkydnil meeaaqilei etfiplllqn
     1081 pqdgfsrlkr wimigdhhql ppviknmafq kysnmeqslf trfvrvgvpt vdldaqgrar
     1141 aslcnlynwr yknlgnlphv qllpefstan agllydfqli nvedfqgvge sepnpyfyqn
     1201 lgeaeyvval fmymcllgyp adkisiltty ngqkhlirdi inrrcgnnpl igrpnkvttv
     1261 drfqgqqndy illslvrtra vghlrdvrrl vvamsrarlg lyifarvslf qncfeltpaf
     1321 sqltarplhl hiiptepfpt trkngerpsh evqiiknmpq manfvynmym hliqtthhyh
     1381 qtllqlppam veegeevqnq eteleteeea mtvqadiips ptdtscrqet pafqtdttps
     1441 etgatstpea ipalsettpt vvgavsapae antpqdatsa peetk
//
LOCUS       NP_115996                461 aa            linear   PRI 27-APR-2025
DEFINITION  cyclic AMP-responsive element-binding protein 3-like protein 3
            isoform a [Homo sapiens].
ACCESSION   NP_115996
VERSION     NP_115996.1
DBSOURCE    REFSEQ: accession NM_032607.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Kim,H., Song,Z., Zhang,R., Davies,B.S.J. and Zhang,K.
  TITLE     A hepatokine derived from the ER protein CREBH promotes
            triglyceride metabolism by stimulating lipoprotein lipase activity
  JOURNAL   Sci Signal 16 (768), eadd6702 (2023)
   PUBMED   36649378
  REMARK    GeneRIF: A hepatokine derived from the ER protein CREBH promotes
            triglyceride metabolism by stimulating lipoprotein lipase activity.
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Shimizu-Albergine,M., Basu,D., Kanter,J.E., Kramer,F., Kothari,V.,
            Barnhart,S., Thornock,C., Mullick,A.E., Clouet-Foraison,N.,
            Vaisar,T., Heinecke,J.W., Hegele,R.A., Goldberg,I.J. and
            Bornfeldt,K.E.
  TITLE     CREBH normalizes dyslipidemia and halts atherosclerosis in diabetes
            by decreasing circulating remnant lipoproteins
  JOURNAL   J Clin Invest 131 (22) (2021)
   PUBMED   34491909
  REMARK    GeneRIF: CREBH normalizes dyslipidemia and halts atherosclerosis in
            diabetes by decreasing circulating remnant lipoproteins.
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Dron,J.S., Dilliott,A.A., Lawson,A., McIntyre,A.D., Davis,B.D.,
            Wang,J., Cao,H., Movsesyan,I., Malloy,M.J., Pullinger,C.R.,
            Kane,J.P. and Hegele,R.A.
  TITLE     Loss-of-Function CREB3L3 Variants in Patients With Severe
            Hypertriglyceridemia
  JOURNAL   Arterioscler Thromb Vasc Biol 40 (8), 1935-1941 (2020)
   PUBMED   32580631
  REMARK    GeneRIF: Loss-of-Function CREB3L3 Variants in Patients With Severe
            Hypertriglyceridemia.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Nakagawa,Y. and Shimano,H.
  TITLE     CREBH Regulates Systemic Glucose and Lipid Metabolism
  JOURNAL   Int J Mol Sci 19 (5), 1396 (2018)
   PUBMED   29738435
  REMARK    GeneRIF: CREBH has a crucial role in glucose and lipid metabolism
            in the liver and small intestine.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Bailey,D., Barreca,C. and O'Hare,P.
  TITLE     Trafficking of the bZIP transmembrane transcription factor CREB-H
            into alternate pathways of ERAD and stress-regulated intramembrane
            proteolysis
  JOURNAL   Traffic 8 (12), 1796-1814 (2007)
   PUBMED   17875199
  REMARK    GeneRIF: analysis of CREB-H trafficking into alternate pathways of
            ERAD and stress-regulated intramembrane proteolysis
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Zhang,K., Shen,X., Wu,J., Sakaki,K., Saunders,T., Rutkowski,D.T.,
            Back,S.H. and Kaufman,R.J.
  TITLE     Endoplasmic reticulum stress activates cleavage of CREBH to induce
            a systemic inflammatory response
  JOURNAL   Cell 124 (3), 587-599 (2006)
   PUBMED   16469704
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Stirling,J. and O'hare,P.
  TITLE     CREB4, a transmembrane bZip transcription factor and potential new
            substrate for regulation and cleavage by S1P
  JOURNAL   Mol Biol Cell 17 (1), 413-426 (2006)
   PUBMED   16236796
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Omori,Y., Imai,J., Watanabe,M., Komatsu,T., Suzuki,Y., Kataoka,K.,
            Watanabe,S., Tanigami,A. and Sugano,S.
  TITLE     CREB-H: a novel mammalian transcription factor belonging to the
            CREB/ATF family and functioning via the box-B element with a
            liver-specific expression
  JOURNAL   Nucleic Acids Res 29 (10), 2154-2162 (2001)
   PUBMED   11353085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313099.1, AB050902.1 and
            AB073612.1.
            
            Summary: This gene encodes a member of the basic-leucine zipper
            family and the AMP-dependent transcription factor family. The
            encoded protein is localized to the endoplasmic reticulum and acts
            as a transcription factor activated by cyclic AMP stimulation. The
            encoded protein binds the cyclic AMP response element (CRE) and the
            box-B element and has been linked to acute inflammatory response,
            hepatocellular carcinoma, triglyceride metabolism, and hepcidin
            expression. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB050902.1, SRR1660803.50103.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2144835
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000078445.7/ ENSP00000078445.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..461
                     /product="cyclic AMP-responsive element-binding protein
                     3-like protein 3 isoform a"
                     /note="CREB/ATF family transcription factor; cyclic
                     AMP-responsive element-binding protein 3-like protein 3;
                     cAMP-responsive element-binding protein, hepatic-specific"
                     /calculated_mol_wt=48946
     Region          51..120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Region          244..304
                     /region_name="bZIP_CREB3"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 3 (CREB3) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14689"
                     /db_xref="CDD:269837"
     Region          245..274
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Region          246..297
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269837"
     Site            order(249..250,252..254,256..261,263..265)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269837"
     Site            order(264,267..268,271..272,274..275,278..279,281..282,
                     285..286,288..289,292..293,295..296)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269837"
     Region          285..306
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Site            363..364
                     /site_type="cleavage"
                     /note="Cleavage, by PS1. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Region          370..408
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Site            379
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:22171320; propagated from
                     UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Site            410
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Site            413
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20356926; propagated from
                     UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Site            420
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20356926; propagated from
                     UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Site            427
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20356926; propagated from
                     UniProtKB/Swiss-Prot (Q68CJ9.2)"
     Region          442..461
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CJ9.2)"
     CDS             1..461
                     /gene="CREB3L3"
                     /gene_synonym="CREB-H; CREBH; HYST1481; HYTG2"
                     /coded_by="NM_032607.3:118..1503"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12121.1"
                     /db_xref="GeneID:84699"
                     /db_xref="HGNC:HGNC:18855"
                     /db_xref="MIM:611998"
ORIGIN      
        1 mntdlaagkm asaacsmdpi dsfelldllf drqdgilrhv elgegwghvk dqqvlpnpds
       61 ddflssilgs gdslpssplw spegsdsgis edlpsdpqdt pprsgpatsp agchpaqpgk
      121 gpclsyhpgn scstttpgpv iqvpeasvti dlemwspggr icaekpadpv dlsprcnltv
      181 kdlllsgssg dlqqhhlgas yllrpgaghc qelvltedek kllakegitl ptqlpltkye
      241 ervlkkirrk irnkqsaqes rkkkkeyidg letrmsacta qnqelqrkvl hlekqnlsll
      301 eqlkklqaiv vqstsksaqt gtcvavllls faliilpsis pfgpnktesp gdfapvrvfs
      361 rtlhndaasr vaadavpgse apgprpeadt treespgspg adwgfqdtan ltnsteeldn
      421 atlvlrnate glgqvalldw vapgpstgsg ragleaagde l
//
LOCUS       NP_065087                604 aa            linear   PRI 27-APR-2025
DEFINITION  ectonucleoside triphosphate diphosphohydrolase 7 isoform 2 [Homo
            sapiens].
ACCESSION   NP_065087
VERSION     NP_065087.1
DBSOURCE    REFSEQ: accession NM_020354.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Tordella,L., Khan,S., Hohmeyer,A., Banito,A., Klotz,S., Raguz,S.,
            Martin,N., Dhamarlingam,G., Carroll,T., Gonzalez Meljem,J.M.,
            Deswal,S., Martinez-Barbera,J.P., Garcia-Escudero,R., Zuber,J.,
            Zender,L. and Gil,J.
  TITLE     SWI/SNF regulates a transcriptional program that induces senescence
            to prevent liver cancer
  JOURNAL   Genes Dev 30 (19), 2187-2198 (2016)
   PUBMED   27737960
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Yegutkin,G.G.
  TITLE     Enzymes involved in metabolism of extracellular nucleotides and
            nucleosides: functional implications and measurement of activities
  JOURNAL   Crit Rev Biochem Mol Biol 49 (6), 473-497 (2014)
   PUBMED   25418535
  REMARK    Review article
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Vaughn,B.P., Robson,S.C. and Longhi,M.S.
  TITLE     Purinergic signaling in liver disease
  JOURNAL   Dig Dis 32 (5), 516-524 (2014)
   PUBMED   25034284
  REMARK    Review article
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Zimmermann,H., Zebisch,M. and Strater,N.
  TITLE     Cellular function and molecular structure of ecto-nucleotidases
  JOURNAL   Purinergic Signal 8 (3), 437-502 (2012)
   PUBMED   22555564
  REMARK    Review article
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Robson,S.C., Sevigny,J. and Zimmermann,H.
  TITLE     The E-NTPDase family of ectonucleotidases: Structure function
            relationships and pathophysiological significance
  JOURNAL   Purinergic Signal 2 (2), 409-430 (2006)
   PUBMED   18404480
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Kirley,T.L., Crawford,P.A. and Smith,T.M.
  TITLE     The structure of the nucleoside triphosphate diphosphohydrolases
            (NTPDases) as revealed by mutagenic and computational modeling
            analyses
  JOURNAL   Purinergic Signal 2 (2), 379-389 (2006)
   PUBMED   17710224
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Shi,J.D., Kukar,T., Wang,C.Y., Li,Q.Z., Cruz,P.E.,
            Davoodi-Semiromi,A., Yang,P., Gu,Y., Lian,W., Wu,D.H. and She,J.X.
  TITLE     Molecular cloning and characterization of a novel mammalian
            endo-apyrase (LALP1)
  JOURNAL   J Biol Chem 276 (20), 17474-17478 (2001)
   PUBMED   11278936
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK055540.1, BC119008.1,
            AL133353.6 and AW629210.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a purine-converting ectoenzyme which
            belongs to the ecto-nucleoside triphosphate diphosphohydrolase
            (E-NTPDase) family. The encoded protein hydrolyzes extracellular
            nucleoside triphosphates (UTP, GTP, and CTP) to nucleoside
            monophosphates as part of a purinergic signaling pathway. It
            contains two transmembrane domains at the N- and C-termini and a
            large, hydrophobic catalytic domain located in between. This gene
            affects oxidative stress as well as DNA damage and is a mediator of
            senescence. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks
            an alternate exon in the 5' region, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) has a shorter and distinct N-terminus, compared to isoform 1.
            Both variants 2 and 3 encode the same isoform (2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.189723.1,
                                           SRR1803615.10665.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370489.5/ ENSP00000359520.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..604
                     /product="ectonucleoside triphosphate diphosphohydrolase 7
                     isoform 2"
                     /EC_number="3.6.1.15"
                     /note="lysosomal apyrase-like protein 1; NTPDase 7"
                     /calculated_mol_wt=68829
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQZ7.1)"
     Region          82..531
                     /region_name="ASKHA_NBD_NTPDase4-like"
                     /note="nucleotide-binding domain (NBD) of the
                     ectonucleoside triphosphate diphosphohydrolase 4
                     (NTPDase4)-like subfamily; cd24045"
                     /db_xref="CDD:466895"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQZ7.1)"
     Site            547..567
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQZ7.1)"
     CDS             1..604
                     /gene="ENTPD7"
                     /gene_synonym="LALP1"
                     /coded_by="NM_020354.5:176..1990"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7480.1"
                     /db_xref="GeneID:57089"
                     /db_xref="HGNC:HGNC:19745"
                     /db_xref="MIM:616753"
ORIGIN      
        1 marisfsylc paswyftvpt vspflrqrva flglffiscl lllmliidfr hwsaslprdr
       61 qyerylarvg eleatdtedp nlnyglvvdc gssgsrifvy fwprhngnph dlldikqmrd
      121 rnsqpvvkki kpgisamadt pehasdylrp llsfaaahvp vkkhketply ilctagmrll
      181 perkqlaila dlvkdlplef dflfsqsqae visgkqegvy awiginfvlg rfdhedesda
      241 eatqelaagr rrtvgildmg gaslqiayev ptstsvlpak qeeaakilla efnlgcdvqh
      301 tehvyrvyvt tflgfggnfa rqryedlvln etlnknrllg qktglspdnp fldpclpvgl
      361 tdvvernsqv lhvrgrgdwv scgamlspll arsntsqasl ngiyqspidf nnsefygfse
      421 ffyctedvlr iggryhgptf akaaqdycgm awsvltqrfk nglfsshade hrlkyqcfks
      481 awmyqvlheg fhfpydypnl rtaqlvydre vqwtlgaily ktrflplrdl rqegvrqahg
      541 swfrlsfvyn hylffacilv vllaiflyll rlrrihhrqt rasapldllw leevvpmmgv
      601 qvgp
//
LOCUS       NP_001239344             174 aa            linear   ROD 27-APR-2025
DEFINITION  RPA-interacting protein isoform 2 [Mus musculus].
ACCESSION   NP_001239344
VERSION     NP_001239344.1
DBSOURCE    REFSEQ: accession NM_001252415.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Kim,K., Lee,E.J., Lee,S.H., Seo,T., Jang,I.S., Park,J. and Lee,J.H.
  TITLE     Species-specific variation of RPA-interacting protein (RIP) splice
            isoforms
  JOURNAL   BMB Rep 42 (1), 22-27 (2009)
   PUBMED   19192389
  REMARK    GeneRIF: The alternative splicing of RIPalpha in the Drosophila,
            Xenopus, and mouse system, was examined.
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Park,J., Seo,T., Kim,H. and Choe,J.
  TITLE     Sumoylation of the novel protein hRIP{beta} is involved in
            replication protein A deposition in PML nuclear bodies
  JOURNAL   Mol Cell Biol 25 (18), 8202-8214 (2005)
   PUBMED   16135809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL596136.5, CB588111.1, DQ810268.1, BC047996.1 and BY576068.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ810268.1, SRR7345562.4049582.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 43.21 cM"
     Protein         1..174
                     /product="RPA-interacting protein isoform 2"
                     /note="RPA interacting protein epsilon; RPA interacting
                     protein delta 2"
                     /calculated_mol_wt=19841
     Region          8..47
                     /region_name="RPA_interact_N"
                     /note="Replication protein A interacting N-terminal;
                     pfam14766"
                     /db_xref="CDD:464304"
     Region          59..127
                     /region_name="RPA_interact_M"
                     /note="Replication protein A interacting middle;
                     pfam14767"
                     /db_xref="CDD:434193"
     Region          136..>163
                     /region_name="RPA_interact_C"
                     /note="Replication protein A interacting C-terminal;
                     pfam14768"
                     /db_xref="CDD:464305"
     CDS             1..174
                     /gene="Rpain"
                     /gene_synonym="2400006N03Rik; Rip"
                     /coded_by="NM_001252415.2:309..833"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS56790.1"
                     /db_xref="GeneID:69723"
                     /db_xref="MGI:MGI:1916973"
ORIGIN      
        1 maessgsphr llykqvgsph wketfrqgcl ermrnsrhrl lnkyrqaags tpgtasdrll
       61 vqevmeeewa slqsvencpe allqlelpld lavlqdieqe lcneeksiis eyeedlefde
      121 sclrrmlaew eanslicpvc ikynlrimns vvtcpcglhi pvhspveqkr spvf
//
LOCUS       NP_001349910             196 aa            linear   ROD 27-APR-2025
DEFINITION  protein RER1 [Mus musculus].
ACCESSION   NP_001349910 XP_006539193
VERSION     NP_001349910.1
DBSOURCE    REFSEQ: accession NM_001362981.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Hara,T., Maejima,I., Akuzawa,T., Hirai,R., Kobayashi,H.,
            Tsukamoto,S., Tsunoda,M., Ono,A., Yamakoshi,S., Oikawa,S. and
            Sato,K.
  TITLE     Rer1-mediated quality control system is required for neural stem
            cell maintenance during cerebral cortex development
  JOURNAL   PLoS Genet 14 (9), e1007647 (2018)
   PUBMED   30260951
  REMARK    GeneRIF: Study in knockout mice and genetically modified human HAP1
            cell line suggests that Rer1 maintains Notch signaling by
            maintaining sufficient expression of the gamma-secretase complex on
            the cell surface and regulating neural stem cell maintenance during
            cerebral cortex development.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Valkova,C., Liebmann,L., Kramer,A., Hubner,C.A. and Kaether,C.
  TITLE     The sorting receptor Rer1 controls Purkinje cell function via
            voltage gated sodium channels
  JOURNAL   Sci Rep 7, 41248 (2017)
   PUBMED   28117367
  REMARK    GeneRIF: Rer1 controls the assembly and transport of Nav1.1 and
            1.6, the principal sodium channels responsible for recurrent
            firing, in Purkinje cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Jurisch-Yaksi,N., Rose,A.J., Lu,H., Raemaekers,T., Munck,S.,
            Baatsen,P., Baert,V., Vermeire,W., Scales,S.J., Verleyen,D.,
            Vandepoel,R., Tylzanowski,P., Yaksi,E., de Ravel,T., Yost,H.J.,
            Froyen,G., Arrington,C.B. and Annaert,W.
  TITLE     Rer1p maintains ciliary length and signaling by regulating
            gamma-secretase activity and Foxj1a levels
  JOURNAL   J Cell Biol 200 (6), 709-720 (2013)
   PUBMED   23479743
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Ulyanova,T., Jiang,Y., Padilla,S., Nakamoto,B. and
            Papayannopoulou,T.
  TITLE     Combinatorial and distinct roles of alpha and alpha integrins in
            stress erythropoiesis in mice
  JOURNAL   Blood 117 (3), 975-985 (2011)
   PUBMED   20956802
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Valkova,C., Albrizio,M., Roder,I.V., Schwake,M., Betto,R.,
            Rudolf,R. and Kaether,C.
  TITLE     Sorting receptor Rer1 controls surface expression of muscle
            acetylcholine receptors by ER retention of unassembled
            alpha-subunits
  JOURNAL   Proc Natl Acad Sci U S A 108 (2), 621-625 (2011)
   PUBMED   21187406
  REMARK    GeneRIF: Rer1 is a functionally important unique factor that
            controls surface expression of muscle acetylcholine receptors by
            localizing unassembled alpha-subunits to the early secretory
            pathway
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL670413.19.
            
            On May 4, 2018 this sequence version replaced XP_006539193.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.4949848.1, AK168192.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164141, SAMN01164143
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 86.17 cM"
     Protein         1..196
                     /product="protein RER1"
                     /note="RER1 retention in endoplasmic reticulum 1 homolog"
                     /calculated_mol_wt=22857
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:O15258; propagated from
                     UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15258; propagated from
                     UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15258; propagated from
                     UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15258; propagated from
                     UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Region          20..185
                     /region_name="Rer1"
                     /note="Rer1 family; pfam03248"
                     /db_xref="CDD:460860"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CQU3.1)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQU3.1)"
     CDS             1..196
                     /gene="Rer1"
                     /gene_synonym="1110060F11Rik; 5830454N22Rik"
                     /coded_by="NM_001362981.1:366..956"
                     /db_xref="CCDS:CCDS19022.1"
                     /db_xref="GeneID:67830"
                     /db_xref="MGI:MGI:1915080"
ORIGIN      
        1 msegdsvgds vhgkpsvvyr ffsrlgqiyq swldkstpyt avrwvvtlgl sfvymirvyl
       61 lqgwyivtya lgiyhlnlfi aflspkvdps lmedsddgps lptkqneefr pfirrlpefk
      121 fwhaatkgil vamictffea fnvpvfwpil vmyfimlfci tmkrqikhmi kyryipfthg
      181 krrykgkedv gktfas
//
LOCUS       NP_038733                548 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 30 isoform c [Mus musculus].
ACCESSION   NP_038733 XP_017177624
VERSION     NP_038733.1
DBSOURCE    REFSEQ: accession NM_013705.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Laudermilk,L.T., Tovar,A., Homstad,A.K., Thomas,J.M.,
            McFadden,K.M., Tune,M.K., Cowley,D.O., Mock,J.R., Ideraabdullah,F.
            and Kelada,S.N.P.
  TITLE     Baseline and innate immune response characterization of a Zfp30
            knockout mouse strain
  JOURNAL   Mamm Genome 31 (7-8), 205-214 (2020)
   PUBMED   32860515
  REMARK    GeneRIF: Baseline and innate immune response characterization of a
            Zfp30 knockout mouse strain.
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Chen,W., Schwalie,P.C., Pankevich,E.V., Gubelmann,C., Raghav,S.K.,
            Dainese,R., Cassano,M., Imbeault,M., Jang,S.M., Russeil,J.,
            Delessa,T., Duc,J., Trono,D., Wolfrum,C. and Deplancke,B.
  TITLE     ZFP30 promotes adipogenesis through the KAP1-mediated activation of
            a retrotransposon-derived Pparg2 enhancer
  JOURNAL   Nat Commun 10 (1), 1809 (2019)
   PUBMED   31000713
  REMARK    GeneRIF: Using murine and human in vitro and in vivo models, study
            demonstrated that ZFP30 promotes adipogenesis by directly targeting
            and activating a retrotransposon-derived Pparg2 enhancer. Through
            mechanistic studies, study further show that ZFP30 recruits the
            co-regulator KAP1, which acts as a ZFP30 co-activator in this
            adipogenic context.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Laudermilk,L.T., Thomas,J.M. and Kelada,S.N.
  TITLE     Differential Regulation of Zfp30 Expression in Murine Airway
            Epithelia Through Altered Binding of ZFP148 to rs51434084
  JOURNAL   G3 (Bethesda) 8 (2), 687-693 (2018)
   PUBMED   29242385
  REMARK    GeneRIF: Data indicate zinc finger protein 148 (ZFP148) as a
            transcription factor that differentially binds to the zinc finger
            protein 30 protein (Zfp30) promoter region harboring rs51434084.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Rutledge,H., Aylor,D.L., Carpenter,D.E., Peck,B.C., Chines,P.,
            Ostrowski,L.E., Chesler,E.J., Churchill,G.A., de Villena,F.P. and
            Kelada,S.N.
  TITLE     Genetic regulation of Zfp30, CXCL1, and neutrophilic inflammation
            in murine lung
  JOURNAL   Genetics 198 (2), 735-745 (2014)
   PUBMED   25114278
  REMARK    GeneRIF: Zfp30 is expressed in airway epithelia in the normal mouse
            lung and Zfp30 expression in vitro affects CXCL1 responses to an
            immune stimulus.
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   8  (residues 1 to 548)
  AUTHORS   Denny,P. and Ashworth,A.
  TITLE     Zfp30, a KRAB domain containing zinc finger protein gene, maps to
            mouse chromosome 7
  JOURNAL   Mamm Genome 5 (10), 643-645 (1994)
   PUBMED   7849402
REFERENCE   9  (residues 1 to 548)
  AUTHORS   Ashworth,A. and Denny,P.
  TITLE     Zinc finger protein genes in the mouse genome
  JOURNAL   Mamm Genome 1 (3), 196-200 (1991)
   PUBMED   1797234
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC156934.1 and Z30174.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (c) is
            shorter at the N-terminus compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC049120.1, AY605122.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 17.26 cM"
     Protein         1..548
                     /product="zinc finger protein 30 isoform c"
                     /calculated_mol_wt=64232
     Region          21..82
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          178..538
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          189..209
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(250,252,254,256..257,260..261,264,278,280,284..285,
                     288..289,292,306,308,310,312..313,316..317,320)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          329..349
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(362,364,366,368..369,372..373,376,390,392,396..397,
                     400..401,404,418,420,422,424..425,428..429,432)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          385..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(474,476,478,480..481,484..485,488,502,504,508..509,
                     512..513,516,530,532,534,536..537,540..541,544)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          525..545
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..548
                     /gene="Zfp30"
                     /gene_synonym="2610306P15Rik; Zfp-30"
                     /coded_by="NM_013705.2:966..2612"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS21075.1"
                     /db_xref="GeneID:22693"
                     /db_xref="MGI:MGI:99178"
ORIGIN      
        1 mileeeqass cdsgimahst vmfrdvavgf sqeeweclsa yerdlyrdvm lenyshlvsl
       61 agcsiskpdv itlleqgkep wmivraekrr wsrdlesrys sngllpeknt yeinlspwei
      121 mgriqrrgpe dsllgkdfey kiyeeqensh rvyfrhvikt tsgkrpryrk rtpvslyqkt
      181 pngekpyecg ecgkafkvrq qltfhqriht gekpyeckec gkafrqcahl srhqrihasd
      241 klyeckkcak iftcssdlrg hqrshvgekp ydckecgkaf rvrgqlmlhq rihtgekpya
      301 ctecgksfrq vahltrhqrl nsgssrheck ecgraflcst glrlhhklht gekpydckec
      361 gkafrvrqql tlherihtge kpfdckecgk tfsrgyhltl hqrihtgekp yeckecrkff
      421 rryselishq gihigekpyd ckecgkafrl fsqltqhqsi hfgekpykcm ecektfrlls
      481 qltqhqsiht gekpydckec gkafrlhssl iqhqrihsge kpykcteckk afrqhshlty
      541 hqrihknl
//
LOCUS       NP_001654                175 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-ribosylation factor 6 [Homo sapiens].
ACCESSION   NP_001654
VERSION     NP_001654.1
DBSOURCE    REFSEQ: accession NM_001663.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Hong,P., Xu,T., Xu,J., Chen,W., Hu,H., Chen,J., Li,L., Zheng,C.,
            Li,B., Liu,J., Dai,W., Li,E., Zhang,F. and Xu,W.
  TITLE     CD24 promotes metastasis and chemoresistance by directly targeting
            Arf6-ERK pathway in esophageal squamous cell carcinoma
  JOURNAL   Cancer Lett 594, 216994 (2024)
   PUBMED   38801885
  REMARK    GeneRIF: CD24 promotes metastasis and chemoresistance by directly
            targeting Arf6-ERK pathway in esophageal squamous cell carcinoma.
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Jiang,C., Zhou,P., Zhang,X., Ma,N., Hu,Y., Zhang,M., Ghonaim,A.H.,
            Li,H., Dong,L., Zeng,W., Li,C., Lang,Y., Sun,Y., He,Q. and Li,W.
  TITLE     ARF6 promotes Streptococcus suis suilysin induced apoptosis in
            HBMECs
  JOURNAL   Int J Biol Macromol 268 (Pt 2), 131839 (2024)
   PUBMED   38663699
  REMARK    GeneRIF: ARF6 promotes Streptococcus suis suilysin induced
            apoptosis in HBMECs.
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Jiang,S., Han,X., Liu,T., He,Y., Zhao,Z., Liu,T., Cheng,S.,
            Zhang,J., Duan,L., Liu,Y., Cheng,T., Liu,Y., Ye,Q. and Gao,S.
  TITLE     HUNK inhibits cargo uptake and lysosomal traffic in the caveolar
            pathway via the AGAP3/ARF6
  JOURNAL   Sci Bull (Beijing) 69 (2), 173-178 (2024)
   PUBMED   38071109
  REMARK    GeneRIF: HUNK inhibits cargo uptake and lysosomal traffic in the
            caveolar pathway via the AGAP3/ARF6.
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Wang,J., Zheng,L.F., Ren,S., Li,D.L., Chen,C., Sun,H.H., Liu,L.Y.,
            Guo,H. and Zhao,T.J.
  TITLE     ARF6 plays a general role in targeting palmitoylated proteins from
            the Golgi to the plasma membrane
  JOURNAL   J Cell Sci 136 (15) (2023)
   PUBMED   37461827
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Zhu,Y., Wang,X., He,Z., Zhao,P., Ren,H. and Qi,Z.
  TITLE     Enterovirus 71 enters human brain microvascular endothelial cells
            through an ARF6-mediated endocytic pathway
  JOURNAL   J Med Virol 95 (7), e28915 (2023)
   PUBMED   37417384
  REMARK    GeneRIF: Enterovirus 71 enters human brain microvascular
            endothelial cells through an ARF6-mediated endocytic pathway.
REFERENCE   6  (residues 1 to 175)
  AUTHORS   D'Souza-Schorey,C. and Stahl,P.D.
  TITLE     Myristoylation is required for the intracellular localization and
            endocytic function of ARF6
  JOURNAL   Exp Cell Res 221 (1), 153-159 (1995)
   PUBMED   7589240
REFERENCE   7  (residues 1 to 175)
  AUTHORS   D'Souza-Schorey,C., Li,G., Colombo,M.I. and Stahl,P.D.
  TITLE     A regulatory role for ARF6 in receptor-mediated endocytosis
  JOURNAL   Science 267 (5201), 1175-1178 (1995)
   PUBMED   7855600
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Welsh,C.F., Moss,J. and Vaughan,M.
  TITLE     ADP-ribosylation factors: a family of approximately 20-kDa guanine
            nucleotide-binding proteins that activate cholera toxin
  JOURNAL   Mol Cell Biochem 138 (1-2), 157-166 (1994)
   PUBMED   7898460
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Tsuchiya,M., Price,S.R., Tsai,S.C., Moss,J. and Vaughan,M.
  TITLE     Molecular identification of ADP-ribosylation factor mRNAs and their
            expression in mammalian cells
  JOURNAL   J Biol Chem 266 (5), 2772-2777 (1991)
   PUBMED   1993656
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Stearns,T., Willingham,M.C., Botstein,D. and Kahn,R.A.
  TITLE     ADP-ribosylation factor is functionally and physically associated
            with the Golgi complex
  JOURNAL   Proc Natl Acad Sci U S A 87 (3), 1238-1242 (1990)
   PUBMED   2105501
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA217686.1, BC008918.2,
            BM838197.1 and BC030291.1.
            
            Summary: This gene encodes a member of the human ARF gene family,
            which is part of the RAS superfamily. The ARF genes encode small
            guanine nucleotide-binding proteins that stimulate the
            ADP-ribosyltransferase activity of cholera toxin and play a role in
            vesicular trafficking and as activators of phospholipase D. The
            product of this gene is localized to the plasma membrane, and
            regulates vesicular trafficking, remodelling of membrane lipids,
            and signaling pathways that lead to actin remodeling. A pseudogene
            of this gene is located on chromosome 7. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.549175.1,
                                           SRR1163658.414775.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298316.7/ ENSP00000298316.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q21.3"
     Protein         1..175
                     /product="ADP-ribosylation factor 6"
                     /EC_number="3.6.5.2"
                     /note="ADP ribosylation factor 6"
                     /calculated_mol_wt=19951
     Region          1..175
                     /region_name="ARF"
                     /note="ARF-like small GTPases; ARF, ADP-ribosylation
                     factor; smart00177"
                     /db_xref="CDD:128474"
     Site            20..27
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206716"
     Site            order(22..23,27,31,43..50,72,77)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206716"
     Site            order(23..28,41,44,66,122..123,125,155..156)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206716"
     Site            32..47
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206716"
     Site            37..38
                     /site_type="active"
                     /note="QS Arf6 conserved motif [active]"
                     /db_xref="CDD:206716"
     Site            order(44..48,53,63,67,73,75..77)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206716"
     Site            44
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206716"
     Site            order(45..52,62,73,76..77)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206716"
     Site            47..62
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206716"
     Site            63..66
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206716"
     Site            65..80
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206716"
     Site            122..125
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206716"
     Site            155..157
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206716"
     CDS             1..175
                     /gene="ARF6"
                     /coded_by="NM_001663.4:558..1085"
                     /db_xref="CCDS:CCDS9695.1"
                     /db_xref="GeneID:382"
                     /db_xref="HGNC:HGNC:659"
                     /db_xref="MIM:600464"
ORIGIN      
        1 mgkvlskifg nkemrilmlg ldaagkttil yklklgqsvt tiptvgfnve tvtyknvkfn
       61 vwdvggqdki rplwrhyytg tqglifvvdc adrdridear qelhriindr emrdaiilif
      121 ankqdlpdam kpheiqeklg ltrirdrnwy vqpscatsgd glyegltwlt snyks
//
LOCUS       NP_003418                570 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 76 isoform 1 [Homo sapiens].
ACCESSION   NP_003418
VERSION     NP_003418.2
DBSOURCE    REFSEQ: accession NM_003427.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Ali Assar,M.F., Abd El Gayed,E.M., Abd El-Hamid Ewis,A.S.,
            Zaid,A.B. and Abd Allah Mahmoud Fouda,E.
  TITLE     Biochemical study of ZNF76 rs10947540 and SCUBE3 rs1888822 single
            nucleotide polymorphisms in the Egyptian patients with systemic
            lupus Erythematosus
  JOURNAL   J Immunoassay Immunochem 45 (5), 415-431 (2024)
   PUBMED   38982741
  REMARK    GeneRIF: Biochemical study of ZNF76 rs10947540 and SCUBE3 rs1888822
            single nucleotide polymorphisms in the Egyptian patients with
            systemic lupus Erythematosus.
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Hua,T., Wang,R.M., Zhang,X.C., Zhao,B.B., Fan,S.B., Liu,D.X. and
            Wang,W.
  TITLE     ZNF76 predicts prognosis and response to platinum chemotherapy in
            human ovarian cancer
  JOURNAL   Biosci Rep 41 (12) (2021)
   PUBMED   34793589
  REMARK    GeneRIF: ZNF76 predicts prognosis and response to platinum
            chemotherapy in human ovarian cancer.
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Qi,Y.Y., Cui,Y., Lang,H., Zhai,Y.L., Zhang,X.X., Wang,X.Y.,
            Liu,X.R., Zhao,Y.F., Ning,X.H. and Zhao,Z.Z.
  TITLE     The ZNF76 rs10947540 polymorphism associated with systemic lupus
            erythematosus risk in Chinese populations
  JOURNAL   Sci Rep 11 (1), 5186 (2021)
   PUBMED   33664275
  REMARK    GeneRIF: The ZNF76 rs10947540 polymorphism associated with systemic
            lupus erythematosus risk in Chinese populations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Zheng,G. and Yang,Y.C.
  TITLE     ZNF76, a novel transcriptional repressor targeting TATA-binding
            protein, is modulated by sumoylation
  JOURNAL   J Biol Chem 279 (41), 42410-42421 (2004)
   PUBMED   15280358
  REMARK    GeneRIF: ZNF76 functions as a transcriptional repressor through its
            interaction with TBP and sumoylation modulates its transcriptional
            repression activity
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Kubota,H., Yokota,S., Yanagi,H. and Yura,T.
  TITLE     Transcriptional regulation of the mouse cytosolic chaperonin
            subunit gene Ccta/t-complex polypeptide 1 by selenocysteine tRNA
            gene transcription activating factor family zinc finger proteins
  JOURNAL   J Biol Chem 275 (37), 28641-28648 (2000)
   PUBMED   10893243
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Myslinski,E., Krol,A. and Carbon,P.
  TITLE     ZNF76 and ZNF143 are two human homologs of the transcriptional
            activator Staf
  JOURNAL   J Biol Chem 273 (34), 21998-22006 (1998)
   PUBMED   9705341
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Ragoussis,J., Senger,G., Mockridge,I., Sanseau,P., Ruddy,S.,
            Dudley,K., Sheer,D. and Trowsdale,J.
  TITLE     A testis-expressed Zn finger gene (ZNF76) in human 6p21.3
            centromeric to the MHC is closely linked to the human homolog of
            the t-complex gene tcp-11
  JOURNAL   Genomics 14 (3), 673-679 (1992)
   PUBMED   1427894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC299240.1, BC002549.2, Z97832.11 and BE962441.2.
            
            On Jun 10, 2002 this sequence version replaced NP_003418.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.204925.1, BC000133.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373953.8/ ENSP00000363064.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..570
                     /product="zinc finger protein 76 isoform 1"
                     /note="zinc finger protein 76 (expressed in testis); zinc
                     finger protein 523"
                     /calculated_mol_wt=61700
     Region          34..99
                     /region_name="3 X 12 AA approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P36508.2)"
     Region          <106..220
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          167..189
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(174,176,178,180..181,184..185,188,204,206,210..211,
                     214..215,218,234,236,238,240..241,244..245,248)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <179..366
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          197..219
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          227..249
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          257..279
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          287..309
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          317..339
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          347..365
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          365..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36508.2)"
     CDS             1..570
                     /gene="ZNF76"
                     /gene_synonym="D6S229E; Zfp523; ZNF523"
                     /coded_by="NM_003427.5:204..1916"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4801.1"
                     /db_xref="GeneID:7629"
                     /db_xref="HGNC:HGNC:13149"
                     /db_xref="MIM:194549"
ORIGIN      
        1 meslglhtvt lsdgttayvq qavkgeklle gqviqledgt tayihqvtvq kealsfedgq
       61 pvqledgsma yihrtpregy dpstleavql edgstayihh pvavpsesti lavqtevgle
      121 dlaaeddegf sadavvaleq yaskvlhdsq iprngkgqqv gdrafrcgyk gcgrlyttah
      181 hlkvheraht gdrpyrcdfp scgkafatgy glkshvrtht gekpykcpee lcskafktsg
      241 dlqkhvrtht gerpfqcpfe gcgrsfttsn irkvhvrtht gerpytcpep hcgrgftsat
      301 nyknhvriht gekpyvctvp gcgkrfteys slykhhvvht hckpytcstc gktyrqtstl
      361 amhkrsahge leateeseqa lyeqqqleaa saaeespppk rpriaylsev keerddipaq
      421 vamvteedga pqvalitqdg aqqvslsped lqalgsaism vtqhgsttlt ipspdadlat
      481 sgthtvtmvs adgtqtqpvt iitsgavvae dssvaslrhq qvallatang thiavqleeq
      541 qtleeainva taamqqgavt lettvsesgc
//
LOCUS       NP_001348836             121 aa            linear   ROD 27-APR-2025
DEFINITION  protein TCL1B5 [Mus musculus].
ACCESSION   NP_001348836 XP_006516000
VERSION     NP_001348836.1
DBSOURCE    REFSEQ: accession NM_001361907.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Hallas,C., Pekarsky,Y., Itoyama,T., Varnum,J., Bichi,R.,
            Rothstein,J.L. and Croce,C.M.
  TITLE     Genomic analysis of human and mouse TCL1 loci reveals a complex of
            tightly clustered genes
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14418-14423 (1999)
   PUBMED   10588720
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK139627.1, BC125294.1 and AF195493.1.
            
            On Mar 30, 2018 this sequence version replaced XP_006516000.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC125294.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN00849374
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 55.23 cM"
     Protein         1..121
                     /product="protein TCL1B5"
                     /calculated_mol_wt=13537
     Region          1..117
                     /region_name="TCL1_MTCP1"
                     /note="TCL1/MTCP1 family; pfam01840"
                     /db_xref="CDD:460358"
     CDS             1..121
                     /gene="Tcl1b5"
                     /gene_synonym="D12Ertd644e"
                     /coded_by="NM_001361907.1:72..437"
                     /db_xref="CCDS:CCDS36546.1"
                     /db_xref="GeneID:27382"
                     /db_xref="MGI:MGI:1351635"
ORIGIN      
        1 maavsvdpqr plpvllvsvs lgiyedehhr vwiavnvets hsshgnriet cvtvhlqhmt
       61 tlpqeptpqq pinnnslptm wrlesrntyt gtdgtywrll dhsqmgdtvq ltldiiiged
      121 d
//
LOCUS       NP_061130                513 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 395 [Homo sapiens].
ACCESSION   NP_061130 NP_060076
VERSION     NP_061130.1
DBSOURCE    REFSEQ: accession NM_018660.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Kurogi,S., Hijiya,N., Hidano,S., Sato,S., Uchida,T., Tsukamoto,Y.,
            Nakada,C., Yada,K., Hirashita,T., Inomata,M., Murakami,K.,
            Takahashi,N., Kobayashi,T. and Moriyama,M.
  TITLE     Downregulation of ZNF395 Drives Progression of Pancreatic Ductal
            Adenocarcinoma through Enhancement of Growth Potential
  JOURNAL   Pathobiology 88 (5), 374-382 (2021)
   PUBMED   33794543
  REMARK    GeneRIF: Downregulation of ZNF395 Drives Progression of Pancreatic
            Ductal Adenocarcinoma through Enhancement of Growth Potential.
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Yao,X., Tan,J., Lim,K.J., Koh,J., Ooi,W.F., Li,Z., Huang,D.,
            Xing,M., Chan,Y.S., Qu,J.Z., Tay,S.T., Wijaya,G., Lam,Y.N.,
            Hong,J.H., Lee-Lim,A.P., Guan,P., Ng,M.S.W., He,C.Z., Lin,J.S.,
            Nandi,T., Qamra,A., Xu,C., Myint,S.S., Davies,J.O.J., Goh,J.Y.,
            Loh,G., Tan,B.C., Rozen,S.G., Yu,Q., Tan,I.B.H., Cheng,C.W.S.,
            Li,S., Chang,K.T.E., Tan,P.H., Silver,D.L., Lezhava,A., Steger,G.,
            Hughes,J.R., Teh,B.T. and Tan,P.
  TITLE     VHL Deficiency Drives Enhancer Activation of Oncogenes in Clear
            Cell Renal Cell Carcinoma
  JOURNAL   Cancer Discov 7 (11), 1284-1305 (2017)
   PUBMED   28893800
  REMARK    GeneRIF: epigenomic profiling of clear cell renal cell carcinoma
            (ccRCC) establishes a compendium of somatically altered
            cis-regulatory elements, uncovering new potential targets including
            ZNF395. Loss of VHL, a ccRCC signature event, causes pervasive
            enhancer malfunction, with binding of enhancer-centric HIF2a and
            recruitment of histone acetyltransferase p300 at preexisting
            lineage-specific promoter-enhancer complexes
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Schroeder,L., Herwartz,C., Jordanovski,D. and Steger,G.
  TITLE     ZNF395 Is an Activator of a Subset of IFN-Stimulated Genes
  JOURNAL   Mediators Inflamm 2017, 1248201 (2017)
   PUBMED   28316371
  REMARK    GeneRIF: The transcriptional activation of CXCL10 and CXCL11 by
            ZNF395 was abolished after inhibition of IKK by BMS-345541, which
            increased the stability of ZNF395. ZNF395 encodes at least two
            motifs that mediate the enhanced degradation of ZNF395 in response
            to IKK activation. Thus, IKK is required for ZNF395-mediated
            activation of transcription and enhances its turn-over to keep the
            activity of ZNF395 low.
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Pang,F., Zha,R., Zhao,Y., Wang,Q., Chen,D., Zhang,Z., Chen,T.,
            Yao,M., Gu,J. and He,X.
  TITLE     MiR-525-3p enhances the migration and invasion of liver cancer
            cells by downregulating ZNF395
  JOURNAL   PLoS One 9 (3), e90867 (2014)
   PUBMED   24599008
  REMARK    GeneRIF: miR-525-3p promotes liver cancer cell migration and
            invasion by directly targeting ZNF395.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Sichtig,N., Korfer,N. and Steger,G.
  TITLE     Papillomavirus binding factor binds to SAP30 and represses
            transcription via recruitment of the HDAC1 co-repressor complex
  JOURNAL   Arch Biochem Biophys 467 (1), 67-75 (2007)
   PUBMED   17897615
  REMARK    GeneRIF: PBF binds to SAP30 and represses transcription via
            recruitment of the HDAC1 co-repressor complex
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Sichtig,N., Silling,S. and Steger,G.
  TITLE     Papillomavirus binding factor (PBF)-mediated inhibition of cell
            growth is regulated by 14-3-3beta
  JOURNAL   Arch Biochem Biophys 464 (1), 90-99 (2007)
   PUBMED   17531190
  REMARK    GeneRIF: PBF is a new cellular factor mediating the effects of
            PI3K/Akt signaling and 14-3-3 on cell growth
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Tsukahara,T., Nabeta,Y., Kawaguchi,S., Ikeda,H., Sato,Y.,
            Shimozawa,K., Ida,K., Asanuma,H., Hirohashi,Y., Torigoe,T.,
            Hiraga,H., Nagoya,S., Wada,T., Yamashita,T. and Sato,N.
  TITLE     Identification of human autologous cytotoxic T-lymphocyte-defined
            osteosarcoma gene that encodes a transcriptional regulator,
            papillomavirus binding factor
  JOURNAL   Cancer Res 64 (15), 5442-5448 (2004)
   PUBMED   15289353
  REMARK    GeneRIF: PBF is an osteosarcoma-associated antigen recognized by
            autologous cytotoxic T-lymphocyte clone in the context of
            HLA-B*5502.
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Tanaka,K., Shouguchi-Miyata,J., Miyamoto,N. and Ikeda,J.E.
  TITLE     Novel nuclear shuttle proteins, HDBP1 and HDBP2, bind to neuronal
            cell-specific cis-regulatory element in the promoter for the human
            Huntington's disease gene
  JOURNAL   J Biol Chem 279 (8), 7275-7286 (2004)
   PUBMED   14625278
  REMARK    GeneRIF: HDBP1 and HDBP2 are novel transcription factors shuttling
            between nucleus and cytoplasm and bind to the specific GCCGGCG,
            which is an essential cis-element for HD gene expression in
            neuronal cells
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Boeckle,S., Pfister,H. and Steger,G.
  TITLE     A new cellular factor recognizes E2 binding sites of
            papillomaviruses which mediate transcriptional repression by E2
  JOURNAL   Virology 293 (1), 103-117 (2002)
   PUBMED   11853404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK023418.1, BG759384.1, BI917232.1, BG249131.1, CB960515.1,
            AK026076.1, BC008870.2, AL137588.1 and AI049727.1.
            
            On Apr 6, 2004 this sequence version replaced NP_060076.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023418.1, AB073627.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344423.10/ ENSP00000340494.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1"
     Protein         1..513
                     /product="zinc finger protein 395"
                     /note="Huntington's disease gene regulatory region-binding
                     protein 2; papillomavirus regulatory factor PRF-1;
                     HD-regulating factor 2; papillomavirus-binding factor;
                     papillomavirus regulatory factor 1; HD gene regulatory
                     region-binding protein 2; huntington disease gene
                     regulatory region-binding protein 2"
                     /calculated_mol_wt=54808
     Region          7..109
                     /region_name="DUF4772"
                     /note="Domain of unknown function (DUF4772); pfam15997"
                     /db_xref="CDD:464964"
     Region          17..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8N7.2)"
     Region          165..174
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8N7.2)"
     Region          204..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8N7.2)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H8N7.2)"
     Region          335..394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8N7.2)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H8N7.2)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8N7.2)"
     CDS             1..513
                     /gene="ZNF395"
                     /gene_synonym="HDBP-2; HDBP2; HDRF-2; PBF; PRF-1; PRF1;
                     Si-1-8-14"
                     /coded_by="NM_018660.3:127..1668"
                     /db_xref="CCDS:CCDS6067.1"
                     /db_xref="GeneID:55893"
                     /db_xref="HGNC:HGNC:18737"
                     /db_xref="MIM:609494"
ORIGIN      
        1 masvlsrrlg krsllgarvl gpsasegpsa appseplleg aapqpfttsd dtpcqeqpke
       61 vlkapstsgl qqvafqpgqk vyvwyggqec tglveqhswm egqvtvwlle qklqvccrve
      121 evwlaelqgp cpqapplepg aqalayrpvs rnidvpkrks davemdemma amvltslscs
      181 pvvqsppgte anfsasraac dpwkesgdis dsgssttsgh wsgssgvstp spphpqaspk
      241 ylgdafgspq tdhgfetdpd pflldepapr krknsvkvmy kclwpncgkv lrsivgikrh
      301 vkalhlgdtv dsdqfkreed fyytevqlke esaaaaaaaa agtpvpgtpt sepaptpsmt
      361 glplsalppp lhkaqssgpe hpgpesslps galsksapgs fwhiqadhay qalpsfqipv
      421 sphiytsvsw aaapsaacsl spvrsrslsf sepqqpapam kshlivtspp raqsgarkar
      481 geakkcrkvy giehrdqwct acrwkkacqr fld
//
LOCUS       NP_071427                317 aa            linear   PRI 27-APR-2025
DEFINITION  tenomodulin [Homo sapiens].
ACCESSION   NP_071427
VERSION     NP_071427.2
DBSOURCE    REFSEQ: accession NM_022144.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Song,W., Wang,H., Ma,L. and Chen,Y.
  TITLE     Associations between the TNMD rs4828038 and ACE2 rs879922
            polymorphisms and preeclampsia susceptibility: a case-control study
  JOURNAL   J Obstet Gynaecol 42 (5), 1132-1136 (2022)
   PUBMED   34996340
  REMARK    GeneRIF: Associations between the TNMD rs4828038 and ACE2 rs879922
            polymorphisms and preeclampsia susceptibility: a case-control
            study.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Lin,D., Alberton,P., Delgado Caceres,M., Prein,C.,
            Clausen-Schaumann,H., Dong,J., Aszodi,A., Shukunami,C.,
            Iatridis,J.C. and Docheva,D.
  TITLE     Loss of tenomodulin expression is a risk factor for age-related
            intervertebral disc degeneration
  JOURNAL   Aging Cell 19 (3), e13091 (2020)
   PUBMED   32083813
  REMARK    GeneRIF: Loss of tenomodulin expression is a risk factor for
            age-related intervertebral disc degeneration.
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Shukunami,C., Oshima,Y. and Hiraki,Y.
  TITLE     Chondromodulin-I and tenomodulin: a new class of tissue-specific
            angiogenesis inhibitors found in hypovascular connective tissues
  JOURNAL   Biochem Biophys Res Commun 333 (2), 299-307 (2005)
   PUBMED   15950187
  REMARK    Review article
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Oshima,Y., Sato,K., Tashiro,F., Miyazaki,J., Nishida,K., Hiraki,Y.,
            Tano,Y. and Shukunami,C.
  TITLE     Anti-angiogenic action of the C-terminal domain of tenomodulin that
            shares homology with chondromodulin-I
  JOURNAL   J Cell Sci 117 (Pt 13), 2731-2744 (2004)
   PUBMED   15150318
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Brandau,O., Meindl,A., Fassler,R. and Aszodi,A.
  TITLE     A novel gene, tendin, is strongly expressed in tendons and
            ligaments and shows high homology with chondromodulin-I
  JOURNAL   Dev Dyn 221 (1), 72-80 (2001)
   PUBMED   11357195
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Shukunami,C., Oshima,Y. and Hiraki,Y.
  TITLE     Molecular cloning of tenomodulin, a novel chondromodulin-I related
            gene
  JOURNAL   Biochem Biophys Res Commun 280 (5), 1323-1327 (2001)
   PUBMED   11162673
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Yamana,K., Wada,H., Takahashi,Y., Sato,H., Kasahara,Y. and
            Kiyoki,M.
  TITLE     Molecular cloning and characterization of CHM1L, a novel membrane
            molecule similar to chondromodulin-I
  JOURNAL   Biochem Biophys Res Commun 280 (4), 1101-1106 (2001)
   PUBMED   11162640
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF191770.1, AF291656.1 and
            AB055421.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 31, 2007 this sequence version replaced NP_071427.1.
            
            Summary: This gene encodes a protein that is related to
            chondromodulin-I, which is a cartilage-specific glycoprotein that
            functions to stimulate chondrocyte growth and to inhibit tube
            formation of endothelial cells. This protein is also an
            angiogenesis inhibitor. Genetic variation in this gene is
            associated with a risk for type 2 diabetes, central obesity and
            serum levels of systemic immune mediators in a body size-dependent
            manner. This gene is also a candidate gene for age-related macular
            degeneration, though a direct link has yet to be demonstrated.
            [provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF234259.1, AF191770.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151741, SAMEA2153427
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373031.5/ ENSP00000362122.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..317
                     /product="tenomodulin"
                     /note="BRICHOS domain containing 4; myodulin; tendin;
                     chondromodulin-IB; hTeM; hChM1L; chondromodulin-1-like
                     protein; chondromodulin-I-like protein"
                     /calculated_mol_wt=37000
     Site            31..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2S6.1)"
     Region          93..186
                     /region_name="BRICHOS"
                     /note="The BRICHOS domain is found in a variety of
                     proteins implicated in dementia, respiratory distress and
                     cancer; smart01039"
                     /db_xref="CDD:198107"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H2S6.1)"
     Site            180
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H2S6.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESC2; propagated from
                     UniProtKB/Swiss-Prot (Q9H2S6.1)"
     CDS             1..317
                     /gene="TNMD"
                     /gene_synonym="BRICD4; CHM1L; TEM"
                     /coded_by="NM_022144.3:84..1037"
                     /db_xref="CCDS:CCDS14469.1"
                     /db_xref="GeneID:64102"
                     /db_xref="HGNC:HGNC:17757"
                     /db_xref="MIM:300459"
ORIGIN      
        1 maknppence dchilnaeaf kskkickslk icglvfgila ltlivlfwgs khfwpevpkk
       61 aydmehtfys ngekkkiyme idpvtrteif rsgngtdetl evhdfkngyt giyfvglqkc
      121 fiktqikvip efsepeeeid eneeitttff eqsviwvpae kpienrdflk nskileicdn
      181 vtmywinptl isvselqdfe eegedlhfpa nekkgieqne qwvvpqvkve ktrharqase
      241 eelpindyte ngiefdpmld ergycciycr rgnrycrrvc epllgyypyp ycyqggrvic
      301 rvimpcnwwv armlgrv
//
LOCUS       NP_056530                509 aa            linear   PRI 27-APR-2025
DEFINITION  group 3 secretory phospholipase A2 precursor [Homo sapiens].
ACCESSION   NP_056530
VERSION     NP_056530.2
DBSOURCE    REFSEQ: accession NM_015715.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ray,U., Roy,D., Jin,L., Thirusangu,P., Staub,J., Xiao,Y.,
            Kalogera,E., Wahner Hendrickson,A.E., Cullen,G.D., Goergen,K.,
            Oberg,A.L. and Shridhar,V.
  TITLE     Group III phospholipase A2 downregulation attenuated survival and
            metastasis in ovarian cancer and promotes chemo-sensitization
  JOURNAL   J Exp Clin Cancer Res 40 (1), 182 (2021)
   PUBMED   34082797
  REMARK    GeneRIF: Group III phospholipase A2 downregulation attenuated
            survival and metastasis in ovarian cancer and promotes
            chemo-sensitization.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Murase,R., Taketomi,Y., Miki,Y., Nishito,Y., Saito,M., Fukami,K.,
            Yamamoto,K. and Murakami,M.
  TITLE     Group III phospholipase A2 promotes colitis and colorectal cancer
  JOURNAL   Sci Rep 7 (1), 12261 (2017)
   PUBMED   28947740
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Ewing,H., Fernandez-Vega,V., Spicer,T.P., Chase,P., Brown,S.,
            Scampavia,L., Roush,W.R., Riley,S., Rosen,H., Hodder,P., Lambeau,G.
            and Gelb,M.H.
  TITLE     Fluorometric High-Throughput Screening Assay for Secreted
            Phospholipases A2 Using Phospholipid Vesicles
  JOURNAL   J Biomol Screen 21 (7), 713-721 (2016)
   PUBMED   27146384
  REMARK    GeneRIF: Several hits were discovered, and data have been uploaded
            to PubChem. This study describes the first high-throughput optical
            screening assay for secreted phospholipase A2 inhibitors based on a
            phospholipid vesicle substrate
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Yui,D., Nishida,Y., Nishina,T., Mogushi,K., Tajiri,M.,
            Ishibashi,S., Ajioka,I., Ishikawa,K., Mizusawa,H., Murayama,S. and
            Yokota,T.
  TITLE     Enhanced Phospholipase A2 Group 3 Expression by Oxidative Stress
            Decreases the Insulin-Degrading Enzyme
  JOURNAL   PLoS One 10 (12), e0143518 (2015)
   PUBMED   26637123
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Kazama,S., Kitayama,J., Hiyoshi,M., Taketomi,Y., Murakami,M.,
            Nishikawa,T., Tanaka,T., Tanaka,J., Kiyomatsu,T., Kawai,K.,
            Hata,K., Yamaguchi,H., Nozawa,H., Ishihara,S., Sunami,E. and
            Watanabe,T.
  TITLE     Phospholipase A2 Group III and Group X Have Opposing Associations
            with Prognosis in Colorectal Cancer
  JOURNAL   Anticancer Res 35 (5), 2983-2990 (2015)
   PUBMED   25964585
  REMARK    GeneRIF: sPLA2GIII expression may be used as a risk factor for
            lymph node metastasis and a prognostic marker in colorectal cancer.
            In addition, sPLA2GIII and sPLA2GX may play opposing roles in
            colorectal carcinogenesis
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Masuda,S., Yamamoto,K., Hirabayashi,T., Ishikawa,Y., Ishii,T.,
            Kudo,I. and Murakami,M.
  TITLE     Human group III secreted phospholipase A2 promotes neuronal
            outgrowth and survival
  JOURNAL   Biochem J 409 (2), 429-438 (2008)
   PUBMED   17868035
  REMARK    GeneRIF: potential contribution of sPLA2-III to neuronal
            differentiation and its function under certain conditions
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Murakami,M., Masuda,S., Shimbara,S., Ishikawa,Y., Ishii,T. and
            Kudo,I.
  TITLE     Cellular distribution, post-translational modification, and
            tumorigenic potential of human group III secreted phospholipase
            A(2)
  JOURNAL   J Biol Chem 280 (26), 24987-24998 (2005)
   PUBMED   15863501
  REMARK    GeneRIF: sPLA(2)-III may have a role in cancer development by
            stimulating tumor cell growth and angiogenesis
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Murakami,M., Masuda,S., Shimbara,S., Bezzine,S., Lazdunski,M.,
            Lambeau,G., Gelb,M.H., Matsukura,S., Kokubu,F., Adachi,M. and
            Kudo,I.
  TITLE     Cellular arachidonate-releasing function of novel classes of
            secretory phospholipase A2s (groups III and XII)
  JOURNAL   J Biol Chem 278 (12), 10657-10667 (2003)
   PUBMED   12522102
  REMARK    GeneRIF: cellular arachidonate (AA) release and prostaglandin (PG)
            production are regulated by novel classes of secretory
            phospholipase A(2)s (sPLA(2)s), groups III and XII
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Chowdhury,B., Mantile-Selvaggi,G., Miele,L., Cordella-Miele,E.,
            Zhang,Z. and Mukherjee,A.B.
  TITLE     Lys 43 and Asp 46 in alpha-helix 3 of uteroglobin are essential for
            its phospholipase A2 inhibitory activity
  JOURNAL   Biochem Biophys Res Commun 295 (4), 877-883 (2002)
   PUBMED   12127976
  REMARK    GeneRIF: Lys 43 and Asp 46 in rhUG are critical residues for the
            sPLA2-inhibitory activity of UG
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Valentin,E., Ghomashchi,F., Gelb,M.H., Lazdunski,M. and Lambeau,G.
  TITLE     Novel human secreted phospholipase A(2) with homology to the group
            III bee venom enzyme
  JOURNAL   J Biol Chem 275 (11), 7492-7496 (2000)
   PUBMED   10713052
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF220490.1, AC005005.1 and
            BC025316.1.
            
            On Apr 6, 2007 this sequence version replaced NP_056530.1.
            
            Summary: This gene encodes a protein that belongs to the secreted
            phospholipase A2 family, whose members include the bee venom
            enzyme. The encoded enzyme functions in lipid metabolism and
            catalyzes the calcium-dependent hydrolysis of the sn-2 acyl bond of
            phospholipids to release arachidonic acid and lysophospholipids.
            This enzyme acts as a negative regulator of ciliogenesis, and may
            play a role in cancer development by stimulating tumor cell growth
            and angiogenesis. This gene is associated with oxidative stress,
            and polymorphisms in this gene are linked to risk for Alzheimer's
            disease. [provided by RefSeq, Apr 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025316.1, AF220490.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215885.4/ ENSP00000215885.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..509
                     /product="group 3 secretory phospholipase A2 precursor"
                     /EC_number="3.1.1.4"
                     /note="group III secreted phospholipase A2;
                     phosphatidylcholine 2-acylhydrolase GIII; group 3
                     secretory phospholipase A2; phosphatidylcholine
                     2-acylhydrolase 3"
                     /calculated_mol_wt=55347
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZ20.2)"
                     /calculated_mol_wt=1838
     mat_peptide     20..509
                     /product="Group 3 secretory phospholipase A2.
                     /evidence=ECO:0000255. /id=PRO_0000022992"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZ20.2)"
                     /calculated_mol_wt=55347
     Region          123..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZ20.2)"
     Region          150..291
                     /region_name="Phospholipase A2-like.
                     /evidence=ECO:0000269|PubMed:12522102,
                     ECO:0000269|PubMed:15863501, ECO:0000269|PubMed:17868035"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZ20.2)"
     Region          151..247
                     /region_name="PLA2_bee_venom_like"
                     /note="A sub-family of Phospholipase A2, similar to bee
                     venom PLA2. PLA2 is a super-family of secretory and
                     cytosolic enzymes; the latter are either Ca dependent or
                     Ca independent. Enzymatically active PLA2 cleaves the sn-2
                     position of the glycerol backbone of...; cd04704"
                     /db_xref="CDD:153093"
     Site            order(158,160,162,185)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153093"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15863501; propagated from
                     UniProtKB/Swiss-Prot (Q9NZ20.2)"
     Site            order(184,214,236)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:153093"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15863501; propagated from
                     UniProtKB/Swiss-Prot (Q9NZ20.2)"
     Region          283..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZ20.2)"
     Region          314..427
                     /region_name="PLA2_group_III_like"
                     /note="A sub-family of Phospholipase A2, similar to human
                     group III PLA2. PLA2 is a super-family of secretory and
                     cytosolic enzymes; the latter are either Ca dependent or
                     Ca independent. Enzymatically active PLA2 cleaves the sn-2
                     position of the glycerol...; cd04705"
                     /db_xref="CDD:153094"
     Site            order(321,323,325,369)
                     /site_type="other"
                     /note="putative metal binding site"
                     /db_xref="CDD:153094"
     Site            325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZ20.2)"
     Site            order(367,398)
                     /site_type="active"
                     /note="putative catalytic residues [active]"
                     /db_xref="CDD:153094"
     Site            396
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZ20.2)"
     Site            439
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZ20.2)"
     Region          458..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZ20.2)"
     CDS             1..509
                     /gene="PLA2G3"
                     /gene_synonym="GIII-SPLA2; sPLA2-III; SPLA2III"
                     /coded_by="NM_015715.5:155..1684"
                     /db_xref="CCDS:CCDS13889.1"
                     /db_xref="GeneID:50487"
                     /db_xref="HGNC:HGNC:17934"
                     /db_xref="MIM:611651"
ORIGIN      
        1 mgvqaglfgm lgflgvalgg spalrwyrts chltkavpgn plgylsflak daqglaliha
       61 rwdahrrlqs cswedepelt aaygalcahe tawgsfihtp gpelqralat lqsqweacra
      121 leespagark kraagqsgvp ggghqrekrg wtmpgtlwcg vgdsagnsse lgvfqgpdlc
      181 crehdrcpqn isplqynygi rnyrfhtish cdcdtrfqqc lqnqhdsisd ivgvaffnvl
      241 eipcfvleeq eacvawywwg gcrmygtvpl arlqprtfyn aswssratsp tpssrspapp
      301 kprqkqhlrk gpphqkgskr pskanttalq dpmvsprldv aptglqgpqg glkpqgarwv
      361 crsfrrhldq cehqigprei efqllnsaqe plfhcnctrr larflrlhsp pevtnmlwel
      421 lgttcfklap pldcvegknc srdprairvs arhlrrlqqr rhqlqdkgtd erqpwpsepl
      481 rgpmsfynqc lqltqaarrp drqqkswsq
//
LOCUS       NP_001104611             497 aa            linear   ROD 27-APR-2025
DEFINITION  DNA-dependent metalloprotease SPRTN isoform 1 [Mus musculus].
ACCESSION   NP_001104611 XP_001480505
VERSION     NP_001104611.1
DBSOURCE    REFSEQ: accession NM_001111141.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Erber,L., Groehler,A.S. 4th, Cyuzuzo,C.I., Baker-Wainwright,J.,
            Maskey,R.S., Li,L., Machida,Y.J. and Tretyakova,N.
  TITLE     SPRTN metalloprotease participates in repair of ROS-mediated
            DNA-protein crosslinks
  JOURNAL   Sci Rep 14 (1), 30919 (2024)
   PUBMED   39730693
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Huang,J., Zhou,Q., Gao,M., Nowsheen,S., Zhao,F., Kim,W., Zhu,Q.,
            Kojima,Y., Yin,P., Zhang,Y., Guo,G., Tu,X., Deng,M., Luo,K.,
            Qin,B., Machida,Y. and Lou,Z.
  TITLE     Tandem Deubiquitination and Acetylation of SPRTN Promotes
            DNA-Protein Crosslink Repair and Protects against Aging
  JOURNAL   Mol Cell 79 (5), 824-835 (2020)
   PUBMED   32649882
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Maskey,R.S., Flatten,K.S., Sieben,C.J., Peterson,K.L., Baker,D.J.,
            Nam,H.J., Kim,M.S., Smyrk,T.C., Kojima,Y., Machida,Y., Santiago,A.,
            van Deursen,J.M., Kaufmann,S.H. and Machida,Y.J.
  TITLE     Spartan deficiency causes accumulation of Topoisomerase 1 cleavage
            complexes and tumorigenesis
  JOURNAL   Nucleic Acids Res 45 (8), 4564-4576 (2017)
   PUBMED   28199696
  REMARK    GeneRIF: It has been shown that the livers of Sprtn deficient mice
            accumulate DNA-protein crosslinks containing Topoisomerase 1
            covalently linked to DNA.
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Lopez-Mosqueda,J., Maddi,K., Prgomet,S., Kalayil,S.,
            Marinovic-Terzic,I., Terzic,J. and Dikic,I.
  TITLE     SPRTN is a mammalian DNA-binding metalloprotease that resolves
            DNA-protein crosslinks
  JOURNAL   Elife 5, e21491 (2016)
   PUBMED   27852435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Maskey,R.S., Kim,M.S., Baker,D.J., Childs,B., Malureanu,L.A.,
            Jeganathan,K.B., Machida,Y., van Deursen,J.M. and Machida,Y.J.
  TITLE     Spartan deficiency causes genomic instability and progeroid
            phenotypes
  JOURNAL   Nat Commun 5, 5744 (2014)
   PUBMED   25501849
  REMARK    GeneRIF: The data demonstrate that Spartan plays a key role in
            maintaining structural and numerical chromosome integrity and
            suggest a link between Spartan insufficiency and progeria.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC139158.3.
            
            On Dec 8, 2007 this sequence version replaced XP_001480505.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.1011420.1,
                                           SRR9219381.280394.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 72.83 cM"
     Protein         1..497
                     /product="DNA-dependent metalloprotease SPRTN isoform 1"
                     /note="spartan; protein with SprT-like domain at the N
                     terminus; sprT-like domain-containing protein Spartan;
                     DNA-dependent metalloprotease SPRTN"
                     /calculated_mol_wt=55186
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9H040; propagated from
                     UniProtKB/Swiss-Prot (G3X912.1)"
     Region          44..213
                     /region_name="SprT"
                     /note="SprT homologues; smart00731"
                     /db_xref="CDD:214794"
     Site            228..229
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000250|UniProtKB:Q9H040; propagated from
                     UniProtKB/Swiss-Prot (G3X912.1)"
     Site            231
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9H040; propagated from
                     UniProtKB/Swiss-Prot (G3X912.1)"
     Region          254..262
                     /region_name="SHP-box.
                     /evidence=ECO:0000250|UniProtKB:Q9H040"
                     /note="propagated from UniProtKB/Swiss-Prot (G3X912.1)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H040; propagated from
                     UniProtKB/Swiss-Prot (G3X912.1)"
     Region          326..333
                     /region_name="PIP-box.
                     /evidence=ECO:0000250|UniProtKB:Q9H040"
                     /note="propagated from UniProtKB/Swiss-Prot (G3X912.1)"
     Region          344..459
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3X912.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H040; propagated from
                     UniProtKB/Swiss-Prot (G3X912.1)"
     Region          413..424
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q9H040"
                     /note="propagated from UniProtKB/Swiss-Prot (G3X912.1)"
     Region          <418..>485
                     /region_name="RAD18"
                     /note="RING-finger-containing E3 ubiquitin ligase [Signal
                     transduction mechanisms]; COG5432"
                     /db_xref="CDD:227719"
     Region          462..485
                     /region_name="ZnF_Rad18"
                     /note="Rad18-like CCHC zinc finger; smart00734"
                     /db_xref="CDD:128973"
     CDS             1..497
                     /gene="Sprtn"
                     /gene_synonym="Gm505"
                     /coded_by="NM_001111141.2:265..1758"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS52705.1"
                     /db_xref="GeneID:244666"
                     /db_xref="MGI:MGI:2685351"
ORIGIN      
        1 mdedlvvalr lqeewdvqma rraaaarepv slvdaswelv dptpdlqalf lqfndrffwg
       61 qleavevkws vrmtlcagic tyegrggmcs irlsepllkl rprkdlvetl lhemihaylf
      121 vtnndkdreg hgpefckhmh rinqltgani tvyhtfhdev deyrrhwwrc ngpcqhrqpy
      181 ygyvkratnr apsvhdywwa dhqktcggty ikikepenys kkgrgktkad kqpasavenk
      241 dklcrgeaql lipfsgkgyv lgdastcpsa gklntsymvn eakglssqdh svsglrlnsn
      301 aevkceqncl pkkphlvspl ptashqsvls syfprvsvan qkafrnvngs pvkngttgdg
      361 tkrpasggsq rkvppsrasl rntskvtapa satvtsaagt satisreesg sedqflnkrp
      421 rledrtaldt ikeqtqsggd lrsssqptaa sapqslssqr rlvncpvcqg vvvesqineh
      481 ldrclegnkt nlrprrv
//
LOCUS       NP_694989                563 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 461 isoform 1 [Homo sapiens].
ACCESSION   NP_694989
VERSION     NP_694989.2
DBSOURCE    REFSEQ: accession NM_153257.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Dai,J., Li,Y., Ji,C., Jin,F., Zheng,Z., Wang,X., Sun,X., Xu,X.,
            Gu,S., Xie,Y. and Mao,Y.
  TITLE     Characterization of two novel KRAB-domain-containing zinc finger
            genes, ZNF460 and ZNF461, on human chromosome 19q13.1-->q13.4
  JOURNAL   Cytogenet Genome Res 103 (1-2), 74-78 (2003)
   PUBMED   15004467
  REMARK    GeneRIF: Molecular cloning and tissue distribution of ZNF461.
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Mizutani,T., Yamada,K., Yazawa,T., Okada,T., Minegishi,T. and
            Miyamoto,K.
  TITLE     Cloning and characterization of gonadotropin-inducible ovarian
            transcription factors (GIOT1 and -2) that are novel members of the
            (Cys)(2)-(His)(2)-type zinc finger protein family
  JOURNAL   Mol Endocrinol 15 (10), 1693-1705 (2001)
   PUBMED   11579202
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK299370.1, AY329493.1, AB021641.1 and AC074138.5.
            
            On Apr 14, 2004 this sequence version replaced NP_694989.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY329493.1, SRR1803614.97950.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000588268.6/ ENSP00000467931.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..563
                     /product="zinc finger protein 461 isoform 1"
                     /note="gonadotropin-inducible ovary transcription
                     repressor 1; zinc finger protein 28"
                     /calculated_mol_wt=66083
     Region          6..66
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          248..267
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          275..295
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          287..312
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          303..323
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(308,310,312,314..315,318..319,322,336,338,342..343,
                     346..347,350,364,366,368,370..371,374..375,378)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <312..515
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          331..351
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          359..379
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          387..407
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          415..435
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          443..463
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(448,450,452,454..455,458..459,462,476,478,482..483,
                     486..487,490,504,506,508,510..511,514..515,518)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          471..491
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          499..519
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          527..544
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..563
                     /gene="ZNF461"
                     /gene_synonym="GIOT-1; GIOT1; HZF28"
                     /coded_by="NM_153257.5:229..1920"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54257.1"
                     /db_xref="GeneID:92283"
                     /db_xref="HGNC:HGNC:21629"
                     /db_xref="MIM:608640"
ORIGIN      
        1 mahelvmfrd vaidvsqeew eclnpaqrnl ykevmlenys nlvslglsvs kpavissleq
       61 gkepwmvvre etgrwcpgtw ktwgfhnnfl dnneatdina dlasrdepqk lspkrdiyet
      121 elsqwvnmee fkshspersi fsaiwegnch feqhqgqeeg yfrqlminhe nmpifsqhtl
      181 ltqefydrek iseckkcrki fsyhlffshh krthskelse ckecteivnt pclfkqqtiq
      241 ngdkcnecke cwkafvhcsq lkhlrihnge kryecnecgk afnygseltl hqrihtgekp
      301 yeckecgkaf rqrsqltqhq rlhtgekpye ckqcgkafir gfqltehlrl htgekpyeck
      361 ecgktfrhrs hltihqriht gekpyecrec gkafsyhssf shhqkihsgk kpyechecgk
      421 afcdglqltl hqrihtgekp yeckecgktf rqcshlkrhq rihtgekphe cmicgkafrl
      481 hshliqhqri htgekpyeck ecgkafsyhs sfshhqrihs gkkpyqcgka fnhrlqlnlh
      541 qtlhtgekpv rfpllpphps las
//
LOCUS       NP_001352709             251 aa            linear   PRI 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.11br [Homo sapiens].
ACCESSION   NP_001352709 XP_005254704
VERSION     NP_001352709.1
DBSOURCE    REFSEQ: accession NM_001365780.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Man,Y., Yi,C., Fan,M., Yang,T., Liu,P., Liu,S. and Wang,G.
  TITLE     Identification of a novel missense mutation in the TPM1 gene via
            exome sequencing in a Chinese family with dilated cardiomyopathy: A
            case report and literature review
  JOURNAL   Medicine (Baltimore) 101 (2), e28551 (2022)
   PUBMED   35029218
  REMARK    GeneRIF: Identification of a novel missense mutation in the TPM1
            gene via exome sequencing in a Chinese family with dilated
            cardiomyopathy: A case report and literature review.
            Review article
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 251)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 251)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 251)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On Sep 12, 2018 this sequence version replaced XP_005254704.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.281224.1,
                                           SRR3476690.167754.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..251
                     /product="tropomyosin alpha-1 chain isoform Tpm1.11br"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=28692
     Region          12..223
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..251
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001365780.1:88..843"
                     /note="isoform Tpm1.11br is encoded by transcript variant
                     TmBr2"
                     /db_xref="CCDS:CCDS92013.1"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeeragt lqreldherk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egkcaeleee lktvtnnlks leaqaekysq
      181 kedryeeeik vlsdklkeae traefaersv tkleksiddl edkflcftsp ktpssswmsh
      241 lselciclfs s
//
LOCUS       NP_003275                 55 aa            linear   PRI 27-APR-2025
DEFINITION  spermatid nuclear transition protein 1 [Homo sapiens].
ACCESSION   NP_003275
VERSION     NP_003275.1
DBSOURCE    REFSEQ: accession NM_003284.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 55)
  AUTHORS   Amor,H., Zeyad,A. and Hammadeh,M.E.
  TITLE     Tobacco smoking and its impact on the expression level of sperm
            nuclear protein genes: H2BFWT, TNP1, TNP2, PRM1 and PRM2
  JOURNAL   Andrologia 53 (3), e13964 (2021)
   PUBMED   33440036
  REMARK    GeneRIF: Tobacco smoking and its impact on the expression level of
            sperm nuclear protein genes: H2BFWT, TNP1, TNP2, PRM1 and PRM2.
REFERENCE   2  (residues 1 to 55)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 55)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 55)
  AUTHORS   Onishi,S., Adnan,E., Ishizaki,J., Miyazaki,T., Tanaka,Y.,
            Matsumoto,T., Suemori,K., Shudou,M., Okura,T., Takeda,H.,
            Sawasaki,T., Yasukawa,M. and Hasegawa,H.
  TITLE     Novel Autoantigens Associated with Lupus Nephritis
  JOURNAL   PLoS One 10 (6), e0126564 (2015)
   PUBMED   26098692
  REMARK    GeneRIF: Among Systemic lupus erythematosus patients, 63.6% and
            45.5% of those with lupus nephritis were positive for anti-RRP8 and
            anti-TNP1 antibodies, compared with 12.5% and 9.4% of Systemic
            lupus erythematosus patients without nephritis, respectively.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 55)
  AUTHORS   Geller,F., Feenstra,B., Zhang,H., Shaffer,J.R., Hansen,T.,
            Esserlind,A.L., Boyd,H.A., Nohr,E.A., Timpson,N.J., Fatemifar,G.,
            Paternoster,L., Evans,D.M., Weyant,R.J., Levy,S.M., Lathrop,M.,
            Smith,G.D., Murray,J.C., Olesen,J., Werge,T., Marazita,M.L.,
            Sorensen,T.I. and Melbye,M.
  TITLE     Genome-wide association study identifies four loci associated with
            eruption of permanent teeth
  JOURNAL   PLoS Genet 7 (9), e1002275 (2011)
   PUBMED   21931568
REFERENCE   6  (residues 1 to 55)
  AUTHORS   Chirat,F., Martinage,A., Briand,G., Kouach,M., Van Dorsselaer,A.,
            Loir,M. and Sautiere,P.
  TITLE     Nuclear transition protein 1 from ram elongating spermatids. Mass
            spectrometric characterization, primary structure and
            phosphorylation sites of two variants
  JOURNAL   Eur J Biochem 198 (1), 13-20 (1991)
   PUBMED   2040274
REFERENCE   7  (residues 1 to 55)
  AUTHORS   Baskaran,R. and Rao,M.R.
  TITLE     Interaction of spermatid-specific protein TP2 with nucleic acids,
            in vitro. A comparative study with TP1
  JOURNAL   J Biol Chem 265 (34), 21039-21047 (1990)
   PUBMED   2250010
REFERENCE   8  (residues 1 to 55)
  AUTHORS   Luerssen,H., Mattei,M.G., Schroter,M., Grzeschik,K.H., Adham,I.M.
            and Engel,W.
  TITLE     Nucleotide sequence of the gene for human transition protein 1 and
            its chromosomal localization on chromosome 2
  JOURNAL   Genomics 8 (2), 324-330 (1990)
   PUBMED   2249851
REFERENCE   9  (residues 1 to 55)
  AUTHORS   Luerssen,H., Hoyer-Fender,S. and Engel,W.
  TITLE     The nucleotide sequence of human transition protein 1 cDNA
  JOURNAL   Nucleic Acids Res 16 (15), 7723 (1988)
   PUBMED   3412903
REFERENCE   10 (residues 1 to 55)
  AUTHORS   Kleene,K.C., Borzorgzadeh,A., Flynn,J.F., Yelick,P.C. and
            Hecht,N.B.
  TITLE     Nucleotide sequence of a cDNA clone encoding mouse transition
            protein 1
  JOURNAL   Biochim Biophys Acta 950 (2), 215-220 (1988)
   PUBMED   3382664
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007557.3 and BC029516.1.
            
            Summary: Transition protein-1 is a spermatid-specific product of
            the haploid genome which replaces histone and is itself replaced in
            the mature sperm by the protamines (see PRM1, MIM 182880; PRM2, MIM
            182890) (Luerssen et al., 1990 [PubMed 2249851]).[supplied by OMIM,
            Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU569792.1, BP371302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000236979.2/ ENSP00000236979.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..55
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..55
                     /product="spermatid nuclear transition protein 1"
                     /note="TP-1; STP-1; transition protein 1 (during histone
                     to protamine replacement)"
                     /calculated_mol_wt=6293
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09430.2)"
     Region          1..51
                     /region_name="TP1"
                     /note="Nuclear transition protein 1; pfam02079"
                     /db_xref="CDD:460439"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P22613; propagated from
                     UniProtKB/Swiss-Prot (P09430.2)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P22613; propagated from
                     UniProtKB/Swiss-Prot (P09430.2)"
     CDS             1..55
                     /gene="TNP1"
                     /gene_synonym="TP1"
                     /coded_by="NM_003284.4:31..198"
                     /db_xref="CCDS:CCDS2406.1"
                     /db_xref="GeneID:7141"
                     /db_xref="HGNC:HGNC:11951"
                     /db_xref="MIM:190231"
ORIGIN      
        1 mstsrklksh gmrrsksrsp hkgvkrggsk rkyrkgnlks rkrgddanrn yrshl
//
LOCUS       NP_859057                149 aa            linear   PRI 27-APR-2025
DEFINITION  dnaJ homolog subfamily C member 24 [Homo sapiens].
ACCESSION   NP_859057
VERSION     NP_859057.4
DBSOURCE    REFSEQ: accession NM_181706.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Liu,D., Zuo,R., Liu,W., He,Y., Wang,Y., Yue,P., Gong,W., Cui,J.,
            Zhu,F., Luo,Y., Qi,L., Guo,Y., Chen,L., Li,G., Liu,Z., Chen,P. and
            Guo,H.
  TITLE     DNAJC24 acts directly with PCNA and promotes malignant progression
            of LUAD by activating phosphorylation of AKT
  JOURNAL   FASEB J 38 (9), e23630 (2024)
   PUBMED   38713100
  REMARK    GeneRIF: DNAJC24 acts directly with PCNA and promotes malignant
            progression of LUAD by activating phosphorylation of AKT.
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Hoffmann,T.J., Tang,H., Thornton,T.A., Caan,B., Haan,M.,
            Millen,A.E., Thomas,F. and Risch,N.
  TITLE     Genome-wide association and admixture analysis of glaucoma in the
            Women's Health Initiative
  JOURNAL   Hum Mol Genet 23 (24), 6634-6643 (2014)
   PUBMED   25027321
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Wei,H., Xiang,L., Wayne,A.S., Chertov,O., FitzGerald,D.J.,
            Bera,T.K. and Pastan,I.
  TITLE     Immunotoxin resistance via reversible methylation of the DPH4
            promoter is a unique survival strategy
  JOURNAL   Proc Natl Acad Sci U S A 109 (18), 6898-6903 (2012)
   PUBMED   22509046
  REMARK    GeneRIF: immunotoxin resistance is associated with reversible CpG
            island methylation and silencing of DPH4 gene transcription
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Thakur,A., Chitoor,B., Goswami,A.V., Pareek,G., Atreya,H.S. and
            D'Silva,P.
  TITLE     Structure and mechanistic insights into novel iron-mediated
            moonlighting functions of human J-protein cochaperone, Dph4
  JOURNAL   J Biol Chem 287 (16), 13194-13205 (2012)
   PUBMED   22367199
  REMARK    GeneRIF: We report here the solution structure and mechanism of
            novel iron-mediated functional roles of human Dph4, a type III
            J-protein playing a vital role in diphthamide biosynthesis and
            normal development.
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Liu,S., Milne,G.T., Kuremsky,J.G., Fink,G.R. and Leppla,S.H.
  TITLE     Identification of the proteins required for biosynthesis of
            diphthamide, the target of bacterial ADP-ribosylating toxins on
            translation elongation factor 2
  JOURNAL   Mol Cell Biol 24 (21), 9487-9497 (2004)
   PUBMED   15485916
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL833128.1 and AC108456.7.
            
            On Mar 2, 2006 this sequence version replaced NP_859057.3.
            
            Summary: Diphthamide is a unique posttranslationally modified
            histidine found only in translation elongation factor-2 (EEF2; MIM
            130610). This modification is conserved from archaebacteria to
            humans and serves as the target for ADP-ribosylation and
            inactivation of EEF2 by diphtheria toxin (DT) and Pseudomonas
            exotoxin A. DPH4 is 1 of several enzymes involved in synthesis of
            diphthamide in EEF2 (Liu et al., 2004 [PubMed 15485916]).[supplied
            by OMIM, Mar 2008].
            
            CCDS Note: This CCDS representation uses the 5'-most in-frame start
            codon, which is conserved in other species. An alternative
            downstream start codon, which has a stronger Kozak signal, also
            exists. It is possible that leaky scanning by ribosomes would allow
            the downstream start codon to be used, at least some of the time.
            The use of the downstream start codon would result in a protein
            that is 1 aa shorter at the N-terminus. There is no experimental
            evidence showing which start codon is preferentially used in vivo.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA659255.1, SRR3476690.655970.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000465995.6/ ENSP00000417548.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..149
                     /product="dnaJ homolog subfamily C member 24"
                     /note="zinc finger, CSL domain containing 3;
                     1700030A21Rik; DPH4 homolog (JJJ3, S. cerevisiae); zinc
                     finger, CSL-type containing 3; diphthamide biosynthesis
                     protein 4; CSL-type zinc finger-containing protein 3;
                     DPH4, JJJ3 homolog; DnaJ (Hsp40) homolog, subfamily C,
                     member 24"
                     /calculated_mol_wt=17008
     Region          11..79
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(39..41,56,59..60,63..64)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     Region          95..148
                     /region_name="zf-CSL"
                     /note="CSL zinc finger; pfam05207"
                     /db_xref="CDD:398744"
     CDS             1..149
                     /gene="DNAJC24"
                     /gene_synonym="DPH4; JJJ3; ZCSL3"
                     /coded_by="NM_181706.5:87..536"
                     /db_xref="CCDS:CCDS7873.2"
                     /db_xref="GeneID:120526"
                     /db_xref="HGNC:HGNC:26979"
                     /db_xref="MIM:611072"
ORIGIN      
        1 mmaveqmpkk dwysilgadp sanisdlkqk yqklilmyhp dkqstdvpag tveecvqkfi
       61 eidqawkilg neetkreydl qrceddlrnv gpvdaqvyle emswnegdhs fylscrcggk
      121 ysvskdeaee vsliscdtcs liiellhyn
//
LOCUS       NP_001354490            2140 aa            linear   PRI 27-APR-2025
DEFINITION  dedicator of cytokinesis protein 7 isoform 7 [Homo sapiens].
ACCESSION   NP_001354490 XP_011540628
VERSION     NP_001354490.1
DBSOURCE    REFSEQ: accession NM_001367561.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2140)
  AUTHORS   Chen,W., Zhou,M., Guan,B., Xie,B., Liu,Y., He,J., Zhao,J., Zhao,Q.
            and Yan,D.
  TITLE     Tumour-associated macrophage-derived DOCK7-enriched extracellular
            vesicles drive tumour metastasis in colorectal cancer via the
            RAC1/ABCA1 axis
  JOURNAL   Clin Transl Med 14 (2), e1591 (2024)
   PUBMED   38385857
  REMARK    GeneRIF: Tumour-associated macrophage-derived DOCK7-enriched
            extracellular vesicles drive tumour metastasis in colorectal cancer
            via the RAC1/ABCA1 axis.
REFERENCE   2  (residues 1 to 2140)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 2140)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 2140)
  AUTHORS   Gao,M., Guo,G., Huang,J., Hou,X., Ham,H., Kim,W., Zhao,F., Tu,X.,
            Zhou,Q., Zhang,C., Zhu,Q., Liu,J., Yan,Y., Xu,Z., Yin,P., Luo,K.,
            Weroha,J., Deng,M., Billadeau,D.D. and Lou,Z.
  TITLE     DOCK7 protects against replication stress by promoting RPA
            stability on chromatin
  JOURNAL   Nucleic Acids Res 49 (6), 3322-3337 (2021)
   PUBMED   33704464
  REMARK    GeneRIF: DOCK7 protects against replication stress by promoting RPA
            stability on chromatin.
REFERENCE   5  (residues 1 to 2140)
  AUTHORS   Haberlandt,E., Valovka,T., Janjic,T., Muller,T., Blatsios,G.,
            Karall,D. and Janecke,A.R.
  TITLE     Characteristic facial features and cortical blindness distinguish
            the DOCK7-related epileptic encephalopathy
  JOURNAL   Mol Genet Genomic Med 9 (3), e1607 (2021)
   PUBMED   33471954
  REMARK    GeneRIF: Characteristic facial features and cortical blindness
            distinguish the DOCK7-related epileptic encephalopathy.
REFERENCE   6  (residues 1 to 2140)
  AUTHORS   Nellist,M., Burgers,P.C., van den Ouweland,A.M., Halley,D.J. and
            Luider,T.M.
  TITLE     Phosphorylation and binding partner analysis of the TSC1-TSC2
            complex
  JOURNAL   Biochem Biophys Res Commun 333 (3), 818-826 (2005)
   PUBMED   15963462
REFERENCE   7  (residues 1 to 2140)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 2140)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   9  (residues 1 to 2140)
  AUTHORS   Cote,J.F. and Vuori,K.
  TITLE     Identification of an evolutionarily conserved superfamily of
            DOCK180-related proteins with guanine nucleotide exchange activity
  JOURNAL   J Cell Sci 115 (Pt 24), 4901-4913 (2002)
   PUBMED   12432077
REFERENCE   10 (residues 1 to 2140)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC103923.2, AL138847.14,
            AL451044.7 and AC096946.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 8, 2018 this sequence version replaced XP_011540628.1.
            
            Summary: The protein encoded by this gene is a guanine nucleotide
            exchange factor (GEF) that plays a role in axon formation and
            neuronal polarization. The encoded protein displays GEF activity
            toward RAC1 and RAC3 Rho small GTPases but not toward CDC42.
            Several transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Dec 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000635253.2/ ENSP00000489124.1
            RefSeq Select criteria    :: based on manual assertion,
                                         conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..2140
                     /product="dedicator of cytokinesis protein 7 isoform 7"
                     /note="dedicator of cytokinesis protein 7"
                     /calculated_mol_wt=242431
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          52..161
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          138..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            381
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          560..737
                     /region_name="C2_Dock-C"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08696"
                     /db_xref="CDD:176078"
     Site            862
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          888..971
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            888
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            905
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            907
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            909
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            910
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            929
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            964
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          1644..2118
                     /region_name="DHR2_DOCK7"
                     /note="Dock Homology Region 2, a GEF domain, of Class C
                     Dedicator of Cytokinesis 7; cd11703"
                     /db_xref="CDD:212576"
     Site            order(1799,1809,1811..1812,1814..1815,1818..1819,
                     1821..1822,1825..1826)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212576"
     Site            order(1841,1843,1866,1869..1872,1874..1875,1894..1896,
                     1913..1915,1943..1946,1956..1957,1960,1962,1999..2000,
                     2003,2019..2020,2022..2023,2026..2028,2031..2033,
                     2036..2037,2040,2068,2090,2093)
                     /site_type="other"
                     /note="Rac/Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212576"
     Site            1962
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            2031..2036
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212576"
     Site            2129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     CDS             1..2140
                     /gene="DOCK7"
                     /gene_synonym="DEE23; EIEE23; ZIR2"
                     /coded_by="NM_001367561.1:123..6545"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS90964.1"
                     /db_xref="GeneID:85440"
                     /db_xref="HGNC:HGNC:19190"
                     /db_xref="MIM:615730"
ORIGIN      
        1 maerrafaqk isrtvaaevr kqisgqysgs pqllknlniv gnishhttvp lteavdpvdl
       61 edylithpla vdsgplrdli efppddievv ysprdcrtlv savpeesemd phvrdcirsy
      121 tedwaivirk yhklgtgfnp ntldkqkerq kglpkqvfes deapdgnsyq ddqddlkrrs
      181 msiddtprgs wacsifdlkn slpdallpnl ldrtpneeid rqnddqrksn rhkelfalhp
      241 spdeeepier lsvpdipkeh fgqrllvkcl slkfeieiep ifaslalydv kekkkisenf
      301 yfdlnseqmk gllrphvppa aittlarsai fsitypsqdv flviklekvl qqgdigecae
      361 pymifkeada tknkeklekl ksqadqfcqr lgkyrmpfaw taihlmnivs sagslerdst
      421 eveistgerk gswserrnss ivgrrslert tsgddacnlt sfrpatltvt nffkqegdrl
      481 sdedlykfla dmrrpssvlr rlrpitaqlk idispapenp hycltpellq vklypdsrvr
      541 ptreilefpa rdvyvpntty rnllyiypqs lnfanrqgsa rnitvkvqfm ygedpsnamp
      601 vifgksscse fskeaytavv yhnrspdfhe eikvklpatl tdhhhllftf yhvscqqkqn
      661 tpletpvgyt wipmlqngrl ktgqfclpvs lekppqaysv lspevplpgm kwvdnhkgvf
      721 nvevvavssi htqdpyldkf falvnaldeh lfpvrigdmr imennlenel kssisalnss
      781 qlepvvrflh llldklillv irppviagqi vnlgqasfea masiinrlhk nlegnhdqhg
      841 rnsllasyih yvfrlpntyp nssspgpggl ggsvhyatma rsavrpasln lnrsrslsns
      901 npdisgtpts pddevrsiig skgldrsnsw vntggpkaap wgsnpspsae stqamdrscn
      961 rmsshtetss flqtltgrlp tkklfheela lqwvvcsgsv resalqqawf ffelmvksmv
     1021 hhlyfndkle aprksrfper fmddiaalvs tiasdivsrf qkdtemverl ntslafflnd
     1081 llsvmdrgfv fslikscykq vssklyslpn psvlvslrld flriicsheh yvtlnlpcsl
     1141 ltppaspsps vssatsqssg fstnvqdqki anmfelsvpf rqqhylaglv ltelavildp
     1201 daeglfglhk kvinmvhnll sshdsdprys dpqikarvam lylpligiim etvpqlydft
     1261 ethnqrgrpi ciatddyese sgsmisqtva maiagtsvpq ltrpgsfllt stsgrqhttf
     1321 saessrslli cllwvlknad etvlqkwftd lsvlqlnrll dllylcvscf eykgkkvfer
     1381 mnsltfkksk dmrakleeai lgsigarqem vrrsrgqlgt ytiasppers psgsafgsqe
     1441 nlrwrkdmth wrqntekldk sraeieheal idgnlatean liildtleiv vqtvsvtesk
     1501 esilggvlkv llhsmacnqs avylqhcfat qralvskfpe llfeeeteqc adlclrllrh
     1561 csssigtirs hasaslyllm rqnfeignnf arvkmqvtms lsslvgtsqn fneeflrrsl
     1621 ktiltyaeed lelrettfpd qvqdlvfnlh milsdtvkmk ehqedpemli dlmyriakgy
     1681 qtspdlrltw lqnmagkhse rsnhaeaaqc lvhsaalvae ylsmledrky lpvgcvtfqn
     1741 issnvleesa vsddvvspde egicsgkyft esglvglleq aaasfsmagm yeavnevykv
     1801 lipiheanrd akklstihgk lqeafskivh qstgwermfg tyfrvgfygt kfgdldeqef
     1861 vykepaitkl aeishrlegf ygerfgedvv evikdsnpvd kckldpnkay iqityvepyf
     1921 dtyemkdrit yfdknynlrr fmyctpftld grahgelheq fkrktiltts hafpyiktrv
     1981 nvthkeeiil tpievaiedm qkktqelafa thqdpadpkm lqmvlqgsvg ttvnqgplev
     2041 aqvflseips dpklfrhhnk lrlcfkdftk rcedalrknk sligpdqkey qrelernyhr
     2101 lkealqplin rkipqlykav lpvtchrdsf srmslrkmdl
//
LOCUS       NP_000974                128 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein eL22 [Homo sapiens].
ACCESSION   NP_000974
VERSION     NP_000974.1
DBSOURCE    REFSEQ: accession NM_000983.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Li,H.Y., Wang,M., Jiang,X., Jing,Y., Wu,Z., He,Y., Yan,K., Sun,S.,
            Ma,S., Ji,Z., Wang,S., Belmonte,J.C.I., Qu,J., Zhang,W., Wei,T. and
            Liu,G.H.
  TITLE     CRISPR screening uncovers nucleolar RPL22 as a heterochromatin
            destabilizer and senescence driver
  JOURNAL   Nucleic Acids Res 52 (19), 11481-11499 (2024)
   PUBMED   39258545
  REMARK    GeneRIF: CRISPR screening uncovers nucleolar RPL22 as a
            heterochromatin destabilizer and senescence driver.
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Cheng,J., Sha,Z., Zhang,R., Ge,J., Chen,P., Kuang,X., Chang,J.,
            Ren,K., Luo,X., Chen,S. and Gou,X.
  TITLE     L22 ribosomal protein is involved in dynamin-related protein
            1-mediated gastric carcinoma progression
  JOURNAL   Bioengineered 13 (3), 6650-6664 (2022)
   PUBMED   35230214
  REMARK    GeneRIF: L22 ribosomal protein is involved in dynamin-related
            protein 1-mediated gastric carcinoma progression.
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Zeng,J., Zhang,Y., Zhang,H., Zhang,Y., Gao,L., Tong,X., Xie,Y.,
            Hu,Q., Chen,C., Ding,S. and Lu,J.
  TITLE     RPL22 Overexpression Promotes Psoriasis-Like Lesion by Inducing
            Keratinocytes Abnormal Biological Behavior
  JOURNAL   Front Immunol 12, 699900 (2021)
   PUBMED   34220863
  REMARK    GeneRIF: RPL22 Overexpression Promotes Psoriasis-Like Lesion by
            Inducing Keratinocytes Abnormal Biological Behavior.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Shu-Nu,C., Lin,C.H. and Lin,A.
  TITLE     An acidic amino acid cluster regulates the nucleolar localization
            and ribosome assembly of human ribosomal protein L22
  JOURNAL   FEBS Lett 484 (1), 22-28 (2000)
   PUBMED   11056215
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Le,S., Sternglanz,R. and Greider,C.W.
  TITLE     Identification of two RNA-binding proteins associated with human
            telomerase RNA
  JOURNAL   Mol Biol Cell 11 (3), 999-1010 (2000)
   PUBMED   10712515
REFERENCE   8  (residues 1 to 128)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   9  (residues 1 to 128)
  AUTHORS   Fujita,Y., Okamoto,T., Noshiro,M., McKeehan,W.L., Crabb,J.W.,
            Whitney,R.G., Kato,Y., Sato,J.D. and Takada,K.
  TITLE     A novel heparin-binding protein, HBp15, is identified as mammalian
            ribosomal protein L22
  JOURNAL   Biochem Biophys Res Commun 199 (2), 706-713 (1994)
   PUBMED   8135813
REFERENCE   10 (residues 1 to 128)
  AUTHORS   Toczyski,D.P. and Steitz,J.A.
  TITLE     EAP, a highly conserved cellular protein associated with
            Epstein-Barr virus small RNAs (EBERs)
  JOURNAL   EMBO J 10 (2), 459-466 (1991)
   PUBMED   1846807
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from CA336134.1, AK097075.1 and AF113701.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a cytoplasmic
            ribosomal protein that is a component of the 60S subunit. The
            protein belongs to the L22E family of ribosomal proteins. Its
            initiating methionine residue is post-translationally removed. The
            protein can bind specifically to Epstein-Barr virus-encoded RNAs
            (EBERs) 1 and 2. The mouse protein has been shown to be capable of
            binding to heparin. Transcript variants utilizing alternative polyA
            signals exist. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            through the genome. It was previously thought that this gene mapped
            to 3q26 and that it was fused to the acute myeloid leukemia 1
            (AML1) gene located at 21q22 in some therapy-related
            myelodysplastic syndrome patients with 3;21 translocations;
            however, these fusions actually involve a ribosomal protein L22
            pseudogene located at 3q26, and this gene actually maps to
            1p36.3-p36.2. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.436838.1,
                                           SRR3476690.1039763.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000234875.9/ ENSP00000346088.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.31"
     Protein         1..128
                     /product="large ribosomal subunit protein eL22"
                     /EC_number="2.1.1.100"
                     /note="60S ribosomal protein L22; Epstein-Barr-encoded
                     RNA-associated protein; Epstein-Barr virus small
                     RNA-associated protein; EBER-associated protein;
                     heparin-binding protein 15; heparin-binding protein HBp15"
                     /calculated_mol_wt=14656
     Region          21..119
                     /region_name="Ribosomal_L22e"
                     /note="Ribosomal L22e protein family; pfam01776"
                     /db_xref="CDD:460321"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P67984; propagated from
                     UniProtKB/Swiss-Prot (P35268.2)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35268.2)"
     CDS             1..128
                     /gene="RPL22"
                     /gene_synonym="EAP; eL22; HBP15; HBP15/L22; L22"
                     /coded_by="NM_000983.4:23..409"
                     /db_xref="CCDS:CCDS58.1"
                     /db_xref="GeneID:6146"
                     /db_xref="HGNC:HGNC:10315"
                     /db_xref="MIM:180474"
ORIGIN      
        1 mapvkklvvk ggkkkkqvlk ftldcthpve dgimdaanfe qflqerikvn gkagnlgggv
       61 vtierskski tvtsevpfsk rylkyltkky lkknnlrdwl rvvanskesy elryfqinqd
      121 eeeeeded
//
LOCUS       NP_001353290             131 aa            linear   PRI 27-APR-2025
DEFINITION  androgen-induced gene 1 protein isoform v [Homo sapiens].
ACCESSION   NP_001353290
VERSION     NP_001353290.1
DBSOURCE    REFSEQ: accession NM_001366361.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Nakada-Tsukui,K., Sekizuka,T., Sato-Ebine,E., Escueta-de Cadiz,A.,
            Ji,D.D., Tomii,K., Kuroda,M. and Nozaki,T.
  TITLE     AIG1 affects in vitro and in vivo virulence in clinical isolates of
            Entamoeba histolytica
  JOURNAL   PLoS Pathog 14 (3), e1006882 (2018)
   PUBMED   29554130
  REMARK    GeneRIF: High AIG1 expression is associated with virulence in
            clinical isolates of Entamoeba histolytica.
            Erratum:[PLoS Pathog. 2018 May 31;14(5):e1007091. doi:
            10.1371/journal.ppat.1007091. PMID: 29851996]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Parsons,W.H., Kolar,M.J., Kamat,S.S., Cognetta,A.B. 3rd,
            Hulce,J.J., Saez,E., Kahn,B.B., Saghatelian,A. and Cravatt,B.F.
  TITLE     AIG1 and ADTRP are atypical integral membrane hydrolases that
            degrade bioactive FAHFAs
  JOURNAL   Nat Chem Biol 12 (5), 367-372 (2016)
   PUBMED   27018888
  REMARK    GeneRIF: These results indicate that AIG1 and ADTRP are founding
            members of an evolutionarily conserved class of transmembrane
            threonine hydrolases involved in bioactive lipid metabolism.
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 131)
  AUTHORS   Wu,G., Sun,M., Zhang,W. and Huo,K.
  TITLE     AIG1 is a novel Pirh2-interacting protein that activates the NFAT
            signaling pathway
  JOURNAL   Front Biosci (Elite Ed) 3 (3), 834-842 (2011)
   PUBMED   21622095
  REMARK    GeneRIF: identified a novel Pirh2-interacting protein, AIG1, by
            yeast two-hybrid screening and confirmed its interaction with p53
            both in vitro and in vivo
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 131)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   8  (residues 1 to 131)
  AUTHORS   Seo,J., Kim,J. and Kim,M.
  TITLE     Cloning of androgen-inducible gene 1 (AIG1) from human dermal
            papilla cells
  JOURNAL   Mol Cells 11 (1), 35-40 (2001)
   PUBMED   11266118
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL391726.8 and AL136116.11.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.25260.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.2"
     Protein         1..131
                     /product="androgen-induced gene 1 protein isoform v"
                     /note="androgen-induced gene 1 protein; FAHFA hydrolase
                     AIG1; fatty acid esters of hydroxy fatty acids hydrolase
                     AIG1"
                     /calculated_mol_wt=15122
     Region          <1..105
                     /region_name="Far-17a_AIG1"
                     /note="FAR-17a/AIG1-like protein; pfam04750"
                     /db_xref="CDD:428104"
     CDS             1..131
                     /gene="AIG1"
                     /gene_synonym="AIG-1; dJ95L4.1"
                     /coded_by="NM_001366361.1:159..554"
                     /note="isoform v is encoded by transcript variant 22"
                     /db_xref="GeneID:51390"
                     /db_xref="HGNC:HGNC:21607"
                     /db_xref="MIM:608514"
ORIGIN      
        1 miypklldnf ipgwlnhgmh ttvlpfilie mrtshhqyps rssgltaict fsvgyilwvc
       61 wvhhvtgmwv ypflehigpg ariiffgstt ilmnflyllg evlnnyiwdt qkkppswqdm
      121 kikfmylgps s
//
LOCUS       NP_116169                366 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 25 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_116169
VERSION     NP_116169.2
DBSOURCE    REFSEQ: accession NM_032780.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Xi,P., Zhang,Z., Liu,Y., Nie,Y., Gong,B., Liu,J., Huang,H., Liu,Z.,
            Sun,T. and Xie,W.
  TITLE     Multidimensional comprehensive and integrated analysis of the
            potential function of TMEM25 in renal clear cell carcinoma with low
            expression status
  JOURNAL   Aging (Albany NY) 16 (1), 367-388 (2024)
   PUBMED   38189809
  REMARK    GeneRIF: Multidimensional comprehensive and integrated analysis of
            the potential function of TMEM25 in renal clear cell carcinoma with
            low expression status.
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Kamakura,S., Hayase,J., Kohda,A., Iwakiri,Y., Chishiki,K., Izaki,T.
            and Sumimoto,H.
  TITLE     TMEM25 is a Par3-binding protein that attenuates claudin assembly
            during tight junction development
  JOURNAL   EMBO Rep 25 (1), 144-167 (2024)
   PUBMED   38177906
  REMARK    GeneRIF: TMEM25 is a Par3-binding protein that attenuates claudin
            assembly during tight junction development.
REFERENCE   3  (residues 1 to 366)
  AUTHORS   An,B., Ando,A., Akuta,H., Morishita,F. and Imamura,T.
  TITLE     Human-biased TMEM25 expression promotes expansion of neural
            progenitor cells to alter cortical structure in the developing
            brain
  JOURNAL   FEBS Lett 597 (21), 2611-2625 (2023)
   PUBMED   37846797
  REMARK    GeneRIF: Human-biased TMEM25 expression promotes expansion of
            neural progenitor cells to alter cortical structure in the
            developing brain.
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Zhang,H., Tian,X., Lu,X., Xu,D., Guo,Y., Dong,Z., Li,Y., Ma,Y.,
            Chen,C., Yang,Y., Yang,M., Yang,Y., Liu,F., Zhou,R., He,M., Xiao,F.
            and Wang,X.
  TITLE     TMEM25 modulates neuronal excitability and NMDA receptor subunit
            NR2B degradation
  JOURNAL   J Clin Invest 129 (9), 3864-3876 (2019)
   PUBMED   31424425
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Hrasovec,S., Hauptman,N., Glavac,D., Jelenc,F. and Ravnik-Glavac,M.
  TITLE     TMEM25 is a candidate biomarker methylated and down-regulated in
            colorectal cancer
  JOURNAL   Dis Markers 34 (2), 93-104 (2013)
   PUBMED   23324576
  REMARK    GeneRIF: TMEM25 hypermethylation might play a significant role in
            altering expression of this gene in colorectal cancer.
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Doolan,P., Clynes,M., Kennedy,S., Mehta,J.P., Germano,S.,
            Ehrhardt,C., Crown,J. and O'Driscoll,L.
  TITLE     TMEM25, REPS2 and Meis 1: favourable prognostic and predictive
            biomarkers for breast cancer
  JOURNAL   Tumour Biol 30 (4), 200-209 (2009)
   PUBMED   19776672
  REMARK    GeneRIF: TMEM25 may be a useful tumor marker for favorable
            prognosis in breast cancer.
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of human TMEM25 and mouse
            Tmem25 genes in silico
  JOURNAL   Oncol Rep 12 (2), 429-433 (2004)
   PUBMED   15254712
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF513120.1, BC042896.1 and AP000941.6.
            
            On Jun 4, 2003 this sequence version replaced NP_116169.1.
            
            Transcript Variant: This variant (1) uses an alternate splice
            junction in the 3' end compared to variant 7. The resulting isoform
            (1) has a shorter and distinct C-terminus compared to isoform 6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The extent of this RefSeq
            transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.29028.1,
                                           SRR1803615.263537.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313236.10/ ENSP00000315635.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..366
                     /product="transmembrane protein 25 isoform 1 precursor"
                     /note="0610039J01Rik"
                     /calculated_mol_wt=36650
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2653
     mat_peptide     27..366
                     /product="Transmembrane protein 25. /id=PRO_0000014984"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YD3.1)"
                     /calculated_mol_wt=36650
     Region          27..118
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          48..52
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          62..66
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          91..94
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86YD3.1)"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86YD3.1)"
     Site            175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86YD3.1)"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86YD3.1)"
     Site            205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86YD3.1)"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YD3.1)"
     Region          299..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YD3.1)"
     CDS             1..366
                     /gene="TMEM25"
                     /coded_by="NM_032780.4:71..1171"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8398.1"
                     /db_xref="GeneID:84866"
                     /db_xref="HGNC:HGNC:25890"
                     /db_xref="MIM:613934"
ORIGIN      
        1 malppgpaal rhtllllpal lssgwgelep qidgqtwaer alrenerhaf tcrvaggpgt
       61 prlawyldgq lqeastsrll svggeafsgg tstftvtahr aqhelncslq dprsgrsana
      121 svilnvqfkp eiaqvgakyq eaqgpgllvv lfalvranpp anvtwidqdg pvtvntsdfl
      181 vldaqnypwl tnhtvqlqlr slahnlsvva tndvgvtsas lpapgllatr vevpllgivv
      241 aaglalgtlv gfstlvaclv crkekktkgp srhpslissd snnlklnnvr lprenmslps
      301 nlqlndltpd sravkpadrq maqnnsrpel ldpepggllt sqgfirlpvl gyiyrvssvs
      361 sdeiwl
//
LOCUS       NP_036420                370 aa            linear   PRI 27-APR-2025
DEFINITION  translocating chain-associated membrane protein 2 [Homo sapiens].
ACCESSION   NP_036420
VERSION     NP_036420.1
DBSOURCE    REFSEQ: accession NM_012288.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Gao,X., Jiang,W., Ke,Z., Huang,Q., Chen,L., Zhang,G., Li,C. and
            Yu,X.
  TITLE     TRAM2 promotes the malignant progression of glioma through
            PI3K/AKT/mTOR pathway
  JOURNAL   Biochem Biophys Res Commun 586, 34-41 (2022)
   PUBMED   34826698
  REMARK    GeneRIF: TRAM2 promotes the malignant progression of glioma through
            PI3K/AKT/mTOR pathway.
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Deng,Y., You,L., Lu,Y., Han,S., Wang,J., Vicas,N., Chen,C. and
            Ye,J.
  TITLE     Identification of TRAMs as sphingolipid-binding proteins using a
            photoactivatable and clickable short-chain ceramide analog
  JOURNAL   J Biol Chem 297 (6), 101415 (2021)
   PUBMED   34793833
  REMARK    GeneRIF: Identification of TRAMs as sphingolipid-binding proteins
            using a photoactivatable and clickable short-chain ceramide analog.
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Li,L., Ugalde,A.P., Scheele,C.L.G.J., Dieter,S.M., Nagel,R., Ma,J.,
            Pataskar,A., Korkmaz,G., Elkon,R., Chien,M.P., You,L., Su,P.R.,
            Bleijerveld,O.B., Altelaar,M., Momchev,L., Manber,Z., Han,R., van
            Breugel,P.C., Lopes,R., Ten Dijke,P., van Rheenen,J. and Agami,R.
  TITLE     A comprehensive enhancer screen identifies TRAM2 as a key and novel
            mediator of YAP oncogenesis
  JOURNAL   Genome Biol 22 (1), 54 (2021)
   PUBMED   33514403
  REMARK    GeneRIF: A comprehensive enhancer screen identifies TRAM2 as a key
            and novel mediator of YAP oncogenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Chen,Q., Denard,B., Lee,C.E., Han,S., Ye,J.S. and Ye,J.
  TITLE     Inverting the Topology of a Transmembrane Protein by Regulating the
            Translocation of the First Transmembrane Helix
  JOURNAL   Mol Cell 63 (4), 567-578 (2016)
   PUBMED   27499293
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Hsu,L.C., Liu,S., Abedinpour,F., Beech,R.D., Lahti,J.M., Kidd,V.J.,
            Greenspan,J.A. and Yeung,C.Y.
  TITLE     The murine G+C-rich promoter binding protein mGPBP is required for
            promoter-specific transcription
  JOURNAL   Mol Cell Biol 23 (23), 8773-8785 (2003)
   PUBMED   14612417
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Onuchic,L.F., Mrug,M., Lakings,A.L., Muecher,G., Becker,J.,
            Zerres,K., Avner,E.D., Dixit,M., Somlo,S., Germino,G.G. and
            Guay-Woodford,L.M.
  TITLE     Genomic organization of the KIAA0057 gene that encodes a TRAM-like
            protein and its exclusion as a polycystic kidney and hepatic
            disease 1 (PKHD1) candidate gene
  JOURNAL   Mamm Genome 10 (12), 1175-1178 (1999)
   PUBMED   10594243
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Dodson,G. and Steiner,D.
  TITLE     The role of assembly in insulin's biosynthesis
  JOURNAL   Curr Opin Struct Biol 8 (2), 189-194 (1998)
   PUBMED   9631292
  REMARK    Review article
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Sudo,K., Chinen,K. and Nakamura,Y.
  TITLE     2058 expressed sequence tags (ESTs) from a human fetal lung cDNA
            library
  JOURNAL   Genomics 24 (2), 276-279 (1994)
   PUBMED   7698749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC028121.1, D31762.1 and
            AL049611.24.
            
            Summary: TRAM2 is a component of the translocon, a gated
            macromolecular channel that controls the posttranslational
            processing of nascent secretory and membrane proteins at the
            endoplasmic reticulum (ER) membrane.[supplied by OMIM, Jul 2004].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D31762.1, SRR1803614.72826.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000182527.4/ ENSP00000182527.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.2"
     Protein         1..370
                     /product="translocating chain-associated membrane protein
                     2"
                     /note="TRAM-like protein"
                     /calculated_mol_wt=43197
     Site            23..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15035.1)"
     Region          49..110
                     /region_name="TRAM1"
                     /note="TRAM1-like protein; pfam08390"
                     /db_xref="CDD:462460"
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15035.1)"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15035.1)"
     Region          112..321
                     /region_name="TLC"
                     /note="TRAM, LAG1 and CLN8 homology domains; smart00724"
                     /db_xref="CDD:214789"
     Site            120..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15035.1)"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15035.1)"
     Site            192..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15035.1)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15035.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15035.1)"
     Site            288..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15035.1)"
     Region          348..370
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15035.1)"
     CDS             1..370
                     /gene="TRAM2"
                     /coded_by="NM_012288.4:146..1258"
                     /db_xref="CCDS:CCDS34477.1"
                     /db_xref="GeneID:9697"
                     /db_xref="HGNC:HGNC:16855"
                     /db_xref="MIM:608485"
ORIGIN      
        1 mafrrrtksy plfsqefvih nhadigfclv lcvliglmfe vtaktaflfi lpqynisvpt
       61 adsetvhyhy gpkdlvtilf yifitiilha vvqeyildki skrlhlskvk hskfnesgql
      121 vvfhftsviw cfyvvvtegy ltnprslwed yphvhlpfqv kffylcqlay wlhalpelyf
      181 qkvrkeeipr qlqyiclylv hiagayllnl srlglillll qysteflfht arlfyfaden
      241 neklfsawaa vfgvtrlfil tlavlaigfg larmenqafd pekgnfntlf crlcvlllvc
      301 aaqawlmwrf ihsqlrhwre ywneqsakrr vpatprlpar likresgyhe ngvvkaengt
      361 sprtkklksp
//
LOCUS       NP_083593                193 aa            linear   ROD 27-APR-2025
DEFINITION  izumo sperm-egg fusion protein 2 isoform 1 precursor [Mus
            musculus].
ACCESSION   NP_083593 XP_620490 XP_922319
VERSION     NP_083593.1
DBSOURCE    REFSEQ: accession NM_029317.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC150895.2, BY087754.1 and AK006268.1.
            
            On or before Jul 9, 2009 this sequence version replaced
            XP_922319.1, XP_620490.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY706349.1, AK006268.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 28.89 cM"
     Protein         1..193
                     /product="izumo sperm-egg fusion protein 2 isoform 1
                     precursor"
                     /note="izumo sperm-egg fusion protein 2"
                     /calculated_mol_wt=19751
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1909
     Region          21..138
                     /region_name="IZUMO"
                     /note="Izumo sperm-egg fusion, Ig domain-associated;
                     pfam15005"
                     /db_xref="CDD:464437"
     CDS             1..193
                     /gene="Izumo2"
                     /gene_synonym="1700023D19Rik"
                     /coded_by="NM_029317.2:14..595"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS52235.1"
                     /db_xref="GeneID:75510"
                     /db_xref="MGI:MGI:1922760"
ORIGIN      
        1 mplalalvll cglggpgawg clqcdqsvll elrqlrdaiv tkrfhleglq araqalllsm
       61 egpffrdyam nafvgkvvvd qlekvatsfk nqaqyikans ktdvplleel vsfrehaike
      121 lkgalrdyem kacdhktcqd gqfrmtlkfq ddnkprnmvl vgdlvtvgla iltflvilia
      181 actyrqnrkl llk
//
LOCUS       NP_004409                314 aa            linear   PRI 27-APR-2025
DEFINITION  dual specificity protein phosphatase 2 [Homo sapiens].
ACCESSION   NP_004409
VERSION     NP_004409.1
DBSOURCE    REFSEQ: accession NM_004418.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Ren,D., Li,W., Zeng,R., Liu,X., Liang,H., Xiong,W., Yang,C. and
            Jin,X.
  TITLE     Retinoblastoma-associated protein is important for TRIM24-mediated
            activation of the mTOR signaling pathway through DUSP2 action in
            prostate cancer
  JOURNAL   Cell Death Differ 31 (5), 592-604 (2024)
   PUBMED   38514847
  REMARK    GeneRIF: Retinoblastoma-associated protein is important for
            TRIM24-mediated activation of the mTOR signaling pathway through
            DUSP2 action in prostate cancer.
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Dan,Lu., Liu,L., Sun,Y., Song,J., Yin,Q., Zhang,G., Qi,F., Hu,Z.,
            Yang,Z., Zhou,Z., Hu,Y., Zhang,L., Ji,J., Zhao,X., Jin,Y.,
            McNutt,M.A. and Yin,Y.
  TITLE     The phosphatase PAC1 acts as a T cell suppressor and attenuates
            host antitumor immunity
  JOURNAL   Nat Immunol 21 (3), 287-297 (2020)
   PUBMED   31932812
  REMARK    GeneRIF: PAC1 is selectively upregulated in exhausted
            tumor-infiltrating lymphocytes and is associated with poor
            prognosis of patients with cancer. PAC1(hi) effector T cells lose
            their proliferative and effector capacities and convert into
            exhausted T cells.
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Liu,W., Tian,X., Ding,X. and Zhang,L.
  TITLE     Expression of Dual-Specificity Phosphatase 2 (DUSP2) in Patients
            with Serous Ovarian Carcinoma and in SKOV3 and OVCAR3 Cells In
            Vitro
  JOURNAL   Med Sci Monit 25, 10180-10189 (2019)
   PUBMED   31889045
  REMARK    GeneRIF: Down-regulation of DUSP2 expression in serous ovarian
            carcinoma was an independent risk factor for patient survival.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Yin,H., He,W., Li,Y., Xu,N., Zhu,X., Lin,Y. and Gou,X.
  TITLE     Loss of DUSP2 predicts a poor prognosis in patients with bladder
            cancer
  JOURNAL   Hum Pathol 85, 152-161 (2019)
   PUBMED   30458195
  REMARK    GeneRIF: Taken together, our findings for the first time suggested
            DUSP2 as a progression and prognosis biomarker for bladder cancer.
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Hou,P.C., Li,Y.H., Lin,S.C., Lin,S.C., Lee,J.C., Lin,B.W.,
            Liou,J.P., Chang,J.Y., Kuo,C.C., Liu,Y.M., Sun,H.S. and Tsai,S.J.
  TITLE     Hypoxia-Induced Downregulation of DUSP-2 Phosphatase Drives Colon
            Cancer Stemness
  JOURNAL   Cancer Res 77 (16), 4305-4316 (2017)
   PUBMED   28652251
  REMARK    GeneRIF: Authors report that hypoxia-mediated downregulation of the
            dual specificity phosphatase 2 (DUSP2) is critical for the
            accumulation of CSC in colorectal cancer.
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Yi,H., Morton,C.C., Weremowicz,S., McBride,O.W. and Kelly,K.
  TITLE     Genomic organization and chromosomal localization of the DUSP2
            gene, encoding a MAP kinase phosphatase, to human 2p11.2-q11
  JOURNAL   Genomics 28 (1), 92-96 (1995)
   PUBMED   7590752
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Raingeaud,J., Gupta,S., Rogers,J.S., Dickens,M., Han,J.,
            Ulevitch,R.J. and Davis,R.J.
  TITLE     Pro-inflammatory cytokines and environmental stress cause p38
            mitogen-activated protein kinase activation by dual phosphorylation
            on tyrosine and threonine
  JOURNAL   J Biol Chem 270 (13), 7420-7426 (1995)
   PUBMED   7535770
REFERENCE   8  (residues 1 to 314)
  AUTHORS   Martell,K.J., Kwak,S., Hakes,D.J., Dixon,J.E. and Trent,J.M.
  TITLE     Chromosomal localization of four human VH1-like protein-tyrosine
            phosphatases
  JOURNAL   Genomics 22 (2), 462-464 (1994)
   PUBMED   7806236
REFERENCE   9  (residues 1 to 314)
  AUTHORS   Ward,Y., Gupta,S., Jensen,P., Wartmann,M., Davis,R.J. and Kelly,K.
  TITLE     Control of MAP kinase activation by the mitogen-induced
            threonine/tyrosine phosphatase PAC1
  JOURNAL   Nature 367 (6464), 651-654 (1994)
   PUBMED   8107850
REFERENCE   10 (residues 1 to 314)
  AUTHORS   Rohan,P.J., Davis,P., Moskaluk,C.A., Kearns,M., Krutzsch,H.,
            Siebenlist,U. and Kelly,K.
  TITLE     PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase
  JOURNAL   Science 259 (5102), 1763-1766 (1993)
   PUBMED   7681221
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB475178.1 and BC007771.2.
            
            Summary:  The protein encoded by this gene is a member of the dual
            specificity protein phosphatase subfamily.  These phosphatases
            inactivate their target kinases by dephosphorylating both the
            phosphoserine/threonine and phosphotyrosine residues.  They
            negatively regulate members of the mitogen-activated protein (MAP)
            kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated
            with cellular proliferation and differentiation.  Different members
            of the family of dual specificity phosphatases show distinct
            substrate specificities for various MAP kinases, different tissue
            distribution and subcellular localization, and different modes of
            inducibility of their expression by extracellular stimuli.  This
            gene product inactivates ERK1 and ERK2, is predominantly expressed
            in hematopoietic tissues, and is localized in the nucleus.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L11329.1, SRR1163655.87018.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000288943.5/ ENSP00000288943.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..314
                     /product="dual specificity protein phosphatase 2"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="serine/threonine specific protein phosphatase; dual
                     specificity protein phosphatase PAC-1"
                     /calculated_mol_wt=34269
     Region          8..143
                     /region_name="DSP_MapKP"
                     /note="N-terminal regulatory rhodanese domain of dual
                     specificity phosphatases (DSP), such as Mapk Phosphatase.
                     This domain is believed to determine substrate specificity
                     by binding the substrate, such as ERK2, and activating the
                     C-terminal catalytic domain by...; cd01446"
                     /db_xref="CDD:238723"
     Site            56..58
                     /site_type="active"
                     /note="putative substrate binding residues [active]"
                     /db_xref="CDD:238723"
     Region          170..313
                     /region_name="DSP_DUSP2"
                     /note="dual specificity phosphatase domain of dual
                     specificity protein phosphatase 2; cd14641"
                     /db_xref="CDD:350489"
     CDS             1..314
                     /gene="DUSP2"
                     /gene_synonym="PAC-1; PAC1"
                     /coded_by="NM_004418.4:87..1031"
                     /db_xref="CCDS:CCDS2016.1"
                     /db_xref="GeneID:1844"
                     /db_xref="HGNC:HGNC:3068"
                     /db_xref="MIM:603068"
ORIGIN      
        1 mgleaarele caalgtllrd preaertlll dcrpflafcr rhvraarpvp wnallrrrar
       61 gppaavlacl lpdralrtrl vrgelaravv ldegsasvae lrpdspahvl laallhetra
      121 gptavyflrg gfdgfqgccp dlcseapapa lpptgdktsr sdsrapvydq ggpveilpyl
      181 flgscshssd lqglqacgit avlnvsascp nhfeglfryk sipvednqmv eisawfqeai
      241 gfidwvknsg grvlvhcqag isrsaticla ylmqsrrvrl deafdfvkqr rgvispnfsf
      301 mgqllqfetq vlch
//
LOCUS       NP_036468                456 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear prelamin A recognition factor isoform a [Homo sapiens].
ACCESSION   NP_036468
VERSION     NP_036468.1
DBSOURCE    REFSEQ: accession NM_012336.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Yang,Y., Chen,C., Zuo,Q., Lu,H., Salman,S., Lyu,Y., Huang,T.Y.,
            Wicks,E.E., Jackson,W. 3rd, Datan,E., Wang,R., Wang,Y., Le,N.,
            Zhu,Y., Qin,W. and Semenza,G.L.
  TITLE     NARF is a hypoxia-induced coactivator for OCT4-mediated breast
            cancer stem cell specification
  JOURNAL   Sci Adv 8 (49), eabo5000 (2022)
   PUBMED   36490339
  REMARK    GeneRIF: NARF is a hypoxia-induced coactivator for OCT4-mediated
            breast cancer stem cell specification.
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Ding,D., Valdivia,A.O. and Bhattacharya,S.K.
  TITLE     Nuclear prelamin a recognition factor and iron dysregulation in
            multiple sclerosis
  JOURNAL   Metab Brain Dis 35 (2), 275-282 (2020)
   PUBMED   31823109
  REMARK    GeneRIF: Nuclear prelamin a recognition factor and iron
            dysregulation in multiple sclerosis.
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Malki,K., Uher,R., Paya-Cano,J., Binder,E., Rietschel,M., Zobel,A.,
            Mors,O., Hauser,J., Henigsberg,N., Jerman,B., Souery,D.,
            Placentino,A., Ng,M.Y., Cohen-Woods,S., Sluyter,F., Farmer,A.,
            Aitchison,K.J., Craig,I.W., Lewis,C.M., McGuffin,P. and
            Schalkwyk,L.C.
  TITLE     Convergent animal and human evidence suggests a role of PPM1A gene
            in response to antidepressants
  JOURNAL   Biol Psychiatry 69 (4), 360-365 (2011)
   PUBMED   20970119
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Moller-Krull,M., Zemann,A., Roos,C., Brosius,J. and Schmitz,J.
  TITLE     Beyond DNA: RNA editing and steps toward Alu exonization in
            primates
  JOURNAL   J Mol Biol 382 (3), 601-609 (2008)
   PUBMED   18680752
  REMARK    GeneRIF: Data suggest that gorilla, chimpanzee, and human nuclear
            prelamin A recognition factor genes exemplify the versatile
            interplay of pre- and posttranscriptional modifications leading to
            novel genetic potential.
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Lattanzi,G., Columbaro,M., Mattioli,E., Cenni,V., Camozzi,D.,
            Wehnert,M., Santi,S., Riccio,M., Del Coco,R., Maraldi,N.M.,
            Squarzoni,S., Foisner,R. and Capanni,C.
  TITLE     Pre-Lamin A processing is linked to heterochromatin organization
  JOURNAL   J Cell Biochem 102 (5), 1149-1159 (2007)
   PUBMED   17654502
  REMARK    GeneRIF: Prelamin A processing is linked to heterochromatin
            organization.
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Lev-Maor,G., Sorek,R., Levanon,E.Y., Paz,N., Eisenberg,E. and
            Ast,G.
  TITLE     RNA-editing-mediated exon evolution
  JOURNAL   Genome Biol 8 (2), R29 (2007)
   PUBMED   17326827
  REMARK    GeneRIF: RNA editing enables exonization of a nuclear prelamin A
            recognition factor Alu-exon.
            GeneRIF: Creation of a novel Alu-exon and elimination of a
            premature stop codon by RNA editing.
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Hackstein,J.H.
  TITLE     Eukaryotic Fe-hydrogenases -- old eukaryotic heritage or adaptive
            acquisitions?
  JOURNAL   Biochem Soc Trans 33 (Pt 1), 47-50 (2005)
   PUBMED   15667261
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Barton,R.M. and Worman,H.J.
  TITLE     Prenylated prelamin A interacts with Narf, a novel nuclear protein
  JOURNAL   J Biol Chem 274 (42), 30008-30018 (1999)
   PUBMED   10514485
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Maltese,W.A.
  TITLE     Posttranslational modification of proteins by isoprenoids in
            mammalian cells
  JOURNAL   FASEB J 4 (15), 3319-3328 (1990)
   PUBMED   2123808
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB123829.1, AF128406.1 and
            AC124287.10.
            
            Summary: Several proteins have been found to be prenylated and
            methylated at their carboxyl-terminal ends. Prenylation was
            initially believed to be important only for membrane attachment.
            However, another role for prenylation appears to be its importance
            in protein-protein interactions. The only nuclear proteins known to
            be prenylated in mammalian cells are prelamin A- and B-type lamins.
            Prelamin A is farnesylated and carboxymethylated on the cysteine
            residue of a carboxyl-terminal CaaX motif. This
            post-translationally modified cysteine residue is removed from
            prelamin A when it is endoproteolytically processed into mature
            lamin A. The protein encoded by this gene binds to the prenylated
            prelamin A carboxyl-terminal tail domain. It may be a component of
            a prelamin A endoprotease complex. The encoded protein is located
            in the nucleus, where it partially colocalizes with the nuclear
            lamina. It shares limited sequence similarity with iron-only
            bacterial hydrogenases. Alternatively spliced transcript variants
            encoding different isoforms have been identified for this gene,
            including one with a novel exon that is generated by RNA editing.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.132017.1,
                                           SRR1803613.21246.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309794.16/ ENSP00000309899.10
            RefSeq Select criteria :: based on expression
            undergoes RNA editing  :: PMID: 17326827
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..456
                     /product="nuclear prelamin A recognition factor isoform a"
                     /note="iron-only hydrogenase-like protein 2;
                     prenyl-dependent prelamin A binding protein"
                     /calculated_mol_wt=51025
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHQ1.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHQ1.1)"
     Region          92..381
                     /region_name="Fe_hyd_lg_C"
                     /note="Iron only hydrogenase large subunit, C-terminal
                     domain; pfam02906"
                     /db_xref="CDD:397172"
     Region          398..446
                     /region_name="Fe_hyd_SSU"
                     /note="Iron hydrogenase small subunit; smart00902"
                     /db_xref="CDD:214899"
     CDS             1..456
                     /gene="NARF"
                     /gene_synonym="IOP2"
                     /coded_by="NM_012336.4:64..1434"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32777.1"
                     /db_xref="GeneID:26502"
                     /db_xref="HGNC:HGNC:29916"
                     /db_xref="MIM:605349"
ORIGIN      
        1 mkcehctrke cskktktddq envsadapsp aqengekgef hkladakifl sdclacdscm
       61 taeegvqlsq qnakdffrvl nlnkkcdtsk hkvlvvsvcp qslpyfaakf nlsvtdasrr
      121 lcgflkslgv hyvfdttiaa dfsilesqke fvrryrqhse eertlpmlts acpgwvryae
      181 rvlgrpitah lctakspqqv mgslvkdyfa rqqnlspeki fhvivapcyd kklealqesl
      241 ppalhgsrga dcvltsgeia qimeqgdlsv rdaavdtlfg dlkedkvtrh dgassdghla
      301 hifrhaakel fnedveevty ralrnkdfqe vtlekngevv lrfaaaygfr niqnmilklk
      361 kgkfpfhfve vlacaggcln grgqaqtpdg hadkallrqm egiyadipvr rpessahvqe
      421 lyqewlegin spkarevlht tyqsqergth sldikw
//
LOCUS       NP_003866                693 aa            linear   PRI 27-APR-2025
DEFINITION  GMP synthase [glutamine-hydrolyzing] [Homo sapiens].
ACCESSION   NP_003866
VERSION     NP_003866.1
DBSOURCE    REFSEQ: accession NM_003875.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Wang,J., Luo,F.F., Huang,T.J., Mei,Y., Peng,L.X., Qian,C.N. and
            Huang,B.J.
  TITLE     The upregulated expression of RFC4 and GMPS mediated by DNA copy
            number alteration is associated with the early diagnosis and immune
            escape of ESCC based on a bioinformatic analysis
  JOURNAL   Aging (Albany NY) 13 (17), 21758-21777 (2021)
   PUBMED   34520390
  REMARK    GeneRIF: The upregulated expression of RFC4 and GMPS mediated by
            DNA copy number alteration is associated with the early diagnosis
            and immune escape of ESCC based on a bioinformatic analysis.
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Wang,J., Wu,Y., Li,Y., Wang,Y., Shen,F., Zhou,J. and Chen,Y.
  TITLE     Guanosine monophosphate synthase upregulation mediates cervical
            cancer progression by inhibiting the apoptosis of cervical cancer
            cells via the Stat3/P53 pathway
  JOURNAL   Int J Oncol 58 (4) (2021)
   PUBMED   33649833
  REMARK    GeneRIF: Guanosine monophosphate synthase upregulation mediates
            cervical cancer progression by inhibiting the apoptosis of cervical
            cancer cells via the Stat3/P53 pathway.
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Mechoud,M.A., Pujol-Carrion,N., Montella-Manuel,S. and de la
            Torre-Ruiz,M.A.
  TITLE     Interactions of GMP with Human Glrx3 and with Saccharomyces
            cerevisiae Grx3 and Grx4 Converge in the Regulation of the Gcn2
            Pathway
  JOURNAL   Appl Environ Microbiol 86 (14), e00221-20 (2020)
   PUBMED   32414791
  REMARK    GeneRIF: Interactions of GMP with Human Glrx3 and with
            Saccharomyces cerevisiae Grx3 and Grx4 Converge in the Regulation
            of the Gcn2 Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Roberts,R.L., Wallace,M.C., Seinen,M.L., van Bodegraven,A.A.,
            Krishnaprasad,K., Jones,G.T., van Rij,A.M., Baird,A.,
            Lawrance,I.C., Prosser,R., Bampton,P., Grafton,R., Simms,L.A.,
            Studd,C., Bell,S.J., Kennedy,M.A., Halliwell,J., Gearry,R.B.,
            Radford-Smith,G., Andrews,J.M., McHugh,P.C. and Barclay,M.L.
  TITLE     Nonsynonymous Polymorphism in Guanine Monophosphate Synthetase Is a
            Risk Factor for Unfavorable Thiopurine Metabolite Ratios in
            Patients With Inflammatory Bowel Disease
  JOURNAL   Inflamm Bowel Dis 24 (12), 2606-2612 (2018)
   PUBMED   29788244
  REMARK    GeneRIF: The GMPS SNP rs61750370 may be a reliable risk factor for
            extreme 6MMP preferential metabolism in patients with inflammatory
            bowel disease
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Davidsson,J. and Johansson,B.
  TITLE     Methylation and expression analyses of Pallister-Killian syndrome
            reveal partial dosage compensation of tetrasomy 12p and
            hypomethylation of gene-poor regions on 12p
  JOURNAL   Epigenetics 11 (3), 194-204 (2016)
   PUBMED   26890086
  REMARK    GeneRIF: Three genes-ATP6V1G1 in 9q32, GMPS in 3q25.31, and TBX5 in
            12q24.21-exhibited concomitant hypermethylation and decreased
            expression. The i(12p)-positive cells displayed global
            hypomethylation of gene-poor regions on 12p, a footprint previously
            associated with constitutional and acquired gains of whole
            chromosomes as well as with X-chromosome inactivation in females
REFERENCE   6  (residues 1 to 693)
  AUTHORS   Nakamura,J., Straub,K., Wu,J. and Lou,L.
  TITLE     The glutamine hydrolysis function of human GMP synthetase.
            Identification of an essential active site cysteine
  JOURNAL   J Biol Chem 270 (40), 23450-23455 (1995)
   PUBMED   7559506
REFERENCE   7  (residues 1 to 693)
  AUTHORS   Nakamura,J. and Lou,L.
  TITLE     Biochemical characterization of human GMP synthetase
  JOURNAL   J Biol Chem 270 (13), 7347-7353 (1995)
   PUBMED   7706277
REFERENCE   8  (residues 1 to 693)
  AUTHORS   Harendza,S.G., Thaiss,F. and Stahl,R.A.
  TITLE     Enhanced in vitro growth of glomerular cells derived from rats with
            immune-mediated mesangial injury
  JOURNAL   Exp Nephrol 1 (1), 55-61 (1993)
   PUBMED   8081953
REFERENCE   9  (residues 1 to 693)
  AUTHORS   Zalkin,H. and Dixon,J.E.
  TITLE     De novo purine nucleotide biosynthesis
  JOURNAL   Prog Nucleic Acid Res Mol Biol 42, 259-287 (1992)
   PUBMED   1574589
  REMARK    Review article
REFERENCE   10 (residues 1 to 693)
  AUTHORS   Page,T., Bakay,B. and Nyhan,W.L.
  TITLE     Human GMP synthetase
  JOURNAL   Int J Biochem 16 (1), 117-120 (1984)
   PUBMED   6698284
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG721087.1, BC012178.1,
            CB159072.1 and AC067721.22.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: In the de novo synthesis of purine nucleotides, IMP is the
            branch point metabolite at which point the pathway diverges to the
            synthesis of either guanine or adenine nucleotides. In the guanine
            nucleotide pathway, there are 2 enzymes involved in converting IMP
            to GMP, namely IMP dehydrogenase (IMPD1), which catalyzes the
            oxidation of IMP to XMP, and GMP synthetase, which catalyzes the
            amination of XMP to GMP. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.185387.1,
                                           SRR1803614.158947.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000496455.7/ ENSP00000419851.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.31"
     Protein         1..693
                     /product="GMP synthase [glutamine-hydrolyzing]"
                     /EC_number="6.3.5.2"
                     /note="GMP synthase; guanosine 5'-monophosphate synthase;
                     GMP synthetase; glutamine amidotransferase; MLL/GMPS
                     fusion protein; guanine monophosphate synthetase;
                     testicular tissue protein Li 82"
                     /calculated_mol_wt=76585
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P49915.1)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49915.1)"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49915.1)"
     Region          28..693
                     /region_name="guaA"
                     /note="GMP synthase; Reviewed; PRK00074"
                     /db_xref="CDD:234614"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P49915.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P49915.1)"
     CDS             1..693
                     /gene="GMPS"
                     /gene_synonym="GATD7"
                     /coded_by="NM_003875.3:222..2303"
                     /db_xref="CCDS:CCDS46941.1"
                     /db_xref="GeneID:8833"
                     /db_xref="HGNC:HGNC:4378"
                     /db_xref="MIM:600358"
ORIGIN      
        1 malcngdskl enaggdlkdg hhhyegavvi ldagaqygkv idrrvrelfv qseifpletp
       61 afaikeqgfr aiiisggpns vyaedapwfd paiftigkpv lgicygmqmm nkvfggtvhk
      121 ksvredgvfn isvdntcslf rglqkeevvl lthgdsvdkv adgfkvvars gnivagiane
      181 skklygaqfh pevgltengk vilknflydi agcsgtftvq nrelecirei kervgtskvl
      241 vllsggvdst vctallnral nqeqviavhi dngfmrkres qsveealkkl giqvkvinaa
      301 hsfyngtttl pisdedrtpr krisktlnmt tspeekrkii gdtfvkiane vigemnlkpe
      361 evflaqgtlr pdliesaslv asgkaelikt hhndtelirk lreegkviep lkdfhkdevr
      421 ilgrelglpe elvsrhpfpg pglairvica eepyickdfp etnnilkiva dfsasvkkph
      481 tllqrvkact teedqeklmq itslhslnaf llpiktvgvq gdcrsysyvc gisskdepdw
      541 esliflarli prmchnvnrv vyifgppvke pptdvtptfl ttgvlstlrq adfeahnilr
      601 esgyagkisq mpviltplhf drdplqkqps cqrsvvirtf itsdfmtgip atpgneipve
      661 vvlkmvteik kipgisrimy dltskppgtt ewe
//
LOCUS       NP_001352157             357 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-dependent glucokinase isoform 7 precursor [Homo sapiens].
ACCESSION   NP_001352157 XP_011520405
VERSION     NP_001352157.1
DBSOURCE    REFSEQ: accession NM_001365228.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Herrera-Morande,A., Vallejos-Baccelliere,G., Cea,P.A., Zamora,R.A.,
            Cid,D., Maturana,P., Gonzalez-Ordenes,F., Castro-Fernandez,V. and
            Guixe,V.
  TITLE     Kinetic characterization and phylogenetic analysis of human
            ADP-dependent glucokinase reveal new insights into its regulatory
            properties
  JOURNAL   Arch Biochem Biophys 741, 109602 (2023)
   PUBMED   37084804
  REMARK    GeneRIF: Kinetic characterization and phylogenetic analysis of
            human ADP-dependent glucokinase reveal new insights into its
            regulatory properties.
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Tandon,A., Birkenhagen,J., Nagalla,D., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase as a novel onco-target for haematological
            malignancies
  JOURNAL   Sci Rep 10 (1), 13584 (2020)
   PUBMED   32788680
  REMARK    GeneRIF: ADP-dependent glucokinase as a novel onco-target for
            haematological malignancies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Jiang,H.Y. and Wang,Z.J.
  TITLE     ADPGK-AS1 promotes the progression of colorectal cancer via
            sponging miR-525 to upregulate FUT1
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2380-2386 (2020)
   PUBMED   32196589
  REMARK    GeneRIF: ADPGK-AS1 promotes the progression of colorectal cancer
            via sponging miR-525 to upregulate FUT1.
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Imle,R., Wang,B.T., Stutzenberger,N., Birkenhagen,J., Tandon,A.,
            Carl,M., Himmelreich,N., Thiel,C., Grone,H.J., Poschet,G.,
            Volkers,M., Gulow,K., Schroder,A., Carillo,S., Mittermayr,S.,
            Bones,J., Kaminski,M.M., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing
  JOURNAL   Sci Rep 9 (1), 14248 (2019)
   PUBMED   31582762
  REMARK    GeneRIF: ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Richter,J.P., Goroncy,A.K., Ronimus,R.S. and Sutherland-Smith,A.J.
  TITLE     The Structural and Functional Characterization of Mammalian
            ADP-dependent Glucokinase
  JOURNAL   J Biol Chem 291 (8), 3694-3704 (2016)
   PUBMED   26555263
  REMARK    GeneRIF: ADPGK is substrate inhibited by high glucose concentration
            and shows high specificity for glucose, with no activity for other
            sugars, as determined by NMR spectroscopy, including 2-deoxyglucose
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Cuesta-Munoz,A.L., Tuomi,T., Cobo-Vuilleumier,N., Koskela,H.,
            Odili,S., Stride,A., Buettger,C., Otonkoski,T., Froguel,P.,
            Grimsby,J., Garcia-Gimeno,M. and Matschinsky,F.M.
  TITLE     Clinical heterogeneity in monogenic diabetes caused by mutations in
            the glucokinase gene (GCK-MODY)
  JOURNAL   Diabetes Care 33 (2), 290-292 (2010)
   PUBMED   19903754
  REMARK    GeneRIF: Glucose and insulin response to oral glucose is higher in
            GCK(261) carriers, indicating clinical heterogeneity in GCK
            maturity diabetes carriers.
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Codner,E., Rocha,A., Deng,L., Martinez-Aguayo,A., Godoy,C.,
            Mericq,V. and Chung,W.K.
  TITLE     Mild fasting hyperglycemia in children: high rate of glucokinase
            mutations and some risk of developing type 1 diabetes mellitus
  JOURNAL   Pediatr Diabetes 10 (6), 382-388 (2009)
   PUBMED   19309449
  REMARK    GeneRIF: The presence of mild persistent hyperglycemia in any
            patient without autoantibodies should lead to genetic analysis of
            glucokinase, particularly if there is a positive family history.
REFERENCE   9  (residues 1 to 357)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 357)
  AUTHORS   Ronimus,R.S. and Morgan,H.W.
  TITLE     Cloning and biochemical characterization of a novel mouse
            ADP-dependent glucokinase
  JOURNAL   Biochem Biophys Res Commun 315 (3), 652-658 (2004)
   PUBMED   14975750
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009712.22 and DA600729.1.
            
            On Aug 9, 2018 this sequence version replaced XP_011520405.1.
            
            Summary: ADPGK (EC 2.7.1.147) catalyzes the ADP-dependent
            phosphorylation of glucose to glucose-6-phosphate and may play a
            role in glycolysis, possibly during ischemic conditions (Ronimus
            and Morgan, 2004 [PubMed 14975750]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.58373.1, BI907588.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2142586,
                                           SAMEA2142853 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..357
                     /product="ADP-dependent glucokinase isoform 7 precursor"
                     /EC_number="2.7.1.147"
                     /note="ATP-dependent glucokinase; rbBP-35"
                     /calculated_mol_wt=36529
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1854
     Region          60..352
                     /region_name="ribokinase_pfkB_like"
                     /note="ribokinase/pfkB superfamily: Kinases that accept a
                     wide variety of substrates, including carbohydrates and
                     aromatic small molecules, all are phosphorylated at a
                     hydroxyl group. The superfamily includes ribokinase,
                     fructokinase, ketohexokinase; cl00192"
                     /db_xref="CDD:469648"
     Site            order(162,338,341)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238177"
     Site            order(185,242,336,339..340,343)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238177"
     CDS             1..357
                     /gene="ADPGK"
                     /gene_synonym="2610017G09Rik; ADP-GK"
                     /coded_by="NM_001365228.1:68..1141"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:83440"
                     /db_xref="HGNC:HGNC:25250"
                     /db_xref="MIM:611861"
ORIGIN      
        1 malwrgsaya gflalavgcv fllepelpgs alrslwsslc lgpapappgp vspegrlaaa
       61 wdalivrpvr rwrrvavgvn acvdvvlsgv kllqalglsp gngkdhsilh srndleeafi
      121 hfmgkgaaae rffsdketfh diaqvasefp gaqhyvggna aligqkfaan sdlkvfpavt
      181 slglneqell fltqsasgph sslsswngvp dvgmvsdilf wilkehgrsk srasdltrih
      241 fhtlvyhila tvdghwanql aavaagarva gtqacateti dtsrvslrap qefmtshsea
      301 gsrivlnpnk pvvewhregi sfhftpvlvc kdpirtvglg daisaeglfy sevhphy
//
LOCUS       NP_060882                554 aa            linear   PRI 27-APR-2025
DEFINITION  suppressor of tumorigenicity 7 protein isoform 5 [Homo sapiens].
ACCESSION   NP_060882
VERSION     NP_060882.2
DBSOURCE    REFSEQ: accession NM_018412.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Liu,H., Lu,W., He,H., Wu,J., Zhang,C., Gong,H. and Yang,C.
  TITLE     Inflammation-dependent overexpression of c-Myc enhances CRL4DCAF4
            E3 ligase activity and promotes ubiquitination of ST7 in
            colitis-associated cancer
  JOURNAL   J Pathol 248 (4), 464-475 (2019)
   PUBMED   30945288
  REMARK    GeneRIF: Inflammation-dependent overexpression of c-Myc enhances
            CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7
            in colitis-associated cancer.
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Yan,F., Alinari,L., Lustberg,M.E., Martin,L.K.,
            Cordero-Nieves,H.M., Banasavadi-Siddegowda,Y., Virk,S.,
            Barnholtz-Sloan,J., Bell,E.H., Wojton,J., Jacob,N.K.,
            Chakravarti,A., Nowicki,M.O., Wu,X., Lapalombella,R., Datta,J.,
            Yu,B., Gordon,K., Haseley,A., Patton,J.T., Smith,P.L., Ryu,J.,
            Zhang,X., Mo,X., Marcucci,G., Nuovo,G., Kwon,C.H., Byrd,J.C.,
            Chiocca,E.A., Li,C., Sif,S., Jacob,S., Lawler,S., Kaur,B. and
            Baiocchi,R.A.
  TITLE     Genetic validation of the protein arginine methyltransferase PRMT5
            as a candidate therapeutic target in glioblastoma
  JOURNAL   Cancer Res 74 (6), 1752-1765 (2014)
   PUBMED   24453002
  REMARK    GeneRIF: The tumor suppressor ST7 is a key gene silenced by PRMT5.
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Hu,L., Wu,C., Zhao,X., Heist,R., Su,L., Zhao,Y., Han,B., Cao,S.,
            Chu,M., Dai,J., Dong,J., Shu,Y., Xu,L., Chen,Y., Wang,Y., Lu,F.,
            Jiang,Y., Yu,D., Chen,H., Tan,W., Ma,H., Chen,J., Jin,G., Wu,T.,
            Lu,D., Christiani,D.C., Lin,D., Hu,Z. and Shen,H.
  TITLE     Genome-wide association study of prognosis in advanced non-small
            cell lung cancer patients receiving platinum-based chemotherapy
  JOURNAL   Clin Cancer Res 18 (19), 5507-5514 (2012)
   PUBMED   22872573
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Zenklusen,J.C., Rodriguez,L.V., LaCava,M., Wang,Z., Goldstein,L.S.
            and Conti,C.J.
  TITLE     Novel susceptibility locus for mouse hepatomas: evidence for a
            conserved tumor suppressor gene
  JOURNAL   Genome Res 6 (11), 1070-1076 (1996)
   PUBMED   8938430
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Zenklusen,J.C., Weitzel,J.N., Ball,H.G. and Conti,C.J.
  TITLE     Allelic loss at 7q31.1 in human primary ovarian carcinomas suggests
            the existence of a tumor suppressor gene
  JOURNAL   Oncogene 11 (2), 359-363 (1995)
   PUBMED   7624150
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Zenklusen,J.C., Thompson,J.C., Troncoso,P., Kagan,J. and Conti,C.J.
  TITLE     Loss of heterozygosity in human primary prostate carcinomas: a
            possible tumor suppressor gene at 7q31.1
  JOURNAL   Cancer Res 54 (24), 6370-6373 (1994)
   PUBMED   7987830
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Zenklusen,J.C., Bieche,I., Lidereau,R. and Conti,C.J.
  TITLE     (C-A)n microsatellite repeat D7S522 is the most commonly deleted
            region in human primary breast cancer
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12155-12158 (1994)
   PUBMED   7991599
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Ogata,T., Ayusawa,D., Namba,M., Takahashi,E., Oshimura,M. and
            Oishi,M.
  TITLE     Chromosome 7 suppresses indefinite division of nontumorigenic
            immortalized human fibroblast cell lines KMST-6 and SUSM-1
  JOURNAL   Mol Cell Biol 13 (10), 6036-6043 (1993)
   PUBMED   8105370
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106873.3, AC002542.1 and
            AC003987.1.
            
            On Dec 14, 2000 this sequence version replaced NP_060882.1.
            
            Summary: The gene for this product maps to a region on chromosome 7
            identified as an autism-susceptibility locus. Mutation screening of
            the entire coding region in autistic individuals failed to identify
            phenotype-specific variants, suggesting that coding mutations for
            this gene are unlikely to be involved in the etiology of autism.
            The function of this gene product has not been determined.
            Transcript variants encoding different isoforms of this protein
            have been described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.269516.1, AK292372.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.2"
     Protein         1..554
                     /product="suppressor of tumorigenicity 7 protein isoform
                     5"
                     /note="family with sequence similarity 4, subfamily A,
                     member 1; suppression of tumorigenicity 7 (breast);
                     suppressor of tumorigenicity 7 protein"
                     /calculated_mol_wt=63349
     Region          18..553
                     /region_name="ST7"
                     /note="ST7 protein; pfam04184"
                     /db_xref="CDD:461214"
     CDS             1..554
                     /gene="ST7"
                     /gene_synonym="ETS7q; FAM4A; FAM4A1; HELG; RAY1; SEN4;
                     TSG7"
                     /coded_by="NM_018412.4:41..1705"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS5769.1"
                     /db_xref="GeneID:7982"
                     /db_xref="HGNC:HGNC:11351"
                     /db_xref="MIM:600833"
ORIGIN      
        1 maeaatgfle qlkscivwsw tylwtvwffi vlflvyilrv plkindnlst vsmflntltp
       61 kfyvaltgts slisglilif ewwyfrkygt sfieqvsvsh lrpllggvdn nssnnsnssn
      121 gdsdsnrqsv seckvwrnpl nlfrgaeynr ytwvtgrepl tyydmnlsaq dhqtfftcds
      181 dhlrpadaim qkawrernpq arisaaheal einecatayi llaeeeatti aeaeklfkqa
      241 lkagdgcyrr sqqlqhhgsq yeaqhrrdtn vlvyikrrla mcarrlgrtr eavkmmrdlm
      301 kefpllsmfn ihenlleall elqayadvqa vlakyddisl pksaticyta allkaravsd
      361 kfspeaasrr glstaemnav eaihravefn phvpkyllem kslilppehi lkrgdseaia
      421 yaffhlahwk rvegalnllh ctwegtfrmi pyplekghlf ypypicteta drellpsfhe
      481 vsvypkkelp ffilftaglc sftamlallt hqfpelmgvf akaflstlfa plnfvmekve
      541 silpsslwhq ltri
//
LOCUS       NP_001354215             501 aa            linear   PRI 27-APR-2025
DEFINITION  phosphoacetylglucosamine mutase isoform 5 [Homo sapiens].
ACCESSION   NP_001354215 XP_024302227
VERSION     NP_001354215.1
DBSOURCE    REFSEQ: accession NM_001367286.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Jacob,M., Masood,A. and Abdel Rahman,A.M.
  TITLE     Multi-Omics Profiling in PGM3 and STAT3 Deficiencies: A Tale of Two
            Patients
  JOURNAL   Int J Mol Sci 24 (3), 2406 (2023)
   PUBMED   36768728
  REMARK    GeneRIF: Multi-Omics Profiling in PGM3 and STAT3 Deficiencies: A
            Tale of Two Patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Zhang,N., Liu,S., Xu,J., Ning,T., Xie,S., Min,L., Zhu,S., Zhang,S.
            and Zhu,S.
  TITLE     PGM3 regulates beta-catenin activity to promote colorectal cancer
            cell progression
  JOURNAL   Exp Biol Med (Maywood) 247 (17), 1518-1528 (2022)
   PUBMED   35723049
  REMARK    GeneRIF: PGM3 regulates beta-catenin activity to promote colorectal
            cancer cell progression.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Lee,H., Cai,F., Kelekar,N., Velupally,N.K. and Kim,J.
  TITLE     Targeting PGM3 as a Novel Therapeutic Strategy in KRAS/LKB1
            Co-Mutant Lung Cancer
  JOURNAL   Cells 11 (1), 176 (2022)
   PUBMED   35011738
  REMARK    GeneRIF: Targeting PGM3 as a Novel Therapeutic Strategy in
            KRAS/LKB1 Co-Mutant Lung Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Pang,H., Amano,S., Inagaki,Y., Okamoto,T., Yamada,K., Kimura,H.,
            Koda,Y. and Yamagishi,S.I.
  TITLE     N-acetylglucosamine-phosphate mutase genotype and diabetic
            microvascular complications
  JOURNAL   Diabet Med 20 (5), 419-420 (2003)
   PUBMED   12752494
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Pang,H., Koda,Y., Soejima,M. and Kimura,H.
  TITLE     Identification of human phosphoglucomutase 3 (PGM3) as
            N-acetylglucosamine-phosphate mutase (AGM1)
  JOURNAL   Ann Hum Genet 66 (Pt 2), 139-144 (2002)
   PUBMED   12174217
  REMARK    GeneRIF: PGM(3) is identical to AGM(1).
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Mio,T., Yamada-Okabe,T., Arisawa,M. and Yamada-Okabe,H.
  TITLE     Functional cloning and mutational analysis of the human cDNA for
            phosphoacetylglucosamine mutase: identification of the amino acid
            residues essential for the catalysis
  JOURNAL   Biochim Biophys Acta 1492 (2-3), 369-376 (2000)
   PUBMED   11004509
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Li,C., Rodriguez,M. and Banerjee,D.
  TITLE     Cloning and characterization of complementary DNA encoding human
            N-acetylglucosamine-phosphate mutase protein
  JOURNAL   Gene 242 (1-2), 97-103 (2000)
   PUBMED   10721701
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Yoshida,H., Abe,T. and Nakamura,F.
  TITLE     Studies on the frequencies of PGM1, PGM3 and Es-D types from hair
            roots in Japanese subjects and the determination of these types
            from old hair roots
  JOURNAL   Forensic Sci Int 14 (1), 1-7 (1979)
   PUBMED   468082
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Chen,S.H., Anderson,J.E., Giblett,E.R. and Stamatoyannopoulos,G.
  TITLE     Isozyme patterns in erythrocytes from human fetuses
  JOURNAL   Am J Hematol 3, 23-28 (1977)
   PUBMED   203189
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049699.8 and AL121716.16.
            
            On Nov 16, 2018 this sequence version replaced XP_024302227.1.
            
            Summary: This gene encodes a member of the phosphohexose mutase
            family. The encoded protein mediates both glycogen formation and
            utilization by catalyzing the interconversion of
            glucose-1-phosphate and glucose-6-phosphate. A non-synonymous
            single nucleotide polymorphism in this gene may play a role in
            resistance to diabetic nephropathy and neuropathy. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.25702.1,
                                           SRR1803612.60263.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..501
                     /product="phosphoacetylglucosamine mutase isoform 5"
                     /EC_number="5.4.2.3"
                     /note="acetylglucosamine phosphomutase;
                     phosphoacetylglucosamine mutase;
                     N-acetylglucosamine-phosphate mutase 1"
                     /calculated_mol_wt=55256
     Region          22..486
                     /region_name="PGM3"
                     /note="PGM3 (phosphoglucomutase 3), also known as PAGM
                     (phosphoacetylglucosamine mutase) and AGM1
                     (N-acetylglucosamine-phosphate mutase), is an essential
                     enzyme found in eukaryotes that reversibly catalyzes the
                     conversion of GlcNAc-6-phosphate into...; cd03086"
                     /db_xref="CDD:100088"
     Site            order(29,64..65,276,278,280..281,351..353,370,372,374,455,
                     457..459,464)
                     /site_type="active"
                     /db_xref="CDD:100088"
     Site            order(276,278,280)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100088"
     Site            order(351..353,370,372,374,455,457..459,464)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100088"
     CDS             1..501
                     /gene="PGM3"
                     /gene_synonym="AGM1; IMD23; PAGM; PGM 3"
                     /coded_by="NM_001367286.1:90..1595"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS93954.1"
                     /db_xref="GeneID:5238"
                     /db_xref="HGNC:HGNC:8907"
                     /db_xref="MIM:172100"
ORIGIN      
        1 mdlgaitkys alhakpngli lqygtagfrt kaehldhvmf rmgllavlrs kqtkstigvm
       61 vtashnpeed ngvklvdplg emlapsweeh atclanaeeq dmqrvlidis ekeavnlqqd
      121 afvvigrdtr psseklsqsv idgvtvlggq fhdygllttp qlhymvycrn tggrygkati
      181 egyyqklska fveltkqasc sgdeyrslkv dcangigalk lremehyfsq glsvqlfndg
      241 skgklnhlcg adfvkshqkp pqgmeiksne rccsfdgdad rivyyyhdad ghfhlidgdk
      301 iatlissflk ellveigesl nigvvqtaya ngsstrylee vmkvpvyctk tgvkhlhhka
      361 qefdigvyfe anghgtalfs tavemkikqs aeqledkkrk aakmleniid lfnqvadrrv
      421 isttdaerqa vtppglqeai ndlvkkykls rafvrpsgte dvvrvyaead sqesadhlah
      481 evslavfqla ggigerpqpg f
//
LOCUS       NP_001341766             135 aa            linear   PRI 27-APR-2025
DEFINITION  protein Aster-B isoform 9 [Homo sapiens].
ACCESSION   NP_001341766
VERSION     NP_001341766.1
DBSOURCE    REFSEQ: accession NM_001354837.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Bandara,S., Ramkumar,S., Imanishi,S., Thomas,L.D., Sawant,O.B.,
            Imanishi,Y. and von Lintig,J.
  TITLE     Aster proteins mediate carotenoid transport in mammalian cells
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2200068119 (2022)
   PUBMED   35394870
  REMARK    GeneRIF: Aster proteins mediate carotenoid transport in mammalian
            cells.
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Ercan,B., Naito,T., Koh,D.H.Z., Dharmawan,D. and Saheki,Y.
  TITLE     Molecular basis of accessible plasma membrane cholesterol
            recognition by the GRAM domain of GRAMD1b
  JOURNAL   EMBO J 40 (6), e106524 (2021)
   PUBMED   33604931
  REMARK    GeneRIF: Molecular basis of accessible plasma membrane cholesterol
            recognition by the GRAM domain of GRAMD1b.
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Andersen,J.P., Zhang,J., Sun,H., Liu,X., Liu,J., Nie,J. and Shi,Y.
  TITLE     Aster-B coordinates with Arf1 to regulate mitochondrial cholesterol
            transport
  JOURNAL   Mol Metab 42, 101055 (2020)
   PUBMED   32738348
  REMARK    GeneRIF: Aster-B coordinates with Arf1 to regulate mitochondrial
            cholesterol transport.
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Dai,X., Guo,X., Liu,J., Cheng,A., Peng,X., Zha,L. and Wang,Z.
  TITLE     Circular RNA circGRAMD1B inhibits gastric cancer progression by
            sponging miR-130a-3p and regulating PTEN and p21 expression
  JOURNAL   Aging (Albany NY) 11 (21), 9689-9708 (2019)
   PUBMED   31719211
  REMARK    GeneRIF: Circular RNA circGRAMD1B inhibits gastric cancer
            progression by sponging miR-130a-3p and regulating PTEN and p21
            expression.
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Sandhu,J., Li,S., Fairall,L., Pfisterer,S.G., Gurnett,J.E.,
            Xiao,X., Weston,T.A., Vashi,D., Ferrari,A., Orozco,J.L.,
            Hartman,C.L., Strugatsky,D., Lee,S.D., He,C., Hong,C., Jiang,H.,
            Bentolila,L.A., Gatta,A.T., Levine,T.P., Ferng,A., Lee,R.,
            Ford,D.A., Young,S.G., Ikonen,E., Schwabe,J.W.R. and Tontonoz,P.
  TITLE     Aster Proteins Facilitate Nonvesicular Plasma Membrane to ER
            Cholesterol Transport in Mammalian Cells
  JOURNAL   Cell 175 (2), 514-529 (2018)
   PUBMED   30220461
REFERENCE   6  (residues 1 to 135)
  AUTHORS   Khanna,P., Lee,J.S., Sereemaspun,A., Lee,H. and Baeg,G.H.
  TITLE     GRAMD1B regulates cell migration in breast cancer cells through
            JAK/STAT and Akt signaling
  JOURNAL   Sci Rep 8 (1), 9511 (2018)
   PUBMED   29934528
  REMARK    GeneRIF: GRAMD1B regulates cell migration in breast cancer cells
            through JAK/STAT and Akt signaling
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 135)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP000783.4, BU622943.1 and BI256024.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.437269.1,
                                           SRR1163655.711860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.1"
     Protein         1..135
                     /product="protein Aster-B isoform 9"
                     /note="GRAM domain-containing protein 1B; long intergenic
                     non-protein coding RNA 1059; protein Aster-B"
                     /calculated_mol_wt=15118
     CDS             1..135
                     /gene="GRAMD1B"
                     /gene_synonym="LINC01059"
                     /coded_by="NM_001354837.2:525..932"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS86254.1"
                     /db_xref="GeneID:57476"
                     /db_xref="HGNC:HGNC:29214"
                     /db_xref="MIM:620179"
ORIGIN      
        1 mpaanmmenr plpalqvpep qgapegspvw sssstptlrr rrfkmrrmkn vqeqsleagl
       61 ardlpavlap gkeflqlpsi eitpssdedt pwsncstpsa sprrkrfllr kwlrvrerke
      121 csesssslri ftaqs
//
LOCUS       NP_001339617              59 aa            linear   PRI 27-APR-2025
DEFINITION  small integral membrane protein 30 precursor [Homo sapiens].
ACCESSION   NP_001339617
VERSION     NP_001339617.1
DBSOURCE    REFSEQ: accession NM_001352688.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 59)
  AUTHORS   Shi,T.T., Huang,Y., Li,Y., Dai,X.L., He,Y.H., Ding,J.C., Ran,T.,
            Shi,Y., Yuan,Q., Li,W.J. and Liu,W.
  TITLE     MAVI1, an endoplasmic reticulum-localized microprotein, suppresses
            antiviral innate immune response by targeting MAVS on mitochondrion
  JOURNAL   Sci Adv 9 (35), eadg7053 (2023)
   PUBMED   37656786
REFERENCE   2  (residues 1 to 59)
  AUTHORS   Yang,J.E., Zhong,W.J., Li,J.F., Lin,Y.Y., Liu,F.T., Tian,H.,
            Chen,Y.J., Luo,X.Y. and Zhuang,S.M.
  TITLE     LINC00998-encoded micropeptide SMIM30 promotes the G1/S transition
            of cell cycle by regulating cytosolic calcium level
  JOURNAL   Mol Oncol 17 (5), 901-916 (2023)
   PUBMED   36495128
  REMARK    GeneRIF: LINC00998-encoded micropeptide SMIM30 promotes the G1/S
            transition of cell cycle by regulating cytosolic calcium level.
REFERENCE   3  (residues 1 to 59)
  AUTHORS   Pang,Y., Liu,Z., Han,H., Wang,B., Li,W., Mao,C. and Liu,S.
  TITLE     Peptide SMIM30 promotes HCC development by inducing SRC/YES1
            membrane anchoring and MAPK pathway activation
  JOURNAL   J Hepatol 73 (5), 1155-1169 (2020)
   PUBMED   32461121
  REMARK    GeneRIF: Peptide SMIM30 promotes HCC development by inducing
            SRC/YES1 membrane anchoring and MAPK pathway activation.
REFERENCE   4  (residues 1 to 59)
  AUTHORS   Chen,J., Brunner,A.D., Cogan,J.Z., Nunez,J.K., Fields,A.P.,
            Adamson,B., Itzhak,D.N., Li,J.Y., Mann,M., Leonetti,M.D. and
            Weissman,J.S.
  TITLE     Pervasive functional translation of noncanonical human open reading
            frames
  JOURNAL   Science 367 (6482), 1140-1146 (2020)
   PUBMED   32139545
REFERENCE   5  (residues 1 to 59)
  AUTHORS   Ye,N., Rao,S., Du,T., Hu,H., Liu,Z., Shen,Y. and Xu,Q.
  TITLE     Intergenic variants may predispose to major depression disorder
            through regulation of long non-coding RNA expression
  JOURNAL   Gene 601, 21-26 (2017)
   PUBMED   27940106
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX537645.1 and BU630382.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.241495.1,
                                           SRR1660809.126565.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397764.8/ ENSP00000490095.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..59
                     /product="small integral membrane protein 30 precursor"
                     /note="long intergenic non-protein coding RNA 998;
                     putative transmembrane protein LINC00998; microprotein in
                     antiviral immunity 1"
                     /calculated_mol_wt=3576
     Region          1..54
                     /region_name="DUF4730"
                     /note="Domain of unknown function (DUF4730); pfam15873"
                     /db_xref="CDD:292498"
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A4D0T7.2)"
                     /calculated_mol_wt=2544
     mat_peptide     25..59
                     /product="Small integral membrane protein 30.
                     /id=PRO_0000349370"
                     /note="propagated from UniProtKB/Swiss-Prot (A4D0T7.2)"
                     /calculated_mol_wt=3576
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A4D0T7.2)"
     CDS             1..59
                     /gene="SMIM30"
                     /gene_synonym="LINC00998; MAVI1"
                     /coded_by="NM_001352688.2:151..330"
                     /db_xref="CCDS:CCDS87543.1"
                     /db_xref="GeneID:401397"
                     /db_xref="HGNC:HGNC:48953"
ORIGIN      
        1 mtsvstqlsl vlmslllvlp vveaveagda ialllgvvls itgicaclgv yarkrngqm
//
LOCUS       NP_079452               1382 aa            linear   PRI 27-APR-2025
DEFINITION  ninein-like protein isoform 1 [Homo sapiens].
ACCESSION   NP_079452
VERSION     NP_079452.3
DBSOURCE    REFSEQ: accession NM_025176.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1382)
  AUTHORS   Ma,X.J., Shang,L., Zhang,W.M., Wang,M.R. and Zhan,Q.M.
  TITLE     Mitotic regulator Nlp interacts with XPA/ERCC1 complexes and
            regulates nucleotide excision repair (NER) in response to UV
            radiation
  JOURNAL   Cancer Lett 373 (2), 214-221 (2016)
   PUBMED   26805762
  REMARK    GeneRIF: Upon UVC radiation, Nlp interacts with XPA and ERCC1, and
            enhances their association
REFERENCE   2  (residues 1 to 1382)
  AUTHORS   Bachmann-Gagescu,R., Dona,M., Hetterschijt,L., Tonnaer,E.,
            Peters,T., de Vrieze,E., Mans,D.A., van Beersum,S.E., Phelps,I.G.,
            Arts,H.H., Keunen,J.E., Ueffing,M., Roepman,R., Boldt,K.,
            Doherty,D., Moens,C.B., Neuhauss,S.C., Kremer,H. and van Wijk,E.
  TITLE     The Ciliopathy Protein CC2D2A Associates with NINL and Functions in
            RAB8-MICAL3-Regulated Vesicle Trafficking
  JOURNAL   PLoS Genet 11 (10), e1005575 (2015)
   PUBMED   26485645
  REMARK    GeneRIF: these data support a model where CC2D2A associates with
            NINL to provide a docking point for cilia-directed cargo vesicles,
            suggesting a mechanism by which transition zone proteins can
            control the protein content of the ciliary compartment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1382)
  AUTHORS   Dona,M., Bachmann-Gagescu,R., Texier,Y., Toedt,G., Hetterschijt,L.,
            Tonnaer,E.L., Peters,T.A., van Beersum,S.E., Bergboer,J.G.,
            Horn,N., de Vrieze,E., Slijkerman,R.W., van Reeuwijk,J., Flik,G.,
            Keunen,J.E., Ueffing,M., Gibson,T.J., Roepman,R., Boldt,K.,
            Kremer,H. and van Wijk,E.
  TITLE     NINL and DZANK1 Co-function in Vesicle Transport and Are Essential
            for Photoreceptor Development in Zebrafish
  JOURNAL   PLoS Genet 11 (10), e1005574 (2015)
   PUBMED   26485514
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1382)
  AUTHORS   Zhao,W., Song,Y., Xu,B. and Zhan,Q.
  TITLE     Overexpression of centrosomal protein Nlp confers breast carcinoma
            resistance to paclitaxel
  JOURNAL   Cancer Biol Ther 13 (3), 156-163 (2012)
   PUBMED   22353935
  REMARK    GeneRIF: Breast cancer patients with high expression of Nlp were
            likely resistant to the treatment of paclitaxel.
REFERENCE   5  (residues 1 to 1382)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   6  (residues 1 to 1382)
  AUTHORS   Casenghi,M., Meraldi,P., Weinhart,U., Duncan,P.I., Korner,R. and
            Nigg,E.A.
  TITLE     Polo-like kinase 1 regulates Nlp, a centrosome protein involved in
            microtubule nucleation
  JOURNAL   Dev Cell 5 (1), 113-125 (2003)
   PUBMED   12852856
REFERENCE   7  (residues 1 to 1382)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   8  (residues 1 to 1382)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   9  (residues 1 to 1382)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   10 (residues 1 to 1382)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA448124.1, DA871028.1, AB023197.1 and BC036380.2.
            
            On Nov 15, 2004 this sequence version replaced NP_079452.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB023197.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278886.11/ ENSP00000278886.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.21"
     Protein         1..1382
                     /product="ninein-like protein isoform 1"
                     /note="ninein-like protein"
                     /calculated_mol_wt=156213
     Region          144..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2I6.2)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZQ12; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2I6.2)"
     Region          198..259
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Region          393..>701
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          495..497
                     /region_name="KEN box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2I6.2)"
     Region          633..641
                     /region_name="D-box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2I6.2)"
     Region          857..969
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2I6.2)"
     Region          982..1006
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2I6.2)"
     Region          1052..>1363
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1382
                     /gene="NINL"
                     /gene_synonym="NLP"
                     /coded_by="NM_025176.6:89..4237"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33452.1"
                     /db_xref="GeneID:22981"
                     /db_xref="HGNC:HGNC:29163"
                     /db_xref="MIM:609580"
ORIGIN      
        1 mdeeenhyvs qlrevysscd ttgtgfldrq eltqlclklh leqqlpvllq tllgndhfar
       61 vnfeefkegf vavlssnagv rpsdedsssl esaassaipp kyvngskwyg rrsrpelcda
      121 atearrvpeq qtqaslkshl wrsaslesve spksdeeaes tkeaqnelfe aqgqlqtwds
      181 edfgspqksc spsfdtpesq irgvweelgv gssghlseqe lavvcqsvgl qglekeeled
      241 lfnkldqdgd gkvsleefql glfshepall lesstrvkps kawshyqvpe esgchtttts
      301 slvslcsslr lfssiddgsg fafpdqvlam wtqegiqngr eilqsldfsv dekvnllelt
      361 waldnelmtv dsavqqaala cyhqelsyqq gqveqlarer dkarqdlera ekrnlefvke
      421 mddchstleq ltekkikhle qgyrerlsll rseveaerel fweqahrqra alewdvgrlq
      481 aeeaglrekl tlalkensrl qkeivevvek lsdserlalk lqkdlefvlk dklepqsael
      541 laqeerfaav lkeyelkcrd lqdrndelqa eleglwarlp knrhspswsp dgrrrqlpgl
      601 gpagisflgn sapvsietel mmeqvkehyq dlrtqletkv nyyereiaal krnfekerkd
      661 meqarrrevs vlegqkadle elheksqevi wglqeqlqdt argpepeqmg lapcctqalc
      721 glalrhhshl qqirreaeae lsgelsglga lparrdltle leeppqgplp rgsqrseqle
      781 leralklqpc asekraqmcv slaleeeele largkrvdgp sleaemqalp kdglvagsgq
      841 egtrgllplr pgcgerplaw lapgdgrese eaagagprrr qaqdteatqs papapapash
      901 gpserwsrmq pcgvdgdivp kepepfgasa agleqpgare lpllgterda sqtqprmwep
      961 plrpaascrg qaerlqaiqe erarswsrgt qeqaseqqar aegalepgch khsvevarrg
     1021 slpshlqlad pqgswqeqla apeegetkia lerekddmet kllhledvvr alekhvdlre
     1081 ndrlefhrls eentllkndl grvrqeleaa esthdaqrke ievlkkdkek acsemevlnr
     1141 qnqnykdqls qlnvrvlqlg qeasthqaqn eehrvtiqml tqsleevvrs gqqqsdqiqk
     1201 lrveleclnq ehqslqlpws eltqtleesq dqvqgahlrl rqaqaqhlqe vrlvpqdrva
     1261 elhrllslqg eqarrrldaq reehekqlka teerveeaem ilknmemllq ekvdklkeqf
     1321 ekntksdlll kelyvenahl vralqateek qrgaekqsrl leekvralnk lvsriapaal
     1381 sv
//
LOCUS       NP_001182011             150 aa            linear   PRI 27-APR-2025
DEFINITION  testis-expressed protein 22 [Homo sapiens].
ACCESSION   NP_001182011 XP_935474
VERSION     NP_001182011.1
DBSOURCE    REFSEQ: accession NM_001195082.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL928654.1 and BX378619.2.
            
            On Aug 21, 2010 this sequence version replaced XP_935474.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX378619.2, BX378618.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000451127.3/ ENSP00000397002.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..150
                     /product="testis-expressed protein 22"
                     /note="testis-expressed sequence 22 protein; testis
                     expressed gene 22"
                     /calculated_mol_wt=16749
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (C9J3V5.1)"
     CDS             1..150
                     /gene="TEX22"
                     /coded_by="NM_001195082.2:138..590"
                     /db_xref="CCDS:CCDS53916.1"
                     /db_xref="GeneID:647310"
                     /db_xref="HGNC:HGNC:40026"
ORIGIN      
        1 mdsrklsprg kkleshlsqe hrrpplglia awgqpsiqss vqqglqtqdw vcepperrrp
       61 grrwsvside rrrlatlggr erpgaagtql hcrdvvqmva qlvsedvdkd vllphplrst
      121 estnafqafl arsapfwhna tfeasrspps
//
LOCUS       NP_057404               1800 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear pore complex protein Nup98-Nup96 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_057404
VERSION     NP_057404.2
DBSOURCE    REFSEQ: accession NM_016320.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1800)
  AUTHORS   Noura,M., Tomita,S., Yasuda,T., Tsuzuki,S., Kiyoi,H. and
            Hayakawa,F.
  TITLE     NUP98-BPTF promotes oncogenic transformation through PIM1
            upregulation
  JOURNAL   Cancer Med 13 (13), e7445 (2024)
   PUBMED   38940430
  REMARK    GeneRIF: NUP98-BPTF promotes oncogenic transformation through PIM1
            upregulation.
REFERENCE   2  (residues 1 to 1800)
  AUTHORS   Guo,Y., Tao,T., Wu,T., Hou,J. and Lin,W.
  TITLE     Nucleoporin Nup98 is an essential factor for ipo4 dependent protein
            import
  JOURNAL   J Cell Biochem 125 (7), e30573 (2024)
   PUBMED   38780165
  REMARK    GeneRIF: Nucleoporin Nup98 is an essential factor for ipo4
            dependent protein import.
REFERENCE   3  (residues 1 to 1800)
  AUTHORS   Gough,S.M., Slape,C.I. and Aplan,P.D.
  TITLE     NUP98 gene fusions and hematopoietic malignancies: common themes
            and new biologic insights
  JOURNAL   Blood 118 (24), 6247-6257 (2011)
   PUBMED   21948299
  REMARK    GeneRIF: Structural chromosomal rearrangements of NUP98, primarily
            balanced translocations and inversions, are associated with wide
            array of hematopoietic malignancies; NUP98 is known to be fused to
            at least 28 different partner genes in patients. [REVIEW]
            Review article
REFERENCE   4  (residues 1 to 1800)
  AUTHORS   Iwamoto,M., Asakawa,H., Hiraoka,Y. and Haraguchi,T.
  TITLE     Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms
  JOURNAL   Genes Cells 15 (7), 661-669 (2010)
   PUBMED   20545767
  REMARK    Review article
REFERENCE   5  (residues 1 to 1800)
  AUTHORS   Hodel,A.E., Hodel,M.R., Griffis,E.R., Hennig,K.A., Ratner,G.A.,
            Xu,S. and Powers,M.A.
  TITLE     The three-dimensional structure of the autoproteolytic, nuclear
            pore-targeting domain of the human nucleoporin Nup98
  JOURNAL   Mol Cell 10 (2), 347-358 (2002)
   PUBMED   12191480
  REMARK    GeneRIF: The three-dimensional structure of the autoproteolytic,
            nuclear pore-targeting domain of the human nucleoporin Nup98.
REFERENCE   6  (residues 1 to 1800)
  AUTHORS   Griffis,E.R., Altan,N., Lippincott-Schwartz,J. and Powers,M.A.
  TITLE     Nup98 is a mobile nucleoporin with transcription-dependent dynamics
  JOURNAL   Mol Biol Cell 13 (4), 1282-1297 (2002)
   PUBMED   11950939
  REMARK    GeneRIF: Nup98 aids in direction of RNAs to the nuclear pore and
            provide the first potential mechanism for the role of a mobile
            nucleoporin.
REFERENCE   7  (residues 1 to 1800)
  AUTHORS   Rosenblum,J.S. and Blobel,G.
  TITLE     Autoproteolysis in nucleoporin biogenesis
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11370-11375 (1999)
   PUBMED   10500183
REFERENCE   8  (residues 1 to 1800)
  AUTHORS   Fontoura,B.M., Blobel,G. and Matunis,M.J.
  TITLE     A conserved biogenesis pathway for nucleoporins: proteolytic
            processing of a 186-kilodalton precursor generates Nup98 and the
            novel nucleoporin, Nup96
  JOURNAL   J Cell Biol 144 (6), 1097-1112 (1999)
   PUBMED   10087256
REFERENCE   9  (residues 1 to 1800)
  AUTHORS   Nakamura,T., Largaespada,D.A., Lee,M.P., Johnson,L.A.,
            Ohyashiki,K., Toyama,K., Chen,S.J., Willman,C.L., Chen,I.M.,
            Feinberg,A.P., Jenkins,N.A., Copeland,N.G. and Shaughnessy,J.D. Jr.
  TITLE     Fusion of the nucleoporin gene NUP98 to HOXA9 by the chromosome
            translocation t(7;11)(p15;p15) in human myeloid leukaemia
  JOURNAL   Nat Genet 12 (2), 154-158 (1996)
   PUBMED   8563753
REFERENCE   10 (residues 1 to 1800)
  AUTHORS   Radu,A., Moore,M.S. and Blobel,G.
  TITLE     The peptide repeat domain of nucleoporin Nup98 functions as a
            docking site in transport across the nuclear pore complex
  JOURNAL   Cell 81 (2), 215-222 (1995)
   PUBMED   7736573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB084013.1, AF231130.1,
            AF071076.1 and BC012906.1.
            
            On May 30, 2002 this sequence version replaced NP_057404.1.
            
            Summary: Nuclear pore complexes (NPCs) regulate the transport of
            macromolecules between the nucleus and cytoplasm, and are composed
            of many polypeptide subunits, many of which belong to the
            nucleoporin family. This gene belongs to the nucleoporin gene
            family and encodes a 186 kDa precursor protein that undergoes
            autoproteolytic cleavage to generate a 98 kDa nucleoporin and 96
            kDa nucleoporin. The 98 kDa nucleoporin contains a Gly-Leu-Phe-Gly
            (GLGF) repeat domain and participates in many cellular processes,
            including nuclear import, nuclear export, mitotic progression, and
            regulation of gene expression. The 96 kDa nucleoporin is a scaffold
            component of the NPC. Proteolytic cleavage is important for
            targeting of the proteins to the NPC. Translocations between this
            gene and many other partner genes have been observed in different
            leukemias. Rearrangements typically result in chimeras with the
            N-terminal GLGF domain of this gene to the C-terminus of the
            partner gene. Alternative splicing results in multiple transcript
            variants encoding different isoforms, at least two of which are
            proteolytically processed. Some variants lack the region that
            encodes the 96 kDa nucleoporin. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.200264.1, AF231130.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324932.12/ ENSP00000316032.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1800
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..1800
                     /product="nuclear pore complex protein Nup98-Nup96 isoform
                     1 precursor"
                     /note="GLFG-repeat containing nucleoporin; Nup98-Nup96;
                     nucleoporin 98kD; nuclear pore complex protein
                     Nup98-Nup96; nucleoporin 98kDa; nucleoporin 96;
                     NUP98/PHF23 fusion 2 protein"
                     /calculated_mol_wt=195687
     mat_peptide     1..863
                     /product="Nuclear pore complex protein Nup98"
                     /experiment="EXISTENCE:western blot evidence
                     [ECO:0000112][PMID:10087256]"
                     /calculated_mol_wt=89923
     Region          1..156
                     /region_name="FG repeats 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P52948.4)"
     Region          25..>435
                     /region_name="COG4625"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal beta-barrel porin domain [Function unknown]"
                     /db_xref="CDD:443664"
     Region          157..213
                     /region_name="GLEBS, interaction with RAE1.
                     /evidence=ECO:0000269|PubMed:10209021"
                     /note="propagated from UniProtKB/Swiss-Prot (P52948.4)"
     Region          <243..666
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            391..392
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP98-RAP1GDS1 fusion protein. Breakpoint for
                     translocation to form the NUP98-RAP1GDS1 fusion protein.
                     /evidence=ECO:0000269|PubMed:10477737,
                     ECO:0000269|PubMed:16419055; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            469..470
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP98-HOXA9 fusion protein. Breakpoint for translocation
                     to form the NUP98-RAP1GDS1 fusion protein.
                     /evidence=ECO:0000269|PubMed:10477737,
                     ECO:0000269|PubMed:8563753; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Region          495..518
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52948.4)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            514..515
                     /site_type="other"
                     /note="Breakpoint for translocation to form NUP98-CCDC28A;
                     Breakpoint for translocation to form NUP98-PHF23 oncogene;
                     Breakpoint for translocation to form the NUP98-KDM5A
                     fusion protein. /evidence=ECO:0000269|PubMed:16419055;
                     propagated from UniProtKB/Swiss-Prot (P52948.4)"
     Site            586
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Region          597..616
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52948.4)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD9; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Region          645..665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52948.4)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Region          721..863
                     /region_name="Nucleoporin2"
                     /note="Nucleoporin autopeptidase; pfam04096"
                     /db_xref="CDD:461171"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P52948.4)"
     Site            863..864
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:10087256,
                     ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:18287282;
                     propagated from UniProtKB/Swiss-Prot (P52948.4)"
     mat_peptide     864..1800
                     /product="Nuclear pore complex protein Nup96"
                     /experiment="EXISTENCE:western blot
                     evidence[ECO:0000112][PMID:10087256]"
                     /calculated_mol_wt=105913
     Region          869..920
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52948.4)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            880
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            917
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            983
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            1006
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            1011
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P52948.4)"
     Site            1026
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            1043
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P52948.4)"
     Site            1047
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD9; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            1053
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Site            1312
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD9; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     Region          1315..1606
                     /region_name="Nup96"
                     /note="Nuclear protein 96; pfam12110"
                     /db_xref="CDD:463462"
     Site            1755
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD9; propagated from
                     UniProtKB/Swiss-Prot (P52948.4)"
     CDS             1..1800
                     /gene="NUP98"
                     /gene_synonym="ADIR2; NUP196; NUP96; Nup98-96"
                     /coded_by="NM_016320.5:184..5586"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS7746.1"
                     /db_xref="GeneID:4928"
                     /db_xref="HGNC:HGNC:8068"
                     /db_xref="MIM:601021"
ORIGIN      
        1 mfnksfgtpf gggtggfgtt stfgqntgfg ttsggafgts afgssnntgg lfgnsqtkpg
       61 glfgtssfsq patststgfg fgtstgtant lfgtastgts lfssqnnafa qnkptgfgnf
      121 gtstssgglf gttnttsnpf gstsgslfgp ssftaaptgt tikfnpptgt dtmvkagvst
      181 nistkhqcit amkeyesksl eelrledyqa nrkgpqnqvg agtttglfgs spatssatgl
      241 fsssttnsgf aygqnktafg tsttgfgtnp gglfgqqnqq ttslfskpfg qatttqntgf
      301 sfgntstigq pstntmglfg vtqasqpggl fgtatntstg tafgtgtglf gqtntgfgav
      361 gstlfgnnkl ttfgssttsa psfgttsggl fgfgtntsgn sifgskpapg tlgtglgagf
      421 gtalgagqas lfgnnqpkig gplgtgafga pgfntttatl gfgapqapva ltdpnasaaq
      481 qavlqqhins ltyspfgdsp lfrnpmsdpk kkeerlkptn paaqkalttp thykltprpa
      541 trvrpkalqt tgtakshlfd gldddepsla ngafmpkksi kklvlknlnn snlfspvnrd
      601 senlaspsey pengerfsfl skpvdenhqq dgdedslvsh fytnpiakpi pqtpesagnk
      661 hsnsnsvddt ivalnmraal rnglegssee tsfhdeslqd dreeiennsy hmhpagiilt
      721 kvgyytipsm ddlakitnek gecivsdfti grkgygsiyf egdvnltnln lddivhirrk
      781 evvvylddnq kppvgeglnr kaevtldgvw ptdktsrcli kspdrladin yegrleavsr
      841 kqgaqfkeyr petgswvfkv shfskyglqd sdeeeeehps ktstkklkta plppasqttp
      901 lqmalngkpa pppqsqspev eqlgrvveld sdmvditqep vldtmleesm pedqepvsas
      961 thiasslgin phvlqimkas lltdeedvdm aldqrfsrlp skadtsqeic sprlpisash
     1021 ssktrslvgg llqskftsga flspsvsvqe crtpraaslm nipstsswsv pppltsvftm
     1081 pspapevplk tvgtrrqlgl vpreksvtyg kgkllmdmal fmgrsfrvgw gpnwtlansg
     1141 eqlngshele nhqiadsmef gflpnpvavk pltespfkvh leklslrqrk pdedmklyqt
     1201 plelklkhst vhvdelcpli vpnlgvavih dyadwvkeas gdlpeaqivk hwsltwtlce
     1261 alwghlkeld sqlnepreyi qilerrrafs rwlsctatpq ieeevsltqk nspveavfsy
     1321 ltgkriseac slaqqsgdhr lalllsqfvg sqsvrelltm qlvdwhqlqa dsfiqderlr
     1381 ifallagkpv wqlsekkqin vcsqldwkrs laihlwyllp ptasisrals myeeafqnts
     1441 dsdryacspl psylegsgcv iaeeqnsqtp lrdvcfhllk lysdrhydln qlleprsita
     1501 dpldyrlswh lwevlralny thlsaqcegv lqasyagqle seglwewaif vllhidnsgi
     1561 rekavrellt rhcqlletpe swaketfltq klrvpakwih eakavrahme sdkhlealcl
     1621 fkaehwnrch kliirhlasd aiinenydyl kgfledlapp erssliqdwe tsglvyldyi
     1681 rviemlrhiq qvdcsgndle qlhikvtslc srieqiqcys akdrlaqsdm akrvanllrv
     1741 vlslhhppdr tsdstpdpqr vplrllaphi grlpmpedya mdelrsltqs ylrelavgsl
//
LOCUS       NP_001078998             525 aa            linear   ROD 27-APR-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 7
            isoform 1 [Mus musculus].
ACCESSION   NP_001078998 XP_001480176 XP_911280
VERSION     NP_001078998.1
DBSOURCE    REFSEQ: accession NM_001085529.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606971.22.
            
            On or before Jul 25, 2007 this sequence version replaced
            XP_911280.1, XP_001480176.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN00849377, SAMN00849378
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 81.04 cM"
     Protein         1..525
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 7 isoform 1"
                     /note="glucose transporter type 7"
                     /calculated_mol_wt=57051
     Region          26..490
                     /region_name="MFS_GLUT_Class2"
                     /note="Class 2 Glucose transporters (GLUTs) of the Major
                     Facilitator Superfamily; cd17432"
                     /db_xref="CDD:340990"
     Site            order(38,42,185,188..189,192,307..308,312..313,316..317,
                     344,406..407,410..411,415,438..439,442)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340990"
     CDS             1..525
                     /gene="Slc2a7"
                     /gene_synonym="GLUT-7"
                     /coded_by="NM_001085529.2:86..1663"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS51385.1"
                     /db_xref="GeneID:435818"
                     /db_xref="MGI:MGI:3650865"
ORIGIN      
        1 medkeigtpl plphsearlq ptlvlttlsa afgsvfqygy niavintphk vgtsnrwgpv
       61 fqvlksfynd thferhgtfm destllllws ctvsmfplgg llgslvvglm vnkwgrkgtl
      121 linnvfaits avlmgvskva rafeliilsr vlvgicagia ystlpmylge lapqnlrgal
      181 gtmtevfvii gvllaqifsl qailgnatgw pillaltgvp aviqllslpf fpesprytli
      241 ekgdeetarq alrrlrgqny nveaemeemr teerteqaeg rlsvlnlftf rplrwqlisi
      301 vvlmagqqls ginavnyyad viytsagvdp tqsqyvtlgs gvinlvmtlv saviierlgr
      361 rilllsgyai ccsaclvltv alllqstape lsylsivcvf syivghsigp spvpsvvrte
      421 ivlqssrtaa ftvdgavhwl tnfivgltfp siqvaigays flvfagvcil taayiyvvip
      481 etkgrtfvei ncafakrngv efpeekevat akphtpslpt ketaf
//
LOCUS       NP_005976                264 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein SNAI1 [Homo sapiens].
ACCESSION   NP_005976
VERSION     NP_005976.2
DBSOURCE    REFSEQ: accession NM_005985.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Ryu,K.J., Lee,K.W., Park,S.H., Kim,T., Hong,K.S., Kim,H., Kim,M.,
            Ok,D.W., Kwon,G.N.B., Park,Y.J., Kwon,H.K., Hwangbo,C., Kim,K.D.,
            Lee,J.E. and Yoo,J.
  TITLE     Chaperone-mediated autophagy modulates Snail protein stability:
            implications for breast cancer metastasis
  JOURNAL   Mol Cancer 23 (1), 227 (2024)
   PUBMED   39390584
  REMARK    GeneRIF: Chaperone-mediated autophagy modulates Snail protein
            stability: implications for breast cancer metastasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Li,M., Zhang,L., Guan,T., Huang,L., Zhu,Y., Wen,Y., Ma,X., Yang,X.,
            Wan,R., Chen,J., Zhang,C., Wang,F., Tang,H. and Liu,T.
  TITLE     Energy stress-activated AMPK phosphorylates Snail1 and suppresses
            its stability and oncogenic function
  JOURNAL   Cancer Lett 595, 216987 (2024)
   PUBMED   38815798
  REMARK    GeneRIF: Energy stress-activated AMPK phosphorylates Snail1 and
            suppresses its stability and oncogenic function.
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Fang,Y., Wang,Y., Ma,H., Guo,Y., Xu,R., Chen,X., Chen,X., Lv,Y.,
            Li,P. and Gao,Y.
  TITLE     TFAP2A downregulation mediates tumor-suppressive effect of miR-8072
            in triple-negative breast cancer via inhibiting SNAI1 transcription
  JOURNAL   Breast Cancer Res 26 (1), 103 (2024)
   PUBMED   38890750
  REMARK    GeneRIF: TFAP2A downregulation mediates tumor-suppressive effect of
            miR-8072 in triple-negative breast cancer via inhibiting SNAI1
            transcription.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Wu,Z., Zhang,Q., Wang,H., Zhou,S., Fu,B., Fang,L., Cheng,J.C. and
            Sun,Y.P.
  TITLE     Growth differentiation factor-11 upregulates matrix
            metalloproteinase 2 expression by inducing Snail in human
            extravillous trophoblast cells
  JOURNAL   Mol Cell Endocrinol 585, 112190 (2024)
   PUBMED   38369181
  REMARK    GeneRIF: Growth differentiation factor-11 upregulates matrix
            metalloproteinase 2 expression by inducing Snail in human
            extravillous trophoblast cells.
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Wang,L., Gao,J., Zheng,S., Luo,Z., Xu,Z., Che,H. and Wang,Z.
  TITLE     CXCR2/Snail-1-Induced Epithelial-Mesenchymal Transition in the
            Formation and Progression of RCC with Inferior Vena Cava Tumour
            Thrombus
  JOURNAL   Arch Esp Urol 77 (3), 292-302 (2024)
   PUBMED   38715171
  REMARK    GeneRIF: CXCR2/Snail-1-Induced Epithelial-Mesenchymal Transition in
            the Formation and Progression of RCC with Inferior Vena Cava Tumour
            Thrombus.
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Okubo,T., Truong,T.K., Yu,B., Itoh,T., Zhao,J., Grube,B., Zhou,D.
            and Chen,S.
  TITLE     Down-regulation of promoter 1.3 activity of the human aromatase
            gene in breast tissue by zinc-finger protein, snail (SnaH)
  JOURNAL   Cancer Res 61 (4), 1338-1346 (2001)
   PUBMED   11245431
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Smith,S., Metcalfe,J.A. and Elgar,G.
  TITLE     Identification and analysis of two snail genes in the pufferfish
            (Fugu rubripes) and mapping of human SNA to 20q
  JOURNAL   Gene 247 (1-2), 119-128 (2000)
   PUBMED   10773451
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Batlle,E., Sancho,E., Franci,C., Dominguez,D., Monfar,M.,
            Baulida,J. and Garcia De Herreros,A.
  TITLE     The transcription factor snail is a repressor of E-cadherin gene
            expression in epithelial tumour cells
  JOURNAL   Nat Cell Biol 2 (2), 84-89 (2000)
   PUBMED   10655587
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Paznekas,W.A., Okajima,K., Schertzer,M., Wood,S. and Jabs,E.W.
  TITLE     Genomic organization, expression, and chromosome location of the
            human SNAIL gene (SNAI1) and a related processed pseudogene
            (SNAI1P)
  JOURNAL   Genomics 62 (1), 42-49 (1999)
   PUBMED   10585766
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Twigg,S.R. and Wilkie,A.O.
  TITLE     Characterisation of the human snail (SNAI1) gene and exclusion as a
            major disease gene in craniosynostosis
  JOURNAL   Hum Genet 105 (4), 320-326 (1999)
   PUBMED   10543399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA972913.1 and BC012910.1.
            
            On Feb 19, 2002 this sequence version replaced NP_005976.1.
            
            Summary: The Drosophila embryonic protein snail is a zinc finger
            transcriptional repressor which downregulates the expression of
            ectodermal genes within the mesoderm. The nuclear protein encoded
            by this gene is structurally similar to the Drosophila snail
            protein, and is also thought to be critical for mesoderm formation
            in the developing embryo. At least two variants of a similar
            processed pseudogene have been found on chromosome 2. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012910.1, SRR5189661.136537.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000244050.3/ ENSP00000244050.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.13"
     Protein         1..264
                     /product="zinc finger protein SNAI1"
                     /note="snail 1 zinc finger protein; snail 1 homolog; snail
                     family zinc finger 1; protein sna; protein snail homolog
                     1"
                     /calculated_mol_wt=28952
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95863.2)"
     Region          1..20
                     /region_name="SNAG domain.
                     /evidence=ECO:0000305|PubMed:20389281,
                     ECO:0000305|PubMed:21300290"
                     /note="propagated from UniProtKB/Swiss-Prot (O95863.2)"
     Region          2..7
                     /region_name="Required and sufficient for interaction with
                     KDM1A. /evidence=ECO:0000269|PubMed:20389281,
                     ECO:0000269|PubMed:23721412"
                     /note="propagated from UniProtKB/Swiss-Prot (O95863.2)"
     Region          10..40
                     /region_name="LATS2 binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O95863.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:19923321; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19923321; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     Region          86..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95863.2)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:19923321; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     Region          95..100
                     /region_name="Destruction motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O95863.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20305697,
                     ECO:0000305|PubMed:15448698; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:15448698; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15647282,
                     ECO:0000269|PubMed:19923321, ECO:0000305|PubMed:15448698;
                     propagated from UniProtKB/Swiss-Prot (O95863.2)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15647282,
                     ECO:0000269|PubMed:19923321, ECO:0000305|PubMed:15448698;
                     propagated from UniProtKB/Swiss-Prot (O95863.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:15448698; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     Site            112
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:20959806; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:15448698; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:15448698; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     Region          120..151
                     /region_name="Required for FBXL14-triggered degradation"
                     /note="propagated from UniProtKB/Swiss-Prot (O95863.2)"
     Region          151..264
                     /region_name="Required for nuclear localization and
                     interaction with KPNB1, NOTCH1 and PARP1.
                     /evidence=ECO:0000269|PubMed:21577210,
                     ECO:0000269|PubMed:22128911"
                     /note="propagated from UniProtKB/Swiss-Prot (O95863.2)"
     Region          156..176
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          182..202
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(187,189,191,193..194,197..198,201,215,217,221..222,
                     225..226,229,243,245,247,249..250,253..254)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          195..218
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by LATS2.
                     /evidence=ECO:0000269|PubMed:21952048; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     Region          208..230
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          210..230
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          238..255
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK1.
                     /evidence=ECO:0000269|PubMed:15833848; propagated from
                     UniProtKB/Swiss-Prot (O95863.2)"
     CDS             1..264
                     /gene="SNAI1"
                     /gene_synonym="dJ710H13.1; SLUGH2; SNA; SNAH; SNAIL;
                     SNAIL1"
                     /coded_by="NM_005985.4:81..875"
                     /db_xref="CCDS:CCDS13423.1"
                     /db_xref="GeneID:6615"
                     /db_xref="HGNC:HGNC:11128"
                     /db_xref="MIM:604238"
ORIGIN      
        1 mprsflvrkp sdpnrkpnys elqdsnpeft fqqpydqahl laaipppeil nptaslpmli
       61 wdsvlapqaq piawaslrlq esprvaelts lsdedsgkgs qppsppspap ssfsstsvss
      121 leaeayaafp glgqvpkqla qlseakdlqa rkafnckycn keylslgalk mhirshtlpc
      181 vcgtcgkafs rpwllqghvr thtgekpfsc phcsrafadr snlrahlqth sdvkkyqcqa
      241 cartfsrmsl lhkhqesgcs gcpr
//
LOCUS       NP_002230                501 aa            linear   PRI 27-APR-2025
DEFINITION  G protein-activated inward rectifier potassium channel 1 isoform 1
            [Homo sapiens].
ACCESSION   NP_002230
VERSION     NP_002230.1
DBSOURCE    REFSEQ: accession NM_002239.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Black,K.A., He,S., Jin,R., Miller,D.M., Bolla,J.R., Clarke,O.B.,
            Johnson,P., Windley,M., Burns,C.J., Hill,A.P., Laver,D.,
            Robinson,C.V., Smith,B.J. and Gulbis,J.M.
  TITLE     A constricted opening in Kir channels does not impede potassium
            conduction
  JOURNAL   Nat Commun 11 (1), 3024 (2020)
   PUBMED   32541684
  REMARK    GeneRIF: A constricted opening in Kir channels does not impede
            potassium conduction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Schratter,G., Scheruebel,S., Langthaler,S., Ester,K., Pelzmann,B.,
            Ghaffari-Tabrizi-Wizsy,N., Rezania,S., Gorischek,A., Platzer,D.,
            Zorn-Pauly,K., Ahammer,H., Prokesch,A., Stanzer,S., Devaney,T.T.J.,
            Schmidt,K., Jahn,S.W., Prassl,R., Bauernhofer,T. and
            Schreibmayer,W.
  TITLE     GIRK1 triggers multiple cancer-related pathways in the benign
            mammary epithelial cell line MCF10A
  JOURNAL   Sci Rep 9 (1), 19277 (2019)
   PUBMED   31848385
  REMARK    GeneRIF: GIRK1 triggers multiple cancer-related pathways in the
            benign mammary epithelial cell line MCF10A.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Yamada,N., Asano,Y., Fujita,M., Yamazaki,S., Inanobe,A.,
            Matsuura,N., Kobayashi,H., Ohno,S., Ebana,Y., Tsukamoto,O.,
            Ishino,S., Takuwa,A., Kioka,H., Yamashita,T., Hashimoto,N.,
            Zankov,D.P., Shimizu,A., Asakura,M., Asanuma,H., Kato,H.,
            Nishida,Y., Miyashita,Y., Shinomiya,H., Naiki,N., Hayashi,K.,
            Makiyama,T., Ogita,H., Miura,K., Ueshima,H., Komuro,I.,
            Yamagishi,M., Horie,M., Kawakami,K., Furukawa,T., Koizumi,A.,
            Kurachi,Y., Sakata,Y., Minamino,T., Kitakaze,M. and Takashima,S.
  TITLE     Mutant KCNJ3 and KCNJ5 Potassium Channels as Novel Molecular
            Targets in Bradyarrhythmias and Atrial Fibrillation
  JOURNAL   Circulation 139 (18), 2157-2169 (2019)
   PUBMED   30764634
  REMARK    GeneRIF: Mutant KCNJ3 and KCNJ5 Potassium Channels as Novel
            Molecular Targets in Bradyarrhythmias and Atrial Fibrillation.
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Tateyama,M. and Kubo,Y.
  TITLE     Gi/o-coupled muscarinic receptors co-localize with GIRK channel for
            efficient channel activation
  JOURNAL   PLoS One 13 (9), e0204447 (2018)
   PUBMED   30240440
  REMARK    GeneRIF: Gi/o-coupled muscarinic receptors co-localize with GIRK
            channel for efficient channel activation
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Kammerer,S., Sokolowski,A., Hackl,H., Platzer,D., Jahn,S.W.,
            El-Heliebi,A., Schwarzenbacher,D., Stiegelbauer,V., Pichler,M.,
            Rezania,S., Fiegl,H., Peintinger,F., Regitnig,P., Hoefler,G.,
            Schreibmayer,W. and Bauernhofer,T.
  TITLE     KCNJ3 is a new independent prognostic marker for estrogen receptor
            positive breast cancer patients
  JOURNAL   Oncotarget 7 (51), 84705-84717 (2016)
   PUBMED   27835900
  REMARK    GeneRIF: these data suggest that patients with estrogen receptor
            positive breast cancer might be stratified into high risk and low
            risk groups based on the KCNJ3 levels in the tumor
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Signorini,S., Liao,Y.J., Duncan,S.A., Jan,L.Y. and Stoffel,M.
  TITLE     Normal cerebellar development but susceptibility to seizures in
            mice lacking G protein-coupled, inwardly rectifying K+ channel
            GIRK2
  JOURNAL   Proc Natl Acad Sci U S A 94 (3), 923-927 (1997)
   PUBMED   9023358
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Liao,Y.J., Jan,Y.N. and Jan,L.Y.
  TITLE     Heteromultimerization of G-protein-gated inwardly rectifying K+
            channel proteins GIRK1 and GIRK2 and their altered expression in
            weaver brain
  JOURNAL   J Neurosci 16 (22), 7137-7150 (1996)
   PUBMED   8929423
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Schoots,O., Yue,K.T., MacDonald,J.F., Hampson,D.R., Nobrega,J.N.,
            Dixon,L.M. and Van Tol,H.H.
  TITLE     Cloning of a G protein-activated inwardly rectifying potassium
            channel from human cerebellum
  JOURNAL   Brain Res Mol Brain Res 39 (1-2), 23-30 (1996)
   PUBMED   8804710
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Chan,K.W., Langan,M.N., Sui,J.L., Kozak,J.A., Pabon,A., Ladias,J.A.
            and Logothetis,D.E.
  TITLE     A recombinant inwardly rectifying potassium channel coupled to
            GTP-binding proteins
  JOURNAL   J Gen Physiol 107 (3), 381-397 (1996)
   PUBMED   8868049
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Stoffel,M., Espinosa,R. 3rd, Powell,K.L., Philipson,L.H., Le
            Beau,M.M. and Bell,G.I.
  TITLE     Human G-protein-coupled inwardly rectifying potassium channel
            (GIRK1) gene (KCNJ3): localization to chromosome 2 and
            identification of a simple tandem repeat polymorphism
  JOURNAL   Genomics 21 (1), 254-256 (1994)
   PUBMED   8088798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U50964.1 and AC093633.3.
            
            Summary: Potassium channels are present in most mammalian cells,
            where they participate in a wide range of physiologic responses.
            The protein encoded by this gene is an integral membrane protein
            and inward-rectifier type potassium channel. The encoded protein,
            which has a greater tendency to allow potassium to flow into a cell
            rather than out of a cell, is controlled by G-proteins and plays an
            important role in regulating heartbeat. It associates with three
            other G-protein-activated potassium channels to form a
            heteromultimeric pore-forming complex that also couples to
            neurotransmitter receptors in the brain and whereby channel
            activation can inhibit action potential firing by hyperpolarizing
            the plasma membrane. These multimeric G-protein-gated
            inwardly-rectifying potassium (GIRK) channels may play a role in
            the pathophysiology of epilepsy, addiction, Down's syndrome,
            ataxia, and Parkinson's disease. Alternative splicing results in
            multiple transcript variants encoding distinct proteins. [provided
            by RefSeq, May 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1; also known as
            GIRK1a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.54688.1,
                                           SRR1803613.164476.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295101.3/ ENSP00000295101.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.1"
     Protein         1..501
                     /product="G protein-activated inward rectifier potassium
                     channel 1 isoform 1"
                     /note="inward rectifier K+ channel KIR3.1; G
                     protein-activated inward rectifier potassium channel 1;
                     GIRK-1; inward rectifier K(+) channel Kir3.1; potassium
                     channel, inwardly rectifying subfamily J member 3;
                     potassium voltage-gated channel subfamily J member 3"
                     /calculated_mol_wt=56472
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48549.1)"
     Region          47..187
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            81..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48549.1)"
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:10889209; propagated from
                     UniProtKB/Swiss-Prot (P48549.1)"
     Region          143..148
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P48549.1)"
     Site            158..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48549.1)"
     Site            173
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P48549.1)"
     Region          182..209
                     /region_name="Polyphosphoinositide (PIP2)-binding.
                     /evidence=ECO:0000250|UniProtKB:P63251"
                     /note="propagated from UniProtKB/Swiss-Prot (P48549.1)"
     Region          194..364
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63250; propagated from
                     UniProtKB/Swiss-Prot (P48549.1)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63250; propagated from
                     UniProtKB/Swiss-Prot (P48549.1)"
     CDS             1..501
                     /gene="KCNJ3"
                     /gene_synonym="GIRK1; KGA; KIR3.1"
                     /coded_by="NM_002239.4:82..1587"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2200.1"
                     /db_xref="GeneID:3760"
                     /db_xref="HGNC:HGNC:6264"
                     /db_xref="MIM:601534"
ORIGIN      
        1 msalrrkfgd dyqvvttsss gsglqpqgpg qdpqqqlvpk kkrqrfvdkn grcnvqhgnl
       61 gsetsrylsd lfttlvdlkw rwnlfifilt ytvawlfmas mwwviaytrg dlnkahvgny
      121 tpcvanvynf psaflffiet eatigygyry itdkcpegii lflfqsilgs ivdafligcm
      181 fikmsqpkkr aetlmfseha vismrdgklt lmfrvgnlrn shmvsaqirc kllksrqtpe
      241 geflpldqle ldvgfstgad qlflvsplti chvidakspf ydlsqrsmqt eqfeivvile
      301 givettgmtc qartsytede vlwghrffpv isleegffkv dysqfhatfe vptppysvke
      361 qeemllmssp liapaitnsk erhnsvecld glddittklp sklqkitgre dfpkkllrms
      421 sttsekaysl gdlpmklqri ssvpgnseek lvskttkmls dpmsqsvadl ppklqkmagg
      481 aarmegnlpa klrkmnsdrf t
//
LOCUS       NP_001010844             260 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-1 receptor-associated kinase 1-binding protein 1 [Homo
            sapiens].
ACCESSION   NP_001010844 XP_059729
VERSION     NP_001010844.1
DBSOURCE    REFSEQ: accession NM_001010844.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 260)
  AUTHORS   He,J., Kelly,T.N., Zhao,Q., Li,H., Huang,J., Wang,L., Jaquish,C.E.,
            Sung,Y.J., Shimmin,L.C., Lu,F., Mu,J., Hu,D., Ji,X., Shen,C.,
            Guo,D., Ma,J., Wang,R., Shen,J., Li,S., Chen,J., Mei,H., Chen,C.S.,
            Chen,S., Chen,J., Li,J., Cao,J., Lu,X., Wu,X., Rice,T.K., Gu,C.C.,
            Schwander,K., Hamm,L.L., Liu,D., Rao,D.C., Hixson,J.E. and Gu,D.
  TITLE     Genome-wide association study identifies 8 novel loci associated
            with blood pressure responses to interventions in Han Chinese
  JOURNAL   Circ Cardiovasc Genet 6 (6), 598-607 (2013)
   PUBMED   24165912
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Luo,Y., Kwon,H.J., Montano,S., Georgiadis,M., Goebl,M.G. and
            Harrington,M.A.
  TITLE     Phosphorylation of SIMPL modulates RelA-associated
            NF-kappaB-dependent transcription
  JOURNAL   Am J Physiol Cell Physiol 292 (3), C1013-C1023 (2007)
   PUBMED   17079333
  REMARK    GeneRIF: Together, these studies reveal that phosphorylation of the
            SIMPL protein plays a critical role in SIMPL regulation by
            affecting both SIMPL subcellular localization and the p65
            coactivator function of SIMPL.
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Kwon,H.J., Breese,E.H., Vig-Varga,E., Luo,Y., Lee,Y., Goebl,M.G.
            and Harrington,M.A.
  TITLE     Tumor necrosis factor alpha induction of NF-kappaB requires the
            novel coactivator SIMPL
  JOURNAL   Mol Cell Biol 24 (21), 9317-9326 (2004)
   PUBMED   15485901
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL450327.12, BC112253.1 and CB321683.1.
            
            On Feb 16, 2005 this sequence version replaced XP_059729.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.685659.1, BU195215.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369940.7/ ENSP00000358956.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..260
                     /product="interleukin-1 receptor-associated kinase
                     1-binding protein 1"
                     /note="ActA binding protein 3; IRAK1-binding protein 1"
                     /calculated_mol_wt=28975
     Region          30..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VVH5.1)"
     Region          53..197
                     /region_name="SIMPL"
                     /note="Protein of unknown function (DUF541); pfam04402"
                     /db_xref="CDD:461292"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESJ7; propagated from
                     UniProtKB/Swiss-Prot (Q5VVH5.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESJ7; propagated from
                     UniProtKB/Swiss-Prot (Q5VVH5.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESJ7; propagated from
                     UniProtKB/Swiss-Prot (Q5VVH5.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESJ7; propagated from
                     UniProtKB/Swiss-Prot (Q5VVH5.1)"
     Region          240..260
                     /region_name="Required for nuclear localization (NLS).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VVH5.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESJ7; propagated from
                     UniProtKB/Swiss-Prot (Q5VVH5.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESJ7; propagated from
                     UniProtKB/Swiss-Prot (Q5VVH5.1)"
     CDS             1..260
                     /gene="IRAK1BP1"
                     /gene_synonym="AIP70; SIMPL"
                     /coded_by="NM_001010844.4:27..809"
                     /db_xref="CCDS:CCDS34488.1"
                     /db_xref="GeneID:134728"
                     /db_xref="HGNC:HGNC:17368"
                     /db_xref="MIM:615375"
ORIGIN      
        1 mslqktpptr vfvelvpwad rsrennlasg retlpglrhp lsstqaqtat revqvsgtse
       61 vsagpdraqv vvrvsstkea aaeakksvcr rldyitqslq qqgvqaenit vtkdfrrven
      121 ayhmeaevci tftefgkmqn icnflvekld ssvvisppqf yhtpgsvenl rrqaclvave
      181 nawrkaqevc nlvgqtlgkp llikeeetke wegqiddhqs srlsssltvq qkiksatiha
      241 askvfitfev kgkekrkkhl
//
LOCUS       NP_001356874             521 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 12 [Homo
            sapiens].
ACCESSION   NP_001356874
VERSION     NP_001356874.1
DBSOURCE    REFSEQ: accession NM_001369945.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.92621.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..521
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 12"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=59181
     Region          233..272
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..521
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369945.1:847..2412"
                     /note="isoform 12 is encoded by transcript variant 28"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mpllelkdiv lylcdtcttl wafldifpla cqtfqkhdfc yrlasfyeaa ipemesaikk
       61 rrledskllg dlwqrlshsr kklmeifhii lnqicllpil esscdniqgf ieeflqifss
      121 llqekrflrd ydalfpvaed isllqqassv ldetrtayil qavesawegv drrkatdakd
      181 psvieepnge pngvtvtaea vsqasshpen seeeecmgaa aavgpamcgv eldslisqvk
      241 dllpdlgegf ilacleyyhy dpeqvinnil eerlaptlsq ldrnldremk pdptplltsr
      301 hnvfqndefd vfsrdsvdls rvhkgkstrk eentrsllnd kravaaqrqr yeqysvvvee
      361 vplqpgeslp yhsvyyedey ddtydgnqvg andadsddel isrrpftipq vlrtkvpreg
      421 qeeddddeed dadeeapkpd hfvqdpavlr ekaearrmaf lakkgyrhds stavagsprg
      481 hgqsrettqe rrkkeankat ranhnrrtma drkrskgmip s
//
LOCUS       NP_001299834             849 aa            linear   ROD 27-APR-2025
DEFINITION  small conductance calcium-activated potassium channel protein 2
            isoform SK2-L [Mus musculus].
ACCESSION   NP_001299834 XP_006525701
VERSION     NP_001299834.1
DBSOURCE    REFSEQ: accession NM_001312905.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Lin,T.F., Busch,S.E. and Hansel,C.
  TITLE     Intrinsic and synaptic determinants of receptive field plasticity
            in Purkinje cells of the mouse cerebellum
  JOURNAL   Nat Commun 15 (1), 4645 (2024)
   PUBMED   38821918
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 849)
  AUTHORS   Xu,J., Zhang,D., Ma,Y., Du,H., Wang,Y., Luo,W., Wang,R. and Yi,F.
  TITLE     ROS in diabetic atria regulate SK2 degradation by Atrogin-1 through
            the NF-kappaB signaling pathway
  JOURNAL   J Biol Chem 300 (3), 105735 (2024)
   PUBMED   38336298
  REMARK    GeneRIF: ROS in diabetic atria regulate SK2 degradation by
            Atrogin-1 through the NF-kappaB signaling pathway.
REFERENCE   3  (residues 1 to 849)
  AUTHORS   Peng,X., Chen,P., Zhang,Y., Wu,K., Ji,N., Gao,J., Wang,H.,
            Zhang,Y.M., Xu,T. and Hua,R.
  TITLE     MPP2 interacts with SK2 to rescue the excitability of glutamatergic
            neurons in the BLA and facilitate the extinction of conditioned
            fear in mice
  JOURNAL   CNS Neurosci Ther 30 (1), e14362 (2024)
   PUBMED   37469037
  REMARK    GeneRIF: MPP2 interacts with SK2 to rescue the excitability of
            glutamatergic neurons in the BLA and facilitate the extinction of
            conditioned fear in mice.
REFERENCE   4  (residues 1 to 849)
  AUTHORS   Chen,H., Xia,F., Chen,X., Cai,Y. and Jin,Z.
  TITLE     Ablation of small conductance calcium-activated potassium type-2
            channel (SK2) delays occurrence of bupivacaine-induced
            cardiotoxicity in isolated mouse hearts
  JOURNAL   Hum Exp Toxicol 40 (3), 464-471 (2021)
   PUBMED   32909839
REFERENCE   5  (residues 1 to 849)
  AUTHORS   Wu,K., Gao,J.H., Hua,R., Peng,X.H., Wang,H. and Zhang,Y.M.
  TITLE     Predisposition of Neonatal Maternal Separation to Visceral
            Hypersensitivity via Downregulation of Small-Conductance
            Calcium-Activated Potassium Channel Subtype 2 (SK2) in Mice
  JOURNAL   Neural Plast 2020, 8876230 (2020)
   PUBMED   33029124
  REMARK    GeneRIF: Predisposition of Neonatal Maternal Separation to Visceral
            Hypersensitivity via Downregulation of Small-Conductance
            Calcium-Activated Potassium Channel Subtype 2 (SK2) in Mice.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 849)
  AUTHORS   Callizot,N., Guenet,J.L., Baillet,C., Warter,J.M. and Poindron,P.
  TITLE     The frissonnant mutant mouse, a model of dopamino-sensitive,
            inherited motor syndrome
  JOURNAL   Neurobiol Dis 8 (3), 447-458 (2001)
   PUBMED   11442353
REFERENCE   7  (residues 1 to 849)
  AUTHORS   Bond,C.T., Sprengel,R., Bissonnette,J.M., Kaufmann,W.A.,
            Pribnow,D., Neelands,T., Storck,T., Baetscher,M., Jerecic,J.,
            Maylie,J., Knaus,H.G., Seeburg,P.H. and Adelman,J.P.
  TITLE     Respiration and parturition affected by conditional overexpression
            of the Ca2+-activated K+ channel subunit, SK3
  JOURNAL   Science 289 (5486), 1942-1946 (2000)
   PUBMED   10988076
REFERENCE   8  (residues 1 to 849)
  AUTHORS   Chan,A.C., van Oers,N.S., Tran,A., Turka,L., Law,C.L., Ryan,J.C.,
            Clark,E.A. and Weiss,A.
  TITLE     Differential expression of ZAP-70 and Syk protein tyrosine kinases,
            and the role of this family of protein tyrosine kinases in TCR
            signaling
  JOURNAL   J Immunol 152 (10), 4758-4766 (1994)
   PUBMED   8176201
REFERENCE   9  (residues 1 to 849)
  AUTHORS   Davisson,M.T., Cook,S.A., Johnson,K.R. and Eicher,E.M.
  TITLE     Balding: a new mutation on mouse chromosome 18 causing hair loss
            and immunological defects
  JOURNAL   J Hered 85 (2), 134-136 (1994)
   PUBMED   8182278
REFERENCE   10 (residues 1 to 849)
  AUTHORS   Lane,P.W., Searle,A.G., Beechey,C.V. and Eicher,E.
  TITLE     Chromosome 18 of the house mouse
  JOURNAL   J Hered 72 (6), 409-412 (1981)
   PUBMED   6949984
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099590.16, AC122852.2, AC121957.2 and AC101593.16.
            
            On Aug 22, 2015 this sequence version replaced XP_006525701.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (SK2-L).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK033158.1, SRR10662772.2393600.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849390, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 24.34 cM"
     Protein         1..849
                     /product="small conductance calcium-activated potassium
                     channel protein 2 isoform SK2-L"
                     /note="small conductance calcium-activated potassium
                     channel protein 2; small conductance calcium-activated
                     potassium channel subfamily N member 2"
                     /calculated_mol_wt=92615
     Region          391..500
                     /region_name="SK_channel"
                     /note="Calcium-activated SK potassium channel; pfam03530"
                     /db_xref="CDD:460958"
     Region          589..668
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          682..757
                     /region_name="CaMBD"
                     /note="Calmodulin binding domain; smart01053"
                     /db_xref="CDD:198121"
     CDS             1..849
                     /gene="Kcnn2"
                     /gene_synonym="bc; fri; KCa2.2; SK2; SKCA2"
                     /coded_by="NM_001312905.2:822..3371"
                     /note="isoform SK2-L is encoded by transcript variant 1"
                     /db_xref="GeneID:140492"
                     /db_xref="MGI:MGI:2153182"
ORIGIN      
        1 mfgrtckcdv mpivlvrptn rtrrldstga gmgpsshqqq esplptithc agcttawspc
       61 sfnssdmetp lqfqrgffpe qppppprssh lhcqqqqqsq dkpcapfapl phphhhphla
      121 hqqpgsggss pclrcnscas sgapaagaga gdnlslllrt sspggafrtr tssplsgssc
      181 ccccssrrgs qlnvseltps shasalrqqy aqqpasasqy hqchslqpat sptgslgslg
      241 sgpplshhhh hphpahhqhh qpqarresnp fteiamsscr ynggvmrpls nlsssrrnlq
      301 emdseaqplq ppasvvgggg gasspsaaaa asssapeivv skpehnnsnn lalygtgggg
      361 stggggggsg hgsssgtkss kkknqnigyk lghrralfek rkrlsdyali fgmfgivvmv
      421 ietelswgay dkaslyslal kclislstii llgliivyha reiqlfmvdn gaddwriamt
      481 yerifficle ilvcaihpip gnytftwtar lafsyapstt tadvdiilsi pmflrlylia
      541 rvmllhsklf tdassrsiga lnkinfntrf vmktlmticp gtvllvfsis lwiiaawtvr
      601 aceryhdqqd vtsnflgamw lisitflsig ygdmvpntyc gkgvclltgi mgagctalvv
      661 avvarklelt kaekhvhnfm mdtqltkrvk naaanvlret wliykntklv kkidhakvrk
      721 hqrkflqaih qlrsvkmeqr klndqantlv dlaktqnimy dmisdlners edfekrivtl
      781 etkletligs ihalpglisq tirqqqrdfi etqmenydkh vsynaersrs ssrrrrssst
      841 apptssess
//
LOCUS       NP_083042                400 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 43 [Mus musculus].
ACCESSION   NP_083042
VERSION     NP_083042.1
DBSOURCE    REFSEQ: accession NM_028766.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Gu,Y., Yao,Y.R., Ding,Y. and Zhang,X.W.
  TITLE     Reduced expression of transmembrane protein 43 during cardiac
            hypertrophy leads to worsening heart failure in mice
  JOURNAL   Exp Biol Med (Maywood) 248 (17), 1437-1445 (2023)
   PUBMED   37697676
  REMARK    GeneRIF: Reduced expression of transmembrane protein 43 during
            cardiac hypertrophy leads to worsening heart failure in mice.
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Orgil,B.O., Munkhsaikhan,U., Pierre,J.F., Li,N., Xu,F.,
            Alberson,N.R., Johnson,J.N., Wetzel,G.T., Boukens,B.J.D., Lu,L.,
            Towbin,J.A. and Purevjav,E.
  TITLE     The TMEM43 S358L mutation affects cardiac, small intestine, and
            metabolic homeostasis in a knock-in mouse model
  JOURNAL   Am J Physiol Heart Circ Physiol 324 (6), H866-H880 (2023)
   PUBMED   37083466
  REMARK    GeneRIF: The TMEM43 S358L mutation affects cardiac, small
            intestine, and metabolic homeostasis in a knock-in mouse model.
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Chen,Z., Cao,Z., Gui,F., Zhang,M., Wu,X., Peng,H., Yu,B., Li,W.,
            Ai,F. and Zhang,J.
  TITLE     TMEM43 Protects against Sepsis-Induced Cardiac Injury via
            Inhibiting Ferroptosis in Mice
  JOURNAL   Cells 11 (19), 2992 (2022)
   PUBMED   36230956
  REMARK    GeneRIF: TMEM43 Protects against Sepsis-Induced Cardiac Injury via
            Inhibiting Ferroptosis in Mice.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Rouhi,L., Cheedipudi,S.M., Chen,S.N., Fan,S., Lombardi,R., Chen,X.,
            Coarfa,C., Robertson,M.J., Gurha,P. and Marian,A.J.
  TITLE     Haploinsufficiency of Tmem43 in cardiac myocytes activates the DNA
            damage response pathway leading to a late-onset
            senescence-associated pro-fibrotic cardiomyopathy
  JOURNAL   Cardiovasc Res 117 (11), 2377-2394 (2021)
   PUBMED   33070193
  REMARK    GeneRIF: Haploinsufficiency of Tmem43 in cardiac myocytes activates
            the DNA damage response pathway leading to a late-onset
            senescence-associated pro-fibrotic cardiomyopathy.
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Jang,M.W., Oh,D.Y., Yi,E., Liu,X., Ling,J., Kim,N., Sharma,K.,
            Kim,T.Y., Lee,S., Kim,A.R., Kim,M.Y., Kim,M.A., Lee,M., Han,J.H.,
            Han,J.J., Park,H.R., Kim,B.J., Lee,S.Y., Woo,D.H., Oh,J., Oh,S.J.,
            Du,T., Koo,J.W., Oh,S.H., Shin,H.W., Seong,M.W., Lee,K.Y.,
            Kim,U.K., Shin,J.B., Sang,S., Cai,X., Mei,L., He,C., Blanton,S.H.,
            Chen,Z.Y., Chen,H., Liu,X., Nourbakhsh,A., Huang,Z., Kang,K.W.,
            Park,W.Y., Feng,Y., Lee,C.J. and Choi,B.Y.
  TITLE     A nonsense TMEM43 variant leads to disruption of connexin-linked
            function and autosomal dominant auditory neuropathy spectrum
            disorder
  JOURNAL   Proc Natl Acad Sci U S A 118 (22) (2021)
   PUBMED   34050020
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Zheng,G., Jiang,C., Li,Y., Yang,D., Ma,Y., Zhang,B., Li,X.,
            Zhang,P., Hu,X., Zhao,X., Du,J. and Lin,X.
  TITLE     TMEM43-S358L mutation enhances NF-kappaB-TGFbeta signal cascade in
            arrhythmogenic right ventricular dysplasia/cardiomyopathy
  JOURNAL   Protein Cell 10 (2), 104-119 (2019)
   PUBMED   29980933
  REMARK    GeneRIF: The authors show that TMEM43-S358L mutation up-regulates
            NF-kappaB (nuclear factor kappaappa B)-TGFbeta (transforming growth
            factor beta 1) signal cascade during arrhythmogenic right
            ventricular dysplasia cardiac fibrosis in mice.
REFERENCE   8  (residues 1 to 400)
  AUTHORS   Stroud,M.J., Fang,X., Zhang,J., Guimaraes-Camboa,N., Veevers,J.,
            Dalton,N.D., Gu,Y., Bradford,W.H., Peterson,K.L., Evans,S.M.,
            Gerace,L. and Chen,J.
  TITLE     Luma is not essential for murine cardiac development and function
  JOURNAL   Cardiovasc Res 114 (3), 378-388 (2018)
   PUBMED   29040414
  REMARK    GeneRIF: Luma is dispensable for murine cardiac development and
            function, and that the Luma S358L mutation alone may not cause
            cardiomyopathy in mice.
REFERENCE   9  (residues 1 to 400)
  AUTHORS   Masuda,T., Kai,N., Sakuma,C., Kobayashi,K., Koga,H. and Yaginuma,H.
  TITLE     Laser capture microdissection and cDNA array analysis for
            identification of mouse KIAA/FLJ genes differentially expressed in
            the embryonic dorsal spinal cord
  JOURNAL   Brain Res 1249, 61-67 (2009)
   PUBMED   19026994
REFERENCE   10 (residues 1 to 400)
  AUTHORS   Bengtsson,L. and Otto,H.
  TITLE     LUMA interacts with emerin and influences its distribution at the
            inner nuclear membrane
  JOURNAL   J Cell Sci 121 (Pt 4), 536-548 (2008)
   PUBMED   18230648
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY152013.1, AK004778.1, AK168559.1 and BB035729.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.132911.1, AK050173.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 40.54 cM"
     Protein         1..400
                     /product="transmembrane protein 43"
                     /EC_number="2.7.1.21"
                     /calculated_mol_wt=44652
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9BTV4; propagated from
                     UniProtKB/Swiss-Prot (Q9DBS1.1)"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBS1.1)"
     Region          121..373
                     /region_name="TMEM43"
                     /note="Transmembrane protein 43; pfam07787"
                     /db_xref="CDD:462267"
     Site            314..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBS1.1)"
     Site            346..366
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBS1.1)"
     Site            369..389
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBS1.1)"
     CDS             1..400
                     /gene="Tmem43"
                     /gene_synonym="1200015A22Rik; LUMA"
                     /coded_by="NM_028766.3:181..1383"
                     /db_xref="CCDS:CCDS20368.1"
                     /db_xref="GeneID:74122"
                     /db_xref="MGI:MGI:1921372"
ORIGIN      
        1 maanysstss rkehvkvtse pqpgflerls etsggmfvgl mtfllsfyli ftnegralkt
       61 atslaeglsl vvspdsihsv apenegrlvh iigalrtskl lsdpnygvhl pavklrrhve
      121 myqwvetees seytedgqvk ketkysynte wrseivnsrn fdreighknp samavesfta
      181 tapfvqigrf flsaglidki dnfkalslak ledphvdiir rgdffyhsen pkypevgdvr
      241 vsfsyaglss ddpdlgpahv vtviarqrgd qlipystksg dtllllhhgd fsaeevfrre
      301 qksnsmktwg lraagwmamf mglnlmtril ytlvdwfpvf rdlvniglka fafcvatslt
      361 lltvaagwlf yrplwaalig clalvpiiia rtrvpakkle
//
LOCUS       NP_067041                104 aa            linear   PRI 27-APR-2025
DEFINITION  SOSS complex subunit C isoform a [Homo sapiens].
ACCESSION   NP_067041
VERSION     NP_067041.1
DBSOURCE    REFSEQ: accession NM_021218.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Vidhyasagar,V., He,Y., Guo,M., Talwar,T., Singh,R.S., Yadav,M.,
            Katselis,G., Vizeacoumar,F.J., Lukong,K.E. and Wu,Y.
  TITLE     Biochemical characterization of INTS3 and C9ORF80, two subunits of
            hNABP1/2 heterotrimeric complex in nucleic acid binding
  JOURNAL   Biochem J 475 (1), 45-60 (2018)
   PUBMED   29150435
  REMARK    GeneRIF: INTS3, but not C9ORF80, affects the nucleic acid-binding
            ability of hNABP1 and hNABP2, indicating that INTS3 might regulate
            hNABP1/hNABP2 biological function, while the role of C9ORF80
            remains unknown.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Ren,W., Chen,H., Sun,Q., Tang,X., Lim,S.C., Huang,J. and Song,H.
  TITLE     Structural basis of SOSS1 complex assembly and recognition of ssDNA
  JOURNAL   Cell Rep 6 (6), 982-991 (2014)
   PUBMED   24630995
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Skaar,J.R., Richard,D.J., Saraf,A., Toschi,A., Bolderson,E.,
            Florens,L., Washburn,M.P., Khanna,K.K. and Pagano,M.
  TITLE     INTS3 controls the hSSB1-mediated DNA damage response
  JOURNAL   J Cell Biol 187 (1), 25-32 (2009)
   PUBMED   19786574
  REMARK    GeneRIF: MISE is part of the INTS3/MISE/hSSB1 (IMS1) complex, which
            controls the DNA damage response
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Li,Y., Bolderson,E., Kumar,R., Muniandy,P.A., Xue,Y., Richard,D.J.,
            Seidman,M., Pandita,T.K., Khanna,K.K. and Wang,W.
  TITLE     HSSB1 and hSSB2 form similar multiprotein complexes that
            participate in DNA damage response
  JOURNAL   J Biol Chem 284 (35), 23525-23531 (2009)
   PUBMED   19605351
  REMARK    GeneRIF: hSSBIP1 forms complexes with INTS3/hSSB1 and INTS3/hSSB2
            and participates in the DNA damage response
REFERENCE   7  (residues 1 to 104)
  AUTHORS   Huang,J., Gong,Z., Ghosal,G. and Chen,J.
  TITLE     SOSS complexes participate in the maintenance of genomic stability
  JOURNAL   Mol Cell 35 (3), 384-393 (2009)
   PUBMED   19683501
  REMARK    GeneRIF: SOSS-C is part of an ssDNA-binding heterotrimeric complex,
            SOSS which is involved in the maintenance of genome stability.
REFERENCE   8  (residues 1 to 104)
  AUTHORS   Richard,D.J., Bolderson,E., Cubeddu,L., Wadsworth,R.I., Savage,K.,
            Sharma,G.G., Nicolette,M.L., Tsvetanov,S., McIlwraith,M.J.,
            Pandita,R.K., Takeda,S., Hay,R.T., Gautier,J., West,S.C.,
            Paull,T.T., Pandita,T.K., White,M.F. and Khanna,K.K.
  TITLE     Single-stranded DNA-binding protein hSSB1 is critical for genomic
            stability
  JOURNAL   Nature 453 (7195), 677-681 (2008)
   PUBMED   18449195
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ219222.1, BC065210.1 and
            AL390067.19.
            
            Summary: The protein encoded by this gene is a subunit of
            single-stranded DNA binding complexes that are important for
            maintaining genome stability. These complexes are involved in G2/M
            checkpoint control and homologous recombination repair. [provided
            by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.75719.1,
                                           SRR1803617.115936.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374242.9/ ENSP00000363360.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..104
                     /product="SOSS complex subunit C isoform a"
                     /note="SOSS complex subunit C; minute
                     INTS3/hSSB-associated element; hSSB-interacting protein 1;
                     SSB-interacting protein 1; sensor of ssDNA subunit C;
                     sensor of single-strand DNA complex subunit C;
                     single-stranded DNA-binding protein-interacting protein 1"
                     /calculated_mol_wt=11294
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9NRY2.1)"
     Region          18..101
                     /region_name="SOSSC"
                     /note="SOSS complex subunit C; pfam15925"
                     /db_xref="CDD:464945"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRY2.1)"
     CDS             1..104
                     /gene="INIP"
                     /gene_synonym="C9orf80; HSPC043; hSSBIP1; MISE; SOSSC;
                     SSBIP1"
                     /coded_by="NM_021218.3:188..502"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6785.1"
                     /db_xref="GeneID:58493"
                     /db_xref="HGNC:HGNC:24994"
                     /db_xref="MIM:613273"
ORIGIN      
        1 maanssgqgf qnknrvaila eldkekrkll mqnqsstnhp gasialsrps lnkdfrdhae
       61 qqhiaaqqka alqhahahss gyfitqdsaf gnlilpvlpr ldpe
//
LOCUS       NP_005042                775 aa            linear   PRI 27-APR-2025
DEFINITION  glutamine--tRNA ligase isoform a [Homo sapiens].
ACCESSION   NP_005042
VERSION     NP_005042.1
DBSOURCE    REFSEQ: accession NM_005051.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 775)
  AUTHORS   Shen,Y.W., Weng,Z.F., He,W., Chen,Y.H., Wang,Q.H., Zou,L.P.,
            Liu,L.Y. and Shang-Guan,H.K.
  TITLE     [QARS1 gene related glutaminyl-tRNA synthetase deficiency syndrome:
            report of three cases and a review of literature]
  JOURNAL   Zhonghua Er Ke Za Zhi 58 (12), 1006-1012 (2020)
   PUBMED   33256324
  REMARK    GeneRIF: [QARS1 gene related glutaminyl-tRNA synthetase deficiency
            syndrome: report of three cases and a review of literature].
            Review article
REFERENCE   2  (residues 1 to 775)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 775)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 775)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 775)
  AUTHORS   Leshinsky-Silver,E., Ling,J., Wu,J., Vinkler,C., Yosovich,K.,
            Bahar,S., Yanoov-Sharav,M., Lerman-Sagie,T. and Lev,D.
  TITLE     Severe growth deficiency, microcephaly, intellectual disability,
            and characteristic facial features are due to a homozygous QARS
            mutation
  JOURNAL   Neurogenetics 18 (3), 141-146 (2017)
   PUBMED   28620870
  REMARK    GeneRIF: patient's fibroblasts demonstrated markedly reduced QARS
            amino acylation activity in vitro
REFERENCE   6  (residues 1 to 775)
  AUTHORS   Bienvenut,W.V., Sumpton,D., Martinez,A., Lilla,S., Espagne,C.,
            Meinnel,T. and Giglione,C.
  TITLE     Comparative large scale characterization of plant versus mammal
            proteins reveals similar and idiosyncratic N-alpha-acetylation
            features
  JOURNAL   Mol Cell Proteomics 11 (6), M111.015131 (2012)
   PUBMED   22223895
REFERENCE   7  (residues 1 to 775)
  AUTHORS   Lamour,V., Quevillon,S., Diriong,S., N'Guyen,V.C., Lipinski,M. and
            Mirande,M.
  TITLE     Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme
            as a case of horizontal gene transfer
  JOURNAL   Proc Natl Acad Sci U S A 91 (18), 8670-8674 (1994)
   PUBMED   8078941
REFERENCE   8  (residues 1 to 775)
  AUTHORS   Shiba,K., Suzuki,N., Shigesada,K., Namba,Y., Schimmel,P. and
            Noda,T.
  TITLE     Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence
            of the anticodon-binding domain and acquisition of a new structural
            unit
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7435-7439 (1994)
   PUBMED   8052601
REFERENCE   9  (residues 1 to 775)
  AUTHORS   Kaiser,E., Hu,B., Becher,S., Eberhard,D., Schray,B., Baack,M.,
            Hameister,H. and Knippers,R.
  TITLE     The human EPRS locus (formerly the QARS locus): a gene encoding a
            class I and a class II aminoacyl-tRNA synthetase
  JOURNAL   Genomics 19 (2), 280-290 (1994)
   PUBMED   8188258
REFERENCE   10 (residues 1 to 775)
  AUTHORS   Norcum,M.T.
  TITLE     Structural analysis of the high molecular mass aminoacyl-tRNA
            synthetase complex. Effects of neutral salts and detergents
  JOURNAL   J Biol Chem 266 (23), 15398-15405 (1991)
   PUBMED   1651330
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM560535.1 and BC000394.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Aminoacyl-tRNA synthetases catalyze the aminoacylation of
            tRNA by their cognate amino acid. Because of their central role in
            linking amino acids with nucleotide triplets contained in tRNAs,
            aminoacyl-tRNA synthetases are thought to be among the first
            proteins that appeared in evolution. In metazoans, 9 aminoacyl-tRNA
            synthetases specific for glutamine (gln), glutamic acid (glu), and
            7 other amino acids are associated within a multienzyme complex.
            Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS)
            is absent from many prokaryotes, mitochondria, and chloroplasts, in
            which Gln-tRNA(Gln) is formed by transamidation of the misacylated
            Glu-tRNA(Gln). Glutaminyl-tRNA synthetase belongs to the class-I
            aminoacyl-tRNA synthetase family. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290523.1, SRR3476690.769775.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:22223895)
            MANE Ensembl match               :: ENST00000306125.12/
                                                ENSP00000307567.6
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..775
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..775
                     /product="glutamine--tRNA ligase isoform a"
                     /EC_number="6.1.1.18"
                     /note="glutamine-tRNA synthetase; glutamine--tRNA ligase"
                     /calculated_mol_wt=87668
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P47897.1)"
     Region          6..774
                     /region_name="PLN02859"
                     /note="glutamine-tRNA ligase"
                     /db_xref="CDD:178450"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P47897.1)"
     Region          270..280
                     /region_name="'HIGH' region.
                     /evidence=ECO:0000305|PubMed:26869582"
                     /note="propagated from UniProtKB/Swiss-Prot (P47897.1)"
     Site            309
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P47897.1)"
     Region          493..497
                     /region_name="'KMSKS' region.
                     /evidence=ECO:0000305|PubMed:26869582"
                     /note="propagated from UniProtKB/Swiss-Prot (P47897.1)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P47897.1)"
     CDS             1..775
                     /gene="QARS1"
                     /gene_synonym="GLNRS; MSCCA; PRO2195; QARS"
                     /coded_by="NM_005051.3:25..2352"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2788.1"
                     /db_xref="GeneID:5859"
                     /db_xref="HGNC:HGNC:9751"
                     /db_xref="MIM:603727"
ORIGIN      
        1 maaldslslf tslglseqka retlknsals aqlreaatqa qqtlgstidk atgillygla
       61 srlrdtrrls flvsyiaskk ihtepqlsaa leyvrshpld pidtvdfere cgvgvivtpe
      121 qieeaveaai nrhrpqllve ryhfnmgllm gearavlkwa dgkmiknevd mqvlhllgpk
      181 leadlekkfk vakarleetd rrtakdvven getadqtlsl meqlrgealk fhkpgenykt
      241 pgyvvtphtm nllkqhleit ggqvrtrfpp epngilhigh akainfnfgy akanngicfl
      301 rfddtnpeke eakfftaicd mvawlgytpy kvtyasdyfd qlyawaveli rrglayvchq
      361 rgeelkghnt lpspwrdrpm eeslllfeam rkgkfsegea tlrmklvmed gkmdpvayrv
      421 kytphhrtgd kwciyptydy thclcdsieh ithslctkef qarrssyfwl cnaldvycpv
      481 qweygrlnlh yavvskrkil qlvatgavrd wddprlftlt alrrrgfppe ainnfcarvg
      541 vtvaqttmep hlleacvrdv lndtaprama vleslrviit nfpaaksldi qvpnfpadet
      601 kgfhqvpfap ivfiertdfk eepepgfkrl awgqpvglrh tgyvielqhv vkgpsgcves
      661 levtcrrada gekpkafihw vsqplmcevr lyerlfqhkn pedptevpgg flsdlnlasl
      721 hvvdaalvdc svalakpfdk fqferlgyfs vdpdshqgkl vfnrtvtlke dpgkv
//
LOCUS       NP_001092315             327 aa            linear   PRI 27-APR-2025
DEFINITION  annexin A8-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001092315 XP_001127358
VERSION     NP_001092315.2
DBSOURCE    REFSEQ: accession NM_001098845.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Karanjawala,Z.E., Illei,P.B., Ashfaq,R., Infante,J.R., Murphy,K.,
            Pandey,A., Schulick,R., Winter,J., Sharma,R., Maitra,A., Goggins,M.
            and Hruban,R.H.
  TITLE     New markers of pancreatic cancer identified through differential
            gene expression analyses: claudin 18 and annexin A8
  JOURNAL   Am J Surg Pathol 32 (2), 188-196 (2008)
   PUBMED   18223320
  REMARK    GeneRIF: Claudin 18 and annexin A8 are frequently highly
            overexpressed in infiltrating ductal adenocarcinomas.
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Gerke,V., Creutz,C.E. and Moss,S.E.
  TITLE     Annexins: linking Ca2+ signalling to membrane dynamics
  JOURNAL   Nat Rev Mol Cell Biol 6 (6), 449-461 (2005)
   PUBMED   15928709
  REMARK    Review article
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Gerke,V. and Moss,S.E.
  TITLE     Annexins: from structure to function
  JOURNAL   Physiol Rev 82 (2), 331-371 (2002)
   PUBMED   11917092
  REMARK    Review article
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Reutelingsperger,C.P., van Heerde,W., Hauptmann,R., Maassen,C., van
            Gool,R.G., de Leeuw,P. and Tiebosch,A.
  TITLE     Differential tissue expression of Annexin VIII in human
  JOURNAL   FEBS Lett 349 (1), 120-124 (1994)
   PUBMED   8045287
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Sarkar,A., Yang,P., Fan,Y.H., Mu,Z.M., Hauptmann,R., Adolf,G.R.,
            Stass,S.A. and Chang,K.S.
  TITLE     Regulation of the expression of annexin VIII in acute promyelocytic
            leukemia
  JOURNAL   Blood 84 (1), 279-286 (1994)
   PUBMED   8018923
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Chambers,J.A., Gardner,E., Hauptmann,R., Ponder,B.A. and
            Mulligan,L.M.
  TITLE     TaqI polymorphisms at the annexin VIII locus (ANX8)
  JOURNAL   Hum Mol Genet 1 (7), 550 (1992)
   PUBMED   1364010
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Hauptmann,R., Maurer-Fogy,I., Krystek,E., Bodo,G., Andree,H. and
            Reutelingsperger,C.P.
  TITLE     Vascular anticoagulant beta: a novel human Ca2+/phospholipid
            binding protein that inhibits coagulation and phospholipase A2
            activity. Its molecular cloning, expression and comparison with
            VAC-alpha
  JOURNAL   Eur J Biochem 185 (1), 63-71 (1989)
   PUBMED   2530088
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK313626.1 and AC244230.3.
            
            On Jul 17, 2013 this sequence version replaced NP_001092315.1.
            
            Summary: This gene encodes a member of the annexin family of
            evolutionarily conserved Ca2+ and phospholipid binding proteins.
            The encoded protein may function as an an anticoagulant that
            indirectly inhibits the thromboplastin-specific complex.
            Overexpression of this gene has been associated with acute
            myelocytic leukemia. A highly similar duplicated copy of this gene
            is found in close proximity on the long arm of chromosome 10.
            [provided by RefSeq, Apr 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.179629.1, X16662.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000619162.5/ ENSP00000480221.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.22"
     Protein         1..327
                     /product="annexin A8-like protein 1 isoform 1"
                     /note="annexin A8-like protein 1; annexin-8; annexin VIII;
                     vascular anticoagulant-beta; annexin A8L2; annexin A8-like
                     protein 2"
                     /calculated_mol_wt=36748
     Region          21..92
                     /region_name="Annexin 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VT79.2)"
     Region          26..90
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          93..164
                     /region_name="Annexin 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VT79.2)"
     Region          97..162
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          177..249
                     /region_name="Annexin 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VT79.2)"
     Region          181..247
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          253..324
                     /region_name="Annexin 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VT79.2)"
     Region          257..322
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     CDS             1..327
                     /gene="ANXA8L1"
                     /gene_synonym="ANXA8; ANXA8L2; bA145E20.2; VAC-beta"
                     /coded_by="NM_001098845.3:77..1060"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS73098.1"
                     /db_xref="GeneID:728113"
                     /db_xref="HGNC:HGNC:23334"
ORIGIN      
        1 mawwkawieq egvtvksssh fnpdpdaetl ykamkgigtn eqaiidvltk rsntqrqqia
       61 ksfkaqfgkd ltetlksels gkferlival myppyryeak elhdamkglg tkegviieil
      121 asrtknqlre imkayeedyg ssleediqad tsgylerilv cllqgsrddv ssfvdpalal
      181 qdaqdlyaag ekirgtdemk fitilctrsa thllrvfeey ekianksied siksethgsl
      241 eeamltvvkc tqnlhsyfae rlyyamkgag trdgtlirni vsrseidlnl ikchfkkmyg
      301 ktlssmimed tsgdyknall slvgsdp
//
LOCUS       NP_982258                404 aa            linear   PRI 27-APR-2025
DEFINITION  immediate early response gene 5-like protein [Homo sapiens].
ACCESSION   NP_982258 XP_372145
VERSION     NP_982258.2
DBSOURCE    REFSEQ: accession NM_203434.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Wang,N., Tan,X., Cao,S. and Liu,M.
  TITLE     Predictive value of immediate early response 5 like (IER5L) in the
            prognosis and immune checkpoint blockade therapy of non-small cell
            lung cancer patients
  JOURNAL   Pathol Res Pract 256, 155270 (2024)
   PUBMED   38552564
  REMARK    GeneRIF: Predictive value of immediate early response 5 like
            (IER5L) in the prognosis and immune checkpoint blockade therapy of
            non-small cell lung cancer patients.
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Doi,K., Takeuchi,H. and Sakurai,H.
  TITLE     PP2A-B55 and its adapter proteins IER2 and IER5 regulate the
            activity of RB family proteins and the expression of cell
            cycle-related genes
  JOURNAL   FEBS J 290 (3), 745-762 (2023)
   PUBMED   36047562
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Ueda,T., Kohama,Y. and Sakurai,H.
  TITLE     IER family proteins are regulators of protein phosphatase PP2A and
            modulate the phosphorylation status of CDC25A
  JOURNAL   Cell Signal 55, 81-89 (2019)
   PUBMED   30599213
  REMARK    GeneRIF: The results suggest that IER2, IER5, and IER5L proteins
            are target protein-specific regulators of PP2A (protein phosphatase
            2A) activity and modulate cell proliferation through CDC25A (cell
            division cycle 25A protein) activity.
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM763373.1, BX458317.2, AL158151.16, BQ574938.1, CN293040.1 and
            BU676697.1.
            
            On Jun 8, 2007 this sequence version replaced NP_982258.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: DRR138511.42761.1, ERR279842.132.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372491.4/ ENSP00000361569.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..404
                     /product="immediate early response gene 5-like protein"
                     /calculated_mol_wt=41978
     Region          1..404
                     /region_name="IER"
                     /note="Immediate early response protein (IER); pfam05760"
                     /db_xref="CDD:461732"
     Region          86..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T953.1)"
     Region          160..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T953.1)"
     Region          308..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T953.1)"
     CDS             1..404
                     /gene="IER5L"
                     /gene_synonym="bA247A12.2"
                     /coded_by="NM_203434.3:210..1424"
                     /db_xref="CCDS:CCDS43888.1"
                     /db_xref="GeneID:389792"
                     /db_xref="HGNC:HGNC:23679"
ORIGIN      
        1 mecaldaqsl isislrkihs srtqrggikl hknllvsyvl rnarqlylse ryaelyrrqq
       61 qqqqqqpphh qhqhlayaap gmpasaadfg plqlggggda earepaarhq lhqlhqlhql
      121 hlqqqlhqhq hpaprgcaaa aaagapagga galselpgca alqpphgaph rgqpleplqp
      181 gpaplplplp ppapaalcpr dprapaacsa ppgaappaaa asppaspapa sspgfyrgay
      241 ptpsdfglhc ssqttvldld thvvttveng ylhqdccasa hcpccgqgap gpglasaagc
      301 krkyypgqee eeddeedagg lgaeppggap fapckrarfe dfcpdsspda snisnlisif
      361 gsgfsglvsr qpdsseqppp lngqlcakqa laslgawtra ivaf
//
LOCUS       NP_006421                539 aa            linear   PRI 27-APR-2025
DEFINITION  T-complex protein 1 subunit delta isoform a [Homo sapiens].
ACCESSION   NP_006421
VERSION     NP_006421.2
DBSOURCE    REFSEQ: accession NM_006430.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Tang,C., Li,C., Chen,C., Chen,T., Zhu,J., Sun,M., Wang,P. and
            Han,C.
  TITLE     LINC01234 promoted malignant behaviors of breast cancer cells via
            hsa-miR-30c-2-3p/CCT4/mTOR signaling pathway
  JOURNAL   Taiwan J Obstet Gynecol 63 (1), 46-56 (2024)
   PUBMED   38216268
  REMARK    GeneRIF: LINC01234 promoted malignant behaviors of breast cancer
            cells via hsa-miR-30c-2-3p/CCT4/mTOR signaling pathway.
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Fang,J., Ma,Y., Li,Y., Li,J., Zhang,X., Han,X., Ma,S. and Guan,F.
  TITLE     CCT4 knockdown enhances the sensitivity of cisplatin by inhibiting
            glycolysis in human esophageal squamous cell carcinomas
  JOURNAL   Mol Carcinog 61 (11), 1043-1055 (2022)
   PUBMED   36102200
  REMARK    GeneRIF: CCT4 knockdown enhances the sensitivity of cisplatin by
            inhibiting glycolysis in human esophageal squamous cell carcinomas.
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Li,F., Liu,C.S., Wu,P., Ling,A.S., Pan,Q. and Li,X.N.
  TITLE     CCT4 suppression inhibits tumor growth in hepatocellular carcinoma
            by interacting with Cdc20
  JOURNAL   Chin Med J (Engl) 134 (22), 2721-2729 (2021)
   PUBMED   34732665
  REMARK    GeneRIF: CCT4 suppression inhibits tumor growth in hepatocellular
            carcinoma by interacting with Cdc20.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Won,K.A., Schumacher,R.J., Farr,G.W., Horwich,A.L. and Reed,S.I.
  TITLE     Maturation of human cyclin E requires the function of eukaryotic
            chaperonin CCT
  JOURNAL   Mol Cell Biol 18 (12), 7584-7589 (1998)
   PUBMED   9819444
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Melki,R., Batelier,G., Soulie,S. and Williams,R.C. Jr.
  TITLE     Cytoplasmic chaperonin containing TCP-1: structural and functional
            characterization
  JOURNAL   Biochemistry 36 (19), 5817-5826 (1997)
   PUBMED   9153422
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Nabetani,A., Hatada,I., Morisaki,H. and Mukai,T.
  TITLE     Chromosomal assignment and imprinting tests for the mouse delta
            subunit of the cytosolic chaperonin containing TCP-1 (Cct4) gene to
            proximal chromosome 11
  JOURNAL   Genomics 34 (2), 246-249 (1996)
   PUBMED   8661059
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Wu-Baer,F., Lane,W.S. and Gaynor,R.B.
  TITLE     Identification of a group of cellular cofactors that stimulate the
            binding of RNA polymerase II and TRP-185 to human immunodeficiency
            virus 1 TAR RNA
  JOURNAL   J Biol Chem 271 (8), 4201-4208 (1996)
   PUBMED   8626763
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Kubota,H., Hynes,G., Carne,A., Ashworth,A. and Willison,K.
  TITLE     Identification of six Tcp-1-related genes encoding divergent
            subunits of the TCP-1-containing chaperonin
  JOURNAL   Curr Biol 4 (2), 89-99 (1994)
   PUBMED   7953530
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB461009.1, BC106934.1, AI439570.1 and AC107081.5.
            
            On Nov 20, 2003 this sequence version replaced NP_006421.1.
            
            Summary: The chaperonin containing TCP1 (MIM 186980) complex (CCT),
            also called the TCP1 ring complex, consists of 2 back-to-back
            rings, each containing 8 unique but homologous subunits, such as
            CCT4. CCT assists the folding of newly translated polypeptide
            substrates through multiple rounds of ATP-driven release and
            rebinding of partially folded intermediate forms. Substrates of CCT
            include the cytoskeletal proteins actin (see MIM 102560) and
            tubulin (see MIM 191130), as well as alpha-transducin (MIM 139330)
            (Won et al., 1998 [PubMed 9819444]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.125403.1,
                                           SRR1803617.1740.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394440.8/ ENSP00000377958.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p15"
     Protein         1..539
                     /product="T-complex protein 1 subunit delta isoform a"
                     /note="chaperonin containing t-complex polypeptide 1,
                     delta subunit; T-complex protein 1 subunit delta;
                     TCP-1-delta; stimulator of TAR RNA-binding; chaperonin
                     containing TCP1, subunit 4 (delta); chaperonin containing
                     T-complex polypeptide 1 subunit 4"
                     /calculated_mol_wt=57793
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50991.4)"
     Site            19
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P50991.4)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P80315; propagated from
                     UniProtKB/Swiss-Prot (P50991.4)"
     Region          25..538
                     /region_name="TCP1_delta"
                     /note="TCP-1 (CTT or eukaryotic type II) chaperonin
                     family, delta subunit. Chaperonins are involved in
                     productive folding of proteins. They share a common
                     general morphology, a double toroid of 2 stacked rings. In
                     contrast to bacterial group I chaperonins...; cd03338"
                     /db_xref="CDD:239454"
     Site            order(25,29,57..60,62,80,82,86,90,93,395,531..537)
                     /site_type="other"
                     /note="ring oligomerisation interface [polypeptide
                     binding]"
                     /db_xref="CDD:239454"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50991.4)"
     Site            order(52..54,104,108,169,407,425,465,508,510)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239454"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50991.4)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50991.4)"
     Site            288
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50991.4)"
     Site            302
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50991.4)"
     Site            319
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50991.4)"
     Site            326
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50991.4)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50991.4)"
     Site            order(445,463,472,474..475,478)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239454"
     CDS             1..539
                     /gene="CCT4"
                     /gene_synonym="CCT-DELTA; Cctd; SRB"
                     /coded_by="NM_006430.4:150..1769"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33206.1"
                     /db_xref="GeneID:10575"
                     /db_xref="HGNC:HGNC:1617"
                     /db_xref="MIM:605142"
ORIGIN      
        1 mpenvaprsg atagaaggrg kgayqdrdkp aqirfsnisa akavadairt slgpkgmdkm
       61 iqdgkgdvti tndgatilkq mqvlhpaarm lvelskaqdi eagdgttsvv iiagslldsc
      121 tkllqkgihp tiisesfqka lekgieiltd msrpvelsdr etllnsatts lnskvvsqys
      181 sllspmsvna vmkvidpata tsvdlrdiki vkklggtidd celveglvlt qkvsnsgitr
      241 vekakigliq fclsapktdm dnqivvsdya qmdrvlreer ayilnlvkqi kktgcnvlli
      301 qksilrdals dlalhflnkm kimvikdier ediefickti gtkpvahidq ftadmlgsae
      361 laeevnlngs gkllkitgca spgktvtivv rgsnklviee aersihdalc virclvkkra
      421 liagggapei elalrlteys rtlsgmesyc vrafadamev ipstlaenag lnpistvtel
      481 rnrhaqgekt aginvrkggi snileelvvq pllvsvsalt latetvrsil kiddvvntr
//
LOCUS       NP_000684                512 aa            linear   PRI 27-APR-2025
DEFINITION  retinaldehyde dehydrogenase 3 isoform 1 [Homo sapiens].
ACCESSION   NP_000684
VERSION     NP_000684.2
DBSOURCE    REFSEQ: accession NM_000693.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Fernando,W., Cruickshank,B.M., Arun,R.P., MacLean,M.R.,
            Cahill,H.F., Morales-Quintanilla,F., Dean,C.A., Wasson,M.D.,
            Dahn,M.L., Coyle,K.M., Walker,O.L., Power Coombs,M.R. and
            Marcato,P.
  TITLE     ALDH1A3 is the switch that determines the balance of ALDH+ and
            CD24-CD44+ cancer stem cells, EMT-MET, and glucose metabolism in
            breast cancer
  JOURNAL   Oncogene 43 (43), 3151-3169 (2024)
   PUBMED   39251846
  REMARK    GeneRIF: ALDH1A3 is the switch that determines the balance of
            ALDH[+] and CD24[-]CD44[+] cancer stem cells, EMT-MET, and glucose
            metabolism in breast cancer.
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Chen,Z., Chen,J., Xu,X., Li,Q., Zhang,C., Li,S., Liu,L., Cao,C.,
            Chen,D. and He,Q.
  TITLE     METTL3-mediated ALDH m6A methylation regulates the malignant
            behavior of BMI1+ HNSCC stem cells
  JOURNAL   Oral Dis 30 (3), 1061-1071 (2024)
   PUBMED   37249063
  REMARK    GeneRIF: METTL3-mediated ALDH m[6]A methylation regulates the
            malignant behavior of BMI1[+] HNSCC stem cells.
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Bharadwaj,A.G., McLean,M.E., Dahn,M.L., Cahill,H.F., Wasson,M.D.,
            Arun,R.P., Walker,O.L., Cruickshank,B.M., Fernando,W.,
            Venkatesh,J., Barnes,P.J., Bethune,G., Knapp,G., Helyer,L.K.,
            Giacomantonio,C.A., Waisman,D.M. and Marcato,P.
  TITLE     ALDH1A3 promotes invasion and metastasis in triple-negative breast
            cancer by regulating the plasminogen activation pathway
  JOURNAL   Mol Oncol 18 (1), 91-112 (2024)
   PUBMED   37753740
  REMARK    GeneRIF: ALDH1A3 promotes invasion and metastasis in
            triple-negative breast cancer by regulating the plasminogen
            activation pathway.
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Wu,Y., Franzmeier,S., Liesche-Starnecker,F. and Schlegel,J.
  TITLE     Enhanced Sensitivity to ALDH1A3-Dependent Ferroptosis in
            TMZ-Resistant Glioblastoma Cells
  JOURNAL   Cells 12 (21), 2522 (2023)
   PUBMED   37947601
  REMARK    GeneRIF: Enhanced Sensitivity to ALDH1A3-Dependent Ferroptosis in
            TMZ-Resistant Glioblastoma Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Kesim,Y., Ceroni,F., Damian,A., Blanco-Kelly,F., Ayuso,C.,
            Williamson,K., Paquis-Flucklinger,V., Bax,D.A., Plaisancie,J.,
            Rieubland,C., Chamlal,M., Corton,M., Chassaing,N., Calvas,P. and
            Ragge,N.K.
  TITLE     Clinical and genetic analysis further delineates the phenotypic
            spectrum of ALDH1A3-related anophthalmia and microphthalmia
  JOURNAL   Eur J Hum Genet 31 (10), 1175-1180 (2023)
   PUBMED   36997679
  REMARK    GeneRIF: Clinical and genetic analysis further delineates the
            phenotypic spectrum of ALDH1A3-related anophthalmia and
            microphthalmia.
            Erratum:[Eur J Hum Genet. 2023 Oct;31(10):1196-1198. doi:
            10.1038/s41431-023-01363-3. PMID: 37106145]
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Everts,H.B., King,L.E. Jr., Sundberg,J.P. and Ong,D.E.
  TITLE     Hair cycle-specific immunolocalization of retinoic acid
            synthesizing enzymes Aldh1a2 and Aldh1a3 indicate complex
            regulation
  JOURNAL   J Invest Dermatol 123 (2), 258-263 (2004)
   PUBMED   15245423
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Nishimura,M., Yoshitsugu,H., Naito,S. and Hiraoka,I.
  TITLE     Evaluation of gene induction of drug-metabolizing enzymes and
            transporters in primary culture of human hepatocytes using
            high-sensitivity real-time reverse transcription PCR
  JOURNAL   Yakugaku Zasshi 122 (5), 339-361 (2002)
   PUBMED   12040753
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Rexer,B.N., Zheng,W.L. and Ong,D.E.
  TITLE     Retinoic acid biosynthesis by normal human breast epithelium is via
            aldehyde dehydrogenase 6, absent in MCF-7 cells
  JOURNAL   Cancer Res 61 (19), 7065-7070 (2001)
   PUBMED   11585737
REFERENCE   9  (residues 1 to 512)
  AUTHORS   Yoshida,A., Rzhetsky,A., Hsu,L.C. and Chang,C.
  TITLE     Human aldehyde dehydrogenase gene family
  JOURNAL   Eur J Biochem 251 (3), 549-557 (1998)
   PUBMED   9490025
  REMARK    Review article
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Hsu,L.C., Chang,W.C., Hiraoka,L. and Hsieh,C.L.
  TITLE     Molecular cloning, genomic organization, and chromosomal
            localization of an additional human aldehyde dehydrogenase gene,
            ALDH6
  JOURNAL   Genomics 24 (2), 333-341 (1994)
   PUBMED   7698756
  REMARK    GeneRIF: play a major role in the detoxification of aldehydes
            generated by alcohol metabolism and lipid peroxidation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB480234.1 and BC069274.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 24, 2007 this sequence version replaced NP_000684.1.
            
            Summary: This gene encodes an aldehyde dehydrogenase enzyme that
            uses retinal as a substrate. Mutations in this gene have been
            associated with microphthalmia, isolated 8, and expression changes
            have also been detected in tumor cells. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jun
            2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC069274.1, SRR1803615.15581.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329841.10/ ENSP00000332256.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.3"
     Protein         1..512
                     /product="retinaldehyde dehydrogenase 3 isoform 1"
                     /EC_number="1.2.1.36"
                     /note="aldehyde dehydrogenase 6; retinaldehyde
                     dehydrogenase 3; acetaldehyde dehydrogenase 6"
                     /calculated_mol_wt=55978
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47895.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.3,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P47895.2)"
     Region          26..506
                     /region_name="ALDH_F1AB_F2_RALDH1"
                     /note="NAD+-dependent retinal dehydrogenase 1, ALDH
                     families 1A, 1B, and 2-like; cd07141"
                     /db_xref="CDD:143459"
     Site            order(84..85,89,92,94,98,139,142..143,147,149..150,
                     153..157,159..160,163..170,263,266,269..270,273..274,276,
                     281,446,448,455,458,460..467,474..476,479..482,484,487,
                     492,499..504,506)
                     /site_type="other"
                     /note="homotetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143459"
     Site            order(177..180,204,207,237,241..242,255,258,261,281..282,
                     314,361,364,411)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143459"
     Site            order(181,280,311,314)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143459"
     Site            181
                     /site_type="other"
                     /note="Transition state stabilizer. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P47895.2)"
     CDS             1..512
                     /gene="ALDH1A3"
                     /gene_synonym="ALDH1A6; ALDH6; MCOP8; RALDH3"
                     /coded_by="NM_000693.4:78..1616"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10389.1"
                     /db_xref="GeneID:220"
                     /db_xref="HGNC:HGNC:409"
                     /db_xref="MIM:600463"
ORIGIN      
        1 matangaven gqpdrkppal prpirnlevk ftkifinnew hesksgkkfa tcnpstreqi
       61 ceveegdkpd vdkaveaaqv afqrgspwrr ldalsrgrll hqladlverd ratlaaletm
      121 dtgkpflhaf fidlegcirt lryfagwadk iqgktiptdd nvvcftrhep igvcgaitpw
      181 nfpllmlvwk lapalccgnt mvlkpaeqtp ltalylgsli keagfppgvv nivpgfgptv
      241 gaaisshpqi nkiaftgste vgklvkeaas rsnlkrvtle lggknpcivc adadldlave
      301 cahqgvffnq gqcctaasrv fveeqvysef vrrsveyakk rpvgdpfdvk teqgpqidqk
      361 qfdkilelie sgkkegakle cggsamedkg lfikptvfse vtdnmriake eifgpvqpil
      421 kfksieevik ranstdyglt aavftknldk alklasales gtvwincyna lyaqapfggf
      481 kmsgngrelg eyalaeytev ktvtiklgdk np
//
LOCUS       NP_001353710             644 aa            linear   PRI 27-APR-2025
DEFINITION  protein BCAP isoform f [Homo sapiens].
ACCESSION   NP_001353710 XP_005271111
VERSION     NP_001353710.1
DBSOURCE    REFSEQ: accession NM_001366781.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Li,J., Lu,J., Xu,M., Yang,S., Yu,T., Zheng,C., Huang,X., Pan,Y.,
            Chen,Y., Long,J., Zhang,C., Huang,H., Dai,Q., Li,B., Wang,W.,
            Yao,S. and Pan,C.
  TITLE     ODF2L acts as a synthetic lethal partner with WEE1 inhibition in
            epithelial ovarian cancer models
  JOURNAL   J Clin Invest 133 (2), e161544 (2023)
   PUBMED   36378528
  REMARK    GeneRIF: ODF2L acts as a synthetic lethal partner with WEE1
            inhibition in epithelial ovarian cancer models.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 644)
  AUTHORS   de Saram,P., Iqbal,A., Murdoch,J.N. and Wilkinson,C.J.
  TITLE     BCAP is a centriolar satellite protein and inhibitor of
            ciliogenesis
  JOURNAL   J Cell Sci 130 (19), 3360-3373 (2017)
   PUBMED   28775150
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Ponsard,C., Seltzer,V., Perret,E., Tournier,F. and Middendorp,S.
  TITLE     Identification of BCAP, a new protein associated with basal bodies
            and centrioles
  JOURNAL   Front Biosci 12, 3683-3693 (2007)
   PUBMED   17485331
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC119749.2 and AL136382.6.
            
            On Oct 19, 2018 this sequence version replaced XP_005271111.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.68507.1,
                                           SRR1660805.149150.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000460698.7/ ENSP00000433092.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.3"
     Protein         1..644
                     /product="protein BCAP isoform f"
                     /note="basal body centriole-associated protein; protein
                     BCAP; ODF2-like protein"
                     /calculated_mol_wt=74635
     Region          <135..443
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          <340..>596
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     CDS             1..644
                     /gene="ODF2L"
                     /coded_by="NM_001366781.1:351..2285"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS90997.1"
                     /db_xref="GeneID:57489"
                     /db_xref="HGNC:HGNC:29225"
                     /db_xref="MIM:620130"
ORIGIN      
        1 mekavndgsh seelfchlkt isekedlprc tseshlsclk qdilnektel eatlkeaelv
       61 thsvelllpl fkdtiekinf enanlsalnl kiseqkeili keldtfksvk lalehllrkr
      121 dykqtgdnls smllenltdn esentnlkkk vfekeahiqe lsclfqseka ntlkanrfsq
      181 svkvvherlq iqihkreaen dklkeyvksl etkiakwnlq srmnkneaiv mkeasrqktv
      241 alkkaskvyk qrldhftgai ekltsqirdq eaklsetisa snawkshyek iviektelev
      301 qietmkkqii nlledlkkme dhgknsceei lrkvhsieye netlnlentk lkttlaalkd
      361 evvsvenels elqevekkqk tliemyktqv qklqeaaeiv ksrcenllhk nnqitktknk
      421 nvekmrgqme shlkelervc dsltaaerrl hecqeslqcc kgkcadqeht irelqgqvdg
      481 nhnlltklsl eeencliqlk cenlqqkleq mdaenkelek klanqeeclk hsnlkfkeks
      541 aeytalarql eaaleegrqk vaeeiekmss resalqikil dletelrkkn eeqnqlvckm
      601 nskaqhqevc lkevqnslek senqnesikn ylqflktsyv tmfe
//
LOCUS       NP_000414                639 aa            linear   PRI 27-APR-2025
DEFINITION  keratin, type II cytoskeletal 2 epidermal [Homo sapiens].
ACCESSION   NP_000414
VERSION     NP_000414.2
DBSOURCE    REFSEQ: accession NM_000423.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Frommherz,L., Komlosi,K., Hewel,C., Kopp,J., Dewenter,M.,
            Zimmer,A., Bartsch,O., Linke,M., Technau-Hafsi,K., Gerber,S.,
            Fischer,J. and Has,C.
  TITLE     Acral lamellar ichthyosis with amino acid substitution in the
            C-terminus of keratin 2
  JOURNAL   J Eur Acad Dermatol Venereol 37 (4), 817-822 (2023)
   PUBMED   36331357
  REMARK    GeneRIF: Acral lamellar ichthyosis with amino acid substitution in
            the C-terminus of keratin 2.
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Diociaiuti,A., Castiglia,D., Corbeddu,M., Rotunno,R., Rossi,S.,
            Pisaneschi,E., Cesario,C., Condorelli,A.G., Zambruno,G. and El
            Hachem,M.
  TITLE     First Case of KRT2 Epidermolytic Nevus and Novel Clinical and
            Genetic Findings in 26 Italian Patients with Keratinopathic
            Ichthyoses
  JOURNAL   Int J Mol Sci 21 (20), 7707 (2020)
   PUBMED   33081034
  REMARK    GeneRIF: First Case of KRT2 Epidermolytic Nevus and Novel Clinical
            and Genetic Findings in 26 Italian Patients with Keratinopathic
            Ichthyoses.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 639)
  AUTHORS   Aldehlawi,H., Usman,S., Lalli,A., Ahmad,F., Williams,G., Teh,M.T.
            and Waseem,A.
  TITLE     Serum lipids, retinoic acid and phenol red differentially regulate
            expression of keratins K1, K10 and K2 in cultured keratinocytes
  JOURNAL   Sci Rep 10 (1), 4829 (2020)
   PUBMED   32179842
  REMARK    GeneRIF: Serum lipids, retinoic acid and phenol red differentially
            regulate expression of keratins K1, K10 and K2 in cultured
            keratinocytes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 639)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 639)
  AUTHORS   Steinert,P.M. and Marekov,L.N.
  TITLE     The proteins elafin, filaggrin, keratin intermediate filaments,
            loricrin, and small proline-rich proteins 1 and 2 are isodipeptide
            cross-linked components of the human epidermal cornified cell
            envelope
  JOURNAL   J Biol Chem 270 (30), 17702-17711 (1995)
   PUBMED   7543090
REFERENCE   7  (residues 1 to 639)
  AUTHORS   Kremer,H., Zeeuwen,P., McLean,W.H., Mariman,E.C., Lane,E.B., van de
            Kerkhof,C.M., Ropers,H.H. and Steijlen,P.M.
  TITLE     Ichthyosis bullosa of Siemens is caused by mutations in the keratin
            2e gene
  JOURNAL   J Invest Dermatol 103 (3), 286-289 (1994)
   PUBMED   8077693
REFERENCE   8  (residues 1 to 639)
  AUTHORS   McLean,W.H., Morley,S.M., Lane,E.B., Eady,R.A., Griffiths,W.A.,
            Paige,D.G., Harper,J.I., Higgins,C. and Leigh,I.M.
  TITLE     Ichthyosis bullosa of Siemens--a disease involving keratin 2e
  JOURNAL   J Invest Dermatol 103 (3), 277-281 (1994)
   PUBMED   7521371
REFERENCE   9  (residues 1 to 639)
  AUTHORS   Rothnagel,J.A., Traupe,H., Wojcik,S., Huber,M., Hohl,D.,
            Pittelkow,M.R., Saeki,H., Ishibashi,Y. and Roop,D.R.
  TITLE     Mutations in the rod domain of keratin 2e in patients with
            ichthyosis bullosa of Siemens
  JOURNAL   Nat Genet 7 (4), 485-490 (1994)
   PUBMED   7524919
REFERENCE   10 (residues 1 to 639)
  AUTHORS   Collin,C., Moll,R., Kubicka,S., Ouhayoun,J.P. and Franke,W.W.
  TITLE     Characterization of human cytokeratin 2, an epidermal cytoskeletal
            protein synthesized late during differentiation
  JOURNAL   Exp Cell Res 202 (1), 132-141 (1992)
   PUBMED   1380918
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC055716.24, M99061.1, BC096294.4 and AL598277.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 12, 2004 this sequence version replaced NP_000414.1.
            
            Summary: The protein encoded by this gene is a member of the
            keratin gene family. The type II cytokeratins consist of basic or
            neutral proteins which are arranged in pairs of heterotypic keratin
            chains coexpressed during differentiation of simple and stratified
            epithelial tissues. This type II cytokeratin is expressed largely
            in the upper spinous layer of epidermal keratinocytes and mutations
            in this gene have been associated with bullous congenital
            ichthyosiform erythroderma. The type II cytokeratins are clustered
            in a region of chromosome 12q12-q13. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M99061.1, BC096294.4 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145893, SAMEA2147596
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309680.4/ ENSP00000310861.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..639
                     /product="keratin, type II cytoskeletal 2 epidermal"
                     /note="keratin-2e; cytokeratin-2e; keratin-2 epidermis;
                     type-II keratin Kb2; epithelial keratin-2e; keratin 2,
                     type II"
                     /calculated_mol_wt=65302
     Region          1..177
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P35908.2)"
     Site            12
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P04104; propagated from
                     UniProtKB/Swiss-Prot (P35908.2)"
     Site            20
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q3TTY5; propagated from
                     UniProtKB/Swiss-Prot (P35908.2)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04104; propagated from
                     UniProtKB/Swiss-Prot (P35908.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04104; propagated from
                     UniProtKB/Swiss-Prot (P35908.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P35908.2)"
     Region          <150..174
                     /region_name="Keratin_2_head"
                     /note="Keratin type II head; pfam16208"
                     /db_xref="CDD:465068"
     Region          177..490
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          178..213
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P35908.2)"
     Region          214..232
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P35908.2)"
     Region          233..324
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P35908.2)"
     Region          325..348
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P35908.2)"
     Region          349..487
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P35908.2)"
     Site            429
                     /site_type="other"
                     /note="Stutter; propagated from UniProtKB/Swiss-Prot
                     (P35908.2)"
     Region          488..639
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P35908.2)"
     Region          514..559
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35908.2)"
     Region          574..639
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35908.2)"
     CDS             1..639
                     /gene="KRT2"
                     /gene_synonym="CK-2e; K2e; KRT2A; KRT2E; KRTE"
                     /coded_by="NM_000423.3:70..1989"
                     /db_xref="CCDS:CCDS8835.1"
                     /db_xref="GeneID:3849"
                     /db_xref="HGNC:HGNC:6439"
                     /db_xref="MIM:600194"
ORIGIN      
        1 mscqiscksr grggggggfr gfssgsavvs ggsrrstssf sclsrhgggg ggfggggfgs
       61 rslvglggtk sisisvaggg ggfgaaggfg grgggfgggs sfgggsgfsg ggfggggfgg
      121 grfggfggpg gvgglggpgg fgpggypggi hevsvnqsll qplnvkvdpe iqnvkaqere
      181 qiktlnnkfa sfidkvrfle qqnqvlqtkw ellqqmnvgt rpinlepifq gyidslkryl
      241 dgltaertsq nselnnmqdl vedykkkyed einkrtaaen dfvtlkkdvd naymikvelq
      301 skvdllnqei eflkvlydae isqihqsvtd tnvilsmdns rnldldsiia evkaqyeeia
      361 qrskeeaeal yhskyeelqv tvgrhgdslk eikieiseln rviqrlqgei ahvkkqcknv
      421 qdaiadaeqr gehalkdarn klndleealq qakedlarll rdyqelmnvk laldveiaty
      481 rkllegeecr msgdlssnvt vsvtsstiss nvaskaafgg sggrgsssgg gyssgsssyg
      541 sggrqsgsrg gsggggsisg ggygsgggsg grygsgggsk ggsisgggyg sgggkhssgg
      601 gsrggsssgg gygsggggss svkgssgeaf gssvtfsfr
//
LOCUS       NP_001271204             337 aa            linear   PRI 27-APR-2025
DEFINITION  serpin A9 isoform C [Homo sapiens].
ACCESSION   NP_001271204 XP_005267636
VERSION     NP_001271204.2
DBSOURCE    REFSEQ: accession NM_001284275.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Berker,N., Yegen,G., Ozluk,Y. and Dogan,O.
  TITLE     Value of GCET1, HGAL (GCET2), and LMO2 in the Determination of
            Germinal Center Phenotype in Diffuse Large B-cell Lymphoma
  JOURNAL   Turk J Haematol 40 (3), 162-173 (2023)
   PUBMED   37519110
  REMARK    GeneRIF: Value of GCET1, HGAL (GCET2), and LMO2 in the
            Determination of Germinal Center Phenotype in Diffuse Large B-cell
            Lymphoma.
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Menter,T., Gasser,A., Juskevicius,D., Dirnhofer,S. and Tzankov,A.
  TITLE     Diagnostic Utility of the Germinal Center-associated Markers GCET1,
            HGAL, and LMO2 in Hematolymphoid Neoplasms
  JOURNAL   Appl Immunohistochem Mol Morphol 23 (7), 491-498 (2015)
   PUBMED   25203428
  REMARK    GeneRIF: Diagnostic Utility of the Germinal Center-associated
            Markers GCET1, HGAL, and LMO2 in Hematolymphoid Neoplasms.
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Heit,C., Jackson,B.C., McAndrews,M., Wright,M.W., Thompson,D.C.,
            Silverman,G.A., Nebert,D.W. and Vasiliou,V.
  TITLE     Update of the human and mouse SERPIN gene superfamily
  JOURNAL   Hum Genomics 7 (1), 22 (2013)
   PUBMED   24172014
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Luke,M.M., O'Meara,E.S., Rowland,C.M., Shiffman,D., Bare,L.A.,
            Arellano,A.R., Longstreth,W.T. Jr., Lumley,T., Rice,K., Tracy,R.P.,
            Devlin,J.J. and Psaty,B.M.
  TITLE     Gene variants associated with ischemic stroke: the cardiovascular
            health study
  JOURNAL   Stroke 40 (2), 363-368 (2009)
   PUBMED   19023099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Morrison,A.C., Bare,L.A., Luke,M.M., Pankow,J.S., Mosley,T.H.,
            Devlin,J.J., Willerson,J.T. and Boerwinkle,E.
  TITLE     Single nucleotide polymorphisms associated with coronary heart
            disease predict incident ischemic stroke in the atherosclerosis
            risk in communities study
  JOURNAL   Cerebrovasc Dis 26 (4), 420-424 (2008)
   PUBMED   18799872
  REMARK    GeneRIF: serpinA9 was associated with stroke in both whites and
            blacks
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Paterson,M.A., Horvath,A.J., Pike,R.N. and Coughlin,P.B.
  TITLE     Molecular characterization of centerin, a germinal centre cell
            serpin
  JOURNAL   Biochem J 405 (3), 489-494 (2007)
   PUBMED   17447896
  REMARK    GeneRIF: The cloning, expression and molecular characterization of
            recombinant serpina9 (centerin) are reported.
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Namciu,S.J., Friedman,R.D., Marsden,M.D., Sarausad,L.M.,
            Jasoni,C.L. and Fournier,R.E.
  TITLE     Sequence organization and matrix attachment regions of the human
            serine protease inhibitor gene cluster at 14q32.1
  JOURNAL   Mamm Genome 15 (3), 162-178 (2004)
   PUBMED   15014966
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Pan,Z., Shen,Y., Du,C., Zhou,G., Rosenwald,A., Staudt,L.M.,
            Greiner,T.C., McKeithan,T.W. and Chan,W.C.
  TITLE     Two newly characterized germinal center B-cell-associated genes,
            GCET1 and GCET2, have differential expression in normal and
            neoplastic B cells
  JOURNAL   Am J Pathol 163 (1), 135-144 (2003)
   PUBMED   12819018
  REMARK    GeneRIF: Results report the cloning of germinal center B-cell
            expressed transcripts 1 and 2 (GCET1 and 2), and show that both are
            expressed in follicular lymphoma and diffuse large B-cell lymphoma
            with germinal center B-cell differentiation.
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Frazer,J.K., Jackson,D.G., Gaillard,J.P., Lutter,M., Liu,Y.J.,
            Banchereau,J., Capra,J.D. and Pascual,V.
  TITLE     Identification of centerin: a novel human germinal center B
            cell-restricted serpin
  JOURNAL   Eur J Immunol 30 (10), 3039-3048 (2000)
   PUBMED   11069088
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL132708.3.
            
            On Jan 17, 2019 this sequence version replaced NP_001271204.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY220120.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.13"
     Protein         1..337
                     /product="serpin A9 isoform C"
                     /note="serine proteinase inhibitor A11; serine (or
                     cysteine) proteinase inhibitor, clade A (alpha-1
                     antiproteinase, antitrypsin), member 9; serpin A9;
                     centerin; serpin peptidase inhibitor, clade A (alpha-1
                     antiproteinase, antitrypsin), member 9; germinal center
                     B-cell-expressed transcript 1 protein"
                     /calculated_mol_wt=37784
     Region          1..337
                     /region_name="serpin"
                     /note="SERine Proteinase INhibitors (serpin) family;
                     cl38926"
                     /db_xref="CDD:476815"
     Site            order(283..293,312)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381024"
     CDS             1..337
                     /gene="SERPINA9"
                     /gene_synonym="GCET1; SERPINA11; SERPINA11b"
                     /coded_by="NM_001284275.2:130..1143"
                     /note="isoform C is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91925.1"
                     /db_xref="GeneID:327657"
                     /db_xref="HGNC:HGNC:15995"
                     /db_xref="MIM:615677"
ORIGIN      
        1 mlslgahsvt ktqilqglgf nlthtpesai hqgfqhlvhs ltvpskdltl kmgsalfvkk
       61 elqlqanflg nvkrlyeaev fstdfsnpsi aqarinshvk kktqgkvvdi iqgldlltam
      121 vlvnhiffka kwekpfhpey trknfpflvg eqvtvhvpmm hqkeqfafgv dtelncfvlq
      181 mdykgdavaf fvlpskgkmr qleqalsart lrkwshslqk rwievfiprf sisasynlet
      241 ilpkmgiqnv fdknadfsgi akrdslqvsk athkavldvs eegteataat ttkfivrskd
      301 gpsyftvsfn rtflmmitnk atdgilflgk venptks
//
LOCUS       NP_080577                140 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF125 isoform 1 [Mus musculus].
ACCESSION   NP_080577
VERSION     NP_080577.1
DBSOURCE    REFSEQ: accession NM_026301.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Chang,H., Hou,P., Wang,X., Xiang,A., Wu,H., Qi,W., Yang,R.,
            Wang,X., Li,X., He,W., Zhao,G., Sun,W., Wang,T., He,D.C., Wang,H.,
            Gao,Y. and He,H.
  TITLE     CD97 negatively regulates the innate immune response against RNA
            viruses by promoting RNF125-mediated RIG-I degradation
  JOURNAL   Cell Mol Immunol 20 (12), 1457-1471 (2023)
   PUBMED   37978243
  REMARK    GeneRIF: CD97 negatively regulates the innate immune response
            against RNA viruses by promoting RNF125-mediated RIG-I degradation.
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Jiang,C., He,L., Xiao,S., Wu,W., Zhao,Q. and Liu,F.
  TITLE     E3 Ubiquitin Ligase RNF125 Suppresses Immune Escape in Head and
            Neck Squamous Cell Carcinoma by Regulating PD-L1 Expression
  JOURNAL   Mol Biotechnol 65 (6), 891-903 (2023)
   PUBMED   36344734
  REMARK    GeneRIF: E3 Ubiquitin Ligase RNF125 Suppresses Immune Escape in
            Head and Neck Squamous Cell Carcinoma by Regulating PD-L1
            Expression.
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Pereira,M., Ko,J.H., Logan,J., Protheroe,H., Kim,K.B., Tan,A.L.M.,
            Croucher,P.I., Park,K.S., Rotival,M., Petretto,E., Bassett,J.D.,
            Williams,G.R. and Behmoaras,J.
  TITLE     A trans-eQTL network regulates osteoclast multinucleation and bone
            mass
  JOURNAL   Elife 9, e55549 (2020)
   PUBMED   32553114
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Tang,J., Tu,S., Lin,G., Guo,H., Yan,C., Liu,Q., Huang,L., Tang,N.,
            Xiao,Y., Pope,R.M., Rajaram,M.V.S., Amer,A.O., Ahmer,B.M.,
            Gunn,J.S., Wozniak,D.J., Tao,L., Coppola,V., Zhang,L.,
            Langdon,W.Y., Torrelles,J.B., Lipkowitz,S. and Zhang,J.
  TITLE     Sequential ubiquitination of NLRP3 by RNF125 and Cbl-b limits
            inflammasome activation and endotoxemia
  JOURNAL   J Exp Med 217 (4) (2020)
   PUBMED   31999304
  REMARK    GeneRIF: Sequential ubiquitination of NLRP3 by RNF125 and Cbl-b
            limits inflammasome activation and endotoxemia.
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Jia,X., Zhou,H., Wu,C., Wu,Q., Ma,S., Wei,C., Cao,Y., Song,J.,
            Zhong,H., Zhou,Z. and Wang,J.
  TITLE     The Ubiquitin Ligase RNF125 Targets Innate Immune Adaptor Protein
            TRIM14 for Ubiquitination and Degradation
  JOURNAL   J Immunol 198 (12), 4652-4658 (2017)
   PUBMED   28476934
  REMARK    GeneRIF: study identifies new gene-type zinc finger protein 125
            (RNF125) as a negative regulator of TRIM14 in the innate antiviral
            immune response
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Zhu,B., Ye,J., Nie,Y., Ashraf,U., Zohaib,A., Duan,X., Fu,Z.F.,
            Song,Y., Chen,H. and Cao,S.
  TITLE     MicroRNA-15b Modulates Japanese Encephalitis Virus-Mediated
            Inflammation via Targeting RNF125
  JOURNAL   J Immunol 195 (5), 2251-2262 (2015)
   PUBMED   26202983
  REMARK    GeneRIF: Data indicate that brain from Japanese encephalitis virus
            (JEV)-infection showed a reciprocal correlation between microRNA
            miR-15b levels and the expression of ring finger protein 125
            (RNF125).
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Arimoto,K., Takahashi,H., Hishiki,T., Konishi,H., Fujita,T. and
            Shimotohno,K.
  TITLE     Negative regulation of the RIG-I signaling by the ubiquitin ligase
            RNF125
  JOURNAL   Proc Natl Acad Sci U S A 104 (18), 7500-7505 (2007)
   PUBMED   17460044
  REMARK    GeneRIF: RNF125 is enhanced by IFN, these functions constitute a
            negative regulatory loop circuit for IFN production
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138611.4, AK050395.1, AK050462.1 and BF148133.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK050395.1, BB654038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849376
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18"
     Protein         1..140
                     /product="E3 ubiquitin-protein ligase RNF125 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF125"
                     /calculated_mol_wt=16170
     Region          2..34
                     /region_name="zf_C2HC_14"
                     /note="C2HC Zing finger domain; pfam18574"
                     /db_xref="CDD:465807"
     Region          49..>81
                     /region_name="zf-Di19"
                     /note="Drought induced 19 protein (Di19), zinc-binding;
                     pfam05605"
                     /db_xref="CDD:428539"
     CDS             1..140
                     /gene="Rnf125"
                     /gene_synonym="4930553F04Rik; C730049O14Rik"
                     /coded_by="NM_026301.3:259..681"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS29088.1"
                     /db_xref="GeneID:67664"
                     /db_xref="MGI:MGI:1914914"
ORIGIN      
        1 mkseyqncae cgtlvclsdm rahirtceky idkygpllel gdttarcvcp fcqreldedc
       61 lldhciihhr serrpvfcpl chsrpdesps tfngslirhl qvshtlfydd fidfdiieea
      121 iirrvldrsl leyvnqsntt
//
LOCUS       NP_061156                434 aa            linear   PRI 27-APR-2025
DEFINITION  N-acylneuraminate cytidylyltransferase [Homo sapiens].
ACCESSION   NP_061156
VERSION     NP_061156.1
DBSOURCE    REFSEQ: accession NM_018686.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Qu,R., Sang,Q., Wang,X., Xu,Y., Chen,B., Mu,J., Zhang,Z., Jin,L.,
            He,L. and Wang,L.
  TITLE     A homozygous mutation in CMAS causes autosomal recessive
            intellectual disability in a Kazakh family
  JOURNAL   Ann Hum Genet 84 (1), 46-53 (2020)
   PUBMED   31495922
  REMARK    GeneRIF: A homozygous mutation in CMAS causes autosomal recessive
            intellectual disability in a Kazakh family.
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Willems,A.P., Sun,L., Schulz,M.A., Tian,W., Ashikov,A., van
            Scherpenzeel,M., Hermans,E., Clausen,H., Yang,Z. and Lefeber,D.J.
  TITLE     Activity of N-acylneuraminate-9-phosphatase (NANP) is not essential
            for de novo sialic acid biosynthesis
  JOURNAL   Biochim Biophys Acta Gen Subj 1863 (10), 1471-1479 (2019)
   PUBMED   31121216
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Ma,Y., Tian,S., Wang,Z., Wang,C., Chen,X., Li,W., Yang,Y. and He,S.
  TITLE     CMP-N-acetylneuraminic acid synthetase interacts with fragile X
            related protein 1
  JOURNAL   Mol Med Rep 14 (2), 1501-1508 (2016)
   PUBMED   27357083
  REMARK    GeneRIF: FXR1P interacts with CMAS, and that FXR1P may enhance the
            activation of sialic acid via interaction with CMAS, and increase
            GM1 levels to affect the development of the nervous system, thus
            providing evidence for further research into the pathogenesis of
            FXS.
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Carette,J.E., Guimaraes,C.P., Varadarajan,M., Park,A.S.,
            Wuethrich,I., Godarova,A., Kotecki,M., Cochran,B.H., Spooner,E.,
            Ploegh,H.L. and Brummelkamp,T.R.
  TITLE     Haploid genetic screens in human cells identify host factors used
            by pathogens
  JOURNAL   Science 326 (5957), 1231-1235 (2009)
   PUBMED   19965467
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Oschlies,M., Dickmanns,A., Haselhorst,T., Schaper,W., Stummeyer,K.,
            Tiralongo,J., Weinhold,B., Gerardy-Schahn,R., von Itzstein,M.,
            Ficner,R. and Munster-Kuhnel,A.K.
  TITLE     A C-terminal phosphatase module conserved in vertebrate CMP-sialic
            acid synthetases provides a tetramerization interface for the
            physiologically active enzyme
  JOURNAL   J Mol Biol 393 (1), 83-97 (2009)
   PUBMED   19666032
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Munster,A.K., Weinhold,B., Gotza,B., Muhlenhoff,M., Frosch,M. and
            Gerardy-Schahn,R.
  TITLE     Nuclear localization signal of murine CMP-Neu5Ac synthetase
            includes residues required for both nuclear targeting and enzymatic
            activity
  JOURNAL   J Biol Chem 277 (22), 19688-19696 (2002)
   PUBMED   11893746
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Angata,T., Varki,N.M. and Varki,A.
  TITLE     A second uniquely human mutation affecting sialic acid biology
  JOURNAL   J Biol Chem 276 (43), 40282-40287 (2001)
   PUBMED   11546777
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Lawrence,S.M., Huddleston,K.A., Tomiya,N., Nguyen,N., Lee,Y.C.,
            Vann,W.F., Coleman,T.A. and Betenbaugh,M.J.
  TITLE     Cloning and expression of human sialic acid pathway genes to
            generate CMP-sialic acids in insect cells
  JOURNAL   Glycoconj J 18 (3), 205-213 (2001)
   PUBMED   11602804
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Munster,A.K., Eckhardt,M., Potvin,B., Muhlenhoff,M., Stanley,P. and
            Gerardy-Schahn,R.
  TITLE     Mammalian cytidine 5'-monophosphate N-acetylneuraminic acid
            synthetase: a nuclear protein with evolutionarily conserved
            structural motifs
  JOURNAL   Proc Natl Acad Sci U S A 95 (16), 9140-9145 (1998)
   PUBMED   9689047
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA344740.1, AL832975.1 and
            DB527942.1.
            
            Summary: This gene encodes an enzyme that converts
            N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate
            N-acetylneuraminic acid (CMP-NeuNAc). This process is important in
            the formation of sialylated glycoprotein and glycolipids. This
            modification plays a role in cell-cell communications and immune
            responses. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.640875.1,
                                           SRR1660807.49931.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000229329.7/ ENSP00000229329.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..434
                     /product="N-acylneuraminate cytidylyltransferase"
                     /EC_number="2.7.7.43"
                     /note="CMP-N-acetylneuraminic acid synthase; CMP-Neu5Ac
                     synthetase; cytidine 5'-monophosphate N-acetylneuraminic
                     acid synthetase; CMP-NeuNAc synthetase;
                     CMP-N-acetylneuraminic acid synthetase; CMP-NeuNAc
                     synthase; CMP-sialic acid synthetase"
                     /calculated_mol_wt=48248
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW8.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8NFW8.2)"
     Region          15..31
                     /region_name="BC1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW8.2)"
     Site            37
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q99KK2; propagated from
                     UniProtKB/Swiss-Prot (Q8NFW8.2)"
     Region          44..259
                     /region_name="CMP-NeuAc_Synthase"
                     /note="CMP-NeuAc_Synthase activates N-acetylneuraminic
                     acid by adding CMP moiety; cd02513"
                     /db_xref="CDD:133006"
     Site            order(50..52,56,62,111,115,122,143,145,213,218,249)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133006"
     Site            52
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q99KK2; propagated from
                     UniProtKB/Swiss-Prot (Q8NFW8.2)"
     Site            order(65,67..68,170,174..175,210..213,218,235,237,249,
                     252..253,256,259)
                     /site_type="active"
                     /note="tetramer interface [active]"
                     /db_xref="CDD:133006"
     Region          200..206
                     /region_name="BC2 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW8.2)"
     Region          269..276
                     /region_name="BC3 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFW8.2)"
     Region          275..419
                     /region_name="HAD_KDO-like"
                     /note="haloacid dehalogenase-like (HAD) hydrolase, similar
                     to Escherichia coli 3-deoxy-D-manno-octulosonate
                     8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout
                     N-acylneuraminate cytidylyltransferase; cd01630"
                     /db_xref="CDD:319769"
     Site            order(281..285,325..326,350,372..373,376..377)
                     /site_type="active"
                     /db_xref="CDD:319769"
     Site            order(283,288..295,297,299..306,309,313,327,331..332,
                     335..336,339,348,373..376,378..379,392,396,411,415,419)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:319769"
     CDS             1..434
                     /gene="CMAS"
                     /gene_synonym="CSS"
                     /coded_by="NM_018686.6:87..1391"
                     /db_xref="CCDS:CCDS8696.1"
                     /db_xref="GeneID:55907"
                     /db_xref="HGNC:HGNC:18290"
                     /db_xref="MIM:603316"
ORIGIN      
        1 mdsvekgaat svsnprgrps rgrppklqrn srggqgrgve kpphlaalil arggskgipl
       61 knikhlagvp ligwvlraal dsgafqsvwv stdhdeienv akqfgaqvhr rssevskdss
      121 tsldaiiefl nyhnevdivg niqatspclh ptdlqkvaem ireegydsvf svvrrhqfrw
      181 seiqkgvrev teplnlnpak rprrqdwdge lyengsfyfa krhliemgyl qggkmayyem
      241 raehsvdidv didwpiaeqr vlrygyfgke klkeikllvc nidgcltngh iyvsgdqkei
      301 isydvkdaig isllkksgie vrliseracs kqtlsslkld ckmevsvsdk lavvdewrke
      361 mglcwkevay lgnevsdeec lkrvglsgap adacstaqka vgyickcngg rgairefaeh
      421 icllmekvnn scqk
//
LOCUS       NP_001121674             186 aa            linear   PRI 27-APR-2025
DEFINITION  testis-expressed protein 36 isoform a [Homo sapiens].
ACCESSION   NP_001121674
VERSION     NP_001121674.1
DBSOURCE    REFSEQ: accession NM_001128202.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Chalasani,N., Guo,X., Loomba,R., Goodarzi,M.O., Haritunians,T.,
            Kwon,S., Cui,J., Taylor,K.D., Wilson,L., Cummings,O.W., Chen,Y.D.
            and Rotter,J.I.
  CONSRTM   Nonalcoholic Steatohepatitis Clinical Research Network
  TITLE     Genome-wide association study identifies variants associated with
            histologic features of nonalcoholic Fatty liver disease
  JOURNAL   Gastroenterology 139 (5), 1567-1576 (2010)
   PUBMED   20708005
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL158835.11, BC062717.1 and AA977508.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.30863.1, BC062717.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368821.4/ ENSP00000357811.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..186
                     /product="testis-expressed protein 36 isoform a"
                     /note="testis-expressed sequence 36 protein;
                     testis-expressed protein 36"
                     /calculated_mol_wt=21413
     Region          1..176
                     /region_name="HDNR"
                     /note="Domain of unknown function with conserved HDNR
                     motif; pfam15115"
                     /db_xref="CDD:464512"
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VZQ5.1)"
     CDS             1..186
                     /gene="TEX36"
                     /gene_synonym="bA383C5.1; C10orf122"
                     /coded_by="NM_001128202.3:175..735"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44493.1"
                     /db_xref="GeneID:387718"
                     /db_xref="HGNC:HGNC:31653"
ORIGIN      
        1 mtkgrrfnpp sdkdgrwfph igltqktpes itsatskepq sphlprqaeg klppiykvre
       61 kqavnnqfpf svhdnrhsle nsgcyldsgl grkkispdkr qhvsrnfnlw acdyvpscld
      121 gfsnnqisyv ykeamvvssf rrfprcykei wnaftflper sytevlkkkp kvrftvdkkv
      181 vssles
//
LOCUS       NP_001124396             666 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 201 isoform 1 [Homo sapiens].
ACCESSION   NP_001124396
VERSION     NP_001124396.2
DBSOURCE    REFSEQ: accession NM_001130924.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Chen,D., Lou,Y., Lu,J., Fan,X., Zhu,Q. and Sun,H.
  TITLE     Characterization of the Clinical Significance and Immunological
            Landscapes of a Novel TMEMs Signature in Hepatocellular Carcinoma
            and the Contribution of TMEM201 to Hepatocarcinogenesis
  JOURNAL   Int J Mol Sci 24 (12), 10285 (2023)
   PUBMED   37373430
  REMARK    GeneRIF: Characterization of the Clinical Significance and
            Immunological Landscapes of a Novel TMEMs Signature in
            Hepatocellular Carcinoma and the Contribution of TMEM201 to
            Hepatocarcinogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Zhang,Y., Kong,Y., Guo,H., Liu,Y., Zang,Y. and Li,J.
  TITLE     Inner nuclear membrane protein TMEM201 maintains endothelial cell
            migration and angiogenesis by interacting with the LINC complex
  JOURNAL   J Mol Cell Biol 14 (3) (2022)
   PUBMED   35311970
  REMARK    GeneRIF: Inner nuclear membrane protein TMEM201 maintains
            endothelial cell migration and angiogenesis by interacting with the
            LINC complex.
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Bergqvist,C., Niss,F., Figueroa,R.A., Beckman,M., Maksel,D.,
            Jafferali,M.H., Kulyte,A., Strom,A.L. and Hallberg,E.
  TITLE     Monitoring of chromatin organization in live cells by FRIC. Effects
            of the inner nuclear membrane protein Samp1
  JOURNAL   Nucleic Acids Res 47 (9), e49 (2019)
   PUBMED   30793190
  REMARK    GeneRIF: We also found that peripheral heterochromatin depended on
            the levels of the inner nuclear membrane protein Samp1, suggesting
            an important role in promoting peripheral heterochromatin. Taken
            together, FRIC is a powerful and robust new tool to study dynamic
            chromatin redistribution in live cells.
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Larsson,V.J., Jafferali,M.H., Vijayaraghavan,B., Figueroa,R.A. and
            Hallberg,E.
  TITLE     Mitotic spindle assembly and gamma-tubulin localisation depend on
            the integral nuclear membrane protein Samp1
  JOURNAL   J Cell Sci 131 (8) (2018)
   PUBMED   29514856
  REMARK    GeneRIF: Authors show that Samp1 is involved in the recruitment of
            HAUS6 and gamma-tubulin to the mitotic spindle. Samp1 is the first
            inner nuclear membrane protein shown to have a function in mitotic
            spindle assembly.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Vijayaraghavan,B., Jafferali,M.H., Figueroa,R.A. and Hallberg,E.
  TITLE     Samp1, a RanGTP binding transmembrane protein in the inner nuclear
            membrane
  JOURNAL   Nucleus 7 (4), 415-423 (2016)
   PUBMED   27541860
REFERENCE   7  (residues 1 to 666)
  AUTHORS   Jafferali,M.H., Vijayaraghavan,B., Figueroa,R.A., Crafoord,E.,
            Gudise,S., Larsson,V.J. and Hallberg,E.
  TITLE     MCLIP, an effective method to detect interactions of transmembrane
            proteins of the nuclear envelope in live cells
  JOURNAL   Biochim Biophys Acta 1838 (10), 2399-2403 (2014)
   PUBMED   24950247
  REMARK    GeneRIF: the nucleoplasmic domains of Samp1 and Emerin can bind
            directly to each other.
REFERENCE   8  (residues 1 to 666)
  AUTHORS   Gudise,S., Figueroa,R.A., Lindberg,R., Larsson,V. and Hallberg,E.
  TITLE     Samp1 is functionally associated with the LINC complex and A-type
            lamina networks
  JOURNAL   J Cell Sci 124 (Pt 12), 2077-2085 (2011)
   PUBMED   21610090
REFERENCE   9  (residues 1 to 666)
  AUTHORS   Figueroa,R., Gudise,S., Larsson,V. and Hallberg,E.
  TITLE     A transmembrane inner nuclear membrane protein in the mitotic
            spindle
  JOURNAL   Nucleus 1 (3), 249-253 (2010)
   PUBMED   21327071
  REMARK    Review article
REFERENCE   10 (residues 1 to 666)
  AUTHORS   Buch,C., Lindberg,R., Figueroa,R., Gudise,S., Onischenko,E. and
            Hallberg,E.
  TITLE     An integral protein of the inner nuclear membrane localizes to the
            mitotic spindle in mammalian cells
  JOURNAL   J Cell Sci 122 (Pt 12), 2100-2107 (2009)
   PUBMED   19494128
  REMARK    GeneRIF: characterization of a transmembrane protein of the nuclear
            envelope that we name spindle-associated membrane protein 1
            (Samp1); Samp1 defines a specific membrane domain associated with
            the mitotic spindle
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC137291.1, BX648377.1, BG828926.1 and BE676679.1.
            
            On Nov 5, 2009 this sequence version replaced NP_001124396.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.117295.1,
                                           SRR9304716.324777.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340381.11/ ENSP00000344503.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..666
                     /product="transmembrane protein 201 isoform 1"
                     /note="spindle-associated membrane protein 1;
                     RP13-15M17.2"
                     /calculated_mol_wt=72105
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Region          47..169
                     /region_name="Ima1_N"
                     /note="Ima1 N-terminal domain; pfam09779"
                     /db_xref="CDD:462895"
     Region          191..379
                     /region_name="DUF2448"
                     /note="Protein of unknown function C-terminus (DUF2448);
                     pfam10476"
                     /db_xref="CDD:463104"
     Site            214..234
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            357..374
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Region          502..581
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q5SNT2.1)"
     Site            645..665
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNT2.1)"
     CDS             1..666
                     /gene="TMEM201"
                     /gene_synonym="Ima1; NET5; SAMP1"
                     /coded_by="NM_001130924.3:21..2021"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44055.2"
                     /db_xref="GeneID:199953"
                     /db_xref="HGNC:HGNC:33719"
ORIGIN      
        1 megvsallar cptaglaggl gvtacaaagv llyriarrmk pthtmvncwf cnqdtlvpyg
       61 nrncwdcphc eqyngfqeng dynkpipaqy lehlnhvvss apslrdpsqp qqwvssqvll
      121 ckrcnhhqtt kikqlaafap reegrydeev evyrhhleqm yklcrpcqaa veyyikhqnr
      181 qlralllshq fkrreadqth aqnfssavks pvqvillral aflacafllt talygasghf
      241 apgttvplal ppggngsatp dngttpgaeg wrqllgllpe hmaeklceaw afgqshqtgv
      301 valglltcll amllagrirl rridafctcl walllglhla eqhlqaasps wldtlkfstt
      361 slcclvgfta avatrkatgp rrfrprrffp gdsaglfpts pslaiphpsv ggspaslfip
      421 sppsflplan qqlfrsprrt spsslpgrls ralslgtips ltradsgylf sgsrppsqvs
      481 rsgefpvsdy fsllsgscps splpspapsv agsvasssgs lrhrrplisp arlnlkgqkl
      541 llfpsppgea pttpsssdeh sphngslftm epphvprkpp lqdvkhaldl rsklergsac
      601 snrsikkedd ssqsstcvvd tttrgcseea atwrgrfgps lvrgllavsl aanalftsvf
      661 lyqslr
//
LOCUS       NP_000901                381 aa            linear   PRI 27-APR-2025
DEFINITION  neuropeptide Y receptor type 2 [Homo sapiens].
ACCESSION   NP_000901
VERSION     NP_000901.1
DBSOURCE    REFSEQ: accession NM_000910.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kang,H., Park,C., Choi,Y.K., Bae,J., Kwon,S., Kim,J., Choi,C.,
            Seok,C., Im,W. and Choi,H.J.
  TITLE     Structural basis for Y2 receptor-mediated neuropeptide Y and
            peptide YY signaling
  JOURNAL   Structure 31 (1), 44-57 (2023)
   PUBMED   36525977
  REMARK    GeneRIF: Structural basis for Y2 receptor-mediated neuropeptide Y
            and peptide YY signaling.
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Wickham,J., Ledri,M., Bengzon,J., Jespersen,B., Pinborg,L.H.,
            Englund,E., Woldbye,D.P.D., Andersson,M. and Kokaia,M.
  TITLE     Inhibition of epileptiform activity by neuropeptide Y in brain
            tissue from drug-resistant temporal lobe epilepsy patients
  JOURNAL   Sci Rep 9 (1), 19393 (2019)
   PUBMED   31852985
  REMARK    GeneRIF: Inhibition of epileptiform activity by neuropeptide Y in
            brain tissue from drug-resistant temporal lobe epilepsy patients.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Derkac,I., Januleviciene,I., Sepetiene,R., Valiauga,R. and
            Velickiene,D.
  TITLE     The Association of CEP135 rs4865047 and NPY2R rs1902491 Single
            Nucleotide Polymorphisms (SNPs) with Rapid Progression of
            Proliferative Diabetic Retinopathy in Patients with Type 1 Diabetes
            Mellitus
  JOURNAL   Med Sci Monit 24, 8891-8898 (2018)
   PUBMED   30531682
  REMARK    GeneRIF: The analysis of the distribution of genotypes in CEP135
            rs4865047 and NPY2R rs1902491 detected significant differences only
            in the single nucleotide polymorphism rs4865047 genotype between
            the case and control group in comparison to the reference group.
            No significant association was found for the NPY2R SNP rs1902491
            genotype.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Aerts,E., Geets,E., Sorber,L., Beckers,S., Verrijken,A., Massa,G.,
            Van Hoorenbeeck,K., Verhulst,S.L., Van Gaal,L.F. and Van Hul,W.
  TITLE     Evaluation of a Role for NPY and NPY2R in the Pathogenesis of
            Obesity by Mutation and Copy Number Variation Analysis in Obese
            Children and Adolescents
  JOURNAL   Ann Hum Genet 82 (1), 1-10 (2018)
   PUBMED   28857123
  REMARK    GeneRIF: genetic variation in NPY and NPY2R is at low frequency and
            thus does not make a major contribution to the obese phenotype in
            the general population
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Gerald,C., Walker,M.W., Vaysse,P.J., He,C., Branchek,T.A. and
            Weinshank,R.L.
  TITLE     Expression cloning and pharmacological characterization of a human
            hippocampal neuropeptide Y/peptide YY Y2 receptor subtype
  JOURNAL   J Biol Chem 270 (45), 26758-26761 (1995)
   PUBMED   7592910
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Rose,P.M., Fernandes,P., Lynch,J.S., Frazier,S.T., Fisher,S.M.,
            Kodukula,K., Kienzle,B. and Seethala,R.
  TITLE     Cloning and functional expression of a cDNA encoding a human type 2
            neuropeptide Y receptor
  JOURNAL   J Biol Chem 270 (39), 22661-22664 (1995)
   PUBMED   7559383
  REMARK    Erratum:[J Biol Chem. 1995 Dec 1;270(48):29038. PMID: 7499438]
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Lynch,J.W., Lemos,V.S., Bucher,B., Stoclet,J.C. and Takeda,K.
  TITLE     A pertussis toxin-insensitive calcium influx mediated by
            neuropeptide Y2 receptors in a human neuroblastoma cell line
  JOURNAL   J Biol Chem 269 (11), 8226-8233 (1994)
   PUBMED   8132547
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Herzog,H., Hort,Y.J., Ball,H.J., Hayes,G., Shine,J. and Selbie,L.A.
  TITLE     Cloned human neuropeptide Y receptor couples to two different
            second messenger systems
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5794-5798 (1992)
   PUBMED   1321422
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Itoh,H., Toyama,R., Kozasa,T., Tsukamoto,T., Matsuoka,M. and
            Kaziro,Y.
  TITLE     Presence of three distinct molecular species of Gi protein alpha
            subunit. Structure of rat cDNAs and human genomic DNAs
  JOURNAL   J Biol Chem 263 (14), 6656-6664 (1988)
   PUBMED   2834384
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U42766.1 and U36269.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U42766.1, SRR1803612.265344.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329476.4/ ENSP00000332591.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q32.1"
     Protein         1..381
                     /product="neuropeptide Y receptor type 2"
                     /note="NPY-Y2 receptor"
                     /calculated_mol_wt=42600
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49146.1)"
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49146.1)"
     Region          51..336
                     /region_name="7tmA_NPY2R"
                     /note="neuropeptide Y receptor type 2, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15399"
                     /db_xref="CDD:320521"
     Region          52..78
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320521"
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49146.1)"
     Region          85..110
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320521"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49146.1)"
     Site            order(107,110..111,123..128,130..131,134,177,179..183,216,
                     219..221,223..225,227..228,281,284..285,287..288,291,
                     303..304,306..308,311,314..315)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320521"
     Region          123..153
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320521"
     Site            125..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49146.1)"
     Region          164..185
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320521"
     Site            166..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49146.1)"
     Region          216..245
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320521"
     Site            217..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49146.1)"
     Region          261..291
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320521"
     Site            269..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49146.1)"
     Region          304..329
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320521"
     Site            305..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49146.1)"
     CDS             1..381
                     /gene="NPY2R"
                     /gene_synonym="NPY2-R"
                     /coded_by="NM_000910.4:483..1628"
                     /db_xref="CCDS:CCDS3791.1"
                     /db_xref="GeneID:4887"
                     /db_xref="HGNC:HGNC:7957"
                     /db_xref="MIM:162642"
ORIGIN      
        1 mgpigaeade nqtveemkve qygpqttprg elvpdpepel idstklievq vvlilaycsi
       61 illgvignsl vihvvikfks mrtvtnffia nlavadllvn tlclpftlty tlmgewkmgp
      121 vlchlvpyaq glavqvstit ltvialdrhr civyhleski skrisfliig lawgisalla
      181 splaifreys lieiipdfei vactekwpge eksiygtvys lssllilyvl plgiisfsyt
      241 riwsklknhv spgaandhyh qrrqkttkml vcvvvvfavs wlplhafqla vdidsqvldl
      301 keykliftvf hiiamcstfa npllygwmns nyrkaflsaf rceqrldaih sevsvtfkak
      361 knlevrknsg pndsfteatn v
//
LOCUS       NP_057622                400 aa            linear   PRI 27-APR-2025
DEFINITION  NAD-dependent protein deacetylase sirtuin-7 [Homo sapiens].
ACCESSION   NP_057622
VERSION     NP_057622.1
DBSOURCE    REFSEQ: accession NM_016538.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Du,J., Yi,X., Guo,S., Wang,H., Shi,Q., Zhang,J., Tian,Y., Wang,H.,
            Zhang,H., Zhang,B., Gao,T., Li,C., Guo,W. and Yang,Y.
  TITLE     SIRT7 promotes mitochondrial biogenesis to render the adaptive
            resistance to MAPK inhibition in melanoma
  JOURNAL   Biochem Biophys Res Commun 722, 150161 (2024)
   PUBMED   38797153
  REMARK    GeneRIF: SIRT7 promotes mitochondrial biogenesis to render the
            adaptive resistance to MAPK inhibition in melanoma.
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Wang,M.D., Gao,T.Y., Huang,W., Yang,Y.K. and Wang,Y.
  TITLE     [Effect of SIRT7 on inhibiting the epithelial-mesenchymal
            transformation in pancreatic cancer cells and related mechanism]
  JOURNAL   Zhonghua Zhong Liu Za Zhi 46 (6), 566-582 (2024)
   PUBMED   38880736
  REMARK    GeneRIF: [Effect of SIRT7 on inhibiting the epithelial-mesenchymal
            transformation in pancreatic cancer cells and related mechanism].
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Kumari,P., Tarighi,S., Fuchshuber,E., Li,L., Fernandez-Duran,I.,
            Wang,M., Ayoson,J., Castello-Garcia,J.M., Gamez-Garcia,A.,
            Espinosa-Alcantud,M., Sreenivasan,K., Guenther,S., Olivella,M.,
            Savai,R., Yue,S., Vaquero,A., Braun,T. and Ianni,A.
  TITLE     SIRT7 promotes lung cancer progression by destabilizing the tumor
            suppressor ARF
  JOURNAL   Proc Natl Acad Sci U S A 121 (25), e2409269121 (2024)
   PUBMED   38870055
  REMARK    GeneRIF: SIRT7 promotes lung cancer progression by destabilizing
            the tumor suppressor ARF.
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Lu,L., Zhu,M., Wu,Q., Sun,Z., Chen,X. and Miao,C.
  TITLE     Sirt7/HIC1 complex participates in hyperglycaemia-mediated EndMT
            via modulation of SDC1 expression in diabetic kidney disease and
            metabolic memory
  JOURNAL   J Cell Mol Med 28 (9), e18336 (2024)
   PUBMED   38686489
  REMARK    GeneRIF: Sirt7/HIC1 complex participates in hyperglycaemia-mediated
            EndMT via modulation of SDC1 expression in diabetic kidney disease
            and metabolic memory.
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Xu,B., Cai,X., Cai,G. and Huang,G.
  TITLE     SIRT7: A potential prognostic marker and therapeutic target in
            gallbladder cancer
  JOURNAL   Pathol Res Pract 256, 155233 (2024)
   PUBMED   38452583
  REMARK    GeneRIF: SIRT7: A potential prognostic marker and therapeutic
            target in gallbladder cancer.
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Michishita,E., Park,J.Y., Burneskis,J.M., Barrett,J.C. and
            Horikawa,I.
  TITLE     Evolutionarily conserved and nonconserved cellular localizations
            and functions of human SIRT proteins
  JOURNAL   Mol Biol Cell 16 (10), 4623-4635 (2005)
   PUBMED   16079181
REFERENCE   7  (residues 1 to 400)
  AUTHORS   De Nigris,F., Cerutti,J., Morelli,C., Califano,D., Chiariotti,L.,
            Viglietto,G., Santelli,G. and Fusco,A.
  TITLE     Isolation of a SIR-like gene, SIR-T8, that is overexpressed in
            thyroid carcinoma cell lines and tissues
  JOURNAL   Br J Cancer 87 (12), 1479 (2002)
   PUBMED   12454780
  REMARK    Correction to:[Br J Cancer. 2002 Mar 18;86(6):917-23. doi:
            10.1038/sj.bjc.6600156. PMID: 11953824]
REFERENCE   8  (residues 1 to 400)
  AUTHORS   de Nigris,F., Cerutti,J., Morelli,C., Califano,D., Chiariotti,L.,
            Viglietto,G., Santelli,G. and Fusco,A.
  TITLE     Isolation of a SIR-like gene, SIR-T8, that is overexpressed in
            thyroid carcinoma cell lines and tissues
  JOURNAL   Br J Cancer 86 (6), 917-923 (2002)
   PUBMED   11953824
  REMARK    Erratum:[Br J Cancer. 2002 Dec 2;87(12):1479. doi:
            10.1038/sj.bjc.6600636. PMID: 12454780]
REFERENCE   9  (residues 1 to 400)
  AUTHORS   Frye,R.A.
  TITLE     Phylogenetic classification of prokaryotic and eukaryotic Sir2-like
            proteins
  JOURNAL   Biochem Biophys Res Commun 273 (2), 793-798 (2000)
   PUBMED   10873683
REFERENCE   10 (residues 1 to 400)
  AUTHORS   Bussow,K., Cahill,D., Nietfeld,W., Bancroft,D., Scherzinger,E.,
            Lehrach,H. and Walter,G.
  TITLE     A method for global protein expression and antibody screening on
            high-density filters of an arrayed cDNA library
  JOURNAL   Nucleic Acids Res 26 (21), 5007-5008 (1998)
   PUBMED   9776767
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ890203.1, BC101791.1,
            CD579273.2 and BC017305.2.
            
            Summary: This gene encodes a member of the sirtuin family of
            proteins, homologs to the yeast Sir2 protein. Members of the
            sirtuin family are characterized by a sirtuin core domain and
            grouped into four classes. The functions of human sirtuins have not
            yet been determined; however, yeast sirtuin proteins are known to
            regulate epigenetic gene silencing and suppress recombination of
            rDNA. Studies suggest that the human sirtuins may function as
            intracellular regulatory proteins with mono-ADP-ribosyltransferase
            activity. The protein encoded by this gene is included in class IV
            of the sirtuin family. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.960718.1,
                                           SRR3476690.230925.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000328666.11/ ENSP00000329466.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..400
                     /product="NAD-dependent protein deacetylase sirtuin-7"
                     /EC_number="2.3.1.286"
                     /note="silent mating type information regulation 2,
                     S.cerevisiae, homolog 7; sir2-related protein type 7;
                     sirtuin type 7; NAD-dependent deacetylase sirtuin-7;
                     SIR2-like protein 7; regulatory protein SIR2 homolog 7;
                     NAD-dependent protein deacylase sirtuin-7"
                     /calculated_mol_wt=44767
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC8.1)"
     Region          <10..>86
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          100..314
                     /region_name="SIRT7"
                     /note="Eukaryotic and prokaryotic group (class4) which
                     includes human sirtuin SIRT6, SIRT7, and several bacterial
                     homologs; and are members of the SIR2 family of proteins,
                     silent information regulator 2 (Sir2) enzymes which
                     catalyze NAD+-dependent protein...; cd01410"
                     /db_xref="CDD:238701"
     Site            order(109,111..112,119..120,149,167..168,170,187,268,273,
                     298..299,314)
                     /site_type="other"
                     /note="NAD+ binding site [chemical binding]"
                     /db_xref="CDD:238701"
     Site            order(169,187,237,239..243,272..273,277)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238701"
     Site            order(195,198,225,228)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:238701"
     Region          354..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC8.1)"
     Site            388
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:30420520;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:30420520,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9NRC8.1)"
     CDS             1..400
                     /gene="SIRT7"
                     /gene_synonym="SIR2L7"
                     /coded_by="NM_016538.3:46..1248"
                     /db_xref="CCDS:CCDS11792.1"
                     /db_xref="GeneID:51547"
                     /db_xref="HGNC:HGNC:14935"
                     /db_xref="MIM:606212"
ORIGIN      
        1 maagglsrse rkaaervrrl reeqqrerlr qvsrilrkaa aersaeegrl laesadlvte
       61 lqgrsrrreg lkrrqeevcd dpeelrgkvr elasavrnak ylvvytgagi staasipdyr
      121 gpngvwtllq kgrsvsaadl seaeptlthm sitrlheqkl vqhvvsqncd glhlrsglpr
      181 taiselhgnm yievctscvp nreyvrvfdv tertalhrhq tgrtchkcgt qlrdtivhfg
      241 ergtlgqpln weaateaasr adtilclgss lkvlkkyprl wcmtkppsrr pklyivnlqw
      301 tpkddwaalk lhgkcddvmr llmaelglei paysrwqdpi fslatplrag eegshsrksl
      361 crsreeappg drgaplssap ilggwfgrgc tkrtkrkkvt
//
LOCUS       NP_005609                723 aa            linear   PRI 27-APR-2025
DEFINITION  delta-like protein 1 precursor [Homo sapiens].
ACCESSION   NP_005609
VERSION     NP_005609.3
DBSOURCE    REFSEQ: accession NM_005618.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Xu,Y., Qiu,Z., Chen,J., Huang,L., Zhang,J. and Lin,J.
  TITLE     LINC00460 promotes neuroblastoma tumorigenesis and cisplatin
            resistance by targeting miR-149-5p/DLL1 axis and activating Notch
            pathway in vitro and in vivo
  JOURNAL   Drug Deliv Transl Res 14 (7), 2003-2018 (2024)
   PUBMED   38161194
  REMARK    GeneRIF: LINC00460 promotes neuroblastoma tumorigenesis and
            cisplatin resistance by targeting miR-149-5p/DLL1 axis and
            activating Notch pathway in vitro and in vivo.
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Engwerda,A., Kerstjens-Frederikse,W.S., Corsten-Janssen,N.,
            Dijkhuizen,T. and van Ravenswaaij-Arts,C.M.A.
  TITLE     The phenotypic spectrum of terminal 6q deletions based on a large
            cohort derived from social media and literature: a prominent role
            for DLL1
  JOURNAL   Orphanet J Rare Dis 18 (1), 59 (2023)
   PUBMED   36935482
  REMARK    GeneRIF: The phenotypic spectrum of terminal 6q deletions based on
            a large cohort derived from social media and literature: a
            prominent role for DLL1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 723)
  AUTHORS   Chen,L., Lu,H., Peng,D., Cao,L.L., Ballout,F., Srirmajayam,K.,
            Chen,Z., Bhat,A., Wang,T.C., Capobianco,A., Que,J., McDonald,O.G.,
            Zaika,A., Zhang,S. and El-Rifai,W.
  TITLE     Activation of NOTCH signaling via DLL1 is mediated by
            APE1-redox-dependent NF-kappaB activation in oesophageal
            adenocarcinoma
  JOURNAL   Gut 72 (3), 421-432 (2023)
   PUBMED   35750470
  REMARK    GeneRIF: Activation of NOTCH signaling via DLL1 is mediated by
            APE1-redox-dependent NF-kappaB activation in oesophageal
            adenocarcinoma.
REFERENCE   4  (residues 1 to 723)
  AUTHORS   Hildebrand,D., Nurjadi,D., Hoan,N.X., Linh,M.T.H., Sang,V.V.,
            Bang,M.H., Pallerla,S.R., Kremsner,P.G., Heeg,K., Song,L.H. and
            Velavan,T.P.
  TITLE     Association Between Soluble Notch Ligand Delta-like Ligand 1 and
            Bleeding Complications in Patients With Dengue Fever Infection
  JOURNAL   J Infect Dis 225 (3), 476-480 (2022)
   PUBMED   34375432
  REMARK    GeneRIF: Association Between Soluble Notch Ligand Delta-like Ligand
            1 and Bleeding Complications in Patients With Dengue Fever
            Infection.
REFERENCE   5  (residues 1 to 723)
  AUTHORS   Lesieur-Sebellin,M., Till,M., Khau Van Kien,P., Herve,B.,
            Bourgon,N., Dupont,C., Tabet,A.C., Barrois,M., Coussement,A.,
            Loeuillet,L., Mousty,E., Ea,V., El Assal,A., Mary,L., Jaillard,S.,
            Beneteau,C., Le Vaillant,C., Coutton,C., Devillard,F., Goumy,C.,
            Delabaere,A., Redon,S., Laurent,Y., Lamouroux,A., Massardier,J.,
            Turleau,C., Sanlaville,D., Cantagrel,V., Sonigo,P., Vialard,F.,
            Salomon,L.J. and Malan,V.
  TITLE     Terminal 6q deletions cause brain malformations, a phenotype
            mimicking heterozygous DLL1 pathogenic variants: A multicenter
            retrospective case series
  JOURNAL   Prenat Diagn 42 (1), 118-135 (2022)
   PUBMED   34894355
  REMARK    GeneRIF: Terminal 6q deletions cause brain malformations, a
            phenotype mimicking heterozygous DLL1 pathogenic variants: A
            multicenter retrospective case series.
REFERENCE   6  (residues 1 to 723)
  AUTHORS   Beckers,J., Clark,A., Wunsch,K., Hrabe De Angelis,M. and Gossler,A.
  TITLE     Expression of the mouse Delta1 gene during organogenesis and fetal
            development
  JOURNAL   Mech Dev 84 (1-2), 165-168 (1999)
   PUBMED   10473134
REFERENCE   7  (residues 1 to 723)
  AUTHORS   Gray,G.E., Mann,R.S., Mitsiadis,E., Henrique,D., Carcangiu,M.L.,
            Banks,A., Leiman,J., Ward,D., Ish-Horowitz,D. and
            Artavanis-Tsakonas,S.
  TITLE     Human ligands of the Notch receptor
  JOURNAL   Am J Pathol 154 (3), 785-794 (1999)
   PUBMED   10079256
REFERENCE   8  (residues 1 to 723)
  AUTHORS   Mitsiadis,T.A., Hirsinger,E., Lendahl,U. and Goridis,C.
  TITLE     Delta-notch signaling in odontogenesis: correlation with
            cytodifferentiation and evidence for feedback regulation
  JOURNAL   Dev Biol 204 (2), 420-431 (1998)
   PUBMED   9882480
REFERENCE   9  (residues 1 to 723)
  AUTHORS   Lewis,A.K., Frantz,G.D., Carpenter,D.A., de Sauvage,F.J. and
            Gao,W.Q.
  TITLE     Distinct expression patterns of notch family receptors and ligands
            during development of the mammalian inner ear
  JOURNAL   Mech Dev 78 (1-2), 159-163 (1998)
   PUBMED   9858718
REFERENCE   10 (residues 1 to 723)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL078605.30, DA243552.1,
            DR000029.1 and AY358892.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 26, 2006 this sequence version replaced NP_005609.2.
            
            Summary:  DLL1 is a human homolog of the Notch Delta ligand and is
            a member of the delta/serrate/jagged family.  It plays a role in
            mediating cell fate decisions during hematopoiesis. It may play a
            role in cell-to-cell communication. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358892.1, SRR1803611.188174.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366756.4/ ENSP00000355718.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q27"
     Protein         1..723
                     /product="delta-like protein 1 precursor"
                     /note="delta-like protein 1; H-Delta-1; drosophila Delta
                     homolog 1; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=75881
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2193
     Region          22..177
                     /region_name="MNNL"
                     /note="N terminus of Notch ligand C2-like domain;
                     pfam07657"
                     /db_xref="CDD:462222"
     Region          159..221
                     /region_name="DSL"
                     /note="delta serrate ligand; smart00051"
                     /db_xref="CDD:128366"
     Region          288..326
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(288,291,306)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          329..364
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          <373..403
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          406..440
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          443..478
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(443,446,460)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            477
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00548.2)"
     Region          <489..517
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            546..568
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00548.2)"
     Region          653..702
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00548.2)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB.
                     /evidence=ECO:0000250|UniProtKB:Q61483; propagated from
                     UniProtKB/Swiss-Prot (O00548.2)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61483; propagated from
                     UniProtKB/Swiss-Prot (O00548.2)"
     Region          720..723
                     /region_name="Interaction with MAGI1.
                     /evidence=ECO:0000250|UniProtKB:Q61483"
                     /note="propagated from UniProtKB/Swiss-Prot (O00548.2)"
     CDS             1..723
                     /gene="DLL1"
                     /gene_synonym="Delta; DELTA1; DL1; NEDBAS"
                     /coded_by="NM_005618.4:940..3111"
                     /db_xref="CCDS:CCDS5313.1"
                     /db_xref="GeneID:28514"
                     /db_xref="HGNC:HGNC:2908"
                     /db_xref="MIM:606582"
ORIGIN      
        1 mgsrcalala vlsallcqvw ssgvfelklq efvnkkgllg nrnccrggag pppcacrtff
       61 rvclkhyqas vspeppctyg savtpvlgvd sfslpdggga dsafsnpirf pfgftwpgtf
      121 sliiealhtd spddlatenp erlisrlatq rhltvgeews qdlhssgrtd lkysyrfvcd
      181 ehyygegcsv fcrprddafg hftcgergek vcnpgwkgpy ctepiclpgc deqhgfcdkp
      241 geckcrvgwq grycdeciry pgclhgtcqq pwqcncqegw gglfcnqdln ycthhkpckn
      301 gatctntgqg sytcscrpgy tgatcelgid ecdpspckng gsctdlensy sctcppgfyg
      361 kicelsamtc adgpcfnggr csdspdggys crcpvgysgf ncekkidycs sspcsngakc
      421 vdlgdaylcr cqagfsgrhc ddnvddcass pcanggtcrd gvndfsctcp pgytgrncsa
      481 pvsrcehapc hngatcherg hryvcecarg yggpncqfll pelppgpavv dlteklegqg
      541 gpfpwvavca gvilvlmlll gcaavvvcvr lrlqkhrppa dpcrgetetm nnlancqrek
      601 disvsiigat qikntnkkad fhgdhsadkn gfkarypavd ynlvqdlkgd dtavrdahsk
      661 rdtkcqpqgs sgeekgtptt lrggeaserk rpdsgcstsk dtkyqsvyvi seekdecvia
      721 tev
//
LOCUS       NP_001347528             741 aa            linear   ROD 27-APR-2025
DEFINITION  protein O-mannosyl-transferase TMTC4 [Mus musculus].
ACCESSION   NP_001347528 XP_006519575
VERSION     NP_001347528.1
DBSOURCE    REFSEQ: accession NM_001360599.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Li,J., Choi,B.Y., Eltawil,Y., Ismail Mohamad,N., Park,Y.,
            Matthews,I.R., Han,J.H., Kim,B.J., Sherr,E.H. and Chan,D.K.
  TITLE     TMTC4 is a hair cell-specific human deafness gene
  JOURNAL   JCI Insight 8 (24), e172665 (2023)
   PUBMED   37943620
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Li,J., Akil,O., Rouse,S.L., McLaughlin,C.W., Matthews,I.R.,
            Lustig,L.R., Chan,D.K. and Sherr,E.H.
  TITLE     Deletion of Tmtc4 activates the unfolded protein response and
            causes postnatal hearing loss
  JOURNAL   J Clin Invest 128 (11), 5150-5162 (2018)
   PUBMED   30188326
  REMARK    GeneRIF: mice with homozygous inactivation of both Tmtc4 and Chop
            had less hearing loss than knockout of Tmtc4 alone. This study
            implicated a novel mechanism for hearing impairment, highlighting a
            potential treatment approach for a broad range of human hearing
            loss disorders.
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   5  (residues 1 to 741)
  AUTHORS   Coulpier,F., Le Crom,S., Maro,G.S., Manent,J., Giovannini,M.,
            Maciorowski,Z., Fischer,A., Gessler,M., Charnay,P. and Topilko,P.
  TITLE     Novel features of boundary cap cells revealed by the analysis of
            newly identified molecular markers
  JOURNAL   Glia 57 (13), 1450-1457 (2009)
   PUBMED   19243017
REFERENCE   6  (residues 1 to 741)
  AUTHORS   Pang,A.L., Taylor,H.C., Johnson,W., Alexander,S., Chen,Y., Su,Y.A.,
            Li,X., Ravindranath,N., Dym,M., Rennert,O.M. and Chan,W.Y.
  TITLE     Identification of differentially expressed genes in mouse
            spermatogenesis
  JOURNAL   J Androl 24 (6), 899-911 (2003)
   PUBMED   14581517
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BB852647.1, AK043293.1, AK033947.1 and BX512100.1.
            
            On Feb 8, 2018 this sequence version replaced XP_006519575.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK043293.1, SRR7345562.819230.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 66.04 cM"
     Protein         1..741
                     /product="protein O-mannosyl-transferase TMTC4"
                     /EC_number="2.4.1.109"
                     /note="transmembrane and TPR repeat-containing protein 4;
                     transmembrane O-mannosyltransferase targeting cadherins 4"
                     /calculated_mol_wt=82832
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            111..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            147..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            167..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            199..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            266..286
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          292..366
                     /region_name="TMTC_DUF1736"
                     /note="Protein O-mannosyl-transferase TMTC, DUF1736;
                     pfam08409"
                     /db_xref="CDD:462468"
     Site            355..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            413..433
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            442..462
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          475..681
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          482..515
                     /region_name="TPR 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          482..510
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(483,486..487,490..491,493,517,520..521,524..525,
                     527..528,551,554..555,558..559,562)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          515..545
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          516..549
                     /region_name="TPR 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          550..583
                     /region_name="TPR 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          550..578
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          584..617
                     /region_name="TPR 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          584..610
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            609
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          618..651
                     /region_name="TPR 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          618..646
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          645..>738
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          651..681
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          652..685
                     /region_name="TPR 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          686..719
                     /region_name="TPR 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          686..714
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            725
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8BG19.1)"
     CDS             1..741
                     /gene="Tmtc4"
                     /gene_synonym="4930403J22Rik; 5730419O14Rik"
                     /coded_by="NM_001360599.1:259..2484"
                     /db_xref="CCDS:CCDS27352.1"
                     /db_xref="GeneID:70551"
                     /db_xref="MGI:MGI:1921050"
ORIGIN      
        1 mveldadldh ivpsvlppfw aklvvgfvsl lcfarsydgd fvfddseaiv nnkdlqsdtp
       61 lgdlwhhdfw gsklssntsh ksyrpltvlt frinyylsgg fhpvgfhvvn illhgsisil
      121 mldvfsvlfg glqytgkgqr vhlaprasll atllfavhpv htecvagvvg radllcalff
      181 llsflgycqa fketgnkegt hsstfwvlls iflgavamlc keqgitvlgl navfdilvig
      241 kldilaavrk vlhkdksqen agmfknggll frialltigg tsmlyirwki mgtgppafte
      301 vdnpasfads mlvrainyny yyslnawlll cpwwlcfdws mgcipliksv gdwrvialaa
      361 lwlcliglif qalcsedsck rriltlglgf lvipflpasn lffrvgfvva ervlylpsag
      421 ycvlltfgfg alsrhtkkkk pvaaiilgil linalrcvir sgewrseeql frsalsvcpl
      481 nakvhynigk nladqgnqta aikyyreavr lnpkyvhamn nlgnilkern elqeaeells
      541 lavqiqpdfa aawmnlgivq nslkrfeeae qsyrtaikhr rkypdcyynl grlyadlnrh
      601 vdalnawrna tvlkpehsla wnnmiilldn tgnlaqaeav grealqlipn dhslmfslan
      661 vlgksqkyke sealflkaik anpnvasyhg nlavlyhrwg hldsakkhye islqldpvav
      721 gtkenysllr rkleqtqkkd v
//
LOCUS       NP_001348571             667 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX42 isoform c [Mus musculus].
ACCESSION   NP_001348571
VERSION     NP_001348571.1
DBSOURCE    REFSEQ: accession NM_001361642.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Perez-Garcia,V., Fineberg,E., Wilson,R., Murray,A., Mazzeo,C.I.,
            Tudor,C., Sienerth,A., White,J.K., Tuck,E., Ryder,E.J., Gleeson,D.,
            Siragher,E., Wardle-Jones,H., Staudt,N., Wali,N., Collins,J.,
            Geyer,S., Busch-Nentwich,E.M., Galli,A., Smith,J.C., Robertson,E.,
            Adams,D.J., Weninger,W.J., Mohun,T. and Hemberger,M.
  TITLE     Placentation defects are highly prevalent in embryonic lethal mouse
            mutants
  JOURNAL   Nature 555 (7697), 463-468 (2018)
   PUBMED   29539633
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Nishiguchi,S., Joh,T., Horie,K., Zou,Z., Yasunaga,T. and Shimada,K.
  TITLE     A survey of genes expressed in undifferentiated mouse embryonal
            carcinoma F9 cells: characterization of low-abundance mRNAs
  JOURNAL   J Biochem 116 (1), 128-139 (1994)
   PUBMED   7798170
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL604045.7.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence and lacks two alternate in-frame exons compared to
            variant 1. The resulting isoform (c) is shorter at the N-terminus
            and lacks an alternate internal segment compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.146974.1,
                                           SRR1660813.99054.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849383, SAMN00849384
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 68.89 cM"
     Protein         1..667
                     /product="ATP-dependent RNA helicase DDX42 isoform c"
                     /EC_number="3.6.4.13"
                     /note="RNA helicase-related protein; ATP-dependent RNA
                     helicase DDX42; DEAD box protein 42; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 42"
                     /calculated_mol_wt=72966
     Region          <80..416
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          <382..>627
                     /region_name="dermokine"
                     /note="cl42387"
                     /db_xref="CDD:455732"
     CDS             1..667
                     /gene="Ddx42"
                     /gene_synonym="1810047H21Rik; B430002H05Rik; RHELP; RNAHP;
                     SF3b125"
                     /coded_by="NM_001361642.1:485..2488"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:72047"
                     /db_xref="MGI:MGI:1919297"
ORIGIN      
        1 maenptagvv qeeeednley dsdgnpiaps kkiidplppi dhseidyppf eknfynehee
       61 itnltpqqli dlrhklnlri haeckrfgka ynlrsvavyg ggsmweqaka lqegaeivvc
      121 tpgrlidhvk kkatnlqrvs ylvfdeadrm fdmgfeyqvr siashvrpdr qtllfsatfr
      181 kkieklardi lidpirvvqg digeanedvt qiveilhsgp skwnwltrrl veftssgsvl
      241 lfvtkkanae elasnlkqeg hnlgllhgdm dqsernkvis dfkkkdipvl vatdvaargl
      301 dipsiktvin ydvardidth thrigrtgra gekgvaytll tpkdsnfagd lvrnleganq
      361 hvskelldla mqnawfrksr fkggkgkkln igggglgyre rpglgsensd rgnnnnvmsn
      421 yeaykpstga mgdrltamka afqsqykshf vaaslsnqka gtssagasgw tsagslnsvp
      481 tnsaqqghns pdnpmtsstk nipgfnnsgn issapvtyps igaqgvnnta sgnnsregig
      541 ggngkreryt enrggsrhsh gdggnrhgdg grhgdgyryp esgsrhtdgh rhgetrhggs
      601 agrhgesrga ndgrngesrk egfnrenkmd pkvdssrmdk vdsktdktpd gfavpeppkr
      661 kksrwds
//
LOCUS       NP_116290                 57 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome c oxidase assembly protein COX14 [Homo sapiens].
ACCESSION   NP_116290
VERSION     NP_116290.1
DBSOURCE    REFSEQ: accession NM_032901.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 57)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 57)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 57)
  AUTHORS   Richter-Dennerlein,R., Oeljeklaus,S., Lorenzi,I., Ronsor,C.,
            Bareth,B., Schendzielorz,A.B., Wang,C., Warscheid,B., Rehling,P.
            and Dennerlein,S.
  TITLE     Mitochondrial Protein Synthesis Adapts to Influx of Nuclear-Encoded
            Protein
  JOURNAL   Cell 167 (2), 471-483 (2016)
   PUBMED   27693358
REFERENCE   4  (residues 1 to 57)
  AUTHORS   Lee,S.Y., Kang,M.G., Park,J.S., Lee,G., Ting,A.Y. and Rhee,H.W.
  TITLE     APEX Fingerprinting Reveals the Subcellular Localization of
            Proteins of Interest
  JOURNAL   Cell Rep 15 (8), 1837-1847 (2016)
   PUBMED   27184847
REFERENCE   5  (residues 1 to 57)
  AUTHORS   Ostergaard,E., Weraarpachai,W., Ravn,K., Born,A.P., Jonson,L.,
            Duno,M., Wibrand,F., Shoubridge,E.A. and Vissing,J.
  TITLE     Mutations in COA3 cause isolated complex IV deficiency associated
            with neuropathy, exercise intolerance, obesity, and short stature
  JOURNAL   J Med Genet 52 (3), 203-207 (2015)
   PUBMED   25604084
  REMARK    GeneRIF: COX14 was undetectable in COA3 subject fibroblasts, and
            that COA3 was undetectable in fibroblasts from a COX14 subject,
            demonstrating the interdependence of these two COX assembly factors
REFERENCE   6  (residues 1 to 57)
  AUTHORS   Lai,Y., Yu,Z., Wang,Y. and Ye,J.
  TITLE     Identification of PCAG1 as a novel prostate cancer-associated gene
  JOURNAL   Mol Med Rep 7 (3), 755-760 (2013)
   PUBMED   23292432
  REMARK    GeneRIF: While PCAG1 mRNA was highly expressed in prostate cancer
            tissues, it was almost absent in all common normal tissues and
            paired adjacent normal prostate tissues.
REFERENCE   7  (residues 1 to 57)
  AUTHORS   Szklarczyk,R., Wanschers,B.F., Cuypers,T.D., Esseling,J.J.,
            Riemersma,M., van den Brand,M.A., Gloerich,J., Lasonder,E., van den
            Heuvel,L.P., Nijtmans,L.G. and Huynen,M.A.
  TITLE     Iterative orthology prediction uncovers new mitochondrial proteins
            and identifies C12orf62 as the human ortholog of COX14, a protein
            involved in the assembly of cytochrome c oxidase
  JOURNAL   Genome Biol 13 (2), R12 (2012)
   PUBMED   22356826
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 57)
  AUTHORS   Weraarpachai,W., Sasarman,F., Nishimura,T., Antonicka,H., Aure,K.,
            Rotig,A., Lombes,A. and Shoubridge,E.A.
  TITLE     Mutations in C12orf62, a factor that couples COX I synthesis with
            cytochrome c oxidase assembly, cause fatal neonatal lactic acidosis
  JOURNAL   Am J Hum Genet 90 (1), 142-151 (2012)
   PUBMED   22243966
REFERENCE   9  (residues 1 to 57)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC007849.2 and AI208662.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a small single-pass transmembrane
            protein that localizes to mitochondria. This protein may play a
            role in coordinating the early steps of cytochrome c oxidase (COX;
            also known as complex IV) subunit assembly and, in particular, the
            synthesis and assembly of the COX I subunit of the holoenzyme.
            Mutations in this gene have been associated with mitochondrial
            complex IV deficiency. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) represents the shortest
            transcript. Variants 1-3 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.446910.1, AL697834.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 22356826, 22243966;
                                                  reported by MitoCarta
            MANE Ensembl match                 :: ENST00000550487.6/
                                                  ENSP00000446524.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..57
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..57
                     /product="cytochrome c oxidase assembly protein COX14"
                     /note="COX14 cytochrome c oxidase assembly homolog;
                     cytochrome c oxidase assembly homolog 14; COX14,
                     cytochrome c oxidase assembly factor"
                     /calculated_mol_wt=6468
     Region          1..57
                     /region_name="COX14"
                     /note="Cytochrome oxidase c assembly; pfam14880"
                     /db_xref="CDD:434280"
     Site            15..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96I36.1)"
     CDS             1..57
                     /gene="COX14"
                     /gene_synonym="C12orf62; MC4DN10; PCAG1"
                     /coded_by="NM_032901.4:75..248"
                     /db_xref="CCDS:CCDS8800.1"
                     /db_xref="GeneID:84987"
                     /db_xref="HGNC:HGNC:28216"
                     /db_xref="MIM:614478"
ORIGIN      
        1 mptgkqladi gyktfstsmm lltvyggylc svrvyhyfqw rraqrqaaee qktsgim
//
LOCUS       NP_115955                 85 aa            linear   PRI 27-APR-2025
DEFINITION  serine protease inhibitor Kazal-type 7 precursor [Homo sapiens].
ACCESSION   NP_115955
VERSION     NP_115955.1
DBSOURCE    REFSEQ: accession NM_032566.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Pennacchiotti,G., Valdes-Gutierrez,F., Gonzalez-Arriagada,W.A.,
            Montes,H.F., Parra,J.M.R., Guida,V.A., Gomez,S.E.,
            Guerrero-Gimenez,M.E., Fernandez-Munoz,J.M., Zoppino,F.C.M.,
            Caron,R.W., Ezquer,M.E., Fernandez-Ramires,R. and Bruna,F.A.
  TITLE     SPINK7 expression changes accompanied by HER2, P53 and RB1 can be
            relevant in predicting oral squamous cell carcinoma at a molecular
            level
  JOURNAL   Sci Rep 11 (1), 6939 (2021)
   PUBMED   33767253
  REMARK    GeneRIF: SPINK7 expression changes accompanied by HER2, P53 and RB1
            can be relevant in predicting oral squamous cell carcinoma at a
            molecular level.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Patel,H., Sheikh,M.S. and Huang,Y.
  TITLE     ECRG2, a novel transcriptional target of p53, modulates cancer cell
            sensitivity to DNA damage
  JOURNAL   Cell Death Dis 11 (7), 543 (2020)
   PUBMED   32681017
  REMARK    GeneRIF: ECRG2, a novel transcriptional target of p53, modulates
            cancer cell sensitivity to DNA damage.
            GeneRIF: ECRG2/SPINK7 is a novel pro-apoptotic target of p53, which
            is induced by DNA damage in a p53-dependent manner.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Azouz,N.P., Ynga-Durand,M.A., Caldwell,J.M., Jain,A., Rochman,M.,
            Fischesser,D.M., Ray,L.M., Bedard,M.C., Mingler,M.K., Forney,C.,
            Eilerman,M., Kuhl,J.T., He,H., Biagini Myers,J.M., Mukkada,V.A.,
            Putnam,P.E., Khurana Hershey,G.K., Kottyan,L.C., Wen,T.,
            Martin,L.J. and Rothenberg,M.E.
  TITLE     The antiprotease SPINK7 serves as an inhibitory checkpoint for
            esophageal epithelial inflammatory responses
  JOURNAL   Sci Transl Med 10 (444) (2018)
   PUBMED   29875205
  REMARK    GeneRIF: SPINK7 (serine peptidase inhibitor, kazal type 7), is part
            of the differentiation program of human esophageal epithelium.
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Weber,C., Fischer,J., Redelfs,L., Rademacher,F., Harder,J.,
            Weidinger,S., Wu,Z. and Meyer-Hoffert,U.
  TITLE     The serine protease inhibitor of Kazal-type 7 (SPINK7) is expressed
            in human skin
  JOURNAL   Arch Dermatol Res 309 (9), 767-771 (2017)
   PUBMED   28852849
  REMARK    GeneRIF: n cultured keratinocytes, SPINK7 mRNA expression was
            up-regulated by IL-17A together with IFNgamma
REFERENCE   5  (residues 1 to 85)
  AUTHORS   Hou,X.F., Xu,L.P., Song,H.Y., Li,S., Wu,C. and Wang,J.F.
  TITLE     ECRG2 enhances the anti-cancer effects of cisplatin in
            cisplatin-resistant esophageal cancer cells via upregulation of p53
            and downregulation of PCNA
  JOURNAL   World J Gastroenterol 23 (10), 1796-1803 (2017)
   PUBMED   28348485
  REMARK    GeneRIF: ECRG2 in combination with cisplatin (DDP) can inhibit
            viability and induce apoptosis in esophageal cancer DDP-resistant
            cells, possibly via upregulation of p53 expression and
            downregulation of PCNA expression.
REFERENCE   6  (residues 1 to 85)
  AUTHORS   Kaifi,J.T., Cataldegirmen,G., Wachowiak,R., Schurr,P.G.,
            Kleinhans,H., Kosti,G., Yekebas,E.F., Mann,O., Kutup,A.,
            Kalinin,V., Strate,T. and Izbicki,J.R.
  TITLE     Short tandem repeat polymorphisms of exon 4 in Kazal-type gene
            ECRG2 in pancreatic carcinoma and chronic pancreatitis
  JOURNAL   Anticancer Res 27 (1A), 69-73 (2007)
   PUBMED   17352218
  REMARK    GeneRIF: Observational study of genotype prevalence and
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 85)
  AUTHORS   Yue,C.M., Bi,M.X., Tan,W., Deng,D.J., Zhang,X.Y., Guo,L.P.,
            Lin,D.X. and Lu,S.H.
  TITLE     Short tandem repeat polymorphism in a novel esophageal
            cancer-related gene (ECRG2) implicates susceptibility to esophageal
            cancer in Chinese population
  JOURNAL   Int J Cancer 108 (2), 232-236 (2004)
   PUBMED   14639608
  REMARK    GeneRIF: Short tandem repeat polymorphism in a novel esophageal
            cancer-related gene (ECRG2) implicates susceptibility to esophageal
            cancer
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 85)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 85)
  AUTHORS   Cui,Y.P., Wang,J.B., Zhang,X.Y., Bi,M.X., Guo,L.P. and Lu,S.H.
  TITLE     Using yeast two-hybrid system to identify ECRG2 associated proteins
            and their possible interactions with ECRG2 gene
  JOURNAL   World J Gastroenterol 9 (9), 1892-1896 (2003)
   PUBMED   12970870
  REMARK    GeneRIF: Potential interaction partner for ECRG2 might be involved
            in regulation of cell proliferation and apoptosis and in various
            physiological processes.
REFERENCE   10 (residues 1 to 85)
  AUTHORS   Cui,Y., Wang,J., Zhang,X., Lang,R., Bi,M., Guo,L. and Lu,S.H.
  TITLE     ECRG2, a novel candidate of tumor suppressor gene in the esophageal
            carcinoma, interacts directly with metallothionein 2A and links to
            apoptosis
  JOURNAL   Biochem Biophys Res Commun 302 (4), 904-915 (2003)
   PUBMED   12646258
  REMARK    GeneRIF: Data suggest that the physical interaction of esophageal
            cancer related gene 2 (ECRG2) and metallothionein 2A (MT2A) may
            play an important role in the carcinogenesis of esophageal cancer.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091948.3, AF268198.1 and AY359072.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF268198.1, ERR279835.10253.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274565.5/ ENSP00000274565.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..85
                     /product="serine protease inhibitor Kazal-type 7
                     precursor"
                     /note="esophagus cancer-related gene-2; serine protease
                     inhibitor Kazal-type 7; ECRG-2; esophagus cancer-related
                     gene 2 protein; serine peptidase inhibitor, Kazal type 7
                     (putative)"
                     /calculated_mol_wt=7201
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P58062.1)"
                     /calculated_mol_wt=2049
     mat_peptide     20..85
                     /product="Serine protease inhibitor Kazal-type 7.
                     /id=PRO_0000016565"
                     /note="propagated from UniProtKB/Swiss-Prot (P58062.1)"
                     /calculated_mol_wt=7201
     Region          41..85
                     /region_name="KAZAL_PSTI"
                     /note="Kazal-type pancreatic secretory trypsin inhibitors
                     (PSTI) and related proteins, including the second domain
                     of the ovomucoid turkey inhibitor and the C-terminal
                     domain of the esophagus cancer-related gene-2 protein
                     (ECRG-2), are members of the...; cd01327"
                     /db_xref="CDD:238648"
     Site            47..48
                     /site_type="active"
                     /note="protease cleavage site [active]"
                     /db_xref="CDD:238648"
     Site            47..48
                     /site_type="other"
                     /note="Reactive bond.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00798; propagated
                     from UniProtKB/Swiss-Prot (P58062.1)"
     Site            47
                     /site_type="active"
                     /note="protease interaction site [active]"
                     /db_xref="CDD:238648"
     CDS             1..85
                     /gene="SPINK7"
                     /gene_synonym="ECG2; ECRG2"
                     /coded_by="NM_032566.3:62..319"
                     /db_xref="CCDS:CCDS4289.1"
                     /db_xref="GeneID:84651"
                     /db_xref="HGNC:HGNC:24643"
                     /db_xref="MIM:617288"
ORIGIN      
        1 mkitggllll ctvvyfcsss eaaslspkkv dcsiykkypv vaipcpityl pvcgsdyity
       61 gnechlctes lksngrvqfl hdgsc
//
LOCUS       NP_079088                145 aa            linear   PRI 27-APR-2025
DEFINITION  brain and acute leukemia cytoplasmic protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_079088
VERSION     NP_079088.1
DBSOURCE    REFSEQ: accession NM_024812.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Verma,D., Kumar,R., Ali,M.S., Singh,J., Arora,M., Singh,I.,
            Kumari,S., Bakhshi,S., Sharma,A., Palanichamy,J.K., Tanwar,P.,
            Singh,A.R. and Chopra,A.
  TITLE     BAALC gene expression tells a serious patient outcome tale in
            NPM1-wild type/FLT3-ITD negative cytogenetically normal-acute
            myeloid leukemia in adults
  JOURNAL   Blood Cells Mol Dis 95, 102662 (2022)
   PUBMED   35429905
  REMARK    GeneRIF: BAALC gene expression tells a serious patient outcome tale
            in NPM1-wild type/FLT3-ITD negative cytogenetically normal-acute
            myeloid leukemia in adults.
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Marjanovic,I., Karan-Djurasevic,T., Kostic,T., Virijevic,M.,
            Vukovic,N.S., Pavlovic,S. and Tosic,N.
  TITLE     Prognostic significance of combined BAALC and MN1 gene expression
            level in acute myeloid leukemia with normal karyotype
  JOURNAL   Int J Lab Hematol 43 (3), 433-440 (2021)
   PUBMED   33242229
  REMARK    GeneRIF: Prognostic significance of combined BAALC and MN1 gene
            expression level in acute myeloid leukemia with normal karyotype.
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Dannenmann,B., Klimiankou,M., Oswald,B., Solovyeva,A., Mardan,J.,
            Nasri,M., Ritter,M., Zahabi,A., Arreba-Tutusaus,P., Mir,P.,
            Stein,F., Kandabarau,S., Lachmann,N., Moritz,T., Morishima,T.,
            Konantz,M., Lengerke,C., Ripperger,T., Steinemann,D., Erlacher,M.,
            Niemeyer,C.M., Zeidler,C., Welte,K. and Skokowa,J.
  TITLE     iPSC modeling of stage-specific leukemogenesis reveals BAALC as a
            key oncogene in severe congenital neutropenia
  JOURNAL   Cell Stem Cell 28 (5), 906-922 (2021)
   PUBMED   33894142
  REMARK    GeneRIF: iPSC modeling of stage-specific leukemogenesis reveals
            BAALC as a key oncogene in severe congenital neutropenia.
            Erratum:[Cell Stem Cell. 2023 Sep 7;30(9):1282. doi:
            10.1016/j.stem.2023.07.015. PMID: 37683606]
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Maki,H., Yoshimi,A., Shimada,T., Arai,S., Morita,K., Kamikubo,Y.,
            Ikegawa,M. and Kurokawa,M.
  TITLE     Physical interaction between BAALC and DBN1 induces chemoresistance
            in leukemia
  JOURNAL   Exp Hematol 94, 31-36 (2021)
   PUBMED   33453340
  REMARK    GeneRIF: Physical interaction between BAALC and DBN1 induces
            chemoresistance in leukemia.
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Jentzsch,M., Bill,M., Grimm,J., Brauer,D., Backhaus,D.,
            Goldmann,K., Schulz,J., Niederwieser,D., Platzbecker,U. and
            Schwind,S.
  TITLE     Allogeneic stem cell transplantation mitigates the adverse
            prognostic impact of high diagnostic BAALC and MN1 expression in
            AML
  JOURNAL   Ann Hematol 99 (10), 2417-2427 (2020)
   PUBMED   32862286
  REMARK    GeneRIF: Allogeneic stem cell transplantation mitigates the adverse
            prognostic impact of high diagnostic BAALC and MN1 expression in
            AML.
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Langer,C., Radmacher,M.D., Ruppert,A.S., Whitman,S.P., Paschka,P.,
            Mrozek,K., Baldus,C.D., Vukosavljevic,T., Liu,C.G., Ross,M.E.,
            Powell,B.L., de la Chapelle,A., Kolitz,J.E., Larson,R.A.,
            Marcucci,G. and Bloomfield,C.D.
  CONSRTM   Cancer and Leukemia Group B (CALGB)
  TITLE     High BAALC expression associates with other molecular prognostic
            markers, poor outcome, and a distinct gene-expression signature in
            cytogenetically normal patients younger than 60 years with acute
            myeloid leukemia: a Cancer and Leukemia Group B (CALGB) study
  JOURNAL   Blood 111 (11), 5371-5379 (2008)
   PUBMED   18378853
  REMARK    GeneRIF: high BAALC expression is an independent adverse prognostic
            factor and is associated with a specific gene-expression profile
REFERENCE   7  (residues 1 to 145)
  AUTHORS   Baldus,C.D., Martus,P., Burmeister,T., Schwartz,S., Gokbuget,N.,
            Bloomfield,C.D., Hoelzer,D., Thiel,E. and Hofmann,W.K.
  TITLE     Low ERG and BAALC expression identifies a new subgroup of adult
            acute T-lymphoblastic leukemia with a highly favorable outcome
  JOURNAL   J Clin Oncol 25 (24), 3739-3745 (2007)
   PUBMED   17646667
  REMARK    GeneRIF: Low expression of both ERG and BAALC identifies T-ALL
            patients with a distinctly favorable long-term outcome.
REFERENCE   8  (residues 1 to 145)
  AUTHORS   Satoskar,A.A., Tanner,S.M., Weinstein,M., Qualman,S.J. and de la
            Chapelle,A.
  TITLE     Baalc, a marker of mesoderm and muscle
  JOURNAL   Gene Expr Patterns 5 (4), 463-473 (2005)
   PUBMED   15749074
  REMARK    GeneRIF: High transcript levels occur in leukemic blasts from some
            patients with acute myeloid leukemia.
REFERENCE   9  (residues 1 to 145)
  AUTHORS   Marcucci,G., Mrozek,K. and Bloomfield,C.D.
  TITLE     Molecular heterogeneity and prognostic biomarkers in adults with
            acute myeloid leukemia and normal cytogenetics
  JOURNAL   Curr Opin Hematol 12 (1), 68-75 (2005)
   PUBMED   15604894
  REMARK    GeneRIF: The BAALC gene, located on chromosome 8q22.3, encodes a
            protein with no homology to any known proteins or functional
            domains.
            Review article
REFERENCE   10 (residues 1 to 145)
  AUTHORS   Tanner,S.M., Austin,J.L., Leone,G., Rush,L.J., Plass,C.,
            Heinonen,K., Mrozek,K., Sill,H., Knuutila,S., Kolitz,J.E.,
            Archer,K.J., Caligiuri,M.A., Bloomfield,C.D. and de La Chapelle,A.
  TITLE     BAALC, the human member of a novel mammalian neuroectoderm gene
            lineage, is implicated in hematopoiesis and acute leukemia
  JOURNAL   Proc Natl Acad Sci U S A 98 (24), 13901-13906 (2001)
   PUBMED   11707601
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI548687.1, AK022077.1 and
            BC035038.2.
            
            Summary: This gene was identified by gene expression studies in
            patients with acute myeloid leukemia (AML). The gene is conserved
            among mammals and is not found in lower organisms. Tissues that
            express this gene develop from the neuroectoderm. Multiple
            alternatively spliced transcript variants that encode different
            proteins have been described for this gene; however, some of the
            transcript variants are found only in AML cell lines. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and it encodes the longer protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP213551.1, AK022077.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309982.10/ ENSP00000312457.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..145
                     /product="brain and acute leukemia cytoplasmic protein
                     isoform 1"
                     /note="brain and acute leukemia cytoplasmic protein; brain
                     and acute leukemia, cytoplasmic; BAALC, MEKK1 and KLF4
                     binding; BAALC, MAP3K1 and KLF4 binding"
                     /calculated_mol_wt=15420
     Region          1..50
                     /region_name="BAALC_N"
                     /note="BAALC N-terminus; pfam06989"
                     /db_xref="CDD:369161"
     Region          3..35
                     /region_name="Interaction with CAMK2A.
                     /evidence=ECO:0000250|UniProtKB:Q920K5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXS3.4)"
     Region          27..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXS3.4)"
     CDS             1..145
                     /gene="BAALC"
                     /coded_by="NM_024812.3:174..611"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6297.1"
                     /db_xref="GeneID:79870"
                     /db_xref="HGNC:HGNC:14333"
                     /db_xref="MIM:606602"
ORIGIN      
        1 mgcggsrada iepryyeswt retestwlty tdsdappsaa apdsgpeagg lhsgmledgl
       61 psngvprsta pggipnpekk tncetqcpnp qslssgpltq kqnglqttea krdakrmpak
      121 evtinvtdsi qqmdrsrrit kncvn
//
LOCUS       NP_060594                774 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RFWD3 isoform 1 [Homo sapiens].
ACCESSION   NP_060594
VERSION     NP_060594.3
DBSOURCE    REFSEQ: accession NM_018124.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Moore,C.E., Yalcindag,S.E., Czeladko,H., Ravindranathan,R.,
            Wijesekara Hanthi,Y., Levy,J.C., Sannino,V., Schindler,D.,
            Ciccia,A., Costanzo,V. and Elia,A.E.H.
  TITLE     RFWD3 promotes ZRANB3 recruitment to regulate the remodeling of
            stalled replication forks
  JOURNAL   J Cell Biol 222 (5) (2023)
   PUBMED   37036693
  REMARK    GeneRIF: RFWD3 promotes ZRANB3 recruitment to regulate the
            remodeling of stalled replication forks.
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Zhu,Y., Peng,X., Wang,X., Ying,P., Wang,H., Li,B., Li,Y., Zhang,M.,
            Cai,Y., Lu,Z., Niu,S., Yang,N., Zhong,R., Tian,J., Chang,J. and
            Miao,X.
  TITLE     Systematic analysis on expression quantitative trait loci
            identifies a novel regulatory variant in ring finger and WD repeat
            domain 3 associated with prognosis of pancreatic cancer
  JOURNAL   Chin Med J (Engl) 135 (11), 1348-1357 (2022)
   PUBMED   35830250
  REMARK    GeneRIF: Systematic analysis on expression quantitative trait loci
            identifies a novel regulatory variant in ring finger and WD repeat
            domain 3 associated with prognosis of pancreatic cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Gallina,I., Hendriks,I.A., Hoffmann,S., Larsen,N.B., Johansen,J.,
            Colding-Christensen,C.S., Schubert,L., Selles-Baiget,S., Fabian,Z.,
            Kuhbacher,U., Gao,A.O., Raschle,M., Rasmussen,S., Nielsen,M.L.,
            Mailand,N. and Duxin,J.P.
  TITLE     The ubiquitin ligase RFWD3 is required for translesion DNA
            synthesis
  JOURNAL   Mol Cell 81 (3), 442-458 (2021)
   PUBMED   33321094
  REMARK    GeneRIF: The ubiquitin ligase RFWD3 is required for translesion DNA
            synthesis.
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Hsu,R.Y.C., Giri,S., Wang,Y., Lin,Y.C., Liu,D., Wopat,S.,
            Chakraborty,A., Prasanth,K.V. and Prasanth,S.G.
  TITLE     The E3 ligase RFWD3 stabilizes ORC in a p53-dependent manner
  JOURNAL   Cell Cycle 19 (21), 2927-2938 (2020)
   PUBMED   33044890
  REMARK    GeneRIF: The E3 ligase RFWD3 stabilizes ORC in a p53-dependent
            manner.
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Jia,J., Yang,Y., Yan,T., Chen,T. and Lu,G.
  TITLE     Down-regulation of RFWD3 inhibits cancer cells proliferation and
            migration in gastric carcinoma
  JOURNAL   Gen Physiol Biophys 39 (4), 363-371 (2020)
   PUBMED   32902405
  REMARK    GeneRIF: Down-regulation of RFWD3 inhibits cancer cells
            proliferation and migration in gastric carcinoma.
REFERENCE   6  (residues 1 to 774)
  AUTHORS   Dastani,Z., Pajukanta,P., Marcil,M., Rudzicz,N., Ruel,I.,
            Bailey,S.D., Lee,J.C., Lemire,M., Faith,J., Platko,J., Rioux,J.,
            Hudson,T.J., Gaudet,D., Engert,J.C. and Genest,J.
  TITLE     Fine mapping and association studies of a high-density lipoprotein
            cholesterol linkage region on chromosome 16 in French-Canadian
            subjects
  JOURNAL   Eur J Hum Genet 18 (3), 342-347 (2010)
   PUBMED   19844255
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 774)
  AUTHORS   Markson,G., Kiel,C., Hyde,R., Brown,S., Charalabous,P., Bremm,A.,
            Semple,J., Woodsmith,J., Duley,S., Salehi-Ashtiani,K., Vidal,M.,
            Komander,D., Serrano,L., Lehner,P. and Sanderson,C.M.
  TITLE     Analysis of the human E2 ubiquitin conjugating enzyme protein
            interaction network
  JOURNAL   Genome Res 19 (10), 1905-1911 (2009)
   PUBMED   19549727
REFERENCE   8  (residues 1 to 774)
  AUTHORS   van Wijk,S.J., de Vries,S.J., Kemmeren,P., Huang,A., Boelens,R.,
            Bonvin,A.M. and Timmers,H.T.
  TITLE     A comprehensive framework of E2-RING E3 interactions of the human
            ubiquitin-proteasome system
  JOURNAL   Mol Syst Biol 5, 295 (2009)
   PUBMED   19690564
  REMARK    Erratum:[Mol Syst Biol. 2009;5:317]
REFERENCE   9  (residues 1 to 774)
  AUTHORS   Tsuritani,K., Irie,T., Yamashita,R., Sakakibara,Y., Wakaguri,H.,
            Kanai,A., Mizushima-Sugano,J., Sugano,S., Nakai,K. and Suzuki,Y.
  TITLE     Distinct class of putative 'non-conserved' promoters in humans:
            comparative studies of alternative promoters of human and mouse
            genes
  JOURNAL   Genome Res 17 (7), 1005-1014 (2007)
   PUBMED   17567985
REFERENCE   10 (residues 1 to 774)
  AUTHORS   Mehta,P.A. and Ebens,C.
  TITLE     Fanconi Anemia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP872110.1, BC059371.1, BC002574.2 and BM467919.1.
            
            On Jul 26, 2005 this sequence version replaced NP_060594.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.21672.1,
                                           SRR1660805.195981.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361070.9/ ENSP00000354361.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..774
                     /product="E3 ubiquitin-protein ligase RFWD3 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="RING finger and WD repeat domain-containing protein
                     3; E3 ubiquitin-protein ligase RFWD3; RING finger protein
                     201; RING-type E3 ubiquitin transferase RFWD3"
                     /calculated_mol_wt=84963
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM and ATR.
                     /evidence=ECO:0000269|PubMed:20173098,
                     ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28575658;
                     propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM and ATR.
                     /evidence=ECO:0000269|PubMed:20173098,
                     ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28575658;
                     propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          95..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          139..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          257..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          283..343
                     /region_name="mRING-C3HGC3_RFWD3"
                     /note="Modified RING finger, C3HGC3-type, found in RING
                     finger and WD repeat domain-containing protein 3 (RFWD3)
                     and similar proteins; cd16450"
                     /db_xref="CDD:438114"
     Region          495..537
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          496..762
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          500..537
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          539..577
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          543..580
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          583..628
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          588..655
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..774
                     /gene="RFWD3"
                     /gene_synonym="FANCW; RNF201"
                     /coded_by="NM_018124.4:95..2419"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32486.1"
                     /db_xref="GeneID:55159"
                     /db_xref="HGNC:HGNC:25539"
                     /db_xref="MIM:614151"
ORIGIN      
        1 maheameydv qvqlnhaeqq papagmassq ggpallqpvp advvssqgvp silqpapaev
       61 issqatppll qpapqlsvdl tevevlgedt veninprtse qhrqgsdgnh tipasslhsm
      121 tnfisglqrl hgmleflrps ssnhsvgpmr trrrvsasrr araggsqrtd sarlraplda
      181 yfqvsrtqpd lpattydset rnpvseelqv ssssdsdsds saeyggvvdq aeesgavile
      241 eqlagvsaeq evtcidggkt lpkqpspqks epllpsasmd eeegdtctic leqwtnagdh
      301 rlsalrcghl fgyrcistwl kgqvrkcpqc nkkarhsdiv vlyartlral dtseqermks
      361 sllkeqmlrk qaelesaqcr lqlqvltdkc trlqrrvqdl qkltshqsqn lqqprgsqaw
      421 vlscspssqg qhkhkyhfqk tftvsqagnc rimaycdals clvisqpspq asflpgfgvk
      481 mlstanmkss qyipmhgkqi rglafssylr glllsasldn tikltsletn tvvqtynagr
      541 pvwsccwcld eanyiyagla ngsilvydvr ntsshvqelv aqkarcplvs lsympraasa
      601 afpyggvlag tledasfweq kmdfshwphv lplepggcid fqtenssrhc lvtyrpdknh
      661 ttirsvlmem syrlddtgnp icscqpvhtf fggptckllt knaifqspen dgnilvctgd
      721 eaansallwd aasgsllqdl qtdqpvldic pfevnrnsyl atltekmvhi ykwe
//
LOCUS       NP_001036162             140 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger SWIM domain-containing protein 7 [Homo sapiens].
ACCESSION   NP_001036162
VERSION     NP_001036162.1
DBSOURCE    REFSEQ: accession NM_001042697.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Hengel,S.R., Oppenheimer,K.G., Smith,C.M., Schaich,M.A., Rein,H.L.,
            Martino,J., Darrah,K.E., Witham,M., Ezekwenna,O.C., Burton,K.R.,
            Van Houten,B., Spies,M. and Bernstein,K.A.
  TITLE     The human Shu complex promotes RAD51 activity by modulating RPA
            dynamics on ssDNA
  JOURNAL   Nat Commun 15 (1), 7197 (2024)
   PUBMED   39169038
  REMARK    GeneRIF: The human Shu complex promotes RAD51 activity by
            modulating RPA dynamics on ssDNA.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Hussain,S., Nawaz,S., Khan,I., Khan,N., Hussain,S., Ullah,I.,
            Fakhro,K.A. and Ahmad,W.
  TITLE     A novel homozygous variant in homologous recombination repair gene
            ZSWIM7 causes azoospermia in males and primary ovarian
            insufficiency in females
  JOURNAL   Eur J Med Genet 65 (11), 104629 (2022)
   PUBMED   36202298
  REMARK    GeneRIF: A novel homozygous variant in homologous recombination
            repair gene ZSWIM7 causes azoospermia in males and primary ovarian
            insufficiency in females.
            Review article
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Yatsenko,S.A., Gurbuz,F., Topaloglu,A.K., Berman,A.J., Martin,P.M.,
            Rodrigue-Escriba,M., Qin,Y. and Rajkovic,A.
  TITLE     Pathogenic Variants in ZSWIM7 Cause Primary Ovarian Insufficiency
  JOURNAL   J Clin Endocrinol Metab 107 (6), e2359-e2364 (2022)
   PUBMED   35218660
  REMARK    GeneRIF: Pathogenic Variants in ZSWIM7 Cause Primary Ovarian
            Insufficiency.
            Erratum:[J Clin Endocrinol Metab. 2022 Aug 18;107(9):e3969. doi:
            10.1210/clinem/dgac345. PMID: 35689663]
REFERENCE   4  (residues 1 to 140)
  AUTHORS   McGlacken-Byrne,S.M., Le Quesne Stabej,P., Del Valle,I., Ocaka,L.,
            Gagunashvili,A., Crespo,B., Moreno,N., James,C., Bacchelli,C.,
            Dattani,M.T., Williams,H.J., Kelberman,D., Achermann,J.C. and
            Conway,G.S.
  TITLE     ZSWIM7 Is Associated With Human Female Meiosis and Familial Primary
            Ovarian Insufficiency
  JOURNAL   J Clin Endocrinol Metab 107 (1), e254-e263 (2022)
   PUBMED   34402903
  REMARK    GeneRIF: ZSWIM7 Is Associated With Human Female Meiosis and
            Familial Primary Ovarian Insufficiency.
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Sung,Y.J., de las Fuentes,L., Schwander,K.L., Simino,J. and
            Rao,D.C.
  TITLE     Gene-smoking interactions identify several novel blood pressure
            loci in the Framingham Heart Study
  JOURNAL   Am J Hypertens 28 (3), 343-354 (2015)
   PUBMED   25189868
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Martin,V., Chahwan,C., Gao,H., Blais,V., Wohlschlegel,J.,
            Yates,J.R. 3rd, McGowan,C.H. and Russell,P.
  TITLE     Sws1 is a conserved regulator of homologous recombination in
            eukaryotic cells
  JOURNAL   EMBO J 25 (11), 2564-2574 (2006)
   PUBMED   16710300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006251.3, BU075283.1 and DQ530600.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA593990.1, SRR1660803.219346.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399277.6/ ENSP00000382218.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..140
                     /product="zinc finger SWIM domain-containing protein 7"
                     /note="SWIM domain-containing and Srs2-interacting protein
                     1 homolog; SWIM-type zinc finger domain-containing protein
                     7"
                     /calculated_mol_wt=15255
     Region          23..133
                     /region_name="COG5431"
                     /note="Predicted nucleic acid-binding protein, contains
                     SWIM-type Zn-finger domain [General function prediction
                     only]"
                     /db_xref="CDD:444183"
     CDS             1..140
                     /gene="ZSWIM7"
                     /gene_synonym="ODG10; SPGF71; SWS1"
                     /coded_by="NM_001042697.2:111..533"
                     /db_xref="CCDS:CCDS42266.1"
                     /db_xref="GeneID:125150"
                     /db_xref="HGNC:HGNC:26993"
                     /db_xref="MIM:614535"
ORIGIN      
        1 mavvlpavve ellsemaaav qesaripdey llslkflfgs satqaldlvd rqsitlissp
       61 sgrrvyqvlg sssktytcla schycscpaf afsvlrksds ilckhllavy lsqvmrtcqq
      121 lsvsdkqltd illmekkqea
//
LOCUS       NP_001390                391 aa            linear   PRI 27-APR-2025
DEFINITION  ectodysplasin-A isoform 1 [Homo sapiens].
ACCESSION   NP_001390
VERSION     NP_001390.1
DBSOURCE    REFSEQ: accession NM_001399.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Agiannitopoulos,K., Potska,K., Douka,A., Gintoni,I., Tsaousis,G.N.,
            Papadopoulou,E., Nasioulas,G. and Yapijakis,C.
  TITLE     A novel deletion of exon 4 in the Ectodysplasin A gene associated
            with X-linked hypohidrotic ectodermal dysplasia
  JOURNAL   Arch Oral Biol 150, 105689 (2023)
   PUBMED   37001412
  REMARK    GeneRIF: A novel deletion of exon 4 in the Ectodysplasin A gene
            associated with X-linked hypohidrotic ectodermal dysplasia.
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Deng,X., Guo,C., Qin,H., Zhao,L., Li,Y., Zhao,Z., Li,H., Yang,L.,
            Wang,D. and Yuan,G.
  TITLE     Association between Circulating Ectodysplasin A and Diabetic Kidney
            Disease
  JOURNAL   J Diabetes Res 2023, 5087761 (2023)
   PUBMED   37091044
  REMARK    GeneRIF: Association between Circulating Ectodysplasin A and
            Diabetic Kidney Disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Elomaa,O., Pulkkinen,K., Hannelius,U., Mikkola,M.,
            Saarialho-Kere,U. and Kere,J.
  TITLE     Ectodysplasin is released by proteolytic shedding and binds to the
            EDAR protein
  JOURNAL   Hum Mol Genet 10 (9), 953-962 (2001)
   PUBMED   11309369
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Bayes,M., Hartung,A.J., Ezer,S., Pispa,J., Thesleff,I.,
            Srivastava,A.K. and Kere,J.
  TITLE     The anhidrotic ectodermal dysplasia gene (EDA) undergoes
            alternative splicing and encodes ectodysplasin-A with deletion
            mutations in collagenous repeats
  JOURNAL   Hum Mol Genet 7 (11), 1661-1669 (1998)
   PUBMED   9736768
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Monreal,A.W., Zonana,J. and Ferguson,B.
  TITLE     Identification of a new splice form of the EDA1 gene permits
            detection of nearly all X-linked hypohidrotic ectodermal dysplasia
            mutations
  JOURNAL   Am J Hum Genet 63 (2), 380-389 (1998)
   PUBMED   9683615
  REMARK    Erratum:[Am J Hum Genet 1998 Oct;63(4):1253-5]
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Montonen,O., Ezer,S., Saarialho-Kere,U.K., Herva,R.,
            Karjalainen-Lindsberg,M.L., Kaitila,I., Schlessinger,D.,
            Srivastava,A.K., Thesleff,I. and Kere,J.
  TITLE     The gene defective in anhidrotic ectodermal dysplasia is expressed
            in the developing epithelium, neuroectoderm, thymus, and bone
  JOURNAL   J Histochem Cytochem 46 (3), 281-289 (1998)
   PUBMED   9487109
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Ferguson,B.M., Thomas,N.S., Munoz,F., Morgan,D., Clarke,A. and
            Zonana,J.
  TITLE     Scarcity of mutations detected in families with X linked
            hypohidrotic ectodermal dysplasia: diagnostic implications
  JOURNAL   J Med Genet 35 (2), 112-115 (1998)
   PUBMED   9507389
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Kere,J., Srivastava,A.K., Montonen,O., Zonana,J., Thomas,N.,
            Ferguson,B., Munoz,F., Morgan,D., Clarke,A., Baybayan,P.,
            Chen,E.Y., Ezer,S., Saarialho-Kere,U., de la Chapelle,A. and
            Schlessinger,D.
  TITLE     X-linked anhidrotic (hypohidrotic) ectodermal dysplasia is caused
            by mutation in a novel transmembrane protein
  JOURNAL   Nat Genet 13 (4), 409-416 (1996)
   PUBMED   8696334
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Srivastava,A.K., Montonen,O., Saarialho-Kere,U., Chen,E.,
            Baybayan,P., Pispa,J., Limon,J., Schlessinger,D. and Kere,J.
  TITLE     Fine mapping of the EDA gene: a translocation breakpoint is
            associated with a CpG island that is transcribed
  JOURNAL   Am J Hum Genet 58 (1), 126-132 (1996)
   PUBMED   8554048
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Wright,J.T., Grange,D.K. and Fete,M.
  TITLE     Hypohidrotic Ectodermal Dysplasia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301291
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF040628.1, BC126143.1,
            AL158141.14 and BQ008767.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a type II membrane
            protein that can be cleaved by furin to produce a secreted form.
            The encoded protein, which belongs to the tumor necrosis factor
            family, acts as a homotrimer and may be involved in cell-cell
            signaling during the development of ectodermal organs. Defects in
            this gene are a cause of ectodermal dysplasia, anhidrotic, which is
            also known as X-linked hypohidrotic ectodermal dysplasia. Several
            transcript variants encoding many different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1, also known as
            EDA-A1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF040628.1, AF060999.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155371, SAMEA2159607
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374552.9/ ENSP00000363680.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..391
                     /product="ectodysplasin-A isoform 1"
                     /note="oligodontia 1; X-linked anhidroitic ectodermal
                     dysplasia protein; tumor necrosis factor ligand 7C"
                     /calculated_mol_wt=41163
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92838.2)"
     Region          73..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92838.2)"
     Region          146..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92838.2)"
     Site            159..160
                     /site_type="cleavage"
                     /note="Cleavage, by furin.
                     /evidence=ECO:0000269|PubMed:11416205; propagated from
                     UniProtKB/Swiss-Prot (Q92838.2)"
     mat_peptide     160..391
                     /product="Ectodysplasin-A, secreted form.
                     /evidence=ECO:0000305|PubMed:11416205. /id=PRO_0000034539"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92838.2)"
                     /calculated_mol_wt=24189
     Region          249..383
                     /region_name="TNF"
                     /note="Tumor Necrosis Factor; TNF superfamily members
                     include the cytokines: TNF (TNF-alpha), LT
                     (lymphotoxin-alpha, TNF-beta), CD40 ligand, Apo2L (TRAIL),
                     Fas ligand, and osteoprotegerin (OPG) ligand. These
                     proteins generally have an intracellular N-terminal...;
                     cl00147"
                     /db_xref="CDD:444713"
     Site            order(252,302,304,347,352,379,383)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238108"
     Site            order(275,277,319,326,328)
                     /site_type="active"
                     /note="receptor binding sites [active]"
                     /db_xref="CDD:238108"
     Site            313
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92838.2)"
     Site            372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92838.2)"
     CDS             1..391
                     /gene="EDA"
                     /gene_synonym="ECTD1; ED1; ED1-A1; ED1-A2; EDA-A1; EDA-A2;
                     EDA1; EDA2; HED; HED1; ODT1; STHAGX1; TNLG7C; XHED; XLHED"
                     /coded_by="NM_001399.5:197..1372"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14394.1"
                     /db_xref="GeneID:1896"
                     /db_xref="HGNC:HGNC:3157"
                     /db_xref="MIM:300451"
ORIGIN      
        1 mgypeverre llpaaaprer gsqgcgcgga paragegnsc llflgffgls lalhlltlcc
       61 ylelrselrr ergaesrlgg sgtpgtsgtl sslggldpds pitshlgqps pkqqplepge
      121 aalhsdsqdg hqmallnfff pdekpyseee srrvrrnkrs ksnegadgpv knkkkgkkag
      181 ppgpngppgp pgppgpqgpp gipgipgipg ttvmgppgpp gppgpqgppg lqgpsgaadk
      241 agtrenqpav vhlqgqgsai qvkndlsggv lndwsritmn pkvfklhprs gelevlvdgt
      301 yfiysqvevy yinftdfasy evvvdekpfl qctrsietgk tnyntcytag vcllkarqki
      361 avkmvhadis inmskhttff gairlgeapa s
//
LOCUS       NP_068780                426 aa            linear   PRI 27-APR-2025
DEFINITION  transcriptional enhancer factor TEF-1 [Homo sapiens].
ACCESSION   NP_068780 XP_933107 XP_945859
VERSION     NP_068780.2
DBSOURCE    REFSEQ: accession NM_021961.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Chen,J., Li,L., Feng,Y., Zhao,Y., Sun,F., Zhou,X., Yiqi,D., Li,Z.,
            Kong,F. and Kong,X.
  TITLE     MKLN1-AS promotes pancreatic cancer progression as a crucial
            downstream mediator of HIF-1alpha through miR-185-5p/TEAD1 pathway
  JOURNAL   Cell Biol Toxicol 40 (1), 30 (2024)
   PUBMED   38740637
  REMARK    GeneRIF: MKLN1-AS promotes pancreatic cancer progression as a
            crucial downstream mediator of HIF-1alpha through miR-185-5p/TEAD1
            pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Isaac,R., Bandyopadhyay,G., Rohm,T.V., Kang,S., Wang,J.,
            Pokhrel,N., Sakane,S., Zapata,R., Libster,A.M., Vinik,Y.,
            Berhan,A., Kisseleva,T., Borok,Z., Zick,Y., Telese,F.,
            Webster,N.J.G. and Olefsky,J.M.
  TITLE     TM7SF3 controls TEAD1 splicing to prevent MASH-induced liver
            fibrosis
  JOURNAL   Cell Metab 36 (5), 1030-1043 (2024)
   PUBMED   38670107
  REMARK    GeneRIF: TM7SF3 controls TEAD1 splicing to prevent MASH-induced
            liver fibrosis.
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Ju,J., Zhang,H., Lin,M., Yan,Z., An,L., Cao,Z., Geng,D., Yue,J.,
            Tang,Y., Tian,L., Chen,F., Han,Y., Wang,W., Zhao,S., Jiao,S. and
            Zhou,Z.
  TITLE     The alanyl-tRNA synthetase AARS1 moonlights as a lactyltransferase
            to promote YAP signaling in gastric cancer
  JOURNAL   J Clin Invest 134 (10), e174587 (2024)
   PUBMED   38512451
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Shi,X., Dang,X., Huang,Z., Lu,Y., Tong,H., Liang,F., Zhuang,F.,
            Li,Y., Cai,Z., Huo,H., Jiang,Z., Pan,C., Wang,X., Gu,C. and He,B.
  TITLE     SUMOylation of TEAD1 Modulates the Mechanism of Pathological
            Cardiac Hypertrophy
  JOURNAL   Adv Sci (Weinh) 11 (12), e2305677 (2024)
   PUBMED   38225750
  REMARK    GeneRIF: SUMOylation of TEAD1 Modulates the Mechanism of
            Pathological Cardiac Hypertrophy.
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Yoshii,H., Kajiya,M., Yoshino,M., Morimoto,S., Horikoshi,S.,
            Tari,M., Motoike,S., Iwata,T., Ouhara,K., Ando,T., Yoshimoto,T.,
            Shintani,T. and Mizuno,N.
  TITLE     Mechanosignaling YAP/TAZ-TEAD Axis Regulates the Immunomodulatory
            Properties of Mesenchymal Stem Cells
  JOURNAL   Stem Cell Rev Rep 20 (1), 347-361 (2024)
   PUBMED   37917410
  REMARK    GeneRIF: Mechanosignaling YAP/TAZ-TEAD Axis Regulates the
            Immunomodulatory Properties of Mesenchymal Stem Cells.
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Boam,D.S., Davidson,I. and Chambon,P.
  TITLE     A TATA-less promoter containing binding sites for ubiquitous
            transcription factors mediates cell type-specific regulation of the
            gene for transcription enhancer factor-1 (TEF-1)
  JOURNAL   J Biol Chem 270 (33), 19487-19494 (1995)
   PUBMED   7642633
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Fossdal,R., Magnusson,L., Weber,J.L. and Jensson,O.
  TITLE     Mapping the locus of atrophia areata, a helicoid peripapillary
            chorioretinal degeneration with autosomal dominant inheritance, to
            chromosome 11p15
  JOURNAL   Hum Mol Genet 4 (3), 479-483 (1995)
   PUBMED   7795606
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Kariya,K., Farrance,I.K. and Simpson,P.C.
  TITLE     Transcriptional enhancer factor-1 in cardiac myocytes interacts
            with an alpha 1-adrenergic- and beta-protein kinase C-inducible
            element in the rat beta-myosin heavy chain promoter
  JOURNAL   J Biol Chem 268 (35), 26658-26662 (1993)
   PUBMED   8253797
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Shimizu,N., Smith,G. and Izumo,S.
  TITLE     Both a ubiquitous factor mTEF-1 and a distinct muscle-specific
            factor bind to the M-CAT motif of the myosin heavy chain beta gene
  JOURNAL   Nucleic Acids Res 21 (17), 4103-4110 (1993)
   PUBMED   8396764
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Xiao,J.H., Davidson,I., Matthes,H., Garnier,J.M. and Chambon,P.
  TITLE     Cloning, expression, and transcriptional properties of the human
            enhancer factor TEF-1
  JOURNAL   Cell 65 (4), 551-568 (1991)
   PUBMED   1851669
  REMARK    GeneRIF: TEAD1 has non-AUG translation initiation
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107881.16, BG720371.1,
            DR000961.1, BC115398.1, AB209858.1, CN420966.1, BU172369.1 and
            CA420177.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 21, 2010 this sequence version replaced NP_068780.1.
            
            Summary: This gene encodes a ubiquitous transcriptional enhancer
            factor that is a member of the TEA/ATTS domain family. This protein
            directs the transactivation of a wide variety of genes and, in
            placental cells, also acts as a transcriptional repressor.
            Mutations in this gene cause Sveinsson's chorioretinal atrophy.
            Additional transcript variants have been described but their
            full-length natures have not been experimentally verified.
            [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803616.77508.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968189, SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match       :: ENST00000527636.7/ ENSP00000435233.2
            non-AUG initiation codon :: PMID: 1851669
            RefSeq Select criteria   :: based on single protein-coding
                                        transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.3"
     Protein         1..426
                     /product="transcriptional enhancer factor TEF-1"
                     /note="protein GT-IIC; transcriptional enhancer factor 1;
                     transcription factor 13; TEA domain family member 1 (SV40
                     transcriptional enhancer factor)"
                     /calculated_mol_wt=47815
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28347.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P28347.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28347.2)"
     Region          30..97
                     /region_name="TEA"
                     /note="TEA domain; smart00426"
                     /db_xref="CDD:128703"
     Region          167..426
                     /region_name="Transcriptional activation.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P28347.2)"
     Region          215..423
                     /region_name="YBD"
                     /note="YAP binding domain; pfam17725"
                     /db_xref="CDD:435993"
     CDS             1..426
                     /gene="TEAD1"
                     /gene_synonym="AA; NTEF-1; REF1; TCF-13; TCF13; TEAD-1;
                     TEF-1"
                     /coded_by="NM_021961.6:622..1902"
                     /exception="alternative start codon"
                     /note="non-AUG (AUU) translation initiation codon"
                     /db_xref="CCDS:CCDS7810.2"
                     /db_xref="GeneID:7003"
                     /db_xref="HGNC:HGNC:11714"
                     /db_xref="MIM:189967"
ORIGIN      
        1 mepsswsgse spaenmerms dsadkpidnd aegvwspdie qsfqealaiy ppcgrrkiil
       61 sdegkmygrn eliaryiklr tgktrtrkqv sshiqvlarr ksrdfhsklk dqtakdkalq
      121 hmaamssaqi vsataihnkl glpgiprptf pgapgfwpgm iqtgqpgssq dvkpfvqqay
      181 piqpavtapi pgfepasapa psvpawqgrs igttklrlve fsafleqqrd pdsynkhlfv
      241 highanhsys dpllesvdir qiydkfpekk gglkelfgkg pqnafflvkf wadlncniqd
      301 dagafygvts qyessenmtv tcstkvcsfg kqvvekvete yarfengrfv yrinrspmce
      361 yminfihklk hlpekymmns vlenftillv vtnrdtqetl lcmacvfevs nsehgaqhhi
      421 yrlvkd
//
LOCUS       NP_001349685             268 aa            linear   ROD 27-APR-2025
DEFINITION  acyl-coenzyme A thioesterase 8 isoform 2 [Mus musculus].
ACCESSION   NP_001349685
VERSION     NP_001349685.1
DBSOURCE    REFSEQ: accession NM_001362756.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Westin,M.A., Hunt,M.C. and Alexson,S.E.
  TITLE     The identification of a succinyl-CoA thioesterase suggests a novel
            pathway for succinate production in peroxisomes
  JOURNAL   J Biol Chem 280 (46), 38125-38132 (2005)
   PUBMED   16141203
  REMARK    GeneRIF: ACOT4 and ACOT8 are responsible for the termination of
            beta-oxidation of dicarboxylic acids of medium-chain length with
            the concomitant release of the corresponding free acids
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Hunt,M.C., Yamada,J., Maltais,L.J., Wright,M.W., Podesta,E.J. and
            Alexson,S.E.
  TITLE     A revised nomenclature for mammalian acyl-CoA
            thioesterases/hydrolases
  JOURNAL   J Lipid Res 46 (9), 2029-2032 (2005)
   PUBMED   16103133
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Kikuchi,M., Hatano,N., Yokota,S., Shimozawa,N., Imanaka,T. and
            Taniguchi,H.
  TITLE     Proteomic analysis of rat liver peroxisome: presence of
            peroxisome-specific isozyme of Lon protease
  JOURNAL   J Biol Chem 279 (1), 421-428 (2004)
   PUBMED   14561759
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Hunt,M.C., Solaas,K., Kase,B.F. and Alexson,S.E.
  TITLE     Characterization of an acyl-coA thioesterase that functions as a
            major regulator of peroxisomal lipid metabolism
  JOURNAL   J Biol Chem 277 (2), 1128-1138 (2002)
   PUBMED   11673457
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Ferdinandusse,S., Denis,S., Mooijer,P.A., Zhang,Z., Reddy,J.K.,
            Spector,A.A. and Wanders,R.J.
  TITLE     Identification of the peroxisomal beta-oxidation enzymes involved
            in the biosynthesis of docosahexaenoic acid
  JOURNAL   J Lipid Res 42 (12), 1987-1995 (2001)
   PUBMED   11734571
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591127.12 and AK033724.1.
            
            Transcript Variant: This variant (2) uses an alternate splice
            junction in the 3' end compared to variant 1, that causes a
            frameshift. The resulting isoform (2) has a shorter and distinct
            C-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK033724.1, ERR2680377.166594.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164133, SAMN01164134
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 85.27 cM"
     Protein         1..268
                     /product="acyl-coenzyme A thioesterase 8 isoform 2"
                     /EC_number="3.1.2.2"
                     /EC_number="3.1.2.1"
                     /EC_number="3.1.2.27"
                     /EC_number="3.1.2.3"
                     /EC_number="3.1.2.11"
                     /EC_number="3.1.2.5"
                     /note="acyl-coenzyme A thioesterase 8; choloyl-coenzyme A
                     thioesterase; peroxisomal acyl-CoA thioesterase 2;
                     peroxisomal long-chain acyl-CoA thioesterase 1;
                     peroxisomal acyl-coenzyme A thioester hydrolase 1;
                     peroxisomal acyl-CoA thioesterase 1"
                     /calculated_mol_wt=29411
     Region          35..>246
                     /region_name="tesB"
                     /note="acyl-CoA thioesterase II; TIGR00189"
                     /db_xref="CDD:272951"
     CDS             1..268
                     /gene="Acot8"
                     /gene_synonym="PTE-1; PTE-2; Pte1"
                     /coded_by="NM_001362756.1:65..871"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS89580.1"
                     /db_xref="GeneID:170789"
                     /db_xref="MGI:MGI:2158201"
ORIGIN      
        1 msapeglgda hgdadrgdls gdlrsvlvts vlnleplded lyrgrhywvp tsqrlfggqi
       61 mgqalvaaak svsedvhvhs lhcyfvragd pkvpvlyhve rirtgasfsv ravkavqhgk
      121 aificqasfq qmqpsplqhq fsmpsvpppe dlldhealid qylrdpnlhk kyrvglnrva
      181 aqevpieikv vnpptltqlq alepkqmfwv rargyigegd ikmhccvaay isdyaflgta
      241 llphqskykv alegwcmggc gvgmgsll
//
LOCUS       NP_001354586             462 aa            linear   PRI 27-APR-2025
DEFINITION  synaptotagmin-16 isoform 5 [Homo sapiens].
ACCESSION   NP_001354586 XP_016877185
VERSION     NP_001354586.1
DBSOURCE    REFSEQ: accession NM_001367657.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Chen,J., Wang,Z., Wang,W., Ren,S., Xue,J., Zhong,L., Jiang,T.,
            Wei,H. and Zhang,C.
  TITLE     SYT16 is a prognostic biomarker and correlated with immune
            infiltrates in glioma: A study based on TCGA data
  JOURNAL   Int Immunopharmacol 84, 106490 (2020)
   PUBMED   32289666
  REMARK    GeneRIF: SYT16 is a prognostic biomarker and correlated with immune
            infiltrates in glioma: A study based on TCGA data.
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Mosing,M.A., Verweij,K.J., Medland,S.E., Painter,J., Gordon,S.D.,
            Heath,A.C., Madden,P.A., Montgomery,G.W. and Martin,N.G.
  TITLE     A genome-wide association study of self-rated health
  JOURNAL   Twin Res Hum Genet 13 (4), 398-403 (2010)
   PUBMED   20707712
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Montes,M., Fuson,K.L., Sutton,R.B. and Robert,J.J.
  TITLE     Purification, crystallization and X-ray diffraction analysis of
            human synaptotagmin 1 C2A-C2B
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 62 (Pt 9), 926-929
            (2006)
   PUBMED   16946482
  REMARK    GeneRIF: Human synaptotagmin tandem C2 domains C2A-C2B have been
            expressed as a glutathione-S-transferase fusion protein in
            Escherichia coli, purified, and crystallized and the preliminary
            X-ray analysis reported.
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Craxton,M.
  TITLE     Synaptotagmin gene content of the sequenced genomes
  JOURNAL   BMC Genomics 5 (1), 43 (2004)
   PUBMED   15238157
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Fukuda,M.
  TITLE     Molecular cloning, expression, and characterization of a novel
            class of synaptotagmin (Syt XIV) conserved from Drosophila to
            humans
  JOURNAL   J Biochem 133 (5), 641-649 (2003)
   PUBMED   12801916
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Craxton,M.
  TITLE     Genomic analysis of synaptotagmin genes
  JOURNAL   Genomics 77 (1-2), 43-49 (2001)
   PUBMED   11543631
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL137918.4, AL356018.5 and AL390816.4.
            
            On Dec 12, 2018 this sequence version replaced XP_016877185.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.445648.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119, SAMEA2158188
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..462
                     /product="synaptotagmin-16 isoform 5"
                     /note="chr14 synaptotagmin; synaptotagmin 14-like protein;
                     synaptotagmin XIV-related protein; synaptotagmin XVI"
                     /calculated_mol_wt=51523
     Region          167..290
                     /region_name="C2A_Synaptotagmin-14_16"
                     /note="C2A domain first repeat present in Synaptotagmins
                     14 and 16; cd08389"
                     /db_xref="CDD:176035"
     Region          323..460
                     /region_name="C2B_Synaptotagmin-14_16"
                     /note="C2 domain second repeat present in Synaptotagmins
                     14 and 16; cd08408"
                     /db_xref="CDD:176053"
     CDS             1..462
                     /gene="SYT16"
                     /gene_synonym="CHR14SYT; Strep14; SYT14L; syt14r"
                     /coded_by="NM_001367657.1:275..1663"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:83851"
                     /db_xref="HGNC:HGNC:23142"
                     /db_xref="MIM:610950"
ORIGIN      
        1 mlvtpeaigf lsavgvfivl lavlflfink klcfetiggl pflehrgkrk hskdktgihk
       61 gldldgasqr rysenlsyge ddhipahsqs pcergdakhh gtshqessvv qslrrqsteg
      121 slemetafns rgfedsyatd sssmwspeeq drtnlqvpsg vsepiskcgd ldvifeyraa
      181 sqkltvtivr aqglpdkdrs gvnswqvhvv llpgkkhrgr tniqrgpnpv frekvtfakl
      241 eprdvaacav rfrlyaarkm trermmgekl fylshlhpeg emkvtlvlep rsnissggsp
      301 lspsavshsd stsstqslsh ggapellvgl synattgrls vemikgshfr nlavnrapdt
      361 ygklfllnsv gqemsrckts irrgqpnpvy ketfvfqval fqlsdvtlmi svynrrtmkr
      421 kemigwialg qnssgeeeqd hweemketkg qqicrwhtll es
//
LOCUS       NP_001352178             486 aa            linear   PRI 27-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 3
            [Homo sapiens].
ACCESSION   NP_001352178
VERSION     NP_001352178.1
DBSOURCE    REFSEQ: accession NM_001365249.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Zhang,S., Huang,J., Lan,Z., Xiao,Y., Liao,Y., Basnet,S., Huang,P.,
            Li,Y., Yan,J., Sheng,Y., Zhou,W., Liu,Q., Tan,H., Tan,Y., Yuan,L.,
            Wang,L., Dai,L., Zhang,W. and Du,C.
  TITLE     CPEB1 Controls NRF2 Proteostasis and Ferroptosis Susceptibility in
            Pancreatic Cancer
  JOURNAL   Int J Biol Sci 20 (8), 3156-3172 (2024)
   PUBMED   38904009
  REMARK    GeneRIF: CPEB1 Controls NRF2 Proteostasis and Ferroptosis
            Susceptibility in Pancreatic Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Pico,S., Parras,A., Santos-Galindo,M., Pose-Utrilla,J., Castro,M.,
            Fraga,E., Hernandez,I.H., Elorza,A., Anta,H., Wang,N.,
            Marti-Sanchez,L., Belloc,E., Garcia-Esparcia,P., Garrido,J.J.,
            Ferrer,I., Macias-Garcia,D., Mir,P., Artuch,R., Perez,B.,
            Hernandez,F., Navarro,P., Lopez-Sendon,J.L., Iglesias,T.,
            Yang,X.W., Mendez,R. and Lucas,J.J.
  TITLE     CPEB alteration and aberrant transcriptome-polyadenylation lead to
            a treatable SLC19A3 deficiency in Huntington's disease
  JOURNAL   Sci Transl Med 13 (613), eabe7104 (2021)
   PUBMED   34586830
  REMARK    GeneRIF: CPEB alteration and aberrant transcriptome-polyadenylation
            lead to a treatable SLC19A3 deficiency in Huntington's disease.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Shao,K., Pu,W., Zhang,J., Guo,S., Qian,F., Glurich,I., Jin,Q.,
            Ma,Y., Ju,S., Zhang,Z. and Ding,W.
  TITLE     DNA hypermethylation contributes to colorectal cancer metastasis by
            regulating the binding of CEBPB and TFCP2 to the CPEB1 promoter
  JOURNAL   Clin Epigenetics 13 (1), 89 (2021)
   PUBMED   33892791
  REMARK    GeneRIF: DNA hypermethylation contributes to colorectal cancer
            metastasis by regulating the binding of CEBPB and TFCP2 to the
            CPEB1 promoter.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Sovijit,W., Sovijit,W., Ishii,Y., Kambe,J., Fujita,T., Watanabe,G.,
            Yamaguchi,H. and Nagaoka,K.
  TITLE     Estrogen promotes increased breast cancer cell proliferation and
            migration through downregulation of CPEB1 expression
  JOURNAL   Biochem Biophys Res Commun 534, 871-876 (2021)
   PUBMED   33162033
  REMARK    GeneRIF: Estrogen promotes increased breast cancer cell
            proliferation and migration through downregulation of CPEB1
            expression.
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Jiao,W., Zhao,S., Liu,R., Guo,T. and Qin,Y.
  TITLE     CPEB1 deletion is not a common explanation for premature ovarian
            insufficiency in a Chinese cohort
  JOURNAL   J Ovarian Res 13 (1), 49 (2020)
   PUBMED   32354341
  REMARK    GeneRIF: CPEB1 deletion is not a common explanation for premature
            ovarian insufficiency in a Chinese cohort.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Hagele,S., Kuhn,U., Boning,M. and Katschinski,D.M.
  TITLE     Cytoplasmic polyadenylation-element-binding protein (CPEB)1 and 2
            bind to the HIF-1alpha mRNA 3'-UTR and modulate HIF-1alpha protein
            expression
  JOURNAL   Biochem J 417 (1), 235-246 (2009)
   PUBMED   18752464
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Sasayama,T., Marumoto,T., Kunitoku,N., Zhang,D., Tamaki,N.,
            Kohmura,E., Saya,H. and Hirota,T.
  TITLE     Over-expression of Aurora-A targets cytoplasmic polyadenylation
            element binding protein and promotes mRNA polyadenylation of Cdk1
            and cyclin B1
  JOURNAL   Genes Cells 10 (7), 627-638 (2005)
   PUBMED   15966895
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Wilczynska,A., Aigueperse,C., Kress,M., Dautry,F. and Weil,D.
  TITLE     The translational regulator CPEB1 provides a link between dcp1
            bodies and stress granules
  JOURNAL   J Cell Sci 118 (Pt 5), 981-992 (2005)
   PUBMED   15731006
  REMARK    GeneRIF: CPEB1 has a role in compartmentalization of mRNA
            metabolism in the cytoplasm, between dcp1 bodies and stress
            granules
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Mendez,R. and Richter,J.D.
  TITLE     Translational control by CPEB: a means to the end
  JOURNAL   Nat Rev Mol Cell Biol 2 (7), 521-529 (2001)
   PUBMED   11433366
  REMARK    Review article
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Welk,J.F., Charlesworth,A., Smith,G.D. and MacNicol,A.M.
  TITLE     Identification and characterization of the gene encoding human
            cytoplasmic polyadenylation element binding protein
  JOURNAL   Gene 263 (1-2), 113-120 (2001)
   PUBMED   11223249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245033.2.
            
            Summary: This gene encodes a member of the cytoplasmic
            polyadenylation element binding protein family. This highly
            conserved protein binds to a specific RNA sequence, called the
            cytoplasmic polyadenylation element, found in the 3' untranslated
            region of some mRNAs. The encoded protein functions in both the
            cytoplasm and the nucleus. It is involved in the regulation of mRNA
            translation, as well as processing of the 3' untranslated region,
            and may play a role in cell proliferation and tumorigenesis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.211450.1,
                                           SRR1660805.132868.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..486
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 3"
                     /note="CPE-binding protein 1"
                     /calculated_mol_wt=53504
     Region          <1..232
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          234..336
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          347..430
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          424..479
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..486
                     /gene="CPEB1"
                     /gene_synonym="CPE-BP1; CPEB; CPEB-1; h-CPEB; hCPEB-1"
                     /coded_by="NM_001365249.1:61..1521"
                     /note="isoform 3 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS45330.2"
                     /db_xref="GeneID:64506"
                     /db_xref="HGNC:HGNC:21744"
                     /db_xref="MIM:607342"
ORIGIN      
        1 mlfptsaqes srglpdandl clglqslslt gwdrpwstqd sdssaqssth svlsmlhnpl
       61 gnvlgkppls flpldplgsd lvdkfpapsv rgsrldtrpi ldsrssspsd sdtsgfssgs
      121 dhlsdlissl rispplpfls lsgggprdpl kmgvgsrmdq eqaalaavtp sptsaskrwp
      181 gasvwpswdl leapkdpfsi erearlhrqa aavneatctw sgqlpprnyk npiysckvfl
      241 ggvpwditea glvntfrvfg slsvewpgkd gkhprcppkg yvylvfelek svrsllqacs
      301 hdplspdgls eyyfkmssrr mrckevqvip wvladsnfvr spsqrldpsr tvfvgalhgm
      361 lnaealaail ndlfggvvya gidtdkhkyp igsgrvtfnn qrsylkavsa afveikttkf
      421 tkkvqidpyl edslchicss qpgpffcrdq vcfkyfcrsc whwrhsmegl rhhsplmrnq
      481 knrdss
//
LOCUS       NP_079940                595 aa            linear   ROD 27-APR-2025
DEFINITION  sorting nexin-9 [Mus musculus].
ACCESSION   NP_079940 XP_978237 XP_989309
VERSION     NP_079940.2
DBSOURCE    REFSEQ: accession NM_025664.6
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Wang,L., Yang,Z., Satoshi,F., Prasanna,X., Yan,Z., Vihinen,H.,
            Chen,Y., Zhao,Y., He,X., Bu,Q., Li,H., Zhao,Y., Jiang,L., Qin,F.,
            Dai,Y., Zhang,N., Qin,M., Kuang,W., Zhao,Y., Jokitalo,E.,
            Vattulainen,I., Kajander,T., Zhao,H. and Cen,X.
  TITLE     Membrane remodeling by FAM92A1 during brain development regulates
            neuronal morphology, synaptic function, and cognition
  JOURNAL   Nat Commun 15 (1), 6209 (2024)
   PUBMED   39043703
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Kawasaki,T., Sugihara,F., Fukushima,K., Matsuki,T., Nabeshima,H.,
            Machida,T., Mitsui,Y., Fujimura,S., Sagawa,R., Gaheun,L.,
            Kuniyoshi,K., Tanaka,H., Narazaki,M., Kumanogoh,A., Akira,S. and
            Satoh,T.
  TITLE     Loss of FCHSD1 leads to amelioration of chronic obstructive
            pulmonary disease
  JOURNAL   Proc Natl Acad Sci U S A 118 (26) (2021)
   PUBMED   34168078
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Liu,C., Zhai,X., Du,H., Cao,Y., Cao,H., Wang,Y., Yu,X., Gao,J. and
            Xu,Z.
  TITLE     Sorting nexin 9 (SNX9) is not essential for development and
            auditory function in mice
  JOURNAL   Oncotarget 7 (42), 68921-68932 (2016)
   PUBMED   27655699
  REMARK    GeneRIF: Snx9-deficient mice do not show defects in development as
            well as auditory function, suggesting that SNX9 is not essential
            for mice development and hearing
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Nandez,R., Balkin,D.M., Messa,M., Liang,L., Paradise,S., Czapla,H.,
            Hein,M.Y., Duncan,J.S., Mann,M. and De Camilli,P.
  TITLE     A role of OCRL in clathrin-coated pit dynamics and uncoating
            revealed by studies of Lowe syndrome cells
  JOURNAL   Elife 3, e02975 (2014)
   PUBMED   25107275
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 595)
  AUTHORS   Cao,H., Yin,X., Cao,Y., Jin,Y., Wang,S., Kong,Y., Chen,Y., Gao,J.,
            Heller,S. and Xu,Z.
  TITLE     FCHSD1 and FCHSD2 are expressed in hair cell stereocilia and
            cuticular plate and regulate actin polymerization in vitro
  JOURNAL   PLoS One 8 (2), e56516 (2013)
   PUBMED   23437151
REFERENCE   6  (residues 1 to 595)
  AUTHORS   Schimenti,J.C., Reynolds,J.L. and Planchart,A.
  TITLE     Mutations in Serac1 or Synj2 cause proximal t haplotype-mediated
            male mouse sterility but not transmission ratio distortion
  JOURNAL   Proc Natl Acad Sci U S A 102 (9), 3342-3347 (2005)
   PUBMED   15722415
REFERENCE   7  (residues 1 to 595)
  AUTHORS   MaCaulay,S.L., Stoichevska,V., Grusovin,J., Gough,K.H.,
            Castelli,L.A. and Ward,C.W.
  TITLE     Insulin stimulates movement of sorting nexin 9 between cellular
            compartments: a putative role mediating cell surface receptor
            expression and insulin action
  JOURNAL   Biochem J 376 (Pt 1), 123-134 (2003)
   PUBMED   12917015
REFERENCE   8  (residues 1 to 595)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC168063.3 and AK155830.1.
            
            On or before May 4, 2006 this sequence version replaced
            XP_989309.1, XP_978237.1, NP_079940.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK170339.1, AK155830.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 3.51 cM"
     Protein         1..595
                     /product="sorting nexin-9"
                     /calculated_mol_wt=66415
     Region          4..60
                     /region_name="SH3_SNX9"
                     /note="Src Homology 3 domain of Sorting nexin 9; cd11898"
                     /db_xref="CDD:212831"
     Site            order(9,11,14,19,38..39,53,55..56)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212831"
     Region          89..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91VH2.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y5X1; propagated from
                     UniProtKB/Swiss-Prot (Q91VH2.1)"
     Region          127..>357
                     /region_name="COG5391"
                     /note="Phox homology (PX) domain protein [Intracellular
                     trafficking and secretion / General function prediction
                     only]"
                     /db_xref="CDD:227680"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q91VH2.1)"
     Region          201..213
                     /region_name="Critical for tubulation activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91VH2.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q91VH2.1)"
     Region          250..375
                     /region_name="PX_SNX9"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 9; cd07285"
                     /db_xref="CDD:132818"
     Site            order(286..288,313,327)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132818"
     Site            288
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y5X1; propagated from
                     UniProtKB/Swiss-Prot (Q91VH2.1)"
     Region          386..595
                     /region_name="BAR_SNX9"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Sorting
                     Nexin 9; cd07668"
                     /db_xref="CDD:153352"
     Site            order(405,408..409,412..413,415..416,419,422..423,426,
                     434..435,437..438,441,444..445,448..449,452,454..455,457,
                     460,471,553,556..557,559..561,564,567..568,570..572,
                     574..575,578..579,581..582,585..586,588..589,592..595)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153352"
     Site            order(407,414,425..426,433,437,497,511,516,522,528)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153352"
     CDS             1..595
                     /gene="Snx9"
                     /gene_synonym="2700073N08Rik; SDP1; SH3PX1"
                     /coded_by="NM_025664.6:212..1999"
                     /db_xref="CCDS:CCDS57041.1"
                     /db_xref="GeneID:66616"
                     /db_xref="MGI:MGI:1913866"
ORIGIN      
        1 matkarvmyd faaepgnnel tvtegeiitv tnpnvgggwl egknnkgeqg lvptdyveil
       61 pndgkdpfsc gnsvadqafl dsltastaqt nsssansnnq vgggndpwta wnapkpgnwd
      121 ssdawgsrtd gtsaqrnssa nnwdtgfghp qayqgpatgd ddewdedwdd pkssspyfkd
      181 sepaeaggiq rgnsragass mklplnkfpg fakpgmeqyl lakqlakpke kiaiivgdyg
      241 pmwvyptstf dcvvadprkg skmyglksyi eyqltptntn rsvnhrykhf dwlyerllvk
      301 fgsaipipsl pdkqvtgrfe eefikmrmer lqawmtrmcr hpvvsesevf qqflnfrdek
      361 ewktgkrkae kdelvgvmif stmepeapdl dlieieqkcd avgkftkamd dgvkelltvg
      421 qehwkrctgp lpkeyqkigk alqslaavfs ssgyqgetdl ndaiteagkt yeeiaslvae
      481 qpkkdlhflm ecnheykgfl gcfpdiigah kgaiekvkes dklvatskit pqdkqtmvkr
      541 vgtmsyalqa emnhfhsnri ydynsvirly leqqvqfyet iaeklrqals rfpvm
//
LOCUS       NP_032337                479 aa            linear   ROD 27-APR-2025
DEFINITION  5-hydroxytryptamine receptor 2B [Mus musculus].
ACCESSION   NP_032337
VERSION     NP_032337.2
DBSOURCE    REFSEQ: accession NM_008311.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Frolova,V.S., Nikishina,Y.O., Shmukler,Y.B. and Nikishin,D.A.
  TITLE     Serotonin Signaling in Mouse Preimplantation Development: Insights
            from Transcriptomic and Structural-Functional Analyses
  JOURNAL   Int J Mol Sci 25 (23), 12954 (2024)
   PUBMED   39684667
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Li,T., Wei,L., Zhang,X., Fu,B., Zhou,Y., Yang,M., Cao,M., Chen,Y.,
            Tan,Y., Shi,Y., Wu,L., Xuan,C., Du,Q. and Hu,R.
  TITLE     Serotonin Receptor HTR2B Facilitates Colorectal Cancer Metastasis
            via CREB1-ZEB1 Axis-Mediated Epithelial-Mesenchymal Transition
  JOURNAL   Mol Cancer Res 22 (6), 538-554 (2024)
   PUBMED   38381131
  REMARK    GeneRIF: Serotonin Receptor HTR2B Facilitates Colorectal Cancer
            Metastasis via CREB1-ZEB1 Axis-Mediated Epithelial-Mesenchymal
            Transition.
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Benhadda,A., Delhaye,C., Moutkine,I., Marques,X., Russeau,M., Le
            Magueresse,C., Roumier,A., Levi,S. and Maroteaux,L.
  TITLE     5-HT1A and 5-HT2B receptor interaction and co-clustering regulate
            serotonergic neuron excitability
  JOURNAL   iScience 26 (8), 107401 (2023)
   PUBMED   37575185
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Albertini,G., D'Andrea,I., Druart,M., Bechade,C., Nieves-Rivera,N.,
            Etienne,F., Le Magueresse,C., Rebsam,A., Heck,N., Maroteaux,L. and
            Roumier,A.
  TITLE     Serotonin sensing by microglia conditions the proper development of
            neuronal circuits and of social and adaptive skills
  JOURNAL   Mol Psychiatry 28 (6), 2328-2342 (2023)
   PUBMED   37217677
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Bonhaus,D.W., Bach,C., DeSouza,A., Salazar,F.H., Matsuoka,B.D.,
            Zuppan,P., Chan,H.W. and Eglen,R.M.
  TITLE     The pharmacology and distribution of human 5-hydroxytryptamine2B
            (5-HT2B) receptor gene products: comparison with 5-HT2A and 5-HT2C
            receptors
  JOURNAL   Br J Pharmacol 115 (4), 622-628 (1995)
   PUBMED   7582481
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Loric,S., Launay,J.M., Colas,J.F. and Maroteaux,L.
  TITLE     New mouse 5-HT2-like receptor. Expression in brain, heart and
            intestine
  JOURNAL   FEBS Lett 312 (2-3), 203-207 (1992)
   PUBMED   1426253
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Kursar,J.D., Nelson,D.L., Wainscott,D.B., Cohen,M.L. and Baez,M.
  TITLE     Molecular cloning, functional expression, and pharmacological
            characterization of a novel serotonin receptor
            (5-hydroxytryptamine2F) from rat stomach fundus
  JOURNAL   Mol Pharmacol 42 (4), 549-557 (1992)
   PUBMED   1331748
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Foguet,M., Hoyer,D., Pardo,L.A., Parekh,A., Kluxen,F.W.,
            Kalkman,H.O., Stuhmer,W. and Lubbert,H.
  TITLE     Cloning and functional characterization of the rat stomach fundus
            serotonin receptor
  JOURNAL   EMBO J 11 (9), 3481-3487 (1992)
   PUBMED   1505525
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Foguet,M., Nguyen,H., Le,H. and Lubbert,H.
  TITLE     Structure of the mouse 5-HT1C, 5-HT2 and stomach fundus serotonin
            receptor genes
  JOURNAL   Neuroreport 3 (4), 345-348 (1992)
   PUBMED   1381232
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC157768.4.
            
            On Nov 17, 2006 this sequence version replaced NP_032337.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK033713.1, BC023690.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 43.94 cM"
     Protein         1..479
                     /product="5-hydroxytryptamine receptor 2B"
                     /note="NP75 protein; serotonin receptor 2B"
                     /calculated_mol_wt=53466
     Site            29
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02152.3)"
     Region          54..397
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          56..80
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341347"
     Site            56..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     Region          89..111
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341347"
     Site            90..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     Region          128..150
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341347"
     Site            129..150
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     Region          151..153
                     /region_name="DRY motif, important for ligand-induced
                     conformation changes.
                     /evidence=ECO:0000250|UniProtKB:P41595"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     Site            171..191
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     Region          173..189
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341347"
     Site            208
                     /site_type="other"
                     /note="Hydrophobic barrier that decreases the speed of
                     ligand binding and dissociation.
                     /evidence=ECO:0000250|UniProtKB:P41595; propagated from
                     UniProtKB/Swiss-Prot (Q02152.3)"
     Region          211..214
                     /region_name="[DE]RFG motif, may stabilize a conformation
                     that preferentially activates signaling via beta-arrestin
                     family members. /evidence=ECO:0000250|UniProtKB:P41595"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     Region          214..237
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341347"
     Site            216..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     Region          322..344
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341347"
     Site            324..344
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     Region          358..383
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341347"
     Site            360..381
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     Region          375..379
                     /region_name="NPxxY motif, important for ligand-induced
                     conformation changes and signaling.
                     /evidence=ECO:0000250|UniProtKB:P41595"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     Region          477..479
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000250|UniProtKB:P41595"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02152.3)"
     CDS             1..479
                     /gene="Htr2b"
                     /gene_synonym="5-HT-2B; 5-HT-2F; 5-HT2B"
                     /coded_by="NM_008311.3:337..1776"
                     /db_xref="CCDS:CCDS35644.1"
                     /db_xref="GeneID:15559"
                     /db_xref="MGI:MGI:109323"
ORIGIN      
        1 massykmseq sttsehilqk tcdhliltnr sgletdsvae emkqtvegqg htvhwaalli
       61 laviiptigg nilvilaval ekrlqyatny flmslaiadl lvglfvmpia lltimfeaiw
      121 plplalcpaw lfldvlfsta simhlcaisl dryiaikkpi qanqcnsrat afikitvvwl
      181 isigiaipvp ikgietdvin phnvtceltk drfgsfmvfg slaaffaplt imvvtyflti
      241 htlqkkaylv knkppqrltr wtvptvflre dssfsspekv amldgshrdk ilpnssdetl
      301 mrrmssvgkr saqtisneqr askalgvvff lfllmwcpff itnltlalcd scnqttlktl
      361 leifvwigyv ssgvnpliyt lfnktfreaf gryitcnyra tksvkalrkf sstlcfgnsm
      421 venskfftkh girnginpam yqspmrlrss tiqsssiill dtlltendgd kaeeqvsyi
//
LOCUS       NP_001357325             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357325
VERSION     NP_001357325.1
DBSOURCE    REFSEQ: accession NM_001370396.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.215588.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370396.1:1525..3174"
                     /note="isoform 1 is encoded by transcript variant 25"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_001348392             173 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein mL62 isoform 4 [Mus musculus].
ACCESSION   NP_001348392
VERSION     NP_001348392.1
DBSOURCE    REFSEQ: accession NM_001361463.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Cheong,A., Lingutla,R. and Mager,J.
  TITLE     Expression analysis of mammalian mitochondrial ribosomal protein
            genes
  JOURNAL   Gene Expr Patterns 38, 119147 (2020)
   PUBMED   32987154
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Feaga,H.A., Quickel,M.D., Hankey-Giblin,P.A. and Keiler,K.C.
  TITLE     Human Cells Require Non-stop Ribosome Rescue Activity in
            Mitochondria
  JOURNAL   PLoS Genet 12 (3), e1005964 (2016)
   PUBMED   27029019
  REMARK    GeneRIF: Because ICT1 is essential in human cells, these results
            suggest that ribosome rescue activity in mitochondria is required
            in humans
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Handa,Y., Hikawa,Y., Tochio,N., Kogure,H., Inoue,M., Koshiba,S.,
            Guntert,P., Inoue,Y., Kigawa,T., Yokoyama,S. and Nameki,N.
  TITLE     Solution structure of the catalytic domain of the mitochondrial
            protein ICT1 that is essential for cell vitality
  JOURNAL   J Mol Biol 404 (2), 260-273 (2010)
   PUBMED   20869366
  REMARK    GeneRIF: solution structure of the catalytic domain of the ICT1
            protein that lacks an N-terminal mitochondrial targeting signal and
            an unstructured C-terminal basic-residue-rich extension
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL603828.9 and AL627096.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BF012650.1, SRR11927938.3700145.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 80.84 cM"
     Protein         1..173
                     /product="large ribosomal subunit protein mL62 isoform 4"
                     /EC_number="3.1.1.29"
                     /note="peptidyl-tRNA hydrolase ICT1, mitochondrial; large
                     ribosomal subunit protein mL62; immature colon carcinoma
                     transcript 1 protein homolog; 39S ribosomal protein L58,
                     mitochondrial"
                     /calculated_mol_wt=19639
     Region          43..173
                     /region_name="PrfB"
                     /note="Protein chain release factor PrfB [Translation,
                     ribosomal structure and biogenesis]; COG1186"
                     /db_xref="CDD:440799"
     CDS             1..173
                     /gene="Mrpl58"
                     /gene_synonym="1110001A02Rik; 1110002E03Rik; Ict1;
                     MRP-L58"
                     /coded_by="NM_001361463.1:24..545"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:68572"
                     /db_xref="MGI:MGI:1915822"
ORIGIN      
        1 matawglrwg lsrtgtllla pparcarral hrqehakqas syipldrlsi sycrssgpgg
       61 qnvnkvnska evrfhlasad wieepvrqki altinkagel vltsessryq frnlaeclqk
      121 irdmiaeasq vpkepskeda rlqrlriekm nrerlrqkrl nsalktsrrm tmd
//
LOCUS       NP_001343263             648 aa            linear   ROD 27-APR-2025
DEFINITION  RAF proto-oncogene serine/threonine-protein kinase isoform 1 [Mus
            musculus].
ACCESSION   NP_001343263 XP_006505428
VERSION     NP_001343263.1
DBSOURCE    REFSEQ: accession NM_001356334.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Luo,X., Zhang,D., Zheng,J., Liu,H., Sun,L., Guo,H., Wang,L. and
            Cui,S.
  TITLE     Casein kinase 1alpha mediates estradiol secretion via CYP19A1
            expression in mouse ovarian granulosa cells
  JOURNAL   BMC Biol 22 (1), 176 (2024)
   PUBMED   39183304
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Liu,H., Niu,T., Qiu,G., Cui,S. and Zhang,D.
  TITLE     Taurine promotes insulin synthesis by enhancing Isl-1 expression
            through miR-7a/RAF1/ERK1/2 pathway
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (1), 23-35 (2024)
   PUBMED   38117455
  REMARK    GeneRIF: Taurine promotes insulin synthesis by enhancing Isl-1
            expression through miR-7a/RAF1/ERK1/2 pathway.
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Geng,W., Cao,M., Dong,K., An,J. and Gao,H.
  TITLE     SHOC2 mediates the drug-resistance of triple-negative breast cancer
            cells to everolimus
  JOURNAL   Cancer Biol Ther 24 (1), 2206362 (2023)
   PUBMED   37170083
  REMARK    GeneRIF: SHOC2 mediates the drug-resistance of triple-negative
            breast cancer cells to everolimus.
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Zhong,S. and Borlak,J.
  TITLE     Sex disparities in non-small cell lung cancer: mechanistic insights
            from a cRaf transgenic disease model
  JOURNAL   EBioMedicine 95, 104763 (2023)
   PUBMED   37625265
  REMARK    GeneRIF: Sex disparities in non-small cell lung cancer: mechanistic
            insights from a cRaf transgenic disease model.
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Kyriakis,J.M., App,H., Zhang,X.F., Banerjee,P., Brautigan,D.L.,
            Rapp,U.R. and Avruch,J.
  TITLE     Raf-1 activates MAP kinase-kinase
  JOURNAL   Nature 358 (6385), 417-421 (1992)
   PUBMED   1322500
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Ludwig,T., Ruther,U., Metzger,R., Copeland,N.G., Jenkins,N.A.,
            Lobel,P. and Hoflack,B.
  TITLE     Gene and pseudogene of the mouse cation-dependent mannose
            6-phosphate receptor. Genomic organization, expression, and
            chromosomal localization
  JOURNAL   J Biol Chem 267 (17), 12211-12219 (1992)
   PUBMED   1376319
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Wilkie,T.M., Gilbert,D.J., Olsen,A.S., Chen,X.N., Amatruda,T.T.,
            Korenberg,J.R., Trask,B.J., de Jong,P., Reed,R.R., Simon,M.I. et
            al.
  TITLE     Evolution of the mammalian G protein alpha subunit multigene family
  JOURNAL   Nat Genet 1 (2), 85-91 (1992)
   PUBMED   1302014
  REMARK    Review article
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Danciger,M., Chakraborti,A., Farber,D.B. and Kozak,C.A.
  TITLE     Localization of the gene for a third G protein beta-subunit to
            mouse chromosome 6 near Raf-1
  JOURNAL   Genomics 12 (4), 688-692 (1992)
   PUBMED   1572642
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Moore,K.J., D'Amore-Bruno,M.A., Korfhagen,T.R., Glasser,S.W.,
            Whitsett,J.A., Jenkins,N.A. and Copeland,N.G.
  TITLE     Chromosomal localization of three pulmonary surfactant protein
            genes in the mouse
  JOURNAL   Genomics 12 (2), 388-393 (1992)
   PUBMED   1346779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC160032.7.
            
            On Sep 29, 2017 this sequence version replaced XP_006505428.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB057663.2, SRR1660813.26695.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164134
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 53.62 cM"
     Protein         1..648
                     /product="RAF proto-oncogene serine/threonine-protein
                     kinase isoform 1"
                     /EC_number="2.7.11.1"
                     /note="murine sarcoma 3611 oncogene 1; RAF proto-oncogene
                     serine/threonine-protein kinase; proto-oncogene c-RAF;
                     Craf1 transforming"
                     /calculated_mol_wt=72787
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:15664191; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and MAPK1.
                     /evidence=ECO:0000269|PubMed:15664191; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Region          55..131
                     /region_name="RBD_CRAF"
                     /note="Ras-binding domain (RBD) found in RAF
                     proto-oncogene serine/threonine-protein kinase RAF1/CRAF;
                     cd17135"
                     /db_xref="CDD:340655"
     Site            order(57,59,64..69,71,84,88..90)
                     /site_type="other"
                     /note="RBD_Raf-Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:340655"
     Site            order(57,64,66..69,84,87..90)
                     /site_type="other"
                     /note="putative RBD_Raf-KRas interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340655"
     Site            125
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:340655"
     Region          136..187
                     /region_name="C1_A_C-Raf"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma)
                     kinases, and similar proteins; cd20870"
                     /db_xref="CDD:410420"
     Region          205..265
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA, PKC and PKB/AKT1.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Region          281..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:15664191; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:15664191,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:15664191,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Region          331..349
                     /region_name="Interaction with PEBP1/RKIP.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N57.2)"
     Region          336..618
                     /region_name="STKc_C-Raf"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; cd14149"
                     /db_xref="CDD:271051"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK1, PAK2, PAK3 and PAK5.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK1, PAK2 and PAK3.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            order(340,342,367,369..370,397..403,407..409,454,457..458,
                     461..462,478,480,607)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271051"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            order(355..359,363,373,375,406,421..424,428,430,468,470,
                     472..473,475,486,489,507..510)
                     /site_type="active"
                     /db_xref="CDD:271051"
     Site            order(355..359,363,373,375,406,421..424,428,468,470,
                     472..473,475,486)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271051"
     Site            order(359,428,430,468,470,472,489,507..510)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271051"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            485..510
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271051"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            563
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT5.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15664191; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:15664191,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99N57.2)"
     CDS             1..648
                     /gene="Raf1"
                     /gene_synonym="6430402F14Rik; c-Raf; cRaf; Craf1;
                     D830050J10Rik; Raf-1; v-Raf"
                     /coded_by="NM_001356334.2:227..2173"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS20441.1"
                     /db_xref="GeneID:110157"
                     /db_xref="MGI:MGI:97847"
ORIGIN      
        1 mehiqgawkt isngfglkda vfdgsscisp tivqqfgyqr rasddgkltd ssktsntirv
       61 flpnkqrtvv nvrngmslhd clmkalkvrg lqpeccavfr llqehkgkka rldwntdaas
      121 ligeelqvdf ldhvpltthn farktflkla fcdicqkfll ngfrcqtcgy kfhehcstkv
      181 ptmcvdwsni rqlllfpnst vgdsgvpapp sfpmrrmres vsrmpassqh rystphaftf
      241 ntsspssegs lsqrqrstst pnvhmvsttl hvdsrmieda irshsesasp salssspnnl
      301 sptgwsqpkt pvpaqrerap gsgtqeknki rprgqrdssy yweieasevm lstrigsgsf
      361 gtvykgkwhg dvavkilkvv dptpeqlqaf rnevavlrkt rhvnillfmg ymtkdnlaiv
      421 tqwcegssly khlhvqetkf qmfqlidiar qtaqgmdylh akniihrdmk snniflhegl
      481 tvkigdfgla tvksrwsgsq qveqptgsvl wmapevirmq ddnpfsfqsd vysygivlye
      541 lmagelpyah innrdqiifm vgrgyaspdl srlykncpka mkrlvadcvk kvkeerplfp
      601 qilssiellq hslpkinrsa sepslhraah tedinactlt tsprlpvf
//
LOCUS       NP_001035218              94 aa            linear   PRI 27-APR-2025
DEFINITION  serine protease inhibitor Kazal-type 13 precursor [Homo sapiens].
ACCESSION   NP_001035218
VERSION     NP_001035218.1
DBSOURCE    REFSEQ: accession NM_001040129.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Xu,W.H., Shi,S.N., Wang,J., Xu,Y., Tian,X., Wan,F.N., Cao,D.L.,
            Qu,Y.Y., Zhang,H.L. and Ye,D.W.
  TITLE     The Role of Serine Peptidase Inhibitor Kazal Type 13 (SPINK13) as a
            Clinicopathological and Prognostic Biomarker in Patients with Clear
            Cell Renal Cell Carcinoma
  JOURNAL   Med Sci Monit 25, 9458-9470 (2019)
   PUBMED   31825950
  REMARK    GeneRIF: Gene set enrichment analysis (GSEA) showed that SPINK13
            expression was involved in complement, apical junction,
            epithelial-mesenchymal transition (EMT), glycolysis, hypoxia, and
            inflammation signaling pathways.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Wei,L., Lun,Y., Zhou,X., He,S., Gao,L., Liu,Y., He,Z., Li,B. and
            Wang,C.
  TITLE     Novel urokinase-plasminogen activator inhibitor SPINK13 inhibits
            growth and metastasis of hepatocellular carcinoma in vivo
  JOURNAL   Pharmacol Res 143, 73-85 (2019)
   PUBMED   30862605
  REMARK    GeneRIF: The results of the study indicated that SPINK13 could
            function as a promising therapeutic approach for patients with
            advanced hepatocellular carcinoma.
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Cai,S., Zhang,P., Dong,S., Li,L., Cai,J. and Xu,M.
  TITLE     Downregulation of SPINK13 Promotes Metastasis by Regulating uPA in
            Ovarian Cancer Cells
  JOURNAL   Cell Physiol Biochem 45 (3), 1061-1071 (2018)
   PUBMED   29439245
  REMARK    GeneRIF: SPINK13 inhibited cell migration and epithelial to
            mesenchymal transition (EMT). SPINK13 was found to inhibit the
            expression of urokinase-type plasminogen activator (uPA), while
            recombinant uPA protein could reverse the inhibitory effect of
            SPINK13 on OC metastasis.
REFERENCE   5  (residues 1 to 94)
  AUTHORS   Ma,L., Yu,H., Ni,Z., Hu,S., Ma,W., Chu,C., Liu,Q. and Zhang,Y.
  TITLE     Spink13, an epididymis-specific gene of the Kazal-type serine
            protease inhibitor (SPINK) family, is essential for the acrosomal
            integrity and male fertility
  JOURNAL   J Biol Chem 288 (14), 10154-10165 (2013)
   PUBMED   23430248
REFERENCE   6  (residues 1 to 94)
  AUTHORS   Li,J.Y., Wang,H.Y., Liu,J., Liu,Q., Zhang,J.S., Wan,F.C., Liu,F.J.,
            Jin,S.H. and Zhang,Y.L.
  TITLE     Transcriptome analysis of a cDNA library from adult human
            epididymis
  JOURNAL   DNA Res 15 (3), 115-122 (2008)
   PUBMED   18390568
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011346.5 and BC128164.1.
            
            On or before Apr 16, 2006 this sequence version replaced
            XP_376433.1, XP_945167.1.
            
            Transcript Variant: This variant (1) represents the protein-coding
            transcript.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128164.1, SRR14038193.719912.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398450.5/ ENSP00000381468.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..94
                     /product="serine protease inhibitor Kazal-type 13
                     precursor"
                     /note="hepatitis B virus DNA polymerase transactivated
                     human serine protease inhibitor; serine protease inhibitor
                     Kazal-type 5-like 3; serine protease inhibitor Kazal-type
                     13; hepatitis B virus DNA polymerase transactivated serine
                     protease inhibitor; Hepatitis B Virus (HBV) DNA polymerase
                     transactivated protein 1; serine peptidase inhibitor,
                     Kazal type 13 (putative)"
                     /calculated_mol_wt=8488
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2581
     mat_peptide     24..94
                     /product="Serine protease inhibitor Kazal-type 13.
                     /id=PRO_0000344510"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1W4C9.1)"
                     /calculated_mol_wt=8488
     Region          53..93
                     /region_name="KAZAL_FS"
                     /note="Kazal type serine protease inhibitors and
                     follistatin-like domains. Kazal inhibitors inhibit serine
                     proteases, such as, trypsin, chyomotrypsin, avian
                     ovomucoids, and elastases. The inhibitory domain has one
                     reactive site peptide bond, which serves the...; cd00104"
                     /db_xref="CDD:238052"
     Site            55..56
                     /site_type="other"
                     /note="Reactive bond.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00798; propagated
                     from UniProtKB/Swiss-Prot (Q1W4C9.1)"
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q1W4C9.1)"
     CDS             1..94
                     /gene="SPINK13"
                     /gene_synonym="HBVDNAPTP1; HESPINTOR; LiESP6; SPINK5L3"
                     /coded_by="NM_001040129.3:129..413"
                     /db_xref="CCDS:CCDS43383.1"
                     /db_xref="GeneID:153218"
                     /db_xref="HGNC:HGNC:27200"
                     /db_xref="MIM:615205"
ORIGIN      
        1 maafphkiif flvcstlthv afsgifnkrd ftrwpkprck myipldpdyn adcpnvtapv
       61 casnghtfqn ecffcveqre fhyrikfeky gkcd
//
LOCUS       NP_004609               1001 aa            linear   PRI 27-APR-2025
DEFINITION  DNA topoisomerase 3-alpha isoform 1 [Homo sapiens].
ACCESSION   NP_004609
VERSION     NP_004609.1
DBSOURCE    REFSEQ: accession NM_004618.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Erdinc,D., Rodriguez-Luis,A., Fassad,M.R., Mackenzie,S.,
            Watson,C.M., Valenzuela,S., Xie,X., Menger,K.E., Sergeant,K.,
            Craig,K., Hopton,S., Falkous,G., Poulton,J., Garcia-Moreno,H.,
            Giunti,P., de Moura Aschoff,C.A., Morales Saute,J.A., Kirby,A.J.,
            Toro,C., Wolfe,L., Novacic,D., Greenbaum,L., Eliyahu,A., Barel,O.,
            Anikster,Y., McFarland,R., Gorman,G.S., Schaefer,A.M.,
            Gustafsson,C.M., Taylor,R.W., Falkenberg,M. and Nicholls,T.J.
  CONSRTM   Genomics England Research Consortium
  TITLE     Pathological variants in TOP3A cause distinct disorders of
            mitochondrial and nuclear genome stability
  JOURNAL   EMBO Mol Med 15 (5), e16775 (2023)
   PUBMED   37013609
  REMARK    GeneRIF: Pathological variants in TOP3A cause distinct disorders of
            mitochondrial and nuclear genome stability.
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Soniat,M.M., Nguyen,G., Kuo,H.C. and Finkelstein,I.J.
  TITLE     The MRN complex and topoisomerase IIIa-RMI1/2 synchronize DNA
            resection motor proteins
  JOURNAL   J Biol Chem 299 (2), 102802 (2023)
   PUBMED   36529288
  REMARK    GeneRIF: The MRN complex and topoisomerase IIIa-RMI1/2 synchronize
            DNA resection motor proteins.
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Menger,K.E., Chapman,J., Diaz-Maldonado,H., Khazeem,M.M., Deen,D.,
            Erdinc,D., Casement,J.W., Di Leo,V., Pyle,A., Rodriguez-Luis,A.,
            Cowell,I.G., Falkenberg,M., Austin,C.A. and Nicholls,T.J.
  TITLE     Two type I topoisomerases maintain DNA topology in human
            mitochondria
  JOURNAL   Nucleic Acids Res 50 (19), 11154-11174 (2022)
   PUBMED   36215039
  REMARK    GeneRIF: Two type I topoisomerases maintain DNA topology in human
            mitochondria.
REFERENCE   4  (residues 1 to 1001)
  AUTHORS   de Nonneville,A., Salas,S., Bertucci,F., Sobinoff,A.P.,
            Adelaide,J., Guille,A., Finetti,P., Noble,J.R., Churikov,D.,
            Chaffanet,M., Lavit,E., Pickett,H.A., Bouvier,C., Birnbaum,D.,
            Reddel,R.R. and Geli,V.
  TITLE     TOP3A amplification and ATRX inactivation are mutually exclusive
            events in pediatric osteosarcomas using ALT
  JOURNAL   EMBO Mol Med 14 (10), e15859 (2022)
   PUBMED   35920001
  REMARK    GeneRIF: TOP3A amplification and ATRX inactivation are mutually
            exclusive events in pediatric osteosarcomas using ALT.
REFERENCE   5  (residues 1 to 1001)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1001)
  AUTHORS   Shimamoto,A., Nishikawa,K., Kitao,S. and Furuichi,Y.
  TITLE     Human RecQ5beta, a large isomer of RecQ5 DNA helicase, localizes in
            the nucleoplasm and interacts with topoisomerases 3alpha and 3beta
  JOURNAL   Nucleic Acids Res 28 (7), 1647-1655 (2000)
   PUBMED   10710432
REFERENCE   7  (residues 1 to 1001)
  AUTHORS   Goulaouic,H., Roulon,T., Flamand,O., Grondard,L., Lavelle,F. and
            Riou,J.F.
  TITLE     Purification and characterization of human DNA topoisomerase
            IIIalpha
  JOURNAL   Nucleic Acids Res 27 (12), 2443-2450 (1999)
   PUBMED   10352172
REFERENCE   8  (residues 1 to 1001)
  AUTHORS   Kim,J.C., Yoon,J.B., Koo,H.S. and Chung,I.K.
  TITLE     Cloning and characterization of the 5'-flanking region for the
            human topoisomerase III gene
  JOURNAL   J Biol Chem 273 (40), 26130-26137 (1998)
   PUBMED   9748294
REFERENCE   9  (residues 1 to 1001)
  AUTHORS   Fritz,E., Elsea,S.H., Patel,P.I. and Meyn,M.S.
  TITLE     Overexpression of a truncated human topoisomerase III partially
            corrects multiple aspects of the ataxia-telangiectasia phenotype
  JOURNAL   Proc Natl Acad Sci U S A 94 (9), 4538-4542 (1997)
   PUBMED   9114025
REFERENCE   10 (residues 1 to 1001)
  AUTHORS   Hanai,R., Caron,P.R. and Wang,J.C.
  TITLE     Human TOP3: a single-copy gene encoding DNA topoisomerase III
  JOURNAL   Proc Natl Acad Sci U S A 93 (8), 3653-3657 (1996)
   PUBMED   8622991
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM462184.1, BC051748.1,
            AF086042.1, AC127537.8 and AW294300.1.
            
            Summary: This gene encodes a DNA topoisomerase, an enzyme that
            controls and alters the topologic states of DNA during
            transcription. This enzyme catalyzes the transient breaking and
            rejoining of a single strand of DNA which allows the strands to
            pass through one another, thus reducing the number of supercoils
            and altering the topology of DNA. This enzyme forms a complex with
            BLM which functions in the regulation of recombination in somatic
            cells. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.82081.1,
                                           SRR1803611.50754.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321105.10/ ENSP00000321636.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..1001
                     /product="DNA topoisomerase 3-alpha isoform 1"
                     /EC_number="5.6.2.1"
                     /note="topo III-alpha; DNA topoisomerase 3-alpha; zinc
                     finger, GRF-type containing 7; topoisomerase (DNA) III
                     alpha"
                     /calculated_mol_wt=112242
     Region          35..193
                     /region_name="TOPRIM_TopoIA_TopoIII"
                     /note="The topoisomerase-primase (TORPIM) domain found in
                     members of the type IA family of DNA topoisomerases (Topo
                     IA) similar to topoisomerase III. Type IA DNA
                     topoisomerases remove (relax) negative supercoils in the
                     DNA by: cleaving one strand of the DNA...; cd03362"
                     /db_xref="CDD:173782"
     Site            order(41..42,45,148,150,152)
                     /site_type="active"
                     /db_xref="CDD:173782"
     Site            order(48,149,151,158..159,161..162)
                     /site_type="other"
                     /note="putative interdomain interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:173782"
     Site            order(148,150)
                     /site_type="other"
                     /note="putative metal-binding site [ion binding]"
                     /db_xref="CDD:173782"
     Site            151
                     /site_type="other"
                     /note="putative nucleotide binding site [chemical
                     binding]"
                     /db_xref="CDD:173782"
     Region          202..617
                     /region_name="TOP1Ac"
                     /note="DNA Topoisomerase, subtype IA; DNA-binding,
                     ATP-binding and catalytic domain of bacterial DNA
                     topoisomerases I and III, and eukaryotic DNA topoisomerase
                     III and eubacterial and archael reverse gyrases.
                     Topoisomerases clevage single or double stranded DNA...;
                     cd00186"
                     /db_xref="CDD:238110"
     Site            order(202..225,239..259)
                     /site_type="active"
                     /note="domain I [active]"
                     /db_xref="CDD:238110"
     Site            order(207..208,211,215,219,352,356,364,536..537,540..541,
                     543,547..548)
                     /site_type="DNA binding"
                     /note="DNA binding groove [nucleotide binding]"
                     /db_xref="CDD:238110"
     Site            order(250,254,573)
                     /site_type="other"
                     /note="phosphate binding site [ion binding]"
                     /db_xref="CDD:238110"
     Site            order(264..271,308..322,447..461,463..481,503..513)
                     /site_type="active"
                     /note="domain II [active]"
                     /db_xref="CDD:238110"
     Site            order(323..329,331..386,413..421,426..446)
                     /site_type="active"
                     /note="domain III [active]"
                     /db_xref="CDD:238110"
     Site            order(334,338..340,414,432,435,439,534,536,559)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:238110"
     Site            order(362,364,414)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:238110"
     Region          400..424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13472.1)"
     Site            order(514..554,559..573,579..617)
                     /site_type="active"
                     /note="domain IV [active]"
                     /db_xref="CDD:238110"
     Region          655..694
                     /region_name="zf-C4_Topoisom"
                     /note="Topoisomerase DNA binding C4 zinc finger;
                     pfam01396"
                     /db_xref="CDD:307520"
     Region          774..810
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13472.1)"
     Region          811..852
                     /region_name="zf-GRF"
                     /note="GRF zinc finger; pfam06839"
                     /db_xref="CDD:462017"
     Region          895..939
                     /region_name="zf-GRF"
                     /note="GRF zinc finger; pfam06839"
                     /db_xref="CDD:462017"
     Region          937..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13472.1)"
     CDS             1..1001
                     /gene="TOP3A"
                     /gene_synonym="MGRISCE2; PEOB5; TOP3; ZGRF7"
                     /coded_by="NM_004618.5:217..3222"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11194.1"
                     /db_xref="GeneID:7156"
                     /db_xref="HGNC:HGNC:11992"
                     /db_xref="MIM:601243"
ORIGIN      
        1 mifpvaryal rwlrrpedra fsraamemal rgvrkvlcva ekndaakgia dllsngrmrr
       61 reglskfnki yefdyhlygq nvtmvmtsvs ghllahdfqm qfrkwqscnp lvlfeaeiek
      121 ycpenfvdik ktleretrqc qalviwtdcd regenigfei ihvckavkpn lqvlrarfse
      181 itphavrtac enltepdqrv sdavdvrqel dlrigaaftr fqtlrlqrif pevlaeqlis
      241 ygscqfptlg fvverfkaiq afvpeifhri kvthdhkdgi vefnwkrhrl fnhtaclvly
      301 qlcvedpmat vvevrskpks kwrpqaldtv eleklasrkl rinaketmri aeklytqgyi
      361 syprtetnif prdlnltvlv eqqtpdprwg afaqsilerg gptprngnks dqahppihpt
      421 kytnnlqgde qrlyefivrh flaccsqdaq gqettveidi aqerfvahgl milarnyldv
      481 ypydhwsdki lpvyeqgshf qpstvemvdg etsppkllte adlialmekh gigtdathae
      541 hietikarmy vgltpdkrfl pghlgmglve gydsmgyems kpdlraelea dlklicdgkk
      601 dkfvvlrqqv qkykqvfiea vakakkldea laqyfgngte laqqediypa mpepirkcpq
      661 cnkdmvlktk knggfylscm gfpecrsavw lpdsvleasr dssvcpvcqp hpvyrlklkf
      721 krgslpptmp lefvcciggc ddtlreildl rfsggppras qpsgrlqanq slnrmdnsqh
      781 pqpadsrqtg sskalaqtlp pptaagesns vtcncgqeav lltvrkegpn rgrqffkcng
      841 gscnfflwad spnpgaggpp alayrplgas lgcppgpgih lggfgnpgdg sgsgtsclcs
      901 qpsvtrtvqk dgpnkgrqfh tcakpreqqc gffqwvdent apgtsgapsw tgdrgrtles
      961 earskrpras ssdmgstakk prkcslchqp ghtrpfcpqn r
//
LOCUS       NP_001353374             605 aa            linear   PRI 27-APR-2025
DEFINITION  rab GTPase-activating protein 1-like isoform F [Homo sapiens].
ACCESSION   NP_001353374
VERSION     NP_001353374.1
DBSOURCE    REFSEQ: accession NM_001366445.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 605)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 605)
  AUTHORS   Anttila,V., Winsvold,B.S., Gormley,P., Kurth,T., Bettella,F.,
            McMahon,G., Kallela,M., Malik,R., de Vries,B., Terwindt,G.,
            Medland,S.E., Todt,U., McArdle,W.L., Quaye,L., Koiranen,M.,
            Ikram,M.A., Lehtimaki,T., Stam,A.H., Ligthart,L., Wedenoja,J.,
            Dunham,I., Neale,B.M., Palta,P., Hamalainen,E., Schurks,M.,
            Rose,L.M., Buring,J.E., Ridker,P.M., Steinberg,S., Stefansson,H.,
            Jakobsson,F., Lawlor,D.A., Evans,D.M., Ring,S.M., Farkkila,M.,
            Artto,V., Kaunisto,M.A., Freilinger,T., Schoenen,J., Frants,R.R.,
            Pelzer,N., Weller,C.M., Zielman,R., Heath,A.C., Madden,P.A.F.,
            Montgomery,G.W., Martin,N.G., Borck,G., Gobel,H., Heinze,A.,
            Heinze-Kuhn,K., Williams,F.M.K., Hartikainen,A.L., Pouta,A., van
            den Ende,J., Uitterlinden,A.G., Hofman,A., Amin,N., Hottenga,J.J.,
            Vink,J.M., Heikkila,K., Alexander,M., Muller-Myhsok,B.,
            Schreiber,S., Meitinger,T., Wichmann,H.E., Aromaa,A.,
            Eriksson,J.G., Traynor,B., Trabzuni,D., Rossin,E., Lage,K.,
            Jacobs,S.B.R., Gibbs,J.R., Birney,E., Kaprio,J., Penninx,B.W.,
            Boomsma,D.I., van Duijn,C., Raitakari,O., Jarvelin,M.R.,
            Zwart,J.A., Cherkas,L., Strachan,D.P., Kubisch,C., Ferrari,M.D.,
            van den Maagdenberg,A.M.J.M., Dichgans,M., Wessman,M., Smith,G.D.,
            Stefansson,K., Daly,M.J., Nyholt,D.R., Chasman,D. and Palotie,A.
  CONSRTM   North American Brain Expression Consortium; UK Brain Expression
            Consortium
  TITLE     Genome-wide meta-analysis identifies new susceptibility loci for
            migraine
  JOURNAL   Nat Genet 45 (8), 912-917 (2013)
   PUBMED   23793025
REFERENCE   5  (residues 1 to 605)
  AUTHORS   Kim,J.H., Jung,S.H., Bae,J.S., Lee,H.S., Yim,S.H., Park,S.Y.,
            Bang,S.Y., Hu,H.J., Shin,H.D., Bae,S.C. and Chung,Y.J.
  TITLE     Deletion variants of RABGAP1L, 10q21.3, and C4 are associated with
            the risk of systemic lupus erythematosus in Korean women
  JOURNAL   Arthritis Rheum 65 (4), 1055-1063 (2013)
   PUBMED   23335107
  REMARK    GeneRIF: Deletion variants of RABGAP1L were found to be
            significantly associated with SLE in Korean women.
REFERENCE   6  (residues 1 to 605)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 605)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   8  (residues 1 to 605)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 605)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031286.2, AL022400.8, AL022171.1 and AL021069.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC041888.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1"
     Protein         1..605
                     /product="rab GTPase-activating protein 1-like isoform F"
                     /note="TBC1 domain family, member 18; expressed in
                     hematopoietic cells, heart, liver (HLL); rab
                     GTPase-activating protein 1-like"
                     /calculated_mol_wt=67872
     Region          92..220
                     /region_name="PTB_Rab6GAP"
                     /note="GTPase activating protein for Rab 6
                     Phosphotyrosine-binding (PTB) domain; cd01211"
                     /db_xref="CDD:269922"
     Site            order(98,176,196)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269922"
     Site            order(162..167,183,204,208)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269922"
     Region          253..384
                     /region_name="DUF3694"
                     /note="Kinesin protein; pfam12473"
                     /db_xref="CDD:463599"
     Region          498..>532
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..605
                     /gene="RABGAP1L"
                     /gene_synonym="HHL; TBC1D18"
                     /coded_by="NM_001366445.1:172..1989"
                     /note="isoform F is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS91110.1"
                     /db_xref="GeneID:9910"
                     /db_xref="HGNC:HGNC:24663"
                     /db_xref="MIM:609238"
ORIGIN      
        1 mevraslqki vsngdeqlek ameeilrdse krpssllvdc qssseisdhs fgdipasqtn
       61 kpslqlildp snteistprp sspgglpeed svlfnkltyl gcmkvssprn evealramat
      121 mksssqypfp vtlyvpnvpe gsvriidqss nveiasfpiy kvlfcarghd gttesncfaf
      181 tesshgseef qihvfsceik eavsrilysf ctafkrssrq vsdvkdsvip tpdsdvftfs
      241 vslevkeddg kgnfspvpkd rdkfyfklkq giekkvvitv qqlsnkelai ercfgmllsp
      301 grnvknsdmh lldmesmgks ydgrayvitg mwnpnapvfl alneetpkdk qvymtvavdm
      361 vvtevvepvr flletvvrvy panerfwyfs rktftetffm rlkqsegkgh tnagdaiyev
      421 vslqresdke epvtptsggg pmspqddeae eesdnelssg tgdvskdcpe kilyswgell
      481 gkwhsnlgar pkglstlvks gvpealraev wqllagchdn qamldryril itkqqmkfsl
      541 tprqtihlvk yegsmkvsmt pcnqlqfdir ldvlitytfc fssfpepely kyvlkhqlik
      601 rlnac
//
LOCUS       NP_056963                380 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-N-acetylneuraminate alpha-2,8-sialyltransferase ST8SIA3 [Homo
            sapiens].
ACCESSION   NP_056963 NP_059999
VERSION     NP_056963.2
DBSOURCE    REFSEQ: accession NM_015879.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Volkers,G., Worrall,L.J., Kwan,D.H., Yu,C.C., Baumann,L.,
            Lameignere,E., Wasney,G.A., Scott,N.E., Wakarchuk,W., Foster,L.J.,
            Withers,S.G. and Strynadka,N.C.
  TITLE     Structure of human ST8SiaIII sialyltransferase provides insight
            into cell-surface polysialylation
  JOURNAL   Nat Struct Mol Biol 22 (8), 627-635 (2015)
   PUBMED   26192331
  REMARK    GeneRIF: Data indicate that the crystal structure of ST8SiaIII
            sialyltransferase show a cluster of polysialyltransferase-specific
            structural motifs that provide an extended electropositive surface
            groove for binding of oligo-polysialic acid chain products.
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Kim,S.J., Chung,T.W., Jin,U.H., Suh,S.J., Lee,Y.C. and Kim,C.H.
  TITLE     Molecular mechanisms involved in transcriptional activation of the
            human Sia-alpha2,3-Gal-beta1,4-GlcNAc-R:alpha2,8-sialyltransferase
            (hST8Sia III) gene induced by KCl in human glioblastoma cells
  JOURNAL   Biochem Biophys Res Commun 344 (4), 1057-1064 (2006)
   PUBMED   16643848
  REMARK    GeneRIF: These results suggest that the expression of hST8Sia III
            gene via the PI-3K signaling pathway is enhanced during KCl-induced
            differentiation of U-87 cells by increasing expression of
            beta-tubulin III.
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Angata,K., Suzuki,M., McAuliffe,J., Ding,Y., Hindsgaul,O. and
            Fukuda,M.
  TITLE     Differential biosynthesis of polysialic acid on neural cell
            adhesion molecule (NCAM) and oligosaccharide acceptors by three
            distinct alpha 2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II
            (STX), and ST8Sia III
  JOURNAL   J Biol Chem 275 (24), 18594-18601 (2000)
   PUBMED   10766765
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Lee,Y.C., Kim,Y.J., Lee,K.Y., Kim,K.S., Kim,B.U., Kim,H.N.,
            Kim,C.H. and Do,S.I.
  TITLE     Cloning and expression of cDNA for a human Sia alpha 2,3Gal beta 1,
            4GlcNA:alpha 2,8-sialyltransferase (hST8Sia III)
  JOURNAL   Arch Biochem Biophys 360 (1), 41-46 (1998)
   PUBMED   9826427
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Zeng,G., Gao,L. and Yu,R.K.
  TITLE     Cloning of the cDNA coding for rat brain CMP-NeuAc:GD3 alpha2-8
            sialyltransferase
  JOURNAL   Gene 187 (1), 131-134 (1997)
   PUBMED   9073076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC090208.4 and AB208996.1.
            
            On Jul 28, 2006 this sequence version replaced NP_056963.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.8248.1,
                                           SRR1803615.56132.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324000.4/ ENSP00000320431.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.31"
     Protein         1..380
                     /product="alpha-N-acetylneuraminate
                     alpha-2,8-sialyltransferase ST8SIA3"
                     /EC_number="2.4.3.8"
                     /note="sialyltransferase 8C (alpha2,3Galbeta1,4GlcNAcalpha
                     2,8-sialyltransferase); alpha-2,8-sialyltransferase III;
                     sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha
                     2,8-sialyltransferase; SIAT8-C; sialytransferase St8Sia
                     III; alpha-2,8-sialyltransferase 8C; sialyltransferase
                     St8Sia III; ST8 alpha-N-acetylneuraminate
                     alpha-2,8-sialyltransferase 3; hST8Sia III; ganglioside
                     GD3 synthase ST8SIA3;
                     sia-a2,3-Gal-b1,4-Glc-NAc-R:a2,8-sialyltransferase"
                     /calculated_mol_wt=43839
     Site            10..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43173.3)"
     Region          92..376
                     /region_name="GT29_ST8SIA3_oligo"
                     /note="alpha-N-acetylneuraminide
                     alpha-2,8-sialyltransferase 3; cd23970"
                     /db_xref="CDD:467698"
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26192331, ECO:0000269|Ref.7,
                     ECO:0007744|PDB:5BO6, ECO:0007744|PDB:5BO8,
                     ECO:0007744|PDB:5BO9, ECO:0007744|PDB:5CXY; propagated
                     from UniProtKB/Swiss-Prot (O43173.3)"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26192331,
                     ECO:0007744|PDB:5BO9; propagated from UniProtKB/Swiss-Prot
                     (O43173.3)"
     Site            160
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26192331, ECO:0000269|Ref.7,
                     ECO:0007744|PDB:5BO6, ECO:0007744|PDB:5BO7,
                     ECO:0007744|PDB:5BO9, ECO:0007744|PDB:5CXY; propagated
                     from UniProtKB/Swiss-Prot (O43173.3)"
     Site            order(166..168,189..190,211,300..302,320..321,335..337,
                     354)
                     /site_type="active"
                     /db_xref="CDD:467698"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:26192331,
                     ECO:0007744|PDB:5BO6, ECO:0007744|PDB:5BO7,
                     ECO:0007744|PDB:5BO8, ECO:0007744|PDB:5BO9,
                     ECO:0007744|PDB:5CXY; propagated from UniProtKB/Swiss-Prot
                     (O43173.3)"
     CDS             1..380
                     /gene="ST8SIA3"
                     /gene_synonym="SIAT8C; ST8SiaIII"
                     /coded_by="NM_015879.3:291..1433"
                     /db_xref="CCDS:CCDS32834.1"
                     /db_xref="GeneID:51046"
                     /db_xref="HGNC:HGNC:14269"
                     /db_xref="MIM:609478"
ORIGIN      
        1 mrnckmarva svlglvmlsv allilslisy vslkkenift tpkyaspgap rmymfhagfr
       61 sqfalkfldp sfvpitnslt qelqekpskw kfnrtaflhq rqeilqhvdv iknfsltkns
      121 vrigqlmhyd ysshkyvfsi snnfrsllpd vspimnkhyn icavvgnsgi ltgsqcgqei
      181 dksdfvfrcn fapteafqrd vgrktnlttf npsilekyyn nlltiqdrnn fflslkkldg
      241 ailwipafff htsatvtrtl vdffvehrgq lkvqlawpgn imqhvnrywk nkhlspkrls
      301 tgilmytlas aiceeihlyg fwpfgfdpnt redlpyhyyd kkgtkfttkw qeshqlpaef
      361 qllyrmhgeg ltkltlshca
//
LOCUS       NP_776487                181 aa            linear   MAM 27-APR-2025
DEFINITION  ferritin heavy chain [Bos taurus].
ACCESSION   NP_776487
VERSION     NP_776487.1
DBSOURCE    REFSEQ: accession NM_174062.4
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Liu,J., Hu,Z., Ma,Q., Wang,S. and Liu,D.
  TITLE     Ferritin-dependent cellular autophagy pathway promotes ferroptosis
            in beef during cold storage
  JOURNAL   Food Chem 412, 135550 (2023)
   PUBMED   36706507
  REMARK    GeneRIF: Ferritin-dependent cellular autophagy pathway promotes
            ferroptosis in beef during cold storage.
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Roperto,S., Borzacchiello,G., Brun,R., Costanzo,F., Faniello,M.C.,
            Raso,C., Rosati,A., Russo,V., Leonardi,L., Saracino,D., Turco,M.C.,
            Urraro,C. and Roperto,F.
  TITLE     Ferritin heavy chain (FHC) is up-regulated in
            papillomavirus-associated urothelial tumours of the urinary bladder
            in cattle
  JOURNAL   J Comp Pathol 142 (1), 9-18 (2010)
   PUBMED   19596355
  REMARK    GeneRIF: ferritin heavy chain up-regulation may be mediated by
            activation of NF-kappaB and that in turn this may be related to the
            resistance of bovine papillomavirus type-2 (BPV-2) infected
            urothelial cells to apoptosis.
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Ishiwata,H., Katsuma,S., Kizaki,K., Patel,O.V., Nakano,H.,
            Takahashi,T., Imai,K., Hirasawa,A., Shiojima,S., Ikawa,H.,
            Suzuki,Y., Tsujimoto,G., Izaike,Y., Todoroki,J. and Hashizume,K.
  TITLE     Characterization of gene expression profiles in early bovine
            pregnancy using a custom cDNA microarray
  JOURNAL   Mol Reprod Dev 65 (1), 9-18 (2003)
   PUBMED   12658628
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105376.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5571260.23453.1, EH172388.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03145449, SAMN06299492
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="29"
                     /map="29"
                     /breed="mixed"
     Protein         1..181
                     /product="ferritin heavy chain"
                     /EC_number="1.16.3.1"
                     /note="ferritin H subunit; ferritin protein"
                     /calculated_mol_wt=20920
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P02794; propagated from
                     UniProtKB/Swiss-Prot (O46414.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in Ferritin heavy chain,
                     N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P02794; propagated from
                     UniProtKB/Swiss-Prot (O46414.3)"
     Region          14..174
                     /region_name="Euk_Ferritin"
                     /note="eukaryotic ferritins; cd01056"
                     /db_xref="CDD:153114"
     Site            order(28,35,62..63,66,108,142)
                     /site_type="other"
                     /note="ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153114"
     Site            order(58,61..62,65)
                     /site_type="active"
                     /note="ferrihydrite nucleation center [active]"
                     /db_xref="CDD:153114"
     Site            order(119,132,135)
                     /site_type="active"
                     /note="iron ion channel [active]"
                     /db_xref="CDD:153114"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02794; propagated from
                     UniProtKB/Swiss-Prot (O46414.3)"
     CDS             1..181
                     /gene="FTH1"
                     /gene_synonym="FTH"
                     /coded_by="NM_174062.4:218..763"
                     /db_xref="BGD:BT26964"
                     /db_xref="GeneID:281173"
                     /db_xref="VGNC:VGNC:56265"
ORIGIN      
        1 mttaspsqvr qnyhqdseaa inrqinlely asyvylsmsy yfdrddvalk nfakyflhqs
       61 heerehaerl mklqnqrggr iflqdikkpd rddwenglta mecalclers vnqsllelhk
      121 latekndphl cdfiethyln eqveaikelg dhitnlrkmg apgsgmaeyl fdkhtlghse
      181 s
//
LOCUS       NP_005863                225 aa            linear   PRI 27-APR-2025
DEFINITION  pre-mRNA-splicing factor SPF27 [Homo sapiens].
ACCESSION   NP_005863
VERSION     NP_005863.1
DBSOURCE    REFSEQ: accession NM_005872.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Yao,X., Wang,C., Sun,L., Yan,L., Chen,X., Lv,Z., Xie,X., Tian,S.,
            Liu,W., Li,L., Zhang,H. and Liu,J.
  TITLE     BCAS2 regulates granulosa cell survival by participating in mRNA
            alternative splicing
  JOURNAL   J Ovarian Res 16 (1), 104 (2023)
   PUBMED   37248466
  REMARK    GeneRIF: BCAS2 regulates granulosa cell survival by participating
            in mRNA alternative splicing.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Wang,L.P., Chen,T.Y., Kang,C.K., Huang,H.P. and Chen,S.L.
  TITLE     BCAS2, a protein enriched in advanced prostate cancer, interacts
            with NBS1 to enhance DNA double-strand break repair
  JOURNAL   Br J Cancer 123 (12), 1796-1807 (2020)
   PUBMED   32963349
  REMARK    GeneRIF: BCAS2, a protein enriched in advanced prostate cancer,
            interacts with NBS1 to enhance DNA double-strand break repair.
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Lee,S., Ha,S., Chung,M., Kim,Y. and Choi,Y.
  TITLE     Mouse DAM1 regulates pro-apoptotic activity of BLK in mammary
            epithelial cells
  JOURNAL   Cancer Lett 188 (1-2), 121-126 (2002)
   PUBMED   12406557
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Maass,N., Rosel,F., Schem,C., Hitomi,J., Jonat,W. and Nagasaki,K.
  TITLE     Amplification of the BCAS2 gene at chromosome 1p13.3-21 in human
            primary breast cancer
  JOURNAL   Cancer Lett 185 (2), 219-223 (2002)
   PUBMED   12169396
  REMARK    GeneRIF: The BCAS2 gene was amplified in two of 60 primary breast
            cancer tissues, but not in other cancer cells, providing the first
            evidence of amplification within this region and indicating that
            BCAS2 gene codes for a nuclear protein.
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Nagasaki,K., Maass,N., Manabe,T., Hanzawa,H., Tsukada,T.,
            Kikuchi,K. and Yamaguchi,K.
  TITLE     Identification of a novel gene, DAM1, amplified at chromosome
            1p13.3-21 region in human breast cancer cell lines
  JOURNAL   Cancer Lett 140 (1-2), 219-226 (1999)
   PUBMED   10403562
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF184377.1, BC039238.1 and BC022880.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC039238.1, AK222637.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369541.4/ ENSP00000358554.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..225
                     /product="pre-mRNA-splicing factor SPF27"
                     /note="spliceosome associated protein, amplified in breast
                     cancer; breast carcinoma amplified sequence 2;
                     spliceosome-associated protein SPF 27; DNA amplified in
                     mammary carcinoma 1 protein"
                     /calculated_mol_wt=26000
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (O75934.1)"
     Region          11..213
                     /region_name="BCAS2"
                     /note="Breast carcinoma amplified sequence 2 (BCAS2);
                     pfam05700"
                     /db_xref="CDD:428593"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75934.1)"
     CDS             1..225
                     /gene="BCAS2"
                     /gene_synonym="DAM1; Snt309; SPF27"
                     /coded_by="NM_005872.3:25..702"
                     /db_xref="CCDS:CCDS874.1"
                     /db_xref="GeneID:10286"
                     /db_xref="HGNC:HGNC:975"
                     /db_xref="MIM:605783"
ORIGIN      
        1 magtglvage vvvdalpyfd qgyeapgvre aaaalveeet rryrptknyl syltapdysa
       61 fetdimrnef erlaarqpie llsmkryelp apssgqkndi tawqecvnns maqlehqavr
      121 ienlelmsqh gcnawkvyne nlvhmiehaq kelqklrkhi qdlnwqrknm qltagsklre
      181 mesnwvslvs knyeiertiv qleneiyqik qqhgeanken irqdf
//
LOCUS       NP_001536                206 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein mL62 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001536
VERSION     NP_001536.1
DBSOURCE    REFSEQ: accession NM_001545.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Kummer,E., Schubert,K.N., Schoenhut,T., Scaiola,A. and Ban,N.
  TITLE     Structural basis of translation termination, rescue, and recycling
            in mammalian mitochondria
  JOURNAL   Mol Cell 81 (12), 2566-2582 (2021)
   PUBMED   33878294
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Pan,X., Tan,J., Weng,X., Du,R., Jiang,Y., Weng,Y., Zhou,D. and
            Shen,Y.
  TITLE     ICT1 Promotes Osteosarcoma Cell Proliferation and Inhibits
            Apoptosis via STAT3/BCL-2 Pathway
  JOURNAL   Biomed Res Int 2021, 8971728 (2021)
   PUBMED   33585660
  REMARK    GeneRIF: ICT1 Promotes Osteosarcoma Cell Proliferation and Inhibits
            Apoptosis via STAT3/BCL-2 Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Peng,X., Yan,B. and Shen,Y.
  TITLE     MiR-1301-3p inhibits human breast cancer cell proliferation by
            regulating cell cycle progression and apoptosis through directly
            targeting ICT1
  JOURNAL   Breast Cancer 25 (6), 742-752 (2018)
   PUBMED   29951881
  REMARK    GeneRIF: miR-1301-3p inhibits cell proliferation via inducing cell
            cycle arrest and apoptosis through targeting ICT1, and might be a
            therapeutic target for BC.
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Li,G.Y., Liu,J.Z., Zhang,L., Liu,G.Z., Li,S.J., Xiao,T.W.,
            Wang,J.X., Wang,L.X. and Hou,M.
  TITLE     Knockdown of immature colon carcinoma transcript 1 induces
            suppression of proliferation, S-phase arrest and apoptosis in
            leukemia cells
  JOURNAL   Oncol Rep 39 (3), 1269-1275 (2018)
   PUBMED   29328466
  REMARK    GeneRIF: High ICT1 expression is associated with leukemia.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Handa,Y., Hikawa,Y., Tochio,N., Kogure,H., Inoue,M., Koshiba,S.,
            Guntert,P., Inoue,Y., Kigawa,T., Yokoyama,S. and Nameki,N.
  TITLE     Solution structure of the catalytic domain of the mitochondrial
            protein ICT1 that is essential for cell vitality
  JOURNAL   J Mol Biol 404 (2), 260-273 (2010)
   PUBMED   20869366
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Antonicka,H., Ostergaard,E., Sasarman,F., Weraarpachai,W.,
            Wibrand,F., Pedersen,A.M., Rodenburg,R.J., van der Knaap,M.S.,
            Smeitink,J.A., Chrzanowska-Lightowlers,Z.M. and Shoubridge,E.A.
  TITLE     Mutations in C12orf65 in patients with encephalomyopathy and a
            mitochondrial translation defect
  JOURNAL   Am J Hum Genet 87 (1), 115-122 (2010)
   PUBMED   20598281
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Richter,R., Rorbach,J., Pajak,A., Smith,P.M., Wessels,H.J.,
            Huynen,M.A., Smeitink,J.A., Lightowlers,R.N. and
            Chrzanowska-Lightowlers,Z.M.
  TITLE     A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into
            the human mitochondrial ribosome
  JOURNAL   EMBO J 29 (6), 1116-1125 (2010)
   PUBMED   20186120
  REMARK    GeneRIF: ICT1 may be essential for hydrolysis of prematurely
            terminated peptidyl-tRNA moieties in stalled mitoribosomes.
REFERENCE   9  (residues 1 to 206)
  AUTHORS   van Belzen,N., Diesveld,M.P., van der Made,A.C., Nozawa,Y.,
            Dinjens,W.N., Vlietstra,R., Trapman,J. and Bosman,F.T.
  TITLE     Identification of mRNAs that show modulated expression during colon
            carcinoma cell differentiation
  JOURNAL   Eur J Biochem 234 (3), 843-848 (1995)
   PUBMED   8575443
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Bae,Y.M., Kim,T.J., Park,W.S., Chung,D.H., Choi,E.Y., Lee,G.K.,
            Song,H.G., Kim,C.W., Kim,B.K. and Ahn,H.S.
  TITLE     A novel T-cell differentiation antigen expressed in immature human
            thymocytes and neuroglial cells
  JOURNAL   Cell Immunol 165 (1), 118-124 (1995)
   PUBMED   7545548
  REMARK    Erratum:[Cell Immunol 1995 Dec;166(2):296]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB456649.1 and BC015335.1.
            
            Summary: The protein encoded by this gene is a peptidyl-tRNA
            hydrolase and a vital component of the large mitochondrial
            ribosome. The encoded protein serves as a ribosome release factor
            for this ribosome, which translates mitochondrial genes. This
            protein may be responsible for degrading prematurely-terminated
            polypeptides and for reusing stalled ribosomes. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the predominant isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.125951.1,
                                           SRR1163655.667687.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000301585.10/
                                                  ENSP00000301585.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..206
                     /product="large ribosomal subunit protein mL62 isoform 1
                     precursor"
                     /EC_number="3.1.1.29"
                     /note="immature colon carcinoma transcript 1 protein;
                     peptidyl-tRNA hydrolase ICT1, mitochondrial; digestion
                     substraction 1; 39S ribosomal protein L58, mitochondrial;
                     mitochondrial large ribosomal subunit protein ICT1;
                     mitochondrial large ribosomal subunit protein mL62"
                     /calculated_mol_wt=20385
     transit_peptide 1..29
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q14197.1)"
                     /calculated_mol_wt=3263
     mat_peptide     30..206
                     /product="Large ribosomal subunit protein mL62.
                     /id=PRO_0000030339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14197.1)"
                     /calculated_mol_wt=20385
     Region          72..202
                     /region_name="PRK09256"
                     /note="aminoacyl-tRNA hydrolase"
                     /db_xref="CDD:181730"
     Site            90
                     /site_type="methylation"
                     /note="N5-methylglutamine.
                     /evidence=ECO:0000269|PubMed:35260756; propagated from
                     UniProtKB/Swiss-Prot (Q14197.1)"
     CDS             1..206
                     /gene="MRPL58"
                     /gene_synonym="DS-1; DS1; ICT1; mL62; MRP-L58"
                     /coded_by="NM_001545.3:18..638"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS11711.1"
                     /db_xref="GeneID:3396"
                     /db_xref="HGNC:HGNC:5359"
                     /db_xref="MIM:603000"
ORIGIN      
        1 maatrclrwg lsragvwllp pparcprral hkqkdgtefk siysldklyp esqgsdtawr
       61 vpngakqads dipldrltis ycrssgpggq nvnkvnskae vrfhlataew iaepvrqkia
      121 ithknkinrl geliltsess ryqfrnladc lqkirdmite asqtpkeptk edvklhriri
      181 enmnrerlrq krihsavkts rrvdmd
//
LOCUS       NP_001124397             538 aa            linear   PRI 27-APR-2025
DEFINITION  syncytin-1 precursor [Homo sapiens].
ACCESSION   NP_001124397
VERSION     NP_001124397.1
DBSOURCE    REFSEQ: accession NM_001130925.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Zhang,D., Wu,X., Xue,X., Li,W., Zhou,P., Lv,Z., Zhao,K. and Zhu,F.
  TITLE     Ancient dormant virus remnant ERVW-1 drives ferroptosis via
            degradation of GPX4 and SLC3A2 in schizophrenia
  JOURNAL   Virol Sin 39 (1), 31-43 (2024)
   PUBMED   37690733
  REMARK    GeneRIF: Ancient dormant virus remnant ERVW-1 drives ferroptosis
            via degradation of GPX4 and SLC3A2 in schizophrenia.
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Xue,X., Wu,X., Liu,L., Liu,L. and Zhu,F.
  TITLE     ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by
            Decreasing GANAB in Recent-Onset Schizophrenia
  JOURNAL   Viruses 15 (6), 1298 (2023)
   PUBMED   37376599
  REMARK    GeneRIF: ERVW-1 Activates ATF6-Mediated Unfolded Protein Response
            by Decreasing GANAB in Recent-Onset Schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Talotta,R.
  TITLE     Interaction between Long Noncoding RNAs and Syncytin-1/Syncytin-2
            Genes and Transcripts: How Noncoding RNAs May Affect Pregnancy in
            Patients with Systemic Lupus Erythematosus
  JOURNAL   Int J Mol Sci 24 (3), 2259 (2023)
   PUBMED   36768581
  REMARK    GeneRIF: Interaction between Long Noncoding RNAs and
            Syncytin-1/Syncytin-2 Genes and Transcripts: How Noncoding RNAs May
            Affect Pregnancy in Patients with Systemic Lupus Erythematosus.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Yao,W., Zhou,P., Yan,Q., Wu,X., Xia,Y., Li,W., Li,X. and Zhu,F.
  TITLE     ERVWE1 Reduces Hippocampal Neuron Density and Impairs Dendritic
            Spine Morphology through Inhibiting Wnt/JNK Non-Canonical Pathway
            via miR-141-3p in Schizophrenia
  JOURNAL   Viruses 15 (1), 168 (2023)
   PUBMED   36680208
  REMARK    GeneRIF: ERVWE1 Reduces Hippocampal Neuron Density and Impairs
            Dendritic Spine Morphology through Inhibiting Wnt/JNK Non-Canonical
            Pathway via miR-141-3p in Schizophrenia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Zhuang,X., Qian,J., Xia,X., Wang,Y., Wang,H., Jing,L., Zhang,Y. and
            Zhang,Y.
  TITLE     Serum circulating free DNA of syncytin-1 as a novel molecular
            marker for early diagnosis of non-small-cell lung cancer
  JOURNAL   Biomark Med 16 (18), 1259-1268 (2022)
   PUBMED   36861469
  REMARK    GeneRIF: Serum circulating free DNA of syncytin-1 as a novel
            molecular marker for early diagnosis of non-small-cell lung cancer.
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Blond,J.L., Lavillette,D., Cheynet,V., Bouton,O., Oriol,G.,
            Chapel-Fernandes,S., Mandrand,B., Mallet,F. and Cosset,F.L.
  TITLE     An envelope glycoprotein of the human endogenous retrovirus HERV-W
            is expressed in the human placenta and fuses cells expressing the
            type D mammalian retrovirus receptor
  JOURNAL   J Virol 74 (7), 3321-3329 (2000)
   PUBMED   10708449
  REMARK    GeneRIF: Env HERV-W glycoprotein mediates cell-cell fusion upon
            interaction with the type D mammalian retrovirus receptor. Env
            protein was detected in the placental syncytiotrophoblast,
            suggesting a physiological role during pregnancy and placenta
            formation.
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Mi,S., Lee,X., Li,X., Veldman,G.M., Finnerty,H., Racie,L.,
            LaVallie,E., Tang,X.Y., Edouard,P., Howes,S., Keith,J.C. Jr. and
            McCoy,J.M.
  TITLE     Syncytin is a captive retroviral envelope protein involved in human
            placental morphogenesis
  JOURNAL   Nature 403 (6771), 785-789 (2000)
   PUBMED   10693809
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Voisset,C., Blancher,A., Perron,H., Mandrand,B., Mallet,F. and
            Paranhos-Baccala,G.
  TITLE     Phylogeny of a novel family of human endogenous retrovirus
            sequences, HERV-W, in humans and other primates
  JOURNAL   AIDS Res Hum Retroviruses 15 (17), 1529-1533 (1999)
   PUBMED   10580403
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Blond,J.L., Beseme,F., Duret,L., Bouton,O., Bedin,F., Perron,H.,
            Mandrand,B. and Mallet,F.
  TITLE     Molecular characterization and placental expression of HERV-W, a
            new human endogenous retrovirus family
  JOURNAL   J Virol 73 (2), 1175-1185 (1999)
   PUBMED   9882319
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Alliel,P.M., Perin,J.P., Pierig,R., Nussbaum,J.L., Menard,A. and
            Rieger,F.
  TITLE     Endogenous retroviruses and multiple sclerosis. II. HERV-7q
  JOURNAL   C R Acad Sci III 321 (10), 857-863 (1998)
   PUBMED   9835022
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007566.2, AF072506.2 and
            BC137381.1.
            
            Summary: Many different human endogenous retrovirus (HERV) families
            are expressed in normal placental tissue at high levels, suggesting
            that HERVs are functionally important in reproduction. This gene is
            part of an HERV provirus on chromosome 7 that has inactivating
            mutations in the gag and pol genes. This gene is the envelope
            glycoprotein gene which appears to have been selectively preserved.
            The gene's protein product is expressed in the placental
            syncytiotrophoblast and is involved in fusion of the
            cytotrophoblast cells to form the syncytial layer of the placenta.
            The protein has the characteristics of a typical retroviral
            envelope protein, including a furin cleavage site that separates
            the surface (SU) and transmembrane (TM) proteins which form a
            heterodimer. Alternatively spliced transcript variants encoding the
            same protein have been found for this gene. [provided by RefSeq,
            Mar 2010].
            
            Transcript Variant: This variant (2) has an alternate 5' UTR, as
            compared to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2162568
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            endogenous retrovirus  :: PMID: 10693809
            MANE Ensembl match     :: ENST00000603053.2/ ENSP00000474984.1
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..538
                     /product="syncytin-1 precursor"
                     /note="envelope glycoprotein; enverin; HERV-tryptophan
                     envelope protein; HERV-7q envelope protein; HERV-W Env
                     glycoprotein; HERV-W_7q21.2 provirus ancestral Env
                     polyprotein; human endogenous retrovirus W envC7-1
                     envelope protein; envelope polyprotein gPr73; syncytin-1;
                     endogenous retroviral family W, env(C7), member 1;
                     endogenous retrovirus group W, member 1; HERV-W envelope
                     protein"
                     /calculated_mol_wt=57560
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2325
     mat_peptide     21..538
                     /product="Syncytin-1. /id=PRO_0000008485"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
                     /calculated_mol_wt=57560
     mat_peptide     21..317
                     /product="Surface protein. /id=PRO_0000008486"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
                     /calculated_mol_wt=33252
     mat_peptide     22..538
                     /product="syncytin"
                     /calculated_mol_wt=57488
     Region          22..477
                     /region_name="TLV_coat"
                     /note="ENV polyprotein (coat polyprotein); pfam00429"
                     /db_xref="CDD:306850"
     Site            169
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Region          186..189
                     /region_name="CXXC. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Site            208
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Site            234
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Site            242
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Site            317..318
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000269|PubMed:15827173;
                     propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
     mat_peptide     318..538
                     /product="Transmembrane protein. /id=PRO_0000008487"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
                     /calculated_mol_wt=24325
     Region          320..340
                     /region_name="Fusion peptide. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Region          380..396
                     /region_name="Immunosuppression. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Region          397..406
                     /region_name="CX6CC. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Site            409
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Site            444..464
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Region          465..484
                     /region_name="Essential for the fusiogenic function"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
     Region          496..538
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF0.1)"
     CDS             1..538
                     /gene="ERVW-1"
                     /gene_synonym="ENV; ENVW; ERVWE1; HERV-7q; HERV-W-ENV;
                     HERV7Q; HERVW; HERVWENV"
                     /coded_by="NM_001130925.2:793..2409"
                     /db_xref="CCDS:CCDS5626.1"
                     /db_xref="GeneID:30816"
                     /db_xref="HGNC:HGNC:13525"
                     /db_xref="MIM:604659"
ORIGIN      
        1 malpyhiflf tvllpsftlt apppcrcmts sspyqeflwr mqrpgnidap syrslskgtp
       61 tftahthmpr ncyhsatlcm hanthywtgk minpscpggl gvtvcwtyft qtgmsdgggv
      121 qdqarekhvk evisqltrvh gtsspykgld lsklhetlrt htrlvslfnt tltglhevsa
      181 qnptncwicl plnfrpyvsi pvpeqwnnfs teinttsvlv gplvsnleit htsnltcvkf
      241 snttyttnsq cirwvtpptq ivclpsgiff vcgtsayrcl ngssesmcfl sflvppmtiy
      301 teqdlysyvi skprnkrvpi lpfvigagvl galgtgiggi ttstqfyykl sqelngdmer
      361 vadslvtlqd qlnslaavvl qnrraldllt aerggtclfl geeccyyvnq sgivtekvke
      421 irdriqrrae elrntgpwgl lsqwmpwilp flgplaaiil lllfgpcifn llvnfvssri
      481 eavklqmepk mqsktkiyrr pldrpasprs dvndikgtpp eeisaaqpll rpnsagss
//
LOCUS       NP_002431                936 aa            linear   PRI 27-APR-2025
DEFINITION  mutS protein homolog 4 [Homo sapiens].
ACCESSION   NP_002431
VERSION     NP_002431.2
DBSOURCE    REFSEQ: accession NM_002440.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Hashemi Sheikhshabani,S., Ghafouri-Fard,S., Hosseini,E. and
            Omrani,M.D.
  TITLE     A novel homozygote nonsense variant of MSH4 leads to primary
            ovarian insufficiency and non-obstructive azoospermia
  JOURNAL   Mol Biol Rep 51 (1), 68 (2024)
   PUBMED   38175272
  REMARK    GeneRIF: A novel homozygote nonsense variant of MSH4 leads to
            primary ovarian insufficiency and non-obstructive azoospermia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Wan,Y., Hong,Z., Ma,B., He,X., Ma,L., Wang,M. and Zhang,Y.
  TITLE     Identification of compound heterozygous variants in MSH4 as a novel
            genetic cause of diminished ovarian reserve
  JOURNAL   Reprod Biol Endocrinol 21 (1), 76 (2023)
   PUBMED   37620942
  REMARK    GeneRIF: Identification of compound heterozygous variants in MSH4
            as a novel genetic cause of diminished ovarian reserve.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 936)
  AUTHORS   Li,P., Ji,Z., Zhi,E., Zhang,Y., Han,S., Zhao,L., Tian,R., Chen,H.,
            Huang,Y., Zhang,J., Chen,H., Zhao,F., Zhou,Z., Li,Z. and Yao,C.
  TITLE     Novel bi-allelic MSH4 variants causes meiotic arrest and
            non-obstructive azoospermia
  JOURNAL   Reprod Biol Endocrinol 20 (1), 21 (2022)
   PUBMED   35090489
  REMARK    GeneRIF: Novel bi-allelic MSH4 variants causes meiotic arrest and
            non-obstructive azoospermia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 936)
  AUTHORS   Wyrwoll,M.J., van Walree,E.S., Hamer,G., Rotte,N., Motazacker,M.M.,
            Meijers-Heijboer,H., Alders,M., Meissner,A., Kaminsky,E., Woste,M.,
            Krallmann,C., Kliesch,S., Hunt,T.J., Clark,A.T., Silber,S.,
            Stallmeyer,B., Friedrich,C., van Pelt,A.M.M., Mathijssen,I.B. and
            Tuttelmann,F.
  TITLE     Bi-allelic variants in DNA mismatch repair proteins MutS Homolog
            MSH4 and MSH5 cause infertility in both sexes
  JOURNAL   Hum Reprod 37 (1), 178-189 (2021)
   PUBMED   34755185
  REMARK    GeneRIF: Bi-allelic variants in DNA mismatch repair proteins MutS
            Homolog MSH4 and MSH5 cause infertility in both sexes.
REFERENCE   5  (residues 1 to 936)
  AUTHORS   Akbari,A., Padidar,K., Salehi,N., Mashayekhi,M., Almadani,N.,
            Sadighi Gilani,M.A., Bashambou,A., McElreavey,K. and Totonchi,M.
  TITLE     Rare missense variant in MSH4 associated with primary gonadal
            failure in both 46, XX and 46, XY individuals
  JOURNAL   Hum Reprod 36 (4), 1134-1145 (2021)
   PUBMED   33448284
  REMARK    GeneRIF: Rare missense variant in MSH4 associated with primary
            gonadal failure in both 46, XX and 46, XY individuals.
REFERENCE   6  (residues 1 to 936)
  AUTHORS   Santucci-Darmanin,S., Walpita,D., Lespinasse,F., Desnuelle,C.,
            Ashley,T. and Paquis-Flucklinger,V.
  TITLE     MSH4 acts in conjunction with MLH1 during mammalian meiosis
  JOURNAL   FASEB J 14 (11), 1539-1547 (2000)
   PUBMED   10928988
REFERENCE   7  (residues 1 to 936)
  AUTHORS   Kneitz,B., Cohen,P.E., Avdievich,E., Zhu,L., Kane,M.F., Hou,H. Jr.,
            Kolodner,R.D., Kucherlapati,R., Pollard,J.W. and Edelmann,W.
  TITLE     MutS homolog 4 localization to meiotic chromosomes is required for
            chromosome pairing during meiosis in male and female mice
  JOURNAL   Genes Dev 14 (9), 1085-1097 (2000)
   PUBMED   10809667
REFERENCE   8  (residues 1 to 936)
  AUTHORS   Bocker,T., Barusevicius,A., Snowden,T., Rasio,D., Guerrette,S.,
            Robbins,D., Schmidt,C., Burczak,J., Croce,C.M., Copeland,T.,
            Kovatich,A.J. and Fishel,R.
  TITLE     hMSH5: a human MutS homologue that forms a novel heterodimer with
            hMSH4 and is expressed during spermatogenesis
  JOURNAL   Cancer Res 59 (4), 816-822 (1999)
   PUBMED   10029069
REFERENCE   9  (residues 1 to 936)
  AUTHORS   Winand,N.J., Panzer,J.A. and Kolodner,R.D.
  TITLE     Cloning and characterization of the human and Caenorhabditis
            elegans homologs of the Saccharomyces cerevisiae MSH5 gene
  JOURNAL   Genomics 53 (1), 69-80 (1998)
   PUBMED   9787078
REFERENCE   10 (residues 1 to 936)
  AUTHORS   Paquis-Flucklinger,V., Santucci-Darmanin,S., Paul,R., Saunieres,A.,
            Turc-Carel,C. and Desnuelle,C.
  TITLE     Cloning and expression analysis of a meiosis-specific MutS homolog:
            the human MSH4 gene
  JOURNAL   Genomics 44 (2), 188-194 (1997)
   PUBMED   9299235
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB077677.1, AF104243.1,
            BC033030.1 and AL445464.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 29, 2003 this sequence version replaced NP_002431.1.
            
            Summary: This gene encodes a member of the DNA mismatch repair mutS
            family. This member is a meiosis-specific protein that is not
            involved in DNA mismatch correction, but is required for reciprocal
            recombination and proper segregation of homologous chromosomes at
            meiosis I. This protein and MSH5 form a heterodimer which binds
            uniquely to a Holliday Junction and its developmental progenitor,
            thus provoking ADP-ATP exchange, and stabilizing the interaction
            between parental chromosomes during meiosis double-stranded break
            repair. [provided by RefSeq, Aug 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033030.1, U89293.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263187.4/ ENSP00000263187.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..936
                     /product="mutS protein homolog 4"
                     /note="hMSH4"
                     /calculated_mol_wt=104625
     Region          1..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15457.2)"
     Region          103..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15457.2)"
     Region          157..864
                     /region_name="MutS"
                     /note="DNA mismatch repair ATPase MutS [Replication,
                     recombination and repair]; COG0249"
                     /db_xref="CDD:440019"
     CDS             1..936
                     /gene="MSH4"
                     /gene_synonym="ASG; POF20; SPGF2"
                     /coded_by="NM_002440.4:105..2915"
                     /db_xref="CCDS:CCDS670.1"
                     /db_xref="GeneID:4438"
                     /db_xref="HGNC:HGNC:7327"
                     /db_xref="MIM:602105"
ORIGIN      
        1 mlrpeissts psapavspss getrspqgpr ynfglqetpq srpsvqvvsa stcpgtsgaa
       61 gdrssssssl pcpapnsrpa qgsyfgnkra yaentvasnf tfgassssar dtnypqtlkt
      121 plstgnpqrs gykswtpqvg ysassssais ahspsvivav vegrglarge igmasidlkn
      181 pqiilsqfad nttyakvitk lkilspleii msntacavgn stklftlite nfknvnftti
      241 qrkyfnetkg leyieqlcia efstvlmevq skyyclaava allkyvefiq nsvyapkslk
      301 icfqgseqta midsssaqnl ellinnqdyr nnhtlfgvln ytktpggsrr lrsnileplv
      361 dietinmrld cvqellqdee lffglqsvis rfldteqlls vlvqipkqdt vnaaeskitn
      421 liylkhtlel vdplkiamkn cntpllrayy gsledkrfgi ilekiktvin ddarymkgcl
      481 nmrtqkcyav rsninefldi arrtyteivd diagmisqlg ekyslplrts fssargffiq
      541 mttdcialps dqlpsefiki skvknsysft sadlikmner cqeslreiyh mtymivckll
      601 seiyehihcl yklsdtvsml dmllsfahac tlsdyvrpef tdtlaikqgw hpilekisae
      661 kpianntyvt egsnfliitg pnmsgkstyl kqialcqima qigsyvpaey ssfriakqif
      721 tristdddie tnsstfmkem keiayilhna ndkslilide lgrgtnteeg igicyavcey
      781 llslkaftlf athflelchi dalypnvenm hfevqhvknt srnkeailyt yklskgltee
      841 knyglkaaev sslppsivld akeittqitr qilqnqrstp emerqravyh latrlvqtar
      901 nsqldpdslr iylsnlkkky kedfprteqv pektee
//
LOCUS       NP_061147                701 aa            linear   PRI 27-APR-2025
DEFINITION  acetyl-coenzyme A synthetase, cytoplasmic isoform 1 [Homo sapiens].
ACCESSION   NP_061147
VERSION     NP_061147.1
DBSOURCE    REFSEQ: accession NM_018677.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Mochmann,L.H., Treue,D., Bockmayr,M., Silva,P., Zasada,C.,
            Mastrobuoni,G., Bayram,S., Forbes,M., Jurmeister,P., Liebig,S.,
            Blau,O., Schleich,K., Splettstoesser,B., Nordmann,T.M., von der
            Heide,E.K., Isaakidis,K., Schulze,V., Busch,C., Siddiq,H.,
            Schlee,C., Hester,S., Fransecky,L., Neumann,M., Kempa,S.,
            Klauschen,F. and Baldus,C.D.
  TITLE     Proteomic profiling reveals ACSS2 facilitating metabolic support in
            acute myeloid leukemia
  JOURNAL   Cancer Gene Ther 31 (9), 1344-1356 (2024)
   PUBMED   38851813
  REMARK    GeneRIF: Proteomic profiling reveals ACSS2 facilitating metabolic
            support in acute myeloid leukemia.
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Mukhi,D., Li,L., Liu,H., Doke,T., Kolligundla,L.P., Ha,E.,
            Kloetzer,K., Abedini,A., Mukherjee,S., Wu,J., Dhillon,P., Hu,H.,
            Guan,D., Funai,K., Uehara,K., Titchenell,P.M., Baur,J.A.,
            Wellen,K.E. and Susztak,K.
  TITLE     ACSS2 gene variants determine kidney disease risk by controlling de
            novo lipogenesis in kidney tubules
  JOURNAL   J Clin Invest 134 (4), e172963 (2023)
   PUBMED   38051585
  REMARK    GeneRIF: ACSS2 gene variants determine kidney disease risk by
            controlling de novo lipogenesis in kidney tubules.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Que,D., Kuang,F., Kang,R., Tang,D. and Liu,J.
  TITLE     ACSS2-mediated NF-kappaB activation promotes alkaliptosis in human
            pancreatic cancer cells
  JOURNAL   Sci Rep 13 (1), 1483 (2023)
   PUBMED   36707625
  REMARK    GeneRIF: ACSS2-mediated NF-kappaB activation promotes alkaliptosis
            in human pancreatic cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Zhou,Z., Ren,Y., Yang,J., Liu,M., Shi,X., Luo,W., Fung,K.M., Xu,C.,
            Bronze,M.S., Zhang,Y., Houchen,C.W. and Li,M.
  TITLE     Acetyl-Coenzyme A Synthetase 2 Potentiates Macropinocytosis and
            Muscle Wasting Through Metabolic Reprogramming in Pancreatic Cancer
  JOURNAL   Gastroenterology 163 (5), 1281-1293 (2022)
   PUBMED   35777482
  REMARK    GeneRIF: Acetyl-Coenzyme A Synthetase 2 Potentiates
            Macropinocytosis and Muscle Wasting Through Metabolic Reprogramming
            in Pancreatic Cancer.
REFERENCE   5  (residues 1 to 701)
  AUTHORS   Ciraku,L., Bacigalupa,Z.A., Ju,J., Moeller,R.A., Le Minh,G.,
            Lee,R.H., Smith,M.D., Ferrer,C.M., Trefely,S., Izzo,L.T.,
            Doan,M.T., Gocal,W.A., D'Agostino,L., Shi,W., Jackson,J.G.,
            Katsetos,C.D., Wellen,K.E., Snyder,N.W. and Reginato,M.J.
  TITLE     O-GlcNAc transferase regulates glioblastoma acetate metabolism via
            regulation of CDK5-dependent ACSS2 phosphorylation
  JOURNAL   Oncogene 41 (14), 2122-2136 (2022)
   PUBMED   35190642
  REMARK    GeneRIF: O-GlcNAc transferase regulates glioblastoma acetate
            metabolism via regulation of CDK5-dependent ACSS2 phosphorylation.
REFERENCE   6  (residues 1 to 701)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 701)
  AUTHORS   Yun,M., Bang,S.H., Kim,J.W., Park,J.Y., Kim,K.S. and Lee,J.D.
  TITLE     The importance of acetyl coenzyme A synthetase for 11C-acetate
            uptake and cell survival in hepatocellular carcinoma
  JOURNAL   J Nucl Med 50 (8), 1222-1228 (2009)
   PUBMED   19617323
  REMARK    GeneRIF: The patterns of (18)F-FDG and (11)C-acetate uptake seemed
            to complement each other in both human HCC and HCC cell lines.
REFERENCE   8  (residues 1 to 701)
  AUTHORS   Lu,Y., Dolle,M.E., Imholz,S., van 't Slot,R., Verschuren,W.M.,
            Wijmenga,C., Feskens,E.J. and Boer,J.M.
  TITLE     Multiple genetic variants along candidate pathways influence plasma
            high-density lipoprotein cholesterol concentrations
  JOURNAL   J Lipid Res 49 (12), 2582-2589 (2008)
   PUBMED   18660489
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 701)
  AUTHORS   Schwer,B., Bunkenborg,J., Verdin,R.O., Andersen,J.S. and Verdin,E.
  TITLE     Reversible lysine acetylation controls the activity of the
            mitochondrial enzyme acetyl-CoA synthetase 2
  JOURNAL   Proc Natl Acad Sci U S A 103 (27), 10224-10229 (2006)
   PUBMED   16788062
  REMARK    GeneRIF: Because the activity of a bacterial ortholog of AceCS2,
            called ACS, is controlled via deacetylation by a bacterial sirtuin
            protein, our observation highlights the conservation of a metabolic
            regulatory pathway from bacteria to humans
REFERENCE   10 (residues 1 to 701)
  AUTHORS   Luong,A., Hannah,V.C., Brown,M.S. and Goldstein,J.L.
  TITLE     Molecular characterization of human acetyl-CoA synthetase, an
            enzyme regulated by sterol regulatory element-binding proteins
  JOURNAL   J Biol Chem 275 (34), 26458-26466 (2000)
   PUBMED   10843999
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA411343.1 and BC073846.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a cytosolic enzyme that catalyzes the
            activation of acetate for use in lipid synthesis and energy
            generation. The protein acts as a monomer and produces acetyl-CoA
            from acetate in a reaction that requires ATP. Expression of this
            gene is regulated by sterol regulatory element-binding proteins,
            transcription factors that activate genes required for the
            synthesis of cholesterol and unsaturated fatty acids. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2009].
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK025990.1, BC012172.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360596.7/ ENSP00000353804.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..701
                     /product="acetyl-coenzyme A synthetase, cytoplasmic
                     isoform 1"
                     /EC_number="6.2.1.1"
                     /EC_number="6.2.1.17"
                     /note="acetyl-Coenzyme A synthetase 2 (ADP forming);
                     cytoplasmic acetyl-coenzyme A synthetase; acetate-CoA
                     ligase; acyl-activating enzyme; acetate thiokinase;
                     acetyl-coenzyme A synthetase, cytoplasmic; propionate--CoA
                     ligase; acetyl-CoA synthetase 1"
                     /calculated_mol_wt=78449
     Region          1..107
                     /region_name="Interaction with TFEB.
                     /evidence=ECO:0000269|PubMed:28552616"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR19.1)"
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NR19.1)"
     Region          45..685
                     /region_name="ACS"
                     /note="Acetyl-CoA synthetase (also known as acetate-CoA
                     ligase and acetyl-activating enzyme); cd05966"
                     /db_xref="CDD:341270"
     Site            order(191..193,219,222,224,357,362..363,385..387,411..412,
                     415,438..441,463..468,552,564,567,575..578,636,641..642)
                     /site_type="active"
                     /db_xref="CDD:341270"
     Site            order(191..193,219,222,224,357,363,385..387,411..412,415,
                     575..577,636,641)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341270"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXG4; propagated from
                     UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXG4; propagated from
                     UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            order(313,316..321,323..324)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341270"
     Site            order(362..363,438..441,463..468,552,564,567,578)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341270"
     Site            order(362..363,438..439,466)
                     /site_type="other"
                     /note="acetate binding site [chemical binding]"
                     /db_xref="CDD:341270"
     Site            418
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NR19.1)"
     Region          656..668
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:28552616"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:28552616; propagated from
                     UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            661
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXG4; propagated from
                     UniProtKB/Swiss-Prot (Q9NR19.1)"
     CDS             1..701
                     /gene="ACSS2"
                     /gene_synonym="ACAS2; ACECS; AceCS1; ACS; ACSA;
                     dJ1161H23.1"
                     /coded_by="NM_018677.4:35..2140"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13243.1"
                     /db_xref="GeneID:55902"
                     /db_xref="HGNC:HGNC:15814"
                     /db_xref="MIM:605832"
ORIGIN      
        1 mglpeervrs gsgsrgqeea gaggrarsws pppevsrsah vpslqryrel hrrsveepre
       61 fwgdiakefy wktpcpgpfl rynfdvtkgk ifiewmkgat tnicynvldr nvhekklgdk
      121 vafywegnep gettqityhq llvqvcqfsn vlrkqgiqkg drvaiympmi pelvvamlac
      181 arigalhsiv fagfsseslc erildsscsl littdafyrg eklvnlkela dealqkcqek
      241 gfpvrccivv khlgraelgm gdstsqsppi krscpdvqis wnqgidlwwh elmqeagdec
      301 epewcdaedp lfilytsgst gkpkgvvhtv ggymlyvatt fkyvfdfhae dvfwctadig
      361 witghsyvty gplangatsv lfegiptypd vnrlwsivdk ykvtkfytap tairllmkfg
      421 depvtkhsra slqvlgtvge pinpeawlwy hrvvgaqrcp ivdtfwqtet gghmltplpg
      481 atpmkpgsat fpffgvapai lnesgeeleg eaegylvfkq pwpgimrtvy gnherfetty
      541 fkkfpgyyvt gdgcqrdqdg yywitgridd mlnvsghlls taevesalve heavaeaavv
      601 ghphpvkgec lycfvtlcdg htfspkltee lkkqirekig piatpdyiqn apglpktrsg
      661 kimrrvlrki aqndhdlgdm stvadpsvis hlfshrclti q
//
LOCUS       NP_001307697             155 aa            linear   PRI 27-APR-2025
DEFINITION  cysteine and tyrosine-rich protein 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001307697 XP_011527751
VERSION     NP_001307697.2
DBSOURCE    REFSEQ: accession NM_001320768.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Perron,T., Boissan,M., Bieche,I., Courtois,L., Dingli,F., Loew,D.,
            Chouchene,M., Colasse,S., Levy,L. and Prunier,C.
  TITLE     CYYR1 promotes the degradation of the E3 ubiquitin ligase WWP1 and
            is associated with favorable prognosis in breast cancer
  JOURNAL   J Biol Chem 300 (9), 107601 (2024)
   PUBMED   39059493
  REMARK    GeneRIF: CYYR1 promotes the degradation of the E3 ubiquitin ligase
            WWP1 and is associated with favorable prognosis in breast cancer.
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Casadei,R., Pelleri,M.C., Vitale,L., Facchin,F., Canaider,S.,
            Strippoli,P., Vian,M., Piovesan,A., Bianconi,E., Mariani,E.,
            Piva,F. and Frabetti,F.
  TITLE     Characterization of human gene locus CYYR1: a complex
            multi-transcript system
  JOURNAL   Mol Biol Rep 41 (9), 6025-6038 (2014)
   PUBMED   24981926
  REMARK    GeneRIF: New CYYR1 alternative isoforms were identified and
            characterized.
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Wilk,J.B., Shrine,N.R., Loehr,L.R., Zhao,J.H., Manichaikul,A.,
            Lopez,L.M., Smith,A.V., Heckbert,S.R., Smolonska,J., Tang,W.,
            Loth,D.W., Curjuric,I., Hui,J., Cho,M.H., Latourelle,J.C.,
            Henry,A.P., Aldrich,M., Bakke,P., Beaty,T.H., Bentley,A.R.,
            Borecki,I.B., Brusselle,G.G., Burkart,K.M., Chen,T.H., Couper,D.,
            Crapo,J.D., Davies,G., Dupuis,J., Franceschini,N., Gulsvik,A.,
            Hancock,D.B., Harris,T.B., Hofman,A., Imboden,M., James,A.L.,
            Khaw,K.T., Lahousse,L., Launer,L.J., Litonjua,A., Liu,Y.,
            Lohman,K.K., Lomas,D.A., Lumley,T., Marciante,K.D., McArdle,W.L.,
            Meibohm,B., Morrison,A.C., Musk,A.W., Myers,R.H., North,K.E.,
            Postma,D.S., Psaty,B.M., Rich,S.S., Rivadeneira,F., Rochat,T.,
            Rotter,J.I., Soler Artigas,M., Starr,J.M., Uitterlinden,A.G.,
            Wareham,N.J., Wijmenga,C., Zanen,P., Province,M.A., Silverman,E.K.,
            Deary,I.J., Palmer,L.J., Cassano,P.A., Gudnason,V., Barr,R.G.,
            Loos,R.J., Strachan,D.P., London,S.J., Boezen,H.M.,
            Probst-Hensch,N., Gharib,S.A., Hall,I.P., O'Connor,G.T., Tobin,M.D.
            and Stricker,B.H.
  TITLE     Genome-wide association studies identify CHRNA5/3 and HTR4 in the
            development of airflow obstruction
  JOURNAL   Am J Respir Crit Care Med 186 (7), 622-632 (2012)
   PUBMED   22837378
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Vitale,L., Frabetti,F., Huntsman,S.A., Canaider,S., Casadei,R.,
            Lenzi,L., Facchin,F., Carinci,P., Zannotti,M., Coppola,D. and
            Strippoli,P.
  TITLE     Sequence, 'subtle' alternative splicing and expression of the CYYR1
            (cysteine/tyrosine-rich 1) mRNA in human neuroendocrine tumors
  JOURNAL   BMC Cancer 7, 66 (2007)
   PUBMED   17442112
  REMARK    GeneRIF: A new 'subtle' splicing isoform (CAG+) of CYYR1 mRNA, the
            sequence & expression of this gene were defined in a series of NE
            tumors. This CAG+ codon determines the presence of an Ala residue
            at the exon 3/exon 4 junction of the CYYR1 mRNA.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 155)
  AUTHORS   Reymond,A., Camargo,A.A., Deutsch,S., Stevenson,B.J.,
            Parmigiani,R.B., Ucla,C., Bettoni,F., Rossier,C., Lyle,R.,
            Guipponi,M., de Souza,S., Iseli,C., Jongeneel,C.V., Bucher,P.,
            Simpson,A.J. and Antonarakis,S.E.
  TITLE     Nineteen additional unpredicted transcripts from human chromosome
            21
  JOURNAL   Genomics 79 (6), 824-832 (2002)
   PUBMED   12036297
REFERENCE   6  (residues 1 to 155)
  AUTHORS   Vitale,L., Casadei,R., Canaider,S., Lenzi,L., Strippoli,P.,
            D'Addabbo,P., Giannone,S., Carinci,P. and Zannotti,M.
  TITLE     Cysteine and tyrosine-rich 1 (CYYR1), a novel unpredicted gene on
            human chromosome 21 (21q21.2), encodes a cysteine and tyrosine-rich
            protein and defines a new family of highly conserved
            vertebrate-specific genes
  JOURNAL   Gene 290 (1-2), 141-151 (2002)
   PUBMED   12062809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC382466.1, AK054581.1, AK223576.1, AF401639.1 and BX100308.1.
            
            On Nov 7, 2018 this sequence version replaced NP_001307697.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.138805.1,
                                           SRR1803611.28666.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000652641.2/
                                                ENSP00000498505.1
            RefSeq Select criteria           :: based on manual assertion,
                                                conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..155
                     /product="cysteine and tyrosine-rich protein 1 isoform 1
                     precursor"
                     /note="proline-rich domain-containing protein;
                     cysteine/tyrosine-rich 1"
                     /calculated_mol_wt=13520
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3196
     Region          7..155
                     /region_name="CYYR1"
                     /note="Cysteine and tyrosine-rich protein 1; pfam10873"
                     /db_xref="CDD:313948"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J86.1)"
     Region          125..155
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J86.1)"
     CDS             1..155
                     /gene="CYYR1"
                     /gene_synonym="C21orf95"
                     /coded_by="NM_001320768.2:347..814"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS93083.1"
                     /db_xref="GeneID:116159"
                     /db_xref="HGNC:HGNC:16274"
                     /db_xref="MIM:616020"
ORIGIN      
        1 mdaprlpvrp gvllpklvll fvyaddclaq cgkdcksycc dgttpyccsy yayignilsg
       61 taiagivfgi vfimgviagi aicicmcmkn hratrvgilr tthintvssy pagpppyghd
      121 hemeycadlp ppysptpqgp aqrsppppyp gnark
//
LOCUS       NP_443099               1738 aa            linear   PRI 27-APR-2025
DEFINITION  sodium leak channel NALCN isoform 2 [Homo sapiens].
ACCESSION   NP_443099
VERSION     NP_443099.1
DBSOURCE    REFSEQ: accession NM_052867.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1738)
  AUTHORS   Monteil,A., Guerineau,N.C., Gil-Nagel,A., Parra-Diaz,P., Lory,P.
            and Senatore,A.
  TITLE     New insights into the physiology and pathophysiology of the
            atypical sodium leak channel NALCN
  JOURNAL   Physiol Rev 104 (1), 399-472 (2024)
   PUBMED   37615954
  REMARK    GeneRIF: New insights into the physiology and pathophysiology of
            the atypical sodium leak channel NALCN.
            Review article
REFERENCE   2  (residues 1 to 1738)
  AUTHORS   Tehrani Fateh,S., Bagheri,S., Sadeghi,H., Salehpour,S., Fazeli
            Bavandpour,F., Sadeghi,B., Jamshidi,S., Tonekaboni,S.H.,
            Mirfakhraie,R., Miryounesi,M. and Ghasemi,M.R.
  TITLE     Extending and outlining the genotypic and phenotypic spectrum of
            novel mutations of NALCN gene in IHPRF1 syndrome: identifying
            recurrent urinary tract infection
  JOURNAL   Neurol Sci 44 (12), 4491-4498 (2023)
   PUBMED   37452996
  REMARK    GeneRIF: Extending and outlining the genotypic and phenotypic
            spectrum of novel mutations of NALCN gene in IHPRF1 syndrome:
            identifying recurrent urinary tract infection.
REFERENCE   3  (residues 1 to 1738)
  AUTHORS   Liao,Z., Liu,Y., Wang,Y., Lu,Q., Peng,Y. and Liu,Q.
  TITLE     Case Report: A de novo Variant in NALCN Associated With CLIFAHDD
            Syndrome in a Chinese Infant
  JOURNAL   Front Pediatr 10, 927392 (2022)
   PUBMED   35911839
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1738)
  AUTHORS   Kschonsak,M., Chua,H.C., Weidling,C., Chakouri,N., Noland,C.L.,
            Schott,K., Chang,T., Tam,C., Patel,N., Arthur,C.P., Leitner,A.,
            Ben-Johny,M., Ciferri,C., Pless,S.A. and Payandeh,J.
  TITLE     Structural architecture of the human NALCN channelosome
  JOURNAL   Nature 603 (7899), 180-186 (2022)
   PUBMED   34929720
  REMARK    GeneRIF: Structural architecture of the human NALCN channelosome.
REFERENCE   5  (residues 1 to 1738)
  AUTHORS   Xie,J., Ke,M., Xu,L., Lin,S., Huang,J., Zhang,J., Yang,F., Wu,J.
            and Yan,Z.
  TITLE     Structure of the human sodium leak channel NALCN in complex with
            FAM155A
  JOURNAL   Nat Commun 11 (1), 5831 (2020)
   PUBMED   33203861
  REMARK    GeneRIF: Structure of the human sodium leak channel NALCN in
            complex with FAM155A.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1738)
  AUTHORS   Cochet-Bissuel,M., Lory,P. and Monteil,A.
  TITLE     The sodium leak channel, NALCN, in health and disease
  JOURNAL   Front Cell Neurosci 8, 132 (2014)
   PUBMED   24904279
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1738)
  AUTHORS   Swayne,L.A., Mezghrani,A., Varrault,A., Chemin,J., Bertrand,G.,
            Dalle,S., Bourinet,E., Lory,P., Miller,R.J., Nargeot,J. and
            Monteil,A.
  TITLE     The NALCN ion channel is activated by M3 muscarinic receptors in a
            pancreatic beta-cell line
  JOURNAL   EMBO Rep 10 (8), 873-880 (2009)
   PUBMED   19575010
  REMARK    GeneRIF: Data show the molecular basis of a muscarinic-activated
            inward sodium current that is independent of G-protein activation,
            and provide new insights into the properties of NALCN channels.
REFERENCE   8  (residues 1 to 1738)
  AUTHORS   Wang,H. and Ren,D.
  TITLE     UNC80 functions as a scaffold for Src kinases in NALCN channel
            function
  JOURNAL   Channels (Austin) 3 (3), 161-163 (2009)
   PUBMED   19535918
  REMARK    GeneRIF: UNC80 functions as a scaffold for Src kinases in NALCN
            channel function.
REFERENCE   9  (residues 1 to 1738)
  AUTHORS   Lu,B., Su,Y., Das,S., Liu,J., Xia,J. and Ren,D.
  TITLE     The neuronal channel NALCN contributes resting sodium permeability
            and is required for normal respiratory rhythm
  JOURNAL   Cell 129 (2), 371-383 (2007)
   PUBMED   17448995
REFERENCE   10 (residues 1 to 1738)
  AUTHORS   Nash,H.A., Scott,R.L., Lear,B.C. and Allada,R.
  TITLE     An unusual cation channel mediates photic control of locomotion in
            Drosophila
  JOURNAL   Curr Biol 12 (24), 2152-2158 (2002)
   PUBMED   12498692
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356778.13, BC012128.1,
            AY141972.1, DA128114.1, AK002089.1 and BF516239.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a voltage-independent, nonselective
            cation channel which belongs to a family of voltage-gated sodium
            and calcium channels that regulates the resting membrane potential
            and excitability of neurons. This family is expressed throughout
            the nervous system and conducts a persistent sodium leak current
            that contributes to tonic neuronal excitability. The encoded
            protein forms a channelosome complex that includes
            G-protein-coupled receptors, UNC-79, UNC-80, NCA localization
            factor-1, and src family tyrosine kinases. Naturally occurring
            mutations in this gene are associated with infantile neuroaxonal
            dystrophy, infantile hypotonia with psychomotor retardation and
            characteristic facies (IHPRF) syndrome, and congenital contractures
            of the limbs and face with hypotonia and developmental delay
            (CLIFAHDD) syndrome. A knockout of the orthologous gene in mice
            results in paralysis with a severely disrupted respiratory rhythm,
            and lethality within 24 hours after birth. [provided by RefSeq, Apr
            2017].
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' coding region but maintains the reading frame, compared to
            variant 1. The encoded isoform (2) is shorter than isoform 1. Both
            variants 2 and 3 encode the same isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.4568.1,
                                           SRR1660809.21145.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000251127.11/ ENSP00000251127.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1738
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q32.3-q33.1"
     Protein         1..1738
                     /product="sodium leak channel NALCN isoform 2"
                     /note="voltage gated channel like 1; four repeat
                     voltage-gated ion channel; sodium leak channel NALCN"
                     /calculated_mol_wt=200201
     Region          36..331
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            66..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            107..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            174..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33203861,
                     ECO:0007744|PDB:7CM3; propagated from UniProtKB/Swiss-Prot
                     (Q8IZF0.1)"
     Site            216
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33203861,
                     ECO:0007744|PDB:7CM3; propagated from UniProtKB/Swiss-Prot
                     (Q8IZF0.1)"
     Site            295..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Region          383..603
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            417..439
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            448..468
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            473..492
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            503..530
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            570..599
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Region          762..785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Region          887..1161
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            887..906
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            916..939
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            948..972
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            981..1003
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            1016..1039
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            1064
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:32698188,
                     ECO:0000269|PubMed:33203861, ECO:0007744|PDB:6XIW,
                     ECO:0007744|PDB:7CM3; propagated from UniProtKB/Swiss-Prot
                     (Q8IZF0.1)"
     Site            1130..1159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Region          1209..1458
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1211..1227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            1237..1260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            1272..1293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            1297..1318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            1332..1357
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Site            1421..1447
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     Region          1611..1678
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF0.1)"
     CDS             1..1738
                     /gene="NALCN"
                     /gene_synonym="bA430M15.1; CanIon; CLIFAHDD; IHPRF;
                     IHPRF1; INNFD; VGCNL1"
                     /coded_by="NM_052867.4:236..5452"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9498.1"
                     /db_xref="GeneID:259232"
                     /db_xref="HGNC:HGNC:19082"
                     /db_xref="MIM:611549"
ORIGIN      
        1 mlkrkqssrv eaqpvtdfgp deslsdnadi lwinkpwvhs llricaiisv isvcmntpmt
       61 fehypplqyv tftldtllmf lytaemiakm hirgivkgds syvkdrwcvf dgfmvfclwv
      121 slvlqvfeia divdqmspwg mlriprplim irafriyfrf elprtritni lkrsgeqiws
      181 vsifllffll lygilgvqmf gtftyhcvvn dtkpgnvtwn slaipdthcs peleegyqcp
      241 pgfkcmdled lglsrqelgy sgfneigtsi ftvyeaasqe gwvflmyrai dsfprwrsyf
      301 yfitliffla wlvknvfiav iietfaeirv qfqqmwgsrs sttstattqm fhedaaggwq
      361 lvavdvnkpq grapaclqkm mrssvfhmfi lsmvtvdviv aasnyykgen frrqydefyl
      421 aevaftvlfd leallkiwcl gftgyisssl hkfelllvig ttlhvypdly hsqftyfqvl
      481 rvvrlikisp aledfvykif gpgkklgslv vftasllivm saislqmfcf veeldrfttf
      541 prafmsmfqi ltqegwvdvm dqtlnavghm wapvvaiyfi lyhlfatlil lslfvavild
      601 nleldedlkk lkqlkqsean adtkeklplr lrifekfpnr pqmvkisklp sdftvpkire
      661 sfmkqfidrq qqdtccllrs lpttsssscd hskrsaiedn kyidqklrks vfsirarnll
      721 eketavtkil ractrqrmls gsfegqpake rsilsvqhhi rqerrslrhg snsqrisrgk
      781 sletltqdhs ntvryrnaqr edseikmiqe kkeqaemkrk vqeeelrenh pyfdkplfiv
      841 grehrfrnfc rvvvrarfna sktdpvtgav kntkyhqlyd llglvtyldw vmiivticsc
      901 ismmfespfr rvmhaptlqi aeyvfvifms ielnlkimad glfftptavi rdfggvmdif
      961 iylvsliflc wmpqnvpaes gaqllmvlrc lrplrifklv pqmrkvvrel fsgfkeiflv
     1021 sillltlmlv fasfgvqlfa gklakcndpn iirredcngi frinvsvskn lnlklrpgek
     1081 kpgfwvprvw anprnfnfdn vgnamlalfe vlslkgwvev rdviihrvgp ihgiyihvfv
     1141 flgcmigltl fvgvvianfn enkgtalltv dqrrwedlks rlkiaqplhl pprpdndgfr
     1201 akmyditqhp ffkrtiallv laqsvllsvk wdvedpvtvp latmsvvftf ifvlevtmki
     1261 iamspagfwq srrnrydllv tslgvvwvvl hfallnayty mmgacvivfr ffsicgkhvt
     1321 lkmllltvvv smyksffiiv gmfllllcya fagvvlfgtv kygeninrha nfssagkait
     1381 vlfrivtged wnkimhdcmv qppfctpdef tywatdcgny agalmyfcsf yviiayimln
     1441 llvaiivenf slfysteedq llsyndlrhf qiiwnmvddk regviptfrv kfllrllrgr
     1501 levdldkdkl lfkhmcyeme rlhnggdvtf hdvlsmlsyr svdirkslql eellareqle
     1561 ytieeevakq tirmwlkkcl krirakqqqs csiihslres qqqelsrfln ppsiettqps
     1621 edtnansqdn smqpetssqq qllsptlsdr ggsrqdaada gkpqrkfgqw rlpsapkpis
     1681 hsvssvnlrf ggrttmksvv ckmnpmtdaa scgsevkkww trqltvesde sgddlldi
//
LOCUS       NP_150232                465 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM15 [Homo sapiens].
ACCESSION   NP_150232
VERSION     NP_150232.2
DBSOURCE    REFSEQ: accession NM_033229.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Yang,C., Jin,X., Liu,X., Wu,G., Yang,W., Pang,B., Jiang,J., Liao,D.
            and Zhang,Y.
  TITLE     TRIM15 forms a regulatory loop with the AKT/FOXO1 axis and LASP1 to
            modulate the sensitivity of HCC cells to TKIs
  JOURNAL   Cell Death Dis 14 (1), 47 (2023)
   PUBMED   36670097
  REMARK    GeneRIF: TRIM15 forms a regulatory loop with the AKT/FOXO1 axis and
            LASP1 to modulate the sensitivity of HCC cells to TKIs.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Liang,M., Wang,L., Sun,Z., Chen,X., Wang,H., Qin,L., Zhao,W. and
            Geng,B.
  TITLE     E3 ligase TRIM15 facilitates non-small cell lung cancer progression
            through mediating Keap1-Nrf2 signaling pathway
  JOURNAL   Cell Commun Signal 20 (1), 62 (2022)
   PUBMED   35534896
  REMARK    GeneRIF: E3 ligase TRIM15 facilitates non-small cell lung cancer
            progression through mediating Keap1-Nrf2 signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Roy,M., Singh,K., Shinde,A., Singh,J., Mane,M., Bedekar,S.,
            Tailor,Y., Gohel,D., Vasiyani,H., Currim,F. and Singh,R.
  TITLE     TNF-alpha-induced E3 ligase, TRIM15 inhibits TNF-alpha-regulated
            NF-kappaB pathway by promoting turnover of K63 linked
            ubiquitination of TAK1
  JOURNAL   Cell Signal 91, 110210 (2022)
   PUBMED   34871740
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Zhu,G., Herlyn,M. and Yang,X.
  TITLE     TRIM15 and CYLD regulate ERK activation via lysine-63-linked
            polyubiquitination
  JOURNAL   Nat Cell Biol 23 (9), 978-991 (2021)
   PUBMED   34497368
  REMARK    GeneRIF: TRIM15 and CYLD regulate ERK activation via
            lysine-63-linked polyubiquitination.
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Zhang,L., Qin,B., Zou,B., Wang,S., Quan,X., Wang,J. and Zhao,H.
  TITLE     Knockdown of TRIM15 inhibits the proliferation, migration and
            invasion of esophageal squamous cell carcinoma cells through
            inactivation of the Wnt/beta-catenin signaling pathway
  JOURNAL   J Bioenerg Biomembr 53 (2), 213-222 (2021)
   PUBMED   33515345
  REMARK    GeneRIF: Knockdown of TRIM15 inhibits the proliferation, migration
            and invasion of esophageal squamous cell carcinoma cells through
            inactivation of the Wnt/beta-catenin signaling pathway.
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Shiina,T., Ota,M., Shimizu,S., Katsuyama,Y., Hashimoto,N.,
            Takasu,M., Anzai,T., Kulski,J.K., Kikkawa,E., Naruse,T., Kimura,N.,
            Yanagiya,K., Watanabe,A., Hosomichi,K., Kohara,S., Iwamoto,C.,
            Umehara,Y., Meyer,A., Wanner,V., Sano,K., Macquin,C., Ikeo,K.,
            Tokunaga,K., Gojobori,T., Inoko,H. and Bahram,S.
  TITLE     Rapid evolution of major histocompatibility complex class I genes
            in primates generates new disease alleles in humans via hitchhiking
            diversity
  JOURNAL   Genetics 173 (3), 1555-1570 (2006)
   PUBMED   16702430
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Harada,H., Harada,Y., O'Brien,D.P., Rice,D.S., Naeve,C.W. and
            Downing,J.R.
  TITLE     HERF1, a novel hematopoiesis-specific RING finger protein, is
            required for terminal differentiation of erythroid cells
  JOURNAL   Mol Cell Biol 19 (5), 3808-3815 (1999)
   PUBMED   10207104
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Gruen,J.R., Nalabolu,S.R., Chu,T.W., Bowlus,C., Fan,W.F.,
            Goei,V.L., Wei,H., Sivakamasundari,R., Liu,Y., Xu,H.X., Parimoo,S.,
            Nallur,G., Ajioka,R., Shukla,H., Bray-Ward,P., Pan,J. and
            Weissman,S.M.
  TITLE     A transcription map of the major histocompatibility complex (MHC)
            class I region
  JOURNAL   Genomics 36 (1), 70-85 (1996)
   PUBMED   8812418
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Goei,V.L., Parimoo,S., Capossela,A., Chu,T.W. and Gruen,J.R.
  TITLE     Isolation of novel non-HLA gene fragments from the hemochromatosis
            region (6p21.3) by cDNA hybridization selection
  JOURNAL   Am J Hum Genet 54 (2), 244-251 (1994)
   PUBMED   8304341
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP270476.1, AL669914.2,
            BC038585.1, U34249.1 and AI739162.1.
            
            On Jun 20, 2007 this sequence version replaced NP_150232.1.
            
            Summary: The protein encoded by this gene is a member of the
            tripartite motif (TRIM) family. The TRIM motif includes three
            zinc-binding domains, a RING, a B-box type 1 and a B-box type 2,
            and a coiled-coil region. The protein localizes to the cytoplasm.
            Alternatively spliced transcript variants have been described, but
            their biological validity has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038585.1, U34249.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376694.9/ ENSP00000365884.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..465
                     /product="E3 ubiquitin-protein ligase TRIM15"
                     /EC_number="2.3.2.27"
                     /note="zinc finger protein 178; tripartite
                     motif-containing protein 15; RING finger protein 93; zinc
                     finger protein B7"
                     /calculated_mol_wt=51982
     Region          13..64
                     /region_name="RING-HC_SHPRH-like"
                     /note="RING finger, HC subclass, found in SNF2
                     histone-linker PHD finger RING finger helicase (SHPRH) and
                     similar proteins; cd16569"
                     /db_xref="CDD:438231"
     Region          81..119
                     /region_name="Bbox2_TRIM10-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins, TRIM10, TRIM15, TRIM26, TRIM31
                     and similar proteins; cd19765"
                     /db_xref="CDD:380823"
     Region          <121..>241
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          295..464
                     /region_name="SPRY_PRY_TRIM15"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     15 (TRIM15); cd15826"
                     /db_xref="CDD:293998"
     CDS             1..465
                     /gene="TRIM15"
                     /gene_synonym="RNF93; ZNF178; ZNFB7"
                     /coded_by="NM_033229.3:140..1537"
                     /db_xref="CCDS:CCDS4677.1"
                     /db_xref="GeneID:89870"
                     /db_xref="HGNC:HGNC:16284"
ORIGIN      
        1 mpatpslkvv helpactlca gpledavtip cghtfcrlcl palsqmgaqs sgkillcplc
       61 qeeeqaetpm apvplgplge tyceehgeki yffcendaef lcvfcregpt hqahtvgfld
      121 eaiqpyrdrl rsrlealste rdeiedvkcq edqklqvllt qieskkhqve taferlqqel
      181 eqqrclllar lreleqqiwk erdeyitkvs eevtrlgaqv keleekcqqp asellqdvrv
      241 nqsrcemktf vspeaispdl vkkirdfhrk iltlpemmrm fsenlahhle idsgvitldp
      301 qtasrslvls edrksvrytr qkkslpdspl rfdglpavlg fpgfssgrhr wqvdlqlgdg
      361 ggctvgvage gvrrkgemgl saedgvwavi ishqqcwast spgtdlplse iprgvrvald
      421 yeagqvtlhn aqtqepiftf tasfsgkvfp ffavwkkgsc ltlkg
//
LOCUS       NP_443179               2170 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-protein kinase 2 [Homo sapiens].
ACCESSION   NP_443179
VERSION     NP_443179.3
DBSOURCE    REFSEQ: accession NM_052947.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2170)
  AUTHORS   Yan,J.S., Chen,Q., Li,Y.L. and Gao,Y.Q.
  TITLE     Hsa_circ_0065217 promotes growth and metastasis of renal cancer
            through regulating the miR-214-3p-ALPK2 axis
  JOURNAL   Cell Cycle 20 (23), 2519-2530 (2021)
   PUBMED   34705617
  REMARK    GeneRIF: Hsa_circ_0065217 promotes growth and metastasis of renal
            cancer through regulating the miR-214-3p-ALPK2 axis.
REFERENCE   2  (residues 1 to 2170)
  AUTHORS   Wang,Y., Wu,J., Luo,W., Zhang,H., Shi,G., Shen,Y., Zhu,Y., Ma,C.,
            Dai,B., Ye,D. and Zhu,Y.
  TITLE     ALPK2 acts as tumor promotor in development of bladder cancer
            through targeting DEPDC1A
  JOURNAL   Cell Death Dis 12 (7), 661 (2021)
   PUBMED   34210956
  REMARK    GeneRIF: ALPK2 acts as tumor promotor in development of bladder
            cancer through targeting DEPDC1A.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2170)
  AUTHORS   McIntosh,A.T., Wei,R., Ahn,J., Aouizerat,B.E., Kassaye,S.G.,
            Augenbraun,M.H., Price,J.C., French,A.L., Gange,S.J., Anastos,K.M.
            and Goldman,R.
  TITLE     A genomic variant of ALPK2 is associated with increased liver
            fibrosis risk in HIV/HCV coinfected women
  JOURNAL   PLoS One 16 (3), e0247277 (2021)
   PUBMED   33705408
  REMARK    GeneRIF: A genomic variant of ALPK2 is associated with increased
            liver fibrosis risk in HIV/HCV coinfected women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2170)
  AUTHORS   Jiang,J., Han,P., Qian,J., Zhang,S., Wang,S., Cao,Q. and Shao,P.
  TITLE     Knockdown of ALPK2 blocks development and progression of renal cell
            carcinoma
  JOURNAL   Exp Cell Res 392 (2), 112029 (2020)
   PUBMED   32330508
  REMARK    GeneRIF: Knockdown of ALPK2 blocks development and progression of
            renal cell carcinoma.
REFERENCE   5  (residues 1 to 2170)
  AUTHORS   Hofsteen,P., Robitaille,A.M., Strash,N., Palpant,N., Moon,R.T.,
            Pabon,L. and Murry,C.E.
  TITLE     ALPK2 Promotes Cardiogenesis in Zebrafish and Human Pluripotent
            Stem Cells
  JOURNAL   iScience 2, 88-100 (2018)
   PUBMED   29888752
REFERENCE   6  (residues 1 to 2170)
  AUTHORS   Nishi,K., Luo,H., Nakabayashi,K., Doi,K., Ishikura,S., Iwaihara,Y.,
            Yoshida,Y., Tanisawa,K., Arai,T., Mori,S., Sawabe,M., Muramatsu,M.,
            Tanaka,M., Sakata,T., Shirasawa,S. and Tsunoda,T.
  TITLE     An Alpha-kinase 2 Gene Variant Disrupts Filamentous Actin
            Localization in the Surface Cells of Colorectal Cancer Spheroids
  JOURNAL   Anticancer Res 37 (7), 3855-3862 (2017)
   PUBMED   28668886
  REMARK    GeneRIF: Results showed that p.Q1853E variant of ALPK2, which had
            been accumulating in the Japanese population, induced a metastatic
            phenotype of colorectal tumors by disrupting ALPK2 function.
REFERENCE   7  (residues 1 to 2170)
  AUTHORS   Yoshida,Y., Tsunoda,T., Doi,K., Fujimoto,T., Tanaka,Y., Ota,T.,
            Ogawa,M., Matsuzaki,H., Kuroki,M., Iwasaki,A. and Shirasawa,S.
  TITLE     ALPK2 is crucial for luminal apoptosis and DNA repair-related gene
            expression in a three-dimensional colonic-crypt model
  JOURNAL   Anticancer Res 32 (6), 2301-2308 (2012)
   PUBMED   22641666
  REMARK    GeneRIF: ALPK2 is crucial for luminal apoptosis and expression of
            DNA repair-related genes, possibly in the transition of normal
            colonic crypt to adenoma.
REFERENCE   8  (residues 1 to 2170)
  AUTHORS   Sawcer,S., Hellenthal,G., Pirinen,M., Spencer,C.C.,
            Patsopoulos,N.A., Moutsianas,L., Dilthey,A., Su,Z., Freeman,C.,
            Hunt,S.E., Edkins,S., Gray,E., Booth,D.R., Potter,S.C., Goris,A.,
            Band,G., Oturai,A.B., Strange,A., Saarela,J., Bellenguez,C.,
            Fontaine,B., Gillman,M., Hemmer,B., Gwilliam,R., Zipp,F.,
            Jayakumar,A., Martin,R., Leslie,S., Hawkins,S., Giannoulatou,E.,
            D'alfonso,S., Blackburn,H., Martinelli Boneschi,F., Liddle,J.,
            Harbo,H.F., Perez,M.L., Spurkland,A., Waller,M.J., Mycko,M.P.,
            Ricketts,M., Comabella,M., Hammond,N., Kockum,I., McCann,O.T.,
            Ban,M., Whittaker,P., Kemppinen,A., Weston,P., Hawkins,C.,
            Widaa,S., Zajicek,J., Dronov,S., Robertson,N., Bumpstead,S.J.,
            Barcellos,L.F., Ravindrarajah,R., Abraham,R., Alfredsson,L.,
            Ardlie,K., Aubin,C., Baker,A., Baker,K., Baranzini,S.E.,
            Bergamaschi,L., Bergamaschi,R., Bernstein,A., Berthele,A.,
            Boggild,M., Bradfield,J.P., Brassat,D., Broadley,S.A., Buck,D.,
            Butzkueven,H., Capra,R., Carroll,W.M., Cavalla,P., Celius,E.G.,
            Cepok,S., Chiavacci,R., Clerget-Darpoux,F., Clysters,K., Comi,G.,
            Cossburn,M., Cournu-Rebeix,I., Cox,M.B., Cozen,W., Cree,B.A.,
            Cross,A.H., Cusi,D., Daly,M.J., Davis,E., de Bakker,P.I.,
            Debouverie,M., D'hooghe,M.B., Dixon,K., Dobosi,R., Dubois,B.,
            Ellinghaus,D., Elovaara,I., Esposito,F., Fontenille,C., Foote,S.,
            Franke,A., Galimberti,D., Ghezzi,A., Glessner,J., Gomez,R.,
            Gout,O., Graham,C., Grant,S.F., Guerini,F.R., Hakonarson,H.,
            Hall,P., Hamsten,A., Hartung,H.P., Heard,R.N., Heath,S., Hobart,J.,
            Hoshi,M., Infante-Duarte,C., Ingram,G., Ingram,W., Islam,T.,
            Jagodic,M., Kabesch,M., Kermode,A.G., Kilpatrick,T.J., Kim,C.,
            Klopp,N., Koivisto,K., Larsson,M., Lathrop,M., Lechner-Scott,J.S.,
            Leone,M.A., Leppa,V., Liljedahl,U., Bomfim,I.L., Lincoln,R.R.,
            Link,J., Liu,J., Lorentzen,A.R., Lupoli,S., Macciardi,F., Mack,T.,
            Marriott,M., Martinelli,V., Mason,D., McCauley,J.L., Mentch,F.,
            Mero,I.L., Mihalova,T., Montalban,X., Mottershead,J., Myhr,K.M.,
            Naldi,P., Ollier,W., Page,A., Palotie,A., Pelletier,J., Piccio,L.,
            Pickersgill,T., Piehl,F., Pobywajlo,S., Quach,H.L., Ramsay,P.P.,
            Reunanen,M., Reynolds,R., Rioux,J.D., Rodegher,M., Roesner,S.,
            Rubio,J.P., Ruckert,I.M., Salvetti,M., Salvi,E., Santaniello,A.,
            Schaefer,C.A., Schreiber,S., Schulze,C., Scott,R.J., Sellebjerg,F.,
            Selmaj,K.W., Sexton,D., Shen,L., Simms-Acuna,B., Skidmore,S.,
            Sleiman,P.M., Smestad,C., Sorensen,P.S., Sondergaard,H.B.,
            Stankovich,J., Strange,R.C., Sulonen,A.M., Sundqvist,E.,
            Syvanen,A.C., Taddeo,F., Taylor,B., Blackwell,J.M., Tienari,P.,
            Bramon,E., Tourbah,A., Brown,M.A., Tronczynska,E., Casas,J.P.,
            Tubridy,N., Corvin,A., Vickery,J., Jankowski,J., Villoslada,P.,
            Markus,H.S., Wang,K., Mathew,C.G., Wason,J., Palmer,C.N.,
            Wichmann,H.E., Plomin,R., Willoughby,E., Rautanen,A.,
            Winkelmann,J., Wittig,M., Trembath,R.C., Yaouanq,J.,
            Viswanathan,A.C., Zhang,H., Wood,N.W., Zuvich,R., Deloukas,P.,
            Langford,C., Duncanson,A., Oksenberg,J.R., Pericak-Vance,M.A.,
            Haines,J.L., Olsson,T., Hillert,J., Ivinson,A.J., De Jager,P.L.,
            Peltonen,L., Stewart,G.J., Hafler,D.A., Hauser,S.L., McVean,G.,
            Donnelly,P. and Compston,A.
  CONSRTM   International Multiple Sclerosis Genetics Consortium; Wellcome
            Trust Case Control Consortium 2
  TITLE     Genetic risk and a primary role for cell-mediated immune mechanisms
            in multiple sclerosis
  JOURNAL   Nature 476 (7359), 214-219 (2011)
   PUBMED   21833088
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2170)
  AUTHORS   McDonough,C.W., Bostrom,M.A., Lu,L., Hicks,P.J., Langefeld,C.D.,
            Divers,J., Mychaleckyj,J.C., Freedman,B.I. and Bowden,D.W.
  TITLE     Genetic analysis of diabetic nephropathy on chromosome 18 in
            African Americans: linkage analysis and dense SNP mapping
  JOURNAL   Hum Genet 126 (6), 805-817 (2009)
   PUBMED   19690890
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 2170)
  AUTHORS   Ryazanov,A.G., Pavur,K.S. and Dorovkov,M.V.
  TITLE     Alpha-kinases: a new class of protein kinases with a novel
            catalytic domain
  JOURNAL   Curr Biol 9 (2), R43-R45 (1999)
   PUBMED   10021370
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104971.5 and AC105105.10.
            
            On Jun 5, 2007 this sequence version replaced NP_443179.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647796.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361673.4/ ENSP00000354991.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.31-q21.32"
     Protein         1..2170
                     /product="alpha-protein kinase 2"
                     /EC_number="2.7.11.1"
                     /note="heart alpha-kinase; heart alpha-protein kinase"
                     /calculated_mol_wt=236883
     Region          12..105
                     /region_name="IgI_titin_I1-like"
                     /note="Immunoglobulin domain I1 of the titin I-band and
                     similar proteins; a member of the I-set of IgSF domains;
                     cd20951"
                     /db_xref="CDD:409543"
     Region          12..14
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409543"
     Region          16..22
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409543"
     Region          29..36
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409543"
     Region          42..47
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409543"
     Region          49..52
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409543"
     Region          60..64
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409543"
     Region          69..76
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409543"
     Region          83..91
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409543"
     Region          94..105
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409543"
     Region          109..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          241..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          287..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          455..475
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          520..634
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          703..732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          924..974
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          1124..1190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          1297..1323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          1340..1378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          1414..1442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          1499..1537
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          1591..1613
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          1679..1722
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          1759..1784
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     Region          1802..1874
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          1804..1808
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1818..1822
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1855..1860
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1867..1870
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1887..2125
                     /region_name="Alpha_kinase_ALPK2"
                     /note="Alpha-kinase domain of alpha-protein kinase 2;
                     cd16974"
                     /db_xref="CDD:341224"
     Site            order(1926..1931,1933,1953,1955,2012,2030..2033,2080,2082,
                     2090)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:341224"
     Region          2136..2170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB3.3)"
     CDS             1..2170
                     /gene="ALPK2"
                     /gene_synonym="HAK"
                     /coded_by="NM_052947.4:349..6861"
                     /db_xref="CCDS:CCDS11966.2"
                     /db_xref="GeneID:115701"
                     /db_xref="HGNC:HGNC:20565"
                     /db_xref="MIM:619965"
ORIGIN      
        1 mkdsegpqrp plcflstlls qkvpeksdav lrciisgqpk pevtwykngq aidgsgiisn
       61 yeffenqyih vlhlscctkn daavyqisak nsfgmiccsa svevecssen pqlspnledd
      121 rdrgwkhetg theeeranqi dekehpykee esispgtprs adsspsksnh slslqslgnl
      181 disvsssenp lgvkgtrhtg eaydpsntee iangllflns shiyekqdrc chktvhsmas
      241 kftdgdlnnd gphdeglrss qqnpkvqkyi sfslplseat ahiypgdsav ankqpspqls
      301 sedsdsdyel cpeitltyte efsdddleyl ecsdvmtdys navwqrnllg tehvfllesd
      361 deemefgehc lggcehflsg mgcgsrvsgd agpmvatagf cghhsqpqev gvrssrvskh
      421 gpsspqtgmt lilgphqdgt ssvteqgryk lptapeaaen dypgiqgetr dshqareefa
      481 sdnllnmdes vretemklls gesensgmsq cwetaadkrv ggkdlwskrg srksarvrqp
      541 gmkgnpkkpn anlrestteg tlhlcsakes aeppltqsdk retshttaaa tgrsshadar
      601 ecaistqaeq eaktlqtstd svskegntnc kgegmqvntl fetsqvpdws dppqvqvqet
      661 vretiscsqm pafsepagee spftgtttis fsnlggvhke naslaqhsev kpctcgpqhe
      721 ekqdrdgnip dnfredlkye qsiseandet mspgvfsrhl pkdaradfre pvavsvaspe
      781 ptdtaltlen vcdeprdrea vcamecfeag dqgtcfdtid slvgrpvdky spqeicsvdt
      841 elaegqnkvs dlcssndktl evffqtqvse tsvstckssk dgnsvmsplf tstftlnish
      901 tasegatgen lakvenstyp lastvhagqe qpspsnsggl detqllssen nplvqfkegg
      961 dkspspsaad ttatpasyss ivsfpwekpt tltannecfq atretedtst vtiatevhpa
     1021 kylavsiped khaggteerf prashekvsq fpsqvqldhi lsgatikstk ellcrapsvp
     1081 gvphhvlqlp egegfcsnsp lqvdnlsgdk sqtvdradfr syeenfqerg setkqgvqqq
     1141 slsqqgslsa pdfqqslptt saaqeernlv ptahspassr egagqrsgwg trvsvvaeta
     1201 geedsqalsn vpslsdille eskeyrpgnw eagnklkiit leasaseiwp prqltnsesk
     1261 asdggliipd kvwavpdslk adavvpelap seiaalahsp edaesalads reshkgeept
     1321 isvhwrslss rgfsqprlle ssvdpvdeke lsvtdslsaa setggkenvn nvsqdqeekq
     1381 lkmdhtaffk kfltcpkile ssvdpideis vieytragkp epsettpqga reggqsndgn
     1441 mgheaeiqpa ilqvpclqgt ilsenrisrs qegsmkqeae qiqpeeakta iwqvlqpseg
     1501 geripsgcsi gqiqessdgs lgeaeqskkd kaelisptsp lssclpimth aslgvdthns
     1561 tgqihdvpen diveprkrqy vfpvsqkrgt ienergkplp sspdltrfpc tsspegnvtd
     1621 flishkmeep kievlqiget kppssssssa ktlafisger elekapkllq dpcqkgtlgc
     1681 akksrereks learagkspg tltavtgsee vkrkpeapgs ghlaegvkkk ilsrvaalrl
     1741 kleekenirk nsaflkkmpk letslshtee kqdpkkpsck regrapvllk kiqaemfpeh
     1801 sgnvklscqf aeihedstic wtkdsksiaq vqrsagdnst vsfaivqasp kdqglyycci
     1861 knsygkvtae fnltaevlkq lssrqdtkgc eeiefsqlif kedflhdsyf ggrlrgqiat
     1921 eelhfgegvh rkafrstvmh glmpvfkpgh acvlkvhnai aygtrnndel iqrnyklaaq
     1981 ecyvqntary yakiyaaeaq plegfgevpe iipiflihrp ennipyatve eeligefvky
     2041 sirdgkeinf lrreseagqk cctfqhwvyq ktsgcllvtd mqgvgmkltd vgiatlakgy
     2101 kgfkgncsmt fidqfkalhq cnkyckmlgl kslqnnnqkq kqpsigkskv qtnsmtikka
     2161 gpetpgekkt
//
LOCUS       NP_004377               1321 aa            linear   PRI 27-APR-2025
DEFINITION  neurocan core protein precursor [Homo sapiens].
ACCESSION   NP_004377
VERSION     NP_004377.2
DBSOURCE    REFSEQ: accession NM_004386.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1321)
  AUTHORS   Assmann,A., Richter,A., Schutze,H., Soch,J., Barman,A.,
            Behnisch,G., Knopf,L., Raschick,M., Schult,A., Wustenberg,T.,
            Behr,J., Duzel,E., Seidenbecher,C.I. and Schott,B.H.
  TITLE     Neurocan genome-wide psychiatric risk variant affects explicit
            memory performance and hippocampal function in healthy humans
  JOURNAL   Eur J Neurosci 53 (12), 3942-3959 (2021)
   PUBMED   32583466
  REMARK    GeneRIF: Neurocan genome-wide psychiatric risk variant affects
            explicit memory performance and hippocampal function in healthy
            humans.
REFERENCE   2  (residues 1 to 1321)
  AUTHORS   Wu,M.J., Yuan,C., Lu,L.L., An,B.Q., Xuan,S.Y. and Xin,Y.N.
  TITLE     Role of NCAN rs2228603 polymorphism in the incidence of
            nonalcoholic fatty liver disease: a case-control study
  JOURNAL   Lipids Health Dis 15 (1), 207 (2016)
   PUBMED   27887608
  REMARK    GeneRIF: NCAN rs2228603 is not a risk factor for the incidence of
            NAFLD in Chinese population. The dual and opposite role of T
            variant in protecting liver with a higher level of HDL was found.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1321)
  AUTHORS   Boonvisut,S., Nakayama,K., Makishima,S., Watanabe,K., Miyashita,H.,
            Lkhagvasuren,M., Kagawa,Y. and Iwamoto,S.
  TITLE     Replication analysis of genetic association of the NCAN-CILP2
            region with plasma lipid levels and non-alcoholic fatty liver
            disease in Asian and Pacific ethnic groups
  JOURNAL   Lipids Health Dis 15, 8 (2016)
   PUBMED   26758378
  REMARK    GeneRIF: This study aims to analyze the influences of
            single-nucleotide polymorphism in the NCAN-CILP2 region on
            non-alcoholic fatty liver disease and plasma lipid levels in the
            Asian and Pacific ethnic groups.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1321)
  AUTHORS   Dannlowski,U., Kugel,H., Grotegerd,D., Redlich,R., Suchy,J.,
            Opel,N., Suslow,T., Konrad,C., Ohrmann,P., Bauer,J., Kircher,T.,
            Krug,A., Jansen,A., Baune,B.T., Heindel,W., Domschke,K.,
            Forstner,A.J., Nothen,M.M., Treutlein,J., Arolt,V., Hohoff,C.,
            Rietschel,M. and Witt,S.H.
  TITLE     NCAN Cross-Disorder Risk Variant Is Associated With Limbic Gray
            Matter Deficits in Healthy Subjects and Major Depression
  JOURNAL   Neuropsychopharmacology 40 (11), 2510-2516 (2015)
   PUBMED   25801500
  REMARK    GeneRIF: NCAN genotype is associated with limbic gray matter
            alterations in healthy and subjects with major depression in brain
            areas implicated in emotion perception and regulation
REFERENCE   5  (residues 1 to 1321)
  AUTHORS   Raum,H., Dietsche,B., Nagels,A., Witt,S.H., Rietschel,M.,
            Kircher,T. and Krug,A.
  TITLE     A genome-wide supported psychiatric risk variant in NCAN influences
            brain function and cognitive performance in healthy subjects
  JOURNAL   Hum Brain Mapp 36 (1), 378-390 (2015)
   PUBMED   25220293
  REMARK    GeneRIF: current data demonstrate that common genetic variation in
            NCAN influences both neural processing and cognitive performance in
            healthy subjects.
REFERENCE   6  (residues 1 to 1321)
  AUTHORS   Retzler,C., Gohring,W. and Rauch,U.
  TITLE     Analysis of neurocan structures interacting with the neural cell
            adhesion molecule N-CAM
  JOURNAL   J Biol Chem 271 (44), 27304-27310 (1996)
   PUBMED   8910306
REFERENCE   7  (residues 1 to 1321)
  AUTHORS   Milev,P., Maurel,P., Haring,M., Margolis,R.K. and Margolis,R.U.
  TITLE     TAG-1/axonin-1 is a high-affinity ligand of neurocan,
            phosphacan/protein-tyrosine phosphatase-zeta/beta, and N-CAM
  JOURNAL   J Biol Chem 271 (26), 15716-15723 (1996)
   PUBMED   8663515
REFERENCE   8  (residues 1 to 1321)
  AUTHORS   Rauch,U., Grimpe,B., Kulbe,G., Arnold-Ammer,I., Beier,D.R. and
            Fassler,R.
  TITLE     Structure and chromosomal localization of the mouse neurocan gene
  JOURNAL   Genomics 28 (3), 405-410 (1995)
   PUBMED   7490074
REFERENCE   9  (residues 1 to 1321)
  AUTHORS   Friedlander,D.R., Milev,P., Karthikeyan,L., Margolis,R.K.,
            Margolis,R.U. and Grumet,M.
  TITLE     The neuronal chondroitin sulfate proteoglycan neurocan binds to the
            neural cell adhesion molecules Ng-CAM/L1/NILE and N-CAM, and
            inhibits neuronal adhesion and neurite outgrowth
  JOURNAL   J Cell Biol 125 (3), 669-680 (1994)
   PUBMED   7513709
REFERENCE   10 (residues 1 to 1321)
  AUTHORS   Rauch,U., Karthikeyan,L., Maurel,P., Margolis,R.U. and
            Margolis,R.K.
  TITLE     Cloning and primary structure of neurocan, a developmentally
            regulated, aggregating chondroitin sulfate proteoglycan of brain
  JOURNAL   J Biol Chem 267 (27), 19536-19547 (1992)
   PUBMED   1326557
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC003110.1, CN282070.1, AB210004.1 and AC138430.2.
            
            On Dec 2, 2006 this sequence version replaced NP_004377.1.
            
            Summary: Neurocan is a chondroitin sulfate proteoglycan thought to
            be involved in the modulation of cell adhesion and
            migration.[supplied by OMIM, Jul 2002].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB210004.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252575.11/ ENSP00000252575.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1321
                     /product="neurocan core protein precursor"
                     /note="chondroitin sulfate proteoglycan 3 (neurocan);
                     neurocan proteoglycan; neurocan core protein"
                     /calculated_mol_wt=140733
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2379
     mat_peptide     23..1321
                     /product="Neurocan core protein. /id=PRO_0000017516"
                     /note="propagated from UniProtKB/Swiss-Prot (O14594.3)"
                     /calculated_mol_wt=140733
     Region          41..162
                     /region_name="Ig_Neurocan"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), neurocan;
                     cd05902"
                     /db_xref="CDD:409483"
     Region          41..44
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409483"
     Region          47..49
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409483"
     Region          53..61
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409483"
     Region          75..81
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409483"
     Region          90..93
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409483"
     Region          111..116
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409483"
     Region          122..128
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409483"
     Site            122
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14594.3)"
     Region          136..143
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409483"
     Region          153..162
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409483"
     Region          160..254
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            170..171
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Region          261..356
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan...; cd03520"
                     /db_xref="CDD:239597"
     Site            268..269
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Site            340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14594.3)"
     Region          362..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14594.3)"
     Site            381
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:25326458; propagated from
                     UniProtKB/Swiss-Prot (O14594.3)"
     Site            411
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:25326458; propagated from
                     UniProtKB/Swiss-Prot (O14594.3)"
     Region          <421..964
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          456..479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14594.3)"
     Region          494..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14594.3)"
     Region          532..579
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14594.3)"
     Region          682..731
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14594.3)"
     Region          708..712
                     /region_name="O-glycosylated at one site"
                     /note="propagated from UniProtKB/Swiss-Prot (O14594.3)"
     Region          820..844
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14594.3)"
     Region          876..955
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14594.3)"
     Region          1012..1042
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Site            1026
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14594.3)"
     Region          1046..1082
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1046,1049,1063)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1088..1211
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:470576"
     Site            order(1182,1186,1188,1194,1196..1199,1202..1204)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          1215..1271
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            1223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14594.3)"
     Site            order(1225,1245)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          1275..1321
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14594.3)"
     CDS             1..1321
                     /gene="NCAN"
                     /gene_synonym="CSPG3"
                     /coded_by="NM_004386.3:115..4080"
                     /db_xref="CCDS:CCDS12397.1"
                     /db_xref="GeneID:1463"
                     /db_xref="HGNC:HGNC:2465"
                     /db_xref="MIM:600826"
ORIGIN      
        1 mgapfvwalg llmlqmllfv ageqgtqdit daserglhmq klgsgsvqaa laelvalpcl
       61 ftlqprpsaa rdaprikwtk vrtasgqrqd lpilvakdnv vrvakswqgr vslpsyprrr
      121 anatlllgpl rasdsglyrc qvvrgiedeq dlvplevtgv vfhyrsardr yaltfaeaqe
      181 acrlssaiia aprhlqaafe dgfdncdagw lsdrtvrypi tqsrpgcygd rsslpgvrsy
      241 grrnpqelyd vycfarelgg evfyvgparr ltlagaraqc rrqgaalasv gqlhlawheg
      301 ldqcdpgwla dgsvrypiqt prrrcggpap gvrtvyrfan rtgfpspaer fdaycfrahh
      361 ptsqhgdlet pssgdegeil saegppvrel eptleeeevv tpdfqeplvs sgeeetlile
      421 ekqesqqtls ptpgdpmlas wptgevwlst vapspsdmga gtaasshtev aptdpmprrr
      481 grfkglngry fqqqepepgl qggmeasaqp ptseaavnqm epplamavte mlgsgqsrsp
      541 wadltnevdm pgagsaggks spepwlwppt mvppsisghs rapvleleka egpsarpatp
      601 dlfwspleat vsapspapwe afpvatspdl pmmamlrgpk ewmlphptpi steanrveah
      661 geatatapps paaetkvysl plsltptgqg geampttpes pradfretge tspaqvnkae
      721 hsssspwpsv nrnvavgfvp tetateptgl rgipgsesgv fdtaesptsg lqatvdevqd
      781 pwpsvyskgl dasspsaplg spgvflvpkv tpnlepwvat degptvnpmd stvtpapsda
      841 sgiwepgsqv feeaesttls pqvaldtsiv tplttleqgd kvgvpamstl gssssqphpe
      901 pedqvetqgt sgasvpphqs splgkpavpp gtptaasvge sasvssgept vpwdpsstll
      961 pvtlgiedfe levlagspgv esfweevasg eepalpgtpm nagaeevhsd pcennpclhg
     1021 gtcnangtmy gcscdqgfag enceididdc lcspcenggt cidevngfvc lclpsyggsf
     1081 cekdtegcdr gwhkfqghcy ryfahrrawe daekdcrrrs ghltsvhspe ehsfinsfgh
     1141 entwiglndr iverdfqwtd ntglqfenwr enqpdnffag gedcvvmvah esgrwndvpc
     1201 nynlpyvckk gtvlcgpppa venasligar kakynvhatv ryqcnegfaq hhvatircrs
     1261 ngkwdrpqiv ctkprrshrm rrhhhhhqhh hqhhhhksrk errkhkkhpt edwekdegnf
     1321 c
//
LOCUS       NP_001349336             133 aa            linear   ROD 27-APR-2025
DEFINITION  beta-synuclein [Mus musculus].
ACCESSION   NP_001349336 XP_006517079
VERSION     NP_001349336.1
DBSOURCE    REFSEQ: accession NM_001362407.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Zhong,W., Yang,Q., Wang,F., Lin,X., Chen,Z., Xue,J., Zhao,W.,
            Liu,X., Rao,B. and Zhang,J.
  TITLE     Cell-specific localization of beta-synuclein in the mouse retina
  JOURNAL   Brain Struct Funct 229 (5), 1279-1298 (2024)
   PUBMED   38703218
  REMARK    GeneRIF: Cell-specific localization of beta-synuclein in the mouse
            retina.
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Pulcrano,S., De Gregorio,R., De Sanctis,C., Volpicelli,F.,
            Piscitelli,R.M., Speranza,L., Perrone-Capano,C., di Porzio,U.,
            Caiazzo,M., Martini,A., Giacomet,C., Medina,D., Awatramani,R.,
            Viggiano,D., Federici,M., Mercuri,N.B., Guatteo,E. and
            Bellenchi,G.C.
  TITLE     miR-218 Promotes Dopaminergic Differentiation and Controls Neuron
            Excitability and Neurotransmitter Release through the Regulation of
            a Synaptic-Related Genes Network
  JOURNAL   J Neurosci 43 (48), 8104-8125 (2023)
   PUBMED   37816598
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Vargas,K.J., Colosi,P.L., Girardi,E., Park,J.M., Harmon,L.E. and
            Chandra,S.S.
  TITLE     alpha-Synuclein colocalizes with AP180 and affects the size of
            clathrin lattices
  JOURNAL   J Biol Chem 299 (9), 105091 (2023)
   PUBMED   37516240
REFERENCE   5  (residues 1 to 133)
  AUTHORS   Carnazza,K.E., Komer,L.E., Xie,Y.X., Pineda,A., Briano,J.A.,
            Gao,V., Na,Y., Ramlall,T., Buchman,V.L., Eliezer,D., Sharma,M. and
            Burre,J.
  TITLE     Synaptic vesicle binding of alpha-synuclein is modulated by beta-
            and gamma-synucleins
  JOURNAL   Cell Rep 39 (2), 110675 (2022)
   PUBMED   35417693
  REMARK    Erratum:[Cell Rep. 2024 May 28;43(5):114280. doi:
            10.1016/j.celrep.2024.114280. PMID: 38758645]
REFERENCE   6  (residues 1 to 133)
  AUTHORS   Windisch,M., Hutter-Paier,B., Rockenstein,E., Hashimoto,M.,
            Mallory,M. and Masliah,E.
  TITLE     Development of a new treatment for Alzheimer's disease and
            Parkinson's disease using anti-aggregatory beta-synuclein-derived
            peptides
  JOURNAL   J Mol Neurosci 19 (1-2), 63-69 (2002)
   PUBMED   12212795
  REMARK    GeneRIF: Beta-synuclein decreased formation of Lewy bodies by 40%,
            and prevented functional deficits associated with overexpression of
            alpha-synuclein. This is a preliminary in vivo proof of
            antiaggregatory function of beta-synuclein.
REFERENCE   7  (residues 1 to 133)
  AUTHORS   Sopher,B.L., Koszdin,K.L., McClain,M.E., Myrick,S.B.,
            Martinez,R.A., Smith,A.C. and La Spada,A.R.
  TITLE     Genomic organization, chromosome location, and expression analysis
            of mouse beta-synuclein, a candidate for involvement in
            neurodegeneration
  JOURNAL   Cytogenet Cell Genet 93 (1-2), 117-123 (2001)
   PUBMED   11474193
REFERENCE   8  (residues 1 to 133)
  AUTHORS   Kahle,P.J., Neumann,M., Ozmen,L., Muller,V., Jacobsen,H.,
            Schindzielorz,A., Okochi,M., Leimer,U., van Der Putten,H.,
            Probst,A., Kremmer,E., Kretzschmar,H.A. and Haass,C.
  TITLE     Subcellular localization of wild-type and Parkinson's
            disease-associated mutant alpha -synuclein in human and transgenic
            mouse brain
  JOURNAL   J Neurosci 20 (17), 6365-6373 (2000)
   PUBMED   10964942
REFERENCE   9  (residues 1 to 133)
  AUTHORS   Lavedan,C.
  TITLE     The synuclein family
  JOURNAL   Genome Res 8 (9), 871-880 (1998)
   PUBMED   9750188
  REMARK    Review article
REFERENCE   10 (residues 1 to 133)
  AUTHORS   Hsu,L.J., Mallory,M., Xia,Y., Veinbergs,I., Hashimoto,M.,
            Yoshimoto,M., Thal,L.J., Saitoh,T. and Masliah,E.
  TITLE     Expression pattern of synucleins (non-Abeta component of
            Alzheimer's disease amyloid precursor protein/alpha-synuclein)
            during murine brain development
  JOURNAL   J Neurochem 71 (1), 338-344 (1998)
   PUBMED   9648883
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC162526.3.
            
            On Apr 14, 2018 this sequence version replaced XP_006517079.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FO720450.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 29.28 cM"
     Protein         1..133
                     /product="beta-synuclein"
                     /calculated_mol_wt=13920
     Region          1..120
                     /region_name="Synuclein"
                     /note="pfam01387"
                     /db_xref="CDD:460186"
     Region          20..66
                     /region_name="4 X 11 AA tandem repeats of
                     [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZZ3.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q91ZZ3.1)"
     Region          96..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZZ3.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by BARK1, CK2 and GRK5.
                     /evidence=ECO:0000250|UniProtKB:Q16143; propagated from
                     UniProtKB/Swiss-Prot (Q91ZZ3.1)"
     CDS             1..133
                     /gene="Sncb"
                     /gene_synonym="betaSYN"
                     /coded_by="NM_001362407.1:325..726"
                     /db_xref="CCDS:CCDS36670.1"
                     /db_xref="GeneID:104069"
                     /db_xref="MGI:MGI:1889011"
ORIGIN      
        1 mdvfmkglsm akegvvaaae ktkqgvteaa ektkegvlyv gsktsgvvqg vasvaektke
       61 qashlggavf sgagniaaat glvkkeefpt dlkpeevaqe aaeepliepl mepegesyed
      121 spqeeyqeye pea
//
LOCUS       NP_033283                375 aa            linear   ROD 27-APR-2025
DEFINITION  serpin B5 isoform a [Mus musculus].
ACCESSION   NP_033283
VERSION     NP_033283.1
DBSOURCE    REFSEQ: accession NM_009257.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Kim,S.H., Mitchel,J.A., McGill,M., Cremona,T.P., Baek,J.W.,
            Kasahara,D.I., Anathy,V., Israel,E. and Park,J.A.
  TITLE     Increased extracellular maspin levels after mechanical compression
            in vitro or allergen challenge in vivo
  JOURNAL   J Allergy Clin Immunol 144 (4), 1116-1118 (2019)
   PUBMED   31228474
  REMARK    GeneRIF: This is the first study to recognize the potential
            implication of maspin in the pathophysiology of asthma
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Mahajan,N., Hoover,B., Rajendram,M., Shi,H.Y., Kawasaki,K.,
            Weibel,D.B. and Zhang,M.
  TITLE     Maspin binds to cardiolipin in mitochondria and triggers apoptosis
  JOURNAL   FASEB J 33 (5), 6354-6364 (2019)
   PUBMED   30786218
  REMARK    GeneRIF: model of apoptosis in which maspin binds to cardiolipin,
            displaces cytochrome c from the membrane, and facilitates its
            release to the cytoplasm.
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Zhang,M., Hendrix,M.J.C., Pemberton,P.A., Sakr,W.A. and Sheng,S.
  TITLE     An Essential Role of Maspin in Embryogenesis and Tumor
            Suppression-Response
  JOURNAL   Cancer Res 77 (18), 5208-5210 (2017)
   PUBMED   28877938
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Dzinic,S.H., Bernardo,M.M., Li,X., Fernandez-Valdivia,R., Ho,Y.S.,
            Mi,Q.S., Bandyopadhyay,S., Lonardo,F., Vranic,S., Oliveira,D.S.,
            Bonfil,R.D., Dyson,G., Chen,K., Omerovic,A., Sheng,X., Han,X.,
            Wu,D., Bi,X., Cabaravdic,D., Jakupovic,U., Wahba,M., Pang,A.,
            Harajli,D., Sakr,W.A. and Sheng,S.
  TITLE     An Essential Role of Maspin in Embryogenesis and Tumor Suppression
  JOURNAL   Cancer Res 77 (4), 886-896 (2017)
   PUBMED   27923833
  REMARK    GeneRIF: maspin is a powerful context-dependent tumor suppressor.
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Kaiserman,D., Knaggs,S., Scarff,K.L., Gillard,A., Mirza,G.,
            Cadman,M., McKeone,R., Denny,P., Cooley,J., Benarafa,C.,
            Remold-O'Donnell,E., Ragoussis,J. and Bird,P.I.
  TITLE     Comparison of human chromosome 6p25 with mouse chromosome 13
            reveals a greatly expanded ov-serpin gene repertoire in the mouse
  JOURNAL   Genomics 79 (3), 349-362 (2002)
   PUBMED   11863365
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Ngamkitidechakul,C., Burke,J.M., O'Brien,W.J. and Twining,S.S.
  TITLE     Maspin: synthesis by human cornea and regulation of in vitro
            stromal cell adhesion to extracellular matrix
  JOURNAL   Invest Ophthalmol Vis Sci 42 (13), 3135-3141 (2001)
   PUBMED   11726614
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Zhang,M., Magit,D., Botteri,F., Shi,H.Y., He,K., Li,M., Furth,P.
            and Sager,R.
  TITLE     Maspin plays an important role in mammary gland development
  JOURNAL   Dev Biol 215 (2), 278-287 (1999)
   PUBMED   10545237
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Sheng,S., Truong,B., Fredrickson,D., Wu,R., Pardee,A.B. and
            Sager,R.
  TITLE     Tissue-type plasminogen activator is a target of the tumor
            suppressor gene maspin
  JOURNAL   Proc Natl Acad Sci U S A 95 (2), 499-504 (1998)
   PUBMED   9435220
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Zhang,M., Sheng,S., Maass,N. and Sager,R.
  TITLE     mMaspin: the mouse homolog of a human tumor suppressor gene
            inhibits mammary tumor invasion and motility
  JOURNAL   Mol Med 3 (1), 49-59 (1997)
   PUBMED   9132279
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK136532.1, AC025047.17 and AC163626.5.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC005434.1, AK136532.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849376
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 50.34 cM"
     Protein         1..375
                     /product="serpin B5 isoform a"
                     /note="serine (or cysteine) proteinase inhibitor, clade B,
                     member 5; serpin B5; protease inhibitor 5; peptidase
                     inhibitor 5; serine (or cysteine) proteinase inhibitor,
                     clade B (ovalbumin), member 5; serine protease inhibitor
                     7"
                     /calculated_mol_wt=41980
     Region          1..375
                     /region_name="serpinB5_maspin"
                     /note="serpin family B member 5, mammary serine proteinase
                     inhibitor; cd02057"
                     /db_xref="CDD:381013"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70124.1)"
     Site            order(181..184,186,192,235)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381013"
     Site            298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70124.1)"
     Site            327..353
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381013"
     Site            340..341
                     /site_type="other"
                     /note="Reactive bond homolog. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P70124.1)"
     Site            361
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70124.1)"
     CDS             1..375
                     /gene="Serpinb5"
                     /gene_synonym="1110036M19Rik; Maspin; ovalbumin; PI-5;
                     Spi7"
                     /coded_by="NM_009257.4:88..1215"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS35684.1"
                     /db_xref="GeneID:20724"
                     /db_xref="MGI:MGI:109579"
ORIGIN      
        1 mdalrlansa favdlfkqlc erdpagnilf spiclstsls laqvgtkgdt aneigqvlhf
       61 envkdvpfgf qtvtsdvnkl ssfyslklvk rlyidkslnp stefisstkr pyakeletvd
      121 fkdkleetkg qinssikelt dghfedilse nsisdqtkil vvnaayfvgk wmkkfpeset
      181 kecpfriskt dtkpvqmmnl eatfclgnid disckiielp fqnkhlsmli vlpkdvedes
      241 tglekieqql npetllqwtn pstmanakvk lslpkfkvek midpkasles lglkslfnes
      301 tsdfsgmset kgvslsnvih rvcleitedg gesievpgsr ilqhkdefna dhpfiyiirh
      361 nktrniiffg kfcsp
//
LOCUS       NP_001349671             314 aa            linear   ROD 27-APR-2025
DEFINITION  serine racemase isoform 2 [Mus musculus].
ACCESSION   NP_001349671
VERSION     NP_001349671.1
DBSOURCE    REFSEQ: accession NM_001362742.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Wang,Y., Xu,D., Zhao,Y., Zhu,H., Xiu,X., Jiang,H., Liu,Y., Shan,G.
            and Wu,S.
  TITLE     Age- and Sex-Specific Regulation of Serine Racemase in the Retina
            of an Alzheimer's Disease Mouse
  JOURNAL   Invest Ophthalmol Vis Sci 66 (1), 36 (2025)
   PUBMED   39813057
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Barragan,E.V., Anisimova,M., Vijayakumar,V., Coblentz,A.,
            Park,D.K., Salaka,R.J., Nisan,A.F.K., Petshow,S., Dore,K., Zito,K.
            and Gray,J.A.
  TITLE     d-Serine Inhibits Non-ionotropic NMDA Receptor Signaling
  JOURNAL   J Neurosci 44 (32), e0140242024 (2024)
   PUBMED   38942470
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Radzishevsky,I., Odeh,M., Bodner,O., Zubedat,S., Shaulov,L.,
            Litvak,M., Esaki,K., Yoshikawa,T., Agranovich,B., Li,W.H.,
            Radzishevsky,A., Gottlieb,E., Avital,A. and Wolosker,H.
  TITLE     Impairment of serine transport across the blood-brain barrier by
            deletion of Slc38a5 causes developmental delay and motor
            dysfunction
  JOURNAL   Proc Natl Acad Sci U S A 120 (42), e2302780120 (2023)
   PUBMED   37812701
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Ni,X., Inoue,R., Wu,Y., Yoshida,T., Yaku,K., Nakagawa,T., Saito,T.,
            Saido,T.C., Takao,K. and Mori,H.
  TITLE     Regional contributions of D-serine to Alzheimer's disease pathology
            in male AppNL-G-F/NL-G-F mice
  JOURNAL   Front Aging Neurosci 15, 1211067 (2023)
   PUBMED   37455930
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Cook,S.P., Galve-Roperh,I., Martinez del Pozo,A. and
            Rodriguez-Crespo,I.
  TITLE     Direct calcium binding results in activation of brain serine
            racemase
  JOURNAL   J Biol Chem 277 (31), 27782-27792 (2002)
   PUBMED   12021263
  REMARK    GeneRIF: Direct calcium binding results in activation in brain
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Panizzutti,R., De Miranda,J., Ribeiro,C.S., Engelender,S. and
            Wolosker,H.
  TITLE     A new strategy to decrease N-methyl-D-aspartate (NMDA) receptor
            coactivation: inhibition of D-serine synthesis by converting serine
            racemase into an eliminase
  JOURNAL   Proc Natl Acad Sci U S A 98 (9), 5294-5299 (2001)
   PUBMED   11309496
REFERENCE   8  (residues 1 to 314)
  AUTHORS   De Miranda,J., Santoro,A., Engelender,S. and Wolosker,H.
  TITLE     Human serine racemase: moleular cloning, genomic organization and
            functional analysis
  JOURNAL   Gene 256 (1-2), 183-188 (2000)
   PUBMED   11054547
REFERENCE   9  (residues 1 to 314)
  AUTHORS   Wolosker,H., Blackshaw,S. and Snyder,S.H.
  TITLE     Serine racemase: a glial enzyme synthesizing D-serine to regulate
            glutamate-N-methyl-D-aspartate neurotransmission
  JOURNAL   Proc Natl Acad Sci U S A 96 (23), 13409-13414 (1999)
   PUBMED   10557334
REFERENCE   10 (residues 1 to 314)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL604066.9 and AK031687.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK031687.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 45.76 cM"
     Protein         1..314
                     /product="serine racemase isoform 2"
                     /EC_number="4.3.1.17"
                     /EC_number="5.1.1.18"
                     /EC_number="4.3.1.18"
                     /note="D-serine dehydratase; L-serine dehydratase;
                     D-serine ammonia-lyase; L-serine ammonia-lyase"
                     /calculated_mol_wt=33899
     Region          5..297
                     /region_name="Trp-synth-beta_II"
                     /note="Tryptophan synthase beta superfamily (fold type
                     II); this family of pyridoxal phosphate (PLP)-dependent
                     enzymes catalyzes beta-replacement and beta-elimination
                     reactions. This CD corresponds to
                     aminocyclopropane-1-carboxylate deaminase (ACCD),
                     tryptophan...; cl00342"
                     /db_xref="CDD:444852"
     Site            order(9..10,13,16..17,48..49,174,243,246..247,250,
                     254..256,290..293)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:107205"
     Site            56
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107205"
     CDS             1..314
                     /gene="Srr"
                     /gene_synonym="M100034; Rgsc34; Srs"
                     /coded_by="NM_001362742.1:561..1505"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS88190.1"
                     /db_xref="GeneID:27364"
                     /db_xref="MGI:MGI:1351636"
ORIGIN      
        1 mcaqycisfa dvekahiniq dsihltpvlt ssilnqiagr nlffkcelfq ktgsfkirga
       61 lnairglipd tpeekpkavv thssgnhgqa ltyaaklegi payivvpqta pnckklaiqa
      121 ygasivycdp sdesrekvtq rimqetegil vhpnqepavi agqgtialev lnqalkpsvk
      181 vyaaepsnad dcyqsklkge ltpnlhppet iadgvkssig lntwpiirdl vddvftvted
      241 eikyatqlvw grmklliept agvalaavls qhfqtvspev knvcivlsgg nvdltslnwv
      301 gqaerpapyq tvsv
//
LOCUS       NP_001350278            1645 aa            linear   PRI 27-APR-2025
DEFINITION  cortactin-binding protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001350278 XP_005250691
VERSION     NP_001350278.1
DBSOURCE    REFSEQ: accession NM_001363349.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1645)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 1645)
  AUTHORS   Shih,P.Y., Lee,S.P., Chen,Y.K. and Hsueh,Y.P.
  TITLE     Cortactin-binding protein 2 increases microtubule stability and
            regulates dendritic arborization
  JOURNAL   J Cell Sci 127 (Pt 16), 3521-3534 (2014)
   PUBMED   24928895
  REMARK    GeneRIF: Cttnbp2 increases microtubule stability and regulates
            dendritic arborization.
REFERENCE   3  (residues 1 to 1645)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   4  (residues 1 to 1645)
  AUTHORS   Zink,D., Amaral,M.D., Englmann,A., Lang,S., Clarke,L.A.,
            Rudolph,C., Alt,F., Luther,K., Braz,C., Sadoni,N., Rosenecker,J.
            and Schindelhauer,D.
  TITLE     Transcription-dependent spatial arrangements of CFTR and adjacent
            genes in human cell nuclei
  JOURNAL   J Cell Biol 166 (6), 815-825 (2004)
   PUBMED   15364959
  REMARK    GeneRIF: CORTBP2 (CTTNBP2) has a transcription-dependent spatial
            arrangement.
REFERENCE   5  (residues 1 to 1645)
  AUTHORS   Cheung,J., Petek,E., Nakabayashi,K., Tsui,L.C., Vincent,J.B. and
            Scherer,S.W.
  TITLE     Identification of the human cortactin-binding protein-2 gene from
            the autism candidate region at 7q31
  JOURNAL   Genomics 78 (1-2), 7-11 (2001)
   PUBMED   11707066
REFERENCE   6  (residues 1 to 1645)
  AUTHORS   Ohoka,Y. and Takai,Y.
  TITLE     Isolation and characterization of cortactin isoforms and a novel
            cortactin-binding protein, CBP90
  JOURNAL   Genes Cells 3 (9), 603-612 (1998)
   PUBMED   9813110
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007568.1 and AC004240.1.
            
            On May 17, 2018 this sequence version replaced XP_005250691.1.
            
            Summary: This gene encodes a protein with six ankyrin repeats and
            several proline-rich regions. A similar gene in rat interacts with
            a central regulator of the actin cytoskeleton. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1645
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.31"
     Protein         1..1645
                     /product="cortactin-binding protein 2 isoform 2"
                     /note="CORTBP2, C7orf8"
                     /calculated_mol_wt=179528
     Region          18..162
                     /region_name="CortBP2"
                     /note="Cortactin-binding protein-2; pfam09727"
                     /db_xref="CDD:462860"
     Region          105..>246
                     /region_name="DR0291"
                     /note="Predicted nucleic acid-binding protein DR0291,
                     contains C4-type Zn-ribbon domain [General function
                     prediction only]; COG1579"
                     /db_xref="CDD:441187"
     Region          <333..700
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          680..952
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          694..723
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          725..756
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(758,760,764..765,768..770,772..773,777,780,789,791,
                     793,797..798,801..803,805..806,810,813,822,824,826,
                     830..831,834..836,838..839,843,846)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          758..789
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          791..822
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..1645
                     /gene="CTTNBP2"
                     /gene_synonym="C7orf8; CORTBP2; Orf4"
                     /coded_by="NM_001363349.1:285..5222"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:83992"
                     /db_xref="HGNC:HGNC:15679"
                     /db_xref="MIM:609772"
ORIGIN      
        1 miwclhpqkk kefdvdtlsk selrmllsvm egeleardlv iealrarrke vfiqerygrf
       61 nlndpflalq rdyeagagdk ekkpvctnpl sileavmahc kkmqermsaq laaaesrqkk
      121 lemeklqlqa leqehkklaa rleeergknk qvvlmlvkec kqlsgkviee aqkledvmak
      181 leeekkktne leeelsaekr rstemeaqme kqlsefdter eqlraklnre eahttdlkee
      241 idkmrkmieq lkrgsdskps lslprktkdr rlvsisvgte gtvtrsvacq tdlvtenadh
      301 mkklpltmpv kpstgsplvs anakgsvcts atmarpgidr qasygdliga svpafpppsa
      361 nkieengpst gstpdptsst pplpsnaapp taqtpgiapq nsqappmhsl hspcantslh
      421 pglnpriqaa rfrfqgnand pdqngnttqs ppsrdvspts rdnlvakqla rntvtqalsr
      481 ftspqagaps rpgvpptgdv gthppvgrts lkthgvarvd rgnpppippk kpglsqtpsp
      541 phpqlkviid ssrasntgak vdnktvastp sslpqgnrvi neenlpksss pqlppkpsid
      601 ltvapagcav salatsqvga wpaatpglnq pacsdsslvi pttiafcssi npvsasscrp
      661 gasdsllvta sgwspsltpl lmsggpapla grptllqqaa aqgnvtllsm llneegldin
      721 yscedghsal ysaaknghtd cvrlllsaea qvnaadkngf tplcaaaaqg hfecvellis
      781 ydaninhaad ggqtplylac kngnkecikl lleagtnrsv kttdgwtpvh aavdtgnvds
      841 lkllmyhrip ahgnsfneee sessvfdldg geespegisk pvvpadlinh anregwtaah
      901 iaaskgfknc leilcrhggl eperrdkcnr tvhdvatddc khllenlnal kiplrisvge
      961 iepsnygsdd lecentical nirkqtswdd fskavsqalt nhfqaissdg wwsledvtcn
     1021 nttdsnigls arsirsitlg nvpwsvgqsf aqspwdfmrk nkaehitvll sgpqegclss
     1081 vtyasmiplq mmqnylrlve qyhnvifhgp egslqdyivh qlalclkhrq maagfsceiv
     1141 raevdagfsk eqlldlfiss aclipvkqsp skkkiiiile nleksslsel lrdflaplen
     1201 rstespctfq kgnglsecyy fhencflmgt iakaclqgsd llvqqhfrwv qlrwdgepmq
     1261 gllqrflrrk vvnkfkgqap spcdpvckiv dwalsvwrql nsclarlgtp eallgpkyfl
     1321 scpvvpghaq vtvkwmsklw ngviaprvqe ailsrasvkr qpgfgqttak rhpsqgqqav
     1381 vkaalsilln kavlhgcplp raeldqhtad fkggsfplsi vssyntcnkk kgesgawrkv
     1441 ntsprrksgr fslptwnkpd lstegmknkt isqlncnrna slskqkslen dlsltlnldq
     1501 rlslgsddea dlvkelqsmc ssksesdisk iadsrddlrm fdssgnnpvl satinnlrmp
     1561 vsqkevspls shqttecsns ksktelgvsr vksflpvprs kvtqcsqntk rsssssntrq
     1621 ieinnnskev nwnlhknehl ekpnk
//
LOCUS       NP_057619                197 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 581 [Homo sapiens].
ACCESSION   NP_057619
VERSION     NP_057619.1
DBSOURCE    REFSEQ: accession NM_016535.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Kovacs,I.A., Luck,K., Spirohn,K., Wang,Y., Pollis,C., Schlabach,S.,
            Bian,W., Kim,D.K., Kishore,N., Hao,T., Calderwood,M.A., Vidal,M.
            and Barabasi,A.L.
  TITLE     Network-based prediction of protein interactions
  JOURNAL   Nat Commun 10 (1), 1240 (2019)
   PUBMED   30886144
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF151023.2 and BC010097.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC010097.2, AF151023.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270451.6/ ENSP00000270451.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..197
                     /product="zinc finger protein 581"
                     /calculated_mol_wt=21879
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0T4.1)"
     Region          89..109
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          101..126
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          117..137
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(122,124,126,128..129,132..133,136,152,154,158..159,
                     162..163,166,180,182,184,186..187,190..191)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          147..167
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          175..193
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..197
                     /gene="ZNF581"
                     /gene_synonym="HSPC189"
                     /coded_by="NM_016535.4:146..739"
                     /db_xref="CCDS:CCDS12932.1"
                     /db_xref="GeneID:51545"
                     /db_xref="HGNC:HGNC:25017"
ORIGIN      
        1 mlvlpspcpq plafssvetm egpprrtcrs pepgpsssig spqasspprp nhyllidtqg
       61 vpytvlvdee sqrepgasga pgqkkcyscp vcsrvfeyms ylqrhsiths evkpfecdic
      121 gkafkrashl arhhsihlag ggrphgcplc prrfrdagel aqhsrvhsge rpfqcphcpr
      181 rfmeqntlqk htrwkhp
//
LOCUS       NP_001106873             258 aa            linear   PRI 27-APR-2025
DEFINITION  protein AMN1 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_001106873
VERSION     NP_001106873.1
DBSOURCE    REFSEQ: accession NM_001113402.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Fang,O., Hu,X., Wang,L., Jiang,N., Yang,J., Li,B. and Luo,Z.
  TITLE     Amn1 governs post-mitotic cell separation in Saccharomyces
            cerevisiae
  JOURNAL   PLoS Genet 14 (10), e1007691 (2018)
   PUBMED   30273335
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Yazar,S., Mishra,A., Ang,W., Kearns,L.S., Mountain,J.A.,
            Pennell,C., Montgomery,G.W., Young,T.L., Hammond,C.J.,
            Macgregor,S., Mackey,D.A. and Hewitt,A.W.
  TITLE     Interrogation of the platelet-derived growth factor receptor alpha
            locus and corneal astigmatism in Australians of Northern European
            ancestry: results of a genome-wide association study
  JOURNAL   Mol Vis 19, 1238-1246 (2013)
   PUBMED   23761726
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC045831.1 and BC067906.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037897.2, SRR1660803.78179.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281471.11/ ENSP00000281471.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.21"
     Protein         1..258
                     /product="protein AMN1 homolog isoform 1"
                     /note="protein AMN1 homolog"
                     /calculated_mol_wt=28277
     Region          37..257
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          63..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          87..116
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          117..142
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          143..168
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          169..195
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          196..221
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..258
                     /gene="AMN1"
                     /coded_by="NM_001113402.2:14..790"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44858.1"
                     /db_xref="GeneID:196394"
                     /db_xref="HGNC:HGNC:27281"
                     /db_xref="MIM:620564"
ORIGIN      
        1 mprprrvsql ldlclwcfmk nisryltdik plppnikdrl ikimsmqgqi tdsniseilh
       61 pevqtldlrs cdisdaallh lsncrklkkl nlnaskgnrv svtsegikav asscsylhea
      121 slkrccnltd egvvalalnc qllkiidlgg clsitdvslh algkncpflq cvdfsatqvs
      181 dsgvialvsg pcakkleeih mghcvnltdg aveavltycp qirillfhgc plitdhsrev
      241 leqlvgpnkl kqvtwtvy
//
LOCUS       NP_001349637             392 aa            linear   ROD 27-APR-2025
DEFINITION  selenide, water dikinase 1 isoform a [Mus musculus].
ACCESSION   NP_001349637 XP_017170393
VERSION     NP_001349637.1
DBSOURCE    REFSEQ: accession NM_001362708.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Bang,J., Kang,D., Jung,J., Yoo,T.J., Shim,M.S., Gladyshev,V.N.,
            Tsuji,P.A., Hatfield,D.L., Kim,J.H. and Lee,B.J.
  TITLE     SEPHS1: Its evolution, function and roles in development and
            diseases
  JOURNAL   Arch Biochem Biophys 730, 109426 (2022)
   PUBMED   36202216
  REMARK    GeneRIF: SEPHS1: Its evolution, function and roles in development
            and diseases.
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Kang,D., Lee,J., Jung,J., Carlson,B.A., Chang,M.J., Chang,C.B.,
            Kang,S.B., Lee,B.C., Gladyshev,V.N., Hatfield,D.L., Lee,B.J. and
            Kim,J.H.
  TITLE     Selenophosphate synthetase 1 deficiency exacerbates osteoarthritis
            by dysregulating redox homeostasis
  JOURNAL   Nat Commun 13 (1), 779 (2022)
   PUBMED   35140209
  REMARK    GeneRIF: Selenophosphate synthetase 1 deficiency exacerbates
            osteoarthritis by dysregulating redox homeostasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Qiao,L., Dho,S.H., Kim,J.Y. and Kim,L.K.
  TITLE     SEPHS1 is dispensable for pluripotency maintenance but
            indispensable for cardiac differentiation in mouse embryonic stem
            cells
  JOURNAL   Biochem Biophys Res Commun 590, 125-131 (2022)
   PUBMED   34974300
  REMARK    GeneRIF: SEPHS1 is dispensable for pluripotency maintenance but
            indispensable for cardiac differentiation in mouse embryonic stem
            cells.
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Bang,J., Han,M., Yoo,T.J., Qiao,L., Jung,J., Na,J., Carlson,B.A.,
            Gladyshev,V.N., Hatfield,D.L., Kim,J.H., Kim,L.K. and Lee,B.J.
  TITLE     Identification of Signaling Pathways for Early Embryonic Lethality
            and Developmental Retardation in Sephs1-/- Mice
  JOURNAL   Int J Mol Sci 22 (21), 11647 (2021)
   PUBMED   34769078
  REMARK    GeneRIF: Identification of Signaling Pathways for Early Embryonic
            Lethality and Developmental Retardation in Sephs1(-/-) Mice.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Jung,J., Kim,Y., Na,J., Qiao,L., Bang,J., Kwon,D., Yoo,T.J.,
            Kang,D., Kim,L.K., Carlson,B.A., Hatfield,D.L., Kim,J.H. and
            Lee,B.J.
  TITLE     Constitutive Oxidative Stress by SEPHS1 Deficiency Induces
            Endothelial Cell Dysfunction
  JOURNAL   Int J Mol Sci 22 (21), 11646 (2021)
   PUBMED   34769076
  REMARK    GeneRIF: Constitutive Oxidative Stress by SEPHS1 Deficiency Induces
            Endothelial Cell Dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Tobe,R., Carlson,B.A., Huh,J.H., Castro,N.P., Xu,X.M., Tsuji,P.A.,
            Lee,S.G., Bang,J., Na,J.W., Kong,Y.Y., Beaglehole,D., Southon,E.,
            Seifried,H., Tessarollo,L., Salomon,D.S., Schweizer,U.,
            Gladyshev,V.N., Hatfield,D.L. and Lee,B.J.
  TITLE     Selenophosphate synthetase 1 is an essential protein with roles in
            regulation of redox homoeostasis in mammals
  JOURNAL   Biochem J 473 (14), 2141-2154 (2016)
   PUBMED   27208177
  REMARK    GeneRIF: Data found that several malignant characteristics of
            SPS1-deficient F9 cells were reversed, suggesting that SPS1 played
            a role in supporting and/or sustaining cancer. Selenophosphate
            synthetase 1 is an essential protein with roles in regulation of
            redox homoeostasis in mammals.
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Saiki,R., Nagata,A., Kainou,T., Matsuda,H. and Kawamukai,M.
  TITLE     Characterization of solanesyl and decaprenyl diphosphate synthases
            in mice and humans
  JOURNAL   FEBS J 272 (21), 5606-5622 (2005)
   PUBMED   16262699
  REMARK    GeneRIF: murine and human solanesyl and decaprenyl diphosphate
            synthases are heterotetramers composed of newly characterized hDPS1
            (mSPS1) and hDLP1 (mDLP1)
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL807778.10.
            
            On Apr 25, 2018 this sequence version replaced XP_017170393.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 all encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660813.255638.1,
                                           SRR13422603.144102.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 3.02 cM"
     Protein         1..392
                     /product="selenide, water dikinase 1 isoform a"
                     /EC_number="2.7.9.3"
                     /note="selenide, water dikinase 1; selenium donor protein
                     1; selenophosphate synthase 1"
                     /calculated_mol_wt=42776
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P49903; propagated from
                     UniProtKB/Swiss-Prot (Q8BH69.1)"
     Region          19..333
                     /region_name="selD"
                     /note="selenium donor protein; TIGR00476"
                     /db_xref="CDD:273100"
     Site            32
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:P16456; propagated from
                     UniProtKB/Swiss-Prot (Q8BH69.1)"
     Site            order(81..84,86,88,110,121,124,127,163,170..171,175,277)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:100031"
     Site            order(106,110,161..163)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:100031"
     CDS             1..392
                     /gene="Sephs1"
                     /gene_synonym="1110046B24Rik; SELD; SPS; SPS1"
                     /coded_by="NM_001362708.1:191..1369"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS15659.1"
                     /db_xref="GeneID:109079"
                     /db_xref="MGI:MGI:1923580"
ORIGIN      
        1 mstresfnpe tyeldksfrl trftelkgtg ckvpqdvlqk lleslqenhf qedeqflgav
       61 mprlgigmdt cviplrhggl slvqttdyiy pivddpymmg riacanvlsd lyamgvtecd
      121 nmlmllgvsn kmtdrerdkv ipliiqgfkd aaeeagtsvt ggqtvlnpwi vlggvattvc
      181 qpnefimpdn avpgdvlvlt kplgtqvava vhqwldipek wnkiklvvtq edvelayqea
      241 mmnmarlnrt aaglmhtfna haatditgfg ilghaqnlak qqrnevsfvi hnlpvlakma
      301 avskacgnmf glmhgtcpet sgglliclpr eqaarfcaei kspkygeghq awiigivekg
      361 nrtariidkp riievapqva tqnvnptpga ts
//
LOCUS       NP_001002919             152 aa            linear   PRI 27-APR-2025
DEFINITION  ALK and LTK ligand 2 precursor [Homo sapiens].
ACCESSION   NP_001002919 XP_211736
VERSION     NP_001002919.2
DBSOURCE    REFSEQ: accession NM_001002919.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Mazzeschi,M., Sgarzi,M., Romaniello,D., Gelfo,V., Cavallo,C.,
            Ambrosi,F., Morselli,A., Miano,C., Laprovitera,N., Girone,C.,
            Ferracin,M., Santi,S., Rihawi,K., Ardizzoni,A., Fiorentino,M.,
            D'Uva,G., Gyorffy,B., Palmer,R. and Lauriola,M.
  TITLE     The autocrine loop of ALK receptor and ALKAL2 ligand is an
            actionable target in consensus molecular subtype 1 colon cancer
  JOURNAL   J Exp Clin Cancer Res 41 (1), 113 (2022)
   PUBMED   35351152
  REMARK    GeneRIF: The autocrine loop of ALK receptor and ALKAL2 ligand is an
            actionable target in consensus molecular subtype 1 colon cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Reshetnyak,A.V., Rossi,P., Myasnikov,A.G., Sowaileh,M., Mohanty,J.,
            Nourse,A., Miller,D.J., Lax,I., Schlessinger,J. and Kalodimos,C.G.
  TITLE     Mechanism for the activation of the anaplastic lymphoma kinase
            receptor
  JOURNAL   Nature 600 (7887), 153-157 (2021)
   PUBMED   34819673
REFERENCE   3  (residues 1 to 152)
  AUTHORS   De Munck,S., Provost,M., Kurikawa,M., Omori,I., Mukohyama,J.,
            Felix,J., Bloch,Y., Abdel-Wahab,O., Bazan,J.F., Yoshimi,A. and
            Savvides,S.N.
  TITLE     Structural basis of cytokine-mediated activation of ALK family
            receptors
  JOURNAL   Nature 600 (7887), 143-147 (2021)
   PUBMED   34646012
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Borenas,M., Umapathy,G., Lai,W.Y., Lind,D.E., Witek,B., Guan,J.,
            Mendoza-Garcia,P., Masudi,T., Claeys,A., Chuang,T.P., El Wakil,A.,
            Arefin,B., Fransson,S., Koster,J., Johansson,M., Gaarder,J., Van
            den Eynden,J., Hallberg,B. and Palmer,R.H.
  TITLE     ALK ligand ALKAL2 potentiates MYCN-driven neuroblastoma in the
            absence of ALK mutation
  JOURNAL   EMBO J 40 (3), e105784 (2021)
   PUBMED   33411331
  REMARK    GeneRIF: ALK ligand ALKAL2 potentiates MYCN-driven neuroblastoma in
            the absence of ALK mutation.
REFERENCE   5  (residues 1 to 152)
  AUTHORS   Reshetnyak,A.V., Mohanty,J., Tome,F., Puleo,D.E., Plotnikov,A.N.,
            Ahmed,M., Kaur,N., Poliakov,A., Cinnaiyan,A.M., Lax,I. and
            Schlessinger,J.
  TITLE     Identification of a biologically active fragment of ALK and
            LTK-Ligand 2 (augmentor-alpha)
  JOURNAL   Proc Natl Acad Sci U S A 115 (33), 8340-8345 (2018)
   PUBMED   30061385
REFERENCE   6  (residues 1 to 152)
  AUTHORS   Fadeev,A., Mendoza-Garcia,P., Irion,U., Guan,J., Pfeifer,K.,
            Wiessner,S., Serluca,F., Singh,A.P., Nusslein-Volhard,C. and
            Palmer,R.H.
  TITLE     ALKALs are in vivo ligands for ALK family receptor tyrosine kinases
            in the neural crest and derived cells
  JOURNAL   Proc Natl Acad Sci U S A 115 (4), E630-E638 (2018)
   PUBMED   29317532
  REMARK    GeneRIF: activation of ALK/LTK family receptors by small ALKAL
            proteins (FAM150, AUG) conserved in vertebrates
REFERENCE   7  (residues 1 to 152)
  AUTHORS   Reshetnyak,A.V., Murray,P.B., Shi,X., Mo,E.S., Mohanty,J., Tome,F.,
            Bai,H., Gunel,M., Lax,I. and Schlessinger,J.
  TITLE     Augmentor alpha and beta (FAM150) are ligands of the receptor
            tyrosine kinases ALK and LTK: Hierarchy and specificity of
            ligand-receptor interactions
  JOURNAL   Proc Natl Acad Sci U S A 112 (52), 15862-15867 (2015)
   PUBMED   26630010
  REMARK    GeneRIF: Data show FAM150B, which was named as augmentor-alpha
            (AUG-alpha), binds and activtes both anaplastic lymphoma kinase
            (ALK) and tyrosine kinase (LTK).
REFERENCE   8  (residues 1 to 152)
  AUTHORS   Guan,J., Umapathy,G., Yamazaki,Y., Wolfstetter,G., Mendoza,P.,
            Pfeifer,K., Mohammed,A., Hugosson,F., Zhang,H., Hsu,A.W.,
            Halenbeck,R., Hallberg,B. and Palmer,R.H.
  TITLE     FAM150A and FAM150B are activating ligands for anaplastic lymphoma
            kinase
  JOURNAL   Elife 4, e09811 (2015)
   PUBMED   26418745
  REMARK    GeneRIF: In conclusion, these data show that ALK is robustly
            activated by the FAM150A/B ligands.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 152)
  AUTHORS   Zhang,H., Pao,L.I., Zhou,A., Brace,A.D., Halenbeck,R., Hsu,A.W.,
            Bray,T.L., Hestir,K., Bosch,E., Lee,E., Wang,G., Liu,H., Wong,B.R.,
            Kavanaugh,W.M. and Williams,L.T.
  TITLE     Deorphanization of the human leukocyte tyrosine kinase (LTK)
            receptor by a signaling screen of the extracellular proteome
  JOURNAL   Proc Natl Acad Sci U S A 111 (44), 15741-15745 (2014)
   PUBMED   25331893
  REMARK    GeneRIF: Only two related secreted factors, FAM150A and FAM150B
            (family with sequence similarity 150 member A and member B),
            stimulated LTK phosphorylation.
REFERENCE   10 (residues 1 to 152)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC033490.1, AI300876.1 and AC079779.7.
            
            On May 23, 2007 this sequence version replaced NP_001002919.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033490.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000403610.9/ ENSP00000384604.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.3"
     Protein         1..152
                     /product="ALK and LTK ligand 2 precursor"
                     /note="protein FAM150B; AUG-alpha; family with sequence
                     similarity 150 member B; augmentor alpha; augmentor-beta"
                     /calculated_mol_wt=14551
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2382
     mat_peptide     25..152
                     /product="ALK and LTK ligand 2. /id=PRO_0000317193"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UX46.2)"
                     /calculated_mol_wt=14551
     Region          33..149
                     /region_name="FAM150"
                     /note="FAM150 family; pfam15129"
                     /db_xref="CDD:464519"
     CDS             1..152
                     /gene="ALKAL2"
                     /gene_synonym="AUGA; FAM150B; PRO1097; RGPG542"
                     /coded_by="NM_001002919.3:137..595"
                     /db_xref="CCDS:CCDS46218.1"
                     /db_xref="GeneID:285016"
                     /db_xref="HGNC:HGNC:27683"
                     /db_xref="MIM:619671"
ORIGIN      
        1 mrgpghplll glllvlgaag rgrggaepre padgqallrl vvelvqelrk hhsaehkglq
       61 llgrdcalgr aeaaglgpsp eqrveivprd lrmkdkflkh ltgplyfspk cskhfhrlyh
      121 ntrdctipay ykrcarlltr lavspvcmed kq
//
LOCUS       NP_001346254             261 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 106A [Mus musculus].
ACCESSION   NP_001346254
VERSION     NP_001346254.1
DBSOURCE    REFSEQ: accession NM_001359325.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Zhang,X., Feng,T., Zhou,X., Sullivan,P.M., Hu,F., Lou,Y., Yu,J.,
            Feng,J., Liu,H. and Chen,Y.
  TITLE     Inactivation of TMEM106A promotes lipopolysaccharide-induced
            inflammation via the MAPK and NF-kappaB signaling pathways in
            macrophages
  JOURNAL   Clin Exp Immunol 203 (1), 125-136 (2021)
   PUBMED   33006758
  REMARK    GeneRIF: Inactivation of TMEM106A promotes
            lipopolysaccharide-induced inflammation via the MAPK and NF-kappaB
            signaling pathways in macrophages.
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Dai,H., Xu,D., Su,J., Jang,J. and Chen,Y.
  TITLE     Transmembrane protein 106a activates mouse peritoneal macrophages
            via the MAPK and NF-kappaB signaling pathways
  JOURNAL   Sci Rep 5, 12461 (2015)
   PUBMED   26215746
  REMARK    GeneRIF: data suggest that mouse Tmem106a might be a new trigger of
            macrophage activation and have some influence toward the M1 state
            through the activation of the MAPKs and NF-kappaB pathway
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Abdallah,B.M., Ditzel,N., Mahmood,A., Isa,A., Traustadottir,G.A.,
            Schilling,A.F., Ruiz-Hidalgo,M.J., Laborda,J., Amling,M. and
            Kassem,M.
  TITLE     DLK1 is a novel regulator of bone mass that mediates estrogen
            deficiency-induced bone loss in mice
  JOURNAL   J Bone Miner Res 26 (7), 1457-1471 (2011)
   PUBMED   21308776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK149650.1 and AK150285.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1 through 4 encode the same protein.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849374,
                              SAMN00849375 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 65.44 cM"
     Protein         1..261
                     /product="transmembrane protein 106A"
                     /calculated_mol_wt=28978
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC04.1)"
     Region          24..251
                     /region_name="DUF1356"
                     /note="Protein of unknown function (DUF1356); pfam07092"
                     /db_xref="CDD:462088"
     Site            93..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VC04.1)"
     CDS             1..261
                     /gene="Tmem106a"
                     /gene_synonym="0610008L10Rik"
                     /coded_by="NM_001359325.1:426..1211"
                     /db_xref="CCDS:CCDS25476.1"
                     /db_xref="GeneID:217203"
                     /db_xref="MGI:MGI:1922056"
ORIGIN      
        1 mgkavsqlts rkdedkpilp dnpamasqaa nyfstgsskp ahscmpyeka asssfvtcpt
       61 cqgngeipqe qekqlvalip ygdqrlkprr tklfvflsva icllifslti fflyprpiav
      121 rpvglnsstv tfedahvqln ttnvlnifns nfypitvtql taevlhqasv vgqvtsslrl
      181 higplaseqm pyevasrild entykictwp kirvhhilln iqgsltcsfl shpqqlpfes
      241 feyvdcrenm slphlelprp a
//
LOCUS       NP_001211                666 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit beta
            isoform 1 [Homo sapiens].
ACCESSION   NP_001211 XP_941407
VERSION     NP_001211.3
DBSOURCE    REFSEQ: accession NM_001220.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Borghi,R., Trivisano,M., Specchio,N., Tartaglia,M. and
            Compagnucci,C.
  TITLE     Understanding the pathogenetic mechanisms underlying altered
            neuronal function associated with CAMK2B mutations
  JOURNAL   Neurosci Biobehav Rev 152, 105299 (2023)
   PUBMED   37391113
  REMARK    GeneRIF: Understanding the pathogenetic mechanisms underlying
            altered neuronal function associated with CAMK2B mutations.
            Review article
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Nicole,O. and Pacary,E.
  TITLE     CaMKIIbeta in Neuronal Development and Plasticity: An Emerging
            Candidate in Brain Diseases
  JOURNAL   Int J Mol Sci 21 (19), 7272 (2020)
   PUBMED   33019657
  REMARK    GeneRIF: CaMKIIbeta in Neuronal Development and Plasticity: An
            Emerging Candidate in Brain Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   7  (residues 1 to 666)
  AUTHORS   Penades,J.R., Bernal,D., Revert,F., Johansson,C., Fresquet,V.J.,
            Cervera,J., Wieslander,J., Quinones,S. and Saus,J.
  TITLE     Characterization and expression of multiple alternatively spliced
            transcripts of the Goodpasture antigen gene region. Goodpasture
            antibodies recognize recombinant proteins representing the
            autoantigen and one of its alternative forms
  JOURNAL   Eur J Biochem 229 (3), 754-760 (1995)
   PUBMED   7758473
REFERENCE   8  (residues 1 to 666)
  AUTHORS   Schworer,C.M., Colbran,R.J., Keefer,J.R. and Soderling,T.R.
  TITLE     Ca2+/calmodulin-dependent protein kinase II. Identification of a
            regulatory autophosphorylation site adjacent to the inhibitory and
            calmodulin-binding domains
  JOURNAL   J Biol Chem 263 (27), 13486-13489 (1988)
   PUBMED   3417668
REFERENCE   9  (residues 1 to 666)
  AUTHORS   Thiel,G., Czernik,A.J., Gorelick,F., Nairn,A.C. and Greengard,P.
  TITLE     Ca2+/calmodulin-dependent protein kinase II: identification of
            threonine-286 as the autophosphorylation site in the alpha subunit
            associated with the generation of Ca2+-independent activity
  JOURNAL   Proc Natl Acad Sci U S A 85 (17), 6337-6341 (1988)
   PUBMED   2842767
REFERENCE   10 (residues 1 to 666)
  AUTHORS   Bennett,M.K. and Kennedy,M.B.
  TITLE     Deduced primary structure of the beta subunit of brain type II
            Ca2+/calmodulin-dependent protein kinase determined by molecular
            cloning
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1794-1798 (1987)
   PUBMED   3470758
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI550751.1, U23460.1,
            AC006454.4 and AK290148.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_941407.1, NP_001211.2.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a beta chain.
            It is possible that distinct isoforms of this chain have different
            cellular localizations and interact differently with calmodulin.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U23460.1, SRR3476690.1104976.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395749.7/ ENSP00000379098.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..666
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit beta isoform 1"
                     /EC_number="2.7.11.17"
                     /note="CaM kinase II beta subunit; CaM-kinase II beta
                     chain; proline rich calmodulin-dependent protein kinase;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit beta; caMK-II subunit beta"
                     /calculated_mol_wt=72547
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P28652; propagated from
                     UniProtKB/Swiss-Prot (Q13554.3)"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:16690701; propagated from
                     UniProtKB/Swiss-Prot (Q13554.3)"
     Region          291..301
                     /region_name="calmodulin-binding domain"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q13554.3)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q13554.3)"
     Region          349..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13554.3)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08413; propagated from
                     UniProtKB/Swiss-Prot (Q13554.3)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28652; propagated from
                     UniProtKB/Swiss-Prot (Q13554.3)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08413; propagated from
                     UniProtKB/Swiss-Prot (Q13554.3)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P28652; propagated from
                     UniProtKB/Swiss-Prot (Q13554.3)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13554.3)"
     Region          534..661
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..666
                     /gene="CAMK2B"
                     /gene_synonym="CAM2; CAMK2; CAMKB; CaMKIIbeta; MRD54"
                     /coded_by="NM_001220.5:174..2174"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5483.1"
                     /db_xref="GeneID:816"
                     /db_xref="HGNC:HGNC:1461"
                     /db_xref="MIM:607707"
ORIGIN      
        1 mattvtctrf tdeyqlyedi gkgafsvvrr cvklctghey aakiintkkl sardhqkler
       61 earicrllkh snivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskckg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkea ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itahealkhp wvcqrstvas mmhrqetvec lkkfnarrkl
      301 kgailttmla trnfsvgrqt tapatmstaa sgttmglveq aksllnkkad gvkpqtnstk
      361 nsaaatspkg tlppaalepq ttvihnpvdg ikessdsant tiededakap rvpdilssvr
      421 rgsgapeaeg plpcpspapf splpapspri sdilnsvrrg sgtpeaegpl sagpppclsp
      481 allgplssps prisdilnsv rrgsgtpeae gpspvgpppc psptipgplp tpsrkqeiik
      541 tteqlieavn ngdfeayaki cdpgltsfep ealgnlvegm dfhrfyfenl laknskpiht
      601 tilnphvhvi gedaaciayi rltqyidgqg rprtsqseet rvwhrrdgkw qnvhfhcsga
      661 pvaplq
//
LOCUS       NP_004636                576 aa            linear   PRI 27-APR-2025
DEFINITION  coilin [Homo sapiens].
ACCESSION   NP_004636
VERSION     NP_004636.1
DBSOURCE    REFSEQ: accession NM_004645.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   White,L., Erbay,B. and Blair,G.E.
  TITLE     The Cajal body protein p80-coilin forms a complex with the
            adenovirus L4-22K protein and facilitates the nuclear export of
            adenovirus mRNA
  JOURNAL   mBio 14 (5), e0145923 (2023)
   PUBMED   37795984
  REMARK    GeneRIF: The Cajal body protein p80-coilin forms a complex with the
            adenovirus L4-22K protein and facilitates the nuclear export of
            adenovirus mRNA.
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Lett,K.E., Logan,M.K., McLaurin,D.M. and Hebert,M.D.
  TITLE     Coilin enhances phosphorylation and stability of DGCR8 and promotes
            miRNA biogenesis
  JOURNAL   Mol Biol Cell 32 (20), br4 (2021)
   PUBMED   34319763
  REMARK    GeneRIF: Coilin enhances phosphorylation and stability of DGCR8 and
            promotes miRNA biogenesis.
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Bohmann,K., Ferreira,J.A. and Lamond,A.I.
  TITLE     Mutational analysis of p80 coilin indicates a functional
            interaction between coiled bodies and the nucleolus
  JOURNAL   J Cell Biol 131 (4), 817-831 (1995)
   PUBMED   7490287
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Kusuda,J., Tanuma,R., Gotoh,E., Toyoda,A. and Hashimoto,K.
  TITLE     Assignment of a human autoimmune antigen, p80-coilin gene to
            chromosome 17q21-q23 and of its possible pseudogene to chromosome
            14
  JOURNAL   Hum Genet 95 (2), 233-234 (1995)
   PUBMED   7860074
REFERENCE   8  (residues 1 to 576)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
REFERENCE   9  (residues 1 to 576)
  AUTHORS   Carmo-Fonseca,M., Ferreira,J. and Lamond,A.I.
  TITLE     Assembly of snRNP-containing coiled bodies is regulated in
            interphase and mitosis--evidence that the coiled body is a kinetic
            nuclear structure
  JOURNAL   J Cell Biol 120 (4), 841-852 (1993)
   PUBMED   7679389
REFERENCE   10 (residues 1 to 576)
  AUTHORS   Andrade,L.E., Chan,E.K., Raska,I., Peebles,C.L., Roos,G. and
            Tan,E.M.
  TITLE     Human autoantibody to a novel protein of the nuclear coiled body:
            immunological characterization and cDNA cloning of p80-coilin
  JOURNAL   J Exp Med 173 (6), 1407-1419 (1991)
   PUBMED   2033369
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004584.2, BC010385.1 and
            AW021880.1.
            
            Summary: The protein encoded by this gene is an integral component
            of Cajal bodies (also called coiled bodies). Cajal bodies are
            nuclear suborganelles of varying number and composition that are
            involved in the post-transcriptional modification of small nuclear
            and small nucleolar RNAs. The N-terminus of the coilin protein
            directs its self-oligomerization while the C-terminus influences
            the number of nuclear bodies assembled per cell. Differential
            methylation and phosphorylation of coilin likely influences its
            localization among nuclear bodies and the composition and assembly
            of Cajal bodies. This gene has pseudogenes on chromosome 4 and
            chromosome 14. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.621235.1, BC010385.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000240316.5/ ENSP00000240316.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q22"
     Protein         1..576
                     /product="coilin"
                     /note="coilin p80"
                     /calculated_mol_wt=62477
     Region          7..138
                     /region_name="Coilin_N"
                     /note="Coilin N-terminus; pfam15862"
                     /db_xref="CDD:464910"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Region          125..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P38432.1)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by VRK1 and VRK2.
                     /evidence=ECO:0000269|PubMed:21920476; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Region          223..271
                     /region_name="2 X 4 AA repeats of A-R-N-S"
                     /note="propagated from UniProtKB/Swiss-Prot (P38432.1)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SU73; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SU73; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SU73; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Region          352..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P38432.1)"
     Region          386..520
                     /region_name="2 X 4 AA repeats of S-L-P-A"
                     /note="propagated from UniProtKB/Swiss-Prot (P38432.1)"
     Region          392..420
                     /region_name="Required for interaction with SMN.
                     /evidence=ECO:0000269|PubMed:11641277"
                     /note="propagated from UniProtKB/Swiss-Prot (P38432.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Region          413..420
                     /region_name="4 X 2 AA tandem repeats of R-G"
                     /note="propagated from UniProtKB/Swiss-Prot (P38432.1)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38432.1)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P38432.1)"
     CDS             1..576
                     /gene="COIL"
                     /gene_synonym="CLN80; p80-coilin"
                     /coded_by="NM_004645.3:32..1762"
                     /db_xref="CCDS:CCDS11592.1"
                     /db_xref="GeneID:8161"
                     /db_xref="HGNC:HGNC:2184"
                     /db_xref="MIM:600272"
ORIGIN      
        1 maasetvrlr lqfdypppat phctafwllv dlnrcrvvtd lislirqrfg fssgaflgly
       61 leggllppae sarlvrdndc lrvkleergv aensvvisng dinlslrkak krafqleege
      121 etepdckysk khwksrennn nnekvldlep kavtdqtvsk knkrknkatc gtvgddneea
      181 krkspkkkek ceykkkaknp kspkvqavkd wanqrcsspk gsarnslvka krkgsvsvcs
      241 kespsssses escdesisdg pskvtlearn sseklptels keepstkntt adklaiklgf
      301 sltpskgkts gttssssdss aesddqclms sstpecaagf lktvglfagr grpgpglssq
      361 tagaagwrrs gsngggqapg aspsvslpas lgrgwgreen lfswkgakgr gmrgrgrgrg
      421 hpvscvvnrs tdnqrqqqln dvvknsstii qnpvetpkkd ysllpllaaa pqvgekiafk
      481 lleltssysp dvsdykegri lshnpetqqv dieilsslpa lrepgkfdlv yhnengaevv
      541 eyavtqeski tvfwkelidp rliiespsnt sstepa
//
LOCUS       NP_057442                519 aa            linear   PRI 27-APR-2025
DEFINITION  iroquois-class homeodomain protein IRX-4 isoform b [Homo sapiens].
ACCESSION   NP_057442
VERSION     NP_057442.1
DBSOURCE    REFSEQ: accession NM_016358.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Malik,A., Jayarathna,D.K., Fisher,M., Barbhuiya,T.K., Gandhi,N.S.
            and Batra,J.
  TITLE     Dynamics and recognition of homeodomain containing protein-DNA
            complex of IRX4
  JOURNAL   Proteins 92 (2), 282-301 (2024)
   PUBMED   37861198
  REMARK    GeneRIF: Dynamics and recognition of homeodomain containing
            protein-DNA complex of IRX4.
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Fernando,A., Liyanage,C., Moradi,A., Janaththani,P. and Batra,J.
  TITLE     Identification and Characterization of Alternatively Spliced
            Transcript Isoforms of IRX4 in Prostate Cancer
  JOURNAL   Genes (Basel) 12 (5), 615 (2021)
   PUBMED   33919200
  REMARK    GeneRIF: Identification and Characterization of Alternatively
            Spliced Transcript Isoforms of IRX4 in Prostate Cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Chakma,K., Gu,Z., Abudurexiti,Y., Hata,T., Motoi,F., Unno,M.,
            Horii,A. and Fukushige,S.
  TITLE     Epigenetic inactivation of IRX4 is responsible for acceleration of
            cell growth in human pancreatic cancer
  JOURNAL   Cancer Sci 111 (12), 4594-4604 (2020)
   PUBMED   32894817
  REMARK    GeneRIF: Epigenetic inactivation of IRX4 is responsible for
            acceleration of cell growth in human pancreatic cancer.
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Xu,X., Hussain,W.M., Vijai,J., Offit,K., Rubin,M.A., Demichelis,F.
            and Klein,R.J.
  TITLE     Variants at IRX4 as prostate cancer expression quantitative trait
            loci
  JOURNAL   Eur J Hum Genet 22 (4), 558-563 (2014)
   PUBMED   24022300
  REMARK    GeneRIF: We independently validated IRX4 as a potential prostate
            cancer risk gene through cis-expression quantitative trait loci
            analysis of prostate cancer risk variants.
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Bayrak,F., Komurcu-Bayrak,E., Mutlu,B., Kahveci,G. and
            Erginel-Unaltuna,N.
  TITLE     Genetic analysis of the Irx4 gene in hypertrophic cardiomyopathy
  JOURNAL   Turk Kardiyol Dern Ars 36 (2), 90-95 (2008)
   PUBMED   18497553
  REMARK    GeneRIF: Polymorphism A381>G of the Irx4 gene may have a modifier
            effect on septal thickness, resulting in increased corrected QT
            dispersion and higher outflow gradients.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Wang,G.F., Nikovits,W. Jr., Bao,Z.Z. and Stockdale,F.E.
  TITLE     Irx4 forms an inhibitory complex with the vitamin D and retinoic X
            receptors to regulate cardiac chamber-specific slow MyHC3
            expression
  JOURNAL   J Biol Chem 276 (31), 28835-28841 (2001)
   PUBMED   11382777
REFERENCE   9  (residues 1 to 519)
  AUTHORS   Bruneau,B.G., Bao,Z.Z., Tanaka,M., Schott,J.J., Izumo,S.,
            Cepko,C.L., Seidman,J.G. and Seidman,C.E.
  TITLE     Cardiac expression of the ventricle-specific homeobox gene Irx4 is
            modulated by Nkx2-5 and dHand
  JOURNAL   Dev Biol 217 (2), 266-277 (2000)
   PUBMED   10625552
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Lewis,M.T., Ross,S., Strickland,P.A., Snyder,C.J. and Daniel,C.W.
  TITLE     Regulated expression patterns of IRX-2, an Iroquois-class homeobox
            gene, in the human breast
  JOURNAL   Cell Tissue Res 296 (3), 549-554 (1999)
   PUBMED   10370142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025183.5, AF124733.1, BC136505.1, BC110912.1 and AI566193.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            lacks an alternate internal exon compared to variant 4. It encodes
            isoform b which is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF124733.1, BC110912.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267757 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000231357.7/ ENSP00000231357.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.33"
     Protein         1..519
                     /product="iroquois-class homeodomain protein IRX-4 isoform
                     b"
                     /note="iroquois homeobox protein 4; homeodomain protein
                     IRXA3"
                     /calculated_mol_wt=54314
     Site            order(145..147,149,169,175,188,190..191,194..195,197..199,
                     201..202)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(145,148,191,194..195,198)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          161..199
                     /region_name="Homeobox_KN"
                     /note="Homeobox KN domain; pfam05920"
                     /db_xref="CDD:428673"
     Region          204..298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78413.2)"
     CDS             1..519
                     /gene="IRX4"
                     /gene_synonym="IRXA3"
                     /coded_by="NM_016358.3:279..1838"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS3867.1"
                     /db_xref="GeneID:50805"
                     /db_xref="HGNC:HGNC:6129"
                     /db_xref="MIM:606199"
ORIGIN      
        1 msypqfgypy ssapqflmat nslstccesg grtladsgpa asaqapvycp vyesrllata
       61 rhelnsaaal gvyggpyggs qgygnyvtyg seasafysln sfdskdgsgs ahgglapaaa
      121 ayypyepalg qypydrygtm dsgtrrknat rettstlkaw lqehrknpyp tkgekimlai
      181 itkmtltqvs twfanarrrl kkenkmtwpp rnkcadekrp yaegeeeegg eeeareeplk
      241 ssknaepvgk eekelelsdl ddfdpleaep pacelkppfh sldgglervp aapdgpvkea
      301 sgalrmslaa gggaaldedl erarsclrsa aagpeplpga eggpqvceak lgfvpagasa
      361 gleakpriws lahtataaaa aatslsqtef pscmlkrqgp aapaavssap atspsvalph
      421 sgaldrhqds pvtslrnwvd gvfhdpilrh stlnqawata kgalldpgpl grslgaganv
      481 ltaplarafp pavpqdapaa gaarellalp kaggkpfca
//
LOCUS       NP_078798                207 aa            linear   PRI 27-APR-2025
DEFINITION  sodium/potassium-transporting ATPase subunit beta-1-interacting
            protein 1 precursor [Homo sapiens].
ACCESSION   NP_078798
VERSION     NP_078798.2
DBSOURCE    REFSEQ: accession NM_024522.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Wang,X., Yang,F., Sun,Z., Zhao,G., Pu,Q., Geng,C., Dong,K.,
            Zhang,X., Liu,Z. and Song,H.
  TITLE     NKAIN1, as an oncogene, promotes the proliferation and metastasis
            of breast cancer, affecting its prognosis
  JOURNAL   Mol Carcinog 63 (7), 1392-1405 (2024)
   PUBMED   38651944
  REMARK    GeneRIF: NKAIN1, as an oncogene, promotes the proliferation and
            metastasis of breast cancer, affecting its prognosis.
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Zuo,L., Wang,K., Zhang,X.Y., Krystal,J.H., Li,C.S., Zhang,F.,
            Zhang,H. and Luo,X.
  TITLE     NKAIN1-SERINC2 is a functional, replicable and genome-wide
            significant risk gene region specific for alcohol dependence in
            subjects of European descent
  JOURNAL   Drug Alcohol Depend 129 (3), 254-264 (2013)
   PUBMED   23455491
  REMARK    GeneRIF: NKAIN1-SERINC2 gene expression is associated with alcohol
            dependence in subjects of European descent.
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Gorokhova,S., Bibert,S., Geering,K. and Heintz,N.
  TITLE     A novel family of transmembrane proteins interacting with beta
            subunits of the Na,K-ATPase
  JOURNAL   Hum Mol Genet 16 (20), 2394-2410 (2007)
   PUBMED   17606467
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB499136.2, AI884789.1, AK299507.1, AK298874.1, AK022712.1 and
            AL832547.1.
            
            On May 20, 2010 this sequence version replaced NP_078798.1.
            
            Summary: NKAIN1 is a member of a family of mammalian proteins with
            similarity to Drosophila Nkain and interacts with the beta subunit
            of Na,K-ATPase (ATP1B1; MIM 182330) (Gorokhova et al., 2007 [PubMed
            17606467]).[supplied by OMIM, Jun 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.195151.1,
                                           SRR1803617.85303.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267762 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373736.7/ ENSP00000362841.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..207
                     /product="sodium/potassium-transporting ATPase subunit
                     beta-1-interacting protein 1 precursor"
                     /note="family with sequence similarity 77, member C;
                     sodium/potassium-transporting ATPase subunit
                     beta-1-interacting protein 1; Na(+)/K(+)-transporting
                     ATPase subunit beta-1-interacting protein 1; Na+/K+
                     transporting ATPase interacting 1"
                     /calculated_mol_wt=21396
     Region          1..206
                     /region_name="NKAIN"
                     /note="Na,K-Atpase Interacting protein; pfam05640"
                     /db_xref="CDD:461699"
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4KMZ8.3)"
                     /calculated_mol_wt=2175
     mat_peptide     22..207
                     /product="Sodium/potassium-transporting ATPase subunit
                     beta-1-interacting protein 1. /id=PRO_0000412169"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMZ8.3)"
                     /calculated_mol_wt=21396
     Site            35..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMZ8.3)"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMZ8.3)"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4KMZ8.3)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMZ8.3)"
     CDS             1..207
                     /gene="NKAIN1"
                     /gene_synonym="FAM77C"
                     /coded_by="NM_024522.3:341..964"
                     /db_xref="CCDS:CCDS339.2"
                     /db_xref="GeneID:79570"
                     /db_xref="HGNC:HGNC:25743"
                     /db_xref="MIM:612871"
ORIGIN      
        1 mgkcsgrctl vafcclqlva alerqifdfl gyqwapilan flhimavilg ifgtvqyrsr
       61 ylilyaawlv lwvgwnafii cfylevgqls qdrdfimtfn tslhrswwme ngpgclvtpv
      121 lnsrlaledh hvisvtgcll dypyiealss alqiflalfg fvfacyvskv fleeedsfdf
      181 iggfdsygyq apqktshlql qplytsg
//
LOCUS       NP_001353629             185 aa            linear   PLN 27-APR-2025
DEFINITION  CASP-like protein 2C3 [Zea mays].
ACCESSION   NP_001353629
VERSION     NP_001353629.1
DBSOURCE    REFSEQ: accession NM_001366700.1
KEYWORDS    RefSeq.
SOURCE      Zea mays
  ORGANISM  Zea mays
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD
            clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
            Zea.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Alexandrov,N.N., Brover,V.V., Freidin,S., Troukhan,M.E.,
            Tatarinova,T.V., Zhang,H., Swaller,T.J., Lu,Y.P., Bouck,J.,
            Flavell,R.B. and Feldmann,K.A.
  TITLE     Insights into corn genes derived from large-scale cDNA sequencing
  JOURNAL   Plant Mol Biol 69 (1-2), 179-194 (2009)
   PUBMED   18937034
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Gardiner,J., Schroeder,S., Polacco,M.L., Sanchez-Villeda,H.,
            Fang,Z., Morgante,M., Landewe,T., Fengler,K., Useche,F.,
            Hanafey,M., Tingey,S., Chou,H., Wing,R., Soderlund,C. and Coe,E.H.
            Jr.
  TITLE     Anchoring 9,371 maize expressed sequence tagged unigenes to the
            bacterial artificial chromosome contig map by two-dimensional
            overgo hybridization
  JOURNAL   Plant Physiol 134 (4), 1317-1326 (2004)
   PUBMED   15020742
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EU958072.1 and FL049324.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU958072.1, SRR3147039.24846.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00780084, SAMN00780085
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Zea mays"
                     /db_xref="taxon:4577"
                     /chromosome="9"
                     /map="9"
     Protein         1..185
                     /product="CASP-like protein 2C3"
                     /note="zmCASPL2C2; zmCASPL2C3; membrane protein 11;
                     CASP-like protein 10; CASP-like protein 2C2"
                     /calculated_mol_wt=19140
     Site            14..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B6SZA7.1)"
     Region          34..159
                     /region_name="CASP_dom"
                     /note="Casparian strip membrane protein domain; pfam04535"
                     /db_xref="CDD:367980"
     Site            54..74
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B6SZA7.1)"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B6SZA7.1)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B6SZA7.1)"
     CDS             1..185
                     /gene="LOC100284498"
                     /gene_synonym="GRMZM2G055273"
                     /coded_by="NM_001366700.1:213..770"
                     /db_xref="GeneID:100284498"
ORIGIN      
        1 maaaarvsev kaegllrgac aalaaaaall vglstqtetv llvrkkatvk dvqalwvlam
       61 aaaaaagyhl lqllkclylg rvggarpcrr ssralawtcl lldkacaytt fattvaaaqa
      121 cvvaldgaha vqwtklcniy trfceqvags lvlgmlaavg tavlsaasar nvfrhyssle
      181 tyaah
//
LOCUS       NP_775760               1585 aa            linear   PRI 27-APR-2025
DEFINITION  maestro heat-like repeat-containing protein family member 2B [Homo
            sapiens].
ACCESSION   NP_775760
VERSION     NP_775760.3
DBSOURCE    REFSEQ: accession NM_173489.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1585)
  AUTHORS   Stanger,S.J., Law,E.A., Jamsai,D., O'Bryan,M.K., Nixon,B.,
            McLaughlin,E.A., Aitken,R.J. and Roman,S.D.
  TITLE     A novel germ cell protein, SPIF (sperm PKA interacting factor), is
            essential for the formation of a PKA/TCP11 complex that undergoes
            conformational and phosphorylation changes upon capacitation
  JOURNAL   FASEB J 30 (8), 2777-2791 (2016)
   PUBMED   27105888
REFERENCE   2  (residues 1 to 1585)
  AUTHORS   Kallio,S.P., Jakkula,E., Purcell,S., Suvela,M., Koivisto,K.,
            Tienari,P.J., Elovaara,I., Pirttila,T., Reunanen,M., Bronnikov,D.,
            Viander,M., Meri,S., Hillert,J., Lundmark,F., Harbo,H.F.,
            Lorentzen,A.R., De Jager,P.L., Daly,M.J., Hafler,D.A., Palotie,A.,
            Peltonen,L. and Saarela,J.
  TITLE     Use of a genetic isolate to identify rare disease variants: C7 on
            5p associated with MS
  JOURNAL   Hum Mol Genet 18 (9), 1670-1683 (2009)
   PUBMED   19221116
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF979306.1, BC034600.1, AC114967.2, BC052962.1, CR749346.1,
            BC044937.1 and AK128183.1.
            
            On Jul 31, 2007 this sequence version replaced NP_775760.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052962.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399564.5/ ENSP00000382476.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1585
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.1"
     Protein         1..1585
                     /product="maestro heat-like repeat-containing protein
                     family member 2B"
                     /note="HEAT repeat family member B2; HEAT
                     repeat-containing protein 7B2; HEAT repeat family member
                     7B2; sperm PKA-interacting factor"
                     /calculated_mol_wt=180650
     Region          28..65
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          228..263
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          272..309
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          310..346
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          405..445
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          531..569
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          572..611
                     /region_name="HEAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          662..699
                     /region_name="HEAT 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          777..819
                     /region_name="HEAT 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          964..1001
                     /region_name="HEAT 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          1021..1059
                     /region_name="HEAT 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          1112..1151
                     /region_name="HEAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          1157..1195
                     /region_name="HEAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          1258..1295
                     /region_name="HEAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          1306..1329
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(1321..1322,1325,1328..1329,1359..1360,1367,
                     1370..1371,1374,1405..1406,1409,1412..1413,1423,
                     1450..1451,1454,1457..1458)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          1341..1374
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1363..1402
                     /region_name="HEAT 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z745.3)"
     Region          1387..1424
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1433..1458
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..1585
                     /gene="MROH2B"
                     /gene_synonym="HEATR7B2; SPIF"
                     /coded_by="NM_173489.5:491..5248"
                     /db_xref="CCDS:CCDS47202.1"
                     /db_xref="GeneID:133558"
                     /db_xref="HGNC:HGNC:26857"
                     /db_xref="MIM:620930"
ORIGIN      
        1 mtlsteesie mfgdinltlg mlnkedivnk ediyshltsv iqntdildda ivqrliyyas
       61 kdmrdnnmlr eirmlagevl vslaahdfns vmyevqsnfr ilelpdefvv lalaelatsy
      121 vsqsipfmmm tlltmqtmlr laedermkgt fcialekfsk aiykyvnhwr dfpyprldan
      181 rlsdkifmlf wyimekwapl aspmqtlsiv kahgptvsll lhredfrgya lgqvpwllnq
      241 ykdkeidfhv tqslkqilta avlydiglpr slrrsifinl lqqicrapep pvkenemkas
      301 scflilahsn pgelmeffde qvrsnneair vgiltllrla vnadeprlrd hiisiertvk
      361 ivmgdlstkv rnsvllliqt mceksyiear egwplidyvf sqfatlnrnl ekpvktnfhe
      421 nekeeesvre tslevlktld plvigmpqvl wpriltfvvp aeytealepl fsiirilima
      481 eekkqhsake stalvvstga vklpspqqll arllvismpa slgelrgaga igllkilpei
      541 ihpklvdlwk trlpellqpl egknistvlw etmllqllke slwkisdvaw tiqltqdfkq
      601 qmgsysnnst ekkflwkalg ttlaccqdsd fvnsqikefl tapnqlgdqr qgitsilgyc
      661 aenhldivlk vlktfqnqek ffmnrckslf sgkksltktd vmviygaval hapkkqllsr
      721 lnqdiisqvl slhgqcsqvl gmsvmnkdmd lqmsftrsit eigiavqdae dqgfqfsyke
      781 mligymldfi rdepldslas pirwkaliai rylsklkpql slqdhlnile enirrllplp
      841 plenlksegq tdkdkehiqf lyersmdalg kllktmmwdn vnaedcqemf nllqmwlvsq
      901 kewererafq itakvltndi eapenfkigs llgllaphsc dtlptirqaa asstiglfyi
      961 kgihleverl qglqeglesd dvqvqikiss kiakivskfi pneeilmfle emldglesln
     1021 ptctkacgiw mitvlkqqga aledqlleil gtiyhhmpvl rqkeesfqfi leaisqiasf
     1081 hmdtvvvnll qkplpfdrdt ktlwkalaek passgkllqa lidkletele ddiarveais
     1141 vacamyevis mgtsvtglyp elftlllklv sctlgqkmlt cpwshrrhvm qqgeqqqipd
     1201 pcrlstatlk clqaqamreg lakesdegdn lwtllsspst hhigvcslar smavwqhgvi
     1261 ldimeqllss ltsssenyri tgaaffselm kepilwkhgn lrnvlilmdq sawdsnatlr
     1321 qmairglgnt asgaphkvkk hkqlmlesii rglyhlarte vvceslkalk kilelltdrd
     1381 vsfyfkeivl qtrtffedeq ddvrltaifl fedlapltgr rwkiffaeei kkslisfllh
     1441 lwdpnpkigv acrdvlmvci pflglqelyg vldrlldqdl prardfyrqf cvklakknqe
     1501 ilwilhthsf tfftstwevi rsaavkltda vvlnltsqyv elldreqltt rlqalrqdpc
     1561 isvqraaeaa lqtllrrcke tsipl
//
LOCUS       NP_872587                996 aa            linear   PRI 27-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 2 isoform A
            [Homo sapiens].
ACCESSION   NP_872587 XP_001130717
VERSION     NP_872587.2
DBSOURCE    REFSEQ: accession NM_182646.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Zhao,G., Zhao,Z., Xia,M., Xiao,L., Zhu,B., Wang,H., Li,X. and Di,J.
  TITLE     CPEB2 inhibit cell proliferation through upregulating p21 mRNA
            stability in glioma
  JOURNAL   Sci Rep 13 (1), 23103 (2023)
   PUBMED   38158431
  REMARK    GeneRIF: CPEB2 inhibit cell proliferation through upregulating p21
            mRNA stability in glioma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Zeng,P., Wang,F., Long,X., Cao,Y., Wen,F., Li,J. and Luo,Z.
  TITLE     CPEB2 enhances cell growth and angiogenesis by upregulating ARPC5
            mRNA stability in multiple myeloma
  JOURNAL   J Orthop Surg Res 18 (1), 384 (2023)
   PUBMED   37231521
  REMARK    GeneRIF: CPEB2 enhances cell growth and angiogenesis by
            upregulating ARPC5 mRNA stability in multiple myeloma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Zhang,M., Yang,C., Ruan,X., Liu,X., Wang,D., Liu,L., Shao,L.,
            Wang,P., Dong,W. and Xue,Y.
  TITLE     CPEB2 m6A methylation regulates blood-tumor barrier permeability by
            regulating splicing factor SRSF5 stability
  JOURNAL   Commun Biol 5 (1), 908 (2022)
   PUBMED   36064747
  REMARK    GeneRIF: CPEB2 m6A methylation regulates blood-tumor barrier
            permeability by regulating splicing factor SRSF5 stability.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 996)
  AUTHORS   Di,J., Zhao,G., Wang,H., Wu,Y., Zhao,Z., Zhu,B., Zhang,Y.,
            Zheng,J., Liu,Y. and Hu,Y.
  TITLE     A p53/CPEB2 negative feedback loop regulates renal cancer cell
            proliferation and migration
  JOURNAL   J Genet Genomics 48 (7), 606-617 (2021)
   PUBMED   34362680
  REMARK    GeneRIF: A p53/CPEB2 negative feedback loop regulates renal cancer
            cell proliferation and migration.
REFERENCE   5  (residues 1 to 996)
  AUTHORS   Pascual,R., Martin,J., Salvador,F., Reina,O., Chanes,V.,
            Millanes-Romero,A., Suner,C., Fernandez-Miranda,G., Bartomeu,A.,
            Huang,Y.S., Gomis,R.R. and Mendez,R.
  TITLE     The RNA binding protein CPEB2 regulates hormone sensing in mammary
            gland development and luminal breast cancer
  JOURNAL   Sci Adv 6 (20), eaax3868 (2020)
   PUBMED   32440535
  REMARK    GeneRIF: The RNA binding protein CPEB2 regulates hormone sensing in
            mammary gland development and luminal breast cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 996)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 996)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 996)
  AUTHORS   Peng,S.C., Lai,Y.T., Huang,H.Y., Huang,H.D. and Huang,Y.S.
  TITLE     A novel role of CPEB3 in regulating EGFR gene transcription via
            association with Stat5b in neurons
  JOURNAL   Nucleic Acids Res 38 (21), 7446-7457 (2010)
   PUBMED   20639532
REFERENCE   9  (residues 1 to 996)
  AUTHORS   Hagele,S., Kuhn,U., Boning,M. and Katschinski,D.M.
  TITLE     Cytoplasmic polyadenylation-element-binding protein (CPEB)1 and 2
            bind to the HIF-1alpha mRNA 3'-UTR and modulate HIF-1alpha protein
            expression
  JOURNAL   Biochem J 417 (1), 235-246 (2009)
   PUBMED   18752464
REFERENCE   10 (residues 1 to 996)
  AUTHORS   Kurihara,Y., Tokuriki,M., Myojin,R., Hori,T., Kuroiwa,A.,
            Matsuda,Y., Sakurai,T., Kimura,M., Hecht,N.B. and Uesugi,S.
  TITLE     CPEB2, a novel putative translational regulator in mouse haploid
            germ cells
  JOURNAL   Biol Reprod 69 (1), 261-268 (2003)
   PUBMED   12672660
  REMARK    GeneRIF: Functional studies of the mouse homolog
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105289.4, AY255519.1 and
            AC098829.3.
            
            On Apr 7, 2010 this sequence version replaced NP_872587.1.
            
            Summary: The protein encoded by this gene is highly similar to
            cytoplasmic polyadenylation element binding protein (CPEB), an
            mRNA-binding protein that regulates cytoplasmic polyadenylation of
            mRNA as a trans factor in oogenesis and spermatogenesis. Studies of
            the similar gene in mice suggested a possible role of this protein
            in transcriptionally inactive haploid spermatids. Alternatively
            spliced transcript variants encoding distinct isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (A) lacks an alternate in-frame
            exon in the central coding region, compared to variant D. The
            resulting isoform (A) lacks an internal segment, compared to
            isoform D.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The genomic coordinates used for
            the transcript record were based on alignments. The 5' CDS is
            inferred based on comparison of the mouse and human orthologs.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY255519.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.32"
     Protein         1..996
                     /product="cytoplasmic polyadenylation element-binding
                     protein 2 isoform A"
                     /note="CPE-binding protein 2"
                     /calculated_mol_wt=105452
     Region          739..830
                     /region_name="RRM1_CPEB2_like"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein CPEB-2, CPEB-3,
                     CPEB-4 and similar protiens; cd12724"
                     /db_xref="CDD:410123"
     Region          847..927
                     /region_name="RRM2_CPEB2_like"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein CPEB-2, CPEB-3,
                     CPEB-4 and similar protiens; cd12726"
                     /db_xref="CDD:410125"
     Region          922..983
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..996
                     /gene="CPEB2"
                     /gene_synonym="CPE-BP2; CPEB-2; hCPEB-2"
                     /coded_by="NM_182646.3:194..3184"
                     /note="isoform A is encoded by transcript variant A"
                     /db_xref="GeneID:132864"
                     /db_xref="HGNC:HGNC:21745"
                     /db_xref="MIM:610605"
ORIGIN      
        1 mrdfgfgvlq taplrssspg plfcgeaygp yavgsvnplp satpfgplsp pplpvtgfle
       61 aaspfsvplg ggagspaaaa sssspflahq qtmqdelllg ltqqparpls gaaateklpd
      121 hhpgggtiag vthllpsqdf kpslhhpsss sassccccrt sspqdfskrq qqqlssqkrk
      181 efspphlphp pdskpppppp plhcpgrfsp ppppagpllq paqlaqrqqq qppqqfsllh
      241 qqhlspqdfa prqrpadlpp lpqlppsppa aprrrhggag sprktpaage gsaaespnag
      301 lasstpvnpa pgsmespnhp llnspsnllp ggalgagafs slqspdlphp gggggggggg
      361 ppgggggggs asppplpgfg tpwsvqtasp ppqpqqpppt qpqqqppppq qppqpqpqpp
      421 gssattpggg sggslsampp pspdsengfy pglpssmnpa ffpsfspvsp hgctglsvpt
      481 sggggggfgg pfsatavppp pppamnipqq qppppaapqq pqsrrspvsp qlqqqhqaaa
      541 aaflqqrnsy nhhqpllkqs pwsnhqssgw gtgsmswgam hgrdhrrtgn mgipgtmnqi
      601 splkkpfsgn viappkftrs tpsltpkswi ednvfrtdnn sntllplqdr srmydslnmh
      661 slenslidim raehdplkgr lsyphpgtdn llmlngrssl fpiddglldd ghsdqvgvln
      721 sptcysahqn gerierfsrk vfvgglppdi dedeitasfr rfgplvvdwp hkaesksyfp
      781 pkgyafllfq eessvqalid acieedgkly lcvssptikd kpvqirpwnl sdsdfvmdgs
      841 qpldprktif vggvprplra velamimdrl yggvcyagid tdpelkypkg agrvafsnqq
      901 syiaaisarf vqlqhgdidk rvevkpyvld dqmcdecqga rcggkfapff canvtclqyy
      961 cefcwanihs ragrefhkpl vkegadrprq ihfrwn
//
LOCUS       NP_001352972             448 aa            linear   PRI 27-APR-2025
DEFINITION  protein ABHD18 isoform 12 [Homo sapiens].
ACCESSION   NP_001352972
VERSION     NP_001352972.1
DBSOURCE    REFSEQ: accession NM_001366043.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099340.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.134742.1,
                                           SRR1803616.31390.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.2"
     Protein         1..448
                     /product="protein ABHD18 isoform 12"
                     /note="abhydrolase domain-containing protein 18;
                     alpha/beta hydrolase domain-containing protein 18; protein
                     ABHD18"
                     /calculated_mol_wt=50959
     Region          16..448
                     /region_name="ABHD18"
                     /note="Alpha/beta hydrolase domain containing 18;
                     pfam09752"
                     /db_xref="CDD:370661"
     CDS             1..448
                     /gene="ABHD18"
                     /gene_synonym="C4orf29"
                     /coded_by="NM_001366043.1:219..1565"
                     /note="isoform 12 is encoded by transcript variant 14"
                     /db_xref="GeneID:80167"
                     /db_xref="HGNC:HGNC:26111"
ORIGIN      
        1 mgvskldily rrllltklfi rgwgrpedlk rlfefrkmig nrercqnlvs sdypvhidki
       61 eeqsdckild ghfvspmahy vpdimpiesv iarfqfivpk ewnskyrpvc ihlagtgdhh
      121 ywrrrtlmar pmikearmas lllenpyygc rkpkdqvrss lknvsdlfvm ggalvlesaa
      181 llhwleregy gplgmtgism gghmaslavs nwpkpmplip clswstasgv fttgvlsksi
      241 nwrelekqyy tqtvyeeeii hmleycgtds fkmgqefvkh ftssadkltn lnlvsrtlnl
      301 disnqvvsqk padchnsskt svsatsegll lqdtskmkrf nqtlstnksg ytsrnpqsyh
      361 llskeqsrns lrkeslifmk gvmdecthva nfsvpvdpsl iivvqakeda yiprtgvrsl
      421 qeiwpgceir ylegghisay lfkqglfr
//
LOCUS       NP_001348958             823 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 11 [Mus musculus].
ACCESSION   NP_001348958
VERSION     NP_001348958.1
DBSOURCE    REFSEQ: accession NM_001362029.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 823)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 823)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 823)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 823)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 823)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 823)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 823)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            Transcript Variant: This variant (39), as well as variant 38,
            encodes isoform 11.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164131
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..823
                     /product="cAMP-regulated phosphoprotein 21 isoform 11"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=89886
     Region          162..223
                     /region_name="R3H_encore_like"
                     /note="R3H domain of encore-like and DIP1-like proteins.
                     Drosophila encore is involved in the germline exit after
                     four mitotic divisions, by facilitating
                     SCF-ubiquitin-proteasome-dependent proteolysis. Maize
                     DBF1-interactor protein 1 (DIP1) containing an R3H...;
                     cd02642"
                     /db_xref="CDD:100071"
     Site            order(195,199)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100071"
     Region          244..299
                     /region_name="SUZ"
                     /note="SUZ domain; pfam12752"
                     /db_xref="CDD:463689"
     Region          569..>798
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..823
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362029.1:474..2945"
                     /note="isoform 11 is encoded by transcript variant 39"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqesih lqlssfpslq eedksrkdds erekekdknr
      121 eklserpkir mlskdcsqey tdstgidlhg flintlknns rdrmillkme qemidfiads
      181 nnhykkfpqm ssyqrmlvhr vaayfgldhn vdqtgksvii nktsstripe qrfcehlkde
      241 kseesqkrfi lkrdnssidk ednqqnrmhp frddrrsksi eereeeyqrv rerifahdsv
      301 csqeslfldn rahrdssgrt sgsrqssset elrwpdhqra wsstdsdssn rnlkptmtkt
      361 asfggitvlt rgdstsstrs agklsktgse ssssagssgs lsrthpqsta ltssvaagsp
      421 gcmaysengm ggqvppssts yillplesat gippgsilln phtgqpfvnp dgtpaiynpp
      481 gsqqtlrgtv ggqpqqppqq qpspqpqqqv qasqpqmagp lvtqsvqslq pssqsvqypa
      541 vsfppqhllp msptqhfplr eelaaqfsql smsrqssgdt peppsgtvyp asllpqtaqp
      601 qsyvitsagq qlstggfsds gppisqqvlq appspqgfvq qpppaqmsvy yypsgqypts
      661 tsqqyrplas vqysaqrsqq ipqttqqagy qpvlsgqqgf qgmmgvqqsa hsqgvmssqq
      721 gapvhgvmvs yptmssyqvp mtqgsqavpq qtyqppimlp sqagqgslpa tgmpvycnvt
      781 ppnpqnnlrl mgphcpsstv pvmsascrtn cgnvsnagwq vkf
//
LOCUS       NP_001348467             574 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM23 isoform 1 [Mus musculus].
ACCESSION   NP_001348467 XP_006517857
VERSION     NP_001348467.1
DBSOURCE    REFSEQ: accession NM_001361538.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Quan,W. and Wang,L.
  TITLE     Tripartite motif containing 23 functions as a critical regulator in
            macrophages to control the pathological feature of diabetic
            nephropathy
  JOURNAL   Int Urol Nephrol 55 (5), 1263-1270 (2023)
   PUBMED   36449224
  REMARK    GeneRIF: Tripartite motif containing 23 functions as a critical
            regulator in macrophages to control the pathological feature of
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Cao,X., Zhou,Z., Tian,Y., Liu,Z., Cheng,K.O., Chen,X., Hu,W.,
            Wong,Y.M., Li,X., Zhang,H., Hu,R. and Huang,P.
  TITLE     Opposing roles of E3 ligases TRIM23 and TRIM21 in regulation of ion
            channel ANO1 protein levels
  JOURNAL   J Biol Chem 296, 100738 (2021)
   PUBMED   33957127
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Watanabe,M., Takahashi,H., Saeki,Y., Ozaki,T., Itoh,S., Suzuki,M.,
            Mizushima,W., Tanaka,K. and Hatakeyama,S.
  TITLE     The E3 ubiquitin ligase TRIM23 regulates adipocyte differentiation
            via stabilization of the adipogenic activator PPARgamma
  JOURNAL   Elife 4, e05615 (2015)
   PUBMED   25905670
  REMARK    GeneRIF: TRIM23 regulates adipocyte differentiation via
            stabilization of the adipogenic activator PPARgamma2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Arimoto,K., Funami,K., Saeki,Y., Tanaka,K., Okawa,K., Takeuchi,O.,
            Akira,S., Murakami,Y. and Shimotohno,K.
  TITLE     Polyubiquitin conjugation to NEMO by triparite motif protein 23
            (TRIM23) is critical in antiviral defense
  JOURNAL   Proc Natl Acad Sci U S A 107 (36), 15856-15861 (2010)
   PUBMED   20724660
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Kudryashova,E., Wu,J., Havton,L.A. and Spencer,M.J.
  TITLE     Deficiency of the E3 ubiquitin ligase TRIM32 in mice leads to a
            myopathy with a neurogenic component
  JOURNAL   Hum Mol Genet 18 (7), 1353-1367 (2009)
   PUBMED   19155210
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK039280.1 and AC154216.1.
            
            On Mar 26, 2018 this sequence version replaced XP_006517857.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK039280.1, AK036210.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 56.35 cM"
     Protein         1..574
                     /product="E3 ubiquitin-protein ligase TRIM23 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="ADP-ribosylation factor domain protein 1, 64kD;
                     tripartite motif protein TRIM23; GTP-binding protein
                     ARD-1; E3 ubiquitin-protein ligase TRIM23; tripartite
                     motif-containing protein 23; ADP-ribosylation factor
                     domain-containing protein 1; RING-type E3 ubiquitin
                     transferase TRIM23"
                     /calculated_mol_wt=63801
     Region          28..77
                     /region_name="mRING-HC-C3HC3D_TRIM23_C-IX"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in tripartite motif-containing protein 23 (TRIM23)
                     and similar proteins; cd16645"
                     /db_xref="CDD:438307"
     Region          123..172
                     /region_name="Bbox2_TRIM23_C-IX_rpt1"
                     /note="first B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 23 (TRIM23) and similar proteins;
                     cd19773"
                     /db_xref="CDD:380831"
     Region          174..223
                     /region_name="Bbox2_TRIM23_C-IX_rpt2"
                     /note="second B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 23 (TRIM23) and similar proteins;
                     cd19774"
                     /db_xref="CDD:380832"
     Region          226..370
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          390..574
                     /region_name="ARF-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGX0.1)"
     Region          406..574
                     /region_name="ARD1"
                     /note="(ADP-ribosylation factor domain protein 1 (ARD1);
                     cd04158"
                     /db_xref="CDD:206723"
     Site            411..418
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206723"
     Site            order(413..419,434..435,457,513..514,516,547..549)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206723"
     Site            order(413..414,418,422,434..441,463,468)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206723"
     Site            423..438
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206723"
     Site            order(435..439,444,454,458,464,466..468)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206723"
     Site            435
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206723"
     Site            order(436..443,453,464,467..468)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206723"
     Site            439..453
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206723"
     Site            order(445..448,555..558)
                     /site_type="other"
                     /note="YxxL localization motifs"
                     /db_xref="CDD:206723"
     Site            454..471
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206723"
     Site            454..457
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206723"
     Site            513..516
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206723"
     Site            547..549
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206723"
     CDS             1..574
                     /gene="Trim23"
                     /gene_synonym="6330516O20Rik; Arfd1"
                     /coded_by="NM_001361538.1:43..1767"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS88515.1"
                     /db_xref="GeneID:81003"
                     /db_xref="MGI:MGI:1933161"
ORIGIN      
        1 maalavnkpg agvdsgrqgs rgtavvkvle cgvcedvfsl qgdkvprlll cghtvchdcl
       61 trlplhgrai rcpfdrqvtd lgdsgvwglk knfallelle rlqnghigqy gaaeeaigts
      121 gesiircded eahvasvyct vcathlcsdc sqvthstktl akhrrvplad kphektmccq
      181 hqvhaiefvc leegcqtspl mccvckeygk hqghkhsvle peanqirasi ldmahcirtf
      241 teeisdysrk lvgivqhieg geqivedgig mahtehvpgt aenarscvra yfsdlhetlc
      301 rqeemalsvv dahvrekliw lrqqqedmti llsqvstacl hcektlqqdd crvvlakqei
      361 trlletlqkq qqqftevadh iqldasipvt ftkdnrvhig pkmeirvvtl gldgagktti
      421 lfklkqdefm qpiptigfnv etveyknlkf tiwdvggkhk lrplwkhyyl ntqavvfvvd
      481 sshrdrisea hselakllte kelrdallli fankqdvaga lsveeitell slhklccgrs
      541 wyiqgcdars gmglyegldw lsrqlvaagv ldva
//
LOCUS       NP_001248363             412 aa            linear   PRI 27-APR-2025
DEFINITION  alanyl-tRNA editing protein Aarsd1 [Homo sapiens].
ACCESSION   NP_001248363
VERSION     NP_001248363.1
DBSOURCE    REFSEQ: accession NM_001261434.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Echeverria,P.C., Briand,P.A. and Picard,D.
  TITLE     A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel
            Cochaperone Aarsd1 Is Required for Muscle Differentiation
  JOURNAL   Mol Cell Biol 36 (8), 1310-1321 (2016)
   PUBMED   26884463
  REMARK    GeneRIF: Aarsd1 inhibits the activity of a paradigmatic Hsp90
            client protein.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   5  (residues 1 to 412)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Miki,Y., Swensen,J., Shattuck-Eidens,D., Futreal,P.A., Harshman,K.,
            Tavtigian,S., Liu,Q., Cochran,C., Bennett,L.M., Ding,W. et al.
  TITLE     A strong candidate for the breast and ovarian cancer susceptibility
            gene BRCA1
  JOURNAL   Science 266 (5182), 66-71 (1994)
   PUBMED   7545954
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP368900.1, AC055866.19, AL515977.3 and AW296090.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1177615.1,
                                           SRR5189652.51095.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2159080
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000427569.7/ ENSP00000400870.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..412
                     /product="alanyl-tRNA editing protein Aarsd1"
                     /note="alanyl-tRNA synthetase domain-containing protein 1"
                     /calculated_mol_wt=45349
     Region          5..235
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BTE6.2)"
     CDS             1..412
                     /gene="AARSD1"
                     /gene_synonym="AlaXp"
                     /coded_by="NM_001261434.2:15..1253"
                     /db_xref="CCDS:CCDS58552.1"
                     /db_xref="GeneID:80755"
                     /db_xref="HGNC:HGNC:28417"
                     /db_xref="MIM:613212"
ORIGIN      
        1 mafwcqrdsy areftttvvs ccpaelqteg sngkkevlsg fqvvledtvl fpegggqpdd
       61 rgtindisvl rvtrrgeqad hftqtpldpg sqvlvrvdwe rrfdhmqqhs gqhlitavad
      121 hlfklkttsw elgrfrsaie ldtpsmtaeq vaaieqsvne kirdrlpvnv relslddpev
      181 eqvsgrglpd dhagpirvvn iegvdsnmcc gthvsnlsdl qvikilgtek gkknrtnlif
      241 lsgnrvlkwm ershgtekal tallkcgaed hveavkklqn stkilqknnl nllrdlavhi
      301 ahslrnspdw ggvvilhrke gdsefmniia neigseetll fltvgdekgg glfllagppa
      361 svetlgprva evlegkgagk kgrfqgkatk msrrmeaqal lqdyistqsa ke
//
LOCUS       NP_002112                258 aa            linear   PRI 27-APR-2025
DEFINITION  HLA class II histocompatibility antigen, DP beta 1 chain precursor
            [Homo sapiens].
ACCESSION   NP_002112 XP_003119144 XP_003119145 XP_003119146 XP_003119147
            XP_003119148 XP_003119149
VERSION     NP_002112.3
DBSOURCE    REFSEQ: accession NM_002121.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Senapati,S., Singh,H., Bk,T., Verma,N. and Kumar,U.
  TITLE     HLA sequencing identifies novel associations and suggests clinical
            relevance of DPB1*04:01 in ANCA-associated Granulomatosis with
            polyangiitis
  JOURNAL   Gene 896, 148024 (2024)
   PUBMED   38040271
  REMARK    GeneRIF: HLA sequencing identifies novel associations and suggests
            clinical relevance of DPB1*04:01 in ANCA-associated Granulomatosis
            with polyangiitis.
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Akgollu,E., Demirkazik,M. and Bilgin,R.
  TITLE     The effect of HLA-DP gene polymorphisms in Plasmodium Vivax-induced
            malaria susceptibility
  JOURNAL   Nucleosides Nucleotides Nucleic Acids 43 (6), 572-584 (2024)
   PUBMED   37980631
  REMARK    GeneRIF: The effect of HLA-DP gene polymorphisms in Plasmodium
            Vivax-induced malaria susceptibility.
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Cargou,M., Elsermans,V., Top,I., Wojciechowski,E. and Visentin,J.
  TITLE     Characterization of the novel HLA-DPB1*11:01:06 allele by
            sequencing-based typing
  JOURNAL   HLA 101 (3), 311-312 (2023)
   PUBMED   36411507
  REMARK    GeneRIF: Characterization of the novel HLA-DPB1*11:01:06 allele by
            sequencing-based typing.
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Cargou,M., Elsermans,V., Top,I., Ralazamahaleo,M. and Visentin,J.
  TITLE     Characterization of the novel HLA-DPB1*1348:01 allele by
            sequencing-based typing
  JOURNAL   HLA 101 (3), 313-314 (2023)
   PUBMED   36394166
  REMARK    GeneRIF: Characterization of the novel HLA-DPB1*1348:01 allele by
            sequencing-based typing.
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Roh,E.Y., Lim,S., Shin,S. and Yoon,J.H.
  TITLE     The novel HLA-DPB1 allele, HLA-DPB1*1344:01, first identified in
            Korean individuals by next-generation sequencing
  JOURNAL   HLA 101 (1), 96-97 (2023)
   PUBMED   36074540
  REMARK    GeneRIF: The novel HLA-DPB1 allele, HLA-DPB1*1344:01, first
            identified in Korean individuals by next-generation sequencing.
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Marsh,S.G. and Bodmer,J.G.
  TITLE     HLA class II nucleotide sequences, 1992
  JOURNAL   Tissue Antigens 40 (5), 229-243 (1992)
   PUBMED   1362295
  REMARK    Correction to:[Tissue Antigens. 1992 Apr;39(4):161-73. doi:
            10.1111/j.1399-0039.1992.tb01932.x. PMID: 1529427]
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Eiermann,T.H., Uhl,S., Fakler,J. and Goldmann,S.F.
  TITLE     A novel HLA-DPB1 sequence, DPB1*2301
  JOURNAL   Tissue Antigens 40 (2), 108-110 (1992)
   PUBMED   1412416
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Mitsunaga,S., Kuwata,S., Tokunaga,K., Uchikawa,C., Takahashi,K.,
            Akaza,T., Mitomi,Y. and Juji,T.
  TITLE     Family study on HLA-DPB1 polymorphism: linkage analysis with
            HLA-DR/DQ and two 'new' alleles
  JOURNAL   Hum Immunol 34 (3), 203-211 (1992)
   PUBMED   1358867
REFERENCE   9  (residues 1 to 258)
  AUTHORS   Korioth,F., Hartung,K., Deicher,H. and Frey,J.
  TITLE     A new HLA-DPB1 allele from a patient with systemic lupus
            erythematosus
  JOURNAL   Tissue Antigens 39 (4), 216-219 (1992)
   PUBMED   1529429
REFERENCE   10 (residues 1 to 258)
  AUTHORS   de Koster,H.S., Kenter,M.J., D'Amaro,J., Luiten,R.M.,
            Schroeijers,W.E., Giphart,M.J. and Termijtelen,A.
  TITLE     Positive correlation between oligonucleotide typing and T-cell
            recognition of HLA-DP molecules
  JOURNAL   Immunogenetics 34 (1), 12-22 (1991)
   PUBMED   1713190
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP213121.1, M28202.1 and
            AL645931.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Nov 16, 2010 this sequence version replaced
            XP_003119146.1, XP_003119148.1, XP_003119144.1, XP_003119145.1,
            XP_003119147.1, XP_003119149.1, NP_002112.2.
            
            Summary: HLA-DPB belongs to the HLA class II beta chain paralogues.
            This class II molecule is a heterodimer consisting of an alpha
            (DPA) and a beta chain (DPB), both anchored in the membrane. It
            plays a central role in the immune system by presenting peptides
            derived from extracellular proteins. Class II molecules are
            expressed in antigen presenting cells (APC: B lymphocytes,
            dendritic cells, macrophages). The beta chain is approximately
            26-28 kDa and its gene contains 6 exons. Exon one encodes the
            leader peptide, exons 2 and 3 encode the two extracellular domains,
            exon 4 encodes the transmembrane domain and exon 5 encodes the
            cytoplasmic tail. Within the DP molecule both the alpha chain and
            the beta chain contain the polymorphisms specifying the peptide
            binding specificities, resulting in up to 4 different molecules.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.97053.1,
                                           SRR1163657.319583.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000418931.7/ ENSP00000408146.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..258
                     /product="HLA class II histocompatibility antigen, DP beta
                     1 chain precursor"
                     /note="HLA-DP histocompatibility type, beta-1 subunit; HLA
                     class II histocompatibility antigen, DP beta 1 chain; MHC
                     HLA DPB1; MHC class II HLA-DP-beta-1; MHC class II antigen
                     DPB1; HLA class II histocompatibility antigen, DP(W4) beta
                     chain"
                     /calculated_mol_wt=26164
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3014
     mat_peptide     30..258
                     /product="HLA class II histocompatibility antigen, DP beta
                     1 chain. /id=PRO_0000018984"
                     /note="propagated from UniProtKB/Swiss-Prot (P04440.1)"
                     /calculated_mol_wt=26164
     Region          30..121
                     /region_name="Beta-1"
                     /note="propagated from UniProtKB/Swiss-Prot (P04440.1)"
     Region          42..114
                     /region_name="MHC_II_beta"
                     /note="Class II histocompatibility antigen, beta domain;
                     pfam00969"
                     /db_xref="CDD:425967"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04440.1)"
     Region          121..216
                     /region_name="IgC1_MHC_II_beta_HLA-DP"
                     /note="Class II major histocompatibility complex (MHC)
                     beta chain immunoglobulin domain of histocompatibility
                     antigen (HLA) DP; member of the C1-set of Ig superfamily
                     (IgSF) domains; cd21003"
                     /db_xref="CDD:409594"
     Region          122..215
                     /region_name="Beta-2"
                     /note="propagated from UniProtKB/Swiss-Prot (P04440.1)"
     Region          123..131
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409594"
     Region          141..150
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409594"
     Region          154..160
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409594"
     Region          162..165
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409594"
     Region          169..177
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409594"
     Region          180..190
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409594"
     Region          197..204
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409594"
     Region          211..216
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409594"
     Region          216..225
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P04440.1)"
     Site            226..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04440.1)"
     CDS             1..258
                     /gene="HLA-DPB1"
                     /gene_synonym="DPB1; HLA-DP; HLA-DP1B; HLA-DPB"
                     /coded_by="NM_002121.6:53..829"
                     /db_xref="CCDS:CCDS4765.1"
                     /db_xref="GeneID:3115"
                     /db_xref="HGNC:HGNC:4940"
                     /db_xref="MIM:142858"
ORIGIN      
        1 mmvlqvsaap rtvaltallm vlltsvvqgr atpenylfqg rqecyafngt qrfleryiyn
       61 reefarfdsd vgefravtel grpaaeywns qkdileekra vpdrmcrhny elggpmtlqr
      121 rvqprvnvsp skkgplqhhn llvchvtdfy pgsiqvrwfl ngqeetagvv stnlirngdw
      181 tfqilvmlem tpqqgdvytc qvehtsldsp vtvewkaqsd sarsktltga ggfvlgliic
      241 gvgifmhrrs kkvqrgsa
//
LOCUS       NP_001356876             521 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 12 [Homo
            sapiens].
ACCESSION   NP_001356876
VERSION     NP_001356876.1
DBSOURCE    REFSEQ: accession NM_001369947.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.246433.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..521
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 12"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=59181
     Region          233..272
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..521
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369947.1:436..2001"
                     /note="isoform 12 is encoded by transcript variant 30"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mpllelkdiv lylcdtcttl wafldifpla cqtfqkhdfc yrlasfyeaa ipemesaikk
       61 rrledskllg dlwqrlshsr kklmeifhii lnqicllpil esscdniqgf ieeflqifss
      121 llqekrflrd ydalfpvaed isllqqassv ldetrtayil qavesawegv drrkatdakd
      181 psvieepnge pngvtvtaea vsqasshpen seeeecmgaa aavgpamcgv eldslisqvk
      241 dllpdlgegf ilacleyyhy dpeqvinnil eerlaptlsq ldrnldremk pdptplltsr
      301 hnvfqndefd vfsrdsvdls rvhkgkstrk eentrsllnd kravaaqrqr yeqysvvvee
      361 vplqpgeslp yhsvyyedey ddtydgnqvg andadsddel isrrpftipq vlrtkvpreg
      421 qeeddddeed dadeeapkpd hfvqdpavlr ekaearrmaf lakkgyrhds stavagsprg
      481 hgqsrettqe rrkkeankat ranhnrrtma drkrskgmip s
//
LOCUS       NP_067022                450 aa            linear   PRI 27-APR-2025
DEFINITION  sulfide:quinone oxidoreductase, mitochondrial [Homo sapiens].
ACCESSION   NP_067022
VERSION     NP_067022.1
DBSOURCE    REFSEQ: accession NM_021199.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Friederich,M.W., Elias,A.F., Kuster,A., Laugwitz,L., Larson,A.A.,
            Landry,A.P., Ellwood-Digel,L., Mirsky,D.M., Dimmock,D., Haven,J.,
            Jiang,H., MacLean,K.N., Styren,K., Schoof,J., Goujon,L.,
            Lefrancois,T., Friederich,M., Coughlin,C.R. 2nd, Banerjee,R.,
            Haack,T.B. and Van Hove,J.L.K.
  TITLE     Pathogenic variants in SQOR encoding sulfide:quinone oxidoreductase
            are a potentially treatable cause of Leigh disease
  JOURNAL   J Inherit Metab Dis 43 (5), 1024-1036 (2020)
   PUBMED   32160317
  REMARK    GeneRIF: Pathogenic variants in SQOR encoding sulfide:quinone
            oxidoreductase are a potentially treatable cause of Leigh disease.
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Jackson,M.R., Loll,P.J. and Jorns,M.S.
  TITLE     X-Ray Structure of Human Sulfide:Quinone Oxidoreductase: Insights
            into the Mechanism of Mitochondrial Hydrogen Sulfide Oxidation
  JOURNAL   Structure 27 (5), 794-805 (2019)
   PUBMED   30905673
  REMARK    GeneRIF: human SQOR contains unique features: an electropositive
            surface depression implicated as a binding site for sulfane sulfur
            acceptors and postulated to funnel negatively charged substrates to
            a hydrophilic H2S-oxidizing active site, which is connected to a
            hydrophobic internal tunnel that binds coenzyme Q
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Cai,X., Yi,X., Zhang,Y., Zhang,D., Zhi,L. and Liu,H.
  TITLE     Genetic susceptibility of postmenopausal osteoporosis on sulfide
            quinone reductase-like gene
  JOURNAL   Osteoporos Int 29 (9), 2041-2047 (2018)
   PUBMED   29855663
  REMARK    GeneRIF: The evidence supported the significant role of SQRDL in
            the etiology of postmenopausal osteoporosis and suggest that it may
            be a genetic risk factor for BMD and osteoporosis in Han Chinese
            postmenopausal women.
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Jackson,M.R., Melideo,S.L. and Jorns,M.S.
  TITLE     Human sulfide:quinone oxidoreductase catalyzes the first step in
            hydrogen sulfide metabolism and produces a sulfane sulfur
            metabolite
  JOURNAL   Biochemistry 51 (34), 6804-6815 (2012)
   PUBMED   22852582
  REMARK    GeneRIF: Sulfide:quinone oxidoreductase catalyzes the first step in
            hydrogen sulfide metabolism and produces a sulfane sulfur
            metabolite.
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Palmfeldt,J., Vang,S., Stenbroen,V., Pavlou,E., Baycheva,M.,
            Buchal,G., Monavari,A.A., Augoustides-Savvopoulou,P., Mandel,H. and
            Gregersen,N.
  TITLE     Proteomics reveals that redox regulation is disrupted in patients
            with ethylmalonic encephalopathy
  JOURNAL   J Proteome Res 10 (5), 2389-2396 (2011)
   PUBMED   21410200
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Lagoutte,E., Mimoun,S., Andriamihaja,M., Chaumontet,C., Blachier,F.
            and Bouillaud,F.
  TITLE     Oxidation of hydrogen sulfide remains a priority in mammalian cells
            and causes reverse electron transfer in colonocytes
  JOURNAL   Biochim Biophys Acta 1797 (8), 1500-1511 (2010)
   PUBMED   20398623
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Hildebrandt,T.M. and Grieshaber,M.K.
  TITLE     Three enzymatic activities catalyze the oxidation of sulfide to
            thiosulfate in mammalian and invertebrate mitochondria
  JOURNAL   FEBS J 275 (13), 3352-3361 (2008)
   PUBMED   18494801
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Vande Weghe,J.G. and Ow,D.W.
  TITLE     A fission yeast gene for mitochondrial sulfide oxidation
  JOURNAL   J Biol Chem 274 (19), 13250-13257 (1999)
   PUBMED   10224084
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA821218.1 and AF042284.1.
            
            Summary: The protein encoded by this gene may function in
            mitochondria to catalyze the conversion of sulfide to persulfides,
            thereby decreasing toxic concencrations of sulfide. Alternative
            splicing results in multiple transcript variants that encode the
            same protein. [provided by RefSeq, Sep 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222463.1, SRR3476690.361824.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000260324.12/
                                                  ENSP00000260324.7
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..450
                     /product="sulfide:quinone oxidoreductase, mitochondrial"
                     /EC_number="1.8.5.8"
                     /note="sulfide dehydrogenase like; sulfide quinone
                     reductase-like"
                     /calculated_mol_wt=49830
     Region          71..389
                     /region_name="FadH2"
                     /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur
                     reductase, or a related oxidoreductase [Lipid transport
                     and metabolism]; COG0446"
                     /db_xref="CDD:440215"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9R112; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6N5.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R112; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6N5.1)"
     CDS             1..450
                     /gene="SQOR"
                     /gene_synonym="CGI-44; PRO1975; SQR; SQRDL"
                     /coded_by="NM_021199.4:98..1450"
                     /db_xref="CCDS:CCDS10127.1"
                     /db_xref="GeneID:58472"
                     /db_xref="HGNC:HGNC:20390"
                     /db_xref="MIM:617658"
ORIGIN      
        1 mvplvavvsg praqlfacll rlgtqqvgpl qlhtgashaa rnhyevlvlg ggsggitmaa
       61 rmkrkvgaen vaivepserh fyqpiwtlvg agakqlsssg rptasvipsg vewikarvte
      121 lnpdknciht dddekisyry liialgiqld yekikglpeg fahpkigsny svktvektwk
      181 alqdfkegna iftfpntpvk cagapqkimy lseayfrktg krskaniifn tslgaifgvk
      241 kyadalqeii qernltvnyk knlievradk qeavfenldk pgetqvisye mlhvtppmsp
      301 pdvlktspva daagwvdvdk etlqhrrypn vfgigdctnl ptsktaaava aqsgildrti
      361 svimknqtpt kkydgytscp lvtgynrvil aefdykaepl etfpfdqske rlsmylmkad
      421 lmpflywnmm lrgywggpaf lrklfhlgms
//
LOCUS       NP_110451                627 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 442 isoform 1 [Homo sapiens].
ACCESSION   NP_110451
VERSION     NP_110451.1
DBSOURCE    REFSEQ: accession NM_030824.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Kimura,K., Wakamatsu,A., Suzuki,Y., Ota,T., Nishikawa,T.,
            Yamashita,R., Yamamoto,J., Sekine,M., Tsuritani,K., Wakaguri,H.,
            Ishii,S., Sugiyama,T., Saito,K., Isono,Y., Irie,R., Kushida,N.,
            Yoneyama,T., Otsuka,R., Kanda,K., Yokoi,T., Kondo,H., Wagatsuma,M.,
            Murakawa,K., Ishida,S., Ishibashi,T., Takahashi-Fujii,A.,
            Tanase,T., Nagai,K., Kikuchi,H., Nakai,K., Isogai,T. and Sugano,S.
  TITLE     Diversification of transcriptional modulation: large-scale
            identification and characterization of putative alternative
            promoters of human genes
  JOURNAL   Genome Res 16 (1), 55-65 (2006)
   PUBMED   16344560
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008758.7, DA151257.1 and AK024418.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK024418.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2467143
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242804.9/ ENSP00000242804.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..627
                     /product="zinc finger protein 442 isoform 1"
                     /calculated_mol_wt=72733
     Region          28..69
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          155..175
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          183..203
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          211..231
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          235..622
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          239..259
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          267..287
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(272,274,276,278..279,282..283,286,300,302,306..307,
                     310..311,314,328,330,332,334..335,338..339,342)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          295..315
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          323..343
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          351..371
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          379..396
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          407..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(412,414,416,418..419,422..423,426,440,442,446..447,
                     450..451,454,467,469,471,473..474,477..478,481)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          463..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          490..510
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(523,525,527,529..530,533..534,537,551,553,557..558,
                     561..562,565,579,581,583,585..586,589..590,593)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          602..622
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..627
                     /gene="ZNF442"
                     /coded_by="NM_030824.3:634..2517"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12271.1"
                     /db_xref="GeneID:79973"
                     /db_xref="HGNC:HGNC:20877"
ORIGIN      
        1 mivfggedrs dlflpdsqtn eerkqydsva fedvavnftq eewallgpsq kslyrdvmwe
       61 tirnldcigm kwedtniedq hrnprrslrc hiierfsesr qpdstvnekp pgvdpckssv
      121 cgeimgcsfl ncyitfdagh kpdecqeyge kphthkqcgt afnyhhsfqt qerphtgkkr
      181 ydckecgktf sssgnlrrhi ivqrgggpyi cklcgkaffw pslfrmhert htgekpyeck
      241 qcckafpiys sylrhertht gekpyeckhc skafpdyssy vrherthtge kpykckrcgr
      301 afsvssslri herthtgekp yeckqcgkaf hhlgsfqrhm irhtgdgphk ckicgkgfdc
      361 psslqshert htgekpyeck qcgkalshhs sfrshmimht gdgphkckvc gkafiypsvf
      421 qgherthtge kpyeckecgk afrissslrr hetthtgekp ykckcgkafi dfysfqnhet
      481 thtgekpyec kecgkafscf tylsqhrrth maekpyeckt ckkafshfgn lkvherihtg
      541 ekpyeckecr kafswltcll rherihtgkk syecqqcgka ftrsrflrgh ekthtgekmh
      601 eckecgkals slsslhrhkr thwrdtl
//
LOCUS       NP_001351216             330 aa            linear   PRI 27-APR-2025
DEFINITION  aquaporin-4 isoform M23x [Homo sapiens].
ACCESSION   NP_001351216
VERSION     NP_001351216.1
DBSOURCE    REFSEQ: accession NM_001364287.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Braun,M., Sevao,M., Keil,S.A., Gino,E., Wang,M.X., Lee,J.,
            Haveliwala,M.A., Klein,E., Agarwal,S., Pedersen,T., Rhodes,C.H.,
            Jansson,D., Cook,D., Peskind,E., Perl,D.P., Piantino,J.,
            Schindler,A.G. and Iliff,J.J.
  TITLE     Macroscopic changes in aquaporin-4 underlie blast traumatic brain
            injury-related impairment in glymphatic function
  JOURNAL   Brain 147 (6), 2214-2229 (2024)
   PUBMED   38802114
  REMARK    GeneRIF: Macroscopic changes in aquaporin-4 underlie blast
            traumatic brain injury-related impairment in glymphatic function.
REFERENCE   2  (residues 1 to 330)
  AUTHORS   De Bellis,M., Pisani,F., Mola,M.G., Rosito,S., Simone,L.,
            Buccoliero,C., Trojano,M., Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     Translational readthrough generates new astrocyte AQP4 isoforms
            that modulate supramolecular clustering, glial endfeet
            localization, and water transport
  JOURNAL   Glia 65 (5), 790-803 (2017)
   PUBMED   28206694
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   4  (residues 1 to 330)
  AUTHORS   De Bellis,M., Pisani,F., Mola,M.G., Basco,D., Catalano,F.,
            Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     A novel human aquaporin-4 splice variant exhibits a
            dominant-negative activity: a new mechanism to regulate water
            permeability
  JOURNAL   Mol Biol Cell 25 (4), 470-480 (2014)
   PUBMED   24356448
  REMARK    GeneRIF: The expression of AQP4-Delta4 may represent a new
            regulatory mechanism through which the cell-surface expression and
            therefore the activity of AQP4 can be physiologically modulated.
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Rossi,A., Pisani,F., Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     Evidences for a leaky scanning mechanism for the synthesis of the
            shorter M23 protein isoform of aquaporin-4: implication in
            orthogonal array formation and neuromyelitis optica antibody
            interaction
  JOURNAL   J Biol Chem 285 (7), 4562-4569 (2010)
   PUBMED   20007705
  REMARK    GeneRIF: In cells transiently transfected with AQP4-M1 coding
            sequence we observed besides AQP4-M1 the additional presence of the
            AQP4-M23 isoform associated with the formation of typical
            orthogonal arrays of particles.
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Umenishi,F. and Verkman,A.S.
  TITLE     Isolation and functional analysis of alternative promoters in the
            human aquaporin-4 water channel gene
  JOURNAL   Genomics 50 (3), 373-377 (1998)
   PUBMED   9676432
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Lu,M., Lee,M.D., Smith,B.L., Jung,J.S., Agre,P., Verdijk,M.A.,
            Merkx,G., Rijss,J.P. and Deen,P.M.
  TITLE     The human AQP4 gene: definition of the locus encoding two water
            channel polypeptides in brain
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10908-10912 (1996)
   PUBMED   8855281
REFERENCE   9  (residues 1 to 330)
  AUTHORS   Yang,B., Ma,T. and Verkman,A.S.
  TITLE     cDNA cloning, gene organization, and chromosomal localization of a
            human mercurial insensitive water channel. Evidence for distinct
            transcriptional units
  JOURNAL   J Biol Chem 270 (39), 22907-22913 (1995)
   PUBMED   7559426
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Min,R., Abbink,T.E.M. and van der Knaap,M.S.
  TITLE     Megalencephalic Leukoencephalopathy with Subcortical Cysts
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HQ901095.1, AK222684.1,
            DT220791.1, DA244620.1, AC018371.10 and BU687682.1.
            
            Summary: This gene encodes a member of the aquaporin family of
            intrinsic membrane proteins that function as water-selective
            channels in the plasma membranes of many cells. This protein is the
            predominant aquaporin found in brain and has an important role in
            brain water homeostasis. Alternatively spliced transcript variants
            encoding different isoforms have been described for this gene.
            Additional isoforms, resulting from the use of alternative in-frame
            translation initiation codons, have also been described. Recent
            studies provided evidence for translational readthrough in this
            gene, and expression of C-terminally extended isoforms via the use
            of an alternative in-frame translation termination codon. [provided
            by RefSeq, Jun 2018].
            
            Transcript Variant: This variant (1, also known as hMIWC2)
            represents the predominant transcript and encodes four isoforms,
            resulting from the use of two alternative in-frame translation
            initiation codons and two alternative in-frame translation
            termination codons. This RefSeq represents a C-terminally extended
            isoform (M23x, also known as M23ex), which results from the use of
            the downstream in-frame AUG start codon and readthrough of the
            upstream UGA stop codon to the downstream UAA stop codon. As the
            UGA stop codon has been reported to specify several alternative
            amino acids (tryptophan, cysteine, arginine and serine), its
            location in this isoform is denoted by an 'X'. An alternatively
            spliced transcript variant (NM_001364289.1) encodes the same
            isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.52586.1,
                                           SRR1803612.168247.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147920, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:20007705)
            stop codon readthrough           :: PMID: 28206694
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..330
                     /product="aquaporin-4 isoform M23x"
                     /note="mercurial-insensitive water channel; aquaporin
                     type4"
                     /calculated_mol_wt=35398
     Region          9..226
                     /region_name="MIP"
                     /note="Major intrinsic protein; pfam00230"
                     /db_xref="CDD:395174"
     Site            order(55,73..75,187..188,191,194)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            order(75..77,191..193)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     CDS             1..330
                     /gene="AQP4"
                     /gene_synonym="hAQP4; MIWC; MLC4; WCH4"
                     /coded_by="NM_001364287.1:181..1173"
                     /note="isoform M23x is encoded by transcript variant 1"
                     /db_xref="GeneID:361"
                     /db_xref="HGNC:HGNC:637"
                     /db_xref="MIM:600308"
ORIGIN      
        1 mvafkgvwtq afwkavtaef lamlifvlls lgstinwggt ekplpvdmvl islcfglsia
       61 tmvqcfghis gghinpavtv amvctrkisi aksvfyiaaq clgaiigagi lylvtppsvv
      121 gglgvtmvhg nltaghgllv eliitfqlvf tifascdskr tdvtgsiala igfsvaighl
      181 fainytgasm nparsfgpav imgnwenhwi ywvgpiigav lagglyeyvf cpdvefkrrf
      241 keafskaaqq tkgsymeved nrsqvetddl ilkpgvvhvi dvdrgeekkg kdqsgevlss
      301 vxledrtesr qdslelssdf lppiketdll
//
LOCUS       NP_004800                398 aa            linear   PRI 27-APR-2025
DEFINITION  stomatin-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_004800
VERSION     NP_004800.2
DBSOURCE    REFSEQ: accession NM_004809.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
  REMARK    GeneRIF: [review] Stomatin family member STOML1 is oligomeric; it
            mostly localizes to membrane domains and has been shown to modulate
            ion channel activity.
            Review article
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Zhang,W., MacDonald,E.M. and Koepp,D.M.
  TITLE     The stomatin-like protein SLP-1 and Cdk2 interact with the F-Box
            protein Fbw7-gamma
  JOURNAL   PLoS One 7 (10), e47736 (2012)
   PUBMED   23082202
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Mairhofer,M., Steiner,M., Salzer,U. and Prohaska,R.
  TITLE     Stomatin-like protein-1 interacts with stomatin and is targeted to
            late endosomes
  JOURNAL   J Biol Chem 284 (42), 29218-29229 (2009)
   PUBMED   19696025
  REMARK    GeneRIF: Stomatin-like protein-1 interacts with stomatin and is
            targeted to late endosomes
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Gilles,F., Glenn,M., Goy,A., Remache,Y. and Zelenetz,A.D.
  TITLE     A novel gene STORP (STOmatin-Related Protein) is localized 2 kb
            upstream of the promyelocytic gene on chromosome 15q22
  JOURNAL   Eur J Haematol 64 (2), 104-113 (2000)
   PUBMED   10997330
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Seidel,G. and Prohaska,R.
  TITLE     Molecular cloning of hSLP-1, a novel human brain-specific member of
            the band 7/MEC-2 family similar to Caenorhabditis elegans UNC-24
  JOURNAL   Gene 225 (1-2), 23-29 (1998)
   PUBMED   9931417
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF156557.1, AK302051.1 and AC108137.8.
            
            On Apr 15, 2002 this sequence version replaced NP_004800.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.198621.1, AF156557.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000541638.6/ ENSP00000442478.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..398
                     /product="stomatin-like protein 1 isoform 1"
                     /note="stomatin (EBP72)-like 1; stomatin-like protein 1;
                     EPB72-like 1; EPB72-like protein 1; protein unc-24
                     homolog; stomatin-related protein; stomatin (EPB72)-like
                     1"
                     /calculated_mol_wt=42837
     Region          6..10
                     /region_name="Tyrosine-type lysosomal sorting signal.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:19696025"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBI4.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBI4.1)"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBI4.1)"
     Region          94..224
                     /region_name="SPFH_SLP-1"
                     /note="Stomatin-like protein 1 (SLP-1), a subgroup of the
                     stomatin-like proteins (slipins) family; belonging to the
                     SPFH (stomatin, prohibitin, flotillin, and HflK/C)
                     superfamily; cd13436"
                     /db_xref="CDD:259814"
     Region          311..395
                     /region_name="SCP2"
                     /note="SCP-2 sterol transfer family; pfam02036"
                     /db_xref="CDD:460423"
     CDS             1..398
                     /gene="STOML1"
                     /gene_synonym="hUNC-24; SLP-1; STORP"
                     /coded_by="NM_004809.5:73..1269"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10254.1"
                     /db_xref="GeneID:9399"
                     /db_xref="HGNC:HGNC:14560"
                     /db_xref="MIM:608326"
ORIGIN      
        1 mlgrsgyral plgdfdrfqq ssfgflgsqk gclsperggv gtgadvpqsw psclchglis
       61 flgfllllvt fpisgwfalk ivptyermiv frlgrirtpq gpgmvlllpf idsfqrvdlr
      121 trafnvppck laskdgavls vgadvqfriw dpvlsvmtvk dlntatrmta qnamtkallk
      181 rplreiqmek lkisdqllle indvtrawgl evdrvelave avlqppqdsp agpnldstlq
      241 qlalhflggs mnsmaggaps pgpadtvemv seveppapqv garsspkqpl aeglltalqp
      301 flsealvsqv gacyqfnvvl psgtqsayfl dlttgrgrvg hgvpdgipdv vvemaeadlr
      361 allcrelrpl gaymsgrlkv kgdlamamkl eavlralk
//
LOCUS       NP_082389                672 aa            linear   ROD 27-APR-2025
DEFINITION  APC membrane recruitment protein 2 isoform 1 [Mus musculus].
ACCESSION   NP_082389 XP_127745
VERSION     NP_082389.2
DBSOURCE    REFSEQ: accession NM_028113.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Pfister,A.S., Hadjihannas,M.V., Rohrig,W., Schambony,A. and
            Behrens,J.
  TITLE     Amer2 protein interacts with EB1 protein and adenomatous polyposis
            coli (APC) and controls microtubule stability and cell migration
  JOURNAL   J Biol Chem 287 (42), 35333-35340 (2012)
   PUBMED   22898821
  REMARK    GeneRIF: the Amer2-EB1-APC complex regulates cell migration by
            altering microtubule stability.
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Comai,G., Boutet,A., Neirijnck,Y. and Schedl,A.
  TITLE     Expression patterns of the Wtx/Amer gene family during mouse
            embryonic development
  JOURNAL   Dev Dyn 239 (6), 1867-1878 (2010)
   PUBMED   20503382
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC166113.3.
            
            On Feb 15, 2019 this sequence version replaced NP_082389.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK139177.1, AK032651.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 31.62 cM"
     Protein         1..672
                     /product="APC membrane recruitment protein 2 isoform 1"
                     /note="protein FAM123A; APC membrane recruitment protein
                     2; family with sequence similarity 123, member A"
                     /calculated_mol_wt=69802
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Region          74..360
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Region          94..591
                     /region_name="WTX"
                     /note="WTX protein; pfam09422"
                     /db_xref="CDD:462794"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747; propagated from
                     UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     Region          443..560
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CCJ4.2)"
     CDS             1..672
                     /gene="Amer2"
                     /gene_synonym="2600011E07Rik; Fam123a"
                     /coded_by="NM_028113.4:556..2574"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS27177.2"
                     /db_xref="GeneID:72125"
                     /db_xref="MGI:MGI:1919375"
ORIGIN      
        1 metgrsrggg aavserggga ragvcgrqeq agalaadmds hcecaaetpa aeppsgkink
       61 aafklfkkrk sggtmpsifg vknkgdgkss gptgmvrsrt hdglaevlvl egskkeeppg
      121 gsdhsgarpi pgppkpsgpg lgslasssva kshsffsllk kngrsetgkg dhaeaskagg
      181 kqkrglkgif ssmrwhrrdk rgkeeeekav raagpgnlvl pgsltaslec vkeeppraar
      241 rpdspgqdas rhaagepagg eqapasaesa pericleags ptgsgdqssr gedaeghrre
      301 ekpgaalesg agevqaaeda sktgdvpikt vplvdseggs grasavpdps svdppsdpsa
      361 driclmfsdv tslksfdslt gcgdiiadpe eeagpscdkh vpgpgkpvls kknasvvayq
      421 gggeemaspd qvddtylpef wdmlsqtedq gqgtqegaak aatasdikla petssdtrcg
      481 eaakdmssvk rrrlhripie sqqkeepkhp ekehqegvpn sdegywdstt pgpeeesisn
      541 sssskkvvip rdsdsgdalc dlyvepeasp atlpatedpp clsrlkpvsp gtitcplrtp
      601 gsllkdskip isikhlsnlp sshpvvhqqp arsevprtki pvskvlvrrv snrglagtti
      661 raaachdsak kl
//
LOCUS       NP_001351927             677 aa            linear   PRI 27-APR-2025
DEFINITION  transcription initiation factor TFIID subunit 6 isoform alpha [Homo
            sapiens].
ACCESSION   NP_001351927 XP_024302665
VERSION     NP_001351927.1
DBSOURCE    REFSEQ: accession NM_001364998.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Tuc,E., Bengur,F.B., Aykut,A., Sahin,O. and Alanay,Y.
  TITLE     The third family with TAF6-related phenotype: Alazami-Yuan syndrome
  JOURNAL   Clin Genet 97 (5), 795-796 (2020)
   PUBMED   32030742
  REMARK    GeneRIF: The third family with TAF6-related phenotype: Alazami-Yuan
            syndrome.
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Delannoy,A., Wilhelm,E., Eilebrecht,S., Alvarado-Cuevas,E.M.,
            Benecke,A.G. and Bell,B.
  TITLE     BIM and NOXA are mitochondrial effectors of TAF6delta-driven
            apoptosis
  JOURNAL   Cell Death Dis 9 (2), 70 (2018)
   PUBMED   29358700
  REMARK    GeneRIF: BIM and NOXA contribute to TAF6delta-dependent cell death.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Gupta,K., Watson,A.A., Baptista,T., Scheer,E., Chambers,A.L.,
            Koehler,C., Zou,J., Obong-Ebong,I., Kandiah,E., Temblador,A.,
            Round,A., Forest,E., Man,P., Bieniossek,C., Laue,E.D., Lemke,E.A.,
            Rappsilber,J., Robinson,C.V., Devys,D., Tora,L. and Berger,I.
  TITLE     Architecture of TAF11/TAF13/TBP complex suggests novel regulation
            properties of general transcription factor TFIID
  JOURNAL   Elife 6, e30395 (2017)
   PUBMED   29111974
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Bell,B., Scheer,E. and Tora,L.
  TITLE     Identification of hTAF(II)80 delta links apoptotic signaling
            pathways to transcription factor TFIID function
  JOURNAL   Mol Cell 8 (3), 591-600 (2001)
   PUBMED   11583621
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Hisatake,K., Ohta,T., Takada,R., Guermah,M., Horikoshi,M.,
            Nakatani,Y. and Roeder,R.G.
  TITLE     Evolutionary conservation of human
            TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and
            interactions of TAFII80 with other TAFs and with general
            transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 92 (18), 8195-8199 (1995)
   PUBMED   7667268
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Weinzierl,R.O., Ruppert,S., Dynlacht,B.D., Tanese,N. and Tjian,R.
  TITLE     Cloning and expression of Drosophila TAFII60 and human TAFII70
            reveal conserved interactions with other subunits of TFIID
  JOURNAL   EMBO J 12 (13), 5303-5309 (1993)
   PUBMED   8262073
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 677)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Mathe,G., Schwarzenberg,L., Halle-Pannenko,O. and Simmler,M.C.
  TITLE     Discussion paper: experimental and clinical immunopharmacology data
            applicable to cancer immunotherapy
  JOURNAL   Ann N Y Acad Sci 277 (00), 467-484 (1976)
   PUBMED   826207
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073842.5.
            
            On Jul 20, 2018 this sequence version replaced XP_024302665.1.
            
            Summary: Initiation of transcription by RNA polymerase II requires
            the activities of more than 70 polypeptides. The protein that
            coordinates these activities is transcription factor IID (TFIID),
            which binds to the core promoter to position the polymerase
            properly, serves as the scaffold for assembly of the remainder of
            the transcription complex, and acts as a channel for regulatory
            signals. TFIID is composed of the TATA-binding protein (TBP) and a
            group of evolutionarily conserved proteins known as TBP-associated
            factors or TAFs. TAFs may participate in basal transcription, serve
            as coactivators, function in promoter recognition or modify general
            transcription factors (GTFs) to facilitate complex assembly and
            transcription initiation. This gene encodes one of the smaller
            subunits of TFIID that binds weakly to TBP but strongly to TAF1,
            the largest subunit of TFIID. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jun 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.88669.1,
                                           SRR1803615.10455.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..677
                     /product="transcription initiation factor TFIID subunit 6
                     isoform alpha"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, E, 70/85kD; transcription initiation
                     factor TFIID subunit 6; RNA polymerase II TBP-associated
                     factor subunit E; transcription initiation factor TFIID 70
                     kDa subunit; TAF6 RNA polymerase II, TATA box binding
                     protein (TBP)-associated factor, 80kDa"
                     /calculated_mol_wt=72538
     Region          9..408
                     /region_name="TAF6"
                     /note="Transcription initiation factor TFIID, subunit TAF6
                     (also component of histone acetyltransferase SAGA)
                     [Transcription]; COG5095"
                     /db_xref="CDD:227426"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          142..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Region          214..430
                     /region_name="TAF6C"
                     /note="C-terminal domain of TATA Binding Protein (TBP)
                     Associated Factor 6 (TAF6); cd08050"
                     /db_xref="CDD:381749"
     Site            order(218..220,222..223,226,237..238,241,245,248..249,255)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:381749"
     Region          218..249
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          256..291
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          301..344
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          351..383
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          385..429
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          524..574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Site            524
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          611..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62311; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            634
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     CDS             1..677
                     /gene="TAF6"
                     /gene_synonym="ALYUS; MGC:8964; TAF(II)70; TAF(II)80;
                     TAF2E; TAFII-70; TAFII-80; TAFII70; TAFII80; TAFII85"
                     /coded_by="NM_001364998.1:671..2704"
                     /note="isoform alpha is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS5686.1"
                     /db_xref="GeneID:6878"
                     /db_xref="HGNC:HGNC:11540"
                     /db_xref="MIM:602955"
ORIGIN      
        1 maeekklkls ntvlpsesmk vvaesmgiaq iqeetcqllt devsyrikei aqdalkfmhm
       61 gkrqklttsd idyalklknv eplygfhaqe fipfrfasgg grelyfyeek evdlsdiint
      121 plprvpldvc lkahwlsieg cqpaipenpp papkeqqkae ateplksakp gqeedgplkg
      181 kgqgattadg kgkekkappl legaplrlkp rsihelsveq qlyykeitea cvgsceakra
      241 ealqsiatdp glyqmlprfs tfisegvrvn vvqnnlalli ylmrmvkalm dnptlyleky
      301 vhelipavmt civsrqlclr pdvdnhwalr dfaarlvaqi ckhfstttnn iqsritktft
      361 kswvdektpw ttrygsiagl aelghdvikt lilprlqqeg erirsvldgp vlsnidriga
      421 dhvqslllkh capvlaklrp ppdnqdayra efgslgpllc sqvvkaraqa alqaqqvnrt
      481 tltitqprpt ltlsqapqpg prtpgllkvp gsialpvqtl vsaraaappq psppptkfiv
      541 msssssapst qqvlslstsa pgsgstttsp vtttvpsvqp ivklvstatt appstapsgp
      601 gsvqkyivvs lpptgegkgg ptshpspvpp passpsplsg salcggkqea gdspppapgt
      661 pkangsqpns gspqpap
//
LOCUS       NP_001346877             746 aa            linear   ROD 27-APR-2025
DEFINITION  protein C-mannosyl-transferase DPY19L1 [Mus musculus].
ACCESSION   NP_001346877 XP_006510359
VERSION     NP_001346877.1
DBSOURCE    REFSEQ: accession NM_001359948.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Shcherbakova,A., Tiemann,B., Buettner,F.F. and Bakker,H.
  TITLE     Distinct C-mannosylation of netrin receptor thrombospondin type 1
            repeats by mammalian DPY19L1 and DPY19L3
  JOURNAL   Proc Natl Acad Sci U S A 114 (10), 2574-2579 (2017)
   PUBMED   28202721
  REMARK    GeneRIF: Mannosylation by DPY19L1 but not DPY19L3 is required for
            transport of UNC5A from the endoplasmic reticulum to the cell
            surface. In vertebrates, a new C-mannosyltransferase has apparently
            evolved to increase glycosylation of TSRs, potentially to increase
            the stability of the structurally essential tryptophan ladder or to
            provide additional adhesion functions.
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Watanabe,K., Bizen,N., Sato,N. and Takebayashi,H.
  TITLE     Endoplasmic Reticulum-Localized Transmembrane Protein Dpy19L1 Is
            Required for Neurite Outgrowth
  JOURNAL   PLoS One 11 (12), e0167985 (2016)
   PUBMED   27959946
  REMARK    GeneRIF: Dpy19L1 is localized to the ER membrane and regulates
            neurite extension during development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Watanabe,K., Takebayashi,H., Bepari,A.K., Esumi,S., Yanagawa,Y. and
            Tamamaki,N.
  TITLE     Dpy19l1, a multi-transmembrane protein, regulates the radial
            migration of glutamatergic neurons in the developing cerebral
            cortex
  JOURNAL   Development 138 (22), 4979-4990 (2011)
   PUBMED   22028030
  REMARK    GeneRIF: Dpy19l1 is required for the proper radial migration of
            glutamatergic neurons, an evolutionarily conserved role for the
            Dpy19 family in neuronal migration.
            Erratum:[Development. 2012 Mar;139(6):1225]
REFERENCE   5  (residues 1 to 746)
  AUTHORS   Bulfone,A., Carotenuto,P., Faedo,A., Aglio,V., Garzia,L.,
            Bello,A.M., Basile,A., Andre,A., Cocchia,M., Guardiola,O.,
            Ballabio,A., Rubenstein,J.L. and Zollo,M.
  TITLE     Telencephalic embryonic subtractive sequences: a unique collection
            of neurodevelopmental genes
  JOURNAL   J Neurosci 25 (33), 7586-7600 (2005)
   PUBMED   16107646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC102554.7, CT010514.9 and BU757480.1.
            
            On Jan 20, 2018 this sequence version replaced XP_006510359.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.19401.1,
                                           SRR1660813.215489.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 10.15 cM"
     Protein         1..746
                     /product="protein C-mannosyl-transferase DPY19L1"
                     /note="protein dpy-19 homolog 1; dpy-19-like protein 1;
                     dpy-19-like 1; probable C-mannosyltransferase DPY19L1"
                     /calculated_mol_wt=84056
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Region          <11..>91
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (A6X919.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (A6X919.1)"
     Region          90..741
                     /region_name="Dpy19L1"
                     /note="C-mannosyltransferase Dpy-19-like protein 1
                     (Dpy19L1); cd20178"
                     /db_xref="CDD:439131"
     Region          90..106
                     /region_name="putative TM segment 1"
                     /note="putative TM segment 1 [structural motif]"
                     /db_xref="CDD:439131"
     Site            137..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Region          226..247
                     /region_name="putative TM segment 2"
                     /note="putative TM segment 2 [structural motif]"
                     /db_xref="CDD:439131"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Region          251..267
                     /region_name="putative TM segment 3"
                     /note="putative TM segment 3 [structural motif]"
                     /db_xref="CDD:439131"
     Site            257..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Region          287..301
                     /region_name="putative TM segment 4"
                     /note="putative TM segment 4 [structural motif]"
                     /db_xref="CDD:439131"
     Site            307..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Region          310..325
                     /region_name="putative TM segment 5"
                     /note="putative TM segment 5 [structural motif]"
                     /db_xref="CDD:439131"
     Site            331..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Region          331..349
                     /region_name="putative TM segment 6"
                     /note="putative TM segment 6 [structural motif]"
                     /db_xref="CDD:439131"
     Region          357..374
                     /region_name="putative TM segment 7"
                     /note="putative TM segment 7 [structural motif]"
                     /db_xref="CDD:439131"
     Site            357..374
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Region          377..393
                     /region_name="putative TM segment 8"
                     /note="putative TM segment 8 [structural motif]"
                     /db_xref="CDD:439131"
     Site            380..396
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Site            405..425
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Region          411..429
                     /region_name="putative TM segment 9"
                     /note="putative TM segment 9 [structural motif]"
                     /db_xref="CDD:439131"
     Region          481..502
                     /region_name="putative TM segment 10"
                     /note="putative TM segment 10 [structural motif]"
                     /db_xref="CDD:439131"
     Site            481..501
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Site            520..540
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Region          526..542
                     /region_name="putative TM segment 11"
                     /note="putative TM segment 11 [structural motif]"
                     /db_xref="CDD:439131"
     Region          546..568
                     /region_name="putative TM segment 12"
                     /note="putative TM segment 12 [structural motif]"
                     /db_xref="CDD:439131"
     Site            562..582
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6X919.1)"
     Region          572..587
                     /region_name="putative TM segment 13"
                     /note="putative TM segment 13 [structural motif]"
                     /db_xref="CDD:439131"
     CDS             1..746
                     /gene="Dpy19l1"
                     /gene_synonym="1100001I19Rik; 6030402K12"
                     /coded_by="NM_001359948.1:11..2251"
                     /db_xref="CCDS:CCDS22931.2"
                     /db_xref="GeneID:244745"
                     /db_xref="MGI:MGI:1915685"
ORIGIN      
        1 mvlqarskhr daaprpprsa rssppplsga sevdagelgs ertppspgrr gaagrkgpra
       61 gtaapapdgl agrlaaglhw alglrrgrgr twstlllasf aallhwshit hlfendrhfs
      121 hlstlerema frtemglyys yfktiveaps flngvwmimn dklteyplvi ntlkrfnlyp
      181 evilaswyri ytkimdligi qtkicwtvtr geglspiesc eglgdpacfy vavifmlngl
      241 mmalffiygt ylsgsrlggv vtvlcfffnh gectrvmwtp plresfsypf lvlqmllvth
      301 ilrapelcrg slialcisnv lfmlpwqfaq fvlltqiasl favyvvgyid thklqkiiym
      361 hmislvlcfv lmfgnsmllt syyasslvii wgmlamkpqf lrmnvselsl wviqgcgwlf
      421 gtvilksvts rifgiaddah ignlltskff sykdfdtlly tcaaefdfme ketplrytkt
      481 lllpvvlvtv aaivrkifnd mrgvvakqrt htrkqqfehg elvyhalqll aytalgvlim
      541 rlklfltphm cvmaslicsr qlfgwlfgkv hpgavvfail aamsiqgsan lqtqwnivge
      601 fsnlpqeeli ewirystkpd avfagamptm asvklsalrp vvnhphyeda glrartkivy
      661 smysrkaped vkkelmklkv nyyileeswc irrskpgcsm peiwdvedpd nagktplcni
      721 lvkdskphft tvfqnsvykv levlrq
//
LOCUS       NP_008998                611 aa            linear   PRI 27-APR-2025
DEFINITION  histone acetyltransferase KAT7 isoform 1 [Homo sapiens].
ACCESSION   NP_008998
VERSION     NP_008998.1
DBSOURCE    REFSEQ: accession NM_007067.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Rondeau,V., Berman,J.M., Ling,T., O'Brien,C., Culp-Hill,R.,
            Reisz,J.A., Wunderlich,M., Chueh,Y., Jimenez-Camacho,K.E.,
            Sexton,C., Carter,K.M., Stillwell,C., St-Germain,J., Yendi,D.,
            Gupta,A., Shi,M., Bourdine,A., Paralkar,V.R., Jahangiri,S.,
            Hope,K.J., Tikhonova,A.N., Arruda,A., Minden,M.D., Raught,B.,
            D'Alessandro,A. and Jones,C.L.
  TITLE     Spermidine metabolism regulates leukemia stem and progenitor cell
            function through KAT7 expression in patient-derived mouse models
  JOURNAL   Sci Transl Med 16 (766), eadn1285 (2024)
   PUBMED   39321266
  REMARK    GeneRIF: Spermidine metabolism regulates leukemia stem and
            progenitor cell function through KAT7 expression in patient-derived
            mouse models.
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Yuan,Q., Wu,Y., Xue,C., Zhao,D., Wang,H. and Shen,Y.
  TITLE     KAT7 serves as an oncogenic gene and regulates CCL3 expression via
            STAT1 signaling in osteosarcoma
  JOURNAL   Biochem Biophys Res Commun 722, 150156 (2024)
   PUBMED   38797155
  REMARK    GeneRIF: KAT7 serves as an oncogenic gene and regulates CCL3
            expression via STAT1 signaling in osteosarcoma.
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Zhang,C., Shan,Y., Lin,H., Zhang,Y., Xing,Q., Zhu,J., Zhou,T.,
            Lin,A., Chen,Q., Wang,J. and Pan,G.
  TITLE     HBO1 determines SMAD action in pluripotency and mesendoderm
            specification
  JOURNAL   Nucleic Acids Res 52 (9), 4935-4949 (2024)
   PUBMED   38421638
  REMARK    GeneRIF: HBO1 determines SMAD action in pluripotency and
            mesendoderm specification.
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Zhang,X., Zhang,X., Chen,L., Zhao,J., Raj,A., Wang,Y., Li,S.,
            Zhang,C., Yang,J. and Sun,D.
  TITLE     Adipose Mesenchymal Stem Cell-derived Exosomes Enhanced Glycolysis
            through the SIX1/HBO1 Pathway against Oxygen and Glucose
            Deprivation Injury in Human Umbilical Vein Endothelial Cells
  JOURNAL   Curr Stem Cell Res Ther 19 (8), 1153-1163 (2024)
   PUBMED   37779410
  REMARK    GeneRIF: Adipose Mesenchymal Stem Cell-derived Exosomes Enhanced
            Glycolysis through the SIX1/HBO1 Pathway against Oxygen and Glucose
            Deprivation Injury in Human Umbilical Vein Endothelial Cells.
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Wang,H., Qiu,Y., Zhang,H., Chang,N., Hu,Y., Chen,J., Hu,R.,
            Liao,P., Li,Z., Yang,Y., Cen,Q., Ding,X., Li,M., Xie,X. and Li,Y.
  TITLE     Histone acetylation by HBO1 (KAT7) activates Wnt/beta-catenin
            signaling to promote leukemogenesis in B-cell acute lymphoblastic
            leukemia
  JOURNAL   Cell Death Dis 14 (8), 498 (2023)
   PUBMED   37542030
  REMARK    GeneRIF: Histone acetylation by HBO1 (KAT7) activates
            Wnt/beta-catenin signaling to promote leukemogenesis in B-cell
            acute lymphoblastic leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 611)
  AUTHORS   Cervoni,N., Detich,N., Seo,S.B., Chakravarti,D. and Szyf,M.
  TITLE     The oncoprotein Set/TAF-1beta, an inhibitor of histone
            acetyltransferase, inhibits active demethylation of DNA,
            integrating DNA methylation and transcriptional silencing
  JOURNAL   J Biol Chem 277 (28), 25026-25031 (2002)
   PUBMED   11978794
  REMARK    GeneRIF: inhibition by Set/TAF-1beta inhibits active demethylation
            of DNA, integrating DNA methylation and transcriptional silencing
REFERENCE   7  (residues 1 to 611)
  AUTHORS   Sharma,D. and Fondell,J.D.
  TITLE     Ordered recruitment of histone acetyltransferases and the
            TRAP/Mediator complex to thyroid hormone-responsive promoters in
            vivo
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 7934-7939 (2002)
   PUBMED   12034878
  REMARK    GeneRIF: ordered recruitmenet to thyroid hormone-responsive
            promoters in vivo
REFERENCE   8  (residues 1 to 611)
  AUTHORS   Burke,T.W., Cook,J.G., Asano,M. and Nevins,J.R.
  TITLE     Replication factors MCM2 and ORC1 interact with the histone
            acetyltransferase HBO1
  JOURNAL   J Biol Chem 276 (18), 15397-15408 (2001)
   PUBMED   11278932
REFERENCE   9  (residues 1 to 611)
  AUTHORS   Sharma,M., Zarnegar,M., Li,X., Lim,B. and Sun,Z.
  TITLE     Androgen receptor interacts with a novel MYST protein, HBO1
  JOURNAL   J Biol Chem 275 (45), 35200-35208 (2000)
   PUBMED   10930412
REFERENCE   10 (residues 1 to 611)
  AUTHORS   Iizuka,M. and Stillman,B.
  TITLE     Histone acetyltransferase HBO1 interacts with the ORC1 subunit of
            the human initiator protein
  JOURNAL   J Biol Chem 274 (33), 23027-23034 (1999)
   PUBMED   10438470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015795.20 and AC027801.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is part of the multimeric
            HBO1 complex, which possesses histone H4-specific acetyltransferase
            activity. This activity is required for functional replication
            origins and is involved in transcriptional activation of some
            genes. In both cases, the acetylation of histone H4 helps unfold
            chromatin so that the DNA can be accessed and replicated or
            transcribed. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.89890.1,
                                           SRR1660807.265636.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259021.9/ ENSP00000259021.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..611
                     /product="histone acetyltransferase KAT7 isoform 1"
                     /EC_number="2.3.1.48"
                     /note="MYST histone acetyltransferase 2; histone
                     acetyltransferase MYST2; MOZ, YBF2/SAS3, SAS2 and TIP60
                     protein 2; histone acetyltransferase binding to ORC1;
                     histone acetyltransferase KAT7; K(lysine)
                     acetyltransferase 7"
                     /calculated_mol_wt=70512
     Region          1..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95251.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:26572825,
                     ECO:0000269|PubMed:28719581, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:26572825,
                     ECO:0000269|PubMed:28719581; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:18250300,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95251.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:18250300,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (O95251.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:18250300,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O95251.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5SVQ0; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5SVQ0; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95251.1)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Region          184..212
                     /region_name="zf-C2HC"
                     /note="Zinc finger, C2HC type; pfam01530"
                     /db_xref="CDD:460240"
     Site            199
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            277
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q5SVQ0; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Region          <324..609
                     /region_name="PLN00104"
                     /note="MYST -like histone acetyltransferase; Provisional"
                     /db_xref="CDD:215056"
     Site            432
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q9H7Z6; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     Site            506
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95251.1)"
     CDS             1..611
                     /gene="KAT7"
                     /gene_synonym="HBO1; HBOA; MYST2; ZC2HC7"
                     /coded_by="NM_007067.5:155..1990"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11554.1"
                     /db_xref="GeneID:11143"
                     /db_xref="HGNC:HGNC:17016"
                     /db_xref="MIM:609880"
ORIGIN      
        1 mprrkrnags ssdgtedsdf stdlehtdss esdgtsrrsa rvtrssarls qssqdsspvr
       61 nlqsfgteep aystrrvtrs qqqptpvtpk kyplrqtrss gseteqvvdf sdretkntad
      121 hdespprtpt gnapssesdi disspnvshd esiakdmslk dsgsdlshrp krrrfhesyn
      181 fnmkcptpgc nslghltgkh erhfsisgcp lyhnlsadec kvraqsrdkq ieermlshrq
      241 ddnnrhatrh qapterqlry kekvaelrkk rnsglskeqk ekymehrqty gntrepllen
      301 ltseydldlf rraqarased leklrlqgqi tegsnmikti afgryeldtw yhspypeeya
      361 rlgrlymcef clkymksqti lrrhmakcvw khppgdeiyr kgsisvfevd gkknkiycqn
      421 lcllaklfld hktlyydvep flfyvmtead ntgchligyf skeknsflny nvsciltmpq
      481 ymrqgygkml idfsyllskv eekvgsperp lsdlglisyr sywkevllry lhnfqgkeis
      541 ikeisqetav npvdivstlq alqmlkywkg khlvlkrqdl idewiakeak rsnsnktmdp
      601 sclkwtppkg t
//
LOCUS       NP_005737                491 aa            linear   PRI 27-APR-2025
DEFINITION  nicotinamide phosphoribosyltransferase precursor [Homo sapiens].
ACCESSION   NP_005737
VERSION     NP_005737.1
DBSOURCE    REFSEQ: accession NM_005746.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Li,Y., Xin,C., Xie,J. and Sun,X.
  TITLE     Association between visfatin and periodontitis: a systematic review
            and meta-analysis
  JOURNAL   PeerJ 12, e17187 (2024)
   PUBMED   38560458
  REMARK    GeneRIF: Association between visfatin and periodontitis: a
            systematic review and meta-analysis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Wang,Y.R. and Ma,Y.P.
  TITLE     [Mechanism and Clinical Significance of NAMPT in Multiple Myeloma]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 32 (1), 138-145 (2024)
   PUBMED   38387912
  REMARK    GeneRIF: [Mechanism and Clinical Significance of NAMPT in Multiple
            Myeloma].
REFERENCE   3  (residues 1 to 491)
  AUTHORS   He,X.L., Guo,H.J., Lei,Y.R., Li,J., Li,J.Y., Li,M.H., Li,N.,
            Wang,F. and Mo,C.F.
  TITLE     NAMPT promotes the malignant progression of HBV-associated
            hepatocellular carcinoma through activation of SREBP1-mediated
            lipogenesis
  JOURNAL   FASEB J 38 (2), e23444 (2024)
   PUBMED   38252081
  REMARK    GeneRIF: NAMPT promotes the malignant progression of HBV-associated
            hepatocellular carcinoma through activation of SREBP1-mediated
            lipogenesis.
REFERENCE   4  (residues 1 to 491)
  AUTHORS   El-Masry,S.A., Farid,M.N., Hassan,N.E., Soliman,M.A., Mekkawy,L.H.,
            Elashry,G.I. and Abd El-Fattah,S.N.
  TITLE     Fibroblast growth factor-21 and Visfatin as potential predictors
            for metabolic risk factors in obese children
  JOURNAL   Sci Rep 14 (1), 1190 (2024)
   PUBMED   38216702
  REMARK    GeneRIF: Fibroblast growth factor-21 and Visfatin as potential
            predictors for metabolic risk factors in obese children.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Masood,S.H., Khan,T.A., Baloch,A.A., Hasan,S.M., Naqvi,A.M. and
            Iqbal,M.U.N.
  TITLE     Association of Visfatin gene polymorphism with obesity related
            metabolic disorders among Pakistani population: a case control
            study
  JOURNAL   Sci Rep 13 (1), 23002 (2023)
   PUBMED   38155161
  REMARK    GeneRIF: Association of Visfatin gene polymorphism with obesity
            related metabolic disorders among Pakistani population: a case
            control study.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Kitani,T., Okuno,S. and Fujisawa,H.
  TITLE     Growth phase-dependent changes in the subcellular localization of
            pre-B-cell colony-enhancing factor
  JOURNAL   FEBS Lett 544 (1-3), 74-78 (2003)
   PUBMED   12782293
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Rongvaux,A., Shea,R.J., Mulks,M.H., Gigot,D., Urbain,J., Leo,O. and
            Andris,F.
  TITLE     Pre-B-cell colony-enhancing factor, whose expression is
            up-regulated in activated lymphocytes, is a nicotinamide
            phosphoribosyltransferase, a cytosolic enzyme involved in NAD
            biosynthesis
  JOURNAL   Eur J Immunol 32 (11), 3225-3234 (2002)
   PUBMED   12555668
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Ognjanovic,S., Bao,S., Yamamoto,S.Y., Garibay-Tupas,J., Samal,B.
            and Bryant-Greenwood,G.D.
  TITLE     Genomic organization of the gene coding for human pre-B-cell colony
            enhancing factor and expression in human fetal membranes
  JOURNAL   J Mol Endocrinol 26 (2), 107-117 (2001)
   PUBMED   11241162
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Samal,B., Sun,Y., Stearns,G., Xie,C., Suggs,S. and McNiece,I.
  TITLE     Cloning and characterization of the cDNA encoding a novel human
            pre-B-cell colony-enhancing factor
  JOURNAL   Mol Cell Biol 14 (2), 1431-1437 (1994)
   PUBMED   8289818
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Siderovski,D.P., Blum,S., Forsdyke,R.E. and Forsdyke,D.R.
  TITLE     A set of human putative lymphocyte G0/G1 switch genes includes
            genes homologous to rodent cytokine and zinc finger
            protein-encoding genes
  JOURNAL   DNA Cell Biol 9 (8), 579-587 (1990)
   PUBMED   1702972
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC106046.1, U02020.1,
            AC007032.2 and AI299587.1.
            
            Summary: This gene encodes a protein that catalyzes the
            condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate
            to yield nicotinamide mononucleotide, one step in the biosynthesis
            of nicotinamide adenine dinucleotide. The protein belongs to the
            nicotinic acid phosphoribosyltransferase (NAPRTase) family and is
            thought to be involved in many important biological processes,
            including metabolism, stress response and aging. This gene has a
            pseudogene on chromosome 10. [provided by RefSeq, Feb 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.127360.1,
                                           SRR1803614.179901.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222553.8/ ENSP00000222553.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..491
                     /product="nicotinamide phosphoribosyltransferase
                     precursor"
                     /EC_number="2.4.2.12"
                     /note="NAmPRTase; pre-B cell-enhancing factor; pre-B-cell
                     colony-enhancing factor 1"
                     /calculated_mol_wt=52521
     sig_peptide     1..26
                     /calculated_mol_wt=3018
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P43490.1)"
     Region          12..428
                     /region_name="PBEF_like"
                     /note="pre-B-cell colony-enhancing factor (PBEF)-like. The
                     mammalian members of this group of nicotinate
                     phosphoribosyltransferases (NAPRTases) were originally
                     identified as genes whose expression is upregulated upon
                     activation in lymphoid cells. In general; cd01569"
                     /db_xref="CDD:238803"
     mat_peptide     27..491
                     /product="nicotinamide phosphoribosyltransferase"
                     /calculated_mol_wt=52521
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P43490.1)"
     Site            order(195..197,220..221,313,352..353,381,383..384,387)
                     /site_type="active"
                     /db_xref="CDD:238803"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P43490.1)"
     CDS             1..491
                     /gene="NAMPT"
                     /gene_synonym="1110035O14Rik; PBEF; PBEF1; VF; VISFATIN"
                     /coded_by="NM_005746.3:100..1575"
                     /db_xref="CCDS:CCDS5737.1"
                     /db_xref="GeneID:10135"
                     /db_xref="HGNC:HGNC:30092"
                     /db_xref="MIM:608764"
ORIGIN      
        1 mnpaaeaefn illatdsykv thykqyppnt skvysyfecr ekktensklr kvkyeetvfy
       61 glqyilnkyl kgkvvtkeki qeakdvykeh fqddvfnekg wnyilekydg hlpieikavp
      121 egfviprgnv lftventdpe cywltnwiet ilvqswypit vatnsreqkk ilakyllets
      181 gnldgleykl hdfgyrgvss qetagigasa hlvnfkgtdt vaglalikky ygtkdpvpgy
      241 svpaaehsti tawgkdhekd afehivtqfs svpvsvvsds ydiynaceki wgedlrhliv
      301 srstqaplii rpdsgnpldt vlkvleilgk kfpvtenskg ykllppylrv iqgdgvdint
      361 lqeivegmkq kmwsieniaf gsgggllqkl trdllncsfk csyvvtnglg invfkdpvad
      421 pnkrskkgrl slhrtpagnf vtleegkgdl eeygqdllht vfkngkvtks ysfdeirkna
      481 qlnieleaah h
//
LOCUS       NP_001070819             439 aa            linear   PRI 27-APR-2025
DEFINITION  probable RNA-binding protein 23 isoform 1 [Homo sapiens].
ACCESSION   NP_001070819
VERSION     NP_001070819.1
DBSOURCE    REFSEQ: accession NM_001077351.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Han,H., Lin,T., Fang,Z. and Zhou,G.
  TITLE     RBM23 Drives Hepatocellular Carcinoma by Activating NF-kappaB
            Signaling Pathway
  JOURNAL   Biomed Res Int 2021, 6697476 (2021)
   PUBMED   33791378
  REMARK    GeneRIF: RBM23 Drives Hepatocellular Carcinoma by Activating
            NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Faust,T.B., Yoon,H., Nowak,R.P., Donovan,K.A., Li,Z., Cai,Q.,
            Eleuteri,N.A., Zhang,T., Gray,N.S. and Fischer,E.S.
  TITLE     Structural complementarity facilitates E7820-mediated degradation
            of RBM39 by DCAF15
  JOURNAL   Nat Chem Biol 16 (1), 7-14 (2020)
   PUBMED   31686031
  REMARK    GeneRIF: aryl-sulfonamides neo-functionalize a shallow,
            non-conserved pocket on DCAF15 to selectively bind and degrade
            RBM39 and the closely related splicing factor RBM23 without the
            requirement for a high-affinity ligand
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 439)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   8  (residues 1 to 439)
  AUTHORS   Dowhan,D.H., Hong,E.P., Auboeuf,D., Dennis,A.P., Wilson,M.M.,
            Berget,S.M. and O'Malley,B.W.
  TITLE     Steroid hormone receptor coactivation and alternative RNA splicing
            by U2AF65-related proteins CAPERalpha and CAPERbeta
  JOURNAL   Mol Cell 17 (3), 429-439 (2005)
   PUBMED   15694343
REFERENCE   9  (residues 1 to 439)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
REFERENCE   10 (residues 1 to 439)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CK003276.1, BX161440.1,
            BC106012.1 and AL135998.6.
            
            Summary: This gene encodes a member of the U2AF-like family of RNA
            binding proteins. This protein interacts with some steroid nuclear
            receptors, localizes to the promoter of a steroid- responsive gene,
            and increases transcription of steroid-responsive transcriptional
            reporters in a hormone-dependent manner. It is also implicated in
            the steroid receptor-dependent regulation of alternative splicing.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225792.1, SRR1660805.183650.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359890.8/ ENSP00000352956.3
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..439
                     /product="probable RNA-binding protein 23 isoform 1"
                     /note="RNA-binding region (RNP1, RRM) containing 4;
                     splicing factor SF2; probable RNA-binding protein 23;
                     RNA-binding region-containing protein 4; coactivator of
                     activating protein-1 and estrogen recep- tors beta; CAPER
                     beta"
                     /calculated_mol_wt=48600
     Region          13..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86U06.1)"
     Region          99..438
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86U06.1)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86U06.1)"
     CDS             1..439
                     /gene="RBM23"
                     /gene_synonym="CAPERbeta; PP239; RNPC4"
                     /coded_by="NM_001077351.2:162..1481"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41921.1"
                     /db_xref="GeneID:55147"
                     /db_xref="HGNC:HGNC:20155"
                     /db_xref="MIM:621023"
ORIGIN      
        1 masddfdivi eamleapykk eedeqqrkev kkdypsntts stsnsgnets gsstigetsk
       61 kkrsrshnks rdrkrsrsrd rdryrrrnsr srspgrqcrh rsrswdrrhg sesrsrdhrr
      121 edrvhyrspp latgyryghs ksphfreksp vrepvdnlsp eerdartvfc mqlaarirpr
      181 dledffsavg kvrdvriisd rnsrrskgia yvefceiqsv plaigltgqr llgvpiivqa
      241 sqaeknrlaa mannlqkgng gpmrlyvgsl hfnitedmlr gifepfgkid nivlmkdsdt
      301 grskgygfit fsdsecarra leqlngfela grpmrvghvt erldggtdit fpdgdqeldl
      361 gsaggrfqlm aklaegagiq lpstaaaaaa aaaqaaalql ngavplgaln paaltalspa
      421 lnlasqcfql sslftpqtm
//
LOCUS       NP_115634                549 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 3F [Homo sapiens].
ACCESSION   NP_115634 NP_001035372 XP_951464
VERSION     NP_115634.3
DBSOURCE    REFSEQ: accession NM_032258.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Hodzic,D., Kong,C., Wainszelbaum,M.J., Charron,A.J., Su,X. and
            Stahl,P.D.
  TITLE     TBC1D3, a hominoid oncoprotein, is encoded by a cluster of
            paralogues located on chromosome 17q12
  JOURNAL   Genomics 88 (6), 731-736 (2006)
   PUBMED   16863688
  REMARK    GeneRIF: We describe eight highly related TBC1D3 paralogues located
            on Chromosome 17q12 that display specific transcription patterns in
            human tissues, and that pattern is altered in several primary
            prostate tumors in comparison to healthy prostate tissues.
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Pei,L., Peng,Y., Yang,Y., Ling,X.B., Van Eyndhoven,W.G.,
            Nguyen,K.C., Rubin,M., Hoey,T., Powers,S. and Li,J.
  TITLE     PRC17, a novel oncogene encoding a Rab GTPase-activating protein,
            is amplified in prostate cancer
  JOURNAL   Cancer Res 62 (19), 5420-5424 (2002)
   PUBMED   12359748
  REMARK    GeneRIF: PRC17 is amplified in 15% of prostate cancers, it is
            highly overexpressed in approximately one-half of metastatic
            prostate tumors.
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Onno,M., Nakamura,T., Hillova,J. and Hill,M.
  TITLE     Identification of novel sequences in the repertoire of
            hypervariable TRE17 genes from immortalized nonmalignant and
            malignant human keratinocytes
  JOURNAL   Gene 131 (2), 209-215 (1993)
   PUBMED   8406013
REFERENCE   7  (residues 1 to 549)
  AUTHORS   Onno,M., Nakamura,T., Mariage-Samson,R., Hillova,J. and Hill,M.
  TITLE     Human TRE17 oncogene is generated from a family of homologous
            polymorphic sequences by single-base changes
  JOURNAL   DNA Cell Biol 12 (2), 107-118 (1993)
   PUBMED   8471161
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233698.3.
            
            On or before May 14, 2015 this sequence version replaced
            NP_001035372.2, NP_115634.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on single protein-coding
                                         transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..549
                     /product="TBC1 domain family member 3F"
                     /note="TBC1 domain family member 3; prostate cancer gene
                     17 protein; protein TRE17-alpha; TBC1 domain family member
                     3G"
                     /calculated_mol_wt=62054
     Region          99..312
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Region          350..425
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NER0.3)"
     Region          <356..>468
                     /region_name="PHA03381"
                     /note="tegument protein VP22; Provisional"
                     /db_xref="CDD:177618"
     CDS             1..549
                     /gene="TBC1D3F"
                     /gene_synonym="TBC1D3; TBC1D3G"
                     /coded_by="NM_032258.5:113..1762"
                     /db_xref="GeneID:84218"
                     /db_xref="HGNC:HGNC:18257"
                     /db_xref="MIM:610809"
ORIGIN      
        1 mdvvevagsw waqerediim kyekghragl pedkgpkpfr synnnvdhlg ivhetelppl
       61 tareakqirr eisrkskwvd mlgdwekyks srklidrayk gmpmnirgpm wsvllnieem
      121 klknpgryqi mkekgkrsse hiqridrdvs gtlrkhiffr drygtkqrel lhillayeey
      181 npevgycrdl shiaalflly lpeedafwal vqllaserhs lqgfhspngg tvqglqdqqe
      241 hvvatsqpkt mghqdkkdlc gqcsplgcli rilidgislg ltlrlwdvyl vegeqalmpi
      301 triafkvqqk rltktsrcgp warfcnrfvd twardedtvl khlrasmkkl trkkgdvppp
      361 akpeqgssas rpvpasrggk tlckgdrqap pgpparfprp iwsaspprap rsstpcpgga
      421 vredtypvgt qgvpspalaq ggpqgswrfl qwnsmprlpt dldvegpwfr hydfrqscwv
      481 raisqedqla pcwqaehpae rvrsafaaps tdsdqgtpfr ardeqqcapt sgpclcglhl
      541 essqfppgf
//
LOCUS       NP_001354457             560 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 21 [Homo sapiens].
ACCESSION   NP_001354457 XP_016872216
VERSION     NP_001354457.1
DBSOURCE    REFSEQ: accession NM_001367528.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 560)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 560)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 560)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 560)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 560)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 560)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 560)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_016872216.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.93981.1,
                                           SRR7346977.2215129.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..560
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 21"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=62128
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          401..>456
                     /region_name="NTF2_like"
                     /note="Nuclear transport factor 2 (NTF2-like) superfamily.
                     This family includes members of the NTF2 family,
                     Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases,
                     and the beta subunit of Ring hydroxylating dioxygenases.
                     This family is a classic example of...; cl09109"
                     /db_xref="CDD:471850"
     CDS             1..560
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367528.1:95..1777"
                     /note="isoform 21 is encoded by transcript variant 21"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk epqttvvhna tdgikgstes cntttededl
      361 kaaplrtgng ssvpegrssr drtapsagmq pqpslcssam rkqeiikite qlieainngd
      421 feaytkicdp gltsfepeal gnlvegmdfh kfyfenrewv raadillpap lplclclllt
      481 fssqlptfpl fdlraalllc mlvplcpdgc rqaplkalll sskchsfcsc fvavpvttik
      541 ltyflpgava yacnpntlgg
//
LOCUS       NP_775766                888 aa            linear   PRI 27-APR-2025
DEFINITION  patched domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_775766
VERSION     NP_775766.2
DBSOURCE    REFSEQ: accession NM_173495.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Xie,C.T.Y., Pastore,S.F., Vincent,J.B., Frankland,P.W. and
            Hamel,P.A.
  TITLE     Nonsynonymous Mutations in Intellectual Disability and Autism
            Spectrum Disorder Gene PTCHD1 Disrupt N-Glycosylation and Reduce
            Protein Stability
  JOURNAL   Cells 13 (2), 199 (2024)
   PUBMED   38275824
  REMARK    GeneRIF: Nonsynonymous Mutations in Intellectual Disability and
            Autism Spectrum Disorder Gene PTCHD1 Disrupt N-Glycosylation and
            Reduce Protein Stability.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Farley,K.O., Forbes,C.A., Shaw,N.C., Kuzminski,E., Ward,M.,
            Baynam,G., Lassmann,T. and Fear,V.S.
  TITLE     CRISPR-Cas9-generated PTCHD1 2489T>G stem cells recapitulate
            patient phenotype when undergoing neural induction
  JOURNAL   HGG Adv 5 (1), 100257 (2024)
   PUBMED   38007613
  REMARK    GeneRIF: CRISPR-Cas9-generated PTCHD1 2489T>G stem cells
            recapitulate patient phenotype when undergoing neural induction.
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Halewa,J., Marouillat,S., Dixneuf,M., Thepault,R.A., Ung,D.C.,
            Chatron,N., Gerard,B., Ghoumid,J., Lesca,G., Till,M., Smol,T.,
            Couque,N., Ruaud,L., Chune,V., Grotto,S., Verloes,A.,
            Vuillaume,M.L., Toutain,A., Raynaud,M. and Laumonnier,F.
  TITLE     Novel missense mutations in PTCHD1 alter its plasma membrane
            subcellular localization and cause intellectual disability and
            autism spectrum disorder
  JOURNAL   Hum Mutat 42 (7), 848-861 (2021)
   PUBMED   33856728
  REMARK    GeneRIF: Novel missense mutations in PTCHD1 alter its plasma
            membrane subcellular localization and cause intellectual disability
            and autism spectrum disorder.
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Ross,P.J., Zhang,W.B., Mok,R.S.F., Zaslavsky,K., Deneault,E.,
            D'Abate,L., Rodrigues,D.C., Yuen,R.K.C., Faheem,M., Mufteev,M.,
            Piekna,A., Wei,W., Pasceri,P., Landa,R.J., Nagy,A., Varga,B.,
            Salter,M.W., Scherer,S.W. and Ellis,J.
  TITLE     Synaptic Dysfunction in Human Neurons With Autism-Associated
            Deletions in PTCHD1-AS
  JOURNAL   Biol Psychiatry 87 (2), 139-149 (2020)
   PUBMED   31540669
  REMARK    GeneRIF: Synaptic Dysfunction in Human Neurons With
            Autism-Associated Deletions in PTCHD1-AS.
REFERENCE   5  (residues 1 to 888)
  AUTHORS   Torrico,B., Fernandez-Castillo,N., Hervas,A., Mila,M., Salgado,M.,
            Rueda,I., Buitelaar,J.K., Rommelse,N., Oerlemans,A.M., Bralten,J.,
            Freitag,C.M., Reif,A., Battaglia,A., Mazzone,L., Maestrini,E.,
            Cormand,B. and Toma,C.
  TITLE     Contribution of common and rare variants of the PTCHD1 gene to
            autism spectrum disorders and intellectual disability
  JOURNAL   Eur J Hum Genet 23 (12), 1694-1701 (2015)
   PUBMED   25782667
  REMARK    GeneRIF: both common and rare PTCHD1 variants contribute to autism
            spectrum disorder.
REFERENCE   6  (residues 1 to 888)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 888)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Pankratz,V.S., Haralambieva,I.H.,
            Vierkant,R.A. and Poland,G.A.
  TITLE     Genome-wide analysis of polymorphisms associated with cytokine
            responses in smallpox vaccine recipients
  JOURNAL   Hum Genet 131 (9), 1403-1421 (2012)
   PUBMED   22610502
REFERENCE   8  (residues 1 to 888)
  AUTHORS   Filges,I., Rothlisberger,B., Blattner,A., Boesch,N., Demougin,P.,
            Wenzel,F., Huber,A.R., Heinimann,K., Weber,P. and Miny,P.
  TITLE     Deletion in Xp22.11: PTCHD1 is a candidate gene for X-linked
            intellectual disability with or without autism
  JOURNAL   Clin Genet 79 (1), 79-85 (2011)
   PUBMED   21091464
  REMARK    GeneRIF: Deletion in Xp22.11: PTCHD1 is a candidate gene for
            X-linked intellectual disability with or without autism.
REFERENCE   9  (residues 1 to 888)
  AUTHORS   Noor,A., Whibley,A., Marshall,C.R., Gianakopoulos,P.J., Piton,A.,
            Carson,A.R., Orlic-Milacic,M., Lionel,A.C., Sato,D., Pinto,D.,
            Drmic,I., Noakes,C., Senman,L., Zhang,X., Mo,R., Gauthier,J.,
            Crosbie,J., Pagnamenta,A.T., Munson,J., Estes,A.M., Fiebig,A.,
            Franke,A., Schreiber,S., Stewart,A.F., Roberts,R., McPherson,R.,
            Guter,S.J., Cook,E.H. Jr., Dawson,G., Schellenberg,G.D.,
            Battaglia,A., Maestrini,E., Jeng,L., Hutchison,T.,
            Rajcan-Separovic,E., Chudley,A.E., Lewis,S.M., Liu,X., Holden,J.J.,
            Fernandez,B., Zwaigenbaum,L., Bryson,S.E., Roberts,W., Szatmari,P.,
            Gallagher,L., Stratton,M.R., Gecz,J., Brady,A.F., Schwartz,C.E.,
            Schachar,R.J., Monaco,A.P., Rouleau,G.A., Hui,C.C., Lucy
            Raymond,F., Scherer,S.W. and Vincent,J.B.
  CONSRTM   Autism Genome Project Consortium
  TITLE     Disruption at the PTCHD1 Locus on Xp22.11 in Autism spectrum
            disorder and intellectual disability
  JOURNAL   Sci Transl Med 2 (49), 49ra68 (2010)
   PUBMED   20844286
  REMARK    GeneRIF: Systematic screen of PTCHD1 and its 5' flanking regions
            suggests that this locus is involved in ~1% of individuals with
            autism spectrum disorder and intellectual disability.
REFERENCE   10 (residues 1 to 888)
  AUTHORS   Pinto,D., Pagnamenta,A.T., Klei,L., Anney,R., Merico,D., Regan,R.,
            Conroy,J., Magalhaes,T.R., Correia,C., Abrahams,B.S., Almeida,J.,
            Bacchelli,E., Bader,G.D., Bailey,A.J., Baird,G., Battaglia,A.,
            Berney,T., Bolshakova,N., Bolte,S., Bolton,P.F., Bourgeron,T.,
            Brennan,S., Brian,J., Bryson,S.E., Carson,A.R., Casallo,G.,
            Casey,J., Chung,B.H., Cochrane,L., Corsello,C., Crawford,E.L.,
            Crossett,A., Cytrynbaum,C., Dawson,G., de Jonge,M., Delorme,R.,
            Drmic,I., Duketis,E., Duque,F., Estes,A., Farrar,P.,
            Fernandez,B.A., Folstein,S.E., Fombonne,E., Freitag,C.M.,
            Gilbert,J., Gillberg,C., Glessner,J.T., Goldberg,J., Green,A.,
            Green,J., Guter,S.J., Hakonarson,H., Heron,E.A., Hill,M., Holt,R.,
            Howe,J.L., Hughes,G., Hus,V., Igliozzi,R., Kim,C., Klauck,S.M.,
            Kolevzon,A., Korvatska,O., Kustanovich,V., Lajonchere,C.M.,
            Lamb,J.A., Laskawiec,M., Leboyer,M., Le Couteur,A., Leventhal,B.L.,
            Lionel,A.C., Liu,X.Q., Lord,C., Lotspeich,L., Lund,S.C.,
            Maestrini,E., Mahoney,W., Mantoulan,C., Marshall,C.R.,
            McConachie,H., McDougle,C.J., McGrath,J., McMahon,W.M.,
            Merikangas,A., Migita,O., Minshew,N.J., Mirza,G.K., Munson,J.,
            Nelson,S.F., Noakes,C., Noor,A., Nygren,G., Oliveira,G.,
            Papanikolaou,K., Parr,J.R., Parrini,B., Paton,T., Pickles,A.,
            Pilorge,M., Piven,J., Ponting,C.P., Posey,D.J., Poustka,A.,
            Poustka,F., Prasad,A., Ragoussis,J., Renshaw,K., Rickaby,J.,
            Roberts,W., Roeder,K., Roge,B., Rutter,M.L., Bierut,L.J.,
            Rice,J.P., Salt,J., Sansom,K., Sato,D., Segurado,R., Sequeira,A.F.,
            Senman,L., Shah,N., Sheffield,V.C., Soorya,L., Sousa,I., Stein,O.,
            Sykes,N., Stoppioni,V., Strawbridge,C., Tancredi,R., Tansey,K.,
            Thiruvahindrapduram,B., Thompson,A.P., Thomson,S., Tryfon,A.,
            Tsiantis,J., Van Engeland,H., Vincent,J.B., Volkmar,F., Wallace,S.,
            Wang,K., Wang,Z., Wassink,T.H., Webber,C., Weksberg,R., Wing,K.,
            Wittemeyer,K., Wood,S., Wu,J., Yaspan,B.L., Zurawiecki,D.,
            Zwaigenbaum,L., Buxbaum,J.D., Cantor,R.M., Cook,E.H., Coon,H.,
            Cuccaro,M.L., Devlin,B., Ennis,S., Gallagher,L., Geschwind,D.H.,
            Gill,M., Haines,J.L., Hallmayer,J., Miller,J., Monaco,A.P.,
            Nurnberger,J.I. Jr., Paterson,A.D., Pericak-Vance,M.A.,
            Schellenberg,G.D., Szatmari,P., Vicente,A.M., Vieland,V.J.,
            Wijsman,E.M., Scherer,S.W., Sutcliffe,J.S. and Betancur,C.
  TITLE     Functional impact of global rare copy number variation in autism
            spectrum disorders
  JOURNAL   Nature 466 (7304), 368-372 (2010)
   PUBMED   20531469
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073910.20, DC365753.1, DC351268.1, BC121061.2 and BX107899.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 23, 2007 this sequence version replaced NP_775766.1.
            
            Summary: This gene encodes a membrane protein with a patched
            domain. The encoded protein is similar to Drosophila proteins which
            act as receptors for the morphogen sonic hedgehog. Deletions in
            this gene, which is located on the X chromosome, are associated
            with intellectual disability and autism (PMID: 21091464, PMID:
            20844286). [provided by RefSeq, Aug 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.837819.1,
                                           SRR1660809.24632.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379361.5/ ENSP00000368666.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.11"
     Protein         1..888
                     /product="patched domain-containing protein 1"
                     /calculated_mol_wt=101211
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96NR3.2)"
     Region          105..851
                     /region_name="Patched"
                     /note="Patched family; pfam02460"
                     /db_xref="CDD:308203"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            273..293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            319
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            326
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            328..348
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            373..393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            407..427
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            502..522
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            568
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            599
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            608
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            707..727
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            738..758
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            762
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            795..815
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            818
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96NR3.2)"
     Site            826..846
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NR3.2)"
     CDS             1..888
                     /gene="PTCHD1"
                     /gene_synonym="AUTSX4; CXDELp22.11; DELXP22.11; SLC65C1"
                     /coded_by="NM_173495.3:28..2694"
                     /db_xref="CCDS:CCDS35215.2"
                     /db_xref="GeneID:139411"
                     /db_xref="HGNC:HGNC:26392"
                     /db_xref="MIM:300828"
ORIGIN      
        1 mlrqvlhrgl rtcfsrlghf iashpvffas apvlisillg asfsryqvee svehllapqh
       61 slakiernlv nslfpvnrsk hrlysdlqtp grygrvivts fqkanmldqh htdlilklha
      121 avtkiqvprp gfnytfahic ilnndktciv ddivhvleel knaratnrtn faitypithl
      181 kdgravyngh qlggvtvhsk drvksaeaiq ltyylqsins lndmvaerwe ssfcdtvrlf
      241 qksnskvkmy pytssslred fqktsrvser ylvtslilvv tmailccsmq dcvrskpwlg
      301 llglvtisla tltaagiinl tggkynstfl gvpfvmlghg lygtfemlss wrktredqhv
      361 kertaavyad smlsfsltta mylvtfgiga spftnieaar ifccnsciai ffnylyvlsf
      421 ygsslvftgy iennyqhsif crkvpkpeal qekpawyrfl ltarfsedta egeeantyes
      481 hllvcflkry ycdwitntyv kpfvvlfyli yisfalmgyl qvsegsdlsn ivatatqtie
      541 yttaqqkyfs nyspvigfyi yesieywnts vqedvleytk gfvriswfes ylnylrklnv
      601 stglpkknft dmlrnsflka pqfshfqedi ifskkyndev dvvasrmflv aktmetnree
      661 lydlletlrr lsvtskvkfi vfnpsfvymd ryasslgapl hnscisalfl lffsaflvad
      721 slinvwitlt vvsvefgvig fmtlwkveld cisvlcliyg inytidncap mlstfvlgkd
      781 ftrtkwvkna levhgvailq sylcyivgli plaavpsnlt ctlfrclfli afvtffhcfa
      841 ilpviltflp pskkkrkekk npenreeiec vemvdidstr vvdqittv
//
LOCUS       NP_001002800            1288 aa            linear   PRI 27-APR-2025
DEFINITION  structural maintenance of chromosomes protein 4 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001002800
VERSION     NP_001002800.1
DBSOURCE    REFSEQ: accession NM_001002800.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1288)
  AUTHORS   Tan,L., Wang,S., Huang,S., Tie,Y., Sai,N., Mao,Y., Zhao,S., Hou,Y.
            and Dou,H.
  TITLE     FoxO1 promotes ovarian cancer by increasing transcription and
            METTL14-mediated m6A modification of SMC4
  JOURNAL   Cancer Sci 115 (4), 1224-1240 (2024)
   PUBMED   38403332
  REMARK    GeneRIF: FoxO1 promotes ovarian cancer by increasing transcription
            and METTL14-mediated m[6]A modification of SMC4.
REFERENCE   2  (residues 1 to 1288)
  AUTHORS   Zhu,M., Zhang,X., Gao,K., Zhang,L., Feng,X., Wang,H., Li,J. and
            Jia,J.
  TITLE     Structural Maintenance of Chromosome Protein 4 Promotes the
            Progression of Cardia Adenocarcinoma via Regulation of the
            Wnt/beta-catenin Signaling Pathway
  JOURNAL   Comb Chem High Throughput Screen 27 (4), 611-620 (2024)
   PUBMED   37170988
  REMARK    GeneRIF: Structural Maintenance of Chromosome Protein 4 Promotes
            the Progression of Cardia Adenocarcinoma via Regulation of the
            Wnt/beta-catenin Signaling Pathway.
REFERENCE   3  (residues 1 to 1288)
  AUTHORS   Yang,Z., Pan,X., Wu,X., Lin,Q., Chen,Y., Cai,S., Zhang,Y., Mai,Z.,
            Ahmad,N., Ma,D. and Deng,L.
  TITLE     TREM-1 induces pyroptosis in cardiomyocytes by activating NLRP3
            inflammasome through the SMC4/NEMO pathway
  JOURNAL   FEBS J 290 (6), 1549-1562 (2023)
   PUBMED   36181338
  REMARK    GeneRIF: TREM-1 induces pyroptosis in cardiomyocytes by activating
            NLRP3 inflammasome through the SMC4/NEMO pathway.
            Erratum:[FEBS J. 2025 Apr;292(8):2145. doi: 10.1111/febs.70066.
            PMID: 40098332]
REFERENCE   4  (residues 1 to 1288)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1288)
  AUTHORS   Wang,J., Shao,J., Lu,Y., Su,W., Dong,H., Wang,P., Lin,Z., Feng,J.,
            Wang,D., Zhao,H. and Tan,J.
  TITLE     Screening Differential CircRNAs Expression Profiles Reveals the
            Regulatory Role of the has_circTPT1_003-has-miR-218-5p-CCNE2/SMC4
            Signaling Axis in Bladder Carcinoma Progression
  JOURNAL   DNA Cell Biol 41 (2), 128-141 (2022)
   PUBMED   35005988
  REMARK    GeneRIF: Screening Differential CircRNAs Expression Profiles
            Reveals the Regulatory Role of the
            has_circTPT1_003-has-miR-218-5p-CCNE2/SMC4 Signaling Axis in
            Bladder Carcinoma Progression.
REFERENCE   6  (residues 1 to 1288)
  AUTHORS   Kimura,K., Cuvier,O. and Hirano,T.
  TITLE     Chromosome condensation by a human condensin complex in Xenopus egg
            extracts
  JOURNAL   J Biol Chem 276 (8), 5417-5420 (2001)
   PUBMED   11136719
REFERENCE   7  (residues 1 to 1288)
  AUTHORS   Ball,A.R. Jr. and Yokomori,K.
  TITLE     The structural maintenance of chromosomes (SMC) family of proteins
            in mammals
  JOURNAL   Chromosome Res 9 (2), 85-96 (2001)
   PUBMED   11321372
  REMARK    Review article
REFERENCE   8  (residues 1 to 1288)
  AUTHORS   Schmiesing,J.A., Gregson,H.C., Zhou,S. and Yokomori,K.
  TITLE     A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a
            homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone
            H3 during the early stage of mitotic chromosome condensation
  JOURNAL   Mol Cell Biol 20 (18), 6996-7006 (2000)
   PUBMED   10958694
REFERENCE   9  (residues 1 to 1288)
  AUTHORS   Nishiwaki,T., Daigo,Y., Kawasoe,T., Nagasawa,Y., Ishiguro,H.,
            Fujita,M., Furukawa,Y. and Nakamura,Y.
  TITLE     Isolation and characterization of a human cDNA homologous to the
            Xenopus laevis XCAP-C gene belonging to the structural maintenance
            of chromosomes (SMC) family
  JOURNAL   J Hum Genet 44 (3), 197-202 (1999)
   PUBMED   10319587
REFERENCE   10 (residues 1 to 1288)
  AUTHORS   Schmiesing,J.A., Ball,A.R. Jr., Gregson,H.C., Alderton,J.M.,
            Zhou,S. and Yokomori,K.
  TITLE     Identification of two distinct human SMC protein complexes involved
            in mitotic chromosome dynamics
  JOURNAL   Proc Natl Acad Sci U S A 95 (22), 12906-12911 (1998)
   PUBMED   9789013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC106033.1, AB019987.1 and
            AL136877.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to the 'structural maintenance of
            chromosomes' (SMC) gene family. Members of this gene family play a
            role in two changes in chromosome structure during mitotic
            segregation of chromosomes- chromosome condensation and sister
            chromatid cohesion. The protein encoded by this gene is likely a
            subunit of the 13S condensin complex, which is involved in
            chromosome condensation. A pseudogene related to this gene is
            located on chromosome 2. [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (2) is the longest transcript and
            encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315070.1, SRR1803615.24208.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357388.8/ ENSP00000349961.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.33"
     Protein         1..1288
                     /product="structural maintenance of chromosomes protein 4
                     isoform 1"
                     /note="chromosome-associated polypeptide C; SMC protein 4;
                     SMC4 structural maintenance of chromosomes 4-like 1"
                     /calculated_mol_wt=147052
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     Region          83..1274
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; pfam02463"
                     /db_xref="CDD:426784"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     Site            381
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8CG47; propagated from
                     UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     Site            679
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     Site            982
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     Site            1056
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NTJ3.2)"
     CDS             1..1288
                     /gene="SMC4"
                     /gene_synonym="CAP-C; CAPC; SMC-4; SMC4L1"
                     /coded_by="NM_001002800.3:106..3972"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3189.1"
                     /db_xref="GeneID:10051"
                     /db_xref="HGNC:HGNC:14013"
                     /db_xref="MIM:605575"
ORIGIN      
        1 mprkgtqpst arrreegppp pspdgassda epeppsgrte spataaetas eeldnrslee
       61 ilnsippppp pamtneagap rlmithivnq nfksyageki lgpfhkrfsc iigpngsgks
      121 nvidsmlfvf gyraqkirsk klsvlihnsd ehkdiqsctv evhfqkiidk egddyevipn
      181 snfyvsrtac rdntsvyhis gkkktfkdvg nllrshgidl dhnrflilqg eveqiammkp
      241 kgqtehdegm leylediigc grlnepikvl crrveilneh rgeklnrvkm vekekdaleg
      301 ekniaieflt leneifrkkn hvcqyyiyel qkriaemetq kekihedtke ineksnilsn
      361 emkaknkdvk dtekklnkit kfieenkekf tqldledvqv reklkhatsk akklekqlqk
      421 dkekveefks ipaksnniin etttrnnale kekekeekkl kevmdslkqe tqglqkekes
      481 rekelmgfsk svnearskmd vaqseldiyl srhntavsql tkakealiaa setlkerkaa
      541 irdiegklpq teqelkekek elqkltqeet nfkslvhdlf qkveeakssl amnrsrgkvl
      601 daiiqekksg ripgiygrlg dlgaidekyd vaisscchal dyivvdsidi aqecvnflkr
      661 qnigvatfig ldkmavwakk mteiqtpent prlfdlvkvk dekirqafyf alrdtlvadn
      721 ldqatrvayq kdrrwrvvtl qgqiieqsgt mtgggskvmk grmgsslvie iseeevnkme
      781 sqlqndskka mqiqeqkvql eervvklrhs eremrntlek ftasiqrlie qeeylnvqvk
      841 eleanvlata pdkkkqklle envsafktey davaekagkv eaevkrlhnt iveinnhklk
      901 aqqdkldkin kqldecasai tkaqvaikta drnlqkaqds vlrtekeikd tekevddlta
      961 elksledkaa evvkntnaae eslpeiqkeh rnllqelkvi qenehalqkd alsiklkleq
     1021 idghiaehns kikywhkeis kislhpiedn pieeisvlsp edleaiknpd sitnqialle
     1081 archemkpnl gaiaeykkke elylqrvael dkityerdsf rqayedlrkq rlnefmagfy
     1141 iitnklkeny qmltlggdae lelvdsldpf segimfsvrp pkkswkkifn lsggektlss
     1201 lalvfalhhy kptplyfmde idaaldfknv sivafyiyeq tknaqfiiis lrnnmfeisd
     1261 rligiyktyn itksvavnpk eiaskglc
//
LOCUS       NP_000628                522 aa            linear   PRI 27-APR-2025
DEFINITION  glutathione reductase, mitochondrial isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_000628
VERSION     NP_000628.2
DBSOURCE    REFSEQ: accession NM_000637.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Vyas,B., Bhowmik,R., Akhter,M. and Ahmad,F.J.
  TITLE     Identification, analysis of deleterious SNPs of the human GSR gene
            and their effects on the structure and functions of associated
            proteins and other diseases
  JOURNAL   Sci Rep 12 (1), 5474 (2022)
   PUBMED   35361806
  REMARK    GeneRIF: Identification, analysis of deleterious SNPs of the human
            GSR gene and their effects on the structure and functions of
            associated proteins and other diseases.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Zhang,C. and Zhao,D.
  TITLE     MicroRNA-362-5p promotes the proliferation and inhibits apoptosis
            of trophoblast cells via targeting glutathione-disulfide reductase
  JOURNAL   Bioengineered 12 (1), 2410-2419 (2021)
   PUBMED   34107852
  REMARK    GeneRIF: MicroRNA-362-5p promotes the proliferation and inhibits
            apoptosis of trophoblast cells via targeting glutathione-disulfide
            reductase.
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Lorestani,S., Bahari,A., Asadi,M. and Zahedi Avval,F.
  TITLE     Evaluation of glutathione reductase activity in colon tissue of
            patients with irritable bowel syndrome
  JOURNAL   Horm Mol Biol Clin Investig 42 (2), 195-198 (2021)
   PUBMED   34090318
  REMARK    GeneRIF: Evaluation of glutathione reductase activity in colon
            tissue of patients with irritable bowel syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Wang,Y.N., Lu,Y.X., Liu,J., Jin,Y., Bi,H.C., Zhao,Q., Liu,Z.X.,
            Li,Y.Q., Hu,J.J., Sheng,H., Jiang,Y.M., Zhang,C., Tian,F., Chen,Y.,
            Pan,Z.Z., Chen,G., Zeng,Z.L., Liu,K.Y., Ogasawara,M., Yun,J.P.,
            Ju,H.Q., Feng,J.X., Xie,D., Gao,S., Jia,W.H., Kopetz,S., Xu,R.H.
            and Wang,F.
  TITLE     AMPKalpha1 confers survival advantage of colorectal cancer cells
            under metabolic stress by promoting redox balance through the
            regulation of glutathione reductase phosphorylation
  JOURNAL   Oncogene 39 (3), 637-650 (2020)
   PUBMED   31530934
  REMARK    GeneRIF: AMPKalpha1 is overexpressed in colorectal cancer (CRC)
            patient specimens and the high expression is correlated with poor
            survival. AMPKalpha1 maintains high level of reduced glutathione to
            keep redox homeostasis under stress conditions, thus promoting CRC
            cell survival. Mechanistically, AMPKalpha1 regulate the glutathione
            reductase (GSR) phosphorylation possibly through residue Thr507
            which enhances its activity.
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Kelner,M.J. and Montoya,M.A.
  TITLE     Structural organization of the human glutathione reductase gene:
            determination of correct cDNA sequence and identification of a
            mitochondrial leader sequence
  JOURNAL   Biochem Biophys Res Commun 269 (2), 366-368 (2000)
   PUBMED   10708558
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Tutic,M., Lu,X.A., Schirmer,R.H. and Werner,D.
  TITLE     Cloning and sequencing of mammalian glutathione reductase cDNA
  JOURNAL   Eur J Biochem 188 (3), 523-528 (1990)
   PUBMED   2185014
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Krohne-Ehrich,G., Schirmer,R.H. and Untucht-Grau,R.
  TITLE     Glutathione reductase from human erythrocytes. Isolation of the
            enzyme and sequence analysis of the redox-active peptide
  JOURNAL   Eur J Biochem 80 (1), 65-71 (1977)
   PUBMED   923580
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Sinet,P.M., Bresson,J.L., Couturier,J., Laurent,C., Prieur,M.,
            Rethore,M.O., Taillemite,J.L., Toudic,D., Jerome,H. and Lejeune,J.
  TITLE     [Possible localization of the glutathione reductase (EC 1.6.4.2) on
            the 8p21 band]
  JOURNAL   Ann Genet 20 (1), 13-17 (1977)
   PUBMED   302667
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Loos,H., Roos,D., Weening,R. and Houwerzijl,J.
  TITLE     Familial deficiency of glutathione reductase in human blood cells
  JOURNAL   Blood 48 (1), 53-62 (1976)
   PUBMED   947404
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC069244.1, AC103959.18 and
            CA944703.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 15, 2004 this sequence version replaced NP_000628.1.
            
            Summary: This gene encodes a member of the class-I pyridine
            nucleotide-disulfide oxidoreductase family. This enzyme is a
            homodimeric flavoprotein. It is a central enzyme of cellular
            antioxidant defense, and reduces oxidized glutathione disulfide
            (GSSG) to the sulfhydryl form GSH, which is an important cellular
            antioxidant. Rare mutations in this gene result in hereditary
            glutathione reductase deficiency. Multiple alternatively spliced
            transcript variants encoding different isoforms have been found.
            [provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035691.1, FJ224321.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 10708558; reported by
                                                  MitoCarta
            MANE Ensembl match                 :: ENST00000221130.11/
                                                  ENSP00000221130.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..522
                     /product="glutathione reductase, mitochondrial isoform 1
                     precursor"
                     /EC_number="1.8.1.7"
                     /note="glutathione reductase, mitochondrial; glutathione
                     S-reductase; epididymis luminal protein 75; GRase;
                     epididymis secretory sperm binding protein Li 122m"
                     /calculated_mol_wt=51701
     transit_peptide 1..43
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P00390.2)"
                     /calculated_mol_wt=4574
     mat_peptide     44..522
                     /product="Glutathione reductase, mitochondrial.
                     /id=PRO_0000030276"
                     /note="propagated from UniProtKB/Swiss-Prot (P00390.2)"
                     /calculated_mol_wt=51701
     Region          63..522
                     /region_name="gluta_reduc_1"
                     /note="glutathione-disulfide reductase, animal/bacterial;
                     TIGR01421"
                     /db_xref="CDD:273614"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47791; propagated from
                     UniProtKB/Swiss-Prot (P00390.2)"
     CDS             1..522
                     /gene="GSR"
                     /gene_synonym="CNSHA10; GR; GSRD; HEL-75; HEL-S-122m"
                     /coded_by="NM_000637.5:12..1580"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS34877.1"
                     /db_xref="GeneID:2936"
                     /db_xref="HGNC:HGNC:4623"
                     /db_xref="MIM:138300"
ORIGIN      
        1 mallpralsa gagpswrraa rafrgfllll pepaaltral sramacrqep qpqgpppaag
       61 avasydylvi gggsgglasa rraaelgara avveshklgg tcvnvgcvpk kvmwntavhs
      121 efmhdhadyg fpscegkfnw rvikekrday vsrlnaiyqn nltkshieii rghaaftsdp
      181 kptievsgkk ytaphiliat ggmpstphes qipgaslgit sdgffqleel pgrsvivgag
      241 yiavemagil salgsktslm irhdkvlrsf dsmistncte elenagvevl kfsqvkevkk
      301 tlsglevsmv tavpgrlpvm tmipdvdcll waigrvpntk dlslnklgiq tddkghiivd
      361 efqntnvkgi yavgdvcgka lltpvaiaag rklahrlfey kedskldynn iptvvfshpp
      421 igtvgltede aihkygienv ktystsftpm yhavtkrktk cvmkmvcank eekvvgihmq
      481 glgcdemlqg favavkmgat kadfdntvai hptsseelvt lr
//
LOCUS       NP_004128                191 aa            linear   PRI 27-APR-2025
DEFINITION  calcium-activated potassium channel subunit beta-1 [Homo sapiens].
ACCESSION   NP_004128
VERSION     NP_004128.1
DBSOURCE    REFSEQ: accession NM_004137.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Scruggs,A.M., Grabauskas,G. and Huang,S.K.
  TITLE     The Role of KCNMB1 and BK Channels in Myofibroblast Differentiation
            and Pulmonary Fibrosis
  JOURNAL   Am J Respir Cell Mol Biol 62 (2), 191-203 (2020)
   PUBMED   31486669
  REMARK    GeneRIF: that epigenetic upregulation of KCNMB1 contributes to
            increased large-conductance (Big) potassium channel activity in
            idiopathic pulmonary fibrosis fibroblasts
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Lu,T., Chai,Q., Jiao,G., Wang,X.L., Sun,X., Furuseth,J.D.,
            Stulak,J.M., Daly,R.C., Greason,K.L., Cha,Y.M. and Lee,H.C.
  TITLE     Downregulation of BK channel function and protein expression in
            coronary arteriolar smooth muscle cells of type 2 diabetic patients
  JOURNAL   Cardiovasc Res 115 (1), 145-153 (2019)
   PUBMED   29850792
  REMARK    GeneRIF: Decreased protein expression and altered intrinsic
            properties of BKbeta1 channels mediates abnormal vasodilation in
            the coronary microvasculature of type 2 diabetics.
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Lorca,R.A., Ma,X. and England,S.K.
  TITLE     The unique N-terminal sequence of the BKCa channel alpha-subunit
            determines its modulation by beta-subunits
  JOURNAL   PLoS One 12 (7), e0182068 (2017)
   PUBMED   28750098
  REMARK    GeneRIF: These results provide further insights into the mechanism
            of modulation of the different N-terminal regions of the BKCa
            channel by beta-subunits.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Li,Y., Wang,X.L., Sun,X., Chai,Q., Li,J., Thompson,B., Shen,W.K.,
            Lu,T. and Lee,H.C.
  TITLE     Regulation of vascular large-conductance calcium-activated
            potassium channels by Nrf2 signalling
  JOURNAL   Diab Vasc Dis Res 14 (4), 353-362 (2017)
   PUBMED   28429615
  REMARK    GeneRIF: Expression of vascular large-conductance calcium-activated
            potassium channel Kcnmb1 is regulated by Nrf2 signaling.
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Valverde,M.A., Rojas,P., Amigo,J., Cosmelli,D., Orio,P.,
            Bahamonde,M.I., Mann,G.E., Vergara,C. and Latorre,R.
  TITLE     Acute activation of Maxi-K channels (hSlo) by estradiol binding to
            the beta subunit
  JOURNAL   Science 285 (5435), 1929-1931 (1999)
   PUBMED   10489376
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Jiang,Z., Wallner,M., Meera,P. and Toro,L.
  TITLE     Human and rodent MaxiK channel beta-subunit genes: cloning and
            characterization
  JOURNAL   Genomics 55 (1), 57-67 (1999)
   PUBMED   9888999
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Tseng-Crank,J., Godinot,N., Johansen,T.E., Ahring,P.K.,
            Strobaek,D., Mertz,R., Foster,C.D., Olesen,S.P. and Reinhart,P.H.
  TITLE     Cloning, expression, and distribution of a Ca(2+)-activated K+
            channel beta-subunit from human brain
  JOURNAL   Proc Natl Acad Sci U S A 93 (17), 9200-9205 (1996)
   PUBMED   8799178
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Dworetzky,S.I., Boissard,C.G., Lum-Ragan,J.T., McKay,M.C.,
            Post-Munson,D.J., Trojnacki,J.T., Chang,C.P. and Gribkoff,V.K.
  TITLE     Phenotypic alteration of a human BK (hSlo) channel by hSlobeta
            subunit coexpression: changes in blocker sensitivity,
            activation/relaxation and inactivation kinetics, and protein kinase
            A modulation
  JOURNAL   J Neurosci 16 (15), 4543-4550 (1996)
   PUBMED   8764643
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Meera,P., Wallner,M., Jiang,Z. and Toro,L.
  TITLE     A calcium switch for the functional coupling between alpha (hslo)
            and beta subunits (KV,Ca beta) of maxi K channels
  JOURNAL   FEBS Lett 382 (1-2), 84-88 (1996)
   PUBMED   8612769
  REMARK    Erratum:[FEBS Lett. 1996 Apr 29;385(1-2):127-8. doi:
            10.1016/0014-5793(96)83884-1. PMID: 8641456]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC134820.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: MaxiK channels are large conductance, voltage and
            calcium-sensitive potassium channels which are fundamental to the
            control of smooth muscle tone and neuronal excitability. MaxiK
            channels can be formed by 2 subunits: the pore-forming alpha
            subunit and the product of this gene, the modulatory beta subunit.
            Intracellular calcium regulates the physical association between
            the alpha and beta subunits. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U25138.1, SRR5189655.201403.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159368 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274629.9/ ENSP00000274629.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.1"
     Protein         1..191
                     /product="calcium-activated potassium channel subunit
                     beta-1"
                     /note="large conductance Ca2+-activated K+ channel beta 1
                     subunit; calcium-activated potassium channel, subfamily M
                     subunit beta-1; BK channel subunit beta-1; maxi K channel
                     subunit beta-1; charybdotoxin receptor subunit beta-1;
                     potassium large conductance calcium-activated channel,
                     subfamily M, beta member 1; BK channel beta subunit 1;
                     MaxiK channel beta-subunit 1; big potassium channel beta
                     subunit 1; potassium channel subfamily M regulatory beta
                     subunit 1"
                     /calculated_mol_wt=21666
     Region          7..190
                     /region_name="CaKB"
                     /note="Calcium-activated potassium channel, beta subunit;
                     pfam03185"
                     /db_xref="CDD:460838"
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16558.5)"
     Site            80
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16558.5)"
     Site            142
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16558.5)"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16558.5)"
     CDS             1..191
                     /gene="KCNMB1"
                     /gene_synonym="BKbeta1; hbeta1; hslo-beta; K(VCA)beta;
                     k(VCA)beta-1; SLO-BETA; slo-beta-1"
                     /coded_by="NM_004137.4:134..709"
                     /db_xref="CCDS:CCDS4373.1"
                     /db_xref="GeneID:3779"
                     /db_xref="HGNC:HGNC:6285"
                     /db_xref="MIM:603951"
ORIGIN      
        1 mvkklvmaqk rgetralclg vtmvvcavit yyilvttvlp lyqksvwtqe skchlietni
       61 rdqeelkgkk vpqypclwvn vsaagrwavl yhtedtrdqn qqcsyipgsv dnyqtaradv
      121 ekvrakfqeq qvfycfsapr gnetsvlfqr lygpqallfs lfwptflltg glliiamvks
      181 nqylsilaaq k
//
LOCUS       NP_004414                716 aa            linear   PRI 27-APR-2025
DEFINITION  segment polarity protein dishevelled homolog DVL-3 [Homo sapiens].
ACCESSION   NP_004414
VERSION     NP_004414.3
DBSOURCE    REFSEQ: accession NM_004423.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Zhao,H., Wu,G., Luo,Y., Xie,Y., Han,Y., Zhang,D., Han,Q., Zhao,X.,
            Qin,Y., Li,Q. and Wang,E.
  TITLE     WNT5B promotes the malignant phenotype of non-small cell lung
            cancer via the FZD3-DVL3-RAC1-PCP-JNK pathway
  JOURNAL   Cell Signal 122, 111330 (2024)
   PUBMED   39094673
  REMARK    GeneRIF: WNT5B promotes the malignant phenotype of non-small cell
            lung cancer via the FZD3-DVL3-RAC1-PCP-JNK pathway.
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Zhang,Y., Lin,N., Liu,X. and Yao,T.
  TITLE     Dishevelled Segment Polarity Protein 3 (DVL3) Induced by Bacterial
            LPS Promotes the Proliferation and Migration of Prostate Cancer
            Cells through the TLR4 Pathway
  JOURNAL   Arch Esp Urol 77 (2), 193-201 (2024)
   PUBMED   38583012
  REMARK    GeneRIF: Dishevelled Segment Polarity Protein 3 (DVL3) Induced by
            Bacterial LPS Promotes the Proliferation and Migration of Prostate
            Cancer Cells through the TLR4 Pathway.
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Li,Z., Yang,Z., Liu,W., Zhu,W., Yin,L., Han,Z., Xian,Y., Wen,J.,
            Tang,H., Lin,X., Yang,Y., Wang,J. and Zhang,K.
  TITLE     Disheveled3 enhanced EMT and cancer stem-like cells properties via
            Wnt/beta-catenin/c-Myc/SOX2 pathway in colorectal cancer
  JOURNAL   J Transl Med 21 (1), 302 (2023)
   PUBMED   37147666
  REMARK    GeneRIF: Disheveled3 enhanced EMT and cancer stem-like cells
            properties via Wnt/beta-catenin/c-Myc/SOX2 pathway in colorectal
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Yang,P., Zhang,P. and Zhang,S.
  TITLE     RNA-Binding Protein MEX3A Interacting with DVL3 Stabilizes
            Wnt/beta-Catenin Signaling in Endometrial Carcinoma
  JOURNAL   Int J Mol Sci 24 (1), 592 (2022)
   PUBMED   36614043
  REMARK    GeneRIF: RNA-Binding Protein MEX3A Interacting with DVL3 Stabilizes
            Wnt/beta-Catenin Signaling in Endometrial Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 716)
  AUTHORS   Pruller,J., Figeac,N. and Zammit,P.S.
  TITLE     DVL1 and DVL3 require nuclear localisation to regulate
            proliferation in human myoblasts
  JOURNAL   Sci Rep 12 (1), 8388 (2022)
   PUBMED   35589804
  REMARK    GeneRIF: DVL1 and DVL3 require nuclear localisation to regulate
            proliferation in human myoblasts.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 716)
  AUTHORS   Kishida,S., Yamamoto,H., Hino,S., Ikeda,S., Kishida,M. and
            Kikuchi,A.
  TITLE     DIX domains of Dvl and axin are necessary for protein interactions
            and their ability to regulate beta-catenin stability
  JOURNAL   Mol Cell Biol 19 (6), 4414-4422 (1999)
   PUBMED   10330181
REFERENCE   7  (residues 1 to 716)
  AUTHORS   Bui,T.D., Beier,D.R., Jonssen,M., Smith,K., Dorrington,S.M.,
            Kaklamanis,L., Kearney,L., Regan,R., Sussman,D.J. and Harris,A.L.
  TITLE     cDNA cloning of a human dishevelled DVL-3 gene, mapping to 3q27,
            and expression in human breast and colon carcinomas
  JOURNAL   Biochem Biophys Res Commun 239 (2), 510-516 (1997)
   PUBMED   9344861
REFERENCE   8  (residues 1 to 716)
  AUTHORS   Semenov,M.V. and Snyder,M.
  TITLE     Human dishevelled genes constitute a DHR-containing multigene
            family
  JOURNAL   Genomics 42 (2), 302-310 (1997)
   PUBMED   9192851
REFERENCE   9  (residues 1 to 716)
  AUTHORS   Pizzuti,A., Amati,F., Calabrese,G., Mari,A., Colosimo,A.,
            Silani,V., Giardino,L., Ratti,A., Penso,D., Calza,L., Palka,G.,
            Scarlato,G., Novelli,G. and Dallapiccola,B.
  TITLE     cDNA characterization and chromosomal mapping of two human
            homologues of the Drosophila dishevelled polarity gene
  JOURNAL   Hum Mol Genet 5 (7), 953-958 (1996)
   PUBMED   8817329
REFERENCE   10 (residues 1 to 716)
  AUTHORS   Roifman,M., Brunner,H., Lohr,J., Mazzeu,J. and Chitayat,D.
  TITLE     Autosomal Dominant Robinow Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25577943
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC131235.4, U75651.1 and
            D86963.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 30, 2004 this sequence version replaced NP_004414.2.
            
            Summary: This gene is a member of a multi-gene family which shares
            strong similarity with the Drosophila dishevelled gene, dsh. The
            Drosophila dishevelled gene encodes a cytoplasmic phosphoprotein
            that regulates cell proliferation. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D86963.1, U75651.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313143.9/ ENSP00000316054.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..716
                     /product="segment polarity protein dishevelled homolog
                     DVL-3"
                     /note="dishevelled 3 (homologous to Drosophila dsh);
                     dishevelled, dsh homolog 3"
                     /calculated_mol_wt=77924
     Region          1..82
                     /region_name="DAX"
                     /note="Domain present in Dishevelled and axin; smart00021"
                     /db_xref="CDD:197474"
     Site            27
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000269|PubMed:22612246; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     Region          85..235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92997.2)"
     Region          87..245
                     /region_name="Dishevelled"
                     /note="Dishevelled specific domain; pfam02377"
                     /db_xref="CDD:460544"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22612246,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92997.2)"
     Site            212
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000269|PubMed:22612246; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     Region          249..335
                     /region_name="PDZ_Dishevelled-like"
                     /note="PDZ domain of segment polarity protein dishevelled
                     homolog DVL1, DVL2, DVL3, and related domains; cd06717"
                     /db_xref="CDD:467201"
     Site            order(259..265,279,282,312,316,319..320)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467201"
     Site            271
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23150776; Symmetric
                     dimethylarginine, by PRMT7, alternate.
                     /evidence=ECO:0000269|PubMed:23150776; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     Site            342
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:22612246,
                     ECO:0000269|PubMed:23150776; Symmetric dimethylarginine,
                     by PRMT7, alternate.
                     /evidence=ECO:0000269|PubMed:22612246,
                     ECO:0000269|PubMed:23150776; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:22612246; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     Region          413..496
                     /region_name="DEP_dishevelled"
                     /note="DEP (Dishevelled, Egl-10, and Pleckstrin) domain
                     found in dishevelled-like proteins. Dishevelled-like
                     proteins play a key role in the transduction of the Wnt
                     signal from the cell surface to the nucleus, which in turn
                     is an important regulatory pathway...; cd04438"
                     /db_xref="CDD:239885"
     Region          500..706
                     /region_name="Dsh_C"
                     /note="Segment polarity protein dishevelled (Dsh) C
                     terminal; pfam12316"
                     /db_xref="CDD:463531"
     Region          546..691
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92997.2)"
     Site            614
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT7.
                     /evidence=ECO:0000269|PubMed:23150776; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     Site            698
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|PubMed:22612246;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:22612246; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22612246; propagated from
                     UniProtKB/Swiss-Prot (Q92997.2)"
     CDS             1..716
                     /gene="DVL3"
                     /gene_synonym="DRS3"
                     /coded_by="NM_004423.4:260..2410"
                     /db_xref="CCDS:CCDS3253.1"
                     /db_xref="GeneID:1857"
                     /db_xref="HGNC:HGNC:3087"
                     /db_xref="MIM:601368"
ORIGIN      
        1 mgetkiiyhl dgqetpylvk lplpaervtl adfkgvlqrp sykfffksmd ddfgvvkeei
       61 sddnaklpcf ngrvvswlvs aegshpdpap fcadnpselp ppmertggig dsrppsfhph
      121 agggsqenld ndtetdslvs aqrerprrrd gpehatrlng takgerrrep ggydssstlm
      181 sselettsff dsdeddstsr fsssteqssa srlmrrhkrr rrkqkvsrie rsssfssitd
      241 stmslniitv tlnmekynfl gisivgqsne rgdggiyigs imkggavaad griepgdmll
      301 qvneinfenm snddavrvlr eivhkpgpit ltvakcwdps prgcftlprs epirpidpaa
      361 wvshtaamtg tfpaygmsps lstitstsss itssipdter lddfhlsihs dmaaivkama
      421 spesglevrd rmwlkitipn afigsdvvdw lyhnvegftd rrearkyasn llkagfirht
      481 vnkitfseqc yyifgdlcgn manlslhdhd gssgasdqdt laplphpgaa pwpmafpyqy
      541 pppphpynph pgfpelgysy gggsassqhs egsrssgsnr sgsdrrkekd pkagdsksgg
      601 sgsesdhttr sslrgprera psersgpaas ehshrshhsl asslrshhth psygppgvpp
      661 lygppmlmmp pppaamgppg appgrdlasv ppeltasrqs frmamgnpse ffvdvm
//
LOCUS       NP_001665                181 aa            linear   PRI 27-APR-2025
DEFINITION  cyclic AMP-dependent transcription factor ATF-3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001665
VERSION     NP_001665.1
DBSOURCE    REFSEQ: accession NM_001674.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Hu,H., Liu,Y., Qiu,C., Zhang,L., Cui,H. and Gu,J.
  TITLE     LINC00894 inhibited neuron cellular apoptosis and regulated
            activating transcription factor 3 expression
  JOURNAL   Gene 927, 148670 (2024)
   PUBMED   38857714
  REMARK    GeneRIF: LINC00894 inhibited neuron cellular apoptosis and
            regulated activating transcription factor 3 expression.
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Wen,Y., Liu,Y., Li,Q., Tan,J., Fu,X., Liang,Y., Tuo,Y., Liu,L.,
            Zhou,X., LiuFu,D., Fan,X., Chen,C., Chen,Z., Wang,Z., Fan,S.,
            Liu,R., Pan,L., Zhang,Y. and Tang,W.H.
  TITLE     Spatiotemporal ATF3 Expression Determines VSMC Fate in Abdominal
            Aortic Aneurysm
  JOURNAL   Circ Res 134 (11), 1495-1511 (2024)
   PUBMED   38686580
  REMARK    GeneRIF: Spatiotemporal ATF3 Expression Determines VSMC Fate in
            Abdominal Aortic Aneurysm.
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Miyazaki,K., Inoue,S., Yamada,K., Watanabe,M., Liu,Q., Watanabe,T.,
            Adachi,M.T., Tanaka,Y. and Kitajima,S.
  TITLE     Differential usage of alternate promoters of the human stress
            response gene ATF3 in stress response and cancer cells
  JOURNAL   Nucleic Acids Res 37 (5), 1438-1451 (2009)
   PUBMED   19136462
  REMARK    GeneRIF: In human prostate and Hodgkin Reed-Sternberg cancer cells
            with elevated expression of ATF3, the P1 promoter was
            constitutively activated and its chromatin structure was modified
            into active configuration.
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Hua,B., Tamamori-Adachi,M., Luo,Y., Tamura,K., Morioka,M.,
            Fukuda,M., Tanaka,Y. and Kitajima,S.
  TITLE     A splice variant of stress response gene ATF3 counteracts
            NF-kappaB-dependent anti-apoptosis through inhibiting recruitment
            of CREB-binding protein/p300 coactivator
  JOURNAL   J Biol Chem 281 (3), 1620-1629 (2006)
   PUBMED   16291753
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Pan,Y., Chen,H., Siu,F. and Kilberg,M.S.
  TITLE     Amino acid deprivation and endoplasmic reticulum stress induce
            expression of multiple activating transcription factor-3 mRNA
            species that, when overexpressed in HepG2 cells, modulate
            transcription by the human asparagine synthetase promoter
  JOURNAL   J Biol Chem 278 (40), 38402-38412 (2003)
   PUBMED   12881527
  REMARK    GeneRIF: ATF3 isoforms have a role in the transcriptional
            regulation of the ASNS gene in response to nutrient deprivation
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Hashimoto,Y., Zhang,C., Kawauchi,J., Imoto,I., Adachi,M.T.,
            Inazawa,J., Amagasa,T., Hai,T. and Kitajima,S.
  TITLE     An alternatively spliced isoform of transcriptional repressor ATF3
            and its induction by stress stimuli
  JOURNAL   Nucleic Acids Res 30 (11), 2398-2406 (2002)
   PUBMED   12034827
  REMARK    GeneRIF: An alternatively spliced isoform of transcriptional
            repressor ATF3 and its induction by stress stimuli.
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Liang,G., Wolfgang,C.D., Chen,B.P., Chen,T.H. and Hai,T.
  TITLE     ATF3 gene. Genomic organization, promoter, and regulation
  JOURNAL   J Biol Chem 271 (3), 1695-1701 (1996)
   PUBMED   8576171
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Chen,B.P., Liang,G., Whelan,J. and Hai,T.
  TITLE     ATF3 and ATF3 delta Zip. Transcriptional repression versus
            activation by alternatively spliced isoforms
  JOURNAL   J Biol Chem 269 (22), 15819-15826 (1994)
   PUBMED   7515060
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Hsu,J.C., Bravo,R. and Taub,R.
  TITLE     Interactions among LRF-1, JunB, c-Jun, and c-Fos define a
            regulatory program in the G1 phase of liver regeneration
  JOURNAL   Mol Cell Biol 12 (10), 4654-4665 (1992)
   PUBMED   1406655
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Hai,T.W., Liu,F., Coukos,W.J. and Green,M.R.
  TITLE     Transcription factor ATF cDNA clones: an extensive family of
            leucine zipper proteins able to selectively form DNA-binding
            heterodimers
  JOURNAL   Genes Dev 3 (12B), 2083-2090 (1989)
   PUBMED   2516827
  REMARK    Erratum:[Genes Dev 1990 Apr;4(4):682]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL560585.3, BC006322.2,
            AI949953.1 and CD742713.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the mammalian activation
            transcription factor/cAMP responsive element-binding (CREB) protein
            family of transcription factors. This gene is induced by a variety
            of signals, including many of those encountered by cancer cells,
            and is involved in the complex process of cellular stress response.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. It is possible that alternative splicing of
            this gene may be physiologically important in the regulation of
            target genes. [provided by RefSeq, Apr 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1), which represses rather than activates transcription from
            promoters with ATF-binding elements. Both variants 1 and 3 encode
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC006322.2, L19871.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341491.9/ ENSP00000344352.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..181
                     /product="cyclic AMP-dependent transcription factor ATF-3
                     isoform 1"
                     /note="cyclic AMP-dependent transcription factor ATF-3;
                     cAMP-dependent transcription factor ATF-3"
                     /calculated_mol_wt=20445
     Region          88..110
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P18847.2)"
     Region          96..149
                     /region_name="bZIP_ATF3"
                     /note="Basic leucine zipper (bZIP) domain of Activating
                     Transcription Factor-3 (ATF-3) and similar proteins: a
                     DNA-binding and dimerization domain; cd14722"
                     /db_xref="CDD:269870"
     Region          96..146
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269870"
     Site            order(107,110..111,114..115,117..118,121..122,124..125,
                     128..129,131..132,135..136,138..139,142..143,145..146)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269870"
     Region          114..142
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P18847.2)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P18847.2)"
     CDS             1..181
                     /gene="ATF3"
                     /coded_by="NM_001674.4:175..720"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1506.1"
                     /db_xref="GeneID:467"
                     /db_xref="HGNC:HGNC:785"
                     /db_xref="MIM:603148"
ORIGIN      
        1 mmlqhpgqvs asevsasaiv pclsppgslv fedfanltpf vkeelrfaiq nkhlchrmss
       61 alesvtvsdr plgvsitkae vapeederkk rrrernkiaa akcrnkkkek teclqkesek
      121 lesvnaelka qieelknekq hliymlnlhr ptcivraqng rtpedernlf iqqikegtlq
      181 s
//
LOCUS       NP_001035521             106 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome c oxidase assembly factor 3 homolog, mitochondrial [Homo
            sapiens].
ACCESSION   NP_001035521
VERSION     NP_001035521.1
DBSOURCE    REFSEQ: accession NM_001040431.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Neira,J.L., Martinez-Rodriguez,S., Hernandez-Cifre,J.G.,
            Camara-Artigas,A., Clemente,P., Peralta,S., Fernandez-Moreno,M.A.,
            Garesse,R., Garcia de la Torre,J. and Rizzuti,B.
  TITLE     Human COA3 Is an Oligomeric Highly Flexible Protein in Solution
  JOURNAL   Biochemistry 55 (45), 6209-6220 (2016)
   PUBMED   27791355
  REMARK    GeneRIF: Data suggest that COX assembly factor 3 (hCOA3) is a
            disordered protein and that the flexibility of hCOA3 is crucial for
            its interaction with other proteins to favor mitochondrial protein
            translocation and assembly of proteins involved in the respiratory
            chain.
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Ban-Ishihara,R., Tomohiro-Takamiya,S., Tani,M., Baudier,J.,
            Ishihara,N. and Kuge,O.
  TITLE     COX assembly factor ccdc56 regulates mitochondrial morphology by
            affecting mitochondrial recruitment of Drp1
  JOURNAL   FEBS Lett 589 (20 Pt B), 3126-3132 (2015)
   PUBMED   26358295
  REMARK    GeneRIF: Data show that mitochondrial protein ccdc56/MITRAC12/COA3
            positively regulates mitochondrial fission by recruiting the
            fission factor Drp1.
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Dennerlein,S., Oeljeklaus,S., Jans,D., Hellwig,C., Bareth,B.,
            Jakobs,S., Deckers,M., Warscheid,B. and Rehling,P.
  TITLE     MITRAC7 Acts as a COX1-Specific Chaperone and Reveals a Checkpoint
            during Cytochrome c Oxidase Assembly
  JOURNAL   Cell Rep 12 (10), 1644-1655 (2015)
   PUBMED   26321642
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Ostergaard,E., Weraarpachai,W., Ravn,K., Born,A.P., Jonson,L.,
            Duno,M., Wibrand,F., Shoubridge,E.A. and Vissing,J.
  TITLE     Mutations in COA3 cause isolated complex IV deficiency associated
            with neuropathy, exercise intolerance, obesity, and short stature
  JOURNAL   J Med Genet 52 (3), 203-207 (2015)
   PUBMED   25604084
  REMARK    GeneRIF: COX14 was undetectable in COA3 subject fibroblasts, and
            that COA3 was undetectable in fibroblasts from a COX14 subject,
            demonstrating the interdependence of these two COX assembly factors
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Clemente,P., Peralta,S., Cruz-Bermudez,A., Echevarria,L.,
            Fontanesi,F., Barrientos,A., Fernandez-Moreno,M.A. and Garesse,R.
  TITLE     hCOA3 stabilizes cytochrome c oxidase 1 (COX1) and promotes
            cytochrome c oxidase assembly in human mitochondria
  JOURNAL   J Biol Chem 288 (12), 8321-8331 (2013)
   PUBMED   23362268
  REMARK    GeneRIF: hCOA3 stabilizes COX1 co-translationally and promotes its
            assembly with COX partner subunits.
REFERENCE   7  (residues 1 to 106)
  AUTHORS   Mick,D.U., Dennerlein,S., Wiese,H., Reinhold,R., Pacheu-Grau,D.,
            Lorenzi,I., Sasarman,F., Weraarpachai,W., Shoubridge,E.A.,
            Warscheid,B. and Rehling,P.
  TITLE     MITRAC links mitochondrial protein translocation to
            respiratory-chain assembly and translational regulation
  JOURNAL   Cell 151 (7), 1528-1541 (2012)
   PUBMED   23260140
  REMARK    GeneRIF: Study comprehensively identified mammalian cytochrome c
            oxidase assembly factors. These analyses led to the discoveryof
            MITRAC12, which defines the MITRAC (mitochondrial translation
            regulation assembly intermediate of cytochrome c oxidase)complexes.
REFERENCE   8  (residues 1 to 106)
  AUTHORS   Peralta,S., Clemente,P., Sanchez-Martinez,A., Calleja,M.,
            Hernandez-Sierra,R., Matsushima,Y., Adan,C., Ugalde,C.,
            Fernandez-Moreno,M.A., Kaguni,L.S. and Garesse,R.
  TITLE     Coiled coil domain-containing protein 56 (CCDC56) is a novel
            mitochondrial protein essential for cytochrome c oxidase function
  JOURNAL   J Biol Chem 287 (29), 24174-24185 (2012)
   PUBMED   22610097
REFERENCE   9  (residues 1 to 106)
  AUTHORS   Szklarczyk,R., Wanschers,B.F., Cuypers,T.D., Esseling,J.J.,
            Riemersma,M., van den Brand,M.A., Gloerich,J., Lasonder,E., van den
            Heuvel,L.P., Nijtmans,L.G. and Huynen,M.A.
  TITLE     Iterative orthology prediction uncovers new mitochondrial proteins
            and identifies C12orf62 as the human ortholog of COX14, a protein
            involved in the assembly of cytochrome c oxidase
  JOURNAL   Genome Biol 13 (2), R12 (2012)
   PUBMED   22356826
  REMARK    GeneRIF: Human ortholog of fungal COA3 (Cytochrome oxidase
            assembly)
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 106)
  AUTHORS   Rommens,J.M., Durocher,F., McArthur,J., Tonin,P., LeBlanc,J.F.,
            Allen,T., Samson,C., Ferri,L., Narod,S., Morgan,K. et al.
  TITLE     Generation of a transcription map at the HSD17B locus centromeric
            to BRCA1 at 17q21
  JOURNAL   Genomics 28 (3), 530-542 (1995)
   PUBMED   7490091
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL524532.3, BC002698.2 and
            AC016889.28.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the cytochrome c oxidase
            assembly factor family. Studies of a related gene in fly suggest
            that the encoded protein is localized to mitochondria and is
            essential for cytochrome c oxidase function. [provided by RefSeq,
            Nov 2012].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225611.1, SRR5189661.151737.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000328434.8/ ENSP00000354762.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..106
                     /product="cytochrome c oxidase assembly factor 3 homolog,
                     mitochondrial"
                     /note="coiled-coil domain-containing protein 56;
                     cytochrome c oxidase assembly protein 3 homolog,
                     mitochondrial; mitochondrial translation regulation
                     assembly intermediate of cytochrome c oxidase protein of
                     12 kDa"
                     /calculated_mol_wt=11600
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2R0.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2R0.1)"
     Region          45..91
                     /region_name="Coa3_cc"
                     /note="Cytochrome c oxidase assembly factor 3; pfam09813"
                     /db_xref="CDD:462910"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2R0.1)"
     CDS             1..106
                     /gene="COA3"
                     /gene_synonym="CCDC56; COX25; hCOA3; HSPC009; MC4DN14;
                     MITRAC12"
                     /coded_by="NM_001040431.3:24..344"
                     /db_xref="CCDS:CCDS32660.1"
                     /db_xref="GeneID:28958"
                     /db_xref="HGNC:HGNC:24990"
                     /db_xref="MIM:614775"
ORIGIN      
        1 massgagdpl dskrgeapfa qridptrekl tpeqlhsmrq aelaqwqkvl prrrtrnivt
       61 glgigalvla iygytfysis qerfldeled eakaararal arasgs
//
LOCUS       NP_001348953             842 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 9 [Mus musculus].
ACCESSION   NP_001348953 XP_017169125
VERSION     NP_001348953.1
DBSOURCE    REFSEQ: accession NM_001362024.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 842)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 842)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 842)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 842)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 842)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 842)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 842)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 842)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 842)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            On Mar 31, 2018 this sequence version replaced XP_017169125.1.
            
            Transcript Variant: This variant (34), as well as variants 32, 33,
            35, and 36, encodes isoform 9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164131
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..842
                     /product="cAMP-regulated phosphoprotein 21 isoform 9"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=92280
     Region          162..223
                     /region_name="R3H_encore_like"
                     /note="R3H domain of encore-like and DIP1-like proteins.
                     Drosophila encore is involved in the germline exit after
                     four mitotic divisions, by facilitating
                     SCF-ubiquitin-proteasome-dependent proteolysis. Maize
                     DBF1-interactor protein 1 (DIP1) containing an R3H...;
                     cd02642"
                     /db_xref="CDD:100071"
     Site            order(195,199)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100071"
     Region          244..298
                     /region_name="SUZ"
                     /note="SUZ domain; pfam12752"
                     /db_xref="CDD:463689"
     Region          588..>817
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..842
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362024.1:434..2962"
                     /note="isoform 9 is encoded by transcript variant 34"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqesih lqlssfpslq eedksrkdds erekekdknr
      121 eklserpkir mlskdcsqey tdstgidlhg flintlknns rdrmillkme qemidfiads
      181 nnhykkfpqm ssyqrmlvhr vaayfgldhn vdqtgksvii nktsstripe qrfcehlkde
      241 kseesqkrfi lkrdnssidk ednqnrmhpf rddrrsksie ereeeyqrvr erifahdsvc
      301 sqeslfldns rlqedmhicn etykkrqlfr ahrdssgrts gsrqsssete lrwpdhqraw
      361 sstdsdssnr nlkptmtkta sfggitvltr gdstsstrsa gklsktgses sssagssgsl
      421 srthpqstal tssvaagspg cmaysengmg gqvppsstsy illplesatg ippgsillnp
      481 htgqpfvnpd gtpaiynppg sqqtlrgtvg gqpqqppqqq pspqpqqqvq asqpqmagpl
      541 vtqsvqslqp ssqsvqypav sfppqhllpm sptqhfplre elaaqfsqls msrqssgdtp
      601 eppsgtvypa sllpqtaqpq syvitsagqq lstggfsdsg ppisqqvlqa ppspqgfvqq
      661 pppaqmsvyy ypsgqyptst sqqyrplasv qysaqrsqqi pqttqqagyq pvlsgqqgfq
      721 gmmgvqqsah sqgvmssqqg apvhgvmvsy ptmssyqvpm tqgsqavpqq tyqppimlps
      781 qagqgslpat gmpvycnvtp pnpqnnlrlm gphcpsstvp vmsascrtnc gnvsnagwqv
      841 kf
//
LOCUS       NP_659447                256 aa            linear   PRI 27-APR-2025
DEFINITION  enkurin isoform 1 [Homo sapiens].
ACCESSION   NP_659447
VERSION     NP_659447.1
DBSOURCE    REFSEQ: accession NM_145010.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Seetharam,S.M., Liu,Y., Wu,J., Fechter,L., Murugesan,K.,
            Maecker,H., Gotlib,J., Zehnder,J., Paulmurugan,R. and Krishnan,A.
  TITLE     Enkurin: a novel marker for myeloproliferative neoplasms from
            platelet, megakaryocyte, and whole blood specimens
  JOURNAL   Blood Adv 7 (18), 5433-5445 (2023)
   PUBMED   37315179
  REMARK    GeneRIF: Enkurin: a novel marker for myeloproliferative neoplasms
            from platelet, megakaryocyte, and whole blood specimens.
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Gui,M., Croft,J.T., Zabeo,D., Acharya,V., Kollman,J.M.,
            Burgoyne,T., Hoog,J.L. and Brown,A.
  TITLE     SPACA9 is a lumenal protein of human ciliary singlet and doublet
            microtubules
  JOURNAL   Proc Natl Acad Sci U S A 119 (41), e2207605119 (2022)
   PUBMED   36191189
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Hou,R., Li,Y., Luo,X., Zhang,W., Yang,H., Zhang,Y., Liu,J., Liu,S.,
            Han,S., Liu,C., Huang,Y., Liu,Z., Li,A. and Fang,W.
  TITLE     ENKUR expression induced by chemically synthesized cinobufotalin
            suppresses malignant activities of hepatocellular carcinoma by
            modulating beta-catenin/c-Jun/MYH9/USP7/c-Myc axis
  JOURNAL   Int J Biol Sci 18 (6), 2553-2567 (2022)
   PUBMED   35414777
  REMARK    GeneRIF: ENKUR expression induced by chemically synthesized
            cinobufotalin suppresses malignant activities of hepatocellular
            carcinoma by modulating beta-catenin/c-Jun/MYH9/USP7/c-Myc axis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Ma,Q., Lu,Y. and Gu,Y.
  TITLE     ENKUR Is Involved in the Regulation of Cellular Biology in
            Colorectal Cancer Cells via PI3K/Akt Signaling Pathway
  JOURNAL   Technol Cancer Res Treat 18, 1533033819841433 (2019)
   PUBMED   30947633
  REMARK    GeneRIF: Decreased ENKUR expression is associated with Colorectal
            Cancer.
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Sigg,M.A., Menchen,T., Lee,C., Johnson,J., Jungnickel,M.K.,
            Choksi,S.P., Garcia,G. 3rd, Busengdal,H., Dougherty,G.W.,
            Pennekamp,P., Werner,C., Rentzsch,F., Florman,H.M., Krogan,N.,
            Wallingford,J.B., Omran,H. and Reiter,J.F.
  TITLE     Evolutionary Proteomics Uncovers Ancient Associations of Cilia with
            Signaling Pathways
  JOURNAL   Dev Cell 43 (6), 744-762 (2017)
   PUBMED   29257953
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Beech,D.J.
  TITLE     Canonical transient receptor potential 5
  JOURNAL   Handb Exp Pharmacol (179), 109-123 (2007)
   PUBMED   17217053
  REMARK    Review article
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Sutton,K.A., Jungnickel,M.K., Wang,Y., Cullen,K., Lambert,S. and
            Florman,H.M.
  TITLE     Enkurin is a novel calmodulin and TRPC channel binding protein in
            sperm
  JOURNAL   Dev Biol 274 (2), 426-435 (2004)
   PUBMED   15385169
  REMARK    GeneRIF: Data suggest that enkurin is an adaptor that functions to
            localize a Ca2+ sensitive signal transduction machinery in sperm to
            a Ca2+-permeable ion channel [enkurin]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL512598.11, BC026165.2,
            AK095021.1 and BM979174.1.
            
            Summary: This gene encodes a protein that interacts with calmodulin
            and several transient receptor potential canonical cation channel
            proteins. The encoded protein may function as an adaptor to
            localize signal transduction machinery to calcium channels.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer protein (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK095021.1, SRR1660803.177500.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331161.9/ ENSP00000331044.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..256
                     /product="enkurin isoform 1"
                     /calculated_mol_wt=29323
     Region          83..89
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC29.1)"
     Region          152..246
                     /region_name="Enkurin"
                     /note="Calmodulin-binding; pfam13864"
                     /db_xref="CDD:464004"
     Region          160..255
                     /region_name="Interaction with TRPC proteins.
                     /evidence=ECO:0000250|UniProtKB:Q6SP97"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC29.1)"
     CDS             1..256
                     /gene="ENKUR"
                     /gene_synonym="C10orf63; CFAP106"
                     /coded_by="NM_145010.4:223..993"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7146.1"
                     /db_xref="GeneID:219670"
                     /db_xref="HGNC:HGNC:28388"
                     /db_xref="MIM:611025"
ORIGIN      
        1 mdptcsseci ynlipsdlke ppqppryisi fkatvkddmq kaktamktmg pakvevpspk
       61 dflkkhskek tlppkknfdr nvpkkpavpl ktdhpvmgiq sgknfintna adiimgvakk
      121 pkpiyvdkrt gdkhdlepsg lvpkyinkkd ygvtpeyick rneeikkaqe dydryiqenl
      181 kkaamkrlsd eereavlqgl kknweevhke fqslsvfids ipkkirkqrl eeemkqlehd
      241 igiiekhkii yianna
//
LOCUS       NP_000842                218 aa            linear   PRI 27-APR-2025
DEFINITION  glutathione S-transferase Mu 5 [Homo sapiens].
ACCESSION   NP_000842
VERSION     NP_000842.2
DBSOURCE    REFSEQ: accession NM_000851.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Hao,X., Zhang,J., Chen,G., Cao,W., Chen,H. and Chen,S.
  TITLE     Aberrant expression of GSTM5 in lung adenocarcinoma is associated
            with DNA hypermethylation and poor prognosis
  JOURNAL   BMC Cancer 22 (1), 685 (2022)
   PUBMED   35729618
  REMARK    GeneRIF: Aberrant expression of GSTM5 in lung adenocarcinoma is
            associated with DNA hypermethylation and poor prognosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Jou,Y.C., Wang,S.C., Dia,Y.C., Wang,S.T., Yu,M.H., Yang,H.Y.,
            Chen,L.C., Shen,C.H. and Liu,Y.W.
  TITLE     Anti-Cancer Effects and Tumor Marker Role of Glutathione
            S-Transferase Mu 5 in Human Bladder Cancer
  JOURNAL   Int J Mol Sci 22 (6), 3056 (2021)
   PUBMED   33802702
  REMARK    GeneRIF: Anti-Cancer Effects and Tumor Marker Role of Glutathione
            S-Transferase Mu 5 in Human Bladder Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Patskovsky,Y.V., Patskovska,L.N. and Listowsky,I.
  TITLE     An asparagine-phenylalanine substitution accounts for catalytic
            differences between hGSTM3-3 and other human class mu glutathione
            S-transferases
  JOURNAL   Biochemistry 38 (49), 16187-16194 (1999)
   PUBMED   10587441
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Xu,S., Wang,Y., Roe,B. and Pearson,W.R.
  TITLE     Characterization of the human class Mu glutathione S-transferase
            gene cluster and the GSTM1 deletion
  JOURNAL   J Biol Chem 273 (6), 3517-3527 (1998)
   PUBMED   9452477
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Rowe,J.D., Nieves,E. and Listowsky,I.
  TITLE     Subunit diversity and tissue distribution of human glutathione
            S-transferases: interpretations based on electrospray ionization-MS
            and peptide sequence-specific antisera
  JOURNAL   Biochem J 325 (Pt 2) (Pt 2), 481-486 (1997)
   PUBMED   9230131
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Pearson,W.R., Vorachek,W.R., Xu,S.J., Berger,R., Hart,I.,
            Vannais,D. and Patterson,D.
  TITLE     Identification of class-mu glutathione transferase genes
            GSTM1-GSTM5 on human chromosome 1p13
  JOURNAL   Am J Hum Genet 53 (1), 220-233 (1993)
   PUBMED   8317488
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Takahashi,Y., Campbell,E.A., Hirata,Y., Takayama,T. and
            Listowsky,I.
  TITLE     A basis for differentiating among the multiple human Mu-glutathione
            S-transferases and molecular cloning of brain GSTM5
  JOURNAL   J Biol Chem 268 (12), 8893-8898 (1993)
   PUBMED   8473333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB089682.1, BC058881.1,
            AC000032.7 and BX281326.1.
            
            On Sep 17, 2002 this sequence version replaced NP_000842.1.
            
            Summary: Cytosolic and membrane-bound forms of glutathione
            S-transferase are encoded by two distinct supergene families. At
            present, eight distinct classes of the soluble cytoplasmic
            mammalian glutathione S-transferases have been identified: alpha,
            kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a
            glutathione S-transferase that belongs to the mu class. The mu
            class of enzymes functions in the detoxification of electrophilic
            compounds, including carcinogens, therapeutic drugs, environmental
            toxins and products of oxidative stress, by conjugation with
            glutathione. The genes encoding the mu class of enzymes are
            organized in a gene cluster on chromosome 1p13.3 and are known to
            be highly polymorphic. These genetic variations can change an
            individual's susceptibility to carcinogens and toxins as well as
            affect the toxicity and efficacy of certain drugs. Diversification
            of these genes has occurred in regions encoding substrate-binding
            domains, as well as in tissue expression patterns, to accommodate
            an increasing number of foreign compounds. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.68655.1,
                                           SRR3476690.576038.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256593.8/ ENSP00000256593.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..218
                     /product="glutathione S-transferase Mu 5"
                     /EC_number="2.5.1.18"
                     /note="glutathione S-transferase M5; glutathione
                     S-alkyltransferase M5; glutathione S-aryltransferase M5;
                     S-(hydroxyalkyl)glutathione lyase M5; glutathione
                     S-aralkyltransferase M5; GST class-mu 5; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=25544
     Region          3..84
                     /region_name="GST_N_Mu"
                     /note="GST_N family, Class Mu subfamily; GSTs are
                     cytosolic dimeric proteins involved in cellular
                     detoxification by catalyzing the conjugation of
                     glutathione (GSH) with a wide range of endogenous and
                     xenobiotic alkylating agents, including carcinogens;
                     cd03075"
                     /db_xref="CDD:239373"
     Site            order(7..8,46,50,59..60,72..73)
                     /site_type="other"
                     /note="GSH binding site (G-site) [chemical binding]"
                     /db_xref="CDD:239373"
     Site            order(10..12,15,18,22,25,35,74,77..78)
                     /site_type="other"
                     /note="C-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:239373"
     Site            order(56..57,68,72,78..79,82)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239373"
     Region          92..212
                     /region_name="GST_C_Mu"
                     /note="C-terminal, alpha helical domain of Class Mu
                     Glutathione S-transferases; cd03209"
                     /db_xref="CDD:198318"
     Site            order(92,94,98,102..103,106,137,141)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198318"
     Site            order(98,101,155,158..159,162,165,193,197)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198318"
     Site            order(105,108..109,112..113,116,163,166,208..210)
                     /site_type="other"
                     /note="substrate binding pocket (H-site) [chemical
                     binding]"
                     /db_xref="CDD:198318"
     CDS             1..218
                     /gene="GSTM5"
                     /gene_synonym="GSTM5-5; GTM5"
                     /coded_by="NM_000851.4:63..719"
                     /db_xref="CCDS:CCDS811.1"
                     /db_xref="GeneID:2949"
                     /db_xref="HGNC:HGNC:4637"
                     /db_xref="MIM:138385"
ORIGIN      
        1 mpmtlgywdi rglahairll leytdssyve kkytlgdapd ydrsqwlnek fklgldfpnl
       61 pylidgahki tqsnailryi arkhnlcget eeekirvdil enqvmdnhme lvrlcydpdf
      121 eklkpkylee lpeklklyse flgkrpwfag dkitfvdfla ydvldmkrif epkcldafln
      181 lkdfisrfeg lkkisaymks sqflrgllfg ksatwnsk
//
LOCUS       NP_001192391             531 aa            linear   MAM 27-APR-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily D member 2 [Bos taurus].
ACCESSION   NP_001192391 XP_001256034
VERSION     NP_001192391.1
DBSOURCE    REFSEQ: accession NM_001205462.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            NKLS02000019.1.
            
            On Apr 20, 2011 this sequence version replaced XP_001256034.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA6648753, SAMEA6648754
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="19"
                     /map="19"
                     /breed="Hereford"
     Protein         1..531
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily D member
                     2"
                     /note="60 kDa BRG-1/Brm-associated factor subunit B;
                     BRG1-associated factor 60B"
                     /calculated_mol_wt=58837
     Region          61..>148
                     /region_name="PHA03201"
                     /note="uracil DNA glycosylase; Provisional"
                     /db_xref="CDD:165468"
     Site            81
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q92925; propagated from
                     UniProtKB/Swiss-Prot (E1BJD1.1)"
     Site            104
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q92925; propagated from
                     UniProtKB/Swiss-Prot (E1BJD1.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92925; propagated from
                     UniProtKB/Swiss-Prot (E1BJD1.1)"
     Region          205..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E1BJD1.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q92925; propagated from
                     UniProtKB/Swiss-Prot (E1BJD1.1)"
     Region          307..386
                     /region_name="SWIB_BAF60B"
                     /note="SWIB domain found in BRG1-associated factor 60B
                     (BAF60B) and similar proteins; cd17675"
                     /db_xref="CDD:349494"
     Site            order(329,332..333,335..336,339..340,345,350..351,353,370,
                     373..374)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349494"
     CDS             1..531
                     /gene="SMARCD2"
                     /gene_synonym="BAF60B"
                     /coded_by="NM_001205462.3:329..1924"
                     /db_xref="BGD:BT28896"
                     /db_xref="GeneID:789613"
                     /db_xref="VGNC:VGNC:34994"
ORIGIN      
        1 msgrgaggfp lpplspggga vaaalgappp pagpgmlpgp alrgpgpagg vggpgaaafr
       61 pmgpagpaaq yqrpgmspgs rmpmaglqvg ppagspfgta aplrpgmppt mmdpfrkrll
      121 vpqaqppmpa qrrglkrrkm adkvlpqrir elvpesqaym dllaferkld qtiarkrmei
      181 qeaikkpltq krklriyisn tfspskaegd tagttgtpgg tpagdkvasw elrvegklld
      241 dpskqkrkfs sffkslviel dkelygpdnh lvewhrmptt qetdgfqvkr pgdlnvkctl
      301 llmldhqppq ykldprlarl lgvhtqtraa imqalwlyik hnqlqdgher eyincnryfr
      361 qifscgrlrf seipmklagl lqhpdpivin hvisvdpndq kktacydidv evddplkaqm
      421 snflasttnq qeiasldvki hetiesinql ktqrdfmlsf stdpqdfiqe wlrsqrrdlk
      481 iitdvignpe eerraafyhq pwaqeavgrh ifakvqqrrq eleqvlgirl t
//
LOCUS       NP_001348512             271 aa            linear   ROD 27-APR-2025
DEFINITION  reticulophagy regulator 3 isoform 3 [Mus musculus].
ACCESSION   NP_001348512 XP_006534095
VERSION     NP_001348512.1
DBSOURCE    REFSEQ: accession NM_001361583.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Iavarone,F., Zaninello,M., Perrone,M., Monaco,M., Barth,E.,
            Gaedke,F., Pizzo,M.T., Di Lorenzo,G., Desiderio,V., Sommella,E.,
            Merciai,F., Salviati,E., Campiglia,P., Luongo,L., De Leonibus,E.,
            Rugarli,E. and Settembre,C.
  TITLE     Fam134c and Fam134b shape axonal endoplasmic reticulum architecture
            in vivo
  JOURNAL   EMBO Rep 25 (8), 3651-3677 (2024)
   PUBMED   39039299
  REMARK    GeneRIF: Fam134c and Fam134b shape axonal endoplasmic reticulum
            architecture in vivo.
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Di Lorenzo,G., Iavarone,F., Maddaluno,M., Plata-Gomez,A.B.,
            Aureli,S., Quezada Meza,C.P., Cinque,L., Palma,A., Reggio,A.,
            Cirillo,C., Sacco,F., Stolz,A., Napolitano,G., Marin,O.,
            Pinna,L.A., Ruzzene,M., Limongelli,V., Efeyan,A., Grumati,P. and
            Settembre,C.
  TITLE     Phosphorylation of FAM134C by CK2 controls starvation-induced
            ER-phagy
  JOURNAL   Sci Adv 8 (35), eabo1215 (2022)
   PUBMED   36044577
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Reggio,A., Buonomo,V., Berkane,R., Bhaskara,R.M., Tellechea,M.,
            Peluso,I., Polishchuk,E., Di Lorenzo,G., Cirillo,C., Esposito,M.,
            Hussain,A., Huebner,A.K., Hubner,C.A., Settembre,C., Hummer,G.,
            Grumati,P. and Stolz,A.
  TITLE     Role of FAM134 paralogues in endoplasmic reticulum remodeling,
            ER-phagy, and Collagen quality control
  JOURNAL   EMBO Rep 22 (9), e52289 (2021)
   PUBMED   34338405
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Fu,B., Wang,L., Li,S. and Dorf,M.E.
  TITLE     ZMPSTE24 defends against influenza and other pathogenic viruses
  JOURNAL   J Exp Med 214 (4), 919-929 (2017)
   PUBMED   28246125
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Kurth,I., Pamminger,T., Hennings,J.C., Soehendra,D., Huebner,A.K.,
            Rotthier,A., Baets,J., Senderek,J., Topaloglu,H., Farrell,S.A.,
            Nurnberg,G., Nurnberg,P., De Jonghe,P., Gal,A., Kaether,C.,
            Timmerman,V. and Hubner,C.A.
  TITLE     Mutations in FAM134B, encoding a newly identified Golgi protein,
            cause severe sensory and autonomic neuropathy
  JOURNAL   Nat Genet 41 (11), 1179-1181 (2009)
   PUBMED   19838196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX255926.10.
            
            On Mar 29, 2018 this sequence version replaced XP_006534095.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660817.191839.1,
                                           SRR12282455.24339580.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 64.2 cM"
     Protein         1..271
                     /product="reticulophagy regulator 3 isoform 3"
                     /note="protein FAM134C; family with sequence similarity
                     134, member C; reticulophagy regulator 3"
                     /calculated_mol_wt=30943
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CQV4.1)"
     Region          41..232
                     /region_name="RETR3_RHD"
                     /note="N-terminal reticulon-homology domain of
                     Reticulophagy regulator 3; cd22562"
                     /db_xref="CDD:411701"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQV4.1)"
     Site            169..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQV4.1)"
     Site            193..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQV4.1)"
     Region          244..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQV4.1)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CQV4.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CQV4.1)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CQV4.1)"
     CDS             1..271
                     /gene="Retreg3"
                     /gene_synonym="1300010M03Rik; 4933404C01Rik; Fam134c"
                     /coded_by="NM_001361583.1:63..878"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:67998"
                     /db_xref="MGI:MGI:1915248"
ORIGIN      
        1 meeaegvaaa pgpasglafr grramsgswe rdqqveaaqr tlvevlgpye pllsrvqaal
       61 vwerparsal wclglnaafw ffaltslrfv fllafslmii vcidqwknki wpeinvprpd
      121 aldneswgfv hprllsvpel chhvaevwvs gtifirnlll fkkqnpgkfc llscgvltfl
      181 amlgryipgl llsylmlvii mmwplavyhr lwdrayvrlk pvlqrldfsv rgymmskqre
      241 rqlrrralhs eratdshsds eeelaafcpq t
//
LOCUS       NP_005849                692 aa            linear   PRI 27-APR-2025
DEFINITION  A-kinase anchor protein 8 [Homo sapiens].
ACCESSION   NP_005849
VERSION     NP_005849.1
DBSOURCE    REFSEQ: accession NM_005858.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Kong,X., An,P., Xu,J., Liu,W., Lin,F. and Yang,Y.
  TITLE     A-Kinase Anchor Protein 95 Is Involved in ERK1/2-Elk-1 Signal
            Transduction in Colon Cancer
  JOURNAL   Anal Cell Pathol (Amst) 2023, 8242646 (2023)
   PUBMED   36691407
  REMARK    GeneRIF: A-Kinase Anchor Protein 95 Is Involved in ERK1/2-Elk-1
            Signal Transduction in Colon Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Li,W., Hu,J., Shi,B., Palomba,F., Digman,M.A., Gratton,E. and
            Jiang,H.
  TITLE     Biophysical properties of AKAP95 protein condensates regulate
            splicing and tumorigenesis
  JOURNAL   Nat Cell Biol 22 (8), 960-972 (2020)
   PUBMED   32719551
  REMARK    GeneRIF: Biophysical properties of AKAP95 protein condensates
            regulate splicing and tumorigenesis.
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Zuo,H., Trombetta-Lima,M., Heijink,I.H., van der Veen,C.H.T.J.,
            Hesse,L., Faber,K.N., Poppinga,W.J., Maarsingh,H., Nikolaev,V.O.
            and Schmidt,A.M.
  TITLE     A-Kinase Anchoring Proteins Diminish TGF-beta1/Cigarette
            Smoke-Induced Epithelial-To-Mesenchymal Transition
  JOURNAL   Cells 9 (2), 356 (2020)
   PUBMED   32028718
  REMARK    GeneRIF: A-Kinase Anchoring Proteins Diminish TGF-beta1/Cigarette
            Smoke-Induced Epithelial-To-Mesenchymal Transition.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Hu,X., Harvey,S.E., Zheng,R., Lyu,J., Grzeskowiak,C.L., Powell,E.,
            Piwnica-Worms,H., Scott,K.L. and Cheng,C.
  TITLE     The RNA-binding protein AKAP8 suppresses tumor metastasis by
            antagonizing EMT-associated alternative splicing
  JOURNAL   Nat Commun 11 (1), 486 (2020)
   PUBMED   31980632
  REMARK    GeneRIF: Identification of A-Kinase Anchor Protein (AKAP8) as a
            splicing regulatory factor that impedes EMT and breast cancer
            metastasis. AKAP8 not only is capable of inhibiting splicing
            activity of the EMT-promoting splicing regulator hnRNPM through
            protein-protein interaction, it also directly binds to RNA and
            alters splicing outcomes. Genome-wide analysis shows that AKAP8
            promotes an epithelial cell state splicing program.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Akileswaran,L., Taraska,J.W., Sayer,J.A., Gettemy,J.M. and
            Coghlan,V.M.
  TITLE     A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix
            and associates with p68 RNA helicase
  JOURNAL   J Biol Chem 276 (20), 17448-17454 (2001)
   PUBMED   11279182
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Steen,R.L., Cubizolles,F., Le Guellec,K. and Collas,P.
  TITLE     A kinase-anchoring protein (AKAP)95 recruits human
            chromosome-associated protein (hCAP)-D2/Eg7 for chromosome
            condensation in mitotic extract
  JOURNAL   J Cell Biol 149 (3), 531-536 (2000)
   PUBMED   10791967
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Collas,P., Le Guellec,K. and Tasken,K.
  TITLE     The A-kinase-anchoring protein AKAP95 is a multivalent protein with
            a key role in chromatin condensation at mitosis
  JOURNAL   J Cell Biol 147 (6), 1167-1180 (1999)
   PUBMED   10601332
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Eide,T., Coghlan,V., Orstavik,S., Holsve,C., Solberg,R.,
            Skalhegg,B.S., Lamb,N.J., Langeberg,L., Fernandez,A., Scott,J.D.,
            Jahnsen,T. and Tasken,K.
  TITLE     Molecular cloning, chromosomal localization, and cell
            cycle-dependent subcellular distribution of the A-kinase anchoring
            protein, AKAP95
  JOURNAL   Exp Cell Res 238 (2), 305-316 (1998)
   PUBMED   9473338
REFERENCE   10 (residues 1 to 692)
  AUTHORS   Lester,L.B. and Scott,J.D.
  TITLE     Anchoring and scaffold proteins for kinases and phosphatases
  JOURNAL   Recent Prog Horm Res 52, 409-29 (1997)
   PUBMED   9238861
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y11997.1, CA429585.1,
            AI581319.1 and AC093060.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the A-kinase anchor protein
            family. A-kinase anchor proteins are scaffold proteins that contain
            a binding domain for the RI/RII subunit of protein kinase A (PKA)
            and recruit PKA and other signaling molecules to specific
            subcellular locations. This gene encodes a nuclear A-kinase anchor
            protein that binds to the RII alpha subunit of PKA and may play a
            role in chromosome condensation during mitosis by targeting PKA and
            the condensin complex to chromatin. A pseudogene of this gene is
            located on the short arm of chromosome 9. [provided by RefSeq, May
            2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.161666.1,
                                           SRR1803614.116134.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269701.7/ ENSP00000269701.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..692
                     /product="A-kinase anchor protein 8"
                     /note="A-kinase anchor protein, 95kDa; A kinase (PRKA)
                     anchor protein 8"
                     /calculated_mol_wt=75977
     Region          1..210
                     /region_name="Interaction with DPY30.
                     /evidence=ECO:0000269|PubMed:23995757"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Region          1..195
                     /region_name="Interaction with MCM2.
                     /evidence=ECO:0000269|PubMed:12740381"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Region          109..201
                     /region_name="Interaction with DDX5.
                     /evidence=ECO:0000250|UniProtKB:Q63014"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Site            109
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR0;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR0; propagated from
                     UniProtKB/Swiss-Prot (O43823.1)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O43823.1)"
     Region          168..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43823.1)"
     Region          231..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Site            233
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR0; propagated from
                     UniProtKB/Swiss-Prot (O43823.1)"
     Region          269..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Site            277
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O43823.1)"
     Region          289..306
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q63014,
                     ECO:0000305|PubMed:16227597"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43823.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Region          387..450
                     /region_name="Involved in chromatin-binding.
                     /evidence=ECO:0000269|PubMed:11964380"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Region          415..546
                     /region_name="AKAP95"
                     /note="A-kinase anchoring protein 95 (AKAP95); pfam04988"
                     /db_xref="CDD:461509"
     Region          525..569
                     /region_name="Involved in condensin complex recruitment.
                     /evidence=ECO:0000269|PubMed:11964380"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Region          545..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Region          <556..664
                     /region_name="LGT"
                     /note="Prolipoprotein diacylglyceryl transferase; cl00478"
                     /db_xref="CDD:469786"
     Region          572..589
                     /region_name="RII-binding.
                     /evidence=ECO:0000250|UniProtKB:Q63014"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Region          576..593
                     /region_name="Required for interaction with MYCBP.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR0"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Region          592..692
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43823.1)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63014; propagated from
                     UniProtKB/Swiss-Prot (O43823.1)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43823.1)"
     CDS             1..692
                     /gene="AKAP8"
                     /gene_synonym="AKAP 95; AKAP-8; AKAP-95; AKAP95"
                     /coded_by="NM_005858.4:57..2135"
                     /db_xref="CCDS:CCDS12329.1"
                     /db_xref="GeneID:10270"
                     /db_xref="HGNC:HGNC:378"
                     /db_xref="MIM:604692"
ORIGIN      
        1 mdqgyggyga wsagpantqg aygtgvaswq gyenynyyga qntsvttgat ysygpaswea
       61 akandgglaa gapamhmasy gpepctdnsd sliakinqrl dmmskeggrg gsggggegiq
      121 dressfrfqp fesydsrpcl pehnpyrpsy sydyefdlgs drngsfggqy secrdparer
      181 gsldgfmrgr gqgrfqdrsn pgtfmrsdpf vppaassepl stpwnelnyv ggrglggpsp
      241 srpppslfsq smapdygvmg mqgaggydst mpygcgrsqp rmrdrdrpkr rgfdrfgpdg
      301 tgrkrkqfql yeepdtklar vdsegdfsen ddaagdfrsg deefkgedel cdsgrqrgek
      361 edededvkkr rekqrrrdrt rdraadriqf acsvckfrsf ddeeiqkhlq skfhketlrf
      421 istklpdktv eflqeyivnr nkkiekrrqe lmeketakpk pdpfkgigqe hffkkieaah
      481 clacdmlipa qpqllqrhlh svdhnhnrrl aaeqfkktsl hvaksvlnnr hivkmlekyl
      541 kgedpftset vdpemegddn lggedkketp eevaadvlae vitaavravd gegapapess
      601 gepaedegpt dtaeagsdpq aeqlleeqvp cgtahekgvp karseaaeag ngaetmaaea
      661 esaqtrvapa paaadaeveq tdaeskdavp te
//
LOCUS       NP_004635               1082 aa            linear   PRI 27-APR-2025
DEFINITION  AP-3 complex subunit beta-2 isoform 2 [Homo sapiens].
ACCESSION   NP_004635
VERSION     NP_004635.2
DBSOURCE    REFSEQ: accession NM_004644.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Dilber,C., Yucel,G. and Sahin,Y.
  TITLE     Novel homozygous AP3B2 mutations in four individuals with
            developmental and epileptic encephalopathy: A rare clinical entity
  JOURNAL   Clin Neurol Neurosurg 223, 107509 (2022)
   PUBMED   36356440
  REMARK    GeneRIF: Novel homozygous AP3B2 mutations in four individuals with
            developmental and epileptic encephalopathy: A rare clinical entity.
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Yang,F., Jing,F., Li,Y., Kong,S., Zhang,S., Huo,Y., Huang,X. and
            Yu,S.
  TITLE     Plasma lncRNA LOC338963 and mRNA AP3B2 are upregulated in
            paraneoplastic Lambert-Eaton myasthenic syndrome
  JOURNAL   Muscle Nerve 66 (2), 216-222 (2022)
   PUBMED   35508598
  REMARK    GeneRIF: Plasma lncRNA LOC338963 and mRNA AP3B2 are upregulated in
            paraneoplastic Lambert-Eaton myasthenic syndrome.
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Ueda,K., Ogawa,S., Matsuda,K., Hasegawa,Y., Nishi,E., Yanagi,K.,
            Kaname,T., Yamamoto,T. and Okamoto,N.
  TITLE     Blended phenotype of combination of HERC2 and AP3B2 deficiency and
            Angelman syndrome caused by paternal isodisomy of chromosome 15
  JOURNAL   Am J Med Genet A 185 (10), 3092-3098 (2021)
   PUBMED   34042275
  REMARK    GeneRIF: Blended phenotype of combination of HERC2 and AP3B2
            deficiency and Angelman syndrome caused by paternal isodisomy of
            chromosome 15.
REFERENCE   4  (residues 1 to 1082)
  AUTHORS   Honorat,J.A., Lopez-Chiriboga,A.S., Kryzer,T.J., Komorowski,L.,
            Scharf,M., Hinson,S.R., Lennon,V.A., Pittock,S.J., Klein,C.J. and
            McKeon,A.
  TITLE     Autoimmune gait disturbance accompanying adaptor protein-3B2-IgG
  JOURNAL   Neurology 93 (10), e954-e963 (2019)
   PUBMED   31371564
  REMARK    GeneRIF: The AP3B2 antigen was identified in sera and cerebrospinal
            fluid of patients with sensory or cerebellar ataxia.
            Erratum:[Neurology. 2019 Oct 1;93(14):647. doi:
            10.1212/WNL.0000000000008232. PMID: 31467253]
REFERENCE   5  (residues 1 to 1082)
  AUTHORS   Assoum,M., Philippe,C., Isidor,B., Perrin,L., Makrythanasis,P.,
            Sondheimer,N., Paris,C., Douglas,J., Lesca,G., Antonarakis,S.,
            Hamamy,H., Jouan,T., Duffourd,Y., Auvin,S., Saunier,A., Begtrup,A.,
            Nowak,C., Chatron,N., Ville,D., Mireskandari,K., Milani,P.,
            Jonveaux,P., Lemeur,G., Milh,M., Amamoto,M., Kato,M., Nakashima,M.,
            Miyake,N., Matsumoto,N., Masri,A., Thauvin-Robinet,C.,
            Riviere,J.B., Faivre,L. and Thevenon,J.
  TITLE     Autosomal-Recessive Mutations in AP3B2, Adaptor-Related Protein
            Complex 3 Beta 2 Subunit, Cause an Early-Onset Epileptic
            Encephalopathy with Optic Atrophy
  JOURNAL   Am J Hum Genet 99 (6), 1368-1376 (2016)
   PUBMED   27889060
  REMARK    GeneRIF: Autosomal-Recessive Mutations in AP3B2, Adaptor-Related
            Protein Complex 3 Beta 2 Subunit, Cause an Early-Onset Epileptic
            Encephalopathy with Optic Atrophy.
REFERENCE   6  (residues 1 to 1082)
  AUTHORS   Dell'Angelica,E.C., Klumperman,J., Stoorvogel,W. and
            Bonifacino,J.S.
  TITLE     Association of the AP-3 adaptor complex with clathrin
  JOURNAL   Science 280 (5362), 431-434 (1998)
   PUBMED   9545220
REFERENCE   7  (residues 1 to 1082)
  AUTHORS   Simpson,F., Peden,A.A., Christopoulou,L. and Robinson,M.S.
  TITLE     Characterization of the adaptor-related protein complex, AP-3
  JOURNAL   J Cell Biol 137 (4), 835-845 (1997)
   PUBMED   9151686
REFERENCE   8  (residues 1 to 1082)
  AUTHORS   Dell'Angelica,E.C., Ohno,H., Ooi,C.E., Rabinovich,E., Roche,K.W.
            and Bonifacino,J.S.
  TITLE     AP-3: an adaptor-like protein complex with ubiquitous expression
  JOURNAL   EMBO J 16 (5), 917-928 (1997)
   PUBMED   9118953
REFERENCE   9  (residues 1 to 1082)
  AUTHORS   Newman,L.S., McKeever,M.O., Okano,H.J. and Darnell,R.B.
  TITLE     Beta-NAP, a cerebellar degeneration antigen, is a neuron-specific
            vesicle coat protein
  JOURNAL   Cell 82 (5), 773-783 (1995)
   PUBMED   7671305
REFERENCE   10 (residues 1 to 1082)
  AUTHORS   Darnell,R.B., Furneaux,H.M. and Posner,J.B.
  TITLE     Antiserum from a patient with cerebellar degeneration identifies a
            novel protein in Purkinje cells, cortical neurons, and
            neuroectodermal tumors
  JOURNAL   J Neurosci 11 (5), 1224-1230 (1991)
   PUBMED   1851215
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ777385.1, BC093739.1 and
            AF022152.1.
            
            On Sep 5, 2003 this sequence version replaced NP_004635.1.
            
            Summary: Adaptor protein complex 3 (AP-3 complex) is a
            heterotrimeric protein complex involved in the formation of
            clathrin-coated synaptic vesicles. The protein encoded by this gene
            represents the beta subunit of the neuron-specific AP-3 complex and
            was first identified as the target antigen in human paraneoplastic
            neurologic disorders. The encoded subunit binds clathrin and is
            phosphorylated by a casein kinase-like protein, which mediates
            synaptic vesicle coat assembly. Defects in this gene are a cause of
            early-onset epileptic encephalopathy. [provided by RefSeq, Feb
            2017].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF022152.1, BC093739.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..1082
                     /product="AP-3 complex subunit beta-2 isoform 2"
                     /note="Neuronal adaptin-like protein, beta-subunit; AP-3
                     complex subunit beta-2; beta-3B-adaptin; adaptor protein
                     complex AP-3 subunit beta-2; neuron-specific vesicle coat
                     protein beta-NAP; clathrin assembly protein complex 3
                     beta-2 large chain; adaptor related protein complex 3 beta
                     2 subunit"
                     /calculated_mol_wt=118929
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13367.2)"
     Region          34..590
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          111..139
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          145..173
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          182..208
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          272..295
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13367.2)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13367.2)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JME5; propagated from
                     UniProtKB/Swiss-Prot (Q13367.2)"
     Region          666..802
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13367.2)"
     Region          803..947
                     /region_name="AP3B1_C"
                     /note="Clathrin-adaptor complex-3 beta-1 subunit
                     C-terminal; pfam14796"
                     /db_xref="CDD:464319"
     CDS             1..1082
                     /gene="AP3B2"
                     /gene_synonym="DEE48; EIEE48; NAPTB"
                     /coded_by="NM_004644.5:170..3418"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45331.1"
                     /db_xref="GeneID:8120"
                     /db_xref="HGNC:HGNC:567"
                     /db_xref="MIM:602166"
ORIGIN      
        1 msaapaysed kggsagpgep eyghdpasgg ifssdykrhd dlkemldtnk dslkleamkr
       61 ivamiargkn asdlfpavvk nvacknievk klvyvylvry aeeqqdlall sistfqrglk
      121 dpnqlirasa lrvlssirvp iivpimmlai keaasdmspy vrktaahaip klysldsdqk
      181 dqlieviekl ladkttlvag svvmafeevc peridlihkn yrklcnllid veewgqvvii
      241 smltryartq flsptqnesl leenaekafy gseedeakga gseetaaaaa psrkpyvmdp
      301 dhrlllrntk pllqsrsaav vmavaqlyfh lapkaevgvi akalvrllrs hsevqyvvlq
      361 nvatmsikrr gmfepylksf yirstdptqi kilklevltn lanetniptv lrefqtyirs
      421 mdkdfvaati qaigrcatni grvrdtclng lvqllsnrde lvvaesvvvi kkllqmqpaq
      481 hgeiikhlak ltdniqvpma rasilwlige ycehvpriap dvlrkmaksf taeedivklq
      541 vinlaaklyl tnskqtkllt qyvlslakyd qnydirdrar ftrqlivpse qggalsrhak
      601 klflapkpap vlessfkdrd hfqlgslshl lnakatgyqe lpdwpeeapd psvrnvevpe
      661 wtkcsnrekr kekekpfysd segesgptes adsdpesese sdsksssesg sgesssesdn
      721 edqdedeekg rgseseqsee dgkrktkkkv perkgeasss degsdsssss sesemtsese
      781 eeqlepasws rktppssksa patkeislld ledftppsvq pvsppaivst slaadleglt
      841 ltdstlvpsl lspvsgvgrq ellhrvageg lavdytfsrq pfsgdphmvs vhihfsnssd
      901 tpikglhvgt pklpagisiq efpeieslap gesatavmgi nfcdstqaan fqlctqtrqf
      961 yvsiqppvge lmapvfmsen efkkeqgklm gmneiteklm lpdtcrsdhi vvqkvtatan
     1021 lgrvpcgtsd eyrfagrtlt ggslvlltld arpagaaqlt vnsekmvigt mlvkdviqal
     1081 tq
//
LOCUS       NP_001347767            2272 aa            linear   ROD 27-APR-2025
DEFINITION  protein TASOR 2 isoform 2 [Mus musculus].
ACCESSION   NP_001347767 XP_006516525
VERSION     NP_001347767.1
DBSOURCE    REFSEQ: accession NM_001360838.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 2272)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 2272)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2272)
  AUTHORS   Antony,C., Huchet,M., Changeux,J.P. and Cartaud,J.
  TITLE     Developmental regulation of membrane traffic organization during
            synaptogenesis in mouse diaphragm muscle
  JOURNAL   J Cell Biol 130 (4), 959-968 (1995)
   PUBMED   7642711
REFERENCE   4  (residues 1 to 2272)
  AUTHORS   Janoueix-Lerosey,I., Jollivet,F., Camonis,J., Marche,P.N. and
            Goud,B.
  TITLE     Two-hybrid system screen with the small GTP-binding protein Rab6.
            Identification of a novel mouse GDP dissociation inhibitor isoform
            and two other potential partners of Rab6
  JOURNAL   J Biol Chem 270 (24), 14801-14808 (1995)
   PUBMED   7782346
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC129597.5.
            
            On Feb 15, 2018 this sequence version replaced XP_006516525.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2272
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 1.99 cM"
     Protein         1..2272
                     /product="protein TASOR 2 isoform 2"
                     /note="PBR associated protein; protein TASOR 2;
                     peripherial benzodiazepine receptor associated protein;
                     peripheral benzodiazepine receptor-associated protein 20;
                     protein FAM208B; family with sequence similarity 208,
                     member B"
                     /calculated_mol_wt=251824
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VWN6; propagated from
                     UniProtKB/Swiss-Prot (Q5DTT3.2)"
     Region          94..167
                     /region_name="DUF3699"
                     /note="Protein of unknown function (DUF3699); pfam12480"
                     /db_xref="CDD:463601"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VWN6; propagated from
                     UniProtKB/Swiss-Prot (Q5DTT3.2)"
     Region          320..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5DTT3.2)"
     Region          412..478
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5DTT3.2)"
     Region          547..699
                     /region_name="DUF3715"
                     /note="Protein of unknown function (DUF3715); pfam12509"
                     /db_xref="CDD:463613"
     Region          620..639
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5DTT3.2)"
     CDS             1..2272
                     /gene="Tasor2"
                     /gene_synonym="Fam208b; mKIAA2006; Pap20"
                     /coded_by="NM_001360838.1:561..7379"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:105203"
                     /db_xref="MGI:MGI:2145274"
ORIGIN      
        1 maaptskiil elnknalisp wkgqfiiqgc llcditlwst ygtvvplqlp reldfkyvmd
       61 vsslkeslpe aafrrrsyle qkvccqdlcf dlyeveltnk qgenidklme yvknkelali
      121 kcledksffi lftssaltpe pgfgaeqmgl hglhlfhapq tagakdlkve dgislkvipi
      181 lpalsyalle akkslseegi ppnilvkhsf qelykvdksl slmappqdgv edtastgkls
      241 hafdlppple tcpseslthl kcyfsdpagy tldlsaaldl laehpqfpci adgvcdagfs
      301 lvmtpdpefl dsemeirkte taeksgrklk vkkkavtpss nqrvqpkrka sttavtlpsk
      361 rvslgrptsk rtvprtdnrs cnptlklvkg qfpqkrkrga evlaaqivqk trlerkkqea
      421 svskdapvpt ntkrakkqek spgriasqpk ppmkkspqkr kvnvargrrn trkqlqpaek
      481 eialhlqsei ssdgqkdgln lstsqqesis mipkgppens viscdsqaln mladlalssa
      541 aasipsckpr nlpcvsdlpr nnvlltkenp llgasdheyh kgvksqkavl lpkpysdeki
      601 ssesdltrsq eenlvpcaqp lpiaqpaphs earelsdasq nsvvvehsya lllaeqsqkh
      661 lhqrklpspa fvkngikgpe agtpvgkvmp frhlqntspl qkhsedslmk hkslfvsstl
      721 keffcshtvl kcdgsfkitf kcegeyvfsl dskytsnple ktvlralhgp wntdlpenvd
      781 dvklllhiwv alfysknnkv igsprkvtgg ktkqelsnkl etsnvvlsgv vsaqshgtci
      841 psedktcqst kmvsyndsvt qatlttayde asselmcqks vfdnlenkvd sfhpsplikt
      901 davqdviqhs shinnecqps vekrednvec mmvnldpvtl afeknasvpi htevhttdkp
      961 tgfnielvkr vspassvqyp msaleevqtq ssrdvpslam seykdskcls assvkketpp
     1021 eslcllqkei ppltssadeg limealslvk sssyslasdk tkcpqddslq tqnglsmsld
     1081 evlepskvnv vsstsvtlre qpspncipam sdvagastvi mnsgssslnq ekilqtfslv
     1141 fpkqtdlslk reevsmelsg eeadinltlt ispptspsee iaageieqfq ktpvsnvgqq
     1201 srseemvepe eeerlirnre insascmsvy pvesrellkn ctpevtekvn vtldfpfgpl
     1261 ievspasspd pivqpgdrps spcclklhss qsektnkfsq iksgevtipe keslflgpes
     1321 pkgqdklaev qvqisaemlq ittnaevegr vnmpgkvtkv svpsehsenl sflekvqcnt
     1381 elnelslpak yggnfkplek sgnsleagcm enrnvdvkhl alessvpscs prkvvenksl
     1441 tdtlvsitts givnmslkqt ssknikknvc dsdvktdsdv kteadsnmqt eavnsalidk
     1501 tdvqayshpe vskfvsssds aqctyhakpv svepgfqtqe ipvvrmasll knigvelhee
     1561 kmdlsatglq snsmsakdeq ktmhvlqdti cevkeflngd vfsqnahscq ntvdfsksis
     1621 eepsasfvpe fvdaicgvyk ehtfnespnm vhetkadaet lsrnteisvn asmfcgprsg
     1681 ayvqdshdck sckfdvenlr gnhesqkdav kdscdsftsl nnsddtwacs skistlethi
     1741 pprdqetepr lispnkcipr yiqipdshgi pktyanftit kefkdttrrl hslkrhrnls
     1801 ancnllsswt stwhvtddlt qhtldleylr fdhklkqikk ggsqqssfpk eslvqissgt
     1861 spstqtseas glhlppesrs pilvtvvrad trqqshhrrg cspssldgss sfwkkkcsqs
     1921 rnlknsersq tvpfhlnklk ynstlkesrn dislilneya efnkimmnsk qivsqdeeln
     1981 vasaeavfqe ayqprqpvsy edvitdlcat lhvklkgvvr eackspfwfy lvetedksfl
     2041 lrtksilkkg ghieielldf cqafhrenet llviiknedi ishlhqipsl lklkhfpsvv
     2101 fagvdspedi vnetyqelfr sggfvvsddv ilesltlvql keilkilekl nengkwkwll
     2161 hyresknlke dvrvdsiahk knlilksyqs vniidllhyh ncdspsstka eifkcllnlq
     2221 iqhisarfav fltdkptvst eifenngilv tdvnyfteni qkiaapfrss yw
//
LOCUS       NP_001938                419 aa            linear   PRI 27-APR-2025
DEFINITION  dual specificity protein phosphatase 7 [Homo sapiens].
ACCESSION   NP_001938 XP_037430
VERSION     NP_001938.2
DBSOURCE    REFSEQ: accession NM_001947.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Li,L., Wang,N., Xiong,Y., Guo,G., Zhu,M. and Gu,Y.
  TITLE     Transcription Factor FOSL1 Enhances Drug Resistance of Breast
            Cancer through DUSP7-Mediated Dephosphorylation of PEA15
  JOURNAL   Mol Cancer Res 20 (4), 515-526 (2022)
   PUBMED   34907034
  REMARK    GeneRIF: Transcription Factor FOSL1 Enhances Drug Resistance of
            Breast Cancer through DUSP7-Mediated Dephosphorylation of PEA15.
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Bai,H., Song,M., Jiao,R., Li,W., Zhao,J., Xiao,M., Jin,M., Zhang,Z.
            and Deng,H.
  TITLE     DUSP7 inhibits cervical cancer progression by inactivating the RAS
            pathway
  JOURNAL   J Cell Mol Med 25 (19), 9306-9318 (2021)
   PUBMED   34435746
  REMARK    GeneRIF: DUSP7 inhibits cervical cancer progression by inactivating
            the RAS pathway.
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Guo,X., Ramirez,I., Garcia,Y.A., Velasquez,E.F., Gholkar,A.A.,
            Cohn,W., Whitelegge,J.P., Tofig,B., Damoiseaux,R. and Torres,J.Z.
  TITLE     DUSP7 regulates the activity of ERK2 to promote proper chromosome
            alignment during cell division
  JOURNAL   J Biol Chem 296, 100676 (2021)
   PUBMED   33865857
  REMARK    GeneRIF: DUSP7 regulates the activity of ERK2 to promote proper
            chromosome alignment during cell division.
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Pasquali,C., Curchod,M.L., Walchli,S., Espanel,X., Guerrier,M.,
            Arigoni,F., Strous,G. and Hooft van Huijsduijnen,R.
  TITLE     Identification of protein tyrosine phosphatases with specificity
            for the ligand-activated growth hormone receptor
  JOURNAL   Mol Endocrinol 17 (11), 2228-2239 (2003)
   PUBMED   12907755
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Dowd,S., Sneddon,A.A. and Keyse,S.M.
  TITLE     Isolation of the human genes encoding the pyst1 and Pyst2
            phosphatases: characterisation of Pyst2 as a cytosolic
            dual-specificity MAP kinase phosphatase and its catalytic
            activation by both MAP and SAP kinases
  JOURNAL   J Cell Sci 111 (Pt 22), 3389-3399 (1998)
   PUBMED   9788880
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Smith,A., Price,C., Cullen,M., Muda,M., King,A., Ozanne,B.,
            Arkinstall,S. and Ashworth,A.
  TITLE     Chromosomal localization of three human dual specificity
            phosphatase genes (DUSP4, DUSP6, and DUSP7)
  JOURNAL   Genomics 42 (3), 524-527 (1997)
   PUBMED   9205128
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Groom,L.A., Sneddon,A.A., Alessi,D.R., Dowd,S. and Keyse,S.M.
  TITLE     Differential regulation of the MAP, SAP and RK/p38 kinases by
            Pyst1, a novel cytosolic dual-specificity phosphatase
  JOURNAL   EMBO J 15 (14), 3621-3632 (1996)
   PUBMED   8670865
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Muda,M., Boschert,U., Dickinson,R., Martinou,J.C., Martinou,I.,
            Camps,M., Schlegel,W. and Arkinstall,S.
  TITLE     MKP-3, a novel cytosolic protein-tyrosine phosphatase that
            exemplifies a new class of mitogen-activated protein kinase
            phosphatase
  JOURNAL   J Biol Chem 271 (8), 4319-4326 (1996)
   PUBMED   8626780
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC115284.4, DN999200.1, BC019107.2, X93921.1, CN429806.1 and
            AL110157.1.
            
            On May 27, 2009 this sequence version replaced NP_001938.1.
            
            Summary: Dual-specificity phosphatases (DUSPs) constitute a large
            heterogeneous subgroup of the type I cysteine-based
            protein-tyrosine phosphatase superfamily. DUSPs are characterized
            by their ability to dephosphorylate both tyrosine and
            serine/threonine residues. DUSP7 belongs to a class of DUSPs,
            designated MKPs, that dephosphorylate MAPK (mitogen-activated
            protein kinase) proteins ERK (see MIM 601795), JNK (see MIM
            601158), and p38 (see MIM 600289) with specificity distinct from
            that of individual MKP proteins. MKPs contain a highly conserved
            C-terminal catalytic domain and an N-terminal Cdc25 (see MIM
            116947)-like (CH2) domain. MAPK activation cascades mediate various
            physiologic processes, including cellular proliferation, apoptosis,
            differentiation, and stress responses (summary by Patterson et al.,
            2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.9560.1,
                                           SRR1660805.169034.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674, SAMN03568911
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000495880.2/ ENSP00000417183.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..419
                     /product="dual specificity protein phosphatase 7"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="dual specificity protein phosphatase PYST2"
                     /calculated_mol_wt=44826
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16829.4)"
     Region          55..186
                     /region_name="DSP_MapKP"
                     /note="N-terminal regulatory rhodanese domain of dual
                     specificity phosphatases (DSP), such as Mapk Phosphatase.
                     This domain is believed to determine substrate specificity
                     by binding the substrate, such as ERK2, and activating the
                     C-terminal catalytic domain by...; cd01446"
                     /db_xref="CDD:238723"
     Site            101..103
                     /site_type="active"
                     /note="putative substrate binding residues [active]"
                     /db_xref="CDD:238723"
     Region          216..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16829.4)"
     Region          240..388
                     /region_name="DSP_DUSP7"
                     /note="dual specificity phosphatase domain of dual
                     specificity protein phosphatase 7; cd14643"
                     /db_xref="CDD:350491"
     CDS             1..419
                     /gene="DUSP7"
                     /gene_synonym="MKPX; PYST2"
                     /coded_by="NM_001947.4:206..1465"
                     /db_xref="CCDS:CCDS33766.2"
                     /db_xref="GeneID:1849"
                     /db_xref="HGNC:HGNC:3073"
                     /db_xref="MIM:602749"
ORIGIN      
        1 mknqlrgppa rahmstsgaa aaggtragse pgagsgsgag tgagaatgag ampcksaewl
       61 qeeleargga slllldcrph elfesshiet ainlaipglm lrrlrkgnlp irsiipnhad
      121 kerfatrcka atvllydeat aewqpepgap asvlglllqk lrddgcqayy lqggfnkfqt
      181 eysehcetnv dsssspsssp ptsvlglggl rissdcsdge sdrelpssat esdgspvpss
      241 qpafpvqilp ylylgcakds tnldvlgkyg ikyilnvtpn lpnafehgge ftykqipisd
      301 hwsqnlsqff peaisfidea rskkcgvlvh clagisrsvt vtvaylmqkm nlslndaydf
      361 vkrkksnisp nfnfmgqlld fertlglssp cdnhasseql yfstptnhnl fplntlest
//
LOCUS       NP_001348930              88 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 1 [Mus musculus].
ACCESSION   NP_001348930
VERSION     NP_001348930.1
DBSOURCE    REFSEQ: accession NM_001362001.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 88)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 88)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 88)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 88)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7.
            
            Transcript Variant: This variant (11), as well as variants 1, 8-10,
            and 12-19, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660825.8108.1,
                                           SRR1660811.57406.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..88
                     /product="cAMP-regulated phosphoprotein 21 isoform 1"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=9408
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q7M2N1; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10854908,
                     ECO:0000269|PubMed:15499021; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     CDS             1..88
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362001.1:434..700"
                     /note="isoform 1 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS40786.1"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqtl
//
LOCUS       NP_061824                410 aa            linear   PRI 27-APR-2025
DEFINITION  homeobox protein Hox-A10 [Homo sapiens].
ACCESSION   NP_061824
VERSION     NP_061824.3
DBSOURCE    REFSEQ: accession NM_018951.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Zhou,H., Deng,C. and Xi,Y.
  TITLE     Mechanism of HOXA10 in nasopharyngeal carcinoma cell proliferation
            through the PTPRG-AS1/USP1 axis
  JOURNAL   J Biochem Mol Toxicol 38 (11), e70025 (2024)
   PUBMED   39445487
  REMARK    GeneRIF: Mechanism of HOXA10 in nasopharyngeal carcinoma cell
            proliferation through the PTPRG-AS1/USP1 axis.
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhong,M., Xu,W., Tian,P., Zhang,Q., Wang,Z., Liang,L., Zhang,Q.,
            Yang,Y., Lu,Y. and Wei,G.H.
  TITLE     An Inherited Allele Confers Prostate Cancer Progression and Drug
            Resistance via RFX6/HOXA10-Orchestrated TGFbeta Signaling
  JOURNAL   Adv Sci (Weinh) 11 (32), e2401492 (2024)
   PUBMED   38932472
  REMARK    GeneRIF: An Inherited Allele Confers Prostate Cancer Progression
            and Drug Resistance via RFX6/HOXA10-Orchestrated TGFbeta Signaling.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Zhao,K., Chen,L., Xie,Y., Ren,N., Li,J., Zhai,X., Zheng,S., Liu,K.,
            Wang,C., Qiu,Q., Peng,X., Wang,W., Liu,J., Che,Q., Fan,J., Hu,H.
            and Liu,M.
  TITLE     m6A/HOXA10-AS/ITGA6 axis aggravates oxidative resistance and
            malignant progression of laryngeal squamous cell carcinoma through
            regulating Notch and Keap1/Nrf2 pathways
  JOURNAL   Cancer Lett 587, 216735 (2024)
   PUBMED   38369001
  REMARK    GeneRIF: m6A/HOXA10-AS/ITGA6 axis aggravates oxidative resistance
            and malignant progression of laryngeal squamous cell carcinoma
            through regulating Notch and Keap1/Nrf2 pathways.
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Chen,S. and Pan,J.
  TITLE     Importin 7 enhances protective autophagy induced by nuclear
            translocation of homeobox A10 in oral squamous cell carcinoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (3), 241-247 (2024)
   PUBMED   38650127
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Huang,Y., Tao,M., Yan,S. and He,X.
  TITLE     Long non-coding RNA Homeobox D gene cluster antisense
            growth-associated long noncoding RNA/microRNA-182-5p/Homeobox
            protein A10 alleviates postmenopausal osteoporosis via accelerating
            osteoblast differentiation of bone marrow mesenchymal stem cells
  JOURNAL   J Orthop Surg Res 18 (1), 726 (2023)
   PUBMED   37752532
  REMARK    GeneRIF: Long non-coding RNA Homeobox D gene cluster antisense
            growth-associated long noncoding RNA/microRNA-182-5p/Homeobox
            protein A10 alleviates postmenopausal osteoporosis via accelerating
            osteoblast differentiation of bone marrow mesenchymal stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Scott,M.P.
  TITLE     Vertebrate homeobox gene nomenclature
  JOURNAL   Cell 71 (4), 551-553 (1992)
   PUBMED   1358459
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Lowney,P., Corral,J., Detmer,K., LeBeau,M.M., Deaven,L.,
            Lawrence,H.J. and Largman,C.
  TITLE     A human Hox 1 homeobox gene exhibits myeloid-specific expression of
            alternative transcripts in human hematopoietic cells
  JOURNAL   Nucleic Acids Res 19 (12), 3443-3449 (1991)
   PUBMED   1676505
REFERENCE   8  (residues 1 to 410)
  AUTHORS   McAlpine,P.J. and Shows,T.B.
  TITLE     Nomenclature for human homeobox genes
  JOURNAL   Genomics 7 (3), 460 (1990)
   PUBMED   1973146
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Acampora,D., D'Esposito,M., Faiella,A., Pannese,M., Migliaccio,E.,
            Morelli,F., Stornaiuolo,A., Nigro,V., Simeone,A. and Boncinelli,E.
  TITLE     The human HOX gene family
  JOURNAL   Nucleic Acids Res 17 (24), 10385-10402 (1989)
   PUBMED   2574852
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Shen,W.F., Largman,C., Lowney,P., Corral,J.C., Detmer,K.,
            Hauser,C.A., Simonitch,T.A., Hack,F.M. and Lawrence,H.J.
  TITLE     Lineage-restricted expression of homeobox-containing genes in human
            hematopoietic cell lines
  JOURNAL   Proc Natl Acad Sci U S A 86 (21), 8536-8540 (1989)
   PUBMED   2573064
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX439708.2, BC013971.2 and
            BF196481.1.
            
            On Apr 12, 2008 this sequence version replaced NP_061824.2.
            
            Summary: In vertebrates, the genes encoding the class of
            transcription factors called homeobox genes are found in clusters
            named A, B, C, and D on four separate chromosomes. Expression of
            these proteins is spatially and temporally regulated during
            embryonic development. This gene is part of the A cluster on
            chromosome 7 and encodes a DNA-binding transcription factor that
            may regulate gene expression, morphogenesis, and differentiation.
            More specifically, it may function in fertility, embryo viability,
            and regulation of hematopoietic lineage commitment. Alternatively
            spliced transcript variants have been described. Read-through
            transcription also exists between this gene and the downstream
            homeobox A9 (HOXA9) gene. [provided by RefSeq, Mar 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            Sequence Note: An upstream start codon is selected for this RefSeq
            based on conservation in at least 24 vertebrate species including
            mouse, rat, human, chimp, macaque, dog, cow, chicken, lizard,
            Xenopus tropicalis, Tetraodon and Fugu. Historically, a start codon
            that is 17 aa downstream has been used as the translation AUG start
            codon. No experimental evidence exists regarding which site is
            preferentially used.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013971.2, ERR279867.2368.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283921.5/ ENSP00000283921.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..410
                     /product="homeobox protein Hox-A10"
                     /note="homeo box A10; homeobox protein 1H; homeobox
                     protein HOXA10; homeobox protein Hox-1H; homeobox protein
                     Hox-1.8"
                     /calculated_mol_wt=42283
     Region          18
                     /region_name="alternative translation initiation codon"
     Region          89..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31260.3)"
     Region          221..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31260.3)"
     Region          337..393
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..410
                     /gene="HOXA10"
                     /gene_synonym="HOX1; HOX1.8; HOX1H; PL"
                     /coded_by="NM_018951.4:15..1247"
                     /db_xref="CCDS:CCDS5410.2"
                     /db_xref="GeneID:3206"
                     /db_xref="HGNC:HGNC:5100"
                     /db_xref="MIM:142957"
ORIGIN      
        1 msarkgyllp spnypttmsc sespaansfl vdslissgrg eaggggggag ggggggyyah
       61 ggvylppaad lpyglqscgl fptlggkrne aaspgsgggg gglgpgahgy gpspidlwld
      121 aprscrmepp dgpppppqqq pppppqppqp apqatscsfa qnikeessyc lydsadkcpk
      181 vsataaelap fprgpppdgc algtssgvpv pgyfrlsqay gtakgygsgg ggaqqlgagp
      241 fpaqppgrgf dlppalasgs adaarkeral dspppptlac gsgggsqgde eahasssaae
      301 elspapsess kaspekdslg nskgenaanw ltaksgrkkr cpytkhqtle lekeflfnmy
      361 ltrerrleis rsvhltdrqv kiwfqnrrmk lkkmnrenri reltanfnfs
//
LOCUS       NP_001355745            1142 aa            linear   ROD 27-APR-2025
DEFINITION  centrosome and spindle pole associated protein 1 isoform 2 [Mus
            musculus].
ACCESSION   NP_001355745 XP_011236667
VERSION     NP_001355745.1
DBSOURCE    REFSEQ: accession NM_001368816.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1142)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1142)
  AUTHORS   Oeschger,F.M., Wang,W.Z., Lee,S., Garcia-Moreno,F., Goffinet,A.M.,
            Arbones,M.L., Rakic,S. and Molnar,Z.
  TITLE     Gene expression analysis of the embryonic subplate
  JOURNAL   Cereb Cortex 22 (6), 1343-1359 (2012)
   PUBMED   21862448
REFERENCE   3  (residues 1 to 1142)
  AUTHORS   Asiedu,M., Wu,D., Matsumura,F. and Wei,Q.
  TITLE     Centrosome/spindle pole-associated protein regulates cytokinesis
            via promoting the recruitment of MyoGEF to the central spindle
  JOURNAL   Mol Biol Cell 20 (5), 1428-1440 (2009)
   PUBMED   19129481
REFERENCE   4  (residues 1 to 1142)
  AUTHORS   Olesen,C., Nyeng,P., Kalisz,M., Jensen,T.H., Moller,M., Tommerup,N.
            and Byskov,A.G.
  TITLE     Global gene expression analysis in fetal mouse ovaries with and
            without meiosis and comparison of selected genes with meiosis in
            the testis
  JOURNAL   Cell Tissue Res 328 (1), 207-221 (2007)
   PUBMED   17431699
REFERENCE   5  (residues 1 to 1142)
  AUTHORS   Patzke,S., Hauge,H., Sioud,M., Finne,E.F., Sivertsen,E.A.,
            Delabie,J., Stokke,T. and Aasheim,H.C.
  TITLE     Identification of a novel centrosome/microtubule-associated
            coiled-coil protein involved in cell-cycle progression and spindle
            organization
  JOURNAL   Oncogene 24 (7), 1159-1173 (2005)
   PUBMED   15580290
REFERENCE   6  (residues 1 to 1142)
  AUTHORS   Nishimura,M., Yokoi,N., Miki,T., Horikawa,Y., Yoshioka,H.,
            Takeda,J., Ohara,O. and Seino,S.
  TITLE     Construction of a multi-functional cDNA library specific for mouse
            pancreatic islets and its application to microarray
  JOURNAL   DNA Res 11 (5), 315-323 (2004)
   PUBMED   15747579
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC102570.8 and AC159972.5.
            
            On Feb 28, 2019 this sequence version replaced XP_011236667.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ008676.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1142
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 2.3 cM"
     Protein         1..1142
                     /product="centrosome and spindle pole associated protein 1
                     isoform 2"
                     /note="centrosome/spindle pole-associated protein 2;
                     centrosome/spindle pole-associated protein 3"
                     /calculated_mol_wt=131078
     Region          <564..>693
                     /region_name="CCDC34"
                     /note="Coiled-coil domain-containing protein 3; pfam13904"
                     /db_xref="CDD:464032"
     CDS             1..1142
                     /gene="Cspp1"
                     /gene_synonym="2310020J12Rik; 4930413O22Rik; Cspp2; Cspp3"
                     /coded_by="NM_001368816.1:1..3429"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS87812.1"
                     /db_xref="GeneID:211660"
                     /db_xref="MGI:MGI:2681832"
ORIGIN      
        1 mdlncyphlv aghahsyliw rgkaseklse nskilismak enippssqqq pkgplgieyg
       61 lslplgedye qkkhklkeel rqdyrryltq gitqakrkkn flstgetdps tlgvslpide
      121 rlsakerlkl ernreynqfl rgkaestekv rqvekniepk sqrnknpisq gksdlplqiq
      181 taythsegpw lsrqeeglyr qldgeielrs rrplkqtkee vgisgaehps lsgsagvper
      241 rarrangerv ldrqhcradr dpgvsedmde rfrfesdfdr rllrvytngr phgsrrgyvd
      301 gddvpeepnt qisaaenksv hcngpprsad lditspfagm lfggedrelt krrkekyrqe
      361 lleqiaeqqk kkrrekdlaf gittsgvqdp ekspdrlkqf sltprhfeem pperprvafq
      421 tppppfsaps spsvppvhsa pshnedlhsg lgstlgelah prvlpvplnp ppppllappa
      481 snyrtpydda yyfygarntl dpnivyygsg miggqpaphv sapvthqvap pavntvgqne
      541 qkvlsdglrn sglvfedkpk pstqslqsyq ealqeqirer earrkkerle keeyeaklea
      601 emriynpwgk ggggaplrda kgnlisplqt qsspfargnt fgeplselqi kqqelyknfl
      661 rfqieekrqr eeaereklrv aeekeekrla eqrariqqey eeeqerrrek eeeqrlknee
      721 lirlaeerrk eaerkkkeee ekhnlqlqhy yereniigde tkhlrqpspv vpalqnkias
      781 klqrppsvdt iissfihess msraqsppvp arknqlraee ekknvimels emrkqlrsee
      841 rrlqgrllhl dsddeipmrk rernpmdifd marhrvqapv rrpspkglda ttfqnihdfn
      901 elrerdsdtr vdlrlmypdp prdhhtleiq qqallreqqk rlnrikmrrd agadldtict
      961 dnaqgrrmpr ddtndflkns llesdsafig aygetypvie dnafpppsql psarerrrnk
     1021 lkgldfdssr lhtpqdglsl ksissvnvdq vrmrnedrmr rlteqqkkpt ntddegslvd
     1081 pddimrhlsd dgrnsaatep wlrpgtsesl krfmaehlne eqhkgpgkpg tftwqglsaa
     1141 ha
//
LOCUS       NP_001350344             235 aa            linear   PRI 27-APR-2025
DEFINITION  motile sperm domain-containing protein 3 isoform a [Homo sapiens].
ACCESSION   NP_001350344 XP_005250586
VERSION     NP_001350344.1
DBSOURCE    REFSEQ: accession NM_001363415.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Cabukusta,B., Berlin,I., van Elsland,D.M., Forkink,I., Spits,M., de
            Jong,A.W.M., Akkermans,J.J.L.L., Wijdeven,R.H.M., Janssen,G.M.C.,
            van Veelen,P.A. and Neefjes,J.
  TITLE     Human VAPome Analysis Reveals MOSPD1 and MOSPD3 as Membrane Contact
            Site Proteins Interacting with FFAT-Related FFNT Motifs
  JOURNAL   Cell Rep 33 (10), 108475 (2020)
   PUBMED   33296653
  REMARK    GeneRIF: Human VAPome Analysis Reveals MOSPD1 and MOSPD3 as
            Membrane Contact Site Proteins Interacting with FFAT-Related FFNT
            Motifs.
            Erratum:[Cell Rep. 2023 Jul 25;42(7):112849. doi:
            10.1016/j.celrep.2023.112849. PMID: 37440407]
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Pall,G.S., Wallis,J., Axton,R., Brownstein,D.G., Gautier,P.,
            Buerger,K., Mulford,C., Mullins,J.J. and Forrester,L.M.
  TITLE     A novel transmembrane MSP-containing protein that plays a role in
            right ventricle development
  JOURNAL   Genomics 84 (6), 1051-1059 (2004)
   PUBMED   15533722
  REMARK    GeneRIF: Deletion fo the Mospd3 locus is mutagenic and breeding to
            homozygosity results in a characteristic right ventricle defect and
            neonatal lethality in 50% of mice.
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Glockner,G., Scherer,S., Schattevoy,R., Boright,A., Weber,J.,
            Tsui,L.C. and Rosenthal,A.
  TITLE     Large-scale sequencing of two regions in human chromosome 7q22:
            analysis of 650 kb of genomic sequence around the EPO and CUTL1
            loci reveals 17 genes
  JOURNAL   Genome Res 8 (10), 1060-1073 (1998)
   PUBMED   9799793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099394.6, BE745548.1 and
            CN256396.1.
            
            On May 18, 2018 this sequence version replaced XP_005250586.1.
            
            Summary: This gene encodes a multi-pass membrane protein with a
            major sperm protein (MSP) domain. The deletion of a similar mouse
            gene is associated with defective cardiac development and neonatal
            lethality. Alternate transcriptional splice variants, encoding
            different isoforms, have been described. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.729924.1,
                                           SRR9304719.253102.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..235
                     /product="motile sperm domain-containing protein 3 isoform
                     a"
                     /note="motile sperm domain-containing protein 3"
                     /calculated_mol_wt=25388
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75425.1)"
     Region          41..133
                     /region_name="Motile_Sperm"
                     /note="MSP (Major sperm protein) domain; pfam00635"
                     /db_xref="CDD:459882"
     Region          143..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75425.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75425.1)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75425.1)"
     CDS             1..235
                     /gene="MOSPD3"
                     /gene_synonym="CDS3; NET30"
                     /coded_by="NM_001363415.1:126..833"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS5701.1"
                     /db_xref="GeneID:64598"
                     /db_xref="HGNC:HGNC:25078"
                     /db_xref="MIM:609125"
ORIGIN      
        1 mrrgapqdqe lvgpgppgrg srgappplgp vvpvlvfppd lvfradqrsg prqlltlynp
       61 tgtalrfrvl ctapakytvf daegyvkpqs cidivirhva pipshydvqd rfrielseeg
      121 aegrvvgrkd itsilrapay plelqgqpdp aprpgppagt ppptarhfqe hprqqlatss
      181 fllflltgiv svaflllplp delgsqlpqv lhvslgqklv aayvlglltm vflrt
//
LOCUS       NP_084241                257 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF170 isoform 1 [Mus musculus].
ACCESSION   NP_084241
VERSION     NP_084241.2
DBSOURCE    REFSEQ: accession NM_029965.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Song,X., Liu,S., Wang,W., Ma,Z., Cao,X. and Jiang,M.
  TITLE     E3 ubiquitin ligase RNF170 inhibits innate immune responses by
            targeting and degrading TLR3 in murine cells
  JOURNAL   Cell Mol Immunol 17 (8), 865-874 (2020)
   PUBMED   31076723
  REMARK    GeneRIF: E3 ubiquitin ligase RNF170 inhibits innate immune
            responses by targeting and degrading TLR3 in murine cells.
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Kim,Y., Kim,S.H., Kim,K.H., Chae,S., Kim,C., Kim,J., Shin,H.S.,
            Lee,M.S. and Kim,D.
  TITLE     Age-dependent gait abnormalities in mice lacking the Rnf170 gene
            linked to human autosomal-dominant sensory ataxia
  JOURNAL   Hum Mol Genet 24 (25), 7196-7206 (2015)
   PUBMED   26433933
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Lu,J.P., Wang,Y., Sliter,D.A., Pearce,M.M. and Wojcikiewicz,R.J.
  TITLE     RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase,
            mediates inositol 1,4,5-trisphosphate receptor ubiquitination and
            degradation
  JOURNAL   J Biol Chem 286 (27), 24426-24433 (2011)
   PUBMED   21610068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093366.9.
            
            On May 14, 2019 this sequence version replaced NP_084241.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK162554.1, BC114210.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 14.38 cM"
     Protein         1..257
                     /product="E3 ubiquitin-protein ligase RNF170 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF170; RING-type E3
                     ubiquitin transferase RNF170"
                     /calculated_mol_wt=29687
     Region          84..139
                     /region_name="RING-HC_RNF170"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 170 (RNF170) and similar proteins; cd16553"
                     /db_xref="CDD:438215"
     Region          203..238
                     /region_name="DUF1232"
                     /note="Protein of unknown function (DUF1232); pfam06803"
                     /db_xref="CDD:462011"
     CDS             1..257
                     /gene="Rnf170"
                     /gene_synonym="6720407G21Rik"
                     /coded_by="NM_029965.4:365..1138"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS22207.1"
                     /db_xref="GeneID:77733"
                     /db_xref="MGI:MGI:1924983"
ORIGIN      
        1 maryysegqs lqqddsfieg vsdqvlvavv vslaltatll yallrnvqqn ihpenqelvr
       61 vlreqfqteq dvpaparqqf ytemycpicl hqasfpvetn cghlfcgsci iaywrygswl
      121 gaiscpicrq tvtllltvfg eddqsqdvir lrqdvndynr rfsgqprsim erimdlptll
      181 rhafrevfsv gglfwmfrir imlclmgaff ylispldfvp ealfgilgfl ddffviflll
      241 iyisimyrev itqrltr
//
LOCUS       NP_001010858             235 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF187 [Homo sapiens].
ACCESSION   NP_001010858 XP_001129309 XP_001715971 XP_933122
VERSION     NP_001010858.2
DBSOURCE    REFSEQ: accession NM_001010858.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Fan,X.T., Gao,B.F., Wang,X.F., Zhou,K., Zhao,Y. and Yuan,J.
  TITLE     Immune infiltration is associated with pan-cancer prognostic
            biomarker RING finger protein 187
  JOURNAL   J Mol Recognit 37 (2), e3071 (2024)
   PUBMED   38167828
  REMARK    GeneRIF: Immune infiltration is associated with pan-cancer
            prognostic biomarker RING finger protein 187.
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Li,X., Niu,Z., Sun,C., Zhuo,S., Yang,H., Yang,X., Liu,Y., Yan,C.,
            Li,Z., Cao,Q., Ji,G., Ding,Y., Zhuang,T. and Zhu,J.
  TITLE     Regulation of P53 signaling in breast cancer by the E3 ubiquitin
            ligase RNF187
  JOURNAL   Cell Death Dis 13 (2), 149 (2022)
   PUBMED   35165289
  REMARK    GeneRIF: Regulation of P53 signaling in breast cancer by the E3
            ubiquitin ligase RNF187.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Pang,D., Wang,W., Zhou,X., Lu,K., Zhang,J., Chen,Z., Wang,L.,
            Shen,F., Chen,Z., Wang,S., Hou,J., Zhang,A., Lv,B., Gao,C., Yan,Z.,
            Hu,Y., Chang,T., Wang,L. and Li,X.
  TITLE     RACO-1 modulates Hippo signalling in oesophageal squamous cell
            carcinoma
  JOURNAL   J Cell Mol Med 24 (20), 11912-11921 (2020)
   PUBMED   32896069
  REMARK    GeneRIF: RACO-1 modulates Hippo signalling in oesophageal squamous
            cell carcinoma.
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Chen,J., Chen,K., Zhou,Z., Huang,L., Cai,Y., Tu,H. and Zhang,X.
  TITLE     RING finger protein 187 as a novel potential biomarker for
            predicting the prognosis of ovarian carcinoma in 2 cancer centers
  JOURNAL   Curr Probl Cancer 44 (5), 100555 (2020)
   PUBMED   32057463
  REMARK    GeneRIF: RING finger protein 187 as a novel potential biomarker for
            predicting the prognosis of ovarian carcinoma in 2 cancer centers.
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Fu,Z., Yu,W., Wang,H. and Chen,X.
  TITLE     Overexpression of RNF187 induces cell EMT and apoptosis resistance
            in NSCLC
  JOURNAL   J Cell Physiol 234 (8), 14161-14169 (2019)
   PUBMED   30624778
  REMARK    GeneRIF: elevated RNF187 expression promotes NSCLC development by
            inducing cell EMT and apoptosis resistance, and RNF187 may be a
            novel prognostic indicator for NSCLC patients after curative
            resection
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Forster,L., Finlayson,J. and Ghassemifar,R.
  TITLE     RNF187 is Downregulated Following NF-kappaB Inhibition in Late
            Erythroblasts
  JOURNAL   Biochem Genet 54 (5), 714-721 (2016)
   PUBMED   27259582
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Chimusa,E.R., Zaitlen,N., Daya,M., Moller,M., van Helden,P.D.,
            Mulder,N.J., Price,A.L. and Hoal,E.G.
  TITLE     Genome-wide association study of ancestry-specific TB risk in the
            South African Coloured population
  JOURNAL   Hum Mol Genet 23 (3), 796-809 (2014)
   PUBMED   24057671
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Davies,C.C., Chakraborty,A., Diefenbacher,M.E., Skehel,M. and
            Behrens,A.
  TITLE     Arginine methylation of the c-Jun coactivator RACO-1 is required
            for c-Jun/AP-1 activation
  JOURNAL   EMBO J 32 (11), 1556-1567 (2013)
   PUBMED   23624934
  REMARK    GeneRIF: Arginine methylation of RACO-1 is required for efficient
            transcriptional activation by c-Jun/AP-1 and thus identify PRMT1 as
            an important regulator of c-Jun/AP-1 function.
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Davies,C.C., Chakraborty,A., Cipriani,F., Haigh,K., Haigh,J.J. and
            Behrens,A.
  TITLE     Identification of a co-activator that links growth factor
            signalling to c-Jun/AP-1 activation
  JOURNAL   Nat Cell Biol 12 (10), 963-972 (2010)
   PUBMED   20852630
  REMARK    GeneRIF: The RACO-1(RING domain AP-1 co-activator-1) is a
            co-activator that links c-Jun to growth factor signalling and is
            essential for AP-1 function in proliferation
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI551408.1, BC012758.2 and AL139288.15.
            
            On Aug 20, 2009 this sequence version replaced NP_001010858.1.
            
            Sequence Note: The annotated protein is predicted to be translated
            from a non-AUG start codon based on cross-species sequence
            conservation, and includes a RING domain that would not be present
            if translation were to initiate from the first in-frame AUG. This
            RefSeq record was created from transcript and genomic sequence data
            to make the sequence consistent with the reference genome assembly.
            The genomic coordinates used for the transcript record were based
            on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279862.4775.1, BC012758.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match       :: ENST00000305943.9/ ENSP00000306396.9
            non-AUG initiation codon :: inferred from conservation
            RefSeq Select criteria   :: based on single protein-coding
                                        transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.13"
     Protein         1..235
                     /product="E3 ubiquitin-protein ligase RNF187"
                     /EC_number="2.3.2.27"
                     /note="protein RNF187; RING domain AP1 coactivator 1;
                     RING-type E3 ubiquitin transferase RNF187; ring domain
                     AP-1 co-activator 1"
                     /calculated_mol_wt=26059
     Region          9..52
                     /region_name="RING-HC_TRIM39_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 39 (TRIM39) and similar proteins;
                     cd16601"
                     /db_xref="CDD:438263"
     Site            98
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23624934; propagated from
                     UniProtKB/Swiss-Prot (Q5TA31.2)"
     Site            109
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23624934; propagated from
                     UniProtKB/Swiss-Prot (Q5TA31.2)"
     CDS             1..235
                     /gene="RNF187"
                     /gene_synonym="RACO-1; RACO1"
                     /coded_by="NM_001010858.3:108..815"
                     /note="non-AUG (CUG) translation initiation codon"
                     /db_xref="CCDS:CCDS76271.1"
                     /db_xref="GeneID:149603"
                     /db_xref="HGNC:HGNC:27146"
                     /db_xref="MIM:613754"
ORIGIN      
        1 malpagpaea acalcqrapr epvradcghr fcracvvrfw aeedgpfpcp ecaddcwqra
       61 vepgrpplsr rllaleeaaa apardgpase aalqllcrad agplcaacrm aagpeppewe
      121 prwrkalrgk enkgsveimr kdlndardlh gqaesaaavw kghvmdrrkk altdykklra
      181 ffveeeehfl qeaekeeglp edeladpter frsllqavse lekkhrnlgl smllq
//
LOCUS       NP_008962                334 aa            linear   PRI 27-APR-2025
DEFINITION  heat shock factor 2-binding protein [Homo sapiens].
ACCESSION   NP_008962
VERSION     NP_008962.1
DBSOURCE    REFSEQ: accession NM_007031.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Pendlebury,D.F., Zhang,J., Agrawal,R., Shibuya,H. and Nandakumar,J.
  TITLE     Structure of a meiosis-specific complex central to BRCA2
            localization at recombination sites
  JOURNAL   Nat Struct Mol Biol 28 (8), 671-680 (2021)
   PUBMED   34373645
  REMARK    GeneRIF: Structure of a meiosis-specific complex central to BRCA2
            localization at recombination sites.
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Ghouil,R., Miron,S., Koornneef,L., Veerman,J., Paul,M.W., Le
            Du,M.H., Sleddens-Linkels,E., van Rossum-Fikkert,S.E., van Loon,Y.,
            Felipe-Medina,N., Pendas,A.M., Maas,A., Essers,J., Legrand,P.,
            Baarends,W.M., Kanaar,R., Zinn-Justin,S. and Zelensky,A.N.
  TITLE     BRCA2 binding through a cryptic repeated motif to HSF2BP oligomers
            does not impact meiotic recombination
  JOURNAL   Nat Commun 12 (1), 4605 (2021)
   PUBMED   34326328
  REMARK    GeneRIF: BRCA2 binding through a cryptic repeated motif to HSF2BP
            oligomers does not impact meiotic recombination.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Sato,K., Brandsma,I., van Rossum-Fikkert,S.E., Verkaik,N.,
            Oostra,A.B., Dorsman,J.C., van Gent,D.C., Knipscheer,P., Kanaar,R.
            and Zelensky,A.N.
  TITLE     HSF2BP negatively regulates homologous recombination in DNA
            interstrand crosslink repair
  JOURNAL   Nucleic Acids Res 48 (5), 2442-2456 (2020)
   PUBMED   31960047
  REMARK    GeneRIF: Naturally occurring elevated production of HSF2BP in
            tumors may be a source of cancer-promoting genomic instability and
            also a targetable vulnerability.
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Kottyan,L.C., Davis,B.P., Sherrill,J.D., Liu,K., Rochman,M.,
            Kaufman,K., Weirauch,M.T., Vaughn,S., Lazaro,S., Rupert,A.M.,
            Kohram,M., Stucke,E.M., Kemme,K.A., Magnusen,A., He,H.,
            Dexheimer,P., Chehade,M., Wood,R.A., Pesek,R.D., Vickery,B.P.,
            Fleischer,D.M., Lindbad,R., Sampson,H.A., Mukkada,V.A.,
            Putnam,P.E., Abonia,J.P., Martin,L.J., Harley,J.B. and
            Rothenberg,M.E.
  TITLE     Genome-wide association analysis of eosinophilic esophagitis
            provides insight into the tissue specificity of this allergic
            disease
  JOURNAL   Nat Genet 46 (8), 895-900 (2014)
   PUBMED   25017104
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Vinayagam,A., Stelzl,U., Foulle,R., Plassmann,S., Zenkner,M.,
            Timm,J., Assmus,H.E., Andrade-Navarro,M.A. and Wanker,E.E.
  TITLE     A directed protein interaction network for investigating
            intracellular signal transduction
  JOURNAL   Sci Signal 4 (189), rs8 (2011)
   PUBMED   21900206
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Yoshima,T., Yura,T. and Yanagi,H.
  TITLE     Novel testis-specific protein that interacts with heat shock factor
            2
  JOURNAL   Gene 214 (1-2), 139-146 (1998)
   PUBMED   9651507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB007131.1 and AP001050.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: HSF2 binding protein (HSF2BP) associates with HSF2. The
            interaction occurs between the trimerization domain of HSF2 and the
            amino terminal hydrophilic region of HSF2BP that comprises two
            leucine zipper motifs. HSF2BP may therefore be involved in
            modulating HSF2 activation. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB007131.1, BC000153.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000291560.7/ ENSP00000291560.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..334
                     /product="heat shock factor 2-binding protein"
                     /note="meiotic localizer of BRCA2"
                     /calculated_mol_wt=37514
     Region          14..51
                     /region_name="Interaction with BRME1.
                     /evidence=ECO:0000250|UniProtKB:Q9D4G2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75031.1)"
     Region          17..>118
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          83..334
                     /region_name="Interaction with BRCA2.
                     /evidence=ECO:0000250|UniProtKB:Q9D4G2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75031.1)"
     CDS             1..334
                     /gene="HSF2BP"
                     /gene_synonym="MEILB2; POF19"
                     /coded_by="NM_007031.2:328..1332"
                     /db_xref="CCDS:CCDS13697.1"
                     /db_xref="GeneID:11077"
                     /db_xref="HGNC:HGNC:5226"
                     /db_xref="MIM:604554"
ORIGIN      
        1 mgeagaaeea crhmgtkeef vkvrkkdler lttevmqird flprilngev lesfqklkiv
       61 eknlerkeqe leqlkmdceh fkarletvqa dnirekkekl alrqqlneak qqllqqaeyc
      121 temgaaactl lwgvssseev vkailggdka lkffsitgqt mesfvksldg dvqeldsdes
      181 qfvfalagiv tnvaaiacgr eflvnssrvl ldtilqllgd lkpgqctklk vlmlmslynv
      241 sinlkglkyi sespgfipll wwllsdpdae vclhvlrlvq svvlepevfs ksasefrssl
      301 plqrilamsk srnprlqtaa qelledlrtl ehnv
//
LOCUS       NP_114141               5635 aa            linear   PRI 27-APR-2025
DEFINITION  hemicentin-1 precursor [Homo sapiens].
ACCESSION   NP_114141
VERSION     NP_114141.2
DBSOURCE    REFSEQ: accession NM_031935.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 5635)
  AUTHORS   Wen,D., Wang,L., Tan,S., Tang,R., Xie,W., Liu,S., Tang,C. and He,Y.
  TITLE     HOXD9 aggravates the development of cervical cancer by
            transcriptionally activating HMCN1
  JOURNAL   Panminerva Med 64 (4), 532-536 (2022)
   PUBMED   32414224
  REMARK    GeneRIF: HOXD9 aggravates the development of cervical cancer by
            transcriptionally activating HMCN1.
REFERENCE   2  (residues 1 to 5635)
  AUTHORS   Gong,Z., Wu,X., Guo,Q., Du,H., Zhang,F. and Kong,Y.
  TITLE     Comprehensive Analysis of HMCN1 Somatic Mutation in Clear Cell
            Renal Cell Carcinoma
  JOURNAL   Genes (Basel) 13 (7), 1282 (2022)
   PUBMED   35886066
  REMARK    GeneRIF: Comprehensive Analysis of HMCN1 Somatic Mutation in Clear
            Cell Renal Cell Carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 5635)
  AUTHORS   Liu,C.L., Pan,H.W., Torng,P.L., Fan,M.H. and Mao,T.L.
  TITLE     SRPX and HMCN1 regulate cancer-associated fibroblasts to promote
            the invasiveness of ovarian carcinoma
  JOURNAL   Oncol Rep 42 (6), 2706-2715 (2019)
   PUBMED   31638245
  REMARK    GeneRIF: the findings of the present study suggest that targeting
            the Cancerassociated fibroblasts genes, SRPX and HMCN1, can inhibit
            ovarian cancer migration and invasion.
REFERENCE   4  (residues 1 to 5635)
  AUTHORS   Toffoli,B., Zennaro,C., Winkler,C., Giordano Attianese,G.M.P.,
            Bernardi,S., Carraro,M., Gilardi,F. and Desvergne,B.
  TITLE     Hemicentin 1 influences podocyte dynamic changes in glomerular
            diseases
  JOURNAL   Am J Physiol Renal Physiol 314 (6), F1154-F1165 (2018)
   PUBMED   29488390
  REMARK    GeneRIF: Identify HMCN1 as a new molecule involved in the dynamic
            changes of podocyte foot processes in glomerular disease.
REFERENCE   5  (residues 1 to 5635)
  AUTHORS   Koruyucu,M., Kasimoglu,Y., Seymen,F., Bayram,M., Patir,A.,
            Ergoz,N., Tuna,E.B., Gencay,K., Deeley,K., Bussaneli,D., Modesto,A.
            and Vieira,A.R.
  TITLE     Rethinking isolated cleft lip and palate as a syndrome
  JOURNAL   Oral Surg Oral Med Oral Pathol Oral Radiol 125 (4), 307-312 (2018)
   PUBMED   29500156
  REMARK    GeneRIF: In the group that combined individuals affected by
            isolated cleft lip and palate, tooth agenesis, supernumerary teeth,
            molar incisor hypomineralization, or dental caries, we found an
            association with rs622260 but not with the rs10798049 marker. We
            determined that allele C of rs622260 was overrepresented in all
            individuals studied compared with a group of unrelated individuals
            who did not present any of these conditions.
REFERENCE   6  (residues 1 to 5635)
  AUTHORS   Hayashi,M., Merriam,J.E., Klaver,C.C., Zernant,J., Bergen,A.A.,
            Smith,R.T., Chang,S., Merriam,J.C. and Allikmets,R.
  TITLE     Evaluation of the ARMD1 locus on 1q25-31 in patients with
            age-related maculopathy: genetic variation in laminin genes and in
            exon 104 of HEMICENTIN-1
  JOURNAL   Ophthalmic Genet 25 (2), 111-119 (2004)
   PUBMED   15370542
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 5635)
  AUTHORS   Schultz,D.W., Klein,M.L., Humpert,A.J., Luzier,C.W., Persun,V.,
            Schain,M., Mahan,A., Runckel,C., Cassera,M., Vittal,V., Doyle,T.M.,
            Martin,T.M., Weleber,R.G., Francis,P.J. and Acott,T.S.
  TITLE     Analysis of the ARMD1 locus: evidence that a mutation in
            HEMICENTIN-1 is associated with age-related macular degeneration in
            a large family
  JOURNAL   Hum Mol Genet 12 (24), 3315-3323 (2003)
   PUBMED   14570714
  REMARK    GeneRIF: We mapped the ARMD1 gene.  Identification of the genes
            involved in AMD will lead to a better understanding of this disease
            at the molecular level.
REFERENCE   8  (residues 1 to 5635)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
  REMARK    Review article
REFERENCE   9  (residues 1 to 5635)
  AUTHORS   Vogel,B.E. and Hedgecock,E.M.
  TITLE     Hemicentin, a conserved extracellular member of the immunoglobulin
            superfamily, organizes epithelial and other cell attachments into
            oriented line-shaped junctions
  JOURNAL   Development 128 (6), 883-894 (2001)
   PUBMED   11222143
REFERENCE   10 (residues 1 to 5635)
  AUTHORS   Klein,M.L., Schultz,D.W., Edwards,A., Matise,T.C., Rust,K.,
            Berselli,C.B., Trzupek,K., Weleber,R.G., Ott,J., Wirtz,M.K. and
            Acott,T.S.
  TITLE     Age-related macular degeneration. Clinical features in a large
            family and linkage to chromosome 1q
  JOURNAL   Arch Ophthalmol 116 (8), 1082-1088 (1998)
   PUBMED   9715689
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121996.15, AL135796.6,
            AL133515.9, AL391824.8, BX928748.3, AL118512.9, AL135797.10 and
            AL133553.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 1, 2006 this sequence version replaced NP_114141.1.
            
            Summary: This gene encodes a large extracellular member of the
            immunoglobulin superfamily. A similar protein in C. elegans forms
            long, fine tracks at specific extracellular sites that are involved
            in many processes such as stabilization of the germline syncytium,
            anchorage of mechanosensory neurons to the epidermis, and
            organization of hemidesmosomes in the epidermis. Mutations in this
            gene may be associated with age-related macular degeneration.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF156100.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000271588.9/ ENSP00000271588.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..5635
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.3-q31.1"
     Protein         1..5635
                     /product="hemicentin-1 precursor"
                     /note="fibulin-6; LOC100507250/HMCN1 fusion"
                     /calculated_mol_wt=610984
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2427
     Region          <12..210
                     /region_name="ChlD"
                     /note="vWFA (von Willebrand factor type A) domain of Mg
                     and Co chelatases [Coenzyme transport and metabolism];
                     COG1240"
                     /db_xref="CDD:440853"
     Site            349
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Site            390
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          448..513
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          448..451
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          460..464
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          482..486
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          496..501
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          510..513
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          526..608
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Site            528
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          537..541
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          550..554
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            550
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Site            573
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          574..578
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          588..593
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          601..604
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          612..696
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Site            620
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          629..633
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          642..646
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          664..668
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          678..683
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          691..694
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            693
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          713..789
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          720..723
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          732..736
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          755..759
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          769..774
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          783..786
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          793..884
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            809
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          810..814
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          823..829
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          850..854
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          864..869
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          877..880
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          890..977
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          907..911
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          921..925
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          943..947
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          957..962
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            970
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          980..1071
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          998..1002
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1011..1015
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1035..1038
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1048..1053
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1061..1064
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1086..1167
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          1097..1101
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1110..1114
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1134..1137
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1147..1152
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            1158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          1160..1163
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1171..1258
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          1188..1192
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1201..1205
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1224..1228
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1238..1243
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1251..1254
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1262..1355
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            1272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          1284..1288
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1297..1301
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1320..1324
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1335..1340
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1348..1351
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1369..1442
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            1369
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          1391..1395
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1414..1418
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1428..1433
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1441..1444
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1451..1529
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            1552
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          1556..1635
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          1565..1569
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1578..1582
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1601..1605
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1615..1620
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1628..1631
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1648..1725
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1659..1663
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1672..1676
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1695..1699
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1709..1714
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1746..1822
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1752..1756
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1765..1769
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1788..1792
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1802..1807
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1828..1905
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1844..1848
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1857..1861
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1881..1885
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1895..1900
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1928..2000
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            1929
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          1938..1942
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1951..1955
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1973..1978
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1988..1993
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2031..2092
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          2042..2046
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2065..2070
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2080..2085
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2103..2178
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            2112
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Site            2155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          2203..2286
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          2227..2231
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2251..2256
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2266..2271
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2289..2367
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          2391..2474
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Site            2395
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          2404..2408
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2417..2421
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2440..2444
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2454..2459
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2478..2567
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          2497..2501
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2510..2514
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2533..2537
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2547..2552
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2582..2663
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          2593..2597
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2606..2610
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2629..2633
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2643..2648
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2656..2659
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          2681..2762
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Site            2689
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          2692..2696
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2705..2709
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2727..2732
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2742..2747
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2789..2858
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          2795..2799
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2808..2812
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2831..2835
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2845..2850
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2879..2960
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Site            2887
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          2890..2894
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2903..2907
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2926..2930
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2940..2945
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2970..3052
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Site            2973
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          2982..2986
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2995..2999
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          3018..3022
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          3032..3037
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          3045..3048
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          3066..3147
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          3077..3081
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          3090..3094
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          3111..3117
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          3127..3132
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          3140..3143
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          3150..3228
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            3221
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          3252..3336
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          3264..3268
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          3277..3281
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            3300
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          3302..3306
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          3316..3321
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          3329..3332
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          3356..3430
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          3360..3364
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          3373..3377
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          3396..3400
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          3410..3415
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          3423..3426
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          3445..3523
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          3453..3457
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          3466..3470
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          3488..3493
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          3503..3508
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          3516..3519
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          3526..3602
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            3530
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          3628..3709
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          3639..3643
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          3652..3656
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          3674..3679
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          3689..3694
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            3689
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          3702..3705
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          3715..3791
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            3727
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          3730..3734
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          3743..3747
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          3766..3770
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          3780..3785
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          3803..3880
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            3812
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          3899..3984
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          3914..3918
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          3927..3931
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          3950..3954
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          3964..3969
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          3977..3980
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          3987..4062
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            4029
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          4079..4165
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          4096..4100
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          4109..4113
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          4131..4135
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          4145..4150
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          4158..4161
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          4168..4243
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          4260..4345
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          4277..4281
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          4290..4294
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          4311..4315
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          4325..4330
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          4364..4435
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          4367..4371
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          4380..4384
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            4401
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          4402..4406
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          4416..4421
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          4429..4432
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          4441..4526
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          4457..4461
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          4470..4474
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            4491
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          4492..4496
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          4506..4511
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          4519..4522
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          4533..4584
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          4589..4641
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            4606
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          4646..4698
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          4703..4755
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          4760..4812
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          4817..4869
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          4868..5092
                     /region_name="G2F"
                     /note="G2 nidogen domain and fibulin; smart00682"
                     /db_xref="CDD:214774"
     Site            order(4874,4894,4896,4906,4908,4910,5067,5072,5076,5078)
                     /site_type="other"
                     /note="collagen/perlecan interaction surface [polypeptide
                     binding]"
                     /db_xref="CDD:238158"
     Site            4894
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Site            5040
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          5107..5146
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(5107,5110,5123)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          5147..5180
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF domain; pfam07645"
                     /db_xref="CDD:429571"
     Site            order(5147,5150,5166)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          5192..5228
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(5192,5195,5208)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          5230..5263
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(5230,5233,5247)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            5267
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     Region          5272..5303
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF domain; pfam07645"
                     /db_xref="CDD:429571"
     Site            order(5272,5275,5291)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          5315..5354
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(5315,5318,5332)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          5432..5471
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(5432,5435,5448)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          5472..5508
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(5472,5475,5491)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            5615
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RW7.2)"
     CDS             1..5635
                     /gene="HMCN1"
                     /gene_synonym="ARMD1; FBLN6; FIBL-6; FIBL6"
                     /coded_by="NM_031935.3:390..17297"
                     /db_xref="CCDS:CCDS30956.1"
                     /db_xref="GeneID:83872"
                     /db_xref="HGNC:HGNC:19194"
                     /db_xref="MIM:608548"
ORIGIN      
        1 miswevvhtv flfallyssl aqdaspqsei raeeipegas tlafvfdvtg smyddlvqvi
       61 egaskilets lkrpkrplfn falvpfhdpe igpvtittdp kkfqyelrel yvqgggdcpe
      121 msigaikial eislpgsfiy vftdarskdy rlthevlqli qqkqsqvvfv ltgdcddrth
      181 igykvyeeia stssgqvfhl dkkqvnevlk wveeavqask vhllstdhle qavntwripf
      241 dpslkevtvs lsgpspmiei rnplgklikk gfglhellni hnsakvvnvk epeagmwtvk
      301 tsssgrhsvr itglstidfr agfsrkptld fkktvsrpvq giptyvllnt sgistparid
      361 llellsisgs slktipvkyy phrkpygiwn isdfvppnea fflkvtgydk ddylfqrvss
      421 vsfssivpda pkvtmpektp gyylqpgqip csvdsllpft lsfvrngvtl gvdqylkesa
      481 svnldiakvt lsdegfyeci avssagtgra qtffdvsepp pviqvpnnvt vtpgeravlt
      541 cliisavdyn ltwqrndrdv rlaeparirt lanlslelks vkfndageyh cmvsseggss
      601 aasvfltvqe ppkvtvmpkn qsftggsevs imcsatgypk pkiawtvndm fivgshryrm
      661 tsdgtlfikn aapkdagiyg clasnsagtd kqnstlryie apklmvvqse llvalgditv
      721 mecktsgipp pqvkwfkgdl elrpstflii dpllgllkiq etqdldagdy tcvaineagr
      781 atgkitldvg sppvfiqepa dvsmeigsnv tlpcyvqgyp eptikwrrld nmpifsrpfs
      841 vssisqlrtg alfilnlwas dkgtyiceae nqfgkiqset tvtvtglvap ligispsvan
      901 viegqqltlp ctllagnpip errwiknsam llqnpyitvr sdgslhierv qlqdggeytc
      961 vasnvagtnn kttsvvvhvl ptiqhgqqil stiegipvtl pckasgnpkp sviwskkgel
     1021 istssakfsa gadgslyvvs pggeesgeyv ctatntagya krkvqltvyv rprvfgdqrg
     1081 lsqdkpveis vlageevtlp cevkslpppi itwaketqli spfsprhtfl psgsmkitet
     1141 rtsdsgmylc vatniagnvt qavklnvhvp pkiqrgpkhl kvqvgqrvdi pcnaqgtplp
     1201 vitwskggst mlvdgehhvs npdgtlsidq atpsdagiyt cvatniagtd eteitlhvqe
     1261 pptvedlepp ynttfqerva nqriefpcpa kgtpkptikw lhngreltgr epgisiledg
     1321 tllviasvtp ydngeyicva vneagtterk ynlkvhvppv ikdkeqvtnv svllnqltnl
     1381 fcevegtpsp iimwykdnvq vtesstiqtv nngkilklfr atpedagrys ckainiagts
     1441 qkyfnidvlv pptiigtnfp nevsvvlnrd valecqvkgt pfpdihwfkd gkplflgdpn
     1501 velldrgqvl hlknarrndk gryqctvsna agkqakdikl tiyippsikg gnvttdisvl
     1561 insliklece trglpmpait wykdgqpims ssqalyidkg qylhipraqv sdsatytchv
     1621 anvagtaeks fhvdvyvppm iegnlatpln kqvviahslt leckaagnps piltwlkdgv
     1681 pvkandniri eaggkkleim saqeidrgqy icvatsvage keikyevdvl vppaieggde
     1741 tsyfivmvnn lleldchvtg sppptimwlk dgqliderdg fkillngrkl viaqaqvsnt
     1801 glyrcmaant agdhkkefev tvhvpptiks sglservvvk ykpvalqcia ngipnpsitw
     1861 lkddqpvnta qgnlkiqssg rvlqiaktll edagrytcva tnaagetqqh iqlhvhepps
     1921 ledagkmlne tvlvsnpvql eckaagnpvp vitwykdnrl lsgstsmtfl nrgqiidies
     1981 aqisdagiyk cvainsagat elfyslqvhv apsisgsnnm vavvvnnpvr leceargipa
     2041 psltwlkdgs pvssfsnglq vlsggrilal tsaqisdtgr ytcvavnaag ekqrdidlrv
     2101 yvppnimgee qnvsvlisqa vellcqsdai ppptltwlkd ghpllkkpgl sisenrsvlk
     2161 iedaqvqdtg rytceatnva gkteknynvn iwvppniggs deltqltvie gnlisllces
     2221 sgipppnliw kkkgspvltd smgrvrilsg grqlqisiae ksdaalyscv asnvagtakk
     2281 eynlqvyirp titnsgshpt eiivtrgksi slecevqgip pptvtwmkdg hplikakgve
     2341 ildeghilql knihvsdtgr yvcvavnvag mtdkkydlsv happsiignh rspenisvve
     2401 knsvsltcea sgiplpsitw fkdgwpvsls nsvrilsggr mlrlmqttme dagqytcvvr
     2461 naageerkif glsvlvpphi vgentledvk vkekqsvtlt cevtgnpvpe itwhkdgqpl
     2521 qedeahhiis ggrflqitnv qvphtgrytc lasspaghks rsfslnvfvs ptiagvgsdg
     2581 npedvtviln sptslvceay syppatitwf kdgtplesnr nirilpggrt lqilnaqedn
     2641 agryscvatn eagemikhye vkvyippiin kgdlwgpgls pkevkikvnn tltleceaya
     2701 ipsaslswyk dgqplksddh vniaanghtl qikeaqisdt grytcvasni agedeldfdv
     2761 niqvppsfqk lweignmldt grngeakdvi innpislyce tnaappptlt wykdghplts
     2821 sdkvlilpgg rvlqiprakv edagrytcva vneagedslq ydvrvlvppi ikgansdlpe
     2881 evtvlvnksa lieclssgsp aprnswqkdg qplleddhhk flsngrilqi lntqitdigr
     2941 yvcvaentag sakkyfnlnv hvppsvigpk senltvvvnn fisltcevsg fpppdlswlk
     3001 neqpiklntn tlivpggrtl qiirakvsdg geytciainq ageskkkfsl tvyvppsikd
     3061 hdseslsvvn vregtsvsle cesnavpppv itwykngrmi testhveila dgqmlhikka
     3121 evsdtgqyvc rainvagrdd knfhlnvyvp psiegperev ivetisnpvt ltcdatgipp
     3181 ptiawlknhk riensdslev rilsggsklq iarsqhsdsg nytciasnme gkaqkyyfls
     3241 iqvppsvaga eipsdvsvll genvelvcna ngiptpliqw lkdgkpiasg eterirvsan
     3301 gstlniygal tsdtgkytcv atnpageedr ifnlnvyvtp tirgnkdeae klmtlvdtsi
     3361 niecratgtp ppqinwlkng lplplsshir llaagqviri vraqvsdvav ytcvasnrag
     3421 vdnkhynlqv fappnmdnsm gteeitvlkg sstsmacitd gtpapsmawl rdgqplglda
     3481 hltvsthgmv lqllkaeted sgkytciasn eagevskhfi lkvlepphin gseeheeisv
     3541 ivnnpleltc iasgipapkm twmkdgrplp qtdqvqtlgg gevlristaq vedtgrytcl
     3601 asspagdddk eylvrvhvpp niagtdeprd itvlrnrqvt lecksdavpp pvitwlrnge
     3661 rlqatprvri lsggrylqin nadlgdtany tcvasniagk ttrefiltvn vppnikggpq
     3721 slvillnkst vleciaegvp tpritwrkdg avlagnhary silengflhi qsahvtdtgr
     3781 ylcmatnaag tdrrridlqv hvppsiapgp tnmtvivnvq ttlaceatgi pkpsinwrkn
     3841 ghllnvdqnq nsyrllssgs lviispsvdd tatyectvtn gagddkrtvd ltvqvppsia
     3901 deptdflvtk hapavitcta sgvpfpsihw tkngirllpr gdgyrilssg aieilatqln
     3961 hagrytcvar naagsahrhv tlhvheppvi qpqpselhvi lnnpillpce atgtpspfit
     4021 wqkeginvnt sgrnhavlps gglqisravr edagtymcva qnpagtalgk iklnvqvppv
     4081 isphlkeyvi avdkpitlsc eadglpppdi twhkdgraiv esirqrvlss gslqiafvqp
     4141 gdaghytcma anvagsssts tkltvhvppr irsteghytv nensqailpc vadgiptpai
     4201 nwkkdnvlla nllgkytaep ygelilenvv ledsgfytcv annaagedth tvsltvhvlp
     4261 tftelpgdvs lnkgeqlrls ckatgiplpk ltwtfnnnii pahfdsvngh selviervsk
     4321 edsgtyvcta ensvgfvkai gfvyvkeppv fkgdypsnwi eplggnailn cevkgdptpt
     4381 iqwnrkgvdi eishrirqlg ngslaiygtv nedagdytcv atneagvver smsltlqspp
     4441 iitlepvetv inaggkiiln cqatgepqpt itwsrqghsi swddrvnvls nnslyiadaq
     4501 kedtsefecv arnlmgsvlv rvpvivqvhg gfsqwsawra csvtcgkgiq krsrlcnqpl
     4561 panggkpcqg sdlemrncqn kpcpvdgsws ewslweectr scgrgnqtrt rtcnnpsvqh
     4621 ggrpcegnav eiimcnirpc pvhgawsawq pwgtcsescg kgtqtrarlc nnpppafggs
     4681 ycdgaetqmq vcnerncpih gkwatwasws acsvscggga rqrtrgcsdp vpqyggrkce
     4741 gsdvqsdfcn sdpcpthgnw spwsgwgtcs rtcnggqmrr yrtcdnppps nggracggpd
     4801 sqiqrcntdm cpvdgswgsw hswsqcsasc gggektrkrl cdhpvpvkgg rpcpgdttqv
     4861 trcnvqacpg gpqrargsvi gnindvefgi aflnatitds pnsdtriira kitnvprslg
     4921 samrkivsil npiywttake igeavngftl tnavfkretq vefatgeilq mshiarglds
     4981 dgsllldivv sgyvlqlqsp aevtvkdyte dyiqtgpgql yaystrlfti dgisipytwn
     5041 htvfydqaqg rmpflvetlh assvesdynq ieetlgfkih asiskgdrsn qcpsgftlds
     5101 vgpfcadede caagnpcshs chnamgtyyc scpkgltiaa dgrtcqdide calgrhtcha
     5161 gqdcdntigs yrcvvrcgsg frrtsdglsc qdinecqess pchqrcfnai gsfhcgcepg
     5221 yqlkgrkcmd vnecrqnvcr pdqhckntrg gykcidlcpn gmtkaengtc idideckdgt
     5281 hqcrynqice ntrgsyrcvc prgyrsqgvg rpcmdinece qvpkpcahqc sntpgsfkci
     5341 cppgqhllgd gkscaglerl pnygtqyssy nlarfspvrn nyqpqqhyrq yshlyssyse
     5401 yrnsrtslsr trrtirktcp egseashdtc vdidecentd acqheckntf gsyqcicppg
     5461 yqlthngktc qdidecleqn vhcgpnrmcf nmrgsyqcid tpcppnyqrd pvsgfclknc
     5521 ppndlecals pyaleyklvs lpfgiatnqd lirlvaytqd gvmhprttfl mvdeeqtvpf
     5581 alrdenlkgv vyttrplrea etyrmrvras sysangtiey qttfivyiav saypy
//
LOCUS       NP_001351212             534 aa            linear   ROD 27-APR-2025
DEFINITION  synaptotagmin-16 isoform 4 [Mus musculus].
ACCESSION   NP_001351212 XP_006515904
VERSION     NP_001351212.1
DBSOURCE    REFSEQ: accession NM_001364283.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Fukuda,M.
  TITLE     Molecular cloning, expression, and characterization of a novel
            class of synaptotagmin (Syt XIV) conserved from Drosophila to
            humans
  JOURNAL   J Biochem 133 (5), 641-649 (2003)
   PUBMED   12801916
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC161591.2 and AC158365.2.
            
            On Jun 14, 2018 this sequence version replaced XP_006515904.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.410553.1,
                                           SRR11927937.3468511.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 32.02 cM"
     Protein         1..534
                     /product="synaptotagmin-16 isoform 4"
                     /note="synaptotagmin-16; synaptotagmin 14-like protein;
                     synaptotagmin XIV-related protein"
                     /calculated_mol_wt=59603
     Region          239..362
                     /region_name="C2A_Synaptotagmin-14_16"
                     /note="C2A domain first repeat present in Synaptotagmins
                     14 and 16; cd08389"
                     /db_xref="CDD:176035"
     Region          395..532
                     /region_name="C2B_Synaptotagmin-14_16"
                     /note="C2 domain second repeat present in Synaptotagmins
                     14 and 16; cd08408"
                     /db_xref="CDD:176053"
     CDS             1..534
                     /gene="Syt16"
                     /gene_synonym="Strep14; Syt14l; syt14r"
                     /coded_by="NM_001364283.1:75..1679"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:238266"
                     /db_xref="MGI:MGI:2673872"
ORIGIN      
        1 matditpeai gflsaigvfv vllavlllfi nkklcsenlr ghpypeqrgk rkhsrdktgg
       61 htgtvnsfgd deepstsses dedvtkqfki svsrsqsfrs gvsekgktte leqkikckrl
      121 lcthqedsae gsacedldrt sqlsyseils yedrpisilp qspfesrnvr hhgpcrpemg
      181 mvrslgrpca dgvletetaf vsrgfedsya thssslwspe eqdgtslqvp hrllepiskc
      241 gdldvifeyr avtqkltvti vraqglpdkd rsgvnswqvh ivllpskkqr gktniqrgpn
      301 pvfkekvtft kleprdvasc avrfrlyaar kmtrermmge klfclshlhp egemkvtlvl
      361 eprsnlssge splspsvvsh sdsasstqsl shggvpellv glsynattgr lsvemikgsh
      421 frnlaanrap dtygklflln cvgqemsrck tsirrgqpnp vyketfvfqv alfqlsdvtl
      481 misiysrrtm krkemigwva lgqnssgeee qehweemkes kgqqtcrwht lles
//
LOCUS       NP_955371                309 aa            linear   PRI 27-APR-2025
DEFINITION  spermatid maturation protein 1 [Homo sapiens].
ACCESSION   NP_955371
VERSION     NP_955371.2
DBSOURCE    REFSEQ: accession NM_199339.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Hashemi,M.S., Mozdarani,H., Ghaedi,K. and Nasr-Esfahani,M.H.
  TITLE     Among seven testis-specific molecular markers, SPEM1 appears to
            have a significant clinical value for prediction of sperm retrieval
            in azoospermic men
  JOURNAL   Andrology 6 (6), 890-895 (2018)
   PUBMED   30054974
  REMARK    GeneRIF: SPEM1 appears to have a significant clinical value for
            prediction of sperm retrieval in azoospermic men.
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Bao,J., Wu,Q., Song,R., Jie,Z., Zheng,H., Xu,C. and Yan,W.
  TITLE     RANBP17 is localized to the XY body of spermatocytes and interacts
            with SPEM1 on the manchette of elongating spermatids
  JOURNAL   Mol Cell Endocrinol 333 (2), 134-142 (2011)
   PUBMED   21184802
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Bao,J., Zhang,J., Zheng,H., Xu,C. and Yan,W.
  TITLE     UBQLN1 interacts with SPEM1 and participates in spermiogenesis
  JOURNAL   Mol Cell Endocrinol 327 (1-2), 89-97 (2010)
   PUBMED   20558241
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Zheng,H., Stratton,C.J., Morozumi,K., Jin,J., Yanagimachi,R. and
            Yan,W.
  TITLE     Lack of Spem1 causes aberrant cytoplasm removal, sperm deformation,
            and male infertility
  JOURNAL   Proc Natl Acad Sci U S A 104 (16), 6852-6857 (2007)
   PUBMED   17426145
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113189.11 and BC033882.1.
            
            On Oct 19, 2006 this sequence version replaced NP_955371.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033882.1, SRR5189667.86767.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323675.4/ ENSP00000315554.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..309
                     /product="spermatid maturation protein 1"
                     /calculated_mol_wt=34642
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4L4.1)"
     Region          46..>147
                     /region_name="Spem1"
                     /note="Spermatid maturation protein 1; pfam15670"
                     /db_xref="CDD:464793"
     Region          209..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4L4.1)"
     CDS             1..309
                     /gene="SPEM1"
                     /gene_synonym="C17orf83"
                     /coded_by="NM_199339.3:62..991"
                     /db_xref="CCDS:CCDS42254.1"
                     /db_xref="GeneID:374768"
                     /db_xref="HGNC:HGNC:32429"
                     /db_xref="MIM:615116"
ORIGIN      
        1 mamverprpe wasyhncnsn scqdlgnsvl lllgliicin isinivtllw srfrgvlyqv
       61 fhdticekea pkssllrkqt qppkkqsspa vhlrctmdpv mmtvspppah rhrrrgsptr
      121 cahcpvawap dtddekphqy paicsyhwdv pedwegfqht qgtwvpwsqd apesppqtir
      181 fqptveerpl ktgiwselgl rayvypvnpp ppspeapshk nggegavpea eaaqyqpvpa
      241 ptlgpavipe fsrhrssgri vydardmrrr lreltrevea lsgcyplasg sstaeetskn
      301 wvyrsltgr
//
LOCUS       NP_932342                118 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome c oxidase assembly protein COX20, mitochondrial isoform
            1 [Homo sapiens].
ACCESSION   NP_932342
VERSION     NP_932342.1
DBSOURCE    REFSEQ: accession NM_198076.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Chen,L. and Liu,Y.
  TITLE     Clinical and genetic characteristics of children with
            COX20-associated mitochondrial disorder: case report and literature
            review
  JOURNAL   BMC Med Genomics 16 (1), 86 (2023)
   PUBMED   37095481
  REMARK    GeneRIF: Clinical and genetic characteristics of children with
            COX20-associated mitochondrial disorder: case report and literature
            review.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Dong,H.L., Ma,Y., Yu,H., Wei,Q., Li,J.Q., Liu,G.L., Li,H.F.,
            Chen,L., Chen,D.F., Bai,G. and Wu,Z.Y.
  TITLE     Bi-allelic loss of function variants in COX20 gene cause autosomal
            recessive sensory neuronopathy
  JOURNAL   Brain 144 (8), 2457-2470 (2021)
   PUBMED   33751098
  REMARK    GeneRIF: Bi-allelic loss of function variants in COX20 gene cause
            autosomal recessive sensory neuronopathy.
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Xu,H., Ji,T., Lian,Y., Wang,S., Chen,X., Li,S., Yin,Y. and Dong,X.
  TITLE     Observation of novel COX20 mutations related to autosomal recessive
            axonal neuropathy and static encephalopathy
  JOURNAL   Hum Genet 138 (7), 749-756 (2019)
   PUBMED   31079202
  REMARK    GeneRIF: COX20 mutation are associated with autosomal recessive
            axonal neuropathy and static encephalopathy.
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Bourens,M., Boulet,A., Leary,S.C. and Barrientos,A.
  TITLE     Human COX20 cooperates with SCO1 and SCO2 to mature COX2 and
            promote the assembly of cytochrome c oxidase
  JOURNAL   Hum Mol Genet 23 (11), 2901-2913 (2014)
   PUBMED   24403053
  REMARK    GeneRIF: COX20 cooperates with SCO1 and SCO2 to mature COX2 and
            promote the assembly of cytochrome c oxidase.
REFERENCE   7  (residues 1 to 118)
  AUTHORS   Doss,S., Lohmann,K., Seibler,P., Arns,B., Klopstock,T., Zuhlke,C.,
            Freimann,K., Winkler,S., Lohnau,T., Drungowski,M., Nurnberg,P.,
            Wiegers,K., Lohmann,E., Naz,S., Kasten,M., Bohner,G., Ramirez,A.,
            Endres,M. and Klein,C.
  TITLE     Recessive dystonia-ataxia syndrome in a Turkish family caused by a
            COX20 (FAM36A) mutation
  JOURNAL   J Neurol 261 (1), 207-212 (2014)
   PUBMED   24202787
  REMARK    GeneRIF: This study deministrated that phenotypic spectrum of
            mutation in COX20 to a recessively inherited, early-onset
            dystonia-ataxia syndrome that is characterized by reduced complex
            IV activity.
REFERENCE   8  (residues 1 to 118)
  AUTHORS   Szklarczyk,R., Wanschers,B.F., Nijtmans,L.G., Rodenburg,R.J.,
            Zschocke,J., Dikow,N., van den Brand,M.A., Hendriks-Franssen,M.G.,
            Gilissen,C., Veltman,J.A., Nooteboom,M., Koopman,W.J.,
            Willems,P.H., Smeitink,J.A., Huynen,M.A. and van den Heuvel,L.P.
  TITLE     A mutation in the FAM36A gene, the human ortholog of COX20, impairs
            cytochrome c oxidase assembly and is associated with ataxia and
            muscle hypotonia
  JOURNAL   Hum Mol Genet 22 (4), 656-667 (2013)
   PUBMED   23125284
  REMARK    GeneRIF: The function of the human gene FAM36A/COX20 in complex IV
            assembly and role of the gene in complex IV deficiency.
REFERENCE   9  (residues 1 to 118)
  AUTHORS   Thierry,G., Beneteau,C., Pichon,O., Flori,E., Isidor,B.,
            Popelard,F., Delrue,M.A., Duboscq-Bidot,L., Thuresson,A.C., van
            Bon,B.W., Cailley,D., Rooryck,C., Paubel,A., Metay,C., Dusser,A.,
            Pasquier,L., Beri,M., Bonnet,C., Jaillard,S., Dubourg,C., Tou,B.,
            Quere,M.P., Soussi-Zander,C., Toutain,A., Lacombe,D., Arveiler,B.,
            de Vries,B.B., Jonveaux,P., David,A. and Le Caignec,C.
  TITLE     Molecular characterization of 1q44 microdeletion in 11 patients
            reveals three candidate genes for intellectual disability and
            seizures
  JOURNAL   Am J Med Genet A 158A (7), 1633-1640 (2012)
   PUBMED   22678713
  REMARK    GeneRIF: These results suggest that HNRNPU, FAM36A, and NCRNA00201
            are not major genes for microcephaly and corpus callosum
            abnormalities but are good candidates for intellectual disability
            (ID) and seizures.
REFERENCE   10 (residues 1 to 118)
  AUTHORS   Szklarczyk,R., Wanschers,B.F., Cuypers,T.D., Esseling,J.J.,
            Riemersma,M., van den Brand,M.A., Gloerich,J., Lasonder,E., van den
            Heuvel,L.P., Nijtmans,L.G. and Huynen,M.A.
  TITLE     Iterative orthology prediction uncovers new mitochondrial proteins
            and identifies C12orf62 as the human ortholog of COX14, a protein
            involved in the assembly of cytochrome c oxidase
  JOURNAL   Genome Biol 13 (2), R12 (2012)
   PUBMED   22356826
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK125259.1, AK000866.1 and
            EL947693.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that plays a role in the
            assembly of cytochrome C oxidase, an important component of the
            respiratory pathway. It contains two transmembrane helices and
            localizes to the mitochondrial membrane. Mutations in this gene can
            cause mitochondrial complex IV deficiency, which results in ataxia
            and muscle hypotonia. There are multiple pseudogenes for this gene.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform 1. Variants 1 and 2 encode the same
            protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.226321.1,
                                           SRR1803614.58235.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 22356826; reported by
                                                  MitoCarta
            MANE Ensembl match                 :: ENST00000411948.7/
                                                  ENSP00000406327.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..118
                     /product="cytochrome c oxidase assembly protein COX20,
                     mitochondrial isoform 1"
                     /note="family with sequence similarity 36, member A;
                     cytochrome c oxidase protein 20 homolog; COX20 Cox2
                     chaperone homolog; cytochrome c oxidase assembly protein
                     COX20, mitochondrial; COX20, cytochrome c oxidase assembly
                     factor"
                     /calculated_mol_wt=13160
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q5RI15.2)"
     Region          14..98
                     /region_name="Cox20"
                     /note="Cytochrome c oxidase assembly protein COX20;
                     pfam12597"
                     /db_xref="CDD:403707"
     Site            34..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RI15.2)"
     Site            61..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RI15.2)"
     CDS             1..118
                     /gene="COX20"
                     /gene_synonym="FAM36A; MC4DN11"
                     /coded_by="NM_198076.6:58..414"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31080.1"
                     /db_xref="GeneID:116228"
                     /db_xref="HGNC:HGNC:26970"
                     /db_xref="MIM:614698"
ORIGIN      
        1 maappepgep eerkslkllg fldventpca rhsilygslg svvagfghfl ftsrirrscd
       61 vgvggfilvt lgcwfhcryn yakqriqeri areeikkkil yegthldper khngsssn
//
LOCUS       NP_001357059             586 aa            linear   PRI 27-APR-2025
DEFINITION  APOBEC1 complementation factor isoform 1 [Homo sapiens].
ACCESSION   NP_001357059 XP_016871649
VERSION     NP_001357059.1
DBSOURCE    REFSEQ: accession NM_001370130.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Liu,Y., Yang,J., Weng,D. and Xie,Y.
  TITLE     A1CF Binding to the p65 Interaction Site on NKRF Decreased IFN-beta
            Expression and p65 Phosphorylation (Ser536) in Renal Carcinoma
            Cells
  JOURNAL   Int J Mol Sci 25 (7), 3576 (2024)
   PUBMED   38612387
  REMARK    GeneRIF: A1CF Binding to the p65 Interaction Site on NKRF Decreased
            IFN-beta Expression and p65 Phosphorylation (Ser536) in Renal
            Carcinoma Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Liu,Q., Chen,C.Y. and Chen,G.L.
  TITLE     High APOBEC1 Complementation Factor Expression Positively Modulates
            the Proliferation, Invasion, and Migration of Endometrial Cancer
            Cells Through Regulating P53/P21 Signaling Pathway
  JOURNAL   Cancer Biother Radiopharm 37 (9), 750-758 (2022)
   PUBMED   32818382
  REMARK    GeneRIF: High APOBEC1 Complementation Factor Expression Positively
            Modulates the Proliferation, Invasion, and Migration of Endometrial
            Cancer Cells Through Regulating P53/P21 Signaling Pathway.
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Kawaguchi,M., Nakayama,A., Aoyagi,Y., Nakamura,T., Shimizu,S.,
            Kawamura,Y., Takao,M., Tamura,T., Hishida,A., Nagayoshi,M.,
            Nagase,M., Ooyama,K., Ooyama,H., Shinomiya,N. and Matsuo,H.
  TITLE     Both variants of A1CF and BAZ1B genes are associated with gout
            susceptibility: a replication study and meta-analysis in a Japanese
            population
  JOURNAL   Hum Cell 34 (2), 293-299 (2021)
   PUBMED   33517564
  REMARK    GeneRIF: Both variants of A1CF and BAZ1B genes are associated with
            gout susceptibility: a replication study and meta-analysis in a
            Japanese population.
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Song,Y., Shao,L., Xue,Y., Ruan,X., Liu,X., Yang,C., Zheng,J.,
            Shen,S., Chen,J., Li,Z. and Liu,Y.
  TITLE     Inhibition of the aberrant A1CF-FAM224A-miR-590-3p-ZNF143 positive
            feedback loop attenuated malignant biological behaviors of glioma
            cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 248 (2019)
   PUBMED   31186064
  REMARK    GeneRIF: this study revealed that A1CF can upregulate the
            expression of FAM224A via strengthening its stability, which in
            turn, influenced the negative modulation of miR-590-3p on
            transcription factor ZNF143.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Chester,A., Scott,J., Anant,S. and Navaratnam,N.
  TITLE     RNA editing: cytidine to uridine conversion in apolipoprotein B
            mRNA
  JOURNAL   Biochim Biophys Acta 1494 (1-2), 1-13 (2000)
   PUBMED   11072063
  REMARK    Review article
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Yang,Y., Sowden,M.P. and Smith,H.C.
  TITLE     Induction of cytidine to uridine editing on cytoplasmic
            apolipoprotein B mRNA by overexpressing APOBEC-1
  JOURNAL   J Biol Chem 275 (30), 22663-22669 (2000)
   PUBMED   10833526
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Lellek,H., Kirsten,R., Diehl,I., Apostel,F., Buck,F. and Greeve,J.
  TITLE     Purification and molecular cloning of a novel essential component
            of the apolipoprotein B mRNA editing enzyme-complex
  JOURNAL   J Biol Chem 275 (26), 19848-19856 (2000)
   PUBMED   10781591
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Mehta,A., Kinter,M.T., Sherman,N.E. and Driscoll,D.M.
  TITLE     Molecular cloning of apobec-1 complementation factor, a novel
            RNA-binding protein involved in the editing of apolipoprotein B
            mRNA
  JOURNAL   Mol Cell Biol 20 (5), 1846-1854 (2000)
   PUBMED   10669759
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL512366.12 and AL589794.7.
            
            On Apr 26, 2019 this sequence version replaced XP_016871649.1.
            
            Summary: Mammalian apolipoprotein B mRNA undergoes site-specific C
            to U deamination, which is mediated by a multi-component enzyme
            complex containing a minimal core composed of APOBEC-1 and a
            complementation factor encoded by this gene. The gene product has
            three non-identical RNA recognition motifs and belongs to the hnRNP
            R family of RNA-binding proteins. It has been proposed that this
            complementation factor functions as an RNA-binding subunit and
            docks APOBEC-1 to deaminate the upstream cytidine. Studies suggest
            that the protein may also be involved in other RNA editing or RNA
            processing events. Several transcript variants encoding a few
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2010].
            
            Transcript Variant: This variant (7) differs in the 5' UTR and
            coding sequence compared to variant 5. The resulting isoform (1)
            has a shorter and distinct N-terminus and lacks a short internal
            segment compared to isoform 4. Variants 1, 4, and  7 encode the
            same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.264325.1,
                                           SRR14038193.4227944.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.23"
     Protein         1..586
                     /product="APOBEC1 complementation factor isoform 1"
                     /note="APOBEC-1 stimulating protein; apo-B RNA editing
                     protein; apobec-1 complementation factor (ACF) (ASP)"
                     /calculated_mol_wt=64125
     Region          2..586
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ94.1)"
     CDS             1..586
                     /gene="A1CF"
                     /gene_synonym="ACF; ACF64; ACF65; APOBEC1CF; ASP"
                     /coded_by="NM_001370130.1:93..1853"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS7241.1"
                     /db_xref="GeneID:29974"
                     /db_xref="HGNC:HGNC:24086"
                     /db_xref="MIM:618199"
ORIGIN      
        1 mesnhksgdg lsgtqkeaal ralvqrtgys lvqengqrky ggpppgwdaa ppergceifi
       61 gklprdlfed eliplcekig kiyemrmmmd fngnnrgyaf vtfsnkveak naikqlnnye
      121 irngrllgvc asvdncrlfv ggipktkkre eilsemkkvt egvvdvivyp saadktknrg
      181 fafveyeshr aaamarrkll pgriqlwghg iavdwaepev evdedtmssv kilyvrnlml
      241 stseemieke fnnikpgave rvkkirdyaf vhfsnredav eamkalngkv ldgspievtl
      301 akpvdkdsyv rytrgtggrg tmlqgeytys lgqvydpttt ylgapvfyap qtyaaipslh
      361 fpatkghlsn raiirapsvr gaagvrglgg rgylaytglg rgyqvkgdkr edklydilpg
      421 meltpmnpvt lkpqgiklap qileeicqkn nwgqpvyqlh saigqdqrql flykitipal
      481 asqnpaihpf tppklsafvd eaktyaaeyt lqtlgiptdg gdgtmataaa aatafpgyav
      541 pnatapvsaa qlkqavtlgq dlaayttyev yptfavtarg dgygtf
//
LOCUS       NP_114427                528 aa            linear   PRI 27-APR-2025
DEFINITION  protein spinster homolog 1 isoform 1 [Homo sapiens].
ACCESSION   NP_114427
VERSION     NP_114427.1
DBSOURCE    REFSEQ: accession NM_032038.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   He,M., Kuk,A.C.Y., Ding,M., Chin,C.F., Galam,D.L.A., Nah,J.M.,
            Tan,B.C., Yeo,H.L., Chua,G.L., Benke,P.I., Wenk,M.R., Ho,L.,
            Torta,F. and Silver,D.L.
  TITLE     Spns1 is a lysophospholipid transporter mediating lysosomal
            phospholipid salvage
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2210353119 (2022)
   PUBMED   36161949
  REMARK    GeneRIF: Spns1 is a lysosomal proton-dependent
            lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine
            (LPE) transporter mediating phospholipid salvage pathway
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Fang,Z., Cao,B., Liao,J.M., Deng,J., Plummer,K.D., Liao,P., Liu,T.,
            Zhang,W., Zhang,K., Li,L., Margolin,D., Zeng,S.X., Xiong,J. and
            Lu,H.
  TITLE     SPIN1 promotes tumorigenesis by blocking the uL18 (universal large
            ribosomal subunit protein 18)-MDM2-p53 pathway in human cancer
  JOURNAL   Elife 7, e31275 (2018)
   PUBMED   29547122
  REMARK    GeneRIF: Spindlin 1 (SPIN1) sequesters ribosomal protein uL18 in
            the nucleolus, preventing it from interacting with c-mdm2
            Proto-oncogene protein (MDM2), and alleviating uL18-mediated
            inhibition of MDM2 ubiquitin ligase activity toward p53 tumor
            suppressor protein (p53).
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Yanagisawa,H., Ishii,T., Endo,K., Kawakami,E., Nagao,K.,
            Miyashita,T., Akiyama,K., Watabe,K., Komatsu,M., Yamamoto,D. and
            Eto,Y.
  TITLE     L-leucine and SPNS1 coordinately ameliorate dysfunction of
            autophagy in mouse and human Niemann-Pick type C disease
  JOURNAL   Sci Rep 7 (1), 15944 (2017)
   PUBMED   29162837
  REMARK    GeneRIF: SPNS1-dependent L-leucine export across the lysosomal
            membrane is a key step for triggering autophagy, and that this
            mechanism is impaired in Niemann-Pick type C disease-1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Rietveld,C.A., Esko,T., Davies,G., Pers,T.H., Turley,P.,
            Benyamin,B., Chabris,C.F., Emilsson,V., Johnson,A.D., Lee,J.J., de
            Leeuw,C., Marioni,R.E., Medland,S.E., Miller,M.B., Rostapshova,O.,
            van der Lee,S.J., Vinkhuyzen,A.A., Amin,N., Conley,D.,
            Derringer,J., van Duijn,C.M., Fehrmann,R., Franke,L., Glaeser,E.L.,
            Hansell,N.K., Hayward,C., Iacono,W.G., Ibrahim-Verbaas,C.,
            Jaddoe,V., Karjalainen,J., Laibson,D., Lichtenstein,P.,
            Liewald,D.C., Magnusson,P.K., Martin,N.G., McGue,M., McMahon,G.,
            Pedersen,N.L., Pinker,S., Porteous,D.J., Posthuma,D.,
            Rivadeneira,F., Smith,B.H., Starr,J.M., Tiemeier,H., Timpson,N.J.,
            Trzaskowski,M., Uitterlinden,A.G., Verhulst,F.C., Ward,M.E.,
            Wright,M.J., Davey Smith,G., Deary,I.J., Johannesson,M., Plomin,R.,
            Visscher,P.M., Benjamin,D.J., Cesarini,D. and Koellinger,P.D.
  TITLE     Common genetic variants associated with cognitive performance
            identified using the proxy-phenotype method
  JOURNAL   Proc Natl Acad Sci U S A 111 (38), 13790-13794 (2014)
   PUBMED   25201988
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2015 Jan 27;112(4):E380. doi:
            10.1073/pnas.1424631112. PMID: 25572966]
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Vastermark,A., Jacobsson,J.A., Johansson,A., Fredriksson,R.,
            Gyllensten,U. and Schioth,H.B.
  TITLE     Polymorphisms in sh2b1 and spns1 loci are associated with
            triglyceride levels in a healthy population in northern Sweden
  JOURNAL   J Genet 91 (2), 237-240 (2012)
   PUBMED   22942098
  REMARK    GeneRIF: A single nucleotide polymorphism located within the spns1
            gene is associated with plasma triglyceride levels.
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Yanagisawa,H., Miyashita,T., Nakano,Y. and Yamamoto,D.
  TITLE     HSpin1, a transmembrane protein interacting with Bcl-2/Bcl-xL,
            induces a caspase-independent autophagic cell death
  JOURNAL   Cell Death Differ 10 (7), 798-807 (2003)
   PUBMED   12815463
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Nakano,Y., Fujitani,K., Kurihara,J., Ragan,J., Usui-Aoki,K.,
            Shimoda,L., Lukacsovich,T., Suzuki,K., Sezaki,M., Sano,Y., Ueda,R.,
            Awano,W., Kaneda,M., Umeda,M. and Yamamoto,D.
  TITLE     Mutations in the novel membrane protein spinster interfere with
            programmed cell death and cause neural degeneration in Drosophila
            melanogaster
  JOURNAL   Mol Cell Biol 21 (11), 3775-3788 (2001)
   PUBMED   11340170
  REMARK    GeneRIF: Spinster protein interferes with programmed cell death in
            Drosophila melanogaster and has orthologs in nematode, mouse, and
            human.
REFERENCE   9  (residues 1 to 528)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG771918.1, BC008325.1 and CD368853.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1). Variants 1 and 2
            both encode isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF212371.1, SRR3476690.774109.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311008.16/ ENSP00000309945.11
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..528
                     /product="protein spinster homolog 1 isoform 1"
                     /note="sphingolipid transporter 1 (putative); solute
                     carrier family 63 member 1; protein spinster homolog 1;
                     spinster-like protein 1; SPNS sphingolipid transporter 1
                     (putative)"
                     /calculated_mol_wt=56499
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            50..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Region          62..479
                     /region_name="MFS_spinster_like"
                     /note="Protein spinster and spinster homologs of the Major
                     Facilitator Superfamily of transporters; cd17328"
                     /db_xref="CDD:340886"
     Site            order(72..73,76..77,80,112,164..165,167..169,172,192,
                     195..196,199,280,283..284,287..289,292,333,337,390..391,
                     395,399,419,422..423,426..427,430)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            127..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            357..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            421..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            465..485
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2V7.1)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H2V7.1)"
     CDS             1..528
                     /gene="SPNS1"
                     /gene_synonym="HSpin1; LAT; nrs; PP2030; SLC62A1; SLC63A1;
                     SPIN1; SPINL"
                     /coded_by="NM_032038.3:375..1961"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10646.1"
                     /db_xref="GeneID:83985"
                     /db_xref="HGNC:HGNC:30621"
                     /db_xref="MIM:612583"
ORIGIN      
        1 magsdtapfl sqaddpddgp vpgtpglpgs tgnpkseepe vpdqeglqri tglspgrsal
       61 ivavlcyinl lnymdrftva gvlpdieqff nigdsssgli qtvfissymv lapvfgylgd
      121 rynrkylmcg giafwslvtl gssfipgehf wlllltrglv gvgeasysti aptliadlfv
      181 adqrsrmlsi fyfaipvgsg lgyiagskvk dmagdwhwal rvtpglgvva vlllflvvre
      241 pprgaverhs dlpplnptsw wadlralarn psfvlsslgf tavafvtgsl alwapafllr
      301 srvvlgetpp clpgdscsss dslifglitc ltgvlgvglg veisrrlrhs npradplvca
      361 tgllgsapfl flslacargs ivatyififi getllsmnwa ivadillyvv iptrrstaea
      421 fqivlshllg dagspyligl isdrlrrnwp psflsefral qfslmlcafv galggaaflg
      481 taifieadrr raqlhvqgll heagstddri vvpqrgrstr vpvasvli
//
LOCUS       NP_065386                179 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-22 precursor [Homo sapiens].
ACCESSION   NP_065386
VERSION     NP_065386.1
DBSOURCE    REFSEQ: accession NM_020525.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Liao,B., Chen,W., Qi,X., Yun,C. and Pang,Y.
  TITLE     Interleukin-22 improves ovulation in polycystic ovary syndrome via
            STAT3 signaling
  JOURNAL   Mol Hum Reprod 30 (10) (2024)
   PUBMED   39423135
  REMARK    GeneRIF: Interleukin-22 improves ovulation in polycystic ovary
            syndrome via STAT3 signaling.
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Hunzeker,Z.E., Zhao,L., Kim,A.M., Parker,J.M., Zhu,Z., Xiao,H.,
            Bai,Q., Wakefield,M.R. and Fang,Y.
  TITLE     The role of IL-22 in cancer
  JOURNAL   Med Oncol 41 (10), 240 (2024)
   PUBMED   39231878
  REMARK    GeneRIF: The role of IL-22 in cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Niu,Q., Wang,M. and Liu,X.S.
  TITLE     The evolving landscape of IL-10, IL-22 and IL-26 in pleurisy
            especially in tuberculous pleurisy
  JOURNAL   Respir Res 25 (1), 275 (2024)
   PUBMED   39003443
  REMARK    GeneRIF: The evolving landscape of IL-10, IL-22 and IL-26 in
            pleurisy especially in tuberculous pleurisy.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Fang,Q., Xie,J., Zong,J., Zhou,Y., Zhou,Q., Yin,S., Cao,L., Yin,H.
            and Zhou,D.
  TITLE     Expression and diagnostic value of interleukin-22 in rheumatoid
            arthritis-associated interstitial lung disease
  JOURNAL   Int Immunopharmacol 134, 112173 (2024)
   PUBMED   38728884
  REMARK    GeneRIF: Expression and diagnostic value of interleukin-22 in
            rheumatoid arthritis-associated interstitial lung disease.
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Singh,A., Beaupre,M., Villegas-Novoa,C., Shiomitsu,K.,
            Gaudino,S.J., Tawch,S., Damle,R., Kempen,C., Choudhury,B.,
            McAleer,J.P., Sheridan,B.S., Denoya,P., Blumberg,R.S., Hearing,P.,
            Allbritton,N.L. and Kumar,P.
  TITLE     IL-22 promotes mucin-type O-glycosylation and MATH1+ cell-mediated
            amelioration of intestinal inflammation
  JOURNAL   Cell Rep 43 (5), 114206 (2024)
   PUBMED   38733584
  REMARK    GeneRIF: IL-22 promotes mucin-type O-glycosylation and MATH1[+]
            cell-mediated amelioration of intestinal inflammation.
            Erratum:[Cell Rep. 2024 Aug 27;43(8):114643. doi:
            10.1016/j.celrep.2024.114643. PMID: 39097926]
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Kotenko,S.V., Izotova,L.S., Mirochnitchenko,O.V., Esterova,E.,
            Dickensheets,H., Donnelly,R.P. and Pestka,S.
  TITLE     Identification of the functional interleukin-22 (IL-22) receptor
            complex: the IL-10R2 chain (IL-10Rbeta) is a common chain of both
            the IL-10 and IL-22 (IL-10-related T cell-derived inducible factor,
            IL-TIF) receptor complexes
  JOURNAL   J Biol Chem 276 (4), 2725-2732 (2001)
   PUBMED   11035029
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Dumoutier,L., Van Roost,E., Ameye,G., Michaux,L. and Renauld,J.C.
  TITLE     IL-TIF/IL-22: genomic organization and mapping of the human and
            mouse genes
  JOURNAL   Genes Immun 1 (8), 488-494 (2000)
   PUBMED   11197690
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Xie,M.H., Aggarwal,S., Ho,W.H., Foster,J., Zhang,Z., Stinson,J.,
            Wood,W.I., Goddard,A.D. and Gurney,A.L.
  TITLE     Interleukin (IL)-22, a novel human cytokine that signals through
            the interferon receptor-related proteins CRF2-4 and IL-22R
  JOURNAL   J Biol Chem 275 (40), 31335-31339 (2000)
   PUBMED   10875937
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Dumoutier,L., Van Roost,E., Colau,D. and Renauld,J.C.
  TITLE     Human interleukin-10-related T cell-derived inducible factor:
            molecular cloning and functional characterization as an
            hepatocyte-stimulating factor
  JOURNAL   Proc Natl Acad Sci U S A 97 (18), 10144-10149 (2000)
   PUBMED   10954742
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Dumoutier,L., Louahed,J. and Renauld,J.C.
  TITLE     Cloning and characterization of IL-10-related T cell-derived
            inducible factor (IL-TIF), a novel cytokine structurally related to
            IL-10 and inducible by IL-9
  JOURNAL   J Immunol 164 (4), 1814-1819 (2000)
   PUBMED   10657629
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC070261.1 and CD638517.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the IL10 family of cytokines that
            mediate cellular inflammatory responses. The encoded protein
            functions in antimicrobial defense at mucosal surfaces and in
            tissue repair. This protein also has pro-inflammatory properties
            and plays a role in in the pathogenesis of several intestinal
            diseases. The encoded protein is a crucial cytokine that regulates
            host immunity in infectious diseases, including COVID-19 (disease
            caused by SARS-CoV-2). [provided by RefSeq, Dec 2021].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070261.1, CD639311.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000538666.6/ ENSP00000442424.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..179
                     /product="interleukin-22 precursor"
                     /note="IL-10-related T-cell-derived inducible factor;
                     cytokine Zcyto18"
                     /calculated_mol_wt=16749
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3280
     mat_peptide     34..179
                     /product="Interleukin-22. /id=PRO_0000015383"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZX6.1)"
                     /calculated_mol_wt=16749
     Region          40..178
                     /region_name="IL22"
                     /note="Interleukin 22 IL-10-related
                     T-cell-derived-inducible factor; pfam14565"
                     /db_xref="CDD:405281"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15983417; propagated from
                     UniProtKB/Swiss-Prot (Q9GZX6.1)"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9GZX6.1)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15983417; propagated from
                     UniProtKB/Swiss-Prot (Q9GZX6.1)"
     CDS             1..179
                     /gene="IL22"
                     /gene_synonym="IL-21; IL-22; IL-D110; IL-TIF; ILTIF; TIFa;
                     TIFIL-23; zcyto18"
                     /coded_by="NM_020525.5:69..608"
                     /db_xref="CCDS:CCDS8982.1"
                     /db_xref="GeneID:50616"
                     /db_xref="HGNC:HGNC:14900"
                     /db_xref="MIM:605330"
ORIGIN      
        1 maalqksvss flmgtlatsc llllallvqg gaaapisshc rldksnfqqp yitnrtfmla
       61 keasladnnt dvrligeklf hgvsmsercy lmkqvlnftl eevlfpqsdr fqpymqevvp
      121 flarlsnrls tchiegddlh iqrnvqklkd tvkklgesge ikaigeldll fmslrnaci
//
LOCUS       NP_001350058            1198 aa            linear   ROD 27-APR-2025
DEFINITION  integrator complex subunit 2 isoform 2 [Mus musculus].
ACCESSION   NP_001350058 XP_006534245
VERSION     NP_001350058.1
DBSOURCE    REFSEQ: accession NM_001363129.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1198)
  AUTHORS   Alvarez-Dominguez,J.R., Zhang,X. and Hu,W.
  TITLE     Widespread and dynamic translational control of red blood cell
            development
  JOURNAL   Blood 129 (5), 619-629 (2017)
   PUBMED   27899360
REFERENCE   4  (residues 1 to 1198)
  AUTHORS   Tkatchenko,T.V., Moreno-Rodriguez,R.A., Conway,S.J.,
            Molkentin,J.D., Markwald,R.R. and Tkatchenko,A.V.
  TITLE     Lack of periostin leads to suppression of Notch1 signaling and
            calcific aortic valve disease
  JOURNAL   Physiol Genomics 39 (3), 160-168 (2009)
   PUBMED   19723774
REFERENCE   5  (residues 1 to 1198)
  AUTHORS   Baillat,D., Hakimi,M.A., Naar,A.M., Shilatifard,A., Cooch,N. and
            Shiekhattar,R.
  TITLE     Integrator, a multiprotein mediator of small nuclear RNA
            processing, associates with the C-terminal repeat of RNA polymerase
            II
  JOURNAL   Cell 123 (2), 265-276 (2005)
   PUBMED   16239144
  REMARK    GeneRIF: characterization of the human Integrator complex
REFERENCE   6  (residues 1 to 1198)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Kitamura,H., Nakagawa,T., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of FLJ
            genes: the complete nucleotide sequences of 110 mouse
            FLJ-homologous cDnas identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (2), 127-135 (2004)
   PUBMED   15449545
REFERENCE   7  (residues 1 to 1198)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   8  (residues 1 to 1198)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL592065.7.
            
            On May 9, 2018 this sequence version replaced XP_006534245.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.121048.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 51.71 cM"
     Protein         1..1198
                     /product="integrator complex subunit 2 isoform 2"
                     /note="int2"
                     /calculated_mol_wt=133385
     Region          27..1131
                     /region_name="INTS2"
                     /note="Integrator complex subunit 2; pfam14750"
                     /db_xref="CDD:464296"
     Site            421..437
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80UK8.2)"
     CDS             1..1198
                     /gene="Ints2"
                     /gene_synonym="2810417D08Rik; mKIAA1287"
                     /coded_by="NM_001363129.1:1170..4766"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS25198.1"
                     /db_xref="GeneID:70422"
                     /db_xref="MGI:MGI:1917672"
ORIGIN      
        1 mtpegtglqf vspfafeamq kvdvvrlasl sdpelrlllp clvrmalcap adqsqswaqd
       61 kklilrllsg veavnsival lsvdfhaleq daskeqqlrh klgggsgesi lvsqlqhglt
      121 lefehsdspr rlrlvlsell aimnkvsecn gefffkssel fesavyleea advlcilqae
      181 lpsllpivdv aeallrvrng awflcllvan vpdsfnevcr glikngerqd eeslggrrrt
      241 dalrflcrmn psqalkvrgm vveechlpgl gvaltldhtk teacedgvsd lvcfvsglll
      301 gtnakvrtwf gtfirngqqr kretsgsvlw qmrrqlllel mgilptvrst riveeadvem
      361 eptvsvysgl keehvvkasa llrlycalmg iaglkpteee aeqllqlmts rppatpagvr
      421 fvslsfcmll afstlvstpe qeqlmvlwls wmikeeayfe stsgvsasfg emlllvamyf
      481 hsnqlsaiid lvcstlgmki vikpsslsrm ktiftqeift eqvvtahavr vpvtsnlsan
      541 itgflpihci yqllrsrsft khkvsikdwi yrqlcetstp lhpqllplid vyinsiltpa
      601 sksnpeatnq pvteqeilnl fqeviggdsv rltqrfsita qllvlyyils yeeallantk
      661 tlasmqrkpk syssslmdqi pikflirqaq glqqelgglh sallrllatn yphlcivddw
      721 iceeeitgtd allrrmllts nakthspkql qeafsavpvs htqvmqimeh ltllsaseli
      781 pyaevltsnm nqllnsgvpr rilqtvnklw mvlntvmprr lwvmtvnalq psikfirqqk
      841 ytqndlmidp livlrcdrrv hrcpplmdvt lhmlngylla skaylsahlk etaeqdrpsp
      901 nntvglvgqt dapevtreel knallaaqds aavqilleic lpteeekakg ansdislrnt
      961 qgvttistps keteegednl lcnlrevqcl iccllhqmyi adpniaklvh fqgypcellp
     1021 ltvagipsmh icldfipeli aqpelekqif aiqllshlci qyalpkslsv arlavnvmgt
     1081 lltvltqakr ysffmptlps lvsfcrafpp lyedimslli qigqvcasdv atqtrdidpi
     1141 itrlqqikek psgwsqickd psykngsrdt gsmdpdvqlc hciestiiei inmsvsgi
//
LOCUS       NP_060903               1321 aa            linear   PRI 27-APR-2025
DEFINITION  lysine-specific demethylase 3A [Homo sapiens].
ACCESSION   NP_060903
VERSION     NP_060903.2
DBSOURCE    REFSEQ: accession NM_018433.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1321)
  AUTHORS   VON Fournier,A., Wilhelm,C., Tirtey,C., Stoth,M., Kasemo,T.E.,
            Hackenberg,S. and Scherzad,A.
  TITLE     Impact of Hypoxia and the Levels of Transcription Factor HIF-1alpha
            and JMJD1A on Epithelial-Mesenchymal Transition in Head and Neck
            Squamous Cell Carcinoma Cell Lines
  JOURNAL   Cancer Genomics Proteomics 21 (6), 591-607 (2024)
   PUBMED   39467631
  REMARK    GeneRIF: Impact of Hypoxia and the Levels of Transcription Factor
            HIF-1alpha and JMJD1A on Epithelial-Mesenchymal Transition in Head
            and Neck Squamous Cell Carcinoma Cell Lines.
REFERENCE   2  (residues 1 to 1321)
  AUTHORS   Han,Y., Maimaiti,N., Sun,Y. and Yao,J.
  TITLE     Knockout of KDM3A in MDA-MB-231 breast cancer cells inhibits tumor
            malignancy and promotes apoptosis
  JOURNAL   J Mol Histol 55 (1), 139-148 (2024)
   PUBMED   38165573
  REMARK    GeneRIF: Knockout of KDM3A in MDA-MB-231 breast cancer cells
            inhibits tumor malignancy and promotes apoptosis.
REFERENCE   3  (residues 1 to 1321)
  AUTHORS   Monte-Serrano,E., Morejon-Garcia,P., Campillo-Marcos,I.,
            Campos-Diaz,A., Navarro-Carrasco,E. and Lazo,P.A.
  TITLE     The pattern of histone H3 epigenetic posttranslational
            modifications is regulated by the VRK1 chromatin kinase
  JOURNAL   Epigenetics Chromatin 16 (1), 18 (2023)
   PUBMED   37179361
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1321)
  AUTHORS   Yang,L., Zhang,Q. and Yang,Q.
  TITLE     KDM3A promotes oral squamous cell carcinoma cell proliferation and
            invasion via H3K9me2 demethylation-activated DCLK1
  JOURNAL   Genes Genomics 44 (11), 1333-1342 (2022)
   PUBMED   36094735
  REMARK    GeneRIF: KDM3A promotes oral squamous cell carcinoma cell
            proliferation and invasion via H3K9me2 demethylation-activated
            DCLK1.
REFERENCE   5  (residues 1 to 1321)
  AUTHORS   Li,C., Zhang,A., Hu,T., Yang,Y., Tang,S. and Li,J.
  TITLE     Histone demethylase JHDM2A participates in the repair of
            arsenic-induced DNA damage in L-02 cells by regulating DDB2
  JOURNAL   Toxicol Ind Health 38 (6), 365-376 (2022)
   PUBMED   35579678
  REMARK    GeneRIF: Histone demethylase JHDM2A participates in the repair of
            arsenic-induced DNA damage in L-02 cells by regulating DDB2.
REFERENCE   6  (residues 1 to 1321)
  AUTHORS   Tateishi,K., Okada,Y., Kallin,E.M. and Zhang,Y.
  TITLE     Role of Jhdm2a in regulating metabolic gene expression and obesity
            resistance
  JOURNAL   Nature 458 (7239), 757-761 (2009)
   PUBMED   19194461
REFERENCE   7  (residues 1 to 1321)
  AUTHORS   Beyer,S., Kristensen,M.M., Jensen,K.S., Johansen,J.V. and
            Staller,P.
  TITLE     The histone demethylases JMJD1A and JMJD2B are transcriptional
            targets of hypoxia-inducible factor HIF
  JOURNAL   J Biol Chem 283 (52), 36542-36552 (2008)
   PUBMED   18984585
  REMARK    GeneRIF: histone demethylases JMJD1A and JMJD2B are transcriptional
            targets of hypoxia-inducible factor HIF
REFERENCE   8  (residues 1 to 1321)
  AUTHORS   Pollard,P.J., Loenarz,C., Mole,D.R., McDonough,M.A., Gleadle,J.M.,
            Schofield,C.J. and Ratcliffe,P.J.
  TITLE     Regulation of Jumonji-domain-containing histone demethylases by
            hypoxia-inducible factor (HIF)-1alpha
  JOURNAL   Biochem J 416 (3), 387-394 (2008)
   PUBMED   18713068
  REMARK    GeneRIF: Results show that many genes regulated by hypoxia and
            HIF-1alpha show patterns of induction with JMJD (Jumonji-domain
            containing)1A and JMJD2B demonstrating robust, and JMJD2C more
            modest, up-regulation by hypoxia.
REFERENCE   9  (residues 1 to 1321)
  AUTHORS   Wellmann,S., Bettkober,M., Zelmer,A., Seeger,K., Faigle,M.,
            Eltzschig,H.K. and Buhrer,C.
  TITLE     Hypoxia upregulates the histone demethylase JMJD1A via HIF-1
  JOURNAL   Biochem Biophys Res Commun 372 (4), 892-897 (2008)
   PUBMED   18538129
  REMARK    GeneRIF: These findings demonstrate that JMJD1A can be stimulated
            by hypoxia both in vitro and in vivo involving binding of HIF-1 to
            a specific HRE in the JMJD1A promoter.
REFERENCE   10 (residues 1 to 1321)
  AUTHORS   Yamane,K., Toumazou,C., Tsukada,Y., Erdjument-Bromage,H.,
            Tempst,P., Wong,J. and Zhang,Y.
  TITLE     JHDM2A, a JmjC-containing H3K9 demethylase, facilitates
            transcription activation by androgen receptor
  JOURNAL   Cell 125 (3), 483-495 (2006)
   PUBMED   16603237
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB087171.1, BX647271.1,
            AB018285.2 and BX648841.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 30, 2002 this sequence version replaced NP_060903.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038297.2, BX640698.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312912.10/ ENSP00000323659.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..1321
                     /product="lysine-specific demethylase 3A"
                     /EC_number="1.14.11.65"
                     /note="testis-specific protein A; jumonji C
                     domain-containing histone demethylase 2A; jumonji
                     domain-containing protein 1A; jmjC domain-containing
                     histone demethylation protein 2A; lysine (K)-specific
                     demethylase 3A; [histone H3]-dimethyl-L-lysine(9)
                     demethylase 3A"
                     /calculated_mol_wt=147211
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C1.4)"
     Region          307..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4C1.4)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C1.4)"
     Region          383..402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4C1.4)"
     Region          438..472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4C1.4)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C1.4)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C1.4)"
     Region          885..889
                     /region_name="LXXLL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4C1.4)"
     Site            895
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4C1.4)"
     Region          1064..1134
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1151..1264
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     CDS             1..1321
                     /gene="KDM3A"
                     /gene_synonym="JHDM2A; JHMD2A; JMJD1; JMJD1A; TSGA"
                     /coded_by="NM_018433.6:105..4070"
                     /db_xref="CCDS:CCDS1990.1"
                     /db_xref="GeneID:55818"
                     /db_xref="HGNC:HGNC:20815"
                     /db_xref="MIM:611512"
ORIGIN      
        1 mvltlgeswp vlvgrrflsl saadgsdgsh dswdvervae wpwlsgtira vshtdvtkkd
       61 lkvcvefdge swrkrrwiev ysllrraflv ehnlvlaerk speiserivq wpaitykpll
      121 dkaglgsits vrflgdqqrv flskdllkpi qdvnslrlsl tdnqivskef qalivkhlde
      181 shllkgdknl vgsevkiysl dpstqwfsat vingnpaskt lqvnceeipa lkivdpslih
      241 vevvhdnlvt cgnsarigav krkssenngt lvskqakscs easpsmcpvq svpttvfkei
      301 llgctaatpp skdprqqstp qaansppnlg akipqgchkq slpeeisscl ntksealrtk
      361 pdvckaglls kssqigtgdl kiltepkgsc tqpktntdqe nrlesvpqal tglpkeclpt
      421 kasskaelei anppelqkhl ehapspsdvs napevkagvn sdspnncsgk kvepsalacr
      481 sqnlkessvk vdnesccsrs nnkiqnapsr ksvltdpakl kklqqsgeaf vqddscvniv
      541 aqlpkcrecr ldslrkdkeq qkdspvfcrf fhfrrlqfnk hgvlrvegfl tpnkydneai
      601 glwlpltknv vgidldtaky ilanigdhfc qmvisekeam stiephrqva wkravkgvre
      661 mcdvcdttif nlhwvcprcg fgvcvdcyrm krkncqqgaa yktfswlkcv ksqihepenl
      721 mptqiipgka lydvgdivhs vrakwgikan cpcsnrqfkl fskpaskedl kqtslagekp
      781 tlgavlqqnp svlepaavgg eaaskpagsm kpacpastsp lnwladltsg nvnkenkekq
      841 ptmpilknei kclpplppls ksstvlhtfn stiltpvsnn nsgflrnlln sstgktengl
      901 kntpkilddi faslvqnktt sdlskrpqgl tikpsilgfd tphywlcdnr llclqdpnnk
      961 snwnvfrecw kqgqpvmvsg vhhklnselw kpesfrkefg eqevdlvncr tneiitgatv
     1021 gdfwdgfedv pnrlknekep mvlklkdwpp gedfrdmmps rfddlmanip lpeytrrdgk
     1081 lnlasrlpny fvrpdlgpkm ynayglitpe drkygttnlh ldvsdaanvm vyvgipkgqc
     1141 eqeeevlkti qdgdsdelti krfiegkekp galwhiyaak dtekireflk kvseeqgqen
     1201 padhdpihdq swyldrslrk rlhqeygvqg waivqflgdv vfipagaphq vhnlyscikv
     1261 aedfvspehv khcfwltqef rylsqthtnh edklqvknvi yhavkdavam lkasessfgk
     1321 p
//
LOCUS       NP_001346231             632 aa            linear   ROD 27-APR-2025
DEFINITION  2-hydroxyacyl-CoA lyase 2 isoform 2 [Mus musculus].
ACCESSION   NP_001346231
VERSION     NP_001346231.1
DBSOURCE    REFSEQ: accession NM_001359302.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Rhein,S., Costalunga,R., Inderhees,J., Gurtzgen,T., Faupel,T.C.,
            Shaheryar,Z., Arrulo Pereira,A., Othman,A., Begemann,K., Binder,S.,
            Stolting,I., Dorta,V., Nawroth,P.P., Fleming,T., Oexle,K.,
            Prevot,V., Nogueiras,R., Meyhofer,S., Meyhofer,S.M. and
            Schwaninger,M.
  TITLE     The reactive pyruvate metabolite dimethylglyoxal mediates
            neurological consequences of diabetes
  JOURNAL   Nat Commun 15 (1), 5745 (2024)
   PUBMED   38987239
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Mori,K., Naganuma,T. and Kihara,A.
  TITLE     Role of 2-hydroxy acyl-CoA lyase HACL2 in odd-chain fatty acid
            production via alpha-oxidation in vivo
  JOURNAL   Mol Biol Cell 34 (9), ar85 (2023)
   PUBMED   37285239
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Liu,S., Lu,S., Xu,R., Atzberger,A., Gunther,S., Wettschureck,N. and
            Offermanns,S.
  TITLE     Members of Bitter Taste Receptor Cluster Tas2r143/Tas2r135/Tas2r126
            Are Expressed in the Epithelium of Murine Airways and Other
            Non-gustatory Tissues
  JOURNAL   Front Physiol 8, 849 (2017)
   PUBMED   29163195
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Wiltshire,T., Pletcher,M., Cole,S.E., Villanueva,M., Birren,B.,
            Lehoczky,J., Dewar,K. and Reeves,R.H.
  TITLE     Perfect conserved linkage across the entire mouse chromosome 10
            region homologous to human chromosome 21
  JOURNAL   Genome Res 9 (12), 1214-1222 (1999)
   PUBMED   10613844
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK133553.1, AK146075.1 and AI842669.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660813.245691.1, AK146075.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 39.72 cM"
     Protein         1..632
                     /product="2-hydroxyacyl-CoA lyase 2 isoform 2"
                     /EC_number="2.2.1.-"
                     /note="acetolactate synthase-like protein; ilvB-like
                     protein; 2-hydroxyacyl-CoA lyase 2"
                     /calculated_mol_wt=68025
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BU33.1)"
     Region          52..624
                     /region_name="IlvB"
                     /note="Acetolactate synthase large subunit or other
                     thiamine pyrophosphate-requiring enzyme [Amino acid
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0028"
                     /db_xref="CDD:439799"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BU33.1)"
     Region          470..550
                     /region_name="Thiamine pyrophosphate binding.
                     /evidence=ECO:0000250|UniProtKB:P40149"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BU33.1)"
     CDS             1..632
                     /gene="Ilvbl"
                     /gene_synonym="5830463I21"
                     /coded_by="NM_001359302.1:107..2005"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS23966.1"
                     /db_xref="GeneID:216136"
                     /db_xref="MGI:MGI:1351911"
ORIGIN      
        1 metsaaaasa ggffpsflll afgtlvaavl gvahrlglfy qlmhkvdkts irhggesvaa
       61 vlrahgvrfv ftlvgghisp llvaceklgi rvvdtrhevt avfaadavar ltgtvgvaav
      121 tagpgltntv tavknaqvaq spvlllggaa stllqkrgal qaidqmslfr plckfcasvr
      181 rvrdivptlr taiaaaqsgt pgpvfvelpl dvlypyfmve kemiptklpn slmgrvvvwy
      241 lqnclanlfv gaweprpegp lpldipqasp qqvqrcveil srakrpllvl gsqallpptp
      301 anklraavet lgvpcflggm srgllgrnhp lhirqnrsaa lkkadvvvla gavcdfrlsy
      361 grvlnrkssi iivnrnrddl llnsdifwkp qeavqgdvgs fmiklveglq gqmwssdwae
      421 elrkadqqke qtyrdkalmp vlqhlnpvwv lqqveetlpd nallvvdggd fvataaylvq
      481 prgplrwldp gafgtlgvga gfalgaklcq peaevwclfg dgafgyslie fdtfvrhkvp
      541 vialvgndag wtqisreqvp rlgsdvacsl aytdyhkaam glgaqglils rdnkdqvvkv
      601 lregqqlcqd ghavvvnili grtdfrdgsi sv
//
LOCUS       NP_057287                569 aa            linear   PRI 27-APR-2025
DEFINITION  5'-AMP-activated protein kinase subunit gamma-2 isoform a [Homo
            sapiens].
ACCESSION   NP_057287
VERSION     NP_057287.2
DBSOURCE    REFSEQ: accession NM_016203.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   van der Steld,L.P., Rocha,M.S., Ladeia,A.M.T., Livramento,H.L.,
            Campos,G.B., Darrieux,F.C.D.C., Campuzano,O. and Brugada,R.
  TITLE     PRKAG2 syndrome, a rare hypertrophic cardiomyopathy: a Brazilian
            long-term follow-up with extracardiac disorders
  JOURNAL   Einstein (Sao Paulo) 22, eAO0549 (2024)
   PUBMED   39082507
  REMARK    GeneRIF: PRKAG2 syndrome, a rare hypertrophic cardiomyopathy: a
            Brazilian long-term follow-up with extracardiac disorders.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Braverman,E.L., McQuaid,M.A., Schuler,H., Qin,M., Hani,S.,
            Hippen,K., Monlish,D.A., Dobbs,A.K., Ramsey,M.J., Kemp,F.,
            Wittmann,C., Ramgopal,A., Brown,H., Blazar,B. and Byersdorfer,C.A.
  TITLE     Overexpression of AMPKgamma2 increases AMPK signaling to augment
            human T cell metabolism and function
  JOURNAL   J Biol Chem 300 (1), 105488 (2024)
   PUBMED   38000657
  REMARK    GeneRIF: Overexpression of AMPKgamma2 increases AMPK signaling to
            augment human T cell metabolism and function.
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Song,X.W., Su,T., Li,B., Huang,Y.J., He,W.X., Jiang,L.L., Li,C.J.,
            Huang,S.Q., Li,S.H., Guo,Z.F., Wu,H. and Zhang,B.L.
  TITLE     Abnormal expression of PRKAG2-AS results in dysfunction of
            cardiomyocytes through regulating PRKAG2 transcription by
            interacting with PPARG
  JOURNAL   Clin Epigenetics 15 (1), 178 (2023)
   PUBMED   37932845
  REMARK    GeneRIF: Abnormal expression of PRKAG2-AS results in dysfunction of
            cardiomyocytes through regulating PRKAG2 transcription by
            interacting with PPARG.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Janin,A., Gouy,E., Putoux,A., Perouse-de-Monclos,T., Chevalier,P.,
            Faucherre,A., Mancilla Abaroa,J., Jopling,C., Collardeau
            Frachon,S., Radojevic,J., El Chehadeh,S. and Millat,G.
  TITLE     Biallelic PRKAG2 Truncating Variants Are Associated with Severe
            Neonatal Cardiomyopathies
  JOURNAL   Circ Genom Precis Med 16 (3), 277-279 (2023)
   PUBMED   37013823
  REMARK    GeneRIF: Biallelic PRKAG2 Truncating Variants Are Associated with
            Severe Neonatal Cardiomyopathies.
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Maron,B.J. and Maron,M.S.
  TITLE     PRKAG2 Glycogen Storage Disease Cardiomyopathy: Out of the Darkness
            and Into the Light
  JOURNAL   J Am Coll Cardiol 76 (2), 198-200 (2020)
   PUBMED   32646570
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Gollob,M.H., Green,M.S., Tang,A.S., Gollob,T., Karibe,A., Ali
            Hassan,A.S., Ahmad,F., Lozado,R., Shah,G., Fananapazir,L.,
            Bachinski,L.L. and Roberts,R.
  TITLE     Identification of a gene responsible for familial
            Wolff-Parkinson-White syndrome
  JOURNAL   N Engl J Med 344 (24), 1823-1831 (2001)
   PUBMED   11407343
  REMARK    Erratum:[N Engl J Med 2001 Aug 16;345(7):552. Hassan AS [corrected
            to Ali Hassan AS]]
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Blair,E., Redwood,C., Ashrafian,H., Oliveira,M., Broxholme,J.,
            Kerr,B., Salmon,A., Ostman-Smith,I. and Watkins,H.
  TITLE     Mutations in the gamma(2) subunit of AMP-activated protein kinase
            cause familial hypertrophic cardiomyopathy: evidence for the
            central role of energy compromise in disease pathogenesis
  JOURNAL   Hum Mol Genet 10 (11), 1215-1220 (2001)
   PUBMED   11371514
REFERENCE   8  (residues 1 to 569)
  AUTHORS   MacRae,C.A., Ghaisas,N., Kass,S., Donnelly,S., Basson,C.T.,
            Watkins,H.C., Anan,R., Thierfelder,L.H., McGarry,K., Rowland,E. et
            al.
  TITLE     Familial Hypertrophic cardiomyopathy with Wolff-Parkinson-White
            syndrome maps to a locus on chromosome 7q3
  JOURNAL   J Clin Invest 96 (3), 1216-1220 (1995)
   PUBMED   7657794
REFERENCE   9  (residues 1 to 569)
  AUTHORS   Hofmann,B., Nishanian,P., Nguyen,T., Insixiengmay,P. and Fahey,J.L.
  TITLE     Human immunodeficiency virus proteins induce the inhibitory
            cAMP/protein kinase A pathway in normal lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6676-6680 (1993)
   PUBMED   7688126
REFERENCE   10 (residues 1 to 569)
  AUTHORS   Hofmann,B., Nishanian,P., Baldwin,R.L., Insixiengmay,P., Nel,A. and
            Fahey,J.L.
  TITLE     HIV inhibits the early steps of lymphocyte activation, including
            initiation of inositol phospholipid metabolism
  JOURNAL   J Immunol 145 (11), 3699-3705 (1990)
   PUBMED   1978848
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA123009.1, AJ249976.1 and
            BC020540.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 24, 2003 this sequence version replaced NP_057287.1.
            
            Summary: AMP-activated protein kinase (AMPK) is a heterotrimeric
            protein composed of a catalytic alpha subunit, a noncatalytic beta
            subunit, and a noncatalytic regulatory gamma subunit. Various forms
            of each of these subunits exist, encoded by different genes. AMPK
            is an important energy-sensing enzyme that monitors cellular energy
            status and functions by inactivating key enzymes involved in
            regulating de novo biosynthesis of fatty acid and cholesterol. This
            gene is a member of the AMPK gamma subunit family. Mutations in
            this gene have been associated with Wolff-Parkinson-White syndrome,
            familial hypertrophic cardiomyopathy, and glycogen storage disease
            of the heart. Alternate transcriptional splice variants, encoding
            different isoforms, have been characterized. [provided by RefSeq,
            Jan 2015].
            
            Transcript Variant: This variant (a) represents the longest
            transcript and encodes the longest isoform (a, also referred to as
            PRKAG2-a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.43012.1,
                                           SRR1803617.91844.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287878.9/ ENSP00000287878.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..569
                     /product="5'-AMP-activated protein kinase subunit gamma-2
                     isoform a"
                     /note="5'-AMP-activated protein kinase subunit gamma-2;
                     AMPK subunit gamma-2; protein kinase, AMP-activated, gamma
                     2 non-catalytic subunit; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=62935
     Region          1..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Region          46..>221
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WG5; propagated from
                     UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WG5; propagated from
                     UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WG5; propagated from
                     UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WG5; propagated from
                     UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WG5; propagated from
                     UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WG5; propagated from
                     UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WG5; propagated from
                     UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q91WG5; propagated from
                     UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WG5; propagated from
                     UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Region          269..406
                     /region_name="CBS_euAMPK_gamma-like_repeat1"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains found in AMP-activated
                     protein kinase gamma-like proteins, repeat 1; cd04618"
                     /db_xref="CDD:341388"
     Site            order(277,279..281,303..305,384,398,400,402..403,406)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341388"
     Region          277..350
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341388"
     Site            order(303,317,321..322,325,362,384..386,402)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341388"
     Region          362..406
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341388"
     Region          370..391
                     /region_name="AMPK pseudosubstrate"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGJ0.1)"
     Region          432..555
                     /region_name="CBS_euAMPK_gamma-like_repeat2"
                     /note="CBS pair domain found in 5'-AMP (adenosine
                     monophosphate)-activated protein kinase; cd04641"
                     /db_xref="CDD:341399"
     Site            order(433,435..437,459..461,531,544,546,548..549,552)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341399"
     Region          433..498
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341399"
     Site            order(459,472,476..477,480,509,531..533,548)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341399"
     Region          509..552
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341399"
     CDS             1..569
                     /gene="PRKAG2"
                     /gene_synonym="AAKG; AAKG2; CMH6; H91620p; WPWS"
                     /coded_by="NM_016203.4:496..2205"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5928.1"
                     /db_xref="GeneID:51422"
                     /db_xref="HGNC:HGNC:9386"
                     /db_xref="MIM:602743"
ORIGIN      
        1 mgsavmdtkk kkdvsspggs ggkknasqkr rslrvhipdl ssfamplldg dlegsgkhss
       61 rkvdspfgpg spskgffsrg pqprpsspms apvrpktspg spktvfpfsy qespprsprr
      121 msfsgifrss skesspnsnp atspggirff srsrktsgls sspstptqvt kqhtfplesy
      181 kheperlenr iyasssppdt gqrfcpssfq sptrpplasp thyapskaaa laaalgpaea
      241 gmleklefed eavedsesgv ymrfmrshkc ydivptsskl vvfdttlqvk kaffalvang
      301 vraaplwesk kqsfvgmlti tdfinilhry ykspmvqiye leehkietwr elylqetfkp
      361 lvnispdasl fdavyslikn kihrlpvidp isgnalyilt hkrilkflql fmsdmpkpaf
      421 mkqnldelgi gtyhniafih pdtpiikaln ifverrisal pvvdesgkvv diyskfdvin
      481 laaektynnl ditvtqalqh rsqyfegvvk cnkleileti vdrivraevh rlvvvneads
      541 ivgiislsdi lqaliltpag akqketete
//
LOCUS       NP_699160                802 aa            linear   PRI 27-APR-2025
DEFINITION  aldehyde dehydrogenase family 16 member A1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_699160
VERSION     NP_699160.2
DBSOURCE    REFSEQ: accession NM_153329.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Vasiliou,V., Sandoval,M., Backos,D.S., Jackson,B.C., Chen,Y.,
            Reigan,P., Lanaspa,M.A., Johnson,R.J., Koppaka,V. and Thompson,D.C.
  TITLE     ALDH16A1 is a novel non-catalytic enzyme that may be involved in
            the etiology of gout via protein-protein interactions with HPRT1
  JOURNAL   Chem Biol Interact 202 (1-3), 22-31 (2013)
   PUBMED   23348497
  REMARK    GeneRIF: Both the short and long forms of human ALDH16A1 protein
            would lack catalytic activity.
REFERENCE   5  (residues 1 to 802)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 802)
  AUTHORS   Hanna,M.C. and Blackstone,C.
  TITLE     Interaction of the SPG21 protein ACP33/maspardin with the aldehyde
            dehydrogenase ALDH16A1
  JOURNAL   Neurogenetics 10 (3), 217-228 (2009)
   PUBMED   19184135
  REMARK    GeneRIF: Data report that maspardin localizes prominently to
            cytoplasm as well as to membranes, possibly at trans-Golgi
            network/late endosomal compartments, and that maspardin interacts
            with the aldehyde dehydrogenase ALDH16A1.
REFERENCE   7  (residues 1 to 802)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA629821.1, BC014895.2,
            DC364604.1, AK297101.1, AY007096.1 and AC010619.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 24, 2009 this sequence version replaced NP_699160.1.
            
            Summary: This gene encodes a member of the aldehyde dehydrogenase
            superfamily. The family members act on aldehyde substrates and use
            nicotinamide adenine dinucleotide phosphate (NADP) as a cofactor.
            This gene is conserved in chimpanzee, dog, cow, mouse, rat, and
            zebrafish. The protein encoded by this gene interacts with
            maspardin, a protein that when truncated is responsible for Mast
            syndrome. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Apr 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.139915.1, BC014895.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000293350.9/ ENSP00000293350.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..802
                     /product="aldehyde dehydrogenase family 16 member A1
                     isoform 1"
                     /note="aldehyde dehydrogenase family 16 member A1"
                     /calculated_mol_wt=84997
     Region          19..492
                     /region_name="ALDH-SF"
                     /note="NAD(P)+-dependent aldehyde dehydrogenase
                     superfamily; cl11961"
                     /db_xref="CDD:448367"
     Site            order(172..176,184,199,201..202,248..251,254,257..258,
                     272..274,305,398,400,426,464)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143395"
     Region          525..>767
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
     CDS             1..802
                     /gene="ALDH16A1"
                     /coded_by="NM_153329.4:108..2516"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12766.1"
                     /db_xref="GeneID:126133"
                     /db_xref="HGNC:HGNC:28114"
                     /db_xref="MIM:613358"
ORIGIN      
        1 maatragpra reiftsleyg pvpeshacal awldtqdrcl ghyvngkwlk pehrnsvpcq
       61 dpitgenlas clqaqaedva aaveaarmaf kgwsahpgvv raqhltrlae viqkhqrllw
      121 tleslvtgra vrevrdgdvq laqqllhyha iqastqeeal agwepmgvig lilpptfsfl
      181 emmwricpal avgctvvalv ppaspaplll aqlagelgpf pgilnvlsgp aslvpilasq
      241 pgirkvafcg apeegralrr slagecaelg lalgteslll ltdtadvdsa vegvvdaaws
      301 drgpgglrll iqesvwdeam rrlqermgrl rsgrgldgav dmgargaaac dlvqrfvrea
      361 qsqgaqvfqa gdvpserpfy pptlvsnlpp aspcaqvevp wpvvvaspfr takeallvan
      421 gtprggsasv wserlgqale lgyglqvgtv winahglrdp svptggckes gcswhggpdg
      481 lyeylrpsgt parlsclskn lnydtfglav pstlpagpei gpspappygl fvggrfqapg
      541 arssrpirds sgnlhgyvae ggakdirgav eaahqafpgw agqspgaraa llwalaaale
      601 rrkstlasrl erqgaelkaa eaevelsarr lrawgarvqa qghtlqvagl rgpvlrlrep
      661 lgvlavvcpd ewpllafvsl lapalaygnt vvmvpsaacp llalevcqdm atvfpaglan
      721 vvtgdrdhlt rclalhqdvq amwyfgsaqg sqfvewasag nlkpvwasrg cprawdqeae
      781 gagpelglrv artkalwlpm gd
//
LOCUS       NP_037524                535 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear receptor-binding protein isoform 1 [Homo sapiens].
ACCESSION   NP_037524
VERSION     NP_037524.1
DBSOURCE    REFSEQ: accession NM_013392.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Zhang,A., Peng,S., Sun,S., Ye,S., Zhao,Y. and Wu,Q.
  TITLE     NRBP1 promotes malignant phenotypes of glioblastoma by regulating
            PI3K/Akt activation
  JOURNAL   Cancer Med 13 (16), e70100 (2024)
   PUBMED   39149873
  REMARK    GeneRIF: NRBP1 promotes malignant phenotypes of glioblastoma by
            regulating PI3K/Akt activation.
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Cao,C., Sun,G., Le,K., Xu,Q. and Liu,C.
  TITLE     The Circular RNA Circ_0085494 Regulates Prostate Cancer Progression
            Through NRBP1/miR-497-5p Axis
  JOURNAL   Biochem Genet 61 (5), 1775-1790 (2023)
   PUBMED   36790665
  REMARK    GeneRIF: The Circular RNA Circ_0085494 Regulates Prostate Cancer
            Progression Through NRBP1/miR-497-5p Axis.
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Yang,X., Cruz,M.I., Nguyen,E.V., Huang,C., Schittenhelm,R.B.,
            Luu,J., Cowley,K.J., Shin,S.Y., Nguyen,L.K., Lim Kam Sian,T.C.C.,
            Clark,K.C., Simpson,K.J., Ma,X. and Daly,R.J.
  TITLE     The pseudokinase NRBP1 activates Rac1/Cdc42 via P-Rex1 to drive
            oncogenic signalling in triple-negative breast cancer
  JOURNAL   Oncogene 42 (11), 833-847 (2023)
   PUBMED   36693952
  REMARK    GeneRIF: The pseudokinase NRBP1 activates Rac1/Cdc42 via P-Rex1 to
            drive oncogenic signalling in triple-negative breast cancer.
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Qin,L., Sun,X., Zhou,F. and Liu,C.
  TITLE     CircLRP6 contributes to prostate cancer growth and metastasis by
            binding to miR-330-5p to up-regulate NRBP1
  JOURNAL   World J Surg Oncol 19 (1), 184 (2021)
   PUBMED   34158077
  REMARK    GeneRIF: CircLRP6 contributes to prostate cancer growth and
            metastasis by binding to miR-330-5p to up-regulate NRBP1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Chua,J.J., Ng,M.M. and Chow,V.T.
  TITLE     The non-structural 3 (NS3) protein of dengue virus type 2 interacts
            with human nuclear receptor binding protein and is associated with
            alterations in membrane structure
  JOURNAL   Virus Res 102 (2), 151-163 (2004)
   PUBMED   15084397
  REMARK    GeneRIF: NS3 protein of dengue virus type 2 interacted specifically
            with nuclear receptor binding protein, a host cellular protein that
            influences trafficking between the endoplasmic reticulum and Golgi,
            and that interacts with Rac3
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Lim,R., Winteringham,L.N., Williams,J.H., McCulloch,R.K.,
            Ingley,E., Tiao,J.Y., Lalonde,J.P., Tsai,S., Tilbrook,P.A., Sun,Y.,
            Wu,X., Morris,S.W. and Klinken,S.P.
  TITLE     MADM, a novel adaptor protein that mediates phosphorylation of the
            14-3-3 binding site of myeloid leukemia factor 1
  JOURNAL   J Biol Chem 277 (43), 40997-41008 (2002)
   PUBMED   12176995
  REMARK    GeneRIF: mediates phosphorylation of the 14-3-3 binding site of
            myeloid leukemia factor 1
REFERENCE   8  (residues 1 to 535)
  AUTHORS   De Langhe,S., Haataja,L., Senadheera,D., Groffen,J. and
            Heisterkamp,N.
  TITLE     Interaction of the small GTPase Rac3 with NRBP, a protein with a
            kinase-homology domain
  JOURNAL   Int J Mol Med 9 (5), 451-459 (2002)
   PUBMED   11956649
  REMARK    GeneRIF: Interaction of the small GTPase Rac3 with NRBP: results
            suggest that NRBP functions in subcellular trafficking and may be
            directed to specific subcellular locations through interaction with
            small GTPases of the Rho family
REFERENCE   9  (residues 1 to 535)
  AUTHORS   Hooper,J.D., Baker,E., Ogbourne,S.M., Sutherland,G.R. and
            Antalis,T.M.
  TITLE     Cloning of the cDNA and localization of the gene encoding human
            NRBP, a ubiquitously expressed, multidomain putative adapter
            protein
  JOURNAL   Genomics 66 (1), 113-118 (2000)
   PUBMED   10843813
REFERENCE   10 (residues 1 to 535)
  AUTHORS   Martinez,P.
  TITLE     [A nurse with the drug addicts]
  JOURNAL   Rev Infirm 26 (7), 557-562 (1976)
   PUBMED   1048605
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ949042.1 and BC001221.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1162419.1, AF113249.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379852.8/ ENSP00000369181.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..535
                     /product="nuclear receptor-binding protein isoform 1"
                     /note="myeloid leukemia factor 1 adaptor molecule;
                     multiple domain putative nuclear protein; nuclear
                     receptor-binding protein"
                     /calculated_mol_wt=59714
     Region          1..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHY1.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9UHY1.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UHY1.1)"
     Region          60..334
                     /region_name="PK_NRBP1"
                     /note="Pseudokinase domain of Nuclear Receptor Binding
                     Protein 1; cd14034"
                     /db_xref="CDD:270936"
     Region          409..437
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHY1.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99J45; propagated from
                     UniProtKB/Swiss-Prot (Q9UHY1.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHY1.1)"
     CDS             1..535
                     /gene="NRBP1"
                     /gene_synonym="BCON3; MADM; MUDPNP; NRBP"
                     /coded_by="NM_013392.4:122..1729"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1753.1"
                     /db_xref="GeneID:29959"
                     /db_xref="HGNC:HGNC:7993"
                     /db_xref="MIM:606010"
ORIGIN      
        1 msegesqtvl ssgsdpkves sssapgltsv sppvtsttsa aspeeeeese deseileesp
       61 cgrwqkrree vnqrnvpgid saylamdtee gvevvwnevq fserknyklq eekvravfdn
      121 liqlehlniv kfhkywadik enkarvifit eymssgslkq flkktkknhk tmnekawkrw
      181 ctqilsalsy lhscdppiih gnltcdtifi qhnglikigs vapdtinnhv ktcreeqknl
      241 hffapeygev tnvttavdiy sfgmcalema vleiqgnges syvpqeaiss aiqlledplq
      301 refiqkclqs eparrptare llfhpalfev pslkllaahc ivghqhmipe naleeitknm
      361 dtsavlaeip agpgrepvqt lysqspalel dkfledvrng iypltafglp rpqqpqqeev
      421 tspvvppsvk tptpepaeve trkvvlmqcn iesveegvkh hltlllkled klnrhlscdl
      481 mpnenipela aelvqlgfis eadqsrltsl leetlnkfnf arnstlnsaa vtvss
//
LOCUS       NP_001346913             913 aa            linear   ROD 27-APR-2025
DEFINITION  sperm-associated antigen 1 isoform 1 [Mus musculus].
ACCESSION   NP_001346913 XP_017172124
VERSION     NP_001346913.1
DBSOURCE    REFSEQ: accession NM_001359984.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Huang,C., Wu,D., Khan,F.A., Jiao,X., Guan,K. and Huo,L.
  TITLE     The GTPase SPAG-1 orchestrates meiotic program by dictating meiotic
            resumption and cytoskeleton architecture in mouse oocytes
  JOURNAL   Mol Biol Cell 27 (11), 1776-1785 (2016)
   PUBMED   27053660
  REMARK    GeneRIF: Findings broaden our knowledge of SPAG-1, showing that it
            exerts a role in oocyte meiotic execution via its involvement in
            AMPK and MAPK signaling pathways.
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Hayashida,K., Omagari,K., Masuda,J. and Kohno,S.
  TITLE     An integrase of endogenous retrovirus is involved in maternal
            mitochondrial DNA inheritance of the mouse
  JOURNAL   Biochem Biophys Res Commun 366 (1), 206-211 (2008)
   PUBMED   18054325
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Hayashida,K., Omagari,K., Masuda,J., Hazama,H., Kadokawa,Y.,
            Ohba,K. and Kohno,S.
  TITLE     The sperm mitochondria-specific translocator has a key role in
            maternal mitochondrial inheritance
  JOURNAL   Cell Biol Int 29 (6), 472-481 (2005)
   PUBMED   15979907
  REMARK    GeneRIF: The number of PCR positives of sperm mtDNA in two-cell
            embryos was significantly increased following sperm incubation with
            anti-tetratricopeptide repeat-containing protein involved in
            spermatogenesis (tpis).
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Yamashita,H., Avraham,S., Jiang,S., London,R., Van Veldhoven,P.P.,
            Subramani,S., Rogers,R.A. and Avraham,H.
  TITLE     Characterization of human and murine PMP20 peroxisomal proteins
            that exhibit antioxidant activity in vitro
  JOURNAL   J Biol Chem 274 (42), 29897-29904 (1999)
   PUBMED   10514471
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Takaishi,M. and Huh,Nh.
  TITLE     A tetratricopeptide repeat-containing protein gene, tpis, whose
            expression is induced with differentiation of spermatogenic cells
  JOURNAL   Biochem Biophys Res Commun 264 (1), 81-85 (1999)
   PUBMED   10527845
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC121577.3.
            
            On Jan 24, 2018 this sequence version replaced XP_017172124.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR compared
            to variant 1. Variants 1, 5 and 6 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660811.115440.1,
                                           SRR1660817.242396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 14.46 cM"
     Protein         1..913
                     /product="sperm-associated antigen 1 isoform 1"
                     /note="infertility-related sperm protein Spag-1;
                     TPR-containing protein involved in spermatogenesis"
                     /calculated_mol_wt=101969
     Region          214..698
                     /region_name="3a0801s09"
                     /note="mitochondrial precursor proteins import receptor
                     (72 kDa mitochondrial outermembrane protein)
                     (mitochondrial import receptor for the ADP/ATP carrier)
                     (translocase of outermembrane tom70); TIGR00990"
                     /db_xref="CDD:273380"
     Site            order(229..230,233..234,236,259,262..263,266..267,
                     269..270,293,296..297,300..301,304)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          229..253
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          230..>343
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          258..287
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          292..320
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          445..471
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(446..447,450..451,453,485,488..489,492..493,
                     495..496,519,522..523,526..527,530)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          483..513
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          518..546
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(619,622..623,626..627,629,653,656..657,660..661,
                     663..664,687,690..691,694..695,698)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          619..646
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          631..>807
                     /region_name="PLN03088"
                     /note="SGT1, suppressor of G2 allele of SKP1; Provisional"
                     /db_xref="CDD:215568"
     Region          651..681
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          790..881
                     /region_name="RPAP3_C"
                     /note="Potential Monad-binding region of RPAP3; pfam13877"
                     /db_xref="CDD:464012"
     CDS             1..913
                     /gene="Spag1"
                     /gene_synonym="tpis"
                     /coded_by="NM_001359984.1:472..3213"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:26942"
                     /db_xref="MGI:MGI:1349387"
ORIGIN      
        1 mqfsilqhet ltmtakakdc pslwgfgttk tfkipiehld fkyiencsdv khlekilyvl
       61 rsgeegyype ltefcekclt nlapksralr kdkpaetass fsaeewekid sdlkswvsei
      121 kreentchfh dpenhpgved plppvrgstc cphsgketys ksktakkrip rdyaewdkfd
      181 vekecskide dykektvinn kahlskietk ietaglteke ksflanrekg kgneafysgd
      241 yeeavmyytr slsalptaia ynnraqaeik lqrwssaled cekaleldpg nvkallrrat
      301 tykhqnklqe avddlrkvlq vepdndlakk tlseverdlk nsepvselqt kgkrmvieev
      361 ensgdeggkg saderedggs deaamgniqk klmvrrsegg rrsrrgrtpg praeqqgglr
      421 etatastgds hypeepraad npsglkrrgn elfrggqfae aaaqysvaia qleptgsana
      481 delsilysnr aacylkegnc rdciqdcnra lelhpfsvkp llrramayet leqyrnayvd
      541 yktvlqidcg iqlasdsanr iarilteldg skwrerlppi pavptseplr vwlpaaetpd
      601 qdpcpnncmp sitdekmfqa lkeegnqlvk dknykdaisk yneclkinsk acaiytnral
      661 cylklgqfee akldceqalq idgenvkash rlalaqkgle ncresgvdps qvllspdsse
      721 aarhldtknd tappskgrer rriqvqevdg ssdeeperpa easatsapar dgvedggsae
      781 paekldvskp tnayefgqvl stisarkdee acahllaita pkdlplllsn klegdtflll
      841 iqslkshlva kdpslvyehl lylskaerfk tmltlinkgq keqmaqlfdg lsdtqsdglt
      901 aedvqalrrq yel
//
LOCUS       NP_001311027             536 aa            linear   PRI 27-APR-2025
DEFINITION  cytokine-like nuclear factor N-PAC isoform 5 [Homo sapiens].
ACCESSION   NP_001311027 XP_005255695
VERSION     NP_001311027.2
DBSOURCE    REFSEQ: accession NM_001324098.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Gonzalez-Teran,B., Pittman,M., Felix,F., Thomas,R.,
            Richmond-Buccola,D., Huttenhain,R., Choudhary,K., Moroni,E.,
            Costa,M.W., Huang,Y., Padmanabhan,A., Alexanian,M., Lee,C.Y.,
            Maven,B.E.J., Samse-Knapp,K., Morton,S.U., McGregor,M.,
            Gifford,C.A., Seidman,J.G., Seidman,C.E., Gelb,B.D., Colombo,G.,
            Conklin,B.R., Black,B.L., Bruneau,B.G., Krogan,N.J., Pollard,K.S.
            and Srivastava,D.
  TITLE     Transcription factor protein interactomes reveal genetic
            determinants in heart disease
  JOURNAL   Cell 185 (5), 794-814 (2022)
   PUBMED   35182466
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Hu,Z., Long,T., Ma,Y., Zhu,J., Gao,L., Zhong,Y., Wang,X., Wang,X.
            and Li,Z.
  TITLE     Downregulation of GLYR1 contributes to microsatellite instability
            colorectal cancer by targeting p21 via the p38MAPK and PI3K/AKT
            pathways
  JOURNAL   J Exp Clin Cancer Res 39 (1), 76 (2020)
   PUBMED   32370786
  REMARK    GeneRIF: Downregulation of GLYR1 contributes to microsatellite
            instability colorectal cancer by targeting p21 via the p38MAPK and
            PI3K/AKT pathways.
            Erratum:[J Exp Clin Cancer Res. 2020 Jul 6;39(1):125. doi:
            10.1186/s13046-020-01635-6. PMID: 32624003]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Fei,J., Ishii,H., Hoeksema,M.A., Meitinger,F., Kassavetis,G.A.,
            Glass,C.K., Ren,B. and Kadonaga,J.T.
  TITLE     NDF, a nucleosome-destabilizing factor that facilitates
            transcription through nucleosomes
  JOURNAL   Genes Dev 32 (9-10), 682-694 (2018)
   PUBMED   29759984
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Fang,R., Chen,F., Dong,Z., Hu,D., Barbera,A.J., Clark,E.A.,
            Fang,J., Yang,Y., Mei,P., Rutenberg,M., Li,Z., Zhang,Y., Xu,Y.,
            Yang,H., Wang,P., Simon,M.D., Zhou,Q., Li,J., Marynick,M.P., Li,X.,
            Lu,H., Kaiser,U.B., Kingston,R.E., Xu,Y. and Shi,Y.G.
  TITLE     LSD2/KDM1B and its cofactor NPAC/GLYR1 endow a structural and
            molecular model for regulation of H3K4 demethylation
  JOURNAL   Mol Cell 49 (3), 558-570 (2013)
   PUBMED   23260659
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Vermeulen,M., Eberl,H.C., Matarese,F., Marks,H., Denissov,S.,
            Butter,F., Lee,K.K., Olsen,J.V., Hyman,A.A., Stunnenberg,H.G. and
            Mann,M.
  TITLE     Quantitative interaction proteomics and genome-wide profiling of
            epigenetic histone marks and their readers
  JOURNAL   Cell 142 (6), 967-980 (2010)
   PUBMED   20850016
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Fu,J., Yang,Z., Wei,J., Han,J. and Gu,J.
  TITLE     Nuclear protein NP60 regulates p38 MAPK activity
  JOURNAL   J Cell Sci 119 (Pt 1), 115-123 (2006)
   PUBMED   16352664
REFERENCE   10 (residues 1 to 536)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020663.1 and KF456151.1.
            
            On May 9, 2019 this sequence version replaced NP_001311027.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..536
                     /product="cytokine-like nuclear factor N-PAC isoform 5"
                     /note="nuclear protein 60 kDa; nuclear protein 60kDa;
                     cytokine-like nuclear factor n-pac; putative
                     oxidoreductase GLYR1; nuclear protein NP60; nuclear
                     protein of 60 kDa; 3-hydroxyisobutyrate dehydrogenase-like
                     protein; nucleosome-destabilizing factor"
                     /calculated_mol_wt=58497
     Region          6..90
                     /region_name="PWWP_GLYR1"
                     /note="PWWP domain found in glyoxylate reductase 1 (GLYR1)
                     and similar proteins; cd05836"
                     /db_xref="CDD:438961"
     Site            order(19,22,46)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438961"
     Site            20..23
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438961"
     Region          110..>173
                     /region_name="DUF4603"
                     /note="Domain of unknown function (DUF4603); pfam15376"
                     /db_xref="CDD:464684"
     Region          251..534
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
     CDS             1..536
                     /gene="GLYR1"
                     /gene_synonym="BM045; HIBDL; hNDF; N-PAC; NP60; NPAC"
                     /coded_by="NM_001324098.2:24..1634"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:84656"
                     /db_xref="HGNC:HGNC:24434"
                     /db_xref="MIM:610660"
ORIGIN      
        1 maavslrlgd lvwgklgryp pwpgkivnpp kdlkkprgkk cffvkffgte dhawikveql
       61 kpyhahkeem ikinkgkrfq qavdaveefl rrakgkdqts shnssddknr rnsseersrp
      121 nsgdekrkls lsegkvkknm gegkkrvssg ssergskspl kraqeqsprk rgrppkdekd
      181 ltipesstvk gmmagpmaaf kwqptasepv kdadphfhhf llsqteketg stsiqaadst
      241 avngsitptd kkigflglgl mgsgivsnll kmghtvtvwn rtaekcdlfi qegarlgrtp
      301 aevvstcdit facvsdpkaa kdlvlgpsgv lqgirpgkcy vdmstvdadt vtelaqvivs
      361 rggrfleapv sgnqqlsndg mlvilaagdr glyedcsscf qamgktsffl gevgnaakmm
      421 livnmvqgsf matiaegltl aqvtgqsqqt lldilnqgql asifldqkcq nilqgnfkpd
      481 fylkyiqkdl rlaialgdav nhptpmaaaa nevykrakal dqsdndmsav yrayih
//
LOCUS       NP_005210               1272 aa            linear   PRI 27-APR-2025
DEFINITION  protein diaphanous homolog 1 isoform 1 [Homo sapiens].
ACCESSION   NP_005210
VERSION     NP_005210.3
DBSOURCE    REFSEQ: accession NM_005219.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1272)
  AUTHORS   Azizoglu,Z.B., Babayeva,R., Haskologlu,Z.S., Acar,M.B.,
            Ayaz-Guner,S., Okus,F.Z., Alsavaf,M.B., Can,S., Basaran,K.E.,
            Canatan,M.F., Ozcan,A., Erkmen,H., Leblebici,C.B., Yilmaz,E.,
            Karakukcu,M., Kose,M., Canoz,O., Ozen,A., Karakoc-Aydiner,E.,
            Ceylaner,S., Gumus,G., Per,H., Gumus,H., Canatan,H., Ozcan,S.,
            Dogu,F., Ikinciogullari,A., Unal,E., Baris,S. and Eken,A.
  TITLE     DIAPH1-Deficiency is Associated with Major T, NK and ILC Defects in
            Humans
  JOURNAL   J Clin Immunol 44 (8), 175 (2024)
   PUBMED   39120629
  REMARK    GeneRIF: DIAPH1-Deficiency is Associated with Major T, NK and ILC
            Defects in Humans.
            Erratum:[J Clin Immunol. 2024 Nov 16;45(1):43. doi:
            10.1007/s10875-024-01832-4. PMID: 39547966]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1272)
  AUTHORS   Palmer,N.J., Barrie,K.R. and Dominguez,R.
  TITLE     Mechanisms of actin filament severing and elongation by formins
  JOURNAL   Nature 632 (8024), 437-442 (2024)
   PUBMED   38843827
  REMARK    GeneRIF: Mechanisms of actin filament severing and elongation by
            formins.
REFERENCE   3  (residues 1 to 1272)
  AUTHORS   Theophall,G.G., Ramirez,L.M.S., Premo,A., Reverdatto,S.,
            Manigrasso,M.B., Yepuri,G., Burz,D.S., Ramasamy,R., Schmidt,A.M.
            and Shekhtman,A.
  TITLE     Disruption of the productive encounter complex results in
            dysregulation of DIAPH1 activity
  JOURNAL   J Biol Chem 299 (11), 105342 (2023)
   PUBMED   37832872
  REMARK    GeneRIF: Disruption of the productive encounter complex results in
            dysregulation of DIAPH1 activity.
REFERENCE   4  (residues 1 to 1272)
  AUTHORS   Yepuri,G., Ramirez,L.M., Theophall,G.G., Reverdatto,S.V.,
            Quadri,N., Hasan,S.N., Bu,L., Thiagarajan,D., Wilson,R., Diez,R.L.,
            Gugger,P.F., Mangar,K., Narula,N., Katz,S.D., Zhou,B., Li,H.,
            Stotland,A.B., Gottlieb,R.A., Schmidt,A.M., Shekhtman,A. and
            Ramasamy,R.
  TITLE     DIAPH1-MFN2 interaction regulates mitochondria-SR/ER contact and
            modulates ischemic/hypoxic stress
  JOURNAL   Nat Commun 14 (1), 6900 (2023)
   PUBMED   37903764
  REMARK    GeneRIF: DIAPH1-MFN2 interaction regulates mitochondria-SR/ER
            contact and modulates ischemic/hypoxic stress.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1272)
  AUTHORS   Mohseni,M., Mohammadi,Y., Zare Ashrafi,F., Ghodratpour,F.,
            Jalalvand,K., Arzhangi,S., Babanejad,M., Azizi,M.H., Kahrizi,K. and
            Najmabadi,H.
  TITLE     An Extended Iranian Family with Autosomal Dominant Non-syndromic
            Hearing Loss Associated with A Nonsense Mutation in the DIAPH1 Gene
  JOURNAL   Arch Iran Med 26 (3), 176-180 (2023)
   PUBMED   37543941
  REMARK    GeneRIF: An Extended Iranian Family with Autosomal Dominant
            Non-syndromic Hearing Loss Associated with A Nonsense Mutation in
            the DIAPH1 Gene.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1272)
  AUTHORS   Kato,T., Watanabe,N., Morishima,Y., Fujita,A., Ishizaki,T. and
            Narumiya,S.
  TITLE     Localization of a mammalian homolog of diaphanous, mDia1, to the
            mitotic spindle in HeLa cells
  JOURNAL   J Cell Sci 114 (Pt 4), 775-784 (2001)
   PUBMED   11171383
REFERENCE   7  (residues 1 to 1272)
  AUTHORS   Lynch,E.D., Lee,M.K., Morrow,J.E., Welcsh,P.L., Leon,P.E. and
            King,M.C.
  TITLE     Nonsyndromic deafness DFNA1 associated with mutation of a human
            homolog of the Drosophila gene diaphanous
  JOURNAL   Science 278 (5341), 1315-1318 (1997)
   PUBMED   9360932
REFERENCE   8  (residues 1 to 1272)
  AUTHORS   Reinhard,M., Giehl,K., Abel,K., Haffner,C., Jarchau,T., Hoppe,V.,
            Jockusch,B.M. and Walter,U.
  TITLE     The proline-rich focal adhesion and microfilament protein VASP is a
            ligand for profilins
  JOURNAL   EMBO J 14 (8), 1583-1589 (1995)
   PUBMED   7737110
REFERENCE   9  (residues 1 to 1272)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 1272)
  AUTHORS   Leon,P.E., Raventos,H., Lynch,E., Morrow,J. and King,M.C.
  TITLE     The gene for an inherited form of deafness maps to chromosome 5q31
  JOURNAL   Proc Natl Acad Sci U S A 89 (11), 5181-5184 (1992)
   PUBMED   1350680
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA593734.1, AB209482.1,
            AY363395.1 and AY007129.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 14, 2006 this sequence version replaced NP_005210.2.
            
            Summary: This gene is a homolog of the Drosophila diaphanous gene,
            and has been linked to autosomal dominant, fully penetrant,
            nonsyndromic sensorineural progressive low-frequency hearing loss.
            Actin polymerization involves proteins known to interact with
            diaphanous protein in Drosophila and mouse. It has therefore been
            speculated that this gene may have a role in the regulation of
            actin polymerization in hair cells of the inner ear. Alternatively
            spliced transcript variants encoding distinct isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB209482.1, BC143413.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389054.8/ ENSP00000373706.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..1272
                     /product="protein diaphanous homolog 1 isoform 1"
                     /note="protein diaphanous homolog 1; mammalian diaphanous
                     related formin 1"
                     /calculated_mol_wt=141217
     Region          1..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60610.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O60610.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60610.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60610.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60610.2)"
     Region          84..268
                     /region_name="Drf_GBD"
                     /note="Diaphanous GTPase-binding Domain; pfam06371"
                     /db_xref="CDD:461886"
     Region          274..464
                     /region_name="Drf_FH3"
                     /note="Diaphanous FH3 Domain; pfam06367"
                     /db_xref="CDD:461885"
     Region          <429..>570
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          573..755
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60610.2)"
     Region          590..>704
                     /region_name="Drf_FH1"
                     /note="Formin Homology Region 1; pfam06346"
                     /db_xref="CDD:461881"
     Site            768
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:23325789; propagated from
                     UniProtKB/Swiss-Prot (O60610.2)"
     Region          769..1145
                     /region_name="FH2"
                     /note="Formin Homology 2 Domain; pfam02181"
                     /db_xref="CDD:396655"
     Site            1057
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60610.2)"
     Site            1103
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60610.2)"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O08808; propagated from
                     UniProtKB/Swiss-Prot (O60610.2)"
     Site            1251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60610.2)"
     Site            1254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60610.2)"
     CDS             1..1272
                     /gene="DIAPH1"
                     /gene_synonym="DFNA1; DIA1; DRF1; hDIA1; LFHL1; mDia1;
                     SCBMS"
                     /coded_by="NM_005219.5:87..3905"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43374.1"
                     /db_xref="GeneID:1729"
                     /db_xref="HGNC:HGNC:2876"
                     /db_xref="MIM:602121"
ORIGIN      
        1 meppggslgp grgtrdkkkg rspdelpsag gdggkskkft lkrlmadele rftsmrikke
       61 kekpnsahrn ssasygddpt aqslqdvsde qvlvlfeqml ldmnlneekq qplrekdiii
      121 kremvsqyly tskagmsqke ssksammyiq elrsglrdmp llscleslrv slnnnpvswv
      181 qtfgaeglas lldilkrlhd ekeetagsyd srnkheiirc lkafmnnkfg iktmleteeg
      241 illlvramdp avpnmmidaa kllsalcilp qpedmnervl eamteraemd everfqplld
      301 glksgttial kvgclqlina litpaeeldf rvhirselmr lglhqvlqdl reienedmrv
      361 qlnvfdeqge edsydlkgrl ddirmemddf nevfqillnt vkdskaephf lsilqhlllv
      421 rndyearpqy yklieecisq ivlhkngadp dfkcrhlqie ieglidqmid ktkvekseak
      481 aaelekklds eltarhelqv emkkmesdfe qklqdlqgek dalhsekqqi atekqdleae
      541 vsqltgevak ltkeledakk emaslsaaai tvppsvpsra pvppapplpg dsgtiipppp
      601 apgdsttppp pppppppppp lpggvcissp pslpggtais pppplsgdat ippppplpeg
      661 vgipspsslp ggtaippppp lpgsarippp ppplpgsagi pppppplpge agmppppppl
      721 pggpgipppp pfpggpgipp pppgmgmppp ppfgfgvpaa pvlpfgltpk klykpevqlr
      781 rpnwsklvae dlsqdcfwtk vkedrfenne lfakltltfs aqtktskakk dqeggeekks
      841 vqkkkvkelk vldsktaqnl siflgsfrmp yqeiknvile vneavltesm iqnlikqmpe
      901 peqlkmlsel kdeyddlaes eqfgvvmgtv prlrprlnai lfklqfseqv enikpeivsv
      961 taaceelrks esfsnlleit llvgnymnag srnagafgfn isflcklrdt kstdqkmtll
     1021 hflaelcend ypdvlkfpde lahvekasrv saenlqknld qmkkqisdve rdvqnfpaat
     1081 dekdkfvekm tsfvkdaqeq ynklrmmhsn metlykelge yflfdpkkls veeffmdlhn
     1141 frnmflqavk enqkrretee kmrraklake kaekerlekq qkreqlidmn aegdetgvmd
     1201 sllealqsga afrrkrgprq anrkagcavt sllaseltkd damaavpakv sknsetfpti
     1261 leeakelvgr as
//
LOCUS       NP_055157                303 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial carrier homolog 2 isoform 1 [Homo sapiens].
ACCESSION   NP_055157
VERSION     NP_055157.1
DBSOURCE    REFSEQ: accession NM_014342.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Ulupinar,P., Caglayan,E., Rayaman,E., Nagata,K. and Turan,K.
  TITLE     The mitochondrial carrier homolog 2 is involved in down-regulation
            of influenza A virus replication
  JOURNAL   Mol Biol Rep 51 (1), 642 (2024)
   PUBMED   38727866
  REMARK    GeneRIF: The mitochondrial carrier homolog 2 is involved in
            down-regulation of influenza A virus replication.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Zheng,X. and Chu,B.
  TITLE     The biology of mitochondrial carrier homolog 2
  JOURNAL   Mitochondrion 75, 101837 (2024)
   PUBMED   38158152
  REMARK    GeneRIF: The biology of mitochondrial carrier homolog 2.
            Review article
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Goldman,A., Mullokandov,M., Zaltsman,Y., Regev,L., Levin-Zaidman,S.
            and Gross,A.
  TITLE     MTCH2 cooperates with MFN2 and lysophosphatidic acid synthesis to
            sustain mitochondrial fusion
  JOURNAL   EMBO Rep 25 (1), 45-67 (2024)
   PUBMED   38177900
  REMARK    GeneRIF: MTCH2 cooperates with MFN2 and lysophosphatidic acid
            synthesis to sustain mitochondrial fusion.
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Guna,A., Stevens,T.A., Inglis,A.J., Replogle,J.M., Esantsi,T.K.,
            Muthukumar,G., Shaffer,K.C.L., Wang,M.L., Pogson,A.N., Jones,J.J.,
            Lomenick,B., Chou,T.F., Weissman,J.S. and Voorhees,R.M.
  TITLE     MTCH2 is a mitochondrial outer membrane protein insertase
  JOURNAL   Science 378 (6617), 317-322 (2022)
   PUBMED   36264797
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Eswarappa,S.M., Potdar,A.A., Koch,W.J., Fan,Y., Vasu,K.,
            Lindner,D., Willard,B., Graham,L.M., DiCorleto,P.E. and Fox,P.L.
  TITLE     Programmed translational readthrough generates antiangiogenic
            VEGF-Ax
  JOURNAL   Cell 157 (7), 1605-1618 (2014)
   PUBMED   24949972
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Renstrom,F., Payne,F., Nordstrom,A., Brito,E.C., Rolandsson,O.,
            Hallmans,G., Barroso,I., Nordstrom,P. and Franks,P.W.
  CONSRTM   GIANT Consortium
  TITLE     Replication and extension of genome-wide association study results
            for obesity in 4923 adults from northern Sweden
  JOURNAL   Hum Mol Genet 18 (8), 1489-1496 (2009)
   PUBMED   19164386
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Willer,C.J., Speliotes,E.K., Loos,R.J., Li,S., Lindgren,C.M.,
            Heid,I.M., Berndt,S.I., Elliott,A.L., Jackson,A.U., Lamina,C.,
            Lettre,G., Lim,N., Lyon,H.N., McCarroll,S.A., Papadakis,K., Qi,L.,
            Randall,J.C., Roccasecca,R.M., Sanna,S., Scheet,P., Weedon,M.N.,
            Wheeler,E., Zhao,J.H., Jacobs,L.C., Prokopenko,I., Soranzo,N.,
            Tanaka,T., Timpson,N.J., Almgren,P., Bennett,A., Bergman,R.N.,
            Bingham,S.A., Bonnycastle,L.L., Brown,M., Burtt,N.P., Chines,P.,
            Coin,L., Collins,F.S., Connell,J.M., Cooper,C., Smith,G.D.,
            Dennison,E.M., Deodhar,P., Elliott,P., Erdos,M.R., Estrada,K.,
            Evans,D.M., Gianniny,L., Gieger,C., Gillson,C.J., Guiducci,C.,
            Hackett,R., Hadley,D., Hall,A.S., Havulinna,A.S., Hebebrand,J.,
            Hofman,A., Isomaa,B., Jacobs,K.B., Johnson,T., Jousilahti,P.,
            Jovanovic,Z., Khaw,K.T., Kraft,P., Kuokkanen,M., Kuusisto,J.,
            Laitinen,J., Lakatta,E.G., Luan,J., Luben,R.N., Mangino,M.,
            McArdle,W.L., Meitinger,T., Mulas,A., Munroe,P.B., Narisu,N.,
            Ness,A.R., Northstone,K., O'Rahilly,S., Purmann,C., Rees,M.G.,
            Ridderstrale,M., Ring,S.M., Rivadeneira,F., Ruokonen,A.,
            Sandhu,M.S., Saramies,J., Scott,L.J., Scuteri,A., Silander,K.,
            Sims,M.A., Song,K., Stephens,J., Stevens,S., Stringham,H.M.,
            Tung,Y.C., Valle,T.T., Van Duijn,C.M., Vimaleswaran,K.S.,
            Vollenweider,P., Waeber,G., Wallace,C., Watanabe,R.M.,
            Waterworth,D.M., Watkins,N., Witteman,J.C., Zeggini,E., Zhai,G.,
            Zillikens,M.C., Altshuler,D., Caulfield,M.J., Chanock,S.J.,
            Farooqi,I.S., Ferrucci,L., Guralnik,J.M., Hattersley,A.T., Hu,F.B.,
            Jarvelin,M.R., Laakso,M., Mooser,V., Ong,K.K., Ouwehand,W.H.,
            Salomaa,V., Samani,N.J., Spector,T.D., Tuomi,T., Tuomilehto,J.,
            Uda,M., Uitterlinden,A.G., Wareham,N.J., Deloukas,P.,
            Frayling,T.M., Groop,L.C., Hayes,R.B., Hunter,D.J., Mohlke,K.L.,
            Peltonen,L., Schlessinger,D., Strachan,D.P., Wichmann,H.E.,
            McCarthy,M.I., Boehnke,M., Barroso,I., Abecasis,G.R. and
            Hirschhorn,J.N.
  CONSRTM   Wellcome Trust Case Control Consortium; Genetic Investigation of
            ANthropometric Traits Consortium
  TITLE     Six new loci associated with body mass index highlight a neuronal
            influence on body weight regulation
  JOURNAL   Nat Genet 41 (1), 25-34 (2009)
   PUBMED   19079261
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Grinberg,M., Schwarz,M., Zaltsman,Y., Eini,T., Niv,H.,
            Pietrokovski,S. and Gross,A.
  TITLE     Mitochondrial carrier homolog 2 is a target of tBID in cells
            signaled to die by tumor necrosis factor alpha
  JOURNAL   Mol Cell Biol 25 (11), 4579-4590 (2005)
   PUBMED   15899861
  REMARK    GeneRIF: Mtch2 is a mitochondrial target of tBID and possibly
            participates in the mitochondrial apoptotic program.
REFERENCE   9  (residues 1 to 303)
  AUTHORS   Yerushalmi,G.M., Leibowitz-Amit,R., Shaharabany,M. and Tsarfaty,I.
  TITLE     Met-HGF/SF signal transduction induces mimp, a novel mitochondrial
            carrier homologue, which leads to mitochondrial depolarization
  JOURNAL   Neoplasia 4 (6), 510-522 (2002)
   PUBMED   12407445
REFERENCE   10 (residues 1 to 303)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313032.1, AY380792.1 and
            AC104942.5.
            
            Summary: This gene encodes a member of the SLC25 family of
            nuclear-encoded transporters that are localized in the inner
            mitochondrial membrane. Members of this superfamily are involved in
            many metabolic pathways and cell functions. Genome-wide association
            studies in human have identified single-nucleotide polymorphisms in
            several loci associated with obesity. This gene is one such locus,
            which is highly expressed in white adipose tissue and adipocytes,
            and thought to play a regulatory role in adipocyte differentiation
            and biology. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. A recent study
            showed this gene to be an authentic stop codon readthrough target
            that can produce two isoforms from the same mRNA by use of
            alternative in-frame translation termination codons. [provided by
            RefSeq, Dec 2017].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes two isoforms, which result from the use of
            alternative in-frame translation termination codons. The shorter
            isoform (1) results from translation termination at the upstream
            UGA stop codon, while the longer isoform (1x) results from UGA stop
            codon readthrough to the downstream UAG termination codon. This
            RefSeq represents the shorter isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.269157.1,
                                           SRR1803614.157346.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000302503.8/
                                                  ENSP00000303222.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..303
                     /product="mitochondrial carrier homolog 2 isoform 1"
                     /note="met-induced mitochondrial protein; mitochondrial
                     carrier homolog 2; solute carrier family 25, member 50"
                     /calculated_mol_wt=33200
     Region          2..98
                     /region_name="Solcar 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            16..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            78..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Region          118..206
                     /region_name="Solcar 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Region          128..>192
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            181..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            281..303
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     CDS             1..303
                     /gene="MTCH2"
                     /gene_synonym="HSPC032; MIMP; SLC25A50"
                     /coded_by="NM_014342.4:95..1006"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7943.1"
                     /db_xref="GeneID:23788"
                     /db_xref="HGNC:HGNC:17587"
                     /db_xref="MIM:613221"
ORIGIN      
        1 madaasqvll gsgltilsqp lmyvkvliqv gyeplpptig rnifgrqvcq lpglfsyaqh
       61 iasidgrrgl ftgltprlcs gvlgtvvhgk vlqhyqesdk geelgpgnvq kevsssfdhv
      121 ikettremia rsaatlithp fhvitlrsmv qfigreskyc glcdsiitiy reegilgffa
      181 glvprllgdi lslwlcnsla ylvntyalds gvstmnemks ysqavtgffa smltypfvlv
      241 snlmavnncg laggcppysp iytswidcwc mlqkegnmsr gnslffrkvp fgktyccdlk
      301 mli
//
LOCUS       NP_060296                425 aa            linear   PRI 27-APR-2025
DEFINITION  spermatogenesis- and oogenesis-specific basic
            helix-loop-helix-containing protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_060296 XP_370720
VERSION     NP_060296.2
DBSOURCE    REFSEQ: accession NM_017826.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Zhang,R., Zhang,X., Zhang,W., Cui,W., Xiao,Y., Liu,L., Zhi,S.,
            Feng,X., Liu,X., Shen,Y., Chai,J. and Hao,J.
  TITLE     Sohlh2 Regulates the Stemness and Differentiation of Colon Cancer
            Stem Cells by Downregulating LncRNA-H19 Transcription
  JOURNAL   Mol Cancer Res 21 (2), 115-126 (2023)
   PUBMED   36287177
  REMARK    GeneRIF: Sohlh2 Regulates the Stemness and Differentiation of Colon
            Cancer Stem Cells by Downregulating LncRNA-H19 Transcription.
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Cui,W., Xiao,Y., Zhang,R., Zhao,N., Zhang,X., Wang,F., Liu,Y.,
            Zhang,X. and Hao,J.
  TITLE     SOHLH2 Suppresses Angiogenesis by Downregulating HIF1alpha
            Expression in Breast Cancer
  JOURNAL   Mol Cancer Res 19 (9), 1498-1509 (2021)
   PUBMED   34158392
  REMARK    GeneRIF: SOHLH2 Suppresses Angiogenesis by Downregulating HIF1alpha
            Expression in Breast Cancer.
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Duran-Lozano,L., Thorleifsson,G., Lopez de Lapuente Portilla,A.,
            Niroula,A., Went,M., Thodberg,M., Pertesi,M., Ajore,R., Cafaro,C.,
            Olason,P.I., Stefansdottir,L., Bragi Walters,G., Halldorsson,G.H.,
            Turesson,I., Kaiser,M.F., Weinhold,N., Abildgaard,N.,
            Andersen,N.F., Mellqvist,U.H., Waage,A., Juul-Vangsted,A.,
            Thorsteinsdottir,U., Hansson,M., Houlston,R., Rafnar,T.,
            Stefansson,K. and Nilsson,B.
  TITLE     Germline variants at SOHLH2 influence multiple myeloma risk
  JOURNAL   Blood Cancer J 11 (4), 76 (2021)
   PUBMED   33875642
  REMARK    GeneRIF: Germline variants at SOHLH2 influence multiple myeloma
            risk.
            Erratum:[Blood Cancer J. 2021 Nov 16;11(11):181. doi:
            10.1038/s41408-021-00575-4. PMID: 34782614]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Cervan-Martin,M., Suazo-Sanchez,M.I., Rivera-Egea,R., Garrido,N.,
            Lujan,S., Romeu,G., Santos-Ribeiro,S., Castilla,J.A.,
            Gonzalvo,M.C., Clavero,A., Vicente,F.J., Maldonado,V., Burgos,M.,
            Barrionuevo,F.J., Jimenez,R., Sanchez-Curbelo,J., Lopez-Rodrigo,O.,
            Peraza,M.F., Pereira-Caetano,I., Marques,P.I., Carvalho,F.,
            Barros,A., Bassas,L., Seixas,S., Goncalves,J., Larriba,S.,
            Lopes,A.M., Palomino-Morales,R.J. and Carmona,F.D.
  CONSRTM   Lisbon Clinical Group; IVIRMA Group
  TITLE     Intronic variation of the SOHLH2 gene confers risk to male
            reproductive impairment
  JOURNAL   Fertil Steril 114 (2), 398-406 (2020)
   PUBMED   32690270
  REMARK    GeneRIF: Intronic variation of the SOHLH2 gene confers risk to male
            reproductive impairment.
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Zhang,X., Liu,X., Cui,W., Zhang,R., Liu,Y., Li,Y. and Hao,J.
  TITLE     Sohlh2 alleviates malignancy of EOC cells under hypoxia via
            inhibiting the HIF1alpha/CA9 signaling pathway
  JOURNAL   Biol Chem 401 (2), 263-271 (2020)
   PUBMED   31318683
  REMARK    GeneRIF: Sohlh2 alleviates malignancy of EOC cells under hypoxia
            via inhibiting the HIF1alpha/CA9 signaling pathway.
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Suzuki,H., Ahn,H.W., Chu,T., Bowden,W., Gassei,K., Orwig,K. and
            Rajkovic,A.
  TITLE     SOHLH1 and SOHLH2 coordinate spermatogonial differentiation
  JOURNAL   Dev Biol 361 (2), 301-312 (2012)
   PUBMED   22056784
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Woloszynska-Read,A., Zhang,W., Yu,J., Link,P.A.,
            Mhawech-Fauceglia,P., Collamat,G., Akers,S.N., Ostler,K.R.,
            Godley,L.A., Odunsi,K. and Karpf,A.R.
  TITLE     Coordinated cancer germline antigen promoter and global DNA
            hypomethylation in ovarian cancer: association with the BORIS/CTCF
            expression ratio and advanced stage
  JOURNAL   Clin Cancer Res 17 (8), 2170-2180 (2011)
   PUBMED   21296871
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Wheeler,H.E., Metter,E.J., Tanaka,T., Absher,D., Higgins,J.,
            Zahn,J.M., Wilhelmy,J., Davis,R.W., Singleton,A., Myers,R.M.,
            Ferrucci,L. and Kim,S.K.
  TITLE     Sequential use of transcriptional profiling, expression
            quantitative trait mapping, and gene association implicates MMP20
            in human kidney aging
  JOURNAL   PLoS Genet 5 (10), e1000685 (2009)
   PUBMED   19834535
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Shen,L., Kondo,Y., Guo,Y., Zhang,J., Zhang,L., Ahmed,S., Shu,J.,
            Chen,X., Waterland,R.A. and Issa,J.P.
  TITLE     Genome-wide profiling of DNA methylation reveals a class of
            normally methylated CpG island promoters
  JOURNAL   PLoS Genet 3 (10), 2023-2036 (2007)
   PUBMED   17967063
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Suzumori,N., Pangas,S.A. and Rajkovic,A.
  TITLE     Candidate genes for premature ovarian failure
  JOURNAL   Curr Med Chem 14 (3), 353-357 (2007)
   PUBMED   17305537
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB022954.1, AK000456.1,
            AL160392.12 and AI368806.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 6, 2009 this sequence version replaced NP_060296.1.
            
            Summary: This gene encodes one of testis-specific transcription
            factors which are essential for spermatogenesis, oogenesis and
            folliculogenesis. This gene is located on chromosome 13. The
            proteins encoded by this gene and another testis-specific
            transcription factor, SOHLH1, can form heterodimers, in addition to
            homodimers. There is a read-through locus (GeneID: 100526761) that
            shares sequence identity with this gene and the upstream CCDC169
            (GeneID: 728591). Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000456.1, HM005590.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379881.8/ ENSP00000369210.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q13.3"
     Protein         1..425
                     /product="spermatogenesis- and oogenesis-specific basic
                     helix-loop-helix-containing protein 2 isoform 1"
                     /note="spermatogenesis- and oogenesis-specific basic
                     helix-loop-helix-containing protein 2; spermatogenesis
                     associated 28; testicular secretory protein Li 50;
                     testicular secretory protein Li 51"
                     /calculated_mol_wt=46810
     Region          201..259
                     /region_name="bHLH_SOHLH1_2"
                     /note="basic helix-loop-helix (bHLH) domain found in the
                     spermatogenesis- and oogenesis-specific basic
                     helix-loop-helix-containing protein (SOHLH) family;
                     cd18908"
                     /db_xref="CDD:381478"
     Site            order(202..207,210..211,213..214,237..238)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381478"
     Site            order(214,216..217,220..221,223..224,227,238..240,
                     242..243,245..246,248..250,252..253)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381478"
     CDS             1..425
                     /gene="SOHLH2"
                     /gene_synonym="bHLHe81; SOSF2; SPATA28; TEB1"
                     /coded_by="NM_017826.3:31..1308"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9355.1"
                     /db_xref="GeneID:54937"
                     /db_xref="HGNC:HGNC:26026"
                     /db_xref="MIM:616066"
ORIGIN      
        1 massiicqeh cqisgqakid illvgdvtvg yladtvqklf aniaevtiti sdtkeaaall
       61 ddcifnmvll kvpsslsaee leaiklirfg kkknthslfv fiipenfkgc isghgmdial
      121 tepltmekms nvvkywttcp sntvktenat gpeelglplq rsysehlgyf ptdlfacses
      181 lrngngleln aslsefeknk kisllhsske klrrerikyc ceqlrtllpy vkgrkndaas
      241 vleatvdyvk yirekispav maqitealqs nmrfckkqqt pielslpgtv maqrensvms
      301 tysperglqf ltntcwngcs tpdaesslde avrvpsssas enaigdpykt hissaalsln
      361 slhtvryysk vtpsydatav tnqnisihlp samppvskll prhctsglgq tctthpnclq
      421 qfway
//
LOCUS       NP_001351406             364 aa            linear   ROD 27-APR-2025
DEFINITION  erlin-2 isoform 2 [Mus musculus].
ACCESSION   NP_001351406 XP_006509177
VERSION     NP_001351406.1
DBSOURCE    REFSEQ: accession NM_001364477.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Gao,X., Bonzerato,C.G. and Wojcikiewicz,R.J.H.
  TITLE     Binding of the erlin1/2 complex to the third intralumenal loop of
            IP3R1 triggers its ubiquitin-proteasomal degradation
  JOURNAL   J Biol Chem 298 (6), 102026 (2022)
   PUBMED   35568199
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Wright,F.A., Bonzerato,C.G., Sliter,D.A. and Wojcikiewicz,R.J.H.
  TITLE     The erlin2 T65I mutation inhibits erlin1/2 complex-mediated
            inositol 1,4,5-trisphosphate receptor ubiquitination and
            phosphatidylinositol 3-phosphate binding
  JOURNAL   J Biol Chem 293 (40), 15706-15714 (2018)
   PUBMED   30135210
  REMARK    GeneRIF: The erlin2 threonine to isoleucine 65 substitution
            inhibits erlin1/erlin2 complex-mediated inositol
            1,4,5-trisphosphate receptor ubiquitination and
            phosphatidylinositol 3-phosphate binding.
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Yang,B., Qu,M., Wang,R., Chatterton,J.E., Liu,X.B., Zhu,B.,
            Narisawa,S., Millan,J.L., Nakanishi,N., Swoboda,K., Lipton,S.A. and
            Zhang,D.
  TITLE     The critical role of membralin in postnatal motor neuron survival
            and disease
  JOURNAL   Elife 4, e06500 (2015)
   PUBMED   25977983
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Pearce,M.M., Wormer,D.B., Wilkens,S. and Wojcikiewicz,R.J.
  TITLE     An endoplasmic reticulum (ER) membrane complex composed of SPFH1
            and SPFH2 mediates the ER-associated degradation of inositol
            1,4,5-trisphosphate receptors
  JOURNAL   J Biol Chem 284 (16), 10433-10445 (2009)
   PUBMED   19240031
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Lyssand,J.S., DeFino,M.C., Tang,X.B., Hertz,A.L., Feller,D.B.,
            Wacker,J.L., Adams,M.E. and Hague,C.
  TITLE     Blood pressure is regulated by an alpha1D-adrenergic
            receptor/dystrophin signalosome
  JOURNAL   J Biol Chem 283 (27), 18792-18800 (2008)
   PUBMED   18468998
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Pearce,M.M., Wang,Y., Kelley,G.G. and Wojcikiewicz,R.J.
  TITLE     SPFH2 mediates the endoplasmic reticulum-associated degradation of
            inositol 1,4,5-trisphosphate receptors and other substrates in
            mammalian cells
  JOURNAL   J Biol Chem 282 (28), 20104-20115 (2007)
   PUBMED   17502376
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Bailey,P.J., Klos,J.M., Andersson,E., Karlen,M., Kallstrom,M.,
            Ponjavic,J., Muhr,J., Lenhard,B., Sandelin,A. and Ericson,J.
  TITLE     A global genomic transcriptional code associated with CNS-expressed
            genes
  JOURNAL   Exp Cell Res 312 (16), 3108-3119 (2006)
   PUBMED   16919269
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Carninci,P., Waki,K., Shiraki,T., Konno,H., Shibata,K., Itoh,M.,
            Aizawa,K., Arakawa,T., Ishii,Y., Sasaki,D., Bono,H., Kondo,S.,
            Sugahara,Y., Saito,R., Osato,N., Fukuda,S., Sato,K., Watahiki,A.,
            Hirozane-Kishikawa,T., Nakamura,M., Shibata,Y., Yasunishi,A.,
            Kikuchi,N., Yoshiki,A., Kusakabe,M., Gustincich,S., Beisel,K.,
            Pavan,W., Aidinis,V., Nakagawara,A., Held,W.A., Iwata,H., Kono,T.,
            Nakauchi,H., Lyons,P., Wells,C., Hume,D.A., Fagiolini,M.,
            Hensch,T.K., Brinkmeier,M., Camper,S., Hirota,J., Mombaerts,P.,
            Muramatsu,M., Okazaki,Y., Kawai,J. and Hayashizaki,Y.
  TITLE     Targeting a complex transcriptome: the construction of the mouse
            full-length cDNA encyclopedia
  JOURNAL   Genome Res 13 (6B), 1273-1289 (2003)
   PUBMED   12819125
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN458370.1, AK030557.1, AC115820.11 and CO042185.1.
            
            On Jun 19, 2018 this sequence version replaced XP_006509177.1.
            
            Transcript Variant: This variant (3) encodes the longest isoform
            (2). Variants 3 and 6 both encode the same isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.87571.1,
                                           SRR7345562.1263516.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 15.91 cM"
     Protein         1..364
                     /product="erlin-2 isoform 2"
                     /note="SPFH domain family, member 2; erlin-2; SPFH
                     domain-containing protein 2; endoplasmic reticulum lipid
                     raft-associated protein 2;
                     stomatin-prohibitin-flotillin-HflC/K domain-containing
                     protein 2"
                     /calculated_mol_wt=40342
     Region          40..332
                     /region_name="SPFH_like_u3"
                     /note="Uncharacterized family; SPFH (stomatin, prohibitin,
                     flotillin, and HflK/C) superfamily; cd03406"
                     /db_xref="CDD:259804"
     CDS             1..364
                     /gene="Erlin2"
                     /gene_synonym="Spfh2"
                     /coded_by="NM_001364477.1:126..1220"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:244373"
                     /db_xref="MGI:MGI:2387215"
ORIGIN      
        1 mgiilpqlrn gmltenkdtd tgslmaqlga vvavassffc aslfsavhki eeghigvyyr
       61 ggalltstsg pgfhlmlpfi tsyksvqttl qtdevknvpc gtsggvmiyf drievvnflv
      121 pnavydivkn ytadydkali fnkihhelnq fcsvhtlqev yielfdqide nlklalqqdl
      181 tsmapglviq avrvtkpnip eairrnyelm esektkllia aqkqkvveke aeterkkali
      241 eaekvaqvae itygqkvmek etekkiseie daaflareka kadaecytal kiaeanklkl
      301 tpeylqlmky kaiasnskiy fgkdipnmfm dsagglgkqf eglsddklgf gledepleap
      361 tken
//
LOCUS       NP_002429               1456 aa            linear   PRI 27-APR-2025
DEFINITION  macrophage mannose receptor 1 precursor [Homo sapiens].
ACCESSION   NP_002429 XP_003959976 XP_003959977
VERSION     NP_002429.1
DBSOURCE    REFSEQ: accession NM_002438.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1456)
  AUTHORS   Saadh,M.J., Pallathadka,H., Abed,H.S., Menon,S.V., Sivaprasad,G.V.,
            Hjazi,A., Rizaev,J., Suri,S., Jawad,M.A. and Husseen,B.
  TITLE     Detailed role of SR-A1 and SR-E3 in tumor biology, progression, and
            therapy
  JOURNAL   Cell Biochem Biophys 82 (3), 1735-1750 (2024)
   PUBMED   38884861
  REMARK    GeneRIF: Detailed role of SR-A1 and SR-E3 in tumor biology,
            progression, and therapy.
            Review article
REFERENCE   2  (residues 1 to 1456)
  AUTHORS   Mallorson,R., Miyagi,E., Kao,S., Sukegawa,S., Saito,H.,
            Fabryova,H., Morellatto Ruggieri,L., Mediouni,S., Valente,S.T. and
            Strebel,K.
  TITLE     Transcriptional regulation of the HIV-1 inhibitory factor human
            mannose receptor 1 by the myeloid-specific transcription factor
            PU.1
  JOURNAL   J Virol 98 (1), e0170223 (2024)
   PUBMED   38078733
  REMARK    GeneRIF: Transcriptional regulation of the HIV-1 inhibitory factor
            human mannose receptor 1 by the myeloid-specific transcription
            factor PU.1.
REFERENCE   3  (residues 1 to 1456)
  AUTHORS   Li,Y., Liu,X., Tian,M., Zou,R., Gao,Y., Huang,M., Zhou,K., Cao,M.
            and Cai,H.
  TITLE     Soluble CD206 levels correlate with disease deterioration and
            predict prognosis of anti-MDA5 antibody-positive dermatomyositis
            related interstitial lung disease
  JOURNAL   Clin Respir J 17 (6), 507-515 (2023)
   PUBMED   37041007
  REMARK    GeneRIF: Soluble CD206 levels correlate with disease deterioration
            and predict prognosis of anti-MDA5 antibody-positive
            dermatomyositis related interstitial lung disease.
REFERENCE   4  (residues 1 to 1456)
  AUTHORS   Aendekerk,J.P., Jiemy,W.F., Raveling-Eelsing,E., Bijnens,N.,
            Abdul-Hamid,M.A., Strating,I.M., Dekkema,G.J., Sanders,J.F.,
            Stegeman,C.A., Damoiseaux,J.G.M.C., Little,M.A., Heeringa,P. and
            van Paassen,P.
  TITLE     CD163 and CD206 expression define distinct macrophage subsets
            involved in active ANCA-associated glomerulonephritis
  JOURNAL   J Autoimmun 133, 102914 (2022)
   PUBMED   36183584
  REMARK    GeneRIF: CD163 and CD206 expression define distinct macrophage
            subsets involved in active ANCA-associated glomerulonephritis.
REFERENCE   5  (residues 1 to 1456)
  AUTHORS   An,X.N., Wei,Z.N., Xie,Y.Y., Xu,J., Shen,Y., Ni,L.Y., Shi,H.,
            Shen,P.Y., Zhang,W. and Chen,Y.X.
  TITLE     CD206+CD68+ mono-macrophages and serum soluble CD206 level are
            increased in antineutrophil cytoplasmic antibodies associated
            glomerulonephritis
  JOURNAL   BMC Immunol 23 (1), 55 (2022)
   PUBMED   36376784
  REMARK    GeneRIF: CD206[+]CD68[+] mono-macrophages and serum soluble CD206
            level are increased in antineutrophil cytoplasmic antibodies
            associated glomerulonephritis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1456)
  AUTHORS   Kim,S.J., Ruiz,N., Bezouska,K. and Drickamer,K.
  TITLE     Organization of the gene encoding the human macrophage mannose
            receptor (MRC1)
  JOURNAL   Genomics 14 (3), 721-727 (1992)
   PUBMED   1294118
REFERENCE   7  (residues 1 to 1456)
  AUTHORS   Taylor,M.E., Bezouska,K. and Drickamer,K.
  TITLE     Contribution to ligand binding by multiple carbohydrate-recognition
            domains in the macrophage mannose receptor
  JOURNAL   J Biol Chem 267 (3), 1719-1726 (1992)
   PUBMED   1730714
REFERENCE   8  (residues 1 to 1456)
  AUTHORS   Ezekowitz,R.A., Sastry,K., Bailly,P. and Warner,A.
  TITLE     Molecular characterization of the human macrophage mannose
            receptor: demonstration of multiple carbohydrate recognition-like
            domains and phagocytosis of yeasts in Cos-1 cells
  JOURNAL   J Exp Med 172 (6), 1785-1794 (1990)
   PUBMED   2258707
REFERENCE   9  (residues 1 to 1456)
  AUTHORS   Taylor,M.E., Conary,J.T., Lennartz,M.R., Stahl,P.D. and
            Drickamer,K.
  TITLE     Primary structure of the mannose receptor contains multiple motifs
            resembling carbohydrate-recognition domains
  JOURNAL   J Biol Chem 265 (21), 12156-12162 (1990)
   PUBMED   2373685
REFERENCE   10 (residues 1 to 1456)
  AUTHORS   Lennartz,M.R., Cole,F.S., Shepherd,V.L., Wileman,T.E. and
            Stahl,P.D.
  TITLE     Isolation and characterization of a mannose-specific endocytosis
            receptor from human placenta
  JOURNAL   J Biol Chem 262 (21), 9942-9944 (1987)
   PUBMED   3611070
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC296466.1, J05550.1,
            AL139238.13, AV659122.1 and AC069023.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 28, 2013 this sequence version replaced
            XP_003959976.1, XP_003959977.1.
            
            Summary: The recognition of complex carbohydrate structures on
            glycoproteins is an important part of several biological processes,
            including cell-cell recognition, serum glycoprotein turnover, and
            neutralization of pathogens. The protein encoded by this gene is a
            type I membrane receptor that mediates the endocytosis of
            glycoproteins by macrophages. The protein has been shown to bind
            high-mannose structures on the surface of potentially pathogenic
            viruses, bacteria, and fungi so that they can be neutralized by
            phagocytic engulfment.[provided by RefSeq, Sep 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J05550.1, X55635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000569591.3/ ENSP00000455897.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.33"
     Protein         1..1456
                     /product="macrophage mannose receptor 1 precursor"
                     /note="mannose receptor, C type 1-like 1; macrophage
                     mannose receptor 1-like protein 1; human mannose receptor;
                     C-type lectin domain family 13 member D"
                     /calculated_mol_wt=164121
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22897.1)"
                     /calculated_mol_wt=1909
     mat_peptide     19..1456
                     /product="Macrophage mannose receptor 1.
                     /id=PRO_0000017548"
                     /note="propagated from UniProtKB/Swiss-Prot (P22897.1)"
                     /calculated_mol_wt=164121
     Region          23..145
                     /region_name="beta-trefoil_Ricin_MRC1"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in macrophage mannose receptor 1 (MRC1) and similar
                     proteins; cd23407"
                     /db_xref="CDD:467785"
     Site            order(37..39,45,47,55..56)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467785"
     Site            order(76..77,87,89,97..98)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467785"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22897.1)"
     Site            order(118,121..122,130,132..137)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467785"
     Region          161..209
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(172,174,179,193,200,206,208)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          234..342
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cd00037"
                     /db_xref="CDD:153057"
     Site            order(314,318,320,326,328..331,334..336)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            344
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22897.1)"
     Region          362..487
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            order(461,465,467,472,474..477,480..482)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          504..626
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            529
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22897.1)"
     Site            order(598,602,604,610,613..616,619..621)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          659..779
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cd00037"
                     /db_xref="CDD:153057"
     Site            order(751,755,757,763,765..768,771..773)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          802..923
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            order(897,901,903,908,910..913,916..918)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            926
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22897.1)"
     Site            930
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22897.1)"
     Region          945..1080
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            order(1044,1054,1059,1065,1067..1070,1073..1075)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          1097..1213
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            1160
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22897.1)"
     Site            order(1192,1194,1198,1200..1203,1206..1208)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            1205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18780401; propagated from
                     UniProtKB/Swiss-Prot (P22897.1)"
     Region          1230..1356
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            order(1330,1334,1336,1341,1343..1346,1349..1351)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Site            1390..1410
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22897.1)"
     CDS             1..1456
                     /gene="MRC1"
                     /gene_synonym="bA541I19.1; CD206; CLEC13D; CLEC13DL; hMR;
                     MMR; MRC1L1"
                     /coded_by="NM_002438.4:119..4489"
                     /db_xref="CCDS:CCDS7123.2"
                     /db_xref="GeneID:4360"
                     /db_xref="HGNC:HGNC:7228"
                     /db_xref="MIM:153618"
ORIGIN      
        1 mrlplllvfa svipgavlll dtrqfliyne dhkrcvdavs psavqtaacn qdaesqkfrw
       61 vsesqimsva fklclgvpsk tdwvaitlya cdsksefqkw eckndtllgi kgedlffnyg
      121 nrqeknimly kgsglwsrwk iygttdnlcs rgyeamytll gnangatcaf pfkfenkwya
      181 dctsagrsdg wlwcgtttdy dtdklfgycp lkfegseslw nkdpltsvsy qinsksaltw
      241 hqarkscqqq naellsitei heqtyltglt ssltsglwig lnslsfnsgw qwsdrspfry
      301 lnwlpgspsa epgkscvsln pgknakwenl ecvqklgyic kkgnttlnsf vipsesdvpt
      361 hcpsqwwpya ghcykihrde kkiqrdaltt crkeggdlts ihtieeldfi isqlgyepnd
      421 elwiglndik iqmyfewsdg tpvtftkwlr gepshennrq edcvvmkgkd gywadrgcew
      481 plgyickmks rsqgpeivev ekgcrkgwkk hhfycymigh tlstfaeanq tcnnenaylt
      541 tiedryeqaf ltsfvglrpe kyfwtglsdi qtkgtfqwti eeevrfthwn sdmpgrkpgc
      601 vamrtgiagg lwdvlkcdek akfvckhwae gvthppkptt tpepkcpedw gassrtslcf
      661 klyakgkhek ktwfesrdfc ralggdlasi nnkeeqqtiw rlitasgsyh klfwlgltyg
      721 spsegftwsd gspvsyenwa ygepnnyqnv eycgelkgdp tmswndince hlnnwicqiq
      781 kgqtpkpept papqdnppvt edgwviykdy qyyfskeket mdnarafckr nfgdlvsiqs
      841 esekkflwky vnrndaqsay figllisldk kfawmdgskv dyvswatgep nfanedencv
      901 tmysnsgfwn dincgypnaf icqrhnssin attvmptmps vpsgckegwn fysnkcfkif
      961 gfmeeerknw qearkacigf ggnlvsiqne keqafltyhm kdstfsawtg lndvnsehtf
     1021 lwtdgrgvhy tnwgkgypgg rrsslsyeda dcvviiggas neagkwmddt cdskrgyicq
     1081 trsdpsltnp patiqtdgfv kygkssyslm rqkfqwheae tycklhnsli asildpysna
     1141 fawlqmetsn ervwialnsn ltdnqytwtd kwrvrytnwa adepklksac vyldldgywk
     1201 tahcnesfyf lckrsdeipa teppqlpgrc pesdhtawip fhghcyyies sytrnwgqas
     1261 leclrmgssl vsiesaaess flsyrveplk sktnfwiglf rnvegtwlwi nnspvsfvnw
     1321 ntgdpsgern dcvalhassg fwsnihcssy kgyickrpki idakpthell ttkadtrkmd
     1381 pskpssnvag vviivillil tgaglaayff ykkrrvhlpq egafentlyf nsqsspgtsd
     1441 mkdlvgnieq nehsvi
//
LOCUS       NP_659410               1274 aa            linear   PRI 27-APR-2025
DEFINITION  DENN domain-containing protein 5B isoform 1 [Homo sapiens].
ACCESSION   NP_659410
VERSION     NP_659410.3
DBSOURCE    REFSEQ: accession NM_144973.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1274)
  AUTHORS   Scala,M., Tomati,V., Ferla,M., Lena,M., Cohen,J.S., Fatemi,A.,
            Brokamp,E., Bican,A., Phillips,J.A. 3rd, Koziura,M.E.,
            Nicouleau,M., Rio,M., Siquier,K., Boddaert,N., Musante,I.,
            Tamburro,S., Baldassari,S., Iacomino,M., Scudieri,P.,
            Rosenfeld,J.A., Bellus,G., Reed,S., Al Saif,H., Russo,R.S.,
            Walsh,M.B., Cantagrel,V., Crunk,A., Gustincich,S., Ruggiero,S.M.,
            Fitzgerald,M.P., Helbig,I., Striano,P., Severino,M., Salpietro,V.,
            Pedemonte,N. and Zara,F.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     De novo variants in DENND5B cause a neurodevelopmental disorder
  JOURNAL   Am J Hum Genet 111 (3), 529-543 (2024)
   PUBMED   38387458
  REMARK    GeneRIF: De novo variants in DENND5B cause a neurodevelopmental
            disorder.
REFERENCE   2  (residues 1 to 1274)
  AUTHORS   Gordon,S.M., Neufeld,E.B., Yang,Z., Pryor,M., Freeman,L.A., Fan,X.,
            Kullo,I.J., Biesecker,L.G. and Remaley,A.T.
  TITLE     DENND5B Regulates Intestinal Triglyceride Absorption and Body Mass
  JOURNAL   Sci Rep 9 (1), 3597 (2019)
   PUBMED   30837651
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1274)
  AUTHORS   Yoshimura,S., Gerondopoulos,A., Linford,A., Rigden,D.J. and
            Barr,F.A.
  TITLE     Family-wide characterization of the DENN domain Rab GDP-GTP
            exchange factors
  JOURNAL   J Cell Biol 191 (2), 367-381 (2010)
   PUBMED   20937701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC022080.37, AI762929.1, BF513808.1, BC020855.1, AB209341.1,
            AC068792.31 and BM676905.1.
            
            On Jan 17, 2007 this sequence version replaced NP_659410.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389082.10/ ENSP00000373734.5
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.21"
     Protein         1..1274
                     /product="DENN domain-containing protein 5B isoform 1"
                     /note="DENN domain-containing protein 5B; rab6IP1-like
                     protein; DENN/MADD domain containing 5B"
                     /calculated_mol_wt=144889
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q6ZUT9.2)"
     Region          19..120
                     /region_name="uDENN"
                     /note="Domain always found upstream of DENN domain, found
                     in a variety of signalling proteins; smart00800"
                     /db_xref="CDD:214824"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2RSQ0; propagated from
                     UniProtKB/Swiss-Prot (Q6ZUT9.2)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2RSQ0; propagated from
                     UniProtKB/Swiss-Prot (Q6ZUT9.2)"
     Region          187..375
                     /region_name="DENN"
                     /note="DENN (AEX-3) domain; pfam02141"
                     /db_xref="CDD:460461"
     Region          499..574
                     /region_name="dDENN"
                     /note="Domain always found downstream of DENN domain,
                     found in a variety of signalling proteins; smart00801"
                     /db_xref="CDD:129037"
     Region          727..932
                     /region_name="RUN1_DENND5B"
                     /note="RUN1 domain found in DENN domain-containing protein
                     5B (DENND5B) and similar proteins; cd17691"
                     /db_xref="CDD:439053"
     Site            order(744,748,751,755,758,907,911,914..915,917,921..922)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439053"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6ZUT9.2)"
     Site            916..936
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZUT9.2)"
     Region          936..1044
                     /region_name="PLAT_RAB6IP1"
                     /note="PLAT/LH2 domain present in RAB6 interacting protein
                     1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an
                     eight stranded beta-barrel. In RabIP1 this domain may
                     participate in lipid-mediated modulation of Rab6IP1's
                     function via it's generally proposed...; cd01757"
                     /db_xref="CDD:238855"
     Site            1062
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAL8; propagated from
                     UniProtKB/Swiss-Prot (Q6ZUT9.2)"
     Site            1068
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAL8; propagated from
                     UniProtKB/Swiss-Prot (Q6ZUT9.2)"
     Site            1076
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6ZUT9.2)"
     Site            1079
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6IQ26; propagated from
                     UniProtKB/Swiss-Prot (Q6ZUT9.2)"
     Region          1091..1269
                     /region_name="RUN2_DENND5B"
                     /note="RUN2 domain found in DENN domain-containing protein
                     5B (DENND5B) and similar proteins; cd17693"
                     /db_xref="CDD:439055"
     CDS             1..1274
                     /gene="DENND5B"
                     /coded_by="NM_144973.4:305..4129"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44857.1"
                     /db_xref="GeneID:160518"
                     /db_xref="HGNC:HGNC:28338"
                     /db_xref="MIM:617279"
ORIGIN      
        1 msgscaapgp gsgsspaacr fahyfvlcgi dadsglepde lagenfdqsp lrrtfkskvl
       61 ahypqniewn pfdqdavnml cmpkglsfrt qtdnkdpqfh sfiitredgs rtygfvltfy
      121 eevtskqict amqtlyqmhn aehyssvyas sscsmdslas sldegdttsl lklqrynsyd
      181 isrdtlyvsk siclitplpf mqackkfliq lykavtsqqp pplplesyih nilyevplpp
      241 pgrslkfygv yepvicqrpg pselplsdyp lreafellgl enlvqvftcv llemqillys
      301 qdyqrlmtva egittllfpf qwqhvyvpil pasllhflda pvpylmglqs kegtdrskle
      361 lpqeanlcfv didnhfielp eefpqfpnkv dfiqelsevl vqfgippegs lhcsestskl
      421 knmvlkdlvn dkkngnvctn nismyellkg netiarlqal akrtgvavek mdlsaslgek
      481 dkdlklhcee aelrdyqlnv qlrevfanrf tqmfadyeaf viqtaqdmes wltnreqmqn
      541 fdkasflsdq pepylpflsr fietqmfatf idnkimsqwe ekdpllrvfd tridkirlyn
      601 vraptlrtsi yqkcstlkea aqsieqrlmk mdhtaihphl ldmkigqgky eqgffpklqs
      661 dvlatgptsn nrwvsrsata qrrkerlrqh sehvgldndl rekymqears lgknlrqpkl
      721 sdlspaviaq tnckfvegll kecrmktkrm lvekmgheav elghgeanit gleentlias
      781 lcdlleriws hglqvkqgks alwshliqfq dreekqehla espvalgper rksdsgvmlp
      841 tlrvsliqdm rhiqnmseik tdvgrarawi rlslekklls qhlkqllsnq pltkklykry
      901 aflrceeere qflyhllsln avdyfcftsv fttimipyrs viipikklsn aiitsnpwic
      961 vsgelgdtgv mqipknllem tfecqnlgkl ttvqighdns gllakwlvdc vmvrneitgh
     1021 tyrfpcgrwl gkgiddgsle riligelmts asdedlvkqc rtppqqkspt tarrlsitsl
     1081 tgknnkpnag qiqegigeav nnivkhfhkp ekergsltvl lcgenglvaa leqvfhhgfk
     1141 sarifhknvf iwdfiekvva yfettdqild neddvliqks scktfchyvn aintaprnig
     1201 kdgkfqilvc lgtrdrllpq wipllaecpa itrmyeesal lrdrmtvnsl irilqtiqdf
     1261 tivlegslik gvdv
//
LOCUS       NP_057323               3530 aa            linear   PRI 27-APR-2025
DEFINITION  unconventional myosin-XV [Homo sapiens].
ACCESSION   NP_057323
VERSION     NP_057323.3
DBSOURCE    REFSEQ: accession NM_016239.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3530)
  AUTHORS   Zheng,K., Lin,S., Gao,J., Chen,S., Su,J., Liu,Z. and Duan,S.
  TITLE     Novel compound heterozygous MYO15A splicing variants in autosomal
            recessive non-syndromic hearing loss
  JOURNAL   BMC Med Genomics 17 (1), 4 (2024)
   PUBMED   38167320
  REMARK    GeneRIF: Novel compound heterozygous MYO15A splicing variants in
            autosomal recessive non-syndromic hearing loss.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 3530)
  AUTHORS   Asaad,M., Mahfood,M., Al Mutery,A. and Tlili,A.
  TITLE     Loss-of-function mutations in MYO15A and OTOF cause non-syndromic
            hearing loss in two Yemeni families
  JOURNAL   Hum Genomics 17 (1), 42 (2023)
   PUBMED   37189200
  REMARK    GeneRIF: Loss-of-function mutations in MYO15A and OTOF cause
            non-syndromic hearing loss in two Yemeni families.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 3530)
  AUTHORS   Yoshino,H., Tatarano,S., Tamai,M., Tsuruda,M., Iizasa,S., Arima,J.,
            Kawakami,I., Fukumoto,W., Kawahara,I., Li,G., Sakaguchi,T.,
            Inoguchi,S., Yamada,Y. and Enokida,H.
  TITLE     Exosomal microRNA-1 and MYO15A as a target for therapy and
            diagnosis in renal cell carcinoma
  JOURNAL   Biochem Biophys Res Commun 630, 71-76 (2022)
   PUBMED   36150242
  REMARK    GeneRIF: Exosomal microRNA-1 and MYO15A as a target for therapy and
            diagnosis in renal cell carcinoma.
REFERENCE   4  (residues 1 to 3530)
  AUTHORS   Wang,L., Zhang,Y., Xue,Q., Huang,P. and Liu,X.
  TITLE     Identification of novel compound heterozygous mutations of the
            MYO15A gene with autosomal recessive non-syndromic hearing loss
  JOURNAL   J Clin Lab Anal 36 (10), e24653 (2022)
   PUBMED   36217262
  REMARK    GeneRIF: Identification of novel compound heterozygous mutations of
            the MYO15A gene with autosomal recessive non-syndromic hearing
            loss.
REFERENCE   5  (residues 1 to 3530)
  AUTHORS   Fu,Y., Huang,S., Gao,X., Han,M., Wang,G., Kang,D., Yuan,Y. and
            Dai,P.
  TITLE     Analysis of the genotype-phenotype correlation of MYO15A variants
            in Chinese non-syndromic hearing loss patients
  JOURNAL   BMC Med Genomics 15 (1), 71 (2022)
   PUBMED   35346193
  REMARK    GeneRIF: Analysis of the genotype-phenotype correlation of MYO15A
            variants in Chinese non-syndromic hearing loss patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 3530)
  AUTHORS   Anderson,D.W., Probst,F.J., Belyantseva,I.A., Fridell,R.A.,
            Beyer,L., Martin,D.M., Wu,D., Kachar,B., Friedman,T.B., Raphael,Y.
            and Camper,S.A.
  TITLE     The motor and tail regions of myosin XV are critical for normal
            structure and function of auditory and vestibular hair cells
  JOURNAL   Hum Mol Genet 9 (12), 1729-1738 (2000)
   PUBMED   10915760
REFERENCE   7  (residues 1 to 3530)
  AUTHORS   Liang,Y., Wang,A., Belyantseva,I.A., Anderson,D.W., Probst,F.J.,
            Barber,T.D., Miller,W., Touchman,J.W., Jin,L., Sullivan,S.L.,
            Sellers,J.R., Camper,S.A., Lloyd,R.V., Kachar,B., Friedman,T.B. and
            Fridell,R.A.
  TITLE     Characterization of the human and mouse unconventional myosin XV
            genes responsible for hereditary deafness DFNB3 and shaker 2
  JOURNAL   Genomics 61 (3), 243-258 (1999)
   PUBMED   10552926
REFERENCE   8  (residues 1 to 3530)
  AUTHORS   Wang,A., Liang,Y., Fridell,R.A., Probst,F.J., Wilcox,E.R.,
            Touchman,J.W., Morton,C.C., Morell,R.J., Noben-Trauth,K.,
            Camper,S.A. and Friedman,T.B.
  TITLE     Association of unconventional myosin MYO15 mutations with human
            nonsyndromic deafness DFNB3
  JOURNAL   Science 280 (5368), 1447-1451 (1998)
   PUBMED   9603736
REFERENCE   9  (residues 1 to 3530)
  AUTHORS   Friedman,T.B., Liang,Y., Weber,J.L., Hinnant,J.T., Barber,T.D.,
            Winata,S., Arhya,I.N. and Asher,J.H. Jr.
  TITLE     A gene for congenital, recessive deafness DFNB3 maps to the
            pericentromeric region of chromosome 17
  JOURNAL   Nat Genet 9 (1), 86-91 (1995)
   PUBMED   7704031
REFERENCE   10 (residues 1 to 3530)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087164.9 and AF144094.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 24, 2006 this sequence version replaced NP_057323.2.
            
            Summary: This gene encodes an unconventional myosin. This protein
            differs from other myosins in that it has a long N-terminal
            extension preceding the conserved motor domain. Studies in mice
            suggest that this protein is necessary for actin organization in
            the hair cells of the cochlea. Mutations in this gene have been
            associated with profound, congenital, neurosensory, nonsyndromal
            deafness. This gene is located within the Smith-Magenis syndrome
            region on chromosome 17. Read-through transcripts containing an
            upstream gene and this gene have been identified, but they are not
            thought to encode a fusion protein. Several alternatively spliced
            transcript variants have been described, but their full length
            sequences have not been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF144094.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000647165.2/ ENSP00000495481.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..3530
                     /product="unconventional myosin-XV"
                     /note="unconventional myosin-15; myosin-XV"
                     /calculated_mol_wt=395163
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN7.2)"
     Region          <320..364
                     /region_name="SGP"
                     /note="Sulphur globule protein; pfam17228"
                     /db_xref="CDD:435798"
     Region          615..710
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN7.2)"
     Region          <723..1144
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          730..1057
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN7.2)"
     Region          1236..1887
                     /region_name="MYSc_Myo15"
                     /note="class XV mammal-like myosin, motor domain; cd01387"
                     /db_xref="CDD:276838"
     Site            order(1263..1271,1315..1322,1360..1361,1366..1370,
                     1588..1593)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276838"
     Site            1263..1271
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276838"
     Site            1315..1322
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276838"
     Site            1360..1370
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276838"
     Site            1537
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:276838"
     Site            1588..1593
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276838"
     Site            order(1617..1628,1631..1640)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276838"
     Region          1792..1799
                     /region_name="Actin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN7.2)"
     Site            1820..1829
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276838"
     Site            order(1832..1852,1868..1874,1875..1887)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276838"
     Region          1888..2029
                     /region_name="Neck or regulatory domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN7.2)"
     Region          1925..1946
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     Region          2030..3530
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN7.2)"
     Region          2065..2217
                     /region_name="MyTH4"
                     /note="Domain in Myosin and Kinesin Tails; smart00139"
                     /db_xref="CDD:214535"
     Region          2311..2381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN7.2)"
     Region          2414..2446
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN7.2)"
     Region          <2432..2672
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          2490..2509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN7.2)"
     Region          2644..2665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN7.2)"
     Region          2871..2950
                     /region_name="SH3_MYO15A"
                     /note="Src Homology 3 domain of Myosin XVa; cd12067"
                     /db_xref="CDD:213000"
     Site            order(2876,2878,2881,2885,2930..2931,2944,2946..2947)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213000"
     Region          3050..3204
                     /region_name="MyTH4"
                     /note="Domain in Myosin and Kinesin Tails; smart00139"
                     /db_xref="CDD:214535"
     Region          3299..3419
                     /region_name="FERM_M"
                     /note="FERM central domain; pfam00373"
                     /db_xref="CDD:459788"
     Region          3415..3516
                     /region_name="FERM_C_MyoXV"
                     /note="FERM domain C-lobe of Myosin XV (MyoXV/Myo15);
                     cd13201"
                     /db_xref="CDD:270022"
     Site            order(3423,3444,3446,3454)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270022"
     Site            order(3458,3463..3466,3505,3509,3512..3513)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270022"
     Site            3505..3516
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270022"
     CDS             1..3530
                     /gene="MYO15A"
                     /gene_synonym="DFNB3; MYO15"
                     /coded_by="NM_016239.4:289..10881"
                     /db_xref="CCDS:CCDS42271.1"
                     /db_xref="GeneID:51168"
                     /db_xref="HGNC:HGNC:7594"
                     /db_xref="MIM:602666"
ORIGIN      
        1 makeedeekk akkgkkgkka pepekpkrsl kgtsrlfmgf rdrtpkiskk gqfrsasaff
       61 wglhtgpqkt krkrkartvl kstsklmtqm rmgkkkramk gkkpsfmvir fpgrrgygrl
      121 rprarslska stainwltkk fllkkaeesg seqatvdawl qrsssrmgsr klpfpsgaei
      181 lrpggrlrrf prsrsiyasg eplgflpfed eapfhhsgsr kslyglegfq dlgeyydyhr
      241 dgddyydrqs lhryeeqepy laglgpyspa wppygdhyyg yppedpydyy hpdyyggpfd
      301 pgytygygyd dyeppyapps gysspysyhd gyegeahpyg yyldpyapyd apyppydlpy
      361 htpydvpyfd pygvhytvpy aegvygggde aiyppevpyf ypeesasafv ypwvpppips
      421 phnpyahamd diaeleeped agverqgtsf rlpsaaffeq qgmdkparsk lslirkfrlf
      481 prpqvklfgk eklevplpps ldiplplgda deeedeeelp pvsavpyghp fwgfltprqr
      541 nlqralsafg ahrglgfgpe fgrpvprpat slarflkktl sekkpiarlr gsqkaraggp
      601 avreaaykrf gyklagmdpe kpgtpivlrr aqprarssnd arrppapqpa prtlshwsal
      661 lsppvpprpp ssgpppappl spalsglprp aspygslrrh pppwaapahv ppapqaswwa
      721 fveppavspe vppdllafpg prpsfrgsrr rgaafgfpga sprasrrraw splaspqpsl
      781 rsspglgycs plappspqls lrtgpfqppf lpparrprsl qespaprraa grlgppgspl
      841 pgsprppspp lglchsprrs slnlpsrlph twrrlseppt ravkpqvrlp fhrppragaw
      901 raplehresp repedsetpw tvpplapswd vdmpptqrpp spwpggagsr rgfsrpppvp
      961 enpflqllgp vpsptlqped paadmtrvfl grhhepgpgq ltksagptpe kpeeeatlgd
     1021 pqlpaetkpp tpappkdvtp pkditppkdv lpeqktlrps lsyplaacdq tratwppwhr
     1081 wgtlpqaaap lapirapepl pkggerrqaa pgrfavvmpr vqklssfqrv gpatlkpqvq
     1141 piqdpkprac slrwsclwlr adaygpwprv hthpqschlg pgaaclslrg sweevgppsw
     1201 rnkmhsirnl psmrfreqhg edgvedmtql edlqettvls nlkirfernl iytyigsilv
     1261 svnpyqmfgi ygpeqvqqyn gralgenpph lfavanlafa kmldakqnqc iiisgesgsg
     1321 kteatklilr ylaamnqkre vmqqikilea tpllesfgna ktvrndnssr fgkfveifle
     1381 ggvisgaits qylleksriv fqaknernyh ifyellaglp aqlrqafslq eaetyyylnq
     1441 ggnceiagks daddfrrlla amevlgfsse dqdsifrila silhlgnvyf ekyetdaqev
     1501 asvvsareiq avaellqisp eglqkaitfk vtetmrekif tpltvesavd ardaiakvly
     1561 allfswlitr vnalvsprqd tlsiaildiy gfedlsfnsf eqlcinyane nlqylfnkiv
     1621 fqeeqeeyir eqidwqeitf adnqpcinli slkpygilri lddqccfpqa tdhtflqkch
     1681 yhhganplys kpkmplpeft ikhyagkvty qvhkfldknh dqvrqdvldl fvrsrtrvva
     1741 hlfsshapqa apqrlgksss vtrlykahtv aakfqqslld lvekmercnp lfmrclkpnh
     1801 kkepglfepd vvmaqlrysg vletvrirke gfpvrlpfqg fidrycclva lkhdlpangd
     1861 mcvsvlsrlc kvmpnmyrvg vsklflkehl yqllesmreh vlnlaaltlq rclrgffikr
     1921 rfrslrhkii llqsrargyl arqryqqmrr slvkfrslvh ayvsrrrylk lraewrcqve
     1981 gallweqeel skrevvavgh levpaelagl lqavaglgla qvpqvapvrt prlqaeprvt
     2041 lpldinnypm akfvqchfke pafgmltvpl rtpltqlpae hhaeavsifk lilrfmgdph
     2101 lhgarenifg nyivqkglav pelrdeilaq lanqvwhnhn ahnaergwll laaclsgfap
     2161 spcfnkyllk fvsdygrngf qavcqhrlmq amgraqqqgs gaartlpptq lewtatyeka
     2221 smaldvgcfn gdqfscpvhs wstgeevagd ilrhrgladg wrgwtvamkn gvqwaelagh
     2281 dyvldlvsdl ellrdfprqk syfivgtegp aasrggpkvv fgnswdsded mstrpqpqeh
     2341 mpkvldsdgy sshnqdgtng eteaqrgtat hqesdslgep avphkgldcy ldslfdpvls
     2401 ygdadlekpt aiayrmkggg qpgggsssgt edtprrppep kpipgldast lalqqafihk
     2461 qavllaremt lqatalqqqp lsaalrslpa ekppapeaqp tsvgtgppak pvllratpkp
     2521 lapaplakap rlpikpvaap vlaqdqaspe ttspspelvr ystlnsehfp qptqqikniv
     2581 rqyqqpfrgg rpealrkdgg kvfmkrpdph eealmilkgq mthlaaapgt qvsreavalv
     2641 kpvtsaprps maptsalpsr sleppeeltq trlhrlinpn fygyqdapwk iflrkevfyp
     2701 kdsyshpvql dllfrqilhd tlseaclris ederlrmkal faqnqldtqk plvtesvkra
     2761 vvstardtwe vyfsrifpat gsvgtgvqll avshvgikll rmvkggqeag gqlrvlrays
     2821 fadilfvtmp sqnmlefnla sekvilfsar ahqvktlvdd filelkkdsd yvvavrnflp
     2881 edpallafhk gdiihlqple pprvgysagc vvrrkvvyle elrrrgpdfg wrfgtihgrv
     2941 grfpselvqp aaapdflqlp tepgrgraaa vaaavasaaa aqevgrrreg ppvrarsadh
     3001 gedalalppy tmlefaqkyf rdpqrrpqdg lrlkskepre srtledmlcf tktplqesli
     3061 elsdsslskm atdmflavmr fmgdaplkgq sdldvlcnll klcgdhevmr decycqvvkq
     3121 itdntsskqd scqrgwrlly ivtayhscse vlhphltrfl qdvsrtpglp fqgiakaceq
     3181 nlqktlrfgg rlelpssiel ramlagrssk rqlfllpggl erhlkiktct valdvveeic
     3241 aemaltrpea fneyvifvvt nrgqhvcpls rrayildvas emeqvdggym lwfrrvlwdq
     3301 plkfenelyv tmhynqvlpd ylkglfssvp asrpseqllq qvsklaslqh rakdhfylps
     3361 vrevqeyipa qlyrttagst wlnlvsqhrq qtqalsphqa raqflgllsa lpmfgssfff
     3421 iqscsniavp apcilainhn glnflsteth elmvkfplke iqstrtqrpt anssypyvei
     3481 algdvaaqrt lqlqleqgle lcrvvavhve nllsahekrl tlppseitll
//
LOCUS       NP_060872                171 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-26 precursor [Homo sapiens].
ACCESSION   NP_060872
VERSION     NP_060872.1
DBSOURCE    REFSEQ: accession NM_018402.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Niu,Q., Wang,M. and Liu,X.S.
  TITLE     The evolving landscape of IL-10, IL-22 and IL-26 in pleurisy
            especially in tuberculous pleurisy
  JOURNAL   Respir Res 25 (1), 275 (2024)
   PUBMED   39003443
  REMARK    GeneRIF: The evolving landscape of IL-10, IL-22 and IL-26 in
            pleurisy especially in tuberculous pleurisy.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Hammitzsch,A., Ossadnik,A., Bachmann,Q., Merwald-Fraenk,H.,
            Lorenz,G., Witt,M., Wiesent,F., Muhlhofer,H., Simone,D.,
            Bowness,P., Heemann,U., Arbogast,M., Moog,P. and Schmaderer,C.
  TITLE     Increased interleukin-26 in the peripheral joints of patients with
            axial spondyloarthritis and psoriatic arthritis, co-localizing with
            CD68-positive synoviocytes
  JOURNAL   Front Immunol 15, 1355824 (2024)
   PUBMED   38799447
  REMARK    GeneRIF: Increased interleukin-26 in the peripheral joints of
            patients with axial spondyloarthritis and psoriatic arthritis,
            co-localizing with CD68-positive synoviocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Kovach,M.A., Kack,U., Che,K.F., Brundin,B., Konradsen,J.R. and
            Linden,A.
  TITLE     Systemic IL-26 correlates with improved asthma control in children
            sensitized to dog allergen
  JOURNAL   Respir Res 25 (1), 163 (2024)
   PUBMED   38622712
  REMARK    GeneRIF: Systemic IL-26 correlates with improved asthma control in
            children sensitized to dog allergen.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 171)
  AUTHORS   He,W., Qian,Q.W., Liu,Q.Y., Li,Y.K., Miao,Q., Wang,Q.X., Ma,X.,
            You,Z.R. and Tang,R.Q.
  TITLE     IL-26 modulates T cell function in autoimmune hepatitis
  JOURNAL   J Dig Dis 24 (3), 231-242 (2023)
   PUBMED   37155188
  REMARK    GeneRIF: IL-26 modulates T cell function in autoimmune hepatitis.
REFERENCE   5  (residues 1 to 171)
  AUTHORS   Mizuno,Y., Shibata,S., Ito,Y., Taira,H., Sugimoto,E., Awaji,K. and
            Sato,S.
  TITLE     Interleukin-26-DNA complexes promote inflammation and
            dermal-epidermal separation in a modified human cryosection model
            of bullous pemphigoid
  JOURNAL   Front Immunol 13, 1013382 (2022)
   PUBMED   36311716
  REMARK    GeneRIF: Interleukin-26-DNA complexes promote inflammation and
            dermal-epidermal separation in a modified human cryosection model
            of bullous pemphigoid.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 171)
  AUTHORS   Hor,S., Pirzer,H., Dumoutier,L., Bauer,F., Wittmann,S., Sticht,H.,
            Renauld,J.C., de Waal Malefyt,R. and Fickenscher,H.
  TITLE     The T-cell lymphokine interleukin-26 targets epithelial cells
            through the interleukin-20 receptor 1 and interleukin-10 receptor 2
            chains
  JOURNAL   J Biol Chem 279 (32), 33343-33351 (2004)
   PUBMED   15178681
  REMARK    GeneRIF: sensitivity to recombinant interleukin-26(IL-26) of
            various cell lines strictly correlated with the expression of IL-20
            receptor 1 and blocking antibodies against either IL-10 receptor 2
            or IL-20 receptor 1 inhibited IL-26-dependent signal transduction
REFERENCE   7  (residues 1 to 171)
  AUTHORS   Sheikh,F., Baurin,V.V., Lewis-Antes,A., Shah,N.K., Smirnov,S.V.,
            Anantha,S., Dickensheets,H., Dumoutier,L., Renauld,J.C., Zdanov,A.,
            Donnelly,R.P. and Kotenko,S.V.
  TITLE     Cutting edge: IL-26 signals through a novel receptor complex
            composed of IL-20 receptor 1 and IL-10 receptor 2
  JOURNAL   J Immunol 172 (4), 2006-2010 (2004)
   PUBMED   14764663
  REMARK    GeneRIF: The active receptor complex for IL-26 is a heterodimer
            composed of two receptor proteins: IL-20 receptor 1 and IL-10
            receptor 2. Signaling through the IL-26 receptor results in
            activation of STAT1 and STAT3.
REFERENCE   8  (residues 1 to 171)
  AUTHORS   Vandenbroeck,K., Cunningham,S., Goris,A., Alloza,I., Heggarty,S.,
            Graham,C., Bell,A. and Rooney,M.
  TITLE     Polymorphisms in the interferon-gamma/interleukin-26 gene region
            contribute to sex bias in susceptibility to rheumatoid arthritis
  JOURNAL   Arthritis Rheum 48 (10), 2773-2778 (2003)
   PUBMED   14558082
  REMARK    GeneRIF: common polymorphisms in the IFNgamma/IL-26 gene region may
            contribute to sex bias in susceptibility to rheumatoid arthritis,
            by distorting the propensity of female carriers versus male
            carriers to contract this disease.
REFERENCE   9  (residues 1 to 171)
  AUTHORS   Goris,A., Marrosu,M.G. and Vandenbroeck,K.
  TITLE     Novel polymorphisms in the IL-10 related AK155 gene (chromosome
            12q15)
  JOURNAL   Genes Immun 2 (5), 284-286 (2001)
   PUBMED   11528524
REFERENCE   10 (residues 1 to 171)
  AUTHORS   Knappe,A., Hor,S., Wittmann,S. and Fickenscher,H.
  TITLE     Induction of a novel cellular homolog of interleukin-10, AK155, by
            transformation of T lymphocytes with herpesvirus saimiri
  JOURNAL   J Virol 74 (8), 3881-3887 (2000)
   PUBMED   10729163
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007458.14 and AJ251549.1.
            
            Summary: This gene was identified by its overexpression
            specifically in herpesvirus samimiri-transformed T cells. The
            encoded protein is a member of the IL10 family of cytokines. It is
            a secreted protein and may function as a homodimer. This protein is
            thought to contribute to the transformed phenotype of T cells after
            infection by herpesvirus samimiri. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ251549.1, CF271979.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA2142586 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000229134.5/ ENSP00000229134.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..171
                     /product="interleukin-26 precursor"
                     /calculated_mol_wt=17587
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2274
     mat_peptide     22..171
                     /product="interleukin-26"
                     /calculated_mol_wt=17587
     Region          <79..164
                     /region_name="IL10"
                     /note="Interleukin 10; cl02501"
                     /db_xref="CDD:413341"
     CDS             1..171
                     /gene="IL26"
                     /gene_synonym="AK155; IL-26"
                     /coded_by="NM_018402.2:55..570"
                     /db_xref="CCDS:CCDS8981.1"
                     /db_xref="GeneID:55801"
                     /db_xref="HGNC:HGNC:17119"
                     /db_xref="MIM:605679"
ORIGIN      
        1 mlvnfilrcg lllvtlslai akhkqssftk scyprgtlsq avdalyikaa wlkatipedr
       61 iknirllkkk tkkqfmkncq fqeqllsffm edvfgqlqlq gckkirfved fhslrqklsh
      121 ciscassare mksitrmkri fyrignkgiy kaiseldill swikklless q
//
LOCUS       NP_001012777             515 aa            linear   PRI 27-APR-2025
DEFINITION  cytoplasmic tRNA 2-thiolation protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001012777 XP_001129676
VERSION     NP_001012777.1
DBSOURCE    REFSEQ: accession NM_001012759.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Xue,C., Wei,Z., Zhang,Y., Liu,Y., Zhang,S., Li,Q., Feng,K.,
            Yang,X., Liu,G., Chen,Y., Li,X., Yao,Z., Han,J. and Duan,Y.
  TITLE     Activation of CTU2 expression by LXR promotes the development of
            hepatocellular carcinoma
  JOURNAL   Cell Biol Toxicol 40 (1), 23 (2024)
   PUBMED   38630355
  REMARK    GeneRIF: Activation of CTU2 expression by LXR promotes the
            development of hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Shaheen,R., Mark,P., Prevost,C.T., AlKindi,A., Alhag,A.,
            Estwani,F., Al-Sheddi,T., Alobeid,E., Alenazi,M.M., Ewida,N.,
            Ibrahim,N., Hashem,M., Abdulwahab,F., Bryant,E.M., Spinelli,E.,
            Millichap,J., Barnett,S.S., Kearney,H.M., Accogli,A., Scala,M.,
            Capra,V., Nigro,V., Fu,D. and Alkuraya,F.S.
  TITLE     Biallelic variants in CTU2 cause DREAM-PL syndrome and impair
            thiolation of tRNA wobble U34
  JOURNAL   Hum Mutat 40 (11), 2108-2120 (2019)
   PUBMED   31301155
  REMARK    GeneRIF: Our data establish a recognizable CTU2-linked autosomal
            recessive syndrome in humans characterized by defective thiolation
            of the wobble uridine. The potential deleterious consequences for
            the translational efficiency and fidelity during development as a
            mechanism for pathogenicity represent an attractive target of
            future investigations.
            Erratum:[Hum Mutat. 2021 Feb;42(2):219. doi: 10.1002/humu.24157.
            PMID: 33559988]
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Chaste,P., Klei,L., Sanders,S.J., Hus,V., Murtha,M.T., Lowe,J.K.,
            Willsey,A.J., Moreno-De-Luca,D., Yu,T.W., Fombonne,E.,
            Geschwind,D., Grice,D.E., Ledbetter,D.H., Mane,S.M., Martin,D.M.,
            Morrow,E.M., Walsh,C.A., Sutcliffe,J.S., Lese Martin,C.,
            Beaudet,A.L., Lord,C., State,M.W., Cook,E.H. Jr. and Devlin,B.
  TITLE     A genome-wide association study of autism using the Simons Simplex
            Collection: Does reducing phenotypic heterogeneity in autism
            increase genetic homogeneity?
  JOURNAL   Biol Psychiatry 77 (9), 775-784 (2015)
   PUBMED   25534755
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Lango Allen,H., Estrada,K., Lettre,G., Berndt,S.I., Weedon,M.N.,
            Rivadeneira,F., Willer,C.J., Jackson,A.U., Vedantam,S.,
            Raychaudhuri,S., Ferreira,T., Wood,A.R., Weyant,R.J., Segre,A.V.,
            Speliotes,E.K., Wheeler,E., Soranzo,N., Park,J.H., Yang,J.,
            Gudbjartsson,D., Heard-Costa,N.L., Randall,J.C., Qi,L., Vernon
            Smith,A., Magi,R., Pastinen,T., Liang,L., Heid,I.M., Luan,J.,
            Thorleifsson,G., Winkler,T.W., Goddard,M.E., Sin Lo,K., Palmer,C.,
            Workalemahu,T., Aulchenko,Y.S., Johansson,A., Zillikens,M.C.,
            Feitosa,M.F., Esko,T., Johnson,T., Ketkar,S., Kraft,P., Mangino,M.,
            Prokopenko,I., Absher,D., Albrecht,E., Ernst,F., Glazer,N.L.,
            Hayward,C., Hottenga,J.J., Jacobs,K.B., Knowles,J.W., Kutalik,Z.,
            Monda,K.L., Polasek,O., Preuss,M., Rayner,N.W., Robertson,N.R.,
            Steinthorsdottir,V., Tyrer,J.P., Voight,B.F., Wiklund,F., Xu,J.,
            Zhao,J.H., Nyholt,D.R., Pellikka,N., Perola,M., Perry,J.R.,
            Surakka,I., Tammesoo,M.L., Altmaier,E.L., Amin,N., Aspelund,T.,
            Bhangale,T., Boucher,G., Chasman,D.I., Chen,C., Coin,L.,
            Cooper,M.N., Dixon,A.L., Gibson,Q., Grundberg,E., Hao,K., Juhani
            Junttila,M., Kaplan,L.M., Kettunen,J., Konig,I.R., Kwan,T.,
            Lawrence,R.W., Levinson,D.F., Lorentzon,M., McKnight,B.,
            Morris,A.P., Muller,M., Suh Ngwa,J., Purcell,S., Rafelt,S.,
            Salem,R.M., Salvi,E., Sanna,S., Shi,J., Sovio,U., Thompson,J.R.,
            Turchin,M.C., Vandenput,L., Verlaan,D.J., Vitart,V., White,C.C.,
            Ziegler,A., Almgren,P., Balmforth,A.J., Campbell,H., Citterio,L.,
            De Grandi,A., Dominiczak,A., Duan,J., Elliott,P., Elosua,R.,
            Eriksson,J.G., Freimer,N.B., Geus,E.J., Glorioso,N., Haiqing,S.,
            Hartikainen,A.L., Havulinna,A.S., Hicks,A.A., Hui,J., Igl,W.,
            Illig,T., Jula,A., Kajantie,E., Kilpelainen,T.O., Koiranen,M.,
            Kolcic,I., Koskinen,S., Kovacs,P., Laitinen,J., Liu,J., Lokki,M.L.,
            Marusic,A., Maschio,A., Meitinger,T., Mulas,A., Pare,G.,
            Parker,A.N., Peden,J.F., Petersmann,A., Pichler,I.,
            Pietilainen,K.H., Pouta,A., Ridderstrale,M., Rotter,J.I.,
            Sambrook,J.G., Sanders,A.R., Schmidt,C.O., Sinisalo,J., Smit,J.H.,
            Stringham,H.M., Bragi Walters,G., Widen,E., Wild,S.H.,
            Willemsen,G., Zagato,L., Zgaga,L., Zitting,P., Alavere,H.,
            Farrall,M., McArdle,W.L., Nelis,M., Peters,M.J., Ripatti,S., van
            Meurs,J.B., Aben,K.K., Ardlie,K.G., Beckmann,J.S., Beilby,J.P.,
            Bergman,R.N., Bergmann,S., Collins,F.S., Cusi,D., den Heijer,M.,
            Eiriksdottir,G., Gejman,P.V., Hall,A.S., Hamsten,A., Huikuri,H.V.,
            Iribarren,C., Kahonen,M., Kaprio,J., Kathiresan,S., Kiemeney,L.,
            Kocher,T., Launer,L.J., Lehtimaki,T., Melander,O., Mosley,T.H. Jr.,
            Musk,A.W., Nieminen,M.S., O'Donnell,C.J., Ohlsson,C., Oostra,B.,
            Palmer,L.J., Raitakari,O., Ridker,P.M., Rioux,J.D., Rissanen,A.,
            Rivolta,C., Schunkert,H., Shuldiner,A.R., Siscovick,D.S.,
            Stumvoll,M., Tonjes,A., Tuomilehto,J., van Ommen,G.J., Viikari,J.,
            Heath,A.C., Martin,N.G., Montgomery,G.W., Province,M.A., Kayser,M.,
            Arnold,A.M., Atwood,L.D., Boerwinkle,E., Chanock,S.J., Deloukas,P.,
            Gieger,C., Gronberg,H., Hall,P., Hattersley,A.T., Hengstenberg,C.,
            Hoffman,W., Lathrop,G.M., Salomaa,V., Schreiber,S., Uda,M.,
            Waterworth,D., Wright,A.F., Assimes,T.L., Barroso,I., Hofman,A.,
            Mohlke,K.L., Boomsma,D.I., Caulfield,M.J., Cupples,L.A.,
            Erdmann,J., Fox,C.S., Gudnason,V., Gyllensten,U., Harris,T.B.,
            Hayes,R.B., Jarvelin,M.R., Mooser,V., Munroe,P.B., Ouwehand,W.H.,
            Penninx,B.W., Pramstaller,P.P., Quertermous,T., Rudan,I.,
            Samani,N.J., Spector,T.D., Volzke,H., Watkins,H., Wilson,J.F.,
            Groop,L.C., Haritunians,T., Hu,F.B., Kaplan,R.C., Metspalu,A.,
            North,K.E., Schlessinger,D., Wareham,N.J., Hunter,D.J.,
            O'Connell,J.R., Strachan,D.P., Wichmann,H.E., Borecki,I.B., van
            Duijn,C.M., Schadt,E.E., Thorsteinsdottir,U., Peltonen,L.,
            Uitterlinden,A.G., Visscher,P.M., Chatterjee,N., Loos,R.J.,
            Boehnke,M., McCarthy,M.I., Ingelsson,E., Lindgren,C.M.,
            Abecasis,G.R., Stefansson,K., Frayling,T.M. and Hirschhorn,J.N.
  TITLE     Hundreds of variants clustered in genomic loci and biological
            pathways affect human height
  JOURNAL   Nature 467 (7317), 832-838 (2010)
   PUBMED   20881960
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Schlieker,C.D., Van der Veen,A.G., Damon,J.R., Spooner,E. and
            Ploegh,H.L.
  TITLE     A functional proteomics approach links the ubiquitin-related
            modifier Urm1 to a tRNA modification pathway
  JOURNAL   Proc Natl Acad Sci U S A 105 (47), 18255-18260 (2008)
   PUBMED   19017811
  REMARK    GeneRIF: Identifies the product of this gene as being involved in
            tRNA modification.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC125269.1, AA448486.1,
            BC080540.1 and AC138028.1.
            
            On Sep 20, 2006 this sequence version replaced XP_001129676.1.
            
            Summary: This gene encodes a protein which is involved in the
            post-transcriptional modification of transfer RNAs (tRNAs). The
            encoded protein plays a role in thiolation of uridine residue
            present at the wobble position in a subset of tRNAs, resulting in
            enhanced codon reading accuracy. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 3. It
            encodes isoform 1, which lacks an internal in-frame segment and is
            shorter, compared to isoform 3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1162382.1,
                                           SRR3476690.364587.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000453996.7/ ENSP00000388320.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..515
                     /product="cytoplasmic tRNA 2-thiolation protein 2 isoform
                     1"
                     /note="cytoplasmic tRNA 2-thiolation protein 2; cytosolic
                     thiouridylase subunit 2 homolog"
                     /calculated_mol_wt=55976
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2VPK5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylcysteine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q2VPK5.1)"
     Region          58..371
                     /region_name="TilS"
                     /note="tRNA(Ile)-lysidine synthase TilS/MesJ [Translation,
                     ribosomal structure and biogenesis]; COG0037"
                     /db_xref="CDD:439807"
     Region          188..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2VPK5.1)"
     Region          341..468
                     /region_name="CTU2"
                     /note="Cytoplasmic tRNA 2-thiolation protein 2; pfam10288"
                     /db_xref="CDD:463044"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q2VPK5.1)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q2VPK5.1)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2VPK5.1)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q2VPK5.1)"
     CDS             1..515
                     /gene="CTU2"
                     /gene_synonym="C16orf84; MFRG; NCS2; UPF0432"
                     /coded_by="NM_001012759.3:29..1576"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45545.1"
                     /db_xref="GeneID:348180"
                     /db_xref="HGNC:HGNC:28005"
                     /db_xref="MIM:617057"
ORIGIN      
        1 mcqvgedyge papeepppap rpsreqkcvk ckeaqpvvvi ragdafcrdc fkafyvhkfr
       61 amlgknrlif pgekvllaws ggpssssmvw qvleglsqds akrlrfvagv ifvdegaacg
      121 qsleersktl aevkpilqat gfpwhvvale evfslppsvl wcsaqelvgs egaykaavds
      181 flqqqhvlga gggpgptqge eqppqppldp qnlarppapa qtealsqlfc svrtltakee
      241 llqtlrthli lhmarahgys kvmtgdsctr laiklmtnla lgrgaflawd tgfsderhgd
      301 vvvvrpmrdh tlkevafynr lfsvpsvftp avdtkapeka sihrlmeafi lrlqtqfpst
      361 vstvyrtsek lvkgprdgpa agdsgprcll cmcaldvdaa dsatafgaqt ssrlsqmqsp
      421 ipltetrtpp gpccspgvgw aqrcgqgacr redpqaciee qlcyscrvnm kdlpsldplp
      481 pyilaeaqlr tqrawglqei rdcliedsdd eagqs
//
LOCUS       NP_001352177             486 aa            linear   PRI 27-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 3
            [Homo sapiens].
ACCESSION   NP_001352177
VERSION     NP_001352177.1
DBSOURCE    REFSEQ: accession NM_001365248.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Zhang,S., Huang,J., Lan,Z., Xiao,Y., Liao,Y., Basnet,S., Huang,P.,
            Li,Y., Yan,J., Sheng,Y., Zhou,W., Liu,Q., Tan,H., Tan,Y., Yuan,L.,
            Wang,L., Dai,L., Zhang,W. and Du,C.
  TITLE     CPEB1 Controls NRF2 Proteostasis and Ferroptosis Susceptibility in
            Pancreatic Cancer
  JOURNAL   Int J Biol Sci 20 (8), 3156-3172 (2024)
   PUBMED   38904009
  REMARK    GeneRIF: CPEB1 Controls NRF2 Proteostasis and Ferroptosis
            Susceptibility in Pancreatic Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Pico,S., Parras,A., Santos-Galindo,M., Pose-Utrilla,J., Castro,M.,
            Fraga,E., Hernandez,I.H., Elorza,A., Anta,H., Wang,N.,
            Marti-Sanchez,L., Belloc,E., Garcia-Esparcia,P., Garrido,J.J.,
            Ferrer,I., Macias-Garcia,D., Mir,P., Artuch,R., Perez,B.,
            Hernandez,F., Navarro,P., Lopez-Sendon,J.L., Iglesias,T.,
            Yang,X.W., Mendez,R. and Lucas,J.J.
  TITLE     CPEB alteration and aberrant transcriptome-polyadenylation lead to
            a treatable SLC19A3 deficiency in Huntington's disease
  JOURNAL   Sci Transl Med 13 (613), eabe7104 (2021)
   PUBMED   34586830
  REMARK    GeneRIF: CPEB alteration and aberrant transcriptome-polyadenylation
            lead to a treatable SLC19A3 deficiency in Huntington's disease.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Shao,K., Pu,W., Zhang,J., Guo,S., Qian,F., Glurich,I., Jin,Q.,
            Ma,Y., Ju,S., Zhang,Z. and Ding,W.
  TITLE     DNA hypermethylation contributes to colorectal cancer metastasis by
            regulating the binding of CEBPB and TFCP2 to the CPEB1 promoter
  JOURNAL   Clin Epigenetics 13 (1), 89 (2021)
   PUBMED   33892791
  REMARK    GeneRIF: DNA hypermethylation contributes to colorectal cancer
            metastasis by regulating the binding of CEBPB and TFCP2 to the
            CPEB1 promoter.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Sovijit,W., Sovijit,W., Ishii,Y., Kambe,J., Fujita,T., Watanabe,G.,
            Yamaguchi,H. and Nagaoka,K.
  TITLE     Estrogen promotes increased breast cancer cell proliferation and
            migration through downregulation of CPEB1 expression
  JOURNAL   Biochem Biophys Res Commun 534, 871-876 (2021)
   PUBMED   33162033
  REMARK    GeneRIF: Estrogen promotes increased breast cancer cell
            proliferation and migration through downregulation of CPEB1
            expression.
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Jiao,W., Zhao,S., Liu,R., Guo,T. and Qin,Y.
  TITLE     CPEB1 deletion is not a common explanation for premature ovarian
            insufficiency in a Chinese cohort
  JOURNAL   J Ovarian Res 13 (1), 49 (2020)
   PUBMED   32354341
  REMARK    GeneRIF: CPEB1 deletion is not a common explanation for premature
            ovarian insufficiency in a Chinese cohort.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Hagele,S., Kuhn,U., Boning,M. and Katschinski,D.M.
  TITLE     Cytoplasmic polyadenylation-element-binding protein (CPEB)1 and 2
            bind to the HIF-1alpha mRNA 3'-UTR and modulate HIF-1alpha protein
            expression
  JOURNAL   Biochem J 417 (1), 235-246 (2009)
   PUBMED   18752464
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Sasayama,T., Marumoto,T., Kunitoku,N., Zhang,D., Tamaki,N.,
            Kohmura,E., Saya,H. and Hirota,T.
  TITLE     Over-expression of Aurora-A targets cytoplasmic polyadenylation
            element binding protein and promotes mRNA polyadenylation of Cdk1
            and cyclin B1
  JOURNAL   Genes Cells 10 (7), 627-638 (2005)
   PUBMED   15966895
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Wilczynska,A., Aigueperse,C., Kress,M., Dautry,F. and Weil,D.
  TITLE     The translational regulator CPEB1 provides a link between dcp1
            bodies and stress granules
  JOURNAL   J Cell Sci 118 (Pt 5), 981-992 (2005)
   PUBMED   15731006
  REMARK    GeneRIF: CPEB1 has a role in compartmentalization of mRNA
            metabolism in the cytoplasm, between dcp1 bodies and stress
            granules
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Mendez,R. and Richter,J.D.
  TITLE     Translational control by CPEB: a means to the end
  JOURNAL   Nat Rev Mol Cell Biol 2 (7), 521-529 (2001)
   PUBMED   11433366
  REMARK    Review article
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Welk,J.F., Charlesworth,A., Smith,G.D. and MacNicol,A.M.
  TITLE     Identification and characterization of the gene encoding human
            cytoplasmic polyadenylation element binding protein
  JOURNAL   Gene 263 (1-2), 113-120 (2001)
   PUBMED   11223249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245033.2.
            
            Summary: This gene encodes a member of the cytoplasmic
            polyadenylation element binding protein family. This highly
            conserved protein binds to a specific RNA sequence, called the
            cytoplasmic polyadenylation element, found in the 3' untranslated
            region of some mRNAs. The encoded protein functions in both the
            cytoplasm and the nucleus. It is involved in the regulation of mRNA
            translation, as well as processing of the 3' untranslated region,
            and may play a role in cell proliferation and tumorigenesis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.79098.1,
                                           SRR1803616.243843.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..486
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 3"
                     /note="CPE-binding protein 1"
                     /calculated_mol_wt=53504
     Region          <1..232
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          234..336
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          347..430
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          424..479
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..486
                     /gene="CPEB1"
                     /gene_synonym="CPE-BP1; CPEB; CPEB-1; h-CPEB; hCPEB-1"
                     /coded_by="NM_001365248.1:201..1661"
                     /note="isoform 3 is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS45330.2"
                     /db_xref="GeneID:64506"
                     /db_xref="HGNC:HGNC:21744"
                     /db_xref="MIM:607342"
ORIGIN      
        1 mlfptsaqes srglpdandl clglqslslt gwdrpwstqd sdssaqssth svlsmlhnpl
       61 gnvlgkppls flpldplgsd lvdkfpapsv rgsrldtrpi ldsrssspsd sdtsgfssgs
      121 dhlsdlissl rispplpfls lsgggprdpl kmgvgsrmdq eqaalaavtp sptsaskrwp
      181 gasvwpswdl leapkdpfsi erearlhrqa aavneatctw sgqlpprnyk npiysckvfl
      241 ggvpwditea glvntfrvfg slsvewpgkd gkhprcppkg yvylvfelek svrsllqacs
      301 hdplspdgls eyyfkmssrr mrckevqvip wvladsnfvr spsqrldpsr tvfvgalhgm
      361 lnaealaail ndlfggvvya gidtdkhkyp igsgrvtfnn qrsylkavsa afveikttkf
      421 tkkvqidpyl edslchicss qpgpffcrdq vcfkyfcrsc whwrhsmegl rhhsplmrnq
      481 knrdss
//
LOCUS       NP_054872                971 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger CCCH domain-containing protein 7A [Homo sapiens].
ACCESSION   NP_054872
VERSION     NP_054872.2
DBSOURCE    REFSEQ: accession NM_014153.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 971)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 971)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 971)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 971)
  AUTHORS   Newton-Cheh,C., Eijgelsheim,M., Rice,K.M., de Bakker,P.I., Yin,X.,
            Estrada,K., Bis,J.C., Marciante,K., Rivadeneira,F.,
            Noseworthy,P.A., Sotoodehnia,N., Smith,N.L., Rotter,J.I.,
            Kors,J.A., Witteman,J.C., Hofman,A., Heckbert,S.R., O'Donnell,C.J.,
            Uitterlinden,A.G., Psaty,B.M., Lumley,T., Larson,M.G. and
            Stricker,B.H.
  TITLE     Common variants at ten loci influence QT interval duration in the
            QTGEN Study
  JOURNAL   Nat Genet 41 (4), 399-406 (2009)
   PUBMED   19305408
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA160892.1, BC046363.1 and AY163807.1.
            
            On Dec 30, 2002 this sequence version replaced NP_054872.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC046363.1, SRR11853564.10389.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355758.9/ ENSP00000347999.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.13"
     Protein         1..971
                     /product="zinc finger CCCH domain-containing protein 7A"
                     /note="zinc finger CCCH-type domain containing 7;
                     zinc-finger protein AY163807"
                     /calculated_mol_wt=110407
     Region          6..>169
                     /region_name="3a0801s09"
                     /note="mitochondrial precursor proteins import receptor
                     (72 kDa mitochondrial outermembrane protein)
                     (mitochondrial import receptor for the ADP/ATP carrier)
                     (translocase of outermembrane tom70); TIGR00990"
                     /db_xref="CDD:273380"
     Region          43..76
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWR0.1)"
     Region          46..71
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(47..48,51..52,54,90,93..94,97..98,100..101,124,
                     127..128,131..132,135)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          86..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          89..122
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWR0.1)"
     Region          123..149
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          124..156
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWR0.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IWR0.1)"
     Region          857..882
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          859..881
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          906..926
                     /region_name="ZnF_C3H1"
                     /note="zinc finger; smart00356"
                     /db_xref="CDD:214632"
     CDS             1..971
                     /gene="ZC3H7A"
                     /gene_synonym="HSPC055; ZC3H7; ZC3HDC7"
                     /coded_by="NM_014153.4:170..3085"
                     /db_xref="CCDS:CCDS10550.1"
                     /db_xref="GeneID:29066"
                     /db_xref="HGNC:HGNC:30959"
                     /db_xref="MIM:619819"
ORIGIN      
        1 msnvseerrk rqqnikeglq fiqsplsypg tqeqyavylr alvrnlfneg ndvyrehdwn
       61 nsisqyteal niadyaksee ilipkeiiek lyinriacys nmgfhdkvle dcnivlslna
      121 snckalyrks kalsdlgryk kaydavakcs lavpqdehvi kltqelaqkl gfkirkayvr
      181 aelslksvpg dgatkalnhs vediepdllt prqeavpvvs lpapsfshev gselasvpvm
      241 pltsilplqv eesalpsavl anggkmpftm peaflddgdm vlgdelddll dsapetnetv
      301 mpsalvrgpl qtasvspsmp fsasllgtlp igaryappps fsefypplts sledfcssln
      361 sfsmseskrd lststsregt plnnsnssll lmngpgslfa senflgissq prndfgnffg
      421 savtkpsssv tprhplegth elrqacqicf vksgpklmdf tyhanidhkc kkdiligrik
      481 nvedkswkki rprptktnye gpyyickdva aeeecrysgh ctfaycqeei dvwtlerkga
      541 fsreaffggn gkinltvfkl lqehlgefif lcekcfdhkp rmiskrnkdn stacshpvtk
      601 hefednkclv hilrettvky skirsfhgqc qldlcrhevr ygclredecf yahslvelkv
      661 wimqnetgis hdaiaqeskr ywqnleanvp gaqvlgnqim pgflnmkikf vcaqclrngq
      721 viepdknrky csakarhswt kdrramrvms ierkkwmnir plptkkqmpl qfdlcnhias
      781 gkkcqyvgnc sfahspeere vwtymkengi qdmeqfyelw lksqknekse diasqsnken
      841 gkqihmptdy aevtvdfhcw mcgkncnsek qwqghissek hkekvfhted dqycwqhrfp
      901 tgyfsicdry mngtcpegns ckfahgnael heweerrdal kmklnkarkd hligpndndf
      961 gkysflfkdl n
//
LOCUS       NP_116016                385 aa            linear   PRI 27-APR-2025
DEFINITION  single-stranded DNA-binding protein 4 isoform a [Homo sapiens].
ACCESSION   NP_116016
VERSION     NP_116016.1
DBSOURCE    REFSEQ: accession NM_032627.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Michailidou,K., Hall,P., Gonzalez-Neira,A., Ghoussaini,M.,
            Dennis,J., Milne,R.L., Schmidt,M.K., Chang-Claude,J., Bojesen,S.E.,
            Bolla,M.K., Wang,Q., Dicks,E., Lee,A., Turnbull,C., Rahman,N.,
            Fletcher,O., Peto,J., Gibson,L., Dos Santos Silva,I.,
            Nevanlinna,H., Muranen,T.A., Aittomaki,K., Blomqvist,C., Czene,K.,
            Irwanto,A., Liu,J., Waisfisz,Q., Meijers-Heijboer,H., Adank,M., van
            der Luijt,R.B., Hein,R., Dahmen,N., Beckman,L., Meindl,A.,
            Schmutzler,R.K., Muller-Myhsok,B., Lichtner,P., Hopper,J.L.,
            Southey,M.C., Makalic,E., Schmidt,D.F., Uitterlinden,A.G.,
            Hofman,A., Hunter,D.J., Chanock,S.J., Vincent,D., Bacot,F.,
            Tessier,D.C., Canisius,S., Wessels,L.F., Haiman,C.A., Shah,M.,
            Luben,R., Brown,J., Luccarini,C., Schoof,N., Humphreys,K., Li,J.,
            Nordestgaard,B.G., Nielsen,S.F., Flyger,H., Couch,F.J., Wang,X.,
            Vachon,C., Stevens,K.N., Lambrechts,D., Moisse,M., Paridaens,R.,
            Christiaens,M.R., Rudolph,A., Nickels,S., Flesch-Janys,D.,
            Johnson,N., Aitken,Z., Aaltonen,K., Heikkinen,T., Broeks,A.,
            Veer,L.J., van der Schoot,C.E., Guenel,P., Truong,T.,
            Laurent-Puig,P., Menegaux,F., Marme,F., Schneeweiss,A., Sohn,C.,
            Burwinkel,B., Zamora,M.P., Perez,J.I., Pita,G., Alonso,M.R.,
            Cox,A., Brock,I.W., Cross,S.S., Reed,M.W., Sawyer,E.J.,
            Tomlinson,I., Kerin,M.J., Miller,N., Henderson,B.E., Schumacher,F.,
            Le Marchand,L., Andrulis,I.L., Knight,J.A., Glendon,G.,
            Mulligan,A.M., Lindblom,A., Margolin,S., Hooning,M.J.,
            Hollestelle,A., van den Ouweland,A.M., Jager,A., Bui,Q.M.,
            Stone,J., Dite,G.S., Apicella,C., Tsimiklis,H., Giles,G.G.,
            Severi,G., Baglietto,L., Fasching,P.A., Haeberle,L., Ekici,A.B.,
            Beckmann,M.W., Brenner,H., Muller,H., Arndt,V., Stegmaier,C.,
            Swerdlow,A., Ashworth,A., Orr,N., Jones,M., Figueroa,J.,
            Lissowska,J., Brinton,L., Goldberg,M.S., Labreche,F., Dumont,M.,
            Winqvist,R., Pylkas,K., Jukkola-Vuorinen,A., Grip,M., Brauch,H.,
            Hamann,U., Bruning,T., Radice,P., Peterlongo,P., Manoukian,S.,
            Bonanni,B., Devilee,P., Tollenaar,R.A., Seynaeve,C., van
            Asperen,C.J., Jakubowska,A., Lubinski,J., Jaworska,K., Durda,K.,
            Mannermaa,A., Kataja,V., Kosma,V.M., Hartikainen,J.M.,
            Bogdanova,N.V., Antonenkova,N.N., Dork,T., Kristensen,V.N.,
            Anton-Culver,H., Slager,S., Toland,A.E., Edge,S., Fostira,F.,
            Kang,D., Yoo,K.Y., Noh,D.Y., Matsuo,K., Ito,H., Iwata,H., Sueta,A.,
            Wu,A.H., Tseng,C.C., Van Den Berg,D., Stram,D.O., Shu,X.O., Lu,W.,
            Gao,Y.T., Cai,H., Teo,S.H., Yip,C.H., Phuah,S.Y., Cornes,B.K.,
            Hartman,M., Miao,H., Lim,W.Y., Sng,J.H., Muir,K., Lophatananon,A.,
            Stewart-Brown,S., Siriwanarangsan,P., Shen,C.Y., Hsiung,C.N.,
            Wu,P.E., Ding,S.L., Sangrajrang,S., Gaborieau,V., Brennan,P.,
            McKay,J., Blot,W.J., Signorello,L.B., Cai,Q., Zheng,W.,
            Deming-Halverson,S., Shrubsole,M., Long,J., Simard,J.,
            Garcia-Closas,M., Pharoah,P.D., Chenevix-Trench,G., Dunning,A.M.,
            Benitez,J. and Easton,D.F.
  CONSRTM   Breast and Ovarian Cancer Susceptibility Collaboration; Hereditary
            Breast and Ovarian Cancer Research Group Netherlands (HEBON);
            kConFab Investigators; Australian Ovarian Cancer Study Group;
            GENICA (Gene Environment Interaction and Breast Cancer in Germany)
            Network
  TITLE     Large-scale genotyping identifies 41 new loci associated with
            breast cancer risk
  JOURNAL   Nat Genet 45 (4), 353-361 (2013)
   PUBMED   23535729
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Ravasi,T., Suzuki,H., Cannistraci,C.V., Katayama,S., Bajic,V.B.,
            Tan,K., Akalin,A., Schmeier,S., Kanamori-Katayama,M., Bertin,N.,
            Carninci,P., Daub,C.O., Forrest,A.R., Gough,J., Grimmond,S.,
            Han,J.H., Hashimoto,T., Hide,W., Hofmann,O., Kamburov,A., Kaur,M.,
            Kawaji,H., Kubosaki,A., Lassmann,T., van Nimwegen,E.,
            MacPherson,C.R., Ogawa,C., Radovanovic,A., Schwartz,A.,
            Teasdale,R.D., Tegner,J., Lenhard,B., Teichmann,S.A., Arakawa,T.,
            Ninomiya,N., Murakami,K., Tagami,M., Fukuda,S., Imamura,K., Kai,C.,
            Ishihara,R., Kitazume,Y., Kawai,J., Hume,D.A., Ideker,T. and
            Hayashizaki,Y.
  TITLE     An atlas of combinatorial transcriptional regulation in mouse and
            man
  JOURNAL   Cell 140 (5), 744-752 (2010)
   PUBMED   20211142
  REMARK    Erratum:[Cell. 2010 Apr 16;141(2):369. Kamburov, Atanas [added];
            Kaur, Mandeep [added]; MacPherson, Cameron Ross [added];
            Radovanovic, Aleksandar [added]; Schwartz, Ariel [added]]
REFERENCE   8  (residues 1 to 385)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 385)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 385)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CX873722.1 and BC000274.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000274.1, SRR1163658.145525.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270061.12/ ENSP00000270061.5
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..385
                     /product="single-stranded DNA-binding protein 4 isoform a"
                     /calculated_mol_wt=39257
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BWG4.1)"
     Region          18..44
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          82..360
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     Region          122..287
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BWG4.1)"
     Region          331..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BWG4.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BWG4.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BWG4.1)"
     CDS             1..385
                     /gene="SSBP4"
                     /coded_by="NM_032627.5:252..1409"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12378.1"
                     /db_xref="GeneID:170463"
                     /db_xref="HGNC:HGNC:15676"
                     /db_xref="MIM:607391"
ORIGIN      
        1 myakggkgsa vpsdsqarek lalyvyeyll higaqksaqt flseirwekn itlgeppgfl
       61 hswwcvfwdl ycaapdrrea cehsgeakaf qdysaaaaps pvmgsmapgd tmaagsmaag
      121 ffqgppgsqp sphnpnapmm gphgqpfmsp rfpggprptl rmpsqppagl pgsqpllpga
      181 mepspraqgh psmggpmqrv tpprgmasvg pqsygggmrp ppnslagpgl pamnmgpgvr
      241 gpwaspsgns ipysssspgs ytgppggggp pgtpimpspg dstnssenmy timnpigqga
      301 granfplgpg pegpmaamsa mephhvngsl gsgdmdglpk sspgavagls napgtprddg
      361 emaaagtflh pfpsesyspg mtmsv
//
LOCUS       NP_008850                390 aa            linear   PRI 27-APR-2025
DEFINITION  serpin B3 [Homo sapiens].
ACCESSION   NP_008850
VERSION     NP_008850.1
DBSOURCE    REFSEQ: accession NM_006919.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Martini,A., Turato,C., Cannito,S., Quarta,S., Biasiolo,A.,
            Ruvoletto,M., Novo,E., Marafatto,F., Guerra,P., Tonon,M.,
            Clemente,N., Bocca,C., Piano,S.S., Guido,M., Gregori,D., Parola,M.,
            Angeli,P. and Pontisso,P.
  TITLE     The polymorphic variant of SerpinB3 (SerpinB3-PD) is associated
            with faster cirrhosis decompensation
  JOURNAL   Aliment Pharmacol Ther 59 (3), 380-392 (2024)
   PUBMED   37990490
  REMARK    GeneRIF: The polymorphic variant of SerpinB3 (SerpinB3-PD) is
            associated with faster cirrhosis decompensation.
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Ohara,Y., Tang,W., Liu,H., Yang,S., Dorsey,T.H., Cawley,H.,
            Moreno,P., Chari,R., Guest,M.R., Azizian,A., Gaedcke,J.,
            Ghadimi,M., Hanna,N., Ambs,S. and Hussain,S.P.
  TITLE     SERPINB3-MYC axis induces the basal-like/squamous subtype and
            enhances disease progression in pancreatic cancer
  JOURNAL   Cell Rep 42 (12), 113434 (2023)
   PUBMED   37980563
  REMARK    GeneRIF: SERPINB3-MYC axis induces the basal-like/squamous subtype
            and enhances disease progression in pancreatic cancer.
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Novo,E., Cappon,A., Villano,G., Quarta,S., Cannito,S., Bocca,C.,
            Turato,C., Guido,M., Maggiora,M., Protopapa,F., Sutti,S.,
            Provera,A., Ruvoletto,M., Biasiolo,A., Foglia,B., Albano,E.,
            Pontisso,P. and Parola,M.
  TITLE     SerpinB3 as a Pro-Inflammatory Mediator in the Progression of
            Experimental Non-Alcoholic Fatty Liver Disease
  JOURNAL   Front Immunol 13, 910526 (2022)
   PUBMED   35874657
  REMARK    GeneRIF: SerpinB3 as a Pro-Inflammatory Mediator in the Progression
            of Experimental Non-Alcoholic Fatty Liver Disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Luke,C.J., Markovina,S., Good,M., Wight,I.E., Thomas,B.J.,
            Linneman,J.M., Lanik,W.E., Koroleva,O., Coffman,M.R., Miedel,M.T.,
            Gong,Q., Andress,A., Campos Guerrero,M., Wang,S., Chen,L.,
            Beatty,W.L., Hausmann,K.N., White,F.V., Fitzpatrick,J.A.J.,
            Orvedahl,A., Pak,S.C. and Silverman,G.A.
  TITLE     Lysoptosis is an evolutionarily conserved cell death pathway
            moderated by intracellular serpins
  JOURNAL   Commun Biol 5 (1), 47 (2022)
   PUBMED   35022507
  REMARK    GeneRIF: Lysoptosis is an evolutionarily conserved cell death
            pathway moderated by intracellular serpins.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Ran,C., Sun,J., Qu,Y. and Long,N.
  TITLE     Clinical value of MRI, serum SCCA, and CA125 levels in the
            diagnosis of lymph node metastasis and para-uterine infiltration in
            cervical cancer
  JOURNAL   World J Surg Oncol 19 (1), 343 (2021)
   PUBMED   34886853
  REMARK    GeneRIF: Clinical value of MRI, serum SCCA, and CA125 levels in the
            diagnosis of lymph node metastasis and para-uterine infiltration in
            cervical cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Schick,C., Pemberton,P.A., Shi,G.P., Kamachi,Y., Cataltepe,S.,
            Bartuski,A.J., Gornstein,E.R., Bromme,D., Chapman,H.A. and
            Silverman,G.A.
  TITLE     Cross-class inhibition of the cysteine proteinases cathepsins K, L,
            and S by the serpin squamous cell carcinoma antigen 1: a kinetic
            analysis
  JOURNAL   Biochemistry 37 (15), 5258-5266 (1998)
   PUBMED   9548757
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Schneider,S.S., Schick,C., Fish,K.E., Miller,E., Pena,J.C.,
            Treter,S.D., Hui,S.M. and Silverman,G.A.
  TITLE     A serine proteinase inhibitor locus at 18q21.3 contains a tandem
            duplication of the human squamous cell carcinoma antigen gene
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3147-3151 (1995)
   PUBMED   7724531
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Suminami,Y., Kishi,F., Sekiguchi,K. and Kato,H.
  TITLE     Squamous cell carcinoma antigen is a new member of the serine
            protease inhibitors
  JOURNAL   Biochem Biophys Res Commun 181 (1), 51-58 (1991)
   PUBMED   1958219
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Mino-Miyagawa,N., Kimura,Y. and Hamamoto,K.
  TITLE     Tumor-antigen 4. Its immunohistochemical distribution and tissue
            and serum concentrations in squamous cell carcinoma of the lung and
            esophagus
  JOURNAL   Cancer 66 (7), 1505-1512 (1990)
   PUBMED   2208001
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Mino,N., Iio,A. and Hamamoto,K.
  TITLE     Availability of tumor-antigen 4 as a marker of squamous cell
            carcinoma of the lung and other organs
  JOURNAL   Cancer 62 (4), 730-734 (1988)
   PUBMED   2840187
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB229922.1, U19556.1 and AK222746.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222746.1, AK222753.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283752.10/ ENSP00000283752.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.33"
     Protein         1..390
                     /product="serpin B3"
                     /note="squamous cell carcinoma antigen 1; serine (or
                     cysteine) proteinase inhibitor, clade B (ovalbumin),
                     member 3; protein T4-A; serpin peptidase inhibitor, clade
                     B (ovalbumin), member 3"
                     /calculated_mol_wt=44434
     Region          1..390
                     /region_name="serpinB3_B4_SCCA1_2"
                     /note="serpin family B members 3 and 4, squamous cell
                     carcinoma antigens 1 and 2; cd19563"
                     /db_xref="CDD:381030"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.13;
                     propagated from UniProtKB/Swiss-Prot (P29508.2)"
     Site            order(337..357,359..368)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381030"
     Site            354..355
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P29508.2)"
     CDS             1..390
                     /gene="SERPINB3"
                     /gene_synonym="HsT1196; SCC; SCCA-1; SCCA-PD; SCCA1;
                     SSCA1; T4-A"
                     /coded_by="NM_006919.3:75..1247"
                     /db_xref="CCDS:CCDS11987.1"
                     /db_xref="GeneID:6317"
                     /db_xref="HGNC:HGNC:10569"
                     /db_xref="MIM:600517"
ORIGIN      
        1 mnslseantk fmfdlfqqfr kskennifys pisitsalgm vllgakdnta qqikkvlhfd
       61 qvtenttgka atyhvdrsgn vhhqfqkllt efnkstdaye lkianklfge ktylflqeyl
      121 daikkfyqts vesvdfanap eesrkkinsw vesqtnekik nlipegnigs nttlvlvnai
      181 yfkgqwekkf nkedtkeekf wpnkntyksi qmmrqytsfh fasledvqak vleipykgkd
      241 lsmivllpne idglqkleek ltaeklmewt slqnmretrv dlhlprfkve esydlkdtlr
      301 tmgmvdifng dadlsgmtgs rglvlsgvlh kafvevteeg aeaaaatavv gfgssptstn
      361 eefhcnhpfl ffirqnktns ilfygrfssp
//
LOCUS       NP_940973                369 aa            linear   PRI 27-APR-2025
DEFINITION  probable N-acetyltransferase 16 [Homo sapiens].
ACCESSION   NP_940973 XP_351736
VERSION     NP_940973.2
DBSOURCE    REFSEQ: accession NM_198571.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Yamada,S. and Arikawa,S.
  TITLE     An ectotherm homologue of human predicted gene NAT16 encodes
            histidine N-acetyltransferase responsible for
            Nalpha-acetylhistidine synthesis
  JOURNAL   Biochim Biophys Acta 1840 (1), 434-442 (2014)
   PUBMED   24121108
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004876.2, AK096556.1, BC037583.1 and BU740913.1.
            
            On Jan 16, 2010 this sequence version replaced NP_940973.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic and transcript sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096556.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2145743,
                                           SAMEA2154405 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300303.7/ ENSP00000300303.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..369
                     /product="probable N-acetyltransferase 16"
                     /note="putative N-acetyltransferase C7orf52; putative
                     N-acetyltransferase 16; N-acetyltransferase 16
                     (GCN5-related, putative)"
                     /calculated_mol_wt=40390
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8M0.2)"
     Region          58..>167
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     CDS             1..369
                     /gene="NAT16"
                     /gene_synonym="C7orf52"
                     /coded_by="NM_198571.3:257..1366"
                     /db_xref="CCDS:CCDS5713.1"
                     /db_xref="GeneID:375607"
                     /db_xref="HGNC:HGNC:22030"
                     /db_xref="MIM:615783"
ORIGIN      
        1 mkleascgta tsevpkpekk tardaepsse trpqeveaep rsgsgpeaea epldfvvate
       61 refeevlais ggiyggldyl psryhswlrd pdrtvvlakr nggvialesv nvidagetvl
      121 veglrvapwe rgkgvagllq rfcsqlvkrq hpgvkvarlt rddqlgprel kkyrlitkqg
      181 illvrfnasa llaglgarla alrtsgtfsp lpteavseag gdvarlllsp svqrdvlpgg
      241 tiiqdwqpyr psesnlrlla akglewrvds rarprvltlc trpfpiphgg dgtwrylnid
      301 afgsdgaqvq sqllwhlqrq aprlvglnvm cqlflepqlw sqladfcqvg lglelvkgyt
      361 eqylleadi
//
LOCUS       NP_001348963             808 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 13 [Mus musculus].
ACCESSION   NP_001348963 XP_017169145
VERSION     NP_001348963.1
DBSOURCE    REFSEQ: accession NM_001362034.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 808)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 808)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 808)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 808)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 808)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 808)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 808)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            On Mar 31, 2018 this sequence version replaced XP_017169145.1.
            
            Transcript Variant: This variant (44), as well as variant 45,
            encodes isoform 13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164131
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..808
                     /product="cAMP-regulated phosphoprotein 21 isoform 13"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=87922
     Region          162..223
                     /region_name="R3H_encore_like"
                     /note="R3H domain of encore-like and DIP1-like proteins.
                     Drosophila encore is involved in the germline exit after
                     four mitotic divisions, by facilitating
                     SCF-ubiquitin-proteasome-dependent proteolysis. Maize
                     DBF1-interactor protein 1 (DIP1) containing an R3H...;
                     cd02642"
                     /db_xref="CDD:100071"
     Site            order(195,199)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100071"
     Region          554..>783
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..808
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362034.1:434..2860"
                     /note="isoform 13 is encoded by transcript variant 44"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqesih lqlssfpslq eedksrkdds erekekdknr
      121 eklserpkir mlskdcsqey tdstgidlhg flintlknns rdrmillkme qemidfiads
      181 nnhykkfpqm ssyqrmlvhr vaayfgldhn vdqtgksvii nktsstripe qrfcehlkde
      241 kseesqkrfi lkrdnssidk ednqsvcsqe slfldnrlqe dmhicnetyk krqlfrahrd
      301 ssgrtsgsrq sssetelrwp dhqrawsstd sdssnrnlkp tmtktasfgg itvltrgdst
      361 sstrsagkls ktgsessssa gssgslsrth pqstaltssv aagspgcmay sengmggqvp
      421 psstsyillp lesatgippg sillnphtgq pfvnpdgtpa iynppgsqqt lrgtvggqpq
      481 qppqqqpspq pqqqvqasqp qmagplvtqs vqslqpssqs vqypavsfpp qhllpmsptq
      541 hfplreelaa qfsqlsmsrq ssgdtpepps gtvypasllp qtaqpqsyvi tsagqqlstg
      601 gfsdsgppis qqvlqappsp qgfvqqpppa qmsvyyypsg qyptstsqqy rplasvqysa
      661 qrsqqipqtt qqagyqpvls gqqgfqgmmg vqqsahsqgv mssqqgapvh gvmvsyptms
      721 syqvpmtqgs qavpqqtyqp pimlpsqagq gslpatgmpv ycnvtppnpq nnlrlmgphc
      781 psstvpvmsa scrtncgnvs nagwqvkf
//
LOCUS       NP_060134                420 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 10 isoform 1 [Homo
            sapiens].
ACCESSION   NP_060134
VERSION     NP_060134.2
DBSOURCE    REFSEQ: accession NM_017664.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK000100.1, AK094222.1 and AL157875.27.
            
            On Jul 19, 2005 this sequence version replaced NP_060134.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000100.1, SRR3476690.677112.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267339.6/ ENSP00000267339.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..420
                     /product="ankyrin repeat domain-containing protein 10
                     isoform 1"
                     /note="ankyrin repeat domain-containing protein 10"
                     /calculated_mol_wt=44637
     Region          21..50
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXR5.2)"
     Region          <25..179
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(57,59,63..64,67..69,71..72,76,79,89,91,93,97..98,
                     101..103,105..106,110,113,122,124,126,130..131,134..136,
                     138..139,143,146,155)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          57..89
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          57..86
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXR5.2)"
     Region          91..122
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          91..120
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXR5.2)"
     Region          124..155
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          124..153
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXR5.2)"
     CDS             1..420
                     /gene="ANKRD10"
                     /coded_by="NM_017664.4:136..1398"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9520.1"
                     /db_xref="GeneID:55608"
                     /db_xref="HGNC:HGNC:20265"
ORIGIN      
        1 msaagagagv eagfsseell slrfplhrac rdgdlatlcs llqqtphahl asedsfygwt
       61 pvhwaahfgk leclvqlvra gatlnvsttr yaqtpahiaa fgghpqclvw liqaganink
      121 pdcegetpih kaarsgslec isalvangah vdlrnasglt aadiaqtqgf qecaqfllnl
      181 qnchlnhfyn ngilngghqn vfpnhisvgt nrkrcledse dfgvkkarte aqsldsavpl
      241 tngdteddad kmhvdrefav vtdmknsssv sntltngcvi nghldfpstt plsgmesrng
      301 qcltgtngis sglapgqpfp ssqgslcisg teepektlra npelcgslhl ngspsscias
      361 rpswvedigd nlyyghyhgf gdtaesipel nsvvehsksv kvqerydsav lgtmhlhhgs
//
LOCUS       NP_001355245             531 aa            linear   ROD 27-APR-2025
DEFINITION  beta-2-syntrophin isoform 1 [Mus musculus].
ACCESSION   NP_001355245
VERSION     NP_001355245.1
DBSOURCE    REFSEQ: accession NM_001368316.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Rein-Fischboeck,L., Pohl,R., Haberl,E.M., Mages,W., Girke,P.,
            Liebisch,G., Krautbauer,S. and Buechler,C.
  TITLE     Lower adiposity does not protect beta-2 syntrophin null mice from
            hepatic steatosis and inflammation in experimental non-alcoholic
            steatohepatitis
  JOURNAL   Gene 859, 147209 (2023)
   PUBMED   36681100
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Kim,M.J., Whitehead,N.P., Bible,K.L., Adams,M.E. and Froehner,S.C.
  TITLE     Mice lacking alpha-, beta1- and beta2-syntrophins exhibit
            diminished function and reduced dystrophin expression in both
            cardiac and skeletal muscle
  JOURNAL   Hum Mol Genet 28 (3), 386-395 (2019)
   PUBMED   30256963
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Krautbauer,S., Neumeier,M., Rein-Fischboeck,L., Haberl,E.M.,
            Tilg,H., Eisinger,K. and Buechler,C.
  TITLE     Adipocyte Hypertrophy and Improved Postprandial Lipid Response in
            Beta 2 Syntrophin Deficient Mice
  JOURNAL   Cell Physiol Biochem 52 (5), 1151-1165 (2019)
   PUBMED   30990585
  REMARK    GeneRIF: Current study shows that high SNTB2 in obese adipose
            tissues restricts adipocyte growth and thereby may contribute to
            metabolic diseases.
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Hebel,T., Eisinger,K., Neumeier,M., Rein-Fischboeck,L., Pohl,R.,
            Meier,E.M., Boettcher,A., Froehner,S.C., Adams,M.E., Liebisch,G.,
            Krautbauer,S. and Buechler,C.
  TITLE     Lipid abnormalities in alpha/beta2-syntrophin null mice are
            independent from ABCA1
  JOURNAL   Biochim Biophys Acta 1851 (5), 527-536 (2015)
   PUBMED   25625330
  REMARK    GeneRIF: Suggest alpha/beta2-syntrophins do not regulate ABCA1
            activity and insulin release but may have a role in regulating
            glucose uptake, ERK and SR-BI levels, and sphingomyelin metabolism
            in obesity.
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Kim,M.J., Froehner,S.C., Adams,M.E. and Kim,H.S.
  TITLE     alpha-Syntrophin is required for the hepatocyte growth
            factor-induced migration of cultured myoblasts
  JOURNAL   Exp Cell Res 317 (20), 2914-2924 (2011)
   PUBMED   22001117
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Ahn,A.H., Freener,C.A., Gussoni,E., Yoshida,M., Ozawa,E. and
            Kunkel,L.M.
  TITLE     The three human syntrophin genes are expressed in diverse tissues,
            have distinct chromosomal locations, and each bind to dystrophin
            and its relatives
  JOURNAL   J Biol Chem 271 (5), 2724-2730 (1996)
   PUBMED   8576247
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Adams,M.E., Dwyer,T.M., Dowler,L.L., White,R.A. and Froehner,S.C.
  TITLE     Mouse alpha 1- and beta 2-syntrophin gene structure, chromosome
            localization, and homology with a discs large domain
  JOURNAL   J Biol Chem 270 (43), 25859-25865 (1995)
   PUBMED   7592771
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Mills,K.A., Sunada,Y., Campbell,K.P. and Mathews,K.D.
  TITLE     A syntrophin gene maps to mouse chromosome 8 and is not the
            myodystrophy gene
  JOURNAL   Mamm Genome 6 (9), 664-665 (1995)
   PUBMED   8535078
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Ahn,A.H., Yoshida,M., Anderson,M.S., Feener,C.A., Selig,S.,
            Hagiwara,Y., Ozawa,E. and Kunkel,L.M.
  TITLE     Cloning of human basic A1, a distinct 59-kDa dystrophin-associated
            protein encoded on chromosome 8q23-24
  JOURNAL   Proc Natl Acad Sci U S A 91 (10), 4446-4450 (1994)
   PUBMED   8183929
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Adams,M.E., Butler,M.H., Dwyer,T.M., Peters,M.F., Murnane,A.A. and
            Froehner,S.C.
  TITLE     Two forms of mouse syntrophin, a 58 kd dystrophin-associated
            protein, differ in primary structure and tissue distribution
  JOURNAL   Neuron 11 (3), 531-540 (1993)
   PUBMED   7691103
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC123864.4 and AC123868.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC145442.1, SRR14995044.153254.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN01164133
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 53.38 cM"
     Protein         1..531
                     /product="beta-2-syntrophin isoform 1"
                     /note="beta-2-syntrophin; syntrophin-3; 59 kDa
                     dystrophin-associated protein A1 basic component 2"
                     /calculated_mol_wt=57297
     Region          45..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61235.2)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319; propagated from
                     UniProtKB/Swiss-Prot (Q61235.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19131326,
                     ECO:0007744|PubMed:19144319; propagated from
                     UniProtKB/Swiss-Prot (Q61235.2)"
     Region          94..176
                     /region_name="PDZ_syntrophin-like"
                     /note="PDZ domain of syntrophins, and related domains;
                     cd06801"
                     /db_xref="CDD:467262"
     Site            order(105..111,123,126,156,160,163..164)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467262"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13425; propagated from
                     UniProtKB/Swiss-Prot (Q61235.2)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13425; propagated from
                     UniProtKB/Swiss-Prot (Q61235.2)"
     Region          195..220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61235.2)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61235.2)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61235.2)"
     Region          <224..281
                     /region_name="PHsplit_syntrophin"
                     /note="Syntrophin Split Pleckstrin homology (PH) domain;
                     cd01258"
                     /db_xref="CDD:269960"
     Region          306..417
                     /region_name="PH"
                     /note="PH domain; pfam00169"
                     /db_xref="CDD:459697"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61235.2)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61235.2)"
     CDS             1..531
                     /gene="Sntb2"
                     /gene_synonym="Snt2; SNT3; SNTL"
                     /coded_by="NM_001368316.1:63..1658"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS90456.1"
                     /db_xref="GeneID:20650"
                     /db_xref="MGI:MGI:101771"
ORIGIN      
        1 mavwtratka glvelllrer wvrvvaelsg eslsltgdaa avepeppaaa fnglpngggg
       61 eslpgspnrg lgppsppapp rgpageasas ppvrrvrvvk qeagglgisi kggrenrmpi
      121 liskifpgla adqsralrlg dailsvngtd lrqathdqav qalkragkev llevkfirev
      181 tpyikkpslv sdlpwegasp qspsfsgsed sgspkhqntt kdrkviplkm cfaarnlsmp
      241 dlenrlielh spdsrntlil rckdtatahs wfvaihtnim allpqvlael namlgatsta
      301 ggskevkhia wlaeqakldg grqqwrpvlm avtekdllly dcmpwtrdaw aspchsyplv
      361 atrlvhsgsg crspslgsdl tfatrtgsrq giemhlfrve thrdlstwtr ilvqgchaaa
      421 elikevsldy gpaflskadc iciahvlirq shshgtacvs skseeraltv trsistskde
      481 kkekattkkh kqkplllpps qclpedlqtt agpqqgfrkg rpfphslgqk f
//
LOCUS       NP_057603                447 aa            linear   PRI 27-APR-2025
DEFINITION  ameloblastin precursor [Homo sapiens].
ACCESSION   NP_057603 XP_942897
VERSION     NP_057603.1
DBSOURCE    REFSEQ: accession NM_016519.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Hany,U., Watson,C.M., Liu,L., Nikolopoulos,G., Smith,C.E.L.,
            Poulter,J.A., Brown,C.J., Patel,A., Rodd,H.D., Balmer,R.,
            Harfoush,A., Al-Jawad,M., Inglehearn,C.F. and Mighell,A.J.
  TITLE     Novel Ameloblastin Variants, Contrasting Amelogenesis Imperfecta
            Phenotypes
  JOURNAL   J Dent Res 103 (1), 22-30 (2024)
   PUBMED   38058155
  REMARK    GeneRIF: Novel Ameloblastin Variants, Contrasting Amelogenesis
            Imperfecta Phenotypes.
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Liang,T., Hu,Y., Smith,C.E., Richardson,A.S., Zhang,H., Yang,J.,
            Lin,B., Wang,S.K., Kim,J.W., Chun,Y.H., Simmer,J.P. and Hu,J.C.
  TITLE     AMBN mutations causing hypoplastic amelogenesis imperfecta and Ambn
            knockout-NLS-lacZ knockin mice exhibiting failed amelogenesis and
            Ambn tissue-specificity
  JOURNAL   Mol Genet Genomic Med 7 (9), e929 (2019)
   PUBMED   31402633
  REMARK    GeneRIF: Ameloblastin is critical for the initiation of enamel
            ribbon formation, and its absence results in pathological
            mineralization within the enamel organ epithelia.
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Mardh,C.K., Backman,B., Simmons,D., Golovleva,I., Gu,T.T.,
            Holmgren,G., MacDougall,M. and Forsman-Semb,K.
  TITLE     Human ameloblastin gene: genomic organization and mutation analysis
            in amelogenesis imperfecta patients
  JOURNAL   Eur J Oral Sci 109 (1), 8-13 (2001)
   PUBMED   11330937
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Toyosawa,S., Fujiwara,T., Ooshima,T., Shintani,S., Sato,A.,
            Ogawa,Y., Sobue,S. and Ijuhin,N.
  TITLE     Cloning and characterization of the human ameloblastin gene
  JOURNAL   Gene 256 (1-2), 1-11 (2000)
   PUBMED   11054529
REFERENCE   7  (residues 1 to 447)
  AUTHORS   MacDougall,M., Simmons,D., Gu,T.T., Forsman-Semb,K., Mardh,C.K.,
            Mesbah,M., Forest,N., Krebsbach,P.H., Yamada,Y. and Berdal,A.
  TITLE     Cloning, characterization and immunolocalization of human
            ameloblastin
  JOURNAL   Eur J Oral Sci 108 (4), 303-310 (2000)
   PUBMED   10946765
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Bartlett,J.D. and Simmer,J.P.
  TITLE     Proteinases in developing dental enamel
  JOURNAL   Crit Rev Oral Biol Med 10 (4), 425-441 (1999)
   PUBMED   10634581
  REMARK    Review article
REFERENCE   9  (residues 1 to 447)
  AUTHORS   MacDougall,M., DuPont,B.R., Simmons,D., Reus,B., Krebsbach,P.,
            Karrman,C., Holmgren,G., Leach,R.J. and Forsman,K.
  TITLE     Ameloblastin gene (AMBN) maps within the critical region for
            autosomal dominant amelogenesis imperfecta at chromosome 4q21
  JOURNAL   Genomics 41 (1), 115-118 (1997)
   PUBMED   9126491
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Lee,S.K., Krebsbach,P.H., Matsuki,Y., Nanci,A., Yamada,K.M. and
            Yamada,Y.
  TITLE     Ameloblastin expression in rat incisors and human tooth germs
  JOURNAL   Int J Dev Biol 40 (6), 1141-1150 (1996)
   PUBMED   9032019
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC134919.3, BP248666.1,
            AJ537437.1, BC106931.1 and AF209780.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_942897.1.
            
            Summary: This gene encodes the nonamelogenin enamel matrix protein
            ameloblastin. The encoded protein may be important in enamel matrix
            formation and mineralization. This gene is located in the
            calcium-binding phosphoprotein gene cluster on chromosome 4.
            Mutations in this gene may be associated with dentinogenesis
            imperfect and autosomal dominant amylogenesis imperfect. [provided
            by RefSeq, Aug 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF209780.1, BC106931.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2145743 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322937.10/ ENSP00000313809.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.3"
     Protein         1..447
                     /product="ameloblastin precursor"
                     /note="enamel matrix protein"
                     /calculated_mol_wt=45344
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2957
     Region          11..447
                     /region_name="Amelin"
                     /note="Ameloblastin precursor (Amelin); pfam05111"
                     /db_xref="CDD:461551"
     mat_peptide     27..447
                     /product="Ameloblastin. /id=PRO_0000001192"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP70.1)"
                     /calculated_mol_wt=45344
     Site            37
                     /site_type="hydroxylation"
                     /note="Hydroxyproline. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9NP70.1)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28989; propagated from
                     UniProtKB/Swiss-Prot (Q9NP70.1)"
     Site            112
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9NP70.1)"
     Region          165..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP70.1)"
     Region          202..214
                     /region_name="Repetitive region"
                     /note="2; propagated from UniProtKB/Swiss-Prot (Q9NP70.1)"
     Region          307..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP70.1)"
     Region          353..383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP70.1)"
     CDS             1..447
                     /gene="AMBN"
                     /gene_synonym="AI1F"
                     /coded_by="NM_016519.6:104..1447"
                     /db_xref="CCDS:CCDS3543.1"
                     /db_xref="GeneID:258"
                     /db_xref="HGNC:HGNC:452"
                     /db_xref="MIM:601259"
ORIGIN      
        1 msaskiplfk mkdlililcl lemsfavpff pqqsgtpgma slsletmrql gslqrlntls
       61 qysrygfgks fnslwmhgll pphsslpwmr prehetqqye yslpvhpppl psqpslkpqq
      121 pglkpflqsa aattnqatal kealqppihl ghlplqegel plvqqqvaps dkppkpelpg
      181 vdfadpqgps lpgmdfpdpq gpslpgldfa dpqgstifqi arlishgpmp qnkqsplypg
      241 mlyvpfganq lnaparlgim sseevaggre dpmaygamfp gfggmrpgfe gmphnpamgg
      301 dftlefdspv aatkgpenee ggaqgspmpe anpdnlenpa fltelepaph agllalpkdd
      361 ipglprspsg kmkglpsvtp aaadplmtpe ladvyrtyda dmttsvdfqe eatmdttmap
      421 nslqtsmpgn kaqepemmhd awhfqep
//
LOCUS       NP_006752                255 aa            linear   PRI 27-APR-2025
DEFINITION  14-3-3 protein epsilon [Homo sapiens].
ACCESSION   NP_006752 XP_940602
VERSION     NP_006752.1
DBSOURCE    REFSEQ: accession NM_006761.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Hu,Y., Zhang,C., Wang,S., Xiong,H., Xie,W., Zeng,Z., Cai,H.,
            Wang,Q.K. and Lu,Z.
  TITLE     14-3-3epsilon/YWHAE regulates the transcriptional expression of
            cardiac sodium channel NaV1.5
  JOURNAL   Heart Rhythm 21 (11), 2320-2329 (2024)
   PUBMED   38750908
  REMARK    GeneRIF: 14-3-3epsilon/YWHAE regulates the transcriptional
            expression of cardiac sodium channel NaV1.5.
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Ye,N., Shi,X., Gao,J., Dong,R., Wang,G., Wang,J., Luo,L. and
            Zhang,T.
  TITLE     Exosomes from Intrahepatic Cholestasis of Pregnancy Induce Cell
            Apoptosis Through the miRNA-6891-5p/YWHAE Pathway
  JOURNAL   Dig Dis Sci 69 (4), 1253-1262 (2024)
   PUBMED   38361148
  REMARK    GeneRIF: Exosomes from Intrahepatic Cholestasis of Pregnancy Induce
            Cell Apoptosis Through the miRNA-6891-5p/YWHAE Pathway.
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Li,Z., Liu,J., Wang,P., Zhang,B., He,G. and Yang,L.
  TITLE     The novel miR-873-5p-YWHAE-PI3K/AKT axis is involved in non-small
            cell lung cancer progression and chemoresistance by mediating
            autophagy
  JOURNAL   Funct Integr Genomics 24 (2), 33 (2024)
   PUBMED   38363382
  REMARK    GeneRIF: The novel miR-873-5p-YWHAE-PI3K/AKT axis is involved in
            non-small cell lung cancer progression and chemoresistance by
            mediating autophagy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Zhang,Y., Yan,M., Yu,Y., Wang,J., Jiao,Y., Zheng,M. and Zhang,S.
  TITLE     14-3-3epsilon: a protein with complex physiology function but
            promising therapeutic potential in cancer
  JOURNAL   Cell Commun Signal 22 (1), 72 (2024)
   PUBMED   38279176
  REMARK    GeneRIF: 14-3-3epsilon: a protein with complex physiology function
            but promising therapeutic potential in cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Jin,D.Y., Lyu,M.S., Kozak,C.A. and Jeang,K.T.
  TITLE     Function of 14-3-3 proteins
  JOURNAL   Nature 382 (6589), 308 (1996)
   PUBMED   8684458
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Conklin,D.S., Galaktionov,K. and Beach,D.
  TITLE     14-3-3 proteins associate with cdc25 phosphatases
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7892-7896 (1995)
   PUBMED   7644510
REFERENCE   8  (residues 1 to 255)
  AUTHORS   Jones,D.H., Ley,S. and Aitken,A.
  TITLE     Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo
            and in vitro: implications for function as adapter proteins
  JOURNAL   FEBS Lett 368 (1), 55-58 (1995)
   PUBMED   7615088
REFERENCE   9  (residues 1 to 255)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 255)
  AUTHORS   Detlav,I.E.
  TITLE     [Anti-brain antibodies in serum and cerebrospinal fluid following
            cranio-cerebral trauma]
  JOURNAL   Zh Nevropatol Psikhiatr Im S S Korsakova 76 (3), 344-348 (1976)
   PUBMED   1266503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC365395.1, AY883089.1 and
            AC032044.28.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_940602.1.
            
            Summary: This gene product belongs to the 14-3-3 family of proteins
            which mediate signal transduction by binding to
            phosphoserine-containing proteins. This highly conserved protein
            family is found in both plants and mammals, and this protein is
            100% identical to the mouse ortholog. It interacts with CDC25
            phosphatases, RAF1 and IRS1 proteins, suggesting its role in
            diverse biochemical activities related to signal transduction, such
            as cell division and regulation of insulin sensitivity. It has also
            been implicated in the pathogenesis of small cell lung cancer. Two
            transcript variants, one protein-coding and the other
            non-protein-coding, have been found for this gene. [provided by
            RefSeq, Aug 2008].
            
            Transcript Variant: This variant (1) represents the protein-coding
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.552827.1,
                                           SRR3476690.305381.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264335.13/ ENSP00000264335.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..255
                     /product="14-3-3 protein epsilon"
                     /note="mitochondrial import stimulation factor L subunit;
                     protein kinase C inhibitor protein-1; tyrosine
                     3/tryptophan 5 -monooxygenase activation protein, epsilon
                     polypeptide; 14-3-3 epsilon; tyrosine
                     3-monooxygenase/tryptophan 5-monooxygenase activation
                     protein, epsilon polypeptide; epididymis luminal protein
                     2"
                     /calculated_mol_wt=29043
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.13,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P62258.1)"
     Region          4..233
                     /region_name="14-3-3_epsilon"
                     /note="14-3-3 epsilon, an isoform of 14-3-3 protein;
                     cd10020"
                     /db_xref="CDD:206757"
     Site            order(6,10,13..14,16,26,59,62,66,81..82,84..85,88..89,92)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:206757"
     Site            order(50,57,130..131,172,175..176,179,182..183,219..220,
                     223,227,230..231)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:206757"
     Site            50
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62258.1)"
     Site            57
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein; propagated from UniProtKB/Swiss-Prot (P62258.1)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62260; propagated from
                     UniProtKB/Swiss-Prot (P62258.1)"
     Site            69
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62258.1)"
     Site            118
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62258.1)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62258.1)"
     Site            130
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein; propagated from UniProtKB/Swiss-Prot (P62258.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P62260; propagated from
                     UniProtKB/Swiss-Prot (P62258.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P62260; propagated from
                     UniProtKB/Swiss-Prot (P62258.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P62258.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P62258.1)"
     Region          234..255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62258.1)"
     Site            236..237
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by poliovirus
                     protease 3C. /evidence=ECO:0000269|PubMed:37555661;
                     propagated from UniProtKB/Swiss-Prot (P62258.1)"
     CDS             1..255
                     /gene="YWHAE"
                     /gene_synonym="14-3-3E; HEL2; KCIP-1; MDCR; MDS"
                     /coded_by="NM_006761.5:113..880"
                     /db_xref="CCDS:CCDS11001.1"
                     /db_xref="GeneID:7531"
                     /db_xref="HGNC:HGNC:12851"
                     /db_xref="MIM:605066"
ORIGIN      
        1 mddredlvyq aklaeqaery demvesmkkv agmdveltve ernllsvayk nvigarrasw
       61 riissieqke enkggedklk mireyrqmve telkliccdi ldvldkhlip aantgeskvf
      121 yykmkgdyhr ylaefatgnd rkeaaenslv aykaasdiam telppthpir lglalnfsvf
      181 yyeilnspdr acrlakaafd daiaeldtls eesykdstli mqllrdnltl wtsdmqgdge
      241 eqnkealqdv edenq
//
LOCUS       NP_003647                370 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type 1 [Homo sapiens].
ACCESSION   NP_003647
VERSION     NP_003647.1
DBSOURCE    REFSEQ: accession NM_003656.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Lei,Y., Yu,T., Li,C., Li,J., Liang,Y., Wang,X., Chen,Y. and Wang,X.
  TITLE     Expression of CAMK1 and its association with clinicopathologic
            characteristics in pancreatic cancer
  JOURNAL   J Cell Mol Med 25 (2), 1198-1206 (2021)
   PUBMED   33342045
  REMARK    GeneRIF: Expression of CAMK1 and its association with
            clinicopathologic characteristics in pancreatic cancer.
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Chin,D., Winkler,K.E. and Means,A.R.
  TITLE     Characterization of substrate phosphorylation and use of calmodulin
            mutants to address implications from the enzyme crystal structure
            of calmodulin-dependent protein kinase I
  JOURNAL   J Biol Chem 272 (50), 31235-31240 (1997)
   PUBMED   9395448
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Yokokura,H., Picciotto,M.R., Nairn,A.C. and Hidaka,H.
  TITLE     The regulatory region of calcium/calmodulin-dependent protein
            kinase I contains closely associated autoinhibitory and
            calmodulin-binding domains
  JOURNAL   J Biol Chem 270 (40), 23851-23859 (1995)
   PUBMED   7559563
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Haribabu,B., Hook,S.S., Selbert,M.A., Goldstein,E.G., Tomhave,E.D.,
            Edelman,A.M., Snyderman,R. and Means,A.R.
  TITLE     Human calcium-calmodulin dependent protein kinase I: cDNA cloning,
            domain structure and activation by phosphorylation at threonine-177
            by calcium-calmodulin dependent protein kinase I kinase
  JOURNAL   EMBO J 14 (15), 3679-3686 (1995)
   PUBMED   7641687
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Liu,F., Thompson,M.A., Wagner,S., Greenberg,M.E. and Green,M.R.
  TITLE     Activating transcription factor-1 can mediate Ca(2+)- and
            cAMP-inducible transcriptional activation
  JOURNAL   J Biol Chem 268 (9), 6714-6720 (1993)
   PUBMED   8384217
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Bredt,D.S., Ferris,C.D. and Snyder,S.H.
  TITLE     Nitric oxide synthase regulatory sites. Phosphorylation by cyclic
            AMP-dependent protein kinase, protein kinase C, and
            calcium/calmodulin protein kinase; identification of flavin and
            calmodulin binding sites
  JOURNAL   J Biol Chem 267 (16), 10976-10981 (1992)
   PUBMED   1375933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN990042.1, BC106754.2 and
            AA724193.1.
            
            Summary: Calcium/calmodulin-dependent protein kinase I is expressed
            in many tissues and is a component of a calmodulin-dependent
            protein kinase cascade.  Calcium/calmodulin directly activates
            calcium/calmodulin-dependent protein kinase I by binding to the
            enzyme and indirectly promotes the phosphorylation and synergistic
            activation of the enzyme by calcium/calmodulin-dependent protein
            kinase I kinase. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1124029.1,
                                           SRR3476690.341547.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256460.8/ ENSP00000256460.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..370
                     /product="calcium/calmodulin-dependent protein kinase type
                     1"
                     /EC_number="2.7.11.17"
                     /note="caM-KI; caMKI-alpha; caM kinase I alpha"
                     /calculated_mol_wt=41206
     Region          16..278
                     /region_name="STKc_CaMKI_alpha"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type I alpha;
                     cd14167"
                     /db_xref="CDD:271069"
     Site            order(26..30,32,34,47,49,79,95..98,102,104,140..141,143,
                     145..146,148,161..162,165,179..183,185)
                     /site_type="active"
                     /db_xref="CDD:271069"
     Site            order(26..30,32,34,47,49,79,95..98,102,141,143,145..146,
                     148,161..162)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271069"
     Site            order(30,102,104,140..141,143,145,165,179..183,185)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271069"
     Site            161..183
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271069"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CaMKK1 and CaMKK2.
                     /evidence=ECO:0000269|PubMed:7641687; propagated from
                     UniProtKB/Swiss-Prot (Q14012.1)"
     Region          276..316
                     /region_name="Autoinhibitory domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14012.1)"
     Region          296..317
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14012.1)"
     Region          315..321
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14012.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14012.1)"
     CDS             1..370
                     /gene="CAMK1"
                     /gene_synonym="CAMKI"
                     /coded_by="NM_003656.5:149..1261"
                     /db_xref="CCDS:CCDS2582.1"
                     /db_xref="GeneID:8536"
                     /db_xref="HGNC:HGNC:1459"
                     /db_xref="MIM:604998"
ORIGIN      
        1 mlgavegprw kqaedirdiy dfrdvlgtga fsevilaedk rtqklvaikc iakealegke
       61 gsmeneiavl hkikhpniva lddiyesggh lylimqlvsg gelfdrivek gfyterdasr
      121 lifqvldavk ylhdlgivhr dlkpenllyy sldedskimi sdfglskmed pgsvlstacg
      181 tpgyvapevl aqkpyskavd cwsigviayi llcgyppfyd endaklfeqi lkaeyefdsp
      241 ywddisdsak dfirhlmekd pekrftceqa lqhpwiagdt aldknihqsv seqikknfak
      301 skwkqafnat avvrhmrklq lgtsqegqgq tashgelltp vaggpaagcc crdccvepgt
      361 elsptlphql
//
LOCUS       NP_001984                295 aa            linear   PRI 27-APR-2025
DEFINITION  tissue factor isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001984
VERSION     NP_001984.1
DBSOURCE    REFSEQ: accession NM_001993.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Zhang,Y., Liu,L., Pei,J., Ren,Z., Deng,Y. and Yu,K.
  TITLE     Tissue factor overexpression promotes resistance to KRAS-G12C
            inhibition in non-small cell lung cancer
  JOURNAL   Oncogene 43 (9), 668-681 (2024)
   PUBMED   38191673
  REMARK    GeneRIF: Tissue factor overexpression promotes resistance to
            KRAS-G12C inhibition in non-small cell lung cancer.
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Eichhorn,T., Weiss,R., Huber,S., Ebeyer-Masotta,M., Mostageer,M.,
            Emprechtinger,R., Knabl,L. Sr., Knabl,L., Wurzner,R. and Weber,V.
  TITLE     Expression of Tissue Factor and Platelet/Leukocyte Markers on
            Extracellular Vesicles Reflect Platelet-Leukocyte Interaction in
            Severe COVID-19
  JOURNAL   Int J Mol Sci 24 (23), 16886 (2023)
   PUBMED   38069209
  REMARK    GeneRIF: Expression of Tissue Factor and Platelet/Leukocyte Markers
            on Extracellular Vesicles Reflect Platelet-Leukocyte Interaction in
            Severe COVID-19.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Brambilla,M., Becchetti,A., Rovati,G.E., Cosentino,N., Conti,M.,
            Canzano,P., Giesen,P.L.A., Loffreda,A., Bonomi,A., Cattaneo,M., De
            Candia,E., Podda,G.M., Trabattoni,D., Werba,P.J., Campodonico,J.,
            Pinna,C., Marenzi,G., Tremoli,E. and Camera,M.
  TITLE     Cell Surface Platelet Tissue Factor Expression: Regulation by P2Y12
            and Link to Residual Platelet Reactivity
  JOURNAL   Arterioscler Thromb Vasc Biol 43 (10), 2042-2057 (2023)
   PUBMED   37589138
  REMARK    GeneRIF: Cell Surface Platelet Tissue Factor Expression: Regulation
            by P2Y12 and Link to Residual Platelet Reactivity.
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Zioncheck,T.F., Roy,S. and Vehar,G.A.
  TITLE     The cytoplasmic domain of tissue factor is phosphorylated by a
            protein kinase C-dependent mechanism
  JOURNAL   J Biol Chem 267 (6), 3561-3564 (1992)
   PUBMED   1740409
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Broze,G.J. Jr., Girard,T.J. and Novotny,W.F.
  TITLE     Regulation of coagulation by a multivalent Kunitz-type inhibitor
  JOURNAL   Biochemistry 29 (33), 7539-7546 (1990)
   PUBMED   2271516
  REMARK    Review article
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Mackman,N., Morrissey,J.H., Fowler,B. and Edgington,T.S.
  TITLE     Complete sequence of the human tissue factor gene, a highly
            regulated cellular receptor that initiates the coagulation protease
            cascade
  JOURNAL   Biochemistry 28 (4), 1755-1762 (1989)
   PUBMED   2719931
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Kao,F.T., Hartz,J., Horton,R., Nemerson,Y. and Carson,S.D.
  TITLE     Regional assignment of human tissue factor gene (F3) to chromosome
            1p21-p22
  JOURNAL   Somat Cell Mol Genet 14 (4), 407-410 (1988)
   PUBMED   3399965
REFERENCE   8  (residues 1 to 295)
  AUTHORS   Scarpati,E.M., Wen,D., Broze,G.J. Jr., Miletich,J.P.,
            Flandermeyer,R.R., Siegel,N.R. and Sadler,J.E.
  TITLE     Human tissue factor: cDNA sequence and chromosome localization of
            the gene
  JOURNAL   Biochemistry 26 (17), 5234-5238 (1987)
   PUBMED   2823875
REFERENCE   9  (residues 1 to 295)
  AUTHORS   Spicer,E.K., Horton,R., Bloem,L., Bach,R., Williams,K.R., Guha,A.,
            Kraus,J., Lin,T.C., Nemerson,Y. and Konigsberg,W.H.
  TITLE     Isolation of cDNA clones coding for human tissue factor: primary
            structure of the protein and cDNA
  JOURNAL   Proc Natl Acad Sci U S A 84 (15), 5148-5152 (1987)
   PUBMED   3037536
REFERENCE   10 (residues 1 to 295)
  AUTHORS   Gouault-Helimann,M. and Josso,F.
  TITLE     [Initiation in vivo of blood coagulation. The role of white blood
            cells and tissue factor (author's transl)]
  JOURNAL   Nouv Presse Med 8 (40), 3249-3253 (1979)
   PUBMED   392457
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB499288.1, M27436.1 and
            AC093117.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes coagulation factor III which is a cell
            surface glycoprotein. This factor enables cells to initiate the
            blood coagulation cascades, and it functions as the high-affinity
            receptor for the coagulation factor VII. The resulting complex
            provides a catalytic event that is responsible for initiation of
            the coagulation protease cascades by specific limited proteolysis.
            Unlike the other cofactors of these protease cascades, which
            circulate as nonfunctional precursors, this factor is a potent
            initiator that is fully functional when expressed on cell surfaces,
            for example, on monocytes. There are 3 distinct domains of this
            factor: extracellular, transmembrane, and cytoplasmic. Platelets
            and monocytes have been shown to express this coagulation factor
            under procoagulatory and proinflammatory stimuli, and a major role
            in HIV-associated coagulopathy has been described.
            Platelet-dependent monocyte expression of coagulation factor III
            has been described to be associated with Coronavirus Disease 2019
            (COVID-19) severity and mortality. This protein is the only one in
            the coagulation pathway for which a congenital deficiency has not
            been described. Alternate splicing results in multiple transcript
            variants.[provided by RefSeq, Aug 2020].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.213497.1,
                                           SRR3476690.491922.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153427 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: relevant for disease process
            MANE Ensembl match     :: ENST00000334047.12/ ENSP00000334145.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.3"
     Protein         1..295
                     /product="tissue factor isoform 1 precursor"
                     /note="coagulation factor III (thromboplastin, tissue
                     factor)"
                     /calculated_mol_wt=29594
     sig_peptide     1..32
                     /calculated_mol_wt=3492
     Region          18..118
                     /region_name="Tissue_fac"
                     /note="Tissue factor; pfam01108"
                     /db_xref="CDD:460067"
     mat_peptide     33..295
                     /product="tissue factor isoform 1"
                     /calculated_mol_wt=29594
     Region          46..48
                     /region_name="WKS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P13726.1)"
     Region          77..79
                     /region_name="WKS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P13726.1)"
     Region          138..242
                     /region_name="Interfer-bind"
                     /note="Interferon-alpha/beta receptor, fibronectin type
                     III; pfam09294"
                     /db_xref="CDD:462746"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P13726.1)"
     Site            169
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P13726.1)"
     Region          190..192
                     /region_name="WKS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P13726.1)"
     Site            252..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13726.1)"
     CDS             1..295
                     /gene="F3"
                     /gene_synonym="CD142; TF; TFA"
                     /coded_by="NM_001993.5:124..1011"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS750.1"
                     /db_xref="GeneID:2152"
                     /db_xref="HGNC:HGNC:3541"
                     /db_xref="MIM:134390"
ORIGIN      
        1 metpawprvp rpetavartl llgwvfaqva gasgttntva aynltwkstn fktilewepk
       61 pvnqvytvqi stksgdwksk cfyttdtecd ltdeivkdvk qtylarvfsy pagnvestgs
      121 ageplyensp eftpyletnl gqptiqsfeq vgtkvnvtve dertlvrrnn tflslrdvfg
      181 kdliytlyyw kssssgkkta ktntneflid vdkgenycfs vqavipsrtv nrkstdspve
      241 cmgqekgefr eifyiigavv fvviilviil aislhkcrka gvgqswkens plnvs
//
LOCUS       NP_001305432             384 aa            linear   PRI 27-APR-2025
DEFINITION  dual specificity protein phosphatase 9 [Homo sapiens].
ACCESSION   NP_001305432 XP_005274712
VERSION     NP_001305432.1
DBSOURCE    REFSEQ: accession NM_001318503.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Binjawhar,D.N., Ansari,M.G.A., Sabico,S., Hussain,S.D.,
            Alenad,A.M., Alokail,M.S., Al-Masri,A.A. and Al-Daghri,N.M.
  TITLE     Genetic Variants of HNF4A, WFS1, DUSP9, FTO, and ZFAND6 Genes Are
            Associated with Prediabetes Susceptibility and Inflammatory Markers
            in the Saudi Arabian Population
  JOURNAL   Genes (Basel) 14 (3), 536 (2023)
   PUBMED   36980809
  REMARK    GeneRIF: Genetic Variants of HNF4A, WFS1, DUSP9, FTO, and ZFAND6
            Genes Are Associated with Prediabetes Susceptibility and
            Inflammatory Markers in the Saudi Arabian Population.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Khoubai,F.Z. and Grosset,C.F.
  TITLE     DUSP9, a Dual-Specificity Phosphatase with a Key Role in Cell
            Biology and Human Diseases
  JOURNAL   Int J Mol Sci 22 (21), 11538 (2021)
   PUBMED   34768967
  REMARK    GeneRIF: DUSP9, a Dual-Specificity Phosphatase with a Key Role in
            Cell Biology and Human Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Jeong,D.G., Yoon,T.S., Jung,S.K., Park,B.C., Park,H., Ryu,S.E. and
            Kim,S.J.
  TITLE     Exploring binding sites other than the catalytic core in the
            crystal structure of the catalytic domain of MKP-4
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 1), 25-31 (2011)
   PUBMED   21206059
  REMARK    GeneRIF: 2.7 A resolution crystal structure of the catalytic domain
            of MKP-4 (MKP-4C) is presented
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Voight,B.F., Scott,L.J., Steinthorsdottir,V., Morris,A.P., Dina,C.,
            Welch,R.P., Zeggini,E., Huth,C., Aulchenko,Y.S., Thorleifsson,G.,
            McCulloch,L.J., Ferreira,T., Grallert,H., Amin,N., Wu,G.,
            Willer,C.J., Raychaudhuri,S., McCarroll,S.A., Langenberg,C.,
            Hofmann,O.M., Dupuis,J., Qi,L., Segre,A.V., van Hoek,M.,
            Navarro,P., Ardlie,K., Balkau,B., Benediktsson,R., Bennett,A.J.,
            Blagieva,R., Boerwinkle,E., Bonnycastle,L.L., Bengtsson Bostrom,K.,
            Bravenboer,B., Bumpstead,S., Burtt,N.P., Charpentier,G.,
            Chines,P.S., Cornelis,M., Couper,D.J., Crawford,G., Doney,A.S.,
            Elliott,K.S., Elliott,A.L., Erdos,M.R., Fox,C.S., Franklin,C.S.,
            Ganser,M., Gieger,C., Grarup,N., Green,T., Griffin,S., Groves,C.J.,
            Guiducci,C., Hadjadj,S., Hassanali,N., Herder,C., Isomaa,B.,
            Jackson,A.U., Johnson,P.R., Jorgensen,T., Kao,W.H., Klopp,N.,
            Kong,A., Kraft,P., Kuusisto,J., Lauritzen,T., Li,M., Lieverse,A.,
            Lindgren,C.M., Lyssenko,V., Marre,M., Meitinger,T., Midthjell,K.,
            Morken,M.A., Narisu,N., Nilsson,P., Owen,K.R., Payne,F.,
            Perry,J.R., Petersen,A.K., Platou,C., Proenca,C., Prokopenko,I.,
            Rathmann,W., Rayner,N.W., Robertson,N.R., Rocheleau,G., Roden,M.,
            Sampson,M.J., Saxena,R., Shields,B.M., Shrader,P., Sigurdsson,G.,
            Sparso,T., Strassburger,K., Stringham,H.M., Sun,Q., Swift,A.J.,
            Thorand,B., Tichet,J., Tuomi,T., van Dam,R.M., van Haeften,T.W.,
            van Herpt,T., van Vliet-Ostaptchouk,J.V., Walters,G.B.,
            Weedon,M.N., Wijmenga,C., Witteman,J., Bergman,R.N., Cauchi,S.,
            Collins,F.S., Gloyn,A.L., Gyllensten,U., Hansen,T., Hide,W.A.,
            Hitman,G.A., Hofman,A., Hunter,D.J., Hveem,K., Laakso,M.,
            Mohlke,K.L., Morris,A.D., Palmer,C.N., Pramstaller,P.P., Rudan,I.,
            Sijbrands,E., Stein,L.D., Tuomilehto,J., Uitterlinden,A.,
            Walker,M., Wareham,N.J., Watanabe,R.M., Abecasis,G.R., Boehm,B.O.,
            Campbell,H., Daly,M.J., Hattersley,A.T., Hu,F.B., Meigs,J.B.,
            Pankow,J.S., Pedersen,O., Wichmann,H.E., Barroso,I., Florez,J.C.,
            Frayling,T.M., Groop,L., Sladek,R., Thorsteinsdottir,U.,
            Wilson,J.F., Illig,T., Froguel,P., van Duijn,C.M., Stefansson,K.,
            Altshuler,D., Boehnke,M. and McCarthy,M.I.
  CONSRTM   MAGIC investigators; GIANT Consortium
  TITLE     Twelve type 2 diabetes susceptibility loci identified through
            large-scale association analysis
  JOURNAL   Nat Genet 42 (7), 579-589 (2010)
   PUBMED   20581827
  REMARK    Erratum:[Nat Genet. 2011 Apr;43(4):388]
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Liu,Y., Lagowski,J., Sundholm,A., Sundberg,A. and Kulesz-Martin,M.
  TITLE     Microtubule disruption and tumor suppression by mitogen-activated
            protein kinase phosphatase 4
  JOURNAL   Cancer Res 67 (22), 10711-10719 (2007)
   PUBMED   18006813
  REMARK    GeneRIF: microtubule disruption by MKP4 provides a novel mechanism
            for tumor suppression by a cytosolic MKP
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Dickinson,R.J., Williams,D.J., Slack,D.N., Williamson,J.,
            Seternes,O.M. and Keyse,S.M.
  TITLE     Characterization of a murine gene encoding a developmentally
            regulated cytoplasmic dual-specificity mitogen-activated protein
            kinase phosphatase
  JOURNAL   Biochem J 364 (Pt 1), 145-155 (2002)
   PUBMED   11988087
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Muda,M., Boschert,U., Smith,A., Antonsson,B., Gillieron,C.,
            Chabert,C., Camps,M., Martinou,I., Ashworth,A. and Arkinstall,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mitogen-activated protein kinase phosphatase, MKP-4
  JOURNAL   J Biol Chem 272 (8), 5141-5151 (1997)
   PUBMED   9030581
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC060837.1, U52111.3 and
            AI253132.1.
            
            On Jan 8, 2016 this sequence version replaced XP_005274712.1.
            
            Summary: The protein encoded by this gene is a member of the dual
            specificity protein phosphatase subfamily. These phosphatases
            inactivate their target kinases by dephosphorylating both the
            phosphoserine/threonine and phosphotyrosine residues. They
            negatively regulate members of the mitogen-activated protein (MAP)
            kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated
            with cellular proliferation and differentiation. Different members
            of the family of dual specificity phosphatases show distinct
            substrate specificities for various MAP kinases, different tissue
            distribution and subcellular localization, and different modes of
            inducibility of their expression by extracellular stimuli. This
            gene product shows selectivity for members of the ERK family of MAP
            kinases and is localized to the cytoplasm and nucleus. Aberrant
            expression of this gene is associated with type 2 diabetes and
            cancer progression in several cell types. Alternate splicing
            results in multiple transcript variants. [provided by RefSeq, Jan
            2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060837.1, ERR3218378.212083.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342782.4/ ENSP00000345853.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..384
                     /product="dual specificity protein phosphatase 9"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="serine/threonine specific protein phosphatase; map
                     kinase phosphatase 4; mitogen-activated protein kinase
                     phosphatase 4"
                     /calculated_mol_wt=41737
     Region          7..138
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99956.1)"
     Site            82
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238089"
     Region          202..346
                     /region_name="DSP_DUSP9"
                     /note="dual specificity phosphatase domain of dual
                     specificity protein phosphatase 9; cd14644"
                     /db_xref="CDD:350492"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99956.1)"
     Region          348..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99956.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q99956.1)"
     CDS             1..384
                     /gene="DUSP9"
                     /gene_synonym="MKP-4; MKP4"
                     /coded_by="NM_001318503.2:259..1413"
                     /db_xref="CCDS:CCDS14724.1"
                     /db_xref="GeneID:1852"
                     /db_xref="HGNC:HGNC:3076"
                     /db_xref="MIM:300134"
ORIGIN      
        1 meglgrsclw lrrelspprp rlllldcrsr elyesarigg alsvalpall lrrlrrgsls
       61 vrallpgppl qppppapvll ydqgggrrrr geaeaeaeew eaesvlgtll qklreegyla
      121 yylqggfsrf qaecphlcet slagragssm apvpgpvpvv glgslclgsd csdaeseadr
      181 dsmscgldse gatpppvglr asfpvqilpn lylgsardsa nleslaklgi ryilnvtpnl
      241 pnffekngdf hykqipisdh wsqnlsrffp eaiefideal sqncgvlvhc lagvsrsvtv
      301 tvaylmqklh lslndaydlv krkksnispn fnfmgqlldf erslrleerh sqeqgsggqa
      361 saasnppsff ttptsdgafe lapt
//
LOCUS       NP_076229                361 aa            linear   ROD 27-APR-2025
DEFINITION  palmitoyltransferase ZDHHC16 isoform 2 [Mus musculus].
ACCESSION   NP_076229
VERSION     NP_076229.2
DBSOURCE    REFSEQ: accession NM_023740.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Cao,N., Li,J.K., Rao,Y.Q., Liu,H., Wu,J., Li,B., Zhao,P., Zeng,L.
            and Li,J.
  TITLE     A potential role for protein palmitoylation and zDHHC16 in DNA
            damage response
  JOURNAL   BMC Mol Biol 17 (1), 12 (2016)
   PUBMED   27159997
  REMARK    GeneRIF: Knockout of zDHHC16, a palmitoyltransferase gene is
            identified as an interacting protein for c-Abl, a non-receptor
            tyrosine kinase involved in DNA damage response, reproduced most of
            the defects in DNA damage responses produced by the inhibition of
            protein palmitoylation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Fukata,Y., Murakami,T., Yokoi,N. and Fukata,M.
  TITLE     Local Palmitoylation Cycles and Specialized Membrane Domain
            Organization
  JOURNAL   Curr Top Membr 77, 97-141 (2016)
   PUBMED   26781831
  REMARK    Review article
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Zhou,T., Li,J., Zhao,P., Liu,H., Jia,D., Jia,H., He,L., Cang,Y.,
            Boast,S., Chen,Y.H., Thibault,H., Scherrer-Crosbie,M., Goff,S.P.
            and Li,B.
  TITLE     Palmitoyl acyltransferase Aph2 in cardiac function and the
            development of cardiomyopathy
  JOURNAL   Proc Natl Acad Sci U S A 112 (51), 15666-15671 (2015)
   PUBMED   26644582
  REMARK    GeneRIF: Aph2 as a critical in vivo regulator of cardiac function
            and reveal roles for protein palmitoylation in the development of
            other organs including eyes.
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Blaskovic,S., Adibekian,A., Blanc,M. and van der Goot,G.F.
  TITLE     Mechanistic effects of protein palmitoylation and the cellular
            consequences thereof
  JOURNAL   Chem Phys Lipids 180, 44-52 (2014)
   PUBMED   24534427
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Chamberlain,L.H., Lemonidis,K., Sanchez-Perez,M., Werno,M.W.,
            Gorleku,O.A. and Greaves,J.
  TITLE     Palmitoylation and the trafficking of peripheral membrane proteins
  JOURNAL   Biochem Soc Trans 41 (1), 62-66 (2013)
   PUBMED   23356259
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Conibear,E. and Davis,N.G.
  TITLE     Palmitoylation and depalmitoylation dynamics at a glance
  JOURNAL   J Cell Sci 123 (Pt 23), 4007-4010 (2010)
   PUBMED   21084560
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Guo,G., Huss,M., Tong,G.Q., Wang,C., Li Sun,L., Clarke,N.D. and
            Robson,P.
  TITLE     Resolution of cell fate decisions revealed by single-cell gene
            expression analysis from zygote to blastocyst
  JOURNAL   Dev Cell 18 (4), 675-685 (2010)
   PUBMED   20412781
REFERENCE   9  (residues 1 to 361)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Li,B., Cong,F., Tan,C.P., Wang,S.X. and Goff,S.P.
  TITLE     Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has
            pro-apoptotic activity
  JOURNAL   J Biol Chem 277 (32), 28870-28876 (2002)
   PUBMED   12021275
  REMARK    GeneRIF: Aph2 may be involved in ER stress-induced apoptosis in
            which c-Abl plays an important role
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DV658063.1, CK619221.1, AK151505.1 and BY634308.1.
            
            On Jun 21, 2008 this sequence version replaced NP_076229.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK151505.1, AK168042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 35.48 cM"
     Protein         1..361
                     /product="palmitoyltransferase ZDHHC16 isoform 2"
                     /EC_number="2.3.1.225"
                     /note="probable palmitoyltransferase ZDHHC16; ablphilin-2;
                     zinc finger DHHC domain-containing protein 16; Abl-philin
                     2"
                     /calculated_mol_wt=41663
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESG8.2)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESG8.2)"
     Region          156..289
                     /region_name="DHHC"
                     /note="DHHC palmitoyltransferase; pfam01529"
                     /db_xref="CDD:396215"
     Site            199..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESG8.2)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESG8.2)"
     CDS             1..361
                     /gene="Zdhhc16"
                     /gene_synonym="1500015N03Rik; Aph2"
                     /coded_by="NM_023740.3:373..1458"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS29817.1"
                     /db_xref="GeneID:74168"
                     /db_xref="MGI:MGI:1921418"
ORIGIN      
        1 mrgqrslllg parlclrlll llgyrrrcpp llrglvqrwr ygkvclrsll ynsfggsdta
       61 vdaafepvyw lvdnvirwfg vvfvvlvivl tgsivaiayl cvlplilrty svprlcwhff
      121 yshwnliliv fhyyqaittp pgyppqgrnd iatvsickkc iypkparthh csicnrcvlk
      181 mdhhcpwlnn cvghynhryf fsfcffmtlg cvycsygswd lfreayaaie tyhqtppptf
      241 sfrerithks lvylwflcss valalgaltm whavlisrge tsierhinkk errrlqakgr
      301 vfrnpynygc ldnwkvflgv dtgrhwltrv llpsshlphg ngmswdpppw vtahsasvma
      361 v
//
LOCUS       NP_002530                461 aa            linear   PRI 27-APR-2025
DEFINITION  ornithine decarboxylase isoform 1 [Homo sapiens].
ACCESSION   NP_002530
VERSION     NP_002530.1
DBSOURCE    REFSEQ: accession NM_002539.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Jin,R., Li,H., Nan,S. and Wang,H.
  TITLE     FOXA1 co-activates circODC1 and ODC1 in HPV-positive cervical
            cancer cell growth
  JOURNAL   Syst Biol Reprod Med 70 (1), 113-123 (2024)
   PUBMED   38743820
  REMARK    GeneRIF: FOXA1 co-activates circODC1 and ODC1 in HPV-positive
            cervical cancer cell growth.
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Li,Y.P., Huang,Z.J., He,Q.K., Li,Y.X., Zhao,X.P., Ma,Z.Q.,
            Qin,M.J., Chen,A.W., Wei,Q., Wang,Y. and Lu,C.H.
  TITLE     Pirin Promotes the Progression of Non-Small-Cell Lung Cancer by
            Increasing ODC1 to Suppress Autophagy
  JOURNAL   J Proteome Res 23 (5), 1713-1724 (2024)
   PUBMED   38648079
  REMARK    GeneRIF: Pirin Promotes the Progression of Non-Small-Cell Lung
            Cancer by Increasing ODC1 to Suppress Autophagy.
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Cressman,A., Morales,D., Zhang,Z., Le,B., Foley,J.,
            Murray-Stewart,T., Genetos,D.C. and Fierro,F.A.
  TITLE     Effects of Spermine Synthase Deficiency in Mesenchymal Stromal
            Cells Are Rescued by Upstream Inhibition of Ornithine Decarboxylase
  JOURNAL   Int J Mol Sci 25 (5), 2463 (2024)
   PUBMED   38473716
  REMARK    GeneRIF: Effects of Spermine Synthase Deficiency in Mesenchymal
            Stromal Cells Are Rescued by Upstream Inhibition of Ornithine
            Decarboxylase.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Keller,T., Koepsell,H. and Groll,J.
  TITLE     Evaluation of the Influence of Biosurface Design on the Interaction
            between the Regulatory Peptide RS1-reg and ODC1 Reveals a
            Membrane-Dependent Affinity Increase
  JOURNAL   Adv Biol (Weinh) 6 (10), e2101108 (2022)
   PUBMED   35735188
  REMARK    GeneRIF: Evaluation of the Influence of Biosurface Design on the
            Interaction between the Regulatory Peptide RS1-reg and ODC1 Reveals
            a Membrane-Dependent Affinity Increase.
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Zhou,X.E., Suino-Powell,K., Schultz,C.R., Aleiwi,B.,
            Brunzelle,J.S., Lamp,J., Vega,I.E., Ellsworth,E., Bachmann,A.S. and
            Melcher,K.
  TITLE     Structural basis of binding and inhibition of ornithine
            decarboxylase by 1-amino-oxy-3-aminopropane
  JOURNAL   Biochem J 478 (23), 4137-4149 (2021)
   PUBMED   34796899
  REMARK    GeneRIF: Structural basis of binding and inhibition of ornithine
            decarboxylase by 1-amino-oxy-3-aminopropane.
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Bupp,C., Michael,J., VanSickle,E., Rajasekaran,S. and Bachmann,A.S.
  TITLE     Bachmann-Bupp Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36007106
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Yoshida,M., Hayashi,H., Taira,M. and Isono,K.
  TITLE     Elevated expression of the ornithine decarboxylase gene in human
            esophageal cancer
  JOURNAL   Cancer Res 52 (23), 6671-6675 (1992)
   PUBMED   1423312
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Moshier,J.A., Osborne,D.L., Skunca,M., Dosescu,J., Gilbert,J.D.,
            Fitzgerald,M.C., Polidori,G., Wagner,R.L., Friezner Degen,S.J.,
            Luk,G.D. et al.
  TITLE     Multiple promoter elements govern expression of the human ornithine
            decarboxylase gene in colon carcinoma cells
  JOURNAL   Nucleic Acids Res 20 (10), 2581-2590 (1992)
   PUBMED   1598217
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Hickok,N.J., Wahlfors,J., Crozat,A., Halmekyto,M., Alhonen,L.,
            Janne,J. and Janne,O.A.
  TITLE     Human ornithine decarboxylase-encoding loci: nucleotide sequence of
            the expressed gene and characterization of a pseudogene
  JOURNAL   Gene 93 (2), 257-263 (1990)
   PUBMED   2227439
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Hsieh,J.T., Denning,M.F., Heidel,S.M. and Verma,A.K.
  TITLE     Expression of human chromosome 2 ornithine decarboxylase gene in
            ornithine decarboxylase-deficient Chinese hamster ovary cells
  JOURNAL   Cancer Res 50 (8), 2239-2244 (1990)
   PUBMED   2317811
  REMARK    Erratum:[Cancer Res 1990 Jul 1;50(13):4174]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007249.5, BC014562.2,
            BC025296.1 and AI277727.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the rate-limiting enzyme of the
            polyamine biosynthesis pathway which catalyzes ornithine to
            putrescine. The activity level for the enzyme varies in response to
            growth-promoting stimuli and exhibits a high turnover rate in
            comparison to other mammalian proteins. Originally localized to
            both chromosomes 2 and 7, the gene encoding this enzyme has been
            determined to be located on 2p25, with a pseudogene located on
            7q31-qter. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been identified. [provided by
            RefSeq, Dec 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Variants 1, 3, and 4
            encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.551440.1,
                                           SRR1163657.208736.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000234111.9/ ENSP00000234111.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..461
                     /product="ornithine decarboxylase isoform 1"
                     /EC_number="4.1.1.17"
                     /calculated_mol_wt=51017
     Region          37..408
                     /region_name="PLPDE_III_ODC"
                     /note="Type III Pyridoxal 5-phosphate (PLP)-Dependent
                     Enzyme Ornithine Decarboxylase; cd00622"
                     /db_xref="CDD:143482"
     Site            order(38,69,90..91,93..94,116,121,134,137,141,168..170,
                     291,293..294,315,317,319,322..323,331,333,357,359,361,364,
                     393,395,397..399,401)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143482"
     Site            order(67,69,88,154,197,200,236..237,274..277,332,360,389)
                     /site_type="active"
                     /db_xref="CDD:143482"
     Site            order(67,69,88,154,197,200,236..237,274..277,360,389)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143482"
     Site            order(69,360)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143482"
     Site            197
                     /site_type="other"
                     /note="Stacks against the aromatic ring of pyridoxal
                     phosphate and stabilizes reaction intermediates.
                     /evidence=ECO:0000250|UniProtKB:P00860; propagated from
                     UniProtKB/Swiss-Prot (P11926.2)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P00860; propagated from
                     UniProtKB/Swiss-Prot (P11926.2)"
     Site            order(331..332,360..361,389,397)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143482"
     CDS             1..461
                     /gene="ODC1"
                     /gene_synonym="BABS; NEDBA; NEDBIA; ODC"
                     /coded_by="NM_002539.3:335..1720"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1672.1"
                     /db_xref="GeneID:4953"
                     /db_xref="HGNC:HGNC:8109"
                     /db_xref="MIM:165640"
ORIGIN      
        1 mnnfgneefd chfldegfta kdildqkine vsssddkdaf yvadlgdilk khlrwlkalp
       61 rvtpfyavkc ndskaivktl aatgtgfdca skteiqlvqs lgvpperiiy anpckqvsqi
      121 kyaanngvqm mtfdsevelm kvarahpkak lvlriatdds kavcrlsvkf gatlrtsrll
      181 lerakelnid vvgvsfhvgs gctdpetfvq aisdarcvfd mgaevgfsmy lldigggfpg
      241 sedvklkfee itgvinpald kyfpsdsgvr iiaepgryyv asaftlavni iakkivlkeq
      301 tgsddedess eqtfmyyvnd gvygsfncil ydhahvkpll qkrpkpdeky ysssiwgptc
      361 dgldriverc dlpemhvgdw mlfenmgayt vaaastfngf qrptiyyvms gpawqlmqqf
      421 qnpdfppeve eqdastlpvs cawesgmkrh raacasasin v
//
LOCUS       NP_008886                778 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 33B isoform 2 [Homo sapiens].
ACCESSION   NP_008886
VERSION     NP_008886.1
DBSOURCE    REFSEQ: accession NM_006955.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Lee,S., Prokopenko,D., Kelly,R.S., Lutz,S., Ann Lasky-Su,J.,
            Cho,M.H., Laurie,C., Celedon,J.C., Lange,C., Weiss,S.T., Hecker,J.
            and DeMeo,D.L.
  TITLE     Zinc finger protein 33B demonstrates sex interaction with
            atopy-related markers in childhood asthma
  JOURNAL   Eur Respir J 61 (1), 2200479 (2023)
   PUBMED   35953101
  REMARK    GeneRIF: Zinc finger protein 33B demonstrates sex interaction with
            atopy-related markers in childhood asthma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 778)
  AUTHORS   de los Santos,M.J., Garcia-Laez,V., Beltran-Torregrosa,D.,
            Horcajadas,J.A., Martinez-Conejero,J.A., Esteban,F.J., Pellicer,A.
            and Labarta,E.
  TITLE     Hormonal and molecular characterization of follicular fluid,
            cumulus cells and oocytes from pre-ovulatory follicles in
            stimulated and unstimulated cycles
  JOURNAL   Hum Reprod 27 (6), 1596-1605 (2012)
   PUBMED   22451503
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Tunnacliffe,A., Liu,L., Moore,J.K., Leversha,M.A., Jackson,M.S.,
            Papi,L., Ferguson-Smith,M.A., Thiesen,H.J. and Ponder,B.A.
  TITLE     Duplicated KOX zinc finger gene clusters flank the centromere of
            human chromosome 10: evidence for a pericentric inversion during
            primate evolution
  JOURNAL   Nucleic Acids Res 21 (6), 1409-1417 (1993)
   PUBMED   8464732
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Rousseau-Merck,M.F., Tunnacliffe,A., Berger,R., Ponder,B.A. and
            Thiesen,H.J.
  TITLE     A cluster of expressed zinc finger protein genes in the
            pericentromeric region of human chromosome 10
  JOURNAL   Genomics 13 (3), 845-848 (1992)
   PUBMED   1639412
REFERENCE   5  (residues 1 to 778)
  AUTHORS   Huebner,K., Druck,T., Croce,C.M. and Thiesen,H.J.
  TITLE     Twenty-seven nonoverlapping zinc finger cDNAs from human T cells
            map to nine different chromosomes with apparent clustering
  JOURNAL   Am J Hum Genet 48 (4), 726-740 (1991)
   PUBMED   2014798
REFERENCE   6  (residues 1 to 778)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK310073.1 and AJ491697.1.
            
            Summary: This gene encodes a member of the zinc finger family of
            proteins. This gene shows decreased expression in cumulus cells
            derived from patients undergoing controlled ovarian stimulation.
            This gene is present in a gene cluster with several related zinc
            finger genes in the pericentromeric region of chromosome 10.
            Pseudogenes have been identified on chromosomes 7 and 10.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Feb 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            contains an alternate exon in the 5' coding region and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (2) has a distinct N-terminus and is shorter
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA540683.1, AJ491697.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359467.8/ ENSP00000352444.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.21"
     Protein         1..778
                     /product="zinc finger protein 33B isoform 2"
                     /note="zinc finger protein 33b (KOX 31); zinc finger
                     protein 11b (KOX 2)"
                     /calculated_mol_wt=90552
     Region          12..71
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          303..323
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          331..351
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          343..367
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          359..379
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(364,366,368,370..371,374..375,378,392,394,398..399,
                     402..403,406,420,422,424,426..427,430..431,434)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          383..772
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          387..407
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          415..435
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          443..463
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          471..491
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          499..519
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          527..547
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          555..575
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          583..603
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(588,590,592,594..595,598..599,602,616,618,622..623,
                     626..627,630,644,646,648,650..651,654..655,658)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          611..631
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          639..659
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          667..687
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          695..715
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          723..743
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          751..771
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..778
                     /gene="ZNF33B"
                     /gene_synonym="KOX2; KOX31; ZNF11B"
                     /coded_by="NM_006955.3:142..2478"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7198.1"
                     /db_xref="GeneID:7582"
                     /db_xref="HGNC:HGNC:13097"
                     /db_xref="MIM:194522"
ORIGIN      
        1 mnkvdqkfqg svsfkdvtvg ftqeewqhld psqralyrdv mlenysnlvs vgycahkpev
       61 ifrleqgeep wrleeefpsq sfpevwtadh lkersqenqs khlwevvfin nemltkeqgn
      121 vigipfnmdv ssfpsrkmfc qydsrgmsfn tvselviski nylgkksdef nacgklllni
      181 khdethtrek nevlknrntl shrentlqhe kiqtldhnfe ysicqetlle kavfntrkre
      241 naeenncdyn efgrtfcdss sllfhqipps kdshyefsdc ekflcvkstl skhdgvpvkh
      301 ydcgesgnnf rrklclsqlq kgdkgekhfe cnecgkafwe kshltrhqrv htgekhfqcn
      361 qcgktfweks nltkhqrsht gekpfecnec gkafshksal tlhqrthtge kpyqcnacgk
      421 tfyqksdltk hqrthtgqkp yecyecgksf cmnshltvhq rthtgekpfe clecgksfcq
      481 kshltqhqrt higdkpyecn acgktfyhks vltrhqiiht glkpyecyec gktfclksdl
      541 tihqrthtge kpfacpecgk ffshkstlsq hyrthtgekp yechecgkif ynksyltkhn
      601 rthtgekpye cnecgktfcq ksqltqhqri higekpyecn ecgkafchks alivhqrtht
      661 qekpykcnec gksfcvksgl ilherkhtge kpyecnecgk sfshkssltv hhrahtgeks
      721 cqcnecgkif yrksdlakhq rshtgekpye cntcrktfsq ksnlivhqrt higekpye
//
LOCUS       NP_001347364             226 aa            linear   ROD 27-APR-2025
DEFINITION  serine/arginine-rich splicing factor 7 isoform 6 [Mus musculus].
ACCESSION   NP_001347364 XP_006524253
VERSION     NP_001347364.1
DBSOURCE    REFSEQ: accession NM_001360435.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schwich,O.D., Blumel,N., Keller,M., Wegener,M., Setty,S.T.,
            Brunstein,M.E., Poser,I., Mozos,I.R.L., Suess,B., Munch,C.,
            McNicoll,F., Zarnack,K. and Muller-McNicoll,M.
  TITLE     SRSF3 and SRSF7 modulate 3'UTR length through suppression or
            activation of proximal polyadenylation sites and regulation of CFIm
            levels
  JOURNAL   Genome Biol 22 (1), 82 (2021)
   PUBMED   33706811
  REMARK    GeneRIF: SRSF3 and SRSF7 modulate 3'UTR length through suppression
            or activation of proximal polyadenylation sites and regulation of
            CFIm levels.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Meinke,S., Goldammer,G., Weber,A.I., Tarabykin,V., Neumann,A.,
            Preussner,M. and Heyd,F.
  TITLE     Srsf10 and the minor spliceosome control tissue-specific and
            dynamic SR protein expression
  JOURNAL   Elife 9, e56075 (2020)
   PUBMED   32338600
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Kadota,Y., Jam,F.A., Yukiue,H., Terakado,I., Morimune,T., Tano,A.,
            Tanaka,Y., Akahane,S., Fukumura,M., Tooyama,I. and Mori,M.
  TITLE     Srsf7 Establishes the Juvenile Transcriptome through Age-Dependent
            Alternative Splicing in Mice
  JOURNAL   iScience 23 (3), 100929 (2020)
   PUBMED   32146325
  REMARK    Erratum:[iScience. 2020 Jun 26;23(6):101242. doi:
            10.1016/j.isci.2020.101242. PMID: 32559732]
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Park,E., Han,J., Son,G.H., Lee,M.S., Chung,S., Park,S.H., Park,K.,
            Lee,K.H., Choi,S., Seong,J.Y. and Kim,K.
  TITLE     Cooperative actions of Tra2alpha with 9G8 and SRp30c in the RNA
            splicing of the gonadotropin-releasing hormone gene transcript
  JOURNAL   J Biol Chem 281 (1), 401-409 (2006)
   PUBMED   16249178
  REMARK    GeneRIF: 9G8 binds to an element in exon 3 and strongly enhances
            the excision of GnRH intron A in the presence of minimal amount of
            other nuclear components
REFERENCE   8  (residues 1 to 226)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Zhang,H., Wada,J., Kanwar,Y.S., Tsuchiyama,Y., Hiragushi,K.,
            Hida,K., Shikata,K. and Makino,H.
  TITLE     Screening for genes up-regulated in 5/6 nephrectomized mouse kidney
  JOURNAL   Kidney Int 56 (2), 549-558 (1999)
   PUBMED   10432394
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Funke,B., Zuleger,B., Benavente,R., Schuster,T., Goller,M.,
            Stevenin,J. and Horak,I.
  TITLE     The mouse poly(C)-binding protein exists in multiple isoforms and
            interacts with several RNA-binding proteins
  JOURNAL   Nucleic Acids Res 24 (19), 3821-3828 (1996)
   PUBMED   8871564
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC132910.8 and AC140361.2.
            
            On Feb 3, 2018 this sequence version replaced XP_006524253.1.
            
            Summary: The protein encoded by this gene is a member of the
            serine/arginine (SR)-rich family of pre-mRNA splicing factors,
            which constitute part of the spliceosome. Each of these factors
            contains an RNA recognition motif (RRM) for binding RNA and an RS
            domain for binding other proteins. The RS domain is rich in serine
            and arginine residues and facilitates interaction between different
            SR splicing factors. In addition to being critical for mRNA
            splicing, the SR proteins have also been shown to be involved in
            mRNA export from the nucleus and in translation. Multiple
            protein-coding and non-protein-coding transcript variants have been
            found for this gene. [provided by RefSeq, Apr 2022].
            
            Transcript Variant: This variant (6) lacks an exon in the coding
            region, compared to variant 1. The encoded isoform (6) is shorter,
            compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.451207.1,
                                           SRR7345562.2898425.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164137, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 50.63 cM"
     Protein         1..226
                     /product="serine/arginine-rich splicing factor 7 isoform
                     6"
                     /note="serine/arginine-rich splicing factor 7; splicing
                     factor, arginine/serine-rich 7"
                     /calculated_mol_wt=25892
     Region          12..88
                     /region_name="RRM_SRSF7"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     serine/arginine-rich splicing factor 7 (SRSF7); cd12646"
                     /db_xref="CDD:410050"
     Site            order(41,43..45,49,51,82,84)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410050"
     CDS             1..226
                     /gene="Srsf7"
                     /gene_synonym="35kDa; 9430065L19Rik; 9G8; NX-96; Sfrs7"
                     /coded_by="NM_001360435.1:104..784"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:225027"
                     /db_xref="MGI:MGI:1926232"
ORIGIN      
        1 msrygrygge tkvyvgnlgt gagkgelera fsyygplrtv wiarnppgfa fvefedprda
       61 edavrgldgk vicgsrvrve lstgmprrsr fdrpparrpf dpndrcyecg ekghyaydch
      121 rysrrrrsrs rsrshsrsrg rrysrsrsrs rgrrsrsasp rrsrsvslrr srsaslrrsr
      181 sgsiigsryf qsrsrsrsrs rsisrprssr spsgsphrsa spermd
//
LOCUS       NP_003424                706 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 132 [Homo sapiens].
ACCESSION   NP_003424
VERSION     NP_003424.3
DBSOURCE    REFSEQ: accession NM_003433.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Liu,Z., Liu,J., Liu,R., Xue,M., Zhang,W., Zhao,X., Zhu,J. and
            Xia,P.
  TITLE     Downregulated ZNF132 predicts unfavorable outcomes in breast Cancer
            via Hypermethylation modification
  JOURNAL   BMC Cancer 21 (1), 367 (2021)
   PUBMED   33827486
  REMARK    GeneRIF: Downregulated ZNF132 predicts unfavorable outcomes in
            breast Cancer via Hypermethylation modification.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Jiang,D., He,Z., Wang,C., Zhou,Y., Li,F., Pu,W., Zhang,X., Feng,X.,
            Zhang,M., Yecheng,X., Xu,Y., Jin,L., Guo,S., Wang,J. and Wang,M.
  TITLE     Epigenetic silencing of ZNF132 mediated by methylation-sensitive
            Sp1 binding promotes cancer progression in esophageal squamous cell
            carcinoma
  JOURNAL   Cell Death Dis 10 (1), 1 (2018)
   PUBMED   30578410
  REMARK    GeneRIF: results suggest that ZNF132 plays an important role in the
            development of esophageal squamous cell carcinoma as a tumor
            suppressor gene and support the underlying mechanism caused by the
            DNA hypermethylation-mediated Sp1-binding decay and gene silencing.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Abildgaard,M.O., Borre,M., Mortensen,M.M., Ulhoi,B.P., Torring,N.,
            Wild,P., Kristensen,H., Mansilla,F., Ottosen,P.D., Dyrskjot,L.,
            Orntoft,T.F. and Sorensen,K.D.
  TITLE     Downregulation of zinc finger protein 132 in prostate cancer is
            associated with aberrant promoter hypermethylation and poor
            prognosis
  JOURNAL   Int J Cancer 130 (4), 885-895 (2012)
   PUBMED   21445975
  REMARK    GeneRIF: downregulation of ZNF132 is associated with aggressive
            prostate cancer.
REFERENCE   4  (residues 1 to 706)
  AUTHORS   Luke,M.M., O'Meara,E.S., Rowland,C.M., Shiffman,D., Bare,L.A.,
            Arellano,A.R., Longstreth,W.T. Jr., Lumley,T., Rice,K., Tracy,R.P.,
            Devlin,J.J. and Psaty,B.M.
  TITLE     Gene variants associated with ischemic stroke: the cardiovascular
            health study
  JOURNAL   Stroke 40 (2), 363-368 (2009)
   PUBMED   19023099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 706)
  AUTHORS   Shiffman,D., O'Meara,E.S., Bare,L.A., Rowland,C.M., Louie,J.Z.,
            Arellano,A.R., Lumley,T., Rice,K., Iakoubova,O., Luke,M.M.,
            Young,B.A., Malloy,M.J., Kane,J.P., Ellis,S.G., Tracy,R.P.,
            Devlin,J.J. and Psaty,B.M.
  TITLE     Association of gene variants with incident myocardial infarction in
            the Cardiovascular Health Study
  JOURNAL   Arterioscler Thromb Vasc Biol 28 (1), 173-179 (2008)
   PUBMED   17975119
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 706)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   7  (residues 1 to 706)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK057460.1, BC109107.1, U09411.1 and BQ774411.1.
            
            On Aug 7, 2007 this sequence version replaced NP_003424.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.65979.1, AK057460.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254166.4/ ENSP00000254166.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..706
                     /product="zinc finger protein 132"
                     /calculated_mol_wt=80492
     Region          37..78
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          105..528
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          116..136
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          144..164
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          238..285
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          293..313
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          321..341
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          349..369
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          377..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          383..>706
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          405..425
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          433..453
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(438,440,442,444..445,448..449,452,466,468,472..473,
                     476..477,480,494,496,498,500..501,504..505,508)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          461..481
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          489..509
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          517..537
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          545..565
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          573..593
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(578,580,582,584..585,588..589,592,606,608,612..613,
                     616..617,620,634,636,638,640..641,644..645,648)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          601..621
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          629..649
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          657..677
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          685..705
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..706
                     /gene="ZNF132"
                     /gene_synonym="pHZ-12"
                     /coded_by="NM_003433.4:333..2453"
                     /db_xref="CCDS:CCDS12980.1"
                     /db_xref="GeneID:7691"
                     /db_xref="HGNC:HGNC:12916"
                     /db_xref="MIM:604074"
ORIGIN      
        1 malpspqvlm glpallmgpa qhtswpcgsa vptlksmvtf edvavyfsqe ewelldaaqr
       61 hlyhsvmlen lelvtslgsw hgvegegahp kqnvsvevlq vripnadpst kkanscdmcg
      121 pflkdilhla ehqgtqseek pytcgacgrd fwlnanlhqh qkehsggkpf rwykdrdalm
      181 ksskvhlsen pftcreggkv ilgscdllql qavdsgqkpy snlgqlpevc ttqklfecsn
      241 cgkaflksst lpnhlrthse eipftcptgg nfleeksilg nkkfhtgeip hvckecgkaf
      301 shssklrkhq kfhtevkyye ciacgktfnh kltfvhhqri hsgerpyecd ecgkafsnrs
      361 hlirhekvht gerpfeclkc grafsqssnf lrhqkvhtqv rpyecsqcgk sfsrssaliq
      421 hwrvhtgerp yecsecgraf nnnsnlaqhq kvhtgerpfe csecgrdfsq sshllrhqkv
      481 htgerpfecc dcgkafsnss tliqhqkvht gqrpyecsec rksfsrsssl iqhwrihtge
      541 kpyecsecgk afahsstlie hwrvhtkerp yecnecgkff sqnsilikhq kvhtgekpyk
      601 csecgkffsr ksslichwrv htgerpyecs ecgrafssns hlvrhqrvht qerpyeciqc
      661 gkafserstl vrhqkvhtre rtyecsqcgk lfshlcnlaq hkkiht
//
LOCUS       NP_059996                131 aa            linear   PRI 27-APR-2025
DEFINITION  leptin receptor gene-related protein isoform 1 [Homo sapiens].
ACCESSION   NP_059996
VERSION     NP_059996.1
DBSOURCE    REFSEQ: accession NM_017526.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Roca-Rivada,A., Do Cruzeiro,M., Denis,R.G., Zhang,Q., Rouault,C.,
            Rouille,Y., Launay,J.M., Cruciani-Guglielmacci,C., Mattot,V.,
            Clement,K., Jockers,R. and Dam,J.
  TITLE     Whole-body deletion of Endospanin 1 protects from
            obesity-associated deleterious metabolic alterations
  JOURNAL   JCI Insight 9 (9), e168418 (2024)
   PUBMED   38716728
  REMARK    GeneRIF: Whole-body deletion of Endospanin 1 protects from
            obesity-associated deleterious metabolic alterations.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Seron,K., Couturier,C., Belouzard,S., Bacart,J., Monte,D.,
            Corset,L., Bocquet,O., Dam,J., Vauthier,V., Lecoeur,C.,
            Bailleul,B., Hoflack,B., Froguel,P., Jockers,R. and Rouille,Y.
  TITLE     Endospanins regulate a postinternalization step of the leptin
            receptor endocytic pathway
  JOURNAL   J Biol Chem 286 (20), 17968-17981 (2011)
   PUBMED   21454707
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 131)
  AUTHORS   Touvier,T., Conte-Auriol,F., Briand,O., Cudejko,C., Paumelle,R.,
            Caron,S., Bauge,E., Rouille,Y., Salles,J.P., Staels,B. and
            Bailleul,B.
  TITLE     LEPROT and LEPROTL1 cooperatively decrease hepatic growth hormone
            action in mice
  JOURNAL   J Clin Invest 119 (12), 3830-3838 (2009)
   PUBMED   19907080
  REMARK    GeneRIF: Transgenic mice expressing either human LEPROT or human
            LEPROTL1 displayed growth retardation, reduced plasma IGF1 levels,
            and impaired hepatic sensitivity to GH, as measured by STAT5
            phosphorylation and Socs2 mRNA expression.
REFERENCE   7  (residues 1 to 131)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 131)
  AUTHORS   Couturier,C., Sarkis,C., Seron,K., Belouzard,S., Chen,P.,
            Lenain,A., Corset,L., Dam,J., Vauthier,V., Dubart,A., Mallet,J.,
            Froguel,P., Rouille,Y. and Jockers,R.
  TITLE     Silencing of OB-RGRP in mouse hypothalamic arcuate nucleus
            increases leptin receptor signaling and prevents diet-induced
            obesity
  JOURNAL   Proc Natl Acad Sci U S A 104 (49), 19476-19481 (2007)
   PUBMED   18042720
REFERENCE   9  (residues 1 to 131)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   10 (residues 1 to 131)
  AUTHORS   Bailleul,B., Akerblom,I. and Strosberg,A.D.
  TITLE     The leptin receptor promoter controls expression of a second
            distinct protein
  JOURNAL   Nucleic Acids Res 25 (14), 2752-2758 (1997)
   PUBMED   9207021
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Y12670.1, AC119800.2 and CA434795.1.
            
            Summary: LEPROT is associated with the Golgi complex and endosomes
            and has a role in cell surface expression of growth hormone
            receptor (GHR; MIM 600946) and leptin receptor (OBR, or LEPR; MIM
            601007), thereby altering receptor-mediated cell signaling
            (Couturier et al., 2007 [PubMed 18042720]; Touvier et al., 2009
            [PubMed 19907080]).[supplied by OMIM, Jul 2010].
            
            Transcript Variant: This variant (1) is dominant and encodes the
            shorter isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.208508.1,
                                           SRR1803616.221243.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371065.9/ ENSP00000360104.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..131
                     /product="leptin receptor gene-related protein isoform 1"
                     /note="OB-R gene-related protein; DnaJ (Hsp40) homolog,
                     subfamily C, member 6; leptin receptor overlapping
                     transcript protein; endospanin-1; leptin receptor
                     gene-related protein"
                     /calculated_mol_wt=14123
     Region          7..124
                     /region_name="Vps55"
                     /note="Vacuolar protein sorting 55; pfam04133"
                     /db_xref="CDD:461188"
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15243.1)"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15243.1)"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15243.1)"
     Site            100..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15243.1)"
     CDS             1..131
                     /gene="LEPROT"
                     /gene_synonym="LEPR; OB-RGRP; OBRGRP; VPS55"
                     /coded_by="NM_017526.5:58..453"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS630.1"
                     /db_xref="GeneID:54741"
                     /db_xref="HGNC:HGNC:29477"
                     /db_xref="MIM:613461"
ORIGIN      
        1 magvkalval sfsgaigltf lmlgcaledy gvywplfvli fhaispiphf iakrvtydsd
       61 atssacrela yffttgivvs afgfpvilar vavikwgacg lvlagnavif ltiqgfflif
      121 grgddfsweq w
//
LOCUS       NP_001347168             610 aa            linear   ROD 27-APR-2025
DEFINITION  copine-5 isoform 1 [Mus musculus].
ACCESSION   NP_001347168
VERSION     NP_001347168.1
DBSOURCE    REFSEQ: accession NM_001360239.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Gomez-Del Arco,P., Isern,J., Jimenez-Carretero,D.,
            Lopez-Maderuelo,D., Pineiro-Sabaris,R., El Abdellaoui-Soussi,F.,
            Torroja,C., Vera-Pedrosa,M.L., Grima-Terren,M., Benguria,A.,
            Simon-Chica,A., Queiro-Palou,A., Dopazo,A., Sanchez-Cabo,F.,
            Jalife,J., de la Pompa,J.L., Filgueiras-Rama,D., Munoz-Canoves,P.
            and Redondo,J.M.
  TITLE     The G4 resolvase Dhx36 modulates cardiomyocyte differentiation and
            ventricular conduction system development
  JOURNAL   Nat Commun 15 (1), 8602 (2024)
   PUBMED   39366945
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Astrof,S., Arriagada,C., Saijoh,Y., Francou,A., Kelly,R.G. and
            Moon,A.
  TITLE     Aberrant differentiation of second heart field mesoderm prefigures
            cellular defects in the outflow tract in response to loss of FGF8
  JOURNAL   Dev Biol 499, 10-21 (2023)
   PUBMED   37060937
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Hiver,S., Shimizu-Mizuno,N., Ikawa,Y., Kajikawa,E., Sai,X.,
            Nishimura,H., Takaoka,K., Nishimura,O., Kuraku,S., Tanaka,S. and
            Hamada,H.
  TITLE     Gse1, a component of the CoREST complex, is required for placenta
            development in the mouse
  JOURNAL   Dev Biol 498, 97-105 (2023)
   PUBMED   37019373
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Goodyer,W.R., Beyersdorf,B.M., Duan,L., van den Berg,N.S.,
            Mantri,S., Galdos,F.X., Puluca,N., Buikema,J.W., Lee,S., Salmi,D.,
            Robinson,E.R., Rogalla,S., Cogan,D.P., Khosla,C., Rosenthal,E.L.
            and Wu,S.M.
  TITLE     In vivo visualization and molecular targeting of the cardiac
            conduction system
  JOURNAL   J Clin Invest 132 (20), e156955 (2022)
   PUBMED   35951416
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Miller,J.A., Nathanson,J., Franjic,D., Shim,S., Dalley,R.A.,
            Shapouri,S., Smith,K.A., Sunkin,S.M., Bernard,A., Bennett,J.L.,
            Lee,C.K., Hawrylycz,M.J., Jones,A.R., Amaral,D.G., Sestan,N.,
            Gage,F.H. and Lein,E.S.
  TITLE     Conserved molecular signatures of neurogenesis in the hippocampal
            subgranular zone of rodents and primates
  JOURNAL   Development 140 (22), 4633-4644 (2013)
   PUBMED   24154525
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Ding,X., Jin,Y., Wu,Y., Wu,Y., Wu,H., Xiong,L., Song,X., Liu,S.,
            Fan,W. and Fan,M.
  TITLE     Localization and cellular distribution of CPNE5 in embryonic mouse
            brain
  JOURNAL   Brain Res 1224, 20-28 (2008)
   PUBMED   18614158
  REMARK    GeneRIF: Our results demonstrate that CPNE5 is expressed in both
            neural progenitor cells and the differentiated neurons during the
            neural development, which suggests that CPNE5 might play an
            important role in the development of murine central nervous system.
REFERENCE   9  (residues 1 to 610)
  AUTHORS   Humphreys,N.E., Xu,D., Hepworth,M.R., Liew,F.Y. and Grencis,R.K.
  TITLE     IL-33, a potent inducer of adaptive immunity to intestinal
            nematodes
  JOURNAL   J Immunol 180 (4), 2443-2449 (2008)
   PUBMED   18250453
REFERENCE   10 (residues 1 to 610)
  AUTHORS   Creutz,C.E., Tomsig,J.L., Snyder,S.L., Gautier,M.C., Skouri,F.,
            Beisson,J. and Cohen,J.
  TITLE     The copines, a novel class of C2 domain-containing,
            calcium-dependent, phospholipid-binding proteins conserved from
            Paramecium to humans
  JOURNAL   J Biol Chem 273 (3), 1393-1402 (1998)
   PUBMED   9430674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC162182.2 and AC167363.3.
            
            Summary: Calcium-dependent membrane-binding proteins may regulate
            molecular events at the interface of the cell membrane and
            cytoplasm. This gene is one of several genes that encodes a
            calcium-dependent protein containing two N-terminal type II C2
            domains and an integrin A domain-like sequence in the C-terminus.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.6355.1,
                                           SRR1660825.63298.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164139 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 15.14 cM"
     Protein         1..610
                     /product="copine-5 isoform 1"
                     /note="copine-5"
                     /calculated_mol_wt=67196
     Region          23..137
                     /region_name="C2A_Copine"
                     /note="C2 domain first repeat in Copine; cd04048"
                     /db_xref="CDD:176013"
     Site            order(38,44,98,100,110)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176013"
     Region          194..305
                     /region_name="C2B_Copine"
                     /note="C2 domain second repeat in Copine; cd04047"
                     /db_xref="CDD:176012"
     Site            order(209,215,271,273,279)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176012"
     Region          315..571
                     /region_name="vWA_copine_like"
                     /note="VWA Copine: Copines are phospholipid-binding
                     proteins originally identified in paramecium. They are
                     found in human and orthologues have been found in C.
                     elegans and Arabidopsis Thaliana. None have been found in
                     D. Melanogaster or S. Cereviciae; cd01459"
                     /db_xref="CDD:238736"
     Site            order(351,353,355,449,479)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238736"
     CDS             1..610
                     /gene="Cpne5"
                     /gene_synonym="A830083G22Rik"
                     /coded_by="NM_001360239.1:84..1916"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:240058"
                     /db_xref="MGI:MGI:2385908"
ORIGIN      
        1 meqpedmasl sefdslagsi patkveitvs crnlldkdmf sksdplcvmy tqgmenkqwr
       61 efgrtevidn tlnpdfvrkf ivdyffeekq nlrfdlydvd skspdlskhd flgqafctlg
      121 eivgssgsrl ekpltigtfs lnsrtgkpmp avsngsglwm essrttgpea sggvpgkkcg
      181 tiilsaeels ncrdvatmqf cankldkkdf fgksdpflvf yrsnedgtft ichktevmkn
      241 tlnpvwqtfs ipvralcngd ydrtikvevy dwdrdgshdf igefttsyre largqsqfni
      301 yevinpkkkm kkkkyvnsgt vtllsfaves estfldyikg gtqinftvai dftasngnps
      361 qstslhymsp yqlnayalal tavgeiiqhy dsdkmfpalg fgaklppdgr vshefplngn
      421 qenpsccgid gileayhssl rtvqlygptn fapvvthvar naaavqdgsq ysvlliitdg
      481 visdmaqtke aivnaaklpm siiivgvgqa efdamveldg ddvrissrgk laerdivqfv
      541 pfrdyvdrtg nhvlsmarla rdvlaeipdq lvsymkaqgi rprpppaapa qsppqspahs
      601 ppgspvhthi
//
LOCUS       NP_997200                364 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 474 [Homo sapiens].
ACCESSION   NP_997200
VERSION     NP_997200.1
DBSOURCE    REFSEQ: accession NM_207317.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB058648.1, AY461732.1 and AK290985.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY461732.1, SRR5189667.219206.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296600.5/ ENSP00000296600.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.2"
     Protein         1..364
                     /product="zinc finger protein 474"
                     /note="4933409D10Rik; TSZFP; testis-specific zinc finger
                     protein"
                     /calculated_mol_wt=40184
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6S9Z5.1)"
     Region          37..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6S9Z5.1)"
     Region          97..116
                     /region_name="zf-C2HC_2"
                     /note="zinc-finger of a C2HC-type; pfam13913"
                     /db_xref="CDD:464037"
     Region          127..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6S9Z5.1)"
     Region          164..188
                     /region_name="zf-C2HC_2"
                     /note="zinc-finger of a C2HC-type; pfam13913"
                     /db_xref="CDD:464037"
     Region          187..214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6S9Z5.1)"
     Region          221..243
                     /region_name="zf-C2HC_2"
                     /note="zinc-finger of a C2HC-type; pfam13913"
                     /db_xref="CDD:464037"
     Region          283..307
                     /region_name="zf-C2HC_2"
                     /note="zinc-finger of a C2HC-type; pfam13913"
                     /db_xref="CDD:464037"
     CDS             1..364
                     /gene="ZNF474"
                     /coded_by="NM_207317.3:351..1445"
                     /db_xref="CCDS:CCDS4130.1"
                     /db_xref="GeneID:133923"
                     /db_xref="HGNC:HGNC:23245"
ORIGIN      
        1 mergkkkris nklqqtfhhs keptflinqa gllssdsyss lspetesvnp geniktdtqk
       61 krpgtvilsk lssrriises qlsppvipar rpgfrvcyic grefgsqsia ihepqclqkw
      121 hiensklpkh lrrpepskpq slsssgsysl qatneaafqs aqaqllpces cgrtflpdhl
      181 lvhhrsckpk gegpraphsn ssdhltglkk acsgtparpr tvicyicgke fgtlslpihe
      241 pkclekwkme ndrlpvelhq plpqkpqplp naqssqagpn qaqlvfcphc sriftsdrll
      301 vhqrsckthp ygpkyqnlnl gskgglkeyt nskqqrnraa psvtdkviha tqdalgepgg
      361 alcl
//
LOCUS       NP_006038                932 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding protein 12 [Homo sapiens].
ACCESSION   NP_006038
VERSION     NP_006038.2
DBSOURCE    REFSEQ: accession NM_006047.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Gao,C., Zhu,R., Shen,J., Xu,T., She,Y. and Chen,Z.
  TITLE     RBM12 regulates the progression of hepatocellular cancer via
            miR-497-5p/CPNE1 Axis
  JOURNAL   Environ Res 239 (Pt 1), 117203 (2023)
   PUBMED   37793588
  REMARK    GeneRIF: RBM12 regulates the progression of hepatocellular cancer
            via miR-497-5p/CPNE1 Axis.
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Semesta,K.M., Garces,A. and Tsvetanova,N.G.
  TITLE     The psychosis risk factor RBM12 encodes a novel repressor of
            GPCR/cAMP signal transduction
  JOURNAL   J Biol Chem 299 (9), 105133 (2023)
   PUBMED   37543364
  REMARK    GeneRIF: The psychosis risk factor RBM12 encodes a novel repressor
            of GPCR/cAMP signal transduction.
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Wakabayashi,A., Kihiu,M., Sharma,M., Thrasher,A.J., Saari,M.S.,
            Quesnel-Vallieres,M., Abdulmalik,O., Peslak,S.A., Khandros,E.,
            Keller,C.A., Giardine,B.M., Barash,Y., Hardison,R.C., Shi,J. and
            Blobel,G.A.
  TITLE     Identification and characterization of RBM12 as a novel regulator
            of fetal hemoglobin expression
  JOURNAL   Blood Adv 6 (23), 5956-5968 (2022)
   PUBMED   35622975
  REMARK    GeneRIF: Identification and characterization of RBM12 as a novel
            regulator of fetal hemoglobin expression.
REFERENCE   4  (residues 1 to 932)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 932)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 932)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 932)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 932)
  AUTHORS   Yang,W., Ng,P., Zhao,M., Wong,T.K., Yiu,S.M. and Lau,Y.L.
  TITLE     Promoter-sharing by different genes in human genome--CPNE1 and
            RBM12 gene pair as an example
  JOURNAL   BMC Genomics 9, 456 (2008)
   PUBMED   18831769
  REMARK    GeneRIF: RBM12 shares a promoter and 5'UTR exons with CPNE1. This
            genomic structure is conserved among multiple species.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 932)
  AUTHORS   Stover,C., Gradl,G., Jentsch,I., Speicher,M.R., Wieser,R. and
            Schwaeble,W.
  TITLE     cDNA cloning, chromosome assignment, and genomic structure of a
            human gene encoding a novel member of the RBM family
  JOURNAL   Cytogenet Cell Genet 92 (3-4), 225-230 (2001)
   PUBMED   11435693
REFERENCE   10 (residues 1 to 932)
  AUTHORS   Ueki,N., Oda,T., Kondo,M., Yano,K., Noguchi,T. and Muramatsu,M.
  TITLE     Selection system for genes encoding nuclear-targeted proteins
  JOURNAL   Nat Biotechnol 16 (13), 1338-1342 (1998)
   PUBMED   9853615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB060608.1, AF345332.1,
            AL109827.8 and AA825305.1.
            
            On Apr 4, 2002 this sequence version replaced NP_006038.1.
            
            Summary: This gene encodes a protein that contains several
            RNA-binding motifs, potential transmembrane domains, and
            proline-rich regions. This gene and the gene for copine I overlap
            at map location 20q11.21. Alternative splicing in the 5' UTR
            results in four transcript variants. All variants encode the same
            protein. [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (1) is the predominant transcript.
            All variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.192945.1,
                                           SRR1660809.199569.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155550, SAMEA2467144
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374114.8/ ENSP00000363228.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..932
                     /product="RNA-binding protein 12"
                     /note="SH3/WW domain anchor protein in the nucleus"
                     /calculated_mol_wt=97265
     Region          1..92
                     /region_name="RRM1_RBM12"
                     /note="RNA recognition motif 1 (RRM1) found in RNA-binding
                     protein 12 (RBM12) and similar proteins; cd12745"
                     /db_xref="CDD:241189"
     Region          96..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTZ6.1)"
     Region          303..377
                     /region_name="RRM2_RBM12"
                     /note="RNA recognition motif 2 (RRM2) found in RNA-binding
                     protein 12 (RBM12) and similar proteins; cd12747"
                     /db_xref="CDD:410141"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NTZ6.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NTZ6.1)"
     Region          392..424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTZ6.1)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NTZ6.1)"
     Region          421..521
                     /region_name="RRM3_RBM12"
                     /note="RNA recognition motif 3 (RRM3) found in RNA-binding
                     protein 12 (RBM12) and similar proteins; cd12512"
                     /db_xref="CDD:409934"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NTZ6.1)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NTZ6.1)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NTZ6.1)"
     Region          545..632
                     /region_name="RRM4_RBM12"
                     /note="RNA recognition motif 4 (RRM4) found in RNA-binding
                     protein 12 (RBM12) and similar proteins; cd12749"
                     /db_xref="CDD:410143"
     Region          <631..>699
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     Region          717..853
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTZ6.1)"
     Region          855..930
                     /region_name="RRM5_RBM12"
                     /note="RNA recognition motif 5 (RRM5) found in RNA-binding
                     protein 12 (RBM12) and similar proteins; cd12751"
                     /db_xref="CDD:410145"
     Site            order(866..871,888,890,893..894)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:410145"
     CDS             1..932
                     /gene="RBM12"
                     /gene_synonym="HRIHFB2091; SCZD19; SWAN"
                     /coded_by="NM_006047.6:249..3047"
                     /db_xref="CCDS:CCDS13261.1"
                     /db_xref="GeneID:10137"
                     /db_xref="HGNC:HGNC:9898"
                     /db_xref="MIM:607179"
ORIGIN      
        1 mavvirlqgl pivagtmdir hffsgltipd ggvhivggel geafivfatd edarlgmmrt
       61 ggtikgskvt lllssktemq nmielsrrrf etanldippa nasrsgppps sgmssrvnlp
      121 ttvsnfnnps psvvtattsv hesnkniqtf stasvgtapp nmgasfgspt fsstvpstas
      181 pmntvppppi ppipampslp pmpsippipv pppvptlppv ppvppippvp svppmtplpp
      241 msgmpplnpp pvaplpagmn gsgapmnlnn nlnpmflgpl npvnpiqmns qssvkplpin
      301 pddlyvsvhg mpfsamendv rdffhglrvd avhllkdhvg rnngnglvkf lspqdtfeal
      361 krnrmlmiqr yvevspater qwvaagghit fkqnmgpsgq thpppqtlpr skspsgqkrs
      421 rsrspheagf cvylkglpfe aenkhvidff kkldivedsi yiaygpngka tgegfvefrn
      481 eadykaalcr hkqymgnrfi qvhpitkkgm lekidmirkr lqnfsydqre milnpegdvn
      541 sakvcahitn ipfsitkmdv lqflegipvd enavhvlvdn ngqglgqalv qfkneddark
      601 serlhrkkln greafvhvvt ledmreiekn ppaqgkkglk mpvpgnpavp gmpnaglpgv
      661 glpsaglpga glpstglpgs aitsaglpga gmpsagipsa ggeehafltv gskeanngpp
      721 fnfpgnfggs nafgppippp glgggafgda rpgmpsvgns glpglgldvp gfgggpnnls
      781 gpsgfgggpq nfgngpgslg gppgfgsgpp glgsapghlg gppafgpgpg pgpgpgpihi
      841 ggppgfasss gkpgptvikv qnmpftvsid eildffygyq vipgsvclky nekgmptgea
      901 mvafesrdea taavidlndr pigsrkvklv lg
//
LOCUS       NP_001353527             820 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001353527
VERSION     NP_001353527.1
DBSOURCE    REFSEQ: accession NM_001366598.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 820)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 820)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 820)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 820)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 820)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 820)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 820)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.245422.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..820
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 9"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=92398
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <522..>656
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..820
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366598.1:2163..4625"
                     /note="isoform 9 is encoded by transcript variant 46"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels esedkggkma aadsvqqrrq yrrqnqqsss dsgsssssed
      421 erpkrshvkn gevgrrrrhs psrsaspspr krqketsprg rrrrspsppp trrrrspspa
      481 ppprrrrtpt ppprrrtpsp pprrrspspr rysppiqrry spspppkrrt aspppppkrr
      541 aspspppkrr vshspppkqr sspvtkrrsp slsskhrkgs spsrstrear spqpnkrhsp
      601 sprprapqts sspppvrrga ssspqrrqsp spstrpirrv srtpepkkik kaaspspqsv
      661 rrvsssrsvs gspepaakkp pappspvqsq spstnwspav pvkkaksptp spspprnsdq
      721 egggkkkkkk kdkkhkkdkk hkkhkkhkke kavaaaaaaa vtpaaiaaat ttlaqeepva
      781 apepkketes eaednlddle khlrekalrs mrkaqvspqs
//
LOCUS       NP_000994                114 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein P1 isoform 1 [Homo sapiens].
ACCESSION   NP_000994 NP_001074326
VERSION     NP_000994.1
DBSOURCE    REFSEQ: accession NM_001003.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Tripathi,M., Gauthier,K., Sandireddy,R., Zhou,J., Guptta,P.,
            Sakthivel,S., Teo,W.W., Naing,Y.T., Arul,K., Tikno,K., Park,S.H.,
            Wu,Y., Wang,L., Bay,B.H., Sun,L., Giguere,V., Chow,P.K.H.,
            Ghosh,S., McDonnell,D.P., Yen,P.M. and Singh,B.K.
  TITLE     Esrra regulates Rplp1-mediated translation of lysosome proteins
            suppressed in metabolic dysfunction-associated steatohepatitis and
            reversed by alternate day fasting
  JOURNAL   Mol Metab 87, 101997 (2024)
   PUBMED   39032642
  REMARK    GeneRIF: Esrra regulates Rplp1-mediated translation of lysosome
            proteins suppressed in metabolic dysfunction-associated
            steatohepatitis and reversed by alternate day fasting.
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Yang,W., Wang,H., Li,Z., Zhang,L., Liu,J., Kirchhoff,F., Huan,C.
            and Zhang,W.
  TITLE     RPLP1 restricts HIV-1 transcription by disrupting C/EBPbeta binding
            to the LTR
  JOURNAL   Nat Commun 15 (1), 5290 (2024)
   PUBMED   38906865
  REMARK    GeneRIF: RPLP1 restricts HIV-1 transcription by disrupting
            C/EBPbeta binding to the LTR.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Peterson,R., Minchella,P., Cui,W., Graham,A. and Nothnick,W.B.
  TITLE     RPLP1 Is Up-Regulated in Human Adenomyosis and Endometrial
            Adenocarcinoma Epithelial Cells and Is Essential for Cell Survival
            and Migration In Vitro
  JOURNAL   Int J Mol Sci 24 (3), 2690 (2023)
   PUBMED   36769010
  REMARK    GeneRIF: RPLP1 Is Up-Regulated in Human Adenomyosis and Endometrial
            Adenocarcinoma Epithelial Cells and Is Essential for Cell Survival
            and Migration In Vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Horbowicz-Drozdzal,P., Kamel,K., Kmiecik,S., Borkiewicz,L.,
            Tumer,N.E., Shaw,P.C., Tchorzewski,M. and Grela,P.
  TITLE     Phosphorylation of the conserved C-terminal domain of ribosomal
            P-proteins impairs the mode of interaction with plant toxins
  JOURNAL   FEBS Lett 595 (17), 2221-2236 (2021)
   PUBMED   34328639
  REMARK    GeneRIF: Phosphorylation of the conserved C-terminal domain of
            ribosomal P-proteins impairs the mode of interaction with plant
            toxins.
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Chan,S.H., Hung,F.S., Chan,D.S. and Shaw,P.C.
  TITLE     Trichosanthin interacts with acidic ribosomal proteins P0 and P1
            and mitotic checkpoint protein MAD2B
  JOURNAL   Eur J Biochem 268 (7), 2107-2112 (2001)
   PUBMED   11277934
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
   PUBMED   11401437
REFERENCE   8  (residues 1 to 114)
  AUTHORS   Tchorzewski,M., Boldyreff,B., Issinger,O.G. and Grankowski,N.
  TITLE     Analysis of the protein-protein interactions between the human
            acidic ribosomal P-proteins: evaluation by the two hybrid system
  JOURNAL   Int J Biochem Cell Biol 32 (7), 737-746 (2000)
   PUBMED   10856704
REFERENCE   9  (residues 1 to 114)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 114)
  AUTHORS   Rich,B.E. and Steitz,J.A.
  TITLE     Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
            cDNA clones, in vitro synthesis, and assembly
  JOURNAL   Mol Cell Biol 7 (11), 4065-4074 (1987)
   PUBMED   3323886
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AC027237.8.
            
            On Mar 28, 2007 this sequence version replaced NP_001074326.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            phosphoprotein that is a component of the 60S subunit. The protein,
            which is a functional equivalent of the E. coli L7/L12 ribosomal
            protein, belongs to the L12P family of ribosomal proteins. It plays
            an important role in the elongation step of protein synthesis.
            Unlike most ribosomal proteins, which are basic, the encoded
            protein is acidic. Its C-terminal end is nearly identical to the
            C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1
            protein can interact with P0 and P2 to form a pentameric complex
            consisting of P1 and P2 dimers, and a P0 monomer. The protein is
            located in the cytoplasm. Two alternatively spliced transcript
            variants that encode different proteins have been observed. As is
            typical for genes encoding ribosomal proteins, there are multiple
            processed pseudogenes of this gene dispersed through the genome.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This predominant variant (1) is the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP367167.1, SRR5189652.227177.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260379.11/ ENSP00000346037.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q23"
     Protein         1..114
                     /product="large ribosomal subunit protein P1 isoform 1"
                     /note="60S acidic ribosomal protein P1; acidic ribosomal
                     phosphoprotein P1; ribosomal protein, large, P1; large
                     ribosomal subunit protein P1"
                     /calculated_mol_wt=11383
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P05386.1)"
     Region          6..>63
                     /region_name="Ribosomal_P1"
                     /note="Ribosomal protein P1. This subfamily represents the
                     eukaryotic large ribosomal protein P1. Eukaryotic P1 and
                     P2 are functionally equivalent to the bacterial protein
                     L7/L12, but are not homologous to L7/L12. P1 is located in
                     the L12 stalk, with proteins...; cd05831"
                     /db_xref="CDD:100109"
     Region          69..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05386.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14997482,
                     ECO:0007744|PubMed:16807684; propagated from
                     UniProtKB/Swiss-Prot (P05386.1)"
     CDS             1..114
                     /gene="RPLP1"
                     /gene_synonym="LP1; P1; RPP1"
                     /coded_by="NM_001003.3:132..476"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10233.1"
                     /db_xref="GeneID:6176"
                     /db_xref="HGNC:HGNC:10372"
                     /db_xref="MIM:180520"
ORIGIN      
        1 masvselaci ysalilhdde vtvtedkina likaagvnve pfwpglfaka lanvnigsli
       61 cnvgaggpap aagaapaggp apstaaapae ekkveakkee seesdddmgf glfd
//
LOCUS       NP_004206                213 aa            linear   PRI 27-APR-2025
DEFINITION  receptor-binding cancer antigen expressed on SiSo cells [Homo
            sapiens].
ACCESSION   NP_004206
VERSION     NP_004206.1
DBSOURCE    REFSEQ: accession NM_004215.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Wirges,A., Bunse,M., Joedicke,J.J., Blanc,E., Gudipati,V.,
            Moles,M.W., Shiku,H., Beule,D., Huppa,J.B., Hopken,U.E. and Rehm,A.
  TITLE     EBAG9 silencing exerts an immune checkpoint function without
            aggravating adverse effects
  JOURNAL   Mol Ther 30 (11), 3358-3378 (2022)
   PUBMED   35821635
  REMARK    GeneRIF: EBAG9 silencing exerts an immune checkpoint function
            without aggravating adverse effects.
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Suwiwat,S., Tungsinmunlong,K. and Siriaungkul,S.
  TITLE     Expression of CD44v6 and RCAS1 in Uterine Cervical Carcinoma
            Infected with Human Papillomavirus and Its Effect on Cell
            Proliferation and Differentiation
  JOURNAL   Asian Pac J Cancer Prev 23 (7), 2431-2439 (2022)
   PUBMED   35901351
  REMARK    GeneRIF: Expression of CD44v6 and RCAS1 in Uterine Cervical
            Carcinoma Infected with Human Papillomavirus and Its Effect on Cell
            Proliferation and Differentiation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Szubert,S., Koper,K., Dutsch-Wicherek,M.M. and Kojs,Z.
  TITLE     The potential predictive value of serum srCaS1 levels for overall
            survival in endometrial cancer
  JOURNAL   Ginekol Pol 90 (3), 134-140 (2019)
   PUBMED   30950002
  REMARK    GeneRIF: Studied soluble cancer-associated surface antigen (srCaS1)
            levels as a biomarker for survival in endometrial cancer. Found
            elevated serum sRCAS1 to be associated with shortened overall
            survival in endometrial cancer patients.
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Dong,J., Sun,G. and Zhu,H.
  TITLE     Diagnostic value of soluble receptor-binding cancer antigen
            expressed on SiSo cells and carcinoembryonic antigen in
            differentiating malignant from benign pleural effusion
  JOURNAL   Tumour Biol 37 (3), 3257-3264 (2016)
   PUBMED   26438059
  REMARK    GeneRIF: Data suggest that joint detection of receptor-binding
            cancer antigen expressed on SiSo cells (RCAS1) and carcinoembryonic
            antigen (CEA) can improve the diagnostic sensitivity and
            specificity.
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Matsushima,T., Nakashima,M., Oshima,K., Abe,Y., Nishimura,J.,
            Nawata,H., Watanabe,T. and Muta,K.
  TITLE     Receptor binding cancer antigen expressed on SiSo cells, a novel
            regulator of apoptosis of erythroid progenitor cells
  JOURNAL   Blood 98 (2), 313-321 (2001)
   PUBMED   11435298
REFERENCE   7  (residues 1 to 213)
  AUTHORS   Ohshima,K., Nakashima,M., Sonoda,K., Kikuchi,M. and Watanabe,T.
  TITLE     Expression of RCAS1 and FasL in human trophoblasts and uterine
            glands during pregnancy: the possible role in immune privilege
  JOURNAL   Clin Exp Immunol 123 (3), 481-486 (2001)
   PUBMED   11298137
REFERENCE   8  (residues 1 to 213)
  AUTHORS   Ikeda,K., Sato,M., Tsutsumi,O., Tsuchiya,F., Tsuneizumi,M., Emi,M.,
            Imoto,I., Inazawa,J., Muramatsu,M. and Inoue,S.
  TITLE     Promoter analysis and chromosomal mapping of human EBAG9 gene
  JOURNAL   Biochem Biophys Res Commun 273 (2), 654-660 (2000)
   PUBMED   10873660
REFERENCE   9  (residues 1 to 213)
  AUTHORS   Nakashima,M., Sonoda,K. and Watanabe,T.
  TITLE     Inhibition of cell growth and induction of apoptotic cell death by
            the human tumor-associated antigen RCAS1
  JOURNAL   Nat Med 5 (8), 938-942 (1999)
   PUBMED   10426319
REFERENCE   10 (residues 1 to 213)
  AUTHORS   Watanabe,T., Inoue,S., Hiroi,H., Orimo,A., Kawashima,H. and
            Muramatsu,M.
  TITLE     Isolation of estrogen-responsive genes with a CpG island library
  JOURNAL   Mol Cell Biol 18 (1), 442-449 (1998)
   PUBMED   9418891
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD108096.1, BC022506.1,
            AA812215.1 and AI619447.1.
            
            Summary: This gene was identified as an estrogen-responsive gene.
            Regulation of transcription by estrogen is mediated by estrogen
            receptor, which binds to the estrogen-responsive element found in
            the 5'-flanking region of this gene. The encoded protein is a
            tumor-associated antigen that is expressed at high frequency in a
            variety of cancers. Alternate splicing results in multiple
            transcript variants. A pseudogene of this gene has been defined on
            chromosome 10. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022506.1, SRR1660809.202546.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337573.10/ ENSP00000337675.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q23.2"
     Protein         1..213
                     /product="receptor-binding cancer antigen expressed on
                     SiSo cells"
                     /note="cancer-associated surface antigen RCAS1; estrogen
                     receptor-binding fragment-associated gene 9 protein;
                     receptor-binding cancer antigen expressed on SiSo cells 1"
                     /calculated_mol_wt=24246
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00559.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00559.1)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (O00559.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (O00559.1)"
     Region          <160..203
                     /region_name="CCDC47"
                     /note="PAT complex subunit CCDC47; cl46382"
                     /db_xref="CDD:480722"
     Region          178..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00559.1)"
     CDS             1..213
                     /gene="EBAG9"
                     /gene_synonym="EB9; PDAF"
                     /coded_by="NM_004215.5:305..946"
                     /db_xref="CCDS:CCDS6313.1"
                     /db_xref="GeneID:9166"
                     /db_xref="HGNC:HGNC:3123"
                     /db_xref="MIM:605772"
ORIGIN      
        1 maitqfrlfk fctclatvfs flkrlicrsg rgrklsgdqi tlpttvdyss vpkqtdveew
       61 tswdedapts vkieggngnv atqqnsleql epdyfkdmtp tirktqkivi kkreplnfgi
      121 pdgstgfssr laatqdlpfi hqsselgdld twqentnawe eeedaawqae evlrqqklad
      181 rekraaeqqr kkmekeaqrl mkkeqnkigv kls
//
LOCUS       NP_001166245             716 aa            linear   PRI 27-APR-2025
DEFINITION  protein C-mannosyl-transferase DPY19L3 [Homo sapiens].
ACCESSION   NP_001166245
VERSION     NP_001166245.1
DBSOURCE    REFSEQ: accession NM_001172774.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Baydoun,H., Kato,Y., Kamo,H., Husch,A., Mizuta,H., Kawahara,R. and
            Simizu,S.
  TITLE     DPY19L3 promotes vasculogenic mimicry by its C-mannosyltransferase
            activity
  JOURNAL   Oncol Res 32 (4), 607-614 (2024)
   PUBMED   38560568
  REMARK    GeneRIF: DPY19L3 promotes vasculogenic mimicry by its
            C-mannosyltransferase activity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Niwa,Y., Nakano,Y., Suzuki,T., Yamagishi,M., Otani,K., Dohmae,N.
            and Simizu,S.
  TITLE     Topological analysis of DPY19L3, a human C-mannosyltransferase
  JOURNAL   FEBS J 285 (6), 1162-1174 (2018)
   PUBMED   29405629
  REMARK    GeneRIF: Data indicate that N-glycosylations of
            C-mannosyltransferase DPY19L3 (DPY19L3) do not have any roles for
            its enzymatic activity.
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Niwa,Y., Suzuki,T., Dohmae,N. and Simizu,S.
  TITLE     Identification of DPY19L3 as the C-mannosyltransferase of
            R-spondin1 in human cells
  JOURNAL   Mol Biol Cell 27 (5), 744-756 (2016)
   PUBMED   26764097
  REMARK    GeneRIF: DPY19L3 is the C-mannosyltransferase of Rspo1 at
            tryptophan(156).
REFERENCE   5  (residues 1 to 716)
  AUTHORS   Smith,E.N., Bloss,C.S., Badner,J.A., Barrett,T., Belmonte,P.L.,
            Berrettini,W., Byerley,W., Coryell,W., Craig,D., Edenberg,H.J.,
            Eskin,E., Foroud,T., Gershon,E., Greenwood,T.A., Hipolito,M.,
            Koller,D.L., Lawson,W.B., Liu,C., Lohoff,F., McInnis,M.G.,
            McMahon,F.J., Mirel,D.B., Murray,S.S., Nievergelt,C.,
            Nurnberger,J., Nwulia,E.A., Paschall,J., Potash,J.B., Rice,J.,
            Schulze,T.G., Scheftner,W., Panganiban,C., Zaitlen,N., Zandi,P.P.,
            Zollner,S., Schork,N.J. and Kelsoe,J.R.
  TITLE     Genome-wide association study of bipolar disorder in European
            American and African American individuals
  JOURNAL   Mol Psychiatry 14 (8), 755-763 (2009)
   PUBMED   19488044
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA852420.1, AK129497.1, AK126757.1 and AL833713.1.
            
            Transcript Variant: This variant (2) represents use of an alternate
            promoter and 5' UTR, compared to variant 1. Both variants 1 and 2
            encode the same isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.211580.1,
                                           SRR1803615.195009.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392250.7/ ENSP00000376081.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..716
                     /product="protein C-mannosyl-transferase DPY19L3"
                     /note="protein dpy-19 homolog 3; dpy-19-like protein 3;
                     probable C-mannosyltransferase DPY19L3; dpy-19-like 3;
                     dpy-19 like 3"
                     /calculated_mol_wt=83066
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Region          46..712
                     /region_name="Dpy19L3"
                     /note="C-mannosyltransferase Dpy-19-like protein 3
                     (Dpy19L3); cd20181"
                     /db_xref="CDD:439134"
     Region          46..62
                     /region_name="putative TM segment 1"
                     /note="putative TM segment 1 [structural motif]"
                     /db_xref="CDD:439134"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29405629; propagated from
                     UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Site            155..182
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Region          155..176
                     /region_name="putative TM segment 2"
                     /note="putative TM segment 2 [structural motif]"
                     /db_xref="CDD:439134"
     Region          180..196
                     /region_name="putative TM segment 3"
                     /note="putative TM segment 3 [structural motif]"
                     /db_xref="CDD:439134"
     Region          216..230
                     /region_name="putative TM segment 4"
                     /note="putative TM segment 4 [structural motif]"
                     /db_xref="CDD:439134"
     Site            240..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Region          242..257
                     /region_name="putative TM segment 5"
                     /note="putative TM segment 5 [structural motif]"
                     /db_xref="CDD:439134"
     Region          263..281
                     /region_name="putative TM segment 6"
                     /note="putative TM segment 6 [structural motif]"
                     /db_xref="CDD:439134"
     Site            263..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Region          289..306
                     /region_name="putative TM segment 7"
                     /note="putative TM segment 7 [structural motif]"
                     /db_xref="CDD:439134"
     Site            290..306
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Region          309..325
                     /region_name="putative TM segment 8"
                     /note="putative TM segment 8 [structural motif]"
                     /db_xref="CDD:439134"
     Site            309..323
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Site            339..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Region          344..362
                     /region_name="putative TM segment 9"
                     /note="putative TM segment 9 [structural motif]"
                     /db_xref="CDD:439134"
     Site            415..437
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Region          416..437
                     /region_name="putative TM segment 10"
                     /note="putative TM segment 10 [structural motif]"
                     /db_xref="CDD:439134"
     Site            466..485
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Region          467..483
                     /region_name="putative TM segment 11"
                     /note="putative TM segment 11 [structural motif]"
                     /db_xref="CDD:439134"
     Region          487..509
                     /region_name="putative TM segment 12"
                     /note="putative TM segment 12 [structural motif]"
                     /db_xref="CDD:439134"
     Site            488..499
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Site            523..539
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     Region          524..539
                     /region_name="putative TM segment 13"
                     /note="putative TM segment 13 [structural motif]"
                     /db_xref="CDD:439134"
     Site            704
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29405629; propagated from
                     UniProtKB/Swiss-Prot (Q6ZPD9.1)"
     CDS             1..716
                     /gene="DPY19L3"
                     /coded_by="NM_001172774.2:178..2328"
                     /db_xref="CCDS:CCDS12422.1"
                     /db_xref="GeneID:147991"
                     /db_xref="HGNC:HGNC:27120"
                     /db_xref="MIM:613894"
ORIGIN      
        1 mmsirqrrei ratevsedfp aqeenvklen klpsgctsrr lwkilsltig gtialcigll
       61 tsvylatlhe ndlwfsnike vereisfrte cglyysyykq mlqaptlvqg fhgliydnkt
      121 esmktinllq rmniyqevfl silyrvlpiq kylepvyfyi ytlfglqaiy vtalyitswl
      181 lsgtwlsgll aafwyvtnri dttrveftip lrenwalpff aiqiaaityf lrpnlqplse
      241 rltllaifis tflfsltwqf nqfmmlmqal vlftldsldm lpavkatwly giqitslllv
      301 cilqffnsmi lgsllisfnl svfiarklqk nlktgsflnr lgklllhlfm vlcltlflnn
      361 iikkilnlks dehifkflka kfglgatrdf danlylceea fgllpfntfg rlsdtllfya
      421 yifvlsitvi vafvvafhnl sdstnqqsvg kmekgtvdlk petaynliht ilfgflalst
      481 mrmkylwtsh mcvfasfglc speiwelllk svhlynpkri cimrysvpil illylcykfw
      541 pgmmdelsel refydpdtve lmnwinsntp rkavfagsmq llagvklctg rtltnhphye
      601 dsslrertra vyqiyakrap eevhallrsf gtdyvileds icyerrhrrg crlrdlldia
      661 nghmmdgpge ndpdlkpadh prfceeikrn lppyvayftr vfqnktfhvy klsrnk
//
LOCUS       NP_001348993             175 aa            linear   ROD 27-APR-2025
DEFINITION  EKC/KEOPS complex subunit Tprkb isoform a [Mus musculus].
ACCESSION   NP_001348993 XP_006506631
VERSION     NP_001348993.1
DBSOURCE    REFSEQ: accession NM_001362064.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Iwata,S., Sasaki,T., Nagahara,M. and Iwamoto,T.
  TITLE     An efficient i-GONAD method for creating and maintaining lethal
            mutant mice using an inversion balancer identified from the
            C3H/HeJJcl strain
  JOURNAL   G3 (Bethesda) 11 (8) (2021)
   PUBMED   34849815
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Braun,D.A., Rao,J., Mollet,G., Schapiro,D., Daugeron,M.C., Tan,W.,
            Gribouval,O., Boyer,O., Revy,P., Jobst-Schwan,T., Schmidt,J.M.,
            Lawson,J.A., Schanze,D., Ashraf,S., Ullmann,J.F.P.,
            Hoogstraten,C.A., Boddaert,N., Collinet,B., Martin,G., Liger,D.,
            Lovric,S., Furlano,M., Guerrera,I.C., Sanchez-Ferras,O., Hu,J.F.,
            Boschat,A.C., Sanquer,S., Menten,B., Vergult,S., De Rocker,N.,
            Airik,M., Hermle,T., Shril,S., Widmeier,E., Gee,H.Y., Choi,W.I.,
            Sadowski,C.E., Pabst,W.L., Warejko,J.K., Daga,A., Basta,T.,
            Matejas,V., Scharmann,K., Kienast,S.D., Behnam,B., Beeson,B.,
            Begtrup,A., Bruce,M., Ch'ng,G.S., Lin,S.P., Chang,J.H., Chen,C.H.,
            Cho,M.T., Gaffney,P.M., Gipson,P.E., Hsu,C.H., Kari,J.A., Ke,Y.Y.,
            Kiraly-Borri,C., Lai,W.M., Lemyre,E., Littlejohn,R.O., Masri,A.,
            Moghtaderi,M., Nakamura,K., Ozaltin,F., Praet,M., Prasad,C.,
            Prytula,A., Roeder,E.R., Rump,P., Schnur,R.E., Shiihara,T.,
            Sinha,M.D., Soliman,N.A., Soulami,K., Sweetser,D.A., Tsai,W.H.,
            Tsai,J.D., Topaloglu,R., Vester,U., Viskochil,D.H.,
            Vatanavicharn,N., Waxler,J.L., Wierenga,K.J., Wolf,M.T.F.,
            Wong,S.N., Leidel,S.A., Truglio,G., Dedon,P.C., Poduri,A., Mane,S.,
            Lifton,R.P., Bouchard,M., Kannu,P., Chitayat,D., Magen,D.,
            Callewaert,B., van Tilbeurgh,H., Zenker,M., Antignac,C. and
            Hildebrandt,F.
  TITLE     Mutations in KEOPS-complex genes cause nephrotic syndrome with
            primary microcephaly
  JOURNAL   Nat Genet 49 (10), 1529-1538 (2017)
   PUBMED   28805828
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Quina,L.A., Wang,S., Ng,L. and Turner,E.E.
  TITLE     Brn3a and Nurr1 mediate a gene regulatory pathway for habenula
            development
  JOURNAL   J Neurosci 29 (45), 14309-14322 (2009)
   PUBMED   19906978
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Daigo,Y., Takayama,I., Ward,S.M., Sanders,K.M. and Fujino,M.A.
  TITLE     Isolation of novel mouse genes that were differentially expressed
            in W/W(V) mouse fundus
  JOURNAL   J Gastroenterol 39 (3), 238-241 (2004)
   PUBMED   15065000
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Miyoshi,A., Kito,K., Aramoto,T., Abe,Y., Kobayashi,N. and Ueda,N.
  TITLE     Identification of CGI-121, a novel PRPK (p53-related protein
            kinase)-binding protein
  JOURNAL   Biochem Biophys Res Commun 303 (2), 399-405 (2003)
   PUBMED   12659830
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC161888.5 and AC158679.8.
            
            On Apr 6, 2018 this sequence version replaced XP_006506631.1.
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longer isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.188143.1,
                                           ERR3363660.1922170.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384, SAMN00849385
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 37.53 cM"
     Protein         1..175
                     /product="EKC/KEOPS complex subunit Tprkb isoform a"
                     /note="TP53RK-binding protein; Prpk (p53-related protein
                     kinase)-binding protein; EKC/KEOPS complex subunit Tprkb;
                     PRPK-binding protein"
                     /calculated_mol_wt=19425
     Region          20..173
                     /region_name="CGI-121"
                     /note="Kinase binding protein CGI-121; pfam08617"
                     /db_xref="CDD:462537"
     CDS             1..175
                     /gene="Tprkb"
                     /gene_synonym="0610033G21Rik; 1810034M08Rik; Cgi-121;
                     DRWMS1; mDRWMS1"
                     /coded_by="NM_001362064.1:539..1066"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS20305.1"
                     /db_xref="GeneID:69786"
                     /db_xref="MGI:MGI:1917036"
ORIGIN      
        1 mqlsqqldlf pecrvtlllf kdvknagdlr kkamegsidg slinpnvivd pfqilvaank
       61 avhlhrlgkm ktrtlsteii fnlspnnnis ealkkfgise tntsvlivyi edgskqvpqe
      121 hlvsqvegqq vpleslpeit rlsevkkiyk lssqeerigt lldaiicrms tkdvl
//
LOCUS       NP_036519                663 aa            linear   PRI 27-APR-2025
DEFINITION  protein-arginine deiminase type-4 [Homo sapiens].
ACCESSION   NP_036519
VERSION     NP_036519.2
DBSOURCE    REFSEQ: accession NM_012387.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Araujo-Abad,S., Rizzuti,B., Soto-Conde,L., Vidal,M., Abian,O.,
            Velazquez-Campoy,A., Neira,J.L. and de Juan Romero,C.
  TITLE     Citrullinating enzyme PADI4 and transcriptional repressor RING1B
            bind in cancer cells
  JOURNAL   Int J Biol Macromol 274 (Pt 1), 133163 (2024)
   PUBMED   38878927
  REMARK    GeneRIF: Citrullinating enzyme PADI4 and transcriptional repressor
            RING1B bind in cancer cells.
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Martinod,K., Denorme,F., Meyers,S., Crescente,M., Van Bruggen,S.,
            Stroobants,M., Siegel,P.M., Grandhi,R., Glatz,K. and Witsch,T.
  TITLE     Involvement of peptidylarginine deiminase 4 in eosinophil
            extracellular trap formation and contribution to citrullinated
            histone signal in thrombi
  JOURNAL   J Thromb Haemost 22 (6), 1649-1659 (2024)
   PUBMED   38395360
  REMARK    GeneRIF: Involvement of peptidylarginine deiminase 4 in eosinophil
            extracellular trap formation and contribution to citrullinated
            histone signal in thrombi.
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Bashir,K., Chaudhary,A., Aslam,M., Fatima,I. and Sarwar,R.
  TITLE     Polymorphic Analysis of Genes PADI4 (rs2240340, rs1748033) and
            HLA-DRB1 (rs2395175) in Arthritis Patients in Pakistani Population
  JOURNAL   Biochem Genet 62 (3), 1840-1856 (2024)
   PUBMED   37751115
  REMARK    GeneRIF: Polymorphic Analysis of Genes PADI4 (rs2240340, rs1748033)
            and HLA-DRB1 (rs2395175) in Arthritis Patients in Pakistani
            Population.
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Osei-Amponsa,V., Chandravanshi,M., Lu,X., Magidson,V., Das,S.,
            Andresson,T., Dyba,M., Sabbasani,V.R., Swenson,R.E., Fromont,C.,
            Shrestha,B., Zhao,Y., Clapp,M.E., Chari,R. and Walters,K.J.
  TITLE     hRpn13 shapes the proteome and transcriptome through epigenetic
            factors HDAC8, PADI4, and transcription factor NF-kappaB p50
  JOURNAL   Mol Cell 84 (3), 522-537 (2024)
   PUBMED   38151017
  REMARK    GeneRIF: hRpn13 shapes the proteome and transcriptome through
            epigenetic factors HDAC8, PADI4, and transcription factor NF-kappaB
            p50.
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Nava-Quiroz,K.J., Rojas-Serrano,J., Perez-Rubio,G.,
            Buendia-Roldan,I., Mejia,M., Fernandez-Lopez,J.C.,
            Rodriguez-Henriquez,P., Ayala-Alcantar,N., Ramos-Martinez,E.,
            Lopez-Flores,L.A., Del Angel-Pablo,A.D. and Falfan-Valencia,R.
  TITLE     Molecular Factors in PAD2 (PADI2) and PAD4 (PADI4) Are Associated
            with Interstitial Lung Disease Susceptibility in Rheumatoid
            Arthritis Patients
  JOURNAL   Cells 12 (18), 2235 (2023)
   PUBMED   37759458
  REMARK    GeneRIF: Molecular Factors in PAD2 (PADI2) and PAD4 (PADI4) Are
            Associated with Interstitial Lung Disease Susceptibility in
            Rheumatoid Arthritis Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 663)
  AUTHORS   Barton,A., Bowes,J., Eyre,S., Spreckley,K., Hinks,A., John,S. and
            Worthington,J.
  TITLE     A functional haplotype of the PADI4 gene associated with rheumatoid
            arthritis in a Japanese population is not associated in a United
            Kingdom population
  JOURNAL   Arthritis Rheum 50 (4), 1117-1121 (2004)
   PUBMED   15077293
  REMARK    GeneRIF: A PADI4 susceptibility haplotype associated with RA in a
            Japanese population is not associated with RA in a UK population
            but other genes involved in the citrullinating pathway remain
            strong candidate
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 663)
  AUTHORS   Suzuki,A., Yamada,R., Chang,X., Tokuhiro,S., Sawada,T., Suzuki,M.,
            Nagasaki,M., Nakayama-Hamada,M., Kawaida,R., Ono,M., Ohtsuki,M.,
            Furukawa,H., Yoshino,S., Yukioka,M., Tohma,S., Matsubara,T.,
            Wakitani,S., Teshima,R., Nishioka,Y., Sekine,A., Iida,A.,
            Takahashi,A., Tsunoda,T., Nakamura,Y. and Yamamoto,K.
  TITLE     Functional haplotypes of PADI4, encoding citrullinating enzyme
            peptidylarginine deiminase 4, are associated with rheumatoid
            arthritis
  JOURNAL   Nat Genet 34 (4), 395-402 (2003)
   PUBMED   12833157
  REMARK    GeneRIF: identified a haplotype of PADI4 associated with
            susceptibility to rheumatoid arthritis that affected stability of
            transcripts and was associated with levels of antibody to
            citrullinated peptide in sera from individuals with rheumatoid
            arthritis
REFERENCE   8  (residues 1 to 663)
  AUTHORS   Nakashima,K., Hagiwara,T. and Yamada,M.
  TITLE     Nuclear localization of peptidylarginine deiminase V and histone
            deimination in granulocytes
  JOURNAL   J Biol Chem 277 (51), 49562-49568 (2002)
   PUBMED   12393868
  REMARK    GeneRIF: PAD V is localized in the nucleus in Hela cells
REFERENCE   9  (residues 1 to 663)
  AUTHORS   Asaga,H., Nakashima,K., Senshu,T., Ishigami,A. and Yamada,M.
  TITLE     Immunocytochemical localization of peptidylarginine deiminase in
            human eosinophils and neutrophils
  JOURNAL   J Leukoc Biol 70 (1), 46-51 (2001)
   PUBMED   11435484
REFERENCE   10 (residues 1 to 663)
  AUTHORS   Nakashima,K., Hagiwara,T., Ishigami,A., Nagata,S., Asaga,H.,
            Kuramoto,M., Senshu,T. and Yamada,M.
  TITLE     Molecular characterization of peptidylarginine deiminase in HL-60
            cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3)
  JOURNAL   J Biol Chem 274 (39), 27786-27792 (1999)
   PUBMED   10488123
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314839.1, AB017919.1 and
            AC004824.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 9, 2008 this sequence version replaced NP_036519.1.
            
            Summary: This gene is a member of a gene family which encodes
            enzymes responsible for the conversion of arginine residues to
            citrulline residues. This gene may play a role in granulocyte and
            macrophage development leading to inflammation and immune response.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB017919.1, SRR1803615.231330.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375448.4/ ENSP00000364597.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..663
                     /product="protein-arginine deiminase type-4"
                     /EC_number="3.5.3.15"
                     /note="peptidyl arginine deiminase, type V; HL-60 PAD;
                     PADI-H protein; protein-arginine deiminase type IV;
                     peptidyl arginine deiminase, type IV"
                     /calculated_mol_wt=73948
     Region          7..112
                     /region_name="PAD_N"
                     /note="N-terminal non-catalytic domain of protein-arginine
                     deiminase; cd04214"
                     /db_xref="CDD:259876"
     Region          113..273
                     /region_name="PAD_M"
                     /note="Protein-arginine deiminase (PAD) middle domain;
                     pfam08527"
                     /db_xref="CDD:462510"
     Region          283..660
                     /region_name="PAD"
                     /note="Protein-arginine deiminase (PAD); pfam03068"
                     /db_xref="CDD:460794"
     CDS             1..663
                     /gene="PADI4"
                     /gene_synonym="PAD; PAD4; PADI5; PDI4; PDI5"
                     /coded_by="NM_012387.3:27..2018"
                     /db_xref="CCDS:CCDS180.1"
                     /db_xref="GeneID:23569"
                     /db_xref="HGNC:HGNC:18368"
                     /db_xref="MIM:605347"
ORIGIN      
        1 maqgtlirvt peqpthavcv lgtltqldic ssapedctsf sinaspgvvv diahgppakk
       61 kstgsstwpl dpgvevtltm kvasgstgdq kvqisyygpk tppvkallyl tgveislcad
      121 itrtgkvkpt ravkdqrtwt wgpcgqgail lvncdrdnle ssamdcedde vldsedlqdm
      181 slmtlstktp kdfftnhtlv lhvarsemdk vrvfqatrgk lsskcsvvlg pkwpshylmv
      241 pggkhnmdfy vealafpdtd fpglitltis lldtsnlelp eavvfqdsvv frvapwimtp
      301 ntqppqevya csifenedfl ksvttlamka kcklticpee enmddqwmqd emeigyiqap
      361 hktlpvvfds prnrglkefp ikrvmgpdfg yvtrgpqtgg isgldsfgnl evsppvtvrg
      421 keyplgrilf gdscypsnds rqmhqalqdf lsaqqvqapv klysdwlsvg hvdeflsfvp
      481 apdrkgfrll lasprscykl fqeqqneghg eallfegikk kkqqkiknil snktlrehns
      541 fvercidwnr ellkrelgla esdiidipql fklkefskae affpnmvnml vlgkhlgipk
      601 pfgpvingrc cleekvcsll eplglqctfi ndfftyhirh gevhcgtnvr rkpfsfkwwn
      661 mvp
//
LOCUS       NP_060204                551 aa            linear   PRI 27-APR-2025
DEFINITION  palmdelphin [Homo sapiens].
ACCESSION   NP_060204
VERSION     NP_060204.1
DBSOURCE    REFSEQ: accession NM_017734.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Su,Y., Du,Y., Ye,S., Jia,G., Ding,B. and Yu,J.
  TITLE     Clinical importance and PI3K/Akt pathway-dependent
            anti-proliferative role of PALMD and DPT in breast cancer
  JOURNAL   Pathol Res Pract 249, 154717 (2023)
   PUBMED   37556876
  REMARK    GeneRIF: Clinical importance and PI3K/Akt pathway-dependent
            anti-proliferative role of PALMD and DPT in breast cancer.
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Wang,S., Yu,H., Gao,J., Chen,J., He,P., Zhong,H., Tan,X.,
            Staines,K.A., Macrae,V.E., Fu,X., Jiang,L. and Zhu,D.
  TITLE     PALMD regulates aortic valve calcification via altered glycolysis
            and NF-kappaB-mediated inflammation
  JOURNAL   J Biol Chem 298 (5), 101887 (2022)
   PUBMED   35367413
  REMARK    GeneRIF: PALMD regulates aortic valve calcification via altered
            glycolysis and NF-kappaB-mediated inflammation.
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Sainz-Jaspeado,M., Smith,R.O., Plunde,O., Pawelzik,S.C., Jin,Y.,
            Nordling,S., Ding,Y., Aspenstrom,P., Hedlund,M., Bastianello,G.,
            Ascione,F., Li,Q., Demir,C.S., Fernando,D., Daniel,G.,
            Franco-Cereceda,A., Kroon,J., Foiani,M., Petrova,T.V.,
            Kilimann,M.W., Back,M. and Claesson-Welsh,L.
  TITLE     Palmdelphin Regulates Nuclear Resilience to Mechanical Stress in
            the Endothelium
  JOURNAL   Circulation 144 (20), 1629-1645 (2021)
   PUBMED   34636652
  REMARK    GeneRIF: Palmdelphin Regulates Nuclear Resilience to Mechanical
            Stress in the Endothelium.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Li,Z., Gaudreault,N., Arsenault,B.J., Mathieu,P., Bosse,Y. and
            Theriault,S.
  TITLE     Phenome-wide analyses establish a specific association between
            aortic valve PALMD expression and calcific aortic valve stenosis
  JOURNAL   Commun Biol 3 (1), 477 (2020)
   PUBMED   32859967
  REMARK    GeneRIF: Phenome-wide analyses establish a specific association
            between aortic valve PALMD expression and calcific aortic valve
            stenosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Dashzeveg,N., Taira,N., Lu,Z.G., Kimura,J. and Yoshida,K.
  TITLE     Palmdelphin, a novel target of p53 with Ser46 phosphorylation,
            controls cell death in response to DNA damage
  JOURNAL   Cell Death Dis 5 (5), e1221 (2014)
   PUBMED   24810057
  REMARK    GeneRIF: findings define palmdelphin as a target of
            serine-46-phosphorylated p53 that controls cell death in response
            to DNA damage.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Vasan,R.S., Glazer,N.L., Felix,J.F., Lieb,W., Wild,P.S.,
            Felix,S.B., Watzinger,N., Larson,M.G., Smith,N.L., Dehghan,A.,
            Grosshennig,A., Schillert,A., Teumer,A., Schmidt,R., Kathiresan,S.,
            Lumley,T., Aulchenko,Y.S., Konig,I.R., Zeller,T., Homuth,G.,
            Struchalin,M., Aragam,J., Bis,J.C., Rivadeneira,F., Erdmann,J.,
            Schnabel,R.B., Dorr,M., Zweiker,R., Lind,L., Rodeheffer,R.J.,
            Greiser,K.H., Levy,D., Haritunians,T., Deckers,J.W., Stritzke,J.,
            Lackner,K.J., Volker,U., Ingelsson,E., Kullo,I., Haerting,J.,
            O'Donnell,C.J., Heckbert,S.R., Stricker,B.H., Ziegler,A.,
            Reffelmann,T., Redfield,M.M., Werdan,K., Mitchell,G.F., Rice,K.,
            Arnett,D.K., Hofman,A., Gottdiener,J.S., Uitterlinden,A.G.,
            Meitinger,T., Blettner,M., Friedrich,N., Wang,T.J., Psaty,B.M., van
            Duijn,C.M., Wichmann,H.E., Munzel,T.F., Kroemer,H.K.,
            Benjamin,E.J., Rotter,J.I., Witteman,J.C., Schunkert,H.,
            Schmidt,H., Volzke,H. and Blankenberg,S.
  TITLE     Genetic variants associated with cardiac structure and function: a
            meta-analysis and replication of genome-wide association data
  JOURNAL   JAMA 302 (2), 168-178 (2009)
   PUBMED   19584346
  REMARK    GeneRIF: Meta-analysis and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Andreu,N., Escarceller,M., Feather,S., Devriendt,K., Wolf,A.S.,
            Estivill,X. and Sumoy,L.
  TITLE     PALML, a novel paralemmin-related gene mapping on human chromosome
            1p21
  JOURNAL   Gene 278 (1-2), 33-40 (2001)
   PUBMED   11707320
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Hu,B., Copeland,N.G., Gilbert,D.J., Jenkins,N.A. and Kilimann,M.W.
  TITLE     The paralemmin protein family: identification of paralemmin-2, an
            isoform differentially spliced to AKAP2/AKAP-KL, and of
            palmdelphin, a more distant cytosolic relative
  JOURNAL   Biochem Biophys Res Commun 285 (5), 1369-1376 (2001)
   PUBMED   11478809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF262379.1 and AL390970.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000278.1, AF262379.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263174.9/ ENSP00000263174.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.2"
     Protein         1..551
                     /product="palmdelphin"
                     /note="paralemnin-like protein; paralemmin-like protein"
                     /calculated_mol_wt=62627
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Region          17..447
                     /region_name="MYO6_MIU_linker"
                     /note="MIU-linker domain found in unconventional
                     myosin-VI; cl46503"
                     /db_xref="CDD:480843"
     Region          78..>204
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Region          248..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHU2; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Region          342..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHU2; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHU2; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Region          449..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     CDS             1..551
                     /gene="PALMD"
                     /gene_synonym="C1orf11; PALML"
                     /coded_by="NM_017734.5:206..1861"
                     /db_xref="CCDS:CCDS758.1"
                     /db_xref="GeneID:54873"
                     /db_xref="HGNC:HGNC:15846"
                     /db_xref="MIM:610182"
ORIGIN      
        1 meeaelvkgr lqaitdkrki qeeisqkrlk ieedklkhqh lkkkalrekw lldgissgke
       61 qeemkkqnqq dqhqiqvleq silrlekeiq dlekaelqis tkeeailkkl ksierttedi
      121 irsvkveree raeesiediy anipdlpksy ipsrlrkein eekeddeqnr kalyameikv
      181 ekdlktgest vlssiplpsd dfkgtgikvy ddgqksvyav ssnhsaayng tdglapveve
      241 ellrqasern skspteyhep vyanpfyrpt tpqretvtpg pnfqerikik tnglgigvne
      301 sihnmgngls eergnnfnhi spippvphpr sviqqaeekl htpqkrlmtp weesnvmqdk
      361 dapspkprls pretifgkse hqnssptcqe deedvryniv hslppdindt epvtmifmgy
      421 qqaedseedk kfltgydgii haelvvidde eeedegeaek psyhpiaphs qvyqpakptp
      481 lprkrseasp hentnhksph knsislkeqe eslgspvhhs pfdaqttgdg tedpsltalr
      541 mrmaklgkkv i
//
LOCUS       NP_149985                549 aa            linear   PRI 27-APR-2025
DEFINITION  tigger transposable element-derived protein 7 [Homo sapiens].
ACCESSION   NP_149985
VERSION     NP_149985.2
DBSOURCE    REFSEQ: accession NM_033208.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Dou,T., Gu,S., Zhou,Z., Ji,C., Zeng,L., Ye,X., Xu,J., Ying,K.,
            Xie,Y. and Mao,Y.
  TITLE     Isolation and characterization of a Jerky and JRK/JH8 like gene,
            tigger transposable element derived 7, TIGD7
  JOURNAL   Biochem Genet 42 (7-8), 279-285 (2004)
   PUBMED   15487591
  REMARK    GeneRIF: TIGD7 is a Jerky and JRK/JH8 like gene
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Hugh Robertson. The reference sequence was
            derived from DC351858.1, BX463753.2, AC004232.1, AK308054.1 and
            AI925903.1.
            
            On Aug 20, 2002 this sequence version replaced NP_149985.1.
            
            Summary: The protein encoded by this gene belongs to the tigger
            subfamily of the pogo superfamily of DNA-mediated transposons in
            humans. These proteins are related to DNA transposons found in
            fungi and nematodes, and more distantly to the Tc1 and mariner
            transposases. They are also very similar to the major mammalian
            centromere protein B. The exact function of this gene is not known.
            [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.218593.1,
                                           SRR1660803.245381.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146411, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396862.2/ ENSP00000380071.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..549
                     /product="tigger transposable element-derived protein 7"
                     /calculated_mol_wt=63106
     Region          4..55
                     /region_name="CENP-B_N"
                     /note="CENP-B N-terminal DNA-binding domain; pfam04218"
                     /db_xref="CDD:461229"
     Region          77..135
                     /region_name="HTH_Tnp_Tc5"
                     /note="Tc5 transposase DNA-binding domain; pfam03221"
                     /db_xref="CDD:460850"
     Region          207..399
                     /region_name="DDE_3"
                     /note="DDE superfamily endonuclease; cl46863"
                     /db_xref="CDD:481203"
     Region          527..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT04.1)"
     CDS             1..549
                     /gene="TIGD7"
                     /gene_synonym="Sancho"
                     /coded_by="NM_033208.4:1615..3264"
                     /db_xref="CCDS:CCDS10500.1"
                     /db_xref="GeneID:91151"
                     /db_xref="HGNC:HGNC:18331"
                     /db_xref="MIM:612969"
ORIGIN      
        1 mnkrgkyttl nleekmkvls rieagrslks vmdefgisks tfydikknkk lildfvlkqd
       61 mplvgaekrk rttgakygdv ddavymwyqq krsagvpvrg velqaaaerf arcfgrtdfk
      121 astgwlfrfr nrhaignrkg cgeqvlssvs envepfrqkl smiikeeklc laqlysgdet
      181 dlfwksmpen sqasrkdicl pgkkinkerl saflcanadg thklksiiig ksklpksvke
      241 dtstlpviyk pskdvwftre lfsewffqnf vpevrhfqln vlrfhdedvr alllldscpa
      301 hpssesltse dgrikcmffp hntstliqpm nqgvilsckr lyrwkqlees lvifeesdde
      361 qekgdkgvsk ikiyniksai fnwaksweev kqitianawe nllykkepey dfqglehgdy
      421 reilekcgel etkldddrvw lngdeekgcl lktkggitke vvqkggeaek qtaefklsav
      481 resldylldf vdatpefqrf hftlkemqqe ivkkqfqski hsrigsflkp rphnikdsfs
      541 gpstsgsnh
//
LOCUS       NP_115575               1188 aa            linear   PRI 27-APR-2025
DEFINITION  AT-rich interactive domain-containing protein 5B isoform 1 [Homo
            sapiens].
ACCESSION   NP_115575 XP_084482
VERSION     NP_115575.1
DBSOURCE    REFSEQ: accession NM_032199.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1188)
  AUTHORS   Ragnarsson,C., Yang,M., Moura-Castro,L.H., Aydin,E., Gunnarsson,R.,
            Olsson-Arvidsson,L., Lilljebjorn,H., Fioretos,T., Duployez,N.,
            Zaliova,M., Zuna,J., Castor,A., Johansson,B. and Paulsson,K.
  TITLE     Constitutional and acquired genetic variants in ARID5B in pediatric
            B-cell precursor acute lymphoblastic leukemia
  JOURNAL   Genes Chromosomes Cancer 63 (5), e23242 (2024)
   PUBMED   38738968
  REMARK    GeneRIF: Constitutional and acquired genetic variants in ARID5B in
            pediatric B-cell precursor acute lymphoblastic leukemia.
REFERENCE   2  (residues 1 to 1188)
  AUTHORS   Tan,Y., Qiao,J., Yang,S., Wang,Q., Liu,H., Liu,Q., Feng,W.,
            Yang,B., Li,Z. and Cui,L.
  TITLE     ARID5B-mediated LINC01128 epigenetically activated pyroptosis and
            apoptosis by promoting the formation of the BTF3/STAT3 complex in
            beta2GPI/anti-beta2GPI-treated monocytes
  JOURNAL   Clin Transl Med 14 (1), e1539 (2024)
   PUBMED   38224186
  REMARK    GeneRIF: ARID5B-mediated LINC01128 epigenetically activated
            pyroptosis and apoptosis by promoting the formation of the
            BTF3/STAT3 complex in beta2GPI/anti-beta2GPI-treated monocytes.
REFERENCE   3  (residues 1 to 1188)
  AUTHORS   Al-Zayan,N.R., Ashour,M.J., Abuwarda,H.N. and Sharif,F.A.
  TITLE     ARID5B, IKZF1, GATA3, CEBPE, and CDKN2A germline polymorphisms and
            predisposition to childhood acute lymphoblastic leukemia
  JOURNAL   Pediatr Hematol Oncol 41 (2), 103-113 (2024)
   PUBMED   37578068
  REMARK    GeneRIF: ARID5B, IKZF1, GATA3, CEBPE, and CDKN2A germline
            polymorphisms and predisposition to childhood acute lymphoblastic
            leukemia.
REFERENCE   4  (residues 1 to 1188)
  AUTHORS   Deng,Y., Dong,Y., Wu,L., Zhang,Q. and Yang,L.
  TITLE     ARID5B promoted the histone demethylation of SORBS2 and hampered
            the metastasis of ovarian cancer
  JOURNAL   Pathol Res Pract 252, 154911 (2023)
   PUBMED   37948999
  REMARK    GeneRIF: ARID5B promoted the histone demethylation of SORBS2 and
            hampered the metastasis of ovarian cancer.
REFERENCE   5  (residues 1 to 1188)
  AUTHORS   Healy,J., Richer,C., Bourgey,M., Kritikou,E.A. and Sinnett,D.
  TITLE     Replication analysis confirms the association of ARID5B with
            childhood B-cell acute lymphoblastic leukemia
  JOURNAL   Haematologica 95 (9), 1608-1611 (2010)
   PUBMED   20460642
  REMARK    GeneRIF: confirmed the association of 5 SNPs [rs7073837 (P=4.2 x
            10(-4)), rs10994982 (P=3.8 x 10(-4)), rs10740055 (P=1.6 x 10(-5)),
            rs10821936 (P=1.7 x 10(-7)) and rs7089424 (P=3.6 x 10(-7))] in the
            ARID5B gene with childhood acute lymphoblastic leukemia
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 1188)
  AUTHORS   Wilsker,D., Patsialou,A., Dallas,P.B. and Moran,E.
  TITLE     ARID proteins: a diverse family of DNA binding proteins implicated
            in the control of cell growth, differentiation, and development
  JOURNAL   Cell Growth Differ 13 (3), 95-106 (2002)
   PUBMED   11959810
  REMARK    Review article
REFERENCE   7  (residues 1 to 1188)
  AUTHORS   Zhu,L., Hu,J., Lin,D., Whitson,R., Itakura,K. and Chen,Y.
  TITLE     Dynamics of the Mrf-2 DNA-binding domain free and in complex with
            DNA
  JOURNAL   Biochemistry 40 (31), 9142-9150 (2001)
   PUBMED   11478881
  REMARK    GeneRIF: NMR spectroscopy studies of Mrf-2 in complex with DNA
            suggest that two flexible interhelical loops, the flexible
            C-terminal tail, and one alpha-helix are involved in DNA
            recognition, indicating the importance of protein dynamics in DNA
            binding.
REFERENCE   8  (residues 1 to 1188)
  AUTHORS   Whitson,R.H., Huang,T. and Itakura,K.
  TITLE     The novel Mrf-2 DNA-binding domain recognizes a five-base core
            sequence through major and minor-groove contacts
  JOURNAL   Biochem Biophys Res Commun 258 (2), 326-331 (1999)
   PUBMED   10329386
REFERENCE   9  (residues 1 to 1188)
  AUTHORS   Yuan,Y.C., Whitson,R.H., Liu,Q., Itakura,K. and Chen,Y.
  TITLE     A novel DNA-binding motif shares structural homology to DNA
            replication and repair nucleases and polymerases
  JOURNAL   Nat Struct Biol 5 (11), 959-964 (1998)
   PUBMED   9808040
REFERENCE   10 (residues 1 to 1188)
  AUTHORS   Huang,T.H., Oka,T., Asai,T., Okada,T., Merrills,B.W., Gertson,P.N.,
            Whitson,R.H. and Itakura,K.
  TITLE     Repression by a differentiation-specific factor of the human
            cytomegalovirus enhancer
  JOURNAL   Nucleic Acids Res 24 (9), 1695-1701 (1996)
   PUBMED   8649988
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB014195.1, BC056680.1,
            M73837.1 and AL671972.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 4, 2005 this sequence version replaced XP_084482.3.
            
            Summary: This gene encodes a member of the AT-rich interaction
            domain (ARID) family of DNA binding proteins. The encoded protein
            forms a histone H3K9Me2 demethylase complex with PHD finger protein
            2 and regulates the transcription of target genes involved in
            adipogenesis and liver development. This gene also plays a role in
            cell growth and differentiation of B-lymphocyte progenitors, and
            single nucleotide polymorphisms in this gene are associated with
            acute lymphoblastic leukemia. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000279873.12/ ENSP00000279873.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.2"
     Protein         1..1188
                     /product="AT-rich interactive domain-containing protein 5B
                     isoform 1"
                     /note="modulator recognition factor 2 (MRF2); MRF1-like
                     protein; ARID domain-containing protein 5B; AT-rich
                     interactive domain 5B (MRF1-like)"
                     /calculated_mol_wt=132244
     Region          251..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14865.3)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14865.3)"
     Region          320..414
                     /region_name="ARID_ARID5B"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 5B (ARID5B) and
                     similar proteins; cd16885"
                     /db_xref="CDD:350649"
     Site            336
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0000269|PubMed:21532585; propagated from
                     UniProtKB/Swiss-Prot (Q14865.3)"
     Site            order(341..347,372,374..375,378,389,391..393,395)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350649"
     Region          <410..>536
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          412..611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14865.3)"
     Region          846..874
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14865.3)"
     Region          891..918
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14865.3)"
     Region          956..978
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14865.3)"
     Region          1028..1070
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14865.3)"
     Site            1032
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14865.3)"
     Site            1133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14865.3)"
     CDS             1..1188
                     /gene="ARID5B"
                     /gene_synonym="DESRT; MRF-2; MRF2"
                     /coded_by="NM_032199.3:12..3578"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31208.1"
                     /db_xref="GeneID:84159"
                     /db_xref="HGNC:HGNC:17362"
                     /db_xref="MIM:608538"
ORIGIN      
        1 mepnslqwvg spcglhgpyi fykafqfhle gkprilslgd fffvrctpkd piciaelqll
       61 weertsrqll sssklyflpe dtpqgrnsdh gedeviavse kvivkledlv kwvhsdfskw
      121 rcgfhagpvk tealgrngqk eallkyrqst lnsglnfkdv lkekadlged eeetnvivls
      181 ypqycryrsm lkriqdkpss iltdqfalal ggiavvsrnp qilycrdtfd hptlienesi
      241 cdefapnlkg rprkkkpcpq rrdsfsgvkd snnnsdgkav akvkcearsa ltkpknnhnc
      301 kkvsneekpk vaigeecrad eqaflvalyk ymkerktpie ripylgfkqi nlwtmfqaaq
      361 klggyetita rrqwkhiyde lggnpgstsa atctrrhyer lilpyerfik geedkplppi
      421 kprkqenssq enenktkvsg tkrikheipk skkekenapk pqdaaevsse qekeqetlis
      481 qksipeplpa admkkkiegy qefsakplas rvdpekdnet dqgsnsekva eeagekgptp
      541 plpsaplape kdsalvpgas kqpltspsal vdskqesklc cftespesep qeasfpsfpt
      601 tqpplanqne teddklpama dyianctvkv dqlgsddihn alkqtpkvlv vqsfdmfkdk
      661 dltgpmnenh glnytpllys rgnpgimspl akkkllsqvs gaslsssypy gspppliskk
      721 kliarddlcs slsqthhgqs tdhmavsrps viqhvqsfrs kpseerktin difkheklsr
      781 sdphrcsfsk hhlnpladsy vlkqeiqegk dkllekralp hshmpsflad fyssphlhsl
      841 yrhtehhlhn eqtskypsrd myresenssf pshrhqeklh vnyltslhlq dkksaaaeap
      901 tddqptdlsl pknphkptgk vlglahsttg pqeskgisqf qvlgsqsrdc hpkacrvspm
      961 tmsgpkkype slsrsgkphh vrlenfrkme gmvhpilhrk mspqnigaar pikrsledld
     1021 lviagkkara vspldpskev sgkekaseqe segskaahgg hsgggseghk lplsspifpg
     1081 lysgslcnsg lnsrlpagys hslqylknqt vlsplmqpla fhslvmqrgi ftsptnsqql
     1141 yrhlaaatpv gssygdllhn siyplaainp qaafpssqls svhpstkl
//
LOCUS       NP_000576                162 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-15 isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_000576
VERSION     NP_000576.1
DBSOURCE    REFSEQ: accession NM_000585.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Jiang,J., Yang,M., Yang,B., Wu,H. and Lu,Q.
  TITLE     Elevated IL-15 levels in systemic lupus erythematosus: potential
            pathogenesis insight and therapeutic target
  JOURNAL   Int Immunopharmacol 142 (Pt A), 112973 (2024)
   PUBMED   39217881
  REMARK    GeneRIF: Elevated IL-15 levels in systemic lupus erythematosus:
            potential pathogenesis insight and therapeutic target.
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Holmberg,C.S., Levinger,C., Abongwa,M., Ceriani,C., Archin,N.M.,
            Siegel,M., Ghosh,M. and Bosque,A.
  TITLE     HIV-1 latency reversal and immune enhancing activity of IL-15 is
            not influenced by sex hormones
  JOURNAL   JCI Insight 9 (17), e180609 (2024)
   PUBMED   39078714
  REMARK    GeneRIF: HIV-1 latency reversal and immune enhancing activity of
            IL-15 is not influenced by sex hormones.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Mohammed,S.I., Hassan,K.M., Azeez,D.M., Qadir,F.A. and Salihi,A.B.
  TITLE     IL-15 gene mutation as a molecular risk factor in acute lymphoid
            leukemia
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 10-17 (2024)
   PUBMED   38814240
  REMARK    GeneRIF: IL-15 gene mutation as a molecular risk factor in acute
            lymphoid leukemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 162)
  AUTHORS   Suzuki,T., Cheret,J., Scala,F.D., Rajabi-Estarabadi,A.,
            Akhundlu,A., Demetrius,D.L., Gherardini,J., Keren,A., Harries,M.,
            Rodriguez-Feliz,J., Epstein,G., Lee,W., Purba,T., Gilhar,A. and
            Paus,R.
  TITLE     Interleukin-15 is a hair follicle immune privilege guardian
  JOURNAL   J Autoimmun 145, 103217 (2024)
   PUBMED   38581915
  REMARK    GeneRIF: Interleukin-15 is a hair follicle immune privilege
            guardian.
REFERENCE   5  (residues 1 to 162)
  AUTHORS   Zekri,L., Hagelstein,I., Marklin,M., Klimovich,B., Christie,M.,
            Lindner,C., Kamereit,S., Prakash,N., Muller,S., Stotz,S.,
            Maurer,A., Greve,C., Schmied,B., Atar,D., Rammensee,H.G., Jung,G.
            and Salih,H.R.
  TITLE     Immunocytokines with target cell-restricted IL-15 activity for
            treatment of B cell malignancies
  JOURNAL   Sci Transl Med 16 (737), eadh1988 (2024)
   PUBMED   38446900
  REMARK    GeneRIF: Immunocytokines with target cell-restricted IL-15 activity
            for treatment of B cell malignancies.
REFERENCE   6  (residues 1 to 162)
  AUTHORS   Johnston,J.A., Bacon,C.M., Finbloom,D.S., Rees,R.C., Kaplan,D.,
            Shibuya,K., Ortaldo,J.R., Gupta,S., Chen,Y.Q., Giri,J.D. et al.
  TITLE     Tyrosine phosphorylation and activation of STAT5, STAT3, and Janus
            kinases by interleukins 2 and 15
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8705-8709 (1995)
   PUBMED   7568001
REFERENCE   7  (residues 1 to 162)
  AUTHORS   Giri,J.G., Kumaki,S., Ahdieh,M., Friend,D.J., Loomis,A.,
            Shanebeck,K., DuBose,R., Cosman,D., Park,L.S. and Anderson,D.M.
  TITLE     Identification and cloning of a novel IL-15 binding protein that is
            structurally related to the alpha chain of the IL-2 receptor
  JOURNAL   EMBO J 14 (15), 3654-3663 (1995)
   PUBMED   7641685
REFERENCE   8  (residues 1 to 162)
  AUTHORS   Anderson,D.M., Johnson,L., Glaccum,M.B., Copeland,N.G.,
            Gilbert,D.J., Jenkins,N.A., Valentine,V., Kirstein,M.N.,
            Shapiro,D.N., Morris,S.W. et al.
  TITLE     Chromosomal assignment and genomic structure of Il15
  JOURNAL   Genomics 25 (3), 701-706 (1995)
   PUBMED   7759105
REFERENCE   9  (residues 1 to 162)
  AUTHORS   Giri,J.G., Ahdieh,M., Eisenman,J., Shanebeck,K., Grabstein,K.,
            Kumaki,S., Namen,A., Park,L.S., Cosman,D. and Anderson,D.
  TITLE     Utilization of the beta and gamma chains of the IL-2 receptor by
            the novel cytokine IL-15
  JOURNAL   EMBO J 13 (12), 2822-2830 (1994)
   PUBMED   8026467
REFERENCE   10 (residues 1 to 162)
  AUTHORS   Grabstein,K.H., Eisenman,J., Shanebeck,K., Rauch,C., Srinivasan,S.,
            Fung,V., Beers,C., Richardson,J., Schoenborn,M.A., Ahdieh,M. et al.
  TITLE     Cloning of a T cell growth factor that interacts with the beta
            chain of the interleukin-2 receptor
  JOURNAL   Science 264 (5161), 965-968 (1994)
   PUBMED   8178155
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC118480.3, CX761071.1,
            AC096774.1, BX116580.1 and AA897685.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a cytokine that
            regulates T and natural killer cell activation and proliferation.
            This cytokine and interleukine 2 share many biological activities.
            They are found to bind common hematopoietin receptor subunits, and
            may compete for the same receptor, and thus negatively regulate
            each other's activity. The number of CD8+ memory cells is shown to
            be controlled by a balance between this cytokine and IL2. This
            cytokine induces the activation of JAK kinases, as well as the
            phosphorylation and activation of transcription activators STAT3,
            STAT5, and STAT6. Studies of the mouse counterpart suggested that
            this cytokine may increase the expression of apoptosis inhibitor
            BCL2L1/BCL-x(L), possibly through the transcription activation
            activity of STAT6, and thus prevent apoptosis. Alternatively
            spliced transcript variants of this gene have been reported.
            [provided by RefSeq, Feb 2011].
            
            Transcript Variant: This variant (3) represents the shortest
            transcript and encodes the longer isoform (1, also known as
            48aa(LSP)-IL15).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.392131.1,
                                           SRR1163655.677066.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000320650.9/ ENSP00000323505.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.21"
     Protein         1..162
                     /product="interleukin-15 isoform 1 preproprotein"
                     /calculated_mol_wt=14716
     sig_peptide     1..29
                     /calculated_mol_wt=3388
     proprotein      30..162
                     /product="interleukin-15 isoform 1 proprotein"
                     /calculated_mol_wt=14716
     Region          33..154
                     /region_name="IL15"
                     /note="Interleukin 15; pfam02372"
                     /db_xref="CDD:308146"
     mat_peptide     49..162
                     /product="interleukin-15 isoform 1"
                     /calculated_mol_wt=12774
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40933.1)"
     CDS             1..162
                     /gene="IL15"
                     /gene_synonym="IL-15"
                     /coded_by="NM_000585.5:388..876"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS3755.1"
                     /db_xref="GeneID:3600"
                     /db_xref="HGNC:HGNC:5977"
                     /db_xref="MIM:600554"
ORIGIN      
        1 mriskphlrs isiqcylcll lnshflteag ihvfilgcfs aglpkteanw vnvisdlkki
       61 edliqsmhid atlytesdvh psckvtamkc fllelqvisl esgdasihdt venliilann
      121 slssngnvte sgckeceele eknikeflqs fvhivqmfin ts
//
LOCUS       NP_004079                509 aa            linear   PRI 27-APR-2025
DEFINITION  DNA nucleotidylexotransferase isoform 1 [Homo sapiens].
ACCESSION   NP_004079
VERSION     NP_004079.3
DBSOURCE    REFSEQ: accession NM_004088.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ukladov,E.O., Tyugashev,T.E. and Kuznetsov,N.A.
  TITLE     Computational Modeling Study of the Molecular Basis of dNTP
            Selectivity in Human Terminal Deoxynucleotidyltransferase
  JOURNAL   Biomolecules 14 (8), 961 (2024)
   PUBMED   39199349
  REMARK    GeneRIF: Computational Modeling Study of the Molecular Basis of
            dNTP Selectivity in Human Terminal Deoxynucleotidyltransferase.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Kim,Y., Calderon,A.A., Favaro,P., Glass,D.R., Tsai,A.G., Ho,D.,
            Borges,L., Greenleaf,W.J. and Bendall,S.C.
  TITLE     Terminal deoxynucleotidyl transferase and CD84 identify human
            multi-potent lymphoid progenitors
  JOURNAL   Nat Commun 15 (1), 5910 (2024)
   PUBMED   39003273
  REMARK    GeneRIF: Terminal deoxynucleotidyl transferase and CD84 identify
            human multi-potent lymphoid progenitors.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Yu,C.H., Su,Y.H., Jou,S.T., Lu,M.Y., Lin,C.Y., Lin,K.H.,
            Chang,H.H., Chou,S.W., Huang,Y.H., Lin,D.T., Lin,S.W., Chen,H.Y.,
            Chang,Y.H. and Yang,Y.L.
  TITLE     Terminal deoxynucleotidyl transferase expression in different
            subtypes of childhood B-cell acute lymphoblastic leukemia
  JOURNAL   Pathol Res Pract 256, 155287 (2024)
   PUBMED   38579576
  REMARK    GeneRIF: Terminal deoxynucleotidyl transferase expression in
            different subtypes of childhood B-cell acute lymphoblastic
            leukemia.
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Yan,B., Fan,H., Ji,H., Li,S., Hu,H., Gu,X., Jia,S., Liu,Y., Guo,J.,
            Yang,Z., Zhou,L., Xiao,X., Li,L. and Mao,Z.
  TITLE     DNA strand displacement and TdT-Mediated DNA extension for swift,
            convenient, and quantitative evaluation of sperm DNA integrity and
            its clinical implications
  JOURNAL   Anal Chim Acta 1280, 341821 (2023)
   PUBMED   37858544
  REMARK    GeneRIF: DNA strand displacement and TdT-Mediated DNA extension for
            swift, convenient, and quantitative evaluation of sperm DNA
            integrity and its clinical implications.
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Koiwai,O. and Morita,A.
  TITLE     Isolation of putative promoter region for human terminal
            deoxynucleotidyltransferase gene
  JOURNAL   Biochem Biophys Res Commun 154 (1), 91-100 (1988)
   PUBMED   3395350
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Riley,L.K., Morrow,J.K., Danton,M.J. and Coleman,M.S.
  TITLE     Human terminal deoxyribonucleotidyltransferase: molecular cloning
            and structural analysis of the gene and 5' flanking region
  JOURNAL   Proc Natl Acad Sci U S A 85 (8), 2489-2493 (1988)
   PUBMED   2833741
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1988 Nov;85(21):7987]
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Koiwai,O., Kaneda,T. and Morishita,R.
  TITLE     Analysis of human terminal deoxynucleotidyl transferase cDNA
            expressible in mammalian cells
  JOURNAL   Biochem Biophys Res Commun 144 (1), 185-190 (1987)
   PUBMED   3579900
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Chang,L.M. and Bollum,F.J.
  TITLE     Molecular biology of terminal transferase
  JOURNAL   CRC Crit Rev Biochem 21 (1), 27-52 (1986)
   PUBMED   3524991
  REMARK    Review article
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Yang-Feng,T.L., Landau,N.R., Baltimore,D. and Francke,U.
  TITLE     The terminal deoxynucleotidyltransferase gene is located on human
            chromosome 10 (10q23----q24) and on mouse chromosome 19
  JOURNAL   Cytogenet Cell Genet 43 (3-4), 121-126 (1986)
   PUBMED   3467897
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Peterson,R.C., Cheung,L.C., Mattaliano,R.J., White,S.T., Chang,L.M.
            and Bollum,F.J.
  TITLE     Expression of human terminal deoxynucleotidyl transferase in
            Escherichia coli
  JOURNAL   J Biol Chem 260 (19), 10495-10502 (1985)
   PUBMED   2863268
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB110609.1, BC012920.1 and
            AL136181.13.
            
            On May 5, 2005 this sequence version replaced NP_004079.2.
            
            Summary: This gene is a member of the DNA polymerase type-X family
            and encodes a template-independent DNA polymerase that catalyzes
            the addition of deoxynucleotides to the 3'-hydroxyl terminus of
            oligonucleotide primers. In vivo, the encoded protein is expressed
            in a restricted population of normal and malignant pre-B and pre-T
            lymphocytes during early differentiation, where it generates
            antigen receptor diversity by synthesizing non-germ line elements
            (N-regions) at the junctions of rearranged Ig heavy chain and T
            cell receptor gene segments. Alternatively spliced transcript
            variants encoding different isoforms of this gene have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279858.4606.1, AB046378.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2152719
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371174.5/ ENSP00000360216.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.1"
     Protein         1..509
                     /product="DNA nucleotidylexotransferase isoform 1"
                     /EC_number="2.7.7.31"
                     /note="terminal transferase; terminal addition enzyme;
                     terminal deoxyribonucleotidyltransferase;
                     nucleosidetriphosphate:DNA deoxynucleotidylexotransferase;
                     terminal deoxynucleotidyltransferase"
                     /calculated_mol_wt=58405
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04053.3)"
     Region          11..17
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:P06526"
                     /note="propagated from UniProtKB/Swiss-Prot (P04053.3)"
     Region          31..125
                     /region_name="BRCT_DNTT"
                     /note="BRCT domain of DNA nucleotidylexotransferase (DNTT)
                     and similar proteins; cd18443"
                     /db_xref="CDD:349396"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09838; propagated from
                     UniProtKB/Swiss-Prot (P04053.3)"
     Region          151..509
                     /region_name="Mediates interaction with DNTTIP2.
                     /evidence=ECO:0000269|PubMed:12786946"
                     /note="propagated from UniProtKB/Swiss-Prot (P04053.3)"
     Region          163..508
                     /region_name="POLXc"
                     /note="DNA polymerase X family; smart00483"
                     /db_xref="CDD:214688"
     Region          258..262
                     /region_name="Involved in DNA binding.
                     /evidence=ECO:0000250|UniProtKB:P09838"
                     /note="propagated from UniProtKB/Swiss-Prot (P04053.3)"
     CDS             1..509
                     /gene="DNTT"
                     /gene_synonym="TDT"
                     /coded_by="NM_004088.4:65..1594"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7447.1"
                     /db_xref="GeneID:1791"
                     /db_xref="HGNC:HGNC:2983"
                     /db_xref="MIM:187410"
ORIGIN      
        1 mdpprashls prkkrprqtg almasspqdi kfqdlvvfil ekkmgttrra flmelarrkg
       61 frvenelsds vthivaenns gsdvlewlqa qkvqvssqpe lldvswliec iragkpvemt
      121 gkhqlvvrrd ysdstnpgpp ktppiavqki sqyacqrrtt lnncnqiftd afdilaence
      181 frenedscvt fmraasvlks lpftiismkd tegipclgsk vkgiieeiie dgessevkav
      241 lnderyqsfk lftsvfgvgl ktsekwfrmg frtlskvrsd kslkftrmqk agflyyedlv
      301 scvtraeaea vsvlvkeavw aflpdafvtm tggfrrgkkm ghdvdflits pgstedeeql
      361 lqkvmnlwek kglllyydlv estfeklrlp srkvdaldhf qkcflifklp rqrvdsdqss
      421 wqegktwkai rvdlvlcpye rrafallgwt gsrqferdlr ryatherkmi ldnhalydkt
      481 kriflkaese eeifahlgld yiepwerna
//
LOCUS       NP_001357516             171 aa            linear   PRI 27-APR-2025
DEFINITION  tudor-interacting repair regulator protein isoform 5 [Homo
            sapiens].
ACCESSION   NP_001357516
VERSION     NP_001357516.1
DBSOURCE    REFSEQ: accession NM_001370587.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Parnandi,N., Rendo,V., Cui,G., Botuyan,M.V., Remisova,M.,
            Nguyen,H., Drane,P., Beroukhim,R., Altmeyer,M., Mer,G. and
            Chowdhury,D.
  TITLE     TIRR inhibits the 53BP1-p53 complex to alter cell-fate programs
  JOURNAL   Mol Cell 81 (12), 2583-2595 (2021)
   PUBMED   33961797
  REMARK    GeneRIF: TIRR inhibits the 53BP1-p53 complex to alter cell-fate
            programs.
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 171)
  AUTHORS   Avolio,R., Jarvelin,A.I., Mohammed,S., Agliarulo,I., Condelli,V.,
            Zoppoli,P., Calice,G., Sarnataro,D., Bechara,E., Tartaglia,G.G.,
            Landriscina,M., Castello,A., Esposito,F. and Matassa,D.S.
  TITLE     Protein Syndesmos is a novel RNA-binding protein that regulates
            primary cilia formation
  JOURNAL   Nucleic Acids Res 46 (22), 12067-12086 (2018)
   PUBMED   30260431
  REMARK    GeneRIF: Identification of a small subset of mRNAs responsible for
            the biogenesis of primary cilium that have been linked to
            developmental and degenerative diseases, known as ciliopathies, and
            cancer. SDOS binds and regulates the translation of several of
            these mRNAs, controlling cilia development.
REFERENCE   6  (residues 1 to 171)
  AUTHORS   Zhang,A., Peng,B., Huang,P., Chen,J. and Gong,Z.
  TITLE     The p53-binding protein 1-Tudor-interacting repair regulator
            complex participates in the DNA damage response
  JOURNAL   J Biol Chem 292 (16), 6461-6467 (2017)
   PUBMED   28213517
  REMARK    GeneRIF: TIRR is a novel 53BP1-interacting protein that
            participates in the DNA damage response
REFERENCE   7  (residues 1 to 171)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 171)
  AUTHORS   Song,M.G., Li,Y. and Kiledjian,M.
  TITLE     Multiple mRNA decapping enzymes in mammalian cells
  JOURNAL   Mol Cell 40 (3), 423-432 (2010)
   PUBMED   21070968
REFERENCE   9  (residues 1 to 171)
  AUTHORS   Taylor,M.J. and Peculis,B.A.
  TITLE     Evolutionary conservation supports ancient origin for Nudt16, a
            nuclear-localized, RNA-binding, RNA-decapping enzyme
  JOURNAL   Nucleic Acids Res 36 (18), 6021-6034 (2008)
   PUBMED   18820299
REFERENCE   10 (residues 1 to 171)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023830.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138508.21207.1, BG469758.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..171
                     /product="tudor-interacting repair regulator protein
                     isoform 5"
                     /note="protein syndesmos; NUDT16-like protein 1; nudix
                     (nucleoside diphosphate linked moiety X)-type motif
                     16-like 1; tudor-interacting repair regulator protein"
                     /calculated_mol_wt=18813
     Region          23..>142
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     CDS             1..171
                     /gene="NUDT16L1"
                     /gene_synonym="SDOS; TIRR"
                     /coded_by="NM_001370587.1:10..525"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS92097.1"
                     /db_xref="GeneID:84309"
                     /db_xref="HGNC:HGNC:28154"
                     /db_xref="MIM:617338"
ORIGIN      
        1 mstaavpelk qisrveamrl gpgwshscha mlyaanpgql fgripmrfsv lmqmrfdgll
       61 gfpggfvdrr fwsledglnr vlglglgclr lteadylssh ltegphrvva hlyarqltle
      121 qlhaveisav hsrdhglevl nmmpeeklve alaaatekqk kalekllpas s
//
LOCUS       NP_001347287             790 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor RFX3 isoform 3 [Mus musculus].
ACCESSION   NP_001347287 XP_017173575
VERSION     NP_001347287.1
DBSOURCE    REFSEQ: accession NM_001360358.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Knoedler,J.R., Inoue,S., Bayless,D.W., Yang,T., Tantry,A.,
            Davis,C.H., Leung,N.Y., Parthasarathy,S., Wang,G., Alvarado,M.,
            Rizvi,A.H., Fenno,L.E., Ramakrishnan,C., Deisseroth,K. and
            Shah,N.M.
  TITLE     A functional cellular framework for sex and estrous cycle-dependent
            gene expression and behavior
  JOURNAL   Cell 185 (4), 654-671 (2022)
   PUBMED   35065713
  REMARK    Erratum:[Cell. 2024 Jul 11;187(14):3781. doi:
            10.1016/j.cell.2024.05.045. PMID: 38810647]
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Sun,Y., Yu,Z., Zhang,Y., Wang,H., Chi,Z., Chen,X. and Xu,D.
  TITLE     Downregulation of microRNA-342-3p Eases Insulin Resistance and
            Liver Gluconeogenesis via Regulating Rfx3 in Gestational Diabetes
            Mellitus
  JOURNAL   Crit Rev Eukaryot Gene Expr 32 (6), 83-95 (2022)
   PUBMED   35997120
  REMARK    GeneRIF: Downregulation of microRNA-342-3p Eases Insulin Resistance
            and Liver Gluconeogenesis via Regulating Rfx3 in Gestational
            Diabetes Mellitus.
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Lemeille,S., Paschaki,M., Baas,D., Morle,L., Duteyrat,J.L.,
            Ait-Lounis,A., Barras,E., Soulavie,F., Jerber,J., Thomas,J.,
            Zhang,Y., Holtzman,M.J., Kistler,W.S., Reith,W. and Durand,B.
  TITLE     Interplay of RFX transcription factors 1, 2 and 3 in motile
            ciliogenesis
  JOURNAL   Nucleic Acids Res 48 (16), 9019-9036 (2020)
   PUBMED   32725242
  REMARK    GeneRIF: Interplay of RFX transcription factors 1, 2 and 3 in
            motile ciliogenesis.
REFERENCE   4  (residues 1 to 790)
  AUTHORS   Lee,H. and Ko,H.W.
  TITLE     Cell cycle-related kinase is a crucial regulator for ciliogenesis
            and Hedgehog signaling in embryonic mouse lung development
  JOURNAL   BMB Rep 53 (7), 367-372 (2020)
   PUBMED   32317081
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Robson,A., Makova,S.Z., Barish,S., Zaidi,S., Mehta,S., Drozd,J.,
            Jin,S.C., Gelb,B.D., Seidman,C.E., Chung,W.K., Lifton,R.P.,
            Khokha,M.K. and Brueckner,M.
  TITLE     Histone H2B monoubiquitination regulates heart development via
            epigenetic control of cilia motility
  JOURNAL   Proc Natl Acad Sci U S A 116 (28), 14049-14054 (2019)
   PUBMED   31235600
  REMARK    GeneRIF: These data suggest that Rnf20 functions at the Rfx3 locus
            regulating cilia motility and cardiac situs and identify H2Bub1 as
            an upstream transcriptional regulator controlling tissue-specific
            expression of cilia genes. Our findings mechanistically link the
            two functional gene ontologies that have been implicated in human
            CHD: chromatin remodeling and cilia function.
REFERENCE   6  (residues 1 to 790)
  AUTHORS   Feistel,K. and Blum,M.
  TITLE     Three types of cilia including a novel 9+4 axoneme on the
            notochordal plate of the rabbit embryo
  JOURNAL   Dev Dyn 235 (12), 3348-3358 (2006)
   PUBMED   17061268
REFERENCE   7  (residues 1 to 790)
  AUTHORS   Baas,D., Meiniel,A., Benadiba,C., Bonnafe,E., Meiniel,O., Reith,W.
            and Durand,B.
  TITLE     A deficiency in RFX3 causes hydrocephalus associated with abnormal
            differentiation of ependymal cells
  JOURNAL   Eur J Neurosci 24 (4), 1020-1030 (2006)
   PUBMED   16930429
  REMARK    GeneRIF: These results demonstrate that regulatory factor X3 is
            necessary for ciliated ependymal cell differentiation in the mouse.
REFERENCE   8  (residues 1 to 790)
  AUTHORS   Bonnafe,E., Touka,M., AitLounis,A., Baas,D., Barras,E., Ucla,C.,
            Moreau,A., Flamant,F., Dubruille,R., Couble,P., Collignon,J.,
            Durand,B. and Reith,W.
  TITLE     The transcription factor RFX3 directs nodal cilium development and
            left-right asymmetry specification
  JOURNAL   Mol Cell Biol 24 (10), 4417-4427 (2004)
   PUBMED   15121860
  REMARK    GeneRIF: RFX3 is essential for the differentiation of nodal
            monocilia and hence for LR body axis determination.
REFERENCE   9  (residues 1 to 790)
  AUTHORS   Dubruille,R., Laurencon,A., Vandaele,C., Shishido,E.,
            Coulon-Bublex,M., Swoboda,P., Couble,P., Kernan,M. and Durand,B.
  TITLE     Drosophila regulatory factor X is necessary for ciliated sensory
            neuron differentiation
  JOURNAL   Development 129 (23), 5487-5498 (2002)
   PUBMED   12403718
REFERENCE   10 (residues 1 to 790)
  AUTHORS   Reith,W., Ucla,C., Barras,E., Gaud,A., Durand,B.,
            Herrero-Sanchez,C., Kobr,M. and Mach,B.
  TITLE     RFX1, a transactivator of hepatitis B virus enhancer I, belongs to
            a novel family of homodimeric and heterodimeric DNA-binding
            proteins
  JOURNAL   Mol Cell Biol 14 (2), 1230-1244 (1994)
   PUBMED   8289803
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC118628.11 and AC118005.9.
            
            On Feb 1, 2018 this sequence version replaced XP_017173575.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.167709.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 22.36 cM"
     Protein         1..790
                     /product="transcription factor RFX3 isoform 3"
                     /note="transcription factor RFX3; regulatory factor X 3"
                     /calculated_mol_wt=88027
     Region          <92..179
                     /region_name="RFX1_trans_act"
                     /note="RFX1 transcription activation region; pfam04589"
                     /db_xref="CDD:461362"
     Region          225..299
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     CDS             1..790
                     /gene="Rfx3"
                     /gene_synonym="C230093O12Rik; MRFX3"
                     /coded_by="NM_001360358.1:67..2439"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:19726"
                     /db_xref="MGI:MGI:106582"
ORIGIN      
        1 mkllnlkrnl firgametvr ellsdvyhlp plsppavset imqtsetgsd tgstvtlqts
       61 vasqaavptq vvqqvpvqqq vqqvqtvqqv qhvypaqvqy vegsdtvytn gairtttypy
      121 tetqmysqnt ggnyfdtqgs saqvttvvss hsmvgtggiq mgvtggqlis ssggtylign
      181 smensghsvt httraspati emaietlqks dglsthrssl lnshlqwlld nyetaegvsl
      241 prstlynhyl rhcqehkldp vnaasfgkli rsifmglrtr rlgtrgnsky hyygirvkpd
      301 splnrlqedm qymamrqqpm qqkqrykpmq kvdgvadgft gsgqqtgtsv eqtviaqsqh
      361 hqqfldasra lpefgeveis slpdgttfed ikslqslyre hceaildvvv nlqfsliekl
      421 wqtfwrysps tpadgttite ssnlseiesr lpkaklitlc khesilkwmc ncdhgmyqal
      481 veilipdvlr pipsaltqai rnfakslegw lsnamnnipq rmiqtkvaav safaqtlrry
      541 tslnhlaqaa ravlqntsqi nqmlsdlnrv dfanvqeqas wvcqcddnmv qrletdfkmt
      601 lqqqstleqw aawldnvmmq alkpyegrps fpkaarqfll kwsfyssmvi rdltlrsaas
      661 fgsfhlirll ydeymfylve hrvaqvtget piavmgefgd lnavspgnld kdegsevese
      721 tdedlddsse prakrektel sqafpvgcmq pvlesavqps llnplhsehi vtstqtirqc
      781 satgntytav
//
LOCUS       NP_079128                860 aa            linear   PRI 27-APR-2025
DEFINITION  protein argonaute-3 isoform a [Homo sapiens].
ACCESSION   NP_079128
VERSION     NP_079128.2
DBSOURCE    REFSEQ: accession NM_024852.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Pan,L., Xu,C., Mei,J., Chen,Y. and Wang,D.
  TITLE     Argonaute 3 (AGO3) promotes malignancy potential of cervical cancer
            via regulation of Wnt/beta-catenin signaling pathway
  JOURNAL   Reprod Biol 21 (1), 100479 (2021)
   PUBMED   33444963
  REMARK    GeneRIF: Argonaute 3 (AGO3) promotes malignancy potential of
            cervical cancer via regulation of Wnt/beta-catenin signaling
            pathway.
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Park,M.S., Sim,G., Kehling,A.C. and Nakanishi,K.
  TITLE     Human Argonaute2 and Argonaute3 are catalytically activated by
            different lengths of guide RNA
  JOURNAL   Proc Natl Acad Sci U S A 117 (46), 28576-28578 (2020)
   PUBMED   33122430
  REMARK    GeneRIF: Human Argonaute2 and Argonaute3 are catalytically
            activated by different lengths of guide RNA.
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Park,M.S., Phan,H.D., Busch,F., Hinckley,S.H., Brackbill,J.A.,
            Wysocki,V.H. and Nakanishi,K.
  TITLE     Human Argonaute3 has slicer activity
  JOURNAL   Nucleic Acids Res 45 (20), 11867-11877 (2017)
   PUBMED   29040713
  REMARK    GeneRIF: Data show that recombinant AGO3 loaded with miR-20a
            cleaves complementary target RNAs.
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Bridge,K.S., Shah,K.M., Li,Y., Foxler,D.E., Wong,S.C.K.,
            Miller,D.C., Davidson,K.M., Foster,J.G., Rose,R., Hodgkinson,M.R.,
            Ribeiro,P.S., Aboobaker,A.A., Yashiro,K., Wang,X., Graves,P.R.,
            Plevin,M.J., Lagos,D. and Sharp,T.V.
  TITLE     Argonaute Utilization for miRNA Silencing Is Determined by
            Phosphorylation-Dependent Recruitment of LIM-Domain-Containing
            Proteins
  JOURNAL   Cell Rep 20 (1), 173-187 (2017)
   PUBMED   28683311
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 860)
  AUTHORS   Wu,L., Fan,J. and Belasco,J.G.
  TITLE     Importance of translation and nonnucleolytic ago proteins for
            on-target RNA interference
  JOURNAL   Curr Biol 18 (17), 1327-1332 (2008)
   PUBMED   18771919
  REMARK    GeneRIF: The specificity of RNA interference depends on the
            concentration of Ago1, Ago3, and Ago4 relative to Ago2.
REFERENCE   7  (residues 1 to 860)
  AUTHORS   Meister,G., Landthaler,M., Patkaniowska,A., Dorsett,Y., Teng,G. and
            Tuschl,T.
  TITLE     Human Argonaute2 mediates RNA cleavage targeted by miRNAs and
            siRNAs
  JOURNAL   Mol Cell 15 (2), 185-197 (2004)
   PUBMED   15260970
REFERENCE   8  (residues 1 to 860)
  AUTHORS   Sasaki,T., Shiohama,A., Minoshima,S. and Shimizu,N.
  TITLE     Identification of eight members of the Argonaute family in the
            human genome
  JOURNAL   Genomics 82 (3), 323-330 (2003)
   PUBMED   12906857
REFERENCE   9  (residues 1 to 860)
  AUTHORS   Doi,N., Zenno,S., Ueda,R., Ohki-Hamazaki,H., Ui-Tei,K. and Saigo,K.
  TITLE     Short-interfering-RNA-mediated gene silencing in mammalian cells
            requires Dicer and eIF2C translation initiation factors
  JOURNAL   Curr Biol 13 (1), 41-46 (2003)
   PUBMED   12526743
REFERENCE   10 (residues 1 to 860)
  AUTHORS   Carmell,M.A., Xuan,Z., Zhang,M.Q. and Hannon,G.J.
  TITLE     The Argonaute family: tentacles that reach into RNAi, developmental
            control, stem cell maintenance, and tumorigenesis
  JOURNAL   Genes Dev 16 (21), 2733-2742 (2002)
   PUBMED   12414724
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF979526.1, AL139286.13,
            AL138787.11, AK303929.1, BX104163.1 and AA251146.1.
            
            On Mar 27, 2003 this sequence version replaced NP_079128.1.
            
            Summary: This gene encodes a member of the Argonaute family of
            proteins which play a role in RNA interference. The encoded protein
            is highly basic, contains a PAZ domain and a PIWI domain, and may
            play a role in short-interfering-RNA-mediated gene silencing. This
            gene is located on chromosome 1 in a tandem cluster of closely
            related family members including argonaute 4 and eukaryotic
            translation initiation factor 2C, 1. Two transcript variants
            encoding distinct isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript, and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.136680.1,
                                           SRR1803612.186539.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373191.9/ ENSP00000362287.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..860
                     /product="protein argonaute-3 isoform a"
                     /EC_number="3.1.26.n2"
                     /note="hAgo3; argonaute 3, RISC catalytic component;
                     eukaryotic translation initiation factor 2C, 3"
                     /calculated_mol_wt=97230
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H9G7.2)"
     Region          73..167
                     /region_name="ArgoN"
                     /note="N-terminal domain of argonaute; pfam16486"
                     /db_xref="CDD:465134"
     Region          177..227
                     /region_name="ArgoL1"
                     /note="Argonaute linker 1 domain; pfam08699"
                     /db_xref="CDD:462567"
     Region          228..348
                     /region_name="PAZ_argonaute_like"
                     /note="PAZ domain, argonaute_like subfamily. Argonaute is
                     part of the RNA-induced silencing complex (RISC), and is
                     an endonuclease that plays a key role in the RNA
                     interference pathway. The PAZ domain has been named after
                     the proteins Piwi,Argonaut, and Zwille; cd02846"
                     /db_xref="CDD:239212"
     Site            order(280,295,309,313,331,338,340)
                     /site_type="other"
                     /note="nucleic acid-binding interface [nucleotide
                     binding]"
                     /db_xref="CDD:239212"
     Region          393..818
                     /region_name="Piwi_ago-like"
                     /note="PIWI domain, Argonaute-like subfamily. Argonaute is
                     the central component of the RNA-induced silencing complex
                     (RISC) and related complexes. The PIWI domain is the
                     C-terminal portion of Argonaute and consists of two
                     subdomains, one of which provides the...; cd04657"
                     /db_xref="CDD:240015"
     Site            order(530,534,546..549,552,560,563,567,571)
                     /site_type="active"
                     /note="5' RNA guide strand anchoring site [active]"
                     /db_xref="CDD:240015"
     Region          530..567
                     /region_name="Interaction with guide RNA.
                     /evidence=ECO:0000305|PubMed:29040713"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9G7.2)"
     Site            order(598,600,670,808)
                     /site_type="active"
                     /db_xref="CDD:240015"
     Region          758..805
                     /region_name="Interaction with guide RNA.
                     /evidence=ECO:0000305|PubMed:29040713"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9G7.2)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H9G7.2)"
     CDS             1..860
                     /gene="AGO3"
                     /gene_synonym="EIF2C3"
                     /coded_by="NM_024852.4:323..2905"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS399.1"
                     /db_xref="GeneID:192669"
                     /db_xref="HGNC:HGNC:18421"
                     /db_xref="MIM:607355"
ORIGIN      
        1 meigsagpag aqpllmvprr pgygtmgkpi kllancfqve ipkidvylye vdikpdkcpr
       61 rvnrevvdsm vqhfkvtifg drrpvydgkr slytanplpv attgvdldvt lpgeggkdrp
      121 fkvsikfvsr vswhllhevl tgrtlpeple ldkpistnpv havdvvlrhl psmkytpvgr
      181 sffsapegyd hplgggrevw fgfhqsvrpa mwkmmlnidv satafykaqp viqfmcevld
      241 ihnideqprp ltdshrvkft keikglkvev thcgtmrrky rvcnvtrrpa shqtfplqle
      301 ngqtvertva qyfrekytlq lkyphlpclq vgqeqkhtyl plevcnivag qrcikkltdn
      361 qtstmikata rsapdrqeei srlvrsanye tdpfvqefqf kvrdemahvt grvlpapmlq
      421 yggrnrtvat pshgvwdmrg kqfhtgveik mwaiacfatq rqcreeilkg ftdqlrkisk
      481 dagmpiqgqp cfckyaqgad svepmfrhlk ntysglqlii vilpgktpvy aevkrvgdtl
      541 lgmatqcvqv knviktspqt lsnlclkinv klgginnilv phqrpsvfqq pviflgadvt
      601 hppagdgkkp siaavvgsmd ahpsrycatv rvqrprqeii qdlasmvrel liqfykstrf
      661 kptriifyrd gvsegqfrqv lyyellaire acislekdyq pgityivvqk rhhtrlfcad
      721 rtervgrsgn ipagttvdtd ithpyefdfy lcshagiqgt srpshyhvlw ddncftadel
      781 qlltyqlcht yvrctrsvsi papayyahlv afraryhlvd kehdsaegsh vsgqsngrdp
      841 qalakavqih qdtlrtmyfa
//
LOCUS       NP_699197               3571 aa            linear   PRI 27-APR-2025
DEFINITION  sushi, von Willebrand factor type A, EGF and pentraxin
            domain-containing protein 1 precursor [Homo sapiens].
ACCESSION   NP_699197 XP_933716 XP_946359
VERSION     NP_699197.3
DBSOURCE    REFSEQ: accession NM_153366.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3571)
  AUTHORS   Tian,Q., Chen,J.H., Ding,Y., Wang,X.Y., Qiu,J.Y., Cao,Q.,
            Zhuang,L.L., Jin,R. and Zhou,G.P.
  TITLE     EGR1 transcriptionally regulates SVEP1 to promote proliferation and
            migration in human coronary artery smooth muscle cells
  JOURNAL   Mol Biol Rep 51 (1), 365 (2024)
   PUBMED   38409611
  REMARK    GeneRIF: EGR1 transcriptionally regulates SVEP1 to promote
            proliferation and migration in human coronary artery smooth muscle
            cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 3571)
  AUTHORS   Andrews,S.L., Ghaderi-Najafabadi,M., Gong,P., Shamkhi,N.,
            Carleton,L., Schofield,C., Kessler,T., Samani,N.J., Webb,T.R. and
            Morris,G.E.
  TITLE     SVEP1 influences monocyte to macrophage differentiation via
            integrin alpha4beta1/alpha9beta1 and Rho/Rac signalling
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1870 (6), 119479 (2023)
   PUBMED   37100352
  REMARK    GeneRIF: SVEP1 influences monocyte to macrophage differentiation
            via integrin alpha4beta1/alpha9beta1 and Rho/Rac signalling.
REFERENCE   3  (residues 1 to 3571)
  AUTHORS   Elenbaas,J.S., Pudupakkam,U., Ashworth,K.J., Kang,C.J., Patel,V.,
            Santana,K., Jung,I.H., Lee,P.C., Burks,K.H., Amrute,J.M.,
            Mecham,R.P., Halabi,C.M., Alisio,A., Di Paola,J. and Stitziel,N.O.
  TITLE     SVEP1 is an endogenous ligand for the orphan receptor PEAR1
  JOURNAL   Nat Commun 14 (1), 850 (2023)
   PUBMED   36792666
  REMARK    Erratum:[Nat Commun. 2023 Mar 17;14(1):1511. doi:
            10.1038/s41467-023-37005-x. PMID: 36932061]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3571)
  AUTHORS   Morris,G.E., Denniff,M.J., Karamanavi,E., Andrews,S.A.,
            Kostogrys,R.B., Bountziouka,V., Ghaderi-Najafabadi,M., Shamkhi,N.,
            McConnell,G., Kaiser,M.A., Carleton,L., Schofield,C., Kessler,T.,
            Rainbow,R.D., Samani,N.J. and Webb,T.R.
  TITLE     The integrin ligand SVEP1 regulates GPCR-mediated vasoconstriction
            via integrins alpha9beta1 and alpha4beta1
  JOURNAL   Br J Pharmacol 179 (21), 4958-4973 (2022)
   PUBMED   35802072
  REMARK    GeneRIF: The integrin ligand SVEP1 regulates GPCR-mediated
            vasoconstriction via integrins alpha9beta1 and alpha4beta1.
REFERENCE   5  (residues 1 to 3571)
  AUTHORS   Gong,W.C., Han,Z.Q., Guo,M.X., Zhao,S., Guo,Y.H., Meng,B., Sun,Y.
            and Chen,L.
  TITLE     Decreased expression of SVEP1 is closely related to a cancer stem
            cell-like phenotype and poor prognosis in hepatocellular carcinoma
  JOURNAL   Neoplasma 69 (5), 1209-1216 (2022)
   PUBMED   35900319
  REMARK    GeneRIF: Decreased expression of SVEP1 is closely related to a
            cancer stem cell-like phenotype and poor prognosis in
            hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 3571)
  AUTHORS   Tang,C.S., Sribudiani,Y., Miao,X.P., de Vries,A.R., Burzynski,G.,
            So,M.T., Leon,Y.Y., Yip,B.H., Osinga,J., Hui,K.J., Verheij,J.B.,
            Cherny,S.S., Tam,P.K., Sham,P.C., Hofstra,R.M. and
            Garcia-Barcelo,M.M.
  TITLE     Fine mapping of the 9q31 Hirschsprung's disease locus
  JOURNAL   Hum Genet 127 (6), 675-683 (2010)
   PUBMED   20361209
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 3571)
  AUTHORS   Schwanzer-Pfeiffer,D., Rossmanith,E., Schildberger,A. and
            Falkenhagen,D.
  TITLE     Characterization of SVEP1, KIAA, and SRPX2 in an in vitro cell
            culture model of endotoxemia
  JOURNAL   Cell Immunol 263 (1), 65-70 (2010)
   PUBMED   20236627
  REMARK    GeneRIF: acts as regulator of ICAM1 and E-selectin during
            endotoxemia
REFERENCE   8  (residues 1 to 3571)
  AUTHORS   Ferreira,M.A., O'Donovan,M.C., Meng,Y.A., Jones,I.R.,
            Ruderfer,D.M., Jones,L., Fan,J., Kirov,G., Perlis,R.H., Green,E.K.,
            Smoller,J.W., Grozeva,D., Stone,J., Nikolov,I., Chambert,K.,
            Hamshere,M.L., Nimgaonkar,V.L., Moskvina,V., Thase,M.E., Caesar,S.,
            Sachs,G.S., Franklin,J., Gordon-Smith,K., Ardlie,K.G.,
            Gabriel,S.B., Fraser,C., Blumenstiel,B., Defelice,M., Breen,G.,
            Gill,M., Morris,D.W., Elkin,A., Muir,W.J., McGhee,K.A.,
            Williamson,R., MacIntyre,D.J., MacLean,A.W., St,C.D., Robinson,M.,
            Van Beck,M., Pereira,A.C., Kandaswamy,R., McQuillin,A.,
            Collier,D.A., Bass,N.J., Young,A.H., Lawrence,J., Ferrier,I.N.,
            Anjorin,A., Farmer,A., Curtis,D., Scolnick,E.M., McGuffin,P.,
            Daly,M.J., Corvin,A.P., Holmans,P.A., Blackwood,D.H., Gurling,H.M.,
            Owen,M.J., Purcell,S.M., Sklar,P. and Craddock,N.
  CONSRTM   Wellcome Trust Case Control Consortium
  TITLE     Collaborative genome-wide association analysis supports a role for
            ANK3 and CACNA1C in bipolar disorder
  JOURNAL   Nat Genet 40 (9), 1056-1058 (2008)
   PUBMED   18711365
REFERENCE   9  (residues 1 to 3571)
  AUTHORS   Shur,I., Socher,R., Hameiri,M., Fried,A. and Benayahu,D.
  TITLE     Molecular and cellular characterization of SEL-OB/SVEP1 in
            osteogenic cells in vivo and in vitro
  JOURNAL   J Cell Physiol 206 (2), 420-427 (2006)
   PUBMED   16206243
  REMARK    GeneRIF: All together makes SEL-OB/SVEP1 an attractive marker for
            studying the role of stromal osteogenic cells and their
            interactions within the bone marrow microenvironment creating a
            network that regulates the skeletal homeostasis.
REFERENCE   10 (residues 1 to 3571)
  AUTHORS   Gilges,D., Vinit,M.A., Callebaut,I., Coulombel,L., Cacheux,V.,
            Romeo,P.H. and Vigon,I.
  TITLE     Polydom: a secreted protein with pentraxin, complement control
            protein, epidermal growth factor and von Willebrand factor A
            domains
  JOURNAL   Biochem J 352 Pt 1 (Pt 1), 49-59 (2000)
   PUBMED   11062057
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC030816.1, AY243503.1, CX165144.1, DR008048.1, BF368046.1,
            DV080389.1, AK075200.1, AL832416.1, AL158158.14 and BX106110.1.
            
            On Jun 16, 2007 this sequence version replaced NP_699197.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1705030.1,
                                           SRR14038193.1838409.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374469.6/ ENSP00000363593.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..3571
                     /product="sushi, von Willebrand factor type A, EGF and
                     pentraxin domain-containing protein 1 precursor"
                     /note="sushi, von Willebrand factor type A, EGF and
                     pentraxin domain-containing protein 1; selectin-like
                     protein; serologically defined breast cancer antigen
                     NY-BR-38; CCP module-containing protein 22; selectin-like
                     osteoblast-derived protein"
                     /calculated_mol_wt=388280
     sig_peptide     1..17
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4LDE5.3)"
                     /calculated_mol_wt=1910
     mat_peptide     18..3571
                     /product="Sushi, von Willebrand factor type A, EGF and
                     pentraxin domain-containing protein 1. /id=PRO_0000320179"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4LDE5.3)"
                     /calculated_mol_wt=388280
     Region          83..258
                     /region_name="VWA"
                     /note="von Willebrand factor type A domain; pfam00092"
                     /db_xref="CDD:459670"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4LDE5.3)"
     Region          310..360
                     /region_name="Ephrin_rec_like"
                     /note="Tyrosine-protein kinase ephrin type A/B
                     receptor-like; pfam07699"
                     /db_xref="CDD:429604"
     Region          378..434
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(388,407)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          438..494
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(448,467)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          560..642
                     /region_name="HYR"
                     /note="HYR domain; pfam02494"
                     /db_xref="CDD:460572"
     Region          644..722
                     /region_name="HYR"
                     /note="HYR domain; pfam02494"
                     /db_xref="CDD:460572"
     Site            847
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4LDE5.3)"
     Region          887..894
                     /region_name="O-glycosylated at one site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4LDE5.3)"
     Region          1005..1052
                     /region_name="Ephrin_rec_like"
                     /note="Tyrosine-protein kinase ephrin type A/B
                     receptor-like; pfam07699"
                     /db_xref="CDD:429604"
     Region          1059..1106
                     /region_name="Ephrin_rec_like"
                     /note="Tyrosine-protein kinase ephrin type A/B
                     receptor-like; pfam07699"
                     /db_xref="CDD:429604"
     Site            1102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4LDE5.3)"
     Region          1113..1160
                     /region_name="Ephrin_rec_like"
                     /note="Tyrosine-protein kinase ephrin type A/B
                     receptor-like; pfam07699"
                     /db_xref="CDD:429604"
     Region          1196..1229
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1231..1267
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1231,1234,1248)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1269..1305
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1269,1272,1286)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1308..1342
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1345..1381
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1345,1348,1362)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1383..1419
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1383,1386,1400)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1424..1622
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cl22861"
                     /db_xref="CDD:473984"
     Site            order(1479,1556,1558,1565,1568)
                     /site_type="active"
                     /note="calcium mediated ligand binding site [active]"
                     /db_xref="CDD:238086"
     Site            order(1518,1535,1573,1622)
                     /site_type="active"
                     /note="intermolecular salt bridges [active]"
                     /db_xref="CDD:238086"
     Region          1628..1685
                     /region_name="Sushi"
                     /note="Sushi repeat (SCR repeat); pfam00084"
                     /db_xref="CDD:459664"
     Region          1690..1743
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(1700,1717)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          1745..1783
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1745,1748,1763)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1789..2017
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          1958..>2079
                     /region_name="PHA02817"
                     /note="EEV Host range protein; Provisional"
                     /db_xref="CDD:165167"
     Region          2094..2319
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          2280..>2436
                     /region_name="PHA02831"
                     /note="EEV host range protein; Provisional"
                     /db_xref="CDD:165176"
     Region          2401..2609
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          2639..2646
                     /region_name="Important for the interaction with integrin
                     ITGA9:ITGB1. /evidence=ECO:0000250|UniProtKB:A2AVA0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4LDE5.3)"
     Site            2642
                     /site_type="other"
                     /note="Required for interaction with integrin ITGA9:ITGB1.
                     /evidence=ECO:0000250|UniProtKB:A2AVA0; propagated from
                     UniProtKB/Swiss-Prot (Q4LDE5.3)"
     Region          <2670..2713
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Region          2714..>2887
                     /region_name="PHA02639"
                     /note="EEV host range protein; Provisional"
                     /db_xref="CDD:165022"
     Region          2833..>3003
                     /region_name="PHA02639"
                     /note="EEV host range protein; Provisional"
                     /db_xref="CDD:165022"
     Region          2845..2847
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4LDE5.3)"
     Region          3015..3229
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Site            3018
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4LDE5.3)"
     Site            3186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4LDE5.3)"
     Region          3195..3411
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Region          3416..3469
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(3426,3443)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     CDS             1..3571
                     /gene="SVEP1"
                     /gene_synonym="C9orf13; CCP22; POLYDOM; SEL-OB; SELOB"
                     /coded_by="NM_153366.4:199..10914"
                     /db_xref="CCDS:CCDS48004.1"
                     /db_xref="GeneID:79987"
                     /db_xref="HGNC:HGNC:15985"
                     /db_xref="MIM:611691"
ORIGIN      
        1 mwprlafccw glalvsgwat fqqmspsrnf sfrlfpetap gapgsipapp apgdeaagsr
       61 verlgqafrr rvrllrelse rlelvflvdd sssvgevnfr selmfvrkll sdfpvvptat
      121 rvaivtfssk nyvvprvdyi strrarqhkc alllqeipai syrgggtytk gafqqaaqil
      181 lharenstkv vflitdgysn ggdprpiaas lrdsgveift fgiwqgnire lndmastpke
      241 ehcyllhsfe efealarral hedlpsgsfi qddmvhcsyl cdegkdccdr mgsckcgtht
      301 ghfecicekg yygkglqyec tacpsgtykp egspggissc ipcpdenhts ppgstspedc
      361 vcregyrasg qtcelvhcpa lkppengyfi qntcnnhfna acgvrchpgf dlvgssiilc
      421 lpnglwsgse sycrvrtcph lrqpkhghis cstremlykt tclvacdegy rlegsdkltc
      481 qgnsqwdgpe prcverhcst fqmpkdviis phncgkqpak fgticyvscr qgfilsgvke
      541 mlrcttsgkw nvgvqaavck dveapqincp kdieaktleq qdsanvtwqi ptakdnsgek
      601 vsvhvhpaft ppylfpigdv aivytatdls gnqascifhi kvidaeppvi dwcrspppvq
      661 vsekvhaasw depqfsdnsg aelvitrsht qgdlfpqget ivqytatdps gnnrtcdihi
      721 vikgspceip ftpvngdfic tpdntgvnct ltclegydft egstdkyyca yedgvwkpty
      781 ttewpdcakk rfanhgfksf emfykaarcd dtdlmkkfse afettlgkmv psfcsdaedi
      841 dcrleenltk kycleynydy engfaigpgg wgaanrldys yddfldtvqe tatsignaks
      901 srikrsapls dykiklifni tasvplpder ndtlewenqq rllqtletit nklkrtlnkd
      961 pmysfqlase iliadsnsle tkkaspfcrp gsvlrgrmcv ncplgtyynl ehftcescri
     1021 gsyqdeegql ecklcpsgmy teyihsrnis dckaqckqgt ysysgletce scplgtyqpk
     1081 fgsrsclscp entstvkrga vnisacgvpc pegkfsrsgl mpchpcprdy yqpnagkafc
     1141 lacpfygttp fagsrsitec ssfsstfsaa eesvvppasl ghikkrheis sqvfhecffn
     1201 pchnsgtcqq lgrgyvclcp lgytglkcet didecsplpc lnngvckdlv geficecpsg
     1261 ytgqrceeni necssspcln kgicvdgvag yrctcvkgfv glhcetevne cqsnpclnna
     1321 vcedqvggfl ckcppgflgt rcgknvdecl sqpckngatc kdgansfrcl caagftgshc
     1381 elninecqsn pcrnqatcvd elnsysckcq pgfsgkrcet eqstgfnldf evsgiygyvm
     1441 ldgmlpslha ltctfwmkss ddmnygtpis yavdngsdnt llltdyngwv lyvngrekit
     1501 ncpsvndgrw hhiaitwtsa ngiwkvyidg klsdggagls vglpipggga lvlgqeqdkk
     1561 gegfspaesf vgsisqlnlw dyvlspqqvk slatscpeel skgnvlawpd flsgivgkvk
     1621 idsksifcsd cprlggsvph lrtasedlkp gskvnlfcdp gfqlvgnpvq yclnqgqwtq
     1681 plphcerisc gvppplengf hsaddfyags tvtyqcnngy yllgdsrmfc tdngswngvs
     1741 pscldvdeca vgsdcsehas clnvdgsyic scvppytgdg kncaepikck apgnpenghs
     1801 sgeiytvgae vtfscqegyq lmgvtkitcl esgewnhlip yckavscgkp aipengciee
     1861 laftfgskvt yrcnkgytla gdkessclan sswshsppvc epvkcsspen inngkyilsg
     1921 ltylstasys cdtgyslqgp siiectasgi wdrappachl vfcgeppaik davitgnnft
     1981 frntvtytck egytlagldt iecladgkws rsdqqclavs cdeppivdha spetahrlfg
     2041 diafyycsdg ysladnsqll cnaqgkwvpp egqdmprcia hfcekppsvs ysilesvska
     2101 kfaagsvvsf kcmegfvlnt sakiecmrgg qwnpspmsiq cipvrcgepp simngyasgs
     2161 nysfgamvay scnkgfyikg ekkstceatg qwsspiptch pvscgeppkv engflehttg
     2221 rifesevryq cnpgyksvgs pvfvcqanrh whsesplmcv pldcgkpppi qngfmkgenf
     2281 evgskvqffc negyelvgds swtcqksgkw nkksnpkcmp akcpepplle nqlvlkeltt
     2341 evgvvtfsck eghvlqgpsv lkclpsqqwn dsfpvckivl ctppplisfg vpipssalhf
     2401 gstvkyscvg gfflrgnstt lcqpdgtwss plpecvpvec pqpeeipngi idvqglayls
     2461 talytckpgf elvgntttlc genghwlggk ptckaieclk pkeilngkfs ytdlhygqtv
     2521 tyscnrgfrl egpsaltcle tgdwdvdaps cnaihcdspq piengfvega dysygaiiiy
     2581 scfpgfqvag hamqtceesg wsssiptcmp idcglpphid fgdctklkdd qgyfeqeddm
     2641 mevpyvtphp pyhlgavakt wentkespat hssnflygtm vsytcnpgye llgnpvlicq
     2701 edgtwngsap scisiecdlp tapengflrf tetsmgsavq ysckpghila gsdlrlclen
     2761 rkwsgasprc eaisckkpnp vmngsikgsn ytylstlyye cdpgyvlngt errtcqddkn
     2821 wdedepicip vdcssppvsa ngqvrgdeyt fqkeieytcn egfllegars rvclangsws
     2881 gatpdcvpvr catppqlang vtegldygfm kevtfhcheg yilhgapklt cqsdgnwdae
     2941 iplckpvncg ppedlahgfp ngfsfihggh iqyqcfpgyk lhgnssrrcl sngswsgssp
     3001 sclpcrcstp vieygtvngt dfdcgkaari qcfkgfkllg lseitceadg qwssgfphce
     3061 htscgslpmi pnafisetss wkenvitysc rsgyviqgss dlictekgvw sqpypvcepl
     3121 scgsppsvan avatgeahty esevklrcle gytmdtdtdt ftcqkdgrwf periscspkk
     3181 cplpenithi lvhgddfsvn rqvsvscaeg ytfegvnisv cqldgtwepp fsdescspvs
     3241 cgkpespehg fvvgskytfe stiiyqcepg yelegnrerv cqenrqwsgg vaicketrce
     3301 tpleflngka dienrttgpn vvyscnrgys legpseahct engtwshpvp lckpnpcpvp
     3361 fvipenalls ekefyvdqnv sikcregfll qghgiitcnp detwtqtsak cekiscgppa
     3421 hvenaiargv hyqygdmity scysgymleg flrsvcleng twtsppicra vcrfpcqngg
     3481 icqrpnacsc pegwmgrlce epicilpcln ggrcvapyqc dcppgwtgsr chtavcqspc
     3541 lnggkcvrpn rchclsswtg hncsrkrrtg f
//
LOCUS       NP_115884                 91 aa            linear   PRI 27-APR-2025
DEFINITION  homeodomain-only protein isoform a [Homo sapiens].
ACCESSION   NP_115884
VERSION     NP_115884.4
DBSOURCE    REFSEQ: accession NM_032495.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Yang,Q., Patrick,M., Lu,J., Chen,J., Zhang,Y., Hemani,H.,
            Lehrmann,E., De,S. and Weng,N.P.
  TITLE     Homeodomain-only protein suppresses proliferation and contributes
            to differentiation- and age-related reduced CD8+ T cell expansion
  JOURNAL   Front Immunol 15, 1360229 (2024)
   PUBMED   38410516
  REMARK    GeneRIF: Homeodomain-only protein suppresses proliferation and
            contributes to differentiation- and age-related reduced CD8[+] T
            cell expansion.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Kashyap,S., Rabbani,M., de Lima,I., Kondrachuk,O., Patel,R.,
            Shafiei,M.S., Mukker,A., Rajakumar,A. and Gupta,M.K.
  TITLE     HOPX Plays a Critical Role in Antiretroviral Drugs Induced
            Epigenetic Modification and Cardiac Hypertrophy
  JOURNAL   Cells 10 (12), 3458 (2021)
   PUBMED   34943964
  REMARK    GeneRIF: HOPX Plays a Critical Role in Antiretroviral Drugs Induced
            Epigenetic Modification and Cardiac Hypertrophy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Pavlova,O., Lefort,K., Mariotto,A., Huber,M. and Hohl,D.
  TITLE     HOPX Exhibits Oncogenic Activity during Squamous Skin
            Carcinogenesis
  JOURNAL   J Invest Dermatol 141 (10), 2354-2368 (2021)
   PUBMED   33845078
  REMARK    GeneRIF: HOPX Exhibits Oncogenic Activity during Squamous Skin
            Carcinogenesis.
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Lott,A., Oroz,J. and Zweckstetter,M.
  TITLE     Molecular basis of the interaction of Hsp90 with its co-chaperone
            Hop
  JOURNAL   Protein Sci 29 (12), 2422-2432 (2020)
   PUBMED   33040396
  REMARK    GeneRIF: Molecular basis of the interaction of Hsp90 with its
            co-chaperone Hop.
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Hng,C.H., Camp,E., Anderson,P., Breen,J., Zannettino,A. and
            Gronthos,S.
  TITLE     HOPX regulates bone marrow-derived mesenchymal stromal cell fate
            determination via suppression of adipogenic gene pathways
  JOURNAL   Sci Rep 10 (1), 11345 (2020)
   PUBMED   32647304
  REMARK    GeneRIF: HOPX regulates bone marrow-derived mesenchymal stromal
            cell fate determination via suppression of adipogenic gene
            pathways.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 91)
  AUTHORS   Kook,H., Lepore,J.J., Gitler,A.D., Lu,M.M., Wing-Man Yung,W.,
            Mackay,J., Zhou,R., Ferrari,V., Gruber,P. and Epstein,J.A.
  TITLE     Cardiac hypertrophy and histone deacetylase-dependent
            transcriptional repression mediated by the atypical homeodomain
            protein Hop
  JOURNAL   J Clin Invest 112 (6), 863-871 (2003)
   PUBMED   12975471
REFERENCE   7  (residues 1 to 91)
  AUTHORS   Asanoma,K., Matsuda,T., Kondo,H., Kato,K., Kishino,T., Niikawa,N.,
            Wake,N. and Kato,H.
  TITLE     NECC1, a candidate choriocarcinoma suppressor gene that encodes a
            homeodomain consensus motif
  JOURNAL   Genomics 81 (1), 15-25 (2003)
   PUBMED   12573257
  REMARK    GeneRIF: Loss of NECC1 expression is involved in malignant
            conversion of placental trophoblasts.
REFERENCE   8  (residues 1 to 91)
  AUTHORS   Chen,Y., Petersen,S., Pacyna-Gengelbach,M., Pietas,A. and
            Petersen,I.
  TITLE     Identification of a novel homeobox-containing gene, LAGY, which is
            downregulated in lung cancer
  JOURNAL   Oncology 64 (4), 450-458 (2003)
   PUBMED   12759545
  REMARK    GeneRIF: Gene mapping locates LAGY on chromosome 4q11-13.1. In 72
            primary lung tumors, this gene was significantly down-regulated
            compared to 9 normal lung tissue samples.
REFERENCE   9  (residues 1 to 91)
  AUTHORS   Adu,J., Leong,F.T., Smith,N.R., Leek,J.P., Markham,A.F.,
            Robinson,P.A. and Mighell,A.J.
  TITLE     Expression of mOb1, a novel atypical 73 amino acid K50-homeodomain
            protein, during mouse development
  JOURNAL   Mech Dev 119 Suppl 1, S43-S47 (2002)
   PUBMED   14516659
REFERENCE   10 (residues 1 to 91)
  AUTHORS   Weaver,A.J., Sullivan,W.P., Felts,S.J., Owen,B.A. and Toft,D.O.
  TITLE     Crystal structure and activity of human p23, a heat shock protein
            90 co-chaperone
  JOURNAL   J Biol Chem 275 (30), 23045-23052 (2000)
   PUBMED   10811660
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA512059.1 and AB059408.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 27, 2009 this sequence version replaced NP_115884.3.
            
            Summary: The protein encoded by this gene is a homeodomain protein
            that lacks certain conserved residues required for DNA binding. It
            was reported that choriocarcinoma cell lines and tissues failed to
            express this gene, which suggested the possible involvement of this
            gene in malignant conversion of placental trophoblasts. Studies in
            mice suggest that this protein may interact with serum response
            factor (SRF) and modulate SRF-dependent cardiac-specific gene
            expression and cardiac development. Multiple alternatively spliced
            transcript variants have been identified for this gene. [provided
            by RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.124401.1,
                                           SRR5189667.283528.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147920 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000420433.6/ ENSP00000396275.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..91
                     /product="homeodomain-only protein isoform a"
                     /note="not expressed in choriocarcinoma clone 1; lung
                     cancer-associated Y protein; homeodomain-only protein; odd
                     homeobox protein 1"
                     /calculated_mol_wt=10296
     Region          28..80
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     CDS             1..91
                     /gene="HOPX"
                     /gene_synonym="CAMEO; HOD; HOP; LAGY; NECC1; OB1; SMAP31;
                     TOTO"
                     /coded_by="NM_032495.6:126..401"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47062.1"
                     /db_xref="GeneID:84525"
                     /db_xref="HGNC:HGNC:24961"
                     /db_xref="MIM:607275"
ORIGIN      
        1 mliflgcyrr rleeragtms aetasgpted qveileynfn kvdkhpdstt lcliaaeagl
       61 seeetqkwfk qrlakwrrse glpsecrsvt d
//
LOCUS       NP_060580                326 aa            linear   PRI 27-APR-2025
DEFINITION  docking protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_060580
VERSION     NP_060580.2
DBSOURCE    REFSEQ: accession NM_018110.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Heidarizadi,A., Salimi,M. and Mozdarani,H.
  TITLE     Study of DOK4 gene expression and promoter methylation in sporadic
            breast cancer
  JOURNAL   Neoplasma 67 (4), 916-921 (2020)
   PUBMED   32386480
  REMARK    GeneRIF: Study of DOK4 gene expression and promoter methylation in
            sporadic breast cancer.
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Petko,J., Justice-Bitner,S., Jin,J., Wong,V., Kittanakom,S.,
            Ferraro,T.N., Stagljar,I. and Levenson,R.
  TITLE     MOR is not enough: identification of novel mu-opioid receptor
            interacting proteins using traditional and modified membrane yeast
            two-hybrid screens
  JOURNAL   PLoS One 8 (6), e67608 (2013)
   PUBMED   23840749
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Hooker,E., Baldwin,C. and Lemay,S.
  TITLE     New insights into Dok-4 PTB domain structure and function
  JOURNAL   Biochem Biophys Res Commun 427 (1), 67-72 (2012)
   PUBMED   22982678
  REMARK    GeneRIF: the current study have explored in more detail the
            structure and function of the Dok-4 PTB domain.
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Jones,R.B., Gordus,A., Krall,J.A. and MacBeath,G.
  TITLE     A quantitative protein interaction network for the ErbB receptors
            using protein microarrays
  JOURNAL   Nature 439 (7073), 168-174 (2006)
   PUBMED   16273093
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Cai,D., Dhe-Paganon,S., Melendez,P.A., Lee,J. and Shoelson,S.E.
  TITLE     Two new substrates in insulin signaling, IRS5/DOK4 and IRS6/DOK5
  JOURNAL   J Biol Chem 278 (28), 25323-25330 (2003)
   PUBMED   12730241
  REMARK    GeneRIF: IRS5/DOK4 and IRS6/DOK5 represent two new signaling
            proteins with potential roles in insulin and IGF-1 action
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Favre,C., Gerard,A., Clauzier,E., Pontarotti,P., Olive,D. and
            Nunes,J.A.
  TITLE     DOK4 and DOK5: new Dok-related genes expressed in human T cells
  JOURNAL   Genes Immun 4 (1), 40-45 (2003)
   PUBMED   12595900
  REMARK    GeneRIF: DOK4 expression in human T cells has been demonstrated,
            and its genomic structure has been predicted.
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Grimm,J., Sachs,M., Britsch,S., Di Cesare,S., Schwarz-Romond,T.,
            Alitalo,K. and Birchmeier,W.
  TITLE     Novel p62dok family members, dok-4 and dok-5, are substrates of the
            c-Ret receptor tyrosine kinase and mediate neuronal differentiation
  JOURNAL   J Cell Biol 154 (2), 345-354 (2001)
   PUBMED   11470823
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009052.8.
            
            On Apr 8, 2002 this sequence version replaced NP_060580.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC003541.1, DRR138524.770421.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340099.10/ ENSP00000344277.4
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q21"
     Protein         1..326
                     /product="docking protein 4 isoform 1"
                     /note="downstream of tyrosine kinase 4; insulin receptor
                     substrate 5"
                     /calculated_mol_wt=36897
     Region          9..113
                     /region_name="PH_DOK4_DOK5_DOK6"
                     /note="Pleckstrin homology (PH) domain of Downstream of
                     tyrosine kinase 4, 5, and 6 proteins; cd14678"
                     /db_xref="CDD:270197"
     Region          133..235
                     /region_name="PTB_DOK4_DOK5_DOK6"
                     /note="Downstream of tyrosine kinase 4, 5, and 6 proteins
                     phosphotyrosine-binding domain (PTBi); cd13164"
                     /db_xref="CDD:241318"
     Site            order(184..189,195,199..200,210,223)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:241318"
     Region          265..275
                     /region_name="DKFBH motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW6.2)"
     CDS             1..326
                     /gene="DOK4"
                     /gene_synonym="IRS-5; IRS5"
                     /coded_by="NM_018110.5:371..1351"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10783.1"
                     /db_xref="GeneID:55715"
                     /db_xref="HGNC:HGNC:19868"
                     /db_xref="MIM:608333"
ORIGIN      
        1 matnfsdivk qgyvkmksrk lgiyrrcwlv frkssskgpq rlekypdeks vclrgcpkvt
       61 eisnvkcvtr lpketkrqav aiiftddsar tftcdselea eewyktlsve clgsrlndis
      121 lgepdllapg vqceqtdrfn vfllpcpnld vygecklqit heniylwdih nprvklvswp
      181 lcslrrygrd atrftfeagr mcdageglyt fqtqegeqiy qrvhsatlai aeqhkrvlle
      241 meknvrllnk gtehysypct pttmlprsay whhitgsqni aeassyageg ygaaqasset
      301 dllnrfillk pkpsqgdsse aktpsq
//
LOCUS       NP_003402                801 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger Y-chromosomal protein isoform 1 [Homo sapiens].
ACCESSION   NP_003402
VERSION     NP_003402.2
DBSOURCE    REFSEQ: accession NM_003411.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Ni,W., Perez,A.A., Schreiner,S., Nicolet,C.M. and Farnham,P.J.
  TITLE     Characterization of the ZFX family of transcription factors that
            bind downstream of the start site of CpG island promoters
  JOURNAL   Nucleic Acids Res 48 (11), 5986-6000 (2020)
   PUBMED   32406922
  REMARK    GeneRIF: Characterization of the ZFX family of transcription
            factors that bind downstream of the start site of CpG island
            promoters.
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Decarpentrie,F., Vernet,N., Mahadevaiah,S.K., Longepied,G.,
            Streichemberger,E., Aknin-Seifer,I., Ojarikre,O.A., Burgoyne,P.S.,
            Metzler-Guillemain,C. and Mitchell,M.J.
  TITLE     Human and mouse ZFY genes produce a conserved testis-specific
            transcript encoding a zinc finger protein with a short acidic
            domain and modified transactivation potential
  JOURNAL   Hum Mol Genet 21 (12), 2631-2645 (2012)
   PUBMED   22407129
  REMARK    GeneRIF: Studies identified a major testis-specific ZFY transcript
            that encodes a protein with the same short acidic domain.
REFERENCE   5  (residues 1 to 801)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 801)
  AUTHORS   Tricoli,J.V. and Bracken,R.B.
  TITLE     ZFY gene expression and retention in human prostate adenocarcinoma
  JOURNAL   Genes Chromosomes Cancer 6 (2), 65-72 (1993)
   PUBMED   7680890
REFERENCE   7  (residues 1 to 801)
  AUTHORS   Kochoyan,M., Keutmann,H.T. and Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            refinement of the NMR structure of an even finger by selective
            deuterium labeling and implications for DNA recognition
  JOURNAL   Biochemistry 30 (29), 7063-7072 (1991)
   PUBMED   1854720
REFERENCE   8  (residues 1 to 801)
  AUTHORS   North,M., Sargent,C., O'Brien,J., Taylor,K., Wolfe,J., Affara,N.A.
            and Ferguson-Smith,M.A.
  TITLE     Comparison of ZFY and ZFX gene structure and analysis of
            alternative 3' untranslated regions of ZFY
  JOURNAL   Nucleic Acids Res 19 (10), 2579-2586 (1991)
   PUBMED   2041734
REFERENCE   9  (residues 1 to 801)
  AUTHORS   Kochoyan,M., Havel,T.F., Nguyen,D.T., Dahl,C.E., Keutmann,H.T. and
            Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            2D NMR structure of an even finger and implications for
            'jumping-linker' DNA recognition
  JOURNAL   Biochemistry 30 (14), 3371-3386 (1991)
   PUBMED   1849423
REFERENCE   10 (residues 1 to 801)
  AUTHORS   Palmer,M.S., Berta,P., Sinclair,A.H., Pym,B. and Goodfellow,P.N.
  TITLE     Comparison of human ZFY and ZFX transcripts
  JOURNAL   Proc Natl Acad Sci U S A 87 (5), 1681-1685 (1990)
   PUBMED   2308929
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006157.2, AI763177.1,
            AI469059.1, M30607.1, BC114526.1 and AL137603.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 25, 2003 this sequence version replaced NP_003402.1.
            
            Summary: This gene encodes a zinc finger-containing protein that
            may function as a transcription factor. This gene was once a
            candidate gene for the testis-determining factor (TDF) and was
            erroneously referred to as TDF. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer protein
            (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.74946.1, BC114960.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000155093.8/ ENSP00000155093.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yp11.2"
     Protein         1..801
                     /product="zinc finger Y-chromosomal protein isoform 1"
                     /note="zinc finger Y-chromosomal protein"
                     /calculated_mol_wt=90374
     Region          71..406
                     /region_name="Zfx_Zfy_act"
                     /note="Zfx / Zfy transcription activation region;
                     pfam04704"
                     /db_xref="CDD:461400"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17012; propagated from
                     UniProtKB/Swiss-Prot (P08048.3)"
     Region          <417..592
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          423..443
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          454..478
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          486..506
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(491,493,495,497..498,501..502,505,551,553,557..558,
                     561..562,565,579,581,583,585..586,589..590,593)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          539..>676
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          558..582
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          574..593
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          603..652
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          660..680
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          715..737
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          717..737
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(722,724,726,728..729,732..733,736,750,752,756..757,
                     760..761,765,779,781,783,785..786,789..790,793)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          729..753
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          745..766
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          774..794
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..801
                     /gene="ZFY"
                     /gene_synonym="ZNF911"
                     /coded_by="NM_003411.4:418..2823"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14774.1"
                     /db_xref="GeneID:7544"
                     /db_xref="HGNC:HGNC:12870"
                     /db_xref="MIM:490000"
ORIGIN      
        1 mdedefelqp qepnsffdgi gadathmdgd qivveiqeav fvsnivdsdi tvhnfvpddp
       61 dsvviqdvve dvvieedvqc sdileeadvs enviipeqvl dsdvteevsl phctvpddvl
      121 asditstsms mpehvltses mhvcdighve hmvhdsvvea eiitdpltsd ivseevlvad
      181 capeavidas gisvdqqdnd kascedylmi slddagkieh dgstgvtida esemdpckvd
      241 stcpevikvy ifkadpgedd lggtvdives ependhgvel ldqnssirvp rekmvymtvn
      301 dsqqededln vaeiadevym evivgeedaa vaaaaaavhe qqidedemkt fvpiawaaay
      361 gnnsdgienr ngtasallhi desaglgrla kqkpkkkrrp dsrqyqtaii igpdghpltv
      421 ypcmicgkkf ksrgflkrhm knhpehlakk kyhctdcdyt tnkkislhnh leshkltska
      481 ekaiecdecg khfshagalf thkmvhkekg ankmhkckfc eyetaeqgll nrhllavhsk
      541 nfphicvecg kgfrhpselr khmrihtgek pyqcqyceyr sadssnlkth iktkhskemp
      601 fkcdiclltf sdtkevqqht lvhqeskthq clhcdhkssn ssdlkrhvis vhtkdyphkc
      661 emcekgfhrp selkkhvavh kgkkmhqcrh cdfkiadpfv lsrhilsvht kdlpfrckrc
      721 rkgfrqqnel kkhmkthsgr kvyqceycey sttdasgfkr hvisihtkdy phrceyckkg
      781 frrpseknqh imrhhkevgl p
//
LOCUS       NP_057413                866 aa            linear   PRI 27-APR-2025
DEFINITION  scm-like with four MBT domains protein 1 [Homo sapiens].
ACCESSION   NP_057413 NP_056294
VERSION     NP_057413.2
DBSOURCE    REFSEQ: accession NM_016329.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Li,Y., Ma,C., Li,S., Wang,J., Li,W., Yang,Y., Li,X., Liu,J.,
            Yang,J., Liu,Y., Li,K., Li,J., Huang,D., Chen,R., Lv,L., Xiao,X.,
            Li,M. and Luo,X.J.
  TITLE     Regulatory Variant rs2535629 in ITIH3 Intron Confers Schizophrenia
            Risk By Regulating CTCF Binding and SFMBT1 Expression
  JOURNAL   Adv Sci (Weinh) 9 (6), e2104786 (2022)
   PUBMED   34978167
  REMARK    GeneRIF: Regulatory Variant rs2535629 in ITIH3 Intron Confers
            Schizophrenia Risk By Regulating CTCF Binding and SFMBT1
            Expression.
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Yuan,Y., Bao,J., Chen,Z., Villanueva,A.D., Wen,W., Wang,F.,
            Zhao,D., Fu,X., Cai,Q., Long,J., Shu,X.O., Zheng,D., Moreno,V.,
            Zheng,W., Lin,W. and Guo,X.
  TITLE     Multi-omics analysis to identify susceptibility genes for
            colorectal cancer
  JOURNAL   Hum Mol Genet 30 (5), 321-330 (2021)
   PUBMED   33481017
  REMARK    GeneRIF: Multi-omics analysis to identify susceptibility genes for
            colorectal cancer.
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Liu,X., Simon,J.M., Xie,H., Hu,L., Wang,J., Zurlo,G., Fan,C.,
            Ptacek,T.S., Herring,L., Tan,X., Li,M., Baldwin,A.S., Kim,W.Y.,
            Wu,T., Kirschner,M.W., Gong,K. and Zhang,Q.
  TITLE     Genome-wide Screening Identifies SFMBT1 as an Oncogenic Driver in
            Cancer with VHL Loss
  JOURNAL   Mol Cell 77 (6), 1294-1306 (2020)
   PUBMED   32023483
  REMARK    GeneRIF: High SFMBT1 expression is associated with clear cell renal
            cell carcinomas.
REFERENCE   5  (residues 1 to 866)
  AUTHORS   Li,R., Qiao,M., Zhao,X., Yan,J., Wang,X. and Sun,Q.
  TITLE     MiR-20a-3p regulates TGF-beta1/Survivin pathway to affect
            keratinocytes proliferation and apoptosis by targeting SFMBT1 in
            vitro
  JOURNAL   Cell Signal 49, 95-104 (2018)
   PUBMED   29886071
  REMARK    GeneRIF: SFMBT1 knockdown was demonstrated to inhibit cell growth
            and induced apoptosis, which was consistent with the function of
            miR-20a- 3p upregulation in HaCaT cells.
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Kottgen,A., Albrecht,E., Teumer,A., Vitart,V., Krumsiek,J.,
            Hundertmark,C., Pistis,G., Ruggiero,D., O'Seaghdha,C.M., Haller,T.,
            Yang,Q., Tanaka,T., Johnson,A.D., Kutalik,Z., Smith,A.V., Shi,J.,
            Struchalin,M., Middelberg,R.P., Brown,M.J., Gaffo,A.L., Pirastu,N.,
            Li,G., Hayward,C., Zemunik,T., Huffman,J., Yengo,L., Zhao,J.H.,
            Demirkan,A., Feitosa,M.F., Liu,X., Malerba,G., Lopez,L.M., van der
            Harst,P., Li,X., Kleber,M.E., Hicks,A.A., Nolte,I.M., Johansson,A.,
            Murgia,F., Wild,S.H., Bakker,S.J., Peden,J.F., Dehghan,A.,
            Steri,M., Tenesa,A., Lagou,V., Salo,P., Mangino,M., Rose,L.M.,
            Lehtimaki,T., Woodward,O.M., Okada,Y., Tin,A., Muller,C.,
            Oldmeadow,C., Putku,M., Czamara,D., Kraft,P., Frogheri,L.,
            Thun,G.A., Grotevendt,A., Gislason,G.K., Harris,T.B., Launer,L.J.,
            McArdle,P., Shuldiner,A.R., Boerwinkle,E., Coresh,J., Schmidt,H.,
            Schallert,M., Martin,N.G., Montgomery,G.W., Kubo,M., Nakamura,Y.,
            Tanaka,T., Munroe,P.B., Samani,N.J., Jacobs,D.R. Jr., Liu,K.,
            D'Adamo,P., Ulivi,S., Rotter,J.I., Psaty,B.M., Vollenweider,P.,
            Waeber,G., Campbell,S., Devuyst,O., Navarro,P., Kolcic,I.,
            Hastie,N., Balkau,B., Froguel,P., Esko,T., Salumets,A., Khaw,K.T.,
            Langenberg,C., Wareham,N.J., Isaacs,A., Kraja,A., Zhang,Q.,
            Wild,P.S., Scott,R.J., Holliday,E.G., Org,E., Viigimaa,M.,
            Bandinelli,S., Metter,J.E., Lupo,A., Trabetti,E., Sorice,R.,
            Doring,A., Lattka,E., Strauch,K., Theis,F., Waldenberger,M.,
            Wichmann,H.E., Davies,G., Gow,A.J., Bruinenberg,M., Stolk,R.P.,
            Kooner,J.S., Zhang,W., Winkelmann,B.R., Boehm,B.O., Lucae,S.,
            Penninx,B.W., Smit,J.H., Curhan,G., Mudgal,P., Plenge,R.M.,
            Portas,L., Persico,I., Kirin,M., Wilson,J.F., Mateo Leach,I., van
            Gilst,W.H., Goel,A., Ongen,H., Hofman,A., Rivadeneira,F.,
            Uitterlinden,A.G., Imboden,M., von Eckardstein,A., Cucca,F.,
            Nagaraja,R., Piras,M.G., Nauck,M., Schurmann,C., Budde,K.,
            Ernst,F., Farrington,S.M., Theodoratou,E., Prokopenko,I.,
            Stumvoll,M., Jula,A., Perola,M., Salomaa,V., Shin,S.Y.,
            Spector,T.D., Sala,C., Ridker,P.M., Kahonen,M., Viikari,J.,
            Hengstenberg,C., Nelson,C.P., Meschia,J.F., Nalls,M.A., Sharma,P.,
            Singleton,A.B., Kamatani,N., Zeller,T., Burnier,M., Attia,J.,
            Laan,M., Klopp,N., Hillege,H.L., Kloiber,S., Choi,H., Pirastu,M.,
            Tore,S., Probst-Hensch,N.M., Volzke,H., Gudnason,V., Parsa,A.,
            Schmidt,R., Whitfield,J.B., Fornage,M., Gasparini,P.,
            Siscovick,D.S., Polasek,O., Campbell,H., Rudan,I., Bouatia-Naji,N.,
            Metspalu,A., Loos,R.J., van Duijn,C.M., Borecki,I.B., Ferrucci,L.,
            Gambaro,G., Deary,I.J., Wolffenbuttel,B.H., Chambers,J.C., Marz,W.,
            Pramstaller,P.P., Snieder,H., Gyllensten,U., Wright,A.F., Navis,G.,
            Watkins,H., Witteman,J.C., Sanna,S., Schipf,S., Dunlop,M.G.,
            Tonjes,A., Ripatti,S., Soranzo,N., Toniolo,D., Chasman,D.I.,
            Raitakari,O., Kao,W.H., Ciullo,M., Fox,C.S., Caulfield,M.,
            Bochud,M. and Gieger,C.
  CONSRTM   LifeLines Cohort Study; CARDIoGRAM Consortium; DIAGRAM Consortium;
            ICBP Consortium; MAGIC Consortium
  TITLE     Genome-wide association analyses identify 18 new loci associated
            with serum urate concentrations
  JOURNAL   Nat Genet 45 (2), 145-154 (2013)
   PUBMED   23263486
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Jostins,L., Ripke,S., Weersma,R.K., Duerr,R.H., McGovern,D.P.,
            Hui,K.Y., Lee,J.C., Schumm,L.P., Sharma,Y., Anderson,C.A.,
            Essers,J., Mitrovic,M., Ning,K., Cleynen,I., Theatre,E.,
            Spain,S.L., Raychaudhuri,S., Goyette,P., Wei,Z., Abraham,C.,
            Achkar,J.P., Ahmad,T., Amininejad,L., Ananthakrishnan,A.N.,
            Andersen,V., Andrews,J.M., Baidoo,L., Balschun,T., Bampton,P.A.,
            Bitton,A., Boucher,G., Brand,S., Buning,C., Cohain,A., Cichon,S.,
            D'Amato,M., De Jong,D., Devaney,K.L., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Ferguson,L.R., Franchimont,D., Fransen,K.,
            Gearry,R., Georges,M., Gieger,C., Glas,J., Haritunians,T., Hart,A.,
            Hawkey,C., Hedl,M., Hu,X., Karlsen,T.H., Kupcinskas,L.,
            Kugathasan,S., Latiano,A., Laukens,D., Lawrance,I.C., Lees,C.W.,
            Louis,E., Mahy,G., Mansfield,J., Morgan,A.R., Mowat,C., Newman,W.,
            Palmieri,O., Ponsioen,C.Y., Potocnik,U., Prescott,N.J.,
            Regueiro,M., Rotter,J.I., Russell,R.K., Sanderson,J.D., Sans,M.,
            Satsangi,J., Schreiber,S., Simms,L.A., Sventoraityte,J.,
            Targan,S.R., Taylor,K.D., Tremelling,M., Verspaget,H.W., De Vos,M.,
            Wijmenga,C., Wilson,D.C., Winkelmann,J., Xavier,R.J., Zeissig,S.,
            Zhang,B., Zhang,C.K., Zhao,H., Silverberg,M.S., Annese,V.,
            Hakonarson,H., Brant,S.R., Radford-Smith,G., Mathew,C.G.,
            Rioux,J.D., Schadt,E.E., Daly,M.J., Franke,A., Parkes,M.,
            Vermeire,S., Barrett,J.C. and Cho,J.H.
  CONSRTM   International IBD Genetics Consortium (IIBDGC)
  TITLE     Host-microbe interactions have shaped the genetic architecture of
            inflammatory bowel disease
  JOURNAL   Nature 491 (7422), 119-124 (2012)
   PUBMED   23128233
REFERENCE   8  (residues 1 to 866)
  AUTHORS   Yang,H.C., Liang,Y.J., Chen,J.W., Chiang,K.M., Chung,C.M., Ho,H.Y.,
            Ting,C.T., Lin,T.H., Sheu,S.H., Tsai,W.C., Chen,J.H., Leu,H.B.,
            Yin,W.H., Chiu,T.Y., Chern,C.L., Lin,S.J., Tomlinson,B., Guo,Y.,
            Sham,P.C., Cherny,S.S., Lam,T.H., Thomas,G.N. and Pan,W.H.
  TITLE     Identification of IGF1, SLC4A4, WWOX, and SFMBT1 as hypertension
            susceptibility genes in Han Chinese with a genome-wide gene-based
            association study
  JOURNAL   PLoS One 7 (3), e32907 (2012)
   PUBMED   22479346
  REMARK    GeneRIF: Data identified IGF1, SLC4A4, WWOX, and SFMBT1 as
            hypertension susceptibility genes by gene based association scan
            and gene expression analysis.
REFERENCE   9  (residues 1 to 866)
  AUTHORS   Kato,T., Sato,H., Emi,M., Seino,T., Arawaka,S., Iseki,C.,
            Takahashi,Y., Wada,M. and Kawanami,T.
  TITLE     Segmental copy number loss of SFMBT1 gene in elderly individuals
            with ventriculomegaly: a community-based study
  JOURNAL   Intern Med 50 (4), 297-303 (2011)
   PUBMED   21325761
  REMARK    GeneRIF: A segmental copy number loss of the SFMBT1 gene may be
            involved in the pathological process in some individuals with
            ventriculomegaly/idiopathic normal pressure hydrocephalus.
REFERENCE   10 (residues 1 to 866)
  AUTHORS   Wu,S., Trievel,R.C. and Rice,J.C.
  TITLE     Human SFMBT is a transcriptional repressor protein that selectively
            binds the N-terminal tail of histone H3
  JOURNAL   FEBS Lett 581 (17), 3289-3296 (2007)
   PUBMED   17599839
  REMARK    GeneRIF: The tandem MBT repeats form a functional structure
            required for biological activity of hSFMBT and predict similar
            properties for other MBT domain-containing proteins.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096887.2, DB085221.1,
            BC014614.2, AC099667.2 and AI206996.1.
            
            On Oct 1, 2004 this sequence version replaced NP_057413.1.
            
            Summary: This gene shares high similarity with the Drosophila Scm
            (sex comb on midleg) gene. It encodes a protein which contains four
            malignant brain tumor repeat (mbt) domains and may be involved in
            antigen recognition. [provided by RefSeq, Jun 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2526614.1, BC014614.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394752.8/ ENSP00000378235.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.1"
     Protein         1..866
                     /product="scm-like with four MBT domains protein 1"
                     /note="Scm-related gene containing four mbt domains;
                     Scm-related gene product containing four mbt domains;
                     renal ubiquitous protein 1"
                     /calculated_mol_wt=98011
     Region          20..120
                     /region_name="MBT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHJ3.2)"
     Region          34..42
                     /region_name="Antigenic epitope"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHJ3.2)"
     Region          47..140
                     /region_name="MBT_SFMBT1_rpt1"
                     /note="first malignant brain tumor (MBT) repeat found in
                     Scm-like with four MBT domains protein 1 (SFMBT1);
                     cd20111"
                     /db_xref="CDD:439101"
     Site            order(60,63,66,68,84,87,93)
                     /site_type="other"
                     /note="putative methyllysine peptide binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439101"
     Region          128..232
                     /region_name="MBT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHJ3.2)"
     Region          159..257
                     /region_name="MBT_SFMBT1_rpt2"
                     /note="second malignant brain tumor (MBT) repeat found in
                     Scm-like with four MBT domains protein 1 (SFMBT1);
                     cd20113"
                     /db_xref="CDD:439103"
     Site            order(172,175,178,180,196,199,205)
                     /site_type="other"
                     /note="putative methyllysine peptide binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439103"
     Region          242..348
                     /region_name="MBT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHJ3.2)"
     Region          273..366
                     /region_name="MBT_SFMBT1_rpt3"
                     /note="third malignant brain tumor (MBT) repeat found in
                     Scm-like with four MBT domains protein 1 (SFMBT1);
                     cd20115"
                     /db_xref="CDD:439105"
     Region          356..453
                     /region_name="MBT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHJ3.2)"
     Region          382..471
                     /region_name="MBT_SFMBT1_rpt4"
                     /note="fourth malignant brain tumor (MBT) repeat found in
                     Scm-like with four MBT domains protein 1 (SFMBT1);
                     cd20117"
                     /db_xref="CDD:439107"
     Region          502..617
                     /region_name="SLED"
                     /note="SLED domain; pfam12140"
                     /db_xref="CDD:463469"
     Region          641..777
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHJ3.2)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHJ3.2)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHJ3.2)"
     Region          782..866
                     /region_name="SAM_Scm-like-4MBT1,2"
                     /note="SAM domain of Scm-like-4MBT1,2 proteins of Polycomb
                     group; cd09581"
                     /db_xref="CDD:188980"
     Site            order(821..823,825..826,829..830,833..834,839)
                     /site_type="other"
                     /note="putative oligomer interface ML [polypeptide
                     binding]"
                     /db_xref="CDD:188980"
     Site            order(842..845,847..848,851,854)
                     /site_type="other"
                     /note="putative oligomer interface EH [polypeptide
                     binding]"
                     /db_xref="CDD:188980"
     CDS             1..866
                     /gene="SFMBT1"
                     /gene_synonym="hSFMBT; RU1; SFMBT"
                     /coded_by="NM_016329.4:389..2989"
                     /db_xref="CCDS:CCDS2867.1"
                     /db_xref="GeneID:51460"
                     /db_xref="HGNC:HGNC:20255"
                     /db_xref="MIM:607319"
ORIGIN      
        1 mngeqqldad agsgmeevel swedyleetg stavpygsfk hvdtrlqngf apgmklevav
       61 rtdpetywva tvittceqll llrydgyged rradfwcdir kadlypigwc eqnkktleap
      121 egirdkvsdw deflrqtlig acsppvplle glrngrnpld liapgsrlec qafqdslstw
      181 ivtvvenigg rlklryegle ssdnyehwly yldpflhhvg waaqqgyelq ppsairhlkn
      241 eaewqeilak vkeeeeeplp sylfkdkqvi gihtfsvnmk leavdpwspf gispatvvkv
      301 fdekyflvem ddlrpenhar rsfvchadsp gifpvqwslk nglhispppg ypsqdfdwad
      361 ylkqcgaeaa pqrcfpplis ehefkenmkl eavnpilpee vcvatitavr gsylwlqleg
      421 skkpipeciv svesmdifpl gwcetnghpl stprrarvyk qrkiavvqpe kqvpssrtvh
      481 eglrnqelns tesvmingky ccpkiyfnhr cfsgpylnkg riaelpqcvg pgncvlvlre
      541 vltllinaay kpsrvlrelq ldkdsvwhgc gevlkakykg ksyratveiv ktadrvtefc
      601 rqtciklecc pnlfgprmvl dkcsencsvl tktkythyyg kkknkrigrp pgghsnlaca
      661 lkkaskrrkr rknvfvhkkk rssasvdntp agspqgsgge deddpdegdd dslsegstse
      721 qqdelqeese msekkscsss ptqseistsl ppdrqrrkre lrtfsfsdde nkppspkeir
      781 ievaerlhld snplkwsvad vvrfirstdc aplarifldq eidgqallll tlptvqecmd
      841 lklgpaiklc hhierikfaf yeqfan
//
LOCUS       NP_620450                271 aa            linear   PRI 27-APR-2025
DEFINITION  oligodendrocyte transcription factor 1 [Homo sapiens].
ACCESSION   NP_620450 XP_001127883 XP_001131712
VERSION     NP_620450.2
DBSOURCE    REFSEQ: accession NM_138983.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Sabo,J.K., Heine,V., Silbereis,J.C., Schirmer,L., Levison,S.W. and
            Rowitch,D.H.
  TITLE     Olig1 is required for noggin-induced neonatal myelin repair
  JOURNAL   Ann Neurol 81 (4), 560-571 (2017)
   PUBMED   28253550
  REMARK    GeneRIF: Olig1 has a critical function in regulation of postnatal
            neural progenitor cell production in response to Noggin.
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Rajkowska,G., Mahajan,G., Maciag,D., Sathyanesan,M., Iyo,A.H.,
            Moulana,M., Kyle,P.B., Woolverton,W.L., Miguel-Hidalgo,J.J.,
            Stockmeier,C.A. and Newton,S.S.
  TITLE     Oligodendrocyte morphometry and expression of myelin - Related mRNA
            in ventral prefrontal white matter in major depressive disorder
  JOURNAL   J Psychiatr Res 65, 53-62 (2015)
   PUBMED   25930075
  REMARK    GeneRIF: This study demonstrated that increased expression of mRNA
            of OLIG1 in ventral prefrontal white matter in major depressive
            disorder.
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Motizuki,M., Isogaya,K., Miyake,K., Ikushima,H., Kubota,T.,
            Miyazono,K., Saitoh,M. and Miyazawa,K.
  TITLE     Oligodendrocyte transcription factor 1 (Olig1) is a Smad cofactor
            involved in cell motility induced by transforming growth
            factor-beta
  JOURNAL   J Biol Chem 288 (26), 18911-18922 (2013)
   PUBMED   23720758
  REMARK    GeneRIF: Olig1 is a Smad cofactor involved in TGF-beta-induced cell
            motility
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Meijer,D.H., Kane,M.F., Mehta,S., Liu,H., Harrington,E.,
            Taylor,C.M., Stiles,C.D. and Rowitch,D.H.
  TITLE     Separated at birth? The functional and molecular divergence of
            OLIG1 and OLIG2
  JOURNAL   Nat Rev Neurosci 13 (12), 819-831 (2012)
   PUBMED   23165259
  REMARK    GeneRIF: This study review OLIG1 have developmental functions in
            patterning, neuron subtype specification and the formation of
            oligodendrocytes and play the role in the postnatal brain during
            repair processes and in neurological disease states.
            Review article
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Arnett,H.A., Fancy,S.P., Alberta,J.A., Zhao,C., Plant,S.R.,
            Kaing,S., Raine,C.S., Rowitch,D.H., Franklin,R.J. and Stiles,C.D.
  TITLE     bHLH transcription factor Olig1 is required to repair demyelinated
            lesions in the CNS
  JOURNAL   Science 306 (5704), 2111-2115 (2004)
   PUBMED   15604411
REFERENCE   7  (residues 1 to 271)
  AUTHORS   McLellan,A.S., Langlands,K. and Kealey,T.
  TITLE     Exhaustive identification of human class II basic helix-loop-helix
            proteins by virtual library screening
  JOURNAL   Mech Dev 119 Suppl 1, S285-S291 (2002)
   PUBMED   14516699
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Lu,Q.R., Park,J.K., Noll,E., Chan,J.A., Alberta,J., Yuk,D.,
            Alzamora,M.G., Louis,D.N., Stiles,C.D., Rowitch,D.H. and Black,P.M.
  TITLE     Oligodendrocyte lineage genes (OLIG) as molecular markers for human
            glial brain tumors
  JOURNAL   Proc Natl Acad Sci U S A 98 (19), 10851-10856 (2001)
   PUBMED   11526205
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Takebayashi,H., Yoshida,S., Sugimori,M., Kosako,H., Kominami,R.,
            Nakafuku,M. and Nabeshima,Y.
  TITLE     Dynamic expression of basic helix-loop-helix Olig family members:
            implication of Olig2 in neuron and oligodendrocyte differentiation
            and identification of a new member, Olig3
  JOURNAL   Mech Dev 99 (1-2), 143-148 (2000)
   PUBMED   11091082
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Zhou,Q., Wang,S. and Anderson,D.J.
  TITLE     Identification of a novel family of oligodendrocyte
            lineage-specific basic helix-loop-helix transcription factors
  JOURNAL   Neuron 25 (2), 331-343 (2000)
   PUBMED   10719889
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP000289.1, BC033290.1, AL834450.1 and AL355743.1.
            
            On May 19, 2009 this sequence version replaced NP_620450.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AL834450.1, BC033290.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382348.2/ ENSP00000371785.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..271
                     /product="oligodendrocyte transcription factor 1"
                     /note="oligodendrocyte-specific bHLH transcription factor
                     1; basic domain, helix-loop-helix protein, class B, 6;
                     oligodendrocyte lineage transcription factor 1; oligo1;
                     class B basic helix-loop-helix protein 6; class E basic
                     helix-loop-helix protein 21"
                     /calculated_mol_wt=27774
     Region          38..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAK6.2)"
     Region          101..175
                     /region_name="bHLH_TS_OLIG1"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     oligodendrocyte transcription factor 1 (Oligo1) and
                     similar proteins; cd18942"
                     /db_xref="CDD:381512"
     Site            order(107,111,113..115,117,122,147..150)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381512"
     Site            order(120..121,124..125,127..128,151,154,158,160..161,165,
                     167..168)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381512"
     CDS             1..271
                     /gene="OLIG1"
                     /gene_synonym="BHLHB6; BHLHE21"
                     /coded_by="NM_138983.3:107..922"
                     /db_xref="CCDS:CCDS42920.2"
                     /db_xref="GeneID:116448"
                     /db_xref="HGNC:HGNC:16983"
                     /db_xref="MIM:606385"
ORIGIN      
        1 myyavsqarv navpgtmlrp qrpgdlqlga slyelvgyrq ppssssssts stsstsssst
       61 tapllpkaar ekpeapaepp gpgpgsgahp ggsarpdake eqqqqlrrki nsrerkrmqd
      121 lnlamdalre vilpysaahc qgapgrklsk iatlllarny illlgsslqe lrralgegag
      181 paaprlllag lpllaaapgs vllapgavgp pdalrpakyl slaldeppcg qfalpgggag
      241 gpglctcavc kfphlvpasl glaavqaqfs k
//
LOCUS       NP_001356383            1019 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 445 isoform 2 [Homo sapiens].
ACCESSION   NP_001356383
VERSION     NP_001356383.1
DBSOURCE    REFSEQ: accession NM_001369454.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Takahashi,N., Coluccio,A., Thorball,C.W., Planet,E., Shi,H.,
            Offner,S., Turelli,P., Imbeault,M., Ferguson-Smith,A.C. and
            Trono,D.
  TITLE     ZNF445 is a primary regulator of genomic imprinting
  JOURNAL   Genes Dev 33 (1-2), 49-54 (2019)
   PUBMED   30602440
REFERENCE   4  (residues 1 to 1019)
  AUTHORS   Luo,K., Yuan,J., Shan,Y., Li,J., Xu,M., Cui,Y., Tang,W., Wan,B.,
            Zhang,N., Wu,Y. and Yu,L.
  TITLE     Activation of transcriptional activities of AP1 and SRE by a novel
            zinc finger protein ZNF445
  JOURNAL   Gene 367, 89-100 (2006)
   PUBMED   16368201
REFERENCE   5  (residues 1 to 1019)
  AUTHORS   Calabro,V., Pengue,G., Bartoli,P.C., Pagliuca,A., Featherstone,T.
            and Lania,L.
  TITLE     Positional cloning of cDNAs from the human chromosome 3p21-22
            region identifies a clustered organization of zinc-finger genes
  JOURNAL   Hum Genet 95 (1), 18-21 (1995)
   PUBMED   7814019
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY295873.2 and AC134943.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.213933.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1019
                     /product="zinc finger protein 445 isoform 2"
                     /note="zinc finger protein 168; zinc finger protein with
                     KRAB and SCAN domains 15"
                     /calculated_mol_wt=117536
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59923.1)"
     Region          51..155
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          222..280
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          403..439
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <445..631
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          448..467
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          475..495
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(480,482,484,486..487,490..491,494,508,510,514..515,
                     518..519,522,536,538,540,542..543,546..547,550)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          503..523
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          531..551
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          583..1019
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          587..607
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          615..635
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          671..691
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          699..719
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          752..772
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(757,759,761,763..764,767..768,771,785,787,791..792,
                     795..796,799,835,837,839,841..842,845..846,849)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          780..800
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          830..850
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          858..878
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          886..906
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          899..927
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59923.1)"
     Region          941..960
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(945,947,949,951..952,955..956,959,973,975,979..980,
                     983..984,987,1001,1003,1005,1007..1008,1011..1012,1015)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          968..988
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          996..1016
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1019
                     /gene="ZNF445"
                     /gene_synonym="ZFP445; ZKSCAN15; ZNF168; ZSCAN47"
                     /coded_by="NM_001369454.1:228..3287"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:353274"
                     /db_xref="HGNC:HGNC:21018"
                     /db_xref="MIM:619508"
ORIGIN      
        1 mppgrwhaay paqaqssrer grlqtvkkee edesytpvqa arpqtlnrpg qelfrqlfrq
       61 lryhessgpl etlsrlrelc rwwlrpdvls kaqilellvl eqflsilpge lrvwvqlhnp
      121 esgeeavall eelqrdldgt swrdpgpaqs pdvhwmgtga lrsaqiwsla splrsssalg
      181 dhleppyeie ardflagqsd tpaaqmpalf pregcpgdqe tmtfkdvevt fsqdewgwld
      241 saqrnlyrdv mlenyrnmas lvgpftkpal iswlearepw glnmqaaqpk gnpvaaptgd
      301 dlqsktnkfi lnqepleeae tlavssgcpa tsvsegiglr esfqqksrqk dqcenpiqvr
      361 vkkeetnfsh rtgkdsevsg snsldlkhvt ylrvsgrkes lkhgcgkhfr msshhydykk
      421 ygkglrhmig gfslhqrihs glkgnkkdvc gkdfslsshh qrgqslhtvg vsfkcsdcgr
      481 tfshsshlay hqrlhtqeka fkcrvcgkaf rwssncarhe kihtgvkpyk cdlcekafrr
      541 lsayrlhret hakkkfleln qyraaltyss gfdhhlgdqs geklfdcsqc rksfhcksyv
      601 lehqrihtqe kpykctkcrk tfrwrsnftr hmrlheeekf ykqdecregf rqspdcsqpq
      661 gapavektfl cqqcgktftr kktlvdhqri htgekpyqcs dcgkdfayrs afivhkkkha
      721 mkrkpeggps fsqdtvfqvp qsshskeepy kcsqcgkafr nhsfllihqr vhtgekpykc
      781 recgkafrws snlyrhqrih slqkqydche sektpnvepk iltgekrfwc qecgktftrk
      841 rtlldhkgih sgekrykcnl cgksydrnyr lvnhqrihst erpfkcqwcg kefigrhtls
      901 shqrkhtraa qaersppars ssqdtklrlq klkpseempl edckeacsqs srltglqdis
      961 igkkchkcsi cgktfnkssq lishkrfhtr erpfkcskcg ktfrwssnla rhmknhird
//
LOCUS       NP_001347368             511 aa            linear   ROD 27-APR-2025
DEFINITION  DNA cross-link repair 1A protein isoform 3 [Mus musculus].
ACCESSION   NP_001347368 XP_006527281
VERSION     NP_001347368.1
DBSOURCE    REFSEQ: accession NM_001360439.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Yan,Y., Akhter,S., Zhang,X. and Legerski,R.
  TITLE     The multifunctional SNM1 gene family: not just nucleases
  JOURNAL   Future Oncol 6 (6), 1015-1029 (2010)
   PUBMED   20528238
  REMARK    Review article
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Akhter,S. and Legerski,R.J.
  TITLE     SNM1A acts downstream of ATM to promote the G1 cell cycle
            checkpoint
  JOURNAL   Biochem Biophys Res Commun 377 (1), 236-241 (2008)
   PUBMED   18848520
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Hemphill,A.W., Bruun,D., Thrun,L., Akkari,Y., Torimaru,Y.,
            Hejna,K., Jakobs,P.M., Hejna,J., Jones,S., Olson,S.B. and
            Moses,R.E.
  TITLE     Mammalian SNM1 is required for genome stability
  JOURNAL   Mol Genet Metab 94 (1), 38-45 (2008)
   PUBMED   18180189
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Ahkter,S., Richie,C.T., Zhang,N., Behringer,R.R., Zhu,C. and
            Legerski,R.J.
  TITLE     Snm1-deficient mice exhibit accelerated tumorigenesis and
            susceptibility to infection
  JOURNAL   Mol Cell Biol 25 (22), 10071-10078 (2005)
   PUBMED   16260620
  REMARK    GeneRIF: Snm1 is a tumor suppressor in mice that in addition has a
            role in immunity
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Bonatto,D., Revers,L.F., Brendel,M. and Henriques,J.A.
  TITLE     The eukaryotic Pso2/Snm1/Artemis proteins and their function as
            genomic and cellular caretakers
  JOURNAL   Braz J Med Biol Res 38 (3), 321-334 (2005)
   PUBMED   15761611
  REMARK    Review article
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Akhter,S., Richie,C.T., Deng,J.M., Brey,E., Zhang,X., Patrick,C.
            Jr., Behringer,R.R. and Legerski,R.J.
  TITLE     Deficiency in SNM1 abolishes an early mitotic checkpoint induced by
            spindle stress
  JOURNAL   Mol Cell Biol 24 (23), 10448-10455 (2004)
   PUBMED   15542852
  REMARK    GeneRIF: Snm1 and 53BP1 are components of a mitotic stress
            checkpoint that negatively targets the APC prior to chromosome
            condensation
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Dronkert,M.L., de Wit,J., Boeve,M., Vasconcelos,M.L., van Steeg,H.,
            Tan,T.L., Hoeijmakers,J.H. and Kanaar,R.
  TITLE     Disruption of mouse SNM1 causes increased sensitivity to the DNA
            interstrand cross-linking agent mitomycin C
  JOURNAL   Mol Cell Biol 20 (13), 4553-4561 (2000)
   PUBMED   10848582
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC166746.7.
            
            On Feb 3, 2018 this sequence version replaced XP_006527281.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6116558.123592.1,
                                           SRR1660821.32962.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164143 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 51.89 cM"
     Protein         1..511
                     /product="DNA cross-link repair 1A protein isoform 3"
                     /EC_number="3.5.2.6"
                     /note="DNA cross-link repair 1A protein; SNM1 homolog A;
                     DNA cross-link repair 1A, PSO2 homolog; beta-lactamase
                     MBLAC2"
                     /calculated_mol_wt=57295
     Region          160..315
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
     Site            order(203,205,207..208,264..265,286,309)
                     /site_type="active"
                     /db_xref="CDD:293792"
     Region          385..491
                     /region_name="DRMBL"
                     /note="DNA repair metallo-beta-lactamase; pfam07522"
                     /db_xref="CDD:429512"
     CDS             1..511
                     /gene="Dclre1a"
                     /gene_synonym="2810043H12Rik; mKIAA0086; Pso2; Smn1a;
                     Snm1"
                     /coded_by="NM_001360439.1:1572..3107"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:55947"
                     /db_xref="MGI:MGI:1930042"
ORIGIN      
        1 mpldkplgts psspkcspsq pskkvmkqmd igvffglppk rqetslresa segpnvspvv
       61 spnqkrprlc krkaqsslsd lefdaknlne sqhsvglsge krqhrrkrhk tsnspregpc
      121 qrrsghlmnn pelgpvilsk gkafvrrtrg rtqrgnmnis essgagevrr tcpfykripg
      181 tgftvdafqy geiegctayf lthfhsdhya glskdftrpv ycseitgnll kkklrvqeqy
      241 irqlpmdtec vvdsvkvvll danhcpgatm ilfqlpngav ilhtgdfrad psmersrlag
      301 rkvhtlfldt tycspeytfp sqqeviqfai ntafeavtln pralvvcgty cigkekvfla
      361 iadvlgskvg msqekyktlq clnipevssl ittdmcdslv hllpmmqinf kglqshlkkc
      421 ggkydqilaf rptgwthsnn itstadiipq trgnisiygi pysehssyle mkrfvqwlkp
      481 qkiiptvnvg sfrsrntmek yfkewrleag y
//
LOCUS       NP_808816                379 aa            linear   PRI 27-APR-2025
DEFINITION  armadillo repeat-containing X-linked protein 3 [Homo sapiens].
ACCESSION   NP_808816
VERSION     NP_808816.1
DBSOURCE    REFSEQ: accession NM_177947.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Du,J., Zhang,X., Zhou,H., Miao,Y., Han,Y., Han,Q. and Wang,E.
  TITLE     Alex3 suppresses non-small cell lung cancer invasion via
            AKT/Slug/E-cadherin pathway
  JOURNAL   Tumour Biol 39 (7), 1010428317701441 (2017)
   PUBMED   28705116
  REMARK    GeneRIF: reduction of Alex3 correlates with the development of
            non-small cell lung cancer and predicts adverse clinical outcome of
            non-small cell lung cancer patients. The effect of Alex3 on
            inhibiting invasion and migration may attribute to upregulation of
            E-cadherin expression through AKT-Slug pathway inactivation.
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Winter,E.E. and Ponting,C.P.
  TITLE     Mammalian BEX, WEX and GASP genes: coding and non-coding chimaerism
            sustained by gene conversion events
  JOURNAL   BMC Evol Biol 5, 54 (2005)
   PUBMED   16221301
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 379)
  AUTHORS   Ross,M.T., Grafham,D.V., Coffey,A.J., Scherer,S., McLay,K.,
            Muzny,D., Platzer,M., Howell,G.R., Burrows,C., Bird,C.P.,
            Frankish,A., Lovell,F.L., Howe,K.L., Ashurst,J.L., Fulton,R.S.,
            Sudbrak,R., Wen,G., Jones,M.C., Hurles,M.E., Andrews,T.D.,
            Scott,C.E., Searle,S., Ramser,J., Whittaker,A., Deadman,R.,
            Carter,N.P., Hunt,S.E., Chen,R., Cree,A., Gunaratne,P., Havlak,P.,
            Hodgson,A., Metzker,M.L., Richards,S., Scott,G., Steffen,D.,
            Sodergren,E., Wheeler,D.A., Worley,K.C., Ainscough,R.,
            Ambrose,K.D., Ansari-Lari,M.A., Aradhya,S., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Ballabio,A., Banerjee,R., Barker,G.E.,
            Barlow,K.F., Barrett,I.P., Bates,K.N., Beare,D.M., Beasley,H.,
            Beasley,O., Beck,A., Bethel,G., Blechschmidt,K., Brady,N.,
            Bray-Allen,S., Bridgeman,A.M., Brown,A.J., Brown,M.J., Bonnin,D.,
            Bruford,E.A., Buhay,C., Burch,P., Burford,D., Burgess,J.,
            Burrill,W., Burton,J., Bye,J.M., Carder,C., Carrel,L., Chako,J.,
            Chapman,J.C., Chavez,D., Chen,E., Chen,G., Chen,Y., Chen,Z.,
            Chinault,C., Ciccodicola,A., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S., Clerc-Blankenburg,K., Clifford,K., Cobley,V., Cole,C.G.,
            Conquer,J.S., Corby,N., Connor,R.E., David,R., Davies,J., Davis,C.,
            Davis,J., Delgado,O., Deshazo,D., Dhami,P., Ding,Y., Dinh,H.,
            Dodsworth,S., Draper,H., Dugan-Rocha,S., Dunham,A., Dunn,M.,
            Durbin,K.J., Dutta,I., Eades,T., Ellwood,M., Emery-Cohen,A.,
            Errington,H., Evans,K.L., Faulkner,L., Francis,F., Frankland,J.,
            Fraser,A.E., Galgoczy,P., Gilbert,J., Gill,R., Glockner,G.,
            Gregory,S.G., Gribble,S., Griffiths,C., Grocock,R., Gu,Y.,
            Gwilliam,R., Hamilton,C., Hart,E.A., Hawes,A., Heath,P.D.,
            Heitmann,K., Hennig,S., Hernandez,J., Hinzmann,B., Ho,S., Hoffs,M.,
            Howden,P.J., Huckle,E.J., Hume,J., Hunt,P.J., Hunt,A.R.,
            Isherwood,J., Jacob,L., Johnson,D., Jones,S., de Jong,P.J.,
            Joseph,S.S., Keenan,S., Kelly,S., Kershaw,J.K., Khan,Z.,
            Kioschis,P., Klages,S., Knights,A.J., Kosiura,A., Kovar-Smith,C.,
            Laird,G.K., Langford,C., Lawlor,S., Leversha,M., Lewis,L., Liu,W.,
            Lloyd,C., Lloyd,D.M., Loulseged,H., Loveland,J.E., Lovell,J.D.,
            Lozado,R., Lu,J., Lyne,R., Ma,J., Maheshwari,M., Matthews,L.H.,
            McDowall,J., McLaren,S., McMurray,A., Meidl,P., Meitinger,T.,
            Milne,S., Miner,G., Mistry,S.L., Morgan,M., Morris,S., Muller,I.,
            Mullikin,J.C., Nguyen,N., Nordsiek,G., Nyakatura,G., O'Dell,C.N.,
            Okwuonu,G., Palmer,S., Pandian,R., Parker,D., Parrish,J.,
            Pasternak,S., Patel,D., Pearce,A.V., Pearson,D.M., Pelan,S.E.,
            Perez,L., Porter,K.M., Ramsey,Y., Reichwald,K., Rhodes,S.,
            Ridler,K.A., Schlessinger,D., Schueler,M.G., Sehra,H.K.,
            Shaw-Smith,C., Shen,H., Sheridan,E.M., Shownkeen,R., Skuce,C.D.,
            Smith,M.L., Sotheran,E.C., Steingruber,H.E., Steward,C.A.,
            Storey,R., Swann,R.M., Swarbreck,D., Tabor,P.E., Taudien,S.,
            Taylor,T., Teague,B., Thomas,K., Thorpe,A., Timms,K., Tracey,A.,
            Trevanion,S., Tromans,A.C., d'Urso,M., Verduzco,D., Villasana,D.,
            Waldron,L., Wall,M., Wang,Q., Warren,J., Warry,G.L., Wei,X.,
            West,A., Whitehead,S.L., Whiteley,M.N., Wilkinson,J.E.,
            Willey,D.L., Williams,G., Williams,L., Williamson,A.,
            Williamson,H., Wilming,L., Woodmansey,R.L., Wray,P.W., Yen,J.,
            Zhang,J., Zhou,J., Zoghbi,H., Zorilla,S., Buck,D., Reinhardt,R.,
            Poustka,A., Rosenthal,A., Lehrach,H., Meindl,A., Minx,P.J.,
            Hillier,L.W., Willard,H.F., Wilson,R.K., Waterston,R.H., Rice,C.M.,
            Vaudin,M., Coulson,A., Nelson,D.L., Weinstock,G., Sulston,J.E.,
            Durbin,R., Hubbard,T., Gibbs,R.A., Beck,S., Rogers,J. and
            Bentley,D.R.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
REFERENCE   8  (residues 1 to 379)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 379)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 379)
  AUTHORS   Kurochkin,I.V., Yonemitsu,N., Funahashi,S.I. and Nomura,H.
  TITLE     ALEX1, a novel human armadillo repeat protein that is expressed
            differentially in normal tissues and carcinomas
  JOURNAL   Biochem Biophys Res Commun 280 (1), 340-347 (2001)
   PUBMED   11162520
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG035798.1, BC005194.1,
            BX647802.1 and AC234775.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the ALEX family of proteins
            which may play a role in tumor suppression. The encoded protein
            contains a potential N-terminal transmembrane domain and a single
            Armadillo (arm) repeat. Other proteins containing the arm repeat
            are involved in development, maintenance of tissue integrity, and
            tumorigenesis. This gene is closely localized with other family
            members on the X chromosome. Three transcript variants encoding the
            same protein have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC005194.1, SRR1803613.187618.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000471229.7/ ENSP00000454483.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..379
                     /product="armadillo repeat-containing X-linked protein 3"
                     /note="arm protein lost in epithelial cancers, X
                     chromosome, 3; ARM protein lost in epithelial cancers on
                     chromosome X 3"
                     /calculated_mol_wt=42370
     Region          1..6
                     /region_name="Mitochondrion outer membrane (MOM)-targeting
                     sequence. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH62.1)"
     Site            7..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH62.1)"
     Region          26..37
                     /region_name="Mitochondrion outer membrane (MOM)-targeting
                     sequence. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH62.1)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UH62.1)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q9UH62.1)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UH62.1)"
     Region          89..98
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q8BHS6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH62.1)"
     Region          95..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH62.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UH62.1)"
     Region          111..151
                     /region_name="ARM 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH62.1)"
     Region          118..338
                     /region_name="Arm_2"
                     /note="Armadillo-like; pfam04826"
                     /db_xref="CDD:461447"
     Region          153..192
                     /region_name="ARM 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH62.1)"
     Region          156..190
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          233..272
                     /region_name="ARM 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH62.1)"
     CDS             1..379
                     /gene="ARMCX3"
                     /gene_synonym="ALEX3; dJ545K15.2; GASP6"
                     /coded_by="NM_177947.3:485..1624"
                     /db_xref="CCDS:CCDS14489.1"
                     /db_xref="GeneID:51566"
                     /db_xref="HGNC:HGNC:24065"
                     /db_xref="MIM:300364"
ORIGIN      
        1 mgyarkvgwv taglvigaga cyciyrltrg rkqnkekmae ggsgdvddag dcsgaryndw
       61 sdddddsnes ksivwyppwa rigteagtra rarararatr arravqkras pnsddtvlsp
      121 qelqkvlclv emsekpyile aalialgnna ayafnrdiir dlgglpivak ilntrdpivk
      181 ekalivlnnl svnaenqrrl kvymnqvcdd titsrlnssv qlaglrlltn mtvtneyqhm
      241 lansisdffr lfsagneetk lqvlklllnl aenpamtrel lraqvpsslg slfnkkenke
      301 vilkllvife nindnfkwee neptqnqfge gslffflkef qvcadkvlgi eshhdflvkv
      361 kvgkfmakla ehmfpksqe
//
LOCUS       NP_065641                212 aa            linear   ROD 27-APR-2025
DEFINITION  A-kinase-interacting protein 1 [Mus musculus].
ACCESSION   NP_065641
VERSION     NP_065641.1
DBSOURCE    REFSEQ: accession NM_020616.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nijholt,K.T., Sanchez-Aguilera,P.I., Mahmoud,B., Gerding,A.,
            Wolters,J.C., Wolters,A.H.G., Giepmans,B.N.G., Sillje,H.H.W., de
            Boer,R.A., Bakker,B.M. and Westenbrink,B.D.
  TITLE     A Kinase Interacting Protein 1 regulates mitochondrial protein
            levels in energy metabolism and promotes mitochondrial turnover
            after exercise
  JOURNAL   Sci Rep 13 (1), 18822 (2023)
   PUBMED   37914850
  REMARK    GeneRIF: A Kinase Interacting Protein 1 regulates mitochondrial
            protein levels in energy metabolism and promotes mitochondrial
            turnover after exercise.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Nijholt,K.T., Sanchez-Aguilera,P.I., Booij,H.G.,
            Oberdorf-Maass,S.U., Dokter,M.M., Wolters,A.H.G., Giepmans,B.N.G.,
            van Gilst,W.H., Brown,J.H., de Boer,R.A., Sillje,H.H.W. and
            Westenbrink,B.D.
  TITLE     A Kinase Interacting Protein 1 (AKIP1) promotes cardiomyocyte
            elongation and physiological cardiac remodelling
  JOURNAL   Sci Rep 13 (1), 4046 (2023)
   PUBMED   36899057
  REMARK    GeneRIF: A Kinase Interacting Protein 1 (AKIP1) promotes
            cardiomyocyte elongation and physiological cardiac remodelling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zhu,L., Gao,T., Huang,Y., Jin,J., Wang,D., Zhang,L., Jin,Y., Li,P.,
            Hu,Y., Wu,Y., Liu,H., Dong,Q., Wang,G., Zheng,T., Song,C., Bai,Y.,
            Zhang,X., Liu,Y., Yang,W., Xu,K., Zou,G., Zhao,L., Cao,R.,
            Zhong,W., Xia,X., Xiao,G., Liu,X. and Cao,C.
  TITLE     Ebola virus VP35 hijacks the PKA-CREB1 pathway for replication and
            pathogenesis by AKIP1 association
  JOURNAL   Nat Commun 13 (1), 2256 (2022)
   PUBMED   35474062
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Tian,Z.Q., Jiang,H. and Lu,Z.B.
  TITLE     MiR-320 regulates cardiomyocyte apoptosis induced by
            ischemia-reperfusion injury by targeting AKIP1
  JOURNAL   Cell Mol Biol Lett 23, 41 (2018)
   PUBMED   30181740
  REMARK    GeneRIF: miR-320 plays an important role in regulating
            cardiomyocyte apoptosis induced by ischemia-reperfusion injury by
            targeting AKIP1 and inducing the mitochondrial apoptotic pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 212)
  AUTHORS   Sastri,M., Haushalter,K.J., Panneerselvam,M., Chang,P.,
            Fridolfsson,H., Finley,J.C., Ng,D., Schilling,J.M., Miyanohara,A.,
            Day,M.E., Hakozaki,H., Petrosyan,S., Koller,A., King,C.C.,
            Darshi,M., Blumenthal,D.K., Ali,S.S., Roth,D.M., Patel,H.H. and
            Taylor,S.S.
  TITLE     A kinase interacting protein (AKIP1) is a key regulator of cardiac
            stress
  JOURNAL   Proc Natl Acad Sci U S A 110 (5), E387-E396 (2013)
   PUBMED   23319652
  REMARK    GeneRIF: Data indicate A-kinase interacting protein 1 (AKIP1) as a
            critical molecular regulator and a therapeutic control point for
            stress adaptation in the heart.
REFERENCE   7  (residues 1 to 212)
  AUTHORS   Yu,K.P., Itokawa,T., Zhu,M.L., Syam,S., Seth,A. and Insogna,K.
  TITLE     Breast cancer-associated gene 3 (BCA3) is a novel Rac1-interacting
            protein
  JOURNAL   J Bone Miner Res 22 (4), 628-637 (2007)
   PUBMED   17227220
REFERENCE   8  (residues 1 to 212)
  AUTHORS   Sastri,M., Barraclough,D.M., Carmichael,P.T. and Taylor,S.S.
  TITLE     A-kinase-interacting protein localizes protein kinase A in the
            nucleus
  JOURNAL   Proc Natl Acad Sci U S A 102 (2), 349-354 (2005)
   PUBMED   15630084
REFERENCE   9  (residues 1 to 212)
  AUTHORS   Kitching,R., Li,H., Wong,M.J., Kanaganayakam,S., Kahn,H. and
            Seth,A.
  TITLE     Characterization of a novel human breast cancer associated gene
            (BCA3) encoding an alternatively spliced proline-rich protein
  JOURNAL   Biochim Biophys Acta 1625 (1), 116-121 (2003)
   PUBMED   12527432
REFERENCE   10 (residues 1 to 212)
  AUTHORS   Amid,C., Bahr,A., Mujica,A., Sampson,N., Bikar,S.E.,
            Winterpacht,A., Zabel,B., Hankeln,T. and Schmidt,E.R.
  TITLE     Comparative genomic sequencing reveals a strikingly similar
            architecture of a conserved syntenic region on human chromosome
            11p15.3 (including gene ST5) and mouse chromosome 7
  JOURNAL   Cytogenet Cell Genet 93 (3-4), 284-290 (2001)
   PUBMED   11528127
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132584.5 and AK163012.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK163012.1, SRR7345562.4945475.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 57.44 cM"
     Protein         1..212
                     /product="A-kinase-interacting protein 1"
                     /note="proline-rich protein BCA3; PKA-interacting protein;
                     breast cancer-associated gene 3 protein; A kinase (PRKA)
                     interacting protein 1"
                     /calculated_mol_wt=23848
     CDS             1..212
                     /gene="Akip1"
                     /gene_synonym="BCA3; C11orf17; D7H11orf17; D930014E17Rik;
                     ICRFP703B1614Q5.6; ORF27"
                     /coded_by="NM_020616.2:106..744"
                     /db_xref="CCDS:CCDS21736.1"
                     /db_xref="GeneID:57373"
                     /db_xref="MGI:MGI:3041226"
ORIGIN      
        1 meyclaaaal ngvdrrslqr sarlgrevle rakrravdwh spersrgnvg vlyrqgpyqe
       61 rwsvpgsqrl lgereercpt lsssfgamae fmdytssqcg kyylsmpeeg gathvyryhr
      121 rkppemhmys dtghsqeqrn crgetsvgqe siyqtsehsq esswptenis kdlyievypg
      181 tysvtvgssa lskkthvvav dpgqsvdlvf pv
//
LOCUS       NP_001357411             319 aa            linear   PRI 27-APR-2025
DEFINITION  olfactory receptor 7A5 [Homo sapiens].
ACCESSION   NP_001357411 XP_011526215
VERSION     NP_001357411.1
DBSOURCE    REFSEQ: accession NM_001370482.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Malnic,B., Godfrey,P.A. and Buck,L.B.
  TITLE     The human olfactory receptor gene family
  JOURNAL   Proc Natl Acad Sci U S A 101 (8), 2584-2589 (2004)
   PUBMED   14983052
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 May 4;101(18):7205]
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Fuchs,T., Malecova,B., Linhart,C., Sharan,R., Khen,M., Herwig,R.,
            Shmulevich,D., Elkon,R., Steinfath,M., O'Brien,J.K., Radelof,U.,
            Lehrach,H., Lancet,D. and Shamir,R.
  TITLE     DEFOG: a practical scheme for deciphering families of genes
  JOURNAL   Genomics 80 (3), 295-302 (2002)
   PUBMED   12213199
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Vanderhaeghen,P., Schurmans,S., Vassart,G. and Parmentier,M.
  TITLE     Molecular cloning and chromosomal mapping of olfactory receptor
            genes expressed in the male germ line: evidence for their wide
            distribution in the human genome
  JOURNAL   Biochem Biophys Res Commun 237 (2), 283-287 (1997)
   PUBMED   9268701
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Vanderhaeghen,P., Schurmans,S., Vassart,G. and Parmentier,M.
  TITLE     Specific repertoire of olfactory receptor genes in the male germ
            cells of several mammalian species
  JOURNAL   Genomics 39 (3), 239-246 (1997)
   PUBMED   9119360
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Parmentier,M., Libert,F., Schurmans,S., Schiffmann,S., Lefort,A.,
            Eggerickx,D., Ledent,C., Mollereau,C., Gerard,C., Perret,J. et al.
  TITLE     Expression of members of the putative olfactory receptor gene
            family in mammalian germ cells
  JOURNAL   Nature 355 (6359), 453-455 (1992)
   PUBMED   1370859
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005255.1.
            
            On May 8, 2019 this sequence version replaced XP_011526215.1.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.11824.1,
                                           SRR1660807.30987.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..319
                     /product="olfactory receptor 7A5"
                     /note="olfactory receptor, family 7, subfamily A, member 5
                     pseudogene; olfactory receptor OR19-17; olfactory receptor
                     TPCR92"
                     /calculated_mol_wt=35448
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15622.2)"
     Region          25..301
                     /region_name="7tmA_OR7-like"
                     /note="olfactory receptor family 7 and related proteins,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15234"
                     /db_xref="CDD:320362"
     Region          26..52
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320362"
     Site            26..46
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15622.2)"
     Site            55..75
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15622.2)"
     Region          59..85
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320362"
     Site            order(81,84..85,97..102,104..105,108,153,155..159,195,
                     198..200,202..204,206..207,252,255..256,258..259,262,
                     268..269,271..273,276,279..280)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320362"
     Region          97..127
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320362"
     Site            100..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15622.2)"
     Region          140..161
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320362"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15622.2)"
     Region          195..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320362"
     Site            198..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15622.2)"
     Region          232..262
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320362"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15622.2)"
     Region          269..294
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320362"
     Site            272..292
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15622.2)"
     CDS             1..319
                     /gene="OR7A5"
                     /gene_synonym="HTPCR2"
                     /coded_by="NM_001370482.1:287..1246"
                     /db_xref="CCDS:CCDS12318.1"
                     /db_xref="GeneID:26659"
                     /db_xref="HGNC:HGNC:8368"
ORIGIN      
        1 mepgndtqis eflllgfsqe pglqpflfgl flsmylvtvl gnlliilati sdshlhtpmy
       61 fflsnlsfad icvtsttipk mlmniqtqnk vityiaclmq myffilfagf enfllsvmay
      121 drfvaichpl hymvimnphl cgllvlaswt msalysllqi lmvvrlsfct aleiphffce
      181 lnqviqlacs dsflnhmviy ftvallgggp ltgilysysk iissihaiss aqgkykafst
      241 cashlsvvsl fygailgvyl ssaatrnshs satasvmytv vtpmlnpfiy slrnkdikra
      301 lgihllwgtm kgqffkkcp
//
LOCUS       NP_001138747             724 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger Y-chromosomal protein isoform 2 [Homo sapiens].
ACCESSION   NP_001138747 XP_001713744
VERSION     NP_001138747.1
DBSOURCE    REFSEQ: accession NM_001145275.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Ni,W., Perez,A.A., Schreiner,S., Nicolet,C.M. and Farnham,P.J.
  TITLE     Characterization of the ZFX family of transcription factors that
            bind downstream of the start site of CpG island promoters
  JOURNAL   Nucleic Acids Res 48 (11), 5986-6000 (2020)
   PUBMED   32406922
  REMARK    GeneRIF: Characterization of the ZFX family of transcription
            factors that bind downstream of the start site of CpG island
            promoters.
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Decarpentrie,F., Vernet,N., Mahadevaiah,S.K., Longepied,G.,
            Streichemberger,E., Aknin-Seifer,I., Ojarikre,O.A., Burgoyne,P.S.,
            Metzler-Guillemain,C. and Mitchell,M.J.
  TITLE     Human and mouse ZFY genes produce a conserved testis-specific
            transcript encoding a zinc finger protein with a short acidic
            domain and modified transactivation potential
  JOURNAL   Hum Mol Genet 21 (12), 2631-2645 (2012)
   PUBMED   22407129
  REMARK    GeneRIF: Studies identified a major testis-specific ZFY transcript
            that encodes a protein with the same short acidic domain.
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 724)
  AUTHORS   Tricoli,J.V. and Bracken,R.B.
  TITLE     ZFY gene expression and retention in human prostate adenocarcinoma
  JOURNAL   Genes Chromosomes Cancer 6 (2), 65-72 (1993)
   PUBMED   7680890
REFERENCE   7  (residues 1 to 724)
  AUTHORS   Kochoyan,M., Keutmann,H.T. and Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            refinement of the NMR structure of an even finger by selective
            deuterium labeling and implications for DNA recognition
  JOURNAL   Biochemistry 30 (29), 7063-7072 (1991)
   PUBMED   1854720
REFERENCE   8  (residues 1 to 724)
  AUTHORS   North,M., Sargent,C., O'Brien,J., Taylor,K., Wolfe,J., Affara,N.A.
            and Ferguson-Smith,M.A.
  TITLE     Comparison of ZFY and ZFX gene structure and analysis of
            alternative 3' untranslated regions of ZFY
  JOURNAL   Nucleic Acids Res 19 (10), 2579-2586 (1991)
   PUBMED   2041734
REFERENCE   9  (residues 1 to 724)
  AUTHORS   Kochoyan,M., Havel,T.F., Nguyen,D.T., Dahl,C.E., Keutmann,H.T. and
            Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            2D NMR structure of an even finger and implications for
            'jumping-linker' DNA recognition
  JOURNAL   Biochemistry 30 (14), 3371-3386 (1991)
   PUBMED   1849423
REFERENCE   10 (residues 1 to 724)
  AUTHORS   Palmer,M.S., Berta,P., Sinclair,A.H., Pym,B. and Goodfellow,P.N.
  TITLE     Comparison of human ZFY and ZFX transcripts
  JOURNAL   Proc Natl Acad Sci U S A 87 (5), 1681-1685 (1990)
   PUBMED   2308929
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006157.2.
            
            On Feb 20, 2009 this sequence version replaced XP_001713744.1.
            
            Summary: This gene encodes a zinc finger-containing protein that
            may function as a transcription factor. This gene was once a
            candidate gene for the testis-determining factor (TDF) and was
            erroneously referred to as TDF. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.177748.1, BC114526.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144335, SAMEA2149398
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yp11.2"
     Protein         1..724
                     /product="zinc finger Y-chromosomal protein isoform 2"
                     /note="zinc finger Y-chromosomal protein"
                     /calculated_mol_wt=82034
     Region          45..329
                     /region_name="Zfx_Zfy_act"
                     /note="Zfx / Zfy transcription activation region;
                     pfam04704"
                     /db_xref="CDD:461400"
     Region          <340..515
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          <346..>368
                     /region_name="ROS_MUCR"
                     /note="ROS/MUCR transcriptional regulator protein;
                     cl19880"
                     /db_xref="CDD:473244"
     Region          346..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          377..401
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          409..429
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(414,416,418,420..421,424..425,428,474,476,480..481,
                     484..485,488,502,504,506,508..509,512..513,516)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          462..>599
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          481..505
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          497..516
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          526..575
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          583..603
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          638..660
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          640..660
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(645,647,649,651..652,655..656,659,673,675,679..680,
                     683..684,688,702,704,706,708..709,712..713,716)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          652..676
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          668..689
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          697..717
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..724
                     /gene="ZFY"
                     /gene_synonym="ZNF911"
                     /coded_by="NM_001145275.2:407..2581"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS48201.1"
                     /db_xref="GeneID:7544"
                     /db_xref="HGNC:HGNC:12870"
                     /db_xref="MIM:490000"
ORIGIN      
        1 mdgdqivvei qeavfvsniv dsditvhnfv pddpdsvviq dvvedvviee dvqcsdilee
       61 advsenviip eqvldsdvte evslphctvp ddvlasdits tsmsmpehvl tsesmhvcdi
      121 ghvehmvhds vveaeiitdp ltsdivseev lvadcapeav idasgisvdq qdndkasced
      181 ylmislddag kiehdgstgv tidaesemdp ckvdstcpev ikvyifkadp geddlggtvd
      241 ivesependh gvelldqnss irvprekmvy mtvndsqqed edlsnnsdgi enrngtasal
      301 lhidesaglg rlakqkpkkk rrpdsrqyqt aiiigpdghp ltvypcmicg kkfksrgflk
      361 rhmknhpehl akkkyhctdc dyttnkkisl hnhleshklt skaekaiecd ecgkhfshag
      421 alfthkmvhk ekgankmhkc kfceyetaeq gllnrhllav hsknfphicv ecgkgfrhps
      481 elrkhmriht gekpyqcqyc eyrsadssnl kthiktkhsk empfkcdicl ltfsdtkevq
      541 qhtlvhqesk thqclhcdhk ssnssdlkrh visvhtkdyp hkcemcekgf hrpselkkhv
      601 avhkgkkmhq crhcdfkiad pfvlsrhils vhtkdlpfrc krcrkgfrqq nelkkhmkth
      661 sgrkvyqcey ceysttdasg fkrhvisiht kdyphrceyc kkgfrrpsek nqhimrhhke
      721 vglp
//
LOCUS       NP_775935                244 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-ribosylation factor-like protein 10 isoform 2 [Homo sapiens].
ACCESSION   NP_775935
VERSION     NP_775935.1
DBSOURCE    REFSEQ: accession NM_173664.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Louro,R., Nakaya,H.I., Paquola,A.C., Martins,E.A., da Silva,A.M.,
            Verjovski-Almeida,S. and Reis,E.M.
  TITLE     RASL11A, member of a novel small monomeric GTPase gene family, is
            down-regulated in prostate tumors
  JOURNAL   Biochem Biophys Res Commun 316 (3), 618-627 (2004)
   PUBMED   15033445
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC059361.1, DR001833.1 and AC138956.3.
            
            Transcript Variant: This variant (2) differs in the 3' coding
            region and 3' UTR compared to variant 1. The encoded isoform (2)
            has a distinct, shorter C-terminus than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.253546.1,
                                           SRR1803612.70474.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310389.6/ ENSP00000308496.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..244
                     /product="ADP-ribosylation factor-like protein 10 isoform
                     2"
                     /note="ADP-ribosylation factor-like 10A; ADP-ribosylation
                     factor-like protein 10; ADP-ribosylation factor-like
                     membrane-associated protein; ADP ribosylation factor like
                     GTPase 10"
                     /calculated_mol_wt=27328
     Region          79..237
                     /region_name="Arl9_Arfrp2_like"
                     /note="Arf-like 9 (Arl9)/Arfrp2-like GTPase; cd04162"
                     /db_xref="CDD:133362"
     Site            84..91
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133362"
     Site            order(86..92,108..109,131,185..186,188,219..221)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133362"
     Site            order(86..87,91,95,108..115,137,142)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133362"
     Site            order(96..99,102..112)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133362"
     Site            order(109..113,118,128,132,138,140..142)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133362"
     Site            109
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133362"
     Site            order(110..117,127,138,141..142)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133362"
     Site            order(113..119,122..127)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:133362"
     Site            128..145
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133362"
     Site            128..131
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133362"
     Site            185..188
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133362"
     Site            219..221
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133362"
     CDS             1..244
                     /gene="ARL10"
                     /gene_synonym="ARL10A"
                     /coded_by="NM_173664.6:78..812"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4400.1"
                     /db_xref="GeneID:285598"
                     /db_xref="HGNC:HGNC:22042"
ORIGIN      
        1 maprplgplv lalggaaavl gsvlfilwkt yfgrgrerrw drgeawwgae aarlpewdew
       61 dpedeedeep aleeleqrev lvlgldgagk stflrvlsgk ppleghiptw gfnsvrlptk
      121 dfevdlleig gsqnlrfywk efvsevdvlv fvvdsadrlr lpwarqelhk lldkdpdlpv
      181 vvvankqdls eamsmgelqr elglqaidnq revfllaasi apagptfeep gtvhiwklll
      241 ells
//
LOCUS       NP_071335                531 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear RNA export factor 3 [Homo sapiens].
ACCESSION   NP_071335
VERSION     NP_071335.1
DBSOURCE    REFSEQ: accession NM_022052.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Zeng,T., Wang,D., Chen,J., Chen,K., Yu,G., Chen,Q., Liu,Y., Yan,S.,
            Zhu,L., Zhou,H., Huang,A. and Tang,H.
  TITLE     AF119895 regulates NXF3 expression to promote migration and
            invasion of hepatocellular carcinoma through an interaction with
            miR-6508-3p
  JOURNAL   Exp Cell Res 363 (1), 129-139 (2018)
   PUBMED   29274323
  REMARK    GeneRIF: observations collectively demonstrate that AF119895
            modulates the repression of NXF3 by binding to miR-6508-3p
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Jun,L., Frints,S., Duhamel,H., Herold,A., Abad-Rodrigues,J.,
            Dotti,C., Izaurralde,E., Marynen,P. and Froyen,G.
  TITLE     NXF5, a novel member of the nuclear RNA export factor family, is
            lost in a male patient with a syndromic form of mental retardation
  JOURNAL   Curr Biol 11 (18), 1381-1391 (2001)
   PUBMED   11566096
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Yang,J., Bogerd,H.P., Wang,P.J., Page,D.C. and Cullen,B.R.
  TITLE     Two closely related human nuclear export factors utilize entirely
            distinct export pathways
  JOURNAL   Mol Cell 8 (2), 397-406 (2001)
   PUBMED   11545741
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Herold,A., Suyama,M., Rodrigues,J.P., Braun,I.C., Kutay,U.,
            Carmo-Fonseca,M., Bork,P. and Izaurralde,E.
  TITLE     TAP (NXF1) belongs to a multigene family of putative RNA export
            factors with a conserved modular architecture
  JOURNAL   Mol Cell Biol 20 (23), 8996-9008 (2000)
   PUBMED   11073998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z75746.1 and AJ277527.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is one member of a family of nuclear RNA export
            factor genes. Common domain features of this family are a
            noncanonical RNP-type RNA-binding domain (RBD), 4 leucine-rich
            repeats (LRRs), a nuclear transport factor 2 (NTF2)-like domain
            that allows heterodimerization with NTF2-related export protein-1
            (NXT1), and a ubiquitin-associated domain that mediates
            interactions with nucleoporins. The LRRs and NTF2-like domains are
            required for export activity. Alternative splicing seems to be a
            common mechanism in this gene family. The encoded protein of this
            gene has shortened LRR and ubiquitin-associated domains and its RDB
            is unable to bind RNA. It is located in the nucleoplasm but is not
            associated with either the nuclear envelope or the nucleolus.
            [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF346619.1, AJ277527.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395065.8/ ENSP00000378504.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..531
                     /product="nuclear RNA export factor 3"
                     /note="TAPL-3; TAP-like protein 3"
                     /calculated_mol_wt=59971
     Region          33..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4D5.1)"
     Region          83..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4D5.1)"
     Region          113..192
                     /region_name="Tap-RNA_bind"
                     /note="Tap, RNA-binding; pfam09162"
                     /db_xref="CDD:462696"
     Region          115..192
                     /region_name="noncanonical RNP-type RNA-binding (RBD)
                     domain"
     Region          193..329
                     /region_name="leucine-rich repeat (LRR) domains"
     Region          218..260
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275382"
     Region          275..305
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275382"
     Region          339..461
                     /region_name="nuclear transport factor 2 (NTF2)-like
                     domain"
     Region          341..496
                     /region_name="NTF2"
                     /note="Nuclear transport factor 2 (NTF2) domain plays an
                     important role in the trafficking of macromolecules, ions
                     and small molecules between the cytoplasm and nucleus.
                     This bi-directional transport of macromolecules across the
                     nuclear envelope requires many...; cd00780"
                     /db_xref="CDD:238403"
     Site            order(369,375,415,440,442..443,452,478,489..491,493,495)
                     /site_type="active"
                     /note="TAP/p15 interaction [active]"
                     /db_xref="CDD:238403"
     Site            order(373,375..376,435..436,440,442..443,450,454..456,460,
                     466..469,472,478,489..491,493..496)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238403"
     Site            order(376..377,427,430,455,457,459..460,466,469,492,494,
                     496)
                     /site_type="active"
                     /note="RanGDP-NTF2 interaction [active]"
                     /db_xref="CDD:238403"
     Region          524..531
                     /region_name="ubiquitin-associated domain"
     CDS             1..531
                     /gene="NXF3"
                     /coded_by="NM_022052.2:121..1716"
                     /db_xref="CCDS:CCDS14503.1"
                     /db_xref="GeneID:56000"
                     /db_xref="HGNC:HGNC:8073"
                     /db_xref="MIM:300316"
ORIGIN      
        1 mslpsghttg htdqvvqrra rcwdiyqrrf ssrsepvnpg mhssshqqqd gdaamhgahm
       61 dspvrytpyt ispynrkgsf rkqdqthvnm ereqkpperr megnmpdgtl gswfkitvpf
      121 gikynekwll nliqnecsvp fvpvefhyen mhasffvena siayalknvs gkiwdednek
      181 isifvnpagi phfvhrelks ekveqiklam nqqcdvsqea ldiqrlpfyp dmvnrdtkma
      241 snprkcmaas ldvheenipt vmsagemdkw kgiepgekca drspvcttfs dtssninsil
      301 elfpkllcld gqqspratlc gteahkrlpt ckgsffgsem lknlvlqflq qyyliydsgd
      361 rqgllsayhd eacfslsipf npedsapssf ckffkdsrni kilkdpylrg ellkhtkldi
      421 vdslsalpkt qhdlssflvd mwyqtewmlc fsvngvfkev egqsqgsvla ftrtfiatpg
      481 sssslcivnd klfvrdtshq gtqsalftlv ptafsssvpa fsqeqqkmlp s
//
LOCUS       NP_079420               1244 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-protein kinase 1 isoform 1 [Homo sapiens].
ACCESSION   NP_079420
VERSION     NP_079420.3
DBSOURCE    REFSEQ: accession NM_025144.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1244)
  AUTHORS   Zhao,J., Feng,Y., Liu,X., Li,H., Guo,H., Ke,J. and Long,X.
  TITLE     The relationship of ALPK1, hyaluronic acid and M1 macrophage
            polarization in the temporomandibular joint synovitis
  JOURNAL   J Cell Mol Med 28 (7), e18172 (2024)
   PUBMED   38494837
  REMARK    GeneRIF: The relationship of ALPK1, hyaluronic acid and M1
            macrophage polarization in the temporomandibular joint synovitis.
REFERENCE   2  (residues 1 to 1244)
  AUTHORS   Lou,S., Wang,J., Chen,J., Xie,H., Chen,H., Zhou,B., Zhang,B.,
            Hou,J. and Jiang,D.K.
  TITLE     The Role of ALPK1 in Inhibiting Hepatitis B Virus Replication
            Facilitates the Identification of ALPK1 P660L Variant for
            Predicting Response to Pegylated Interferon alpha Therapy
  JOURNAL   J Infect Dis 228 (6), 694-703 (2023)
   PUBMED   36932045
  REMARK    GeneRIF: The Role of ALPK1 in Inhibiting Hepatitis B Virus
            Replication Facilitates the Identification of ALPK1 P660L Variant
            for Predicting Response to Pegylated Interferon alpha Therapy.
REFERENCE   3  (residues 1 to 1244)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1244)
  AUTHORS   Bauer,M., Nascakova,Z., Mihai,A.I., Cheng,P.F., Levesque,M.P.,
            Lampart,S., Hurwitz,R., Pfannkuch,L., Dobrovolna,J., Jacobs,M.,
            Bartfeld,S., Dohlman,A., Shen,X., Gall,A.A., Salama,N.R.,
            Topfer,A., Weber,A., Meyer,T.F., Janscak,P. and Muller,A.
  TITLE     The ALPK1/TIFA/NF-kappaB axis links a bacterial carcinogen to
            R-loop-induced replication stress
  JOURNAL   Nat Commun 11 (1), 5117 (2020)
   PUBMED   33037203
  REMARK    GeneRIF: The ALPK1/TIFA/NF-kappaB axis links a bacterial carcinogen
            to R-loop-induced replication stress.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1244)
  AUTHORS   Zhong,L., Wang,J., Wang,W., Wang,L., Quan,M., Tang,X., Gou,L.,
            Wei,M., Xiao,J., Zhang,T., Sui,R., Zhou,Q. and Song,H.
  TITLE     Juvenile Onset Splenomegaly and Oculopathy Due to Germline Mutation
            in ALPK1
  JOURNAL   J Clin Immunol 40 (2), 350-358 (2020)
   PUBMED   31939038
  REMARK    GeneRIF: Juvenile Onset Splenomegaly and Oculopathy Due to Germline
            Mutation in ALPK1.
REFERENCE   6  (residues 1 to 1244)
  AUTHORS   Kalsi,G., Kuo,P.H., Aliev,F., Alexander,J., McMichael,O.,
            Patterson,D.G., Walsh,D., Zhao,Z., Schuckit,M., Nurnberger,J. Jr.,
            Edenberg,H., Kramer,J., Hesselbrock,V., Tischfield,J.A.,
            Vladimirov,V., Prescott,C.A., Dick,D.M., Kendler,K.S. and
            Riley,B.P.
  TITLE     A systematic gene-based screen of chr4q22-q32 identifies
            association of a novel susceptibility gene, DKK2, with the
            quantitative trait of alcohol dependence symptom counts
  JOURNAL   Hum Mol Genet 19 (12), 2497-2506 (2010)
   PUBMED   20332099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Erratum:[Hum Mol Genet. 2010 Oct 15;19(20):4121. Hesselbrock,
            Victor [added]; Tischfield, Jay A [added]]
REFERENCE   7  (residues 1 to 1244)
  AUTHORS   Heine,M., Cramm-Behrens,C.I., Ansari,A., Chu,H.P., Ryazanov,A.G.,
            Naim,H.Y. and Jacob,R.
  TITLE     Alpha-kinase 1, a new component in apical protein transport
  JOURNAL   J Biol Chem 280 (27), 25637-25643 (2005)
   PUBMED   15883161
  REMARK    GeneRIF: the phosphorylation of myosin I by ALPK1 is an essential
            process in the apical trafficking of raft-associated
            sucrose-isomaltase
REFERENCE   8  (residues 1 to 1244)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
REFERENCE   9  (residues 1 to 1244)
  AUTHORS   Ryazanov,A.G., Pavur,K.S. and Dorovkov,M.V.
  TITLE     Alpha-kinases: a new class of protein kinases with a novel
            catalytic domain
  JOURNAL   Curr Biol 9 (2), R43-R45 (1999)
   PUBMED   10021370
REFERENCE   10 (residues 1 to 1244)
  AUTHORS   Kozycki,C., Kastner,D., Huryn,L., Kodati,S. and Warner,B.M.
  TITLE     ALPK1-Related Autoinflammatory Disease
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   38935811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB250317.1, AY044164.1, BC060780.1, AK026715.1, BE155590.1 and
            AC004049.1.
            
            On Aug 22, 2007 this sequence version replaced NP_079420.2.
            
            Summary: This gene encodes an alpha kinase. Mice which were
            homozygous for disrupted copies of this gene exhibited coordination
            defects (PMID: 21208416). Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1 and 2 encode the same protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.21906.1,
                                           SRR1660809.114154.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000650871.1/ ENSP00000498374.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..1244
                     /product="alpha-protein kinase 1 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="lymphocyte alpha-kinase; alpha-protein kinase 1;
                     chromosome 4 kinase; lymphocyte alpha-protein kinase"
                     /calculated_mol_wt=138730
     Region          650..675
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QP1.3)"
     Region          701..737
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QP1.3)"
     Region          757..798
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QP1.3)"
     Region          824..848
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QP1.3)"
     Region          1004..1230
                     /region_name="Alpha_kinase_ALPK1"
                     /note="Alpha-kinase domain of alpha-protein kinase 1;
                     cd16969"
                     /db_xref="CDD:341219"
     Site            order(1042..1047,1049,1065,1067,1111,1131..1134,1177,1179,
                     1194)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:341219"
     CDS             1..1244
                     /gene="ALPK1"
                     /gene_synonym="8430410J10Rik; LAK; ROSAH"
                     /coded_by="NM_025144.4:254..3988"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3697.1"
                     /db_xref="GeneID:80216"
                     /db_xref="HGNC:HGNC:20917"
                     /db_xref="MIM:607347"
ORIGIN      
        1 mnnqkvvavl lqeckqvldq llleapdvse edksedqrcr allpselrtl iqeakemkwp
       61 fvpekwqykq avgpedktnl kdvigaglqq llaslrasil ardcaaaaai vflvdrflyg
      121 ldvsgkllqv akglhklqpa tpiapqvvir qarisvnsgk llkaeyilss lisnngatgt
      181 wlyrnesdkv lvqsvciqir gqilqklgmw yeaaeliwas ivgylalpqp dkkglstslg
      241 iladifvsms kndyekfknn pqinlsllke fdhhllsaae acklaaafsa ytplfvltav
      301 nirgtcllsy sssndcppel knlhlceake afeiglltkr ddepvtgkqe lhsfvkaafg
      361 lttvhrrlhg etgtvhaasq lckeamgkly nfstssrsqd realsqevms viaqvkehlq
      421 vqsfsnvddr syvpesfecr ldklilhgqg dfqkildtys qhhtsvcevf esdcgnnkne
      481 qkdaktgvci talkteikni dtvsttqekp hcqrdtgiss slmgknvqre lrrggrrnwt
      541 hsdafrvsld qdveteteps dysngegavf nkslsgsqts sawsnlsgfs ssasweevny
      601 hvddrsarke pgkehlvdtq cstalseele ndregramhs lhsqlhdlsl qepnndnlep
      661 sqnqpqqqmp ltpfsphntp giflapgagl legapegiqe vrnmgprnts ahsrpsyrsa
      721 swssdsgrpk nmgthpsvqk eeafeiivef petncdvkdr qgkeqgeeis ergagptfka
      781 spswvdpege taestedapl dfhrvlhnsl gnismlpcss ftpnwpvqnp dsrksggpva
      841 eqgidpdast vdeegqllds mdvpctnghg shrlcilrqp pgqraetpns svsgnilfpv
      901 lsedctttee gnqpgnmlnc sqnsssssvw wlkspafssg ssegdspwsy lnssgsswvs
      961 lpgkmrkeil eartlqpddf ekllagvrhd wlfqrlentg vfkpsqlhra hsalllkysk
     1021 kselwtaqet ivylgdyltv kkkgrqrnaf wvhhlhqeei lgryvgkdyk eqkglwhhft
     1081 dverqmtaqh yvtefnkrly eqniptqify ipstillile dktikgcisv epyilgefvk
     1141 lsnntkvvkt eykateygla yghfsyefsn hrdvvvdlqg wvtgngkgli yltdpqihsv
     1201 dqkvfttnfg krgifyffnn qhvecneich rlsltrpsme kpct
//
LOCUS       NP_001074514            1036 aa            linear   ROD 27-APR-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 1 [Mus musculus].
ACCESSION   NP_001074514 XP_109700
VERSION     NP_001074514.1
DBSOURCE    REFSEQ: accession NM_001081045.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Guhathakurta,S., Erdogdu,N.U., Hoffmann,J.J., Grzadzielewska,I.,
            Schendzielorz,A., Seyfferth,J., Martensson,C.U., Corrado,M.,
            Karoutas,A., Warscheid,B., Pfanner,N., Becker,T. and Akhtar,A.
  TITLE     COX17 acetylation via MOF-KANSL complex promotes mitochondrial
            integrity and function
  JOURNAL   Nat Metab 5 (11), 1931-1952 (2023)
   PUBMED   37813994
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Wang,D., Li,H., Chandel,N.S., Dou,Y. and Yi,R.
  TITLE     MOF-mediated histone H4 Lysine 16 acetylation governs mitochondrial
            and ciliary functions by controlling gene promoters
  JOURNAL   Nat Commun 14 (1), 4404 (2023)
   PUBMED   37479688
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Li,T., Lu,D., Yao,C., Li,T., Dong,H., Li,Z., Xu,G., Chen,J.,
            Zhang,H., Yi,X., Zhu,H., Liu,G., Wen,K., Zhao,H., Gao,J., Zhang,Y.,
            Han,Q., Li,T., Zhang,W., Zhao,J., Li,T., Bai,Z., Song,M., He,X.,
            Zhou,T., Xia,Q., Li,A. and Pan,X.
  TITLE     Kansl1 haploinsufficiency impairs autophagosome-lysosome fusion and
            links autophagic dysfunction with Koolen-de Vries syndrome in mice
  JOURNAL   Nat Commun 13 (1), 931 (2022)
   PUBMED   35177641
  REMARK    GeneRIF: Kansl1 haploinsufficiency impairs autophagosome-lysosome
            fusion and links autophagic dysfunction with Koolen-de Vries
            syndrome in mice.
            Erratum:[Nat Commun. 2022 Mar 17;13(1):1575. doi:
            10.1038/s41467-022-29129-3. PMID: 35301327]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1036)
  AUTHORS   Sheikh,B.N., Guhathakurta,S., Tsang,T.H., Schwabenland,M.,
            Renschler,G., Herquel,B., Bhardwaj,V., Holz,H., Stehle,T.,
            Bondareva,O., Aizarani,N., Mossad,O., Kretz,O., Reichardt,W.,
            Chatterjee,A., Braun,L.J., Thevenon,J., Sartelet,H., Blank,T.,
            Grun,D., von Elverfeldt,D., Huber,T.B., Vestweber,D., Avilov,S.,
            Prinz,M., Buescher,J.M. and Akhtar,A.
  TITLE     Neural metabolic imbalance induced by MOF dysfunction triggers
            pericyte activation and breakdown of vasculature
  JOURNAL   Nat Cell Biol 22 (7), 828-841 (2020)
   PUBMED   32541879
REFERENCE   5  (residues 1 to 1036)
  AUTHORS   Arbogast,T., Iacono,G., Chevalier,C., Afinowi,N.O., Houbaert,X.,
            van Eede,M.C., Laliberte,C., Birling,M.C., Linda,K., Meziane,H.,
            Selloum,M., Sorg,T., Nadif Kasri,N., Koolen,D.A., Stunnenberg,H.G.,
            Henkelman,R.M., Kopanitsa,M., Humeau,Y., De Vries,B.B.A. and
            Herault,Y.
  TITLE     Mouse models of 17q21.31 microdeletion and microduplication
            syndromes highlight the importance of Kansl1 for cognition
  JOURNAL   PLoS Genet 13 (7), e1006886 (2017)
   PUBMED   28704368
  REMARK    GeneRIF: Our results demonstrate the implication of KANSL1 in the
            manifestation of Koolen-de Vries syndrome phenotypes and extend
            substantially our knowledge about biological processes affected by
            these mutations. Clear differences in social behavior and gene
            expression profiles between Del/+ and Kansl1+/- mice suggested
            potential roles of other genes affected by the 17q21.31 deletion.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1036)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Aizawa,H., Yuasa,S.,
            Nakajima,D., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: II. The complete nucleotide sequences of 400 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (1), 35-48 (2003)
   PUBMED   12693553
REFERENCE   7  (residues 1 to 1036)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   8  (residues 1 to 1036)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1036)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
REFERENCE   10 (residues 1 to 1036)
  AUTHORS   Nishiguchi,S., Sakuma,R., Nomura,M., Zou,Z., Jearanaisilavong,J.,
            Joh,T., Yasunaga,T. and Shimada,K.
  TITLE     A catalogue of genes in mouse embryonal carcinoma F9 cells
            identified with expressed sequence tags
  JOURNAL   J Biochem 119 (4), 749-767 (1996)
   PUBMED   8743579
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL593843.9, BC054752.1 and BC079594.1.
            
            On Feb 6, 2007 this sequence version replaced XP_109700.4.
            
            Transcript Variant: This variant (1) encodes isoform 1. Variants 1
            and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK122484.1, SRR10662774.63405.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164142 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 67.79 cM"
     Protein         1..1036
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 1"
                     /note="NSL complex protein NSL1; non-specific lethal 1
                     homolog"
                     /calculated_mol_wt=113048
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z3B3; propagated from
                     UniProtKB/Swiss-Prot (Q80TG1.1)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TG1.1)"
     Region          226..257
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TG1.1)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TG1.1)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TG1.1)"
     Region          399..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TG1.1)"
     Region          739..787
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TG1.1)"
     Region          781..813
                     /region_name="Required for activation of KAT8 histone
                     acetyltransferase activity. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TG1.1)"
     Region          816..936
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     Region          841..859
                     /region_name="Interaction with KAT8 HAT domain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01397"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TG1.1)"
     Region          869..931
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TG1.1)"
     Site            922
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z3B3; propagated from
                     UniProtKB/Swiss-Prot (Q80TG1.1)"
     Site            925
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z3B3; propagated from
                     UniProtKB/Swiss-Prot (Q80TG1.1)"
     Site            934
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z3B3; propagated from
                     UniProtKB/Swiss-Prot (Q80TG1.1)"
     Site            976
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z3B3; propagated from
                     UniProtKB/Swiss-Prot (Q80TG1.1)"
     Region          989..1020
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TG1.1)"
     CDS             1..1036
                     /gene="Kansl1"
                     /gene_synonym="1700081L11Rik; 9430041J06Rik; mKIAA1267"
                     /coded_by="NM_001081045.2:651..3761"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS48953.1"
                     /db_xref="GeneID:76719"
                     /db_xref="MGI:MGI:1923969"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna nilisangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pakeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnssslnggk
      181 rsltssslqg gevggpdsgn lkggmtnctl phrsldiqht tlysnnstan kssvnsmdqp
      241 alqgssrlsp stdsssnltn vklevkkspl ssilfsalds dtritallrr qadieirarr
      301 lqkrlqvvqa kqverhlqhq lggflettls klpnleslrs rsqlmltrka eaalrkaase
      361 satseglsnf lksdsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqchvpl krrsewrwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgeapfpdh ttdllslsse vktdhgrdkl iesvsqpsen hgilvsnite slstkscgap
      541 rpvngvvnsl qpvladqvpg dssdaeeqlh kkqrlnlvss sdgtcvaart rpvltckkrr
      601 lvrpssivpl skkvhrnvrs gcdvnpscal cgsgsvntmp peihyeapll erlsqldscv
      661 hpvlafpddv ptslhfqsml ksqwqnkpfd kikptkkfsl khratmpcsl sdpvrkdrhk
      721 lvnsflttam lkhhtdmssp syltathhpp hsplvrqlst ssdtstptss gsqvaastsq
      781 pvrrrrgess fdinnivipm svaattrvek lqykeiltps wrevdvqslk gspdeeneei
      841 edlsdaafaa lhakceemer arwlwttsvp pqrrgsrsyr ssdgrttpql gsanpstpqp
      901 aspdvssshs lsefshgqsp rspispelhs apltpvards lrhlasedtr cstpelglde
      961 qsvqpwerrt fplayspqae ceeqldaqdt aarctrrtsg sktgreaeva ptsppvvplk
     1021 srhlaatvta qrpahr
//
LOCUS       NP_001357469             496 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RFWD3 isoform 3 [Homo sapiens].
ACCESSION   NP_001357469
VERSION     NP_001357469.1
DBSOURCE    REFSEQ: accession NM_001370540.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Moore,C.E., Yalcindag,S.E., Czeladko,H., Ravindranathan,R.,
            Wijesekara Hanthi,Y., Levy,J.C., Sannino,V., Schindler,D.,
            Ciccia,A., Costanzo,V. and Elia,A.E.H.
  TITLE     RFWD3 promotes ZRANB3 recruitment to regulate the remodeling of
            stalled replication forks
  JOURNAL   J Cell Biol 222 (5) (2023)
   PUBMED   37036693
  REMARK    GeneRIF: RFWD3 promotes ZRANB3 recruitment to regulate the
            remodeling of stalled replication forks.
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Zhu,Y., Peng,X., Wang,X., Ying,P., Wang,H., Li,B., Li,Y., Zhang,M.,
            Cai,Y., Lu,Z., Niu,S., Yang,N., Zhong,R., Tian,J., Chang,J. and
            Miao,X.
  TITLE     Systematic analysis on expression quantitative trait loci
            identifies a novel regulatory variant in ring finger and WD repeat
            domain 3 associated with prognosis of pancreatic cancer
  JOURNAL   Chin Med J (Engl) 135 (11), 1348-1357 (2022)
   PUBMED   35830250
  REMARK    GeneRIF: Systematic analysis on expression quantitative trait loci
            identifies a novel regulatory variant in ring finger and WD repeat
            domain 3 associated with prognosis of pancreatic cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Gallina,I., Hendriks,I.A., Hoffmann,S., Larsen,N.B., Johansen,J.,
            Colding-Christensen,C.S., Schubert,L., Selles-Baiget,S., Fabian,Z.,
            Kuhbacher,U., Gao,A.O., Raschle,M., Rasmussen,S., Nielsen,M.L.,
            Mailand,N. and Duxin,J.P.
  TITLE     The ubiquitin ligase RFWD3 is required for translesion DNA
            synthesis
  JOURNAL   Mol Cell 81 (3), 442-458 (2021)
   PUBMED   33321094
  REMARK    GeneRIF: The ubiquitin ligase RFWD3 is required for translesion DNA
            synthesis.
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Hsu,R.Y.C., Giri,S., Wang,Y., Lin,Y.C., Liu,D., Wopat,S.,
            Chakraborty,A., Prasanth,K.V. and Prasanth,S.G.
  TITLE     The E3 ligase RFWD3 stabilizes ORC in a p53-dependent manner
  JOURNAL   Cell Cycle 19 (21), 2927-2938 (2020)
   PUBMED   33044890
  REMARK    GeneRIF: The E3 ligase RFWD3 stabilizes ORC in a p53-dependent
            manner.
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Jia,J., Yang,Y., Yan,T., Chen,T. and Lu,G.
  TITLE     Down-regulation of RFWD3 inhibits cancer cells proliferation and
            migration in gastric carcinoma
  JOURNAL   Gen Physiol Biophys 39 (4), 363-371 (2020)
   PUBMED   32902405
  REMARK    GeneRIF: Down-regulation of RFWD3 inhibits cancer cells
            proliferation and migration in gastric carcinoma.
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Dastani,Z., Pajukanta,P., Marcil,M., Rudzicz,N., Ruel,I.,
            Bailey,S.D., Lee,J.C., Lemire,M., Faith,J., Platko,J., Rioux,J.,
            Hudson,T.J., Gaudet,D., Engert,J.C. and Genest,J.
  TITLE     Fine mapping and association studies of a high-density lipoprotein
            cholesterol linkage region on chromosome 16 in French-Canadian
            subjects
  JOURNAL   Eur J Hum Genet 18 (3), 342-347 (2010)
   PUBMED   19844255
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Markson,G., Kiel,C., Hyde,R., Brown,S., Charalabous,P., Bremm,A.,
            Semple,J., Woodsmith,J., Duley,S., Salehi-Ashtiani,K., Vidal,M.,
            Komander,D., Serrano,L., Lehner,P. and Sanderson,C.M.
  TITLE     Analysis of the human E2 ubiquitin conjugating enzyme protein
            interaction network
  JOURNAL   Genome Res 19 (10), 1905-1911 (2009)
   PUBMED   19549727
REFERENCE   8  (residues 1 to 496)
  AUTHORS   van Wijk,S.J., de Vries,S.J., Kemmeren,P., Huang,A., Boelens,R.,
            Bonvin,A.M. and Timmers,H.T.
  TITLE     A comprehensive framework of E2-RING E3 interactions of the human
            ubiquitin-proteasome system
  JOURNAL   Mol Syst Biol 5, 295 (2009)
   PUBMED   19690564
  REMARK    Erratum:[Mol Syst Biol. 2009;5:317]
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Tsuritani,K., Irie,T., Yamashita,R., Sakakibara,Y., Wakaguri,H.,
            Kanai,A., Mizushima-Sugano,J., Sugano,S., Nakai,K. and Suzuki,Y.
  TITLE     Distinct class of putative 'non-conserved' promoters in humans:
            comparative studies of alternative promoters of human and mouse
            genes
  JOURNAL   Genome Res 17 (7), 1005-1014 (2007)
   PUBMED   17567985
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Mehta,P.A. and Ebens,C.
  TITLE     Fanconi Anemia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC109599.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.19411.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..496
                     /product="E3 ubiquitin-protein ligase RFWD3 isoform 3"
                     /EC_number="2.3.2.27"
                     /note="RING finger and WD repeat domain-containing protein
                     3; E3 ubiquitin-protein ligase RFWD3; RING finger protein
                     201; RING-type E3 ubiquitin transferase RFWD3"
                     /calculated_mol_wt=55476
     Region          5..65
                     /region_name="mRING-C3HGC3_RFWD3"
                     /note="Modified RING finger, C3HGC3-type, found in RING
                     finger and WD repeat domain-containing protein 3 (RFWD3)
                     and similar proteins; cd16450"
                     /db_xref="CDD:438114"
     Region          218..484
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          264..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..496
                     /gene="RFWD3"
                     /gene_synonym="FANCW; RNF201"
                     /coded_by="NM_001370540.1:579..2069"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="GeneID:55159"
                     /db_xref="HGNC:HGNC:25539"
                     /db_xref="MIM:614151"
ORIGIN      
        1 mdeeegdtct icleqwtnag dhrlsalrcg hlfgyrcist wlkgqvrkcp qcnkkarhsd
       61 ivvlyartlr aldtseqerm kssllkeqml rkqaelesaq crlqlqvltd kctrlqrrvq
      121 dlqkltshqs qnlqqprgsq awvlscspss qgqhkhkyhf qktftvsqag ncrimaycda
      181 lsclvisqps pqasflpgfg vkmlstanmk ssqyipmhgk qirglafssy lrglllsasl
      241 dntikltsle tntvvqtyna grpvwsccwc ldeanyiyag langsilvyd vrntsshvqe
      301 lvaqkarcpl vslsympraa saafpyggvl agtledasfw eqkmdfshwp hvlplepggc
      361 idfqtenssr hclvtyrpdk nhttirsvlm emsyrlddtg npicscqpvh tffggptckl
      421 ltknaifqsp endgnilvct gdeaansall wdaasgsllq dlqtdqpvld icpfevnrns
      481 ylatltekmv hiykwe
//
LOCUS       NP_001347502             683 aa            linear   ROD 27-APR-2025
DEFINITION  synaptic vesicle glycoprotein 2B [Mus musculus].
ACCESSION   NP_001347502 XP_017167699
VERSION     NP_001347502.1
DBSOURCE    REFSEQ: accession NM_001360573.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Paulussen,I., Beckert,H., Musial,T.F., Gschossmann,L.J., Wolf,J.,
            Schmitt,M., Clasadonte,J., Mairet-Coello,G., Wolff,C., Schoch,S.
            and Dietrich,D.
  TITLE     SV2B defines a subpopulation of synaptic vesicles
  JOURNAL   J Mol Cell Biol 15 (9) (2024)
   PUBMED   37682518
  REMARK    GeneRIF: SV2B defines a subpopulation of synaptic vesicles.
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Bolz,S., Kaempf,N., Puchkov,D., Krauss,M., Russo,G., Soykan,T.,
            Schmied,C., Lehmann,M., Muller,R., Schultz,C., Perrais,D.,
            Maritzen,T. and Haucke,V.
  TITLE     Synaptotagmin 1-triggered lipid signaling facilitates coupling of
            exo- and endocytosis
  JOURNAL   Neuron 111 (23), 3765-3774 (2023)
   PUBMED   37738980
  REMARK    Erratum:[Neuron. 2023 Dec 6;111(23):3900. doi:
            10.1016/j.neuron.2023.11.003. PMID: 38061332]
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Vana,N.S., van Loo,K.M.J., van Waardenberg,A.J., Tiessen,M.,
            Cases-Cunillera,S., Sun,W., Quatraccioni,A., Schoch,S. and
            Dietrich,D.
  TITLE     Early cortical oligodendrocyte precursor cells are
            transcriptionally distinct and lack synaptic connections
  JOURNAL   Glia 71 (9), 2210-2233 (2023)
   PUBMED   37226895
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Lopez-Tello,J. and Sferruzzi-Perri,A.N.
  TITLE     Characterization of placental endocrine function and fetal brain
            development in a mouse model of small for gestational age
  JOURNAL   Front Endocrinol (Lausanne) 14, 1116770 (2023)
   PUBMED   36843585
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Noakes,P.G., Chin,D., Kim,S.S., Liang,S. and Phillips,W.D.
  TITLE     Expression and localisation of dynamin and syntaxin during neural
            development and neuromuscular synapse formation
  JOURNAL   J Comp Neurol 410 (4), 531-540 (1999)
   PUBMED   10398046
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Serpinskaya,A.S., Feng,G., Sanes,J.R. and Craig,A.M.
  TITLE     Synapse formation by hippocampal neurons from agrin-deficient mice
  JOURNAL   Dev Biol 205 (1), 65-78 (1999)
   PUBMED   9882498
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Rich,K.A., Zhan,Y. and Blanks,J.C.
  TITLE     Migration and synaptogenesis of cone photoreceptors in the
            developing mouse retina
  JOURNAL   J Comp Neurol 388 (1), 47-63 (1997)
   PUBMED   9364238
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Gautam,M., Noakes,P.G., Moscoso,L., Rupp,F., Scheller,R.H.,
            Merlie,J.P. and Sanes,J.R.
  TITLE     Defective neuromuscular synaptogenesis in agrin-deficient mutant
            mice
  JOURNAL   Cell 85 (4), 525-535 (1996)
   PUBMED   8653788
REFERENCE   10 (residues 1 to 683)
  AUTHORS   Ahnert-Hilger,G., Kutay,U., Chahoud,I., Rapoport,T. and
            Wiedenmann,B.
  TITLE     Synaptobrevin is essential for secretion but not for the
            development of synaptic processes
  JOURNAL   Eur J Cell Biol 70 (1), 1-11 (1996)
   PUBMED   8738414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC127355.4, AC116898.11 and AC113471.9.
            
            On Feb 7, 2018 this sequence version replaced XP_017167699.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 3. All seven variants encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR9219382.50883.1,
                                           SRR9219379.7439.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 43.62 cM"
     Protein         1..683
                     /product="synaptic vesicle glycoprotein 2B"
                     /note="synaptic vesicle protein 2B; synaptic vesicle
                     glycoprotein 2 b"
                     /calculated_mol_wt=77327
     Region          1..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Region          8..683
                     /region_name="synapt_SV2"
                     /note="synaptic vesicle protein SV2; TIGR01299"
                     /db_xref="CDD:130366"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            111..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            183..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            206..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            391..411
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18034455; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            441
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            491
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            516
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            536..556
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            566..586
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            593..613
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            627..649
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     Site            654..672
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG39.1)"
     CDS             1..683
                     /gene="Sv2b"
                     /gene_synonym="A830038F04Rik; mKIAA0735"
                     /coded_by="NM_001360573.1:700..2751"
                     /db_xref="CCDS:CCDS21368.1"
                     /db_xref="GeneID:64176"
                     /db_xref="MGI:MGI:1927338"
ORIGIN      
        1 mddyryrdny egyapsdgyy rsneqnqeed aqsdvteghd eedeiyegey qgiphpddvk
       61 skqtkmapsr adglggqadl maermedeee lahqyetiid ecghgrfqwt lffvlglalm
      121 adgveifvvs falpsaekdm clssskkgml glivylgmma gafilgglad klgrkkvlsm
      181 slainasfas lssfvqgyga flfcrlisgi giggslpivf ayfseflsre krgehlswlg
      241 ifwmtggiya samawsiiph ygwgfsmgtn yhfhswrvfv ivcalpatvs mvalkfmpes
      301 prfllemgkh deawmilkqv hdtnmrakgt pekvftvshi ktpkqmdefi eiqsstgtwy
      361 qrwlvrfmti fkqvwdnaly cvmgpyrmnt lilavvwftm alsyygltvw fpdmiryfqd
      421 eeykskmkvf fgehvhgati nftmenqihq hgklvndkfi kmyfkhvlfe dtffdkcyfe
      481 dvtstdtyfk nctiesttfy ntdlykhkfi ncrfinstfl eqkegchmdf eedndfliyl
      541 vsflgslsvl pgniisallm drigrlkmig gsmlisavcc fflffgnses amigwqclfc
      601 gtsiaawnal dvitvelypt nqratafgil nglckfgail gntifasfvg itkvvpilla
      661 aaslvgggli alrlpetreq vlm
//
LOCUS       NP_598898               1178 aa            linear   ROD 27-APR-2025
DEFINITION  leucine--tRNA ligase, cytoplasmic [Mus musculus].
ACCESSION   NP_598898 XP_619533 XP_906261 XP_906266 XP_906270 XP_906275
            XP_906280 XP_918522 XP_927848 XP_927860 XP_927864 XP_927868
            XP_927875 XP_927878 XP_994309
VERSION     NP_598898.2
DBSOURCE    REFSEQ: accession NM_134137.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1178)
  AUTHORS   You,J.S., Karaman,K., Reyes-Ordonez,A., Lee,S., Kim,Y., Bashir,R.
            and Chen,J.
  TITLE     Leucyl-tRNA Synthetase Contributes to Muscle Weakness through
            Mammalian Target of Rapamycin Complex 1 Activation and Autophagy
            Suppression in a Mouse Model of Duchenne Muscular Dystrophy
  JOURNAL   Am J Pathol 194 (8), 1571-1580 (2024)
   PUBMED   38762116
  REMARK    GeneRIF: Leucyl-tRNA Synthetase Contributes to Muscle Weakness
            through Mammalian Target of Rapamycin Complex 1 Activation and
            Autophagy Suppression in a Mouse Model of Duchenne Muscular
            Dystrophy.
REFERENCE   2  (residues 1 to 1178)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 1178)
  AUTHORS   Passarelli,M.C., Pinzaru,A.M., Asgharian,H., Liberti,M.V.,
            Heissel,S., Molina,H., Goodarzi,H. and Tavazoie,S.F.
  TITLE     Leucyl-tRNA synthetase is a tumour suppressor in breast cancer and
            regulates codon-dependent translation dynamics
  JOURNAL   Nat Cell Biol 24 (3), 307-315 (2022)
   PUBMED   35288656
REFERENCE   4  (residues 1 to 1178)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1178)
  AUTHORS   Menendez-Montes,I., Escobar,B., Gomez,M.J., Albendea-Gomez,T.,
            Palacios,B., Bonzon-Kulichenko,E., Izquierdo-Garcia,J.L.,
            Alonso,A.V., Ferrarini,A., Jimenez-Borreguero,L.J.,
            Ruiz-Cabello,J., Vazquez,J. and Martin-Puig,S.
  TITLE     Activation of amino acid metabolic program in cardiac
            HIF1-alpha-deficient mice
  JOURNAL   iScience 24 (2), 102124 (2021)
   PUBMED   33665549
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1178)
  AUTHORS   Yoon,I., Nam,M., Kim,H.K., Moon,H.S., Kim,S., Jang,J., Song,J.A.,
            Jeong,S.J., Kim,S.B., Cho,S., Kim,Y., Lee,J., Yang,W.S., Yoo,H.C.,
            Kim,K., Kim,M.S., Yang,A., Cho,K., Park,H.S., Hwang,G.S.,
            Hwang,K.Y., Han,J.M., Kim,J.H. and Kim,S.
  TITLE     Glucose-dependent control of leucine metabolism by leucyl-tRNA
            synthetase 1
  JOURNAL   Science 367 (6474), 205-210 (2020)
   PUBMED   31780625
  REMARK    GeneRIF: this study provides evidence for a role of leucyl-tRNA
            synthetase 1 (LARS1) in glucose-dependent control of leucine usage
REFERENCE   7  (residues 1 to 1178)
  AUTHORS   Li,B., Wang,Z., Chen,R., Hong,J., Wu,Q., Hu,J., Hu,Z. and Zhang,M.
  TITLE     Up regulation of isoleucyl-tRNA synthetase promotes vascular smooth
            muscle cells dysfunction via p38 MAPK/PI3K signaling pathways
  JOURNAL   Life Sci 224, 51-57 (2019)
   PUBMED   30905780
  REMARK    GeneRIF: High LARS expression is associated with abdominal aortic
            aneurysm.
REFERENCE   8  (residues 1 to 1178)
  AUTHORS   Son,K., You,J.S., Yoon,M.S., Dai,C., Kim,J.H., Khanna,N.,
            Banerjee,A., Martinis,S.A., Han,G., Han,J.M., Kim,S. and Chen,J.
  TITLE     Nontranslational function of leucyl-tRNA synthetase regulates
            myogenic differentiation and skeletal muscle regeneration
  JOURNAL   J Clin Invest 129 (5), 2088-2093 (2019)
   PUBMED   30985292
  REMARK    GeneRIF: leucyl-tRNA synthetase has a nontranslational function in
            regulating myogenic differentiation and skeletal muscle
            regeneration
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1178)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1178)
  AUTHORS   Kim,J.Y., Kang,Y.S., Lee,J.W., Kim,H.J., Ahn,Y.H., Park,H., Ko,Y.G.
            and Kim,S.
  TITLE     p38 is essential for the assembly and stability of macromolecular
            tRNA synthetase complex: implications for its physiological
            significance
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 7912-7916 (2002)
   PUBMED   12060739
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BB652360.1, BC052715.1 and BE989557.1.
            
            On or before Jan 3, 2007 this sequence version replaced
            XP_619533.2, XP_906270.1, XP_906280.1, XP_906266.1, XP_906261.1,
            XP_906275.1, XP_918522.1, XP_927848.1, XP_927868.1, XP_927878.1,
            XP_927864.1, XP_927860.1, XP_927875.1, XP_994309.1, NP_598898.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.5804.1, BC052715.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1178
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 22.37 cM"
     Protein         1..1178
                     /product="leucine--tRNA ligase, cytoplasmic"
                     /EC_number="6.1.1.4"
                     /note="leucyl-tRNA synthetase, cytoplasmic"
                     /calculated_mol_wt=134062
     Region          3..1064
                     /region_name="PLN02959"
                     /note="aminoacyl-tRNA ligase"
                     /db_xref="CDD:215518"
     Region          62..65
                     /region_name="'HIGH' region.
                     /evidence=ECO:0000250|UniProtKB:Q9P2J5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BMJ2.2)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2J5; propagated from
                     UniProtKB/Swiss-Prot (Q8BMJ2.2)"
     Region          262..511
                     /region_name="Editing domain.
                     /evidence=ECO:0000250|UniProtKB:Q9P2J5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BMJ2.2)"
     Region          718..722
                     /region_name="'KMSKS' region.
                     /evidence=ECO:0000250|UniProtKB:Q9P2J5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BMJ2.2)"
     Site            722
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2J5; propagated from
                     UniProtKB/Swiss-Prot (Q8BMJ2.2)"
     Site            972
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q8BMJ2.2)"
     Site            1049
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q8BMJ2.2)"
     CDS             1..1178
                     /gene="Lars1"
                     /gene_synonym="2310045K21Rik; 3110009L02Rik; Lars; leuRS"
                     /coded_by="NM_134137.3:160..3696"
                     /db_xref="CCDS:CCDS37796.1"
                     /db_xref="GeneID:107045"
                     /db_xref="MGI:MGI:1913808"
ORIGIN      
        1 magrkgtakv dflkeiekea qqkweaekvf evsasrlekq kqsskgkyfv tfpypymngr
       61 lhlghtfsls kcefavgyqr lkgksclfpf glhctgmpik acadklkrei elygcppdfp
      121 eeeeeeeess akpgdivvrd kakgkkskaa akagsskyqw dimkslglsd ddivkfseae
      181 hwldyfppla vqdlktiglk vdwrrsfitt dvnpyydsfv rwqfltlrer nkikfgkryt
      241 iyspkdgqpc mdhdrqtgeg vgpqeytlvk lkvlepypsk lsglkgknif lvaatlrpet
      301 mfgqtncwvr pdmkyigfet angdifictq raarnmsyqg ftkhngvvpv vkelmgeeil
      361 gaslsapltc ykvvyvlpml tikedkgtgv vtsvpsdspd dlaalrdlkk kqalrtkfgi
      421 rddmvlpfep vpvleipgig nlpavtvcde lkiqsqndre klaeakekly lrgfydgvml
      481 vdgfkgqkiq hvkktiqknm idagdaliym epekqvmsrs adecvvalcd qwyldygden
      541 wkkqtfqclk nmetfceesr knfeasldwl qehacsrtyg lgtrlpwdeq wlieslsdst
      601 iymafytvah llqggdlngq aesplgirpq qmtkdvwdyv ffkdapfpkt qipkekldql
      661 kqefefwypv dlrasgkdli pnhlsyyiyn hvamwpeqsd kwpvsvrang hlllnsekms
      721 kstgnfltls qavdkfsadg mrlaladagd tvedanfvea madagilrly twvewvkeml
      781 ascsslrsgp adsfndrvfa semnagiikt dqnyekmmfk ealktgffef qaakdkyrel
      841 ategmhrelv frfievqtil ltpfcphlce hiwtllgkpd simhaswpva gpvdeslirs
      901 sqylmevahd lrlrlknymm pakgkktdkq paqrpshcti yvaknypvwq hitlttlrsh
      961 feanngklpd nkviaselgs lpelkkymkk vmpfvamike nmekkgprvl dlelefdeqa
     1021 vlmenivylt nslelehiev kfaseaedkv reeccpgkpl nvfrtepgvp vslvnpqpss
     1081 ghfstkidir qgdscesiir rlmktdrgik dlskvklmrf ddpllgprrv pvlgrehsek
     1141 tlisenavfh vdlvskkvhl tenglrtdig dtmvylvh
//
LOCUS       NP_001356694             682 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 28 isoform 6 [Homo sapiens].
ACCESSION   NP_001356694
VERSION     NP_001356694.1
DBSOURCE    REFSEQ: accession NM_001369765.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Rousseau-Merck,M.F., Hillion,J., Jonveaux,P., Couillin,P.,
            Seite,P., Thiesen,H.J. and Berger,R.
  TITLE     Chromosomal localization of 9 KOX zinc finger genes: physical
            linkages suggest clustering of KOX genes on chromosomes 12, 16, and
            19
  JOURNAL   Hum Genet 92 (6), 583-587 (1993)
   PUBMED   8262519
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008813.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..682
                     /product="zinc finger protein 28 isoform 6"
                     /note="zinc finger protein KOX24"
                     /calculated_mol_wt=79305
     Region          <113..337
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          181..201
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          209..229
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <228..338
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          237..257
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          265..285
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          293..313
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(298,300,302,304..305,308..309,312,326,328,332..333,
                     336..337,340,354,356,358,360..361,364..365,368)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          317..678
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          321..341
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          349..369
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          377..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          405..425
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          433..453
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          461..481
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          489..509
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          517..537
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(522,524,526,528..529,532..533,536,550,552,556..557,
                     560..561,564,578,580,582,584..585,588..589,592)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          545..565
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          573..593
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          601..621
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(606,608,610,612..613,616..617,620,634,636,640..641,
                     644..645,648,662,664,666,668..669,672..673,676)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          629..649
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          657..677
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..682
                     /gene="ZNF28"
                     /gene_synonym="KOX24"
                     /coded_by="NM_001369765.1:477..2525"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:7576"
                     /db_xref="HGNC:HGNC:13073"
                     /db_xref="MIM:620466"
ORIGIN      
        1 mlenyrnlvs ldisskcmmk tffstgqgnt eafhtgtlqr qashhigdfc fqkiekdihg
       61 fqfqwkedet ndhaapmtei keltgstgqh dqrhagnkhi kdqlglsfhs hlpelhifqp
      121 egkignqvek sinnassvst sqriccrpkt hisnkygnns lhsslltqkr nvhmreksfq
      181 ciesgksfnc ssllkkhqit hleekqckcd vygkvfnqkr ylachrrshi dekpykcnec
      241 gkifghntsl flhkalhtad kpyeceecdk vfsrkshlet hkiiytggkp ykckvcdkaf
      301 tcnsylakht iihtgekpyk cnecgkvfnr lstlarhrrl htgekpyece ecekvfsrks
      361 hlerhkriht gekpykckvc dkafaynsyl akhsiihtge kpykcnecgk vfnqqstlar
      421 hhrlhtaekp ykceecdkvf rckshlerhr rihtgekpyk ckvcdkafrs dscltehqrv
      481 htgekpymcn ecgkvfstka nlachhklht aekpykceec ekvfsrkshm erhrrihtge
      541 kpykckvcdk afrrdshlaq hqrvhtgekp ykcnecgktf rqtssliihr rlhtgekpyk
      601 cnecgktfsq msslvyhhrl hsgekpykcn ecgkvfnqqa hlaqhqrvht gekpykcnec
      661 gktfsqmsnl vyhhrlhsge kp
//
LOCUS       NP_001356676             150 aa            linear   PRI 27-APR-2025
DEFINITION  integrin beta-1-binding protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001356676 XP_005246246
VERSION     NP_001356676.1
DBSOURCE    REFSEQ: accession NM_001369747.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Su,V.L., Simon,B., Draheim,K.M. and Calderwood,D.A.
  TITLE     Serine phosphorylation of the small phosphoprotein ICAP1 inhibits
            its nuclear accumulation
  JOURNAL   J Biol Chem 295 (10), 3269-3284 (2020)
   PUBMED   32005669
  REMARK    GeneRIF: Serine phosphorylation of the small phosphoprotein ICAP1
            inhibits its nuclear accumulation.
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Bouin,A.P., Kyumurkov,A., Regent-Kloeckner,M., Ribba,A.S.,
            Faurobert,E., Fournier,H.N., Bourrin-Reynard,I., Manet-Dupe,S.,
            Oddou,C., Balland,M., Planus,E. and Albiges-Rizo,C.
  TITLE     ICAP-1 monoubiquitylation coordinates matrix density and rigidity
            sensing for cell migration through ROCK2-MRCKalpha balance
  JOURNAL   J Cell Sci 130 (3), 626-636 (2017)
   PUBMED   28049720
  REMARK    GeneRIF: ICAP-1 monoubiquitylation helps in switching from
            ROCK2-mediated to MRCKalpha-mediated cell contractility.
            Erratum:[J Cell Sci. 2017 Mar 15;130(6):1195. doi:
            10.1242/jcs.202218. PMID: 28298614]
REFERENCE   6  (residues 1 to 150)
  AUTHORS   Chang,D.D., Hoang,B.Q., Liu,J. and Springer,T.A.
  TITLE     Molecular basis for interaction between Icap1 alpha PTB domain and
            beta 1 integrin
  JOURNAL   J Biol Chem 277 (10), 8140-8145 (2002)
   PUBMED   11741908
  REMARK    GeneRIF: Site-directed mutagenesis showed that Leu(135), Ile(138),
            and Ile(139) of Icap1 alpha, and Leu(82) and Tyr(144), are required
            for the Icap1 alpha-beta(1) integrin interaction
REFERENCE   7  (residues 1 to 150)
  AUTHORS   Zhang,J., Clatterbuck,R.E., Rigamonti,D., Chang,D.D. and Dietz,H.C.
  TITLE     Interaction between krit1 and icap1alpha infers perturbation of
            integrin beta1-mediated angiogenesis in the pathogenesis of
            cerebral cavernous malformation
  JOURNAL   Hum Mol Genet 10 (25), 2953-2960 (2001)
   PUBMED   11741838
REFERENCE   8  (residues 1 to 150)
  AUTHORS   Gotthardt,M., Trommsdorff,M., Nevitt,M.F., Shelton,J.,
            Richardson,J.A., Stockinger,W., Nimpf,J. and Herz,J.
  TITLE     Interactions of the low density lipoprotein receptor gene family
            with cytosolic adaptor and scaffold proteins suggest diverse
            biological functions in cellular communication and signal
            transduction
  JOURNAL   J Biol Chem 275 (33), 25616-25624 (2000)
   PUBMED   10827173
REFERENCE   9  (residues 1 to 150)
  AUTHORS   Bouvard,D. and Block,M.R.
  TITLE     Calcium/calmodulin-dependent protein kinase II controls integrin
            alpha5beta1-mediated cell adhesion through the integrin cytoplasmic
            domain associated protein-1alpha
  JOURNAL   Biochem Biophys Res Commun 252 (1), 46-50 (1998)
   PUBMED   9813144
REFERENCE   10 (residues 1 to 150)
  AUTHORS   Chang,D.D., Wong,C., Smith,H. and Liu,J.
  TITLE     ICAP-1, a novel beta1 integrin cytoplasmic domain-associated
            protein, binds to a conserved and functionally important NPXY
            sequence motif of beta1 integrin
  JOURNAL   J Cell Biol 138 (5), 1149-1157 (1997)
   PUBMED   9281591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC080162.7.
            
            On Apr 17, 2019 this sequence version replaced XP_005246246.1.
            
            Summary: The cytoplasmic domains of integrins are essential for
            cell adhesion. The protein encoded by this gene binds to the beta1
            integrin cytoplasmic domain. The interaction between this protein
            and beta1 integrin is highly specific. Two isoforms of this protein
            are derived from alternatively spliced transcripts. The shorter
            form of this protein does not interact with the beta1 integrin
            cytoplasmic domain. The longer form is a phosphoprotein and the
            extent of its phosphorylation is regulated by the cell-matrix
            interaction, suggesting an important role of this protein during
            integrin-dependent cell adhesion. Several transcript variants, some
            protein-coding and some non-protein coding, have been found for
            this gene. [provided by RefSeq, Jan 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.333020.1,
                                           ERR3218368.189221.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..150
                     /product="integrin beta-1-binding protein 1 isoform 2"
                     /note="integrin cytoplasmic domain-associated protein
                     1-beta; integrin cytoplasmic domain-associated protein
                     1-alpha; bodenin; integrin beta-1-binding protein 1"
                     /calculated_mol_wt=16009
     Region          1..150
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     CDS             1..150
                     /gene="ITGB1BP1"
                     /gene_synonym="ICAP-1A; ICAP-1alpha; ICAP-1B; ICAP1;
                     ICAP1A; ICAP1B"
                     /coded_by="NM_001369747.1:329..781"
                     /note="isoform 2 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS1663.1"
                     /db_xref="GeneID:9270"
                     /db_xref="HGNC:HGNC:23927"
                     /db_xref="MIM:607153"
ORIGIN      
        1 mfrkgkkrhs ssssqsseis tksksvdssl gglsrsstva sldtdstkss gqsnnnsdtc
       61 aefrikyvga ieklklsegk glegpldlin yidvaqqdgk lpfvppeeef imgvskygik
      121 vstsdqyeqa qaickvlsta fdsvltsekp
//
LOCUS       NP_009138                482 aa            linear   PRI 27-APR-2025
DEFINITION  dual specificity protein phosphatase 10 [Homo sapiens].
ACCESSION   NP_009138 XP_005273082
VERSION     NP_009138.1
DBSOURCE    REFSEQ: accession NM_007207.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Xiao,F., Zhu,H., Guo,Y., Zhang,Z., Sun,G., Huang,K., Guo,H. and
            Hu,G.
  TITLE     DUSP10 is a novel immune-related biomarker connected with survival
            and cellular proliferation in lower-grade glioma
  JOURNAL   Aging (Albany NY) 15 (12), 5673-5697 (2023)
   PUBMED   37387540
  REMARK    GeneRIF: DUSP10 is a novel immune-related biomarker connected with
            survival and cellular proliferation in lower-grade glioma.
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhou,W., Xu,Y., Zhang,J., Zhang,P., Yao,Z., Yan,Z., Wang,H.,
            Chu,J., Yao,S., Zhao,S., Yang,S., Guo,Y., Miao,J., Liu,K.,
            Chan,W.C., Xia,Q. and Liu,Y.
  TITLE     MiRNA-363-3p/DUSP10/JNK axis mediates chemoresistance by enhancing
            DNA damage repair in diffuse large B-cell lymphoma
  JOURNAL   Leukemia 36 (7), 1861-1869 (2022)
   PUBMED   35488020
  REMARK    GeneRIF: MiRNA-363-3p/DUSP10/JNK axis mediates chemoresistance by
            enhancing DNA damage repair in diffuse large B-cell lymphoma.
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Foray,A.P., Candon,S., Hildebrand,S., Marquet,C., Valette,F.,
            Pecquet,C., Lemoine,S., Langa-Vives,F., Dumas,M., Hu,P.,
            Santamaria,P., You,S., Lyon,S., Scott,L., Bu,C.H., Wang,T., Xu,D.,
            Moresco,E.M.Y., Scazzocchio,C., Bach,J.F., Beutler,B. and
            Chatenoud,L.
  TITLE     De novo germline mutation in the dual specificity phosphatase 10
            gene accelerates autoimmune diabetes
  JOURNAL   Proc Natl Acad Sci U S A 118 (47) (2021)
   PUBMED   34782469
  REMARK    GeneRIF: De novo germline mutation in the dual specificity
            phosphatase 10 gene accelerates autoimmune diabetes.
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Liu,M., Qin,Y., Hu,Q., Liu,W., Ji,S., Xu,W., Fan,G., Ye,Z.,
            Zhang,Z., Xu,X., Yu,X. and Zhuo,Q.
  TITLE     SETD8 potentiates constitutive ERK1/2 activation via epigenetically
            silencing DUSP10 expression in pancreatic cancer
  JOURNAL   Cancer Lett 499, 265-278 (2021)
   PUBMED   33232789
  REMARK    GeneRIF: SETD8 potentiates constitutive ERK1/2 activation via
            epigenetically silencing DUSP10 expression in pancreatic cancer.
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Gannam,Z.T.K., Min,K., Shillingford,S.R., Zhang,L., Herrington,J.,
            Abriola,L., Gareiss,P.C., Pantouris,G., Tzouvelekis,A.,
            Kaminski,N., Zhang,X., Yu,J., Jamali,H., Ellman,J.A., Lolis,E.,
            Anderson,K.S. and Bennett,A.M.
  TITLE     An allosteric site on MKP5 reveals a strategy for small-molecule
            inhibition
  JOURNAL   Sci Signal 13 (646) (2020)
   PUBMED   32843541
  REMARK    GeneRIF: An allosteric site on MKP5 reveals a strategy for
            small-molecule inhibition.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Masuda,K., Shima,H., Kikuchi,K., Watanabe,Y. and Matsuda,Y.
  TITLE     Expression and comparative chromosomal mapping of MKP-5 genes
            DUSP10/Dusp10
  JOURNAL   Cytogenet Cell Genet 90 (1-2), 71-74 (2000)
   PUBMED   11060451
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Theodosiou,A., Smith,A., Gillieron,C., Arkinstall,S. and
            Ashworth,A.
  TITLE     MKP5, a new member of the MAP kinase phosphatase family, which
            selectively dephosphorylates stress-activated kinases
  JOURNAL   Oncogene 18 (50), 6981-6988 (1999)
   PUBMED   10597297
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Tanoue,T., Moriguchi,T. and Nishida,E.
  TITLE     Molecular cloning and characterization of a novel dual specificity
            phosphatase, MKP-5
  JOURNAL   J Biol Chem 274 (28), 19949-19956 (1999)
   PUBMED   10391943
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Claudio,J.O., Liew,C.C., Dempsey,A.A., Cukerman,E., Stewart,A.K.,
            Na,E., Atkins,H.L., Iscove,N.N. and Hawley,R.G.
  TITLE     Identification of sequence-tagged transcripts differentially
            expressed within the human hematopoietic hierarchy
  JOURNAL   Genomics 50 (1), 44-52 (1998)
   PUBMED   9628821
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Martell,K.J., Angelotti,T. and Ullrich,A.
  TITLE     The 'VH1-like' dual-specificity protein tyrosine phosphatases
  JOURNAL   Mol Cells 8 (1), 2-11 (1998)
   PUBMED   9571625
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG720911.1, BC031405.1,
            BC063826.1 and AI261880.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005273082.1.
            
            Summary: Dual specificity protein phosphatases inactivate their
            target kinases by dephosphorylating both the
            phosphoserine/threonine and phosphotyrosine residues. They
            negatively regulate members of the MAP kinase superfamily, which is
            associated with cellular proliferation and differentiation.
            Different members of this family of dual specificity phosphatases
            show distinct substrate specificities for MAP kinases, different
            tissue distribution and subcellular localization, and different
            modes of expression induction by extracellular stimuli. This gene
            product binds to and inactivates p38 and SAPK/JNK. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Apr 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the functional protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC031405.1, BC063826.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366899.4/ ENSP00000355866.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..482
                     /product="dual specificity protein phosphatase 10"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="dual specificity phosphatase MKP-5;
                     serine/threonine specific protein phosphatase; map kinase
                     phosphatase 5; mitogen-activated protein kinase
                     phosphatase 5"
                     /calculated_mol_wt=52511
     Region          149..284
                     /region_name="DSP_MapKP"
                     /note="N-terminal regulatory rhodanese domain of dual
                     specificity phosphatases (DSP), such as Mapk Phosphatase.
                     This domain is believed to determine substrate specificity
                     by binding the substrate, such as ERK2, and activating the
                     C-terminal catalytic domain by...; cd01446"
                     /db_xref="CDD:238723"
     Region          199..215
                     /region_name="Interaction with MAP kinases"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6W6.1)"
     Site            202..204
                     /site_type="active"
                     /note="putative substrate binding residues [active]"
                     /db_xref="CDD:238723"
     Region          322..473
                     /region_name="DSP_DUSP10"
                     /note="dual specificity phosphatase domain of dual
                     specificity protein phosphatase 10; cd14567"
                     /db_xref="CDD:350415"
     CDS             1..482
                     /gene="DUSP10"
                     /gene_synonym="MKP-5; MKP5"
                     /coded_by="NM_007207.6:153..1601"
                     /db_xref="CCDS:CCDS1528.1"
                     /db_xref="GeneID:11221"
                     /db_xref="HGNC:HGNC:3065"
                     /db_xref="MIM:608867"
ORIGIN      
        1 mppsplddrv vvalsrpvrp qdlnlcldss ylgsanpgsn shppviattv vslkaanlty
       61 mpsssgsars lncgcssasc ctvatydkdn qaqtqaiaag ttttaigtst tcpanqmvnn
      121 nentgslsps sgvgspvsgt pkqlasikii ypndlakkmt kcskshlpsq gpviidcrpf
      181 meynkshiqg avhincadki srrrlqqgki tvldliscre gkdsfkrifs keiivydent
      241 nepsrvmpsq plhivleslk regkeplvlk gglssfkqnh enlcdnslql qecrevggga
      301 saassllpqp ipttpdiena eltpilpflf lgneqdaqdl dtmqrlnigy vinvtthlpl
      361 yhyekglfny krlpatdsnk qnlrqyfeea fefieeahqc gkgllihcqa gvsrsativi
      421 aylmkhtrmt mtdaykfvkg krpiispnln fmgqllefee dlnngvtpri ltpklmgvet
      481 vv
//
LOCUS       NP_082563                566 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger-containing ubiquitin peptidase 1 isoform 2 [Mus
            musculus].
ACCESSION   NP_082563
VERSION     NP_082563.1
DBSOURCE    REFSEQ: accession NM_028287.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Li,T. and Li,S.
  TITLE     MAVS promotes interferon signaling in RNA virus infection by
            ZUFSP-mediated chromatin regulation
  JOURNAL   Int Immunopharmacol 131, 111819 (2024)
   PUBMED   38460305
  REMARK    GeneRIF: MAVS promotes interferon signaling in RNA virus infection
            by ZUFSP-mediated chromatin regulation.
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Guo,G., Huss,M., Tong,G.Q., Wang,C., Li Sun,L., Clarke,N.D. and
            Robson,P.
  TITLE     Resolution of cell fate decisions revealed by single-cell gene
            expression analysis from zygote to blastocyst
  JOURNAL   Dev Cell 18 (4), 675-685 (2010)
   PUBMED   20412781
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK077304.1, AK046191.1 and AK164710.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK046191.1, AK160928.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164137, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 18.85 cM"
     Protein         1..566
                     /product="zinc finger-containing ubiquitin peptidase 1
                     isoform 2"
                     /EC_number="3.4.19.12"
                     /note="zinc finger with UFM1-specific peptidase domain
                     protein; lys-63-specific deubiquitinase ZUFSP; ubiquitin
                     carboxyl-terminal hydrolase ZUFSP"
                     /calculated_mol_wt=64163
     Region          124..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3T9Z9.2)"
     Region          225..247
                     /region_name="MIU. /evidence=ECO:0000250|UniProtKB:Q96AP4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3T9Z9.2)"
     Region          238..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3T9Z9.2)"
     Region          248..273
                     /region_name="zUBD/ZHA.
                     /evidence=ECO:0000250|UniProtKB:Q96AP4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3T9Z9.2)"
     Site            261
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96AP4; propagated from
                     UniProtKB/Swiss-Prot (Q3T9Z9.2)"
     Region          335..550
                     /region_name="Peptidase_C78"
                     /note="Peptidase family C78; pfam07910"
                     /db_xref="CDD:400318"
     Site            486
                     /site_type="other"
                     /note="Involved in the stabilization of negative charge on
                     the oxyanion by the formation of the oxyanion hole.
                     /evidence=ECO:0000250|UniProtKB:Q96AP4; propagated from
                     UniProtKB/Swiss-Prot (Q3T9Z9.2)"
     CDS             1..566
                     /gene="Zup1"
                     /gene_synonym="2700019D07Rik; DUB; Zufsp"
                     /coded_by="NM_028287.3:261..1961"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS23772.1"
                     /db_xref="GeneID:72580"
                     /db_xref="MGI:MGI:1919830"
ORIGIN      
        1 mlscnicget vnsepdmkah livhmeneii cpfcklsgin yneicfhiet vhfeqnapek
       61 nseklaavqy ghsdrkntnl qstaevtsgi hsacassfpk esseslpkdr tvkheafyte
      121 nitesrkyqk srekkpglse aqgsiyetty sppecpfcgk iegcsqdmei hvktkhasll
      181 esplkdchqp lydcpmcglv ctnyhilqeh vdlhleessf qqgmdrvqcs sdrelahrlq
      241 qeedrkrkse esrqereefq klqrqygldn sggykqqqlr hmelevnrgr mhpsefhsrk
      301 admlesiaig iddgktktsg iiealhryyq ntatdvrcvw lstvvdhfhs sfgdkgwgcg
      361 yrnfqmllss llqsdvygdc lkgmavpcip kiqsmiedaw negfdpqgas qlnnklqgtk
      421 awigaceiyt lltslrvkcr iidfhkstgp lgthprlfew ilnyyssete gtpkivctsk
      481 ppiylqhqgh srtvvgieek knrtlcllvf dpgcpsremq kllkqdmeas slrqlrksvg
      541 nlkhkqyqiv avegvlspee kvvsig
//
LOCUS       NP_001096124             270 aa            linear   PRI 27-APR-2025
DEFINITION  neurotrophin-3 isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_001096124
VERSION     NP_001096124.1
DBSOURCE    REFSEQ: accession NM_001102654.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Xu,X., Song,L., Li,Y., Guo,J., Huang,S., Du,S., Li,W., Cao,R. and
            Cui,S.
  TITLE     Neurotrophin-3 promotes peripheral nerve regeneration by
            maintaining a repair state of Schwann cells after chronic
            denervation via the TrkC/ERK/c-Jun pathway
  JOURNAL   J Transl Med 21 (1), 733 (2023)
   PUBMED   37848983
  REMARK    GeneRIF: Neurotrophin-3 promotes peripheral nerve regeneration by
            maintaining a repair state of Schwann cells after chronic
            denervation via the TrkC/ERK/c-Jun pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wang,H., Zhong,C., Qi,L., Fang,X. and Yuan,Y.
  TITLE     Expression and prognostic impact of NTF3 and TrkC in hepatocellular
            carcinoma
  JOURNAL   Scand J Gastroenterol 58 (11), 1309-1316 (2023)
   PUBMED   37272057
  REMARK    GeneRIF: Expression and prognostic impact of NTF3 and TrkC in
            hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Yang,Z., Zhang,H., Yin,M., Cheng,Z., Jiang,P., Feng,M., Liao,B. and
            Liu,Z.
  TITLE     Neurotrophin3 promotes hepatocellular carcinoma apoptosis through
            the JNK and P38 MAPK pathways
  JOURNAL   Int J Biol Sci 18 (15), 5963-5977 (2022)
   PUBMED   36263167
  REMARK    GeneRIF: Neurotrophin3 promotes hepatocellular carcinoma apoptosis
            through the JNK and P38 MAPK pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Cui,X., Jing,J., Wu,R., Cao,Q., Li,F., Li,K., Wang,S., Yu,L.,
            Schwartz,G., Shi,H., Xue,B. and Shi,H.
  TITLE     Adipose tissue-derived neurotrophic factor 3 regulates sympathetic
            innervation and thermogenesis in adipose tissue
  JOURNAL   Nat Commun 12 (1), 5362 (2021)
   PUBMED   34508100
  REMARK    GeneRIF: Adipose tissue-derived neurotrophic factor 3 regulates
            sympathetic innervation and thermogenesis in adipose tissue.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Rodrigues-Amorim,D., Iglesias-Martinez-Almeida,M.,
            Rivera-Baltanas,T., Fernandez-Palleiro,P., Freiria-Martinez,L.,
            Rodriguez-Jamardo,C., Comis-Tuche,M., Vallejo-Curto,M.D.C.,
            Alvarez-Ariza,M., Lopez-Garcia,M., de Las Heras,E.,
            Garcia-Caballero,A., Olivares,J.M. and Spuch,C.
  TITLE     The Role of the Second Extracellular Loop of Norepinephrine
            Transporter, Neurotrophin-3 and Tropomyosin Receptor Kinase C in T
            Cells: A Peripheral Biomarker in the Etiology of Schizophrenia
  JOURNAL   Int J Mol Sci 22 (16), 8499 (2021)
   PUBMED   34445205
  REMARK    GeneRIF: The Role of the Second Extracellular Loop of
            Norepinephrine Transporter, Neurotrophin-3 and Tropomyosin Receptor
            Kinase C in T Cells: A Peripheral Biomarker in the Etiology of
            Schizophrenia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Kalcheim,C., Carmeli,C. and Rosenthal,A.
  TITLE     Neurotrophin 3 is a mitogen for cultured neural crest cells
  JOURNAL   Proc Natl Acad Sci U S A 89 (5), 1661-1665 (1992)
   PUBMED   1542658
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Ozcelik,T., Rosenthal,A. and Francke,U.
  TITLE     Chromosomal mapping of brain-derived neurotrophic factor and
            neurotrophin-3 genes in man and mouse
  JOURNAL   Genomics 10 (3), 569-575 (1991)
   PUBMED   1889807
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Maisonpierre,P.C., Le Beau,M.M., Espinosa,R. 3rd, Ip,N.Y.,
            Belluscio,L., de la Monte,S.M., Squinto,S., Furth,M.E. and
            Yancopoulos,G.D.
  TITLE     Human and rat brain-derived neurotrophic factor and neurotrophin-3:
            gene structures, distributions, and chromosomal localizations
  JOURNAL   Genomics 10 (3), 558-568 (1991)
   PUBMED   1889806
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Hallbook,F., Ibanez,C.F. and Persson,H.
  TITLE     Evolutionary studies of the nerve growth factor family reveal a
            novel member abundantly expressed in Xenopus ovary
  JOURNAL   Neuron 6 (5), 845-858 (1991)
   PUBMED   2025430
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Jones,K.R. and Reichardt,L.F.
  TITLE     Molecular cloning of a human gene that is a member of the nerve
            growth factor family
  JOURNAL   Proc Natl Acad Sci U S A 87 (20), 8060-8064 (1990)
   PUBMED   2236018
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007848.11, BU939830.1,
            CN267386.1, BC069773.1 and CD672441.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            neurotrophin family, that controls survival and differentiation of
            mammalian neurons. This protein is closely related to both nerve
            growth factor and brain-derived neurotrophic factor. It may be
            involved in the maintenance of the adult nervous system, and may
            affect development of neurons in the embryo when it is expressed in
            human placenta. NTF3-deficient mice generated by gene targeting
            display severe movement defects of the limbs. The mature peptide of
            this protein is identical in all mammals examined including human,
            pig, rat and mouse. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.232075.1,
                                           SRR3476690.165428.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000423158.4/ ENSP00000397297.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..270
                     /product="neurotrophin-3 isoform 1 preproprotein"
                     /note="neurotrophic factor; nerve growth factor 2"
                     /calculated_mol_wt=27453
     sig_peptide     1..29
                     /calculated_mol_wt=3365
     proprotein      30..270
                     /product="neurotrophin-3 isoform 1 proprotein"
                     /calculated_mol_wt=27453
     Region          33..146
                     /region_name="NTF3_N"
                     /note="Neutrophin-3 N-terminus; pfam19338"
                     /db_xref="CDD:437170"
     mat_peptide     152..270
                     /product="neurotrophin-3 isoform 1"
                     /calculated_mol_wt=13625
     Region          157..268
                     /region_name="NGF"
                     /note="Nerve growth factor family; pfam00243"
                     /db_xref="CDD:459728"
     CDS             1..270
                     /gene="NTF3"
                     /gene_synonym="HDNF; NGF-2; NGF2; NT-3; NT3"
                     /coded_by="NM_001102654.2:218..1030"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS44806.1"
                     /db_xref="GeneID:4908"
                     /db_xref="HGNC:HGNC:8023"
                     /db_xref="MIM:162660"
ORIGIN      
        1 mvtfatilqv nkvmsilfyv iflaylrgiq gnnmdqrslp edslnsliik liqadilknk
       61 lskqmvdvke nyqstlpkae apreperggp aksafqpvia mdtellrqqr rynsprvlls
      121 dstplepppl ylmedyvgsp vvanrtsrrk ryaehkshrg eysvcdsesl wvtdkssaid
      181 irghqvtvlg eiktgnspvk qyfyetrcke arpvkngcrg iddkhwnsqc ktsqtyvral
      241 tsennklvgw rwiridtscv calsrkigrt
//
LOCUS       NP_112518                368 aa            linear   ROD 27-APR-2025
DEFINITION  endophilin-A2 [Rattus norvegicus].
ACCESSION   NP_112518
VERSION     NP_112518.1
DBSOURCE    REFSEQ: accession NM_031239.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Norin,U., Rintisch,C., Meng,L., Forster,F., Ekman,D., Tuncel,J.,
            Klocke,K., Backlund,J., Yang,M., Bonner,M.Y., Lahore,G.F.,
            James,J., Shchetynsky,K., Bergquist,M., Gjertsson,I., Hubner,N.,
            Backdahl,L. and Holmdahl,R.
  TITLE     Endophilin A2 deficiency protects rodents from autoimmune arthritis
            by modulating T cell activation
  JOURNAL   Nat Commun 12 (1), 610 (2021)
   PUBMED   33504785
  REMARK    GeneRIF: Endophilin A2 deficiency protects rodents from autoimmune
            arthritis by modulating T cell activation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Liu,Y., Shen,H.J., Wang,X.Q., Liu,H.Q., Zheng,L.Y. and Luo,J.D.
  TITLE     EndophilinA2 protects against angiotensin II-induced cardiac
            hypertrophy by inhibiting angiotensin II type 1 receptor
            trafficking in neonatal rat cardiomyocytes
  JOURNAL   J Cell Biochem 119 (10), 8290-8303 (2018)
   PUBMED   29923351
  REMARK    GeneRIF: EndophilinA2 protects against angiotensin II-induced
            cardiac hypertrophy by inhibiting angiotensin II type 1 receptor
            trafficking in neonatal rat cardiomyocytes.
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Liu,Y., Liu,H.Q., Xiao,J.Y., Ma,K.T., Wang,X.Q., Shen,H.J. and
            Luo,J.D.
  TITLE     Autophagy is involved in the protective effect of endophilin A2 on
            H2O2-induced apoptosis in H9C2 cardiomyocytes
  JOURNAL   Biochem Biophys Res Commun 499 (2), 299-306 (2018)
   PUBMED   29574155
  REMARK    GeneRIF: EndoA2 inhibited hydrogen peroxide-induced apoptosis in
            H9C2 cardiomyocytes.
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Zhang,J., Yin,Y., Ji,Z., Cai,Z., Zhao,B., Li,J., Tan,M. and Guo,G.
  TITLE     Endophilin2 Interacts with GluA1 to Mediate AMPA Receptor
            Endocytosis Induced by Oligomeric Amyloid-beta
  JOURNAL   Neural Plast 2017, 8197085 (2017)
   PUBMED   28758034
  REMARK    GeneRIF: Study demonstrates that endophilin2 does not contribute to
            constitutive AMPA receptor endocytosis.
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Wuertenberger,S. and Groemping,Y.
  TITLE     A single PXXP motif in the C-terminal region of srGAP3 mediates
            binding to multiple SH3 domains
  JOURNAL   FEBS Lett 589 (10), 1156-1163 (2015)
   PUBMED   25819436
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Ralser,M., Nonhoff,U., Albrecht,M., Lengauer,T., Wanker,E.E.,
            Lehrach,H. and Krobitsch,S.
  TITLE     Ataxin-2 and huntingtin interact with endophilin-A complexes to
            function in plastin-associated pathways
  JOURNAL   Hum Mol Genet 14 (19), 2893-2909 (2005)
   PUBMED   16115810
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Chen,Y., Deng,L., Maeno-Hikichi,Y., Lai,M., Chang,S., Chen,G. and
            Zhang,J.F.
  TITLE     Formation of an endophilin-Ca2+ channel complex is critical for
            clathrin-mediated synaptic vesicle endocytosis
  JOURNAL   Cell 115 (1), 37-48 (2003)
   PUBMED   14532001
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Ringstad,N., Nemoto,Y. and De Camilli,P.
  TITLE     Differential expression of endophilin 1 and 2 dimers at central
            nervous system synapses
  JOURNAL   J Biol Chem 276 (44), 40424-40430 (2001)
   PUBMED   11518713
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Nemoto,Y., Wenk,M.R., Watanabe,M., Daniell,L., Murakami,T.,
            Ringstad,N., Yamada,H., Takei,K. and De Camilli,P.
  TITLE     Identification and characterization of a synaptojanin 2 splice
            isoform predominantly expressed in nerve terminals
  JOURNAL   J Biol Chem 276 (44), 41133-41142 (2001)
   PUBMED   11498538
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Ringstad,N., Nemoto,Y. and De Camilli,P.
  TITLE     The SH3p4/Sh3p8/SH3p13 protein family: binding partners for
            synaptojanin and dynamin via a Grb2-like Src homology 3 domain
  JOURNAL   Proc Natl Acad Sci U S A 94 (16), 8569-8574 (1997)
   PUBMED   9238017
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB615317.1 and BC070893.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070893.1, AB008161.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..368
                     /product="endophilin-A2"
                     /note="endophilin-2; SH3 domain protein 2B; SH3
                     domain-containing GRB2-like protein 1; SH3-domain
                     GRB2-like 1; SH3 domain-containing GRB2-like 1"
                     /calculated_mol_wt=41361
     Region          1..21
                     /region_name="Membrane-binding amphipathic helix.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O35964.1)"
     Region          25..247
                     /region_name="BAR_Endophilin_A"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of
                     Endophilin-A; cd07592"
                     /db_xref="CDD:153276"
     Site            order(38..39,42..43,45..46,49..50,53,57,60..61,89..90,
                     92..93,96..97,100,103..104,108..110,113..114,208..209,
                     211..213,215..216,219,222..223,225..227,229..230,233..234,
                     236..237,240,244)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153276"
     Site            order(45,53,65,152,156,159,164..165,173..174,177,184)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153276"
     Region          60..87
                     /region_name="Required for dimerization upon membrane
                     association. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O35964.1)"
     Region          218..254
                     /region_name="Interaction with ARC.
                     /evidence=ECO:0000269|PubMed:17088211"
                     /note="propagated from UniProtKB/Swiss-Prot (O35964.1)"
     Region          243..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35964.1)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35964.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99961; propagated from
                     UniProtKB/Swiss-Prot (O35964.1)"
     Region          309..363
                     /region_name="SH3_Endophilin_A"
                     /note="Src homology 3 domain of Endophilin-A; cd11803"
                     /db_xref="CDD:212737"
     Site            order(315,317,320,324,342..343,356,358..359)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212737"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62419; propagated from
                     UniProtKB/Swiss-Prot (O35964.1)"
     CDS             1..368
                     /gene="Sh3gl1"
                     /gene_synonym="SH3P8"
                     /coded_by="NM_031239.3:142..1248"
                     /db_xref="GeneID:81922"
                     /db_xref="RGD:708456"
ORIGIN      
        1 msvaglkkqf ykasqlvsek vggaegtkld ddfremekkv ditskavaev lvrtieylqp
       61 npasrakltm lntvskirgq vknpgypqse gllgecmvrh gkelggesnf gdalldages
      121 mkrlaevkds ldievkqnfi dplqnlcdkd lkeiqhhlkk legrrldfdy kkkrqgkipd
      181 eelrqalekf eeskevaets mhnlletdie qvsqlsalvd aqldyhrqav qileeladkl
      241 krrvreassr prrefkprpq epfelgeleq pnggfpcasa pkitasssfr sgdkptrtps
      301 ksmppldqps ckalydfepe ndgelgfreg dlitltnqid enwyegmlhg qsgffplsyv
      361 qvlvplpq
//
LOCUS       NP_001244333             571 aa            linear   MAM 27-APR-2025
DEFINITION  keratin, type II cytoskeletal 59 kDa, component IV [Bos taurus].
ACCESSION   NP_001244333 XP_002687294 XP_585454
VERSION     NP_001244333.1
DBSOURCE    REFSEQ: accession NM_001257404.2
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Jorcano,J.L., Franz,J.K. and Franke,W.W.
  TITLE     Amino acid sequence diversity between bovine epidermal cytokeratin
            polypeptides of the basic (type II) subfamily as determined from
            cDNA clones
  JOURNAL   Differentiation 28 (2), 155-163 (1984)
   PUBMED   6084625
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000005.1.
            
            On or before Apr 12, 2012 this sequence version replaced
            XP_585454.1, XP_002687294.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5721695.7786.1, SRR5721696.8337.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03145412, SAMN03145413
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="5"
                     /map="5"
                     /breed="Hereford"
     Protein         1..571
                     /product="keratin, type II cytoskeletal 59 kDa, component
                     IV"
                     /note="cytokeratin type II, component IV; keratin
                     K6-gamma"
                     /calculated_mol_wt=60725
     Region          16..159
                     /region_name="Keratin_2_head"
                     /note="Keratin type II head; pfam16208"
                     /db_xref="CDD:465068"
     Region          162..475
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     CDS             1..571
                     /gene="KRT6B"
                     /gene_synonym="KERIV"
                     /coded_by="NM_001257404.2:71..1786"
                     /db_xref="BGD:BT14201"
                     /db_xref="GeneID:404115"
ORIGIN      
        1 msckstvktq sisrrgfsag sarvpgvcrs gfssvslsrs rgsgglagvc ggagfgsrsl
       61 yglggskris iaggscvigg gyggrigvgy gfgggagsgf gfgagagsgf glgggagfgg
      121 gfggpgfpvc ppggiqevtv nqslltplnl qidptiqrvr teereqiktl nnkfasfidk
      181 vrfleqqnkv ldtkwtllqe qgtrtvrqnl eplfeqyinn lrrqldsilg ergrldselr
      241 gmqdtvedfk nkyedeinkr taaenefvkl kkdvdiaymn kvelqakvda ltdeinflrt
      301 fydaelaqmq thisdtsvvl smdnnrnldl dsiiaevkaq yeeiaqrsra eaeswyqsky
      361 eelrvtagrh gddlrntkqe iseinrviqr lrseidhvkk qcaslqsaia daeqrgelal
      421 kdarskladl edalqkakqd marllkeyqe lmnvklaldv eiatyrklle geecrlsgeg
      481 vgqvnisvvq stvsggygga ggyggasglg sglgvsggsg ysyssghslg ggfssgsgra
      541 igcgfgssgg ssstikyttt tssssrkgyk h
//
LOCUS       NP_001025056             214 aa            linear   PRI 27-APR-2025
DEFINITION  ceramide-1-phosphate transfer protein [Homo sapiens].
ACCESSION   NP_001025056 NP_085052 XP_496335
VERSION     NP_001025056.1
DBSOURCE    REFSEQ: accession NM_001029885.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Zhang,Y., Ji,S., Zhang,X., Lu,M., Hu,Y., Han,Y., Shui,G., Lam,S.M.
            and Zou,X.
  TITLE     Human CPTP promotes growth and metastasis via sphingolipid
            metabolite ceramide and PI4KA/AKT signaling in pancreatic cancer
            cells
  JOURNAL   Int J Biol Sci 18 (13), 4963-4983 (2022)
   PUBMED   35982909
  REMARK    GeneRIF: Human CPTP promotes growth and metastasis via sphingolipid
            metabolite ceramide and PI4KA/AKT signaling in pancreatic cancer
            cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Gao,Y.G., McDonald,J., Malinina,L., Patel,D.J. and Brown,R.E.
  TITLE     Ceramide-1-phosphate transfer protein promotes sphingolipid
            reorientation needed for binding during membrane interaction
  JOURNAL   J Lipid Res 63 (1), 100151 (2022)
   PUBMED   34808193
  REMARK    GeneRIF: Ceramide-1-phosphate transfer protein promotes
            sphingolipid reorientation needed for binding during membrane
            interaction.
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Zhang,Y., Zhang,X., Lu,M. and Zou,X.
  TITLE     Ceramide-1-phosphate and its transfer proteins in eukaryotes
  JOURNAL   Chem Phys Lipids 240, 105135 (2021)
   PUBMED   34499882
  REMARK    GeneRIF: Ceramide-1-phosphate and its transfer proteins in
            eukaryotes.
            Review article
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Gao,Y.G., Zhai,X., Boldyrev,I.A., Molotkovsky,J.G., Patel,D.J.,
            Malinina,L. and Brown,R.E.
  TITLE     Ceramide-1-phosphate transfer protein (CPTP) regulation by
            phosphoinositides
  JOURNAL   J Biol Chem 296, 100600 (2021)
   PUBMED   33781749
  REMARK    GeneRIF: Ceramide-1-phosphate transfer protein (CPTP) regulation by
            phosphoinositides.
REFERENCE   5  (residues 1 to 214)
  AUTHORS   Mishra,S.K., Gao,Y.G., Deng,Y., Chalfant,C.E., Hinchcliffe,E.H. and
            Brown,R.E.
  TITLE     CPTP: A sphingolipid transfer protein that regulates autophagy and
            inflammasome activation
  JOURNAL   Autophagy 14 (5), 862-879 (2018)
   PUBMED   29164996
  REMARK    GeneRIF: These findings identify human CPTP as an endogenous
            regulator of early-stage autophagosome assembly and
            inflammasome-driven, pro-inflammatory cytokine generation and
            release.
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Simanshu,D.K., Kamlekar,R.K., Wijesinghe,D.S., Zou,X., Zhai,X.,
            Mishra,S.K., Molotkovsky,J.G., Malinina,L., Hinchcliffe,E.H.,
            Chalfant,C.E., Brown,R.E. and Patel,D.J.
  TITLE     Non-vesicular trafficking by a ceramide-1-phosphate transfer
            protein regulates eicosanoids
  JOURNAL   Nature 500 (7463), 463-467 (2013)
   PUBMED   23863933
  REMARK    GeneRIF: a ubiquitously expressed lipid transfer protein, human
            GLTPD1, named here CPTP, is shown to specifically transfer C1P
            between membranes.
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 214)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 214)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139287.24.
            
            On or before Aug 4, 2007 this sequence version replaced
            NP_085052.1, XP_496335.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.827296.1,
                                           SRR3476690.456880.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000343938.9/ ENSP00000343890.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..214
                     /product="ceramide-1-phosphate transfer protein"
                     /note="glycolipid transfer protein domain-containing
                     protein 1; GLTP domain-containing protein 1; glycolipid
                     transfer protein domain containing 1"
                     /calculated_mol_wt=24234
     Region          27..173
                     /region_name="GLTP"
                     /note="Glycolipid transfer protein (GLTP); pfam08718"
                     /db_xref="CDD:462575"
     CDS             1..214
                     /gene="CPTP"
                     /gene_synonym="GLTPD1"
                     /coded_by="NM_001029885.2:377..1021"
                     /db_xref="CCDS:CCDS30555.1"
                     /db_xref="GeneID:80772"
                     /db_xref="HGNC:HGNC:28116"
                     /db_xref="MIM:615467"
ORIGIN      
        1 mddsetgfnl kvvlvsfkqc ldekeevlld pyiaswkglv rflnslgtif sfiskdvvsk
       61 lrimerlrgg pqsehyrslq amvahelsnr lvdlerrshh pesgcrtvlr lhralhwlql
      121 fleglrtspe dartsalcad synaslaayh pwvvrravtv afctlptrev fleamnvgpp
      181 eqavqmlgea lpfiqrvynv sqklyaehsl ldlp
//
LOCUS       NP_001008801             522 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 468 isoform 2 [Homo sapiens].
ACCESSION   NP_001008801
VERSION     NP_001008801.1
DBSOURCE    REFSEQ: accession NM_001008801.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Zhu,J., Qiu,X., Jin,X., Nie,X., Ou,S., Wu,G., Shen,J. and Zhang,R.
  TITLE     ZNF468-mediated epigenetic upregulation of VEGF-C facilitates
            lymphangiogenesis and lymphatic metastasis in ESCC via PI3K/Akt and
            ERK1/2 signaling pathways
  JOURNAL   Cell Oncol (Dordr) 47 (5), 1927-1942 (2024)
   PUBMED   39141315
  REMARK    GeneRIF: ZNF468-mediated epigenetic upregulation of VEGF-C
            facilitates lymphangiogenesis and lymphatic metastasis in ESCC via
            PI3K/Akt and ERK1/2 signaling pathways.
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Bai,G., Mahati,S., Tulahong,A., Eli,M. and Mao,R.
  TITLE     ZNF468 inhibits irradiation-induced G2/M cell cycle arrest and
            apoptosis by facilitating AURKA transcription in Esophageal
            Squamous Cell Carcinoma
  JOURNAL   Biochem Biophys Res Commun 703, 149687 (2024)
   PUBMED   38368674
  REMARK    GeneRIF: ZNF468 inhibits irradiation-induced G2/M cell cycle arrest
            and apoptosis by facilitating AURKA transcription in Esophageal
            Squamous Cell Carcinoma.
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Sun,L., Gu,S., Li,N., Zheng,D., Sun,Y., Li,D., Ji,C., Ying,K.,
            Xie,Y. and Mao,Y.
  TITLE     A novel zinc finger gene ZNF468 with two co-expressional splice
            variants, ZNF468.1 and ZNF468.2
  JOURNAL   Biochem Genet 43 (5-6), 271-286 (2005)
   PUBMED   16144304
  REMARK    GeneRIF: 2 splice variants ZNF468.1 and ZNF468.2 contain 11
            C2H2-type zinc finger motifs at their C-termini. They are widely
            expressed in normal human tissues, except in heart and brain, and
            they are also co-expressional.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY442330.1, BC037409.1, AK025501.1 and AC008813.6.
            
            Transcript Variant: This variant (2) encodes the longer isoform
            (2).
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR936695.1, SRR1803612.67081.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267753 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000595646.6/ ENSP00000470381.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..522
                     /product="zinc finger protein 468 isoform 2"
                     /note="zinc finger protein ZNF468"
                     /calculated_mol_wt=60442
     Region          7..48
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(250,252,254,256..257,260..261,264,278,280,284..285,
                     288..289,292,306,308,310,312..313,316..317,320)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..321
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <305..478
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          329..349
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(362,364,366,368..369,372..373,376,390,392,396..397,
                     400..401,404,418,420,422,424..425,428..429,432)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          385..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          481..506
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..522
                     /gene="ZNF468"
                     /coded_by="NM_001008801.2:122..1690"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33094.1"
                     /db_xref="GeneID:90333"
                     /db_xref="HGNC:HGNC:33105"
                     /db_xref="MIM:616841"
ORIGIN      
        1 malpqglltf rdvaiefsqe ewkcldpaqr tlyrdvmlen yrnlvsldis skcmlktlss
       61 tgqgntevih tgtlhrqash higefcfhei ekdihgfefq wkedetngha apmteikela
      121 gstgqhdqrh agnkrikdql gssfhlhlpe phifqsegki gnqveksinn assvstsqri
      181 ccrpkthisn kygnnslhss lltqkwevhm reksfeciqs fksfncssll kkhqiihlee
      241 kqckcdvcgk vfnqkrylac hrrchtgekp ykcnecgktf ghnsslfihk alhtgekpye
      301 ceecdkvfsr kshlerhkri htgekpykck vcdeafayns ylakhtilht gekpytcnec
      361 gkvfnrlstl arhhrlhtge kpykceecdk vfsrkshler hrrihsgekp ykceecckvf
      421 srksnlerhr rihtgekpyk ckvcdkafqr dshlaqhqrv htgekpykcn ecgktfgqts
      481 sliihrrlht gekpykcnec gktfsqmssl vyhhrlhsge kp
//
LOCUS       NP_060452                490 aa            linear   PRI 27-APR-2025
DEFINITION  sushi domain-containing protein 4 isoform a precursor [Homo
            sapiens].
ACCESSION   NP_060452
VERSION     NP_060452.3
DBSOURCE    REFSEQ: accession NM_017982.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Zhong,Y., Zheng,C., Zhang,W., Wu,H., Zhang,Q., Li,D., Ju,H.,
            Feng,H., Chen,Y., Fan,Y., Chen,W., Wang,M. and Wang,G.
  TITLE     Pan-cancer analysis of Sushi domain-containing protein 4 (SUSD4)
            and validated in colorectal cancer
  JOURNAL   Aging (Albany NY) 16 (7), 6417-6444 (2024)
   PUBMED   38579174
  REMARK    GeneRIF: Pan-cancer analysis of Sushi domain-containing protein 4
            (SUSD4) and validated in colorectal cancer.
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Papadakos,K.S., Ekstrom,A., Slipek,P., Skourti,E., Reid,S.,
            Pietras,K. and Blom,A.M.
  TITLE     Sushi domain-containing protein 4 binds to epithelial growth factor
            receptor and initiates autophagy in an EGFR phosphorylation
            independent manner
  JOURNAL   J Exp Clin Cancer Res 41 (1), 363 (2022)
   PUBMED   36578014
  REMARK    GeneRIF: Sushi domain-containing protein 4 binds to epithelial
            growth factor receptor and initiates autophagy in an EGFR
            phosphorylation independent manner.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Englund,E., Reitsma,B., King,B.C., Escudero-Esparza,A., Owen,S.,
            Orimo,A., Okroj,M., Anagnostaki,L., Jiang,W.G., Jirstrom,K. and
            Blom,A.M.
  TITLE     The human complement inhibitor Sushi Domain-Containing Protein 4
            (SUSD4) expression in tumor cells and infiltrating T cells is
            associated with better prognosis of breast cancer patients
  JOURNAL   BMC Cancer 15, 737 (2015)
   PUBMED   26480818
  REMARK    GeneRIF: SUSD4 expression in both breast cancer cells and T cells
            infiltrating the tumor-associated stroma is useful to predict
            better prognosis of breast cancer patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Holmquist,E., Okroj,M., Nodin,B., Jirstrom,K. and Blom,A.M.
  TITLE     Sushi domain-containing protein 4 (SUSD4) inhibits complement by
            disrupting the formation of the classical C3 convertase
  JOURNAL   FASEB J 27 (6), 2355-2366 (2013)
   PUBMED   23482636
  REMARK    GeneRIF: Membrane-bound isoform SUSD4a inhibits the classical and
            alternative complement pathways when expressed on the surface of
            Chinese hamster cells but not when expressed as a soluble,
            truncated protein.
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Tu,Z., Cohen,M., Bu,H. and Lin,F.
  TITLE     Tissue distribution and functional analysis of Sushi
            domain-containing protein 4
  JOURNAL   Am J Pathol 176 (5), 2378-2384 (2010)
   PUBMED   20348246
  REMARK    GeneRIF: analysis of cloning, expression, refolding, and tissue
            distribution of Sushi domain-containing protein 4
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 490)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA125047.1, AY358495.1, AK096265.1 and BF446433.1.
            
            On Jun 2, 2007 this sequence version replaced NP_060452.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.169269.1,
                                           SRR1803611.82764.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366878.9/ ENSP00000355843.4
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..490
                     /product="sushi domain-containing protein 4 isoform a
                     precursor"
                     /note="YHGM196; sushi domain-containing protein 4;
                     testicular secretory protein Li 55"
                     /calculated_mol_wt=49052
     sig_peptide     1..41
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VX71.1)"
                     /calculated_mol_wt=4744
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VX71.1)"
     Region          30..>238
                     /region_name="PHA02639"
                     /note="EEV host range protein; Provisional"
                     /db_xref="CDD:165022"
     mat_peptide     42..490
                     /product="Sushi domain-containing protein 4.
                     /id=PRO_0000251975"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VX71.1)"
                     /calculated_mol_wt=49052
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VX71.1)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VX71.1)"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VX71.1)"
     Region          243..297
                     /region_name="CCP"
                     /note="Domain abundant in complement control proteins;
                     SUSHI repeat; short complement-like repeat (SCR);
                     smart00032"
                     /db_xref="CDD:214478"
     Site            order(253,275)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Site            320..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VX71.1)"
     Region          401..490
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VX71.1)"
     CDS             1..490
                     /gene="SUSD4"
                     /gene_synonym="PRO222"
                     /coded_by="NM_017982.4:156..1628"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS41471.1"
                     /db_xref="GeneID:55061"
                     /db_xref="HGNC:HGNC:25470"
                     /db_xref="MIM:615827"
ORIGIN      
        1 myhgmnpsng dgfleqqqqq qqpqspqrll avilwfqlal cfgpaqltgg fddlqvcadp
       61 gipengfrtp sggvffegsv arfhcqdgfk lkgatkrlcl khfngtlgwi psdnsicvqe
      121 dcripqieda eihnktyrhg ekliitcheg fkirypdlhn mvslcrddgt wnnlpicqgc
      181 lrplassngy vniselqtsf pvgtvisyrc fpgfkldgsa yleclqnliw ssspprclal
      241 evcplppmvs hgdfvchprp cerynhgtvv efycdpgysl tsdykyitcq ygewfpsyqv
      301 ycikseqtwp sthetllttw kivaftatsv llvlllvila rmfqtkfkah fpprgpprss
      361 ssdpdfvvvd gvpvmlpsyd eavsgglsal gpgymasvgq gcplpvddqs ppaypgsgdt
      421 dtgpgesetc dsvsgssell qslyspprcq esthpasdnp diiastaeev astspgidia
      481 deiplmeedp
//
LOCUS       NP_001537                161 aa            linear   PRI 27-APR-2025
DEFINITION  DNA-binding protein inhibitor ID-4 [Homo sapiens].
ACCESSION   NP_001537
VERSION     NP_001537.1
DBSOURCE    REFSEQ: accession NM_001546.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Choi,J.H., Park,J.D., Choi,S.H., Ko,E.S., Jang,H.J. and Park,K.S.
  TITLE     ELK3-ID4 axis governs the metastatic features of triple negative
            breast cancer
  JOURNAL   Oncol Res 32 (1), 127-138 (2023)
   PUBMED   38188675
  REMARK    GeneRIF: ELK3-ID4 axis governs the metastatic features of triple
            negative breast cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Qin,W., Zhang,J., Rong,R., Zhang,L., Gao,H., Liu,C., Ren,Q.,
            Zheng,G., Wang,J., Meng,L., Qiao,S., Qian,R., Zhou,C., Wang,H. and
            Zhang,Y.
  TITLE     Osteoglycin (OGN) promotes tumorigenesis of pancreatic cancer cell
            via targeting ID4
  JOURNAL   Tissue Cell 78, 101867 (2022)
   PUBMED   35908351
  REMARK    GeneRIF: Osteoglycin (OGN) promotes tumorigenesis of pancreatic
            cancer cell via targeting ID4.
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Feng,Y., Wang,X., Huang,C., Zhang,D., Liu,T., Zhang,C., Zhang,Y.,
            Ji,D., Tang,J. and Sun,Y.
  TITLE     Upregulated circTMEM59 Inhibits Cell Growth and Metastasis by
            miR-668-3p/ID4 Axis in Colorectal Cancer
  JOURNAL   Oxid Med Cell Longev 2022, 7242124 (2022)
   PUBMED   35656024
  REMARK    GeneRIF: Upregulated circTMEM59 Inhibits Cell Growth and Metastasis
            by miR-668-3p/ID4 Axis in Colorectal Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Nasif,D., Real,S., Roque,M. and Branham,M.T.
  TITLE     CDC42 as an epigenetic regulator of ID4 in triple-negative breast
            tumors
  JOURNAL   Breast Cancer 29 (3), 562-573 (2022)
   PUBMED   35094293
  REMARK    GeneRIF: CDC42 as an epigenetic regulator of ID4 in triple-negative
            breast tumors.
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Zhu,K., Lin,J., Chen,S. and Xu,Q.
  TITLE     miR-9-5p Promotes Lung Adenocarcinoma Cell Proliferation, Migration
            and Invasion by Targeting ID4
  JOURNAL   Technol Cancer Res Treat 20, 15330338211048592 (2021)
   PUBMED   34723712
  REMARK    GeneRIF: miR-9-5p Promotes Lung Adenocarcinoma Cell Proliferation,
            Migration and Invasion by Targeting ID4.
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Lasorella,A., Benezra,R. and Iavarone,A.
  TITLE     The ID proteins: master regulators of cancer stem cells and tumour
            aggressiveness
  JOURNAL   Nat Rev Cancer 14 (2), 77-91 (2014)
   PUBMED   24442143
  REMARK    Review article
REFERENCE   7  (residues 1 to 161)
  AUTHORS   Rigolet,M., Rich,T., Gross-Morand,M.S., Molina-Gomes,D.,
            Viegas-Pequignot,E. and Junien,C.
  TITLE     cDNA cloning, tissue distribution and chromosomal localization of
            the human ID4 gene
  JOURNAL   DNA Res 5 (5), 309-313 (1998)
   PUBMED   9872455
REFERENCE   8  (residues 1 to 161)
  AUTHORS   Stewart,H.J., Zoidl,G., Rossner,M., Brennan,A., Zoidl,C.,
            Nave,K.A., Mirsky,R. and Jessen,K.R.
  TITLE     Helix-loop-helix proteins in Schwann cells: a study of regulation
            and subcellular localization of Ids, REB, and E12/47 during
            embryonic and postnatal development
  JOURNAL   J Neurosci Res 50 (5), 684-701 (1997)
   PUBMED   9418957
REFERENCE   9  (residues 1 to 161)
  AUTHORS   Loveys,D.A., Streiff,M.B. and Kato,G.J.
  TITLE     E2A basic-helix-loop-helix transcription factors are negatively
            regulated by serum growth factors and by the Id3 protein
  JOURNAL   Nucleic Acids Res 24 (14), 2813-2820 (1996)
   PUBMED   8759016
REFERENCE   10 (residues 1 to 161)
  AUTHORS   Pagliuca,A., Bartoli,P.C., Saccone,S., Della Valle,G. and Lania,L.
  TITLE     Molecular cloning of ID4, a novel dominant negative
            helix-loop-helix human gene on chromosome 6p21.3-p22
  JOURNAL   Genomics 27 (1), 200-203 (1995)
   PUBMED   7665172
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB461864.1, BC014941.1,
            AL022726.1 and AI692586.1.
            
            Summary: This gene encodes a member of the inhibitor of DNA binding
            (ID) protein family. The encoded protein lacks DNA binding ability,
            and instead regulates gene expression through binding to and
            inhibiting basic helix-loop-helix transcription factors. This
            protein has been implicated in the regulation of diverse cellular
            processes that play a role in development and tumorigenesis.
            [provided by RefSeq, Aug 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.9507.1,
                                           SRR1803614.153180.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378700.8/ ENSP00000367972.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.3"
     Protein         1..161
                     /product="DNA-binding protein inhibitor ID-4"
                     /note="class B basic helix-loop-helix protein 27;
                     inhibitor of differentiation 4; inhibitor of DNA binding
                     4, dominant negative helix-loop-helix protein; inhibitor
                     of DNA binding 4, HLH protein"
                     /calculated_mol_wt=16491
     Region          62..117
                     /region_name="bHLH_dnHLH_ID4"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     DNA-binding protein inhibitor ID4 and similar proteins;
                     cd19694"
                     /db_xref="CDD:381537"
     Site            order(64,67..68,71..72,74..75,78,90..91,94..95,97..98,
                     100..102,104..105,108,112)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381537"
     Region          117..161
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47928.1)"
     CDS             1..161
                     /gene="ID4"
                     /gene_synonym="bHLHb27; IDB4"
                     /coded_by="NM_001546.4:386..871"
                     /db_xref="CCDS:CCDS4544.1"
                     /db_xref="GeneID:3400"
                     /db_xref="HGNC:HGNC:5363"
                     /db_xref="MIM:600581"
ORIGIN      
        1 mkavspvrps grkapsgcgg gelalrclae hghslggsaa aaaaaaaarc kaaeaaadep
       61 alclqcdmnd cysrlrrlvp tippnkkvsk veilqhvidy ildlqlalet hpallrqppp
      121 papphhpagt cpaapprtpl talntdpaga vnkqgdsilc r
//
LOCUS       NP_055132                415 aa            linear   PRI 27-APR-2025
DEFINITION  all trans-polyprenyl-diphosphate synthase PDSS1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_055132
VERSION     NP_055132.2
DBSOURCE    REFSEQ: accession NM_014317.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Yu,T.J., Liu,Y.Y., Li,X.G., Lian,B., Lu,X.X., Jin,X., Shao,Z.M.,
            Hu,X., Di,G.H. and Jiang,Y.Z.
  TITLE     PDSS1-Mediated Activation of CAMK2A-STAT3 Signaling Promotes
            Metastasis in Triple-Negative Breast Cancer
  JOURNAL   Cancer Res 81 (21), 5491-5505 (2021)
   PUBMED   34408002
  REMARK    GeneRIF: PDSS1-Mediated Activation of CAMK2A-STAT3 Signaling
            Promotes Metastasis in Triple-Negative Breast Cancer.
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Nardecchia,F., De Giorgi,A., Palombo,F., Fiorini,C., De Negri,A.M.,
            Carelli,V., Caporali,L. and Leuzzi,V.
  TITLE     Missense PDSS1 mutations in CoenzymeQ10 synthesis cause optic
            atrophy and sensorineural deafness
  JOURNAL   Ann Clin Transl Neurol 8 (1), 247-251 (2021)
   PUBMED   33285023
  REMARK    GeneRIF: Missense PDSS1 mutations in CoenzymeQ10 synthesis cause
            optic atrophy and sensorineural deafness.
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Dai,W., Liu,H., Chen,K., Xu,X., Qian,D., Luo,S., Amos,C.I.,
            Lee,J.E., Li,X., Nan,H., Li,C. and Wei,Q.
  TITLE     Genetic variants in PDSS1 and SLC16A6 of the ketone body metabolic
            pathway predict cutaneous melanoma-specific survival
  JOURNAL   Mol Carcinog 59 (6), 640-650 (2020)
   PUBMED   32232919
  REMARK    GeneRIF: Genetic variants in PDSS1 and SLC16A6 of the ketone body
            metabolic pathway predict cutaneous melanoma-specific survival.
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Rotig,A., Appelkvist,E.L., Geromel,V., Chretien,D., Kadhom,N.,
            Edery,P., Lebideau,M., Dallner,G., Munnich,A., Ernster,L. and
            Rustin,P.
  TITLE     Quinone-responsive multiple respiratory-chain dysfunction due to
            widespread coenzyme Q10 deficiency
  JOURNAL   Lancet 356 (9227), 391-395 (2000)
   PUBMED   10972372
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Runquist,M., Ericsson,J., Thelin,A., Chojnacki,T. and Dallner,G.
  TITLE     Isoprenoid biosynthesis in rat liver mitochondria. Studies on
            farnesyl pyrophosphate synthase and trans-prenyltransferase
  JOURNAL   J Biol Chem 269 (8), 5804-5809 (1994)
   PUBMED   8119922
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Appelkvist,E.L., Aberg,F., Guan,Z., Parmryd,I. and Dallner,G.
  TITLE     Regulation of coenzyme Q biosynthesis
  JOURNAL   Mol Aspects Med 15 Suppl, s37-s46 (1994)
   PUBMED   7752843
  REMARK    Review article
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Teclebrhan,H., Olsson,J., Swiezewska,E. and Dallner,G.
  TITLE     Biosynthesis of the side chain of
            ubiquinone:trans-prenyltransferase in rat liver microsomes
  JOURNAL   J Biol Chem 268 (31), 23081-23086 (1993)
   PUBMED   8226825
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Salviati,L., Trevisson,E., Agosto,C., Doimo,M. and Navas,P.
  TITLE     Primary Coenzyme Q10 Deficiency Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28125198
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK024802.1 and BC049211.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 27, 2004 this sequence version replaced NP_055132.1.
            
            Summary: The protein encoded by this gene is an enzyme that
            elongates the prenyl side-chain of coenzyme Q, or ubiquinone, one
            of the key elements in the respiratory chain. The gene product
            catalyzes the formation of all trans-polyprenyl pyrophosphates from
            isopentyl diphosphate in the assembly of polyisoprenoid side
            chains, the first step in coenzyme Q biosynthesis. The protein may
            be peripherally associated with the inner mitochondrial membrane,
            though no transit peptide has been definitively identified to date.
            Defects in this gene are a cause of coenzyme Q10 deficiency.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB210838.1, AK024802.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376215.10/ ENSP00000365388.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..415
                     /product="all trans-polyprenyl-diphosphate synthase PDSS1
                     isoform 1"
                     /EC_number="2.5.1.91"
                     /note="polyprenyl pyrophosphate synthetase; coenzyme Q1
                     homolog; subunit 1 of decaprenyl diphosphate synthase;
                     trans-prenyltransferase (TPT); decaprenyl pyrophosphate
                     synthase subunit 1; trans-prenyltransferase 1;
                     all-trans-decaprenyl-diphosphate synthase subunit 1;
                     prenyl (decaprenyl) diphosphate synthase, subunit 1;
                     solanesyl-diphosphate synthase subunit 1; all
                     trans-polyprenyl-diphosphate synthase PDSS1"
                     /calculated_mol_wt=46130
     Region          6..415
                     /region_name="PLN02890"
                     /note="geranyl diphosphate synthase"
                     /db_xref="CDD:178478"
     Region          16..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T2R2.1)"
     CDS             1..415
                     /gene="PDSS1"
                     /gene_synonym="COQ1; COQ10D2; COQ1A; DPS; hDPS1; SPS;
                     TPRT; TPT; TPT 1"
                     /coded_by="NM_014317.5:12..1259"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31168.1"
                     /db_xref="GeneID:23590"
                     /db_xref="HGNC:HGNC:17759"
                     /db_xref="MIM:607429"
ORIGIN      
        1 masrwwrwrr gcswkpaars pgpgspgrag plgpsaaaev raqvhrrkgl dlsqipyinl
       61 vkhltsacpn vcrisrfhht tpdskthsge kytdpfklgw rdlkglyedi rkellistse
      121 lkemseyyfd gkgkafrpii valmaracni hhnnsrhvqa sqraialiae mihtaslvhd
      181 dviddassrr gkhtvnkiwg ekkavlagdl ilsaasiala rignttvisi ltqviedlvr
      241 geflqlgske nenerfahyl ektfkktasl iansckavsv lgcpdpvvhe iayqygknvg
      301 iafqliddvl dftscsdqmg kptsadlklg latgpvlfac qqfpemnami mrrfslpgdv
      361 drarqyvlqs dgvqqttyla qqycheaire isklrpsper daliqlseiv ltrdk
//
LOCUS       NP_031390                217 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane emp24 domain-containing protein 3 isoform a precursor
            [Homo sapiens].
ACCESSION   NP_031390
VERSION     NP_031390.1
DBSOURCE    REFSEQ: accession NM_007364.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Chen,X., Zhang,W., Han,X., Li,X., Xia,L., Wu,Y. and Zhou,Y.
  TITLE     TMED3 stabilizes SMAD2 by counteracting NEDD4-mediated
            ubiquitination to promote ovarian cancer
  JOURNAL   Mol Carcinog 63 (5), 803-816 (2024)
   PUBMED   38411267
  REMARK    GeneRIF: TMED3 stabilizes SMAD2 by counteracting NEDD4-mediated
            ubiquitination to promote ovarian cancer.
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Liao,G., Zhang,M. and Wang,C.
  TITLE     Analysis and Validation of TMED3 correlates with poor prognosis and
            tumor immune infiltration of glioma
  JOURNAL   J Cancer Res Clin Oncol 149 (7), 3485-3494 (2023)
   PUBMED   35951089
  REMARK    GeneRIF: Analysis and Validation of TMED3 correlates with poor
            prognosis and tumor immune infiltration of glioma.
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Yang,Y., Liu,S., Xie,C., Li,Q., Gao,T., Liu,M., Xi,M. and Zhao,L.
  TITLE     Trafficking protein TMED3 promotes esophageal squamous cell
            carcinoma
  JOURNAL   Biomed J 46 (2), 100528 (2023)
   PUBMED   35358714
  REMARK    GeneRIF: Trafficking protein TMED3 promotes esophageal squamous
            cell carcinoma.
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Zhang,D., Sun,L. and Zhang,J.
  TITLE     TMED3 exerts a protumor function in non-small cell lung cancer by
            enhancing the Wnt/beta-catenin pathway via regulation of AKT
  JOURNAL   Toxicol Appl Pharmacol 433, 115793 (2021)
   PUBMED   34758370
  REMARK    GeneRIF: TMED3 exerts a protumor function in non-small cell lung
            cancer by enhancing the Wnt/beta-catenin pathway via regulation of
            AKT.
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Xie,A., Xu,X., Kuang,P., Zhang,L. and Yu,F.
  TITLE     TMED3 promotes the progression and development of lung squamous
            cell carcinoma by regulating EZR
  JOURNAL   Cell Death Dis 12 (9), 804 (2021)
   PUBMED   34429402
  REMARK    GeneRIF: TMED3 promotes the progression and development of lung
            squamous cell carcinoma by regulating EZR.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Zheng,H., Yang,Y., Han,J., Jiang,W.H., Chen,C., Wang,M.C., Gao,R.,
            Li,S., Tian,T., Wang,J., Ma,L.J., Ren,H. and Zhou,W.P.
  TITLE     TMED3 promotes hepatocellular carcinoma progression via IL-11/STAT3
            signaling
  JOURNAL   Sci Rep 6, 37070 (2016)
   PUBMED   27901021
  REMARK    GeneRIF: Study demonstrates that transmembrane p24 trafficking
            protein 3 (TMED3) promotes hepatocellular carcinoma (HCC)
            metastasis and is a potential prognostic biomarker in
            hepatocellular carcinoma. Study propose that TMED3 promotes HCC
            metastasis through IL-11/STAT3 signaling.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Duquet,A., Melotti,A., Mishra,S., Malerba,M., Seth,C., Conod,A. and
            Ruiz i Altaba,A.
  TITLE     A novel genome-wide in vivo screen for metastatic suppressors in
            human colon cancer identifies the positive WNT-TCF pathway
            modulators TMED3 and SOX12
  JOURNAL   EMBO Mol Med 6 (7), 882-901 (2014)
   PUBMED   24920608
  REMARK    GeneRIF: This genome-wide screen has identified two novel
            metastatic suppressors: TMED3 and SOX12, the knockdown of which
            increases metastatic growth after direct seeding.
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Vainio,P., Mpindi,J.P., Kohonen,P., Fey,V., Mirtti,T., Alanen,K.A.,
            Perala,M., Kallioniemi,O. and Iljin,K.
  TITLE     High-throughput transcriptomic and RNAi analysis identifies AIM1,
            ERGIC1, TMED3 and TPX2 as potential drug targets in prostate cancer
  JOURNAL   PLoS One 7 (6), e39801 (2012)
   PUBMED   22761906
  REMARK    GeneRIF: AIM1, ERGIC1, and TPX2 were shown to be highly expressed
            especially in prostate cancer tissues, and high mRNA expression of
            ERGIC1 and TMED3 associated with AR and ERG oncogene expression
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Jenne,N., Frey,K., Brugger,B. and Wieland,F.T.
  TITLE     Oligomeric state and stoichiometry of p24 proteins in the early
            secretory pathway
  JOURNAL   J Biol Chem 277 (48), 46504-46511 (2002)
   PUBMED   12237308
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011797.8, KF459564.1 and AC027811.9.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.519148.1,
                                           SRR3476690.664899.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299705.10/ ENSP00000299705.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..217
                     /product="transmembrane emp24 domain-containing protein 3
                     isoform a precursor"
                     /note="integral type I protein; transmembrane emp24
                     domain-containing protein 3; membrane protein p24B; p24
                     family protein gamma-4; transmembrane emp24 protein
                     transport domain containing 3; testis tissue sperm-binding
                     protein Li 48e"
                     /calculated_mol_wt=22271
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q3.1)"
                     /calculated_mol_wt=2524
     mat_peptide     24..217
                     /product="Transmembrane emp24 domain-containing protein 3.
                     /id=PRO_0000010384"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q3.1)"
                     /calculated_mol_wt=22271
     Region          28..205
                     /region_name="EMP24_GP25L"
                     /note="emp24/gp25L/p24 family/GOLD; pfam01105"
                     /db_xref="CDD:426051"
     Site            181..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q3.1)"
     Region          204..217
                     /region_name="COPI vesicle coat-binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q3.1)"
     Region          204..205
                     /region_name="COPII vesicle coat-binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q3.1)"
     CDS             1..217
                     /gene="TMED3"
                     /gene_synonym="C15orf22; P24B; p24g4; p24gamma4; p26"
                     /coded_by="NM_007364.4:139..792"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10310.1"
                     /db_xref="GeneID:23423"
                     /db_xref="HGNC:HGNC:28889"
                     /db_xref="MIM:620437"
ORIGIN      
        1 mgstvprsas vlllllllrr aeqpcgaelt felpdnakqc fheeveqgvk fsldyqvitg
       61 ghydvdcyve dpqgntiyre tkkqydsfty raevkgvyqf cfsnefstfs hktvyfdfqv
      121 gdeppilpdm gnrvtaltqm esacvtihea lktvidsqth yrlreaqdra raedlnsrvs
      181 ywsvgetial fvvsfsqvll lksfftekrp isravhs
//
LOCUS       NP_112197                395 aa            linear   PRI 27-APR-2025
DEFINITION  TSC22 domain family protein 4 isoform a [Homo sapiens].
ACCESSION   NP_112197
VERSION     NP_112197.1
DBSOURCE    REFSEQ: accession NM_030935.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Goto,N., Suzuki,H., Zheng,L., Okano,Y., Okita,Y., Watanabe,Y.,
            Kato,Y. and Kato,M.
  TITLE     Promotion of squamous cell carcinoma tumorigenesis by
            oncogene-mediated THG-1/TSC22D4 phosphorylation
  JOURNAL   Cancer Sci 114 (10), 3972-3983 (2023)
   PUBMED   37607779
  REMARK    GeneRIF: Promotion of squamous cell carcinoma tumorigenesis by
            oncogene-mediated THG-1/TSC22D4 phosphorylation.
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Sakurai,M., Weber,P., Wolff,G., Wieder,A., Szendroedi,J., Herzig,S.
            and Ekim Ustunel,B.
  TITLE     TSC22D4 promotes TGFbeta1-induced activation of hepatic stellate
            cells
  JOURNAL   Biochem Biophys Res Commun 618, 46-53 (2022)
   PUBMED   35714570
  REMARK    GeneRIF: TSC22D4 promotes TGFbeta1-induced activation of hepatic
            stellate cells.
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Wolff,G., Sakurai,M., Mhamane,A., Troullinaki,M., Maida,A.,
            Deligiannis,I.K., Yin,K., Weber,P., Morgenstern,J., Wieder,A.,
            Kwon,Y., Sekar,R., Zeigerer,A., Roden,M., Bluher,M., Volk,N.,
            Poth,T., Hackert,T., Wiedmann,L., De Angelis Rigotti,F.,
            Rodriguez-Vita,J., Fischer,A., Mukthavaram,R., Limphong,P.,
            Tachikawa,K., Karmali,P., Payne,J., Chivukula,P., Ekim-Ustunel,B.,
            Martinez-Jimenez,C.P., Szendrodi,J., Nawroth,P. and Herzig,S.
  TITLE     Hepatocyte-specific activity of TSC22D4 triggers progressive NAFLD
            by impairing mitochondrial function
  JOURNAL   Mol Metab 60, 101487 (2022)
   PUBMED   35378329
  REMARK    GeneRIF: Hepatocyte-specific activity of TSC22D4 triggers
            progressive NAFLD by impairing mitochondrial function.
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Petersen,H.H., Hilpert,J., Militz,D., Zandler,V., Jacobsen,C.,
            Roebroek,A.J. and Willnow,T.E.
  TITLE     Functional interaction of megalin with the megalinbinding protein
            (MegBP), a novel tetratrico peptide repeat-containing adaptor
            molecule
  JOURNAL   J Cell Sci 116 (Pt 3), 453-461 (2003)
   PUBMED   12508107
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Fiorenza,M.T., Mukhopadhyay,M. and Westphal,H.
  TITLE     Expression screening for Lhx3 downstream genes identifies Thg-1pit
            as a novel mouse gene involved in pituitary development
  JOURNAL   Gene 278 (1-2), 125-130 (2001)
   PUBMED   11707329
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Kester,H.A., Blanchetot,C., den Hertog,J., van der Saag,P.T. and
            van der Burg,B.
  TITLE     Transforming growth factor-beta-stimulated clone-22 is a member of
            a family of leucine zipper proteins that can homo- and
            heterodimerize and has transcriptional repressor activity
  JOURNAL   J Biol Chem 274 (39), 27439-27447 (1999)
   PUBMED   10488076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC001486.2, AC092849.4, AK296580.1, BC010406.2 and AA991748.1.
            
            Summary: TSC22D4 is a member of the TSC22 domain family of leucine
            zipper transcriptional regulators (see TSC22D3; MIM 300506) (Kester
            et al., 1999 [PubMed 10488076]; Fiorenza et al., 2001 [PubMed
            11707329]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1 and 2 encode the protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001486.2, BC010406.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153031 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300181.7/ ENSP00000300181.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..395
                     /product="TSC22 domain family protein 4 isoform a"
                     /note="TSC22 domain family protein 4; tsc-22-like protein
                     THG-1; TSC22-related-inducible leucine zipper protein 2;
                     sperm acrosome developmental regulator"
                     /calculated_mol_wt=40895
     Region          1..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Region          103..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Region          <137..224
                     /region_name="Med4"
                     /note="Vitamin-D-receptor interacting Mediator subunit 4;
                     pfam10018"
                     /db_xref="CDD:401849"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQN3; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQN3; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQN3; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQN3; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Region          316..390
                     /region_name="ZIP_TSC22D4"
                     /note="leucine zipper domain found in TSC22 domain family
                     protein 4; cd21941"
                     /db_xref="CDD:409281"
     Site            order(339..341,344,347..348,351..352,354..355,358..359,
                     361..362,365..366,369,373)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409281"
     Region          344..365
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     Region          376..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q8.2)"
     CDS             1..395
                     /gene="TSC22D4"
                     /gene_synonym="SPACDR; THG-1; THG1; TILZ2"
                     /coded_by="NM_030935.5:691..1878"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5695.1"
                     /db_xref="GeneID:81628"
                     /db_xref="HGNC:HGNC:21696"
                     /db_xref="MIM:611914"
ORIGIN      
        1 msggkkkssf qitsvttdye gpgspgasdp ptpqpptgpp prlpngepsp dpggkgtprn
       61 gspppgapss rfrvvklphg lgepyrrgrw tcvdvyerdl ephsfgglle girgasggag
      121 grsldsrlel aslglgaptp psglsqgpts wlrppptspg pqarsftggl gqlvvpskak
      181 aekpplsass pqqrppepet gesagtsraa tplpslrvea eaggsgartp plsrrkavdm
      241 rlrmelgape emgqvpplds rpsspalyft hdaslvhksp dpfgavaaqk fslahsmlai
      301 sghldsddds gsgslvgidn kieqamdlvk shlmfavree vevlkeqire laernaaleq
      361 engllralas peqlaqlpss gvprlgppap ngpsv
//
LOCUS       NP_001356473             477 aa            linear   PRI 27-APR-2025
DEFINITION  BDNF/NT-3 growth factors receptor isoform b precursor [Homo
            sapiens].
ACCESSION   NP_001356473 XP_016870247
VERSION     NP_001356473.1
DBSOURCE    REFSEQ: accession NM_001369544.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Gupta,R., Dittmeier,M., Wohlleben,G., Nickl,V., Bischler,T.,
            Luzak,V., Wegat,V., Doll,D., Sodmann,A., Bady,E., Langlhofer,G.,
            Wachter,B., Havlicek,S., Gupta,J., Horn,E., Luningschror,P.,
            Villmann,C., Polat,B., Wischhusen,J., Monoranu,C.M., Kuper,J. and
            Blum,R.
  TITLE     Atypical cellular responses mediated by intracellular constitutive
            active TrkB (NTRK2) kinase domains and a solely intracellular
            NTRK2-fusion oncogene
  JOURNAL   Cancer Gene Ther 31 (9), 1357-1379 (2024)
   PUBMED   39039193
  REMARK    GeneRIF: Atypical cellular responses mediated by intracellular
            constitutive active TrkB (NTRK2) kinase domains and a solely
            intracellular NTRK2-fusion oncogene.
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X., Zhang,Y., Yan,H., Yu,H., Zhang,D., Mattay,V.S., Tan,H.Y.
            and Yue,W.
  TITLE     Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2
  JOURNAL   BMC Med 22 (1), 146 (2024)
   PUBMED   38561734
  REMARK    GeneRIF: Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Ikhlef,L., Yassine,M., Chandouri,B., Riviere,L., Naves,T.,
            Dmytruk,N., Gachard,N., Jauberteau,M.O. and Gallet,P.F.
  TITLE     Targeting the NTSR2/TrkB oncogenic pathway in chronic lymphocytic
            leukemia
  JOURNAL   Sci Rep 14 (1), 6084 (2024)
   PUBMED   38480783
  REMARK    GeneRIF: Targeting the NTSR2/TrkB oncogenic pathway in chronic
            lymphocytic leukemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Wang,Y., Liang,J., Xu,B., Yang,J., Wu,Z. and Cheng,L.
  TITLE     TrkB/BDNF signaling pathway and its small molecular agonists in CNS
            injury
  JOURNAL   Life Sci 336, 122282 (2024)
   PUBMED   38008209
  REMARK    GeneRIF: TrkB/BDNF signaling pathway and its small molecular
            agonists in CNS injury.
            Review article
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Luberg,K., Wong,J., Weickert,C.S. and Timmusk,T.
  TITLE     Human TrkB gene: novel alternative transcripts, protein isoforms
            and expression pattern in the prefrontal cerebral cortex during
            postnatal development
  JOURNAL   J Neurochem 113 (4), 952-964 (2010)
   PUBMED   20193039
  REMARK    GeneRIF: Identification of 36 potential TrkB protein isoforms
            suggests high complexity in the synthesis, regulation and function
            of this important neurotrophin receptor emphasizing the need for
            further study of these novel TrkB variants.
REFERENCE   6  (residues 1 to 477)
  AUTHORS   Stoilov,P., Castren,E. and Stamm,S.
  TITLE     Analysis of the human TrkB gene genomic organization reveals novel
            TrkB isoforms, unusual gene length, and splicing mechanism
  JOURNAL   Biochem Biophys Res Commun 290 (3), 1054-1065 (2002)
   PUBMED   11798182
  REMARK    GeneRIF: analysis of TrkB gene reveals novel gene length and
            splicing mechanism
REFERENCE   7  (residues 1 to 477)
  AUTHORS   Haniu,M., Talvenheimo,J., Le,J., Katta,V., Welcher,A. and
            Rohde,M.F.
  TITLE     Extracellular domain of neurotrophin receptor trkB: disulfide
            structure, N-glycosylation sites, and ligand binding
  JOURNAL   Arch Biochem Biophys 322 (1), 256-264 (1995)
   PUBMED   7574684
REFERENCE   8  (residues 1 to 477)
  AUTHORS   Nakagawara,A., Liu,X.G., Ikegaki,N., White,P.S., Yamashiro,D.J.,
            Nycum,L.M., Biegel,J.A. and Brodeur,G.M.
  TITLE     Cloning and chromosomal localization of the human TRK-B tyrosine
            kinase receptor gene (NTRK2)
  JOURNAL   Genomics 25 (2), 538-546 (1995)
   PUBMED   7789988
REFERENCE   9  (residues 1 to 477)
  AUTHORS   Squinto,S.P., Stitt,T.N., Aldrich,T.H., Davis,S., Blanco,S.M.,
            RadzieJewski,C., Glass,D.J., Masiakowski,P., Furth,M.E.,
            Valenzuela,D.M., Distefano,P.S. and Yancopoulos,G.D.
  TITLE     trkB encodes a functional receptor for brain-derived neurotrophic
            factor and neurotrophin-3 but not nerve growth factor
  JOURNAL   Cell 65 (5), 885-893 (1991)
   PUBMED   1710174
REFERENCE   10 (residues 1 to 477)
  AUTHORS   Soppet,D., Escandon,E., Maragos,J., Middlemas,D.S., Reid,S.W.,
            Blair,J., Burton,L.E., Stanton,B.R., Kaplan,D.R., Hunter,T.,
            Nikolics,K. and Parada,L.F.
  TITLE     The neurotrophic factors brain-derived neurotrophic factor and
            neurotrophin-3 are ligands for the trkB tyrosine kinase receptor
  JOURNAL   Cell 65 (5), 895-903 (1991)
   PUBMED   1645620
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390777.13.
            
            On Apr 10, 2019 this sequence version replaced XP_016870247.1.
            
            Summary: This gene encodes a member of the neurotrophic tyrosine
            receptor kinase (NTRK) family. This kinase is a membrane-bound
            receptor that, upon neurotrophin binding, phosphorylates itself and
            members of the MAPK pathway. Signalling through this kinase leads
            to cell differentiation. Mutations in this gene have been
            associated with obesity and mood disorders. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (t), as well as variants b, o-s,
            and u-w, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.57014.1,
                                           SRR1660807.21925.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..477
                     /product="BDNF/NT-3 growth factors receptor isoform b
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="BDNF/NT-3 growth factors receptor; tyrosine kinase
                     receptor B; BDNF-tropomyosine receptor kinase B;
                     tropomyosin-related kinase B; neurotrophic tyrosine kinase
                     receptor type 2"
                     /calculated_mol_wt=49372
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3697
     Region          31..60
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; pfam01462"
                     /db_xref="CDD:396168"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          92..150
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          92..113
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          96..116
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          116..137
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Region          117..139
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          140..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          151..195
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          205..283
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          214..218
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          227..230
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          245..252
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            254
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          262..268
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          276..279
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          286..379
                     /region_name="IgI_TrkB_d5"
                     /note="Fifth domain (immunoglobulin-like) of Trk receptor
                     TrkB; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05855"
                     /db_xref="CDD:409441"
     Region          286..294
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409441"
     Region          295..298
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409441"
     Region          301..309
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409441"
     Site            310
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409441"
     Region          312..319
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409441"
     Region          322..325
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409441"
     Site            325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          330..335
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409441"
     Site            order(335,349..350,353)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:409441"
     Site            338
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          341..349
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409441"
     Region          357..365
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409441"
     Region          368..376
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409441"
     Site            412
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Site            431..454
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Region          455..466
                     /region_name="Interaction with MAPK8IP3/JIP3.
                     /evidence=ECO:0000250|UniProtKB:Q63604"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     CDS             1..477
                     /gene="NTRK2"
                     /gene_synonym="DEE58; EIEE58; GP145-TrkB; OBHD; trk-B;
                     TRKB"
                     /coded_by="NM_001369544.1:968..2401"
                     /note="isoform b precursor is encoded by transcript
                     variant t"
                     /db_xref="CCDS:CCDS35053.1"
                     /db_xref="GeneID:4915"
                     /db_xref="HGNC:HGNC:8032"
                     /db_xref="MIM:600456"
ORIGIN      
        1 msswirwhgp amarlwgfcw lvvgfwraaf acptsckcsa sriwcsdpsp givafprlep
       61 nsvdpenite ifianqkrle iineddveay vglrnltivd sglkfvahka flknsnlqhi
      121 nftrnkltsl srkhfrhldl selilvgnpf tcscdimwik tlqeaksspd tqdlyclnes
      181 skniplanlq ipncglpsan laapnltvee gksitlscsv agdpvpnmyw dvgnlvskhm
      241 netshtqgsl ritnissdds gkqiscvaen lvgedqdsvn ltvhfaptit flesptsdhh
      301 wcipftvkgn pkpalqwfyn gailneskyi ctkihvtnht eyhgclqldn pthmnngdyt
      361 liakneygkd ekqisahfmg wpgiddganp nypdviyedy gtaandigdt tnrsneipst
      421 dvtdktgreh lsvyavvvia svvgfcllvm lfllklarhs kfgmkgfvlf hkipldg
//
LOCUS       NP_653106                476 aa            linear   ROD 27-APR-2025
DEFINITION  cytoplasmic 60S subunit biogenesis factor ZNF622 [Mus musculus].
ACCESSION   NP_653106
VERSION     NP_653106.1
DBSOURCE    REFSEQ: accession NM_144523.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Guo,G., Huss,M., Tong,G.Q., Wang,C., Li Sun,L., Clarke,N.D. and
            Robson,P.
  TITLE     Resolution of cell fate decisions revealed by single-cell gene
            expression analysis from zygote to blastocyst
  JOURNAL   Dev Cell 18 (4), 675-685 (2010)
   PUBMED   20412781
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Cobellis,G., Nicolaus,G., Iovino,M., Romito,A., Marra,E.,
            Barbarisi,M., Sardiello,M., Di Giorgio,F.P., Iovino,N., Zollo,M.,
            Ballabio,A. and Cortese,R.
  TITLE     Tagging genes with cassette-exchange sites
  JOURNAL   Nucleic Acids Res 33 (4), e44 (2005)
   PUBMED   15741177
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC162303.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK031232.1, SRR7345562.2513633.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 9.71 cM"
     Protein         1..476
                     /product="cytoplasmic 60S subunit biogenesis factor
                     ZNF622"
                     /calculated_mol_wt=53320
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q969S3; propagated from
                     UniProtKB/Swiss-Prot (Q91VY9.1)"
     Region          <4..49
                     /region_name="PTZ00448"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:185627"
     Region          6..28
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(13..15,17..18,22,27,76,79..83,85..86)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          70..93
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          71..93
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          137..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91VY9.1)"
     Region          253..352
                     /region_name="zf-C2H2_2"
                     /note="C2H2 type zinc-finger (2 copies); pfam12756"
                     /db_xref="CDD:463690"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q969S3; propagated from
                     UniProtKB/Swiss-Prot (Q91VY9.1)"
     CDS             1..476
                     /gene="Zfp622"
                     /gene_synonym="1110033B05Rik; D15Ertd806e; Znf622; ZPR9"
                     /coded_by="NM_144523.3:185..1615"
                     /db_xref="CCDS:CCDS27400.1"
                     /db_xref="GeneID:52521"
                     /db_xref="MGI:MGI:1289282"
ORIGIN      
        1 maaltcitcr vafrdaelqr ahyktdwhry nlrrkvaama pvtaegfqer vraqravaea
       61 aeaskgaaty ctacgkkfat fnayenhlgs rrhaelerka vraasrrvel lnaknlekgl
      121 gadgvdkdav naaiqqaika qpstspkkap fvptdecgra aagargvper dptekpprlq
      181 wfeqqakkla kqqwedgeee geeeeedded edwedidsdd glecedpgve dqdaedaaae
      241 espplgaipi tdclfcshhs sslvknvahm tkvhsffipd ieylsdlkgl ikylgekvgv
      301 gkiclwcnek gksfysteav qahmndkshc klftdgdaal efadfydfrs sypdykegqd
      361 paelealstd kilecddetm elilpsgarv ghrslmryyk qrfglpravt varnqkavgr
      421 vlqqyralgw mgstgaalmr erdmqyvqrm kskwmlkigm knnatkqmhf raqvrf
//
LOCUS       NP_001753                531 aa            linear   PRI 27-APR-2025
DEFINITION  T-complex protein 1 subunit zeta isoform a [Homo sapiens].
ACCESSION   NP_001753
VERSION     NP_001753.1
DBSOURCE    REFSEQ: accession NM_001762.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Chen,Y., Chen,Y. and Liu,W.
  TITLE     Chaperonin containing TCP1 subunit 6A may activate Notch and Wnt
            pathways to facilitate the malignant behaviors and cancer stemness
            in oral squamous cell carcinoma
  JOURNAL   Cancer Biol Ther 25 (1), 2287122 (2024)
   PUBMED   38084868
  REMARK    GeneRIF: Chaperonin containing TCP1 subunit 6A may activate Notch
            and Wnt pathways to facilitate the malignant behaviors and cancer
            stemness in oral squamous cell carcinoma.
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Zhang,H., Zheng,T., Qin,C., Zhang,X., Lin,H., Huang,X., Liu,Q.,
            Chang,S., Zhang,L., Guo,J., Zhang,Y., Bian,C. and Liu,H.
  TITLE     CCT6A promotes cell proliferation in colon cancer by targeting
            BIRC5 associated with p53 status
  JOURNAL   Cancer Gene Ther 31 (8), 1151-1163 (2024)
   PUBMED   38997438
  REMARK    GeneRIF: CCT6A promotes cell proliferation in colon cancer by
            targeting BIRC5 associated with p53 status.
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yu,S.K., Yu,T., Wang,Y.M., Sun,A., Liu,J. and Lu,K.H.
  TITLE     CCT6A facilitates lung adenocarcinoma progression and glycolysis
            via STAT1/HK2 axis
  JOURNAL   J Transl Med 22 (1), 460 (2024)
   PUBMED   38750462
  REMARK    GeneRIF: CCT6A facilitates lung adenocarcinoma progression and
            glycolysis via STAT1/HK2 axis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Xia,X., Zhao,S., Chen,W., Xu,C. and Zhao,D.
  TITLE     CCT6A promotes esophageal squamous cell carcinoma cell
            proliferation, invasion and epithelial-mesenchymal transition by
            activating TGF-beta/Smad/c-Myc pathway
  JOURNAL   Ir J Med Sci 192 (6), 2653-2660 (2023)
   PUBMED   37017854
  REMARK    GeneRIF: CCT6A promotes esophageal squamous cell carcinoma cell
            proliferation, invasion and epithelial-mesenchymal transition by
            activating TGF-beta/Smad/c-Myc pathway.
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Zeng,W., Wu,M., Cheng,Y., Liu,L., Han,Y., Xie,Q., Li,J., Wei,L.,
            Fang,Y., Chen,Y., Peng,J. and Shen,A.
  TITLE     CCT6A knockdown suppresses osteosarcoma cell growth and Akt pathway
            activation in vitro
  JOURNAL   PLoS One 17 (12), e0279851 (2022)
   PUBMED   36584147
  REMARK    GeneRIF: CCT6A knockdown suppresses osteosarcoma cell growth and
            Akt pathway activation in vitro.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Schwartz,G.J., Kittelberger,A.M. and Segel,G.B.
  TITLE     Cloning of rabbit Cct6 and the distribution of the Cct complex in
            mammalian tissues
  JOURNAL   Exp Nephrol 8 (3), 152-160 (2000)
   PUBMED   10810232
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Li,W.Z., Lin,P., Frydman,J., Boal,T.R., Cardillo,T.S.,
            Richard,L.M., Toth,D., Lichtman,M.A., Hartl,F.U., Sherman,F. et al.
  TITLE     Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and
            yeast
  JOURNAL   J Biol Chem 269 (28), 18616-18622 (1994)
   PUBMED   8034610
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Kubota,H., Hynes,G., Carne,A., Ashworth,A. and Willison,K.
  TITLE     Identification of six Tcp-1-related genes encoding divergent
            subunits of the TCP-1-containing chaperonin
  JOURNAL   Curr Biol 4 (2), 89-99 (1994)
   PUBMED   7953530
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Segel,G.B., Boal,T.R., Cardillo,T.S., Murant,F.G., Lichtman,M.A.
            and Sherman,F.
  TITLE     Isolation of a gene encoding a chaperonin-like protein by
            complementation of yeast amino acid transport mutants with human
            cDNA
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 6060-6064 (1992)
   PUBMED   1352881
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI464886.1, AC092579.3,
            AC092101.5 and AW411253.1.
            
            Summary: The protein encoded by this gene is a molecular chaperone
            that is a member of the chaperonin containing TCP1 complex (CCT),
            also known as the TCP1 ring complex (TRiC). This complex consists
            of two identical stacked rings, each containing eight different
            proteins. Unfolded polypeptides enter the central cavity of the
            complex and are folded in an ATP-dependent manner. The complex
            folds various proteins, including actin and tubulin. Alternate
            transcriptional splice variants of this gene, encoding different
            isoforms, have been characterized. In addition, several pseudogenes
            of this gene have been located. [provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB063318.1, SRR1660807.196711.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000275603.9/ ENSP00000275603.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p11.2"
     Protein         1..531
                     /product="T-complex protein 1 subunit zeta isoform a"
                     /note="chaperonin containing T-complex subunit 6;
                     histidine transport regulator 3; amino acid transport
                     defect-complementing; T-complex protein 1, zeta subunit;
                     acute morphine dependence related protein 2; T-complex
                     protein 1 subunit zeta; chaperonin containing TCP1,
                     subunit 6A (zeta 1); chaperonin containing T-complex
                     polypeptide 1 subunit 6A"
                     /calculated_mol_wt=57893
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P40227.3)"
     Region          3..530
                     /region_name="chap_CCT_zeta"
                     /note="T-complex protein 1, zeta subunit; TIGR02347"
                     /db_xref="CDD:274088"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P80317; propagated from
                     UniProtKB/Swiss-Prot (P40227.3)"
     Site            199
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P40227.3)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P40227.3)"
     Site            287
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P80317; propagated from
                     UniProtKB/Swiss-Prot (P40227.3)"
     Site            365
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P40227.3)"
     Site            377
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P40227.3)"
     Site            388
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P40227.3)"
     CDS             1..531
                     /gene="CCT6A"
                     /gene_synonym="CCT-zeta; CCT-zeta-1; CCT6; Cctz; HTR3;
                     MoDP-2; TCP-1-zeta; TCP20; TCPZ; TTCP20"
                     /coded_by="NM_001762.4:85..1680"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5523.1"
                     /db_xref="GeneID:908"
                     /db_xref="HGNC:HGNC:1620"
                     /db_xref="MIM:104613"
ORIGIN      
        1 maavktlnpk aevaraqaal avnisaargl qdvlrtnlgp kgtmkmlvsg agdikltkdg
       61 nvllhemqiq hptasliakv ataqdditgd gttsnvliig ellkqadlyi seglhpriit
      121 egfeaakeka lqfleevkvs remdretlid vartslrtkv haeladvlte avvdsilaik
      181 kqdepidlfm ieimemkhks etdtslirgl vldhgarhpd mkkrvedayi ltcnvsleye
      241 ktevnsgffy ksaeereklv kaerkfiedr vkkiielkrk vcgdsdkgfv vinqkgidpf
      301 sldalskegi valrrakrrn merltlacgg valnsfddls pdclghaglv yeytlgeekf
      361 tfiekcnnpr svtllikgpn khtltqikda vrdglravkn aiddgcvvpg agavevamae
      421 alikhkpsvk graqlgvqaf adalliipkv laqnsgfdlq etlvkiqaeh sesgqlvgvd
      481 lntgepmvaa evgvwdnycv kkqllhsctv iatnillvde imragmsslk g
//
LOCUS       NP_003731                499 aa            linear   PRI 27-APR-2025
DEFINITION  potassium channel subfamily K member 5 [Homo sapiens].
ACCESSION   NP_003731
VERSION     NP_003731.1
DBSOURCE    REFSEQ: accession NM_003740.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Liao,K., Zeng,H., Yang,X., He,D., Wang,B. and Yuan,J.
  TITLE     KCNK5 Regulating Potassium Efflux and Inducing Pyroptosis in
            Corneal Epithelial Cells Through TNFSF10-Mediated Autophagy in Dry
            Eye
  JOURNAL   Invest Ophthalmol Vis Sci 65 (1), 34 (2024)
   PUBMED   38236186
  REMARK    GeneRIF: KCNK5 Regulating Potassium Efflux and Inducing Pyroptosis
            in Corneal Epithelial Cells Through TNFSF10-Mediated Autophagy in
            Dry Eye.
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Khoubza,L., Gilbert,N., Kim,E.J., Chatelain,F.C., Feliciangeli,S.,
            Abelanet,S., Kang,D., Lesage,F. and Bichet,D.
  TITLE     Alkaline-sensitive two-pore domain potassium channels form
            functional heteromers in pancreatic beta-cells
  JOURNAL   J Biol Chem 298 (10), 102447 (2022)
   PUBMED   36063992
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Jiang,Z., Zhao,L., Zhang,X., Zhang,W., Feng,Y. and Li,T.
  TITLE     Common variants in KCNK5 and FHL5 genes contributed to the
            susceptibility of migraine without aura in Han Chinese population
  JOURNAL   Sci Rep 11 (1), 6807 (2021)
   PUBMED   33762637
  REMARK    GeneRIF: Common variants in KCNK5 and FHL5 genes contributed to the
            susceptibility of migraine without aura in Han Chinese population.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Lenzini,L., Prisco,S., Gallina,M., Kuppusamy,M. and Rossi,G.P.
  TITLE     Mutations of the Twik-Related Acid-Sensitive K+ Channel 2 Promoter
            in Human Primary Aldosteronism
  JOURNAL   Endocrinology 159 (3), 1352-1359 (2018)
   PUBMED   29293917
  REMARK    GeneRIF: mutations in the promoter region of the TWIK-related
            acid-sensitive K(+) channel 2 (TASK-2) gene did not result in
            hypertension or primary aldosteronism (PA) during long-term
            follow-up in healthy participants thus they do not seem to be a
            factor in causing PA by themselves.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Niemeyer,M.I., Cid,L.P., Valenzuela,X., Paeile,V. and
            Sepulveda,F.V.
  TITLE     Extracellular conserved cysteine forms an intersubunit disulphide
            bridge in the KCNK5 (TASK-2) K+ channel without having an essential
            effect upon activity
  JOURNAL   Mol Membr Biol 20 (2), 185-191 (2003)
   PUBMED   12851074
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Morton,M.J., O'Connell,A.D., Sivaprasadarao,A. and Hunter,M.
  TITLE     Determinants of pH sensing in the two-pore domain K(+) channels
            TASK-1 and -2
  JOURNAL   Pflugers Arch 445 (5), 577-583 (2003)
   PUBMED   12634929
  REMARK    GeneRIF: TASK-2 does not possess a histidine residue at homologous
            position. Inclusion of such a residue failed to produce expected
            increase in pH sensitivity; instead, a slight decrease was observed
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Goldstein,S.A., Bockenhauer,D., O'Kelly,I. and Zilberberg,N.
  TITLE     Potassium leak channels and the KCNK family of two-P-domain
            subunits
  JOURNAL   Nat Rev Neurosci 2 (3), 175-184 (2001)
   PUBMED   11256078
  REMARK    Review article
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Gray,A.T., Zhao,B.B., Kindler,C.H., Winegar,B.D., Mazurek,M.J.,
            Xu,J., Chavez,R.A., Forsayeth,J.R. and Yost,C.S.
  TITLE     Volatile anesthetics activate the human tandem pore domain baseline
            K+ channel KCNK5
  JOURNAL   Anesthesiology 92 (6), 1722-1730 (2000)
   PUBMED   10839924
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Reyes,R., Duprat,F., Lesage,F., Fink,M., Salinas,M., Farman,N. and
            Lazdunski,M.
  TITLE     Cloning and expression of a novel pH-sensitive two pore domain K+
            channel from human kidney
  JOURNAL   J Biol Chem 273 (47), 30863-30869 (1998)
   PUBMED   9812978
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC060793.1 and BU608155.1.
            
            Summary: This gene encodes one of the members of the superfamily of
            potassium channel proteins containing two pore-forming P domains.
            The message for this gene is mainly expressed in the cortical
            distal tubules and collecting ducts of the kidney. The protein is
            highly sensitive to external pH and this, in combination with its
            expression pattern, suggests it may play an important role in renal
            potassium transport. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060793.1, AF084830.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359534.4/ ENSP00000352527.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..499
                     /product="potassium channel subfamily K member 5"
                     /note="potassium channel, subfamily K, member 1 (TASK-2);
                     acid-sensitive potassium channel protein TASK-2;
                     TWIK-related acid-sensitive K+ channel 2; K2P5.1 potassium
                     channel; TWIK-related acid-sensitive K(+) channel 2;
                     potassium channel, subfamily, member 5 (KCNK5); potassium
                     channel, two pore domain subfamily K, member 5;
                     TWIK-related acid-sensitive K+ 2"
                     /calculated_mol_wt=54999
     Site            8..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95279.1)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95279.1)"
     Region          <83..137
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     misc_feature    85..111
                     /note="pore-forming domain"
     Region          98..103
                     /region_name="Selectivity filter 1.
                     /evidence=ECO:0000250|UniProtKB:P57789"
                     /note="propagated from UniProtKB/Swiss-Prot (O95279.1)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95279.1)"
     Site            158..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95279.1)"
     Region          171..243
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     misc_feature    190..215
                     /note="pore-forming domain"
     Region          203..208
                     /region_name="Selectivity filter 2.
                     /evidence=ECO:0000250|UniProtKB:P57789"
                     /note="propagated from UniProtKB/Swiss-Prot (O95279.1)"
     Site            230..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95279.1)"
     Region          312..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95279.1)"
     Region          360..388
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95279.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (O95279.1)"
     Region          428..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95279.1)"
     CDS             1..499
                     /gene="KCNK5"
                     /gene_synonym="K2p5.1; KCNK5b; TASK-2; TASK2"
                     /coded_by="NM_003740.4:365..1864"
                     /db_xref="CCDS:CCDS4841.1"
                     /db_xref="GeneID:8645"
                     /db_xref="HGNC:HGNC:6280"
                     /db_xref="MIM:603493"
ORIGIN      
        1 mvdrgpllts aiifylaiga aifevleeph wkeakknyyt qklhllkefp clgqegldki
       61 levvsdaagq gvaitgnqtf nnwnwpnami faatvittig ygnvapktpa grlfcvfygl
      121 fgvplcltwi salgkffggr akrlgqfltk rgvslrkaqi tctvifivwg vlvhlvippf
      181 vfmvtegwny ieglyysfit istigfgdfv agvnpsanyh alyryfvelw iylglawlsl
      241 fvnwkvsmfv evhkaikkrr rrrkesfess phsrkalqvk gstaskdvni fsflskkeet
      301 yndlikqigk kamktsggge tgpgpglgpq ggglpalpps lvplvvyskn rvptleevsq
      361 tlrskghvsr spdeeavara pedsspapev fmnqldrise ecepwdaqdy hplifqdasi
      421 tfvnteagls deetskssle dnlageespq qgaeakapln mgefpssses tftstesels
      481 vpyeqlmney nkanspkgt
//
LOCUS       NP_612423                293 aa            linear   PRI 27-APR-2025
DEFINITION  SAGA-associated factor 29 [Homo sapiens].
ACCESSION   NP_612423 XP_946261
VERSION     NP_612423.1
DBSOURCE    REFSEQ: accession NM_138414.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Barbosa,K., Deshpande,A., Perales,M., Xiang,P., Murad,R.,
            Pramod,A.B., Minkina,A., Robertson,N., Schischlik,F., Lei,X.,
            Sun,Y., Brown,A., Amend,D., Jeremias,I., Doench,J.G.,
            Humphries,R.K., Ruppin,E., Shendure,J., Mali,P., Adams,P.D. and
            Deshpande,A.J.
  TITLE     Transcriptional control of leukemogenesis by the chromatin reader
            SGF29
  JOURNAL   Blood 143 (8), 697-712 (2024)
   PUBMED   38048593
  REMARK    GeneRIF: Transcriptional control of leukemogenesis by the chromatin
            reader SGF29.
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Arras,S.D.M., Ormerod,K.L., Erpf,P.E., Espinosa,M.I.,
            Carpenter,A.C., Blundell,R.D., Stowasser,S.R., Schulz,B.L.,
            Tanurdzic,M. and Fraser,J.A.
  TITLE     Convergent microevolution of Cryptococcus neoformans hypervirulence
            in the laboratory and the clinic
  JOURNAL   Sci Rep 7 (1), 17918 (2017)
   PUBMED   29263343
  REMARK    GeneRIF: Loss of function SGF29 mutation is associated with
            Cryptococcus neoformans hypervirulence.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Guelman,S., Kozuka,K., Mao,Y., Pham,V., Solloway,M.J., Wang,J.,
            Wu,J., Lill,J.R. and Zha,J.
  TITLE     The double-histone-acetyltransferase complex ATAC is essential for
            mammalian development
  JOURNAL   Mol Cell Biol 29 (5), 1176-1188 (2009)
   PUBMED   19103755
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
REFERENCE   8  (residues 1 to 293)
  AUTHORS   Zhao,Y., Lang,G., Ito,S., Bonnet,J., Metzger,E., Sawatsubashi,S.,
            Suzuki,E., Le Guezennec,X., Stunnenberg,H.G., Krasnov,A.,
            Georgieva,S.G., Schule,R., Takeyama,K., Kato,S., Tora,L. and
            Devys,D.
  TITLE     A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
            coactivates nuclear receptors, and counteracts heterochromatin
            silencing
  JOURNAL   Mol Cell 29 (1), 92-101 (2008)
   PUBMED   18206972
REFERENCE   9  (residues 1 to 293)
  AUTHORS   Kurabe,N., Katagiri,K., Komiya,Y., Ito,R., Sugiyama,A., Kawasaki,Y.
            and Tashiro,F.
  TITLE     Deregulated expression of a novel component of TFTC/STAGA histone
            acetyltransferase complexes, rat SGF29, in hepatocellular
            carcinoma: possible implication for the oncogenic potential of
            c-Myc
  JOURNAL   Oncogene 26 (38), 5626-5634 (2007)
   PUBMED   17334388
REFERENCE   10 (residues 1 to 293)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020765.8, AA132818.1, BC011981.1 and AA132314.1.
            
            On Mar 4, 2006 this sequence version replaced XP_946261.1.
            
            Summary: CCDC101 is a subunit of 2 histone acetyltransferase
            complexes: the ADA2A (TADA2A; MIM 602276)-containing (ATAC) complex
            and the SPT3 (SUPT3H; MIM 602947)-TAF9 (MIM 600822)-GCN5 (KAT2A;
            MIM 602301)/PCAF (KAT2B; MIM 602303) acetylase (STAGA) complex.
            Both of these complexes contain either GCN5 or PCAF, which are
            paralogous acetyltransferases (Wang et al., 2008 [PubMed
            18838386]).[supplied by OMIM, Apr 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.22172.1,
                                           SRR5189667.236079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317058.8/ ENSP00000316114.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..293
                     /product="SAGA-associated factor 29"
                     /note="SAGA-associated factor 29 homolog; coiled-coil
                     domain-containing protein 101; coiled-coil domain
                     containing 101"
                     /calculated_mol_wt=33107
     Region          158..288
                     /region_name="DUF1325"
                     /note="SGF29 tudor-like domain; pfam07039"
                     /db_xref="CDD:462071"
     Region          194..196
                     /region_name="Histone H3K4me3 N-terminus binding.
                     /evidence=ECO:0000269|PubMed:21685874,
                     ECO:0000269|PubMed:26578293"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ES7.1)"
     Site            238
                     /site_type="other"
                     /note="Histone H3K4me3 binding.
                     /evidence=ECO:0000269|PubMed:21685874; propagated from
                     UniProtKB/Swiss-Prot (Q96ES7.1)"
     Region          240..243
                     /region_name="Histone H3K4me3 N-terminus binding.
                     /evidence=ECO:0000269|PubMed:21685874,
                     ECO:0000269|PubMed:26578293"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ES7.1)"
     Site            245
                     /site_type="other"
                     /note="Histone H3K4me3 binding.
                     /evidence=ECO:0000269|PubMed:21685874,
                     ECO:0000269|PubMed:26578293; propagated from
                     UniProtKB/Swiss-Prot (Q96ES7.1)"
     Region          264..266
                     /region_name="Histone H3K4me3 binding.
                     /evidence=ECO:0000269|PubMed:21685874"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ES7.1)"
     Site            288
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96ES7.1)"
     CDS             1..293
                     /gene="SGF29"
                     /gene_synonym="CCDC101; STAF36; TDRD29"
                     /coded_by="NM_138414.3:194..1075"
                     /db_xref="CCDS:CCDS10635.1"
                     /db_xref="GeneID:112869"
                     /db_xref="HGNC:HGNC:25156"
                     /db_xref="MIM:613374"
ORIGIN      
        1 malvsadsri aelltelhql ikqtqeersr sehnlvniqk thermqtenk ispyyrtklr
       61 glyttakada eaecnilrka ldkiaeiksl leerriaaki aglyndsepp rktmrrgvlm
      121 tllqqsamtl plwigkpgdk ppplcgaipa sgdyvarpgd kvaarvkavd gdeqwilaev
      181 vsyshatnky evddideegk erhtlsrrrv iplpqwkanp etdpealfqk eqlvlalypq
      241 ttcfyralih appqrpqddy svlfedtsya dgyspplnva qryvvackep kkk
//
LOCUS       NP_001032410            1253 aa            linear   PRI 27-APR-2025
DEFINITION  cytoplasmic FMR1-interacting protein 2 isoform a [Homo sapiens].
ACCESSION   NP_001032410
VERSION     NP_001032410.1
DBSOURCE    REFSEQ: accession NM_001037333.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1253)
  AUTHORS   Peng,X., Wellard,N., Ghosh,A., Troakes,C. and Giese,K.P.
  TITLE     Different dysregulations of CYFIP1 and CYFIP2 in distinct types of
            dementia
  JOURNAL   Brain Res Bull 206, 110849 (2024)
   PUBMED   38128786
  REMARK    GeneRIF: Different dysregulations of CYFIP1 and CYFIP2 in distinct
            types of dementia.
REFERENCE   2  (residues 1 to 1253)
  AUTHORS   Peng,Q., Ren,B., Xin,K., Liu,W., Alam,M.S., Yang,Y., Gu,X., Zhu,Y.
            and Tian,Y.
  TITLE     CYFIP2 serves as a prognostic biomarker and correlates with tumor
            immune microenvironment in human cancers
  JOURNAL   Eur J Med Res 28 (1), 364 (2023)
   PUBMED   37735711
  REMARK    GeneRIF: CYFIP2 serves as a prognostic biomarker and correlates
            with tumor immune microenvironment in human cancers.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1253)
  AUTHORS   Biembengut,I.V., Shigunov,P., Frota,N.F., Lourenzoni,M.R. and de
            Souza,T.A.C.B.
  TITLE     Molecular Dynamics of CYFIP2 Protein and Its R87C Variant Related
            to Early Infantile Epileptic Encephalopathy
  JOURNAL   Int J Mol Sci 23 (15), 8708 (2022)
   PUBMED   35955843
  REMARK    GeneRIF: Molecular Dynamics of CYFIP2 Protein and Its R87C Variant
            Related to Early Infantile Epileptic Encephalopathy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1253)
  AUTHORS   Li,Y., Song,X., Liu,L. and Yue,L.
  TITLE     NUAK2 silencing inhibits the proliferation, migration and
            epithelial-to-mesenchymal transition of cervical cancer cells via
            upregulating CYFIP2
  JOURNAL   Mol Med Rep 24 (5) (2021)
   PUBMED   34558636
  REMARK    GeneRIF: NUAK2 silencing inhibits the proliferation, migration and
            epithelialtomesenchymal transition of cervical cancer cells via
            upregulating CYFIP2.
REFERENCE   5  (residues 1 to 1253)
  AUTHORS   Biembengut,I.V., Silva,I.L.Z., Souza,T.A.C.B. and Shigunov,P.
  TITLE     Cytoplasmic FMR1 interacting protein (CYFIP) family members and
            their function in neural development and disorders
  JOURNAL   Mol Biol Rep 48 (8), 6131-6143 (2021)
   PUBMED   34327661
  REMARK    GeneRIF: Cytoplasmic FMR1 interacting protein (CYFIP) family
            members and their function in neural development and disorders.
            Review article
REFERENCE   6  (residues 1 to 1253)
  AUTHORS   Eden,S., Rohatgi,R., Podtelejnikov,A.V., Mann,M. and Kirschner,M.W.
  TITLE     Mechanism of regulation of WAVE1-induced actin nucleation by Rac1
            and Nck
  JOURNAL   Nature 418 (6899), 790-793 (2002)
   PUBMED   12181570
REFERENCE   7  (residues 1 to 1253)
  AUTHORS   Schenck,A., Bardoni,B., Moro,A., Bagni,C. and Mandel,J.L.
  TITLE     A highly conserved protein family interacting with the fragile X
            mental retardation protein (FMRP) and displaying selective
            interactions with FMRP-related proteins FXR1P and FXR2P
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8844-8849 (2001)
   PUBMED   11438699
REFERENCE   8  (residues 1 to 1253)
  AUTHORS   Saller,E., Tom,E., Brunori,M., Otter,M., Estreicher,A., Mack,D.H.
            and Iggo,R.
  TITLE     Increased apoptosis induction by 121F mutant p53
  JOURNAL   EMBO J 18 (16), 4424-4437 (1999)
   PUBMED   10449408
REFERENCE   9  (residues 1 to 1253)
  AUTHORS   Witke,W., Podtelejnikov,A.V., Di Nardo,A., Sutherland,J.D.,
            Gurniak,C.B., Dotti,C. and Mann,M.
  TITLE     In mouse brain profilin I and profilin II associate with regulators
            of the endocytic pathway and actin assembly
  JOURNAL   EMBO J 17 (4), 967-976 (1998)
   PUBMED   9463375
REFERENCE   10 (residues 1 to 1253)
  AUTHORS   Kitamura,T., Kitamura,Y., Yonezawa,K., Totty,N.F., Gout,I.,
            Hara,K., Waterfield,M.D., Sakaue,M., Ogawa,W. and Kasuga,M.
  TITLE     Molecular cloning of p125Nap1, a protein that associates with an
            SH3 domain of Nck
  JOURNAL   Biochem Biophys Res Commun 219 (2), 509-514 (1996)
   PUBMED   8605018
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG699081.1, BC011762.1, AL136549.1 and AC008676.6.
            
            Transcript Variant: This variant (1) and variant 2 encode the same
            isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.158742.1,
                                           SRR1660805.48154.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000620254.5/ ENSP00000479968.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1253
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..1253
                     /product="cytoplasmic FMR1-interacting protein 2 isoform
                     a"
                     /note="p53-inducible protein 121"
                     /calculated_mol_wt=145543
     Region          388..1221
                     /region_name="FragX_IP"
                     /note="Cytoplasmic Fragile-X interacting family;
                     pfam05994"
                     /db_xref="CDD:461799"
     Site            1037
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96F07.2)"
     CDS             1..1253
                     /gene="CYFIP2"
                     /gene_synonym="DEE65; EIEE65; PIR121"
                     /coded_by="NM_001037333.3:97..3858"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS75364.1"
                     /db_xref="GeneID:26999"
                     /db_xref="HGNC:HGNC:13760"
                     /db_xref="MIM:606323"
ORIGIN      
        1 mtthvtleda lsnvdlleel plpdqqpcie pppssimyqa nfdtnfedrn afvtgiaryi
       61 eqatvhssmn emleegheya vmlytwrscs raipqvkcne qpnrveiyek tvevlepevt
      121 klmkfmyfqr kaierfcsev krlchaerrk dfvseayllt lgkfinmfav ldelknmkcs
      181 vkndhsaykr aaqflrkmad pqsiqesqnl smflanhnri tqclhqqlev ipgyeellad
      241 ivnicvdyye nkmyltpsek hmllkvmgfg lylmdgnvsn iykldakkri nlskidkffk
      301 qlqvvplfgd mqielaryik tsahyeenks kwtctqssis pqyniceqmv qirddhirfi
      361 selarysnse vvtgsgldsq ksdeeyrelf dlalrglqll skwsahvmev yswklvhptd
      421 kfcnkdcpgt aeeyeratry nytseekfaf veviamikgl qvlmgrmesv fnqairntiy
      481 aalqdfaqvt lreplrqavr kkknvlisvl qairkticdw eggreppndp clrgekdpkg
      541 gfdikvprra vgpsstqlym vrtmleslia dksgskktlr ssldgpivla iedfhkqsff
      601 fthllnisea lqqccdlsql wfrefflelt mgrriqfpie msmpwiltdh iletkepsmm
      661 eyvlypldly ndsayyaltk fkkqflydei eaevnlcfdq fvykladqif ayykamagsv
      721 lldkrfraec knygviipyp psnryetllk qrhvqllgrs idlnrlitqr isaamyksld
      781 qaisrfesed ltsivelewl leinrlthrl lckhmtldsf damfreanhn vsapygritl
      841 hvfwelnfdf lpnycyngst nrfvrtaipf tqepqrdkpa nvqpyylygs kplniayshi
      901 yssyrnfvgp phfkticrll gyqgiavvme ellkivksll qgtilqyvkt lievmpkicr
      961 lprheygspg ileffhhqlk diieyaelkt dvfqslrevg nailfcllie qalsqeevcd
     1021 llhaapfqni lprvyikege rlevrmkrle akyaplhlvp lierlgtpqq iaiaregdll
     1081 tkerlccgls mfeviltrir sylqdpiwrg ppptngvmhv decvefhrlw samqfvycip
     1141 vgtneftaeq cfgdglnwag csiivllgqq rrfdlfdfcy hllkvqrqdg kdeiiknvpl
     1201 kkmadrirky qilnnevfai lnkymksvet dsstvehvrc fqppihqsla ttc
//
LOCUS       NP_001353546             567 aa            linear   PRI 27-APR-2025
DEFINITION  regulator of G-protein signaling 14 isoform 2 [Homo sapiens].
ACCESSION   NP_001353546 XP_005265851
VERSION     NP_001353546.1
DBSOURCE    REFSEQ: accession NM_001366617.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Sneddon,W.B., Ramineni,S., Van Doorn,G.E., Hepler,J.R. and
            Friedman,P.A.
  TITLE     Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport
  JOURNAL   Biochem Biophys Res Commun 733, 150700 (2024)
   PUBMED   39293332
  REMARK    GeneRIF: Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport.
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Wang,J., Guo,Y., He,Y., Qin,Y., Li,X., Yang,L., Liu,K. and Xiao,L.
  TITLE     Hepatic regulator of G protein signaling 14 ameliorates NAFLD
            through activating cAMP-AMPK signaling by targeting Gialpha1/3
  JOURNAL   Mol Metab 80, 101882 (2024)
   PUBMED   38237897
  REMARK    GeneRIF: Hepatic regulator of G protein signaling 14 ameliorates
            NAFLD through activating cAMP-AMPK signaling by targeting
            Gialpha1/3.
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Montanez-Miranda,C., Bramlett,S.N. and Hepler,J.R.
  TITLE     RGS14 expression in CA2 hippocampus, amygdala, and basal ganglia:
            Implications for human brain physiology and disease
  JOURNAL   Hippocampus 33 (3), 166-181 (2023)
   PUBMED   36541898
  REMARK    GeneRIF: RGS14 expression in CA2 hippocampus, amygdala, and basal
            ganglia: Implications for human brain physiology and disease.
            Review article
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Friedman,P.A., Sneddon,W.B., Mamonova,T., Montanez-Miranda,C.,
            Ramineni,S., Harbin,N.H., Squires,K.E., Gefter,J.V., Magyar,C.E.,
            Emlet,D.R. and Hepler,J.R.
  TITLE     RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated renal
            phosphate uptake via binding to the NHERF1 scaffolding protein
  JOURNAL   J Biol Chem 298 (5), 101836 (2022)
   PUBMED   35307350
  REMARK    GeneRIF: RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated
            renal phosphate uptake via binding to the NHERF1 scaffolding
            protein.
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Sierra,D.A., Gilbert,D.J., Householder,D., Grishin,N.V., Yu,K.,
            Ukidwe,P., Barker,S.A., He,W., Wensel,T.G., Otero,G., Brown,G.,
            Copeland,N.G., Jenkins,N.A. and Wilkie,T.M.
  TITLE     Evolution of the regulators of G-protein signaling multigene family
            in mouse and human
  JOURNAL   Genomics 79 (2), 177-185 (2002)
   PUBMED   11829488
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Kimple,R.J., De Vries,L., Tronchere,H., Behe,C.I., Morris,R.A.,
            Gist Farquhar,M. and Siderovski,D.P.
  TITLE     RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with
            guanine nucleotide dissociation inhibitor Activity
  JOURNAL   J Biol Chem 276 (31), 29275-29281 (2001)
   PUBMED   11387333
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Cho,H., Kozasa,T., Takekoshi,K., De Gunzburg,J. and Kehrl,J.H.
  TITLE     RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha-
            and G13alpha-mediated signaling pathways
  JOURNAL   Mol Pharmacol 58 (3), 569-576 (2000)
   PUBMED   10953050
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Traver,S., Bidot,C., Spassky,N., Baltauss,T., De Tand,M.F.,
            Thomas,J.L., Zalc,B., Janoueix-Lerosey,I. and Gunzburg,J.D.
  TITLE     RGS14 is a novel Rap effector that preferentially regulates the
            GTPase activity of galphao
  JOURNAL   Biochem J 350 Pt 1 (Pt 1), 19-29 (2000)
   PUBMED   10926822
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Snow,B.E., Antonio,L., Suggs,S., Gutstein,H.B. and Siderovski,D.P.
  TITLE     Molecular cloning and expression analysis of rat Rgs12 and Rgs14
  JOURNAL   Biochem Biophys Res Commun 233 (3), 770-777 (1997)
   PUBMED   9168931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC146507.2.
            
            On Oct 13, 2018 this sequence version replaced XP_005265851.1.
            
            Summary: This gene encodes a member of the regulator of G-protein
            signaling family. This protein contains one RGS domain, two
            Raf-like Ras-binding domains (RBDs), and one GoLoco domain. The
            protein attenuates the signaling activity of G-proteins by binding,
            through its GoLoco domain, to specific types of activated,
            GTP-bound G alpha subunits. Acting as a GTPase activating protein
            (GAP), the protein increases the rate of conversion of the GTP to
            GDP. This hydrolysis allows the G alpha subunits to bind G
            beta/gamma subunit heterodimers, forming inactive G-protein
            heterotrimers, thereby terminating the signal. Alternate
            transcriptional splice variants of this gene have been observed but
            have not been thoroughly characterized. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.114244.1,
                                           SRR1660807.8302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..567
                     /product="regulator of G-protein signaling 14 isoform 2"
                     /calculated_mol_wt=61444
     Region          19..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Region          58..186
                     /region_name="RGS_RGS14"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS14 protein; cd08743"
                     /db_xref="CDD:188697"
     Site            order(88..90,92..93,130..135,137..138,165,167..169,173)
                     /site_type="other"
                     /note="putative G-alpha-3 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:188697"
     Region          192..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97492; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Region          302..372
                     /region_name="RBD1_RGS14"
                     /note="Ras-binding domain (RBD) 1 of regulator of G
                     protein signaling 14 (RGS14); cd17137"
                     /db_xref="CDD:340657"
     Site            order(334,352)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340657"
     Region          373..444
                     /region_name="RBD2_RGS14"
                     /note="Ras-binding domain (RBD) 2 of regulator of G
                     protein signaling 14 (RGS14); cd17139"
                     /db_xref="CDD:340659"
     Site            order(385,407)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340659"
     Region          452..491
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Region          500..521
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          531..567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     CDS             1..567
                     /gene="RGS14"
                     /coded_by="NM_001366617.1:102..1805"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:10636"
                     /db_xref="HGNC:HGNC:9996"
                     /db_xref="MIM:602513"
ORIGIN      
        1 mpgkpkhlgv pngrmvlavs dgelssttgp qgqgegrgss lsihslpsgp sspfpteeqp
       61 vaswalsfer llqdplglay fteflkkefs aenvtfwkac erfqqipasd tqqlaqearn
      121 iyqeflssqa lspvnidrqa wlgeevlaep rpdmfraqql qifnlmkfds yarfvksply
      181 recllaeaeg rplrepgssr lgspdatrkk pklkpgkslp lgveelgqlp pvegpggrpl
      241 rksfrrelgg tanaalrres qgslnssasl dlgflafvss kseshrkslg stegesesrp
      301 gkyccvylpd gtaslalarp gltirdmlag icekrglslp dikvylvgne qkalvldqdc
      361 tvladqevrl enritfelel talervvris akptkrlqea lqpilekhgl splevvlhrp
      421 gekqpldlgk lvssvaaqrl vldtlpgvki skardkspcr sqgcpprtqd kathpppasp
      481 sslvkvpssa tgkrqtcdie glvellnrvq ssgahdqrgl lrkedlvlpe flqlpaqgps
      541 seetppqtks aaqpiggsln sttdsal
//
LOCUS       NP_056490                160 aa            linear   PRI 27-APR-2025
DEFINITION  growth arrest and DNA damage-inducible protein GADD45 beta [Homo
            sapiens].
ACCESSION   NP_056490
VERSION     NP_056490.2
DBSOURCE    REFSEQ: accession NM_015675.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Huang,M., Tao,X., Bao,J., Wang,J., Gong,X., Luo,L., Pan,S.,
            Yang,R., Gui,Y., Zhou,H., Xia,Y., Yang,Y., Sun,B., Liu,W. and
            Shu,X.
  TITLE     GADD45B in the ventral hippocampal CA1 modulates aversive memory
            acquisition and spatial cognition
  JOURNAL   Life Sci 346, 122618 (2024)
   PUBMED   38614306
  REMARK    GeneRIF: GADD45B in the ventral hippocampal CA1 modulates aversive
            memory acquisition and spatial cognition.
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Chen,L., Fang,C., Yuan,X., Liu,M., Wu,P., Zhong,L. and Chen,Z.
  TITLE     Has-miR-300-GADD45B promotes melanoma growth via cell cycle
  JOURNAL   Aging (Albany NY) 15 (23), 13920-13943 (2023)
   PUBMED   38070141
  REMARK    GeneRIF: Has-miR-300-GADD45B promotes melanoma growth via cell
            cycle.
            Erratum:[Aging (Albany NY). 2024 Jan 14;16(1):983. doi:
            10.18632/aging.205515. PMID: 38219232]
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Li,C., Wei,A. and Qin,Y.
  TITLE     Expression of GADD45B in Renal Tissue of Children with IgA
            Nephropathy and Correlation with Mesangial Hypercellularity
  JOURNAL   Fetal Pediatr Pathol 42 (5), 785-795 (2023)
   PUBMED   37534585
  REMARK    GeneRIF: Expression of GADD45B in Renal Tissue of Children with IgA
            Nephropathy and Correlation with Mesangial Hypercellularity.
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Li,Y., Shen,L., Tao,K., Xu,G. and Ji,K.
  TITLE     Key Roles of p53 Signaling Pathway-Related Factors GADD45B and
            SERPINE1 in the Occurrence and Development of Gastric Cancer
  JOURNAL   Mediators Inflamm 2023, 6368893 (2023)
   PUBMED   37662480
  REMARK    GeneRIF: Key Roles of p53 Signaling Pathway-Related Factors GADD45B
            and SERPINE1 in the Occurrence and Development of Gastric Cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Xu,W., Jiang,T., Shen,K., Zhao,D., Zhang,M., Zhu,W., Liu,Y. and
            Xu,C.
  TITLE     GADD45B regulates the carcinogenesis process of chronic atrophic
            gastritis and the metabolic pathways of gastric cancer
  JOURNAL   Front Endocrinol (Lausanne) 14, 1224832 (2023)
   PUBMED   37608794
  REMARK    GeneRIF: GADD45B regulates the carcinogenesis process of chronic
            atrophic gastritis and the metabolic pathways of gastric cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 160)
  AUTHORS   Sakaue,M., Adachi,H. and Jetten,A.M.
  TITLE     Post-transcriptional regulation of MyD118 and GADD45 in human lung
            carcinoma cells during 6-[3-(1-adamantyl)-4-hydroxyphenyl]-2-
            naphthalene carboxylic acid-induced apoptosis
  JOURNAL   Mol Pharmacol 55 (4), 668-676 (1999)
   PUBMED   10101024
REFERENCE   7  (residues 1 to 160)
  AUTHORS   Takekawa,M. and Saito,H.
  TITLE     A family of stress-inducible GADD45-like proteins mediate
            activation of the stress-responsive MTK1/MEKK4 MAPKKK
  JOURNAL   Cell 95 (4), 521-530 (1998)
   PUBMED   9827804
REFERENCE   8  (residues 1 to 160)
  AUTHORS   Koonin,E.V.
  TITLE     Cell cycle and apoptosis: possible roles of Gadd45 and MyD118
            proteins inferred from their homology to ribosomal proteins
  JOURNAL   J Mol Med (Berl) 75 (4), 236-238 (1997)
   PUBMED   9151207
REFERENCE   9  (residues 1 to 160)
  AUTHORS   Vairapandi,M., Balliet,A.G., Fornace,A.J. Jr., Hoffman,B. and
            Liebermann,D.A.
  TITLE     The differentiation primary response gene MyD118, related to
            GADD45, encodes for a nuclear protein which interacts with PCNA and
            p21WAF1/CIP1
  JOURNAL   Oncogene 12 (12), 2579-2594 (1996)
   PUBMED   8700517
REFERENCE   10 (residues 1 to 160)
  AUTHORS   Abdollahi,A., Lord,K.A., Hoffman-Liebermann,B. and Liebermann,D.A.
  TITLE     Sequence and expression of a cDNA encoding MyD118: a novel myeloid
            differentiation primary response gene induced by multiple cytokines
  JOURNAL   Oncogene 6 (1), 165-167 (1991)
   PUBMED   1899477
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK293087.1 and BM670459.1.
            
            On Feb 8, 2006 this sequence version replaced NP_056490.1.
            
            Summary: This gene is a member of a group of genes whose transcript
            levels are increased following stressful growth arrest conditions
            and treatment with DNA-damaging agents. The genes in this group
            respond to environmental stresses by mediating activation of the
            p38/JNK pathway.  This activation is mediated via their proteins
            binding and activating MTK1/MEKK4 kinase, which is an upstream
            activator of both p38 and JNK MAPKs. The function of these genes or
            their protein products is involved in the regulation of growth and
            apoptosis. These genes are regulated by different mechanisms, but
            they are often coordinately expressed and can function
            cooperatively in inhibiting cell growth. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.236157.1,
                                           SRR3476690.397772.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215631.9/ ENSP00000215631.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..160
                     /product="growth arrest and DNA damage-inducible protein
                     GADD45 beta"
                     /note="negative growth regulatory protein MyD118; myeloid
                     differentiation primary response protein MyD118"
                     /calculated_mol_wt=17687
     Region          21..120
                     /region_name="Ribosomal_L7Ae"
                     /note="Ribosomal protein L7Ae/L30e/S12e/Gadd45 family;
                     pfam01248"
                     /db_xref="CDD:426153"
     CDS             1..160
                     /gene="GADD45B"
                     /gene_synonym="GADD45BETA; MYD118"
                     /coded_by="NM_015675.4:233..715"
                     /db_xref="CCDS:CCDS32868.1"
                     /db_xref="GeneID:4616"
                     /db_xref="HGNC:HGNC:4096"
                     /db_xref="MIM:604948"
ORIGIN      
        1 mtleelvacd naaqkmqtvt aaveellvaa qrqdrltvgv yesaklmnvd pdsvvlclla
       61 ideeeeddia lqihftliqs fccdndiniv rvsgmqrlaq llgepaetqg tteardlhcl
      121 lvtnphtdaw kshglvevas yceesrgnnq wvpyislqer
//
LOCUS       NP_001347141             467 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 30 isoform e [Mus musculus].
ACCESSION   NP_001347141 XP_017177626
VERSION     NP_001347141.1
DBSOURCE    REFSEQ: accession NM_001360212.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Laudermilk,L.T., Tovar,A., Homstad,A.K., Thomas,J.M.,
            McFadden,K.M., Tune,M.K., Cowley,D.O., Mock,J.R., Ideraabdullah,F.
            and Kelada,S.N.P.
  TITLE     Baseline and innate immune response characterization of a Zfp30
            knockout mouse strain
  JOURNAL   Mamm Genome 31 (7-8), 205-214 (2020)
   PUBMED   32860515
  REMARK    GeneRIF: Baseline and innate immune response characterization of a
            Zfp30 knockout mouse strain.
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Chen,W., Schwalie,P.C., Pankevich,E.V., Gubelmann,C., Raghav,S.K.,
            Dainese,R., Cassano,M., Imbeault,M., Jang,S.M., Russeil,J.,
            Delessa,T., Duc,J., Trono,D., Wolfrum,C. and Deplancke,B.
  TITLE     ZFP30 promotes adipogenesis through the KAP1-mediated activation of
            a retrotransposon-derived Pparg2 enhancer
  JOURNAL   Nat Commun 10 (1), 1809 (2019)
   PUBMED   31000713
  REMARK    GeneRIF: Using murine and human in vitro and in vivo models, study
            demonstrated that ZFP30 promotes adipogenesis by directly targeting
            and activating a retrotransposon-derived Pparg2 enhancer. Through
            mechanistic studies, study further show that ZFP30 recruits the
            co-regulator KAP1, which acts as a ZFP30 co-activator in this
            adipogenic context.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Laudermilk,L.T., Thomas,J.M. and Kelada,S.N.
  TITLE     Differential Regulation of Zfp30 Expression in Murine Airway
            Epithelia Through Altered Binding of ZFP148 to rs51434084
  JOURNAL   G3 (Bethesda) 8 (2), 687-693 (2018)
   PUBMED   29242385
  REMARK    GeneRIF: Data indicate zinc finger protein 148 (ZFP148) as a
            transcription factor that differentially binds to the zinc finger
            protein 30 protein (Zfp30) promoter region harboring rs51434084.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Rutledge,H., Aylor,D.L., Carpenter,D.E., Peck,B.C., Chines,P.,
            Ostrowski,L.E., Chesler,E.J., Churchill,G.A., de Villena,F.P. and
            Kelada,S.N.
  TITLE     Genetic regulation of Zfp30, CXCL1, and neutrophilic inflammation
            in murine lung
  JOURNAL   Genetics 198 (2), 735-745 (2014)
   PUBMED   25114278
  REMARK    GeneRIF: Zfp30 is expressed in airway epithelia in the normal mouse
            lung and Zfp30 expression in vitro affects CXCL1 responses to an
            immune stimulus.
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Denny,P. and Ashworth,A.
  TITLE     Zfp30, a KRAB domain containing zinc finger protein gene, maps to
            mouse chromosome 7
  JOURNAL   Mamm Genome 5 (10), 643-645 (1994)
   PUBMED   7849402
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Ashworth,A. and Denny,P.
  TITLE     Zinc finger protein genes in the mouse genome
  JOURNAL   Mamm Genome 1 (3), 196-200 (1991)
   PUBMED   1797234
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC156934.1.
            
            On Jan 30, 2018 this sequence version replaced XP_017177626.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (e) is
            shorter at the N-terminus compared to isoform a. Variants 5, 6, and
            7 all encode the same isoform (e).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3196936.1,
                                           SRR7652917.1162110.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 17.26 cM"
     Protein         1..467
                     /product="zinc finger protein 30 isoform e"
                     /calculated_mol_wt=55073
     Region          97..457
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          108..128
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          136..156
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          164..184
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(169,171,173,175..176,179..180,183,197,199,203..204,
                     207..208,211,225,227,229,231..232,235..236,239)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          192..212
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          220..239
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          248..268
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          276..296
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(281,283,285,287..288,291..292,295,309,311,315..316,
                     319..320,323,337,339,341,343..344,347..348,351)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          304..324
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          332..352
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          360..380
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          388..408
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(393,395,397,399..400,403..404,407,421,423,427..428,
                     431..432,435,449,451,453,455..456,459..460,463)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          416..436
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          444..464
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..467
                     /gene="Zfp30"
                     /gene_synonym="2610306P15Rik; Zfp-30"
                     /coded_by="NM_001360212.1:1123..2526"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS90199.1"
                     /db_xref="GeneID:22693"
                     /db_xref="MGI:MGI:99178"
ORIGIN      
        1 mivraekrrw srdlesryss ngllpeknty einlspweim griqrrgped sllgkdfeyk
       61 iyeeqenshr vyfrhviktt sgkrpryrkr tpvslyqktp ngekpyecge cgkafkvrqq
      121 ltfhqrihtg ekpyeckecg kafrqcahls rhqrihasdk lyeckkcaki ftcssdlrgh
      181 qrshvgekpy dckecgkafr vrgqlmlhqr ihtgekpyac tecgksfrqv ahltrhqrln
      241 sgssrhecke cgraflcstg lrlhhklhtg ekpydckecg kafrvrqqlt lherihtgek
      301 pfdckecgkt fsrgyhltlh qrihtgekpy eckecrkffr ryselishqg ihigekpydc
      361 kecgkafrlf sqltqhqsih fgekpykcme cektfrllsq ltqhqsihtg ekpydckecg
      421 kafrlhssli qhqrihsgek pykcteckka frqhshltyh qrihknl
//
LOCUS       NP_742160                175 aa            linear   ROD 27-APR-2025
DEFINITION  B9 domain-containing protein 2 [Mus musculus].
ACCESSION   NP_742160 XP_994805 XP_994845
VERSION     NP_742160.1
DBSOURCE    REFSEQ: accession NM_172148.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Riehl,D.R., Sharma,A., Roewe,J., Reinhardt,C., Schafer,K. and
            Bosmann,M.
  TITLE     Reply to Chong et al.: Investigating TGFbeta1 biological activities
            using genetically engineered mouse strains
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2408647121 (2024)
   PUBMED   39423253
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Martinez-Mayer,J., Brinkmeier,M.L., O'Connell,S.P., Ukagwu,A.,
            Marti,M.A., Miras,M., Forclaz,M.V., Benzrihen,M.G., Cheung,L.Y.M.,
            Camper,S.A., Ellsworth,B.S., Raetzman,L.T., Perez-Millan,M.I. and
            Davis,S.W.
  TITLE     Knockout mice with pituitary malformations help identify human
            cases of hypopituitarism
  JOURNAL   Genome Med 16 (1), 75 (2024)
   PUBMED   38822427
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Chong,D.L.W., Mikolasch,T.A., Sahota,J., Rebeyrol,C.,
            Garthwaite,H.S., Booth,H.L., Heightman,M., Denneny,E.K., Jose,R.J.,
            Khawaja,A.A., Duckworth,A., Labelle,M., Scotton,C.J. and
            Porter,J.C.
  TITLE     Investigating the role of platelets and platelet-derived
            transforming growth factor-beta in idiopathic pulmonary fibrosis
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 325 (4), L487-L499 (2023)
   PUBMED   37643008
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Gutcher,I., Donkor,M.K., Ma,Q., Rudensky,A.Y., Flavell,R.A. and
            Li,M.O.
  TITLE     Autocrine transforming growth factor-beta1 promotes in vivo Th17
            cell differentiation
  JOURNAL   Immunity 34 (3), 396-408 (2011)
   PUBMED   21435587
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Breunig,J.J., Sarkisian,M.R., Arellano,J.I., Morozov,Y.M.,
            Ayoub,A.E., Sojitra,S., Wang,B., Flavell,R.A., Rakic,P. and Town,T.
  TITLE     Primary cilia regulate hippocampal neurogenesis by mediating sonic
            hedgehog signaling
  JOURNAL   Proc Natl Acad Sci U S A 105 (35), 13127-13132 (2008)
   PUBMED   18728187
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Town,T., Breunig,J.J., Sarkisian,M.R., Spilianakis,C., Ayoub,A.E.,
            Liu,X., Ferrandino,A.F., Gallagher,A.R., Li,M.O., Rakic,P. and
            Flavell,R.A.
  TITLE     The stumpy gene is required for mammalian ciliogenesis
  JOURNAL   Proc Natl Acad Sci U S A 105 (8), 2853-2858 (2008)
   PUBMED   18287022
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Kaplan,D.H., Li,M.O., Jenison,M.C., Shlomchik,W.D., Flavell,R.A.
            and Shlomchik,M.J.
  TITLE     Autocrine/paracrine TGFbeta1 is required for the development of
            epidermal Langerhans cells
  JOURNAL   J Exp Med 204 (11), 2545-2552 (2007)
   PUBMED   17938236
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Li,M.O., Wan,Y.Y. and Flavell,R.A.
  TITLE     T cell-produced transforming growth factor-beta1 controls T cell
            tolerance and regulates Th1- and Th17-cell differentiation
  JOURNAL   Immunity 26 (5), 579-591 (2007)
   PUBMED   17481928
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC028440.1 and BX517802.1.
            
            On or before May 4, 2006 this sequence version replaced
            XP_994805.1, XP_994845.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028440.1, SRR1660819.271342.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 13.97 cM"
     Protein         1..175
                     /product="B9 domain-containing protein 2"
                     /calculated_mol_wt=19119
     Region          4..159
                     /region_name="B9-C2"
                     /note="Ciliary basal body-associated, B9 protein;
                     pfam07162"
                     /db_xref="CDD:462108"
     CDS             1..175
                     /gene="B9d2"
                     /gene_synonym="stumpy"
                     /coded_by="NM_172148.2:230..757"
                     /db_xref="CCDS:CCDS20992.1"
                     /db_xref="GeneID:232987"
                     /db_xref="MGI:MGI:2387643"
ORIGIN      
        1 maevhvigqi igatgfsess lfckwgihtg aawkllsgvr egqtqvdtpq igdmaywshp
       61 idlhfatkgl qgwprlhlqv wsqdsfgrcq lagygfchvp sspgthqldc ptwrplgswr
      121 eqlarafvgg gpqllhadti ysgadryrlh taaggtvhlg iglllrhfdr ygvec
//
LOCUS       NP_001350611             782 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear factor of activated T-cells, cytoplasmic 4 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001350611 XP_011535101
VERSION     NP_001350611.1
DBSOURCE    REFSEQ: accession NM_001363682.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Yu,S., Sun,Z., Ju,T., Liu,Y., Mei,Z., Wang,C., Qu,Z., Li,N., Wu,F.,
            Liu,K., Lu,M., Huang,M., Pang,X., Jia,Y., Li,Y., Zhang,Y., Dou,S.,
            Jiang,J., Dong,X., Huang,C., Li,W., Zhang,Y., Yuan,Y., Yang,B. and
            Du,W.
  TITLE     The m7G Methyltransferase Mettl1 Drives Cardiac Hypertrophy by
            Regulating SRSF9-Mediated Splicing of NFATc4
  JOURNAL   Adv Sci (Weinh) 11 (29), e2308769 (2024)
   PUBMED   38810124
  REMARK    GeneRIF: The m7G Methyltransferase Mettl1 Drives Cardiac
            Hypertrophy by Regulating SRSF9-Mediated Splicing of NFATc4.
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Zhang,X., Lei,F., Wang,X.M., Deng,K.Q., Ji,Y.X., Zhang,Y., Li,H.,
            Zhang,X.D., Lu,Z. and Zhang,P.
  TITLE     NULP1 Alleviates Cardiac Hypertrophy by Suppressing NFAT3
            Transcriptional Activity
  JOURNAL   J Am Heart Assoc 9 (16), e016419 (2020)
   PUBMED   32805187
  REMARK    GeneRIF: NULP1 Alleviates Cardiac Hypertrophy by Suppressing NFAT3
            Transcriptional Activity.
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Cole,A.J., Iyengar,M., Panesso-Gomez,S., O'Hayer,P., Chan,D.,
            Delgoffe,G.M., Aird,K.M., Yoon,E., Bai,S. and Buckanovich,R.J.
  TITLE     NFATC4 promotes quiescence and chemotherapy resistance in ovarian
            cancer
  JOURNAL   JCI Insight 5 (7), 131486 (2020)
   PUBMED   32182216
  REMARK    GeneRIF: NFATC4 promotes quiescence and chemotherapy resistance in
            ovarian cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Kaminuma,O., Kitamura,N., Nishito,Y., Nemoto,S., Tatsumi,H.,
            Mori,A. and Hiroi,T.
  TITLE     Downregulation of NFAT3 Due to Lack of T-Box Transcription Factor
            TBX5 Is Crucial for Cytokine Expression in T Cells
  JOURNAL   J Immunol 200 (1), 92-100 (2018)
   PUBMED   29180489
  REMARK    GeneRIF: TBX5 deficiency-mediated downregulation of NFAT3 is
            crucial for the high cytokine-producing activity of T cells
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Molkentin,J.D., Lu,J.R., Antos,C.L., Markham,B., Richardson,J.,
            Robbins,J., Grant,S.R. and Olson,E.N.
  TITLE     A calcineurin-dependent transcriptional pathway for cardiac
            hypertrophy
  JOURNAL   Cell 93 (2), 215-228 (1998)
   PUBMED   9568714
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Aramburu,J., Garcia-Cozar,F., Raghavan,A., Okamura,H., Rao,A. and
            Hogan,P.G.
  TITLE     Selective inhibition of NFAT activation by a peptide spanning the
            calcineurin targeting site of NFAT
  JOURNAL   Mol Cell 1 (5), 627-637 (1998)
   PUBMED   9660947
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Rao,A., Luo,C. and Hogan,P.G.
  TITLE     Transcription factors of the NFAT family: regulation and function
  JOURNAL   Annu Rev Immunol 15, 707-747 (1997)
   PUBMED   9143705
  REMARK    Review article
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Hoey,T., Sun,Y.L., Williamson,K. and Xu,X.
  TITLE     Isolation of two new members of the NF-AT gene family and
            functional characterization of the NF-AT proteins
  JOURNAL   Immunity 2 (5), 461-472 (1995)
   PUBMED   7749981
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Vacca,A., Farina,M., Maroder,M., Alesse,E., Screpanti,I., Frati,L.
            and Gulino,A.
  TITLE     Human immunodeficiency virus type-1 tat enhances interleukin-2
            promoter activity through synergism with phorbol ester and
            calcium-mediated activation of the NF-AT cis-regulatory motif
  JOURNAL   Biochem Biophys Res Commun 205 (1), 467-474 (1994)
   PUBMED   7999066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL096870.5 and EU887645.1.
            
            On May 29, 2018 this sequence version replaced XP_011535101.1.
            
            Summary: This gene encodes a member of the nuclear factor of
            activated T cells (NFAT) protein family. The encoded protein is
            part of a DNA-binding transcription complex. This complex consists
            of at least two components: a preexisting cytosolic component that
            translocates to the nucleus upon T cell receptor stimulation and an
            inducible nuclear component. NFAT proteins are activated by the
            calmodulin-dependent phosphatase, calcineurin. The encoded protein
            plays a role in the inducible expression of cytokine genes in T
            cells, especially in the induction of interleukin-2 and
            interleukin-4. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jan 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU887645.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..782
                     /product="nuclear factor of activated T-cells, cytoplasmic
                     4 isoform 9"
                     /note="nuclear factor of activated T-cells, cytoplasmic 4;
                     T-cell transcription factor NFAT3; nuclear factor of
                     activated T-cells, cytoplasmic, calcineurin-dependent 4"
                     /calculated_mol_wt=82860
     Region          <202..401
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          395..568
                     /region_name="RHD-n_NFAT"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor of activated T-cells (NFAT)
                     proteins; cd07881"
                     /db_xref="CDD:143641"
     Site            order(418,421,423..424,426..428,475,516,518..519,533..534,
                     536,567)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143641"
     Region          573..673
                     /region_name="IPT_NFAT"
                     /note="IPT domain of the NFAT family of transcription
                     factors. NFAT transcription complexes are a target of
                     calcineurin, a calcium dependent phosphatase, and activate
                     genes mainly involved in cell-cell-interaction; cd01178"
                     /db_xref="CDD:238583"
     Site            order(597,661)
                     /site_type="DNA binding"
                     /note="DNA binding sites [nucleotide binding]"
                     /db_xref="CDD:238583"
     CDS             1..782
                     /gene="NFATC4"
                     /gene_synonym="NF-AT3; NF-ATC4; NFAT3"
                     /coded_by="NM_001363682.1:316..2664"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS86379.1"
                     /db_xref="GeneID:4776"
                     /db_xref="HGNC:HGNC:7778"
                     /db_xref="MIM:602699"
ORIGIN      
        1 mpasissifp gptlllscgs eeldsedapp ccrlalgepp pygaapigip rpppprpgmh
       61 sppprpapsp gtwesqpars vrlggpggga ggagggrvle cpsiritsis ptpeppaale
      121 dnpdawgdgs prdypppegf ggyreaggqg ggaffspspg ssslsswsff sdasdeaaly
      181 aacdevesel neaasrfglg splpsprasp rpwtpedpws lygpspggrg pedswlllsa
      241 pgptpasprp aspcgkrrys ssgtpssasp alsrrgslge egsepppppp lplardpgsp
      301 gpfdyvgapp aesipqktrr tsseqavalp rseepascng klplgaeesv appggsrkev
      361 agmdylavps plawskarig ghspifrtsa lppldwplps qyeqlelrie vqprahhrah
      421 yetegsrgav kaapgghpvv kllgysekpl tlqmfigtad ernlrphafy qvhritgkmv
      481 atasyeavvs gtkvlemtll pennmaanid cagilklrns dielrkgetd igrkntrvrl
      541 vfrvhvpqgg gkvvsvqaas vpiecsqrsa qelpqveays psacsvrgge elvltgsnfl
      601 pdskvvfier gpdgklqwee eatvnrlqsn evtltltvpe ysnkrvsrpv qvyfyvsngr
      661 rkrsptqsfr flpvickeep lpdsslrgfp sasatpfgtd mdfspprppy psyphedpac
      721 etpylsegfg ygmpplypqt gpppsyrpgl rmfpetrgtt vseiigrdls gfpappgeep
      781 pa
//
LOCUS       NP_001350045             427 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX39A isoform a [Mus musculus].
ACCESSION   NP_001350045 XP_006531395
VERSION     NP_001350045.1
DBSOURCE    REFSEQ: accession NM_001363116.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Nai,S., Wang,M., Yang,J., Ling,B., Dong,Q., Yang,X., Du,X., Lu,M.,
            Liu,L., Yu,Z. and Chen,L.
  TITLE     Novel role for Ddx39 in differentiation and telomere length
            regulation of embryonic stem cells
  JOURNAL   Cell Death Differ 31 (11), 1534-1544 (2024)
   PUBMED   39107495
  REMARK    GeneRIF: Novel role for Ddx39 in differentiation and telomere
            length regulation of embryonic stem cells.
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Cesari,E., Farini,D., Medici,V., Ehrmann,I., Guerra,M., Testa,E.,
            Naro,C., Geloso,M.C., Pagliarini,V., La Barbera,L., D'Amelio,M.,
            Orsini,T., Vecchioli,S.F., Tamagnone,L., Fort,P., Viscomi,M.T.,
            Elliott,D.J. and Sette,C.
  TITLE     Differential expression of paralog RNA binding proteins establishes
            a dynamic splicing program required for normal cerebral cortex
            development
  JOURNAL   Nucleic Acids Res 52 (8), 4167-4184 (2024)
   PUBMED   38324473
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Brandsma,I., Sato,K., van Rossum-Fikkert,S.E., van Vliet,N.,
            Sleddens,E., Reuter,M., Odijk,H., van den Tempel,N.,
            Dekkers,D.H.W., Bezstarosti,K., Demmers,J.A.A., Maas,A.,
            Lebbink,J., Wyman,C., Essers,J., van Gent,D.C., Baarends,W.M.,
            Knipscheer,P., Kanaar,R. and Zelensky,A.N.
  TITLE     HSF2BP Interacts with a Conserved Domain of BRCA2 and Is Required
            for Mouse Spermatogenesis
  JOURNAL   Cell Rep 27 (13), 3790-3798 (2019)
   PUBMED   31242413
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Kuramitsu,Y., Suenaga,S., Wang,Y., Tokuda,K., Kitagawa,T.,
            Tanaka,T., Akada,J., Maehara,S., Maehara,Y. and Nakamura,K.
  TITLE     Up-regulation of DDX39 in human pancreatic cancer cells with
            acquired gemcitabine resistance compared to gemcitabine-sensitive
            parental cells
  JOURNAL   Anticancer Res 33 (8), 3133-3136 (2013)
   PUBMED   23898070
  REMARK    GeneRIF: The expression of DDX39 in gemcitabine-sensitive KLM1 and
            -resistant KLM1-R cells was compared.
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Wisskirchen,C., Ludersdorfer,T.H., Muller,D.A., Moritz,E. and
            Pavlovic,J.
  TITLE     Interferon-induced antiviral protein MxA interacts with the
            cellular RNA helicases UAP56 and URH49
  JOURNAL   J Biol Chem 286 (40), 34743-34751 (2011)
   PUBMED   21859714
  REMARK    GeneRIF: Mx proteins exert their antiviral activity against IAV by
            interfering with the function of the RNA helicases UAP56 and URH49
REFERENCE   8  (residues 1 to 427)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Pryor,A., Tung,L., Yang,Z., Kapadia,F., Chang,T.H. and Johnson,L.F.
  TITLE     Growth-regulated expression and G0-specific turnover of the mRNA
            that encodes URH49, a mammalian DExH/D box protein that is highly
            related to the mRNA export protein UAP56
  JOURNAL   Nucleic Acids Res 32 (6), 1857-1865 (2004)
   PUBMED   15047853
  REMARK    GeneRIF: Regulation of URH49 mRNA expression and comparison with
            the related UAP56 RNA helicase.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC164432.3.
            
            On May 8, 2018 this sequence version replaced XP_006531395.1.
            
            Transcript Variant: This variant (1) represents the longest
            protein-coding transcript and encodes isoform a. Variants 1 and 2
            both encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.51111.1,
                                           SRR7345562.835759.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849379, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 40.22 cM"
     Protein         1..427
                     /product="ATP-dependent RNA helicase DDX39A isoform a"
                     /EC_number="3.6.4.13"
                     /note="DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 39;
                     UAP56-related helicase, 49 kDa; ATP-dependent RNA helicase
                     DDX39; ATP-dependent RNA helicase DDX39A; DEAD box protein
                     39; DEAD (Asp-Glu-Ala-Asp) box polypeptide 39"
                     /calculated_mol_wt=48936
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDW0.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O00148; propagated from
                     UniProtKB/Swiss-Prot (Q8VDW0.1)"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O00148; propagated from
                     UniProtKB/Swiss-Prot (Q8VDW0.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00148; propagated from
                     UniProtKB/Swiss-Prot (Q8VDW0.1)"
     Region          43..250
                     /region_name="DEADc_DDX39"
                     /note="DEAD-box helicase domain of DEAD box protein 39;
                     cd17950"
                     /db_xref="CDD:350708"
     Region          44..72
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDW0.1)"
     Site            order(46,64,66..68,71,90..96,195..196)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350708"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O00148; propagated from
                     UniProtKB/Swiss-Prot (Q8VDW0.1)"
     Region          195..198
                     /region_name="DECD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDW0.1)"
     Region          261..390
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(349,351,376,379..380)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00148; propagated from
                     UniProtKB/Swiss-Prot (Q8VDW0.1)"
     CDS             1..427
                     /gene="Ddx39a"
                     /gene_synonym="2610307C23Rik; BAT1; Ddx39; DDXL; URH49"
                     /coded_by="NM_001363116.1:278..1561"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS22460.1"
                     /db_xref="GeneID:68278"
                     /db_xref="MGI:MGI:1915528"
ORIGIN      
        1 maeqdvenel ldydedeepq apqestpapp kkdvkgsyvs ihssgfrdfl lkpellraiv
       61 dcgfehpsev qhecipqail gmdvlcqaks gmgktavfvl atlqqiepvn gqvsvlvmch
      121 trelafqisk eyerfskymp svkvsvffgg lsikkdedvl kkncphvvvg tpgrilalvr
      181 srslnlrnvk hfvldecdkm leqldmrrdv qeifrltphe kqcmmfsatl skeirpvcrk
      241 fmqdpmevfv ddetkltlhg lqqyyvklkd seknrklfdl ldvlefnqvv ifvksvqrcm
      301 alaqllveqn fpaiaihrgm aqeerlsryq qfkdfqrril vatnlfgrgm diervnivfn
      361 ydmpedsdty lhrvaragrf gtkglavtfv sdendakiln dvqdrfevnv aelpeeidis
      421 tyieqsr
//
LOCUS       NP_872338                210 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 61 [Homo sapiens].
ACCESSION   NP_872338
VERSION     NP_872338.1
DBSOURCE    REFSEQ: accession NM_182532.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590440.1, BG430102.1, BC029775.1 and AA918832.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029775.1, BI764342.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371268.4/ ENSP00000360315.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..210
                     /product="transmembrane protein 61"
                     /calculated_mol_wt=22039
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N0U2.1)"
     Region          20..201
                     /region_name="TMEM61"
                     /note="TMEM61 protein family; pfam15105"
                     /db_xref="CDD:464506"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N0U2.1)"
     Region          140..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N0U2.1)"
     CDS             1..210
                     /gene="TMEM61"
                     /coded_by="NM_182532.3:439..1071"
                     /db_xref="CCDS:CCDS601.1"
                     /db_xref="GeneID:199964"
                     /db_xref="HGNC:HGNC:27296"
ORIGIN      
        1 malpqmcdgs hlastlrycm tvsgtvvlva gtlcfawwse gdataqpgql appteypvpe
       61 gpspllrsvs fvccgaggll lligllwsvk asipgpprwd pyhlsrdlyy ltvessekes
      121 crtpkvvdip tyeeavsfpv aegpptppay pteealepsg srdallstqp awpppsyesi
      181 slaldavsae ttpsatrscs glvqtarggs
//
LOCUS       NP_005319                552 aa            linear   PRI 27-APR-2025
DEFINITION  hyaluronan synthase 2 [Homo sapiens].
ACCESSION   NP_005319 XP_943808
VERSION     NP_005319.1
DBSOURCE    REFSEQ: accession NM_005328.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Liu,Z., Yu,K., Chen,K., Liu,J., Dai,K. and Zhao,P.
  TITLE     HAS2 facilitates glioma cell malignancy and suppresses ferroptosis
            in an FZD7-dependent manner
  JOURNAL   Cancer Sci 115 (8), 2602-2616 (2024)
   PUBMED   38816349
  REMARK    GeneRIF: HAS2 facilitates glioma cell malignancy and suppresses
            ferroptosis in an FZD7-dependent manner.
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Wang,J., Ruan,S., Yu,T., Meng,X., Ran,J., Cen,C., Kong,C., Bao,X.,
            Li,Z., Wang,Y., Ren,M., Guo,P., Teng,Y. and Zhang,D.
  TITLE     Upregulation of HAS2 promotes glioma cell proliferation and
            chemoresistance via c-myc
  JOURNAL   Cell Signal 120, 111218 (2024)
   PUBMED   38734194
  REMARK    GeneRIF: Upregulation of HAS2 promotes glioma cell proliferation
            and chemoresistance via c-myc.
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Faizal,A.M., Elias,M.H., Jin,N.M., Abu,M.A., Syafruddin,S.E.,
            Zainuddin,A.A., Suzuki,N. and Karim,A.K.A.
  TITLE     Unravelling the role of HAS2, GREM1, and PTGS2 gene expression in
            cumulus cells: implications for human oocyte development competency
            - a systematic review and integrated bioinformatic analysis
  JOURNAL   Front Endocrinol (Lausanne) 15, 1274376 (2024)
   PUBMED   38524634
  REMARK    GeneRIF: Unravelling the role of HAS2, GREM1, and PTGS2 gene
            expression in cumulus cells: implications for human oocyte
            development competency - a systematic review and integrated
            bioinformatic analysis.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Liu,R., Ye,Z., Liu,Q., Xuan,M., Li,R., Zhang,L., Zhang,K., Fang,P.
            and Xue,Y.
  TITLE     MicroRNA-376b is involved in the pathogenesis of thyroid-associated
            ophthalmopathy by regulating HAS2
  JOURNAL   Endocrine 82 (1), 87-95 (2023)
   PUBMED   37231239
  REMARK    GeneRIF: MicroRNA-376b is involved in the pathogenesis of
            thyroid-associated ophthalmopathy by regulating HAS2.
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Yang,J., Wang,L., Zhang,Z., Sun,Q. and Zhang,Y.
  TITLE     Downregulation of HAS-2 regulates the chondrocyte cytoskeleton and
            induces cartilage degeneration by activating the RhoA/ROCK
            signaling pathway
  JOURNAL   Int J Mol Med 52 (1) (2023)
   PUBMED   37232339
  REMARK    GeneRIF: Downregulation of HAS-2 regulates the chondrocyte
            cytoskeleton and induces cartilage degeneration by activating the
            RhoA/ROCK signaling pathway.
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Suzuki,K., Yamamoto,T., Usui,T., Suzuki,K., Heldin,P. and
            Yamashita,H.
  TITLE     Expression of hyaluronan synthase in intraocular proliferative
            diseases: regulation of expression in human vascular endothelial
            cells by transforming growth factor-beta
  JOURNAL   Jpn J Ophthalmol 47 (6), 557-564 (2003)
   PUBMED   14636845
  REMARK    GeneRIF: Expression of each hyaluronan synthase isoform is
            regulated differently by growth factors and cytokines in vascular
            endothelial cells. Expressed in proliferative membranes from
            proliferative vitreoretinal diseases. May affect progression of
            diseases.
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Simpson,M.A., Wilson,C.M., Furcht,L.T., Spicer,A.P., Oegema,T.R.
            Jr. and McCarthy,J.B.
  TITLE     Manipulation of hyaluronan synthase expression in prostate
            adenocarcinoma cells alters pericellular matrix retention and
            adhesion to bone marrow endothelial cells
  JOURNAL   J Biol Chem 277 (12), 10050-10057 (2002)
   PUBMED   11790779
  REMARK    GeneRIF: hyaluronan synthase expression in prostate adenocarcinoma
            cells
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Spicer,A.P. and Nguyen,T.K.
  TITLE     Mammalian hyaluronan synthases: investigation of functional
            relationships in vivo
  JOURNAL   Biochem Soc Trans 27 (2), 109-115 (1999)
   PUBMED   10093717
  REMARK    Review article
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Spicer,A.P., Seldin,M.F., Olsen,A.S., Brown,N., Wells,D.E.,
            Doggett,N.A., Itano,N., Kimata,K., Inazawa,J. and McDonald,J.A.
  TITLE     Chromosomal localization of the human and mouse hyaluronan synthase
            genes
  JOURNAL   Genomics 41 (3), 493-497 (1997)
   PUBMED   9169154
REFERENCE   10 (residues 1 to 552)
  AUTHORS   Watanabe,K. and Yamaguchi,Y.
  TITLE     Molecular identification of a putative human hyaluronan synthase
  JOURNAL   J Biol Chem 271 (38), 22945-22948 (1996)
   PUBMED   8798477
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104233.2, U54804.1 and
            AC022909.13.
            
            On Mar 4, 2006 this sequence version replaced XP_943808.1.
            
            Summary:  Hyaluronan or hyaluronic acid (HA) is a high molecular
            weight unbranched polysaccharide synthesized by a wide variety of
            organisms from bacteria to mammals, and is a constituent of the
            extracellular matrix.  It consists of alternating glucuronic acid
            and N-acetylglucosamine residues that are linked by beta-1-3 and
            beta-1-4 glycosidic bonds.  HA is synthesized by membrane-bound
            synthase at the inner surface of the plasma membrane, and the
            chains are extruded through pore-like structures into the
            extracellular space.  It serves a variety of functions, including
            space filling, lubrication of joints, and provision of a matrix
            through which cells can migrate.  HA is actively produced during
            wound healing and tissue repair to provide a framework for ingrowth
            of blood vessels and fibroblasts.  Changes in the serum
            concentration of HA are associated with inflammatory and
            degenerative arthropathies such as rheumatoid arthritis.  In
            addition, the interaction of HA with the leukocyte receptor CD44 is
            important in tissue-specific homing by leukocytes, and
            overexpression of HA receptors has been correlated with tumor
            metastasis.  HAS2 is a member of the newly identified vertebrate
            gene family encoding putative hyaluronan synthases, and its amino
            acid sequence shows significant homology to glycosaminoglycan
            synthetase (DG42) from Xenopus laevis, and human and murine
            hyaluronan synthase 1. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence consistent with
            the reference genome assembly was not available for all regions of
            the RefSeq transcript. The extent of this transcript is supported
            by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297724.1, SRR1803614.257799.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267750 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303924.5/ ENSP00000306991.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..552
                     /product="hyaluronan synthase 2"
                     /EC_number="2.4.1.212"
                     /note="hyaluronate synthase 2; hyaluronic acid synthase 2;
                     HA synthase 2"
                     /calculated_mol_wt=63436
     Site            12..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92819.1)"
     Site            46..66
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92819.1)"
     Region          84..361
                     /region_name="GT2_HAS"
                     /note="Hyaluronan synthases catalyze polymerization of
                     hyaluronan; cd06434"
                     /db_xref="CDD:133056"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:21228273; propagated from
                     UniProtKB/Swiss-Prot (Q92819.1)"
     Site            212..214
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133056"
     Site            221
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:22887999; propagated from
                     UniProtKB/Swiss-Prot (Q92819.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:32993960; propagated from
                     UniProtKB/Swiss-Prot (Q92819.1)"
     Site            375..395
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92819.1)"
     Site            403..423
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92819.1)"
     Site            430..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92819.1)"
     Site            476..496
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92819.1)"
     Site            511..531
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92819.1)"
     CDS             1..552
                     /gene="HAS2"
                     /coded_by="NM_005328.3:589..2247"
                     /db_xref="CCDS:CCDS6335.1"
                     /db_xref="GeneID:3037"
                     /db_xref="HGNC:HGNC:4819"
                     /db_xref="MIM:601636"
ORIGIN      
        1 mhcerflcil riigttlfgv slllgitaay ivgyqfiqtd nyyfsfglyg aflashliiq
       61 slfaflehrk mkksletpik lnktvalcia ayqedpdylr kclqsvkrlt ypgikvvmvi
      121 dgnseddlym mdifsevmgr dksatyiwkn nfhekgpget deshkessqh vtqlvlsnks
      181 icimqkwggk revmytafra lgrsvdyvqv cdsdtmldpa ssvemvkvle edpmvggvgg
      241 dvqilnkyds wisflssvry wmafnierac qsyfgcvqci sgplgmyrns llhefvedwy
      301 nqefmgnqcs fgddrhltnr vlslgyatky tarskcltet pieylrwlnq qtrwsksyfr
      361 ewlynamwfh khhlwmtyea iitgffpffl iatviqlfyr gkiwnillfl ltvqlvglik
      421 ssfasclrgn ivmvfmslys vlymssllpa kmfaiatink agwgtsgrkt ivvnfiglip
      481 vsvwftillg gviftiykes krpfseskqt vlivgtllya cywvmlltly vvlinkcgrr
      541 kkgqqydmvl dv
//
LOCUS       NP_001348935              88 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 1 [Mus musculus].
ACCESSION   NP_001348935
VERSION     NP_001348935.1
DBSOURCE    REFSEQ: accession NM_001362006.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 88)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 88)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 88)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 88)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7.
            
            Transcript Variant: This variant (16), as well as variants 1, 8-15,
            and 17-19, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.244859.1,
                                           SRR7345562.4855432.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..88
                     /product="cAMP-regulated phosphoprotein 21 isoform 1"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=9408
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q7M2N1; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10854908,
                     ECO:0000269|PubMed:15499021; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     CDS             1..88
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362006.1:540..806"
                     /note="isoform 1 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS40786.1"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqtl
//
LOCUS       NP_001346881             819 aa            linear   ROD 27-APR-2025
DEFINITION  splicing factor, suppressor of white-apricot homolog isoform 2 [Mus
            musculus].
ACCESSION   NP_001346881 XP_006504367
VERSION     NP_001346881.1
DBSOURCE    REFSEQ: accession NM_001359952.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Crisci,A., Raleff,F., Bagdiul,I., Raabe,M., Urlaub,H., Rain,J.C.
            and Kramer,A.
  TITLE     Mammalian splicing factor SF1 interacts with SURP domains of U2
            snRNP-associated proteins
  JOURNAL   Nucleic Acids Res 43 (21), 10456-10473 (2015)
   PUBMED   26420826
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Roberts,J.M., Ennajdaoui,H., Edmondson,C., Wirth,B., Sanford,J.R.
            and Chen,B.
  TITLE     Splicing factor TRA2B is required for neural progenitor survival
  JOURNAL   J Comp Neurol 522 (2), 372-392 (2014)
   PUBMED   23818142
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Moayedi,Y., Basch,M.L., Pacheco,N.L., Gao,S.S., Wang,R.,
            Harrison,W., Xiao,N., Oghalai,J.S., Overbeek,P.A., Mardon,G. and
            Groves,A.K.
  TITLE     The candidate splicing factor Sfswap regulates growth and
            patterning of inner ear sensory organs
  JOURNAL   PLoS Genet 10 (1), e1004055 (2014)
   PUBMED   24391519
  REMARK    GeneRIF: We show that Jag1; Sfswap compound mutants have inner ear
            defects that are more severe than expected from simple additive
            effects of the single mutants, indicating a genetic interaction
            between Sfswap and Jag1
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Manley,J.L. and Krainer,A.R.
  TITLE     A rational nomenclature for serine/arginine-rich protein splicing
            factors (SR proteins)
  JOURNAL   Genes Dev 24 (11), 1073-1074 (2010)
   PUBMED   20516191
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Cobellis,G., Nicolaus,G., Iovino,M., Romito,A., Marra,E.,
            Barbarisi,M., Sardiello,M., Di Giorgio,F.P., Iovino,N., Zollo,M.,
            Ballabio,A. and Cortese,R.
  TITLE     Tagging genes with cassette-exchange sites
  JOURNAL   Nucleic Acids Res 33 (4), e44 (2005)
   PUBMED   15741177
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Sarkissian,M., Winne,A. and Lafyatis,R.
  TITLE     The mammalian homolog of suppressor-of-white-apricot regulates
            alternative mRNA splicing of CD45 exon 4 and fibronectin IIICS
  JOURNAL   J Biol Chem 271 (49), 31106-31114 (1996)
   PUBMED   8940107
REFERENCE   9  (residues 1 to 819)
  AUTHORS   Denhez,F. and Lafyatis,R.
  TITLE     Conservation of regulated alternative splicing and identification
            of functional domains in vertebrate homologs to the Drosophila
            splicing regulator, suppressor-of-white-apricot
  JOURNAL   J Biol Chem 269 (23), 16170-16179 (1994)
   PUBMED   8206918
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Ayane,M., Preuss,U., Kohler,G. and Nielsen,P.J.
  TITLE     A differentially expressed murine RNA encoding a protein with
            similarities to two types of nucleic acid binding motifs
  JOURNAL   Nucleic Acids Res 19 (6), 1273-1278 (1991)
   PUBMED   2030943
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114614.9 and AC114657.9.
            
            On Jan 20, 2018 this sequence version replaced XP_006504367.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6116558.7331.1,
                                           SRR10662774.2505890.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 68.13 cM"
     Protein         1..819
                     /product="splicing factor, suppressor of white-apricot
                     homolog isoform 2"
                     /note="splicing factor, arginine/serine-rich 8;
                     serine/arginine-rich splicing factor 8; suppressor of
                     white apricot protein homolog; splicing factor, suppressor
                     of white-apricot homolog"
                     /calculated_mol_wt=90023
     Region          83..136
                     /region_name="SWAP"
                     /note="Suppressor-of-White-APricot splicing regulator;
                     smart00648"
                     /db_xref="CDD:197818"
     Region          334..381
                     /region_name="SWAP"
                     /note="Suppressor-of-White-APricot splicing regulator;
                     smart00648"
                     /db_xref="CDD:197818"
     CDS             1..819
                     /gene="Sfswap"
                     /gene_synonym="1190005N23Rik; 6330437E22Rik; Sfrs8; Srsf8;
                     SWAP"
                     /coded_by="NM_001359952.1:480..2939"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:231769"
                     /db_xref="MGI:MGI:101760"
ORIGIN      
        1 mkreeeykrl sealaedgny savgftygsd yydpseptee eepskqrekn eaenleenee
       61 pfiaplglsv psdvelppta kmhaiierta nfvckqgaqf eimlkakqar nsqfdflrfd
      121 hylnpyykfi qkamkegryt vlaeskneek kksgptsdne eeddeedgsy lhpslfaskk
      181 ssrleelmkp lkvvdpdhpl aalvrkaqad ssapapptad gtpaqpsqve ytadstvaam
      241 yysyymlpdg tyclappppg idvatyystl pagvtvsssp gvtttvpppp gttppppptt
      301 aepssgvtst ttttsalapv aiippppdiq pvidklaeyv arnglkfets vrakndqrfe
      361 flqpwhqyna yyefkkqffl qkegggstqa astaeeapte taveesgeag edgapegmae
      421 tggrgsgkke agsskstvdg klvkasfapi sfaikakend llpleknrvk ldddseedee
      481 srecqestss vanpspaaap psvaveekkp qltqeeleak qakqkledrl aaaareklaq
      541 askeskekql qaerkrkaal flqtlknplp eaevgklees tfgvedtgvm pcpllvggrt
      601 lpilegkppe rpsnrcrdpp reeerekkkk khkkrsrtrs rspkyhsssk prsrshskak
      661 hslpsayrtv rrsrsrsrsp rrrahsperr reersvptay rmsgspgvsr krtrsrsphe
      721 kkkkrrsrsr tkakarsqst spskqaaqrp sahsahsasi spvesrgssq ersrgvsqek
      781 dgqissaivs svqskitqdl makvramlaa sknlqtsas
//
LOCUS       NP_036463                235 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial peptide methionine sulfoxide reductase isoform a
            precursor [Homo sapiens].
ACCESSION   NP_036463
VERSION     NP_036463.1
DBSOURCE    REFSEQ: accession NM_012331.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Milovanovic,V., Topic,A., Milinkovic,N., Lazic,Z., Ivosevic,A.,
            Radojkovic,D. and Rankov,A.D.
  TITLE     Association of the methionine sulfoxide reductase A rs10903323 gene
            polymorphism with functional activity and oxidative modification of
            alpha-1-antitrypsin in COPD patients
  JOURNAL   Pulmonology 30 (2), 122-129 (2024)
   PUBMED   34674978
  REMARK    GeneRIF: Association of the methionine sulfoxide reductase A
            rs10903323 gene polymorphism with functional activity and oxidative
            modification of alpha-1-antitrypsin in COPD patients.
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Kantorow,M., Hawse,J.R., Cowell,T.L., Benhamed,S., Pizarro,G.O.,
            Reddy,V.N. and Hejtmancik,J.F.
  TITLE     Methionine sulfoxide reductase A is important for lens cell
            viability and resistance to oxidative stress
  JOURNAL   Proc Natl Acad Sci U S A 101 (26), 9654-9659 (2004)
   PUBMED   15199188
  REMARK    GeneRIF: MsrA is present throughout the human lens, where it is
            likely to defend lens cells and their components against methionine
            oxidation
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Picot,C.R., Perichon,M., Cintrat,J.C., Friguet,B. and
            Petropoulos,I.
  TITLE     The peptide methionine sulfoxide reductases, MsrA and MsrB
            (hCBS-1), are downregulated during replicative senescence of human
            WI-38 fibroblasts
  JOURNAL   FEBS Lett 558 (1-3), 74-78 (2004)
   PUBMED   14759519
  REMARK    GeneRIF: MSRA is down-regulated during cell aging.
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Vougier,S., Mary,J. and Friguet,B.
  TITLE     Subcellular localization of methionine sulphoxide reductase A
            (MsrA): evidence for mitochondrial and cytosolic isoforms in rat
            liver cells
  JOURNAL   Biochem J 373 (Pt 2), 531-537 (2003)
   PUBMED   12693988
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Hansel,A., Kuschel,L., Hehl,S., Lemke,C., Agricola,H.J., Hoshi,T.
            and Heinemann,S.H.
  TITLE     Mitochondrial targeting of the human peptide methionine sulfoxide
            reductase (MSRA), an enzyme involved in the repair of oxidized
            proteins
  JOURNAL   FASEB J 16 (8), 911-913 (2002)
   PUBMED   12039877
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Kuschel,L., Hansel,A., Schonherr,R., Weissbach,H., Brot,N.,
            Hoshi,T. and Heinemann,S.H.
  TITLE     Molecular cloning and functional expression of a human peptide
            methionine sulfoxide reductase (hMsrA)
  JOURNAL   FEBS Lett 456 (1), 17-21 (1999)
   PUBMED   10452521
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Moskovitz,J., Jenkins,N.A., Gilbert,D.J., Copeland,N.G., Jursky,F.,
            Weissbach,H. and Brot,N.
  TITLE     Chromosomal localization of the mammalian peptide-methionine
            sulfoxide reductase gene and its differential expression in various
            tissues
  JOURNAL   Proc Natl Acad Sci U S A 93 (8), 3205-3208 (1996)
   PUBMED   8622914
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC034111.6, AC023385.10,
            AC079200.6 and AC112673.7.
            
            Summary: This gene encodes a ubiquitous and highly conserved
            protein that carries out the enzymatic reduction of methionine
            sulfoxide to methionine. Human and animal studies have shown the
            highest levels of expression in kidney and nervous tissue. The
            protein functions in the repair of oxidatively damaged proteins to
            restore biological activity. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY958429.1, BC054033.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317173.9/ ENSP00000313921.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..235
                     /product="mitochondrial peptide methionine sulfoxide
                     reductase isoform a precursor"
                     /EC_number="1.8.4.11"
                     /note="peptide met (O) reductase; mitochondrial peptide
                     methionine sulfoxide reductase; cytosolic
                     methionine-S-sulfoxide reductase; peptide Met(O)
                     reductase; peptide-methionine (S)-S-oxide reductase"
                     /calculated_mol_wt=23496
     transit_peptide 1..23
                     /note="Mitochondrion; propagated from UniProtKB/Swiss-Prot
                     (Q9UJ68.1)"
                     /calculated_mol_wt=2654
     mat_peptide     24..235
                     /product="Mitochondrial peptide methionine sulfoxide
                     reductase. /id=PRO_0000138626"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJ68.1)"
                     /calculated_mol_wt=23496
     Region          62..231
                     /region_name="MsrA"
                     /note="Peptide methionine sulfoxide reductase MsrA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0225"
                     /db_xref="CDD:439995"
     Site            106
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9D6Y7; propagated from
                     UniProtKB/Swiss-Prot (Q9UJ68.1)"
     CDS             1..235
                     /gene="MSRA"
                     /gene_synonym="PMSR"
                     /coded_by="NM_012331.5:226..933"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS5975.1"
                     /db_xref="GeneID:4482"
                     /db_xref="HGNC:HGNC:7377"
                     /db_xref="MIM:601250"
ORIGIN      
        1 mlsatrracq llllhslfpv prmgnsasni vspqealpgr keqtpvaakh hvngnrtvep
       61 fpegtqmavf gmgcfwgaer kfwvlkgvys tqvgfaggyt snptykevcs ektghaevvr
      121 vvyqpehmsf eellkvfwen hdptqgmrqg ndhgtqyrsa iyptsakqme aalsskenyq
      181 kvlsehgfgp ittdiregqt fyyaedyhqq ylsknpngyc glggtgvscp vgikk
//
LOCUS       NP_001355322             299 aa            linear   ROD 27-APR-2025
DEFINITION  NAD-capped RNA hydrolase NUDT12 isoform 2 [Mus musculus].
ACCESSION   NP_001355322 XP_006524898
VERSION     NP_001355322.1
DBSOURCE    REFSEQ: accession NM_001368393.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Sharma,S., Grudzien-Nogalska,E., Hamilton,K., Jiao,X., Yang,J.,
            Tong,L. and Kiledjian,M.
  TITLE     Mammalian Nudix proteins cleave nucleotide metabolite caps on RNAs
  JOURNAL   Nucleic Acids Res 48 (12), 6788-6798 (2020)
   PUBMED   32432673
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Wu,H., Li,L., Chen,K.M., Homolka,D., Gos,P., Fleury-Olela,F.,
            McCarthy,A.A. and Pillai,R.S.
  TITLE     Decapping Enzyme NUDT12 Partners with BLMH for Cytoplasmic
            Surveillance of NAD-Capped RNAs
  JOURNAL   Cell Rep 29 (13), 4422-4434 (2019)
   PUBMED   31875550
  REMARK    GeneRIF: Decapping Enzyme NUDT12 Partners with BLMH for Cytoplasmic
            Surveillance of NAD-Capped RNAs.
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Grudzien-Nogalska,E., Wu,Y., Jiao,X., Cui,H., Mateyak,M.K.,
            Hart,R.P., Tong,L. and Kiledjian,M.
  TITLE     Structural and mechanistic basis of mammalian Nudt12 RNA deNADding
  JOURNAL   Nat Chem Biol 15 (6), 575-582 (2019)
   PUBMED   31101919
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Abdelraheim,S.R., Spiller,D.G. and McLennan,A.G.
  TITLE     Mammalian NADH diphosphatases of the Nudix family: cloning and
            characterization of the human peroxisomal NUDT12 protein
  JOURNAL   Biochem J 374 (Pt 2), 329-335 (2003)
   PUBMED   12790796
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CT009564.11.
            
            On Feb 9, 2019 this sequence version replaced XP_006524898.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR17253012.2043508.1,
                                           SRR17784647.476801.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164133
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 30.64 cM"
     Protein         1..299
                     /product="NAD-capped RNA hydrolase NUDT12 isoform 2"
                     /EC_number="3.6.1.22"
                     /note="peroxisomal NADH pyrophosphatase NUDT12; nudix
                     (nucleoside diphosphnudix (nucleoside diphosphate linked
                     moiety X)-type motif 12ate linked moiety X)-type motif 12;
                     nudix motif 12; nucleoside diphosphate-linked moiety X
                     motif 12; deNADding enzyme NUDT12; NAD-capped RNA
                     hydrolase NUDT12; nudix (nucleoside diphosphate linked
                     moiety X)-type motif 12"
                     /calculated_mol_wt=32933
     Region          11..40
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DCN1.1)"
     Region          14..43
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(17..18,21..23,25..26,30,33,43,45,47,51..52,55..57,
                     59..60,64,67,76,78,80,84..85,88..90,92..93,97)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          38..294
                     /region_name="NPY1"
                     /note="NADH pyrophosphatase NudC, Nudix superfamily
                     [Nucleotide transport and metabolism]; COG2816"
                     /db_xref="CDD:442065"
     Region          45..76
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          45..74
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DCN1.1)"
     Region          78..98
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DCN1.1)"
     CDS             1..299
                     /gene="Nudt12"
                     /gene_synonym="0610016O18Rik"
                     /coded_by="NM_001368393.1:112..1011"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:67993"
                     /db_xref="MGI:MGI:1915243"
ORIGIN      
        1 mssvkrnpkk emiselhssa aegnvaklag ilshspslln etsengwtal myaarnghpd
       61 vvqfllekgc drslvnkarq taldiaafwg yrhianllan akgvvaqars vlawhsrykf
      121 cptcgsatki eeggykrvcv retcpslqgv hntsyprvdp vvimqvihpd gtkcllgrqk
      181 rfppgmftcl agfiepgeti edavrrevee esgvkvghvq yvscqpwpmp sslmigclav
      241 avsteikvdk neiedarwft reqvvdvltk gkqqaffvpp sraiahqlik hwvgmnpnl
//
LOCUS       NP_631918                672 aa            linear   PRI 27-APR-2025
DEFINITION  diacylglycerol lipase-beta isoform 1 [Homo sapiens].
ACCESSION   NP_631918
VERSION     NP_631918.3
DBSOURCE    REFSEQ: accession NM_139179.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Shin,M., Ware,T.B. and Hsu,K.L.
  TITLE     DAGL-Beta Functions as a PUFA-Specific Triacylglycerol Lipase in
            Macrophages
  JOURNAL   Cell Chem Biol 27 (3), 314-321 (2020)
   PUBMED   31991095
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Zhou,D., Zhang,D., Sun,X., Li,Z., Ni,Y., Shan,Z., Li,H., Liu,C.,
            Zhang,S., Liu,Y., Zheng,R., Pan,F., Zhu,Y., Shi,Y. and Lai,M.
  TITLE     A novel variant associated with HDL-C levels by modifying DAGLB
            expression levels: An annotation-based genome-wide association
            study
  JOURNAL   Eur J Hum Genet 26 (6), 838-847 (2018)
   PUBMED   29476167
  REMARK    GeneRIF: we identified a novel HDL-C-associated variant which
            explained nearly half of the expression variance of DAGLB.
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Singh,P.K., Markwick,R., Lu,L., Howell,F.V., Williams,G. and
            Doherty,P.
  TITLE     Assay and Inhibition of the Purified Catalytic Domain of
            Diacylglycerol Lipase Beta
  JOURNAL   Biochemistry 55 (19), 2713-2721 (2016)
   PUBMED   27115711
  REMARK    GeneRIF: The purified DAGLbeta catalytic domain assay described
            here provides the basis for a relatively clean and convenient assay
            with the potential to be adapted for high-throughput drug discovery
            efforts.
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   6  (residues 1 to 672)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   7  (residues 1 to 672)
  AUTHORS   Ma,J., Dempsey,A.A., Stamatiou,D., Marshall,K.W. and Liew,C.C.
  TITLE     Identifying leukocyte gene expression patterns associated with
            plasma lipid levels in human subjects
  JOURNAL   Atherosclerosis 191 (1), 63-72 (2007)
   PUBMED   16806233
REFERENCE   8  (residues 1 to 672)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   9  (residues 1 to 672)
  AUTHORS   Bisogno,T., Howell,F., Williams,G., Minassi,A., Cascio,M.G.,
            Ligresti,A., Matias,I., Schiano-Moriello,A., Paul,P.,
            Williams,E.J., Gangadharan,U., Hobbs,C., Di Marzo,V. and Doherty,P.
  TITLE     Cloning of the first sn1-DAG lipases points to the spatial and
            temporal regulation of endocannabinoid signaling in the brain
  JOURNAL   J Cell Biol 163 (3), 463-468 (2003)
   PUBMED   14610053
  REMARK    GeneRIF: This gene has been functionally characterized as a
            diacylglycerol-lipase (DAGL), referred to as DAGL beta.  These
            enzymes may have a role in the biosynthesis of the endocannabinoid
            2-arachidnoyl glycerol (2-AG).
REFERENCE   10 (residues 1 to 672)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC304654.1, AK075128.1 and F17444.2.
            
            On Dec 30, 2008 this sequence version replaced NP_631918.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF450090.1, SRR1803613.277166.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297056.11/ ENSP00000297056.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..672
                     /product="diacylglycerol lipase-beta isoform 1"
                     /EC_number="3.1.1.3"
                     /EC_number="3.1.1.116"
                     /note="sn1-specific diacylglycerol lipase beta; DGL-beta;
                     DAGL-beta; PUFA-specific triacylglycerol lipase"
                     /calculated_mol_wt=73601
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCG7.2)"
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCG7.2)"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCG7.2)"
     Site            133..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCG7.2)"
     Region          274..507
                     /region_name="Lipase_3"
                     /note="Lipase (class 3). Lipases are esterases that can
                     hydrolyze long-chain acyl-triglycerides into di- and
                     monoglycerides, glycerol, and free fatty acids at a
                     water/lipid interface. A typical feature of lipases is
                     'interfacial activation,' the process of...; cd00519"
                     /db_xref="CDD:238287"
     Site            order(376..377,379..387)
                     /site_type="active"
                     /note="active site flap/lid [active]"
                     /db_xref="CDD:238287"
     Site            441..445
                     /site_type="active"
                     /note="nucleophilic elbow [active]"
                     /db_xref="CDD:238287"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q8NCG7.2)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NCG7.2)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NCG7.2)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WC9; propagated from
                     UniProtKB/Swiss-Prot (Q8NCG7.2)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NCG7.2)"
     CDS             1..672
                     /gene="DAGLB"
                     /gene_synonym="DAGLBETA; KCCR13L"
                     /coded_by="NM_139179.4:113..2131"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5350.1"
                     /db_xref="GeneID:221955"
                     /db_xref="HGNC:HGNC:28923"
                     /db_xref="MIM:614016"
ORIGIN      
        1 mpgmvlfgrr waiasddlvf pgffelvvrv lwwigiltly lmhrgkldca ggallssyli
       61 vlmillavvi ctvsaimcvs mrgticnpgp rksmskllyi rlalffpemv waslgaawva
      121 dgvqcdrtvv ngiiatvvvs wiiiaatvvs iiivfdplgg kmapyssagp shldshdssq
      181 llnglktaat svwetrikll cccigkddht rvafsstael fstyfsdtdl vpsdiaagla
      241 llhqqqdnir nnqepaqvvc hapgssqead ldaelenchh ymqfaaaayg wplyiyrnpl
      301 tglcriggdc crsrttdydl vggdqlnchf gsilhttglq yrdfihvsfh dkvyelpflv
      361 aldhrkesvv vavrgtmslq dvltdlsaes evldvecevq drlahkgisq aaryvyqrli
      421 ndgilsqafs iapeyrlviv ghslgggaaa llatmlraay pqvrcyafsp prglwskalq
      481 eysqsfivsl vlgkdviprl svtnledlkr rilrvvahcn kpkykillhg lwyelfggnp
      541 nnlpteldgg dqevltqpll geqslltrws paysfssdsp ldsspkyppl yppgriihlq
      601 eegasgrfgc csaahysakw sheaefskil igpkmltdhm pdilmralds vvsdraacvs
      661 cpaqgvssvd va
//
LOCUS       NP_066938               1024 aa            linear   PRI 27-APR-2025
DEFINITION  seizure 6-like protein isoform 1 precursor [Homo sapiens].
ACCESSION   NP_066938
VERSION     NP_066938.2
DBSOURCE    REFSEQ: accession NM_021115.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Chapman,N.H., Nato,A.Q. Jr., Bernier,R., Ankenman,K., Sohi,H.,
            Munson,J., Patowary,A., Archer,M., Blue,E.M., Webb,S.J., Coon,H.,
            Raskind,W.H., Brkanac,Z. and Wijsman,E.M.
  TITLE     Whole exome sequencing in extended families with autism spectrum
            disorder implicates four candidate genes
  JOURNAL   Hum Genet 134 (10), 1055-1068 (2015)
   PUBMED   26204995
  REMARK    GeneRIF: SEZ6L, HISPPD1, FEZF1, SAMD11 gene variants may be
            associated with autism spectrum disorder.
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Xu,C., Mullersman,J.E., Wang,L., Bin Su,B., Mao,C., Posada,Y.,
            Camarillo,C., Mao,Y., Escamilla,M.A. and Wang,K.S.
  TITLE     Polymorphisms in seizure 6-like gene are associated with bipolar
            disorder I: evidence of gene x gender interaction
  JOURNAL   J Affect Disord 145 (1), 95-99 (2013)
   PUBMED   22920719
  REMARK    GeneRIF: This is the first demonstration that genetic variants in
            the SEZ6L gene are associated with bipolar disorder Iin female
            patients and provides additional compelling evidence for genetic
            variation at 22q11-13 that influences BD-I risk.
REFERENCE   4  (residues 1 to 1024)
  AUTHORS   Wilk,J.B., Shrine,N.R., Loehr,L.R., Zhao,J.H., Manichaikul,A.,
            Lopez,L.M., Smith,A.V., Heckbert,S.R., Smolonska,J., Tang,W.,
            Loth,D.W., Curjuric,I., Hui,J., Cho,M.H., Latourelle,J.C.,
            Henry,A.P., Aldrich,M., Bakke,P., Beaty,T.H., Bentley,A.R.,
            Borecki,I.B., Brusselle,G.G., Burkart,K.M., Chen,T.H., Couper,D.,
            Crapo,J.D., Davies,G., Dupuis,J., Franceschini,N., Gulsvik,A.,
            Hancock,D.B., Harris,T.B., Hofman,A., Imboden,M., James,A.L.,
            Khaw,K.T., Lahousse,L., Launer,L.J., Litonjua,A., Liu,Y.,
            Lohman,K.K., Lomas,D.A., Lumley,T., Marciante,K.D., McArdle,W.L.,
            Meibohm,B., Morrison,A.C., Musk,A.W., Myers,R.H., North,K.E.,
            Postma,D.S., Psaty,B.M., Rich,S.S., Rivadeneira,F., Rochat,T.,
            Rotter,J.I., Soler Artigas,M., Starr,J.M., Uitterlinden,A.G.,
            Wareham,N.J., Wijmenga,C., Zanen,P., Province,M.A., Silverman,E.K.,
            Deary,I.J., Palmer,L.J., Cassano,P.A., Gudnason,V., Barr,R.G.,
            Loos,R.J., Strachan,D.P., London,S.J., Boezen,H.M.,
            Probst-Hensch,N., Gharib,S.A., Hall,I.P., O'Connor,G.T., Tobin,M.D.
            and Stricker,B.H.
  TITLE     Genome-wide association studies identify CHRNA5/3 and HTR4 in the
            development of airflow obstruction
  JOURNAL   Am J Respir Crit Care Med 186 (7), 622-632 (2012)
   PUBMED   22837378
REFERENCE   5  (residues 1 to 1024)
  AUTHORS   Irvin,M.R., Wineinger,N.E., Rice,T.K., Pajewski,N.M.,
            Kabagambe,E.K., Gu,C.C., Pankow,J., North,K.E., Wilk,J.B.,
            Freedman,B.I., Franceschini,N., Broeckel,U., Tiwari,H.K. and
            Arnett,D.K.
  TITLE     Genome-wide detection of allele specific copy number variation
            associated with insulin resistance in African Americans from the
            HyperGEN study
  JOURNAL   PLoS One 6 (8), e24052 (2011)
   PUBMED   21901158
REFERENCE   6  (residues 1 to 1024)
  AUTHORS   Raji,O.Y., Agbaje,O.F., Duffy,S.W., Cassidy,A. and Field,J.K.
  TITLE     Incorporation of a genetic factor into an epidemiologic model for
            prediction of individual risk of lung cancer: the Liverpool Lung
            Project
  JOURNAL   Cancer Prev Res (Phila) 3 (5), 664-669 (2010)
   PUBMED   20424129
  REMARK    GeneRIF: the addition of SEZ6L improved the performance of the
            Liverpool Lung Project risk model.
            GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 1024)
  AUTHORS   Gorlov,I.P., Meyer,P., Liloglou,T., Myles,J., Boettger,M.B.,
            Cassidy,A., Girard,L., Minna,J.D., Fischer,R., Duffy,S.,
            Spitz,M.R., Haeussinger,K., Kammerer,S., Cantor,C., Dierkesmann,R.,
            Field,J.K. and Amos,C.I.
  TITLE     Seizure 6-like (SEZ6L) gene and risk for lung cancer
  JOURNAL   Cancer Res 67 (17), 8406-8411 (2007)
   PUBMED   17804757
  REMARK    GeneRIF: A role of the SEZ6L Met430Ile polymorphic variant in
            increasing lung cancer risk.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1024)
  AUTHORS   Nishioka,M., Kohno,T., Takahashi,M., Niki,T., Yamada,T., Sone,S.
            and Yokota,J.
  TITLE     Identification of a 428-kb homozygously deleted region disrupting
            the SEZ6L gene at 22q12.1 in a lung cancer cell line
  JOURNAL   Oncogene 19 (54), 6251-6260 (2000)
   PUBMED   11175339
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL022337.19, AY358405.1, AB041736.1 and AL078460.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 26, 2003 this sequence version replaced NP_066938.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and it encodes the longest protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.158973.1,
                                           SRR1803614.135029.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248933.11/ ENSP00000248933.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.1"
     Protein         1..1024
                     /product="seizure 6-like protein isoform 1 precursor"
                     /note="seizure related gene 6-like; seizure 6-like
                     protein"
                     /calculated_mol_wt=109097
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2703
     Region          <6..239
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     mat_peptide     29..1024
                     /product="Seizure 6-like protein. /id=PRO_0000022323"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYH1.1)"
                     /calculated_mol_wt=109097
     Region          33..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Site            49
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:23234360; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Region          108..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Region          147..161
                     /region_name="O-glycosylated at one site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Region          176..180
                     /region_name="O-glycosylated at one site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Region          212..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Region          281..388
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(289,291,293,321,326,359,383,385,387..388)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Site            311
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Site            328
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Site            350
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Region          393..448
                     /region_name="CCP"
                     /note="Domain abundant in complement control proteins;
                     SUSHI repeat; short complement-like repeat (SCR);
                     smart00032"
                     /db_xref="CDD:214478"
     Site            order(403,420)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Site            435
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Region          452..561
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            458
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Site            order(461,463,465,492,497,531,556,558,560..561)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Site            474
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Site            514
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Region          567..624
                     /region_name="Sushi"
                     /note="Sushi repeat (SCR repeat); pfam00084"
                     /db_xref="CDD:459664"
     Site            576
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Site            618
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Region          628..736
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(636,638,640,667,672,705,733,735)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Site            674
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Site            742
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYH1.1)"
     Region          <745..930
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Site            959..979
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYH1.1)"
     CDS             1..1024
                     /gene="SEZ6L"
                     /gene_synonym="SEZ6L1"
                     /coded_by="NM_021115.5:209..3283"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS13833.1"
                     /db_xref="GeneID:23544"
                     /db_xref="HGNC:HGNC:10763"
                     /db_xref="MIM:607021"
ORIGIN      
        1 mpaarppaag lrgislflal llgspaaale rdalpegdas plgpyllpsg apergspgke
       61 hpeervvtap psssqsaevl gelvldgtap sahhdipals pllpeearpk halppkkklp
      121 slkqvnsark qlrpkatsaa tvqragsqpa sqgldllsss tekpgppgdp dpivaseeas
      181 evplwldrke savpttpapl qispftsqpy vahtlpqrpe pgepgpdmaq eapqedtspm
      241 almdkgenel tgsaseesqe tttstiittt vitteqapal csvsfsnpeg yidssdypll
      301 plnnflecty nvtvytgygv elqvksvnls dgellsirgv dgptltvlan qtllvegqvi
      361 rsptntisvy frtfqddglg tfqlhyqafm lscnfprrpd sgdvtvmdlh sggvahfhch
      421 lgyelqgakm ltcinaskph wssqepicsa pcggavhnat igrvlspsyp entngsqfci
      481 wtieapegqk lhlhferlll hdkdrmtvhs gqtnksally dslqtesvpf egllsegnti
      541 rieftsdqar aastfnirfe afekghcyep yiqngnftts dptynigtiv eftcdpghsl
      601 eqgpaiieci nvrdpywndt eplcramcgg elsavagvvl spnwpepyve gedciwkihv
      661 geekrifldi qflnlsnsdi ltiydgdevm philgqylgn sgpqklysst pdltiqfhsd
      721 paglifgkgq gfimnyievs rndscsdlpe iqngwkttsh telvrgarit yqcdpgydiv
      781 gsdtltcqwd lswssdppfc ekimyctdpg evdhstrlis dpvllvgtti qytcnpgfvl
      841 egsslltcys retgtpiwts rlphcvsees lacdnpglpe ngyqilykrl ylpgesltfm
      901 cyegfelmge vtircilgqp shwngplpvc kvnqdsfeha levaeaaaet sleggnmala
      961 ifipvliisl llggayiyit rcryysnlrl plmyshpysq itvetefdnp iyetgetrey
     1021 evsi
//
LOCUS       NP_808398                356 aa            linear   ROD 27-APR-2025
DEFINITION  Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase [Mus
            musculus].
ACCESSION   NP_808398
VERSION     NP_808398.1
DBSOURCE    REFSEQ: accession NM_177730.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Eisele,B.S., Wu,A.J., Luka,Z., Hale,A.T. and York,J.D.
  TITLE     Bisphosphate nucleotidase 2 (BPNT2), a molecular target of lithium,
            regulates chondroitin sulfation patterns in the cerebral cortex and
            hippocampus
  JOURNAL   Adv Biol Regul 83, 100858 (2022)
   PUBMED   34920982
  REMARK    GeneRIF: Bisphosphate nucleotidase 2 (BPNT2), a molecular target of
            lithium, regulates chondroitin sulfation patterns in the cerebral
            cortex and hippocampus.
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Eisele,B.S., Luka,Z., Wu,A.J., Yang,F., Hale,A.T. and York,J.D.
  TITLE     Sulfation of glycosaminoglycans depends on the catalytic activity
            of lithium-inhibited phosphatase BPNT2 in vitro
  JOURNAL   J Biol Chem 297 (5), 101293 (2021)
   PUBMED   34634304
  REMARK    GeneRIF: Sulfation of glycosaminoglycans depends on the catalytic
            activity of lithium-inhibited phosphatase BPNT2 in vitro.
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Capulli,M., Costantini,R., Sonntag,S., Maurizi,A., Paganini,C.,
            Monti,L., Forlino,A., Shmerling,D., Teti,A. and Rossi,A.
  TITLE     Testing the Cre-mediated genetic switch for the generation of
            conditional knock-in mice
  JOURNAL   PLoS One 14 (3), e0213660 (2019)
   PUBMED   30865697
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Hudson,B.H., Frederick,J.P., Drake,L.Y., Megosh,L.C., Irving,R.P.
            and York,J.D.
  TITLE     Role for cytoplasmic nucleotide hydrolysis in hepatic function and
            protein synthesis
  JOURNAL   Proc Natl Acad Sci U S A 110 (13), 5040-5045 (2013)
   PUBMED   23479625
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Frederick,J.P., Tafari,A.T., Wu,S.M., Megosh,L.C., Chiou,S.T.,
            Irving,R.P. and York,J.D.
  TITLE     A role for a lithium-inhibited Golgi nucleotidase in skeletal
            development and sulfation
  JOURNAL   Proc Natl Acad Sci U S A 105 (33), 11605-11612 (2008)
   PUBMED   18695242
  REMARK    GeneRIF: Golgi plays an important role in glycosaminoglycan
            sulfation and define a function for gPAPP in the formation of
            skeletal elements derived through endochondral
            ossification[3'-phosphoadenosine 5'-phosphate phosphatase]
REFERENCE   8  (residues 1 to 356)
  AUTHORS   McGowan,K.A., Li,J.Z., Park,C.Y., Beaudry,V., Tabor,H.K.,
            Sabnis,A.J., Zhang,W., Fuchs,H., de Angelis,M.H., Myers,R.M.,
            Attardi,L.D. and Barsh,G.S.
  TITLE     Ribosomal mutations cause p53-mediated dark skin and pleiotropic
            effects
  JOURNAL   Nat Genet 40 (8), 963-970 (2008)
   PUBMED   18641651
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Sohaskey,M.L., Yu,J., Diaz,M.A., Plaas,A.H. and Harland,R.M.
  TITLE     JAWS coordinates chondrogenesis and synovial joint positioning
  JOURNAL   Development 135 (13), 2215-2220 (2008)
   PUBMED   18539921
  REMARK    GeneRIF: identify JAWS as a key regulator of chondrogenesis and
            synovial joint positioning required for the restriction of joint
            formation to discrete stereotyped locations in the embryonic
            skeleton
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Alavizadeh,A., Kiernan,A.E., Nolan,P., Lo,C., Steel,K.P. and
            Bucan,M.
  TITLE     The Wheels mutation in the mouse causes vascular, hindbrain, and
            inner ear defects
  JOURNAL   Dev Biol 234 (1), 244-260 (2001)
   PUBMED   11356033
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL772346.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC048776.1, AK045511.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164140, SAMN01164142
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 2.56 cM"
     Protein         1..356
                     /product="Golgi-resident adenosine 3',5'-bisphosphate
                     3'-phosphatase"
                     /EC_number="3.1.3.7"
                     /note="inositol monophosphatase 3; myo-inositol
                     monophosphatase A3; inositol-1(or 4)-monophosphatase 3;
                     inositol monophosphatase domain containing 1; inositol
                     monophosphatase domain-containing protein 1;
                     golgi-resident PAP phosphatase; Golgi 3-prime
                     phosphoadenosine 5-prime phosphate 3-prime phosphatase;
                     phosphoadenosine phosphate 3'-nucleotidase"
                     /calculated_mol_wt=38485
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9NX62; propagated from
                     UniProtKB/Swiss-Prot (Q80V26.1)"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80V26.1)"
     Region          64..347
                     /region_name="IPPase"
                     /note="Inositol polyphosphate-1-phosphatase, a member of
                     the Mg++ dependent family of inositol monophosphatase-like
                     domains, hydrolyzes the 1' position phosphate from
                     inositol 1,3,4-trisphosphate and inositol
                     1,4-bisphosphate. Members in this group may also...;
                     cd01640"
                     /db_xref="CDD:238818"
     Region          84..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80V26.1)"
     Site            order(108,131..132,172..177,179,242,264..267,270,288,290,
                     293..294,297..298)
                     /site_type="active"
                     /db_xref="CDD:238818"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80V26.1)"
     CDS             1..356
                     /gene="Bpnt2"
                     /gene_synonym="1110001C20Rik; B230207P20; gPAPP; IMP 3;
                     Impad1; IMPase 3; Jaws"
                     /coded_by="NM_177730.4:204..1274"
                     /db_xref="CCDS:CCDS17947.1"
                     /db_xref="GeneID:242291"
                     /db_xref="MGI:MGI:1915720"
ORIGIN      
        1 mapmgirlsp lgvavffllg lgvlyhlysg flagrfslfg lgsepaagea evasdggtvd
       61 lremlavavl aaerggdevr rvresnvlhe kskgktrega ddkmtsgdvl snrkmfyllk
      121 tafpnvqint eehvdasdke vivwnrkipe dilkeiaapk evpaesvtvw idpldatqey
      181 tedlrkyvtt mvcvavngkp vlgvihkpfs eytawamvdg gsnvkarssy nektpkiivs
      241 rshagmvkqv alqtfgnqts iipaggagyk vlalldvpdm tqekadlyih vtyikkwdic
      301 agnailkalg ghmttlngee isytgsdgie ggllasirmn hqalvrklpd leksgh
//
LOCUS       NP_079124                497 aa            linear   PRI 27-APR-2025
DEFINITION  MORN repeat-containing protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_079124
VERSION     NP_079124.1
DBSOURCE    REFSEQ: accession NM_024848.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Xu,Z., Gu,Y., Chen,J., Chen,X., Song,Y., Fan,J., Ji,X., Li,Y.,
            Zhang,W. and Zhang,R.
  TITLE     Epigenome-wide gene-age interaction study reveals reversed effects
            of MORN1 DNA methylation on survival between young and elderly oral
            squamous cell carcinoma patients
  JOURNAL   Front Oncol 12, 941731 (2022)
   PUBMED   35965572
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK024003.1 and AI674190.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK024003.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378531.8/ ENSP00000367792.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.32"
     Protein         1..497
                     /product="MORN repeat-containing protein 1 isoform 1"
                     /note="MORN repeat-containing protein 1"
                     /calculated_mol_wt=53719
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T089.2)"
     Region          <5..207
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          39..61
                     /region_name="MORN 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T089.2)"
     Region          62..84
                     /region_name="MORN 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T089.2)"
     Region          86..108
                     /region_name="MORN 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T089.2)"
     Region          109..131
                     /region_name="MORN 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T089.2)"
     Region          132..154
                     /region_name="MORN 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T089.2)"
     Region          155..177
                     /region_name="MORN 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T089.2)"
     Region          178..200
                     /region_name="MORN 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T089.2)"
     Region          393..425
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T089.2)"
     Region          468..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T089.2)"
     CDS             1..497
                     /gene="MORN1"
                     /coded_by="NM_024848.3:22..1515"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS40.1"
                     /db_xref="GeneID:79906"
                     /db_xref="HGNC:HGNC:25852"
ORIGIN      
        1 maaagegtps srgprrdppr rpprngygvy vypnsffrye gewkagrkhg hgkllfkdgs
       61 yyegafvdge itgegrrhwa wsgdtfsgqf vlgepqgygv meykaggcye gevshgmreg
      121 hgflvdrdgq vyqgsfhdnk rhgpgqmlfq ngdkydgdwv rdrrqghgvl rcadgstykg
      181 qwhsdvfsgl gsmahcsgvt yyglwinghp aeqatrivil gpevmevaqg spfsvnvqll
      241 qdhgeiakse sgrvlqisag vryvqlsays evnffkvdrd nqetliqtpf gfecipypvs
      301 spaagvpgpr aakggaeadv plprgdlelh lgalhgqedt pggllargha phcpgacqrv
      361 eqgcaeftdv llgppppgyh pflfldslhk kaggrsrggl hprgtpptaq eppggsrpeg
      421 rateeqaaaa hlgeyvlmir dvttppflgr rlppafkhlr vvakragqpp hvleegpeas
      481 sswqaahsct peppapr
//
LOCUS       NP_037508                236 aa            linear   PRI 27-APR-2025
DEFINITION  SERTA domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_037508
VERSION     NP_037508.2
DBSOURCE    REFSEQ: accession NM_013376.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Ha,J., Kim,M., Park,J.S., Lee,Y., Lee,J.Y., Shin,J.C., Seo,D.,
            Park,S.S., You,J., Jung,S.M., Kim,H.Y., Mizuno,S., Takahashi,S.,
            Kim,S.J. and Park,S.H.
  TITLE     SERTAD1 initiates NLRP3-mediated inflammasome activation through
            restricting NLRP3 polyubiquitination
  JOURNAL   Cell Rep 43 (2), 113752 (2024)
   PUBMED   38341852
  REMARK    GeneRIF: SERTAD1 initiates NLRP3-mediated inflammasome activation
            through restricting NLRP3 polyubiquitination.
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Sandag,Z., Jung,S., Quynh,N.T.N., Myagmarjav,D., Anh,N.H., Le,D.T.,
            Lee,B.S., Mongre,R.K., Jo,T. and Lee,M.
  TITLE     Inhibitory Role of TRIP-Br1/XIAP in Necroptosis under
            Nutrient/Serum Starvation
  JOURNAL   Mol Cells 43 (3), 236-250 (2020)
   PUBMED   32050753
  REMARK    GeneRIF: Inhibitory Role of TRIP-Br1/XIAP in Necroptosis under
            Nutrient/Serum Starvation.
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Gupta,S., Takhar,P.P., Degenkolbe,R., Koh,C.H., Zimmermann,H.,
            Yang,C.M., Guan Sim,K., Hsu,S.I. and Bernard,H.U.
  TITLE     The human papillomavirus type 11 and 16 E6 proteins modulate the
            cell-cycle regulator and transcription cofactor TRIP-Br1
  JOURNAL   Virology 317 (1), 155-164 (2003)
   PUBMED   14675634
  REMARK    GeneRIF: interacts with low- and high-risk HPV11 and HPV16 E6
            proteins in yeast, in vitro and in mammalian cell cultures
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Hirose,T., Fujii,R., Nakamura,H., Aratani,S., Fujita,H.,
            Nakazawa,M., Nakamura,K., Nishioka,K. and Nakajima,T.
  TITLE     Regulation of CREB-mediated transcription by association of CDK4
            binding protein p34SEI-1 with CBP
  JOURNAL   Int J Mol Med 11 (6), 705-712 (2003)
   PUBMED   12736710
  REMARK    GeneRIF: p34SEI-1 strongly suppressed CREB-mediated transcription,
            and this suppression was overcome by excess amount of CBP
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Hsu,S.I., Yang,C.M., Sim,K.G., Hentschel,D.M., O'Leary,E. and
            Bonventre,J.V.
  TITLE     TRIP-Br: a novel family of PHD zinc finger- and
            bromodomain-interacting proteins that regulate the transcriptional
            activity of E2F-1/DP-1
  JOURNAL   EMBO J 20 (9), 2273-2285 (2001)
   PUBMED   11331592
REFERENCE   9  (residues 1 to 236)
  AUTHORS   Sugimoto,M., Nakamura,T., Ohtani,N., Hampson,L., Hampson,I.N.,
            Shimamoto,A., Furuichi,Y., Okumura,K., Niwa,S., Taya,Y. and Hara,E.
  TITLE     Regulation of CDK4 activity by a novel CDK4-binding protein,
            p34(SEI-1)
  JOURNAL   Genes Dev 13 (22), 3027-3033 (1999)
   PUBMED   10580009
REFERENCE   10 (residues 1 to 236)
  AUTHORS   Besley,G.T., Broadhead,D.M. and Lawlor,E.
  TITLE     Acid esterase deficiency: comparison of biochemical findings in
            infantile and adult forms
  JOURNAL   J Inherit Metab Dis 7 Suppl 2, 155-156 (1984)
   PUBMED   6434876
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK074652.1, AA928491.1 and AC010271.8.
            
            On Jul 25, 2007 this sequence version replaced NP_037508.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222970.1, AK074652.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357949.5/ ENSP00000350633.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..236
                     /product="SERTA domain-containing protein 1"
                     /note="transcriptional regulator interacting with the
                     PHD-bromodomain 1; CDK4-binding protein p34SEI;
                     CDK4-binding protein p34SEI1; SEI-1; p34(SEI-1)"
                     /calculated_mol_wt=24573
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHV2.2)"
     Region          45..79
                     /region_name="SERTA"
                     /note="SERTA motif; pfam06031"
                     /db_xref="CDD:461806"
     Region          189..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHV2.2)"
     CDS             1..236
                     /gene="SERTAD1"
                     /gene_synonym="SEI1; TRIP-Br1; TRIPBR1"
                     /coded_by="NM_013376.4:127..837"
                     /db_xref="CCDS:CCDS12557.1"
                     /db_xref="GeneID:29950"
                     /db_xref="HGNC:HGNC:17932"
                     /db_xref="MIM:617850"
ORIGIN      
        1 mlskglkrkr eeeeekepla vdswwldpgh tavaqappav assslfdlsv lklhhslqqs
       61 epdlrhlvlv vntlrriqas mapaaalppv psppaapsva dnllassdaa lsasmaslle
      121 dlshieglsq apqpladegp pgrsiggaap slgaldllgp atgcllddgl eglfedidts
      181 mydnelwapa seglkpgped gpgkeeapel deaeldylmd vlvgtqaler ppgpgr
//
LOCUS       NP_940845                165 aa            linear   PRI 27-APR-2025
DEFINITION  neuritin-like protein isoform 1 precursor [Homo sapiens].
ACCESSION   NP_940845 XP_058747
VERSION     NP_940845.1
DBSOURCE    REFSEQ: accession NM_198443.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 165)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Fujino,T., Wu,Z., Lin,W.C., Phillips,M.A. and Nedivi,E.
  TITLE     cpg15 and cpg15-2 constitute a family of activity-regulated ligands
            expressed differentially in the nervous system to promote neurite
            growth and neuronal survival
  JOURNAL   J Comp Neurol 507 (5), 1831-1845 (2008)
   PUBMED   18265009
  REMARK    GeneRIF: CPG15 and CPG15-2 perform similar cellular functions but
            may play distinct roles in vivo through their cell-type- and
            tissue-specific transcriptional regulation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY358782.1.
            
            On Dec 17, 2003 this sequence version replaced XP_058747.2.
            
            Summary: The protein encoded by this gene is extracellular and
            enhances both neurite growth and neuronal survival. The encoded
            protein is found both as a GPI anchored membrane-bound form and as
            a secreted form. This activity-related ligand functions as a
            homodimer or heterodimer. [provided by RefSeq, Feb 2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358782.1, BM676935.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000339176.8/ ENSP00000342411.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..165
                     /product="neuritin-like protein isoform 1 precursor"
                     /note="neuritin-like protein"
                     /calculated_mol_wt=13821
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3983
     mat_peptide     36..139
                     /product="Neuritin-like protein. /id=PRO_0000319429"
                     /note="propagated from UniProtKB/Swiss-Prot (Q496H8.2)"
                     /calculated_mol_wt=11243
     Region          42..117
                     /region_name="NRN1"
                     /note="Neuritin protein family; pfam15056"
                     /db_xref="CDD:434424"
     CDS             1..165
                     /gene="NRN1L"
                     /gene_synonym="cpg15-2; MRCC2446; UNQ2446"
                     /coded_by="NM_198443.2:20..517"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10850.1"
                     /db_xref="GeneID:123904"
                     /db_xref="HGNC:HGNC:29811"
ORIGIN      
        1 mmrccrrrcc crqpphalrp llllplvllp plaaaaagpn rcdtiyqgfa eclirlgdsm
       61 grggeletic rswndfhaca sqvlsgcpee aaavweslqq earqaprpnn lhtlcgapvh
      121 vrergtgset nqetlratap alpmapappl laaalalayl lrpla
//
LOCUS       NP_001349832             436 aa            linear   ROD 27-APR-2025
DEFINITION  protein artemis isoform 6 [Mus musculus].
ACCESSION   NP_001349832 XP_017172666
VERSION     NP_001349832.1
DBSOURCE    REFSEQ: accession NM_001362903.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Collins,P.L., Purman,C., Porter,S.I., Nganga,V., Saini,A.,
            Hayer,K.E., Gurewitz,G.L., Sleckman,B.P., Bednarski,J.J.,
            Bassing,C.H. and Oltz,E.M.
  TITLE     DNA double-strand breaks induce H2Ax phosphorylation domains in a
            contact-dependent manner
  JOURNAL   Nat Commun 11 (1), 3158 (2020)
   PUBMED   32572033
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Liu,X., Wang,X.S., Lee,B.J., Wu-Baer,F.K., Lin,X., Shao,Z.,
            Estes,V.M., Gautier,J., Baer,R. and Zha,S.
  TITLE     CtIP is essential for early B cell proliferation and development in
            mice
  JOURNAL   J Exp Med 216 (7), 1648-1663 (2019)
   PUBMED   31097467
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Spehalski,E., Capper,K.M., Smith,C.J., Morgan,M.J., Dinkelmann,M.,
            Buis,J., Sekiguchi,J.M. and Ferguson,D.O.
  TITLE     MRE11 Promotes Tumorigenesis by Facilitating Resistance to
            Oncogene-Induced Replication Stress
  JOURNAL   Cancer Res 77 (19), 5327-5338 (2017)
   PUBMED   28819025
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Jiang,W., Crowe,J.L., Liu,X., Nakajima,S., Wang,Y., Li,C.,
            Lee,B.J., Dubois,R.L., Liu,C., Yu,X., Lan,L. and Zha,S.
  TITLE     Differential phosphorylation of DNA-PKcs regulates the interplay
            between end-processing and end-ligation during nonhomologous
            end-joining
  JOURNAL   Mol Cell 58 (1), 172-185 (2015)
   PUBMED   25818648
  REMARK    GeneRIF: ATM phosphorylates DNA-PKcs to recruit Artemis and promote
            end-processing.
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Desai,A. and Gerson,S.
  TITLE     Exo1 independent DNA mismatch repair involves multiple compensatory
            nucleases
  JOURNAL   DNA Repair (Amst) 21, 55-64 (2014)
   PUBMED   25037770
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Yan,Y., Akhter,S., Zhang,X. and Legerski,R.
  TITLE     The multifunctional SNM1 gene family: not just nucleases
  JOURNAL   Future Oncol 6 (6), 1015-1029 (2010)
   PUBMED   20528238
  REMARK    Review article
REFERENCE   7  (residues 1 to 436)
  AUTHORS   Mills,K.D., Ferguson,D.O. and Alt,F.W.
  TITLE     The role of DNA breaks in genomic instability and tumorigenesis
  JOURNAL   Immunol Rev 194, 77-95 (2003)
   PUBMED   12846809
  REMARK    Review article
REFERENCE   8  (residues 1 to 436)
  AUTHORS   Rooney,S., Alt,F.W., Lombard,D., Whitlow,S., Eckersdorff,M.,
            Fleming,J., Fugmann,S., Ferguson,D.O., Schatz,D.G. and Sekiguchi,J.
  TITLE     Defective DNA repair and increased genomic instability in
            Artemis-deficient murine cells
  JOURNAL   J Exp Med 197 (5), 553-565 (2003)
   PUBMED   12615897
  REMARK    GeneRIF: Data show that Artemis appears to be required for a subset
            of nonhomologous DNA end joining reactions that require end
            processing [Artemis].
REFERENCE   9  (residues 1 to 436)
  AUTHORS   Rooney,S., Sekiguchi,J., Zhu,C., Cheng,H.L., Manis,J., Whitlow,S.,
            DeVido,J., Foy,D., Chaudhuri,J., Lombard,D. and Alt,F.W.
  TITLE     Leaky Scid phenotype associated with defective V(D)J coding end
            processing in Artemis-deficient mice
  JOURNAL   Mol Cell 10 (6), 1379-1390 (2002)
   PUBMED   12504013
  REMARK    GeneRIF: deficient mice have a phenotype similar to that of
            DNA-PKcs-deficient mice-including severe combined immunodeficiency
            associated with defects in opening and joining V(D)J coding hairpin
            ends and increased cellular ionizing radiation sensitivity
            (artemis)
REFERENCE   10 (residues 1 to 436)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL732620.14.
            
            On May 3, 2018 this sequence version replaced XP_017172666.1.
            
            Summary: This gene encodes a member of the SNM1 family of nucleases
            and is involved in V(D)J recombination and DNA repair. This protein
            has single-strand-specific 5'-3' exonuclease activity; it also
            exhibits endonuclease activity on 5' and 3' overhangs and hairpins.
            The protein also functions in the regulation of the cell cycle in
            response to DNA damage. Homozygous knockout mice for this gene
            exhibit severe combined immunodeficiency with sensitivity to
            ionizing radiation. Mutations in this gene in humans can cause
            Athabascan-type severe combined immunodeficiency (SCIDA) and Omenn
            syndrome. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Nov
            2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.46032.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849382, SAMN00849383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            multifunctional gene product(s) :: PMID: 20528238
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 1.93 cM"
     Protein         1..436
                     /product="protein artemis isoform 6"
                     /note="protein artemis; SNM1-like protein; DNA cross-link
                     repair 1C protein; DNA cross-link repair 1A, PSO2 homolog;
                     DNA cross-link repair 1C, PSO2 homolog"
                     /calculated_mol_wt=49884
     Region          <5..56
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
     Region          124..230
                     /region_name="DRMBL"
                     /note="DNA repair metallo-beta-lactamase; pfam07522"
                     /db_xref="CDD:429512"
     CDS             1..436
                     /gene="Dclre1c"
                     /gene_synonym="9930121L06Rik; Art; Snm1l"
                     /coded_by="NM_001362903.1:377..1687"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:227525"
                     /db_xref="MGI:MGI:2441769"
ORIGIN      
        1 mrlrvrflfq gsngtvlytg dfrlakgeas rmellhsggr vkdiqsvyld ttfcdprfyq
       61 ipsreqclrg ilelvrswvt rsphhvvwln ckaaygyeyl ftnlseelgv qvhvdkldmf
      121 knmpdilhhl ttdrntqiha crhpkaeecf qwnklpcgit sqnktalhti sikpstmwfg
      181 ertrktnviv rtgessyrac fsfhssfsei kdflsyicpv nvypnvipvg ltvdkvmdvl
      241 kplcrspqsv epkykplgkl krartihlds eedddlfddp lptplrhkvp yqltlqpelf
      301 smkalpldqp elrqspggck aesvwspsla nfidceesns dsgeeletpp pslqgglgps
      361 tlvqqnadpd vdipqwevff krrdeitvdt mirtprprkm kgcgqwslkm llqnleiqee
      421 khifenrgwk magqdi
//
LOCUS       NP_112581                315 aa            linear   PRI 27-APR-2025
DEFINITION  ADP/ATP translocase 4 isoform 1 [Homo sapiens].
ACCESSION   NP_112581
VERSION     NP_112581.1
DBSOURCE    REFSEQ: accession NM_031291.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Trisolini,L., Laera,L., Favia,M., Muscella,A., Castegna,A.,
            Pesce,V., Guerra,L., De Grassi,A., Volpicella,M. and Pierri,C.L.
  TITLE     Differential Expression of ADP/ATP Carriers as a Biomarker of
            Metabolic Remodeling and Survival in Kidney Cancers
  JOURNAL   Biomolecules 11 (1), 38 (2020)
   PUBMED   33396658
  REMARK    GeneRIF: Differential Expression of ADP/ATP Carriers as a Biomarker
            of Metabolic Remodeling and Survival in Kidney Cancers.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Marginedas-Freixa,I., Hattab,C., Bouyer,G., Halle,F., Chene,A.,
            Lefevre,S.D., Cambot,M., Cueff,A., Schmitt,M., Gamain,B.,
            Lacapere,J.J., Egee,S., Bihel,F., Le Van Kim,C. and Ostuni,M.A.
  TITLE     TSPO ligands stimulate ZnPPIX transport and ROS accumulation
            leading to the inhibition of P. falciparum growth in human blood
  JOURNAL   Sci Rep 6, 33516 (2016)
   PUBMED   27641616
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Gallerne,C., Touat,Z., Chen,Z.X., Martel,C., Mayola,E., Sharaf el
            dein,O., Buron,N., Le Bras,M., Jacotot,E., Borgne-Sanchez,A.,
            Lemoine,A., Lemaire,C., Pervaiz,S. and Brenner,C.
  TITLE     The fourth isoform of the adenine nucleotide translocator inhibits
            mitochondrial apoptosis in cancer cells
  JOURNAL   Int J Biochem Cell Biol 42 (5), 623-629 (2010)
   PUBMED   20060930
  REMARK    GeneRIF: data highlight a cytoprotective activity of ANT4, and
            provide a novel dichotomy in the ANT isoform sub-family with ANT1
            and 3 isoforms functioning as pro-apoptotic while ANT2 and 4
            isoforms render cells resistant to death inducing stimuli
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Brower,J.V., Lim,C.H., Jorgensen,M., Oh,S.P. and Terada,N.
  TITLE     Adenine nucleotide translocase 4 deficiency leads to early meiotic
            arrest of murine male germ cells
  JOURNAL   Reproduction 138 (3), 463-470 (2009)
   PUBMED   19556438
  REMARK    GeneRIF: Male mice with disruptions of Slc25a31 are sterile and
            display an early meiotic arrest phenotype.
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Kim,Y.H., Haidl,G., Schaefer,M., Egner,U., Mandal,A. and Herr,J.C.
  TITLE     Compartmentalization of a unique ADP/ATP carrier protein SFEC
            (Sperm Flagellar Energy Carrier, AAC4) with glycolytic enzymes in
            the fibrous sheath of the human sperm flagellar principal piece
  JOURNAL   Dev Biol 302 (2), 463-476 (2007)
   PUBMED   17137571
  REMARK    GeneRIF: The co-localization of SFEC and glycolytic enzymes in the
            fibrous sheath supports a growing literature that the principal
            piece of the flagellum is capable of generating and regulating ATP
            independently from mitochondrial oxidation in the mid-piece.
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Dolce,V., Scarcia,P., Iacopetta,D. and Palmieri,F.
  TITLE     A fourth ADP/ATP carrier isoform in man: identification, bacterial
            expression, functional characterization and tissue distribution
  JOURNAL   FEBS Lett 579 (3), 633-637 (2005)
   PUBMED   15670820
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ438347.1, BC022032.2 and
            BG192958.1.
            
            Summary: The protein encoded by this gene is a member of the
            ADP/ATP carrier family of proteins that exchange cytosolic ADP for
            matrix ATP in the mitochondria. Cells over-expressing this gene
            have been shown to display an anti-apoptotic phenotype. This
            protein is also thought to play a role in spermatogenesis, where it
            is believed to associate with a part of the flagellar cytoskeleton
            and with glycolytic enzymes. Male mice with mutations in the mouse
            ortholog of this gene are sterile and spermatocytes display an
            early meiotic arrest phenotype. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.180379.1,
                                           SRR5189667.246184.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000281154.6/
                                                  ENSP00000281154.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.1"
     Protein         1..315
                     /product="ADP/ATP translocase 4 isoform 1"
                     /note="adenine nucleotide translocase 4; ADP/ATP
                     translocase 4; ADP,ATP carrier protein 4; adenine
                     nucleotide translocator 4; sperm flagellar energy carrier
                     protein; solute carrier family 25 (mitochondrial carrier;
                     adenine nucleotide translocator), member 31"
                     /calculated_mol_wt=34891
     Region          18..110
                     /region_name="Solcar 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     Region          19..309
                     /region_name="PTZ00169"
                     /note="ADP/ATP transporter on adenylate translocase;
                     Provisional"
                     /db_xref="CDD:240302"
     Site            20..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     Site            87..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     Region          123..213
                     /region_name="Solcar 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     Site            191..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     Region          220..307
                     /region_name="Solcar 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     Site            223..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     Region          247..252
                     /region_name="Important for transport activity.
                     /evidence=ECO:0000250|UniProtKB:P12235"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     Region          247..252
                     /region_name="Nucleotide carrier signature motif.
                     /evidence=ECO:0000250|UniProtKB:P02722"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     Site            284..301
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C2.1)"
     CDS             1..315
                     /gene="SLC25A31"
                     /gene_synonym="AAC4; ANT 4; ANT4; SFEC35kDa"
                     /coded_by="NM_031291.4:147..1094"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3733.1"
                     /db_xref="GeneID:83447"
                     /db_xref="HGNC:HGNC:25319"
                     /db_xref="MIM:610796"
ORIGIN      
        1 mhrepakkka ekrlfdassf gkdllaggva aavsktavap iervklllqv qasskqispe
       61 arykgmvdcl vripreqgff sfwrgnlanv iryfptqaln fafkdkykql fmsgvnkekq
      121 fwrwflanla sggaagatsl cvvypldfar trlgvdigkg peerqfkglg dcimkiaksd
      181 giaglyqgfg vsvqgiivyr asyfgaydtv kgllpkpkkt pflvsffiaq vvttcsgils
      241 ypfdtvrrrm mmqsgeakrq ykgtldcfvk iyqhegissf frgafsnvlr gtggalvlvl
      301 ydkikeffhi diggr
//
LOCUS       NP_057405                479 aa            linear   PRI 27-APR-2025
DEFINITION  ammonium transporter Rh type C [Homo sapiens].
ACCESSION   NP_057405
VERSION     NP_057405.1
DBSOURCE    REFSEQ: accession NM_016321.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Zhang,Q., Liu,J., Yao,D., Shi,J.X., Liu,Y.J., Wei,Y.G. and Guo,S.
  TITLE     Comprehensive Analysis to Identify Rh Family C Glycoprotein (RHCG)
            as the Causative Gene for Psoriasis and Search for Alternative
            Treatment Modalities
  JOURNAL   Drug Des Devel Ther 17, 2593-2611 (2023)
   PUBMED   37664450
  REMARK    GeneRIF: Comprehensive Analysis to Identify Rh Family C
            Glycoprotein (RHCG) as the Causative Gene for Psoriasis and Search
            for Alternative Treatment Modalities.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Chen,P., Liu,C., Li,P., Wang,Q., Gao,X., Wu,H. and Huang,J.
  TITLE     High RhCG expression predicts poor survival and promotes migration
            and proliferation of gastric cancer via keeping intracellular
            alkaline
  JOURNAL   Exp Cell Res 386 (2), 111740 (2020)
   PUBMED   31756312
  REMARK    GeneRIF: High RhCG level was correlated with poor prognosis of
            gastric cancer patients.
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Xu,W., Zou,H., Wei,Z., Song,C., Tang,C., Yin,X., Wang,Y., Han,S.,
            Cai,Y. and Han,W.
  TITLE     Rh type C-glycoprotein functions as a novel tumor suppressor gene
            by inhibiting tumorigenicity and metastasis in head and neck
            squamous cell carcinoma
  JOURNAL   Aging (Albany NY) 11 (11), 3601-3623 (2019)
   PUBMED   31170090
  REMARK    GeneRIF: Our study reveals that RHCG acts as a tumor suppressor
            gene that plays a crucial role in inhibiting tumorigenicity and
            metastasis in head and neck squamous cell carcinoma.
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Verlander,J.W., Miller,R.T., Frank,A.E., Royaux,I.E., Kim,Y.H. and
            Weiner,I.D.
  TITLE     Localization of the ammonium transporter proteins RhBG and RhCG in
            mouse kidney
  JOURNAL   Am J Physiol Renal Physiol 284 (2), F323-F337 (2003)
   PUBMED   12388412
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Chen,B.S., Xu,Z.X., Xu,X., Cai,Y., Han,Y.L., Wang,J., Xia,S.H.,
            Hu,H., Wei,F., Wu,M. and Wang,M.R.
  TITLE     RhCG is downregulated in oesophageal squamous cell carcinomas, but
            expressed in multiple squamous epithelia
  JOURNAL   Eur J Cancer 38 (14), 1927-1936 (2002)
   PUBMED   12204676
  REMARK    Erratum:[Eur J Cancer. 2003 Feb;39(3):405.]
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Marini,A.M., Matassi,G., Raynal,V., Andre,B., Cartron,J.P. and
            Cherif-Zahar,B.
  TITLE     The human Rhesus-associated RhAG protein and a kidney homologue
            promote ammonium transport in yeast
  JOURNAL   Nat Genet 26 (3), 341-344 (2000)
   PUBMED   11062476
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Liu,Z., Chen,Y., Mo,R., Hui,C., Cheng,J.F., Mohandas,N. and
            Huang,C.H.
  TITLE     Characterization of human RhCG and mouse Rhcg as novel nonerythroid
            Rh glycoprotein homologues predominantly expressed in kidney and
            testis
  JOURNAL   J Biol Chem 275 (33), 25641-25651 (2000)
   PUBMED   10852913
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Ridgwell,K., Spurr,N.K., Laguda,B., MacGeoch,C., Avent,N.D. and
            Tanner,M.J.
  TITLE     Isolation of cDNA clones for a 50 kDa glycoprotein of the human
            erythrocyte membrane associated with Rh (rhesus) blood-group
            antigen expression
  JOURNAL   Biochem J 287 (Pt 1) (Pt 1), 223-228 (1992)
   PUBMED   1417776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC306265.1, AF193809.1 and BC030965.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes a protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030965.1, AK290899.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2156670 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268122.9/ ENSP00000268122.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..479
                     /product="ammonium transporter Rh type C"
                     /note="Rh type C glycoprotein; Rhesus blood group, C
                     glycoprotein; rh glycoprotein kidney; tumor-related
                     protein DRC2; rh family type C glycoprotein; rhesus blood
                     group family type C glycoprotein"
                     /calculated_mol_wt=53048
     Site            10..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20457942; propagated from
                     UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Region          60..435
                     /region_name="Ammonium_transp"
                     /note="Ammonium Transporter Family; cl03012"
                     /db_xref="CDD:445985"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            124..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            178..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            282..302
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            304..324
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            346..366
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            395..415
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     CDS             1..479
                     /gene="RHCG"
                     /gene_synonym="C15orf6; PDRC2; RHGK; SLC42A3"
                     /coded_by="NM_016321.3:40..1479"
                     /db_xref="CCDS:CCDS10351.1"
                     /db_xref="GeneID:51458"
                     /db_xref="HGNC:HGNC:18140"
                     /db_xref="MIM:605381"
ORIGIN      
        1 mawntnlrwr lpltclllqv imvilfgvfv rydfeadahw wserthknls dmenefyyry
       61 psfqdvhvmv fvgfgflmtf lqrygfsavg fnfllaafgi qwallmqgwf hflqdryivv
      121 gvenlinadf cvasvcvafg avlgkvspiq llimtffqvt lfavnefill nllkvkdagg
      181 smtihtfgay fgltvtrily rrnleqsker qnsvyqsdlf amigtlflwm ywpsfnsais
      241 yhgdsqhraa intycslaac vltsvaissa lhkkgkldmv hiqnatlagg vavgtaaemm
      301 lmpygaliig fvcgiistlg fvyltpfles rlhiqdtcgi nnlhgipgii ggivgavtaa
      361 saslevygke glvhsfdfqg fngdwtartq gkfqiygllv tlamalmggi ivglilrlpf
      421 wgqpsdencf edavywempe gnstvyiped ptfkpsgpsv psvpmvsplp massvplvp
//
LOCUS       NP_004485                240 aa            linear   PRI 27-APR-2025
DEFINITION  hepatoma-derived growth factor isoform a [Homo sapiens].
ACCESSION   NP_004485
VERSION     NP_004485.1
DBSOURCE    REFSEQ: accession NM_004494.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wu,J.K., Lee,Y.Y., Hung,H., Chang,Y.P., Tai,M.H. and Fan,H.F.
  TITLE     Binding Behavior of Human Hepatoma-Derived Growth Factor on SMYD1
  JOURNAL   J Phys Chem B 128 (32), 7722-7735 (2024)
   PUBMED   39091133
  REMARK    GeneRIF: Binding Behavior of Human Hepatoma-Derived Growth Factor
            on SMYD1.
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Jia,Y., Liu,S., Zhang,M., Wu,X., Chen,X., Xing,M., Hou,X. and
            Jiang,W.
  TITLE     The m6A reader IGF2BP2 promotes ESCC progression by stabilizing
            HDGF mRNA
  JOURNAL   J Cancer Res Ther 20 (4), 1173-1185 (2024)
   PUBMED   39206979
  REMARK    GeneRIF: The m6A reader IGF2BP2 promotes ESCC progression by
            stabilizing HDGF mRNA.
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Zhou,J., Huang,C.L., Liu,H.W., Zeng,Z.Y. and Tan,J.
  TITLE     [miR-29a-3p Targets Hepatoma-Derived Growth Factor to Inhibit the
            Proliferation and Promote the Apoptosis of E6-1 Cells]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1650-1654 (2022)
   PUBMED   36476884
  REMARK    GeneRIF: [miR-29a-3p Targets Hepatoma-Derived Growth Factor to
            Inhibit the Proliferation and Promote the Apoptosis of E6-1 Cells].
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Hoelzinger,D.B., Quinton,S.J., Walters,D.K., Vardam-Kaur,T.,
            Tschumper,R.C., Borges da Silva,H. and Jelinek,D.F.
  TITLE     Extracellular vesicle proteomic analysis leads to the discovery of
            HDGF as a new factor in multiple myeloma biology
  JOURNAL   Blood Adv 6 (11), 3458-3471 (2022)
   PUBMED   35395072
  REMARK    GeneRIF: Extracellular vesicle proteomic analysis leads to the
            discovery of HDGF as a new factor in multiple myeloma biology.
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Fang,Y. and Yang,Q.
  TITLE     Specificity protein 1-induced serine peptidase inhibitor, Kunitz
            Type 1 antisense RNA1 regulates colorectal cancer cell
            proliferation, migration, invasion and apoptosis through targeting
            heparin binding growth factor via sponging microRNA-214
  JOURNAL   Bioengineered 13 (2), 3309-3322 (2022)
   PUBMED   35068341
  REMARK    GeneRIF: Specificity protein 1-induced serine peptidase inhibitor,
            Kunitz Type 1 antisense RNA1 regulates colorectal cancer cell
            proliferation, migration, invasion and apoptosis through targeting
            heparin binding growth factor via sponging microRNA-214.
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Mori,M., Morishita,H., Nakamura,H., Matsuoka,H., Yoshida,K.,
            Kishima,Y., Zhou,Z., Kida,H., Funakoshi,T., Goya,S., Yoshida,M.,
            Kumagai,T., Tachibana,I., Yamamoto,Y., Kawase,I. and Hayashi,S.
  TITLE     Hepatoma-derived growth factor is involved in lung remodeling by
            stimulating epithelial growth
  JOURNAL   Am J Respir Cell Mol Biol 30 (4), 459-469 (2004)
   PUBMED   12972397
  REMARK    GeneRIF: may be involved in lung remodeling after injury
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Yoshida,K., Nakamura,H., Okuda,Y., Enomoto,H., Kishima,Y.,
            Uyama,H., Ito,H., Hirasawa,T., Inagaki,S. and Kawase,I.
  TITLE     Expression of hepatoma-derived growth factor in
            hepatocarcinogenesis
  JOURNAL   J Gastroenterol Hepatol 18 (11), 1293-1301 (2003)
   PUBMED   14535987
REFERENCE   8  (residues 1 to 240)
  AUTHORS   Kishima,Y., Yamamoto,H., Izumoto,Y., Yoshida,K., Enomoto,H.,
            Yamamoto,M., Kuroda,T., Ito,H., Yoshizaki,K. and Nakamura,H.
  TITLE     Hepatoma-derived growth factor stimulates cell growth after
            translocation to the nucleus by nuclear localization signals
  JOURNAL   J Biol Chem 277 (12), 10315-10322 (2002)
   PUBMED   11751870
  REMARK    GeneRIF: Hepatoma-derived growth factor stimulates cell growth
            after translocation to the nucleus
REFERENCE   9  (residues 1 to 240)
  AUTHORS   Wanschura,S., Schoenmakers,E.F., Huysmans,C., Bartnitzke,S., Van de
            Ven,W.J. and Bullerdiek,J.
  TITLE     Mapping of the gene encoding the human hepatoma-derived growth
            factor (HDGF) with homology to the high-mobility group (HMG)-1
            protein to Xq25
  JOURNAL   Genomics 32 (2), 298-300 (1996)
   PUBMED   8833162
REFERENCE   10 (residues 1 to 240)
  AUTHORS   Nakamura,H., Izumoto,Y., Kambe,H., Kuroda,T., Mori,T., Kawamura,K.,
            Yamamoto,H. and Kishimoto,T.
  TITLE     Molecular cloning of complementary DNA for a novel human
            hepatoma-derived growth factor. Its homology with high mobility
            group-1 protein
  JOURNAL   J Biol Chem 269 (40), 25143-25149 (1994)
   PUBMED   7929202
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590666.8.
            
            Summary: This gene encodes a member of the hepatoma-derived growth
            factor family. The encoded protein has mitogenic and DNA-binding
            activity and may play a role in cellular proliferation and
            differentiation. High levels of expression of this gene enhance the
            growth of many tumors. This gene was thought initially to be
            located on chromosome X; however, that location has been determined
            to correspond to a related pseudogene. Alternatively spliced
            transcript variants encoding distinct isoforms have been described.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) differs in the 5' UTR and
            coding sequence and uses an alternate in-frame splice junction
            compared to variant 4. The resulting isoform (a) has a shorter and
            distinct N-terminus and lacks an alternate internal segment
            compared to isoform d.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279872.2695.1, D16431.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357325.10/ ENSP00000349878.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.1"
     Protein         1..240
                     /product="hepatoma-derived growth factor isoform a"
                     /note="high mobility group protein 1-like 2; hepatoma
                     derived growth factor; epididymis secretory sperm binding
                     protein"
                     /calculated_mol_wt=26657
     Region          10..96
                     /region_name="PWWP"
                     /note="PWWP (Pro-Trp-Trp-Pro) domain; cl02554"
                     /db_xref="CDD:470613"
     Site            order(23,26,49)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438958"
     Site            24..27
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438958"
     Site            44
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51858.1)"
     Region          69..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51858.1)"
     Region          75..80
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:11751870"
                     /note="propagated from UniProtKB/Swiss-Prot (P51858.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16807684,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17487921,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P51858.1)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16807684,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17487921,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P51858.1)"
     Region          155..170
                     /region_name="Bipartite nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P51858.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15302935,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51858.1)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51858.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VHK7; propagated from
                     UniProtKB/Swiss-Prot (P51858.1)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51858.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51858.1)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P51858.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51858.1)"
     CDS             1..240
                     /gene="HDGF"
                     /gene_synonym="HMG1L2"
                     /coded_by="NM_004494.3:247..969"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1156.1"
                     /db_xref="GeneID:3068"
                     /db_xref="HGNC:HGNC:4856"
                     /db_xref="MIM:600339"
ORIGIN      
        1 msrsnrqkey kcgdlvfakm kgyphwpari dempeaavks tankyqvfff gthetaflgp
       61 kdlfpyeesk ekfgkpnkrk gfseglweie nnptvkasgy qssqkkscve epepepeaae
      121 gdgdkkgnae gssdeegklv idepakekne kgalkrragd lledspkrpk eaenpegeek
      181 eaatleverp lpmeveknst psepgsgrgp pqeeeeeede eeeatkedae apgirdhesl
//
LOCUS       NP_005329               1037 aa            linear   PRI 27-APR-2025
DEFINITION  huntingtin-interacting protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_005329
VERSION     NP_005329.3
DBSOURCE    REFSEQ: accession NM_005338.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Laragione,T., Harris,C. and Gulko,P.S.
  TITLE     KIF1C and new Huntingtin-interacting protein 1 binding proteins
            regulate rheumatoid arthritis fibroblast-like synoviocytes'
            phenotypes
  JOURNAL   Front Immunol 15, 1323410 (2024)
   PUBMED   38726004
  REMARK    GeneRIF: KIF1C and new Huntingtin-interacting protein 1 binding
            proteins regulate rheumatoid arthritis fibroblast-like
            synoviocytes' phenotypes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Bettencourt,C., Miki,Y., Piras,I.S., de Silva,R., Foti,S.C.,
            Talboom,J.S., Revesz,T., Lashley,T., Balazs,R., Vire,E.,
            Warner,T.T., Huentelman,M.J. and Holton,J.L.
  TITLE     MOBP and HIP1 in multiple system atrophy: New alpha-synuclein
            partners in glial cytoplasmic inclusions implicated in the disease
            pathogenesis
  JOURNAL   Neuropathol Appl Neurobiol 47 (5), 640-652 (2021)
   PUBMED   33368549
  REMARK    GeneRIF: MOBP and HIP1 in multiple system atrophy: New
            alpha-synuclein partners in glial cytoplasmic inclusions implicated
            in the disease pathogenesis.
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1037)
  AUTHORS   Gervais,F.G., Singaraja,R., Xanthoudakis,S., Gutekunst,C.A.,
            Leavitt,B.R., Metzler,M., Hackam,A.S., Tam,J., Vaillancourt,J.P.,
            Houtzager,V., Rasper,D.M., Roy,S., Hayden,M.R. and Nicholson,D.W.
  TITLE     Recruitment and activation of caspase-8 by the
            Huntingtin-interacting protein Hip-1 and a novel partner Hippi
  JOURNAL   Nat Cell Biol 4 (2), 95-105 (2002)
   PUBMED   11788820
  REMARK    GeneRIF: Results show that pro-apoptotic Hippi-Hip-1 heterodimers
            can recruit procaspase-8 into a complex of Hippi, Hip-1 and
            procaspase-8, and launch apoptosis through components of the
            'extrinsic' cell-death pathway.
REFERENCE   5  (residues 1 to 1037)
  AUTHORS   Rao,D.S., Chang,J.C., Kumar,P.D., Mizukami,I., Smithson,G.M.,
            Bradley,S.V., Parlow,A.F. and Ross,T.S.
  TITLE     Huntingtin interacting protein 1 Is a clathrin coat binding protein
            required for differentiation of late spermatogenic progenitors
  JOURNAL   Mol Cell Biol 21 (22), 7796-7806 (2001)
   PUBMED   11604514
REFERENCE   6  (residues 1 to 1037)
  AUTHORS   Chopra,V.S., Metzler,M., Rasper,D.M., Engqvist-Goldstein,A.E.,
            Singaraja,R., Gan,L., Fichter,K.M., McCutcheon,K., Drubin,D.,
            Nicholson,D.W. and Hayden,M.R.
  TITLE     HIP12 is a non-proapoptotic member of a gene family including HIP1,
            an interacting protein with huntingtin
  JOURNAL   Mamm Genome 11 (11), 1006-1015 (2000)
   PUBMED   11063258
REFERENCE   7  (residues 1 to 1037)
  AUTHORS   Ross,T.S., Bernard,O.A., Berger,R. and Gilliland,D.G.
  TITLE     Fusion of Huntingtin interacting protein 1 to platelet-derived
            growth factor beta receptor (PDGFbetaR) in chronic myelomonocytic
            leukemia with t(5;7)(q33;q11.2)
  JOURNAL   Blood 91 (12), 4419-4426 (1998)
   PUBMED   9616134
REFERENCE   8  (residues 1 to 1037)
  AUTHORS   Wedemeyer,N., Peoples,R., Himmelbauer,H., Lehrach,H., Francke,U.
            and Wanker,E.E.
  TITLE     Localization of the human HIP1 gene close to the elastin (ELN)
            locus on 7q11.23
  JOURNAL   Genomics 46 (2), 313-315 (1997)
   PUBMED   9417924
REFERENCE   9  (residues 1 to 1037)
  AUTHORS   Kalchman,M.A., Koide,H.B., McCutcheon,K., Graham,R.K., Nichol,K.,
            Nishiyama,K., Kazemi-Esfarjani,P., Lynn,F.C., Wellington,C.,
            Metzler,M., Goldberg,Y.P., Kanazawa,I., Gietz,R.D. and Hayden,M.R.
  TITLE     HIP1, a human homologue of S. cerevisiae Sla2p, interacts with
            membrane-associated huntingtin in the brain
  JOURNAL   Nat Genet 16 (1), 44-53 (1997)
   PUBMED   9140394
REFERENCE   10 (residues 1 to 1037)
  AUTHORS   Wanker,E.E., Rovira,C., Scherzinger,E., Hasenbank,R., Walter,S.,
            Tait,D., Colicelli,J. and Lehrach,H.
  TITLE     HIP-I: a huntingtin interacting protein isolated by the yeast
            two-hybrid system
  JOURNAL   Hum Mol Genet 6 (3), 487-495 (1997)
   PUBMED   9147654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC110545.2, AF365404.1,
            AK296390.1, AC211429.4 and BQ446538.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 30, 2003 this sequence version replaced NP_005329.2.
            
            Summary: The product of this gene is a membrane-associated protein
            that functions in clathrin-mediated endocytosis and protein
            trafficking within the cell. The encoded protein binds to the
            huntingtin protein in the brain; this interaction is lost in
            Huntington's disease. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110545.2, AF365404.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336926.11/ ENSP00000336747.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..1037
                     /product="huntingtin-interacting protein 1 isoform 1"
                     /note="huntingtin-interacting protein I"
                     /calculated_mol_wt=116091
     Region          39..306
                     /region_name="ANTH"
                     /note="ANTH domain; pfam07651"
                     /db_xref="CDD:400137"
     Site            order(46,56,58..59)
                     /site_type="other"
                     /note="PtdIns(4,5)P2-binding site [chemical binding]"
                     /db_xref="CDD:340810"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00291.5)"
     Region          <370..>644
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          410..491
                     /region_name="pDED"
                     /note="propagated from UniProtKB/Swiss-Prot (O00291.5)"
     Region          482..580
                     /region_name="HIP1_clath_bdg"
                     /note="Clathrin-binding domain of Huntingtin-interacting
                     protein 1; pfam16515"
                     /db_xref="CDD:465154"
     Region          814..1012
                     /region_name="ILWEQ"
                     /note="I/LWEQ domain; smart00307"
                     /db_xref="CDD:214607"
     Region          867..924
                     /region_name="Important for actin binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O00291.5)"
     Region          1017..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00291.5)"
     CDS             1..1037
                     /gene="HIP1"
                     /gene_synonym="HIP-I; ILWEQ; SHON; SHONbeta; SHONgamma"
                     /coded_by="NM_005338.7:22..3135"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34669.1"
                     /db_xref="GeneID:3092"
                     /db_xref="HGNC:HGNC:4913"
                     /db_xref="MIM:601767"
ORIGIN      
        1 mdrmassmkq vpnplpkvls rrgvgaglea aeresfertq tvsinkaint qevavkekha
       61 rtcilgthhe kgaqtfwsvv nrlplssnav lcwkfchvfh kllrdghpnv lkdslryrne
      121 lsdmsrmwgh lsegygqlcs iylkllrtkm eyhtknprfp gnlqmsdrql deagesdvnn
      181 ffqltvemfd ylecelnlfq tvfnsldmsr svsvtaagqc rlapliqvil dcshlydytv
      241 kllfklhscl padtlqghrd rfmeqftklk dlfyrssnlq yfkrliqipq lpenppnflr
      301 asalsehisp vvvipaeass pdsepvlekd dlmdmdasqq nlfdnkfddi fgssfssdpf
      361 nfnsqngvnk dekdhlierl yreisglkaq lenmktesqr vvlqlkghvs eleadlaeqq
      421 hlrqqaaddc eflraeldel rrqredteka qrslseierk aqaneqrysk lkekyselvq
      481 nhadllrkna evtkqvsmar qaqvdlerek keledsleri sdqgqrktqe qlevleslkq
      541 elatsqrelq vlqgsletsa qseanwaaef aelekerdsl vsgaahreee lsalrkelqd
      601 tqlklastee smcqlakdqr kmllvgsrka aeqviqdaln qleepplisc agsadhllst
      661 vtsisscieq lekswsqyla cpedisgllh sitllahlts daiahgattc lrappepads
      721 lteackqygr etlaylasle eegslenads tamrnclski kaigeellpr gldikqeelg
      781 dlvdkemaat saaietatar ieemlsksra gdtgvklevn erilgcctsl mqaiqvliva
      841 skdlqreive sgrgtaspke fyaknsrwte glisaskavg wgatvmvdaa dlvvqgrgkf
      901 eelmvcshei aastaqlvaa skvkadkdsp nlaqlqqasr gvnqatagvv astisgksqi
      961 eetdnmdfss mtltqikrqe mdsqvrvlel enelqkerqk lgelrkkhye lagvaegwee
     1021 gteaspptlq evvteke
//
LOCUS       NP_001347983             304 aa            linear   ROD 27-APR-2025
DEFINITION  small glutamine-rich tetratricopeptide repeat-containing protein
            beta [Mus musculus].
ACCESSION   NP_001347983 XP_006517673
VERSION     NP_001347983.1
DBSOURCE    REFSEQ: accession NM_001361054.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Vuong,T.A., Lee,S.J., Leem,Y.E., Lee,J.R., Bae,G.U. and Kang,J.S.
  TITLE     SGTb regulates a surface localization of a guidance receptor BOC to
            promote neurite outgrowth
  JOURNAL   Cell Signal 55, 100-108 (2019)
   PUBMED   30639199
  REMARK    GeneRIF: The data suggest that SGTb interacts with BOC (brother of
            CDO protein) and regulates its surface level and consequent JNK
            activation, thereby promoting neuronal differentiation and neurite
            outgrowth.
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Tobaben,S., Varoqueaux,F., Brose,N., Stahl,B. and Meyer,G.
  TITLE     A brain-specific isoform of small glutamine-rich tetratricopeptide
            repeat-containing protein binds to Hsc70 and the cysteine string
            protein
  JOURNAL   J Biol Chem 278 (40), 38376-38383 (2003)
   PUBMED   12878599
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC154216.1.
            
            On Feb 27, 2018 this sequence version replaced XP_006517673.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.33319.1,
                                           SRR9219380.54118.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849385
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 56.23 cM"
     Protein         1..304
                     /product="small glutamine-rich tetratricopeptide
                     repeat-containing protein beta"
                     /note="beta-SGT"
                     /calculated_mol_wt=33298
     Region          5..64
                     /region_name="SGTA_dimer"
                     /note="Homodimerization domain of SGTA; pfam16546"
                     /db_xref="CDD:465168"
     Region          15..49
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VD33.1)"
     Region          85..118
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VD33.1)"
     Region          85..113
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(86,89..90,93..94,96,120,123..124,127..128,130..131,
                     154,157..158,161..162,165)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          92..>200
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          118..148
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          120..152
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VD33.1)"
     Site            131
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O43765; propagated from
                     UniProtKB/Swiss-Prot (Q8VD33.1)"
     Region          153..186
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VD33.1)"
     Region          153..181
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43765; propagated from
                     UniProtKB/Swiss-Prot (Q8VD33.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96EQ0; propagated from
                     UniProtKB/Swiss-Prot (Q8VD33.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96EQ0; propagated from
                     UniProtKB/Swiss-Prot (Q8VD33.1)"
     CDS             1..304
                     /gene="Sgtb"
                     /gene_synonym="C630001O05Rik"
                     /coded_by="NM_001361054.1:274..1188"
                     /db_xref="CCDS:CCDS26746.1"
                     /db_xref="GeneID:218544"
                     /db_xref="MGI:MGI:2444615"
ORIGIN      
        1 mssvkplvya virflreqsq mdaytsdeqe slevaiqcle tvfkispedt hlavsqplte
       61 mftnsvcknd irplsnsvpe dvgkadqlkd egnnhmkeen yaaavdcytq aieldpnnav
      121 yycnraaaqs klshytdaik dcekaiaids kyskaygrmg laltamnkfe eavtsyqkal
      181 dldpendsyk snlkiaeqkl revssptgtg lsfdmaslin npafitmaas lmqnpqvqql
      241 msgmmtnaig gpaagvgglt dlssliqagq qfaqqiqqqn pelieqlrnh irsrsfsssa
      301 dehs
//
LOCUS       NP_037423               1443 aa            linear   PRI 27-APR-2025
DEFINITION  cleavage and polyadenylation specificity factor subunit 1 [Homo
            sapiens].
ACCESSION   NP_037423
VERSION     NP_037423.2
DBSOURCE    REFSEQ: accession NM_013291.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1443)
  AUTHORS   Chen,X., Lloyd,S.M., Kweon,J., Gamalong,G.M. and Bao,X.
  TITLE     Epidermal progenitors suppress GRHL3-mediated differentiation
            through intronic polyadenylation promoted by CPSF-HNRNPA3
            collaboration
  JOURNAL   Nat Commun 12 (1), 448 (2021)
   PUBMED   33469008
  REMARK    GeneRIF: Epidermal progenitors suppress GRHL3-mediated
            differentiation through intronic polyadenylation promoted by
            CPSF-HNRNPA3 collaboration.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1443)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1443)
  AUTHORS   Ouyang,J., Sun,W., Xiao,X., Li,S., Jia,X., Zhou,L., Wang,P. and
            Zhang,Q.
  TITLE     CPSF1 mutations are associated with early-onset high myopia and
            involved in retinal ganglion cell axon projection
  JOURNAL   Hum Mol Genet 28 (12), 1959-1970 (2019)
   PUBMED   30689892
  REMARK    GeneRIF: Heterozygous loss-of-function mutations in CPSF1 are
            associated with early-onset high myopia and that CPSF1 may play an
            important role in the development of retinal ganglion cell axon
            projection.
REFERENCE   4  (residues 1 to 1443)
  AUTHORS   Clerici,M., Faini,M., Muckenfuss,L.M., Aebersold,R. and Jinek,M.
  TITLE     Structural basis of AAUAAA polyadenylation signal recognition by
            the human CPSF complex
  JOURNAL   Nat Struct Mol Biol 25 (2), 135-138 (2018)
   PUBMED   29358758
  REMARK    GeneRIF: cryo-electron microscopic analysis of a core CPSF module
            bound to the polyadenylation signal hexamer motif
            Erratum:[Nat Struct Mol Biol. 2018 Apr;25(4):355. doi:
            10.1038/s41594-018-0044-6. PMID: 29540792]
REFERENCE   5  (residues 1 to 1443)
  AUTHORS   Zhang,B., Liu,Y., Liu,D. and Yang,L.
  TITLE     Targeting cleavage and polyadenylation specific factor 1 via shRNA
            inhibits cell proliferation in human ovarian cancer
  JOURNAL   J Biosci 42 (3), 417-425 (2017)
   PUBMED   29358555
  REMARK    GeneRIF: Knockdown of CPSF inhibits the proliferation, migration
            and invasion of ovarian carcinoma cells.
REFERENCE   6  (residues 1 to 1443)
  AUTHORS   Schul,W., Groenhout,B., Koberna,K., Takagaki,Y., Jenny,A.,
            Manders,E.M., Raska,I., van Driel,R. and de Jong,L.
  TITLE     The RNA 3' cleavage factors CstF 64 kDa and CPSF 100 kDa are
            concentrated in nuclear domains closely associated with coiled
            bodies and newly synthesized RNA
  JOURNAL   EMBO J 15 (11), 2883-2892 (1996)
   PUBMED   8654386
REFERENCE   7  (residues 1 to 1443)
  AUTHORS   Murthy,K.G. and Manley,J.L.
  TITLE     The 160-kD subunit of human cleavage-polyadenylation specificity
            factor coordinates pre-mRNA 3'-end formation
  JOURNAL   Genes Dev 9 (21), 2672-2683 (1995)
   PUBMED   7590244
REFERENCE   8  (residues 1 to 1443)
  AUTHORS   Jenny,A. and Keller,W.
  TITLE     Cloning of cDNAs encoding the 160 kDa subunit of the bovine
            cleavage and polyadenylation specificity factor
  JOURNAL   Nucleic Acids Res 23 (14), 2629-2635 (1995)
   PUBMED   7651824
REFERENCE   9  (residues 1 to 1443)
  AUTHORS   Thuresson,A.C., Astrom,J., Astrom,A., Gronvik,K.O. and Virtanen,A.
  TITLE     Multiple forms of poly(A) polymerases in human cells
  JOURNAL   Proc Natl Acad Sci U S A 91 (3), 979-983 (1994)
   PUBMED   8302877
REFERENCE   10 (residues 1 to 1443)
  AUTHORS   Keller,W., Bienroth,S., Lang,K.M. and Christofori,G.
  TITLE     Cleavage and polyadenylation factor CPF specifically interacts with
            the pre-mRNA 3' processing signal AAUAAA
  JOURNAL   EMBO J 10 (13), 4241-4249 (1991)
   PUBMED   1756731
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD299980.1 and BC017232.2.
            
            On Dec 16, 2004 this sequence version replaced NP_037423.1.
            
            Summary: Cleavage and polyadenylation specificity factor (CPSF) is
            a multisubunit complex that plays a central role in 3-prime
            processing of pre-mRNAs. CPSF recognizes the AAUAAA signal in the
            pre-mRNA and interacts with other proteins to facilitate both RNA
            cleavage and poly(A) synthesis. CPSF1 is the largest subunit of the
            CPSF complex (Murthy and Manley, 1995 [PubMed 7590244]).[supplied
            by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017232.2, U37012.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000616140.2/ ENSP00000484669.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..1443
                     /product="cleavage and polyadenylation specificity factor
                     subunit 1"
                     /EC_number="2.4.2.30"
                     /note="polyadenylation specificity factor; CPSF 160 kDa
                     subunit; cleavage and polyadenylation specificity factor
                     160 kDa subunit; cleavage and polyadenylation specific
                     factor 1, 160kDa"
                     /calculated_mol_wt=160754
     Region          1..1437
                     /region_name="SFT1"
                     /note="Pre-mRNA cleavage and polyadenylation specificity
                     factor [RNA processing and modification]; COG5161"
                     /db_xref="CDD:227490"
     Region          404..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10570.2)"
     Region          546..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10570.2)"
     Region          715..777
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10570.2)"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EPU4; propagated from
                     UniProtKB/Swiss-Prot (Q10570.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q10570.2)"
     Region          893..908
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10570.2)"
     Region          901..921
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10570.2)"
     CDS             1..1443
                     /gene="CPSF1"
                     /gene_synonym="CPSF160; HSU37012; MYP27; P/cl.18"
                     /coded_by="NM_013291.3:62..4393"
                     /db_xref="CCDS:CCDS34966.1"
                     /db_xref="GeneID:29894"
                     /db_xref="HGNC:HGNC:2324"
                     /db_xref="MIM:606027"
ORIGIN      
        1 myavykqahp ptglefsmyc nffnnsernl vvagtsqlyv yrlnrdaeal tkndrstegk
       61 ahreklelaa sfsffgnvms masvqlagak rdalllsfkd aklsvveydp gthdlktlsl
      121 hyfeepelrd gfvqnvhtpr vrvdpdgrca amlvygtrlv vlpfrresla eeheglvgeg
      181 qrssflpsyi idvraldekl lniidlqflh gyyeptllil fepnqtwpgr vavrqdtcsi
      241 vaislnitqk vhpviwslts lpfdctqala vpkpiggvvv favnsllyln qsvppygval
      301 nslttgttaf plrtqegvri tldcaqatfi sydkmvislk ggeiyvltli tdgmrsvraf
      361 hfdkaaasvl ttsmvtmepg ylflgsrlgn slllkytekl qeppasavre aadkeeppsk
      421 kkrvdatagw saagksvpqd evdeievygs eaqsgtqlat ysfevcdsil nigpcanaav
      481 gepaflseef qnspepdlei vvcsghgkng alsvlqksir pqvvttfelp gcydmwtvia
      541 pvrkeeednp kgegteqeps ttpeadddgr rhgflilsre dstmilqtgq eimeldtsgf
      601 atqgptvfag nigdnryivq vsplgirlle gvnqlhfipv dlgapivqca vadpyvvims
      661 aeghvtmfll ksdsyggrhh rlalhkpplh hqskvitlcl yrdlsgmftt esrlggarde
      721 lggrsgpeae glgsetsptv ddeeemlygd sgslfspske earrssqppa drdpapfrae
      781 pthwcllvre ngtmeiyqlp dwrlvflvkn fpvgqrvlvd ssfgqpttqg earreeatrq
      841 gelplvkevl lvalgsrqsr pyllvhvdqe lliyeafphd sqlgqgnlkv rfkkvphnin
      901 frekkpkpsk kkaegggaee gagargrvar fryfediygy sgvficgpsp hwllvtgrga
      961 lrlhpmaidg pvdsfapfhn vncprgflyf nrqgelrisv lpaylsydap wpvrkiplrc
     1021 tahyvayhve skvyavatst ntpcariprm tgeekefeti erderyihpq qeafsiqlis
     1081 pvsweaipna rielqewehv tcmktvslrs eetvsglkgy vaagtclmqg eevtcrgril
     1141 imdvievvpe pgqpltknkf kvlyekeqkg pvtalchcng hlvsaigqki flwslrasel
     1201 tgmafidtql yihqmisvkn filaadvmks isllryqees ktlslvsrda kplevysvdf
     1261 mvdnaqlgfl vsdrdrnlmv ymylpeakes fggmrllrra dfhvgahvnt fwrtpcrgat
     1321 eglskksvvw enkhitwfat ldggiglllp mqektyrrll mlqnalttml phhaglnpra
     1381 frmlhvdrrt lqnavrnvld gellnrylyl stmerselak kigttpdiil ddlletdrvt
     1441 ahf
//
LOCUS       NP_037452                792 aa            linear   PRI 27-APR-2025
DEFINITION  host cell factor 2 [Homo sapiens].
ACCESSION   NP_037452
VERSION     NP_037452.1
DBSOURCE    REFSEQ: accession NM_013320.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Park,S.H., Ayoub,A., Lee,Y.T., Xu,J., Kim,H., Zheng,W., Zhang,B.,
            Sha,L., An,S., Zhang,Y., Cianfrocco,M.A., Su,M., Dou,Y. and
            Cho,U.S.
  TITLE     Cryo-EM structure of the human MLL1 core complex bound to the
            nucleosome
  JOURNAL   Nat Commun 10 (1), 5540 (2019)
   PUBMED   31804488
  REMARK    Erratum:[Nat Commun. 2020 Feb 27;11(1):1165. doi:
            10.1038/s41467-020-14973-y. PMID: 32109228]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 792)
  AUTHORS   Gudkova,D., Dergai,O., Praz,V. and Herr,W.
  TITLE     HCF-2 inhibits cell proliferation and activates
            differentiation-gene expression programs
  JOURNAL   Nucleic Acids Res 47 (11), 5792-5808 (2019)
   PUBMED   31049581
  REMARK    GeneRIF: HCF-2 is broadly present in human and mouse cells, and
            possesses activities distinct from HCF-1
REFERENCE   4  (residues 1 to 792)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 792)
  AUTHORS   Li,Y., Han,J., Zhang,Y., Cao,F., Liu,Z., Li,S., Wu,J., Hu,C.,
            Wang,Y., Shuai,J., Chen,J., Cao,L., Li,D., Shi,P., Tian,C.,
            Zhang,J., Dou,Y., Li,G., Chen,Y. and Lei,M.
  TITLE     Structural basis for activity regulation of MLL family
            methyltransferases
  JOURNAL   Nature 530 (7591), 447-452 (2016)
   PUBMED   26886794
REFERENCE   6  (residues 1 to 792)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   7  (residues 1 to 792)
  AUTHORS   van Nuland,R., Smits,A.H., Pallaki,P., Jansen,P.W., Vermeulen,M.
            and Timmers,H.T.
  TITLE     Quantitative dissection and stoichiometry determination of the
            human SET1/MLL histone methyltransferase complexes
  JOURNAL   Mol Cell Biol 33 (10), 2067-2077 (2013)
   PUBMED   23508102
REFERENCE   8  (residues 1 to 792)
  AUTHORS   Yokoyama,A., Wang,Z., Wysocka,J., Sanyal,M., Aufiero,D.J.,
            Kitabayashi,I., Herr,W. and Cleary,M.L.
  TITLE     Leukemia proto-oncoprotein MLL forms a SET1-like histone
            methyltransferase complex with menin to regulate Hox gene
            expression
  JOURNAL   Mol Cell Biol 24 (13), 5639-5649 (2004)
   PUBMED   15199122
REFERENCE   9  (residues 1 to 792)
  AUTHORS   Johnson,K.M., Mahajan,S.S. and Wilson,A.C.
  TITLE     Herpes simplex virus transactivator VP16 discriminates between
            HCF-1 and a novel family member, HCF-2
  JOURNAL   J Virol 73 (5), 3930-3940 (1999)
   PUBMED   10196288
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB030069.1, BC033799.1,
            AC089983.23 and AI247087.1.
            
            Summary: This gene encodes one of two proteins which interact with
            VP16, a herpes simplex virus protein that initiates virus
            infection. Both the encoded protein and the original Herpes host
            cell factor interact with VP16 through a beta-propeller domain. The
            original Herpes host cell factor, however, is effective at
            initiating viral infection while the encoded protein is not.
            Transcripts of varying length due to alternative polyadenylation
            signals have been described. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.206310.1,
                                           SRR1660803.229480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000229330.9/ ENSP00000229330.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..792
                     /product="host cell factor 2"
                     /note="C2 factor"
                     /calculated_mol_wt=86648
     Region          14..332
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          23..69
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          34..79
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Z7.1)"
     Region          83..130
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Z7.1)"
     Region          127..186
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          190..241
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          207..255
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Z7.1)"
     Region          245..312
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          257..303
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Z7.1)"
     Region          312..355
                     /region_name="Kelch_5"
                     /note="Kelch motif; pfam13854"
                     /db_xref="CDD:433528"
     Region          399..447
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Z7.1)"
     Region          535..>704
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          <618..672
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(661..662,664..665)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          678..778
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(678,751,772)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(773..774,776..777)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     CDS             1..792
                     /gene="HCFC2"
                     /gene_synonym="HCF-2; HCF2"
                     /coded_by="NM_013320.3:31..2409"
                     /db_xref="CCDS:CCDS9097.1"
                     /db_xref="GeneID:29915"
                     /db_xref="HGNC:HGNC:24972"
                     /db_xref="MIM:607926"
ORIGIN      
        1 maapsllnwr rvssftgpvp rarhghrava irelmiifgg gnegiadelh vyntatnqwf
       61 lpavrgdipp gcaahgfvcd gtrilvfggm veygrysnel yelqasrwlw kkvkphppps
      121 glppcprlgh sfslygnkcy lfgglanese dsnnnvpryl ndfyelelqh gsgvvgwsip
      181 vtkgvvpspr eshtaviyck kdsgspkmyv fggmcgarld dlwqldletm swskpetkgt
      241 vplprslhta svignkmyif ggwvphkgen tetsphdcew rctssfsyln ldttewttlv
      301 sdsqedkkns rprpraghca vaigtrlyfw sgrdgykkal nsqvcckdlw yldtekppap
      361 sqvqlikatt nsfhvkwdev stvegyllql stdlpyqaas sdssaapnmq gvrmdphrqg
      421 snnivpnsin dtinstkteq patketsmkn kpdfkaltds nailypslas nasnhnshvv
      481 dmlrknegph tsanvgvlss cldvrtvipe tsvsstvsst qtmvtqqtik tessstngav
      541 vkdetslttf stksevdety alpatkisrv ethatatpfs ketpsnpvat vkagerqwcd
      601 vgifknntal vsqfyllpkg kqsiskvgna dvpdysllkk qdlvpgtgyr frvaaingcg
      661 igpfskisef ktcipgfpga psavrisknv egihlswepp tspsgniley saylairtaq
      721 iqdnpsqlvf mriycglkts civtagqlan ahidytsrpa ivfrisakne kgygpatqvr
      781 wlqgnnkkap ln
//
LOCUS       NP_001356708             246 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase MARCHF2 isoform 1 [Homo sapiens].
ACCESSION   NP_001356708
VERSION     NP_001356708.1
DBSOURCE    REFSEQ: accession NM_001369779.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Ni,D., Qi,Z., Wang,Y., Man,Y., Pang,J., Tang,W., Chen,J., Li,J. and
            Li,G.
  TITLE     KLF15-activated MARCH2 boosts cell proliferation and
            epithelial-mesenchymal transition and presents diagnostic
            significance for hepatocellular carcinoma
  JOURNAL   Exp Cell Res 440 (1), 114117 (2024)
   PUBMED   38848952
  REMARK    GeneRIF: KLF15-activated MARCH2 boosts cell proliferation and
            epithelial-mesenchymal transition and presents diagnostic
            significance for hepatocellular carcinoma.
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Seo,T., Lowery,A.M., Xu,H., Giang,W., Troyanovsky,S.M.,
            Vincent,P.A. and Kowalczyk,A.P.
  TITLE     MARCH family E3 ubiquitin ligases selectively target and degrade
            cadherin family proteins
  JOURNAL   PLoS One 19 (5), e0290485 (2024)
   PUBMED   38722959
  REMARK    GeneRIF: MARCH family E3 ubiquitin ligases selectively target and
            degrade cadherin family proteins.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Ito,K., Harada,I., Martinez,C., Sato,K., Lee,E., Port,E.,
            Byerly,J.H., Nayak,A., Tripathi,E., Zhu,J. and Irie,H.Y.
  TITLE     MARCH2, a Novel Oncogene-regulated SNAIL E3 Ligase, Suppresses
            Triple-negative Breast Cancer Metastases
  JOURNAL   Cancer Res Commun 4 (3), 946-957 (2024)
   PUBMED   38457262
  REMARK    GeneRIF: MARCH2, a Novel Oncogene-regulated SNAIL E3 Ligase,
            Suppresses Triple-negative Breast Cancer Metastases.
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Yu,C., Bai,Y., Tan,W., Bai,Y., Li,X., Zhou,Y., Zhai,J., Xue,M.,
            Tang,Y.D., Zheng,C. and Liu,Q.
  TITLE     Human MARCH1, 2, and 8 block Ebola virus envelope glycoprotein
            cleavage via targeting furin P domain
  JOURNAL   J Med Virol 96 (2), e29445 (2024)
   PUBMED   38299743
  REMARK    GeneRIF: Human MARCH1, 2, and 8 block Ebola virus envelope
            glycoprotein cleavage via targeting furin P domain.
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Chathuranga,K., Kim,T.H., Lee,H., Park,J.S., Kim,J.H.,
            Chathuranga,W.A.G., Ekanayaka,P., Choi,Y.J., Lee,C.H., Kim,C.J.,
            Jung,J.U. and Lee,J.S.
  TITLE     Negative regulation of NEMO signaling by the ubiquitin E3 ligase
            MARCH2
  JOURNAL   EMBO J 39 (21), e105139 (2020)
   PUBMED   32935379
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   8  (residues 1 to 246)
  AUTHORS   Fukuda,H., Nakamura,N. and Hirose,S.
  TITLE     MARCH-III Is a novel component of endosomes with properties similar
            to those of MARCH-II
  JOURNAL   J Biochem 139 (1), 137-145 (2006)
   PUBMED   16428329
REFERENCE   9  (residues 1 to 246)
  AUTHORS   Nakamura,N., Fukuda,H., Kato,A. and Hirose,S.
  TITLE     MARCH-II is a syntaxin-6-binding protein involved in endosomal
            trafficking
  JOURNAL   Mol Biol Cell 16 (4), 1696-1710 (2005)
   PUBMED   15689499
  REMARK    GeneRIF: Depletion of MARCH-II by small interfering RNA perturbed
            the trans-Golgi network (TGN) localization of syntaxin 6 and
            TGN38/46
REFERENCE   10 (residues 1 to 246)
  AUTHORS   Bartee,E., Mansouri,M., Hovey Nerenberg,B.T., Gouveia,K. and
            Fruh,K.
  TITLE     Downregulation of major histocompatibility complex class I by human
            ubiquitin ligases related to viral immune evasion proteins
  JOURNAL   J Virol 78 (3), 1109-1120 (2004)
   PUBMED   14722266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC136469.2 and BC032624.1.
            
            Summary: MARCH2 is a member of the MARCH family of membrane-bound
            E3 ubiquitin ligases (EC 6.3.2.19). MARCH enzymes add ubiquitin
            (see MIM 191339) to target lysines in substrate proteins, thereby
            signaling their vesicular transport between membrane compartments.
            MARCH2 reduces surface accumulation of several glycoproteins and
            appears to regulate early endosome-to-trans-Golgi network (TGN)
            trafficking (Bartee et al., 2004 [PubMed 14722266]; Nakamura et
            al., 2005 [PubMed 15689499]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (7) differs in the 5' UTR compared
            to variant 4. Variants 1, 2, and 4-7 all encode the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032624.1, SRR3476690.512676.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..246
                     /product="E3 ubiquitin-protein ligase MARCHF2 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="membrane-associated RING-CH protein II;
                     membrane-associated ring finger (C3HC4) 2, E3 ubiquitin
                     protein ligase; membrane associated ring finger 2; E3
                     ubiquitin-protein ligase MARCH2; RING finger protein 172;
                     membrane-associated RING finger protein 2; RING-type E3
                     ubiquitin transferase MARCHF2; E3 ubiquitin-protein ligase
                     MARCHF2; RING-type E3 ubiquitin transferase MARCH2"
                     /calculated_mol_wt=26864
     Region          56..116
                     /region_name="Required for inhibition of HIV-1 virus
                     production and VSV G protein expression.
                     /evidence=ECO:0000269|PubMed:29573664"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0N8.1)"
     Region          62..113
                     /region_name="RING_CH-C4HC3_MARCH2"
                     /note="RING-CH finger, H2 subclass (C4HC3-type), found in
                     membrane-associated RING-CH2 (MARCH2); cd16808"
                     /db_xref="CDD:319722"
     Region          121..246
                     /region_name="Required for interaction with IKBKG.
                     /evidence=ECO:0000269|PubMed:32935379"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0N8.1)"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0N8.1)"
     Site            175..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0N8.1)"
     CDS             1..246
                     /gene="MARCHF2"
                     /gene_synonym="HSPC240; MARCH-II; MARCH2; RNF172"
                     /coded_by="NM_001369779.1:509..1249"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS12202.1"
                     /db_xref="GeneID:51257"
                     /db_xref="HGNC:HGNC:28038"
                     /db_xref="MIM:613332"
ORIGIN      
        1 mttgdcchlp gslcdcsgsp afskvveatg lgppqyvaqv tsrdgrllst viraldtpsd
       61 gpfcricheg angecllspc gctgtlgavh ksclekwlss sntsycelch tefavekrpr
      121 pltewlkdpg prtekrtlcc dmvcflfitp laaisgwlcl rgaqdhlrlh sqleavglia
      181 ltialftiyv lwtlvsfryh cqlysewrkt nqkvrlkire adspegpqhs plaagllkkv
      241 aeetpv
//
LOCUS       NP_001094058            1191 aa            linear   PRI 27-APR-2025
DEFINITION  roquin-2 isoform 1 [Homo sapiens].
ACCESSION   NP_001094058 XP_005252112
VERSION     NP_001094058.1
DBSOURCE    REFSEQ: accession NM_001100588.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1191)
  AUTHORS   Zhou,M., Lu,W., Li,B., Yuan,X., Liu,M., Han,J., Liu,X. and Li,A.
  TITLE     Roquin2 suppresses breast cancer progression by inhibiting tumor
            angiogenesis via selectively destabilizing proangiogenic factors
            mRNA
  JOURNAL   Int J Biol Sci 17 (11), 2884-2898 (2021)
   PUBMED   34345214
  REMARK    GeneRIF: Roquin2 suppresses breast cancer progression by inhibiting
            tumor angiogenesis via selectively destabilizing proangiogenic
            factors mRNA.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1191)
  AUTHORS   Choi,J., Lee,K., Ingvarsdottir,K., Bonasio,R., Saraf,A.,
            Florens,L., Washburn,M.P., Tadros,S., Green,M.R. and Busino,L.
  TITLE     Loss of KLHL6 promotes diffuse large B-cell lymphoma growth and
            survival by stabilizing the mRNA decay factor roquin2
  JOURNAL   Nat Cell Biol 20 (5), 586-596 (2018)
   PUBMED   29695787
  REMARK    GeneRIF: Loss of KLHL6 promotes diffuse large B-cell lymphoma
            growth and survival by stabilizing the mRNA decay factor roquin2.
REFERENCE   3  (residues 1 to 1191)
  AUTHORS   Zhang,Q., Fan,L., Hou,F., Dong,A., Wang,Y.X. and Tong,Y.
  TITLE     New Insights into the RNA-Binding and E3 Ubiquitin Ligase
            Activities of Roquins
  JOURNAL   Sci Rep 5, 15660 (2015)
   PUBMED   26489670
  REMARK    GeneRIF: Crystal structures, small-angle X-ray scattering, and E2
            profiling revealed that while the two paralogs are highly
            homologous, RC3H2 and RC3H1 are different in their structures and
            functions.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1191)
  AUTHORS   Sakurai,S., Ohto,U. and Shimizu,T.
  TITLE     Structure of human Roquin-2 and its complex with constitutive-decay
            element RNA
  JOURNAL   Acta Crystallogr F Struct Biol Commun 71 (Pt 8), 1048-1054 (2015)
   PUBMED   26249698
  REMARK    GeneRIF: Roquin-1 and roquin-2 proteins function redundantly in
            mRNA degradation.
REFERENCE   5  (residues 1 to 1191)
  AUTHORS   Maruyama,T., Araki,T., Kawarazaki,Y., Naguro,I., Heynen,S.,
            Aza-Blanc,P., Ronai,Z., Matsuzawa,A. and Ichijo,H.
  TITLE     Roquin-2 promotes ubiquitin-mediated degradation of ASK1 to
            regulate stress responses
  JOURNAL   Sci Signal 7 (309), ra8 (2014)
   PUBMED   24448648
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1191)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 1191)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 1191)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 1191)
  AUTHORS   Siess,D.C., Vedder,C.T., Merkens,L.S., Tanaka,T., Freed,A.C.,
            McCoy,S.L., Heinrich,M.C., Deffebach,M.E., Bennett,R.M. and
            Hefeneider,S.H.
  TITLE     A human gene coding for a membrane-associated nucleic acid-binding
            protein
  JOURNAL   J Biol Chem 275 (43), 33655-33662 (2000)
   PUBMED   10938276
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007066.4 and AL359512.15.
            
            On Aug 31, 2013 this sequence version replaced XP_005252112.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.33863.1,
                                           SRR11853567.30819.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357244.7/ ENSP00000349783.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.2"
     Protein         1..1191
                     /product="roquin-2 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="membrane associated DNA binding protein; roquin-2;
                     ring finger and CCCH-type zinc finger domains 2; ring
                     finger and CCCH-type zinc finger domain-containing protein
                     2; RING finger protein 164; membrane-associated nucleic
                     acid-binding protein; RING-type E3 ubiquitin transferase
                     Roquin-2"
                     /calculated_mol_wt=131538
     Region          7..55
                     /region_name="mRING-HC-C3HC3D_Roquin2"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in Roquin-2; cd16782"
                     /db_xref="CDD:438437"
     Region          91..170
                     /region_name="HEPN-N.
                     /evidence=ECO:0000269|PubMed:26489670"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBD1.2)"
     Region          171..325
                     /region_name="ROQ. /evidence=ECO:0000269|PubMed:26249698"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBD1.2)"
     Region          268..323
                     /region_name="ROQ_II"
                     /note="Roquin II domain; pfam18386"
                     /db_xref="CDD:436456"
     Region          326..396
                     /region_name="HEPN-C.
                     /evidence=ECO:0000269|PubMed:26489670"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBD1.2)"
     Region          <393..>513
                     /region_name="CTH1"
                     /note="CCCH-type Zn-finger protein [General function
                     prediction only]; COG5063"
                     /db_xref="CDD:227395"
     Region          411..437
                     /region_name="zf-CCCH"
                     /note="Zinc finger C-x8-C-x5-C-x3-H type (and similar);
                     pfam00642"
                     /db_xref="CDD:459885"
     Site            509
                     /site_type="cleavage"
                     /note="Cleavage, by MALT1.
                     /evidence=ECO:0000250|UniProtKB:Q4VGL6; propagated from
                     UniProtKB/Swiss-Prot (Q9HBD1.2)"
     Region          528..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBD1.2)"
     Region          <536..798
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9HBD1.2)"
     Site            585
                     /site_type="cleavage"
                     /note="Cleavage, by MALT1.
                     /evidence=ECO:0000250|UniProtKB:Q4VGL6; propagated from
                     UniProtKB/Swiss-Prot (Q9HBD1.2)"
     Region          644..680
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBD1.2)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9HBD1.2)"
     Site            983
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HBD1.2)"
     Site            1119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HBD1.2)"
     CDS             1..1191
                     /gene="RC3H2"
                     /gene_synonym="MNAB; RNF164"
                     /coded_by="NM_001100588.3:318..3893"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43874.1"
                     /db_xref="GeneID:54542"
                     /db_xref="HGNC:HGNC:21461"
                     /db_xref="MIM:615231"
ORIGIN      
        1 mpvqaaqwte flscpicyne fdenvhkpis lgcshtvckt clnklhrkac pfdqtaintd
       61 idvlpvnfal lqlvgaqvpd hqsiklsnlg enkhyevakk cvedlalylk plsggkgvas
      121 lnqsalsrpm qrklvtlvnc qlveeegrvr amraarslge rtvtelilqh qnpqqlsanl
      181 waavrargcq flgpamqeea lklvllaled gsalsrkvlv lfvvqrlepr fpqasktsig
      241 hvvqllyras cfkvtkrded sslmqlkeef rsyealrreh daqivhiame aglrispeqw
      301 ssllygdlah kshmqsiidk lqspesfaks vqeltivlqr tgdpanlnrl rphlellani
      361 dpnpdavspt weqlenamva vktvvhglvd fiqnysrkgh etpqpqpnsk yktsmcrdlr
      421 qqggcprgtn ctfahsqeel ekyrlrnkki natvrtfpll nkvgvnntvt ttagnvisvi
      481 gstettgkiv pstngisnae nsvsqlisrs tdstlralet vkkvgkvgan gqnaagpsad
      541 svtenkigsp pktpvsnvaa tsagpsnvgt elnsvpqkss pfltrvpvyp phseniqyfq
      601 dprtqipfev pqypqtgyyp ppptvpagva pcvprfvrsn nvpesslppa smpyadhyst
      661 fsprdrmnss pyqppppqpy gpvppvpsgm yapvydsrri wrppmyqrdd iirsnslppm
      721 dvmhssvyqt slrerynsld gyysvacqpp seprttvplp repcghlkts ceeqirrkpd
      781 qwaqyhtqka plvsstlpva tqsptppspl fsvdfradfs esvsgtkfee dhlshyspws
      841 cgtigscina idsepkdvia nsnavlmdld sgdvkrrvhl fetqrrtkee dpiipfsdgp
      901 iiskwgaisr ssrtgyhttd pvqatasqgs atkpisvsdy vpyvnavdsr wssygneats
      961 sahyverdrf ivtdlsghrk hsstgdllsl elqqaksnsl llqreanala mqqkwnslde
     1021 grhltlnlls keielrngel qsdytedatd tkpdrdiele lsaldtdepd gqsepieeil
     1081 diqlgissqn dqllngmave nghpvqqhqk eppkqkkqsl gedhvileeq ktilpvtscf
     1141 sqplpvsisn asclpittsv sagnlilkth vmsedkndfl kpvangkmvn s
//
LOCUS       NP_060817                200 aa            linear   PRI 27-APR-2025
DEFINITION  AP-5 complex subunit sigma-1 [Homo sapiens].
ACCESSION   NP_060817
VERSION     NP_060817.1
DBSOURCE    REFSEQ: accession NM_018347.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Hirst,J., Barlow,L.D., Francisco,G.C., Sahlender,D.A., Seaman,M.N.,
            Dacks,J.B. and Robinson,M.S.
  TITLE     The fifth adaptor protein complex
  JOURNAL   PLoS Biol 9 (10), e1001170 (2011)
   PUBMED   22022230
  REMARK    Erratum:[PLoS Biol. 2012 Mar;10(3). doi:
            10.1371/annotation/89dff893-c156-44bb-a731-bfcc91843583]
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Slabicki,M., Theis,M., Krastev,D.B., Samsonov,S., Mundwiller,E.,
            Junqueira,M., Paszkowski-Rogacz,M., Teyra,J., Heninger,A.K.,
            Poser,I., Prieur,F., Truchetto,J., Confavreux,C., Marelli,C.,
            Durr,A., Camdessanche,J.P., Brice,A., Shevchenko,A.,
            Pisabarro,M.T., Stevanin,G. and Buchholz,F.
  TITLE     A genome-scale DNA repair RNAi screen identifies SPG48 as a novel
            gene associated with hereditary spastic paraplegia
  JOURNAL   PLoS Biol 8 (6), e1000408 (2010)
   PUBMED   20613862
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA253969.1, BC043344.1, AK002030.1 and AL109804.41.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1, 2, and 3 encode the same
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.400910.1, AK002030.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000615891.2/ ENSP00000481750.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..200
                     /product="AP-5 complex subunit sigma-1"
                     /note="protein C20orf29; sigma5; adapter-related protein
                     complex 5 sigma subunit; adaptor-related protein complex 5
                     sigma subunit; adaptor related protein complex 5 sigma 1
                     subunit"
                     /calculated_mol_wt=22391
     Region          1..195
                     /region_name="AP-5_subunit_s1"
                     /note="AP-5 complex subunit sigma-1; pfam15001"
                     /db_xref="CDD:434380"
     CDS             1..200
                     /gene="AP5S1"
                     /gene_synonym="C20orf29"
                     /coded_by="NM_018347.3:229..831"
                     /db_xref="CCDS:CCDS13070.1"
                     /db_xref="GeneID:55317"
                     /db_xref="HGNC:HGNC:15875"
                     /db_xref="MIM:614824"
ORIGIN      
        1 mvhaflihtl rapntedtgl crvlyscvfg aekspddprp hgaerdrllr keqilavarq
       61 vesmcrlqqq asgrppmdlq pqssdeqvpl heaprgafrl aaenpfqepr tvvwlgvlsl
      121 gfalvldahe nlllaegtlr lltrllldhl rllapstsll lradriegil trflphgqll
      181 flndqfvqgl ekefsaawpr
//
LOCUS       NP_689625                529 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 572 [Homo sapiens].
ACCESSION   NP_689625
VERSION     NP_689625.2
DBSOURCE    REFSEQ: accession NM_152412.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009908.13, DB093007.1, BC130517.1 and AK095321.1.
            
            On Feb 12, 2009 this sequence version replaced NP_689625.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX537876.1, AK095321.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319286.6/ ENSP00000319305.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..529
                     /product="zinc finger protein 572"
                     /calculated_mol_wt=61107
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3I7.1)"
     Region          122..494
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          134..154
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(134,137,150,154)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          162..182
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(162,165,178,182)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          190..210
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(190,193,206,210)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          218..238
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(218,221,234,238)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(223,225,227,229..230,233..234,237,251,253,257..258,
                     261..262,265,279,281,283,285..286,289..290,293)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          246..266
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          274..294
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          302..322
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          330..350
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          386..406
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(386,389,402,406)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(391,393,395,397..398,401..402,405,419,421,425..426,
                     429..430,433,447,449,451,453..454,457..458,461)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          414..434
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          442..462
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          470..490
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..529
                     /gene="ZNF572"
                     /coded_by="NM_152412.3:158..1747"
                     /db_xref="CCDS:CCDS6354.1"
                     /db_xref="GeneID:137209"
                     /db_xref="HGNC:HGNC:26758"
ORIGIN      
        1 meqekkllvs dsnsfmeres lkspftgdts mnnletvhhn nskadklkek psewskrhrp
       61 qhykhedake mpltwvqdei wchdsyesdg ksenwgnfia keeekpnhqe wdsgehtnac
      121 vqqnssfvdr pykcsecwks fsnsshlrth qrthsgekpy kcsecakcfc nsshliqhlr
      181 mhtgekpyqc gecgksfsnt shliiherth tgekpykcpe cgkrfssssh liqhhrshtg
      241 ekpyecsvcg kgfshsyvli ehqrthtgek pykcpdcgks fsqssslirh qrthtgekpy
      301 kcleceksfg cnstlikhqr ihtgekpyqc pecgknfsrs snlithqkmh tgeksyesse
      361 yeeslgqncn vieecriqlg ekpyrccecg ksfglsshli rhqrthtgek pyrcsecwkt
      421 fsqsstlvih qrthtgekpy kcpdcgesfs qsfnlirhrr thigekpykc tscekcfsrs
      481 aylsqhrkih vekpfespdv gdfphewtwk ncsgempfis sfsvsnsss
//
LOCUS       NP_079114                743 aa            linear   PRI 27-APR-2025
DEFINITION  threonine synthase-like 1 [Homo sapiens].
ACCESSION   NP_079114
VERSION     NP_079114.3
DBSOURCE    REFSEQ: accession NM_024838.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Donini,S., Percudani,R., Credali,A., Montanini,B., Sartori,A. and
            Peracchi,A.
  TITLE     A threonine synthase homolog from a mammalian genome
  JOURNAL   Biochem Biophys Res Commun 350 (4), 922-928 (2006)
   PUBMED   17034760
REFERENCE   3  (residues 1 to 743)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 743)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA496769.1, AK125249.1, BX647989.1 and AK025655.1.
            
            On Jul 25, 2007 this sequence version replaced NP_079114.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.187176.1,
                                           SRR1660807.244171.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376356.5/ ENSP00000365534.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..743
                     /product="threonine synthase-like 1"
                     /calculated_mol_wt=82940
     Region          <31..>93
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
     Region          64..221
                     /region_name="SKI"
                     /note="Shikimate kinase; pfam01202"
                     /db_xref="CDD:426122"
     Site            order(65..70,164,171,209)
                     /site_type="other"
                     /note="ADP binding site [chemical binding]"
                     /db_xref="CDD:238260"
     Site            order(69,85,87)
                     /site_type="other"
                     /note="magnesium binding site [ion binding]"
                     /db_xref="CDD:238260"
     Site            order(87,112,115,132..134,189)
                     /site_type="active"
                     /note="putative shikimate binding site [active]"
                     /db_xref="CDD:238260"
     Region          230..733
                     /region_name="Thr-synth_2"
                     /note="Threonine synthase catalyzes the final step of
                     threonine biosynthesis. The conversion of
                     O-phosphohomoserine into threonine and inorganic phosphate
                     is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD
                     includes members from higher plants, cyanobacteria;
                     cd01560"
                     /db_xref="CDD:107203"
     Site            281
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8IYQ7.2)"
     Site            order(351,509..510,665)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107203"
     Site            351
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107203"
     CDS             1..743
                     /gene="THNSL1"
                     /gene_synonym="TSH1"
                     /coded_by="NM_024838.5:297..2528"
                     /db_xref="CCDS:CCDS7147.1"
                     /db_xref="GeneID:79896"
                     /db_xref="HGNC:HGNC:26160"
                     /db_xref="MIM:611260"
ORIGIN      
        1 mlhfnrchhl kkitqkcfss ihvktdkhaq rflsrtfala elrkswysth slvgdkniil
       61 mgppgagktt vgriigqklg ccvidvdddi lektwnmsvs eklqdvgneq fleeegkavl
      121 nfsasgsvis ltgsnpmhda smwhlkkngi ivyldvplld licrlklmkt drivgqnsgt
      181 smkdllkfrr qyykkwydar vfcesgaspe evadkvlnai kryqdvdset fistrhvwpe
      241 dceqkvsakf fseaviegla sdgglfvpak efpklscgew kslvgatyve raqillerci
      301 hpadipaarl gemietayge nfacskiapv rhlsgnqfil elfhgptgsf kdlslqlmph
      361 ifahcippsc nymilvatsg dtgsavlngf srlnkndkqr iavvaffpen gvsdfqkaqi
      421 igsqrengwa vgvesdfdfc qtaikrifnd sdftgfltve ygtilssans inwgrllpqv
      481 vyhasayldl vsqgfisfgs pvdvciptgn fgnilaavya kmmgipirkf icasnqnhvl
      541 tdfiktghyd lrerklaqtf spsidilkss nlerhlhlma nkdgqlmtel fnrlesqhhf
      601 qiekalvekl qqdfvadwcs egeclaains tyntsgyild phtavakvva drvqdktcpv
      661 iisstahysk fapaimqalk ikeinetsss qlyllgsyna lpplhealle rtkqqekmey
      721 qvcaadmnvl kshveqlvqn qfi
//
LOCUS       NP_003620                461 aa            linear   PRI 27-APR-2025
DEFINITION  phosphatidylinositol 3-kinase regulatory subunit gamma isoform 1
            [Homo sapiens].
ACCESSION   NP_003620
VERSION     NP_003620.3
DBSOURCE    REFSEQ: accession NM_003629.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Qian,W., Mei,K., Zhu,L., Chu,Y., Lv,J. and Yun,C.
  TITLE     Circ_0044235 regulates the development of osteoarthritis by the
            modulation of miR-375/PIK3R3 axis
  JOURNAL   J Orthop Surg Res 19 (1), 241 (2024)
   PUBMED   38622668
  REMARK    GeneRIF: Circ_0044235 regulates the development of osteoarthritis
            by the modulation of miR-375/PIK3R3 axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Lee,H., Zhuang,L. and Gan,B.
  TITLE     VHL governs m6A modification and PIK3R3 mRNA stability in clear
            cell renal cell carcinomas
  JOURNAL   J Clin Invest 134 (8), e179560 (2024)
   PUBMED   38618953
  REMARK    GeneRIF: VHL governs m6A modification and PIK3R3 mRNA stability in
            clear cell renal cell carcinomas.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Li,Z., Dai,R., Chen,M., Huang,L., Zhu,K., Li,M., Zhu,W., Li,Y.,
            Xie,N., Li,J., Wang,L., Lan,F. and Cao,C.M.
  TITLE     p55gamma degrades RIP3 via MG53 to suppress ischaemia-induced
            myocardial necroptosis and mediates cardioprotection of
            preconditioning
  JOURNAL   Cardiovasc Res 119 (14), 2421-2440 (2023)
   PUBMED   37527538
  REMARK    GeneRIF: p55gamma degrades RIP3 via MG53 to suppress
            ischaemia-induced myocardial necroptosis and mediates
            cardioprotection of preconditioning.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Lin,W., Wang,K., Mo,J., Wang,L., Song,Z., Jiang,H., Wang,C. and
            Jin,C.
  TITLE     PIK3R3 is upregulated in liver cancer and activates Akt signaling
            to control cancer growth by regulation of CDKN1C and SMC1A
  JOURNAL   Cancer Med 12 (13), 14413-14425 (2023)
   PUBMED   37212524
  REMARK    GeneRIF: PIK3R3 is upregulated in liver cancer and activates Akt
            signaling to control cancer growth by regulation of CDKN1C and
            SMC1A.
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Wang,B., Min,W., Zhang,W., Liu,Q., Guo,X., Zhan,J., Lei,M., Zan,Y.,
            Ma,Q. and Ma,H.
  TITLE     PIK3R3 Missense and NOTCH2 Synonymous Single Nucleotide
            Polymorphisms Are Associated with Liver Cancer
  JOURNAL   Dig Dis 41 (3), 458-467 (2023)
   PUBMED   36535266
  REMARK    GeneRIF: PIK3R3 Missense and NOTCH2 Synonymous Single Nucleotide
            Polymorphisms Are Associated with Liver Cancer.
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Dey,B.R., Furlanetto,R.W. and Nissley,S.P.
  TITLE     Cloning of human p55 gamma, a regulatory subunit of
            phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen
            with the insulin-like growth factor-I receptor
  JOURNAL   Gene 209 (1-2), 175-183 (1998)
   PUBMED   9524259
  REMARK    Erratum:[Gene 1998 May 28;212(1):155]
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Mothe,I., Delahaye,L., Filloux,C., Pons,S., White,M.F. and Van
            Obberghen,E.
  TITLE     Interaction of wild type and dominant-negative p55PIK regulatory
            subunit of phosphatidylinositol 3-kinase with insulin-like growth
            factor-1 signaling proteins
  JOURNAL   Mol Endocrinol 11 (13), 1911-1923 (1997)
   PUBMED   9415396
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Takahashi-Tezuka,M., Hibi,M., Fujitani,Y., Fukada,T., Yamaguchi,T.
            and Hirano,T.
  TITLE     Tec tyrosine kinase links the cytokine receptors to PI-3 kinase
            probably through JAK
  JOURNAL   Oncogene 14 (19), 2273-2282 (1997)
   PUBMED   9178903
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Tuscano,J.M., Engel,P., Tedder,T.F., Agarwal,A. and Kehrl,J.H.
  TITLE     Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl
            inositol-3 kinase in signal transduction via the human B lymphocyte
            antigen CD22
  JOURNAL   Eur J Immunol 26 (6), 1246-1252 (1996)
   PUBMED   8647200
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Pons,S., Asano,T., Glasheen,E., Miralpeix,M., Zhang,Y.,
            Fisher,T.L., Myers,M.G. Jr., Sun,X.J. and White,M.F.
  TITLE     The structure and function of p55PIK reveal a new regulatory
            subunit for phosphatidylinositol 3-kinase
  JOURNAL   Mol Cell Biol 15 (8), 4453-4465 (1995)
   PUBMED   7542745
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC021622.1, BC094768.1 and
            U90907.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 2, 2008 this sequence version replaced NP_003620.2.
            
            Summary: Phosphatidylinositol 3-kinase (PI3K) phosphorylates
            phosphatidylinositol and similar compounds, which then serve as
            second messengers in growth signaling pathways. PI3K is composed of
            a catalytic and a regulatory subunit. The protein encoded by this
            gene represents a regulatory subunit of PI3K. The encoded protein
            contains two SH2 domains through which it binds activated protein
            tyrosine kinases to regulate their activity. [provided by RefSeq,
            Jun 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749649.1, BC021622.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262741.10/ ENSP00000262741.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..461
                     /product="phosphatidylinositol 3-kinase regulatory subunit
                     gamma isoform 1"
                     /note="phosphatidylinositol 3-kinase, regulatory subunit,
                     polypeptide 3 (p55, gamma); PI3-kinase subunit p55-gamma;
                     PI3K regulatory subunit gamma; PI3-kinase regulatory
                     subunit gamma; ptdIns-3-kinase regulatory subunit
                     p55-gamma; phosphatidylinositol 3-kinase 55 kDa regulatory
                     subunit gamma; phosphoinositide-3-kinase, regulatory
                     subunit 3 (gamma)"
                     /calculated_mol_wt=54317
     Region          59..167
                     /region_name="SH2_nSH2_p85_like"
                     /note="N-terminal Src homology 2 (nSH2) domain found in
                     p85; cd09942"
                     /db_xref="CDD:198195"
     Site            order(72,90,112,114)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198195"
     Site            order(113,140)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198195"
     Region          172..332
                     /region_name="iSH2_PI3K_IA_R"
                     /note="Inter-Src homology 2 (iSH2) helical domain of Class
                     IA Phosphoinositide 3-kinase Regulatory subunits; cl25402"
                     /db_xref="CDD:355389"
     Site            order(195,202,213..215,217..219,221..222,225..226,
                     228..229,232..233,236,252,255..256,259,263,266,292..293,
                     296,299)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:214018"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q64143; propagated from
                     UniProtKB/Swiss-Prot (Q92569.2)"
     Region          351..454
                     /region_name="SH2_cSH2_p85_like"
                     /note="C-terminal Src homology 2 (cSH2) domain found in
                     p85; cd09930"
                     /db_xref="CDD:198184"
     Site            order(365,383,385..386,403,405)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198184"
     Site            order(404,415,437,440,444)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198184"
     CDS             1..461
                     /gene="PIK3R3"
                     /gene_synonym="p55; p55-GAMMA; p55PIK"
                     /coded_by="NM_003629.4:678..2063"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS529.1"
                     /db_xref="GeneID:8503"
                     /db_xref="HGNC:HGNC:8981"
                     /db_xref="MIM:606076"
ORIGIN      
        1 myntvwsmdr ddadwrevmm pystelifyi emdppalppk ppkpmtsavp ngmkdssvsl
       61 qdaewywgdi sreevndklr dmpdgtflvr dastkmqgdy tltlrkggnn klikiyhrdg
      121 kygfsdpltf nsvvelinhy hheslaqynp kldvklmypv sryqqdqlvk ednidavgkk
      181 lqeyhsqyqe kskeydrlye eytrtsqeiq mkrtaieafn etikifeeqc htqeqhskey
      241 ierfrregne keierimmny dklksrlgei hdskmrleqd lknqaldnre idkkmnsikp
      301 dliqlrkird qhlvwlnhkg vrqkrlnvwl giknedaden yfineedenl phydektwfv
      361 edinrvqaed llygkpdgaf liresskkgc yacsvvadge vkhcviysta rgygfaepyn
      421 lysslkelvl hyqqtslvqh ndslnvrlay pvhaqmpslc r
//
LOCUS       NP_000205               1218 aa            linear   PRI 27-APR-2025
DEFINITION  protein jagged-1 precursor [Homo sapiens].
ACCESSION   NP_000205
VERSION     NP_000205.1
DBSOURCE    REFSEQ: accession NM_000214.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1218)
  AUTHORS   Keefer-Jacques,E., Valente,N., Jacko,A.M., Matwijec,G., Reese,A.,
            Tekriwal,A., Loomes,K.M., Spinner,N.B. and Gilbert,M.A.
  TITLE     Investigation of cryptic JAG1 splice variants as a cause of
            Alagille syndrome and performance evaluation of splice predictor
            tools
  JOURNAL   HGG Adv 5 (4), 100351 (2024)
   PUBMED   39244638
  REMARK    GeneRIF: Investigation of cryptic JAG1 splice variants as a cause
            of Alagille syndrome and performance evaluation of splice predictor
            tools.
REFERENCE   2  (residues 1 to 1218)
  AUTHORS   Wu,X., Zhu,H., Liu,J., Ouyang,S., Lyu,Z., Jin,Y., Chen,X. and
            Meng,Q.
  TITLE     Jagged1-Notch1 Signaling Pathway Induces M1 Microglia to Disrupt
            the Barrier Function of Retinal Microvascular Endothelial Cells
  JOURNAL   Curr Eye Res 49 (10), 1098-1106 (2024)
   PUBMED   38783634
  REMARK    GeneRIF: Jagged1-Notch1 Signaling Pathway Induces M1 Microglia to
            Disrupt the Barrier Function of Retinal Microvascular Endothelial
            Cells.
REFERENCE   3  (residues 1 to 1218)
  AUTHORS   Xiao,X., Wang,W., Guo,C., Wu,J., Zhang,S., Shi,H., Kwon,S., Chen,J.
            and Dong,Z.
  TITLE     Hypermethylation leads to the loss of HOXA5, resulting in JAG1
            expression and NOTCH signaling contributing to kidney fibrosis
  JOURNAL   Kidney Int 106 (1), 98-114 (2024)
   PUBMED   38521405
  REMARK    GeneRIF: Hypermethylation leads to the loss of HOXA5, resulting in
            JAG1 expression and NOTCH signaling contributing to kidney
            fibrosis.
REFERENCE   4  (residues 1 to 1218)
  AUTHORS   Huang,H., Jiang,Y., Liu,J., Luo,D., Yuan,J., Mu,R., Yu,X., Sun,D.,
            Lin,J., Chen,Q., Li,X., Jiang,M., Xu,J., Chu,B., Yin,C., Zhang,L.,
            Ye,Y., Cao,B., Wang,Q. and Zhang,Y.
  TITLE     Jag1/2 maintain esophageal homeostasis and suppress foregut
            tumorigenesis by restricting the basal progenitor cell pool
  JOURNAL   Nat Commun 15 (1), 4124 (2024)
   PUBMED   38750026
  REMARK    GeneRIF: Jag1/2 maintain esophageal homeostasis and suppress
            foregut tumorigenesis by restricting the basal progenitor cell
            pool.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1218)
  AUTHORS   Feng,X., Ping,J., Gao,S., Han,D., Song,W., Li,X., Tao,Y. and
            Wang,L.
  TITLE     Novel JAG1 variants leading to Alagille syndrome in two Chinese
            cases
  JOURNAL   Sci Rep 14 (1), 1812 (2024)
   PUBMED   38245625
  REMARK    GeneRIF: Novel JAG1 variants leading to Alagille syndrome in two
            Chinese cases.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1218)
  AUTHORS   Zimrin,A.B., Pepper,M.S., McMahon,G.A., Nguyen,F., Montesano,R. and
            Maciag,T.
  TITLE     An antisense oligonucleotide to the notch ligand jagged enhances
            fibroblast growth factor-induced angiogenesis in vitro
  JOURNAL   J Biol Chem 271 (51), 32499-32502 (1996)
   PUBMED   8955070
REFERENCE   7  (residues 1 to 1218)
  AUTHORS   Genini,M., Schwalbe,P., Scholl,F.A. and Schafer,B.W.
  TITLE     Isolation of genes differentially expressed in human primary
            myoblasts and embryonal rhabdomyosarcoma
  JOURNAL   Int J Cancer 66 (4), 571-577 (1996)
   PUBMED   8635876
REFERENCE   8  (residues 1 to 1218)
  AUTHORS   Lindsell,C.E., Boulter,J., diSibio,G., Gossler,A. and Weinmaster,G.
  TITLE     Expression patterns of Jagged, Delta1, Notch1, Notch2, and Notch3
            genes identify ligand-receptor pairs that may function in neural
            development
  JOURNAL   Mol Cell Neurosci 8 (1), 14-27 (1996)
   PUBMED   8923452
REFERENCE   9  (residues 1 to 1218)
  AUTHORS   Lindsell,C.E., Shawber,C.J., Boulter,J. and Weinmaster,G.
  TITLE     Jagged: a mammalian ligand that activates Notch1
  JOURNAL   Cell 80 (6), 909-917 (1995)
   PUBMED   7697721
REFERENCE   10 (residues 1 to 1218)
  AUTHORS   Spinner,N.B., Loomes,K.M., Krantz,I.D. and Gilbert,M.A.
  TITLE     Alagille Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301450
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF056748.1, U73936.1,
            AF028593.1, AA933912.1 and AI268246.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The jagged 1 protein encoded by JAG1 is the human homolog
            of the Drosophilia jagged protein. Human jagged 1 is the ligand for
            the receptor notch 1, the latter is involved in signaling
            processes. Mutations that alter the jagged 1 protein cause Alagille
            syndrome. Jagged 1 signalling through notch 1 has also been shown
            to play a role in hematopoiesis. [provided by RefSeq, Nov 2019].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF003837.1, BC098393.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254958.10/ ENSP00000254958.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.2"
     Protein         1..1218
                     /product="protein jagged-1 precursor"
                     /note="protein jagged-1"
                     /calculated_mol_wt=130349
     sig_peptide     1..33
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78504.3)"
                     /calculated_mol_wt=3468
     Region          32..185
                     /region_name="MNNL"
                     /note="N terminus of Notch ligand C2-like domain;
                     pfam07657"
                     /db_xref="CDD:462222"
     mat_peptide     34..1218
                     /product="Protein jagged-1. /id=PRO_0000007625"
                     /note="propagated from UniProtKB/Swiss-Prot (P78504.3)"
                     /calculated_mol_wt=130349
     Site            143
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78504.3)"
     Region          167..229
                     /region_name="DSL"
                     /note="delta serrate ligand; smart00051"
                     /db_xref="CDD:128366"
     Region          199..207
                     /region_name="Important for interaction with NOTCH1.
                     /evidence=ECO:0000269|PubMed:18660822"
                     /note="propagated from UniProtKB/Swiss-Prot (P78504.3)"
     Site            217
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78504.3)"
     Region          296..334
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(296,299,314)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          340..370
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          374..410
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(374,377,391)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78504.3)"
     Region          412..447
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(412,415,429)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          450..485
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(450,453,466)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          487..523
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(487,490,504)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          525..560
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(525,528,542)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            559
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78504.3)"
     Region          629..665
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(629,632,646)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          667..702
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(667,670,684)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            745
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78504.3)"
     Region          748..777
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          782..817
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(782,785,799)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          820..856
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(820,823,837)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          863..930
                     /region_name="VWC_out"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00215"
                     /db_xref="CDD:214565"
     Site            960
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78504.3)"
     Site            991
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78504.3)"
     Site            1045
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78504.3)"
     Site            1064
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78504.3)"
     Site            1068..1093
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P78504.3)"
     Region          1152..1218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78504.3)"
     CDS             1..1218
                     /gene="JAG1"
                     /gene_synonym="AGS; AGS1; AHD; AWS; CD339; CMT2HH; DCHE;
                     HJ1; JAGL1"
                     /coded_by="NM_000214.3:470..4126"
                     /db_xref="CCDS:CCDS13112.1"
                     /db_xref="GeneID:182"
                     /db_xref="HGNC:HGNC:6188"
                     /db_xref="MIM:601920"
ORIGIN      
        1 mrsprtrgrs grplslllal lcalrakvcg asgqfeleil smqnvngelq ngnccggarn
       61 pgdrkctrde cdtyfkvclk eyqsrvtagg pcsfgsgstp viggntfnlk asrgndrnri
      121 vlpfsfawpr sytllveawd ssndtvqpds iiekashsgm inpsrqwqtl kqntgvahfe
      181 yqirvtcddy yygfgcnkfc rprddffghy acdqngnktc megwmgpecn raicrqgcsp
      241 khgscklpgd crcqygwqgl ycdkciphpg cvhgicnepw qclcetnwgg qlcdkdlnyc
      301 gthqpclngg tcsntgpdky qcscpegysg pnceiaehac lsdpchnrgs cketslgfec
      361 ecspgwtgpt cstniddcsp nncshggtcq dlvngfkcvc ppqwtgktcq ldaneceakp
      421 cvnakscknl iasyycdclp gwmgqncdin indclgqcqn dascrdlvng yrcicppgya
      481 gdhcerdide casnpclngg hcqneinrfq clcptgfsgn lcqldidyce pnpcqngaqc
      541 ynrasdyfck cpedyegknc shlkdhcrtt pcevidsctv amasndtpeg vryissnvcg
      601 phgkcksqsg gkftcdcnkg ftgtycheni ndcesnpcrn ggtcidgvns ykcicsdgwe
      661 gaycetnind csqnpchngg tcrdlvndfy cdckngwkgk tchsrdsqcd eatcnnggtc
      721 ydegdafkcm cpggwegttc niarnssclp npchnggtcv vngesftcvc kegwegpica
      781 qntndcsphp cynsgtcvdg dnwyrcecap gfagpdcrin inecqsspca fgatcvdein
      841 gyrcvcppgh sgakcqevsg rpcitmgsvi pdgakwdddc ntcqclngri acskvwcgpr
      901 pcllhkghse cpsgqscipi lddqcfvhpc tgvgecrsss lqpvktkcts dsyyqdncan
      961 itftfnkemm spglttehic selrnlnilk nvsaeysiyi acepspsann eihvaisaed
     1021 irddgnpike itdkiidlvs krdgnsslia avaevrvqrr plknrtdflv pllssvltva
     1081 wicclvtafy wclrkrrkpg shthsasedn ttnnvreqln qiknpiekhg antvpikdye
     1141 nknskmskir thnseveedd mdkhqqkarf akqpaytlvd reekppngtp tkhpnwtnkq
     1201 dnrdlesaqs lnrmeyiv
//
LOCUS       NP_001356535             527 aa            linear   PRI 27-APR-2025
DEFINITION  suppressor of tumorigenicity 7 protein isoform 10 [Homo sapiens].
ACCESSION   NP_001356535
VERSION     NP_001356535.1
DBSOURCE    REFSEQ: accession NM_001369606.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Liu,H., Lu,W., He,H., Wu,J., Zhang,C., Gong,H. and Yang,C.
  TITLE     Inflammation-dependent overexpression of c-Myc enhances CRL4DCAF4
            E3 ligase activity and promotes ubiquitination of ST7 in
            colitis-associated cancer
  JOURNAL   J Pathol 248 (4), 464-475 (2019)
   PUBMED   30945288
  REMARK    GeneRIF: Inflammation-dependent overexpression of c-Myc enhances
            CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7
            in colitis-associated cancer.
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Yan,F., Alinari,L., Lustberg,M.E., Martin,L.K.,
            Cordero-Nieves,H.M., Banasavadi-Siddegowda,Y., Virk,S.,
            Barnholtz-Sloan,J., Bell,E.H., Wojton,J., Jacob,N.K.,
            Chakravarti,A., Nowicki,M.O., Wu,X., Lapalombella,R., Datta,J.,
            Yu,B., Gordon,K., Haseley,A., Patton,J.T., Smith,P.L., Ryu,J.,
            Zhang,X., Mo,X., Marcucci,G., Nuovo,G., Kwon,C.H., Byrd,J.C.,
            Chiocca,E.A., Li,C., Sif,S., Jacob,S., Lawler,S., Kaur,B. and
            Baiocchi,R.A.
  TITLE     Genetic validation of the protein arginine methyltransferase PRMT5
            as a candidate therapeutic target in glioblastoma
  JOURNAL   Cancer Res 74 (6), 1752-1765 (2014)
   PUBMED   24453002
  REMARK    GeneRIF: The tumor suppressor ST7 is a key gene silenced by PRMT5.
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Hu,L., Wu,C., Zhao,X., Heist,R., Su,L., Zhao,Y., Han,B., Cao,S.,
            Chu,M., Dai,J., Dong,J., Shu,Y., Xu,L., Chen,Y., Wang,Y., Lu,F.,
            Jiang,Y., Yu,D., Chen,H., Tan,W., Ma,H., Chen,J., Jin,G., Wu,T.,
            Lu,D., Christiani,D.C., Lin,D., Hu,Z. and Shen,H.
  TITLE     Genome-wide association study of prognosis in advanced non-small
            cell lung cancer patients receiving platinum-based chemotherapy
  JOURNAL   Clin Cancer Res 18 (19), 5507-5514 (2012)
   PUBMED   22872573
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 527)
  AUTHORS   Zenklusen,J.C., Rodriguez,L.V., LaCava,M., Wang,Z., Goldstein,L.S.
            and Conti,C.J.
  TITLE     Novel susceptibility locus for mouse hepatomas: evidence for a
            conserved tumor suppressor gene
  JOURNAL   Genome Res 6 (11), 1070-1076 (1996)
   PUBMED   8938430
REFERENCE   7  (residues 1 to 527)
  AUTHORS   Zenklusen,J.C., Weitzel,J.N., Ball,H.G. and Conti,C.J.
  TITLE     Allelic loss at 7q31.1 in human primary ovarian carcinomas suggests
            the existence of a tumor suppressor gene
  JOURNAL   Oncogene 11 (2), 359-363 (1995)
   PUBMED   7624150
REFERENCE   8  (residues 1 to 527)
  AUTHORS   Zenklusen,J.C., Thompson,J.C., Troncoso,P., Kagan,J. and Conti,C.J.
  TITLE     Loss of heterozygosity in human primary prostate carcinomas: a
            possible tumor suppressor gene at 7q31.1
  JOURNAL   Cancer Res 54 (24), 6370-6373 (1994)
   PUBMED   7987830
REFERENCE   9  (residues 1 to 527)
  AUTHORS   Zenklusen,J.C., Bieche,I., Lidereau,R. and Conti,C.J.
  TITLE     (C-A)n microsatellite repeat D7S522 is the most commonly deleted
            region in human primary breast cancer
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12155-12158 (1994)
   PUBMED   7991599
REFERENCE   10 (residues 1 to 527)
  AUTHORS   Ogata,T., Ayusawa,D., Namba,M., Takahashi,E., Oshimura,M. and
            Oishi,M.
  TITLE     Chromosome 7 suppresses indefinite division of nontumorigenic
            immortalized human fibroblast cell lines KMST-6 and SUSM-1
  JOURNAL   Mol Cell Biol 13 (10), 6036-6043 (1993)
   PUBMED   8105370
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106873.3, AC002542.1 and
            AC003987.1.
            
            Summary: The gene for this product maps to a region on chromosome 7
            identified as an autism-susceptibility locus. Mutation screening of
            the entire coding region in autistic individuals failed to identify
            phenotype-specific variants, suggesting that coding mutations for
            this gene are unlikely to be involved in the etiology of autism.
            The function of this gene product has not been determined.
            Transcript variants encoding different isoforms of this protein
            have been described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.156693.1,
                                           SRR3476690.891467.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267751, SAMN03267756
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.2"
     Protein         1..527
                     /product="suppressor of tumorigenicity 7 protein isoform
                     10"
                     /note="family with sequence similarity 4, subfamily A,
                     member 1; suppression of tumorigenicity 7 (breast);
                     suppressor of tumorigenicity 7 protein"
                     /calculated_mol_wt=60090
     Region          4..491
                     /region_name="ST7"
                     /note="Suppression of tumorigenicity 7; cd11557"
                     /db_xref="CDD:211407"
     CDS             1..527
                     /gene="ST7"
                     /gene_synonym="ETS7q; FAM4A; FAM4A1; HELG; RAY1; SEN4;
                     TSG7"
                     /coded_by="NM_001369606.1:615..2198"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:7982"
                     /db_xref="HGNC:HGNC:11351"
                     /db_xref="MIM:600833"
ORIGIN      
        1 msmflntltp kfyvaltgts slisglilif ewwyfrkygt sfieqvsvsh lrpllggvdn
       61 nssnnsnssn gdsdsnrqsv seckvwrnpl nlfrgaeynr ytwvtgrepl tyydmnlsaq
      121 dhqtfftcds dhlrpadaim qkawrernpq arisaaheal eineirsrve vpliasstiw
      181 eikllpkcat ayillaeeea ttiaeaeklf kqalkagdgc yrrsqqlqhh gsqyeaqhrr
      241 dtnvlvyikr rlamcarrlg rtreavkmmr dlmkefplls mfnihenlle allelqayad
      301 vqavlakydd islpksatic ytaallkara vsdkfspeaa srrglstaem naveaihrav
      361 efnphvpkyl lemkslilpp ehilkrgdse aiayaffhla hwkrvegaln llhctwegtf
      421 rmipyplekg hlfypypict etadrellps fhevsvypkk elpffilfta glcsftamla
      481 llthqfpelm gvfakaflst lfaplnfvme kvesilpssl whqltri
//
LOCUS       NP_055160               2279 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 318 [Homo sapiens].
ACCESSION   NP_055160
VERSION     NP_055160.2
DBSOURCE    REFSEQ: accession NM_014345.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2279)
  AUTHORS   Tao,R.H., Kawate,H., Ohnaka,K., Ishizuka,M., Hagiwara,H. and
            Takayanagi,R.
  TITLE     Opposite effects of alternative TZF spliced variants on androgen
            receptor
  JOURNAL   Biochem Biophys Res Commun 341 (2), 515-521 (2006)
   PUBMED   16446156
  REMARK    GeneRIF: in the unique regulation system of AR-mediated
            transactivation, two spliced isoforms of TZF act as coactivator and
            corepressor, respectively
REFERENCE   2  (residues 1 to 2279)
  AUTHORS   Ishizuka,M., Kawate,H., Takayanagi,R., Ohshima,H., Tao,R.H. and
            Hagiwara,H.
  TITLE     A zinc finger protein TZF is a novel corepressor of androgen
            receptor
  JOURNAL   Biochem Biophys Res Commun 331 (4), 1025-1031 (2005)
   PUBMED   15882980
REFERENCE   3  (residues 1 to 2279)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   4  (residues 1 to 2279)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   5  (residues 1 to 2279)
  AUTHORS   Inoue,A., Ishiji,A., Kasagi,S., Ishizuka,M., Hirose,S., Baba,T. and
            Hagiwara,H.
  TITLE     The transcript for a novel protein with a zinc finger motif is
            expressed at specific stages of mouse spermatogenesis
  JOURNAL   Biochem Biophys Res Commun 273 (2), 398-403 (2000)
   PUBMED   10873617
REFERENCE   6  (residues 1 to 2279)
  AUTHORS   Ueki,N., Oda,T., Kondo,M., Yano,K., Noguchi,T. and Muramatsu,M.
  TITLE     Selection system for genes encoding nuclear-targeted proteins
  JOURNAL   Nat Biotechnol 16 (13), 1338-1342 (1998)
   PUBMED   9853615
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590383.6, BC098434.1, AL583834.6 and AK027061.1.
            
            On Jan 4, 2007 this sequence version replaced NP_055160.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF090114.1, BC098434.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361428.3/ ENSP00000354964.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2279
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..2279
                     /product="zinc finger protein 318"
                     /note="testicular zinc finger; endocrine regulator;
                     endocrine regulatory protein"
                     /calculated_mol_wt=250982
     Region          1..1092
                     /region_name="Interaction with AR.
                     /evidence=ECO:0000250|UniProtKB:Q99PP2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          1..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          <52..>143
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          164..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q99PP2; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          279..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          397..416
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          514..533
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          540..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          664..709
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          <684..876
                     /region_name="PHA03377"
                     /note="EBNA-3C; Provisional"
                     /db_xref="CDD:177614"
     Site            842
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          <877..1346
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          881..>997
                     /region_name="MAD"
                     /note="Mitotic checkpoint protein; pfam05557"
                     /db_xref="CDD:461677"
     Region          922..942
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          989..1051
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            1010
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            1037
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          1063..1097
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          1133..1167
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          1195..1319
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            1243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            1267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            1420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          1428..1463
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          1577..1628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          1702..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            1713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          1753..1775
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            1856
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            1896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            1971
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            2030
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            2035
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            2091
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            2101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            2189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            2192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Site            2243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     Region          2252..2279
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUA4.2)"
     CDS             1..2279
                     /gene="ZNF318"
                     /gene_synonym="HRIHFB2436; TZF; ZFP318"
                     /coded_by="NM_014345.3:283..7122"
                     /db_xref="CCDS:CCDS4895.2"
                     /db_xref="GeneID:24149"
                     /db_xref="HGNC:HGNC:13578"
                     /db_xref="MIM:617512"
ORIGIN      
        1 myrssarssv sshrpkddgg ggprsgrssg sssgparrss pppppsgsss rtparrprsp
       61 sghrgrrasp spprgrrvsp spprarrgsp spprgrrlfp pgpagfrgss rgesradyar
      121 dgrgdhpgds gsrrrspglc sdslekslri tvgndhfcvs tperrrlsdr lgspvdnled
      181 mdrddltdds vftrssqcsr gleryisqee gplspflgql dedyrtketf lhrsdysphi
      241 schdellrgt ernreklkgy sirseersre akrpryddtv kinsmggdhp sftsgtrnyr
      301 qrrrspsprf ldpefreldl arrkreeeee rsrslsqelv gvdgggtgcs ipglsgvlta
      361 sepgyslhrp eevsvmpkks ilkkrievdi mepsmqlesf ssstsssqdh plysghpslp
      421 lsgaiaafas eienkgtmve talkepqgnl yqwgplpgip kdnsplrekf gsflchkdnl
      481 dlkaegperh tdfllphera sqdgsgfsri lsmladstst qekrrrsfpd iedeekflyg
      541 deeedlkaes vpkplgsses evmrqkassl pssapavkle sleetnpeya kihdllktig
      601 ldigvaeisq laartqerlh gkkpslrssa drrssvdryf sadhcssvdh rfsadrcssv
      661 dhcfsadrrs sdphrlesre ahhsnthspe vshphppspv dpylltknsp pflksdhpvg
      721 hisgpevvgs gfqssvavrc mlpsapsapi rlphtaalsq fhmprasqfa aarippnyqg
      781 paippasfda yrhymayaas rwpmyptsqp snhpvpephr impitkqatr srpnlrvipt
      841 vtpdkpkqke slrgsipaaq vpvqvsipsl irynpekisd eknrasqkqk vieereklkn
      901 drearqkkmy ylrtelerlh kqqgemlrkk rrekdghkdp llvevsrlqd nimkdiaelr
      961 qeaeeaekkq seldkvaqil ginifdksqk slsdsrepte kpgkaeksks pekvssfsns
     1021 ssnkeskvnn ekfrtkspkp aespqsatkq ldqptaayey ydagnhwckd cnticgtmfd
     1081 ffthmhnkkh tqtldpynrp wasktqseak qdaikrtdki tvpakgsefl vpisgfycql
     1141 ceeflgdpis geqhvkghqh nekykkyvde nplyeerrnl drqaglavvl eterrrqsel
     1201 krklsekpke ekkekkakav kevkeddkvs ekledqlseg rnspekaenk rntgiklqlk
     1261 eevkkespts ssfgkfswkk pekeeekssl vtpsiskeei lesskdkedg kteagkakpi
     1321 kiklsgktvv ahtspwmpvv ttstqtkirp nlpipstvlr kscsatmskp aplntflsik
     1381 ssgttakplp vvkessadll lppdiiskaf ggeevilkgs peekvvlaek sepshlpeqi
     1441 lppppppppp ppppppviph paapsaaqan ailapvksnp vvsqtlspgf vgpnilnpvl
     1501 pvaimasaqp aaipsdetap gvsesdrdqt lfsvlvrppp plssvfseqa kklekrnscl
     1561 atanakdlyd ifyssggkga petkgapetk lsggplange nsnlsrtkss dtsstsplns
     1621 sasqeelhqd eglvaapivs nsekpiaktl valgkwsvve hvgpkstgst ygflqpltrl
     1681 cqsrpyetit pktdtlaiwt sssfqsdtsr dispekseld lgepgppgve pppqlldiqc
     1741 kesqklveih lresvnqdke sqelrksedc reseietnte lkervkelse givdegvsts
     1801 igphsiddsn lnhgnrymwe gevkqpnllm idkeaeqsnk lmtgsetpsk vviklspqac
     1861 sftkakldsf lsearsllnp qdtpvkisap elllhspars amcltgspqe qgvsvvseeg
     1921 lensapesas rtsryrslkl krerskdfqv kkiyelavwd enkkrpetwe spekpkteal
     1981 elqdvhpelt vtieskaled featdlkvee ltalgnlgdm pvdfcttrvs pahrsptvlc
     2041 qkvceensvs pigcnssdpa dfepipsfsg fpldspktlv ldfetegern spnprsvrip
     2101 spnilktglt envdrglggl egthqaldll aggmmpeevk essqldkqes lglelktins
     2161 aglgpspclp dlvdfvtrts gvqkdklcsp lsepgdpskc sslelgplql eisnasttev
     2221 ailqvdddsg dplnlvkapv srsppreqvi ednmvpqgmp eqettvgaiq dhtessvhn
//
LOCUS       NP_766392                549 aa            linear   ROD 27-APR-2025
DEFINITION  synaptotagmin-16 isoform 3 [Mus musculus].
ACCESSION   NP_766392
VERSION     NP_766392.2
DBSOURCE    REFSEQ: accession NM_172804.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fukuda,M.
  TITLE     Molecular cloning, expression, and characterization of a novel
            class of synaptotagmin (Syt XIV) conserved from Drosophila to
            humans
  JOURNAL   J Biochem 133 (5), 641-649 (2003)
   PUBMED   12801916
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK137129.1, AV348245.2 and BB074919.1.
            
            On Jan 11, 2007 this sequence version replaced NP_766392.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.86365.1,
                                           SRR1660821.188143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 32.02 cM"
     Protein         1..549
                     /product="synaptotagmin-16 isoform 3"
                     /note="synaptotagmin-16; synaptotagmin 14-like protein;
                     synaptotagmin XIV-related protein"
                     /calculated_mol_wt=61208
     Region          254..377
                     /region_name="C2A_Synaptotagmin-14_16"
                     /note="C2A domain first repeat present in Synaptotagmins
                     14 and 16; cd08389"
                     /db_xref="CDD:176035"
     Region          410..547
                     /region_name="C2B_Synaptotagmin-14_16"
                     /note="C2 domain second repeat present in Synaptotagmins
                     14 and 16; cd08408"
                     /db_xref="CDD:176053"
     CDS             1..549
                     /gene="Syt16"
                     /gene_synonym="Strep14; Syt14l; syt14r"
                     /coded_by="NM_172804.3:75..1724"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS49089.1"
                     /db_xref="GeneID:238266"
                     /db_xref="MGI:MGI:2673872"
ORIGIN      
        1 matditpeai gflsaigvfv vllavlllfi nkklcsenlr ghpypeqrgk rkhsrdktgg
       61 htgtvnsfgd deepstsses dedvtkqfki svsrsqsfrs gvsekgktte leqkikckrl
      121 lcthqedsae gsacegihcs alhcrqgqvn dldrtsqlsy seilsyedrp isilpqspfe
      181 srnvrhhgpc rpemgmvrsl grpcadgvle tetafvsrgf edsyathsss lwspeeqdgt
      241 slqvphrlle piskcgdldv ifeyravtqk ltvtivraqg lpdkdrsgvn swqvhivllp
      301 skkqrgktni qrgpnpvfke kvtftklepr dvascavrfr lyaarkmtre rmmgeklfcl
      361 shlhpegemk vtlvleprsn lssgesplsp svvshsdsas stqslshggv pellvglsyn
      421 attgrlsvem ikgshfrnla anrapdtygk lfllncvgqe msrcktsirr gqpnpvyket
      481 fvfqvalfql sdvtlmisiy srrtmkrkem igwvalgqns sgeeeqehwe emkeskgqqt
      541 crwhtlles
//
LOCUS       NP_001354126             481 aa            linear   PRI 27-APR-2025
DEFINITION  ADAMTS-like protein 5 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001354126 XP_005259606
VERSION     NP_001354126.1
DBSOURCE    REFSEQ: accession NM_001367197.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Kong,S., Tian,S., Wang,Z., Shi,Y., Zhang,J. and Zhuo,H.
  TITLE     Circular RNA circPFKP suppresses the proliferation and metastasis
            of gastric cancer cell via sponging miR-644 and regulating ADAMTSL5
            expression
  JOURNAL   Bioengineered 13 (5), 12326-12337 (2022)
   PUBMED   35587154
  REMARK    GeneRIF: Circular RNA circPFKP suppresses the proliferation and
            metastasis of gastric cancer cell via sponging miR-644 and
            regulating ADAMTSL5 expression.
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Abdullah,M., Choo,C.W., Alias,H., Abdul Rahman,E.J., Mohd
            Ibrahim,H., Jamal,R. and Hussin,N.H.
  TITLE     ADAMTSL5 and CDH11: putative epigenetic markers for therapeutic
            resistance in acute lymphoblastic leukemia
  JOURNAL   Hematology 22 (7), 386-391 (2017)
   PUBMED   28292214
  REMARK    GeneRIF: Chemoresistant B-ALL patients are associated with
            increased methylation in ADAMTSL5 and CDH11.
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Arakawa,A., Siewert,K., Stohr,J., Besgen,P., Kim,S.M., Ruhl,G.,
            Nickel,J., Vollmer,S., Thomas,P., Krebs,S., Pinkert,S.,
            Spannagl,M., Held,K., Kammerbauer,C., Besch,R., Dornmair,K. and
            Prinz,J.C.
  TITLE     Melanocyte antigen triggers autoimmunity in human psoriasis
  JOURNAL   J Exp Med 212 (13), 2203-2212 (2015)
   PUBMED   26621454
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Bader,H.L., Wang,L.W., Ho,J.C., Tran,T., Holden,P., Fitzgerald,J.,
            Atit,R.P., Reinhardt,D.P. and Apte,S.S.
  TITLE     A disintegrin-like and metalloprotease domain containing
            thrombospondin type 1 motif-like 5 (ADAMTSL5) is a novel
            fibrillin-1-, fibrillin-2-, and heparin-binding member of the
            ADAMTS superfamily containing a netrin-like module
  JOURNAL   Matrix Biol 31 (7-8), 398-411 (2012)
   PUBMED   23010571
  REMARK    GeneRIF: ADAMTSL5 could have a role in modulating microfibril
            functions.
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 481)
  AUTHORS   Kim,Y.C., Jung,Y.C., Xuan,Z., Dong,H., Zhang,M.Q. and Wang,S.M.
  TITLE     Pan-genome isolation of low abundance transcripts using SAGE tag
  JOURNAL   FEBS Lett 580 (28-29), 6721-6729 (2006)
   PUBMED   17113583
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX951496.1, AC027307.5 and AW167554.1.
            
            On Nov 10, 2018 this sequence version replaced XP_005259606.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..481
                     /product="ADAMTS-like protein 5 isoform 1 precursor"
                     /note="thrombospondin, type I, domain containing 6;
                     ADAMTS-like protein 5; ADAMTSL-5; thrombospondin type-1
                     domain-containing protein 6"
                     /calculated_mol_wt=48509
     sig_peptide     1..42
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4703
     mat_peptide     43..481
                     /product="ADAMTS-like protein 5. /id=PRO_0000249582"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZMM2.3)"
                     /calculated_mol_wt=48509
     Region          48..97
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          103..200
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Region          215..311
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Site            218
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23010571; propagated from
                     UniProtKB/Swiss-Prot (Q6ZMM2.3)"
     Region          331..361
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZMM2.3)"
     Region          375..476
                     /region_name="NTR_like"
                     /note="NTR_like domain; a beta barrel with an
                     oligosaccharide/oligonucleotide-binding fold found in
                     netrins, complement proteins, tissue inhibitors of
                     metalloproteases (TIMP), and procollagen C-proteinase
                     enhancers (PCOLCE), amongst others. In netrins, the...;
                     cd03523"
                     /db_xref="CDD:239600"
     CDS             1..481
                     /gene="ADAMTSL5"
                     /gene_synonym="THSD6"
                     /coded_by="NM_001367197.1:105..1550"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:339366"
                     /db_xref="HGNC:HGNC:27912"
ORIGIN      
        1 mgklrpgrve wlasghterp hlfqnlllfl wallncglgv saqgpgewtp wvswtrcsss
       61 cgrgvsvrsr rclrlpgeep cwgdsheyrl cqlpdcppga vpfrdlqcal yngrpvlgtq
      121 ktyqwvpfhg apnqcdlncl aeghafyhsf grvldgtacs pgaqgvcvag rclsagcdgl
      181 lgsgaledrc grcggandsc lfvqrvfrda gafagywnvt lipegarhir vehrsrnhla
      241 lmggdgryvl nghwvvsppg tyeaagthvv ytrdtgpqet lqaagptshd lllqvllqep
      301 npgiefefwl preryspfqa rvqalgwplr qpqprgvepq ppaapavtpa qtptlapdpc
      361 ppcpdtrgra hrllhycgsd fvfqarvlgh hhqaqetrye vriqlvyknr splrareyvw
      421 apghcpcpml aphrdylmav qrlvspdgtq dqlllphagy arpwspaeds rirltarrcp
      481 g
//
LOCUS       NP_659171                859 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein U-like protein 1 isoform 1
            [Mus musculus].
ACCESSION   NP_659171
VERSION     NP_659171.1
DBSOURCE    REFSEQ: accession NM_144922.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Vivori,C., Papasaikas,P., Stadhouders,R., Di Stefano,B.,
            Rubio,A.R., Balaguer,C.B., Generoso,S., Mallol,A., Sardina,J.L.,
            Payer,B., Graf,T. and Valcarcel,J.
  TITLE     Dynamics of alternative splicing during somatic cell reprogramming
            reveals functions for RNA-binding proteins CPSF3, hnRNP UL1, and
            TIA1
  JOURNAL   Genome Biol 22 (1), 171 (2021)
   PUBMED   34082786
  REMARK    GeneRIF: Dynamics of alternative splicing during somatic cell
            reprogramming reveals functions for RNA-binding proteins CPSF3,
            hnRNP UL1, and TIA1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Distler,U., Schmeisser,M.J., Pelosi,A., Reim,D., Kuharev,J.,
            Weiczner,R., Baumgart,J., Boeckers,T.M., Nitsch,R., Vogt,J. and
            Tenzer,S.
  TITLE     In-depth protein profiling of the postsynaptic density from mouse
            hippocampus using data-independent acquisition proteomics
  JOURNAL   Proteomics 14 (21-22), 2607-2613 (2014)
   PUBMED   25211037
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Guo,G., Huss,M., Tong,G.Q., Wang,C., Li Sun,L., Clarke,N.D. and
            Robson,P.
  TITLE     Resolution of cell fate decisions revealed by single-cell gene
            expression analysis from zygote to blastocyst
  JOURNAL   Dev Cell 18 (4), 675-685 (2010)
   PUBMED   20412781
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK143666.1, AK155604.1, AK087545.1, BY482198.1 and CD804713.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164138,
                              SAMN01164142 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 14.0 cM"
     Protein         1..859
                     /product="heterogeneous nuclear ribonucleoprotein U-like
                     protein 1 isoform 1"
                     /note="EIB-55kDa associated protein 5; heterogeneous
                     nuclear ribonucleoprotein U-like protein 1"
                     /calculated_mol_wt=95871
     Region          1..103
                     /region_name="Necessary for interaction with HRMT1L1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Region          2..>73
                     /region_name="PLN03124"
                     /note="poly [ADP-ribose] polymerase; Provisional"
                     /db_xref="CDD:215591"
     Region          3..37
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Region          36..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Region          146..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Region          212..389
                     /region_name="SPRY_hnRNP"
                     /note="SPRY domain in heterogeneous nuclear
                     ribonucleoprotein U-like (hnRNP) protein 1; cd12884"
                     /db_xref="CDD:293942"
     Region          214..859
                     /region_name="Necessary for interaction with TP53.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Region          425..569
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
     Region          457..595
                     /region_name="Necessary for interaction with BRD7 and
                     transcriptional activation. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUJ2; propagated from
                     UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Region          595..814
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Region          613..661
                     /region_name="5 X 3 AA repeats of R-G-G"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Region          613..661
                     /region_name="Necessary for transcription repression.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Site            639
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Site            645
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Site            659
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Site            664
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Site            674
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUJ2; propagated from
                     UniProtKB/Swiss-Prot (Q8VDM6.1)"
     Site            721
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUJ2; propagated from
                     UniProtKB/Swiss-Prot (Q8VDM6.1)"
     CDS             1..859
                     /gene="Hnrnpul1"
                     /gene_synonym="E130317O14Rik; E1B-AP5; E1BAP5; Hnrnpul;
                     Hnrpul1"
                     /coded_by="NM_144922.3:125..2704"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS20995.1"
                     /db_xref="GeneID:232989"
                     /db_xref="MGI:MGI:2443517"
ORIGIN      
        1 mdvrrlkvne lreelqrrgl dtrglkaela erllaaleae epederelea dddpglpghn
       61 neeveteggs elegtaqppp pglqphpepg gysgpdghyv mdnitrqnqf yetpvikqen
      121 essydrrpld mepqqqvyhp elktemkqea ppsflppeas qlktdrpqfq nrkrpfeenr
      181 grgyfehred rrgrspqppa eededdfddt lvaidtyncd lhfkvardrs sgypltiegf
      241 aylwsgaras ygvrrgrvcf emkineeisv khlpstepdp hvvrigwsld scstqlgeep
      301 fsygyggtgk kstnsrfeny gdkfaendvi gcfadfecgn dvelsftkng kwmgiafriq
      361 kealggqaly phvlvkncav efnfgqraep ycsvlpgftf iqhlplseri rgtigpkska
      421 eceilmmvgl paagkttwai khaasnpskk ynilgtnaim dkmrvmglrr qrnyagrwdv
      481 liqqatqcln rliqiaarkk rnyildqtnv ygsaqrrkmr pfegfqrkai vicptdedlk
      541 drtvkrtdee gkdvpdhavl emkanftlpd vgdfldevlf ielqreeadk lvrqyneegr
      601 kagpppekrf dsrgggfrgr gggggfqryd nrgppggnrg gfqnrggggg sgggggnyrg
      661 gfnrsggggy nqnrwgnnnr dnnnsnnrgn ynrapqqqpp pqqppppqpp pqqpppppsy
      721 sparnppgas synknsnipg ssantstptv ssytppqpsy sqppynqggy tqgytapppp
      781 pppppaynyg sygpynpapy tppppptaqt ypqpsynqyq qyaqqwsqyy qnqsqwppyy
      841 gnydyggysg stqggtstq
//
LOCUS       NP_001349385             129 aa            linear   ROD 27-APR-2025
DEFINITION  potassium voltage-gated channel subfamily E member 1 [Mus
            musculus].
ACCESSION   NP_001349385 XP_006523004
VERSION     NP_001349385.1
DBSOURCE    REFSEQ: accession NM_001362456.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Gomez-Del Arco,P., Isern,J., Jimenez-Carretero,D.,
            Lopez-Maderuelo,D., Pineiro-Sabaris,R., El Abdellaoui-Soussi,F.,
            Torroja,C., Vera-Pedrosa,M.L., Grima-Terren,M., Benguria,A.,
            Simon-Chica,A., Queiro-Palou,A., Dopazo,A., Sanchez-Cabo,F.,
            Jalife,J., de la Pompa,J.L., Filgueiras-Rama,D., Munoz-Canoves,P.
            and Redondo,J.M.
  TITLE     The G4 resolvase Dhx36 modulates cardiomyocyte differentiation and
            ventricular conduction system development
  JOURNAL   Nat Commun 15 (1), 8602 (2024)
   PUBMED   39366945
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Van Wauwe,J., Mahy,A., Craps,S., Ekhteraei-Tousi,S., Vrancaert,P.,
            Kemps,H., Dheedene,W., Donate Puertas,R., Trenson,S.,
            Roderick,H.L., Beerens,M. and Luttun,A.
  TITLE     PRDM16 determines specification of ventricular cardiomyocytes by
            suppressing alternative cell fates
  JOURNAL   Life Sci Alliance 7 (12), e202402719 (2024)
   PUBMED   39304345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Wu,Y., Chen,S., Huang,G., Zhang,L., Zhong,L., Feng,Y., Wen,P. and
            Liu,J.
  TITLE     Transcriptome analysis reveals EBF1 ablation-induced injuries in
            cardiac system
  JOURNAL   Theranostics 14 (12), 4894-4915 (2024)
   PUBMED   39239522
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Talbi,K., Ousingsawat,J., Centeio,R., Schreiber,R. and
            Kunzelmann,K.
  TITLE     KCNE1 does not shift TMEM16A from a Ca2+ dependent to a voltage
            dependent Cl- channel and is not expressed in renal proximal tubule
  JOURNAL   Pflugers Arch 475 (8), 995-1007 (2023)
   PUBMED   37442855
  REMARK    GeneRIF: KCNE1 does not shift TMEM16A from a Ca[2+] dependent to a
            voltage dependent Cl[-] channel and is not expressed in renal
            proximal tubule.
REFERENCE   6  (residues 1 to 129)
  AUTHORS   Barhanin,J., Lesage,F., Guillemare,E., Fink,M., Lazdunski,M. and
            Romey,G.
  TITLE     K(V)LQT1 and lsK (minK) proteins associate to form the I(Ks)
            cardiac potassium current
  JOURNAL   Nature 384 (6604), 78-80 (1996)
   PUBMED   8900282
REFERENCE   7  (residues 1 to 129)
  AUTHORS   Felipe,A., Knittle,T.J., Doyle,K.L., Snyders,D.J. and Tamkun,M.M.
  TITLE     Differential expression of Isk mRNAs in mouse tissue during
            development and pregnancy
  JOURNAL   Am J Physiol 267 (3 Pt 1), C700-C705 (1994)
   PUBMED   7943198
REFERENCE   8  (residues 1 to 129)
  AUTHORS   Lesage,F., Attali,B., Lazdunski,M. and Barhanin,J.
  TITLE     Developmental expression of voltage-sensitive K+ channels in mouse
            skeletal muscle and C2C12 cells
  JOURNAL   FEBS Lett 310 (2), 162-166 (1992)
   PUBMED   1383027
REFERENCE   9  (residues 1 to 129)
  AUTHORS   Lesage,F., Attali,B., Lazdunski,M. and Barhanin,J.
  TITLE     ISK, a slowly activating voltage-sensitive K+ channel.
            Characterization of multiple cDNAs and gene organization in the
            mouse
  JOURNAL   FEBS Lett 301 (2), 168-172 (1992)
   PUBMED   1568475
REFERENCE   10 (residues 1 to 129)
  AUTHORS   Honore,E., Attali,B., Romey,G., Heurteaux,C., Ricard,P., Lesage,F.,
            Lazdunski,M. and Barhanin,J.
  TITLE     Cloning, expression, pharmacology and regulation of a delayed
            rectifier K+ channel in mouse heart
  JOURNAL   EMBO J 10 (10), 2805-2811 (1991)
   PUBMED   1655403
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC162305.5.
            
            On Apr 18, 2018 this sequence version replaced XP_006523004.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X60457.1, SRR7345562.4571975.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="16"
                     /map="16 53.57 cM"
     Protein         1..129
                     /product="potassium voltage-gated channel subfamily E
                     member 1"
                     /note="minimal potassium channel; delayed rectifier
                     potassium channel subunit IsK; IKs producing slow
                     voltage-gated potassium channel subunit beta Mink"
                     /calculated_mol_wt=14447
     Region          1..126
                     /region_name="ISK_Channel"
                     /note="Slow voltage-gated potassium channel; pfam02060"
                     /db_xref="CDD:460432"
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23299.1)"
     Site            7
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P23299.1)"
     Site            26
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23299.1)"
     Site            44..66
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23299.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P23299.1)"
     CDS             1..129
                     /gene="Kcne1"
                     /gene_synonym="Isk; MinK; nmf190"
                     /coded_by="NM_001362456.1:79..468"
                     /db_xref="CCDS:CCDS28336.1"
                     /db_xref="GeneID:16509"
                     /db_xref="MGI:MGI:96673"
ORIGIN      
        1 mslpnsttvl pflarlwqet aeqggnvsgl arksqlrdds klealyilmv lgffgfftlg
       61 imlsyirskk lehshdpfnv yiesdawqek gkavfqarvl esfracyvie nqaaveqpat
      121 hlpelkpls
//
LOCUS       NP_056180                333 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear protein AMMECR1 isoform 1 [Homo sapiens].
ACCESSION   NP_056180
VERSION     NP_056180.1
DBSOURCE    REFSEQ: accession NM_015365.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Ge,H., Cheng,N., Xu,X., Yang,Z., Hoffman,R.M. and Zhu,J.
  TITLE     AMMECR1 Inhibits Apoptosis and Promotes Cell-cycle Progression and
            Proliferation of the A549 Human Lung Cancer Cell Line
  JOURNAL   Anticancer Res 39 (9), 4637-4642 (2019)
   PUBMED   31519561
  REMARK    GeneRIF: AMMECR1 plays a critical role in cell proliferation,
            cell-cycle progression, and apoptosis of human lung cancer cells,
            and may serve as a potential therapeutic target for non-small-cell
            lung cancer.
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Moyses-Oliveira,M., Giannuzzi,G., Fish,R.J., Rosenfeld,J.A.,
            Petit,F., Soares,M.F., Kulikowski,L.D., Di-Battista,A.,
            Zamariolli,M., Xia,F., Liehr,T., Kosyakova,N., Carvalheira,G.,
            Parker,M., Seaby,E.G., Ennis,S., Gilbert,R.D., Hagelstrom,R.T.,
            Cremona,M.L., Li,W.L., Malhotra,A., Chandrasekhar,A., Perry,D.L.,
            Taft,R.J., McCarrier,J., Basel,D.G., Andrieux,J., Stumpp,T.,
            Antunes,F., Pereira,G.J., Neerman-Arbez,M., Meloni,V.A.,
            Drummond-Borg,M., Melaragno,M.I. and Reymond,A.
  TITLE     Inactivation of AMMECR1 is associated with growth, bone, and heart
            alterations
  JOURNAL   Hum Mutat 39 (2), 281-291 (2018)
   PUBMED   29193635
  REMARK    GeneRIF: results suggest that AMMECR1 is potentially involved in
            cell cycle control and linked to a new syndrome with growth, bone,
            heart, and kidney alterations with or without elliptocytosis.
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Tanneberger,K., Pfister,A.S., Brauburger,K., Schneikert,J.,
            Hadjihannas,M.V., Kriz,V., Schulte,G., Bryja,V. and Behrens,J.
  TITLE     Amer1/WTX couples Wnt-induced formation of PtdIns(4,5)P2 to LRP6
            phosphorylation
  JOURNAL   EMBO J 30 (8), 1433-1443 (2011)
   PUBMED   21304492
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Ross,M.T., Grafham,D.V., Coffey,A.J., Scherer,S., McLay,K.,
            Muzny,D., Platzer,M., Howell,G.R., Burrows,C., Bird,C.P.,
            Frankish,A., Lovell,F.L., Howe,K.L., Ashurst,J.L., Fulton,R.S.,
            Sudbrak,R., Wen,G., Jones,M.C., Hurles,M.E., Andrews,T.D.,
            Scott,C.E., Searle,S., Ramser,J., Whittaker,A., Deadman,R.,
            Carter,N.P., Hunt,S.E., Chen,R., Cree,A., Gunaratne,P., Havlak,P.,
            Hodgson,A., Metzker,M.L., Richards,S., Scott,G., Steffen,D.,
            Sodergren,E., Wheeler,D.A., Worley,K.C., Ainscough,R.,
            Ambrose,K.D., Ansari-Lari,M.A., Aradhya,S., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Ballabio,A., Banerjee,R., Barker,G.E.,
            Barlow,K.F., Barrett,I.P., Bates,K.N., Beare,D.M., Beasley,H.,
            Beasley,O., Beck,A., Bethel,G., Blechschmidt,K., Brady,N.,
            Bray-Allen,S., Bridgeman,A.M., Brown,A.J., Brown,M.J., Bonnin,D.,
            Bruford,E.A., Buhay,C., Burch,P., Burford,D., Burgess,J.,
            Burrill,W., Burton,J., Bye,J.M., Carder,C., Carrel,L., Chako,J.,
            Chapman,J.C., Chavez,D., Chen,E., Chen,G., Chen,Y., Chen,Z.,
            Chinault,C., Ciccodicola,A., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S., Clerc-Blankenburg,K., Clifford,K., Cobley,V., Cole,C.G.,
            Conquer,J.S., Corby,N., Connor,R.E., David,R., Davies,J., Davis,C.,
            Davis,J., Delgado,O., Deshazo,D., Dhami,P., Ding,Y., Dinh,H.,
            Dodsworth,S., Draper,H., Dugan-Rocha,S., Dunham,A., Dunn,M.,
            Durbin,K.J., Dutta,I., Eades,T., Ellwood,M., Emery-Cohen,A.,
            Errington,H., Evans,K.L., Faulkner,L., Francis,F., Frankland,J.,
            Fraser,A.E., Galgoczy,P., Gilbert,J., Gill,R., Glockner,G.,
            Gregory,S.G., Gribble,S., Griffiths,C., Grocock,R., Gu,Y.,
            Gwilliam,R., Hamilton,C., Hart,E.A., Hawes,A., Heath,P.D.,
            Heitmann,K., Hennig,S., Hernandez,J., Hinzmann,B., Ho,S., Hoffs,M.,
            Howden,P.J., Huckle,E.J., Hume,J., Hunt,P.J., Hunt,A.R.,
            Isherwood,J., Jacob,L., Johnson,D., Jones,S., de Jong,P.J.,
            Joseph,S.S., Keenan,S., Kelly,S., Kershaw,J.K., Khan,Z.,
            Kioschis,P., Klages,S., Knights,A.J., Kosiura,A., Kovar-Smith,C.,
            Laird,G.K., Langford,C., Lawlor,S., Leversha,M., Lewis,L., Liu,W.,
            Lloyd,C., Lloyd,D.M., Loulseged,H., Loveland,J.E., Lovell,J.D.,
            Lozado,R., Lu,J., Lyne,R., Ma,J., Maheshwari,M., Matthews,L.H.,
            McDowall,J., McLaren,S., McMurray,A., Meidl,P., Meitinger,T.,
            Milne,S., Miner,G., Mistry,S.L., Morgan,M., Morris,S., Muller,I.,
            Mullikin,J.C., Nguyen,N., Nordsiek,G., Nyakatura,G., O'Dell,C.N.,
            Okwuonu,G., Palmer,S., Pandian,R., Parker,D., Parrish,J.,
            Pasternak,S., Patel,D., Pearce,A.V., Pearson,D.M., Pelan,S.E.,
            Perez,L., Porter,K.M., Ramsey,Y., Reichwald,K., Rhodes,S.,
            Ridler,K.A., Schlessinger,D., Schueler,M.G., Sehra,H.K.,
            Shaw-Smith,C., Shen,H., Sheridan,E.M., Shownkeen,R., Skuce,C.D.,
            Smith,M.L., Sotheran,E.C., Steingruber,H.E., Steward,C.A.,
            Storey,R., Swann,R.M., Swarbreck,D., Tabor,P.E., Taudien,S.,
            Taylor,T., Teague,B., Thomas,K., Thorpe,A., Timms,K., Tracey,A.,
            Trevanion,S., Tromans,A.C., d'Urso,M., Verduzco,D., Villasana,D.,
            Waldron,L., Wall,M., Wang,Q., Warren,J., Warry,G.L., Wei,X.,
            West,A., Whitehead,S.L., Whiteley,M.N., Wilkinson,J.E.,
            Willey,D.L., Williams,G., Williams,L., Williamson,A.,
            Williamson,H., Wilming,L., Woodmansey,R.L., Wray,P.W., Yen,J.,
            Zhang,J., Zhou,J., Zoghbi,H., Zorilla,S., Buck,D., Reinhardt,R.,
            Poustka,A., Rosenthal,A., Lehrach,H., Meindl,A., Minx,P.J.,
            Hillier,L.W., Willard,H.F., Wilson,R.K., Waterston,R.H., Rice,C.M.,
            Vaudin,M., Coulson,A., Nelson,D.L., Weinstock,G., Sulston,J.E.,
            Durbin,R., Hubbard,T., Gibbs,R.A., Beck,S., Rogers,J. and
            Bentley,D.R.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Tajika,Y., Sakai,N., Tamura,T., Yao,M., Watanabe,N. and Tanaka,I.
  TITLE     Crystal structure of PH0010 from Pyrococcus horikoshii, which is
            highly homologous to human AMMECR 1C-terminal region
  JOURNAL   Proteins 58 (2), 501-503 (2005)
   PUBMED   15558565
  REMARK    GeneRIF: PH0010 from Pyrococcus horikoshii is highly homologous to
            human AMMECR 1C-terminal region
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Vitelli,F., Piccini,M., Caroli,F., Franco,B., Malandrini,A.,
            Pober,B., Jonsson,J., Sorrentino,V. and Renieri,A.
  TITLE     Identification and characterization of a highly conserved protein
            absent in the Alport syndrome (A), mental retardation (M), midface
            hypoplasia (M), and elliptocytosis (E) contiguous gene deletion
            syndrome (AMME)
  JOURNAL   Genomics 55 (3), 335-340 (1999)
   PUBMED   10049589
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Piccini,M., Vitelli,F., Bruttini,M., Pober,B.R., Jonsson,J.J.,
            Villanova,M., Zollo,M., Borsani,G., Ballabio,A. and Renieri,A.
  TITLE     FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is
            deleted in a family with Alport syndrome, elliptocytosis, and
            mental retardation
  JOURNAL   Genomics 47 (3), 350-358 (1998)
   PUBMED   9480748
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ007014.1, BC060813.1,
            BC037983.1 and BC051895.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The exact function of this gene is not known, however,
            submicroscopic deletion of the X chromosome including this gene,
            COL4A5, and FACL4 genes, result in a contiguous gene deletion
            syndrome, the AMME complex (Alport syndrome, mental retardation,
            midface hypoplasia, and elliptocytosis). Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.76746.1,
                                           SRR1660809.67929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262844.10/ ENSP00000262844.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq23"
     Protein         1..333
                     /product="nuclear protein AMMECR1 isoform 1"
                     /note="AMME syndrome candidate gene 1 protein; nuclear
                     protein AMMECR1"
                     /calculated_mol_wt=35332
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4X0.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4X0.1)"
     Region          101..120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4X0.1)"
     Region          132..301
                     /region_name="AMMECR1"
                     /note="pfam01871"
                     /db_xref="CDD:460368"
     CDS             1..333
                     /gene="AMMECR1"
                     /gene_synonym="AMMERC1; MFHIEN"
                     /coded_by="NM_015365.3:15..1016"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14551.1"
                     /db_xref="GeneID:9949"
                     /db_xref="HGNC:HGNC:467"
                     /db_xref="MIM:300195"
ORIGIN      
        1 maagccgvkk qklsssppsg sgggggasss shcsgesqcr agelglggag trlnglgglt
       61 gggsgsgctl sppqgcgggg ggialsppps cgvgtllstp aaatssspss ssaasssspg
      121 srkmvvsaem ccfcfdvlyc hlygyqqprt prftnepypl fvtwkigrdk rlrgcigtfs
      181 amnlhsglre ytltsalkds rfppmtrdel prlfcsvsll tnfedvcdyl dwevgvhgir
      241 iefinekgsk rtatylpeva keqgwdhiqt idsllrkggy kapitnefrk tikltryrse
      301 kmtlsyaeyl ahrqhhhfqn gighplppyn hys
//
LOCUS       NP_998755                407 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM13 isoform 1 [Homo sapiens].
ACCESSION   NP_998755
VERSION     NP_998755.1
DBSOURCE    REFSEQ: accession NM_213590.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Govatati,S., Kumar,R., Boro,M., Traylor,J.G. Jr., Orr,A.W.,
            Lusis,A.J. and Rao,G.N.
  TITLE     TRIM13 reduces cholesterol efflux and increases oxidized LDL uptake
            leading to foam cell formation and atherosclerosis
  JOURNAL   J Biol Chem 300 (5), 107224 (2024)
   PUBMED   38537695
  REMARK    GeneRIF: TRIM13 reduces cholesterol efflux and increases oxidized
            LDL uptake leading to foam cell formation and atherosclerosis.
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Yu,B., Zhou,Y. and He,J.
  TITLE     TRIM13 inhibits cell proliferation and induces autophagy in lung
            adenocarcinoma by regulating KEAP1/NRF2 pathway
  JOURNAL   Cell Cycle 22 (12), 1496-1513 (2023)
   PUBMED   37245083
  REMARK    GeneRIF: TRIM13 inhibits cell proliferation and induces autophagy
            in lung adenocarcinoma by regulating KEAP1/NRF2 pathway.
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Roshanazadeh,M.R., Adelipour,M., Sanaei,A., Chenane,H. and
            Rashidi,M.
  TITLE     TRIM3 and TRIM16 as potential tumor suppressors in breast cancer
            patients
  JOURNAL   BMC Res Notes 15 (1), 312 (2022)
   PUBMED   36180926
  REMARK    GeneRIF: TRIM3 and TRIM16 as potential tumor suppressors in breast
            cancer patients.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Li,Y., Ren,D., Shen,Y., Zheng,X. and Xu,G.
  TITLE     Altered DNA methylation of TRIM13 in diabetic nephropathy
            suppresses mesangial collagen synthesis by promoting ubiquitination
            of CHOP
  JOURNAL   EBioMedicine 51, 102582 (2020)
   PUBMED   31901873
  REMARK    GeneRIF: Altered DNA methylation of TRIM13 in diabetic nephropathy
            suppresses mesangial collagen synthesis by promoting ubiquitination
            of CHOP.
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Xu,L., Wu,Q., Zhou,X., Wu,Q. and Fang,M.
  TITLE     TRIM13 inhibited cell proliferation and induced cell apoptosis by
            regulating NF-kappaB pathway in non-small-cell lung carcinoma cells
  JOURNAL   Gene 715, 144015 (2019)
   PUBMED   31357025
  REMARK    GeneRIF: results indicate that TRIM13 behaves as a tumor suppressor
            in non-small-cell lung carcinoma through regulating NF-kappaB
            pathway.
REFERENCE   6  (residues 1 to 407)
  AUTHORS   van Everdink,W.J., Baranova,A., Lummen,C., Tyazhelova,T.,
            Looman,M.W., Ivanov,D., Verlind,E., Pestova,A., Faber,H., van der
            Veen,A.Y., Yankovsky,N., Vellenga,E. and Buys,C.H.
  TITLE     RFP2, c13ORF1, and FAM10A4 are the most likely tumor suppressor
            gene candidates for B-cell chronic lymphocytic leukemia
  JOURNAL   Cancer Genet Cytogenet 146 (1), 48-57 (2003)
   PUBMED   14499696
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Migliazza,A., Bosch,F., Komatsu,H., Cayanis,E., Martinotti,S.,
            Toniato,E., Guccione,E., Qu,X., Chien,M., Murty,V.V., Gaidano,G.,
            Inghirami,G., Zhang,P., Fischer,S., Kalachikov,S.M., Russo,J.,
            Edelman,I., Efstratiadis,A. and Dalla-Favera,R.
  TITLE     Nucleotide sequence, transcription map, and mutation analysis of
            the 13q14 chromosomal region deleted in B-cell chronic lymphocytic
            leukemia
  JOURNAL   Blood 97 (7), 2098-2104 (2001)
   PUBMED   11264177
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Kapanadze,B., Makeeva,N., Corcoran,M., Jareborg,N., Hammarsund,M.,
            Baranova,A., Zabarovsky,E., Vorontsova,O., Merup,M., Gahrton,G.,
            Jansson,M., Yankovsky,N., Einhorn,S., Oscier,D., Grander,D. and
            Sangfelt,O.
  TITLE     Comparative sequence analysis of a region on human chromosome
            13q14, frequently deleted in B-cell chronic lymphocytic leukemia,
            and its homologous region on mouse chromosome 14
  JOURNAL   Genomics 70 (3), 327-334 (2000)
   PUBMED   11161783
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Kapanadze,B., Kashuba,V., Baranova,A., Rasool,O., van Everdink,W.,
            Liu,Y., Syomov,A., Corcoran,M., Poltaraus,A., Brodyansky,V.,
            Syomova,N., Kazakov,A., Ibbotson,R., van den Berg,A.,
            Gizatullin,R., Fedorova,L., Sulimova,G., Zelenin,A., Deaven,L.,
            Lehrach,H., Grander,D., Buys,C., Oscier,D., Zabarovsky,E.R.,
            Einhorn,S. and Yankovsky,N.
  TITLE     A cosmid and cDNA fine physical map of a human chromosome 13q14
            region frequently lost in B-cell chronic lymphocytic leukemia and
            identification of a new putative tumor suppressor gene, Leu5
  JOURNAL   FEBS Lett 426 (2), 266-270 (1998)
   PUBMED   9599022
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY455758.1, KF455768.1 and
            AL832695.1.
            
            Summary: This gene encodes a member of the tripartite motif (TRIM)
            family. The TRIM motif includes three zinc-binding domains, a RING,
            a B-box type 1 and a B-box type 2, and a coiled-coil region. This
            gene is located on chromosome 13 within the minimal deletion region
            for B-cell chronic lymphocytic leukemia. Multiple alternatively
            spliced transcript variants have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein (isoform
            1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY455758.1, SRR1803612.133511.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378182.4/ ENSP00000367424.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..407
                     /product="E3 ubiquitin-protein ligase TRIM13 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="ret finger protein 2; tripartite motif protein 13;
                     CLL-associated RING finger; tripartite motif-containing
                     protein 13; E3 ubiquitin-protein ligase TRIM13; RING
                     finger protein 77; leukemia-associated protein 5; putative
                     tumor suppressor RFP2; B-cell chronic lymphocytic leukemia
                     tumor suppressor Leu5; RING-type E3 ubiquitin transferase
                     TRIM13"
                     /calculated_mol_wt=46857
     Region          5..61
                     /region_name="RING-HC_TRIM13_C-V"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 13 (TRIM13) and similar proteins;
                     cd16762"
                     /db_xref="CDD:438418"
     Region          92..133
                     /region_name="Bbox2_TRIM13_C-XI"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 13 (TRIM13) and similar proteins;
                     cd19767"
                     /db_xref="CDD:380825"
     Site            317..337
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60858.2)"
     CDS             1..407
                     /gene="TRIM13"
                     /gene_synonym="CAR; DLEU5; LEU5; RFP2; RNF77"
                     /coded_by="NM_213590.3:729..1952"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS9423.1"
                     /db_xref="GeneID:10206"
                     /db_xref="HGNC:HGNC:9976"
                     /db_xref="MIM:605661"
ORIGIN      
        1 melleedltc piccslfddp rvlpcshnfc kkclegileg svrnslwrpa pfkcptcrke
       61 tsatginslq vnyslkgive kynkikispk mpvckghlgq plnifcltdm qlicgicatr
      121 gehtkhvfcs iedayaqerd afeslfqsfe twrrgdalsr ldtletskrk slqlltkdsd
      181 kvkeffeklq htldqkknei lsdfetmkla vmqaydpein klntilqeqr mafniaeafk
      241 dvsepivflq qmqefrekik viketplpps nlpasplmkn fdtsqwedik lvdvdklslp
      301 qdtgtfiski pwsfyklfll illlglvivf gptmflewsl fddlatwkgc lsnfssyltk
      361 tadfieqsvf yweqvtdgff ifnerfknft lvvlnnvaef vckykll
//
LOCUS       NP_061821                462 aa            linear   PRI 27-APR-2025
DEFINITION  ERBB receptor feedback inhibitor 1 [Homo sapiens].
ACCESSION   NP_061821
VERSION     NP_061821.1
DBSOURCE    REFSEQ: accession NM_018948.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Wang,H., Liu,H., Lu,G., Tang,X., Luo,S., Du,M., Christiani,D.C. and
            Wei,Q.
  TITLE     Potentially functional variants of ERRFI1 in hypoxia-related genes
            predict survival of non-small cell lung cancer patients
  JOURNAL   Cancer Med 13 (15), e70073 (2024)
   PUBMED   39096122
  REMARK    GeneRIF: Potentially functional variants of ERRFI1 in
            hypoxia-related genes predict survival of non-small cell lung
            cancer patients.
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Kondo,N., Utsumi,T., Shimizu,Y., Takemoto,A., Oh-Hara,T.,
            Uchibori,K., Subat-Motoshi,S., Ninomiya,H., Takeuchi,K., Nishio,M.,
            Miyazaki,Y. and Katayama,R.
  TITLE     MIG6 loss confers resistance to ALK/ROS1 inhibitors in NSCLC
            through EGFR activation by low-dose EGF
  JOURNAL   JCI Insight 8 (24), e173688 (2023)
   PUBMED   37917191
  REMARK    GeneRIF: MIG6 loss confers resistance to ALK/ROS1 inhibitors in
            NSCLC through EGFR activation by low-dose EGF.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Jeong,O., Broaddus,R.R., Lessey,B.A., Risinger,J.I., Hunter,M.I.
            and Kim,T.H.
  TITLE     MIG-6 Is Critical for Progesterone Responsiveness in Human Complex
            Atypical Hyperplasia and Early-Stage Endometrial Cancer
  JOURNAL   Int J Mol Sci 23 (23), 14596 (2022)
   PUBMED   36498921
  REMARK    GeneRIF: MIG-6 Is Critical for Progesterone Responsiveness in Human
            Complex Atypical Hyperplasia and Early-Stage Endometrial Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Kan,Y. and Miller,W.T.
  TITLE     Activity of the nonreceptor tyrosine kinase Ack1 is regulated by
            tyrosine phosphorylation of its Mig6 homology region
  JOURNAL   FEBS Lett 596 (21), 2808-2820 (2022)
   PUBMED   36178070
  REMARK    GeneRIF: Activity of the nonreceptor tyrosine kinase Ack1 is
            regulated by tyrosine phosphorylation of its Mig6 homology region.
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Li,C., Edeni,D., Platkin,S., Liu,R., Li,J., Hossain,M., Rahman,M.,
            Islam,H., Phillips,J.L. and Xu,D.
  TITLE     Effect of Gene 33/Mig6/ERRFI1 on hexavalent chromium-induced
            transformation of human bronchial epithelial cells depends on the
            length of exposure
  JOURNAL   J Environ Sci Health C Toxicol Carcinog 40 (3-4), 227-247 (2022)
   PUBMED   36715065
  REMARK    GeneRIF: Effect of Gene 33/Mig6/ERRFI1 on hexavalent
            chromium-induced transformation of human bronchial epithelial cells
            depends on the length of exposure.
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Hackel,P.O., Gishizky,M. and Ullrich,A.
  TITLE     Mig-6 is a negative regulator of the epidermal growth factor
            receptor signal
  JOURNAL   Biol Chem 382 (12), 1649-1662 (2001)
   PUBMED   11843178
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Fiorentino,L., Pertica,C., Fiorini,M., Talora,C., Crescenzi,M.,
            Castellani,L., Alema,S., Benedetti,P. and Segatto,O.
  TITLE     Inhibition of ErbB-2 mitogenic and transforming activity by RALT, a
            mitogen-induced signal transducer which binds to the ErbB-2 kinase
            domain
  JOURNAL   Mol Cell Biol 20 (20), 7735-7750 (2000)
   PUBMED   11003669
  REMARK    GeneRIF: MIG-6/RALT is a transcriptionally controlled inhibitor of
            mitogenic and transforming signals generated by the ErbB-2
            oncogene. MIG-6/RALT forms a physical complex with activated ErbB-2
            and co-localizes with ErbB-2 in living cells.
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Makkinje,A., Quinn,D.A., Chen,A., Cadilla,C.L., Force,T.,
            Bonventre,J.V. and Kyriakis,J.M.
  TITLE     Gene 33/Mig-6, a transcriptionally inducible adapter protein that
            binds GTP-Cdc42 and activates SAPK/JNK. A potential marker
            transcript for chronic pathologic conditions, such as diabetic
            nephropathy. Possible role in the response to persistent stress
  JOURNAL   J Biol Chem 275 (23), 17838-17847 (2000)
   PUBMED   10749885
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Wick,M., Burger,C., Funk,M. and Muller,R.
  TITLE     Identification of a novel mitogen-inducible gene (mig-6):
            regulation during G1 progression and differentiation
  JOURNAL   Exp Cell Res 219 (2), 527-535 (1995)
   PUBMED   7641805
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Chrapkiewicz,N.B., Davis,C.M., Chu,D.T., Caldwell,C.M. and
            Granner,D.K.
  TITLE     Rat gene 33: analysis of its structure, messenger RNA and basal
            promoter activity
  JOURNAL   Nucleic Acids Res 17 (16), 6651-6667 (1989)
   PUBMED   2780291
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB033666.1, AK096149.1, BC025337.1 and AL137274.1.
            
            Summary: ERRFI1 is a cytoplasmic protein whose expression is
            upregulated with cell growth (Wick et al., 1995 [PubMed 7641805]).
            It shares significant homology with the protein product of rat
            gene-33, which is induced during cell stress and mediates cell
            signaling (Makkinje et al., 2000 [PubMed 10749885]; Fiorentino et
            al., 2000 [PubMed 11003669]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.181073.1, AK096149.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151405 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377482.10/ ENSP00000366702.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.23"
     Protein         1..462
                     /product="ERBB receptor feedback inhibitor 1"
                     /note="receptor-associated late transducer;
                     mitogen-inducible gene 6 protein"
                     /calculated_mol_wt=50429
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Region          6..69
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JZ7; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JZ7; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Region          225..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JZ7; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Region          315..367
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          334..363
                     /region_name="Interaction with EGFR and ERBB2 and
                     regulation of EGFR activation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Region          415..448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UJM3.1)"
     CDS             1..462
                     /gene="ERRFI1"
                     /gene_synonym="GENE-33; MIG-6; MIG6; RALT"
                     /coded_by="NM_018948.4:226..1614"
                     /db_xref="CCDS:CCDS94.1"
                     /db_xref="GeneID:54206"
                     /db_xref="HGNC:HGNC:18185"
                     /db_xref="MIM:608069"
ORIGIN      
        1 msiagvaaqe irvplktgfl hngramgnmr ktywssrsef knnflnidpi tmayslnssa
       61 qerliplgha sksapmnghc faengpsqks slppllipps enlgpheedq vvcgfkkltv
      121 ngvcastppl tpiknspslf pcaplcergs rplpplpise alslddtdce vefltssdtd
      181 flledstlsd fkydvpgrrs frgcgqinya yfdtpavsaa dlsyvsdqng gvpdpnpppp
      241 qthrrlrrsh sgpagsfnkp airisnccih raspnsdedk pevpprvpip prpvkpdyrr
      301 wsaevtssty sdedrppkvp preplspsns rtpspkslps ylngvmpptq sfapdpkyvs
      361 skalqrqnse gsaskvpcil piiengkkvs sthyyllper ppyldkyekf freaeetngg
      421 aqiqplpadc gissatekpd sktkmdlggh vkrkhlsyvv sp
//
LOCUS       NP_001107               1353 aa            linear   PRI 27-APR-2025
DEFINITION  adenylate cyclase type 9 [Homo sapiens].
ACCESSION   NP_001107
VERSION     NP_001107.2
DBSOURCE    REFSEQ: accession NM_001116.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1353)
  AUTHORS   Teixeira,H.M.P., Cruz,A.A., Jesus,T.S., de Santana,M.B.R.,
            Jesus,M.S., Tugores,R., Araujo,W.S., Reis,R.C.C., Pinheiro,G.P.,
            Figueiredo,C.A. and Costa,R.S.
  TITLE     The rs2601796 variant in ADCY9 gene is associated with severe
            asthma and less bronchodilator response
  JOURNAL   Gene 886, 147714 (2023)
   PUBMED   37579959
  REMARK    GeneRIF: The rs2601796 variant in ADCY9 gene is associated with
            severe asthma and less bronchodilator response.
REFERENCE   2  (residues 1 to 1353)
  AUTHORS   Chen,Z. and Antoni,F.A.
  TITLE     Human adenylyl cyclase 9 is auto-stimulated by its isoform-specific
            C-terminal domain
  JOURNAL   Life Sci Alliance 6 (4), e202201791 (2023)
   PUBMED   36657828
  REMARK    GeneRIF: Human adenylyl cyclase 9 is auto-stimulated by its
            isoform-specific C-terminal domain.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1353)
  AUTHORS   Jia,J.J., Wei,B., Li,L.X., Ren,M.Y., Zhang,S.N., Liu,J. and
            Zhang,Y.X.
  TITLE     [Association of the ADCY9 gene and gene-environmental interaction
            with the susceptibility to childhood bronchial asthma]
  JOURNAL   Zhongguo Dang Dai Er Ke Za Zhi 24 (9), 1027-1035 (2022)
   PUBMED   36111722
  REMARK    GeneRIF: [Association of the ADCY9 gene and gene-environmental
            interaction with the susceptibility to childhood bronchial
            asthma].', trans 'ADCY9.
REFERENCE   4  (residues 1 to 1353)
  AUTHORS   Gamache,I., Legault,M.A., Grenier,J.C., Sanchez,R., Rheaume,E.,
            Asgari,S., Barhdadi,A., Zada,Y.F., Trochet,H., Luo,Y., Lecca,L.,
            Murray,M., Raychaudhuri,S., Tardif,J.C., Dube,M.P. and Hussin,J.
  TITLE     A sex-specific evolutionary interaction between ADCY9 and CETP
  JOURNAL   Elife 10, e69198 (2021)
   PUBMED   34609279
  REMARK    GeneRIF: A sex-specific evolutionary interaction between ADCY9 and
            CETP.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1353)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1353)
  AUTHORS   Paterson,J.M., Smith,S.M., Simpson,J., Grace,O.C., Sosunov,A.A.,
            Bell,J.E. and Antoni,F.A.
  TITLE     Characterisation of human adenylyl cyclase IX reveals inhibition by
            Ca(2+)/Calcineurin and differential mRNA plyadenylation
  JOURNAL   J Neurochem 75 (4), 1358-1367 (2000)
   PUBMED   10987815
REFERENCE   7  (residues 1 to 1353)
  AUTHORS   Hacker,B.M., Tomlinson,J.E., Wayman,G.A., Sultana,R., Chan,G.,
            Villacres,E., Disteche,C. and Storm,D.R.
  TITLE     Cloning, chromosomal mapping, and regulatory properties of the
            human type 9 adenylyl cyclase (ADCY9)
  JOURNAL   Genomics 50 (1), 97-104 (1998)
   PUBMED   9628827
REFERENCE   8  (residues 1 to 1353)
  AUTHORS   Tesmer,J.J., Sunahara,R.K., Gilman,A.G. and Sprang,S.R.
  TITLE     Crystal structure of the catalytic domains of adenylyl cyclase in a
            complex with Gsalpha.GTPgammaS
  JOURNAL   Science 278 (5345), 1907-1916 (1997)
   PUBMED   9417641
REFERENCE   9  (residues 1 to 1353)
  AUTHORS   Dessauer,C.W. and Gilman,A.G.
  TITLE     Purification and characterization of a soluble form of mammalian
            adenylyl cyclase
  JOURNAL   J Biol Chem 271 (28), 16967-16974 (1996)
   PUBMED   8663304
REFERENCE   10 (residues 1 to 1353)
  AUTHORS   Premont,R.T., Matsuoka,I., Mattei,M.G., Pouille,Y., Defer,N. and
            Hanoune,J.
  TITLE     Identification and characterization of a widely expressed form of
            adenylyl cyclase
  JOURNAL   J Biol Chem 271 (23), 13900-13907 (1996)
   PUBMED   8662814
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005736.1, AJ133123.1 and
            BQ614080.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 4, 2004 this sequence version replaced NP_001107.1.
            
            Summary: Adenylate cyclase is a membrane bound enzyme that
            catalyses the formation of cyclic AMP from ATP. It is regulated by
            a family of G protein-coupled receptors, protein kinases, and
            calcium. The type 9 adenylyl cyclase is a widely distributed
            adenylyl cyclase, and it is stimulated by beta-adrenergic receptor
            activation but is insensitive to forskolin, calcium, and
            somatostatin. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC151229.1, AB011092.3 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294016.8/ ENSP00000294016.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..1353
                     /product="adenylate cyclase type 9"
                     /EC_number="4.6.1.1"
                     /note="type IX ATP pyrophosphate-lyase; adenylyl cyclase
                     9; ATP pyrophosphate-lyase 9; adenylate cyclase type IX"
                     /calculated_mol_wt=150570
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Region          49..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            118..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            142..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Region          167..576
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
     Site            172..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     Site            216..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            242..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            281..301
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Region          349..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Region          385..573
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(397,399..404,439,441..443,446,508..510,514..515,
                     518..519,564)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(399,443)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(404,416,419..420,423,427,439..440,496,499,509..512,
                     515,564)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51830; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     Region          642..684
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51830; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     Site            691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51830; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     Site            706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     Site            787..807
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            819..839
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            868..888
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            892..912
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            921..941
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            955
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     Site            964
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     Site            976..996
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Region          1050..1241
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(1061,1063..1068,1108,1110..1112,1115,1185..1187,
                     1191..1192,1195..1196,1232)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(1063,1112)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(1068,1082,1085..1086,1089,1093,1108..1109,1173,1176,
                     1186..1189,1192,1232)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     Site            1257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     Site            1259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     Region          1292..1326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60503.4)"
     Site            1295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51830; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     Site            1307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60503.4)"
     CDS             1..1353
                     /gene="ADCY9"
                     /gene_synonym="AC9; ACIX"
                     /coded_by="NM_001116.4:797..4858"
                     /db_xref="CCDS:CCDS32382.1"
                     /db_xref="GeneID:115"
                     /db_xref="HGNC:HGNC:240"
                     /db_xref="MIM:603302"
ORIGIN      
        1 maspphqqll hhhstevscd ssgdsnsvrv kinpkqlssn shpkhckysi ssscsssgds
       61 ggvprrvggg grlrrqkklp qlferassrw wdpkfdsvnl eeaclercfp qtqrrfryal
      121 fyigfacllw siyfavhmrs rlivmvapal cfllvcvgff lftftklyar hyawtslalt
      181 llvfaltlaa qfqvltpvsg rgdssnltat arptdtclsq vgsfsmciev lfllytvmhl
      241 plylslclgv aysvlfetfg yhfrdeacfp spgagalhwe llsrgllhgc ihaigvhlfv
      301 msqvrsrstf lkvgqsimhg kdlevekalk ermihsvmpr iiaddlmkqg deesensvkr
      361 hatsspknrk kkssiqkapi afrpfkmqqi eevsilfadi vgftkmsank sahalvglln
      421 dlfgrfdrlc eetkcekist lgdcyycvag cpepradhay cciemglgmi kaieqfcqek
      481 kemvnmrvgv htgtvlcgil gmrrfkfdvw sndvnlanlm eqlgvagkvh iseatakyld
      541 dryemedgkv ierlgqsvva dqlkglktyl isgqrakesr cscaeallsg fevidgsqvs
      601 sgprgqgtas sgnvsdlaqt vktfdnlktc pscgitfapk seagaeggap qngcqdehkn
      661 stkasggpnp ktqngllspp qeekltnsqt slceilqekg rwagvsldqs allplrfkni
      721 rektdahfvd vikedslmkd yffkppinqf slnfldqele rsyrtsyqee viknspvktf
      781 asptfsslld vflsttvflt lsttcflkye aatvppppaa lavfsaalll evlslavsir
      841 mvffledvma ctkrllewia gwlprhciga ilvslpalav yshvtseyet nihfpvftgs
      901 aaliavvhyc nfcqlsswmr sslatvvgag pllllyvslc pdssvltspl davqnfsser
      961 npcnssvprd lrrpasligq evvlvfflll llvwflnref evsyrlhyhg dveadlhrtk
     1021 iqsmrdqadw llrniipyhv aeqlkvsqty sknhdsggvi fasivnfsef yeenyeggke
     1081 cyrvlnelig dfdellskpd yssiekikti gatymaasgl ntaqaqdgsh pqehlqilfe
     1141 fakemmrvvd dfnnnmlwfn fklrvgfnhg pltagvigtt kllydiwgdt vniasrmdtt
     1201 gvecriqvse esyrvlskmg ydfdyrgtvn vkgkgqmkty lypkctdhrv ipqhqlsisp
     1261 dirvqvdgsi grsptdeian lvpsvqyvdk tslgsdsstq akdahlspkr pwkepvkaee
     1321 rgrfgkaiek ddcdetgiee aneltklnvs ksv
//
LOCUS       NP_075048               1088 aa            linear   PRI 27-APR-2025
DEFINITION  ran-binding protein 17 [Homo sapiens].
ACCESSION   NP_075048
VERSION     NP_075048.1
DBSOURCE    REFSEQ: accession NM_022897.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Akter,M., Cui,H., Hosain,M.A., Liu,J., Duan,Y. and Ding,B.
  TITLE     RANBP17 Overexpression Restores Nucleocytoplasmic Transport and
            Ameliorates Neurodevelopment in Induced DYT1 Dystonia Motor Neurons
  JOURNAL   J Neurosci 44 (15), e1728232024 (2024)
   PUBMED   38438257
  REMARK    GeneRIF: RANBP17 Overexpression Restores Nucleocytoplasmic
            Transport and Ameliorates Neurodevelopment in Induced DYT1 Dystonia
            Motor Neurons.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Mandic,R., Marquardt,A., Terhorst,P., Ali,U., Nowak-Rossmann,A.,
            Cai,C., Rodepeter,F.R., Stiewe,T., Wezorke,B., Wanzel,M., Neff,A.,
            Stuck,B.A. and Bette,M.
  TITLE     The importin beta superfamily member RanBP17 exhibits a role in
            cell proliferation and is associated with improved survival of
            patients with HPV+ HNSCC
  JOURNAL   BMC Cancer 22 (1), 785 (2022)
   PUBMED   35850701
  REMARK    GeneRIF: The importin beta superfamily member RanBP17 exhibits a
            role in cell proliferation and is associated with improved survival
            of patients with HPV+ HNSCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   4  (residues 1 to 1088)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   5  (residues 1 to 1088)
  AUTHORS   Lee,J.H., Zhou,S. and Smas,C.M.
  TITLE     Identification of RANBP16 and RANBP17 as novel interaction partners
            for the bHLH transcription factor E12
  JOURNAL   J Cell Biochem 111 (1), 195-206 (2010)
   PUBMED   20503194
  REMARK    GeneRIF: These biochemical and functional data reveal RANBP16 and
            RANBP17 as novel regulators of E2A protein action, and demonstrate
            specific interaction of E12 with RANBP17.
REFERENCE   6  (residues 1 to 1088)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1088)
  AUTHORS   Kutay,U., Hartmann,E., Treichel,N., Calado,A., Carmo-Fonseca,M.,
            Prehn,S., Kraft,R., Gorlich,D. and Bischoff,F.R.
  TITLE     Identification of two novel RanGTP-binding proteins belonging to
            the importin beta superfamily
  JOURNAL   J Biol Chem 275 (51), 40163-40168 (2000)
   PUBMED   11024021
REFERENCE   8  (residues 1 to 1088)
  AUTHORS   Koch,P., Bohlmann,I., Schafer,M., Hansen-Hagge,T.E., Kiyoi,H.,
            Wilda,M., Hameister,H., Bartram,C.R. and Janssen,J.W.
  TITLE     Identification of a novel putative Ran-binding protein and its
            close homologue
  JOURNAL   Biochem Biophys Res Commun 278 (1), 241-249 (2000)
   PUBMED   11071879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC404010.1, AJ271459.1 and AC091980.4.
            
            Summary: The transport of protein and large RNAs through the
            nuclear pore complexes (NPC) is an energy-dependent and regulated
            process. The import of proteins with a nuclear localization signal
            (NLS) is accomplished by recognition of one or more clusters of
            basic amino acids by the importin-alpha/beta complex; see MIM
            600685 and MIM 602738. The small GTPase RAN (MIM 601179) plays a
            key role in NLS-dependent protein import. RAN-binding protein-17 is
            a member of the importin-beta superfamily of nuclear transport
            receptors.[supplied by OMIM, Jul 2002].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ271459.1, AF222747.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000523189.6/ ENSP00000427975.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.1"
     Protein         1..1088
                     /product="ran-binding protein 17"
                     /calculated_mol_wt=124245
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9UIA9; propagated from
                     UniProtKB/Swiss-Prot (Q9H2T7.1)"
     Region          8..>291
                     /region_name="CRM1"
                     /note="Importin beta-related nuclear transport receptor
                     [Nuclear structure / Intracellular trafficking and
                     secretion]; COG5101"
                     /db_xref="CDD:227432"
     Region          30..95
                     /region_name="IBN_N"
                     /note="Importin-beta N-terminal domain; smart00913"
                     /db_xref="CDD:197981"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UIA9; propagated from
                     UniProtKB/Swiss-Prot (Q9H2T7.1)"
     CDS             1..1088
                     /gene="RANBP17"
                     /coded_by="NM_022897.5:17..3283"
                     /db_xref="CCDS:CCDS34287.1"
                     /db_xref="GeneID:64901"
                     /db_xref="HGNC:HGNC:14428"
                     /db_xref="MIM:606141"
ORIGIN      
        1 malhfqslae levlcthlyi gtdltqriea ekallelids peclskcqll leqgttsyaq
       61 llaatclskl vsrvsplpve qrmdirnyil nyvasqpkla pfviqaliqv iakitklgwf
      121 evqkdqfvfr eiiadvkkfl qgtvehciig viilseltqe mnlvdysrps akhrkiatsf
      181 rdtslkdvlv lacsllkevf akplnlqdqc qqnlvmqvlk lvlnclnfdf igssadesad
      241 dlctvqiptt wrtiflepet ldlffnlyhs lppllsqlal sclvqfastr rslfnspera
      301 kylgnlikgv krilenpqgl sdpgnyhefc rflarlktny qlgelvmvke ypevirlian
      361 ftitslqhwe fapnsvhyll tlwqrmvasv pfvkstephl ldtyapeitk afitsrldsv
      421 aivvrdhldd plddtatvfq qleqlctvsr ceyektcall vqlfdqnaqn yqkllhpysg
      481 vtvditiqeg rlawlvylvg tvvggrltyt stdehdamdg elscrvfqli slmdtglprc
      541 cnekielail wfldqfrkty vgdqlqrtsk vyarmsevlg itddnhvlet fmtkivtnlk
      601 ywgryepvis rtlqflndls vgyillkklv kidavkfmlk nhtsehfpfl gisdnhslsd
      661 frcrttfyta ltrllmvdlg ededefenfm lpltvafetv lqifnnnfkq edvkrmligl
      721 ardlrgiafa lntktsytml fdwmyptylp llqnaverwy geptcttpil klmaelmqnr
      781 sqrlnfdvss pngillfrea skmvctygnq ilslgslskd qiypmklkgi sicysalksa
      841 lcgnyvsfgv fklygdnhfd nvlqafvkml lsvshsdllq yrklsqsyyp llecltqdhm
      901 sfiinleppv lmyvltsise glttldtvvs sscctsldyi vtylfkhiak egkkplrcre
      961 atqagqrllh fmqqnpdvlq qmmsvlmnti vfedcrnqws vsrpllglil lnekyfselr
     1021 aslinsqplp kqevlaqcfr nlmegveqnl svknrdrftq nlsvfrrdva ealrsdgnte
     1081 pcsldmms
//
LOCUS       NP_006205                338 aa            linear   PRI 27-APR-2025
DEFINITION  phytanoyl-CoA dioxygenase, peroxisomal isoform a precursor [Homo
            sapiens].
ACCESSION   NP_006205
VERSION     NP_006205.1
DBSOURCE    REFSEQ: accession NM_006214.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Daich Varela,M., Schiff,E., Malka,S., Wright,G., Mahroo,O.A.,
            Webster,A.R., Michaelides,M. and Arno,G.
  TITLE     PHYH c.678+5G>T Leads to In-Frame Exon Skipping and Is Associated
            With Attenuated Refsum Disease
  JOURNAL   Invest Ophthalmol Vis Sci 65 (2), 38 (2024)
   PUBMED   38411969
  REMARK    GeneRIF: PHYH c.678+5G>T Leads to In-Frame Exon Skipping and Is
            Associated With Attenuated Refsum Disease.
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Zhengqi,Q., Zezhi,G., Lei,J., He,Q., Jinyao,P. and Ying,A.
  TITLE     Prognostic role of PHYH for overall survival (OS) in clear cell
            renal cell carcinoma (ccRCC)
  JOURNAL   Eur J Med Res 26 (1), 9 (2021)
   PUBMED   33468235
  REMARK    GeneRIF: Prognostic role of PHYH for overall survival (OS) in clear
            cell renal cell carcinoma (ccRCC).
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Searls,T., Butler,D., Chien,W., Mukherji,M., Lloyd,M.D. and
            Schofield,C.J.
  TITLE     Studies on the specificity of unprocessed and mature forms of
            phytanoyl-CoA 2-hydroxylase and mutation of the iron binding
            ligands
  JOURNAL   J Lipid Res 46 (8), 1660-1667 (2005)
   PUBMED   15930519
  REMARK    GeneRIF: demonstrate that both unprocessed and processed forms are
            able to hydroxylate a range of CoA derivatives; site-directed
            mutagenesis was used to support proposals for the identity of the
            iron binding istes of PAHX
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Jansen,G.A., Wanders,R.J., Watkins,P.A. and Mihalik,S.J.
  TITLE     Phytanoyl-coenzyme A hydroxylase deficiency -- the enzyme defect in
            Refsum's disease
  JOURNAL   N Engl J Med 337 (2), 133-134 (1997)
   PUBMED   9221344
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Jansen,G.A., Mihalik,S.J., Watkins,P.A., Moser,H.W., Jakobs,C.,
            Denis,S. and Wanders,R.J.
  TITLE     Phytanoyl-CoA hydroxylase is present in human liver, located in
            peroxisomes, and deficient in Zellweger syndrome: direct,
            unequivocal evidence for the new, revised pathway of phytanic acid
            alpha-oxidation in humans
  JOURNAL   Biochem Biophys Res Commun 229 (1), 205-210 (1996)
   PUBMED   8954107
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Waterham,H.R., Wanders,R.J.A. and Leroy,B.P.
  TITLE     Adult Refsum Disease
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301527
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Skjeldal,O.H., Stokke,O., Refsum,S., Norseth,J. and Petit,H.
  TITLE     Clinical and biochemical heterogeneity in conditions with phytanic
            acid accumulation
  JOURNAL   J Neurol Sci 77 (1), 87-96 (1987)
   PUBMED   2433405
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC029512.1, AL138764.21 and
            BM351828.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the PhyH family and encodes a
            peroxisomal protein that is involved in the alpha-oxidation of
            3-methyl branched fatty acids. Specifically, this protein converts
            phytanoyl-CoA to 2-hydroxyphytanoyl-CoA. Mutations in this gene
            have been associated with Refsum disease (RD) and deficient protein
            activity has been associated with Zellweger syndrome and rhizomelic
            chondrodysplasia punctata. Alternate transcriptional splice
            variants, encoding different isoforms, have been characterized.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029512.1, SRR3476690.665677.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2146411
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263038.9/ ENSP00000263038.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..338
                     /product="phytanoyl-CoA dioxygenase, peroxisomal isoform a
                     precursor"
                     /EC_number="1.14.11.18"
                     /note="phytanoyl-CoA 2 oxoglutarate dioxygenase; phytanic
                     acid oxidase; phytanoyl-CoA alpha-hydroxylase;
                     phytanoil-CoA alpha hydroxylase; phytanoyl-CoA
                     dioxygenase, peroxisomal"
                     /calculated_mol_wt=35436
     transit_peptide 1..30
                     /note="PTS2 - peroxisomal targeting signal 2"
                     /calculated_mol_wt=3121
     mat_peptide     31..338
                     /product="phytanoyl-CoA dioxygenase, peroxisomal isoform
                     a"
                     /calculated_mol_wt=35436
     Region          61..277
                     /region_name="PhyH"
                     /note="Phytanoyl-CoA dioxygenase (PhyH); pfam05721"
                     /db_xref="CDD:399029"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O14832.1)"
     CDS             1..338
                     /gene="PHYH"
                     /gene_synonym="LN1; LNAP1; PAHX; PHYH1; RD"
                     /coded_by="NM_006214.4:23..1039"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS7097.1"
                     /db_xref="GeneID:5264"
                     /db_xref="HGNC:HGNC:8940"
                     /db_xref="MIM:602026"
ORIGIN      
        1 meqlraaarl qivlghlgrp sagavvahpt sgtissasfh pqqfqytldn nvltleqrkf
       61 yeengflvik nlvpdadiqr frnefekicr kevkplgltv mrdvtiskse yapsekmitk
      121 vqdfqedkel fryctlpeil kyvecftgpn imamhtmlin kppdsgkkts rhplhqdlhy
      181 fpfrpsdliv cawtamehis rnngclvvlp gthkgslkph dypkweggvn kmfhgiqdye
      241 enkarvhlvm ekgdtvffhp llihgsgqnk tqgfrkaisc hfasadchyi dvkgtsqeni
      301 ekevvgiahk ffgaensvnl kdiwmfrarl vkgertnl
//
LOCUS       NP_001348994             175 aa            linear   ROD 27-APR-2025
DEFINITION  EKC/KEOPS complex subunit Tprkb isoform a [Mus musculus].
ACCESSION   NP_001348994 XP_006506632
VERSION     NP_001348994.1
DBSOURCE    REFSEQ: accession NM_001362065.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Iwata,S., Sasaki,T., Nagahara,M. and Iwamoto,T.
  TITLE     An efficient i-GONAD method for creating and maintaining lethal
            mutant mice using an inversion balancer identified from the
            C3H/HeJJcl strain
  JOURNAL   G3 (Bethesda) 11 (8) (2021)
   PUBMED   34849815
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Braun,D.A., Rao,J., Mollet,G., Schapiro,D., Daugeron,M.C., Tan,W.,
            Gribouval,O., Boyer,O., Revy,P., Jobst-Schwan,T., Schmidt,J.M.,
            Lawson,J.A., Schanze,D., Ashraf,S., Ullmann,J.F.P.,
            Hoogstraten,C.A., Boddaert,N., Collinet,B., Martin,G., Liger,D.,
            Lovric,S., Furlano,M., Guerrera,I.C., Sanchez-Ferras,O., Hu,J.F.,
            Boschat,A.C., Sanquer,S., Menten,B., Vergult,S., De Rocker,N.,
            Airik,M., Hermle,T., Shril,S., Widmeier,E., Gee,H.Y., Choi,W.I.,
            Sadowski,C.E., Pabst,W.L., Warejko,J.K., Daga,A., Basta,T.,
            Matejas,V., Scharmann,K., Kienast,S.D., Behnam,B., Beeson,B.,
            Begtrup,A., Bruce,M., Ch'ng,G.S., Lin,S.P., Chang,J.H., Chen,C.H.,
            Cho,M.T., Gaffney,P.M., Gipson,P.E., Hsu,C.H., Kari,J.A., Ke,Y.Y.,
            Kiraly-Borri,C., Lai,W.M., Lemyre,E., Littlejohn,R.O., Masri,A.,
            Moghtaderi,M., Nakamura,K., Ozaltin,F., Praet,M., Prasad,C.,
            Prytula,A., Roeder,E.R., Rump,P., Schnur,R.E., Shiihara,T.,
            Sinha,M.D., Soliman,N.A., Soulami,K., Sweetser,D.A., Tsai,W.H.,
            Tsai,J.D., Topaloglu,R., Vester,U., Viskochil,D.H.,
            Vatanavicharn,N., Waxler,J.L., Wierenga,K.J., Wolf,M.T.F.,
            Wong,S.N., Leidel,S.A., Truglio,G., Dedon,P.C., Poduri,A., Mane,S.,
            Lifton,R.P., Bouchard,M., Kannu,P., Chitayat,D., Magen,D.,
            Callewaert,B., van Tilbeurgh,H., Zenker,M., Antignac,C. and
            Hildebrandt,F.
  TITLE     Mutations in KEOPS-complex genes cause nephrotic syndrome with
            primary microcephaly
  JOURNAL   Nat Genet 49 (10), 1529-1538 (2017)
   PUBMED   28805828
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Quina,L.A., Wang,S., Ng,L. and Turner,E.E.
  TITLE     Brn3a and Nurr1 mediate a gene regulatory pathway for habenula
            development
  JOURNAL   J Neurosci 29 (45), 14309-14322 (2009)
   PUBMED   19906978
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Daigo,Y., Takayama,I., Ward,S.M., Sanders,K.M. and Fujino,M.A.
  TITLE     Isolation of novel mouse genes that were differentially expressed
            in W/W(V) mouse fundus
  JOURNAL   J Gastroenterol 39 (3), 238-241 (2004)
   PUBMED   15065000
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Miyoshi,A., Kito,K., Aramoto,T., Abe,Y., Kobayashi,N. and Ueda,N.
  TITLE     Identification of CGI-121, a novel PRPK (p53-related protein
            kinase)-binding protein
  JOURNAL   Biochem Biophys Res Commun 303 (2), 399-405 (2003)
   PUBMED   12659830
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158679.8.
            
            On Apr 6, 2018 this sequence version replaced XP_006506632.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 3. Variants 1-5 all encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.274588.1,
                                           SRR7345562.290963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 37.53 cM"
     Protein         1..175
                     /product="EKC/KEOPS complex subunit Tprkb isoform a"
                     /note="TP53RK-binding protein; Prpk (p53-related protein
                     kinase)-binding protein; EKC/KEOPS complex subunit Tprkb;
                     PRPK-binding protein"
                     /calculated_mol_wt=19425
     Region          20..173
                     /region_name="CGI-121"
                     /note="Kinase binding protein CGI-121; pfam08617"
                     /db_xref="CDD:462537"
     CDS             1..175
                     /gene="Tprkb"
                     /gene_synonym="0610033G21Rik; 1810034M08Rik; Cgi-121;
                     DRWMS1; mDRWMS1"
                     /coded_by="NM_001362065.1:249..776"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS20305.1"
                     /db_xref="GeneID:69786"
                     /db_xref="MGI:MGI:1917036"
ORIGIN      
        1 mqlsqqldlf pecrvtlllf kdvknagdlr kkamegsidg slinpnvivd pfqilvaank
       61 avhlhrlgkm ktrtlsteii fnlspnnnis ealkkfgise tntsvlivyi edgskqvpqe
      121 hlvsqvegqq vpleslpeit rlsevkkiyk lssqeerigt lldaiicrms tkdvl
//
LOCUS       NP_444428                313 aa            linear   ROD 27-APR-2025
DEFINITION  sideroflexin-4 isoform 1 [Mus musculus].
ACCESSION   NP_444428
VERSION     NP_444428.3
DBSOURCE    REFSEQ: accession NM_053198.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Fleming,M.D., Campagna,D.R., Haslett,J.N., Trenor,C.C. 3rd and
            Andrews,N.C.
  TITLE     A mutation in a mitochondrial transmembrane protein is responsible
            for the pleiotropic hematological and skeletal phenotype of
            flexed-tail (f/f) mice
  JOURNAL   Genes Dev 15 (6), 652-657 (2001)
   PUBMED   11274051
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC102432.9 and AC163019.5.
            
            On Jul 29, 2009 this sequence version replaced NP_444428.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089535.1, AF325263.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 56.52 cM"
     Protein         1..313
                     /product="sideroflexin-4 isoform 1"
                     /calculated_mol_wt=35449
     Region          15..312
                     /region_name="SFXNs"
                     /note="Sideroflexins; cl04275"
                     /db_xref="CDD:470990"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N1.2)"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N1.2)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6P4A7; propagated from
                     UniProtKB/Swiss-Prot (Q925N1.2)"
     Site            175..191
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N1.2)"
     Site            230..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N1.2)"
     Site            269..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N1.2)"
     CDS             1..313
                     /gene="Sfxn4"
                     /coded_by="NM_053198.4:92..1033"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS29943.1"
                     /db_xref="GeneID:94281"
                     /db_xref="MGI:MGI:2137680"
ORIGIN      
        1 mepnlqfwis erqaffrrfc qwmdlldpvn mfisigsiek srqllftted apkhyldnqv
       61 ikdawnksls tvhpdsskli phlfrpaafl pvtapmvfll mmpdtgiksi iltqgclygy
      121 ttafnitngn asyshgpver tllgagvsvs stfigliphl fqmkyppnnf wlkrtlpivf
      181 laqvsgmnvf asrsfenhrg ievmdkeghv vghsrkagrk aikdtaksra vlfgtsalap
      241 elfihifkrt rfypqtllsl vilrmsstff mmglmvpvsf smfpqigqiq csqleekiqs
      301 steekelfyy rgv
//
LOCUS       NP_001352844             965 aa            linear   PRI 27-APR-2025
DEFINITION  SKI family transcriptional corepressor 1 [Homo sapiens].
ACCESSION   NP_001352844 XP_016877662
VERSION     NP_001352844.1
DBSOURCE    REFSEQ: accession NM_001365915.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 965)
  AUTHORS   Morales-Prieto,N., Bevans,R., O'Mahony,A., Barron,A., Giles
            Doran,C., McCarthy,E., Concannon,R.M., Goulding,S.R.,
            McCarthy,C.M., Collins,L.M., Sullivan,A.M. and O'Keeffe,G.W.
  TITLE     Human alpha-synuclein overexpression upregulates SKOR1 in a rat
            model of simulated nigrostriatal ageing
  JOURNAL   Aging Cell 23 (6), e14155 (2024)
   PUBMED   38529808
  REMARK    GeneRIF: Human alpha-synuclein overexpression upregulates SKOR1 in
            a rat model of simulated nigrostriatal ageing.
REFERENCE   2  (residues 1 to 965)
  AUTHORS   Sarayloo,F., Spiegelman,D., Rochefort,D., Akcimen,F., De Barros
            Oliveira,R., Dion,P.A. and Rouleau,G.A.
  TITLE     SKOR1 has a transcriptional regulatory role on genes involved in
            pathways related to restless legs syndrome
  JOURNAL   Eur J Hum Genet 28 (11), 1520-1528 (2020)
   PUBMED   32572201
  REMARK    GeneRIF: SKOR1 has a transcriptional regulatory role on genes
            involved in pathways related to restless legs syndrome.
REFERENCE   3  (residues 1 to 965)
  AUTHORS   Chen,J., Huang,P., He,Y., Shen,J., Du,J., Cui,S., Cui,P., Chen,S.
            and Ma,J.
  TITLE     A haplotype of MAP2K5/SKOR1 was associated with essential tremor in
            Chinese population
  JOURNAL   Parkinsonism Relat Disord 53, 118-119 (2018)
   PUBMED   29798820
  REMARK    GeneRIF: MAP2K5/SKOR1 may be associated with Chinese essential
            tremor patients.
REFERENCE   4  (residues 1 to 965)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   5  (residues 1 to 965)
  AUTHORS   Winkelmann,J., Czamara,D., Schormair,B., Knauf,F., Schulte,E.C.,
            Trenkwalder,C., Dauvilliers,Y., Polo,O., Hogl,B., Berger,K.,
            Fuhs,A., Gross,N., Stiasny-Kolster,K., Oertel,W., Bachmann,C.G.,
            Paulus,W., Xiong,L., Montplaisir,J., Rouleau,G.A., Fietze,I.,
            Vavrova,J., Kemlink,D., Sonka,K., Nevsimalova,S., Lin,S.C.,
            Wszolek,Z., Vilarino-Guell,C., Farrer,M.J., Gschliesser,V.,
            Frauscher,B., Falkenstetter,T., Poewe,W., Allen,R.P., Earley,C.J.,
            Ondo,W.G., Le,W.D., Spieler,D., Kaffe,M., Zimprich,A., Kettunen,J.,
            Perola,M., Silander,K., Cournu-Rebeix,I., Francavilla,M.,
            Fontenille,C., Fontaine,B., Vodicka,P., Prokisch,H., Lichtner,P.,
            Peppard,P., Faraco,J., Mignot,E., Gieger,C., Illig,T.,
            Wichmann,H.E., Muller-Myhsok,B. and Meitinger,T.
  TITLE     Genome-wide association study identifies novel restless legs
            syndrome susceptibility loci on 2p14 and 16q12.1
  JOURNAL   PLoS Genet 7 (7), e1002171 (2011)
   PUBMED   21779176
  REMARK    Erratum:[PLoS Genet. 2011 Aug;7(8). doi:
            10.1371/annotation/393ad2d3-df4f-4770-87bc-00bfabf79362]
REFERENCE   6  (residues 1 to 965)
  AUTHORS   Kemlink,D., Polo,O., Frauscher,B., Gschliesser,V., Hogl,B.,
            Poewe,W., Vodicka,P., Vavrova,J., Sonka,K., Nevsimalova,S.,
            Schormair,B., Lichtner,P., Silander,K., Peltonen,L., Gieger,C.,
            Wichmann,H.E., Zimprich,A., Roeske,D., Muller-Myhsok,B.,
            Meitinger,T. and Winkelmann,J.
  TITLE     Replication of restless legs syndrome loci in three European
            populations
  JOURNAL   J Med Genet 46 (5), 315-318 (2009)
   PUBMED   19279021
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 965)
  AUTHORS   Winkelmann,J.
  TITLE     Genetics of restless legs syndrome
  JOURNAL   Curr Neurol Neurosci Rep 8 (3), 211-216 (2008)
   PUBMED   18541116
  REMARK    GeneRIF: MEIS1 and LBXCOR1 are developmental factors and raise new
            pathophysiologic questions for RLS.
            Review article
REFERENCE   8  (residues 1 to 965)
  AUTHORS   Winkelmann,J., Schormair,B., Lichtner,P., Ripke,S., Xiong,L.,
            Jalilzadeh,S., Fulda,S., Putz,B., Eckstein,G., Hauk,S.,
            Trenkwalder,C., Zimprich,A., Stiasny-Kolster,K., Oertel,W.,
            Bachmann,C.G., Paulus,W., Peglau,I., Eisensehr,I., Montplaisir,J.,
            Turecki,G., Rouleau,G., Gieger,C., Illig,T., Wichmann,H.E.,
            Holsboer,F., Muller-Myhsok,B. and Meitinger,T.
  TITLE     Genome-wide association study of restless legs syndrome identifies
            common variants in three genomic regions
  JOURNAL   Nat Genet 39 (8), 1000-1006 (2007)
   PUBMED   17637780
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 965)
  AUTHORS   Arndt,S., Poser,I., Moser,M. and Bosserhoff,A.K.
  TITLE     Fussel-15, a novel Ski/Sno homolog protein, antagonizes BMP
            signaling
  JOURNAL   Mol Cell Neurosci 34 (4), 603-611 (2007)
   PUBMED   17292623
  REMARK    GeneRIF: a novel gene, fussel-15 (functional smad suppressing
            element on chromosome 15) with high homology to the recently
            discovered Fussel-18 protein.
REFERENCE   10 (residues 1 to 965)
  AUTHORS   Mizuhara,E., Nakatani,T., Minaki,Y., Sakamoto,Y. and Ono,Y.
  TITLE     Corl1, a novel neuronal lineage-specific transcriptional
            corepressor for the homeodomain transcription factor Lbx1
  JOURNAL   J Biol Chem 280 (5), 3645-3655 (2005)
   PUBMED   15528197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009292.11.
            
            On Sep 15, 2018 this sequence version replaced XP_016877662.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000380035.3/ ENSP00000369374.2
            RefSeq Select criteria    :: based on single protein-coding
                                         transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q23"
     Protein         1..965
                     /product="SKI family transcriptional corepressor 1"
                     /note="corepressor for LBX1; ladybird homeobox corepressor
                     1; transcriptional corepressor CORL1; LBX1 corepressor 1;
                     functional Smad-suppressing element on chromosome 15;
                     Lbxcor1 homolog"
                     /calculated_mol_wt=99700
     Region          45..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84550.1)"
     Region          77..167
                     /region_name="DHD_Skor"
                     /note="Dachshund-homology domain found in SKI family
                     transcriptional corepressors, Skor1, Skor2 and similar
                     proteins; cd21080"
                     /db_xref="CDD:410783"
     Region          180..272
                     /region_name="c-SKI_SMAD_bind"
                     /note="c-SKI Smad4 binding domain; smart01046"
                     /db_xref="CDD:198114"
     Region          278..367
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84550.1)"
     Region          410..458
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84550.1)"
     Region          530..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84550.1)"
     Region          615..777
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84550.1)"
     Region          <659..846
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          796..843
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84550.1)"
     Region          861..>936
                     /region_name="OmpH"
                     /note="Outer membrane protein (OmpH-like); pfam03938"
                     /db_xref="CDD:461098"
     CDS             1..965
                     /gene="SKOR1"
                     /gene_synonym="CORL1; FUSSEL15; LBXCOR1"
                     /coded_by="NM_001365915.1:95..2992"
                     /db_xref="CCDS:CCDS92030.1"
                     /db_xref="GeneID:390598"
                     /db_xref="HGNC:HGNC:21326"
                     /db_xref="MIM:611273"
ORIGIN      
        1 mallcglgqv tlriwvslps qsengigfla araflrsggm ealttqlgpg regssspnsk
       61 qelqpysgss alkpnqvget slygvpivsl vidgqerlcl aqisntllkn ysyneihnrr
      121 valgitcvqc tpvqleilrr agampissrr cgmitkreae rlcksflgeh kppklpenfa
      181 fdvvhecawg srgsfipary nssrakcikc gycsmyfspn kfifhshrtp dakytqpdaa
      241 nfnswrrhlk lsdksatdel shawedvkam fnggtrkrtf slqgggggga nggsggqgkg
      301 gagggggggp gcgaemapgp pphkslrcge deaagppgpp pphpqrglgl atgasgpagp
      361 ggpgggagvr sypvipvpsk gfgllqklpp plfphpygfp tafglcpkkd dpvlgagepk
      421 ggpgtgsggg gagtgggagg pgashlppga gagpgggamf wghqpsgaak daaavaaaaa
      481 aatvyptfpm fwpaagslpv psypaaqsqa kavaaavaaa aaaaaaaags gapepldgae
      541 pakesglgae ercpsalsrg pldedgtdea lppplaplpp ppppparkgs yvsafrpvvk
      601 dtesiaklyg sareaygagp argpgpgags ggyvspdfls egsssynsas pdvdtadepe
      661 vdvesnrfpd dedaqeetep sapsagggpd geqptgppsa tssgadgpan spdggsprpr
      721 rrlgpppagr pafgdlaaed lvrrperspp sggggyelre pcgplggpap akvfaperde
      781 hvksaavalg paasyvctpe ahepdkednh spaddletrk sypdqrsisq pspantdrge
      841 dgltldvtgt hlvekdienl areelqklll eqmelrkkle refqslkdnf qdqmkrelay
      901 reemvqqlqi vrdtlcneld qerkaryaiq qklkeahdal hhfsckmltp rhctgncsfk
      961 ppllp
//
LOCUS       NP_056277                719 aa            linear   PRI 27-APR-2025
DEFINITION  nucleolar protein 11 isoform 1 [Homo sapiens].
ACCESSION   NP_056277
VERSION     NP_056277.2
DBSOURCE    REFSEQ: accession NM_015462.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   McCool,M.A., Bryant,C.J., Huang,H., Ogawa,L.M., Farley-Barnes,K.I.,
            Sondalle,S.B., Abriola,L., Surovtseva,Y.V. and Baserga,S.J.
  TITLE     Human nucleolar protein 7 (NOL7) is required for early pre-rRNA
            accumulation and pre-18S rRNA processing
  JOURNAL   RNA Biol 20 (1), 257-271 (2023)
   PUBMED   37246770
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Fujimura,A., Hayashi,Y., Kato,K., Kogure,Y., Kameyama,M.,
            Shimamoto,H., Daitoku,H., Fukamizu,A., Hirota,T. and Kimura,K.
  TITLE     Identification of a novel nucleolar protein complex required for
            mitotic chromosome segregation through centromeric accumulation of
            Aurora B
  JOURNAL   Nucleic Acids Res 48 (12), 6583-6596 (2020)
   PUBMED   32479628
  REMARK    GeneRIF: Identification of a novel nucleolar protein complex
            required for mitotic chromosome segregation through centromeric
            accumulation of Aurora B.
REFERENCE   5  (residues 1 to 719)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 719)
  AUTHORS   Carvill,G.L., Weckhuysen,S., McMahon,J.M., Hartmann,C.,
            Moller,R.S., Hjalgrim,H., Cook,J., Geraghty,E., O'Roak,B.J.,
            Petrou,S., Clarke,A., Gill,D., Sadleir,L.G., Muhle,H., von
            Spiczak,S., Nikanorova,M., Hodgson,B.L., Gazina,E.V., Suls,A.,
            Shendure,J., Dibbens,L.M., De Jonghe,P., Helbig,I., Berkovic,S.F.,
            Scheffer,I.E. and Mefford,H.C.
  TITLE     GABRA1 and STXBP1: novel genetic causes of Dravet syndrome
  JOURNAL   Neurology 82 (14), 1245-1253 (2014)
   PUBMED   24623842
REFERENCE   7  (residues 1 to 719)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 719)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 719)
  AUTHORS   Freed,E.F., Prieto,J.L., McCann,K.L., McStay,B. and Baserga,S.J.
  TITLE     NOL11, implicated in the pathogenesis of North American Indian
            childhood cirrhosis, is required for pre-rRNA transcription and
            processing
  JOURNAL   PLoS Genet 8 (8), e1002892 (2012)
   PUBMED   22916032
  REMARK    GeneRIF: NOL11 is a novel protein required for the early stages of
            ribosome biogenesis in humans and is implicated in the pathogenesis
            of North American Indian childhood cirrhosis.
REFERENCE   10 (residues 1 to 719)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA772356.1, AK023702.1, AK299483.1, AW273123.1 and AC006534.10.
            
            On Jun 10, 2002 this sequence version replaced NP_056277.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.20070.1,
                                           SRR1803613.1671.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253247.9/ ENSP00000253247.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..719
                     /product="nucleolar protein 11 isoform 1"
                     /calculated_mol_wt=80993
     Region          200..243
                     /region_name="NUC205"
                     /note="NUC205 domain; pfam08168"
                     /db_xref="CDD:429856"
     Site            346
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H8H0.1)"
     CDS             1..719
                     /gene="NOL11"
                     /coded_by="NM_015462.5:13..2172"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11671.1"
                     /db_xref="GeneID:25926"
                     /db_xref="HGNC:HGNC:24557"
                     /db_xref="MIM:615366"
ORIGIN      
        1 maaleeeftl ssvvlsagpe gllgveqsdk tdqflvtdsg rtvilykvsd qkplgswsvk
       61 qgqiitcpav cnfqtgeyvv vhdnkvlriw nnedvnldkv fkatlsaevy rilsvqgtep
      121 lvlfkegavr glealladpq qkietvisde evikwtkffv vfrhpvlifi tekhgnyfay
      181 vqmfnsrilt kytlllgqde nsviksftas vdrkfislms lssdgciyet lipirpadpe
      241 knqslvksll lkavvsgnar ngvaltaldq dhvavlgspl aaskeclsvw nikfqtlqts
      301 kelpqgtsgq lwyygehlfm lhgksltvip ykcevsslag algklkhsqd pgthvvshfv
      361 nwetpqgcgl gfqnseqsrr ilrrrkievs lqpevppskq llstimkdse khievevrkf
      421 lalkqtpdfh tvigdtvtgl lerckaepsf yprnclmqli qthvlsyslc pdlmeialkk
      481 kdvqllqlcl qqfpdipesv tcaclkifls igddslqetd vnmesvfdys insvhdekme
      541 eqteilqngf npeedkcnnc dqelnkkpqd etkestscpv vqkraallna ilhsaysetf
      601 llphlkdipa qhitlflkyl yflylkcsen atmtlpgihp ptlnqimdwi cllldanftv
      661 vvmmpeakrl linlyklvks qisvyselnk ievsfrelqk lnqeknnrgl ysievlelf
//
LOCUS       NP_789811               1845 aa            linear   ROD 27-APR-2025
DEFINITION  girdin isoform 3 [Mus musculus].
ACCESSION   NP_789811 NP_795963 XP_484001
VERSION     NP_789811.2
DBSOURCE    REFSEQ: accession NM_176841.5
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1845)
  AUTHORS   Wang,H., Yuan,Y.C., Chang,C., Izumi,T., Wang,H.H. and Yang,J.K.
  TITLE     The signaling protein GIV/Girdin mediates the Nephrin-dependent
            insulin secretion of pancreatic islet beta cells in response to
            high glucose
  JOURNAL   J Biol Chem 299 (4), 103045 (2023)
   PUBMED   36822326
REFERENCE   2  (residues 1 to 1845)
  AUTHORS   Reynoso,S., Castillo,V., Katkar,G.D., Lopez-Sanchez,I., Taheri,S.,
            Espinoza,C., Rohena,C., Sahoo,D., Gagneux,P. and Ghosh,P.
  TITLE     GIV/Girdin, a non-receptor modulator for Galphai/s, regulates
            spatiotemporal signaling during sperm capacitation and is required
            for male fertility
  JOURNAL   Elife 10, e69160 (2021)
   PUBMED   34409938
  REMARK    GeneRIF: GIV/Girdin, a non-receptor modulator for Galphai/s,
            regulates spatiotemporal signaling during sperm capacitation and is
            required for male fertility.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1845)
  AUTHORS   Swanson,L., Katkar,G.D., Tam,J., Pranadinata,R.F., Chareddy,Y.,
            Coates,J., Anandachar,M.S., Castillo,V., Olson,J., Nizet,V.,
            Kufareva,I., Das,S. and Ghosh,P.
  TITLE     TLR4 signaling and macrophage inflammatory responses are dampened
            by GIV/Girdin
  JOURNAL   Proc Natl Acad Sci U S A 117 (43), 26895-26906 (2020)
   PUBMED   33055214
  REMARK    GeneRIF: TLR4 signaling and macrophage inflammatory responses are
            dampened by GIV/Girdin.
REFERENCE   4  (residues 1 to 1845)
  AUTHORS   Pan,S., Ren,F., Li,L., Liu,D., Li,Y., Wang,A., Li,W., Dong,Y. and
            Guo,W.
  TITLE     MiR-328-3p inhibits cell proliferation and metastasis in colorectal
            cancer by targeting Girdin and inhibiting the PI3K/Akt signaling
            pathway
  JOURNAL   Exp Cell Res 390 (1), 111939 (2020)
   PUBMED   32142853
  REMARK    GeneRIF: MiR-328-3p inhibits cell proliferation and metastasis in
            colorectal cancer by targeting Girdin and inhibiting the PI3K/Akt
            signaling pathway.
REFERENCE   5  (residues 1 to 1845)
  AUTHORS   Weng,L., Han,Y.P., Enomoto,A., Kitaura,Y., Nagamori,S., Kanai,Y.,
            Asai,N., An,J., Takagishi,M., Asai,M., Mii,S., Masuko,T.,
            Shimomura,Y. and Takahashi,M.
  TITLE     Negative regulation of amino acid signaling by MAPK-regulated
            4F2hc/Girdin complex
  JOURNAL   PLoS Biol 16 (3), e2005090 (2018)
   PUBMED   29538402
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1845)
  AUTHORS   Jiang,P., Enomoto,A., Jijiwa,M., Kato,T., Hasegawa,T., Ishida,M.,
            Sato,T., Asai,N., Murakumo,Y. and Takahashi,M.
  TITLE     An actin-binding protein Girdin regulates the motility of breast
            cancer cells
  JOURNAL   Cancer Res 68 (5), 1310-1318 (2008)
   PUBMED   18316593
  REMARK    GeneRIF: Girdin has an important role in tumor progression with
            aberrant activation of the Akt signaling pathway
REFERENCE   7  (residues 1 to 1845)
  AUTHORS   Kitamura,T., Asai,N., Enomoto,A., Maeda,K., Kato,T., Ishida,M.,
            Jiang,P., Watanabe,T., Usukura,J., Kondo,T., Costantini,F.,
            Murohara,T. and Takahashi,M.
  TITLE     Regulation of VEGF-mediated angiogenesis by the Akt/PKB substrate
            Girdin
  JOURNAL   Nat Cell Biol 10 (3), 329-337 (2008)
   PUBMED   18264090
  REMARK    GeneRIF: the Akt/Girdin signalling pathway is essential in
            VEGF-mediated postneonatal angiogenesis
REFERENCE   8  (residues 1 to 1845)
  AUTHORS   Le-Niculescu,H., Niesman,I., Fischer,T., DeVries,L. and
            Farquhar,M.G.
  TITLE     Identification and characterization of GIV, a novel Galpha
            i/s-interacting protein found on COPI, endoplasmic reticulum-Golgi
            transport vesicles
  JOURNAL   J Biol Chem 280 (23), 22012-22020 (2005)
   PUBMED   15749703
REFERENCE   9  (residues 1 to 1845)
  AUTHORS   Simpson,F., Martin,S., Evans,T.M., Kerr,M., James,D.E.,
            Parton,R.G., Teasdale,R.D. and Wicking,C.
  TITLE     A novel hook-related protein family and the characterization of
            hook-related protein 1
  JOURNAL   Traffic 6 (6), 442-458 (2005)
   PUBMED   15882442
  REMARK    GeneRIF: HkRP1 (A430106J12Rik) is involved in the process of
            tubulation of sorting nexin-1 positive membranes from early
            endosome subdomains.
REFERENCE   10 (residues 1 to 1845)
  AUTHORS   Anai,M., Shojima,N., Katagiri,H., Ogihara,T., Sakoda,H., Onishi,Y.,
            Ono,H., Fujishiro,M., Fukushima,Y., Horike,N., Viana,A.,
            Kikuchi,M., Noguchi,N., Takahashi,S., Takata,K., Oka,Y.,
            Uchijima,Y., Kurihara,H. and Asano,T.
  TITLE     A novel protein kinase B (PKB)/AKT-binding protein enhances PKB
            kinase activity and regulates DNA synthesis
  JOURNAL   J Biol Chem 280 (18), 18525-18535 (2005)
   PUBMED   15753085
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL935054.11, AI530462.1, BX284634.8, CD803848.1, AK082029.1,
            CN532842.1, CN458498.1 and CO044538.1.
            
            On or before Feb 15, 2011 this sequence version replaced
            NP_795963.1, XP_484001.1, NP_789811.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB087827.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN00849384, SAMN01164131 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1845
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 16.61 cM"
     Protein         1..1845
                     /product="girdin isoform 3"
                     /note="Hook-related protein 1; Akt-phosphorylation
                     enhancer; girders of actin filament; coiled-coil
                     domain-containing protein 88A; g alpha-interacting
                     vesicle-associated protein"
                     /calculated_mol_wt=212367
     Region          10..165
                     /region_name="HkD_Girdin"
                     /note="Hook domain found in Girdin and similar proteins;
                     cd22229"
                     /db_xref="CDD:411800"
     Site            order(133,139,142..143,145,150,153..154,156..157,160..161,
                     164)
                     /site_type="other"
                     /note="putative LIC-binding interface [polypeptide
                     binding]"
                     /db_xref="CDD:411800"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          258..1079
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          816..841
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          1013..1034
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            1020
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          1036..>1371
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            1387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          1390..1408
                     /region_name="Phosphoinositide-binding.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          1407..1459
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            1417
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            1421
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          1532..1574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          1588..1615
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          1646..1676
                     /region_name="GBA. /evidence=ECO:0000250|UniProtKB:Q3V6T2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            1649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            1664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          1687..1797
                     /region_name="SH2-like, required for interaction with
                     growth factor receptors.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            1691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Region          1710..1845
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            1739
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            1773
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            1794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     Site            1811
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3V6T2; propagated from
                     UniProtKB/Swiss-Prot (Q5SNZ0.2)"
     CDS             1..1845
                     /gene="Ccdc88a"
                     /gene_synonym="A430106J12Rik; Ape; C130096N06Rik;
                     C330012F17Rik; D130005J21Rik; Girdin; Giv; Grdn; Hkrp1"
                     /coded_by="NM_176841.5:691..6228"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS24494.1"
                     /db_xref="GeneID:108686"
                     /db_xref="MGI:MGI:1925177"
ORIGIN      
        1 meneiftpll eqfmtsplvt wvktfgplaa gngtnldeyv alvdgvflnq vmlqinpkse
       61 sqrvnkkvnn daslrihnls ilvkqikfyy qetlqqlimm plpdiliigk npfseqgtee
      121 vkkllllllg cavqcqkkee fiekiqgldf dtkaavaahi qevthnqenv fdlqwmevtd
      181 msqediepll knmvshlrrl iderdehset ivelseerdg vhflphasss aqspcgspgm
      241 krtesrqhls veladakaki rrlrqeleek teqlldckqe leqievelkr lqqenmnlls
      301 darsarmyrd eldalrekav rvdklesels rykerlhdie fykarveelk ednqvlletk
      361 tmledqlegt rarsdklhel ekenlqlkak lhdmemerdm drkkieelme enmtlemaqk
      421 qsmdeslhlg weleqisrts elaeapqksl ghevneltss kllklemenq sltktveelr
      481 stadsaagst skilkveken qrlnkkveil eneiiqekqs lqncqnlskd lmkekaqlek
      541 tietlrense rqikileqen ehlnqtvssl rqrsqisaea rvkdiekenk ilhesiketc
      601 gklskiefek rqmkkelely kekgeraeel enelnhlgke nellqkkitn lkitceklet
      661 leqenseler enrkfkktld sfknltfqle slekensqld eenlelrrsv eslkcasmrm
      721 aqlqlenkel esekeqlrkg lelmrasfkk terlevsyqg ldtenqrlqk alensnkkiq
      781 qleselqdle menqtlqksl eelkisskrl eqlekenksl eqetsqlekd kkqlekenkr
      841 lrqqaeikdt tleennvkig nlekenktlf keinvykesc vrlkeleken kelvkratid
      901 iktlvtlred lvseklktqq mnndleklth elekiglnke rllhdeqstd dsrykllesk
      961 lestlkksle ikeekiaale arleestnyn qqlrhelktv kknyealkqr qdeermvqss
     1021 ipvsgeddkw gresqeatre llkvkdrlie vernnatlqa ekqalktqlk qletqnnnlq
     1081 aqilalqrqt vslqeqnttl qtqnaklqve nstlnsqsts lmnqnaqlli qqsslenene
     1141 simkeredlk slydalikdh eklellherq aseyeslisk hgtlksahkn levehkdled
     1201 rynqllkqkg qledlekmik teqekmlles knhevvasey kklcgendrl nytysqllke
     1261 teilqmdhkn lksvlnnskl eqtrleaefs klkeqyqqld itstklnnqc ellsqlkgnl
     1321 eeenrhlldq iqtlmlqnrt lleqnmeskd lfhveqrqyi dklnelrrqk ekleekimdq
     1381 ykfydpsppr rrgnwitlkm rklikskkdi nrerqksltl tptrsdsseg flqlphqdsq
     1441 dsssvgsnsl edgqtlgtkk sstmndlvqs mvlaggqwtg stenlevpdd istgkrrkel
     1501 gamafsttai nfstvnssaa frskqlvnnk dttsfedisp qgisddsstg srvhasrpas
     1561 ldsgrtstsn snnnaslhev kagavniqsr pqshssgdfs llhdhetwss sgsspiqylk
     1621 rqtrsspmlq hkisetiesr ahhkmkagsp gsevvtlqqf leesnkltsi qlksssqenl
     1681 ldevmkslsv ssdflgkdkp vsctlarsvs gktpgdfydr rttkpeflrt gpqktedayt
     1741 issagkptps tqgkiklvke tsvsrqskds npyatlpras svistaegtt rrtsihdfls
     1801 kdsrlpvsvd sspptagsss ttasnvnkvq esrnsksrsr eqqss
//
LOCUS       NP_001354581             535 aa            linear   PRI 27-APR-2025
DEFINITION  synaptotagmin-16 isoform 1 [Homo sapiens].
ACCESSION   NP_001354581 XP_011535525
VERSION     NP_001354581.1
DBSOURCE    REFSEQ: accession NM_001367652.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Chen,J., Wang,Z., Wang,W., Ren,S., Xue,J., Zhong,L., Jiang,T.,
            Wei,H. and Zhang,C.
  TITLE     SYT16 is a prognostic biomarker and correlated with immune
            infiltrates in glioma: A study based on TCGA data
  JOURNAL   Int Immunopharmacol 84, 106490 (2020)
   PUBMED   32289666
  REMARK    GeneRIF: SYT16 is a prognostic biomarker and correlated with immune
            infiltrates in glioma: A study based on TCGA data.
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Mosing,M.A., Verweij,K.J., Medland,S.E., Painter,J., Gordon,S.D.,
            Heath,A.C., Madden,P.A., Montgomery,G.W. and Martin,N.G.
  TITLE     A genome-wide association study of self-rated health
  JOURNAL   Twin Res Hum Genet 13 (4), 398-403 (2010)
   PUBMED   20707712
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Montes,M., Fuson,K.L., Sutton,R.B. and Robert,J.J.
  TITLE     Purification, crystallization and X-ray diffraction analysis of
            human synaptotagmin 1 C2A-C2B
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 62 (Pt 9), 926-929
            (2006)
   PUBMED   16946482
  REMARK    GeneRIF: Human synaptotagmin tandem C2 domains C2A-C2B have been
            expressed as a glutathione-S-transferase fusion protein in
            Escherichia coli, purified, and crystallized and the preliminary
            X-ray analysis reported.
REFERENCE   8  (residues 1 to 535)
  AUTHORS   Craxton,M.
  TITLE     Synaptotagmin gene content of the sequenced genomes
  JOURNAL   BMC Genomics 5 (1), 43 (2004)
   PUBMED   15238157
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 535)
  AUTHORS   Fukuda,M.
  TITLE     Molecular cloning, expression, and characterization of a novel
            class of synaptotagmin (Syt XIV) conserved from Drosophila to
            humans
  JOURNAL   J Biochem 133 (5), 641-649 (2003)
   PUBMED   12801916
REFERENCE   10 (residues 1 to 535)
  AUTHORS   Craxton,M.
  TITLE     Genomic analysis of synaptotagmin genes
  JOURNAL   Genomics 77 (1-2), 43-49 (2001)
   PUBMED   11543631
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL137918.4, AL356018.5 and AL390816.4.
            
            On Dec 12, 2018 this sequence version replaced XP_011535525.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.105658.1,
                                           SRR1803611.272213.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..535
                     /product="synaptotagmin-16 isoform 1"
                     /note="chr14 synaptotagmin; synaptotagmin 14-like protein;
                     synaptotagmin XIV-related protein; synaptotagmin XVI"
                     /calculated_mol_wt=59495
     Region          240..363
                     /region_name="C2A_Synaptotagmin-14_16"
                     /note="C2A domain first repeat present in Synaptotagmins
                     14 and 16; cd08389"
                     /db_xref="CDD:176035"
     Region          396..533
                     /region_name="C2B_Synaptotagmin-14_16"
                     /note="C2 domain second repeat present in Synaptotagmins
                     14 and 16; cd08408"
                     /db_xref="CDD:176053"
     CDS             1..535
                     /gene="SYT16"
                     /gene_synonym="CHR14SYT; Strep14; SYT14L; syt14r"
                     /coded_by="NM_001367652.1:96..1703"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:83851"
                     /db_xref="HGNC:HGNC:23142"
                     /db_xref="MIM:610950"
ORIGIN      
        1 matditpeai gflsavgvfi vllavlflfi nkklcfetig glpflehrgk rkhskdktgi
       61 hkglvnsfgd deelstssds deevikqfei svsrsqsfrs vtsekgkqtg leqkpkfsrs
      121 llthgedgte vsacedldga sqrrysenls ygeddhipah sqspcergda khhgtshqes
      181 svvqslrrqs tegslemeta fnsrgfedsy atdsssmwsp eeqdrtnlqv psgvsepisk
      241 cgdldvifey raasqkltvt ivraqglpdk drsgvnswqv hvvllpgkkh rgrtniqrgp
      301 npvfrekvtf akleprdvaa cavrfrlyaa rkmtrermmg eklfylshlh pegemkvtlv
      361 leprsnissg gsplspsavs hsdstsstqs lshggapell vglsynattg rlsvemikgs
      421 hfrnlavnra pdtygklfll nsvgqemsrc ktsirrgqpn pvyketfvfq valfqlsdvt
      481 lmisvynrrt mkrkemigwi algqnssgee eqdhweemke tkgqqicrwh tlles
//
LOCUS       NP_001355207             106 aa            linear   ROD 27-APR-2025
DEFINITION  small membrane A-kinase anchor protein [Mus musculus].
ACCESSION   NP_001355207 XP_006496262
VERSION     NP_001355207.1
DBSOURCE    REFSEQ: accession NM_001368278.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Shalom-Barak,T., Zhang,X., Chu,T., Timothy Schaiff,W., Reddy,J.K.,
            Xu,J., Sadovsky,Y. and Barak,Y.
  TITLE     Placental PPARgamma regulates spatiotemporally diverse genes and a
            unique metabolic network
  JOURNAL   Dev Biol 372 (1), 143-155 (2012)
   PUBMED   22967998
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Thiagarajan,R.D., Georgas,K.M., Rumballe,B.A., Lesieur,E.,
            Chiu,H.S., Taylor,D., Tang,D.T., Grimmond,S.M. and Little,M.H.
  TITLE     Identification of anchor genes during kidney development defines
            ontological relationships, molecular subcompartments and regulatory
            pathways
  JOURNAL   PLoS One 6 (2), e17286 (2011)
   PUBMED   21386911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Lin,Q., Donahue,S.L., Moore-Jarrett,T., Cao,S., Osipovich,A.B. and
            Ruley,H.E.
  TITLE     Mutagenesis of diploid mammalian genes by gene entrapment
  JOURNAL   Nucleic Acids Res 34 (20), e139 (2006)
   PUBMED   17062627
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC129337.4.
            
            On Feb 2, 2019 this sequence version replaced XP_006496262.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC048645.1, AK006110.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 26.99 cM"
     Protein         1..106
                     /product="small membrane A-kinase anchor protein"
                     /note="UPF0733 protein C2orf88 homolog; small membrane
                     AKAP"
                     /calculated_mol_wt=11795
     Region          1..100
                     /region_name="SmAKAP"
                     /note="Small membrane A-kinase anchor protein; pfam15127"
                     /db_xref="CDD:464517"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CPS8.1)"
     Region          62..85
                     /region_name="PKA-RI-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CPS8.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BSF0; propagated from
                     UniProtKB/Swiss-Prot (Q9CPS8.1)"
     CDS             1..106
                     /gene="1700019D03Rik"
                     /gene_synonym="2410136C24Rik; smAKAP"
                     /coded_by="NM_001368278.1:347..667"
                     /db_xref="CCDS:CCDS14949.1"
                     /db_xref="GeneID:67080"
                     /db_xref="MGI:MGI:1914330"
ORIGIN      
        1 mgcmksketf pfpttldidk lheseeafip ddssqyrtps pgeqqqvqev kklpepgavi
       61 galilefadr laseivedal qqwaceniqy ynipyieseg sdttin
//
LOCUS       NP_001348154             418 aa            linear   ROD 27-APR-2025
DEFINITION  nucleolar protein 4 isoform 6 [Mus musculus].
ACCESSION   NP_001348154 XP_017173412
VERSION     NP_001348154.1
DBSOURCE    REFSEQ: accession NM_001361225.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Toor,S.M., Wani,S. and Albagha,O.M.E.
  TITLE     Comprehensive Transcriptomic Profiling of Murine Osteoclast
            Differentiation Reveals Novel Differentially Expressed Genes and
            LncRNAs
  JOURNAL   Front Genet 12, 781272 (2021)
   PUBMED   34868271
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Takayanagi-Kiya,S., Misawa-Hojo,K., Kiya,T., Kunieda,T. and Kubo,T.
  TITLE     Splicing variants of NOL4 differentially regulate the transcription
            activity of Mlr1 and Mlr2 in cultured cells
  JOURNAL   Zoolog Sci 31 (11), 735-740 (2014)
   PUBMED   25366156
  REMARK    GeneRIF: These findings suggest that transactivation activities of
            Mlr1 and Mlr2 are differentially regulated by splicing variants of
            NOL4, which are expressed in a tissue-selective manner.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC102361.13, AC131338.4 and AC103368.7.
            
            On Mar 13, 2018 this sequence version replaced XP_017173412.1.
            
            Transcript Variant: This variant (7) contains a distinct 5' UTR and
            lacks an in-frame portion of the 5' coding region, compared to
            variant 3. The resulting isoform (6) has a shorter N-terminus,
            compared to isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.171175.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 11.96 cM"
     Protein         1..418
                     /product="nucleolar protein 4 isoform 6"
                     /calculated_mol_wt=45238
     CDS             1..418
                     /gene="Nol4"
                     /gene_synonym="1700013J13Rik; 4930568N03Rik; Gm1262"
                     /coded_by="NM_001361225.1:781..2037"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:319211"
                     /db_xref="MGI:MGI:2441684"
ORIGIN      
        1 mscsecqkrm hlnpdgtdhk dngkpptlvt smidynmpit maymkhmklq llnsqqdede
       61 ssiesdefdm sdstrmsavn sdlssnleer mqspqtvhgq qdddsaaess ngnetlghss
      121 aasggahgre pedsssdgkt gleqeeqpln lsdspssaql tsefriddqg sdgknkyknl
      181 lisdlkmere arengskspa hsyssydsgk nesvdrgaed lslnrgdede dehdehedse
      241 kvnetdgvea erlkafnsrp ipshltsava esilasaces esrnaakrmr ldkaqdeaap
      301 adkqckpeaa qatystatvp gsqevlying ngtysyhsyr glggllsldd tsssgptdls
      361 mkrqlatgsg ssssstsrpq lspteinavr qlvagyresa afllrsadel enlilqqn
//
LOCUS       NP_079401                123 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 254 isoform 1 [Homo sapiens].
ACCESSION   NP_079401
VERSION     NP_079401.2
DBSOURCE    REFSEQ: accession NM_025125.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Kim,D.K., Cho,M.H., Hersh,C.P., Lomas,D.A., Miller,B.E., Kong,X.,
            Bakke,P., Gulsvik,A., Agusti,A., Wouters,E., Celli,B., Coxson,H.,
            Vestbo,J., MacNee,W., Yates,J.C., Rennard,S., Litonjua,A., Qiu,W.,
            Beaty,T.H., Crapo,J.D., Riley,J.H., Tal-Singer,R. and
            Silverman,E.K.
  CONSRTM   ECLIPSE, ICGN, and COPDGene Investigators
  TITLE     Genome-wide association analysis of blood biomarkers in chronic
            obstructive pulmonary disease
  JOURNAL   Am J Respir Crit Care Med 186 (12), 1238-1247 (2012)
   PUBMED   23144326
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Fortna,A., Kim,Y., MacLaren,E., Marshall,K., Hahn,G., Meltesen,L.,
            Brenton,M., Hink,R., Burgers,S., Hernandez-Boussard,T.,
            Karimpour-Fard,A., Glueck,D., McGavran,L., Berry,R., Pollack,J. and
            Sikela,J.M.
  TITLE     Lineage-specific gene duplication and loss in human and great ape
            evolution
  JOURNAL   PLoS Biol 2 (7), E207 (2004)
   PUBMED   15252450
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA520338.1, BC022252.1 and AL832397.1.
            
            On Jun 9, 2003 this sequence version replaced NP_079401.1.
            
            Transcript Variant: This variant (1) represents the most common
            transcript and encodes isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.244658.1,
                                           SRR1660803.211854.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372281.8/ ENSP00000361355.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.3"
     Protein         1..123
                     /product="transmembrane protein 254 isoform 1"
                     /note="transmembrane protein C10orf57"
                     /calculated_mol_wt=14112
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8TBM7.1)"
     Site            15..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBM7.1)"
     Region          24..113
                     /region_name="TMEM254"
                     /note="Transmembrane protein 254; pfam14934"
                     /db_xref="CDD:464385"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBM7.1)"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBM7.1)"
     CDS             1..123
                     /gene="TMEM254"
                     /gene_synonym="bA369J21.6; C10orf57"
                     /coded_by="NM_025125.4:36..407"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7363.1"
                     /db_xref="GeneID:80195"
                     /db_xref="HGNC:HGNC:25804"
ORIGIN      
        1 mataagatyf qrgslfwftv itlsfgyytw vvfwpqsipy qnlgplgpft qylvdhhhtl
       61 lcngywlawl ihvgeslyai vlckhkgits graqllwflq tfffgiaslt iliaykrkrq
      121 kqt
//
LOCUS       NP_001403                144 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 1A, X-chromosomal [Homo
            sapiens].
ACCESSION   NP_001403 XP_947688
VERSION     NP_001403.1
DBSOURCE    REFSEQ: accession NM_001412.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Ye,Y., Lv,C., Sun,J., Lin,Z., Liu,Y., Huang,Y., Chen,Y., Li,H.,
            Lian,X., Jiang,X., Zhang,S. and Wang,S.
  TITLE     XPO1-Mediated EIF1AX Cytoplasmic Relocation Promotes Tumor
            Migration and Invasion in Endometrial Carcinoma
  JOURNAL   Oxid Med Cell Longev 2022, 1361135 (2022)
   PUBMED   36589683
  REMARK    GeneRIF: XPO1-Mediated EIF1AX Cytoplasmic Relocation Promotes Tumor
            Migration and Invasion in Endometrial Carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Elsherbini,N., Kim,D.H., Payne,R.J., Hudson,T., Forest,V.I.,
            Hier,M.P., Payne,A.E. and Pusztaszeri,M.P.
  TITLE     EIF1AX mutation in thyroid tumors: a retrospective analysis of
            cytology, histopathology and co-mutation profiles
  JOURNAL   J Otolaryngol Head Neck Surg 51 (1), 43 (2022)
   PUBMED   36371345
  REMARK    GeneRIF: EIF1AX mutation in thyroid tumors: a retrospective
            analysis of cytology, histopathology and co-mutation profiles.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Lapointe,C.P., Grosely,R., Sokabe,M., Alvarado,C., Wang,J.,
            Montabana,E., Villa,N., Shin,B.S., Dever,T.E., Fraser,C.S.,
            Fernandez,I.S. and Puglisi,J.D.
  TITLE     eIF5B and eIF1A reorient initiator tRNA to allow ribosomal subunit
            joining
  JOURNAL   Nature 607 (7917), 185-190 (2022)
   PUBMED   35732735
  REMARK    GeneRIF: eIF5B and eIF1A reorient initiator tRNA to allow ribosomal
            subunit joining.
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Karslioglu French,E., Nikitski,A.V., Yip,L., Nikiforova,M.N.,
            Nikiforov,Y.E. and Carty,S.E.
  TITLE     Clinicopathological features and outcomes of thyroid nodules with
            EIF1AX mutations
  JOURNAL   Endocr Relat Cancer 29 (8), 467-473 (2022)
   PUBMED   35609001
  REMARK    GeneRIF: Clinicopathological features and outcomes of thyroid
            nodules with EIF1AX mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Lv,C., Sun,J., Ye,Y., Lin,Z., Li,H., Liu,Y., Mo,K., Xu,W., Hu,W.,
            Draz,E. and Wang,S.
  TITLE     Long noncoding RNA EIF1AX-AS1 promotes endometrial cancer cell
            apoptosis by affecting EIF1AX mRNA stabilization
  JOURNAL   Cancer Sci 113 (4), 1277-1291 (2022)
   PUBMED   35080085
  REMARK    GeneRIF: Long noncoding RNA EIF1AX-AS1 promotes endometrial cancer
            cell apoptosis by affecting EIF1AX mRNA stabilization.
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Choi,S.K., Olsen,D.S., Roll-Mecak,A., Martung,A., Remo,K.L.,
            Burley,S.K., Hinnebusch,A.G. and Dever,T.E.
  TITLE     Physical and functional interaction between the eukaryotic
            orthologs of prokaryotic translation initiation factors IF1 and IF2
  JOURNAL   Mol Cell Biol 20 (19), 7183-7191 (2000)
   PUBMED   10982835
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Battiste,J.L., Pestova,T.V., Hellen,C.U. and Wagner,G.
  TITLE     The eIF1A solution structure reveals a large RNA-binding surface
            important for scanning function
  JOURNAL   Mol Cell 5 (1), 109-119 (2000)
   PUBMED   10678173
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Pestova,T.V., Borukhov,S.I. and Hellen,C.U.
  TITLE     Eukaryotic ribosomes require initiation factors 1 and 1A to locate
            initiation codons
  JOURNAL   Nature 394 (6696), 854-859 (1998)
   PUBMED   9732867
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Dever,T.E., Wei,C.L., Benkowski,L.A., Browning,K., Merrick,W.C. and
            Hershey,J.W.
  TITLE     Determination of the amino acid sequence of rabbit, human, and
            wheat germ protein synthesis factor eIF-4C by cloning and chemical
            sequencing
  JOURNAL   J Biol Chem 269 (5), 3212-3218 (1994)
   PUBMED   8106356
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AL732366.7 and L18960.1.
            
            On Mar 4, 2006 this sequence version replaced XP_947688.1.
            
            Summary: This gene encodes an essential eukaryotic translation
            initiation factor. The protein is required for the binding of the
            43S complex (a 40S subunit, eIF2/GTP/Met-tRNAi and eIF3) to the 5'
            end of capped RNA. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.256397.1,
                                           SRR1803617.7738.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379607.10/ ENSP00000368927.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..144
                     /product="eukaryotic translation initiation factor 1A,
                     X-chromosomal"
                     /note="eukaryotic translation initiation factor 4C;
                     eukaryotic translation initiation factor 1A, X chromosome;
                     Putative eukaryotic translation initiation factor 1A;
                     eIF1A X isoform"
                     /calculated_mol_wt=16329
     Region          1..131
                     /region_name="PTZ00329"
                     /note="eukaryotic translation initiation factor 1A;
                     Provisional"
                     /db_xref="CDD:185558"
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47813.2)"
     Site            order(41..42,46,60..63,66,71)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:240219"
     Region          114..144
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47813.2)"
     CDS             1..144
                     /gene="EIF1AX"
                     /gene_synonym="eIF-1A; eIF-4C; EIF1A; EIF1AP1; EIF4C"
                     /coded_by="NM_001412.4:199..633"
                     /db_xref="CCDS:CCDS14196.1"
                     /db_xref="GeneID:1964"
                     /db_xref="HGNC:HGNC:3250"
                     /db_xref="MIM:300186"
ORIGIN      
        1 mpknkgkggk nrrrgknene sekrelvfke dgqeyaqvik mlgngrleam cfdgvkrlch
       61 irgklrkkvw intsdiilvg lrdyqdnkad vilkynadea rslkaygelp ehakinetdt
      121 fgpgdddeiq fddigddded iddi
//
LOCUS       NP_001275575             409 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 286A isoform 5 [Homo sapiens].
ACCESSION   NP_001275575
VERSION     NP_001275575.1
DBSOURCE    REFSEQ: accession NM_001288646.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Murakami,T., Sun,Z.S., Lee,C.C. and Lupski,J.R.
  TITLE     Isolation of novel genes from the CMT1A duplication/HNPP deletion
            critical region in 17p11.2-p12
  JOURNAL   Genomics 39 (1), 99-103 (1997)
   PUBMED   9027492
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005324.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.133880.1,
                                           SRR1803613.271460.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..409
                     /product="zinc finger protein 286A isoform 5"
                     /note="zinc finger protein ZNF286"
                     /calculated_mol_wt=47341
     Region          <110..245
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          133..153
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          161..181
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          188..208
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          216..236
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <240..395
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          244..264
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          272..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(277,279,281,283..284,287..288,291,305,307,311..312,
                     315..316,319,333,335,337,339..340,343..344,347)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          356..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          384..404
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..409
                     /gene="ZNF286A"
                     /gene_synonym="ZNF286"
                     /coded_by="NM_001288646.2:617..1846"
                     /note="isoform 5 is encoded by transcript variant 7"
                     /db_xref="GeneID:57335"
                     /db_xref="HGNC:HGNC:13501"
ORIGIN      
        1 metrpqskds tsvqdfskae sckvaiidrl trnsvydsnl eaalecenwl enqqgnqerh
       61 lremfthmns lseetdhkhd vywksfnqks vlitedrvpk gsyafhtlek slkqksnlmk
      121 kqrtykekkp hkcndcgelf tyhsvlirhq rvhtgekpyt cnecgksfsh ranltkhqrt
      181 htrilfecse ckktftesss lathqrihvg erpyecnecg kgfnrsthlv qhqlihtgvk
      241 pyecnecdka fihssalikh qrthtgekpy kcqecgkafs hcssltkhqr vhtgekpyec
      301 secgktfsqs thlvqhqrih tgekpyecne cgktfsrssn fakhqrihig kkpykcsecg
      361 kafihssali qhqrthtgek pfrcnecgks fkcssslirh qrvhteeqp
//
LOCUS       NP_001355929             288 aa            linear   PRI 27-APR-2025
DEFINITION  aprataxin isoform h [Homo sapiens].
ACCESSION   NP_001355929 XP_016870326
VERSION     NP_001355929.1
DBSOURCE    REFSEQ: accession NM_001369000.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_016870326.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.166522.1,
                                           SRR7346977.612358.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..288
                     /product="aprataxin isoform h"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=32994
     Region          3..>44
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Region          110..211
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(204,206,208..210)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            206
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          229..288
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..288
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001369000.1:322..1188"
                     /note="isoform h is encoded by transcript variant 21"
                     /db_xref="CCDS:CCDS75827.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqefeeea knpglethrk
       61 rkrsgnsdsi erdaaqeaea gtglepgsns gqcsvplkkg kdapikkesl ghwsqglkis
      121 mqdpkmqvyk deqvvvikdk ypkaryhwlv lpwtsisslk avarehlell khmhtvgekv
      181 ivdfagsskl rfrlgyhaip smshvhlhvi sqdfdspclk nkkhwnsfnt eyflesqavi
      241 emvqeagrvt vrdgmpellk lplrchecqq llpsipqlke hlrkhwtq
//
LOCUS       NP_001265222             186 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-ribosylation factor-like protein 6 isoform 1 [Homo sapiens].
ACCESSION   NP_001265222
VERSION     NP_001265222.1
DBSOURCE    REFSEQ: accession NM_001278293.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Wang,J., Che,F., Zhao,Y., Wei,L., Chen,D., Dai,C., Zhang,B.,
            Zhou,X., Yang,B. and Chen,Z.
  TITLE     The Prognostic and Therapeutic Roles of ARL-6 Gene in
            Hepatocellular Carcinoma
  JOURNAL   Int J Med Sci 21 (2), 207-218 (2024)
   PUBMED   38169538
  REMARK    GeneRIF: The Prognostic and Therapeutic Roles of ARL-6 Gene in
            Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Gouronc,A., Zilliox,V., Jacquemont,M.L., Darcel,F., Leuvrey,A.S.,
            Nourisson,E., Antin,M., Alessandri,J.L., Doray,B., Gueguen,P.,
            Payet,F., Randrianaivo,H., Stoetzel,C., Scheidecker,S.,
            Flodrops,H., Dollfus,H. and Muller,J.
  TITLE     High prevalence of Bardet-Biedl syndrome in La Reunion Island is
            due to a founder variant in ARL6/BBS3
  JOURNAL   Clin Genet 98 (2), 166-171 (2020)
   PUBMED   32361989
  REMARK    GeneRIF: High prevalence of Bardet-Biedl syndrome in La Reunion
            Island is due to a founder variant in ARL6/BBS3.
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Singh,S.K., Gui,M., Koh,F., Yip,M.C. and Brown,A.
  TITLE     Structure and activation mechanism of the BBSome membrane protein
            trafficking complex
  JOURNAL   Elife 9, e53322 (2020)
   PUBMED   31939736
  REMARK    GeneRIF: Structure and activation mechanism of the BBSome membrane
            protein trafficking complex.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Pretorius,P.R., Baye,L.M., Nishimura,D.Y., Searby,C.C., Bugge,K.,
            Yang,B., Mullins,R.F., Stone,E.M., Sheffield,V.C. and
            Slusarski,D.C.
  TITLE     Identification and functional analysis of the vision-specific BBS3
            (ARL6) long isoform
  JOURNAL   PLoS Genet 6 (3), e1000884 (2010)
   PUBMED   20333246
  REMARK    GeneRIF: These data demonstrate that the BBS3L transcript is
            required for proper retinal function and organization.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Ingley,E., Williams,J.H., Walker,C.E., Tsai,S., Colley,S.,
            Sayer,M.S., Tilbrook,P.A., Sarna,M., Beaumont,J.G. and Klinken,S.P.
  TITLE     A novel ADP-ribosylation like factor (ARL-6), interacts with the
            protein-conducting channel SEC61beta subunit
  JOURNAL   FEBS Lett 459 (1), 69-74 (1999)
   PUBMED   10508919
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Jacobs,S., Schilf,C., Fliegert,F., Koling,S., Weber,Y.,
            Schurmann,A. and Joost,H.G.
  TITLE     ADP-ribosylation factor (ARF)-like 4, 6, and 7 represent a subgroup
            of the ARF family characterization by rapid nucleotide exchange and
            a nuclear localization signal
  JOURNAL   FEBS Lett 456 (3), 384-388 (1999)
   PUBMED   10462049
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Sheffield,V.C., Carmi,R., Kwitek-Black,A., Rokhlina,T.,
            Nishimura,D., Duyk,G.M., Elbedour,K., Sunden,S.L. and Stone,E.M.
  TITLE     Identification of a Bardet-Biedl syndrome locus on chromosome 3 and
            evaluation of an efficient approach to homozygosity mapping
  JOURNAL   Hum Mol Genet 3 (8), 1331-1335 (1994)
   PUBMED   7987310
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292958.1, BU183949.1,
            AC110491.5, BM464340.1, BQ441226.1, BM982145.1 and AL138043.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the ARF-like
            (ADP ribosylation factor-like) sub-family of the ARF family of
            GTP-binding proteins which are involved in regulation of
            intracellular traffic. Mutations in this gene are associated with
            Bardet-Biedl syndrome (BBS). A vision-specific transcript, encoding
            long isoform BBS3L, has been described (PMID: 20333246). [provided
            by RefSeq, Apr 2016].
            
            Transcript Variant: Variants 1, 2 and 3 encode the same isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292958.1, SRR1660809.94976.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000463745.6/ ENSP00000419619.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q11.2"
     Protein         1..186
                     /product="ADP-ribosylation factor-like protein 6 isoform
                     1"
                     /note="Bardet-Biedl syndrome 3 protein; ADP ribosylation
                     factor like GTPase 6; ARL6 interacting reticulophagy
                     regulator 1"
                     /calculated_mol_wt=20966
     Region          19..180
                     /region_name="Arl6"
                     /note="Arf-like 6 (Arl6) GTPase; cd04157"
                     /db_xref="CDD:206722"
     Site            24..31
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206722"
     Site            order(26..32,49..50,72,130..131,133,163..165)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206722"
     Site            order(26..27,31,35,49..56,78,83)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206722"
     Site            order(36..40,43..53)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206722"
     Site            order(50..54,59,69,73,79,81..83)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206722"
     Site            50
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206722"
     Site            order(51..58,68,79,82..83)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206722"
     Site            order(54..60,63..68)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206722"
     Site            69..86
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206722"
     Site            69..72
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206722"
     Site            130..133
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206722"
     Site            163..165
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206722"
     CDS             1..186
                     /gene="ARL6"
                     /gene_synonym="BBS3; RP55"
                     /coded_by="NM_001278293.3:248..808"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS2928.1"
                     /db_xref="GeneID:84100"
                     /db_xref="HGNC:HGNC:13210"
                     /db_xref="MIM:608845"
ORIGIN      
        1 mglldrlsvl lglkkkevhv lclgldnsgk ttiinklkps naqsqnilpt igfsiekfks
       61 sslsftvfdm sgqgryrnlw ehyykegqai ifvidssdrl rmvvakeeld tllnhpdikh
      121 rripilffan kmdlrdavts vkvsqllcle nikdkpwhic asdaikgegl qegvdwlqdq
      181 iqtvkt
//
LOCUS       NP_001351372             468 aa            linear   ROD 27-APR-2025
DEFINITION  procollagen galactosyltransferase 1 isoform 2 precursor [Mus
            musculus].
ACCESSION   NP_001351372 XP_011240603
VERSION     NP_001351372.1
DBSOURCE    REFSEQ: accession NM_001364443.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   He,L., Ye,X., Gao,M., Yang,J., Ma,J., Xiao,F. and Wei,H.
  TITLE     Down-regulation of GLT25D1 inhibited collagen secretion and
            involved in liver fibrogenesis
  JOURNAL   Gene 729, 144233 (2020)
   PUBMED   31759980
  REMARK    GeneRIF: Results demonstrate that Glt25d1 knockout results in
            embryonic lethality and down-regulation of Glt25d1 may inhibit
            collagen secretion during liver fibrogenesis.
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Terajima,M., Taga,Y., Sricholpech,M., Kayashima,Y., Sumida,N.,
            Maeda,N., Hattori,S. and Yamauchi,M.
  TITLE     Role of Glycosyltransferase 25 Domain 1 in Type I Collagen
            Glycosylation and Molecular Phenotypes
  JOURNAL   Biochemistry 58 (50), 5040-5051 (2019)
   PUBMED   31726007
  REMARK    GeneRIF: GLT25D1 catalyzes galactosylation of Hyl throughout the
            type I collagen molecule and that this modification may regulate
            maturation of collagen cross-linking, fibrillogenesis, and
            mineralization
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Geister,K.A., Lopez-Jimenez,A.J., Houghtaling,S., Ho,T.H.,
            Vanacore,R. and Beier,D.R.
  TITLE     Loss of function of Colgalt1 disrupts collagen post-translational
            modification and causes musculoskeletal defects
  JOURNAL   Dis Model Mech 12 (6) (2019)
   PUBMED   31101663
  REMARK    GeneRIF: Colgalt1 mutant could serve as a model of a human
            connective tissue disorder and/or congenital muscular dystrophy or
            myopathy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Ye,X., He,L., Ma,J., Li,Y., Zhang,M., Yang,J., Zhang,J., Xiao,F.
            and Wei,H.
  TITLE     Downregulation of Glt25d1 aggravates carbon tetrachloride-induced
            acute hepatic injury through activation of the TGF-beta1/Smad2
            signaling pathway
  JOURNAL   Mol Med Rep 18 (4), 3611-3618 (2018)
   PUBMED   30132521
  REMARK    GeneRIF: The downregulation of Glt25d1 deteriorated CCl4induced
            liver injury in mice, which may involve triggering inflammatory
            responses, apoptosis and TGFbeta1/Smad2 signaling pathway
            activation.
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Geister,K.A., Timms,A.E. and Beier,D.R.
  TITLE     Optimizing Genomic Methods for Mapping and Identification of
            Candidate Variants in ENU Mutagenesis Screens Using Inbred Mice
  JOURNAL   G3 (Bethesda) 8 (2), 401-409 (2018)
   PUBMED   29208648
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Tao,G., Levay,A.K., Peacock,J.D., Huk,D.J., Both,S.N.,
            Purcell,N.H., Pinto,J.R., Galantowicz,M.L., Koch,M., Lucchesi,P.A.,
            Birk,D.E. and Lincoln,J.
  TITLE     Collagen XIV is important for growth and structural integrity of
            the myocardium
  JOURNAL   J Mol Cell Cardiol 53 (5), 626-638 (2012)
   PUBMED   22906538
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM944342.1 and AK029433.1.
            
            On Jun 16, 2018 this sequence version replaced XP_011240603.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK029433.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 34.43 cM"
     Protein         1..468
                     /product="procollagen galactosyltransferase 1 isoform 2
                     precursor"
                     /EC_number="2.4.1.50"
                     /note="procollagen galactosyltransferase 1; hydroxylysine
                     galactosyltransferase 1; glycosyltransferase 25 family
                     member 1; glycosyltransferase 25 domain containing 1"
                     /calculated_mol_wt=50837
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3090
     Region          37..>194
                     /region_name="BcsA"
                     /note="Glycosyltransferase, catalytic subunit of cellulose
                     synthase and poly-beta-1,6-N-acetylglucosamine synthase
                     [Cell motility]; COG1215"
                     /db_xref="CDD:440828"
     Site            91
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q8K297.2)"
     Site            179
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8K297.2)"
     Region          335..>463
                     /region_name="Glyco_transf_25"
                     /note="Glycosyltransferase family 25 [lipooligosaccharide
                     (LOS) biosynthesis protein] is a family of
                     glycosyltransferases involved in LOS biosynthesis. The
                     members include the beta(1,4) galactosyltransferases: Lgt2
                     of Moraxella catarrhalis, LgtB and LgtE of...; cl01298"
                     /db_xref="CDD:470150"
     Site            376
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8K297.2)"
     CDS             1..468
                     /gene="Colgalt1"
                     /gene_synonym="2810024B22Rik; Glt25d1"
                     /coded_by="NM_001364443.1:33..1439"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:234407"
                     /db_xref="MGI:MGI:1924348"
ORIGIN      
        1 maalprgsrg lpllplllll pplggprgad gyfpeerwsp esplqaprvl iallarnaap
       61 alpatlgale qlrhprerta lwvatdhntd ntsailrewl vavkglyhsv ewrpaeepss
      121 ypdeegpkhw sdsryehvmk lrqaalksar dmwadyilfm didnlitnpd tlslliaenk
      181 tvvapmldsr aaysnfwcgm tsqgyykrtp ayipirkrdr rgcfavpmvh stflidlrka
      241 asrnlafypt hpdytwsfdd iivfafsckq aevqmyvcnk evygflpvpl rahsslqdea
      301 esfmhvqlev mvkhppvqls rfisaprkts dkmgfdevfm inlkrrrdrr ermlralheq
      361 eidcqlveav dgkamntsqv eamgiqmlpg yrdpyhgrpl tkgelgcfls hyniwkevvd
      421 rglqkslvfe ddlrfeiffk rrlmnlmrdv eregldwdli ilwqvgdm
//
LOCUS       NP_083990               1145 aa            linear   ROD 27-APR-2025
DEFINITION  cation channel sperm-associated auxiliary subunit gamma 2 precursor
            [Mus musculus].
ACCESSION   NP_083990 XP_284290
VERSION     NP_083990.2
DBSOURCE    REFSEQ: accession NM_029714.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Lin,S., Ke,M., Zhang,Y., Yan,Z. and Wu,J.
  TITLE     Structure of a mammalian sperm cation channel complex
  JOURNAL   Nature 595 (7869), 746-750 (2021)
   PUBMED   34225353
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Chung,J.J., Navarro,B., Krapivinsky,G., Krapivinsky,L. and
            Clapham,D.E.
  TITLE     A novel gene required for male fertility and functional CATSPER
            channel formation in spermatozoa
  JOURNAL   Nat Commun 2, 153 (2011)
   PUBMED   21224844
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Wang,H., Liu,J., Cho,K.H. and Ren,D.
  TITLE     A novel, single, transmembrane protein CATSPERG is associated with
            CATSPER1 channel protein
  JOURNAL   Biol Reprod 81 (3), 539-544 (2009)
   PUBMED   19516020
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK006911.1, BY724013.1, BB614579.1, AC112789.4, BU938829.1 and
            AV277342.2.
            
            On Oct 6, 2007 this sequence version replaced NP_083990.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: GQ225581.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMN00849374,
                                    SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 17.2 cM"
     Protein         1..1145
                     /product="cation channel sperm-associated auxiliary
                     subunit gamma 2 precursor"
                     /note="cation channel sperm-associated protein subunit
                     gamma 2; CATSPER gamma subunit protein; cation channel,
                     sperm-associated, gamma 2; catsper channel auxiliary
                     subunit gamma 2"
                     /calculated_mol_wt=127003
     sig_peptide     1..38
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4433
     Region          7..973
                     /region_name="CATSPERG"
                     /note="Cation channel sperm-associated protein subunit
                     gamma; pfam15064"
                     /db_xref="CDD:464479"
     mat_peptide     39..1145
                     /product="Cation channel sperm-associated auxiliary
                     subunit gamma 2. /id=PRO_0000388712"
                     /note="propagated from UniProtKB/Swiss-Prot (C6KI89.1)"
                     /calculated_mol_wt=127003
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34225353; propagated from
                     UniProtKB/Swiss-Prot (C6KI89.1)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34225353; propagated from
                     UniProtKB/Swiss-Prot (C6KI89.1)"
     Site            356
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34225353; propagated from
                     UniProtKB/Swiss-Prot (C6KI89.1)"
     Site            402
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34225353; propagated from
                     UniProtKB/Swiss-Prot (C6KI89.1)"
     Site            672
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34225353; propagated from
                     UniProtKB/Swiss-Prot (C6KI89.1)"
     Site            743
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (C6KI89.1)"
     Site            1038
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (C6KI89.1)"
     Site            1062..1083
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (C6KI89.1)"
     CDS             1..1145
                     /gene="Catsperg2"
                     /gene_synonym="1700067C01Rik; CATSPERG"
                     /coded_by="NM_029714.4:117..3554"
                     /db_xref="CCDS:CCDS52173.1"
                     /db_xref="GeneID:76718"
                     /db_xref="MGI:MGI:1923968"
ORIGIN      
        1 mvsrpamspv spvwprkpnl wafwvlrlvl llslkswaed alqhctwllv lnkfekvglh
       61 lskdrfqdhe pidtvakvfq kltdspidps enylsfpyyl qinfscpgqn ieelarkghl
      121 mgmkpmvqin ymysvnfyrw emenvqilme aapmrstgyc paeamcvlnw ytpmpfkngs
      181 vvssvdiytn gigpfvskkr fyvnmngflk rdasgkslfa igyeslvlks shfrlsksrp
      241 lwytvnhapv filggfydek silfsdsnfq dyvllelsid scwvgsfycp ilgfsatihd
      301 aiatestlfi rqnqlvyyft gtyitlfdks hgssrwvrvl psecikrlcp vyasgngsey
      361 vlalttgkne gyihigtitd glvsfemvpd gwsvceklpg kncsidwaty iadernllll
      421 vkidsgqfyl vnfntefktl nilykipefi peakeldflv lldtvtytnt pmtpkglffn
      481 tlnnmlyiwg nfilqsynre efifladfpk estikymvns fkgqmavvte neeiwyfleg
      541 gydvyqvvps qgwetyhnlq kmqkssfhse deslvslffe dgklfqlvyl fdvgkerlvk
      601 rllpvgtlme ynlpkpftvv nqgnyqaisf thtcpfkeih lidvpkkhha srtesyvalp
      661 plvseslgfh nnntlavyqg lvyyllwlhs kydkpyadpv hdptwrwwqh ktkdkdyffy
      721 lfsnrlaaeg iyinmnayqk lynmsgdygi pdlffldkgn wftitvvlls hqdtftssds
      781 qgptinvdkk laiavtiadp eclsvtvtqd vllnrnavin kikvidkkrc seqgmigrni
      841 kktsmmlkvl gapgnciqrt ylggiiqgfk vvpifigcpp gkrlafdvsy timhseeink
      901 hyfdcvikda empcflfrdl fqpfflvqdl vtgdsgsflg syvlkvvggg rtlntirdyt
      961 eeeifrynsp ldttnsliwk tkverttedk kfyimshesp gvewlclens pcydiipqsi
     1021 yppefffkll vsnrgvdnst ycdykltfiv hihglplssk rtsfivmvst sffialvvfy
     1081 ilfclvwphi vkawvslrwr innimasesy ytyasstagf slqshsfegp sragskednv
     1141 qakta
//
LOCUS       NP_689540                723 aa            linear   PRI 27-APR-2025
DEFINITION  adenylate kinase 7 isoform 1 [Homo sapiens].
ACCESSION   NP_689540
VERSION     NP_689540.2
DBSOURCE    REFSEQ: accession NM_152327.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Chang,T., Tang,H., Zhou,X., He,J., Liu,N., Li,Y., Xiang,W. and
            Yao,Z.
  TITLE     A novel homozygous nonsense variant of AK7 is associated with
            multiple morphological abnormalities of the sperm flagella
  JOURNAL   Reprod Biomed Online 48 (5), 103765 (2024)
   PUBMED   38492416
  REMARK    GeneRIF: A novel homozygous nonsense variant of AK7 is associated
            with multiple morphological abnormalities of the sperm flagella.
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Wang,H.S., Zhu,Y. and Sun,F.
  TITLE     [Expressions of the adenylate kinase family in asthenospermia]
  JOURNAL   Zhonghua Nan Ke Xue 25 (12), 1077-1082 (2019)
   PUBMED   32251557
  REMARK    GeneRIF: The mRNA and protein expressions of AK1, AK6 and AK7 are
            significantly down-regulated in the sperm of asthenospermia
            patients, which may be closely related with reduced sperm motility.
REFERENCE   3  (residues 1 to 723)
  AUTHORS   Lores,P., Coutton,C., El Khouri,E., Stouvenel,L., Givelet,M.,
            Thomas,L., Rode,B., Schmitt,A., Louis,B., Sakheli,Z., Chaudhry,M.,
            Fernandez-Gonzales,A., Mitsialis,A., Dacheux,D., Wolf,J.P.,
            Papon,J.F., Gacon,G., Escudier,E., Arnoult,C., Bonhivers,M.,
            Savinov,S.N., Amselem,S., Ray,P.F., Dulioust,E. and Toure,A.
  TITLE     Homozygous missense mutation L673P in adenylate kinase 7 (AK7)
            leads to primary male infertility and multiple morphological
            anomalies of the flagella but not to primary ciliary dyskinesia
  JOURNAL   Hum Mol Genet 27 (7), 1196-1211 (2018)
   PUBMED   29365104
  REMARK    GeneRIF: a novel genetic cause of asthenozoospermia due to MMAF and
            suggests that in humans, more deleterious mutations of AK7 might
            induce primary ciliary dyskinesia.
REFERENCE   4  (residues 1 to 723)
  AUTHORS   Amiri,M., Conserva,F., Panayiotou,C., Karlsson,A. and Solaroli,N.
  TITLE     The human adenylate kinase 9 is a nucleoside mono- and diphosphate
            kinase
  JOURNAL   Int J Biochem Cell Biol 45 (5), 925-931 (2013)
   PUBMED   23416111
REFERENCE   5  (residues 1 to 723)
  AUTHORS   Mata,M., Lluch-Estelles,J., Armengot,M., Sarrion,I., Carda,C. and
            Cortijo,J.
  TITLE     New adenylate kinase 7 (AK7) mutation in primary ciliary dyskinesia
  JOURNAL   Am J Rhinol Allergy 26 (4), 260-264 (2012)
   PUBMED   22801010
  REMARK    GeneRIF: AK7 may be involved in the development of Primary ciliary
            dyskinesia (PCD).
REFERENCE   6  (residues 1 to 723)
  AUTHORS   Panayiotou,C., Solaroli,N., Xu,Y., Johansson,M. and Karlsson,A.
  TITLE     The characterization of human adenylate kinases 7 and 8
            demonstrates differences in kinetic parameters and structural
            organization among the family of adenylate kinase isoenzymes
  JOURNAL   Biochem J 433 (3), 527-534 (2011)
   PUBMED   21080915
  REMARK    GeneRIF: Both AK7 and full-length AK8 showed highest affinity for
            AMP with ATP as the phosphate donor, and proved to be more
            efficient in AMP phosphorylation as compared with the major
            cytosolic isoform AK1
REFERENCE   7  (residues 1 to 723)
  AUTHORS   Milara,J., Armengot,M., Mata,M., Morcillo,E.J. and Cortijo,J.
  TITLE     Role of adenylate kinase type 7 expression on cilia motility:
            possible link in primary ciliary dyskinesia
  JOURNAL   Am J Rhinol Allergy 24 (3), 181-185 (2010)
   PUBMED   20537283
  REMARK    GeneRIF: expression is decreased in patients with primary ciliary
            dyskinesia and is correlated with ciliary beat frequency of nasal
            epithelium cellsepithelium
REFERENCE   8  (residues 1 to 723)
  AUTHORS   Van Rompay,A.R., Johansson,M. and Karlsson,A.
  TITLE     Identification of a novel human adenylate kinase. cDNA cloning,
            expression analysis, chromosome localization and characterization
            of the recombinant protein
  JOURNAL   Eur J Biochem 261 (2), 509-517 (1999)
   PUBMED   10215863
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK057426.1, BC035256.1,
            AL359240.4, AL163051.5 and BM981526.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 8, 2007 this sequence version replaced NP_689540.1.
            
            Summary: This gene encodes a member of the adenylate kinase family
            of enzymes. The encoded enzyme is a phosphotransferase that
            catalyzes the reversible phosphorylation of adenine nucleotides.
            This enzyme plays a role in energy homeostasis of the cell.
            Alternative splicing results in multiple transcript variants.
            Mutations in the mouse gene are associated with primary ciliary
            dyskinesia. [provided by RefSeq, Apr 2017].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.48747.1,
                                           SRR1803613.229181.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267584.9/ ENSP00000267584.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.2"
     Protein         1..723
                     /product="adenylate kinase 7 isoform 1"
                     /EC_number="2.7.4.3"
                     /EC_number="2.7.4.6"
                     /note="putative adenylate kinase 7; ATP-AMP
                     transphosphorylase 7"
                     /calculated_mol_wt=82528
     Region          <168..297
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
     Region          367..612
                     /region_name="Adenylate kinase.
                     /evidence=ECO:0000305|PubMed:21080915"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96M32.3)"
     Region          369..>548
                     /region_name="ADK"
                     /note="Adenylate kinase (ADK) catalyzes the reversible
                     phosphoryl transfer from adenosine triphosphates (ATP) to
                     adenosine monophosphates (AMP) and to yield adenosine
                     diphosphates (ADP). This enzyme is required for the
                     biosynthesis of ADP and is essential for...; cd01428"
                     /db_xref="CDD:238713"
     Region          397..455
                     /region_name="NMP. /evidence=ECO:0000250|UniProtKB:P69441"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96M32.3)"
     Site            order(398,403,455,481..482,484..485,489)
                     /site_type="other"
                     /note="AMP-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Region          537..547
                     /region_name="LID. /evidence=ECO:0000250|UniProtKB:P69441"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96M32.3)"
     Region          679..723
                     /region_name="DPY-30.
                     /evidence=ECO:0000305|PubMed:21080915"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96M32.3)"
     Region          679..719
                     /region_name="DD_AK7"
                     /note="dimerization/docking (D/D) domain found in
                     adenylate kinase 7 and similar proteins; cd22967"
                     /db_xref="CDD:438536"
     CDS             1..723
                     /gene="AK7"
                     /gene_synonym="AK 7; CFAP75; FAP75; SPGF27"
                     /coded_by="NM_152327.5:28..2199"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9945.1"
                     /db_xref="GeneID:122481"
                     /db_xref="HGNC:HGNC:20091"
                     /db_xref="MIM:615364"
ORIGIN      
        1 maeeeetaal tekvirtqrv finlldsyss gnigkflsnc vvgasleeit eeeeeedenk
       61 samleasstk vkegtfqivg tlskpdsprp dfavetysai sredllmrll ecdviiynit
      121 essqqmeeai wavsalseev shfekrklfi llstvmtwar skaldpedse vpfteedyrr
      181 rkshpnfldh inaekmvlkf gkkarkfaay vvaaglqyga eggmlhtffk mawlgeipal
      241 pvfgdgtnvi ptihvldlag viqnvidhvp kphylvavde svhtledivk ciskntgpgk
      301 iqkiprenay ltkdltqdcl dhllvnlrme alfvkenfni rwaaqtgfve nintilkeyk
      361 qsrglmpiki cilgppavgk ssiakelany yklhhiqlkd viseaiakle aivapndvge
      421 geeeveeeee eenvedaqel ldgikesmeq nagqlddqyi irfmkeklks mpcrnqgyil
      481 dgfpktydqa kdlfnqedee eeddvrgrmf pfdkliipef vcaldasdef lkervinlpe
      541 sivagthysq drflralsny rdiniddetv fnyfdeleih pihidvgkle daqnrlaikq
      601 likeigeprn ygltdeekae eerkaaeerl areaaeeaer ehqeavemae kiarweewnk
      661 rleevkreer elleaqsipl rnylmtyvmp tliqglnecc nvrpedpvdf laeylfknnp
      721 eaq
//
LOCUS       NP_082445                212 aa            linear   ROD 27-APR-2025
DEFINITION  Golgi-associated RAB2 interactor protein 5A isoform 1 [Mus
            musculus].
ACCESSION   NP_082445 XP_906568 XP_929826
VERSION     NP_082445.1
DBSOURCE    REFSEQ: accession NM_028169.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Wang,H., Iida-Norita,R., Mashiko,D., Pham,A.H., Miyata,H. and
            Ikawa,M.
  TITLE     Golgi associated RAB2 interactor protein family contributes to
            murine male fertility to various extents by assuring correct
            morphogenesis of sperm heads
  JOURNAL   PLoS Genet 20 (6), e1011337 (2024)
   PUBMED   38935810
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Takahama,M., Fukuda,M., Ohbayashi,N., Kozaki,T., Misawa,T.,
            Okamoto,T., Matsuura,Y., Akira,S. and Saitoh,T.
  TITLE     The RAB2B-GARIL5 Complex Promotes Cytosolic DNA-Induced Innate
            Immune Responses
  JOURNAL   Cell Rep 20 (12), 2944-2954 (2017)
   PUBMED   28930687
  REMARK    GeneRIF: the RAB2B-GARIL5 complex promotes IFN responses against
            DNA viruses by regulating the cGAS-STING signaling axis.
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Fukuda,M., Kanno,E., Ishibashi,K. and Itoh,T.
  TITLE     Large scale screening for novel rab effectors reveals unexpected
            broad Rab binding specificity
  JOURNAL   Mol Cell Proteomics 7 (6), 1031-1042 (2008)
   PUBMED   18256213
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC149607.6.
            
            On or before Apr 10, 2009 this sequence version replaced
            XP_929826.2, XP_906568.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC130017.1, AB473729.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 28.83 cM"
     Protein         1..212
                     /product="Golgi-associated RAB2 interactor protein 5A
                     isoform 1"
                     /note="Golgi-associated Rab2B interactor-like 5; Protein
                     FAM71E1; family with sequence similarity 71, member E1;
                     Golgi associated RAB2 interactor protein 5A"
                     /calculated_mol_wt=24041
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3C1.2)"
     Region          93..158
                     /region_name="DUF3699"
                     /note="Protein of unknown function (DUF3699); pfam12480"
                     /db_xref="CDD:463601"
     Region          162..212
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3C1.2)"
     CDS             1..212
                     /gene="Garin5a"
                     /gene_synonym="0610007G24Rik; 1700021N13Rik;
                     1700021P22Rik; Fam71e1; GARI-L5; GARIL5"
                     /coded_by="NM_028169.2:94..732"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS52232.1"
                     /db_xref="GeneID:75538"
                     /db_xref="MGI:MGI:1922788"
ORIGIN      
        1 mkggrdlkaa rggadrplap ayapcrpgrl qrhllsgefd qlrdfpifes nfvqvtrfge
       61 vankvtmgva asspalelpd llllagpdke nghlqllglf plqfvqlfvh desrqqlkvk
      121 frtgrafylq lrsppetrdc efgrwvrlly rlrfhsptca vpfthedtap eeeeeeeeee
      181 eeeevkegql qppefqatea rldpqvselw gl
//
LOCUS       NP_689771                695 aa            linear   PRI 27-APR-2025
DEFINITION  IQ domain-containing protein E isoform 1 [Homo sapiens].
ACCESSION   NP_689771 NP_060074
VERSION     NP_689771.3
DBSOURCE    REFSEQ: accession NM_152558.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Estrada-Cuzcano,A., Etard,C., Delvallee,C., Stoetzel,C.,
            Schaefer,E., Scheidecker,S., Geoffroy,V., Schneider,A., Studer,F.,
            Mattioli,F., Chennen,K., Sigaudy,S., Plassard,D., Poch,O.,
            Piton,A., Strahle,U., Muller,J. and Dollfus,H.
  TITLE     Novel IQCE variations confirm its role in postaxial polydactyly and
            cause ciliary defect phenotype in zebrafish
  JOURNAL   Hum Mutat 41 (1), 240-254 (2020)
   PUBMED   31549751
  REMARK    GeneRIF: Novel IQCE variations confirm its role in postaxial
            polydactyly and cause ciliary defect phenotype in zebrafish.
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Umair,M., Shah,K., Alhaddad,B., Haack,T.B., Graf,E., Strom,T.M.,
            Meitinger,T. and Ahmad,W.
  TITLE     Exome sequencing revealed a splice site variant in the IQCE gene
            underlying post-axial polydactyly type A restricted to lower limb
  JOURNAL   Eur J Hum Genet 25 (8), 960-965 (2017)
   PUBMED   28488682
  REMARK    GeneRIF: Frameshift and a premature stop codon 22 in IQCE
            completely co-segregated with post-axial polydactyly phenotype
            within the family.
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY029256.1, BC071858.1, AL136792.1 and AL137525.1.
            
            On Aug 7, 2007 this sequence version replaced NP_689771.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC071858.1, KJ534872.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000402050.7/ ENSP00000385597.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..695
                     /product="IQ domain-containing protein E isoform 1"
                     /note="IQ domain-containing protein E"
                     /calculated_mol_wt=77167
     Region          29..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IPM2.2)"
     Region          <141..472
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PCQ0; propagated from
                     UniProtKB/Swiss-Prot (Q6IPM2.2)"
     Region          357..390
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IPM2.2)"
     Region          465..521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IPM2.2)"
     Region          564..599
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IPM2.2)"
     Region          618..695
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IPM2.2)"
     CDS             1..695
                     /gene="IQCE"
                     /gene_synonym="1700028P05Rik; PAPA7"
                     /coded_by="NM_152558.5:204..2291"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43542.1"
                     /db_xref="GeneID:23288"
                     /db_xref="HGNC:HGNC:29171"
                     /db_xref="MIM:617631"
ORIGIN      
        1 mflgtgepal dtgddslsav tfdsdvetka krkafhkppp tspkspylsk prkvaswrsl
       61 rtagsmplgg rasltpqklw lgtakpgslt qalnspltwe hawtgvpggt pdcltdtfrv
      121 krphlrrsas nghvpgtpvy rekedmydei ielkkslhvq ksdvdlmrtk lrrleeensr
      181 kdrqieqlld psrgtdfvrt laekrpdasw vinglkqril kleqqckekd gtisklqtdm
      241 kttnleemri ametyyeevh rlqtllasse ttgkkplgek ktgakrqkkm gsallslsrs
      301 vqelteenqs lkedldrvls tsptisktqg yvewskprll rrivelekkl svmessksha
      361 aepvrshppa classsalhr qprgdrnkdh erlrgavrdl keertalqeq llqrdlevkq
      421 llqakadlek elecaregee errereevlr eeiqtltskl qelqemkkee kedcpevphk
      481 aqelpaptps srhceqdwpp dsseeglprp rspcsdgrrd aaarvlqaqw kvykhkkkka
      541 vldeaavvlq aafrghltrt kllaskahgs eppsvpglpd qsspvprvps piaqatgspv
      601 qeeaiviiqs alrahlarar hsatgkrttt aastrrrsas athgdasspp flaalpdpsp
      661 sgpqalaplp gddvnsddsd diviapslpt knfpv
//
LOCUS       NP_001107605             977 aa            linear   PRI 27-APR-2025
DEFINITION  synaptopodin 2-like protein isoform a [Homo sapiens].
ACCESSION   NP_001107605
VERSION     NP_001107605.1
DBSOURCE    REFSEQ: accession NM_001114133.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Wu,J., Ouyang,P., Huang,R., Cui,Y., Yang,Z., Xu,W., Ma,R.,
            Xiang,G., Zeng,W., Wu,W. and Li,J.
  TITLE     METTL16 Promotes Stability of SYNPO2L mRNA and leading to Cancer
            Cell Lung Metastasis by Secretion of COL10A1 and attract the
            Cancer-Associated Fibroblasts
  JOURNAL   Int J Biol Sci 20 (11), 4128-4145 (2024)
   PUBMED   39247832
  REMARK    GeneRIF: METTL16 Promotes Stability of SYNPO2L mRNA and leading to
            Cancer Cell Lung Metastasis by Secretion of COL10A1 and attract the
            Cancer-Associated Fibroblasts.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 977)
  AUTHORS   van Eldik,W., den Adel,B., Monshouwer-Kloots,J., Salvatori,D.,
            Maas,S., van der Made,I., Creemers,E.E., Frank,D., Frey,N.,
            Boontje,N., van der Velden,J., Steendijk,P., Mummery,C., Passier,R.
            and Beqqali,A.
  TITLE     Z-disc protein CHAPb induces cardiomyopathy and contractile
            dysfunction in the postnatal heart
  JOURNAL   PLoS One 12 (12), e0189139 (2017)
   PUBMED   29206857
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 977)
  AUTHORS   Lubitz,S.A., Brody,J.A., Bihlmeyer,N.A., Roselli,C., Weng,L.C.,
            Christophersen,I.E., Alonso,A., Boerwinkle,E., Gibbs,R.A.,
            Bis,J.C., Cupples,L.A., Mohler,P.J., Nickerson,D.A., Muzny,D.,
            Perez,M.V., Psaty,B.M., Soliman,E.Z., Sotoodehnia,N., Lunetta,K.L.,
            Benjamin,E.J., Heckbert,S.R., Arking,D.E., Ellinor,P.T. and Lin,H.
  CONSRTM   NHLBI GO Exome Sequencing Project
  TITLE     Whole Exome Sequencing in Atrial Fibrillation
  JOURNAL   PLoS Genet 12 (9), e1006284 (2016)
   PUBMED   27589061
  REMARK    GeneRIF: we did not observe associations between coding genetic
            variants and Atrial fibrillation (AF), suggesting that large-effect
            coding variation is not the predominant mechanism underlying AF. A
            coding variant in SYNPO2L requires further evaluation to determine
            whether it is causally related to AF
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 977)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 977)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 977)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB188489.1 and AK022983.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB188489.1, AK295873.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2142363 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394810.3/ ENSP00000378289.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..977
                     /product="synaptopodin 2-like protein isoform a"
                     /note="synaptopodin 2-like protein"
                     /calculated_mol_wt=102350
     Region          8..85
                     /region_name="PDZ_SYNPO2-like"
                     /note="PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin
                     2-like protein (SYNPO2L), and related domains; cd10820"
                     /db_xref="CDD:467264"
     Site            order(16..22,34,37,66,70,73..74)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467264"
     Region          91..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          <168..650
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          317..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          364..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            386
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          <415..550
                     /region_name="PRK14954"
                     /note="DNA polymerase III subunits gamma and tau;
                     Provisional"
                     /db_xref="CDD:184918"
     Site            466
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            469
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            479
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          697..802
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            757
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            790
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            792
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            806
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            826
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            889
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            891
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            910
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            921
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          922..950
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            955
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            957
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     CDS             1..977
                     /gene="SYNPO2L"
                     /coded_by="NM_001114133.3:108..3041"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44438.1"
                     /db_xref="GeneID:79933"
                     /db_xref="HGNC:HGNC:23532"
ORIGIN      
        1 mgaeeevlvt lsggapwgfr lhggaeqrkp lqvskirrrs qagraglrer dqllaingvs
       61 ctnlshasam slidasgnql vltvqrlade gpvqspsphe lqvlsplspl speppgapvp
      121 qplqpgslrs ppdseayyge tdsdadgpat qekprrprrr gptrptppga ppdevylsds
      181 paepaptipg ppsqgdsrvs spswedgaal qpppaealll phgplrpgph lipmvgpvph
      241 pvaedlttty tqkakqaklq raeslqeksi keaktkcrti aslltaapnp hskgvlmfkk
      301 rrqrakkytl vsfgaaagtg aeeedgvppt seseldeeaf sdarsltnqs dwdspyldme
      361 laragsrase gqgsglggql sevsgrgvql feqqrqrads stqelarvep aamlngeglq
      421 sppraqsapp eaavlppspl papvasprpf qpgggaptpa psifnrsarp ftpglqgqrp
      481 tttsvifrpl apkrandslg glspapppfl ssqgptplps ftsgvpshap vsgspstprs
      541 sgpvtatssl yipapsrpvt pggapeppap psaaamtsta siflsaplrp sarpeapapg
      601 pgapeppsar eqrisvpaar tgilqearrr gtrkqmfrpg keetknspnp ellslvqnld
      661 ekpraggaes gpeedalslg aeacnfmqpv garsyktlph vtpktpppma pktpppmtpk
      721 tpppvapkpp srglldglvn gaassagipe pprlqgrgge lfakrqsrad ryvvegtpgp
      781 glgprprsps ptpslppswk yspnirappp iaynpllspf fpqaartlpk aqsqgpratp
      841 kqgikaldfm rhqpyqlkta mfcfdevppt pgpiasgspk tarvqeirrf stpapqptae
      901 plaptvlapr aattldepiw rtelasapvp spapppeapr glgaspsscg fqvarprfsa
      961 trtglqahvw rpgaghq
//
LOCUS       NP_065974               2354 aa            linear   PRI 27-APR-2025
DEFINITION  DBF4-type zinc finger-containing protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_065974 XP_371590 XP_942327
VERSION     NP_065974.1
DBSOURCE    REFSEQ: accession NM_020923.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2354)
  AUTHORS   Chacon-Camacho,O.F., Sobreira,N., You,J., Pina-Aguilar,R.E.,
            Villegas-Ruiz,V. and Zenteno,J.C.
  TITLE     Exome sequencing identifies a de novo frameshift mutation in the
            imprinted gene ZDBF2 in a sporadic patient with Nasopalpebral
            Lipoma-coloboma syndrome
  JOURNAL   Am J Med Genet A 170 (7), 1934-1937 (2016)
   PUBMED   27139419
  REMARK    GeneRIF: Exome sequencing identified a de novo heterozygous
            frameshift dinucleotide insertion c.6245_6246 insTT
            (p.His2082fs*67) in ZDBF2 (zinc finger, DBF-type containing 2), a
            gene located at 2q33.3. This variant was absent in parental DNA, in
            a set of 300 ethnically matched controls, and in public exome
            variant databases
REFERENCE   2  (residues 1 to 2354)
  AUTHORS   Kobayashi,H., Yanagisawa,E., Sakashita,A., Sugawara,N.,
            Kumakura,S., Ogawa,H., Akutsu,H., Hata,K., Nakabayashi,K. and
            Kono,T.
  TITLE     Epigenetic and transcriptional features of the novel human
            imprinted lncRNA GPR1AS suggest it is a functional ortholog to
            mouse Zdbf2linc
  JOURNAL   Epigenetics 8 (6), 635-645 (2013)
   PUBMED   23764515
REFERENCE   3  (residues 1 to 2354)
  AUTHORS   Kobayashi,H., Yamada,K., Morita,S., Hiura,H., Fukuda,A., Kagami,M.,
            Ogata,T., Hata,K., Sotomaru,Y. and Kono,T.
  TITLE     Identification of the mouse paternally expressed imprinted gene
            Zdbf2 on chromosome 1 and its imprinted human homolog ZDBF2 on
            chromosome 2
  JOURNAL   Genomics 93 (5), 461-472 (2009)
   PUBMED   19200453
  REMARK    GeneRIF: the human homolog (ZDBF2) of the mouse Zdbf2 gene showed
            paternal allele-specific expression in human lymphocytes but not in
            the human placenta.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB775781.1 and BQ021839.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Nov 21, 2007 this sequence version replaced
            XP_371590.3, XP_942327.1.
            
            Summary: This gene encodes a protein containing DBF4-type zinc
            finger domains. This gene is imprinted and paternally expressed in
            lymphocytes but is more stochastically expressed in the placenta.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB775781.1, AK127271.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene         :: PMID: 19200453
            MANE Ensembl match     :: ENST00000374423.9/ ENSP00000363545.3
            RefSeq Select criteria :: based on longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..2354
                     /product="DBF4-type zinc finger-containing protein 2
                     isoform 1"
                     /note="DBF4-type zinc finger-containing protein 2"
                     /calculated_mol_wt=265488
     Region          3..>34
                     /region_name="ZnF_DBF"
                     /note="Zinc finger in DBF-like proteins; smart00586"
                     /db_xref="CDD:128854"
     Region          85..134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK1.3)"
     Region          229..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK1.3)"
     Region          493..512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK1.3)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q9HCK1.3)"
     Region          693..723
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK1.3)"
     Region          862..886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK1.3)"
     Region          1352..1375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK1.3)"
     Region          1680..1736
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK1.3)"
     Region          1752..1793
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK1.3)"
     Region          2280..2326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK1.3)"
     CDS             1..2354
                     /gene="ZDBF2"
                     /gene_synonym="Slx9"
                     /coded_by="NM_020923.3:387..7451"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46501.1"
                     /db_xref="GeneID:57683"
                     /db_xref="HGNC:HGNC:29313"
                     /db_xref="MIM:617059"
ORIGIN      
        1 mqkrqgycsy crvqynnleq hlfsaqhrsl trqsrrqict sslmerflqd vlqhhpyhcq
       61 essstqdeth vntgsssevv hlddafseee eededkvede dateerpsev sepieelhsr
      121 phksqegtqe vsvrpsviqk lekgqqqple fvhkigasvr kcnlvdigqa tnnrsnlvrp
      181 pvicnapasc lpessndrpv tanttslppa ahldsvskcd pnkvekyleq pdgasrnpvp
      241 sshvettsfs yqkhkesnrk slrmnsdklv lwkdvksqgk tlsaglkfhe rmgtkgslrv
      301 kspsklavnp nktdmpsnkg ifedtiaknh eeffsnmdct qeekhlvfnk tafweqkcsv
      361 ssemkfdcis lqsasdqpqe taqdlslwke eqidqednye srgsemsfdc sssfhsltdq
      421 skvsakevnl skevrtdvqy knnksyvski ssdcddilhl vtnqsqmivk eislqnarhi
      481 slvdqsyess ssetnfdcda spqstsdypq qsvtevnlpk evhiglvdkn ygssssevsa
      541 dsvfplqsvv drppvavtet klrkkahtsl vdnygsscse tsfdcdvsle svvdhpqltv
      601 kgrnlkgrqv hlkhkkrkps sakahldcdv slgtvadesq ravekinllk eknadlmdmn
      661 ceshgpemgf qadaqladqs qvaeierqkv dvdlenksvq ssrsslssds paslyhsahd
      721 epqealdevn lkelnidmev rsydcsssel tfdsdpplls vteqshldae gkerhidled
      781 escesdssei tfdsdiplys vidqpevavy eeetvdlesk snescvseit fdsdiplhsg
      841 ndhpevavke viqkeeyihl erkndepsgs eissdshapl hsvtnspeva vkklnpqkee
      901 qvhlenkene pidsevsldy niifhsvtgr sedpikeisl htkehmylen ksvfetslds
      961 dvplqaathk pevivketwl qrekhaefqg rstefsgskt sldsgvphys vtepqvavnk
     1021 inrkkqyvle nkndkcsgse iildsnvppq smtdqpqlaf lkekhvnlkd knsksgdski
     1081 tfdseqlqea vkkidqwkee viglknkine pstyklihhp dvsvqsvadq pkvaikhvnl
     1141 gnenhmylev knsqyscsem nldsgflgqs ivnrpqitil eqehielegk hnqccgsevs
     1201 fdsddplqsv adrlretvke islwkdeevd tedrrneakg feimydsdvl qpvagqpeev
     1261 vkevslwkeh vdlenkivkp tdsrinfdsh eplqsvtnki pgankeinll reehvclddk
     1321 gyvpsdseii yvsniplqsv ikqphileee hasledkssn syspeessds ndsfqaaade
     1381 lqkpvkeinl wkedhiyled ksyklgdfdv syashipvqf vtdqssvpvk einlqkkdhn
     1441 dlenkncevc gseikchscv hlqsevdqpq vsykeadlqk eehvvmeekt dqpsdsemmy
     1501 dsdvpfqivv nqfpgsvket hlpkvvlvdl vpgdsdyevi sddiplqlvt dppqltvkdi
     1561 scintecidi edkscdffgs evrcnckast psmtnqcket fkiinrkkdy iilgepscqs
     1621 cgsemnfnvd asdqsmtyes qgpdekmvky idsedkscgy ngskgkfnle dtshrtthrl
     1681 qkahkeaslr kdprnaglkg kscqssasav dfgassksal hrradkkkrs klkhrdlevs
     1741 cepdgfemnf qcapplpsdt dqpqetvkkr hpckkvssdl keknhdsqss svlkvdsvrn
     1801 lkkakdvied npdepvleal phvppsfvgk twsqimredd ikinalvkef regrfhcyfd
     1861 ddcetkkvss kgkkkvtwad lqgkedtapt qavsesddiv cgisdiddls valdkpchrh
     1921 ppaerppkqk grvasqcqta kishstqtsc knypvmkrki irqeedppks kcsrlqddrk
     1981 tkkkvkigtv efpasctkvl kpmqpkalvc vlsslniklk egeglpfpkm rhhswdndir
     2041 fickykrnif dyyeplikqi vispplsviv peferrnwvk ihfnrsnqns sagdndadgq
     2101 gsasaplmav parygfnshq gtsdsslfle eskvlharel pkkrnfqltf lnhdvvkisp
     2161 ksvrnklles qskkkihgkr vttssnklgf pkkvykpiil qqkprkasek qsiwirtkps
     2221 diirkyisky svflrhryqs rsaflgrylk kkksvvsrlk kakrtakvll nssvppagae
     2281 elssamanpp pkrpvrascr varrrkktde syhgrqkgps tpvraydlrs ssclqqrerm
     2341 mtrlanklrg nevk
//
LOCUS       NP_066013               1250 aa            linear   PRI 27-APR-2025
DEFINITION  immunoglobulin superfamily DCC subclass member 4 precursor [Homo
            sapiens].
ACCESSION   NP_066013
VERSION     NP_066013.1
DBSOURCE    REFSEQ: accession NM_020962.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1250)
  AUTHORS   Kutting,F., Gebauer,F., Zweerink,S., Kramer,L., Schramm,C.,
            Quaas,A., Bruns,C., Goeser,T. and Nierhoff,D.
  TITLE     Expression of Neighbor of Punc E11 (NOPE) in early stage esophageal
            adenocarcinoma is associated with reduced survival
  JOURNAL   Sci Rep 12 (1), 3584 (2022)
   PUBMED   35246597
  REMARK    GeneRIF: Expression of Neighbor of Punc E11 (NOPE) in early stage
            esophageal adenocarcinoma is associated with reduced survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1250)
  AUTHORS   Zweerink,S., Mesghenna,S., Mueck,V., Schulte,S., Kuetting,F.,
            Quaas,A., Goeser,T. and Nierhoff,D.
  TITLE     First evaluation of Neighbor of Punc E11 (NOPE) as a novel marker
            in human hepatocellular carcinoma
  JOURNAL   Cancer Biomark 30 (1), 75-83 (2021)
   PUBMED   32986656
  REMARK    GeneRIF: First evaluation of Neighbor of Punc E11 (NOPE) as a novel
            marker in human hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 1250)
  AUTHORS   Marquardt,J.U., Quasdorff,M., Varnholt,H., Curth,H.M.,
            Mesghenna,S., Protzer,U., Goeser,T. and Nierhoff,D.
  TITLE     Neighbor of Punc E11, a novel oncofetal marker for hepatocellular
            carcinoma
  JOURNAL   Int J Cancer 128 (10), 2353-2363 (2011)
   PUBMED   20658536
  REMARK    GeneRIF: identified Nope as a novel oncofetal surface marker for
            murine and human HCC. Nope is specifically expressed by epithelial
            tumor cells but not in preneoplastic stages and is a promising
            marker
REFERENCE   4  (residues 1 to 1250)
  AUTHORS   Kamatani,Y., Matsuda,K., Okada,Y., Kubo,M., Hosono,N., Daigo,Y.,
            Nakamura,Y. and Kamatani,N.
  TITLE     Genome-wide association study of hematological and biochemical
            traits in a Japanese population
  JOURNAL   Nat Genet 42 (3), 210-215 (2010)
   PUBMED   20139978
REFERENCE   5  (residues 1 to 1250)
  AUTHORS   Salbaum,J.M. and Kappen,C.
  TITLE     Cloning and expression of nope, a new mouse gene of the
            immunoglobulin superfamily related to guidance receptors
  JOURNAL   Genomics 64 (1), 15-23 (2000)
   PUBMED   10708514
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB052622.1 and AC105129.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB052622.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000352385.3/ ENSP00000319623.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..1250
                     /product="immunoglobulin superfamily DCC subclass member 4
                     precursor"
                     /note="likely ortholog of mouse neighbor of Punc E11"
                     /calculated_mol_wt=131782
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2447
     mat_peptide     25..1250
                     /product="Immunoglobulin superfamily DCC subclass member
                     4. /id=PRO_0000304622"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY8.1)"
                     /calculated_mol_wt=131782
     Region          53..135
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          53..57
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          69..73
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            90
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY8.1)"
     Region          91..95
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY8.1)"
     Region          118..123
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          132..135
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          145..218
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY8.1)"
     Region          160..164
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409544"
     Region          173..177
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409544"
     Region          195..199
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409544"
     Region          209..214
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409544"
     Region          250..331
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Site            252
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY8.1)"
     Region          261..265
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409389"
     Region          274..279
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409389"
     Region          295..299
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409389"
     Region          309..314
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409389"
     Region          324..327
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409389"
     Region          350..422
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          352..356
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:143205"
     Region          365..369
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:143205"
     Region          388..392
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:143205"
     Region          402..407
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:143205"
     Region          415..418
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:143205"
     Site            order(429,495,510)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          430..515
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          <477..812
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            order(511..512,514..515)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            582
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY8.1)"
     Region          850..942
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(931..932,934..935)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            958..978
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY8.1)"
     Region          <984..1250
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            995
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY8.1)"
     Region          1140..1175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY8.1)"
     Region          1215..1250
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY8.1)"
     CDS             1..1250
                     /gene="IGDCC4"
                     /gene_synonym="DDM36; NOPE"
                     /coded_by="NM_020962.3:86..3838"
                     /db_xref="CCDS:CCDS10206.1"
                     /db_xref="GeneID:57722"
                     /db_xref="HGNC:HGNC:13770"
                     /db_xref="MIM:616810"
ORIGIN      
        1 margdagrgr gllaltfcll aargelllpq ettvelscgv gplqvilgpe qaavlncslg
       61 aaaagpptrv twskdgdtll ehdhlhllpn gslwlsqpla pngsdesvpe avgviegnys
      121 clahgplgvl asqtavvkla tladfslhpe sqtveengta rfechieglp apiitwekdq
      181 vtlpeeprli vlpngvlqil dvqesdagpy rcvatnsarq hfsqeallsv ahrgslastr
      241 gqdvvivaap enttvvsgqs vvmecvasad ptpfvswvrq dgkpistdvi vlgrtnllia
      301 naqpwhsgvy vcrankprtr dfataaaelr vlaapaitqa pealsrtras tarfvcrasg
      361 eprpalrwlh ngaplrpngr vkvqggggsl vitqiglqda gyyqcvaens agmacaaasl
      421 avvvreglps aptrvtatpl sssavlvawe rpemhseqii gfslhyqkar gmdnveyqfa
      481 vnndttelqv rdlepntdye fyvvaysqlg asrtstpalv htlddvpsaa pqlslsspnp
      541 sdirvawlpl ppslsngqvv kykieyglgk edqifstevr gnetqlmlns lqpnkvyrvr
      601 isagtaagfg apsqwmhhrt psmhnqshvp fapaelkvqa kmeslvvswq ppphptqisg
      661 yklywrevga eeeangdrlp ggrgdqawdv gpvrlkkkvk qyeltqlvpg rlyevklvaf
      721 nkhedgyaav wkgktekapa pdmpiqrgpp lppahvhaes nsstsiwlrw kkpdfttvki
      781 vnytvrfspw glrnaslvty ytssgedili gglkpftkye favqshgvdm dgpfgsvver
      841 stlpdrpstp psdlrlsplt pstvrlhwcp ptepngeive ylilyssnht qpehqwtllt
      901 tqgnifsaev hglesdtryf fkmgartevg pgpfsrlqdv itlqeklsds ldmhsvtgii
      961 vgvclgllcl lacmcaglrr sphreslpgl sstatpgnpa lysrarlgpp sppaaheles
     1021 lvhphpqdws pppsdvedra evhslmgggv segrshskrk iswaqpsgls wagswagcel
     1081 pqagprpalt rallppagtg qtlllqalvy daikgngrkk sppacrnqve aevivhsdfs
     1141 asngnpdlhl qdlepedplp peapdlisgv gdpgqgaawl drelggcela apgpdrltcl
     1201 peaasascsy pdlqpgevle etpgdscqlk spcplgaspg lprspvsssa
//
LOCUS       NP_060742                722 aa            linear   PRI 27-APR-2025
DEFINITION  dynein axonemal intermediate chain 7 isoform a [Homo sapiens].
ACCESSION   NP_060742
VERSION     NP_060742.4
DBSOURCE    REFSEQ: accession NM_018272.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Eijgelsheim,M., Newton-Cheh,C., Sotoodehnia,N., de Bakker,P.I.,
            Muller,M., Morrison,A.C., Smith,A.V., Isaacs,A., Sanna,S., Dorr,M.,
            Navarro,P., Fuchsberger,C., Nolte,I.M., de Geus,E.J., Estrada,K.,
            Hwang,S.J., Bis,J.C., Ruckert,I.M., Alonso,A., Launer,L.J.,
            Hottenga,J.J., Rivadeneira,F., Noseworthy,P.A., Rice,K.M., Perz,S.,
            Arking,D.E., Spector,T.D., Kors,J.A., Aulchenko,Y.S., Tarasov,K.V.,
            Homuth,G., Wild,S.H., Marroni,F., Gieger,C., Licht,C.M.,
            Prineas,R.J., Hofman,A., Rotter,J.I., Hicks,A.A., Ernst,F.,
            Najjar,S.S., Wright,A.F., Peters,A., Fox,E.R., Oostra,B.A.,
            Kroemer,H.K., Couper,D., Volzke,H., Campbell,H., Meitinger,T.,
            Uda,M., Witteman,J.C., Psaty,B.M., Wichmann,H.E., Harris,T.B.,
            Kaab,S., Siscovick,D.S., Jamshidi,Y., Uitterlinden,A.G.,
            Folsom,A.R., Larson,M.G., Wilson,J.F., Penninx,B.W., Snieder,H.,
            Pramstaller,P.P., van Duijn,C.M., Lakatta,E.G., Felix,S.B.,
            Gudnason,V., Pfeufer,A., Heckbert,S.R., Stricker,B.H.,
            Boerwinkle,E. and O'Donnell,C.J.
  TITLE     Genome-wide association analysis identifies multiple loci related
            to resting heart rate
  JOURNAL   Hum Mol Genet 19 (19), 3885-3894 (2010)
   PUBMED   20639392
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Kohno,T., Kunitoh,H., Suzuki,K., Yamamoto,S., Kuchiba,A.,
            Matsuno,Y., Yanagitani,N. and Yokota,J.
  TITLE     Association of KRAS polymorphisms with risk for lung adenocarcinoma
            accompanied by atypical adenomatous hyperplasias
  JOURNAL   Carcinogenesis 29 (5), 957-963 (2008)
   PUBMED   18299280
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Manenti,G., Galbiati,F., Pettinicchio,A., Spinola,M., Piconese,S.,
            Leoni,V.P., Conti,B., Ravagnani,F., Incarbone,M., Pastorino,U. and
            Dragani,T.A.
  TITLE     A V141L polymorphism of the human LRMP gene is associated with
            survival of lung cancer patients
  JOURNAL   Carcinogenesis 27 (7), 1386-1390 (2006)
   PUBMED   16410263
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092794.10 and AC023510.16.
            
            On Nov 23, 2018 this sequence version replaced NP_060742.3.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC031047.1, AK093102.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395987.8/ ENSP00000379310.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..722
                     /product="dynein axonemal intermediate chain 7 isoform a"
                     /note="cancer susceptibility 1; dynein intermediate chain
                     CFAP94, axonemal; protein phosphatase 1 regulatory subunit
                     54; lung adenoma susceptibility 1-like protein; cancer
                     susceptibility candidate gene 1 protein; protein CASC1;
                     cilia and flagella associated protein 94; cancer
                     susceptibility candidate 1"
                     /calculated_mol_wt=83639
     Region          40..230
                     /region_name="Casc1_N"
                     /note="Cancer susceptibility candidate 1 N-terminus;
                     pfam15927"
                     /db_xref="CDD:464947"
     Region          467..633
                     /region_name="Casc1_C"
                     /note="Cancer susceptibility candidate 1 C-terminal;
                     pfam12366"
                     /db_xref="CDD:432508"
     CDS             1..722
                     /gene="DNAI7"
                     /gene_synonym="CASC1; CFAP94; LAS1; PPP1R54"
                     /coded_by="NM_018272.5:83..2251"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31759.2"
                     /db_xref="GeneID:55259"
                     /db_xref="HGNC:HGNC:29599"
                     /db_xref="MIM:616906"
ORIGIN      
        1 mgpkakksgs kkkkvtkaer lkllqeeeer rlkeeeearl kyekeemerl eiqriekekw
       61 hrleakdler rneeleelyl lercfpeaek lkqetkllsq wkhyiqcdgs pdpsvaqemn
      121 tfislwkekt netfeeviek skvvlnliek lkfilletpp cdlqdkniiq yqesilqlqe
      181 llhlkfgvat eillkqastl adldsgnmek vikdenvtly vwanlkknpr hrsvrfsetq
      241 igfeiprila tsdiavrllh thydhvsalh pvstpskeyt savtelvkdd vknvekaisk
      301 eveeeskqqe rgshliqeee ikveeeqgdi evkmssaeee seaikcerem kvlsetvsaa
      361 qlllvensse kpdffednvv dlcqfttlgg vyhldilelp pqckpvkgwm iveilkeglq
      421 kytyppette efetenafpp ievtlevhen viffedpvvv rwdaegkhwr tdgisnvsyk
      481 pkerlvtfsl dtfgpvtliq dahinmpyqs welrpldvnk vlltvttvft eiqiqikenl
      541 cmlssiklkd kkhisilegt wmtpipfiia lkeaglnifp trhshfyvii nnkvplvevk
      601 ayrqmallss afafgwskwn llcnstkvvf kvrehlteac tenpnwallm fsgdraqrlk
      661 ikeeseafse alkeetefhs tlyhmvkdfa seeamekvrs sncqfvnsvc hmllstrlls
      721 ys
//
LOCUS       NP_003923                369 aa            linear   PRI 27-APR-2025
DEFINITION  hsc70-interacting protein isoform 1 [Homo sapiens].
ACCESSION   NP_003923
VERSION     NP_003923.2
DBSOURCE    REFSEQ: accession NM_003932.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Stetskaya,T.A., Krapiva,A.B., Kobzeva,K.A., Gurtovoy,D.E.,
            Komkova,G.V., Polonikov,A.V. and Bushueva,O.Y.
  TITLE     Polymorphism in Genes Encoding Adaptor Proteins ST13 and STIP1 and
            the Risk of Ischemic Stroke: a Pilot Study
  JOURNAL   Bull Exp Biol Med 176 (4), 477-480 (2024)
   PUBMED   38492099
  REMARK    GeneRIF: Polymorphism in Genes Encoding Adaptor Proteins ST13 and
            STIP1 and the Risk of Ischemic Stroke: a Pilot Study.
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Luo,M.S., Huang,G.J. and Liu,H.B.
  TITLE     An autophagy-related model of 4 key genes for predicting prognosis
            of patients with laryngeal cancer
  JOURNAL   Medicine (Baltimore) 99 (30), e21163 (2020)
   PUBMED   32791689
  REMARK    GeneRIF: An autophagy-related model of 4 key genes for predicting
            prognosis of patients with laryngeal cancer.
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Vijverberg,S.J., Koster,E.S., Tavendale,R., Leusink,M.,
            Koenderman,L., Raaijmakers,J.A., Postma,D.S., Koppelman,G.H.,
            Turner,S.W., Mukhopadhyay,S., Tse,S.M., Tantisira,K.G.,
            Hawcutt,D.B., Francis,B., Pirmohamed,M., Pino-Yanes,M., Eng,C.,
            Burchard,E.G., Palmer,C.N. and Maitland-van der Zee,A.H.
  TITLE     ST13 polymorphisms and their effect on exacerbations in
            steroid-treated asthmatic children and young adults
  JOURNAL   Clin Exp Allergy 45 (6), 1051-1059 (2015)
   PUBMED   25616159
  REMARK    GeneRIF: A novel susceptibility gene, ST13, coding for a
            cochaperone of the glucocorticoid receptor, is associated with
            exacerbations in asthmatic children and young adults despite their
            ICS use.
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Hosp,F., Vossfeldt,H., Heinig,M., Vasiljevic,D., Arumughan,A.,
            Wyler,E., Landthaler,M., Hubner,N., Wanker,E.E., Lannfelt,L.,
            Ingelsson,M., Lalowski,M., Voigt,A. and Selbach,M.
  CONSRTM   Genetic and Environmental Risk for Alzheimer's Disease GERAD1
            Consortium
  TITLE     Quantitative interaction proteomics of neurodegenerative disease
            proteins
  JOURNAL   Cell Rep 11 (7), 1134-1146 (2015)
   PUBMED   25959826
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Johnson,B.D., Schumacher,R.J., Ross,E.D. and Toft,D.O.
  TITLE     Hop modulates Hsp70/Hsp90 interactions in protein folding
  JOURNAL   J Biol Chem 273 (6), 3679-3686 (1998)
   PUBMED   9452498
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Cao,J., Cai,X., Zheng,L., Geng,L., Shi,Z., Pao,C.C. and Zheng,S.
  TITLE     Characterization of colorectal-cancer-related cDNA clones obtained
            by subtractive hybridization screening
  JOURNAL   J Cancer Res Clin Oncol 123 (8), 447-451 (1997)
   PUBMED   9292708
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Prapapanich,V., Chen,S., Toran,E.J., Rimerman,R.A. and Smith,D.F.
  TITLE     Mutational analysis of the hsp70-interacting protein Hip
  JOURNAL   Mol Cell Biol 16 (11), 6200-6207 (1996)
   PUBMED   8887650
REFERENCE   9  (residues 1 to 369)
  AUTHORS   Mo,Y., Zheng,S. and Shen,D.
  TITLE     [Differential expression of HSU17714 gene in colorectal cancer and
            normal colonic mucosa]
  JOURNAL   Zhonghua Zhong Liu Za Zhi 18 (4), 241-243 (1996)
   PUBMED   9387309
REFERENCE   10 (residues 1 to 369)
  AUTHORS   Prapapanich,V., Chen,S., Nair,S.C., Rimerman,R.A. and Smith,D.F.
  TITLE     Molecular cloning of human p48, a transient component of
            progesterone receptor complexes and an Hsp70-binding protein
  JOURNAL   Mol Endocrinol 10 (4), 420-431 (1996)
   PUBMED   8721986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z98048.1, BC121107.1, U17714.1
            and BM679025.1.
            
            On Apr 4, 2002 this sequence version replaced NP_003923.1.
            
            Summary: The protein encoded by this gene is an adaptor protein
            that mediates the association of the heat shock proteins HSP70 and
            HSP90. This protein has been shown to be involved in the assembly
            process of glucocorticoid receptor, which requires the assistance
            of multiple molecular chaperones. The expression of this gene is
            reported to be downregulated in colorectal carcinoma tissue
            suggesting that it is a candidate tumor suppressor gene.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.910865.1,
                                           SRR1660805.170772.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216218.8/ ENSP00000216218.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..369
                     /product="hsc70-interacting protein isoform 1"
                     /note="progesterone receptor-associated p48 protein;
                     Hsp70-interacting protein; putative tumor suppressor ST13;
                     heat shock 70kD protein binding protein; hsc70-interacting
                     protein; aging-associated protein 2; renal carcinoma
                     antigen NY-REN-33; suppression of tumorigenicity 13
                     protein; suppression of tumorigenicity 13 (colon
                     carcinoma) (Hsp70 interacting protein); testis secretory
                     sperm-binding protein Li 233m"
                     /calculated_mol_wt=41201
     Region          3..43
                     /region_name="Hip_N"
                     /note="N-terminal dimerization domain of the
                     Hsp70-interacting protein (Hip) and similar proteins;
                     cd14438"
                     /db_xref="CDD:271228"
     Site            order(5..6,8..10,12..13,16..17,23,27,30..31,33..35,37..43)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:271228"
     Region          38..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50502.2)"
     Region          114..147
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P50502.2)"
     Site            order(122..123,125,149,152..153,156..157,159..160,183,
                     186..187,190..191,194)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <128..>221
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          147..177
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          148..181
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P50502.2)"
     Region          182..215
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P50502.2)"
     Region          182..210
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          256..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50502.2)"
     Region          319..358
                     /region_name="STI1"
                     /note="Heat shock chaperonin-binding motif; smart00727"
                     /db_xref="CDD:128966"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GRK5.
                     /evidence=ECO:0000269|PubMed:21728385; propagated from
                     UniProtKB/Swiss-Prot (P50502.2)"
     Site            353
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99L47; propagated from
                     UniProtKB/Swiss-Prot (P50502.2)"
     Site            360
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99L47; propagated from
                     UniProtKB/Swiss-Prot (P50502.2)"
     CDS             1..369
                     /gene="ST13"
                     /gene_synonym="AAG2; FAM10A1; FAM10A4; HIP; HOP; HSPABP;
                     HSPABP1; P48; PRO0786; SNC6"
                     /coded_by="NM_003932.5:100..1209"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14006.1"
                     /db_xref="GeneID:6767"
                     /db_xref="HGNC:HGNC:11343"
                     /db_xref="MIM:606796"
ORIGIN      
        1 mdprkvnelr afvkmckqdp svlhteemrf lrewvesmgg kvppatqkak seentkeekp
       61 dskkveedlk adepsseesd leidkegvie pdtdapqemg denaeiteem mdqandkkva
      121 aiealndgel qkaidlftda iklnprlail yakrasvfvk lqkpnaaird cdraieinpd
      181 saqpykwrgk ahrllghwee aahdlalack ldydedasam lkevqpraqk iaehrrkyer
      241 kreereiker iervkkaree heraqreeea rrqsgaqygs fpggfpggmp gnfpggmpgm
      301 gggmpgmagm pglneilsdp evlaamqdpe vmvafqdvaq npanmskyqs npkvmnlisk
      361 lsakfggqa
//
LOCUS       NP_444270               1074 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 518B [Homo sapiens].
ACCESSION   NP_444270 XP_114418
VERSION     NP_444270.2
DBSOURCE    REFSEQ: accession NM_053042.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Riffo-Campos,A.L., Castillo,J., Vallet-Sanchez,A., Ayala,G.,
            Cervantes,A., Lopez-Rodas,G. and Franco,L.
  TITLE     In silico RNA-seq and experimental analyses reveal the differential
            expression and splicing of EPDR1 and ZNF518B genes in relation to
            KRAS mutations in colorectal cancer cells
  JOURNAL   Oncol Rep 36 (6), 3627-3634 (2016)
   PUBMED   27805251
  REMARK    GeneRIF: ZNF518B exhibits a pattern of isoform abundance dependent
            on KRAS G13D and G12D mutations.
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Zhang,X.Y., Geng,T.T., Liu,L.J., Yuan,D.Y., Feng,T., Kang,L.L.,
            Jin,T.B. and Chen,C.
  TITLE     SLC2A9 and ZNF518B polymorphisms correlate with gout-related
            metabolic indices in Chinese Tibetan populations
  JOURNAL   Genet Mol Res 14 (3), 9915-9921 (2015)
   PUBMED   26345926
  REMARK    GeneRIF: SLC2A9 and ZNF518B polymorphisms correlate with
            gout-related metabolic indices in Chinese Tibetan populations
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Jin,T.B., Ren,Y., Shi,X., Jiri,M., He,N., Feng,T., Yuan,D. and
            Kang,L.
  TITLE     Genetic variations in the CLNK gene and ZNF518B gene are associated
            with gout in case-control sample sets
  JOURNAL   Rheumatol Int 35 (7), 1141-1147 (2015)
   PUBMED   25591661
  REMARK    GeneRIF: CLNK and ZNF518B SNPs may have potential as diagnostic and
            prognostic marker for Chinese gout patients.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC110768.5, BC040874.1, CD656908.1 and AL833306.1.
            
            On Feb 8, 2005 this sequence version replaced NP_444270.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.86079.1,
                                           SRR1803611.273721.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145774 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326756.4/ ENSP00000317614.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.1"
     Protein         1..1074
                     /product="zinc finger protein 518B"
                     /calculated_mol_wt=119401
     Region          12..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D4.2)"
     Region          137..157
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(142,144,146,148..149,152..153,156,169,175..176,
                     179..180,183,197,199,201,203..204,207..208,212)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          164..186
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          164..184
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          192..213
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          568..590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D4.2)"
     Region          603..632
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D4.2)"
     Region          678..704
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D4.2)"
     CDS             1..1074
                     /gene="ZNF518B"
                     /coded_by="NM_053042.3:506..3730"
                     /db_xref="CCDS:CCDS33960.1"
                     /db_xref="GeneID:85460"
                     /db_xref="HGNC:HGNC:29365"
                     /db_xref="MIM:617734"
ORIGIN      
        1 mkdigqqlyt thlngghnsl tmspkqpdan gaprpnrqea qtllyqgsea eaammtiatc
       61 akcksvhkis lqdlqkgtgk dgmyvcfqcs lgaappnfhf vsnnssathv gnktenfsss
      121 vnskfkvrnf kpgkyycdkc rfstkdplqy kkhtlqheei kficshcsyi sytkgefqrh
      181 lvkhtgifpy qceycdygai rndyivkhtk rvheragakr pvkavaklep krtgtskqnp
      241 ellkasnprt tfqnkwsdql sgfslhankd kmhnimllpe pkeyqkdvvc ipnkmtlsep
      301 nevnlfenkn vevevlspak epvqpgmplt vvapaelvvp anclaqlidv kvvngtqqlv
      361 lklfpleenn cleagrdngg nsermvkekg sneqekvlsa ektksltvdg nvgklvgids
      421 fqpsvqkqlk nvkwvrsydf impnssvhnn gksfinseti edfqkknnly phrtafpsva
      481 lkghslasvf knsvlrslga asnpfpykaa vcfaesgrnl hsssqqllpf aaspatcsfs
      541 gekgllpvse ndlestskvn ipvkvvssnr kqednqteeh kavstvgqis sqhkseylhi
      601 nitgedrsqq pgdkplelkn sertnntndg pvissvfsls sgsenvpegi kwnsstskik
      661 siellrrkia qliescgkps slasnsahrr svgqaskgts katsegiqei nvsltglghs
      721 tgtlqkppnd ggitgnrqlt hqqiyphfad gsnrktksrv arkahvatpv lipkgavlrv
      781 lnssenahii eatceapvsi pcserqlikp vpfcpvrqad sdlqplrser gpidmspnie
      841 tplrpklrke savcstihrk tgllygqqgs selnkqgrll srslsisrnk tkqvhlsrkk
      901 nkiqaepsrc lkdpsifqva rqlrliaakp dqlikcprrn qpvivlnhpd vdspevtnvm
      961 kvinkykgnv lkvvlsertr cqlgirrhhv rltyqnaeea sqikrqmmlk mklkkvhknn
     1021 yqvvdslpdd ssqcvfkcwf cgrlyedqee wmshgqrhli eatrdwdvls skgk
//
LOCUS       NP_690863                567 aa            linear   PRI 27-APR-2025
DEFINITION  L-amino-acid oxidase isoform 1 precursor [Homo sapiens].
ACCESSION   NP_690863
VERSION     NP_690863.1
DBSOURCE    REFSEQ: accession NM_152899.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Ye,F., Wang,L., Li,Y., Dong,C., Zhou,L. and Xu,J.
  TITLE     IL4I1 in M2-like macrophage promotes glioma progression and is a
            promising target for immunotherapy
  JOURNAL   Front Immunol 14, 1338244 (2024)
   PUBMED   38250074
  REMARK    GeneRIF: IL4I1 in M2-like macrophage promotes glioma progression
            and is a promising target for immunotherapy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Run,L., Tian,Z., Xu,L., Du,J., Li,N., Wang,Q. and Sun,H.
  TITLE     Knockdown of IL4I1 Improved High Glucose-evoked Insulin Resistance
            in HepG2 Cells by Alleviating Inflammation and Lipotoxicity Through
            AHR Activation
  JOURNAL   Appl Biochem Biotechnol 195 (11), 6694-6707 (2023)
   PUBMED   36913096
  REMARK    GeneRIF: Knockdown of IL4I1 Improved High Glucose-evoked Insulin
            Resistance in HepG2 Cells by Alleviating Inflammation and
            Lipotoxicity Through AHR Activation.
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Zeitler,L. and Murray,P.J.
  TITLE     IL4i1 and IDO1: Oxidases that control a tryptophan metabolic nexus
            in cancer
  JOURNAL   J Biol Chem 299 (6), 104827 (2023)
   PUBMED   37196768
  REMARK    GeneRIF: IL4i1 and IDO1: Oxidases that control a tryptophan
            metabolic nexus in cancer.
            Review article
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Luo,J.M., Zhang,T.T., He,Y.Y., Luo,H.N., Hong,Y.Q. and Yang,Z.M.
  TITLE     Human Chorionic Gonadotropin-Stimulated Interleukin-4-Induced-1
            (IL4I1) Promotes Human Decidualization via Aryl Hydrocarbon
            Receptor
  JOURNAL   Int J Mol Sci 24 (4), 3163 (2023)
   PUBMED   36834576
  REMARK    GeneRIF: Human Chorionic Gonadotropin-Stimulated
            Interleukin-4-Induced-1 (IL4I1) Promotes Human Decidualization via
            Aryl Hydrocarbon Receptor.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Gatineau,J., Nidercorne,C., Dupont,A., Puiffe,M.L., Cohen,J.L.,
            Molinier-Frenkel,V., Niedergang,F. and Castellano,F.
  TITLE     IL4I1 binds to TMPRSS13 and competes with SARS-CoV-2 spike
  JOURNAL   Front Immunol 13, 982839 (2022)
   PUBMED   36131918
  REMARK    GeneRIF: IL4I1 binds to TMPRSS13 and competes with SARS-CoV-2
            spike.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Wiemann,S., Kolb-Kokocinski,A. and Poustka,A.
  TITLE     Alternative pre-mRNA processing regulates cell-type specific
            expression of the IL4l1 and NUP62 genes
  JOURNAL   BMC Biol 3, 16 (2005)
   PUBMED   16029492
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Copie-Bergman,C., Boulland,M.L., Dehoulle,C., Moller,P.,
            Farcet,J.P., Dyer,M.J., Haioun,C., Romeo,P.H., Gaulard,P. and
            Leroy,K.
  TITLE     Interleukin 4-induced gene 1 is activated in primary mediastinal
            large B-cell lymphoma
  JOURNAL   Blood 101 (7), 2756-2761 (2003)
   PUBMED   12446450
  REMARK    GeneRIF: is activated in primary mediastinal large B-cell lymphoma,
            which might be due to a constitutive activation of a cytokine
            signaling pathway
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Chavan,S.S., Tian,W., Hsueh,K., Jawaheer,D., Gregersen,P.K. and
            Chu,C.C.
  TITLE     Characterization of the human homolog of the IL-4 induced gene-1
            (Fig1)
  JOURNAL   Biochim Biophys Acta 1576 (1-2), 70-80 (2002)
   PUBMED   12031486
  REMARK    GeneRIF: genomic structure, cDNA sequence, chromosome location and
            RNA expression in immune tissues
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF293462.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a secreted L-amino acid oxidase protein
            which primarily catabolizes L-phenylalanine and, to a lesser
            extent, L-arginine. The expression of this gene is induced by the
            cytokine interleukin 4 in B cells. This gene is also expressed in
            macrophages and dendritic cells. This protein may play a role
            immune system escape as it is expressed in tumor-associated
            macrophages and suppresses T-cell responses. This protein also
            contains domains thought to be involved in the binding of flavin
            adenine dinucleotide (FAD) cofactor. Multiple transcript variants
            encoding different isoforms have been found for this gene. Some
            transcripts of this gene share a promoter and exons of the 5' UTR
            with the overlapping NUP62 gene. [provided by RefSeq, Jul 2020].
            
            Transcript Variant: This variant (1) differs in the 5' UTR and
            coding region, compared to variant 2, and is expressed from a
            different promoter. The resulting isoform (1) contains a distinct
            and shorter N-terminus, as compared to isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF293462.1, AY358933.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000391826.7/ ENSP00000375702.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..567
                     /product="L-amino-acid oxidase isoform 1 precursor"
                     /EC_number="1.4.3.2"
                     /EC_number="1.4.3.25"
                     /note="interleukin four induced 1; Fig-1 protein;
                     L-amino-acid oxidase; IL4-induced protein 1"
                     /calculated_mol_wt=60715
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2184
     mat_peptide     22..567
                     /product="L-amino-acid oxidase isoform 1"
                     /calculated_mol_wt=60715
     Region          53..507
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RQ9.1)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RQ9.1)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q96RQ9.1)"
     Region          506..567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RQ9.1)"
     Site            559
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96RQ9.1)"
     CDS             1..567
                     /gene="IL4I1"
                     /gene_synonym="FIG1; hIL4I1; LAAO; LAO"
                     /coded_by="NM_152899.2:76..1779"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12787.1"
                     /db_xref="GeneID:259307"
                     /db_xref="HGNC:HGNC:19094"
                     /db_xref="MIM:609742"
ORIGIN      
        1 maplalhllv lvpillslva sqdwkaersq dpfekcmqdp dyeqllkvvt wglnrtlkpq
       61 rvivvgagva glvaakvlsd aghkvtilea dnriggrift yrdqntgwig elgamrmpss
      121 hrilhklcqg lglnltkftq ydkntwtevh evklrnyvve kvpeklgyal rpqekghspe
      181 diyqmalnqa lkdlkalgcr kamkkferht lleyllgegn lsrpavqllg dvmsedgffy
      241 lsfaealrah sclsdrlqys rivggwdllp rallsslsgl vllnapvvam tqgphdvhvq
      301 ietspparnl kvlkadvvll tasgpavkri tfspplprhm qealrrlhyv patkvflsfr
      361 rpfwreehie gghsntdrps rmifypppre galllasytw sdaaaafagl sreealrlal
      421 ddvaalhgpv vrqlwdgtgv vkrwaedqhs qggfvvqppa lwqtekddwt vpygriyfag
      481 ehtayphgwv etavksalra aikinsrkgp asdtaspegh asdmegqghv hgvasspshd
      541 lakeegshpp vqgqlslqnt thtrtsh
//
LOCUS       NP_060667                681 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 64 isoform a [Homo sapiens].
ACCESSION   NP_060667
VERSION     NP_060667.2
DBSOURCE    REFSEQ: accession NM_018197.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Han,R., Dermawan,J.K., Demicco,E.G., Ferguson,P.C., Griffin,A.M.,
            Swanson,D., Antonescu,C.R. and Dickson,B.C.
  TITLE     ZFP64::NCOA3 gene fusion defines a novel subset of spindle cell
            rhabdomyosarcoma
  JOURNAL   Genes Chromosomes Cancer 61 (11), 645-652 (2022)
   PUBMED   35521817
  REMARK    GeneRIF: ZFP64::NCOA3 gene fusion defines a novel subset of spindle
            cell rhabdomyosarcoma.
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Qiu,G. and Deng,Y.
  TITLE     ZFP64 transcriptionally activates PD-1 and CTLA-4 and plays an
            oncogenic role in esophageal cancer
  JOURNAL   Biochem Biophys Res Commun 622, 72-78 (2022)
   PUBMED   35843097
  REMARK    GeneRIF: ZFP64 transcriptionally activates PD-1 and CTLA-4 and
            plays an oncogenic role in esophageal cancer.
REFERENCE   3  (residues 1 to 681)
  AUTHORS   Jiang,J., Zhang,J., Fu,K. and Zhang,T.
  TITLE     Function and mechanism exploration of zinc finger protein 64 in
            lung adenocarcinoma cell growth and metastasis
  JOURNAL   J Recept Signal Transduct Res 41 (5), 457-465 (2021)
   PUBMED   33054540
  REMARK    GeneRIF: Function and mechanism exploration of zinc finger protein
            64 in lung adenocarcinoma cell growth and metastasis.
REFERENCE   4  (residues 1 to 681)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 681)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 681)
  AUTHORS   Sakamoto,K., Tamamura,Y., Katsube,K. and Yamaguchi,A.
  TITLE     Zfp64 participates in Notch signaling and regulates differentiation
            in mesenchymal cells
  JOURNAL   J Cell Sci 121 (Pt 10), 1613-1623 (2008)
   PUBMED   18430783
REFERENCE   7  (residues 1 to 681)
  AUTHORS   Schymick,J.C., Scholz,S.W., Fung,H.C., Britton,A., Arepalli,S.,
            Gibbs,J.R., Lombardo,F., Matarin,M., Kasperaviciute,D.,
            Hernandez,D.G., Crews,C., Bruijn,L., Rothstein,J., Mora,G.,
            Restagno,G., Chio,A., Singleton,A., Hardy,J. and Traynor,B.J.
  TITLE     Genome-wide genotyping in amyotrophic lateral sclerosis and
            neurologically normal controls: first stage analysis and public
            release of data
  JOURNAL   Lancet Neurol 6 (4), 322-328 (2007)
   PUBMED   17362836
REFERENCE   8  (residues 1 to 681)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   9  (residues 1 to 681)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 681)
  AUTHORS   Mack,H.G., Beck,F. and Bowtell,D.D.
  TITLE     A search for a mammalian homologue of the Drosophila photoreceptor
            development gene glass yields Zfp64, a zinc finger encoding gene
            which maps to the distal end of mouse chromosome 2
  JOURNAL   Gene 185 (1), 11-17 (1997)
   PUBMED   9034307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC041622.1 and AK001744.1.
            
            On Jan 13, 2004 this sequence version replaced NP_060667.1.
            
            Transcript Variant: This variant (1) lacks several exons and
            includes an alternate 3' terminal exon resulting in a novel 3'
            coding region and 3' UTR compared to variant 4. The encoded isoform
            (a) has a longer and distinct C-terminus compared to isoform d.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012759.2, AK001596.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216923.5/ ENSP00000216923.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.2"
     Protein         1..681
                     /product="zinc finger protein 64 isoform a"
                     /note="zinc finger protein 338; zinc finger protein 64
                     homolog"
                     /calculated_mol_wt=74513
     Region          161..186
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          177..197
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(182,184,186,188..189,192..193,196,210,212,216..217,
                     220..221,224,238,240,242,244..245,248..249,252)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          190..211
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          203..226
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          205..225
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <227..311
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          233..253
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          261..281
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          273..>292
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          289..308
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          315..337
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          371..395
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          373..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          427..447
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..681
                     /gene="ZFP64"
                     /gene_synonym="ZNF338"
                     /coded_by="NM_018197.3:144..2189"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13440.1"
                     /db_xref="GeneID:55734"
                     /db_xref="HGNC:HGNC:15940"
                     /db_xref="MIM:618111"
ORIGIN      
        1 mnassegesf agsvqipggt tvlveltpdi hicgickqqf nnldafvahk qsgcqltgts
       61 aaapstvqfv seetvpatqt qtttrtitse tqtitvsape fvfehgyqty lptesnenqt
      121 atvislpaks rtkkpttppa qkrlnccypg cqfktaygmk dmerhlkiht gdkphkcevc
      181 gkcfsrkdkl kthmrchtgv kpykcktcdy aaadssslnk hlrihsderp fkcqicpyas
      241 rnssqltvhl rshtgdapfq cwlcsakfki ssdlkrhmrv hsgekpfkce fcnvrctmkg
      301 nlkshirikh sgnnfkcphc dflgdskatl rkhsrvhqse hpekcsecsy scsskaalri
      361 herihctdrp fkcnycsfdt kqpsnlskhm kkfhgdmvkt ealerkdtgr qssrqvakld
      421 akksfhcdic dasfmredsl rshkrqhsey sesknsdvtv lqfqidpskq patpltvghl
      481 qvplqpsqvp qfsegrvkii vghqvpqant ivqaaaaavn ivppalvaqn peelpgnsrl
      541 qilrqvslia ppqssrcpse agamtqpavl lttheqtdga tlhqtlipta sggpqegsgn
      601 qtfitssgit ctdfeglnal iqegtaevtv vsdggqniav attappvfss ssqqelpkqt
      661 ysiiqgaahp allcpadsip d
//
LOCUS       NP_001001410             312 aa            linear   PRI 27-APR-2025
DEFINITION  18S rRNA aminocarboxypropyltransferase [Homo sapiens].
ACCESSION   NP_001001410
VERSION     NP_001001410.1
DBSOURCE    REFSEQ: accession NM_001001410.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Meyer,B., Wurm,J.P., Sharma,S., Immer,C., Pogoryelov,D., Kotter,P.,
            Lafontaine,D.L., Wohnert,J. and Entian,K.D.
  TITLE     Ribosome biogenesis factor Tsr3 is the aminocarboxypropyl
            transferase responsible for 18S rRNA hypermodification in yeast and
            humans
  JOURNAL   Nucleic Acids Res 44 (9), 4304-4316 (2016)
   PUBMED   27084949
  REMARK    GeneRIF: Structurally, Tsr3 represents a novel class of acp
            transferase enzymes.
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Daniels,R.J., Peden,J.F., Lloyd,C., Horsley,S.W., Clark,K.,
            Tufarelli,C., Kearney,L., Buckle,V.J., Doggett,N.A., Flint,J. and
            Higgs,D.R.
  TITLE     Sequence, structure and pathology of the fully annotated terminal 2
            Mb of the short arm of human chromosome 16
  JOURNAL   Hum Mol Genet 10 (4), 339-352 (2001)
   PUBMED   11157797
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031709.12, BC016699.1 and BC017325.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017325.2, BC013943.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000007390.3/ ENSP00000007390.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..312
                     /product="18S rRNA aminocarboxypropyltransferase"
                     /EC_number="2.5.1.157"
                     /note="probable ribosome biogenesis protein C16orf42;
                     ribosome biogenesis protein TSR3 homolog; TSR3, 20S rRNA
                     accumulation, homolog; TSR3, acp transferase ribosome
                     maturation factor; 20S S rRNA accumulation protein 3
                     homolog"
                     /calculated_mol_wt=33465
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJK0.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5HZH2; propagated from
                     UniProtKB/Swiss-Prot (Q9UJK0.1)"
     Region          60..92
                     /region_name="RLI"
                     /note="Possible Fer4-like domain in RNase L inhibitor,
                     RLI; pfam04068"
                     /db_xref="CDD:427689"
     Region          96..222
                     /region_name="Ribo_biogen_C"
                     /note="Ribosome biogenesis protein, C-terminal; pfam04034"
                     /db_xref="CDD:461139"
     Region          224..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJK0.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UJK0.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UJK0.1)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UJK0.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UJK0.1)"
     CDS             1..312
                     /gene="TSR3"
                     /gene_synonym="C16orf42; HsTsr3"
                     /coded_by="NM_001001410.3:75..1013"
                     /db_xref="CCDS:CCDS10435.1"
                     /db_xref="GeneID:115939"
                     /db_xref="HGNC:HGNC:14175"
                     /db_xref="MIM:617058"
ORIGIN      
        1 mgrrraargp gaeggrprhl ptrsleafae evgaalqasv epgaadgegg pgpaalpctl
       61 amwelghcdp rrctgrklar lglvrclrlg hrfgglvlsp vgkqyaspad rqlvaqsgva
      121 vidcswarld etpfgkmrgs hlrllpylva anpvnygrpy rlscveafaa tfcivgfpdl
      181 avillrkfkw gkgfldlnrq lldkyaacgs peevlqaeqe flanakespq eeeidpfdvd
      241 sgrefgnpnr pvastrlpsd tddsdasedp gpgaerggas sscceeeqtq grgaearapa
      301 evwkgikkrq rd
//
LOCUS       NP_001350305             406 aa            linear   PRI 27-APR-2025
DEFINITION  sugar phosphate exchanger 3 isoform 7 [Homo sapiens].
ACCESSION   NP_001350305 XP_024302741
VERSION     NP_001350305.1
DBSOURCE    REFSEQ: accession NM_001363376.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Yu,Z., Surface,L.E., Park,C.Y., Horlbeck,M.A., Wyant,G.A.,
            Abu-Remaileh,M., Peterson,T.R., Sabatini,D.M., Weissman,J.S. and
            O'Shea,E.K.
  TITLE     Identification of a transporter complex responsible for the
            cytosolic entry of nitrogen-containing bisphosphonates
  JOURNAL   Elife 7, e36620 (2018)
   PUBMED   29745899
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Palmieri,M., Impey,S., Kang,H., di Ronza,A., Pelz,C., Sardiello,M.
            and Ballabio,A.
  TITLE     Characterization of the CLEAR network reveals an integrated control
            of cellular clearance pathways
  JOURNAL   Hum Mol Genet 20 (19), 3852-3866 (2011)
   PUBMED   21752829
  REMARK    GeneRIF: SLC37A3 protein localizes in lysosomes in HeLa cells
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Pan,C.J., Chen,S.Y., Jun,H.S., Lin,S.R., Mansfield,B.C. and
            Chou,J.Y.
  TITLE     SLC37A1 and SLC37A2 are phosphate-linked, glucose-6-phosphate
            antiporters
  JOURNAL   PLoS One 6 (9), e23157 (2011)
   PUBMED   21949678
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Bartoloni,L. and Antonarakis,S.E.
  TITLE     The human sugar-phosphate/phosphate exchanger family SLC37
  JOURNAL   Pflugers Arch 447 (5), 780-783 (2004)
   PUBMED   12811562
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093087.3.
            
            On May 17, 2018 this sequence version replaced XP_024302741.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.68560.1,
                                           SRR1660803.179235.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..406
                     /product="sugar phosphate exchanger 3 isoform 7"
                     /note="sugar phosphate exchanger 3; solute carrier family
                     37 (glycerol-3-phosphate transporter), member 3;
                     sugar-phosphate exchange protein 3"
                     /calculated_mol_wt=44826
     Site            16..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Region          20..388
                     /region_name="MFS_SLC37A3"
                     /note="Solute carrier family 37 member 3 of the Major
                     Facilitator Superfamily of transporters; cd17342"
                     /db_xref="CDD:340900"
     Site            order(34..35,38..39,42,99,155..156,158..160,163,183,
                     186..187,190,211,214..215,218..220,223,251,255,306..307,
                     311,315,339,342..343,346..347,350)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340900"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     Site            177..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCC5.2)"
     CDS             1..406
                     /gene="SLC37A3"
                     /gene_synonym="SPX3"
                     /coded_by="NM_001363376.1:186..1406"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:84255"
                     /db_xref="HGNC:HGNC:20651"
                     /db_xref="MIM:619137"
ORIGIN      
        1 mawpnvfqrg sllsqfshhh vvvflltffs ysllhasrkt fsnvkvsise qwtpsafnts
       61 velpveiwss nhlfpsaeka tlflgtldti flfsyavglf isgivgdrln lrwvlsfgmc
      121 ssalvvfvfg altewlrfyn kwlycclwiv ngllqstgwp cvvavmgnwf gkagrgvvfg
      181 lwsacasvgn ilgaclassv lqygyeysla yaclklvnys fffwlpfyls nnfgwkeaea
      241 dklsiwydvg giiggtlqgf isdvlqkrap vlalslllav gsligysrsp ndksinallm
      301 tvtgffiggp snmissaisa dlgrqeliqr ssealatvtg ivdgsgsiga avgqylvsli
      361 rdklgwmwvf yffilmtsct ivfisplivr eifslvlrrq ahilre
//
LOCUS       NP_005137                800 aa            linear   PRI 27-APR-2025
DEFINITION  U4/U6.U5 tri-snRNP-associated protein 1 [Homo sapiens].
ACCESSION   NP_005137
VERSION     NP_005137.1
DBSOURCE    REFSEQ: accession NM_005146.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Pan,T., Zhou,Q., Miao,K., Zhang,L., Wu,G., Yu,J., Xu,Y., Xiong,W.,
            Li,Y. and Wang,Y.
  TITLE     Suppressing Sart1 to modulate macrophage polarization by
            siRNA-loaded liposomes: a promising therapeutic strategy for
            pulmonary fibrosis
  JOURNAL   Theranostics 11 (3), 1192-1206 (2021)
   PUBMED   33391530
  REMARK    GeneRIF: Suppressing Sart1 to modulate macrophage polarization by
            siRNA-loaded liposomes: a promising therapeutic strategy for
            pulmonary fibrosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 800)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 800)
  AUTHORS   Charenton,C., Wilkinson,M.E. and Nagai,K.
  TITLE     Mechanism of 5' splice site transfer for human spliceosome
            activation
  JOURNAL   Science 364 (6438), 362-367 (2019)
   PUBMED   30975767
REFERENCE   6  (residues 1 to 800)
  AUTHORS   Ishida,H., Komiya,S., Inoue,Y., Yutani,S., Inoue,A. and Itoh,K.
  TITLE     Expression of the SART1 tumor-rejection antigen in human
            osteosarcomas
  JOURNAL   Int J Oncol 17 (1), 29-32 (2000)
   PUBMED   10853014
REFERENCE   7  (residues 1 to 800)
  AUTHORS   Matsunaga,K., Nakao,M., Masuoka,K., Inoue,Y., Gouhara,R.,
            Imaizumi,T., Nishizaka,S. and Itoh,K.
  TITLE     Cytokines required for induction of histocompatibility leukocyte
            antigen-class I-restricted and tumor-specific cytotoxic T
            lymphocytes by a SART1-derived peptide
  JOURNAL   Jpn J Cancer Res 90 (9), 1007-1015 (1999)
   PUBMED   10551332
REFERENCE   8  (residues 1 to 800)
  AUTHORS   Kikuchi,M., Nakao,M., Inoue,Y., Matsunaga,K., Shichijo,S.,
            Yamana,H. and Itoh,K.
  TITLE     Identification of a SART-1-derived peptide capable of inducing
            HLA-A24-restricted and tumor-specific cytotoxic T lymphocytes
  JOURNAL   Int J Cancer 81 (3), 459-466 (1999)
   PUBMED   10209962
REFERENCE   9  (residues 1 to 800)
  AUTHORS   Valenta,R., Natter,S., Seiberler,S., Wichlas,S., Maurer,D.,
            Hess,M., Pavelka,M., Grote,M., Ferreira,F., Szepfalusi,Z.,
            Valent,P. and Stingl,G.
  TITLE     Molecular characterization of an autoallergen, Hom s 1, identified
            by serum IgE from atopic dermatitis patients
  JOURNAL   J Invest Dermatol 111 (6), 1178-1183 (1998)
   PUBMED   9856836
REFERENCE   10 (residues 1 to 800)
  AUTHORS   Shichijo,S., Nakao,M., Imai,Y., Takasu,H., Kawamoto,M., Niiya,F.,
            Yang,D., Toh,Y., Yamana,H. and Itoh,K.
  TITLE     A gene encoding antigenic peptides of human squamous cell carcinoma
            recognized by cytotoxic T lymphocytes
  JOURNAL   J Exp Med 187 (3), 277-288 (1998)
   PUBMED   9449708
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU136920.1, AB006198.1 and
            AP006287.2.
            
            Summary: This gene encodes two proteins, the SART1(800) protein
            expressed in the nucleus of the majority of proliferating cells,
            and the SART1(259) protein expressed in the cytosol of epithelial
            cancers. The SART1(259) protein is translated by the mechanism of
            -1 frameshifting during posttranscriptional regulation; its
            full-length sequence is not published yet. The two encoded proteins
            are thought to be involved in the regulation of proliferation. Both
            proteins have tumor-rejection antigens. The SART1(259) protein
            possesses tumor epitopes capable of inducing HLA-A2402-restricted
            cytotoxic T lymphocytes in cancer patients. This SART1(259) antigen
            may be useful in specific immunotherapy for cancer patients and may
            serve as a paradigmatic tool for the diagnosis and treatment of
            patients with atopy. The SART1(259) protein is found to be
            essential for the recruitment of the tri-snRNP to the
            pre-spliceosome in the spliceosome assembly pathway. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.130432.1,
                                           SRR1660807.226377.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312397.10/ ENSP00000310448.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..800
                     /product="U4/U6.U5 tri-snRNP-associated protein 1"
                     /note="squamous cell carcinoma antigen recognised by T
                     cells; small nuclear ribonucleoprotein 110kDa (U4/U6.U5);
                     U4/U6.U5 tri-snRNP-associated 110 kDa protein; IgE
                     autoantigen; SART1(259) protein; SART1(800) protein;
                     squamous cell carcinoma antigen recognized by T-cells 1;
                     hypoxia associated factor; SART-1; hSnu66; hSART-1; SNU66
                     homolog; SART1, U4/U6.U5 tri-snRNP-associated protein 1"
                     /calculated_mol_wt=90124
     Region          1..120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Region          117..137
                     /region_name="HIND"
                     /note="HIND motif; pfam19252"
                     /db_xref="CDD:466011"
     Region          165..753
                     /region_name="SART-1"
                     /note="SART-1 family; pfam03343"
                     /db_xref="CDD:460888"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z315; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Region          311..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Region          419..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Region          571..604
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            764
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     CDS             1..800
                     /gene="SART1"
                     /gene_synonym="Ara1; HAF; HOMS1; SART1259; SNRNP110;
                     Snu66"
                     /coded_by="NM_005146.5:48..2450"
                     /db_xref="CCDS:CCDS31611.1"
                     /db_xref="GeneID:9092"
                     /db_xref="HGNC:HGNC:10538"
                     /db_xref="MIM:605941"
ORIGIN      
        1 mgsskkhrge keaagttaaa gtggateqpp rhrehkkhkh rsggsggsgg errkrsrerg
       61 gergsgrrga eaearssthg rersqaepse rrvkrekrdd gyeaaasskt ssgdasslsi
      121 eetnklrakl glkplevnai kkeagtkeep vtadvinpma lrqreelrek laaakekrll
      181 nqklgkiktl geddpwlddt aawiersrql qkekdlaekr aklleemdqe fgvstlveee
      241 fgqrrqdlys ardlqgltve haidsfrege tmiltlkdkg vlqeeedvlv nvnlvdkera
      301 eknvelrkkk pdylpyaede svddlaqqkp rsilskydee legerphsfr leqggtadgl
      361 rereleeira klrlqaqsls tvgprlasey ltpeemvtfk ktkrrvkkir kkekevvvra
      421 ddllplgdqt qdgdfgsrlr grgrrrvsev eeekepvpqp lpsddtrven mdisdeeegg
      481 apppgspqvl eedeaelelq kqlekgrrlr qlqqlqqlrd sgekvveivk klesrqrgwe
      541 ededperkga ivfnatsefc rtlgeiptyg lagnreeqee lmdferdeer sanggsesdg
      601 eenigwstvn ldeekqqqdf sassttilde epivnrglaa alllcqnkgl lettvqkvar
      661 vkapnkslps avyciedkma iddkysrree yrgftqdfke kdgykpdvki eyvdetgrkl
      721 tpkeafrqls hrfhgkgsgk mkterrmkkl deeallkkms ssdtplgtva llqekqkaqk
      781 tpyivlsgsg ksmnantitk
//
LOCUS       NP_001073887             979 aa            linear   PRI 27-APR-2025
DEFINITION  disks large-associated protein 3 [Homo sapiens].
ACCESSION   NP_001073887 XP_035601
VERSION     NP_001073887.1
DBSOURCE    REFSEQ: accession NM_001080418.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 979)
  AUTHORS   Kajs,B.L., van Roessel,P.J., Davis,G.L., Williams,L.M.,
            Rodriguez,C.I. and Gunaydin,L.A.
  TITLE     Valence processing alterations in SAPAP3 knockout mice and human
            OCD
  JOURNAL   J Psychiatr Res 151, 657-666 (2022)
   PUBMED   35661523
  REMARK    GeneRIF: Valence processing alterations in SAPAP3 knockout mice and
            human OCD.
REFERENCE   2  (residues 1 to 979)
  AUTHORS   Zhang,Y., Wu,J., Yan,Y., Gu,Y., Ma,Y., Wang,M., Zhang,H., Tao,K.,
            Lu,Y., Yu,W., Jing,W., Wang,X. and Tian,X.
  TITLE     SAPAP3 regulates epileptic seizures involving GluN2A in
            post-synaptic densities
  JOURNAL   Cell Death Dis 13 (5), 437 (2022)
   PUBMED   35513389
  REMARK    GeneRIF: SAPAP3 regulates epileptic seizures involving GluN2A in
            post-synaptic densities.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 979)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 979)
  AUTHORS   Li,J.M., Lu,C.L., Cheng,M.C., Luu,S.U., Hsu,S.H. and Chen,C.H.
  TITLE     Exonic resequencing of the DLGAP3 gene as a candidate gene for
            schizophrenia
  JOURNAL   Psychiatry Res 208 (1), 84-87 (2013)
   PUBMED   23414653
  REMARK    GeneRIF: several rare variants of the DLGAP3 gene were found in
            this study which may be associated with schizophrenia.
REFERENCE   5  (residues 1 to 979)
  AUTHORS   Chua,J.J., Schob,C., Rehbein,M., Gkogkas,C.G., Richter,D. and
            Kindler,S.
  TITLE     Synthesis of two SAPAP3 isoforms from a single mRNA is mediated via
            alternative translational initiation
  JOURNAL   Sci Rep 2, 484 (2012)
   PUBMED   22761992
REFERENCE   6  (residues 1 to 979)
  AUTHORS   Ryu,S., Oh,S., Cho,E.Y., Nam,H.J., Yoo,J.H., Park,T., Joo,Y.H.,
            Kwon,J.S. and Hong,K.S.
  TITLE     Interaction between genetic variants of DLGAP3 and SLC1A1 affecting
            the risk of atypical antipsychotics-induced obsessive-compulsive
            symptoms
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 156B (8), 949-959 (2011)
   PUBMED   21990008
  REMARK    GeneRIF: This study provides suggestive evidence that DLGAP3 and
            its interactive effect with SLC1A1 might be involved in
            susceptibility to developing OC symptoms in schizophrenia patients
            receiving AAP treatment.
REFERENCE   7  (residues 1 to 979)
  AUTHORS   Bienvenu,O.J., Wang,Y., Shugart,Y.Y., Welch,J.M., Grados,M.A.,
            Fyer,A.J., Rauch,S.L., McCracken,J.T., Rasmussen,S.A., Murphy,D.L.,
            Cullen,B., Valle,D., Hoehn-Saric,R., Greenberg,B.D., Pinto,A.,
            Knowles,J.A., Piacentini,J., Pauls,D.L., Liang,K.Y., Willour,V.L.,
            Riddle,M., Samuels,J.F., Feng,G. and Nestadt,G.
  TITLE     Sapap3 and pathological grooming in humans: Results from the OCD
            collaborative genetics study
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 150B (5), 710-720 (2009)
   PUBMED   19051237
  REMARK    GeneRIF: Sapap3 is a promising functional candidate gene for human
            grooming disorder (obsessive compulsive disorder).
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 979)
  AUTHORS   Zuchner,S., Wendland,J.R., Ashley-Koch,A.E., Collins,A.L.,
            Tran-Viet,K.N., Quinn,K., Timpano,K.C., Cuccaro,M.L.,
            Pericak-Vance,M.A., Steffens,D.C., Krishnan,K.R., Feng,G. and
            Murphy,D.L.
  TITLE     Multiple rare SAPAP3 missense variants in trichotillomania and OCD
  JOURNAL   Mol Psychiatry 14 (1), 6-9 (2009)
   PUBMED   19096451
  REMARK    GeneRIF: Multiple rare SAPAP3 missense variants in trichotillomania
            and OCD.
            Review article
REFERENCE   9  (residues 1 to 979)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   10 (residues 1 to 979)
  AUTHORS   Bongiorno-Borbone,L., Kadare,G., Benfenati,F. and Girault,J.A.
  TITLE     FAK and PYK2 interact with SAP90/PSD-95-Associated Protein-3
  JOURNAL   Biochem Biophys Res Commun 337 (2), 641-646 (2005)
   PUBMED   16202977
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114490.2 and AL122010.10.
            
            On Jan 18, 2007 this sequence version replaced XP_035601.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145743,
                              SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373347.6/ ENSP00000362444.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..979
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..979
                     /product="disks large-associated protein 3"
                     /note="PSD-95/SAP90-binding protein 3; DAP-3; discs large
                     homolog associated protein 3; SAP90/PSD-95-associated
                     protein 3"
                     /calculated_mol_wt=105910
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95886.3)"
     Region          52..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95886.3)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (O95886.3)"
     Region          136..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95886.3)"
     Region          182..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95886.3)"
     Region          400..429
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95886.3)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (O95886.3)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (O95886.3)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (O95886.3)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (O95886.3)"
     Region          537..581
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95886.3)"
     Region          628..979
                     /region_name="GKAP"
                     /note="Guanylate-kinase-associated protein (GKAP) protein;
                     pfam03359"
                     /db_xref="CDD:460897"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (O95886.3)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (O95886.3)"
     Region          741..790
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95886.3)"
     Region          908..940
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95886.3)"
     Site            932
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97838; propagated from
                     UniProtKB/Swiss-Prot (O95886.3)"
     Site            935
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97838; propagated from
                     UniProtKB/Swiss-Prot (O95886.3)"
     Site            967
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (O95886.3)"
     CDS             1..979
                     /gene="DLGAP3"
                     /gene_synonym="DAP3; SAPAP3; SPAPA3"
                     /coded_by="NM_001080418.3:335..3274"
                     /db_xref="CCDS:CCDS30670.1"
                     /db_xref="GeneID:58512"
                     /db_xref="HGNC:HGNC:30368"
                     /db_xref="MIM:611413"
ORIGIN      
        1 mrgyhgdrgs hprparfadq qhmdvgpaar apyllgsrea fsteprfcap raglghispe
       61 gplslsegps vgpeggpaga gvgggsstfp rmypgqgpfd tcedcvghpq gkgaprlppt
      121 lldqfekqlp vqqdgfhtlp yqrgpagagp gpapgtgtap eprsespsri rhlvhsvqkl
      181 fakshsleap gkrdyngpka egrggsggds ypgpgsggph tshhhhhhhh hhhhqsrhgk
      241 rskskdrkgd grhqakstgw wssddnldsd sgflaggrpp gepggpfcle gpdgsyrdls
      301 fkgrsggseg rclactgmsm sldgqsvkrs awhtmmvsqg rdgypgagpg kgllgpetka
      361 kartyhylqv pqddwggypt ggkdgeipcr rmrsgsyika mgdeesgdsd gspktspkav
      421 arrfttrrss svdqarincc vpprihprss ipgysrsltt gqlsdelnqq leavcgsvfg
      481 elesqavdal dlpgcfrmrs hsylraiqag csqdddclpl latpaavsgr pgssfnfrka
      541 pppippgsqa pprisitaqs stdsahesft aaegparrcs sadgldgpam gartlelapv
      601 ppraspkppt liiktipgre elrslarqrk wrpsigvqve tisdsdtenr srrefhsigv
      661 qveedkrrar fkrsnsvtag vqadlelegl aglatvated kalqfgrsfq rhasepqpgp
      721 raptysvfrt vhtqgqwayr egyplpyepp atdgspgpap aptpgpgagr rdswiergsr
      781 slpdsgrasp cprdgewfik mlraevekle hwcqqmerea edyelpeeil ekirsavgst
      841 qlllsqkvqq ffrlcqqsmd ptafpvptfq dlagfwdllq lsiedvtlkf lelqqlkans
      901 wkllepkeek kvpppipkkp lrgrgvpvke rsldsvdrqr qearkrllaa kraasfrhss
      961 atesadsiei yipeaqtrl
//
LOCUS       NP_997465                538 aa            linear   PRI 27-APR-2025
DEFINITION  syncytin-2 preproprotein [Homo sapiens].
ACCESSION   NP_997465
VERSION     NP_997465.1
DBSOURCE    REFSEQ: accession NM_207582.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Gruchot,J., Lewen,I., Dietrich,M., Reiche,L., Sindi,M., Hecker,C.,
            Herrero,F., Charvet,B., Weber-Stadlbauer,U., Hartung,H.P.,
            Albrecht,P., Perron,H., Meyer,U. and Kury,P.
  TITLE     Transgenic expression of the HERV-W envelope protein leads to
            polarized glial cell populations and a neurodegenerative
            environment
  JOURNAL   Proc Natl Acad Sci U S A 120 (38), e2308187120 (2023)
   PUBMED   37695891
  REMARK    GeneRIF: Transgenic expression of the HERV-W envelope protein leads
            to polarized glial cell populations and a neurodegenerative
            environment.
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Talotta,R.
  TITLE     Interaction between Long Noncoding RNAs and Syncytin-1/Syncytin-2
            Genes and Transcripts: How Noncoding RNAs May Affect Pregnancy in
            Patients with Systemic Lupus Erythematosus
  JOURNAL   Int J Mol Sci 24 (3), 2259 (2023)
   PUBMED   36768581
  REMARK    GeneRIF: Interaction between Long Noncoding RNAs and
            Syncytin-1/Syncytin-2 Genes and Transcripts: How Noncoding RNAs May
            Affect Pregnancy in Patients with Systemic Lupus Erythematosus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Martinez-Molledo,M., Nji,E. and Reyes,N.
  TITLE     Structural insights into the lysophospholipid brain uptake
            mechanism and its inhibition by syncytin-2
  JOURNAL   Nat Struct Mol Biol 29 (6), 604-612 (2022)
   PUBMED   35710838
  REMARK    GeneRIF: Structural insights into the lysophospholipid brain uptake
            mechanism and its inhibition by syncytin-2.
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Roberts,R.M., Ezashi,T., Schulz,L.C., Sugimoto,J., Schust,D.J.,
            Khan,T. and Zhou,J.
  TITLE     Syncytins expressed in human placental trophoblast
  JOURNAL   Placenta 113, 8-14 (2021)
   PUBMED   33504453
  REMARK    Review article
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Garcia-Montojo,M. and Nath,A.
  TITLE     HERV-W envelope expression in blood leukocytes as a marker of
            disease severity of COVID-19
  JOURNAL   EBioMedicine 67, 103363 (2021)
   PUBMED   33993053
  REMARK    GeneRIF: HERV-W envelope expression in blood leukocytes as a marker
            of disease severity of COVID-19.
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Renard,M., Varela,P.F., Letzelter,C., Duquerroy,S., Rey,F.A. and
            Heidmann,T.
  TITLE     Crystal structure of a pivotal domain of human syncytin-2, a 40
            million years old endogenous retrovirus fusogenic envelope gene
            captured by primates
  JOURNAL   J Mol Biol 352 (5), 1029-1034 (2005)
   PUBMED   16140326
  REMARK    GeneRIF: The crystal structure of a central fragment of syncytin 2
            'fossil' ectodomain is reported, allowing a remarkable
            superposition with the structures of the corresponding domains of
            present-day infectious retroviruses
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Villesen,P., Aagaard,L., Wiuf,C. and Pedersen,F.S.
  TITLE     Identification of endogenous retroviral reading frames in the human
            genome
  JOURNAL   Retrovirology 1, 32 (2004)
   PUBMED   15476554
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Blaise,S., Ruggieri,A., Dewannieux,M., Cosset,F.L. and Heidmann,T.
  TITLE     Identification of an envelope protein from the FRD family of human
            endogenous retroviruses (HERV-FRD) conferring infectivity and
            functional conservation among simians
  JOURNAL   J Virol 78 (2), 1050-1054 (2004)
   PUBMED   14694139
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Blaise,S., de Parseval,N., Benit,L. and Heidmann,T.
  TITLE     Genomewide screening for fusogenic human endogenous retrovirus
            envelopes identifies syncytin 2, a gene conserved on primate
            evolution
  JOURNAL   Proc Natl Acad Sci U S A 100 (22), 13013-13018 (2003)
   PUBMED   14557543
REFERENCE   10 (residues 1 to 538)
  AUTHORS   de Parseval,N., Lazar,V., Casella,J.F., Benit,L. and Heidmann,T.
  TITLE     Survey of human genes of retroviral origin: identification and
            transcriptome of the genes with coding capacity for complete
            envelope proteins
  JOURNAL   J Virol 77 (19), 10414-10422 (2003)
   PUBMED   12970426
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC068585.1 and AL136139.6.
            
            Summary: Many different human endogenous retrovirus (HERV) families
            are expressed in normal placental tissue at high levels, suggesting
            that HERVs are functionally important in reproduction. This gene is
            part of a human endogenous retrovirus provirus on chromosome 6 that
            has inactivating mutations in the gag and pol genes. This gene is
            the envelope glycoprotein gene which appears to have been
            selectively preserved. The gene's protein product plays a major
            role in placental development and trophoblast fusion. The protein
            has the characteristics of a typical retroviral envelope protein,
            including a cleavage site that separates the surface (SU) and
            transmembrane (TM) proteins which form a heterodimer. [provided by
            RefSeq, Jun 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068585.1, AK123938.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            endogenous retrovirus  :: PMID: 14557543
            MANE Ensembl match     :: ENST00000472091.2/ ENSP00000420174.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.2"
     Protein         1..538
                     /product="syncytin-2 preproprotein"
                     /note="HERV-FRD_6p24.1 provirus ancestral Env polyprotein;
                     syncytin 2; HERV-FRD provirus ancestral Env polyprotein;
                     envelope polyprotein; endogenous retrovirus group FRD,
                     member 1"
                     /calculated_mol_wt=57974
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1567
     mat_peptide     16..538
                     /product="Syncytin-2. /id=PRO_0000008439"
                     /note="propagated from UniProtKB/Swiss-Prot (P60508.1)"
                     /calculated_mol_wt=57974
     mat_peptide     16..350
                     /product="Surface protein. /evidence=ECO:0000250.
                     /id=PRO_0000008440"
                     /note="propagated from UniProtKB/Swiss-Prot (P60508.1)"
                     /calculated_mol_wt=37419
     Region          43..46
                     /region_name="CXXC. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P60508.1)"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P60508.1)"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P60508.1)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P60508.1)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P60508.1)"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P60508.1)"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P60508.1)"
     Region          <296..486
                     /region_name="TLV_coat"
                     /note="ENV polyprotein (coat polyprotein); pfam00429"
                     /db_xref="CDD:306850"
     Site            312
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P60508.1)"
     Site            332
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P60508.1)"
     Site            350..351
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250|UniProtKB:Q9UQF0;
                     propagated from UniProtKB/Swiss-Prot (P60508.1)"
     mat_peptide     351..538
                     /product="Transmembrane protein. /evidence=ECO:0000250.
                     /id=PRO_0000008441"
                     /note="propagated from UniProtKB/Swiss-Prot (P60508.1)"
                     /calculated_mol_wt=20573
     Region          354..374
                     /region_name="Fusion peptide. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P60508.1)"
     Region          414..430
                     /region_name="CKS-17. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P60508.1)"
     Region          431..439
                     /region_name="CX6CC. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P60508.1)"
     Site            443
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P60508.1)"
     Site            479..499
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P60508.1)"
     CDS             1..538
                     /gene="ERVFRD-1"
                     /gene_synonym="envFRD; ERVFRDE1; GLLL6191; HERV-FRD;
                     HERV-W/FRD; UNQ6191"
                     /coded_by="NM_207582.3:370..1986"
                     /db_xref="CCDS:CCDS4519.1"
                     /db_xref="GeneID:405754"
                     /db_xref="HGNC:HGNC:33823"
                     /db_xref="MIM:610524"
ORIGIN      
        1 mgllllvlil tpslaayrhp dfpllekaqq llqstgspys tncwlctsss tetpgtaypa
       61 sprewtsiea elhisyrwdp nlkglmrpan sllstvkqdf pdirqkppif gpiftninlm
      121 giapicvmak rkngtnvgtl pstvcnvtft vdsnqqtyqt ythnqfrhqp rfpkppnitf
      181 pqgtlldkss rfcqgrpssc strnfwfrpa dynqclqisn lsstaewvll dqtrnslfwe
      241 nktkganqsq tpcvqvlagm tiatsylgis avseffgtsl tplfhfhist clktqgafyi
      301 cgqsihqclp snwtgtctig yvtpdifiap gnlslpipiy gnsplprvrr aihfipllag
      361 lgilagtgtg iagitkaslt ysqlskeian nidtmakalt tmqeqidsla avvlqnrrgl
      421 dmltaaqggi claldekccf wvnqsgkvqd nirqllnqas slreratqgw lnwegtwkwf
      481 swvlpltgpl vsllllllfg pcllnlitqf vssrlqaikl qtnlsagrhp rniqespf
//
LOCUS       NP_002592                150 aa            linear   PRI 27-APR-2025
DEFINITION  retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase
            subunit delta isoform 1 [Homo sapiens].
ACCESSION   NP_002592
VERSION     NP_002592.1
DBSOURCE    REFSEQ: accession NM_002601.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Faber,S., Letteboer,S.J.F., Junger,K., Butcher,R., Tammana,T.V.S.,
            van Beersum,S.E.C., Ueffing,M., Collin,R.W.J., Liu,Q., Boldt,K. and
            Roepman,R.
  TITLE     PDE6D Mediates Trafficking of Prenylated Proteins NIM1K and UBL3 to
            Primary Cilia
  JOURNAL   Cells 12 (2), 312 (2023)
   PUBMED   36672247
  REMARK    GeneRIF: PDE6D Mediates Trafficking of Prenylated Proteins NIM1K
            and UBL3 to Primary Cilia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Canovas Nunes,S., De Vita,S., Anighoro,A., Autelitano,F.,
            Beaumont,E., Klingbeil,P., McGuinness,M., Duvert,B., Harris,C.,
            Yang,L., Pokharel,S.P., Chen,C.W., Ermann,M., Williams,D.A. and
            Xu,H.
  TITLE     Validation of a small molecule inhibitor of PDE6D-RAS interaction
            with favorable anti-leukemic effects
  JOURNAL   Blood Cancer J 12 (4), 64 (2022)
   PUBMED   35422065
  REMARK    GeneRIF: Validation of a small molecule inhibitor of PDE6D-RAS
            interaction with favorable anti-leukemic effects.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Thomas,S., Wright,K.J., Le Corre,S., Micalizzi,A., Romani,M.,
            Abhyankar,A., Saada,J., Perrault,I., Amiel,J., Litzler,J.,
            Filhol,E., Elkhartoufi,N., Kwong,M., Casanova,J.L., Boddaert,N.,
            Baehr,W., Lyonnet,S., Munnich,A., Burglen,L., Chassaing,N.,
            Encha-Ravazi,F., Vekemans,M., Gleeson,J.G., Valente,E.M.,
            Jackson,P.K., Drummond,I.A., Saunier,S. and Attie-Bitach,T.
  TITLE     A homozygous PDE6D mutation in Joubert syndrome impairs targeting
            of farnesylated INPP5E protein to the primary cilium
  JOURNAL   Hum Mutat 35 (1), 137-146 (2014)
   PUBMED   24166846
  REMARK    GeneRIF: Study identifies PDE6D as a novel Joubert syndrome gene
            and provides the first evidence of prenyl-binding-dependent
            trafficking in ciliopathies.
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Linari,M., Ueffing,M., Manson,F., Wright,A., Meitinger,T. and
            Becker,J.
  TITLE     The retinitis pigmentosa GTPase regulator, RPGR, interacts with the
            delta subunit of rod cyclic GMP phosphodiesterase
  JOURNAL   Proc Natl Acad Sci U S A 96 (4), 1315-1320 (1999)
   PUBMED   9990021
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Marzesco,A.M., Galli,T., Louvard,D. and Zahraoui,A.
  TITLE     The rod cGMP phosphodiesterase delta subunit dissociates the small
            GTPase Rab13 from membranes
  JOURNAL   J Biol Chem 273 (35), 22340-22345 (1998)
   PUBMED   9712853
REFERENCE   6  (residues 1 to 150)
  AUTHORS   Lorenz,B., Migliaccio,C., Lichtner,P., Meyer,C., Strom,T.M.,
            D'Urso,M., Becker,J., Ciccodicola,A. and Meitinger,T.
  TITLE     Cloning and gene structure of the rod cGMP phosphodiesterase delta
            subunit gene (PDED) in man and mouse
  JOURNAL   Eur J Hum Genet 6 (3), 283-290 (1998)
   PUBMED   9781033
REFERENCE   7  (residues 1 to 150)
  AUTHORS   Li,N., Florio,S.K., Pettenati,M.J., Rao,P.N., Beavo,J.A. and
            Baehr,W.
  TITLE     Characterization of human and mouse rod cGMP phosphodiesterase
            delta subunit (PDE6D) and chromosomal localization of the human
            gene
  JOURNAL   Genomics 49 (1), 76-82 (1998)
   PUBMED   9570951
REFERENCE   8  (residues 1 to 150)
  AUTHORS   Ershova,G., Derre,J., Chetelin,S., Nancy,V., Berger,R., Kaplan,J.,
            Munnich,A. and de Gunzburg,J.
  TITLE     cDNA sequence, genomic organization and mapping of PDE6D, the human
            gene encoding the delta subunit of the cGMP phosphodiesterase of
            retinal rod cells to chromosome 2q36
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 139-141 (1997)
   PUBMED   9533031
REFERENCE   9  (residues 1 to 150)
  AUTHORS   Florio,S.K., Prusti,R.K. and Beavo,J.A.
  TITLE     Solubilization of membrane-bound rod phosphodiesterase by the rod
            phosphodiesterase recombinant delta subunit
  JOURNAL   J Biol Chem 271 (39), 24036-24047 (1996)
   PUBMED   8798640
REFERENCE   10 (residues 1 to 150)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY037751.1 and BC007831.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the delta subunit of rod-specific
            photoreceptor phosphodiesterase (PDE), a key enzyme in the
            phototransduction cascade. A similar protein in cow functions in
            solubilizing membrane-bound PDE. In addition to its role in the PDE
            complex, the encoded protein is thought to bind to prenyl groups of
            proteins to target them to subcellular organelles called cilia.
            Mutations in this gene are associated with Joubert syndrome-22.
            Alternative splicing results in multiple splice variants. [provided
            by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001054.2, BP329757.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287600.9/ ENSP00000287600.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..150
                     /product="retinal rod rhodopsin-sensitive cGMP
                     3',5'-cyclic phosphodiesterase subunit delta isoform 1"
                     /EC_number="3.1.4.17"
                     /note="retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic
                     phosphodiesterase subunit delta; protein p17; GMP-PDE
                     delta; phosphodiesterase 6D, cGMP-specific, rod, delta"
                     /calculated_mol_wt=17289
     Region          10..149
                     /region_name="GMP_PDE_delta"
                     /note="GMP-PDE, delta subunit; pfam05351"
                     /db_xref="CDD:428436"
     Region          144..150
                     /region_name="Required for association with membranes.
                     /evidence=ECO:0000269|PubMed:9712853"
                     /note="propagated from UniProtKB/Swiss-Prot (O43924.1)"
     CDS             1..150
                     /gene="PDE6D"
                     /gene_synonym="JBTS22; PDED"
                     /coded_by="NM_002601.4:169..621"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33398.1"
                     /db_xref="GeneID:5147"
                     /db_xref="HGNC:HGNC:8788"
                     /db_xref="MIM:602676"
ORIGIN      
        1 msakderare ilrgfklnwm nlrdaetgki lwqgtedlsv pgvehearvp kkilkckavs
       61 relnfssteq mekfrleqkv yfkgqcleew ffefgfvipn stntwqslie aapesqmmpa
      121 svltgnviie tkffdddllv stsrvrlfyv
//
LOCUS       NP_036474                260 aa            linear   PRI 27-APR-2025
DEFINITION  BMP and activin membrane-bound inhibitor homolog precursor [Homo
            sapiens].
ACCESSION   NP_036474
VERSION     NP_036474.1
DBSOURCE    REFSEQ: accession NM_012342.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Monshizadeh,K., Tajamolian,M., Anbari,F., Mehrjardi,M.Y.V.,
            Kalantar,S.M. and Dehghani,M.
  TITLE     The association of RBX1 and BAMBI gene expression with oocyte
            maturation in PCOS women
  JOURNAL   BMC Med Genomics 17 (1), 24 (2024)
   PUBMED   38238750
  REMARK    GeneRIF: The association of RBX1 and BAMBI gene expression with
            oocyte maturation in PCOS women.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Wang,L., Si,W., Yu,X., Piffko,A., Dou,X., Ding,X., Bugno,J.,
            Yang,K., Wen,C., Zhang,L., Chen,D., Huang,X., Wang,J., Arina,A.,
            Pitroda,S., Chmura,S.J., He,C., Liang,H.L. and Weichselbaum,R.
  TITLE     Epitranscriptional regulation of TGF-beta pseudoreceptor BAMBI by
            m6A/YTHDF2 drives extrinsic radioresistance
  JOURNAL   J Clin Invest 133 (24), e172919 (2023)
   PUBMED   38099498
  REMARK    GeneRIF: Epitranscriptional regulation of TGF-beta pseudoreceptor
            BAMBI by m6A/YTHDF2 drives extrinsic radioresistance.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Ehnert,S., Rinderknecht,H., Liu,C., Voss,M., Konrad,F.M.,
            Eisler,W., Alexander,D., Ngamsri,K.C., Histing,T., Rollmann,M.F.
            and Nussler,A.K.
  TITLE     Increased Levels of BAMBI Inhibit Canonical TGF-beta Signaling in
            Chronic Wound Tissues
  JOURNAL   Cells 12 (16), 2095 (2023)
   PUBMED   37626905
  REMARK    GeneRIF: Increased Levels of BAMBI Inhibit Canonical TGF-beta
            Signaling in Chronic Wound Tissues.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Zhi,Y., Gao,Q., Wang,Z., Dong,Y., Guan,Y., Yuan,J. and Zhang,Z.
  TITLE     Circular RNA circSP5 promotes liver metastasis of colorectal cancer
            via SP5-mediated BAMBI transcription
  JOURNAL   Funct Integr Genomics 23 (3), 275 (2023)
   PUBMED   37596430
  REMARK    GeneRIF: Circular RNA circSP5 promotes liver metastasis of
            colorectal cancer via SP5-mediated BAMBI transcription.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Gao,H., Fan,H. and Xie,H.
  TITLE     The regulatory effect of the YY1/miR-HCC2/BAMBI axis on the
            stemness of liver cancer cells
  JOURNAL   Int J Oncol 62 (5) (2023)
   PUBMED   36999621
  REMARK    GeneRIF: The regulatory effect of the YY1/miR-HCC2/BAMBI axis on
            the stemness of liver cancer cells.
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Sekiya,T., Adachi,S., Kohu,K., Yamada,T., Higuchi,O., Furukawa,Y.,
            Nakamura,Y., Nakamura,T., Tashiro,K., Kuhara,S., Ohwada,S. and
            Akiyama,T.
  TITLE     Identification of BMP and activin membrane-bound inhibitor (BAMBI),
            an inhibitor of transforming growth factor-beta signaling, as a
            target of the beta-catenin pathway in colorectal tumor cells
  JOURNAL   J Biol Chem 279 (8), 6840-6846 (2004)
   PUBMED   14660579
  REMARK    GeneRIF: beta-catenin interferes with transforming growth
            factor-beta-mediated growth arrest by inducing the expression of
            BAMBI
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Degen,W.G., Weterman,M.A., van Groningen,J.J., Cornelissen,I.M.,
            Lemmers,J.P., Agterbos,M.A., Geurts van Kessel,A., Swart,G.W. and
            Bloemers,H.P.
  TITLE     Expression of nma, a novel gene, inversely correlates with the
            metastatic potential of human melanoma cell lines and xenografts
  JOURNAL   Int J Cancer 65 (4), 460-465 (1996)
   PUBMED   8621228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ640107.1, U23070.1 and
            AI680996.1.
            
            Summary: This gene encodes a transmembrane glycoprotein related to
            the type I receptors of the transforming growth factor-beta
            (TGF-beta) family, whose members play important roles in signal
            transduction in many developmental and pathological processes. The
            encoded protein however is a pseudoreceptor, lacking an
            intracellular serine/threonine kinase domain required for
            signaling. Similar proteins in frog, mouse and zebrafish function
            as negative regulators of TGF-beta, which has led to the suggestion
            that the encoded protein may function to limit the signaling range
            of the TGF-beta family during early embryogenesis. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223065.1, U23070.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375533.6/ ENSP00000364683.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..260
                     /product="BMP and activin membrane-bound inhibitor homolog
                     precursor"
                     /note="non-metastatic gene A protein; putative
                     transmembrane protein NMA; BMP and activin membrane-bound
                     inhibitor homolog"
                     /calculated_mol_wt=26086
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3040
     Region          4..111
                     /region_name="BAMBI"
                     /note="BMP and activin membrane-bound inhibitor (BAMBI)
                     N-terminal domain; pfam06211"
                     /db_xref="CDD:283793"
     mat_peptide     21..260
                     /product="BMP and activin membrane-bound inhibitor
                     homolog"
                     /calculated_mol_wt=26698
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13145.1)"
     Region          123..260
                     /region_name="BAMBI_C"
                     /note="BMP and activin membrane-bound inhibitor homolog
                     C-terminus; pfam19337"
                     /db_xref="CDD:437169"
     Site            153..173
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13145.1)"
     CDS             1..260
                     /gene="BAMBI"
                     /gene_synonym="NMA"
                     /coded_by="NM_012342.3:378..1160"
                     /db_xref="CCDS:CCDS7162.1"
                     /db_xref="GeneID:25805"
                     /db_xref="HGNC:HGNC:30251"
                     /db_xref="MIM:604444"
ORIGIN      
        1 mdrhssyifi wlqlelcama vlltkgeirc ycdaahcvat gymckselsa cfsrlldpqn
       61 snsplthgcl dslasttdic qakqarnhsg ttiptlecch edmcnyrglh dvlspprgea
      121 sgqgnryqhd gsrnlitkvq eltsskelwf raaviavpia gglilvllim lalrmlrsen
      181 krlqdqrqqm lsrlhysfhg hhskkgqvak ldlecmvpvs ghenccltcd kmrqadlsnd
      241 kilslvhwgm ysghgklefv
//
LOCUS       NP_001255982             177 aa            linear   PRI 27-APR-2025
DEFINITION  DPY30 domain-containing protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001255982
VERSION     NP_001255982.1
DBSOURCE    REFSEQ: accession NM_001269053.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Li,S., Qiao,Y., Di,Q., Le,X., Zhang,L., Zhang,X., Zhang,C.,
            Cheng,J., Zong,S., Koide,S.S., Miao,S. and Wang,L.
  TITLE     Interaction of SH3P13 and DYDC1 protein: a germ cell component that
            regulates acrosome biogenesis during spermiogenesis
  JOURNAL   Eur J Cell Biol 88 (9), 509-520 (2009)
   PUBMED   19545932
  REMARK    Erratum:[Eur J Cell Biol. 2019 Jan;98(1):51-52. doi:
            10.1016/j.ejcb.2018.11.002. PMID: 30497823]
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Kuhl,A., Melberg,A., Meinl,E., Nurnberg,G., Nurnberg,P.,
            Kehrer-Sawatzki,H. and Jenne,D.E.
  TITLE     Myofibrillar myopathy with arrhythmogenic right ventricular
            cardiomyopathy 7: corroboration and narrowing of the critical
            region on 10q22.3
  JOURNAL   Eur J Hum Genet 16 (3), 367-373 (2008)
   PUBMED   18197198
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359195.24, BI828082.1 and
            BC019250.1.
            
            Summary: This gene encodes a member of a family of proteins that
            contains a DPY30 domain. The encoded protein is involved in
            acrosome formation during spermatid development. This gene locus
            overlaps with a closely related gene on the opposite strand.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 3. Variants 1-4 all encode the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI828082.1, DRR138524.1153727.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372202.6/ ENSP00000361276.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..177
                     /product="DPY30 domain-containing protein 1 isoform a"
                     /note="DPY30 domain-containing protein 1"
                     /calculated_mol_wt=20762
     Region          2..43
                     /region_name="DD_DYDC-like"
                     /note="dimerization/docking (D/D) domain found in the
                     DPY30 domain-containing protein (DYDC)-like family;
                     cd22966"
                     /db_xref="CDD:438535"
     CDS             1..177
                     /gene="DYDC1"
                     /gene_synonym="DPY30D1"
                     /coded_by="NM_001269053.2:54..587"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7366.1"
                     /db_xref="GeneID:143241"
                     /db_xref="HGNC:HGNC:23460"
                     /db_xref="MIM:615154"
ORIGIN      
        1 mesiylqkhl gacltqglae varvrpvdpi eylalwiyky kenvtmeqlr qkemaklere
       61 relalmeqem merlkaeell lqqqqlalql elemqekerq riqelqraqe qlgkemrmnm
      121 enlvrnedil hseeatldsg ktlaeisdry gapnlsrvee ldepmfsdia lnidqdl
//
LOCUS       NP_115679                418 aa            linear   PRI 27-APR-2025
DEFINITION  hydroxysteroid dehydrogenase-like protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_115679
VERSION     NP_115679.2
DBSOURCE    REFSEQ: accession NM_032303.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Wang,D., Yang,S., Lyu,M., Xu,L., Zhong,S. and Yu,D.
  TITLE     Circular RNA HSDL2 promotes breast cancer progression via miR-7978
            ZNF704 axis and regulating hippo signaling pathway
  JOURNAL   Breast Cancer Res 26 (1), 105 (2024)
   PUBMED   38937788
  REMARK    GeneRIF: Circular RNA HSDL2 promotes breast cancer progression via
            miR-7978 ZNF704 axis and regulating hippo signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Samson,N., Bosoi,C.R., Roy,C., Turcotte,L., Tribouillard,L.,
            Mouchiroud,M., Berthiaume,L., Trottier,J., Silva,H.C.G.,
            Guerbette,T., Plata-Gomez,A.B., Besse-Patin,A., Montoni,A.,
            Ilacqua,N., Lamothe,J., Citron,Y.R., Gelinas,Y., Gobeil,S.,
            Zoncu,R., Caron,A., Morissette,M., Pellegrini,L., Rochette,P.J.,
            Estall,J.L., Efeyan,A., Shum,M., Audet-Walsh,E., Barbier,O.,
            Marette,A. and Laplante,M.
  TITLE     HSDL2 links nutritional cues to bile acid and cholesterol
            homeostasis
  JOURNAL   Sci Adv 10 (22), eadk9681 (2024)
   PUBMED   38820148
  REMARK    GeneRIF: HSDL2 links nutritional cues to bile acid and cholesterol
            homeostasis.
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Ma,S., Ma,Y., Qi,F., Lei,J., Chen,F., Sun,W., Wang,D., Zhou,S.,
            Liu,Z., Lu,Z. and Zhang,D.
  TITLE     HSDL2 knockdown promotes the progression of cholangiocarcinoma by
            inhibiting ferroptosis through the P53/SLC7A11 axis
  JOURNAL   World J Surg Oncol 21 (1), 293 (2023)
   PUBMED   37718459
  REMARK    GeneRIF: HSDL2 knockdown promotes the progression of
            cholangiocarcinoma by inhibiting ferroptosis through the
            P53/SLC7A11 axis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Cheng,Y., He,X., Wang,L., Xu,Y., Shen,M., Zhang,W., Xia,Y.,
            Zhang,J., Zhang,M., Wang,Y., Hu,J. and Hu,J.
  TITLE     [HSDL2 overexpression promotes rectal cancer progression by
            regulating cancer cell cycle and promoting cell proliferation]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 43 (4), 544-551 (2023)
   PUBMED   37202189
  REMARK    GeneRIF: [HSDL2 overexpression promotes rectal cancer progression
            by regulating cancer cell cycle and promoting cell proliferation].
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Kowalik,D., Haller,F., Adamski,J. and Moeller,G.
  TITLE     In search for function of two human orphan SDR enzymes:
            hydroxysteroid dehydrogenase like 2 (HSDL2) and short-chain
            dehydrogenase/reductase-orphan (SDR-O)
  JOURNAL   J Steroid Biochem Mol Biol 117 (4-5), 117-124 (2009)
   PUBMED   19703561
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   8  (residues 1 to 418)
  AUTHORS   Skogsberg,J., Lundstrom,J., Kovacs,A., Nilsson,R., Noori,P.,
            Maleki,S., Kohler,M., Hamsten,A., Tegner,J. and Bjorkegren,J.
  TITLE     Transcriptional profiling uncovers a network of
            cholesterol-responsive atherosclerosis target genes
  JOURNAL   PLoS Genet 4 (3), e1000036 (2008)
   PUBMED   18369455
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 418)
  AUTHORS   Edqvist,J. and Blomqvist,K.
  TITLE     Fusion and fission, the evolution of sterol carrier protein-2
  JOURNAL   J Mol Evol 62 (3), 292-306 (2006)
   PUBMED   16501878
REFERENCE   10 (residues 1 to 418)
  AUTHORS   Dai,J., Xie,Y., Wu,Q., Wang,L., Yin,G., Ye,X., Zeng,L., Xu,J.,
            Ji,C., Gu,S., Huang,Q., Zhao,R.C. and Mao,Y.
  TITLE     Molecular cloning and characterization of a novel human
            hydroxysteroid dehydrogenase-like 2 (HSDL2) cDNA from fetal brain
  JOURNAL   Biochem Genet 41 (5-6), 165-174 (2003)
   PUBMED   12834046
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK098721.1, BC095451.1, AY093428.1 and BC004331.1.
            
            On Dec 20, 2003 this sequence version replaced NP_115679.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.236544.1,
                                           SRR1803613.62003.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398805.8/ ENSP00000381785.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..418
                     /product="hydroxysteroid dehydrogenase-like protein 2
                     isoform 1"
                     /note="hydroxysteroid dehydrogenase-like protein 2; short
                     chain dehydrogenase/reductase family 13C member 1"
                     /calculated_mol_wt=45264
     Region          8..248
                     /region_name="HSDL2_SDR_c"
                     /note="human hydroxysteroid dehydrogenase-like protein 2
                     (HSDL2), classical (c) SDRs; cd09762"
                     /db_xref="CDD:187663"
     Site            order(17,19..22,41..43,50,73..75,101..103,124,151,168,172,
                     196,200..201,203..205)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187663"
     Site            order(78,113,115,118..119,122,127,130,134,137,155,157,159,
                     166,170,177..178,180..182,184..185)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187663"
     Site            116
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q2TPA8; propagated from
                     UniProtKB/Swiss-Prot (Q6YN16.1)"
     Site            order(125,153,168,172)
                     /site_type="active"
                     /db_xref="CDD:187663"
     Region          311..414
                     /region_name="SCP2"
                     /note="Putative sterol carrier protein, contains SCP2
                     domain [Lipid transport and metabolism]; COG3255"
                     /db_xref="CDD:442486"
     CDS             1..418
                     /gene="HSDL2"
                     /gene_synonym="C9orf99; SDR13C1"
                     /coded_by="NM_032303.5:57..1313"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43864.1"
                     /db_xref="GeneID:84263"
                     /db_xref="HGNC:HGNC:18572"
ORIGIN      
        1 mlpntgrlag ctvfitgasr gigkaialka akdganivia aktaqphpkl lgtiytaaee
       61 ieavggkalp civdvrdeqq isaavekaik kfggidilvn nasaisltnt ldtptkrldl
      121 mmnvntrgty laskacipyl kkskvahiln ispplnlnpv wfkqhcayti akygmsmyvl
      181 gmaeefkgei avnalwpkta ihtaamdmlg gpgiesqcrk vdiiadaays ifqkpksftg
      241 nfvidenilk eegienfdvy aikpghplqp dffldeypea vskkvestga vpefkeeklq
      301 lqpkprsgav eetfrivkds lsddvvkatq aiylfelsge dggtwfldlk skggnvgyge
      361 psdqadvvms mttddfvkmf sgklkptmaf msgklkikgn malaiklekl mnqmnarl
//
LOCUS       NP_001136116            1700 aa            linear   PRI 27-APR-2025
DEFINITION  A-kinase anchor protein SPHKAP isoform 1 [Homo sapiens].
ACCESSION   NP_001136116
VERSION     NP_001136116.1
DBSOURCE    REFSEQ: accession NM_001142644.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1700)
  AUTHORS   Long,J., Yao,Z., Sui,Y. and Fang,S.
  TITLE     SphK1 Promotes Cancer Progression through Activating JAK/STAT
            Pathway and Up-Regulating S1PR1 Expression in Colon Cancer Cells
  JOURNAL   Anticancer Agents Med Chem 22 (2), 254-260 (2022)
   PUBMED   33797381
  REMARK    GeneRIF: SphK1 Promotes Cancer Progression through Activating
            JAK/STAT Pathway and Up-Regulating S1PR1 Expression in Colon Cancer
            Cells.
REFERENCE   2  (residues 1 to 1700)
  AUTHORS   Ghazaly,E.A., Miraki-Moud,F., Smith,P., Gnanaranjan,C., Koniali,L.,
            Oke,A., Saied,M.H., Petty,R., Matthews,J., Stronge,R., Joel,S.P.,
            Young,B.D., Gribben,J. and Taussig,D.C.
  TITLE     Repression of sphingosine kinase (SK)-interacting protein (SKIP) in
            acute myeloid leukemia diminishes SK activity and its re-expression
            restores SK function
  JOURNAL   J Biol Chem 295 (16), 5496-5508 (2020)
   PUBMED   32161116
  REMARK    GeneRIF: Repression of sphingosine kinase (SK)-interacting protein
            (SKIP) in acute myeloid leukemia diminishes SK activity and its
            re-expression restores SK function.
REFERENCE   3  (residues 1 to 1700)
  AUTHORS   Wade,T.D., Gordon,S., Medland,S., Bulik,C.M., Heath,A.C.,
            Montgomery,G.W. and Martin,N.G.
  TITLE     Genetic variants associated with disordered eating
  JOURNAL   Int J Eat Disord 46 (6), 594-608 (2013)
   PUBMED   23568457
REFERENCE   4  (residues 1 to 1700)
  AUTHORS   Saied,M.H., Marzec,J., Khalid,S., Smith,P., Down,T.A., Rakyan,V.K.,
            Molloy,G., Raghavan,M., Debernardi,S. and Young,B.D.
  TITLE     Genome wide analysis of acute myeloid leukemia reveal leukemia
            specific methylome and subtype specific hypomethylation of repeats
  JOURNAL   PLoS One 7 (3), e33213 (2012)
   PUBMED   22479372
  REMARK    GeneRIF: Results showed that DPP6, SPHKAP and ID4 were down
            regulated in acute myeloid leukemia (AML) patients.
REFERENCE   5  (residues 1 to 1700)
  AUTHORS   Means,C.K., Lygren,B., Langeberg,L.K., Jain,A., Dixon,R.E.,
            Vega,A.L., Gold,M.G., Petrosyan,S., Taylor,S.S., Murphy,A.N.,
            Ha,T., Santana,L.F., Tasken,K. and Scott,J.D.
  TITLE     An entirely specific type I A-kinase anchoring protein that can
            sequester two molecules of protein kinase A at mitochondria
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), E1227-E1235 (2011)
   PUBMED   22084075
  REMARK    GeneRIF: SKIP is an entirely specific type I A-kinase anchoring
            protein that can sequester two molecules of protein kinase A at
            mitochondria.
REFERENCE   6  (residues 1 to 1700)
  AUTHORS   Anelli,V., Gault,C.R., Cheng,A.B. and Obeid,L.M.
  TITLE     Sphingosine kinase 1 is up-regulated during hypoxia in U87MG glioma
            cells. Role of hypoxia-inducible factors 1 and 2
  JOURNAL   J Biol Chem 283 (6), 3365-3375 (2008)
   PUBMED   18055454
  REMARK    GeneRIF: HIF-1 and HIF-2 have roles in SK1 upregulation during
            hypoxia in glioma cells
REFERENCE   7  (residues 1 to 1700)
  AUTHORS   You,B., Ren,A., Yan,G. and Sun,J.
  TITLE     Activation of sphingosine kinase-1 mediates inhibition of vascular
            smooth muscle cell apoptosis by hyperglycemia
  JOURNAL   Diabetes 56 (5), 1445-1453 (2007)
   PUBMED   17325258
  REMARK    GeneRIF: Hyperglycemia stimulates SK1 activity via protein kinase C
            and oxidative stress-dependent pathways, leading to decreased
            apoptosis in vvascular smooth muscle.
REFERENCE   8  (residues 1 to 1700)
  AUTHORS   Jeng,Y.J., Suarez,V.R., Izban,M.G., Wang,H.Q. and Soloff,M.S.
  TITLE     Progesterone-induced sphingosine kinase-1 expression in the rat
            uterus during pregnancy and signaling consequences
  JOURNAL   Am J Physiol Endocrinol Metab 292 (4), E1110-E1121 (2007)
   PUBMED   17164439
  REMARK    GeneRIF: Uterine expression of SphK1 mediates processes involved in
            growth and differentiation of uterine tissues during pregnancy.
REFERENCE   9  (residues 1 to 1700)
  AUTHORS   Yamanaka,M., Shegogue,D., Pei,H., Bu,S., Bielawska,A.,
            Bielawski,J., Pettus,B., Hannun,Y.A., Obeid,L. and Trojanowska,M.
  TITLE     Sphingosine kinase 1 (SPHK1) is induced by transforming growth
            factor-beta and mediates TIMP-1 up-regulation
  JOURNAL   J Biol Chem 279 (52), 53994-54001 (2004)
   PUBMED   15485866
  REMARK    GeneRIF: experiments demonstrate that sphingosine kinase
            1/sphingosine-1-phosphate are important components of the
            transforming growth factor-beta signaling pathway involved in
            up-regulation of the tissue inhibitor of metalloproteinase-1
            (TIMP-1)
REFERENCE   10 (residues 1 to 1700)
  AUTHORS   Lacana,E., Maceyka,M., Milstien,S. and Spiegel,S.
  TITLE     Cloning and characterization of a protein kinase A anchoring
            protein (AKAP)-related protein that interacts with and regulates
            sphingosine kinase 1 activity
  JOURNAL   J Biol Chem 277 (36), 32947-32953 (2002)
   PUBMED   12080051
  REMARK    GeneRIF: cloning and characterization; results indicate that SKIP
            is a novel protein likely to play a regulatory role in the
            modulation of sphingosine kinase type 1 (SPHK1) activity
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC109825.4, BC104956.1, AB051465.1 and AK095042.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC104954.1, SRR1660805.163362.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392056.8/ ENSP00000375909.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1700
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q36.3"
     Protein         1..1700
                     /product="A-kinase anchor protein SPHKAP isoform 1"
                     /note="A-kinase anchor protein SPHKAP; SPHK1 (sphingosine
                     kinase type 1) interacting protein; sphingosine kinase
                     type 1-interacting protein; SPHK1-interactor and AKAP
                     domain-containing protein"
                     /calculated_mol_wt=186326
     Region          364..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Region          742..778
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Region          793..885
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Region          929..946
                     /region_name="PKA-RII subunit binding domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Region          980..1006
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Site            1025
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NSW3; propagated from
                     UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Site            1085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NSW3; propagated from
                     UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Site            1107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NSW3; propagated from
                     UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Site            1120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NSW3; propagated from
                     UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NSW3; propagated from
                     UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Site            1124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NSW3; propagated from
                     UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Site            1259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NSW3; propagated from
                     UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Site            1288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NSW3; propagated from
                     UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Region          1374..1414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Region          1481..1535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Region          1585..1604
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M3C7.1)"
     Region          <1597..1697
                     /region_name="AKAP_110"
                     /note="A-kinase anchor protein 110 kDa (AKAP 110);
                     cl14906"
                     /db_xref="CDD:449376"
     CDS             1..1700
                     /gene="SPHKAP"
                     /gene_synonym="SKIP"
                     /coded_by="NM_001142644.2:90..5192"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46537.1"
                     /db_xref="GeneID:80309"
                     /db_xref="HGNC:HGNC:30619"
                     /db_xref="MIM:611646"
ORIGIN      
        1 mdgnsllsvp snlessrmyd vlepqqgrgc gssgsgpgns itackkvlrs nsllestdyw
       61 lqnqrmpcqi gfvedksenc asvcfvnldv nkdecstehl qqklvnvspd lpklissmnv
      121 qqpkeneivv lsglasgnlq adfevsqcpw lpdiclvqca rgnrpnstnc iifeinkfli
      181 glelvqerql hletnilkle ddtncslssi eedfltaseh leeesevdes rndyeninvs
      241 anvleskqlk gatqvewncn kekwlyaled kyinkyptpl ikterspenl tkntalqsld
      301 psakpsqwkr eavgngrqat hyyhseafkg qmeksqalyi pkdayfsmmd kdvpsacava
      361 eqrsnlnpgd hedtrnalpp rqdgevttgk yatnlaesvl qdafirlsqs qstlpqesav
      421 svsvgssllp scystkdtvv srswnelpki vvvqspdgsd aapqpgissw pemevsvets
      481 silsgenssr qpqsaleval acaatvigti sspqaterlk meqvvsnfpp gssgalqtqa
      541 pqglkepsin eysfpsalcg mtqvasavav cglgereevt csvapsgslp paaeaseamp
      601 plcglasmel gkeaiakgll keaalvltrp ntyssigdfl dsmnrrimet asksqtlcse
      661 nvvrnelaht lsnvilrhsi devhhknmii dpndnrhsse ildtlmestn qllldvicft
      721 fkkmshivrl gecpavlske tirrreteps cqpsdpgasq awtkatesss ssplsnshnt
      781 slvinnlvdg myskqdkggv rpglfknptl qsqlsrshrv pdsstattss keiylkgiag
      841 edtksphhse necrassegq rsptvsqsrs gsqeaeesih pntqekynca tsrinevqvn
      901 lsllgddlll paqstlqtkh pdiycitdfa eeladtvvsm ateiaaicld nssgkqpwfc
      961 awkrgseflm tpnvpcrslk rkkesqgsgt avrkhkpprl seikrktdeh pelkeklmnr
     1021 vvdesmnled vpdsvnlfan evaakimnlt efsmvdgmwq aqgyprnrll sgdrwsrlka
     1081 sscesipeed searayvnsl glmstlsqpv srassvskqs scesitdefs rfmvnqmene
     1141 grgfellldy yagknassil nsamqqacrk sdhlsvrpsc pskqsstesi teefyrymlr
     1201 dierdsresa ssrrssqdwt agllspslrs pvchrqssmp dsrspcsrlt vnvpikansl
     1261 dgfaqncpqd flsvqpvssa sssglcksds clyrrggtdh itnmlihetw assiealmrk
     1321 nkiivddaee adtepvsggs psqaekcanr laasrmcsgp tllvqesldc prkdsvteck
     1381 qppvsslskt asltnhspld skketsscqd pvpinhkrrs lcsrevpliq ietdqreaca
     1441 gepepflsks slleeaeghs ndknipdvvr ggdtavsacq ihsdsldtrd vpeaeastea
     1501 rapdeapnpp ssseestgsw tqlaneednp ddtssflqls ersmsngnss atsslgimdl
     1561 diyqesmpss pminelveek kilkgqsest eapasgpptg taspqrsllv infdlepecp
     1621 daelratlqw iaaselgipt iyfkksqenr iekfldvvql vhrkswkvgd ifhavvqyck
     1681 mheeqkdgrl slfdwllelg
//
LOCUS       NP_849154                146 aa            linear   PRI 27-APR-2025
DEFINITION  MORN repeat-containing protein 4 [Homo sapiens].
ACCESSION   NP_849154
VERSION     NP_849154.1
DBSOURCE    REFSEQ: accession NM_178832.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Mecklenburg,K.L., Freed,S.A., Raval,M., Quintero,O.A., Yengo,C.M.
            and O'Tousa,J.E.
  TITLE     Invertebrate and vertebrate class III myosins interact with MORN
            repeat-containing adaptor proteins
  JOURNAL   PLoS One 10 (3), e0122502 (2015)
   PUBMED   25822849
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Bhattacharya,M.R., Gerdts,J., Naylor,S.A., Royse,E.X.,
            Ebstein,S.Y., Sasaki,Y., Milbrandt,J. and DiAntonio,A.
  TITLE     A model of toxic neuropathy in Drosophila reveals a role for MORN4
            in promoting axonal degeneration
  JOURNAL   J Neurosci 32 (15), 5054-5061 (2012)
   PUBMED   22496551
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Mecklenburg,K.L.
  TITLE     Drosophila retinophilin contains MORN repeats and is conserved in
            humans
  JOURNAL   Mol Genet Genomics 277 (5), 481-489 (2007)
   PUBMED   17285308
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AJ312050.1 and AL834132.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093023.1, SRR1803614.28751.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149178 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307450.11/ ENSP00000307636.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..146
                     /product="MORN repeat-containing protein 4"
                     /note="44050 protein; protein 44050; retinophilin homolog"
                     /calculated_mol_wt=16105
     Region          <5..118
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          16..38
                     /region_name="MORN 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDC4.1)"
     Region          39..61
                     /region_name="MORN 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDC4.1)"
     Region          62..84
                     /region_name="MORN 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDC4.1)"
     Region          85..107
                     /region_name="MORN 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDC4.1)"
     CDS             1..146
                     /gene="MORN4"
                     /gene_synonym="bA548K23.4; C10orf83; rtp; UTA"
                     /coded_by="NM_178832.4:185..625"
                     /db_xref="CCDS:CCDS7468.1"
                     /db_xref="GeneID:118812"
                     /db_xref="HGNC:HGNC:24001"
                     /db_xref="MIM:617736"
ORIGIN      
        1 mtltkgsfty ssgeeyrgew kegrrhgfgq lmfadggtyl ghfenglfng fgvltfsdgs
       61 ryegefaqgk fngvgvfiry dnmtfegefk ngrvdgfgll tfpdgshgip rneglfennk
      121 llrrekcsai vqraqsasks arnlta
//
LOCUS       NP_055875                648 aa            linear   PRI 27-APR-2025
DEFINITION  late secretory pathway protein AVL9 homolog isoform 1 [Homo
            sapiens].
ACCESSION   NP_055875 XP_376589 XP_379801
VERSION     NP_055875.1
DBSOURCE    REFSEQ: accession NM_015060.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Wei,D., Sun,L. and Feng,W.
  TITLE     hsa_circ_0058357 acts as a ceRNA to promote non-small cell lung
            cancer progression via the hsa-miR-24-3p/AVL9 axis
  JOURNAL   Mol Med Rep 23 (6) (2021)
   PUBMED   33880595
  REMARK    GeneRIF: hsa_circ_0058357 acts as a ceRNA to promote nonsmall cell
            lung cancer progression via the hsamiR243p/AVL9 axis.
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Liang,J., Sun,T., Wang,G. and Zhang,H.
  TITLE     Clinical significance and functions of miR-203a-3p/AVL9 axis in
            human non-small-cell lung cancer
  JOURNAL   Per Med 17 (4), 271-282 (2020)
   PUBMED   32678693
  REMARK    GeneRIF: Clinical significance and functions of miR-203a-3p/AVL9
            axis in human non-small-cell lung cancer.
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Linford,A., Yoshimura,S., Nunes Bastos,R., Langemeyer,L.,
            Gerondopoulos,A., Rigden,D.J. and Barr,F.A.
  TITLE     Rab14 and its exchange factor FAM116 link endocytic recycling and
            adherens junction stability in migrating cells
  JOURNAL   Dev Cell 22 (5), 952-966 (2012)
   PUBMED   22595670
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Harsay,E. and Schekman,R.
  TITLE     Avl9p, a member of a novel protein superfamily, functions in the
            late secretory pathway
  JOURNAL   Mol Biol Cell 18 (4), 1203-1219 (2007)
   PUBMED   17229886
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB477229.1, AK090619.1, CN312870.1 and AC018633.2.
            
            On or before Jan 13, 2005 this sequence version replaced
            XP_379801.2, XP_376589.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK090619.1, SRR1163657.367014.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000318709.9/ ENSP00000315568.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..648
                     /product="late secretory pathway protein AVL9 homolog
                     isoform 1"
                     /note="late secretory pathway protein AVL9 homolog; AVL9
                     homolog (S. cerevisiase)"
                     /calculated_mol_wt=71817
     Region          16..520
                     /region_name="Avl9"
                     /note="Transport protein Avl9; pfam09794"
                     /db_xref="CDD:430832"
     Site            214..230
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBF6.1)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80U56; propagated from
                     UniProtKB/Swiss-Prot (Q8NBF6.1)"
     Region          299..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBF6.1)"
     Region          349..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBF6.1)"
     Site            588
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8NBF6.1)"
     CDS             1..648
                     /gene="AVL9"
                     /gene_synonym="KIAA0241"
                     /coded_by="NM_015060.3:222..2168"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34613.1"
                     /db_xref="GeneID:23080"
                     /db_xref="HGNC:HGNC:28994"
                     /db_xref="MIM:612927"
ORIGIN      
        1 mekarrggdg vprgpvlhiv vvgfhhkkgc qvefsyppli pgdghdshtl peewkylpfl
       61 alpdgahnyq edtvffhlpp rngngatvfg iscyrqieak alkvrqadit retvqksvcv
      121 lsklplygll qaklqlitha yfeekdfsqi silkelyehm nsslggasle gsqvylglsp
      181 rdlvlhfrhk vlilfklill ekkvlfyisp vnklvgalmt vlslfpgmie hglsdcsqyr
      241 prksmsedgg lqesnpcadd fvsastadvs htnlgtirkv magnhgedaa mkteeplfqv
      301 edsskgqepn dtnqylkpps rpspdssesd wetldpsvle dpnlkereql gsdqtnlfpk
      361 dsvpseslpi tvqpqantgq vvlipglisg leedqygmpl aiftkgylcl pymalqqhhl
      421 lsdvtvrgfv agatnilfrq qkhlsdaive veealiqihd pelrkllnpt tadlrfadyl
      481 vrhvtenrdd vfldgtgweg gdewiraqfa vyihallaat lqldnekils dygttfvtaw
      541 knthnyrvwn snkhpalaei npnhpfqgqy svsdmklrfs hsvqnsergk kignvmvtts
      601 rnvvqtgkav gqsvggafss aktamsswls tfttstsqsl teppdekp
//
LOCUS       NP_008919                967 aa            linear   PRI 27-APR-2025
DEFINITION  A disintegrin and metalloproteinase with thrombospondin motifs 1
            preproprotein [Homo sapiens].
ACCESSION   NP_008919
VERSION     NP_008919.3
DBSOURCE    REFSEQ: accession NM_006988.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 967)
  AUTHORS   Wen,Y.C., Lin,Y.W., Ho,K.H., Yang,Y.C., Lai,F.R., Chu,C.Y.,
            Chen,J.Q., Lee,W.J. and Chien,M.H.
  TITLE     The oncogenic ADAMTS1-VCAN-EGFR cyclic axis drives anoikis
            resistance and invasion in renal cell carcinoma
  JOURNAL   Cell Mol Biol Lett 29 (1), 126 (2024)
   PUBMED   39333870
  REMARK    GeneRIF: The oncogenic ADAMTS1-VCAN-EGFR cyclic axis drives anoikis
            resistance and invasion in renal cell carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 967)
  AUTHORS   Chien,M.H., Yang,Y.C., Ho,K.H., Ding,Y.F., Chen,L.H., Chiu,W.K.,
            Chen,J.Q., Tung,M.C., Hsiao,M. and Lee,W.J.
  TITLE     Cyclic increase in the ADAMTS1-L1CAM-EGFR axis promotes the EMT and
            cervical lymph node metastasis of oral squamous cell carcinoma
  JOURNAL   Cell Death Dis 15 (1), 82 (2024)
   PUBMED   38263290
  REMARK    GeneRIF: Cyclic increase in the ADAMTS1-L1CAM-EGFR axis promotes
            the EMT and cervical lymph node metastasis of oral squamous cell
            carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 967)
  AUTHORS   Silva,S.V., Lima,M.A., Hodgson,L., Freitas,V.M. and
            Rodriguez-Manzaneque,J.C.
  TITLE     ADAMTS-1 has nuclear localization in cells with epithelial origin
            and leads to decreased cell migration
  JOURNAL   Exp Cell Res 433 (2), 113852 (2023)
   PUBMED   37951335
  REMARK    GeneRIF: ADAMTS-1 has nuclear localization in cells with epithelial
            origin and leads to decreased cell migration.
REFERENCE   4  (residues 1 to 967)
  AUTHORS   Shi,W., Scialdone,A.P., Emerson,J.I., Mei,L., Wasson,L.K.,
            Davies,H.A., Seidman,C.E., Seidman,J.G., Cook,J.G. and Conlon,F.L.
  TITLE     Missense Mutation in Human CHD4 Causes Ventricular Noncompaction by
            Repressing ADAMTS1
  JOURNAL   Circ Res 133 (1), 48-67 (2023)
   PUBMED   37254794
  REMARK    GeneRIF: Missense Mutation in Human CHD4 Causes Ventricular
            Noncompaction by Repressing ADAMTS1.
REFERENCE   5  (residues 1 to 967)
  AUTHORS   Wang,S., Zhang,J., Wang,K., Zhao,Y. and Liu,D.
  TITLE     ADAMTS1 as potential prognostic biomarker promotes malignant
            invasion of glioma
  JOURNAL   Int J Clin Oncol 28 (1), 52-68 (2023)
   PUBMED   36371587
  REMARK    GeneRIF: ADAMTS1 as potential prognostic biomarker promotes
            malignant invasion of glioma.
REFERENCE   6  (residues 1 to 967)
  AUTHORS   Vazquez,F., Hastings,G., Ortega,M.A., Lane,T.F., Oikemus,S.,
            Lombardo,M. and Iruela-Arispe,M.L.
  TITLE     METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a
            new family of proteins with angio-inhibitory activity
  JOURNAL   J Biol Chem 274 (33), 23349-23357 (1999)
   PUBMED   10438512
REFERENCE   7  (residues 1 to 967)
  AUTHORS   Kuno,K., Terashima,Y. and Matsushima,K.
  TITLE     ADAMTS-1 is an active metalloproteinase associated with the
            extracellular matrix
  JOURNAL   J Biol Chem 274 (26), 18821-18826 (1999)
   PUBMED   10373500
REFERENCE   8  (residues 1 to 967)
  AUTHORS   Tang,B.L. and Hong,W.
  TITLE     ADAMTS: a novel family of proteases with an ADAM protease domain
            and thrombospondin 1 repeats
  JOURNAL   FEBS Lett 445 (2-3), 223-225 (1999)
   PUBMED   10094461
  REMARK    Review article
REFERENCE   9  (residues 1 to 967)
  AUTHORS   Kuno,K. and Matsushima,K.
  TITLE     ADAMTS-1 protein anchors at the extracellular matrix through the
            thrombospondin type I motifs and its spacing region
  JOURNAL   J Biol Chem 273 (22), 13912-13917 (1998)
   PUBMED   9593739
REFERENCE   10 (residues 1 to 967)
  AUTHORS   Kuno,K., Kanada,N., Nakashima,E., Fujiki,F., Ichimura,F. and
            Matsushima,K.
  TITLE     Molecular cloning of a gene encoding a new type of
            metalloproteinase-disintegrin family protein with thrombospondin
            motifs as an inflammation associated gene
  JOURNAL   J Biol Chem 272 (1), 556-562 (1997)
   PUBMED   8995297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314475.1, AF207664.1 and
            AP001599.1.
            
            On Jul 30, 2004 this sequence version replaced NP_008919.2.
            
            Summary: This gene encodes a member of the ADAMTS (a disintegrin
            and metalloproteinase with thrombospondin motif) protein family.
            Members of the family share several distinct protein modules,
            including a propeptide region, a metalloproteinase domain, a
            disintegrin-like domain, and a thrombospondin type 1 (TS) motif.
            Individual members of this family differ in the number of
            C-terminal TS motifs, and some have unique C-terminal domains. The
            protein encoded by this gene contains two disintegrin loops and
            three C-terminal TS motifs and has anti-angiogenic activity. The
            expression of this gene may be associated with various inflammatory
            processes as well as development of cancer cachexia. This gene is
            likely to be necessary for normal growth, fertility, and organ
            morphology and function. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036515.2, SRR1803617.273049.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2155371
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000284984.8/ ENSP00000284984.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..967
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 1 preproprotein"
                     /note="a disintegrin-like and metalloprotease (reprolysin
                     type) with thrombospondin type 1 motif, 1; human
                     metalloproteinase with thrombospondin type 1 motifs;
                     metalloprotease and thrombospondin-1; a disintegrin and
                     metalloproteinase with thrombospondin motifs 1; METH-1;
                     ADAM-TS1; ADAMTS-1; ADAM-TS 1"
                     /calculated_mol_wt=100323
     sig_peptide     1..49
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI8.4)"
                     /calculated_mol_wt=5053
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI8.4)"
     Region          59..166
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          192..250
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI8.4)"
     Region          196..203
                     /region_name="Cysteine switch. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI8.4)"
     mat_peptide     253..967
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 1. /id=PRO_0000029151"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI8.4)"
                     /calculated_mol_wt=78640
     Region          258..463
                     /region_name="ZnMc_ADAMTS_like"
                     /note="Zinc-dependent metalloprotease, ADAMTS_like
                     subgroup. ADAMs (A Disintegrin And Metalloprotease) are
                     glycoproteins, which play roles in cell signaling, cell
                     fusion, and cell-cell interactions. This particular
                     subfamily represents domain architectures that...;
                     cd04273"
                     /db_xref="CDD:239801"
     Site            order(401..402,405,411)
                     /site_type="active"
                     /db_xref="CDD:239801"
     Region          478..546
                     /region_name="ADAMTS_CR_2"
                     /note="ADAMTS cysteine-rich domain 2; pfam17771"
                     /db_xref="CDD:465496"
     Site            547
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI8.4)"
     Region          562..614
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          <658..724
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Site            720
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI8.4)"
     Region          725..849
                     /region_name="Spacer"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI8.4)"
     Region          726..842
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Site            764
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI8.4)"
     Region          858..909
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          912..>954
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     CDS             1..967
                     /gene="ADAMTS1"
                     /gene_synonym="C3-C5; METH1"
                     /coded_by="NM_006988.5:456..3359"
                     /db_xref="CCDS:CCDS33524.1"
                     /db_xref="GeneID:9510"
                     /db_xref="HGNC:HGNC:217"
                     /db_xref="MIM:605174"
ORIGIN      
        1 mqravpegfg rrklgsdmgn aerapgsrsf gpvptlllla aallavsdal grpseedeel
       61 vvpelerapg hgttrlrlha fdqqldlelr pdssflapgf tlqnvgrksg setplpetdl
      121 ahcfysgtvn gdpssaaals lcegvrgafy llgeayfiqp lpaaserlat aapgekppap
      181 lqfhllrrnr qgdvggtcgv vddeprptgk aetededegt egedegaqws pqdpalqgvg
      241 qptgtgsirk krfvsshryv etmlvadqsm aefhgsglkh ylltlfsvaa rlykhpsirn
      301 svslvvvkil vihdeqkgpe vtsnaaltlr nfcnwqkqhn ppsdrdaehy dtailftrqd
      361 lcgsqtcdtl gmadvgtvcd psrscsvied dglqaaftta helghvfnmp hddakqcasl
      421 ngvnqdshmm asmlsnldhs qpwspcsaym itsfldnghg eclmdkpqnp iqlpgdlpgt
      481 sydanrqcqf tfgedskhcp daastcstlw ctgtsggvlv cqtkhfpwad gtscgegkwc
      541 ingkcvnktd rkhfdtpfhg swgmwgpwgd csrtcgggvq ytmrecdnpv pknggkyceg
      601 krvryrscnl edcpdnngkt freeqceahn efskasfgsg pavewipkya gvspkdrckl
      661 icqakgigyf fvlqpkvvdg tpcspdstsv cvqgqcvkag cdriidskkk fdkcgvcggn
      721 gstckkisgs vtsakpgyhd iitiptgatn ievkqrnqrg srnngsflai kaadgtyiln
      781 gdytlstleq dimykgvvlr ysgssaaler irsfsplkep ltiqvltvgn alrpkikyty
      841 fvkkkkesfn aiptfsawvi eewgecsksc elgwqrrlve crdingqpas ecakevkpas
      901 trpcadhpcp qwqlgewssc sktcgkgykk rslkclshdg gvlshescdp lkkpkhfidf
      961 ctmaecs
//
LOCUS       NP_004747                609 aa            linear   PRI 27-APR-2025
DEFINITION  numb-like protein isoform a [Homo sapiens].
ACCESSION   NP_004747
VERSION     NP_004747.1
DBSOURCE    REFSEQ: accession NM_004756.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Xin,Y., Shang,X., Sun,X., Xu,G., Liu,Y. and Liu,Y.
  TITLE     SLC8A1 antisense RNA 1 suppresses papillary thyroid cancer
            malignant progression via the FUS RNA binding protein (FUS)/NUMB
            like endocytic adaptor protein (Numbl) axis
  JOURNAL   Bioengineered 13 (5), 12572-12582 (2022)
   PUBMED   35599603
  REMARK    GeneRIF: SLC8A1 antisense RNA 1 suppresses papillary thyroid cancer
            malignant progression via the FUS RNA binding protein (FUS)/NUMB
            like endocytic adaptor protein (Numbl) axis.
REFERENCE   3  (residues 1 to 609)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 609)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 609)
  AUTHORS   Hirai,M., Arita,Y., McGlade,C.J., Lee,K.F., Chen,J. and Evans,S.M.
  TITLE     Adaptor proteins NUMB and NUMBL promote cell cycle withdrawal by
            targeting ERBB2 for degradation
  JOURNAL   J Clin Invest 127 (2), 569-582 (2017)
   PUBMED   28067668
  REMARK    GeneRIF: investigations revealed that NUMB and NUMBL interacted
            with small GTPase Rab7 to transition ERBB2 from early to late
            endosome for degradation.
REFERENCE   6  (residues 1 to 609)
  AUTHORS   Salcini,A.E., Confalonieri,S., Doria,M., Santolini,E., Tassi,E.,
            Minenkova,O., Cesareni,G., Pelicci,P.G. and Di Fiore,P.P.
  TITLE     Binding specificity and in vivo targets of the EH domain, a novel
            protein-protein interaction module
  JOURNAL   Genes Dev 11 (17), 2239-2249 (1997)
   PUBMED   9303539
REFERENCE   7  (residues 1 to 609)
  AUTHORS   Margolis,R.L., Abraham,M.R., Gatchell,S.B., Li,S.H., Kidwai,A.S.,
            Breschel,T.S., Stine,O.C., Callahan,C., McInnis,M.G. and Ross,C.A.
  TITLE     cDNAs with long CAG trinucleotide repeats from human brain
  JOURNAL   Hum Genet 100 (1), 114-122 (1997)
   PUBMED   9225980
REFERENCE   8  (residues 1 to 609)
  AUTHORS   Zhong,W., Jiang,M.M., Weinmaster,G., Jan,L.Y. and Jan,Y.N.
  TITLE     Differential expression of mammalian Numb, Numblike and Notch1
            suggests distinct roles during mouse cortical neurogenesis
  JOURNAL   Development 124 (10), 1887-1897 (1997)
   PUBMED   9169836
REFERENCE   9  (residues 1 to 609)
  AUTHORS   Zhong,W., Feder,J.N., Jiang,M.M., Jan,L.Y. and Jan,Y.N.
  TITLE     Asymmetric localization of a mammalian numb homolog during mouse
            cortical neurogenesis
  JOURNAL   Neuron 17 (1), 43-53 (1996)
   PUBMED   8755477
REFERENCE   10 (residues 1 to 609)
  AUTHORS   Wong,W.T., Schumacher,C., Salcini,A.E., Romano,A., Castagnino,P.,
            Pelicci,P.G. and Di Fiore,P.P.
  TITLE     A protein-binding domain, EH, identified in the receptor tyrosine
            kinase substrate Eps15 and conserved in evolution
  JOURNAL   Proc Natl Acad Sci U S A 92 (21), 9530-9534 (1995)
   PUBMED   7568168
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010412.9 and AK289398.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF015041.2, SRR3476690.920880.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252891.8/ ENSP00000252891.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..609
                     /product="numb-like protein isoform a"
                     /note="numb homolog-like; numb-like protein; numb-related
                     protein"
                     /calculated_mol_wt=64761
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6R0.1)"
     Region          64..198
                     /region_name="PTB_Numb"
                     /note="Numb Phosphotyrosine-binding (PTB) domain; cd01268"
                     /db_xref="CDD:241298"
     Site            order(83,155,175)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:241298"
     Site            order(96,146..149,185,189,192,196)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:241298"
     Region          223..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6R0.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6R0.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6R0.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6R0.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6R0.1)"
     Region          287..371
                     /region_name="NumbF"
                     /note="NUMB domain; pfam06311"
                     /db_xref="CDD:461874"
     Region          372..421
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6R0.1)"
     Region          <394..584
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08919; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6R0.1)"
     Region          434..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6R0.1)"
     Region          537..609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6R0.1)"
     CDS             1..609
                     /gene="NUMBL"
                     /gene_synonym="CAG3A; CTG3a; NBL; NUMB-R; NUMBLIKE; NUMBR;
                     TNRC23"
                     /coded_by="NM_004756.5:169..1998"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12561.1"
                     /db_xref="GeneID:9253"
                     /db_xref="HGNC:HGNC:8061"
                     /db_xref="MIM:604018"
ORIGIN      
        1 msrsaaasgg prrperhlpp apcgapgppe tcrtepdgag tmnklrqslr rrkpayvpea
       61 srphqwqade davrkgtcsf pvrylghvev eesrgmhvce davkklkamg rksvksvlwv
      121 sadglrvvdd ktkdllvdqt iekvsfcapd rnldkafsyi crdgttrrwi chcflalkds
      181 gerlshavgc afaaclerkq rrekecgvta afdasrtsfa regsfrlsgg grpaereapd
      241 kkkaeaaaap tvapgpaqpg hvsptpatts pgekgeagtp vaagttaaai prrhapleql
      301 vrqgsfrgfp alsqknspfk rqlslrlnel pstlqrrtdf qvkgtvpeme ppgagdsdsi
      361 nalctqisss fasagapapg pppattgtsa wgepsvppaa afqpghkrtp seaerwleev
      421 sqvakaqqqq qqqqqqqqqq qqqqqqaasv apvptmppal qpfpapvgpf daapaqvavf
      481 lppphmqppf vpaypglgyp pmprvpvvgi tpsqmvanaf csaaqlqpqp atllgkagaf
      541 pppaipsapg sqarprpnga pwppepapap apeldpfeaq waalegkatv ekpsnpfsgd
      601 lqktfeiel
//
LOCUS       NP_001230679             236 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial coenzyme A diphosphatase NUDT8 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001230679
VERSION     NP_001230679.1
DBSOURCE    REFSEQ: accession NM_001243750.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Gasmi,L. and McLennan,A.G.
  TITLE     The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific
            for coenzyme A and its derivatives
  JOURNAL   Biochem J 357 (Pt 1), 33-38 (2001)
   PUBMED   11415433
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB140633.1, AK123561.1 and AP003385.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.549547.1,
                                           SRR1163658.22651.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376693.3/ ENSP00000365883.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..236
                     /product="mitochondrial coenzyme A diphosphatase NUDT8
                     isoform 1"
                     /EC_number="3.6.1.77"
                     /note="nucleoside diphosphate-linked moiety X motif 8,
                     mitochondrial; nudix motif 8; nudix (nucleoside
                     diphosphate linked moiety X)-type motif 8; mitochondrial
                     coenzyme A diphosphatase NUDT8"
                     /calculated_mol_wt=25239
     Region          32..186
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
     Region          70..91
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV74.2)"
     CDS             1..236
                     /gene="NUDT8"
                     /coded_by="NM_001243750.2:27..737"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS58151.1"
                     /db_xref="GeneID:254552"
                     /db_xref="HGNC:HGNC:8055"
ORIGIN      
        1 mlpdclsaeg elrcrrllag atarlrarpa saavlvplcs vrgvpallyt lrssrltgrh
       61 kgdvsfpggk cdpadqdvvh talretreel glavpeehvw gllrpvydpq katvvpvlag
      121 vgpldpqslr pnseevdevf alplahllqt qnqgythfcr gghfrytlpv flhgphrvwg
      181 ltavitefal qllapgtyqp rlagltcsga eglarpkqpl aspcqasstp glnkgl
//
LOCUS       NP_006011                389 aa            linear   PRI 27-APR-2025
DEFINITION  nucleic acid dioxygenase ALKBH1 [Homo sapiens].
ACCESSION   NP_006011
VERSION     NP_006011.2
DBSOURCE    REFSEQ: accession NM_006020.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Guo,C., Liu,Z. and Zhang,H.
  TITLE     DNA 6mA demethylase ALKBH1 regulates DDX18 expression to promote
            proliferation of human head and neck squamous cell carcinoma
  JOURNAL   Cell Oncol (Dordr) 46 (4), 1097-1111 (2023)
   PUBMED   36976498
  REMARK    GeneRIF: DNA 6mA demethylase ALKBH1 regulates DDX18 expression to
            promote proliferation of human head and neck squamous cell
            carcinoma.
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Li,L., Zhu,C., Xu,Q., Xu,S., Ye,J., Xu,D., Wang,L., Gan,S., Liu,B.
            and Tang,C.
  TITLE     ALKBH1 contributes to renal cell carcinoma progression by reducing
            N6-methyladenine of GPR137
  JOURNAL   Eur J Clin Invest 53 (7), e13986 (2023)
   PUBMED   36920340
  REMARK    GeneRIF: ALKBH1 contributes to renal cell carcinoma progression by
            reducing N6-methyladenine of GPR137.
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Verhoeff,K., Cuesta-Gomez,N., Albers,P., Pawlick,R.,
            Marfil-Garza,B.A., Jasra,I., Dadheech,N., O'Gorman,D., Kin,T.,
            Halpin,A., West,L.J. and Shapiro,A.M.J.
  TITLE     Evaluating the Potential for ABO-incompatible Islet
            Transplantation: Expression of ABH Antigens on Human Pancreata,
            Isolated Islets, and Embryonic Stem Cell-derived Islets
  JOURNAL   Transplantation 107 (4), e98-e108 (2023)
   PUBMED   36228319
  REMARK    GeneRIF: Evaluating the Potential for ABO-incompatible Islet
            Transplantation: Expression of ABH Antigens on Human Pancreata,
            Isolated Islets, and Embryonic Stem Cell-derived Islets.
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Wang,X., Wong,C.C., Chen,H., Fu,K., Shi,L., Su,H., Guo,S., Gou,H.,
            Hu,X., Zhang,L., Ji,J. and Yu,J.
  TITLE     The N6-methyladenine DNA demethylase ALKBH1 promotes gastric
            carcinogenesis by disrupting NRF1 binding capacity
  JOURNAL   Cell Rep 42 (3), 112279 (2023)
   PUBMED   36989111
  REMARK    GeneRIF: The N[6]-methyladenine DNA demethylase ALKBH1 promotes
            gastric carcinogenesis by disrupting NRF1 binding capacity.
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Liu,Y., Chen,Y., Wang,Y., Jiang,S., Lin,W., Wu,Y., Li,Q., Guo,Y.,
            Liu,W. and Yuan,Q.
  TITLE     DNA demethylase ALKBH1 promotes adipogenic differentiation via
            regulation of HIF-1 signaling
  JOURNAL   J Biol Chem 298 (1), 101499 (2022)
   PUBMED   34922943
  REMARK    GeneRIF: DNA demethylase ALKBH1 promotes adipogenic differentiation
            via regulation of HIF-1 signaling.
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Muller,T.A., Meek,K. and Hausinger,R.P.
  TITLE     Human AlkB homologue 1 (ABH1) exhibits DNA lyase activity at abasic
            sites
  JOURNAL   DNA Repair (Amst) 9 (1), 58-65 (2010)
   PUBMED   19959401
  REMARK    GeneRIF: show that ABH1 unexpectedly has a second activity,
            cleaving DNA at abasic (AP) sites such as those arising
            spontaneously from alkylation-dependent depurination reactions.
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Westbye,M.P., Feyzi,E., Aas,P.A., Vagbo,C.B., Talstad,V.A.,
            Kavli,B., Hagen,L., Sundheim,O., Akbari,M., Liabakk,N.B.,
            Slupphaug,G., Otterlei,M. and Krokan,H.E.
  TITLE     Human AlkB homolog 1 is a mitochondrial protein that demethylates
            3-methylcytosine in DNA and RNA
  JOURNAL   J Biol Chem 283 (36), 25046-25056 (2008)
   PUBMED   18603530
  REMARK    GeneRIF: hABH1 is a functional mitochondrial AlkB homolog that
            repairs 3-methylcytosine in single-stranded DNA and RNA.
REFERENCE   8  (residues 1 to 389)
  AUTHORS   Aas,P.A., Otterlei,M., Falnes,P.O., Vagbo,C.B., Skorpen,F.,
            Akbari,M., Sundheim,O., Bjoras,M., Slupphaug,G., Seeberg,E. and
            Krokan,H.E.
  TITLE     Human and bacterial oxidative demethylases repair alkylation damage
            in both RNA and DNA
  JOURNAL   Nature 421 (6925), 859-863 (2003)
   PUBMED   12594517
  REMARK    GeneRIF: AlkB homologues, hABH2 and hABH3, also are oxidative DNA
            demethylases; AlkB and hABH3, but not hABH2, also repair RNA
REFERENCE   9  (residues 1 to 389)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
REFERENCE   10 (residues 1 to 389)
  AUTHORS   Wei,Y.F., Carter,K.C., Wang,R.P. and Shell,B.K.
  TITLE     Molecular cloning and functional analysis of a human cDNA encoding
            an Escherichia coli AlkB homolog, a protein involved in DNA
            alkylation damage repair
  JOURNAL   Nucleic Acids Res 24 (5), 931-937 (1996)
   PUBMED   8600462
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008044.4, BC025787.1 and
            BC015024.1.
            
            On Feb 15, 2006 this sequence version replaced NP_006011.1.
            
            Summary: This gene encodes a homolog to the E. coli alkB gene
            product. The E. coli alkB protein is part of the adaptive response
            mechanism of DNA alkylation damage repair. It is involved in damage
            reversal by oxidative demethylation of 1-methyladenine and
            3-methylcytosine. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.180648.1,
                                           SRR1660805.27277.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMN03267755
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216489.8/ ENSP00000216489.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..389
                     /product="nucleic acid dioxygenase ALKBH1"
                     /EC_number="4.2.99.18"
                     /EC_number="1.14.11.33"
                     /EC_number="1.14.11.51"
                     /note="alkylated DNA repair protein alkB homolog 1;
                     alkylation repair, alkB homolog; DNA lyase ABH1;
                     alpha-ketoglutarate-dependent dioxygenase ABH1; DNA
                     oxidative demethylase ALKBH1; alkB, alkylation repair
                     homolog 1; DNA 6mA demethylase; DNA demethylase ALKBH1;
                     tRNA N1-methyl adenine demethylase; mRNA
                     N(3)-methylcytidine demethylase; DNA N6-methyl adenine
                     demethylase ALKBH1"
                     /calculated_mol_wt=43701
     Region          86..389
                     /region_name="tRNA-binding.
                     /evidence=ECO:0000305|PubMed:27745969"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13686.2)"
     Region          119..289
                     /region_name="alkb"
                     /note="DNA alkylation damage repair protein AlkB;
                     TIGR00568"
                     /db_xref="CDD:129659"
     Site            133
                     /site_type="other"
                     /note="Primary catalytic residue forming the imine linkage
                     with DNA. /evidence=ECO:0000269|PubMed:23577621; Secondary
                     catalytic residue forming the imine linkage with DNA.
                     /evidence=ECO:0000269|PubMed:23577621; propagated from
                     UniProtKB/Swiss-Prot (Q13686.2)"
     CDS             1..389
                     /gene="ALKBH1"
                     /gene_synonym="ABH; ABH1; alkB; ALKBH; hABH"
                     /coded_by="NM_006020.3:20..1189"
                     /db_xref="CCDS:CCDS32127.1"
                     /db_xref="GeneID:8846"
                     /db_xref="HGNC:HGNC:17911"
                     /db_xref="MIM:605345"
ORIGIN      
        1 mgkmaaavgs vatlatepge dafrklfrfy rqsrpgtadl egvidfsaah aargkgpgaq
       61 kviksqlnvs svseqnayra glqpvskwqa yglkgypgfi fipnpflpgy qwhwvkqclk
      121 lysqkpnvcn ldkhmskeet qdlweqskef lrykeatkrr prslleklrw vtvgyhynwd
      181 skkysadhyt pfpsdlgfls eqvaaacgfe dfraeagiln yyrldstlgi hvdrseldhs
      241 kpllsfsfgq saifllgglq rdeaptamfm hsgdimimsg fsrllnhavp rvlpnpegeg
      301 lphcleaplp avlprdsmve pcsmedwqvc asylktarvn mtvrqvlatd qnfplepied
      361 ekrdistegf chlddqnsev krarinpds
//
LOCUS       NP_073604                325 aa            linear   PRI 27-APR-2025
DEFINITION  apoptosis-enhancing nuclease [Homo sapiens].
ACCESSION   NP_073604
VERSION     NP_073604.3
DBSOURCE    REFSEQ: accession NM_022767.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Eby,K.G., Rosenbluth,J.M., Mays,D.J., Marshall,C.B., Barton,C.E.,
            Sinha,S., Johnson,K.N., Tang,L. and Pietenpol,J.A.
  TITLE     ISG20L1 is a p53 family target gene that modulates genotoxic
            stress-induced autophagy
  JOURNAL   Mol Cancer 9, 95 (2010)
   PUBMED   20429933
  REMARK    GeneRIF: identification of ISG20L1 as a p53 family target and
            discovery that modulation of this target can regulate autophagic
            processes further strengthens the connection between p53 signaling
            and autophagy
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 325)
  AUTHORS   Kawase,T., Ichikawa,H., Ohta,T., Nozaki,N., Tashiro,F., Ohki,R. and
            Taya,Y.
  TITLE     p53 target gene AEN is a nuclear exonuclease required for
            p53-dependent apoptosis
  JOURNAL   Oncogene 27 (27), 3797-3810 (2008)
   PUBMED   18264133
  REMARK    GeneRIF: AEN is an important downstream mediator of p53 in
            apoptosis induction in cancer.
REFERENCE   9  (residues 1 to 325)
  AUTHORS   Lee,J.H., Koh,Y.A., Cho,C.K., Lee,S.J., Lee,Y.S. and Bae,S.
  TITLE     Identification of a novel ionizing radiation-induced nuclease, AEN,
            and its functional characterization in apoptosis
  JOURNAL   Biochem Biophys Res Commun 337 (1), 39-47 (2005)
   PUBMED   16171785
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC013489.17.
            
            On Jul 12, 2008 this sequence version replaced NP_073604.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.198050.1,
                                           SRR1803616.258846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000332810.4/ ENSP00000331944.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..325
                     /product="apoptosis-enhancing nuclease"
                     /note="interferon stimulated exonuclease gene 20kDa-like
                     1; interferon-stimulated 20 kDa exonuclease-like 1"
                     /calculated_mol_wt=36219
     Region          27..35
                     /region_name="Nucleolar localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WTP8.2)"
     Region          85..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WTP8.2)"
     Region          111..267
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Site            order(114..117,193..194,196..198,258)
                     /site_type="active"
                     /db_xref="CDD:99852"
     Site            order(114,116,198,258)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99852"
     Site            order(115..117,193..194,196..197,258)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99852"
     Region          165..188
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:18264133"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WTP8.2)"
     Region          281..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WTP8.2)"
     CDS             1..325
                     /gene="AEN"
                     /gene_synonym="ISG20L1; pp12744"
                     /coded_by="NM_022767.4:108..1085"
                     /db_xref="CCDS:CCDS10344.1"
                     /db_xref="GeneID:64782"
                     /db_xref="HGNC:HGNC:25722"
                     /db_xref="MIM:610177"
ORIGIN      
        1 mvpreapesa qclcpsltip nakdvlrkrh krrsrqhqrf markallqeq gllsmppepg
       61 ssplptpfga atateaassg kqclragsgs apcsrrpapg kasgplpskc vaidcemvgt
      121 gprgrvsela rcsivsyhgn vlydkyirpe mpiadyrtrw sgitrqhmrk avpfqvaqke
      181 ilkllkgkvv vghalhndfq alkyvhprsq trdttyvpnf lsepglhtra rvslkdlalq
      241 llhkkiqvgq hghssvedat tamelyrlve vqweqqears lwtcpedrep dsstdmeqym
      301 edqywpddla hgsrggarea qdrrn
//
LOCUS       NP_001347846             445 aa            linear   ROD 27-APR-2025
DEFINITION  GRAM domain-containing protein 2B isoform 1 [Mus musculus].
ACCESSION   NP_001347846 XP_006525557
VERSION     NP_001347846.1
DBSOURCE    REFSEQ: accession NM_001360917.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC120797.9 and AC162035.5.
            
            On Feb 17, 2018 this sequence version replaced XP_006525557.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057978.1, SRR5189685.110865.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849377, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 30.43 cM"
     Protein         1..445
                     /product="GRAM domain-containing protein 2B isoform 1"
                     /note="HCV NS3-transactivated protein 2; GRAM
                     domain-containing protein 3; GRAM domain-containing
                     protein 2B; GRAM domain containing 3"
                     /calculated_mol_wt=49141
     Region          1..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PEM6.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q96HH9; propagated from
                     UniProtKB/Swiss-Prot (Q6PEM6.2)"
     Region          135..227
                     /region_name="PH-GRAM_GRAMDC"
                     /note="GRAM domain-containing protein (GRAMDC) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13220"
                     /db_xref="CDD:275406"
     Region          233..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PEM6.2)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6PEM6.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6PEM6.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6PEM6.2)"
     Region          277..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PEM6.2)"
     CDS             1..445
                     /gene="Gramd2b"
                     /gene_synonym="9030613F08Rik; 9130427A09Rik; Gramd3;
                     NS3TP2"
                     /coded_by="NM_001360917.1:115..1452"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS89243.1"
                     /db_xref="GeneID:107022"
                     /db_xref="MGI:MGI:1914815"
ORIGIN      
        1 mvkkrlsssd nvfkfeipsn sktsaeaphs stdspssvfl sseaengaed rrrvskspta
       61 qsptssveae spdqkrslgl wskssfdgss llsdkndckt esktdskter kksssssqyk
      121 anmhfhklfl dvpteeplrq sftcalqkei lyqgklfvse nwicfhskvf gkdtkisipa
      181 fsvtlikktk tallvpnali iatvtdryif vsllsrdsty kliksvcghl entsvgnspn
      241 pssaensfra drpsslpldf ndefsdldgv vrqrrqdleg ysssgsqtpe sensrdfhvt
      301 esqtvlnvtk getkpprtda hgsrapdgka kilpahgqse tigilhkmes rkcptlhhil
      361 ivyaiivcal iistfymryr intleerlgt ltsimdphst eqtapsglgs qmqlnvevlc
      421 qeltanivkl ekiqnnlqkl lengd
//
LOCUS       NP_835464                692 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein kinase Nek8 [Homo sapiens].
ACCESSION   NP_835464
VERSION     NP_835464.1
DBSOURCE    REFSEQ: accession NM_178170.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Claus,L.R., Chen,C., Stallworth,J., Turner,J.L., Slaats,G.G.,
            Hawks,A.L., Mabillard,H., Senum,S.R., Srikanth,S.,
            Flanagan-Steet,H., Louie,R.J., Silver,J., Lerner-Ellis,J.,
            Morel,C., Mighton,C., Sleutels,F., van Slegtenhorst,M., van Ham,T.,
            Brooks,A.S., Dorresteijn,E.M., Barakat,T.S., Dahan,K., Demoulin,N.,
            Goffin,E.J., Olinger,E., Larsen,M., Hertz,J.M., Lilien,M.R.,
            Obeidova,L., Seeman,T., Stone,H.K., Kerecuk,L., Gurgu,M., Yousef
            Yengej,F.A., Ammerlaan,C.M.E., Rookmaaker,M.B., Hanna,C.,
            Rogers,R.C., Duran,K., Peters,E., Sayer,J.A., van Haaften,G.,
            Harris,P.C., Ling,K., Mason,J.M., van Eerde,A.M. and Steet,R.
  CONSRTM   Genomics England Research Consortium
  TITLE     Certain heterozygous variants in the kinase domain of the
            serine/threonine kinase NEK8 can cause an autosomal dominant form
            of polycystic kidney disease
  JOURNAL   Kidney Int 104 (5), 995-1007 (2023)
   PUBMED   37598857
  REMARK    GeneRIF: Certain heterozygous variants in the kinase domain of the
            serine/threonine kinase NEK8 can cause an autosomal dominant form
            of polycystic kidney disease.
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Cao,B., Zhang,K., Pan,C., Dong,Y. and Lu,F.
  TITLE     NEK8 regulates colorectal cancer progression via phosphorylating
            MYC
  JOURNAL   Cell Commun Signal 21 (1), 209 (2023)
   PUBMED   37596667
  REMARK    GeneRIF: NEK8 regulates colorectal cancer progression via
            phosphorylating MYC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Valkova,N., Yunis,R., Mak,S.K., Kang,K. and Kultz,D.
  TITLE     Nek8 mutation causes overexpression of galectin-1, sorcin, and
            vimentin and accumulation of the major urinary protein in renal
            cysts of jck mice
  JOURNAL   Mol Cell Proteomics 4 (7), 1009-1018 (2005)
   PUBMED   15872312
  REMARK    GeneRIF: characterization of the proteome in mice that have a
            double point mutation in the related gene.
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Bowers,A.J. and Boylan,J.F.
  TITLE     Nek8, a NIMA family kinase member, is overexpressed in primary
            human breast tumors
  JOURNAL   Gene 328, 135-142 (2004)
   PUBMED   15019993
  REMARK    GeneRIF: Data demonstrate for the first time that Nek8 is a novel
            tumor associated gene, and shares considerable sequence homology
            with the Nek family of protein kinases and may be involved in
            G(2)/M progression.
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Holland,P.M., Milne,A., Garka,K., Johnson,R.S., Willis,C.,
            Sims,J.E., Rauch,C.T., Bird,T.A. and Virca,G.D.
  TITLE     Purification, cloning, and characterization of Nek8, a novel
            NIMA-related kinase, and its candidate substrate Bicd2
  JOURNAL   J Biol Chem 277 (18), 16229-16240 (2002)
   PUBMED   11864968
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Stokman,M., Lilien,M. and Knoers,N.
  TITLE     Nephronophthisis-Related Ciliopathies
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27336129
REFERENCE   10 (residues 1 to 692)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010761.10, AY242354.1 and
            CV811826.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the serine/threionine
            protein kinase family related to NIMA (never in mitosis, gene A) of
            Aspergillus nidulans. The encoded protein may play a role in cell
            cycle progression from G2 to M phase. Mutations in the related
            mouse gene are associated with a disease phenotype that closely
            parallels the juvenile autosomal recessive form of polycystic
            kidney disease in humans. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY242354.1, SRR1803611.273324.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268766.11/ ENSP00000268766.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..692
                     /product="serine/threonine-protein kinase Nek8"
                     /EC_number="2.7.11.1"
                     /note="NIMA-related kinase 12a; NIMA-family kinase NEK8;
                     serine/thrionine-protein kinase NEK8; nephrocystin 9;
                     nimA-related protein kinase 8; nima-related protein kinase
                     12a; NIMA (never in mitosis gene a)- related kinase 8;
                     never in mitosis A-related kinase 8"
                     /calculated_mol_wt=74675
     Region          3..258
                     /region_name="STKc_Nek8"
                     /note="Catalytic domain of the Protein Serine/Threonine
                     Kinase, Never In Mitosis gene A (NIMA)-related kinase 8;
                     cd08220"
                     /db_xref="CDD:270859"
     Site            order(10..14,18,31,33,64,80..83,87,89,128,130,132..133,
                     135,147,150,152,165..168)
                     /site_type="active"
                     /db_xref="CDD:270859"
     Site            order(10..11,13..14,18,31,33,64,81..83,87,133,135,152)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270859"
     Site            order(14,87,89,128,130,132,150,165..168)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270859"
     Site            146..168
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270859"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q86SG6.1)"
     Region          277..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SG6.1)"
     Region          312..350
                     /region_name="RCC1 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SG6.1)"
     Region          313..647
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          410..461
                     /region_name="RCC1 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SG6.1)"
     Region          462..513
                     /region_name="RCC1 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SG6.1)"
     Region          580..631
                     /region_name="RCC1 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SG6.1)"
     Region          632..684
                     /region_name="RCC1 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SG6.1)"
     Region          633..673
                     /region_name="RCC1"
                     /note="Regulator of chromosome condensation (RCC1) repeat;
                     pfam00415"
                     /db_xref="CDD:395335"
     CDS             1..692
                     /gene="NEK8"
                     /gene_synonym="JCK; NEK12A; NPHP9; PKD8; RHPD2"
                     /coded_by="NM_178170.3:27..2105"
                     /db_xref="CCDS:CCDS32597.1"
                     /db_xref="GeneID:284086"
                     /db_xref="HGNC:HGNC:13387"
                     /db_xref="MIM:609799"
ORIGIN      
        1 mekyerirvv grgafgivhl clrkadqklv iikqipveqm tkeerqaaqn ecqvlkllnh
       61 pnvieyyenf ledkalmiam eyapggtlae fiqkrcnsll eeetilhffv qillalhhvh
      121 thlilhrdlk tqnilldkhr mvvkigdfgi skilsskska ytvvgtpcyi spelcegkpy
      181 nqksdiwalg cvlyelaslk rafeaanlpa lvlkimsgtf apisdryspe lrqlvlslls
      241 lepaqrppls himaqplcir allnlhtdvg svrmrraeks vapsntgsrt tsvrcrgipr
      301 gpvrpaippp lssvyawggg lgtplrlpml ntevvqvaag rtqkagvtrs grlilweapp
      361 lgagggsllp gaveqpqpqf isrflegqsg vtikhvacgd fftacltdrg iimtfgsgsn
      421 gclghgsltd isqptiveal lgyemvqvac gashvlalst erelfawgrg dsgrlglgtr
      481 eshscpqqvp mppgqeaqrv vcgidssmil tvpgqalacg snrfnklgld hlslgeepvp
      541 hqqveealsf tllgsapldq epllsidlgt ahsaavtasg dcytfgsnqh gqlgtntrrg
      601 srapckvqgl egikmamvac gdaftvaiga esevyswgkg argrlgrrde daglprpvql
      661 dethpytvts vscchgntll avrsvtdepv pp
//
LOCUS       NP_034270                984 aa            linear   ROD 27-APR-2025
DEFINITION  ephrin type-A receptor 3 isoform 1 precursor [Mus musculus].
ACCESSION   NP_034270
VERSION     NP_034270.1
DBSOURCE    REFSEQ: accession NM_010140.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Lo Giudice,Q., Wagener,R.J., Abe,P., Frangeul,L. and Jabaudon,D.
  TITLE     Developmental emergence of first- and higher-order thalamic neuron
            molecular identities
  JOURNAL   Development 151 (18) (2024)
   PUBMED   39348458
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Alderman,P.J., Saxon,D., Torrijos-Saiz,L.I., Sharief,M., Page,C.E.,
            Baroudi,J.K., Biagiotti,S.W., Butyrkin,V.A., Melamed,A., Kuo,C.T.,
            Vicini,S., Garcia-Verdugo,J.M., Herranz-Perez,V., Corbin,J.G. and
            Sorrells,S.F.
  TITLE     Delayed maturation and migration of excitatory neurons in the
            juvenile mouse paralaminar amygdala
  JOURNAL   Neuron 112 (4), 574-592 (2024)
   PUBMED   38086370
REFERENCE   4  (residues 1 to 984)
  AUTHORS   Lee,Y., Yeo,I.S., Kim,N., Lee,D.K., Kim,K.T., Yoon,J., Yi,J.,
            Hong,Y.B., Choi,B.O., Kosodo,Y., Kim,D., Park,J. and Song,M.R.
  TITLE     Transcriptional control of motor pool formation and motor circuit
            connectivity by the LIM-HD protein Isl2
  JOURNAL   Elife 12, e84596 (2023)
   PUBMED   37869988
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 984)
  AUTHORS   Ozekin,Y.H., O'Rourke,R. and Bates,E.A.
  TITLE     Single cell sequencing of the mouse anterior palate reveals
            mesenchymal heterogeneity
  JOURNAL   Dev Dyn 252 (6), 713-727 (2023)
   PUBMED   36734036
REFERENCE   6  (residues 1 to 984)
  AUTHORS   Cheng,H.J. and Flanagan,J.G.
  TITLE     Identification and cloning of ELF-1, a developmentally expressed
            ligand for the Mek4 and Sek receptor tyrosine kinases
  JOURNAL   Cell 79 (1), 157-168 (1994)
   PUBMED   7522971
REFERENCE   7  (residues 1 to 984)
  AUTHORS   Fujimoto,J. and Yamamoto,T.
  TITLE     brt, a mouse gene encoding a novel receptor-type protein-tyrosine
            kinase, is preferentially expressed in the brain
  JOURNAL   Oncogene 9 (3), 693-698 (1994)
   PUBMED   8108111
REFERENCE   8  (residues 1 to 984)
  AUTHORS   Gilardi-Hebenstreit,P., Nieto,M.A., Frain,M., Mattei,M.G.,
            Chestier,A., Wilkinson,D.G. and Charnay,P.
  TITLE     An Eph-related receptor protein tyrosine kinase gene segmentally
            expressed in the developing mouse hindbrain
  JOURNAL   Oncogene 7 (12), 2499-2506 (1992)
   PUBMED   1281307
  REMARK    Erratum:[Oncogene. 1993 Apr;8(4):1103. PMID: 8455939]
REFERENCE   9  (residues 1 to 984)
  AUTHORS   Sajjadi,F.G., Pasquale,E.B. and Subramani,S.
  TITLE     Identification of a new eph-related receptor tyrosine kinase gene
            from mouse and chicken that is developmentally regulated and
            encodes at least two forms of the receptor
  JOURNAL   New Biol 3 (8), 769-778 (1991)
   PUBMED   1657122
REFERENCE   10 (residues 1 to 984)
  AUTHORS   Lai,C. and Lemke,G.
  TITLE     An extended family of protein-tyrosine kinase genes differentially
            expressed in the vertebrate nervous system
  JOURNAL   Neuron 6 (5), 691-704 (1991)
   PUBMED   2025425
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC154844.2, AC155275.1 and AC154568.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093483.1, AK132335.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="16"
                     /map="16 36.49 cM"
     Protein         1..984
                     /product="ephrin type-A receptor 3 isoform 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 3; EPH-like kinase 4;
                     tyrosine-protein kinase TYRO4; tyrosine-protein kinase
                     receptor ETK1"
                     /calculated_mol_wt=107990
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2067
     Region          29..201
                     /region_name="EphR_LBD_A3"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 3;
                     cd10481"
                     /db_xref="CDD:198449"
     Site            order(53,55..59,66..67,69,71,102,104,109..110,152,
                     156..157,160..162,189..191,193)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198449"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29319.1)"
     Region          <323..>516
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29319.1)"
     Site            391
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29319.1)"
     Site            404
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29319.1)"
     Region          437..528
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(437,501,516)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            493
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29319.1)"
     Site            order(517..518,520..521)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            542..565
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29319.1)"
     Region          <566..619
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P29320; propagated from
                     UniProtKB/Swiss-Prot (P29319.1)"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P29320; propagated from
                     UniProtKB/Swiss-Prot (P29319.1)"
     Region          617..883
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(628,630..632,636,652,654,700..701,703,747,751..752,
                     754,765,784..788,797,831)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(628..632,636,652,654,700..703,706..707,751..752,754,
                     765)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P29320; propagated from
                     UniProtKB/Swiss-Prot (P29319.1)"
     Site            order(747,751,784..788,797,831)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            764..790
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P29320; propagated from
                     UniProtKB/Swiss-Prot (P29319.1)"
     Region          913..975
                     /region_name="SAM_EPH-A3"
                     /note="SAM domain of EPH-A3 subfamily of tyrosine kinase
                     receptors; cd09544"
                     /db_xref="CDD:188943"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:17947660; propagated from
                     UniProtKB/Swiss-Prot (P29319.1)"
     Region          982..984
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P29319.1)"
     CDS             1..984
                     /gene="Epha3"
                     /gene_synonym="Cek4; EK4; End3; ETK1; Hek; Hek4; Mek4;
                     Tyro4"
                     /coded_by="NM_010140.4:129..3083"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS28264.1"
                     /db_xref="GeneID:13837"
                     /db_xref="MGI:MGI:99612"
ORIGIN      
        1 mdchlsilvl lgccvlscsg elspqpsnev nlldsktiqg elgwisypsh gweeisgvde
       61 hytpirtyqv cnvmdhsqnn wlrtnwvprn saqkiyvelk ftlrdcnsip lvlgtcketf
      121 nlyymesddd hgvkfrehqf tkidtiaade sftqmdlgdr ilklnteire vgpvnkkgfy
      181 lafqdvgacv alvsvrvyfk kcpftvknla mfpdtvpmds qslvevrgsc vnnskeedpp
      241 rmycstegew lvpigkctcn agyeergfic qacrpgfyka sdgaakcakc pphsstqedg
      301 smncrcenny fraekdppsm actrppsapr nvisninets vildwswpld tggrkditfn
      361 iickkcgwnv rqcepcspnv rflprqlglt nttvtvtdll ahtnytfeid avngvselss
      421 pprqyaavsi ttnqaapspv mtikkdrtsr nsislswqep ehpngiildy evkyyekqeq
      481 etsytilrar gtnvtisslk pdttyvfqir artaagygtn srkfefetsp dsfsisgens
      541 hvvmiaisaa vaiivltvvt yvlvgrfcgy hkskhsaeek rlhfgnghlk lpglrtyvdp
      601 htyedptqav hefakeldat nisidkvvga gefgevcsgr lklpskkeis vaiktlkvgy
      661 tekqrrdflg easimgqfdh pniirlegvv tkskpvmivt eymengslds flrkhdaqft
      721 viqlvgmlrg iasgmkylsd mgyvhrdlaa rnilinsnlv ckvsdfglsr vleddpeaay
      781 ttrggkipir wtspeaiayr kftsasdvws ygivlwevms ygerpywems nqdvikavde
      841 gyrlpppmdc paalyqlmld cwqkdrnnrp kfeqivsild klirnpgslk iitsaaarps
      901 nllldqsnvd iatfhttgdw lngmrtahck eiftgveyss cdtiakistd dmkkvgvtvv
      961 gpqkkiisti kaletqskng pvpv
//
LOCUS       NP_006294                320 aa            linear   PRI 27-APR-2025
DEFINITION  aminoacyl tRNA synthase complex-interacting multifunctional protein
            2 isoform a [Homo sapiens].
ACCESSION   NP_006294
VERSION     NP_006294.2
DBSOURCE    REFSEQ: accession NM_006303.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Kim,H., Shin,J.Y., Ham,S., Kim,J.H., Lee,G.H., Lee,N.E., Kim,H.T.,
            Cho,S.H., Kim,S. and Lee,Y.
  TITLE     AIMP2 accumulation in brain leads to cognitive deficits and blood
            secretion in Parkinson's disease
  JOURNAL   J Transl Med 22 (1), 919 (2024)
   PUBMED   39390613
  REMARK    GeneRIF: AIMP2 accumulation in brain leads to cognitive deficits
            and blood secretion in Parkinson's disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Ren,J., Yu,L., Zhang,Q., Ren,P., Cai,Y., Wang,X., Lan,K. and Wu,S.
  TITLE     AIMP2 restricts EV71 replication by recruiting SMURF2 to promote
            the degradation of 3D polymerase
  JOURNAL   Virol Sin 39 (4), 632-644 (2024)
   PUBMED   38945214
  REMARK    GeneRIF: AIMP2 restricts EV71 replication by recruiting SMURF2 to
            promote the degradation of 3D polymerase.
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Jaramillo Ponce,J.R., Kapps,D., Paulus,C., Chicher,J. and
            Frugier,M.
  TITLE     Discovery of two distinct aminoacyl-tRNA synthetase complexes
            anchored to the Plasmodium surface tRNA import protein
  JOURNAL   J Biol Chem 298 (6), 101987 (2022)
   PUBMED   35487244
  REMARK    GeneRIF: Discovery of two distinct aminoacyl-tRNA synthetase
            complexes anchored to the Plasmodium surface tRNA import protein.
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Kim,D.G., Choi,Y., Lee,Y., Lim,S., Kong,J., Song,J., Roh,Y.,
            Harmalkar,D.S., Lee,K., Goo,J.I., Cho,H.Y., Mushtaq,A.U., Lee,J.,
            Park,S.H., Kim,D., Min,B.S., Lee,K.Y., Jeon,Y.H., Lee,S., Lee,K.
            and Kim,S.
  TITLE     AIMP2-DX2 provides therapeutic interface to control KRAS-driven
            tumorigenesis
  JOURNAL   Nat Commun 13 (1), 2572 (2022)
   PUBMED   35546148
  REMARK    GeneRIF: AIMP2-DX2 provides therapeutic interface to control
            KRAS-driven tumorigenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Lamour,V., Quevillon,S., Diriong,S., N'Guyen,V.C., Lipinski,M. and
            Mirande,M.
  TITLE     Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme
            as a case of horizontal gene transfer
  JOURNAL   Proc Natl Acad Sci U S A 91 (18), 8670-8674 (1994)
   PUBMED   8078941
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Shiba,K., Suzuki,N., Shigesada,K., Namba,Y., Schimmel,P. and
            Noda,T.
  TITLE     Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence
            of the anticodon-binding domain and acquisition of a new structural
            unit
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7435-7439 (1994)
   PUBMED   8052601
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Kaiser,E., Hu,B., Becher,S., Eberhard,D., Schray,B., Baack,M.,
            Hameister,H. and Knippers,R.
  TITLE     The human EPRS locus (formerly the QARS locus): a gene encoding a
            class I and a class II aminoacyl-tRNA synthetase
  JOURNAL   Genomics 19 (2), 280-290 (1994)
   PUBMED   8188258
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Escalante,C. and Yang,D.C.
  TITLE     Expression of human aspartyl-tRNA synthetase in Escherichia coli.
            Functional analysis of the N-terminal putative amphiphilic helix
  JOURNAL   J Biol Chem 268 (8), 6014-6023 (1993)
   PUBMED   8449960
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Norcum,M.T.
  TITLE     Structural analysis of the high molecular mass aminoacyl-tRNA
            synthetase complex. Effects of neutral salts and detergents
  JOURNAL   J Biol Chem 266 (23), 15398-15405 (1991)
   PUBMED   1651330
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005995.3 and BC002853.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 8, 2000 this sequence version replaced NP_006294.1.
            
            Summary: The protein encoded by this gene is part of the
            aminoacyl-tRNA synthetase complex, which contains nine different
            aminoacyl-tRNA synthetases and three non-enzymatic factors. The
            encoded protein is one of the non-enzymatic factors and is required
            for assembly and stability of the complex. [provided by RefSeq, May
            2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U24169.1, SRR1163655.540417.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000223029.8/ ENSP00000223029.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..320
                     /product="aminoacyl tRNA synthase complex-interacting
                     multifunctional protein 2 isoform a"
                     /note="ARS-interacting multi-functional protein 2;
                     aminoacyl tRNA synthase complex-interacting
                     multifunctional protein 2; multisynthetase complex
                     auxiliary component p38; multisynthase complex auxiliary
                     component p38; protein JTV-1"
                     /calculated_mol_wt=35218
     Region          1..44
                     /region_name="AIMP2_LysRS_bd"
                     /note="AIMP2 lysyl-tRNA synthetase binding domain;
                     pfam16780"
                     /db_xref="CDD:465269"
     Region          82..162
                     /region_name="Interaction with PRKN.
                     /evidence=ECO:0000269|PubMed:16135753"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13155.2)"
     Region          117..208
                     /region_name="Thioredoxin_16"
                     /note="Thioredoxin-like domain; pfam18569"
                     /db_xref="CDD:436585"
     Region          162..225
                     /region_name="Interaction with TP53.
                     /evidence=ECO:0000269|PubMed:18695251"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13155.2)"
     Region          214..309
                     /region_name="GST_C_AIMP2"
                     /note="Glutathione S-transferase C-terminal-like, alpha
                     helical domain of Aminoacyl tRNA synthetase
                     complex-Interacting Multifunctional Protein 2; cd03200"
                     /db_xref="CDD:198309"
     Site            order(230..232,234..239,241..242,255,258,264..265)
                     /site_type="other"
                     /note="putative protein interface 1 [polypeptide binding]"
                     /db_xref="CDD:198309"
     Site            order(263..267,297..298,300..301,305,308..309)
                     /site_type="other"
                     /note="putative protein interface 2 [polypeptide binding]"
                     /db_xref="CDD:198309"
     CDS             1..320
                     /gene="AIMP2"
                     /gene_synonym="HLD17; JTV-1; JTV1; P38"
                     /coded_by="NM_006303.4:93..1055"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5344.1"
                     /db_xref="GeneID:7965"
                     /db_xref="HGNC:HGNC:20609"
                     /db_xref="MIM:600859"
ORIGIN      
        1 mpmyqvkpyh gggaplrvel ptcmyrlpnv hgrsygpapg aghvqeesnl slqalesrqd
       61 dilkrlyelk aavdglskmi qtpdadldvt niiqadeptt lttnaldlns vlgkdygalk
      121 divinanpas pplsllvlhr llcehfrvls tvhthssvks vpenllkcfg eqnkkqprqd
      181 yqlgftliwk nvpktqmkfs iqtmcpiege gniarflfsl fgqkhnavna tlidswvdia
      241 ifqlkegssk ekaavfrsmn salgkspwla gneltvadvv lwsvlqqigg csvtvpanvq
      301 rwmrscenla pfntalkllk
//
LOCUS       NP_001128123             224 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 4E type 3 isoform a [Homo
            sapiens].
ACCESSION   NP_001128123
VERSION     NP_001128123.1
DBSOURCE    REFSEQ: accession NM_001134651.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Xu,X., Zhao,Y., Ying,Y., Zhu,H., Luo,J., Mou,T. and Zhang,Z.
  TITLE     m7G-related genes-NCBP2 and EIF4E3 determine immune contexture in
            head and neck squamous cell carcinoma by regulating CCL4/CCL5
            expression
  JOURNAL   Mol Carcinog 62 (8), 1091-1106 (2023)
   PUBMED   37067401
  REMARK    GeneRIF: m7G-related genes-NCBP2 and EIF4E3 determine immune
            contexture in head and neck squamous cell carcinoma by regulating
            CCL4/CCL5 expression.
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Weiss,B., Allen,G.E., Kloehn,J., Abid,K., Jaquier-Gubler,P. and
            Curran,J.A.
  TITLE     eIF4E3 forms an active eIF4F complex during stresses (eIF4FS)
            targeting mTOR and re-programs the translatome
  JOURNAL   Nucleic Acids Res 49 (9), 5159-5176 (2021)
   PUBMED   33893802
  REMARK    GeneRIF: eIF4E3 forms an active eIF4F complex during stresses
            (eIF4FS) targeting mTOR and re-programs the translatome.
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Mrvova,S., Frydryskova,K., Pospisek,M., Vopalensky,V. and Masek,T.
  TITLE     Major splice variants and multiple polyadenylation site utilization
            in mRNAs encoding human translation initiation factors eIF4E1 and
            eIF4E3 regulate the translational regulators?
  JOURNAL   Mol Genet Genomics 293 (1), 167-186 (2018)
   PUBMED   28942592
  REMARK    GeneRIF: We performed bioinformatics analyses of ESTs and the
            3'UTRs of the main transcript splice variants of the translational
            initiation factor eIF4E1 and its family members, eIF4E2 and eIF4E3.
            We propose to elucidate the minor splice variants of eIF4E2 and
            eIF4E3 in great detail because they might produce proteins with
            modified features that fulfill different cellular roles from their
            major counterparts.
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Frydryskova,K., Masek,T., Borcin,K., Mrvova,S., Venturi,V. and
            Pospisek,M.
  TITLE     Distinct recruitment of human eIF4E isoforms to processing bodies
            and stress granules
  JOURNAL   BMC Mol Biol 17 (1), 21 (2016)
   PUBMED   27578149
  REMARK    GeneRIF: Following heat shock, eIF4E2 is found in both processing
            bodies and stress granules, whereas eIF4E3_A relocates only to
            stress granules.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Landon,A.L., Muniandy,P.A., Shetty,A.C., Lehrmann,E., Volpon,L.,
            Houng,S., Zhang,Y., Dai,B., Peroutka,R., Mazan-Mamczarz,K.,
            Steinhardt,J., Mahurkar,A., Becker,K.G., Borden,K.L. and
            Gartenhaus,R.B.
  TITLE     MNKs act as a regulatory switch for eIF4E1 and eIF4E3 driven mRNA
            translation in DLBCL
  JOURNAL   Nat Commun 5, 5413 (2014)
   PUBMED   25403230
  REMARK    GeneRIF: MNK1 and MNK2 inhibition ablates eIF4E1 phosphorylation
            and concurrently enhances eIF4E3 expression in diffuse large B-cell
            lymphoma.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Volpon,L., Osborne,M.J., Culjkovic-Kraljacic,B. and Borden,K.L.
  TITLE     eIF4E3, a new actor in mRNA metabolism and tumor suppression
  JOURNAL   Cell Cycle 12 (8), 1159-1160 (2013)
   PUBMED   23587918
  REMARK    GeneRIF: eIF4E3 impedes oncogenic transformation and its expression
            is lost in some cancers.
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Osborne,M.J., Volpon,L., Kornblatt,J.A., Culjkovic-Kraljacic,B.,
            Baguet,A. and Borden,K.L.
  TITLE     eIF4E3 acts as a tumor suppressor by utilizing an atypical mode of
            methyl-7-guanosine cap recognition
  JOURNAL   Proc Natl Acad Sci U S A 110 (10), 3877-3882 (2013)
   PUBMED   23431134
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Joshi,B., Cameron,A. and Jagus,R.
  TITLE     Characterization of mammalian eIF4E-family members
  JOURNAL   Eur J Biochem 271 (11), 2189-2203 (2004)
   PUBMED   15153109
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC134770.2, DR159502.1, AK126999.1, AC097634.2 and AL161983.1.
            
            Summary: EIF4E3 belongs to the EIF4E family of translational
            initiation factors that interact with the 5-prime cap structure of
            mRNA and recruit mRNA to the ribosome (Joshi et al., 2004 [PubMed
            15153109]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK126999.1, SRR18074969.1378412.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000425534.8/ ENSP00000393324.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..224
                     /product="eukaryotic translation initiation factor 4E type
                     3 isoform a"
                     /note="eukaryotic translation initiation factor 4E type 3"
                     /calculated_mol_wt=24310
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5X7.4)"
     Region          48..198
                     /region_name="IF4E"
                     /note="Eukaryotic initiation factor 4E; pfam01652"
                     /db_xref="CDD:460281"
     CDS             1..224
                     /gene="EIF4E3"
                     /gene_synonym="eIF-4E3; eIF4E-3"
                     /coded_by="NM_001134651.2:36..710"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46867.1"
                     /db_xref="GeneID:317649"
                     /db_xref="HGNC:HGNC:31837"
                     /db_xref="MIM:609896"
ORIGIN      
        1 malppaaapp agareppgsr aaaaaaapep plglqqlsal qpepggvplh sswtfwldrs
       61 lpgataaeca snlkkiytvq tvqifwsvyn nippvtslpl rcsyhlmrge rrplweeesn
      121 akggvwkmkv pkdststvwk elllatigeq ftdcaaadde vigvsvsvrd redvvqvwnv
      181 naslvgeatv lekiyellph itfkavfykp heehhafegg rgkh
//
LOCUS       NP_006712                362 aa            linear   PRI 27-APR-2025
DEFINITION  adenosine kinase isoform b [Homo sapiens].
ACCESSION   NP_006712
VERSION     NP_006712.2
DBSOURCE    REFSEQ: accession NM_006721.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Chen,T., Yu,J., Guo,X., Wang,S., Wang,Z., Chen,Y., Hu,X., Li,H.,
            Chen,L. and Zheng,J.
  TITLE     Adenosine kinase inhibits beta-cell proliferation by upregulating
            DNA methyltransferase 3A expression
  JOURNAL   Diabetes Obes Metab 26 (7), 2956-2968 (2024)
   PUBMED   38699782
  REMARK    GeneRIF: Adenosine kinase inhibits beta-cell proliferation by
            upregulating DNA methyltransferase 3A expression.
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Li,H., Zheng,J., Xu,Q., Yang,Y., Zhou,J., Guo,X., Cai,Y., Cai,J.J.,
            Xie,L., Awika,J., Han,X., Li,Q., Kennedy,L., Francis,H., Glaser,S.,
            Huo,Y., Alpini,G. and Wu,C.
  TITLE     Hepatocyte Adenosine Kinase Promotes Excessive Fat Deposition and
            Liver Inflammation
  JOURNAL   Gastroenterology 164 (1), 134-146 (2023)
   PUBMED   36181835
  REMARK    GeneRIF: Hepatocyte Adenosine Kinase Promotes Excessive Fat
            Deposition and Liver Inflammation.
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Zhang,Y., Wang,X., Tang,C., Guan,Y., Chen,F., Gao,Q., Wang,J.,
            Zhou,J., Zhai,F., Boison,D., Luan,G. and Li,T.
  TITLE     Genetic variations of adenosine kinase as predictable biomarkers of
            efficacy of vagus nerve stimulation in patients with
            pharmacoresistant epilepsy
  JOURNAL   J Neurosurg 136 (3), 726-735 (2021)
   PUBMED   34479194
  REMARK    GeneRIF: Genetic variations of adenosine kinase as predictable
            biomarkers of efficacy of vagus nerve stimulation in patients with
            pharmacoresistant epilepsy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Becker,P.H., Demir,Z., Mozer Glassberg,Y., Sevin,C., Habes,D.,
            Imbard,A., Mussini,C., Rozenfeld Bar Lev,M., Davit-Spraul,A.,
            Benoist,J.F., Therond,P., Slama,A., Jacquemin,E., Gonzales,E. and
            Gaignard,P.
  TITLE     Adenosine kinase deficiency: Three new cases and diagnostic value
            of hypermethioninemia
  JOURNAL   Mol Genet Metab 132 (1), 38-43 (2021)
   PUBMED   33309011
  REMARK    GeneRIF: Adenosine kinase deficiency: Three new cases and
            diagnostic value of hypermethioninemia.
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Luan,G., Wang,X., Gao,Q., Guan,Y., Wang,J., Deng,J., Zhai,F.,
            Chen,Y. and Li,T.
  TITLE     Upregulation of Neuronal Adenosine A1 Receptor in Human Rasmussen
            Encephalitis
  JOURNAL   J Neuropathol Exp Neurol 76 (8), 720-731 (2017)
   PUBMED   28789481
  REMARK    GeneRIF: The results of this study showed that over-expression of
            the major adenosine removing enzyme ADK in reactive astrocytes and
            subpopulation of remaining neurons in Rasmussen Encephalitis
            patients plays an important role in the epileptogensis of Rasmussen
            Encephalitis.
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Singh,B., Hao,W., Wu,Z., Eigl,B. and Gupta,R.S.
  TITLE     Cloning and characterization of cDNA for adenosine kinase from
            mammalian (Chinese hamster, mouse, human and rat) species. High
            frequency mutants of Chinese hamster ovary cells involve structural
            alterations in the gene
  JOURNAL   Eur J Biochem 241 (2), 564-571 (1996)
   PUBMED   8917457
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Spychala,J., Datta,N.S., Takabayashi,K., Datta,M., Fox,I.H.,
            Gribbin,T. and Mitchell,B.S.
  TITLE     Cloning of human adenosine kinase cDNA: sequence similarity to
            microbial ribokinases and fructokinases
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1232-1237 (1996)
   PUBMED   8577746
REFERENCE   8  (residues 1 to 362)
  AUTHORS   Hurley,M.C., Lin,B. and Fox,I.H.
  TITLE     Regulation of deoxyadenosine and nucleoside analog phosphorylation
            by human placental adenosine kinase
  JOURNAL   J Biol Chem 260 (29), 15675-15681 (1985)
   PUBMED   2999129
REFERENCE   9  (residues 1 to 362)
  AUTHORS   Andres,C.M. and Fox,I.H.
  TITLE     Purification and properties of human placental adenosine kinase
  JOURNAL   J Biol Chem 254 (22), 11388-11393 (1979)
   PUBMED   227870
REFERENCE   10 (residues 1 to 362)
  AUTHORS   Klobutcher,L.A., Nichols,E.A., Kucherlapati,R.S. and Ruddle,F.H.
  TITLE     Assignment of the gene for human adenosine kinase to chromosome 10
            using a somatic cell hybrid clone panel
  JOURNAL   Cytogenet Cell Genet 16 (1-5), 171-174 (1976)
   PUBMED   185014
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301590.1, U90338.1 and
            HM005327.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 9, 2003 this sequence version replaced NP_006712.1.
            
            Summary: This gene an enzyme which catalyzes the transfer of the
            gamma-phosphate from ATP to adenosine, thereby serving as a
            regulator of concentrations of both extracellular adenosine and
            intracellular adenine nucleotides. Adenosine has widespread effects
            on the cardiovascular, nervous, respiratory, and immune systems and
            inhibitors of the enzyme could play an important pharmacological
            role in increasing intravascular adenosine concentrations and
            acting as anti-inflammatory agents. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (2), alternately referred to as
            ADK-long, differs in the 5' UTR and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (b) is longer than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000539909.6/ ENSP00000443965.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..362
                     /product="adenosine kinase isoform b"
                     /EC_number="2.7.1.20"
                     /note="adenosine 5'-phosphotransferase; testicular tissue
                     protein Li 14"
                     /calculated_mol_wt=40414
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P55263.2)"
     Region          8..16
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:19635462"
                     /note="propagated from UniProtKB/Swiss-Prot (P55263.2)"
     Region          29..361
                     /region_name="ribokinase_pfkB_like"
                     /note="ribokinase/pfkB superfamily: Kinases that accept a
                     wide variety of substrates, including carbohydrates and
                     aromatic small molecules, all are phosphorylated at a
                     hydroxyl group. The superfamily includes ribokinase,
                     fructokinase, ketohexokinase; cl00192"
                     /db_xref="CDD:469648"
     Site            order(31,33,35,55,80..82,85,140,151,153,155,187,218,
                     313..314,317)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238573"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:12112843; propagated from
                     UniProtKB/Swiss-Prot (P55263.2)"
     Site            order(282,284..285,288,299,301,309,312,315..316,319,344,
                     348)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238573"
     CDS             1..362
                     /gene="ADK"
                     /gene_synonym="AK"
                     /coded_by="NM_006721.4:59..1147"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7343.1"
                     /db_xref="GeneID:132"
                     /db_xref="HGNC:HGNC:257"
                     /db_xref="MIM:102750"
ORIGIN      
        1 maaaeeepkp kklkveapqa lrenilfgmg nplldisavv dkdfldkysl kpndqilaed
       61 khkelfdelv kkfkveyhag gstqnsikva qwmiqqphka atffgcigid kfgeilkrka
      121 aeahvdahyy eqneqptgtc aacitgdnrs lianlaaanc ykkekhldle knwmlvekar
      181 vcyiagfflt vspesvlkva hhasennrif tlnlsapfis qfykeslmkv mpyvdilfgn
      241 eteaatfare qgfetkdike iakktqalpk mnskrqrivi ftqgrddtim atesevtafa
      301 vldqdqkeii dtngagdafv ggflsqlvsd kpltecirag hyaasiiirr tgctfpekpd
      361 fh
//
LOCUS       NP_001353140             883 aa            linear   PRI 27-APR-2025
DEFINITION  disks large homolog 1 isoform 10 [Homo sapiens].
ACCESSION   NP_001353140
VERSION     NP_001353140.1
DBSOURCE    REFSEQ: accession NM_001366211.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Veljacic Viskovic,D., Lozic,M., Vukoja,M., Soljic,V., Vukojevic,K.,
            Glavina Durdov,M., Filipovic,N. and Lozic,B.
  TITLE     Spatio-Temporal Expression Pattern of CAKUT Candidate Genes DLG1
            and KIF12 during Human Kidney Development
  JOURNAL   Biomolecules 13 (2), 340 (2023)
   PUBMED   36830709
  REMARK    GeneRIF: Spatio-Temporal Expression Pattern of CAKUT Candidate
            Genes DLG1 and KIF12 during Human Kidney Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 883)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 883)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 883)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 883)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 883)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 883)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.211204.1,
                                           SRR1803611.123990.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..883
                     /product="disks large homolog 1 isoform 10"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=98183
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          692..870
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..883
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366211.1:495..3146"
                     /note="isoform 10 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS93453.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt snasdsessy
      661 lilitdeygc skggqeeyvl syepvnqqev nytrpviilg pmkdrinddl isefpdkfgs
      721 cvphttrpkr dyevdgrdyh fvtsreqmek diqehkfiea gqynnhlygt svqsvrevae
      781 kgkhcildvs gnaikrlqia qlypisifik pksmenimem nkrlteeqar ktferamkle
      841 qeftehftai vqgdtlediy nqvkqiieeq sgsyiwvpak ekl
//
LOCUS       NP_112578                356 aa            linear   PRI 27-APR-2025
DEFINITION  INO80 complex subunit B [Homo sapiens].
ACCESSION   NP_112578
VERSION     NP_112578.2
DBSOURCE    REFSEQ: accession NM_031288.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Zhang,S., Zhou,B., Wang,L., Li,P., Bennett,B.D., Snyder,R.,
            Garantziotis,S., Fargo,D.C., Cox,A.D., Chen,L. and Hu,G.
  TITLE     INO80 is required for oncogenic transcription and tumor growth in
            non-small cell lung cancer
  JOURNAL   Oncogene 36 (10), 1430-1439 (2017)
   PUBMED   27641337
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Cao,L., Ding,J., Dong,L., Zhao,J., Su,J., Wang,L., Sui,Y., Zhao,T.,
            Wang,F., Jin,J. and Cai,Y.
  TITLE     Negative Regulation of p21Waf1/Cip1 by Human INO80 Chromatin
            Remodeling Complex Is Implicated in Cell Cycle Phase G2/M Arrest
            and Abnormal Chromosome Stability
  JOURNAL   PLoS One 10 (9), e0137411 (2015)
   PUBMED   26340092
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Oudejans,C.B., Michel,O.J., Janssen,R., Habets,R., Poutsma,A.,
            Sistermans,E.A., Weiss,M.M., Incarnato,D., Oliviero,S.,
            Kleiverda,G., Van Dijk,M. and Arngrimsson,R.
  TITLE     Susceptibility allele-specific loss of miR-1324-mediated silencing
            of the INO80B chromatin-assembly complex gene in pre-eclampsia
  JOURNAL   Hum Mol Genet 24 (1), 118-127 (2015)
   PUBMED   25143393
  REMARK    GeneRIF: pathway-guided genome-wide meta-analysis and mutational
            analysis identified INO80B gene is a susceptibility gene for
            pre-eclampsia.
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Vassileva,I., Yanakieva,I., Peycheva,M., Gospodinov,A. and
            Anachkova,B.
  TITLE     The mammalian INO80 chromatin remodeling complex is required for
            replication stress recovery
  JOURNAL   Nucleic Acids Res 42 (14), 9074-9086 (2014)
   PUBMED   25016522
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Miyako,K., Cobb,L.J., Francis,M., Huang,A., Peng,B., Pintar,J.E.,
            Ariga,H. and Cohen,P.
  TITLE     PAPA-1 Is a nuclear binding partner of IGFBP-2 and modulates its
            growth-promoting actions
  JOURNAL   Mol Endocrinol 23 (2), 169-175 (2009)
   PUBMED   19095771
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Jin,J., Cai,Y., Yao,T., Gottschalk,A.J., Florens,L., Swanson,S.K.,
            Gutierrez,J.L., Coleman,M.K., Workman,J.L., Mushegian,A.,
            Washburn,M.P., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian chromatin remodeling complex with similarities to the
            yeast INO80 complex
  JOURNAL   J Biol Chem 280 (50), 41207-41212 (2005)
   PUBMED   16230350
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Kuroda,T.S., Maita,H., Tabata,T., Taira,T., Kitaura,H., Ariga,H.
            and Iguchi-Ariga,S.M.
  TITLE     A novel nucleolar protein, PAPA-1, induces growth arrest as a
            result of cell cycle arrest at the G1 phase
  JOURNAL   Gene 340 (1), 83-98 (2004)
   PUBMED   15556297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB451812.1 and BC064425.1.
            
            On May 4, 2006 this sequence version replaced NP_112578.1.
            
            Summary: This gene encodes a subunit of an ATP-dependent chromatin
            remodeling complex, INO80, which plays a role in DNA and
            nucleosome-activated ATPase activity and ATP-dependent nucleosome
            sliding. Readthrough transcription of this gene into the
            neighboring downstream gene, which encodes WW domain-binding
            protein 1, generates a non-coding transcript. [provided by RefSeq,
            Feb 2011].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064425.1, ERR279845.3562.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000233331.12/ ENSP00000233331.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..356
                     /product="INO80 complex subunit B"
                     /note="PAP (Pim-1 associated protein) associated protein
                     1; high mobility group AT-hook 1-like 4; zinc finger, HIT
                     type 4; IES2 homolog; PAP-1 binding protein;
                     PAP-1-associated protein 1; zinc finger HIT
                     domain-containing protein 4"
                     /calculated_mol_wt=38506
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C086.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99PT3; propagated from
                     UniProtKB/Swiss-Prot (Q9C086.2)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99PT3; propagated from
                     UniProtKB/Swiss-Prot (Q9C086.2)"
     Region          124..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C086.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99PT3; propagated from
                     UniProtKB/Swiss-Prot (Q9C086.2)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99PT3; propagated from
                     UniProtKB/Swiss-Prot (Q9C086.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99PT3; propagated from
                     UniProtKB/Swiss-Prot (Q9C086.2)"
     Region          211..287
                     /region_name="PAPA-1"
                     /note="PAPA-1-like conserved region; pfam04795"
                     /db_xref="CDD:461431"
     Region          246..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C086.2)"
     Region          286..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C086.2)"
     Region          309..339
                     /region_name="zf-HIT_IN80B"
                     /note="zinc finger HIT (zf-HIT) found in INO80 complex
                     subunit B (INO80B) and similar proteins; cd23021"
                     /db_xref="CDD:467793"
     Site            order(314,330,334)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:467793"
     Site            order(318..324,330..332,335..336)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467793"
     CDS             1..356
                     /gene="INO80B"
                     /gene_synonym="hIes2; HMGA1L4; HMGIYL4; IES2; PAP-1BP;
                     PAPA-1; PAPA1; ZNHIT4"
                     /coded_by="NM_031288.4:31..1101"
                     /db_xref="CCDS:CCDS1942.2"
                     /db_xref="GeneID:83444"
                     /db_xref="HGNC:HGNC:13324"
                     /db_xref="MIM:616456"
ORIGIN      
        1 msklwrrgst sgameapepg ealelslaga hghgvhkkkh kkhkkkhkkk hhqeedagpt
       61 qpspakpqlk lkiklggqvl gtksvptftv ipegprspsp lmvvdneeep megvpleqyr
      121 awldedsnls psplrdlsgg lggqeeeeeq rwldalekge lddngdlkke inerlltarq
      181 rallqkarsq pspmlplpva egcpppalte emllkreera rkrrlqaarr aeehknqtie
      241 rltktaatsg rggrggarge rrggraaapa pmvrycsgaq gstlsfppgv paptavsqrp
      301 spsgppprcs vpgcphprry acsrtgqalc slqcyrinlq mrlggpegpg spllat
//
LOCUS       NP_001416                163 aa            linear   PRI 27-APR-2025
DEFINITION  epithelial membrane protein 3 [Homo sapiens].
ACCESSION   NP_001416
VERSION     NP_001416.1
DBSOURCE    REFSEQ: accession NM_001425.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Li,L., Xia,S., Zhao,Z., Deng,L., Wang,H., Yang,D., Hu,Y., Ji,J.,
            Huang,D. and Xin,T.
  TITLE     EMP3 as a prognostic biomarker correlates with EMT in GBM
  JOURNAL   BMC Cancer 24 (1), 89 (2024)
   PUBMED   38229014
  REMARK    GeneRIF: EMP3 as a prognostic biomarker correlates with EMT in GBM.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Martija,A.A., Krauss,A., Bachle,N., Doth,L., Christians,A.,
            Krunic,D., Schneider,M., Helm,D., Will,R., Hartmann,C.,
            Herold-Mende,C., von Deimling,A. and Pusch,S.
  TITLE     EMP3 sustains oncogenic EGFR/CDK2 signaling by restricting receptor
            degradation in glioblastoma
  JOURNAL   Acta Neuropathol Commun 11 (1), 177 (2023)
   PUBMED   37936247
  REMARK    GeneRIF: EMP3 sustains oncogenic EGFR/CDK2 signaling by restricting
            receptor degradation in glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Ilsley,M.D., Storry,J.R. and Olsson,M.L.
  TITLE     Yes, MAM: how the cancer-related EMP3 protein became a regulator of
            erythropoiesis and the key protein underlying a new blood group
            system
  JOURNAL   Immunohematology 38 (4), 130-136 (2022)
   PUBMED   36789459
  REMARK    GeneRIF: Yes, MAM: how the cancer-related EMP3 protein became a
            regulator of erythropoiesis and the key protein underlying a new
            blood group system.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Kim,E.K. and Koo,J.S.
  TITLE     Expression of epithelial membrane protein (EMP) 1, EMP 2, and EMP 3
            in thyroid cancer
  JOURNAL   Histol Histopathol 37 (1), 51-61 (2022)
   PUBMED   34617578
  REMARK    GeneRIF: Expression of epithelial membrane protein (EMP) 1, EMP 2,
            and EMP 3 in thyroid cancer.
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Lv,Q., Xiao,W., Xiong,Z., Shi,J., Miao,D., Meng,X., Yuan,H.,
            Yang,H. and Zhang,X.
  TITLE     Identification of candidate biomarker EMP3 and its prognostic
            potential in clear cell renal cell carcinoma
  JOURNAL   Front Biosci (Landmark Ed) 26 (11), 1176-1190 (2021)
   PUBMED   34856762
  REMARK    GeneRIF: Identification of candidate biomarker EMP3 and its
            prognostic potential in clear cell renal cell carcinoma.
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Liehr,T., Kuhlenbaumer,G., Wulf,P., Taylor,V., Suter,U., Van
            Broeckhoven,C., Lupski,J.R., Claussen,U. and Rautenstrauss,B.
  TITLE     Regional localization of the human epithelial membrane protein
            genes 1, 2, and 3 (EMP1, EMP2, EMP3) to 12p12.3, 16p13.2, and
            19q13.3
  JOURNAL   Genomics 58 (1), 106-108 (1999)
   PUBMED   10331954
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Bolin,L.M., McNeil,T., Lucian,L.A., DeVaux,B., Franz-Bacon,K.,
            Gorman,D.M., Zurawski,S., Murray,R. and McClanahan,T.K.
  TITLE     HNMP-1: a novel hematopoietic and neural membrane protein
            differentially regulated in neural development and injury
  JOURNAL   J Neurosci 17 (14), 5493-5502 (1997)
   PUBMED   9204931
REFERENCE   8  (residues 1 to 163)
  AUTHORS   Ben-Porath,I. and Benvenisty,N.
  TITLE     Characterization of a tumor-associated gene, a member of a novel
            family of genes encoding membrane glycoproteins
  JOURNAL   Gene 183 (1-2), 69-75 (1996)
   PUBMED   8996089
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Taylor,V. and Suter,U.
  TITLE     Epithelial membrane protein-2 and epithelial membrane protein-3:
            two novel members of the peripheral myelin protein 22 gene family
  JOURNAL   Gene 175 (1-2), 115-120 (1996)
   PUBMED   8917086
REFERENCE   10 (residues 1 to 163)
  AUTHORS   Lobsiger,C.S., Magyar,J.P., Taylor,V., Wulf,P., Welcher,A.A.,
            Program,A.E. and Suter,U.
  TITLE     Identification and characterization of a cDNA and the structural
            gene encoding the mouse epithelial membrane protein-1
  JOURNAL   Genomics 36 (3), 379-387 (1996)
   PUBMED   8884260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL541088.3 and BC009718.1.
            
            Summary: The protein encoded by this gene belongs to the
            PMP-22/EMP/MP20 family of proteins. The protein contains four
            transmembrane domains and two N-linked glycosylation sites. It is
            thought to be involved in cell proliferation, cell-cell
            interactions and function as a tumor suppressor. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.570470.1, BQ017062.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270221.11/ ENSP00000270221.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..163
                     /product="epithelial membrane protein 3"
                     /note="EMP-3; HNMP-1; hematopoietic neural membrane
                     protein 1"
                     /calculated_mol_wt=18298
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54852.1)"
     Region          20..156
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54852.1)"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54852.1)"
     Site            66..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54852.1)"
     Site            100..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54852.1)"
     Site            139..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54852.1)"
     CDS             1..163
                     /gene="EMP3"
                     /gene_synonym="YMP"
                     /coded_by="NM_001425.3:75..566"
                     /db_xref="CCDS:CCDS12715.1"
                     /db_xref="GeneID:2014"
                     /db_xref="HGNC:HGNC:3335"
                     /db_xref="MIM:602335"
ORIGIN      
        1 msllllvvsa lhililillf vatldkswwt lpgkeslnlw ydctwnndtk twacsnvsen
       61 gwlkavqvlm vlslilccls filfmfqlyt mrrgglfyat glcqlctsva vftgaliyai
      121 haeeilekhp rggsfgycfa lawvafplal vsgiiyihlr kre
//
LOCUS       NP_001355186             131 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 234 isoform 4 precursor [Mus musculus].
ACCESSION   NP_001355186
VERSION     NP_001355186.1
DBSOURCE    REFSEQ: accession NM_001368257.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Tang,T., Li,L., Tang,J., Li,Y., Lin,W.Y., Martin,F., Grant,D.,
            Solloway,M., Parker,L., Ye,W., Forrest,W., Ghilardi,N., Oravecz,T.,
            Platt,K.A., Rice,D.S., Hansen,G.M., Abuin,A., Eberhart,D.E.,
            Godowski,P., Holt,K.H., Peterson,A., Zambrowicz,B.P. and de
            Sauvage,F.J.
  TITLE     A mouse knockout library for secreted and transmembrane proteins
  JOURNAL   Nat Biotechnol 28 (7), 749-755 (2010)
   PUBMED   20562862
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL671759.10.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR9219381.167410.1, BY278842.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 63.26 cM"
     Protein         1..131
                     /product="transmembrane protein 234 isoform 4 precursor"
                     /calculated_mol_wt=11480
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2340
     Region          18..117
                     /region_name="TMEM234"
                     /note="Putative transmembrane family 234; cl46810"
                     /db_xref="CDD:481150"
     CDS             1..131
                     /gene="Tmem234"
                     /gene_synonym="1500002D11Rik; 2510006D16Rik;
                     4933407D05Rik"
                     /coded_by="NM_001368257.1:37..432"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS89832.1"
                     /db_xref="GeneID:76799"
                     /db_xref="MGI:MGI:1924049"
ORIGIN      
        1 maaswgqvla lvlvaalwgg tqpllkrass gleqvrertw awqllqeika lfgntesgsl
       61 lyyltlastd ltlavpicns laivftlivg kvlgediggk eavagmvlti tgitvcitss
      121 vsktqgqpsh s
//
LOCUS       NP_001129973             666 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 844 [Homo sapiens].
ACCESSION   NP_001129973
VERSION     NP_001129973.1
DBSOURCE    REFSEQ: accession NM_001136501.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK098117.1, AL832297.1 and AC022415.5.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK098117.1, AL832297.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000439326.8/ ENSP00000392024.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..666
                     /product="zinc finger protein 844"
                     /calculated_mol_wt=76803
     Region          3..44
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          73..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08AG5.1)"
     Region          <102..327
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          106..125
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          143..163
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          171..191
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          199..219
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          215..236
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          227..247
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(232,234,236,238..239,242..243,246,260,262,266..267,
                     270..271,274,288,290,292,294..295,298..299,302)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          239..262
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          255..275
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          267..290
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          283..303
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          295..320
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          311..331
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          339..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..666
                     /gene="ZNF844"
                     /coded_by="NM_001136501.3:144..2144"
                     /db_xref="CCDS:CCDS45985.1"
                     /db_xref="GeneID:284391"
                     /db_xref="HGNC:HGNC:25932"
ORIGIN      
        1 mdlvafedva vnftqeewsl ldpsqknlyr evmqetlrnl asigekwkdq niedqyknpr
       61 nnlrsllger vdenteenhc getssqipdd tlnkktspgv kscessvcge vfvghsslnr
      121 hiradtahkp seyqeygqep ykcqqrkkaf rchpsfqmqe kahtgeklyd ckecgktfis
      181 hssiqrhmim hngdgtykck fcgkacpcls iylihervht gekpykckqc gkafsystsl
      241 qiherthtge kpyeckecgk afgspnslye hrrthtgekp yeckqcgkaf rwfhsfqihe
      301 rthseekaye ctkcgkafkc psylcrhevt hsgkkpceck qcgkalsyln fqrhmkmhtr
      361 mrpykcktve kplilpvrfe dmkeltlern lmnastvvkp sivpvpftim kgltlernpm
      421 nvssvvkpsf lplpfdimkg ltlernrmsv snvgkpsdlp htfkcmeglt lkrnpmnvss
      481 vvkpsffplp fdimkgltle rnpmsvsnvg kpshlphtfk cmkgltlesn cmnlnnvkkp
      541 ldlsetfkfm krhtlernpi rnmekhstis lpfkymqqct edrmpmnvks vtkhsylprs
      601 feymqehtle rnpmnvrnae krsiifllcv ytkgctlern hinvrivgkh svclvpfvdi
      661 kgltle
//
LOCUS       NP_001030017             601 aa            linear   PRI 27-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase-like 6 [Homo
            sapiens].
ACCESSION   NP_001030017 XP_497981
VERSION     NP_001030017.2
DBSOURCE    REFSEQ: accession NM_001034845.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Diaz Ramirez,J., Alvarez-Herms,J., Castaneda-Babarro,A.,
            Larruskain,J., Ramirez de la Piscina,X., Borisov,O.V.,
            Semenova,E.A., Kostryukova,E.S., Kulemin,N.A., Andryushchenko,O.N.,
            Larin,A.K., Andryushchenko,L.B., Generozov,E.V., Ahmetov,I.I. and
            Odriozola,A.
  TITLE     The GALNTL6 Gene rs558129 Polymorphism Is Associated With Power
            Performance
  JOURNAL   J Strength Cond Res 34 (11), 3031-3036 (2020)
   PUBMED   33105351
  REMARK    GeneRIF: The GALNTL6 Gene rs558129 Polymorphism Is Associated With
            Power Performance.
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Raman,J., Guan,Y., Perrine,C.L., Gerken,T.A. and Tabak,L.A.
  TITLE     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
            N-acetylgalactosaminyltransferases: completion of the family tree
  JOURNAL   Glycobiology 22 (6), 768-777 (2012)
   PUBMED   22186971
  REMARK    Erratum:[Glycobiology. 2015 Apr;25(4):465. doi:
            10.1093/glycob/cwv003. PMID: 25715345]
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Peng,C., Togayachi,A., Kwon,Y.D., Xie,C., Wu,G., Zou,X., Sato,T.,
            Ito,H., Tachibana,K., Kubota,T., Noce,T., Narimatsu,H. and Zhang,Y.
  TITLE     Identification of a novel human UDP-GalNAc transferase with unique
            catalytic activity and expression profile
  JOURNAL   Biochem Biophys Res Commun 402 (4), 680-686 (2010)
   PUBMED   20977886
  REMARK    GeneRIF: a novel member of the human ppGalNAc-T family,
            ppGalNAc-T20, which has high homology with human ppGalNAc-T10 was
            identified.
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
            David,S.P., Niaura,R. and Lerman,C.
  TITLE     Molecular genetics of successful smoking cessation: convergent
            genome-wide association study results
  JOURNAL   Arch Gen Psychiatry 65 (6), 683-693 (2008)
   PUBMED   18519826
  REMARK    GeneRIF: Clinical trial and genome-wide association study of
            gene-disease association, gene-environment interaction, and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025561.6, AJ626725.1, BX108658.1 and AC131952.1.
            
            On Jul 10, 2008 this sequence version replaced NP_001030017.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047551.1, SRR1660803.31102.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMN03465404
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000506823.6/ ENSP00000423313.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q34.1"
     Protein         1..601
                     /product="polypeptide
                     N-acetylgalactosaminyltransferase-like 6"
                     /EC_number="2.4.1.41"
                     /note="GalNAc transferase 17; UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase 17; GaNTase 17;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase-like 6; polypeptide
                     GalNAc transferase-like 6;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 20; galNAc-T17;
                     pp-GaNTase 17; polypeptide GalNAc transferase 17;
                     protein-UDP acetylgalactosaminyltransferase 17; putative
                     polypeptide N-acetylgalactosaminyltransferase 17"
                     /calculated_mol_wt=69657
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q49A17.2)"
     Region          139..248
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q49A17.2)"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q49A17.2)"
     Region          143..438
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(147..149,151,180,209,212,216,232..234,314..315,
                     337..338,340,365,368,373)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(232,234,365)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          306..368
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q49A17.2)"
     Region          449..596
                     /region_name="beta-trefoil_Ricin_GALNTL6"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide
                     N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and
                     similar proteins; cd23477"
                     /db_xref="CDD:467355"
     Site            order(520,531,534,538..539)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467355"
     Site            588
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q49A17.2)"
     CDS             1..601
                     /gene="GALNTL6"
                     /gene_synonym="GalNAc-T6L; GALNACT20; GALNT17"
                     /coded_by="NM_001034845.3:757..2562"
                     /db_xref="CCDS:CCDS34104.1"
                     /db_xref="GeneID:442117"
                     /db_xref="HGNC:HGNC:33844"
                     /db_xref="MIM:615138"
ORIGIN      
        1 mkrkqkrflq mtllftvali flpnvglwsl ykdkhlvksa epgeqqtfpl glgdgqfysw
       61 tdglrrkdwh dyesiqkeam rsgkgehgkp yplteedhdd sayrengfni fvsnnialer
      121 slpdirhanc khkmylerlp ntsiiipfhn egwtsllrti hsiinrtpgs liaeiilvdd
      181 fserehlkdk leeymarfsk vrivrtkkre glirtrllga smargevltf ldshcevnvn
      241 wlppllnqia lnhktivcpm idvidhnhfg yeaqagdamr gafdwemyyk ripippelqr
      301 adpsdpfesp vmagglfavd rkwfwelggy dpgleiwgge qyeisfkvwm cggemfdvpc
      361 srvghiyrky vpykvpsgts larnlkrvae twmdefaeyi yqrrpeyrhl stgdisaqke
      421 lrkqlkckdf kwfmaavawd vpkyyppvep ppaawgeirn vaanlcvdsk hgatgtelrl
      481 dicvkdgser twsheqlftf gwredirpge plhtrkfcfd aishnspvtl ydchgmkgnq
      541 lwgyrkdrtl fhpvsnscmd cnpaekkifm arcdplsetq qwifehinmt vlekfnhhan
      601 s
//
LOCUS       NP_006538                579 aa            linear   PRI 27-APR-2025
DEFINITION  insulin-like growth factor 2 mRNA-binding protein 3 [Homo sapiens].
ACCESSION   NP_006538
VERSION     NP_006538.2
DBSOURCE    REFSEQ: accession NM_006547.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Fujiwara,Y., Takahashi,R.U., Saito,M., Umakoshi,M., Shimada,Y.,
            Koyama,K., Yatabe,Y., Watanabe,S.I., Koyota,S., Minamiya,Y.,
            Tahara,H., Kono,K., Shiraishi,K., Kohno,T., Goto,A. and Tsuchiya,N.
  TITLE     Oncofetal IGF2BP3-mediated control of microRNA structural diversity
            in the malignancy of early-stage lung adenocarcinoma
  JOURNAL   Proc Natl Acad Sci U S A 121 (36), e2407016121 (2024)
   PUBMED   39196622
  REMARK    GeneRIF: Oncofetal IGF2BP3-mediated control of microRNA structural
            diversity in the malignancy of early-stage lung adenocarcinoma.
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Dai,F., Zhang,Y., Deng,Z., Zhang,J., Wang,R., Chen,J., Yang,D.,
            Mao,S., Liu,H., Cheng,Y. and Hu,M.
  TITLE     IGF2BP3 participates in the pathogenesis of recurrent spontaneous
            abortion by regulating ferroptosis
  JOURNAL   J Reprod Immunol 165, 104271 (2024)
   PUBMED   39054220
  REMARK    GeneRIF: IGF2BP3 participates in the pathogenesis of recurrent
            spontaneous abortion by regulating ferroptosis.
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Liu,C., Dou,X., Zhao,Y., Zhang,L., Zhang,L., Dai,Q., Liu,J., Wu,T.,
            Xiao,Y. and He,C.
  TITLE     IGF2BP3 promotes mRNA degradation through internal m7G modification
  JOURNAL   Nat Commun 15 (1), 7421 (2024)
   PUBMED   39198433
  REMARK    GeneRIF: IGF2BP3 promotes mRNA degradation through internal m[7]G
            modification.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Gong,S., Liu,H., Gou,H. and Sun,W.
  TITLE     METTL5: A Potential Biomarker for Nonsmall Cell Lung Cancer That
            Promotes Cancer Cell Proliferation by Interacting with IGF2BP3
  JOURNAL   Genet Test Mol Biomarkers 28 (8), 311-321 (2024)
   PUBMED   39023781
  REMARK    GeneRIF: METTL5: A Potential Biomarker for Nonsmall Cell Lung
            Cancer That Promotes Cancer Cell Proliferation by Interacting with
            IGF2BP3.
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Salum,S.O.R., Candido,E.B., Domingues,M.A.C., Ojopi,E.P.B.,
            Tonon,A.F.S. and da Silva-Filho,A.L.
  TITLE     Association of insulin-like growth factor II mrna-binding protein 3
            (IMP3) expression with prognostic and morphological factors in
            endometrial cancer
  JOURNAL   Rev Bras Ginecol Obstet 46 (2024)
   PUBMED   39176196
  REMARK    GeneRIF: Association of insulin-like growth factor II mrna-binding
            protein 3 (IMP3) expression with prognostic and morphological
            factors in endometrial cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Yaniv,K. and Yisraeli,J.K.
  TITLE     The involvement of a conserved family of RNA binding proteins in
            embryonic development and carcinogenesis
  JOURNAL   Gene 287 (1-2), 49-54 (2002)
   PUBMED   11992722
  REMARK    Review article
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Zhang,J.Y., Chan,E.K., Peng,X.X., Lu,M., Wang,X., Mueller,F. and
            Tan,E.M.
  TITLE     Autoimmune responses to mRNA binding proteins p62 and Koc in
            diverse malignancies
  JOURNAL   Clin Immunol 100 (2), 149-156 (2001)
   PUBMED   11465943
REFERENCE   8  (residues 1 to 579)
  AUTHORS   Mueller-Pillasch,F., Pohl,B., Wilda,M., Lacher,U., Beil,M.,
            Wallrapp,C., Hameister,H., Knochel,W., Adler,G. and Gress,T.M.
  TITLE     Expression of the highly conserved RNA binding protein KOC in
            embryogenesis
  JOURNAL   Mech Dev 88 (1), 95-99 (1999)
   PUBMED   10525192
REFERENCE   9  (residues 1 to 579)
  AUTHORS   Nielsen,J., Christiansen,J., Lykke-Andersen,J., Johnsen,A.H.,
            Wewer,U.M. and Nielsen,F.C.
  TITLE     A family of insulin-like growth factor II mRNA-binding proteins
            represses translation in late development
  JOURNAL   Mol Cell Biol 19 (2), 1262-1270 (1999)
   PUBMED   9891060
REFERENCE   10 (residues 1 to 579)
  AUTHORS   Mueller-Pillasch,F., Lacher,U., Wallrapp,C., Micha,A.,
            Zimmerhackl,F., Hameister,H., Varga,G., Friess,H., Buchler,M.,
            Beger,H.G., Vila,M.R., Adler,G. and Gress,T.M.
  TITLE     Cloning of a gene highly overexpressed in cancer coding for a novel
            KH-domain containing protein
  JOURNAL   Oncogene 14 (22), 2729-2733 (1997)
   PUBMED   9178771
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079780.6, AC021876.5 and
            AC005082.3.
            
            On May 16, 2003 this sequence version replaced NP_006538.1.
            
            Summary: The protein encoded by this gene is primarily found in the
            nucleolus, where it can bind to the 5' UTR of the insulin-like
            growth factor II leader 3 mRNA and may repress translation of
            insulin-like growth factor II during late development. The encoded
            protein contains several KH domains, which are important in RNA
            binding and are known to be involved in RNA synthesis and
            metabolism. A pseudogene exists on chromosome 7, and there are
            putative pseudogenes on other chromosomes. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF117108.1, U97188.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258729.8/ ENSP00000258729.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.3"
     Protein         1..579
                     /product="insulin-like growth factor 2 mRNA-binding
                     protein 3"
                     /note="cancer/testis antigen 98; IGF-II mRNA-binding
                     protein 3; KH domain containing protein overexpressed in
                     cancer; VICKZ family member 3; IGF2 mRNA-binding protein
                     3"
                     /calculated_mol_wt=63574
     Region          1..77
                     /region_name="RRM1_IGF2BP3"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     insulin-like growth factor 2 mRNA-binding protein 3
                     (IGF2BP3); cd12627"
                     /db_xref="CDD:410036"
     Region          81..156
                     /region_name="RRM2_IGF2BP3"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     insulin-like growth factor 2 mRNA-binding protein 3
                     (IGF2BP3); cd12630"
                     /db_xref="CDD:410039"
     Region          160..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00425.2)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O00425.2)"
     Region          197..272
                     /region_name="KH-I_IGF2BP3_rpt1"
                     /note="first type I K homology (KH) RNA-binding domain
                     found in insulin-like growth factor 2 mRNA-binding protein
                     3 (IGF2BP3) and similar proteins; cd22492"
                     /db_xref="CDD:411920"
     Site            order(205,207..209,211..215,218..219,222..223,228..231)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411920"
     Region          275..369
                     /region_name="KH-I"
                     /note="K homology (KH) RNA-binding domain, type I;
                     cl00098"
                     /db_xref="CDD:469614"
     Region          402..479
                     /region_name="KH-I_IGF2BP3_rpt3"
                     /note="third type I K homology (KH) RNA-binding domain
                     found in insulin-like growth factor 2 mRNA-binding protein
                     3 (IGF2BP3) and similar proteins; cd22498"
                     /db_xref="CDD:411926"
     Site            order(417..419,421..425,428..429,439..443,452)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:411926"
     Region          487..562
                     /region_name="KH-I"
                     /note="K homology (KH) RNA-binding domain, type I;
                     cl00098"
                     /db_xref="CDD:469614"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00425.2)"
     CDS             1..579
                     /gene="IGF2BP3"
                     /gene_synonym="CT98; IMP-3; IMP3; KOC; KOC1; VICKZ3"
                     /coded_by="NM_006547.3:382..2121"
                     /db_xref="CCDS:CCDS5382.1"
                     /db_xref="GeneID:10643"
                     /db_xref="HGNC:HGNC:28868"
                     /db_xref="MIM:608259"
ORIGIN      
        1 mnklyignls enaapsdles ifkdakipvs gpflvktgya fvdcpdeswa lkaiealsgk
       61 ielhgkpiev ehsvpkrqri rklqirnipp hlqwevldsl lvqygvvesc eqvntdseta
      121 vvnvtysskd qarqaldkln gfqlenftlk vayipdemaa qqnplqqprg rrglgqrgss
      181 rqgspgsvsk qkpcdlplrl lvptqfvgai igkegatirn itkqtqskid vhrkenagaa
      241 eksitilstp egtsaacksi leimhkeaqd ikfteeiplk ilahnnfvgr ligkegrnlk
      301 kieqdtdtki tisplqeltl ynpertitvk gnvetcakae eeimkkires yendiasmnl
      361 qahlipglnl nalglfppts gmppptsgpp samtppypqf eqsetetvhl fipalsvgai
      421 igkqgqhikq lsrfagasik iapaeapdak vrmviitgpp eaqfkaqgri ygkikeenfv
      481 spkeevklea hirvpsfaag rvigkggktv nelqnlssae vvvprdqtpd endqvvvkit
      541 ghfyacqvaq rkiqeiltqv kqhqqqkalq sgppqsrrk
//
LOCUS       NP_038803                117 aa            linear   ROD 27-APR-2025
DEFINITION  protein TCL1B2 [Mus musculus].
ACCESSION   NP_038803
VERSION     NP_038803.1
DBSOURCE    REFSEQ: accession NM_013775.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Yu,C., Ji,S.Y., Dang,Y.J., Sha,Q.Q., Yuan,Y.F., Zhou,J.J.,
            Yan,L.Y., Qiao,J., Tang,F. and Fan,H.Y.
  TITLE     Oocyte-expressed yes-associated protein is a key activator of the
            early zygotic genome in mouse
  JOURNAL   Cell Res 26 (3), 275-287 (2016)
   PUBMED   26902285
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Hallas,C., Pekarsky,Y., Itoyama,T., Varnum,J., Bichi,R.,
            Rothstein,J.L. and Croce,C.M.
  TITLE     Genomic analysis of human and mouse TCL1 loci reveals a complex of
            tightly clustered genes
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14418-14423 (1999)
   PUBMED   10588720
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK139548.1 and AF195489.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF195489.1, DV662615.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN01164134
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 55.19 cM"
     Protein         1..117
                     /product="protein TCL1B2"
                     /calculated_mol_wt=13541
     Region          1..116
                     /region_name="TCL1_MTCP1"
                     /note="TCL1/MTCP1 family; pfam01840"
                     /db_xref="CDD:460358"
     CDS             1..117
                     /gene="Tcl1b2"
                     /coded_by="NM_013775.2:72..425"
                     /db_xref="CCDS:CCDS36544.1"
                     /db_xref="GeneID:27381"
                     /db_xref="MGI:MGI:1351609"
ORIGIN      
        1 maaagfyppr llpqvlistg pgfyedehhr lwmvakletc shspycnkie tcvtvhlwqm
       61 trypqepapy npmnynflpm twrlasmnty rgtdamhwrl lnhsqvgdtv qlilmle
//
LOCUS       NP_001357060             594 aa            linear   PRI 27-APR-2025
DEFINITION  APOBEC1 complementation factor isoform 2 [Homo sapiens].
ACCESSION   NP_001357060 XP_005269777
VERSION     NP_001357060.1
DBSOURCE    REFSEQ: accession NM_001370131.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Liu,Y., Yang,J., Weng,D. and Xie,Y.
  TITLE     A1CF Binding to the p65 Interaction Site on NKRF Decreased IFN-beta
            Expression and p65 Phosphorylation (Ser536) in Renal Carcinoma
            Cells
  JOURNAL   Int J Mol Sci 25 (7), 3576 (2024)
   PUBMED   38612387
  REMARK    GeneRIF: A1CF Binding to the p65 Interaction Site on NKRF Decreased
            IFN-beta Expression and p65 Phosphorylation (Ser536) in Renal
            Carcinoma Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Liu,Q., Chen,C.Y. and Chen,G.L.
  TITLE     High APOBEC1 Complementation Factor Expression Positively Modulates
            the Proliferation, Invasion, and Migration of Endometrial Cancer
            Cells Through Regulating P53/P21 Signaling Pathway
  JOURNAL   Cancer Biother Radiopharm 37 (9), 750-758 (2022)
   PUBMED   32818382
  REMARK    GeneRIF: High APOBEC1 Complementation Factor Expression Positively
            Modulates the Proliferation, Invasion, and Migration of Endometrial
            Cancer Cells Through Regulating P53/P21 Signaling Pathway.
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Kawaguchi,M., Nakayama,A., Aoyagi,Y., Nakamura,T., Shimizu,S.,
            Kawamura,Y., Takao,M., Tamura,T., Hishida,A., Nagayoshi,M.,
            Nagase,M., Ooyama,K., Ooyama,H., Shinomiya,N. and Matsuo,H.
  TITLE     Both variants of A1CF and BAZ1B genes are associated with gout
            susceptibility: a replication study and meta-analysis in a Japanese
            population
  JOURNAL   Hum Cell 34 (2), 293-299 (2021)
   PUBMED   33517564
  REMARK    GeneRIF: Both variants of A1CF and BAZ1B genes are associated with
            gout susceptibility: a replication study and meta-analysis in a
            Japanese population.
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Song,Y., Shao,L., Xue,Y., Ruan,X., Liu,X., Yang,C., Zheng,J.,
            Shen,S., Chen,J., Li,Z. and Liu,Y.
  TITLE     Inhibition of the aberrant A1CF-FAM224A-miR-590-3p-ZNF143 positive
            feedback loop attenuated malignant biological behaviors of glioma
            cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 248 (2019)
   PUBMED   31186064
  REMARK    GeneRIF: this study revealed that A1CF can upregulate the
            expression of FAM224A via strengthening its stability, which in
            turn, influenced the negative modulation of miR-590-3p on
            transcription factor ZNF143.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   7  (residues 1 to 594)
  AUTHORS   Chester,A., Scott,J., Anant,S. and Navaratnam,N.
  TITLE     RNA editing: cytidine to uridine conversion in apolipoprotein B
            mRNA
  JOURNAL   Biochim Biophys Acta 1494 (1-2), 1-13 (2000)
   PUBMED   11072063
  REMARK    Review article
REFERENCE   8  (residues 1 to 594)
  AUTHORS   Yang,Y., Sowden,M.P. and Smith,H.C.
  TITLE     Induction of cytidine to uridine editing on cytoplasmic
            apolipoprotein B mRNA by overexpressing APOBEC-1
  JOURNAL   J Biol Chem 275 (30), 22663-22669 (2000)
   PUBMED   10833526
REFERENCE   9  (residues 1 to 594)
  AUTHORS   Lellek,H., Kirsten,R., Diehl,I., Apostel,F., Buck,F. and Greeve,J.
  TITLE     Purification and molecular cloning of a novel essential component
            of the apolipoprotein B mRNA editing enzyme-complex
  JOURNAL   J Biol Chem 275 (26), 19848-19856 (2000)
   PUBMED   10781591
REFERENCE   10 (residues 1 to 594)
  AUTHORS   Mehta,A., Kinter,M.T., Sherman,N.E. and Driscoll,D.M.
  TITLE     Molecular cloning of apobec-1 complementation factor, a novel
            RNA-binding protein involved in the editing of apolipoprotein B
            mRNA
  JOURNAL   Mol Cell Biol 20 (5), 1846-1854 (2000)
   PUBMED   10669759
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL512366.12 and AL589794.7.
            
            On Apr 26, 2019 this sequence version replaced XP_005269777.1.
            
            Summary: Mammalian apolipoprotein B mRNA undergoes site-specific C
            to U deamination, which is mediated by a multi-component enzyme
            complex containing a minimal core composed of APOBEC-1 and a
            complementation factor encoded by this gene. The gene product has
            three non-identical RNA recognition motifs and belongs to the hnRNP
            R family of RNA-binding proteins. It has been proposed that this
            complementation factor functions as an RNA-binding subunit and
            docks APOBEC-1 to deaminate the upstream cytidine. Studies suggest
            that the protein may also be involved in other RNA editing or RNA
            processing events. Several transcript variants encoding a few
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2010].
            
            Transcript Variant: This variant (8) differs in the 5' UTR and
            coding sequence compared to variant 5. The resulting isoform (2)
            has a shorter and distinct N-terminus compared to isoform 4.
            Variants 2 and 8 encode the same isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1386846.1,
                                           SRR14038193.2826319.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.23"
     Protein         1..594
                     /product="APOBEC1 complementation factor isoform 2"
                     /note="APOBEC-1 stimulating protein; apo-B RNA editing
                     protein; apobec-1 complementation factor (ACF) (ASP)"
                     /calculated_mol_wt=65072
     Region          2..594
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Region          360..409
                     /region_name="Required for nuclear localization.
                     /evidence=ECO:0000269|PubMed:12896982"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ94.1)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ94.1)"
     CDS             1..594
                     /gene="A1CF"
                     /gene_synonym="ACF; ACF64; ACF65; APOBEC1CF; ASP"
                     /coded_by="NM_001370131.1:93..1877"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS7242.1"
                     /db_xref="GeneID:29974"
                     /db_xref="HGNC:HGNC:24086"
                     /db_xref="MIM:618199"
ORIGIN      
        1 mesnhksgdg lsgtqkeaal ralvqrtgys lvqengqrky ggpppgwdaa ppergceifi
       61 gklprdlfed eliplcekig kiyemrmmmd fngnnrgyaf vtfsnkveak naikqlnnye
      121 irngrllgvc asvdncrlfv ggipktkkre eilsemkkvt egvvdvivyp saadktknrg
      181 fafveyeshr aaamarrkll pgriqlwghg iavdwaepev evdedtmssv kilyvrnlml
      241 stseemieke fnnikpgave rvkkirdyaf vhfsnredav eamkalngkv ldgspievtl
      301 akpvdkdsyv rytrgtggrg tmlqgeytys lgqvydpttt ylgapvfyap qtyaaipslh
      361 fpatkghlsn raiirapsvr eiymnvpvga agvrglggrg ylaytglgrg yqvkgdkred
      421 klydilpgme ltpmnpvtlk pqgiklapqi leeicqknnw gqpvyqlhsa igqdqrqlfl
      481 ykitipalas qnpaihpftp pklsafvdea ktyaaeytlq tlgiptdggd gtmataaaaa
      541 tafpgyavpn atapvsaaql kqavtlgqdl aayttyevyp tfavtargdg ygtf
//
LOCUS       NP_004115                142 aa            linear   PRI 27-APR-2025
DEFINITION  glia maturation factor beta [Homo sapiens].
ACCESSION   NP_004115
VERSION     NP_004115.1
DBSOURCE    REFSEQ: accession NM_004124.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Sun,W., Wang,J., Liu,C., Gao,F., Ou,Q., Tian,H., Xu,J., Zhang,J.,
            Li,J., Xu,J., Jia,S., Zhang,J., Xu,G., Huang,J., Jin,C. and Lu,L.
  TITLE     SUMOylation of GMFB regulates its stability and function in retinal
            pigment epithelial cells under hyperglycemia
  JOURNAL   Int J Biol Macromol 268 (Pt 2), 131678 (2024)
   PUBMED   38657921
  REMARK    GeneRIF: SUMOylation of GMFB regulates its stability and function
            in retinal pigment epithelial cells under hyperglycemia.
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Bellver-Sanchis,A., Geng,Q., Navarro,G., Avila-Lopez,P.A.,
            Companys-Alemany,J., Marsal-Garcia,L., Larramona-Arcas,R., Miro,L.,
            Perez-Bosque,A., Ortuno-Sahagun,D., Banerjee,D.R., Choudhary,B.S.,
            Soriano,F.X., Poulard,C., Pallas,M., Du,H.N. and Grinan-Ferre,C.
  TITLE     G9a Inhibition Promotes Neuroprotection through GMFB Regulation in
            Alzheimer's Disease
  JOURNAL   Aging Dis 15 (1), 311-337 (2024)
   PUBMED   37307824
  REMARK    GeneRIF: G9a Inhibition Promotes Neuroprotection through GMFB
            Regulation in Alzheimer's Disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Thangavel,R., Kaur,H., Dubova,I., Selvakumar,G.P., Ahmed,M.E.,
            Raikwar,S.P., Govindarajan,R. and Kempuraj,D.
  TITLE     Parkinson's Disease Dementia Patients: Expression of Glia
            Maturation Factor in the Brain
  JOURNAL   Int J Mol Sci 25 (2), 1182 (2024)
   PUBMED   38256254
  REMARK    GeneRIF: Parkinson's Disease Dementia Patients: Expression of Glia
            Maturation Factor in the Brain.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Liu,J., Hou,Y., Lin,L., Yu,N. and Zhang,Y.
  TITLE     MicroRNA-5195-3p alleviates high glucose-induced injury in human
            ARPE-19 cells by targeting GMFB
  JOURNAL   PLoS One 16 (11), e0260071 (2021)
   PUBMED   34793551
  REMARK    GeneRIF: MicroRNA-5195-3p alleviates high glucoseinduced injury in
            human ARPE-19 cells by targeting GMFB.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Selvakumar,G.P., Iyer,S.S., Kempuraj,D., Raju,M., Thangavel,R.,
            Saeed,D., Ahmed,M.E., Zahoor,H., Raikwar,S.P., Zaheer,S. and
            Zaheer,A.
  TITLE     Glia Maturation Factor Dependent Inhibition of Mitochondrial
            PGC-1alpha Triggers Oxidative Stress-Mediated Apoptosis in N27 Rat
            Dopaminergic Neuronal Cells
  JOURNAL   Mol Neurobiol 55 (9), 7132-7152 (2018)
   PUBMED   29383690
  REMARK    GeneRIF: GMF acts as an important upstream regulator of PGC-1alpha
            in promoting dopaminergic neuronal death through its effect on
            oxidative stress-mediated apoptosis.
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Asai,K., Fujita,K., Yamamoto,M., Hotta,T., Morikawa,M., Kokubo,M.,
            Moriyama,A. and Kato,T.
  TITLE     Isolation of novel human cDNA (hGMF-gamma) homologous to Glia
            Maturation Factor-beta gene
  JOURNAL   Biochim Biophys Acta 1396 (3), 242-244 (1998)
   PUBMED   9545571
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Lim,R. and Zaheer,A.
  TITLE     In vitro enhancement of p38 mitogen-activated protein kinase
            activity by phosphorylated glia maturation factor
  JOURNAL   J Biol Chem 271 (38), 22953-22956 (1996)
   PUBMED   8798479
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Zaheer,A. and Lim,R.
  TITLE     In vitro inhibition of MAP kinase (ERK1/ERK2) activity by
            phosphorylated glia maturation factor (GMF)
  JOURNAL   Biochemistry 35 (20), 6283-6288 (1996)
   PUBMED   8639570
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Lim,R. and Zaheer,A.
  TITLE     Phorbol ester stimulates rapid intracellular phosphorylation of
            glia maturation factor
  JOURNAL   Biochem Biophys Res Commun 211 (3), 928-934 (1995)
   PUBMED   7598724
REFERENCE   10 (residues 1 to 142)
  AUTHORS   Kaplan,R., Zaheer,A., Jaye,M. and Lim,R.
  TITLE     Molecular cloning and expression of biologically active human glia
            maturation factor-beta
  JOURNAL   J Neurochem 57 (2), 483-490 (1991)
   PUBMED   1712830
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI547506.1, AB001106.1, BG622077.1, AI342496.1 and AL359792.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.257394.1,
                                           SRR1660807.79112.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358056.8/ ENSP00000350757.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.2"
     Protein         1..142
                     /product="glia maturation factor beta"
                     /note="GMF-beta"
                     /calculated_mol_wt=16582
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P60983.2)"
     Region          9..130
                     /region_name="ADF_GMF-beta_like"
                     /note="ADF-homology domain of glia maturation factor beta
                     and related proteins; cd11283"
                     /db_xref="CDD:200439"
     CDS             1..142
                     /gene="GMFB"
                     /gene_synonym="GMF"
                     /coded_by="NM_004124.3:54..482"
                     /db_xref="CCDS:CCDS9718.1"
                     /db_xref="GeneID:2764"
                     /db_xref="HGNC:HGNC:4373"
                     /db_xref="MIM:601713"
ORIGIN      
        1 mseslvvcdv aedlveklrk frfrketnna aiimkidkdk rlvvldeele gispdelkde
       61 lperqprfiv ysykyqhddg rvsyplcfif sspvgckpeq qmmyagsknk lvqtaeltkv
      121 feirntedlt eewlreklgf fh
//
LOCUS       NP_001349959             273 aa            linear   ROD 27-APR-2025
DEFINITION  syntaxin-16 isoform f [Mus musculus].
ACCESSION   NP_001349959 XP_006499498
VERSION     NP_001349959.1
DBSOURCE    REFSEQ: accession NM_001363030.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Hara,Y., Katsuyama,T., Fukaya,M., Sugawara,T., Shiroshima,T.,
            Sadakata,T., Osumi,N. and Sakagami,H.
  TITLE     ADP Ribosylation Factor 4 (Arf4) Regulates Radial Migration through
            N-Cadherin Trafficking during Cerebral Cortical Development
  JOURNAL   eNeuro 10 (11) (2023)
   PUBMED   37848288
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Sundberg,J.P., Dadras,S.S., Silva,K.A., Kennedy,V.E., Garland,G.,
            Murray,S.A., Sundberg,B.A., Schofield,P.N. and Pratt,C.H.
  TITLE     Systematic screening for skin, hair, and nail abnormalities in a
            large-scale knockout mouse program
  JOURNAL   PLoS One 12 (7), e0180682 (2017)
   PUBMED   28700664
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Beaton,N., Rudigier,C., Moest,H., Muller,S., Mrosek,N., Roder,E.,
            Rudofsky,G., Rulicke,T., Ukropec,J., Ukropcova,B., Augustin,R.,
            Neubauer,H. and Wolfrum,C.
  TITLE     TUSC5 regulates insulin-mediated adipose tissue glucose uptake by
            modulation of GLUT4 recycling
  JOURNAL   Mol Metab 4 (11), 795-810 (2015)
   PUBMED   26629404
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Chua,C.E. and Tang,B.L.
  TITLE     Syntaxin 16 is enriched in neuronal dendrites and may have a role
            in neurite outgrowth
  JOURNAL   Mol Membr Biol 25 (1), 35-45 (2008)
   PUBMED   17852734
  REMARK    GeneRIF: Syntaxin 16 may thus play a role in neurite outgrowth and
            perhaps other specific dendritic anterograde/retrograde traffic.
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Frohlich,L.F., Bastepe,M., Ozturk,D., Abu-Zahra,H. and Juppner,H.
  TITLE     Lack of Gnas epigenetic changes and pseudohypoparathyroidism type
            Ib in mice with targeted disruption of syntaxin-16
  JOURNAL   Endocrinology 148 (6), 2925-2935 (2007)
   PUBMED   17317779
  REMARK    GeneRIF: Mice genetically altered to carry the equivalent of
            STX16del4-6 contributing to pseudohypoparathyroidism type 1b.
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Nishimura,M., Yokoi,N., Miki,T., Horikawa,Y., Yoshioka,H.,
            Takeda,J., Ohara,O. and Seino,S.
  TITLE     Construction of a multi-functional cDNA library specific for mouse
            pancreatic islets and its application to microarray
  JOURNAL   DNA Res 11 (5), 315-323 (2004)
   PUBMED   15747579
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL669896.7 and AK029571.1.
            
            On May 5, 2018 this sequence version replaced XP_006499498.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (f) is
            shorter at the N-terminus compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK029571.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 97.85 cM"
     Protein         1..273
                     /product="syntaxin-16 isoform f"
                     /calculated_mol_wt=31016
     Region          20..249
                     /region_name="COG5325"
                     /note="t-SNARE complex subunit, syntaxin [Intracellular
                     trafficking and secretion]"
                     /db_xref="CDD:227635"
     Region          181..239
                     /region_name="SNARE_syntaxin16"
                     /note="SNARE motif of syntaxin 16; cd15845"
                     /db_xref="CDD:277198"
     Site            order(182,184..185,187..192,194..196,198..199,201..203,
                     205..206,208..210,212..213,215..220,222..227,229..234,
                     236..238)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277198"
     Site            212
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277198"
     CDS             1..273
                     /gene="Stx16"
                     /gene_synonym="4930401D03; 5430410K23Rik; 6330500A18Rik;
                     Syn16"
                     /coded_by="NM_001363030.1:175..996"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:228960"
                     /db_xref="MGI:MGI:1923396"
ORIGIN      
        1 malvsgisld peaaigvtkr sppkwvdgvd eiqydvgrik qkmkelaslh dkhlnrptld
       61 dsseeehaie ittqevtqlf hrcqravqal psrarracse qeerllrnvv aslaqalqel
      121 stsfrhaqsd ylkrmknree rsqhffdtpv plmddgddat lygqgftddq lvlveqntlm
      181 veerereirq ivqsisdlne ifrdlgamiv eqgtvldrid ynveqscvkt edglkqlhka
      241 eqyqkknrkm lvivilvavi ivllvalvav ksr
//
LOCUS       NP_659399                227 aa            linear   PRI 27-APR-2025
DEFINITION  phosphatidylethanolamine-binding protein 4 precursor [Homo
            sapiens].
ACCESSION   NP_659399
VERSION     NP_659399.2
DBSOURCE    REFSEQ: accession NM_144962.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Huang,R.Q., Chen,F., Jiang,Y.B., Jin,Y.M., Wang,S.Q., Liang,H.H.,
            Chen,Z.P. and Qian,J.
  TITLE     Overexpression of phosphatidylethanolamine-binding protein 4
            (PEBP4) associates with recurrence of meningiomas
  JOURNAL   Clin Neurol Neurosurg 214, 107148 (2022)
   PUBMED   35158167
  REMARK    GeneRIF: Overexpression of phosphatidylethanolamine-binding protein
            4 (PEBP4) associates with recurrence of meningiomas.
REFERENCE   2  (residues 1 to 227)
  AUTHORS   He,P., Zhou,C. and Shen,H.
  TITLE     Diagnostic value of phosphatidylethanolamine binding protein 4
            levels in patients receiving nursing interventions for advanced
            chronic kidney disease
  JOURNAL   J Int Med Res 49 (3), 300060521996179 (2021)
   PUBMED   33752499
  REMARK    GeneRIF: Diagnostic value of phosphatidylethanolamine binding
            protein 4 levels in patients receiving nursing interventions for
            advanced chronic kidney disease.
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Taylor,S., Pieri,K., Nanni,P., Tica,J., Barratt,J. and
            Didangelos,A.
  TITLE     Phosphatidylethanolamine binding protein-4 (PEBP4) is increased in
            IgA nephropathy and is associated with IgA-positive B-cells in
            affected kidneys
  JOURNAL   J Autoimmun 105, 102309 (2019)
   PUBMED   31402200
  REMARK    GeneRIF: PEBP4 colocalised with IgA and CD19.
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Jian,W., Bai,Y., Li,X., Kang,J., Lei,Y. and Xue,Y.
  TITLE     Phosphatidylethanolamine-binding protein 4 promotes the
            epithelial-to-mesenchymal transition in non-small cell lung cancer
            cells by activating the sonic hedgehog signaling pathway
  JOURNAL   J Cell Biochem 120 (4), 5386-5395 (2019)
   PUBMED   30367510
  REMARK    GeneRIF: these results suggest that PEBP4 may promote tumorigenesis
            in non-small cell lung cancer by regulating cell proliferation and
            epithelial-to-mesenchymal transition via activation of the Shh
            signaling pathway.
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Huang,R.Q., Wang,S.Q., Zhu,Q.B., Guo,S.C., Shi,D.L., Chen,F.,
            Fang,Y.C., Chen,R. and Lu,Y.C.
  TITLE     Knockdown of PEBP4 inhibits human glioma cell growth and invasive
            potential via ERK1/2 signaling pathway
  JOURNAL   Mol Carcinog 58 (1), 135-143 (2019)
   PUBMED   30255656
  REMARK    GeneRIF: High PEBP4 expression is associated with glioma cell
            growth and invasiveness.
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Garcia,R., Grindlay,J., Rath,O., Fee,F. and Kolch,W.
  TITLE     Regulation of human myoblast differentiation by PEBP4
  JOURNAL   EMBO Rep 10 (3), 278-284 (2009)
   PUBMED   19197339
  REMARK    GeneRIF: Data show that PEBP4 participates in the control of muscle
            cell differentiation by modulating the activity of MEK and ERK.
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
            David,S.P., Niaura,R. and Lerman,C.
  TITLE     Molecular genetics of successful smoking cessation: convergent
            genome-wide association study results
  JOURNAL   Arch Gen Psychiatry 65 (6), 683-693 (2008)
   PUBMED   18519826
  REMARK    GeneRIF: Clinical trial and genome-wide association study of
            gene-disease association, gene-environment interaction, and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
REFERENCE   8  (residues 1 to 227)
  AUTHORS   Li,P., Wang,X., Li,N., Kong,H., Guo,Z., Liu,S. and Cao,X.
  TITLE     Anti-apoptotic hPEBP4 silencing promotes TRAIL-induced apoptosis of
            human ovarian cancer cells by activating ERK and JNK pathways
  JOURNAL   Int J Mol Med 18 (3), 505-510 (2006)
   PUBMED   16865237
  REMARK    GeneRIF: Silencing of hPEBP4, an important potential target, may be
            a promising approach for the treatment of ovarian cancer.
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   10 (residues 1 to 227)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC037441.12, BF853000.1, AY359109.1, AY037148.1 and AC105046.10.
            
            On Oct 28, 2006 this sequence version replaced NP_659399.1.
            
            Summary: The phosphatidylethanolamine (PE)-binding proteins,
            including PEBP4, are an evolutionarily conserved family of proteins
            with pivotal biologic functions, such as lipid binding and
            inhibition of serine proteases (Wang et al., 2004 [PubMed
            15302887]).[supplied by OMIM, Dec 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.220788.1,
                                           SRR5189655.192308.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145313, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256404.8/ ENSP00000256404.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..227
                     /product="phosphatidylethanolamine-binding protein 4
                     precursor"
                     /note="cousin-of-RKIP 1 protein; protein cousin-of-RKIP 1;
                     epididymis secretory protein Li 300; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=23387
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2365
     mat_peptide     23..227
                     /product="Phosphatidylethanolamine-binding protein 4.
                     /id=PRO_0000023279"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S96.3)"
                     /calculated_mol_wt=23387
     Region          46..197
                     /region_name="PEBP_euk"
                     /note="PhosphatidylEthanolamine-Binding Protein (PEBP)
                     domain present in eukaryotes; cd00866"
                     /db_xref="CDD:176644"
     Site            order(96,110,112,139..142,148,150)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176644"
     Site            169
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:27033522; propagated from
                     UniProtKB/Swiss-Prot (Q96S96.3)"
     Region          188..227
                     /region_name="Important for secretion.
                     /evidence=ECO:0000269|PubMed:27033522"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S96.3)"
     Region          202..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S96.3)"
     CDS             1..227
                     /gene="PEBP4"
                     /gene_synonym="CORK-1; CORK1; GWTM1933; HEL-S-300; hPEBP4;
                     PEBP-4; PRO4408"
                     /coded_by="NM_144962.3:99..782"
                     /db_xref="CCDS:CCDS43724.1"
                     /db_xref="GeneID:157310"
                     /db_xref="HGNC:HGNC:28319"
                     /db_xref="MIM:612473"
ORIGIN      
        1 mgwtmrlvta alllglmmvv tgdedenspc ahealldedt lfcqglevfy pelgnigckv
       61 vpdcnnyrqk itswmepivk fpgavdgaty ilvmvdpdap sraeprqrfw rhwlvtdikg
      121 adlkkgkiqg qelsayqaps ppahsgfhry qffvylqegk visllpkenk trgswkmdrf
      181 lnrfhlgepe astqfmtqny qdsptlqapr erasepkhkn qaeiaac
//
LOCUS       NP_008980                527 aa            linear   PRI 27-APR-2025
DEFINITION  butyrophilin subfamily 2 member A1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_008980
VERSION     NP_008980.1
DBSOURCE    REFSEQ: accession NM_007049.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Yuan,L., Ma,X., Yang,Y., Qu,Y., Li,X., Zhu,X., Ma,W., Duan,J.,
            Xue,J., Yang,H., Huang,J.W., Yi,S., Zhang,M., Cai,N., Zhang,L.,
            Ding,Q., Lai,K., Liu,C., Zhang,L., Liu,X., Yao,Y., Zhou,S., Li,X.,
            Shen,P., Chang,Q., Malwal,S.R., He,Y., Li,W., Chen,C., Chen,C.C.,
            Oldfield,E., Guo,R.T. and Zhang,Y.
  TITLE     Phosphoantigens glue butyrophilin 3A1 and 2A1 to activate
            Vgamma9Vdelta2 T cells
  JOURNAL   Nature 621 (7980), 840-848 (2023)
   PUBMED   37674084
  REMARK    GeneRIF: Phosphoantigens glue butyrophilin 3A1 and 2A1 to activate
            Vgamma9Vdelta2 T cells.
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Nguyen,K., Jin,Y., Howell,M., Hsiao,C.C., Wiemer,A.J. and
            Vinogradova,O.
  TITLE     Mutations to the BTN2A1 Linker Region Impact Its Homodimerization
            and Its Cytoplasmic Interaction with Phospho-Antigen-Bound BTN3A1
  JOURNAL   J Immunol 211 (1), 23-33 (2023)
   PUBMED   37171180
  REMARK    GeneRIF: Mutations to the BTN2A1 Linker Region Impact Its
            Homodimerization and Its Cytoplasmic Interaction with
            Phospho-Antigen-Bound BTN3A1.
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Gay,L., Mezouar,S., Cano,C., Foucher,E., Gabriac,M., Fullana,M.,
            Madakamutil,L., Mege,J.L. and Olive,D.
  TITLE     BTN3A Targeting Vgamma9Vdelta2 T Cells Antimicrobial Activity
            Against Coxiella burnetii-Infected Cells
  JOURNAL   Front Immunol 13, 915244 (2022)
   PUBMED   35833118
  REMARK    GeneRIF: BTN3A Targeting Vgamma9Vdelta2 T Cells Antimicrobial
            Activity Against Coxiella burnetii-Infected Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Hsiao,C.C., Nguyen,K., Jin,Y., Vinogradova,O. and Wiemer,A.J.
  TITLE     Ligand-induced interactions between butyrophilin 2A1 and 3A1
            internal domains in the HMBPP receptor complex
  JOURNAL   Cell Chem Biol 29 (6), 985-995 (2022)
   PUBMED   35081362
  REMARK    GeneRIF: The intracellular domain of BTN2A1 binds to the
            intracellular domain of BTN3A1 only in the presence of
            phosphoantigen.
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Cano,C.E., Pasero,C., De Gassart,A., Kerneur,C., Gabriac,M.,
            Fullana,M., Granarolo,E., Hoet,R., Scotet,E., Rafia,C.,
            Herrmann,T., Imbert,C., Gorvel,L., Vey,N., Briantais,A., le
            Floch,A.C. and Olive,D.
  TITLE     BTN2A1, an immune checkpoint targeting Vgamma9Vdelta2 T cell
            cytotoxicity against malignant cells
  JOURNAL   Cell Rep 36 (2), 109359 (2021)
   PUBMED   34260935
  REMARK    GeneRIF: BTN2A1, an immune checkpoint targeting Vgamma9Vdelta2 T
            cell cytotoxicity against malignant cells.
REFERENCE   6  (residues 1 to 527)
  AUTHORS   Yamada,Y., Nishida,T., Ichihara,S., Sawabe,M., Fuku,N.,
            Nishigaki,Y., Aoyagi,Y., Tanaka,M., Fujiwara,Y., Yoshida,H.,
            Shinkai,S., Satoh,K., Kato,K., Fujimaki,T., Yokoi,K., Oguri,M.,
            Yoshida,T., Watanabe,S., Nozawa,Y., Hasegawa,A., Kojima,T.,
            Han,B.G., Ahn,Y., Lee,M., Shin,D.J., Lee,J.H. and Jang,Y.
  TITLE     Association of a polymorphism of BTN2A1 with myocardial infarction
            in East Asian populations
  JOURNAL   Atherosclerosis 215 (1), 145-152 (2011)
   PUBMED   21211798
  REMARK    GeneRIF: BTN2A1 may be a susceptibility gene for myocardial
            infarction in Japanese individuals.
REFERENCE   7  (residues 1 to 527)
  AUTHORS   Malcherek,G., Mayr,L., Roda-Navarro,P., Rhodes,D., Miller,N. and
            Trowsdale,J.
  TITLE     The B7 homolog butyrophilin BTN2A1 is a novel ligand for DC-SIGN
  JOURNAL   J Immunol 179 (6), 3804-3811 (2007)
   PUBMED   17785817
  REMARK    GeneRIF: Rather than interacting with T cells, butyrophilin BTN2A1
            is recognized by DC-SIGN on immature monocyte-derived dendritic
            cells.
REFERENCE   8  (residues 1 to 527)
  AUTHORS   Rhodes,D.A., Stammers,M., Malcherek,G., Beck,S. and Trowsdale,J.
  TITLE     The cluster of BTN genes in the extended major histocompatibility
            complex
  JOURNAL   Genomics 71 (3), 351-362 (2001)
   PUBMED   11170752
REFERENCE   9  (residues 1 to 527)
  AUTHORS   Ruddy,D.A., Kronmal,G.S., Lee,V.K., Mintier,G.A., Quintana,L.,
            Domingo,R. Jr., Meyer,N.C., Irrinki,A., McClelland,E.E., Fullan,A.,
            Mapa,F.A., Moore,T., Thomas,W., Loeb,D.B., Harmon,C.,
            Tsuchihashi,Z., Wolff,R.K., Schatzman,R.C. and Feder,J.N.
  TITLE     A 1.1-Mb transcript map of the hereditary hemochromatosis locus
  JOURNAL   Genome Res 7 (5), 441-456 (1997)
   PUBMED   9149941
REFERENCE   10 (residues 1 to 527)
  AUTHORS   Tazi-Ahnini,R., Henry,J., Offer,C., Bouissou-Bouchouata,C.,
            Mather,I.H. and Pontarotti,P.
  TITLE     Cloning, localization, and structure of new members of the
            butyrophilin gene family in the juxta-telomeric region of the major
            histocompatibility complex
  JOURNAL   Immunogenetics 47 (1), 55-63 (1997)
   PUBMED   9382921
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY157783.1, DC348937.1 and
            U90543.1.
            
            Summary: This gene encodes a member of the immunoglobulin
            superfamily. The gene is located in a cluster of butyrophilin-like
            genes in the juxta-telomeric region of the major histocompatibility
            complex on chromosome 6. A pseudogene of this gene has been
            identified in this cluster. The encoded protein is an integral
            plasma membrane protein involved in lipid, fatty-acid, and sterol
            metabolism. Alterations in this gene may be associated with several
            disease states including metabolic syndrome. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U90543.1, SRR1803615.169318.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312541.10/ ENSP00000312158.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.2"
     Protein         1..527
                     /product="butyrophilin subfamily 2 member A1 isoform 1
                     precursor"
                     /calculated_mol_wt=56752
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2899
     mat_peptide     29..527
                     /product="Butyrophilin subfamily 2 member A1.
                     /id=PRO_0000014529"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7KYR7.3)"
                     /calculated_mol_wt=56752
     Region          30..143
                     /region_name="IgV_MOG_like"
                     /note="Immunoglobulin (Ig)-like domain of myelin
                     oligodendrocyte glycoprotein (MOG); cd05713"
                     /db_xref="CDD:409378"
     Region          30..53
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409378"
     Region          31..35
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409378"
     Region          38..42
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409378"
     Region          45..53
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409378"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7KYR7.3)"
     Region          54..62
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409378"
     Site            order(60..61,80,91,128..129,131..132,134..135)
                     /site_type="other"
                     /note="Fab binding site [polypeptide binding]"
                     /db_xref="CDD:409378"
     Region          62..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409378"
     Region          63..67
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409378"
     Region          68..86
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409378"
     Region          72..80
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409378"
     Region          81..84
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409378"
     Region          88..128
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409378"
     Region          95..100
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409378"
     Region          106..114
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409378"
     Site            114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q7KYR7.3)"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q7KYR7.3)"
     Region          121..129
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409378"
     Region          129..131
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409378"
     Region          131..143
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409378"
     Region          132..143
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409378"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7KYR7.3)"
     Region          251..>322
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          327..500
                     /region_name="SPRY_PRY_BTN1_2"
                     /note="butyrophilin subfamily member A1 and A2 (BTN1A and
                     BTN2A); cd15819"
                     /db_xref="CDD:293991"
     CDS             1..527
                     /gene="BTN2A1"
                     /gene_synonym="BK14H9.1; BT2.1; BTF1; BTN2.1; DJ3E1.1"
                     /coded_by="NM_007049.5:219..1802"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4613.1"
                     /db_xref="GeneID:11120"
                     /db_xref="HGNC:HGNC:1136"
                     /db_xref="MIM:613590"
ORIGIN      
        1 mesaaalhfs rpasllllll slcalvsaqf ivvgptdpil atvgenttlr chlspeknae
       61 dmevrwfrsq fspavfvykg grerteeqme eyrgrttfvs kdisrgsval vihnitaqen
      121 gtyrcyfqeg rsydeailhl vvaglgskpl ismrghedgg irlecisrgw ypkpltvwrd
      181 pyggvapalk evsmpdadgl fmvttaviir dksvrnmscs inntllgqkk esvifipesf
      241 mpsvspcava lpiivvilmi piavciywin klqkekkils gekeferetr eialkeleke
      301 rvqkeeelqv keklqeelrw rrtflhavdv vldpdtahpd lflsedrrsv rrcpfrhlge
      361 svpdnperfd sqpcvlgres fasgkhywev evenviewtv gvcrdsverk gevllipqng
      421 fwtlemhkgq yravsspdri lplkeslcrv gvfldyeagd vsfynmrdrs hiytcprsaf
      481 svpvrpffrl gcedspific paltgangvt vpeegltlhr vgthqsl
//
LOCUS       NP_001350392             363 aa            linear   ROD 27-APR-2025
DEFINITION  O-phosphoseryl-tRNA(Sec) selenium transferase isoform 2 [Mus
            musculus].
ACCESSION   NP_001350392
VERSION     NP_001350392.1
DBSOURCE    REFSEQ: accession NM_001363463.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Fradejas-Villar,N., Zhao,W., Reuter,U., Doengi,M., Ingold,I.,
            Bohleber,S., Conrad,M. and Schweizer,U.
  TITLE     Missense mutation in selenocysteine synthase causes
            cardio-respiratory failure and perinatal death in mice which can be
            compensated by selenium-independent GPX4
  JOURNAL   Redox Biol 48, 102188 (2021)
   PUBMED   34794077
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Mix,H., Weiler-Normann,C., Thimme,R., Ahlenstiel,G., Shin,E.C.,
            Herkel,J., David,C.S., Lohse,A.W. and Rehermann,B.
  TITLE     Identification of CD4 T-cell epitopes in soluble liver
            antigen/liver pancreas autoantigen in autoimmune hepatitis
  JOURNAL   Gastroenterology 135 (6), 2107-2118 (2008)
   PUBMED   18773898
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Ganichkin,O.M., Xu,X.M., Carlson,B.A., Mix,H., Hatfield,D.L.,
            Gladyshev,V.N. and Wahl,M.C.
  TITLE     Structure and catalytic mechanism of eukaryotic selenocysteine
            synthase
  JOURNAL   J Biol Chem 283 (9), 5849-5865 (2008)
   PUBMED   18093968
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Xu,X.M., Carlson,B.A., Mix,H., Zhang,Y., Saira,K., Glass,R.S.,
            Berry,M.J., Gladyshev,V.N. and Hatfield,D.L.
  TITLE     Biosynthesis of selenocysteine on its tRNA in eukaryotes
  JOURNAL   PLoS Biol 5 (1), e4 (2007)
   PUBMED   17194211
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Small-Howard,A., Morozova,N., Stoytcheva,Z., Forry,E.P.,
            Mansell,J.B., Harney,J.W., Carlson,B.A., Xu,X.M., Hatfield,D.L. and
            Berry,M.J.
  TITLE     Supramolecular complexes mediate selenocysteine incorporation in
            vivo
  JOURNAL   Mol Cell Biol 26 (6), 2337-2346 (2006)
   PUBMED   16508009
REFERENCE   8  (residues 1 to 363)
  AUTHORS   Xu,X.M., Mix,H., Carlson,B.A., Grabowski,P.J., Gladyshev,V.N.,
            Berry,M.J. and Hatfield,D.L.
  TITLE     Evidence for direct roles of two additional factors, SECp43 and
            soluble liver antigen, in the selenoprotein synthesis machinery
  JOURNAL   J Biol Chem 280 (50), 41568-41575 (2005)
   PUBMED   16230358
  REMARK    GeneRIF: SECp43 and SLA have roles in selenoprotein synthesis
            [soluble liver antigen]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK153792.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK153792.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164143 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 28.44 cM"
     Protein         1..363
                     /product="O-phosphoseryl-tRNA(Sec) selenium transferase
                     isoform 2"
                     /EC_number="2.9.1.2"
                     /note="O-phosphoseryl-tRNA(Sec) selenium transferase;
                     selenocysteinyl-tRNA(Sec) synthase; UGA suppressor
                     tRNA-associated protein"
                     /calculated_mol_wt=39863
     Region          <1..317
                     /region_name="AAT_I"
                     /note="Aspartate aminotransferase (AAT) superfamily (fold
                     type I) of pyridoxal phosphate (PLP)-dependent enzymes.
                     PLP combines with an alpha-amino acid to form a compound
                     called a Schiff base or aldimine intermediate, which
                     depending on the reaction, is the...; cl18945"
                     /db_xref="CDD:450240"
     Site            143
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99742"
     CDS             1..363
                     /gene="Sepsecs"
                     /gene_synonym="D5Ertd135e; SecS; SLA"
                     /coded_by="NM_001363463.1:370..1461"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:211006"
                     /db_xref="MGI:MGI:1098791"
ORIGIN      
        1 matgmsltlc fltlrhkrpk akyiiwprid qkscfksmvt agfepvvien vlegdelrtd
       61 lkaveakiqe lgpehilclh sttacfaprv pdrleelavi canydiphvv nnayglqssk
      121 cmhliqqgar vgridafvqs ldknfmvpvg gaiiagfnep fiqdiskmyp grasaspsld
      181 vlitllslgc sgyrkllker kemfvylstq lkklaeahne rllqtphnpi slamtlktid
      241 ghhdkavtql gsmlftrqvs garavplgnv qtvsghtfrg fmshadnypc aylnaaaaig
      301 mkmqdvdlfi krldkclniv rkeqtrasvv sgadrnkaed adieemalkl ddvlgdvgqg
      361 pal
//
LOCUS       NP_808227                391 aa            linear   PRI 27-APR-2025
DEFINITION  casein kinase II subunit alpha isoform a [Homo sapiens].
ACCESSION   NP_808227
VERSION     NP_808227.1
DBSOURCE    REFSEQ: accession NM_177559.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Goel,H. and O'Donnell,S.
  TITLE     Inherited loss of function variant in CSNK2A1: the oldest reported
            cases of Okur-Chung syndrome in a single family
  JOURNAL   Clin Dysmorphol 33 (3), 121-124 (2024)
   PUBMED   38818820
  REMARK    GeneRIF: Inherited loss of function variant in CSNK2A1: the oldest
            reported cases of Okur-Chung syndrome in a single family.
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ampofo,E., Pack,M., Wrublewsky,S., Boewe,A.S., Spigelman,A.F.,
            Koch,H., MacDonald,P.E., Laschke,M.W., Montenarh,M. and Gotz,C.
  TITLE     CK2 activity is crucial for proper glucagon expression
  JOURNAL   Diabetologia 67 (7), 1368-1385 (2024)
   PUBMED   38503901
  REMARK    GeneRIF: CK2 activity is crucial for proper glucagon expression.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Liu,Z.D., Shi,Y.H., Xu,Q.C., Zhao,G.Y., Zhu,Y.Q., Li,F.X., Ma,M.J.,
            Ye,J.Y., Huang,X.T., Wang,X.Y., Xu,X., Wang,J.Q., Zhao,W. and
            Yin,X.Y.
  TITLE     CSNK2A1 confers gemcitabine resistance to pancreatic ductal
            adenocarcinoma via inducing autophagy
  JOURNAL   Cancer Lett 585, 216640 (2024)
   PUBMED   38290659
  REMARK    GeneRIF: CSNK2A1 confers gemcitabine resistance to pancreatic
            ductal adenocarcinoma via inducing autophagy.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Nan,H., Chu,M., Zhang,J., Jiang,D., Wang,Y. and Wu,L.
  TITLE     Okur-Chung neurodevelopmental syndrome: Implications for phenotype
            and genotype expansion
  JOURNAL   Mol Genet Genomic Med 12 (3), e2398 (2024)
   PUBMED   38444259
  REMARK    GeneRIF: Okur-Chung neurodevelopmental syndrome: Implications for
            phenotype and genotype expansion.
            Review article
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Chung,W. and Okur,V.
  TITLE     Okur-Chung Neurodevelopmental Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35679446
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Hagiwara,T., Nakaya,K., Nakamura,Y., Nakajima,H., Nishimura,S. and
            Taya,Y.
  TITLE     Specific phosphorylation of the acidic central region of the N-myc
            protein by casein kinase II
  JOURNAL   Eur J Biochem 209 (3), 945-950 (1992)
   PUBMED   1425701
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Russo,G.L., Vandenberg,M.T., Yu,I.J., Bae,Y.S., Franza,B.R. Jr. and
            Marshak,D.R.
  TITLE     Casein kinase II phosphorylates p34cdc2 kinase in G1 phase of the
            HeLa cell division cycle
  JOURNAL   J Biol Chem 267 (28), 20317-20325 (1992)
   PUBMED   1400350
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Lin,A., Frost,J., Deng,T., Smeal,T., al-Alawi,N., Kikkawa,U.,
            Hunter,T., Brenner,D. and Karin,M.
  TITLE     Casein kinase II is a negative regulator of c-Jun DNA binding and
            AP-1 activity
  JOURNAL   Cell 70 (5), 777-789 (1992)
   PUBMED   1516134
  REMARK    Erratum:[Cell. 1992 Nov 27;71(5):887. PMID: 1423636]
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Sacks,D.B., Davis,H.W., Crimmins,D.L. and McDonald,J.M.
  TITLE     Insulin-stimulated phosphorylation of calmodulin
  JOURNAL   Biochem J 286 (Pt 1) (Pt 1), 211-216 (1992)
   PUBMED   1520270
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU132198.1, M55265.1,
            BC053532.1 and AL049761.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Casein kinase II is a serine/threonine protein kinase that
            phosphorylates acidic proteins such as casein. It is involved in
            various cellular processes, including cell cycle control,
            apoptosis, and circadian rhythm. The kinase exists as a tetramer
            and is composed of an alpha, an alpha-prime, and two beta subunits.
            The alpha subunits contain the catalytic activity while the beta
            subunits undergo autophosphorylation. The protein encoded by this
            gene represents the alpha subunit. Multiple transcript variants
            encoding different protein isoforms have been found for this gene.
            [provided by RefSeq, Apr 2018].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a). Variants 1, 2, 4 and 5 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.35161.1,
                                           SRR1803613.132695.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000217244.9/ ENSP00000217244.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..391
                     /product="casein kinase II subunit alpha isoform a"
                     /EC_number="2.7.11.1"
                     /note="CK2 catalytic subunit alpha; protein kinase CK2;
                     casein kinase II alpha 1 subunit; casein kinase II alpha 1
                     polypeptide pseudogene; casein kinase 2, alpha 1
                     polypeptide"
                     /calculated_mol_wt=45013
     Region          20..325
                     /region_name="STKc_CK2_alpha"
                     /note="Catalytic subunit (alpha) of the Serine/Threonine
                     Kinase, Casein Kinase 2; cd14132"
                     /db_xref="CDD:271034"
     Site            order(36,39..41,67,69,101,103..104,110)
                     /site_type="other"
                     /note="allosteric inhibitor binding site [chemical
                     binding]"
                     /db_xref="CDD:271034"
     Site            order(36..37,39..42,50,54,103)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:271034"
     Site            order(36..37,39..41,57,59,103)
                     /site_type="other"
                     /note="CK2 beta interface [polypeptide binding]"
                     /db_xref="CDD:271034"
     Region          36..41
                     /region_name="Interaction with beta subunit.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P68400.1)"
     Site            order(45..49,53,66,68,80,95,113..116,120,122..123,156,158,
                     160..161,163,175,178,189,191..194,196,235)
                     /site_type="active"
                     /db_xref="CDD:271034"
     Site            order(47..48,50..51,53,66,68,95,113..114,116,160..161,163,
                     174..175)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271034"
     Site            order(80,122,156,158,178,189,191..194,196,235)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271034"
     Site            order(174..184,189..196)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271034"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773,
                     ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     CDS             1..391
                     /gene="CSNK2A1"
                     /gene_synonym="CK2A1; Cka1; Cka2; CKII; OCNDS"
                     /coded_by="NM_177559.3:346..1521"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13003.1"
                     /db_xref="GeneID:1457"
                     /db_xref="HGNC:HGNC:2457"
                     /db_xref="MIM:115440"
ORIGIN      
        1 msgpvpsrar vytdvnthrp reywdyeshv vewgnqddyq lvrklgrgky sevfeainit
       61 nnekvvvkil kpvkkkkikr eikilenlrg gpniitladi vkdpvsrtpa lvfehvnntd
      121 fkqlyqtltd ydirfymyei lkaldychsm gimhrdvkph nvmidhehrk lrlidwglae
      181 fyhpgqeynv rvasryfkgp ellvdyqmyd ysldmwslgc mlasmifrke pffhghdnyd
      241 qlvriakvlg tedlydyidk ynieldprfn dilgrhsrkr werfvhsenq hlvspealdf
      301 ldkllrydhq srltareame hpyfytvvkd qarmgsssmp ggstpvssan mmsgissvpt
      361 psplgplags pviaaanplg mpvpaaagaq q
//
LOCUS       NP_775753                499 aa            linear   PRI 27-APR-2025
DEFINITION  tektin-like protein 1 [Homo sapiens].
ACCESSION   NP_775753
VERSION     NP_775753.2
DBSOURCE    REFSEQ: accession NM_173482.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Hosgood,H.D. 3rd, Zhang,L., Shen,M., Berndt,S.I., Vermeulen,R.,
            Li,G., Yin,S., Yeager,M., Yuenger,J., Rothman,N., Chanock,S.,
            Smith,M. and Lan,Q.
  TITLE     Association between genetic variants in VEGF, ERCC3 and
            occupational benzene haematotoxicity
  JOURNAL   Occup Environ Med 66 (12), 848-853 (2009)
   PUBMED   19773279
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004659.1, AK097684.1 and AC104528.2.
            
            On Apr 10, 2009 this sequence version replaced NP_775753.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK097684.1, BC035678.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000292574.4/ ENSP00000292574.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..499
                     /product="tektin-like protein 1"
                     /note="coiled-coil domain-containing protein 105;
                     coiled-coil domain containing 105"
                     /calculated_mol_wt=56778
     Region          140..451
                     /region_name="Tektin"
                     /note="Tektin family; pfam03148"
                     /db_xref="CDD:460827"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9D4K7; propagated from
                     UniProtKB/Swiss-Prot (Q8IYK2.3)"
     CDS             1..499
                     /gene="TEKTL1"
                     /gene_synonym="CCDC105"
                     /coded_by="NM_173482.3:101..1600"
                     /db_xref="CCDS:CCDS12322.1"
                     /db_xref="GeneID:126402"
                     /db_xref="HGNC:HGNC:26866"
ORIGIN      
        1 mrvlvppaer sqdtrvgapa wreaaqamar tahiltdrcg qeavtmwqpk dsvldpnvah
       61 hlgraayiqp wrfrvemikg ggtlekpppg egvtlwkgkm kppawyarlp lplhrkaral
      121 qttevvhaha rgarltaarl graqhqingr vrqllrqrev tdhrlsevrk gllinqqsvk
      181 lrgyrpksek vpdkadsmlt wekeelksmk rkmerdmeks evllktlasc rdtlnfcfke
      241 rlqavdlmnq pldkvleqar rhswvnlsra ptprtqgqkt pppdpvgtyn pacalalnea
      301 krllveskdt lvemaknevd vreqqlqisd rvcaslaqka setlelkerl nmtlglmrgt
      361 ilrctkynqe lytthglikg plskvhleta ekldrplvrm yqrhvgtqlp eaarlaqgtd
      421 klqchityle knldellath knlswglnck nighevdgnv vrlrlrqrqp hvcyeqaqrl
      481 vkdwdprtpp prskssadp
//
LOCUS       NP_059990                860 aa            linear   PRI 27-APR-2025
DEFINITION  M-phase phosphoprotein 8 [Homo sapiens].
ACCESSION   NP_059990 XP_167894
VERSION     NP_059990.2
DBSOURCE    REFSEQ: accession NM_017520.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Li,T., Li,N., Wang,L., Li,J. and Zhang,X.
  TITLE     MPP8 Promotes Proliferation and Restrains Apoptosis in Osteosarcoma
            by Regulating p38alphaMAPK Pathway
  JOURNAL   Technol Cancer Res Treat 20, 1533033821995272 (2021)
   PUBMED   33596786
  REMARK    GeneRIF: MPP8 Promotes Proliferation and Restrains Apoptosis in
            Osteosarcoma by Regulating p38alphaMAPK Pathway.
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Wang,Y., Xiao,H., Wang,C., Wu,H., He,H., Yao,C., Cui,J. and Li,W.
  TITLE     M-phase phosphoprotein 8 promotes gastric cancer growth and
            metastasis via p53/Bcl-2 and EMT-related signaling pathways
  JOURNAL   J Cell Biochem 121 (3), 2330-2342 (2020)
   PUBMED   31692032
  REMARK    GeneRIF: M-phase phosphoprotein 8 promotes gastric cancer growth
            and metastasis via p53/Bcl-2 and EMT-related signaling pathways.
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Gao,X.Y., Qiao,Y.L., Zhang,Y., Wang,J., Shen,X. and Xu,C.W.
  TITLE     Knockdown of MPP8 suppresses cell proliferation via regulation of
            HOXA5 in non-small cell lung cancer cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 64 (1), 27-31 (2018)
   PUBMED   29412790
  REMARK    GeneRIF: The study demonstrated that MPP8 was associated with
            non-small cell lung cancer cell proliferation through regulation of
            HOXA5.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Liu,N., Lee,C.H., Swigut,T., Grow,E., Gu,B., Bassik,M.C. and
            Wysocka,J.
  TITLE     Selective silencing of euchromatic L1s revealed by genome-wide
            screens for L1 regulators
  JOURNAL   Nature 553 (7687), 228-232 (2018)
   PUBMED   29211708
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Tchasovnikarova,I.A., Timms,R.T., Douse,C.H., Roberts,R.C.,
            Dougan,G., Kingston,R.E., Modis,Y. and Lehner,P.J.
  TITLE     Hyperactivation of HUSH complex function by Charcot-Marie-Tooth
            disease mutation in MORC2
  JOURNAL   Nat Genet 49 (7), 1035-1044 (2017)
   PUBMED   28581500
REFERENCE   6  (residues 1 to 860)
  AUTHORS   Kokura,K., Sun,L., Bedford,M.T. and Fang,J.
  TITLE     Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing
            and promotes tumour cell motility and invasion
  JOURNAL   EMBO J 29 (21), 3673-3687 (2010)
   PUBMED   20871592
  REMARK    GeneRIF: MPP8 mediates E-cadherin gene silencing and promotes
            breast tumour cell motility and invasion.
REFERENCE   7  (residues 1 to 860)
  AUTHORS   Maksimov,V.V., Arman,I.P. and Tarantul,V.Z.
  TITLE     [Identification of the proteins interacting with neuroprotective
            peptide humanin in a yeast two-hybrid system]
  JOURNAL   Genetika 42 (2), 274-277 (2006)
   PUBMED   16583711
REFERENCE   8  (residues 1 to 860)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   9  (residues 1 to 860)
  AUTHORS   Umeda,M., Nishitani,H. and Nishimoto,T.
  TITLE     A novel nuclear protein, Twa1, and Muskelin comprise a complex with
            RanBPM
  JOURNAL   Gene 303, 47-54 (2003)
   PUBMED   12559565
REFERENCE   10 (residues 1 to 860)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA672302.1, BC003542.1, AL354808.24 and R60056.1.
            
            On or before Jan 24, 2004 this sequence version replaced
            XP_167894.1, NP_059990.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.262443.1, BC003542.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361479.10/ ENSP00000355388.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..860
                     /product="M-phase phosphoprotein 8"
                     /EC_number="2.4.2.30"
                     /note="M-phase phosphoprotein, mpp8; two hybrid-associated
                     protein 3 with RanBPM"
                     /calculated_mol_wt=97051
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Region          58..108
                     /region_name="CD_MMP8"
                     /note="chromodomain of M-phase phosphoprotein 8; cd18633"
                     /db_xref="CDD:349283"
     Site            order(58..61,80,83,89,91,95..96,98..102)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349283"
     Site            59
                     /site_type="other"
                     /note="Interaction with histone H3K9me3.
                     /evidence=ECO:0000269|PubMed:21419134; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Region          80..87
                     /region_name="Histone H3K9me3 binding.
                     /evidence=ECO:0000269|PubMed:21419134"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TYA6; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Region          129..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3TYA6; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000305|PubMed:23416073,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000305|PubMed:23416073; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Region          <200..>550
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          206..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TYA6; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000305|PubMed:23416073; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000305|PubMed:23416073; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Region          431..560
                     /region_name="Interaction with humanin.
                     /evidence=ECO:0000269|PubMed:23532874"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Region          458..496
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Region          485..746
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(600,602,606..607,610..612,614..615,619,622,631,633,
                     635,639..640,643..645,647..648,652,655,664,666,668,
                     672..673,676..678,680..681,685,688)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          600..631
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          600..629
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Region          633..664
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          633..662
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Region          666..695
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          666..695
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Region          699..728
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     CDS             1..860
                     /gene="MPHOSPH8"
                     /gene_synonym="HSMPP8; mpp8; TWA3"
                     /coded_by="NM_017520.4:91..2673"
                     /db_xref="CCDS:CCDS9287.1"
                     /db_xref="GeneID:54737"
                     /db_xref="HGNC:HGNC:29810"
                     /db_xref="MIM:611626"
ORIGIN      
        1 meqvaegarv tavpvsaads teelaeveeg vgvvgednda aargaeafgd seedgedvfe
       61 vekildmkte ggkvlykvrw kgytsdddtw epeihledck evllefrkki aenkakavrk
      121 diqrlslnnd ifeansdsdq qsetkedtsp kkkkkklrqr eekspddlkk kkakagklkd
      181 kskpdlessl eslvfdlrtk kriseakeel keskkpkkde vketkelkkv kkgeirdlkt
      241 ktredpkenr ktkkekfves qvesessvln dspfpeddse glhsdsreek qntksarera
      301 gqdmglehgf ekpldsamsa eedtdvrgrr kkktprkaed trenrklenk naflekktvp
      361 kkqrnqdrsk saaeleklmp vsaqtpkgrr lsgeerglws tdsaeedket krneskekyq
      421 krhdsdkeek grkepkglkt lkeirnafdl fkltpeeknd vsennrkree ipldfktidd
      481 hktkenkqsl kerrntrdet dtwayiaaeg dqevldsvcq adensdgrqq ilslgmdlql
      541 ewmkledfqk hldgkdenfa atdaipsnvl rdavkngdyi tvkvalnsne eynldqedss
      601 gmtlvmlaaa ggqddllrll itkgakvngr qkngttalih aaeknflttv ailleagafv
      661 nvqqsngeta lmkackrgns divrlviecg adcnilskhq nsalhfakqs nnvlvydllk
      721 nhletlsrva eetikdyfea rlallepvfp iachrlcegp dfstdfnykp pqnipegsgi
      781 llfifhanfl gkeviarlcg pcsvqavvln dkfqlpvfld shfvysfspv agpnklfirl
      841 teapsakvkl ligayrvqlq
//
LOCUS       NP_001357110             633 aa            linear   PRI 27-APR-2025
DEFINITION  glutathione S-transferase C-terminal domain-containing protein
            isoform 1 [Homo sapiens].
ACCESSION   NP_001357110 XP_005263279
VERSION     NP_001357110.1
DBSOURCE    REFSEQ: accession NM_001370181.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Henry,A.P., Probert,K., Stewart,C.E., Thakker,D., Bhaker,S.,
            Azimi,S., Hall,I.P. and Sayers,I.
  TITLE     Defining a role for lung function associated gene GSTCD in cell
            homeostasis
  JOURNAL   Respir Res 20 (1), 172 (2019)
   PUBMED   31370853
  REMARK    GeneRIF: Targeted knock-down of GSTCD in bronchial epithelial cells
            identified a role for GSTCD in cell viability.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Levinsson,A., Olin,A.C., Modig,L., Dahgam,S., Bjorck,L.,
            Rosengren,A. and Nyberg,F.
  TITLE     Interaction effects of long-term air pollution exposure and
            variants in the GSTP1, GSTT1 and GSTCD genes on risk of acute
            myocardial infarction and hypertension: a case-control study
  JOURNAL   PLoS One 9 (6), e99043 (2014)
   PUBMED   24915237
  REMARK    GeneRIF: Air pollution exposure entails an increased risk of acute
            myocardial infarction, and this risk differed over genotype strata
            for variants in the GSTP1, GSTT1 and GSTCD genes, albeit not
            statistically-significantly.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Obeidat,M., Miller,S., Probert,K., Billington,C.K., Henry,A.P.,
            Hodge,E., Nelson,C.P., Stewart,C.E., Swan,C., Wain,L.V., Soler
            Artigas,M., Melen,E., Ushey,K., Hao,K., Lamontagne,M., Bosse,Y.,
            Postma,D.S., Tobin,M.D., Sayers,I. and Hall,I.P.
  TITLE     GSTCD and INTS12 regulation and expression in the human lung
  JOURNAL   PLoS One 8 (9), e74630 (2013)
   PUBMED   24058608
  REMARK    GeneRIF: In fixed sections of human lung tissue, GSTCD protein
            expression was ubiquitous, whereas INTS12 expression was
            predominantly in epithelial cells and pneumocytes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Ong,B.A., Li,J., McDonough,J.M., Wei,Z., Kim,C., Chiavacci,R.,
            Mentch,F., Caboot,J.B., Spergel,J., Allen,J.L., Sleiman,P.M. and
            Hakonarson,H.
  TITLE     Gene network analysis in a pediatric cohort identifies novel lung
            function genes
  JOURNAL   PLoS One 8 (9), e72899 (2013)
   PUBMED   24023788
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Weimann,M., Grossmann,A., Woodsmith,J., Ozkan,Z., Birth,P.,
            Meierhofer,D., Benlasfer,N., Valovka,T., Timmermann,B.,
            Wanker,E.E., Sauer,S. and Stelzl,U.
  TITLE     A Y2H-seq approach defines the human protein methyltransferase
            interactome
  JOURNAL   Nat Methods 10 (4), 339-342 (2013)
   PUBMED   23455924
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Soler Artigas,M., Wain,L.V., Repapi,E., Obeidat,M., Sayers,I.,
            Burton,P.R., Johnson,T., Zhao,J.H., Albrecht,E., Dominiczak,A.F.,
            Kerr,S.M., Smith,B.H., Cadby,G., Hui,J., Palmer,L.J.,
            Hingorani,A.D., Wannamethee,S.G., Whincup,P.H., Ebrahim,S.,
            Smith,G.D., Barroso,I., Loos,R.J., Wareham,N.J., Cooper,C.,
            Dennison,E., Shaheen,S.O., Liu,J.Z., Marchini,J., Dahgam,S.,
            Naluai,A.T., Olin,A.C., Karrasch,S., Heinrich,J., Schulz,H.,
            McKeever,T.M., Pavord,I.D., Heliovaara,M., Ripatti,S., Surakka,I.,
            Blakey,J.D., Kahonen,M., Britton,J.R., Nyberg,F., Holloway,J.W.,
            Lawlor,D.A., Morris,R.W., James,A.L., Jackson,C.M., Hall,I.P. and
            Tobin,M.D.
  CONSRTM   Medical Research Council National Survey of Health and Development
            (NSHD) Respiratory Study Team; SpiroMeta Consortium
  TITLE     Effect of five genetic variants associated with lung function on
            the risk of chronic obstructive lung disease, and their joint
            effects on lung function
  JOURNAL   Am J Respir Crit Care Med 184 (7), 786-795 (2011)
   PUBMED   21965014
  REMARK    GeneRIF: GSTCD polymorphism associated with COPD risk and lung
            function decline
REFERENCE   7  (residues 1 to 633)
  AUTHORS   Kalsi,G., Kuo,P.H., Aliev,F., Alexander,J., McMichael,O.,
            Patterson,D.G., Walsh,D., Zhao,Z., Schuckit,M., Nurnberger,J. Jr.,
            Edenberg,H., Kramer,J., Hesselbrock,V., Tischfield,J.A.,
            Vladimirov,V., Prescott,C.A., Dick,D.M., Kendler,K.S. and
            Riley,B.P.
  TITLE     A systematic gene-based screen of chr4q22-q32 identifies
            association of a novel susceptibility gene, DKK2, with the
            quantitative trait of alcohol dependence symptom counts
  JOURNAL   Hum Mol Genet 19 (12), 2497-2506 (2010)
   PUBMED   20332099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Erratum:[Hum Mol Genet. 2010 Oct 15;19(20):4121. Hesselbrock,
            Victor [added]; Tischfield, Jay A [added]]
REFERENCE   8  (residues 1 to 633)
  AUTHORS   Hancock,D.B., Eijgelsheim,M., Wilk,J.B., Gharib,S.A., Loehr,L.R.,
            Marciante,K.D., Franceschini,N., van Durme,Y.M., Chen,T.H.,
            Barr,R.G., Schabath,M.B., Couper,D.J., Brusselle,G.G., Psaty,B.M.,
            van Duijn,C.M., Rotter,J.I., Uitterlinden,A.G., Hofman,A.,
            Punjabi,N.M., Rivadeneira,F., Morrison,A.C., Enright,P.L.,
            North,K.E., Heckbert,S.R., Lumley,T., Stricker,B.H., O'Connor,G.T.
            and London,S.J.
  TITLE     Meta-analyses of genome-wide association studies identify multiple
            loci associated with pulmonary function
  JOURNAL   Nat Genet 42 (1), 45-52 (2010)
   PUBMED   20010835
  REMARK    GeneRIF: Meta-analysis and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 633)
  AUTHORS   Repapi,E., Sayers,I., Wain,L.V., Burton,P.R., Johnson,T.,
            Obeidat,M., Zhao,J.H., Ramasamy,A., Zhai,G., Vitart,V.,
            Huffman,J.E., Igl,W., Albrecht,E., Deloukas,P., Henderson,J.,
            Granell,R., McArdle,W.L., Rudnicka,A.R., Barroso,I., Loos,R.J.,
            Wareham,N.J., Mustelin,L., Rantanen,T., Surakka,I., Imboden,M.,
            Wichmann,H.E., Grkovic,I., Jankovic,S., Zgaga,L., Hartikainen,A.L.,
            Peltonen,L., Gyllensten,U., Johansson,A., Zaboli,G., Campbell,H.,
            Wild,S.H., Wilson,J.F., Glaser,S., Homuth,G., Volzke,H.,
            Mangino,M., Soranzo,N., Spector,T.D., Polasek,O., Rudan,I.,
            Wright,A.F., Heliovaara,M., Ripatti,S., Pouta,A., Naluai,A.T.,
            Olin,A.C., Toren,K., Cooper,M.N., James,A.L., Palmer,L.J.,
            Hingorani,A.D., Wannamethee,S.G., Whincup,P.H., Smith,G.D.,
            Ebrahim,S., McKeever,T.M., Pavord,I.D., MacLeod,A.K., Morris,A.D.,
            Porteous,D.J., Cooper,C., Dennison,E., Shaheen,S., Karrasch,S.,
            Schnabel,E., Schulz,H., Grallert,H., Bouatia-Naji,N.,
            Delplanque,J., Froguel,P., Blakey,J.D., Britton,J.R., Morris,R.W.,
            Holloway,J.W., Lawlor,D.A., Hui,J., Nyberg,F., Jarvelin,M.R.,
            Jackson,C., Kahonen,M., Kaprio,J., Probst-Hensch,N.M., Koch,B.,
            Hayward,C., Evans,D.M., Elliott,P., Strachan,D.P., Hall,I.P. and
            Tobin,M.D.
  CONSRTM   Wellcome Trust Case Control Consortium; NSHD Respiratory Study Team
  TITLE     Genome-wide association study identifies five loci associated with
            lung function
  JOURNAL   Nat Genet 42 (1), 36-44 (2010)
   PUBMED   20010834
  REMARK    GeneRIF: Data show expression of TNS1, GSTCD, AGER, HTR4 and THSD4
            in lung tissue and indicate potential targets for interventions to
            alleviate respiratory disease.
            GeneRIF: Meta-analysis and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   10 (residues 1 to 633)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC105391.1 and AC008243.6.
            
            On May 2, 2019 this sequence version replaced XP_005263279.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.130931.1,
                                           SRR1660805.39396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000515279.6/ ENSP00000422354.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..633
                     /product="glutathione S-transferase C-terminal
                     domain-containing protein isoform 1"
                     /note="glutathione S-transferase C-terminal
                     domain-containing protein"
                     /calculated_mol_wt=70948
     Region          191..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEC7.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEC7.2)"
     Region          <273..331
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
     Region          423..541
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
     CDS             1..633
                     /gene="GSTCD"
                     /coded_by="NM_001370181.1:255..2156"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS43257.1"
                     /db_xref="GeneID:79807"
                     /db_xref="HGNC:HGNC:25806"
                     /db_xref="MIM:615912"
ORIGIN      
        1 mkaikkslte eeylyldfsh qtegcifplh tsvtlfllsy cdckifkicl vvtkevsrds
       61 sllrddliqd veiqiisrqe lppivqnccl pavversdnf craglavvlr hiiqksyead
      121 plkkellell gfkktclkac aevsqwtrlc eltiplaien flressdqpp tipveilqle
      181 kklsepvrvh nddklrrqkl kqqkadgvgp pltkgkaksk vhtqetsegl dssskslelk
      241 vafskltvqe epattnreps hirkakasdl pplehvfaeg lyftladivl lpcihhflvi
      301 isrkfseklv efpllaswyq riqevpgvkt aaskcgiqfl hlpkllttst eqhpnlcevp
      361 gveeqsdplf iggprptmak lmekgievmf sphpcptwtl dwnvlpaavs pkegkmssdr
      421 alrkqqqlnn lvyvvtnqak pgdrivdfcs ggghvgivla hmlpscqvtl ienkelslir
      481 akkrsdelgl sniwfiqanm eyftgmfnig valhacgvat dmviehcikt rasfvtcpcc
      541 ygfiqntskf nfpkseqfkk tlsykehmil crfadqtavq lppqrrligk qcmclvdldr
      601 araaeecgys vqvismepes cspknnmivg vpi
//
LOCUS       NP_115484                888 aa            linear   PRI 27-APR-2025
DEFINITION  semaphorin-6B precursor [Homo sapiens].
ACCESSION   NP_115484
VERSION     NP_115484.2
DBSOURCE    REFSEQ: accession NM_032108.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Castellotti,B., Canafoglia,L., Freri,E., Tappata,M., Messina,G.,
            Magri,S., DiFrancesco,J.C., Fanella,M., Di Bonaventura,C.,
            Morano,A., Granata,T., Gellera,C., Franceschetti,S. and
            Michelucci,R.
  TITLE     Progressive myoclonus epilepsies due to SEMA6B mutations. New
            variants and appraisal of published phenotypes
  JOURNAL   Epilepsia Open 8 (2), 645-650 (2023)
   PUBMED   36719163
  REMARK    GeneRIF: Progressive myoclonus epilepsies due to SEMA6B mutations.
            New variants and appraisal of published phenotypes.
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Cordovado,A., Schaettin,M., Jeanne,M., Panasenkava,V.,
            Denomme-Pichon,A.S., Keren,B., Mignot,C., Doco-Fenzy,M., Rodan,L.,
            Ramsey,K., Narayanan,V., Jones,J.R., Prijoles,E.J., Mitchell,W.G.,
            Ozmore,J.R., Juliette,K., Torti,E., Normand,E.A., Granger,L.,
            Petersen,A.K., Au,M.G., Matheny,J.P., Phornphutkul,C.,
            Chambers,M.K., Fernandez-Ramos,J.A., Lopez-Laso,E., Kruer,M.C.,
            Bakhtiari,S., Zollino,M., Morleo,M., Marangi,G., Mei,D., Pisano,T.,
            Guerrini,R., Louie,R.J., Childers,A., Everman,D.B., Isidor,B.,
            Audebert-Bellanger,S., Odent,S., Bonneau,D., Gilbert-Dussardier,B.,
            Redon,R., Bezieau,S., Laumonnier,F., Stoeckli,E.T., Toutain,A. and
            Vuillaume,M.L.
  TITLE     SEMA6B variants cause intellectual disability and alter dendritic
            spine density and axon guidance
  JOURNAL   Hum Mol Genet 31 (19), 3325-3340 (2022)
   PUBMED   35604360
  REMARK    GeneRIF: SEMA6B variants cause intellectual disability and alter
            dendritic spine density and axon guidance.
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Shu,L., Xu,Y., Tian,Q., Chen,Y., Wang,Y., Xi,H., Wang,H., Xiao,N.
            and Mao,X.
  TITLE     A Frameshift Variant in the SEMA6B Gene Causes Global Developmental
            Delay and Febrile Seizures
  JOURNAL   Neurosci Bull 37 (9), 1357-1360 (2021)
   PUBMED   34110594
  REMARK    GeneRIF: A Frameshift Variant in the SEMA6B Gene Causes Global
            Developmental Delay and Febrile Seizures.
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Lv,X.J., Chen,X., Wang,Y., Yu,S., Pang,L. and Huang,C.
  TITLE     Aberrant expression of semaphorin 6B affects cell phenotypes in
            thyroid carcinoma by activating the Notch signalling pathway
  JOURNAL   Endokrynol Pol 72 (1), 29-36 (2021)
   PUBMED   33125690
  REMARK    GeneRIF: Aberrant expression of semaphorin 6B affects cell
            phenotypes in thyroid carcinoma by activating the Notch signalling
            pathway.
REFERENCE   5  (residues 1 to 888)
  AUTHORS   Tian,S., Liu,Y., Wu,H., Liu,H., Zeng,J., Choi,M.Y., Chen,H.,
            Gerhard,R. and Dong,M.
  TITLE     Genome-Wide CRISPR Screen Identifies Semaphorin 6A and 6B as
            Receptors for Paeniclostridium sordellii Toxin TcsL
  JOURNAL   Cell Host Microbe 27 (5), 782-792 (2020)
   PUBMED   32302524
  REMARK    GeneRIF: Genome-Wide CRISPR Screen Identifies Semaphorin 6A and 6B
            as Receptors for Paeniclostridium sordellii Toxin TcsL.
REFERENCE   6  (residues 1 to 888)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   7  (residues 1 to 888)
  AUTHORS   Collet,P., Domenjoud,L., Devignes,M.D., Murad,H., Schohn,H. and
            Dauca,M.
  TITLE     The human semaphorin 6B gene is down regulated by PPARs
  JOURNAL   Genomics 83 (6), 1141-1150 (2004)
   PUBMED   15177567
  REMARK    GeneRIF: Gene SEMA6B is strongly down regulated by peroxisome
            proliferator-activated receptors.
REFERENCE   8  (residues 1 to 888)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 888)
  AUTHORS   Correa,R.G., Sasahara,R.M., Bengtson,M.H., Katayama,M.L.,
            Salim,A.C., Brentani,M.M., Sogayar,M.C., de Souza,S.J. and
            Simpson,A.J.
  TITLE     Human semaphorin 6B [(HSA)SEMA6B], a novel human class 6 semaphorin
            gene: alternative splicing and all-trans-retinoic acid-dependent
            downregulation in glioblastoma cell lines
  JOURNAL   Genomics 73 (3), 343-348 (2001)
   PUBMED   11350127
REFERENCE   10 (residues 1 to 888)
  AUTHORS   Buchanan,J.G., Dunn,A.D. and Edgar,A.R.
  TITLE     C-nucleoside studies. Part III. Glycofuranosylethynes from
            2,3:5,6-di-O-isopropylidene-D-mannose
  JOURNAL   J Chem Soc Perkin 1 (1), 68-75 (1976)
   PUBMED   942725
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA818632.1, DB257858.1 and
            BC142617.1.
            
            On Mar 26, 2002 this sequence version replaced NP_115484.1.
            
            Summary: This gene encodes a member of the semaphorin family, a
            group of proteins characterized by the presence of a conserved
            semaphorin (sema) domain. Whereas some semaphorins are
            transmembrane proteins, others are secreted. Semaphorins play a
            major role in axon guidance. The protein encoded by this gene may
            be involved in both peripheral and central nervous system
            development. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC142617.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000586582.6/ ENSP00000467290.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..888
                     /product="semaphorin-6B precursor"
                     /note="semaphorin VIB; semaphorin Z; semaphorin-6Ba; sema
                     domain, transmembrane domain (TM), and cytoplasmic domain,
                     (semaphorin) 6B"
                     /calculated_mol_wt=92710
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2593
     mat_peptide     26..888
                     /product="semaphorin-6B"
                     /calculated_mol_wt=92710
     Region          57..524
                     /region_name="Sema_6B"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 6B (Sema6B); cd11267"
                     /db_xref="CDD:200528"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Site            order(117..120,171..172,197,199..200,207,221..223,228,
                     275..276,279,400)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200528"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Site            order(252,294,296,298..300,302,326,328..332,361,421..422,
                     424)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200528"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Site            386
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Site            441
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Site            462
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Region          525..>554
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Site            604..624
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Region          651..679
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Site            665
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O54951; propagated from
                     UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Region          695..742
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3T3.4)"
     Region          <706..888
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          757..888
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3T3.4)"
     CDS             1..888
                     /gene="SEMA6B"
                     /gene_synonym="EPM11; SEM-SEMA-Y; SEM-SEMA-Z; SEMA-VIB;
                     SEMAN; semaZ"
                     /coded_by="NM_032108.4:188..2854"
                     /db_xref="CCDS:CCDS12131.1"
                     /db_xref="GeneID:10501"
                     /db_xref="HGNC:HGNC:10739"
                     /db_xref="MIM:608873"
ORIGIN      
        1 mqtprasppr pallllllll ggahglfpee ppplsvaprd ylnhypvfvg sgpgrltpae
       61 gaddlniqrv lrvnrtlfig drdnlyrvel epptstelry qrkltwrsnp sdinvcrmkg
      121 kqegecrnfv kvlllrdest lfvcgsnafn pvcanysidt lqpvgdnisg marcpydpkh
      181 anvalfsdgm lftatvtdfl aidaviyrsl gdrptlrtvk hdskwfkepy fvhavewgsh
      241 vyfffreiam efnylekvvv srvarvcknd vggsprvlek qwtsflkarl ncsvpgdshf
      301 yfnvlqavtg vvslggrpvv lavfstpsns ipgsavcafd ltqvaavfeg rfreqkspes
      361 iwtpvpedqv prprpgccaa pgmqynassa lpddilnfvk thplmdeavp slghapwilr
      421 tlmrhqltrv avdvgagpwg nqtvvflgse agtvlkflvr pnastsgtsg lsvfleefet
      481 yrpdrcgrpg ggetgqrlls leldaasggl laafprcvvr vpvarcqqys gcmkncigsq
      541 dpycgwapdg sciflspgtr aafeqdvsga stsglgdctg llraslsedr aglvsvnllv
      601 tssvaafvvg avvsgfsvgw fvglrerrel arrkdkeail ahgageavls vsrlgerraq
      661 gpggrggggg ggagvppeal laplmqngwa katllqggph dldsgllptp eqtplpqkrl
      721 ptphphphal gprawdhghp llpasasssl lllaparape qppapgeptp dgrlyaarpg
      781 rashgdfplt phaspdrrrv vsaptgpldp asaadglprp wsppptgslr rplgphappa
      841 atlrrthtfn sgearpgdrh rgcharpgtd lahllpygga drtappvp
//
LOCUS       NP_001010887             275 aa            linear   PRI 27-APR-2025
DEFINITION  alkaline ceramidase 2 [Homo sapiens].
ACCESSION   NP_001010887 XP_294540
VERSION     NP_001010887.2
DBSOURCE    REFSEQ: accession NM_001010887.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chen,X., Lu,T., Ding,M., Cai,Y., Yu,Z., Zhou,X. and Wang,X.
  TITLE     Targeting YTHDF2 inhibits tumorigenesis of diffuse large B-cell
            lymphoma through ACER2-mediated ceramide catabolism
  JOURNAL   J Adv Res 63, 17-33 (2024)
   PUBMED   37865189
  REMARK    GeneRIF: Targeting YTHDF2 inhibits tumorigenesis of diffuse large
            B-cell lymphoma through ACER2-mediated ceramide catabolism.
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Zheng,J., Jiang,X., Jiang,K., Yan,Y., Pan,J., Liu,F., Wen,Y. and
            Li,P.
  TITLE     miR-196a-5p Correlates with Chronic Atrophic Gastritis Progression
            to Gastric Cancer and Induces Malignant Biological Behaviors of
            Gastric Cancer Cells by Targeting ACER2
  JOURNAL   Mol Biotechnol 65 (8), 1306-1317 (2023)
   PUBMED   36513872
  REMARK    GeneRIF: miR-196a-5p Correlates with Chronic Atrophic Gastritis
            Progression to Gastric Cancer and Induces Malignant Biological
            Behaviors of Gastric Cancer Cells by Targeting ACER2.
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Zhang,S., Huang,P., Dai,H., Li,Q., Hu,L., Peng,J., Jiang,S., Xu,Y.,
            Wu,Z., Nie,H., Zhang,Z., Yin,W., Zhang,X. and Lu,J.
  TITLE     TIMELESS regulates sphingolipid metabolism and tumor cell growth
            through Sp1/ACER2/S1P axis in ER-positive breast cancer
  JOURNAL   Cell Death Dis 11 (10), 892 (2020)
   PUBMED   33093451
  REMARK    GeneRIF: TIMELESS regulates sphingolipid metabolism and tumor cell
            growth through Sp1/ACER2/S1P axis in ER-positive breast cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Xu,R., Garcia-Barros,M., Wen,S., Li,F., Lin,C.L., Hannun,Y.A.,
            Obeid,L.M. and Mao,C.
  TITLE     Tumor suppressor p53 links ceramide metabolism to DNA damage
            response through alkaline ceramidase 2
  JOURNAL   Cell Death Differ 25 (5), 841-856 (2018)
   PUBMED   29229990
  REMARK    GeneRIF: These results suggest that p53 mediates DDR and exerts its
            tumor suppressive role in part by regulating the expression of
            ACER2, which in turn regulates the bioactive sphingolipid lipids.
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Sun,W., Jin,J., Xu,R., Hu,W., Szulc,Z.M., Bielawski,J., Obeid,L.M.
            and Mao,C.
  TITLE     Substrate specificity, membrane topology, and activity regulation
            of human alkaline ceramidase 2 (ACER2)
  JOURNAL   J Biol Chem 285 (12), 8995-9007 (2010)
   PUBMED   20089856
  REMARK    GeneRIF: ACER2 has broad substrate specificity and requires Ca(2+)
            for its activity; ACER2 has the cytosolic C terminus and luminal N
            terminus, which are essential for its activity, correct cellular
            localization, and regulation for protein glycosylation
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Sun,W., Hu,W., Xu,R., Jin,J., Szulc,Z.M., Zhang,G., Galadari,S.H.,
            Obeid,L.M. and Mao,C.
  TITLE     Alkaline ceramidase 2 regulates beta1 integrin maturation and cell
            adhesion
  JOURNAL   FASEB J 23 (2), 656-666 (2009)
   PUBMED   18945876
  REMARK    GeneRIF: ACER2/sphingosine pathway plays an important role in
            regulating beta1 maturation and cell adhesion mediated by beta1
            integrins
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Xu,R., Jin,J., Hu,W., Sun,W., Bielawski,J., Szulc,Z., Taha,T.,
            Obeid,L.M. and Mao,C.
  TITLE     Golgi alkaline ceramidase regulates cell proliferation and survival
            by controlling levels of sphingosine and S1P
  JOURNAL   FASEB J 20 (11), 1813-1825 (2006)
   PUBMED   16940153
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK123581.1, AY312516.1, BC092487.1 and AL158206.8.
            
            On Jul 20, 2005 this sequence version replaced NP_001010887.1.
            
            Summary: The sphingolipid metabolite sphingosine-1-phosphate
            promotes cell proliferation and survival, whereas its precursor,
            sphingosine, has the opposite effect. The ceramidase ACER2
            hydrolyzes very long chain ceramides to generate sphingosine (Xu et
            al., 2006 [PubMed 16940153]).[supplied by OMIM, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.78002.1,
                                           SRR1660805.128610.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340967.3/ ENSP00000342609.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p22.1"
     Protein         1..275
                     /product="alkaline ceramidase 2"
                     /EC_number="3.5.1.23"
                     /note="ceramide hydrolase; haCER2; alkCDase 2; alkaline
                     CDase 2"
                     /calculated_mol_wt=31178
     Region          1..13
                     /region_name="Required for proper localization to the
                     Golgi apparatus. /evidence=ECO:0000269|PubMed:20089856"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJU3.2)"
     Region          13..262
                     /region_name="Ceramidase"
                     /note="pfam05875"
                     /db_xref="CDD:461766"
     Site            23
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5QJU3.2)"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJU3.2)"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJU3.2)"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJU3.2)"
     Site            125..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJU3.2)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJU3.2)"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJU3.2)"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJU3.2)"
     CDS             1..275
                     /gene="ACER2"
                     /gene_synonym="ALKCDase2; ASAH3L"
                     /coded_by="NM_001010887.3:77..904"
                     /db_xref="CCDS:CCDS34992.1"
                     /db_xref="GeneID:340485"
                     /db_xref="HGNC:HGNC:23675"
                     /db_xref="MIM:613492"
ORIGIN      
        1 mgaphwwdql qagssevdwc ednytivpai aefyntisnv lffilppicm clfrqyatcf
       61 nsgiyliwtl lvvvgigsvy fhatlsflgq mldelavlwv lmcalamwfp rrylpkifrn
      121 drgrfkvvvs vlsavttcla fvkpainnis lmtlgvpcta lliaelkrcd nmrvfklglf
      181 sglwwtlalf cwisdrafce llssfnfpyl hcmwhilicl aaylgcvcfa yfdaaseipe
      241 qgpvikfwpn ekwafigvpy vsllcankks svkit
//
LOCUS       NP_083051                501 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome P450 2S1 [Mus musculus].
ACCESSION   NP_083051
VERSION     NP_083051.1
DBSOURCE    REFSEQ: accession NM_028775.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Schwartz,B., Levi,H., Menon,G., Maria,R., Upcher,A., Kotlovski,Y.,
            Oss-Ronen,L. and Cohen,I.
  TITLE     ZNF750 Regulates Skin Barrier Function by Driving Cornified
            Envelope and Lipid Processing Pathways
  JOURNAL   J Invest Dermatol 144 (2), 296-306 (2024)
   PUBMED   37660780
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Fekry,M.I., Xiao,Y., Berg,J.Z. and Guengerich,F.P.
  TITLE     A Role for the Orphan Human Cytochrome P450 2S1 in Polyunsaturated
            Fatty Acid omega-1 Hydroxylation Using an Untargeted Metabolomic
            Approach
  JOURNAL   Drug Metab Dispos 47 (11), 1325-1332 (2019)
   PUBMED   31511258
  REMARK    GeneRIF: P450 2S1 is a fatty acid omega-1 hydroxylase, although the
            physiologic relevance of these oxidations remains to be
            established.
            Erratum:[Drug Metab Dispos. 2020 Mar;48(3):159. doi:
            10.1124/dmd.119.089086err. PMID: 32001573]
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Wu,D., Schieren,I., Qian,Y., Zhang,C., Jessell,T.M. and de
            Nooij,J.C.
  TITLE     A Role for Sensory end Organ-Derived Signals in Regulating Muscle
            Spindle Proprioceptor Phenotype
  JOURNAL   J Neurosci 39 (22), 4252-4267 (2019)
   PUBMED   30926747
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Li,L., Megaraj,V., Wei,Y. and Ding,X.
  TITLE     Identification of cytochrome P450 enzymes critical for lung
            tumorigenesis by the tobacco-specific carcinogen
            4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK): insights from
            a novel Cyp2abfgs-null mouse
  JOURNAL   Carcinogenesis 35 (11), 2584-2591 (2014)
   PUBMED   25173884
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Fromel,T., Kohlstedt,K., Popp,R., Yin,X., Awwad,K.,
            Barbosa-Sicard,E., Thomas,A.C., Lieberz,R., Mayr,M. and Fleming,I.
  TITLE     Cytochrome P4502S1: a novel monocyte/macrophage fatty acid
            epoxygenase in human atherosclerotic plaques
  JOURNAL   Basic Res Cardiol 108 (1), 319 (2013)
   PUBMED   23224081
  REMARK    GeneRIF: no Cyp2s1 protein was detected in aortae from wild-type
            mice it was expressed in aortae and macrophage foam cells from
            ApoE(-/-) mice
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Wei,Y., Li,L., Zhou,X., Zhang,Q.Y., Dunbar,A., Liu,F.,
            Kluetzman,K., Yang,W. and Ding,X.
  TITLE     Generation and characterization of a novel Cyp2a(4/5)bgs-null mouse
            model
  JOURNAL   Drug Metab Dispos 41 (1), 132-140 (2013)
   PUBMED   23073733
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Rivera,S.P., Wang,F., Saarikoski,S.T., Taylor,R.T., Chapman,B.,
            Zhang,R. and Hankinson,O.
  TITLE     A novel promoter element containing multiple overlapping xenobiotic
            and hypoxia response elements mediates induction of cytochrome
            P4502S1 by both dioxin and hypoxia
  JOURNAL   J Biol Chem 282 (15), 10881-10893 (2007)
   PUBMED   17277313
  REMARK    GeneRIF: identify a novel regulatory cassette that mediates changes
            in Cyp2s1 expression
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Choudhary,D., Jansson,I., Stoilov,I., Sarfarazi,M. and
            Schenkman,J.B.
  TITLE     Expression patterns of mouse and human CYP orthologs (families 1-4)
            during development and in different adult tissues
  JOURNAL   Arch Biochem Biophys 436 (1), 50-61 (2005)
   PUBMED   15752708
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Wang,H., Donley,K.M., Keeney,D.S. and Hoffman,S.M.
  TITLE     Organization and evolution of the Cyp2 gene cluster on mouse
            chromosome 7, and comparison with the syntenic human cluster
  JOURNAL   Environ Health Perspect 111 (15), 1835-1842 (2003)
   PUBMED   14630516
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Choudhary,D., Jansson,I., Schenkman,J.B., Sarfarazi,M. and
            Stoilov,I.
  TITLE     Comparative expression profiling of 40 mouse cytochrome P450 genes
            in embryonic and adult tissues
  JOURNAL   Arch Biochem Biophys 414 (1), 91-100 (2003)
   PUBMED   12745259
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC119211.8.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064733.1, AK004699.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 14.05 cM"
     Protein         1..501
                     /product="cytochrome P450 2S1"
                     /EC_number="5.3.99.5"
                     /EC_number="4.2.1.152"
                     /note="thromboxane-A synthase; hydroperoxy
                     icosatetraenoate dehydratase"
                     /calculated_mol_wt=55501
     Region          65..491
                     /region_name="CYP2"
                     /note="cytochrome P450 family 2; cd11026"
                     /db_xref="CDD:410652"
     Site            order(102,117..118,125,129,300,303..304,307..308,311,362,
                     368,372,374,397,433..435,439,441..443,446..447)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410652"
     Site            order(105,118..119,206,209..210,213,242,245..246,249,295,
                     298..299,302..303,307,368,372,482..483)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410652"
     CDS             1..501
                     /gene="Cyp2s1"
                     /gene_synonym="1200011C15Rik; CYPIIS1"
                     /coded_by="NM_028775.4:24..1529"
                     /db_xref="CCDS:CCDS20997.1"
                     /db_xref="GeneID:74134"
                     /db_xref="MGI:MGI:1921384"
ORIGIN      
        1 meaastwall lallllllll sltlfrtpar gylppgptpl pllgnllqlr pgalysgllr
       61 lskkygpvft vylgpwrrvv vlvghdavre alggqaeefs grgtlatldk tfdghgvffa
      121 ngerwkqlrk ftllalrdlg mgkregeeli qaevqslvea fqktegrpfn psmllaqats
      181 nvvcslvfgi rlpyddkefq aviqaasgtl lgisspwgqa yemfswllqp lpgphtqlqh
      241 hlgtlaafti qqvqkhqgrf qtsgpardvv dafllkmaqe kqdpgtefte knllmtvtyl
      301 lfagtmtiga tiryalllll rypqvqqrvr eeliqelgpg rapslsdrvr lpytdavlhe
      361 aqrllalvpm gmphtitrtt cfrgytlpkg tevfpligsi lhdpavfqnp gefhpgrfld
      421 edgrlrkhea flpyslgkrv clgeglarae lwlfftsilq afsletpcpp gdlslkpais
      481 glfnippdfq lrvwptgdqs r
//
LOCUS       NP_001354977            1334 aa            linear   PRI 27-APR-2025
DEFINITION  nck-associated protein 5-like [Homo sapiens].
ACCESSION   NP_001354977 XP_011536912
VERSION     NP_001354977.1
DBSOURCE    REFSEQ: accession NM_001368048.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1334)
  AUTHORS   Shintomi,M., Shiratori,M., Negishi,L. and Terada,Y.
  TITLE     Identification of Cep169-interacting proteins and the in vivo
            modification sites of Cep169 via proteomic analysis
  JOURNAL   Biochem Biophys Res Commun 495 (3), 2275-2281 (2018)
   PUBMED   29269292
  REMARK    GeneRIF: Our findings suggest that Cep169 regulates cell growth by
            interacting with multiple proteins.
REFERENCE   2  (residues 1 to 1334)
  AUTHORS   Mori,Y., Inoue,Y., Taniyama,Y., Tanaka,S. and Terada,Y.
  TITLE     Phosphorylation of the centrosomal protein, Cep169, by Cdk1
            promotes its dissociation from centrosomes in mitosis
  JOURNAL   Biochem Biophys Res Commun 468 (4), 642-646 (2015)
   PUBMED   26549230
  REMARK    GeneRIF: These data suggest that the dissociation of Cep169 from
            centrosomes is controlled by Cdk1/Cyclin B during mitosis, and that
            Cep169 might regulate MT dynamics of mitotic spindle.
REFERENCE   3  (residues 1 to 1334)
  AUTHORS   Mori,Y., Inoue,Y., Tanaka,S., Doda,S., Yamanaka,S., Fukuchi,H. and
            Terada,Y.
  TITLE     Cep169, a Novel Microtubule Plus-End-Tracking Centrosomal Protein,
            Binds to CDK5RAP2 and Regulates Microtubule Stability
  JOURNAL   PLoS One 10 (10), e0140968 (2015)
   PUBMED   26485573
  REMARK    GeneRIF: These results show that Cep169 targets microtubule tips
            and regulates stability of microtubules with CDK5RAP2.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131157.4.
            
            On Jan 9, 2019 this sequence version replaced XP_011536912.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2158841.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..1334
                     /product="nck-associated protein 5-like"
                     /note="NCKAP5-like; centrosomal protein of 169 kDa"
                     /calculated_mol_wt=139331
     Region          1..139
                     /region_name="Mediates interaction with CDK5RAP2 and is
                     required for homodimerization and microtubule bundle
                     formation. /evidence=ECO:0000269|PubMed:26482847,
                     ECO:0000269|PubMed:26485573"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          115..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          210..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          <214..663
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          266..316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          349..711
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          484..487
                     /region_name="(S/T)X(I/L)P motif 1.
                     /evidence=ECO:0000269|PubMed:26482847,
                     ECO:0000269|PubMed:26485573"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            577
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          750..1146
                     /region_name="Mediates interaction with beta-tubulin and
                     is required for microtubule bundle formation.
                     /evidence=ECO:0000269|PubMed:26482847"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          782..884
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          816..819
                     /region_name="(S/T)X(I/L)P motif 2.
                     /evidence=ECO:0000269|PubMed:26482847,
                     ECO:0000269|PubMed:26485573"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          879..1181
                     /region_name="NCKAP5"
                     /note="Nck-associated protein 5, Peripheral clock protein;
                     pfam15246"
                     /db_xref="CDD:464586"
     Region          926..929
                     /region_name="(S/T)X(I/L)P motif 3, required for
                     interaction with MAPRE1.
                     /evidence=ECO:0000269|PubMed:26482847,
                     ECO:0000269|PubMed:26485573"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          931..953
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          986..1015
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          1030..1183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            1194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          1197..1334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     CDS             1..1334
                     /gene="NCKAP5L"
                     /gene_synonym="Cep169; FP1193; KIAA1602"
                     /coded_by="NM_001368048.1:270..4274"
                     /db_xref="CCDS:CCDS41781.2"
                     /db_xref="GeneID:57701"
                     /db_xref="HGNC:HGNC:29321"
                     /db_xref="MIM:615104"
ORIGIN      
        1 mseamdqpag gpgnprpgeg ddgsmepgtc qellhrlrel eaensalaqa nenqretyer
       61 cldevanhvv qallnqkdlr eeciklkkrv fdlerqnqml salfqqklql ttgslpqipl
      121 tplqppsepp aspslssteg paaplplghc agqrevcweq qlrpggpgpp aapppaldal
      181 spflrkkaqi levlraleet dplllcspat pwrppgqgpg spepingelc gppqpepspw
      241 apclllgpgn lggllhwerl lgglggeedt grpwgpsrgp pqaqgtssgp ncapgsssss
      301 ssdeagdpne apspdtllga larrqlnlgq lledtesylq aflagaagpl ngdhpgpgqs
      361 sspdqappql skskglpksa wgggtpeahr pgfgatsegq gplpflsmfm gagdaplgsr
      421 pghphsssqv ksklqigpps pgeaqgpllp sparglkflk lpptseksps pggpqlspql
      481 prnsripcrn sgsdgspspl larrglggge lspegaqglp tspspcyttp dstqlrppqs
      541 alsttlspgp vvspcyenil dlsrstfrgp spepppsplq vptypqltle vpqapevlrs
      601 pgvppspclp esypygspqe ksldkagses phpgrrtpgn sskkpsqgsg rrpgdpgstp
      661 lrdrlaalgk lktgpegalg sekngvparp gtektrgpgk sgesagdmvp sihrpleqle
      721 akggirgava lgtnslkqqe pglmgdpgar vysshsmgar vdlepvsprs cltkvelaks
      781 rlagalcpqv prtpakvpts apslgkpnks phssptklps ksptkvvprp gaplvtkesp
      841 kpdkgkgppw adcgsttaqs tplvpgptdp sqgpeglaph saieekvmkg ieenvlrlqg
      901 qerapgaevk hrntssiasw fglkksklpa lnrrteatkn kegagggspl rrevkmeark
      961 leaeslnisk lmakaedlrr aleeekayls srarprpggp apgpntglgq vqgqlagmyq
     1021 gadtfmqqll nrvdgkelps kswrepkpey gdfqpvssdp kspwpacgpr nglvgplqgc
     1081 gkppgkpsse pgrreempse dslaepvpts hftacgsltr tldsgigtfp ppdhgssgtp
     1141 sknlpktkpp rldpppgvpp arpppltkvp rrahtlerev pgieellvsg rhpsmpafpa
     1201 llpaapghrg hetcpddpce dpgptppvql aknwtfpntr aagsssdplm cpprqleglp
     1261 rtpmalpvdr krsqepsrps ptpqgppfgg srtpstsdma eegrvasggp pgletsesls
     1321 dslydslssc gsqg
//
LOCUS       NP_004510                872 aa            linear   PRI 27-APR-2025
DEFINITION  potassium voltage-gated channel subfamily KQT member 3 isoform 1
            [Homo sapiens].
ACCESSION   NP_004510
VERSION     NP_004510.1
DBSOURCE    REFSEQ: accession NM_004519.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 872)
  AUTHORS   Jiang,S., Liu,B., Lin,K., Li,L., Li,R., Tan,S., Zhang,X., Jiang,L.,
            Ni,H., Wang,Y., Ding,H., Hu,J., Qian,H. and Ge,R.
  TITLE     Impacted spike frequency adaptation associated with reduction of
            KCNQ2/3 exacerbates seizure activity in temporal lobe epilepsy
  JOURNAL   Hippocampus 34 (2), 58-72 (2024)
   PUBMED   38049972
  REMARK    GeneRIF: Impacted spike frequency adaptation associated with
            reduction of KCNQ2/3 exacerbates seizure activity in temporal lobe
            epilepsy.
REFERENCE   2  (residues 1 to 872)
  AUTHORS   Foley,K., Shorthouse,D., Rahrmann,E., Zhuang,L., Devonshire,G.,
            Gilbertson,R.J., Fitzgerald,R.C. and Hall,B.A.
  CONSRTM   OCCAMS consortium
  TITLE     SMAD4 and KCNQ3 alterations are associated with lymph node
            metastases in oesophageal adenocarcinoma
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (1), 166867 (2024)
   PUBMED   37648039
  REMARK    GeneRIF: SMAD4 and KCNQ3 alterations are associated with lymph node
            metastases in oesophageal adenocarcinoma.
REFERENCE   3  (residues 1 to 872)
  AUTHORS   Arredondo,K., Myers,C., Hansen-Kiss,E., Mathew,M.T., Jayaraman,V.,
            Siemon,A., Bartholomew,D., Herman,G.E. and Mori,M.
  TITLE     Phenotypic Spectrum in a Family Sharing a Heterozygous KCNQ3
            Variant
  JOURNAL   J Child Neurol 37 (6), 517-523 (2022)
   PUBMED   35384780
  REMARK    GeneRIF: Phenotypic Spectrum in a Family Sharing a Heterozygous
            KCNQ3 Variant.
REFERENCE   4  (residues 1 to 872)
  AUTHORS   Miyake,N., Heydari,S., Garshasbi,M., Saitoh,S., Nasiri,J.,
            Hamanaka,K., Takata,A., Matsumoto,N., Beheshti,F.H. and
            Chaleshtori,A.R.S.
  TITLE     The identification of two pathogenic variants in a family with mild
            and severe forms of developmental delay
  JOURNAL   J Hum Genet 66 (4), 445-448 (2021)
   PUBMED   33037390
  REMARK    GeneRIF: The identification of two pathogenic variants in a family
            with mild and severe forms of developmental delay.
REFERENCE   5  (residues 1 to 872)
  AUTHORS   Wang,H.S., Pan,Z., Shi,W., Brown,B.S., Wymore,R.S., Cohen,I.S.,
            Dixon,J.E. and McKinnon,D.
  TITLE     KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of
            the M-channel
  JOURNAL   Science 282 (5395), 1890-1893 (1998)
   PUBMED   9836639
REFERENCE   6  (residues 1 to 872)
  AUTHORS   Yang,W.P., Levesque,P.C., Little,W.A., Conder,M.L.,
            Ramakrishnan,P., Neubauer,M.G. and Blanar,M.A.
  TITLE     Functional expression of two KvLQT1-related potassium channels
            responsible for an inherited idiopathic epilepsy
  JOURNAL   J Biol Chem 273 (31), 19419-19423 (1998)
   PUBMED   9677360
REFERENCE   7  (residues 1 to 872)
  AUTHORS   Charlier,C., Singh,N.A., Ryan,S.G., Lewis,T.B., Reus,B.E.,
            Leach,R.J. and Leppert,M.
  TITLE     A pore mutation in a novel KQT-like potassium channel gene in an
            idiopathic epilepsy family
  JOURNAL   Nat Genet 18 (1), 53-55 (1998)
   PUBMED   9425900
REFERENCE   8  (residues 1 to 872)
  AUTHORS   Miceli,F., Soldovieri,M.V., Weckhuysen,S., Cooper,E.C. and
            Taglialatela,M.
  TITLE     KCNQ3-Related Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24851285
REFERENCE   9  (residues 1 to 872)
  AUTHORS   Miceli,F., Soldovieri,M.V., Weckhuysen,S., Cooper,E. and
            Taglialatela,M.
  TITLE     KCNQ2-Related Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20437616
REFERENCE   10 (residues 1 to 872)
  AUTHORS   Ryan,S.G., Wiznitzer,M., Hollman,C., Torres,M.C., Szekeresova,M.
            and Schneider,S.
  TITLE     Benign familial neonatal convulsions: evidence for clinical and
            genetic heterogeneity
  JOURNAL   Ann Neurol 29 (5), 469-473 (1991)
   PUBMED   1859177
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018540.13, AF033347.1,
            AV728013.1, AC131042.6 and BX538233.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that functions in the
            regulation of neuronal excitability. The encoded protein forms an
            M-channel by associating with the products of the related KCNQ2 or
            KCNQ5 genes, which both encode integral membrane proteins.
            M-channel currents are inhibited by M1 muscarinic acetylcholine
            receptors and are activated by retigabine, a novel anti-convulsant
            drug. Defects in this gene are a cause of benign familial neonatal
            convulsions type 2 (BFNC2), also known as epilepsy, benign neonatal
            type 2 (EBN2). Alternative splicing of this gene results in
            multiple transcript variants. [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1). The 5' extent of
            this variant is inferred based on orthologous alignments.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF033347.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000388996.10/ ENSP00000373648.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.22"
     Protein         1..872
                     /product="potassium voltage-gated channel subfamily KQT
                     member 3 isoform 1"
                     /note="potassium channel, voltage-gated, subfamily Q,
                     member 3; potassium channel subunit alpha KvLQT3;
                     voltage-gated potassium channel subunit Kv7.3; potassium
                     voltage-gated channel, KQT-like subfamily, member 3;
                     potassium channel, voltage gated KQT-like subfamily Q,
                     member 3"
                     /calculated_mol_wt=96612
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88944; propagated from
                     UniProtKB/Swiss-Prot (O43525.2)"
     Region          121..363
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            121..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Site            154..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Site            194..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Site            226..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:16319223; propagated from
                     UniProtKB/Swiss-Prot (O43525.2)"
     Site            257..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Region          316..321
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Site            327..353
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Region          356..537
                     /region_name="Mediates interaction with calmodulin.
                     /evidence=ECO:0000269|PubMed:27564677"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Region          446..650
                     /region_name="KCNQ_channel"
                     /note="KCNQ voltage-gated potassium channel; pfam03520"
                     /db_xref="CDD:460954"
     Region          575..611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Region          764..872
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43525.2)"
     Region          770..866
                     /region_name="KCNQC3-Ank-G_bd"
                     /note="Ankyrin-G binding motif of KCNQ2-3; pfam11956"
                     /db_xref="CDD:463411"
     CDS             1..872
                     /gene="KCNQ3"
                     /gene_synonym="BFNC2; EBN2; KV7.3"
                     /coded_by="NM_004519.4:564..3182"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34943.1"
                     /db_xref="GeneID:3786"
                     /db_xref="HGNC:HGNC:6297"
                     /db_xref="MIM:602232"
ORIGIN      
        1 mglkarraag aaggggdggg ggggaanpag gdaaaagdee rkvglapgdv eqvtlalgag
       61 adkdgtllle gggrdegqrr tpqgigllak tplsrpvkrn nakyrriqtl iydalerprg
      121 wallyhalvf livlgclila vlttfkeyet vsgdwlllle tfaififgae falriwaagc
      181 ccrykgwrgr lkfarkplcm ldifvliasv pvvavgnqgn vlatslrslr flqilrmlrm
      241 drrggtwkll gsaicahske litawyigfl tlilssflvy lvekdvpevd aqgeemkeef
      301 etyadalwwg litlatigyg dktpktwegr liaatfslig vsffalpagi lgsglalkvq
      361 eqhrqkhfek rrkpaaeliq aawryyatnp nridlvatwr fyesvvsfpf frkeqleaas
      421 sqklglldrv rlsnprgsnt kgklftplnv daieespske pkpvglnnke rfrtafrmka
      481 yafwqsseda gtgdpmaedr gygndfpied miptlkaair avrilqfrly kkkfketlrp
      541 ydvkdvieqy saghldmlsr ikylqtridm iftpgppstp khkksqkgsa ftfpsqqspr
      601 nepyvarpst seiedqsmmg kfvkverqvq dmgkkldflv dmhmqhmerl qvqvteyypt
      661 kgtsspaeae kkednrysdl ktiicnyset gppeppysfh qvtidkvspy gffahdpvnl
      721 prggpssgkv qatppssatt yverptvlpi ltlldsrvsc hsqadlqgpy sdrisprqrr
      781 sitrdsdtpl slmsvnheel erspsgfsis qdrddyvfgp nggsswmrek rylaegetdt
      841 dtdpftpsgs mplsstgdgi sdsvwtpsnk pi
//
LOCUS       NP_000386                897 aa            linear   PRI 27-APR-2025
DEFINITION  cytokine receptor common subunit beta isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_000386
VERSION     NP_000386.1
DBSOURCE    REFSEQ: accession NM_000395.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 897)
  AUTHORS   Charlet,A., Kappenstein,M., Keye,P., Klasener,K., Endres,C.,
            Poggio,T., Gorantla,S.P., Kreutmair,S., Sanger,J., Illert,A.L.,
            Miething,C., Reth,M., Duyster,J., Rummelt,C. and von Bubnoff,N.
  TITLE     The IL-3, IL-5, and GM-CSF common receptor beta chain mediates
            oncogenic activity of FLT3-ITD-positive AML
  JOURNAL   Leukemia 36 (3), 701-711 (2022)
   PUBMED   34750506
  REMARK    GeneRIF: The IL-3, IL-5, and GM-CSF common receptor beta chain
            mediates oncogenic activity of FLT3-ITD-positive AML.
REFERENCE   2  (residues 1 to 897)
  AUTHORS   Rashid,M., Ali,R., Almuzzaini,B., Song,H., AlHallaj,A.,
            Abdulkarim,A.A., Mohamed Baz,O., Al Zahrani,H., Mustafa Sabeena,M.,
            Alharbi,W., Hussein,M. and Boudjelal,M.
  TITLE     Discovery of a novel potentially transforming somatic mutation in
            CSF2RB gene in breast cancer
  JOURNAL   Cancer Med 10 (22), 8138-8150 (2021)
   PUBMED   34729943
  REMARK    GeneRIF: Discovery of a novel potentially transforming somatic
            mutation in CSF2RB gene in breast cancer.
REFERENCE   3  (residues 1 to 897)
  AUTHORS   Sakaue,S., Yamaguchi,E., Inoue,Y., Takahashi,M., Hirata,J.,
            Suzuki,K., Ito,S., Arai,T., Hirose,M., Tanino,Y., Nikaido,T.,
            Ichiwata,T., Ohkouchi,S., Hirano,T., Takada,T., Miyawaki,S.,
            Dofuku,S., Maeda,Y., Nii,T., Kishikawa,T., Ogawa,K., Masuda,T.,
            Yamamoto,K., Sonehara,K., Tazawa,R., Morimoto,K., Takaki,M.,
            Konno,S., Suzuki,M., Tomii,K., Nakagawa,A., Handa,T., Tanizawa,K.,
            Ishii,H., Ishida,M., Kato,T., Takeda,N., Yokomura,K., Matsui,T.,
            Watanabe,M., Inoue,H., Imaizumi,K., Goto,Y., Kida,H., Fujisawa,T.,
            Suda,T., Yamada,T., Satake,Y., Ibata,H., Hizawa,N., Mochizuki,H.,
            Kumanogoh,A., Matsuda,F., Nakata,K., Hirota,T., Tamari,M. and
            Okada,Y.
  TITLE     Genetic determinants of risk in autoimmune pulmonary alveolar
            proteinosis
  JOURNAL   Nat Commun 12 (1), 1032 (2021)
   PUBMED   33589587
  REMARK    GeneRIF: Genetic determinants of risk in autoimmune pulmonary
            alveolar proteinosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 897)
  AUTHORS   Schulte,V., Sipol,A., Burdach,S. and Rieger-Fackeldey,E.
  TITLE     The Truncated Splice Variant of the
            Granulocyte-Macrophage-Colony-Stimulating Factor Receptor beta-
            Chain in Peripheral Blood Serves as Severity Biomarker of
            Respiratory Failure in Newborns
  JOURNAL   Neonatology 118 (2), 187-193 (2021)
   PUBMED   33784678
  REMARK    GeneRIF: The Truncated Splice Variant of the
            Granulocyte-Macrophage-Colony-Stimulating Factor Receptor beta-
            Chain in Peripheral Blood Serves as Severity Biomarker of
            Respiratory Failure in Newborns.
REFERENCE   5  (residues 1 to 897)
  AUTHORS   Denson,L.A., Jurickova,I., Karns,R., Shaw,K.A., Cutler,D.J.,
            Okou,D., Valencia,C.A., Dodd,A., Mondal,K., Aronow,B.J.,
            Haberman,Y., Linn,A., Price,A., Bezold,R., Lake,K., Jackson,K.,
            Walters,T.D., Griffiths,A., Baldassano,R.N., Noe,J.D., Hyams,J.S.,
            Crandall,W.V., Kirschner,B.S., Heyman,M.B., Snapper,S.,
            Guthery,S.L., Dubinsky,M.C., Leleiko,N.S., Otley,A.R., Xavier,R.J.,
            Stevens,C., Daly,M.J., Zwick,M.E. and Kugathasan,S.
  TITLE     Genetic and Transcriptomic Variation Linked to Neutrophil
            Granulocyte-Macrophage Colony-Stimulating Factor Signaling in
            Pediatric Crohn's Disease
  JOURNAL   Inflamm Bowel Dis 25 (3), 547-560 (2019)
   PUBMED   30124884
  REMARK    GeneRIF: Missense mutations in CSF2RB gene is associated with
            Pediatric Crohn's Disease.
REFERENCE   6  (residues 1 to 897)
  AUTHORS   Sakamaki,K., Miyajima,I., Kitamura,T. and Miyajima,A.
  TITLE     Critical cytoplasmic domains of the common beta subunit of the
            human GM-CSF, IL-3 and IL-5 receptors for growth signal
            transduction and tyrosine phosphorylation
  JOURNAL   EMBO J 11 (10), 3541-3549 (1992)
   PUBMED   1396555
REFERENCE   7  (residues 1 to 897)
  AUTHORS   Torigoe,T., O'Connor,R., Santoli,D. and Reed,J.C.
  TITLE     Interleukin-3 regulates the activity of the LYN protein-tyrosine
            kinase in myeloid-committed leukemic cell lines
  JOURNAL   Blood 80 (3), 617-624 (1992)
   PUBMED   1638019
REFERENCE   8  (residues 1 to 897)
  AUTHORS   Tavernier,J., Tuypens,T., Plaetinck,G., Verhee,A., Fiers,W. and
            Devos,R.
  TITLE     Molecular basis of the membrane-anchored and two soluble isoforms
            of the human interleukin 5 receptor alpha subunit
  JOURNAL   Proc Natl Acad Sci U S A 89 (15), 7041-7045 (1992)
   PUBMED   1495999
REFERENCE   9  (residues 1 to 897)
  AUTHORS   Shen,Y., Baker,E., Callen,D.F., Sutherland,G.R., Willson,T.A.,
            Rakar,S. and Gough,N.M.
  TITLE     Localization of the human GM-CSF receptor beta chain gene (CSF2RB)
            to chromosome 22q12.2-->q13.1
  JOURNAL   Cytogenet Cell Genet 61 (3), 175-177 (1992)
   PUBMED   1424804
REFERENCE   10 (residues 1 to 897)
  AUTHORS   Hayashida,K., Kitamura,T., Gorman,D.M., Arai,K., Yokota,T. and
            Miyajima,A.
  TITLE     Molecular cloning of a second subunit of the receptor for human
            granulocyte-macrophage colony-stimulating factor (GM-CSF):
            reconstitution of a high-affinity GM-CSF receptor
  JOURNAL   Proc Natl Acad Sci U S A 87 (24), 9655-9659 (1990)
   PUBMED   1702217
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL008637.1, BC070085.1 and
            AL133392.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is the common beta chain
            of the high affinity receptor for IL-3, IL-5 and CSF. Defects in
            this gene have been reported to be associated with protein alveolar
            proteinosis (PAP). [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2969825.1,
                                           SRR14038194.2573355.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000403662.8/ ENSP00000384053.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..897
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..897
                     /product="cytokine receptor common subunit beta isoform 2
                     precursor"
                     /note="interleukin 3 receptor/granulocyte-macrophage
                     colony stimulating factor 3 receptor, beta (high
                     affinity); cytokine receptor common subunit beta;
                     GM-CSF/IL-3/IL-5 receptor common beta-chain;
                     colony-stimulating factor-2 receptor, beta, low-affinity;
                     colony stimulating factor 2 receptor, beta, low-affinity
                     (granulocyte-macrophage); GM-CSF/IL-3/IL-5 receptor common
                     beta subunit; beta common cytokine receptor; beta-GM-CSF
                     receptor; colony stimulating factor 2 receptor beta common
                     subunit"
                     /calculated_mol_wt=95707
     sig_peptide     1..16
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
                     /calculated_mol_wt=1647
     mat_peptide     17..897
                     /product="Cytokine receptor common subunit beta.
                     /id=PRO_0000010862"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
                     /calculated_mol_wt=95707
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16754968,
                     ECO:0000269|PubMed:18692472; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Region          133..233
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(133,204,219)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16754968,
                     ECO:0000269|PubMed:18692472; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Site            order(226..227,229..230)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          247..>324
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Region          341..436
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            346
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Region          425..429
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Site            order(425..426,428..429)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            444..460
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          474..482
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          498..517
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          532..630
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          <548..867
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          648..812
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P26955; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Region          830..849
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     CDS             1..897
                     /gene="CSF2RB"
                     /gene_synonym="betaGMR; CD131; CDw131; IL3RB; IL5RB;
                     SMDP5"
                     /coded_by="NM_000395.3:223..2916"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS13936.1"
                     /db_xref="GeneID:1439"
                     /db_xref="HGNC:HGNC:2436"
                     /db_xref="MIM:138981"
ORIGIN      
        1 mvlaqgllsm allalcwers lagaeetipl qtlrcyndyt shitcrwadt qdaqrlvnvt
       61 lirrvnedll epvscdlsdd mpwsacphpr cvprrcvipc qsfvvtdvdy fsfqpdrplg
      121 trltvtltqh vqppeprdlq istdqdhfll twsvalgspq shwlspgdle fevvykrlqd
      181 swedaaills ntsqatlgpe hlmpsstyva rvrtrlapgs rlsgrpskws pevcwdsqpg
      241 deaqpqnlec ffdgaavlsc swevrkevas svsfglfykp spdageeecs pvlreglgsl
      301 htrhhcqipv pdpathgqyi vsvqprraek hikssvniqm appslnvtkd gdsyslrwet
      361 mkmryehidh tfeiqyrkdt atwkdsktet lqnahsmalp alepstrywa rvrvrtsrtg
      421 yngiwsewse arswdtesvl pmwvlalivi fltiavllal rfcgiygyrl rrkweekipn
      481 pskshlfqng saelwppgsm saftsgspph qgpwgsrfpe legvfpvgfg dsevspltie
      541 dpkhvcdpps gpdttpaasd lpteqppspq pgppaashtp ekqassfdfn gpylgpphsr
      601 slpdilgqpe ppqeggsqks pppgsleylc lpaggqvqlv plaqamgpgq aveverrpsq
      661 gaagspsles gggpappalg prvggqdqkd spvaipmssg dtedpgvasg yvssadlvft
      721 pnsgassvsl vpslglpsdq tpslcpglas gppgapgpvk sgfegyvelp piegrsprsp
      781 rnnpvppeak spvlnpgerp advsptspqp egllvlqqvg dycflpglgp gplslrskps
      841 spgpgpeikn ldqafqvkkp pgqavpqvpv iqlfkalkqq dylslppwev nkpgevc
//
LOCUS       NP_001025168             571 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 181 isoform 1 [Homo sapiens].
ACCESSION   NP_001025168 XP_290835
VERSION     NP_001025168.2
DBSOURCE    REFSEQ: accession NM_001029997.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Wang,R., Cukerman,E., Heng,H.H. and Liew,C.C.
  TITLE     Identification of a locus of zinc finger genes in human chromosome
            19q13.1-q13.3 region by fluorescence in situ hybridization
  JOURNAL   Somat Cell Mol Genet 22 (3), 245-248 (1996)
   PUBMED   8914611
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020910.7, DC304794.1, DC299701.1, BC104759.1, AK297316.1 and
            AI800428.1.
            
            On Mar 6, 2009 this sequence version replaced NP_001025168.1.
            
            Summary: Zinc finger proteins have been shown to interact with
            nucleic acids and to have diverse functions. The zinc finger domain
            is a conserved amino acid sequence motif containing 2 specifically
            positioned cysteines and 2 histidines that are involved in
            coordinating zinc. Kruppel-related proteins form 1 family of zinc
            finger proteins. See MIM 604749 for additional information on zinc
            finger proteins.[supplied by OMIM, Jul 2003].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.213776.1,
                                           SRR1660809.238763.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000492450.3/ ENSP00000420727.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..571
                     /product="zinc finger protein 181 isoform 1"
                     /calculated_mol_wt=65711
     Region          4..65
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          211..>539
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          239..259
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          267..287
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          295..315
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          323..343
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(328,330,332,334..335,338..339,342,356,358,362..363,
                     366..367,370,384,386,388,390..391,394..395,398)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          351..371
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          379..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          407..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          463..483
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(468,470,472,474..475,478..479,482,496,498,502..503,
                     506..507,510,524,526,528,530..531,534..535,538)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          491..511
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          519..539
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..571
                     /gene="ZNF181"
                     /gene_synonym="HHZ181"
                     /coded_by="NM_001029997.4:796..2511"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32990.2"
                     /db_xref="GeneID:339318"
                     /db_xref="HGNC:HGNC:12971"
                     /db_xref="MIM:606741"
ORIGIN      
        1 mpqvtfndva idftheewgw lssaqrdlyk dvmvqnyenl vsvaglsvtk pyvitlledg
       61 kepwmmekkl skgmipdwes rwenkelstk kdnydedspq tviiekvvkq syefsnskkn
      121 leyieklegk hgsqvdhfrp ailtsrespt adsvykynif rstfhskstl sepqkisaeg
      181 nshkydilkk nlpkksvikn ekvnggkkll nsnksgaafs qgksltlpqt cnrekiytcs
      241 ecgkafgkqs ilnrhwriht gekpyecrec gktfshgssl trhlishsge kpykciecgk
      301 afshvssltn hqsthtgekp yecmncgksf srvshliehl rihtqeklye cricgkafih
      361 rsslihhqki htgekpyecr ecgkafccss hltrhqriht mekqyecnkc lkvfsslsfl
      421 vqhqsihtee kpfecqkcrk sfnqleslnm hlrnhirlkp yecsicgkaf shrssllqhh
      481 rihtgekpye cikcgktfsc ssnltvhqri htgekpykcn ecgkafskgs nltahqrvhn
      541 gekpnsvvsv ekpldymnhy tceksyrret v
//
LOCUS       NP_001291433             347 aa            linear   PRI 27-APR-2025
DEFINITION  high mobility group protein 20A isoform a [Homo sapiens].
ACCESSION   NP_001291433 XP_005254180
VERSION     NP_001291433.1
DBSOURCE    REFSEQ: accession NM_001304504.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Na,L., Meijie,Z., Wenjing,Z., Bing,Z., Yanhao,D., Shanshan,L. and
            Yongle,Q.
  TITLE     HMG20A was identified as a key enhancer driver associated with DNA
            damage repair in oral squamous cell carcinomas
  JOURNAL   BMC Oral Health 22 (1), 473 (2022)
   PUBMED   36335317
  REMARK    GeneRIF: HMG20A was identified as a key enhancer driver associated
            with DNA damage repair in oral squamous cell carcinomas.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Gomez-Marin,E., Posavec-Marjanovic,M., Zarzuela,L.,
            Basurto-Cayuela,L., Guerrero-Martinez,J.A., Arribas,G., Yerbes,R.,
            Ceballos-Chavez,M., Rodriguez-Paredes,M., Tome,M., Duran,R.V.,
            Buschbeck,M. and Reyes,J.C.
  TITLE     The high mobility group protein HMG20A cooperates with the histone
            reader PHF14 to modulate TGFbeta and Hippo pathways
  JOURNAL   Nucleic Acids Res 50 (17), 9838-9857 (2022)
   PUBMED   36124662
  REMARK    GeneRIF: The high mobility group protein HMG20A cooperates with the
            histone reader PHF14 to modulate TGFbeta and Hippo pathways.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Yamamoto,M., Kondo,R., Hozumi,H., Doi,S., Denda,M., Magari,M.,
            Kanayama,N., Hatano,N., Morishita,R. and Tokumitsu,H.
  TITLE     Identification and Biochemical Characterization of High Mobility
            Group Protein 20A as a Novel Ca2+/S100A6 Target
  JOURNAL   Biomolecules 11 (4), 510 (2021)
   PUBMED   33808200
  REMARK    GeneRIF: Identification and Biochemical Characterization of High
            Mobility Group Protein 20A as a Novel Ca(2+)/S100A6 Target.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Huang,T., Wang,L., Bai,M., Zheng,J., Yuan,D., He,Y., Wang,Y.,
            Jin,T. and Cui,W.
  TITLE     Influence of IGF2BP2, HMG20A, and HNF1B genetic polymorphisms on
            the susceptibility to Type 2 diabetes mellitus in Chinese Han
            population
  JOURNAL   Biosci Rep 40 (5) (2020)
   PUBMED   32329795
  REMARK    GeneRIF: Influence of IGF2BP2, HMG20A, and HNF1B genetic
            polymorphisms on the susceptibility to Type 2 diabetes mellitus in
            Chinese Han population.
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Bantscheff,M., Hopf,C., Savitski,M.M., Dittmann,A., Grandi,P.,
            Michon,A.M., Schlegl,J., Abraham,Y., Becher,I., Bergamini,G.,
            Boesche,M., Delling,M., Dumpelfeld,B., Eberhard,D., Huthmacher,C.,
            Mathieson,T., Poeckel,D., Reader,V., Strunk,K., Sweetman,G.,
            Kruse,U., Neubauer,G., Ramsden,N.G. and Drewes,G.
  TITLE     Chemoproteomics profiling of HDAC inhibitors reveals selective
            targeting of HDAC complexes
  JOURNAL   Nat Biotechnol 29 (3), 255-265 (2011)
   PUBMED   21258344
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Nicolas,E., Poitelon,Y., Chouery,E., Salem,N., Levy,N.,
            Megarbane,A. and Delague,V.
  TITLE     CAMOS, a nonprogressive, autosomal recessive, congenital cerebellar
            ataxia, is caused by a mutant zinc-finger protein, ZNF592
  JOURNAL   Eur J Hum Genet 18 (10), 1107-1113 (2010)
   PUBMED   20531441
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Artegiani,B., Labbaye,C., Sferra,A., Quaranta,M.T., Torreri,P.,
            Macchia,G., Ceccarini,M., Petrucci,T.C. and Macioce,P.
  TITLE     The interaction with HMG20a/b proteins suggests a potential role
            for beta-dystrobrevin in neuronal differentiation
  JOURNAL   J Biol Chem 285 (32), 24740-24750 (2010)
   PUBMED   20530487
  REMARK    GeneRIF: beta-dystrobrevin interacts with the HMG20 proteins iBRAF
            and BRAF35
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Ravasi,T., Suzuki,H., Cannistraci,C.V., Katayama,S., Bajic,V.B.,
            Tan,K., Akalin,A., Schmeier,S., Kanamori-Katayama,M., Bertin,N.,
            Carninci,P., Daub,C.O., Forrest,A.R., Gough,J., Grimmond,S.,
            Han,J.H., Hashimoto,T., Hide,W., Hofmann,O., Kamburov,A., Kaur,M.,
            Kawaji,H., Kubosaki,A., Lassmann,T., van Nimwegen,E.,
            MacPherson,C.R., Ogawa,C., Radovanovic,A., Schwartz,A.,
            Teasdale,R.D., Tegner,J., Lenhard,B., Teichmann,S.A., Arakawa,T.,
            Ninomiya,N., Murakami,K., Tagami,M., Fukuda,S., Imamura,K., Kai,C.,
            Ishihara,R., Kitazume,Y., Kawai,J., Hume,D.A., Ideker,T. and
            Hayashizaki,Y.
  TITLE     An atlas of combinatorial transcriptional regulation in mouse and
            man
  JOURNAL   Cell 140 (5), 744-752 (2010)
   PUBMED   20211142
  REMARK    Erratum:[Cell. 2010 Apr 16;141(2):369. Kamburov, Atanas [added];
            Kaur, Mandeep [added]; MacPherson, Cameron Ross [added];
            Radovanovic, Aleksandar [added]; Schwartz, Ariel [added]]
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Sumoy,L., Carim,L., Escarceller,M., Nadal,M., Gratacos,M.,
            Pujana,M.A., Estivill,X. and Peral,B.
  TITLE     HMG20A and HMG20B map to human chromosomes 15q24 and 19p13.3 and
            constitute a distinct class of HMG-box genes with ubiquitous
            expression
  JOURNAL   Cytogenet Cell Genet 88 (1-2), 62-67 (2000)
   PUBMED   10773667
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK001601.1, AK096546.1 and AA233289.1.
            
            On Jan 30, 2015 this sequence version replaced XP_005254180.1.
            
            Transcript Variant: This variant (2) lacks an exon in the 5' UTR
            compared to variant 1. Variants 1 and 2 encode the same isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001601.1, SRR1660807.132029.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336216.9/ ENSP00000336856.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.3"
     Protein         1..347
                     /product="high mobility group protein 20A isoform a"
                     /note="HMG box domain containing 1; high mobility group
                     protein 20A; HMG box-containing protein 20A; HMG
                     domain-containing protein 1; HMG domain-containing protein
                     HMGX1"
                     /calculated_mol_wt=40013
     Region          1..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP66.1)"
     Region          <59..313
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          83..186
                     /region_name="HMG-box_HMG20A"
                     /note="high mobility group (HMG)-box found in high
                     mobility group protein 20A (HMG20A) and similar proteins;
                     cd22017"
                     /db_xref="CDD:438833"
     Site            order(104..105,107..111,114..115,122,134..135,138,
                     141..142,149,153,156,160,163)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438833"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NP66.1)"
     Region          179..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP66.1)"
     CDS             1..347
                     /gene="HMG20A"
                     /gene_synonym="HMGX1; HMGXB1"
                     /coded_by="NM_001304504.2:122..1165"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10295.1"
                     /db_xref="GeneID:10363"
                     /db_xref="HGNC:HGNC:5001"
                     /db_xref="MIM:605534"
ORIGIN      
        1 menlmtsstl pplfadedgs kesndlattg lnhpevpyss gatsstnnpe fvedlsqgql
       61 lqsessnaae gneqrhedeq rskrggwskg rkrkkplrds napkspltgy vrfmnerreq
      121 lrakrpevpf peitrmlgne wsklppeekq ryldeadrdk erymkeleqy qkteaykvfs
      181 rktqdrqkgk shrqdaarqa thdheketev kersvfdipi fteeflnhsk areaelrqlr
      241 ksnmefeern aalqkhvesm rtaveklevd viqersrntv lqqhletlrq vltssfasmp
      301 lpgsgetptv dtidsymnrl hsiilanpqd nenfiatvre vvnrldr
//
LOCUS       NP_055302                320 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 330 isoform 1 [Homo sapiens].
ACCESSION   NP_055302
VERSION     NP_055302.1
DBSOURCE    REFSEQ: accession NM_014487.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Sanchez-Brinas,A., Duran-Ruiz,C., Astola,A., Arroyo,M.M.,
            Raposo,F.G., Valle,A. and Bolivar,J.
  TITLE     ZNF330/NOA36 interacts with HSPA1 and HSPA8 and modulates cell
            cycle and proliferation in response to heat shock in HEK293 cells
  JOURNAL   Biol Direct 18 (1), 26 (2023)
   PUBMED   37254218
  REMARK    GeneRIF: ZNF330/NOA36 interacts with HSPA1 and HSPA8 and modulates
            cell cycle and proliferation in response to heat shock in HEK293
            cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 320)
  AUTHORS   de Melo,I.S., Jimenez-Nunez,M.D., Iglesias,C., Campos-Caro,A.,
            Moreno-Sanchez,D., Ruiz,F.A. and Bolivar,J.
  TITLE     NOA36 protein contains a highly conserved nucleolar localization
            signal capable of directing functional proteins to the nucleolus,
            in mammalian cells
  JOURNAL   PLoS One 8 (3), e59065 (2013)
   PUBMED   23516598
  REMARK    GeneRIF: NOA36 protein contains a highly conserved nucleolar
            localization signal capable of directing functional proteins to the
            nucleolus, in mammalian cells.
REFERENCE   6  (residues 1 to 320)
  AUTHORS   de Melo,I.S., Iglesias,C., Benitez-Rondan,A., Medina,F.,
            Martinez-Barbera,J.P. and Bolivar,J.
  TITLE     NOA36/ZNF330 is a conserved cystein-rich protein with proapoptotic
            activity in human cells
  JOURNAL   Biochim Biophys Acta 1793 (12), 1876-1885 (2009)
   PUBMED   19895853
  REMARK    GeneRIF: NOA36/ZNF330 is translocated from the mitochondria to the
            cytoplasm when apoptosis is induced and that it contributes to
            cytochrome c release.
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Bolivar,J., Garcia-Cozar,F.J., Astola,A., Iglesias,C., Pendon,C.
            and Valdivia,M.M.
  TITLE     Genomic structure and chromosome location of the human gene
            encoding the zinc finger autoantigen ZNF330
  JOURNAL   Cytogenet Cell Genet 93 (3-4), 234-238 (2001)
   PUBMED   11528117
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Bolivar,J., Diaz,I., Iglesias,C. and Valdivia,M.M.
  TITLE     Molecular cloning of a zinc finger autoantigen transiently
            associated with interphase nucleolus and mitotic centromeres and
            midbodies. Orthologous proteins with nine CXXC motifs highly
            conserved from nematodes to humans
  JOURNAL   J Biol Chem 274 (51), 36456-36464 (1999)
   PUBMED   10593942
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU532661.1, AK223609.1, BC004421.1, AK002106.1 and AJ006591.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.87237.1,
                                           SRR3476690.971316.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262990.9/ ENSP00000262990.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.21"
     Protein         1..320
                     /product="zinc finger protein 330 isoform 1"
                     /note="nucleolar cysteine-rich protein; zinc finger
                     autoantigen 330; nucleolar autoantigen 36"
                     /calculated_mol_wt=36070
     Region          1..268
                     /region_name="NOA36"
                     /note="NOA36 protein; pfam06524"
                     /db_xref="CDD:368953"
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3S2.1)"
     Region          3..11
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3S2.1)"
     Region          206..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3S2.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3S2.1)"
     CDS             1..320
                     /gene="ZNF330"
                     /gene_synonym="HSA6591; NOA36"
                     /coded_by="NM_014487.6:221..1183"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3754.1"
                     /db_xref="GeneID:27309"
                     /db_xref="HGNC:HGNC:15462"
                     /db_xref="MIM:609550"
ORIGIN      
        1 mpkkktgark kaenrrerek qlrasrstid lakhpcnasm ecdkcqrrqk nrafcyfcns
       61 vqklpicaqc gktkcmmkss dcvikhagvy stglamvgai cdfceawvch grkclsthac
      121 acpltdaecv ecergvwdhg grifscsfch nflceddqfe hqascqvlea etfkcvscnr
      181 lgqhsclrck acfcddhtrs kvfkqekgkq ppcpkcghet qetkdlsmst rslkfgrqtg
      241 geegdgasgy daywknlssd kygdtsyhde eedeyeaedd eeeedegrkd sdtessdlft
      301 nlnlgrtyas gyahyeeqen
//
LOCUS       NP_001605                375 aa            linear   PRI 27-APR-2025
DEFINITION  actin, cytoplasmic 2 [Homo sapiens].
ACCESSION   NP_001605
VERSION     NP_001605.1
DBSOURCE    REFSEQ: accession NM_001614.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Greve,J.N., Marquardt,A., Heiringhoff,R., Reindl,T., Thiel,C., Di
            Donato,N., Taft,M.H. and Manstein,D.J.
  TITLE     The non-muscle actinopathy-associated mutation E334Q in
            cytoskeletal gamma-actin perturbs interaction of actin filaments
            with myosin and ADF/cofilin family proteins
  JOURNAL   Elife 12, 93013 (2024)
   PUBMED   38446501
  REMARK    GeneRIF: The non-muscle actinopathy-associated mutation E334Q in
            cytoskeletal gamma-actin perturbs interaction of actin filaments
            with myosin and ADF/cofilin family proteins.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Yao,H., Zhou,Y., Li,T., Li,Y., Li,F., Zhang,G., Fu,X., Kang,Y. and
            Wu,Q.
  TITLE     Bioinformatic identification and experiment validation revealed
            that ACTG1 is a promising prognostic signature and therapeutic
            target for sepsis
  JOURNAL   J Leukoc Biol 114 (4), 325-334 (2023)
   PUBMED   37368839
  REMARK    GeneRIF: Bioinformatic identification and experiment validation
            revealed that ACTG1 is a promising prognostic signature and
            therapeutic target for sepsis.
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Luo,J.Q., Yang,T.W., Wu,J., Lai,H.H., Zou,L.B., Chen,W.B.,
            Zhou,X.M., Lv,D.J., Cen,S.R., Long,Z.N., Mao,Y.Y., Zheng,P.X.,
            Su,X.H., Xian,Z.Y., Shu,F.P. and Mao,X.M.
  TITLE     Exosomal PGAM1 promotes prostate cancer angiogenesis and metastasis
            by interacting with ACTG1
  JOURNAL   Cell Death Dis 14 (8), 502 (2023)
   PUBMED   37542027
  REMARK    GeneRIF: Exosomal PGAM1 promotes prostate cancer angiogenesis and
            metastasis by interacting with ACTG1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Verloes,A., Drunat,S., Pilz,D. and Di Donato,N.
  TITLE     Baraitser-Winter Cerebrofrontofacial Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26583190
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Rodriguez Del Castillo,A., Vitale,M.L. and Trifaro,J.M.
  TITLE     Ca2+ and pH determine the interaction of chromaffin cell scinderin
            with phosphatidylserine and phosphatidylinositol 4,5,-biphosphate
            and its cellular distribution during nicotinic-receptor stimulation
            and protein kinase C activation
  JOURNAL   J Cell Biol 119 (4), 797-810 (1992)
   PUBMED   1331119
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Erba,H.P., Eddy,R., Shows,T., Kedes,L. and Gunning,P.
  TITLE     Structure, chromosome location, and expression of the human
            gamma-actin gene: differential evolution, location, and expression
            of the cytoskeletal beta- and gamma-actin genes
  JOURNAL   Mol Cell Biol 8 (4), 1775-1789 (1988)
   PUBMED   2837653
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Vandekerckhove,J., Schering,B., Barmann,M. and Aktories,K.
  TITLE     Botulinum C2 toxin ADP-ribosylates cytoplasmic beta/gamma-actin in
            arginine 177
  JOURNAL   J Biol Chem 263 (2), 696-700 (1988)
   PUBMED   3335520
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X04098.1 and BC063495.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Actins are highly conserved proteins that are involved in
            various types of cell motility and in maintenance of the
            cytoskeleton. Three main groups of actin isoforms have been
            identified in vertebrate animals: alpha, beta, and gamma. The alpha
            actins are found in muscle tissues and are a major constituent of
            the contractile apparatus. The beta and gamma actins co-exist in
            most cell types as components of the cytoskeleton and as mediators
            of internal cell motility. Actin gamma 1, encoded by this gene, is
            a cytoplasmic actin found in all cell types. Mutations in this gene
            are associated with DFNA20/26, a subtype of autosomal dominant
            non-syndromic sensorineural progressive hearing loss and also with
            Baraitser-Winter syndrome. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.90241.1,
                                           SRR3476690.105074.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000573283.7/ ENSP00000458435.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..375
                     /product="actin, cytoplasmic 2"
                     /note="cytoskeletal gamma-actin; epididymis luminal
                     protein 176"
                     /calculated_mol_wt=41662
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:36173861,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P63261.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglutamate, in Actin, cytoplasmic 2,
                     N-terminally processed, partial.
                     /evidence=ECO:0000269|PubMed:29581253,
                     ECO:0000269|PubMed:30028079, ECO:0000269|Ref.7,
                     ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P63261.1)"
     Region          6..370
                     /region_name="ASKHA_NBD_actin"
                     /note="nucleotide-binding domain (NBD) of actin and
                     similar proteins; cd10224"
                     /db_xref="CDD:466823"
     Site            73
                     /site_type="methylation"
                     /note="Tele-methylhistidine.
                     /evidence=ECO:0000269|PubMed:30626964, ECO:0000269|Ref.8;
                     propagated from UniProtKB/Swiss-Prot (P63261.1)"
     Site            84
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:23673617; propagated from
                     UniProtKB/Swiss-Prot (P63261.1)"
     CDS             1..375
                     /gene="ACTG1"
                     /gene_synonym="ACT; ACTG; DFNA20; DFNA26; HEL-176"
                     /coded_by="NM_001614.5:73..1200"
                     /db_xref="CCDS:CCDS11782.1"
                     /db_xref="GeneID:71"
                     /db_xref="HGNC:HGNC:144"
                     /db_xref="MIM:102560"
ORIGIN      
        1 meeeiaalvi dngsgmckag fagddaprav fpsivgrprh qgvmvgmgqk dsyvgdeaqs
       61 krgiltlkyp iehgivtnwd dmekiwhhtf ynelrvapee hpvllteapl npkanrekmt
      121 qimfetfntp amyvaiqavl slyasgrttg ivmdsgdgvt htvpiyegya lphailrldl
      181 agrdltdylm kiltergysf tttaereivr dikeklcyva ldfeqemata assssleksy
      241 elpdgqviti gnerfrcpea lfqpsflgme scgihettfn simkcdvdir kdlyantvls
      301 ggttmypgia drmqkeital apstmkikii apperkysvw iggsilasls tfqqmwiskq
      361 eydesgpsiv hrkcf
//
LOCUS       NP_003027                728 aa            linear   PRI 27-APR-2025
DEFINITION  ski oncogene [Homo sapiens].
ACCESSION   NP_003027
VERSION     NP_003027.1
DBSOURCE    REFSEQ: accession NM_003036.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Fusco,C., Nardella,G., Morlino,S., Micale,L., Tragni,V.,
            Agolini,E., Novelli,A., Massuras,S., Giambra,V., Pierri,C.L. and
            Castori,M.
  TITLE     Nucleotide substitutions at the p.Gly117 and p.Thr180 mutational
            hot-spots of SKI alter molecular dynamics and may affect cell cycle
  JOURNAL   J Hum Genet 69 (1), 53-58 (2024)
   PUBMED   37697026
  REMARK    GeneRIF: Nucleotide substitutions at the p.Gly117 and p.Thr180
            mutational hot-spots of SKI alter molecular dynamics and may affect
            cell cycle.
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Pelgrims,E., Lynch,S.A., Hannes,L., Hoffer,M.J.V., Melotte,C., Van
            Haeringen,A., Swillen,A. and Breckpot,J.
  TITLE     Triplications of chromosome 1p36.3, including the genes GABRD and
            SKI, are associated with a developmental disorder and a facial
            gestalt
  JOURNAL   Am J Med Genet A 191 (7), 1889-1899 (2023)
   PUBMED   37129290
  REMARK    GeneRIF: Triplications of chromosome 1p36.3, including the genes
            GABRD and SKI, are associated with a developmental disorder and a
            facial gestalt.
REFERENCE   3  (residues 1 to 728)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 728)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 728)
  AUTHORS   Pearson-White,S.
  TITLE     SnoI, a novel alternatively spliced isoform of the ski
            protooncogene homolog, sno
  JOURNAL   Nucleic Acids Res 21 (19), 4632-4638 (1993)
   PUBMED   8233802
REFERENCE   6  (residues 1 to 728)
  AUTHORS   Nagase,T., Nomura,N. and Ishii,S.
  TITLE     Complex formation between proteins encoded by the ski gene family
  JOURNAL   J Biol Chem 268 (18), 13710-13716 (1993)
   PUBMED   8514802
REFERENCE   7  (residues 1 to 728)
  AUTHORS   Greally,M.T.
  TITLE     Shprintzen-Goldberg Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301454
REFERENCE   8  (residues 1 to 728)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
REFERENCE   9  (residues 1 to 728)
  AUTHORS   Nomura,N., Sasamoto,S., Ishii,S., Date,T., Matsui,M. and
            Ishizaki,R.
  TITLE     Isolation of human cDNA clones of ski and the ski-related gene, sno
  JOURNAL   Nucleic Acids Res 17 (14), 5489-5500 (1989)
   PUBMED   2762147
REFERENCE   10 (residues 1 to 728)
  AUTHORS   Chaganti,R.S., Balazs,I., Jhanwar,S.C., Murty,V.V., Koduru,P.R.,
            Grzeschik,K.H. and Stavnezer,E.
  TITLE     The cellular homologue of the transforming gene of SKV avian
            retrovirus maps to human chromosome region 1q22----q24
  JOURNAL   Cytogenet Cell Genet 43 (3-4), 181-186 (1986)
   PUBMED   3026737
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590822.37 and X15218.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the nuclear protooncogene protein
            homolog of avian sarcoma viral (v-ski) oncogene. It functions as a
            repressor of TGF-beta signaling, and may play a role in neural tube
            development and muscle differentiation. [provided by RefSeq, Oct
            2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X15218.1, SRR14038192.3809015.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378536.5/ ENSP00000367797.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33-p36.32"
     Protein         1..728
                     /product="ski oncogene"
                     /note="ski oncoprotein; proto-oncogene c-Ski; v-ski avian
                     sarcoma viral oncogene homolog; Sloan-Kettering Institute
                     proto-oncogene"
                     /calculated_mol_wt=79874
     Region          91..192
                     /region_name="DHD_Ski"
                     /note="Dachshund-homology domain found in Ski and similar
                     proteins; cd21083"
                     /db_xref="CDD:410786"
     Region          217..311
                     /region_name="c-SKI_SMAD_bind"
                     /note="c-SKI Smad4 binding domain; pfam08782"
                     /db_xref="CDD:462602"
     Region          <318..478
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          321..357
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12755.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P12755.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P12755.1)"
     Region          452..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12755.1)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P12755.1)"
     Region          538..>709
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P12755.1)"
     CDS             1..728
                     /gene="SKI"
                     /gene_synonym="SGS; SKV"
                     /coded_by="NM_003036.4:449..2635"
                     /db_xref="CCDS:CCDS39.1"
                     /db_xref="GeneID:6497"
                     /db_xref="HGNC:HGNC:10896"
                     /db_xref="MIM:164780"
ORIGIN      
        1 meaaaggrgc fqphpglqkt leqfhlssms slggpaafsa rwaqeaykke sakeagaaav
       61 papvpaatep ppvlhlpaiq ppppvlpgpf fmpsdrster cetvlegeti scfvvggekr
      121 lclpqilnsv lrdfslqqin avcdelhiyc srctadqlei lkvmgilpfs apscglitkt
      181 daerlcnall yggaypppck kelaaslalg lelsersvrv yhecfgkckg llvpelyssp
      241 saaciqcldc rlmypphkfv vhshkalenr tchwgfdsan wrayillsqd ytgkeeqarl
      301 grclddvkek fdygnkykrr vprvsseppa sirpktddts sqspapsekd kpsswlrtla
      361 gssnkslgcv hprqrlsafr pwspavsase kelsphlpal irdsfysyks fetavapnva
      421 lappaqqkvv ssppcaaavs rapeplatct qprkrkltvd tpgapetlap vaapeedkds
      481 eaevevesre eftsslssls spsftssssa kdlgspgara lpsavpdaaa padapsglea
      541 elehlrqale ggldtkeake kflhevvkmr vkqeeklsaa lqakrslhqe leflrvakke
      601 klreateakr nlrkeierlr aenekkmkea nesrlrlkre leqarqarvc dkgceagrlr
      661 akysaqiedl qvklqhaead reqlradllr erearehlek vvkelqeqlw prarpeaags
      721 egaaelep
//
LOCUS       NP_004087                120 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 4E-binding protein 2 [Homo
            sapiens].
ACCESSION   NP_004087
VERSION     NP_004087.1
DBSOURCE    REFSEQ: accession NM_004096.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Shi,J.Y., Wen,R., Chen,J.Y., Feng,Y.Q., Zhang,Y.Y., Hou,S.J.,
            Xi,Y.J., Wang,J.F. and Zhang,Y.F.
  TITLE     Genetic evidence supporting potential causal roles of EIF4 family
            in breast cancer: a two-sample randomized Mendelian study
  JOURNAL   Sci Rep 14 (1), 20191 (2024)
   PUBMED   39215053
  REMARK    GeneRIF: Genetic evidence supporting potential causal roles of EIF4
            family in breast cancer: a two-sample randomized Mendelian study.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Levy,T., Voeltzke,K., Hruby,L., Alasad,K., Bas,Z.,
            Snaebjornsson,M., Marciano,R., Scharov,K., Planque,M., Vriens,K.,
            Christen,S., Funk,C.M., Hassiepen,C., Kahler,A., Heider,B.,
            Picard,D., Lim,J.K.M., Stefanski,A., Bendrin,K., Vargas-Toscano,A.,
            Kahlert,U.D., Stuhler,K., Remke,M., Elkabets,M., Grunewald,T.G.P.,
            Reichert,A.S., Fendt,S.M., Schulze,A., Reifenberger,G., Rotblat,B.
            and Leprivier,G.
  TITLE     mTORC1 regulates cell survival under glucose starvation through
            4EBP1/2-mediated translational reprogramming of fatty acid
            metabolism
  JOURNAL   Nat Commun 15 (1), 4083 (2024)
   PUBMED   38744825
  REMARK    GeneRIF: mTORC1 regulates cell survival under glucose starvation
            through 4EBP1/2-mediated translational reprogramming of fatty acid
            metabolism.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Zeng,J., Lu,C., Huang,X. and Li,Y.
  TITLE     The human eIF4E:4E-BP2 complex structure for studying
            hyperphosphorylation
  JOURNAL   Phys Chem Chem Phys 26 (14), 10660-10672 (2024)
   PUBMED   38511550
  REMARK    GeneRIF: The human eIF4E:4E-BP2 complex structure for studying
            hyperphosphorylation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Han,X., Yang,F., Zhang,Z., Hou,Z., Sun,Q., Su,T., Lv,W., Wang,Z.,
            Yuan,C., Zhang,G., Pi,X., Long,J. and Liu,H.
  TITLE     4EBP2-regulated protein translation has a critical role in high-fat
            diet-induced insulin resistance in hepatocytes
  JOURNAL   J Biol Chem 299 (11), 105315 (2023)
   PUBMED   37797700
  REMARK    GeneRIF: 4EBP2-regulated protein translation has a critical role in
            high-fat diet-induced insulin resistance in hepatocytes.
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Gingras,A.C. and Sonenberg,N.
  TITLE     Adenovirus infection inactivates the translational inhibitors
            4E-BP1 and 4E-BP2
  JOURNAL   Virology 237 (1), 182-186 (1997)
   PUBMED   9344920
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Lawrence,J.C. Jr., Fadden,P., Haystead,T.A. and Lin,T.A.
  TITLE     PHAS proteins as mediators of the actions of insulin, growth
            factors and cAMP on protein synthesis and cell proliferation
  JOURNAL   Adv Enzyme Regul 37, 239-267 (1997)
   PUBMED   9381973
  REMARK    Review article
REFERENCE   7  (residues 1 to 120)
  AUTHORS   Tsukiyama-Kohara,K., Vidal,S.M., Gingras,A.C., Glover,T.W.,
            Hanash,S.M., Heng,H. and Sonenberg,N.
  TITLE     Tissue distribution, genomic structure, and chromosome mapping of
            mouse and human eukaryotic initiation factor 4E-binding proteins 1
            and 2
  JOURNAL   Genomics 38 (3), 353-363 (1996)
   PUBMED   8975712
REFERENCE   8  (residues 1 to 120)
  AUTHORS   Lin,T.A. and Lawrence,J.C. Jr.
  TITLE     Control of the translational regulators PHAS-I and PHAS-II by
            insulin and cAMP in 3T3-L1 adipocytes
  JOURNAL   J Biol Chem 271 (47), 30199-30204 (1996)
   PUBMED   8939971
REFERENCE   9  (residues 1 to 120)
  AUTHORS   Mader,S., Lee,H., Pause,A. and Sonenberg,N.
  TITLE     The translation initiation factor eIF-4E binds to a common motif
            shared by the translation factor eIF-4 gamma and the translational
            repressors 4E-binding proteins
  JOURNAL   Mol Cell Biol 15 (9), 4990-4997 (1995)
   PUBMED   7651417
REFERENCE   10 (residues 1 to 120)
  AUTHORS   Pause,A., Belsham,G.J., Gingras,A.C., Donze,O., Lin,T.A.,
            Lawrence,J.C. Jr. and Sonenberg,N.
  TITLE     Insulin-dependent stimulation of protein synthesis by
            phosphorylation of a regulator of 5'-cap function
  JOURNAL   Nature 371 (6500), 762-767 (1994)
   PUBMED   7935836
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG717474.1, BC050633.1 and
            AC022532.13.
            
            Summary: This gene encodes a member of the eukaryotic translation
            initiation factor 4E binding protein family. The gene products of
            this family bind eIF4E and inhibit translation initiation. However,
            insulin and other growth factors can release this inhibition via a
            phosphorylation-dependent disruption of their binding to eIF4E.
            Regulation of protein production through these gene products have
            been implicated in cell proliferation, cell differentiation and
            viral infection. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.33657.1,
                                           SRR1803611.66710.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373218.5/ ENSP00000362314.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..120
                     /product="eukaryotic translation initiation factor
                     4E-binding protein 2"
                     /note="phosphorylated, heat and acid stable regulated by
                     insulin protein II; eIF4E-binding protein 2"
                     /calculated_mol_wt=12808
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000305|PubMed:24207126,
                     ECO:0000305|PubMed:25533957"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13542.1)"
     Region          11..120
                     /region_name="eIF_4EBP"
                     /note="Eukaryotic translation initiation factor 4E binding
                     protein (EIF4EBP); pfam05456"
                     /db_xref="CDD:461656"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MTOR.
                     /evidence=ECO:0000269|PubMed:25533957,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q13542.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MTOR.
                     /evidence=ECO:0000269|PubMed:25533957,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13542.1)"
     Region          54..60
                     /region_name="YXXXXLphi motif.
                     /evidence=ECO:0000269|PubMed:24207126,
                     ECO:0000269|PubMed:25533957"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13542.1)"
     Region          65..120
                     /region_name="Disordered.
                     /evidence=ECO:0000305|PubMed:24207126,
                     ECO:0000305|PubMed:25533957"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13542.1)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:25533957; propagated from
                     UniProtKB/Swiss-Prot (Q13542.1)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MTOR.
                     /evidence=ECO:0000269|PubMed:25533957; propagated from
                     UniProtKB/Swiss-Prot (Q13542.1)"
     Region          78..82
                     /region_name="Secondary EIF4E binding site.
                     /evidence=ECO:0000269|PubMed:24207126,
                     ECO:0000269|PubMed:25533957"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13542.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:25533957; propagated from
                     UniProtKB/Swiss-Prot (Q13542.1)"
     Region          116..120
                     /region_name="TOS motif.
                     /evidence=ECO:0000250|UniProtKB:Q13541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13542.1)"
     CDS             1..120
                     /gene="EIF4EBP2"
                     /gene_synonym="4EBP2; PHASII"
                     /coded_by="NM_004096.5:258..620"
                     /db_xref="CCDS:CCDS7303.1"
                     /db_xref="GeneID:1979"
                     /db_xref="HGNC:HGNC:3289"
                     /db_xref="MIM:602224"
ORIGIN      
        1 msssagsghq psqsraiptr tvaisdaaql phdycttpgg tlfsttpggt riiydrkfll
       61 drrnspmaqt ppchlpnipg vtspgtlied skvevnnlnn lnnhdrkhav gddaqfemdi
//
LOCUS       NP_061857               1049 aa            linear   PRI 27-APR-2025
DEFINITION  protein phosphatase Slingshot homolog 1 isoform 1 [Homo sapiens].
ACCESSION   NP_061857
VERSION     NP_061857.3
DBSOURCE    REFSEQ: accession NM_018984.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Lai,S.W., Cheng,Y.C., Huang,W.C., Yadav,V.K., Fong,I.H., Yeh,C.T.,
            Yang,C.K., Lee,W.H. and Chen,M.Y.
  TITLE     Dysregulated expression of slingshot protein phosphatase 1 (SSH1)
            disrupts circadian rhythm and WNT signaling associated to
            hepatocellular carcinoma pathogenesis
  JOURNAL   Aging (Albany NY) 15 (20), 11033-11051 (2023)
   PUBMED   37837551
  REMARK    GeneRIF: Dysregulated expression of slingshot protein phosphatase 1
            (SSH1) disrupts circadian rhythm and WNT signaling associated to
            hepatocellular carcinoma pathogenesis.
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cazzaro,S., Woo,J.A., Wang,X., Liu,T., Rego,S., Kee,T.R., Koh,Y.,
            Vazquez-Rosa,E., Pieper,A.A. and Kang,D.E.
  TITLE     Slingshot homolog-1-mediated Nrf2 sequestration tips the balance
            from neuroprotection to neurodegeneration in Alzheimer's disease
  JOURNAL   Proc Natl Acad Sci U S A 120 (30), e2217128120 (2023)
   PUBMED   37463212
  REMARK    GeneRIF: Slingshot homolog-1-mediated Nrf2 sequestration tips the
            balance from neuroprotection to neurodegeneration in Alzheimer's
            disease.
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Chen,F., Aye,L., Yu,L., Liu,L., Liu,Y., Lin,Y., Gao,D., Gao,Q. and
            Zhang,S.
  TITLE     SSH1 promotes progression of intrahepatic cholangiocarcinoma via
            p38 MAPK-CXCL8 axis
  JOURNAL   Carcinogenesis 44 (3), 232-241 (2023)
   PUBMED   36857607
  REMARK    GeneRIF: SSH1 promotes progression of intrahepatic
            cholangiocarcinoma via p38 MAPK-CXCL8 axis.
REFERENCE   4  (residues 1 to 1049)
  AUTHORS   Cazzaro,S., Zhao,X., Zhao,V.K., Kim,Y.K. and Woo,J.A.
  TITLE     Slingshot homolog-1 amplifies mitochondrial abnormalities by
            distinctly impairing health and clearance of mitochondria
  JOURNAL   Hum Mol Genet 32 (10), 1660-1672 (2023)
   PUBMED   36637427
  REMARK    GeneRIF: Slingshot homolog-1 amplifies mitochondrial abnormalities
            by distinctly impairing health and clearance of mitochondria.
REFERENCE   5  (residues 1 to 1049)
  AUTHORS   Song,X., Xie,D., Xia,X., Tan,F., Pei,Q., Li,Y., Zhou,Z., Zhou,Y.,
            Li,C., Wang,K. and Pei,H.
  TITLE     Role of SSH1 in colorectal cancer prognosis and tumor progression
  JOURNAL   J Gastroenterol Hepatol 35 (7), 1180-1188 (2020)
   PUBMED   32020663
  REMARK    GeneRIF: Role of SSH1 in colorectal cancer prognosis and tumor
            progression.
REFERENCE   6  (residues 1 to 1049)
  AUTHORS   Nishita,M., Wang,Y., Tomizawa,C., Suzuki,A., Niwa,R., Uemura,T. and
            Mizuno,K.
  TITLE     Phosphoinositide 3-kinase-mediated activation of cofilin
            phosphatase Slingshot and its role for insulin-induced membrane
            protrusion
  JOURNAL   J Biol Chem 279 (8), 7193-7198 (2004)
   PUBMED   14645219
  REMARK    GeneRIF: findings suggest that SSH1L is activated downstream of
            PI3K and plays a critical role in insulin-induced membrane
            protrusion by dephosphorylating and activating cofilin
REFERENCE   7  (residues 1 to 1049)
  AUTHORS   Ohta,Y., Kousaka,K., Nagata-Ohashi,K., Ohashi,K., Muramoto,A.,
            Shima,Y., Niwa,R., Uemura,T. and Mizuno,K.
  TITLE     Differential activities, subcellular distribution and tissue
            expression patterns of three members of Slingshot family
            phosphatases that dephosphorylate cofilin
  JOURNAL   Genes Cells 8 (10), 811-824 (2003)
   PUBMED   14531860
REFERENCE   8  (residues 1 to 1049)
  AUTHORS   Kaji,N., Ohashi,K., Shuin,M., Niwa,R., Uemura,T. and Mizuno,K.
  TITLE     Cell cycle-associated changes in Slingshot phosphatase activity and
            roles in cytokinesis in animal cells
  JOURNAL   J Biol Chem 278 (35), 33450-33455 (2003)
   PUBMED   12807904
  REMARK    GeneRIF: SSH1 plays a critical role in cytokinesis by
            dephosphorylating and reactivating cofilin in later stages of
            mitosis
REFERENCE   9  (residues 1 to 1049)
  AUTHORS   Endo,M., Ohashi,K., Sasaki,Y., Goshima,Y., Niwa,R., Uemura,T. and
            Mizuno,K.
  TITLE     Control of growth cone motility and morphology by LIM kinase and
            Slingshot via phosphorylation and dephosphorylation of cofilin
  JOURNAL   J Neurosci 23 (7), 2527-2537 (2003)
   PUBMED   12684437
REFERENCE   10 (residues 1 to 1049)
  AUTHORS   Niwa,R., Nagata-Ohashi,K., Takeichi,M., Mizuno,K. and Uemura,T.
  TITLE     Control of actin reorganization by Slingshot, a family of
            phosphatases that dephosphorylate ADF/cofilin
  JOURNAL   Cell 108 (2), 233-246 (2002)
   PUBMED   11832213
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP363810.1, AB072355.1,
            AC087893.15, BC020243.1 and AI621348.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 6, 2009 this sequence version replaced NP_061857.2.
            
            Summary: The protein encoded by this gene belongs to the slingshot
            homolog (SSH) family of phosphatases, which regulate actin filament
            dynamics. The SSH proteins dephosphorylate and activate the actin
            binding/depolymerizing factor cofilin, which subsequently binds to
            actin filaments and stimulates their disassembly. Cofilin is
            inactivated by kinases such as LIM domain kinase-1 (LIMK1), which
            may also be dephosphorylated and inactivated by SSH proteins. The
            SSH family thus appears to play a role in actin dynamics by
            reactivating cofilin proteins. Alternatively spliced transcript
            variants encoding different isoforms have been described for this
            gene. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1, also known as
            SSH-1L). This isoform has been shown to be enzymatically active
            (PMID:11832213).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062341.1, AB072355.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326495.10/ ENSP00000315713.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..1049
                     /product="protein phosphatase Slingshot homolog 1 isoform
                     1"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="protein phosphatase Slingshot homolog 1; hSSH-1L;
                     SSH-like protein 1; slingshot homolog 1"
                     /calculated_mol_wt=115380
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Region          3..237
                     /region_name="SSH-N"
                     /note="N-terminal domain conserved in slingshot (SSH)
                     phosphatases; cd11652"
                     /db_xref="CDD:212166"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Region          251..303
                     /region_name="DEK_C"
                     /note="DEK C terminal domain; pfam08766"
                     /db_xref="CDD:462592"
     Region          306..449
                     /region_name="DSP_slingshot_1"
                     /note="dual specificity phosphatase domain of slingshot
                     homolog 1; cd14570"
                     /db_xref="CDD:350418"
     Region          456..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q76I79; propagated from
                     UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Region          544..603
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Region          <655..1044
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          693..787
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Region          825..899
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Region          897..1049
                     /region_name="Interaction with YWHAG.
                     /evidence=ECO:0000269|PubMed:15159416"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Site            897
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Region          923..955
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Site            978
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15159416; propagated from
                     UniProtKB/Swiss-Prot (Q8WYL5.2)"
     Region          989..1049
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYL5.2)"
     CDS             1..1049
                     /gene="SSH1"
                     /gene_synonym="SSH1L"
                     /coded_by="NM_018984.4:88..3237"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9121.1"
                     /db_xref="GeneID:54434"
                     /db_xref="HGNC:HGNC:30579"
                     /db_xref="MIM:606778"
ORIGIN      
        1 malvtlqrsp tpsaasssas nseleagsee drklnlslse sffmvkgaal flqqgsspqg
       61 qrslqhphkh agdlpqhlqv minllrcedr iklavrlesa wadrvrymvv vyssgrqdte
      121 enillgvdfs skesksctig mvlrlwsdtk ihldgdggfs vstagrmhif kpvsvqamws
      181 alqvlhkace varrhnyfpg gvaliwatyy escisseqsc inewnamqdl estrpdspal
      241 fvdkpteger terlikaklr simmsqdlen vtskeirnel ekqmncnlke lkefidneml
      301 lilgqmdkps lifdhlylgs ewnasnleel qgsgvdyiln vtreidnffp glfayhnirv
      361 ydeettdlla hwneayhfin kakrnhskcl vhckmgvsrs astviayamk efgwplekay
      421 nyvkqkrsit rpnagfmrql seyegildas kqrhnklwrq qtdsslqqpv ddpagpgdfl
      481 petpdgtpes qlpflddaaq pglgpplpcc frrlsdpllp spedetgslv hledpereal
      541 leeaappaev hrparqpqqg sglcekdvkk klefgspkgr sgsllqveet ereeglgagr
      601 wgqlptqldq nllnsenlnn nskrscpngm eddaifgiln kvkpsyksca dcmyptasga
      661 peasrerced pnapaictqp aflphitssp vahlasrsrv pekpasgpte pppflppags
      721 rradtsgpga gaaleppasl lepsretpkv lpkslllkns hcdknppste vvikeesspk
      781 kdmkpakdlr llfsnesekp ttnsylmqhq esiiqlqkag lvrkhtkele rlksvpadpa
      841 ppsrdgpasr leasipeesq dpaalhelgp lvmpsqagsd ekseaapasl eggslksppp
      901 ffyrldhtss fskdflktic ytptsssmss nltrssssds ihsvrgkpgl vkqrtqeiet
      961 rlrlagltvs splkrshsla klgsltfste dlsseadpst vadsqdttls essflhepqg
     1021 tprdpaatsk psgkpapenl kspswmsks
//
LOCUS       NP_067072                290 aa            linear   PRI 27-APR-2025
DEFINITION  sorting nexin-6 isoform a [Homo sapiens].
ACCESSION   NP_067072
VERSION     NP_067072.3
DBSOURCE    REFSEQ: accession NM_021249.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Ghosh,C., Xing,Y., Li,S., Hoyle,R.G., Sun,M., Li,J. and Sun,Y.
  TITLE     Sorting nexin 6 interacts with Cullin3 and regulates programmed
            death ligand 1 expression
  JOURNAL   FEBS Lett 595 (20), 2558-2569 (2021)
   PUBMED   34510437
  REMARK    GeneRIF: Sorting nexin 6 interacts with Cullin3 and regulates
            programmed death ligand 1 expression.
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Camargo,L.M., Collura,V., Rain,J.C., Mizuguchi,K., Hermjakob,H.,
            Kerrien,S., Bonnert,T.P., Whiting,P.J. and Brandon,N.J.
  TITLE     Disrupted in Schizophrenia 1 Interactome: evidence for the close
            connectivity of risk genes and a potential synaptic basis for
            schizophrenia
  JOURNAL   Mol Psychiatry 12 (1), 74-86 (2007)
   PUBMED   17043677
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Ishibashi,Y., Maita,H., Yano,M., Koike,N., Tamai,K., Ariga,H. and
            Iguchi-Ariga,S.M.
  TITLE     Pim-1 translocates sorting nexin 6/TRAF4-associated factor 2 from
            cytoplasm to nucleus
  JOURNAL   FEBS Lett 506 (1), 33-38 (2001)
   PUBMED   11591366
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Parks,W.T., Frank,D.B., Huff,C., Renfrew Haft,C., Martin,J.,
            Meng,X., de Caestecker,M.P., McNally,J.G., Reddi,A., Taylor,S.I.,
            Roberts,A.B., Wang,T. and Lechleider,R.J.
  TITLE     Sorting nexin 6, a novel SNX, interacts with the transforming
            growth factor-beta family of receptor serine-threonine kinases
  JOURNAL   J Biol Chem 276 (22), 19332-19339 (2001)
   PUBMED   11279102
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Wurthner,J.U., Frank,D.B., Felici,A., Green,H.M., Cao,Z.,
            Schneider,M.D., McNally,J.G., Lechleider,R.J. and Roberts,A.B.
  TITLE     Transforming growth factor-beta receptor-associated protein 1 is a
            Smad4 chaperone
  JOURNAL   J Biol Chem 276 (22), 19495-19502 (2001)
   PUBMED   11278302
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB021488.1, AL445883.3,
            BC001798.1, BI870378.1, AF121856.2, AK124315.1 and AI446034.1.
            
            On Feb 23, 2006 this sequence version replaced NP_067072.2.
            
            Summary: This gene encodes a member of the sorting nexin family.
            Members of this family contain a phox (PX) domain, which is a
            phosphoinositide binding domain, and are involved in intracellular
            trafficking. This protein associates with the long isoform of the
            leptin receptor, the transforming growth factor-beta family of
            receptor serine-threonine kinases, and with receptor tyrosine
            kinases for platelet-derived growth factor, insulin, and epidermal
            growth factor. This protein may form oligomeric complexes with
            family member proteins through interactions of both the PX domain
            and the coiled coil regions of the molecules. Translocation of this
            protein from the cytoplasm to the nucleus occurs after binding to
            proviral integration site 1 protein. This gene results in two
            transcripts encoding two distinct isoforms. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) retains an intron in the 5'
            UTR and represents the longest transcript. The resulting isoform
            (a) has a shorter N-terminus compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.110079.1,
                                           SRR1660805.54258.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..290
                     /product="sorting nexin-6 isoform a"
                     /note="tumor necrosis factor receptor-associated factor
                     4(TRAF4)-associated factor 2; TRAF4-associated factor 2"
                     /calculated_mol_wt=33439
     Region          <1..54
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Region          70..287
                     /region_name="BAR"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain, a
                     dimerization module that binds membranes and detects
                     membrane curvature; cl12013"
                     /db_xref="CDD:472257"
     Site            order(100,103..104,108,110..111,114..115,117..118,
                     128..129,131..132,135..136,138..139,142,154,157..158,247,
                     250..251,253,258,261..262,264..265,268..269,272..273,
                     275..276,279..280,282..283)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153271"
     CDS             1..290
                     /gene="SNX6"
                     /gene_synonym="MSTP010; TFAF2"
                     /coded_by="NM_021249.5:537..1409"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9648.1"
                     /db_xref="GeneID:58533"
                     /db_xref="HGNC:HGNC:14970"
                     /db_xref="MIM:606098"
ORIGIN      
        1 mtkeeftkmk qeleaeylai fkktvamhev flcrvaahpi lrrdlnfhvf leynqdlsvr
       61 gknkkekled ffknmvksad gvivsgvkdv ddffehertf lleyhnrvkd asaksdrmtr
      121 shksaaddyn rigsslyalg tqdstdickf flkvselfdk trkiearvsa dedlklsdll
      181 kyylresqaa kdllyrrsrs lvdyenanka ldkaraknkd vlqaetsqql ccqkfekise
      241 sakqelidfk trrvaafrkn lvelaelelk hakgnlqllq nclavlngdt
//
LOCUS       NP_001354355             547 aa            linear   PRI 27-APR-2025
DEFINITION  rho GTPase-activating protein 9 isoform 3 [Homo sapiens].
ACCESSION   NP_001354355 XP_016875290
VERSION     NP_001354355.1
DBSOURCE    REFSEQ: accession NM_001367426.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Sun,J., Zhao,X., Jiang,H., Yang,T., Li,D., Yang,X., Jia,A., Ma,Y.
            and Qian,Z.
  TITLE     ARHGAP9 inhibits colorectal cancer cell proliferation, invasion and
            EMT via targeting PI3K/AKT/mTOR signaling pathway
  JOURNAL   Tissue Cell 77, 101817 (2022)
   PUBMED   35679685
  REMARK    GeneRIF: ARHGAP9 inhibits colorectal cancer cell proliferation,
            invasion and EMT via targeting PI3K/AKT/mTOR signaling pathway.
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Ji,W., Zhang,L. and Zhu,H.
  TITLE     GATA binding protein 5 (GATA5) induces Rho GTPase activating
            protein 9 (ARHGAP9) to inhibit the malignant process of lung
            adenocarcinoma cells
  JOURNAL   Bioengineered 13 (2), 2878-2888 (2022)
   PUBMED   35040754
  REMARK    GeneRIF: GATA binding protein 5 (GATA5) induces Rho GTPase
            activating protein 9 (ARHGAP9) to inhibit the malignant process of
            lung adenocarcinoma cells.
REFERENCE   3  (residues 1 to 547)
  AUTHORS   He,X., Zou,H. and Wang,F.
  TITLE     SOX4-induced upregulation of ARHGAP9 promotes the progression of
            acute myeloid leukemia
  JOURNAL   Drug Dev Res 82 (8), 1227-1234 (2021)
   PUBMED   34159626
  REMARK    GeneRIF: SOX4-induced upregulation of ARHGAP9 promotes the
            progression of acute myeloid leukemia.
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Han,C., He,S., Wang,R., Gao,X., Wang,H., Qiao,J., Meng,X., Li,Y.
            and Yu,L.
  TITLE     The role of ARHGAP9: clinical implication and potential function in
            acute myeloid leukemia
  JOURNAL   J Transl Med 19 (1), 65 (2021)
   PUBMED   33579308
  REMARK    GeneRIF: The role of ARHGAP9: clinical implication and potential
            function in acute myeloid leukemia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 547)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 547)
  AUTHORS   Voss,M., Lettau,M. and Janssen,O.
  TITLE     Identification of SH3 domain interaction partners of human FasL
            (CD178) by phage display screening
  JOURNAL   BMC Immunol 10, 53 (2009)
   PUBMED   19807924
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 547)
  AUTHORS   Ceccarelli,D.F., Blasutig,I.M., Goudreault,M., Li,Z., Ruston,J.,
            Pawson,T. and Sicheri,F.
  TITLE     Non-canonical interaction of phosphoinositides with pleckstrin
            homology domains of Tiam1 and ArhGAP9
  JOURNAL   J Biol Chem 282 (18), 13864-13874 (2007)
   PUBMED   17339315
REFERENCE   8  (residues 1 to 547)
  AUTHORS   Ang,B.K., Lim,C.Y., Koh,S.S., Sivakumar,N., Taib,S., Lim,K.B.,
            Ahmed,S., Rajagopal,G. and Ong,S.H.
  TITLE     ArhGAP9, a novel MAP kinase docking protein, inhibits Erk and p38
            activation through WW domain binding
  JOURNAL   J Mol Signal 2, 1 (2007)
   PUBMED   17284314
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 547)
  AUTHORS   Peck,J., Douglas,G. 4th, Wu,C.H. and Burbelo,P.D.
  TITLE     Human RhoGAP domain-containing proteins: structure, function and
            evolutionary relationships
  JOURNAL   FEBS Lett 528 (1-3), 27-34 (2002)
   PUBMED   12297274
  REMARK    Review article
REFERENCE   10 (residues 1 to 547)
  AUTHORS   Furukawa,Y., Kawasoe,T., Daigo,Y., Nishiwaki,T., Ishiguro,H.,
            Takahashi,M., Kitayama,J. and Nakamura,Y.
  TITLE     Isolation of a novel human gene, ARHGAP9, encoding a rho-GTPase
            activating protein
  JOURNAL   Biochem Biophys Res Commun 284 (3), 643-649 (2001)
   PUBMED   11396949
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022506.38.
            
            On Nov 28, 2018 this sequence version replaced XP_016875290.1.
            
            Summary: This gene encodes a member of the Rho-GAP family of GTPase
            activating proteins. The protein has substantial GAP activity
            towards several Rho-family GTPases in vitro, converting them to an
            inactive GDP-bound state. It is implicated in regulating adhesion
            of hematopoietic cells to the extracellular matrix. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (11), as well as variant 3,
            encodes isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.336944.1,
                                           SRR14038192.1524146.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..547
                     /product="rho GTPase-activating protein 9 isoform 3"
                     /note="rho-type GTPase-activating protein 9"
                     /calculated_mol_wt=61052
     Region          140..252
                     /region_name="PH_ARHGAP9-like"
                     /note="Beta-spectrin pleckstrin homology (PH) domain;
                     cd13233"
                     /db_xref="CDD:270053"
     Site            order(148,159..161,212..214)
                     /site_type="other"
                     /note="non-cannonial phosphoinositide binding site
                     [chemical binding]"
                     /db_xref="CDD:270053"
     Region          337..541
                     /region_name="RhoGAP_ARHGAP27_15_12_9"
                     /note="GTPase-activator protein (GAP) domain for Rho-like
                     GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15,
                     12 and 9-like proteins; This subgroup of ARHGAPs are
                     multidomain proteins that contain RhoGAP, PH, SH3 and WW
                     domains. Most members that are...; cd04403"
                     /db_xref="CDD:239868"
     Site            order(375,432,436,505,508..509,532)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239868"
     Site            375
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239868"
     CDS             1..547
                     /gene="ARHGAP9"
                     /gene_synonym="10C; RGL1"
                     /coded_by="NM_001367426.1:98..1741"
                     /note="isoform 3 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS44928.1"
                     /db_xref="GeneID:64333"
                     /db_xref="HGNC:HGNC:14130"
                     /db_xref="MIM:610576"
ORIGIN      
        1 mseppvycnl vdlrrcprsp ppgpacpllq rldaweqhld pnsgrcfyin sltgckswkp
       61 prrsrsetnp gsmegtqtlk rnndvlqpqa kgfrsdtgtp epldpqgsls lsqrtsqldp
      121 palqaprplp qllddpheve ksgllnmtki aqggrklrkn wgpswvvltg nslvfyrepp
      181 ptapssgwgp agsrpessvd lrgaalahgr hlssrrnvlh irtipghefl lqsdhetelr
      241 awhralrtvi erldrenple lrlsgsgpae lsagedeeee selvskpllr lssrrssirg
      301 pegteqnrvr nklkrliakr pplqslqerg llrdqvfgcq leslcqregd tvpsflrlci
      361 aavdkrgldv dgiyrvsgnl avvqklrflv dreravtsdg ryvfpeqpgq egrldldste
      421 wddihvvtga lklflrelpq plvpplllph fraalalses eqclsqiqel igsmpkpnhd
      481 tlryllehlc rviahsdknr mtphnlgivf gptlfrpeqe tsdpaahaly pgqlvqlmlt
      541 nftslfp
//
LOCUS       NP_569734                130 aa            linear   PRI 27-APR-2025
DEFINITION  P antigen family member 5 isoform 1 [Homo sapiens].
ACCESSION   NP_569734
VERSION     NP_569734.2
DBSOURCE    REFSEQ: accession NM_130467.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Nylund,C., Rappu,P., Pakula,E., Heino,A., Laato,L., Elo,L.L.,
            Vihinen,P., Pyrhonen,S., Owen,G.R., Larjava,H., Kallajoki,M. and
            Heino,J.
  TITLE     Melanoma-associated cancer-testis antigen 16 (CT16) regulates the
            expression of apoptotic and antiapoptotic genes and promotes cell
            survival
  JOURNAL   PLoS One 7 (9), e45382 (2012)
   PUBMED   23028975
  REMARK    GeneRIF: Results indicate that CT16 promotes the survival of
            melanoma cells and is therefore a potential target for future drug
            development.
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Rappu,P., Nylund,C., Ristiniemi,N., Kulpakko,J., Vihinen,P.,
            Hernberg,M., Mirtti,T., Alanen,K., Kallajoki,M., Vuoristo,M.S.,
            Pyrhonen,S. and Heino,J.
  TITLE     Detection of melanoma-derived cancer-testis antigen CT16 in patient
            sera by a novel immunoassay
  JOURNAL   Int J Cancer 128 (10), 2382-2392 (2011)
   PUBMED   20658534
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Hellman,M., Tossavainen,H., Rappu,P., Heino,J. and Permi,P.
  TITLE     Characterization of intrinsically disordered prostate associated
            gene (PAGE5) at single residue resolution by NMR spectroscopy
  JOURNAL   PLoS One 6 (11), e26633 (2011)
   PUBMED   22073178
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Takagaki,K., Katsuma,S., Horio,T., Kaminishi,Y., Hada,Y.,
            Tanaka,T., Ohgi,T. and Yano,J.
  TITLE     cDNA microarray analysis of altered gene expression in
            Ara-C-treated leukemia cells
  JOURNAL   Biochem Biophys Res Commun 309 (2), 351-358 (2003)
   PUBMED   12951057
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Zendman,A.J., Van Kraats,A.A., Weidle,U.H., Ruiter,D.J. and Van
            Muijen,G.N.
  TITLE     The XAGE family of cancer/testis-associated genes: alignment and
            expression profile in normal tissues, melanoma lesions and Ewing's
            sarcoma
  JOURNAL   Int J Cancer 99 (3), 361-369 (2002)
   PUBMED   11992404
REFERENCE   8  (residues 1 to 130)
  AUTHORS   Scanlan,M.J., Gordon,C.M., Williamson,B., Lee,S.Y., Chen,Y.T.,
            Stockert,E., Jungbluth,A., Ritter,G., Jager,D., Jager,E., Knuth,A.
            and Old,L.J.
  TITLE     Identification of cancer/testis genes by database mining and mRNA
            expression analysis
  JOURNAL   Int J Cancer 98 (4), 485-492 (2002)
   PUBMED   11920606
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158819.14, BP429046.1,
            BC009230.2 and BQ437151.1.
            
            On Mar 26, 2002 this sequence version replaced NP_569734.1.
            
            Summary: This gene is a member of family of proteins that are
            expressed in a variety of tumors and in some fetal and reproductive
            tissues. The encoded protein may protect cells from programmed cell
            death. Multiple alternatively spliced transcript variants encoding
            distinct isoforms have been found. [provided by RefSeq, Jan 2015].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG477487.1, BC009230.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.21"
     Protein         1..130
                     /product="P antigen family member 5 isoform 1"
                     /note="cancer/testis antigen family 16, member 1;
                     cancer/testis antigen family 16, member 2; P antigen
                     family, member 5 (prostate associated); g antigen family E
                     member 1; cancer/testis antigen 16.1; prostate-associated
                     gene 5 protein; P antigen family member 5"
                     /calculated_mol_wt=13915
     Region          1..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GU1.2)"
     Region          21..126
                     /region_name="GAGE"
                     /note="GAGE protein; pfam05831"
                     /db_xref="CDD:461753"
     Region          101..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GU1.2)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96GU1.2)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96GU1.2)"
     CDS             1..130
                     /gene="PAGE5"
                     /gene_synonym="CT16; CT16.1; CT16.2; GAGEE1; PAGE-5"
                     /coded_by="NM_130467.5:255..647"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14368.1"
                     /db_xref="GeneID:90737"
                     /db_xref="HGNC:HGNC:29992"
                     /db_xref="MIM:301009"
ORIGIN      
        1 mqapwagnrg wagtreevrd msehvtrsqs sergndqess qpvgpvivqq pteekrqeee
       61 pptdnqgiap sgeiknegap avqgtdveaf qqelallkie dapgdgpdvr egtlptfdpt
      121 kvleagegql
//
LOCUS       NP_001034553            1323 aa            linear   PRI 27-APR-2025
DEFINITION  maestro heat-like repeat-containing protein family member 7 isoform
            1 [Homo sapiens].
ACCESSION   NP_001034553
VERSION     NP_001034553.3
DBSOURCE    REFSEQ: accession NM_001039464.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1323)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590093.10 and AL139244.21.
            
            On Nov 22, 2018 this sequence version replaced NP_001034553.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302446.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000421030.7/ ENSP00000396622.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..1323
                     /product="maestro heat-like repeat-containing protein
                     family member 7 isoform 1"
                     /note="HEAT repeat-containing protein 8; maestro heat-like
                     repeat-containing protein family member 7"
                     /calculated_mol_wt=145517
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Region          <5..135
                     /region_name="KLF17_N"
                     /note="N-terminal domain of Kruppel-like factor 17;
                     cd21574"
                     /db_xref="CDD:410567"
     Region          66..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Region          106..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Site            438
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Site            586
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Site            593..613
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Site            767..787
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Region          957..995
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Region          1036..1074
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Region          1079..1117
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CQ1.4)"
     Region          1125..1162
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68CQ1.4)"
     CDS             1..1323
                     /gene="MROH7"
                     /gene_synonym="C1orf175; HEATR8"
                     /coded_by="NM_001039464.4:293..4264"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41342.2"
                     /db_xref="GeneID:374977"
                     /db_xref="HGNC:HGNC:24802"
ORIGIN      
        1 malspganlv fhedpkmtps ppscgapglg sgtipqphpd maqvpmlnll pspglalvpd
       61 lndslspvsg easglvsent prpddsraia paslqitssc sgealdldsk dvsrpdsqgr
      121 lcpasnpils pssteaprls sgnhpqsnse dafkclsski fklgqrnsnp srhelnpfir
      181 hhsreglvlg hcisrpsska lliptsnssl dldsnpllnm gsrntsklnl nvapdshgtl
      241 ipdtnetitl ashnisesvs kgafsttwst ssketmnvas sghsrsdlsv titqasyvtl
      301 ipgssygisl hssthepnst isppscmtli lgsnetlsld ssllfsdtst ltlssqqdda
      361 kdnsihtvpl eenleswsem asikvgqfpl gfpisnpagk davtlqgipe gafdevtscl
      421 vkvpektegg nnmalvenvt tlqksqdlle aegekktmik kimrqiqeep ldslsssvrk
      481 qameiltqls htqptlgmre rselvnvcvh svfslpsvqa mqekdeakae tiqalyhqtl
      541 ealqtllkal fiedptpagl ksilealgpw mnsgkahera ravntnvsvl nhmlltlpff
      601 mplgfpalgl llgrlilhig dpdeeigcea ldgiiilyti lelqkrardk eetnkkelye
      661 snkhflgpyn pvspcqnilr vieefgdflg pqqikdllla aleglkgsse apgkdsremm
      721 qlasevmlss vlewyrhral evipeimqgi ymqlshiqep rarqvallpv sllassfmte
      781 vvvallmcpl plnsngaemw rqlilckpsc dvrdlldlll gslkekpvtk egrasivpla
      841 aasglcells vnscmgrvrr iypqlllall iqvhyhigln lpgcvappkd tkkgaqpspf
      901 vpvrwvvkvv ktlllrmgcs yettfledqg gwelmeqves hhrgvallar amvqyscqel
      961 crilyllipl lergdekhri tataffvell qmeqvrripe eyslgrmaeg lshhdpimkv
     1021 lsirglvila rrsektakvk allpsmvkgl knmdgmlvve avhnlkavfk grdqklmdsa
     1081 vyvemlqill phfsdarevv rsscinlygk vvqklraprt qameeqlvst lvpllltmqe
     1141 gnskvsqkcv ktllrcsyfm awelpkrays rkpwdnqqqt vakickclvn thrdsafifl
     1201 sqsleyakns raslrkcsvm figslvpcme simtedrlne vkaaldnlrh dpeasvciya
     1261 aqvqdhilas cwqnswlphg nswvcysatt hrwspscenl ptshqrrswi mqalgswkms
     1321 lkk
//
LOCUS       NP_002089                200 aa            linear   PRI 27-APR-2025
DEFINITION  guanylyl cyclase-activating protein 2 [Homo sapiens].
ACCESSION   NP_002089
VERSION     NP_002089.4
DBSOURCE    REFSEQ: accession NM_002098.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Avesani,A., Marino,V., Zanzoni,S., Koch,K.W. and Dell'Orco,D.
  TITLE     Molecular properties of human guanylate cyclase-activating protein
            2 (GCAP2) and its retinal dystrophy-associated variant G157R
  JOURNAL   J Biol Chem 296, 100619 (2021)
   PUBMED   33812995
  REMARK    GeneRIF: Molecular properties of human guanylate cyclase-activating
            protein 2 (GCAP2) and its retinal dystrophy-associated variant
            G157R.
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Sulmann,S., Kussrow,A., Bornhop,D.J. and Koch,K.W.
  TITLE     Label-free quantification of calcium-sensor targeting to
            photoreceptor guanylate cyclase and rhodopsin kinase by
            backscattering interferometry
  JOURNAL   Sci Rep 7, 45515 (2017)
   PUBMED   28361875
  REMARK    GeneRIF: GCAP1 and GCAP2 bound to different regions on the target
            guanylate cyclase type 1 with submicromolar affinity (apparent
            KD-values of 663 +/- 121 nM and 231 +/- 63 nM for Ca(2+)-free GCAP1
            and GCAP2, respectively).
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Peshenko,I.V., Olshevskaya,E.V. and Dizhoor,A.M.
  TITLE     Dimerization Domain of Retinal Membrane Guanylyl Cyclase 1 (RetGC1)
            Is an Essential Part of Guanylyl Cyclase-activating Protein (GCAP)
            Binding Interface
  JOURNAL   J Biol Chem 290 (32), 19584-19596 (2015)
   PUBMED   26100624
  REMARK    GeneRIF: Dimerization domain of RETGC1 is an essential part of
            GCAP1 and GCAP2 binding interface.
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Peshenko,I.V., Olshevskaya,E.V. and Dizhoor,A.M.
  TITLE     Evaluating the role of retinal membrane guanylyl cyclase 1 (RetGC1)
            domains in binding guanylyl cyclase-activating proteins (GCAPs)
  JOURNAL   J Biol Chem 290 (11), 6913-6924 (2015)
   PUBMED   25616661
  REMARK    GeneRIF: The GCAP1 and GCAP2 binding site(s) overlaps within the
            kinase homology and/or dimerization domains of retinal GC1.
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Otto-Bruc,A., Fariss,R.N., Haeseleer,F., Huang,J., Buczylko,J.,
            Surgucheva,I., Baehr,W., Milam,A.H. and Palczewski,K.
  TITLE     Localization of guanylate cyclase-activating protein 2 in mammalian
            retinas
  JOURNAL   Proc Natl Acad Sci U S A 94 (9), 4727-4732 (1997)
   PUBMED   9114059
REFERENCE   7  (residues 1 to 200)
  AUTHORS   Surguchov,A., Bronson,J.D., Banerjee,P., Knowles,J.A., Ruiz,C.,
            Subbaraya,I., Palczewski,K. and Baehr,W.
  TITLE     The human GCAP1 and GCAP2 genes are arranged in a tail-to-tail
            array on the short arm of chromosome 6 (p21.1)
  JOURNAL   Genomics 39 (3), 312-322 (1997)
   PUBMED   9119368
REFERENCE   8  (residues 1 to 200)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   9  (residues 1 to 200)
  AUTHORS   Wiegand,R.C., Kato,J., Huang,M.D., Fok,K.F., Kachur,J.F. and
            Currie,M.G.
  TITLE     Human guanylin: cDNA isolation, structure, and activity
  JOURNAL   FEBS Lett 311 (2), 150-154 (1992)
   PUBMED   1327879
REFERENCE   10 (residues 1 to 200)
  AUTHORS   de Sauvage,F.J., Keshav,S., Kuang,W.J., Gillett,N., Henzel,W. and
            Goeddel,D.V.
  TITLE     Precursor structure, expression, and tissue distribution of human
            guanylin
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 9089-9093 (1992)
   PUBMED   1409606
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL096814.26.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 26, 2007 this sequence version replaced NP_002089.3.
            
            Summary: The protein encoded by this gene is a calcium-binding
            protein that activates photoreceptor guanylate cyclases. This gene
            may have arisen due to a gene duplication event since there is a
            highly similar gene clustered with it on chromosome 6. Mutations in
            this gene can cause a form of retinitis pigmentosa. [provided by
            RefSeq, Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX537393.1, BQ636025.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1968968 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000230361.4/
                                                ENSP00000230361.3
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..200
                     /product="guanylyl cyclase-activating protein 2"
                     /note="guanylate cyclase-activating protein, photoreceptor
                     2; guanylate cyclase activator 1B (retina)"
                     /calculated_mol_wt=23289
     Region          34..171
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..200
                     /gene="GUCA1B"
                     /gene_synonym="GCAP 2; GCAP-2; GCAP-II; GCAP2; GUCA2;
                     RP48"
                     /coded_by="NM_002098.6:137..739"
                     /db_xref="CCDS:CCDS4865.1"
                     /db_xref="GeneID:2979"
                     /db_xref="HGNC:HGNC:4679"
                     /db_xref="MIM:602275"
ORIGIN      
        1 mgqefsweea eaageidvae lqewykkfvm ecpsgtlfmh efkrffkvtd deeasqyveg
       61 mfrafdkngd ntidfleyva alnlvlrgtl ehklkwtfki ydkdgngcid rlellniveg
      121 iyqlkkacrr elqteqgqll tpeevvdrif llvdengdgq lslnefvega rrdkwvmkml
      181 qmdmnpsswl aqqrrksamf
//
LOCUS       NP_079022                724 aa            linear   PRI 27-APR-2025
DEFINITION  HHIP-like protein 2 precursor [Homo sapiens].
ACCESSION   NP_079022
VERSION     NP_079022.2
DBSOURCE    REFSEQ: accession NM_024746.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Doyard,M., Fatih,N., Monnier,A., Island,M.L., Aubry,M., Leroyer,P.,
            Bouvet,R., Chales,G., Mosser,J., Loreal,O. and Guggenbuhl,P.
  TITLE     Iron excess limits HHIPL-2 gene expression and decreases
            osteoblastic activity in human MG-63 cells
  JOURNAL   Osteoporos Int 23 (10), 2435-2445 (2012)
   PUBMED   22237814
  REMARK    GeneRIF: HHIPL-2 was identified as a candidate gene involved in
            iron-related modulation of osteoblast markers.
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL592148.7, BC016552.1, DA868891.1 and AY358602.1.
            
            On Jan 27, 2007 this sequence version replaced NP_079022.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007638.1, AY358602.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000343410.7/ ENSP00000342118.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..724
                     /product="HHIP-like protein 2 precursor"
                     /note="HHIP-like protein 2; hedgehog interacting
                     protein-like 2"
                     /calculated_mol_wt=76442
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4356
     mat_peptide     42..724
                     /product="HHIP-like protein 2. /id=PRO_0000314964"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWX4.1)"
                     /calculated_mol_wt=76442
     Region          44..>182
                     /region_name="Folate_rec"
                     /note="Folate receptor family; pfam03024"
                     /db_xref="CDD:397250"
     Region          207..598
                     /region_name="YliI"
                     /note="Glucose/arabinose dehydrogenase, beta-propeller
                     fold [Carbohydrate transport and metabolism]; COG2133"
                     /db_xref="CDD:441736"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWX4.1)"
     Region          643..724
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWX4.1)"
     CDS             1..724
                     /gene="HHIPL2"
                     /gene_synonym="KIAA1822L"
                     /coded_by="NM_024746.4:61..2235"
                     /db_xref="CCDS:CCDS1530.2"
                     /db_xref="GeneID:79802"
                     /db_xref="HGNC:HGNC:25842"
                     /db_xref="MIM:620214"
ORIGIN      
        1 mlrtstpnlc gglhcrapwl ssgilclcli fllgqvgllq ghpqcldygp pfqpplhlef
       61 csdyesfgcc dqhkdrriaa rywdimeyfd lkrhelcgdy ikdilcqecs pyaahlydae
      121 ntqtplrnlp glcsdycsaf hsnchsaisl ltndrglqes hgrdgtrfch lldlpdkdyc
      181 fpnvlrndyl nrhlgmvaqd pqgclqlcls evanglrnpv smvhagdgth rffvaeqvgv
      241 vwvylpdgsr leqpfldlkn ivlttpwigd ergflglafh pkfrhnrkfy iyyscldkkk
      301 vekirisemk vsradpnkad lkservilei eepasnhngg qllfgldgym yiftgdggqa
      361 gdpfglfgna qnkssllgkv lridvnrags hgkryrvpsd npfvsepgah paiyaygirn
      421 mwrcavdrgd pitrqgrgri fcgdvgqnrf eevdlilkgg nygwrakegf acydkklchn
      481 aslddvlpiy ayghavgksv tggyvyrgce spnlnglyif gdfmsgrlma lqedrknkkw
      541 kkqdlclgst tscafpglis thskfiisfa edeagelyfl atsypsayap rgsiykfvdp
      601 srrappgkck ykpvpvrtks kripfrplak tvldllkeqs ekaarksssa tlasgpaqgl
      661 sekgsskkla sptsskntlr gpgtkkkarv gphvrqgkrr kslkshsgrm rpsaeqkrag
      721 rslp
//
LOCUS       NP_060510                528 aa            linear   PRI 27-APR-2025
DEFINITION  G patch domain-containing protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_060510
VERSION     NP_060510.1
DBSOURCE    REFSEQ: accession NM_018040.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Hu,F., Gou,L., Liu,Q., Zhang,W., Luo,M. and Zhang,X.
  TITLE     G-patch domain containing 2, a gene highly expressed in testes,
            inhibits nuclear factor-kappaB and cell proliferation
  JOURNAL   Mol Med Rep 11 (2), 1252-1257 (2015)
   PUBMED   25376275
  REMARK    GeneRIF: GPATC2 may be involved in inhibiting G1-S phase transition
            in 293T cells.
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Lin,M.L., Fukukawa,C., Park,J.H., Naito,K., Kijima,K., Shimo,A.,
            Ajiro,M., Nishidate,T., Nakamura,Y. and Katagiri,T.
  TITLE     Involvement of G-patch domain containing 2 overexpression in breast
            carcinogenesis
  JOURNAL   Cancer Sci 100 (8), 1443-1450 (2009)
   PUBMED   19432882
  REMARK    GeneRIF: Involvement of GPATCH2 overexpression in breast
            carcinogensis is reported.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354659.14, AK001114.1,
            AC096641.2 and CA311820.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The gene encodes a nuclear factor that may play a role in
            spermatogenesis and in tumor growth during breast cancer. The
            encoded protein contains a G-patch domain with an RNA binding
            motif. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Feb 2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.23504.1, AK001114.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366935.8/ ENSP00000355902.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..528
                     /product="G patch domain-containing protein 2 isoform 1"
                     /note="cancer/testis antigen 110; protein phosphatase 1,
                     regulatory subunit 30; G patch domain-containing protein
                     2"
                     /calculated_mol_wt=58813
     Region          36..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW75.1)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9NW75.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NW75.1)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NW75.1)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NW75.1)"
     Region          232..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW75.1)"
     Region          468..509
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     Region          487..528
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW75.1)"
     CDS             1..528
                     /gene="GPATCH2"
                     /gene_synonym="CT110; GPATC2; Pfa1; PPP1R30"
                     /coded_by="NM_018040.5:120..1706"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1518.1"
                     /db_xref="GeneID:55105"
                     /db_xref="HGNC:HGNC:25499"
                     /db_xref="MIM:616836"
ORIGIN      
        1 mfgaagrqpi gapaagnswh fsrtmeelvh dlvsaleess eqarggfaet gdhsrsiscp
       61 lkrqarkrrg rkrrsynvhh pwetghclse gsdssleeps kdyrenhnnn kkdhsdsddq
      121 mlvakrrpss nlnnnvrgkr plwhesdfav dnvgnrtlrr rrkvkrmavd lpqdisnkrt
      181 mtqppegcrd qdmdsdrayq yqeftknkvk krklkiirqg pkiqdegvvl eseetnqtnk
      241 dkmeceeqkv sdelmsesds sslsstdagl ftndegrqgd deqsdwfyek esggacgitg
      301 vvpwwekedp teldknvpdp vfesiltgsf plmshpsrrg fqarlsrlhg mssknikksg
      361 gtptsmvpip gpvgnkrmvh fspdshhhdh wfspgarteh dqhqllrdnr aerghkkncs
      421 vrtasrqtsm hlgslctgdi krrrkaaplp gpttagfvge naqpilenni gnrmlqnmgw
      481 tpgsglgrdg kgisepiqam qrpkglglgf plpkstsatt tpnagksa
//
LOCUS       NP_001356017             372 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001356017 XP_016871781
VERSION     NP_001356017.1
DBSOURCE    REFSEQ: accession NM_001369088.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            On Mar 18, 2019 this sequence version replaced XP_016871781.1.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.52721.1,
                                           SRR1660809.151213.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..372
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 5"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=42098
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..321
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..372
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369088.1:209..1327"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilks fallprleyn daisahcnlc lpgssdspas asqvagitgv
      361 sdaysqslpg ks
//
LOCUS       NP_001096640             407 aa            linear   PRI 27-APR-2025
DEFINITION  arylacetamide deacetylase-like 3 [Homo sapiens].
ACCESSION   NP_001096640 XP_006710400 XP_933387 XP_943439
VERSION     NP_001096640.2
DBSOURCE    REFSEQ: accession NM_001103170.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC244670.3, BG697255.1 and AK127828.1.
            
            On or before Apr 19, 2014 this sequence version replaced
            XP_006710400.1, NP_001096640.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG697255.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359318.8/ ENSP00000352268.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.21"
     Protein         1..407
                     /product="arylacetamide deacetylase-like 3"
                     /EC_number="3.1.1.-"
                     /calculated_mol_wt=46024
     Region          115..378
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
     Region          119..121
                     /region_name="Involved in the stabilization of the
                     negatively charged intermediate by the formation of the
                     oxyanion hole. /evidence=ECO:0000250|UniProtKB:Q5NUF3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUY0.5)"
     CDS             1..407
                     /gene="AADACL3"
                     /coded_by="NM_001103170.3:68..1291"
                     /db_xref="CCDS:CCDS41253.2"
                     /db_xref="GeneID:126767"
                     /db_xref="HGNC:HGNC:32037"
ORIGIN      
        1 mwdlalifla aacvfslgvt lwvicshfft vhipaavghp vklrvlhcif qllltwgmif
       61 eklricsmpq ffcfmqdlpp lkydpdvvvt dfrfgtipvk lyqpkastct lkpgivyyhg
      121 gggvmgslkt hhgicsrlck esdsvvlavg yrklpkhkfp vpvrdclvat ihflkslday
      181 gvdparvvvc gdsfggaiaa vvcqqlvdrp dlpriraqil iyailqaldl qtpsfqqrkn
      241 iplltwsfic yfffqnldfs sswqevimkg ahlpaevwek yrkwlgpeni perfkergyq
      301 lkphepmnea aylevsvvld vmcspliaed divsqlpetc ivsceydalr dnsllykkrl
      361 edlgvpvtwh hmedgfhgvl rtidmsflhf pcsmrilsal vqfvkgl
//
LOCUS       NP_001356033             320 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 11 [Homo
            sapiens].
ACCESSION   NP_001356033
VERSION     NP_001356033.1
DBSOURCE    REFSEQ: accession NM_001369104.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.46466.1,
                                           SRR1660805.184989.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..320
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 11"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=36568
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..281
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..320
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369104.1:209..1171"
                     /note="isoform 11 is encoded by transcript variant 25"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefikl qelvdrvler fqasglivke wnsvklhatv
      241 mntlfrkdpn aegrynlyta egkyifkere sfdgrnilks fallprleyn daisahcnlc
      301 lpgssdspas asqvagitvv
//
LOCUS       NP_001357464             774 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RFWD3 isoform 1 [Homo sapiens].
ACCESSION   NP_001357464 XP_005256078
VERSION     NP_001357464.1
DBSOURCE    REFSEQ: accession NM_001370535.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Moore,C.E., Yalcindag,S.E., Czeladko,H., Ravindranathan,R.,
            Wijesekara Hanthi,Y., Levy,J.C., Sannino,V., Schindler,D.,
            Ciccia,A., Costanzo,V. and Elia,A.E.H.
  TITLE     RFWD3 promotes ZRANB3 recruitment to regulate the remodeling of
            stalled replication forks
  JOURNAL   J Cell Biol 222 (5) (2023)
   PUBMED   37036693
  REMARK    GeneRIF: RFWD3 promotes ZRANB3 recruitment to regulate the
            remodeling of stalled replication forks.
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Zhu,Y., Peng,X., Wang,X., Ying,P., Wang,H., Li,B., Li,Y., Zhang,M.,
            Cai,Y., Lu,Z., Niu,S., Yang,N., Zhong,R., Tian,J., Chang,J. and
            Miao,X.
  TITLE     Systematic analysis on expression quantitative trait loci
            identifies a novel regulatory variant in ring finger and WD repeat
            domain 3 associated with prognosis of pancreatic cancer
  JOURNAL   Chin Med J (Engl) 135 (11), 1348-1357 (2022)
   PUBMED   35830250
  REMARK    GeneRIF: Systematic analysis on expression quantitative trait loci
            identifies a novel regulatory variant in ring finger and WD repeat
            domain 3 associated with prognosis of pancreatic cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Gallina,I., Hendriks,I.A., Hoffmann,S., Larsen,N.B., Johansen,J.,
            Colding-Christensen,C.S., Schubert,L., Selles-Baiget,S., Fabian,Z.,
            Kuhbacher,U., Gao,A.O., Raschle,M., Rasmussen,S., Nielsen,M.L.,
            Mailand,N. and Duxin,J.P.
  TITLE     The ubiquitin ligase RFWD3 is required for translesion DNA
            synthesis
  JOURNAL   Mol Cell 81 (3), 442-458 (2021)
   PUBMED   33321094
  REMARK    GeneRIF: The ubiquitin ligase RFWD3 is required for translesion DNA
            synthesis.
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Hsu,R.Y.C., Giri,S., Wang,Y., Lin,Y.C., Liu,D., Wopat,S.,
            Chakraborty,A., Prasanth,K.V. and Prasanth,S.G.
  TITLE     The E3 ligase RFWD3 stabilizes ORC in a p53-dependent manner
  JOURNAL   Cell Cycle 19 (21), 2927-2938 (2020)
   PUBMED   33044890
  REMARK    GeneRIF: The E3 ligase RFWD3 stabilizes ORC in a p53-dependent
            manner.
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Jia,J., Yang,Y., Yan,T., Chen,T. and Lu,G.
  TITLE     Down-regulation of RFWD3 inhibits cancer cells proliferation and
            migration in gastric carcinoma
  JOURNAL   Gen Physiol Biophys 39 (4), 363-371 (2020)
   PUBMED   32902405
  REMARK    GeneRIF: Down-regulation of RFWD3 inhibits cancer cells
            proliferation and migration in gastric carcinoma.
REFERENCE   6  (residues 1 to 774)
  AUTHORS   Dastani,Z., Pajukanta,P., Marcil,M., Rudzicz,N., Ruel,I.,
            Bailey,S.D., Lee,J.C., Lemire,M., Faith,J., Platko,J., Rioux,J.,
            Hudson,T.J., Gaudet,D., Engert,J.C. and Genest,J.
  TITLE     Fine mapping and association studies of a high-density lipoprotein
            cholesterol linkage region on chromosome 16 in French-Canadian
            subjects
  JOURNAL   Eur J Hum Genet 18 (3), 342-347 (2010)
   PUBMED   19844255
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 774)
  AUTHORS   Markson,G., Kiel,C., Hyde,R., Brown,S., Charalabous,P., Bremm,A.,
            Semple,J., Woodsmith,J., Duley,S., Salehi-Ashtiani,K., Vidal,M.,
            Komander,D., Serrano,L., Lehner,P. and Sanderson,C.M.
  TITLE     Analysis of the human E2 ubiquitin conjugating enzyme protein
            interaction network
  JOURNAL   Genome Res 19 (10), 1905-1911 (2009)
   PUBMED   19549727
REFERENCE   8  (residues 1 to 774)
  AUTHORS   van Wijk,S.J., de Vries,S.J., Kemmeren,P., Huang,A., Boelens,R.,
            Bonvin,A.M. and Timmers,H.T.
  TITLE     A comprehensive framework of E2-RING E3 interactions of the human
            ubiquitin-proteasome system
  JOURNAL   Mol Syst Biol 5, 295 (2009)
   PUBMED   19690564
  REMARK    Erratum:[Mol Syst Biol. 2009;5:317]
REFERENCE   9  (residues 1 to 774)
  AUTHORS   Tsuritani,K., Irie,T., Yamashita,R., Sakakibara,Y., Wakaguri,H.,
            Kanai,A., Mizushima-Sugano,J., Sugano,S., Nakai,K. and Suzuki,Y.
  TITLE     Distinct class of putative 'non-conserved' promoters in humans:
            comparative studies of alternative promoters of human and mouse
            genes
  JOURNAL   Genome Res 17 (7), 1005-1014 (2007)
   PUBMED   17567985
REFERENCE   10 (residues 1 to 774)
  AUTHORS   Mehta,P.A. and Ebens,C.
  TITLE     Fanconi Anemia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC109599.4.
            
            On May 9, 2019 this sequence version replaced XP_005256078.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.110044.1,
                                           SRR1803611.149781.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..774
                     /product="E3 ubiquitin-protein ligase RFWD3 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="RING finger and WD repeat domain-containing protein
                     3; E3 ubiquitin-protein ligase RFWD3; RING finger protein
                     201; RING-type E3 ubiquitin transferase RFWD3"
                     /calculated_mol_wt=84963
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM and ATR.
                     /evidence=ECO:0000269|PubMed:20173098,
                     ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28575658;
                     propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM and ATR.
                     /evidence=ECO:0000269|PubMed:20173098,
                     ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28575658;
                     propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          95..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          139..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          257..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          283..343
                     /region_name="mRING-C3HGC3_RFWD3"
                     /note="Modified RING finger, C3HGC3-type, found in RING
                     finger and WD repeat domain-containing protein 3 (RFWD3)
                     and similar proteins; cd16450"
                     /db_xref="CDD:438114"
     Region          495..537
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          496..762
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          500..537
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          539..577
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          543..580
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          583..628
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCD5.3)"
     Region          588..655
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..774
                     /gene="RFWD3"
                     /gene_synonym="FANCW; RNF201"
                     /coded_by="NM_001370535.1:217..2541"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS32486.1"
                     /db_xref="GeneID:55159"
                     /db_xref="HGNC:HGNC:25539"
                     /db_xref="MIM:614151"
ORIGIN      
        1 maheameydv qvqlnhaeqq papagmassq ggpallqpvp advvssqgvp silqpapaev
       61 issqatppll qpapqlsvdl tevevlgedt veninprtse qhrqgsdgnh tipasslhsm
      121 tnfisglqrl hgmleflrps ssnhsvgpmr trrrvsasrr araggsqrtd sarlraplda
      181 yfqvsrtqpd lpattydset rnpvseelqv ssssdsdsds saeyggvvdq aeesgavile
      241 eqlagvsaeq evtcidggkt lpkqpspqks epllpsasmd eeegdtctic leqwtnagdh
      301 rlsalrcghl fgyrcistwl kgqvrkcpqc nkkarhsdiv vlyartlral dtseqermks
      361 sllkeqmlrk qaelesaqcr lqlqvltdkc trlqrrvqdl qkltshqsqn lqqprgsqaw
      421 vlscspssqg qhkhkyhfqk tftvsqagnc rimaycdals clvisqpspq asflpgfgvk
      481 mlstanmkss qyipmhgkqi rglafssylr glllsasldn tikltsletn tvvqtynagr
      541 pvwsccwcld eanyiyagla ngsilvydvr ntsshvqelv aqkarcplvs lsympraasa
      601 afpyggvlag tledasfweq kmdfshwphv lplepggcid fqtenssrhc lvtyrpdknh
      661 ttirsvlmem syrlddtgnp icscqpvhtf fggptckllt knaifqspen dgnilvctgd
      721 eaansallwd aasgsllqdl qtdqpvldic pfevnrnsyl atltekmvhi ykwe
//
LOCUS       NP_004861                247 aa            linear   PRI 27-APR-2025
DEFINITION  mannose-P-dolichol utilization defect 1 protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_004861
VERSION     NP_004861.2
DBSOURCE    REFSEQ: accession NM_004870.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Bennett,D.C., Cazet,A., Charest,J. and Contessa,J.N.
  TITLE     MPDU1 regulates CEACAM1 and cell adhesion in vitro and in vivo
  JOURNAL   Glycoconj J 35 (3), 265-274 (2018)
   PUBMED   29671116
  REMARK    GeneRIF: These experiments also confirmed that protein levels of
            CEACAM-1, which functions in cell adhesion, is dependent on LLO
            biosynthesis in vivo. Kato III cells and the MPDU1-rescued Kato
            IIIM cells therefore provide a novel model to examine the
            consequences of defective LLO biosynthesis both in vitro and in
            vivo.
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Bastaki,F., Bizzari,S., Hamici,S., Nair,P., Mohamed,M., Saif,F.,
            Malik,E.M., Al-Ali,M.T. and Hamzeh,A.R.
  TITLE     Single-center experience of N-linked Congenital Disorders of
            Glycosylation with a Summary of Molecularly Characterized Cases in
            Arabs
  JOURNAL   Ann Hum Genet 82 (1), 35-47 (2018)
   PUBMED   28940310
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Chen,Z., Tao,S., Gao,Y., Zhang,J., Hu,Y., Mo,L., Kim,S.T., Yang,X.,
            Tan,A., Zhang,H., Qin,X., Li,L., Wu,Y., Zhang,S., Zheng,S.L.,
            Xu,J., Mo,Z. and Sun,J.
  TITLE     Genome-wide association study of sex hormones, gonadotropins and
            sex hormone-binding protein in Chinese men
  JOURNAL   J Med Genet 50 (12), 794-801 (2013)
   PUBMED   24049095
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Schenk,B., Imbach,T., Frank,C.G., Grubenmann,C.E., Raymond,G.V.,
            Hurvitz,H., Korn-Lubetzki,I., Revel-Vik,S., Raas-Rotschild,A.,
            Luder,A.S., Jaeken,J., Berger,E.G., Matthijs,G., Hennet,T. and
            Aebi,M.
  TITLE     MPDU1 mutations underlie a novel human congenital disorder of
            glycosylation, designated type If
  JOURNAL   J Clin Invest 108 (11), 1687-1695 (2001)
   PUBMED   11733564
  REMARK    Erratum:[J Clin Invest. 2003 Mar;111(6):925]
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Kranz,C., Denecke,J., Lehrman,M.A., Ray,S., Kienz,P., Kreissel,G.,
            Sagi,D., Peter-Katalinic,J., Freeze,H.H., Schmid,T.,
            Jackowski-Dohrmann,S., Harms,E. and Marquardt,T.
  TITLE     A mutation in the human MPDU1 gene causes congenital disorder of
            glycosylation type If (CDG-If)
  JOURNAL   J Clin Invest 108 (11), 1613-1619 (2001)
   PUBMED   11733556
REFERENCE   8  (residues 1 to 247)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
REFERENCE   9  (residues 1 to 247)
  AUTHORS   Ware,F.E. and Lehrman,M.A.
  TITLE     Expression cloning of a novel suppressor of the Lec15 and Lec35
            glycosylation mutations of Chinese hamster ovary cells
  JOURNAL   J Biol Chem 271 (24), 13935-13938 (1996)
   PUBMED   8663248
  REMARK    Erratum:[J Biol Chem. 1998 May 22;273(21):13366. PMID: 12755100]
REFERENCE   10 (residues 1 to 247)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC001898.1, BG776573.1,
            BM127836.1 and BQ002417.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 24, 2006 this sequence version replaced NP_004861.1.
            
            Summary: This gene encodes an endoplasmic reticulum membrane
            protein that is required for utilization of the mannose donor
            mannose-P-dolichol in the synthesis of lipid-linked
            oligosaccharides and glycosylphosphatidylinositols. Mutations in
            this gene result in congenital disorder of glycosylation type If.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KY814480.1, KY814481.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000250124.11/ ENSP00000250124.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..247
                     /product="mannose-P-dolichol utilization defect 1 protein
                     isoform 1"
                     /note="mannose-P-dolichol utilization defect 1 protein;
                     suppressor of Lec15 and Lec35 glycosylation mutation
                     homolog; HBeAg-binding protein 2 binding protein A"
                     /calculated_mol_wt=26507
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (O75352.2)"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75352.2)"
     Region          40..235
                     /region_name="2A43"
                     /note="Lysosomal Cystine Transporter; TIGR00951"
                     /db_xref="CDD:130026"
     Site            74..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75352.2)"
     Site            100..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75352.2)"
     Site            128..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75352.2)"
     Site            151..171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75352.2)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75352.2)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75352.2)"
     CDS             1..247
                     /gene="MPDU1"
                     /gene_synonym="CDGIF; HBEBP2BPA; Lec35; My008; PP3958;
                     PQLC5; SL15; SLC66A5"
                     /coded_by="NM_004870.4:12..755"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11115.1"
                     /db_xref="GeneID:9526"
                     /db_xref="HGNC:HGNC:7207"
                     /db_xref="MIM:604041"
ORIGIN      
        1 maaeadgplk rllvpillpe kcydqlfvqw dllhvpclki llskglglgi vagsllvklp
       61 qvfkilgaks aeglslqsvm lelvaltgtm vysitnnfpf sswgealflm lqtiticflv
      121 mhyrgqtvkg vaflacyglv llvllspltp ltvvtllqas nvpavvvgrl lqaatnyhng
      181 htgqlsaitv fllfggslar iftsiqetgd plmagtfvvs slcngliaaq llfywnakpp
      241 hkqkkaq
//
LOCUS       NP_001354476             565 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 40 [Homo sapiens].
ACCESSION   NP_001354476
VERSION     NP_001354476.1
DBSOURCE    REFSEQ: accession NM_001367547.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..565
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 40"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=63050
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          433..560
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..565
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367547.1:95..1792"
                     /note="isoform 40 is encoded by transcript variant 40"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk krkssssvhl msnnknslvs paqepaplqt
      361 amepqttvvh natdgikgst escntttede dlkaaplrtg ngssvpegrs srdrtapsag
      421 mqpqpslcss amrkqeiiki teqlieainn gdfeaytkic dpgltsfepe algnlvegmd
      481 fhkfyfenll sknskpihtt ilnphvhvig edaaciayir ltqyidgqgr prtsqseetr
      541 vwhrrdgkwl nvhyhcsgap aaplq
//
LOCUS       NP_055052                739 aa            linear   PRI 27-APR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 18
            isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_055052
VERSION     NP_055052.1
DBSOURCE    REFSEQ: accession NM_014237.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Lingappa,J.R., Petrovski,S., Kahle,E., Fellay,J., Shianna,K.,
            McElrath,M.J., Thomas,K.K., Baeten,J.M., Celum,C., Wald,A., de
            Bruyn,G., Mullins,J.I., Nakku-Joloba,E., Farquhar,C., Essex,M.,
            Donnell,D., Kiarie,J., Haynes,B. and Goldstein,D.
  CONSRTM   Partners in Prevention HSV/HIV Transmission Study Team
  TITLE     Genomewide association study for determinants of HIV-1 acquisition
            and viral set point in HIV-1 serodiscordant couples with quantified
            virus exposure
  JOURNAL   PLoS One 6 (12), e28632 (2011)
   PUBMED   22174851
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Frayne,J., Hurd,E.A. and Hall,L.
  TITLE     Human tMDC III: a sperm protein with a potential role in oocyte
            recognition
  JOURNAL   Mol Hum Reprod 8 (9), 817-822 (2002)
   PUBMED   12200459
  REMARK    GeneRIF: we have determined the complete nucleotide sequence of
            human tMDC III cDNA , human tMDC III contains a putative
            integrin-binding glu-cys-asp (ECD) motif, the relevance of which is
            discussed in the context of a possible role in oolemma binding.
REFERENCE   4  (residues 1 to 739)
  AUTHORS   Zhu,G.Z., Lin,Y., Myles,D.G. and Primakoff,P.
  TITLE     Identification of four novel ADAMs with potential roles in
            spermatogenesis and fertilization
  JOURNAL   Gene 234 (2), 227-237 (1999)
   PUBMED   10395895
REFERENCE   5  (residues 1 to 739)
  AUTHORS   Frayne,J., Jury,J.A., Barker,H.L., Perry,A.C., Jones,R. and Hall,L.
  TITLE     Macaque MDC family of proteins: sequence analysis, tissue
            distribution and processing in the male reproductive tract
  JOURNAL   Mol Hum Reprod 4 (5), 429-437 (1998)
   PUBMED   9665629
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB049415.1, AK313961.1,
            AY358321.1 and AC136365.5.
            
            Summary: This gene encodes a member of the ADAM (a disintegrin and
            metalloprotease domain) family. Members of this family are
            membrane-anchored proteins structurally related to snake venom
            disintegrins, and have been implicated in a variety of biologic
            processes involving cell-cell and cell-matrix interactions,
            including fertilization, muscle development, and neurogenesis. The
            encoded preproprotein is proteolytically processed to generate the
            mature sperm surface protein. Alternative splicing results in
            multiple transcript variants, at least one of which encodes an
            isoform that is proteolytically processed. [provided by RefSeq, Feb
            2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes isoform 1 (disintegrin and metalloproteinase
            domain-containing protein 18).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313961.1, BC121045.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265707.10/ ENSP00000265707.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.22"
     Protein         1..739
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 18 isoform 1 preproprotein"
                     /note="a disintegrin and metalloproteinase domain 18;
                     disintegrin and metalloproteinase domain-containing
                     protein 18; transmembrane metalloproteinase-like,
                     disintegrin-like, and cysteine-rich protein III"
                     /calculated_mol_wt=81073
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1802
     Region          27..141
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Site            122
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Site            149
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Region          184..378
                     /region_name="ZnMc_adamalysin_II_like"
                     /note="Zinc-dependent metalloprotease; adamalysin_II_like
                     subfamily. Adamalysin II is a snake venom zinc
                     endopeptidase. This subfamily contains other snake venom
                     metalloproteinases, as well as membrane-anchored
                     metalloproteases belonging to the ADAM family; cd04269"
                     /db_xref="CDD:239797"
     mat_peptide     185..739
                     /product="Disintegrin and metalloproteinase
                     domain-containing protein 18. /id=PRO_0000029097"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
                     /calculated_mol_wt=61770
     Site            294
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Site            order(319..320,323,329)
                     /site_type="active"
                     /db_xref="CDD:239797"
     Site            359
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Region          399..476
                     /region_name="DISIN"
                     /note="Homologues of snake disintegrins; smart00050"
                     /db_xref="CDD:214490"
     Site            465
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Region          478..617
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     Site            561
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Site            611
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Site            625
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     Site            688..708
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3Q7.1)"
     CDS             1..739
                     /gene="ADAM18"
                     /gene_synonym="ADAM27; tMDCIII"
                     /coded_by="NM_014237.3:56..2275"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS6113.1"
                     /db_xref="GeneID:8749"
                     /db_xref="HGNC:HGNC:196"
                     /db_xref="MIM:619495"
ORIGIN      
        1 mflllallte lgrlqahegs egiflhvtvp rkiksndsev serkmiyiit idgqpytlhl
       61 gkqsflpqnf lvytynetgs lhsvspyfmm hchyqgyaae fpnsfvtlsi csglrgflqf
      121 enisygiepv essarfehii yqmknndpnv silavnyshi wqkdqpykvp lnsqiknlsk
      181 llpqyleiyi ivekalydym gsemmavtqk ivqviglvnt mftqfkltvi lsslelwsne
      241 nqistsgdad dilqrflawk rdylilrphd iayllvyrkh pkyvgatfpg tvcnksydag
      301 iamypdaigl egfsviiaql lglnvgltyd ditqcfclra tcimnheavs asgrkifsnc
      361 smhdyryfvs kfetkclqkl snlqplhqnq pvcgngiles neecdcgnkn ecqfkkccdy
      421 ntcklkgsvk cgsgpcctsk celsiagtpc rksidpecdf teycngtssn cvpdtyalng
      481 rlcklgtayc yngqcqttdn qcakifgkga qgapfacfke vnslhersen cgfknsqplp
      541 cerkdvlcgk lacvqphkna nksdaqstvy syiqdhvcvs iatgssmrsd gtdnayvadg
      601 tmcgpemycv nktcrkvhlm gyncnattkc kgkgicnnfg ncqcfpghrp pdckfqfgsp
      661 ggsiddgnfq ksgdfytekg ynthwnnwfi lsfciflpff ivfttvifkr neiskscnre
      721 naeynrnssv vsesddvgh
//
LOCUS       NP_084097                118 aa            linear   ROD 27-APR-2025
DEFINITION  5-hydroxyisourate hydrolase isoform 2 [Mus musculus].
ACCESSION   NP_084097 XP_001000224 XP_001000233 XP_001000250 XP_001000264
            XP_133915 XP_905171 XP_905173 XP_905176 XP_923031 XP_930465
            XP_930467 XP_930468
VERSION     NP_084097.1
DBSOURCE    REFSEQ: accession NM_029821.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Lu,J., Dalbeth,N., Yin,H., Li,C., Merriman,T.R. and Wei,W.H.
  TITLE     Mouse models for human hyperuricaemia: a critical review
  JOURNAL   Nat Rev Rheumatol 15 (7), 413-426 (2019)
   PUBMED   31118497
  REMARK    Review article
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Baey,C., Yang,J., Ronchese,F. and Harper,J.L.
  TITLE     Hyperuricaemic UrahPlt2/Plt2 mice show altered T cell proliferation
            and defective tumor immunity after local immunotherapy with Poly
            I:C
  JOURNAL   PLoS One 13 (11), e0206827 (2018)
   PUBMED   30383838
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Stevenson,W.S., Hyland,C.D., Zhang,J.G., Morgan,P.O., Willson,T.A.,
            Gill,A., Hilton,A.A., Viney,E.M., Bahlo,M., Masters,S.L.,
            Hennebry,S., Richardson,S.J., Nicola,N.A., Metcalf,D., Hilton,D.J.,
            Roberts,A.W. and Alexander,W.S.
  TITLE     Deficiency of 5-hydroxyisourate hydrolase causes hepatomegaly and
            hepatocellular carcinoma in mice
  JOURNAL   Proc Natl Acad Sci U S A 107 (38), 16625-16630 (2010)
   PUBMED   20823251
  REMARK    GeneRIF: Substitution of cysteine for tyrosine in a conserved
            helical region of HIU hydrolase resulted in undetectable protein
            expression. Homozygotes for the mutation had elevated platelet
            counts secondary to excess thrombopoietin production and
            hepatomegaly.
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Lee,Y., Park,B.C., Lee,D.H., Bae,K.H., Cho,S., Lee,C.H., Lee,J.S.,
            Myung,P.K. and Park,S.G.
  TITLE     Mouse transthyretin-related protein is a hydrolase which degrades
            5-hydroxyisourate, the end product of the uricase reaction
  JOURNAL   Mol Cells 22 (2), 141-145 (2006)
   PUBMED   17085964
  REMARK    GeneRIF: Study provides evidence that mouse transthyretin-related
            protein facilitates the hydrolysis of 5-hydroxyisourate, the end
            product of the uricase reaction.
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Ramazzina,I., Folli,C., Secchi,A., Berni,R. and Percudani,R.
  TITLE     Completing the uric acid degradation pathway through phylogenetic
            comparison of whole genomes
  JOURNAL   Nat Chem Biol 2 (3), 144-148 (2006)
   PUBMED   16462750
  REMARK    GeneRIF: Identified as the gene encoding the enzyme catalyzing the
            second step of the pathway from uric acid to S-allantoin.
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Nishimura,M., Yokoi,N., Miki,T., Horikawa,Y., Yoshioka,H.,
            Takeda,J., Ohara,O. and Seino,S.
  TITLE     Construction of a multi-functional cDNA library specific for mouse
            pancreatic islets and its application to microarray
  JOURNAL   DNA Res 11 (5), 315-323 (2004)
   PUBMED   15747579
REFERENCE   7  (residues 1 to 118)
  AUTHORS   Trams,E.G. and Lauter,C.J.
  TITLE     Adenosine deaminase of cultured brain cells
  JOURNAL   Biochem J 152 (3), 681-687 (1975)
   PUBMED   16742956
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK004470.1, BY145477.1, AK013117.1 and BP776625.1.
            
            On or before Jul 24, 2006 this sequence version replaced
            XP_923031.1, XP_930468.1, XP_930467.1, XP_930465.1, XP_133915.3,
            XP_905176.1, XP_905173.1, XP_905171.1, XP_001000250.1,
            XP_001000233.1, XP_001000264.1, XP_001000224.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2) is
            shorter at the N-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY704695.1, AK004470.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 86.03 cM"
     Protein         1..118
                     /product="5-hydroxyisourate hydrolase isoform 2"
                     /EC_number="3.5.2.17"
                     /note="5-hydroxyisourate hydrolase; HIU hydrolase;
                     transthyretin-related protein"
                     /calculated_mol_wt=13428
     Region          6..118
                     /region_name="TLP_HIUase"
                     /note="HIUase (5-hydroxyisourate hydrolase) catalyzes the
                     second step in a three-step ureide pathway in which
                     5-hydroxyisourate (HIU), a product of the uricase (urate
                     oxidase) reaction, is hydrolyzed to
                     2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU);
                     cd05822"
                     /db_xref="CDD:100114"
     Site            order(11,13,51,102,104,106,115)
                     /site_type="active"
                     /db_xref="CDD:100114"
     Site            order(15..18,84..85,87,91..93,108,110..116)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:100114"
     CDS             1..118
                     /gene="Urah"
                     /gene_synonym="1190003J15Rik; 2810420C16Rik; HIUHase"
                     /coded_by="NM_029821.3:343..699"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS21986.1"
                     /db_xref="GeneID:76974"
                     /db_xref="MGI:MGI:1916142"
ORIGIN      
        1 matesspltt hvldtasglp aqglclrlsr leapcqqwme lrtsytnldg rcpglltpsq
       61 ikpgtyklff dterywkerg qesfypyvev vftitketqk fhvplllspw syttyrgs
//
LOCUS       NP_057356                344 aa            linear   PRI 27-APR-2025
DEFINITION  protein Tob2 [Homo sapiens].
ACCESSION   NP_057356
VERSION     NP_057356.1
DBSOURCE    REFSEQ: accession NM_016272.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Wang,Y.H., Li,S.Y., Yuan,S.J., Pan,Y.X., Hua,Y. and Liu,J.Y.
  TITLE     MiR-375 promotes human periodontal ligament stem cells
            proliferation and osteogenic differentiation by targeting
            transducer of ERBB2, 2
  JOURNAL   Arch Oral Biol 117, 104818 (2020)
   PUBMED   32619704
  REMARK    GeneRIF: MiR-375 promotes human periodontal ligament stem cells
            proliferation and osteogenic differentiation by targeting
            transducer of ERBB2, 2.
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Chen,C.A., Strouz,K., Huang,K.L. and Shyu,A.B.
  TITLE     Tob2 phosphorylation regulates global mRNA turnover to reshape
            transcriptome and impact cell proliferation
  JOURNAL   RNA 26 (9), 1143-1159 (2020)
   PUBMED   32404348
  REMARK    GeneRIF: Tob2 phosphorylation regulates global mRNA turnover to
            reshape transcriptome and impact cell proliferation.
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Yoshida,Y., Hosoda,E., Nakamura,T. and Yamamoto,T.
  TITLE     Association of ANA, a member of the antiproliferative Tob family
            proteins, with a Caf1 component of the CCR4 transcriptional
            regulatory complex
  JOURNAL   Jpn J Cancer Res 92 (6), 592-596 (2001)
   PUBMED   11429045
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Hirosawa,M., Nagase,T., Murahashi,Y., Kikuno,R. and Ohara,O.
  TITLE     Identification of novel transcribed sequences on human chromosome
            22 by expressed sequence tag mapping
  JOURNAL   DNA Res 8 (1), 1-9 (2001)
   PUBMED   11258795
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Suzuki,T., Matsuda,S., Tsuzuku,J.K., Yoshida,Y. and Yamamoto,T.
  TITLE     A serine/threonine kinase p90rsk1 phosphorylates the
            anti-proliferative protein Tob
  JOURNAL   Genes Cells 6 (2), 131-138 (2001)
   PUBMED   11260258
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Ikematsu,N., Yoshida,Y., Kawamura-Tsuzuku,J., Ohsugi,M., Onda,M.,
            Hirai,M., Fujimoto,J. and Yamamoto,T.
  TITLE     Tob2, a novel anti-proliferative Tob/BTG1 family member, associates
            with a component of the CCR4 transcriptional regulatory complex
            capable of binding cyclin-dependent kinases
  JOURNAL   Oncogene 18 (52), 7432-7441 (1999)
   PUBMED   10602502
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM453650.1, AB051450.1, BC038957.1 and AI362988.1.
            
            Summary: TOB2 belongs to the TOB (see TOB1; MIM 605523)/BTG1 (MIM
            109580) family of antiproliferative proteins, which are involved in
            the regulation of cell cycle progression.[supplied by OMIM, Apr
            2004].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038957.1, AB051450.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327492.4/ ENSP00000331305.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..344
                     /product="protein Tob2"
                     /note="protein Tob4; transducer of erbB-2 2"
                     /calculated_mol_wt=36501
     Region          1..106
                     /region_name="BTG"
                     /note="BTG family; cl15439"
                     /db_xref="CDD:472808"
     Region          144..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14106.2)"
     Region          191..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14106.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14106.2)"
     CDS             1..344
                     /gene="TOB2"
                     /gene_synonym="APRO5; TOB4; TOBL; TROB2"
                     /coded_by="NM_016272.4:486..1520"
                     /db_xref="CCDS:CCDS14015.1"
                     /db_xref="GeneID:10766"
                     /db_xref="HGNC:HGNC:11980"
                     /db_xref="MIM:607396"
ORIGIN      
        1 mqleikvaln fiisylynkl prrradlfge elerllkkky eghwypekpl kgsgfrcvhi
       61 gemvdpvvel aakrsglave dvranvpeel svwidpfevs yqigekgavk vlylddsegc
      121 gapeldkeik ssfnpdaqvf vpigsqdssl snspspsfgq spsptfiprs aqpitfttas
      181 faatkfgstk mkkgggaasg ggvassgagg qqppqqprma rsptnsllkh kslslsmhsl
      241 nfitanpapq sqlspnakef vyngggspsl ffdaadgqgs gtpgpfggsg agtcnsssfd
      301 maqvfgggan slflektpfv eglsynlntm qypsqqfqpv vlan
//
LOCUS       NP_775876                272 aa            linear   PRI 27-APR-2025
DEFINITION  potassium channel regulatory protein isoform 1 [Homo sapiens].
ACCESSION   NP_775876
VERSION     NP_775876.1
DBSOURCE    REFSEQ: accession NM_173605.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Usman,H. and Mathew,M.K.
  TITLE     Potassium channel regulator KCNRG regulates surface expression of
            Shaker-type potassium channels
  JOURNAL   Biochem Biophys Res Commun 391 (3), 1301-1305 (2010)
   PUBMED   19968958
  REMARK    GeneRIF: KCNRG is an ER-associated protein, which is proposed to
            regulate Kv1 family channel proteins by retaining a fraction of
            channels in endomembranes.
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Birerdinc,A., Nohelty,E., Marakhonov,A., Manyam,G., Panov,I.,
            Coon,S., Nikitin,E., Skoblov,M., Chandhoke,V. and Baranova,A.
  TITLE     Pro-apoptotic and antiproliferative activity of human KCNRG, a
            putative tumor suppressor in 13q14 region
  JOURNAL   Tumour Biol 31 (1), 33-45 (2010)
   PUBMED   20237900
  REMARK    GeneRIF: The haploinsufficiency of KCNRG might be relevant to the
            progression of chronic lymphocytic leukemia (CLL)and multiple
            myeloma(MM) at least in a subset of patients.
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Alimohammadi,M., Dubois,N., Skoldberg,F., Hallgren,A., Tardivel,I.,
            Hedstrand,H., Haavik,J., Husebye,E.S., Gustafsson,J., Rorsman,F.,
            Meloni,A., Janson,C., Vialettes,B., Kajosaari,M., Egner,W.,
            Sargur,R., Ponten,F., Amoura,Z., Grimfeld,A., De Luca,F.,
            Betterle,C., Perheentupa,J., Kampe,O. and Carel,J.C.
  TITLE     Pulmonary autoimmunity as a feature of autoimmune polyendocrine
            syndrome type 1 and identification of KCNRG as a bronchial
            autoantigen
  JOURNAL   Proc Natl Acad Sci U S A 106 (11), 4396-4401 (2009)
   PUBMED   19251657
  REMARK    GeneRIF: Autoantibodies to KCNRG were present in 7 of the 8
            patients with respiratory symptoms in autoimmune polyendocrine
            syndrome type 1
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Cho,Y.G., Kim,C.J., Song,J.H., Rhie,D.J., Park,Y.K., Kim,S.Y.,
            Nam,S.W., Yoo,N.J., Lee,J.Y. and Park,W.S.
  TITLE     Genetic and expression analysis of the KCNRG gene in hepatocellular
            carcinomas
  JOURNAL   Exp Mol Med 38 (3), 247-255 (2006)
   PUBMED   16819283
  REMARK    GeneRIF: Results suggest that genetic alterations and the
            expression of KCNRG might play an important role in the development
            and/or progression of a subset of hepatocellular carcinoma.
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Skoblov,M., Shakhbazov,K., Oshchepkov,D., Ivanov,D., Guskova,A.,
            Ivanov,D., Rubtsov,P., Prasolov,V., Yankovsky,N. and Baranova,A.
  TITLE     Human RFP2 gene promoter: unique structure and unusual strength
  JOURNAL   Biochem Biophys Res Commun 342 (3), 859-866 (2006)
   PUBMED   16499869
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Corcoran,M.M., Hammarsund,M., Zhu,C., Lerner,M., Kapanadze,B.,
            Wilson,B., Larsson,C., Forsberg,L., Ibbotson,R.E., Einhorn,S.,
            Oscier,D.G., Grander,D. and Sangfelt,O.
  TITLE     DLEU2 encodes an antisense RNA for the putative bicistronic
            RFP2/LEU5 gene in humans and mouse
  JOURNAL   Genes Chromosomes Cancer 40 (4), 285-297 (2004)
   PUBMED   15188451
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Ivanov,D.V., Tyazhelova,T.V., Lemonnier,L., Kononenko,N.,
            Pestova,A.A., Nikitin,E.A., Prevarskaya,N., Skryma,R.,
            Panchin,Y.V., Yankovsky,N.K. and Baranova,A.V.
  TITLE     A new human gene KCNRG encoding potassium channel regulating
            protein is a cancer suppressor gene candidate located in 13q14.3
  JOURNAL   FEBS Lett 539 (1-3), 156-160 (2003)
   PUBMED   12650944
  REMARK    GeneRIF: the primary characterization of a new gene KCNRG mapped at
            chromosome band 13q14.3; is a candidate for a B-cell chronic
            lymphocytic leukemia and prostate cancer tumor suppressor gene
            GeneRIF: KCNRG suppresses K+ channel activity in human prostate
            cell line LNCaP.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY169388.1.
            
            Summary: This gene encodes a protein which regulates the activity
            of voltage-gated potassium channels. This gene is on chromosome 13
            and overlaps the gene for tripartite motif containing 13 on the
            same strand. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Feb
            2012].
            
            Transcript Variant: This variant (1) is the shorter transcript and
            encodes the longer protein (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY129654.1, AY169388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312942.2/ ENSP00000324191.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..272
                     /product="potassium channel regulatory protein isoform 1"
                     /note="putative potassium channel regulatory protein"
                     /calculated_mol_wt=30917
     Region          5..101
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     CDS             1..272
                     /gene="KCNRG"
                     /gene_synonym="DLTET"
                     /coded_by="NM_173605.2:51..869"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9424.1"
                     /db_xref="GeneID:283518"
                     /db_xref="HGNC:HGNC:18893"
                     /db_xref="MIM:607947"
ORIGIN      
        1 mssqelvtln vggkifttrf stikqfpasr larmldgrdq efkmvggqif vdrdgdlfsf
       61 ildflrthql llptefsdyl rlqrealfye lrslvdllnp yllqprpalv evhflsrntq
      121 affrvfgscs ktiemltgri tvfteqpsap twngnffppq mtllplppqr psyhdlvfqc
      181 gsdsttdnqt gvryvsikpd nrklangtnv lgllidtllk egfhlvstrt vssedktecy
      241 sferikspev litnetpkpe tiiipeqsqi kk
//
LOCUS       NP_071731                448 aa            linear   PRI 27-APR-2025
DEFINITION  tumor necrosis factor receptor superfamily member EDAR precursor
            [Homo sapiens].
ACCESSION   NP_071731
VERSION     NP_071731.1
DBSOURCE    REFSEQ: accession NM_022336.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Fang,Z., Wang,Y., Huang,B., Chen,X., Jiang,R. and Yin,M.
  TITLE     Depletion of G9A attenuates imiquimod-induced psoriatic dermatitis
            via targeting EDAR-NF-kappaB signaling in keratinocyte
  JOURNAL   Cell Death Dis 14 (9), 627 (2023)
   PUBMED   37739945
  REMARK    GeneRIF: Depletion of G9A attenuates imiquimod-induced psoriatic
            dermatitis via targeting EDAR-NF-kappaB signaling in keratinocyte.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Yagi,S., Yasuno,S., Ansai,O., Hayashi,R. and Shimomura,Y.
  TITLE     Different degree of loss-of-function among four missense mutations
            in the EDAR gene responsible for autosomal recessive hypohidrotic
            ectodermal dysplasia may be associated with the phenotypic severity
  JOURNAL   J Dermatol 50 (3), 349-356 (2023)
   PUBMED   36258277
  REMARK    GeneRIF: Different degree of loss-of-function among four missense
            mutations in the EDAR gene responsible for autosomal recessive
            hypohidrotic ectodermal dysplasia may be associated with the
            phenotypic severity.
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Zhao,Z., Zhang,T., Li,T., Ye,Y., Feng,C., Wang,H. and Zhang,X.
  TITLE     A novel EDAR variant identified in non-syndromic tooth agenesis:
            Insights from molecular dynamics
  JOURNAL   Arch Oral Biol 146, 105600 (2023)
   PUBMED   36470092
  REMARK    GeneRIF: A novel EDAR variant identified in non-syndromic tooth
            agenesis: Insights from molecular dynamics.
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Williams,R., Jobling,S., Sims,A.H., Mou,C., Wilkinson,L.,
            Collu,G.M., Streuli,C.H., Gilmore,A.P., Headon,D.J. and Brennan,K.
  TITLE     Elevated EDAR signalling promotes mammary gland tumourigenesis with
            squamous metaplasia
  JOURNAL   Oncogene 41 (7), 1040-1049 (2022)
   PUBMED   34916592
  REMARK    GeneRIF: Elevated EDAR signalling promotes mammary gland
            tumourigenesis with squamous metaplasia.
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Coletta,D.K., Hlusko,L.J., Scott,G.R., Garcia,L.A., Vachon,C.M.,
            Norman,A.D., Funk,J.L., Shaibi,G.Q., Hernandez,V., De Filippis,E.
            and Mandarino,L.J.
  TITLE     Association of EDARV370A with breast density and metabolic syndrome
            in Latinos
  JOURNAL   PLoS One 16 (10), e0258212 (2021)
   PUBMED   34618839
  REMARK    GeneRIF: Association of EDARV370A with breast density and metabolic
            syndrome in Latinos.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Kumar,A., Eby,M.T., Sinha,S., Jasmin,A. and Chaudhary,P.M.
  TITLE     The ectodermal dysplasia receptor activates the nuclear
            factor-kappaB, JNK, and cell death pathways and binds to
            ectodysplasin A
  JOURNAL   J Biol Chem 276 (4), 2668-2677 (2001)
   PUBMED   11035039
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Monreal,A.W., Ferguson,B.M., Headon,D.J., Street,S.L.,
            Overbeek,P.A. and Zonana,J.
  TITLE     Mutations in the human homologue of mouse dl cause autosomal
            recessive and dominant hypohidrotic ectodermal dysplasia
  JOURNAL   Nat Genet 22 (4), 366-369 (1999)
   PUBMED   10431241
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Ho,L., Williams,M.S. and Spritz,R.A.
  TITLE     A gene for autosomal dominant hypohidrotic ectodermal dysplasia
            (EDA3) maps to chromosome 2q11-q13
  JOURNAL   Am J Hum Genet 62 (5), 1102-1106 (1998)
   PUBMED   9545409
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Aswegan,A.L., Josephson,K.D., Mowbray,R., Pauli,R.M., Spritz,R.A.
            and Williams,M.S.
  TITLE     Autosomal dominant hypohidrotic ectodermal dysplasia in a large
            family
  JOURNAL   Am J Med Genet 72 (4), 462-467 (1997)
   PUBMED   9375732
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Wright,J.T., Grange,D.K. and Fete,M.
  TITLE     Hypohidrotic Ectodermal Dysplasia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301291
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092160.5, AF130988.1,
            AC133784.2, AC073415.6 and AI017384.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor family. The encoded transmembrane protein is a receptor
            for the soluble ligand ectodysplasin A, and can activate the
            nuclear factor-kappaB, JNK, and caspase-independent cell death
            pathways. It is required for the development of hair, teeth, and
            other ectodermal derivatives. Mutations in this gene result in
            autosomal dominant and recessive forms of hypohidrotic ectodermal
            dysplasia. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF130988.1, AK313781.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258443.7/ ENSP00000258443.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..448
                     /product="tumor necrosis factor receptor superfamily
                     member EDAR precursor"
                     /note="downless, mouse, homolog of; ectodysplasin 1,
                     anhidrotic receptor; tumor necrosis factor receptor
                     superfamily member EDAR; EDA-A1 receptor; downless
                     homolog; ectodermal dysplasia receptor; anhidrotic
                     ectodysplasin receptor 1; hypohidrotic ectodermal
                     dysplasia; ectodysplasin A1 receptor"
                     /calculated_mol_wt=45814
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2786
     Region          13..148
                     /region_name="TNFRSF_EDAR"
                     /note="Tumor necrosis factor receptor superfamily member
                     ectodysplasin A receptor (EDAR); cd13421"
                     /db_xref="CDD:276926"
     mat_peptide     27..448
                     /product="tumor necrosis factor receptor superfamily
                     member EDAR"
                     /calculated_mol_wt=45814
     Region          30..71
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          31..71
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276926"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          73..113
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          74..113
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276926"
     Region          115..148
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          116..148
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276926"
     Site            188..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          220..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          354..428
                     /region_name="DD"
                     /note="Death Domain Superfamily of protein-protein
                     interaction domains; cl14633"
                     /db_xref="CDD:472698"
     CDS             1..448
                     /gene="EDAR"
                     /gene_synonym="DL; ECTD10A; ECTD10B; ED1R; ED3; ED5;
                     EDA-A1R; EDA1R; EDA3; HRM1"
                     /coded_by="NM_022336.4:280..1626"
                     /db_xref="CCDS:CCDS2081.1"
                     /db_xref="GeneID:10913"
                     /db_xref="HGNC:HGNC:2895"
                     /db_xref="MIM:604095"
ORIGIN      
        1 mahvgdctqt pwlpvlvvsl mcsaraeysn cgeneyynqt tglcqecppc gpgeepylsc
       61 gygtkdedyg cvpcpaekfs kggyqicrrh kdcegffrat vltpgdmend aecgpclpgy
      121 ymlenrprni ygmvcyscll appntkecvg atsgasanfp gtsgsstlsp fqhahkelsg
      181 qghlatalii amstifimai aivliimfyi lktkpsapac ctshpgksve aqvskdeekk
      241 eapdnvvmfs ekdefeklta tpakptksen dasseneqll srsvdsdeep apdkqgspel
      301 cllslvhlar eksatsnksa giqsrrkkil dvyanvcgvv eglsptelpf dclektsrml
      361 sstynsekav vktwrhlaes fglkrdeigg mtdgmqlfdr istagysipe lltklvqier
      421 ldaveslcad ilewagvvpp asqphaas
//
LOCUS       NP_848663                441 aa            linear   PRI 27-APR-2025
DEFINITION  reticulon-4 receptor-like 1 precursor [Homo sapiens].
ACCESSION   NP_848663
VERSION     NP_848663.1
DBSOURCE    REFSEQ: accession NM_178568.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 441)
  AUTHORS   He,J.Y., Han,P., Zhang,Y., Liu,Y.D., Song,S.J., Feng,G.K., An,Y.,
            Zhou,A.J., Wang,H.B., Yuan,L., Lin,Z.R., Xia,T.L., Li,M.Z.,
            Liu,Y.M., Huang,X.M., Zhang,H. and Zhong,Q.
  TITLE     Overexpression of Nogo receptor 3 (NgR3) correlates with poor
            prognosis and contributes to the migration of epithelial cells of
            nasopharyngeal carcinoma patients
  JOURNAL   J Mol Med (Berl) 96 (3-4), 265-279 (2018)
   PUBMED   29327067
  REMARK    GeneRIF: RTN4RL1 plays an important role in promoting the EMT of
            nasopharyngeal carcinoma (NPC) by regulating the phosphorylation of
            Src and FAK, thus activating their downstream pathways and
            eventually altering E-cadherin levels, F-actin polymerization, and
            cell polarity. Additionally, a high level of RTN4RL1 correlates
            with a poor prognosis of NPC.
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Tang,M., Yang,Y.F., Xie,L., Chen,J.L., Zhang,W.Z., Wang,J.,
            Zhao,T.L., Yang,J.F. and Tan,Z.P.
  TITLE     Duplication of 10q22.3-q23.3 encompassing BMPR1A and NGR3
            associated with congenital heart disease, microcephaly, and mild
            intellectual disability
  JOURNAL   Am J Med Genet A 167A (12), 3174-3179 (2015)
   PUBMED   26383923
  REMARK    GeneRIF: Duplication of 10q22.3-q23.3 encompassing NGR3 gene is
            associated with congenital heart disease, microcephaly, and mild
            intellectual disability
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Zhang,L., Kuang,X. and Zhang,J.
  TITLE     Nogo receptor 3, a paralog of Nogo-66 receptor 1 (NgR1), may
            function as a NgR1 co-receptor for Nogo-66
  JOURNAL   J Genet Genomics 38 (11), 515-523 (2011)
   PUBMED   22133682
  REMARK    GeneRIF: Nogo receptor 3, a paralog of NgR1,functions as a NgR1
            co-receptor for Nogo-66.
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Thomas,R., Favell,K., Morante-Redolat,J., Pool,M., Kent,C.,
            Wright,M., Daignault,K., Ferraro,G.B., Montcalm,S., Durocher,Y.,
            Fournier,A., Perez-Tur,J. and Barker,P.A.
  TITLE     LGI1 is a Nogo receptor 1 ligand that antagonizes myelin-based
            growth inhibition
  JOURNAL   J Neurosci 30 (19), 6607-6612 (2010)
   PUBMED   20463223
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Lauren,J., Airaksinen,M.S., Saarma,M. and Timmusk,T.
  TITLE     Two novel mammalian Nogo receptor homologs differentially expressed
            in the central and peripheral nervous systems
  JOURNAL   Mol Cell Neurosci 24 (3), 581-594 (2003)
   PUBMED   14664809
  REMARK    GeneRIF: predominantly expressed in the neurons of the embryonic
            and adult nervous systems
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Barton,W.A., Liu,B.P., Tzvetkova,D., Jeffrey,P.D., Fournier,A.E.,
            Sah,D., Cate,R., Strittmatter,S.M. and Nikolov,D.B.
  TITLE     Structure and axon outgrowth inhibitor binding of the Nogo-66
            receptor and related proteins
  JOURNAL   EMBO J 22 (13), 3291-3302 (2003)
   PUBMED   12839991
REFERENCE   8  (residues 1 to 441)
  AUTHORS   Pignot,V., Hein,A.E., Barske,C., Wiessner,C., Walmsley,A.R.,
            Kaupmann,K., Mayeur,H., Sommer,B., Mir,A.K. and Frentzel,S.
  TITLE     Characterization of two novel proteins, NgRH1 and NgRH2,
            structurally and biochemically homologous to the Nogo-66 receptor
  JOURNAL   J Neurochem 85 (3), 717-728 (2003)
   PUBMED   12694398
REFERENCE   9  (residues 1 to 441)
  AUTHORS   Wang,K.C., Koprivica,V., Kim,J.A., Sivasankaran,R., Guo,Y.,
            Neve,R.L. and He,Z.
  TITLE     Oligodendrocyte-myelin glycoprotein is a Nogo receptor ligand that
            inhibits neurite outgrowth
  JOURNAL   Nature 417 (6892), 941-944 (2002)
   PUBMED   12068310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099684.7 and AC130689.8.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138522.549692.1, AL535679.3
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331238.7/ ENSP00000330631.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..441
                     /product="reticulon-4 receptor-like 1 precursor"
                     /note="Nogo-66 receptor homolog 2; Nogo-66
                     receptor-related protein 3; nogo receptor-like 2"
                     /calculated_mol_wt=46614
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2469
     mat_peptide     25..420
                     /product="Reticulon-4 receptor-like 1. /id=PRO_0000046042"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
                     /calculated_mol_wt=44545
     Region          37..54
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          55..76
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
     Region          <57..>255
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          57..77
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          77..98
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
     Region          78..101
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          101..123
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
     Region          102..126
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          126..147
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
     Region          127..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          150..171
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
     Region          151..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          174..195
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
     Region          175..198
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          198..219
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
     Region          199..222
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          222..243
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
     Region          223..246
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          255..300
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Region          304..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
     Region          397..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UN2.1)"
     CDS             1..441
                     /gene="RTN4RL1"
                     /gene_synonym="NgR3; NGRH2"
                     /coded_by="NM_178568.4:470..1795"
                     /db_xref="CCDS:CCDS45569.1"
                     /db_xref="GeneID:146760"
                     /db_xref="HGNC:HGNC:21329"
                     /db_xref="MIM:610461"
ORIGIN      
        1 mlrkgccvel llllvaaelp lgggcprdcv cypapmtvsc qahnfaaipe gipvdservf
       61 lqnnrigllq pghfspamvt lwiysnnity ihpstfegfv hleeldlgdn rqlrtlapet
      121 fqglvklhal ylykcglsal pagvfgglhs lqylylqdnh ieylqddifv dlvnlshlfl
      181 hgnklwslgp gtfrglvnld rlllhenqlq wvhhkafhdl rrlttlflfn nslselqgec
      241 laplgalefl rlngnpwdcg crarslwewl qrfrgsssav pcvspglrhg qdlkllraed
      301 frnctgpasp hqikshtltt tdraarkehh sphgptrskg hphgprpghr kpgknctnpr
      361 nrnqiskaga gkqapelpdy apdyqhkfsf dimptarpkr kgkcarrtpi rapsgvqqas
      421 sasslgasll awtlglavtl r
//
LOCUS       NP_001127704             274 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 106B [Homo sapiens].
ACCESSION   NP_001127704
VERSION     NP_001127704.1
DBSOURCE    REFSEQ: accession NM_001134232.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Rodney,A., Karanjeet,K., Benzow,K. and Koob,M.D.
  TITLE     A common Alu insertion in the 3'UTR of TMEM106B is associated with
            risk of dementia
  JOURNAL   Alzheimers Dement 20 (7), 5071-5077 (2024)
   PUBMED   38924247
  REMARK    GeneRIF: A common Alu insertion in the 3'UTR of TMEM106B is
            associated with risk of dementia.
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Zhu,M., Zhang,G., Meng,L., Xiao,T., Fang,X. and Zhang,Z.
  TITLE     Physiological and pathological functions of TMEM106B in
            neurodegenerative diseases
  JOURNAL   Cell Mol Life Sci 81 (1), 209 (2024)
   PUBMED   38710967
  REMARK    GeneRIF: Physiological and pathological functions of TMEM106B in
            neurodegenerative diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Picard,C., Miron,J. and Poirier,J.
  TITLE     Association of TMEM106B with Cortical APOE Gene Expression in
            Neurodegenerative Conditions
  JOURNAL   Genes (Basel) 15 (4), 416 (2024)
   PUBMED   38674351
  REMARK    GeneRIF: Association of TMEM106B with Cortical APOE Gene Expression
            in Neurodegenerative Conditions.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Marks,J.D., Ayuso,V.E., Carlomagno,Y., Yue,M., Todd,T.W., Hao,Y.,
            Li,Z., McEachin,Z.T., Shantaraman,A., Duong,D.M., Daughrity,L.M.,
            Jansen-West,K., Shao,W., Calliari,A., Bejarano,J.G., DeTure,M.,
            Rawlinson,B., Casey,M.C., Lilley,M.T., Donahue,M.H., Jawahar,V.M.,
            Boeve,B.F., Petersen,R.C., Knopman,D.S., Oskarsson,B.,
            Graff-Radford,N.R., Wszolek,Z.K., Dickson,D.W., Josephs,K.A.,
            Qi,Y.A., Seyfried,N.T., Ward,M.E., Zhang,Y.J., Prudencio,M.,
            Petrucelli,L. and Cook,C.N.
  TITLE     TMEM106B core deposition associates with TDP-43 pathology and is
            increased in risk SNP carriers for frontotemporal dementia
  JOURNAL   Sci Transl Med 16 (730), eadf9735 (2024)
   PUBMED   38232138
  REMARK    GeneRIF: TMEM106B core deposition associates with TDP-43 pathology
            and is increased in risk SNP carriers for frontotemporal dementia.
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Lee,J.Y., Harney,D.J., Teo,J.D., Kwok,J.B., Sutherland,G.T.,
            Larance,M. and Don,A.S.
  TITLE     The major TMEM106B dementia risk allele affects TMEM106B protein
            levels, fibril formation, and myelin lipid homeostasis in the
            ageing human hippocampus
  JOURNAL   Mol Neurodegener 18 (1), 63 (2023)
   PUBMED   37726834
  REMARK    GeneRIF: The major TMEM106B dementia risk allele affects TMEM106B
            protein levels, fibril formation, and myelin lipid homeostasis in
            the ageing human hippocampus.
            Erratum:[Mol Neurodegener. 2024 Feb 27;19(1):21. doi:
            10.1186/s13024-024-00709-9. PMID: 38409051]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Cruchaga,C., Graff,C., Chiang,H.H., Wang,J., Hinrichs,A.L.,
            Spiegel,N., Bertelsen,S., Mayo,K., Norton,J.B., Morris,J.C. and
            Goate,A.
  TITLE     Association of TMEM106B gene polymorphism with age at onset in
            granulin mutation carriers and plasma granulin protein levels
  JOURNAL   Arch Neurol 68 (5), 581-586 (2011)
   PUBMED   21220649
  REMARK    GeneRIF: Our results suggest that genetic variation in TMEM106B
            (rs1990622) may influence risk for frontotemporal lobar
            degeneration with TAR DNA-binding protein inclusions (FTLD-TDP) by
            modulating secreted levels of GRN.
REFERENCE   7  (residues 1 to 274)
  AUTHORS   van der Zee,J., Van Langenhove,T., Kleinberger,G., Sleegers,K.,
            Engelborghs,S., Vandenberghe,R., Santens,P., Van den Broeck,M.,
            Joris,G., Brys,J., Mattheijssens,M., Peeters,K., Cras,P., De
            Deyn,P.P., Cruts,M. and Van Broeckhoven,C.
  TITLE     TMEM106B is associated with frontotemporal lobar degeneration in a
            clinically diagnosed patient cohort
  JOURNAL   Brain 134 (Pt 3), 808-815 (2011)
   PUBMED   21354975
  REMARK    GeneRIF: This study strongly supported TMEM106B as a risk gene for
            frontotemporal lobar degeneration.
REFERENCE   8  (residues 1 to 274)
  AUTHORS   Vass,R., Ashbridge,E., Geser,F., Hu,W.T., Grossman,M.,
            Clay-Falcone,D., Elman,L., McCluskey,L., Lee,V.M., Van
            Deerlin,V.M., Trojanowski,J.Q. and Chen-Plotkin,A.S.
  TITLE     Risk genotypes at TMEM106B are associated with cognitive impairment
            in amyotrophic lateral sclerosis
  JOURNAL   Acta Neuropathol 121 (3), 373-380 (2011)
   PUBMED   21104415
  REMARK    GeneRIF: FTLD-TDP risk gene TMEM106B is involved in the development
            of cognitive impairment in amyotrophic lateral sclerosis.
REFERENCE   9  (residues 1 to 274)
  AUTHORS   Wood,H.B.
  TITLE     TMEM106B is a susceptibility locus for Ftld
  JOURNAL   Nat Rev Neurol 6 (4), 184 (2010)
   PUBMED   20383883
  REMARK    GeneRIF: The genome-wide association study revealed a strong
            association between FTLD-TDP and several single nucleotide
            polymorphisms (SNPs) that mapped in the region of the TMEM106B gene
REFERENCE   10 (residues 1 to 274)
  AUTHORS   Van Deerlin,V.M., Sleiman,P.M., Martinez-Lage,M., Chen-Plotkin,A.,
            Wang,L.S., Graff-Radford,N.R., Dickson,D.W., Rademakers,R.,
            Boeve,B.F., Grossman,M., Arnold,S.E., Mann,D.M.,
            Pickering-Brown,S.M., Seelaar,H., Heutink,P., van Swieten,J.C.,
            Murrell,J.R., Ghetti,B., Spina,S., Grafman,J., Hodges,J.,
            Spillantini,M.G., Gilman,S., Lieberman,A.P., Kaye,J.A.,
            Woltjer,R.L., Bigio,E.H., Mesulam,M., Al-Sarraj,S., Troakes,C.,
            Rosenberg,R.N., White,C.L. 3rd, Ferrer,I., Llado,A., Neumann,M.,
            Kretzschmar,H.A., Hulette,C.M., Welsh-Bohmer,K.A., Miller,B.L.,
            Alzualde,A., Lopez de Munain,A., McKee,A.C., Gearing,M.,
            Levey,A.I., Lah,J.J., Hardy,J., Rohrer,J.D., Lashley,T.,
            Mackenzie,I.R., Feldman,H.H., Hamilton,R.L., Dekosky,S.T., van der
            Zee,J., Kumar-Singh,S., Van Broeckhoven,C., Mayeux,R.,
            Vonsattel,J.P., Troncoso,J.C., Kril,J.J., Kwok,J.B., Halliday,G.M.,
            Bird,T.D., Ince,P.G., Shaw,P.J., Cairns,N.J., Morris,J.C.,
            McLean,C.A., DeCarli,C., Ellis,W.G., Freeman,S.H., Frosch,M.P.,
            Growdon,J.H., Perl,D.P., Sano,M., Bennett,D.A., Schneider,J.A.,
            Beach,T.G., Reiman,E.M., Woodruff,B.K., Cummings,J., Vinters,H.V.,
            Miller,C.A., Chui,H.C., Alafuzoff,I., Hartikainen,P., Seilhean,D.,
            Galasko,D., Masliah,E., Cotman,C.W., Tunon,M.T., Martinez,M.C.,
            Munoz,D.G., Carroll,S.L., Marson,D., Riederer,P.F., Bogdanovic,N.,
            Schellenberg,G.D., Hakonarson,H., Trojanowski,J.Q. and Lee,V.M.
  TITLE     Common variants at 7p21 are associated with frontotemporal lobar
            degeneration with TDP-43 inclusions
  JOURNAL   Nat Genet 42 (3), 234-239 (2010)
   PUBMED   20154673
  REMARK    GeneRIF: Variants in TMEM106B are strong risk factors for
            frontotemporal lobar degeneration with TDP-43 inculsions.
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA452299.1, BC033901.2 and AC007321.2.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.25783.1,
                                           SRR1803616.277442.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396668.8/ ENSP00000379902.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.3"
     Protein         1..274
                     /product="transmembrane protein 106B"
                     /calculated_mol_wt=30996
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUM4.2)"
     Region          27..258
                     /region_name="DUF1356"
                     /note="Protein of unknown function (DUF1356); pfam07092"
                     /db_xref="CDD:462088"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NUM4.2)"
     Site            97..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUM4.2)"
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22511793; propagated from
                     UniProtKB/Swiss-Prot (Q9NUM4.2)"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22511793; propagated from
                     UniProtKB/Swiss-Prot (Q9NUM4.2)"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22511793; propagated from
                     UniProtKB/Swiss-Prot (Q9NUM4.2)"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:22511793, ECO:0000269|PubMed:23742080;
                     propagated from UniProtKB/Swiss-Prot (Q9NUM4.2)"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22511793; propagated from
                     UniProtKB/Swiss-Prot (Q9NUM4.2)"
     CDS             1..274
                     /gene="TMEM106B"
                     /gene_synonym="HLD16"
                     /coded_by="NM_001134232.2:135..959"
                     /db_xref="CCDS:CCDS5358.1"
                     /db_xref="GeneID:54664"
                     /db_xref="HGNC:HGNC:22407"
                     /db_xref="MIM:613413"
ORIGIN      
        1 mgkslshlpl hsskedaydg vtsenmrngl vnsevhnedg rngdvsqfpy veftgrdsvt
       61 cptcqgtgri prgqenqlva lipysdqrlr prrtklyvma svfvclllsg lavfflfprs
      121 idvkyigvks ayvsydvqkr tiylnitntl nitnnnyysv evenitaqvq fsktvigkar
      181 lnnitiigpl dmkqidytvp tviaeemsym ydfctlisik vhnivlmmqv tvtttyfghs
      241 eqisqeryqy vdcgrnttyq lgqseylnvl qpqq
//
LOCUS       NP_001265553             911 aa            linear   PRI 27-APR-2025
DEFINITION  NF-X1-type zinc finger protein NFXL1 [Homo sapiens].
ACCESSION   NP_001265553
VERSION     NP_001265553.1
DBSOURCE    REFSEQ: accession NM_001278624.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Villanueva,P., Nudel,R., Hoischen,A., Fernandez,M.A., Simpson,N.H.,
            Gilissen,C., Reader,R.H., Jara,L., Echeverry,M.M., Francks,C.,
            Baird,G., Conti-Ramsden,G., O'Hare,A., Bolton,P.F., Hennessy,E.R.,
            Palomino,H., Carvajal-Carmona,L., Veltman,J.A., Cazier,J.B., De
            Barbieri,Z., Fisher,S.E. and Newbury,D.F.
  CONSRTM   SLI Consortium
  TITLE     Exome sequencing in an admixed isolated population indicates NFXL1
            variants confer a risk for specific language impairment
  JOURNAL   PLoS Genet 11 (3), e1004925 (2015)
   PUBMED   25781923
  REMARK    GeneRIF: We conclude that coding variants within NFXL1 confer an
            increased risk of Specific Language Impairment within a complex
            genetic model
            Erratum:[PLoS Genet. 2015 Jun 26;11(6):e1005336. doi:
            10.1371/journal.pgen.1005336. Echeverry, Maria Magdalena [corrected
            to Echeverry, Maria Magdalena]. PMID: 26114769]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Mussig,C., Schroder,F., Usadel,B. and Lisso,J.
  TITLE     Structure and putative function of NFX1-like proteins in plants
  JOURNAL   Plant Biol (Stuttg) 12 (3), 381-394 (2010)
   PUBMED   20522174
  REMARK    Review article
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Tang,W., Yuan,J., Chen,X., Shan,Y., Luo,K., Guo,Z., Zhang,Y.,
            Wan,B. and Yu,L.
  TITLE     Cloning and characterization of the CDZFP gene which encodes a
            putative zinc finger protein
  JOURNAL   DNA Seq 16 (5), 391-396 (2005)
   PUBMED   16323267
  REMARK    Erratum:[DNA Seq. 2006 Apr;17(2):174]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC107068.3, DA801937.1 and AB181916.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB181916.1, SRR1660807.62305.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000507489.2/ ENSP00000422037.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p12"
     Protein         1..911
                     /product="NF-X1-type zinc finger protein NFXL1"
                     /note="ovarian zinc finger protein; up-regulated in colon
                     cancer 5; cytoplasm-distribution zinc finger protein"
                     /calculated_mol_wt=101209
     Region          1..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZNB6.2)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6ZNB6.2)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6ZNB6.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6ZNB6.2)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6ZNB6.2)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6ZNB6.2)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6ZNB6.2)"
     Region          158..220
                     /region_name="RING-CH-C4HC3_NFXL1"
                     /note="RING-CH finger, H2 subclass (C4HC3-type), found in
                     nuclear transcription factor, X-box binding-like 1 (NFXL1)
                     and similar proteins; cd16697"
                     /db_xref="CDD:438358"
     Region          308..356
                     /region_name="NF-X1-zinc-finger"
                     /note="Presumably a zinc binding domain, which has been
                     shown to bind to DNA in the human nuclear transcriptional
                     repressor NF-X1. The zinc finger can be characterized by
                     the pattern
                     C-X(1-6)-H-X-C-X3-C(H/C)-X(3-4)-(H/C)-X(1-10)-C. The NF-X1
                     zinc finger...; cd06008"
                     /db_xref="CDD:100116"
     Region          361..409
                     /region_name="NF-X1-zinc-finger"
                     /note="Presumably a zinc binding domain, which has been
                     shown to bind to DNA in the human nuclear transcriptional
                     repressor NF-X1. The zinc finger can be characterized by
                     the pattern
                     C-X(1-6)-H-X-C-X3-C(H/C)-X(3-4)-(H/C)-X(1-10)-C. The NF-X1
                     zinc finger...; cd06008"
                     /db_xref="CDD:100116"
     Region          414..462
                     /region_name="NF-X1-zinc-finger"
                     /note="Presumably a zinc binding domain, which has been
                     shown to bind to DNA in the human nuclear transcriptional
                     repressor NF-X1. The zinc finger can be characterized by
                     the pattern
                     C-X(1-6)-H-X-C-X3-C(H/C)-X(3-4)-(H/C)-X(1-10)-C. The NF-X1
                     zinc finger...; cd06008"
                     /db_xref="CDD:100116"
     Region          493..541
                     /region_name="NF-X1-zinc-finger"
                     /note="Presumably a zinc binding domain, which has been
                     shown to bind to DNA in the human nuclear transcriptional
                     repressor NF-X1. The zinc finger can be characterized by
                     the pattern
                     C-X(1-6)-H-X-C-X3-C(H/C)-X(3-4)-(H/C)-X(1-10)-C. The NF-X1
                     zinc finger...; cd06008"
                     /db_xref="CDD:100116"
     Region          701..748
                     /region_name="NF-X1-zinc-finger"
                     /note="Presumably a zinc binding domain, which has been
                     shown to bind to DNA in the human nuclear transcriptional
                     repressor NF-X1. The zinc finger can be characterized by
                     the pattern
                     C-X(1-6)-H-X-C-X3-C(H/C)-X(3-4)-(H/C)-X(1-10)-C. The NF-X1
                     zinc finger...; cd06008"
                     /db_xref="CDD:100116"
     Region          765..811
                     /region_name="NF-X1-zinc-finger"
                     /note="Presumably a zinc binding domain, which has been
                     shown to bind to DNA in the human nuclear transcriptional
                     repressor NF-X1. The zinc finger can be characterized by
                     the pattern
                     C-X(1-6)-H-X-C-X3-C(H/C)-X(3-4)-(H/C)-X(1-10)-C. The NF-X1
                     zinc finger...; cd06008"
                     /db_xref="CDD:100116"
     Site            889..906
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZNB6.2)"
     CDS             1..911
                     /gene="NFXL1"
                     /gene_synonym="CDZFP; HOZFP; OZFP; URCC5"
                     /coded_by="NM_001278624.2:222..2957"
                     /db_xref="CCDS:CCDS3478.2"
                     /db_xref="GeneID:152518"
                     /db_xref="HGNC:HGNC:18726"
                     /db_xref="MIM:620488"
ORIGIN      
        1 measwrqvag grgrsrgrat aapsgngvhl rgagggrekg svgavpsgts pggvattaaa
       61 gsrhspagsq alqttaasel msqkkfeeik kanqaaarkl veeqfsssse egdedfegkq
      121 gkilantfit yttqtdgdtr elertkqyvn eafqagamtc liciasvkrn qavwscsgcf
      181 cifhmpciqk wakdsqflvs svtdddfgkk dcpwpcpkcr feykrsetps ryycycgkve
      241 dppldpwlvp hscgqvcere fkppcghkcl llchpgpcpp cpkmvtttcy ckkakpiprr
      301 csakewscql pcgqkllcgq hkcenpchag scqpcprvsr qkcvcgkkva erscasplwh
      361 cdqvcgktlp cgnhtceqvc hvgacgecpr sgkrfcpcqk skfslpcted vptcgdscdk
      421 vlecgihrcs qrchrgpcet crqevekhcr cgkhtkrmpc hkpylcetkc vkmrdcqkhq
      481 crrkccpgnc ppcdqncgrt lgcrnhkcps vchrgscypc petvdvkcnc gntkvtvpcg
      541 rerttrppkc keqcsrpptc hhtsqekhrc hfgscppchq pcqkvlekcg hlcpapchdq
      601 alikqtgrhq ptgpweqpse pafiqtalpc ppcqvpipme clgkhevspl pchavgpysc
      661 krvcgrildc qnhtcmkech kvtktdgctg knkagpeclh ceegcsksrp lgclhpcilr
      721 chpgecppcv qmlrikchck itslyvecrk ittadvnekn llsccknqcp kelpcghrck
      781 emchpgecpf ncnqkvklrc pckrikkelq cnkvrenqvs iecdttckem krkaseikea
      841 eakaaleeek rrqqaeleaf enrlkgrrkk nrkrdevave lslwqkhkyy lisvcgvvvv
      901 vfawyithdv n
//
LOCUS       NP_689878                179 aa            linear   PRI 27-APR-2025
DEFINITION  dynein light chain Tctex-type 5 [Homo sapiens].
ACCESSION   NP_689878
VERSION     NP_689878.2
DBSOURCE    REFSEQ: accession NM_152665.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Spitali,P., Zaharieva,I., Bohringer,S., Hiller,M., Chaouch,A.,
            Roos,A., Scotton,C., Claustres,M., Bello,L., McDonald,C.M.,
            Hoffman,E.P., Koeks,Z., Eka Suchiman,H., Cirak,S., Scoto,M.,
            Reza,M., 't Hoen,P.A.C., Niks,E.H., Tuffery-Giraud,S.,
            Lochmuller,H., Ferlini,A., Muntoni,F. and Aartsma-Rus,A.
  CONSRTM   CINRG Investigators
  TITLE     TCTEX1D1 is a genetic modifier of disease progression in Duchenne
            muscular dystrophy
  JOURNAL   Eur J Hum Genet 28 (6), 815-825 (2020)
   PUBMED   31896777
  REMARK    GeneRIF: TCTEX1D1 is a genetic modifier of disease progression in
            Duchenne muscular dystrophy.
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Cho,K.J., Noh,S.H., Han,S.M., Choi,W.I., Kim,H.Y., Yu,S., Lee,J.S.,
            Rim,J.H., Lee,M.G., Hildebrandt,F. and Gee,H.Y.
  TITLE     ZMYND10 stabilizes intermediate chain proteins in the cytoplasmic
            pre-assembly of dynein arms
  JOURNAL   PLoS Genet 14 (3), e1007316 (2018)
   PUBMED   29601588
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK098192.1, AL354978.20 and AI016360.1.
            
            On Jun 10, 2009 this sequence version replaced NP_689878.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.103940.1,
                                           SRR1803616.15586.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282670.7/ ENSP00000282670.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..179
                     /product="dynein light chain Tctex-type 5"
                     /note="tctex1 domain-containing protein 1; Tctex1 domain
                     containing 1"
                     /calculated_mol_wt=20599
     Region          76..179
                     /region_name="DLC-like_TCTEX1D1"
                     /note="dynein light chain (DLC)-like domain found in
                     Tctex1 domain-containing protein 1 (TCTEX1D1) and similar
                     proteins; cd21458"
                     /db_xref="CDD:412006"
     CDS             1..179
                     /gene="DYNLT5"
                     /gene_synonym="TCTEX1D1"
                     /coded_by="NM_152665.3:130..669"
                     /db_xref="CCDS:CCDS633.1"
                     /db_xref="GeneID:200132"
                     /db_xref="HGNC:HGNC:26882"
                     /db_xref="MIM:619994"
ORIGIN      
        1 mmmsdnakgr aahswkkrgs isslsnhefw rkeihgrikd smstvsymee psqrddisrl
       61 tvqmentyql gppkhfpvvt vnhilkdvvt sylqveeyep elcrqmtkti sevikaqvkd
      121 lmiprykliv ivhigqlnrq siligsrclw dpksdtfssy vfrnsslfal anvyavyle
//
LOCUS       NP_001076954             511 aa            linear   MAM 27-APR-2025
DEFINITION  zinc finger protein AEBP2 [Bos taurus].
ACCESSION   NP_001076954 XP_617975
VERSION     NP_001076954.2
DBSOURCE    REFSEQ: accession NM_001083485.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000005.1.
            
            On Oct 17, 2009 this sequence version replaced NP_001076954.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC123767.1, GGVE01061665.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA6648753,
                                           SAMEA6648754 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="5"
                     /map="5"
                     /breed="Hereford"
     Protein         1..511
                     /product="zinc finger protein AEBP2"
                     /note="adipocyte enhancer-binding protein 2"
                     /calculated_mol_wt=53918
     Region          1..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4FV57.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN18; propagated from
                     UniProtKB/Swiss-Prot (A4FV57.2)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN18; propagated from
                     UniProtKB/Swiss-Prot (A4FV57.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN18; propagated from
                     UniProtKB/Swiss-Prot (A4FV57.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN18; propagated from
                     UniProtKB/Swiss-Prot (A4FV57.2)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN18; propagated from
                     UniProtKB/Swiss-Prot (A4FV57.2)"
     Region          203..288
                     /region_name="Interaction with RBBP4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A4FV57.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN18; propagated from
                     UniProtKB/Swiss-Prot (A4FV57.2)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN18; propagated from
                     UniProtKB/Swiss-Prot (A4FV57.2)"
     Region          <209..358
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          260..280
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(264,266,268,270..271,274..275,279,297,299,303..304,
                     311..312,315,331,333,335,337..338,341..342,345)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          291..316
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          324..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          346..388
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4FV57.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN18; propagated from
                     UniProtKB/Swiss-Prot (A4FV57.2)"
     Region          401..472
                     /region_name="Interaction with SUZ12.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN18"
                     /note="propagated from UniProtKB/Swiss-Prot (A4FV57.2)"
     Region          489..511
                     /region_name="Important for nucleosome binding activity of
                     the PRC2 complex. /evidence=ECO:0000250|UniProtKB:Q6ZN18"
                     /note="propagated from UniProtKB/Swiss-Prot (A4FV57.2)"
     CDS             1..511
                     /gene="AEBP2"
                     /coded_by="NM_001083485.3:1..1536"
                     /db_xref="BGD:BT18865"
                     /db_xref="GeneID:537791"
                     /db_xref="VGNC:VGNC:25704"
ORIGIN      
        1 maaaltdmad leelsrlspl ppgspgpaar graeppeeee eedeeeeaea eavaalllng
       61 ggggggvggg eaetmsepsp esasqagedd deeedddeee edesssggge eessaeslvg
      121 sssggsssde trslspgaas sssgdgdgke gleepkgprg sqggggggss sssvvssggd
      181 egygtggggs satsggrrgs lemssdgepl srmdsedsis stimdvdsti ssgrstpamm
      241 ngqgsttsss kniaynccwd qcqacftssp dladhirsih vdgqrggvfv clwkgckvyn
      301 tpstsqswlq rhmlthsgdk pfkcvvggcn asfasqggla rhvpthfsqq nsskvssqpk
      361 akeespskag mnkrrklknk rrrslprphd ffdaqtldai rhraicfnls ahieslgkgh
      421 svvfhstvia krkedsgkik lllhwmpedi lpdvwvnese rhqlktkvvh lsklpkdtal
      481 lldpniyrtm pqkrlkrtli rkvfnlylsk q
//
LOCUS       NP_001007564             278 aa            linear   PRI 27-APR-2025
DEFINITION  insulin-like growth factor-binding protein-like 1 precursor [Homo
            sapiens].
ACCESSION   NP_001007564 XP_294567
VERSION     NP_001007564.1
DBSOURCE    REFSEQ: accession NM_001007563.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Hou,L., Feng,X., Zhu,Z., Mi,Y., He,Q., Yin,K. and Zhao,G.
  TITLE     IGFBPL1 inhibits macrophage lipid accumulation by enhancing the
            activation of IGR1R/LXRalpha/ABCG1 pathway
  JOURNAL   Aging (Albany NY) 15 (24), 14791-14802 (2023)
   PUBMED   38157252
  REMARK    GeneRIF: IGFBPL1 inhibits macrophage lipid accumulation by
            enhancing the activation of IGR1R/LXRalpha/ABCG1 pathway.
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Pan,L., Cho,K.S., Wei,X., Xu,F., Lennikov,A., Hu,G., Tang,J.,
            Guo,S., Chen,J., Kriukov,E., Kyle,R., Elzaridi,F., Jiang,S.,
            Dromel,P.A., Young,M., Baranov,P., Do,C.W., Williams,R.W., Chen,J.,
            Lu,L. and Chen,D.F.
  TITLE     IGFBPL1 is a master driver of microglia homeostasis and resolution
            of neuroinflammation in glaucoma and brain tauopathy
  JOURNAL   Cell Rep 42 (8), 112889 (2023)
   PUBMED   37527036
  REMARK    GeneRIF: IGFBPL1 is a master driver of microglia homeostasis and
            resolution of neuroinflammation in glaucoma and brain tauopathy.
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Butti,E., Cattaneo,S., Bacigaluppi,M., Cambiaghi,M., Scotti,G.M.,
            Brambilla,E., Ruffini,F., Sferruzza,G., Ripamonti,M., Simeoni,F.,
            Cacciaguerra,L., Zanghi,A., Quattrini,A., Fesce,R.,
            Panina-Bordignon,P., Giannese,F., Cittaro,D., Kuhlmann,T.,
            D'Adamo,P., Rocca,M.A., Taverna,S. and Martino,G.
  TITLE     Neural precursor cells tune striatal connectivity through the
            release of IGFBPL1
  JOURNAL   Nat Commun 13 (1), 7579 (2022)
   PUBMED   36482070
  REMARK    GeneRIF: Neural precursor cells tune striatal connectivity through
            the release of IGFBPL1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Liu,Y., Zhang,M., He,T., Yang,W., Wang,L., Zhang,L. and Guo,M.
  TITLE     Epigenetic silencing of IGFBPL1 promotes esophageal cancer growth
            by activating PI3K-AKT signaling
  JOURNAL   Clin Epigenetics 12 (1), 22 (2020)
   PUBMED   32041673
  REMARK    GeneRIF: Epigenetic silencing of IGFBPL1 promotes esophageal cancer
            growth by activating PI3K-AKT signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Guo,C., Cho,K.S., Li,Y., Tchedre,K., Antolik,C., Ma,J., Chew,J.,
            Utheim,T.P., Huang,X.A., Yu,H., Malik,M.T.A., Anzak,N. and
            Chen,D.F.
  TITLE     IGFBPL1 Regulates Axon Growth through IGF-1-mediated Signaling
            Cascades
  JOURNAL   Sci Rep 8 (1), 2054 (2018)
   PUBMED   29391597
  REMARK    GeneRIF: Expression of IGFBPL1 correlates with RGC axon growth, and
            acute knockdown of IGFBPL1 with shRNA or IGFBPL1 knockout in vivo
            impaired RGC axon growth.  IGFBPL1 binds IGF-1, induces calcium
            signaling mTOR phosphorylation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Kutsukake,M., Ishihara,R., Yoshie,M., Kogo,H. and Tamura,K.
  TITLE     Involvement of insulin-like growth factor-binding protein-related
            protein 1 in decidualization of human endometrial stromal cells
  JOURNAL   Mol Hum Reprod 13 (10), 737-743 (2007)
   PUBMED   17884839
  REMARK    GeneRIF: These results suggest that insulin-like growth
            factor-binding protein-related protein 1 may play a role in
            decidualization of human endometrial stromal cells.
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Smith,P., Nicholson,L.J., Syed,N., Payne,A., Hiller,L., Garrone,O.,
            Occelli,M., Gasco,M. and Crook,T.
  TITLE     Epigenetic inactivation implies independent functions for
            insulin-like growth factor binding protein (IGFBP)-related protein
            1 and the related IGFBPL1 in inhibiting breast cancer phenotypes
  JOURNAL   Clin Cancer Res 13 (14), 4061-4068 (2007)
   PUBMED   17634530
  REMARK    GeneRIF: Expression of IGFBPL1 is regulated by aberrant
            hypermethylation in breast cancer, implying that inactivation of
            these genes is involved in the pathogenesis of this malignancy.
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Cai,Z., Chen,H.T., Boyle,B., Rupp,F., Funk,W.D. and Dedera,D.A.
  TITLE     Identification of a novel insulin-like growth factor binding
            protein gene homologue with tumor suppressor like properties
  JOURNAL   Biochem Biophys Res Commun 331 (1), 261-266 (2005)
   PUBMED   15845387
  REMARK    GeneRIF: IGFBP-RP4 may be a novel putative tumor suppressor
            protein.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL135785.10.
            
            On Nov 29, 2004 this sequence version replaced XP_294567.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.261087.1,
                                           SRR1660803.135280.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377694.2/ ENSP00000366923.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.1"
     Protein         1..278
                     /product="insulin-like growth factor-binding protein-like
                     1 precursor"
                     /note="insulin-like growth factor binding protein related
                     protein 4; IGFBP-related protein 10; insulin-like growth
                     factor-binding-related protein 4"
                     /calculated_mol_wt=26290
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WX77.1)"
                     /calculated_mol_wt=2734
     mat_peptide     26..278
                     /product="Insulin-like growth factor-binding protein-like
                     1. /id=PRO_0000297687"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WX77.1)"
                     /calculated_mol_wt=26290
     Region          <114..151
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WX77.1)"
     Region          169..260
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          185..189
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          226..230
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          240..245
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          254..257
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..278
                     /gene="IGFBPL1"
                     /gene_synonym="bA113O24.1; IGFBP-RP4; IGFBPRP4"
                     /coded_by="NM_001007563.3:31..867"
                     /db_xref="CCDS:CCDS35017.1"
                     /db_xref="GeneID:347252"
                     /db_xref="HGNC:HGNC:20081"
                     /db_xref="MIM:610413"
ORIGIN      
        1 mprlslllpl llllllpllp plspslgird vggrrpkcgp crpegcpapa pcpapgisal
       61 decgccarcl gaegascggr aggrcgpglv casqaagaap egtglcvcaq rgtvcgsdgr
      121 sypsvcalrl rarhtprahp ghlhkardgp cefapvvvvp prsvhnvtga qvglscevra
      181 vptpvitwrk vtkspegtqa leelpgdhvn iavqvrggps dheatawili nplrkedegv
      241 yqchaanmvg eaeshstvtv ldlskyrsfh fpapddrm
//
LOCUS       NP_705613                667 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-17 receptor E isoform 1 precursor [Homo sapiens].
ACCESSION   NP_705613
VERSION     NP_705613.1
DBSOURCE    REFSEQ: accession NM_153480.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Wang,J., Wang,X., Wang,M., Wang,J., Wu,Y. and Qi,X.
  TITLE     Clinical significance of Interleukin 17 receptor E in diabetic
            nephropathy
  JOURNAL   Int Immunopharmacol 120, 110324 (2023)
   PUBMED   37235960
  REMARK    GeneRIF: Clinical significance of Interleukin 17 receptor E in
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Jiang,Y., Wang,L., Peng,Y., Qin,J., Tan,A. and Wang,S.
  TITLE     Interleukin 17 receptor E identifies heterogeneous T helper 17
            cells in peritoneal fluid of moderate and severe endometriosis
            patients
  JOURNAL   Clin Exp Immunol 207 (3), 360-369 (2022)
   PUBMED   35553626
  REMARK    GeneRIF: Interleukin 17 receptor E identifies heterogeneous T
            helper 17 cells in peritoneal fluid of moderate and severe
            endometriosis patients.
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Barati,M., Sinaeian,M., Shokrollahi Barough,M., Pak,F., Semnani,V.,
            Kokhaei,P. and Momtazi-Borojeni,A.A.
  TITLE     Evaluation of Interleukin 25 and Interleukin 25 Receptor Expression
            in Peripheral Blood Mononuclear Cells of Breast Cancer Patients and
            Normal Subjects
  JOURNAL   J Interferon Cytokine Res 40 (3), 139-144 (2020)
   PUBMED   31905037
  REMARK    GeneRIF: Evaluation of Interleukin 25 and Interleukin 25 Receptor
            Expression in Peripheral Blood Mononuclear Cells of Breast Cancer
            Patients and Normal Subjects.
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Nies,J.F. and Panzer,U.
  TITLE     IL-17C/IL-17RE: Emergence of a Unique Axis in TH17 Biology
  JOURNAL   Front Immunol 11, 341 (2020)
   PUBMED   32174926
  REMARK    GeneRIF: IL-17C/IL-17RE: Emergence of a Unique Axis in TH17
            Biology.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Tang,W., Smith,S.G., Salter,B., Oliveria,J.P., Mitchell,P.,
            Nusca,G.M., Howie,K., Gauvreau,G.M., O'Byrne,P.M. and Sehmi,R.
  TITLE     Allergen-Induced Increases in Interleukin-25 and Interleukin-25
            Receptor Expression in Mature Eosinophils from Atopic Asthmatics
  JOURNAL   Int Arch Allergy Immunol 170 (4), 234-242 (2016)
   PUBMED   27685606
  REMARK    GeneRIF: Our findings suggest that the IL-25/IL-25R axis may play
            an important role in promoting the recruitment and proinflammatory
            function of eosinophils in allergic asthma.
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Wu,B., Jin,M., Zhang,Y., Wei,T. and Bai,Z.
  TITLE     Evolution of the IL17 receptor family in chordates: a new subfamily
            IL17REL
  JOURNAL   Immunogenetics 63 (12), 835-845 (2011)
   PUBMED   21732179
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Chang,S.H., Reynolds,J.M., Pappu,B.P., Chen,G., Martinez,G.J. and
            Dong,C.
  TITLE     Interleukin-17C promotes Th17 cell responses and autoimmune disease
            via interleukin-17 receptor E
  JOURNAL   Immunity 35 (4), 611-621 (2011)
   PUBMED   21982598
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Song,X., Zhu,S., Shi,P., Liu,Y., Shi,Y., Levin,S.D. and Qian,Y.
  TITLE     IL-17RE is the functional receptor for IL-17C and mediates mucosal
            immunity to infection with intestinal pathogens
  JOURNAL   Nat Immunol 12 (12), 1151-1158 (2011)
   PUBMED   21993849
  REMARK    GeneRIF: IL-17RE as a receptor of IL-17C that regulates early
            innate immunity to intestinal pathogens.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 667)
  AUTHORS   Ramirez-Carrozzi,V., Sambandam,A., Luis,E., Lin,Z., Jeet,S.,
            Lesch,J., Hackney,J., Kim,J., Zhou,M., Lai,J., Modrusan,Z., Sai,T.,
            Lee,W., Xu,M., Caplazi,P., Diehl,L., de Voss,J., Balazs,M.,
            Gonzalez,L. Jr., Singh,H., Ouyang,W. and Pappu,R.
  TITLE     IL-17C regulates the innate immune function of epithelial cells in
            an autocrine manner
  JOURNAL   Nat Immunol 12 (12), 1159-1166 (2011)
   PUBMED   21993848
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 667)
  AUTHORS   Li,T.S., Li,X.N., Chang,Z.J., Fu,X.Y. and Liu,L.
  TITLE     Identification and functional characterization of a novel
            interleukin 17 receptor: a possible mitogenic activation through
            ras/mitogen-activated protein kinase signaling pathway
  JOURNAL   Cell Signal 18 (8), 1287-1298 (2006)
   PUBMED   16310341
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF458069.1, BC137077.1 and
            AK074238.1.
            
            Summary: This gene encodes a transmembrane protein that functions
            as the receptor for interleukin-17C. The encoded protein signals to
            downstream components of the mitogen activated protein kinase
            (MAPK) pathway. Activity of this protein is important in the immune
            response to bacterial pathogens. Alternatively spliced transcript
            variants have been described for this gene. [provided by RefSeq,
            Sep 2013].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF458069.1, AY358451.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000383814.8/ ENSP00000373325.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..667
                     /product="interleukin-17 receptor E isoform 1 precursor"
                     /note="IL-17 receptor E"
                     /calculated_mol_wt=72417
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2411
     mat_peptide     24..667
                     /product="Interleukin-17 receptor E. /id=PRO_0000309467"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFR9.1)"
                     /calculated_mol_wt=72417
     Region          79..448
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Region          126..174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFR9.1)"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFR9.1)"
     Site            347
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFR9.1)"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFR9.1)"
     Site            455..475
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFR9.1)"
     Region          488..611
                     /region_name="SEFIR"
                     /note="SEFIR domain; cl23749"
                     /db_xref="CDD:474043"
     CDS             1..667
                     /gene="IL17RE"
                     /coded_by="NM_153480.2:86..2089"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2589.1"
                     /db_xref="GeneID:132014"
                     /db_xref="HGNC:HGNC:18439"
                     /db_xref="MIM:614995"
ORIGIN      
        1 mgssrlaall lplllividl sdsagigfrh lphwntrcpl ashtddsftg ssayipcrtw
       61 walfstkpwc vrvwhcsrcl cqhllsggsg lqrglfhllv qkskksstfk fyrrhkmpap
      121 aqrkllprrh lsekshhisi pspdishkgl rskrtqpsdp etweslprld sqrhggpefs
      181 fdllpearai rvtissgpev svrlchqwal eceelsspyd vqkivsgght velpyefllp
      241 clcieasylq edtvrrkkcp fqswpeaygs dfwksvhftd ysqhtqmvma ltlrcplkle
      301 aalcqrhdwh tlckdlpnat aresdgwyvl ekvdlhpqlc fkfsfgnssh vecphqtgsl
      361 tswnvsmdtq aqqlilhfss rmhatfsaaw slpglgqdtl vppvytvsqa rgsspvsldl
      421 iipflrpgcc vlvwrsdvqf awkhllcpdv syrhlgllil allalltllg vvlaltcrrp
      481 qsgpgparpv lllhaadsea qrrlvgalae llraalgggr dvivdlwegr hvarvgplpw
      541 lwaartrvar eqgtvlllws gadlrpvsgp dpraapllal lhaaprplll layfsrlcak
      601 gdippplral pryrllrdlp rllraldarp faeatswgrl garqrrqsrl elcsrlerea
      661 arladlg
//
LOCUS       NP_060269                707 aa            linear   PRI 27-APR-2025
DEFINITION  protein O-mannosyl-transferase TMEM260 precursor [Homo sapiens].
ACCESSION   NP_060269
VERSION     NP_060269.3
DBSOURCE    REFSEQ: accession NM_017799.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Inoue,T., Takase,R., Uchida,K., Kodo,K., Suda,K., Watanabe,Y.,
            Yoshiura,K.I., Kunimatsu,M., Ishizaki,R., Azuma,K., Inai,K.,
            Muneuchi,J., Furutani,Y., Akagawa,H. and Yamagishi,H.
  TITLE     The c.1617del variant of TMEM260 is identified as the most frequent
            single gene determinant for Japanese patients with a specific type
            of congenital heart disease
  JOURNAL   J Hum Genet 69 (5), 215-222 (2024)
   PUBMED   38409496
  REMARK    GeneRIF: The c.1617del variant of TMEM260 is identified as the most
            frequent single gene determinant for Japanese patients with a
            specific type of congenital heart disease.
            Erratum:[J Hum Genet. 2024 May;69(5):223. doi:
            10.1038/s10038-024-01238-5. PMID: 38459226]
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Yaoita,H., Kawai,E., Takayama,J., Iwasawa,S., Saijo,N., Abiko,M.,
            Suzuki,K., Kimura,M., Ozawa,A., Tamiya,G., Kure,S. and Kikuchi,A.
  TITLE     Genetic etiology of truncus arteriosus excluding 22q11.2 deletion
            syndrome and identification of c.1617del, a prevalent variant in
            TMEM260, in the Japanese population
  JOURNAL   J Hum Genet 69 (5), 177-183 (2024)
   PUBMED   38351237
  REMARK    GeneRIF: Genetic etiology of truncus arteriosus excluding 22q11.2
            deletion syndrome and identification of c.1617del, a prevalent
            variant in TMEM260, in the Japanese population.
            Erratum:[J Hum Genet. 2024 May;69(5):185. doi:
            10.1038/s10038-024-01245-6. PMID: 38548934]
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Larsen,I.S.B., Povolo,L., Zhou,L., Tian,W., Mygind,K.J., Hintze,J.,
            Jiang,C., Hartill,V., Prescott,K., Johnson,C.A., Mullegama,S.V.,
            McConkie-Rosell,A., McDonald,M., Hansen,L., Vakhrushev,S.Y.,
            Schjoldager,K.T., Clausen,H., Worzfeld,T., Joshi,H.J. and Halim,A.
  TITLE     The SHDRA syndrome-associated gene TMEM260 encodes a
            protein-specific O-mannosyltransferase
  JOURNAL   Proc Natl Acad Sci U S A 120 (21), e2302584120 (2023)
   PUBMED   37186866
  REMARK    GeneRIF: The SHDRA syndrome-associated gene TMEM260 encodes a
            protein-specific O-mannosyltransferase.
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Pagnamenta,A.T., Jackson,A., Perveen,R., Beaman,G., Petts,G.,
            Gupta,A., Hyder,Z., Chung,B.H., Kan,A.S., Cheung,K.W.,
            Kerstjens-Frederikse,W.S., Abbott,K.M., Elpeleg,O., Taylor,J.C.,
            Banka,S. and Ta-Shma,A.
  CONSRTM   Genomics England Research Consortium
  TITLE     Biallelic TMEM260 variants cause truncus arteriosus, with or
            without renal defects
  JOURNAL   Clin Genet 101 (1), 127-133 (2022)
   PUBMED   34612517
  REMARK    GeneRIF: Biallelic TMEM260 variants cause truncus arteriosus, with
            or without renal defects.
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Ta-Shma,A., Khan,T.N., Vivante,A., Willer,J.R., Matak,P., Jalas,C.,
            Pode-Shakked,B., Salem,Y., Anikster,Y., Hildebrandt,F.,
            Katsanis,N., Elpeleg,O. and Davis,E.E.
  TITLE     Mutations in TMEM260 Cause a Pediatric Neurodevelopmental, Cardiac,
            and Renal Syndrome
  JOURNAL   Am J Hum Genet 100 (4), 666-675 (2017)
   PUBMED   28318500
  REMARK    GeneRIF: Study showed that truncating mutations in TMEM260 cause a
            syndrome characterized by central nervous sustem, cardiac, renal,
            and axial skeletal defects. Notably, the homozygous truncating
            mutations found in the two families affected specifically one of
            the two splice isoforms generated by this locus, arguing
            specificity in the phenotypic driver.
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Yang,B., Liu,C., Diao,L., Wang,C. and Guo,Z.
  TITLE     A polymorphism at the microRNA binding site in the 3' untranslated
            region of C14orf101 is associated with non-Hodgkin lymphoma overall
            survival
  JOURNAL   Cancer Genet 207 (4), 141-146 (2014)
   PUBMED   24831772
  REMARK    GeneRIF: Data indicate that rs4901706, located in the 3' UTR of
            C14orf101, was shown to be independently related to overall
            survival in non-Hodgkin lymphoma (NHL).
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK056291.1, AK023885.1, AL161757.4 and BX647387.1.
            
            On Apr 25, 2006 this sequence version replaced NP_060269.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.176013.1,
                                           SRR1803617.207447.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261556.11/ ENSP00000261556.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..707
                     /product="protein O-mannosyl-transferase TMEM260
                     precursor"
                     /EC_number="2.4.1.109"
                     /note="UPF0679 protein C14orf101; protein
                     O-mannosyl-transferase TMEM260"
                     /calculated_mol_wt=74565
     sig_peptide     1..50
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4990
     Site            28..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX78.3)"
     Region          52..206
                     /region_name="DUF2723"
                     /note="Protein of unknown function (DUF2723); pfam11028"
                     /db_xref="CDD:463208"
     Site            71..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX78.3)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX78.3)"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX78.3)"
     Site            189..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX78.3)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX78.3)"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX78.3)"
     Site            356..376
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX78.3)"
     Site            407
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NX78.3)"
     Site            535
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NX78.3)"
     Site            568
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:37186866; propagated from
                     UniProtKB/Swiss-Prot (Q9NX78.3)"
     CDS             1..707
                     /gene="TMEM260"
                     /gene_synonym="C14orf101; SHDRA"
                     /coded_by="NM_017799.4:118..2241"
                     /db_xref="CCDS:CCDS9727.2"
                     /db_xref="GeneID:54916"
                     /db_xref="HGNC:HGNC:20185"
                     /db_xref="MIM:617449"
ORIGIN      
        1 msphgdgrgq aqgravrvgl rrsggirggv avfaavaavf tftlppsvpg gdsgelitaa
       61 helgvahppg yplftlvakl aitlfpfgsi ayrvnllcgl fgavaasllf ftvfrlsgss
      121 aggilaagvf sfsrltwqws iaaevfslnn lfvgllmalt vhfeeaatak erskvakiga
      181 fccglslcnq htiilyvlci ipwilfqllk kkelslgsll klslyfsagl lpyvhlpiss
      241 ylnharwtwg dqttlqgflt hflreeygtf slakseigss mseillsqvt nmrtelsfni
      301 qalavcanic latkdrqnps lvwlftgmfc iyslffawra nldiskplfm gvverfwmqs
      361 navvavlagi glaavvsetn rvlnsnglqc lewlsatlfv vyqiysnysv cdqrtnyvid
      421 kfaknlltsm phdaiillrg dlpgnslrym hyceglrpdi slvdqemmty ewylpkmakh
      481 lpgvnfpgnr wnpvegilps gmvtfnlyhf levnkqketf vcigihegdp twkknyslwp
      541 wgscdklvpl eivfnpeewi kltksiynwt eeygrfdpss wesvaneemw qarmktpffi
      601 fnlaetahmp skvkaqlyaq aydlykeivy lqkehpvnwh knyaiacerm lrlqardadp
      661 evllsetirh frlysqkapn dpqqadilga lkhlrkelqs lrnrknv
//
LOCUS       NP_071332                384 aa            linear   PRI 27-APR-2025
DEFINITION  G protein-coupled receptor 88 [Homo sapiens].
ACCESSION   NP_071332
VERSION     NP_071332.2
DBSOURCE    REFSEQ: accession NM_022049.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ben Hamida,S., Sengupta,S.M., Clarke,E., McNicholas,M.,
            Moroncini,E., Darcq,E., Ter-Stepanian,M., Fortier,M.E.,
            Grizenko,N., Joober,R. and Kieffer,B.L.
  TITLE     The orphan receptor GPR88 controls impulsivity and is a risk factor
            for Attention-Deficit/Hyperactivity Disorder
  JOURNAL   Mol Psychiatry 27 (11), 4662-4672 (2022)
   PUBMED   36075963
  REMARK    GeneRIF: The orphan receptor GPR88 controls impulsivity and is a
            risk factor for Attention-Deficit/Hyperactivity Disorder.
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Chen,G., Xu,J., Inoue,A., Schmidt,M.F., Bai,C., Lu,Q., Gmeiner,P.,
            Liu,Z. and Du,Y.
  TITLE     Activation and allosteric regulation of the orphan GPR88-Gi1
            signaling complex
  JOURNAL   Nat Commun 13 (1), 2375 (2022)
   PUBMED   35501348
  REMARK    GeneRIF: Activation and allosteric regulation of the orphan
            GPR88-Gi1 signaling complex.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Badgandi,H.B., Hwang,S.H., Shimada,I.S., Loriot,E. and
            Mukhopadhyay,S.
  TITLE     Tubby family proteins are adapters for ciliary trafficking of
            integral membrane proteins
  JOURNAL   J Cell Biol 216 (3), 743-760 (2017)
   PUBMED   28154160
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Jin,C., Decker,A.M., Harris,D.L. and Blough,B.E.
  TITLE     Effect of Substitution on the Aniline Moiety of the GPR88 Agonist
            2-PCCA: Synthesis, Structure-Activity Relationships, and Molecular
            Modeling Studies
  JOURNAL   ACS Chem Neurosci 7 (10), 1418-1432 (2016)
   PUBMED   27499251
  REMARK    GeneRIF: Study designed and synthesized a series of 2-PCCA
            analogues bearing a variety of substituents at the phenyl ring of
            the aniline moiety to determine the structure-activity relationship
            (SAR) in this region; SAR studies suggested that there is a
            hydrophobic pocket in the GPR88 binding site interacting with the
            aniline region of 2-PCCA
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Alkufri,F., Shaag,A., Abu-Libdeh,B. and Elpeleg,O.
  TITLE     Deleterious mutation in GPR88 is associated with chorea, speech
            delay, and learning disabilities
  JOURNAL   Neurol Genet 2 (3), e64 (2016)
   PUBMED   27123486
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Jin,C., Decker,A.M., Huang,X.P., Gilmour,B.P., Blough,B.E.,
            Roth,B.L., Hu,Y., Gill,J.B. and Zhang,X.P.
  TITLE     Synthesis, pharmacological characterization, and structure-activity
            relationship studies of small molecular agonists for the orphan
            GPR88 receptor
  JOURNAL   ACS Chem Neurosci 5 (7), 576-587 (2014)
   PUBMED   24793972
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Del Zompo,M., Deleuze,J.F., Chillotti,C., Cousin,E., Niehaus,D.,
            Ebstein,R.P., Ardau,R., Mace,S., Warnich,L., Mujahed,M.,
            Severino,G., Dib,C., Jordaan,E., Murad,I., Soubigou,S., Koen,L.,
            Bannoura,I., Rocher,C., Laurent,C., Derock,M., Faucon Biguet,N.,
            Mallet,J. and Meloni,R.
  TITLE     Association study in three different populations between the GPR88
            gene and major psychoses
  JOURNAL   Mol Genet Genomic Med 2 (2), 152-159 (2014)
   PUBMED   24689078
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Marley,A., Choy,R.W. and von Zastrow,M.
  TITLE     GPR88 reveals a discrete function of primary cilia as selective
            insulators of GPCR cross-talk
  JOURNAL   PLoS One 8 (8), e70857 (2013)
   PUBMED   23936473
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Mizushima,K., Miyamoto,Y., Tsukahara,F., Hirai,M., Sakaki,Y. and
            Ito,T.
  TITLE     A novel G-protein-coupled receptor gene expressed in striatum
  JOURNAL   Genomics 69 (3), 314-321 (2000)
   PUBMED   11056049
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099670.2 and BC036775.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 12, 2006 this sequence version replaced NP_071332.1.
            
            Summary: The protein encoded by this gene is a G protein-coupled
            receptor found almost exclusively in the striatum, a brain
            structure that controls motor function and cognition. Defects in
            this gene have been associated with chorea, speech delay, and
            learning difficulties, as well as some neuropsychiatric disorders.
            [provided by RefSeq, Mar 2017].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB042410.1, BC036775.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315033.5/ ENSP00000314223.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.2"
     Protein         1..384
                     /product="G protein-coupled receptor 88"
                     /note="probable G-protein coupled receptor 88;
                     striatum-specific G-protein coupled receptor"
                     /calculated_mol_wt=40115
     Site            3
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9GZN0.2)"
     Region          33..347
                     /region_name="7tmA_GPR88-like"
                     /note="G protein-coupled receptor 88, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15211"
                     /db_xref="CDD:320339"
     Region          33..59
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320339"
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZN0.2)"
     Region          66..91
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320339"
     Site            74..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZN0.2)"
     Site            order(88,91..92,113..118,120..121,124,170,172..176,189,
                     192..194,196..198,200..201,297,300..301,303..304,307,
                     314..315,317..319,322,325..326)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320339"
     Region          112..143
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320339"
     Site            117..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZN0.2)"
     Region          156..178
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320339"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZN0.2)"
     Region          189..218
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320339"
     Site            196..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZN0.2)"
     Region          277..307
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320339"
     Site            286..306
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZN0.2)"
     Site            311..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZN0.2)"
     Region          315..340
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320339"
     CDS             1..384
                     /gene="GPR88"
                     /gene_synonym="COCPMR; STRG"
                     /coded_by="NM_022049.3:438..1592"
                     /db_xref="CCDS:CCDS772.1"
                     /db_xref="GeneID:54112"
                     /db_xref="HGNC:HGNC:4539"
                     /db_xref="MIM:607468"
ORIGIN      
        1 mtnssststs sttggsllll ceeeeswagr ripvsllysg laiggtlang mviylvssfr
       61 klqttsnafi vngcaadlsv calwmpqeav lgllptgsae ppadwdgagg syrllrggll
      121 glgltvslls hclvalnryl litrapatyq alyqrrhtag mlalswalal glvlllppwa
      181 prpgaapprv hypallaaaa llaqtalllh cylgivrrvr vsvkrvsvln fhllhqlpgc
      241 aaaaaafpga qhapgpggaa hpaqaqplpp alhprraqrr lsglsvlllc cvfllatqpl
      301 vwvslasgfs lpvpwgvqaa swllccalsa lnpllytwrn eefrrsvrsv lpgvgdaaaa
      361 avaatavpav sqaqlgtraa gqhw
//
LOCUS       NP_861452                723 aa            linear   PRI 27-APR-2025
DEFINITION  probable C-mannosyltransferase DPY19L4 [Homo sapiens].
ACCESSION   NP_861452
VERSION     NP_861452.2
DBSOURCE    REFSEQ: accession NM_181787.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   3  (residues 1 to 723)
  AUTHORS   Tsuritani,K., Irie,T., Yamashita,R., Sakakibara,Y., Wakaguri,H.,
            Kanai,A., Mizushima-Sugano,J., Sugano,S., Nakai,K. and Suzuki,Y.
  TITLE     Distinct class of putative 'non-conserved' promoters in humans:
            comparative studies of alternative promoters of human and mouse
            genes
  JOURNAL   Genome Res 17 (7), 1005-1014 (2007)
   PUBMED   17567985
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP873374.1, BC110870.1 and AP003692.2.
            
            On Feb 8, 2008 this sequence version replaced NP_861452.1.
            
            Sequence Note: This RefSeq was created from transcript and genomic
            sequence data because no single transcript was available for the
            full length of the gene. The extent of this transcript is supported
            by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.219160.1,
                                           SRR1660803.19639.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000414645.6/ ENSP00000389630.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.1"
     Protein         1..723
                     /product="probable C-mannosyltransferase DPY19L4"
                     /note="protein dpy-19 homolog 4; dpy-19-like protein 4"
                     /calculated_mol_wt=83625
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z388.1)"
     Region          51..714
                     /region_name="Dpy19L4"
                     /note="C-mannosyltransferase Dpy-19-like protein 4
                     (Dpy19L4); cd20180"
                     /db_xref="CDD:439133"
     Region          51..67
                     /region_name="putative TM segment 1"
                     /note="putative TM segment 1 [structural motif]"
                     /db_xref="CDD:439133"
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Region          160..181
                     /region_name="putative TM segment 2"
                     /note="putative TM segment 2 [structural motif]"
                     /db_xref="CDD:439133"
     Site            161..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Site            184..202
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Region          185..201
                     /region_name="putative TM segment 3"
                     /note="putative TM segment 3 [structural motif]"
                     /db_xref="CDD:439133"
     Region          221..235
                     /region_name="putative TM segment 4"
                     /note="putative TM segment 4 [structural motif]"
                     /db_xref="CDD:439133"
     Site            222..240
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Region          247..262
                     /region_name="putative TM segment 5"
                     /note="putative TM segment 5 [structural motif]"
                     /db_xref="CDD:439133"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Region          268..286
                     /region_name="putative TM segment 6"
                     /note="putative TM segment 6 [structural motif]"
                     /db_xref="CDD:439133"
     Site            292..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Region          294..311
                     /region_name="putative TM segment 7"
                     /note="putative TM segment 7 [structural motif]"
                     /db_xref="CDD:439133"
     Region          314..330
                     /region_name="putative TM segment 8"
                     /note="putative TM segment 8 [structural motif]"
                     /db_xref="CDD:439133"
     Site            316..337
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Region          348..366
                     /region_name="putative TM segment 9"
                     /note="putative TM segment 9 [structural motif]"
                     /db_xref="CDD:439133"
     Site            349..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Region          420..441
                     /region_name="putative TM segment 10"
                     /note="putative TM segment 10 [structural motif]"
                     /db_xref="CDD:439133"
     Site            421..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Site            466..486
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Region          470..486
                     /region_name="putative TM segment 11"
                     /note="putative TM segment 11 [structural motif]"
                     /db_xref="CDD:439133"
     Site            489..509
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     Region          490..512
                     /region_name="putative TM segment 12"
                     /note="putative TM segment 12 [structural motif]"
                     /db_xref="CDD:439133"
     Region          520..535
                     /region_name="putative TM segment 13"
                     /note="putative TM segment 13 [structural motif]"
                     /db_xref="CDD:439133"
     Site            522..542
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z388.1)"
     CDS             1..723
                     /gene="DPY19L4"
                     /coded_by="NM_181787.3:100..2271"
                     /db_xref="CCDS:CCDS34924.1"
                     /db_xref="GeneID:286148"
                     /db_xref="HGNC:HGNC:27829"
                     /db_xref="MIM:613895"
ORIGIN      
        1 maeeegppve lrqrkkpkss enkesakeek isdipipera pkhvlfqrfa kifigclaav
       61 tsgmmyalyl sayherkfwf snrqelerei tfqgdsaiyy syykdmlkap sfergvyelt
      121 hnnktvslkt inavqqmsly peliasilyq atgsneiiep vyfyigivfg lqgiyvtalf
      181 vtswlmsgtw lagmltvawf vinrvdttri eysiplrenw alpyfacqia altgylksnl
      241 ntygerfcyl lmsastytfm mmweyshyll flqaislfll dtfsveqsdk vyevykiyif
      301 slflgyllqf enpallvspl lslvaalmla kclqlnvkkg sfvakiikvi nfylvctlti
      361 tlniimkmfv phkenghmlk flevkfglnm tknftmnwll cqeslqapsq dfflrltqss
      421 llpfyilvli icflsmlqvi frringkslk etvtledgri gerpeiiyhv ihtillgsla
      481 mvieglkyiw ipyvcmlaaf gvcspelwmt lfkwlrlrtv hpillalils mavptiigls
      541 lwkeffprlm telmelqefy dpdtvelmtw ikrqapvaav fagspqlmga iklctgwmvt
      601 slplyndddl lkrneniyqi yskrsaediy kiltsykany livedaicne vgpmrgcrvk
      661 dlldianghm vceegdklty skygrfchev kinyspyvny ftrvywnrsy fvykintvis
      721 fqs
//
LOCUS       NP_060232                777 aa            linear   PRI 27-APR-2025
DEFINITION  myotubularin-related protein 10 [Homo sapiens].
ACCESSION   NP_060232
VERSION     NP_060232.2
DBSOURCE    REFSEQ: accession NM_017762.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 777)
  AUTHORS   Weissglas-Volkov,D., Aguilar-Salinas,C.A., Nikkola,E., Deere,K.A.,
            Cruz-Bautista,I., Arellano-Campos,O., Munoz-Hernandez,L.L.,
            Gomez-Munguia,L., Ordonez-Sanchez,M.L., Reddy,P.M., Lusis,A.J.,
            Matikainen,N., Taskinen,M.R., Riba,L., Cantor,R.M.,
            Sinsheimer,J.S., Tusie-Luna,T. and Pajukanta,P.
  TITLE     Genomic study in Mexicans identifies a new locus for triglycerides
            and refines European lipid loci
  JOURNAL   J Med Genet 50 (5), 298-308 (2013)
   PUBMED   23505323
REFERENCE   3  (residues 1 to 777)
  AUTHORS   Lorenzo,O., Urbe,S. and Clague,M.J.
  TITLE     Systematic analysis of myotubularins: heteromeric interactions,
            subcellular localisation and endosome related functions
  JOURNAL   J Cell Sci 119 (Pt 14), 2953-2959 (2006)
   PUBMED   16787938
REFERENCE   4  (residues 1 to 777)
  AUTHORS   Wishart,M.J. and Dixon,J.E.
  TITLE     PTEN and myotubularin phosphatases: from 3-phosphoinositide
            dephosphorylation to disease
  JOURNAL   Trends Cell Biol 12 (12), 579-585 (2002)
   PUBMED   12495846
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC090829.3, AL598227.1, AL832603.1, AC087481.9, BC094750.1 and
            AA461184.1.
            
            On Jan 23, 2007 this sequence version replaced NP_060232.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832603.1, SRR1803614.25324.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000435680.6/ ENSP00000402537.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q13.3"
     Protein         1..777
                     /product="myotubularin-related protein 10"
                     /note="inactive phosphatidylinositol 3-phosphatase 10"
                     /calculated_mol_wt=88142
     Region          21..195
                     /region_name="PH-GRAM_MTMR10"
                     /note="Myotubularian (MTM) related 10 protein (MTMR10)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13346"
                     /db_xref="CDD:270154"
     Region          196..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXD2.3)"
     Region          279..472
                     /region_name="PTP-MTMR10"
                     /note="protein tyrosine phosphatase-like pseudophosphatase
                     domain of myotubularin related phosphoinositide
                     phosphatase 10; cd14593"
                     /db_xref="CDD:350441"
     Region          574..705
                     /region_name="3-PAP"
                     /note="Myotubularin-associated protein; pfam12578"
                     /db_xref="CDD:463634"
     Site            607
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NXD2.3)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NXD2.3)"
     CDS             1..777
                     /gene="MTMR10"
                     /coded_by="NM_017762.3:123..2456"
                     /db_xref="CCDS:CCDS45204.1"
                     /db_xref="GeneID:54893"
                     /db_xref="HGNC:HGNC:25999"
ORIGIN      
        1 mfslkppkpt frsyllpppq tddkinsepk ikklepvllp geivvnevnf vrkciatdts
       61 qydlwgklic snfkisfitd dpmplqkfhy rnlllgehdv pltcieqivt vndhkrkqkv
      121 lgpnqklkfn pteliiyckd frivrfrfde sgpesakkvc laiahysqpt dlqllfafey
      181 vgkkyhnsan kingipsgdg gggggggnga gggssqktpl fetysdwdre ikrtgasgwr
      241 vcsinegymi stclpeyivv pssladqdlk ifshsfvgrr mplwcwshsn gsalvrmali
      301 kdvlqqrkid qricnaitks hpqrsdvyks dldktlpniq evqaafvklk qlcvnepfee
      361 teekwlssle ntrwleyvra flkhsaelvy mleskhlsvv lqeeegrdls ccvaslvqvm
      421 ldpyfrtitg fqsliqkewv magyqfldrc nhlkrsekes plfllfldat wqlleqypaa
      481 fefsetylav lydstrislf gtflfnsphq rvkqstefai skniqlgdek glkfpsvwdw
      541 slqftakdrt lfhnpfyigk stpciqngsv ksfkrtkksy sstlrgmpsa lkngiisdqe
      601 llprrnslil kpkpdpaqqt dsqnsdteqy frewfskpan lhgvilprvs gthiklwklc
      661 yfrwvpeaqi slggsitafh klslladevd vlsrmlrqqr sgpleacyge lgqsrmyfna
      721 sgphhtdtsg tpeflsssfp fspvgnlcrr silgtplskf lsgakiwlst etlaned
//
LOCUS       NP_525125                450 aa            linear   PRI 27-APR-2025
DEFINITION  tubulin alpha-3D chain [Homo sapiens].
ACCESSION   NP_525125 XP_054284
VERSION     NP_525125.2
DBSOURCE    REFSEQ: accession NM_080386.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Hao,X.D., Chen,P., Zhang,Y.Y., Li,S.X., Shi,W.Y. and Gao,H.
  TITLE     De novo mutations of TUBA3D are associated with keratoconus
  JOURNAL   Sci Rep 7 (1), 13570 (2017)
   PUBMED   29051577
  REMARK    GeneRIF: TUBA3D is a new gene that causes keratoconus.The c.31 C >
            T (Gln11stop) and c.201insTT (Val68Leufs*2) mutations lead to
            TUBA3D degradation and higher matrix metalloproteinases expression
            in cornea fibroblasts.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 450)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Villasante,A., Wang,D., Dobner,P., Dolph,P., Lewis,S.A. and
            Cowan,N.J.
  TITLE     Six mouse alpha-tubulin mRNAs encode five distinct isotypes:
            testis-specific expression of two sister genes
  JOURNAL   Mol Cell Biol 6 (7), 2409-2419 (1986)
   PUBMED   3785200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB051220.1, BC057810.1 and
            AK292253.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 29, 2007 this sequence version replaced NP_525125.1.
            
            Summary: This gene encodes a member of the alpha tubulin family.
            Tubulin is a major component of microtubules, which are composed of
            alpha- and beta-tubulin heterodimers and microtubule-associated
            proteins in the cytoskeleton. Microtubules maintain cellular
            structure, function in intracellular transport, and play a role in
            spindle formation during mitosis. [provided by RefSeq, Oct 2011].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.179383.1,
                                           SRR5189667.179807.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321253.7/ ENSP00000326042.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.1"
     Protein         1..450
                     /product="tubulin alpha-3D chain"
                     /note="alpha-tubulin isotype H2-alpha; tubulin alpha-3C/D
                     chain; tubulin alpha-2 chain; alpha-tubulin 3D; Tubulin
                     alpha-3C chain; Alpha-tubulin 3C"
                     /calculated_mol_wt=49829
     mat_peptide     1..449
                     /product="Detyrosinated tubulin alpha-3D chain.
                     /evidence=ECO:0000305|PubMed:25908662,
                     ECO:0000305|PubMed:29146869. /id=PRO_0000444672"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DPH8.1)"
                     /calculated_mol_wt=49797
     Region          1..440
                     /region_name="PTZ00335"
                     /note="tubulin alpha chain; Provisional"
                     /db_xref="CDD:185562"
     Region          1..4
                     /region_name="MREC motif.
                     /evidence=ECO:0000250|UniProtKB:P68363"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DPH8.1)"
     Site            40
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24906155; propagated from
                     UniProtKB/Swiss-Prot (P0DPH8.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P68373; propagated from
                     UniProtKB/Swiss-Prot (P0DPH8.1)"
     Site            450
                     /site_type="other"
                     /note="Involved in polymerization; propagated from
                     UniProtKB/Swiss-Prot (P0DPH8.1)"
     CDS             1..450
                     /gene="TUBA3D"
                     /gene_synonym="H2-ALPHA; KTCN9; TUBA2"
                     /coded_by="NM_080386.4:82..1434"
                     /db_xref="CCDS:CCDS33290.1"
                     /db_xref="GeneID:113457"
                     /db_xref="HGNC:HGNC:24071"
                     /db_xref="MIM:617878"
ORIGIN      
        1 mrecisihvg qagvqignac welyclehgi qpdgqmpsdk tigggddsfn tffsetgagk
       61 hvpravfvdl eptvvdevrt gtyrqlfhpe qlitgkedaa nnyarghyti gkeivdlvld
      121 rirkladlct glqgflifhs fgggtgsgfa sllmerlsvd ygkksklefa iypapqvsta
      181 vvepynsilt thttlehsdc afmvdneaiy dicrrnldie rptytnlnrl igqivssita
      241 slrfdgalnv dltefqtnlv pyprihfpla tyapvisaek ayheqlsvae itnacfepan
      301 qmvkcdprhg kymaccmlyr gdvvpkdvna aiatiktkrt iqfvdwcptg fkvginyqpp
      361 tvvpggdlak vqravcmlsn ttaiaeawar ldhkfdlmya krafvhwyvg egmeegefse
      421 aredlaalek dyeevgvdsv eaeaeegeey
//
LOCUS       NP_001352781             262 aa            linear   PRI 27-APR-2025
DEFINITION  OX-2 membrane glycoprotein isoform f precursor [Homo sapiens].
ACCESSION   NP_001352781 XP_016861943
VERSION     NP_001352781.1
DBSOURCE    REFSEQ: accession NM_001365852.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wedig,J., Jasani,S., Mukherjee,D., Lathrop,H., Matreja,P., Pfau,T.,
            D'Alesio,L., Guenther,A., Fenn,L., Kaiser,M., Torok,M.A., McGue,J.,
            Sizemore,G.M., Noonan,A.M., Dillhoff,M.E., Blaser,B.W.,
            Frankel,T.L., Culp,S., Hart,P.A., Cruz-Monserrate,Z. and Mace,T.A.
  TITLE     CD200 is overexpressed in the pancreatic tumor microenvironment and
            predictive of overall survival
  JOURNAL   Cancer Immunol Immunother 73 (6), 96 (2024)
   PUBMED   38619621
  REMARK    GeneRIF: CD200 is overexpressed in the pancreatic tumor
            microenvironment and predictive of overall survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Gonzalez-Montes,Y., Osca-Gelis,G., Rodriguez-Romanos,R.,
            Villavicencio,A., Gonzalez-Bartulos,M., Llopis,F., Clapes,V.,
            Oriol,A., Sureda,A., Escoda,L., Sarra,J., Garzo,A., Lloveras,N.,
            Gomez,B., Granada,I. and Gallardo,D.
  TITLE     CD200 genotype is associated with clinical outcome of patients with
            multiple myeloma
  JOURNAL   Front Immunol 15, 1252445 (2024)
   PUBMED   38455039
  REMARK    GeneRIF: CD200 genotype is associated with clinical outcome of
            patients with multiple myeloma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Tang,Y., Liu,W., Kadu,S., Johnson,O., Hasanali,Z.S., Kelly,A.,
            Shestov,A., Pajarillo,R., Greenblatt,E., Holmes,M., Wang,L.P.,
            Shih,N., O'Connor,R.S., Ruella,M., Garfall,A.L., Allman,D.,
            Vogl,D.T., Cohen,A., June,C.H. and Sheppard,N.C.
  TITLE     Exploiting the CD200-CD200R immune checkpoint axis in multiple
            myeloma to enhance CAR T-cell therapy
  JOURNAL   Blood 143 (2), 139-151 (2024)
   PUBMED   37616575
  REMARK    GeneRIF: Exploiting the CD200-CD200R immune checkpoint axis in
            multiple myeloma to enhance CAR T-cell therapy.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Zhang,M., Qian,X.H., Hu,J., Zhang,Y., Lin,X., Hai,W., Shi,K.,
            Jiang,X., Li,Y., Tang,H.D. and Li,B.
  TITLE     Integrating TSPO PET imaging and transcriptomics to unveil the role
            of neuroinflammation and amyloid-beta deposition in Alzheimer's
            disease
  JOURNAL   Eur J Nucl Med Mol Imaging 51 (2), 455-467 (2024)
   PUBMED   37801139
  REMARK    GeneRIF: Integrating TSPO PET imaging and transcriptomics to unveil
            the role of neuroinflammation and amyloid-beta deposition in
            Alzheimer's disease.
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Moon,S.Y., Han,M., Ryu,G., Shin,S.A., Lee,J.H. and Lee,C.S.
  TITLE     Emerging Immune Checkpoint Molecules on Cancer Cells: CD24 and
            CD200
  JOURNAL   Int J Mol Sci 24 (20), 15072 (2023)
   PUBMED   37894750
  REMARK    GeneRIF: Emerging Immune Checkpoint Molecules on Cancer Cells: CD24
            and CD200.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Chen,Z., Marsden,P.A. and Gorczynski,R.M.
  TITLE     Cloning and characterization of the human CD200 promoter region
  JOURNAL   Mol Immunol 43 (6), 579-587 (2006)
   PUBMED   15955564
  REMARK    GeneRIF: revealed a 169 bp region responsible for constitutive
            expression of CD200; positive regulatory domains were identified in
            the core promoter; and documented evidence for C/EBPbeta as being
            important in transcriptional regulation of CD200
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Preston,S., Wright,G.J., Starr,K., Barclay,A.N. and Brown,M.H.
  TITLE     The leukocyte/neuron cell surface antigen OX2 binds to a ligand on
            macrophages
  JOURNAL   Eur J Immunol 27 (8), 1911-1918 (1997)
   PUBMED   9295026
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Douglas,J., Albertson,D.G., Barclay,A.N., Davis,M. and
            Rabbitts,P.H.
  TITLE     RFLP and mapping of human MOX-1 gene on chromosome 3
  JOURNAL   Nucleic Acids Res 16 (18), 9067 (1988)
   PUBMED   2902568
REFERENCE   9  (residues 1 to 262)
  AUTHORS   McCaughan,G.W., Clark,M.J., Hurst,J., Grosveld,F. and Barclay,A.N.
  TITLE     The gene for MRC OX-2 membrane glycoprotein is localized on human
            chromosome 3
  JOURNAL   Immunogenetics 25 (2), 133-135 (1987)
   PUBMED   3817906
REFERENCE   10 (residues 1 to 262)
  AUTHORS   McCaughan,G.W., Clark,M.J. and Barclay,A.N.
  TITLE     Characterization of the human homolog of the rat MRC OX-2 membrane
            glycoprotein
  JOURNAL   Immunogenetics 25 (5), 329-335 (1987)
   PUBMED   3032785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112487.3.
            
            On Sep 20, 2018 this sequence version replaced XP_016861943.1.
            
            Summary: This gene encodes a type I membrane glycoprotein
            containing two extracellular immunoglobulin domains, a
            transmembrane and a cytoplasmic domain. This gene is expressed by
            various cell types, including B cells, a subset of T cells,
            thymocytes, endothelial cells, and neurons. The encoded protein
            plays an important role in immunosuppression and regulation of
            anti-tumor activity. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.164209.1,
                                           SRR1803613.140558.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.2"
     Protein         1..262
                     /product="OX-2 membrane glycoprotein isoform f precursor"
                     /note="CD200 antigen; antigen identified by monoclonal
                     antibody MRC OX-2; OX-2 membrane glycoprotein"
                     /calculated_mol_wt=26924
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2527
     Region          25..132
                     /region_name="IgV_1_MRC-OX-2_like"
                     /note="First immunoglobulin (Ig) variable (V) domain of
                     rat MRC OX-2 antigen, and similar domains; cd05846"
                     /db_xref="CDD:409433"
     Region          25..45
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409433"
     Region          25..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409433"
     Region          31..35
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409433"
     Region          38..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409433"
     Region          46..52
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409433"
     Region          53..62
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409433"
     Region          54..60
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409433"
     Region          63..80
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409433"
     Region          63..71
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409433"
     Region          76..80
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409433"
     Region          86..116
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409433"
     Region          86..93
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409433"
     Region          96..102
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409433"
     Region          110..117
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409433"
     Region          117..123
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409433"
     Region          123..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409433"
     Region          124..132
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409433"
     Region          <152..223
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          162..166
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          190..194
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          204..209
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          219..222
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..262
                     /gene="CD200"
                     /gene_synonym="MOX1; MOX2; MRC; OX-2"
                     /coded_by="NM_001365852.1:492..1280"
                     /note="isoform f precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:4345"
                     /db_xref="HGNC:HGNC:7203"
                     /db_xref="MIM:155970"
ORIGIN      
        1 mpfshlstys lvwvmaavvl ctaqvqvvtq dereqlytpa slkcslqnaq ealivtwqkk
       61 kavspenmvt fsenhgvviq paykdkinit qlglqnstit fwnitledeg cymclfntfg
      121 fgkisgtacl tvyvqpivsl hykfsedhln itcsatarpa pmvfwkvprs gienstvtls
      181 hpngttsvts ilhikdpknq vgkevicqvl hlgtvtdfkq tvnkgywfsv plllsivslv
      241 illvlisill ywkrhrnqdr ep
//
LOCUS       NP_001348965             774 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 14 [Mus musculus].
ACCESSION   NP_001348965 XP_017169152
VERSION     NP_001348965.1
DBSOURCE    REFSEQ: accession NM_001362036.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 774)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 774)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 774)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 774)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 774)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            On Mar 31, 2018 this sequence version replaced XP_017169152.1.
            
            Transcript Variant: This variant (46), as well as variant 47,
            encodes isoform 14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AK032543.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMN00849374,
                                    SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..774
                     /product="cAMP-regulated phosphoprotein 21 isoform 14"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=84166
     Region          162..223
                     /region_name="R3H_encore_like"
                     /note="R3H domain of encore-like and DIP1-like proteins.
                     Drosophila encore is involved in the germline exit after
                     four mitotic divisions, by facilitating
                     SCF-ubiquitin-proteasome-dependent proteolysis. Maize
                     DBF1-interactor protein 1 (DIP1) containing an R3H...;
                     cd02642"
                     /db_xref="CDD:100071"
     Site            order(195,199)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100071"
     Region          520..>749
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..774
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362036.1:434..2758"
                     /note="isoform 14 is encoded by transcript variant 46"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqesih lqlssfpslq eedksrkdds erekekdknr
      121 eklserpkir mlskdcsqey tdstgidlhg flintlknns rdrmillkme qemidfiads
      181 nnhykkfpqm ssyqrmlvhr vaayfgldhn vdqtgksvii nktsstripe qrfcehlkde
      241 kseesqkrfi lkrdnssidk ednqsvcsqe slfldnsrlq edmhicnety kkrqlfrahr
      301 dssgrtsgsr qsssetelrw pdhqrawsst dsdssnrnlk ptmtktasfg gitvltrgds
      361 tsstrsagkl sktgsessss agssgslsrt hpqstaltss vaagspgcma ysengmggqv
      421 ppsstsyill plesatgipp gsillnphtg qpfvnpdgtp aiynppgsqq tlrgtvggqp
      481 qqppqqqpsp qpqqqvqasq pqmagplvtq reelaaqfsq lsmsrqssgd tpeppsgtvy
      541 pasllpqtaq pqsyvitsag qqlstggfsd sgppisqqvl qappspqgfv qqpppaqmsv
      601 yyypsgqypt stsqqyrpla svqysaqrsq qipqttqqag yqpvlsgqqg fqgmmgvqqs
      661 ahsqgvmssq qgapvhgvmv syptmssyqv pmtqgsqavp qqtyqppiml psqagqgslp
      721 atgmpvycnv tppnpqnnlr lmgphcpsst vpvmsascrt ncgnvsnagw qvkf
//
LOCUS       NP_060268                559 aa            linear   PRI 27-APR-2025
DEFINITION  YTH domain-containing family protein 1 [Homo sapiens].
ACCESSION   NP_060268
VERSION     NP_060268.2
DBSOURCE    REFSEQ: accession NM_017798.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Han,Y., Pu,Y., Liu,X., Liu,Z., Chen,Y., Tang,L., Zhou,J., Song,Q.
            and Ji,Q.
  TITLE     YTHDF1 regulates GID8-mediated glutamine metabolism to promote
            colorectal cancer progression in m6A-dependent manner
  JOURNAL   Cancer Lett 601, 217186 (2024)
   PUBMED   39151722
  REMARK    GeneRIF: YTHDF1 regulates GID8-mediated glutamine metabolism to
            promote colorectal cancer progression in m6A-dependent manner.
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Zhang,L., Cai,E., Xu,Y., Liu,Z., Zheng,M., Sun,Z., Pei,D. and
            Wang,Q.
  TITLE     YTHDF1 facilitates esophageal cancer progression via augmenting
            m6A-dependent TINAGL1 translation
  JOURNAL   Cell Signal 122, 111332 (2024)
   PUBMED   39098703
  REMARK    GeneRIF: YTHDF1 facilitates esophageal cancer progression via
            augmenting m6A-dependent TINAGL1 translation.
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Chen,D., Ji,F., Zhou,Q., Cheung,H., Pan,Y., Lau,H.C., Liang,C.,
            Yang,Z., Huang,P., Wei,Q., Cheung,A.H., Kang,W., Chen,H., Yu,J. and
            Wong,C.C.
  TITLE     RUVBL1/2 Blockade Targets YTHDF1 Activity to Suppress m6A-Dependent
            Oncogenic Translation and Colorectal Tumorigenesis
  JOURNAL   Cancer Res 84 (17), 2856-2872 (2024)
   PUBMED   38900944
  REMARK    GeneRIF: RUVBL1/2 Blockade Targets YTHDF1 Activity to Suppress
            m6A-Dependent Oncogenic Translation and Colorectal Tumorigenesis.
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Wang,S., Xu,L., Wang,D., Zhao,S., Li,K., Ma,F., Yao,Q., Zhang,Y.,
            Wu,Z., Shao,Y., Song,S. and Yan,W.
  TITLE     YTHDF1 promotes the osteolytic bone metastasis of breast cancer via
            inducing EZH2 and CDH11 translation
  JOURNAL   Cancer Lett 597, 217047 (2024)
   PUBMED   38871245
  REMARK    GeneRIF: YTHDF1 promotes the osteolytic bone metastasis of breast
            cancer via inducing EZH2 and CDH11 translation.
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Wu,Y., Luo,Y., Yao,X., Shi,X., Xu,Z., Re,J., Shi,M., Li,M., Liu,J.,
            He,Y. and Du,X.
  TITLE     KIAA1429 increases FOXM1 expression through YTHDF1-mediated m6A
            modification to promote aerobic glycolysis and tumorigenesis in
            multiple myeloma
  JOURNAL   Cell Biol Toxicol 40 (1), 58 (2024)
   PUBMED   39060874
  REMARK    GeneRIF: KIAA1429 increases FOXM1 expression through
            YTHDF1-mediated m6A modification to promote aerobic glycolysis and
            tumorigenesis in multiple myeloma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Wang,X., Lu,Z., Gomez,A., Hon,G.C., Yue,Y., Han,D., Fu,Y.,
            Parisien,M., Dai,Q., Jia,G., Ren,B., Pan,T. and He,C.
  TITLE     N6-methyladenosine-dependent regulation of messenger RNA stability
  JOURNAL   Nature 505 (7481), 117-120 (2014)
   PUBMED   24284625
REFERENCE   8  (residues 1 to 559)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   9  (residues 1 to 559)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   10 (residues 1 to 559)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC050284.1 and BC003681.1.
            
            On Jun 4, 2003 this sequence version replaced NP_060268.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050284.1, AK095795.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370339.8/ ENSP00000359364.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..559
                     /product="YTH domain-containing family protein 1"
                     /note="YTH domain family 1; YTH domain family protein 1;
                     DACA-1; dermatomyositis associated with cancer putative
                     autoantigen 1; YTH domain family, member 1; YTH
                     N(6)-methyladenosine RNA binding protein 1; YTH
                     N6-methyladenosine RNA binding protein 1"
                     /calculated_mol_wt=60743
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYJ9.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BYJ9.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BYJ9.1)"
     Region          <227..364
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          238..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYJ9.1)"
     Region          <258..311
                     /region_name="Replication protein A, class 2b
                     aminoacyl-tRNA synthetases, and related proteins with
                     oligonucleotide/oligosaccharide (OB) fold."
                     /note="This superfamily includes two
                     oligonucleotide/oligosaccharide binding fold (OBF) domain
                     families. One of these contains the OBF domains of the
                     large (RPA1, 70kDa), middle (RPA2, RPA4, 32kDa) and small
                     (RPA3, 14 kDa) subunits of human heterotrimeric...;
                     cl09930"
                     /db_xref="CDD:471953"
     Region          390..523
                     /region_name="YTH"
                     /note="YT521-B-like domain; pfam04146"
                     /db_xref="CDD:461195"
     CDS             1..559
                     /gene="YTHDF1"
                     /gene_synonym="C20orf21; DF1"
                     /coded_by="NM_017798.4:240..1919"
                     /db_xref="CCDS:CCDS13511.1"
                     /db_xref="GeneID:54915"
                     /db_xref="HGNC:HGNC:15867"
                     /db_xref="MIM:616529"
ORIGIN      
        1 msatsvdtqr tkgqdnkvqn gslhqkdtvh dndfepyltg qsnqsnsyps msdpylssyy
       61 ppsigfpysl neapwstagd ppipylttyg qlsngdhhfm hdavfgqpgg lgnniyqhrf
      121 nffpenpafs awgtsgsqgq qtqssaygss ytyppsslgg tvvdgqpgfh sdtlskapgm
      181 nsleqgmvgl kigdvsssav ktvgsvvssv altgvlsgng gtnvnmpvsk ptswaaiask
      241 pakpqpkmkt ksgpvmgggl ppppikhnmd igtwdnkgpv pkapvpqqap spqaapqpqq
      301 vaqplpaqpp alaqpqyqsp qqppqtrwva prnrnaafgq sggagsdsns pgnvqpnsap
      361 sveshpvlek lkaahsynpk efewnlksgr vfiiksysed dihrsikysi wcstehgnkr
      421 ldsafrcmss kgpvyllfsv ngsghfcgva emkspvdygt sagvwsqdkw kgkfdvqwif
      481 vkdvpnnqlr hirlenndnk pvtnsrdtqe vplekakqvl kiissykhtt sifddfahye
      541 krqeeeevvr kerqsrnkq
//
LOCUS       NP_000966                178 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein uL5 isoform 1 [Homo sapiens].
ACCESSION   NP_000966
VERSION     NP_000966.2
DBSOURCE    REFSEQ: accession NM_000975.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Chen,J., Lei,C., Zhang,H., Huang,X., Yang,Y., Liu,J., Jia,Y.,
            Shi,H., Zhang,Y., Zhang,J. and Du,J.
  TITLE     RPL11 promotes non-small cell lung cancer cell proliferation by
            regulating endoplasmic reticulum stress and cell autophagy
  JOURNAL   BMC Mol Cell Biol 24 (1), 7 (2023)
   PUBMED   36869281
  REMARK    GeneRIF: RPL11 promotes non-small cell lung cancer cell
            proliferation by regulating endoplasmic reticulum stress and cell
            autophagy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Babaylova,E.S., Gopanenko,A.V., Tupikin,A.E., Kabilov,M.R.,
            Malygin,A.A. and Karpova,G.G.
  TITLE     Deficiency of the Ribosomal Protein uL5 Leads to Significant
            Rearrangements of the Transcriptional and Translational Landscapes
            in Mammalian Cells
  JOURNAL   Int J Mol Sci 22 (24), 13485 (2021)
   PUBMED   34948282
  REMARK    GeneRIF: Deficiency of the Ribosomal Protein uL5 Leads to
            Significant Rearrangements of the Transcriptional and Translational
            Landscapes in Mammalian Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Panici,B., Nakajima,H., Carlston,C.M., Ozadam,H., Cenik,C. and
            Cenik,E.S.
  TITLE     Loss of coordinated expression between ribosomal and mitochondrial
            genes revealed by comprehensive characterization of a large family
            with a rare Mendelian disorder
  JOURNAL   Genomics 113 (4), 1895-1905 (2021)
   PUBMED   33862179
  REMARK    GeneRIF: Loss of coordinated expression between ribosomal and
            mitochondrial genes revealed by comprehensive characterization of a
            large family with a rare Mendelian disorder.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Graphodatsky,A.S., Vorobieva,N.V., Filipenko,M.L., Voronina,E.V.,
            Frengen,E. and Prydz,H.
  TITLE     Assignment of the L11 ribosomal protein gene (RPL11) to human
            chromosome 1p36.1-->p35 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 84 (1-2), 97-98 (1999)
   PUBMED   10343117
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Mishin,V.P., Filipenko,M.L., Muravlev,A.I., Karpova,G.G. and
            Mertvetsov,N.P.
  TITLE     [Cloning and determination of the primary structure of DNA
            complementary to the mRNA of human ribosomal protein L11]
  JOURNAL   Bioorg Khim 21 (2), 158-160 (1995)
   PUBMED   7748210
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Sieff,C.
  TITLE     Diamond-Blackfan Anemia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BU954396.1, CA335141.1, BX118515.1, AL451000.16 and
            AA748897.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 5, 2001 this sequence version replaced NP_000966.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L5P family of ribosomal proteins. It is located in the
            cytoplasm. The protein probably associates with the 5S rRNA.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. As is typical for genes
            encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM740317.1, DA529750.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000643754.2/ ENSP00000496250.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..178
                     /product="large ribosomal subunit protein uL5 isoform 1"
                     /note="cell growth-inhibiting protein 34; 60S ribosomal
                     protein L11; CLL-associated antigen KW-12; large ribosomal
                     subunit protein uL5"
                     /calculated_mol_wt=20121
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:12962325, ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P62913.2)"
     Region          5..175
                     /region_name="PTZ00156"
                     /note="60S ribosomal protein L11; Provisional"
                     /db_xref="CDD:185485"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P62913.2)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62913.2)"
     Site            52
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62913.2)"
     Site            85
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62913.2)"
     CDS             1..178
                     /gene="RPL11"
                     /gene_synonym="DBA7; GIG34; L11; uL5"
                     /coded_by="NM_000975.5:19..555"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS238.1"
                     /db_xref="GeneID:6135"
                     /db_xref="HGNC:HGNC:10301"
                     /db_xref="MIM:604175"
ORIGIN      
        1 maqdqgeken pmrelrirkl clnicvgesg drltraakvl eqltgqtpvf skarytvrsf
       61 girrnekiav hctvrgakae eilekglkvr eyelrknnfs dtgnfgfgiq ehidlgikyd
      121 psigiygldf yvvlgrpgfs iadkkrrtgc igakhriske eamrwfqqky dgiilpgk
//
LOCUS       NP_872422                226 aa            linear   PRI 27-APR-2025
DEFINITION  arpin isoform 1 [Homo sapiens].
ACCESSION   NP_872422
VERSION     NP_872422.1
DBSOURCE    REFSEQ: accession NM_182616.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Park,M.J., Jeong,E., Lee,E.J., Choi,H.J., Moon,B.H., Kang,K. and
            Chang,S.
  TITLE     RNA Editing Enzyme ADAR1 Suppresses the Mobility of Cancer Cells
            via ARPIN
  JOURNAL   Mol Cells 46 (6), 351-359 (2023)
   PUBMED   36921992
  REMARK    GeneRIF: RNA Editing Enzyme ADAR1 Suppresses the Mobility of Cancer
            Cells via ARPIN.
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Simanov,G., Dang,I., Fokin,A.I., Oguievetskaia,K., Campanacci,V.,
            Cherfils,J. and Gautreau,A.M.
  TITLE     Arpin Regulates Migration Persistence by Interacting with Both
            Tankyrases and the Arp2/3 Complex
  JOURNAL   Int J Mol Sci 22 (8), 4115 (2021)
   PUBMED   33923443
  REMARK    GeneRIF: Arpin Regulates Migration Persistence by Interacting with
            Both Tankyrases and the Arp2/3 Complex.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Jubrail,J., Africano-Gomez,K., Herit,F., Mularski,A.,
            Bourdoncle,P., Oberg,L., Israelsson,E., Burgel,P.R., Mayer,G.,
            Cunoosamy,D.M., Kurian,N. and Niedergang,F.
  TITLE     Arpin is critical for phagocytosis in macrophages and is targeted
            by human rhinovirus
  JOURNAL   EMBO Rep 21 (1), e47963 (2020)
   PUBMED   31721415
  REMARK    GeneRIF: Arpin is critical for phagocytosis in macrophages and is
            targeted by human rhinovirus.
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Li,Y., Qiu,J., Pang,T., Guo,Z., Su,Y., Zeng,Q. and Zhang,X.
  TITLE     Restoration of Arpin suppresses aggressive phenotype of breast
            cancer cells
  JOURNAL   Biomed Pharmacother 92, 116-121 (2017)
   PUBMED   28531800
  REMARK    GeneRIF: ARPIN is down-regulated in breast cancer cells and
            predicts poor prognosis in breast cancer patients. Data suggest
            that restoration of ARPIN in breast cancer cells suppresses cell
            proliferation, colony formation, cell cycle distribution, invasion
            in vitro, and tumorigenesis in vivo (xenograft experiments in nude
            mice); Arpin acts as tumor suppressor in breast cancer and is
            associated with inhibition of Akt signaling.
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Li,T., Zheng,H.M., Deng,N.M., Jiang,Y.J., Wang,J. and Zhang,D.L.
  TITLE     Clinicopathological and prognostic significance of aberrant Arpin
            expression in gastric cancer
  JOURNAL   World J Gastroenterol 23 (8), 1450-1457 (2017)
   PUBMED   28293092
  REMARK    GeneRIF: Low Arpin levels are associated with clinicopathological
            variables and a poor prognosis in gastric cancer patients
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Liu,X., Zhao,B., Wang,H., Wang,Y., Niu,M., Sun,M., Zhao,Y., Yao,R.
            and Qu,Z.
  TITLE     Aberrant expression of Arpin in human breast cancer and its
            clinical significance
  JOURNAL   J Cell Mol Med 20 (3), 450-458 (2016)
   PUBMED   26648569
  REMARK    GeneRIF: Arpin downregulation may contribute to the initiation and
            development of breast cancer metastasis.
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Fetics,S., Thureau,A., Campanacci,V., Aumont-Nicaise,M., Dang,I.,
            Gautreau,A., Perez,J. and Cherfils,J.
  TITLE     Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies
            Its Acidic Tail as a Primary Binding Epitope
  JOURNAL   Structure 24 (2), 252-260 (2016)
   PUBMED   26774128
  REMARK    GeneRIF: Data reveal that Arpin is comprised of an elongated
            globular core from which the C-terminal tail extends as a linear
            peptide, thus forming a primary epitope that is readily available
            to tether Arpin to interacting proteins.
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Deng,W.S., Zhang,J., Ju,H., Zheng,H.M., Wang,J., Wang,S. and
            Zhang,D.L.
  TITLE     Arpin contributes to bacterial translocation and development of
            severe acute pancreatitis
  JOURNAL   World J Gastroenterol 21 (14), 4293-4301 (2015)
   PUBMED   25892881
  REMARK    GeneRIF: Arpin protein affects the expression of tight junction
            proteins and may have an impact on bacterial translocation in
            severe acute pancreatitis.
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Dang,I., Gorelik,R., Sousa-Blin,C., Derivery,E., Guerin,C.,
            Linkner,J., Nemethova,M., Dumortier,J.G., Giger,F.A.,
            Chipysheva,T.A., Ermilova,V.D., Vacher,S., Campanacci,V.,
            Herrada,I., Planson,A.G., Fetics,S., Henriot,V., David,V.,
            Oguievetskaia,K., Lakisic,G., Pierre,F., Steffen,A., Boyreau,A.,
            Peyrieras,N., Rottner,K., Zinn-Justin,S., Cherfils,J., Bieche,I.,
            Alexandrova,A.Y., David,N.B., Small,J.V., Faix,J., Blanchoin,L. and
            Gautreau,A.
  TITLE     Inhibitory signalling to the Arp2/3 complex steers cell migration
  JOURNAL   Nature 503 (7475), 281-284 (2013)
   PUBMED   24132237
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB285255.1, AC027176.23, BC053602.1, AK055252.1 and BM023230.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the  longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.231591.1,
                                           SRR1660803.240932.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357484.10/ ENSP00000350075.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..226
                     /product="arpin isoform 1"
                     /note="UPF0552 protein C15orf38; arp2/3 inhibition
                     protein"
                     /calculated_mol_wt=24812
     Region          1..224
                     /region_name="UPF0552"
                     /note="Arp2/3-interacting proteins Arpin; pfam10574"
                     /db_xref="CDD:463152"
     Region          211..226
                     /region_name="Necessary and sufficient for interaction
                     with ARPC2. /evidence=ECO:0000269|PubMed:24132237"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6K5.1)"
     CDS             1..226
                     /gene="ARPIN"
                     /gene_synonym="C15orf38"
                     /coded_by="NM_182616.4:118..798"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42080.1"
                     /db_xref="GeneID:348110"
                     /db_xref="HGNC:HGNC:28782"
                     /db_xref="MIM:615543"
ORIGIN      
        1 msriyhdgal rnkavqsvrl pgawdpaahq ggngvllege lidvsrhsil dthgrkeryy
       61 vlyirpshih rrkfdakgne iepnfsatrk vntgflmssy kveakgdtdr ltpealkglv
      121 nkpellalte sltpdhtvaf wmpesemevm elelgagvrl ktrgdgpfld slakleagtv
      181 tkcnftgdgk tgaswtdnim aqkcskgaaa eireqgdgae deewdd
//
LOCUS       NP_001356288             509 aa            linear   ROD 27-APR-2025
DEFINITION  dermokine isoform e precursor [Mus musculus].
ACCESSION   NP_001356288 XP_006540453
VERSION     NP_001356288.1
DBSOURCE    REFSEQ: accession NM_001369359.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Zhang,Y., Zhang,H.W., Zhu,X.D., Wang,Y.Q., Wang,X.W., Zheng,B.S.,
            Chen,B.C. and Chen,Z.J.
  TITLE     Overexpression of Dermokine-alpha enhances the proliferation and
            epithelial-mesenchymal transition of pancreatic tumor cells
  JOURNAL   Cell Signal 99, 110439 (2022)
   PUBMED   35981655
  REMARK    GeneRIF: Overexpression of Dermokine-alpha enhances the
            proliferation and epithelial-mesenchymal transition of pancreatic
            tumor cells.
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Utsunomiya,A., Chino,T., Utsunomiya,N., Luong,V.H., Tokuriki,A.,
            Naganuma,T., Arita,M., Higashi,K., Saito,K., Suzuki,N., Ohara,A.,
            Sugai,M., Sugawara,K., Tsuruta,D., Oyama,N. and Hasegawa,M.
  TITLE     Homeostatic Function of Dermokine in the Skin Barrier and
            Inflammation
  JOURNAL   J Invest Dermatol 140 (4), 838-849 (2020)
   PUBMED   31669414
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Leclerc,E.A., Huchenq,A., Kezic,S., Serre,G. and Jonca,N.
  TITLE     Mice deficient for the epidermal dermokine beta and gamma isoforms
            display transient cornification defects
  JOURNAL   J Cell Sci 127 (Pt 13), 2862-2872 (2014)
   PUBMED   24794495
  REMARK    GeneRIF: Authors improved the knowledge of Dmkn expression in mouse
            and highlighted a role for Dmkn beta and gamma in cornification.
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Hasegawa,M., Higashi,K., Matsushita,T., Hamaguchi,Y., Saito,K.,
            Fujimoto,M. and Takehara,K.
  TITLE     Dermokine inhibits ELR(+)CXC chemokine expression and delays early
            skin wound healing
  JOURNAL   J Dermatol Sci 70 (1), 34-41 (2013)
   PUBMED   23428944
  REMARK    GeneRIF: These results suggest that dermokine-beta delays early
            cutaneous wound healing in part by inhibiting expression of CXC
            chemokines containing the ERL-sequence motif.
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Jheon,A.H., Mostowfi,P., Snead,M.L., Ihrie,R.A., Sone,E.,
            Pramparo,T., Attardi,L.D. and Klein,O.D.
  TITLE     PERP regulates enamel formation via effects on cell-cell adhesion
            and gene expression
  JOURNAL   J Cell Sci 124 (Pt 5), 745-754 (2011)
   PUBMED   21285247
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Naso,M.F., Liang,B., Huang,C.C., Song,X.Y., Shahied-Arruda,L.,
            Belkowski,S.M., D'Andrea,M.R., Polkovitch,D.A., Lawrence,D.R.,
            Griswold,D.E., Sweet,R.W. and Amegadzie,B.Y.
  TITLE     Dermokine: an extensively differentially spliced gene expressed in
            epithelial cells
  JOURNAL   J Invest Dermatol 127 (7), 1622-1631 (2007)
   PUBMED   17380110
  REMARK    GeneRIF: Dermokine gene is expressed in epithelial tissues other
            than the skin and this expression is transcriptionally and
            posttranscriptionally complex.
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Bazzi,H., Fantauzzo,K.A., Richardson,G.D., Jahoda,C.A. and
            Christiano,A.M.
  TITLE     Transcriptional profiling of developing mouse epidermis reveals
            novel patterns of coordinated gene expression
  JOURNAL   Dev Dyn 236 (4), 961-970 (2007)
   PUBMED   17330888
  REMARK    GeneRIF: Drmkn and Krtdap are the highest differentially expressed
            genes in epidermis embryonic development in mice.
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Matsui,T., Hayashi-Kisumi,F., Kinoshita,Y., Katahira,S., Morita,K.,
            Miyachi,Y., Ono,Y., Imai,T., Tanigawa,Y., Komiya,T. and Tsukita,S.
  TITLE     Identification of novel keratinocyte-secreted peptides
            dermokine-alpha/-beta and a new stratified epithelium-secreted
            protein gene complex on human chromosome 19q13.1
  JOURNAL   Genomics 84 (2), 384-397 (2004)
   PUBMED   15234001
  REMARK    GeneRIF: identification of a novel gene (dermokine)giving rise to
            two splicing variants, both of which are expressed in the spinous
            layer of epidermis
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Moffatt,P., Salois,P., St-Amant,N., Gaumond,M.H. and Lanctot,C.
  TITLE     Identification of a conserved cluster of skin-specific genes
            encoding secreted proteins
  JOURNAL   Gene 334, 123-131 (2004)
   PUBMED   15256262
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Takahashi,Y., Miyata,M., Zheng,P., Imazato,T., Horwitz,A. and
            Smith,J.D.
  TITLE     Identification of cAMP analogue inducible genes in RAW264
            macrophages
  JOURNAL   Biochim Biophys Acta 1492 (2-3), 385-394 (2000)
   PUBMED   11004510
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC165340.3.
            
            On Apr 5, 2019 this sequence version replaced XP_006540453.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189676.95040.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 19.24 cM"
     Protein         1..509
                     /product="dermokine isoform e precursor"
                     /note="epidermis-specific secreted protein SK30/SK89"
                     /calculated_mol_wt=49126
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2004
     Region          22..509
                     /region_name="dermokine"
                     /note="cd21118"
                     /db_xref="CDD:411053"
     CDS             1..509
                     /gene="Dmkn"
                     /gene_synonym="1110014F24Rik; C130074A08; cI-36; SK30;
                     SK89"
                     /coded_by="NM_001369359.1:167..1696"
                     /note="isoform e precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:73712"
                     /db_xref="MGI:MGI:1920962"
ORIGIN      
        1 mklqgslacl llalclggga anplhsggeg tgasaahgag daishgigea vgqgakeaas
       61 sgiqnalgqg hgeeggstlm gsrgdvfehr lgeaarslgn agneigrqae diirqgvdav
      121 hnagswgtsg ghgaygsqgg agvqgnpgpq gtpwasggny gtnslggsvg qggnggplny
      181 etnaqgavaq pgygtvrgnn qnsgctnppp sgshesfsns ggssndgsrg sqgshgsngq
      241 gssgrgggqg nsdnngssss ssgsnsgnsn sgnsgnsnsg nsgnsgsgsr gtgsrggsgg
      301 sggsgggnkp ecnnpgndvr maggsgsqes kesshllggs hdyqghgsng gniqkeavng
      361 lntmnsdast lpfnidnfwe nlksktrfin wdainkghap spstrallyf rklwenfkrs
      421 tpffnwkqie gsdlsslqkr aggadqfskp earqdlsads sknyynnqqv nptynwqyyt
      481 kttakagvtp ssssasraqp gllkwlkfw
//
LOCUS       NP_059973                256 aa            linear   PRI 27-APR-2025
DEFINITION  surfeit locus protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_059973
VERSION     NP_059973.4
DBSOURCE    REFSEQ: accession NM_017503.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Vinayagam,A., Stelzl,U., Foulle,R., Plassmann,S., Zenkner,M.,
            Timm,J., Assmus,H.E., Andrade-Navarro,M.A. and Wanker,E.E.
  TITLE     A directed protein interaction network for investigating
            intracellular signal transduction
  JOURNAL   Sci Signal 4 (189), rs8 (2011)
   PUBMED   21900206
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Duhig,T., Ruhrberg,C., Mor,O. and Fried,M.
  TITLE     The human Surfeit locus
  JOURNAL   Genomics 52 (1), 72-78 (1998)
   PUBMED   9740673
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Lennard,A., Gaston,K. and Fried,M.
  TITLE     The Surf-1 and Surf-2 genes and their essential bidirectional
            promoter elements are conserved between mouse and human
  JOURNAL   DNA Cell Biol 13 (11), 1117-1126 (1994)
   PUBMED   7702754
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Yon,J., Jones,T., Garson,K., Sheer,D. and Fried,M.
  TITLE     The organization and conservation of the human Surfeit gene cluster
            and its localization telomeric to the c-abl and can proto-oncogenes
            at chromosome band 9q34.1
  JOURNAL   Hum Mol Genet 2 (3), 237-240 (1993)
   PUBMED   8499913
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP244646.1 and BC014411.1.
            
            On Jul 17, 2013 this sequence version replaced NP_059973.3.
            
            Summary: This gene shares a bidirectional promoter with surfeit 1
            (SURF1; GeneID: 6834), which is located on the opposite strand. It
            encodes a conserved protein that is expressed in a variety of
            tissues. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.148954.1,
                                           SRR5189655.18728.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371964.5/ ENSP00000361032.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2"
     Protein         1..256
                     /product="surfeit locus protein 2 isoform 1"
                     /note="surfeit locus protein 2"
                     /calculated_mol_wt=29486
     Region          5..245
                     /region_name="SURF2"
                     /note="Surfeit locus protein 2 (SURF2); pfam05477"
                     /db_xref="CDD:461659"
     Region          133..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15527.4)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15527.4)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15527.4)"
     CDS             1..256
                     /gene="SURF2"
                     /gene_synonym="SURF-2"
                     /coded_by="NM_017503.5:44..814"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6967.1"
                     /db_xref="GeneID:6835"
                     /db_xref="HGNC:HGNC:11475"
                     /db_xref="MIM:185630"
ORIGIN      
        1 mselpgdvra flrehpslrl qtdarkvrci ltghelpcrl pelqvytrgk kyqrlvrasp
       61 afdyaefeph ivpstknphq lfckltlrhi nkcpehvlrh tqgrryqral ckyeecqkqg
      121 veyvpaclvh rrrrredqmd gdgprpreaf weptssdegg aasddsmtdl yppelftrkd
      181 lgstedgdgt ddfltdkede kakpprekat degrrettvy rglvqkrgkk qlgslkkkfk
      241 shhrkpksfs sckqpg
//
LOCUS       NP_002346                277 aa            linear   PRI 27-APR-2025
DEFINITION  cation-dependent mannose-6-phosphate receptor isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_002346
VERSION     NP_002346.1
DBSOURCE    REFSEQ: accession NM_002355.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Calcagni',A., Staiano,L., Zampelli,N., Minopoli,N., Herz,N.J., Di
            Tullio,G., Huynh,T., Monfregola,J., Esposito,A., Cirillo,C.,
            Bajic,A., Zahabiyon,M., Curnock,R., Polishchuk,E., Parkitny,L.,
            Medina,D.L., Pastore,N., Cullen,P.J., Parenti,G., De Matteis,M.A.,
            Grumati,P. and Ballabio,A.
  TITLE     Loss of the batten disease protein CLN3 leads to mis-trafficking of
            M6PR and defective autophagic-lysosomal reformation
  JOURNAL   Nat Commun 14 (1), 3911 (2023)
   PUBMED   37400440
  REMARK    GeneRIF: Loss of the batten disease protein CLN3 leads to
            mis-trafficking of M6PR and defective autophagic-lysosomal
            reformation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Mihalic,F., Simonetti,L., Giudice,G., Sander,M.R., Lindqvist,R.,
            Peters,M.B.A., Benz,C., Kassa,E., Badgujar,D., Inturi,R., Ali,M.,
            Krystkowiak,I., Sayadi,A., Andersson,E., Aronsson,H., Soderberg,O.,
            Dobritzsch,D., Petsalaki,E., Overby,A.K., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Large-scale phage-based screening reveals extensive pan-viral
            mimicry of host short linear motifs
  JOURNAL   Nat Commun 14 (1), 2409 (2023)
   PUBMED   37100772
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Dai,P., Ruan,P., Mao,Y., Tang,Z., Qiu,X., Bajinka,O. and Tan,Y.
  TITLE     Gimap5 promoted RSV degradation through interaction with M6PR
  JOURNAL   J Med Virol 95 (1), e28390 (2023)
   PUBMED   36484389
  REMARK    GeneRIF: Gimap5 promoted RSV degradation through interaction with
            M6PR.
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Usategui-Martin,R., Perez-Castrillon,J.L., Mansego,M.L.,
            Lara-Hernandez,F., Manzano,I., Briongos,L., Abadia-Otero,J.,
            Martin-Vallejo,J., Garcia-Garcia,A.B., Martin-Escudero,J.C. and
            Chaves,F.J.
  TITLE     Association between genetic variants in oxidative stress-related
            genes and osteoporotic bone fracture. The Hortega follow-up study
  JOURNAL   Gene 809, 146036 (2022)
   PUBMED   34688818
  REMARK    GeneRIF: Association between genetic variants in oxidative
            stress-related genes and osteoporotic bone fracture. The Hortega
            follow-up study.
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Hille-Rehfeld,A.
  TITLE     Mannose 6-phosphate receptors in sorting and transport of lysosomal
            enzymes
  JOURNAL   Biochim Biophys Acta 1241 (2), 177-194 (1995)
   PUBMED   7640295
  REMARK    Review article
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Klumperman,J., Hille,A., Veenendaal,T., Oorschot,V., Stoorvogel,W.,
            von Figura,K. and Geuze,H.J.
  TITLE     Differences in the endosomal distributions of the two mannose
            6-phosphate receptors
  JOURNAL   J Cell Biol 121 (5), 997-1010 (1993)
   PUBMED   8099077
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Klier,H.J., von Figura,K. and Pohlmann,R.
  TITLE     Isolation and analysis of the human 46-kDa mannose 6-phosphate
            receptor gene
  JOURNAL   Eur J Biochem 197 (1), 23-28 (1991)
   PUBMED   1849818
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Watanabe,H., Grubb,J.H. and Sly,W.S.
  TITLE     The overexpressed human 46-kDa mannose 6-phosphate receptor
            mediates endocytosis and sorting of beta-glucuronidase
  JOURNAL   Proc Natl Acad Sci U S A 87 (20), 8036-8040 (1990)
   PUBMED   2172972
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Faust,P.L., Chirgwin,J.M. and Kornfeld,S.
  TITLE     Renin, a secretory glycoprotein, acquires phosphomannosyl residues
  JOURNAL   J Cell Biol 105 (5), 1947-1955 (1987)
   PUBMED   2960682
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Pohlmann,R., Nagel,G., Schmidt,B., Stein,M., Lorkowski,G.,
            Krentler,C., Cully,J., Meyer,H.E., Grzeschik,K.H., Mersmann,G. et
            al.
  TITLE     Cloning of a cDNA encoding the human cation-dependent mannose
            6-phosphate-specific receptor
  JOURNAL   Proc Natl Acad Sci U S A 84 (16), 5575-5579 (1987)
   PUBMED   2441386
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC341018.1, M16985.1 and
            AA648974.1.
            
            Summary: This gene encodes a member of the P-type lectin family.
            P-type lectins play a critical role in lysosome function through
            the specific transport of mannose-6-phosphate-containing acid
            hydrolases from the Golgi complex to lysosomes. The encoded protein
            functions as a homodimer and requires divalent cations for ligand
            binding. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. A pseudogene of
            this gene is located on the long arm of chromosome X. [provided by
            RefSeq, May 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Variants 1, 3, and 14-16 all encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.173024.1,
                                           SRR1803617.184384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000000412.8/ ENSP00000000412.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..277
                     /product="cation-dependent mannose-6-phosphate receptor
                     isoform 1 precursor"
                     /note="46-kDa mannose 6-phosphate receptor; small mannose
                     6-phosphate receptor; Mr 46,000 Man6PR; cation-dependent
                     mannose-6-phosphate receptor; CD Man-6-P receptor"
                     /calculated_mol_wt=27911
     sig_peptide     1..26
                     /note="propagated from UniProtKB/Swiss-Prot (P20645.1)"
                     /calculated_mol_wt=3101
     Region          24..277
                     /region_name="Man-6-P_recep"
                     /note="Mannose-6-phosphate receptor; pfam02157"
                     /db_xref="CDD:460468"
     mat_peptide     27..277
                     /product="Cation-dependent mannose-6-phosphate receptor.
                     /id=PRO_0000019226"
                     /note="propagated from UniProtKB/Swiss-Prot (P20645.1)"
                     /calculated_mol_wt=27911
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20645.1)"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P20645.1)"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20645.1)"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P20645.1)"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20645.1)"
     Site            186..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20645.1)"
     Region          256..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20645.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P24668; propagated from
                     UniProtKB/Swiss-Prot (P20645.1)"
     CDS             1..277
                     /gene="M6PR"
                     /gene_synonym="CD-M6PR; CD-MPR; MPR 46; MPR-46; MPR46;
                     SMPR"
                     /coded_by="NM_002355.4:160..993"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8598.1"
                     /db_xref="GeneID:4074"
                     /db_xref="HGNC:HGNC:6752"
                     /db_xref="MIM:154540"
ORIGIN      
        1 mfpfyscwrt gllllllava vreswqteek tcdlvgekgk esekelalvk rlkplfnksf
       61 estvgqgsdt yiyifrvcre agnhtsgagl vqinksngke tvvgrlneth ifngsnwiml
      121 iykggdeydn hcgkeqrrav vmiscnrhtl adnfnpvsee rgkvqdcfyl femdsslacs
      181 peishlsvgs illvtfaslv avyvvggfly qrlvvgakgm eqfphlafwq dlgnlvadgc
      241 dfvcrskprn vpaayrgvgd dqlgeeseer ddhllpm
//
LOCUS       NP_057349                697 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 12 isoform a [Homo sapiens].
ACCESSION   NP_057349
VERSION     NP_057349.2
DBSOURCE    REFSEQ: accession NM_016265.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Lagou,V., Magi,R., Hottenga,J.J., Grallert,H., Perry,J.R.B.,
            Bouatia-Naji,N., Marullo,L., Rybin,D., Jansen,R., Min,J.L.,
            Dimas,A.S., Ulrich,A., Zudina,L., Gadin,J.R., Jiang,L., Faggian,A.,
            Bonnefond,A., Fadista,J., Stathopoulou,M.G., Isaacs,A.,
            Willems,S.M., Navarro,P., Tanaka,T., Jackson,A.U., Montasser,M.E.,
            O'Connell,J.R., Bielak,L.F., Webster,R.J., Saxena,R.,
            Stafford,J.M., Pourcain,B.S., Timpson,N.J., Salo,P., Shin,S.Y.,
            Amin,N., Smith,A.V., Li,G., Verweij,N., Goel,A., Ford,I.,
            Johnson,P.C.D., Johnson,T., Kapur,K., Thorleifsson,G.,
            Strawbridge,R.J., Rasmussen-Torvik,L.J., Esko,T., Mihailov,E.,
            Fall,T., Fraser,R.M., Mahajan,A., Kanoni,S., Giedraitis,V.,
            Kleber,M.E., Silbernagel,G., Meyer,J., Muller-Nurasyid,M.,
            Ganna,A., Sarin,A.P., Yengo,L., Shungin,D., Luan,J., Horikoshi,M.,
            An,P., Sanna,S., Boettcher,Y., Rayner,N.W., Nolte,I.M., Zemunik,T.,
            Iperen,E.V., Kovacs,P., Hastie,N.D., Wild,S.H., McLachlan,S.,
            Campbell,S., Polasek,O., Carlson,O., Egan,J., Kiess,W.,
            Willemsen,G., Kuusisto,J., Laakso,M., Dimitriou,M., Hicks,A.A.,
            Rauramaa,R., Bandinelli,S., Thorand,B., Liu,Y., Miljkovic,I.,
            Lind,L., Doney,A., Perola,M., Hingorani,A., Kivimaki,M., Kumari,M.,
            Bennett,A.J., Groves,C.J., Herder,C., Koistinen,H.A., Kinnunen,L.,
            Faire,U., Bakker,S.J.L., Uusitupa,M., Palmer,C.N.A., Jukema,J.W.,
            Sattar,N., Pouta,A., Snieder,H., Boerwinkle,E., Pankow,J.S.,
            Magnusson,P.K., Krus,U., Scapoli,C., de Geus,E.J.C.N., Bluher,M.,
            Wolffenbuttel,B.H.R., Province,M.A., Abecasis,G.R., Meigs,J.B.,
            Hovingh,G.K., Lindstrom,J., Wilson,J.F., Wright,A.F.,
            Dedoussis,G.V., Bornstein,S.R., Schwarz,P.E.H., Tonjes,A.,
            Winkelmann,B.R., Boehm,B.O., Marz,W., Metspalu,A., Price,J.F.,
            Deloukas,P., Korner,A., Lakka,T.A., Keinanen-Kiukaanniemi,S.M.,
            Saaristo,T.E., Bergman,R.N., Tuomilehto,J., Wareham,N.J.,
            Langenberg,C., Mannisto,S., Franks,P.W., Hayward,C., Vitart,V.,
            Kaprio,J., Visvikis-Siest,S., Balkau,B., Altshuler,D., Rudan,I.,
            Stumvoll,M., Campbell,H., van Duijn,C.M., Gieger,C., Illig,T.,
            Ferrucci,L., Pedersen,N.L., Pramstaller,P.P., Boehnke,M.,
            Frayling,T.M., Shuldiner,A.R., Peyser,P.A., Kardia,S.L.R.,
            Palmer,L.J., Penninx,B.W., Meneton,P., Harris,T.B., Navis,G.,
            Harst,P.V., Smith,G.D., Forouhi,N.G., Loos,R.J.F., Salomaa,V.,
            Soranzo,N., Boomsma,D.I., Groop,L., Tuomi,T., Hofman,A.,
            Munroe,P.B., Gudnason,V., Siscovick,D.S., Watkins,H., Lecoeur,C.,
            Vollenweider,P., Franco-Cereceda,A., Eriksson,P., Jarvelin,M.R.,
            Stefansson,K., Hamsten,A., Nicholson,G., Karpe,F.,
            Dermitzakis,E.T., Lindgren,C.M., McCarthy,M.I., Froguel,P.,
            Kaakinen,M.A., Lyssenko,V., Watanabe,R.M., Ingelsson,E.,
            Florez,J.C., Dupuis,J., Barroso,I., Morris,A.P. and Prokopenko,I.
  CONSRTM   Meta-Analyses of Glucose and Insulin-related traits Consortium
            (MAGIC)
  TITLE     Sex-dimorphic genetic effects and novel loci for fasting glucose
            and insulin variability
  JOURNAL   Nat Commun 12 (1), 24 (2021)
   PUBMED   33402679
  REMARK    GeneRIF: Sex-dimorphic genetic effects and novel loci for fasting
            glucose and insulin variability.
            Erratum:[Nat Commun. 2021 Feb 8;12(1):995. doi:
            10.1038/s41467-021-21276-3. PMID: 33558525]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 697)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   4  (residues 1 to 697)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   5  (residues 1 to 697)
  AUTHORS   Zhao,Y., Zhou,L., Liu,B., Deng,Y., Wang,Y., Wang,Y., Huang,W.,
            Yuan,W., Wang,Z., Zhu,C., Liu,M., Wu,X. and Li,Y.
  TITLE     ZNF325, a novel human zinc finger protein with a RBaK-like
            RB-binding domain, inhibits AP-1- and SRE-mediated transcriptional
            activity
  JOURNAL   Biochem Biophys Res Commun 346 (4), 1191-1199 (2006)
   PUBMED   16806083
  REMARK    GeneRIF: A zinc finger protein with a RBaK-like RB-binding domain,
            inhibits AP-1- and SRE-mediated transcriptional activity
REFERENCE   6  (residues 1 to 697)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
REFERENCE   7  (residues 1 to 697)
  AUTHORS   Seite,P., Huebner,K., Rousseau-Merck,M.F., Berger,R. and
            Thiesen,H.J.
  TITLE     Two human genes encoding zinc finger proteins, ZNF 12 (KOX 3) and
            ZNF 26 (KOX 20), map to chromosome 7p22-p21 and 12q24.33,
            respectively
  JOURNAL   Hum Genet 86 (6), 585-590 (1991)
   PUBMED   2026422
REFERENCE   8  (residues 1 to 697)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073343.6, AI879099.1,
            AF505656.1, BC051892.1 and BX114779.1.
            
            On May 20, 2005 this sequence version replaced NP_057349.1.
            
            Summary: This gene is a member of the krueppel C2H2-type
            zinc-finger protein family and encodes a protein with eight
            C2H2-type zinc fingers and a KRAB domain. This nuclear protein is
            involved in developmental control of gene expression. Alternate
            transcriptional splice variants, encoding different isoforms, have
            been characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC154414.1, DRR138524.1162568.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000405858.6/ ENSP00000385939.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..697
                     /product="zinc finger protein 12 isoform a"
                     /note="zinc finger protein 325; gonadotropin inducible
                     transcription repressor 3; zinc finger protein 11; zinc
                     finger protein KOX3; gonadotropin-inducible ovary
                     transcription repressor 3"
                     /calculated_mol_wt=81071
     Region          8..68
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          271..291
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          287..306
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          299..319
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          307..683
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          327..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(332,334,336,338..339,342..343,346,360,362,366..367,
                     370..371,374,388,390,392,394..395,398..399,402)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          355..375
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          383..403
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..459
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          467..487
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(472,474,476,478..479,482..483,486,500,502,506..507,
                     510..511,514,528,530,532,534..535,538..539,542)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          495..515
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          523..543
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          551..571
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          579..599
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(584,586,588,590..591,594..595,598,612,614,618..619,
                     622..623,626,640,642,644,646..647,650..651,654)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          607..627
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          635..655
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          663..683
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..697
                     /gene="ZNF12"
                     /gene_synonym="GIOT-3; HZF11; KOX3; ZNF325"
                     /coded_by="NM_016265.4:567..2660"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47538.1"
                     /db_xref="GeneID:7559"
                     /db_xref="HGNC:HGNC:12902"
                     /db_xref="MIM:194536"
ORIGIN      
        1 mnkslgpvsf kdvavdftqe ewqqldpeqk ityrdvmlen ysnlvsvgyh iikpdviskl
       61 eqgeepwive gefllqsypd evwqtddlie riqeeenkps rqtvfietli eergnvpgkt
      121 fdvetnpvps rkiayknslc dscekcltsv seyissdgsy armkadecsg cgksllhikl
      181 ekthpgdqay efnqngepyt lneeslyqki rilekpfeyi ecqkafqkdt vfvnhmeekp
      241 ykwngseiaf lqmsdltvhq tshmemkpye csecgksfck kskfiihqrt htgekpyecn
      301 qcgksfcqkg tltvhqrtht gekpyecnec gknfyqklhl iqhqrthsge kpyecsycgk
      361 sfcqkthltq hqrthsgerp yvchdcgktf sqksalndhq kihtgvklyk csecgkcfcr
      421 kstltthlrt htgekpyecn ecgkffsrls yltvhyrths gekpyecnec gktfylnsal
      481 mrhqrvhtge kpyecnecgk lfsqlsylti hhrthsgvkp yecsecgktf yqnsalcrhr
      541 rihkgekpye cyicgkffsq msyltihhri hsgekpyecs ecgktfcqns alnrhqrtht
      601 gekayecyec gkcfsqmsyl tihhrihsge kpfecnecgk afsrmsyltv hyrthsgekp
      661 yectecgkkf yhksafnshq rihrrgnmnv idvgrll
//
LOCUS       NP_065715                292 aa            linear   PRI 27-APR-2025
DEFINITION  peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]
            [Homo sapiens].
ACCESSION   NP_065715
VERSION     NP_065715.1
DBSOURCE    REFSEQ: accession NM_020664.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Mah,C.Y., Nguyen,A.D.T., Niijima,T., Helm,M., Dehairs,J.,
            Ryan,F.J., Ryan,N., Quek,L.E., Hoy,A.J., Don,A.S., Mills,I.G.,
            Swinnen,J.V., Lynn,D.J., Nassar,Z.D. and Butler,L.M.
  TITLE     Peroxisomal beta-oxidation enzyme, DECR2, regulates lipid
            metabolism and promotes treatment resistance in advanced prostate
            cancer
  JOURNAL   Br J Cancer 130 (5), 741-754 (2024)
   PUBMED   38216720
  REMARK    GeneRIF: Peroxisomal beta-oxidation enzyme, DECR2, regulates lipid
            metabolism and promotes treatment resistance in advanced prostate
            cancer.
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   7  (residues 1 to 292)
  AUTHORS   De Nys,K., Meyhi,E., Mannaerts,G.P., Fransen,M. and Van
            Veldhoven,P.P.
  TITLE     Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase
  JOURNAL   Biochim Biophys Acta 1533 (1), 66-72 (2001)
   PUBMED   11514237
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Daniels,R.J., Peden,J.F., Lloyd,C., Horsley,S.W., Clark,K.,
            Tufarelli,C., Kearney,L., Buckle,V.J., Doggett,N.A., Flint,J. and
            Higgs,D.R.
  TITLE     Sequence, structure and pathology of the fully annotated terminal 2
            Mb of the short arm of human chromosome 16
  JOURNAL   Hum Mol Genet 10 (4), 339-352 (2001)
   PUBMED   11157797
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Das,A.K., Uhler,M.D. and Hajra,A.K.
  TITLE     Molecular cloning and expression of mammalian peroxisomal
            trans-2-enoyl-coenzyme A reductase cDNAs
  JOURNAL   J Biol Chem 275 (32), 24333-24340 (2000)
   PUBMED   10811639
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC010740.1 and BC030226.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.814114.1, BC010740.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219481.10/ ENSP00000219481.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..292
                     /product="peroxisomal 2,4-dienoyl-CoA reductase
                     [(3E)-enoyl-CoA-producing]"
                     /EC_number="1.3.1.124"
                     /note="peroxisomal 2,4-dienoyl-CoA reductase; short chain
                     dehydrogenase/reductase family 17C member 1;
                     2,4-dienoyl-CoA reductase 2, peroxisomal"
                     /calculated_mol_wt=30647
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NUI1.1)"
     Region          26..273
                     /region_name="TER_DECR_SDR_a"
                     /note="Trans-2-enoyl-CoA reductase (TER) and
                     2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR;
                     cd05369"
                     /db_xref="CDD:187627"
     Site            order(35,38..40,59..61,85..88,113..115,136,163..165,182,
                     208..211,213)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            order(60,88,115..118,126,128..129,132,165,167,178,210)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            order(90,121..123,125..127,130..131,134,138..139,142..143,
                     146,150,153,157,167,171..174,176,179..180,183..184,
                     187..188,190..197,199,210,234..236,238..240,244,247..248,
                     251,256,258..263,265..273)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
     Site            order(117,167,178,182)
                     /site_type="active"
                     /db_xref="CDD:187627"
     Site            order(121..123,125,130..131,134,139,142..143,171..174,176,
                     179..180,183..184,187..188,191,194..195)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
     Site            151
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NUI1.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NUI1.1)"
     Region          290..292
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUI1.1)"
     Site            291
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NUI1.1)"
     CDS             1..292
                     /gene="DECR2"
                     /gene_synonym="PDCR; SDR17C1"
                     /coded_by="NM_020664.4:80..958"
                     /db_xref="CCDS:CCDS10409.1"
                     /db_xref="GeneID:26063"
                     /db_xref="HGNC:HGNC:2754"
                     /db_xref="MIM:615839"
ORIGIN      
        1 maqpppdveg ddclpayrhl fcpdllrdkv afitgggsgi gfriaeifmr hgchtviasr
       61 slprvltaar klagatgrrc lplsmdvrap pavmaavdqa lkefgridil incaagnflc
      121 pagalsfnaf ktvmdidtsg tfnvsrvlye kffrdhggvi vnitatlgnr gqalqvhags
      181 akaavdamtr hlavewgpqn irvnslapgp isgteglrrl ggpqaslstk vtasplqrlg
      241 nkteiahsvl ylasplasyv tgavlvadgg awltfpngvk glpdfasfsa kl
//
LOCUS       NP_001357021             261 aa            linear   PRI 27-APR-2025
DEFINITION  gap junction beta-6 protein [Homo sapiens].
ACCESSION   NP_001357021
VERSION     NP_001357021.1
DBSOURCE    REFSEQ: accession NM_001370092.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   O'Shaughnessy,E.M., Duffy,W., Garcia-Vega,L., Hussey,K.,
            Burden,A.D., Zamiri,M. and Martin,P.E.
  TITLE     Dysregulation of Connexin Expression Plays a Pivotal Role in
            Psoriasis
  JOURNAL   Int J Mol Sci 22 (11), 6060 (2021)
   PUBMED   34199748
  REMARK    GeneRIF: Dysregulation of Connexin Expression Plays a Pivotal Role
            in Psoriasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Buonfiglio,P., Bruque,C.D., Luce,L., Giliberto,F., Lotersztein,V.,
            Menazzi,S., Paoli,B., Elgoyhen,A.B. and Dalamon,V.
  TITLE     GJB2 and GJB6 Genetic Variant Curation in an Argentinean
            Non-Syndromic Hearing-Impaired Cohort
  JOURNAL   Genes (Basel) 11 (10), 1233 (2020)
   PUBMED   33096615
  REMARK    GeneRIF: GJB2 and GJB6 Genetic Variant Curation in an Argentinean
            Non-Syndromic Hearing-Impaired Cohort.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Zhan,Y., Luo,S., Pi,Z. and Zhang,G.
  TITLE     A recurrent mutation of GJB6 in a big Chinese family with Hidrotic
            ectodermal dysplasia
  JOURNAL   Hereditas 157 (1), 34 (2020)
   PUBMED   32843087
  REMARK    GeneRIF: A recurrent mutation of GJB6 in a big Chinese family with
            Hidrotic ectodermal dysplasia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Eggena,M., Targan,S.R., Iwanczyk,L., Vidrich,A., Gordon,L.K. and
            Braun,J.
  TITLE     Phage display cloning and characterization of an immunogenetic
            marker (perinuclear anti-neutrophil cytoplasmic antibody) in
            ulcerative colitis
  JOURNAL   J Immunol 156 (10), 4005-4011 (1996)
   PUBMED   8621942
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Kibar,Z., Der Kaloustian,V.M., Brais,B., Hani,V., Fraser,F.C. and
            Rouleau,G.A.
  TITLE     The gene responsible for Clouston hidrotic ectodermal dysplasia
            maps to the pericentromeric region of chromosome 13q
  JOURNAL   Hum Mol Genet 5 (4), 543-547 (1996)
   PUBMED   8845850
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Stoppini,M., Bellotti,V., Negri,A., Merlini,G., Garver,F. and
            Ferri,G.
  TITLE     Characterization of the two unique human anti-flavin monoclonal
            immunoglobulins
  JOURNAL   Eur J Biochem 228 (3), 886-893 (1995)
   PUBMED   7737190
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Smith,R.J.H. and Ranum,P.T.
  TITLE     Nonsyndromic Hearing Loss and Deafness, DFNA3 - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301708
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Smith,R.J.H., Azaiez,H. and Booth,K.
  TITLE     GJB2-Related Autosomal Recessive Nonsyndromic Hearing Loss
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301449
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Mellerio,J. and Greenblatt,D.
  TITLE     Hidrotic Ectodermal Dysplasia 2
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301379
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355984.11.
            
            Summary: Gap junctions allow the transport of ions and metabolites
            between the cytoplasm of adjacent cells. They are formed by two
            hemichannels, made up of six connexin proteins assembled in groups.
            Each connexin protein has four transmembrane segments, two
            extracellular loops, a cytoplasmic loop formed between the two
            inner transmembrane segments, and the N- and C-terminus both being
            in the cytoplasm. The specificity of the gap junction is determined
            by which connexin proteins comprise the hemichannel. In the past,
            connexin protein names were based on their molecular weight,
            however the new nomenclature uses sequential numbers based on which
            form (alpha or beta) of the gap junction is present. This gene
            encodes one of the connexin proteins. Mutations in this gene have
            been found in some forms of deafness and in some families with
            hidrotic ectodermal dysplasia. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.256616.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147975, SAMEA2156670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..261
                     /product="gap junction beta-6 protein"
                     /note="ectodermal dysplasia 2, hidrotic (Clouston
                     syndrome); connexin 30; gap junction protein, beta 6,
                     30kDa"
                     /calculated_mol_wt=30256
     Region          2..215
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            23..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     Site            76..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     Site            132..154
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     Site            193..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95452.2)"
     CDS             1..261
                     /gene="GJB6"
                     /gene_synonym="CX30; DFNA3; DFNA3B; DFNB1B; ECTD2; ED2;
                     EDH; HED; HED2"
                     /coded_by="NM_001370092.1:643..1428"
                     /db_xref="CCDS:CCDS9291.1"
                     /db_xref="GeneID:10804"
                     /db_xref="HGNC:HGNC:4288"
                     /db_xref="MIM:604418"
ORIGIN      
        1 mdwgtlhtfi ggvnkhstsi gkvwitvifi frvmilvvaa qevwgdeqed fvcntlqpgc
       61 knvcydhffp vshirlwalq lifvstpall vamhvayyrh ettrkfrrge krndfkdied
      121 ikkqkvrieg slwwtytssi ffriifeaaf myvfyflyng yhlpwvlkcg idpcpnlvdc
      181 fisrptektv ftifmisasv icmllnvael cylllkvcfr rskraqtqkn hpnhalkesk
      241 qnemnelisd sgqnaitgfp s
//
LOCUS       NP_059963                145 aa            linear   PRI 27-APR-2025
DEFINITION  OTU domain-containing protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_059963 NP_055743
VERSION     NP_059963.1
DBSOURCE    REFSEQ: accession NM_017493.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Li,Z., Tian,Y., Zong,H., Wang,X., Li,D., Keranmu,A., Xin,S., Ye,B.,
            Bai,R., Chen,W., Yang,G., Ye,L. and Wang,S.
  TITLE     Deubiquitinating enzyme OTUD4 stabilizes RBM47 to induce ATF3
            transcription: a novel mechanism underlying the restrained
            malignant properties of ccRCC cells
  JOURNAL   Apoptosis 29 (7-8), 1051-1069 (2024)
   PUBMED   38553613
  REMARK    GeneRIF: Deubiquitinating enzyme OTUD4 stabilizes RBM47 to induce
            ATF3 transcription: a novel mechanism underlying the restrained
            malignant properties of ccRCC cells.
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Hu,S., Yuan,Y., Yan,R., Xie,H., Cai,R. and Xu,J.
  TITLE     NRF2 regulates EGF stability through OTUD4 in lung adenocarcinoma
  JOURNAL   Biochem Biophys Res Commun 708, 149798 (2024)
   PUBMED   38518721
  REMARK    GeneRIF: NRF2 regulates EGF stability through OTUD4 in lung
            adenocarcinoma.
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Ci,M., Zhao,G., Li,C., Liu,R., Hu,X., Pan,J., Shen,Y., Zhang,G.,
            Li,Y., Zhang,L., Liang,P. and Cui,H.
  TITLE     OTUD4 promotes the progression of glioblastoma by deubiquitinating
            CDK1 and activating MAPK signaling pathway
  JOURNAL   Cell Death Dis 15 (3), 179 (2024)
   PUBMED   38429268
  REMARK    GeneRIF: OTUD4 promotes the progression of glioblastoma by
            deubiquitinating CDK1 and activating MAPK signaling pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Ma,X., Wan,R., Wen,Y., Liu,T., Song,Y. and Zhu,Y.
  TITLE     Deubiquitinating enzyme OTUD4 regulates metastasis in
            triple-negative breast cancer by stabilizing Snail1
  JOURNAL   Exp Cell Res 434 (1), 113864 (2024)
   PUBMED   38040050
  REMARK    GeneRIF: Deubiquitinating enzyme OTUD4 regulates metastasis in
            triple-negative breast cancer by stabilizing Snail1.
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Gao,Y., Tang,J., Ma,X., Zhang,C., Huang,L., Che,J., Wen,Y.,
            Zhang,Y., Zhu,Y., Liu,T. and Zhang,H.
  TITLE     OTUD4 regulates metastasis and chemoresistance in melanoma by
            stabilizing Snail1
  JOURNAL   J Cell Physiol 238 (11), 2546-2555 (2023)
   PUBMED   37642406
  REMARK    GeneRIF: OTUD4 regulates metastasis and chemoresistance in melanoma
            by stabilizing Snail1.
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Zhao,Y., Majid,M.C., Soll,J.M., Brickner,J.R., Dango,S. and
            Mosammaparast,N.
  TITLE     Noncanonical regulation of alkylation damage resistance by the
            OTUD4 deubiquitinase
  JOURNAL   EMBO J 34 (12), 1687-1703 (2015)
   PUBMED   25944111
  REMARK    GeneRIF: OTUD4 is a positive regulator of ALKBH2 and ALKBH3, two
            DNA demethylases critical for alkylation repair.
REFERENCE   7  (residues 1 to 145)
  AUTHORS   Mevissen,T.E., Hospenthal,M.K., Geurink,P.P., Elliott,P.R.,
            Akutsu,M., Arnaudo,N., Ekkebus,R., Kulathu,Y., Wauer,T., El
            Oualid,F., Freund,S.M., Ovaa,H. and Komander,D.
  TITLE     OTU deubiquitinases reveal mechanisms of linkage specificity and
            enable ubiquitin chain restriction analysis
  JOURNAL   Cell 154 (1), 169-184 (2013)
   PUBMED   23827681
REFERENCE   8  (residues 1 to 145)
  AUTHORS   Margolin,D.H., Kousi,M., Chan,Y.M., Lim,E.T., Schmahmann,J.D.,
            Hadjivassiliou,M., Hall,J.E., Adam,I., Dwyer,A., Plummer,L.,
            Aldrin,S.V., O'Rourke,J., Kirby,A., Lage,K., Milunsky,A.,
            Milunsky,J.M., Chan,J., Hedley-Whyte,E.T., Daly,M.J., Katsanis,N.
            and Seminara,S.B.
  TITLE     Ataxia, dementia, and hypogonadotropism caused by disordered
            ubiquitination
  JOURNAL   N Engl J Med 368 (21), 1992-2003 (2013)
   PUBMED   23656588
  REMARK    GeneRIF: The syndrome of hypogonadotropic hypogonadism, ataxia, and
            dementia can be caused by inactivating mutations in RNF216 or by
            the combination of mutations in RNF216 and OTUD4
REFERENCE   9  (residues 1 to 145)
  AUTHORS   Li,S., Zheng,H., Mao,A.P., Zhong,B., Li,Y., Liu,Y., Gao,Y., Ran,Y.,
            Tien,P. and Shu,H.B.
  TITLE     Regulation of virus-triggered signaling by OTUB1- and
            OTUB2-mediated deubiquitination of TRAF3 and TRAF6
  JOURNAL   J Biol Chem 285 (7), 4291-4297 (2010)
   PUBMED   19996094
REFERENCE   10 (residues 1 to 145)
  AUTHORS   Raineri,I. and Senn,H.P.
  TITLE     HIV-1 promotor insertion revealed by selective detection of
            chimeric provirus-host gene transcripts
  JOURNAL   Nucleic Acids Res 20 (23), 6261-6266 (1992)
   PUBMED   1475186
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X68242.1 and AC096757.3.
            
            On Dec 1, 2003 this sequence version replaced NP_055743.1.
            
            Summary: Alternatively spliced transcript variants have been found
            for this gene. The smaller protein isoform encoded by the shorter
            transcript variant is found only in HIV-1 infected cells. [provided
            by RefSeq, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X68242.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.21"
     Protein         1..145
                     /product="OTU domain-containing protein 4 isoform 2"
                     /EC_number="3.4.19.12"
                     /note="OTU domain-containing protein 4; HIV-1 induced
                     protein HIN-1"
                     /calculated_mol_wt=16905
     Region          <1..89
                     /region_name="OTU"
                     /note="OTU (ovarian tumor) domain family; cl45892"
                     /db_xref="CDD:459237"
     Site            order(25,28,35..38,64,66,78,82..84)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:438615"
     CDS             1..145
                     /gene="OTUD4"
                     /gene_synonym="DUBA6; HIN1; HSHIN1"
                     /coded_by="NM_017493.7:68..505"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3764.1"
                     /db_xref="GeneID:54726"
                     /db_xref="HGNC:HGNC:24949"
                     /db_xref="MIM:611744"
ORIGIN      
        1 macihylren rekfeafieg sfeeylkrle npqewvgqve isalslmyrk dfiiyrepnv
       61 spsqvtennf pekvllcfsn gnhydivypi kykessamcq sllyellyek vfktdvskiv
      121 meldtlevad ednseisdse ddsck
//
LOCUS       NP_942568               1250 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 9B isoform a [Homo sapiens].
ACCESSION   NP_942568 XP_371792
VERSION     NP_942568.2
DBSOURCE    REFSEQ: accession NM_198868.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1250)
  AUTHORS   Liao,Y., Li,M., Chen,X., Jiang,Y. and Yin,X.M.
  TITLE     Interaction of TBC1D9B with Mammalian ATG8 Homologues Regulates
            Autophagic Flux
  JOURNAL   Sci Rep 8 (1), 13496 (2018)
   PUBMED   30202024
  REMARK    GeneRIF: Study found that TBC1D9B, a GTPase activating protein for
            RAB11A, interacted with LC3B. TBC1D9B could also interact with
            other mammalian ATG8 homologues and revealed that TBC1D9B can
            positively regulate autophagic flux, possibly through its GTPase
            activity to inactivate RAB11A, facilitating the proper destination
            of the autophagosomes to the degradation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1250)
  AUTHORS   Popovic,D., Akutsu,M., Novak,I., Harper,J.W., Behrends,C. and
            Dikic,I.
  TITLE     Rab GTPase-activating proteins in autophagy: regulation of
            endocytic and autophagy pathways by direct binding to human ATG8
            modifiers
  JOURNAL   Mol Cell Biol 32 (9), 1733-1744 (2012)
   PUBMED   22354992
REFERENCE   3  (residues 1 to 1250)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   4  (residues 1 to 1250)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010285.4 and AC008393.7.
            
            On Mar 19, 2004 this sequence version replaced NP_942568.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.227798.1,
                                           SRR1803611.128859.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..1250
                     /product="TBC1 domain family member 9B isoform a"
                     /note="TBC1 domain family, member 9B (with GRAM domain)"
                     /calculated_mol_wt=140394
     Region          153..251
                     /region_name="PH-GRAM1_TCB1D9_TCB1D9B"
                     /note="TBC1 domain family members 9 and 9B (TBC1D9 and
                     TBC1D9B) Pleckstrin Homology-Glucosyltransferases,
                     Rab-like GTPase activators and Myotubularins (PH-GRAM)
                     domain, repeat 1; cd13351"
                     /db_xref="CDD:275420"
     Region          299..394
                     /region_name="PH-GRAM2_TCB1D9_TCB1D9B"
                     /note="TBC1 domain family members 9 and 9B (TBC1D9 and
                     TBC1D9B) Pleckstrin Homology-Glucosyltransferases,
                     Rab-like GTPase activators and Myotubularins (PH-GRAM)
                     domain, repeat 2; cd13354"
                     /db_xref="CDD:270161"
     Region          397..443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66K14.3)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q66K14.3)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q66K14.3)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q66K14.3)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q66K14.3)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q66K14.3)"
     Region          505..715
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            555
                     /site_type="other"
                     /note="Arginine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q66K14.3)"
     Site            594
                     /site_type="other"
                     /note="Glutamine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q66K14.3)"
     Site            668..688
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66K14.3)"
     Region          886..911
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; smart00054"
                     /db_xref="CDD:197492"
     Region          974..999
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66K14.3)"
     Region          1069..1093
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66K14.3)"
     Region          1128..1157
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66K14.3)"
     Site            1241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q66K14.3)"
     CDS             1..1250
                     /gene="TBC1D9B"
                     /gene_synonym="GRAMD9B"
                     /coded_by="NM_198868.3:77..3829"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43408.1"
                     /db_xref="GeneID:23061"
                     /db_xref="HGNC:HGNC:29097"
                     /db_xref="MIM:618039"
ORIGIN      
        1 mwlspeevlv analwvtera npffvlqrrr ghgrgggltg llvgtldvvl dssarvapyr
       61 ilhqtqdsqv ywtvacgssr keitkhwewl ennllqtlsi fdseedittf vkgkihgiia
      121 eenknlqpqg dedpgkfkea elkmrkqfgm pegeklvnyy scsywkgrvp rqgwlyltvn
      181 hlcfysfllg kevslvvqwv ditrleknat llfpesirvd trdqelffsm flnigetfkl
      241 meqlanlamr qlldsegfle dkalprpirp hrnisalkrd ldaraknecy ratfrlprde
      301 rldghtsctl wtpfnklhip gqmfisnnyi cfaskeedac hliiplrevt ivekadsssv
      361 lpsplsistk skmtflfanl kdrdflvqri sdflqktpsk qpgsigsrka svvdpstess
      421 papqegseqp aspasplssr qsfcaqeapt asqgllklfq knspmedlga kgakekmkee
      481 swhihffeyg rgvcmyrtak tralvlkgip eslrgelwll fsgawnemvt hpgyyaelve
      541 kstgkyslat eeierdlhrs mpehpafqne lgiaalrrvl tayafrnpti gycqamnivt
      601 svlllygsee eafwllvalc ermlpdyynt rvvgalvdqg ifeeltrdfl pqlsekmqdl
      661 gvissislsw fltlflsvmp fesavvivdc ffyegikvil qvalavldan meqllgcsde
      721 geamtmlgry ldnvvnkqsv sppiphlral lsssddppae vdifellkvs yekfsslrae
      781 dieqmrfkqr lkviqsledt akrsvvraip vdigfsieel edlymvfkak hlasqywgcs
      841 rtmagrrdps lpyleqyrid asqfrelfas ltpwacgsht pllagrmfrl ldenkdslin
      901 fkefvtgmsg myhgdltekl kvlyklhlpp alspeeaesa leaahyfted ssseasplas
      961 dldlflpwea qealpqeeqe gsgseergee kgtsspdyrh ylrmwakeke aqketikdlp
     1021 kmnqeqfiel cktlynmfse dpmeqdlyha iatvaslllr igevgkkfsa rtgrkprdca
     1081 teedeppape lhqdaarelq ppaagdpqak aggdthlgka pqesqvvveg gsgegqgsps
     1141 qllsddetkd dmsmssysvv stgslqcedl addtvlvgge acsptarigg tvdtdwcisf
     1201 eqilasilte svlvnffekr vdiglkikdq kkverqfsta sdheqpgvsg
//
LOCUS       NP_055815                464 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein kinase 38-like [Homo sapiens].
ACCESSION   NP_055815
VERSION     NP_055815.1
DBSOURCE    REFSEQ: accession NM_015000.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Levallet,J., Biojout,T., Bazille,C., Douyere,M., Dubois,F.,
            Ferreira,D.L., Taylor,J., Teulier,S., Toutain,J., Elie,N.,
            Bernaudin,M., Valable,S., Bergot,E. and Levallet,G.
  TITLE     Hypoxia-induced activation of NDR2 underlies brain metastases from
            Non-Small Cell Lung Cancer
  JOURNAL   Cell Death Dis 14 (12), 823 (2023)
   PUBMED   38092743
  REMARK    GeneRIF: Hypoxia-induced activation of NDR2 underlies brain
            metastases from Non-Small Cell Lung Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Yang,Y., Zhu,Y., Zhou,S., Tang,P., Xu,R., Zhang,Y., Wei,D., Wen,J.,
            Thorne,R.F., Zhang,X.D., Guan,J.L., Liu,L., Wu,M. and Chen,S.
  TITLE     TRIM27 cooperates with STK38L to inhibit ULK1-mediated autophagy
            and promote tumorigenesis
  JOURNAL   EMBO J 41 (14), e109777 (2022)
   PUBMED   35670107
  REMARK    GeneRIF: TRIM27 cooperates with STK38L to inhibit ULK1-mediated
            autophagy and promote tumorigenesis.
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Devroe,E., Silver,P.A. and Engelman,A.
  TITLE     HIV-1 incorporates and proteolytically processes human NDR1 and
            NDR2 serine-threonine kinases
  JOURNAL   Virology 331 (1), 181-189 (2005)
   PUBMED   15582665
  REMARK    GeneRIF: The NDR1 and NDR2 kinases were incorporated into HIV-1
            particles and were cleaved by the HIV-1 protease.
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Bichsel,S.J., Tamaskovic,R., Stegert,M.R. and Hemmings,B.A.
  TITLE     Mechanism of activation of NDR (nuclear Dbf2-related) protein
            kinase by the hMOB1 protein
  JOURNAL   J Biol Chem 279 (34), 35228-35235 (2004)
   PUBMED   15197186
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Devroe,E., Erdjument-Bromage,H., Tempst,P. and Silver,P.A.
  TITLE     Human Mob proteins regulate the NDR1 and NDR2 serine-threonine
            kinases
  JOURNAL   J Biol Chem 279 (23), 24444-24451 (2004)
   PUBMED   15067004
  REMARK    GeneRIF: NDR1 and NDR2 serine-threonine kinases are regulated by
            mob proteins
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Stegert,M.R., Tamaskovic,R., Bichsel,S.J., Hergovich,A. and
            Hemmings,B.A.
  TITLE     Regulation of NDR2 protein kinase by multi-site phosphorylation and
            the S100B calcium-binding protein
  JOURNAL   J Biol Chem 279 (22), 23806-23812 (2004)
   PUBMED   15037617
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB023182.2, BX390969.1 and BU681056.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB023182.2, SRR1660807.139823.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389032.8/ ENSP00000373684.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.23"
     Protein         1..464
                     /product="serine/threonine-protein kinase 38-like"
                     /EC_number="2.7.11.1"
                     /note="nuclear Dbf2-related 2; NDR2 protein kinase;
                     nuclear Dbf2-related kinase 2"
                     /calculated_mol_wt=53872
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8;
                     propagated from UniProtKB/Swiss-Prot (Q9Y2H1.3)"
     Region          12..86
                     /region_name="MobB_NDR_LATS-like"
                     /note="Mob-binding domain found in the NDR/LATS family
                     serine/threonine protein kinases; cl45907"
                     /db_xref="CDD:459252"
     Site            order(24..25,27..29,31..32,35..36,39,42,46,71,74..76,
                     78..79,82..83)
                     /site_type="other"
                     /note="Mob binding site [polypeptide binding]"
                     /db_xref="CDD:439267"
     Region          63..88
                     /region_name="S100B binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2H1.3)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:15037617; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2H1.3)"
     Region          87..452
                     /region_name="STKc_NDR2"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Nuclear Dbf2-Related kinase 2; cd05627"
                     /db_xref="CDD:270776"
     Site            order(96..100,104,117,119,151,167..168,170,174,176,213,
                     215,217..218,220,230..231,234,283..288,315,321,324)
                     /site_type="active"
                     /db_xref="CDD:270776"
     Site            order(96..100,104,117,119,151,168..170,174,213,215,
                     217..218,220,230..231)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270776"
     Site            order(100,174,176,213,215,217,234,283..288,315,321,324)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270776"
     Site            order(230..242,279..288)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270776"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15037617; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2H1.3)"
     Site            438..443
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270776"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by STK24/MST3.
                     /evidence=ECO:0000269|PubMed:15037617,
                     ECO:0000269|PubMed:16314523; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2H1.3)"
     CDS             1..464
                     /gene="STK38L"
                     /gene_synonym="NDR2"
                     /coded_by="NM_015000.4:59..1453"
                     /db_xref="CCDS:CCDS31761.1"
                     /db_xref="GeneID:23012"
                     /db_xref="HGNC:HGNC:17848"
                     /db_xref="MIM:615836"
ORIGIN      
        1 mamtagtttt fpmsnhtrer vtvakltlen fysnlilqhe eretrqkkle vameeeglad
       61 eekklrrsqh arketeflrl krtrlglddf eslkvigrga fgevrlvqkk dtghiyamki
      121 lrksdmleke qvahiraerd ilveadgawv vkmfysfqdk rnlylimefl pggdmmtllm
      181 kkdtlteeet qfyisetvla idaihqlgfi hrdikpdnll ldakghvkls dfglctglkk
      241 ahrtefyrnl thnppsdfsf qnmnskrkae twkknrrqla ystvgtpdyi apevfmqtgy
      301 nklcdwwslg vimyemligy ppfcsetpqe tyrkvmnwke tlvfppevpi sekakdlilr
      361 fcidsenrig nsgveeikgh pffegvdweh irerpaaipi eiksiddtsn fddfpesdil
      421 qpvpnttepd ykskdwvfln ytykrfeglt qrgsiptymk agkl
//
LOCUS       NP_001489                637 aa            linear   PRI 27-APR-2025
DEFINITION  glutamate--cysteine ligase catalytic subunit isoform a [Homo
            sapiens].
ACCESSION   NP_001489
VERSION     NP_001489.1
DBSOURCE    REFSEQ: accession NM_001498.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Xu,C., Bian,Z., Wang,X., Niu,N., Liu,L., Xiao,Y., Zhu,J., Huang,N.,
            Zhang,Y., Chen,Y., Wu,Q., Sun,F., Zhu,X. and Pan,Q.
  TITLE     SNORA56-mediated pseudouridylation of 28 S rRNA inhibits
            ferroptosis and promotes colorectal cancer proliferation by
            enhancing GCLC translation
  JOURNAL   J Exp Clin Cancer Res 42 (1), 331 (2023)
   PUBMED   38049865
  REMARK    GeneRIF: SNORA56-mediated pseudouridylation of 28 S rRNA inhibits
            ferroptosis and promotes colorectal cancer proliferation by
            enhancing GCLC translation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Liu,C., Wu,X., Bing,X., Qi,W., Zhu,F., Guo,N., Li,C., Gao,X.,
            Cao,X., Zhao,M. and Xia,M.
  TITLE     H1N1 influenza virus infection through NRF2-KEAP1-GCLC pathway
            induces ferroptosis in nasal mucosal epithelial cells
  JOURNAL   Free Radic Biol Med 204, 226-242 (2023)
   PUBMED   37146698
  REMARK    GeneRIF: H1N1 influenza virus infection through NRF2-KEAP1-GCLC
            pathway induces ferroptosis in nasal mucosal epithelial cells.
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Da,D., Pan,Z., Zeng,L., Dang,Y., Dang,C., Huang,Y., Shi,D. and
            Li,H.
  TITLE     Glutamate-cysteine ligase catalytic and its modifier function as
            novel immunotargets in gastric adenocarcinoma
  JOURNAL   Asian J Surg 46 (1), 143-149 (2023)
   PUBMED   35241341
  REMARK    GeneRIF: Glutamate-cysteine ligase catalytic and its modifier
            function as novel immunotargets in gastric adenocarcinoma.
REFERENCE   4  (residues 1 to 637)
  AUTHORS   Luo,L., Zhang,Z., Weng,Y. and Zeng,J.
  TITLE     Ferroptosis-Related Gene GCLC Is a Novel Prognostic Molecular and
            Correlates with Immune Infiltrates in Lung Adenocarcinoma
  JOURNAL   Cells 11 (21), 3371 (2022)
   PUBMED   36359768
  REMARK    GeneRIF: Ferroptosis-Related Gene GCLC Is a Novel Prognostic
            Molecular and Correlates with Immune Infiltrates in Lung
            Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 637)
  AUTHORS   Bykanova,M.A., Solodilova,M.A., Azarova,I.E., Klyosova,E.Y.,
            Bushueva,O.Y., Polonikova,A.A., Churnosov,M.I. and Polonikov,A.V.
  TITLE     Genetic variation at the catalytic subunit of glutamate cysteine
            ligase contributes to the susceptibility to sporadic colorectal
            cancer: a pilot study
  JOURNAL   Mol Biol Rep 49 (7), 6145-6154 (2022)
   PUBMED   35386070
  REMARK    GeneRIF: Genetic variation at the catalytic subunit of glutamate
            cysteine ligase contributes to the susceptibility to sporadic
            colorectal cancer: a pilot study.
REFERENCE   6  (residues 1 to 637)
  AUTHORS   Mulcahy,R.T. and Gipp,J.J.
  TITLE     Identification of a putative antioxidant response element in the
            5'-flanking region of the human gamma-glutamylcysteine synthetase
            heavy subunit gene
  JOURNAL   Biochem Biophys Res Commun 209 (1), 227-233 (1995)
   PUBMED   7726839
REFERENCE   7  (residues 1 to 637)
  AUTHORS   Gipp,J.J., Chang,C. and Mulcahy,R.T.
  TITLE     Cloning and nucleotide sequence of a full-length cDNA for human
            liver gamma-glutamylcysteine synthetase
  JOURNAL   Biochem Biophys Res Commun 185 (1), 29-35 (1992)
   PUBMED   1350904
REFERENCE   8  (residues 1 to 637)
  AUTHORS   Beutler,E., Moroose,R., Kramer,L., Gelbart,T. and Forman,L.
  TITLE     Gamma-glutamylcysteine synthetase deficiency and hemolytic anemia
  JOURNAL   Blood 75 (1), 271-273 (1990)
   PUBMED   2294991
REFERENCE   9  (residues 1 to 637)
  AUTHORS   Lebo,R.V. and Kredich,N.M.
  TITLE     Inactivation of human gamma-glutamylcysteine synthetase by
            cystamine. Demonstration and quantification of enzyme-ligand
            complexes
  JOURNAL   J Biol Chem 253 (8), 2615-2623 (1978)
   PUBMED   24639
REFERENCE   10 (residues 1 to 637)
  AUTHORS   Konrad,P.N., Richards,F. 2nd, Valentine,W.N. and Paglia,D.E.
  TITLE     -Glutamyl-cysteine synthetase deficiency. A cause of hereditary
            hemolytic anemia
  JOURNAL   N Engl J Med 286 (11), 557-561 (1972)
   PUBMED   5058793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI550814.1, AL531593.3,
            AK313480.1, AB262176.1 and BC039894.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Glutamate-cysteine ligase, also known as
            gamma-glutamylcysteine synthetase is the first rate-limiting enzyme
            of glutathione synthesis. The enzyme consists of two subunits, a
            heavy catalytic subunit and a light regulatory subunit. This locus
            encodes the catalytic subunit, while the regulatory subunit is
            derived from a different gene located on chromosome 1p22-p21.
            Mutations at this locus have been associated with hemolytic anemia
            due to deficiency of gamma-glutamylcysteine synthetase and
            susceptibility to myocardial infarction.[provided by RefSeq, Oct
            2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.95345.1, AB262176.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000650454.1/ ENSP00000497574.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.1"
     Protein         1..637
                     /product="glutamate--cysteine ligase catalytic subunit
                     isoform a"
                     /EC_number="6.3.2.2"
                     /note="gamma-glutamylcysteine synthetase; gamma-ECS; GCS
                     heavy chain"
                     /calculated_mol_wt=72635
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P48506.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P48506.2)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48506.2)"
     Region          <22..76
                     /region_name="PRK00087"
                     /note="bifunctional 4-hydroxy-3-methylbut-2-enyl
                     diphosphate reductase/30S ribosomal protein S1"
                     /db_xref="CDD:234623"
     Region          236..608
                     /region_name="GCS"
                     /note="Glutamate-cysteine ligase; pfam03074"
                     /db_xref="CDD:460796"
     CDS             1..637
                     /gene="GCLC"
                     /gene_synonym="CNSHA7; GCL; GCS; GLCL; GLCLC"
                     /coded_by="NM_001498.4:457..2370"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4952.1"
                     /db_xref="GeneID:2729"
                     /db_xref="HGNC:HGNC:4311"
                     /db_xref="MIM:606857"
ORIGIN      
        1 mgllsqgspl sweetkrhad hvrrhgilqf lhiyhavkdr hkdvlkwgde veymlvsfdh
       61 enkkvrlvls gekvletlqe kgertnpnhp tlwrpeygsy miegtpgqpy ggtmsefntv
      121 eanmrkrrke atsileenqa lctitsfprl gcpgftlpev kpnpveggas kslffpdeai
      181 nkhprfstlt rnirhrrgek vvinvpifkd kntpspfiet fteddeasra skpdhiymda
      241 mgfgmgnccl qvtfqacsis earylydqla ticpivmals aaspfyrgyv sdidcrwgvi
      301 sasvddrtre ergleplknn nyrisksryd sidsylskcg ekyndidlti dkeiyeqllq
      361 egidhllaqh vahlfirdpl tlfeekihld danesdhfen iqstnwqtmr fkppppnsdi
      421 gwrvefrpme vqltdfensa yvvfvvlltr vilsykldfl iplskvdenm kvaqkrdavl
      481 qgmfyfrkdi ckggnavvdg cgkaqnstel aaeeytlmsi dtiingkegv fpglipilns
      541 ylenmevdvd trcsilnylk likkrasgel mtvarwmref ianhpdykqd svitdemnys
      601 lilkcnqian elcecpellg safrkvkysg sktdssn
//
LOCUS       NP_057711                360 aa            linear   PRI 27-APR-2025
DEFINITION  archaemetzincin-2 isoform 1 [Homo sapiens].
ACCESSION   NP_057711
VERSION     NP_057711.3
DBSOURCE    REFSEQ: accession NM_016627.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Huang,W., Wang,Y., Chu,W. and Tseng,R.
  TITLE     Refined-mapping of the novel TSG within the 17q24.3 chromosomal
            region in non-small cell lung cancer samples
  JOURNAL   Oncol Lett 12 (3), 1975-1980 (2016)
   PUBMED   27602123
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK126146.1 and BQ432895.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 17, 2005 this sequence version replaced NP_057711.2.
            
            Summary: The protein encoded by this gene is a zinc metalloprotease
            that displays some activity against angiotensin-3. The encoded
            protein is inhibited by the aminopeptidase inhibitor amastatin, as
            well as by the general inhibitors o-phenanthroline and batimastat.
            Defects in this gene may be associated with lung tumorigenesis.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Variants 1-5 and 7-17 all encode the same isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.627744.1, AK126146.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359904.8/ ENSP00000352976.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..360
                     /product="archaemetzincin-2 isoform 1"
                     /note="archaemetzincins-2; archeobacterial
                     metalloproteinase-like protein 2"
                     /calculated_mol_wt=41132
     Region          89..297
                     /region_name="Peptidase_M54"
                     /note="Peptidase family M54, also called archaemetzincins
                     or archaelysins; cd11375"
                     /db_xref="CDD:213029"
     Site            order(186,188,254..255,258,264..265,270,272,289,292)
                     /site_type="active"
                     /db_xref="CDD:213029"
     CDS             1..360
                     /gene="AMZ2"
                     /coded_by="NM_016627.5:664..1746"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11674.1"
                     /db_xref="GeneID:51321"
                     /db_xref="HGNC:HGNC:28041"
                     /db_xref="MIM:615169"
ORIGIN      
        1 mqiirhseqt lktalisknp vlvsqyekln ageqrlmnea fqpasdlfgp itlhspsdwi
       61 tshpeapqdf eqffsdpyrk tpspnkrsiy iqsigslgnt riiseeyikw ltgyckayfy
      121 glrvkllepv pvsvtrcsfr vnenthnlqi hagdilkflk kkkpedafcv vgitmidlyp
      181 rdswnfvfgq asltdgvgif sfarygsdfy smhykgkvkk lkktsssdys ifdnyyipei
      241 tsvlllrsck tltheighif glrhcqwlac lmqgsnhlee adrrplnlcp iclhklqcav
      301 gfsiveryka lvrwiddess dtpgatpehs hedngnlpkp veafkewkew iikclavlqk
//
LOCUS       NP_742056                586 aa            linear   PRI 27-APR-2025
DEFINITION  protein phosphatase EYA1 isoform 3 [Homo sapiens].
ACCESSION   NP_742056
VERSION     NP_742056.2
DBSOURCE    REFSEQ: accession NM_172059.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Shao,H., Li,Y., Zhao,H., Lin,K., Gao,Y., Ming,C. and Ma,J.
  TITLE     [Clinical phenotypic and genetic analysis of syndrome families with
            EYA1 gene variants]
  JOURNAL   Lin Chuang Er Bi Yan Hou Tou Jing Wai Ke Za Zhi 38 (7), 636-640
            (2024)
   PUBMED   38973045
  REMARK    GeneRIF: [Clinical phenotypic and genetic analysis of syndrome
            families with EYA1 gene variants].
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Zhang,H., Gao,J., Wang,H., Liu,M., Lu,S., Xu,H., Tang,W. and
            Zheng,G.
  TITLE     Novel likely pathogenic variant in the EYA1 gene causing Branchio
            oto renal syndrome and the exploration of pathogenic mechanisms
  JOURNAL   BMC Med Genomics 17 (1), 89 (2024)
   PUBMED   38627775
  REMARK    GeneRIF: Novel likely pathogenic variant in the EYA1 gene causing
            Branchio oto renal syndrome and the exploration of pathogenic
            mechanisms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Wang,F., Zhang,R., Jian,J., Sun,Y. and Li,Q.
  TITLE     Identification and Functional Study of Enhancers of EYA1: The
            Causative Gene of Branchio-Oto-Renal Syndrome
  JOURNAL   Dev Neurosci 46 (5), 333-340 (2024)
   PUBMED   38228108
  REMARK    GeneRIF: Identification and Functional Study of Enhancers of EYA1:
            The Causative Gene of Branchio-Oto-Renal Syndrome.
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Yalcouye,A., Traore,O., Diarra,S., Schrauwen,I., Esoh,K.,
            Kadlubowska,M.K., Bharadwaj,T., Adadey,S.M., Keita,M., Guinto,C.O.,
            Leal,S.M., Landoure,G. and Wonkam,A.
  TITLE     A monoallelic variant in EYA1 is associated with Branchio-Otic
            syndrome in a Malian family
  JOURNAL   Mol Genet Genomic Med 10 (7), e1995 (2022)
   PUBMED   35698919
  REMARK    GeneRIF: A monoallelic variant in EYA1 is associated with
            Branchio-Otic syndrome in a Malian family.
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Pignoni,F., Hu,B., Zavitz,K.H., Xiao,J., Garrity,P.A. and
            Zipursky,S.L.
  TITLE     The eye-specification proteins So and Eya form a complex and
            regulate multiple steps in Drosophila eye development
  JOURNAL   Cell 91 (7), 881-891 (1997)
   PUBMED   9428512
  REMARK    Erratum:[Cell 1998 Feb 20;92(4):following 585]
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Abdelhak,S., Kalatzis,V., Heilig,R., Compain,S., Samson,D.,
            Vincent,C., Levi-Acobas,F., Cruaud,C., Le Merrer,M., Mathieu,M.,
            Konig,R., Vigneron,J., Weissenbach,J., Petit,C. and Weil,D.
  TITLE     Clustering of mutations responsible for branchio-oto-renal (BOR)
            syndrome in the eyes absent homologous region (eyaHR) of EYA1
  JOURNAL   Hum Mol Genet 6 (13), 2247-2255 (1997)
   PUBMED   9361030
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Abdelhak,S., Kalatzis,V., Heilig,R., Compain,S., Samson,D.,
            Vincent,C., Weil,D., Cruaud,C., Sahly,I., Leibovici,M.,
            Bitner-Glindzicz,M., Francis,M., Lacombe,D., Vigneron,J.,
            Charachon,R., Boven,K., Bedbeder,P., Van Regemorter,N.,
            Weissenbach,J. and Petit,C.
  TITLE     A human homologue of the Drosophila eyes absent gene underlies
            branchio-oto-renal (BOR) syndrome and identifies a novel gene
            family
  JOURNAL   Nat Genet 15 (2), 157-164 (1997)
   PUBMED   9020840
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Smith,R.J.H.
  TITLE     Branchiootorenal Spectrum Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301554
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Stoppa-Lyonnet,D., Carter,P.E., Meo,T. and Tosi,M.
  TITLE     Clusters of intragenic Alu repeats predispose the human C1
            inhibitor locus to deleterious rearrangements
  JOURNAL   Proc Natl Acad Sci U S A 87 (4), 1551-1555 (1990)
   PUBMED   2154751
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099805.2, AC016465.8 and
            AC022858.8.
            
            On Nov 18, 2017 this sequence version replaced NP_742056.1.
            
            Summary: This gene encodes a member of the eyes absent (EYA) family
            of proteins. The encoded protein may play a role in the developing
            kidney, branchial arches, eye, and ear. Mutations of this gene have
            been associated with branchiootorenal dysplasia syndrome,
            branchiootic syndrome, and sporadic cases of congenital cataracts
            and ocular anterior segment anomalies. A similar protein in mice
            can act as a transcriptional activator. Alternatively spliced
            transcript variants have been identified for this gene. [provided
            by RefSeq, Dec 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.189290.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.3"
     Protein         1..586
                     /product="protein phosphatase EYA1 isoform 3"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="eyes absent homolog 1; protein phosphatase EYA1"
                     /calculated_mol_wt=63495
     Region          <29..303
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          345..586
                     /region_name="HAD_Eya"
                     /note="protein tyrosine phosphatase domain of the nuclear
                     transcription factor of Eyes absent (Eya) and related
                     phosphatase domains; cd02601"
                     /db_xref="CDD:319789"
     Site            order(347,544,546,562,564..567,573,576,579..580,583..586)
                     /site_type="other"
                     /note="SIX1 interface [polypeptide binding]"
                     /db_xref="CDD:319789"
     Site            order(352..356,416..417,525,549..550,554..555)
                     /site_type="active"
                     /db_xref="CDD:319789"
     CDS             1..586
                     /gene="EYA1"
                     /gene_synonym="BOP; BOR; BOS1; OFC1; OTFCS"
                     /coded_by="NM_172059.5:263..2023"
                     /note="isoform 3 is encoded by transcript variant EYA1D"
                     /db_xref="CCDS:CCDS34907.2"
                     /db_xref="GeneID:2138"
                     /db_xref="HGNC:HGNC:3519"
                     /db_xref="MIM:601653"
ORIGIN      
        1 medprgingq svqtsqassd vavssscrsm emqdltsphs rlsgssesps gpklgnshin
       61 snsmtpngte vktepmssse tasttadgsl nnfsgsaigs ssfsprpthq fsppqiypsn
      121 rpyphilptp ssqtmaaygq tqfttgmqqa tayatypqpg qpygissygi ktegglsqsq
      181 spgqtgflsy gtsfstpqpg qapysyqmqg ssfttssgiy tgnnsltnss gfnssqqdyp
      241 sypsfgqgqy aqyynsspyp ahymtssnts pttpstnaty qlqeppsgit sqavtdptae
      301 ystihspstp ikdsdsdrlr rgsdgksrgr grrnnnpspp pdsdlervfi wdldetiivf
      361 hslltgsyan rygrecdqvh iddvssddng qdlstynfgt dgfpaaatsa nlclatgvrg
      421 gvdwmrklaf ryrrvkeiyn tyknnvggll gpakreawlq lraeiealtd swltlalkal
      481 slihsrtncv nilvtttqli palakvllyg lgivfpieni ysatkigkes cferiiqrfg
      541 rkvvyvvigd gveeeqgakk hampfwriss hsdlmalhha leleyl
//
LOCUS       NP_068813                855 aa            linear   PRI 27-APR-2025
DEFINITION  suppressor of tumorigenicity 14 protein [Homo sapiens].
ACCESSION   NP_068813
VERSION     NP_068813.1
DBSOURCE    REFSEQ: accession NM_021978.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Ye,F., Yuan,Z., Tang,Y., Li,J., Liu,X., Sun,X., Chen,S., Ye,X.,
            Zeng,Z., Zhang,X.K. and Zhou,H.
  TITLE     Endocytic activation and exosomal secretion of matriptase stimulate
            the second wave of EGF signaling to promote skin and breast cancer
            invasion
  JOURNAL   Cell Rep 43 (4), 114002 (2024)
   PUBMED   38547126
  REMARK    GeneRIF: Endocytic activation and exosomal secretion of matriptase
            stimulate the second wave of EGF signaling to promote skin and
            breast cancer invasion.
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Jang,J., Cho,E.H., Cho,Y., Ganzorig,B., Kim,K.Y., Kim,M.G. and
            Kim,C.
  TITLE     Environment-Sensitive Ectodomain Shedding of Epithin/PRSS14
            Increases Metastatic Potential of Breast Cancer Cells by Producing
            CCL2
  JOURNAL   Mol Cells 45 (8), 564-574 (2022)
   PUBMED   35950457
  REMARK    GeneRIF: Environment-Sensitive Ectodomain Shedding of
            Epithin/PRSS14 Increases Metastatic Potential of Breast Cancer
            Cells by Producing CCL2.
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Serra,G., Memo,L., Cavicchioli,P., Cutrone,M., Giuffre,M., La
            Torre,M.L., Schierz,I.A.M. and Corsello,G.
  TITLE     Novel mutations of the ABCA12, KRT1 and ST14 genes in three
            unrelated newborns showing congenital ichthyosis
  JOURNAL   Ital J Pediatr 48 (1), 145 (2022)
   PUBMED   35964051
  REMARK    GeneRIF: Novel mutations of the ABCA12, KRT1 and ST14 genes in
            three unrelated newborns showing congenital ichthyosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Yamashita,F., Kaieda,T., Shimomura,T., Kawaguchi,M., Lin,C.Y.,
            Johnson,M.D., Tanaka,H., Kiwaki,T., Fukushima,T. and Kataoka,H.
  TITLE     Role of the polycystic kidney disease domain in matriptase
            chaperone activity and localization of hepatocyte growth factor
            activator inhibitor-1
  JOURNAL   FEBS J 289 (12), 3422-3439 (2022)
   PUBMED   35020274
  REMARK    GeneRIF: Role of the polycystic kidney disease domain in matriptase
            chaperone activity and localization of hepatocyte growth factor
            activator inhibitor-1.
            Review article
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Dai,Y.H., Wang,Y.F., Shen,P.C., Lo,C.H., Yang,J.F., Lin,C.S.,
            Chao,H.L. and Huang,W.Y.
  TITLE     Gene-associated methylation status of ST14 as a predictor of
            survival and hormone receptor positivity in breast Cancer
  JOURNAL   BMC Cancer 21 (1), 945 (2021)
   PUBMED   34418985
  REMARK    GeneRIF: Gene-associated methylation status of ST14 as a predictor
            of survival and hormone receptor positivity in breast Cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Takeuchi,T., Harris,J.L., Huang,W., Yan,K.W., Coughlin,S.R. and
            Craik,C.S.
  TITLE     Cellular localization of membrane-type serine protease 1 and
            identification of protease-activated receptor-2 and single-chain
            urokinase-type plasminogen activator as substrates
  JOURNAL   J Biol Chem 275 (34), 26333-26342 (2000)
   PUBMED   10831593
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Takeuchi,T., Shuman,M.A. and Craik,C.S.
  TITLE     Reverse biochemistry: use of macromolecular protease inhibitors to
            dissect complex biological processes and identify a membrane-type
            serine protease in epithelial cancer and normal tissue
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11054-11061 (1999)
   PUBMED   10500122
REFERENCE   8  (residues 1 to 855)
  AUTHORS   Lin,C.Y., Anders,J., Johnson,M. and Dickson,R.B.
  TITLE     Purification and characterization of a complex containing
            matriptase and a Kunitz-type serine protease inhibitor from human
            milk
  JOURNAL   J Biol Chem 274 (26), 18237-18242 (1999)
   PUBMED   10373425
REFERENCE   9  (residues 1 to 855)
  AUTHORS   Lin,C.Y., Anders,J., Johnson,M., Sang,Q.A. and Dickson,R.B.
  TITLE     Molecular cloning of cDNA for matriptase, a matrix-degrading serine
            protease with trypsin-like activity
  JOURNAL   J Biol Chem 274 (26), 18231-18236 (1999)
   PUBMED   10373424
REFERENCE   10 (residues 1 to 855)
  AUTHORS   Zhang,Y., Cai,X., Schlegelberger,B. and Zheng,S.
  TITLE     Assignment1 of human putative tumor suppressor genes ST13 (alias
            SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and
            11q24-->q25 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 56-57 (1998)
   PUBMED   9925927
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001183.6, BM791311.1,
            AB030036.1 and BC005826.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is an epithelial-derived,
            integral membrane serine protease. This protease forms a complex
            with the Kunitz-type serine protease inhibitor, HAI-1, and is found
            to be activated by sphingosine 1-phosphate. This protease has been
            shown to cleave and activate hepatocyte growth factor/scattering
            factor, and urokinase plasminogen activator, which suggest the
            function of this protease as an epithelial membrane activator for
            other proteases and latent growth factors. The expression of this
            protease has been associated with breast, colon, prostate, and
            ovarian tumors, which implicates its role in cancer invasion, and
            metastasis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030532.1, AF133086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278742.6/ ENSP00000278742.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.3"
     Protein         1..855
                     /product="suppressor of tumorigenicity 14 protein"
                     /EC_number="3.4.21.109"
                     /note="suppression of tumorigenicity 14 (colon carcinoma,
                     matriptase, epithin); membrane-type serine protease 1;
                     serine protease 14; prostamin; serine protease TADG-15;
                     tumor associated differentially expressed gene 15 protein;
                     suppression of tumorigenicity 14 (colon carcinoma);
                     channel-activating protein 3"
                     /calculated_mol_wt=94639
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Y6.2)"
     Site            56..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Y6.2)"
     Region          88..>162
                     /region_name="SEA"
                     /note="SEA domain; pfam01390"
                     /db_xref="CDD:460188"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Y6.2)"
     Region          227..332
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(227,229,257,262,304,328,330,332)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Site            302
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Y6.2)"
     Region          340..444
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(348,350,352,379,384,417,441,443)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          454..486
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(457,465,476..477)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(469,472,476,482..483)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            479..483
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            485
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Y6.2)"
     Region          488..523
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(494,502,513..514)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(506,509,513,519..520)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            516..520
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          525..559
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(530,538,549..550)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(542,545,549,555..556)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            552..556
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          567..602
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(572,580,592..593)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(584,588,592,598..599)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            595..599
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          615..852
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            615
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(656,711,805)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            772
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Y6.2)"
     Site            order(799,825,827)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..855
                     /gene="ST14"
                     /gene_synonym="ARCI11; CAP3; HAI; MT-SP1; MTSP1; PRSS14;
                     SNC19; TADG15; TMPRSS14"
                     /coded_by="NM_021978.4:199..2766"
                     /db_xref="CCDS:CCDS8487.1"
                     /db_xref="GeneID:6768"
                     /db_xref="HGNC:HGNC:11344"
                     /db_xref="MIM:606797"
ORIGIN      
        1 mgsdrarkgg ggpkdfgagl kynsrhekvn gleegveflp vnnvkkvekh gpgrwvvlaa
       61 vliglllvll gigflvwhlq yrdvrvqkvf ngymritnen fvdayensns tefvslaskv
      121 kdalkllysg vpflgpyhke savtafsegs viayywsefs ipqhlveeae rvmaeervvm
      181 lpprarslks fvvtsvvafp tdsktvqrtq dnscsfglha rgvelmrftt pgfpdspypa
      241 harcqwalrg dadsvlsltf rsfdlascde rgsdlvtvyn tlspmephal vqlcgtypps
      301 ynltfhssqn vllitlitnt errhpgfeat ffqlprmssc ggrlrkaqgt fnspyypghy
      361 ppnidctwni evpnnqhvkv rfkffyllep gvpagtcpkd yveingekyc gersqfvvts
      421 nsnkitvrfh sdqsytdtgf laeylsydss dpcpgqftcr tgrcirkelr cdgwadctdh
      481 sdelncscda ghqftcknkf ckplfwvcds vndcgdnsde qgcscpaqtf rcsngkclsk
      541 sqqcngkddc gdgsdeascp kvnvvtctkh tyrclnglcl skgnpecdgk edcsdgsdek
      601 dcdcglrsft rqarvvggtd adegewpwqv slhalgqghi cgaslispnw lvsaahcyid
      661 drgfrysdpt qwtaflglhd qsqrsapgvq errlkriish pffndftfdy diallelekp
      721 aeyssmvrpi clpdashvfp agkaiwvtgw ghtqyggtga lilqkgeirv inqttcenll
      781 pqqitprmmc vgflsggvds cqgdsggpls sveadgrifq agvvswgdgc aqrnkpgvyt
      841 rlplfrdwik entgv
//
LOCUS       NP_075060                247 aa            linear   PRI 27-APR-2025
DEFINITION  centromere protein H [Homo sapiens].
ACCESSION   NP_075060
VERSION     NP_075060.1
DBSOURCE    REFSEQ: accession NM_022909.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Tian,T., Chen,L., Dou,Z., Yang,Z., Gao,X., Yuan,X., Wang,C.,
            Liu,R., Shen,Z., Gui,P., Teng,M., Meng,X., Hill,D.L., Li,L.,
            Zhang,X., Liu,X., Sun,L., Zang,J. and Yao,X.
  TITLE     Structural insights into human CCAN complex assembled onto DNA
  JOURNAL   Cell Discov 8 (1), 90 (2022)
   PUBMED   36085283
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Lu,G., Hou,H., Lu,X., Ke,X., Wang,X., Zhang,D., Zhao,Y., Zhang,J.,
            Ren,M. and He,S.
  TITLE     CENP-H regulates the cell growth of human hepatocellular carcinoma
            cells through the mitochondrial apoptotic pathway
  JOURNAL   Oncol Rep 37 (6), 3484-3492 (2017)
   PUBMED   28498417
  REMARK    GeneRIF: In summary, CENP-H may be involved in cell proliferation
            and apoptosis of hepatocellular carcinoma (HCC)cells through the
            mitochondrial apoptotic pathway. Combined with previous studies,
            the data provide a new perspective on HCC development and
            progression.
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Mikami,Y., Hori,T., Kimura,H. and Fukagawa,T.
  TITLE     The functional region of CENP-H interacts with the Nuf2 complex
            that localizes to centromere during mitosis
  JOURNAL   Mol Cell Biol 25 (5), 1958-1970 (2005)
   PUBMED   15713649
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Obuse,C., Iwasaki,O., Kiyomitsu,T., Goshima,G., Toyoda,Y. and
            Yanagida,M.
  TITLE     A conserved Mis12 centromere complex is linked to heterochromatic
            HP1 and outer kinetochore protein Zwint-1
  JOURNAL   Nat Cell Biol 6 (11), 1135-1141 (2004)
   PUBMED   15502821
REFERENCE   8  (residues 1 to 247)
  AUTHORS   Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K.
  TITLE     Proteomics analysis of the centromere complex from HeLa interphase
            cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
            the CEN-complex, while BMI-1 is transiently co-localized with the
            centromeric region in interphase
  JOURNAL   Genes Cells 9 (2), 105-120 (2004)
   PUBMED   15009096
REFERENCE   9  (residues 1 to 247)
  AUTHORS   Saffery,R., Sumer,H., Hassan,S., Wong,L.H., Craig,J.M.,
            Todokoro,K., Anderson,M., Stafford,A. and Choo,K.H.
  TITLE     Transcription within a functional human centromere
  JOURNAL   Mol Cell 12 (2), 509-516 (2003)
   PUBMED   14536089
REFERENCE   10 (residues 1 to 247)
  AUTHORS   Sugata,N., Li,S., Earnshaw,W.C., Yen,T.J., Yoda,K., Masumoto,H.,
            Munekata,E., Warburton,P.E. and Todokoro,K.
  TITLE     Human CENP-H multimers colocalize with CENP-A and CENP-C at active
            centromere--kinetochore complexes
  JOURNAL   Hum Mol Genet 9 (19), 2919-2926 (2000)
   PUBMED   11092768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022107.8.
            
            Summary: Centromere and kinetochore proteins play a critical role
            in centromere structure, kinetochore formation, and sister
            chromatid separation. The protein encoded by this gene colocalizes
            with inner kinetochore plate proteins CENP-A and CENP-C in both
            interphase and metaphase. It localizes outside of centromeric
            heterochromatin, where CENP-B is localized, and inside the
            kinetochore corona, where CENP-E is localized during prometaphase.
            It is thought that this protein can bind to itself, as well as to
            CENP-A, CENP-B or CENP-C. Multimers of the protein localize
            constitutively to the inner kinetochore plate and play an important
            role in the organization and function of the active
            centromere-kinetochore complex. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.400574.1, BC012024.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283006.7/ ENSP00000283006.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.2"
     Protein         1..247
                     /product="centromere protein H"
                     /note="kinetochore protein CENP-H; interphase centromere
                     complex protein 35"
                     /calculated_mol_wt=28350
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3R5.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H3R5.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H3R5.1)"
     Region          <42..>208
                     /region_name="46"
                     /note="endonuclease subunit; Provisional; PHA02562"
                     /db_xref="CDD:222878"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H3R5.1)"
     Region          126..239
                     /region_name="CENP-H"
                     /note="Centromere protein H (CENP-H); pfam05837"
                     /db_xref="CDD:461756"
     CDS             1..247
                     /gene="CENPH"
                     /coded_by="NM_022909.4:53..796"
                     /db_xref="CCDS:CCDS3998.1"
                     /db_xref="GeneID:64946"
                     /db_xref="HGNC:HGNC:17268"
                     /db_xref="MIM:605607"
ORIGIN      
        1 meeqpqmqda depadsggeg raggppqvag aqaacsedrm tlllrlraqt kqqlleyksm
       61 vdaseektpe qimqekqiea kiedleneie evkvafeikk laldrmrlst alkknlekis
      121 rqssvlmdnm khllelnkli mksqqeswdl eeklldirkk rlqlkqases klleiqtekn
      181 kqkidldsme nserikiirq nlqmeikitt viqhvfqnli lgskvnwaed palkeivlql
      241 eknvdmm
//
LOCUS       NP_083138                663 aa            linear   ROD 27-APR-2025
DEFINITION  RING finger protein 145 isoform 1 [Mus musculus].
ACCESSION   NP_083138 XP_203376
VERSION     NP_083138.2
DBSOURCE    REFSEQ: accession NM_028862.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Menzies,S.A., Volkmar,N., van den Boomen,D.J., Timms,R.T.,
            Dickson,A.S., Nathan,J.A. and Lehner,P.J.
  TITLE     The sterol-responsive RNF145 E3 ubiquitin ligase mediates the
            degradation of HMG-CoA reductase together with gp78 and Hrd1
  JOURNAL   Elife 7, e40009 (2018)
   PUBMED   30543180
  REMARK    GeneRIF: n the absence of both RNF145 and gp78, Hrd1, a third
            UBE2G2-dependent E3 ligase, partially regulates HMGCR activity. Our
            findings reveal a critical role for the sterol-responsive RNF145 in
            HMGCR regulation and elucidate the complexity of sterol-accelerated
            HMGCR degradation
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Zhang,L., Rajbhandari,P., Priest,C., Sandhu,J., Wu,X., Temel,R.,
            Castrillo,A., de Aguiar Vallim,T.Q., Sallam,T. and Tontonoz,P.
  TITLE     Inhibition of cholesterol biosynthesis through RNF145-dependent
            ubiquitination of SCAP
  JOURNAL   Elife 6, e28766 (2017)
   PUBMED   29068315
  REMARK    GeneRIF: Mechanistic studies show that RNF145 triggers
            ubiquitination of SCAP on lysine residues within a cytoplasmic loop
            essential for COPII binding, potentially inhibiting its transport
            to Golgi and subsequent processing of SREBP-2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Cook,E.C., Nelson,J.K., Sorrentino,V., Koenis,D., Moeton,M.,
            Scheij,S., Ottenhoff,R., Bleijlevens,B., Loregger,A. and Zelcer,N.
  TITLE     Identification of the ER-resident E3 ubiquitin ligase RNF145 as a
            novel LXR-regulated gene
  JOURNAL   PLoS One 12 (2), e0172721 (2017)
   PUBMED   28231341
  REMARK    GeneRIF: we report the identification of RNF145 as an ER-resident
            E3 ubiquitin ligase that is transcriptionally controlled by LXR.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Graham,D.B., Becker,C.E., Doan,A., Goel,G., Villablanca,E.J.,
            Knights,D., Mok,A., Ng,A.C.Y., Doench,J.G., Root,D.E., Clish,C.B.
            and Xavier,R.J.
  TITLE     Functional genomics identifies negative regulatory nodes
            controlling phagocyte oxidative burst
  JOURNAL   Nat Commun 6, 7838 (2015)
   PUBMED   26194095
  REMARK    GeneRIF: implicated in proteostasis of Nox2 complex
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 663)
  AUTHORS   Gineste,C., De Winter,J.M., Kohl,C., Witt,C.C., Giannesini,B.,
            Brohm,K., Le Fur,Y., Gretz,N., Vilmen,C., Pecchi,E., Jubeau,M.,
            Cozzone,P.J., Stienen,G.J., Granzier,H., Labeit,S.,
            Ottenheijm,C.A., Bendahan,D. and Gondin,J.
  TITLE     In vivo and in vitro investigations of heterozygous nebulin
            knock-out mice disclose a mild skeletal muscle phenotype
  JOURNAL   Neuromuscul Disord 23 (4), 357-369 (2013)
   PUBMED   23375831
REFERENCE   7  (residues 1 to 663)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 663)
  AUTHORS   Mager,J., Schultz,R.M., Brunk,B.P. and Bartolomei,M.S.
  TITLE     Identification of candidate maternal-effect genes through
            comparison of multiple microarray data sets
  JOURNAL   Mamm Genome 17 (9), 941-949 (2006)
   PUBMED   16964442
REFERENCE   9  (residues 1 to 663)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL603913.14, AK014408.1, BB618481.1, AK043002.1 and CK624836.1.
            
            On Oct 28, 2009 this sequence version replaced NP_083138.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK043002.1, AK014408.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 25.94 cM"
     Protein         1..663
                     /product="RING finger protein 145 isoform 1"
                     /EC_number="2.3.2.27"
                     /calculated_mol_wt=74517
     Region          8..506
                     /region_name="TRC8_N"
                     /note="TRC8 N-terminal domain; pfam13705"
                     /db_xref="CDD:463960"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Region          81..84
                     /region_name="YLYF motif.
                     /evidence=ECO:0000269|PubMed:29374057"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            123..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            146..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            168..188
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            205..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            316..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            340..360
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            410..430
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            460..480
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Site            482..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     Region          <520..627
                     /region_name="HRD1"
                     /note="HRD ubiquitin ligase complex, ER membrane component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5243"
                     /db_xref="CDD:227568"
     Region          533..575
                     /region_name="RING-H2_RNF145"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 145 (RNF145) and similar proteins; cd16684"
                     /db_xref="CDD:319598"
     Region          587..663
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SWK7.1)"
     CDS             1..663
                     /gene="Rnf145"
                     /gene_synonym="3732413I11Rik; TMRF1"
                     /coded_by="NM_028862.4:352..2343"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS24565.1"
                     /db_xref="GeneID:74315"
                     /db_xref="MGI:MGI:1921565"
ORIGIN      
        1 maakekleav lnvalrvpsi mlldvlyrwd vssffqqiqr sslnnnplfq ykylalnmhy
       61 vgyilsvvll tlprqhlvql ylyfvtalll yaghqisrdy vrselesaye gpmyleplsm
      121 nrfttaligq lvvctlcscv mktkqiwlfs ahmlpllarl clvpletivi inkfamiftg
      181 levlyflgsn llvpynlaks ayrelvqvve vygllalgms lwnqlvvpvl fmvfwlvlfa
      241 lqiysyfstr dqpasrerll flfltsiaec cstpysllgl vftvsfvalg vltlckfylq
      301 gyrafmndpa mnrgmtegvt llilavqtgl ielqvvhraf llsiilfivv asilqsmlei
      361 adpivlalga srdkslwkhf ravslclfll vfpaymaymi cqffhmdfwl liiisssilt
      421 slqvlgtlfi yvlfmveefr kepvenmddv iyyvngtyrl lefvvalcvv aygvsetifg
      481 ewtvmgsmii fihsyynvwl raqlgwksfl lrrdavnkik slpvatqeql ekhndicaic
      541 yqdmksavit pcshffhagc lkkwlyvqdt cplchchlkn ssqlpglgte aapqppagae
      601 qnivlqegpe ppdhesppgt gtqegsgdss ehinrgsasq egaadagegp qipegevcpv
      661 esa
//
LOCUS       NP_001265372             578 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat and LEM domain-containing protein 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001265372
VERSION     NP_001265372.2
DBSOURCE    REFSEQ: accession NM_001278443.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Freeman,A.D.J., Declais,A.C., Wilson,T.J. and Lilley,D.M.J.
  TITLE     Biochemical and mechanistic analysis of the cleavage of branched
            DNA by human ANKLE1
  JOURNAL   Nucleic Acids Res 51 (11), 5743-5754 (2023)
   PUBMED   37216589
  REMARK    GeneRIF: Biochemical and mechanistic analysis of the cleavage of
            branched DNA by human ANKLE1.
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Kaspers,M.S., Pogenberg,V., Pett,C., Ernst,S., Ecker,F.,
            Ochtrop,P., Groll,M., Hedberg,C. and Itzen,A.
  TITLE     Dephosphocholination by Legionella effector Lem3 functions through
            remodelling of the switch II region of Rab1b
  JOURNAL   Nat Commun 14 (1), 2245 (2023)
   PUBMED   37076474
  REMARK    GeneRIF: Dephosphocholination by Legionella effector Lem3 functions
            through remodelling of the switch II region of Rab1b.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Jiang,H., Kong,N., Liu,Z., West,S.C. and Chan,Y.W.
  TITLE     Human Endonuclease ANKLE1 Localizes at the Midbody and Processes
            Chromatin Bridges to Prevent DNA Damage and cGAS-STING Activation
  JOURNAL   Adv Sci (Weinh) 10 (12), e2204388 (2023)
   PUBMED   36825683
  REMARK    GeneRIF: Human Endonuclease ANKLE1 Localizes at the Midbody and
            Processes Chromatin Bridges to Prevent DNA Damage and cGAS-STING
            Activation.
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Martini,R., Chen,Y., Jenkins,B.D., Elhussin,I.A., Cheng,E.,
            Hoda,S.A., Ginter,P.S., Hanover,J., Zeidan,R.B., Oppong,J.K.,
            Adjei,E.K., Jibril,A., Chitale,D., Bensenhaver,J.M., Awuah,B.,
            Bekele,M., Abebe,E., Kyei,I., Aitpillah,F.S., Adinku,M.O.,
            Ankomah,K., Osei-Bonsu,E.B., Nathansan,S.D., Jackson,L., Jiagge,E.,
            Petersen,L.F., Proctor,E., Nikolinakos,P., Gyan,K.K., Yates,C.,
            Kittles,R., Newman,L.A. and Davis,M.B.
  TITLE     Investigation of triple-negative breast cancer risk alleles in an
            International African-enriched cohort
  JOURNAL   Sci Rep 11 (1), 9247 (2021)
   PUBMED   33927264
  REMARK    GeneRIF: Investigation of triple-negative breast cancer risk
            alleles in an International African-enriched cohort.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Song,J., Freeman,A.D.J., Knebel,A., Gartner,A. and Lilley,D.M.J.
  TITLE     Human ANKLE1 Is a Nuclease Specific for Branched DNA
  JOURNAL   J Mol Biol 432 (21), 5825-5834 (2020)
   PUBMED   32866453
  REMARK    GeneRIF: Human ANKLE1 Is a Nuclease Specific for Branched DNA.
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Brachner,A., Braun,J., Ghodgaonkar,M., Castor,D., Zlopasa,L.,
            Ehrlich,V., Jiricny,J., Gotzmann,J., Knasmuller,S. and Foisner,R.
  TITLE     The endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA
            cleavage in vivo
  JOURNAL   J Cell Sci 125 (Pt 4), 1048-1057 (2012)
   PUBMED   22399800
  REMARK    GeneRIF: Ankle1 is conserved in metazoans and contains a unique
            C-terminal GIY-YIG motif that confers endonuclease activity in
            vitro and in vivo
REFERENCE   7  (residues 1 to 578)
  AUTHORS   Bolton,K.L., Tyrer,J., Song,H., Ramus,S.J., Notaridou,M., Jones,C.,
            Sher,T., Gentry-Maharaj,A., Wozniak,E., Tsai,Y.Y., Weidhaas,J.,
            Paik,D., Van Den Berg,D.J., Stram,D.O., Pearce,C.L., Wu,A.H.,
            Brewster,W., Anton-Culver,H., Ziogas,A., Narod,S.A., Levine,D.A.,
            Kaye,S.B., Brown,R., Paul,J., Flanagan,J., Sieh,W., McGuire,V.,
            Whittemore,A.S., Campbell,I., Gore,M.E., Lissowska,J., Yang,H.P.,
            Medrek,K., Gronwald,J., Lubinski,J., Jakubowska,A., Le,N.D.,
            Cook,L.S., Kelemen,L.E., Brooks-Wilson,A., Massuger,L.F.,
            Kiemeney,L.A., Aben,K.K., van Altena,A.M., Houlston,R.,
            Tomlinson,I., Palmieri,R.T., Moorman,P.G., Schildkraut,J.,
            Iversen,E.S., Phelan,C., Vierkant,R.A., Cunningham,J.M.,
            Goode,E.L., Fridley,B.L., Kruger-Kjaer,S., Blaeker,J., Hogdall,E.,
            Hogdall,C., Gross,J., Karlan,B.Y., Ness,R.B., Edwards,R.P.,
            Odunsi,K., Moyisch,K.B., Baker,J.A., Modugno,F., Heikkinenen,T.,
            Butzow,R., Nevanlinna,H., Leminen,A., Bogdanova,N., Antonenkova,N.,
            Doerk,T., Hillemanns,P., Durst,M., Runnebaum,I., Thompson,P.J.,
            Carney,M.E., Goodman,M.T., Lurie,G., Wang-Gohrke,S., Hein,R.,
            Chang-Claude,J., Rossing,M.A., Cushing-Haugen,K.L., Doherty,J.,
            Chen,C., Rafnar,T., Besenbacher,S., Sulem,P., Stefansson,K.,
            Birrer,M.J., Terry,K.L., Hernandez,D., Cramer,D.W., Vergote,I.,
            Amant,F., Lambrechts,D., Despierre,E., Fasching,P.A.,
            Beckmann,M.W., Thiel,F.C., Ekici,A.B., Chen,X., Johnatty,S.E.,
            Webb,P.M., Beesley,J., Chanock,S., Garcia-Closas,M., Sellers,T.,
            Easton,D.F., Berchuck,A., Chenevix-Trench,G., Pharoah,P.D. and
            Gayther,S.A.
  CONSRTM   Australian Ovarian Cancer Study Group; Australian Cancer Study
            (Ovarian Cancer); Ovarian Cancer Association Consortium
  TITLE     Common variants at 19p13 are associated with susceptibility to
            ovarian cancer
  JOURNAL   Nat Genet 42 (10), 880-884 (2010)
   PUBMED   20852633
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
            Erratum:[Nat Genet. 2016 Jan;48(1):101. doi: 10.1038/ng0116-101b.
            Brook-Wilson, Angela [corrected to Brooks-Wilson, Angela]. PMID:
            26711112]
REFERENCE   8  (residues 1 to 578)
  AUTHORS   Antoniou,A.C., Wang,X., Fredericksen,Z.S., McGuffog,L., Tarrell,R.,
            Sinilnikova,O.M., Healey,S., Morrison,J., Kartsonaki,C.,
            Lesnick,T., Ghoussaini,M., Barrowdale,D., Peock,S., Cook,M.,
            Oliver,C., Frost,D., Eccles,D., Evans,D.G., Eeles,R., Izatt,L.,
            Chu,C., Douglas,F., Paterson,J., Stoppa-Lyonnet,D., Houdayer,C.,
            Mazoyer,S., Giraud,S., Lasset,C., Remenieras,A., Caron,O.,
            Hardouin,A., Berthet,P., Hogervorst,F.B., Rookus,M.A., Jager,A.,
            van den Ouweland,A., Hoogerbrugge,N., van der Luijt,R.B.,
            Meijers-Heijboer,H., Gomez Garcia,E.B., Devilee,P., Vreeswijk,M.P.,
            Lubinski,J., Jakubowska,A., Gronwald,J., Huzarski,T., Byrski,T.,
            Gorski,B., Cybulski,C., Spurdle,A.B., Holland,H., Goldgar,D.E.,
            John,E.M., Hopper,J.L., Southey,M., Buys,S.S., Daly,M.B.,
            Terry,M.B., Schmutzler,R.K., Wappenschmidt,B., Engel,C., Meindl,A.,
            Preisler-Adams,S., Arnold,N., Niederacher,D., Sutter,C.,
            Domchek,S.M., Nathanson,K.L., Rebbeck,T., Blum,J.L., Piedmonte,M.,
            Rodriguez,G.C., Wakeley,K., Boggess,J.F., Basil,J., Blank,S.V.,
            Friedman,E., Kaufman,B., Laitman,Y., Milgrom,R., Andrulis,I.L.,
            Glendon,G., Ozcelik,H., Kirchhoff,T., Vijai,J., Gaudet,M.M.,
            Altshuler,D., Guiducci,C., Loman,N., Harbst,K., Rantala,J.,
            Ehrencrona,H., Gerdes,A.M., Thomassen,M., Sunde,L., Peterlongo,P.,
            Manoukian,S., Bonanni,B., Viel,A., Radice,P., Caldes,T., de la
            Hoya,M., Singer,C.F., Fink-Retter,A., Greene,M.H., Mai,P.L.,
            Loud,J.T., Guidugli,L., Lindor,N.M., Hansen,T.V., Nielsen,F.C.,
            Blanco,I., Lazaro,C., Garber,J., Ramus,S.J., Gayther,S.A.,
            Phelan,C., Narod,S., Szabo,C.I., Benitez,J., Osorio,A.,
            Nevanlinna,H., Heikkinen,T., Caligo,M.A., Beattie,M.S., Hamann,U.,
            Godwin,A.K., Montagna,M., Casella,C., Neuhausen,S.L., Karlan,B.Y.,
            Tung,N., Toland,A.E., Weitzel,J., Olopade,O., Simard,J., Soucy,P.,
            Rubinstein,W.S., Arason,A., Rennert,G., Martin,N.G.,
            Montgomery,G.W., Chang-Claude,J., Flesch-Janys,D., Brauch,H.,
            Severi,G., Baglietto,L., Cox,A., Cross,S.S., Miron,P., Gerty,S.M.,
            Tapper,W., Yannoukakos,D., Fountzilas,G., Fasching,P.A.,
            Beckmann,M.W., Dos Santos Silva,I., Peto,J., Lambrechts,D.,
            Paridaens,R., Rudiger,T., Forsti,A., Winqvist,R., Pylkas,K.,
            Diasio,R.B., Lee,A.M., Eckel-Passow,J., Vachon,C., Blows,F.,
            Driver,K., Dunning,A., Pharoah,P.P., Offit,K., Pankratz,V.S.,
            Hakonarson,H., Chenevix-Trench,G., Easton,D.F. and Couch,F.J.
  CONSRTM   EMBRACE; GEMO Study Collaborators; HEBON; kConFab; SWE-BRCA; MOD
            SQUAD; GENICA
  TITLE     A locus on 19p13 modifies risk of breast cancer in BRCA1 mutation
            carriers and is associated with hormone receptor-negative breast
            cancer in the general population
  JOURNAL   Nat Genet 42 (10), 885-892 (2010)
   PUBMED   20852631
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-gene interaction. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 578)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 578)
  AUTHORS   Lee,K.K. and Wilson,K.L.
  TITLE     All in the family: evidence for four new LEM-domain proteins Lem2
            (NET-25), Lem3, Lem4 and Lem5 in the human genome
  JOURNAL   Symp Soc Exp Biol (56), 329-339 (2004)
   PUBMED   15565891
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK303628.1, AK096688.1 and AC010463.6.
            
            On Nov 10, 2018 this sequence version replaced NP_001265372.1.
            
            Transcript Variant: This variant (2) uses two alternate in-frame
            splice sites in the coding region, compared to variant 1. The
            encoded isoform (2) is shorter, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC125274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..578
                     /product="ankyrin repeat and LEM domain-containing protein
                     1 isoform 2"
                     /note="LEM domain containing 6; ankyrin repeat and LEM
                     domain-containing protein 1; LEM-domain containing 3;
                     ankyrin repeat domain-containing protein 41"
                     /calculated_mol_wt=62367
     Region          <11..>117
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          64..95
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          413..528
                     /region_name="GIY-YIG_COG3680_Meta"
                     /note="GIY-YIG domain of hypothetical proteins from
                     Metazoa; cd10454"
                     /db_xref="CDD:198401"
     Site            order(414..416,449..451)
                     /site_type="other"
                     /note="GIY-YIG motif/motif A"
                     /db_xref="CDD:198401"
     Site            order(416,449,451..452,457,461,514,528)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:198401"
     Site            514
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:198401"
     CDS             1..578
                     /gene="ANKLE1"
                     /gene_synonym="ANKRD41; LEM3; LEMD6"
                     /coded_by="NM_001278443.2:21..1757"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS92554.1"
                     /db_xref="GeneID:126549"
                     /db_xref="HGNC:HGNC:26812"
                     /db_xref="MIM:619348"
ORIGIN      
        1 mcsearlarr aveellrcga dpnlvledga aavhlaagar hprglrclga llrqggdpna
       61 rsvealtplh vaaawgcrrg lelllsqgad palrdqdglr pldlalqqgh lecarvlqdl
      121 dtrtrtrtri gaetqepepa pgtpglsgpt detldsialq kqpcrgdnrd igleadpgpp
      181 slpvpletvd khgssasppg hwdyssdasf vtavevsgae dpasdtppwa gslpptrqgl
      241 lhvvhanqrv prsqgteael narlqaltlt ppnaagfqss pssmplldrs pahspprtpt
      301 pgasdchclw ehqtsidsdm atlwltedea sstggrepvg pcrhlpvstv sdlellkglr
      361 algpefsghs lelaaalrtg cipdvqaded alaqqfeqpd parrwregvv kssftyllld
      421 pretqdlpar afsltpaerl qtfiraifyv gkgtrarpyv hlwealghhg rsrkqphqac
      481 pkvrqildiw asgcgvvslh cfqhvvavea ytreacivea lgiqtltnqk qghcygvvag
      541 wpparrrrlg vhllhrallv flaegerqlh pqdiqarg
//
LOCUS       NP_787050                887 aa            linear   PRI 27-APR-2025
DEFINITION  PAN2-PAN3 deadenylation complex subunit PAN3 [Homo sapiens].
ACCESSION   NP_787050 NP_001161723
VERSION     NP_787050.6
DBSOURCE    REFSEQ: accession NM_175854.8
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Shang,J., Chen,W.M., Liu,S., Wang,Z.H., Wei,T.N., Chen,Z.Z. and
            Wu,W.B.
  TITLE     CircPAN3 contributes to drug resistance in acute myeloid leukemia
            through regulation of autophagy
  JOURNAL   Leuk Res 85, 106198 (2019)
   PUBMED   31401408
  REMARK    GeneRIF: the present study revealed that circPAN3 is most likely a
            key modulator for acquired drug resistance of AML, which may
            facilitate drug resistance in AML cells by regulating autophagy as
            an autophagy inducer via the AMPK/mTOR pathway.
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Chen,C.A., Zhang,Y., Xiang,Y., Han,L., Chang,J.T. and Shyu,A.B.
  TITLE     Antagonistic actions of two human Pan3 isoforms on global mRNA
            turnover
  JOURNAL   RNA 23 (9), 1404-1418 (2017)
   PUBMED   28559491
  REMARK    GeneRIF: These results reveal a new fundamental step governing
            mammalian mRNA metabolism. We propose that the first phase of
            deadenylation, coordinated through the interplay among the two Pan3
            isoforms, Pan2, and PABP, represents a cytoplasmic mRNA maturation
            step important for proper mRNA turnover.
            Erratum:[RNA. 2018 Nov;24(11):1607-1612. doi:
            10.1261/rna.068387.118. PMID: 30327423]
REFERENCE   4  (residues 1 to 887)
  AUTHORS   Yamagishi,R., Hosoda,N. and Hoshino,S.
  TITLE     Arsenite inhibits mRNA deadenylation through proteolytic
            degradation of Tob and Pan3
  JOURNAL   Biochem Biophys Res Commun 455 (3-4), 323-331 (2014)
   PUBMED   25446091
  REMARK    GeneRIF: arsenite-induced oxidative stress inhibits deadenylation
            of mRNA primarily through downregulation of Tob and Pan3, both of
            which mediate the recruitment of deadenylases to mRNA
REFERENCE   5  (residues 1 to 887)
  AUTHORS   Wolpin,B.M., Rizzato,C., Kraft,P., Kooperberg,C., Petersen,G.M.,
            Wang,Z., Arslan,A.A., Beane-Freeman,L., Bracci,P.M., Buring,J.,
            Canzian,F., Duell,E.J., Gallinger,S., Giles,G.G., Goodman,G.E.,
            Goodman,P.J., Jacobs,E.J., Kamineni,A., Klein,A.P., Kolonel,L.N.,
            Kulke,M.H., Li,D., Malats,N., Olson,S.H., Risch,H.A., Sesso,H.D.,
            Visvanathan,K., White,E., Zheng,W., Abnet,C.C., Albanes,D.,
            Andreotti,G., Austin,M.A., Barfield,R., Basso,D., Berndt,S.I.,
            Boutron-Ruault,M.C., Brotzman,M., Buchler,M.W.,
            Bueno-de-Mesquita,H.B., Bugert,P., Burdette,L., Campa,D.,
            Caporaso,N.E., Capurso,G., Chung,C., Cotterchio,M., Costello,E.,
            Elena,J., Funel,N., Gaziano,J.M., Giese,N.A., Giovannucci,E.L.,
            Goggins,M., Gorman,M.J., Gross,M., Haiman,C.A., Hassan,M.,
            Helzlsouer,K.J., Henderson,B.E., Holly,E.A., Hu,N., Hunter,D.J.,
            Innocenti,F., Jenab,M., Kaaks,R., Key,T.J., Khaw,K.T., Klein,E.A.,
            Kogevinas,M., Krogh,V., Kupcinskas,J., Kurtz,R.C., LaCroix,A.,
            Landi,M.T., Landi,S., Le Marchand,L., Mambrini,A., Mannisto,S.,
            Milne,R.L., Nakamura,Y., Oberg,A.L., Owzar,K., Patel,A.V.,
            Peeters,P.H., Peters,U., Pezzilli,R., Piepoli,A., Porta,M.,
            Real,F.X., Riboli,E., Rothman,N., Scarpa,A., Shu,X.O.,
            Silverman,D.T., Soucek,P., Sund,M., Talar-Wojnarowska,R.,
            Taylor,P.R., Theodoropoulos,G.E., Thornquist,M., Tjonneland,A.,
            Tobias,G.S., Trichopoulos,D., Vodicka,P., Wactawski-Wende,J.,
            Wentzensen,N., Wu,C., Yu,H., Yu,K., Zeleniuch-Jacquotte,A.,
            Hoover,R., Hartge,P., Fuchs,C., Chanock,S.J.,
            Stolzenberg-Solomon,R.S. and Amundadottir,L.T.
  TITLE     Genome-wide association study identifies multiple susceptibility
            loci for pancreatic cancer
  JOURNAL   Nat Genet 46 (9), 994-1000 (2014)
   PUBMED   25086665
REFERENCE   6  (residues 1 to 887)
  AUTHORS   Huang,K.L., Chadee,A.B., Chen,C.Y., Zhang,Y. and Shyu,A.B.
  TITLE     Phosphorylation at intrinsically disordered regions of PAM2
            motif-containing proteins modulates their interactions with PABPC1
            and influences mRNA fate
  JOURNAL   RNA 19 (3), 295-305 (2013)
   PUBMED   23340509
REFERENCE   7  (residues 1 to 887)
  AUTHORS   Braun,J.E., Huntzinger,E., Fauser,M. and Izaurralde,E.
  TITLE     GW182 proteins directly recruit cytoplasmic deadenylase complexes
            to miRNA targets
  JOURNAL   Mol Cell 44 (1), 120-133 (2011)
   PUBMED   21981923
REFERENCE   8  (residues 1 to 887)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   9  (residues 1 to 887)
  AUTHORS   Siddiqui,N., Mangus,D.A., Chang,T.C., Palermino,J.M., Shyu,A.B. and
            Gehring,K.
  TITLE     Poly(A) nuclease interacts with the C-terminal domain of
            polyadenylate-binding protein domain from poly(A)-binding protein
  JOURNAL   J Biol Chem 282 (34), 25067-25075 (2007)
   PUBMED   17595167
REFERENCE   10 (residues 1 to 887)
  AUTHORS   Uchida,N., Hoshino,S. and Katada,T.
  TITLE     Identification of a human cytoplasmic poly(A) nuclease complex
            stimulated by poly(A)-binding protein
  JOURNAL   J Biol Chem 279 (2), 1383-1391 (2004)
   PUBMED   14583602
  REMARK    GeneRIF: hPan2 and hPan3 have roles in mRNA decay and exhibit
            cytoplasmic co-localization
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK296435.1, AB109552.1, AL138712.19 and BE671612.1.
            
            On or before Dec 19, 2009 this sequence version replaced
            NP_001161723.1, NP_787050.5.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380958.8/ ENSP00000370345.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.2"
     Protein         1..887
                     /product="PAN2-PAN3 deadenylation complex subunit PAN3"
                     /EC_number="3.1.13.4"
                     /note="PABP-dependent poly(A) nuclease 3; PAB-dependent
                     poly(A)-specific ribonuclease subunit 3; PABP1-dependent
                     poly A-specific ribonuclease subunit PAN3; PAN3 poly(A)
                     specific ribonuclease subunit homolog; PAB1P-dependent
                     poly(A)-nuclease; PAN deadenylation complex subunit 3;
                     PAB-dependent poly(A)-specific ribonuclease subunit PAN3;
                     PAB1P-dependent poly(A)-specific ribonuclease;
                     poly(A)-nuclease deadenylation complex subunit 3"
                     /calculated_mol_wt=95482
     Region          45..68
                     /region_name="zf-CCCH"
                     /note="Zinc finger C-x8-C-x5-C-x3-H type (and similar);
                     pfam00642"
                     /db_xref="CDD:459885"
     Region          102..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A45.3)"
     Region          147..498
                     /region_name="Necessary and sufficient for interaction
                     with PABPC1 but not needed for interaction with PAN2.
                     /evidence=ECO:0000269|PubMed:28559491"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A45.3)"
     Region          284..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A45.3)"
     Region          284..299
                     /region_name="PABPC-interacting motif-2 (PAM-2).
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03181,
                     ECO:0000269|PubMed:17595167"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A45.3)"
     Region          325..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A45.3)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q58A45.3)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q640Q5; propagated from
                     UniProtKB/Swiss-Prot (Q58A45.3)"
     Region          463..750
                     /region_name="Pseudokinase domain.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03181"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A45.3)"
     Region          493..>661
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(498..501,504,506,519,521,549,565..568,640,644..645,
                     647,657..658)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          <610..733
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          742..879
                     /region_name="Pan3_PK"
                     /note="Pan3 Pseudokinase domain; pfam18101"
                     /db_xref="CDD:465649"
     Region          790..887
                     /region_name="Knob domain.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03181"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58A45.3)"
     CDS             1..887
                     /gene="PAN3"
                     /coded_by="NM_175854.8:114..2777"
                     /db_xref="CCDS:CCDS9329.2"
                     /db_xref="GeneID:255967"
                     /db_xref="HGNC:HGNC:29991"
                     /db_xref="MIM:617448"
ORIGIN      
        1 mnsggglppp saaaspssss laaavavvap pgvggvpgga avgvklkycr yyakdktcfy
       61 geecqflhed paagaapglg lhsnsvplal agapvagfpp gavagggagp ppgpkkpdlg
      121 dpgtgaaagg ggssggldgp rlaipgmdgg altdtsltds yfstsfigvn gfgspvetky
      181 plmqrmtnss sspsllndsa kpysahdplt spasslfndf galnisqrrk prkyrlgmle
      241 erlvpmgska rkaknpigcl adrcksgvpi nmvwwnrvte nnlqtpnpta sefipkggst
      301 srlsnvsqsn msafsqvfsh psmgspatag lapgmslsag ssplhspkit phtspaprrr
      361 shtpnpasym vpssastsvn npvsqtpssg qviqketvgg ttyfytdttp apltgmvfpn
      421 yhiypptaph vaymqpkana psffmadelr qelinrhlit maqidqadmp avptevdsyh
      481 slfpleplpp pnriqkssnf gyitscykav nskddlpycl rrihgfrlvn tkcmvlvdmw
      541 kkiqhsnivt lrevfttkaf aepslvfayd fhaggetmms rhfndpnada yftkrkwgqh
      601 egplprqhag llpesliway ivqlssalrt ihtaglacrv mdptkilitg ktrlrvncvg
      661 vfdvltfdns qnnnplalma qyqqadlisl gkvvlalacn slagiqrenl qkamelvtin
      721 yssdlknlil ylltdqnrmr svndimpmig arfytqldaa qmrndvieed lakevqngrl
      781 frllaklgti nerpefqkdp twsetgdryl lklfrdhlfh qvteagapwi dlshiiscln
      841 kldagvpeki slisrdeksv lvvtysdlkr cfentfqeli aaangql
//
LOCUS       NP_001074805            1180 aa            linear   ROD 27-APR-2025
DEFINITION  diacylglycerol kinase eta isoform 1 [Mus musculus].
ACCESSION   NP_001074805 XP_011243403 XP_900123
VERSION     NP_001074805.2
DBSOURCE    REFSEQ: accession NM_001081336.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1180)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1180)
  AUTHORS   Masuda,Y., Murakami,C., Suzuki,R. and Sakane,F.
  TITLE     Diacylglycerol kinase eta regulates cell proliferation and its
            levels are elevated by glucocorticoids in undifferentiated
            neuroblastoma cells
  JOURNAL   Biochem Biophys Res Commun 602, 41-48 (2022)
   PUBMED   35248948
  REMARK    GeneRIF: Diacylglycerol kinase eta regulates cell proliferation and
            its levels are elevated by glucocorticoids in undifferentiated
            neuroblastoma cells.
REFERENCE   3  (residues 1 to 1180)
  AUTHORS   Asami,M., Suzuki,Y. and Sakane,F.
  TITLE     Dopamine and the phosphorylated dopamine transporter are increased
            in the diacylglycerol kinase eta-knockout mouse brain
  JOURNAL   FEBS Lett 595 (9), 1313-1321 (2021)
   PUBMED   33599293
  REMARK    GeneRIF: Dopamine and the phosphorylated dopamine transporter are
            increased in the diacylglycerol kinase eta-knockout mouse brain.
REFERENCE   4  (residues 1 to 1180)
  AUTHORS   Sakai,H., Murakami,C., Usuki,T., Lu,Q., Matsumoto,K.I., Urano,T.
            and Sakane,F.
  TITLE     Diacylglycerol kinase eta regulates C2C12 myoblast proliferation
            through the mTOR signaling pathway
  JOURNAL   Biochimie 177, 13-24 (2020)
   PUBMED   32791090
  REMARK    GeneRIF: Diacylglycerol kinase eta regulates C2C12 myoblast
            proliferation through the mTOR signaling pathway.
REFERENCE   5  (residues 1 to 1180)
  AUTHORS   Komenoi,S., Suzuki,Y., Asami,M., Murakami,C., Hoshino,F., Chiba,S.,
            Takahashi,D., Kado,S. and Sakane,F.
  TITLE     Microarray analysis of gene expression in the diacylglycerol kinase
            eta knockout mouse brain
  JOURNAL   Biochem Biophys Rep 19, 100660 (2019)
   PUBMED   31297456
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1180)
  AUTHORS   Shionoya,T., Usuki,T., Komenoi,S., Isozaki,T., Sakai,H. and
            Sakane,F.
  TITLE     Distinct expression and localization of the type II diacylglycerol
            kinase isozymes delta, eta and kappa in the mouse reproductive
            organs
  JOURNAL   BMC Dev Biol 15, 6 (2015)
   PUBMED   25613821
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1180)
  AUTHORS   Newbury,A.J. and Rosen,G.D.
  TITLE     Genetic, morphometric, and behavioral factors linked to the
            midsagittal area of the corpus callosum
  JOURNAL   Front Genet 3, 91 (2012)
   PUBMED   22666227
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1180)
  AUTHORS   Eng,S.R., Dykes,I.M., Lanier,J., Fedtsova,N. and Turner,E.E.
  TITLE     POU-domain factor Brn3a regulates both distinct and common programs
            of gene expression in the spinal and trigeminal sensory ganglia
  JOURNAL   Neural Dev 2, 3 (2007)
   PUBMED   17239249
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1180)
  AUTHORS   Crotty,T., Cai,J., Sakane,F., Taketomi,A., Prescott,S.M. and
            Topham,M.K.
  TITLE     Diacylglycerol kinase delta regulates protein kinase C and
            epidermal growth factor receptor signaling
  JOURNAL   Proc Natl Acad Sci U S A 103 (42), 15485-15490 (2006)
   PUBMED   17021016
REFERENCE   10 (residues 1 to 1180)
  AUTHORS   Ghazalpour,A., Doss,S., Zhang,B., Wang,S., Plaisier,C.,
            Castellanos,R., Brozell,A., Schadt,E.E., Drake,T.A., Lusis,A.J. and
            Horvath,S.
  TITLE     Integrating genetic and network analysis to characterize genes
            related to mouse weight
  JOURNAL   PLoS Genet 2 (8), e130 (2006)
   PUBMED   16934000
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC124715.4, AC126251.4 and AC161608.5.
            
            On Feb 17, 2018 this sequence version replaced NP_001074805.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcripts and orthologous alignments from
            human (NM_001204504.1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.5175.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1180
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 41.56 cM"
     Protein         1..1180
                     /product="diacylglycerol kinase eta isoform 1"
                     /EC_number="2.7.1.107"
                     /note="DGK-eta; DAG kinase eta; diglyceride kinase eta"
                     /calculated_mol_wt=129973
     Region          88..184
                     /region_name="PH_DGK_type2"
                     /note="Type 2 Diacylglycerol kinase Pleckstrin homology
                     (PH) domain; cd13274"
                     /db_xref="CDD:270093"
     Region          168..253
                     /region_name="C1_DGKeta_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase eta (DAG kinase
                     eta) and similar proteins; cd20848"
                     /db_xref="CDD:410398"
     Region          264..325
                     /region_name="C1_DGKeta_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase eta (DAG kinase
                     eta) and similar proteins; cd20894"
                     /db_xref="CDD:410444"
     Region          355..477
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          786..943
                     /region_name="DAGKa"
                     /note="Diacylglycerol kinase accessory domain (presumed);
                     smart00045"
                     /db_xref="CDD:214486"
     CDS             1..1180
                     /gene="Dgkh"
                     /gene_synonym="5930402B05Rik; D130015C16; DGK"
                     /coded_by="NM_001081336.2:313..3855"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS36986.2"
                     /db_xref="GeneID:380921"
                     /db_xref="MGI:MGI:2444188"
ORIGIN      
        1 mepqhvrpvl gaqspaweep esermagags qhhpqgvagg avagasavsp taagpgedss
       61 dseaeqegpq klirkvstsg qmrtktsike gqllkqtssf qrwkkryfkl rgrtlyyakd
      121 skslifdevd lsdasvaeas tknannsfti itpfrrlmlc aenrkemevw isslksvqsr
      181 epyevaqfnv ehfsgmhnwy acsharptfc nvcreslsgv tshglscevc kfkahkrcav
      241 ratnnckwtt lasigkdiie dedgvamphq wlegnlpvsa kcavcdktcg svlrlqdwkc
      301 lwcktmvhta ckdvyhpvcp lgqckvsiip pialnstdsd gfcratfsfc vspllvfvns
      361 ksgdnqgvkf lrrfkqllnp aqvfdlmngg pylglrlfqk fdnfrilvcg gdgsvgwvls
      421 eidklnlhkq cqlgvlplgt gndlarvlgw ggsydddtql pqileklera stkmldrwsi
      481 mtyelklpak ssllpepvaa teefymtiye dsvanhltki vnsdehavvi ssakilcetv
      541 kdfvakveka qdrtlentvv aeavaskcsv lnekleqllq alhadsqasr vppgigpaip
      601 eedtvesasd eslgeskdql vndigkpssq kavkpreiml ranslkkavr qvieeaekvm
      661 depavqpsep vspscdydte tdeakeddak eslsakttsq spdaqascgh pqtdsvagpa
      721 mattkenlpv lntriicpgl raglaasiag ssiinkmlla nidpfgatpf idpdldsldg
      781 ysekcvmnny fgigldakis lefnnkreeh pekcrsrtkn lmwygvlgtr ellqrsyknl
      841 eqrvqlecdg qyiplpslqg iavlnipsya ggtnfwggtk eddifaapsf ddkilevvav
      901 fdsvqmavsr viklqhhria qcrtvkitif gdegvpvqvd geawvqppgi ikivhknraq
      961 mltrdrafes tlkswedkqk cdsgkpvlrt nlyihpapdl ateevsqmrl csqaaeelit
     1021 ricdaatihc lleqelahav nacshalnka nprfpesltr dtateiainv kalyneteal
     1081 lvgrvplhle spheervssa lhsvemelqk lteipwlyyi lrpsedeepp ldctkrnnks
     1141 tvfrivpkfk kekaqkqkts sqpgpgdses gsyeanspgn
//
LOCUS       NP_766234                859 aa            linear   ROD 27-APR-2025
DEFINITION  dynamin-3 isoform 2 [Mus musculus].
ACCESSION   NP_766234
VERSION     NP_766234.1
DBSOURCE    REFSEQ: accession NM_172646.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Hanke-Gogokhia,C., Zapadka,T.E., Finkelstein,S., Klingeborn,M.,
            Maugel,T.K., Singer,J.H., Arshavsky,V.Y. and Demb,J.B.
  TITLE     The Structural and Functional Integrity of Rod Photoreceptor Ribbon
            Synapses Depends on Redundant Actions of Dynamins 1 and 3
  JOURNAL   J Neurosci 44 (25), e1379232024 (2024)
   PUBMED   38641407
  REMARK    GeneRIF: The Structural and Functional Integrity of Rod
            Photoreceptor Ribbon Synapses Depends on Redundant Actions of
            Dynamins 1 and 3.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Wu,J., Moriwaki,K., Asuka,T., Nakai,R., Kanda,S., Taniguchi,M.,
            Sugiyama,T., Yoshimura,S.I., Kunii,M., Nagasawa,T., Hosen,N.,
            Miyoshi,E. and Harada,A.
  TITLE     EHBP1L1, an apicobasal polarity regulator, is critical for nuclear
            polarization during enucleation of erythroblasts
  JOURNAL   Blood Adv 7 (14), 3382-3394 (2023)
   PUBMED   37042948
  REMARK    Erratum:[Blood Adv. 2024 Mar 12;8(5):1151. doi:
            10.1182/bloodadvances.2023011838. PMID: 38421726]
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Imoto,Y., Raychaudhuri,S., Ma,Y., Fenske,P., Sandoval,E., Itoh,K.,
            Blumrich,E.M., Matsubayashi,H.T., Mamer,L., Zarebidaki,F.,
            Sohl-Kielczynski,B., Trimbuch,T., Nayak,S., Iwasa,J.H., Liu,J.,
            Wu,B., Ha,T., Inoue,T., Jorgensen,E.M., Cousin,M.A., Rosenmund,C.
            and Watanabe,S.
  TITLE     Dynamin is primed at endocytic sites for ultrafast endocytosis
  JOURNAL   Neuron 110 (17), 2815-2835 (2022)
   PUBMED   35809574
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Yang,S., Park,D., Manning,L., Hill,S.E., Cao,M., Xuan,Z.,
            Gonzalez,I., Dong,Y., Clark,B., Shao,L., Okeke,I.,
            Almoril-Porras,A., Bai,J., De Camilli,P. and Colon-Ramos,D.A.
  TITLE     Presynaptic autophagy is coupled to the synaptic vesicle cycle via
            ATG-9
  JOURNAL   Neuron 110 (5), 824-840 (2022)
   PUBMED   35065714
REFERENCE   5  (residues 1 to 859)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 859)
  AUTHORS   Medrihan,L., Rohlmann,A., Fairless,R., Andrae,J., Doring,M.,
            Missler,M., Zhang,W. and Kilimann,M.W.
  TITLE     Neurobeachin, a protein implicated in membrane protein traffic and
            autism, is required for the formation and functioning of central
            synapses
  JOURNAL   J Physiol 587 (Pt 21), 5095-5106 (2009)
   PUBMED   19723784
REFERENCE   7  (residues 1 to 859)
  AUTHORS   Reems,J.A., Wang,W., Tsubata,K., Abdurrahman,N., Sundell,B.,
            Tijssen,M.R., van der Schoot,E., Di Summa,F., Patel-Hett,S.,
            Italiano,J. Jr. and Gilligan,D.M.
  TITLE     Dynamin 3 participates in the growth and development of
            megakaryocytes
  JOURNAL   Exp Hematol 36 (12), 1714-1727 (2008)
   PUBMED   19007685
  REMARK    GeneRIF: Dynamin 3 participates in the growth and development of
            megakaryocytes.
REFERENCE   8  (residues 1 to 859)
  AUTHORS   Watanabe,T., Sato,T., Amano,T., Kawamura,Y., Kawamura,N.,
            Kawaguchi,H., Yamashita,N., Kurihara,H. and Nakaoka,T.
  TITLE     Dnm3os, a non-coding RNA, is required for normal growth and
            skeletal development in mice
  JOURNAL   Dev Dyn 237 (12), 3738-3748 (2008)
   PUBMED   18985749
REFERENCE   9  (residues 1 to 859)
  AUTHORS   Loebel,D.A., Tsoi,B., Wong,N. and Tam,P.P.
  TITLE     A conserved noncoding intronic transcript at the mouse Dnm3 locus
  JOURNAL   Genomics 85 (6), 782-789 (2005)
   PUBMED   15885504
REFERENCE   10 (residues 1 to 859)
  AUTHORS   Noakes,P.G., Chin,D., Kim,S.S., Liang,S. and Phillips,W.D.
  TITLE     Expression and localisation of dynamin and syntaxin during neural
            development and neuromuscular synapse formation
  JOURNAL   J Comp Neurol 410 (4), 531-540 (1999)
   PUBMED   10398046
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK049724.1, AK046124.1, AK147678.1 and AW047427.1.
            
            Transcript Variant: This variant (2) lacks an exon in the 3' coding
            region, compared to variant 1, and encodes a shorter protein
            (isoform 2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK049724.1, SRR14995047.33611.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 69.95 cM"
     Protein         1..859
                     /product="dynamin-3 isoform 2"
                     /EC_number="3.6.5.5"
                     /note="t-dynamin; testicular dynamin; dynamin III"
                     /calculated_mol_wt=96673
     Region          6..245
                     /region_name="DYNc"
                     /note="Dynamin, GTPase; smart00053"
                     /db_xref="CDD:197491"
     Region          38..45
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Site            38..45
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(39,41..46,59..60,65,136,206,208..209,235..239,242)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(40..41,140,153,178,180,182..185,187..188,209,
                     211..214,238..240)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          64..66
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Site            65
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            69..71
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          136..139
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Site            136..139
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(138..139,169..170)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          205..208
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Site            205..208
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          215..502
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Region          235..238
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Site            235..237
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P39054; propagated from
                     UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Region          514..625
                     /region_name="PH_dynamin"
                     /note="Dynamin pleckstrin homology (PH) domain; cd01256"
                     /db_xref="CDD:269958"
     Site            order(516,518..519,521,538,607..608,611,614..615,618)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:269958"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Site            594
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50570; propagated from
                     UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Region          645..735
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          738..859
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Region          <743..831
                     /region_name="MISS"
                     /note="MAPK-interacting and spindle-stabilising
                     protein-like; pfam15822"
                     /db_xref="CDD:318115"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08877; propagated from
                     UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Site            763
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q8BZ98.1)"
     Site            843
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08877; propagated from
                     UniProtKB/Swiss-Prot (Q8BZ98.1)"
     CDS             1..859
                     /gene="Dnm3"
                     /gene_synonym="9630020E24Rik; B230343F03Rik; C530045C17;
                     Dyna III; mKIAA0820"
                     /coded_by="NM_172646.3:212..2791"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS48417.1"
                     /db_xref="GeneID:103967"
                     /db_xref="MGI:MGI:1341299"
ORIGIN      
        1 mgnremeeli plvnrlqdaf salgqsclle lpqiavvggq sagkssvlen fvgrdflprg
       61 sgivtrrplv lqlvtskaey aeflhckgkk ftdfdevrhe ieaetdrvtg mnkgissipi
      121 nlrvysphvl nltlidlpgi tkvpvgdqpp dieyqirdmi mqfitrencl ilavtpantd
      181 lansdalkla kevdpqglrt igvitkldlm degtdardvl enkllplrrg yvgvvnrsqk
      241 didgkkdika amlaerkffl shpayrhiad rmgtphlqkv lnqqltnhir dtlpnfrnkl
      301 qgqllsiehe veafknfkpe dptrktkall qmvqqfavdf ekriegsgdq vdtlelsgga
      361 kinrifherf pfeivkmefn ekelrreisy aiknihgirt glftpdmafe aivkkqivkl
      421 kgpslksvdl vmqelintvk kctkrlanfp rlceeteriv anhireregk tkdqvlllid
      481 iqvsyintnh edfigfanaq qrssqvhkks tignqvirkg wltvsnigim kggskgywfv
      541 ltaeslswyk ddeekekkym lpldnlkvrd vekgfmsskh vfalfnteqr nvykdyrfle
      601 lacdsqedvd swkasllrag vypdksvten dengqaenfs mdpqlerqve tirnlvdsym
      661 siinkcirdl ipktimhlmi nnvkdfinse llaqlyssed qntlmeesae qaqrrdemlr
      721 myqalkeala iigdintatv stpapppvdd swlqhsrrsp ppspttqrrl tisaplprpt
      781 sgrgpapaip spgphsgapp vpfrpgplpp fpnssdsfga ppqvpsrptr appsvpsrrp
      841 ppsptrptii rplesslld
//
LOCUS       NP_005611                105 aa            linear   PRI 27-APR-2025
DEFINITION  protein S100-A11 [Homo sapiens].
ACCESSION   NP_005611
VERSION     NP_005611.1
DBSOURCE    REFSEQ: accession NM_005620.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Deng,C., Xu,Y., Chen,H., Zhu,X., Huang,L., Chen,Z., Xu,H., Song,G.,
            Lu,J., Huang,W., Liu,R., Tang,Q. and Wang,J.
  TITLE     Extracellular-vesicle-packaged S100A11 from osteosarcoma cells
            mediates lung premetastatic niche formation by recruiting gMDSCs
  JOURNAL   Cell Rep 43 (2), 113751 (2024)
   PUBMED   38341855
  REMARK    GeneRIF: Extracellular-vesicle-packaged S100A11 from osteosarcoma
            cells mediates lung premetastatic niche formation by recruiting
            gMDSCs.
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Han,D., Guo,C., Cheng,H., Lu,J., Hou,Z., Zhang,X., Luo,Y.,
            Zhang,B., Zhao,W. and Shang,P.
  TITLE     Downregulation of S100A11 promotes T cell infiltration by
            regulating cancer-associated fibroblasts in prostate cancer
  JOURNAL   Int Immunopharmacol 128, 111323 (2024)
   PUBMED   38286714
  REMARK    GeneRIF: Downregulation of S100A11 promotes T cell infiltration by
            regulating cancer-associated fibroblasts in prostate cancer.
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Zhou,R., Pei,B., Li,X. and Zhang,X.
  TITLE     Involvement of S100A6/S100A11 in T-Cell Immune Regulatory in HCC
            Revealed by Single Cell RNA-seq
  JOURNAL   Technol Cancer Res Treat 23, 15330338241252610 (2024)
   PUBMED   38766816
  REMARK    GeneRIF: Involvement of S100A6/S100A11 in T-Cell Immune Regulatory
            in HCC Revealed by Single Cell RNA-seq.
REFERENCE   4  (residues 1 to 105)
  AUTHORS   He,J., Lei,Y., Li,X., Wu,B. and Tang,Y.
  TITLE     Exploring the prognostic value of S100A11 and its association with
            immune infiltration in breast cancer
  JOURNAL   Sci Rep 13 (1), 22922 (2023)
   PUBMED   38129538
  REMARK    GeneRIF: Exploring the prognostic value of S100A11 and its
            association with immune infiltration in breast cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Zheng,M., Meng,H., Li,Y., Shi,J., Han,Y., Zhao,C., Chen,J., Han,J.,
            Liang,J., Chen,Y., Liu,Q. and Wang,Y.
  TITLE     S100A11 Promotes Metastasis via AKT and ERK Signaling Pathways and
            Has a Diagnostic Role in Hepatocellular Carcinoma
  JOURNAL   Int J Med Sci 20 (3), 318-328 (2023)
   PUBMED   36860671
  REMARK    GeneRIF: S100A11 Promotes Metastasis via AKT and ERK Signaling
            Pathways and Has a Diagnostic Role in Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Mailliard,W.S., Haigler,H.T. and Schlaepfer,D.D.
  TITLE     Calcium-dependent binding of S100C to the N-terminal domain of
            annexin I
  JOURNAL   J Biol Chem 271 (2), 719-725 (1996)
   PUBMED   8557678
REFERENCE   7  (residues 1 to 105)
  AUTHORS   Tomasetto,C., Regnier,C., Moog-Lutz,C., Mattei,M.G., Chenard,M.P.,
            Lidereau,R., Basset,P. and Rio,M.C.
  TITLE     Identification of four novel human genes amplified and
            overexpressed in breast carcinoma and localized to the q11-q21.3
            region of chromosome 17
  JOURNAL   Genomics 28 (3), 367-376 (1995)
   PUBMED   7490069
REFERENCE   8  (residues 1 to 105)
  AUTHORS   Tanaka,M., Adzuma,K., Iwami,M., Yoshimoto,K., Monden,Y. and
            Itakura,M.
  TITLE     Human calgizzarin; one colorectal cancer-related gene selected by a
            large scale random cDNA sequencing and northern blot analysis
  JOURNAL   Cancer Lett 89 (2), 195-200 (1995)
   PUBMED   7889529
REFERENCE   9  (residues 1 to 105)
  AUTHORS   Schafer,B.W., Wicki,R., Engelkamp,D., Mattei,M.G. and Heizmann,C.W.
  TITLE     Isolation of a YAC clone covering a cluster of nine S100 genes on
            human chromosome 1q21: rationale for a new nomenclature of the S100
            calcium-binding protein family
  JOURNAL   Genomics 25 (3), 638-643 (1995)
   PUBMED   7759097
REFERENCE   10 (residues 1 to 105)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D38583.1.
            
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21. This protein may function
            in motility, invasion, and tubulin polymerization. Chromosomal
            rearrangements and altered expression of this gene have been
            implicated in tumor metastasis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP305686.1, D38583.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000271638.3/ ENSP00000271638.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..105
                     /product="protein S100-A11"
                     /note="calgizzarin; MLN 70; protein S100-C; metastatic
                     lymph node gene 70 protein; epididymis secretory protein
                     Li 43"
                     /calculated_mol_wt=11609
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P31949.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine, in Protein S100-A11, N-terminally
                     processed. /evidence=ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P31949.2)"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31949.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P31949.2)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31949.2)"
     Region          7..95
                     /region_name="S-100A11"
                     /note="S-100A11 domain found in proteins similar to
                     S100A11. S100A11 is a member of the S-100 domain family
                     within EF-hand Ca2+-binding proteins superfamily. Note
                     that the S-100 hierarchy, to which this S-100A11 group
                     belongs, contains only S-100 EF-hand...; cd05023"
                     /db_xref="CDD:240150"
     Site            order(8,10..11,13..18,20..22,32,42,46..50,77..78,81..82,
                     84..86,88..89,92..95)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240150"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18618420; propagated from
                     UniProtKB/Swiss-Prot (P31949.2)"
     Site            order(25,28,30,33,38,68,70,72,74,79)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:240150"
     Region          25..38
                     /region_name="Calcium binding region"
     Site            27
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50543; propagated from
                     UniProtKB/Swiss-Prot (P31949.2)"
     Site            order(47,49..50,53..54,59,87,90..91,94..95)
                     /site_type="active"
                     /note="annexin I binding site [active]"
                     /db_xref="CDD:240150"
     Region          68..79
                     /region_name="Calcium binding region"
     CDS             1..105
                     /gene="S100A11"
                     /gene_synonym="HEL-S-43; MLN70; S100C"
                     /coded_by="NM_005620.2:90..407"
                     /db_xref="CCDS:CCDS1009.1"
                     /db_xref="GeneID:6282"
                     /db_xref="HGNC:HGNC:10488"
                     /db_xref="MIM:603114"
ORIGIN      
        1 makissptet erciesliav fqkyagkdgy nytlsktefl sfmntelaaf tknqkdpgvl
       61 drmmkkldtn sdgqldfsef lnligglama chdsflkavp sqkrt
//
LOCUS       NP_077140                217 aa            linear   ROD 27-APR-2025
DEFINITION  UDP-N-acetylglucosamine transferase subunit ALG14 [Mus musculus].
ACCESSION   NP_077140
VERSION     NP_077140.1
DBSOURCE    REFSEQ: accession NM_024178.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC161210.5 and AC105336.14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK011733.1, BC002278.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3 52.94 cM"
     Protein         1..217
                     /product="UDP-N-acetylglucosamine transferase subunit
                     ALG14"
                     /note="UDP-N-acetylglucosamine transferase subunit ALG14
                     homolog; asparagine-linked glycosylation 14 homolog"
                     /calculated_mol_wt=24298
     Site            4..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D081.1)"
     Region          39..216
                     /region_name="Alg14"
                     /note="Oligosaccharide biosynthesis protein Alg14 like;
                     pfam08660"
                     /db_xref="CDD:370045"
     CDS             1..217
                     /gene="Alg14"
                     /gene_synonym="5430428G01Rik"
                     /coded_by="NM_024178.3:109..762"
                     /db_xref="CCDS:CCDS17801.1"
                     /db_xref="GeneID:66789"
                     /db_xref="MGI:MGI:1914039"
ORIGIN      
        1 mlsililaat aaglvillfq rlwtvlgphh vtpreslrll ivagsgghtt eilrlvgsls
       61 naysprhyvi aesdemsakk ihsleelsra qndstteypk yhlhriprsr evrqswlssv
      121 fttfysmwfs fplvlrikpd lvlcngpgtc vpicvsalll gilgvkkvii vyvesicrve
      181 tlslsgkilr hlsdyfivqw ptlkekypks vylgriv
//
LOCUS       NP_003558                825 aa            linear   PRI 27-APR-2025
DEFINITION  breast cancer anti-estrogen resistance protein 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_003558
VERSION     NP_003558.1
DBSOURCE    REFSEQ: accession NM_003567.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Zhao,G., Chen,H. and Luo,J.
  TITLE     CircBCAR3 sponges miR-27a-3p and mediates ferroptosis in human
            B-prolymphocytic leukaemia cells via SLC7A11
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (12), 181-187 (2023)
   PUBMED   38063095
  REMARK    GeneRIF: CircBCAR3 sponges miR-27a-3p and mediates ferroptosis in
            human B-prolymphocytic leukaemia cells via SLC7A11.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Pavanelli,A.C., Mangone,F.R., Yoganathan,P., Bessa,S.A.,
            Nonogaki,S., de Toledo Osorio,C.A.B., de Andrade,V.P., Soares,I.C.,
            de Mello,E.S., Mulligan,L.M. and Nagai,M.A.
  TITLE     Comprehensive immunohistochemical analysis of RET, BCAR1, and BCAR3
            expression in patients with Luminal A and B breast cancer subtypes
  JOURNAL   Breast Cancer Res Treat 192 (1), 43-52 (2022)
   PUBMED   35031902
  REMARK    GeneRIF: Comprehensive immunohistochemical analysis of RET, BCAR1,
            and BCAR3 expression in patients with Luminal A and B breast cancer
            subtypes.
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Steenkiste,E.M., Berndt,J.D., Pilling,C., Simpkins,C. and
            Cooper,J.A.
  TITLE     A Cas-BCAR3 co-regulatory circuit controls lamellipodia dynamics
  JOURNAL   Elife 10, e67078 (2021)
   PUBMED   34169835
  REMARK    GeneRIF: A Cas-BCAR3 co-regulatory circuit controls lamellipodia
            dynamics.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Cai,D., Felekkis,K.N., Near,R.I., O'Neill,G.M., van Seventer,J.M.,
            Golemis,E.A. and Lerner,A.
  TITLE     The GDP exchange factor AND-34 is expressed in B cells, associates
            with HEF1, and activates Cdc42
  JOURNAL   J Immunol 170 (2), 969-978 (2003)
   PUBMED   12517963
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Lu,Y., Brush,J. and Stewart,T.A.
  TITLE     NSP1 defines a novel family of adaptor proteins linking integrin
            and tyrosine kinase receptors to the c-Jun N-terminal
            kinase/stress-activated protein kinase signaling pathway
  JOURNAL   J Biol Chem 274 (15), 10047-10052 (1999)
   PUBMED   10187783
REFERENCE   8  (residues 1 to 825)
  AUTHORS   van Agthoven,T., van Agthoven,T.L., Dekker,A., van der Spek,P.J.,
            Vreede,L. and Dorssers,L.C.
  TITLE     Identification of BCAR3 by a random search for genes involved in
            antiestrogen resistance of human breast cancer cells
  JOURNAL   EMBO J 17 (10), 2799-2808 (1998)
   PUBMED   9582273
REFERENCE   9  (residues 1 to 825)
  AUTHORS   Johnston,S.R.
  TITLE     Acquired tamoxifen resistance in human breast cancer--potential
            mechanisms and clinical implications
  JOURNAL   Anticancer Drugs 8 (10), 911-930 (1997)
   PUBMED   9436634
  REMARK    Review article
REFERENCE   10 (residues 1 to 825)
  AUTHORS   Dorssers,L.C. and van Agthoven,T.
  TITLE     Genetic mechanisms of estrogen-independence in breast cancer
  JOURNAL   Pathol Res Pract 192 (7), 743-751 (1996)
   PUBMED   8880875
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN337133.1, AF124250.1,
            BQ015705.1 and AL109613.11.
            
            Summary: Breast tumors are initially dependent on estrogens for
            growth and progression and can be inhibited by anti-estrogens such
            as tamoxifen. However, breast cancers progress to become
            anti-estrogen resistant. Breast cancer anti-estrogen resistance
            gene 3 was identified in the search for genes involved in the
            development of estrogen resistance. The gene encodes a component of
            intracellular signal transduction that causes estrogen-independent
            proliferation in human breast cancer cells. The protein contains a
            putative src homology 2 (SH2) domain, a hall mark of cellular
            tyrosine kinase signaling molecules, and is partly homologous to
            the cell division cycle protein CDC48. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein (isoform
            1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF124250.1, GQ891488.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260502.11/ ENSP00000260502.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..825
                     /product="breast cancer anti-estrogen resistance protein 3
                     isoform 1"
                     /note="breast cancer anti-estrogen resistance protein 3;
                     dJ1033H22.2 (breast cancer anti-estrogen resistance 3);
                     novel SH2-containing protein 2; SH2 domain-containing
                     protein 3B; breast cancer antiestrogen resistance 3
                     protein; epididymis secretory sperm binding protein;
                     BCAR3, NSP family adaptor protein; mig-7; migration
                     inducting gene-7"
                     /calculated_mol_wt=92435
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Region          40..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75815.1)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Region          147..282
                     /region_name="SH2_BCAR3"
                     /note="Src homology 2 (SH2) domain in the Breast Cancer
                     Anti-estrogen Resistance protein 3; cd10337"
                     /db_xref="CDD:198200"
     Site            order(161,177,198,200)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198200"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Site            order(199,234)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198200"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Site            334
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75815.1)"
     Site            442
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZK2; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     Region          544..819
                     /region_name="RasGEF"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     small GTPases; smart00147"
                     /db_xref="CDD:214539"
     Site            order(579..581,595..596,598..600,602..603,606..607,610,
                     645,648..649,651..653,655..658,660..661,678,683..685,688,
                     709..711,714..716,718..720,722..725,739,743,784,787..788)
                     /site_type="other"
                     /note="Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:238087"
     Region          744..748
                     /region_name="Mediates the interaction with BCAR1/p130CAS.
                     /evidence=ECO:0000305|PubMed:22081014"
                     /note="propagated from UniProtKB/Swiss-Prot (O75815.1)"
     Site            748
                     /site_type="other"
                     /note="Required for interaction with NEDD9.
                     /evidence=ECO:0000250|UniProtKB:Q9QZK2; propagated from
                     UniProtKB/Swiss-Prot (O75815.1)"
     CDS             1..825
                     /gene="BCAR3"
                     /gene_synonym="AND-34; MIG7; NSP2; SH2D3B"
                     /coded_by="NM_003567.4:252..2729"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS745.1"
                     /db_xref="GeneID:8412"
                     /db_xref="HGNC:HGNC:973"
                     /db_xref="MIM:604704"
ORIGIN      
        1 maagkfaslp rnmpvnhqfp lassmdllss rsplaehrpd ayqdvsihgt lprkkkgppp
       61 irscddfshm gtlphskspr qnspvtqdgi qespwqdrhg etftfrdphl ldptveyvkf
      121 skerhimdrt peklkkelee elllssedlr shawyhgrip rqvsenlvqr dgdflvrdsl
      181 sspgnfvltc qwknlaqhfk inrtvlrlse aysrvqyqfe mesfdsipgl vrcyvgnrrp
      241 isqqsgaiif qpinrtvplr cleehygtsp gqaregsltk grpdvakrls ltmggvqare
      301 qnlprgnllr nkeksgsqpa cldhmqdrra lslkahqses ylpigcklpp qssgvdtspc
      361 pnspvfrtgs epalspavvr rvssdarage alrgsdsqlc pkpppkpckv pflkvpssps
      421 awlnseanyc elnpafatgc grgaklpsca qgshtellta kqneapgprn sgvnylildd
      481 ddrerpwepa aaqmekgqwd kgefvtplle tvssfrpnef eskflppenk pletamlkra
      541 kelftnndpk viaqhvlsmd crvarilgvs eemrrnmgvs sglelitlph ghqlrldiie
      601 rhntmaigia vdilgctgtl edraatlski iqvavelkds mgdlysfsal mkalempqit
      661 rlektwtalr hqytqtaily ekqlkpfskl lhegrestcv ppnnvsvpll mplvtlmerq
      721 avtfegtdmw ekndqsceim lnhlatarfm aeaadsyrmn aerilagfqp deemneickt
      781 efqmrllwgs kgaqvnqter yekfnqilta lsrklepppv kqael
//
LOCUS       NP_115985                262 aa            linear   PRI 27-APR-2025
DEFINITION  sperm microtubule inner protein 6 isoform 1 [Homo sapiens].
ACCESSION   NP_115985
VERSION     NP_115985.2
DBSOURCE    REFSEQ: accession NM_032596.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Leung,M.R., Zeng,J., Wang,X., Roelofs,M.C., Huang,W., Zenezini
            Chiozzi,R., Hevler,J.F., Heck,A.J.R., Dutcher,S.K., Brown,A.,
            Zhang,R. and Zeev-Ben-Mordehai,T.
  TITLE     Structural specializations of the sperm tail
  JOURNAL   Cell 186 (13), 2880-2896 (2023)
   PUBMED   37327785
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Pleuger,C., Fietz,D., Hartmann,K., Schuppe,H.C., Weidner,W.,
            Kliesch,S., Baker,M., O'Bryan,M.K. and Bergmann,M.
  TITLE     Expression of ciliated bronchial epithelium 1 during human
            spermatogenesis
  JOURNAL   Fertil Steril 108 (1), 47-54 (2017)
   PUBMED   28601408
  REMARK    GeneRIF: Our data strongly suggest an influence of CBE1 in
            ciliogenesis in spermatids due to the localization at the
            microtubules of the elongating spermatids, indicating a role in the
            intramanchette and/or intraflagellar transport mechanism.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Haitchi,H.M., Yoshisue,H., Ribbene,A., Wilson,S.J., Holloway,J.W.,
            Bucchieri,F., Hanley,N.A., Wilson,D.I., Zummo,G., Holgate,S.T. and
            Davies,D.E.
  TITLE     Chronological expression of Ciliated Bronchial Epithelium 1 during
            pulmonary development
  JOURNAL   Eur Respir J 33 (5), 1095-1104 (2009)
   PUBMED   19213785
  REMARK    GeneRIF: Chronological regulation of CBE1/Cbe1 expression during
            pulmonary differentiation suggests involvement in ciliogenesis,
            with an additional role during early lung development.
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Matsuoka,Y., Miyagawa,Y., Tokuhiro,K., Kitamura,K., Iguchi,N.,
            Maekawa,M., Takahashi,T., Tsujimura,A., Matsumiya,K., Okuyama,A.,
            Nishimune,Y. and Tanaka,H.
  TITLE     Isolation and characterization of the spermatid-specific Smrp1 gene
            encoding a novel manchette protein
  JOURNAL   Mol Reprod Dev 75 (6), 967-975 (2008)
   PUBMED   18163442
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Pope,S.N. and Lee,I.R.
  TITLE     Yeast two-hybrid identification of prostatic proteins interacting
            with human sex hormone-binding globulin
  JOURNAL   J Steroid Biochem Mol Biol 94 (1-3), 203-208 (2005)
   PUBMED   15862967
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Yoshisue,H., Puddicombe,S.M., Wilson,S.J., Haitchi,H.M.,
            Powell,R.M., Wilson,D.I., Pandit,A., Berger,A.E., Davies,D.E.,
            Holgate,S.T. and Holloway,J.W.
  TITLE     Characterization of ciliated bronchial epithelium 1, a ciliated
            cell-associated gene induced during mucociliary differentiation
  JOURNAL   Am J Respir Cell Mol Biol 31 (5), 491-500 (2004)
   PUBMED   15242845
  REMARK    GeneRIF: CBE1 may play an important role in the differentiation
            and/or function of ciliated cells in human airways
REFERENCE   9  (residues 1 to 262)
  AUTHORS   Sha,J., Zhou,Z., Li,J., Yin,L., Yang,H., Hu,G., Luo,M., Chan,H.C.
            and Zhou,K.
  CONSRTM   Spermatogenesis study group
  TITLE     Identification of testis development and spermatogenesis-related
            genes in human and mouse testes using cDNA arrays
  JOURNAL   Mol Hum Reprod 8 (6), 511-517 (2002)
   PUBMED   12029067
REFERENCE   10 (residues 1 to 262)
  AUTHORS   Adams,M.D., Soares,M.B., Kerlavage,A.R., Fields,C. and Venter,J.C.
  TITLE     Rapid cDNA sequencing (expressed sequence tags) from a
            directionally cloned human infant brain cDNA library
  JOURNAL   Nat Genet 4 (4), 373-380 (1993)
   PUBMED   8401585
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC029484.1 and AK058087.1.
            
            On Jun 10, 2002 this sequence version replaced NP_115985.1.
            
            Summary: This gene encodes a nuclear- or perinuclear-localized
            protein with no predicted domains or similarity to other known
            proteins. Expression of this gene is induced during the
            differentiation of bronchial epithelial cells, and the encoded
            protein may play a role in ciliogenesis. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Nov 2011].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022084.1, SRR5189667.362332.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297623.7/ ENSP00000297623.2
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..262
                     /product="sperm microtubule inner protein 6 isoform 1"
                     /note="ciliated bronchial epithelium 1; testis development
                     protein NYD-SP22; ciliated bronchial epithelial protein 1;
                     spermatid-specific manchette-related protein 1"
                     /calculated_mol_wt=30036
     Region          1..262
                     /region_name="SMRP1"
                     /note="Spermatid-specific manchette-related protein 1;
                     pfam15181"
                     /db_xref="CDD:464548"
     CDS             1..262
                     /gene="SPMIP6"
                     /gene_synonym="bA573M23.4; C9orf24; CBE1; NYD-SP22; SMRP1"
                     /coded_by="NM_032596.4:178..966"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6554.1"
                     /db_xref="GeneID:84688"
                     /db_xref="HGNC:HGNC:19919"
                     /db_xref="MIM:619502"
ORIGIN      
        1 mflfsrktrt pistysdsyr aptsikevyk dpplcawean kfltpgltht merhvdpeal
       61 qkmakcavqd ytyrgsisgh pylpekywls qeeadkcspn ylgsdwyntw rmepynsscc
      121 nkyttylprl pkearmetav rgmplecppr perlnayere vmvnmlnsls rnqqlpritp
      181 rcgcvdplpg rlpfhgyesa csgrhyclrg mdyyasgapc tdrrlrpwcr eqptmctslr
      241 aparnavccy nspavilpis ep
//
LOCUS       NP_620058                 77 aa            linear   PRI 27-APR-2025
DEFINITION  high mobility group nucleosome-binding domain-containing protein 3
            isoform b [Homo sapiens].
ACCESSION   NP_620058
VERSION     NP_620058.1
DBSOURCE    REFSEQ: accession NM_138730.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Bian,Y., Li,J., Shen,H., Li,Y., Hou,Y., Huang,L., Song,G. and
            Qiao,C.
  TITLE     WTAP dysregulation-mediated HMGN3-m6A modification inhibited
            trophoblast invasion in early-onset preeclampsia
  JOURNAL   FASEB J 36 (12), e22617 (2022)
   PUBMED   36412513
  REMARK    GeneRIF: WTAP dysregulation-mediated HMGN3-m6A modification
            inhibited trophoblast invasion in early-onset preeclampsia.
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Sorin,S., Kubota,S., Hamidi,S., Yokomizo-Nakano,T.,
            Vaeteewoottacharn,K., Wongkham,S., Waraasawapati,S., Pairojkul,C.,
            Bai,J., Morii,M., Sheng,G., Sawanyawisuth,K. and Sashida,G.
  TITLE     HMGN3 represses transcription of epithelial regulators to promote
            migration of cholangiocarcinoma in a SNAI2-dependent manner
  JOURNAL   FASEB J 36 (7), e22345 (2022)
   PUBMED   35635715
  REMARK    GeneRIF: HMGN3 represses transcription of epithelial regulators to
            promote migration of cholangiocarcinoma in a SNAI2-dependent
            manner.
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Koh,M., Ahmad,I., Ko,Y., Zhang,Y., Martinez,T.F., Diedrich,J.K.,
            Chu,Q., Moresco,J.J., Erb,M.A., Saghatelian,A., Schultz,P.G. and
            Bollong,M.J.
  TITLE     A short ORF-encoded transcriptional regulator
  JOURNAL   Proc Natl Acad Sci U S A 118 (4) (2021)
   PUBMED   33468658
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Lei,S.F., Shen,H., Yang,T.L., Guo,Y., Dong,S.S., Xu,X.H.,
            Deng,F.Y., Tian,Q., Liu,Y.J., Liu,Y.Z., Li,J. and Deng,H.W.
  TITLE     Genome-wide association study identifies HMGN3 locus for spine bone
            size variation in Chinese
  JOURNAL   Hum Genet 131 (3), 463-469 (2012)
   PUBMED   21947420
  REMARK    GeneRIF: The SNPs in the region of HMGN3 gene formed a tightly
            combined haplotype block in both Chinese and Caucasians. The
            results suggest that the genomic region containing HMGN3 gene may
            be associated with spine BS in Chinese.
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Ueda,T., Furusawa,T., Kurahashi,T., Tessarollo,L. and Bustin,M.
  TITLE     The nucleosome binding protein HMGN3 modulates the transcription
            profile of pancreatic beta cells and affects insulin secretion
  JOURNAL   Mol Cell Biol 29 (19), 5264-5276 (2009)
   PUBMED   19651901
  REMARK    GeneRIF: loss of HMGN3 impairs glucose-stimulated insulin secretion
            and leads to a diabetic phenotype.
REFERENCE   6  (residues 1 to 77)
  AUTHORS   West,K.L., Castellini,M.A., Duncan,M.K. and Bustin,M.
  TITLE     Chromosomal proteins HMGN3a and HMGN3b regulate the expression of
            glycine transporter 1
  JOURNAL   Mol Cell Biol 24 (9), 3747-3756 (2004)
   PUBMED   15082770
REFERENCE   7  (residues 1 to 77)
  AUTHORS   Leong,P.W., Liew,K., Lim,W. and Chow,V.T.
  TITLE     Differential display RT-PCR analysis of enterovirus-71-infected
            rhabdomyosarcoma cells reveals mRNA expression responses of
            multiple human genes with known and novel functions
  JOURNAL   Virology 295 (1), 147-159 (2002)
   PUBMED   12033773
REFERENCE   8  (residues 1 to 77)
  AUTHORS   West,K.L., Ito,Y., Birger,Y., Postnikov,Y., Shirakawa,H. and
            Bustin,M.
  TITLE     HMGN3a and HMGN3b, two protein isoforms with a tissue-specific
            expression pattern, expand the cellular repertoire of
            nucleosome-binding proteins
  JOURNAL   J Biol Chem 276 (28), 25959-25969 (2001)
   PUBMED   11356838
REFERENCE   9  (residues 1 to 77)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355796.11.
            
            Summary: The protein encoded by this gene binds thyroid hormone
            receptor beta in the presence of thyroid hormone. The encoded
            protein, a member of the HMGN protein family, is thought to reduce
            the compactness of the chromatin fiber in nucleosomes, thereby
            enhancing transcription from chromatin templates. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. There is a related pseudogene on chromosome 1.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region, which results in a frameshift, compared to
            variant 1. The resulting isoform (b) is shorter and has a distinct
            C-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.9821.1,
                                           SRR1803612.385916.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267752, SAMN03267760
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..77
                     /product="high mobility group nucleosome-binding
                     domain-containing protein 3 isoform b"
                     /note="thyroid hormone receptor interacting protein 7;
                     high mobility group nucleosome-binding domain-containing
                     protein 3; TR-interacting protein 7"
                     /calculated_mol_wt=8246
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15651.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q15651.2)"
     CDS             1..77
                     /gene="HMGN3"
                     /gene_synonym="PNAS-24; PNAS-25; TRIP7"
                     /coded_by="NM_138730.3:123..356"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4989.1"
                     /db_xref="GeneID:9324"
                     /db_xref="HGNC:HGNC:12312"
                     /db_xref="MIM:604502"
ORIGIN      
        1 mpkrkspent egkdgskvtk qeptrrsarl sakpappkpe pkprktsakk epgakisrga
       61 kgkkeekqea gkegten
//
LOCUS       NP_001348491             348 aa            linear   ROD 27-APR-2025
DEFINITION  IST1 homolog isoform 2 [Mus musculus].
ACCESSION   NP_001348491 XP_017168459
VERSION     NP_001348491.1
DBSOURCE    REFSEQ: accession NM_001361562.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Tang,Q., Fang,Z., Liao,H., Zhang,Y., Li,C., Zhou,C., Liu,F. and
            Shen,J.
  TITLE     Reduced circ_lrrc49 in trigeminal ganglion contributes to
            neuropathic pain in mice by downregulating Ist1 and impairing
            autophagy
  JOURNAL   J Neurochem 168 (7), 1265-1280 (2024)
   PUBMED   38348636
  REMARK    GeneRIF: Reduced circ_lrrc49 in trigeminal ganglion contributes to
            neuropathic pain in mice by downregulating Ist1 and impairing
            autophagy.
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Hermosilla Aguayo,V., Martin,P., Tian,N., Zheng,J., Aho,R., Losa,M.
            and Selleri,L.
  TITLE     ESCRT-dependent control of craniofacial morphogenesis with
            concomitant perturbation of NOTCH signaling
  JOURNAL   Dev Biol 503, 25-42 (2023)
   PUBMED   37573008
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Feng,Q., Luo,Y., Zhang,X.N., Yang,X.F., Hong,X.Y., Sun,D.S.,
            Li,X.C., Hu,Y., Li,X.G., Zhang,J.F., Li,X., Yang,Y., Wang,Q.,
            Liu,G.P. and Wang,J.Z.
  TITLE     MAPT/Tau accumulation represses autophagy flux by disrupting
            IST1-regulated ESCRT-III complex formation: a vicious cycle in
            Alzheimer neurodegeneration
  JOURNAL   Autophagy 16 (4), 641-658 (2020)
   PUBMED   31223056
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Nakahara,M., Tateyama,H., Araki,M., Nakagata,N., Yamamura,K. and
            Araki,K.
  TITLE     Gene-trap mutagenesis using Mol/MSM-1 embryonic stem cells from
            MSM/Ms mice
  JOURNAL   Mamm Genome 24 (5-6), 228-239 (2013)
   PUBMED   23604909
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Hanson,P.I., Roth,R., Lin,Y. and Heuser,J.E.
  TITLE     Plasma membrane deformation by circular arrays of ESCRT-III protein
            filaments
  JOURNAL   J Cell Biol 180 (2), 389-402 (2008)
   PUBMED   18209100
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Taniwaki,T., Haruna,K., Nakamura,H., Sekimoto,T., Oike,Y.,
            Imaizumi,T., Saito,F., Muta,M., Soejima,Y., Utoh,A., Nakagata,N.,
            Araki,M., Yamamura,K. and Araki,K.
  TITLE     Characterization of an exchangeable gene trap using pU-17 carrying
            a stop codon-beta geo cassette
  JOURNAL   Dev Growth Differ 47 (3), 163-172 (2005)
   PUBMED   15840001
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Aizawa,H., Yuasa,S.,
            Nakajima,D., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: II. The complete nucleotide sequences of 400 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (1), 35-48 (2003)
   PUBMED   12693553
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125162.4.
            
            On Mar 29, 2018 this sequence version replaced XP_017168459.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            segment compared to variant 1. The resulting isoform (2) has the
            same N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849380,
                              SAMN00849381 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 57.18 cM"
     Protein         1..348
                     /product="IST1 homolog isoform 2"
                     /note="IST1 homolog; charged multivesicular body protein
                     8"
                     /calculated_mol_wt=37907
     Region          12..176
                     /region_name="Ist1"
                     /note="Regulator of Vps4 activity in the MVB pathway;
                     pfam03398"
                     /db_xref="CDD:460910"
     CDS             1..348
                     /gene="Ist1"
                     /gene_synonym="2400003C14Rik; CHMP8; mKIAA0174"
                     /coded_by="NM_001361562.1:127..1173"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:71955"
                     /db_xref="MGI:MGI:1919205"
ORIGIN      
        1 mlgsgfkaer lrvnlrlvin rlkllekkkt elaqkarkei adylaagkde rarirvehii
       61 redylveame ilelycdlll arfgliqsmk eldsglaesv stliwaaprl qsevaelkiv
      121 adqlcakysk eygklcrtnq igtvndrlmh klsveappki lverylieia knynvpyepd
      181 svvmaeapvg vetdlidvgf tddvkkggpg rgggggftap vggpdgivpm pmpmpmpspn
      241 apfayplpkg psdfsglpvg tyqafpnihp pqipatppsy esivgpkpea pakppsrpvd
      301 nyntfvlpel psvpdtlpta sagastsase didfddlsrr feelkkkt
//
LOCUS       NP_001035826             266 aa            linear   PRI 27-APR-2025
DEFINITION  meiotic recombination protein REC114 isoform 1 [Homo sapiens].
ACCESSION   NP_001035826
VERSION     NP_001035826.1
DBSOURCE    REFSEQ: accession NM_001042367.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Xu,S., Zhao,J., Gao,F., Zhang,Y., Luo,J., Zhang,C., Tian,R.,
            Zhi,E., Zhang,J., Bai,F., Sun,H., Zhao,F., Huang,Y., Li,P.,
            Jiang,L., Li,Z., Yao,C. and Zhou,Z.
  TITLE     A bi-allelic REC114 loss-of-function variant causes meiotic arrest
            and nonobstructive azoospermia
  JOURNAL   Clin Genet 105 (4), 440-445 (2024)
   PUBMED   38148155
  REMARK    GeneRIF: A bi-allelic REC114 loss-of-function variant causes
            meiotic arrest and nonobstructive azoospermia.
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Wang,W., Dong,J., Chen,B., Du,J., Kuang,Y., Sun,X., Fu,J., Li,B.,
            Mu,J., Zhang,Z., Zhou,Z., Lin,Z., Wu,L., Yan,Z., Mao,X., Li,Q.,
            He,L., Wang,L. and Sang,Q.
  TITLE     Homozygous mutations in REC114 cause female infertility
            characterised by multiple pronuclei formation and early embryonic
            arrest
  JOURNAL   J Med Genet 57 (3), 187-194 (2020)
   PUBMED   31704776
  REMARK    GeneRIF: Homozygous mutations in REC114 cause female infertility
            characterised by multiple pronuclei formation and early embryonic
            arrest.
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Ueta,M., Sawai,H., Shingaki,R., Kawai,Y., Sotozono,C., Kojima,K.,
            Yoon,K.C., Kim,M.K., Seo,K.Y., Joo,C.K., Nagasaki,M., Kinoshita,S.
            and Tokunaga,K.
  TITLE     Genome-wide association study using the ethnicity-specific Japonica
            array: identification of new susceptibility loci for cold
            medicine-related Stevens-Johnson syndrome with severe ocular
            complications
  JOURNAL   J Hum Genet 62 (4), 485-489 (2017)
   PUBMED   28100913
  REMARK    GeneRIF: In Japanese individuals, combined genotyping for the
            associated variants thus far identified; that is, HLA-A*02:06, TLR3
            rs3775296 T/T and Rec114 rs16957893 CG, may help to predict the
            risk for cold medicine-related Stevens-Johnson syndrome /TEN with
            severe ocular complications
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Kumar,R., Bourbon,H.M. and de Massy,B.
  TITLE     Functional conservation of Mei4 for meiotic DNA double-strand break
            formation from yeasts to mice
  JOURNAL   Genes Dev 24 (12), 1266-1280 (2010)
   PUBMED   20551173
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB465854.1, BC055412.1 and
            BX113903.1.
            
            Summary: The protein encoded by this gene is orthologous to the
            mouse meiotic recombination protein REC114, which is involved in
            DNA double-strand break formation during meiosis. The encoded
            protein is conserved in most eukaryotes and was first discovered
            and characterized in yeast. [provided by RefSeq, Feb 2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.103808.1,
                                           SRR5189667.12067.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331090.11/ ENSP00000328423.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..266
                     /product="meiotic recombination protein REC114 isoform 1"
                     /note="meiotic recombination protein REC114-like"
                     /calculated_mol_wt=29024
     Region          21..261
                     /region_name="REC114-like"
                     /note="Meiotic recombination protein REC114-like;
                     pfam15165"
                     /db_xref="CDD:464541"
     Region          157..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z4M0.2)"
     Region          210..261
                     /region_name="Interaction with MEI4.
                     /evidence=ECO:0000269|PubMed:38148155"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z4M0.2)"
     CDS             1..266
                     /gene="REC114"
                     /gene_synonym="C15orf60; CT147; OOMD10; OZEMA10"
                     /coded_by="NM_001042367.2:23..823"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45296.1"
                     /db_xref="GeneID:283677"
                     /db_xref="HGNC:HGNC:25065"
                     /db_xref="MIM:618421"
ORIGIN      
        1 maeagkvpls lgltggeaae wplqryarci psntrdppgp cleagtapcp twkvfdsnee
       61 sgylvltivi sghffifqgq tllegfslig skdwlkivrr vdcllfgtti kdksrlfrvq
      121 fsgeskeqal ehccscvqkl aqyitvqvpd gniqelqlip gppratesqg kdsaksvprq
      181 pgshqhseqq qvcvtagtga pdgrtsltql aqtllaseel phvyeqsawg aeelgpflrl
      241 clmdqnfpaf veevekelkk laglrn
//
LOCUS       NP_004223                535 aa            linear   PRI 27-APR-2025
DEFINITION  suppressor of cytokine signaling 6 [Homo sapiens].
ACCESSION   NP_004223
VERSION     NP_004223.2
DBSOURCE    REFSEQ: accession NM_004232.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Li,Z.B., Li,Z.Z., Li,L., Chu,H.T. and Jia,M.
  TITLE     Publisher Correction: MiR-21 and miR-183 can simultaneously target
            SOCS6 and modulate growth and invasion of hepatocellular carcinoma
            (HCC) cells
  JOURNAL   Eur Rev Med Pharmacol Sci 28 (9), 3290 (2024)
   PUBMED   38766781
  REMARK    GeneRIF: Publisher Correction: MiR-21 and miR-183 can
            simultaneously target SOCS6 and modulate growth and invasion of
            hepatocellular carcinoma (HCC) cells.
            Correction to:[Eur Rev Med Pharmacol Sci. 2015 Sep;19(17):3208-17.
            PMID: 26400524]
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Sun,L., Ke,M., Yin,M., Zeng,Y., Ji,Y., Hu,Y., Fu,S. and Zhang,C.
  TITLE     Extracellular vesicle-encapsulated microRNA-296-3p from
            cancer-associated fibroblasts promotes ovarian cancer development
            through regulation of the PTEN/AKT and SOCS6/STAT3 pathways
  JOURNAL   Cancer Sci 115 (1), 155-169 (2024)
   PUBMED   37972389
  REMARK    GeneRIF: Extracellular vesicle-encapsulated microRNA-296-3p from
            cancer-associated fibroblasts promotes ovarian cancer development
            through regulation of the PTEN/AKT and SOCS6/STAT3 pathways.
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Li,S., Lu,X., Zheng,D., Chen,W., Li,Y. and Li,F.
  TITLE     Methyltransferase-like 3 facilitates lung cancer progression by
            accelerating m6A methylation-mediated primary miR-663 processing
            and impeding SOCS6 expression
  JOURNAL   J Cancer Res Clin Oncol 148 (12), 3485-3499 (2022)
   PUBMED   35907010
  REMARK    GeneRIF: Methyltransferase-like 3 facilitates lung cancer
            progression by accelerating m6A methylation-mediated primary
            miR-663 processing and impeding SOCS6 expression.
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Xue,X., Liu,M., Wang,Y., Yang,Y., Li,Z., Shi,R. and Miao,Y.
  TITLE     MicroRNA-494-3p Exacerbates Renal Epithelial Cell Dysfunction by
            Targeting SOCS6 under High Glucose Treatment
  JOURNAL   Kidney Blood Press Res 47 (4), 247-255 (2022)
   PUBMED   35038704
  REMARK    GeneRIF: MicroRNA-494-3p Exacerbates Renal Epithelial Cell
            Dysfunction by Targeting SOCS6 under High Glucose Treatment.
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Ouyang,J., An,T., Wang,Y., Lu,X., Zhang,Y., Wang,X., Zhang,X. and
            Zhang,C.
  TITLE     Down-regulation of SOCS6: an unfavorable prognostic factor for
            gastrointestinal stromal tumor proven by survival analysis
  JOURNAL   Diagn Pathol 16 (1), 113 (2021)
   PUBMED   34895274
  REMARK    GeneRIF: Down-regulation of SOCS6: an unfavorable prognostic factor
            for gastrointestinal stromal tumor proven by survival analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Bayle,J., Letard,S., Frank,R., Dubreuil,P. and De Sepulveda,P.
  TITLE     Suppressor of cytokine signaling 6 associates with KIT and
            regulates KIT receptor signaling
  JOURNAL   J Biol Chem 279 (13), 12249-12259 (2004)
   PUBMED   14707129
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Krebs,D.L., Uren,R.T., Metcalf,D., Rakar,S., Zhang,J.G., Starr,R.,
            De Souza,D.P., Hanzinikolas,K., Eyles,J., Connolly,L.M.,
            Simpson,R.J., Nicola,N.A., Nicholson,S.E., Baca,M., Hilton,D.J. and
            Alexander,W.S.
  TITLE     SOCS-6 binds to insulin receptor substrate 4, and mice lacking the
            SOCS-6 gene exhibit mild growth retardation
  JOURNAL   Mol Cell Biol 22 (13), 4567-4578 (2002)
   PUBMED   12052866
REFERENCE   8  (residues 1 to 535)
  AUTHORS   Kile,B.T., Schulman,B.A., Alexander,W.S., Nicola,N.A., Martin,H.M.
            and Hilton,D.J.
  TITLE     The SOCS box: a tale of destruction and degradation
  JOURNAL   Trends Biochem Sci 27 (5), 235-241 (2002)
   PUBMED   12076535
  REMARK    Review article
REFERENCE   9  (residues 1 to 535)
  AUTHORS   Mooney,R.A., Senn,J., Cameron,S., Inamdar,N., Boivin,L.M., Shang,Y.
            and Furlanetto,R.W.
  TITLE     Suppressors of cytokine signaling-1 and -6 associate with and
            inhibit the insulin receptor. A potential mechanism for
            cytokine-mediated insulin resistance
  JOURNAL   J Biol Chem 276 (28), 25889-25893 (2001)
   PUBMED   11342531
REFERENCE   10 (residues 1 to 535)
  AUTHORS   Masuhara,M., Sakamoto,H., Matsumoto,A., Suzuki,R., Yasukawa,H.,
            Mitsui,K., Wakioka,T., Tanimura,S., Sasaki,A., Misawa,H.,
            Yokouchi,M., Ohtsubo,M. and Yoshimura,A.
  TITLE     Cloning and characterization of novel CIS family genes
  JOURNAL   Biochem Biophys Res Commun 239 (2), 439-446 (1997)
   PUBMED   9344848
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC020082.1 and AC023395.8.
            
            On Jun 18, 2002 this sequence version replaced NP_004223.1.
            
            Summary: The protein encoded by this gene contains a SH2 domain and
            a CIS homolog domain. The protein thus belongs to the
            cytokine-induced STAT inhibitor (CIS), also known as suppressor of
            cytokine signaling (SOCS) or STAT-induced STAT inhibitor (SSI),
            protein family. CIS family members are known to be
            cytokine-inducible negative regulators of cytokine signaling. The
            expression of this gene can be induced by GM-CSF and EPO in
            hematopoietic cells. A high expression level of this gene was found
            in factor-independent chronic myelogenous leukemia (CML) and
            erythroleukemia (HEL) cell lines. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.214235.1,
                                           SRR1660807.205991.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397942.4/ ENSP00000381034.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q22.2"
     Protein         1..535
                     /product="suppressor of cytokine signaling 6"
                     /note="STAT induced STAT inhibitor-4; suppressor of
                     cytokine signaling 4; cytokine-inducible SH2 protein 4"
                     /calculated_mol_wt=59397
     Region          80..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14544.2)"
     Region          373..472
                     /region_name="SH2_SOCS6"
                     /note="Src homology 2 (SH2) domain found in suppressor of
                     cytokine signaling (SOCS) proteins; cd10387"
                     /db_xref="CDD:198250"
     Site            order(391,409,411,419,432)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198250"
     Site            order(442,444,461)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198250"
     Region          495..535
                     /region_name="SOCS_SOCS6"
                     /note="SOCS (suppressors of cytokine signaling) box of
                     SOCS6-like proteins. Together with CIS1, the CIS/SOCS
                     family of proteins is characterized by the presence of a
                     C-terminal SOCS box and a central SH2 domain. The general
                     function of the SOCS box is the...; cd03740"
                     /db_xref="CDD:239709"
     Site            order(496..501,507,514,520,525)
                     /site_type="other"
                     /note="putative elongin B/C interaction [polypeptide
                     binding]"
                     /db_xref="CDD:239709"
     CDS             1..535
                     /gene="SOCS6"
                     /gene_synonym="CIS-4; CIS4; HSPC060; SOCS-4; SOCS-6;
                     SOCS4; SSI4; STAI4; STATI4"
                     /coded_by="NM_004232.4:173..1780"
                     /db_xref="CCDS:CCDS11998.1"
                     /db_xref="GeneID:9306"
                     /db_xref="HGNC:HGNC:16833"
                     /db_xref="MIM:605118"
ORIGIN      
        1 mkkislktlr ksfnlnkske etdfmvvqqp slasdfgkdd slfgscygkd mascdinged
       61 ekggknrsks eslmgtlkrr lsakqkskgk agtpsgssad edtfssssap ivfkdvraqr
      121 pirstslrsh hyspapwplr ptnseetcik mevrvkalvh ssspspalng vrkdfhdlqs
      181 ettcqeqans lkssashngd lhlhldehvp vviglmpqdy iqytvpldeg myplegsrsy
      241 cldssspmev savppqvggr afpedesqvd qdlvvapeif vdqsvnglli gttgvmlqsp
      301 raghddvppl spllppmqnn qiqrnfsglt gteahvaesm rchlnfdpns apgvarvyds
      361 vqssgpmvvt slteelkkla kqgwywgpit rweaegklan vpdgsflvrd ssddryllsl
      421 sfrshgktlh triehsngrf sfyeqpdveg htsivdlieh sirdsengaf cysrsrlpgs
      481 atypvrltnp vsrfmqvrsl qylcrfvirq ytridliqkl plpnkmkdyl qekhy
//
LOCUS       NP_001075042             587 aa            linear   PRI 27-APR-2025
DEFINITION  GRB2-associated-binding protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001075042
VERSION     NP_001075042.1
DBSOURCE    REFSEQ: accession NM_001081573.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Li,C., Ye,Z., Wang,Y., Wang,G., Zhang,Q. and Zhang,C.
  TITLE     High expression of GRB2 associated binding protein 3 mRNA predicts
            positive prognosis in melanoma
  JOURNAL   Melanoma Res 33 (1), 27-37 (2023)
   PUBMED   36545920
  REMARK    GeneRIF: High expression of GRB2 associated binding protein 3 mRNA
            predicts positive prognosis in melanoma.
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Wang,N., Zhou,X., Wang,X. and Zhu,X.
  TITLE     Identification of Grb2-associated binding protein 3 expression to
            predict clinical outcomes and immunotherapeutic responses in lung
            adenocarcinoma
  JOURNAL   J Biochem Mol Toxicol 36 (10), e23166 (2022)
   PUBMED   35822560
  REMARK    GeneRIF: Identification of Grb2-associated binding protein 3
            expression to predict clinical outcomes and immunotherapeutic
            responses in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Xiang,S., Wang,N., Hui,P. and Ma,J.
  TITLE     Gab3 is required for human colorectal cancer cell proliferation
  JOURNAL   Biochem Biophys Res Commun 484 (4), 719-725 (2017)
   PUBMED   28115166
  REMARK    GeneRIF: Together, our results suggest that Gab3 expression in CRC
            cells is important for Akt-Erk activation and cell proliferation.
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Jia,P., Li,F., Gu,W., Zhang,W. and Cai,Y.
  TITLE     Gab3 overexpression in human glioma mediates Akt activation and
            tumor cell proliferation
  JOURNAL   PLoS One 12 (3), e0173473 (2017)
   PUBMED   28291820
  REMARK    GeneRIF: we conclude that Gab3 overexpression in human glioma
            mediates Akt activation and cancer cell proliferation
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Nakaoka,Y. and Komuro,I.
  TITLE     Gab docking proteins in cardiovascular disease, cancer, and
            inflammation
  JOURNAL   Int J Inflam 2013, 141068 (2013)
   PUBMED   23431498
REFERENCE   6  (residues 1 to 587)
  AUTHORS   Sarmay,G., Angyal,A., Kertesz,A., Maus,M. and Medgyesi,D.
  TITLE     The multiple function of Grb2 associated binder (Gab)
            adaptor/scaffolding protein in immune cell signaling
  JOURNAL   Immunol Lett 104 (1-2), 76-82 (2006)
   PUBMED   16386802
  REMARK    Review article
REFERENCE   7  (residues 1 to 587)
  AUTHORS   Seiffert,M., Custodio,J.M., Wolf,I., Harkey,M., Liu,Y.,
            Blattman,J.N., Greenberg,P.D. and Rohrschneider,L.R.
  TITLE     Gab3-deficient mice exhibit normal development and hematopoiesis
            and are immunocompetent
  JOURNAL   Mol Cell Biol 23 (7), 2415-2424 (2003)
   PUBMED   12640125
  REMARK    GeneRIF: Hematopoiesis in mice lacking Gab3 is not impaired,
            macrophages develop in normal numbers and exhibit normal function,
            and there is no major immune deficiency in T- and B-lymphocyte
            responses to protein antigens or during viral infection.
REFERENCE   8  (residues 1 to 587)
  AUTHORS   Bourgin,C., Bourette,R.P., Arnaud,S., Liu,Y., Rohrschneider,L.R.
            and Mouchiroud,G.
  TITLE     Induced expression and association of the Mona/Gads adapter and
            Gab3 scaffolding protein during monocyte/macrophage differentiation
  JOURNAL   Mol Cell Biol 22 (11), 3744-3756 (2002)
   PUBMED   11997510
  REMARK    GeneRIF: The carboxy-terminal SH3 domain of the adapter protein
            Mona interacts with the atypical proline-rich domain of Gab3 to
            mediate late signaling of the macrophage colony-stimulating factor
            receptor.
REFERENCE   9  (residues 1 to 587)
  AUTHORS   Liu,Y. and Rohrschneider,L.R.
  TITLE     The gift of Gab
  JOURNAL   FEBS Lett 515 (1-3), 1-7 (2002)
   PUBMED   11943184
  REMARK    Review article
REFERENCE   10 (residues 1 to 587)
  AUTHORS   Wolf,I., Jenkins,B.J., Liu,Y., Seiffert,M., Custodio,J.M., Young,P.
            and Rohrschneider,L.R.
  TITLE     Gab3, a new DOS/Gab family member, facilitates macrophage
            differentiation
  JOURNAL   Mol Cell Biol 22 (1), 231-244 (2002)
   PUBMED   11739737
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK307927.1, AK126283.1,
            AY057989.1, AC244107.3 and AA808085.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the GRB2-associated binding
            protein gene family. These proteins are scaffolding/docking
            proteins that are involved in several growth factor and cytokine
            signaling pathways, and they contain a pleckstrin homology domain,
            and bind SHP2 tyrosine phosphatase and GRB2 adapter protein. The
            protein encoded by this gene facilitates macrophage
            differentiation. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK307927.1, DRR138524.1295072.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000424127.3/ ENSP00000399588.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..587
                     /product="GRB2-associated-binding protein 3 isoform 1"
                     /note="DOS/Gab family member 3; Gab3 scaffolding protein;
                     GRB2-associated binder 3; growth factor receptor bound
                     protein 2-associated protein 3"
                     /calculated_mol_wt=65529
     Region          1..125
                     /region_name="PH_Gab3"
                     /note="Grb2-associated binding protein 3 pleckstrin
                     homology (PH) domain; cd13385"
                     /db_xref="CDD:270184"
     Region          150..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWW8.1)"
     Region          282..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWW8.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WWW8.1)"
     Region          402..454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWW8.1)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WWW8.1)"
     CDS             1..587
                     /gene="GAB3"
                     /coded_by="NM_001081573.3:53..1816"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS48198.1"
                     /db_xref="GeneID:139716"
                     /db_xref="HGNC:HGNC:17515"
                     /db_xref="MIM:300482"
ORIGIN      
        1 msagdavctg wlvkspperk lqryawrkrw fvlrrgrmsg npdvleyyrn khsskpirvi
       61 dlsecavwkh vgpsfvrkef qnnfvfivkt tsrtfylvak teqemqvwvh sisqvcnlgh
      121 ledgaadsme slsytpsslq pssassllta haassslprd dpntnavate etrsesellf
      181 lpdylvlsnc etgrlhhtsl ptrcdswsns drsleqasfd dvfvdclqpl psshlvhpsc
      241 hgsgaqevps srpqaaliws reingpprdh lsssplless lsstiqvdkn qgslpcgake
      301 ldimsntppp rppkpshlse rrqeewsths gskkpectlv prrislsgld nmrtwkadve
      361 gqslrhrdkr lslnlpcrfs pmyptasasi edsyvpmspq agasglgphc spddyipmns
      421 gsissplpel panlepppvn rdlkpqrksr pppldlrnls iirehasltr trtvpcsrts
      481 flsperngin sarffanpvs redeesyiem eehrtassls sgaltwtkkf sldylaldfn
      541 saspapmqqk lllseeqrvd yvqvdeqktq alqstkqewt derqskv
//
LOCUS       NP_001347524             373 aa            linear   ROD 27-APR-2025
DEFINITION  palmitoyltransferase ZDHHC6 isoform 2 [Mus musculus].
ACCESSION   NP_001347524 XP_006527332
VERSION     NP_001347524.1
DBSOURCE    REFSEQ: accession NM_001360595.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Yu,T., Hou,D., Zhao,J., Lu,X., Greentree,W.K., Zhao,Q., Yang,M.,
            Conde,D.G., Linder,M.E. and Lin,H.
  TITLE     NLRP3 Cys126 palmitoylation by ZDHHC7 promotes inflammasome
            activation
  JOURNAL   Cell Rep 43 (4), 114070 (2024)
   PUBMED   38583156
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Komaniecki,G., Camarena,M.D.C., Gelsleichter,E., Mendoza,R.,
            Subler,M., Windle,J.J., Dozmorov,M.G., Lai,Z., Sarkar,D. and Lin,H.
  TITLE     Astrocyte Elevated Gene-1 Cys75 S-Palmitoylation by ZDHHC6
            Regulates Its Biological Activity
  JOURNAL   Biochemistry 62 (2), 543-553 (2023)
   PUBMED   36548985
  REMARK    GeneRIF: Astrocyte Elevated Gene-1 Cys75 S-Palmitoylation by ZDHHC6
            Regulates Its Biological Activity.
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Fukata,Y., Murakami,T., Yokoi,N. and Fukata,M.
  TITLE     Local Palmitoylation Cycles and Specialized Membrane Domain
            Organization
  JOURNAL   Curr Top Membr 77, 97-141 (2016)
   PUBMED   26781831
  REMARK    Review article
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Fredericks,G.J., Hoffmann,F.W., Rose,A.H., Osterheld,H.J.,
            Hess,F.M., Mercier,F. and Hoffmann,P.R.
  TITLE     Stable expression and function of the inositol 1,4,5-triphosphate
            receptor requires palmitoylation by a DHHC6/selenoprotein K complex
  JOURNAL   Proc Natl Acad Sci U S A 111 (46), 16478-16483 (2014)
   PUBMED   25368151
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Blaskovic,S., Adibekian,A., Blanc,M. and van der Goot,G.F.
  TITLE     Mechanistic effects of protein palmitoylation and the cellular
            consequences thereof
  JOURNAL   Chem Phys Lipids 180, 44-52 (2014)
   PUBMED   24534427
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Chamberlain,L.H., Lemonidis,K., Sanchez-Perez,M., Werno,M.W.,
            Gorleku,O.A. and Greaves,J.
  TITLE     Palmitoylation and the trafficking of peripheral membrane proteins
  JOURNAL   Biochem Soc Trans 41 (1), 62-66 (2013)
   PUBMED   23356259
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 373)
  AUTHORS   Conibear,E. and Davis,N.G.
  TITLE     Palmitoylation and depalmitoylation dynamics at a glance
  JOURNAL   J Cell Sci 123 (Pt 23), 4007-4010 (2010)
   PUBMED   21084560
REFERENCE   9  (residues 1 to 373)
  AUTHORS   Lu,J., Qian,J., Izvolsky,K.I. and Cardoso,W.V.
  TITLE     Global analysis of genes differentially expressed in branching and
            non-branching regions of the mouse embryonic lung
  JOURNAL   Dev Biol 273 (2), 418-435 (2004)
   PUBMED   15328023
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC133100.5.
            
            On Feb 8, 2018 this sequence version replaced XP_006527332.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.9312.1,
                                           SRR7974084.24631.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 51.33 cM"
     Protein         1..373
                     /product="palmitoyltransferase ZDHHC6 isoform 2"
                     /EC_number="2.3.1.225"
                     /note="H4 homolog; zinc finger DHHC domain-containing
                     protein 6; palmitoyltransferase ZDHHC6;
                     stearoyltransferase ZDHHC6"
                     /calculated_mol_wt=42859
     Site            25..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CPV7.1)"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CPV7.1)"
     Region          95..241
                     /region_name="DHHC"
                     /note="DHHC palmitoyltransferase; pfam01529"
                     /db_xref="CDD:396215"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CPV7.1)"
     Site            195..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CPV7.1)"
     CDS             1..373
                     /gene="Zdhhc6"
                     /gene_synonym="2400007G07Rik; 5930409M18Rik; DHHC-6"
                     /coded_by="NM_001360595.1:447..1568"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:66980"
                     /db_xref="MGI:MGI:1914230"
ORIGIN      
        1 mgifcsvikf enlqdlrrlc hwgpiialgv iaicstmami dsvlwywplh ttggsvnfim
       61 linwtvmily nyfnamfagp gfvprgwkpe ksqdsmylqy ckvcqaykap rshhcrkcnr
      121 cvmkmdhhcp winnccghqn hasftlflll aplgcthaaf ifvmtmytql ynrlsfgwnt
      181 vkidmsaarr dpppivpfgl aafaatlfal glalgttiav gmlffiqiki ilrnktsies
      241 wieekakdri qyyqldevfi fpydmgskwk nfkqvftwsg vpegdglewp iregcdqysl
      301 tieqlkqkad krvrsvrykv iedyngaccp lnrgvrtfft spcteeprir lqkgefilat
      361 rglryfkskr vvs
//
LOCUS       NP_001354462             542 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 26 [Homo sapiens].
ACCESSION   NP_001354462 XP_005270258
VERSION     NP_001354462.1
DBSOURCE    REFSEQ: accession NM_001367533.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_005270258.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.724858.1,
                                           SRR3476690.738679.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..542
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 26"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=60612
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          410..537
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..542
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367533.1:95..1723"
                     /note="isoform 26 is encoded by transcript variant 26"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk pqsnnknsle pqttvvhnat dgikgstesc
      361 ntttededlk aaplrtgngs svpegrssrd rtapsagmqp qpslcssamr kqeiikiteq
      421 lieainngdf eaytkicdpg ltsfepealg nlvegmdfhk fyfenllskn skpihttiln
      481 phvhvigeda aciayirltq yidgqgrprt sqseetrvwh rrdgkwlnvh yhcsgapaap
      541 lq
//
LOCUS       NP_001350262             526 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 655 isoform f [Homo sapiens].
ACCESSION   NP_001350262 XP_016868093
VERSION     NP_001350262.1
DBSOURCE    REFSEQ: accession NM_001363333.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Fan,S., Liu,Y., Lin,Z., Zhang,Y., Zhang,N., Zhao,Y., Zhou,J.,
            Mao,A., Wang,L., Feng,Y., He,X., Wang,L. and Pan,Q.
  TITLE     ZNF655 promotes the progression of hepatocellular carcinoma through
            PSMB8
  JOURNAL   Cell Biol Int 47 (9), 1535-1546 (2023)
   PUBMED   37272200
  REMARK    GeneRIF: ZNF655 promotes the progression of hepatocellular
            carcinoma through PSMB8.
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Teng,Z., Yao,J., Zhu,L., Zhao,L. and Chen,G.
  TITLE     ZNF655 is involved in development and progression of non-small-cell
            lung cancer
  JOURNAL   Life Sci 280, 119727 (2021)
   PUBMED   34144060
  REMARK    GeneRIF: ZNF655 is involved in development and progression of
            non-small-cell lung cancer.
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Thompson,E.E., Kuttab-Boulos,H., Yang,L., Roe,B.A. and Di Rienzo,A.
  TITLE     Sequence diversity and haplotype structure at the human CYP3A
            cluster
  JOURNAL   Pharmacogenomics J 6 (2), 105-114 (2006)
   PUBMED   16314882
REFERENCE   7  (residues 1 to 526)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Houlard,M., Romero-Portillo,F., Germani,A., Depaux,A.,
            Regnier-Ricard,F., Gisselbrecht,S. and Varin-Blank,N.
  TITLE     Characterization of VIK-1: a new Vav-interacting Kruppel-like
            protein
  JOURNAL   Oncogene 24 (1), 28-38 (2005)
   PUBMED   15558030
REFERENCE   9  (residues 1 to 526)
  AUTHORS   Rual,J.F., Hirozane-Kishikawa,T., Hao,T., Bertin,N., Li,S.,
            Dricot,A., Li,N., Rosenberg,J., Lamesch,P., Vidalain,P.O.,
            Clingingsmith,T.R., Hartley,J.L., Esposito,D., Cheo,D., Moore,T.,
            Simmons,B., Sequerra,R., Bosak,S., Doucette-Stamm,L., Le Peuch,C.,
            Vandenhaute,J., Cusick,M.E., Albala,J.S., Hill,D.E. and Vidal,M.
  TITLE     Human ORFeome version 1.1: a platform for reverse proteomics
  JOURNAL   Genome Res 14 (10B), 2128-2135 (2004)
   PUBMED   15489335
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Laity,J.H., Lee,B.M. and Wright,P.E.
  TITLE     Zinc finger proteins: new insights into structural and functional
            diversity
  JOURNAL   Curr Opin Struct Biol 11 (1), 39-46 (2001)
   PUBMED   11179890
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA314253.1, BI548533.1,
            AK128057.1, CR749270.1 and BC024770.1.
            
            On May 17, 2018 this sequence version replaced XP_016868093.1.
            
            Summary: This gene encodes a zinc finger protein. The zinc finger
            proteins are involved in DNA binding and protein-protein
            interactions. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.236452.1,
                                           SRR1660807.71293.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..526
                     /product="zinc finger protein 655 isoform f"
                     /note="vav-1 interacting Kruppel-like protein"
                     /calculated_mol_wt=61239
     Region          220..>325
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          222..241
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          249..269
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(254,256,258,260..261,264..265,268,282,284,288..289,
                     292..293,296,345,347,349,351..352,355..356,359)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          277..297
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          305..360
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          367..387
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(372,374,376,378..379,382..383,386,422,424,428..429,
                     432..433,436,450,452,454,456..457,460..461,464)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          417..437
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          429..454
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          445..465
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..526
                     /gene="ZNF655"
                     /gene_synonym="VIK; VIK-1"
                     /coded_by="NM_001363333.1:202..1782"
                     /note="isoform f is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS47655.1"
                     /db_xref="GeneID:79027"
                     /db_xref="HGNC:HGNC:30899"
                     /db_xref="MIM:617891"
ORIGIN      
        1 meeipaqeaa gsprvqfqsl etqseclspe pqfvqdtdme qgltggfpis kpdgisqleq
       61 dlqvfdletk trevlrddcs dgetreenkl lipkqkisee vhsykvrvgr lkhditqvpe
      121 trevyksedr lerlqeilrk flylerefrq itisketfts eknnechepe ksfsldstid
      181 adqrvlriqn tddndkydms fnqnsasgkh ehlnltedfq sseckeslmd lshlnkwesi
      241 pnteksykcd vcgkifhqss altrhqriht rekpykckec eksfsqsssl srhkrihtre
      301 kpykceasdk sceasdkscs pssgiiqhkk ihtraksykc sscervfsrs vhltqhqkih
      361 kempckctvc gsdfchtsyl lehqrvhhee kayeydeygl ayikqqgihf rekpytcsec
      421 gkdfrlnshl iqhqrihtge kahecnecgk afsqtscliq hhkmhrkeks yecneyegsf
      481 shssdlilqq evltrqkafd cdvweknssq rahlvqhqsi htkens
//
LOCUS       NP_001355556             484 aa            linear   ROD 27-APR-2025
DEFINITION  EF-hand calcium-binding domain-containing protein 14 isoform 2 [Mus
            musculus].
ACCESSION   NP_001355556
VERSION     NP_001355556.1
DBSOURCE    REFSEQ: accession NM_001368627.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK028618.1 and AL626806.14.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK030011.1, AK028618.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 53.06 cM"
     Protein         1..484
                     /product="EF-hand calcium-binding domain-containing
                     protein 14 isoform 2"
                     /note="EF-hand calcium-binding domain-containing protein
                     14"
                     /calculated_mol_wt=53563
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGQ6.1)"
     Region          227..255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGQ6.1)"
     Region          313..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BGQ6.1)"
     CDS             1..484
                     /gene="Efcab14"
                     /gene_synonym="4732418C07Rik"
                     /coded_by="NM_001368627.1:890..2344"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS89810.1"
                     /db_xref="GeneID:230648"
                     /db_xref="MGI:MGI:2442397"
ORIGIN      
        1 mkkrkelnal iglagdhrrk ktkqgsgshr llrteppdsd sesstdeeef gaignrsrfv
       61 kgdyarccki ccplcafvil aacvvasvgl vwmqmalked ldvlkekfrt mesnqkssfq
      121 eipklneell skqkqlekie sgelglsrvw initemnkqi sllssavnhl kasvksaadl
      181 lslpstvegl qksvasignt lnsvhlavev iqktvdehrt tlgllqgsme nngsnqilps
      241 psppseldnk shsesakqdi lylhnsleev nstvveyqrq ndlklkgmse tlsnltqrls
      301 lieshvvals kaeqrtnvss stmenraatl kreslvtnrs dtvqaqsmkk ednsnsqvse
      361 lreklqlisa ltnkpesnrp pettdeeqvq nftsdpsalp efsqllrnqi etqvkplslp
      421 gissikdlqd lfhktgqdvd gmltyqelwn slgsamprpe slrafdsngd grysflelrl
      481 algi
//
LOCUS       NP_060708                422 aa            linear   PRI 27-APR-2025
DEFINITION  acylglycerol kinase, mitochondrial isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_060708
VERSION     NP_060708.1
DBSOURCE    REFSEQ: accession NM_018238.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Wu,C.W., Caha,M., Smoot,L., Harris,D.J., Roberts,A.E., Sacharow,S.
            and Bodamer,O.
  TITLE     Sengers syndrome and AGK-related disorders - Minireview of
            phenotypic variability and clinical outcomes in molecularly
            confirmed cases
  JOURNAL   Mol Genet Metab 139 (3), 107626 (2023)
   PUBMED   37354892
  REMARK    GeneRIF: Sengers syndrome and AGK-related disorders - Minireview of
            phenotypic variability and clinical outcomes in molecularly
            confirmed cases.
            Review article
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Meng,K., Lu,S., Li,Y.Y., Hu,L.L., Zhang,J., Cao,Y., Wang,Y.,
            Zhang,C.Z. and He,Q.Y.
  TITLE     LINC00493-encoded microprotein SMIM26 exerts anti-metastatic
            activity in renal cell carcinoma
  JOURNAL   EMBO Rep 24 (6), e56282 (2023)
   PUBMED   37009826
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Sun,F., Wei,Y., Liu,Z., Jie,Q., Yang,X., Long,P., Wang,J.,
            Xiong,Y., Li,Q., Quan,S. and Ma,Y.
  TITLE     Acylglycerol kinase promotes ovarian cancer progression and
            regulates mitochondria function by interacting with ribosomal
            protein L39
  JOURNAL   J Exp Clin Cancer Res 41 (1), 238 (2022)
   PUBMED   35934718
  REMARK    GeneRIF: Acylglycerol kinase promotes ovarian cancer progression
            and regulates mitochondria function by interacting with ribosomal
            protein L39.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Long,Y., Li,C. and Zhu,B.
  TITLE     Circ_0008068 facilitates the oral squamous cell carcinoma
            development by microRNA-153-3p/acylgycerol kinase (AGK) axis
  JOURNAL   Bioengineered 13 (5), 13055-13069 (2022)
   PUBMED   35635053
  REMARK    GeneRIF: Circ_0008068 facilitates the oral squamous cell carcinoma
            development by microRNA-153-3p/acylgycerol kinase (AGK) axis.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Nouh,M.A., Wu,X.X., Okazoe,H., Tsunemori,H., Haba,R.,
            Abou-Zeid,A.M., Saleem,M.D., Inui,M., Sugimoto,M., Aoki,J. and
            Kakehi,Y.
  TITLE     Expression of autotaxin and acylglycerol kinase in prostate cancer:
            association with cancer development and progression
  JOURNAL   Cancer Sci 100 (9), 1631-1638 (2009)
   PUBMED   19549252
  REMARK    GeneRIF: High Expression of acylglycerol kinase is associated with
            development and progression of prostate cancer.
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Epand,R.M., Shulga,Y.V., Timmons,H.C., Perri,A.L., Belani,J.D.,
            Perinpanathan,K., Johnson-McIntire,L.B., Bajjalieh,S., Dicu,A.O.,
            Elias,C., Rychnovsky,S.D. and Topham,M.K.
  TITLE     Substrate chirality and specificity of diacylglycerol kinases and
            the multisubstrate lipid kinase
  JOURNAL   Biochemistry 46 (49), 14225-14231 (2007)
   PUBMED   18004883
  REMARK    GeneRIF: The chiral specificity of diacylglycerol kinase alpha,
            zeta & epsilon mimics the substrate specificity, with MuLK being
            the least selective and the epsilon isoform of diacylglycerol
            kinase exhibiting the greatest selectivity.
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Spiegel,S. and Milstien,S.
  TITLE     Functions of the multifaceted family of sphingosine kinases and
            some close relatives
  JOURNAL   J Biol Chem 282 (4), 2125-2129 (2007)
   PUBMED   17135245
  REMARK    Review article
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Van Overloop,H., Gijsbers,S. and Van Veldhoven,P.P.
  TITLE     Further characterization of mammalian ceramide kinase: substrate
            delivery and (stereo)specificity, tissue distribution, and
            subcellular localization studies
  JOURNAL   J Lipid Res 47 (2), 268-283 (2006)
   PUBMED   16269826
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Bektas,M., Payne,S.G., Liu,H., Goparaju,S., Milstien,S. and
            Spiegel,S.
  TITLE     A novel acylglycerol kinase that produces lysophosphatidic acid
            modulates cross talk with EGFR in prostate cancer cells
  JOURNAL   J Cell Biol 169 (5), 801-811 (2005)
   PUBMED   15939762
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Waggoner,D.W., Johnson,L.B., Mann,P.C., Morris,V., Guastella,J. and
            Bajjalieh,S.M.
  TITLE     MuLK, a eukaryotic multi-substrate lipid kinase
  JOURNAL   J Biol Chem 279 (37), 38228-38235 (2004)
   PUBMED   15252046
  REMARK    GeneRIF: identification and characterization of a novel lipid
            kinase that phosphorylates multiple substrates, MuLK
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK001704.1, BC022777.1,
            AJ278150.1, AW961934.1 and BU740733.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a mitochondrial
            membrane protein involved in lipid and glycerolipid metabolism. The
            encoded protein is a lipid kinase that catalyzes the formation of
            phosphatidic and lysophosphatidic acids. Defects in this gene have
            been associated with mitochondrial DNA depletion syndrome 10.
            [provided by RefSeq, Feb 2012].
            
            Transcript Variant: The variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.213505.1,
                                           SRR1660807.21362.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000649286.2/
                                                  ENSP00000497280.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..422
                     /product="acylglycerol kinase, mitochondrial isoform 1
                     precursor"
                     /EC_number="2.7.1.107"
                     /EC_number="2.7.1.94"
                     /EC_number="2.7.1.138"
                     /note="multi-substrate lipid kinase; multiple substrate
                     lipid kinase; acylglycerol kinase, mitochondrial; hAGK;
                     hsMuLK"
                     /calculated_mol_wt=47006
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q53H12.2)"
     Region          15..31
                     /region_name="Hydrophobic. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53H12.2)"
     Region          62..195
                     /region_name="DAGK_cat"
                     /note="Diacylglycerol kinase catalytic domain; pfam00781"
                     /db_xref="CDD:425868"
     Region          206..421
                     /region_name="AGK_C"
                     /note="Acylglycerol kinase C-terminal; pfam19712"
                     /db_xref="CDD:466156"
     Region          249..271
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53H12.2)"
     CDS             1..422
                     /gene="AGK"
                     /gene_synonym="CATC5; CTRCT38; MTDPS10; MULK"
                     /coded_by="NM_018238.4:40..1308"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS5865.1"
                     /db_xref="GeneID:55750"
                     /db_xref="HGNC:HGNC:21869"
                     /db_xref="MIM:610345"
ORIGIN      
        1 mtvffktlrn hwkkttaglc lltwgghwly gkhcdnllrr aacqeaqvfg nqlippnaqv
       61 kkatvflnpa ackgkartlf eknaapilhl sgmdvtivkt dyegqakkll elmentdvii
      121 vaggdgtlqe vvtgvlrrtd eatfskipig fiplgetssl shtlfaesgn kvqhitdatl
      181 aivkgetvpl dvlqikgeke qpvfamtglr wgsfrdagvk vskywylgpl kikaahffst
      241 lkewpqthqa sisytgpter ppnepeetpv qrpslyrril rrlasywaqp qdalsqevsp
      301 evwkdvqlst ielsittrnn qldptskedf lniciepdti skgdfitigs rkvrnpklhv
      361 egteclqasq ctllipegag gsfsidseey eampvevkll prklqffcdp rkreqmltsp
      421 tq
//
LOCUS       NP_061931                232 aa            linear   PRI 27-APR-2025
DEFINITION  DNA damage-inducible transcript 4 protein [Homo sapiens].
ACCESSION   NP_061931
VERSION     NP_061931.1
DBSOURCE    REFSEQ: accession NM_019058.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Campoy-Campos,G., Solana-Balaguer,J., Guisado-Corcoll,A.,
            Chicote-Gonzalez,A., Garcia-Segura,P., Perez-Sisques,L.,
            Torres,A.G., Canal,M., Molina-Porcel,L., Fernandez-Irigoyen,J.,
            Santamaria,E., Ribas de Pouplana,L., Alberch,J., Marti,E.,
            Giralt,A., Perez-Navarro,E. and Malagelada,C.
  TITLE     RTP801 interacts with the tRNA ligase complex and dysregulates its
            RNA ligase activity in Alzheimer's disease
  JOURNAL   Nucleic Acids Res 52 (18), 11158-11176 (2024)
   PUBMED   39268577
  REMARK    GeneRIF: RTP801 interacts with the tRNA ligase complex and
            dysregulates its RNA ligase activity in Alzheimer's disease.
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Li,F., Miao,J., Liu,R., Zhang,R. and He,A.
  TITLE     Pan-cancer analysis of DDIT4 identifying its prognostic value and
            function in acute myeloid leukemia
  JOURNAL   J Cancer Res Clin Oncol 150 (3), 144 (2024)
   PUBMED   38507057
  REMARK    GeneRIF: Pan-cancer analysis of DDIT4 identifying its prognostic
            value and function in acute myeloid leukemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   McCurry,C.M., Sunilkumar,S., Subrahmanian,S.M., Yerlikaya,E.I.,
            Toro,A.L., VanCleave,A.M., Stevens,S.A., Barber,A.J.,
            Sundstrom,J.M. and Dennis,M.D.
  TITLE     NLRP3 Inflammasome Priming in the Retina of Diabetic Mice Requires
            REDD1-Dependent Activation of GSK3beta
  JOURNAL   Invest Ophthalmol Vis Sci 65 (3), 34 (2024)
   PUBMED   38546584
  REMARK    GeneRIF: NLRP3 Inflammasome Priming in the Retina of Diabetic Mice
            Requires REDD1-Dependent Activation of GSK3beta.
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Tajik,F., Fattahi,F., Rezagholizadeh,F., Bouzari,B.,
            Babaheidarian,P., Baghai Wadji,M. and Madjd,Z.
  TITLE     Nuclear overexpression of DNA damage-inducible transcript 4 (DDIT4)
            is associated with aggressive tumor behavior in patients with
            pancreatic tumors
  JOURNAL   Sci Rep 13 (1), 19403 (2023)
   PUBMED   37938616
  REMARK    GeneRIF: Nuclear overexpression of DNA damage-inducible transcript
            4 (DDIT4) is associated with aggressive tumor behavior in patients
            with pancreatic tumors.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Chudakova,D.A., Trubetskoy,D., Baida,G., Bhalla,P., Readhead,B. and
            Budunova,I.
  TITLE     REDD1 (regulated in development and DNA damage 1) modulates the
            glucocorticoid receptor function in keratinocytes
  JOURNAL   Exp Dermatol 32 (10), 1725-1733 (2023)
   PUBMED   37483165
  REMARK    GeneRIF: REDD1 (regulated in development and DNA damage 1)
            modulates the glucocorticoid receptor function in keratinocytes.
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Lee,M., Bikram,M., Oh,S., Bull,D.A. and Kim,S.W.
  TITLE     Sp1-dependent regulation of the RTP801 promoter and its application
            to hypoxia-inducible VEGF plasmid for ischemic disease
  JOURNAL   Pharm Res 21 (5), 736-741 (2004)
   PUBMED   15180327
  REMARK    GeneRIF: co-transfection with antisense Sp1 oligonucleotide
            suggests that hypoxia induction of the RTP801 promoter is mediated
            by Sp1
REFERENCE   7  (residues 1 to 232)
  AUTHORS   Kim,J.R., Lee,S.R., Chung,H.J., Kim,S., Baek,S.H., Kim,J.H. and
            Kim,Y.S.
  TITLE     Identification of amyloid beta-peptide responsive genes by cDNA
            microarray technology: involvement of RTP801 in amyloid
            beta-peptide toxicity
  JOURNAL   Exp Mol Med 35 (5), 403-411 (2003)
   PUBMED   14646594
  REMARK    GeneRIF: RTP801 might play important roles in Abeta toxicity and
            the pathogenesis of Alzheimer's disease
REFERENCE   8  (residues 1 to 232)
  AUTHORS   Ellisen,L.W., Ramsayer,K.D., Johannessen,C.M., Yang,A., Beppu,H.,
            Minda,K., Oliner,J.D., McKeon,F. and Haber,D.A.
  TITLE     REDD1, a developmentally regulated transcriptional target of p63
            and p53, links p63 to regulation of reactive oxygen species
  JOURNAL   Mol Cell 10 (5), 995-1005 (2002)
   PUBMED   12453409
REFERENCE   9  (residues 1 to 232)
  AUTHORS   Shoshani,T., Faerman,A., Mett,I., Zelin,E., Tenne,T., Gorodin,S.,
            Moshel,Y., Elbaz,S., Budanov,A., Chajut,A., Kalinski,H., Kamer,I.,
            Rozen,A., Mor,O., Keshet,E., Leshkowitz,D., Einat,P., Skaliter,R.
            and Feinstein,E.
  TITLE     Identification of a novel hypoxia-inducible factor 1-responsive
            gene, RTP801, involved in apoptosis
  JOURNAL   Mol Cell Biol 22 (7), 2283-2293 (2002)
   PUBMED   11884613
REFERENCE   10 (residues 1 to 232)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BE882343.1, BC015236.1, BC007714.1 and AF335324.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000507.1, AL136668.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307365.4/ ENSP00000307305.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..232
                     /product="DNA damage-inducible transcript 4 protein"
                     /note="HIF-1 responsive protein RTP801; protein regulated
                     in development and DNA damage response 1"
                     /calculated_mol_wt=25240
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX09.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19557001; propagated from
                     UniProtKB/Swiss-Prot (Q9NX09.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19557001; propagated from
                     UniProtKB/Swiss-Prot (Q9NX09.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19557001; propagated from
                     UniProtKB/Swiss-Prot (Q9NX09.1)"
     Region          104..223
                     /region_name="RTP801_C"
                     /note="RTP801 C-terminal region; pfam07809"
                     /db_xref="CDD:462274"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19557001; propagated from
                     UniProtKB/Swiss-Prot (Q9NX09.1)"
     CDS             1..232
                     /gene="DDIT4"
                     /gene_synonym="Dig2; REDD-1; REDD1"
                     /coded_by="NM_019058.4:198..896"
                     /db_xref="CCDS:CCDS7315.1"
                     /db_xref="GeneID:54541"
                     /db_xref="HGNC:HGNC:24944"
                     /db_xref="MIM:607729"
ORIGIN      
        1 mpslwdrfss sstssspssl prtptpdrpp rsawgsatre egfdrstsle ssdcesldss
       61 nsgfgpeedt ayldgvslpd fellsdpede hlcanlmqll qeslaqarlg srrparllmp
      121 sqlvsqvgke llrlaysepc glrgalldvc veqgkschsv gqlaldpslv ptfqltlvlr
      181 ldsrlwpkiq glfssanspf lpgfsqsltl stgfrvikkk lysseqllie ec
//
LOCUS       NP_004144                861 aa            linear   PRI 27-APR-2025
DEFINITION  origin recognition complex subunit 1 isoform 1 [Homo sapiens].
ACCESSION   NP_004144
VERSION     NP_004144.2
DBSOURCE    REFSEQ: accession NM_004153.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Xia,L., Nie,T., Lu,F., Huang,L., Shi,X., Ren,D., Lu,J., Li,X.,
            Xu,T., Cui,B., Wang,Q., Gao,G. and Yang,Q.
  TITLE     Direct regulation of FNIP1 and FNIP2 by MEF2 sustains MTORC1
            activation and tumor progression in pancreatic cancer
  JOURNAL   Autophagy 20 (3), 505-524 (2024)
   PUBMED   37772772
  REMARK    GeneRIF: Direct regulation of FNIP1 and FNIP2 by MEF2 sustains
            MTORC1 activation and tumor progression in pancreatic cancer.
REFERENCE   2  (residues 1 to 861)
  AUTHORS   Wu,L., Chen,H. and Yang,C.
  TITLE     Origin recognition complex subunit 1(ORC1) is a potential biomarker
            and therapeutic target in cancer
  JOURNAL   BMC Med Genomics 16 (1), 243 (2023)
   PUBMED   37833711
  REMARK    GeneRIF: Origin recognition complex subunit 1(ORC1) is a potential
            biomarker and therapeutic target in cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 861)
  AUTHORS   Han,L. and Li,F.
  TITLE     Origin recognition complex subunit 1 (ORC1) augments malignant
            behaviors of lung adenocarcinoma cells via targeting Wnt signaling
  JOURNAL   Bioengineered 13 (5), 13520-13533 (2022)
   PUBMED   36700467
  REMARK    GeneRIF: Origin recognition complex subunit 1 (ORC1) augments
            malignant behaviors of lung adenocarcinoma cells via targeting Wnt
            signaling.
REFERENCE   4  (residues 1 to 861)
  AUTHORS   Hossain,M., Bhalla,K. and Stillman,B.
  TITLE     Multiple, short protein binding motifs in ORC1 and CDC6 control the
            initiation of DNA replication
  JOURNAL   Mol Cell 81 (9), 1951-1969 (2021)
   PUBMED   33761311
  REMARK    GeneRIF: Multiple, short protein binding motifs in ORC1 and CDC6
            control the initiation of DNA replication.
REFERENCE   5  (residues 1 to 861)
  AUTHORS   Jaremko,M.J., On,K.F., Thomas,D.R., Stillman,B. and Joshua-Tor,L.
  TITLE     The dynamic nature of the human origin recognition complex revealed
            through five cryoEM structures
  JOURNAL   Elife 9, e58622 (2020)
   PUBMED   32808929
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 861)
  AUTHORS   Herbig,U., Marlar,C.A. and Fanning,E.
  TITLE     The Cdc6 nucleotide-binding site regulates its activity in DNA
            replication in human cells
  JOURNAL   Mol Biol Cell 10 (8), 2631-2645 (1999)
   PUBMED   10436018
REFERENCE   7  (residues 1 to 861)
  AUTHORS   Saha,P., Chen,J., Thome,K.C., Lawlis,S.J., Hou,Z.H., Hendricks,M.,
            Parvin,J.D. and Dutta,A.
  TITLE     Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is
            selectively eliminated from the nucleus at the onset of S phase
  JOURNAL   Mol Cell Biol 18 (5), 2758-2767 (1998)
   PUBMED   9566895
REFERENCE   8  (residues 1 to 861)
  AUTHORS   Ohtani,K., DeGregori,J., Leone,G., Herendeen,D.R., Kelly,T.J. and
            Nevins,J.R.
  TITLE     Expression of the HsOrc1 gene, a human ORC1 homolog, is regulated
            by cell proliferation via the E2F transcription factor
  JOURNAL   Mol Cell Biol 16 (12), 6977-6984 (1996)
   PUBMED   8943353
REFERENCE   9  (residues 1 to 861)
  AUTHORS   Eki,T., Okumura,K., Amin,A., Ishiai,M., Abe,M., Nogami,M.,
            Taguchi,H., Hurwitz,J., Murakami,Y. and Hanaoka,F.
  TITLE     Mapping of the human homologue (ORC1L) of the yeast origin
            recognition complex subunit 1 gene to chromosome band 1p32
  JOURNAL   Genomics 36 (3), 559-561 (1996)
   PUBMED   8884289
REFERENCE   10 (residues 1 to 861)
  AUTHORS   Gavin,K.A., Hidaka,M. and Stillman,B.
  TITLE     Conserved initiator proteins in eukaryotes
  JOURNAL   Science 270 (5242), 1667-1671 (1995)
   PUBMED   7502077
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U40152.1 and U43416.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 17, 2003 this sequence version replaced NP_004144.1.
            
            Summary: The origin recognition complex (ORC) is a highly conserved
            six subunits protein complex essential for the initiation of the
            DNA replication in eukaryotic cells. Studies in yeast demonstrated
            that ORC binds specifically to origins of replication and serves as
            a platform for the assembly of additional initiation factors such
            as Cdc6 and Mcm proteins. The protein encoded by this gene is the
            largest subunit of the ORC complex. While other ORC subunits are
            stable throughout the cell cycle, the levels of this protein vary
            during the cell cycle, which has been shown to be controlled by
            ubiquitin-mediated proteolysis after initiation of DNA replication.
            This protein is found to be selectively phosphorylated during
            mitosis. It is also reported to interact with MYST histone
            acetyltransferase 2 (MyST2/HBO1), a protein involved in control of
            transcription silencing. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (1) is the longest transcript and
            encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U43416.1, SRR1803613.50543.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371568.8/ ENSP00000360623.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..861
                     /product="origin recognition complex subunit 1 isoform 1"
                     /note="origin recognition complex, subunit 1 homolog;
                     replication control protein 1"
                     /calculated_mol_wt=97219
     Region          44..170
                     /region_name="BAH_Orc1p_animal"
                     /note="BAH, or Bromo Adjacent Homology domain, as present
                     in animal homologs of Saccharomyces cerevisiae Orc1p. Orc1
                     is part of the Yeast Sir1-origin recognition complex. The
                     Orc1p BAH doman functions in epigenetic silencing. In
                     vertebrates, a similar ORC...; cd04719"
                     /db_xref="CDD:240070"
     Site            94
                     /site_type="other"
                     /note="Histone H4K20me2 binding.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1N2; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Region          183..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13415.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1N2; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1N2; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Region          269..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13415.2)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13415.2)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Site            326
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Region          360..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13415.2)"
     Region          <362..>487
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          412..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13415.2)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13415.2)"
     Region          <495..743
                     /region_name="PTZ00112"
                     /note="origin recognition complex 1 protein; Provisional"
                     /db_xref="CDD:240274"
     Region          501..861
                     /region_name="Necessary and sufficient for ORC complex
                     assembly"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13415.2)"
     Region          778..857
                     /region_name="Cdc6_C"
                     /note="CDC6, C terminal winged helix domain; pfam09079"
                     /db_xref="CDD:462672"
     CDS             1..861
                     /gene="ORC1"
                     /gene_synonym="HSORC1; ORC1L; PARC1"
                     /coded_by="NM_004153.4:184..2769"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS566.1"
                     /db_xref="GeneID:4998"
                     /db_xref="HGNC:HGNC:8487"
                     /db_xref="MIM:601902"
ORIGIN      
        1 mahyptrlkt rktyswvgrp lldrklhyqt yremcvkteg csteihiqig qfvliegddd
       61 enpyvaklle lfeddsdppp kkrarvqwfv rfcevpackr hllgrkpgaq eifwydypac
      121 dsninaetii glvrviplap kdvvptnlkn ektlfvklsw nekkfrplss elfaelnkpq
      181 esaakcqkpv raksksaesp swtpaehvak riesrhsask srqtpthplt prarkrlelg
      241 nlgnpqmsqq tscasldspg rikrkvafse itspskrsqp dklqtlspal kapektretg
      301 lsyteddkka spehriilrt riaasktidi reertltpis ggqrssvvps vilkpenikk
      361 rdakeakaqn eatstphrir rkssvltmnr irqqlrflgn sksdqeekei lpaaeisdss
      421 sdeeeastpp lprraprtvs rnlrsslkss lhtltkvpkk slkprtprca apqirsrsla
      481 aqepasvlee arlrlhvsav peslpcreqe fqdiynfves klldhtggcm yisgvpgtgk
      541 tatvhevirc lqqaaqandv ppfqyievng mkltephqvy vqilqkltgq katanhaael
      601 lakqfctrgs pqettvllvd eldllwthkq dimynlfdwp thkearlvvl aiantmdlpe
      661 rimmnrvssr lgltrmcfqp ytysqlqqil rsrlkhlkaf eddaiqlvar kvaalsgdar
      721 rcldicrrat eicefsqqkp dspglvtiah smeavdemfs ssyitaikns svleqsflra
      781 ilaefrrsgl eeatfqqiys qhvalcrmeg lpyptmsetm avcshlgscr lllvepsrnd
      841 lllrvrlnvs qddvlyalkd e
//
LOCUS       NP_002306                156 aa            linear   PRI 27-APR-2025
DEFINITION  rhombotin-1 isoform a [Homo sapiens].
ACCESSION   NP_002306
VERSION     NP_002306.1
DBSOURCE    REFSEQ: accession NM_002315.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Yu,Y., Li,H., Wu,C. and Li,J.
  TITLE     Circ_0021087 acts as a miR-184 sponge and represses gastric cancer
            progression by adsorbing miR-184 and elevating FOSB expression
  JOURNAL   Eur J Clin Invest 51 (11), e13605 (2021)
   PUBMED   34076278
  REMARK    GeneRIF: Circ_0021087 acts as a miR-184 sponge and represses
            gastric cancer progression by adsorbing miR-184 and elevating FOSB
            expression.
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Hashemi,M., Sarabandi,S., Karami,S., Smieja,J., Moazeni-Roodi,A.,
            Ghavami,S. and Los,M.J.
  TITLE     LMO1 polymorphisms and the risk of neuroblastoma: Assessment of
            meta-analysis of case-control studies
  JOURNAL   J Cell Mol Med 24 (2), 1160-1168 (2020)
   PUBMED   31830377
  REMARK    GeneRIF: LMO1 polymorphisms and the risk of neuroblastoma:
            Assessment of meta-analysis of case-control studies.
            Review article
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Wang,L., Tan,T.K., Durbin,A.D., Zimmerman,M.W., Abraham,B.J.,
            Tan,S.H., Ngoc,P.C.T., Weichert-Leahey,N., Akahane,K., Lawton,L.N.,
            Rokita,J.L., Maris,J.M., Young,R.A., Look,A.T. and Sanda,T.
  TITLE     ASCL1 is a MYCN- and LMO1-dependent member of the adrenergic
            neuroblastoma core regulatory circuitry
  JOURNAL   Nat Commun 10 (1), 5622 (2019)
   PUBMED   31819055
  REMARK    GeneRIF: ASCL1 and LMO1 directly regulate the expression of CRC
            genes, indicating that ASCL1 is a member and LMO1 is a coregulator
            of the ADRN neuroblastoma core regulatory circuitry.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Foroni,L., Boehm,T., White,L., Forster,A., Sherrington,P.,
            Liao,X.B., Brannan,C.I., Jenkins,N.A., Copeland,N.G. and
            Rabbitts,T.H.
  TITLE     The rhombotin gene family encode related LIM-domain proteins whose
            differing expression suggests multiple roles in mouse development
  JOURNAL   J Mol Biol 226 (3), 747-761 (1992)
   PUBMED   1507224
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Boehm,T., Foroni,L., Kaneko,Y., Perutz,M.F. and Rabbitts,T.H.
  TITLE     The rhombotin family of cysteine-rich LIM-domain oncogenes:
            distinct members are involved in T-cell translocations to human
            chromosomes 11p15 and 11p13
  JOURNAL   Proc Natl Acad Sci U S A 88 (10), 4367-4371 (1991)
   PUBMED   2034676
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Boehm,T., Spillantini,M.G., Sofroniew,M.V., Surani,M.A. and
            Rabbitts,T.H.
  TITLE     Developmentally regulated and tissue specific expression of mRNAs
            encoding the two alternative forms of the LIM domain oncogene
            rhombotin: evidence for thymus expression
  JOURNAL   Oncogene 6 (5), 695-703 (1991)
   PUBMED   2052354
REFERENCE   9  (residues 1 to 156)
  AUTHORS   McGuire,E.A., Davis,A.R. and Korsmeyer,S.J.
  TITLE     T-cell translocation gene 1 (Ttg-1) encodes a nuclear protein
            normally expressed in neural lineage cells
  JOURNAL   Blood 77 (3), 599-606 (1991)
   PUBMED   1703797
REFERENCE   10 (residues 1 to 156)
  AUTHORS   Chen,Q., Cheng,J.T., Tasi,L.H., Schneider,N., Buchanan,G.,
            Carroll,A., Crist,W., Ozanne,B., Siciliano,M.J. and Baer,R.
  TITLE     The tal gene undergoes chromosome translocation in T cell leukemia
            and potentially encodes a helix-loop-helix protein
  JOURNAL   EMBO J 9 (2), 415-424 (1990)
   PUBMED   2303035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091013.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This locus encodes a transcriptional regulator that
            contains two cysteine-rich LIM domains but lacks a DNA-binding
            domain. LIM domains may play a role in protein interactions; thus
            the encoded protein may regulate transcription by competitively
            binding to specific DNA-binding transcription factors. Alterations
            at this locus have been associated with acute lymphoblastic T-cell
            leukemia. Chromosomal rearrangements have been observed between
            this locus and at least two loci, the delta subunit of the T-cell
            antigen receptor gene and the LIM domain binding 1 gene.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M26682.1, BC069793.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335790.8/ ENSP00000338207.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..156
                     /product="rhombotin-1 isoform a"
                     /note="rhombotin-1; LMO-1; LIM domain only protein 1;
                     cysteine-rich protein TTG-1; T-cell translocation protein
                     1; T-cell translocation gene 1; LIM domain only 1
                     (rhombotin 1)"
                     /calculated_mol_wt=17697
     Region          24..78
                     /region_name="LIM1_LMO1_LMO3"
                     /note="The first LIM domain of LMO1 and LMO3 (LIM domain
                     only protein 1 and 3); cd09388"
                     /db_xref="CDD:188774"
     Site            order(24,27,45,48,51,54,74,77)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188774"
     Region          88..142
                     /region_name="LIM2_LMO1_LMO3"
                     /note="The second LIM domain of LMO1 and LMO3 (LIM domain
                     only protein 1 and 3); cd09389"
                     /db_xref="CDD:188775"
     Site            order(88,91,110,113,116,119,138,141)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188775"
     CDS             1..156
                     /gene="LMO1"
                     /gene_synonym="RBTN1; RHOM1; TTG1"
                     /coded_by="NM_002315.3:517..987"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44534.1"
                     /db_xref="GeneID:4004"
                     /db_xref="HGNC:HGNC:6641"
                     /db_xref="MIM:186921"
ORIGIN      
        1 mmvldkedgv pmlsvqpkgk qkgcagcnrk ikdryllkal dkywhedclk caccdcrlge
       61 vgstlytkan lilcrrdylr lfgttgncaa csklipafem vmrardnvyh ldcfacqlcn
      121 qrfcvgdkff lknnmilcqm dyeegqlngt fesqvq
//
LOCUS       NP_036329               1069 aa            linear   PRI 27-APR-2025
DEFINITION  rab GTPase-activating protein 1 [Homo sapiens].
ACCESSION   NP_036329
VERSION     NP_036329.3
DBSOURCE    REFSEQ: accession NM_012197.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Nagai,H., Yasuda,S., Ohba,Y., Fukuda,M. and Nakamura,T.
  TITLE     All members of the EPI64 subfamily of TBC/RabGAPs also have GAP
            activities towards Ras
  JOURNAL   J Biochem 153 (3), 283-288 (2013)
   PUBMED   23248241
  REMARK    GeneRIF: suggest that EPI64A and B, which are ubiquitously
            expressed members of the EPI64 subfamily, inactivate Ras and
            certain Rabs at the periphery of cells.
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Popovic,D., Akutsu,M., Novak,I., Harper,J.W., Behrends,C. and
            Dikic,I.
  TITLE     Rab GTPase-activating proteins in autophagy: regulation of
            endocytic and autophagy pathways by direct binding to human ATG8
            modifiers
  JOURNAL   Mol Cell Biol 32 (9), 1733-1744 (2012)
   PUBMED   22354992
REFERENCE   4  (residues 1 to 1069)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   5  (residues 1 to 1069)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   6  (residues 1 to 1069)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   7  (residues 1 to 1069)
  AUTHORS   Fuchs,E., Haas,A.K., Spooner,R.A., Yoshimura,S., Lord,J.M. and
            Barr,F.A.
  TITLE     Specific Rab GTPase-activating proteins define the Shiga toxin and
            epidermal growth factor uptake pathways
  JOURNAL   J Cell Biol 177 (6), 1133-1143 (2007)
   PUBMED   17562788
REFERENCE   8  (residues 1 to 1069)
  AUTHORS   Echard,A., Opdam,F.J., de Leeuw,H.J., Jollivet,F., Savelkoul,P.,
            Hendriks,W., Voorberg,J., Goud,B. and Fransen,J.A.
  TITLE     Alternative splicing of the human Rab6A gene generates two close
            but functionally different isoforms
  JOURNAL   Mol Biol Cell 11 (11), 3819-3833 (2000)
   PUBMED   11071909
REFERENCE   9  (residues 1 to 1069)
  AUTHORS   Opdam,F.J., Echard,A., Croes,H.J., van den Hurk,J.A., van de
            Vorstenbosch,R.A., Ginsel,L.A., Goud,B. and Fransen,J.A.
  TITLE     The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type
            specifically expressed and localised to the Golgi apparatus
  JOURNAL   J Cell Sci 113 (Pt 15), 2725-2735 (2000)
   PUBMED   10893188
REFERENCE   10 (residues 1 to 1069)
  AUTHORS   Cuif,M.H., Possmayer,F., Zander,H., Bordes,N., Jollivet,F.,
            Couedel-Courteille,A., Janoueix-Lerosey,I., Langsley,G., Bornens,M.
            and Goud,B.
  TITLE     Characterization of GAPCenA, a GTPase activating protein for Rab6,
            part of which associates with the centrosome
  JOURNAL   EMBO J 18 (7), 1772-1782 (1999)
   PUBMED   10202141
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG622097.1, BC054492.1, AL365338.17 and AA948302.1.
            
            On Jan 9, 2008 this sequence version replaced NP_036329.2.
            
            Sequence Note: The RefSeq transcript and protein was created from
            transcript and genomic sequence data to make the sequence
            consistent with the reference genome assembly. The extent of this
            transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ011679.2, BC054492.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373647.9/ ENSP00000362751.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.2-q33.3"
     Protein         1..1069
                     /product="rab GTPase-activating protein 1"
                     /note="rab6 GTPase activating protein (GAP and
                     centrosome-associated); TBC1 domain family, member 11;
                     Rab6 GTPase activating protein, GAPCenA; GAP and
                     centrosome-associated protein; rab6 GTPase-activating
                     protein GAPCenA"
                     /calculated_mol_wt=121606
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3P9.3)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3P9.3)"
     Region          145..273
                     /region_name="PTB_Rab6GAP"
                     /note="GTPase activating protein for Rab 6
                     Phosphotyrosine-binding (PTB) domain; cd01211"
                     /db_xref="CDD:269922"
     Site            order(151,229,249)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269922"
     Site            order(215..220,236,257,261)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269922"
     Region          307..437
                     /region_name="DUF3694"
                     /note="Kinesin protein; pfam12473"
                     /db_xref="CDD:463599"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AWA9; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3P9.3)"
     Region          482..527
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3P9.3)"
     Region          563..772
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            608
                     /site_type="other"
                     /note="Arginine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9Y3P9.3)"
     Site            649
                     /site_type="other"
                     /note="Glutamine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9Y3P9.3)"
     Region          <825..>1032
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            996
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3P9.3)"
     CDS             1..1069
                     /gene="RABGAP1"
                     /gene_synonym="GAPCENA; TBC1D11"
                     /coded_by="NM_012197.4:124..3333"
                     /db_xref="CCDS:CCDS6848.2"
                     /db_xref="GeneID:23637"
                     /db_xref="HGNC:HGNC:17155"
                     /db_xref="MIM:615882"
ORIGIN      
        1 mddkasvgki svssdsvstl nsedfvlvsr qgdetpstnn gsddektglk ivgngseqql
       61 qkeladvlmd ppmddqpgek elvkrsqldg egdgplsnql sasstinpvp lvglqkpems
      121 lpvkpgqgds easspftpva dedsvvfskl tylgcasvna prsevealrm msilrsqcqi
      181 sldvtlsvpn vsegivrlld pqtnteiany piykilfcvr ghdgtpesdc fafteshyna
      241 elfrihvfrc eiqeavsril ysfatafrrs akqtplsata apqtpdsdif tfsvsleike
      301 ddgkgyfsav pkdkdrqcfk lrqgidkkiv iyvqqttnke laiercfgll lspgkdvrns
      361 dmhlldlesm gkssdgksyv itgswnpksp hfqvvneetp kdkvlfmtta vdlvitevqe
      421 pvrflletkv rvcspnerlf wpfskrstte nfflklkqik qrerknntdt lyevvclese
      481 sererrktta spsvrlpqsg sqssvipspp eddeeednde pllsgsgdvs kecaekilet
      541 wgellskwhl nlnvrpkqls slvrngvpea lrgevwqlla gchnndhlve kyrilitkes
      601 pqdsaitrdi nrtfpahdyf kdtggdgqds lykickaysv ydeeigycqg qsflaavlll
      661 hmpeeqafsv lvkimfdygl relfkqnfed lhckfyqler lmqeyipdly nhfldislea
      721 hmyasqwflt lftakfplym vfhiidlllc egisvifnva lgllktskdd llltdfegal
      781 kffrvqlpkr yrseenakkl melacnmkis qkklkkyeke yhtmreqqaq qedpierfer
      841 enrrlqeanm rleqenddla helvtskial rkdldnaeek adalnkellm tkqklidaee
      901 ekrrleeesa qlkemcrrel dkaeseikkn ssiigdykqi csqlserlek qqtankveie
      961 kirqkvddce rcreffnkeg rvkgisstke vldedtdeek etlknqlrem elelaqtklq
     1021 lveaeckiqd lehhlglaln evqaakktwf nrtlssikta tgvqgketc
//
LOCUS       NP_443095                104 aa            linear   PRI 27-APR-2025
DEFINITION  secretoglobin family 3A member 1 precursor [Homo sapiens].
ACCESSION   NP_443095
VERSION     NP_443095.2
DBSOURCE    REFSEQ: accession NM_052863.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Costa,A.L., Moreira-Barbosa,C., Lobo,J., Vilela-Salgueiro,B.,
            Cantante,M., Guimaraes,R., Lopes,P., Braga,I., Oliveira,J.,
            Antunes,L., Henrique,R. and Jeronimo,C.
  TITLE     DNA methylation profiling as a tool for testicular germ cell tumors
            subtyping
  JOURNAL   Epigenomics 10 (12), 1511-1523 (2018)
   PUBMED   30418048
  REMARK    GeneRIF: HOXA9, RASSF1A and SCGB3A1 promoter methylation
            significantly associated with testicular germ cell tumor stage.
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Atilla,M.H., Ozdas,S., Ozdas,T., Bastimur,S., Muz,S.E., Oz,I.,
            Kurt,K., Izbirak,A., Babademez,M.A. and Vatandas,N.
  TITLE     Association of Ugrp2 gene polymorphisms with adenoid hypertrophy in
            the pediatric population
  JOURNAL   Braz J Otorhinolaryngol 84 (5), 599-607 (2018)
   PUBMED   28823693
  REMARK    GeneRIF: Some single nucleotide polymorphisms and their
            combinations in the Ugrp2 gene are associated with an increased
            risk of developing adenoid hypertrophy.
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Herranz,M., Padin-Iruegas,M.E., Martinez-Lago,N., Losada,S.A.,
            Rana-Diez,P., Vazquez,E.B., Carrera,J.J., Antunez,J.R., Ruibal,A.
            and Lopez-Lopez,R.
  TITLE     HIN-1: a New Epigenetic Biomarker Crucial for Therapy Selection in
            Glioblastoma Multiforme
  JOURNAL   Mol Neurobiol 53 (3), 1802-1807 (2016)
   PUBMED   25752997
  REMARK    GeneRIF: The role of high in normal-1 (HIN-1) as a potential
            biomarker in combating glioblastoma is being described for the
            first time in this study.
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Spitzwieser,M., Holzweber,E., Pfeiler,G., Hacker,S. and
            Cichna-Markl,M.
  TITLE     Applicability of HIN-1, MGMT and RASSF1A promoter methylation as
            biomarkers for detecting field cancerization in breast cancer
  JOURNAL   Breast Cancer Res 17 (1), 125 (2015)
   PUBMED   26370119
  REMARK    GeneRIF: Tumor-adjacent tissues showed higher methylation status of
            RASSF1A, HIN-1 and MGMT promoters.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Krop,I., Maguire,P., Lahti-Domenici,J., Lodeiro,G., Richardson,A.,
            Johannsdottir,H.K., Nevanlinna,H., Borg,A., Gelman,R.,
            Barkardottir,R.B., Lindblom,A. and Polyak,K.
  TITLE     Lack of HIN-1 methylation in BRCA1-linked and 'BRCA1-like' breast
            tumors
  JOURNAL   Cancer Res 63 (9), 2024-2027 (2003)
   PUBMED   12727813
  REMARK    GeneRIF: Sporadic breast tumors with a 'BRCA1-like'
            histopathological phenotype also demonstrated significantly lower
            frequency of HIN-1 promoter methylation.
REFERENCE   7  (residues 1 to 104)
  AUTHORS   Reynolds,S.D., Reynolds,P.R., Pryhuber,G.S., Finder,J.D. and
            Stripp,B.R.
  TITLE     Secretoglobins SCGB3A1 and SCGB3A2 define secretory cell subsets in
            mouse and human airways
  JOURNAL   Am J Respir Crit Care Med 166 (11), 1498-1509 (2002)
   PUBMED   12406855
REFERENCE   8  (residues 1 to 104)
  AUTHORS   Porter,D., Lahti-Domenici,J., Torres-Arzayus,M., Chin,L. and
            Polyak,K.
  TITLE     Expression of high in normal-1 (HIN-1) and uteroglobin related
            protein-1 (UGRP-1) in adult and developing tissues
  JOURNAL   Mech Dev 114 (1-2), 201-204 (2002)
   PUBMED   12175512
REFERENCE   9  (residues 1 to 104)
  AUTHORS   Niimi,T., Copeland,N.G., Gilbert,D.J., Jenkins,N.A., Srisodsai,A.,
            Zimonjic,D.B., Keck-Waggoner,C.L., Popescu,N.C. and Kimura,S.
  TITLE     Cloning, expression, and chromosomal localization of the mouse gene
            (Scgb3a1, alias Ugrp2) that encodes a member of the novel
            uteroglobin-related protein gene family
  JOURNAL   Cytogenet Genome Res 97 (1-2), 120-127 (2002)
   PUBMED   12438750
REFERENCE   10 (residues 1 to 104)
  AUTHORS   Krop,I.E., Sgroi,D., Porter,D.A., Lunetta,K.L., LeVangie,R.,
            Seth,P., Kaelin,C.M., Rhei,E., Bosenberg,M., Schnitt,S.,
            Marks,J.R., Pagon,Z., Belina,D., Razumovic,J. and Polyak,K.
  TITLE     HIN-1, a putative cytokine highly expressed in normal but not
            cancerous mammary epithelial cells
  JOURNAL   Proc Natl Acad Sci U S A 98 (17), 9796-9801 (2001)
   PUBMED   11481438
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC122714.2 and AY359064.1.
            
            On Jul 19, 2004 this sequence version replaced NP_443095.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY359064.1, AF436839.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2147920
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000292641.4/ ENSP00000292641.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..104
                     /product="secretoglobin family 3A member 1 precursor"
                     /note="pneumo secretory protein 2; cytokine high in
                     normal-1; cytokine HIN-1; high in normal 1;
                     uteroglobin-related protein 2"
                     /calculated_mol_wt=8225
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1893
     Region          19..94
                     /region_name="SCGB3A"
                     /note="Secretoglobin 3A; pfam20490"
                     /db_xref="CDD:466639"
     mat_peptide     21..104
                     /product="Secretoglobin family 3A member 1.
                     /id=PRO_0000036383"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QR1.2)"
                     /calculated_mol_wt=8225
     CDS             1..104
                     /gene="SCGB3A1"
                     /gene_synonym="HIN-1; HIN1; LU105; PnSP-2; UGRP2"
                     /coded_by="NM_052863.3:38..352"
                     /db_xref="CCDS:CCDS4456.1"
                     /db_xref="GeneID:92304"
                     /db_xref="HGNC:HGNC:18384"
                     /db_xref="MIM:606500"
ORIGIN      
        1 mklaallglc valscssaaa flvgsakpva qpvaalesaa eagagtlanp lgtlnplkll
       61 lsslgipvnh liegsqkcva elgpqavgav kalkallgal tvfg
//
LOCUS       NP_001268996             242 aa            linear   ROD 27-APR-2025
DEFINITION  lysosomal membrane ascorbate-dependent ferrireductase CYB561A3
            isoform 1 [Mus musculus].
ACCESSION   NP_001268996
VERSION     NP_001268996.1
DBSOURCE    REFSEQ: accession NM_001282067.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Zhang,D.L., Su,D., Berczi,A., Vargas,A. and Asard,H.
  TITLE     An ascorbate-reducible cytochrome b561 is localized in macrophage
            lysosomes
  JOURNAL   Biochim Biophys Acta 1760 (12), 1903-1913 (2006)
   PUBMED   16996694
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Su,D. and Asard,H.
  TITLE     Three mammalian cytochromes b561 are ascorbate-dependent
            ferrireductases
  JOURNAL   FEBS J 273 (16), 3722-3734 (2006)
   PUBMED   16911521
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK139533.1, AK168841.1 and BY387699.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK170911.1, SRR5286961.49469.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 6.6 cM"
     Protein         1..242
                     /product="lysosomal membrane ascorbate-dependent
                     ferrireductase CYB561A3 isoform 1"
                     /EC_number="7.2.1.3"
                     /note="cytochrome b ascorbate-dependent protein 3;
                     lysosomal cytochrome b; lysosomal membrane
                     ascorbate-dependent ferrireductase CYB561A3"
                     /calculated_mol_wt=26955
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     Region          10..188
                     /region_name="Cytochrome_b_N"
                     /note="Cytochrome b (N-terminus)/b6/petB: Cytochrome b is
                     a subunit of cytochrome bc1, an 11-subunit mitochondrial
                     respiratory enzyme. Cytochrome b spans the mitochondrial
                     membrane with 8 transmembrane helices (A-H) in eukaryotes.
                     In plants and cyanobacteria; cl23723"
                     /db_xref="CDD:474033"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     Site            order(47,83,117,156)
                     /site_type="other"
                     /note="putative heme binding sites [chemical binding]"
                     /db_xref="CDD:176489"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     Site            120..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     Site            155..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     Site            203..223
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     CDS             1..242
                     /gene="Cyb561a3"
                     /gene_synonym="2310004G04Rik; Cybasc3; Lcytb"
                     /coded_by="NM_001282067.2:675..1403"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS29582.1"
                     /db_xref="GeneID:225912"
                     /db_xref="MGI:MGI:2686925"
ORIGIN      
        1 masgwfylsc mvlgslgsmc ilftaywmqy wrggfawdgt vlmfnwhpvl mvagmvvlyg
       61 aaslvyrlps swvgprlpwk vlhaalhlla ftctvvglia vfrfhnhsri ahlyslhswl
      121 gittvvlfac qwflgfavfl lpwasqwlrs llkplhvffg acilslsits visgineklf
      181 fvlknatkpy sslpgeavfa nstgllvvaf gllvlyvlla sswkrpdpga ltdrqpllhd
      241 re
//
LOCUS       NP_057289                345 aa            linear   PRI 27-APR-2025
DEFINITION  platelet-derived growth factor C precursor [Homo sapiens].
ACCESSION   NP_057289
VERSION     NP_057289.1
DBSOURCE    REFSEQ: accession NM_016205.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Shi,Y.H., Liu,Z.D., Ma,M.J., Zhao,G.Y., Zhu,Y.Q., Wang,J.Q.,
            Yu,Y.Y., Huang,X.T., Ye,J.Y., Li,F.X., Wang,X.Y., Xu,Q.C. and
            Yin,X.Y.
  TITLE     Platelet-Derived Growth Factor C Facilitates Malignant Behavior of
            Pancreatic Ductal Adenocarcinoma by Regulating SREBP1 Mediated
            Lipid Metabolism
  JOURNAL   Adv Sci (Weinh) 11 (40), e2407069 (2024)
   PUBMED   39225567
  REMARK    GeneRIF: Platelet-Derived Growth Factor C Facilitates Malignant
            Behavior of Pancreatic Ductal Adenocarcinoma by Regulating SREBP1
            Mediated Lipid Metabolism.
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Li,J., Hu,W., Zhang,R., Chen,W., Li,X. and Tang,Z.
  TITLE     PDGF-C promotes cell proliferation partially via downregulating
            BOP1
  JOURNAL   Cell Biol Int 47 (12), 1942-1949 (2023)
   PUBMED   37615370
  REMARK    GeneRIF: PDGF-C promotes cell proliferation partially via
            downregulating BOP1.
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Rodriguez,A.G., Rodriguez,J.Z., Barreto,A., Sanabria-Barrera,S.,
            Iglesias,J. and Morales,L.
  TITLE     Impact of Acute High Glucose on Mitochondrial Function in a Model
            of Endothelial Cells: Role of PDGF-C
  JOURNAL   Int J Mol Sci 24 (5), 4394 (2023)
   PUBMED   36901825
  REMARK    GeneRIF: Impact of Acute High Glucose on Mitochondrial Function in
            a Model of Endothelial Cells: Role of PDGF-C.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Tan,Z., Shi,S., Xu,J., Liu,X., Lei,Y., Zhang,B., Hua,J., Meng,Q.,
            Wang,W., Yu,X. and Liang,C.
  TITLE     RNA N6-methyladenosine demethylase FTO promotes pancreatic cancer
            progression by inducing the autocrine activity of PDGFC in an
            m6A-YTHDF2-dependent manner
  JOURNAL   Oncogene 41 (20), 2860-2872 (2022)
   PUBMED   35422475
  REMARK    GeneRIF: RNA N6-methyladenosine demethylase FTO promotes pancreatic
            cancer progression by inducing the autocrine activity of PDGFC in
            an m(6)A-YTHDF2-dependent manner.
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Gilbertson,D.G., Duff,M.E., West,J.W., Kelly,J.D., Sheppard,P.O.,
            Hofstrand,P.D., Gao,Z., Shoemaker,K., Bukowski,T.R., Moore,M.,
            Feldhaus,A.L., Humes,J.M., Palmer,T.E. and Hart,C.E.
  TITLE     Platelet-derived growth factor C (PDGF-C), a novel growth factor
            that binds to PDGF alpha and beta receptor
  JOURNAL   J Biol Chem 276 (29), 27406-27414 (2001)
   PUBMED   11297552
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Zwerner,J.P. and May,W.A.
  TITLE     PDGF-C is an EWS/FLI induced transforming growth factor in Ewing
            family tumors
  JOURNAL   Oncogene 20 (5), 626-633 (2001)
   PUBMED   11313995
  REMARK    GeneRIF: PDGFC was identified as target of EWS/ETS
            transcriptionalderegulation specific to EWS/FLI-1 chimeras in the
            Ewing Family Tumors suggesting that it may be a significant
            mediator of EWS/FLI driven oncogenesis.
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Tsai,Y.J., Lee,R.K., Lin,S.P. and Chen,Y.H.
  TITLE     Identification of a novel platelet-derived growth factor-like gene,
            fallotein, in the human reproductive tract
  JOURNAL   Biochim Biophys Acta 1492 (1), 196-202 (2000)
   PUBMED   11004490
REFERENCE   9  (residues 1 to 345)
  AUTHORS   Hamada,T., Ui-Tei,K. and Miyata,Y.
  TITLE     A novel gene derived from developing spinal cords, SCDGF, is a
            unique member of the PDGF/VEGF family
  JOURNAL   FEBS Lett 475 (2), 97-102 (2000)
   PUBMED   10858496
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Li,X., Ponten,A., Aase,K., Karlsson,L., Abramsson,A., Uutela,M.,
            Backstrom,G., Hellstrom,M., Bostrom,H., Li,H., Soriano,P.,
            Betsholtz,C., Heldin,C.H., Alitalo,K., Ostman,A. and Eriksson,U.
  TITLE     PDGF-C is a new protease-activated ligand for the PDGF
            alpha-receptor
  JOURNAL   Nat Cell Biol 2 (5), 302-309 (2000)
   PUBMED   10806482
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093325.3, AF091434.1,
            AI446155.1 and AC092608.2.
            
            Summary: The protein encoded by this gene is a member of the
            platelet-derived growth factor family. The four members of this
            family are mitogenic factors for cells of mesenchymal origin and
            are characterized by a core motif of eight cysteines. This gene
            product appears to form only homodimers. It differs from the
            platelet-derived growth factor alpha and beta polypeptides in
            having an unusual N-terminal domain, the CUB domain. Alternatively
            spliced transcript variants have been found for this gene.
            [provided by RefSeq, Sep 2010].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the functional protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF091434.1, AY358493.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000502773.6/ ENSP00000422464.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q32.1"
     Protein         1..345
                     /product="platelet-derived growth factor C precursor"
                     /note="secretory growth factor-like protein; spinal
                     cord-derived growth factor; PDGF-C; VEGF-E"
                     /calculated_mol_wt=37598
     sig_peptide     1..14
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1450
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA1.2)"
     Region          49..162
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(55,57,59,87,92,132,157,159,161..162)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA1.2)"
     Site            225..226
                     /site_type="cleavage"
                     /note="Cleavage; propagated from UniProtKB/Swiss-Prot
                     (Q9NRA1.2)"
     Site            231..232
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA1.2)"
     Site            234..235
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA1.2)"
     Region          248..340
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family domain; PDGF is a potent
                     activator for cells of mesenchymal origin; PDGF-A and
                     PDGF-B form AA and BB homodimers and an AB heterodimer;
                     VEGF is a potent mitogen in embryonic and...; cd00135"
                     /db_xref="CDD:238079"
     Site            order(248..251,287,291..294,309..312)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(250,280,287,296,335,337)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(274,286)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     CDS             1..345
                     /gene="PDGFC"
                     /gene_synonym="FALLOTEIN; SCDGF"
                     /coded_by="NM_016205.3:897..1934"
                     /db_xref="CCDS:CCDS3795.1"
                     /db_xref="GeneID:56034"
                     /db_xref="HGNC:HGNC:8801"
                     /db_xref="MIM:608452"
ORIGIN      
        1 mslfgllllt salagqrqgt qaesnlsskf qfssnkeqng vqdpqherii tvstngsihs
       61 prfphtyprn tvlvwrlvav eenvwiqltf derfgledpe ddickydfve veepsdgtil
      121 grwcgsgtvp gkqiskgnqi rirfvsdeyf psepgfcihy nivmpqftea vspsvlppsa
      181 lpldllnnai tafstledli ryleperwql dledlyrptw qllgkafvfg rksrvvdlnl
      241 lteevrlysc tprnfsvsir eelkrtdtif wpgcllvkrc ggncacclhn cnecqcvpsk
      301 vtkkyhevlq lrpktgvrgl hksltdvale hheecdcvcr gstgg
//
LOCUS       NP_001351665              90 aa            linear   ROD 27-APR-2025
DEFINITION  H/ACA ribonucleoprotein complex subunit 2 isoform 2 [Mus musculus].
ACCESSION   NP_001351665
VERSION     NP_001351665.1
DBSOURCE    REFSEQ: accession NM_001364736.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Kappei,D., Butter,F., Benda,C., Scheibe,M., Draskovic,I.,
            Stevense,M., Novo,C.L., Basquin,C., Araki,M., Araki,K.,
            Krastev,D.B., Kittler,R., Jessberger,R., Londono-Vallejo,J.A.,
            Mann,M. and Buchholz,F.
  TITLE     HOT1 is a mammalian direct telomere repeat-binding protein
            contributing to telomerase recruitment
  JOURNAL   EMBO J 32 (12), 1681-1701 (2013)
   PUBMED   23685356
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Egan,E.D. and Collins,K.
  TITLE     Specificity and stoichiometry of subunit interactions in the human
            telomerase holoenzyme assembled in vivo
  JOURNAL   Mol Cell Biol 30 (11), 2775-2786 (2010)
   PUBMED   20351177
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK019134.1, AV472909.1 and CR518445.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV472909.1, SRR11927934.4505306.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849383, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 31.14 cM"
     Protein         1..90
                     /product="H/ACA ribonucleoprotein complex subunit 2
                     isoform 2"
                     /note="nucleolar protein family A, member 2; h/ACA
                     ribonucleoprotein complex subunit 2; snoRNP protein NHP2;
                     H/ACA small nucleolar RNPs; NHP2 ribonucleoprotein
                     homolog"
                     /calculated_mol_wt=10045
     Region          32..>74
                     /region_name="SNU13"
                     /note="U4/U6.U5 small nuclear ribonucleoprotein SNU13;
                     cl42391"
                     /db_xref="CDD:455736"
     CDS             1..90
                     /gene="Nhp2"
                     /gene_synonym="2410130M07Rik; D11Ertd175e; Nola2"
                     /coded_by="NM_001364736.1:46..318"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:52530"
                     /db_xref="MGI:MGI:1098547"
ORIGIN      
        1 mtkvkaapee seaqaegcse ertykellvn lnpiaqplas rrltrklykc ikkavkqkqi
       61 rrgvkevqkf vnkgekgtwv qpqapsvplv
//
LOCUS       NP_000902                372 aa            linear   PRI 27-APR-2025
DEFINITION  delta-type opioid receptor [Homo sapiens].
ACCESSION   NP_000902
VERSION     NP_000902.3
DBSOURCE    REFSEQ: accession NM_000911.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Bigliardi,P.L., Lo,S., Bigliardi,E., Dancik,Y., Leblanc-Noblesse,E.
            and Bigliardi-Qi,M.
  TITLE     Delta opioid receptor expression correlates to skin ageing and
            melanin expression in Asian women
  JOURNAL   Exp Dermatol 33 (6), e15096 (2024)
   PUBMED   38922774
  REMARK    GeneRIF: Delta opioid receptor expression correlates to skin ageing
            and melanin expression in Asian women.
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Ying,Y., Li,X. and Chen,Y.
  TITLE     Hypomethylation of the opioid receptor delta 1 gene combined with
            high opioid receptor delta 1 protein levels indicates increased
            risk of gout
  JOURNAL   J Clin Lab Anal 36 (9), e24634 (2022)
   PUBMED   35908776
  REMARK    GeneRIF: Hypomethylation of the opioid receptor delta 1 gene
            combined with high opioid receptor delta 1 protein levels indicates
            increased risk of gout.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Miyano,K., Yoshida,Y., Hirayama,S., Takahashi,H., Ono,H.,
            Meguro,Y., Manabe,S., Komatsu,A., Nonaka,M., Mizuguchi,T.,
            Fujii,H., Higami,Y., Narita,M. and Uezono,Y.
  TITLE     Oxytocin Is a Positive Allosteric Modulator of kappa-Opioid
            Receptors but Not delta-Opioid Receptors in the G Protein Signaling
            Pathway
  JOURNAL   Cells 10 (10), 2651 (2021)
   PUBMED   34685631
  REMARK    GeneRIF: Oxytocin Is a Positive Allosteric Modulator of
            kappa-Opioid Receptors but Not delta-Opioid Receptors in the G
            Protein Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Wu,B., Hand,W. and Alexov,E.
  TITLE     Opioid Addiction and Opioid Receptor Dimerization: Structural
            Modeling of the OPRD1 and OPRM1 Heterodimer and Its Signaling
            Pathways
  JOURNAL   Int J Mol Sci 22 (19), 10290 (2021)
   PUBMED   34638633
  REMARK    GeneRIF: Opioid Addiction and Opioid Receptor Dimerization:
            Structural Modeling of the OPRD1 and OPRM1 Heterodimer and Its
            Signaling Pathways.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Crist,R.C., Arauco-Shapiro,G., Zhang,A., Reiner,B.C.,
            Berrettini,W.H. and Doyle,G.A.
  TITLE     Differential expression and transcription factor binding associated
            with genotype at a pharmacogenetic variant in OPRD1
  JOURNAL   Am J Drug Alcohol Abuse 47 (5), 581-589 (2021)
   PUBMED   34407719
  REMARK    GeneRIF: Differential expression and transcription factor binding
            associated with genotype at a pharmacogenetic variant in OPRD1.
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Simonin,F., Befort,K., Gaveriaux-Ruff,C., Matthes,H., Nappey,V.,
            Lannes,B., Micheletti,G. and Kieffer,B.
  TITLE     The human delta-opioid receptor: genomic organization, cDNA
            cloning, functional expression, and distribution in human brain
  JOURNAL   Mol Pharmacol 46 (6), 1015-1021 (1994)
   PUBMED   7808419
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Befort,K., Mattei,M.G., Roeckel,N. and Kieffer,B.
  TITLE     Chromosomal localization of the delta opioid receptor gene to human
            1p34.3-p36.1 and mouse 4D bands by in situ hybridization
  JOURNAL   Genomics 20 (1), 143-145 (1994)
   PUBMED   8020949
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Evans,C.J., Keith,D.E. Jr., Morrison,H., Magendzo,K. and
            Edwards,R.H.
  TITLE     Cloning of a delta opioid receptor by functional expression
  JOURNAL   Science 258 (5090), 1952-1955 (1992)
   PUBMED   1335167
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Offermanns,S., Schultz,G. and Rosenthal,W.
  TITLE     Evidence for opioid receptor-mediated activation of the G-proteins,
            Go and Gi2, in membranes of neuroblastoma x glioma (NG108-15)
            hybrid cells
  JOURNAL   J Biol Chem 266 (6), 3365-3368 (1991)
   PUBMED   1671672
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Itoh,H., Toyama,R., Kozasa,T., Tsukamoto,T., Matsuoka,M. and
            Kaziro,Y.
  TITLE     Presence of three distinct molecular species of Gi protein alpha
            subunit. Structure of rat cDNAs and human genomic DNAs
  JOURNAL   J Biol Chem 263 (14), 6656-6664 (1988)
   PUBMED   2834384
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF434068.1, U10504.1 and AL009181.1.
            
            On May 12, 2005 this sequence version replaced NP_000902.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U07882.2, U10504.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000234961.7/ ENSP00000234961.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..372
                     /product="delta-type opioid receptor"
                     /note="delta opioid receptor 1; DOR-1; D-OR-1"
                     /calculated_mol_wt=40238
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P41143.4)"
     Site            33
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P41143.4)"
     Site            48..75
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P41143.4)"
     Region          50..329
                     /region_name="7tmA_Delta_opioid_R"
                     /note="opioid receptor subtype delta, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15089"
                     /db_xref="CDD:320217"
     Region          51..77
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320217"
     Region          84..110
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320217"
     Site            86..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P41143.4)"
     Site            order(105,108..109,121..126,128..129,132,177,179..183,
                     199..200,210,213..215,217..219,221..222,274,277..278,
                     280..281,284,296..297,299..301,304,307..308)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320217"
     Region          121..151
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320217"
     Site            123..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P41143.4)"
     Region          163..185
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320217"
     Site            164..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P41143.4)"
     Site            207..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P41143.4)"
     Region          209..239
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320217"
     Region          258..284
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320217"
     Site            262..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P41143.4)"
     Region          297..322
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320217"
     Site            300..321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P41143.4)"
     Region          340..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41143.4)"
     CDS             1..372
                     /gene="OPRD1"
                     /gene_synonym="DOP; DOR; DOR1; OPRD"
                     /coded_by="NM_000911.4:215..1333"
                     /db_xref="CCDS:CCDS329.1"
                     /db_xref="GeneID:4985"
                     /db_xref="HGNC:HGNC:8153"
                     /db_xref="MIM:165195"
ORIGIN      
        1 mepapsagae lqpplfanas daypsacpsa ganasgppga rsasslalai aitalysavc
       61 avgllgnvlv mfgivrytkm ktatniyifn laladalats tlpfqsakyl metwpfgell
      121 ckavlsidyy nmftsiftlt mmsvdryiav chpvkaldfr tpakaklini ciwvlasgvg
      181 vpimvmavtr prdgavvcml qfpspswywd tvtkicvflf afvvpiliit vcyglmllrl
      241 rsvrllsgsk ekdrslrrit rmvlvvvgaf vvcwapihif vivwtlvdid rrdplvvaal
      301 hlcialgyan sslnpvlyaf ldenfkrcfr qlcrkpcgrp dpssfsrare atarervtac
      361 tpsdgpggga aa
//
LOCUS       NP_001123230             487 aa            linear   PRI 27-APR-2025
DEFINITION  dipeptidase 3 isoform b precursor [Homo sapiens].
ACCESSION   NP_001123230
VERSION     NP_001123230.2
DBSOURCE    REFSEQ: accession NM_001129758.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Hayashi,K., Longenecker,K.L., Koenig,P., Prashar,A., Hampl,J.,
            Stoll,V. and Vivona,S.
  TITLE     Structure of human DPEP3 in complex with the SC-003 antibody Fab
            fragment reveals basis for lack of dipeptidase activity
  JOURNAL   J Struct Biol 211 (1), 107512 (2020)
   PUBMED   32325220
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Schiza,C., Korbakis,D., Panteleli,E., Jarvi,K., Drabovich,A.P. and
            Diamandis,E.P.
  TITLE     Discovery of a Human Testis-specific Protein Complex TEX101-DPEP3
            and Selection of Its Disrupting Antibodies
  JOURNAL   Mol Cell Proteomics 17 (12), 2480-2495 (2018)
   PUBMED   30097533
REFERENCE   3  (residues 1 to 487)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Sabatti,C., Service,S.K., Hartikainen,A.L., Pouta,A., Ripatti,S.,
            Brodsky,J., Jones,C.G., Zaitlen,N.A., Varilo,T., Kaakinen,M.,
            Sovio,U., Ruokonen,A., Laitinen,J., Jakkula,E., Coin,L.,
            Hoggart,C., Collins,A., Turunen,H., Gabriel,S., Elliot,P.,
            McCarthy,M.I., Daly,M.J., Jarvelin,M.R., Freimer,N.B. and
            Peltonen,L.
  TITLE     Genome-wide association analysis of metabolic traits in a birth
            cohort from a founder population
  JOURNAL   Nat Genet 41 (1), 35-46 (2009)
   PUBMED   19060910
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Habib,G.M., Shi,Z.Z., Cuevas,A.A. and Lieberman,M.W.
  TITLE     Identification of two additional members of the membrane-bound
            dipeptidase family
  JOURNAL   FASEB J 17 (10), 1313-1315 (2003)
   PUBMED   12738806
  REMARK    GeneRIF: This paper describes differences in substrate specificity
            and tissue distribution of membrane-bound dipeptidase 3 from mouse
            in comparison to other mouse members of this family.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HM005556.1.
            
            On May 2, 2019 this sequence version replaced NP_001123230.1.
            
            Summary: This gene encodes a membrane-bound glycoprotein from the
            family of dipeptidases involved in hydrolytic metabolism of various
            dipeptides, including penem and carbapenem beta-lactam antibiotics.
            This gene is located on chromosome 16 in a cluster with another
            member of this family. Alternatively spliced transcript variants
            that encode different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the mid-coding region, compared to variant 1,
            resulting in an isoform (b) that is 1 aa shorter, compared to
            isoform a.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..487
                     /product="dipeptidase 3 isoform b precursor"
                     /EC_number="3.4.13.19"
                     /note="membrane-bound dipeptidase 3; metallopeptidase
                     (family M19); testis secretory sperm-binding protein Li
                     211a"
                     /calculated_mol_wt=49346
     sig_peptide     1..36
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4231
     Region          87..406
                     /region_name="Peptidase_M19"
                     /note="Membrane dipeptidase (Peptidase family M19);
                     pfam01244"
                     /db_xref="CDD:395996"
     Site            order(97,99,143,196,269,290,301,358,361)
                     /site_type="active"
                     /db_xref="CDD:238626"
     Site            order(145,154..156,158..159,162,166,206..207,209..210,
                     213..214)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238626"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H4B8.2)"
     CDS             1..487
                     /gene="DPEP3"
                     /gene_synonym="MBD3"
                     /coded_by="NM_001129758.2:120..1583"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:64180"
                     /db_xref="HGNC:HGNC:23029"
                     /db_xref="MIM:609926"
ORIGIN      
        1 mqptgregsr alsrrylrrl lllllllllr qpvtraettp gapralstlg spslfttpgv
       61 psalttpglt tpgtpktldl rgraqalmrs fplvdghndl pqvlrqrykn vlqdvnlrnf
      121 shgqtsldrl rdglvgaqfw sasvscqsqd qtavrlaleq idlihrmcas yselelvtsa
      181 eglnssqkla cligvegghs ldsslsvlrs fyvlgvrylt ltftcstpwa esstkfrhhm
      241 ytnvsgltsf gekvveelnr lgmmidlsya sdtlirrvle vsqapvifsh saaravcdnl
      301 lnvpddilql lknggivmvt lsmgvlqcnl lanvstvadh fdhiravigs efigiggnyd
      361 gtgrfpqgle dvstypvlie ellsrswsee elqgvlrgnl lrvfrqvekv reesraqspv
      421 eaefpygqls tschshlvpq nghqathlev tkqptnrvpw rssnaspylv pglvaaatip
      481 tftqwlc
//
LOCUS       NP_006102                397 aa            linear   PRI 27-APR-2025
DEFINITION  3-ketoacyl-CoA thiolase, mitochondrial [Homo sapiens].
ACCESSION   NP_006102
VERSION     NP_006102.2
DBSOURCE    REFSEQ: accession NM_006111.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Leng,Y., Tian,T., Tang,B., Ma,Y., Li,Z., Shi,Q., Liu,J., Zhou,Y.,
            Wang,W., Huang,C., Zhao,X., Feng,W., Liu,Y., Liang,J., Liu,T.,
            Liu,S., Ren,Q., Liu,J., Zhang,T., Zhou,J., Huang,Q., Zhang,Y.,
            Yin,B., Xu,Y., Liu,L., Shen,L. and Zhao,H.
  TITLE     The oncogenic role and regulatory mechanism of ACAA2 in human
            ovarian cancer
  JOURNAL   Mol Carcinog 63 (7), 1362-1377 (2024)
   PUBMED   38656551
  REMARK    GeneRIF: The oncogenic role and regulatory mechanism of ACAA2 in
            human ovarian cancer.
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Shen,M., Liu,S., Toland,A., Hsu,E.C., Hartono,A.B., Alabi,B.R.,
            Aslan,M., Nguyen,H.M., Sessions,C.J., Nolley,R., Shi,C., Huang,J.,
            Brooks,J.D., Corey,E. and Stoyanova,T.
  TITLE     ACAA2 is a novel molecular indicator for cancers with
            neuroendocrine phenotype
  JOURNAL   Br J Cancer 129 (11), 1818-1828 (2023)
   PUBMED   37798372
  REMARK    GeneRIF: ACAA2 is a novel molecular indicator for cancers with
            neuroendocrine phenotype.
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yuan,Y., Sun,X., Liu,M., Li,S., Dong,Y., Hu,K., Zhang,J., Xu,B.,
            Ma,S., Jiang,H., Hou,P., Lin,Y., Gan,L. and Liu,T.
  TITLE     Negative correlation between acetyl-CoA acyltransferase 2 and
            cetuximab resistance in colorectal cancer
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (9), 1467-1478 (2023)
   PUBMED   37310146
  REMARK    GeneRIF: Negative correlation between acetyl-CoA acyltransferase 2
            and cetuximab resistance in colorectal cancer.
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Zhang,H., Pan,E., Zhang,Y., Zhao,C., Liu,Q., Pu,Y. and Yin,L.
  TITLE     LncRNA RPL34-AS1 suppresses the proliferation, migration and
            invasion of esophageal squamous cell carcinoma via targeting
            miR-575/ACAA2 axis
  JOURNAL   BMC Cancer 22 (1), 1017 (2022)
   PUBMED   36162992
  REMARK    GeneRIF: LncRNA RPL34-AS1 suppresses the proliferation, migration
            and invasion of esophageal squamous cell carcinoma via targeting
            miR-575/ACAA2 axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Cao,W., Liu,N., Tang,S., Bao,L., Shen,L., Yuan,H., Zhao,X. and
            Lu,H.
  TITLE     Acetyl-Coenzyme A acyltransferase 2 attenuates the apoptotic
            effects of BNIP3 in two human cell lines
  JOURNAL   Biochim Biophys Acta 1780 (6), 873-880 (2008)
   PUBMED   18371312
  REMARK    GeneRIF: ACAA2 is a functional BNIP3 binding partner and provide a
            possible linkage between fatty acid metabolism and apoptosis of
            cells.
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Kathiresan,S., Melander,O., Guiducci,C., Surti,A., Burtt,N.P.,
            Rieder,M.J., Cooper,G.M., Roos,C., Voight,B.F., Havulinna,A.S.,
            Wahlstrand,B., Hedner,T., Corella,D., Tai,E.S., Ordovas,J.M.,
            Berglund,G., Vartiainen,E., Jousilahti,P., Hedblad,B.,
            Taskinen,M.R., Newton-Cheh,C., Salomaa,V., Peltonen,L., Groop,L.,
            Altshuler,D.M. and Orho-Melander,M.
  TITLE     Six new loci associated with blood low-density lipoprotein
            cholesterol, high-density lipoprotein cholesterol or triglycerides
            in humans
  JOURNAL   Nat Genet 40 (2), 189-197 (2008)
   PUBMED   18193044
  REMARK    Erratum:[Nat Genet. 2008 Nov;40(11):1384]
REFERENCE   8  (residues 1 to 397)
  AUTHORS   Aboulaich,N., Vainonen,J.P., Stralfors,P. and Vener,A.V.
  TITLE     Vectorial proteomics reveal targeting, phosphorylation and specific
            fragmentation of polymerase I and transcript release factor (PTRF)
            at the surface of caveolae in human adipocytes
  JOURNAL   Biochem J 383 (Pt 2), 237-248 (2004)
   PUBMED   15242332
REFERENCE   9  (residues 1 to 397)
  AUTHORS   Seedorf,U., Ellinghaus,P. and Roch Nofer,J.
  TITLE     Sterol carrier protein-2
  JOURNAL   Biochim Biophys Acta 1486 (1), 45-54 (2000)
   PUBMED   10856712
  REMARK    Review article
REFERENCE   10 (residues 1 to 397)
  AUTHORS   Abe,H., Ohtake,A., Yamamoto,S., Satoh,Y., Takayanagi,M., Amaya,Y.,
            Takiguchi,M., Sakuraba,H., Suzuki,Y., Mori,M. et al.
  TITLE     Cloning and sequence analysis of a full length cDNA encoding human
            mitochondrial 3-oxoacyl-CoA thiolase
  JOURNAL   Biochim Biophys Acta 1216 (2), 304-306 (1993)
   PUBMED   8241273
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK054673.1, BC001918.1 and
            AC090227.10.
            
            On Feb 11, 2008 this sequence version replaced NP_006102.1.
            
            Summary: The encoded protein catalyzes the last step of the
            mitochondrial fatty acid beta-oxidation spiral. Unlike most
            mitochondrial matrix proteins, it contains a non-cleavable
            amino-terminal targeting signal. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.260875.1,
                                           SRR1803612.226072.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000285093.15/
                                                  ENSP00000285093.8
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..397
                     /product="3-ketoacyl-CoA thiolase, mitochondrial"
                     /EC_number="2.3.1.9"
                     /EC_number="2.3.1.16"
                     /EC_number="3.1.2.2"
                     /EC_number="3.1.2.1"
                     /note="mitochondrial 3-oxoacyl-CoA thiolase; beta
                     ketothiolase; mitochondrial 3-oxoacyl-Coenzyme A thiolase;
                     acetyl-Coenzyme A acyltransferase 2; acetyl-CoA
                     acetyltransferase; acyl-CoA hydrolase, mitochondrial"
                     /calculated_mol_wt=40213
     transit_peptide 1..16
                     /note="Mitochondrion, not cleaved; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
                     /calculated_mol_wt=1729
     Region          8..394
                     /region_name="thiolase"
                     /note="Thiolase are ubiquitous enzymes that catalyze the
                     reversible thiolytic cleavage of 3-ketoacyl-CoA into
                     acyl-CoA and acetyl-CoA, a 2-step reaction involving a
                     covalent intermediate formed with a catalytic cysteine.
                     They are found in prokaryotes and...; cd00751"
                     /db_xref="CDD:238383"
     Site            25
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            order(26,53,68,71,75,86..89,97,104..105,108,123,282,284,
                     286,306,385..386)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238383"
     Site            order(92,352,382)
                     /site_type="active"
                     /db_xref="CDD:238383"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            143
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            191
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            209
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            234
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            269
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            270
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            305
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            312
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            340
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            352
                     /site_type="other"
                     /note="Increases nucleophilicity of active site Cys.
                     /evidence=ECO:0000305|PubMed:25478839; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     Site            375
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT1; propagated from
                     UniProtKB/Swiss-Prot (P42765.2)"
     CDS             1..397
                     /gene="ACAA2"
                     /gene_synonym="DSAEC; T1"
                     /coded_by="NM_006111.3:50..1243"
                     /db_xref="CCDS:CCDS11939.1"
                     /db_xref="GeneID:10449"
                     /db_xref="HGNC:HGNC:83"
                     /db_xref="MIM:604770"
ORIGIN      
        1 mallrgvfvv aakrtpfgay ggllkdftat dlsefaakaa lsagkvspet vdsvimgnvl
       61 qsssdaiyla rhvglrvgip ketpaltinr lcgsgfqsiv ngcqeicvke aevvlcggte
      121 smsqapycvr nvrfgtklgs dikledslwv sltdqhvqlp mamtaenlav khkisreecd
      181 kyalqsqqrw kaandagyfn demapievkt kkgkqtmqvd eharpqttle qlqklppvfk
      241 kdgtvtagna sgvadgagav iiasedavkk hnftplariv gyfvsgcdps imgigpvpai
      301 sgalkkagls lkdmdlvevn eafapqylav ersldldisk tnvnggaial ghplggsgsr
      361 itahlvhelr rrggkyavgs acigggqgia viiqsta
//
LOCUS       NP_055267                655 aa            linear   PRI 27-APR-2025
DEFINITION  tumor necrosis factor receptor superfamily member 21 precursor
            [Homo sapiens].
ACCESSION   NP_055267 NP_057713
VERSION     NP_055267.1
DBSOURCE    REFSEQ: accession NM_014452.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Clay,S., Alladina,J., Smith,N.P., Visness,C.M., Wood,R.A.,
            O'Connor,G.T., Cohen,R.T., Khurana Hershey,G.K., Kercsmar,C.M.,
            Gruchalla,R.S., Gill,M.A., Liu,A.H., Kim,H., Kattan,M.,
            Bacharier,L.B., Rastogi,D., Rivera-Spoljaric,K., Robison,R.G.,
            Gergen,P.J., Busse,W.W., Villani,A.C., Cho,J.L., Medoff,B.D.,
            Gern,J.E., Jackson,D.J., Ober,C. and Dapas,M.
  TITLE     Gene-based association study of rare variants in children of
            diverse ancestries implicates TNFRSF21 in the development of
            allergic asthma
  JOURNAL   J Allergy Clin Immunol 153 (3), 809-820 (2024)
   PUBMED   37944567
  REMARK    GeneRIF: Gene-based association study of rare variants in children
            of diverse ancestries implicates TNFRSF21 in the development of
            allergic asthma.
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Cheng,J., Tang,Y., Cai,X. and Gong,J.
  TITLE     Long Noncoding RNAs Testis Development Related Gene 1 Aggravates
            Transforming Growth Factor-beta1-Induced Fibrogenesis and
            Inflammatory Response of Cardiac Fibroblasts Via miR-605-3p/Tumor
            Necrosis Factor Receptor Superfamily-21 Axis
  JOURNAL   J Cardiovasc Pharmacol 79 (3), 296-303 (2022)
   PUBMED   34775426
  REMARK    GeneRIF: Long Noncoding RNAs Testis Development Related Gene 1
            Aggravates Transforming Growth Factor-beta1-Induced Fibrogenesis
            and Inflammatory Response of Cardiac Fibroblasts Via
            miR-605-3p/Tumor Necrosis Factor Receptor Superfamily-21 Axis.
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Stegmann,S.K., Kuhl,S., Im,N.G., Diem-Dinh,D.T., Goertz,L.,
            Goldbrunner,R. and Timmer,M.
  TITLE     Death Receptor 6 as a Prognostic Marker in Low-grade Glioma
  JOURNAL   Anticancer Res 42 (3), 1237-1245 (2022)
   PUBMED   35220214
  REMARK    GeneRIF: Death Receptor 6 as a Prognostic Marker in Low-grade
            Glioma.
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Liu,Y., Chang,Y. and Cai,Y.
  TITLE     circTNFRSF21, a newly identified circular RNA promotes endometrial
            carcinoma pathogenesis through regulating miR-1227-MAPK13/ATF2 axis
  JOURNAL   Aging (Albany NY) 12 (8), 6774-6792 (2020)
   PUBMED   32299063
  REMARK    GeneRIF: circTNFRSF21, a newly identified circular RNA promotes
            endometrial carcinoma pathogenesis through regulating
            miR-1227-MAPK13/ATF2 axis.
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Cho,S.M., Kim,J., Ryu,H.J., Kim,J.J., Kim,H.H., Park,J.H.,
            Kim,H.T., Kim,K.H., Cho,H.Y., Oh,B., Park,C., Kimm,K., Jo,I.,
            Lee,J.E., Shin,H.D. and Lee,J.K.
  TITLE     Identification of single nucleotide polymorphisms in the tumor
            necrosis factor (TNF) and TNF receptor superfamily in the Korean
            population
  JOURNAL   Hum Immunol 65 (7), 710-718 (2004)
   PUBMED   15301860
  REMARK    GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Kasof,G.M., Lu,J.J., Liu,D., Speer,B., Mongan,K.N., Gomes,B.C. and
            Lorenzi,M.V.
  TITLE     Tumor necrosis factor-alpha induces the expression of DR6, a member
            of the TNF receptor family, through activation of NF-kappaB
  JOURNAL   Oncogene 20 (55), 7965-7975 (2001)
   PUBMED   11753679
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Zhao,H., Yan,M., Wang,H., Erickson,S., Grewal,I.S. and Dixit,V.M.
  TITLE     Impaired c-Jun amino terminal kinase activity and T cell
            differentiation in death receptor 6-deficient mice
  JOURNAL   J Exp Med 194 (10), 1441-1448 (2001)
   PUBMED   11714751
  REMARK    GeneRIF: DR6 knockout mice are viable and fertile, and show
            hyperproliferation of T cells when stimulated.
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Liu,J., Na,S., Glasebrook,A., Fox,N., Solenberg,P.J., Zhang,Q.,
            Song,H.Y. and Yang,D.D.
  TITLE     Enhanced CD4+ T cell proliferation and Th2 cytokine production in
            DR6-deficient mice
  JOURNAL   Immunity 15 (1), 23-34 (2001)
   PUBMED   11485735
  REMARK    GeneRIF: DR6 mediates T cell proliferation and differentiation in
            mice.
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Pan,G., Bauer,J.H., Haridas,V., Wang,S., Liu,D., Yu,G., Vincenz,C.,
            Aggarwal,B.B., Ni,J. and Dixit,V.M.
  TITLE     Identification and functional characterization of DR6, a novel
            death domain-containing TNF receptor
  JOURNAL   FEBS Lett 431 (3), 351-356 (1998)
   PUBMED   9714541
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY007775.1 and AY358304.1.
            
            On Nov 4, 2002 this sequence version replaced NP_057713.1.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The encoded protein activates nuclear factor
            kappa-B and mitogen-activated protein kinase 8 (also called c-Jun
            N-terminal kinase 1), and induces cell apoptosis. Through its death
            domain, the encoded receptor interacts with tumor necrosis factor
            receptor type 1-associated death domain (TRADD) protein, which is
            known to mediate signal transduction of tumor necrosis factor
            receptors. Knockout studies in mice suggest that this gene plays a
            role in T-helper cell activation, and may be involved in
            inflammation and immune regulation. [provided by RefSeq, Jul 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.910204.1,
                                           SRR1803617.15433.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296861.2/ ENSP00000296861.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.3"
     Protein         1..655
                     /product="tumor necrosis factor receptor superfamily
                     member 21 precursor"
                     /note="death receptor 6; TNFR-related death receptor 6;
                     tumor necrosis factor receptor superfamily member 21"
                     /calculated_mol_wt=67789
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4075
     mat_peptide     42..655
                     /product="Tumor necrosis factor receptor superfamily
                     member 21. /id=PRO_0000034602"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
                     /calculated_mol_wt=67789
     Region          50..88
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Region          53..211
                     /region_name="TNFRSF21"
                     /note="Tumor necrosis factor receptor superfamily member
                     21 (TNFRSF21), also known as death receptor (DR6);
                     cd10583"
                     /db_xref="CDD:276909"
     Region          67..88
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276909"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Region          90..131
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Region          91..131
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276909"
     Region          133..186
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276909"
     Region          133..167
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Region          170..211
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Region          243..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Site            252
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Region          318..337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Site            350..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Region          414..497
                     /region_name="Death_TNFRSF21"
                     /note="Death domain of tumor necrosis factor receptor
                     superfamily member 21; cd08778"
                     /db_xref="CDD:176756"
     CDS             1..655
                     /gene="TNFRSF21"
                     /gene_synonym="BM-018; CD358; DR6"
                     /coded_by="NM_014452.5:395..2362"
                     /db_xref="CCDS:CCDS4921.1"
                     /db_xref="GeneID:27242"
                     /db_xref="HGNC:HGNC:13469"
                     /db_xref="MIM:605732"
ORIGIN      
        1 mgtspsssta lascsriarr atatmiagsl lllgflsttt aqpeqkasnl igtyrhvdra
       61 tgqvltcdkc pagtyvsehc tntslrvcss cpvgtftrhe ngiekchdcs qpcpwpmiek
      121 lpcaaltdre ctcppgmfqs natcaphtvc pvgwgvrkkg tetedvrckq cargtfsdvp
      181 ssvmkckayt dclsqnlvvi kpgtketdnv cgtlpsfsss tspspgtaif prpehmethe
      241 vpsstyvpkg mnstesnssa svrpkvlssi qegtvpdnts sargkedvnk tlpnlqvvnh
      301 qqgphhrhil kllpsmeatg geksstpikg pkrghprqnl hkhfdinehl pwmivlflll
      361 vlvvivvcsi rkssrtlkkg prqdpsaive kaglkksmtp tqnrekwiyy cnghgidilk
      421 lvaaqvgsqw kdiyqflcna serevaafsn gytadheray aalqhwtirg peaslaqlis
      481 alrqhrrndv vekirglmed ttqletdkla lpmspsplsp spipspnakl ensalltvep
      541 spqdknkgff vdesepllrc dstssgssal srngsfitke kkdtvlrqvr ldpcdlqpif
      601 ddmlhflnpe elrvieeipq aedkldrlfe iigvksqeas qtlldsvysh lpdll
//
LOCUS       NP_002228                513 aa            linear   PRI 27-APR-2025
DEFINITION  voltage-gated potassium channel regulatory subunit KCNG1 [Homo
            sapiens].
ACCESSION   NP_002228
VERSION     NP_002228.2
DBSOURCE    REFSEQ: accession NM_002237.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Kuhnisch,J., Thiering,E., Heitmuller,D., Tiesler,C.M., Grallert,H.,
            Heinrich-Weltzien,R., Hickel,R. and Heinrich,J.
  CONSRTM   GINI-10 Plus Study Group; LISA-10Plus Study Group
  TITLE     Genome-wide association study (GWAS) for molar-incisor
            hypomineralization (MIH)
  JOURNAL   Clin Oral Investig 18 (2), 677-682 (2014)
   PUBMED   23918034
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Mederos Y Schnitzler,M., Rinne,S., Skrobek,L., Renigunta,V.,
            Schlichthorl,G., Derst,C., Gudermann,T., Daut,J. and
            Preisig-Muller,R.
  TITLE     Mutation of histidine 105 in the T1 domain of the potassium channel
            Kv2.1 disrupts heteromerization with Kv6.3 and Kv6.4
  JOURNAL   J Biol Chem 284 (7), 4695-4704 (2009)
   PUBMED   19074135
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Gutman,G.A., Chandy,K.G., Grissmer,S., Lazdunski,M., McKinnon,D.,
            Pardo,L.A., Robertson,G.A., Rudy,B., Sanguinetti,M.C., Stuhmer,W.
            and Wang,X.
  TITLE     International Union of Pharmacology. LIII. Nomenclature and
            molecular relationships of voltage-gated potassium channels
  JOURNAL   Pharmacol Rev 57 (4), 473-508 (2005)
   PUBMED   16382104
  REMARK    Review article
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Su,K., Kyaw,H., Fan,P., Zeng,Z., Shell,B.K., Carter,K.C. and Li,Y.
  TITLE     Isolation, characterization, and mapping of two human potassium
            channels
  JOURNAL   Biochem Biophys Res Commun 241 (3), 675-681 (1997)
   PUBMED   9434767
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Post,M.A., Kirsch,G.E. and Brown,A.M.
  TITLE     Kv2.1 and electrically silent Kv6.1 potassium channel subunits
            combine and express a novel current
  JOURNAL   FEBS Lett 399 (1-2), 177-182 (1996)
   PUBMED   8980147
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA684016.1, CN301212.1,
            BC046629.2, AF033383.1, BG029104.1 and CN480356.1.
            
            On Dec 31, 2002 this sequence version replaced NP_002228.1.
            
            Summary: Voltage-gated potassium (Kv) channels represent the most
            complex class of voltage-gated ion channels from both functional
            and structural standpoints. Their diverse functions include
            regulating neurotransmitter release, heart rate, insulin secretion,
            neuronal excitability, epithelial electrolyte transport, smooth
            muscle contraction, and cell volume. This gene encodes a member of
            the potassium channel, voltage-gated, subfamily G. This gene is
            abundantly expressed in skeletal muscle. Multiple alternatively
            spliced transcript variants have been found in normal and cancerous
            tissues. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC046629.2, SRR3476690.990094.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371571.5/ ENSP00000360626.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.13"
     Protein         1..513
                     /product="voltage-gated potassium channel regulatory
                     subunit KCNG1"
                     /note="potassium channel KH2; potassium channel Kv6.1;
                     potassium channel, voltage gated modifier subfamily G,
                     member 1; voltage-gated potassium channel subunit Kv6.1;
                     potassium voltage-gated channel, subfamily G, member 1"
                     /calculated_mol_wt=57782
     Region          60..173
                     /region_name="BTB_POZ_KCNG1_2"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     voltage-gated channel subfamily G members, KCNG1 and
                     KCNG2; cd18421"
                     /db_xref="CDD:349728"
     Site            order(68,70..77,80,116,118..119,122,125,129,132,135,137,
                     145..146,149)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349728"
     Region          184..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIX4.1)"
     Site            225..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIX4.1)"
     Region          227..471
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            268..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIX4.1)"
     Site            301..321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIX4.1)"
     Site            339..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIX4.1)"
     Site            375..396
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIX4.1)"
     Region          424..429
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIX4.1)"
     Site            439..467
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIX4.1)"
     CDS             1..513
                     /gene="KCNG1"
                     /gene_synonym="K13; KCNG; kH2; KV6.1"
                     /coded_by="NM_002237.4:265..1806"
                     /db_xref="CCDS:CCDS13436.1"
                     /db_xref="GeneID:3755"
                     /db_xref="HGNC:HGNC:6248"
                     /db_xref="MIM:603788"
ORIGIN      
        1 mtllpgdnsd ydysalscts dasfhpaflp qrqaikgafy rraqrlrpqd eprqgcqped
       61 rrrriiinvg gikyslpwtt ldefpltrlg qlkactnfdd ilnvcddydv tcnefffdrn
      121 pgafgtiltf lragklrllr emcalsfqee llywgiaedh ldgcckrryl qkieefaemv
      181 ereeeddald segrdsegpa egegrlgrcm rrlrdmverp hsglpgkvfa clsvlfvtvt
      241 avnlsvstlp slreeeeqgh csqmchnvfi vesvcvgwfs lefllrliqa pskfaflrsp
      301 ltlidlvail pyyitllvdg aaagrrkpga gnsyldkvgl vlrvlralri lyvmrlarhs
      361 lglqtlglta rrctrefgll llflcvaial fapllyvien emadspefts ipacywwavi
      421 tmttvgygdm vprstpgqvv alssilsgil lmafpvtsif htfsrsylel kqeqervmfr
      481 raqfliktks qlsvsqdsdi lfgsassdtr dnn
//
LOCUS       NP_008824                584 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 2D isoform 1 [Homo
            sapiens].
ACCESSION   NP_008824
VERSION     NP_008824.2
DBSOURCE    REFSEQ: accession NM_006893.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Grove,D.J., Russell,P.J. and Kearse,M.G.
  TITLE     To initiate or not to initiate: A critical assessment of eIF2A,
            eIF2D, and MCT-1.DENR to deliver initiator tRNA to ribosomes
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1833 (2024)
   PUBMED   38433101
  REMARK    GeneRIF: To initiate or not to initiate: A critical assessment of
            eIF2A, eIF2D, and MCT-1.DENR to deliver initiator tRNA to
            ribosomes.
            Review article
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Kim,H., Aponte-Diaz,D., Sotoudegan,M.S., Shengjuler,D., Arnold,J.J.
            and Cameron,C.E.
  TITLE     The enterovirus genome can be translated in an IRES-independent
            manner that requires the initiation factors eIF2A/eIF2D
  JOURNAL   PLoS Biol 21 (1), e3001693 (2023)
   PUBMED   36689548
  REMARK    GeneRIF: The enterovirus genome can be translated in an
            IRES-independent manner that requires the initiation factors
            eIF2A/eIF2D.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Gilabert-Juan,J., Lopez-Campos,G., Sebastia-Ortega,N.,
            Guara-Ciurana,S., Ruso-Julve,F., Prieto,C., Crespo-Facorro,B.,
            Sanjuan,J. and Molto,M.D.
  TITLE     Time dependent expression of the blood biomarkers EIF2D and TOX in
            patients with schizophrenia
  JOURNAL   Brain Behav Immun 80, 909-915 (2019)
   PUBMED   31078689
  REMARK    GeneRIF: We observed a positive correlation trend between EIF2D
            mRNA levels and years of schizophrenia (SZ) disease (p=0.0794;
            r=0.35). We found a trend of an increase in the expression levels
            of EIF2D (p=0.0634) in patients suffering from the disease more
            than 10years compared with the SZ patients from the other subgroup
            .
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Basu,K., Maurya,N., Kaur,J., Saxena,R., Gupta,V., Sihota,R. and
            Ghosh,I.
  TITLE     Possible role of differentially expressing novel protein markers
            (ligatin and fibulin-7) in human aqueous humor and trabecular
            meshwork tissue in glaucoma progression
  JOURNAL   Cell Biol Int 43 (7), 820-834 (2019)
   PUBMED   30958601
  REMARK    GeneRIF: this is the first report which confirms the presence of
            ligatin and fibulin-7 in human aqueous humor, quantified their
            differential expression, and indicated the possibility of their
            involvement in the maintenance of the trabecular meshwork structure
            in glaucoma progression.
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Akulich,K.A., Sinitcyn,P.G., Makeeva,D.S., Andreev,D.E.,
            Terenin,I.M., Anisimova,A.S., Shatsky,I.N. and Dmitriev,S.E.
  TITLE     A novel uORF-based regulatory mechanism controls translation of the
            human MDM2 and eIF2D mRNAs during stress
  JOURNAL   Biochimie 157, 92-101 (2019)
   PUBMED   30419262
  REMARK    GeneRIF: a novel uORF-based regulatory mechanism that is employed
            under conditions of hyperosmotic stress by at least two human
            mRNAs, coding for translation reinitiation/recycling factor eIF2D
            and E3 ubiquitin ligase MDM2. This novel mode of translational
            control selectively downregulates their expression and requires as
            few as one uORF.
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Sanz,M.A., Gonzalez Almela,E. and Carrasco,L.
  TITLE     Translation of Sindbis Subgenomic mRNA is Independent of eIF2,
            eIF2A and eIF2D
  JOURNAL   Sci Rep 7, 43876 (2017)
   PUBMED   28240315
  REMARK    GeneRIF: Data suggest that neither eIF2A nor eIF2D are involved in
            the translation of this Sindbis virus subgenomic mRNA (sgmRNA)
            bearing non-AUG codons
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 584)
  AUTHORS   Dmitriev,S.E., Terenin,I.M., Andreev,D.E., Ivanov,P.A.,
            Dunaevsky,J.E., Merrick,W.C. and Shatsky,I.N.
  TITLE     GTP-independent tRNA delivery to the ribosomal P-site by a novel
            eukaryotic translation factor
  JOURNAL   J Biol Chem 285 (35), 26779-26787 (2010)
   PUBMED   20566627
REFERENCE   8  (residues 1 to 584)
  AUTHORS   Skabkin,M.A., Skabkina,O.V., Dhote,V., Komar,A.A., Hellen,C.U. and
            Pestova,T.V.
  TITLE     Activities of Ligatin and MCT-1/DENR in eukaryotic translation
            initiation and ribosomal recycling
  JOURNAL   Genes Dev 24 (16), 1787-1801 (2010)
   PUBMED   20713520
REFERENCE   9  (residues 1 to 584)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 584)
  AUTHORS   Wang,Y., Han,K.J., Pang,X.W., Vaughan,H.A., Qu,W., Dong,X.Y.,
            Peng,J.R., Zhao,H.T., Rui,J.A., Leng,X.S., Cebon,J., Burgess,A.W.
            and Chen,W.F.
  TITLE     Large scale identification of human hepatocellular
            carcinoma-associated antigens by autoantibodies
  JOURNAL   J Immunol 169 (2), 1102-1109 (2002)
   PUBMED   12097419
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI465059.1 and BC058905.1.
            
            On Dec 17, 2004 this sequence version replaced NP_008824.1.
            
            Summary: This gene encodes a translation initiation factor involved
            in the recruitment and delivery of aminoacyl-tRNAs to the P-site of
            the eukaryotic ribosome in a GTP-independent manner. This gene was
            previously referred to as ligatin, but is now known to localize to
            the cytoplasm and localize and function with translation factors.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.205242.1, AK001852.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000271764.7/ ENSP00000271764.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..584
                     /product="eukaryotic translation initiation factor 2D
                     isoform 1"
                     /note="ligatin; hepatocellular carcinoma-associated
                     antigen 56"
                     /calculated_mol_wt=64576
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P41214.3)"
     Region          6..81
                     /region_name="eIF2D_N"
                     /note="N-terminal domain of eIF2D and related proteins;
                     cd11610"
                     /db_xref="CDD:211423"
     Site            order(29..30,73,75,78..81)
                     /site_type="other"
                     /note="PUA domain interface [polypeptide binding]"
                     /db_xref="CDD:211423"
     Region          92..173
                     /region_name="PUA_eIF2d-like"
                     /note="PUA RNA-binding domain of eukaryotic translation
                     initiation factor 2D and similar proteins; cd21156"
                     /db_xref="CDD:409298"
     Region          93..173
                     /region_name="PUA domain"
     Site            order(101..102,105,110..111,113)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409298"
     Region          223..257
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41214.3)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P41214.3)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61211; propagated from
                     UniProtKB/Swiss-Prot (P41214.3)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P41214.3)"
     Region          490..574
                     /region_name="eIF2D_C"
                     /note="C-terminal domain of eIF2D and related proteins;
                     cd11608"
                     /db_xref="CDD:211321"
     Region          491..564
                     /region_name="SUI1 domain"
     Site            order(498,501..502,504,522,525..527,529..531,533,549,552)
                     /site_type="other"
                     /note="putative rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:211321"
     CDS             1..584
                     /gene="EIF2D"
                     /gene_synonym="HCA56; LGTN"
                     /coded_by="NM_006893.3:124..1878"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1465.1"
                     /db_xref="GeneID:1939"
                     /db_xref="HGNC:HGNC:6583"
                     /db_xref="MIM:613709"
ORIGIN      
        1 mfakafrvks ntaikgsdrr klradvttaf ptlgtdqvse lvpgkeelni vklyahkgda
       61 vtvyvsggnp ilfeleknly ptvytlwsyp dllptfttwp lvleklvgga dlmlpglvmp
      121 paglpqvqkg dlcaislvgn rapvaigvaa mstaemltsg lkgrgfsvlh tyqdhlwrsg
      181 nkssppsiap laldsadlse ekgsvqmdst lqgdmrhmtl egeeengevh qaredkslse
      241 apedtstrgl nqdstdsktl qeqmdellqq cflhalkcrv kkadlpllts tflgshmfsc
      301 cpegrqldik kssykklskf lqqmqqeqii qvkelskgve sivavdwkhp ritsfvipep
      361 sptsqtiqeg sreqpyhppd ikplycvpas mtllfqesgh kkgsflegse vrtivinyak
      421 kndlvdadnk nlvrldpilc dcilekneqh tvmklpwdsl ltrcleklqp ayqvtlpgqe
      481 pivkkgricp iditlaqras nkkvtvvrnl eaygldpysv aailqqrcqa sttvnpapga
      541 kdslqvqiqg nqvhhlgwll leeyqlprkh iqglekalkp gkkk
//
LOCUS       NP_060493               1422 aa            linear   PRI 27-APR-2025
DEFINITION  YEATS domain-containing protein 2 isoform 3 [Homo sapiens].
ACCESSION   NP_060493
VERSION     NP_060493.3
DBSOURCE    REFSEQ: accession NM_018023.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1422)
  AUTHORS   Wu,Q., Zheng,Q., Yuan,L., Gao,D., Hu,Y., Jiang,X., Zhai,Q., Liu,M.,
            Xu,L., Xu,H., Ye,J. and Zhang,F.
  TITLE     Repression of YEATS2 induces cellular senescence in hepatocellular
            carcinoma and inhibits tumor growth
  JOURNAL   Cell Cycle 23 (4), 478-494 (2024)
   PUBMED   38619971
  REMARK    GeneRIF: Repression of YEATS2 induces cellular senescence in
            hepatocellular carcinoma and inhibits tumor growth.
REFERENCE   2  (residues 1 to 1422)
  AUTHORS   Sheng,H., Zheng,F., Lan,T., Chen,H.F., Xu,C.Y., Wang,S.W.,
            Weng,Y.Y., Xu,L.F. and Zhang,F.
  TITLE     YEATS2 regulates the activation of TAK1/NF-kappaB pathway and is
            critical for pancreatic ductal adenocarcinoma cell survival
  JOURNAL   Cell Biol Toxicol 39 (3), 1-16 (2023)
   PUBMED   34686948
  REMARK    GeneRIF: YEATS2 regulates the activation of TAK1/NF-kappaB pathway
            and is critical for pancreatic ductal adenocarcinoma cell survival.
REFERENCE   3  (residues 1 to 1422)
  AUTHORS   Sha,T., Li,J., Sun,S., Li,J., Zhao,X., Li,Z. and Cui,Z.
  TITLE     YEATS domain-containing 2 (YEATS2), targeted by microRNA
            miR-378a-5p, regulates growth and metastasis in head and neck
            squamous cell carcinoma
  JOURNAL   Bioengineered 12 (1), 7286-7296 (2021)
   PUBMED   34587874
  REMARK    GeneRIF: YEATS domain-containing 2 (YEATS2), targeted by microRNA
            miR-378a-5p, regulates growth and metastasis in head and neck
            squamous cell carcinoma.
REFERENCE   4  (residues 1 to 1422)
  AUTHORS   Zeng,Z., Lei,S., He,Z., Chen,T. and Jiang,J.
  TITLE     YEATS2 is a target of HIF1alpha and promotes pancreatic cancer cell
            proliferation and migration
  JOURNAL   J Cell Physiol 236 (3), 2087-2098 (2021)
   PUBMED   32749678
  REMARK    GeneRIF: YEATS2 is a target of HIF1alpha and promotes pancreatic
            cancer cell proliferation and migration.
REFERENCE   5  (residues 1 to 1422)
  AUTHORS   Yeetong,P., Pongpanich,M., Srichomthong,C., Assawapitaksakul,A.,
            Shotelersuk,V., Tantirukdham,N., Chunharas,C., Suphapeetiporn,K.
            and Shotelersuk,V.
  TITLE     TTTCA repeat insertions in an intron of YEATS2 in benign adult
            familial myoclonic epilepsy type 4
  JOURNAL   Brain 142 (11), 3360-3366 (2019)
   PUBMED   31539032
  REMARK    GeneRIF: our findings suggest that benign adult familial myoclonic
            epilepsy type 4 is caused by the insertions of the intronic TTTCA
            repeats in YEATS2
REFERENCE   6  (residues 1 to 1422)
  AUTHORS   Nagy,Z., Riss,A., Fujiyama,S., Krebs,A., Orpinell,M., Jansen,P.,
            Cohen,A., Stunnenberg,H.G., Kato,S. and Tora,L.
  TITLE     The metazoan ATAC and SAGA coactivator HAT complexes regulate
            different sets of inducible target genes
  JOURNAL   Cell Mol Life Sci 67 (4), 611-628 (2010)
   PUBMED   19936620
REFERENCE   7  (residues 1 to 1422)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   8  (residues 1 to 1422)
  AUTHORS   Guelman,S., Kozuka,K., Mao,Y., Pham,V., Solloway,M.J., Wang,J.,
            Wu,J., Lill,J.R. and Zha,J.
  TITLE     The double-histone-acetyltransferase complex ATAC is essential for
            mammalian development
  JOURNAL   Mol Cell Biol 29 (5), 1176-1188 (2009)
   PUBMED   19103755
REFERENCE   9  (residues 1 to 1422)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
REFERENCE   10 (residues 1 to 1422)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068769.19, BC150273.1,
            BC082270.1 and CA416892.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 13, 2003 this sequence version replaced NP_060493.2.
            
            Summary: Summary: The protein encoded by this gene is a scaffolding
            subunit of the ATAC complex, which is a complex with
            acetyltransferase activity on histones H3 and H4. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, May 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150273.1, AB033023.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305135.10/ ENSP00000306983.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..1422
                     /product="YEATS domain-containing protein 2 isoform 3"
                     /note="YEATS domain-containing protein 2"
                     /calculated_mol_wt=150651
     Region          117..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TUF7; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Region          208..331
                     /region_name="YEATS_YEATS2_like"
                     /note="YEATS domain found in YEATS2 and Drosophila D12;
                     cd16907"
                     /db_xref="CDD:341126"
     Site            order(259..262,280..285,309)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:341126"
     Region          259..261
                     /region_name="Histone H3K27cr binding.
                     /evidence=ECO:0000269|PubMed:27103431,
                     ECO:0007744|PDB:5IQL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Region          282..284
                     /region_name="Histone H3K27cr binding.
                     /evidence=ECO:0000269|PubMed:27103431,
                     ECO:0007744|PDB:5IQL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Region          465..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Region          513..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Region          794..842
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM3.2)"
     Region          <868..>1118
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     Site            1219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULM3.2)"
     CDS             1..1422
                     /gene="YEATS2"
                     /gene_synonym="FAME4"
                     /coded_by="NM_018023.5:217..4485"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS43175.1"
                     /db_xref="GeneID:55689"
                     /db_xref="HGNC:HGNC:25489"
                     /db_xref="MIM:613373"
ORIGIN      
        1 msgikrtike tdpdyedvsv alpnkrhkai ensardaavq kietiikeqf alemknkehe
       61 ievidqrlie arrmmdklra civanyyasa gllkvsegsk tcdtmvfnhp aikkflesps
      121 rssspanqra etpsanhses dslsqhndfl sdkdnnsnmd ieerlsnnme qrpsrntgrd
      181 tsritgshkt eqrnadltde tsrlfvkkti vvgnvskyip pdkreendqs thkwmvyvrg
      241 srrepsinhf vkkvwfflhp sykpndlvev reppfhltrr gwgefpvrvq vhfkdsqnkr
      301 idiihnlkld rtytglqtlg aetvvdvelh rhslgedciy pqssesdisd appslpltip
      361 apvkasspik qshepvpdts vekgfpaste aerhtpfyal psslertptk mttsqkvtfc
      421 shgnsafqpi assckivpqs qvpnpespgk sfqpitmsck ivsgspistp spsplprtpt
      481 stpvhvkqgt agsvinnpyv imdkqpgqvi gattpstgsp tnkistasqv sqgtgspvpk
      541 ihgssfvtst vkqedslfas mpplcpigsh pkvqspkpit gglgaftkvi ikqepgeaph
      601 vpatgaasqs plpqyvtvkg ghmiavspqk qvitpgegia qsakvqpskv vgvpvgsalp
      661 stvkqavais ggqilvakas ssvskavgpk qvvtqgvaka ivsggggtiv aqpvqtltka
      721 qvtaagpqks gsqgsvmatl qlpatnlanl anlppgtkly lttnsknpsg kgklllipqg
      781 ailratnnan lqsgsaasgg sgaggggggg ggggsgsggg gstgggggta gggtqstagp
      841 ggisqhltyt syilkqtpqg tflvgqpspq tsgkqlttgs vvqgtlgvst ssaqgqqtlk
      901 visgqkttlf tqaahggqas lmkisdstlk tvpatsqlsk pgttmlrvag gvittatspa
      961 valsangpaq qsegmapvss stvssvtkts gqqqvcvsqa tvgtckaatp tvvsatslvp
     1021 tpnpisgkat vsgllkihss qsspqqavlt ipsqlkplsv ntsggvqtil mpvnkvvqsf
     1081 stskppailp vaaptpvvps sapaavakvk tepetpgpsc lsqegqtavk teesselgny
     1141 vikidhleti qqlltavvkk iplitaksed ascfsaksve qyygwnigkr raaewqramt
     1201 mrkvlqeile knprfhhltp lktkhiahwc rchgytppdp eslrndgdsi edvltqidse
     1261 pecpssfssa dnlcrkledl qqfqkrepen eeevdilsls epvkinikke qeekqeevkf
     1321 ylpptpgsef igdvtqkigi tlqpvalhrn vyasvvedmi lkateqlvnd ilrqalavgy
     1381 qtashnripk eitvsnihqa icnipfldfl tnkhmgilne dq
//
LOCUS       NP_776512                179 aa            linear   MAM 27-APR-2025
DEFINITION  insulin-like growth factor 2 preproprotein [Bos taurus].
ACCESSION   NP_776512 XP_024842737 XP_870711
VERSION     NP_776512.2
DBSOURCE    REFSEQ: accession NM_174087.4
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Willhelm,B.R., Ticiani,E., Campagnolo,K., Rodrigues,J.L.,
            Roberts,A.J., Anderson,G.B. and Bertolini,M.
  TITLE     Components of the insulin-like growth factor system in in vivo -
            and in vitro-derived fetuses of cattle, and the association with
            growth and development
  JOURNAL   Anim Reprod Sci 234, 106856 (2021)
   PUBMED   34626867
  REMARK    GeneRIF: Components of the insulin-like growth factor system in in
            vivo - and in vitro-derived fetuses of cattle, and the association
            with growth and development.
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Ghanipoor-Samami,M., Javadmanesh,A., Burns,B.M., Thomsen,D.A.,
            Nattrass,G.S., Estrella,C.A.S., Kind,K.L. and Hiendleder,S.
  TITLE     Atlas of tissue- and developmental stage specific gene expression
            for the bovine insulin-like growth factor (IGF) system
  JOURNAL   PLoS One 13 (7), e0200466 (2018)
   PUBMED   30001361
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Bouwman,A.C., Daetwyler,H.D., Chamberlain,A.J., Ponce,C.H.,
            Sargolzaei,M., Schenkel,F.S., Sahana,G., Govignon-Gion,A.,
            Boitard,S., Dolezal,M., Pausch,H., Brondum,R.F., Bowman,P.J.,
            Thomsen,B., Guldbrandtsen,B., Lund,M.S., Servin,B., Garrick,D.J.,
            Reecy,J., Vilkki,J., Bagnato,A., Wang,M., Hoff,J.L., Schnabel,R.D.,
            Taylor,J.F., Vinkhuyzen,A.A.E., Panitz,F., Bendixen,C., Holm,L.E.,
            Gredler,B., Hoze,C., Boussaha,M., Sanchez,M.P., Rocha,D.,
            Capitan,A., Tribout,T., Barbat,A., Croiseau,P., Drogemuller,C.,
            Jagannathan,V., Vander Jagt,C., Crowley,J.J., Bieber,A.,
            Purfield,D.C., Berry,D.P., Emmerling,R., Gotz,K.U.,
            Frischknecht,M., Russ,I., Solkner,J., Van Tassell,C.P., Fries,R.,
            Stothard,P., Veerkamp,R.F., Boichard,D., Goddard,M.E. and
            Hayes,B.J.
  TITLE     Meta-analysis of genome-wide association studies for cattle stature
            identifies common genes that regulate body size in mammals
  JOURNAL   Nat Genet 50 (3), 362-367 (2018)
   PUBMED   29459679
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Su,J., Wang,Y., Xing,X., Zhang,L., Sun,H. and Zhang,Y.
  TITLE     Melatonin significantly improves the developmental competence of
            bovine somatic cell nuclear transfer embryos
  JOURNAL   J Pineal Res 59 (4), 455-468 (2015)
   PUBMED   26331949
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Mendonca Ados,S., Guimaraes,A.L., da Silva,N.M., Caetano,A.R.,
            Dode,M.A. and Franco,M.M.
  TITLE     Characterization of the IGF2 Imprinted Gene Methylation Status in
            Bovine Oocytes during Folliculogenesis
  JOURNAL   PLoS One 10 (10), e0142072 (2015)
   PUBMED   26517264
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Congote,L.F., Mazza,L. and Palfree,R.G.
  TITLE     Nucleotide sequence of the central coding region of bovine
            erythrotropin/insulin-like growth factor II cDNA from fetal
            intestine and northern analysis of the major IGF II transcripts at
            the time of hepatic erythropoiesis
  JOURNAL   Comp Biochem Physiol B 103 (1), 127-131 (1992)
   PUBMED   1280544
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Brown,W.M., Dziegielewska,K.M., Foreman,R.C. and Saunders,N.R.
  TITLE     The nucleotide and deduced amino acid sequences of insulin-like
            growth factor II cDNAs from adult bovine and fetal sheep liver
  JOURNAL   Nucleic Acids Res 18 (15), 4614 (1990)
   PUBMED   2388846
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Li,Q.G., Blacher,R., Esch,F. and Congote,L.F.
  TITLE     A heparin-binding erythroid cell stimulating factor from fetal
            bovine serum has the N-terminal sequence of insulin-like growth
            factor II
  JOURNAL   Biochem Biophys Res Commun 166 (2), 557-561 (1990)
   PUBMED   2302223
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Francis,G.L., Upton,F.M., Ballard,F.J., McNeil,K.A. and
            Wallace,J.C.
  TITLE     Insulin-like growth factors 1 and 2 in bovine colostrum. Sequences
            and biological activities compared with those of a potent truncated
            form
  JOURNAL   Biochem J 251 (1), 95-103 (1988)
   PUBMED   3390164
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Honegger,A. and Humbel,R.E.
  TITLE     Insulin-like growth factors I and II in fetal and adult bovine
            serum. Purification, primary structures, and immunological
            cross-reactivities
  JOURNAL   J Biol Chem 261 (2), 569-575 (1986)
   PUBMED   3941093
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from NKLS02000029.1.
            
            On or before Dec 12, 2018 this sequence version replaced
            XP_024842737.1, NP_776512.1.
            
            Summary: This gene encodes a member of the insulin family of
            protein growth factors, which are involved in fetal development and
            growth. It is an imprinted gene that is expressed from the paternal
            allele while the maternal allele is silenced. The encoded protein
            is proteolytically processed to generate the mature peptide
            hormone, which binds to receptors of the insulin receptor family.
            This peptide plays a role in oocyte development and
            folliculogenesis in female cattle. Polymorphisms in this gene may
            be associated with cattle body mass. [provided by RefSeq, Dec
            2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5571260.41918.1,
                                           SRR5571257.34097.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03145427, SAMN04019641
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="29"
                     /map="29"
                     /breed="Hereford"
     Protein         1..179
                     /product="insulin-like growth factor 2 preproprotein"
                     /note="insulin-like growth factor II; IGF-II;
                     erythrotropin; insulin-like growth factor 2 (somatomedin
                     A)"
                     /calculated_mol_wt=17250
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2450
     mat_peptide     25..91
                     /product="Insulin-like growth factor 2.
                     /id=PRO_0000015711"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
                     /calculated_mol_wt=7533
     Region          25..52
                     /region_name="B"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Region          28..91
                     /region_name="IlGF"
                     /note="insulin_like growth factors; specific to
                     vertebrates. Members include a number of peptides
                     including insulin-like growth factors I and II, which play
                     a variety of roles in controlling processes such as
                     growth, differentiation, and reproduction. On a...;
                     cd04368"
                     /db_xref="CDD:239834"
     Site            order(30,39,47..51)
                     /site_type="active"
                     /note="IGFBP binding surface [active]"
                     /db_xref="CDD:239834"
     Site            order(48,50..51,67)
                     /site_type="active"
                     /note="type 1 IGF- and insulin-receptor binding surface
                     [active]"
                     /db_xref="CDD:239834"
     Site            48
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          53..64
                     /region_name="C"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Site            58
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Site            61
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Site            62
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          65..85
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Site            order(72..74,78..79)
                     /site_type="active"
                     /note="type 2 IGF-receptor binding surface [active]"
                     /db_xref="CDD:239834"
     Region          86..91
                     /region_name="D"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     mat_peptide     93..126
                     /product="Preptin. /id=PRO_0000370373"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
                     /calculated_mol_wt=3877
     Site            106
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19674964; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          112..166
                     /region_name="IGF2_C"
                     /note="Insulin-like growth factor II E-peptide; pfam08365"
                     /db_xref="CDD:462445"
     Site            154
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:19674964; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          160..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Site            163
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19674964; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     CDS             1..179
                     /gene="IGF2"
                     /coded_by="NM_174087.4:577..1116"
                     /db_xref="BGD:BT11333"
                     /db_xref="GeneID:281240"
                     /db_xref="VGNC:VGNC:30078"
ORIGIN      
        1 mgitagksvl vllaflafas ccyaayrpse tlcggelvdt lqfvcgdrgf yfsrpssrin
       61 rrsrgiveec cfrscdlall etycatpaks erdvsasttv lpddvtaypv gkffqydiwk
      121 qstqrlrrgl paflrarrgr tlakelealr eakshrplia lptqdpathg gasskassd
//
LOCUS       NP_080979                172 aa            linear   ROD 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 [Mus
            musculus].
ACCESSION   NP_080979
VERSION     NP_080979.1
DBSOURCE    REFSEQ: accession NM_026703.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Fu,Q., Lv,R., Wang,S., Wang,W., Li,Y., Qiu,G., Chen,X. and Sun,C.
  TITLE     Ndufa8 promotes white fat Browning by improving mitochondrial
            respiratory chain complex I function to ameliorate obesity by in
            vitro and in vivo
  JOURNAL   Cell Signal 122, 111340 (2024)
   PUBMED   39127135
  REMARK    GeneRIF: Ndufa8 promotes white fat Browning by improving
            mitochondrial respiratory chain complex I function to ameliorate
            obesity by in vitro and in vivo.
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Vercellino,I. and Sazanov,L.A.
  TITLE     SCAF1 drives the compositional diversity of mammalian respirasomes
  JOURNAL   Nat Struct Mol Biol 31 (7), 1061-1071 (2024)
   PUBMED   38575788
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Yao,Y., Liu,Q., Adrianto,I., Wu,X., Glassbrook,J., Khalasawi,N.,
            Yin,C., Yi,Q., Dong,Z., Geissmann,F., Zhou,L. and Mi,Q.S.
  TITLE     Histone deacetylase 3 controls lung alveolar macrophage development
            and homeostasis
  JOURNAL   Nat Commun 11 (1), 3822 (2020)
   PUBMED   32732898
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Wirtz,S. and Schuelke,M.
  TITLE     Region-specific expression of mitochondrial complex I genes during
            murine brain development
  JOURNAL   PLoS One 6 (4), e18897 (2011)
   PUBMED   21556144
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL773525.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI871940.1, CX242850.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 24.13 cM"
     Protein         1..172
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 8"
                     /note="complex I-19kD; complex I-PGIV; NADH-ubiquinone
                     oxidoreductase 19 kDa subunit; NADH dehydrogenase
                     (ubiquinone) 1 alpha subcomplex, 8"
                     /calculated_mol_wt=19861
     Region          36..46
                     /region_name="Cx9C motif 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DCJ5.3)"
     Region          56..66
                     /region_name="Cx9C motif 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DCJ5.3)"
     Region          78..111
                     /region_name="CHCH"
                     /note="CHCH domain; pfam06747"
                     /db_xref="CDD:429096"
     Region          78..88
                     /region_name="Cx9C motif 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DCJ5.3)"
     Region          100..110
                     /region_name="Cx9C motif 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DCJ5.3)"
     CDS             1..172
                     /gene="Ndufa8"
                     /gene_synonym="0610033L03Rik; CI-19kD; CI-PGIV"
                     /coded_by="NM_026703.3:97..615"
                     /db_xref="CCDS:CCDS15967.1"
                     /db_xref="GeneID:68375"
                     /db_xref="MGI:MGI:1915625"
ORIGIN      
        1 mpgivelptl eelkveevkv ssavlkaaah hygaqcdktn kefmlcrwee kdprrclkeg
       61 klvngcalnf frqikshcae pfteywtcld ysnmqlfrhc rqqqakfdqc vldklgwvrp
      121 dlgqlskvtk vktdrplpen pyhsrarpep npviegdlkp akhgtrfffw tv
//
LOCUS       NP_001346435            1249 aa            linear   ROD 27-APR-2025
DEFINITION  plasma membrane calcium-transporting ATPase 1 isoform 1 [Mus
            musculus].
ACCESSION   NP_001346435 XP_006514078
VERSION     NP_001346435.1
DBSOURCE    REFSEQ: accession NM_001359506.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1249)
  AUTHORS   Gomez-Del Arco,P., Isern,J., Jimenez-Carretero,D.,
            Lopez-Maderuelo,D., Pineiro-Sabaris,R., El Abdellaoui-Soussi,F.,
            Torroja,C., Vera-Pedrosa,M.L., Grima-Terren,M., Benguria,A.,
            Simon-Chica,A., Queiro-Palou,A., Dopazo,A., Sanchez-Cabo,F.,
            Jalife,J., de la Pompa,J.L., Filgueiras-Rama,D., Munoz-Canoves,P.
            and Redondo,J.M.
  TITLE     The G4 resolvase Dhx36 modulates cardiomyocyte differentiation and
            ventricular conduction system development
  JOURNAL   Nat Commun 15 (1), 8602 (2024)
   PUBMED   39366945
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1249)
  AUTHORS   Javkhlant,A., Toyama,K., Abe,Y., Spin,J.M. and Mogi,M.
  TITLE     Lack of ATP2B1 in CD4+ T Cells Causes Colitis
  JOURNAL   Inflamm Bowel Dis 30 (10), 1852-1864 (2024)
   PUBMED   38507609
  REMARK    GeneRIF: Lack of ATP2B1 in CD4+ T Cells Causes Colitis.
REFERENCE   3  (residues 1 to 1249)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 1249)
  AUTHORS   Beckmann,D., Langnaese,K., Gottfried,A., Hradsky,J., Tedford,K.,
            Tiwari,N., Thomas,U., Fischer,K.D. and Korthals,M.
  TITLE     Ca2+ Homeostasis by Plasma Membrane Ca2+ ATPase (PMCA) 1 Is
            Essential for the Development of DP Thymocytes
  JOURNAL   Int J Mol Sci 24 (2), 1442 (2023)
   PUBMED   36674959
  REMARK    GeneRIF: Ca[2+] Homeostasis by Plasma Membrane Ca[2+] ATPase (PMCA)
            1 Is Essential for the Development of DP Thymocytes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1249)
  AUTHORS   Savy,V., Stein,P., Shi,M. and Williams,C.J.
  TITLE     PMCA1 depletion in mouse eggs amplifies calcium signaling and
            impacts offspring growthdagger
  JOURNAL   Biol Reprod 107 (6), 1439-1451 (2022)
   PUBMED   36130203
REFERENCE   6  (residues 1 to 1249)
  AUTHORS   Garcia,M.L. and Strehler,E.E.
  TITLE     Plasma membrane calcium ATPases as critical regulators of calcium
            homeostasis during neuronal cell function
  JOURNAL   Front Biosci 4, D869-D882 (1999)
   PUBMED   10577388
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1249)
  AUTHORS   Zacharias,D.A. and Kappen,C.
  TITLE     Developmental expression of the four plasma membrane calcium ATPase
            (Pmca) genes in the mouse
  JOURNAL   Biochim Biophys Acta 1428 (2-3), 397-405 (1999)
   PUBMED   10434059
REFERENCE   8  (residues 1 to 1249)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
REFERENCE   9  (residues 1 to 1249)
  AUTHORS   Jaisser,F. and Beggah,A.T.
  TITLE     The nongastric H+-K+-ATPases: molecular and functional properties
  JOURNAL   Am J Physiol 276 (6), F812-F824 (1999)
   PUBMED   10362770
  REMARK    Review article
REFERENCE   10 (residues 1 to 1249)
  AUTHORS   Du,Y., Carlock,L. and Kuo,T.H.
  TITLE     The mouse plasma membrane Ca2+ pump isoform 1 promoter: cloning and
            characterization
  JOURNAL   Arch Biochem Biophys 316 (1), 302-310 (1995)
   PUBMED   7840630
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC153906.4, CJ128577.1, AK133920.1, AI892140.1, CJ321142.1,
            CV559947.1, CK624413.1, CK393435.1, CF750345.1, CN691756.1,
            BI732378.1, AC160410.3 and BQ176881.1.
            
            On Jan 13, 2018 this sequence version replaced XP_006514078.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR10223971.10514.1,
                                           SRR10223970.12678.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849390, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1249
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 50.97 cM"
     Protein         1..1249
                     /product="plasma membrane calcium-transporting ATPase 1
                     isoform 1"
                     /EC_number="7.2.2.10"
                     /note="plasma membrane calcium pump; plasma membrane
                     calcium ATPase; plasma membrane calcium-transporting
                     ATPase 1"
                     /calculated_mol_wt=137736
     Region          15..1064
                     /region_name="ATPase-IIB_Ca"
                     /note="plasma-membrane calcium-translocating P-type
                     ATPase; TIGR01517"
                     /db_xref="CDD:273668"
     Region          1103..1178
                     /region_name="ATP_Ca_trans_C"
                     /note="Plasma membrane calcium transporter ATPase C
                     terminal; pfam12424"
                     /db_xref="CDD:463575"
     CDS             1..1249
                     /gene="Atp2b1"
                     /gene_synonym="2810442I22Rik; E130111D10Rik; Pmca1"
                     /coded_by="NM_001359506.1:376..4125"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:67972"
                     /db_xref="MGI:MGI:104653"
ORIGIN      
        1 mgdmannsva ysgvknslke anhdgdfgit ltelralmel rstdalrkiq esygdvygic
       61 tklktspneg lsgnpadler reavfgknfi ppkkpktflq lvwealqdvt liileiaaiv
      121 slglsfyqpp egdnalcgev svgeeegege tgwiegaail lsvvcvvlvt afndwskekq
      181 frglqsrieq eqkftvirgg qviqipvadi tvgdiaqvky gdllpadgil iqgndlkide
      241 ssltgesdhv kksldkdpll lsgthvmegs grmvvtavgv nsqtgiiftl lgaggeeeek
      301 kdekkkekkn kkqdgaienr nkakaqdgaa memqplksee ggdgdekdkk kanlpkkeks
      361 vlqgkltkla vqigkagllm saitviilvl yfvidtfwvq krpwlaectp iyiqyfvkff
      421 iigvtvlvva vpeglplavt islaysvkkm mkdnnlvrhl dacetmgnat aicsdktgtl
      481 tmnrmtvvqa yinekhykkv pepeaippni lsylvtgisv ncaytskilp pekegglprh
      541 vgnktecall gflldlkrdy qdvrneipee alykvytfns vrksmstvlk nsdgsfrifs
      601 kgaseiilkk cfkilsange akvfrprdrd divktviepm aseglrticl afrdfpagep
      661 epewdnendv vtgltciavv giedpvrpev peaikkcqra gitvrmvtgd nintaraiat
      721 kcgilhpged flclegkdfn rrirnekgei eqeridkiwp klrvlarssp tdkhtlvkgi
      781 idstvseqrq vvavtgdgtn dgpalkkadv gfamgiagtd vakeasdiil tddnftsivk
      841 avmwgrnvyd siskflqfql tvnvvaviva ftgacitqds plkavqmlwv nlimdtlasl
      901 alatepptes lllrkpygrn kplisrtmmk nilghafyql vvvftllfag ekffdidsgr
      961 naplhappse hytivfntfv lmqlfneina rkihgernvf egifnnaifc tivlgtfvvq
     1021 iiivqfggkp fscselsieq wlwsiflgmg tllwgqlist iptsrlkflk eaghgtqkee
     1081 ipeeelaedv eeidhaerel rrgqilwfrg lnriqtqmdv vnafqsgssi qgalrrqpsi
     1141 asqhhdirvv nafrsslyeg lekpesrssi hnfmthpefr iedsephipl iddtdaedda
     1201 ptkrnssppp spnknnnavd sgihltiemn ksatssspgs plhsletsl
//
LOCUS       NP_058556                376 aa            linear   ROD 27-APR-2025
DEFINITION  alpha-centractin isoform 1 [Mus musculus].
ACCESSION   NP_058556 XP_986115
VERSION     NP_058556.1
DBSOURCE    REFSEQ: accession NM_016860.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Lee,M., Liu,Y.C., Chen,C., Lu,C.H., Lu,S.T., Huang,T.N., Hsu,M.T.,
            Hsueh,Y.P. and Cheng,P.L.
  TITLE     Ecm29-mediated proteasomal distribution modulates excitatory GABA
            responses in the developing brain
  JOURNAL   J Cell Biol 219 (2) (2020)
   PUBMED   31910261
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Clarkson,Y.L., Gillespie,T., Perkins,E.M., Lyndon,A.R. and
            Jackson,M.
  TITLE     Beta-III spectrin mutation L253P associated with spinocerebellar
            ataxia type 5 interferes with binding to Arp1 and protein
            trafficking from the Golgi
  JOURNAL   Hum Mol Genet 19 (18), 3634-3641 (2010)
   PUBMED   20603325
  REMARK    GeneRIF: Beta-III spectrin mutation L253P interferes with binding
            to Arp1 and protein trafficking from the Golgi.
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Lin,S.S., Bassik,M.C., Suh,H., Nishino,M., Arroyo,J.D., Hahn,W.C.,
            Korsmeyer,S.J. and Roberts,T.M.
  TITLE     PP2A regulates BCL-2 phosphorylation and proteasome-mediated
            degradation at the endoplasmic reticulum
  JOURNAL   J Biol Chem 281 (32), 23003-23012 (2006)
   PUBMED   16717086
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Eckley,D.M. and Schroer,T.A.
  TITLE     Interactions between the evolutionarily conserved, actin-related
            protein, Arp11, actin, and Arp1
  JOURNAL   Mol Biol Cell 14 (7), 2645-2654 (2003)
   PUBMED   12857853
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Carninci,P., Waki,K., Shiraki,T., Konno,H., Shibata,K., Itoh,M.,
            Aizawa,K., Arakawa,T., Ishii,Y., Sasaki,D., Bono,H., Kondo,S.,
            Sugahara,Y., Saito,R., Osato,N., Fukuda,S., Sato,K., Watahiki,A.,
            Hirozane-Kishikawa,T., Nakamura,M., Shibata,Y., Yasunishi,A.,
            Kikuchi,N., Yoshiki,A., Kusakabe,M., Gustincich,S., Beisel,K.,
            Pavan,W., Aidinis,V., Nakagawara,A., Held,W.A., Iwata,H., Kono,T.,
            Nakauchi,H., Lyons,P., Wells,C., Hume,D.A., Fagiolini,M.,
            Hensch,T.K., Brinkmeier,M., Camper,S., Hirota,J., Mombaerts,P.,
            Muramatsu,M., Okazaki,Y., Kawai,J. and Hayashizaki,Y.
  TITLE     Targeting a complex transcriptome: the construction of the mouse
            full-length cDNA encyclopedia
  JOURNAL   Genome Res 13 (6B), 1273-1289 (2003)
   PUBMED   12819125
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Kusano,K., Abe,H. and Obinata,T.
  TITLE     Primary structure of mouse actin-related protein 1 (Arp1) and its
            tissue expression
  JOURNAL   Zoolog Sci 14 (1), 77-82 (1997)
   PUBMED   9200982
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY794369.1, AB010297.1 and CD776146.1.
            
            On May 4, 2006 this sequence version replaced XP_986115.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK167450.1, SRR7345562.4696985.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164138
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 38.84 cM"
     Protein         1..376
                     /product="alpha-centractin isoform 1"
                     /note="actin-related protein 1 alpha; alpha-centractin;
                     centrosome-associated actin homolog; ARP1 actin-related
                     protein 1 homolog A, centractin alpha"
                     /calculated_mol_wt=42483
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P61163; propagated from
                     UniProtKB/Swiss-Prot (P61164.1)"
     Region          9..375
                     /region_name="ASKHA_NBD_Arp1"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein 1 (Arp1) and similar proteins; cd10216"
                     /db_xref="CDD:466820"
     CDS             1..376
                     /gene="Actr1a"
                     /gene_synonym="actin-RPV; alpha-Arp1; Arp1"
                     /coded_by="NM_016860.2:65..1195"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS29878.1"
                     /db_xref="GeneID:54130"
                     /db_xref="MGI:MGI:1858964"
ORIGIN      
        1 mesydvianq pvvidngsgv ikagfagdqi pkycfpnyvg rpkhvrvmag alegdifigp
       61 kaeehrglls irypmehgiv kdwndmeriw qyvyskdqlq tfseehpvll teaplnprkn
      121 reraaevffe tfnvpalfis mqavlslyat grttgvvlds gdgvthavpi yegfamphsi
      181 mridiagrdv srflrlylrk egydfhssse feivkaiker acylsinpqk detletekaq
      241 yylpdgstie igpsrfrape llfrpdlige esegihevlv faiqksdmdl rrtlfsnivl
      301 sggstlfkgf gdrllsevkk lapkdvkiri sapqerlyst wiggsilasl dtfkkmwvsk
      361 keyeedgars ihrktf
//
LOCUS       NP_001080               1704 aa            linear   PRI 27-APR-2025
DEFINITION  phospholipid-transporting ATPase ABCA3 [Homo sapiens].
ACCESSION   NP_001080
VERSION     NP_001080.2
DBSOURCE    REFSEQ: accession NM_001089.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1704)
  AUTHORS   Diesler,R., Legendre,M., Si-Mohamed,S., Brillet,P.Y., Wemeau,L.,
            Manali,E.D., Gagnadoux,F., Hirschi,S., Lorillon,G.,
            Reynaud-Gaubert,M., Bironneau,V., Blanchard,E., Bourdin,A.,
            Dominique,S., Justet,A., Macey,J., Marchand-Adam,S.,
            Morisse-Pradier,H., Nunes,H., Papiris,S.A., Traclet,J., Traore,I.,
            Crestani,B., Amselem,S., Nathan,N., Borie,R. and Cottin,V.
  CONSRTM   OrphaLung network
  TITLE     Similarities and differences of interstitial lung disease
            associated with pathogenic variants in SFTPC and ABCA3 in adults
  JOURNAL   Respirology 29 (4), 312-323 (2024)
   PUBMED   38345107
  REMARK    GeneRIF: Similarities and differences of interstitial lung disease
            associated with pathogenic variants in SFTPC and ABCA3 in adults.
REFERENCE   2  (residues 1 to 1704)
  AUTHORS   Anciuc-Crauciuc,M., Cucerea,M.C., Crauciuc,G.A., Tripon,F. and
            Banescu,C.V.
  TITLE     Evaluation of the Copy Number Variants and Single-Nucleotide
            Polymorphisms of ABCA3 in Newborns with Respiratory Distress
            Syndrome-A Pilot Study
  JOURNAL   Medicina (Kaunas) 60 (3), 419 (2024)
   PUBMED   38541145
  REMARK    GeneRIF: Evaluation of the Copy Number Variants and
            Single-Nucleotide Polymorphisms of ABCA3 in Newborns with
            Respiratory Distress Syndrome-A Pilot Study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1704)
  AUTHORS   El Demellawy,D., Kovesi,T., Gowans,R., Oltean,I., Huang,L.,
            White-Brown,A. and Sawyer,S.L.
  TITLE     Interstitial lung disease in a family with bi-allelic variants in
            ABCA3: non-specific interstitial pneumonitis pattern of injury
  JOURNAL   Pathology 56 (1), 104-107 (2024)
   PUBMED   37657992
  REMARK    GeneRIF: Interstitial lung disease in a family with bi-allelic
            variants in ABCA3: non-specific interstitial pneumonitis pattern of
            injury.
REFERENCE   4  (residues 1 to 1704)
  AUTHORS   Sun,Y.L., Hennessey,E.E., Heins,H., Yang,P., Villacorta-Martin,C.,
            Kwan,J., Gopalan,K., James,M., Emili,A., Cole,F.S., Wambach,J.A.
            and Kotton,D.N.
  TITLE     Human pluripotent stem cell modeling of alveolar type 2 cell
            dysfunction caused by ABCA3 mutations
  JOURNAL   J Clin Invest 134 (2), e164274 (2024)
   PUBMED   38226623
  REMARK    GeneRIF: Human pluripotent stem cell modeling of alveolar type 2
            cell dysfunction caused by ABCA3 mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1704)
  AUTHORS   Al-Shumary,D.S., Al-Shammari,A.M. and Rasheed,M.N.
  TITLE     Increased Expression of the ABCA1 and ABCA3 Transporter Genes is
            Associated with Cisplatin Resistance in Breast Cancer Cells
  JOURNAL   Asian Pac J Cancer Prev 24 (11), 3969-3977 (2023)
   PUBMED   38019257
  REMARK    GeneRIF: Increased Expression of the ABCA1 and ABCA3 Transporter
            Genes is Associated with Cisplatin Resistance in Breast Cancer
            Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1704)
  AUTHORS   Mulugeta,S., Gray,J.M., Notarfrancesco,K.L., Gonzales,L.W.,
            Koval,M., Feinstein,S.I., Ballard,P.L., Fisher,A.B. and Shuman,H.
  TITLE     Identification of LBM180, a lamellar body limiting membrane protein
            of alveolar type II cells, as the ABC transporter protein ABCA3
  JOURNAL   J Biol Chem 277 (25), 22147-22155 (2002)
   PUBMED   11940594
  REMARK    GeneRIF: Identification of LBM180, a lamellar body limiting
            membrane protein of alveolar type II cells, as the ABC transporter
            protein ABCA3
REFERENCE   7  (residues 1 to 1704)
  AUTHORS   Yamano,G., Funahashi,H., Kawanami,O., Zhao,L.X., Ban,N., Uchida,Y.,
            Morohoshi,T., Ogawa,J., Shioda,S. and Inagaki,N.
  TITLE     ABCA3 is a lamellar body membrane protein in human lung alveolar
            type II cells
  JOURNAL   FEBS Lett 508 (2), 221-225 (2001)
   PUBMED   11718719
REFERENCE   8  (residues 1 to 1704)
  AUTHORS   Connors,T.D., Van Raay,T.J., Petry,L.R., Klinger,K.W., Landes,G.M.
            and Burn,T.C.
  TITLE     The cloning of a human ABC gene (ABC3) mapping to chromosome
            16p13.3
  JOURNAL   Genomics 39 (2), 231-234 (1997)
   PUBMED   9027511
REFERENCE   9  (residues 1 to 1704)
  AUTHORS   Klugbauer,N. and Hofmann,F.
  TITLE     Primary structure of a novel ABC transporter with a chromosomal
            localization on the band encoding the multidrug
            resistance-associated protein
  JOURNAL   FEBS Lett 391 (1-2), 61-65 (1996)
   PUBMED   8706931
REFERENCE   10 (residues 1 to 1704)
  AUTHORS   Garcia,C.K. and Talbert,J.L.
  TITLE     Pulmonary Fibrosis Predisposition Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301408
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106820.4, AC098805.2 and
            AC009065.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 26, 2006 this sequence version replaced NP_001080.1.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters.  ABC proteins transport various molecules across
            extra- and intracellular membranes.  ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White).  This protein is a member of the ABC1 subfamily.  Members
            of the ABC1 subfamily comprise the only major ABC subfamily found
            exclusively in multicellular eukaryotes.  The full transporter
            encoded by this gene may be involved in development of resistance
            to xenobiotics and engulfment during programmed cell death.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC151840.1, U78735.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301732.10/ ENSP00000301732.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1704
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..1704
                     /product="phospholipid-transporting ATPase ABCA3"
                     /EC_number="7.6.2.2"
                     /EC_number="7.6.2.1"
                     /note="ABC transporter 3; ATP-binding cassette sub-family
                     A member 3; ABC-C transporter; ATP-binding cassette
                     transporter 3; ATP-binding cassette, sub-family A (ABC1),
                     member 3; xenobiotic-transporting ATPase ABCA3"
                     /calculated_mol_wt=191232
     Region          1..>43
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            14
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99758.2)"
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99758.2)"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:24142515;
                     propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Region          <131..1699
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:24142515;
                     propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            174..175
                     /site_type="cleavage"
                     /note="Cleavage, by CTSL.
                     /evidence=ECO:0000269|PubMed:27031696; propagated from
                     UniProtKB/Swiss-Prot (Q99758.2)"
     Site            261..283
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            307..327
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            344..364
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            373..393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            405..425
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            447..467
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            620
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99758.2)"
     Site            783
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99758.2)"
     Site            925..945
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            1100..1120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            1144..1164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            1183..1203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            1213..1233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            1245..1265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     Site            1306..1326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99758.2)"
     CDS             1..1704
                     /gene="ABCA3"
                     /gene_synonym="ABC-C; ABC3; EST111653; LBM180; SMDP3"
                     /coded_by="NM_001089.3:695..5809"
                     /db_xref="CCDS:CCDS10466.1"
                     /db_xref="GeneID:21"
                     /db_xref="HGNC:HGNC:33"
                     /db_xref="MIM:601615"
ORIGIN      
        1 mavlrqlall lwknytlqkr kvlvtvlelf lpllfsgili wlrlkiqsen vpnatiypgq
       61 siqelplfft fpppgdtwel ayipshsdaa ktvtetvrra lvinmrvrgf psekdfedyi
      121 rydncsssvl aavvfehpfn hskeplplav kyhlrfsytr rnymwtqtgs fflketegwh
      181 ttslfplfpn pgpreptspd ggepgyireg flavqhavdr aimeyhadaa trqlfqrltv
      241 tikrfpyppf iadpflvaiq yqlpllllls ftytaltiar avvqekerrl keymrmmgls
      301 swlhwsawfl lfflflliaa sfmtllfcvk vkpnvavlsr sdpslvlafl lcfaistisf
      361 sfmvstffsk anmaaafggf lyfftyipyf fvaprynwmt lsqklcscll snvamamgaq
      421 ligkfeakgm giqwrdllsp vnvdddfcfg qvlgmlllds vlyglvtwym eavfpgqfgv
      481 pqpwyffimp sywcgkprav agkeeedsdp ekalrneyfe aepedlvagi kikhlskvfr
      541 vgnkdraavr dlnlnlyegq itvllghnga gktttlsmlt glfpptsgra yisgyeisqd
      601 mvqirkslgl cpqhdilfdn ltvaehlyfy aqlkglsrqk cpeevkqmlh iigledkwns
      661 rsrflsggmr rklsigiali agskvlilde ptsgmdaisr raiwdllqrq ksdrtivltt
      721 hfmdeadllg driaimakge lqccgsslfl kqkygagyhm tlvkephcnp edisqlvhhh
      781 vpnatlessa gaelsfilpr esthrfeglf aklekkqkel giasfgasit tmeevflrvg
      841 klvdssmdiq aiqlpalqyq herrasdwav dsnlcgamdp sdgigaliee ertavklntg
      901 lalhcqqfwa mflkkaaysw rewkmvaaqv lvpltcvtla llainyssel fddpmlrltl
      961 geygrtvvpf svpgtsqlgq qlsehlkdal qaegqeprev lgdleeflif rasvegggfn
     1021 erclvaasfr dvgertvvna lfnnqayhsp atalavvdnl lfkllcgpha sivvsnfpqp
     1081 rsalqaakdq fnegrkgfdi alnllfamaf lastfsilav seravqakhv qfvsgvhvas
     1141 fwlsallwdl isflipslll lvvfkafdvr aftrdghmad tllllllygw aiiplmylmn
     1201 ffflgaatay trltifnils giatflmvti mripavklee lsktldhvfl vlpnhclgma
     1261 vssfyenyet rryctsseva ahyckkyniq yqenfyawsa pgvgrfvasm aasgcaylil
     1321 lflietnllq rlrgilcalr rrrtltelyt rmpvlpedqd vadertrila pspdsllhtp
     1381 liikelskvy eqrvpllavd rlslavqkge cfgllgfnga gktttfkmlt geesltsgda
     1441 fvgghrissd vgkvrqrigy cpqfdalldh mtgremlvmy arlrgiperh igacventlr
     1501 glllephank lvrtysggnk rklstgiali gepaviflde pstgmdpvar rllwdtvara
     1561 resgkaiiit shsmeeceal ctrlaimvqg qfkclgspqh lkskfgsgys lrakvqsegq
     1621 qealeefkaf vdltfpgsvl edehqgmvhy hlpgrdlswa kvfgilekak ekygvddysv
     1681 sqisleqvfl sfahlqppta eegr
//
LOCUS       NP_705618               1391 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear pore complex protein Nup155 isoform 1 [Homo sapiens].
ACCESSION   NP_705618
VERSION     NP_705618.1
DBSOURCE    REFSEQ: accession NM_153485.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1391)
  AUTHORS   Holzer,K., Ori,A., Cooke,A., Dauch,D., Drucker,E.,
            Riemenschneider,P., Andres-Pons,A., DiGuilio,A.L., Mackmull,M.T.,
            Bassler,J., Roessler,S., Breuhahn,K., Zender,L., Glavy,J.S.,
            Dombrowski,F., Hurt,E., Schirmacher,P., Beck,M. and Singer,S.
  TITLE     Nucleoporin Nup155 is part of the p53 network in liver cancer
  JOURNAL   Nat Commun 10 (1), 2147 (2019)
   PUBMED   31089132
  REMARK    GeneRIF: Study revealed that NUP155 controls mRNA translation
            CDKN1A, a key mediator of the p53 response.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1391)
  AUTHORS   Han,M., Zhao,M., Cheng,C., Huang,Y., Han,S., Li,W., Tu,X., Luo,X.,
            Yu,X., Liu,Y., Chen,Q., Ren,X., Wang,Q.K. and Ke,T.
  TITLE     Lamin A mutation impairs interaction with nucleoporin NUP155 and
            disrupts nucleocytoplasmic transport in atrial fibrillation
  JOURNAL   Hum Mutat 40 (3), 310-325 (2019)
   PUBMED   30488537
  REMARK    GeneRIF: lamin A/C mutation p.Arg399Cys weakens the interaction
            between nuclear lamina (lamin A/C) and the nuclear pore complex
            (NUP155), leading to the development of atrial fibrillation.
REFERENCE   3  (residues 1 to 1391)
  AUTHORS   Liu,X., Salokas,K., Tamene,F., Jiu,Y., Weldatsadik,R.G., Ohman,T.
            and Varjosalo,M.
  TITLE     An AP-MS- and BioID-compatible MAC-tag enables comprehensive
            mapping of protein interactions and subcellular localizations
  JOURNAL   Nat Commun 9 (1), 1188 (2018)
   PUBMED   29568061
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1391)
  AUTHORS   Schwartz,T.U.
  TITLE     The Structure Inventory of the Nuclear Pore Complex
  JOURNAL   J Mol Biol 428 (10 Pt A), 1986-2000 (2016)
   PUBMED   27016207
  REMARK    Review article
REFERENCE   5  (residues 1 to 1391)
  AUTHORS   Rayala,H.J., Kendirgi,F., Barry,D.M., Majerus,P.W. and Wente,S.R.
  TITLE     The mRNA export factor human Gle1 interacts with the nuclear pore
            complex protein Nup155
  JOURNAL   Mol Cell Proteomics 3 (2), 145-155 (2004)
   PUBMED   14645504
REFERENCE   6  (residues 1 to 1391)
  AUTHORS   Le Rouzic,E., Mousnier,A., Rustum,C., Stutz,F., Hallberg,E.,
            Dargemont,C. and Benichou,S.
  TITLE     Docking of HIV-1 Vpr to the nuclear envelope is mediated by the
            interaction with the nucleoporin hCG1
  JOURNAL   J Biol Chem 277 (47), 45091-45098 (2002)
   PUBMED   12228227
REFERENCE   7  (residues 1 to 1391)
  AUTHORS   Zhang,X., Yang,H., Yu,J., Chen,C., Zhang,G., Bao,J., Du,Y.,
            Kibukawa,M., Li,Z., Wang,J., Hu,S., Dong,W., Wang,J., Gregersen,N.,
            Niebuhr,E. and Bolund,L.
  TITLE     Genomic organization, transcript variants and comparative analysis
            of the human nucleoporin 155 (NUP155) gene
  JOURNAL   Gene 288 (1-2), 9-18 (2002)
   PUBMED   12034489
REFERENCE   8  (residues 1 to 1391)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   9  (residues 1 to 1391)
  AUTHORS   Zhang,X., Yang,H., Corydon,M.J., Zhang,X., Pedersen,S.,
            Korenberg,J.R., Chen,X.N., Laporte,J., Gregersen,N., Niebuhr,E.,
            Liu,G. and Bolund,L.
  TITLE     Localization of a human nucleoporin 155 gene (NUP155) to the 5p13
            region and cloning of its cDNA
  JOURNAL   Genomics 57 (1), 144-151 (1999)
   PUBMED   10191094
REFERENCE   10 (residues 1 to 1391)
  AUTHORS   Gorlich,D. and Mattaj,I.W.
  TITLE     Nucleocytoplasmic transport
  JOURNAL   Science 271 (5255), 1513-1518 (1996)
   PUBMED   8599106
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC401967.1, BC039257.1,
            BM478072.1, AI037962.1, BQ435836.1 and AC025449.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Nucleoporins are proteins that play an important role in
            the assembly and functioning of the nuclear pore complex (NPC)
            which regulates the movement of macromolecules across the nuclear
            envelope (NE). The protein encoded by this gene plays a role in the
            fusion of NE vesicles and formation of the double membrane NE. The
            protein may also be involved in cardiac physiology and may be
            associated with the pathogenesis of atrial fibrillation.
            Alternative splicing results in multiple transcript variants of
            this gene. A pseudogene associated with this gene is located on
            chromosome 6. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2671155.1, BC039257.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000231498.8/ ENSP00000231498.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..1391
                     /product="nuclear pore complex protein Nup155 isoform 1"
                     /note="nuclear pore complex protein Nup155; 155 kDa
                     nucleoporin; nucleoporin 155kD; nucleoporin 155kDa"
                     /calculated_mol_wt=155069
     Region          77..507
                     /region_name="Nucleoporin_N"
                     /note="Nup133 N terminal like; pfam08801"
                     /db_xref="CDD:400932"
     Region          89..1311
                     /region_name="NUP170"
                     /note="Nuclear pore complex subunit [Intracellular
                     trafficking and secretion]; COG5308"
                     /db_xref="CDD:227624"
     Site            526
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O75694.1)"
     Region          985..1012
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75694.1)"
     Site            1057
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75694.1)"
     CDS             1..1391
                     /gene="NUP155"
                     /gene_synonym="ATFB15; N155"
                     /coded_by="NM_153485.3:130..4305"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3921.1"
                     /db_xref="GeneID:9631"
                     /db_xref="HGNC:HGNC:8063"
                     /db_xref="MIM:606694"
ORIGIN      
        1 mpssllgaam pastsaaalq ealenagrli drqlqedrmy pdlsellmvs apnnptvsgm
       61 sdmdyplqgp gllsvpnlpe issirrvplp pelveqfghm qcncmmgvfp pisrawltid
      121 sdifmwnyed ggdlayfdgl setilavglv kpkagifqph vrhllvlatp vdivilglsy
      181 anlqtgsgvl ndslsggmql lpdplyslpt dntylltits tdngriflag kdgclyevay
      241 qaeagwfsqr crkinhskss lsflvpsllq ftfseddpil qiaidnsrni lytrsekgvi
      301 qvydlgqdgq gmsrvasvsq naivsaagni artidrsvfk pivqiavien sesldcqlla
      361 vthagvrlyf stcpfrqpla rpntltlvhv rlppgfsass tvekpskvhr alyskgillm
      421 aasenedndi lwcvnhdtfp fqkpmmetqm tagvdghswa lsaidelkvd kiitplnkdh
      481 ipitdspvvv qqhmlppkkf vllsaqgslm fhklrpvdql rhllvsnvgg dgeeierffk
      541 lhqedqacat clilacstaa cdrevsawat raffryggea qmrfpttlpp psnvgpilgs
      601 pvyssspvps gspypnpsfl gtpshgiqpp amstpvcalg npatqatnms cvtgpeivys
      661 gkhngiciyf srimgniwda slvverifks gnreitaies svpcqllesv lqelkglqef
      721 ldrnsqfagg plgnpnttak vqqrligfmr pengnpqqmq qelqrkfhea qlsekislqa
      781 iqqlvrksyq alalwkllce hqftiivael qkelqeqlki ttfkdlvird keltgalias
      841 lincyirdna avdgislhlq dicpllystd daicskanel lqrsrqvqnk tekermlres
      901 lkeyqkisnq vdlsnvcaqy rqvrfyegvv elsltaaekk dpqglglhfy khgepeediv
      961 glqafqerln sykcitdtlq elvnqskaap qspsvpkkpg ppvlssdpnm lsneeaghhf
     1021 eqmlklsqrs kdelfsialy nwliqvdlad kllqvaspfl ephlvrmakv dqnrvrymdl
     1081 lwryyeknrs fsnaarvlsr ladmhsteis lqqrleyiar ailsakssta issiaadgef
     1141 lheleekmev ariqlqiqet lqrqyshhss vqdavsqlds elmditklyg efadpfklae
     1201 cklaiihcag ysdpilvqtl wqdiiekels dsvtlsssdr mhalslkivl lgkiyagtpr
     1261 ffpldfivqf leqqvctlnw dvgfviqtmn eigvplprll evydqlfksr dpfwnrmkkp
     1321 lhlldcihvl liryvenpsq vlncerrrft nlcldavcgy lvelqsmsss vavqaitgnf
     1381 kslqaklerl h
//
LOCUS       NP_001310                415 aa            linear   PRI 27-APR-2025
DEFINITION  casein kinase I isoform gamma-2 [Homo sapiens].
ACCESSION   NP_001310
VERSION     NP_001310.3
DBSOURCE    REFSEQ: accession NM_001319.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Nguyen Hoang,A.T., Hoe,K.L. and Lee,S.J.
  TITLE     CSNK1G2 differently sensitizes tamoxifen-induced decrease in
            PI3K/AKT/mTOR/S6K and ERK signaling according to the estrogen
            receptor existence in breast cancer cells
  JOURNAL   PLoS One 16 (4), e0246264 (2021)
   PUBMED   33861751
  REMARK    GeneRIF: CSNK1G2 differently sensitizes tamoxifen-induced decrease
            in PI3K/AKT/mTOR/S6K and ERK signaling according to the estrogen
            receptor existence in breast cancer cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Li,X., Zhong,L., Wang,Z., Chen,H., Liao,D., Zhang,R., Zhang,H. and
            Kang,T.
  TITLE     Phosphorylation of IRS4 by CK1gamma2 promotes its degradation by
            CHIP through the ubiquitin/lysosome pathway
  JOURNAL   Theranostics 8 (13), 3643-3653 (2018)
   PUBMED   30026872
  REMARK    GeneRIF: IRS4, as a new substrate of CHIP, is negatively regulated
            by CK1gamma2 at the posttranslational level.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Zemlickova,E., Johannes,F.J., Aitken,A. and Dubois,T.
  TITLE     Association of CPI-17 with protein kinase C and casein kinase I
  JOURNAL   Biochem Biophys Res Commun 316 (1), 39-47 (2004)
   PUBMED   15003508
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Dubois,T., Howell,S., Zemlickova,E. and Aitken,A.
  TITLE     Identification of casein kinase Ialpha interacting protein partners
  JOURNAL   FEBS Lett 517 (1-3), 167-171 (2002)
   PUBMED   12062430
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Kitabayashi,A.N., Kusuda,J., Hirai,M. and Hashimoto,K.
  TITLE     Cloning and chromosomal mapping of human casein kinase I gamma 2
            (CSNK1G2)
  JOURNAL   Genomics 46 (1), 133-137 (1997)
   PUBMED   9403068
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Lussier,G. and Larose,L.
  TITLE     A casein kinase I activity is constitutively associated with Nck
  JOURNAL   J Biol Chem 272 (5), 2688-2694 (1997)
   PUBMED   9006905
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012615.4 and AC005306.2.
            
            On Jul 25, 2007 this sequence version replaced NP_001310.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.217532.1,
                                           SRR1163658.269787.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000255641.13/ ENSP00000255641.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..415
                     /product="casein kinase I isoform gamma-2"
                     /EC_number="2.7.11.1"
                     /note="CKI-gamma 2"
                     /calculated_mol_wt=47326
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78368.1)"
     Region          45..332
                     /region_name="STKc_CK1_gamma"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, Casein Kinase 1 gamma; cd14126"
                     /db_xref="CDD:271028"
     Site            order(52..58,60,73,75,119..123,125,127,165,167,169..170,
                     172,188,191,214..217)
                     /site_type="active"
                     /db_xref="CDD:271028"
     Site            order(52..58,60,73,75,119..123,167,169..170,172,188)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271028"
     Site            order(56,125,127,165,167,169,191,214..217)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271028"
     Site            187..217
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271028"
     Region          332..385
                     /region_name="CK1gamma_C"
                     /note="Casein kinase 1 gamma C terminal; pfam12605"
                     /db_xref="CDD:463640"
     Region          340..383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78368.1)"
     Region          369..415
                     /region_name="Phospho-regulated basic and hydrophobic
                     (PRBH) motif. /evidence=ECO:0000269|PubMed:26481050"
                     /note="propagated from UniProtKB/Swiss-Prot (P78368.1)"
     CDS             1..415
                     /gene="CSNK1G2"
                     /gene_synonym="CK1g2"
                     /coded_by="NM_001319.7:513..1760"
                     /db_xref="CCDS:CCDS12077.1"
                     /db_xref="GeneID:1455"
                     /db_xref="HGNC:HGNC:2455"
                     /db_xref="MIM:602214"
ORIGIN      
        1 mdfdkkggkg eteegrrmsk agggrsshgi rssgtssgvl mvgpnfrvgk kigcgnfgel
       61 rlgknlytne yvaiklepik srapqlhley rfykqlsate gvpqvyyfgp cgkynamvle
      121 llgpsledlf dlcdrtftlk tvlmiaiqli trmeyvhtks liyrdvkpen flvgrpgtkr
      181 qhaihiidfg lakeyidpet kkhipyrehk sltgtaryms inthlgkeqs rrddlealgh
      241 mfmyflrgsl pwqglkadtl keryqkigdt kratpievlc enfpeematy lryvrrldff
      301 ekpdydylrk lftdlfdrsg fvfdyeydwa gkplptpigt vhtdlpsqpq lrdktqphsk
      361 nqalnstnge lnaddptagh snapitapae vevadetkcc cffkrrkrks lqrhk
//
LOCUS       NP_001013828             541 aa            linear   ROD 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 13C isoform 1 [Mus
            musculus].
ACCESSION   NP_001013828 XP_485322
VERSION     NP_001013828.1
DBSOURCE    REFSEQ: accession NM_001013806.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Parent,A., Roy,S.J., Iorio-Morin,C., Lepine,M.C., Labrecque,P.,
            Gallant,M.A., Slipetz,D. and Parent,J.L.
  TITLE     ANKRD13C acts as a molecular chaperone for G protein-coupled
            receptors
  JOURNAL   J Biol Chem 285 (52), 40838-40851 (2010)
   PUBMED   20959461
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC117211.3, BC065088.1, BQ562764.1, CF736962.1, AC145301.4,
            AK135906.1 and AI835245.1.
            
            On Jun 19, 2005 this sequence version replaced XP_485322.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.16236.1,
                                           SRR7652917.682974.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3 81.59 cM"
     Protein         1..541
                     /product="ankyrin repeat domain-containing protein 13C
                     isoform 1"
                     /note="ankyrin repeat domain-containing protein 13C"
                     /calculated_mol_wt=60019
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UX43.2)"
     Region          111..142
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UX43.2)"
     Region          <115..>199
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          115..141
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(117..118,121..123,125..126,130,141,143,145,149..150,
                     153..155,157..158,162,165,174,176,178,182..183,186..188,
                     190..191,195,198)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          143..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          143..172
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UX43.2)"
     Region          176..205
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UX43.2)"
     Region          259..532
                     /region_name="GPCR_chapero_1"
                     /note="GPCR-chaperone; pfam11904"
                     /db_xref="CDD:463391"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3UX43.2)"
     CDS             1..541
                     /gene="Ankrd13c"
                     /coded_by="NM_001013806.2:528..2153"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS17933.1"
                     /db_xref="GeneID:433667"
                     /db_xref="MGI:MGI:2139746"
ORIGIN      
        1 mtgekirslr rdhkpskedg dvlepceeea taalggaftg grsgpggsgk ggkachkifs
       61 hhhrlqlkap avpgpgvpap pqhnavtatc papaclggsn palvadgggc pslypvhecv
      121 fkgdvrrlss lirthnigqk dnhgntplhl avmlgnkeca hlllahnapv kvknaqgwsp
      181 laeaisygdr qmitallrkl kqqsresvge krprllkalk elgdfylelh wdfqswvpll
      241 srilpsdack iykqginirl dttlidftdm kcqrgdlsfi fngdaapses fvvldneqkv
      301 yqrihheese meteeevdil mssdiysatl stksisftra qtgwlfredk tervgnflad
      361 fylvnglvle srkrrehlse edilrnkaim eslskggsla eqsfepvrrq sltpppqnti
      421 tweeyisaen gkaphlgrel vckeskktfk atvamsqefp lgiesllnvl eviapfkhfn
      481 klrefvqmkl ppgfpvkldi pvfptitatv tfqefrcdef dgsifaiped ykedpsrfpd
      541 l
//
LOCUS       NP_001186125             501 aa            linear   PRI 27-APR-2025
DEFINITION  armadillo repeat-containing protein 6 isoform 1 [Homo sapiens].
ACCESSION   NP_001186125
VERSION     NP_001186125.1
DBSOURCE    REFSEQ: accession NM_001199196.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Adamik,M., Soldanova,Z., Drotarova,M., Breckova,K., Petr,M.,
            Helma,R., Jenner,L.P., Vorlickova,M., Sykorova,E. and Brazdova,M.
  TITLE     Human ARMC6 binds in vitro to both cancer genes and telomeric RNA,
            favoring G-quadruplex structure recognition
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1867 (3), 195050 (2024)
   PUBMED   39029558
  REMARK    GeneRIF: Human ARMC6 binds in vitro to both cancer genes and
            telomeric RNA, favoring G-quadruplex structure recognition.
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Dokladal,L., Benkova,E., Honys,D., Duplakova,N., Lee,L.Y.,
            Gelvin,S.B. and Sykorova,E.
  TITLE     An armadillo-domain protein participates in a telomerase
            interaction network
  JOURNAL   Plant Mol Biol 97 (4-5), 407-420 (2018)
   PUBMED   29948659
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Gress,T.M., Muller-Pillasch,F., Geng,M., Zimmerhackl,F.,
            Zehetner,G., Friess,H., Buchler,M., Adler,G. and Lehrach,H.
  TITLE     A pancreatic cancer-specific expression profile
  JOURNAL   Oncogene 13 (8), 1819-1830 (1996)
   PUBMED   8895530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CX869901.1, BC067125.1 and
            BQ012036.1.
            
            Summary: The function of this gene's protein product has not been
            determined. A related protein in mouse suggests that this protein
            has a conserved function. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.100075.1,
                                           SRR1803613.286489.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000535612.6/ ENSP00000444156.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..501
                     /product="armadillo repeat-containing protein 6 isoform 1"
                     /note="armadillo repeat-containing protein 6"
                     /calculated_mol_wt=54011
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q6NXE6.2)"
     Region          171..205
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(195,200,204,240,244,248,294,298,302)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          209..251
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          213..251
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          220..264
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXE6.2)"
     Site            263
                     /site_type="methylation"
                     /note="Pros-methylhistidine.
                     /evidence=ECO:0000269|PubMed:33563959; propagated from
                     UniProtKB/Swiss-Prot (Q6NXE6.2)"
     Region          267..303
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          274..318
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXE6.2)"
     Region          313..354
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          319..369
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXE6.2)"
     Site            order(345,349,353,388,392,396,432,436,440)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          361..399
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          370..412
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXE6.2)"
     Region          406..441
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..501
                     /gene="ARMC6"
                     /gene_synonym="R30923_1"
                     /coded_by="NM_001199196.2:408..1913"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS56089.1"
                     /db_xref="GeneID:93436"
                     /db_xref="HGNC:HGNC:25049"
ORIGIN      
        1 mserccsrys sgasigctpt stqakmvskr iaqetfdaav renieefamg peeavkeave
       61 qfesqgvdls nivktapkvs adgsqepthd ilqmlsdlqe svassrpqev sayltrfcdq
      121 ckqdkacrfl aaqkgaypii ftawklatag dqglllqsln alsvltdgqp dlldaqglql
      181 lvatltqnad eadltcsgir cvrhaclkhe qnrqdlvkag vlplltgait hhghhtdvvr
      241 eacwalrvmt fdddirvpfg hahnhakmiv qenkglkvli eatkafldnp gilselcgtl
      301 srlairnefc qevvdlggls ilvslladcn dhqmrdqsgv qelvkqvlst lraiagnddv
      361 kdaivraggt esivaamtqh ltspqvceqs caalcflalr kpdnsriive gggavaalqa
      421 mkahpqkagv qkqacmlirn lvahgqafsk pildlgaeal imqarsahrd cedvakaalr
      481 dlgchvelre lwtgqrgnla p
//
LOCUS       NP_001278369             384 aa            linear   ROD 27-APR-2025
DEFINITION  DNA repair protein RAD51 homolog 3 isoform 1 [Mus musculus].
ACCESSION   NP_001278369
VERSION     NP_001278369.1
DBSOURCE    REFSEQ: accession NM_001291440.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Tomaszowski,K.H., Roy,S., Guerrero,C., Shukla,P., Keshvani,C.,
            Chen,Y., Ott,M., Wu,X., Zhang,J., DiNardo,C.D., Schindler,D. and
            Schlacher,K.
  TITLE     Hypomorphic Brca2 and Rad51c double mutant mice display Fanconi
            anemia, cancer and polygenic replication stress
  JOURNAL   Nat Commun 14 (1), 1333 (2023)
   PUBMED   36906610
  REMARK    GeneRIF: Hypomorphic Brca2 and Rad51c double mutant mice display
            Fanconi anemia, cancer and polygenic replication stress.
            Erratum:[Nat Commun. 2024 Mar 12;15(1):2214. doi:
            10.1038/s41467-024-46561-9. PMID: 38472265]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Rojas,E., Martinez-Pacheco,M., Rodriguez-Sastre,M.A.,
            Ramos-Espinosa,P. and Valverde,M.
  TITLE     Post-transcriptional regulation of Rad51c by miR-222 contributes
            cellular transformation
  JOURNAL   PLoS One 15 (1), e0221681 (2020)
   PUBMED   31923208
  REMARK    GeneRIF: we demonstrate that miR-222 up-regulation, directly
            regulates Rad51c expression negatively, and impairs homologous
            recombination of double-strand break DNA repair during the
            initiation stage of cell transformation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Tumiati,M., Munne,P.M., Edgren,H., Eldfors,S., Hemmes,A. and
            Kuznetsov,S.G.
  TITLE     Rad51c- and Trp53-double-mutant mouse model reveals common features
            of homologous recombination-deficient breast cancers
  JOURNAL   Oncogene 35 (35), 4601-4610 (2016)
   PUBMED   26820992
  REMARK    GeneRIF: Similar to other BC models, Rad51c/p53 double-mutant mouse
            mammary tumors also reveal a propensity for genomic instability,
            but lack the focal amplification of the Met locus or distinct
            mutational signatures reported for other HR genes
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Tumiati,M., Hemmes,A., Uusivirta,S., Koopal,S., Kankainen,M.,
            Lehtonen,E. and Kuznetsov,S.G.
  TITLE     Loss of Rad51c accelerates tumourigenesis in sebaceous glands of
            Trp53-mutant mice
  JOURNAL   J Pathol 235 (1), 136-146 (2015)
   PUBMED   25270124
  REMARK    GeneRIF: a critical synergy between Rad51c and Trp53 in tumour
            progression and provide a predictable in vivo model system for
            studying mechanisms of Rad51c-mediated carcinogenesis
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Badie,S., Escandell,J.M., Bouwman,P., Carlos,A.R., Thanasoula,M.,
            Gallardo,M.M., Suram,A., Jaco,I., Benitez,J., Herbig,U.,
            Blasco,M.A., Jonkers,J. and Tarsounas,M.
  TITLE     BRCA2 acts as a RAD51 loader to facilitate telomere replication and
            capping
  JOURNAL   Nat Struct Mol Biol 17 (12), 1461-1469 (2010)
   PUBMED   21076401
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Kuznetsov,S.G., Haines,D.C., Martin,B.K. and Sharan,S.K.
  TITLE     Loss of Rad51c leads to embryonic lethality and modulation of
            Trp53-dependent tumorigenesis in mice
  JOURNAL   Cancer Res 69 (3), 863-872 (2009)
   PUBMED   19155299
  REMARK    GeneRIF: Rad51c mutation in DH-cis mice promoted the development of
            tumors of specialized sebaceous glands and suppressed tumors
            characteristic of Trp53 mutation. In addition, DH-cis females
            developed tumors significantly earlier than any other group.
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Kuznetsov,S., Pellegrini,M., Shuda,K., Fernandez-Capetillo,O.,
            Liu,Y., Martin,B.K., Burkett,S., Southon,E., Pati,D.,
            Tessarollo,L., West,S.C., Donovan,P.J., Nussenzweig,A. and
            Sharan,S.K.
  TITLE     RAD51C deficiency in mice results in early prophase I arrest in
            males and sister chromatid separation at metaphase II in females
  JOURNAL   J Cell Biol 176 (5), 581-592 (2007)
   PUBMED   17312021
  REMARK    GeneRIF: RAD51C has a late role in meiotic recombination.
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Liu,Y., Tarsounas,M., O'regan,P. and West,S.C.
  TITLE     Role of RAD51C and XRCC3 in genetic recombination and DNA repair
  JOURNAL   J Biol Chem 282 (3), 1973-1979 (2007)
   PUBMED   17114795
  REMARK    GeneRIF: the RAD51C-XRCC3-associated Holliday junction resolvase
            complex associates with crossovers and may play an essential role
            in the resolution of recombination intermediates prior to
            chromosome segregation
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Godthelp,B.C., Wiegant,W.W., van Duijn-Goedhart,A., Scharer,O.D.,
            van Buul,P.P., Kanaar,R. and Zdzienicka,M.Z.
  TITLE     Mammalian Rad51C contributes to DNA cross-link resistance, sister
            chromatid cohesion and genomic stability
  JOURNAL   Nucleic Acids Res 30 (10), 2172-2182 (2002)
   PUBMED   12000837
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Leasure,C.S., Chandler,J., Gilbert,D.J., Householder,D.B.,
            Stephens,R., Copeland,N.G., Jenkins,N.A. and Sharan,S.K.
  TITLE     Sequence, chromosomal location and expression analysis of the
            murine homologue of human RAD51L2/RAD51C
  JOURNAL   Gene 271 (1), 59-67 (2001)
   PUBMED   11410366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL669902.8 and AL596130.13.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK076551.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 52.08 cM"
     Protein         1..384
                     /product="DNA repair protein RAD51 homolog 3 isoform 1"
                     /note="DNA repair protein RAD51 homolog 3; RAD51-like
                     protein 2; RAD51 homolog C"
                     /calculated_mol_wt=42907
     Region          127..339
                     /region_name="Rad51C"
                     /note="RAD51C recombinase; cd19492"
                     /db_xref="CDD:410900"
     Site            order(137..142,170,251,294,326)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:410900"
     CDS             1..384
                     /gene="Rad51c"
                     /gene_synonym="R51H3; Rad51l2"
                     /coded_by="NM_001291440.2:189..1343"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS79013.1"
                     /db_xref="GeneID:114714"
                     /db_xref="MGI:MGI:2150020"
ORIGIN      
        1 mlyrvhlawl psprlrplfl flcslsgyir nvtrtsetrr qpymkpvcgi ssaaarpqvg
       61 iskeealetl qilrrecltn kprcagtsva nekctalell eqehtqgfii tfcsaldnil
      121 gggiplmktt evcgvpgvgk tqlcmqlavd vqipecfggv ageavfidte gsfmvdrvvs
      181 lataciqhlh liagthteee hqkalkdftl enilshiyyf rchdytella qvyllpdfls
      241 dhpkvqlvii dgiafpfrhd ledlslrtrl lnglaqqmis lannhrlavi ltnqmttkid
      301 knqallvpal geswghaati rlifhweqkq rfatlyksps qkestipfqi tpqgfrdavv
      361 taassqtess lnfrkrsrep eeec
//
LOCUS       NP_001354560             179 aa            linear   MAM 27-APR-2025
DEFINITION  insulin-like growth factor 2 preproprotein [Bos taurus].
ACCESSION   NP_001354560 XP_005227331
VERSION     NP_001354560.1
DBSOURCE    REFSEQ: accession NM_001367631.1
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Willhelm,B.R., Ticiani,E., Campagnolo,K., Rodrigues,J.L.,
            Roberts,A.J., Anderson,G.B. and Bertolini,M.
  TITLE     Components of the insulin-like growth factor system in in vivo -
            and in vitro-derived fetuses of cattle, and the association with
            growth and development
  JOURNAL   Anim Reprod Sci 234, 106856 (2021)
   PUBMED   34626867
  REMARK    GeneRIF: Components of the insulin-like growth factor system in in
            vivo - and in vitro-derived fetuses of cattle, and the association
            with growth and development.
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Ghanipoor-Samami,M., Javadmanesh,A., Burns,B.M., Thomsen,D.A.,
            Nattrass,G.S., Estrella,C.A.S., Kind,K.L. and Hiendleder,S.
  TITLE     Atlas of tissue- and developmental stage specific gene expression
            for the bovine insulin-like growth factor (IGF) system
  JOURNAL   PLoS One 13 (7), e0200466 (2018)
   PUBMED   30001361
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Bouwman,A.C., Daetwyler,H.D., Chamberlain,A.J., Ponce,C.H.,
            Sargolzaei,M., Schenkel,F.S., Sahana,G., Govignon-Gion,A.,
            Boitard,S., Dolezal,M., Pausch,H., Brondum,R.F., Bowman,P.J.,
            Thomsen,B., Guldbrandtsen,B., Lund,M.S., Servin,B., Garrick,D.J.,
            Reecy,J., Vilkki,J., Bagnato,A., Wang,M., Hoff,J.L., Schnabel,R.D.,
            Taylor,J.F., Vinkhuyzen,A.A.E., Panitz,F., Bendixen,C., Holm,L.E.,
            Gredler,B., Hoze,C., Boussaha,M., Sanchez,M.P., Rocha,D.,
            Capitan,A., Tribout,T., Barbat,A., Croiseau,P., Drogemuller,C.,
            Jagannathan,V., Vander Jagt,C., Crowley,J.J., Bieber,A.,
            Purfield,D.C., Berry,D.P., Emmerling,R., Gotz,K.U.,
            Frischknecht,M., Russ,I., Solkner,J., Van Tassell,C.P., Fries,R.,
            Stothard,P., Veerkamp,R.F., Boichard,D., Goddard,M.E. and
            Hayes,B.J.
  TITLE     Meta-analysis of genome-wide association studies for cattle stature
            identifies common genes that regulate body size in mammals
  JOURNAL   Nat Genet 50 (3), 362-367 (2018)
   PUBMED   29459679
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Su,J., Wang,Y., Xing,X., Zhang,L., Sun,H. and Zhang,Y.
  TITLE     Melatonin significantly improves the developmental competence of
            bovine somatic cell nuclear transfer embryos
  JOURNAL   J Pineal Res 59 (4), 455-468 (2015)
   PUBMED   26331949
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Mendonca Ados,S., Guimaraes,A.L., da Silva,N.M., Caetano,A.R.,
            Dode,M.A. and Franco,M.M.
  TITLE     Characterization of the IGF2 Imprinted Gene Methylation Status in
            Bovine Oocytes during Folliculogenesis
  JOURNAL   PLoS One 10 (10), e0142072 (2015)
   PUBMED   26517264
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Congote,L.F., Mazza,L. and Palfree,R.G.
  TITLE     Nucleotide sequence of the central coding region of bovine
            erythrotropin/insulin-like growth factor II cDNA from fetal
            intestine and northern analysis of the major IGF II transcripts at
            the time of hepatic erythropoiesis
  JOURNAL   Comp Biochem Physiol B 103 (1), 127-131 (1992)
   PUBMED   1280544
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Brown,W.M., Dziegielewska,K.M., Foreman,R.C. and Saunders,N.R.
  TITLE     The nucleotide and deduced amino acid sequences of insulin-like
            growth factor II cDNAs from adult bovine and fetal sheep liver
  JOURNAL   Nucleic Acids Res 18 (15), 4614 (1990)
   PUBMED   2388846
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Li,Q.G., Blacher,R., Esch,F. and Congote,L.F.
  TITLE     A heparin-binding erythroid cell stimulating factor from fetal
            bovine serum has the N-terminal sequence of insulin-like growth
            factor II
  JOURNAL   Biochem Biophys Res Commun 166 (2), 557-561 (1990)
   PUBMED   2302223
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Francis,G.L., Upton,F.M., Ballard,F.J., McNeil,K.A. and
            Wallace,J.C.
  TITLE     Insulin-like growth factors 1 and 2 in bovine colostrum. Sequences
            and biological activities compared with those of a potent truncated
            form
  JOURNAL   Biochem J 251 (1), 95-103 (1988)
   PUBMED   3390164
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Honegger,A. and Humbel,R.E.
  TITLE     Insulin-like growth factors I and II in fetal and adult bovine
            serum. Purification, primary structures, and immunological
            cross-reactivities
  JOURNAL   J Biol Chem 261 (2), 569-575 (1986)
   PUBMED   3941093
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC116039.1 and NKLS02000029.1.
            
            On Dec 12, 2018 this sequence version replaced XP_005227331.1.
            
            Summary: This gene encodes a member of the insulin family of
            protein growth factors, which are involved in fetal development and
            growth. It is an imprinted gene that is expressed from the paternal
            allele while the maternal allele is silenced. The encoded protein
            is proteolytically processed to generate the mature peptide
            hormone, which binds to receptors of the insulin receptor family.
            This peptide plays a role in oocyte development and
            folliculogenesis in female cattle. Polymorphisms in this gene may
            be associated with cattle body mass. [provided by RefSeq, Dec
            2018].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC116039.1, SRR5571262.20864.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA6648759, SAMEA6648763
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="29"
                     /map="29"
                     /breed="L1 Hereford"
     Protein         1..179
                     /product="insulin-like growth factor 2 preproprotein"
                     /note="insulin-like growth factor II; IGF-II;
                     erythrotropin; insulin-like growth factor 2 (somatomedin
                     A)"
                     /calculated_mol_wt=17250
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2450
     mat_peptide     25..91
                     /product="Insulin-like growth factor 2.
                     /id=PRO_0000015711"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
                     /calculated_mol_wt=7533
     Region          25..52
                     /region_name="B"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Region          28..91
                     /region_name="IlGF"
                     /note="insulin_like growth factors; specific to
                     vertebrates. Members include a number of peptides
                     including insulin-like growth factors I and II, which play
                     a variety of roles in controlling processes such as
                     growth, differentiation, and reproduction. On a...;
                     cd04368"
                     /db_xref="CDD:239834"
     Site            order(30,39,47..51)
                     /site_type="active"
                     /note="IGFBP binding surface [active]"
                     /db_xref="CDD:239834"
     Site            order(48,50..51,67)
                     /site_type="active"
                     /note="type 1 IGF- and insulin-receptor binding surface
                     [active]"
                     /db_xref="CDD:239834"
     Site            48
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          53..64
                     /region_name="C"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Site            58
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Site            61
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Site            62
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P01344; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          65..85
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Site            order(72..74,78..79)
                     /site_type="active"
                     /note="type 2 IGF-receptor binding surface [active]"
                     /db_xref="CDD:239834"
     Region          86..91
                     /region_name="D"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     mat_peptide     93..126
                     /product="Preptin. /id=PRO_0000370373"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
                     /calculated_mol_wt=3877
     Site            106
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19674964; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          112..166
                     /region_name="IGF2_C"
                     /note="Insulin-like growth factor II E-peptide; pfam08365"
                     /db_xref="CDD:462445"
     Site            154
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:19674964; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     Region          160..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07456.4)"
     Site            163
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19674964; propagated from
                     UniProtKB/Swiss-Prot (P07456.4)"
     CDS             1..179
                     /gene="IGF2"
                     /coded_by="NM_001367631.1:591..1130"
                     /db_xref="BGD:BT11333"
                     /db_xref="GeneID:281240"
                     /db_xref="VGNC:VGNC:30078"
ORIGIN      
        1 mgitagksvl vllaflafas ccyaayrpse tlcggelvdt lqfvcgdrgf yfsrpssrin
       61 rrsrgiveec cfrscdlall etycatpaks erdvsasttv lpddvtaypv gkffqydiwk
      121 qstqrlrrgl paflrarrgr tlakelealr eakshrplia lptqdpathg gasskassd
//
LOCUS       NP_001495                368 aa            linear   PRI 27-APR-2025
DEFINITION  C-X-C chemokine receptor type 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001495
VERSION     NP_001495.1
DBSOURCE    REFSEQ: accession NM_001504.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wang,F., Guo,B., Jia,Z., Jing,Z., Wang,Q., Li,M., Lu,B., Liang,W.,
            Hu,W. and Fu,X.
  TITLE     The Role of CXCR3 in Nervous System-Related Diseases
  JOURNAL   Mediators Inflamm 2024, 8347647 (2024)
   PUBMED   39429695
  REMARK    GeneRIF: The Role of CXCR3 in Nervous System-Related Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Wang,K., Wu,J., Yang,Z., Zheng,B., Shen,S., Wang,R.R., Zhang,Y.,
            Wang,H.Y., Chen,L. and Qiu,X.
  TITLE     Hyperactivation of beta-catenin signal in hepatocellular carcinoma
            recruits myeloid-derived suppressor cells through PF4-CXCR3 axis
  JOURNAL   Cancer Lett 586, 216690 (2024)
   PUBMED   38307410
  REMARK    GeneRIF: Hyperactivation of beta-catenin signal in hepatocellular
            carcinoma recruits myeloid-derived suppressor cells through
            PF4-CXCR3 axis.
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Liu,H., Wang,Y., Le,Q., Tong,J. and Wang,H.
  TITLE     The IFN-gamma-CXCL9/CXCL10-CXCR3 axis in vitiligo: Pathological
            mechanism and treatment
  JOURNAL   Eur J Immunol 54 (4), e2250281 (2024)
   PUBMED   37937817
  REMARK    GeneRIF: The IFN-gamma-CXCL9/CXCL10-CXCR3 axis in vitiligo:
            Pathological mechanism and treatment.
            Review article
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Hosaka,S., Imagawa,K., Yano,Y., Lin,L., Shiono,J.,
            Takahashi-Igari,M., Hara,H., Hayashi,D., Imai,H., Morita,A.,
            Fukushima,H. and Takada,H.
  TITLE     The CXCL10-CXCR3 axis plays an important role in Kawasaki disease
  JOURNAL   Clin Exp Immunol 216 (1), 104-111 (2024)
   PUBMED   37952216
  REMARK    GeneRIF: The CXCL10-CXCR3 axis plays an important role in Kawasaki
            disease.
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Shamsi,A., Roghani,S.A., Abdan,Z., Soufivand,P., Pournazari,M.,
            Bahrehmand,F., Vafaei,A., Salari,N., Soroush,M.G. and Taghadosi,M.
  TITLE     CXCL9 and its Receptor CXCR3, an Important Link Between
            Inflammation and Cardiovascular Risks in RA Patients
  JOURNAL   Inflammation 46 (6), 2374-2385 (2023)
   PUBMED   37542661
  REMARK    GeneRIF: CXCL9 and its Receptor CXCR3, an Important Link Between
            Inflammation and Cardiovascular Risks in RA Patients.
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Qin,S., Rottman,J.B., Myers,P., Kassam,N., Weinblatt,M.,
            Loetscher,M., Koch,A.E., Moser,B. and Mackay,C.R.
  TITLE     The chemokine receptors CXCR3 and CCR5 mark subsets of T cells
            associated with certain inflammatory reactions
  JOURNAL   J Clin Invest 101 (4), 746-754 (1998)
   PUBMED   9466968
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Bonecchi,R., Bianchi,G., Bordignon,P.P., D'Ambrosio,D., Lang,R.,
            Borsatti,A., Sozzani,S., Allavena,P., Gray,P.A., Mantovani,A. and
            Sinigaglia,F.
  TITLE     Differential expression of chemokine receptors and chemotactic
            responsiveness of type 1 T helper cells (Th1s) and Th2s
  JOURNAL   J Exp Med 187 (1), 129-134 (1998)
   PUBMED   9419219
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Loetscher,M., Gerber,B., Loetscher,P., Jones,S.A., Piali,L.,
            Clark-Lewis,I., Baggiolini,M. and Moser,B.
  TITLE     Chemokine receptor specific for IP10 and mig: structure, function,
            and expression in activated T-lymphocytes
  JOURNAL   J Exp Med 184 (3), 963-969 (1996)
   PUBMED   9064356
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Marchese,A., Heiber,M., Nguyen,T., Heng,H.H., Saldivia,V.R.,
            Cheng,R., Murphy,P.M., Tsui,L.C., Shi,X., Gregor,P. et al.
  TITLE     Cloning and chromosomal mapping of three novel genes, GPR9, GPR10,
            and GPR14, encoding receptors related to interleukin 8,
            neuropeptide Y, and somatostatin receptors
  JOURNAL   Genomics 29 (2), 335-344 (1995)
   PUBMED   8666380
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Itoh,H., Toyama,R., Kozasa,T., Tsukamoto,T., Matsuoka,M. and
            Kaziro,Y.
  TITLE     Presence of three distinct molecular species of Gi protein alpha
            subunit. Structure of rat cDNAs and human genomic DNAs
  JOURNAL   J Biol Chem 263 (14), 6656-6664 (1988)
   PUBMED   2834384
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X95876.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a G protein-coupled receptor with
            selectivity for three chemokines, termed CXCL9/Mig (monokine
            induced by interferon-g), CXCL10/IP10 (interferon-g-inducible 10
            kDa protein) and CXCL11/I-TAC (interferon-inducible T cell
            a-chemoattractant). Binding of chemokines to this protein induces
            cellular responses that are involved in leukocyte traffic, most
            notably integrin activation, cytoskeletal changes and chemotactic
            migration. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. One of the
            isoforms (CXCR3-B) shows high affinity binding to chemokine,
            CXCL4/PF4 (PMID:12782716). [provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes isoform 1 (also known as CXCR3-A). This
            isoform functions as a receptor for chemokines CXCL9/Mig,
            CXCL10/IP-10, and CXCL11/I-TAC (PMID:12782716).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.105067.1, X95876.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373693.4/ ENSP00000362797.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..368
                     /product="C-X-C chemokine receptor type 3 isoform 1"
                     /note="Mig receptor; G protein-coupled receptor 9; C-X-C
                     chemokine receptor type 3; IP-10 receptor; chemokine
                     (C-X-C motif) receptor 3; interferon-inducible protein 10
                     receptor; chemokine receptor 3"
                     /calculated_mol_wt=40529
     Site            22
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49682.2)"
     Site            27
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000269|PubMed:16847335,
                     ECO:0000269|PubMed:19151743; propagated from
                     UniProtKB/Swiss-Prot (P49682.2)"
     Site            29
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000269|PubMed:19151743; propagated from
                     UniProtKB/Swiss-Prot (P49682.2)"
     Site            32
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49682.2)"
     Region          54..329
                     /region_name="7tmA_CXCR3"
                     /note="CXC chemokine receptor type 3, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15180"
                     /db_xref="CDD:341335"
     Region          54..81
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341335"
     Site            54..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49682.2)"
     Site            order(60,109,112,128,131..132,203..208,212,215..216,271,
                     278,281,293,297,300..301,304)
                     /site_type="other"
                     /note="putative chemokine binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341335"
     Region          88..113
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341335"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49682.2)"
     Region          124..154
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341335"
     Site            126..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49682.2)"
     Region          166..188
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341335"
     Site            170..189
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49682.2)"
     Region          212..241
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341335"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49682.2)"
     Region          248..278
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341335"
     Site            256..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49682.2)"
     Region          297..322
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341335"
     Site            299..321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49682.2)"
     Region          342..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49682.2)"
     CDS             1..368
                     /gene="CXCR3"
                     /gene_synonym="CD182; CD183; CKR-L2; CMKAR3; GPR9; IP10-R;
                     Mig-R; MigR"
                     /coded_by="NM_001504.2:63..1169"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14416.1"
                     /db_xref="GeneID:2833"
                     /db_xref="HGNC:HGNC:4540"
                     /db_xref="MIM:300574"
ORIGIN      
        1 mvlevsdhqv lndaevaall enfsssydyg enesdsccts ppcpqdfsln fdraflpaly
       61 sllfllgllg ngavaavlls rrtalsstdt fllhlavadt llvltlplwa vdaavqwvfg
      121 sglckvagal fninfyagal llacisfdry lnivhatqly rrgpparvtl tclavwglcl
      181 lfalpdfifl sahhderlna thcqynfpqv grtalrvlql vagfllpllv maycyahila
      241 vllvsrgqrr lramrlvvvv vvafalcwtp yhlvvlvdil mdlgalarnc gresrvdvak
      301 svtsglgymh cclnpllyaf vgvkfrermw mlllrlgcpn qrglqrqpss srrdsswset
      361 seasysgl
//
LOCUS       NP_005554                149 aa            linear   PRI 27-APR-2025
DEFINITION  stathmin isoform a [Homo sapiens].
ACCESSION   NP_005554 XP_005245928
VERSION     NP_005554.1
DBSOURCE    REFSEQ: accession NM_005563.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Aksoy,A., Varoglu,A., Onalan,E.E., Tektemur,A., Artas,G., Koc,M.,
            Cakmak,M., Aydin,S., Kilic,M. and Ulas,M.
  TITLE     The knockdown of stathmin with si-RNA inhibits invasion of
            mesothelioma
  JOURNAL   Tissue Cell 87, 102303 (2024)
   PUBMED   38244401
  REMARK    GeneRIF: The knockdown of stathmin with si-RNA inhibits invasion of
            mesothelioma.
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Wang,L., Cao,J., Tao,J. and Liang,Y.
  TITLE     STMN1 promotes cell malignancy and bortezomib resistance of
            multiple myeloma cell lines via PI3K/AKT signaling
  JOURNAL   Expert Opin Drug Saf 23 (3), 277-286 (2024)
   PUBMED   37642368
  REMARK    GeneRIF: STMN1 promotes cell malignancy and bortezomib resistance
            of multiple myeloma cell lines via PI3K/AKT signaling.
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Handa,T., Yokobori,T., Obayashi,S., Fujii,T., Shirabe,K. and
            Oyama,T.
  TITLE     Association Between High Expression of Phosphorylated-STMN1 and
            Mesenchymal Marker Expression and Cancer Stemness in Breast Cancer
  JOURNAL   Anticancer Res 43 (12), 5341-5348 (2023)
   PUBMED   38030185
  REMARK    GeneRIF: Association Between High Expression of
            Phosphorylated-STMN1 and Mesenchymal Marker Expression and Cancer
            Stemness in Breast Cancer.
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Lombardo,C., Broggi,G., Vitale,E., Ledda,C., Loreto,C., Matera,S.,
            Hagnas,M., Caltabiano,R. and Filetti,V.
  TITLE     Expression of stathmin in asbestos-like fibers-induced
            mesothelioma: A preliminary report
  JOURNAL   Histol Histopathol 38 (11), 1249-1256 (2023)
   PUBMED   37466108
  REMARK    GeneRIF: Expression of stathmin in asbestos-like fibers-induced
            mesothelioma: A preliminary report.
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Ozge,Z., Sevil,K., Ahmet,Y., Hulya,A. and Sema,A.
  TITLE     Stathmin 1 and p53 Expression in Cutaneous Squamous Cell Carcinoma
            and Precursor Lesions
  JOURNAL   Am J Dermatopathol 45 (3), 170-175 (2023)
   PUBMED   36749137
  REMARK    GeneRIF: Stathmin 1 and p53 Expression in Cutaneous Squamous Cell
            Carcinoma and Precursor Lesions.
REFERENCE   6  (residues 1 to 149)
  AUTHORS   Doye,V., Le Gouvello,S., Dobransky,T., Chneiweiss,H., Beretta,L.
            and Sobel,A.
  TITLE     Expression of transfected stathmin cDNA reveals novel
            phosphorylated forms associated with developmental and functional
            cell regulation
  JOURNAL   Biochem J 287 (Pt 2) (Pt 2), 549-554 (1992)
   PUBMED   1445213
REFERENCE   7  (residues 1 to 149)
  AUTHORS   Labdon,J.E., Nieves,E. and Schubart,U.K.
  TITLE     Analysis of phosphoprotein p19 by liquid chromatography/mass
            spectrometry. Identification of two proline-directed serine
            phosphorylation sites and a blocked amino terminus
  JOURNAL   J Biol Chem 267 (5), 3506-3513 (1992)
   PUBMED   1737801
REFERENCE   8  (residues 1 to 149)
  AUTHORS   Melhem,R.F., Zhu,X.X., Hailat,N., Strahler,J.R. and Hanash,S.M.
  TITLE     Characterization of the gene for a proliferation-related
            phosphoprotein (oncoprotein 18) expressed in high amounts in acute
            leukemia
  JOURNAL   J Biol Chem 266 (27), 17747-17753 (1991)
   PUBMED   1917919
REFERENCE   9  (residues 1 to 149)
  AUTHORS   Sobel,A.
  TITLE     Stathmin: a relay phosphoprotein for multiple signal transduction?
  JOURNAL   Trends Biochem Sci 16 (8), 301-305 (1991)
   PUBMED   1957351
  REMARK    Review article
REFERENCE   10 (residues 1 to 149)
  AUTHORS   Ferrari,A.C., Seuanez,H.N., Hanash,S.M. and Atweh,G.F.
  TITLE     A gene that encodes for a leukemia-associated phosphoprotein (p18)
            maps to chromosome bands 1p35-36.1
  JOURNAL   Genes Chromosomes Cancer 2 (2), 125-129 (1990)
   PUBMED   2278968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG030679.1, AK054594.1 and
            BQ772197.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005245928.1.
            
            Summary: This gene belongs to the stathmin family of genes. It
            encodes a ubiquitous cytosolic phosphoprotein proposed to function
            as an intracellular relay integrating regulatory signals of the
            cellular environment. The encoded protein is involved in the
            regulation of the microtubule filament system by destabilizing
            microtubules. It prevents assembly and promotes disassembly of
            microtubules. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Feb
            2009].
            
            Transcript Variant: This variant (3) uses an alternate terminal
            exon, compared to variant 4. The resulting isoform (a) has a
            shorter and distinct C-terminus, compared to isoform b. Variants 1,
            2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.230008.1,
                                           SRR3476690.775749.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000455785.7/ ENSP00000387858.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..149
                     /product="stathmin isoform a"
                     /note="stathmin 1/oncoprotein 18; metablastin; prosolin;
                     phosphoprotein 19; transmembrane protein C1orf215;
                     leukemia-associated phosphoprotein p18; phosphoprotein
                     p19; testicular tissue protein Li 189"
                     /calculated_mol_wt=17171
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:1737801,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P16949.3)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16949.3)"
     Region          5..139
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P16949.3)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8125092,
                     ECO:0000269|PubMed:8245003, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16949.3)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1, MAPK1 and MAPK3.
                     /evidence=ECO:0000269|PubMed:1737801,
                     ECO:0000269|PubMed:8125092, ECO:0000269|PubMed:8245003,
                     ECO:0000269|PubMed:8325880, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P16949.3)"
     Site            29
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P16949.3)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16949.3)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1, MAPK1 and MAPK3.
                     /evidence=ECO:0000269|PubMed:1737801,
                     ECO:0000269|PubMed:8125092, ECO:0000269|PubMed:8245003,
                     ECO:0000269|PubMed:8325880, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P16949.3)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P16949.3)"
     Site            100
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P16949.3)"
     Site            119
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P16949.3)"
     Region          121..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16949.3)"
     CDS             1..149
                     /gene="STMN1"
                     /gene_synonym="C1orf215; Lag; LAP18; OP18; PP17; PP19;
                     PR22; SMN"
                     /coded_by="NM_005563.4:94..543"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS269.1"
                     /db_xref="GeneID:3925"
                     /db_xref="HGNC:HGNC:6510"
                     /db_xref="MIM:151442"
ORIGIN      
        1 massdiqvke lekrasgqaf elilsprske svpefplspp kkkdlsleei qkkleaaeer
       61 rksheaevlk qlaekrehek evlqkaieen nnfskmaeek lthkmeanke nreaqmaakl
      121 erlrekdkhi eevrknkesk dpadetead
//
LOCUS       NP_001353440             477 aa            linear   PRI 27-APR-2025
DEFINITION  repulsive guidance molecule B isoform 3 [Homo sapiens].
ACCESSION   NP_001353440 XP_005272023
VERSION     NP_001353440.1
DBSOURCE    REFSEQ: accession NM_001366511.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Novak,R., Ahmad,Y.A., Timaner,M., Bitman-Lotan,E.,
            Oknin-Vaisman,A., Horwitz,R., Hartmann,O., Reissland,M., Buck,V.,
            Rosenfeldt,M., Nikomarov,D., Diefenbacher,M.E., Shaked,Y. and
            Orian,A.
  TITLE     RNF4 RGMb BMP6 axis required for osteogenic differentiation and
            cancer cell survival
  JOURNAL   Cell Death Dis 13 (9), 820 (2022)
   PUBMED   36153321
  REMARK    GeneRIF: RNF4~RGMb~BMP6 axis required for osteogenic
            differentiation and cancer cell survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Malinauskas,T., Peer,T.V., Bishop,B., Mueller,T.D. and Siebold,C.
  TITLE     Repulsive guidance molecules lock growth differentiation factor 5
            in an inhibitory complex
  JOURNAL   Proc Natl Acad Sci U S A 117 (27), 15620-15631 (2020)
   PUBMED   32576689
  REMARK    GeneRIF: Repulsive guidance molecules lock growth differentiation
            factor 5 in an inhibitory complex.
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Sekiya,T. and Takaki,S.
  TITLE     RGMB enhances the suppressive activity of the monomeric secreted
            form of CTLA-4
  JOURNAL   Sci Rep 9 (1), 6984 (2019)
   PUBMED   31061392
  REMARK    GeneRIF: RGMB enhances the suppressive activity of the monomeric
            secreted form of CTLA-4.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Li,J., Ye,L., Shi,X., Chen,J., Feng,F., Chen,Y., Xiao,Y., Shen,J.,
            Li,P., Jiang,W.G. and He,J.
  TITLE     Repulsive guidance molecule B inhibits metastasis and is associated
            with decreased mortality in non-small cell lung cancer
  JOURNAL   Oncotarget 7 (13), 15678-15689 (2016)
   PUBMED   26910889
  REMARK    GeneRIF: Our results demonstrate that RGMB is an important
            inhibitor of non-small cell lung cancer metastasis and that low
            RGMB expression is a novel predictor or a poor prognosis.
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Li,P., Li,J., Yang,R., Zhang,F., Wang,H., Chu,H., Lu,Y., Dun,S.,
            Wang,Y., Zang,W., Du,Y., Chen,X., Zhao,G. and Zhang,G.
  TITLE     Study on expression of lncRNA RGMB-AS1 and repulsive guidance
            molecule b in non-small cell lung cancer
  JOURNAL   Diagn Pathol 10, 63 (2015)
   PUBMED   26055877
  REMARK    GeneRIF: RGMB was down-regulation in non-small cell lung cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 477)
  AUTHORS   Li,J., Ye,L., Mansel,R.E. and Jiang,W.G.
  TITLE     Potential prognostic value of repulsive guidance molecules in
            breast cancer
  JOURNAL   Anticancer Res 31 (5), 1703-1711 (2011)
   PUBMED   21617229
  REMARK    GeneRIF: Reduced expression of RGMB in breast cancer was associated
            with breast cancer.
REFERENCE   7  (residues 1 to 477)
  AUTHORS   Salyakina,D., Ma,D.Q., Jaworski,J.M., Konidari,I., Whitehead,P.L.,
            Henson,R., Martinez,D., Robinson,J.L., Sacharow,S., Wright,H.H.,
            Abramson,R.K., Gilbert,J.R., Cuccaro,M.L. and Pericak-Vance,M.A.
  TITLE     Variants in several genomic regions associated with asperger
            disorder
  JOURNAL   Autism Res 3 (6), 303-310 (2010)
   PUBMED   21182207
REFERENCE   8  (residues 1 to 477)
  AUTHORS   Liu,X., Hashimoto,M., Horii,H., Yamaguchi,A., Naito,K. and
            Yamashita,T.
  TITLE     Repulsive guidance molecule b inhibits neurite growth and is
            increased after spinal cord injury
  JOURNAL   Biochem Biophys Res Commun 382 (4), 795-800 (2009)
   PUBMED   19324014
REFERENCE   9  (residues 1 to 477)
  AUTHORS   Samad,T.A., Rebbapragada,A., Bell,E., Zhang,Y., Sidis,Y.,
            Jeong,S.J., Campagna,J.A., Perusini,S., Fabrizio,D.A.,
            Schneyer,A.L., Lin,H.Y., Brivanlou,A.H., Attisano,L. and Woolf,C.J.
  TITLE     DRAGON, a bone morphogenetic protein co-receptor
  JOURNAL   J Biol Chem 280 (14), 14122-14129 (2005)
   PUBMED   15671031
REFERENCE   10 (residues 1 to 477)
  AUTHORS   Samad,T.A., Srinivasan,A., Karchewski,L.A., Jeong,S.J.,
            Campagna,J.A., Ji,R.R., Fabrizio,D.A., Zhang,Y., Lin,H.Y., Bell,E.
            and Woolf,C.J.
  TITLE     DRAGON: a member of the repulsive guidance molecule-related family
            of neuronal- and muscle-expressed membrane proteins is regulated by
            DRG11 and has neuronal adhesive properties
  JOURNAL   J Neurosci 24 (8), 2027-2036 (2004)
   PUBMED   14985445
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008522.6.
            
            On Oct 10, 2018 this sequence version replaced XP_005272023.1.
            
            Summary: RGMB is a glycosylphosphatidylinositol (GPI)-anchored
            member of the repulsive guidance molecule family (see RGMA, MIM
            607362) and contributes to the patterning of the developing nervous
            system (Samad et al., 2005 [PubMed 15671031]).[supplied by OMIM,
            Apr 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.137714.1,
                                           SRR1803616.49600.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q15"
     Protein         1..477
                     /product="repulsive guidance molecule B isoform 3"
                     /note="repulsive guidance molecule B; DRG11-responsive
                     axonal guidance and outgrowth of neurite; RGM domain
                     family, member B; repulsive guidance molecule family
                     member b"
                     /calculated_mol_wt=51656
     Region          94..261
                     /region_name="RGM_N"
                     /note="Repulsive guidance molecule (RGM) N-terminus;
                     pfam06535"
                     /db_xref="CDD:461940"
     Region          266..440
                     /region_name="RGM_C"
                     /note="Repulsive guidance molecule (RGM) C-terminus;
                     pfam06534"
                     /db_xref="CDD:461939"
     CDS             1..477
                     /gene="RGMB"
                     /gene_synonym="DRAGON"
                     /coded_by="NM_001366511.1:262..1695"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:285704"
                     /db_xref="HGNC:HGNC:26896"
                     /db_xref="MIM:612687"
ORIGIN      
        1 mmkkrkrsap pgpcrshgpr patapappps peptrpawtg mglraapssa aaaaaeveqr
       61 rspglcpppl ellllllfsl gllhagdcqq paqcriqkct tdfvsltshl nsavdgfdse
      121 fckalrayag ctqrtskacr gnlvyhsavl gisdlmsqrn cskdgptsst npevthdpcn
      181 yhshagareh rrgdqnppsy lfcglfgdph lrtfkdnfqt ckvegawpli dnnylsvqvt
      241 nvpvvpgssa tatnkitiif kahhectdqk vyqavtddlp aafvdgttsg gdsdakslri
      301 veresghyve mharyigttv fvrqvgrylt lairmpedla msyeesqdlq lcvngcplse
      361 riddgqgqvs ailghslprt slvqawpgyt letantqche kmpvkdiyfq scvfdllttg
      421 danftaaahs aledvealhp rkerwhifps sgngtprggs dlsvslgltc lilivfl
//
LOCUS       NP_065899               1359 aa            linear   PRI 27-APR-2025
DEFINITION  junctional cadherin 5-associated protein isoform 1 [Homo sapiens].
ACCESSION   NP_065899 XP_166132 XP_934405 XP_945904 XP_949912
VERSION     NP_065899.1
DBSOURCE    REFSEQ: accession NM_020848.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1359)
  AUTHORS   Xie,L., Chen,H., Zhang,L., Ma,Y., Zhou,Y., Yang,Y.Y., Liu,C.,
            Wang,Y.L., Yan,Y.J., Ding,J., Teng,X., Yang,Q., Liu,X.P. and Wu,J.
  TITLE     JCAD deficiency attenuates activation of hepatic stellate cells and
            cholestatic fibrosis
  JOURNAL   Clin Mol Hepatol 30 (2), 206-224 (2024)
   PUBMED   38190829
  REMARK    GeneRIF: JCAD deficiency attenuates activation of hepatic stellate
            cells and cholestatic fibrosis.
REFERENCE   2  (residues 1 to 1359)
  AUTHORS   Liberale,L., Puspitasari,Y.M., Ministrini,S., Akhmedov,A.,
            Kraler,S., Bonetti,N.R., Beer,G., Vukolic,A., Bongiovanni,D.,
            Han,J., Kirmes,K., Bernlochner,I., Pelisek,J., Beer,J.H., Jin,Z.G.,
            Pedicino,D., Liuzzo,G., Stellos,K., Montecucco,F., Crea,F.,
            Luscher,T.F. and Camici,G.G.
  TITLE     JCAD promotes arterial thrombosis through PI3K/Akt modulation: a
            translational study
  JOURNAL   Eur Heart J 44 (20), 1818-1833 (2023)
   PUBMED   36469488
  REMARK    GeneRIF: JCAD promotes arterial thrombosis through PI3K/Akt
            modulation: a translational study.
            Erratum:[Eur Heart J. 2023 May 21;44(20):1843. doi:
            10.1093/eurheartj/ehad174. PMID: 37171028]
REFERENCE   3  (residues 1 to 1359)
  AUTHORS   Douglas,G., Mehta,V., Al Haj Zen,A., Akoumianakis,I., Goel,A.,
            Rashbrook,V.S., Trelfa,L., Donovan,L., Drydale,E., Chuaiphichai,S.,
            Antoniades,C., Watkins,H., Kyriakou,T., Tzima,E. and Channon,K.M.
  TITLE     A key role for the novel coronary artery disease gene JCAD in
            atherosclerosis via shear stress mechanotransduction
  JOURNAL   Cardiovasc Res 116 (11), 1863-1874 (2020)
   PUBMED   31584065
  REMARK    GeneRIF: A key role for the novel coronary artery disease gene JCAD
            in atherosclerosis via shear stress mechanotransduction.
REFERENCE   4  (residues 1 to 1359)
  AUTHORS   Xu,S., Xu,Y., Liu,P., Zhang,S., Liu,H., Slavin,S., Kumar,S.,
            Koroleva,M., Luo,J., Wu,X., Rahman,A., Pelisek,J., Jo,H., Si,S.,
            Miller,C.L. and Jin,Z.G.
  TITLE     The novel coronary artery disease risk gene JCAD/KIAA1462 promotes
            endothelial dysfunction and atherosclerosis
  JOURNAL   Eur Heart J 40 (29), 2398-2408 (2019)
   PUBMED   31539914
  REMARK    GeneRIF: The novel coronary artery disease risk gene JCAD/KIAA1462
            promotes endothelial dysfunction and atherosclerosis.
REFERENCE   5  (residues 1 to 1359)
  AUTHORS   Jones,P.D., Kaiser,M.A., Ghaderi Najafabadi,M., Koplev,S., Zhao,Y.,
            Douglas,G., Kyriakou,T., Andrews,S., Rajmohan,R., Watkins,H.,
            Channon,K.M., Ye,S., Yang,X., Bjorkegren,J.L.M., Samani,N.J. and
            Webb,T.R.
  TITLE     JCAD, a Gene at the 10p11 Coronary Artery Disease Locus, Regulates
            Hippo Signaling in Endothelial Cells
  JOURNAL   Arterioscler Thromb Vasc Biol 38 (8), 1711-1722 (2018)
   PUBMED   29794114
  REMARK    GeneRIF: JCAD negatively regulates Hippo signaling in endothelial
            cells and contributes to atherosclerosis by regulating YAP activity
            and endothelial dysfunction.
REFERENCE   6  (residues 1 to 1359)
  AUTHORS   Murdock,D.G., Bradford,Y., Schnetz-Boutaud,N., Mayo,P., Allen,M.J.,
            D'Aoust,L.N., Liang,X., Mitchell,S.L., Zuchner,S., Small,G.W.,
            Gilbert,J.R., Pericak-Vance,M.A. and Haines,J.L.
  TITLE     KIAA1462, a coronary artery disease associated gene, is a candidate
            gene for late onset Alzheimer disease in APOE carriers
  JOURNAL   PLoS One 8 (12), e82194 (2013)
   PUBMED   24349219
  REMARK    GeneRIF: Results in this study identify the KIAA1462 locus as a
            candidate locus for late onset Alzheimer disease in APOE4 carriers.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1359)
  AUTHORS   Akashi,M., Higashi,T., Masuda,S., Komori,T. and Furuse,M.
  TITLE     A coronary artery disease-associated gene product, JCAD/KIAA1462,
            is a novel component of endothelial cell-cell junctions
  JOURNAL   Biochem Biophys Res Commun 413 (2), 224-229 (2011)
   PUBMED   21884682
REFERENCE   8  (residues 1 to 1359)
  CONSRTM   Coronary Artery Disease (C4D) Genetics Consortium
  TITLE     A genome-wide association study in Europeans and South Asians
            identifies five new loci for coronary artery disease
  JOURNAL   Nat Genet 43 (4), 339-344 (2011)
   PUBMED   21378988
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1359)
  AUTHORS   Erdmann,J., Willenborg,C., Nahrstaedt,J., Preuss,M., Konig,I.R.,
            Baumert,J., Linsel-Nitschke,P., Gieger,C., Tennstedt,S.,
            Belcredi,P., Aherrahrou,Z., Klopp,N., Loley,C., Stark,K.,
            Hengstenberg,C., Bruse,P., Freyer,J., Wagner,A.K., Medack,A.,
            Lieb,W., Grosshennig,A., Sager,H.B., Reinhardt,A., Schafer,A.,
            Schreiber,S., El Mokhtari,N.E., Raaz-Schrauder,D., Illig,T.,
            Garlichs,C.D., Ekici,A.B., Reis,A., Schrezenmeir,J., Rubin,D.,
            Ziegler,A., Wichmann,H.E., Doering,A., Meisinger,C., Meitinger,T.,
            Peters,A. and Schunkert,H.
  TITLE     Genome-wide association study identifies a new locus for coronary
            artery disease on chromosome 10p11.23
  JOURNAL   Eur Heart J 32 (2), 158-168 (2011)
   PUBMED   21088011
  REMARK    GeneRIF: KIAA1462 gene encodes a yet uncharacterized protein, on
            chromosome 10p11.23 with genome-wide significant association for
            CAD/MI
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   10 (residues 1 to 1359)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158036.14 and CB988996.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jun 15, 2007 this sequence version replaced
            XP_934405.1, XP_166132.3, XP_945904.1, XP_949912.1.
            
            Summary: This gene encodes an endothelial cell-to-cell junction
            protein. Naturally occurring mutations in this gene are associated
            with coronary artery disease, late onset alzheimer disease, and
            emphysema distribution. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.100409.1,
                                           SRR1803614.16211.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2467143
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375377.2/ ENSP00000364526.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p11.23"
     Protein         1..1359
                     /product="junctional cadherin 5-associated protein isoform
                     1"
                     /note="junctional protein associated with coronary artery
                     disease; junctional cadherin 5-associated protein"
                     /calculated_mol_wt=148220
     Region          1..1348
                     /region_name="JCAD"
                     /note="Junctional protein associated with coronary artery
                     disease; pfam15351"
                     /db_xref="CDD:434658"
     Region          1..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P266.3)"
     Region          249..411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P266.3)"
     Region          454..554
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P266.3)"
     Region          591..813
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P266.3)"
     Region          840..1076
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P266.3)"
     Site            1044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P266.3)"
     Site            1050
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5DTX6; propagated from
                     UniProtKB/Swiss-Prot (Q9P266.3)"
     Region          1105..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P266.3)"
     Region          1157..1207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P266.3)"
     Site            1194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P266.3)"
     Region          1225..1260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P266.3)"
     Region          1276..1359
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P266.3)"
     Site            1281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5DTX6; propagated from
                     UniProtKB/Swiss-Prot (Q9P266.3)"
     CDS             1..1359
                     /gene="JCAD"
                     /gene_synonym="KIAA1462"
                     /coded_by="NM_020848.4:165..4244"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41500.1"
                     /db_xref="GeneID:57608"
                     /db_xref="HGNC:HGNC:29283"
                     /db_xref="MIM:614398"
ORIGIN      
        1 mysvedllis hgyklsrdpp asrednpkgr qaartgtrag qglqnghedg paalahrkts
       61 agkghvsdse srrstprghg epqstsasrt seagfcnqpp sawsshpptg ndqayrrrgr
      121 qearsqkpre henleargma qahslpvhvr egpwevggrs ehvmkkpvwe eelrmsgpak
      181 wqnvsleswn qprklgrqms dgdgerlfqd lypfiqgehv lnsqnkgksr slprvlspes
      241 lscteipipl nerhspkmpp ypptcapnld strnseksgc sapfprpkfg rplkppsyss
      301 hqqsrggads sdsqdsqqmd ayvprhelcl sdpgleppvy vpppsyrspp qnipnpyled
      361 tvpinvcggh sqqqspteka gasgqppsgp pgtgneygvs prlpqglpah prpvtaydgf
      421 vqyipfddpr lrhfklaqpq gfcedikldd ksynsspvta qepahggmqp dgaiwnpqsl
      481 ippsgdergl vladssprwl wgqppgdgen sglpnqrdrc vargqwpdvr gsqhghtgrq
      541 vsspysqges tcetqtklkk fqtgtrtkks skkkmnetif clvsipvkse shlpdrdmdn
      601 ndlkpsadqk ngsdkspalq eqsllsmsst dlelqaltgs mggrtefqkq dlgepeedrq
      661 tndlsfihlt khrelkhsgs wpghryrdqq tqtsfseepq ssqllpgakl ggpsraalsp
      721 kcsdpaasea qthtafptgd hkqrpsarnl kghrslspss nsafsrtsls vdqaptpkag
      781 rsqpcvdvhg lgahpgpkre vvkgeptgpc nskqlfgqfl lkpvsrrpwd lisqlesfnk
      841 elqeeeesss ssssssssse eseaepqqen rahcrqedvg frgnspemrv epqprmwvpe
      901 spvcrsgrge skseswseel qpghprawpp spgrfrveeg ggapfcsadg stsaekrhle
      961 vsngmdelag spfpvtrmss rssdakplpa sypaeprepq espkitsafs svkpseavpr
     1021 kfdsggerga glplslsnkn rglsapdlrs vgltpgqeqg aselegslge astieippge
     1081 slqaraaril gievavesll pgirragqnq paepdasact pespqeells rpapadvprv
     1141 stdafygrrk cgwtksplfv gdrdsarrap qafehsdvdg vvtstdpvpe pepspleskf
     1201 feqkdvetkp pfrstlfhfv ertpsvagse krlrspskvi eslqeklasp prradpdrlm
     1261 rmkevssvsr mrvlsfrnad sqedaeelka ttrgqaglpg glvspgsgdr aqrlghslsv
     1321 skdsisreek ehpaaqkeks mdqdfwcpds ydpsrverv
//
LOCUS       NP_005333                200 aa            linear   PRI 27-APR-2025
DEFINITION  high mobility group protein B3 isoform a [Homo sapiens].
ACCESSION   NP_005333
VERSION     NP_005333.2
DBSOURCE    REFSEQ: accession NM_005342.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Cui,Y., Wen,H., Tang,J., Chen,J., Zhou,J., Hou,M., Rong,X., Lan,Y.
            and Wu,Q.
  TITLE     ELAVL1 regulates glycolysis in nasopharyngeal carcinoma cells
            through the HMGB3/beta-catenin axis
  JOURNAL   Mol Med 30 (1), 172 (2024)
   PUBMED   39390359
  REMARK    GeneRIF: ELAVL1 regulates glycolysis in nasopharyngeal carcinoma
            cells through the HMGB3/beta-catenin axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Zhao,T., He,X., Liang,X., Kellum,A.H. Jr., Tang,F., Yin,J., Guo,S.,
            Wang,Y., Gao,Z. and Wang,Y.
  TITLE     HMGB3 and SUB1 Bind to and Facilitate the Repair of N2-Alkylguanine
            Lesions in DNA
  JOURNAL   J Am Chem Soc 146 (32), 22553-22562 (2024)
   PUBMED   39101269
  REMARK    GeneRIF: HMGB3 and SUB1 Bind to and Facilitate the Repair of
            N[2]-Alkylguanine Lesions in DNA.
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Chikhirzhina,E., Tsimokha,A., Tomilin,A.N. and Polyanichko,A.
  TITLE     Structure and Functions of HMGB3 Protein
  JOURNAL   Int J Mol Sci 25 (14), 7656 (2024)
   PUBMED   39062899
  REMARK    GeneRIF: Structure and Functions of HMGB3 Protein.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Hu,P., Yan,T., Lv,S., Ye,M., Wu,M., Fang,H. and Xiao,B.
  TITLE     Exosomal HMGB3 released by glioma cells confers the activation of
            NLRP3 inflammasome and pyroptosis in tumor-associated macrophages
  JOURNAL   Tissue Cell 88, 102406 (2024)
   PUBMED   38761792
  REMARK    GeneRIF: Exosomal HMGB3 released by glioma cells confers the
            activation of NLRP3 inflammasome and pyroptosis in tumor-associated
            macrophages.
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Ma,H., Qi,G., Han,F., Gai,P., Peng,J. and Kong,B.
  TITLE     HMGB3 promotes the malignant phenotypes and stemness of epithelial
            ovarian cancer through the MAPK/ERK signaling pathway
  JOURNAL   Cell Commun Signal 21 (1), 144 (2023)
   PUBMED   37328851
  REMARK    GeneRIF: HMGB3 promotes the malignant phenotypes and stemness of
            epithelial ovarian cancer through the MAPK/ERK signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Nemeth,M.J., Kirby,M.R. and Bodine,D.M.
  TITLE     Hmgb3 regulates the balance between hematopoietic stem cell
            self-renewal and differentiation
  JOURNAL   Proc Natl Acad Sci U S A 103 (37), 13783-13788 (2006)
   PUBMED   16945912
REFERENCE   7  (residues 1 to 200)
  AUTHORS   Nemeth,M.J., Cline,A.P., Anderson,S.M., Garrett-Beal,L.J. and
            Bodine,D.M.
  TITLE     Hmgb3 deficiency deregulates proliferation and differentiation of
            common lymphoid and myeloid progenitors
  JOURNAL   Blood 105 (2), 627-634 (2005)
   PUBMED   15358624
REFERENCE   8  (residues 1 to 200)
  AUTHORS   Nemeth,M.J., Curtis,D.J., Kirby,M.R., Garrett-Beal,L.J.,
            Seidel,N.E., Cline,A.P. and Bodine,D.M.
  TITLE     Hmgb3: an HMG-box family member expressed in primitive
            hematopoietic cells that inhibits myeloid and B-cell
            differentiation
  JOURNAL   Blood 102 (4), 1298-1306 (2003)
   PUBMED   12714519
REFERENCE   9  (residues 1 to 200)
  AUTHORS   Vaccari,T., Beltrame,M., Ferrari,S. and Bianchi,M.E.
  TITLE     Hmg4, a new member of the Hmg1/2 gene family
  JOURNAL   Genomics 49 (2), 247-252 (1998)
   PUBMED   9598312
REFERENCE   10 (residues 1 to 200)
  AUTHORS   Wilke,K., Wiemann,S., Gaul,R., Gong,W. and Poustka,A.
  TITLE     Isolation of human and mouse HMG2a cDNAs: evidence for an
            HMG2a-specific 3' untranslated region
  JOURNAL   Gene 198 (1-2), 269-274 (1997)
   PUBMED   9370291
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y10043.1, BC037210.1 and
            AF003626.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 26, 2005 this sequence version replaced NP_005333.1.
            
            Summary: This gene encodes a member of a family of proteins
            containing one or more high mobility group DNA-binding motifs. The
            encoded protein plays an important role in maintaining stem cell
            populations, and may be aberrantly expressed in tumor cells. A
            mutation in this gene was associated with microphthalmia, syndromic
            13. There are numerous pseudogenes of this gene on multiple
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to vaiant 1. Variants 1, 2, and 3 encode the same isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA236625.1, SRR1803617.204072.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325307.12/ ENSP00000359393.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..200
                     /product="high mobility group protein B3 isoform a"
                     /note="high-mobility group (nonhistone chromosomal)
                     protein 4; high mobility group protein B3; high mobility
                     group protein 2a"
                     /calculated_mol_wt=22849
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63159; propagated from
                     UniProtKB/Swiss-Prot (O15347.4)"
     Region          13..76
                     /region_name="HMG-box_HMGB_rpt1"
                     /note="first high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21978"
                     /db_xref="CDD:438794"
     Site            order(13,16..17,19..21,25,28,35..36,38..39,41..43,45..46,
                     50)
                     /site_type="other"
                     /note="p53 binding site [polypeptide binding]"
                     /db_xref="CDD:438794"
     Site            order(13..17,20..21,36,38..39,41..43,46,49)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438794"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P09429; propagated from
                     UniProtKB/Swiss-Prot (O15347.4)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (O15347.4)"
     Region          71..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15347.4)"
     Region          91..161
                     /region_name="HMG-box_HMGB_rpt2"
                     /note="second high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21979"
                     /db_xref="CDD:438795"
     Site            order(92..98,100..102,104..105,108,120..121,123..125,128,
                     131,150,153..154,157,160..161)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438795"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09429; propagated from
                     UniProtKB/Swiss-Prot (O15347.4)"
     Site            112
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P30681; propagated from
                     UniProtKB/Swiss-Prot (O15347.4)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (O15347.4)"
     Region          161..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15347.4)"
     CDS             1..200
                     /gene="HMGB3"
                     /gene_synonym="HMG-2a; HMG-4; HMG2A; HMG4"
                     /coded_by="NM_005342.4:48..650"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS35428.1"
                     /db_xref="GeneID:3149"
                     /db_xref="HGNC:HGNC:5004"
                     /db_xref="MIM:300193"
ORIGIN      
        1 makgdpkkpk gkmsayaffv qtcreehkkk npevpvnfae fskkcserwk tmsgkekskf
       61 demakadkvr ydremkdygp akggkkkkdp napkrppsgf flfcsefrpk ikstnpgisi
      121 gdvakklgem wnnlndsekq pyitkaaklk ekyekdvady kskgkfdgak gpakvarkkv
      181 eeedeeeeee eeeeeeeede
//
LOCUS       NP_001352173             486 aa            linear   PRI 27-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 3
            [Homo sapiens].
ACCESSION   NP_001352173
VERSION     NP_001352173.1
DBSOURCE    REFSEQ: accession NM_001365244.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Zhang,S., Huang,J., Lan,Z., Xiao,Y., Liao,Y., Basnet,S., Huang,P.,
            Li,Y., Yan,J., Sheng,Y., Zhou,W., Liu,Q., Tan,H., Tan,Y., Yuan,L.,
            Wang,L., Dai,L., Zhang,W. and Du,C.
  TITLE     CPEB1 Controls NRF2 Proteostasis and Ferroptosis Susceptibility in
            Pancreatic Cancer
  JOURNAL   Int J Biol Sci 20 (8), 3156-3172 (2024)
   PUBMED   38904009
  REMARK    GeneRIF: CPEB1 Controls NRF2 Proteostasis and Ferroptosis
            Susceptibility in Pancreatic Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Pico,S., Parras,A., Santos-Galindo,M., Pose-Utrilla,J., Castro,M.,
            Fraga,E., Hernandez,I.H., Elorza,A., Anta,H., Wang,N.,
            Marti-Sanchez,L., Belloc,E., Garcia-Esparcia,P., Garrido,J.J.,
            Ferrer,I., Macias-Garcia,D., Mir,P., Artuch,R., Perez,B.,
            Hernandez,F., Navarro,P., Lopez-Sendon,J.L., Iglesias,T.,
            Yang,X.W., Mendez,R. and Lucas,J.J.
  TITLE     CPEB alteration and aberrant transcriptome-polyadenylation lead to
            a treatable SLC19A3 deficiency in Huntington's disease
  JOURNAL   Sci Transl Med 13 (613), eabe7104 (2021)
   PUBMED   34586830
  REMARK    GeneRIF: CPEB alteration and aberrant transcriptome-polyadenylation
            lead to a treatable SLC19A3 deficiency in Huntington's disease.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Shao,K., Pu,W., Zhang,J., Guo,S., Qian,F., Glurich,I., Jin,Q.,
            Ma,Y., Ju,S., Zhang,Z. and Ding,W.
  TITLE     DNA hypermethylation contributes to colorectal cancer metastasis by
            regulating the binding of CEBPB and TFCP2 to the CPEB1 promoter
  JOURNAL   Clin Epigenetics 13 (1), 89 (2021)
   PUBMED   33892791
  REMARK    GeneRIF: DNA hypermethylation contributes to colorectal cancer
            metastasis by regulating the binding of CEBPB and TFCP2 to the
            CPEB1 promoter.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Sovijit,W., Sovijit,W., Ishii,Y., Kambe,J., Fujita,T., Watanabe,G.,
            Yamaguchi,H. and Nagaoka,K.
  TITLE     Estrogen promotes increased breast cancer cell proliferation and
            migration through downregulation of CPEB1 expression
  JOURNAL   Biochem Biophys Res Commun 534, 871-876 (2021)
   PUBMED   33162033
  REMARK    GeneRIF: Estrogen promotes increased breast cancer cell
            proliferation and migration through downregulation of CPEB1
            expression.
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Jiao,W., Zhao,S., Liu,R., Guo,T. and Qin,Y.
  TITLE     CPEB1 deletion is not a common explanation for premature ovarian
            insufficiency in a Chinese cohort
  JOURNAL   J Ovarian Res 13 (1), 49 (2020)
   PUBMED   32354341
  REMARK    GeneRIF: CPEB1 deletion is not a common explanation for premature
            ovarian insufficiency in a Chinese cohort.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Hagele,S., Kuhn,U., Boning,M. and Katschinski,D.M.
  TITLE     Cytoplasmic polyadenylation-element-binding protein (CPEB)1 and 2
            bind to the HIF-1alpha mRNA 3'-UTR and modulate HIF-1alpha protein
            expression
  JOURNAL   Biochem J 417 (1), 235-246 (2009)
   PUBMED   18752464
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Sasayama,T., Marumoto,T., Kunitoku,N., Zhang,D., Tamaki,N.,
            Kohmura,E., Saya,H. and Hirota,T.
  TITLE     Over-expression of Aurora-A targets cytoplasmic polyadenylation
            element binding protein and promotes mRNA polyadenylation of Cdk1
            and cyclin B1
  JOURNAL   Genes Cells 10 (7), 627-638 (2005)
   PUBMED   15966895
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Wilczynska,A., Aigueperse,C., Kress,M., Dautry,F. and Weil,D.
  TITLE     The translational regulator CPEB1 provides a link between dcp1
            bodies and stress granules
  JOURNAL   J Cell Sci 118 (Pt 5), 981-992 (2005)
   PUBMED   15731006
  REMARK    GeneRIF: CPEB1 has a role in compartmentalization of mRNA
            metabolism in the cytoplasm, between dcp1 bodies and stress
            granules
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Mendez,R. and Richter,J.D.
  TITLE     Translational control by CPEB: a means to the end
  JOURNAL   Nat Rev Mol Cell Biol 2 (7), 521-529 (2001)
   PUBMED   11433366
  REMARK    Review article
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Welk,J.F., Charlesworth,A., Smith,G.D. and MacNicol,A.M.
  TITLE     Identification and characterization of the gene encoding human
            cytoplasmic polyadenylation element binding protein
  JOURNAL   Gene 263 (1-2), 113-120 (2001)
   PUBMED   11223249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105339.9, AC110291.7 and
            AC245033.2.
            
            Summary: This gene encodes a member of the cytoplasmic
            polyadenylation element binding protein family. This highly
            conserved protein binds to a specific RNA sequence, called the
            cytoplasmic polyadenylation element, found in the 3' untranslated
            region of some mRNAs. The encoded protein functions in both the
            cytoplasm and the nucleus. It is involved in the regulation of mRNA
            translation, as well as processing of the 3' untranslated region,
            and may play a role in cell proliferation and tumorigenesis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.188471.1,
                                           SRR1660805.200295.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..486
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 3"
                     /note="CPE-binding protein 1"
                     /calculated_mol_wt=53504
     Region          <1..232
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          234..336
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          347..430
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          424..479
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..486
                     /gene="CPEB1"
                     /gene_synonym="CPE-BP1; CPEB; CPEB-1; h-CPEB; hCPEB-1"
                     /coded_by="NM_001365244.1:366..1826"
                     /note="isoform 3 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS45330.2"
                     /db_xref="GeneID:64506"
                     /db_xref="HGNC:HGNC:21744"
                     /db_xref="MIM:607342"
ORIGIN      
        1 mlfptsaqes srglpdandl clglqslslt gwdrpwstqd sdssaqssth svlsmlhnpl
       61 gnvlgkppls flpldplgsd lvdkfpapsv rgsrldtrpi ldsrssspsd sdtsgfssgs
      121 dhlsdlissl rispplpfls lsgggprdpl kmgvgsrmdq eqaalaavtp sptsaskrwp
      181 gasvwpswdl leapkdpfsi erearlhrqa aavneatctw sgqlpprnyk npiysckvfl
      241 ggvpwditea glvntfrvfg slsvewpgkd gkhprcppkg yvylvfelek svrsllqacs
      301 hdplspdgls eyyfkmssrr mrckevqvip wvladsnfvr spsqrldpsr tvfvgalhgm
      361 lnaealaail ndlfggvvya gidtdkhkyp igsgrvtfnn qrsylkavsa afveikttkf
      421 tkkvqidpyl edslchicss qpgpffcrdq vcfkyfcrsc whwrhsmegl rhhsplmrnq
      481 knrdss
//
LOCUS       NP_065827                577 aa            linear   PRI 27-APR-2025
DEFINITION  protein hinderin isoform 1 [Homo sapiens].
ACCESSION   NP_065827 XP_029429
VERSION     NP_065827.1
DBSOURCE    REFSEQ: accession NM_020776.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Drew,K., Lee,C., Huizar,R.L., Tu,F., Borgeson,B., McWhite,C.D.,
            Ma,Y., Wallingford,J.B. and Marcotte,E.M.
  TITLE     Integration of over 9,000 mass spectrometry experiments builds a
            global map of human protein complexes
  JOURNAL   Mol Syst Biol 13 (6), 932 (2017)
   PUBMED   28596423
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Barone,R., Fichera,M., De Grandi,M., Battaglia,M., Lo Faro,V.,
            Mattina,T. and Rizzo,R.
  TITLE     Familial 18q12.2 deletion supports the role of RNA-binding protein
            CELF4 in autism spectrum disorders
  JOURNAL   Am J Med Genet A 173 (6), 1649-1655 (2017)
   PUBMED   28407444
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Shaffer,J.R., Polk,D.E., Wang,X., Feingold,E., Weeks,D.E.,
            Lee,M.K., Cuenco,K.T., Weyant,R.J., Crout,R.J., McNeil,D.W. and
            Marazita,M.L.
  TITLE     Genome-wide association study of periodontal health measured by
            probing depth in adults ages 18-49 years
  JOURNAL   G3 (Bethesda) 4 (2), 307-314 (2014)
   PUBMED   24347629
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Patel,C.A. and Ghiselli,G.
  TITLE     Hinderin, a five-domains protein including coiled-coil motifs that
            binds to SMC3
  JOURNAL   BMC Cell Biol 6 (1), 3 (2005)
   PUBMED   15656913
  REMARK    GeneRIF: Hinderin is a novel binding partner of SMC3. Based on its
            ability to modulate SMC1/SMC3 interaction we postulate that
            Hinderin affects the availability of SMC3 to engage in the
            formation of multimeric protein complexes.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL832625.2, BC045585.1, BC008670.1, BC037903.1, BX648875.1,
            AB037749.2 and AC015961.16.
            
            On Nov 22, 2004 this sequence version replaced XP_029429.7.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832625.2, SRR1660803.30522.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280020.10/ ENSP00000280020.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..577
                     /product="protein hinderin isoform 1"
                     /note="hinderin; protein hinderin"
                     /calculated_mol_wt=65242
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZK5; propagated from
                     UniProtKB/Swiss-Prot (Q86T90.2)"
     Region          93..410
                     /region_name="KIAA1328"
                     /note="Uncharacterized protein KIAA1328; pfam15369"
                     /db_xref="CDD:464679"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86T90.2)"
     Region          251..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T90.2)"
     Region          425..444
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T90.2)"
     Region          449..492
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T90.2)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86T90.2)"
     Region          520..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T90.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZK5; propagated from
                     UniProtKB/Swiss-Prot (Q86T90.2)"
     CDS             1..577
                     /gene="KIAA1328"
                     /coded_by="NM_020776.3:13..1746"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45855.1"
                     /db_xref="GeneID:57536"
                     /db_xref="HGNC:HGNC:29248"
                     /db_xref="MIM:616480"
ORIGIN      
        1 madvagpsrp saaafwsrdf sdeeqsvvyv pgisaegnvr srhklmspka dvklktsrvt
       61 dasismeslk gtgdsvdeqn scrgeiksas lkdlcledkr rianlikela rvseekevte
      121 erlkaeqesf ekkirqleeq neliikerea lqlqyrecqe llslyqkyls eqqekltmsl
      181 selgaarmqe qqvssrkstl qcssveldgs ylsiarpqty yqtkqrpksa vqdsasesli
      241 afrnnslkpv tlhhpkddld kipsetttcn cespgrkpav ptekmpqeel hmkecphlkp
      301 tpsqccghrl aadrvhdshp tnmtpqhpkt hpescsycrl swaslvhggg alqpietlkk
      361 qisedrkqql mlqkmeleie kerlqhllaq qetklllkqq qlhqsrldyn cllksncdgw
      421 llgtsssikk hqdppnsgen rkerktvgfh shmkddaqws cqkkdtcrpq rgtvtgvrkd
      481 astspmptgs lkdfvttasp slqhttsrye tslldlvqsl spnsapkpqr ypsreagawn
      541 hgtfrlsplk strkkmgmhr tpeeleenqi lediffi
//
LOCUS       NP_002535                440 aa            linear   PRI 27-APR-2025
DEFINITION  oligodendrocyte-myelin glycoprotein precursor [Homo sapiens].
ACCESSION   NP_002535
VERSION     NP_002535.3
DBSOURCE    REFSEQ: accession NM_002544.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Park,G.H., Lee,S.J., Yim,H., Han,J.H., Kim,H.J., Sohn,Y.B., Ko,J.M.
            and Jeong,S.Y.
  TITLE     TAGLN expression is upregulated in NF1-associated malignant
            peripheral nerve sheath tumors by hypomethylation in its promoter
            and subpromoter regions
  JOURNAL   Oncol Rep 32 (4), 1347-1354 (2014)
   PUBMED   25109740
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Terzi,Y.K., Oguzkan-Balci,S., Anlar,B., Erdogan-Bakar,E. and
            Ayter,S.
  TITLE     Learning disability and oligodendrocyte myelin glycoprotein (OMGP)
            gene in neurofibromatosis type 1
  JOURNAL   Turk J Pediatr 53 (1), 75-78 (2011)
   PUBMED   21534343
  REMARK    GeneRIF: The results do not support a relationship between the OMGP
            gene and the learning disability phenotype observed in
            neurofibromatosis type 1.
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Martins-de-Souza,D., Gattaz,W.F., Schmitt,A., Rewerts,C.,
            Marangoni,S., Novello,J.C., Maccarrone,G., Turck,C.W. and
            Dias-Neto,E.
  TITLE     Alterations in oligodendrocyte proteins, calcium homeostasis and
            new potential markers in schizophrenia anterior temporal lobe are
            revealed by shotgun proteome analysis
  JOURNAL   J Neural Transm (Vienna) 116 (3), 275-289 (2009)
   PUBMED   19034380
  REMARK    GeneRIF: Data show that oligodendrocyte-myelin glycoprotein is
            downregulated in schizophrenia anterior temporal lobe revealed by
            shotgun proteome analysis.
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Douglas,J., Cilliers,D., Coleman,K., Tatton-Brown,K., Barker,K.,
            Bernhard,B., Burn,J., Huson,S., Josifova,D., Lacombe,D., Malik,M.,
            Mansour,S., Reid,E., Cormier-Daire,V., Cole,T. and Rahman,N.
  CONSRTM   Childhood Overgrowth Collaboration
  TITLE     Mutations in RNF135, a gene within the NF1 microdeletion region,
            cause phenotypic abnormalities including overgrowth
  JOURNAL   Nat Genet 39 (8), 963-965 (2007)
   PUBMED   17632510
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Zhou,X.F. and Li,H.Y.
  TITLE     Roles of glial p75NTR in axonal regeneration
  JOURNAL   J Neurosci Res 85 (8), 1601-1605 (2007)
   PUBMED   17335080
  REMARK    Review article
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Mikol,D.D., Rongnoparut,P., Allwardt,B.A., Marton,L.S. and
            Stefansson,K.
  TITLE     The oligodendrocyte-myelin glycoprotein of mouse: primary structure
            and gene structure
  JOURNAL   Genomics 17 (3), 604-610 (1993)
   PUBMED   8244377
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Viskochil,D., Cawthon,R., O'Connell,P., Xu,G.F., Stevens,J.,
            Culver,M., Carey,J. and White,R.
  TITLE     The gene encoding the oligodendrocyte-myelin glycoprotein is
            embedded within the neurofibromatosis type 1 gene
  JOURNAL   Mol Cell Biol 11 (2), 906-912 (1991)
   PUBMED   1899288
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Mikol,D.D., Alexakos,M.J., Bayley,C.A., Lemons,R.S., Le Beau,M.M.
            and Stefansson,K.
  TITLE     Structure and chromosomal localization of the gene for the
            oligodendrocyte-myelin glycoprotein
  JOURNAL   J Cell Biol 111 (6 Pt 1), 2673-2679 (1990)
   PUBMED   2277079
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Mikol,D.D., Gulcher,J.R. and Stefansson,K.
  TITLE     The oligodendrocyte-myelin glycoprotein belongs to a distinct
            family of proteins and contains the HNK-1 carbohydrate
  JOURNAL   J Cell Biol 110 (2), 471-479 (1990)
   PUBMED   1688857
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Mikol,D.D. and Stefansson,K.
  TITLE     A phosphatidylinositol-linked peanut agglutinin-binding
            glycoprotein in central nervous system myelin and on
            oligodendrocytes
  JOURNAL   J Cell Biol 106 (4), 1273-1279 (1988)
   PUBMED   3283151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA206834.1, BC018050.1 and AC134669.4.
            
            On Sep 22, 2004 this sequence version replaced NP_002535.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222663.1, SRR1660805.165268.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247271.5/ ENSP00000247271.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..440
                     /product="oligodendrocyte-myelin glycoprotein precursor"
                     /calculated_mol_wt=46823
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2804
     mat_peptide     25..417
                     /product="Oligodendrocyte-myelin glycoprotein.
                     /id=PRO_0000021888"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
                     /calculated_mol_wt=44356
     Region          <37..>226
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          37..56
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          56..77
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            61
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          79..100
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          80..100
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          101..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          101..121
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          124..145
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          125..147
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          147..168
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          148..168
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          169..192
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          169..189
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Site            189
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          192..213
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          193..216
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          216..239
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          229..270
                     /region_name="Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            234
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          271..292
                     /region_name="Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          293..335
                     /region_name="Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          336..377
                     /region_name="Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          378..416
                     /region_name="Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Site            425
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     CDS             1..440
                     /gene="OMG"
                     /gene_synonym="OMGP"
                     /coded_by="NM_002544.5:91..1413"
                     /db_xref="CCDS:CCDS11265.1"
                     /db_xref="GeneID:4974"
                     /db_xref="HGNC:HGNC:8135"
                     /db_xref="MIM:164345"
ORIGIN      
        1 meyqilkmsl clfillfltp gilcicplqc icterhrhvd csgrnlstlp sglqeniihl
       61 nlsynhftdl hnqltqytnl rtldisnnrl eslpahlprs lwnmsaannn iklldksdta
      121 yqwnlkyldv sknmlekvvl ikntlrslev lnlssnklwt vptnmpsklh ivdlsnnslt
      181 qilpgtlinl tnlthlylhn nkftfipdqs fdqlfqlqei tlynnrwscd hkqnityllk
      241 wmmetkahvi gtpcstqiss lkehnmyptp sgftsslftv sgmqtvdtin slsvvtqpkv
      301 tkipkqyrtk ettfgatlsk dttftstdka fvpypedtst etinsheaaa atltihlqdg
      361 mvtntsltss tkssptpmtl sitsgmpnnf sempqqsttl nlwreetttn vktplpsvan
      421 awkvnasfll llnvvvmlav
//
LOCUS       NP_001346374             200 aa            linear   ROD 27-APR-2025
DEFINITION  palmitoyltransferase ZDHHC4 isoform 2 [Mus musculus].
ACCESSION   NP_001346374
VERSION     NP_001346374.1
DBSOURCE    REFSEQ: accession NM_001359445.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Wang,J., Hao,J.W., Wang,X., Guo,H., Sun,H.H., Lai,X.Y., Liu,L.Y.,
            Zhu,M., Wang,H.Y., Li,Y.F., Yu,L.Y., Xie,C., Wang,H.R., Mo,W.,
            Zhou,H.M., Chen,S., Liang,G. and Zhao,T.J.
  TITLE     DHHC4 and DHHC5 Facilitate Fatty Acid Uptake by Palmitoylating and
            Targeting CD36 to the Plasma Membrane
  JOURNAL   Cell Rep 26 (1), 209-221 (2019)
   PUBMED   30605677
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Hald,J., Galbo,T., Rescan,C., Radzikowski,L., Sprinkel,A.E.,
            Heimberg,H., Ahnfelt-Ronne,J., Jensen,J., Scharfmann,R.,
            Gradwohl,G., Kaestner,K.H., Stoeckert,C. Jr., Jensen,J.N. and
            Madsen,O.D.
  TITLE     Pancreatic islet and progenitor cell surface markers with cell
            sorting potential
  JOURNAL   Diabetologia 55 (1), 154-165 (2012)
   PUBMED   21947380
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Guo,G., Huss,M., Tong,G.Q., Wang,C., Li Sun,L., Clarke,N.D. and
            Robson,P.
  TITLE     Resolution of cell fate decisions revealed by single-cell gene
            expression analysis from zygote to blastocyst
  JOURNAL   Dev Cell 18 (4), 675-685 (2010)
   PUBMED   20412781
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Hoffman,B.G., Zavaglia,B., Witzsche,J., Ruiz de Algara,T.,
            Beach,M., Hoodless,P.A., Jones,S.J., Marra,M.A. and Helgason,C.D.
  TITLE     Identification of transcripts with enriched expression in the
            developing and adult pancreas
  JOURNAL   Genome Biol 9 (6), R99 (2008)
   PUBMED   18554416
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC123686.11.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2) is
            shorter at the N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660813.203339.1,
                                           ERR3363658.3027326.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164143 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 82.08 cM"
     Protein         1..200
                     /product="palmitoyltransferase ZDHHC4 isoform 2"
                     /EC_number="2.3.1.225"
                     /note="probable palmitoyltransferase ZDHHC4; zinc finger
                     DHHC domain-containing protein 4"
                     /calculated_mol_wt=23056
     Region          8..149
                     /region_name="DHHC"
                     /note="DHHC palmitoyltransferase; pfam01529"
                     /db_xref="CDD:396215"
     CDS             1..200
                     /gene="Zdhhc4"
                     /gene_synonym="1810021D01Rik; 2900029I10Rik; DHHC-4"
                     /coded_by="NM_001359445.1:1267..1869"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:72881"
                     /db_xref="MGI:MGI:1920131"
ORIGIN      
        1 mfpknsrcpt cdlrkparsk hcrlcdrcvh rfdhhcvwvn ncigawntry fliylltlta
       61 saatiatvta afllrlvtvs dlyqetyldd vghfqavdtv fliqhlflaf privfllgfv
      121 ivlsmllagy lcfalylaat nqttnewykg dwawcqrwpl vawspsaepr ihqnihshgf
      181 rsnlreiflp atpsykkkek
//
LOCUS       NP_001277745             668 aa            linear   ROD 27-APR-2025
DEFINITION  actin-binding LIM protein 1 isoform 6 [Mus musculus].
ACCESSION   NP_001277745 XP_006527105
VERSION     NP_001277745.1
DBSOURCE    REFSEQ: accession NM_001290816.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Chen,X., Liu,Y., Xu,C., Ba,L., Liu,Z., Li,X., Huang,J., Simpson,E.,
            Gao,H., Cao,D., Sheng,W., Qi,H., Ji,H., Sanderson,M., Cai,C.L.,
            Li,X., Yang,L., Na,J., Yamamura,K., Liu,Y., Huang,G., Shou,W. and
            Sun,N.
  TITLE     QKI is a critical pre-mRNA alternative splicing regulator of
            cardiac myofibrillogenesis and contractile function
  JOURNAL   Nat Commun 12 (1), 89 (2021)
   PUBMED   33397958
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Jin,S.H., Kim,H., Gu,D.R., Park,K.H., Lee,Y.R., Choi,Y. and
            Lee,S.H.
  TITLE     Actin-binding LIM protein 1 regulates receptor activator of
            NF-kappaB ligand-mediated osteoclast differentiation and motility
  JOURNAL   BMB Rep 51 (7), 356-361 (2018)
   PUBMED   29921413
  REMARK    GeneRIF: ABLIM1 is associated with the regulation of preosteoclast
            motility via the PI3K/Akt/Rac1 pathway during RANKL-mediated
            osteoclastogenesis.
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Zhang,Q., Huang,R., Ye,Y., Guo,X., Lu,J., Zhu,F., Gong,X.,
            Zhang,Q., Yan,J., Luo,L., Zhuang,S., Chen,Y., Zhao,X., Evans,S.M.,
            Jiang,C., Liang,X. and Sun,Y.
  TITLE     Temporal requirements for ISL1 in sympathetic neuron proliferation,
            differentiation, and diversification
  JOURNAL   Cell Death Dis 9 (2), 247 (2018)
   PUBMED   29445148
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Narahara,H., Sakai,E., Yamaguchi,Y., Narahara,S., Iwatake,M.,
            Okamoto,K., Yoshida,N. and Tsukuba,T.
  TITLE     Actin binding LIM 1 (abLIM1) negatively controls osteoclastogenesis
            by regulating cell migration and fusion
  JOURNAL   J Cell Physiol 234 (1), 486-499 (2018)
   PUBMED   29904924
  REMARK    GeneRIF: abLIM1 regulated the localization of tubulin, migration,
            and fusion in osteoclasts. Thus, these results indicate that abLIM1
            negatively controls osteoclast differentiation by regulating cell
            migration and fusion mediated via actin formation.
REFERENCE   6  (residues 1 to 668)
  AUTHORS   Erkman,L., Yates,P.A., McLaughlin,T., McEvilly,R.J., Whisenhunt,T.,
            O'Connell,S.M., Krones,A.I., Kirby,M.A., Rapaport,D.H.,
            Bermingham,J.R., O'Leary,D.D. and Rosenfeld,M.G.
  TITLE     A POU domain transcription factor-dependent program regulates axon
            pathfinding in the vertebrate visual system
  JOURNAL   Neuron 28 (3), 779-792 (2000)
   PUBMED   11163266
REFERENCE   7  (residues 1 to 668)
  AUTHORS   Suriyapperuma,S.P., Lozovatsky,L., Ciciotte,S.L., Peters,L.L. and
            Gilligan,D.M.
  TITLE     The mouse adducin gene family: alternative splicing and chromosomal
            localization
  JOURNAL   Mamm Genome 11 (1), 16-23 (2000)
   PUBMED   10602987
REFERENCE   8  (residues 1 to 668)
  AUTHORS   Kim,H.J., Noben-Trauth,K. and Morell,R.J.
  TITLE     Tectorin-beta (Tectb) maps to mouse chromosome 19
  JOURNAL   Genomics 53 (3), 419-420 (1998)
   PUBMED   9799617
REFERENCE   9  (residues 1 to 668)
  AUTHORS   Kim,A.C., Peters,L.L., Knoll,J.H., Van Huffel,C., Ciciotte,S.L.,
            Kleyn,P.W. and Chishti,A.H.
  TITLE     Limatin (LIMAB1), an actin-binding LIM protein, maps to mouse
            chromosome 19 and human chromosome 10q25, a region frequently
            deleted in human cancers
  JOURNAL   Genomics 46 (2), 291-293 (1997)
   PUBMED   9417918
REFERENCE   10 (residues 1 to 668)
  AUTHORS   Roof,D.J., Hayes,A., Adamian,M., Chishti,A.H. and Li,T.
  TITLE     Molecular characterization of abLIM, a novel actin-binding and
            double zinc finger protein
  JOURNAL   J Cell Biol 138 (3), 575-588 (1997)
   PUBMED   9245787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC102655.7, AK143907.1, AC161518.3 and BE994737.1.
            
            On Mar 20, 2014 this sequence version replaced XP_006527105.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and lacks four alternate in-frame
            exons and uses an alternate in-frame splice site in the 3' coding
            region, compared to variant 1. It initiates translation at an
            alternate start codon. The encoded isoform (6) has a distinct
            N-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK143907.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 52.09 cM"
     Protein         1..668
                     /product="actin-binding LIM protein 1 isoform 6"
                     /note="actin-binding double zinc finger protein;
                     actin-binding LIM protein family member 1"
                     /calculated_mol_wt=75162
     Region          23..74
                     /region_name="LIM1_abLIM"
                     /note="The first LIM domain of actin binding LIM (abLIM)
                     proteins; cd09327"
                     /db_xref="CDD:188713"
     Site            order(23,26,43,46,49,52,70,73)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188713"
     Region          79..134
                     /region_name="LIM2_abLIM"
                     /note="The second LIM domain on actin binding LIM (abLIM)
                     proteins; cd09328"
                     /db_xref="CDD:188714"
     Site            order(82,85,102,105,108,111,130,133)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188714"
     Region          150..201
                     /region_name="LIM3_abLIM"
                     /note="The third LIM domain of actin binding LIM (abLIM)
                     proteins; cd09329"
                     /db_xref="CDD:188715"
     Site            order(150,153,171,174,177,180,197,200)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188715"
     Region          209..264
                     /region_name="LIM4_abLIM"
                     /note="The fourth LIM domain of actin binding LIM (abLIM)
                     proteins; cd09330"
                     /db_xref="CDD:188716"
     Site            order(209,212,229,232,235,238,257,260)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188716"
     Region          273..618
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          633..668
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..668
                     /gene="Ablim1"
                     /gene_synonym="2210411C18Rik; 2610209L21Rik;
                     4833406P10Rik; 9330196J19Rik; Limab1; mKIAA0059"
                     /coded_by="NM_001290816.2:318..2324"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS70963.1"
                     /db_xref="GeneID:226251"
                     /db_xref="MGI:MGI:1194500"
ORIGIN      
        1 mvkekvahpq dphhssekpv ihchkcgepc kgevlrvqtk hfhikcftck vcgcdlaqgg
       61 ffikngdylc tldyqrmygt rchgcgefve gevvtalgkt yhpncfacti ckrpfppgdr
      121 vtfngrdclc qlcaqpmsss pkeascssnc agcgrdikng qallaldkqw hlgcfkcksc
      181 gkvltgeyis kdgspycekd yqglfgvkce achqfitgkv leagdkhyhp scarcsrcnq
      241 mftegeemyl qgstvwhpdc kqstkteekl rptrtssesi ysrpgssipg spghtiyakv
      301 dneildykdl aaipkvkaiy dierpdlity epfytsgyed kqerqslges prtlsptpsa
      361 egyqdvrdrm ihrstsqgsi nspvysrhsy tpttsrspqh fhrpdqgini yrkppiykqh
      421 daaalaaqsk asediikfsk fpaaqapdpn eipkietdhw pgppslaavg tdprrrssgr
      481 eedeeellrr rqlqeeqlmk lnsglgqlil keemekesre raslasryds plhsashaps
      541 sktsslpgyg knglhrpvst dfaqynsygd isggvrdyqt lpdghmpavr mdrgvsmpnm
      601 lepkifpyem lmvtnrgrnk ilrdvdrtrl erhlapevfw eifgmsiqef dklplwrrnd
      661 mkkkaklf
//
LOCUS       NP_003783                148 aa            linear   PRI 27-APR-2025
DEFINITION  endothelial differentiation-related factor 1 isoform alpha [Homo
            sapiens].
ACCESSION   NP_003783
VERSION     NP_003783.1
DBSOURCE    REFSEQ: accession NM_003792.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Sinha,N.K., Ordureau,A., Best,K., Saba,J.A., Zinshteyn,B.,
            Sundaramoorthy,E., Fulzele,A., Garshott,D.M., Denk,T., Thoms,M.,
            Paulo,J.A., Harper,J.W., Bennett,E.J., Beckmann,R. and Green,R.
  TITLE     EDF1 coordinates cellular responses to ribosome collisions
  JOURNAL   Elife 9, e58828 (2020)
   PUBMED   32744497
  REMARK    GeneRIF: EDF1 coordinates cellular responses to ribosome
            collisions.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Nassa,G., Giurato,G., Salvati,A., Gigantino,V., Pecoraro,G.,
            Lamberti,J., Rizzo,F., Nyman,T.A., Tarallo,R. and Weisz,A.
  TITLE     The RNA-mediated estrogen receptor alpha interactome of
            hormone-dependent human breast cancer cell nuclei
  JOURNAL   Sci Data 6 (1), 173 (2019)
   PUBMED   31527615
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Kabe,Y., Goto,M., Shima,D., Imai,T., Wada,T., Morohashi,Ki.,
            Shirakawa,M., Hirose,S. and Handa,H.
  TITLE     The role of human MBF1 as a transcriptional coactivator
  JOURNAL   J Biol Chem 274 (48), 34196-34202 (1999)
   PUBMED   10567391
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Ozaki,J., Takemaru,K.I., Ikegami,T., Mishima,M., Ueda,H.,
            Hirose,S., Kabe,Y., Handa,H. and Shirakawa,M.
  TITLE     Identification of the core domain and the secondary structure of
            the transcriptional coactivator MBF1
  JOURNAL   Genes Cells 4 (7), 415-424 (1999)
   PUBMED   10469174
REFERENCE   8  (residues 1 to 148)
  AUTHORS   Dragoni,I., Mariotti,M., Consalez,G.G., Soria,M.R. and Maier,J.A.
  TITLE     EDF-1, a novel gene product down-regulated in human endothelial
            cell differentiation
  JOURNAL   J Biol Chem 273 (47), 31119-31124 (1998)
   PUBMED   9813014
REFERENCE   9  (residues 1 to 148)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   10 (residues 1 to 148)
  AUTHORS   Li,F.Q., Ueda,H. and Hirose,S.
  TITLE     Mediators of activation of fushi tarazu gene transcription by
            BmFTZ-F1
  JOURNAL   Mol Cell Biol 14 (5), 3013-3021 (1994)
   PUBMED   8164657
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY029111.1 and BC015500.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that may regulate endothelial
            cell differentiation, lipid metabolism, and hormone-induced
            cardiomyocyte hypertrophy. The encoded protein has also been found
            to act as a transcriptional coactivator by interconnecting the
            general transcription factor TATA element-binding protein (TBP) and
            gene-specific activators. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (alpha) encodes the longest
            isoform (alpha).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.234522.1,
                                           SRR5189655.171420.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000224073.6/ ENSP00000224073.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..148
                     /product="endothelial differentiation-related factor 1
                     isoform alpha"
                     /note="multiprotein bridging factor 1"
                     /calculated_mol_wt=16238
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (O60869.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60869.1)"
     Region          5..71
                     /region_name="MBF1"
                     /note="Multiprotein bridging factor 1; pfam08523"
                     /db_xref="CDD:462508"
     Site            25
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O60869.1)"
     Region          33..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60869.1)"
     Region          37..113
                     /region_name="Interaction with NR5A2, PPARG and NR1H3.
                     /evidence=ECO:0000269|PubMed:12040021"
                     /note="propagated from UniProtKB/Swiss-Prot (O60869.1)"
     Region          69..108
                     /region_name="Interaction with TBP and NR5A1.
                     /evidence=ECO:0000269|PubMed:10567391"
                     /note="propagated from UniProtKB/Swiss-Prot (O60869.1)"
     Region          76..132
                     /region_name="aMBF1"
                     /note="Archaeal ribosome-binding protein aMBF1, putative
                     translation factor, contains Zn-ribbon and HTH domains
                     [Translation, ribosomal structure and biogenesis];
                     COG1813"
                     /db_xref="CDD:441418"
     Region          81..88
                     /region_name="IQ motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O60869.1)"
     CDS             1..148
                     /gene="EDF1"
                     /gene_synonym="CFAP280; EDF-1; MBF1"
                     /coded_by="NM_003792.4:51..497"
                     /note="isoform alpha is encoded by transcript variant
                     alpha"
                     /db_xref="CCDS:CCDS7011.1"
                     /db_xref="GeneID:8721"
                     /db_xref="HGNC:HGNC:3164"
                     /db_xref="MIM:605107"
ORIGIN      
        1 maesdwdtvt vlrkkgptaa qakskqaila aqrrgedvet skkwaagqnk qhsitkntak
       61 ldreteelhh drvtlevgkv iqqgrqskgl tqkdlatkin ekpqviadye sgraipnnqv
      121 lgkieraigl klrgkdigkp iekgprak
//
LOCUS       NP_055687                677 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 5 [Homo sapiens].
ACCESSION   NP_055687 XP_376832
VERSION     NP_055687.1
DBSOURCE    REFSEQ: accession NM_014872.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Choi,S.H., Koh,D.I., Ahn,H., Kim,J.Y., Kim,Y. and Hur,M.W.
  TITLE     Cell fate decisions by c-Myc depend on ZBTB5 and p53
  JOURNAL   Biochem Biophys Res Commun 533 (4), 1247-1254 (2020)
   PUBMED   33051058
  REMARK    GeneRIF: Cell fate decisions by c-Myc depend on ZBTB5 and p53.
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Koh,D.I., Choi,W.I., Jeon,B.N., Lee,C.E., Yun,C.O. and Hur,M.W.
  TITLE     A novel POK family transcription factor, ZBTB5, represses
            transcription of p21CIP1 gene
  JOURNAL   J Biol Chem 284 (30), 19856-19866 (2009)
   PUBMED   19491398
  REMARK    GeneRIF: ZBTB5 directly repressed transcription of cell cycle
            arrest gene p21 by binding to the proximal GC-box 5/6 elements and
            the two distal p53-responsive elements (bp -2323 to -2299; bp -1416
            to -1392)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL158155.24, DB457364.1, BC010007.2, AB002352.1 and AW075599.1.
            
            On Mar 22, 2004 this sequence version replaced XP_376832.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB002352.1, SRR1803613.14829.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307750.5/ ENSP00000307604.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.2"
     Protein         1..677
                     /product="zinc finger and BTB domain-containing protein 5"
                     /calculated_mol_wt=74147
     Region          3..128
                     /region_name="BTB_POZ_ZBTB5"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 5 (ZBTB5); cd18196"
                     /db_xref="CDD:349505"
     Region          158..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15062.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15062.1)"
     Region          287..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15062.1)"
     Region          331..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15062.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15062.1)"
     Region          447..474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15062.1)"
     Region          552..585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15062.1)"
     Site            order(597,599,601,603..604,607,620,622,626..627,630..631,
                     634,648,650,652,654..655,658..659,662)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          615..635
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          629..652
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          643..662
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..677
                     /gene="ZBTB5"
                     /coded_by="NM_014872.3:241..2274"
                     /db_xref="CCDS:CCDS6610.1"
                     /db_xref="GeneID:9925"
                     /db_xref="HGNC:HGNC:23836"
                     /db_xref="MIM:616590"
ORIGIN      
        1 mdfpghfeqi fqqlnyqrlh gqlcdcvivv gnrhfkahrs vlaacsthfr alfsvaegdq
       61 tmnmiqldse vvtaeafaal idmmytstlm lgesnvmdvl laashlhlns vvkackhylt
      121 trtlpmspps ervqeqsarm qrsfmlqqlg lsivssalns sqngeeqpap msssmrsnld
      181 qrtpfpmrrl hkrkqsaeer arqrlrpsid esaisdvtpe ngpsgvhsre effspdslki
      241 vdnpkadgmt dnqedsaimf dqsfgtqeda qvpsqsdnsa gnmaqlsmas ratqvetsfd
      301 qeaapekssf qcenpevglg ekehmrvvvk seplsspepq devsdvtsqa egsesveveg
      361 vvvsaekidl spessdrsfs dpqsstdrvg dihilevtnn lehkstfsis nflnksrgnn
      421 ftanqnnddn ipnttsdcrl eseapyllsp eagpaggpss apgshvenpf sepadshfvr
      481 pmqevmglpc vqtsgyqgge qfgmdfsrsg lglhssfsrv migsprggas nfpyyrriap
      541 kmpvvtsvrs sqipenstss qlmmngatss fenghpsqpg ppqltrasad vlskckkals
      601 ehnvlvvega rkyackicck tfltltdckk hirvhtgekp yaclkcgkrf sqsshlykhs
      661 kttclrwqss nlpstll
//
LOCUS       NP_008896                368 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 24 isoform 1 [Homo sapiens].
ACCESSION   NP_008896
VERSION     NP_008896.2
DBSOURCE    REFSEQ: accession NM_006965.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Meng,F., Ai,C., Yan,G. and Wang,G.
  TITLE     Tumor-suppressive zinc finger protein 24 (ZNF24) sensitizes
            colorectal cancer cells to 5-fluorouracil by inhibiting the Wnt
            pathway and activating the p53 signaling
  JOURNAL   Exp Cell Res 433 (1), 113796 (2023)
   PUBMED   37774763
  REMARK    GeneRIF: Tumor-suppressive zinc finger protein 24 (ZNF24)
            sensitizes colorectal cancer cells to 5-fluorouracil by inhibiting
            the Wnt pathway and activating the p53 signaling.
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Liu,Y., Cheng,H., Cheng,C., Zheng,F., Zhao,Z., Chen,Q., Zeng,W.,
            Zhang,P., Huang,C., Jiang,W., Liu,X. and Liu,G.
  TITLE     ZNF191 alters DNA methylation and activates the PI3K-AKT pathway in
            hepatoma cells via transcriptional regulation of DNMT1
  JOURNAL   Cancer Med 11 (5), 1269-1280 (2022)
   PUBMED   35092191
  REMARK    GeneRIF: ZNF191 alters DNA methylation and activates the PI3K-AKT
            pathway in hepatoma cells via transcriptional regulation of DNMT1.
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Liu,Y., Wu,D., Cheng,H., Chen,L., Zhang,W., Zou,L., Gao,Q.,
            Zhao,Z., Chen,Q., Zeng,W., Zhang,Z., Jiang,W., Huang,C. and Liu,G.
  TITLE     Wnt8B, transcriptionally regulated by ZNF191, promotes cell
            proliferation of hepatocellular carcinoma via Wnt signaling
  JOURNAL   Cancer Sci 112 (2), 629-640 (2021)
   PUBMED   33197287
  REMARK    GeneRIF: Wnt8B, transcriptionally regulated by ZNF191, promotes
            cell proliferation of hepatocellular carcinoma via Wnt signaling.
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Albanese,V., Biguet,N.F., Kiefer,H., Bayard,E., Mallet,J. and
            Meloni,R.
  TITLE     Quantitative effects on gene silencing by allelic variation at a
            tetranucleotide microsatellite
  JOURNAL   Hum Mol Genet 10 (17), 1785-1792 (2001)
   PUBMED   11532988
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Han,Z.G., Zhang,Q.H., Ye,M., Kan,L.X., Gu,B.W., He,K.L., Shi,S.L.,
            Zhou,J., Fu,G., Mao,M., Chen,S.J., Yu,L. and Chen,Z.
  TITLE     Molecular cloning of six novel Kruppel-like zinc finger genes from
            hematopoietic cells and identification of a novel transregulatory
            domain KRNB
  JOURNAL   J Biol Chem 274 (50), 35741-35748 (1999)
   PUBMED   10585455
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Williams,A.J., Blacklow,S.C. and Collins,T.
  TITLE     The zinc finger-associated SCAN box is a conserved oligomerization
            domain
  JOURNAL   Mol Cell Biol 19 (12), 8526-8535 (1999)
   PUBMED   10567577
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Rousseau-Merck,M.F., Huebner,K., Berger,R. and Thiesen,H.J.
  TITLE     Chromosomal localization of two human zinc finger protein genes,
            ZNF24 (KOX17) and ZNF29 (KOX26), to 18q12 and 17p13-p12,
            respectively
  JOURNAL   Genomics 9 (1), 154-161 (1991)
   PUBMED   2004757
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116447.10.
            
            On Jun 18, 2008 this sequence version replaced NP_008896.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.15229.1,
                                           SRR1660805.7258.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2155770
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261332.11/ ENSP00000261332.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..368
                     /product="zinc finger protein 24 isoform 1"
                     /note="zinc finger protein 191; zinc finger protein 24
                     (KOX 17); zinc finger protein KOX17; retinoic acid
                     suppression protein A; zinc finger and SCAN
                     domain-containing protein 3"
                     /calculated_mol_wt=42024
     Region          48..160
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Region          <249..329
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          251..301
                     /region_name="Necessary and sufficient for nuclear
                     localization"
                     /note="propagated from UniProtKB/Swiss-Prot (P17028.4)"
     Region          253..273
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(258,260,262,264..265,268..269,272,286,288,292..293,
                     296..297,300,314,316,318,320..321,324..325,328)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Region          281..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Region          305..>358
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          309..329
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Region          337..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..368
                     /gene="ZNF24"
                     /gene_synonym="KOX17; RSG-A; Zfp191; ZNF191; ZSCAN3"
                     /coded_by="NM_006965.4:145..1251"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11912.1"
                     /db_xref="GeneID:7572"
                     /db_xref="HGNC:HGNC:13032"
                     /db_xref="MIM:194534"
ORIGIN      
        1 msaqsveeds iliiptpdee ekilrvklee dpdgeegssi pwnhlpdpei frqrfrqfgy
       61 qdspgpreav sqlrelcrlw lrpethtkeq ilelvvleqf vailpkelqt wvrdhhpeng
      121 eeavtvledl eselddpgqp vslrrrkrev lvedmvsqee aqglpsseld avenqlkwas
      181 welhslrhcd ddgrtengal apkqelpsal eshevpgtln mgvpqifkyg etcfpkgrfe
      241 rkrnpsrkkq hicdecgkhf sqgsalilhq rihsgekpyg cvecgkafsr ssilvqhqrv
      301 htgekpykcl ecgkafsqns glinhqriht gekpyecvqc gksysqssnl frhqrrhnae
      361 kllnvvkv
//
LOCUS       NP_001348496             146 aa            linear   ROD 27-APR-2025
DEFINITION  ras-like protein family member 10B isoform 2 [Mus musculus].
ACCESSION   NP_001348496 XP_006533550
VERSION     NP_001348496.1
DBSOURCE    REFSEQ: accession NM_001361567.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Shigesawa,I., Nakamura,A., Yamauchi,Y., Kawata,S., Miyazaki,A.,
            Nomoto,H., Kameda,H., Terauchi,Y. and Atsumi,T.
  TITLE     Effects of glucokinase haploinsufficiency on the pancreatic
            beta-cell mass and function of long-term high-fat, high-sucrose
            diet-fed mice
  JOURNAL   J Diabetes Investig 15 (12), 1732-1742 (2024)
   PUBMED   39305123
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Rybkin,I.I., Kim,M.S., Bezprozvannaya,S., Qi,X., Richardson,J.A.,
            Plato,C.F., Hill,J.A., Bassel-Duby,R. and Olson,E.N.
  TITLE     Regulation of atrial natriuretic peptide secretion by a novel
            Ras-like protein
  JOURNAL   J Cell Biol 179 (3), 527-537 (2007)
   PUBMED   17984325
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK045997.1, AK158941.1 and AW456843.1.
            
            On Mar 29, 2018 this sequence version replaced XP_006533550.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK045997.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849378, SAMN00849379
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 50.3 cM"
     Protein         1..146
                     /product="ras-like protein family member 10B isoform 2"
                     /EC_number="3.6.5.2"
                     /note="ras-like protein family member 10B"
                     /calculated_mol_wt=16095
     Region          5..>117
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            11..18
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133342"
     Region          33..42
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
     Site            36
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133342"
     Site            40..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133342"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133342"
     Site            order(61..62,86..87)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133342"
     CDS             1..146
                     /gene="Rasl10b"
                     /gene_synonym="B230331P10Rik; Gm729; VTS58635"
                     /coded_by="NM_001361567.1:336..776"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS88208.1"
                     /db_xref="GeneID:276952"
                     /db_xref="MGI:MGI:2685575"
ORIGIN      
        1 mvstyrvavl gargvgksai vrqflynefs evcvptttrr lylpavvmng hvhdlqildf
       61 ppisafpvnt lqewadaccr glrsvhayil vydiccfdsf eyvktirqqi letrgwgctw
      121 nrahasaeps gcetgsapkf lpppag
//
LOCUS       NP_060193                423 aa            linear   PRI 27-APR-2025
DEFINITION  torsin-4A [Homo sapiens].
ACCESSION   NP_060193 XP_001130541
VERSION     NP_060193.2
DBSOURCE    REFSEQ: accession NM_017723.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Wang,Q., Li,Y., Li,J., Yao,Z., Ma,X. and Ma,J.W.
  TITLE     Delta and Notch-like epidermal growth factor-related receptor
            suppresses human glioma growth by inhibiting oncogene TOR4A
  JOURNAL   J Cancer Res Ther 18 (5), 1372-1379 (2022)
   PUBMED   36204885
  REMARK    GeneRIF: Delta and Notch-like epidermal growth factor-related
            receptor suppresses human glioma growth by inhibiting oncogene
            TOR4A.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX255925.17, AK000252.1 and AK000392.1.
            
            On Oct 12, 2006 this sequence version replaced NP_060193.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000252.1, DB226617.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357503.3/ ENSP00000350102.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..423
                     /product="torsin-4A"
                     /note="torsin family protein C9orf167"
                     /calculated_mol_wt=46783
     Region          47..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXH8.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NXH8.2)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NXH8.2)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NXH8.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NXH8.2)"
     Site            122..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXH8.2)"
     Region          149..253
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     CDS             1..423
                     /gene="TOR4A"
                     /gene_synonym="C9orf167"
                     /coded_by="NM_017723.3:220..1491"
                     /db_xref="CCDS:CCDS7041.1"
                     /db_xref="GeneID:54863"
                     /db_xref="HGNC:HGNC:25981"
ORIGIN      
        1 mdrgqpslep aaaaprasgr cviapvravl rlrrrvcvlr krrllqpggg pdvgtgaprp
       61 gcspraprad ldqpkfftfd spaelpsrtp rkkrrrsrlv lypetsrkyr prvehrsraq
      121 rcllllvaiv gfqvlnaien lddnaqrydl dglekalqra vfgqpaavsr ivalmrdyla
      181 thvhsrplll alhgpsgvgk shvgrllarh frsvledsal vlqyharhhc pearaaqdcr
      241 eelarrvadv varaeaeekt pllvlddvel mprplldelh gflqpqrshh fhnaiyvlls
      301 gaggaevtrf vlqnasralp lrpdgfrsae aaaaqaeedl rasllavlsr ehplwqaaai
      361 vpfllldkrd vvscfrdema gegffpdqar aenlaaqlsf yrvagrefav tgckqvvatv
      421 nll
//
LOCUS       NP_067317                170 aa            linear   ROD 27-APR-2025
DEFINITION  potassium voltage-gated channel subfamily E member 4 [Mus
            musculus].
ACCESSION   NP_067317
VERSION     NP_067317.1
DBSOURCE    REFSEQ: accession NM_021342.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Mano,R., Tanaka,T., Hashiguchi,S., Takahashi,H., Sakata,N.,
            Kondo,S. and Kodama,S.
  TITLE     Induction of potassium channel regulator KCNE4 in a submandibular
            lymph node metastasis model
  JOURNAL   Sci Rep 12 (1), 13208 (2022)
   PUBMED   35915077
  REMARK    GeneRIF: Induction of potassium channel regulator KCNE4 in a
            submandibular lymph node metastasis model.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Vallejo-Gracia,A., Sastre,D., Colomer-Molera,M., Sole,L.,
            Navarro-Perez,M., Capera,J., Roig,S.R., Pedros-Gamez,O.,
            Estadella,I., Szilagyi,O., Panyi,G., Hajdu,P. and Felipe,A.
  TITLE     KCNE4-dependent functional consequences of Kv1.3-related leukocyte
            physiology
  JOURNAL   Sci Rep 11 (1), 14632 (2021)
   PUBMED   34272451
  REMARK    GeneRIF: KCNE4-dependent functional consequences of Kv1.3-related
            leukocyte physiology.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Sole,L., Sastre,D., Colomer-Molera,M., Vallejo-Gracia,A.,
            Roig,S.R., Perez-Verdaguer,M., Lillo,P., Tamkun,M.M. and Felipe,A.
  TITLE     Functional Consequences of the Variable Stoichiometry of the
            Kv1.3-KCNE4 Complex
  JOURNAL   Cells 9 (5), 1128 (2020)
   PUBMED   32370164
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Estrada,S.M., Thagard,A.S., Dehart,M.J., Damicis,J.R.,
            Dornisch,E.M., Ippolito,D.L., Burd,I., Napolitano,P.G. and
            Ieronimakis,N.
  TITLE     The orphan nuclear receptor Nr4a1 mediates perinatal
            neuroinflammation in a murine model of preterm labor
  JOURNAL   Cell Death Dis 11 (1), 11 (2020)
   PUBMED   31907354
  REMARK    Erratum:[Cell Death Dis. 2020 Jun 30;11(6):495. doi:
            10.1038/s41419-020-2682-y. PMID: 32606386]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Sole,L., Roig,S.R., Sastre,D., Vallejo-Gracia,A.,
            Serrano-Albarras,A., Ferrer-Montiel,A., Fernandez-Ballester,G.,
            Tamkun,M.M. and Felipe,A.
  TITLE     The calmodulin-binding tetraleucine motif of KCNE4 is responsible
            for association with Kv1.3
  JOURNAL   FASEB J 33 (7), 8263-8279 (2019)
   PUBMED   30969795
  REMARK    GeneRIF: experimental data and the in silico structure suggest that
            the KCNE4 interaction hides a forward-trafficking motif within
            Kv1.3 in addition to adding a strong endoplasmic reticulum
            retention signature to the Kv1.3-KCNE4 complex.
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Grunnet,M., Olesen,S.P., Klaerke,D.A. and Jespersen,T.
  TITLE     hKCNE4 inhibits the hKCNQ1 potassium current without affecting the
            activation kinetics
  JOURNAL   Biochem Biophys Res Commun 328 (4), 1146-1153 (2005)
   PUBMED   15707997
  REMARK    GeneRIF: Based upon previous studies and the present results, it is
            concluded that both hKCNE4 and mKCNE4 have a drastic inhibitory
            impact on both hKCNQ1 and mKCNQ1 currents.
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Grunnet,M., Rasmussen,H.B., Hay-Schmidt,A., Rosenstierne,M.,
            Klaerke,D.A., Olesen,S.P. and Jespersen,T.
  TITLE     KCNE4 is an inhibitory subunit to Kv1.1 and Kv1.3 potassium
            channels
  JOURNAL   Biophys J 85 (3), 1525-1537 (2003)
   PUBMED   12944270
  REMARK    GeneRIF: KCNE4 beta-subunit has a drastic inhibitory effect on
            currents generated by Kv1.1 and Kv1.3 potassium channels
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Boettger-Tong,H.L., Rohozinski,J., Agoulnik,A.I., Dohmae,K.,
            Nishimune,Y., Levy,N. and Bishop,C.E.
  TITLE     Identification and sequencing the juvenile spermatogonial depletion
            critical interval on mouse chromosome 1 reveals the presence of
            eight candidate genes
  JOURNAL   Biochem Biophys Res Commun 288 (5), 1129-1135 (2001)
   PUBMED   11700028
REFERENCE   9  (residues 1 to 170)
  AUTHORS   Abbott,G.W., Sesti,F., Splawski,I., Buck,M.E., Lehmann,M.H.,
            Timothy,K.W., Keating,M.T. and Goldstein,S.A.
  TITLE     MiRP1 forms IKr potassium channels with HERG and is associated with
            cardiac arrhythmia
  JOURNAL   Cell 97 (2), 175-187 (1999)
   PUBMED   10219239
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Vullhorst,D., Klocke,R., Bartsch,J.W. and Jockusch,H.
  TITLE     Expression of the potassium channel KV3.4 in mouse skeletal muscle
            parallels fiber type maturation and depends on excitation pattern
  JOURNAL   FEBS Lett 421 (3), 259-262 (1998)
   PUBMED   9468318
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK133469.1 and BE948375.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY328498.1, BC032920.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 40.89 cM"
     Protein         1..170
                     /product="potassium voltage-gated channel subfamily E
                     member 4"
                     /note="minK-related peptide 3; potassium channel subunit
                     beta MiRP3; minimum potassium ion channel-related peptide
                     3"
                     /calculated_mol_wt=18508
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTW3.1)"
     Site            8
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WTW3.1)"
     Region          17..>64
                     /region_name="ISK_Channel"
                     /note="Slow voltage-gated potassium channel; pfam02060"
                     /db_xref="CDD:460432"
     Site            28
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WTW3.1)"
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTW3.1)"
     Region          121..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTW3.1)"
     CDS             1..170
                     /gene="Kcne4"
                     /gene_synonym="MiRP3"
                     /coded_by="NM_021342.2:113..625"
                     /db_xref="CCDS:CCDS15088.1"
                     /db_xref="GeneID:57814"
                     /db_xref="MGI:MGI:1891125"
ORIGIN      
        1 mlrmeplnst ypsaaasssp leshvpsnss gngneyfyil vvmsfygvfl igimlgymks
       61 krrekkssll llykdeerlw geamkplpmm sglrsgqvpm mlnmlqesva palsctlcsm
      121 egdsvssess spdvhlpiqe egaddeleet setplndsse gssenihqns
//
LOCUS       NP_001265485             178 aa            linear   PRI 27-APR-2025
DEFINITION  actin-related protein 2/3 complex subunit 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001265485 NP_005710
VERSION     NP_001265485.1
DBSOURCE    REFSEQ: accession NM_001278556.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Zhao,X., Yang,Z., Qian,M. and Zhu,X.
  TITLE     Interactions among subunits of human Arp2/3 complex: p20-Arc as the
            hub
  JOURNAL   Biochem Biophys Res Commun 280 (2), 513-517 (2001)
   PUBMED   11162547
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Marchand,J.B., Kaiser,D.A., Pollard,T.D. and Higgs,H.N.
  TITLE     Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3
            complex
  JOURNAL   Nat Cell Biol 3 (1), 76-82 (2001)
   PUBMED   11146629
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Machesky,L.M., Reeves,E., Wientjes,F., Mattheyse,F.J., Grogan,A.,
            Totty,N.F., Burlingame,A.L., Hsuan,J.J. and Segal,A.W.
  TITLE     Mammalian actin-related protein 2/3 complex localizes to regions of
            lamellipodial protrusion and is composed of evolutionarily
            conserved proteins
  JOURNAL   Biochem J 328 (Pt 1) (Pt 1), 105-112 (1997)
   PUBMED   9359840
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Welch,M.D., DePace,A.H., Verma,S., Iwamatsu,A. and Mitchison,T.J.
  TITLE     The human Arp2/3 complex is composed of evolutionarily conserved
            subunits and is localized to cellular regions of dynamic actin
            filament assembly
  JOURNAL   J Cell Biol 138 (2), 375-384 (1997)
   PUBMED   9230079
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Welch,M.D., Iwamatsu,A. and Mitchison,T.J.
  TITLE     Actin polymerization is induced by Arp2/3 protein complex at the
            surface of Listeria monocytogenes
  JOURNAL   Nature 385 (6613), 265-269 (1997)
   PUBMED   9000076
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF434378.1, BC067747.1,
            AI144468.1 and AC144548.8.
            
            On Dec 10, 2013 this sequence version replaced NP_005710.1.
            
            Summary: This gene encodes one of seven subunits of the human
            Arp2/3 protein complex. The Arp2/3 protein complex has been
            conserved through evolution and is implicated in the control of
            actin polymerization in cells. Alternatively spliced transcript
            variants have been found for this gene. [provided by RefSeq, Dec
            2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.121631.1,
                                           SRR5189658.196420.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000228825.12/ ENSP00000228825.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..178
                     /product="actin-related protein 2/3 complex subunit 3
                     isoform 1"
                     /note="ARP2/3 protein complex subunit p21; arp2/3 complex
                     21 kDa subunit; actin related protein 2/3 complex, subunit
                     3, 21kDa"
                     /calculated_mol_wt=20416
     Region          1..173
                     /region_name="P21-Arc"
                     /note="ARP2/3 complex ARPC3 (21 kDa) subunit; pfam04062"
                     /db_xref="CDD:461152"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O15145.3)"
     Site            56
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15145.3)"
     Site            61
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15145.3)"
     CDS             1..178
                     /gene="ARPC3"
                     /gene_synonym="ARC21; p21-Arc"
                     /coded_by="NM_001278556.2:78..614"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9146.1"
                     /db_xref="GeneID:10094"
                     /db_xref="HGNC:HGNC:706"
                     /db_xref="MIM:604225"
ORIGIN      
        1 mpayhsslmd pdtklignma llpirsqfkg papretkdtd ivdeaiyyfk anvffknyei
       61 kneadrtliy itlyiseclk klqkcnsksq gekemytlgi tnfpipgepg fplnaiyakp
      121 ankqedevmr aylqqlrqet glrlcekvfd pqndkpskww tcfvkrqfmn kslsgpgq
//
LOCUS       NP_058539                475 aa            linear   ROD 27-APR-2025
DEFINITION  ataxin-10 [Mus musculus].
ACCESSION   NP_058539
VERSION     NP_058539.2
DBSOURCE    REFSEQ: accession NM_016843.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Bentley-Ford,M.R., Andersen,R.S., Croyle,M.J., Haycraft,C.J.,
            Clearman,K.R., Foote,J.B., Reiter,J.F. and Yoder,B.K.
  TITLE     ATXN10 Is Required for Embryonic Heart Development and Maintenance
            of Epithelial Cell Phenotypes in the Adult Kidney and Pancreas
  JOURNAL   Front Cell Dev Biol 9, 705182 (2021)
   PUBMED   34970537
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Khang,R., Jo,A., Kang,H., Kim,H., Kwag,E., Lee,J.Y., Koo,O.,
            Park,J., Kim,H.K., Jo,D.G., Hwang,I., Ahn,J.Y., Lee,Y., Choi,J.Y.,
            Lee,Y.S. and Shin,J.H.
  TITLE     Loss of zinc-finger protein 212 leads to Purkinje cell death and
            locomotive abnormalities with phospholipase D3 downregulation
  JOURNAL   Sci Rep 11 (1), 22745 (2021)
   PUBMED   34815492
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Andrali,S.S., Marz,P. and Ozcan,S.
  TITLE     Ataxin-10 interacts with O-GlcNAc transferase OGT in pancreatic
            beta cells
  JOURNAL   Biochem Biophys Res Commun 337 (1), 149-153 (2005)
   PUBMED   16182253
  REMARK    GeneRIF: Ataxin-10, encoded by the SCA10 gene, interacts with
            O-linked N-acetylglucosamine in vivo and is modified by O-linked
            glycosylation in the insulinoma MIN6 cell line.
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Lopez-Fernandez,L.A., Parraga,M. and del Mazo,J.
  TITLE     Tex261, a novel gene presumably related but distinct from
            steroidogenic acute regulatory (StAR) gene, is regulated during the
            development of germ cells
  JOURNAL   Biochem Biophys Res Commun 242 (3), 565-569 (1998)
   PUBMED   9464256
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Lopez-Fernandez,L.A. and del Mazo,J.
  TITLE     Characterization of genes expressed early in mouse spermatogenesis,
            isolated from a subtractive cDNA library
  JOURNAL   Mamm Genome 7 (9), 698-700 (1996)
   PUBMED   8703127
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Zoppe,M., Frattini,A., Faranda,S. and Vezzoni,P.
  TITLE     The complete sequence of the host cell factor 1 (HCFC1) gene and
            its promoter: a role for YY1 transcription factor in the regulation
            of its expression
  JOURNAL   Genomics 34 (1), 85-91 (1996)
   PUBMED   8661027
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Kato,K.
  TITLE     A Collection of cDNA Clones with Specific Expression Patterns in
            Mouse Brain
  JOURNAL   Eur J Neurosci 2 (8), 704-711 (1990)
   PUBMED   12106288
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC046802.1, AK153271.1 and BQ176715.1.
            
            On Dec 15, 2005 this sequence version replaced NP_058539.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK161950.1, AK153271.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 40.32 cM"
     Protein         1..475
                     /product="ataxin-10"
                     /note="brain protein E46; spinocerebellar ataxia type 10
                     protein homolog; testis expressed gene 169"
                     /calculated_mol_wt=53576
     Site            10
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P28658.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBB4; propagated from
                     UniProtKB/Swiss-Prot (P28658.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBB4; propagated from
                     UniProtKB/Swiss-Prot (P28658.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBB4; propagated from
                     UniProtKB/Swiss-Prot (P28658.2)"
     Region          370..467
                     /region_name="Atx10homo_assoc"
                     /note="Spinocerebellar ataxia type 10 protein domain;
                     pfam09759"
                     /db_xref="CDD:462885"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBB4; propagated from
                     UniProtKB/Swiss-Prot (P28658.2)"
     CDS             1..475
                     /gene="Atxn10"
                     /gene_synonym="E46; Sca10; TEG-169; Tex169"
                     /coded_by="NM_016843.4:211..1638"
                     /db_xref="CCDS:CCDS37170.1"
                     /db_xref="GeneID:54138"
                     /db_xref="MGI:MGI:1859293"
ORIGIN      
        1 maaprmppsr lsgimvpapi qdlealralt alfkeqrnre taprtifqrv ldilkkstha
       61 velacrdpsq vehlasslql itecfrclrn aciecsvnqn sirnldtigv avdlvllfre
      121 lrveqdsllt afrcglqflg nvasrneesq sivwvhafpe lfmsclnhpd kkivaycsmi
      181 lftslnaerm kdleenlnia invieahqkh pasewpflii sdhflkspel veamygklsn
      241 qeritlldiv iaklvgeeql tkddisifvr haeliansfm dqcrnvlklt sephtedkea
      301 lvtirlldvl cemtsntell gylqvfpglm ervidvlrvi hevgkestni fspsdslkae
      361 gdiehmtegf kshlirlign lcyknkenqd kvneldgipl ildssniddn npfmmqwvvy
      421 avrnltedns qnqdviakme eqgladasll kkmgfeieks gdklilksnn dippp
//
LOCUS       NP_001348280             125 aa            linear   ROD 27-APR-2025
DEFINITION  syntaxin-8 isoform 3 [Mus musculus].
ACCESSION   NP_001348280
VERSION     NP_001348280.1
DBSOURCE    REFSEQ: accession NM_001361351.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Castonguay,J., Orth,J.H.C., Muller,T., Sleman,F., Grimm,C.,
            Wahl-Schott,C., Biel,M., Mallmann,R.T., Bildl,W., Schulte,U. and
            Klugbauer,N.
  TITLE     The two-pore channel TPC1 is required for efficient protein
            processing through early and recycling endosomes
  JOURNAL   Sci Rep 7 (1), 10038 (2017)
   PUBMED   28855648
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Raspa,M., Guan,M., Paoletti,R., Montoliu,L., Ayadi,A.,
            Marschall,S., Fray,M. and Scavizzi,F.
  CONSRTM   EMMA/Infrafrontier Technical Working Group
  TITLE     Dry ice is a reliable substrate for the distribution of frozen
            mouse spermatozoa: A multi-centric study
  JOURNAL   Theriogenology 96, 49-57 (2017)
   PUBMED   28532839
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Golebiewska,E.M., Harper,M.T., Williams,C.M., Savage,J.S.,
            Goggs,R., Fischer von Mollard,G. and Poole,A.W.
  TITLE     Syntaxin 8 regulates platelet dense granule secretion, aggregation,
            and thrombus stability
  JOURNAL   J Biol Chem 290 (3), 1536-1545 (2015)
   PUBMED   25404741
  REMARK    GeneRIF: Syntaxin 8 has a role in regulating platelet dense granule
            secretion, aggregation, and thrombus stability
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Pirooz,S.D., He,S., Zhang,T., Zhang,X., Zhao,Z., Oh,S.,
            O'Connell,D., Khalilzadeh,P., Amini-Bavil-Olyaee,S., Farzan,M. and
            Liang,C.
  TITLE     UVRAG is required for virus entry through combinatorial interaction
            with the class C-Vps complex and SNAREs
  JOURNAL   Proc Natl Acad Sci U S A 111 (7), 2716-2721 (2014)
   PUBMED   24550300
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Zhang,L., Kang,L., Bond,W. and Zhang,N.
  TITLE     Interaction between syntaxin 8 and HECTd3, a HECT domain ligase
  JOURNAL   Cell Mol Neurobiol 29 (1), 115-121 (2009)
   PUBMED   18821010
  REMARK    GeneRIF: Syntaxin 8 and HECTd3 have similar subcellular
            localization.
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Salazar,G., Craige,B., Styers,M.L., Newell-Litwa,K.A.,
            Doucette,M.M., Wainer,B.H., Falcon-Perez,J.M., Dell'Angelica,E.C.,
            Peden,A.A., Werner,E. and Faundez,V.
  TITLE     BLOC-1 complex deficiency alters the targeting of adaptor protein
            complex-3 cargoes
  JOURNAL   Mol Biol Cell 17 (9), 4014-4026 (2006)
   PUBMED   16760431
REFERENCE   9  (residues 1 to 125)
  AUTHORS   MacLaren,E.J., Bennett,B., Johnson,T.E. and Sikela,J.M.
  TITLE     Expression profiling identifies novel candidate genes for ethanol
            sensitivity QTLs
  JOURNAL   Mamm Genome 17 (2), 147-156 (2006)
   PUBMED   16465594
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Kim,B.Y., Ueda,M., Kominami,E., Akagawa,K., Kohsaka,S. and
            Akazawa,C.
  TITLE     Identification of mouse Vps16 and biochemical characterization of
            mammalian class C Vps complex
  JOURNAL   Biochem Biophys Res Commun 311 (3), 577-582 (2003)
   PUBMED   14623309
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK003297.1, AK018716.1 and BC048167.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK018716.1, ERR3363660.2672252.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 41.2 cM"
     Protein         1..125
                     /product="syntaxin-8 isoform 3"
                     /note="syntaxin-like protein 3I35"
                     /calculated_mol_wt=13975
     Region          41..95
                     /region_name="SNARE_Syntaxin8"
                     /note="SNARE motif of syntaxin 8; cd15852"
                     /db_xref="CDD:277205"
     Site            order(43..44,46..48,50..51,53..55,57..62,64..69,71..72,
                     74..76,78..80,82..83,85..87,89..90,92..94)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277205"
     Site            68
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277205"
     CDS             1..125
                     /gene="Stx8"
                     /gene_synonym="0610007H08Rik; 1110002H11Rik;
                     4930571E13Rik; CARB"
                     /coded_by="NM_001361351.1:210..587"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:55943"
                     /db_xref="MGI:MGI:1890156"
ORIGIN      
        1 mseeakrgtp npwlceepee trglgfdeir qqqqkiiqeq dagldalssi isrqkqmgqe
       61 igneldeqne iiddlanlve ntdeklrtea rrvtlvdrks tscgmimvil lllvaivvva
      121 vwptn
//
LOCUS       NP_009098               1325 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger MYM-type protein 6 [Homo sapiens].
ACCESSION   NP_009098
VERSION     NP_009098.3
DBSOURCE    REFSEQ: accession NM_007167.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1325)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 1325)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 1325)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1325)
  AUTHORS   Hayward,A., Ghazal,A., Andersson,G., Andersson,L. and Jern,P.
  TITLE     ZBED evolution: repeated utilization of DNA transposons as
            regulators of diverse host functions
  JOURNAL   PLoS One 8 (3), e59940 (2013)
   PUBMED   23533661
REFERENCE   5  (residues 1 to 1325)
  AUTHORS   Bai,S.W., Herrera-Abreu,M.T., Rohn,J.L., Racine,V., Tajadura,V.,
            Suryavanshi,N., Bechtel,S., Wiemann,S., Baum,B. and Ridley,A.J.
  TITLE     Identification and characterization of a set of conserved and new
            regulators of cytoskeletal organization, cell morphology and
            migration
  JOURNAL   BMC Biol 9, 54 (2011)
   PUBMED   21834987
  REMARK    Erratum:[BMC Biol. 2024 Oct 10;22(1):228. doi:
            10.1186/s12915-024-02036-3. PMID: 39390519]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1325)
  AUTHORS   Smedley,D., Hamoudi,R., Lu,Y.J., Cooper,C. and Shipley,J.
  TITLE     Cloning and mapping of members of the MYM family
  JOURNAL   Genomics 60 (2), 244-247 (1999)
   PUBMED   10486218
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC068534.1, BC107880.1 and AL833263.1.
            
            On Oct 4, 2006 this sequence version replaced NP_009098.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.122074.1,
                                           SRR1660805.52459.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357182.9/ ENSP00000349708.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1325
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..1325
                     /product="zinc finger MYM-type protein 6"
                     /note="zinc finger protein 258; transposon-derived Buster2
                     transposase-like protein; zinc finger, BED-type containing
                     7; zinc finger, MYM-type 6"
                     /calculated_mol_wt=147958
     Region          134..174
                     /region_name="zf-FCS"
                     /note="MYM-type Zinc finger with FCS sequence motif;
                     pfam06467"
                     /db_xref="CDD:428958"
     Region          193..228
                     /region_name="TRASH"
                     /note="metallochaperone-like domain; smart00746"
                     /db_xref="CDD:214799"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95789.2)"
     Region          665..733
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95789.2)"
     Region          <873..992
                     /region_name="DUF4371"
                     /note="Domain of unknown function (DUF4371); cl46273"
                     /db_xref="CDD:480613"
     CDS             1..1325
                     /gene="ZMYM6"
                     /gene_synonym="Buster2; MYM; ZBED7; ZNF198L4; ZNF258"
                     /coded_by="NM_007167.4:206..4183"
                     /db_xref="CCDS:CCDS387.2"
                     /db_xref="GeneID:9204"
                     /db_xref="HGNC:HGNC:13050"
                     /db_xref="MIM:613567"
ORIGIN      
        1 mkepldgecg kavvpqqell dkikeepdna qeygcvqqpk tqesklkigg vssvnerpia
       61 qqlnpgfqls fassgpsvll psvpavaikv fcsgckkmly kgqtayhktg stqlfcstrc
      121 itrhsspacl ppppkktctn cskdilnpkd vittrfensy pskdfcsqsc lssyelkkkp
      181 vvtiytksis tkcsmcqkna dtrfevkyqn vvhglcsdac fskfhstnnl tmnccencgs
      241 ycysssgpcq sqkvfsstsv taykqnsaqi ppyalgkslr psaemiettn dsgktelfcs
      301 inclsayrvk tvtssgvqvs chscktsaip qyhlamsngt iysfcssscv vafqnvfskp
      361 kgtnssavpl sqgqvvvspp ssrsavsigg gntsavspss irgsaaaslq plaeqsqqva
      421 lthtvvklkc qhcnhlfatk pellfykgkm flfcgkncsd eykkknkvva mcdycklqki
      481 iketvrfsgv dkpfcsevck flsardfger wgnyckmcsy csqtspnlve nrlegkleef
      541 ccedcmskft vlfyqmakcd gckrqgklse sikwrgnikh fcnlfcvlef chqqimndcl
      601 pqnkvniska ktavtelpsa rtdttpvits vmslakipat lstgntnsvl kgavtkeaak
      661 iiqdestqed amkfpssqss qpsrllknkg isckpvtqtk atsckphtqh kecqtdlpmp
      721 nekndaelds ppskkkrlgf fqtydteylk vgfiicpgsk essprpqcvi cgeilssenm
      781 kpanlshhlk tkhselenkp vdffeqksle mecqnsslkk cllvekslvk asyliafqta
      841 askkpfsiae elikpylvem csevlgssag dkmktiplsn vtiqhridel sadiedqliq
      901 kvreskwfal qidesseisn itlllcyirf idydcrdvke ellfciempt qitgfeifel
      961 inkyidsksl nwkhcvglct dgaasmtgry sglkakiqev amntaafthc fihrerlvae
     1021 klspclhkil lqsaqilsfi ksnalnsrml tilceemgse hvslplhaev rwisrgrmlk
     1081 rlfelrheie iflsqkhsdl akyfhdeewv gklaylsdif slinelnlsl qgtlttffnl
     1141 cnkidvfkrk lkmwlkrtqe ndydmfpsfs efsnssglnm tditriifeh leglsqvfsd
     1201 cfppeqdlrs gnlwiihpfm nhqnnnltdf eeekltelss dlglqalfks vsvtqfwina
     1261 ktsypelher amkfllpfst vylcdaafsa lteskqknll gsgpalrlav tslipriekl
     1321 vkeke
//
LOCUS       NP_061238                236 aa            linear   ROD 27-APR-2025
DEFINITION  syntaxin-8 isoform 1 [Mus musculus].
ACCESSION   NP_061238 XP_922213 XP_929775 XP_929782 XP_929789 XP_929797
            XP_929801 XP_929804 XP_929806
VERSION     NP_061238.1
DBSOURCE    REFSEQ: accession NM_018768.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Castonguay,J., Orth,J.H.C., Muller,T., Sleman,F., Grimm,C.,
            Wahl-Schott,C., Biel,M., Mallmann,R.T., Bildl,W., Schulte,U. and
            Klugbauer,N.
  TITLE     The two-pore channel TPC1 is required for efficient protein
            processing through early and recycling endosomes
  JOURNAL   Sci Rep 7 (1), 10038 (2017)
   PUBMED   28855648
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Raspa,M., Guan,M., Paoletti,R., Montoliu,L., Ayadi,A.,
            Marschall,S., Fray,M. and Scavizzi,F.
  CONSRTM   EMMA/Infrafrontier Technical Working Group
  TITLE     Dry ice is a reliable substrate for the distribution of frozen
            mouse spermatozoa: A multi-centric study
  JOURNAL   Theriogenology 96, 49-57 (2017)
   PUBMED   28532839
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Golebiewska,E.M., Harper,M.T., Williams,C.M., Savage,J.S.,
            Goggs,R., Fischer von Mollard,G. and Poole,A.W.
  TITLE     Syntaxin 8 regulates platelet dense granule secretion, aggregation,
            and thrombus stability
  JOURNAL   J Biol Chem 290 (3), 1536-1545 (2015)
   PUBMED   25404741
  REMARK    GeneRIF: Syntaxin 8 has a role in regulating platelet dense granule
            secretion, aggregation, and thrombus stability
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Pirooz,S.D., He,S., Zhang,T., Zhang,X., Zhao,Z., Oh,S.,
            O'Connell,D., Khalilzadeh,P., Amini-Bavil-Olyaee,S., Farzan,M. and
            Liang,C.
  TITLE     UVRAG is required for virus entry through combinatorial interaction
            with the class C-Vps complex and SNAREs
  JOURNAL   Proc Natl Acad Sci U S A 111 (7), 2716-2721 (2014)
   PUBMED   24550300
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Zhang,L., Kang,L., Bond,W. and Zhang,N.
  TITLE     Interaction between syntaxin 8 and HECTd3, a HECT domain ligase
  JOURNAL   Cell Mol Neurobiol 29 (1), 115-121 (2009)
   PUBMED   18821010
  REMARK    GeneRIF: Syntaxin 8 and HECTd3 have similar subcellular
            localization.
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Salazar,G., Craige,B., Styers,M.L., Newell-Litwa,K.A.,
            Doucette,M.M., Wainer,B.H., Falcon-Perez,J.M., Dell'Angelica,E.C.,
            Peden,A.A., Werner,E. and Faundez,V.
  TITLE     BLOC-1 complex deficiency alters the targeting of adaptor protein
            complex-3 cargoes
  JOURNAL   Mol Biol Cell 17 (9), 4014-4026 (2006)
   PUBMED   16760431
REFERENCE   9  (residues 1 to 236)
  AUTHORS   MacLaren,E.J., Bennett,B., Johnson,T.E. and Sikela,J.M.
  TITLE     Expression profiling identifies novel candidate genes for ethanol
            sensitivity QTLs
  JOURNAL   Mamm Genome 17 (2), 147-156 (2006)
   PUBMED   16465594
REFERENCE   10 (residues 1 to 236)
  AUTHORS   Kim,B.Y., Ueda,M., Kominami,E., Akagawa,K., Kohsaka,S. and
            Akazawa,C.
  TITLE     Identification of mouse Vps16 and biochemical characterization of
            mammalian class C Vps complex
  JOURNAL   Biochem Biophys Res Commun 311 (3), 577-582 (2003)
   PUBMED   14623309
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK003297.1 and BC048167.1.
            
            On or before Dec 7, 2005 this sequence version replaced
            XP_929775.1, XP_922213.1, XP_929782.1, XP_929789.1, XP_929797.1,
            XP_929801.1, XP_929804.1, XP_929806.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC048167.1, AK003297.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 41.2 cM"
     Protein         1..236
                     /product="syntaxin-8 isoform 1"
                     /note="syntaxin-like protein 3I35"
                     /calculated_mol_wt=26794
     Region          152..206
                     /region_name="SNARE_Syntaxin8"
                     /note="SNARE motif of syntaxin 8; cd15852"
                     /db_xref="CDD:277205"
     Site            order(154..155,157..159,161..162,164..166,168..173,
                     175..180,182..183,185..187,189..191,193..194,196..198,
                     200..201,203..205)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277205"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319; propagated from
                     UniProtKB/Swiss-Prot (O88983.1)"
     Site            179
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277205"
     Site            216..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88983.1)"
     CDS             1..236
                     /gene="Stx8"
                     /gene_synonym="0610007H08Rik; 1110002H11Rik;
                     4930571E13Rik; CARB"
                     /coded_by="NM_018768.3:44..754"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS24863.1"
                     /db_xref="GeneID:55943"
                     /db_xref="MGI:MGI:1890156"
ORIGIN      
        1 mapdpwfsty dstcqiaqei aekiqernqc errgektpkl tltirtllkn lkvkidllkd
       61 lllravstrq itqlegdrrq nllddlvtre rlllasfkne gaepdlirss lmseeakrgt
      121 pnpwlceepe etrglgfdei rqqqqkiiqe qdagldalss iisrqkqmgq eigneldeqn
      181 eiiddlanlv entdeklrte arrvtlvdrk stscgmimvi llllvaivvv avwptn
//
LOCUS       NP_001356533             562 aa            linear   PRI 27-APR-2025
DEFINITION  suppressor of tumorigenicity 7 protein isoform 9 [Homo sapiens].
ACCESSION   NP_001356533
VERSION     NP_001356533.1
DBSOURCE    REFSEQ: accession NM_001369604.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Liu,H., Lu,W., He,H., Wu,J., Zhang,C., Gong,H. and Yang,C.
  TITLE     Inflammation-dependent overexpression of c-Myc enhances CRL4DCAF4
            E3 ligase activity and promotes ubiquitination of ST7 in
            colitis-associated cancer
  JOURNAL   J Pathol 248 (4), 464-475 (2019)
   PUBMED   30945288
  REMARK    GeneRIF: Inflammation-dependent overexpression of c-Myc enhances
            CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7
            in colitis-associated cancer.
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Yan,F., Alinari,L., Lustberg,M.E., Martin,L.K.,
            Cordero-Nieves,H.M., Banasavadi-Siddegowda,Y., Virk,S.,
            Barnholtz-Sloan,J., Bell,E.H., Wojton,J., Jacob,N.K.,
            Chakravarti,A., Nowicki,M.O., Wu,X., Lapalombella,R., Datta,J.,
            Yu,B., Gordon,K., Haseley,A., Patton,J.T., Smith,P.L., Ryu,J.,
            Zhang,X., Mo,X., Marcucci,G., Nuovo,G., Kwon,C.H., Byrd,J.C.,
            Chiocca,E.A., Li,C., Sif,S., Jacob,S., Lawler,S., Kaur,B. and
            Baiocchi,R.A.
  TITLE     Genetic validation of the protein arginine methyltransferase PRMT5
            as a candidate therapeutic target in glioblastoma
  JOURNAL   Cancer Res 74 (6), 1752-1765 (2014)
   PUBMED   24453002
  REMARK    GeneRIF: The tumor suppressor ST7 is a key gene silenced by PRMT5.
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Hu,L., Wu,C., Zhao,X., Heist,R., Su,L., Zhao,Y., Han,B., Cao,S.,
            Chu,M., Dai,J., Dong,J., Shu,Y., Xu,L., Chen,Y., Wang,Y., Lu,F.,
            Jiang,Y., Yu,D., Chen,H., Tan,W., Ma,H., Chen,J., Jin,G., Wu,T.,
            Lu,D., Christiani,D.C., Lin,D., Hu,Z. and Shen,H.
  TITLE     Genome-wide association study of prognosis in advanced non-small
            cell lung cancer patients receiving platinum-based chemotherapy
  JOURNAL   Clin Cancer Res 18 (19), 5507-5514 (2012)
   PUBMED   22872573
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Zenklusen,J.C., Rodriguez,L.V., LaCava,M., Wang,Z., Goldstein,L.S.
            and Conti,C.J.
  TITLE     Novel susceptibility locus for mouse hepatomas: evidence for a
            conserved tumor suppressor gene
  JOURNAL   Genome Res 6 (11), 1070-1076 (1996)
   PUBMED   8938430
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Zenklusen,J.C., Weitzel,J.N., Ball,H.G. and Conti,C.J.
  TITLE     Allelic loss at 7q31.1 in human primary ovarian carcinomas suggests
            the existence of a tumor suppressor gene
  JOURNAL   Oncogene 11 (2), 359-363 (1995)
   PUBMED   7624150
REFERENCE   8  (residues 1 to 562)
  AUTHORS   Zenklusen,J.C., Thompson,J.C., Troncoso,P., Kagan,J. and Conti,C.J.
  TITLE     Loss of heterozygosity in human primary prostate carcinomas: a
            possible tumor suppressor gene at 7q31.1
  JOURNAL   Cancer Res 54 (24), 6370-6373 (1994)
   PUBMED   7987830
REFERENCE   9  (residues 1 to 562)
  AUTHORS   Zenklusen,J.C., Bieche,I., Lidereau,R. and Conti,C.J.
  TITLE     (C-A)n microsatellite repeat D7S522 is the most commonly deleted
            region in human primary breast cancer
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12155-12158 (1994)
   PUBMED   7991599
REFERENCE   10 (residues 1 to 562)
  AUTHORS   Ogata,T., Ayusawa,D., Namba,M., Takahashi,E., Oshimura,M. and
            Oishi,M.
  TITLE     Chromosome 7 suppresses indefinite division of nontumorigenic
            immortalized human fibroblast cell lines KMST-6 and SUSM-1
  JOURNAL   Mol Cell Biol 13 (10), 6036-6043 (1993)
   PUBMED   8105370
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106873.3 and AC002542.1.
            
            Summary: The gene for this product maps to a region on chromosome 7
            identified as an autism-susceptibility locus. Mutation screening of
            the entire coding region in autistic individuals failed to identify
            phenotype-specific variants, suggesting that coding mutations for
            this gene are unlikely to be involved in the etiology of autism.
            The function of this gene product has not been determined.
            Transcript variants encoding different isoforms of this protein
            have been described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.197573.1,
                                           SRR1660809.200467.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.2"
     Protein         1..562
                     /product="suppressor of tumorigenicity 7 protein isoform
                     9"
                     /note="family with sequence similarity 4, subfamily A,
                     member 1; suppression of tumorigenicity 7 (breast);
                     suppressor of tumorigenicity 7 protein"
                     /calculated_mol_wt=64404
     Region          18..523
                     /region_name="ST7"
                     /note="ST7 protein; pfam04184"
                     /db_xref="CDD:461214"
     CDS             1..562
                     /gene="ST7"
                     /gene_synonym="ETS7q; FAM4A; FAM4A1; HELG; RAY1; SEN4;
                     TSG7"
                     /coded_by="NM_001369604.1:41..1729"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:7982"
                     /db_xref="HGNC:HGNC:11351"
                     /db_xref="MIM:600833"
ORIGIN      
        1 maeaatgfle qlkscivwsw tylwtvwffi vlflvyilrv plkindnlst vsmflntltp
       61 kfyvaltgts slisglilif ewwyfrkygt sfieqvsvsh lrpllggvdn nssnnsnssn
      121 gdsdsnrqsv seckvwrnpl nlfrgaeynr ytwvtgrepl tyydmnlsaq dhqtfftcds
      181 dhlrpadaim qkawrernpq arisaaheal einecatayi llaeeeatti aeaeklfkqa
      241 lkagdgcyrr sqqlqhhgsq yeaqhrrdtn vlvyikrrla mcarrlgrtr eavkmmrdlm
      301 kefpllsmfn ihenlleall elqayadvqa vlakyddisl pksaticyta allkaravsd
      361 kfspeaasrr glstaemnav eaihravefn phvpkyllem kslilppehi lkrgdseaia
      421 yaffhlahwk rvegalnllh ctwegtfrmi pyplekghlf ypypicteta drellpsfhe
      481 vsvypkkelp ffilftaglc sftamlallt hqfpelmgvf akamidifcs aefrdwncks
      541 ifmrvedele ippapqsqhf qn
//
LOCUS       NP_000204               1822 aa            linear   PRI 27-APR-2025
DEFINITION  integrin beta-4 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_000204
VERSION     NP_000204.3
DBSOURCE    REFSEQ: accession NM_000213.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1822)
  AUTHORS   Ma,D., Liu,S., Liu,K., Kong,L., Xiao,L., Xin,Q., Jiang,C. and Wu,J.
  TITLE     MDFI promotes the proliferation and tolerance to chemotherapy of
            colorectal cancer cells by binding ITGB4/LAMB3 to activate the AKT
            signaling pathway
  JOURNAL   Cancer Biol Ther 25 (1), 2314324 (2024)
   PUBMED   38375821
  REMARK    GeneRIF: MDFI promotes the proliferation and tolerance to
            chemotherapy of colorectal cancer cells by binding ITGB4/LAMB3 to
            activate the AKT signaling pathway.
REFERENCE   2  (residues 1 to 1822)
  AUTHORS   Yamanaka,K., Koma,Y.I., Urakami,S., Takahashi,R., Nagamata,S.,
            Omori,M., Torigoe,R., Yokoo,H., Nakanishi,T., Ishihara,N.,
            Tsukamoto,S., Kodama,T., Nishio,M., Shigeoka,M., Yokozaki,H. and
            Terai,Y.
  TITLE     YKL40/Integrin beta4 Axis Induced by the Interaction between Cancer
            Cells and Tumor-Associated Macrophages Is Involved in the
            Progression of High-Grade Serous Ovarian Carcinoma
  JOURNAL   Int J Mol Sci 25 (19), 10598 (2024)
   PUBMED   39408927
  REMARK    GeneRIF: YKL40/Integrin beta4 Axis Induced by the Interaction
            between Cancer Cells and Tumor-Associated Macrophages Is Involved
            in the Progression of High-Grade Serous Ovarian Carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1822)
  AUTHORS   Shi,Y., Fang,N., Wu,Y., Xu,H., Ning,A., Zhang,W., Liu,Y., Tao,X.,
            Chen,Q., Tian,T., Zhang,L., Chu,M. and Cui,J.
  TITLE     NEDD4L mediates ITGB4 ubiquitination and degradation to suppress
            esophageal carcinoma progression
  JOURNAL   Cell Commun Signal 22 (1), 302 (2024)
   PUBMED   38831335
  REMARK    GeneRIF: NEDD4L mediates ITGB4 ubiquitination and degradation to
            suppress esophageal carcinoma progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1822)
  AUTHORS   Topuz,B.T., Guldiken,S., Tastekin,E., Topuz,C., Celik,M.,
            Bulbul,B.Y., Andac,B. and Yekdes,A.C.
  TITLE     The association between integrin beta4 overexpression and
            lymphovascular invasion in papillary thyroid cancer
  JOURNAL   Endokrynol Pol 75 (3), 310-316 (2024)
   PUBMED   38887115
  REMARK    GeneRIF: The association between integrin beta4 overexpression and
            lymphovascular invasion in papillary thyroid cancer.
REFERENCE   5  (residues 1 to 1822)
  AUTHORS   Lucky,A.W. and Gorell,E.
  TITLE     Epidermolysis Bullosa with Pyloric Atresia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301336
REFERENCE   6  (residues 1 to 1822)
  AUTHORS   Pfendner,E.G. and Lucky,A.W.
  TITLE     Junctional Epidermolysis Bullosa
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301304
REFERENCE   7  (residues 1 to 1822)
  AUTHORS   Hogervorst,F., Kuikman,I., van Kessel,A.G. and Sonnenberg,A.
  TITLE     Molecular cloning of the human alpha 6 integrin subunit.
            Alternative splicing of alpha 6 mRNA and chromosomal localization
            of the alpha 6 and beta 4 genes
  JOURNAL   Eur J Biochem 199 (2), 425-433 (1991)
   PUBMED   2070796
REFERENCE   8  (residues 1 to 1822)
  AUTHORS   Tamura,R.N., Rozzo,C., Starr,L., Chambers,J., Reichardt,L.F.,
            Cooper,H.M. and Quaranta,V.
  TITLE     Epithelial integrin alpha 6 beta 4: complete primary structure of
            alpha 6 and variant forms of beta 4
  JOURNAL   J Cell Biol 111 (4), 1593-1604 (1990)
   PUBMED   1976638
REFERENCE   9  (residues 1 to 1822)
  AUTHORS   Hogervorst,F., Kuikman,I., von dem Borne,A.E. and Sonnenberg,A.
  TITLE     Cloning and sequence analysis of beta-4 cDNA: an integrin subunit
            that contains a unique 118 kd cytoplasmic domain
  JOURNAL   EMBO J 9 (3), 765-770 (1990)
   PUBMED   2311578
REFERENCE   10 (residues 1 to 1822)
  AUTHORS   Suzuki,S. and Naitoh,Y.
  TITLE     Amino acid sequence of a novel integrin beta 4 subunit and primary
            expression of the mRNA in epithelial cells
  JOURNAL   EMBO J 9 (3), 757-763 (1990)
   PUBMED   2311577
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CA391583.1, X53587.1, X51841.1,
            AC087749.12, AI318403.1 and X52186.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 23, 2004 this sequence version replaced NP_000204.2.
            
            Summary: Integrins are heterodimers comprised of alpha and beta
            subunits, that are noncovalently associated transmembrane
            glycoprotein receptors. Different combinations of alpha and beta
            polypeptides form complexes that vary in their ligand-binding
            specificities. Integrins mediate cell-matrix or cell-cell adhesion,
            and transduced signals that regulate gene expression and cell
            growth. This gene encodes the integrin beta 4 subunit, a receptor
            for the laminins. This subunit tends to associate with alpha 6
            subunit and is likely to play a pivotal role in the biology of
            invasive carcinoma. Mutations in this gene are associated with
            epidermolysis bullosa with pyloric atresia. Multiple alternatively
            spliced transcript variants encoding distinct isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X53587.1, SRR14038197.633936.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000200181.8/ ENSP00000200181.3
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..1822
                     /product="integrin beta-4 isoform 1 precursor"
                     /note="CD104 antigen"
                     /calculated_mol_wt=199437
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2749
     mat_peptide     28..1822
                     /product="Integrin beta-4. /id=PRO_0000016346"
                     /note="propagated from UniProtKB/Swiss-Prot (P16144.5)"
                     /calculated_mol_wt=199437
     Region          37..453
                     /region_name="INB"
                     /note="Integrin beta subunits (N-terminal portion of
                     extracellular region); smart00187"
                     /db_xref="CDD:197563"
     Region          194..199
                     /region_name="Involved in NRG1-and IGF1-binding.
                     /evidence=ECO:0000269|PubMed:20682778,
                     ECO:0000269|PubMed:22351760"
                     /note="propagated from UniProtKB/Swiss-Prot (P16144.5)"
     Site            327
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Region          457..485
                     /region_name="I-EGF_1"
                     /note="Integrin beta epidermal growth factor like domain
                     1; pfam18372"
                     /db_xref="CDD:465729"
     Site            491
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Region          550..573
                     /region_name="EGF_2"
                     /note="EGF-like domain; pfam07974"
                     /db_xref="CDD:400365"
     Site            579
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Site            617
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Region          626..709
                     /region_name="Integrin_B_tail"
                     /note="Integrin beta tail domain; pfam07965"
                     /db_xref="CDD:462325"
     Site            695
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Site            711..733
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16144.5)"
     Region          732..749
                     /region_name="Palmitoylated on several cysteines"
                     /note="propagated from UniProtKB/Swiss-Prot (P16144.5)"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64632; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Region          990..1084
                     /region_name="Calx-beta"
                     /note="Calx-beta domain; pfam03160"
                     /db_xref="CDD:397326"
     Site            1069
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Region          1113..1140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16144.5)"
     Site            1119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64632; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Region          1128..1208
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(1204..1205,1207..1208)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            order(1220,1290,1305)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          1221..1309
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(1306..1307,1309..1310)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1400..1444
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16144.5)"
     Site            1454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Site            1457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Site            1474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Site            1487
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Site            1494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64632; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Region          1495..1525
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16144.5)"
     Site            order(1528,1592,1607)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          1529..1611
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            1530
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     Site            order(1641,1708,1723)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          1642..1727
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            1791
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64632; propagated from
                     UniProtKB/Swiss-Prot (P16144.5)"
     CDS             1..1822
                     /gene="ITGB4"
                     /gene_synonym="CD104; GP150; JEB5A; JEB5B"
                     /coded_by="NM_000213.5:165..5633"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS11727.1"
                     /db_xref="GeneID:3691"
                     /db_xref="HGNC:HGNC:6158"
                     /db_xref="MIM:147557"
ORIGIN      
        1 magprpspwa rlllaalisv slsgtlanrc kkapvkscte cvrvdkdcay ctdemfrdrr
       61 cntqaellaa gcqresivvm essfqiteet qidttlrrsq mspqglrvrl rpgeerhfel
      121 evfeplespv dlyilmdfsn smsddldnlk kmgqnlarvl sqltsdytig fgkfvdkvsv
      181 pqtdmrpekl kepwpnsdpp fsfknvislt edvdefrnkl qgerisgnld apeggfdail
      241 qtavctrdig wrpdsthllv fstesafhye adganvlagi msrnderchl dttgtytqyr
      301 tqdypsvptl vrllakhnii pifavtnysy syyeklhtyf pvsslgvlqe dssnivelle
      361 eafnrirsnl diraldsprg lrtevtskmf qktrtgsfhi rrgevgiyqv qlralehvdg
      421 thvcqlpedq kgnihlkpsf sdglkmdagi icdvctcelq kevrsarcsf ngdfvcgqcv
      481 csegwsgqtc ncstgslsdi qpclregedk pcsgrgecqc ghcvcygegr yegqfceydn
      541 fqcprtsgfl cndrgrcsmg qcvcepgwtg pscdcplsna tcidsnggic ngrghcecgr
      601 chchqqslyt dticeinysa ihpglcedlr scvqcqawgt gekkgrtcee cnfkvkmvde
      661 lkraeevvvr csfrdedddc tysytmegdg apgpnstvlv hkkkdcppgs fwwlipllll
      721 llpllallll lcwkycacck aclallpccn rghmvgfked hymlrenlma sdhldtpmlr
      781 sgnlkgrdvv rwkvtnnmqr pgfathaasi nptelvpygl slrlarlcte nllkpdtrec
      841 aqlrqeveen lnevyrqisg vhklqqtkfr qqpnagkkqd htivdtvlma prsakpallk
      901 ltekqveqra fhdlkvapgy ytltadqdar gmvefqegve lvdvrvplfi rpedddekql
      961 lveaidvpag tatlgrrlvn itiikeqard vvsfeqpefs vsrgdqvari pvirrvldgg
     1021 ksqvsyrtqd gtaqgnrdyi pvegellfqp geawkelqvk llelqevdsl lrgrqvrrfh
     1081 vqlsnpkfga hlgqphstti iirdpdeldr sftsqmlssq ppphgdlgap qnpnakaags
     1141 rkihfnwlpp sgkpmgyrvk ywiqgdsese ahlldskvps veltnlypyc dyemkvcayg
     1201 aqgegpyssl vscrthqevp sepgrlafnv vsstvtqlsw aepaetngei tayevcyglv
     1261 nddnrpigpm kkvlvdnpkn rmllienlre sqpyrytvka rngagwgper eaiinlatqp
     1321 krpmsipiip dipivdaqsg edydsflmys ddvlrspsgs qrpsvsddtg cgwkfepllg
     1381 eeldlrrvtw rlppeliprl sassgrssda eaphgppddg gaggkggslp rsatpgppge
     1441 hlvngrmdfa fpgstnslhr mtttsaaayg thlsphvphr vlstsstltr dynsltrseh
     1501 shsttlprdy stltsvsshd srltagvpdt ptrlvfsalg ptslrvswqe prcerplqgy
     1561 sveyqllngg elhrlnipnp aqtsvvvedl lpnhsyvfrv raqsqegwgr eregvities
     1621 qvhpqsplcp lpgsaftlst psapgplvft alspdslqls werprrpngd ivgylvtcem
     1681 aqgggpataf rvdgdspesr ltvpglsenv pykfkvqart tegfgpereg iitiesqdgg
     1741 pfpqlgsrag lfqhplqsey ssittthtsa tepflvdglt lgaqhleagg sltrhvtqef
     1801 vsrtlttsgt lsthmdqqff qt
//
LOCUS       NP_001277742             730 aa            linear   ROD 27-APR-2025
DEFINITION  actin-binding LIM protein 1 isoform 4 [Mus musculus].
ACCESSION   NP_001277742
VERSION     NP_001277742.1
DBSOURCE    REFSEQ: accession NM_001290813.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Chen,X., Liu,Y., Xu,C., Ba,L., Liu,Z., Li,X., Huang,J., Simpson,E.,
            Gao,H., Cao,D., Sheng,W., Qi,H., Ji,H., Sanderson,M., Cai,C.L.,
            Li,X., Yang,L., Na,J., Yamamura,K., Liu,Y., Huang,G., Shou,W. and
            Sun,N.
  TITLE     QKI is a critical pre-mRNA alternative splicing regulator of
            cardiac myofibrillogenesis and contractile function
  JOURNAL   Nat Commun 12 (1), 89 (2021)
   PUBMED   33397958
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 730)
  AUTHORS   Jin,S.H., Kim,H., Gu,D.R., Park,K.H., Lee,Y.R., Choi,Y. and
            Lee,S.H.
  TITLE     Actin-binding LIM protein 1 regulates receptor activator of
            NF-kappaB ligand-mediated osteoclast differentiation and motility
  JOURNAL   BMB Rep 51 (7), 356-361 (2018)
   PUBMED   29921413
  REMARK    GeneRIF: ABLIM1 is associated with the regulation of preosteoclast
            motility via the PI3K/Akt/Rac1 pathway during RANKL-mediated
            osteoclastogenesis.
REFERENCE   4  (residues 1 to 730)
  AUTHORS   Zhang,Q., Huang,R., Ye,Y., Guo,X., Lu,J., Zhu,F., Gong,X.,
            Zhang,Q., Yan,J., Luo,L., Zhuang,S., Chen,Y., Zhao,X., Evans,S.M.,
            Jiang,C., Liang,X. and Sun,Y.
  TITLE     Temporal requirements for ISL1 in sympathetic neuron proliferation,
            differentiation, and diversification
  JOURNAL   Cell Death Dis 9 (2), 247 (2018)
   PUBMED   29445148
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 730)
  AUTHORS   Narahara,H., Sakai,E., Yamaguchi,Y., Narahara,S., Iwatake,M.,
            Okamoto,K., Yoshida,N. and Tsukuba,T.
  TITLE     Actin binding LIM 1 (abLIM1) negatively controls osteoclastogenesis
            by regulating cell migration and fusion
  JOURNAL   J Cell Physiol 234 (1), 486-499 (2018)
   PUBMED   29904924
  REMARK    GeneRIF: abLIM1 regulated the localization of tubulin, migration,
            and fusion in osteoclasts. Thus, these results indicate that abLIM1
            negatively controls osteoclast differentiation by regulating cell
            migration and fusion mediated via actin formation.
REFERENCE   6  (residues 1 to 730)
  AUTHORS   Erkman,L., Yates,P.A., McLaughlin,T., McEvilly,R.J., Whisenhunt,T.,
            O'Connell,S.M., Krones,A.I., Kirby,M.A., Rapaport,D.H.,
            Bermingham,J.R., O'Leary,D.D. and Rosenfeld,M.G.
  TITLE     A POU domain transcription factor-dependent program regulates axon
            pathfinding in the vertebrate visual system
  JOURNAL   Neuron 28 (3), 779-792 (2000)
   PUBMED   11163266
REFERENCE   7  (residues 1 to 730)
  AUTHORS   Suriyapperuma,S.P., Lozovatsky,L., Ciciotte,S.L., Peters,L.L. and
            Gilligan,D.M.
  TITLE     The mouse adducin gene family: alternative splicing and chromosomal
            localization
  JOURNAL   Mamm Genome 11 (1), 16-23 (2000)
   PUBMED   10602987
REFERENCE   8  (residues 1 to 730)
  AUTHORS   Kim,H.J., Noben-Trauth,K. and Morell,R.J.
  TITLE     Tectorin-beta (Tectb) maps to mouse chromosome 19
  JOURNAL   Genomics 53 (3), 419-420 (1998)
   PUBMED   9799617
REFERENCE   9  (residues 1 to 730)
  AUTHORS   Kim,A.C., Peters,L.L., Knoll,J.H., Van Huffel,C., Ciciotte,S.L.,
            Kleyn,P.W. and Chishti,A.H.
  TITLE     Limatin (LIMAB1), an actin-binding LIM protein, maps to mouse
            chromosome 19 and human chromosome 10q25, a region frequently
            deleted in human cancers
  JOURNAL   Genomics 46 (2), 291-293 (1997)
   PUBMED   9417918
REFERENCE   10 (residues 1 to 730)
  AUTHORS   Roof,D.J., Hayes,A., Adamian,M., Chishti,A.H. and Li,T.
  TITLE     Molecular characterization of abLIM, a novel actin-binding and
            double zinc finger protein
  JOURNAL   J Cell Biol 138 (3), 575-588 (1997)
   PUBMED   9245787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF404774.1, AC161518.3 and BE994737.1.
            
            Transcript Variant: This variant (4) lacks four alternate in-frame
            exons in the 3' coding region, compared to variant 1. The encoded
            isoform (4) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC141083.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 52.09 cM"
     Protein         1..730
                     /product="actin-binding LIM protein 1 isoform 4"
                     /note="actin-binding double zinc finger protein;
                     actin-binding LIM protein family member 1"
                     /calculated_mol_wt=82217
     Region          99..150
                     /region_name="LIM1_abLIM"
                     /note="The first LIM domain of actin binding LIM (abLIM)
                     proteins; cd09327"
                     /db_xref="CDD:188713"
     Site            order(99,102,119,122,125,128,146,149)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188713"
     Region          155..210
                     /region_name="LIM2_abLIM"
                     /note="The second LIM domain on actin binding LIM (abLIM)
                     proteins; cd09328"
                     /db_xref="CDD:188714"
     Site            order(158,161,178,181,184,187,206,209)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188714"
     Region          226..277
                     /region_name="LIM3_abLIM"
                     /note="The third LIM domain of actin binding LIM (abLIM)
                     proteins; cd09329"
                     /db_xref="CDD:188715"
     Site            order(226,229,247,250,253,256,273,276)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188715"
     Region          285..340
                     /region_name="LIM4_abLIM"
                     /note="The fourth LIM domain of actin binding LIM (abLIM)
                     proteins; cd09330"
                     /db_xref="CDD:188716"
     Site            order(285,288,305,308,311,314,333,336)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188716"
     Region          349..680
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          695..730
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..730
                     /gene="Ablim1"
                     /gene_synonym="2210411C18Rik; 2610209L21Rik;
                     4833406P10Rik; 9330196J19Rik; Limab1; mKIAA0059"
                     /coded_by="NM_001290813.2:76..2268"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:226251"
                     /db_xref="MGI:MGI:1194500"
ORIGIN      
        1 mpsllglkcl gklcsseigk vpsperaslr nshrrllied lsvpetpdpa hrrrgtvihl
       61 vylysagcgp pelrfssydp svahpqdphh ssekpvihch kcgepckgev lrvqtkhfhi
      121 kcftckvcgc dlaqggffik ngdylctldy qrmygtrchg cgefvegevv talgktyhpn
      181 cfactickrp fppgdrvtfn grdclcqlca qpmssspkea scssncagcg rdikngqall
      241 aldkqwhlgc fkckscgkvl tgeyiskdgs pycekdyqgl fgvkceachq fitgkvleag
      301 dkhyhpscar csrcnqmfte geemylqgst vwhpdckqst kteeklrptr tssesiysrp
      361 gssipgspgh tiyakvdnei ldykdlaaip kvkaiydier pdlityepfy tsgyedkqer
      421 qslgesprtl sptpsaegyq dvrdrmihrs tsqgsinspv ysrhsytptt srspqhfhrp
      481 gnepssgrns plpyrpdsrp ltptyaqapk hfhvpdqgin iyrkppiykq hgtdprrrss
      541 greedeeell rrrqlqeeql mklnsglgql ilkeemekes reraslasry dsplhsasha
      601 pssktsslpg ygknglhrpv stdfaqynsy gdisggvrdy qtlpdghmpa vrmdrgvsmp
      661 nmlepkifpy emlmvtnrgr nkilrdvdrt rlerhlapev fweifgmsiq efdklplwrr
      721 ndmkkkaklf
//
LOCUS       NP_035056                207 aa            linear   ROD 27-APR-2025
DEFINITION  ER membrane protein complex subunit 8 [Mus musculus].
ACCESSION   NP_035056 XP_489534
VERSION     NP_035056.1
DBSOURCE    REFSEQ: accession NM_010926.6
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Guna,A., Volkmar,N., Christianson,J.C. and Hegde,R.S.
  TITLE     The ER membrane protein complex is a transmembrane domain insertase
  JOURNAL   Science 359 (6374), 470-473 (2018)
   PUBMED   29242231
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   6  (residues 1 to 207)
  AUTHORS   Bachman,N.J., Wu,W., Schmidt,T.R., Grossman,L.I. and Lomax,M.I.
  TITLE     The 5' region of the COX4 gene contains a novel overlapping gene,
            NOC4
  JOURNAL   Mamm Genome 10 (5), 506-512 (1999)
   PUBMED   10337626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC103360.9.
            
            On Sep 3, 2004 this sequence version replaced XP_489534.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK164130.1, AK143131.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135, SAMN01164142
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 69.98 cM"
     Protein         1..207
                     /product="ER membrane protein complex subunit 8"
                     /note="neighbor of Cox4; COX4 neighbor"
                     /calculated_mol_wt=23217
     Region          6..196
                     /region_name="MPN_UPF0172"
                     /note="Mov34/MPN/PAD-1 family: UPF0172 family of unknown
                     function includes neighbor of COX4 (Noc4p); cd08060"
                     /db_xref="CDD:163691"
     CDS             1..207
                     /gene="Emc8"
                     /gene_synonym="Cox4nb; Fam158b; Noc4"
                     /coded_by="NM_010926.6:110..733"
                     /db_xref="CCDS:CCDS22719.1"
                     /db_xref="GeneID:18117"
                     /db_xref="MGI:MGI:1343095"
ORIGIN      
        1 mpgvklttqa yckmvlhgak yphcavngll vaerqrprke hppgagshtl fvdciplfhg
       61 tlaltpmlev altlidswck dnsyviagyy qanervkdas pnqvaekvas riaegfgdaa
      121 limvdnakft mdcaaptihv yeqhenrwrc rdphhdyced wpeaqrisas lldsrsyetl
      181 vdfdnhlddi rsdwtnpein kavlhlc
//
LOCUS       NP_001273462             259 aa            linear   PRI 27-APR-2025
DEFINITION  cell cycle checkpoint control protein RAD9B isoform c [Homo
            sapiens].
ACCESSION   NP_001273462
VERSION     NP_001273462.1
DBSOURCE    REFSEQ: accession NM_001286533.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Barroso-Chinea,P., Salas-Hernandez,J., Cruz-Muros,I.,
            Lopez-Fernandez,J., Freire,R. and Afonso-Oramas,D.
  TITLE     Expression of RAD9B in the mesostriatal system of rats and humans:
            Overexpression in a 6-OHDA rat model of Parkinson's disease
  JOURNAL   Ann Anat 250, 152135 (2023)
   PUBMED   37460044
  REMARK    GeneRIF: Expression of RAD9B in the mesostriatal system of rats and
            humans: Overexpression in a 6-OHDA rat model of Parkinson's
            disease.
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Cao,X., Tian,T., Steele,J.W., Cabrera,R.M., Aguiar-Pulido,V.,
            Wadhwa,S., Bhavani,N., Bi,P., Gargurevich,N.H., Hoffman,E.N.,
            Cai,C.Q., Marini,N.J., Yang,W., Shaw,G.M., Ross,M.E., Finnell,R.H.
            and Lei,Y.
  TITLE     Loss of RAD9B impairs early neural development and contributes to
            the risk for human spina bifida
  JOURNAL   Hum Mutat 41 (4), 786-799 (2020)
   PUBMED   31898828
  REMARK    GeneRIF: Loss of RAD9B impairs early neural development and
            contributes to the risk for human spina bifida.
            Erratum:[Hum Mutat. 2021 Apr;42(4):487. doi: 10.1002/humu.24175.
            PMID: 33856736]
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Lyndaker,A.M., Vasileva,A., Wolgemuth,D.J., Weiss,R.S. and
            Lieberman,H.B.
  TITLE     Clamping down on mammalian meiosis
  JOURNAL   Cell Cycle 12 (19), 3135-3145 (2013)
   PUBMED   24013428
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Perez-Castro,A.J. and Freire,R.
  TITLE     Rad9B responds to nucleolar stress through ATR and JNK signalling,
            and delays the G1-S transition
  JOURNAL   J Cell Sci 125 (Pt 5), 1152-1164 (2012)
   PUBMED   22399810
  REMARK    GeneRIF: Rad9B responds to nucleolar stress after the activation of
            JNK-dependent stress signalling and ATR-dependent DNA damage
            response pathways, and actively accumulates within nucleoli, where
            it does not cause a transcription block.
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Lieberman,H.B.
  TITLE     Rad9, an evolutionarily conserved gene with multiple functions for
            preserving genomic integrity
  JOURNAL   J Cell Biochem 97 (4), 690-697 (2006)
   PUBMED   16365875
  REMARK    GeneRIF: The encoded mammalian proteins participate in promoting
            resistance to DNA damage, cell cycle checkpoint control, DNA
            repair, and apoptosis.
            Review article
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Dufault,V.M., Oestreich,A.J., Vroman,B.T. and Karnitz,L.M.
  TITLE     Identification and characterization of RAD9B, a paralog of the RAD9
            checkpoint gene
  JOURNAL   Genomics 82 (6), 644-651 (2003)
   PUBMED   14611806
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Hopkins,K.M., Wang,X., Berlin,A., Hang,H., Thaker,H.M. and
            Lieberman,H.B.
  TITLE     Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint
            control genes in normal and cancerous testicular tissue
  JOURNAL   Cancer Res 63 (17), 5291-5298 (2003)
   PUBMED   14500360
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Zou,L. and Elledge,S.J.
  TITLE     Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
  JOURNAL   Science 300 (5625), 1542-1548 (2003)
   PUBMED   12791985
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002350.1.
            
            Transcript Variant: This variant (4) contains multiple differences
            in both the 5' and 3' coding regions, compared to variant 1,
            including initiation of translation from a downstream in-frame
            start codon. The encoded isoform (c) has a shorter N-terminus and a
            distinct C-terminus, and is shorter than isoform a. Variants 4 and
            5 encode the same isoform (c).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047645.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..259
                     /product="cell cycle checkpoint control protein RAD9B
                     isoform c"
                     /EC_number="3.1.11.2"
                     /note="DNA repair exonuclease rad9 homolog B; cell cycle
                     checkpoint control protein RAD9B; RAD9 homolog B"
                     /calculated_mol_wt=28387
     Region          <1..118
                     /region_name="Rad9"
                     /note="pfam04139"
                     /db_xref="CDD:427739"
     CDS             1..259
                     /gene="RAD9B"
                     /coded_by="NM_001286533.2:631..1410"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:144715"
                     /db_xref="HGNC:HGNC:21700"
                     /db_xref="MIM:608368"
ORIGIN      
        1 miqprllada ivlftssqee vtlavtplnf clkssneesm dlsnavhsem fvgsdefdff
       61 qigmdteitf cfkelkgilt fseathapis iyfdfpgkpl alsiddmlve anfilatlad
      121 eqsrasspqs lclsqkrkrs dliekkagkn vtgqalecis kkaaprrlyp ketltnisal
      181 encgspamkr vdgdvsevse ssvsnteevp gslclrkfsc mffgavssdq qehfnhpfds
      241 larasdseed mnngsfsif
//
LOCUS       NP_003076                134 aa            linear   PRI 27-APR-2025
DEFINITION  beta-synuclein isoform 1 [Homo sapiens].
ACCESSION   NP_003076 XP_941585
VERSION     NP_003076.1
DBSOURCE    REFSEQ: accession NM_003085.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Mahur,P., Sharma,A., Jahan,G., S,G. A, Kumar Singh,A.,
            Muthukumaran,J. and Jain,M.
  TITLE     Understanding Genetic Risks: Computational Exploration of Human
            beta-Synuclein nsSNPs and their Potential Impact on Structural
            Alteration
  JOURNAL   Neurosci Lett 833, 137826 (2024)
   PUBMED   38768940
  REMARK    GeneRIF: Understanding Genetic Risks: Computational Exploration of
            Human beta-Synuclein nsSNPs and their Potential Impact on
            Structural Alteration.
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Barba,L., Vollmuth,C., Abu-Rumeileh,S., Halbgebauer,S., Oeckl,P.,
            Steinacker,P., Kollikowski,A.M., Schultz,C., Wolf,J., Pham,M.,
            Schuhmann,M.K., Heuschmann,P.U., Haeusler,K.G., Stoll,G.,
            Neugebauer,H. and Otto,M.
  TITLE     Serum beta-synuclein, neurofilament light chain and glial
            fibrillary acidic protein as prognostic biomarkers in
            moderate-to-severe acute ischemic stroke
  JOURNAL   Sci Rep 13 (1), 20941 (2023)
   PUBMED   38017278
  REMARK    GeneRIF: Serum beta-synuclein, neurofilament light chain and glial
            fibrillary acidic protein as prognostic biomarkers in
            moderate-to-severe acute ischemic stroke.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Abu-Rumeileh,S., Barba,L., Bache,M., Halbgebauer,S., Oeckl,P.,
            Steinacker,P., Guttler,A., Kessler,J., Illert,J., Strauss,C.,
            Vordermark,D. and Otto,M.
  TITLE     Plasma beta-synuclein, GFAP, and neurofilaments in patients with
            malignant gliomas undergoing surgical and adjuvant therapy
  JOURNAL   Ann Clin Transl Neurol 10 (10), 1924-1930 (2023)
   PUBMED   37608748
  REMARK    GeneRIF: Plasma beta-synuclein, GFAP, and neurofilaments in
            patients with malignant gliomas undergoing surgical and adjuvant
            therapy.
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Halbgebauer,S., Abu-Rumeileh,S., Oeckl,P., Steinacker,P.,
            Roselli,F., Wiesner,D., Mammana,A., Beekes,M.,
            Kortazar-Zubizarreta,I., Perez de Nanclares,G., Capellari,S.,
            Giese,A., Castilla,J., Ludolph,A.C., Zakova,D., Parchi,P. and
            Otto,M.
  TITLE     Blood beta-Synuclein and Neurofilament Light Chain During the
            Course of Prion Disease
  JOURNAL   Neurology 98 (14), e1434-e1445 (2022)
   PUBMED   35110380
  REMARK    GeneRIF: Blood beta-Synuclein and Neurofilament Light Chain During
            the Course of Prion Disease.
REFERENCE   5  (residues 1 to 134)
  AUTHORS   Beyer,K., Munoz-Marmol,A.M., Sanz,C., Marginet-Flinch,R., Ferrer,I.
            and Ariza,A.
  TITLE     New brain-specific beta-synuclein isoforms show expression ratio
            changes in Lewy body diseases
  JOURNAL   Neurogenetics 13 (1), 61-72 (2012)
   PUBMED   22205345
  REMARK    GeneRIF: Data provide evidence for the role of beta-synuclein minor
            transcript variants in the development of complex diseases and
            provide new insights into the pathogenesis of Lewy body diseases.
REFERENCE   6  (residues 1 to 134)
  AUTHORS   Lavedan,C., Buchholtz,S., Auburger,G., Albin,R.L.,
            Athanassiadou,A., Blancato,J., Burguera,J.A., Ferrell,R.E.,
            Kostic,V., Leroy,E., Leube,B., Mota-Vieira,L., Papapetropoulos,T.,
            Pericak-Vance,M.A., Pinkus,J., Scott,W.K., Ulm,G., Vasconcelos,J.,
            Vilchez,J.J., Nussbaum,R.L. and Polymeropoulos,M.H.
  TITLE     Absence of mutation in the beta- and gamma-synuclein genes in
            familial autosomal dominant Parkinson's disease
  JOURNAL   DNA Res 5 (6), 401-402 (1998)
   PUBMED   10048491
REFERENCE   7  (residues 1 to 134)
  AUTHORS   Lavedan,C., Leroy,E., Torres,R., Dehejia,A., Dutra,A.,
            Buchholtz,S., Nussbaum,R.L. and Polymeropoulos,M.H.
  TITLE     Genomic organization and expression of the human beta-synuclein
            gene (SNCB)
  JOURNAL   Genomics 54 (1), 173-175 (1998)
   PUBMED   9806846
REFERENCE   8  (residues 1 to 134)
  AUTHORS   Jensen,P.H., Hojrup,P., Hager,H., Nielsen,M.S., Jacobsen,L.,
            Olesen,O.F., Gliemann,J. and Jakes,R.
  TITLE     Binding of Abeta to alpha- and beta-synucleins: identification of
            segments in alpha-synuclein/NAC precursor that bind Abeta and NAC
  JOURNAL   Biochem J 323 (Pt 2) (Pt 2), 539-546 (1997)
   PUBMED   9163350
REFERENCE   9  (residues 1 to 134)
  AUTHORS   Spillantini,M.G., Divane,A. and Goedert,M.
  TITLE     Assignment of human alpha-synuclein (SNCA) and beta-synuclein
            (SNCB) genes to chromosomes 4q21 and 5q35
  JOURNAL   Genomics 27 (2), 379-381 (1995)
   PUBMED   7558013
REFERENCE   10 (residues 1 to 134)
  AUTHORS   Jakes,R., Spillantini,M.G. and Goedert,M.
  TITLE     Identification of two distinct synucleins from human brain
  JOURNAL   FEBS Lett 345 (1), 27-32 (1994)
   PUBMED   8194594
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM543516.1, S69965.1,
            BC002902.2, BQ184193.1 and AC091934.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_941585.1.
            
            Summary: This gene encodes a member of a small family of proteins
            that inhibit phospholipase D2 and may function in neuronal
            plasticity. The encoded protein is abundant in lesions of patients
            with Alzheimer disease. A mutation in this gene was found in
            individuals with dementia with Lewy bodies. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Dec
            2015].
            
            Transcript Variant: This variant (2) lacks an exon in the 5' UTR
            compared to variant 1. Variants 1, 2 and 7 encode the same protein
            (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.496284.1,
                                           SRR3476690.148744.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393693.7/ ENSP00000377296.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..134
                     /product="beta-synuclein isoform 1"
                     /note="beta-synuclein; I(2)-synuclein"
                     /calculated_mol_wt=14157
     Region          1..121
                     /region_name="Synuclein"
                     /note="pfam01387"
                     /db_xref="CDD:460186"
     Region          20..67
                     /region_name="4 X 11 AA tandem repeats of
                     [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16143.1)"
     Region          89..134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16143.1)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by BARK1, CK2 and GRK5.
                     /evidence=ECO:0000269|PubMed:10852916; propagated from
                     UniProtKB/Swiss-Prot (Q16143.1)"
     CDS             1..134
                     /gene="SNCB"
                     /coded_by="NM_003085.5:265..669"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4406.1"
                     /db_xref="GeneID:6620"
                     /db_xref="HGNC:HGNC:11140"
                     /db_xref="MIM:602569"
ORIGIN      
        1 mdvfmkglsm akegvvaaae ktkqgvteaa ektkegvlyv gsktregvvq gvasvaektk
       61 eqashlggav fsgagniaaa tglvkreefp tdlkpeevaq eaaeepliep lmepegesye
      121 dppqeeyqey epea
//
LOCUS       NP_006418                175 aa            linear   PRI 27-APR-2025
DEFINITION  apoptosis regulatory protein Siva isoform 1 [Homo sapiens].
ACCESSION   NP_006418
VERSION     NP_006418.2
DBSOURCE    REFSEQ: accession NM_006427.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Vermehren-Schmaedick,A., Peto,M., Wagoner,W., Chiotti,K.E.,
            Ramsey,E., Wang,X., Rakshe,S., Minnier,J., Sears,R., Spellman,P.
            and Luoh,S.W.
  TITLE     Mutation of SIVA, a candidate metastasis gene identified from
            clonally related bilateral breast cancers, promotes breast cancer
            cell spread in vitro and in vivo
  JOURNAL   PLoS One 19 (5), e0302856 (2024)
   PUBMED   38722955
  REMARK    GeneRIF: Mutation of SIVA, a candidate metastasis gene identified
            from clonally related bilateral breast cancers, promotes breast
            cancer cell spread in vitro and in vivo.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Kong,F., Wu,K., Pang,L., Huang,Y., Li,L., Xu,J., Li,F., Qing,Y.,
            Wang,Z., Huang,X., Xu,S., Zhong,X., Zhu,Z., Wang,X. and Yang,J.
  TITLE     Inhibition of apoptosis-regulatory protein Siva-1 reverses
            multidrug resistance in gastric cancer by targeting PCBP1
  JOURNAL   Oncol Res 30 (6), 277-288 (2023)
   PUBMED   37303491
  REMARK    GeneRIF: Inhibition of apoptosis-regulatory protein Siva-1 reverses
            multidrug resistance in gastric cancer by targeting PCBP1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Lin,Z., Wan,A.H., Sun,L., Liang,H., Niu,Y., Deng,Y., Yan,S.,
            Wang,Q.P., Bu,X., Zhang,X., Hu,K., Wan,G. and He,W.
  TITLE     N6-methyladenosine demethylase FTO enhances chemo-resistance in
            colorectal cancer through SIVA1-mediated apoptosis
  JOURNAL   Mol Ther 31 (2), 517-534 (2023)
   PUBMED   36307991
  REMARK    GeneRIF: N6-methyladenosine demethylase FTO enhances
            chemo-resistance in colorectal cancer through SIVA1-mediated
            apoptosis.
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Kong,F.B., Deng,Q.M., Deng,H.Q., Dong,C.C., Li,L., He,C.G.,
            Wang,X.T., Xu,S. and Mai,W.
  TITLE     Siva-1 regulates multidrug resistance of gastric cancer by
            targeting MDR1 and MRP1 via the NF-kappaB pathway
  JOURNAL   Mol Med Rep 22 (2), 1558-1566 (2020)
   PUBMED   32626967
  REMARK    GeneRIF: Siva1 regulates multidrug resistance of gastric cancer by
            targeting MDR1 and MRP1 via the NFkappaB pathway.
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Xu,F., Xu,A., Guo,Y., Bai,Q., Wu,X., Ji,S.P. and Xia,R.X.
  TITLE     PM2.5 exposure induces alveolar epithelial cell apoptosis and
            causes emphysema through p53/Siva-1
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (7), 3943-3950 (2020)
   PUBMED   32329870
  REMARK    GeneRIF: PM2.5 exposure induces alveolar epithelial cell apoptosis
            and causes emphysema through p53/Siva-1.
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Held-Feindt,J. and Mentlein,R.
  TITLE     CD70/CD27 ligand, a member of the TNF family, is expressed in human
            brain tumors
  JOURNAL   Int J Cancer 98 (3), 352-356 (2002)
   PUBMED   11920585
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Henke,A., Nestler,M., Strunze,S., Saluz,H.P., Hortschansky,P.,
            Menzel,B., Martin,U., Zell,R., Stelzner,A. and Munder,T.
  TITLE     The apoptotic capability of coxsackievirus B3 is influenced by the
            efficient interaction between the capsid protein VP2 and the
            proapoptotic host protein Siva
  JOURNAL   Virology 289 (1), 15-22 (2001)
   PUBMED   11601913
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Cao,C., Ren,X., Kharbanda,S., Koleske,A.J., Prasad,K.V. and Kufe,D.
  TITLE     The ARG tyrosine kinase interacts with Siva-1 in the apoptotic
            response to oxidative stress
  JOURNAL   J Biol Chem 276 (15), 11465-11468 (2001)
   PUBMED   11278261
  REMARK    Erratum:[J Biol Chem. 2012 Oct 19;287(43):36527. Koleske, A
            [corrected to Koleske, A J]]
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Henke,A., Launhardt,H., Klement,K., Stelzner,A., Zell,R. and
            Munder,T.
  TITLE     Apoptosis in coxsackievirus B3-caused diseases: interaction between
            the capsid protein VP2 and the proapoptotic protein siva
  JOURNAL   J Virol 74 (9), 4284-4290 (2000)
   PUBMED   10756043
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Prasad,K.V., Ao,Z., Yoon,Y., Wu,M.X., Rizk,M., Jacquot,S. and
            Schlossman,S.F.
  TITLE     CD27, a member of the tumor necrosis factor receptor family,
            induces apoptosis and binds to Siva, a proapoptotic protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (12), 6346-6351 (1997)
   PUBMED   9177220
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU195069.1, CK001877.1 and
            BC034562.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2000 this sequence version replaced NP_006418.1.
            
            Summary: This gene encodes an E3 ubiquitin ligase that regulates
            cell cycle progression, cell proliferation and apoptosis. The
            N-terminus of this protein binds to the cytoplasmic tail of the
            CD27 antigen, a member of the tumor necrosis factor receptor (TNFR)
            superfamily. In response to UV radiation-induced DNA damage, this
            protein has been shown to mediate the ubiquitination of
            proliferating cell nuclear antigen (PCNA), an important step in
            translesion DNA synthesis. [provided by RefSeq, Sep 2018].
            
            Transcript Variant: This variant (1) is the predominant and longer
            transcript. It encodes isoform 1 and includes the apoptotic
            properties of Siva.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223332.1, BQ943607.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329967.11/ ENSP00000329213.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..175
                     /product="apoptosis regulatory protein Siva isoform 1"
                     /note="CD27-binding (Siva) protein; apoptosis regulatory
                     protein Siva"
                     /calculated_mol_wt=18564
     Region          1..175
                     /region_name="Siva"
                     /note="Cd27 binding protein (Siva); pfam05458"
                     /db_xref="CDD:283184"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL2.
                     /evidence=ECO:0000269|PubMed:11278261; propagated from
                     UniProtKB/Swiss-Prot (O15304.2)"
     Region          36..55
                     /region_name="Interaction with BCL2L1 isoform Bcl-x(L) and
                     inhibition of BCL2L1 anti-apoptotic activity"
                     /note="propagated from UniProtKB/Swiss-Prot (O15304.2)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O15304.2)"
     Region          105..123
                     /region_name="Interaction with coxsackievirus B3 VP2"
                     /note="propagated from UniProtKB/Swiss-Prot (O15304.2)"
     CDS             1..175
                     /gene="SIVA1"
                     /gene_synonym="CD27BP; SIVA; Siva-1; Siva-2"
                     /coded_by="NM_006427.4:56..583"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9992.1"
                     /db_xref="GeneID:10572"
                     /db_xref="HGNC:HGNC:17712"
                     /db_xref="MIM:605567"
ORIGIN      
        1 mpkrscpfad vaplqlkvrv sqrelsrgvc aerysqevfe ktkrllflga qayldhvwde
       61 gcavvhlpes pkpgptgapr aargqmligp dgrlirslgq aseadpsgva siacsscvra
      121 vdgkavcgqc eralcgqcvr tcwgcgsvac tlcglvdcsd myekvlctsc amfet
//
LOCUS       NP_671728                992 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 18A isoform 2 [Homo
            sapiens].
ACCESSION   NP_671728 XP_001714022 XP_001717672 XP_001726157
VERSION     NP_671728.2
DBSOURCE    REFSEQ: accession NM_147195.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Liu,W.B., Han,F., Jiang,X., Yang,L.J., Li,Y.H., Liu,Y., Chen,H.Q.,
            Ao,L., Cui,Z.H., Cao,J. and Liu,J.Y.
  TITLE     ANKRD18A as a novel epigenetic regulation gene in lung cancer
  JOURNAL   Biochem Biophys Res Commun 429 (3-4), 180-185 (2012)
   PUBMED   23131552
  REMARK    GeneRIF: These results suggest that ANKRD18A hypermethylation and
            consequent mRNA alterations might be a vital molecular mechanism in
            lung cancer.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC056266.1, AB095935.1 and AL591543.22.
            
            On or before Jan 13, 2010 this sequence version replaced
            XP_001714022.2, XP_001717672.2, XP_001726157.2, NP_671728.1.
            
            Transcript Variant: This variant (2) lacks two in-frame exons
            compared to variant 1. The encoded isoform (2) is shorter than
            isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB095935.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399703.6/ ENSP00000382610.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.1"
     Protein         1..992
                     /product="ankyrin repeat domain-containing protein 18A
                     isoform 2"
                     /note="ankyrin repeat domain-containing protein 18A"
                     /calculated_mol_wt=115467
     Region          38..65
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          39..268
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          67..96
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVF6.3)"
     Site            order(69,73..74,77..79,81..82,86,89,98,100,102,106..107,
                     110..112,114..115,119,122,131,133,135,139..140,143..145,
                     147..148,152,155,164)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          69..98
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          100..131
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          100..129
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVF6.3)"
     Region          133..164
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          133..162
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVF6.3)"
     Region          166..197
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          166..195
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVF6.3)"
     Region          199..230
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          199..228
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVF6.3)"
     Region          262..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVF6.3)"
     Region          327..617
                     /region_name="CCDC144C"
                     /note="CCDC144C protein coiled-coil region; pfam14915"
                     /db_xref="CDD:464371"
     Region          <460..907
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          863..969
                     /region_name="DUF3496"
                     /note="Domain of unknown function (DUF3496); pfam12001"
                     /db_xref="CDD:463425"
     CDS             1..992
                     /gene="ANKRD18A"
                     /coded_by="NM_147195.4:312..3290"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55311.1"
                     /db_xref="GeneID:253650"
                     /db_xref="HGNC:HGNC:23643"
                     /db_xref="MIM:620259"
ORIGIN      
        1 mrklfsfgrr lgqallssmd qeyagpgydi rdwelrkihr aaikgdaaev ercltrrfrd
       61 ldardrkdrt vlhlacahgr vqvvtlllhr rcqidicdrl nrtplmkavh sqeeacaivl
      121 lecganpnie diygntalhy avynkgtsla erllshhani ealnkegntp llfainsrrq
      181 hmvefllknq anihavdnfk rtalilavqh nlssivtlll qqnirissqd mfgqtaedya
      241 lcsdlrsirq qilehknkml knhlrndnqe taamkpanlk krkerakaeh nlkvaseekq
      301 erlqrsenkq pqdsqsygkk kdamygnfml kkdiamlkee lyaikndslr kekkyiqeik
      361 siteinanfe ksvrlnekmi tktvarysqq lndlkaenar lnselekekh nkerleaeve
      421 slhsslatai neyneiverk dlelvlwrad dvsrhekmgs nisqltdkne llteqvhkar
      481 vkfntlkgkl retrdalrek tlalgsvqld lrqaqhrike mkqmhpngea kesqsigkqn
      541 sleerirqqe lenlllerql edarkegdnk eivinihrdc lengkedlle ernkelmkey
      601 nylkekllqc ekekaerevi vrefqeelvd hlktfsises plegtshchi nlnetwtskk
      661 klfqveiqpe ekheefrklf elisllnyta dqirkknrel eeeatgykkc lemtinmlna
      721 fanedfschg dlntdqlkmd ilfkklkqkf ndlvaekeav ssecvnlakd nevlhqells
      781 mrnvqekcek lekdkkmlee evlnlkthme kdmvelgklq eykseldera vqeiekleei
      841 hlqkqaeyek qleqlnkdnt aslkkkeltl kdveckfskm ktayeevtte leefkeafag
      901 avkannsmsk klmksdkkia vistklftek qrmkyflstl ptrpepelpc venlnsieln
      961 rkyipktair iptsnpqtsn ncknfltevl lc
//
LOCUS       NP_001011658             140 aa            linear   PRI 27-APR-2025
DEFINITION  trafficking protein particle complex subunit 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001011658
VERSION     NP_001011658.1
DBSOURCE    REFSEQ: accession NM_001011658.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Won,J.Y., Kim,D., Park,S.Y., Lee,H.R., Lim,J.S., Park,J.H.,
            Song,M.H., Song,H.R., Kim,O.H., Kim,Y. and Cho,T.J.
  TITLE     Novel loss-of-function variants of TRAPPC2 manifesting X-linked
            spondyloepiphyseal dysplasia tarda: report of two cases
  JOURNAL   BMC Med Genet 20 (1), 70 (2019)
   PUBMED   31053099
  REMARK    GeneRIF: Novel loss-of-function variants of TRAPPC2 manifesting
            X-linked spondyloepiphyseal dysplasia tarda: report of two cases
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Kim,J.J., Lipatova,Z. and Segev,N.
  TITLE     TRAPP Complexes in Secretion and Autophagy
  JOURNAL   Front Cell Dev Biol 4, 20 (2016)
   PUBMED   27066478
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Wu,X., Deng,K., Wang,C., Li,G., Lin,J., Wang,R., Wu,H. and Huang,S.
  TITLE     [Mutation analysis of the TRAPPC2 gene in a Chinese family with
            X-linked spondyloepiphyseal dysplasia tarda]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 32 (4), 476-480 (2015)
   PUBMED   26252088
  REMARK    GeneRIF: c.93+5G>A mutation in the TRAPPC2 gene is associated with
            X-linked spondyloepiphyseal dysplasia in a Chinese family.
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Milev,M.P., Hasaj,B., Saint-Dic,D., Snounou,S., Zhao,Q. and
            Sacher,M.
  TITLE     TRAMM/TrappC12 plays a role in chromosome congression, kinetochore
            stability, and CENP-E recruitment
  JOURNAL   J Cell Biol 209 (2), 221-234 (2015)
   PUBMED   25918224
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Gecz,J., Hillman,M.A., Gedeon,A.K., Cox,T.C., Baker,E. and
            Mulley,J.C.
  TITLE     Gene structure and expression study of the SEDL gene for
            spondyloepiphyseal dysplasia tarda
  JOURNAL   Genomics 69 (2), 242-251 (2000)
   PUBMED   11031107
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Gedeon,A.K., Colley,A., Jamieson,R., Thompson,E.M., Rogers,J.,
            Sillence,D., Tiller,G.E., Mulley,J.C. and Gecz,J.
  TITLE     Identification of the gene (SEDL) causing X-linked
            spondyloepiphyseal dysplasia tarda
  JOURNAL   Nat Genet 22 (4), 400-404 (1999)
   PUBMED   10431248
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Bernard,L.E., Chitayat,D., Weksberg,R., Van Allen,M.I. and
            Langlois,S.
  TITLE     Linkage analysis of two Canadian families segregating for X linked
            spondyloepiphyseal dysplasia
  JOURNAL   J Med Genet 33 (5), 432-434 (1996)
   PUBMED   8733060
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Adams,M.D., Soares,M.B., Kerlavage,A.R., Fields,C. and Venter,J.C.
  TITLE     Rapid cDNA sequencing (expressed sequence tags) from a
            directionally cloned human infant brain cDNA library
  JOURNAL   Nat Genet 4 (4), 373-380 (1993)
   PUBMED   8401585
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Tiller,G.E.
  TITLE     X-Linked Spondyloepiphyseal Dysplasia Tarda
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA344866.1, AK313736.1,
            AC003037.1 and AA770629.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is thought to be part of
            a large multi-subunit complex involved in the targeting and fusion
            of endoplasmic reticulum-to-Golgi transport vesicles with their
            acceptor compartment. In addition, the encoded protein can bind
            c-myc promoter-binding protein 1 and block its transcriptional
            repression capability. Mutations in this gene are a cause of
            spondyloepiphyseal dysplasia tarda (SEDT). A processed pseudogene
            of this gene is located on chromosome 19, and other pseudogenes are
            found on chromosomes 8 and Y. Alternatively spliced transcript
            variants have been found for this gene. [provided by RefSeq, Mar
            2010].
            
            Transcript Variant: This variant (1) encodes the shorter isoform
            (1). Variants 1 and 2 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.338880.1,
                                           SRR1660809.193340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380579.6/ ENSP00000369953.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..140
                     /product="trafficking protein particle complex subunit 2
                     isoform 1"
                     /note="sedlin; trafficking protein particle complex 2"
                     /calculated_mol_wt=16314
     Region          4..138
                     /region_name="TRAPPC2_sedlin"
                     /note="Trafficking protein particle complex subunit 2;
                     cd14825"
                     /db_xref="CDD:341429"
     Site            order(53..54,76..78,80,103,107,111)
                     /site_type="other"
                     /note="TRAPPC5 interface [polypeptide binding]"
                     /db_xref="CDD:341429"
     Site            order(108,111..114)
                     /site_type="other"
                     /note="TRAPPC3 interface [polypeptide binding]"
                     /db_xref="CDD:341429"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P0DI81.1)"
     CDS             1..140
                     /gene="TRAPPC2"
                     /gene_synonym="hYP38334; MIP2A; SEDL; SEDT; TRAPPC2P1;
                     TRS20; ZNF547L"
                     /coded_by="NM_001011658.4:258..680"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS48082.1"
                     /db_xref="GeneID:6399"
                     /db_xref="HGNC:HGNC:23068"
                     /db_xref="MIM:300202"
ORIGIN      
        1 msgsfyfviv ghhdnpvfem eflpagkaes kddhrhlnqf iahaaldlvd enmwlsnnmy
       61 lktvdkfnew fvsafvtagh mrfimlhdir qedgiknfft dvydlyikfs mnpfyepnsp
      121 irssafdrkv qflgkkhlls
//
LOCUS       NP_001171918              76 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial
            precursor [Homo sapiens].
ACCESSION   NP_001171918
VERSION     NP_001171918.1
DBSOURCE    REFSEQ: accession NM_001184989.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Guo,R., Zong,S., Wu,M., Gu,J. and Yang,M.
  TITLE     Architecture of Human Mitochondrial Respiratory Megacomplex
            I2III2IV2
  JOURNAL   Cell 170 (6), 1247-1257 (2017)
   PUBMED   28844695
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Stroud,D.A., Surgenor,E.E., Formosa,L.E., Reljic,B., Frazier,A.E.,
            Dibley,M.G., Osellame,L.D., Stait,T., Beilharz,T.H., Thorburn,D.R.,
            Salim,A. and Ryan,M.T.
  TITLE     Accessory subunits are integral for assembly and function of human
            mitochondrial complex I
  JOURNAL   Nature 538 (7623), 123-126 (2016)
   PUBMED   27626371
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 76)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   8  (residues 1 to 76)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
REFERENCE   9  (residues 1 to 76)
  AUTHORS   Emahazion,T., Beskow,A., Gyllensten,U. and Brookes,A.J.
  TITLE     Intron based radiation hybrid mapping of 15 complex I genes of the
            human electron transport chain
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 115-119 (1998)
   PUBMED   9763677
REFERENCE   10 (residues 1 to 76)
  AUTHORS   Ton,C., Hwang,D.M., Dempsey,A.A. and Liew,C.C.
  TITLE     Identification and primary structure of five human NADH-ubiquinone
            oxidoreductase subunits
  JOURNAL   Biochem Biophys Res Commun 241 (2), 589-594 (1997)
   PUBMED   9425316
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB160001.1 and W56292.1.
            
            Summary: The encoded protein is a subunit of the NADH:ubiquinone
            oxidoreductase (complex I), the first enzyme complex in the
            electron transport chain located in the inner mitochondrial
            membrane. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. Variants 1 through 7 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB160001.1, SRR18074968.2785795.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000394223.2/
                                                  ENSP00000377770.1
            RefSeq Select criteria             :: based on conservation,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..76
                     /product="NADH dehydrogenase [ubiquinone] 1 subunit C1,
                     mitochondrial precursor"
                     /note="complex I KFYI subunit; CI-KFYI; complex I-KFYI;
                     NADH-ubiquinone oxidoreductase KFYI subunit; NADH
                     dehydrogenase (ubiquinone) 1, subcomplex unknown, 1, 6kDa"
                     /calculated_mol_wt=5938
     transit_peptide 1..27
                     /inference="protein motif:SignalP:3.0"
                     /note="The cleavage site of the signal peptide has not
                     been experimentally determined."
                     /calculated_mol_wt=2814
     Region          28..76
                     /region_name="NADH_dh_m_C1"
                     /note="NADH dehydrogenase [ubiquinone] 1 subunit C1,
                     mitochondrial; pfam15088"
                     /db_xref="CDD:434447"
     Site            41..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43677.1)"
     CDS             1..76
                     /gene="NDUFC1"
                     /gene_synonym="KFYI"
                     /coded_by="NM_001184989.2:284..514"
                     /db_xref="CCDS:CCDS3746.1"
                     /db_xref="GeneID:4717"
                     /db_xref="HGNC:HGNC:7705"
                     /db_xref="MIM:603844"
ORIGIN      
        1 mapsallrpl srllaparlp sgpsvrskfy vreppnakpd wlkvgftlgt tvflwiylik
       61 qhnedileyk rrngle
//
LOCUS       NP_036410                347 aa            linear   PRI 27-APR-2025
DEFINITION  integrin beta-1-binding protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_036410
VERSION     NP_036410.1
DBSOURCE    REFSEQ: accession NM_012278.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Ferretti,R., Sbroggio,M., Di Savino,A., Fusella,F., Bertero,A.,
            Michowski,W., Tarone,G. and Brancaccio,M.
  TITLE     Morgana and melusin: two fairies chaperoning signal transduction
  JOURNAL   Cell Cycle 10 (21), 3678-3683 (2011)
   PUBMED   22037254
  REMARK    Review article
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Barki-Harrington,L. and Rockman,H.A.
  TITLE     Sensing heart stress
  JOURNAL   Nat Med 9 (1), 19-20 (2003)
   PUBMED   12514714
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Brancaccio,M., Fratta,L., Notte,A., Hirsch,E., Poulet,R.,
            Guazzone,S., De Acetis,M., Vecchione,C., Marino,G., Altruda,F.,
            Silengo,L., Tarone,G. and Lembo,G.
  TITLE     Melusin, a muscle-specific integrin beta1-interacting protein, is
            required to prevent cardiac failure in response to chronic pressure
            overload
  JOURNAL   Nat Med 9 (1), 68-75 (2003)
   PUBMED   12496958
  REMARK    GeneRIF: Studies in mouse show that melusin prevents cardiac
            dilation during chronic pressure overload by specifically sensing
            mechanical stress.
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Koistinen,P. and Heino,J.
  TITLE     The selective regulation of alpha Vbeta 1 integrin expression is
            based on the hierarchical formation of alpha V-containing
            heterodimers
  JOURNAL   J Biol Chem 277 (27), 24835-24841 (2002)
   PUBMED   11997396
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Brancaccio,M., Guazzone,S., Menini,N., Sibona,E., Hirsch,E., De
            Andrea,M., Rocchi,M., Altruda,F., Tarone,G. and Silengo,L.
  TITLE     Melusin is a new muscle-specific interactor for beta(1) integrin
            cytoplasmic domain
  JOURNAL   J Biol Chem 274 (41), 29282-29288 (1999)
   PUBMED   10506186
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Yan,Z., Chen,M., Perucho,M. and Friedman,E.
  TITLE     Oncogenic Ki-ras but not oncogenic Ha-ras blocks integrin
            beta1-chain maturation in colon epithelial cells
  JOURNAL   J Biol Chem 272 (49), 30928-30936 (1997)
   PUBMED   9388239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA895605.1 and AF110225.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein with two cysteine and
            histidine-rich (CHORD) domains, PXXP motifs, YXXI/P motifs,
            putative SH2 and SH3 domain binding motifs, and an acidic region at
            the C-terminus that can bind calcium. Two hybrid analysis showed
            that this protein interacts with the cytoplasmic domain of the beta
            1 integrin subunit and is thought to act as a chaperone protein.
            Studies in the mouse ortholog of this gene indicate that absence of
            this gene in mouse results in failed cardiac hypertrophy in
            response to mechanical stress. Alternative splicing results in
            multiple transcript variants encoding different isoforms, including
            an isoform that lacks several domains, including one of the CHORD
            domains. [provided by RefSeq, May 2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.133193.1,
                                           SRR5189655.208466.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373829.8/ ENSP00000362935.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..347
                     /product="integrin beta-1-binding protein 2 isoform 1"
                     /note="integrin beta-1-binding protein 2; integrin beta 1
                     binding protein (melusin) 2"
                     /calculated_mol_wt=38251
     Region          3..64
                     /region_name="CHORD"
                     /note="pfam04968"
                     /db_xref="CDD:461502"
     Region          28..31
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKP3.1)"
     Region          70..78
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKP3.1)"
     Region          148..208
                     /region_name="CHORD"
                     /note="pfam04968"
                     /db_xref="CDD:461502"
     Region          158..161
                     /region_name="SH2-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKP3.1)"
     Region          172..175
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKP3.1)"
     Region          218..304
                     /region_name="p23_melusin_like"
                     /note="p23_like domain similar to the C-terminal (tail)
                     domain of vertebrate Melusin and related proteins.
                     Melusin's tail domain interacts with the cytoplasmic
                     domain of beta1-A and beta1-D isoforms of beta1 integrin,
                     it does not bind other integrin beta...; cd06488"
                     /db_xref="CDD:107238"
     Region          234..237
                     /region_name="SH2-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKP3.1)"
     Region          319..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKP3.1)"
     CDS             1..347
                     /gene="ITGB1BP2"
                     /gene_synonym="CHORDC3; ITGB1BP; MELUSIN; MSTP015"
                     /coded_by="NM_012278.4:58..1101"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14411.1"
                     /db_xref="GeneID:26548"
                     /db_xref="HGNC:HGNC:6154"
                     /db_xref="MIM:300332"
ORIGIN      
        1 msllcrnkgc gqhfdpntnl pdscchhpgv pifhdalkgw sccrkrtvdf seflnikgct
       61 mgphcaeklp eapqpegpat ssslqeqkpl nvipksaetl rrerpkselp lkllplnisq
      121 alemaleqke ldqepgagld slirtgsscq npgcdavyqg pesdatpcty hpgaprfheg
      181 mkswsccgiq tldfgaflaq pgcrvgrhdw gkqlpascrh dwhqtdslvv vtvygqiplp
      241 afnwvkasqt elhvhivfdg nrvfqaqmkl wgvinveqss vflmpsrvei slvkadpgsw
      301 aqlehpdala kkaragvvle mdeeesddsd ddlswteeee eeeamge
//
LOCUS       NP_001357321             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357321
VERSION     NP_001357321.1
DBSOURCE    REFSEQ: accession NM_001370392.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2101561.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370392.1:1507..3156"
                     /note="isoform 1 is encoded by transcript variant 21"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_001144                321 aa            linear   PRI 27-APR-2025
DEFINITION  annexin A4 isoform a [Homo sapiens].
ACCESSION   NP_001144
VERSION     NP_001144.1
DBSOURCE    REFSEQ: accession NM_001153.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Vicic,N., Guo,X., Chan,D., Flanagan,J.G., Sigal,I.A. and Sivak,J.M.
  TITLE     Evidence of an Annexin A4 mediated plasma membrane repair response
            to biomechanical strain associated with glaucoma pathogenesis
  JOURNAL   J Cell Physiol 237 (9), 3687-3702 (2022)
   PUBMED   35862065
  REMARK    GeneRIF: Evidence of an Annexin A4 mediated plasma membrane repair
            response to biomechanical strain associated with glaucoma
            pathogenesis.
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Peng,Y., Zhang,Z., Zhang,A., Liu,C., Sun,Y., Peng,Z. and Liu,Y.
  TITLE     Membrane-cytoplasm translocation of annexin A4 is involved in the
            metastasis of colorectal carcinoma
  JOURNAL   Aging (Albany NY) 13 (7), 10312-10325 (2021)
   PUBMED   33761465
  REMARK    GeneRIF: Membrane-cytoplasm translocation of annexin A4 is involved
            in the metastasis of colorectal carcinoma.
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Liu,J., Wang,H., Zheng,M., Deng,L., Zhang,X. and Lin,B.
  TITLE     p53 and ANXA4/NF-kappaB p50 complexes regulate cell proliferation,
            apoptosis and tumor progression in ovarian clear cell carcinoma
  JOURNAL   Int J Mol Med 46 (6), 2102-2114 (2020)
   PUBMED   33125094
  REMARK    GeneRIF: p53 and ANXA4/NFkappaB p50 complexes regulate cell
            proliferation, apoptosis and tumor progression in ovarian clear
            cell carcinoma.
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Saad,Z.M., Fouad,Y., Ali,L.H. and Hassanin,T.M.
  TITLE     Clinical Significance of Annexin A4 as a Biomarker in the Early
            Diagnosis of Hepatocellular Carcinoma
  JOURNAL   Asian Pac J Cancer Prev 21 (9), 2661-2665 (2020)
   PUBMED   32986366
  REMARK    GeneRIF: Clinical Significance of Annexin A4 as a Biomarker in the
            Early Diagnosis of Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Tait,J.F., Smith,C., Frankenberry,D.A., Miao,C.H., Adler,D.A. and
            Disteche,C.M.
  TITLE     Chromosomal mapping of the human annexin IV (ANX4) gene
  JOURNAL   Genomics 12 (2), 313-318 (1992)
   PUBMED   1346776
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Freemont,P.S., Driessen,H.P., Verbi,W. and Crumpton,M.J.
  TITLE     Crystallization and preliminary X-ray crystallographic studies of
            human placental annexin IV
  JOURNAL   J Mol Biol 216 (2), 219-221 (1990)
   PUBMED   2254922
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Romisch,J., Grote,M., Weithmann,K.U., Heimburger,N. and Amann,E.
  TITLE     Annexin proteins PP4 and PP4-X. Comparative characterization of
            biological activities of placental and recombinant proteins
  JOURNAL   Biochem J 272 (1), 223-229 (1990)
   PUBMED   2148260
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Romisch,J. and Heimburger,N.
  TITLE     Purification and characterization of six annexins from human
            placenta
  JOURNAL   Biol Chem Hoppe Seyler 371 (5), 383-388 (1990)
   PUBMED   2143074
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Blackwood,R.A. and Ernst,J.D.
  TITLE     Characterization of Ca2(+)-dependent phospholipid binding, vesicle
            aggregation and membrane fusion by annexins
  JOURNAL   Biochem J 266 (1), 195-200 (1990)
   PUBMED   2138016
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC000182.1, D78152.1,
            AK058017.1, DB562261.1 and AC019206.4.
            
            Summary: Annexin IV (ANX4) belongs to the annexin family of
            calcium-dependent phospholipid binding proteins. Although their
            functions are still not clearly defined, several members of the
            annexin family have been implicated in membrane-related events
            along exocytotic and endocytotic pathways. ANX4 has 45 to 59%
            identity with other members of its family and shares a similar size
            and exon-intron organization. Isolated from human placenta, ANX4
            encodes a protein that has possible interactions with ATP, and has
            in vitro anticoagulant activity and also inhibits phospholipase A2
            activity. ANX4 is almost exclusively expressed in epithelial cells.
            Several transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK058017.1, SRR1163655.259565.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394295.6/ ENSP00000377833.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..321
                     /product="annexin A4 isoform a"
                     /note="annexin IV (placental anticoagulant protein II);
                     proliferation-inducing gene 28; proliferation-inducing
                     protein 28; annexin-4; endonexin I; lipocortin IV;
                     chromobindin-4; 35-beta calcimedin; carbohydrate-binding
                     protein p33/p41; epididymis secretory protein Li 274"
                     /calculated_mol_wt=35954
     Region          21..85
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          92..157
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          175..241
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          251..316
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     CDS             1..321
                     /gene="ANXA4"
                     /gene_synonym="ANX4; HEL-S-274; P32.5; PAP-II; PIG28;
                     PP4-X; ZAP36"
                     /coded_by="NM_001153.5:89..1054"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1894.1"
                     /db_xref="GeneID:307"
                     /db_xref="HGNC:HGNC:542"
                     /db_xref="MIM:106491"
ORIGIN      
        1 mamatkggtv kaasgfname daqtlrkamk glgtdedaii svlayrntaq rqeirtayks
       61 tigrdliddl kselsgnfeq vivgmmtptv lydvqelrra mkgagtdegc lieilasrtp
      121 eeirrisqty qqqygrsled dirsdtsfmf qrvlvslsag grdegnyldd alvrqdaqdl
      181 yeagekkwgt devkfltvlc srnrnhllhv fdeykrisqk dieqsikset sgsfedalla
      241 ivkcmrnksa yfaeklyksm kglgtddntl irvmvsraei dmldirahfk rlygkslysf
      301 ikgdtsgdyr kvllvlcggd d
//
LOCUS       NP_653168                544 aa            linear   PRI 27-APR-2025
DEFINITION  protein angel homolog 2 isoform a [Homo sapiens].
ACCESSION   NP_653168
VERSION     NP_653168.2
DBSOURCE    REFSEQ: accession NM_144567.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Clemente,P., Calvo-Garrido,J., Pearce,S.F., Schober,F.A.,
            Shigematsu,M., Siira,S.J., Laine,I., Spahr,H., Steinmetzger,C.,
            Petzold,K., Kirino,Y., Wibom,R., Rackham,O., Filipovska,A.,
            Rorbach,J., Freyer,C. and Wredenberg,A.
  TITLE     ANGEL2 phosphatase activity is required for non-canonical
            mitochondrial RNA processing
  JOURNAL   Nat Commun 13 (1), 5750 (2022)
   PUBMED   36180430
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Pinto,P.H., Kroupova,A., Schleiffer,A., Mechtler,K., Jinek,M.,
            Weitzer,S. and Martinez,J.
  TITLE     ANGEL2 is a member of the CCR4 family of deadenylases with
            2',3'-cyclic phosphatase activity
  JOURNAL   Science 369 (6503), 524-530 (2020)
   PUBMED   32732418
  REMARK    GeneRIF: ANGEL2 is a member of the CCR4 family of deadenylases with
            2',3'-cyclic phosphatase activity.
REFERENCE   4  (residues 1 to 544)
  AUTHORS   Yi,X., Hong,M., Gui,B., Chen,Z., Li,L., Xie,G., Liang,J., Wang,X.
            and Shang,Y.
  TITLE     RNA processing and modification protein, carbon catabolite
            repression 4 (Ccr4), arrests the cell cycle through p21-dependent
            and p53-independent pathway
  JOURNAL   J Biol Chem 287 (25), 21045-21057 (2012)
   PUBMED   22547059
REFERENCE   5  (residues 1 to 544)
  AUTHORS   Wagner,E., Clement,S.L. and Lykke-Andersen,J.
  TITLE     An unconventional human Ccr4-Caf1 deadenylase complex in nuclear
            cajal bodies
  JOURNAL   Mol Cell Biol 27 (5), 1686-1695 (2007)
   PUBMED   17178830
REFERENCE   6  (residues 1 to 544)
  AUTHORS   Lipovich,L., Hughes,A.L., King,M.C., Abkowitz,J.L. and Quigley,J.G.
  TITLE     Genomic structure and evolutionary context of the human feline
            leukemia virus subgroup C receptor (hFLVCR) gene: evidence for
            block duplications and de novo gene formation within duplicons of
            the hFLVCR locus
  JOURNAL   Gene 286 (2), 203-213 (2002)
   PUBMED   11943475
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC395916.1, AF510741.1, AL079275.1, BC016966.1, BC047469.1,
            AK022855.1, BX103687.1 and AI658922.1.
            
            On Sep 26, 2003 this sequence version replaced NP_653168.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.273818.1,
                                           SRR1660803.81945.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366962.8/ ENSP00000355929.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..544
                     /product="protein angel homolog 2 isoform a"
                     /note="protein angel homolog 2"
                     /calculated_mol_wt=62208
     Region          23..159
                     /region_name="ANGEL2_N"
                     /note="Protein angel homolog 2 N-terminal; pfam19339"
                     /db_xref="CDD:466047"
     Region          169..542
                     /region_name="EEP"
                     /note="Exonuclease-Endonuclease-Phosphatase (EEP) domain
                     superfamily; cl00490"
                     /db_xref="CDD:469791"
     Site            order(173,220,310,351,353,479,532..533)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197331"
     Site            order(220,532)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197331"
     Site            order(310,353,533)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197331"
     CDS             1..544
                     /gene="ANGEL2"
                     /gene_synonym="Ccr4d; KIAA0759L"
                     /coded_by="NM_144567.5:197..1831"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1512.1"
                     /db_xref="GeneID:90806"
                     /db_xref="HGNC:HGNC:30534"
                     /db_xref="MIM:619001"
ORIGIN      
        1 meawrcvrkg yghcvvgrgr ypmfphhsrs lgrdwttpwe nlqrccwnrh isscmrwpgh
       61 ysrapypyfs srhfslnwrp pclfesrtqf qycnwrpdnl sqtslihlss yvmnaegdep
      121 sskrrkhqgv ikrnweyics hdkektkilg dknvdpkced senkfdfsvm synilsqdll
      181 ednshlyrhc rrpvlhwsfr fpnilkeikh fdadvlclqe vqedhygaei rpsleslgyh
      241 ceykmrtgrk pdgcaicfkh skfsllsvnp veffrpdisl ldrdnvglvl llqpkipyaa
      301 cpaicvanth llynprrgdi kltqlamlla eissvahqkd gsfcpivmcg dfnsvpgspl
      361 ysfikegkln yeglpigkvs gqeqssrgqr ilsipiwppn lgisqncvye vqqvpkvekt
      421 dsdltqtqlk qtevlvtaek lssnlqhhfs lssvyshyfp dtgipevttc hsrsaitvdy
      481 ifysaekedv aghpgaeval vgglkllarl sllteqdlwt vnglpnenns sdhlpllakf
      541 rlel
//
LOCUS       NP_000293                727 aa            linear   PRI 27-APR-2025
DEFINITION  procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 isoform 2
            precursor [Homo sapiens].
ACCESSION   NP_000293 XP_001715814 XP_001720476 XP_001721327
VERSION     NP_000293.2
DBSOURCE    REFSEQ: accession NM_000302.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Cao,Z.R., Zheng,W.X., Jiang,Y.X., Chai,H., Gong,J.H., Zhao,M.J.,
            Yan,P., Liu,Y.Y., Liu,X.Y., Huang,Z.T., Yang,H., Peng,D.D.,
            Zong,K.Z. and Wu,Z.J.
  TITLE     miR-449a ameliorates acute rejection after liver transplantation
            via targeting procollagen-lysine1,2-oxoglutarate5-dioxygenase 1 in
            macrophages
  JOURNAL   Am J Transplant 23 (3), 336-352 (2023)
   PUBMED   36695693
  REMARK    GeneRIF: miR-449a ameliorates acute rejection after liver
            transplantation via targeting
            procollagen-lysine1,2-oxoglutarate5-dioxygenase 1 in macrophages.
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Zhang,J., Dong,Y., Shi,Z., He,H., Chen,J., Zhang,S., Wu,W.,
            Zhang,Q., Han,C. and Hao,L.
  TITLE     P3H4 and PLOD1 expression associates with poor prognosis in bladder
            cancer
  JOURNAL   Clin Transl Oncol 24 (8), 1524-1532 (2022)
   PUBMED   35149972
  REMARK    GeneRIF: P3H4 and PLOD1 expression associates with poor prognosis
            in bladder cancer.
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Yuan,B., Xu,Y. and Zheng,S.
  TITLE     PLOD1 acts as a tumor promoter in glioma via activation of the HSF1
            signaling pathway
  JOURNAL   Mol Cell Biochem 477 (2), 549-557 (2022)
   PUBMED   34845571
  REMARK    GeneRIF: PLOD1 acts as a tumor promoter in glioma via activation of
            the HSF1 signaling pathway.
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Koenig,S.N., Cavus,O., Williams,J., Bernier,M., Tonniges,J.,
            Sucharski,H., Dew,T., Akel,M., Baker,P., Madiai,F., De Giorgi,F.,
            Scietti,L., Faravelli,S., Forneris,F., Mohler,P.J. and Bradley,E.A.
  TITLE     New mechanistic insights to PLOD1-mediated human vascular disease
  JOURNAL   Transl Res 239, 1-17 (2022)
   PUBMED   34400365
  REMARK    GeneRIF: New mechanistic insights to PLOD1-mediated human vascular
            disease.
REFERENCE   5  (residues 1 to 727)
  AUTHORS   Zhang,Y., Wu,Y. and Su,X.
  TITLE     PLOD1 promotes cell growth and aerobic glycolysis by regulating the
            SOX9/PI3K/Akt/mTOR signaling pathway in gastric cancer
  JOURNAL   Front Biosci (Landmark Ed) 26 (8), 322-334 (2021)
   PUBMED   34455762
  REMARK    GeneRIF: PLOD1 promotes cell growth and aerobic glycolysis by
            regulating the SOX9/PI3K/Akt/mTOR signaling pathway in gastric
            cancer.
REFERENCE   6  (residues 1 to 727)
  AUTHORS   Rohrbach,M. and Giunta,C.
  TITLE     PLOD1-Related Kyphoscoliotic Ehlers-Danlos Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301635
REFERENCE   7  (residues 1 to 727)
  AUTHORS   Anttinen,H., Tuderman,L., Oikarinen,A. and Kivirikko,K.I.
  TITLE     Intracellular enzymes of collagen biosynthesis in human platelets
  JOURNAL   Blood 50 (1), 29-37 (1977)
   PUBMED   194639
REFERENCE   8  (residues 1 to 727)
  AUTHORS   Lanier,V.C. Jr., Serafin,D., Kleinert,H.F., Kutz,J.E., Atasoy,E.
            and Lister,G.
  TITLE     Microvascular procedures in reconstructive surgery
  JOURNAL   South Med J 69 (12), 1595-1597 (1976)
   PUBMED   798297
REFERENCE   9  (residues 1 to 727)
  AUTHORS   Steinmann,B., Gitzelmann,R., Vogel,A., Grant,M.E., Harwood,R. and
            Sear,C.H.
  TITLE     Ehlers-Danlos syndrome in two siblings with deficient lysyl
            hydroxylase activity in cultured skin fibroblasts but only mild
            hydroxylysine deficit in skin
  JOURNAL   Helv Paediatr Acta 30 (3), 255-274 (1975)
   PUBMED   1184396
REFERENCE   10 (residues 1 to 727)
  AUTHORS   Ryhanen,L.
  TITLE     Hydroxylation of lysyl residues in lysine-rich and arginine-rich
            histones by lysyl hydroxylase in vitro
  JOURNAL   Biochim Biophys Acta 397 (1), 50-57 (1975)
   PUBMED   1148262
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC334246.1, M98252.1 and
            BQ447373.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jun 11, 2008 this sequence version replaced
            XP_001720476.1, XP_001721327.1, XP_001715814.1, NP_000293.1.
            
            Summary: Lysyl hydroxylase is a membrane-bound homodimeric protein
            localized to the cisternae of the endoplasmic reticulum. The enzyme
            (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl
            residues in collagen-like peptides. The resultant hydroxylysyl
            groups are attachment sites for carbohydrates in collagen and thus
            are critical for the stability of intermolecular crosslinks. Some
            patients with Ehlers-Danlos syndrome type VI have deficiencies in
            lysyl hydroxylase activity. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2015].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region compared to variant 1. The resulting
            isoform (2) has the same N- and C-termini but is shorter compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.277372.1,
                                           SRR1803611.179944.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000196061.5/ ENSP00000196061.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..727
                     /product="procollagen-lysine,2-oxoglutarate 5-dioxygenase
                     1 isoform 2 precursor"
                     /EC_number="1.14.11.4"
                     /note="lysine hydroxylase; procollagen-lysine 1,
                     2-oxoglutarate 5-dioxygenase 1; procollagen lysyl
                     hydroxylase 1; lysyl hydroxlase 1"
                     /calculated_mol_wt=81562
     sig_peptide     1..18
                     /note="/evidence=ECO:0000269|PubMed:1577494; propagated
                     from UniProtKB/Swiss-Prot (Q02809.2)"
                     /calculated_mol_wt=2007
     mat_peptide     19..727
                     /product="Procollagen-lysine,2-oxoglutarate 5-dioxygenase
                     1. /id=PRO_0000024678"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02809.2)"
                     /calculated_mol_wt=81562
     Region          26..254
                     /region_name="GT_LH1"
                     /note="catalytic glycosyltransferase (GT) domain found in
                     lysyl hydroxylase 1 (LH1) and similar proteins; cd23004"
                     /db_xref="CDD:438560"
     Site            order(33..35,64,77,100..101,103,241,243)
                     /site_type="other"
                     /note="UDP binding site [chemical binding]"
                     /db_xref="CDD:438560"
     Site            order(100,103,241)
                     /site_type="other"
                     /note="Mn binding site [ion binding]"
                     /db_xref="CDD:438560"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02809.2)"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q02809.2)"
     Site            538
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q02809.2)"
     Region          562..725
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     Site            686
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02809.2)"
     CDS             1..727
                     /gene="PLOD1"
                     /gene_synonym="EDS6; EDSKCL1; LH; LH1; LLH; PLOD"
                     /coded_by="NM_000302.4:64..2247"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS142.1"
                     /db_xref="GeneID:5351"
                     /db_xref="HGNC:HGNC:9081"
                     /db_xref="MIM:153454"
ORIGIN      
        1 mrpllllall gwlllaeakg dakpednllv ltvatketeg frrfkrsaqf fnykiqalgl
       61 gedwnvekgt sagggqkvrl lkkalekhad kedlvilfad sydvlfasgp rellkkfrqa
      121 rsqvvfsaee liypdrrlet kypvvsdgkr flgsggfigy apnlsklvae wegqdsdsdq
      181 lfytkifldp ekreqinitl dhrcrifqnl dgaldevvlk femghvrarn laydtlpvli
      241 hgngptklql nylgnyiprf wtfetgctvc deglrslkgi gdealptvlv gvfieqptpf
      301 vslffqrllr lhypqkhmrl fihnheqhhk aqveeflaqh gseyqsvklv gpevrmanad
      361 arnmgadlcr qdrsctyyfs vdadvaltep nslrlliqqn knviaplmtr hgrlwsnfwg
      421 alsadgyyar sedyvdivqg rrvgvwnvpy isniylikgs alrgelqssd lfhhskldpd
      481 mafcanirqq dvfmfltnrh tlghllslds yrtthlhndl wevfsnpedw kekyihqnyt
      541 kalagklvet pcpdvywfpi ftevacdelv eemehfgqws lgnnkdnriq ggyenvptid
      601 ihmnqigfer ewhkflleyi apmteklypg yytraqfdla fvvrykpdeq pslmphhdas
      661 tftinialnr vgvdyegggc rflryncsir aprkgwtlmh pgrlthyheg lpttrgtryi
      721 avsfvdp
//
LOCUS       NP_003957               1074 aa            linear   PRI 27-APR-2025
DEFINITION  semaphorin-5A precursor [Homo sapiens].
ACCESSION   NP_003957
VERSION     NP_003957.2
DBSOURCE    REFSEQ: accession NM_003966.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Ye,Q., Liu,S., Lin,S. and Xie,W.
  TITLE     Circular RNA circSEMA5A facilitates colorectal cancer development
            by regulating microRNA-195-5p to target CCNE1 axis
  JOURNAL   Cell Signal 107, 110649 (2023)
   PUBMED   37164546
  REMARK    GeneRIF: Circular RNA circSEMA5A facilitates colorectal cancer
            development by regulating microRNA-195-5p to target CCNE1 axis.
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Wang,K., He,M., Fan,X., Zhou,J., Yang,J., Wang,L., Zhao,Z., Dai,C.
            and Zhang,Z.
  TITLE     SEMA5A-PLXNB3 Axis Promotes PDAC Liver Metastasis Outgrowth through
            Enhancing the Warburg Effect
  JOURNAL   J Immunol Res 2023, 3274467 (2023)
   PUBMED   36741230
  REMARK    GeneRIF: SEMA5A-PLXNB3 Axis Promotes PDAC Liver Metastasis
            Outgrowth through Enhancing the Warburg Effect.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Cheng,Q., Chen,M., Liu,M., Chen,X., Zhu,L., Xu,J., Xue,J., Wu,H.
            and Du,Y.
  TITLE     Semaphorin 5A suppresses ferroptosis through activation of
            PI3K-AKT-mTOR signaling in rheumatoid arthritis
  JOURNAL   Cell Death Dis 13 (7), 608 (2022)
   PUBMED   35835748
  REMARK    GeneRIF: Semaphorin 5A suppresses ferroptosis through activation of
            PI3K-AKT-mTOR signaling in rheumatoid arthritis.
            Erratum:[Cell Death Dis. 2023 Mar 14;14(3):196. doi:
            10.1038/s41419-023-05697-0. PMID: 36918551]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1074)
  AUTHORS   Karatas,K.S., Bahceci,I., Telatar,T.G., Bahceci,B. and Hocaoglu,C.
  TITLE     Relationship between disease and disease severity and semaphorin 5A
            and hemogram level in obsessive-compulsive disorder
  JOURNAL   Nord J Psychiatry 75 (7), 509-515 (2021)
   PUBMED   33771090
  REMARK    GeneRIF: Relationship between disease and disease severity and
            semaphorin 5A and hemogram level in obsessive-compulsive disorder.
REFERENCE   5  (residues 1 to 1074)
  AUTHORS   Lobna,M., Nasren,E., Adi,S., Jacob,B., Maria,G.A., Marcus,M. and
            Zahava,V.
  TITLE     The Expression of IL-17, in Chronic Spontaneous Urticaria Is Linked
            to Semaphorin5A
  JOURNAL   Biomolecules 11 (3), 373 (2021)
   PUBMED   33801296
  REMARK    GeneRIF: The Expression of IL-17, in Chronic Spontaneous Urticaria
            Is Linked to Semaphorin5A.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1074)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 1074)
  AUTHORS   Artigiani,S., Conrotto,P., Fazzari,P., Gilestro,G.F., Barberis,D.,
            Giordano,S., Comoglio,P.M. and Tamagnone,L.
  TITLE     Plexin-B3 is a functional receptor for semaphorin 5A
  JOURNAL   EMBO Rep 5 (7), 710-714 (2004)
   PUBMED   15218527
  REMARK    GeneRIF: Plexin-B3 is a functional receptor for semaphorin 5A
REFERENCE   8  (residues 1 to 1074)
  AUTHORS   Simmons,A.D., Puschel,A.W., McPherson,J.D., Overhauser,J. and
            Lovett,M.
  TITLE     Molecular cloning and mapping of human semaphorin F from the
            Cri-du-chat candidate interval
  JOURNAL   Biochem Biophys Res Commun 242 (3), 685-691 (1998)
   PUBMED   9464278
REFERENCE   9  (residues 1 to 1074)
  AUTHORS   Simmons,A.D., Overhauser,J. and Lovett,M.
  TITLE     Isolation of cDNAs from the Cri-du-chat critical region by direct
            screening of a chromosome 5-specific cDNA library
  JOURNAL   Genome Res 7 (2), 118-127 (1997)
   PUBMED   9049630
REFERENCE   10 (residues 1 to 1074)
  AUTHORS   Adams,R.H., Betz,H. and Puschel,A.W.
  TITLE     A novel class of murine semaphorins with homology to thrombospondin
            is differentially expressed during early embryogenesis
  JOURNAL   Mech Dev 57 (1), 33-45 (1996)
   PUBMED   8817451
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC034214.5, AC027335.6,
            AC091906.3, AC022446.6, AC027336.4 and AC021088.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 22, 2007 this sequence version replaced NP_003957.1.
            
            Summary: This gene belongs to the semaphorin gene family that
            encodes membrane proteins containing a semaphorin domain and
            several thrombospondin type-1 repeats. Members of this family are
            involved in axonal guidance during neural development. This gene
            has been implicated as an autism susceptibility gene.[provided by
            RefSeq, Jan 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK307587.1, U52840.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382496.10/ ENSP00000371936.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.31"
     Protein         1..1074
                     /product="semaphorin-5A precursor"
                     /note="semaphorin F; sema F; sema domain, seven
                     thrombospondin repeats (type 1 and type 1-like),
                     transmembrane domain (TM) and short cytoplasmic domain,
                     (semaphorin) 5A"
                     /calculated_mol_wt=118147
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2487
     mat_peptide     23..1074
                     /product="semaphorin-5A"
                     /calculated_mol_wt=118147
     Region          50..485
                     /region_name="Sema_5A"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 5A (Sema5A); cd11263"
                     /db_xref="CDD:200524"
     Site            order(105..108,158..159,163,185,187..188,195,205,208..209,
                     211,216,238,261..265,267,370,374,377)
                     /site_type="other"
                     /note="putative plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200524"
     Site            142
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Site            order(239..241,244..246,280,284..286,288,290,309..311,
                     315..316,383,398)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200524"
     Site            277
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Site            323
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Site            367
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Site            437
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Region          486..533
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Site            536
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Region          544..595
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            591
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Region          598..651
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          656..702
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            717
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Region          787..839
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          844..896
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          899..940
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            933
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13591.3)"
     Site            969..989
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13591.3)"
     CDS             1..1074
                     /gene="SEMA5A"
                     /gene_synonym="SEMAF; semF"
                     /coded_by="NM_003966.3:667..3891"
                     /db_xref="CCDS:CCDS3875.1"
                     /db_xref="GeneID:9037"
                     /db_xref="HGNC:HGNC:10736"
                     /db_xref="MIM:609297"
ORIGIN      
        1 mkgtcviawl fsslglwrla hpeaqgttqc qrtehpvisy keigpwlref raknavdfsq
       61 ltfdpgqkel vvgarnylfr lqledlsliq avewecdeat kkacyskgks keecqnyirv
      121 llvggdrlft cgtnaftpvc tnrslsnlte ihdqisgmar cpyspqhnst alltaggely
      181 aatamdfpgr dpaiyrslgi lpplrtaqyn skwlnepnfv ssydignfty fffrenaveh
      241 dcgktvfsra arvckndigg rflledtwtt fmkarlncsr pgevpfyyne lqstfflpel
      301 dliygifttn vnsiaasavc vfnlsaiaqa fsgpfkyqen srsawlpypn pnphfqcgtv
      361 dqglyvnlte rnlqdaqkfi lmhevvqpvt tvpsfmedns rfshvavdvv qgrealvhii
      421 ylatdygtik kvrvplnqts ssclleeiel fperrrepir slqilhsqsv lfvglrehvv
      481 kiplkrcqfy rtrstcigaq dpycgwdvvm kkctsleesl smtqweqsis acptrnltvd
      541 ghfgvwspwt pcthtdgsav gsclcrtrsc dspapqcggw qcegpgmeia ncsrnggwtp
      601 wtswspcstt cgigfqvrqr scsnptprhg grvcvgqnre erycnehllc pphmfwtgwg
      661 pwerctaqcg ggiqarrric engpdcagcn veyqscntnp cpelkkttpw tpwtpvnisd
      721 ngghyeqrfr ytckarladp nllevgrqri emrycssdgt sgcstdglsg dflragrysa
      781 htvngawsaw tswsqcsrdc srgirnrkrv cnnpepkygg mpclgpsley qecnilpcpv
      841 dgvwscwspw tkcsatcggg hymrtrscsn papayggdic lglhteealc ntqpcpesws
      901 ewsdwsecea sgvqvrarqc illfpmgsqc sgnttesrpc vfdsnfipev svarsssvee
      961 krcgefnmfh miavglsssi lgclltllvy tycqryqqqs hdatvihpvs paplntsitn
     1021 hinkldkyds veaikafnkn nlileernky fnphltgkty snayftdlnn ydey
//
LOCUS       NP_078936                355 aa            linear   PRI 27-APR-2025
DEFINITION  IGF-like family receptor 1 isoform a precursor [Homo sapiens].
ACCESSION   NP_078936
VERSION     NP_078936.1
DBSOURCE    REFSEQ: accession NM_024660.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Lobito,A.A., Ramani,S.R., Tom,I., Bazan,J.F., Luis,E.,
            Fairbrother,W.J., Ouyang,W. and Gonzalez,L.C.
  TITLE     Murine insulin growth factor-like (IGFL) and human IGFL1 proteins
            are induced in inflammatory skin conditions and bind to a novel
            tumor necrosis factor receptor family member, IGFLR1
  JOURNAL   J Biol Chem 286 (21), 18969-18981 (2011)
   PUBMED   21454693
  REMARK    GeneRIF: Murine insulin growth factor-like (IGFL) and human IGFL1
            proteins are induced in inflammatory skin conditions and bind to a
            novel tumor necrosis factor receptor family member, IGFLR1.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AD000671.1, AK026226.1 and BU621457.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026226.1, SRR1163657.212401.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000246532.6/ ENSP00000246532.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..355
                     /product="IGF-like family receptor 1 isoform a precursor"
                     /note="transmembrane protein 149"
                     /calculated_mol_wt=35695
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2218
     mat_peptide     23..355
                     /product="IGF-like family receptor 1. /id=PRO_0000290357"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H665.1)"
                     /calculated_mol_wt=35695
     Region          120..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H665.1)"
     Site            164..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H665.1)"
     CDS             1..355
                     /gene="IGFLR1"
                     /gene_synonym="TMEM149"
                     /coded_by="NM_024660.4:101..1168"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12472.1"
                     /db_xref="GeneID:79713"
                     /db_xref="HGNC:HGNC:23620"
                     /db_xref="MIM:614143"
ORIGIN      
        1 mgpgrcllta llllalappp easqycgrle ywnpdnkccs sclqrfgppp cpdyefrenc
       61 glndhgdfvt ppfrkcssgq cnpdgaelcs pcgggavtpt paagggrtpw rcrerpvpak
      121 ghcpltpgnp gapssqerss passiawrtp epvpqqawpn flplvvlvll ltlaviaill
      181 fillwhlcwp kekadpypyp glvcgvpnth tpssshlssp galetgdtwk easllpllsr
      241 elsslasqpl srlldelevl eelivlldpe pgpgggmahg ttrhlaaryg lpaawstfay
      301 slrpsrsplr aliemvvare psaslgqlgt hlaqlgrada lrvlsklgss gvcwa
//
LOCUS       NP_001030331             384 aa            linear   PRI 27-APR-2025
DEFINITION  early estrogen-induced gene 1 protein isoform a [Homo sapiens].
ACCESSION   NP_001030331
VERSION     NP_001030331.1
DBSOURCE    REFSEQ: accession NM_001035254.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Nongpiur,M.E., Cheng,C.Y., Duvesh,R., Vijayan,S., Baskaran,M.,
            Khor,C.C., Allen,J., Kavitha,S., Venkatesh,R., Goh,D., Husain,R.,
            Boey,P.Y., Quek,D., Ho,C.L., Wong,T.T., Perera,S., Wong,T.Y.,
            Krishnadas,S.R., Sundaresan,P., Aung,T. and Vithana,E.N.
  TITLE     Evaluation of Primary Angle-Closure Glaucoma Susceptibility Loci in
            Patients with Early Stages of Angle-Closure Disease
  JOURNAL   Ophthalmology 125 (5), 664-670 (2018)
   PUBMED   29310965
  REMARK    GeneRIF: In this study, 2 of 8 (primary angle-closure glaucoma)
            PACG-associated loci were associated significantly with PACS
            status, the earliest stage in the angle-closure glaucoma disease
            course. The association of these PACG loci with PACS status
            suggests that these loci may confer susceptibility to a narrow
            angle configuration.
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Choi,H.K., Kang,H.R., Jung,E., Kim,T.E., Lin,J.J. and Lee,S.Y.
  TITLE     Early estrogen-induced gene 1, a novel RANK signaling component, is
            essential for osteoclastogenesis
  JOURNAL   Cell Res 23 (4), 524-536 (2013)
   PUBMED   23478294
  REMARK    GeneRIF: EEIG1 is a novel RANK signaling component controlling
            RANK-mediated osteoclast formation.
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Wang,D.Y., Fulthorpe,R., Liss,S.N. and Edwards,E.A.
  TITLE     Identification of estrogen-responsive genes by complementary
            deoxyribonucleic acid microarray and characterization of a novel
            early estrogen-induced gene: EEIG1
  JOURNAL   Mol Endocrinol 18 (2), 402-411 (2004)
   PUBMED   14605097
  REMARK    GeneRIF: A novel estrogen-responsive gene was identified and named
            EEIG1 for early estrogen-induced gene 1
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL157935.28, AK058004.1, CN482844.1, BC047949.1 and BI008660.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.145466.1,
                                           SRR1803613.76497.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373095.6/ ENSP00000362187.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..384
                     /product="early estrogen-induced gene 1 protein isoform a"
                     /note="early estrogen-induced gene 1 protein; protein
                     FAM102A; sym-3 homolog A; family with sequence similarity
                     102 member A"
                     /calculated_mol_wt=41654
     Region          12..152
                     /region_name="NT-C2"
                     /note="N-terminal C2 in EEIG1 and EHBP1 proteins;
                     pfam10358"
                     /db_xref="CDD:463058"
     Region          129..138
                     /region_name="Required for interaction with
                     TNFRSF11A/RANK. /evidence=ECO:0000250|UniProtKB:Q78T81"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9C2.2)"
     Region          173..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9C2.2)"
     CDS             1..384
                     /gene="EEIG1"
                     /gene_synonym="bA203J24.7; C9orf132; FAM102A; SYM-3A"
                     /coded_by="NM_001035254.3:853..2007"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35150.1"
                     /db_xref="GeneID:399665"
                     /db_xref="HGNC:HGNC:31419"
                     /db_xref="MIM:610891"
ORIGIN      
        1 maflmkkkkf kfqttftlee ltavpfvngv lfckvrlldg gdfvslssre evqencvrwr
       61 krftfvckms anpatglldp cvfrvsvrke lkggkayskl gfadlnlaef agsgstvrcc
      121 llegydtknt rqdnsilkvt igmfllsgdp cfktppstak sisipgqdss lqltckgggt
      181 ssggsstnsl tgsrppkarp tilssglpee pdqnlsspee vfhsghsrns syasqqskis
      241 gystehsrss slsdlthrrn tstsssasgg lgmtvegpeg serehrppek pprpprplhl
      301 sdrsfrrkkd sveshptwvd dtridadaiv ekivqsqdft dgsntedsnl rlfvsrdgsa
      361 tlsgiqlatr vssgvyepvv iesh
//
LOCUS       NP_083813                226 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 98 [Mus musculus].
ACCESSION   NP_083813 XP_001001766
VERSION     NP_083813.1
DBSOURCE    REFSEQ: accession NM_029537.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Hassall,M.M., Javadiyan,S., Klebe,S., Awadalla,M.S., Sharma,S.,
            Qassim,A., White,M., Thomas,P.Q., Craig,J.E. and Siggs,O.M.
  TITLE     Phenotypic consequences of a nanophthalmos-associated TMEM98
            variant in human and mouse
  JOURNAL   Sci Rep 13 (1), 11017 (2023)
   PUBMED   37419942
  REMARK    GeneRIF: Phenotypic consequences of a nanophthalmos-associated
            TMEM98 variant in human and mouse.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Cross,S.H., Mckie,L., Hurd,T.W., Riley,S., Wills,J., Barnard,A.R.,
            Young,F., MacLaren,R.E. and Jackson,I.J.
  TITLE     The nanophthalmos protein TMEM98 inhibits MYRF self-cleavage and is
            required for eye size specification
  JOURNAL   PLoS Genet 16 (4), e1008583 (2020)
   PUBMED   32236127
  REMARK    GeneRIF: findings highlight the importance of the interplay between
            TMEM98 and MYRF in determining the size of the eye
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 226)
  AUTHORS   van der Wal,T., Lambooij,J.P. and van Amerongen,R.
  TITLE     TMEM98 is a negative regulator of FRAT mediated Wnt/ss-catenin
            signalling
  JOURNAL   PLoS One 15 (1), e0227435 (2020)
   PUBMED   31961879
  REMARK    GeneRIF: TMEM98 reduces FRAT2 protein levels and, accordingly,
            inhibits the FRAT2-mediated induction of ss-catenin/TCF signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Cross,S.H., Mckie,L., Keighren,M., West,K., Thaung,C., Davey,T.,
            Soares,D.C., Sanchez-Pulido,L. and Jackson,I.J.
  TITLE     Missense Mutations in the Human Nanophthalmos Gene TMEM98 Cause
            Retinal Defects in the Mouse
  JOURNAL   Invest Ophthalmol Vis Sci 60 (8), 2875-2887 (2019)
   PUBMED   31266059
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Huang,H., Teng,P., Du,J., Meng,J., Hu,X., Tang,T., Zhang,Z.,
            Qi,Y.B. and Qiu,M.
  TITLE     Interactive Repression of MYRF Self-Cleavage and Activity in
            Oligodendrocyte Differentiation by TMEM98 Protein
  JOURNAL   J Neurosci 38 (46), 9829-9839 (2018)
   PUBMED   30249802
  REMARK    GeneRIF: TMEM98 membrane protein physically interacts with MYRF in
            the endoplasmic reticulum and subsequently blocks its
            self-cleavage.
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Fu,W., Cheng,Y., Zhang,Y., Mo,X., Li,T., Liu,Y., Wang,P., Pan,W.,
            Chen,Y., Xue,Y., Ma,D., Zhang,Y. and Han,W.
  TITLE     The Secreted Form of Transmembrane Protein 98 Promotes the
            Differentiation of T Helper 1 Cells
  JOURNAL   J Interferon Cytokine Res 35 (9), 720-733 (2015)
   PUBMED   25946230
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Liakath-Ali,K., Vancollie,V.E., Heath,E., Smedley,D.P., Estabel,J.,
            Sunter,D., Ditommaso,T., White,J.K., Ramirez-Solis,R., Smyth,I.,
            Steel,K.P. and Watt,F.M.
  TITLE     Novel skin phenotypes revealed by a genome-wide mouse reverse
            genetic screen
  JOURNAL   Nat Commun 5, 3540 (2014)
   PUBMED   24721909
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Thaung,C., West,K., Clark,B.J., McKie,L., Morgan,J.E., Arnold,K.,
            Nolan,P.M., Peters,J., Hunter,A.J., Brown,S.D., Jackson,I.J. and
            Cross,S.H.
  TITLE     Novel ENU-induced eye mutations in the mouse: models for human eye
            disease
  JOURNAL   Hum Mol Genet 11 (7), 755-767 (2002)
   PUBMED   11929848
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BB872316.1 and AK148132.1.
            
            On May 4, 2006 this sequence version replaced XP_001001766.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011208.1, AK148132.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11"
     Protein         1..226
                     /product="transmembrane protein 98"
                     /calculated_mol_wt=24553
     Region          1..88
                     /region_name="Required for interaction with MYRF.
                     /evidence=ECO:0000269|PubMed:30249802"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91X86.1)"
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91X86.1)"
     Region          <48..152
                     /region_name="GCIP"
                     /note="Grap2 and cyclin-D-interacting; pfam13324"
                     /db_xref="CDD:463844"
     Region          207..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91X86.1)"
     CDS             1..226
                     /gene="Tmem98"
                     /gene_synonym="6530411B15Rik; Rwhs"
                     /coded_by="NM_029537.2:148..828"
                     /db_xref="CCDS:CCDS25135.1"
                     /db_xref="GeneID:103743"
                     /db_xref="MGI:MGI:1923457"
ORIGIN      
        1 metvvivaig vlatiflasf aalvvvcrqr ycrprdllqr ydskpivdli gametqseps
       61 elelddvvit nphieailen edwiedasgl mshciailki chtlteklva mtmgsgakmk
      121 tsasvsdiiv vakrisprvd dvvksmyppl dpklldartt alllsvshlv lvtrnachlt
      181 ggldwidqsl saaeehlevl reaalasepd kslpnpegfl qeqsai
//
LOCUS       NP_001275503             586 aa            linear   PRI 27-APR-2025
DEFINITION  protein phosphatase EYA1 isoform 4 [Homo sapiens].
ACCESSION   NP_001275503 XP_005251240
VERSION     NP_001275503.1
DBSOURCE    REFSEQ: accession NM_001288574.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Shao,H., Li,Y., Zhao,H., Lin,K., Gao,Y., Ming,C. and Ma,J.
  TITLE     [Clinical phenotypic and genetic analysis of syndrome families with
            EYA1 gene variants]
  JOURNAL   Lin Chuang Er Bi Yan Hou Tou Jing Wai Ke Za Zhi 38 (7), 636-640
            (2024)
   PUBMED   38973045
  REMARK    GeneRIF: [Clinical phenotypic and genetic analysis of syndrome
            families with EYA1 gene variants].
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Zhang,H., Gao,J., Wang,H., Liu,M., Lu,S., Xu,H., Tang,W. and
            Zheng,G.
  TITLE     Novel likely pathogenic variant in the EYA1 gene causing Branchio
            oto renal syndrome and the exploration of pathogenic mechanisms
  JOURNAL   BMC Med Genomics 17 (1), 89 (2024)
   PUBMED   38627775
  REMARK    GeneRIF: Novel likely pathogenic variant in the EYA1 gene causing
            Branchio oto renal syndrome and the exploration of pathogenic
            mechanisms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Wang,F., Zhang,R., Jian,J., Sun,Y. and Li,Q.
  TITLE     Identification and Functional Study of Enhancers of EYA1: The
            Causative Gene of Branchio-Oto-Renal Syndrome
  JOURNAL   Dev Neurosci 46 (5), 333-340 (2024)
   PUBMED   38228108
  REMARK    GeneRIF: Identification and Functional Study of Enhancers of EYA1:
            The Causative Gene of Branchio-Oto-Renal Syndrome.
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Yalcouye,A., Traore,O., Diarra,S., Schrauwen,I., Esoh,K.,
            Kadlubowska,M.K., Bharadwaj,T., Adadey,S.M., Keita,M., Guinto,C.O.,
            Leal,S.M., Landoure,G. and Wonkam,A.
  TITLE     A monoallelic variant in EYA1 is associated with Branchio-Otic
            syndrome in a Malian family
  JOURNAL   Mol Genet Genomic Med 10 (7), e1995 (2022)
   PUBMED   35698919
  REMARK    GeneRIF: A monoallelic variant in EYA1 is associated with
            Branchio-Otic syndrome in a Malian family.
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Pignoni,F., Hu,B., Zavitz,K.H., Xiao,J., Garrity,P.A. and
            Zipursky,S.L.
  TITLE     The eye-specification proteins So and Eya form a complex and
            regulate multiple steps in Drosophila eye development
  JOURNAL   Cell 91 (7), 881-891 (1997)
   PUBMED   9428512
  REMARK    Erratum:[Cell 1998 Feb 20;92(4):following 585]
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Abdelhak,S., Kalatzis,V., Heilig,R., Compain,S., Samson,D.,
            Vincent,C., Levi-Acobas,F., Cruaud,C., Le Merrer,M., Mathieu,M.,
            Konig,R., Vigneron,J., Weissenbach,J., Petit,C. and Weil,D.
  TITLE     Clustering of mutations responsible for branchio-oto-renal (BOR)
            syndrome in the eyes absent homologous region (eyaHR) of EYA1
  JOURNAL   Hum Mol Genet 6 (13), 2247-2255 (1997)
   PUBMED   9361030
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Abdelhak,S., Kalatzis,V., Heilig,R., Compain,S., Samson,D.,
            Vincent,C., Weil,D., Cruaud,C., Sahly,I., Leibovici,M.,
            Bitner-Glindzicz,M., Francis,M., Lacombe,D., Vigneron,J.,
            Charachon,R., Boven,K., Bedbeder,P., Van Regemorter,N.,
            Weissenbach,J. and Petit,C.
  TITLE     A human homologue of the Drosophila eyes absent gene underlies
            branchio-oto-renal (BOR) syndrome and identifies a novel gene
            family
  JOURNAL   Nat Genet 15 (2), 157-164 (1997)
   PUBMED   9020840
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Smith,R.J.H.
  TITLE     Branchiootorenal Spectrum Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301554
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Stoppa-Lyonnet,D., Carter,P.E., Meo,T. and Tosi,M.
  TITLE     Clusters of intragenic Alu repeats predispose the human C1
            inhibitor locus to deleterious rearrangements
  JOURNAL   Proc Natl Acad Sci U S A 87 (4), 1551-1555 (1990)
   PUBMED   2154751
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016465.8 and AC022858.8.
            
            On Dec 21, 2013 this sequence version replaced XP_005251240.1.
            
            Summary: This gene encodes a member of the eyes absent (EYA) family
            of proteins. The encoded protein may play a role in the developing
            kidney, branchial arches, eye, and ear. Mutations of this gene have
            been associated with branchiootorenal dysplasia syndrome,
            branchiootic syndrome, and sporadic cases of congenital cataracts
            and ocular anterior segment anomalies. A similar protein in mice
            can act as a transcriptional activator. Alternatively spliced
            transcript variants have been identified for this gene. [provided
            by RefSeq, Dec 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.201108.1,
                                           SRR14038193.3926553.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.3"
     Protein         1..586
                     /product="protein phosphatase EYA1 isoform 4"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="eyes absent homolog 1; protein phosphatase EYA1"
                     /calculated_mol_wt=63822
     Region          <32..273
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          234..314
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99502.2)"
     Region          315..586
                     /region_name="HAD_Eya"
                     /note="protein tyrosine phosphatase domain of the nuclear
                     transcription factor of Eyes absent (Eya) and related
                     phosphatase domains; cd02601"
                     /db_xref="CDD:319789"
     Site            order(317,544,546,562,564..567,573,576,579..580,583..586)
                     /site_type="other"
                     /note="SIX1 interface [polypeptide binding]"
                     /db_xref="CDD:319789"
     Site            order(322..326,416..417,525,549..550,554..555)
                     /site_type="active"
                     /db_xref="CDD:319789"
     CDS             1..586
                     /gene="EYA1"
                     /gene_synonym="BOP; BOR; BOS1; OFC1; OTFCS"
                     /coded_by="NM_001288574.2:478..2238"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS75750.1"
                     /db_xref="GeneID:2138"
                     /db_xref="HGNC:HGNC:3519"
                     /db_xref="MIM:601653"
ORIGIN      
        1 memqdltsph srlsgssesp sgpklgnshi nsnsmtpngt evktepmsss etasttadgs
       61 lnnfsgsaig sssfsprpth qfsppqiyps kpyphilptp ssqtmaaygq tqfttgmqqa
      121 tayatypqpg qpygissygi ktegglsqsq spgqtgflsy gtsfstpqpg qapysyqmqg
      181 ssfttssgiy tgnnsltnss gfnssqqdyp sypsfgqgqy aqyynsspyp ahymtssnts
      241 pttpstnaty qlqeppsgit sqavtdptae ystihspstp ikdsdsdrlr rgsdgksrgr
      301 grrnnnpspp pdsdlervfi wdldetiivf hslltgsyan rygrdpptsv slglrmeemi
      361 fnladthlff ndleecdqvh iddvssddng qdlstynfgt dgfpaaatsa nlclatgvrg
      421 gvdwmrklaf ryrrvkeiyn tyknnvggll gpakreawlq lraeiealtd swltlalkal
      481 slihsrtncv nilvtttqli palakvllyg lgivfpieni ysatkigkes cferiiqrfg
      541 rkvvyvvigd gveeeqgakk hampfwriss hsdlmalhha leleyl
//
LOCUS       NP_001357318             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357318
VERSION     NP_001357318.1
DBSOURCE    REFSEQ: accession NM_001370389.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.4935.1,
                                           SRR1803615.41995.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370389.1:1634..3283"
                     /note="isoform 1 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_083333                766 aa            linear   ROD 27-APR-2025
DEFINITION  TBC1 domain family member 30 isoform 1 [Mus musculus].
ACCESSION   NP_083333 XP_001481319 XP_137322
VERSION     NP_083333.1
DBSOURCE    REFSEQ: accession NM_029057.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC138286.1 and BC059081.1.
            
            On or before Jun 26, 2009 this sequence version replaced
            XP_001481319.1, XP_137322.8.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC138286.1, BC072607.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164139 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10"
     Protein         1..766
                     /product="TBC1 domain family member 30 isoform 1"
                     /note="TBC1 domain family member 30-like"
                     /calculated_mol_wt=84762
     Region          85..306
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Region          380..406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q69ZT9.2)"
     Region          475..603
                     /region_name="DUF4682"
                     /note="Domain of unknown function (DUF4682); pfam15733"
                     /db_xref="CDD:464830"
     Region          603..647
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q69ZT9.2)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q69ZT9.2)"
     Region          731..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q69ZT9.2)"
     CDS             1..766
                     /gene="Tbc1d30"
                     /gene_synonym="4930505D03Rik; 9530013E20Rik"
                     /coded_by="NM_029057.2:597..2897"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS48704.1"
                     /db_xref="GeneID:74694"
                     /db_xref="MGI:MGI:1921944"
ORIGIN      
        1 mrqdkltgsl rrggrclkrq ggggvgtils nvlkkrscis rtaprllctl epgvdtklkf
       61 tlepslgqng fqqwydalka varlstgipk ewrrkvwltl adhylhsiai dwdktmrftf
      121 nersnpddds mgiqivkdlh rtgcssycgq eaeqdrvvlk rvllayarwn knvgycqgfn
      181 ilaalilevm egnegdalki miylidkvlp esyfvnnlra lsvdmavfrd llrlklpels
      241 qhldtlqrta nkesgggyep pltnvftmqw fltlfatclp nhtvlkiwds vffegseiil
      301 rvslaiwakl geqiecceta defygtmgrl tqemleqdll qshelmqtvy smapfpfpql
      361 aelrekytyn itpfpatikp tsvsgrhska rdsddengpd dedavasavg clgplsglla
      421 pelqkyqkqi keateeqtlr snniaelspg ainscrseyh aafnsmmmer mttdinalkr
      481 qysrikkkqq qqlhqvyira dkgpvtsilp sqansspvin hlllgkkmki tnraaknavi
      541 hvpghpggki spvpyedikt klnspwrthi rvhkknmprt kshlgcgdtv glieeqsegc
      601 kasslgaaee fpsgrtvtah segssgdgdg ggstprtieg qspepvfgda dvdvaavqvk
      661 lealelnqrd aaaetepkvh fpcqrhasel adapgenqta ikllpgstsk tpifspfpsv
      721 kplrksatar nlglygpter tpnvhfpqms rgfnksgign sstkkr
//
LOCUS       NP_001350456             448 aa            linear   PRI 27-APR-2025
DEFINITION  interferon gamma receptor 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001350456 XP_006715534
VERSION     NP_001350456.1
DBSOURCE    REFSEQ: accession NM_001363527.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Dhiman,N.S., Saini,V. and Kumar,V.
  TITLE     Single nucleotide polymorphism rs2234711 of interferon gamma
            receptor 1 is associated with pulmonary tuberculosis in the
            population of North India
  JOURNAL   Cytokine 169, 156274 (2023)
   PUBMED   37327531
  REMARK    GeneRIF: Single nucleotide polymorphism rs2234711 of interferon
            gamma receptor 1 is associated with pulmonary tuberculosis in the
            population of North India.
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Tsai,K.D., Lee,Y.C., Chen,B.Y., Wu,L.S., Liang,S.Y., Liu,M.Y.,
            Hung,Y.W., Hsu,H.L., Chen,P.Q., Shieh,J.C., Lee,Y.J. and Lin,T.H.
  TITLE     Recombinant Klotho attenuates IFNgamma receptor signaling and
            SAMHD1 expression through blocking NF-kappaB translocation in
            glomerular mesangial cells
  JOURNAL   Int J Med Sci 20 (6), 810-817 (2023)
   PUBMED   37213666
  REMARK    GeneRIF: Recombinant Klotho attenuates IFNgamma receptor signaling
            and SAMHD1 expression through blocking NF-kappaB translocation in
            glomerular mesangial cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Wu,S.Q., Ding,X.J., Yang,Q.L., Wang,M.G. and He,J.Q.
  TITLE     IFNG and IFNGR1 polymorphisms are associated with tuberculosis: a
            case-control study
  JOURNAL   Eur Rev Med Pharmacol Sci 26 (23), 8777-8787 (2022)
   PUBMED   36524496
  REMARK    GeneRIF: IFNG and IFNGR1 polymorphisms are associated with
            tuberculosis: a case-control study.
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Cheng,L., Zhang,F., Wang,Y., Chen,J. and Yuan,X.
  TITLE     Association between IFNGR1 gene polymorphisms and tuberculosis
            susceptibility: A meta-analysis
  JOURNAL   Front Public Health 10, 976221 (2022)
   PUBMED   36148347
  REMARK    GeneRIF: Association between IFNGR1 gene polymorphisms and
            tuberculosis susceptibility: A meta-analysis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Varahram,M., Besharati,S., Farnia,P., Ghanavi,J., Saif,S.,
            Nia,J.H., Madani,M.R., Farnia,P. and Velayati,A.A.
  TITLE     Correlation of single-nucleotide polymorphism at interferon-gamma
            R1 (at Position - 56) in positive purified protein derivative
            health workers with COVID-19 infection
  JOURNAL   Int J Mycobacteriol 11 (3), 318-322 (2022)
   PUBMED   36260452
  REMARK    GeneRIF: Correlation of single-nucleotide polymorphism at
            interferon-gamma R1 (at Position - 56) in positive purified protein
            derivative health workers with COVID-19 infection.
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Szente,B.E., Subramaniam,P.S. and Johnson,H.M.
  TITLE     Identification of IFN-gamma receptor binding sites for JAK2 and
            enhancement of binding by IFN-gamma and its C-terminal peptide
            IFN-gamma(95-133)
  JOURNAL   J Immunol 155 (12), 5617-5622 (1995)
   PUBMED   7499845
REFERENCE   7  (residues 1 to 448)
  AUTHORS   van Loon,A.P., Ozmen,L., Fountoulakis,M., Kania,M., Haiker,M. and
            Garotta,G.
  TITLE     High-affinity receptor for interferon-gamma (IFN-gamma), a
            ubiquitous protein occurring in different molecular forms on human
            cells: blood monocytes and eleven different cell lines have the
            same IFN-gamma receptor protein
  JOURNAL   J Leukoc Biol 49 (5), 462-473 (1991)
   PUBMED   1826725
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Le Coniat,M., Alcaide-Loridan,C., Fellous,M. and Berger,R.
  TITLE     Human interferon gamma receptor 1 (IFNGR1) gene maps to chromosome
            region 6q23-6q24
  JOURNAL   Hum Genet 84 (1), 92-94 (1989)
   PUBMED   2532616
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Aguet,M., Dembic,Z. and Merlin,G.
  TITLE     Molecular cloning and expression of the human interferon-gamma
            receptor
  JOURNAL   Cell 55 (2), 273-280 (1988)
   PUBMED   2971451
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Novick,D., Orchansky,P., Revel,M. and Rubinstein,M.
  TITLE     The human interferon-gamma receptor. Purification,
            characterization, and preparation of antibodies
  JOURNAL   J Biol Chem 262 (18), 8483-8487 (1987)
   PUBMED   2954953
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL050337.6.
            
            On May 21, 2018 this sequence version replaced XP_006715534.1.
            
            Summary: This gene (IFNGR1) encodes the ligand-binding chain
            (alpha) of the gamma interferon receptor. Human interferon-gamma
            receptor is a heterodimer of IFNGR1 and IFNGR2. A genetic variation
            in IFNGR1 is associated with susceptibility to Helicobacter pylori
            infection. In addition, defects in IFNGR1 are a cause of mendelian
            susceptibility to mycobacterial disease, also known as familial
            disseminated atypical mycobacterial infection. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3) is
            shorter at the N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.27943.1,
                                           SRR11853560.25375.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.3"
     Protein         1..448
                     /product="interferon gamma receptor 1 isoform 3"
                     /note="antiviral protein, type 2; CD119 antigen; AVP, type
                     2; interferon-gamma receptor alpha chain; immune
                     interferon receptor 1; IFN-gamma-R-alpha; CDw119;
                     IFN-gamma-R1; IFN-gamma receptor 1"
                     /calculated_mol_wt=49970
     Region          <1..72
                     /region_name="Tissue_fac"
                     /note="Tissue factor; pfam01108"
                     /db_xref="CDD:460067"
     Region          120..276
                     /region_name="Interfer-bind"
                     /note="Interferon-alpha/beta receptor, fibronectin type
                     III; cl46366"
                     /db_xref="CDD:480706"
     CDS             1..448
                     /gene="IFNGR1"
                     /gene_synonym="CD119; IFNGR; IMD27A; IMD27B"
                     /coded_by="NM_001363527.1:564..1910"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS87445.1"
                     /db_xref="GeneID:3459"
                     /db_xref="HGNC:HGNC:5439"
                     /db_xref="MIM:107470"
ORIGIN      
        1 mnpivyweyq impqvpvftv evknygvkns ewidacinis hhycnisdhv gdpsnslwvr
       61 vkarvgqkes ayakseefav crdgkigppk ldirkeekqi midifhpsvf vngdeqevdy
      121 dpettcyirv ynvyvrmngs eiqykiltqk eddcdeiqcq laipvsslns qycvsaegvl
      181 hvwgvtteks kevcitifns sikgslwipv vaalllflvl slvficfyik kinplkeksi
      241 ilpkslisvv rsatletkpe skyvslitsy qpfslekevv ceeplspatv pgmhtednpg
      301 kvehteelss itevvtteen ipdvvpgshl tpieresssp lssnqsepgs ialnsyhsrn
      361 csesdhsrng fdtdsscles hsslsdsefp pnnkgeikte gqelitvika ptsfgydkph
      421 vlvdllvdds gkesligyrp tedskefs
//
LOCUS       NP_001353904             343 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type 1B isoform c [Homo
            sapiens].
ACCESSION   NP_001353904
VERSION     NP_001353904.1
DBSOURCE    REFSEQ: accession NM_001366975.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Cho,Y.A., Choi,S., Park,S., Park,C.K. and Ha,S.Y.
  TITLE     Expression of Pregnancy Up-regulated Non-ubiquitous Calmodulin
            Kinase (PNCK) in Hepatocellular Carcinoma
  JOURNAL   Cancer Genomics Proteomics 17 (6), 747-755 (2020)
   PUBMED   33099476
  REMARK    GeneRIF: Expression of Pregnancy Up-regulated Non-ubiquitous
            Calmodulin Kinase (PNCK) in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Deb,T.B., Zuo,A.H., Barndt,R.J., Sengupta,S., Jankovic,R. and
            Johnson,M.D.
  TITLE     Pnck overexpression in HER-2 gene-amplified breast cancer causes
            Trastuzumab resistance through a paradoxical PTEN-mediated process
  JOURNAL   Breast Cancer Res Treat 150 (2), 347-361 (2015)
   PUBMED   25773930
  REMARK    GeneRIF: Pnck may be a marker of Trastuzumab resistance and
            possibly a therapeutic target in breast cancer.
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Wu,S., Lv,Z., Wang,Y., Sun,L., Jiang,Z., Xu,C., Zhao,J., Sun,X.,
            Li,X., Hu,L., Tang,A., Gui,Y., Zhou,F., Cai,Z. and Wang,R.
  TITLE     Increased expression of pregnancy up-regulated non-ubiquitous
            calmodulin kinase is associated with poor prognosis in clear cell
            renal cell carcinoma
  JOURNAL   PLoS One 8 (4), e59936 (2013)
   PUBMED   23634203
  REMARK    GeneRIF: the relationship between PNCK and prognosis in clear cell
            renal cell carcinoma
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Deb,T.B., Zuo,A.H., Wang,Y., Barndt,R.J., Cheema,A.K., Sengupta,S.,
            Coticchia,C.M. and Johnson,M.D.
  TITLE     Pnck induces ligand-independent EGFR degradation by probable
            perturbation of the Hsp90 chaperone complex
  JOURNAL   Am J Physiol Cell Physiol 300 (5), C1139-C1154 (2011)
   PUBMED   21325639
  REMARK    GeneRIF: Pnck induces epidermal growth factor receptor degradation,
            most likely through perturbation of Hsp90 chaperone activity due to
            Hsp90 phosphorylation.  Epidermal growth factor receptor
            degradation is coupled to proteasomal degradation of Pnck.
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Deb,T.B., Coticchia,C.M., Barndt,R., Zuo,H., Dickson,R.B. and
            Johnson,M.D.
  TITLE     Pregnancy-upregulated nonubiquitous calmodulin kinase induces
            ligand-independent EGFR degradation
  JOURNAL   Am J Physiol Cell Physiol 295 (2), C365-C377 (2008)
   PUBMED   18562482
  REMARK    GeneRIF: Pnck induces ligand-independent EGFR degradation, and it
            may represent an attractive therapeutic target in EGFR-regulated
            oncogenesis.
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Gardner,H.P., Ha,S.I., Reynolds,C. and Chodosh,L.A.
  TITLE     The caM kinase, Pnck, is spatially and temporally regulated during
            murine mammary gland development and may identify an epithelial
            cell subtype involved in breast cancer
  JOURNAL   Cancer Res 60 (19), 5571-5577 (2000)
   PUBMED   11034105
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Gardner,H.P., Rajan,J.V., Ha,S.I., Copeland,N.G., Gilbert,D.J.,
            Jenkins,N.A., Marquis,S.T. and Chodosh,L.A.
  TITLE     Cloning, characterization, and chromosomal localization of Pnck, a
            Ca(2+)/calmodulin-dependent protein kinase
  JOURNAL   Genomics 63 (2), 279-288 (2000)
   PUBMED   10673339
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U52111.3.
            
            Summary: PNCK is a member of the calcium/calmodulin-dependent
            protein kinase family of protein serine/threonine kinases (see
            CAMK1; MIM 604998) (Gardner et al., 2000 [PubMed
            10673339]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (3), as well as variants 4-8,
            encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.797576.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..343
                     /product="calcium/calmodulin-dependent protein kinase type
                     1B isoform c"
                     /EC_number="2.7.11.17"
                     /note="pregnancy upregulated non-ubiquitously expressed
                     CaM kinase; calcium/calmodulin-dependent protein kinase
                     type 1B; caMKI-beta; caM-KI beta; caM kinase IB; caM
                     kinase I beta; pregnancy up-regulated
                     non-ubiquitously-expressed CaM kinase"
                     /calculated_mol_wt=38369
     Region          11..287
                     /region_name="STKc_CaMKI_beta"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type I beta;
                     cd14169"
                     /db_xref="CDD:271071"
     Site            order(21..25,29,42,44,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,173..177,179)
                     /site_type="active"
                     /db_xref="CDD:271071"
     Site            order(21..24,29,42,44,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271071"
     Site            order(25,97,99,135..136,138,140,160,173..177,179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271071"
     Site            156..177
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271071"
     Region          290..311
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2M8.2)"
     Region          319..343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2M8.2)"
     CDS             1..343
                     /gene="PNCK"
                     /gene_synonym="BSTK3; CaMK1b"
                     /coded_by="NM_001366975.1:668..1699"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS94698.1"
                     /db_xref="GeneID:139728"
                     /db_xref="HGNC:HGNC:13415"
                     /db_xref="MIM:300680"
ORIGIN      
        1 mlllkkhted issvyeirer lgsgafsevv laqergsahl valkcipkka lrgkealven
       61 eiavlrrish pnivaledvh espshlylam elvtggelfd rimergsyte kdashlvgqv
      121 lgavsylhsl givhrdlkpe nllyatpfed skimvsdfgl skiqagnmlg tacgtpgyva
      181 pelleqkpyg kavdvwalgv isyillcgyp pfydesdpel fsqilrasye fdspfwddis
      241 esakdfirhl lerdpqkrft cqqalrhlwi sgdtafdrdi lgsvseqirk nfarthwkra
      301 fnatsflrhi rklgqipege gaseqgmarh shsglragqp pkw
//
LOCUS       NP_078817                689 aa            linear   PRI 27-APR-2025
DEFINITION  armadillo-like helical domain-containing protein 3 [Homo sapiens].
ACCESSION   NP_078817
VERSION     NP_078817.2
DBSOURCE    REFSEQ: accession NM_024541.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Mizuike,A. and Hanada,K.
  TITLE     DGARM/C10orf76/ARMH3 for Ceramide Transfer Zone at the Endoplasmic
            Reticulum-Distal Golgi Contacts
  JOURNAL   Contact (Thousand Oaks) 7, 25152564241239443 (2024)
   PUBMED   38515862
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Mizuike,A., Sakai,S., Katoh,K., Yamaji,T. and Hanada,K.
  TITLE     The C10orf76-PI4KB axis orchestrates CERT-mediated ceramide
            trafficking to the distal Golgi
  JOURNAL   J Cell Biol 222 (7) (2023)
   PUBMED   37195633
  REMARK    GeneRIF: The C10orf76-PI4KB axis orchestrates CERT-mediated
            ceramide trafficking to the distal Golgi.
REFERENCE   3  (residues 1 to 689)
  AUTHORS   McPhail,J.A., Lyoo,H., Pemberton,J.G., Hoffmann,R.M., van Elst,W.,
            Strating,J.R.P.M., Jenkins,M.L., Stariha,J.T.B., Powell,C.J.,
            Boulanger,M.J., Balla,T., van Kuppeveld,F.J.M. and Burke,J.E.
  TITLE     Characterization of the c10orf76-PI4KB complex and its necessity
            for Golgi PI4P levels and enterovirus replication
  JOURNAL   EMBO Rep 21 (2), e48441 (2020)
   PUBMED   31829496
REFERENCE   4  (residues 1 to 689)
  AUTHORS   Chan,C.J., Le,R., Burns,K., Ahmed,K., Coyaud,E., Laurent,E.M.N.,
            Raught,B. and Melancon,P.
  TITLE     BioID Performed on Golgi Enriched Fractions Identify C10orf76 as a
            GBF1 Binding Protein Essential for Golgi Maintenance and Secretion
  JOURNAL   Mol Cell Proteomics 18 (11), 2285-2297 (2019)
   PUBMED   31519766
REFERENCE   5  (residues 1 to 689)
  AUTHORS   Rietveld,C.A., Esko,T., Davies,G., Pers,T.H., Turley,P.,
            Benyamin,B., Chabris,C.F., Emilsson,V., Johnson,A.D., Lee,J.J., de
            Leeuw,C., Marioni,R.E., Medland,S.E., Miller,M.B., Rostapshova,O.,
            van der Lee,S.J., Vinkhuyzen,A.A., Amin,N., Conley,D.,
            Derringer,J., van Duijn,C.M., Fehrmann,R., Franke,L., Glaeser,E.L.,
            Hansell,N.K., Hayward,C., Iacono,W.G., Ibrahim-Verbaas,C.,
            Jaddoe,V., Karjalainen,J., Laibson,D., Lichtenstein,P.,
            Liewald,D.C., Magnusson,P.K., Martin,N.G., McGue,M., McMahon,G.,
            Pedersen,N.L., Pinker,S., Porteous,D.J., Posthuma,D.,
            Rivadeneira,F., Smith,B.H., Starr,J.M., Tiemeier,H., Timpson,N.J.,
            Trzaskowski,M., Uitterlinden,A.G., Verhulst,F.C., Ward,M.E.,
            Wright,M.J., Davey Smith,G., Deary,I.J., Johannesson,M., Plomin,R.,
            Visscher,P.M., Benjamin,D.J., Cesarini,D. and Koellinger,P.D.
  TITLE     Common genetic variants associated with cognitive performance
            identified using the proxy-phenotype method
  JOURNAL   Proc Natl Acad Sci U S A 111 (38), 13790-13794 (2014)
   PUBMED   25201988
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2015 Jan 27;112(4):E380. doi:
            10.1073/pnas.1424631112. PMID: 25572966]
REFERENCE   6  (residues 1 to 689)
  AUTHORS   Wojczynski,M.K., Li,M., Bielak,L.F., Kerr,K.F., Reiner,A.P.,
            Wong,N.D., Yanek,L.R., Qu,L., White,C.C., Lange,L.A.,
            Ferguson,J.F., He,J., Young,T., Mosley,T.H., Smith,J.A., Kral,B.G.,
            Guo,X., Wong,Q., Ganesh,S.K., Heckbert,S.R., Griswold,M.E.,
            O'Leary,D.H., Budoff,M., Carr,J.J., Taylor,H.A. Jr., Bluemke,D.A.,
            Demissie,S., Hwang,S.J., Paltoo,D.N., Polak,J.F., Psaty,B.M.,
            Becker,D.M., Province,M.A., Post,W.S., O'Donnell,C.J., Wilson,J.G.,
            Harris,T.B., Kavousi,M., Cupples,L.A., Rotter,J.I., Fornage,M.,
            Becker,L.C., Peyser,P.A., Borecki,I.B. and Reilly,M.P.
  TITLE     Genetics of coronary artery calcification among African Americans,
            a meta-analysis
  JOURNAL   BMC Med Genet 14, 75 (2013)
   PUBMED   23870195
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 689)
  AUTHORS   Greninger,A.L., Knudsen,G.M., Betegon,M., Burlingame,A.L. and
            DeRisi,J.L.
  TITLE     ACBD3 interaction with TBC1 domain 22 protein is differentially
            affected by enteroviral and kobuviral 3A protein binding
  JOURNAL   mBio 4 (2), e00098-e00013 (2013)
   PUBMED   23572552
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 689)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DR002231.1, AW936405.1, DA311439.1, DT932690.1, DA020448.1,
            AK023176.1 and AK097972.1.
            
            On Aug 1, 2007 this sequence version replaced NP_078817.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.266502.1,
                                           SRR1803615.209554.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370033.9/ ENSP00000359050.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..689
                     /product="armadillo-like helical domain-containing protein
                     3"
                     /note="UPF0668 protein C10orf76; distal Golgi armadillo
                     repeat protein"
                     /calculated_mol_wt=78580
     Region          441..669
                     /region_name="ARMH3_C"
                     /note="Armadillo-like helical domain-containing protein 3,
                     C-terminal; pfam08427"
                     /db_xref="CDD:462473"
     Site            520..538
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T2E6.1)"
     CDS             1..689
                     /gene="ARMH3"
                     /gene_synonym="C10orf76; DGARM"
                     /coded_by="NM_024541.3:101..2170"
                     /db_xref="CCDS:CCDS41563.1"
                     /db_xref="GeneID:79591"
                     /db_xref="HGNC:HGNC:25788"
                     /db_xref="MIM:620867"
ORIGIN      
        1 maqvekrggl lrkssaskkp lkekvvlmyd eifmtedpsk csprfweelf lmkvnleyle
       61 gklesldgee lmkikdninc lfqhciqalg eehpirvvna lqtlcalirg vhqknkstsg
      121 fdiinmlmgf dkaelcmknl mesldsllca egseslkslc lklllclvtv tdnisqntil
      181 eyvminsife ailqilshpp srrehgydav vllallvnyr kyesvnpyiv klsivddeat
      241 lngmglviaq alseynrqyk dkeeehqsgf fsaltnmvgs mfiadaheki svqtneaill
      301 alyeavhlnr nfitvlaqsh pemglvttpv spapttpvtp lgttppssdv issvelplda
      361 dvqtsnllit flkyssivmq dtkdehrlhs gklcliiltc iaedqyanaf lhddnmnfrv
      421 nlhrmpmrhr kkaadknlpc rplvcavldl mvefivthmm kefpmdlyir ciqvvhkllc
      481 yqkkcrvrlh ytwrelwsal inllkflmsn etvllakhni ftlalmivnl fnmfitygdt
      541 flptpssyde lyyeiirmhq sfdnlysmvl rlstnagqwk eaaskvthal vniraiinhf
      601 npkiesyaav nhisqlseeq vlevvranyd tltlklqdgl dqyeryseqh keaaffkelv
      661 rsistnvrrn lafhtlsqev llkefstis
//
LOCUS       NP_899006                763 aa            linear   ROD 27-APR-2025
DEFINITION  G protein-regulated inducer of neurite outgrowth 3 [Mus musculus].
ACCESSION   NP_899006
VERSION     NP_899006.1
DBSOURCE    REFSEQ: accession NM_183183.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Karadurmus,D., Rial,D., De Backer,J.F., Communi,D., de Kerchove
            d'Exaerde,A. and Schiffmann,S.N.
  TITLE     GPRIN3 Controls Neuronal Excitability, Morphology, and
            Striatal-Dependent Behaviors in the Indirect Pathway of the
            Striatum
  JOURNAL   J Neurosci 39 (38), 7513-7528 (2019)
   PUBMED   31363062
  REMARK    GeneRIF: we identified GPRIN3 as a putative selective controller of
            D2R function in the striatum playing a critical role in
            striatal-associated behaviors and cellular functions
REFERENCE   2  (residues 1 to 763)
  AUTHORS   Jones,M.R., Dilai,S., Lingampally,A., Chao,C.M., Danopoulos,S.,
            Carraro,G., Mukhametshina,R., Wilhelm,J., Baumgart-Vogt,E., Al
            Alam,D., Chen,C., Minoo,P., Zhang,J.S. and Bellusci,S.
  TITLE     A Comprehensive Analysis of Fibroblast Growth Factor Receptor 2b
            Signaling on Epithelial Tip Progenitor Cells During Early Mouse
            Lung Branching Morphogenesis
  JOURNAL   Front Genet 9, 746 (2019)
   PUBMED   30728831
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 763)
  AUTHORS   Mototani,Y., Okamura,T., Goto,M., Shimizu,Y., Yanobu-Takanashi,R.,
            Ito,A., Kawamura,N., Yagisawa,Y., Umeki,D., Nariyama,M., Suita,K.,
            Ohnuki,Y., Shiozawa,K., Sahara,Y., Kozasa,T., Saeki,Y. and
            Okumura,S.
  TITLE     Role of G protein-regulated inducer of neurite outgrowth 3 (GRIN3)
            in beta-arrestin 2-Akt signaling and dopaminergic behaviors
  JOURNAL   Pflugers Arch 470 (6), 937-947 (2018)
   PUBMED   29500670
  REMARK    GeneRIF: GRIN3 is involved in regulation of dopamine-dependent
            behaviors and is essential for activation of the dopamine receptors
            (DAR)-beta-arrestin signaling cascade.
REFERENCE   4  (residues 1 to 763)
  AUTHORS   Collins,M.O., Yu,L., Coba,M.P., Husi,H., Campuzano,I.,
            Blackstock,W.P., Choudhary,J.S. and Grant,S.G.
  TITLE     Proteomic analysis of in vivo phosphorylated synaptic proteins
  JOURNAL   J Biol Chem 280 (7), 5972-5982 (2005)
   PUBMED   15572359
REFERENCE   5  (residues 1 to 763)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   6  (residues 1 to 763)
  AUTHORS   Iida,N. and Kozasa,T.
  TITLE     Identification and biochemical analysis of GRIN1 and GRIN2
  JOURNAL   Methods Enzymol 390, 475-483 (2004)
   PUBMED   15488195
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131708.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK050148.1, AK173336.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 28.48 cM"
     Protein         1..763
                     /product="G protein-regulated inducer of neurite outgrowth
                     3"
                     /note="GRIN3"
                     /calculated_mol_wt=80354
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BWS5.1)"
     Region          65..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BWS5.1)"
     Region          192..268
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BWS5.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BWS5.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BWS5.1)"
     Region          420..452
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BWS5.1)"
     Region          471..624
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BWS5.1)"
     Region          <479..>623
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          638..758
                     /region_name="GRIN_C"
                     /note="G protein-regulated inducer of neurite outgrowth
                     C-terminus; pfam15235"
                     /db_xref="CDD:464577"
     Region          711..737
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BWS5.1)"
     CDS             1..763
                     /gene="Gprin3"
                     /gene_synonym="C030038J10Rik; C730021L23"
                     /coded_by="NM_183183.3:257..2548"
                     /db_xref="CCDS:CCDS20199.1"
                     /db_xref="GeneID:243385"
                     /db_xref="MGI:MGI:1924785"
ORIGIN      
        1 mgtvpdplrv tkasivaasg keesrgesqs vspqpaqpdn nasgignvpa elslqlsaaa
       61 qalmqacvse ssqqdmaspg vfsegepvsp kqktpddfll hgskesaapg lnataqkeli
      121 sapclisvvq hthhaiqrda pntstcavpe gslvkseans ngenpekpgc parvtccssk
      181 nqeglcdfps pensqgilqt pdiaspsadr pegegqkvin nitavssepp vregcsenkq
      241 psatalntta ersenpppsh ltskgatcss earqallpaq ypvsrfkeas tmtcqaesga
      301 kevsgrawqd aevqavasve srsvstspsi lpaylkenpa pelengqeql rvichgkgsg
      361 nhllelsnsm vdsqesrqcp sivpqvhiqa atatpaafkg gckpanqpae glksplihvt
      421 ssqnteteed lrlsaskeat srqpegtnpd fqkanaigqi slpagsqaei nqglwnsgpr
      481 epeivvktak dhkaessckp snsgggankd yppesldptd kkgakdkkpa splivkdhap
      541 gatstldakt lllnpksqvk egegpevspa pspgrksqqn tleelrqpkt vmslslpsdg
      601 tgdsspgsgk rtpslsvkas prrgsrvsef lkelsvtaaa aqvgltpgek kkqlgadskl
      661 hlkqskrvrd vvwddqgmtw evygasldpe slgvaiqnhl qrqireheki vktqsgqtrr
      721 sissdssssk klkgrqhgvl qsmlqnfrrp nccvrpapss vld
//
LOCUS       NP_001351152             337 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 410 isoform 4 [Mus musculus].
ACCESSION   NP_001351152 XP_017170624
VERSION     NP_001351152.1
DBSOURCE    REFSEQ: accession NM_001364223.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Vinjamur,D.S., Yao,Q., Cole,M.A., McGuckin,C., Ren,C., Zeng,J.,
            Hossain,M., Luk,K., Wolfe,S.A., Pinello,L. and Bauer,D.E.
  TITLE     ZNF410 represses fetal globin by singular control of CHD4
  JOURNAL   Nat Genet 53 (5), 719-728 (2021)
   PUBMED   33859416
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Campbell,G.R., Baudhuin,A., Vranizan,K. and Ngai,J.
  TITLE     Transcription factors expressed in olfactory bulb local progenitor
            cells revealed by genome-wide transcriptome profiling
  JOURNAL   Mol Cell Neurosci 46 (2), 548-561 (2011)
   PUBMED   21194568
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Guo,G., Huss,M., Tong,G.Q., Wang,C., Li Sun,L., Clarke,N.D. and
            Robson,P.
  TITLE     Resolution of cell fate decisions revealed by single-cell gene
            expression analysis from zygote to blastocyst
  JOURNAL   Dev Cell 18 (4), 675-685 (2010)
   PUBMED   20412781
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Pritsker,M., Doniger,T.T., Kramer,L.C., Westcot,S.E. and
            Lemischka,I.R.
  TITLE     Diversification of stem cell molecular repertoire by alternative
            splicing
  JOURNAL   Proc Natl Acad Sci U S A 102 (40), 14290-14295 (2005)
   PUBMED   16183747
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Benanti,J.A., Williams,D.K., Robinson,K.L., Ozer,H.L. and
            Galloway,D.A.
  TITLE     Induction of extracellular matrix-remodeling genes by the
            senescence-associated protein APA-1
  JOURNAL   Mol Cell Biol 22 (21), 7385-7397 (2002)
   PUBMED   12370286
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC159649.3.
            
            On Jun 12, 2018 this sequence version replaced XP_017170624.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660815.115471.1,
                                           SRR17253012.3526635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849383
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 39.15 cM"
     Protein         1..337
                     /product="zinc finger protein 410 isoform 4"
                     /note="another partner for ARF 1; zinc finger protein
                     APA-1"
                     /calculated_mol_wt=36203
     Region          198..220
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          200..220
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..337
                     /gene="Zfp410"
                     /gene_synonym="Apa1; D12Ertd748e; Znf410"
                     /coded_by="NM_001364223.1:335..1348"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:52708"
                     /db_xref="MGI:MGI:1289280"
ORIGIN      
        1 mlsdeleskp ellvqfvqnt siplgqglve seakditcls llpvteasec srlmlpdetp
       61 nhansskevp ssavlrslqv nvgpdgeetr aqtvqkspef lttpespsll qdlqpsdsts
      121 fillnltrag lgssaehfvf vqdetedsga dflsaestds sipwflrvqe lahdsliaat
      181 raqlaknakt gsngekphqc qvcgktfsqs gsrnvhmrkh hlqlgttgsq eqdqtaeplm
      241 gsslledasv pnknlvsmns qsslggesln lsntnsilgv ddevlteras rplssvpdvt
      301 hhlvtmqsgr qsyevsvlta vnpqellnqg dlterqt
//
LOCUS       NP_036414                142 aa            linear   PRI 27-APR-2025
DEFINITION  potassium voltage-gated channel subfamily E regulatory beta subunit
            5 [Homo sapiens].
ACCESSION   NP_036414
VERSION     NP_036414.1
DBSOURCE    REFSEQ: accession NM_012282.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Lin,Y., Huang,J., He,S., Feng,R., Zhong,Z., Liu,Y., Ye,W., Li,X.,
            Liao,H., Fei,H., Rao,F., Shan,Z., Deng,C., Zhan,X., Xue,Y., Liu,H.,
            Zhang,B., Wang,K., Zhang,Q., Wu,S. and Lin,X.
  TITLE     Case report of familial sudden cardiac death caused by a DSG2
            p.F531C mutation as genetic background when carrying with
            heterozygous KCNE5 p.D92E/E93X mutation
  JOURNAL   BMC Med Genet 19 (1), 148 (2018)
   PUBMED   30129429
  REMARK    GeneRIF: Carriers of DSG2p.F531C showed various phenotypes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Abbott,G.W.
  TITLE     KCNE4 and KCNE5: K(+) channel regulation and cardiac
            arrhythmogenesis
  JOURNAL   Gene 593 (2), 249-260 (2016)
   PUBMED   27484720
  REMARK    Review article
REFERENCE   4  (residues 1 to 142)
  AUTHORS   David,J.P., Stas,J.I., Schmitt,N. and Bocksteins,E.
  TITLE     Auxiliary KCNE subunits modulate both homotetrameric Kv2.1 and
            heterotetrameric Kv2.1/Kv6.4 channels
  JOURNAL   Sci Rep 5, 12813 (2015)
   PUBMED   26242757
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Palmer,B.R., Frampton,C.M., Skelton,L., Yandle,T.G., Doughty,R.N.,
            Whalley,G.A., Ellis,C.J., Troughton,R.W., Richards,A.M. and
            Cameron,V.A.
  TITLE     KCNE5 polymorphism rs697829 is associated with QT interval and
            survival in acute coronary syndromes patients
  JOURNAL   J Cardiovasc Electrophysiol 23 (3), 319-324 (2012)
   PUBMED   21985337
  REMARK    GeneRIF: common single nucleotide polymorphism (SNP) from KCNE5,
            and ECG measurements and survival in postacute acute coronary
            syndrome patients
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Yang,Y., Xia,M., Jin,Q., Bendahhou,S., Shi,J., Chen,Y., Liang,B.,
            Lin,J., Liu,Y., Liu,B., Zhou,Q., Zhang,D., Wang,R., Ma,N., Su,X.,
            Niu,K., Pei,Y., Xu,W., Chen,Z., Wan,H., Cui,J., Barhanin,J. and
            Chen,Y.
  TITLE     Identification of a KCNE2 gain-of-function mutation in patients
            with familial atrial fibrillation
  JOURNAL   Am J Hum Genet 75 (5), 899-905 (2004)
   PUBMED   15368194
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Hofman-Bang,J., Jespersen,T., Grunnet,M., Larsen,L.A.,
            Andersen,P.S., Kanters,J.K., Kjeldsen,K. and Christiansen,M.
  TITLE     Does KCNE5 play a role in long QT syndrome?
  JOURNAL   Clin Chim Acta 345 (1-2), 49-53 (2004)
   PUBMED   15193977
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Angelo,K., Jespersen,T., Grunnet,M., Nielsen,M.S., Klaerke,D.A. and
            Olesen,S.P.
  TITLE     KCNE5 induces time- and voltage-dependent modulation of the KCNQ1
            current
  JOURNAL   Biophys J 83 (4), 1997-2006 (2002)
   PUBMED   12324418
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Piccini,M., Vitelli,F., Seri,M., Galietta,L.J., Moran,O.,
            Bulfone,A., Banfi,S., Pober,B. and Renieri,A.
  TITLE     KCNE1-like gene is deleted in AMME contiguous gene syndrome:
            identification and characterization of the human and mouse homologs
  JOURNAL   Genomics 60 (3), 251-257 (1999)
   PUBMED   10493825
REFERENCE   10 (residues 1 to 142)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL118496.22, AK314923.1 and
            BC035330.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of a family of single pass
            transmembrane domain proteins that function as ancillary subunits
            to voltage-gated potassium channels. Members of this family affect
            diverse processes in potassium channel regulation, including ion
            selectivity, voltage dependence, and anterograde recycling from the
            plasma membrane. Variants of this gene are associated with
            idiopathic ventricular fibrillation and Brugada syndrome. [provided
            by RefSeq, Nov 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR3476690.1123102.1, AK223306.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372101.3/ ENSP00000361173.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq23"
     Protein         1..142
                     /product="potassium voltage-gated channel subfamily E
                     regulatory beta subunit 5"
                     /note="potassium voltage-gated channel, Isk-related
                     family, member 1-like; AMMECR2 protein; KCNE1-like;
                     potassium channel subunit beta MiRP4; potassium
                     voltage-gated channel subfamily E member 1-like protein;
                     cardiac voltage-gated potassium channel accessory subunit
                     5; AMME syndrome candidate gene 2 protein"
                     /calculated_mol_wt=14862
     Site            2
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UJ90.1)"
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UJ90.1)"
     Region          <51..>92
                     /region_name="ISK_Channel"
                     /note="Slow voltage-gated potassium channel; pfam02060"
                     /db_xref="CDD:460432"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJ90.1)"
     Region          119..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJ90.1)"
     CDS             1..142
                     /gene="KCNE5"
                     /gene_synonym="KCNE1L"
                     /coded_by="NM_012282.4:153..581"
                     /db_xref="CCDS:CCDS14547.1"
                     /db_xref="GeneID:23630"
                     /db_xref="HGNC:HGNC:6241"
                     /db_xref="MIM:300328"
ORIGIN      
        1 mncsesqrlr tllsrlllel hhrgnasglg agprpsmgmg vvpdpfvgre vtsakgdday
       61 lyillimify aclagglila ytrsrklvea kdepsqacae hewapggalt adaeaaagsq
      121 aegrrqlase glpalaqgae rv
//
LOCUS       NP_006124               1042 aa            linear   PRI 27-APR-2025
DEFINITION  diacylglycerol lipase-alpha [Homo sapiens].
ACCESSION   NP_006124
VERSION     NP_006124.1
DBSOURCE    REFSEQ: accession NM_006133.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Yan,Y.C., Meng,G.X., Yang,C.C., Yang,Y.F., Tan,S.Y., Yan,L.J.,
            Ding,Z.N., Ma,Y.L., Dong,Z.R. and Li,T.
  TITLE     Diacylglycerol lipase alpha promotes hepatocellular carcinoma
            progression and induces lenvatinib resistance by enhancing YAP
            activity
  JOURNAL   Cell Death Dis 14 (7), 404 (2023)
   PUBMED   37414748
  REMARK    GeneRIF: Diacylglycerol lipase alpha promotes hepatocellular
            carcinoma progression and induces lenvatinib resistance by
            enhancing YAP activity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Okubo,Y., Kasamatsu,A., Yamatoji,M., Fushimi,K., Ishigami,T.,
            Shimizu,T., Kasama,H., Shiiba,M., Tanzawa,H. and Uzawa,K.
  TITLE     Diacylglycerol lipase alpha promotes tumorigenesis in oral cancer
            by cell-cycle progression
  JOURNAL   Exp Cell Res 367 (1), 112-118 (2018)
   PUBMED   29614312
  REMARK    GeneRIF: Overexpression of DAGLA in human oral squamous cell
            carcinomas cells controlled cell proliferation through cell-cycle
            progression.
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Ishiguro,H., Higuchi,S., Arinami,T. and Onaivi,E.S.
  TITLE     Association between alcoholism and the gene encoding the
            endocannabinoid synthesizing enzyme diacylglycerol lipase alpha in
            the Japanese population
  JOURNAL   Alcohol 68, 59-62 (2018)
   PUBMED   29477030
  REMARK    GeneRIF: Our findings indicated the involvement of DAGLA in
            alcoholism, possibly by its genetic dysfunction and also by the
            influence of stress
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Smith,D.R., Stanley,C.M., Foss,T., Boles,R.G. and McKernan,K.
  TITLE     Rare genetic variants in the endocannabinoid system genes CNR1 and
            DAGLA are associated with neurological phenotypes in humans
  JOURNAL   PLoS One 12 (11), e0187926 (2017)
   PUBMED   29145497
  REMARK    GeneRIF: phenotypes associated with rare CNR1 variants are
            reminiscent of those implicated in the theory of clinical
            endocannabinoid deficiency syndrome. The severe phenotypes
            associated with rare DAGLA variants underscore the critical role of
            rapid 2-AG synthesis and the endocannabinoid system in regulating
            neurological function and development
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Pankratz,V.S., Haralambieva,I.H.,
            Vierkant,R.A. and Poland,G.A.
  TITLE     Genome-wide analysis of polymorphisms associated with cytokine
            responses in smallpox vaccine recipients
  JOURNAL   Hum Genet 131 (9), 1403-1421 (2012)
   PUBMED   22610502
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   Lemaitre,R.N., Tanaka,T., Tang,W., Manichaikul,A., Foy,M.,
            Kabagambe,E.K., Nettleton,J.A., King,I.B., Weng,L.C.,
            Bhattacharya,S., Bandinelli,S., Bis,J.C., Rich,S.S., Jacobs,D.R.
            Jr., Cherubini,A., McKnight,B., Liang,S., Gu,X., Rice,K.,
            Laurie,C.C., Lumley,T., Browning,B.L., Psaty,B.M., Chen,Y.D.,
            Friedlander,Y., Djousse,L., Wu,J.H., Siscovick,D.S.,
            Uitterlinden,A.G., Arnett,D.K., Ferrucci,L., Fornage,M., Tsai,M.Y.,
            Mozaffarian,D. and Steffen,L.M.
  TITLE     Genetic loci associated with plasma phospholipid n-3 fatty acids: a
            meta-analysis of genome-wide association studies from the CHARGE
            Consortium
  JOURNAL   PLoS Genet 7 (7), e1002193 (2011)
   PUBMED   21829377
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Knight,M.A., Hernandez,D., Diede,S.J., Dauwerse,H.G., Rafferty,I.,
            van de Leemput,J., Forrest,S.M., Gardner,R.J., Storey,E., van
            Ommen,G.J., Tapscott,S.J., Fischbeck,K.H. and Singleton,A.B.
  TITLE     A duplication at chromosome 11q12.2-11q12.3 is associated with
            spinocerebellar ataxia type 20
  JOURNAL   Hum Mol Genet 17 (24), 3847-3853 (2008)
   PUBMED   18801880
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   Jung,K.M., Mangieri,R., Stapleton,C., Kim,J., Fegley,D.,
            Wallace,M., Mackie,K. and Piomelli,D.
  TITLE     Stimulation of endocannabinoid formation in brain slice cultures
            through activation of group I metabotropic glutamate receptors
  JOURNAL   Mol Pharmacol 68 (5), 1196-1202 (2005)
   PUBMED   16051747
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Bisogno,T., Howell,F., Williams,G., Minassi,A., Cascio,M.G.,
            Ligresti,A., Matias,I., Schiano-Moriello,A., Paul,P.,
            Williams,E.J., Gangadharan,U., Hobbs,C., Di Marzo,V. and Doherty,P.
  TITLE     Cloning of the first sn1-DAG lipases points to the spatial and
            temporal regulation of endocannabinoid signaling in the brain
  JOURNAL   J Cell Biol 163 (3), 463-468 (2003)
   PUBMED   14610053
  REMARK    GeneRIF: This gene was functionally characterized as a
            diacylglycerol-lipase (DAGL), specifically referred to as DAGL
            alpha.  This enzyme may play a role in the biosynthesis of the
            endocannbinoid 2-arachidonoylglycerol (2-AG).
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002380.3 and BC150176.1.
            
            Summary: This gene encodes a diacylglycerol lipase. The encoded
            enzyme is involved in the biosynthesis of the endocannabinoid
            2-arachidonoyl-glycerol.[provided by RefSeq, Nov 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150176.1, BC152453.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257215.10/ ENSP00000257215.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.2"
     Protein         1..1042
                     /product="diacylglycerol lipase-alpha"
                     /EC_number="3.1.1.116"
                     /note="neural stem cell-derived dendrite regulator;
                     sn1-specific diacylglycerol lipase alpha; DGL-alpha;
                     DAGL-alpha"
                     /calculated_mol_wt=114821
     Site            23..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            102..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Region          288..529
                     /region_name="Lipase_3"
                     /note="Lipase (class 3). Lipases are esterases that can
                     hydrolyze long-chain acyl-triglycerides into di- and
                     monoglycerides, glycerol, and free fatty acids at a
                     water/lipid interface. A typical feature of lipases is
                     'interfacial activation,' the process of...; cd00519"
                     /db_xref="CDD:238287"
     Site            order(400..401,403..411)
                     /site_type="active"
                     /note="active site flap/lid [active]"
                     /db_xref="CDD:238287"
     Site            470..474
                     /site_type="active"
                     /note="nucleophilic elbow [active]"
                     /db_xref="CDD:238287"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5YLM1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WQJ1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WQJ1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            743
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WQJ1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            782
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23502535; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            784
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WQJ1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            806
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5YLM1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23502535; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5YLM1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Region          846..903
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            847
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5YLM1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            952
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WQJ1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Region          1014..1042
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     Site            1023
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6WQJ1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4D2.3)"
     CDS             1..1042
                     /gene="DAGLA"
                     /gene_synonym="C11orf11; DAGL(ALPHA); DAGLALPHA; NOC2;
                     NSDDR"
                     /coded_by="NM_006133.3:159..3287"
                     /db_xref="CCDS:CCDS31578.1"
                     /db_xref="GeneID:747"
                     /db_xref="HGNC:HGNC:1165"
                     /db_xref="MIM:614015"
ORIGIN      
        1 mpgivvfrrr wsvgsddlvl paiflfllht twfvilsvvl fglvynphea cslnlvdhgr
       61 gylgillscm iaemaiiwls mrggilytep rdsmqyvlyv rlailviefi yaivgivwlt
      121 qyytscndlt aknvtlgmvv cnwvvilsvc itvlcvfdpt grtfvklrat krrqrnlrty
      181 nlrhrleegq atswsrrlkv flcctrtkds qsdayseiay lfaeffrdld ivpsdiiagl
      241 vllrqrqrak rnavldeann dilaflsgmp vtrntkyldl knsqemlryk evcyymlfal
      301 aaygwpmylm rkpacglcql arscscclcp arprfapgvt ieednccgcn aiairrhfld
      361 enmtavdivy tschdavyet pfyvavdhdk kkvvisirgt lspkdaltdl tgdaerlpve
      421 ghhgtwlghk gmvlsaeyik kkleqemvls qafgrdlgrg tkhyglivvg hslgagtaai
      481 lsfllrpqyp tlkcfayspp ggllsedame yskefvtavv lgkdlvprig lsqlegfrrq
      541 lldvlqrstk pkwriivgat kcipkselpe evevttlast rlwthpsdlt ialsastply
      601 ppgriihvvh nhpaeqcccc eqeeptyfai wgdnkafnev iispamlheh lpyvvmegln
      661 kvlenynkgk tallsaakvm vsptevdltp elifqqqplp tgppmptgla lelptadhrn
      721 ssvrsksqse mslegfsegr llspvvaaaa rqdpvellll stqerlaael qarraplatm
      781 eslsdtesly sfdsrrssgf rsirgspslh avlerdeghl fyidpaipee npslssrtel
      841 laadslskhs qdtqpleaal gsggvtperp psaaandeee evggggggpa srgelalhng
      901 rlgdspspqv lefaefidsl fnldsksssf qdlycmvvpe sptsdyaegp kspsqqeill
      961 raqfepnlvp kpprlfagsa dpssgislsp sfplsssgel mdltptglss qeclaadkir
     1021 tstptghgas pakqdelvis ar
//
LOCUS       NP_009049               3097 aa            linear   PRI 27-APR-2025
DEFINITION  triple functional domain protein [Homo sapiens].
ACCESSION   NP_009049 XP_001720119 XP_001721635 XP_001723981
VERSION     NP_009049.2
DBSOURCE    REFSEQ: accession NM_007118.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3097)
  AUTHORS   Rao,S., Sadybekov,A., DeWitt,D.C., Lipka,J., Katritch,V. and
            Herring,B.E.
  TITLE     Detection of autism spectrum disorder-related pathogenic trio
            variants by a novel structure-based approach
  JOURNAL   Mol Autism 15 (1), 12 (2024)
   PUBMED   38566250
  REMARK    GeneRIF: Detection of autism spectrum disorder-related pathogenic
            trio variants by a novel structure-based approach.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 3097)
  AUTHORS   Bonnet,M., Roche,F., Fagotto-Kaufmann,C., Gazdagh,G., Truong,I.,
            Comunale,F., Barbosa,S., Bonhomme,M., Nafati,N., Hunt,D.,
            Rodriguez,M.P., Chaudhry,A., Shears,D., Madruga,M., Vansenne,F.,
            Curie,A., Kajava,A.V., Baralle,D., Fassier,C., Debant,A. and
            Schmidt,S.
  TITLE     Pathogenic TRIO variants associated with neurodevelopmental
            disorders perturb the molecular regulation of TRIO and axon
            pathfinding in vivo
  JOURNAL   Mol Psychiatry 28 (4), 1527-1544 (2023)
   PUBMED   36717740
  REMARK    GeneRIF: Pathogenic TRIO variants associated with
            neurodevelopmental disorders perturb the molecular regulation of
            TRIO and axon pathfinding in vivo.
REFERENCE   3  (residues 1 to 3097)
  AUTHORS   Bircher,J.E., Corcoran,E.E., Lam,T.T., Trnka,M.J. and Koleske,A.J.
  TITLE     Autoinhibition of the GEF activity of cytoskeletal regulatory
            protein Trio is disrupted in neurodevelopmental disorder-related
            genetic variants
  JOURNAL   J Biol Chem 298 (9), 102361 (2022)
   PUBMED   35963430
  REMARK    GeneRIF: Autoinhibition of the GEF activity of cytoskeletal
            regulatory protein Trio is disrupted in neurodevelopmental
            disorder-related genetic variants.
REFERENCE   4  (residues 1 to 3097)
  AUTHORS   Bandekar,S.J., Chen,C.L., Ravala,S.K., Cash,J.N., Avramova,L.V.,
            Zhalnina,M.V., Gutkind,J.S., Li,S. and Tesmer,J.J.G.
  TITLE     Structural/functional studies of Trio provide insights into its
            configuration and show that conserved linker elements enhance its
            activity for Rac1
  JOURNAL   J Biol Chem 298 (8), 102209 (2022)
   PUBMED   35779635
  REMARK    GeneRIF: Structural/functional studies of Trio provide insights
            into its configuration and show that conserved linker elements
            enhance its activity for Rac1.
REFERENCE   5  (residues 1 to 3097)
  AUTHORS   Wang,J., Yuan,L., Xu,X., Zhang,Z., Ma,Y., Hong,L. and Ma,J.
  TITLE     Rho-GEF Trio regulates osteosarcoma progression and osteogenic
            differentiation through Rac1 and RhoA
  JOURNAL   Cell Death Dis 12 (12), 1148 (2021)
   PUBMED   34893584
  REMARK    GeneRIF: Rho-GEF Trio regulates osteosarcoma progression and
            osteogenic differentiation through Rac1 and RhoA.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 3097)
  AUTHORS   Seipel,K., Medley,Q.G., Kedersha,N.L., Zhang,X.A., O'Brien,S.P.,
            Serra-Pages,C., Hemler,M.E. and Streuli,M.
  TITLE     Trio amino-terminal guanine nucleotide exchange factor domain
            expression promotes actin cytoskeleton reorganization, cell
            migration and anchorage-independent cell growth
  JOURNAL   J Cell Sci 112 (Pt 12), 1825-1834 (1999)
   PUBMED   10341202
REFERENCE   7  (residues 1 to 3097)
  AUTHORS   Liu,X., Wang,H., Eberstadt,M., Schnuchel,A., Olejniczak,E.T.,
            Meadows,R.P., Schkeryantz,J.M., Janowick,D.A., Harlan,J.E.,
            Harris,E.A., Staunton,D.E. and Fesik,S.W.
  TITLE     NMR structure and mutagenesis of the N-terminal Dbl homology domain
            of the nucleotide exchange factor Trio
  JOURNAL   Cell 95 (2), 269-277 (1998)
   PUBMED   9790533
REFERENCE   8  (residues 1 to 3097)
  AUTHORS   Taviaux,S., Diriong,S., Bellanger,J.M., Streuli,M. and Debant,A.
  TITLE     Assignment of TRIO, the Trio gene (PTPRF interacting) to human
            chromosome bands 5p 15.1-->p 14 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 76 (1-2), 107-108 (1997)
   PUBMED   9154137
REFERENCE   9  (residues 1 to 3097)
  AUTHORS   Debant,A., Serra-Pages,C., Seipel,K., O'Brien,S., Tang,M.,
            Park,S.H. and Streuli,M.
  TITLE     The multidomain protein Trio binds the LAR transmembrane tyrosine
            phosphatase, contains a protein kinase domain, and has separate
            rac-specific and rho-specific guanine nucleotide exchange factor
            domains
  JOURNAL   Proc Natl Acad Sci U S A 93 (11), 5466-5471 (1996)
   PUBMED   8643598
REFERENCE   10 (residues 1 to 3097)
  AUTHORS   Varvagiannis,K., Vissers,L.E.L.M., Baralle,D., de Vries,B.B.A. and
            Gazdagh,G.
  TITLE     TRIO-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28796471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010419.6, BF058117.1,
            BC035585.1, U42390.1, AI478154.1, BQ691537.1, AF091395.1,
            BC017268.2, AK131423.1 and BQ184284.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jun 11, 2008 this sequence version replaced
            XP_001720119.1, XP_001723981.1, XP_001721635.1, NP_009049.1.
            
            Summary: This gene encodes a large protein that functions as a GDP
            to GTP exchange factor. This protein promotes the reorganization of
            the actin cytoskeleton, thereby playing a role in cell migration
            and growth. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF091395.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344204.9/ ENSP00000339299.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3097
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..3097
                     /product="triple functional domain protein"
                     /EC_number="2.7.11.1"
                     /note="PTPRF-interacting protein; triple functional domain
                     (PTPRF interacting)"
                     /calculated_mol_wt=346771
     Region          69..204
                     /region_name="SEC14"
                     /note="Domain in homologues of a S. cerevisiae
                     phosphatidylinositol transfer protein (Sec14p);
                     smart00516"
                     /db_xref="CDD:214706"
     Region          230..445
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          311..418
                     /region_name="Spectrin 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75962.2)"
     Site            339..344
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          341..566
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            447..452
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          538..644
                     /region_name="Spectrin 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75962.2)"
     Region          567..783
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          787..1014
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          878..984
                     /region_name="Spectrin 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75962.2)"
     Site            906..911
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          908..1137
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            1013..1018
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1109..1216
                     /region_name="Spectrin 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75962.2)"
     Region          1143..1243
                     /region_name="SPEC"
                     /note="Spectrin repeats; smart00150"
                     /db_xref="CDD:197544"
     Region          1295..1465
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(1299,1303,1398,1419..1420,1423..1424,1426..1427,
                     1430..1431,1434..1435,1438,1461,1465)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          1472..1594
                     /region_name="PH1_Kalirin_Trio_like"
                     /note="Triple functional domain pleckstrin homology
                     pleckstrin homology (PH) domain, repeat 1; cd13240"
                     /db_xref="CDD:270060"
     Site            order(1489,1529,1531)
                     /site_type="other"
                     /note="Rac1 binding site [polypeptide binding]"
                     /db_xref="CDD:270060"
     Region          1601..1650
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75962.2)"
     Site            1627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q0KL02; propagated from
                     UniProtKB/Swiss-Prot (O75962.2)"
     Site            1632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F1M0Z1; propagated from
                     UniProtKB/Swiss-Prot (O75962.2)"
     Site            1633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F1M0Z1; propagated from
                     UniProtKB/Swiss-Prot (O75962.2)"
     Region          1659..1718
                     /region_name="SH3_Kalirin_1"
                     /note="First Src homology 3 domain of the RhoGEF kinase,
                     Kalirin; cd11852"
                     /db_xref="CDD:212786"
     Site            order(1665,1667,1670,1674,1694..1695,1712,1714..1715)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212786"
     Region          1715..1972
                     /region_name="SH3-RhoG_link"
                     /note="SH3-RhoGEF linking unstructured region; pfam16609"
                     /db_xref="CDD:465196"
     Region          1779..1906
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75962.2)"
     Site            1824
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:F1M0Z1; propagated from
                     UniProtKB/Swiss-Prot (O75962.2)"
     Region          1927..1965
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75962.2)"
     Region          1970..2143
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(1976,1980,2073,2094..2095,2098..2099,2101..2102,
                     2105..2106,2109..2110,2113,2139,2143)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          2148..2286
                     /region_name="PH2_Kalirin_Trio_p63RhoGEF"
                     /note="p63RhoGEF pleckstrin homology (PH) domain, repeat
                     2; cd13241"
                     /db_xref="CDD:270061"
     Site            order(2157,2192..2193,2219,2221,2273,2276..2278,
                     2280..2281,2283..2285)
                     /site_type="other"
                     /note="Galpha i/q binding site [polypeptide binding]"
                     /db_xref="CDD:270061"
     Site            2282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75962.2)"
     Region          2287..2552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75962.2)"
     Region          <2330..2540
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75962.2)"
     Site            2459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75962.2)"
     Region          2555..2613
                     /region_name="SH3_Kalirin_2"
                     /note="Second Src homology 3 domain of the RhoGEF kinase,
                     Kalirin; cd11853"
                     /db_xref="CDD:212787"
     Site            order(2560,2562,2565,2569,2587..2588,2607,2609..2610)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212787"
     Site            2631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75962.2)"
     Region          2639..2660
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75962.2)"
     Region          2685..2776
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          2702..2706
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2715..2719
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2742..2746
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2756..2761
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2769..2772
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          2788..3050
                     /region_name="STKc_Trio_C"
                     /note="C-terminal kinase domain of the Large
                     Serine/Threonine Kinase and Rho Guanine Nucleotide
                     Exchange Factor, Triple functional domain protein;
                     cd14113"
                     /db_xref="CDD:271015"
     Site            order(2802..2806,2808,2810,2823,2825,2853,2869..2870,2872,
                     2876,2878,2915,2917,2919..2920,2922,2935..2936,2939,
                     2954..2957)
                     /site_type="active"
                     /db_xref="CDD:271015"
     Site            order(2802..2806,2808,2810,2823,2825,2853,2869..2870,2872,
                     2876,2919..2920,2922,2935..2936)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271015"
     Site            order(2806,2876,2878,2915,2917,2919,2939,2954..2957)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271015"
     Site            2935..2957
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271015"
     CDS             1..3097
                     /gene="TRIO"
                     /gene_synonym="ARHGEF23; MEBAS; MRD44; MRD63; tgat"
                     /coded_by="NM_007118.4:385..9678"
                     /db_xref="CCDS:CCDS3883.1"
                     /db_xref="GeneID:7204"
                     /db_xref="HGNC:HGNC:12303"
                     /db_xref="MIM:601893"
ORIGIN      
        1 msgssggaaa paassgpaaa asaagsgcgg gagegaeeaa kdladiaaff rsgfrkndem
       61 kamdvlpilk ekvaylsggr dkrggpiltf parsnhdrir qedlrrlisy lacipseevc
      121 krgftvivdm rgskwdsikp llkilqesfp ccihvaliik pdnfwqkqrt nfgsskfefe
      181 tnmvsleglt kvvdpsqltp efdgcleynh eewieirvaf edyisnathm lsrleelqdi
      241 lakkelpqdl egarnmieeh sqlkkkvika piedldlegq kllqriqsse sfpkknsgsg
      301 nadlqnllpk vstmldrlhs trqhlhqmwh vrklkldqcf qlrlfeqdae kmfdwithnk
      361 glflnsytei gtshphamel qtqhnhfamn cmnvyvninr imsvanrlve sghyasqqir
      421 qiasqleqew kafaaalder stlldmssif hqkaekymsn vdswckacge vdlpselqdl
      481 edaihhhqgi yehitlayse vsqdgkslld klqrpltpgs sdsltasany skavhhvldv
      541 ihevlhhqrq leniwqhrkv rlhqrlqlcv fqqdvqqvld wienhgeafl skhtgvgksl
      601 hraralqkrh edfeevaqnt ytnadkllea aeqlaqtgec dpeeiyqaah qledriqdfv
      661 rrveqrkill dmsvsfhthv kelwtwleel qkellddvya esveavqdli krfgqqqqtt
      721 lqvtvnvike gedliqqlrd saissnktph nssinhietv lqqldeaqsq meelfqerki
      781 klelflqlri ferdaidiis dleswndels qqmndfdted ltiaeqrlqh hadkaltmnn
      841 ltfdvihqgq dllqyvnevq asgvellcdr dvdmatrvqd lleflhekqq eldlaaeqhr
      901 khleqcvqlr hlqaevkqvl gwirngesml naglitassl qeaeqlqreh eqfqhaiekt
      961 hqsalqvqqk aeamlqanhy dmdmirdcae kvashwqqlm lkmedrlklv nasvafykts
     1021 eqvcsvlesl eqeykreedw cggadklgpn setdhvtpmi skhleqkeaf lkactlarrn
     1081 advflkylhr nsvnmpgmvt hikapeqqvk nilnelfqre nrvlhywtmr krrldqcqqy
     1141 vvfersakqa lewihdngef ylsthtstgs siqhtqellk eheefqitak qtkervklli
     1201 qladgfcekg hahaaeikkc vtavdkryrd fslrmekyrt slekalgiss dsnksskslq
     1261 ldiipasipg sevklrdaah elneekrksa rrkefimael iqtekayvrd lrecmdtylw
     1321 emtsgveeip pgivnkelii fgnmqeiyef hnniflkele kyeqlpedvg hcfvtwadkf
     1381 qmyvtycknk pdstqlileh agsyfdeiqq rhglansiss ylikpvqrit kyqlllkell
     1441 tcceegkgei kdglevmlsv pkrandamhl smlegfdeni esqgelilqe sfqvwdpktl
     1501 irkgrerhlf lfemslvfsk evkdssgrsk ylyksklfts elgvtehveg dpckfalwvg
     1561 rtptsdnkiv lkassienkq dwikhirevi qertihlkga lkepihipkt apatrqkgrr
     1621 dgedldsqgd gssqpdtisi asrtsqntld sdklsggcel tvvihdftac nsneltirrg
     1681 qtvevlerph dkpdwclvrt tdrspaaegl vpcgslciah srssmemegi fnhkdslsvs
     1741 sndasppasv aslqphmiga qsspgpkrpg ntlrkwltsp vrrlssgkad ghvkklahkh
     1801 kksrevrksa dagsqkdsdd saatpqdetv eergrnegls sgtlskssss gmqscgeeeg
     1861 eegadavplp ppmaiqqhsl lqpdsqddka ssrllvrpts setpsaaelv saieelvksk
     1921 maledrpssl lvdqgdsssp sfnpsdnsll sssspideme erkssslkrr hyvlqelvet
     1981 erdyvrdlgy vvegymalmk edgvpddmkg kdkivfgnih qiydwhrdff lgelekcled
     2041 peklgslfvk herrlhmyia ycqnkpkseh ivseyidtff edlkqrlghr lqltdllikp
     2101 vqrimkyqll lkdflkyskk asldtseler avevmcivpr rcndmmnvgr lqgfdgkiva
     2161 qgklllqdtf lvtdqdagll prcrerrifl feqivifsep ldkkkgfsmp gflfknsikv
     2221 sclcleenve ndpckfalts rtgdvvetfi lhssspsvrq twiheinqil enqrnflnal
     2281 tspieyqrnh sgggggggsg gsgggggsgg ggapsggsgh sggpsscgga pstsrsrpsr
     2341 ipqpvrhhpp vlvssaassq aeadkmsgts tpgpslpppg aapeagpsap srrppgadae
     2401 gsereaepip kmkvlesprk gaanasgssp dapakdaras lgtlplgkpr agaasplnsp
     2461 lssavpslgk epfppssplq kggsfwssip aspasrpgsf tfpgdsdslq rqtprhaapg
     2521 kdtdrmstcs saseqsvqst qsngsessss snistmlvth dytavkedei nvyqgevvqi
     2581 lasnqqnmfl vfraatdqcp aaegwipgfv lghtsavive npdgtlkkst swhtalrlrk
     2641 ksekkdkdgk regklengyr ksreglsnkv svkllnpnyi ydvppefvip lsevtcetge
     2701 tvvlrcrvcg rpkasitwkg pehntlnndg hysisysdlg eatlkivgvt teddgiytci
     2761 avndmgsass saslrvlgpg mdgimvtwkd nfdsfyseva elgrgrfsvv kkcdqkgtkr
     2821 avatkfvnkk lmkrdqvthe lgilqslqhp llvglldtfe tptsyilvle madqgrlldc
     2881 vvrwgslteg kirahlgevl eavrylhncr iahldlkpen ilvdeslakp tikladfgda
     2941 vqlnttyyih qllgnpefaa peiilgnpvs ltsdtwsvgv ltyvllsgvs pflddsveet
     3001 clnicrldfs fpddyfkgvs qkakefvcfl lqedpakrps aalalqeqwl qagngrstgv
     3061 ldtsrltsfi errkhqndvr pirsiknflq srllprv
//
LOCUS       NP_001346471            1748 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase MRCK alpha isoform 5 [Mus
            musculus].
ACCESSION   NP_001346471 XP_006496871
VERSION     NP_001346471.1
DBSOURCE    REFSEQ: accession NM_001359542.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1748)
  AUTHORS   Bourdais,A., Dehapiot,B. and Halet,G.
  TITLE     MRCK activates mouse oocyte myosin II for spindle rotation and male
            pronucleus centration
  JOURNAL   J Cell Biol 222 (11) (2023)
   PUBMED   37651121
  REMARK    GeneRIF: MRCK activates mouse oocyte myosin II for spindle rotation
            and male pronucleus centration.
REFERENCE   2  (residues 1 to 1748)
  AUTHORS   Richard,C., Viret,S., Cantero Aguilar,L., Lefevre,C., Leduc,M.,
            Faouzi,E.H., Azar,N., Lavazec,C., Mayeux,P. and Verdier,F.
  TITLE     Myotonic dystrophy kinase-related CDC42-binding kinase alpha, a new
            transferrin receptor type 2-binding partner, is a regulator of
            erythropoiesis
  JOURNAL   Am J Hematol 96 (4), 480-492 (2021)
   PUBMED   33476437
  REMARK    GeneRIF: Myotonic dystrophy kinase-related CDC42-binding kinase
            alpha, a new transferrin receptor type 2-binding partner, is a
            regulator of erythropoiesis.
REFERENCE   3  (residues 1 to 1748)
  AUTHORS   Nakano,Y., Wiechert,S. and Banfi,B.
  TITLE     Overlapping Activities of Two Neuronal Splicing Factors Switch the
            GABA Effect from Excitatory to Inhibitory by Regulating REST
  JOURNAL   Cell Rep 27 (3), 860-871 (2019)
   PUBMED   30995482
REFERENCE   4  (residues 1 to 1748)
  AUTHORS   Dobrowolski,S.F., Lyons-Weiler,J., Spridik,K., Vockley,J.,
            Skvorak,K. and Biery,A.
  TITLE     DNA methylation in the pathophysiology of hyperphenylalaninemia in
            the PAH(enu2) mouse model of phenylketonuria
  JOURNAL   Mol Genet Metab 119 (1-2), 1-7 (2016)
   PUBMED   26822703
REFERENCE   5  (residues 1 to 1748)
  AUTHORS   Lee,I.C.J., Leung,T. and Tan,I.
  TITLE     Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related
            Cdc42-binding kinase (MRCK) regulation of LIMK1 protein in
            lamellipodial F-actin dynamics
  JOURNAL   J Biol Chem 289 (39), 26989-27003 (2014)
   PUBMED   25107909
REFERENCE   6  (residues 1 to 1748)
  AUTHORS   Osipovich,A.B., Long,Q., Manduchi,E., Gangula,R., Hipkens,S.B.,
            Schneider,J., Okubo,T., Stoeckert,C.J. Jr., Takada,S. and
            Magnuson,M.A.
  TITLE     Insm1 promotes endocrine cell differentiation by modulating the
            expression of a network of genes that includes Neurog3 and Ripply3
  JOURNAL   Development 141 (15), 2939-2949 (2014)
   PUBMED   25053427
REFERENCE   7  (residues 1 to 1748)
  AUTHORS   Gomes,E.R., Jani,S. and Gundersen,G.G.
  TITLE     Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow
            establishes MTOC polarization in migrating cells
  JOURNAL   Cell 121 (3), 451-463 (2005)
   PUBMED   15882626
REFERENCE   8  (residues 1 to 1748)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125380.4 and AC132436.3.
            
            On Jan 13, 2018 this sequence version replaced XP_006496871.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660813.399.1,
                                           SRR6116558.158251.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1748
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 84.01 cM"
     Protein         1..1748
                     /product="serine/threonine-protein kinase MRCK alpha
                     isoform 5"
                     /EC_number="2.7.11.1"
                     /note="myotonic dystrophy kinase-related CDC-42-binding
                     kinase-alpha; serine/threonine-protein kinase MRCK alpha"
                     /calculated_mol_wt=198460
     Region          4..412
                     /region_name="STKc_MRCK_alpha"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     DMPK-related cell division control protein 42 binding
                     kinase (MRCK) alpha; cd05623"
                     /db_xref="CDD:270773"
     Site            order(6..7,10..11,14..15,26,28,30..31,34..35,38,47,52..53,
                     56,59,63,69..73,76,96,101,114,142,394,397..398,400,
                     407..410)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270773"
     Site            order(83..87,91,104,106,138,154..155,157,161,163,201,203,
                     205..206,208,218..219,222,237..242,274,280,283)
                     /site_type="active"
                     /db_xref="CDD:270773"
     Site            order(83..87,91,104,106,138,155..157,161,201,203,205..206,
                     208,218..219)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270773"
     Site            order(87,161,163,201,203,205,222,237..242,274,280,283)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270773"
     Site            218..242
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270773"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            399..404
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270773"
     Region          <438..824
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            478..479
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3 in vitro.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Region          529..608
                     /region_name="KELK"
                     /note="KELK-motif containing domain of MRCK Ser/Thr
                     protein kinase; pfam15796"
                     /db_xref="CDD:464876"
     Region          881..941
                     /region_name="DMPK_coil"
                     /note="DMPK coiled coil domain like; pfam08826"
                     /db_xref="CDD:117396"
     Region          1027..1086
                     /region_name="C1_MRCKalpha"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in myotonic dystrophy kinase-related Cdc42-binding
                     kinase alpha (MRCK alpha) and similar proteins; cd20864"
                     /db_xref="CDD:410414"
     Site            order(1034..1040,1048..1052,1055)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410414"
     Region          1088..1222
                     /region_name="PH_MRCK"
                     /note="MRCK (myotonic dystrophy-related Cdc42-binding
                     kinase) pleckstrin homology (PH) domain; cd01243"
                     /db_xref="CDD:269949"
     Region          1253..1511
                     /region_name="CNH"
                     /note="CNH domain; pfam00780"
                     /db_xref="CDD:459938"
     Site            1561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Region          1608..1748
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1680
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1709
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     Site            1737
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VT25; propagated from
                     UniProtKB/Swiss-Prot (Q3UU96.2)"
     CDS             1..1748
                     /gene="Cdc42bpa"
                     /gene_synonym="A930014J19Rik; DMPK-like"
                     /coded_by="NM_001359542.1:351..5597"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS87933.1"
                     /db_xref="GeneID:226751"
                     /db_xref="MGI:MGI:2441841"
ORIGIN      
        1 msgevrlrql eqfildgpaq tngqcfsvet lldiliclyd ecnnsplrre knileylewa
       61 kpftskvkqm rlhredfeil kvigrgafge vavvklknad kvfamkilnk wemlkraeta
      121 cfreerdvlv ngdskwittl hyafqddnnl ylvmdyyvgg dlltllskfe drlpeemarf
      181 ylaemviaid svhqlhyvhr dikpdnilmd mnghirladf gsclklmedg tvqssvavgt
      241 pdyispeilq amedgkgryg pecdwwslgv cmyemlyget pfyaeslvet ygkimnhker
      301 fqfpaqvtdv senakdlirr licsrehrlg qngiedfkkh pffsgidwdn irnceapyip
      361 evssptdtsn fdvdddclkn setmppptht afsghhlpfv gftytsscvl sdrsclrvta
      421 gptsldldvs vqrtldnnla teayerrikr leqekleltr klqestqtvq alqystvdgp
      481 ltaskdleik slkeeieklr kqvaevnhle qqleeansvr relddafrqi kasekqiktl
      541 qqereelnke lvqaserlkn qskelkdahc qrklamqefm einerltelh tqkqklarhv
      601 rdkeeevdlv mqkaeslrqe lrraerakke levhtealia easkdkklre qsehyskqle
      661 neleglkqkq isyspgicsi ehqqeitklk tdlekksify eeeiskregi haseiknlkk
      721 elhdsegqql alnkeilvlk dklektrres qsereefene fkqqyerekv llteenkklt
      781 seldkltsly eslslrnqhl eeevkdladk kesvahweaq iteiiqwvsd ekdargylqa
      841 laskmteele alrnsslgtr atdmpwkmrr fakldmsarl elqsaldaei rakqaiqeel
      901 nkvkasnilt ecklkdsekk nlellseieq likdteelrs ekgiehqdsq hsflaflntp
      961 tdaldqfeds lsssssslid flddrspsct paskgrriad caplpahtpt lrkkgcpast
     1021 gfppkrkthq ffvksftapt kchqctslmv glirqgcsce vcgfschitc vnkaptvcpv
     1081 ppeqtkgplg idpqkgvgta yeghvripkp agvkkgwqra lavvcdfklf lydiaegkas
     1141 qptsvisqvi dmrdeefsvs svlasdviha srkdipcifr vtasqlsaps nkcsilmlad
     1201 senerskwvg vlselhkilk knkfrdrsvy vpkeaydstl plikttqaaa iidherialg
     1261 neeglfvvhv tkdeivrvgd nkkihqieli psdqlvavis grnrhvrlfp msaldgretd
     1321 fyklaetkgc qtiaagkvrh galsclcvam krqvlcyelf qsktrhrkfk eiqvpcnvqw
     1381 maifsehlcv gfqsgflryp lngeggpcnm lhsndhtlsf ishqpmdalc aveisnkeyl
     1441 lcfnsigiyt dcqgrrsrqq elmwpanpss ccynapylsv ysenavdifd vnsmewiqtl
     1501 plkkvrplnt egslnllgle tirliyfknk maegdelvvp etsdnsrkqm vrninnkrry
     1561 sfrvpeeerm qqrremlrdp emrnklisnp tnfnhiahmg pgdgiqilkd lpmnprpqes
     1621 rtvfsgsvsi psitksrpep grsmsassgl sarssaqngs alkrefsggs yntkrqpmps
     1681 psegslssgg mdqgsdapar dydgedsdsp rhstasnssn lssppspisp qktkslsles
     1741 tdrgswdp
//
LOCUS       NP_115669               1013 aa            linear   PRI 27-APR-2025
DEFINITION  GTPase-activating Rap/Ran-GAP domain-like protein 3 isoform a [Homo
            sapiens].
ACCESSION   NP_115669
VERSION     NP_115669.3
DBSOURCE    REFSEQ: accession NM_032293.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Luykx,J.J., Bakker,S.C., Lentjes,E., Neeleman,M., Strengman,E.,
            Mentink,L., DeYoung,J., de Jong,S., Sul,J.H., Eskin,E., van
            Eijk,K., van Setten,J., Buizer-Voskamp,J.E., Cantor,R.M., Lu,A.,
            van Amerongen,M., van Dongen,E.P., Keijzers,P., Kappen,T.,
            Borgdorff,P., Bruins,P., Derks,E.M., Kahn,R.S. and Ophoff,R.A.
  TITLE     Genome-wide association study of monoamine metabolite levels in
            human cerebrospinal fluid
  JOURNAL   Mol Psychiatry 19 (2), 228-234 (2014)
   PUBMED   23319000
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Ferreira,M.A., O'Donovan,M.C., Meng,Y.A., Jones,I.R.,
            Ruderfer,D.M., Jones,L., Fan,J., Kirov,G., Perlis,R.H., Green,E.K.,
            Smoller,J.W., Grozeva,D., Stone,J., Nikolov,I., Chambert,K.,
            Hamshere,M.L., Nimgaonkar,V.L., Moskvina,V., Thase,M.E., Caesar,S.,
            Sachs,G.S., Franklin,J., Gordon-Smith,K., Ardlie,K.G.,
            Gabriel,S.B., Fraser,C., Blumenstiel,B., Defelice,M., Breen,G.,
            Gill,M., Morris,D.W., Elkin,A., Muir,W.J., McGhee,K.A.,
            Williamson,R., MacIntyre,D.J., MacLean,A.W., St,C.D., Robinson,M.,
            Van Beck,M., Pereira,A.C., Kandaswamy,R., McQuillin,A.,
            Collier,D.A., Bass,N.J., Young,A.H., Lawrence,J., Ferrier,I.N.,
            Anjorin,A., Farmer,A., Curtis,D., Scolnick,E.M., McGuffin,P.,
            Daly,M.J., Corvin,A.P., Holmans,P.A., Blackwood,D.H., Gurling,H.M.,
            Owen,M.J., Purcell,S.M., Sklar,P. and Craddock,N.
  CONSRTM   Wellcome Trust Case Control Consortium
  TITLE     Collaborative genome-wide association analysis supports a role for
            ANK3 and CACNA1C in bipolar disorder
  JOURNAL   Nat Genet 40 (9), 1056-1058 (2008)
   PUBMED   18711365
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK293732.1, DA183830.1, BC034983.2 and AL445222.9.
            
            On Oct 1, 2008 this sequence version replaced NP_115669.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.30622.1,
                                           SRR1803616.254804.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373387.9/ ENSP00000362485.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..1013
                     /product="GTPase-activating Rap/Ran-GAP domain-like
                     protein 3 isoform a"
                     /note="GTPase activating RANGAP domain-like 3;
                     GTPase-activating Rap/Ran-GAP domain-like protein 3"
                     /calculated_mol_wt=112722
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3V0G7; propagated from
                     UniProtKB/Swiss-Prot (Q5VVW2.2)"
     Region          221..399
                     /region_name="Rap_GAP"
                     /note="Rap/ran-GAP; pfam02145"
                     /db_xref="CDD:460463"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3V0G7; propagated from
                     UniProtKB/Swiss-Prot (Q5VVW2.2)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3V0G7; propagated from
                     UniProtKB/Swiss-Prot (Q5VVW2.2)"
     Region          498..796
                     /region_name="CNH"
                     /note="CNH domain; pfam00780"
                     /db_xref="CDD:459938"
     Region          810..842
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VVW2.2)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3V0G7; propagated from
                     UniProtKB/Swiss-Prot (Q5VVW2.2)"
     Region          913..1013
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VVW2.2)"
     CDS             1..1013
                     /gene="GARNL3"
                     /gene_synonym="bA356B19.1"
                     /coded_by="NM_032293.5:105..3146"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6869.2"
                     /db_xref="GeneID:84253"
                     /db_xref="HGNC:HGNC:25425"
ORIGIN      
        1 mvvdfcrrfv arslciilmk hfcsssvsed lgcrrgdfsr khygsvelli ssdadgaiqr
       61 agrfrvengs sdenatalpg twrrtdvhle npeyhtrwyf kyflgqvhqn yigndaeksp
      121 fflsvtlsdq nnqrvpqyra ilwrktgtqk iclpysptkt lsvksilsam nldkfekgpr
      181 eifhpeiqkd llvleeqegs vnfkfgvlfa kdgqltddem fsneigsepf qkflnllgdt
      241 itlkgwtgyr ggldtkndtt gihsvytvyq gheimfhvst mlpyskenkq qverkrhign
      301 divtivfqeg eesspafkps mirshfthif alvrynqqnd nyrlkifsee svplfgpplp
      361 tppvftdhqe frdfllvkli ngekatletp tfaqkrrrtl dmlirslhqd lmpdlhknml
      421 nrrsfsdvlp espksarkke earqaefvri gqalklksiv rgdapsslaa sgickkepwe
      481 pqcfcsnfph eavcadpwgq allvstdagv llvdddlpsv pvfdrtlpvk qmhvletldl
      541 lvlradkgkd arlfvfrlsa lqkglegkqa gksrsdcren klektkgchl yainthhsre
      601 lrivvairnk lllitrkhnk psgvtstsll splsespvee fqyireicls dspmvmtlvd
      661 gpaeesdnli cvayrhqfdv vnestgeafr lhhveanrvn fvaaidvyed geaglllcyn
      721 ysciykkvcp fnggsflvqp sasdfqfcwn qapyaivcaf pyllafttds meirlvvngn
      781 lvhtavvpql qlvasrsdiy ftataavnev ssggsskgas arnspqtppg rdtpvfpssl
      841 gegeiqsknl ykiplrnlvg rsierplksp lvskvitppt pisvglaaip vthslslsrm
      901 eikeiasrtr rellglsdeg gpksegapka kskprkrlee sqggpkpgav rssssdrips
      961 gslesastse anpeghsass dqdpvadreg spvsgsspfq ltafsdedii dlk
//
LOCUS       NP_001123645             761 aa            linear   PRI 27-APR-2025
DEFINITION  transcriptional activator Myb isoform 1 [Homo sapiens].
ACCESSION   NP_001123645
VERSION     NP_001123645.1
DBSOURCE    REFSEQ: accession NM_001130173.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Liu,C., Wang,Y., Shi,M., Tao,X., Man,D., Zhang,J. and Han,B.
  TITLE     hnRNPA0 promotes MYB expression by interacting with enhancer lncRNA
            MY34UE-AS in human leukemia cells
  JOURNAL   Biochem Biophys Res Commun 724, 150221 (2024)
   PUBMED   38865811
  REMARK    GeneRIF: hnRNPA0 promotes MYB expression by interacting with
            enhancer lncRNA MY34UE-AS in human leukemia cells.
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Zhang,X.Y., Zhu,B.C., He,M. and Dong,S.S.
  TITLE     Proto-oncogene c-Myb potentiates cisplatin resistance of ovarian
            cancer cells by downregulating lncRNA NKILA and modulating cancer
            stemness and LIN28A-let7 axis
  JOURNAL   J Ovarian Res 17 (1), 102 (2024)
   PUBMED   38745302
  REMARK    GeneRIF: Proto-oncogene c-Myb potentiates cisplatin resistance of
            ovarian cancer cells by downregulating lncRNA NKILA and modulating
            cancer stemness and LIN28A-let7 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Li,S.Q., Lv,F., Xu,W.T., Yin,Y.X., Wei,H.T., Li,K.Z. and Hu,B.L.
  TITLE     lncRNA SNHG4 inhibits ferroptosis by orchestrating miR-150-5p/c-Myb
            axis in colorectal cancer
  JOURNAL   Int J Biol Macromol 268 (Pt 2), 131961 (2024)
   PUBMED   38692535
  REMARK    GeneRIF: lncRNA SNHG4 inhibits ferroptosis by orchestrating
            miR-150-5p/c-Myb axis in colorectal cancer.
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Zhou,Y.E., O'Rourke,J.P., Edwards,J.S. and Ness,S.A.
  TITLE     Single molecule analysis of c-myb alternative splicing reveals
            novel classifiers for precursor B-ALL
  JOURNAL   PLoS One 6 (8), e22880 (2011)
   PUBMED   21853052
  REMARK    GeneRIF: c-myb alternative RNA splicing was elevated and much more
            complex in leukemia samples.
REFERENCE   5  (residues 1 to 761)
  AUTHORS   O'Rourke,J.P. and Ness,S.A.
  TITLE     Alternative RNA splicing produces multiple forms of c-Myb with
            unique transcriptional activities
  JOURNAL   Mol Cell Biol 28 (6), 2091-2101 (2008)
   PUBMED   18195038
  REMARK    GeneRIF: An array of variant transcripts, expressed in highly
            regulated, lineage-specific patterns were formed from alternate
            exons 8A, 9A, 9B, 10A, 13A, & 14A. They encoded c-Myb proteins with
            identical DNA binding domains but unique C-terminal domains.
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Nicolaides,N.C., Gualdi,R., Casadevall,C., Manzella,L. and
            Calabretta,B.
  TITLE     Positive autoregulation of c-myb expression via Myb binding sites
            in the 5' flanking region of the human c-myb gene
  JOURNAL   Mol Cell Biol 11 (12), 6166-6176 (1991)
   PUBMED   1944282
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Westin,E.H., Gorse,K.M. and Clarke,M.F.
  TITLE     Alternative splicing of the human c-myb gene
  JOURNAL   Oncogene 5 (8), 1117-1124 (1990)
   PUBMED   2202948
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Kalkbrenner,F., Guehmann,S. and Moelling,K.
  TITLE     Transcriptional activation by human c-myb and v-myb genes
  JOURNAL   Oncogene 5 (5), 657-661 (1990)
   PUBMED   2189102
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Dasgupta,P. and Reddy,E.P.
  TITLE     Identification of alternatively spliced transcripts for human
            c-myb: molecular cloning and sequence analysis of human c-myb exon
            9A sequences
  JOURNAL   Oncogene 4 (12), 1419-1423 (1989)
   PUBMED   2687764
REFERENCE   10 (residues 1 to 761)
  AUTHORS   Majello,B., Kenyon,L.C. and Dalla-Favera,R.
  TITLE     Human c-myb protooncogene: nucleotide sequence of cDNA and
            organization of the genomic locus
  JOURNAL   Proc Natl Acad Sci U S A 83 (24), 9636-9640 (1986)
   PUBMED   3540945
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL023693.25, AJ606319.1 and
            D25774.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein with three HTH DNA-binding
            domains that functions as a transcription regulator. This protein
            plays an essential role in the regulation of hematopoiesis. This
            gene may be aberrently expressed or rearranged or undergo
            translocation in leukemias and lymphomas, and is considered to be
            an oncogene. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1, also known as 9Aii) represents
            the longest transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ606319.1, AY787467.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341911.10/ ENSP00000339992.5
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.3"
     Protein         1..761
                     /product="transcriptional activator Myb isoform 1"
                     /note="transcriptional activator Myb; proto-oncogene
                     c-Myb; oncogene AMV; v-myb avian myeloblastosis viral
                     oncogene homolog; MYB-GATA1 fusion protein"
                     /calculated_mol_wt=85344
     Region          40..88
                     /region_name="SANT"
                     /note="SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding
                     domains; smart00717"
                     /db_xref="CDD:197842"
     Site            order(43,73..74,76..77,79..81,83..85)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          89..>202
                     /region_name="REB1"
                     /note="Myb superfamily proteins, including transcription
                     factors and mRNA splicing factors [Transcription / RNA
                     processing and modification / Cell division and chromosome
                     partitioning]; COG5147"
                     /db_xref="CDD:227476"
     Region          268..313
                     /region_name="LMSTEN"
                     /note="LMSTEN motif; pfam07988"
                     /db_xref="CDD:462332"
     Region          518..677
                     /region_name="Cmyb_C"
                     /note="C-myb, C-terminal; pfam09316"
                     /db_xref="CDD:462753"
     CDS             1..761
                     /gene="MYB"
                     /gene_synonym="c-myb; c-myb_CDS; Cmyb; efg"
                     /coded_by="NM_001130173.2:207..2492"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47481.1"
                     /db_xref="GeneID:4602"
                     /db_xref="HGNC:HGNC:7545"
                     /db_xref="MIM:189990"
ORIGIN      
        1 marrprhsiy ssdeddedfe mcdhdydgll pksgkrhlgk trwtreedek lkklveqngt
       61 ddwkvianyl pnrtdvqcqh rwqkvlnpel ikgpwtkeed qrvielvqky gpkrwsviak
      121 hlkgrigkqc rerwhnhlnp evkktswtee edriiyqahk rlgnrwaeia kllpgrtdna
      181 iknhwnstmr rkveqegylq esskasqpav atsfqknshl mgfaqappta qlpatgqptv
      241 nndysyyhis eaqnvsshvp ypvalhvniv nvpqpaaaai qrhyndedpe kekrikelel
      301 llmstenelk gqqvlptqnh tcsypgwhst tiadhtrphg dsapvsclge hhstpslpad
      361 pgslpeesas parcmivhqg tildnvknll efaetlqfid sdssswcdls sfeffeeadf
      421 spsqhhtgka lqlqqregng tkpagepspr vnkrmlsess ldppkvlppa rhstiplvil
      481 rkkrgqaspl atgdcssfif advssstpkr spvkslpfsp sqflntssnh ensdlempsl
      541 tstplighkl tvttpfhrdq tvktqkentv frtpaikrsi lessprtptp fkhalaaqei
      601 kygplkmlpq tpshlvedlq dvikqesdes givaefqeng ppllkkikqe vesptdksgn
      661 ffcshhwegd slntqlftqt spvadapnil tssvlmapas edednvlkaf tvpknrslas
      721 plqpcsstwe pascgkmeeq mtsssqarky vnafsartlv m
//
LOCUS       NP_003101                613 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor Sp2 [Homo sapiens].
ACCESSION   NP_003101 NP_612415
VERSION     NP_003101.3
DBSOURCE    REFSEQ: accession NM_003110.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Zheng,R., Zhu,P., Gu,J., Ni,B., Sun,H., He,K., Bian,J., Shao,Y. and
            Du,J.
  TITLE     Transcription factor Sp2 promotes TGFB-mediated interstitial cell
            osteogenic differentiation in bicuspid aortic valves through a
            SMAD-dependent pathway
  JOURNAL   Exp Cell Res 411 (1), 112972 (2022)
   PUBMED   34914964
  REMARK    GeneRIF: Transcription factor Sp2 promotes TGFB-mediated
            interstitial cell osteogenic differentiation in bicuspid aortic
            valves through a SMAD-dependent pathway.
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Da,C.M., Liao,H.Y., Deng,Y.S., Zhao,G.H., Ma,L. and Zhang,H.H.
  TITLE     Transcription Factor SP2 Regulates Ski-mediated Astrocyte
            Proliferation In Vitro
  JOURNAL   Neuroscience 479, 22-34 (2021)
   PUBMED   34687796
  REMARK    GeneRIF: Transcription Factor SP2 Regulates Ski-mediated Astrocyte
            Proliferation In Vitro.
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 613)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 613)
  AUTHORS   Bakovic,M., Waite,K.A. and Vance,D.E.
  TITLE     Functional significance of Sp1, Sp2, and Sp3 transcription factors
            in regulation of the murine CTP:phosphocholine cytidylyltransferase
            alpha promoter
  JOURNAL   J Lipid Res 41 (4), 583-594 (2000)
   PUBMED   10744779
REFERENCE   7  (residues 1 to 613)
  AUTHORS   Rotheneder,H., Geymayer,S. and Haidweger,E.
  TITLE     Transcription factors of the Sp1 family: interaction with E2F and
            regulation of the murine thymidine kinase promoter
  JOURNAL   J Mol Biol 293 (5), 1005-1015 (1999)
   PUBMED   10547281
REFERENCE   8  (residues 1 to 613)
  AUTHORS   Philipsen,S. and Suske,G.
  TITLE     A tale of three fingers: the family of mammalian Sp/XKLF
            transcription factors
  JOURNAL   Nucleic Acids Res 27 (15), 2991-3000 (1999)
   PUBMED   10454592
  REMARK    Review article
REFERENCE   9  (residues 1 to 613)
  AUTHORS   Scohy,S., Van Vooren,P., Szpirer,C. and Szpirer,J.
  TITLE     Assignment1 of Sp genes to rat chromosome bands 7q36 (Sp1),
            10q31-->q32.1 (Sp2), 3q24-->q31 (Sp3) and 6q33 (Sp4) and of the SP2
            gene to human chromosome bands 17q21.3-->q22 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 81 (3-4), 273-274 (1998)
   PUBMED   9730617
REFERENCE   10 (residues 1 to 613)
  AUTHORS   Kingsley,C. and Winoto,A.
  TITLE     Cloning of GT box-binding proteins: a novel Sp1 multigene family
            regulating T-cell receptor gene expression
  JOURNAL   Mol Cell Biol 12 (10), 4251-4261 (1992)
   PUBMED   1341900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB451570.1, BC016680.2,
            M97190.1 and BC033814.2.
            
            On Feb 9, 2007 this sequence version replaced NP_003101.2.
            
            Summary: This gene encodes a member of the Sp subfamily of Sp/XKLF
            transcription factors. Sp family proteins are sequence-specific
            DNA-binding proteins characterized by an amino-terminal
            trans-activation domain and three carboxy-terminal zinc finger
            motifs. This protein contains the least conserved DNA-binding
            domain within the Sp subfamily of proteins, and its DNA sequence
            specificity differs from the other Sp proteins. It localizes
            primarily within subnuclear foci associated with the nuclear
            matrix, and can activate or in some cases repress expression from
            different promoters. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033814.2, SRR1163657.302502.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376741.5/ ENSP00000365931.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..613
                     /product="transcription factor Sp2"
                     /calculated_mol_wt=64769
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02086.3)"
     Region          9..526
                     /region_name="SP2_N"
                     /note="N-terminal domain of transcription factor
                     Specificity Protein (SP) 2; cd22540"
                     /db_xref="CDD:411776"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q02086.3)"
     Region          225..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02086.3)"
     Region          361..369
                     /region_name="9aaTAD, inactive.
                     /evidence=ECO:0000269|PubMed:31375868"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02086.3)"
     Region          372..404
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02086.3)"
     Region          530..549
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(534,536,538,540..541,544..545,548,564,566,570..571,
                     574..575,578,592,594,596,598..599,602..603,606)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          542..568
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          557..579
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          571..594
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          585..607
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          587..607
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..613
                     /gene="SP2"
                     /coded_by="NM_003110.6:52..1893"
                     /db_xref="CCDS:CCDS11521.2"
                     /db_xref="GeneID:6668"
                     /db_xref="HGNC:HGNC:11207"
                     /db_xref="MIM:601801"
ORIGIN      
        1 msdpqtsmaa taavspsdyl qpaasttqds qpsplallaa tcskigppav eaavtppapp
       61 qptprklvpi kpaplplspg knsfgilssk gnilqiqgsq lsasypggql vfaiqnptmi
      121 nkgtrsnani qyqavpqiqa snsqtiqvqp nltnqiqiip gtnqaiitps psshkpvpik
      181 papiqksstt ttpvqsganv vkltggggnv tltlpvnnlv nasdtgaptq lltespptpl
      241 sktnkkarkk slpasqppva vaeqvetvli ettadniiqa gnnllivqsp gggqpavvqq
      301 vqvvppkaeq qqvvqipqqa lrvvqaasat lptvpqkpsq nfqiqaaept ptqvyirtps
      361 gevqtvlvqd sppataaats nttcsspasr aphlsgtskk hsaailrker plpkiapags
      421 iislnaaqla aaaqamqtin ingvqvqgvp vtitntggqq qltvqnvsgn nltisglspt
      481 qiqlqmeqal agetqpgekr rrmactcpnc kdgekrsgeq gkkkhvchip dcgktfrkts
      541 llrahvrlht gerpfvcnwf fcgkrftrsd elqrhartht gdkrfecaqc qkrfmrsdhl
      601 tkhykthlvt knl
//
LOCUS       NP_055639                740 aa            linear   PRI 27-APR-2025
DEFINITION  F-BAR and double SH3 domains protein 2 [Homo sapiens].
ACCESSION   NP_055639
VERSION     NP_055639.2
DBSOURCE    REFSEQ: accession NM_014824.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Frisby,D., Murakonda,A.B., Ashraf,B., Dhawan,K., Almeida-Souza,L.,
            Naslavsky,N. and Caplan,S.
  TITLE     Endosomal actin branching, fission, and receptor recycling require
            FCHSD2 recruitment by MICAL-L1
  JOURNAL   Mol Biol Cell 35 (11), ar144 (2024)
   PUBMED   39382837
  REMARK    GeneRIF: Endosomal actin branching, fission, and receptor recycling
            require FCHSD2 recruitment by MICAL-L1.
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Zhai,X., Shen,Y., Zhang,X., Li,T., Lu,Q. and Xu,Z.
  TITLE     FCHSD2 cooperates with CDC42 and N-WASP to regulate cell protrusion
            formation
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119134 (2022)
   PUBMED   34520816
  REMARK    GeneRIF: FCHSD2 cooperates with CDC42 and N-WASP to regulate cell
            protrusion formation.
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Xiao,G.Y. and Schmid,S.L.
  TITLE     FCHSD2 controls oncogenic ERK1/2 signaling outcome by regulating
            endocytic trafficking
  JOURNAL   PLoS Biol 18 (7), e3000778 (2020)
   PUBMED   32678845
  REMARK    GeneRIF: FCHSD2 controls oncogenic ERK1/2 signaling outcome by
            regulating endocytic trafficking.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Taylor,T.D., Noguchi,H., Totoki,Y., Toyoda,A., Kuroki,Y., Dewar,K.,
            Lloyd,C., Itoh,T., Takeda,T., Kim,D.W., She,X., Barlow,K.F.,
            Bloom,T., Bruford,E., Chang,J.L., Cuomo,C.A., Eichler,E.,
            FitzGerald,M.G., Jaffe,D.B., LaButti,K., Nicol,R., Park,H.S.,
            Seaman,C., Sougnez,C., Yang,X., Zimmer,A.R., Zody,M.C.,
            Birren,B.W., Nusbaum,C., Fujiyama,A., Hattori,M., Rogers,J.,
            Lander,E.S. and Sakaki,Y.
  TITLE     Human chromosome 11 DNA sequence and analysis including novel gene
            identification
  JOURNAL   Nature 440 (7083), 497-500 (2006)
   PUBMED   16554811
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of human FCHSD1 and FCHSD2
            genes in silico
  JOURNAL   Int J Mol Med 13 (5), 749-754 (2004)
   PUBMED   15067381
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Coyle,I.P., Koh,Y.H., Lee,W.C., Slind,J., Fergestad,T.,
            Littleton,J.T. and Ganetzky,B.
  TITLE     Nervous wreck, an SH3 adaptor protein that interacts with Wsp,
            regulates synaptic growth in Drosophila
  JOURNAL   Neuron 41 (4), 521-534 (2004)
   PUBMED   14980202
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Ohno,H., Hirabayashi,S., Kansaku,A., Yao,I., Tajima,M.,
            Nishimura,W., Ohnishi,H., Mashima,H., Fujita,T., Omata,M. and
            Hata,Y.
  TITLE     Carom: a novel membrane-associated guanylate kinase-interacting
            protein with two SH3 domains
  JOURNAL   Oncogene 22 (52), 8422-8431 (2003)
   PUBMED   14627983
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Petitjean,C., Scheydeker,J.L., Suinat,J.L. and Rendoing,J.
  TITLE     [Pulmonary edema in hangings]
  JOURNAL   Ann Anesthesiol Fr 16 Spec No 2-3, 57-65 (1975)
   PUBMED   9873
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP002455.4, AP004241.2 and AP002381.3.
            
            On Apr 12, 2008 this sequence version replaced NP_055639.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.8584.1,
                                           SRR1803614.240764.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409418.9/ ENSP00000386722.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..740
                     /product="F-BAR and double SH3 domains protein 2"
                     /note="SH3 multiple domains 3; FCH and double SH3 domains
                     protein 2; carom; SH3 multiple domains protein 3; nervous
                     wreck homolog; protein nervous wreck 1"
                     /calculated_mol_wt=84146
     Region          16..275
                     /region_name="F-BAR_FCHSD2"
                     /note="The F-BAR (FES-CIP4 Homology and
                     Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains
                     2 (FCHSD2); cd07677"
                     /db_xref="CDD:153361"
     Site            order(21,24,31,34..35,38,41..42,45..46,49,53,56,60,93,96,
                     194,198,223,228,231,234..235,238,242,245,249,253,256..257,
                     260)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153361"
     Region          303..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94868.3)"
     Region          471..527
                     /region_name="SH3_FCHSD_1"
                     /note="First Src Homology 3 domain of FCH and double SH3
                     domains proteins; cd11761"
                     /db_xref="CDD:212695"
     Site            order(478,480,483,487,506..507,521,523..524)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212695"
     Region          567..629
                     /region_name="Required and sufficient for location at
                     clathrin-coated pits.
                     /evidence=ECO:0000269|PubMed:29887380"
                     /note="propagated from UniProtKB/Swiss-Prot (O94868.3)"
     Region          571..626
                     /region_name="SH3_FCHSD2_2"
                     /note="Second Src Homology 3 domain of FCH and double SH3
                     domains protein 2; cd11894"
                     /db_xref="CDD:212827"
     Site            order(576,578,581,585,606..607,620,622..623)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212827"
     Region          633..740
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94868.3)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94868.3)"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:30249660,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94868.3)"
     CDS             1..740
                     /gene="FCHSD2"
                     /gene_synonym="NWK; NWK1; SH3MD3"
                     /coded_by="NM_014824.3:442..2664"
                     /db_xref="CCDS:CCDS8218.2"
                     /db_xref="GeneID:9873"
                     /db_xref="HGNC:HGNC:29114"
                     /db_xref="MIM:617556"
ORIGIN      
        1 mqppprkvkv tqelkniqve qmtklqakhq aecdlledmr tfsqkkaaie reyaqgmqkl
       61 asqylkrdwp gvkaddrndy rsmypvwksf legtmqvaqs rmnicenykn fisepartvr
      121 slkeqqlkrc vdqltkiqte lqetvkdlak gkkkyfeteq mahavrekad ieaksklslf
      181 qsrislqkas vklkarrsec nskatharnd ylltlaaana hqdryyqtdl vnimkaldgn
      241 vydhlkdyli afsrteletc qavqntfqfl lensskvvrd ynlqlflqen avfhkpqpfq
      301 fqpcdsdtsr qlesetgtte ehslnkeark watrvarehk nivhqqrvln dlechgaavs
      361 eqsraeleqk idearenirk aeiiklkaea rldllkqigv svdtwlksam nqvmeelene
      421 rwarppavts ngtlhslnad tereegeefe dnmdvfddss sspsgtlrny pltckvvysy
      481 kasqpdelti eehevlevie dgdmedwvka rnkvgqvgyv pekylqfpts nsllsmlqsl
      541 aaldsrshts snsteaelvs gslngdasvc fvkalydyeg qtddelsfpe gaiirilnke
      601 nqdddgfweg efngrigvfp svlveelsas engdtpwmre iqispspkph aslpplplyd
      661 qppsspypsp dkrsslyfpr spsanekslh aespgfsqas rhtpetsygk lrpvraappp
      721 ptqnhrrpae kiedveitlv
//
LOCUS       NP_001028253             364 aa            linear   PRI 27-APR-2025
DEFINITION  protein L-Myc isoform 1 [Homo sapiens].
ACCESSION   NP_001028253
VERSION     NP_001028253.1
DBSOURCE    REFSEQ: accession NM_001033081.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Shabir,S. and Asiaf,A.
  TITLE     Comparative study on the mutation spectrum of L-MYC and C-MYC genes
            of blood cfDNA in patients with ovarian cancer and healthy females
  JOURNAL   J Obstet Gynaecol Res 49 (12), 2894-2904 (2023)
   PUBMED   37827180
  REMARK    GeneRIF: Comparative study on the mutation spectrum of L-MYC and
            C-MYC genes of blood cfDNA in patients with ovarian cancer and
            healthy females.
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Jiang,H., Li,X., Wang,W., Hu,Y. and Ren,D.
  TITLE     MYCL promotes the progression of triple-negative breast cancer by
            activating the JAK/STAT3 pathway
  JOURNAL   Oncol Rep 48 (5) (2022)
   PUBMED   36177900
  REMARK    GeneRIF: MYCL promotes the progression of triplenegative breast
            cancer by activating the JAK/STAT3 pathway.
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Akifuji,C., Iwasaki,M., Kawahara,Y., Sakurai,C., Cheng,Y.S.,
            Imai,T. and Nakagawa,M.
  TITLE     MYCL promotes iPSC-like colony formation via MYC Box 0 and 2
            domains
  JOURNAL   Sci Rep 11 (1), 24254 (2021)
   PUBMED   34930932
  REMARK    GeneRIF: MYCL promotes iPSC-like colony formation via MYC Box 0 and
            2 domains.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 364)
  AUTHORS   FitzGerald,M.J., Arsura,M., Bellas,R.E., Yang,W., Wu,M., Chin,L.,
            Mann,K.K., DePinho,R.A. and Sonenshein,G.E.
  TITLE     Differential effects of the widely expressed dMax splice variant of
            Max on E-box vs initiator element-mediated regulation by c-Myc
  JOURNAL   Oncogene 18 (15), 2489-2498 (1999)
   PUBMED   10229200
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Speleman,F., Van Camp,G. and Van Roy,N.
  TITLE     Reassignment of MYCL1 to human chromosome 1p34.3 by fluorescence in
            situ hybridization
  JOURNAL   Cytogenet Cell Genet 72 (2-3), 189-190 (1996)
   PUBMED   8978772
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Atchley,W.R. and Fitch,W.M.
  TITLE     Myc and Max: molecular evolution of a family of proto-oncogene
            products and their dimerization partner
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10217-10221 (1995)
   PUBMED   7479755
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Ikegaki,N., Minna,J. and Kennett,R.H.
  TITLE     The human L-myc gene is expressed as two forms of protein in small
            cell lung carcinoma cell lines: detection by monoclonal antibodies
            specific to two myc homology box sequences
  JOURNAL   EMBO J 8 (6), 1793-1799 (1989)
   PUBMED   2548855
REFERENCE   8  (residues 1 to 364)
  AUTHORS   De Greve,J., Battey,J., Fedorko,J., Birrer,M., Evan,G., Kaye,F.,
            Sausville,E. and Minna,J.
  TITLE     The human L-myc gene encodes multiple nuclear phosphoproteins from
            alternatively processed mRNAs
  JOURNAL   Mol Cell Biol 8 (10), 4381-4388 (1988)
   PUBMED   3054516
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Kaye,F., Battey,J., Nau,M., Brooks,B., Seifter,E., De Greve,J.,
            Birrer,M., Sausville,E. and Minna,J.
  TITLE     Structure and expression of the human L-myc gene reveal a complex
            pattern of alternative mRNA processing
  JOURNAL   Mol Cell Biol 8 (1), 186-195 (1988)
   PUBMED   2827002
REFERENCE   10 (residues 1 to 364)
  AUTHORS   DePinho,R.A., Hatton,K.S., Tesfaye,A., Yancopoulos,G.D. and
            Alt,F.W.
  TITLE     The human myc gene family: structure and activity of L-myc and an
            L-myc pseudogene
  JOURNAL   Genes Dev 1 (10), 1311-1326 (1987)
   PUBMED   3322939
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL033527.26 and AI144219.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.188700.1,
                                           SRR1660807.29451.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372816.3/ ENSP00000361903.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..364
                     /product="protein L-Myc isoform 1"
                     /note="myc-related gene from lung cancer; l-myc-1
                     proto-oncogene; protein L-Myc-1; class E basic
                     helix-loop-helix protein 38; v-myc myelocytomatosis viral
                     oncogene homolog 1, lung carcinoma derived; v-myc avian
                     myelocytomatosis viral oncogene lung carcinoma derived
                     homolog"
                     /calculated_mol_wt=40196
     Region          2..231
                     /region_name="Myc_N"
                     /note="Myc amino-terminal region; pfam01056"
                     /db_xref="CDD:460045"
     Region          41..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12524.2)"
     Region          111..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12524.2)"
     Region          219..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12524.2)"
     Region          276..364
                     /region_name="bHLHzip_L-Myc"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in L-Myc and similar proteins; cd11457"
                     /db_xref="CDD:381463"
     Site            order(278,282..283,286..287,289..291,293..294,298,
                     318..319)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381463"
     Site            order(297,300..301,303..304,307,320,323..324,327,329..331,
                     333..334,336..337,340,343..344,347..348,350..352,354..355,
                     357..364)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381463"
     Site            order(297,300..301,303..304,307,320,323..324,327,329..331,
                     333..334,336..337,340,343..344,347..348,350..351,354,
                     357..358,361..362,364)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381463"
     Region          333..361
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P12524.2)"
     CDS             1..364
                     /gene="MYCL"
                     /gene_synonym="bHLHe38; L-Myc; LMYC; MYCL1"
                     /coded_by="NM_001033081.3:484..1578"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30682.1"
                     /db_xref="GeneID:4610"
                     /db_xref="HGNC:HGNC:7555"
                     /db_xref="MIM:164850"
ORIGIN      
        1 mdydsyqhyf ydydcgedfy rstapsediw kkfelvpspp tsppwglgpg agdpapgigp
       61 pepwpggctg deaesrghsk gwgrnyasii rrdcmwsgfs arerleravs drlapgaprg
      121 nppkasaapd ctpsleagnp apaapcplge pktqacsgse spsdseneei dvvtvekrqs
      181 lgirkpvtit vradpldpcm khfhisihqq qhnyaarfpp escsqeease rgpqeevler
      241 daagekedee deeivspppv eseaaqschp kpvssdtedv tkrknhnfle rkrrndlrsr
      301 flalrdqvpt lascskapkv vilskaleyl qalvgaekrm atekrqlrcr qqqlqkriay
      361 ltgy
//
LOCUS       NP_059122                507 aa            linear   PRI 27-APR-2025
DEFINITION  nucleoporin p54 isoform 1 [Homo sapiens].
ACCESSION   NP_059122
VERSION     NP_059122.2
DBSOURCE    REFSEQ: accession NM_017426.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Tang,C., Zhuang,H., Wang,W., Wang,Q., Ma,X., Wang,B., Zhang,Z.,
            Jiang,J., Xie,Z., Tan,W., Yang,L., Liu,S., Hua,Y., Xiao,Y.,
            Ding,B., Chen,Y. and Shang,C.
  TITLE     CircNUP54 promotes hepatocellular carcinoma progression via
            facilitating HuR cytoplasmic export and stabilizing BIRC3 mRNA
  JOURNAL   Cell Death Dis 15 (3), 191 (2024)
   PUBMED   38443362
  REMARK    GeneRIF: CircNUP54 promotes hepatocellular carcinoma progression
            via facilitating HuR cytoplasmic export and stabilizing BIRC3 mRNA.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Harrer,P., Schalk,A., Shimura,M., Baer,S., Calmels,N., Spitz,M.A.,
            Warde,M.A., Schaefer,E., Kittke,V.M.S., Dincer,Y., Wagner,M.,
            Dzinovic,I., Berutti,R., Sato,T., Shirakawa,T., Okazaki,Y.,
            Murayama,K., Oexle,K., Prokisch,H., Mall,V., Melcak,I.,
            Winkelmann,J. and Zech,M.
  TITLE     Recessive NUP54 Variants Underlie Early-Onset Dystonia with
            Striatal Lesions
  JOURNAL   Ann Neurol 93 (2), 330-335 (2023)
   PUBMED   36333996
  REMARK    GeneRIF: Recessive NUP54 Variants Underlie Early-Onset Dystonia
            with Striatal Lesions.
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Stoffler,D., Fahrenkrog,B. and Aebi,U.
  TITLE     The nuclear pore complex: from molecular architecture to functional
            dynamics
  JOURNAL   Curr Opin Cell Biol 11 (3), 391-401 (1999)
   PUBMED   10395558
  REMARK    Review article
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Bodoor,K., Shaikh,S., Enarson,P., Chowdhury,S., Salina,D.,
            Raharjo,W.H. and Burke,B.
  TITLE     Function and assembly of nuclear pore complex proteins
  JOURNAL   Biochem Cell Biol 77 (4), 321-329 (1999)
   PUBMED   10546895
  REMARK    Review article
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Popov,S., Rexach,M., Ratner,L., Blobel,G. and Bukrinsky,M.
  TITLE     Viral protein R regulates docking of the HIV-1 preintegration
            complex to the nuclear pore complex
  JOURNAL   J Biol Chem 273 (21), 13347-13352 (1998)
   PUBMED   9582382
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Hu,T., Guan,T. and Gerace,L.
  TITLE     Molecular and functional characterization of the p62 complex, an
            assembly of nuclear pore complex glycoproteins
  JOURNAL   J Cell Biol 134 (3), 589-601 (1996)
   PUBMED   8707840
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Finlay,D.R., Meier,E., Bradley,P., Horecka,J. and Forbes,D.J.
  TITLE     A complex of nuclear pore proteins required for pore function
  JOURNAL   J Cell Biol 114 (1), 169-183 (1991)
   PUBMED   2050741
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA577078.1, BC012559.1,
            AF157322.1 and AI580839.1.
            
            On Dec 5, 2002 this sequence version replaced NP_059122.1.
            
            Summary: The nuclear envelope creates distinct nuclear and
            cytoplasmic compartments in eukaryotic cells. It consists of two
            concentric membranes perforated by nuclear pores, large protein
            complexes that form aqueous channels to regulate the flow of
            macromolecules between the nucleus and the cytoplasm. These
            complexes are composed of at least 100 different polypeptide
            subunits, many of which belong to the nucleoporin family. This gene
            encodes a member of the phe-gly (FG) repeat-containing nucleoporin
            subset. Multiple alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001517.1, BC012559.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264883.8/ ENSP00000264883.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.1"
     Protein         1..507
                     /product="nucleoporin p54 isoform 1"
                     /note="nucleoporin p54; 54 kDa nucleoporin; nucleoporin
                     54kD; nucleoporin 54kDa"
                     /calculated_mol_wt=55305
     Region          5..445
                     /region_name="9 X 2 AA repeats of F-G"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B4.2)"
     Region          300..437
                     /region_name="Nup54"
                     /note="Nucleoporin complex subunit 54; pfam13874"
                     /db_xref="CDD:464011"
     Region          453..491
                     /region_name="Nup54_C"
                     /note="Nup54 C-terminal interacting domain; pfam18437"
                     /db_xref="CDD:465767"
     CDS             1..507
                     /gene="NUP54"
                     /gene_synonym="DYT37"
                     /coded_by="NM_017426.4:24..1547"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3576.1"
                     /db_xref="GeneID:53371"
                     /db_xref="HGNC:HGNC:17359"
                     /db_xref="MIM:607607"
ORIGIN      
        1 mafnfgapsg tsgtaaataa paggfggfgt tsttagsafs fsaptntgtt glfggtqnkg
       61 fgfgtgfgtt tgtstglgtg lgtglgfggf ntqqqqqttl gglfsqptqa ptqsnqlint
      121 asalsaptll gderdailak wnqlqafwgt gkgyfnnnip pveftqenpf crfkavgysc
      181 mpsnkdedgl vvlvfnkket eirsqqqqlv eslhkvlggn qtltvnvegt ktlpddqtev
      241 viyvverspn gtsrrvpatt lyahfeqani ktqlqqlgvt lsmtrtelsp aqikqllqnp
      301 pagvdpiiwe qakvdnpdse klipvpmvgf kellrrlkvq dqmtkqhqtr ldiisedise
      361 lqknqttsva kiaqykrklm dlshrtlqvl ikqeiqrksg yaiqadeeql rvqldtiqge
      421 lnaptqfkgr lnelmsqirm qnhfgavrse eryyidadll reikqhlkqq qeglshlisi
      481 ikddledikl vehglnetih irggvfs
//
LOCUS       NP_057124                229 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane emp24 domain-containing protein 5 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_057124
VERSION     NP_057124.3
DBSOURCE    REFSEQ: accession NM_016040.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Cheng,X., Deng,X., Zeng,H., Zhou,T., Li,D. and Zheng,W.V.
  TITLE     Silencing of TMED5 inhibits proliferation, migration and invasion,
            and enhances apoptosis of hepatocellular carcinoma cells
  JOURNAL   Adv Clin Exp Med 32 (6), 677-688 (2023)
   PUBMED   36530030
  REMARK    GeneRIF: Silencing of TMED5 inhibits proliferation, migration and
            invasion, and enhances apoptosis of hepatocellular carcinoma cells.
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Zou,H., Chen,H., Liu,S. and Gan,X.
  TITLE     Identification of a novel circ_0018289/miR-183-5p/TMED5 regulatory
            network in cervical cancer development
  JOURNAL   World J Surg Oncol 19 (1), 246 (2021)
   PUBMED   34404391
  REMARK    GeneRIF: Identification of a novel circ_0018289/miR-183-5p/TMED5
            regulatory network in cervical cancer development.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Theiler,R., Fujita,M., Nagae,M., Yamaguchi,Y., Maeda,Y. and
            Kinoshita,T.
  TITLE     The alpha-helical region in p24gamma2 subunit of p24 protein cargo
            receptor is pivotal for the recognition and transport of
            glycosylphosphatidylinositol-anchored proteins
  JOURNAL   J Biol Chem 289 (24), 16835-16843 (2014)
   PUBMED   24778190
  REMARK    GeneRIF: The luminal alpha-helical but not GOLD domain of p24gamma2
            was required for efficient GPI-AP transport.
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Weimann,M., Grossmann,A., Woodsmith,J., Ozkan,Z., Birth,P.,
            Meierhofer,D., Benlasfer,N., Valovka,T., Timmermann,B.,
            Wanker,E.E., Sauer,S. and Stelzl,U.
  TITLE     A Y2H-seq approach defines the human protein methyltransferase
            interactome
  JOURNAL   Nat Methods 10 (4), 339-342 (2013)
   PUBMED   23455924
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Koegler,E., Bonnon,C., Waldmeier,L., Mitrovic,S., Halbeisen,R. and
            Hauri,H.P.
  TITLE     p28, a novel ERGIC/cis Golgi protein, required for Golgi ribbon
            formation
  JOURNAL   Traffic 11 (1), 70-89 (2010)
   PUBMED   19948005
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Huang,F.X., Zhang,Y. and Wang,W.J.
  TITLE     [Effects of matrine on cgi-100 gene expression and proliferation in
            K562 cells]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 16 (3), 525-530 (2008)
   PUBMED   18549622
  REMARK    GeneRIF: Expression of cgi-100 mRNA decreased in a dose- and
            time-dependent manner in the K562 cells treated with matrine and
            over-expression of cgi-100 elevates the proliferation and the
            immaturity level of K562 cells.
REFERENCE   8  (residues 1 to 229)
  AUTHORS   Breuza,L., Halbeisen,R., Jeno,P., Otte,S., Barlowe,C., Hong,W. and
            Hauri,H.P.
  TITLE     Proteomics of endoplasmic reticulum-Golgi intermediate compartment
            (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies
            ERGIC-32, a new cycling protein that interacts with human Erv46
  JOURNAL   J Biol Chem 279 (45), 47242-47253 (2004)
   PUBMED   15308636
REFERENCE   9  (residues 1 to 229)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AI436590.1, BC070051.1, AL117354.12 and CA314982.1.
            
            On Dec 29, 2009 this sequence version replaced NP_057124.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.77817.1,
                                           SRR1660807.209501.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370282.8/ ENSP00000359305.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..229
                     /product="transmembrane emp24 domain-containing protein 5
                     isoform 1 precursor"
                     /note="transmembrane emp24 domain-containing protein 5;
                     p24gamma2; p24 family protein gamma-2; transmembrane emp24
                     protein transport domain containing 5"
                     /calculated_mol_wt=23253
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2770
     mat_peptide     28..229
                     /product="Transmembrane emp24 domain-containing protein 5.
                     /id=PRO_0000010389"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3A6.1)"
                     /calculated_mol_wt=23253
     Region          35..222
                     /region_name="EMP24_GP25L"
                     /note="emp24/gp25L/p24 family/GOLD; pfam01105"
                     /db_xref="CDD:426051"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3A6.1)"
     CDS             1..229
                     /gene="TMED5"
                     /gene_synonym="CGI-100; p24g2; p28"
                     /coded_by="NM_016040.5:172..861"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS743.1"
                     /db_xref="GeneID:50999"
                     /db_xref="HGNC:HGNC:24251"
                     /db_xref="MIM:616876"
ORIGIN      
        1 mgdkiwlpfp vlllaalppv llpgaagftp sldsdftftl pagqkecfyq pmplkaslei
       61 eyqvldgagl didfhlaspe gktlvfeqrk sdgvhtvete vgdymfcfdn tfstisekvi
      121 ffelildnmg eqaqeqedwk kyitgtdild mkledilesi nsiksrlsks ghiqtllraf
      181 eardrniqes nfdrvnfwsm vnlvvmvvvs aiqvymlksl fedkrksrt
//
LOCUS       NP_689506                420 aa            linear   PRI 27-APR-2025
DEFINITION  transcriptional adapter 2-beta [Homo sapiens].
ACCESSION   NP_689506 XP_001128012 XP_001128029 XP_001128049
VERSION     NP_689506.2
DBSOURCE    REFSEQ: accession NM_152293.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Caliskan,G., Baris,I.C., Ayaydin,F., Dobson,M.J., Senarisoy,M.,
            Boros,I.M., Topcu,Z. and Zencir,S.
  TITLE     Che1/AATF interacts with subunits of the histone acetyltransferase
            core module of SAGA complexes
  JOURNAL   PLoS One 12 (12), e0189193 (2017)
   PUBMED   29232376
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Nagy,Z., Riss,A., Romier,C., le Guezennec,X., Dongre,A.R.,
            Orpinell,M., Han,J., Stunnenberg,H. and Tora,L.
  TITLE     The human SPT20-containing SAGA complex plays a direct role in the
            regulation of endoplasmic reticulum stress-induced genes
  JOURNAL   Mol Cell Biol 29 (6), 1649-1660 (2009)
   PUBMED   19114550
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Gamper,A.M., Kim,J. and Roeder,R.G.
  TITLE     The STAGA subunit ADA2b is an important regulator of human GCN5
            catalysis
  JOURNAL   Mol Cell Biol 29 (1), 266-280 (2009)
   PUBMED   18936164
  REMARK    GeneRIF: ADA2a and ADA2b, two human homologues of yeast Ada2, each
            have the ability to form a heterotrimer with ADA3 and GCN5L but
            that only the ADA2b homologue is found in STAGA.
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Zhao,Y., Lang,G., Ito,S., Bonnet,J., Metzger,E., Sawatsubashi,S.,
            Suzuki,E., Le Guezennec,X., Stunnenberg,H.G., Krasnov,A.,
            Georgieva,S.G., Schule,R., Takeyama,K., Kato,S., Tora,L. and
            Devys,D.
  TITLE     A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
            coactivates nuclear receptors, and counteracts heterochromatin
            silencing
  JOURNAL   Mol Cell 29 (1), 92-101 (2008)
   PUBMED   18206972
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Barlev,N.A., Emelyanov,A.V., Castagnino,P., Zegerman,P.,
            Bannister,A.J., Sepulveda,M.A., Robert,F., Tora,L., Kouzarides,T.,
            Birshtein,B.K. and Berger,S.L.
  TITLE     A novel human Ada2 homologue functions with Gcn5 or Brg1 to
            coactivate transcription
  JOURNAL   Mol Cell Biol 23 (19), 6944-6957 (2003)
   PUBMED   12972612
REFERENCE   10 (residues 1 to 420)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC097382.3, BC047794.1 and AK093974.1.
            
            On or before Aug 29, 2007 this sequence version replaced
            XP_001128049.1, XP_001128012.1, XP_001128029.1, NP_689506.1.
            
            Summary: TADA2B functions as a transcriptional adaptor protein that
            potentiates transcription through coordination of histone
            acetyltransferase (HAT) activity and by linking activation factors
            to basal transcriptional machinery (Barlev et al., 2003 [PubMed
            12972612]).[supplied by OMIM, Apr 2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.41781.1,
                                           SRR1660805.231682.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310074.8/ ENSP00000308022.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.1"
     Protein         1..420
                     /product="transcriptional adapter 2-beta"
                     /note="transcriptional adaptor 2 (ADA2 homolog,
                     yeast)-beta; ADA2-beta; ADA2-like protein beta"
                     /calculated_mol_wt=48339
     Region          6..415
                     /region_name="COG5114"
                     /note="Histone acetyltransferase complex SAGA/ADA, subunit
                     ADA2 [Chromatin structure and dynamics]"
                     /db_xref="CDD:227445"
     Region          305..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TJ2.2)"
     CDS             1..420
                     /gene="TADA2B"
                     /gene_synonym="ADA2(beta); ADA2B"
                     /coded_by="NM_152293.3:209..1471"
                     /db_xref="CCDS:CCDS47007.1"
                     /db_xref="GeneID:93624"
                     /db_xref="HGNC:HGNC:30781"
                     /db_xref="MIM:608790"
ORIGIN      
        1 maelgkkycv yclaevsplr frctecqdie lcpecfsaga eighhrryhg yqlvdggrft
       61 lwgpeaeggw tsreeqllld aieqfgfgnw edmaahvgas rtpqevmehy vsmyihgnlg
      121 kacipdtipn rvtdhtcpsg gplspslttp lppldisvae qqqlgymplr ddyeieydqd
      181 aetlisglsv nyddddveie lkrahvdmyv rklkerqrrk niardynlvp aflgkdkkek
      241 ekalkrkitk eekelrlklr plyqfmscke fddlfenmhk ekmlrakire lqryrrngit
      301 kmeesaeyea arhkrekrke nknlagskrg kedgkdsefa aienlpgfel lsdrekvlcs
      361 slnlsparyv tvktiiikdh lqkrqgipsk srlpsyldkv lkkrilnflt esgwisrdas
//
LOCUS       NP_001350154             607 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor Sp2 isoform 3 [Mus musculus].
ACCESSION   NP_001350154
VERSION     NP_001350154.1
DBSOURCE    REFSEQ: accession NM_001363225.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Johnson,C.A. and Ghashghaei,H.T.
  TITLE     Sp2 regulates late neurogenic but not early expansive divisions of
            neural stem cells underlying population growth in the mouse cortex
  JOURNAL   Development 147 (4) (2020)
   PUBMED   32001437
  REMARK    GeneRIF: there is a stage-specific requirement for Sp2 in neural
            stem and progenitor cells in the mouse cortex
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Norrie,J.L., Lupo,M.S., Xu,B., Al Diri,I., Valentine,M., Putnam,D.,
            Griffiths,L., Zhang,J., Johnson,D., Easton,J., Shao,Y., Honnell,V.,
            Frase,S., Miller,S., Stewart,V., Zhou,X., Chen,X. and Dyer,M.A.
  TITLE     Nucleome Dynamics during Retinal Development
  JOURNAL   Neuron 104 (3), 512-528 (2019)
   PUBMED   31493975
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Volkel,S., Stielow,B., Finkernagel,F., Berger,D., Stiewe,T.,
            Nist,A. and Suske,G.
  TITLE     Transcription factor Sp2 potentiates binding of the TALE
            homeoproteins Pbx1:Prep1 and the histone-fold domain protein Nf-y
            to composite genomic sites
  JOURNAL   J Biol Chem 293 (50), 19250-19262 (2018)
   PUBMED   30337366
  REMARK    GeneRIF: a mechanism by which the DNA binding-independent activity
            of Sp2 potentiates genomic loading of Pbx1:Prep1 and Nf-y to
            composite motifs present in many promoters of highly expressed
            genes
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Wegener,A., Kuspert,M., Sock,E., Philipsen,S., Suske,G. and
            Wegner,M.
  TITLE     Sp2 is the only glutamine-rich specificity protein with minor
            impact on development and differentiation in myelinating glia
  JOURNAL   J Neurochem 140 (2), 245-256 (2017)
   PUBMED   27889927
REFERENCE   5  (residues 1 to 607)
  AUTHORS   Zschemisch,N.H., Brusch,I., Hambusch,A.S. and Bleich,A.
  TITLE     Transcription Factor SP2 Enhanced the Expression of Cd14 in
            Colitis-Susceptible C3H/HeJBir
  JOURNAL   PLoS One 11 (5), e0155821 (2016)
   PUBMED   27191968
  REMARK    GeneRIF: SP2 as important factor responsible for higher Cd14
            expression and reduced IBD susceptibility mediated by the C3Bir
            allele.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 607)
  AUTHORS   Suske,G., Bruford,E. and Philipsen,S.
  TITLE     Mammalian SP/KLF transcription factors: bring in the family
  JOURNAL   Genomics 85 (5), 551-556 (2005)
   PUBMED   15820306
REFERENCE   7  (residues 1 to 607)
  AUTHORS   Moorefield,K.S., Fry,S.J. and Horowitz,J.M.
  TITLE     Sp2 DNA binding activity and trans-activation are negatively
            regulated in mammalian cells
  JOURNAL   J Biol Chem 279 (14), 13911-13924 (2004)
   PUBMED   14726517
REFERENCE   8  (residues 1 to 607)
  AUTHORS   Hammer,F., Compagnone,N.A., Vigne,J.L., Bair,S.R. and Mellon,S.H.
  TITLE     Transcriptional regulation of P450scc gene expression in the
            embryonic rodent nervous system
  JOURNAL   Endocrinology 145 (2), 901-912 (2004)
   PUBMED   14576192
REFERENCE   9  (residues 1 to 607)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 607)
  AUTHORS   Bakovic,M., Waite,K.A. and Vance,D.E.
  TITLE     Functional significance of Sp1, Sp2, and Sp3 transcription factors
            in regulation of the murine CTP:phosphocholine cytidylyltransferase
            alpha promoter
  JOURNAL   J Lipid Res 41 (4), 583-594 (2000)
   PUBMED   10744779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK019649.2 and AL596384.17.
            
            Summary: This gene encodes a member of the Sp subfamily of Sp/XKLF
            transcription factors. Sp family proteins are sequence-specific
            DNA-binding proteins characterized by an amino-terminal
            trans-activation domain and three carboxy-terminal zinc finger
            motifs. This protein contains the least conserved DNA-binding
            domain within the Sp subfamily of proteins, and its DNA sequence
            specificity differs from the other Sp proteins. The protein can act
            as a transcriptional activator or repressor, depending on the
            promoter and cell type. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK019649.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 60.17 cM"
     Protein         1..607
                     /product="transcription factor Sp2 isoform 3"
                     /note="transcription factor Sp2"
                     /calculated_mol_wt=64219
     Region          4..520
                     /region_name="SP2_N"
                     /note="N-terminal domain of transcription factor
                     Specificity Protein (SP) 2; cd22540"
                     /db_xref="CDD:411776"
     Region          524..543
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(528,530,532,534..535,538..539,542,558,560,564..565,
                     568..569,572,586,588,590,592..593,596..597,600)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          536..562
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          551..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          565..588
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          579..601
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          581..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..607
                     /gene="Sp2"
                     /gene_synonym="4930480I16Rik; mKIAA0048"
                     /coded_by="NM_001363225.1:293..2116"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS88237.1"
                     /db_xref="GeneID:78912"
                     /db_xref="MGI:MGI:1926162"
ORIGIN      
        1 msmaataavs psdylqpaaa ttqdsqpspl allaatcski gppaveaavt ppappqptpr
       61 klvpikpapl plspcknsfs ilsskgnilq iqgsqlstsy pggqfvfaiq nptlinkgsr
      121 snasiqyqvp qiqgnssqti qvqpsltnqi qvipgtnqai ttpstsghkp vpikpapvqk
      181 ssttttpvqs ganvvkltgg gsnmtltlpl nnlvntsdig gpaqlltesp ptplsktnkk
      241 arkkslpvsq psvavaeqve tvliettadn iiqagnnlli vqspgggqpa vvqqvqvvpp
      301 kaeqqqvvqi pqqalrvvqa asatlptvpq kpsqnfqiqt teptptqvyi rtpsgevqtv
      361 lvqdsppata attstvtcns palraphlsg tskkhsaail rkerplpkia pagsiislna
      421 aqlaaaaqam qtiningvqv qgvpvtitnt ggqqqltvqn vsgnnltisg lsptqiqlqm
      481 eqalageaqp gekrrrmact cpnckdgekr sgeqgkkkhv chipdcgktf rktsllrahv
      541 rlhtgerpfv cnwffcgkrf trsdelqrha rthtgdkrfe caqcqkrfmr sdhltkhykt
      601 hlgtkgl
//
LOCUS       NP_001269058            1450 aa            linear   PRI 27-APR-2025
DEFINITION  protein phosphatase Slingshot homolog 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001269058
VERSION     NP_001269058.1
DBSOURCE    REFSEQ: accession NM_001282129.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1450)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 1450)
  AUTHORS   Yang,D., Xiao,P., Li,Q., Fu,X., Pan,C., Lu,D., Wen,S., Xia,W.,
            He,D., Li,H., Fang,H., Shen,Y., Xu,Z., Lin,A., Wang,C., Yu,X.,
            Wu,J. and Sun,J.
  TITLE     Allosteric modulation of the catalytic VYD loop in Slingshot by its
            N-terminal domain underlies both Slingshot auto-inhibition and
            activation
  JOURNAL   J Biol Chem 293 (42), 16226-16241 (2018)
   PUBMED   30154244
  REMARK    GeneRIF: the N-terminal region of human Slingshot2 auto-inhibits
            its phosphatase activity in a noncompetitive manner
            Erratum:[J Biol Chem. 2019 Feb 22;294(8):2947. doi:
            10.1074/jbc.AAC119.007803. PMID: 30796175]
REFERENCE   3  (residues 1 to 1450)
  AUTHORS   Cornelis,M.C., Byrne,E.M., Esko,T., Nalls,M.A., Ganna,A.,
            Paynter,N., Monda,K.L., Amin,N., Fischer,K., Renstrom,F.,
            Ngwa,J.S., Huikari,V., Cavadino,A., Nolte,I.M., Teumer,A., Yu,K.,
            Marques-Vidal,P., Rawal,R., Manichaikul,A., Wojczynski,M.K.,
            Vink,J.M., Zhao,J.H., Burlutsky,G., Lahti,J., Mikkila,V.,
            Lemaitre,R.N., Eriksson,J., Musani,S.K., Tanaka,T., Geller,F.,
            Luan,J., Hui,J., Magi,R., Dimitriou,M., Garcia,M.E., Ho,W.K.,
            Wright,M.J., Rose,L.M., Magnusson,P.K., Pedersen,N.L., Couper,D.,
            Oostra,B.A., Hofman,A., Ikram,M.A., Tiemeier,H.W.,
            Uitterlinden,A.G., van Rooij,F.J., Barroso,I., Johansson,I.,
            Xue,L., Kaakinen,M., Milani,L., Power,C., Snieder,H., Stolk,R.P.,
            Baumeister,S.E., Biffar,R., Gu,F., Bastardot,F., Kutalik,Z.,
            Jacobs,D.R. Jr., Forouhi,N.G., Mihailov,E., Lind,L., Lindgren,C.,
            Michaelsson,K., Morris,A., Jensen,M., Khaw,K.T., Luben,R.N.,
            Wang,J.J., Mannisto,S., Perala,M.M., Kahonen,M., Lehtimaki,T.,
            Viikari,J., Mozaffarian,D., Mukamal,K., Psaty,B.M., Doring,A.,
            Heath,A.C., Montgomery,G.W., Dahmen,N., Carithers,T., Tucker,K.L.,
            Ferrucci,L., Boyd,H.A., Melbye,M., Treur,J.L., Mellstrom,D.,
            Hottenga,J.J., Prokopenko,I., Tonjes,A., Deloukas,P., Kanoni,S.,
            Lorentzon,M., Houston,D.K., Liu,Y., Danesh,J., Rasheed,A.,
            Mason,M.A., Zonderman,A.B., Franke,L., Kristal,B.S.,
            Karjalainen,J., Reed,D.R., Westra,H.J., Evans,M.K., Saleheen,D.,
            Harris,T.B., Dedoussis,G., Curhan,G., Stumvoll,M., Beilby,J.,
            Pasquale,L.R., Feenstra,B., Bandinelli,S., Ordovas,J.M., Chan,A.T.,
            Peters,U., Ohlsson,C., Gieger,C., Martin,N.G., Waldenberger,M.,
            Siscovick,D.S., Raitakari,O., Eriksson,J.G., Mitchell,P.,
            Hunter,D.J., Kraft,P., Rimm,E.B., Boomsma,D.I., Borecki,I.B.,
            Loos,R.J., Wareham,N.J., Vollenweider,P., Caporaso,N., Grabe,H.J.,
            Neuhouser,M.L., Wolffenbuttel,B.H., Hu,F.B., Hypponen,E.,
            Jarvelin,M.R., Cupples,L.A., Franks,P.W., Ridker,P.M., van
            Duijn,C.M., Heiss,G., Metspalu,A., North,K.E., Ingelsson,E.,
            Nettleton,J.A., van Dam,R.M. and Chasman,D.I.
  CONSRTM   Coffee and Caffeine Genetics Consortium; International Parkinson's
            Disease Genomics Consortium (IPDGC); North American Brain
            Expression Consortium (NABEC); UK Brain Expression Consortium
            (UKBEC)
  TITLE     Genome-wide meta-analysis identifies six novel loci associated with
            habitual coffee consumption
  JOURNAL   Mol Psychiatry 20 (5), 647-656 (2015)
   PUBMED   25288136
  REMARK    Review article
REFERENCE   4  (residues 1 to 1450)
  AUTHORS   Xu,X., Gera,N., Li,H., Yun,M., Zhang,L., Wang,Y., Wang,Q.J. and
            Jin,T.
  TITLE     GPCR-mediated PLCbetagamma/PKCbeta/PKD signaling pathway regulates
            the cofilin phosphatase slingshot 2 in neutrophil chemotaxis
  JOURNAL   Mol Biol Cell 26 (5), 874-886 (2015)
   PUBMED   25568344
  REMARK    GeneRIF: Novel signaling pathway consisting of chemoattractant
            GPCR/Galphai protein, PLC, PKCbeta and PKDs that regulates
            SSH2/cofilin activity, F-actin polymerization and directional
            assembly of actin cytoskeleton in neutrophil chemotaxis was
            identified.
REFERENCE   5  (residues 1 to 1450)
  AUTHORS   Song,S.Y., Kang,M.R., Yoo,N.J. and Lee,S.H.
  TITLE     Mutational analysis of mononucleotide repeats in dual specificity
            tyrosine phosphatase genes in gastric and colon carcinomas with
            microsatellite instability
  JOURNAL   APMIS 118 (5), 389-393 (2010)
   PUBMED   20477815
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Erratum:[APMIS. 2021 May;129(5):280. doi: 10.1111/apm.13126. PMID:
            33864290]
REFERENCE   6  (residues 1 to 1450)
  AUTHORS   Kligys,K., Claiborne,J.N., DeBiase,P.J., Hopkinson,S.B., Wu,Y.,
            Mizuno,K. and Jones,J.C.
  TITLE     The slingshot family of phosphatases mediates Rac1 regulation of
            cofilin phosphorylation, laminin-332 organization, and motility
            behavior of keratinocytes
  JOURNAL   J Biol Chem 282 (44), 32520-32528 (2007)
   PUBMED   17848544
  REMARK    GeneRIF: Expression of phosphatase-dead versions of SSH proteins,
            SSH1, SSH2 & SSH3 results in phosphorylation/inactivation of
            cofilin, changes in cytoskeleton organization, loss of cell
            polarity, and assembly of aberrant arrays of laminin-332 in
            keratinocytes.
REFERENCE   7  (residues 1 to 1450)
  AUTHORS   Jung,S.K., Jeong,D.G., Yoon,T.S., Kim,J.H., Ryu,S.E. and Kim,S.J.
  TITLE     Crystal structure of human slingshot phosphatase 2
  JOURNAL   Proteins 68 (1), 408-412 (2007)
   PUBMED   17427953
REFERENCE   8  (residues 1 to 1450)
  AUTHORS   Ohta,Y., Kousaka,K., Nagata-Ohashi,K., Ohashi,K., Muramoto,A.,
            Shima,Y., Niwa,R., Uemura,T. and Mizuno,K.
  TITLE     Differential activities, subcellular distribution and tissue
            expression patterns of three members of Slingshot family
            phosphatases that dephosphorylate cofilin
  JOURNAL   Genes Cells 8 (10), 811-824 (2003)
   PUBMED   14531860
REFERENCE   9  (residues 1 to 1450)
  AUTHORS   Chan,S.Y., Chan,A.K., Cheung,B.P., Liang,Y. and Leung,M.P.
  TITLE     Identification of genes expressed during myocardial development
  JOURNAL   Chin Med J (Engl) 116 (9), 1329-1332 (2003)
   PUBMED   14527359
REFERENCE   10 (residues 1 to 1450)
  AUTHORS   Niwa,R., Nagata-Ohashi,K., Takeichi,M., Mizuno,K. and Uemura,T.
  TITLE     Control of actin reorganization by Slingshot, a family of
            phosphatases that dephosphorylate ADF/cofilin
  JOURNAL   Cell 108 (2), 233-246 (2002)
   PUBMED   11832213
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104982.7, DA749059.1,
            AK296413.1, AB099290.1 and AI609950.1.
            
            Summary: This gene encodes a protein tyrosine phosphatase that
            plays a key role in the regulation of actin filaments. The encoded
            protein dephosphorylates and activates cofilin, which promotes
            actin filament depolymerization. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296413.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000540801.6/ ENSP00000444743.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..1450
                     /product="protein phosphatase Slingshot homolog 2 isoform
                     1"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="protein phosphatase Slingshot homolog 2; SSH-like
                     protein 2"
                     /calculated_mol_wt=161017
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SW75; propagated from
                     UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          38..263
                     /region_name="SSH-N"
                     /note="N-terminal domain conserved in slingshot (SSH)
                     phosphatases; cd11652"
                     /db_xref="CDD:212166"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SW75; propagated from
                     UniProtKB/Swiss-Prot (Q76I76.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          277..329
                     /region_name="DEK_C"
                     /note="DEK C terminal domain; pfam08766"
                     /db_xref="CDD:462592"
     Region          332..475
                     /region_name="DSP_slingshot_2"
                     /note="dual specificity phosphatase domain of slingshot
                     homolog 2; cd14569"
                     /db_xref="CDD:350417"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SW75; propagated from
                     UniProtKB/Swiss-Prot (Q76I76.1)"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q76I76.1)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SW75; propagated from
                     UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          644..668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76I76.1)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SW75; propagated from
                     UniProtKB/Swiss-Prot (Q76I76.1)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SW75; propagated from
                     UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          691..711
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          723..755
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          824..852
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          867..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          904..981
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          989..1008
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          1046..1068
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          1097..1135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76I76.1)"
     Region          1171..1206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76I76.1)"
     Site            1244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q76I76.1)"
     Site            1449
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q76I76.1)"
     CDS             1..1450
                     /gene="SSH2"
                     /gene_synonym="SSH-2; SSH-2L"
                     /coded_by="NM_001282129.2:229..4581"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS74024.1"
                     /db_xref="GeneID:85464"
                     /db_xref="HGNC:HGNC:30580"
                     /db_xref="MIM:606779"
ORIGIN      
        1 malvtvqrsp tpsttsspca ssshledses aallccecee seiftdsnea dsgeeecrsq
       61 prsisesflt vkgaalflpr gngsstpris hrrnkhagdl qqhlqamfil lrpednirla
      121 vrlestyqnr trymvvvstn grqdteesiv lgmdfssnds stctmglvlp lwsdtlihld
      181 gdggfsvstd nrvhifkpvs vqamwsalqs lhkacevara hnyypgslfl twvsyyeshi
      241 nsdqssvnew namqdvqshr pdspalftdi ptererterl iktklreimm qkdlenitsk
      301 eirtelemqm vcnlrefkef idnemivilg qmdsptqife hvflgsewna snledlqnrg
      361 vryilnvtre idnffpgvfe yhnirvydee atdllaywnd tykfiskakk hgskclvhck
      421 mgvsrsastv iayamkeygw nldraydyvk errtvtkpnp sfmrqleeyq gillaskqrh
      481 nklwrshsds dlsdhhepic kpglelnkkd ittsadqiae vktmeshppi ppvfvehmvp
      541 qdanqkglct kermicleft srefhagqie delnlnding cssgcclnes kfpldnchas
      601 kaliqpghvp emankfpdlt vedletdalk admnvhllpm eeltsplkdp pmspdpesps
      661 pqpscqteis dfstdridff salekfvels qetrsrsfsh srmeelgggr nescrlsvve
      721 vapskvtadd qrssslsntp haseessmde eqskaiselv spdifmqshs enaisvkeiv
      781 teiesisqgv gqiqlkgdil pnpchtpkkn sihelllera qtpenkpghm eqdedsctaq
      841 pelakdsgmc npegcltths siadleegep aegeqelqgs gmhpgakwyp gsvrratlef
      901 eerlrqeqeh hgaaptctsl strknsknds svadlapkgk sdeappehsf vlkepemskg
      961 kgkysgseag slshseqnat vpaprvlefd hlpdpqegpg sdtgtqqegv lkdlrtvipy
     1021 qesetqavpl plpkrveiie ythivtspnh tgpgseiats eksgeqglrk vnmeksvtvl
     1081 ctldenlnrt ldpnqvslhp qvlplphsss pehnrptdhp tsilsspedr gsslstalet
     1141 aapfvshtth llsasldylh pqtmvhlegf teqssttdep saeqvswees qesplssgse
     1201 vpykdsqlss adlslisklg dntgelqekm dplpvacrlp hsssseniks lshspgvvke
     1261 rakeiesrvv fqagltkpsq mrrsaslakl gyldlckdcl perepasces phlkllqpfl
     1321 rtdsgmhame dqeslenpga phnpeptksf veqlttteci vqskpverpl vqyakefgss
     1381 qqyllpragl eltssegglp vlqtqglqca cpapglavap rqqhgrthpl rrlkkandkk
     1441 rttnpfyntm
//
LOCUS       NP_002172                411 aa            linear   PRI 27-APR-2025
DEFINITION  indian hedgehog protein preproprotein [Homo sapiens].
ACCESSION   NP_002172 XP_050846
VERSION     NP_002172.2
DBSOURCE    REFSEQ: accession NM_002181.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Harimi,S., Khansarinejad,B., Fesahat,F. and Mondanizadeh,M.
  TITLE     Hsa-miR-15b-5p/miR-195-5p Controls Osteogenic Differentiation of
            Human Adipose-Derived Mesenchymal Stem Cells Through Regulating
            Indian Hedgehog Expression
  JOURNAL   Appl Biochem Biotechnol 196 (8), 4793-4806 (2024)
   PUBMED   37964167
  REMARK    GeneRIF: Hsa-miR-15b-5p/miR-195-5p Controls Osteogenic
            Differentiation of Human Adipose-Derived Mesenchymal Stem Cells
            Through Regulating Indian Hedgehog Expression.
REFERENCE   2  (residues 1 to 411)
  AUTHORS   O'Sullivan,E.D., Mylonas,K.J., Xin,C., Baird,D.P., Carvalho,C.,
            Docherty,M.H., Campbell,R., Matchett,K.P., Waddell,S.H.,
            Walker,A.D., Gallagher,K.M., Jia,S., Leung,S., Laird,A.,
            Wilflingseder,J., Willi,M., Reck,M., Finnie,S., Pisco,A.,
            Gordon-Keylock,S., Medvinsky,A., Boulter,L., Henderson,N.C.,
            Kirschner,K., Chandra,T., Conway,B.R., Hughes,J., Denby,L.,
            Bonventre,J.V. and Ferenbach,D.A.
  TITLE     Indian Hedgehog release from TNF-activated renal epithelia drives
            local and remote organ fibrosis
  JOURNAL   Sci Transl Med 15 (698), eabn0736 (2023)
   PUBMED   37256934
  REMARK    GeneRIF: Indian Hedgehog release from TNF-activated renal epithelia
            drives local and remote organ fibrosis.
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Ozyavuz Cubuk,P. and Duz,M.B.
  TITLE     Acrocapitofemoral dysplasia: Novel mutation in IHH in two adult
            patients from the third family in the literature and progression of
            the disease
  JOURNAL   Eur J Med Genet 64 (11), 104343 (2021)
   PUBMED   34530144
  REMARK    GeneRIF: Acrocapitofemoral dysplasia: Novel mutation in IHH in two
            adult patients from the third family in the literature and
            progression of the disease.
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Wang,X., Liu,H., Liu,Y., Han,G., Wang,Y., Chen,H., He,L. and Ma,G.
  TITLE     Highly Conserved C-Terminal Region of Indian Hedgehog N-Fragment
            Contributes to Its Auto-Processing and Multimer Formation
  JOURNAL   Biomolecules 11 (6), 792 (2021)
   PUBMED   34070546
  REMARK    GeneRIF: Highly Conserved C-Terminal Region of Indian Hedgehog
            N-Fragment Contributes to Its Auto-Processing and Multimer
            Formation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Chuang,P.T. and McMahon,A.P.
  TITLE     Vertebrate Hedgehog signalling modulated by induction of a
            Hedgehog-binding protein
  JOURNAL   Nature 397 (6720), 617-621 (1999)
   PUBMED   10050855
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Carpenter,D., Stone,D.M., Brush,J., Ryan,A., Armanini,M.,
            Frantz,G., Rosenthal,A. and de Sauvage,F.J.
  TITLE     Characterization of two patched receptors for the vertebrate
            hedgehog protein family
  JOURNAL   Proc Natl Acad Sci U S A 95 (23), 13630-13634 (1998)
   PUBMED   9811851
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Leek,J.P., Moynihan,T.P., Anwar,R., Bonthron,D.T., Markham,A.F. and
            Lench,N.J.
  TITLE     Assignment of Indian hedgehog (IHH) to human chromosome bands
            2q33-->q35 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 76 (3-4), 187-188 (1997)
   PUBMED   9186520
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Porter,J.A., Young,K.E. and Beachy,P.A.
  TITLE     Cholesterol modification of hedgehog signaling proteins in animal
            development
  JOURNAL   Science 274 (5285), 255-259 (1996)
   PUBMED   8824192
  REMARK    Erratum:[Science 1996 Dec 6;274(5293):1597]
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Marigo,V., Roberts,D.J., Lee,S.M., Tsukurov,O., Levi,T.,
            Gastier,J.M., Epstein,D.J., Gilbert,D.J., Copeland,N.G.,
            Seidman,C.E. et al.
  TITLE     Cloning, expression, and chromosomal location of SHH and IHH: two
            human homologues of the Drosophila segment polarity gene hedgehog
  JOURNAL   Genomics 28 (1), 44-51 (1995)
   PUBMED   7590746
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Chang,D.T., Lopez,A., von Kessler,D.P., Chiang,C., Simandl,B.K.,
            Zhao,R., Seldin,M.F., Fallon,J.F. and Beachy,P.A.
  TITLE     Products, genetic linkage and limb patterning activity of a murine
            hedgehog gene
  JOURNAL   Development 120 (11), 3339-3353 (1994)
   PUBMED   7720571
  REMARK    GeneRIF: describes cloning of human IHH
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC097468.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 14, 2006 this sequence version replaced NP_002172.1.
            
            Summary: This gene encodes a member of the hedgehog family of
            proteins. The encoded preproprotein is proteolytically processed to
            generate multiple protein products, including an N-terminal
            fragment that is involved in signaling. Hedgehog family proteins
            are essential secreted signaling molecules that regulate a variety
            of developmental processes including growth, patterning and
            morphogenesis. The protein encoded by this gene specifically plays
            a role in bone growth and differentiation. Mutations in this gene
            are the cause of brachydactyly type A1, which is characterized by
            shortening or malformation of the fingers and toes. Mutations in
            this gene are also the cause of acrocapitofemoral dysplasia.
            [provided by RefSeq, Nov 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034757.1, BC136587.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267771 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295731.7/ ENSP00000295731.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..411
                     /product="indian hedgehog protein preproprotein"
                     /note="indian hedgehog protein; Indian hedgehog homolog"
                     /calculated_mol_wt=42226
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3043
     mat_peptide     28..411
                     /product="Indian hedgehog protein. /id=PRO_0000013229"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14623.4)"
                     /calculated_mol_wt=42226
     mat_peptide     28..202
                     /product="Indian hedgehog protein N-product.
                     /id=PRO_0000013230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14623.4)"
                     /calculated_mol_wt=19676
     Region          28..189
                     /region_name="HH_signal"
                     /note="Hedgehog amino-terminal signalling domain;
                     pfam01085"
                     /db_xref="CDD:460055"
     Region          191..386
                     /region_name="Hint"
                     /note="Hint module; pfam01079"
                     /db_xref="CDD:460051"
     Site            202..203
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000250|UniProtKB:Q02936; propagated from
                     UniProtKB/Swiss-Prot (Q14623.4)"
     Site            248
                     /site_type="other"
                     /note="Involved in cholesterol transfer.
                     /evidence=ECO:0000250|UniProtKB:Q02936; propagated from
                     UniProtKB/Swiss-Prot (Q14623.4)"
     Site            272
                     /site_type="other"
                     /note="Involved in auto-cleavage.
                     /evidence=ECO:0000250|UniProtKB:Q02936; propagated from
                     UniProtKB/Swiss-Prot (Q14623.4)"
     Site            275
                     /site_type="other"
                     /note="Essential for auto-cleavage.
                     /evidence=ECO:0000250|UniProtKB:Q02936; propagated from
                     UniProtKB/Swiss-Prot (Q14623.4)"
     Site            282
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q14623.4)"
     CDS             1..411
                     /gene="IHH"
                     /gene_synonym="BDA1; HHG2"
                     /coded_by="NM_002181.4:455..1690"
                     /db_xref="CCDS:CCDS33380.1"
                     /db_xref="GeneID:3549"
                     /db_xref="HGNC:HGNC:5956"
                     /db_xref="MIM:600726"
ORIGIN      
        1 msparlrprl hfclvlllll vvpaawgcgp grvvgsrrrp prklvplayk qfspnvpekt
       61 lgasgryegk iarsserfke ltpnynpdii fkdeentgad rlmtqrckdr lnslaisvmn
      121 qwpgvklrvt egwdedghhs eeslhyegra vdittsdrdr nkygllarla veagfdwvyy
      181 eskahvhcsv ksehsaaakt ggcfpagaqv rlesgarval savrpgdrvl amgedgsptf
      241 sdvlifldre phrlrafqvi etqdpprrla ltpahllfta dnhtepaarf ratfashvqp
      301 gqyvlvagvp glqparvaav sthvalgaya pltkhgtlvv edvvascfaa vadhhlaqla
      361 fwplrlfhsl awgswtpgeg vhwypqllyr lgrllleegs fhplgmsgag s
//
LOCUS       NP_003878               1006 aa            linear   PRI 27-APR-2025
DEFINITION  arf-GAP with SH3 domain, ANK repeat and PH domain-containing
            protein 2 isoform a [Homo sapiens].
ACCESSION   NP_003878
VERSION     NP_003878.1
DBSOURCE    REFSEQ: accession NM_003887.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Fujii,A., Masuda,T., Iwata,M., Tobo,T., Wakiyama,H., Koike,K.,
            Kosai,K., Nakano,T., Kuramitsu,S., Kitagawa,A., Sato,K.,
            Kouyama,Y., Shimizu,D., Matsumoto,Y., Utsunomiya,T., Ohtsuka,T.,
            Yamanishi,Y., Nakamura,M. and Mimori,K.
  TITLE     The novel driver gene ASAP2 is a potential druggable target in
            pancreatic cancer
  JOURNAL   Cancer Sci 112 (4), 1655-1668 (2021)
   PUBMED   33605496
  REMARK    GeneRIF: The novel driver gene ASAP2 is a potential druggable
            target in pancreatic cancer.
REFERENCE   4  (residues 1 to 1006)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1006)
  AUTHORS   Seuter,S., Ryynanen,J. and Carlberg,C.
  TITLE     The ASAP2 gene is a primary target of 1,25-dihydroxyvitamin D3 in
            human monocytes and macrophages
  JOURNAL   J Steroid Biochem Mol Biol 144 Pt A, 12-18 (2014)
   PUBMED   23999061
REFERENCE   6  (residues 1 to 1006)
  AUTHORS   Kim,H. and Lee,Y.
  TITLE     Interaction of poly(A) polymerase with the 25-kDa subunit of
            cleavage factor I
  JOURNAL   Biochem Biophys Res Commun 289 (2), 513-518 (2001)
   PUBMED   11716503
REFERENCE   7  (residues 1 to 1006)
  AUTHORS   Uchida,H., Kondo,A., Yoshimura,Y., Mazaki,Y. and Sabe,H.
  TITLE     PAG3/Papalpha/KIAA0400, a GTPase-activating protein for
            ADP-ribosylation factor (ARF), regulates ARF6 in Fcgamma
            receptor-mediated phagocytosis of macrophages
  JOURNAL   J Exp Med 193 (8), 955-966 (2001)
   PUBMED   11304556
REFERENCE   8  (residues 1 to 1006)
  AUTHORS   Kondo,A., Hashimoto,S., Yano,H., Nagayama,K., Mazaki,Y. and Sabe,H.
  TITLE     A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an
            ADP-ribosylation factor GTPase-activating protein activity, is
            involved in paxillin recruitment to focal adhesions and cell
            migration
  JOURNAL   Mol Biol Cell 11 (4), 1315-1327 (2000)
   PUBMED   10749932
REFERENCE   9  (residues 1 to 1006)
  AUTHORS   Andreev,J., Simon,J.P., Sabatini,D.D., Kam,J., Plowman,G.,
            Randazzo,P.A. and Schlessinger,J.
  TITLE     Identification of a new Pyk2 target protein with Arf-GAP activity
  JOURNAL   Mol Cell Biol 19 (3), 2338-2350 (1999)
   PUBMED   10022920
REFERENCE   10 (residues 1 to 1006)
  AUTHORS   Brown,M.T., Andrade,J., Radhakrishna,H., Donaldson,J.G.,
            Cooper,J.A. and Randazzo,P.A.
  TITLE     ASAP1, a phospholipid-dependent arf GTPase-activating protein that
            associates with and is phosphorylated by Src
  JOURNAL   Mol Cell Biol 18 (12), 7038-7051 (1998)
   PUBMED   9819391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB007860.1, AC079782.6 and
            AA918883.1.
            
            Summary: This gene encodes a multidomain protein containing an
            N-terminal alpha-helical region with a coiled-coil motif, followed
            by a pleckstrin homology (PH) domain, an Arf-GAP domain, an ankyrin
            homology region, a proline-rich region, and a C-terminal Src
            homology 3 (SH3) domain. The protein localizes in the Golgi
            apparatus and at the plasma membrane, where it colocalizes with
            protein tyrosine kinase 2-beta (PYK2). The encoded protein forms a
            stable complex with PYK2 in vivo. This interaction appears to be
            mediated by binding of its SH3 domain to the C-terminal
            proline-rich domain of PYK2. The encoded protein is tyrosine
            phosphorylated by activated PYK2. It has catalytic activity for
            class I and II ArfGAPs in vitro, and can bind the class III Arf
            ARF6 without immediate GAP activity. The encoded protein is
            believed to function as an ARF GAP that controls ARF-mediated
            vesicle budding when recruited to Golgi membranes. In addition, it
            functions as a substrate and downstream target for PYK2 and SRC, a
            pathway that may be involved in the regulation of vesicular
            transport. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB007860.1, SRR7346977.2974628.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281419.8/ ENSP00000281419.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..1006
                     /product="arf-GAP with SH3 domain, ANK repeat and PH
                     domain-containing protein 2 isoform a"
                     /note="centaurin, beta 3; PYK2 C terminus-associated
                     protein; arf-GAP with SH3 domain, ANK repeat and PH
                     domain-containing protein 2; pyk2 C-terminus-associated
                     protein; development and differentiation-enhancing factor
                     2; paxillin-associated protein with ARF GAP activity 3"
                     /calculated_mol_wt=111520
     Region          34..248
                     /region_name="BAR_ASAP2"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with
                     SH3 domain, ANK repeat and PH domain containing protein 2;
                     cd07642"
                     /db_xref="CDD:153326"
     Site            order(43,46..47,51,53..54,57..58,60..61,71..72,74..75,
                     78..79,81..82,85,101,104..105,206,209..210,212,214,
                     217..218,220..221,227..228,231..232,234..235,238..239,
                     241..242)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153326"
     Region          288..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43150.3)"
     Region          297..403
                     /region_name="PH_ASAP"
                     /note="ArfGAP with SH3 domain, ankyrin repeat and PH
                     domain Pleckstrin homology (PH) domain; cd13251"
                     /db_xref="CDD:270071"
     Region          419..541
                     /region_name="ArfGap_ASAP2"
                     /note="ArfGAP domain of ASAP2 (ArfGAP2 with SH3 domain,
                     ANK repeat and PH domain-containing protein 2); cd08849"
                     /db_xref="CDD:350074"
     Site            order(422..423,426,449..451,472,480..484,486..488,
                     490..492,496..497,500..501,533,536..537)
                     /site_type="other"
                     /note="ANK repeat binding site [polypeptide binding]"
                     /db_xref="CDD:350074"
     Site            order(436,439,456,459,522)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350074"
     Site            order(436,439,456,459,464)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350074"
     Site            order(461,464..465)
                     /site_type="other"
                     /note="GTP binding site [chemical binding]"
                     /db_xref="CDD:350074"
     Region          550..582
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <562..677
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          584..616
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O43150.3)"
     Site            order(586,590..591,594,598..599,601..602,606,609,618,620,
                     622,626..627,630..632,634..635,639,642,651,653,655,
                     659..660,663..665,667..668,672,675)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          586..618
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          620..651
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          620..649
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O43150.3)"
     Region          701..720
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43150.3)"
     Site            701
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43150.3)"
     Region          764..916
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43150.3)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O43150.3)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O43150.3)"
     Region          948..1003
                     /region_name="SH3_ASAP2"
                     /note="Src homology 3 domain of ArfGAP with SH3 domain,
                     ankyrin repeat and PH domain containing protein 2;
                     cd11966"
                     /db_xref="CDD:212899"
     Site            order(953,955,958,962,980..981,997,999..1000)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212899"
     CDS             1..1006
                     /gene="ASAP2"
                     /gene_synonym="AMAP2; CENTB3; DDEF2; PAG3; PAP; Pap-alpha;
                     SHAG1"
                     /coded_by="NM_003887.3:294..3314"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1661.1"
                     /db_xref="GeneID:8853"
                     /db_xref="HGNC:HGNC:2721"
                     /db_xref="MIM:603817"
ORIGIN      
        1 mpdqisvsef vaethedyka ptassfttrt aqcrntvaai eealdvdrmv lykmkksvka
       61 inssglahve neeqytqale kfggncvcrd dpdlgsaflk fsvftkelta lfknliqnmn
      121 niisfpldsl lkgdlkgvkg dlkkpfdkaw kdyetkitki ekekkehakl hgmirteisg
      181 aeiaeemeke rrffqlqmce yllkvneiki kkgvdllqnl ikyfhaqcnf fqdglkaves
      241 lkpsietlst dlhtikqaqd eerrqliqlr dilksalqve qkedsqirqs tayslhqpqg
      301 nkehgterng slykksdgir kvwqkrkcsv kngfltishg tanrppakln lltcqvktnp
      361 eekkcfdlis hdrtyhfqae deqecqiwms vlqnskeeal nnafkgddnt gennivqelt
      421 keiisevqrm tgndvccdcg apdptwlstn lgiltciecs gihrelgvhy srmqsltldv
      481 lgtselllak nignagfnei mecclpaeds vkpnpgsdmn arkdyitaky ierryarkkh
      541 adnaaklhsl ceavktrdif gllqayadgv dltekiplan ghepdetalh lavrsvdrts
      601 lhivdflvqn sgnldkqtgk gstalhyccl tdnaeclkll lrgkasieia nesgetpldi
      661 akrlkhehce elltqalsgr fnshvhveye wrllhedlde sdddmdeklq pspnrredrp
      721 isfyqlgsnq lqsnavslar daanlakekq rafmpsilqn etygallsgs pppaqpaaps
      781 ttsapplppr nvgkvqtass antlwktnsv svdggsrqrs ssdppavhpp lpplrvtstn
      841 pltptppppv aktpsvmeal sqpskpappg isqirppplp pqppsrlpqk kpapgadkst
      901 pltnkgqprg pvdlsateal gplsnamvlq ppapmprksq atklkpkrvk alyncvadnp
      961 deltfsegdv iivdgeedqe wwighidgdp grkgafpvsf vhfiad
//
LOCUS       NP_997195                450 aa            linear   PRI 27-APR-2025
DEFINITION  tubulin alpha-3E chain [Homo sapiens].
ACCESSION   NP_997195
VERSION     NP_997195.2
DBSOURCE    REFSEQ: accession NM_207312.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Alazami,A.M., Patel,N., Shamseldin,H.E., Anazi,S., Al-Dosari,M.S.,
            Alzahrani,F., Hijazi,H., Alshammari,M., Aldahmesh,M.A., Salih,M.A.,
            Faqeih,E., Alhashem,A., Bashiri,F.A., Al-Owain,M., Kentab,A.Y.,
            Sogaty,S., Al Tala,S., Temsah,M.H., Tulbah,M., Aljelaify,R.F.,
            Alshahwan,S.A., Seidahmed,M.Z., Alhadid,A.A., Aldhalaan,H.,
            AlQallaf,F., Kurdi,W., Alfadhel,M., Babay,Z., Alsogheer,M.,
            Kaya,N., Al-Hassnan,Z.N., Abdel-Salam,G.M., Al-Sannaa,N., Al
            Mutairi,F., El Khashab,H.Y., Bohlega,S., Jia,X., Nguyen,H.C.,
            Hammami,R., Adly,N., Mohamed,J.Y., Abdulwahab,F., Ibrahim,N.,
            Naim,E.A., Al-Younes,B., Meyer,B.F., Hashem,M., Shaheen,R.,
            Xiong,Y., Abouelhoda,M., Aldeeri,A.A., Monies,D.M. and
            Alkuraya,F.S.
  TITLE     Accelerating novel candidate gene discovery in neurogenetic
            disorders via whole-exome sequencing of prescreened multiplex
            consanguineous families
  JOURNAL   Cell Rep 10 (2), 148-161 (2015)
   PUBMED   25558065
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Masliah,E., Dumaop,W., Galasko,D. and Desplats,P.
  TITLE     Distinctive patterns of DNA methylation associated with Parkinson
            disease: identification of concordant epigenetic changes in brain
            and peripheral blood leukocytes
  JOURNAL   Epigenetics 8 (10), 1030-1038 (2013)
   PUBMED   23907097
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018804.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_997195.1.
            
            Summary: Microtubules of the eukaryotic cytoskeleton perform
            essential and diverse functions and are composed of a heterodimer
            of alpha and beta tubulin. The genes encoding these microtubule
            constituents are part of the tubulin superfamily, which is composed
            of six distinct families. Genes from the alpha, beta and gamma
            tubulin families are found in all eukaryotes. The alpha and beta
            tubulins represent the major components of microtubules, while
            gamma tubulin plays a critical role in the nucleation of
            microtubule assembly. This gene encodes an alpha tubulin that
            highly conserved among species. A missense mutation in this gene
            has been potentially linked to microlissencephaly and global
            developmental delay. [provided by RefSeq, Jul 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057811.1, SRR5189667.146939.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149178, SAMEA2158188
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312988.9/ ENSP00000318197.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.1"
     Protein         1..450
                     /product="tubulin alpha-3E chain"
                     /calculated_mol_wt=49728
     mat_peptide     1..449
                     /product="Detyrosinated tubulin alpha-3E chain.
                     /evidence=ECO:0000305|PubMed:25908662,
                     ECO:0000305|PubMed:29146869. /id=PRO_0000437400"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PEY2.2)"
                     /calculated_mol_wt=49696
     Region          1..440
                     /region_name="PTZ00335"
                     /note="tubulin alpha chain; Provisional"
                     /db_xref="CDD:185562"
     Region          1..4
                     /region_name="MREC motif.
                     /evidence=ECO:0000250|UniProtKB:P68363"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PEY2.2)"
     Site            40
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24906155; propagated from
                     UniProtKB/Swiss-Prot (Q6PEY2.2)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P68373; propagated from
                     UniProtKB/Swiss-Prot (Q6PEY2.2)"
     Site            450
                     /site_type="other"
                     /note="Involved in polymerization. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q6PEY2.2)"
     CDS             1..450
                     /gene="TUBA3E"
                     /coded_by="NM_207312.3:80..1432"
                     /db_xref="CCDS:CCDS2158.1"
                     /db_xref="GeneID:112714"
                     /db_xref="HGNC:HGNC:20765"
                     /db_xref="MIM:619918"
ORIGIN      
        1 mrecisihvg qagvqignac welyclehgi qpdgqmpsdk tigggddsfn tffsetgagk
       61 hvpravfvdl eptvvdevrt gtyrqlfhpe qlitgkedaa snyarghyti gkeivdlvld
      121 rirkladlct glqgflifhs fgggtgsgfa sllmerlsvd yskksklefa iypapqvsta
      181 vvepynsilt thttlehsdc afmvdneaiy dicrrnldie rptytnlnrl igqivssita
      241 slrfdgalnv dltefqtnlv pyprihfpla tyapvisaek ayheqlsvae itnacfepan
      301 qmvkcdprhg kymaccmlyr gdvvpkdvna aiatiktkrt iqfvdwcptg fkvginyqpp
      361 tvvpggdlak vqravcmlsn ttaiaeawar lvhkfdlmya kwafvhwyvg egmeegefse
      421 aredlaalek dceevgvdsv eaeaeegeay
//
LOCUS       NP_001353275             249 aa            linear   PRI 27-APR-2025
DEFINITION  androgen-induced gene 1 protein isoform h [Homo sapiens].
ACCESSION   NP_001353275 XP_016866416
VERSION     NP_001353275.1
DBSOURCE    REFSEQ: accession NM_001366346.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Nakada-Tsukui,K., Sekizuka,T., Sato-Ebine,E., Escueta-de Cadiz,A.,
            Ji,D.D., Tomii,K., Kuroda,M. and Nozaki,T.
  TITLE     AIG1 affects in vitro and in vivo virulence in clinical isolates of
            Entamoeba histolytica
  JOURNAL   PLoS Pathog 14 (3), e1006882 (2018)
   PUBMED   29554130
  REMARK    GeneRIF: High AIG1 expression is associated with virulence in
            clinical isolates of Entamoeba histolytica.
            Erratum:[PLoS Pathog. 2018 May 31;14(5):e1007091. doi:
            10.1371/journal.ppat.1007091. PMID: 29851996]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Parsons,W.H., Kolar,M.J., Kamat,S.S., Cognetta,A.B. 3rd,
            Hulce,J.J., Saez,E., Kahn,B.B., Saghatelian,A. and Cravatt,B.F.
  TITLE     AIG1 and ADTRP are atypical integral membrane hydrolases that
            degrade bioactive FAHFAs
  JOURNAL   Nat Chem Biol 12 (5), 367-372 (2016)
   PUBMED   27018888
  REMARK    GeneRIF: These results indicate that AIG1 and ADTRP are founding
            members of an evolutionarily conserved class of transmembrane
            threonine hydrolases involved in bioactive lipid metabolism.
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Wu,G., Sun,M., Zhang,W. and Huo,K.
  TITLE     AIG1 is a novel Pirh2-interacting protein that activates the NFAT
            signaling pathway
  JOURNAL   Front Biosci (Elite Ed) 3 (3), 834-842 (2011)
   PUBMED   21622095
  REMARK    GeneRIF: identified a novel Pirh2-interacting protein, AIG1, by
            yeast two-hybrid screening and confirmed its interaction with p53
            both in vitro and in vivo
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   8  (residues 1 to 249)
  AUTHORS   Seo,J., Kim,J. and Kim,M.
  TITLE     Cloning of androgen-inducible gene 1 (AIG1) from human dermal
            papilla cells
  JOURNAL   Mol Cells 11 (1), 35-40 (2001)
   PUBMED   11266118
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL023581.1, AL391726.8 and AL136116.11.
            
            On Oct 2, 2018 this sequence version replaced XP_016866416.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.271251.1,
                                           SRR1803616.43444.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.2"
     Protein         1..249
                     /product="androgen-induced gene 1 protein isoform h"
                     /note="androgen-induced gene 1 protein; FAHFA hydrolase
                     AIG1; fatty acid esters of hydroxy fatty acids hydrolase
                     AIG1"
                     /calculated_mol_wt=28399
     Region          12..219
                     /region_name="Far-17a_AIG1"
                     /note="FAR-17a/AIG1-like protein; pfam04750"
                     /db_xref="CDD:428104"
     Site            13..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVV5.3)"
     Site            43
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000269|PubMed:27018888; propagated from
                     UniProtKB/Swiss-Prot (Q9NVV5.3)"
     Site            45..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVV5.3)"
     Site            88..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVV5.3)"
     Site            125..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVV5.3)"
     Site            134
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000269|PubMed:27018888; propagated from
                     UniProtKB/Swiss-Prot (Q9NVV5.3)"
     Site            157..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVV5.3)"
     Site            194..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVV5.3)"
     CDS             1..249
                     /gene="AIG1"
                     /gene_synonym="AIG-1; dJ95L4.1"
                     /coded_by="NM_001366346.1:38..787"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="GeneID:51390"
                     /db_xref="HGNC:HGNC:21607"
                     /db_xref="MIM:608514"
ORIGIN      
        1 malvpcqvlr maillsycsi lcnykaiemp shqtyggswk fltfidlviq avffgicvlt
       61 dlsslltrgs gnqeqerqlk klislrdwml avlafpvgvf vvavfwiiya ydremiypkl
      121 ldnfipgwln hgmhttvlpf iliemrtshh qypsrssglt aictfsvgyi lwvcwvhhvt
      181 gmwvypfleh igpgariiff gsttilmnfl yllgevlnny iwdtqkscaf gsaaiwqyes
      241 lksrgpelf
//
LOCUS       NP_683694                125 aa            linear   PRI 27-APR-2025
DEFINITION  neuropeptide B preproprotein [Homo sapiens].
ACCESSION   NP_683694 XP_939571
VERSION     NP_683694.1
DBSOURCE    REFSEQ: accession NM_148896.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Patra,M.C., Maharana,J., Pradhan,S.K. and Rath,S.N.
  TITLE     Molecular dynamics simulation of neuropeptide B and neuropeptide W
            in the dipalmitoylphosphatidylcholine membrane bilayer
  JOURNAL   J Biomol Struct Dyn 32 (7), 1118-1131 (2014)
   PUBMED   23815761
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Sakurai,T.
  TITLE     NPBWR1 and NPBWR2: Implications in Energy Homeostasis, Pain, and
            Emotion
  JOURNAL   Front Endocrinol (Lausanne) 4, 23 (2013)
   PUBMED   23515889
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Kanesaka,M., Matsuda,M., Hirano,A., Tanaka,K., Kanatani,A. and
            Tokita,S.
  TITLE     Development of a potent and selective GPR7 (NPBW1) agonist: a
            systematic structure-activity study of neuropeptide B
  JOURNAL   J Pept Sci 13 (6), 379-385 (2007)
   PUBMED   17486669
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Singh,G. and Davenport,A.P.
  TITLE     Neuropeptide B and W: neurotransmitters in an emerging
            G-protein-coupled receptor system
  JOURNAL   Br J Pharmacol 148 (8), 1033-1041 (2006)
   PUBMED   16847439
  REMARK    Review article
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Andreis,P.G., Rucinski,M., Neri,G., Conconi,M.T., Petrelli,L.,
            Parnigotto,P.P., Malendowicz,L.K. and Nussdorfer,G.G.
  TITLE     Neuropeptides B and W enhance the growth of human adrenocortical
            carcinoma-derived NCI-H295 cells by exerting MAPK p42/p44-mediated
            proliferogenic and antiapoptotic effects
  JOURNAL   Int J Mol Med 16 (6), 1021-1028 (2005)
   PUBMED   16273281
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Lucyk,S., Miskolzie,M. and Kotovych,G.
  TITLE     NMR conformational analyses on (des-bromo) neuropeptide B [1-23]
            and neuropeptide W [1-23]: the importance of alpha-helices, a
            cation-pi interaction and a beta-turn
  JOURNAL   J Biomol Struct Dyn 23 (1), 77-90 (2005)
   PUBMED   15918679
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Tanaka,H., Yoshida,T., Miyamoto,N., Motoike,T., Kurosu,H.,
            Shibata,K., Yamanaka,A., Williams,S.C., Richardson,J.A.,
            Tsujino,N., Garry,M.G., Lerner,M.R., King,D.S., O'Dowd,B.F.,
            Sakurai,T. and Yanagisawa,M.
  TITLE     Characterization of a family of endogenous neuropeptide ligands for
            the G protein-coupled receptors GPR7 and GPR8
  JOURNAL   Proc Natl Acad Sci U S A 100 (10), 6251-6256 (2003)
   PUBMED   12719537
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Davenport,A.P.
  TITLE     Peptide and trace amine orphan receptors: prospects for new
            therapeutic targets
  JOURNAL   Curr Opin Pharmacol 3 (2), 127-134 (2003)
   PUBMED   12681233
  REMARK    Review article
REFERENCE   9  (residues 1 to 125)
  AUTHORS   Brezillon,S., Lannoy,V., Franssen,J.D., Le Poul,E., Dupriez,V.,
            Lucchetti,J., Detheux,M. and Parmentier,M.
  TITLE     Identification of natural ligands for the orphan G protein-coupled
            receptors GPR7 and GPR8
  JOURNAL   J Biol Chem 278 (2), 776-783 (2003)
   PUBMED   12401809
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Fujii,R., Yoshida,H., Fukusumi,S., Habata,Y., Hosoya,M.,
            Kawamata,Y., Yano,T., Hinuma,S., Kitada,C., Asami,T., Mori,M.,
            Fujisawa,Y. and Fujino,M.
  TITLE     Identification of a neuropeptide modified with bromine as an
            endogenous ligand for GPR7
  JOURNAL   J Biol Chem 277 (37), 34010-34016 (2002)
   PUBMED   12118011
  REMARK    GeneRIF: identified a neuropeptide modified with bromine; an
            endogenous ligand for GPR7
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC126128.1 and BM978256.1.
            
            On Jul 9, 2009 this sequence version replaced XP_939571.1.
            
            Summary: This gene encodes a member of the neuropeptide B/W family
            of proteins and preproprotein that is proteolytically processed to
            generate multiple protein products. The encoded products include
            neuropeptide B-23 and a C-terminally extended form, neuropeptide
            B-29, which are characterized by an N-terminal brominated
            tryptophan amino acid. Both of the encoded peptides bind with
            higher affinity to neuropeptide B/W (NPB/W) receptor 1 compared to
            the related NPB/W receptor 2. These peptides may regulate feeding,
            pain perception, and stress in rodents. [provided by RefSeq, Jul
            2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM978256.1, SRR1803612.301958.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000333383.8/ ENSP00000332766.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..125
                     /product="neuropeptide B preproprotein"
                     /note="preproneuropeptide B; preproprotein L7; prepro-NPB"
                     /calculated_mol_wt=10835
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2280
     Region          20..124
                     /region_name="NPBW"
                     /note="Neuropeptides B and W; pfam15180"
                     /db_xref="CDD:464547"
     mat_peptide     25..53
                     /product="Neuropeptide B-29. /id=PRO_0000019836"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NG41.1)"
                     /calculated_mol_wt=3079
     mat_peptide     25..48
                     /product="Neuropeptide B-23. /id=PRO_0000019837"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NG41.1)"
                     /calculated_mol_wt=2505
     Region          54..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NG41.1)"
     CDS             1..125
                     /gene="NPB"
                     /gene_synonym="L7; PPL7; PPNPB"
                     /coded_by="NM_148896.5:41..418"
                     /db_xref="CCDS:CCDS11790.1"
                     /db_xref="GeneID:256933"
                     /db_xref="HGNC:HGNC:30099"
                     /db_xref="MIM:607996"
ORIGIN      
        1 marsatlaaa alalclllap pglawykpaa ghssysvgra agllsglrrs pyarrsqpyr
       61 gaeppggaga spelqlhprl rslavcvqdv apnlqrcerl pdgrgtyqck anvflslraa
      121 dclaa
//
LOCUS       NP_001131147             689 aa            linear   PRI 27-APR-2025
DEFINITION  ataxin-1-like [Homo sapiens].
ACCESSION   NP_001131147 XP_933557
VERSION     NP_001131147.1
DBSOURCE    REFSEQ: accession NM_001137675.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Wong,D., Sogerer,L., Lee,S.S., Wong,V., Lum,A., Levine,A.B.,
            Marra,M.A. and Yip,S.
  TITLE     TRIM25 promotes Capicua degradation independently of ERK in the
            absence of ATXN1L
  JOURNAL   BMC Biol 18 (1), 154 (2020)
   PUBMED   33115448
  REMARK    GeneRIF: TRIM25 promotes Capicua degradation independently of ERK
            in the absence of ATXN1L.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 689)
  AUTHORS   Wong,D., Lounsbury,K., Lum,A., Song,J., Chan,S., LeBlanc,V.,
            Chittaranjan,S., Marra,M. and Yip,S.
  TITLE     Transcriptomic analysis of CIC and ATXN1L reveal a functional
            relationship exploited by cancer
  JOURNAL   Oncogene 38 (2), 273-290 (2019)
   PUBMED   30093628
  REMARK    GeneRIF: This study highlights the CIC-ATXN1-ATXN1L axis as a more
            potent regulator of the cell cycle than previously appreciated
REFERENCE   4  (residues 1 to 689)
  AUTHORS   Wang,B., Krall,E.B., Aguirre,A.J., Kim,M., Widlund,H.R.,
            Doshi,M.B., Sicinska,E., Sulahian,R., Goodale,A., Cowley,G.S.,
            Piccioni,F., Doench,J.G., Root,D.E. and Hahn,W.C.
  TITLE     ATXN1L, CIC, and ETS Transcription Factors Modulate Sensitivity to
            MAPK Pathway Inhibition
  JOURNAL   Cell Rep 18 (6), 1543-1557 (2017)
   PUBMED   28178529
  REMARK    GeneRIF: The ATXN1L-CIC-ETS transcription factor axis as a mediator
            of resistance to MAPKi.
REFERENCE   5  (residues 1 to 689)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 689)
  AUTHORS   Tong,X., Gui,H., Jin,F., Heck,B.W., Lin,P., Ma,J., Fondell,J.D. and
            Tsai,C.C.
  TITLE     Ataxin-1 and Brother of ataxin-1 are components of the Notch
            signalling pathway
  JOURNAL   EMBO Rep 12 (5), 428-435 (2011)
   PUBMED   21475249
  REMARK    GeneRIF: Both ATXN1 and BOAT1 bind to the promoter region of Hey1
            and inhibit the transcriptional output of Notch through direct
            interactions with CBF1, a transcription factor that is crucial for
            the Notch pathway.
REFERENCE   7  (residues 1 to 689)
  AUTHORS   Bowman,A.B., Lam,Y.C., Jafar-Nejad,P., Chen,H.K., Richman,R.,
            Samaco,R.C., Fryer,J.D., Kahle,J.J., Orr,H.T. and Zoghbi,H.Y.
  TITLE     Duplication of Atxn1l suppresses SCA1 neuropathology by decreasing
            incorporation of polyglutamine-expanded ataxin-1 into native
            complexes
  JOURNAL   Nat Genet 39 (3), 373-379 (2007)
   PUBMED   17322884
REFERENCE   8  (residues 1 to 689)
  AUTHORS   Mizutani,A., Wang,L., Rajan,H., Vig,P.J., Alaynick,W.A.,
            Thaler,J.P. and Tsai,C.C.
  TITLE     Boat, an AXH domain protein, suppresses the cytotoxicity of mutant
            ataxin-1
  JOURNAL   EMBO J 24 (18), 3339-3351 (2005)
   PUBMED   16121196
  REMARK    GeneRIF: Boat is an in vivo binding partner of ataxin-1 whose
            altered expression in Purkinje cells may contribute to their
            degeneration in causes spinocerebellar ataxia type 1 animals
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010653.10, DB097328.1 and AI720164.1.
            
            On Nov 13, 2008 this sequence version replaced XP_933557.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB621810.1, ERR279876.3977.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000427980.7/ ENSP00000415822.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.2"
     Protein         1..689
                     /product="ataxin-1-like"
                     /note="brother of ataxin-1; brother of ATXN1"
                     /calculated_mol_wt=73175
     Region          1..>253
                     /region_name="ATXN-1_C"
                     /note="Ataxin-1 like family; pfam12547"
                     /db_xref="CDD:463627"
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C7T5.1)"
     Region          20..197
                     /region_name="Interaction with NCOR2 and ATXN1.
                     /evidence=ECO:0000269|PubMed:16121196"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C7T5.1)"
     Region          20..197
                     /region_name="Self-association"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C7T5.1)"
     Region          <86..432
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          185..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C7T5.1)"
     Region          242..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C7T5.1)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P0C7T5.1)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P0C7T5.1)"
     Region          357..405
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C7T5.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P0C7T5.1)"
     Region          469..582
                     /region_name="AXH"
                     /note="Ataxin-1 and HBP1 module (AXH); pfam08517"
                     /db_xref="CDD:462505"
     Site            615
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P0C7T5.1)"
     Region          617..647
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C7T5.1)"
     CDS             1..689
                     /gene="ATXN1L"
                     /gene_synonym="BOAT; BOAT1"
                     /coded_by="NM_001137675.4:309..2378"
                     /db_xref="CCDS:CCDS45523.1"
                     /db_xref="GeneID:342371"
                     /db_xref="HGNC:HGNC:33279"
                     /db_xref="MIM:614301"
ORIGIN      
        1 mkpvhersqe clppkkrdlp vtsedmgrtt scstnhtpss dasewsrgvv vagqsqagar
       61 vslggdgaea itgltvdqyg mlykvavppa tfsptglpsv vnmsplpptf nvassliqhp
      121 gihypplhya qlpstslqfi gspyslpyav ppnflpspll spsanlatsh lphfvpyasl
      181 laegatpppq apspahsfnk apsatspsgq lphhsstqpl dlapgrmpiy yqmsrlpagy
      241 tlhetppaga spvltpqesq saleaaaang gqrprernlv rresealdsp nskgegqglv
      301 pvvecvvdgq lfsgsqtprv evaapahrgt pdtdlevqrv vgalasqdyr vvaaqrkeep
      361 splnlshhtp dhqgegrgsa rnpaelaeks qargfypqsh qepvkhrplp kamvvangnl
      421 vptgtdsgll pvgseilvas sldvqaratf pdkeptpppi tsshlpshfm kgaiiqlatg
      481 elkrvedlqt qdfvrsaevs gglkidsstv vdiqesqwpg fvmlhfvvge qqskvsievp
      541 pehpffvygq gwsscspgrt tqlfslpchr lqvgdvcisi slqslnsnsv sqascappsq
      601 lgpprerper tvlgsrelcd segksqpage gsrvvepsqp esgaqacwpa psfqrysmqg
      661 eearaallrp sfipqevkls iegrsnagk
//
LOCUS       NP_115820               1834 aa            linear   PRI 27-APR-2025
DEFINITION  structure-specific endonuclease subunit SLX4 [Homo sapiens].
ACCESSION   NP_115820 XP_375298
VERSION     NP_115820.2
DBSOURCE    REFSEQ: accession NM_032444.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1834)
  AUTHORS   Kim,S., Park,S.H., Kang,N., Ra,J.S., Myung,K. and Lee,K.Y.
  TITLE     Polyubiquitinated PCNA triggers SLX4-mediated break-induced
            replication in alternative lengthening of telomeres (ALT) cancer
            cells
  JOURNAL   Nucleic Acids Res 52 (19), 11785-11805 (2024)
   PUBMED   39291733
  REMARK    GeneRIF: Polyubiquitinated PCNA triggers SLX4-mediated
            break-induced replication in alternative lengthening of telomeres
            (ALT) cancer cells.
REFERENCE   2  (residues 1 to 1834)
  AUTHORS   Alghoul,E., Paloni,M., Takedachi,A., Urbach,S., Barducci,A.,
            Gaillard,P.H., Basbous,J. and Constantinou,A.
  TITLE     Compartmentalization of the SUMO/RNF4 pathway by SLX4 drives DNA
            repair
  JOURNAL   Mol Cell 83 (10), 1640-1658 (2023)
   PUBMED   37059091
  REMARK    GeneRIF: Compartmentalization of the SUMO/RNF4 pathway by SLX4
            drives DNA repair.
REFERENCE   3  (residues 1 to 1834)
  AUTHORS   Katsuki,Y., Abe,M., Park,S.Y., Wu,W., Yabe,H., Yabe,M., van
            Attikum,H., Nakada,S., Ohta,T., Seidman,M.M., Kim,Y. and Takata,M.
  TITLE     RNF168 E3 ligase participates in ubiquitin signaling and
            recruitment of SLX4 during DNA crosslink repair
  JOURNAL   Cell Rep 37 (4), 109879 (2021)
   PUBMED   34706224
  REMARK    GeneRIF: RNF168 E3 ligase participates in ubiquitin signaling and
            recruitment of SLX4 during DNA crosslink repair.
REFERENCE   4  (residues 1 to 1834)
  AUTHORS   Wu,X. and Wang,B.
  TITLE     Abraxas suppresses DNA end resection and limits break-induced
            replication by controlling SLX4/MUS81 chromatin loading in response
            to TOP1 inhibitor-induced DNA damage
  JOURNAL   Nat Commun 12 (1), 4373 (2021)
   PUBMED   34272385
  REMARK    GeneRIF: Abraxas suppresses DNA end resection and limits
            break-induced replication by controlling SLX4/MUS81 chromatin
            loading in response to TOP1 inhibitor-induced DNA damage.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1834)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1834)
  AUTHORS   Fekairi,S., Scaglione,S., Chahwan,C., Taylor,E.R., Tissier,A.,
            Coulon,S., Dong,M.Q., Ruse,C., Yates,J.R. 3rd, Russell,P.,
            Fuchs,R.P., McGowan,C.H. and Gaillard,P.H.L.
  TITLE     Human SLX4 is a Holliday junction resolvase subunit that binds
            multiple DNA repair/recombination endonucleases
  JOURNAL   Cell 138 (1), 78-89 (2009)
   PUBMED   19596236
  REMARK    GeneRIF: Study reports the identification of Slx4 orthologs in
            metazoa, including fly MUS312, essential for meiotic recombination,
            and human BTBD12, an ATM/ATR checkpoint kinase.
            GeneRIF: show that SLX4 binds the XPF(ERCC4) and MUS81 subunits of
            the XPF-ERCC1 and MUS81-EME1 endonucleases and is required for DNA
            interstrand crosslink repair.
REFERENCE   7  (residues 1 to 1834)
  AUTHORS   Svendsen,J.M., Smogorzewska,A., Sowa,M.E., O'Connell,B.C.,
            Gygi,S.P., Elledge,S.J. and Harper,J.W.
  TITLE     Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and
            is required for DNA repair
  JOURNAL   Cell 138 (1), 63-77 (2009)
   PUBMED   19596235
  REMARK    GeneRIF: BTBD12/SLX4 was identified as the human ortholog of yeast
            DNA repair factor Slx4p and Drosophila MUS312; SLX4 assembles a
            modular toolkit for repair of specific types of DNA lesions and is
            critical for cellular responses to replication fork failure.
REFERENCE   8  (residues 1 to 1834)
  AUTHORS   Andersen,S.L., Bergstralh,D.T., Kohl,K.P., LaRocque,J.R.,
            Moore,C.B. and Sekelsky,J.
  TITLE     Drosophila MUS312 and the vertebrate ortholog BTBD12 interact with
            DNA structure-specific endonucleases in DNA repair and
            recombination
  JOURNAL   Mol Cell 35 (1), 128-135 (2009)
   PUBMED   19595722
  REMARK    GeneRIF: Genetic and biochemical evidence suggest that MUS312 and
            BTBD12 direct Holliday junction resolution by at least two distinct
            endonucleases in different recombination and repair contexts.
REFERENCE   9  (residues 1 to 1834)
  AUTHORS   Munoz,I.M., Hain,K., Declais,A.C., Gardiner,M., Toh,G.W.,
            Sanchez-Pulido,L., Heuckmann,J.M., Toth,R., Macartney,T.,
            Eppink,B., Kanaar,R., Ponting,C.P., Lilley,D.M. and Rouse,J.
  TITLE     Coordination of structure-specific nucleases by human SLX4/BTBD12
            is required for DNA repair
  JOURNAL   Mol Cell 35 (1), 116-127 (2009)
   PUBMED   19595721
REFERENCE   10 (residues 1 to 1834)
  AUTHORS   Mehta,P.A. and Ebens,C.
  TITLE     Fanconi Anemia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301575
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY246029.1, BM541728.1,
            BE887716.1, BC029952.1, AI380342.1, DA242337.1, HY050233.1,
            AA279053.1, AK095411.1, AC006111.4 and AL442083.1.
            
            On or before May 14, 2005 this sequence version replaced
            XP_375298.2, NP_115820.1.
            
            Summary: This gene encodes a protein that functions as an assembly
            component of multiple structure-specific endonucleases. These
            endonuclease complexes are required for repair of specific types of
            DNA lesions and critical for cellular responses to replication fork
            failure. Mutations in this gene were found in patients with Fanconi
            anemia. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000294008.4/ ENSP00000294008.3
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1834
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..1834
                     /product="structure-specific endonuclease subunit SLX4"
                     /note="BTB/POZ domain-containing protein 12"
                     /calculated_mol_wt=199882
     Region          1..669
                     /region_name="Interaction with SLX4IP, ERCC4/XPF and MSH2.
                     /evidence=ECO:0000269|PubMed:19596235"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          24..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          69..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          376..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          452..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          561..610
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          673..787
                     /region_name="BTB_POZ_BTBD12_SLX4"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in
                     Structure-specific endonuclease subunit SLX4; cd18288"
                     /db_xref="CDD:349597"
     Region          684..1834
                     /region_name="Interaction with PLK1 and TERF2-TERF2IP.
                     /evidence=ECO:0000269|PubMed:19596235"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          826..846
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          902..1151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            1028
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            1044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P1D7; propagated from
                     UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P1D7; propagated from
                     UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            1185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          1195..1504
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          1328..1648
                     /region_name="Interaction with MUS81"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            1464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P1D7; propagated from
                     UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            1469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          1516..1564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          1556..1605
                     /region_name="SAP_SLX4"
                     /note="SAP domain of structure-specific endonuclease
                     subunit SLX4 and similar proteins; cd22999"
                     /db_xref="CDD:439380"
     Site            order(1558,1560..1563,1565,1579..1584,1594,1597..1598,
                     1600..1605)
                     /site_type="other"
                     /note="MUS81 interaction site [polypeptide binding]"
                     /db_xref="CDD:439380"
     Region          1605..1746
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Site            1610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P1D7; propagated from
                     UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          1632..1834
                     /region_name="Interaction with SLX1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY92.3)"
     Region          1754..1810
                     /region_name="Slx4"
                     /note="Slx4 endonuclease; pfam09494"
                     /db_xref="CDD:430644"
     CDS             1..1834
                     /gene="SLX4"
                     /gene_synonym="BTBD12; FANCP; MUS312"
                     /coded_by="NM_032444.4:650..6154"
                     /db_xref="CCDS:CCDS10506.2"
                     /db_xref="GeneID:84464"
                     /db_xref="HGNC:HGNC:23845"
                     /db_xref="MIM:613278"
ORIGIN      
        1 mklsvneaql gfylgslshl sacpgidprs sedqpeslkt gqmmdesded fkelcasffq
       61 rvkkhgikev sgerktqkaa sngtqirskl krtkqtatkt ktlqgpaekk ppsgsqaprt
      121 kkqrvtkwqa sepahsvnge ggvlasapdp pvlretaqnt qtgnqqepsp nlsrektren
      181 vpnsdsqppp sclttavpsp skprtaqlvl qrmqqfkrad perlrhasee csleaareen
      241 vpkdpqeemm agnvyglgpp apesdaaval tlqqefarvg asahddslee kglffcqicq
      301 knlsamnvtr reqhvnrcld eaektlrpsv pqipecpicg kpfltlksrt shlkqcavkm
      361 evgpqlllqa vrlqtaqpeg sssppmfsfs dhsrglkrrg ptskkeprkr rkvdeapsed
      421 llvamalsrs emepgaavpa lrlesafser irpeaenksr kkkppvsppl llvqdsettg
      481 rqiedrvall lseevelsst pplpasrilk egweragqcp ppperkqsfl wegsaltgaw
      541 amedfytarl vpplvpqrpa qglmqepvpp lvppehsels errspalhgt ptagcgsrgp
      601 spsasqrehq alqdlvdlar eglsaspwpg sgglagsegt agldvvpggl pltgfvvpsq
      661 dkhpdrggrt llslgllvad fgamvnnphl sdvqfqtdsg evlyahkfvl yarcplliqy
      721 vnnegfsave dgvltqrvll gdvsteaart flhylytadt glppglssel sslahrfgvs
      781 elvhlceqvp iatdsegkpw eekeaences raenfqellr smwadeeeea etllkskdhe
      841 edqenvneae meeiyefaat qrkllqeera agagedadwl eggspvsgql lagvqvqkqw
      901 dkveemeple pgrdeaattw ekmgqcalpp pqgqhsgarg aeapeqeape ealghsscss
      961 psrdcqaerk egslphsdda gdyeqlfsst qgeisepsqi tsepeeqsga vrerglevsh
     1021 rlapwqaspp hpcrfllgpp qggsprgshh tsgsslstpr srggtsqvgs ptllspavps
     1081 kqkrdrsilt lskepghqkg kerrsvlecr nkgvlmfpek spsidltqsn pdhsssrsqk
     1141 sssklneede villldsdee leleqtkmks issdpleekk aleisprsce lfsiidvdad
     1201 qepsqspprs eavlqqedeg alpenrgslg rrgapwlfcd resspseast tdtswlvpat
     1261 plasrsrdcs sqtqisslrs glavqavtqh tprasvgnre gnevaqkfsv irpqtpppqt
     1321 psscltpvsp gtsdgrrqgh rspsrphpgg hphssplaph pisgdrahfs rrflkhsppg
     1381 psflnqtpag evvevgdsdd eqevashqan rsppldsdpp ipiddccwhm eplspipidh
     1441 wnlertgpls tsspsrrmne aadsrdcrsp glldttpirg scttqrklqe kssgagslgn
     1501 srpsflnsal wdvwdgeeqr ppetpppaqm psaggaqkpe gletpkganr kknlppkvpi
     1561 tpmpqysime tpvlkkeldr fgvrplpkrq mvlklkeifq ythqtldsds edesqssqpl
     1621 lqaphcqtla sqtykpsrag vhaqqeattg pgahrpkgpa ktkgprhqrk hhesitppsr
     1681 sptkeappgl nddaqipasq esvatsvdgs dsslssqsss scefgaafes ageeegegev
     1741 sasqaavqaa dtdealrcyi rskpalyqkv llyqpfelre lqaelrqngl rvssrrlldf
     1801 ldthcitftt aatrreklqg rrrqprgkkk vern
//
LOCUS       NP_955452               2590 aa            linear   PRI 27-APR-2025
DEFINITION  DNA polymerase theta [Homo sapiens].
ACCESSION   NP_955452 NP_054844
VERSION     NP_955452.3
DBSOURCE    REFSEQ: accession NM_199420.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2590)
  AUTHORS   Carvajal-Maldonado,D., Li,Y., Returan,M., Averill,A.M., Doublie,S.
            and Wood,R.D.
  TITLE     Dynamic stem-loop extension by Pol theta; and templated insertion
            during DNA repair
  JOURNAL   J Biol Chem 300 (7), 107461 (2024)
   PUBMED   38876299
  REMARK    GeneRIF: Dynamic stem-loop extension by Pol theta; and templated
            insertion during DNA repair.
REFERENCE   2  (residues 1 to 2590)
  AUTHORS   Sun,Z., Xu,Y., Shao,B., Dang,P., Hu,S., Sun,H., Chen,C., Wang,C.,
            Liu,J., Liu,Y. and Hu,J.
  TITLE     Exosomal circPOLQ promotes macrophage M2 polarization via
            activating IL-10/STAT3 axis in a colorectal cancer model
  JOURNAL   J Immunother Cancer 12 (5), e008491 (2024)
   PUBMED   38782541
  REMARK    GeneRIF: Exosomal circPOLQ promotes macrophage M2 polarization via
            activating IL-10/STAT3 axis in a colorectal cancer model.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2590)
  AUTHORS   Thomas,C., Avalos-Irving,L., Victorino,J., Green,S., Andrews,M.,
            Rodrigues,N., Ebirim,S., Mudd,A. and Towle-Weicksel,J.B.
  TITLE     Melanoma-Derived DNA Polymerase Theta Variants Exhibit Altered DNA
            Polymerase Activity
  JOURNAL   Biochemistry 63 (9), 1107-1117 (2024)
   PUBMED   38671548
  REMARK    GeneRIF: Melanoma-Derived DNA Polymerase Theta Variants Exhibit
            Altered DNA Polymerase Activity.
REFERENCE   4  (residues 1 to 2590)
  AUTHORS   Carvajal-Maldonado,D., Zahn,K., Jensen,R., Wood,R.D. and Doublie,S.
  TITLE     Human DNA polymerase theta; does not harbor intrinsic nuclease
            activity
  JOURNAL   Mol Cell 84 (8), 1394-1395 (2024)
   PUBMED   38640889
  REMARK    GeneRIF: Human DNA polymerase theta; does not harbor intrinsic
            nuclease activity.
REFERENCE   5  (residues 1 to 2590)
  AUTHORS   Peng,Y., Zheng,W., Chen,Y., Lei,X., Yang,Z., Yang,Y., Liang,W.,
            Sun,K., Li,G. and Yu,J.
  TITLE     POLQ inhibition attenuates the stemness and ferroptosis resistance
            in gastric cancer cells via downregulation of dihydroorotate
            dehydrogenase
  JOURNAL   Cell Death Dis 15 (4), 248 (2024)
   PUBMED   38575587
  REMARK    GeneRIF: POLQ inhibition attenuates the stemness and ferroptosis
            resistance in gastric cancer cells via downregulation of
            dihydroorotate dehydrogenase.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2590)
  AUTHORS   Kawamura,K., Bahar,R., Seimiya,M., Chiyo,M., Wada,A., Okada,S.,
            Hatano,M., Tokuhisa,T., Kimura,H., Watanabe,S., Honda,I.,
            Sakiyama,S., Tagawa,M. and O-Wang,J.
  TITLE     DNA polymerase theta is preferentially expressed in lymphoid
            tissues and upregulated in human cancers
  JOURNAL   Int J Cancer 109 (1), 9-16 (2004)
   PUBMED   14735462
  REMARK    GeneRIF: DNA Pol theta has a specialized function in lymphocytes
            and in tumor progression
REFERENCE   7  (residues 1 to 2590)
  AUTHORS   Seki,M., Marini,F. and Wood,R.D.
  TITLE     POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in
            human cells
  JOURNAL   Nucleic Acids Res 31 (21), 6117-6126 (2003)
   PUBMED   14576298
  REMARK    GeneRIF: the isolation of the full-length human DNA POLQ gene, and
            an initial characterization of its gene product, DNA polymerase
            theta
REFERENCE   8  (residues 1 to 2590)
  AUTHORS   Maga,G., Shevelev,I., Ramadan,K., Spadari,S. and Hubscher,U.
  TITLE     DNA polymerase theta purified from human cells is a high-fidelity
            enzyme
  JOURNAL   J Mol Biol 319 (2), 359-369 (2002)
   PUBMED   12051913
  REMARK    GeneRIF: DNA polymerase theta purified from human cells is a
            high-fidelity enzyme.
REFERENCE   9  (residues 1 to 2590)
  AUTHORS   Sharief,F.S., Vojta,P.J., Ropp,P.A. and Copeland,W.C.
  TITLE     Cloning and chromosomal mapping of the human DNA polymerase theta
            (POLQ), the eighth human DNA polymerase
  JOURNAL   Genomics 59 (1), 90-96 (1999)
   PUBMED   10395804
REFERENCE   10 (residues 1 to 2590)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY338826.2, AC069239.16, AB209867.1 and AC079841.10.
            
            On Apr 3, 2007 this sequence version replaced NP_955452.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript matching the
            genomic sequence was available for the full length of the gene. The
            extent of this transcript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY338826.2, AB209867.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264233.6/ ENSP00000264233.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2590
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.33"
     Protein         1..2590
                     /product="DNA polymerase theta"
                     /EC_number="2.7.7.7"
                     /EC_number="2.7.7.49"
                     /EC_number="3.6.4.12"
                     /note="polymerase (DNA directed), theta; polymerase (DNA)
                     theta; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=289489
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     Region          76..661
                     /region_name="BRR2"
                     /note="Replicative superfamily II helicase [Replication,
                     recombination and repair]; COG1204"
                     /db_xref="CDD:440817"
     Region          102..554
                     /region_name="Helicase activity. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     Region          216..219
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     Region          847..894
                     /region_name="Interaction with RAD51.
                     /evidence=ECO:0000269|PubMed:25642963"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     Site            990
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Region          1034..1060
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     Site            1289
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:37674080; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Site            1482
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:37674080; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Site            1486
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:37674080; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:37674080; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Site            1493
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:37674080; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Site            1555
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:37674080; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Site            1563
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:37674080; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Region          1594..1622
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     Site            1628
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:37674080; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Site            1635
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:37674080; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Site            1755
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PLK1.
                     /evidence=ECO:0000269|PubMed:37674080; propagated from
                     UniProtKB/Swiss-Prot (O75417.2)"
     Region          1777..1797
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     Region          1900..2085
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Region          2091..2585
                     /region_name="DNA_pol_A_theta"
                     /note="DNA polymerase theta is a low-fidelity family A
                     enzyme implicated in translesion synthesis and in somatic
                     hypermutation; cd08638"
                     /db_xref="CDD:176475"
     Region          2097..2584
                     /region_name="DNA polymerase activity.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     Region          2142..2177
                     /region_name="Loop 1.
                     /evidence=ECO:0000269|PubMed:21050863"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     Site            order(2201,2205,2208..2209,2237..2239,2241,2243..2246,
                     2330..2331,2359,2379,2383,2467,2474,2538..2540)
                     /site_type="active"
                     /db_xref="CDD:176475"
     Site            order(2201,2205,2208..2209,2237..2239,2241,2243..2246,
                     2391,2466..2467,2470,2474,2538..2540)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176475"
     Region          2257..2322
                     /region_name="Loop 2.
                     /evidence=ECO:0000269|PubMed:21050863,
                     ECO:0000269|PubMed:25643323"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     Site            order(2330..2331,2333,2359,2379,2383,2540)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176475"
     Region          2491..2535
                     /region_name="Loop 3.
                     /evidence=ECO:0000269|PubMed:21050863"
                     /note="propagated from UniProtKB/Swiss-Prot (O75417.2)"
     CDS             1..2590
                     /gene="POLQ"
                     /gene_synonym="PRO0327"
                     /coded_by="NM_199420.4:112..7884"
                     /db_xref="CCDS:CCDS33833.1"
                     /db_xref="GeneID:10721"
                     /db_xref="HGNC:HGNC:9186"
                     /db_xref="MIM:604419"
ORIGIN      
        1 mnllrrsgkr rrsesgsdsf sgsggdssas pqflsgsvls pppglgrclk aaaageckpt
       61 vpdyerdkll lanwglpkav lekyhsfgvk kmfewqaecl llgqvlegkn lvysaptsag
      121 ktlvaellil krvlemrkka lfilpfvsva kekkyylqsl fqevgikvdg ymgstspsrh
      181 fssldiavct ieranglinr lieenkmdll gmvvvdelhm lgdshrgyll ellltkicyi
      241 trksascqad lasslsnavq ivgmsatlpn lelvaswlna elyhtdfrpv pllesvkvgn
      301 siydssmklv refepmlqvk gdedhvvslc yeticdnhsv llfcpskkwc ekladiiare
      361 fynlhhqaeg lvkpsecppv ileqkellev mdqlrrlpsg ldsvlqktvp wgvafhhagl
      421 tfeerdiieg afrqglirvl aatstlssgv nlparrviir tpifggrpld iltykqmvgr
      481 agrkgvdtvg esilicknse kskgiallqg slkpvrsclq rregeevtgs miraileiiv
      541 ggvastsqdm htyaactfla asmkegkqgi qrnqesvqlg aieacvmwll enefiqstea
      601 sdgtegkvyh pthlgsatls sslspadtld ifadlqramk gfvlendlhi lylvtpmfed
      661 wttidwyrff clweklptsm krvaelvgve egflarcvkg kvvarterqh rqmaihkrff
      721 tslvlldlis evplreinqk ygcnrgqiqs lqqsaavyag mitvfsnrlg whnmelllsq
      781 fqkrltfgiq relcdlvrvs llnaqrarvl yasgfhtvad laraniveve vilknavpfk
      841 sarkavdeee eaveerrnmr tiwvtgrkgl tereaaaliv eearmilqqd lvemgvqwnp
      901 callhsstcs lthsesevke htfisqtkss ykkltsknks ntifsdsyik hspnivqdln
      961 ksrehtssfn cnfqngnqeh qtcsifrark rasldinkek pgasqnegkt sdkkvvqtfs
     1021 qktkkaplnf nsekmsrsfr swkrrkhlkr srdssplkds gacrihlqgq tlsnpslced
     1081 pftldekkte frnsgpfakn vslsgkekdn ktsfplqikq ncswnitltn dnfvehivtg
     1141 sqsknvtcqa tsvvsekgrg vaveaekine vliqngsknq nvymkhhdih pinqylrkqs
     1201 heqtstitkq kniierqmpc eavssyinrd snvtinceri klnteenkps hfqalgddis
     1261 rtvipsevlp sagafskseg qhenflnisr lqektgtytt nktknnhvsd lglvlcdfed
     1321 sfyldtqsek iiqqmatena klgakdtnla agimqkslvq qnsmnsfqke chipfpaeqh
     1381 plgatkidhl dlktvgtmkq ssdshgvdil tpespifhsp illeenglfl kknevsvtds
     1441 qlnsflqgyq tqetvkpvil lipqkrtptg vegeclpvpe tslnmsdsll fdsfsddylv
     1501 keqlpdmqmk eplpsevtsn hfsdslclqe dlikksnvne nqdthqqltc sndesiifse
     1561 mdsvqmveal dnvdifpvqe knhtvvspra lelsdpvlde hhqgdqdggd qderaekskl
     1621 tgtrqnhsfi wsgasfdlsp glqrildkvs spleneklks mtinfsslnr kntelneeqe
     1681 visnletkqv qgisfssnne vkskiemlen nanhdetssl lprkesnivd dnglipptpi
     1741 ptsaskltfp giletpvnpw ktnnvlqpge sylfgspsdi knhdlspgsr ngfkdnspis
     1801 dtsfslqlsq dglqltpass sseslsiidv asdqnlfqtf ikewrckkrf sislacekir
     1861 sltssktati gsrfkqassp qeipirddgf pikgcddtlv vglavcwggr dayyfslqke
     1921 qkhseisasl vppsldpslt lkdrmwylqs clrkesdkec svviydfiqs ykilllscgi
     1981 sleqsyedpk vacwlldpds qeptlhsivt sflphelpll egmetsqgiq slglnagseh
     2041 sgryrasves ilifnsmnql nsllqkenlq dvfrkvemps qyclalleln gigfstaece
     2101 sqkhimqakl daietqayql aghsfsftss ddiaevlfle lklppnremk nqgskktlgs
     2161 trrgidngrk lrlgrqfsts kdvlnklkal hplpglilew rritnaitkv vfplqrekcl
     2221 npflgmeriy pvsqshtatg ritftepniq nvprdfeikm ptlvgespps qavgkgllpm
     2281 grgkykkgfs vnprcqaqme eraadrgmpf sismrhafvp fpggsilaad ysqlelrila
     2341 hlshdrrliq vlntgadvfr siaaewkmie pesvgddlrq qakqicygii ygmgakslge
     2401 qmgikendaa cyidsfksry tginqfmtet vknckrdgfv qtilgrrryl pgikdnnpyr
     2461 kahaerqain tivqgsaadi vkiatvniqk qletfhstfk shghregmlq sdqtglsrkr
     2521 klqgmfcpir ggffilqlhd ellyevaeed vvqvaqivkn emesavklsv klkvkvkiga
     2581 swgelkdfdv
//
LOCUS       NP_001297769             548 aa            linear   ROD 27-APR-2025
DEFINITION  RING finger protein 214 isoform 3 [Mus musculus].
ACCESSION   NP_001297769 XP_011240806
VERSION     NP_001297769.1
DBSOURCE    REFSEQ: accession NM_001310840.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Faghihi,M.A., Modarresi,F., Khalil,A.M., Wood,D.E., Sahagan,B.G.,
            Morgan,T.E., Finch,C.E., St Laurent,G. 3rd, Kenny,P.J. and
            Wahlestedt,C.
  TITLE     Expression of a noncoding RNA is elevated in Alzheimer's disease
            and drives rapid feed-forward regulation of beta-secretase
  JOURNAL   Nat Med 14 (7), 723-730 (2008)
   PUBMED   18587408
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Carninci,P., Waki,K., Shiraki,T., Konno,H., Shibata,K., Itoh,M.,
            Aizawa,K., Arakawa,T., Ishii,Y., Sasaki,D., Bono,H., Kondo,S.,
            Sugahara,Y., Saito,R., Osato,N., Fukuda,S., Sato,K., Watahiki,A.,
            Hirozane-Kishikawa,T., Nakamura,M., Shibata,Y., Yasunishi,A.,
            Kikuchi,N., Yoshiki,A., Kusakabe,M., Gustincich,S., Beisel,K.,
            Pavan,W., Aidinis,V., Nakagawara,A., Held,W.A., Iwata,H., Kono,T.,
            Nakauchi,H., Lyons,P., Wells,C., Hume,D.A., Fagiolini,M.,
            Hensch,T.K., Brinkmeier,M., Camper,S., Hirota,J., Mombaerts,P.,
            Muramatsu,M., Okazaki,Y., Kawai,J. and Hayashizaki,Y.
  TITLE     Targeting a complex transcriptome: the construction of the mouse
            full-length cDNA encyclopedia
  JOURNAL   Genome Res 13 (6B), 1273-1289 (2003)
   PUBMED   12819125
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY785775.1, AK030208.1, AK032376.1, AK136229.1 and CJ286540.1.
            
            On Jul 21, 2015 this sequence version replaced XP_011240806.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR, uses an
            alternate in-frame splice site in the 5' coding region, and
            contains an alternate in-frame exon in the 3' coding region
            compared to variant 1. It encodes isoform 3, which is shorter than
            isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC049909.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 25.26 cM"
     Protein         1..548
                     /product="RING finger protein 214 isoform 3"
                     /calculated_mol_wt=61119
     Region          501..545
                     /region_name="RING-H2_RNF214"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 214 (RNF214) and similar proteins; cd16477"
                     /db_xref="CDD:438140"
     CDS             1..548
                     /gene="Rnf214"
                     /gene_synonym="D130054N24Rik"
                     /coded_by="NM_001310840.2:182..1828"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS80988.1"
                     /db_xref="GeneID:235315"
                     /db_xref="MGI:MGI:2444451"
ORIGIN      
        1 maasevaglg agtpspsess alcasksdes lpdglspkds aqkqknlspp stdfktadse
       61 vntdqdiekn ldkmmtertl lkeryqevld kqrqvesqlq vqlkqlqqrr eeemknhqei
      121 lkaiqdvtik reetkkkiek ekkeflqkeq dlkaeieklc ekgrrevwem eldrlknqdg
      181 einrnimeet erawkaeils lesrkellvl kleeaekeae lhltylkstp ptletvrskq
      241 ewetrlngvr imkknvrdqf nshiqlvrng aklsslpqip tptlppppse adfmlqvfqp
      301 spsltprmpf sigqvtmpmv mpsadprsls fpilnpalsq ssqpspplpg shgrnspglg
      361 slvsphgphm ppaasipppp glggikasse tprpqpvdkl ekileklltr fpqcnkaqmt
      421 nilqqiktar ttmagltmee liqlvaarla ehervasstq plgriralhp aplaqisppm
      481 flpsaqvsyp grsshapptc klclmcqklv qpselhpmac thalhkecik fwaqtntndt
      541 cpfcptlk
//
LOCUS       NP_940943                110 aa            linear   PRI 27-APR-2025
DEFINITION  insulin growth factor-like family member 1 precursor [Homo
            sapiens].
ACCESSION   NP_940943 XP_353188
VERSION     NP_940943.1
DBSOURCE    REFSEQ: accession NM_198541.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Wang,H., Shi,Y., Chen,C.H., Wen,Y., Zhou,Z., Yang,C., Sun,J.,
            Du,G., Wu,J., Mao,X., Liu,R. and Chen,C.
  TITLE     KLF5-induced lncRNA IGFL2-AS1 promotes basal-like breast cancer
            cell growth and survival by upregulating the expression of IGFL1
  JOURNAL   Cancer Lett 515, 49-62 (2021)
   PUBMED   34052325
  REMARK    GeneRIF: KLF5-induced lncRNA IGFL2-AS1 promotes basal-like breast
            cancer cell growth and survival by upregulating the expression of
            IGFL1.
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Lobito,A.A., Ramani,S.R., Tom,I., Bazan,J.F., Luis,E.,
            Fairbrother,W.J., Ouyang,W. and Gonzalez,L.C.
  TITLE     Murine insulin growth factor-like (IGFL) and human IGFL1 proteins
            are induced in inflammatory skin conditions and bind to a novel
            tumor necrosis factor receptor family member, IGFLR1
  JOURNAL   J Biol Chem 286 (21), 18969-18981 (2011)
   PUBMED   21454693
  REMARK    GeneRIF: Murine insulin growth factor-like (IGFL) and human IGFL1
            proteins are induced in inflammatory skin conditions and bind to a
            novel tumor necrosis factor receptor family member, IGFLR1.
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Ester,W.A., van Meurs,J.B., Arends,N.J., Uitterlinden,A.G., de
            Ridder,M.A. and Hokken-Koelega,A.C.
  TITLE     The -G1245A IGF1 polymorphism is related with small head size and
            less brain sparing in small for gestational age born children
  JOURNAL   Eur J Endocrinol 160 (4), 549-555 (2009)
   PUBMED   19147602
  REMARK    GeneRIF: The -1245 A-allele of the IGF1 promoter single nucleotide
            polymorphism is associated with a small head size and less brain
            sparing in small for gestational age born subjects
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Emtage,P., Vatta,P., Arterburn,M., Muller,M.W., Park,E., Boyle,B.,
            Hazell,S., Polizotto,R., Funk,W.D. and Tang,Y.T.
  TITLE     IGFL: A secreted family with conserved cysteine residues and
            similarities to the IGF superfamily
  JOURNAL   Genomics 88 (4), 513-520 (2006)
   PUBMED   16890402
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006262.2 and AY359013.1.
            
            On Dec 17, 2003 this sequence version replaced XP_353188.1.
            
            Summary: The protein encoded by this gene is a member of the
            insulin-like growth factor family of signaling molecules. The
            encoded protein is synthesized as a precursor protein and is
            proteolytically cleaved to form a secreted mature peptide. The
            mature peptide binds to a receptor, which in mouse was found on the
            cell surface of T cells. Increased expression of this gene may be
            linked to psoriasis. [provided by RefSeq, Aug 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY359013.1, DN995474.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000437936.2/ ENSP00000415823.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..110
                     /product="insulin growth factor-like family member 1
                     precursor"
                     /note="insulin growth factor-like family member 1"
                     /calculated_mol_wt=9815
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2565
     mat_peptide     25..110
                     /product="Insulin growth factor-like family member 1.
                     /id=PRO_0000044633"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UW32.1)"
                     /calculated_mol_wt=9815
     Region          34..>86
                     /region_name="IGFL"
                     /note="Insulin growth factor-like family; pfam14653"
                     /db_xref="CDD:464239"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UW32.1)"
     CDS             1..110
                     /gene="IGFL1"
                     /gene_synonym="APRG644; UNQ644"
                     /coded_by="NM_198541.2:34..366"
                     /db_xref="CCDS:CCDS46123.1"
                     /db_xref="GeneID:374918"
                     /db_xref="HGNC:HGNC:24093"
                     /db_xref="MIM:610544"
ORIGIN      
        1 maprgcivav faifcisrll cshgapvapm tpylmlcqph krcgdkfydp lqhccyddav
       61 vplartqtcg nctfrvcfeq ccpwtfmvkl inqncdsart sddrlcrsvs
//
LOCUS       NP_005106                893 aa            linear   PRI 27-APR-2025
DEFINITION  major vault protein isoform 1 [Homo sapiens].
ACCESSION   NP_005106
VERSION     NP_005106.2
DBSOURCE    REFSEQ: accession NM_005115.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Li,C., Gao,M., Zha,N. and Guo,G.
  TITLE     The prognostic value and immunological role of MVP in pan-cancer
            study
  JOURNAL   Aging (Albany NY) 16 (10), 8497-8510 (2024)
   PUBMED   38713157
  REMARK    GeneRIF: The prognostic value and immunological role of MVP in
            pan-cancer study.
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Yu,C., Zhu,Q., Ma,C., Luo,C., Nie,L., Cai,H., Wang,Q., Wang,F.,
            Ren,H., Yan,H., Xu,K., Zhou,L., Zhang,C., Lu,G., Lu,Z., Zhu,Y. and
            Liu,S.
  TITLE     Major vault protein regulates tumor-associated macrophage
            polarization through interaction with signal transducer and
            activator of transcription 6
  JOURNAL   Front Immunol 14, 1289795 (2024)
   PUBMED   38264642
  REMARK    GeneRIF: Major vault protein regulates tumor-associated macrophage
            polarization through interaction with signal transducer and
            activator of transcription 6.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Pietras,P., Lesniczak-Staszak,M., Kasprzak,A., Andrzejewska,M.,
            Jopek,K., Sowinski,M., Rucinski,M., Lyons,S.M., Ivanov,P. and
            Szaflarski,W.
  TITLE     MVP Expression Facilitates Tumor Cell Proliferation and Migration
            Supporting the Metastasis of Colorectal Cancer Cells
  JOURNAL   Int J Mol Sci 22 (22), 12121 (2021)
   PUBMED   34829999
  REMARK    GeneRIF: MVP Expression Facilitates Tumor Cell Proliferation and
            Migration Supporting the Metastasis of Colorectal Cancer Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Wang,W., Yan,T., Guo,W., Niu,J., Zhao,Z., Sun,K., Zhang,H., Yu,Y.
            and Ren,T.
  TITLE     Constitutive GLI1 expression in chondrosarcoma is regulated by
            major vault protein via mTOR/S6K1 signaling cascade
  JOURNAL   Cell Death Differ 28 (7), 2221-2237 (2021)
   PUBMED   33637972
  REMARK    GeneRIF: Constitutive GLI1 expression in chondrosarcoma is
            regulated by major vault protein via mTOR/S6K1 signaling cascade.
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Holzmann,K., Ambrosch,I., Elbling,L., Micksche,M. and Berger,W.
  TITLE     A small upstream open reading frame causes inhibition of human
            major vault protein expression from a ubiquitous mRNA splice
            variant
  JOURNAL   FEBS Lett 494 (1-2), 99-104 (2001)
   PUBMED   11297743
  REMARK    GeneRIF: MVP gene expression regulated by alternative splicing due
            to generation of an upstream open reading frame
REFERENCE   6  (residues 1 to 893)
  AUTHORS   Dingemans,A.M., van Ark-Otte,J., van der Valk,P., Apolinario,R.M.,
            Scheper,R.J., Postmus,P.E. and Giaccone,G.
  TITLE     Expression of the human major vault protein LRP in human lung
            cancer samples and normal lung tissues
  JOURNAL   Ann Oncol 7 (6), 625-630 (1996)
   PUBMED   8879378
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Izquierdo,M.A., Scheffer,G.L., Flens,M.J., Schroeijers,A.B., van
            der Valk,P. and Scheper,R.J.
  TITLE     Major vault protein LRP-related multidrug resistance
  JOURNAL   Eur J Cancer 32A (6), 979-984 (1996)
   PUBMED   8763338
  REMARK    Review article
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Izquierdo,M.A., Scheffer,G.L., Flens,M.J., Giaccone,G.,
            Broxterman,H.J., Meijer,C.J., van der Valk,P. and Scheper,R.J.
  TITLE     Broad distribution of the multidrug resistance-related vault lung
            resistance protein in normal human tissues and tumors
  JOURNAL   Am J Pathol 148 (3), 877-887 (1996)
   PUBMED   8774142
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Slovak,M.L., Ho,J.P., Cole,S.P., Deeley,R.G., Greenberger,L., de
            Vries,E.G., Broxterman,H.J., Scheffer,G.L. and Scheper,R.J.
  TITLE     The LRP gene encoding a major vault protein associated with drug
            resistance maps proximal to MRP on chromosome 16: evidence that
            chromosome breakage plays a key role in MRP or LRP gene
            amplification
  JOURNAL   Cancer Res 55 (19), 4214-4219 (1995)
   PUBMED   7671223
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Scheffer,G.L., Wijngaard,P.L., Flens,M.J., Izquierdo,M.A.,
            Slovak,M.L., Pinedo,H.M., Meijer,C.J., Clevers,H.C. and
            Scheper,R.J.
  TITLE     The drug resistance-related protein LRP is the human major vault
            protein
  JOURNAL   Nat Med 1 (6), 578-582 (1995)
   PUBMED   7585126
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA940597.1, BQ932800.1,
            BC015623.2 and BM999583.1.
            
            On Apr 3, 2002 this sequence version replaced NP_005106.1.
            
            Summary: This gene encodes the major component of the vault
            complex. Vaults are multi-subunit ribonucleoprotein structures that
            may be involved in nucleo-cytoplasmic transport. The encoded
            protein may play a role in multiple cellular processes by
            regulating the MAP kinase, JAK/STAT and phosphoinositide
            3-kinase/Akt signaling pathways. The encoded protein also plays a
            role in multidrug resistance, and expression of this gene may be a
            prognostic marker for several types of cancer. Alternatively
            spliced transcript variants have been observed for this gene.
            [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (2, also known as S-MVP) uses a
            different splice site in the 5' UTR, compared to variant 1.
            Variants 1 and 2 encode the same isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005570.1, SRR1803617.77162.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357402.10/ ENSP00000349977.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..893
                     /product="major vault protein isoform 1"
                     /note="lung resistance-related protein; testicular
                     secretory protein Li 30"
                     /calculated_mol_wt=99196
     Region          2..56
                     /region_name="MVP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          4..850
                     /region_name="PTZ00491"
                     /note="major vault protein; Provisional"
                     /db_xref="CDD:240439"
     Region          57..111
                     /region_name="MVP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          112..164
                     /region_name="MVP 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          165..217
                     /region_name="MVP 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          218..272
                     /region_name="MVP 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          273..323
                     /region_name="MVP 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          324..379
                     /region_name="MVP 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          380..457
                     /region_name="MVP 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14764.4)"
     Region          458..520
                     /region_name="MVP 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          856..893
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     CDS             1..893
                     /gene="MVP"
                     /gene_synonym="LRP; VAULT1"
                     /coded_by="NM_005115.5:85..2766"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10656.1"
                     /db_xref="GeneID:9961"
                     /db_xref="HGNC:HGNC:7531"
                     /db_xref="MIM:605088"
ORIGIN      
        1 mateefiiri ppyhyihvld qnsnvsrvev gpktyirqdn ervlfapmrm vtvpprhyct
       61 vanpvsrdaq glvlfdvtgq vrlrhadlei rlaqdpfply pgevlekdit plqvvlpnta
      121 lhlkalldfe dkdgdkvvag dewlfegpgt yiprkevevv eiiqatiirq nqalrlrark
      181 ecwdrdgker vtgeewlvtt vgaylpavfe evldlvdavi ltektalhlr arrnfrdfrg
      241 vsrrtgeewl vtvqdteahv pdvheevlgv vpittlgphn ycvildpvgp dgknqlgqkr
      301 vvkgeksffl qpgeqleqgi qdvyvlseqq glllralqpl eegedeekvs hqagdhwlir
      361 gpleyvpsak vevveerqai pldenegiyv qdvktgkvra vigstymltq devlwekelp
      421 pgveellnkg qdpladrgek dtakslqpla prnktrvvsy rvphnaavqv ydyrekrarv
      481 vfgpelvslg peeqftvlsl sagrpkrpha rralclllgp dfftdvitie tadharlqlq
      541 laynwhfevn drkdpqetak lfsvpdfvgd ackaiasrvr gavasvtfdd fhknsariir
      601 tavfgfetse akgpdgmalp rprdqavfpq nglvvssvdv qsvepvdqrt rdalqrsvql
      661 aieittnsqe aaakheaqrl eqeargrler qkildqseae karkellele alsmavestg
      721 takaeaesra eaariegegs vlqaklkaqa laieteaelq rvqkvrelel vyaraqlele
      781 vskaqqlaev evkkfkqmte aigpstirdl avagpemqvk llqslglkst litdgstpin
      841 lfntafgllg mgpegqplgr rvasgpspge gispqsaqap qapgdnhvvp vlr
//
LOCUS       NP_000512                556 aa            linear   PRI 27-APR-2025
DEFINITION  beta-hexosaminidase subunit beta isoform 1 preproprotein [Homo
            sapiens].
ACCESSION   NP_000512
VERSION     NP_000512.2
DBSOURCE    REFSEQ: accession NM_000521.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Abtahi,R., Karimzadeh,P., Rezayi,A., Salehpour,S., Akbarzadeh,D.,
            Tonekaboni,S.H., Emameh,R.Z. and Houshmand,M.
  TITLE     Analysis of the HEXA, HEXB, ARSA, and SMPD1 Genes in 68 Iranian
            Patients
  JOURNAL   J Mol Neurosci 72 (3), 555-564 (2022)
   PUBMED   34554397
  REMARK    GeneRIF: Analysis of the HEXA, HEXB, ARSA, and SMPD1 Genes in 68
            Iranian Patients.
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Tim-Aroon,T., Wichajarn,K., Katanyuwong,K., Tanpaiboon,P.,
            Vatanavicharn,N., Sakpichaisakul,K., Kongkrapan,A.,
            Eu-Ahsunthornwattana,J., Thongpradit,S., Moolsuwan,K.,
            Satproedprai,N., Mahasirimongkol,S., Lerksuthirat,T.,
            Suktitipat,B., Jinawath,N. and Wattanasirichaigoon,D.
  TITLE     Infantile onset Sandhoff disease: clinical manifestation and a
            novel common mutation in Thai patients
  JOURNAL   BMC Pediatr 21 (1), 22 (2021)
   PUBMED   33407268
  REMARK    GeneRIF: Infantile onset Sandhoff disease: clinical manifestation
            and a novel common mutation in Thai patients.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 556)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 556)
  AUTHORS   Xiao,C., Tifft,C. and Toro,C.
  TITLE     Sandhoff Disease
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35420740
REFERENCE   7  (residues 1 to 556)
  AUTHORS   Bolhuis,P.A. and Bikker,H.
  TITLE     Deletion of the 5'-region in one or two alleles of HEXB in 15 out
            of 30 patients with Sandhoff disease
  JOURNAL   Hum Genet 90 (3), 328-329 (1992)
   PUBMED   1487253
REFERENCE   8  (residues 1 to 556)
  AUTHORS   McInnes,B., Potier,M., Wakamatsu,N., Melancon,S.B., Klavins,M.H.,
            Tsuji,S. and Mahuran,D.J.
  TITLE     An unusual splicing mutation in the HEXB gene is associated with
            dramatically different phenotypes in patients from different racial
            backgrounds
  JOURNAL   J Clin Invest 90 (2), 306-314 (1992)
   PUBMED   1386607
REFERENCE   9  (residues 1 to 556)
  AUTHORS   Wakamatsu,N., Kobayashi,H., Miyatake,T. and Tsuji,S.
  TITLE     A novel exon mutation in the human beta-hexosaminidase beta subunit
            gene affects 3' splice site selection
  JOURNAL   J Biol Chem 267 (4), 2406-2413 (1992)
   PUBMED   1531140
REFERENCE   10 (residues 1 to 556)
  AUTHORS   Gilbert,F., Kucherlapati,R., Creagan,R.P., Murnane,M.J.,
            Darlington,G.J. and Ruddle,F.H.
  TITLE     Tay-Sachs' and Sandhoff's diseases: the assignment of genes for
            hexosaminidase A and B to individual human chromosomes
  JOURNAL   Proc Natl Acad Sci U S A 72 (1), 263-267 (1975)
   PUBMED   1054503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026405.5 and AC093214.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2018 this sequence version replaced NP_000512.1.
            
            Summary: Hexosaminidase B is the beta subunit of the lysosomal
            enzyme beta-hexosaminidase that, together with the cofactor GM2
            activator protein, catalyzes the degradation of the ganglioside
            GM2, and other molecules containing terminal N-acetyl hexosamines.
            Beta-hexosaminidase is composed of two subunits, alpha and beta,
            which are encoded by separate genes. Both beta-hexosaminidase alpha
            and beta subunits are members of family 20 of glycosyl hydrolases.
            Mutations in the alpha or beta subunit genes lead to an
            accumulation of GM2 ganglioside in neurons and neurodegenerative
            disorders termed the GM2 gangliosidoses. Beta subunit gene
            mutations lead to Sandhoff disease (GM2-gangliosidosis type II).
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF378118.1, SRR3476690.59226.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261416.12/ ENSP00000261416.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.3"
     Protein         1..556
                     /product="beta-hexosaminidase subunit beta isoform 1
                     preproprotein"
                     /EC_number="3.2.1.52"
                     /note="beta-hexosaminidase subunit beta; HCC-7;
                     hexosaminidase subunit B; beta-N-acetylhexosaminidase
                     subunit beta; cervical cancer proto-oncogene 7 protein;
                     N-acetyl-beta-glucosaminidase subunit beta; epididymis
                     luminal protein 248; epididymis secretory protein Li 111;
                     hexosaminidase B (beta polypeptide); beta-hexosaminidase
                     beta-subunit; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=58813
     sig_peptide     1..42
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07686.4)"
                     /calculated_mol_wt=4343
     Region          56..178
                     /region_name="Glycohydro_20b2"
                     /note="beta-acetyl hexosaminidase like; pfam14845"
                     /db_xref="CDD:434261"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:11447134,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P07686.4)"
     mat_peptide     122..556
                     /product="Beta-hexosaminidase subunit beta.
                     /id=PRO_0000012003"
                     /note="propagated from UniProtKB/Swiss-Prot (P07686.4)"
                     /calculated_mol_wt=49927
     mat_peptide     122..311
                     /product="Beta-hexosaminidase subunit beta chain B.
                     /id=PRO_0000012004"
                     /note="propagated from UniProtKB/Swiss-Prot (P07686.4)"
                     /calculated_mol_wt=21631
     Site            142
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:11447134; propagated from
                     UniProtKB/Swiss-Prot (P07686.4)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:11447134; propagated from
                     UniProtKB/Swiss-Prot (P07686.4)"
     Region          200..540
                     /region_name="GH20_HexA_HexB-like"
                     /note="Beta-N-acetylhexosaminidases catalyze the removal
                     of beta-1,4-linked N-acetyl-D-hexosamine residues from the
                     non-reducing ends of N-acetyl-beta-D-hexosaminides
                     including N-acetylglucosides and N-acetylgalactosides. The
                     hexA and hexB genes encode the...; cd06562"
                     /db_xref="CDD:119332"
     Site            order(211,240,294,354..355,405,424,450,452,489,491)
                     /site_type="active"
                     /db_xref="CDD:119332"
     mat_peptide     315..556
                     /product="Beta-hexosaminidase subunit beta chain A.
                     /id=PRO_0000012005"
                     /note="propagated from UniProtKB/Swiss-Prot (P07686.4)"
                     /calculated_mol_wt=27916
     Site            327
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:11447134,
                     ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (P07686.4)"
     Site            497
                     /site_type="other"
                     /note="Not glycosylated.
                     /evidence=ECO:0000269|PubMed:11447134; propagated from
                     UniProtKB/Swiss-Prot (P07686.4)"
     CDS             1..556
                     /gene="HEXB"
                     /gene_synonym="ENC-1AS; HEL-248; HEL-S-111"
                     /coded_by="NM_000521.4:29..1699"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4022.1"
                     /db_xref="GeneID:3074"
                     /db_xref="HGNC:HGNC:4879"
                     /db_xref="MIM:606873"
ORIGIN      
        1 melcglglpr ppmllallla tllaamlall tqvalvvqva eaarapsvsa kpgpalwplp
       61 llvkmtpnll hlapenfyis hspnstagps ctlleeafrr yhgyifgfyk whhepaefqa
      121 ktqvqqllvs itlqsecdaf pnissdesyt llvkepvavl kanrvwgalr gletfsqlvy
      181 qdsygtftin estiidsprf shrgilidts rhylpvkiil ktldamafnk fnvlhwhivd
      241 dqsfpyqsit fpelsnkgsy slshvytpnd vrmvieyarl rgirvlpefd tpghtlswgk
      301 gqkdlltpcy srqnkldsfg pinptlntty sflttffkei sevfpdqfih lggdevefkc
      361 wesnpkiqdf mrqkgfgtdf kklesfyiqk vldiiatink gsivwqevfd dkaklapgti
      421 vevwkdsayp eelsrvtasg fpvilsapwy ldlisygqdw rkyykvepld fggtqkqkql
      481 figgeaclwg eyvdatnltp rlwprasavg erlwsskdvr dmddaydrlt rhrcrmverg
      541 iaaqplyagy cnhenm
//
LOCUS       NP_001317404             131 aa            linear   PRI 27-APR-2025
DEFINITION  protein archease isoform 6 [Homo sapiens].
ACCESSION   NP_001317404 XP_016856623
VERSION     NP_001317404.1
DBSOURCE    REFSEQ: accession NM_001330475.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Mason,C.C., Khorashad,J.S., Tantravahi,S.K., Kelley,T.W.,
            Zabriskie,M.S., Yan,D., Pomicter,A.D., Reynolds,K.R., Eiring,A.M.,
            Kronenberg,Z., Sherman,R.L., Tyner,J.W., Dalley,B.K., Dao,K.H.,
            Yandell,M., Druker,B.J., Gotlib,J., O'Hare,T. and Deininger,M.W.
  TITLE     Age-related mutations and chronic myelomonocytic leukemia
  JOURNAL   Leukemia 30 (4), 906-913 (2016)
   PUBMED   26648538
  REMARK    GeneRIF: ARCH mutation is associated with chronic myelomonocytic
            leukemia.
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Jurkin,J., Henkel,T., Nielsen,A.F., Minnich,M., Popow,J.,
            Kaufmann,T., Heindl,K., Hoffmann,T., Busslinger,M. and Martinez,J.
  TITLE     The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA
            and controls antibody secretion in plasma cells
  JOURNAL   EMBO J 33 (24), 2922-2936 (2014)
   PUBMED   25378478
  REMARK    GeneRIF: RTCB, the catalytic subunit of the tRNA ligase complex,
            and its co-factor archease mediate XBP1 mRNA splicing both in vitro
            and in vivo.
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Popow,J., Jurkin,J., Schleiffer,A. and Martinez,J.
  TITLE     Analysis of orthologous groups reveals archease and DDX1 as tRNA
            splicing factors
  JOURNAL   Nature 511 (7507), 104-107 (2014)
   PUBMED   24870230
  REMARK    GeneRIF: archease (also called ZBTB8OS), a protein of unknown
            function, is required for full activity of the human tRNA ligase
            complex and, in cooperation with DDX1, facilitates the formation of
            an RTCB-guanylate intermediate central to mammalian RNA ligation
REFERENCE   6  (residues 1 to 131)
  AUTHORS   Popow,J., Englert,M., Weitzer,S., Schleiffer,A., Mierzwa,B.,
            Mechtler,K., Trowitzsch,S., Will,C.L., Luhrmann,R., Soll,D. and
            Martinez,J.
  TITLE     HSPC117 is the essential subunit of a human tRNA splicing ligase
            complex
  JOURNAL   Science 331 (6018), 760-764 (2011)
   PUBMED   21311021
REFERENCE   7  (residues 1 to 131)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 131)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2 and AL033529.25.
            
            On Aug 29, 2016 this sequence version replaced XP_016856623.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.398486.1,
                                           SRR1660809.313917.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2153733
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..131
                     /product="protein archease isoform 6"
                     /note="protein archease; archease-like protein; archease
                     (ARCH); zinc finger and BTB domain-containing opposite
                     strand protein 8"
                     /calculated_mol_wt=15128
     Region          6..131
                     /region_name="Archease"
                     /note="Archease protein family (MTH1598/TM1083);
                     pfam01951"
                     /db_xref="CDD:426527"
     CDS             1..131
                     /gene="ZBTB8OS"
                     /gene_synonym="ARCH; ARCH2"
                     /coded_by="NM_001330475.2:578..973"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS81292.1"
                     /db_xref="GeneID:339487"
                     /db_xref="HGNC:HGNC:24094"
                     /db_xref="MIM:615891"
ORIGIN      
        1 mfqswlhawg dtleeafeqc amamfgymtd tgtveplqtv evetqgddlq sllfhfldew
       61 lykfsadeff iprevkvlsi dqrnfklrsi gwgeefslsk hpqgtevkai tysamqvyne
      121 enpevfviid i
//
LOCUS       NP_001352211             227 aa            linear   PRI 27-APR-2025
DEFINITION  hydroxyacylglutathione hydrolase-like protein isoform 4 [Homo
            sapiens].
ACCESSION   NP_001352211 XP_016879263
VERSION     NP_001352211.1
DBSOURCE    REFSEQ: accession NM_001365282.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Xu,Y., Zhou,X., Gao,L., Yan,S., Li,Z., Zhang,D., Pu,J., Zou,S. and
            Mao,Z.
  TITLE     Identification of HAGHL as a novel metabolic oncogene regulating
            human colorectal cancer progression
  JOURNAL   Clin Transl Oncol 25 (4), 1033-1042 (2023)
   PUBMED   36417085
  REMARK    GeneRIF: Identification of HAGHL as a novel metabolic oncogene
            regulating human colorectal cancer progression.
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Daniels,R.J., Peden,J.F., Lloyd,C., Horsley,S.W., Clark,K.,
            Tufarelli,C., Kearney,L., Buckle,V.J., Doggett,N.A., Flint,J. and
            Higgs,D.R.
  TITLE     Sequence, structure and pathology of the fully annotated terminal 2
            Mb of the short arm of human chromosome 16
  JOURNAL   Hum Mol Genet 10 (4), 339-352 (2001)
   PUBMED   11157797
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z98258.1.
            
            On Aug 14, 2018 this sequence version replaced XP_016879263.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2154665
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..227
                     /product="hydroxyacylglutathione hydrolase-like protein
                     isoform 4"
                     /EC_number="3.1.2.6"
                     /note="hydroxyacylglutathione hydrolase-like protein;
                     GLO2-like/ RJD12"
                     /calculated_mol_wt=25054
     Region          1..226
                     /region_name="PLN02469"
                     /note="hydroxyacylglutathione hydrolase"
                     /db_xref="CDD:178088"
     CDS             1..227
                     /gene="HAGHL"
                     /coded_by="NM_001365282.1:61..744"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS92077.1"
                     /db_xref="GeneID:84264"
                     /db_xref="HGNC:HGNC:14177"
ORIGIN      
        1 mkvkvipvle dnymylviee ltreavavdv avpkrlleiv gregvsltav ltthhhwdha
       61 rgnpelarlr pglavlgade rifsltrrla hgeelrfgai hvrclltpgh taghmsyflw
      121 eddcpdppal fsgdalsvag cgsclegsaq qmyqslaelg tlppetkvfc ghehtlsnle
      181 faqkvepcnd hvraklswak krdeddvptv pstlgeerly npflrva
//
LOCUS       NP_006274                805 aa            linear   PRI 27-APR-2025
DEFINITION  transforming acidic coiled-coil-containing protein 1 isoform 1
            [Homo sapiens].
ACCESSION   NP_006274
VERSION     NP_006274.2
DBSOURCE    REFSEQ: accession NM_006283.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Wang,Y., Li,M., Zhang,L., Chen,Y. and Ha,M.
  TITLE     LINC01140 inhibits nonsmall cell lung cancer progression and
            cisplatin resistance through the miR-4742-5p/TACC1 axis
  JOURNAL   J Biochem Mol Toxicol 36 (7), e23048 (2022)
   PUBMED   35307914
  REMARK    GeneRIF: LINC01140 inhibits nonsmall cell lung cancer progression
            and cisplatin resistance through the miR-4742-5p/TACC1 axis.
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Devereaux,K.A., Weiel,J.J., Mills,A.M., Kunder,C.A. and
            Longacre,T.A.
  TITLE     Neurofibrosarcoma Revisited: An Institutional Case Series of
            Uterine Sarcomas Harboring Kinase-related Fusions With Report of a
            Novel FGFR1-TACC1 Fusion
  JOURNAL   Am J Surg Pathol 45 (5), 638-652 (2021)
   PUBMED   33481389
  REMARK    GeneRIF: Neurofibrosarcoma Revisited: An Institutional Case Series
            of Uterine Sarcomas Harboring Kinase-related Fusions With Report of
            a Novel FGFR1-TACC1 Fusion.
REFERENCE   4  (residues 1 to 805)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 805)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 805)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
REFERENCE   7  (residues 1 to 805)
  AUTHORS   Lauffart,B., Howell,S.J., Tasch,J.E., Cowell,J.K. and Still,I.H.
  TITLE     Interaction of the transforming acidic coiled-coil 1 (TACC1)
            protein with ch-TOG and GAS41/NuBI1 suggests multiple
            TACC1-containing protein complexes in human cells
  JOURNAL   Biochem J 363 (Pt 1), 195-200 (2002)
   PUBMED   11903063
  REMARK    GeneRIF: Interaction of the transforming acidic coiled-coil 1
            (TACC1) protein with ch-TOG and GAS41/NuBI1 suggests multiple
            TACC1-containing protein complexes in human cells
REFERENCE   8  (residues 1 to 805)
  AUTHORS   Gergely,F., Karlsson,C., Still,I., Cowell,J., Kilmartin,J. and
            Raff,J.W.
  TITLE     The TACC domain identifies a family of centrosomal proteins that
            can interact with microtubules
  JOURNAL   Proc Natl Acad Sci U S A 97 (26), 14352-14357 (2000)
   PUBMED   11121038
REFERENCE   9  (residues 1 to 805)
  AUTHORS   Still,I.H., Hamilton,M., Vince,P., Wolfman,A. and Cowell,J.K.
  TITLE     Cloning of TACC1, an embryonically expressed, potentially
            transforming coiled coil containing gene, from the 8p11 breast
            cancer amplicon
  JOURNAL   Oncogene 18 (27), 4032-4038 (1999)
   PUBMED   10435627
REFERENCE   10 (residues 1 to 805)
  AUTHORS   Still,I.H., Vince,P. and Cowell,J.K.
  TITLE     The third member of the transforming acidic coiled coil-containing
            gene family, TACC3, maps in 4p16, close to translocation
            breakpoints in multiple myeloma, and is upregulated in various
            cancer cell lines
  JOURNAL   Genomics 58 (2), 165-170 (1999)
   PUBMED   10366448
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB084271.1, AF049910.1,
            AY072876.2 and AY139007.1.
            
            On Mar 25, 2008 this sequence version replaced NP_006274.1.
            
            Summary: This locus may represent a breast cancer candidate gene.
            It is located close to FGFR1 on a region of chromosome 8 that is
            amplified in some breast cancers. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jun 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF049910.1, SRR1803617.15172.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317827.9/ ENSP00000321703.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.22"
     Protein         1..805
                     /product="transforming acidic coiled-coil-containing
                     protein 1 isoform 1"
                     /note="gastric cancer antigen Ga55; taxin-1"
                     /calculated_mol_wt=87664
     Region          2..55
                     /region_name="Interaction with LSM7 and SNRPG.
                     /evidence=ECO:0000269|PubMed:12165861"
                     /note="propagated from UniProtKB/Swiss-Prot (O75410.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Region          23..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75410.2)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Region          152..259
                     /region_name="Interaction with TDRD7.
                     /evidence=ECO:0000269|PubMed:14603251"
                     /note="propagated from UniProtKB/Swiss-Prot (O75410.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Region          206..427
                     /region_name="Interaction with YEATS4.
                     /evidence=ECO:0000269|PubMed:11903063"
                     /note="propagated from UniProtKB/Swiss-Prot (O75410.2)"
     Region          215..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75410.2)"
     Region          226..241
                     /region_name="Bipartite nuclear localization signal 1.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75410.2)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKC.
                     /evidence=ECO:0000269|PubMed:21531210; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75410.2)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6Y685; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6Y685; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Region          455..471
                     /region_name="Bipartite nuclear localization signal 2.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75410.2)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6Y685; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Region          493..526
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75410.2)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75410.2)"
     Region          599..798
                     /region_name="TACC_C"
                     /note="Transforming acidic coiled-coil-containing protein
                     (TACC), C-terminal; pfam05010"
                     /db_xref="CDD:461517"
     Region          701..805
                     /region_name="Interaction with CH-TOG"
                     /note="propagated from UniProtKB/Swiss-Prot (O75410.2)"
     CDS             1..805
                     /gene="TACC1"
                     /gene_synonym="Ga55"
                     /coded_by="NM_006283.3:348..2765"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6109.1"
                     /db_xref="GeneID:6867"
                     /db_xref="HGNC:HGNC:11522"
                     /db_xref="MIM:605301"
ORIGIN      
        1 mafspwqils pvqwakwtws avrggaaged eaggpegdpe eedsqaetks lsfssdsegn
       61 fetpeaetpi rspfkescdp slglagpgak sqesqeadeq lvaevvekcs sktcskpsen
      121 evpqqaidsh svknfreepe hdfskisivr pfsietkdst disavlgtka ahgcvtavsg
      181 kalpssppda lqdeamtegs mgvtleasae adlkagnscp elvpsrrskl rkpkpvplrk
      241 kaiggefsdt naavegtplp kasyhfspee ldentspllg darfqksppd lketpgtlss
      301 dtndsgvelg eesrssplkl efdftedtgn iearkalprk lgrklgstlt pkiqkdgisk
      361 sagleqptdp vardgplsqt sskpdpsqwe spsfnpfgsh svlqnsppls segsyhfdpd
      421 nfdesmdpfk ptttltssdf csptgnhvne ilespkkaks rlitsgckvk khetqslald
      481 acsrdegavi sqisdisnrd ghatdeekla stscgqksag aevkgepeed leyfecsnvp
      541 vstinhafss seagieketc qkmeedgstv lgllessaek apvsvscgge spldgiclse
      601 sdktavltli reeiitkeie anewkkkyee trqevlemrk ivaeyektia qmiedeqrts
      661 mtsqksfqql tmekeqalad lnsverslsd lfrryenlkg vlegfkknee alkkcaqdyl
      721 arvkqeeqry qalkihaeek ldkaneeiaq vrtkakaesa alhaglrkeq mkvesleral
      781 qqknqeieel tkicdeliak lgktd
//
LOCUS       NP_008844                180 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF5 [Homo sapiens].
ACCESSION   NP_008844
VERSION     NP_008844.1
DBSOURCE    REFSEQ: accession NM_006913.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Wei,G., Chen,X., Ruan,T., Ma,X., Zhu,X., Wen,W., He,D., Tao,K. and
            Wu,C.
  TITLE     Human gastric cancer progression and stabilization of ATG2B through
            RNF5 binding facilitated by autophagy-associated CircDHX8
  JOURNAL   Cell Death Dis 15 (6), 410 (2024)
   PUBMED   38866787
  REMARK    GeneRIF: Human gastric cancer progression and stabilization of
            ATG2B through RNF5 binding facilitated by autophagy-associated
            CircDHX8.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Li,X., Wang,F., Huang,L., Yang,M. and Kuang,E.
  TITLE     Downregulation of EphA2 stability by RNF5 limits its
            tumor-suppressive function in HER2-negative breast cancers
  JOURNAL   Cell Death Dis 14 (10), 662 (2023)
   PUBMED   37816703
  REMARK    GeneRIF: Downregulation of EphA2 stability by RNF5 limits its
            tumor-suppressive function in HER2-negative breast cancers.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Li,Z., Hao,P., Zhao,Z., Gao,W., Huan,C., Li,L., Chen,X., Wang,H.,
            Jin,N., Luo,Z.Q., Li,C. and Zhang,W.
  TITLE     The E3 ligase RNF5 restricts SARS-CoV-2 replication by targeting
            its envelope protein for degradation
  JOURNAL   Signal Transduct Target Ther 8 (1), 53 (2023)
   PUBMED   36737599
  REMARK    GeneRIF: The E3 ligase RNF5 restricts SARS-CoV-2 replication by
            targeting its envelope protein for degradation.
            Erratum:[Signal Transduct Target Ther. 2023 Feb 27;8(1):85. doi:
            10.1038/s41392-023-01374-y. PMID: 36849529]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Li,X., Wang,F., Zhang,X., Sun,Q. and Kuang,E.
  TITLE     Suppression of KSHV lytic replication and primary effusion lymphoma
            by selective RNF5 inhibition
  JOURNAL   PLoS Pathog 19 (1), e1011103 (2023)
   PUBMED   36656913
  REMARK    GeneRIF: Suppression of KSHV lytic replication and primary effusion
            lymphoma by selective RNF5 inhibition.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Didier,C., Broday,L., Bhoumik,A., Israeli,S., Takahashi,S.,
            Nakayama,K., Thomas,S.M., Turner,C.E., Henderson,S., Sabe,H. and
            Ronai,Z.
  TITLE     RNF5, a RING finger protein that regulates cell motility by
            targeting paxillin ubiquitination and altered localization
  JOURNAL   Mol Cell Biol 23 (15), 5331-5345 (2003)
   PUBMED   12861019
  REMARK    GeneRIF: RNF5 regulates cell motility by targeting paxillin
            ubiquitination and altered localization
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Matsuda,N., Suzuki,T., Tanaka,K. and Nakano,A.
  TITLE     Rma1, a novel type of RING finger protein conserved from
            Arabidopsis to human, is a membrane-bound ubiquitin ligase
  JOURNAL   J Cell Sci 114 (Pt 10), 1949-1957 (2001)
   PUBMED   11329381
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Barritt,D.S., Pearn,M.T., Zisch,A.H., Lee,S.S., Javier,R.T.,
            Pasquale,E.B. and Stallcup,W.B.
  TITLE     The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the
            membrane-spanning proteoglycan NG2
  JOURNAL   J Cell Biochem 79 (2), 213-224 (2000)
   PUBMED   10967549
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Kyushiki,H., Kuga,Y., Suzuki,M., Takahashi,E. and Horie,M.
  TITLE     Cloning, expression and mapping of a novel RING-finger gene (RNF5),
            a human homologue of a putative zinc-finger gene from
            Caenorhabditis elegans
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 114-117 (1997)
   PUBMED   9533025
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Kendall,E., Sargent,C.A. and Campbell,R.D.
  TITLE     Human major histocompatibility complex contains a new cluster of
            genes between the HLA-D and complement C4 loci
  JOURNAL   Nucleic Acids Res 18 (24), 7251-7257 (1990)
   PUBMED   2259622
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM712189.1, BC127652.1 and
            BC004155.2.
            
            Summary: The protein encoded by this gene contains a RING finger,
            which is a motif known to be involved in protein-protein
            interactions. This protein is a membrane-bound ubiquitin ligase. It
            can regulate cell motility by targeting paxillin ubiquitination and
            altering the distribution and localization of paxillin in cytoplasm
            and cell focal adhesions. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC111392.1, SRR5189667.389884.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375094.4/ ENSP00000364235.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..180
                     /product="E3 ubiquitin-protein ligase RNF5"
                     /EC_number="2.3.2.27"
                     /note="protein G16; ram1 homolog; ring finger protein 5,
                     E3 ubiquitin protein ligase; RING-type E3 ubiquitin
                     transferase RNF5"
                     /calculated_mol_wt=19750
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:25489052,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q99942.1)"
     Region          25..78
                     /region_name="RING-HC_RNF5"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 5 (RNF5) and similar proteins; cd16743"
                     /db_xref="CDD:438401"
     Region          79..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99942.1)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99942.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99942.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99942.1)"
     Site            118..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99942.1)"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99942.1)"
     CDS             1..180
                     /gene="RNF5"
                     /gene_synonym="RING5; RMA1"
                     /coded_by="NM_006913.4:108..650"
                     /db_xref="CCDS:CCDS4745.1"
                     /db_xref="GeneID:6048"
                     /db_xref="HGNC:HGNC:10068"
                     /db_xref="MIM:602677"
ORIGIN      
        1 maaaeeedgg pegpnrergg agatfecnic letareavvs vcghlycwpc lhqwletrpe
       61 rqecpvckag isrekvvply grgsqkpqdp rlktpprpqg qrpapesrgg fqpfgdtggf
      121 hfsfgvgafp fgffttvfna hepfrrgtgv dlgqghpass wqdslflfla iffffwllsi
//
LOCUS       NP_079091                323 aa            linear   PRI 27-APR-2025
DEFINITION  8-oxo-dGDP phosphatase NUDT18 [Homo sapiens].
ACCESSION   NP_079091
VERSION     NP_079091.3
DBSOURCE    REFSEQ: accession NM_024815.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Takagi,Y., Setoyama,D., Ito,R., Kamiya,H., Yamagata,Y. and
            Sekiguchi,M.
  TITLE     Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine
            and deoxyguanosine diphosphates: comparison with MTH1 and MTH2
  JOURNAL   J Biol Chem 287 (25), 21541-21549 (2012)
   PUBMED   22556419
  REMARK    GeneRIF: MTH3 is specifically active against 8-oxo-dGDP and hardly
            cleaves 8-oxo-dGTP. Other types of oxidized nucleoside
            diphosphates, 2-hydroxy-dADP and 8-hydroxy-dADP, were also
            hydrolyzed by MTH3.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Simonis,N., Rual,J.F., Lemmens,I., Boxus,M., Hirozane-Kishikawa,T.,
            Gatot,J.S., Dricot,A., Hao,T., Vertommen,D., Legros,S., Daakour,S.,
            Klitgord,N., Martin,M., Willaert,J.F., Dequiedt,F., Navratil,V.,
            Cusick,M.E., Burny,A., Van Lint,C., Hill,D.E., Tavernier,J.,
            Kettmann,R., Vidal,M. and Twizere,J.C.
  TITLE     Host-pathogen interactome mapping for HTLV-1 and -2 retroviruses
  JOURNAL   Retrovirology 9, 26 (2012)
   PUBMED   22458338
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA015404.1, BC016902.1 and
            AC091171.15.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 16, 2006 this sequence version replaced NP_079091.2.
            
            Summary: The protein encoded by this gene is a member of the Nudix
            hydrolase family. Nudix hydrolases eliminate potentially toxic
            nucleotide metabolites from the cell and regulate the
            concentrations and availability of many different nucleotide
            substrates, cofactors, and signaling molecules. This protein
            contains a Nudix hydrolase domain and hydrolyzes oxidized forms of
            guanosine and deoxyguanosine diphosphates. [provided by RefSeq, Sep
            2012].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.192486.1,
                                           SRR1803614.173760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000611621.2/ ENSP00000480722.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..323
                     /product="8-oxo-dGDP phosphatase NUDT18"
                     /EC_number="3.6.1.58"
                     /note="nucleoside diphosphate-linked moiety X motif 18;
                     nudix motif 18; mutT human homolog 3; mutT homolog 3;
                     2-hydroxy-dADP phosphatase; 7,8-dihydro-8-oxoguanine
                     phosphatase; nudix (nucleoside diphosphate linked moiety
                     X)-type motif 18"
                     /calculated_mol_wt=35370
     Region          44..173
                     /region_name="NUDIX_8DGDPP_Nudt18"
                     /note="8-oxo-DGDP phosphatase; cd04671"
                     /db_xref="CDD:467555"
     Region          76..97
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVK8.3)"
     CDS             1..323
                     /gene="NUDT18"
                     /gene_synonym="MTH3"
                     /coded_by="NM_024815.4:120..1091"
                     /db_xref="CCDS:CCDS75706.1"
                     /db_xref="GeneID:79873"
                     /db_xref="HGNC:HGNC:26194"
                     /db_xref="MIM:615791"
ORIGIN      
        1 maseglagal asvlagqgss vhscdsapag eppapvrlrk nvcyvvlavf lseqdevlli
       61 qeakrecrgs wylpagrmep getivealqr evkeeaglhc epetllsvee rgpswvrfvf
      121 larptggilk tskeadaesl qaawyprtsl ptplrahdil hlvelaaqyr qqarhplilp
      181 qelpcdlvcq rlvatftsaq tvwvlvgtvg mphlpvtacg ldpmeqrggm kmavlrllqe
      241 cltlhhlvve ikgllglqhl grdhsdgicl nvlvtvafrs pgiqdeppkv rgenfswwkv
      301 meedlqsqll qrlqgssvvp vnr
//
LOCUS       NP_005661                331 aa            linear   PRI 27-APR-2025
DEFINITION  laforin isoform a [Homo sapiens].
ACCESSION   NP_005661
VERSION     NP_005661.1
DBSOURCE    REFSEQ: accession NM_005670.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lomax,L.B., Verhalen,B. and Minassian,B.A.
  TITLE     EPM2A in-frame deletion slows neurological decline in Lafora
            Disease
  JOURNAL   Seizure 91, 97-98 (2021)
   PUBMED   34147889
  REMARK    GeneRIF: EPM2A in-frame deletion slows neurological decline in
            Lafora Disease.
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Sanchez-Martin,P., Lahuerta,M., Viana,R., Knecht,E. and Sanz,P.
  TITLE     Regulation of the autophagic PI3KC3 complex by laforin/malin
            E3-ubiquitin ligase, two proteins involved in Lafora disease
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1867 (2), 118613 (2020)
   PUBMED   31758957
  REMARK    GeneRIF: Laforin/malin complex interacts physically and
            co-localizes intracellularly with core components of the PI3KC3
            complex (Beclin1, Vps34 and Vps15), and that this interaction is
            specific and results in the polyubiquitination of these proteins.
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Sullivan,M.A., Nitschke,S., Steup,M., Minassian,B.A. and
            Nitschke,F.
  TITLE     Pathogenesis of Lafora Disease: Transition of Soluble Glycogen to
            Insoluble Polyglucosan
  JOURNAL   Int J Mol Sci 18 (8), 1743 (2017)
   PUBMED   28800070
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Minassian,B.A., Lee,J.R., Herbrick,J.A., Huizenga,J., Soder,S.,
            Mungall,A.J., Dunham,I., Gardner,R., Fong,C.Y., Carpenter,S.,
            Jardim,L., Satishchandra,P., Andermann,E., Snead,O.C. 3rd,
            Lopes-Cendes,I., Tsui,L.C., Delgado-Escueta,A.V., Rouleau,G.A. and
            Scherer,S.W.
  TITLE     Mutations in a gene encoding a novel protein tyrosine phosphatase
            cause progressive myoclonus epilepsy
  JOURNAL   Nat Genet 20 (2), 171-174 (1998)
   PUBMED   9771710
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Sainz,J., Minassian,B.A., Serratosa,J.M., Gee,M.N., Sakamoto,L.M.,
            Iranmanesh,R., Bohlega,S., Baumann,R.J., Ryan,S., Sparkes,R.S. and
            Delgado-Escueta,A.V.
  TITLE     Lafora progressive myoclonus epilepsy: narrowing the chromosome
            6q24 locus by recombinations and homozygosities
  JOURNAL   Am J Hum Genet 61 (5), 1205-1209 (1997)
   PUBMED   9345091
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Maddox,L.O., Descartes,M., Collins,J., Keating,J., Rosenfeld,S.,
            Palmer,C., Carroll,A.J. and Kuzniecky,R.
  TITLE     Identification of a recombination event narrowing the Lafora
            disease gene region
  JOURNAL   J Med Genet 34 (7), 590-591 (1997)
   PUBMED   9222970
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Labauge,P., Beck,C., Bellet,H., Coquillat,G., Vespignani,H.,
            Dulac,O., Gilgenkrantz,S., Dravet,C., Genton,P., Pellissier,J.F. et
            al.
  TITLE     Lafora disease is not linked to the Unverricht-Lundborg locus
  JOURNAL   Am J Med Genet 60 (1), 80-84 (1995)
   PUBMED   7485240
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Minassian,B.
  TITLE     Progressive Myoclonus Epilepsy, Lafora Type
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301563
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF284580.1, AF454494.1 and
            BC005286.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a dual-specificity phosphatase and may
            be involved in the regulation of glycogen metabolism. The protein
            acts on complex carbohydrates to prevent glycogen
            hyperphosphorylation, thus avoiding the formation of insoluble
            aggregates. Loss-of-function mutations in this gene have been
            associated with Lafora disease, a rare, adult-onset recessive
            neurodegenerative disease, which results in myoclonus epilepsy and
            usually results in death several years after the onset of symptoms.
            The disease is characterized by the accumulation of insoluble
            particles called Lafora bodies, which are derived from glycogen.
            [provided by RefSeq, Jan 2018].
            
            Transcript Variant: This variant (1) represents the longest
            transcript, and encodes the longest isoform (a). Isoform a has been
            localized to the rough endoplasmic reticulum.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070047.1, AF284580.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367519.9/ ENSP00000356489.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.3"
     Protein         1..331
                     /product="laforin isoform a"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="epilepsy, progressive myoclonus type 2, Lafora
                     disease (laforin); EPM2A, laforin glucan phosphatase;
                     LAFPTPase; lafora PTPase; epilepsy, progressive myoclonus
                     type 2A, Lafora disease (laforin); glycogen phosphatase"
                     /calculated_mol_wt=37027
     Region          1..129
                     /region_name="CBM20_laforin"
                     /note="Laforin protein tyrosine phosphatase, N-terminal
                     CBM20 (carbohydrate-binding module, family 20) domain.
                     Laforin, encoded by the EPM2A gene, is a dual-specificity
                     phosphatase that dephosphorylates complex carbohydrates.
                     Mutations in the gene encoding...; cd05806"
                     /db_xref="CDD:99881"
     Site            order(12,15..19,42,58,60)
                     /site_type="other"
                     /note="starch-binding site 2 [chemical binding]"
                     /db_xref="CDD:99881"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:21728993; propagated from
                     UniProtKB/Swiss-Prot (O95278.2)"
     Site            order(32,87,99..100,104)
                     /site_type="other"
                     /note="starch-binding site 1 [chemical binding]"
                     /db_xref="CDD:99881"
     Region          155..312
                     /region_name="DSP_laforin-like"
                     /note="dual specificity phosphatase domain of laforin and
                     similar domains; cd14526"
                     /db_xref="CDD:350375"
     Region          266..272
                     /region_name="Glucan phosphatase signature motif CXAGXGR.
                     /evidence=ECO:0000305|PubMed:25544560,
                     ECO:0000305|PubMed:26231210"
                     /note="propagated from UniProtKB/Swiss-Prot (O95278.2)"
     Site            329
                     /site_type="other"
                     /note="Required for homodimerization.
                     /evidence=ECO:0000269|PubMed:23922729; propagated from
                     UniProtKB/Swiss-Prot (O95278.2)"
     CDS             1..331
                     /gene="EPM2A"
                     /gene_synonym="EPM2; MELF; MELF2"
                     /coded_by="NM_005670.4:23..1018"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5206.1"
                     /db_xref="GeneID:7957"
                     /db_xref="HGNC:HGNC:3413"
                     /db_xref="MIM:607566"
ORIGIN      
        1 mrfrfgvvvp pavagarpel lvvgsrpelg rweprgavrl rpagtaagdg alalqepglw
       61 lgevelaaee aaqdgaepgr vdtfwykflk repggelswe gngphhdrcc tynennlvdg
      121 vyclpighwi eatghtnemk httdfyfnia ghqamhysri lpniwlgscp rqvehvtikl
      181 khelgitavm nfqtewdivq nssgcnrype pmtpdtmikl yreeglayiw mptpdmsteg
      241 rvqmlpqavc llhallekgh ivyvhcnagv grstaavcgw lqyvmgwnlr kvqyflmakr
      301 pavyideeal araqedffqk fgkvrssvcs l
//
LOCUS       NP_064502               1176 aa            linear   PRI 27-APR-2025
DEFINITION  leucine--tRNA ligase, cytoplasmic isoform 1 [Homo sapiens].
ACCESSION   NP_064502
VERSION     NP_064502.9
DBSOURCE    REFSEQ: accession NM_020117.11
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1176)
  AUTHORS   Chen,W., Lin,Y., Jiang,M., Wang,Q. and Shu,Q.
  TITLE     Identification of LARS as an essential gene for osteosarcoma
            proliferation through large-Scale CRISPR-Cas9 screening database
            and experimental verification
  JOURNAL   J Transl Med 20 (1), 355 (2022)
   PUBMED   35962451
  REMARK    GeneRIF: Identification of LARS as an essential gene for
            osteosarcoma proliferation through large-Scale CRISPR-Cas9
            screening database and experimental verification.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1176)
  AUTHORS   Kim,K., Yoo,H.C., Kim,B.G., Kim,S., Sung,Y., Yoon,I., Yu,Y.C.,
            Park,S.J., Kim,J.H., Myung,K., Hwang,K.Y., Kim,S. and Han,J.M.
  TITLE     O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates
            leucine and glucose availability to regulate mTORC1 and the
            metabolic fate of leucine
  JOURNAL   Nat Commun 13 (1), 2904 (2022)
   PUBMED   35614056
  REMARK    GeneRIF: O-GlcNAc modification of leucyl-tRNA synthetase 1
            integrates leucine and glucose availability to regulate mTORC1 and
            the metabolic fate of leucine.
            Erratum:[Nat Commun. 2022 Oct 21;13(1):6253. doi:
            10.1038/s41467-022-34146-3. PMID: 36271081]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1176)
  AUTHORS   Bae,J.H. and Kim,J.H.
  TITLE     Leucyl-tRNA synthetase 1 is required for proliferation of TSC-null
            cells
  JOURNAL   Biochem Biophys Res Commun 571, 159-166 (2021)
   PUBMED   34325132
  REMARK    GeneRIF: Leucyl-tRNA synthetase 1 is required for proliferation of
            TSC-null cells.
REFERENCE   4  (residues 1 to 1176)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1176)
  AUTHORS   Tabolacci,E., Molinario,C., Marangi,G., Nobile,V., Arena,V.,
            Mendes,M.I., Smith,D.E.C., Salomons,G.S., Tana,M., Costa,S.,
            Vento,G. and Genuardi,M.
  TITLE     Infantile Liver Failure Syndrome 1 associated with a novel variant
            of the LARS1 gene: Clinical, genetic, and functional
            characterization
  JOURNAL   Clin Genet 99 (4), 601-603 (2021)
   PUBMED   33314043
  REMARK    GeneRIF: Infantile Liver Failure Syndrome 1 associated with a novel
            variant of the LARS1 gene: Clinical, genetic, and functional
            characterization.
REFERENCE   6  (residues 1 to 1176)
  AUTHORS   Lamour,V., Quevillon,S., Diriong,S., N'Guyen,V.C., Lipinski,M. and
            Mirande,M.
  TITLE     Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme
            as a case of horizontal gene transfer
  JOURNAL   Proc Natl Acad Sci U S A 91 (18), 8670-8674 (1994)
   PUBMED   8078941
REFERENCE   7  (residues 1 to 1176)
  AUTHORS   Shiba,K., Suzuki,N., Shigesada,K., Namba,Y., Schimmel,P. and
            Noda,T.
  TITLE     Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence
            of the anticodon-binding domain and acquisition of a new structural
            unit
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7435-7439 (1994)
   PUBMED   8052601
REFERENCE   8  (residues 1 to 1176)
  AUTHORS   Norcum,M.T.
  TITLE     Structural analysis of the high molecular mass aminoacyl-tRNA
            synthetase complex. Effects of neutral salts and detergents
  JOURNAL   J Biol Chem 266 (23), 15398-15405 (1991)
   PUBMED   1651330
REFERENCE   9  (residues 1 to 1176)
  AUTHORS   Dana,S. and Wasmuth,J.J.
  TITLE     Selective linkage disruption in human-Chinese hamster cell hybrids:
            deletion mapping of the leuS, hexB, emtB, and chr genes on human
            chromosome 5
  JOURNAL   Mol Cell Biol 2 (10), 1220-1228 (1982)
   PUBMED   7177110
REFERENCE   10 (residues 1 to 1176)
  AUTHORS   Giles,R.E., Shimizu,N. and Ruddle,F.H.
  TITLE     Assignment of a human genetic locus to chromosome 5 which corrects
            the heat sensitive lesion associated with reduced leucyl-tRNA
            synthetase activity in ts025Cl Chinese hamster cells
  JOURNAL   Somatic Cell Genet 6 (5), 667-687 (1980)
   PUBMED   6933703
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB037773.1, AC091887.3 and
            CK902545.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 9, 2006 this sequence version replaced NP_064502.8.
            
            Summary: This gene encodes a cytosolic leucine-tRNA synthetase, a
            member of the class I aminoacyl-tRNA synthetase family. The encoded
            enzyme catalyzes the ATP-dependent ligation of L-leucine to
            tRNA(Leu). It is found in the cytoplasm as part of a
            multisynthetase complex and interacts with the arginine tRNA
            synthetase through its C-terminal domain. A mutation in this gene
            was found in affected individuals with infantile liver failure
            syndrome 1. Alternatively spliced transcript variants of this gene
            have been observed. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.12971.1,
                                           SRR1803614.84918.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394434.7/ ENSP00000377954.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..1176
                     /product="leucine--tRNA ligase, cytoplasmic isoform 1"
                     /EC_number="6.1.1.4"
                     /note="leucine tRNA ligase 1, cytoplasmic;
                     proliferation-inducing gene 44; cytoplasmic leucyl-tRNA
                     synthetase; cytosolic leucyl-tRNA synthetase; leucine
                     translase"
                     /calculated_mol_wt=134336
     Region          5..1062
                     /region_name="PLN02959"
                     /note="aminoacyl-tRNA ligase"
                     /db_xref="CDD:215518"
     Region          60..63
                     /region_name="'HIGH' region.
                     /evidence=ECO:0000305|PubMed:32232361,
                     ECO:0007744|PDB:6LPF"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2J5.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2J5.2)"
     Region          260..509
                     /region_name="Editing domain.
                     /evidence=ECO:0000305|PubMed:19426743"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2J5.2)"
     Region          716..720
                     /region_name="'KMSKS' region.
                     /evidence=ECO:0000305|PubMed:32232361,
                     ECO:0007744|PDB:6LPF"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2J5.2)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2J5.2)"
     Site            970
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BMJ2; propagated from
                     UniProtKB/Swiss-Prot (Q9P2J5.2)"
     Site            1047
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BMJ2; propagated from
                     UniProtKB/Swiss-Prot (Q9P2J5.2)"
     CDS             1..1176
                     /gene="LARS1"
                     /gene_synonym="cLRS; hr025Cl; HSPC192; ILFS1; LARS; LEURS;
                     LEUS; LFIS; LRS; PIG44; RNTLS"
                     /coded_by="NM_020117.11:158..3688"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34265.1"
                     /db_xref="GeneID:51520"
                     /db_xref="HGNC:HGNC:6512"
                     /db_xref="MIM:151350"
ORIGIN      
        1 maerkgtakv dflkkiekei qqkwdtervf evnasnlekq tskgkyfvtf pypymngrlh
       61 lghtfslskc efavgyqrlk gkcclfpfgl hctgmpikac adklkreiel ygcppdfpde
      121 eeeeeetsvk tediiikdka kgkkskaaak agsskyqwgi mkslglsdee ivkfseaehw
      181 ldyfpplaiq dlkrmglkvd wrrsfittdv npyydsfvrw qfltlrernk ikfgkrytiy
      241 spkdgqpcmd hdrqtgegvg pqeytllklk vlepypskls glkgkniflv aatlrpetmf
      301 gqtncwvrpd mkyigfetvn gdifictqka arnmsyqgft kdngvvpvvk elmgeeilga
      361 slsapltsyk viyvlpmlti kedkgtgvvt svpsdspddi aalrdlkkkq alrakygird
      421 dmvlpfepvp vieipgfgnl savticdelk iqsqndrekl aeakekiylk gfyegimlvd
      481 gfkgqkvqdv kktiqkkmid agdaliymep ekqvmsrssd ecvvalcdqw yldygeenwk
      541 kqtsqclknl etfceetrrn featlgwlqe hacsrtyglg thlpwdeqwl ieslsdstiy
      601 mafytvahll qggnlhgqae splgirpqqm tkevwdyvff keapfpktqi akekldqlkq
      661 efefwypvdl rvsgkdlvpn hlsyylynhv amwpeqsdkw ptavranghl llnsekmsks
      721 tgnfltltqa idkfsadgmr laladagdtv edanfveama dagilrlytw vewvkemvan
      781 wdslrsgpas tfndrvfase lnagiiktdq nyekmmfkea lktgffefqa akdkyrelav
      841 egmhrelvfr fievqtllla pfcphlcehi wtllgkpdsi mnaswpvagp vnevlihssq
      901 ylmevthdlr lrlknymmpa kgkktdkqpl qkpshctiyv aknyppwqht tlsvlrkhfe
      961 anngklpdnk viaselgsmp elkkymkkvm pfvamikenl ekmgprildl qlefdekavl
     1021 menivyltns lelehievkf aseaedkire dccpgkplnv friepgvsvs lvnpqpsngh
     1081 fstkieirqg dncdsiirrl mkmnrgikdl skvklmrfdd pllgprrvpv lgkeytektp
     1141 isehavfnvd lmskkihlte ngirvdigdt iiylvh
//
LOCUS       NP_001347826             984 aa            linear   ROD 27-APR-2025
DEFINITION  importin-11 isoform 2 [Mus musculus].
ACCESSION   NP_001347826 XP_006517849
VERSION     NP_001347826.1
DBSOURCE    REFSEQ: accession NM_001360897.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Gu,Y., Wang,Y., He,L., Zhang,J., Zhu,X., Liu,N., Wang,J., Lu,T.,
            He,L., Tian,Y. and Fan,Z.
  TITLE     Circular RNA circIPO11 drives self-renewal of liver cancer
            initiating cells via Hedgehog signaling
  JOURNAL   Mol Cancer 20 (1), 132 (2021)
   PUBMED   34649567
  REMARK    GeneRIF: Circular RNA circIPO11 drives self-renewal of liver cancer
            initiating cells via Hedgehog signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Lee,J.Y., Rahman,F.U., Kim,E.K., Cho,S.M., Kim,H.R., Lee,K.,
            Lee,C.S., Yoon,W.K., Moon,O.S., Seo,Y.W., Won,Y.S., Kim,H.C.,
            Kim,B.H. and Nam,K.H.
  TITLE     Importin-11 is Essential for Normal Embryonic Development in Mice
  JOURNAL   Int J Med Sci 17 (6), 815-823 (2020)
   PUBMED   32218703
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 984)
  AUTHORS   Chen,M., Nowak,D.G., Narula,N., Robinson,B., Watrud,K., Ambrico,A.,
            Herzka,T.M., Zeeman,M.E., Minderer,M., Zheng,W., Ebbesen,S.H.,
            Plafker,K.S., Stahlhut,C., Wang,V.M., Wills,L., Nasar,A.,
            Castillo-Martin,M., Cordon-Cardo,C., Wilkinson,J.E., Powers,S.,
            Sordella,R., Altorki,N.K., Mittal,V., Stiles,B.M., Plafker,S.M. and
            Trotman,L.C.
  TITLE     The nuclear transport receptor Importin-11 is a tumor suppressor
            that maintains PTEN protein
  JOURNAL   J Cell Biol 216 (3), 641-656 (2017)
   PUBMED   28193700
REFERENCE   5  (residues 1 to 984)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   6  (residues 1 to 984)
  AUTHORS   Taniwaki,T., Haruna,K., Nakamura,H., Sekimoto,T., Oike,Y.,
            Imaizumi,T., Saito,F., Muta,M., Soejima,Y., Utoh,A., Nakagata,N.,
            Araki,M., Yamamura,K. and Araki,K.
  TITLE     Characterization of an exchangeable gene trap using pU-17 carrying
            a stop codon-beta geo cassette
  JOURNAL   Dev Growth Differ 47 (3), 163-172 (2005)
   PUBMED   15840001
REFERENCE   7  (residues 1 to 984)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   8  (residues 1 to 984)
  AUTHORS   Plafker,S.M. and Macara,I.G.
  TITLE     Ribosomal protein L12 uses a distinct nuclear import pathway
            mediated by importin 11
  JOURNAL   Mol Cell Biol 22 (4), 1266-1275 (2002)
   PUBMED   11809816
REFERENCE   9  (residues 1 to 984)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC154328.2 and BC031900.1.
            
            On Feb 16, 2018 this sequence version replaced XP_006517849.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC031900.1, SRR17253012.9042145.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 58.06 cM"
     Protein         1..984
                     /product="importin-11 isoform 2"
                     /note="imp11; ran-binding protein 11"
                     /calculated_mol_wt=113200
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9UI26; propagated from
                     UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          10..981
                     /region_name="CSE1"
                     /note="CAS/CSE protein involved in chromosome segregation
                     [Cell division and chromosome partitioning]; COG5657"
                     /db_xref="CDD:227944"
     Region          123..160
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          283..317
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          318..356
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UI26; propagated from
                     UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          422..459
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          426..459
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(451..452,455,458..459,494..495,498,501..502,505,
                     533..534,537,540..541,544,578..579,582,585..586,621..622,
                     625,628..629)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          473..509
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          478..505
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          511..548
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          515..545
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          552..586
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          555..593
                     /region_name="HEAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          599..630
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          600..636
                     /region_name="HEAT 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          640..677
                     /region_name="HEAT 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          740..782
                     /region_name="HEAT 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          828..858
                     /region_name="HEAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          859..896
                     /region_name="HEAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     Region          966..983
                     /region_name="HEAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2V6.1)"
     CDS             1..984
                     /gene="Ipo11"
                     /gene_synonym="1700081H05Rik; 2510001A17Rik;
                     E330021B14Rik; Ranbp11"
                     /coded_by="NM_001360897.1:206..3160"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS88519.1"
                     /db_xref="GeneID:76582"
                     /db_xref="MGI:MGI:2442377"
ORIGIN      
        1 mdlnsassvv lqvltqatsq dtavlkpaee qlkqwetqpg fysvllnift nhtldinvrw
       61 lavlyfkhgi drywrrvaph alseeekstl raglitnfne pinqiatqia vliakvarld
      121 cprqwpelip tlvesvkvqd dlrqhrallt fyhvtktlas krlaadrklf ydlasgiynf
      181 acslwnhhtd tflqhvssgn eaavlssler tllslkvlrk ltvngfveph knmevmgflh
      241 giferlkqfl ecsrsigtdn vcrdrlekti ilftkvlldf ldqhpisftp liqrslefsv
      301 syvftevgeg vtferfivqc mnlikmivkn yaykpsknfe dsspetleah kikmafftyp
      361 tlteicrrlv shyfllteee ltmweedpeg ftveetggds wkyslrpcte vlfidifhey
      421 nqtltpvlle mmqtlegptn vedmnallik davynavgla afelfdsvdf dqwfktqllp
      481 elqvshnryk plrrrviwli gqwisvkfks dlrpmlyeai cnllqdqdlv vrietattlk
      541 ltvddfefrt dqflpyletm ftllfqllqq vtecdtkmhv lhvlscvier vnvqirpyvg
      601 clvqylpllw kqseehnmlr cailttlihl vqglgadskn lypfllpviq lstdvsqpph
      661 vylledglel wlvtlenspc vtpellrifq nmspllelps sclanelsse nlrtcfkiin
      721 gyiflsstef lqtyaaglcq sfyellpeit tegqvqvlkv venalkvnpv lgpqmfqril
      781 pcvfrgvieg erypvvmsiy lavmgrvllq ntsffsslln emghefnqem dqllgnviem
      841 wvdrmdnitq perkklsala llsllpsdns viqdkfcgii nisvealhdv mtedpetrty
      901 kdcmlmsqhe epkvtedeep pteqdkrkkm lalkdpvhtv slqqfiyekl kaqqeilgeq
      961 gfqslmetvd teivtqlqef lqgf
//
LOCUS       NP_116254                715 aa            linear   PRI 27-APR-2025
DEFINITION  tensin-4 precursor [Homo sapiens].
ACCESSION   NP_116254
VERSION     NP_116254.4
DBSOURCE    REFSEQ: accession NM_032865.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Yang,J., Li,X., Chen,S., Li,G., Pu,P., Yang,Y., Wu,W., Geng,Y. and
            Liu,Y.
  TITLE     GPRC5A promotes gallbladder cancer metastasis by upregulating TNS4
            via the JAK2-STAT3 pathway
  JOURNAL   Cancer Lett 598, 217067 (2024)
   PUBMED   38942137
  REMARK    GeneRIF: GPRC5A promotes gallbladder cancer metastasis by
            upregulating TNS4 via the JAK2-STAT3 pathway.
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Heo,H., Kim,H.J., Haam,K., Sohn,H.A., Shin,Y.J., Go,H., Jung,H.J.,
            Kim,J.H., Lee,S.I., Song,K.S., Kim,M.J., Lee,H., Kwon,E.S.,
            Kim,S.Y., Kim,Y.S. and Kim,M.
  TITLE     Epigenetic Activation of Tensin 4 Promotes Gastric Cancer
            Progression
  JOURNAL   Mol Cells 46 (5), 298-308 (2023)
   PUBMED   36896596
  REMARK    GeneRIF: Epigenetic Activation of Tensin 4 Promotes Gastric Cancer
            Progression.
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Wang,Y.X., Huang,C.Y., Chiu,H.J., Huang,P.H., Chien,H.T., Jwo,S.H.
            and Liao,Y.C.
  TITLE     Nuclear-localized CTEN is a novel transcriptional regulator and
            promotes cancer cell migration through its downstream target CDC27
  JOURNAL   J Physiol Biochem 79 (1), 163-174 (2023)
   PUBMED   36399312
  REMARK    GeneRIF: Nuclear-localized CTEN is a novel transcriptional
            regulator and promotes cancer cell migration through its downstream
            target CDC27.
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Liu,F., Gao,X., Liu,W. and Xue,W.
  TITLE     Mining TCGA and GEO databases for the prediction of poor prognosis
            in lung adenocarcinoma based on up-regulated expression of TNS4
  JOURNAL   Medicine (Baltimore) 101 (42), e31120 (2022)
   PUBMED   36281194
  REMARK    GeneRIF: Mining TCGA and GEO databases for the prediction of poor
            prognosis in lung adenocarcinoma based on up-regulated expression
            of TNS4.
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Lu,X., Zhou,B., Cao,M., Shao,Q., Pan,Y. and Zhao,T.
  TITLE     CTEN Inhibits Tumor Angiogenesis and Growth by Targeting VEGFA
            Through Down-Regulation of beta-Catenin in Breast Cancer
  JOURNAL   Technol Cancer Res Treat 20, 15330338211045506 (2021)
   PUBMED   34817293
  REMARK    GeneRIF: CTEN Inhibits Tumor Angiogenesis and Growth by Targeting
            VEGFA Through Down-Regulation of beta-Catenin in Breast Cancer.
REFERENCE   6  (residues 1 to 715)
  AUTHORS   Lo,S.S., Lo,S.H. and Lo,S.H.
  TITLE     Cleavage of cten by caspase-3 during apoptosis
  JOURNAL   Oncogene 24 (26), 4311-4314 (2005)
   PUBMED   15806167
REFERENCE   7  (residues 1 to 715)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
REFERENCE   8  (residues 1 to 715)
  AUTHORS   Sasaki,H., Yukiue,H., Kobayashi,Y., Fukai,I. and Fujii,Y.
  TITLE     Cten mRNA expression is correlated with tumor progression in
            thymoma
  JOURNAL   Tumour Biol 24 (5), 271-274 (2003)
   PUBMED   15001839
  REMARK    GeneRIF: Cten/GAPDH mRNA expression was correlated with evidence of
            tumor progression in thymoma.
REFERENCE   9  (residues 1 to 715)
  AUTHORS   Sasaki,H., Moriyama,S., Mizuno,K., Yukiue,H., Konishi,A., Yano,M.,
            Kaji,M., Fukai,I., Kiriyama,M., Yamakawa,Y. and Fujii,Y.
  TITLE     Cten mRNA expression was correlated with tumor progression in lung
            cancers
  JOURNAL   Lung Cancer 40 (2), 151-155 (2003)
   PUBMED   12711115
  REMARK    GeneRIF: Increased cten mRNA expression was correlated with tumor
            progression in lung cancers
REFERENCE   10 (residues 1 to 715)
  AUTHORS   Lo,S.H. and Lo,T.B.
  TITLE     Cten, a COOH-terminal tensin-like protein with prostate restricted
            expression, is down-regulated in prostate cancer
  JOURNAL   Cancer Res 62 (15), 4217-4221 (2002)
   PUBMED   12154022
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018629.12, BM710196.1, AF417488.1, BC018706.1, AW937802.1 and
            AW378527.1.
            
            On Sep 28, 2007 this sequence version replaced NP_116254.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF417488.1, AF370421.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254051.11/ ENSP00000254051.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..715
                     /product="tensin-4 precursor"
                     /note="C terminal tensin like; C-terminal tensin-like
                     protein"
                     /calculated_mol_wt=74997
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZW8.3)"
                     /calculated_mol_wt=1785
     mat_peptide     19..715
                     /product="Tensin-4. /id=PRO_0000248213"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZW8.3)"
                     /calculated_mol_wt=74997
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q8IZW8.3)"
     Region          159..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZW8.3)"
     Region          <191..438
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          195..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZW8.3)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q8IZW8.3)"
     Region          291..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZW8.3)"
     Region          376..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZW8.3)"
     Region          445..558
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(456,474,510,512)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198173"
     Site            order(511,540)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198173"
     Site            570..571
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000269|PubMed:15806167; propagated from
                     UniProtKB/Swiss-Prot (Q8IZW8.3)"
     Region          580..710
                     /region_name="PTB_tensin"
                     /note="Tensin Phosphotyrosine-binding (PTB) domain;
                     cd01213"
                     /db_xref="CDD:269924"
     Site            order(585,669,690)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269924"
     Site            order(649..654,676,699,703)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269924"
     CDS             1..715
                     /gene="TNS4"
                     /gene_synonym="CTEN; PP14434"
                     /coded_by="NM_032865.6:186..2333"
                     /db_xref="CCDS:CCDS11368.1"
                     /db_xref="GeneID:84951"
                     /db_xref="HGNC:HGNC:24352"
                     /db_xref="MIM:608385"
ORIGIN      
        1 msqvmsspll agghavslap cdeprrtlhp apspslppqc syyttegwga qalmapvpcm
       61 gppgrlqqap qveakatcfl pspgekalgt pedldsyidf sleslnqmil eldptfqllp
      121 pgtggsqael aqstmsmrkk eesealdiky ievtsarsrc hdgpqhcssp svtppfgslr
      181 sgglllsrdv pretrssses lifsgnqgrg hqrplppseg lsprppnsps isipcmgska
      241 ssphglgspl vasprlekrl gglapqrgsr isvlsaspvs dvsymfgssq sllhssnssh
      301 qsssrslesp ansssslhsl gsvslctrps dfqaprnptl tmgqprtphs pplakehass
      361 cppsitnsmv dipivlingc pepgssppqr tpghqnsvqp gaaspsnpcp atrsnsqtls
      421 dapfttcpeg pardmqptmk fvmdtskywf kpnitreqai ellrkeepga fvirdsssyr
      481 gsfglalkvq evpasaqsrp gedsndlirh fliessakgv hlkgadeepy fgslsafvcq
      541 hsimalalpc kltipqrelg gadgasdstd spascqkksa gchtlylssv svetltgala
      601 vqkaisttfe rdilptptvv hfkvteqgit ltdvqrkvff rrhyplttlr fcgmdpeqrk
      661 wqkyckpswi fgfvaksqte pqenvchlfa eydmvqpasq viglvtallq daerm
//
LOCUS       NP_003073                368 aa            linear   PRI 27-APR-2025
DEFINITION  snRNA-activating protein complex subunit 1 [Homo sapiens].
ACCESSION   NP_003073
VERSION     NP_003073.1
DBSOURCE    REFSEQ: accession NM_003082.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Sun,J., Li,X., Hou,X., Cao,S., Cao,W., Zhang,Y., Song,J., Wang,M.,
            Wang,H., Yan,X., Li,Z., Roeder,R.G. and Wang,W.
  TITLE     Structural basis of human SNAPc recognizing proximal sequence
            element of snRNA promoter
  JOURNAL   Nat Commun 13 (1), 6871 (2022)
   PUBMED   36369505
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Hasegawa,Y., Taylor,D., Ovchinnikov,D.A., Wolvetang,E.J., de
            Torrente,L. and Mar,J.C.
  TITLE     Variability of Gene Expression Identifies Transcriptional
            Regulators of Early Human Embryonic Development
  JOURNAL   PLoS Genet 11 (8), e1005428 (2015)
   PUBMED   26288249
  REMARK    GeneRIF: Results from a study on gene expression variability
            markers in early-stage human embryos shows that is a putative
            expression variability marker as well as a differential gene
            expression marker for the 3-day, 8-cell embryo stage.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Maeng,J.H. and Yoon,J.B.
  TITLE     The human PTFgamma/SNAP43 gene: structure, chromosomal location,
            and identification of a VNTR in 5'-UTR
  JOURNAL   J Biochem 124 (1), 23-27 (1998)
   PUBMED   9644240
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Wong,M.W., Henry,R.W., Ma,B., Kobayashi,R., Klages,N., Matthias,P.,
            Strubin,M. and Hernandez,N.
  TITLE     The large subunit of basal transcription factor SNAPc is a Myb
            domain protein that interacts with Oct-1
  JOURNAL   Mol Cell Biol 18 (1), 368-377 (1998)
   PUBMED   9418884
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Henry,R.W., Ma,B., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     Cloning and characterization of SNAP50, a subunit of the
            snRNA-activating protein complex SNAPc
  JOURNAL   EMBO J 15 (24), 7129-7136 (1996)
   PUBMED   9003788
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Yoon,J.B. and Roeder,R.G.
  TITLE     Cloning of two proximal sequence element-binding transcription
            factor subunits (gamma and delta) that are required for
            transcription of small nuclear RNA genes by RNA polymerases II and
            III and interact with the TATA-binding protein
  JOURNAL   Mol Cell Biol 16 (1), 1-9 (1996)
   PUBMED   8524284
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Henry,R.W., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     A TBP-TAF complex required for transcription of human snRNA genes
            by RNA polymerase II and III
  JOURNAL   Nature 374 (6523), 653-656 (1995)
   PUBMED   7715707
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK314933.1 and BC014984.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.221889.1,
                                           SRR3476690.931522.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216294.5/ ENSP00000216294.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..368
                     /product="snRNA-activating protein complex subunit 1"
                     /note="PTF subunit gamma; SNAPc 43 kDa subunit;
                     PSE-binding factor subunit gamma; snRNA-activating protein
                     complex 43 kDa subunit; proximal sequence element-binding
                     transcription factor subunit gamma; SNAPc subunit 1; small
                     nuclear RNA activating complex, polypeptide 1, 43kD; small
                     nuclear RNA activating complex, polypeptide 1, 43kDa"
                     /calculated_mol_wt=42863
     Region          1..168
                     /region_name="SNAPC3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16533.1)"
     Region          7..191
                     /region_name="SNAPC1"
                     /note="Small nuclear RNA activating complex (SNAPc),
                     subunit 1; pfam09808"
                     /db_xref="CDD:430842"
     Region          164..268
                     /region_name="SNAPC4-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16533.1)"
     Region          224..257
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16533.1)"
     Region          275..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16533.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16533.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16533.1)"
     CDS             1..368
                     /gene="SNAPC1"
                     /gene_synonym="PTFgamma; SNAP43"
                     /coded_by="NM_003082.4:42..1148"
                     /db_xref="CCDS:CCDS9755.1"
                     /db_xref="GeneID:6617"
                     /db_xref="HGNC:HGNC:11134"
                     /db_xref="MIM:600591"
ORIGIN      
        1 mgtppglqtd ceallsrfqe tdsvrfedft elwrnmkfgt ifcgrmrnle knmftkeala
       61 lawryflppy tfqirvgaly llyglyntql cqpkqkirva lkdwdevlkf qqdlvnaqhf
      121 daayifrklr ldrafhftam pkllsyrmkk kihraevtee fkdpsdrvmk litsdvleem
      181 lnvhdhyqnm khvisvdksk pdkalslikd dffdnikniv lehqqwhkdr knpslksktn
      241 dgeekmegns qetercerae slakikskaf svviqasksr rhrqvkldss dsdsasgqgq
      301 vkatrkkekk erlkpagrkm slrnkgnvqn ihkedkplsl smpviteeee neslsgteft
      361 askkrrkh
//
LOCUS       NP_065083                159 aa            linear   PRI 27-APR-2025
DEFINITION  type-1 angiotensin II receptor-associated protein isoform a [Homo
            sapiens].
ACCESSION   NP_065083
VERSION     NP_065083.3
DBSOURCE    REFSEQ: accession NM_020350.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Wang,D., Jin,X., Lei,M., Jiang,Y., Liu,Y., Yu,F., Guo,Y., Han,B.,
            Yang,Y., Sun,W., Liu,Y., Zeng,G., Liu,F., Hu,J. and Chen,X.
  TITLE     USF1-ATRAP-PBX3 Axis Promote Breast Cancer Glycolysis and Malignant
            Phenotype by Activating AKT/mTOR Signaling
  JOURNAL   Int J Biol Sci 18 (6), 2452-2471 (2022)
   PUBMED   35414770
  REMARK    GeneRIF: USF1-ATRAP-PBX3 Axis Promote Breast Cancer Glycolysis and
            Malignant Phenotype by Activating AKT/mTOR Signaling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Guo,T., Dai,Z., You,K., Battaglia-Hsu,S.F., Feng,J., Wang,F.,
            Li,B., Yang,J. and Li,Z.
  TITLE     S-adenosylmethionine upregulates the angiotensin receptor-binding
            protein ATRAP via the methylation of HuR in NAFLD
  JOURNAL   Cell Death Dis 12 (4), 306 (2021)
   PUBMED   33753727
  REMARK    GeneRIF: S-adenosylmethionine upregulates the angiotensin
            receptor-binding protein ATRAP via the methylation of HuR in NAFLD.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Wakui,H.
  TITLE     The pathophysiological role of angiotensin receptor-binding protein
            in hypertension and kidney diseases: Oshima Award Address 2019
  JOURNAL   Clin Exp Nephrol 24 (4), 289-294 (2020)
   PUBMED   32112267
  REMARK    GeneRIF: The pathophysiological role of angiotensin
            receptor-binding protein in hypertension and kidney diseases:
            Oshima Award Address 2019.
            Review article
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Yamaji,T., Yamashita,A., Wakui,H., Azushima,K., Uneda,K.,
            Fujikawa,Y., Haku,S., Kobayashi,R., Ohki,K., Haruhara,K.,
            Kinguchi,S., Ishii,T., Yamada,T., Urate,S., Suzuki,T., Abe,E.,
            Tanaka,S., Kamimura,D., Ishigami,T., Toya,Y., Takahashi,H. and
            Tamura,K.
  TITLE     Angiotensin II type 1 receptor-associated protein deficiency
            attenuates sirtuin1 expression in an immortalised human renal
            proximal tubule cell line
  JOURNAL   Sci Rep 9 (1), 16550 (2019)
   PUBMED   31719572
  REMARK    GeneRIF: Angiotensin II type 1 receptor-associated protein
            deficiency attenuates sirtuin1 expression in an immortalised human
            renal proximal tubule cell line.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Lopez-Ilasaca,M., Liu,X., Tamura,K. and Dzau,V.J.
  TITLE     The angiotensin II type I receptor-associated protein, ATRAP, is a
            transmembrane protein and a modulator of angiotensin II signaling
  JOURNAL   Mol Biol Cell 14 (12), 5038-5050 (2003)
   PUBMED   12960423
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Wang,W., Huang,Y., Zhou,Z., Tang,R., Zhao,W., Zeng,L., Xu,M.,
            Cheng,C., Gu,S., Ying,K., Xie,Y. and Mao,Y.
  TITLE     Identification and characterization of AGTRAP, a human homolog of
            murine Angiotensin II Receptor-Associated Protein (Agtrap)
  JOURNAL   Int J Biochem Cell Biol 34 (1), 93-102 (2002)
   PUBMED   11733189
  REMARK    GeneRIF: cloned a new human gene cDNA that codes for a homolog of
            the murine Agtrap protein
REFERENCE   9  (residues 1 to 159)
  AUTHORS   Cui,T., Nakagami,H., Iwai,M., Takeda,Y., Shiuchi,T., Tamura,K.,
            Daviet,L. and Horiuchi,M.
  TITLE     ATRAP, novel AT1 receptor associated protein, enhances
            internalization of AT1 receptor and inhibits vascular smooth muscle
            cell growth
  JOURNAL   Biochem Biophys Res Commun 279 (3), 938-941 (2000)
   PUBMED   11162453
REFERENCE   10 (residues 1 to 159)
  AUTHORS   Daviet,L., Lehtonen,J.Y., Tamura,K., Griese,D.P., Horiuchi,M. and
            Dzau,V.J.
  TITLE     Cloning and characterization of ATRAP, a novel protein that
            interacts with the angiotensin II type 1 receptor
  JOURNAL   J Biol Chem 274 (24), 17058-17062 (1999)
   PUBMED   10358057
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI117521.1, AF312374.1,
            BC017328.2, AI741916.1 and BQ672962.1.
            
            On Apr 26, 2006 this sequence version replaced NP_065083.2.
            
            Summary: This gene encodes a transmembrane protein localized to the
            plasma membrane and perinuclear vesicular structures. The gene
            product interacts with the angiotensin II type I receptor and
            negatively regulates angiotensin II signaling. Alternative splicing
            of this gene generates multiple transcript variants encoding
            different isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant represents the most common
            transcript and encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP355708.1, AK290042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000314340.10/ ENSP00000319713.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..159
                     /product="type-1 angiotensin II receptor-associated
                     protein isoform a"
                     /note="angiotensin II, type I receptor-associated protein;
                     ATI receptor-associated protein; type-1 angiotensin II
                     receptor-associated protein; AT1 receptor-associated
                     protein"
                     /calculated_mol_wt=17288
     Region          9..154
                     /region_name="AGTRAP"
                     /note="Angiotensin II, type I receptor-associated protein
                     (AGTRAP); pfam06396"
                     /db_xref="CDD:461896"
     Site            24..44
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6RW13.1)"
     Site            56..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6RW13.1)"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6RW13.1)"
     Region          110..122
                     /region_name="Interaction with AGTR1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6RW13.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6RW13.1)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6RW13.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6RW13.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6RW13.1)"
     Region          140..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6RW13.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6RW13.1)"
     CDS             1..159
                     /gene="AGTRAP"
                     /gene_synonym="ATRAP"
                     /coded_by="NM_020350.5:74..553"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS136.1"
                     /db_xref="GeneID:57085"
                     /db_xref="HGNC:HGNC:13539"
                     /db_xref="MIM:608729"
ORIGIN      
        1 melpavnlkv illghwlltt wgcivfsgsy awanftilal gvwavaqrds idaismflgg
       61 llatifldiv hisifyprvs ltdtgrfgvg mailslllkp lsccfvyhmy rerggellvh
      121 tgflgssqdr sayqtidsae apadpfavpe grsqdargy
//
LOCUS       NP_064550                495 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RAD18 [Homo sapiens].
ACCESSION   NP_064550
VERSION     NP_064550.3
DBSOURCE    REFSEQ: accession NM_020165.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Jiang,B., Yan,B., Yang,H., Geng,H. and Li,P.
  TITLE     Transcription Factor E2F7 Hampers the Killing Effect of NK Cells
            against Colorectal Cancer Cells via Activating RAD18 Transcription
  JOURNAL   J Microbiol Biotechnol 34 (4), 920-929 (2024)
   PUBMED   38073330
  REMARK    GeneRIF: Transcription Factor E2F7 Hampers the Killing Effect of NK
            Cells against Colorectal Cancer Cells via Activating RAD18
            Transcription.
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Shimada,M., Tokumiya,T., Miyake,T., Tsukada,K., Kanzaki,N.,
            Yanagihara,H., Kobayashi,J. and Matsumoto,Y.
  TITLE     Implication of E3 ligase RAD18 in UV-induced mutagenesis in human
            induced pluripotent stem cells and neuronal progenitor cells
  JOURNAL   J Radiat Res 64 (2), 345-351 (2023)
   PUBMED   36634340
  REMARK    GeneRIF: Implication of E3 ligase RAD18 in UV-induced mutagenesis
            in human induced pluripotent stem cells and neuronal progenitor
            cells.
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Wells,J.P., Chang,E.Y., Dinatto,L., White,J., Ryall,S. and
            Stirling,P.C.
  TITLE     RAD18 opposes transcription-associated genome instability through
            FANCD2 recruitment
  JOURNAL   PLoS Genet 18 (12), e1010309 (2022)
   PUBMED   36480547
  REMARK    GeneRIF: RAD18 opposes transcription-associated genome instability
            through FANCD2 recruitment.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Yu,R., Hu,Y., Zhang,S., Li,X., Tang,M., Yang,M., Wu,X., Li,Z.,
            Liao,X., Xu,Y., Li,M., Chen,S., Qian,W., Gong,L.Y., Song,L. and
            Li,J.
  TITLE     LncRNA CTBP1-DT-encoded microprotein DDUP sustains DNA damage
            response signalling to trigger dual DNA repair mechanisms
  JOURNAL   Nucleic Acids Res 50 (14), 8060-8079 (2022)
   PUBMED   35849344
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Du,M., Gu,J., Liu,C., Liu,N., Yu,Z., Zhou,C., Heng,W., Cao,Z.,
            Wei,F., Zhu,K., Wang,Y., Zhang,W., Xue,X., Zhang,Y. and Qian,J.
  TITLE     Genome-wide CRISPR screen identified Rad18 as a determinant of
            doxorubicin sensitivity in osteosarcoma
  JOURNAL   J Exp Clin Cancer Res 41 (1), 154 (2022)
   PUBMED   35459258
  REMARK    GeneRIF: Genome-wide CRISPR screen identified Rad18 as a
            determinant of doxorubicin sensitivity in osteosarcoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Nikiforov,A.A., Sasina,L.K., Svetlova,M.P., Solovjeva,L.V.,
            Oei,S.L., Bradbury,E.M. and Tomilin,N.V.
  TITLE     Early immobilization of nuclease FEN1 and accumulation of hRAD18
            protein at stalled DNA replication forks in mammalian cells
  JOURNAL   Dokl Biochem Biophys 389, 122-125 (2003)
   PUBMED   12856420
  REMARK    GeneRIF: action at DNA replication forks
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Mulder,L.C., Chakrabarti,L.A. and Muesing,M.A.
  TITLE     Interaction of HIV-1 integrase with DNA repair protein hRad18
  JOURNAL   J Biol Chem 277 (30), 27489-27493 (2002)
   PUBMED   12016221
  REMARK    GeneRIF: hRad18 is a novel interacting partner of HIV-1 integrase;
            role for post-replication/translesion DNA repair in the retroviral
            integration process.
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Xin,H., Lin,W., Sumanasekera,W., Zhang,Y., Wu,X. and Wang,Z.
  TITLE     The human RAD18 gene product interacts with HHR6A and HHR6B
  JOURNAL   Nucleic Acids Res 28 (14), 2847-2854 (2000)
   PUBMED   10908344
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Tateishi,S., Sakuraba,Y., Masuyama,S., Inoue,H. and Yamaizumi,M.
  TITLE     Dysfunction of human Rad18 results in defective postreplication
            repair and hypersensitivity to multiple mutagens
  JOURNAL   Proc Natl Acad Sci U S A 97 (14), 7927-7932 (2000)
   PUBMED   10884424
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DW433240.1, AK023075.1,
            AC034186.5 and AC008151.1.
            
            On Aug 29, 2009 this sequence version replaced NP_064550.2.
            
            Summary: The protein encoded by this gene is highly similar to S.
            cerevisiae DNA damage repair protein Rad18. Yeast Rad18 functions
            through its interaction with Rad6, which is an
            ubiquitin-conjugating enzyme required for post-replication repair
            of damaged DNA. Similar to its yeast counterpart, this protein is
            able to interact with the human homolog of yeast Rad6 protein
            through a conserved ring-finger motif.  Mutation of this motif
            results in defective replication of UV-damaged DNA and
            hypersensitivity to multiple mutagens. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.211327.1,
                                           SRR1660807.200457.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264926.7/ ENSP00000264926.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..495
                     /product="E3 ubiquitin-protein ligase RAD18"
                     /EC_number="2.3.2.27"
                     /note="postreplication repair protein hRAD18p; RAD18, S.
                     cerevisiae, homolog; hHR18; RING finger protein 73;
                     postreplication repair protein RAD18; RAD18 homolog;
                     RING-type E3 ubiquitin transferase RAD18"
                     /calculated_mol_wt=56092
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NS91.2)"
     Region          13..363
                     /region_name="rad18"
                     /note="DNA repair protein rad18; TIGR00599"
                     /db_xref="CDD:273165"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NS91.2)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NS91.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NS91.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NS91.2)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NS91.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NS91.2)"
     Region          152..197
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NS91.2)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NS91.2)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NS91.2)"
     Region          232..240
                     /region_name="LR motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NS91.2)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NS91.2)"
     Region          400..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NS91.2)"
     Region          456..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NS91.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NS91.2)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NS91.2)"
     CDS             1..495
                     /gene="RAD18"
                     /gene_synonym="RNF73"
                     /coded_by="NM_020165.4:88..1575"
                     /db_xref="CCDS:CCDS2571.1"
                     /db_xref="GeneID:56852"
                     /db_xref="HGNC:HGNC:18278"
                     /db_xref="MIM:605256"
ORIGIN      
        1 mdslaesrwp pglavmktid dllrcgicfe yfniamiipq cshnycslci rkflsyktqc
       61 ptccvtvtep dlknnrilde lvkslnfarn hllqfalesp akspassssk nlavkvytpv
      121 asrqslkqgs rlmdnflire msgstselli kenkskfspq keaspaaktk etrsveeiap
      181 dpseakrpep pststlkqvt kvdcpvcgvn ipeshinkhl dsclsreekk eslrssvhkr
      241 kplpktvynl lsdrdlkkkl kehglsiqgn kqqlikrhqe fvhmynaqcd alhpksaaei
      301 vreieniekt rmrleaskln esvmvftkdq tekeideihs kyrkkhksef qllvdqarkg
      361 ykkiagmsqk tvtitkedes teklssvcmg qednmtsvtn hfsqskldsp eelepdreed
      421 ssscidiqev lsssesdscn ssssdiirdl leeeeaweas hkndlqdtei sprqnrrtra
      481 aesaeieprn krnrn
//
LOCUS       NP_835470                341 aa            linear   PRI 27-APR-2025
DEFINITION  2-acylglycerol O-acyltransferase 3 isoform a [Homo sapiens].
ACCESSION   NP_835470
VERSION     NP_835470.1
DBSOURCE    REFSEQ: accession NM_178176.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Ma,Z., Onorato,J.M., Chen,L., Nelson,D.W., Yen,C.E. and Cheng,D.
  TITLE     Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid
            acyltransferases
  JOURNAL   J Lipid Res 58 (6), 1091-1099 (2017)
   PUBMED   28420705
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Brandt,C., McFie,P.J. and Stone,S.J.
  TITLE     Biochemical characterization of human acyl coenzyme A:
            2-monoacylglycerol acyltransferase-3 (MGAT3)
  JOURNAL   Biochem Biophys Res Commun 475 (3), 264-270 (2016)
   PUBMED   27184406
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Cheng,D., Nelson,T.C., Chen,J., Walker,S.G., Wardwell-Swanson,J.,
            Meegalla,R., Taub,R., Billheimer,J.T., Ramaker,M. and Feder,J.N.
  TITLE     Identification of acyl coenzyme A:monoacylglycerol acyltransferase
            3, an intestinal specific enzyme implicated in dietary fat
            absorption
  JOURNAL   J Biol Chem 278 (16), 13611-13614 (2003)
   PUBMED   12618427
  REMARK    GeneRIF: MGAT3 encodes a approximately 36-kDa transmembrane protein
            that is highly homologous to MGAT1 and -2 and is expressed in the
            human gastrointestinal tract with the highest level found in the
            ileum
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Winter,A., van Eckeveld,M., Bininda-Emonds,O.R., Habermann,F.A. and
            Fries,R.
  TITLE     Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos
            taurus) and other mammals
  JOURNAL   Cytogenet Genome Res 102 (1-4), 42-47 (2003)
   PUBMED   14970677
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004876.2, AY229854.1 and BE042458.1.
            
            Summary: Acyl-CoA:monoacylglycerol acyltransferase (MOGAT; EC
            2.3.1.22) catalyzes the synthesis of diacylglycerol from
            2-monoacylglycerol and fatty acyl-CoA (Cheng et al., 2003 [PubMed
            12618427]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY229854.1, AY358200.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000223114.9/ ENSP00000223114.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..341
                     /product="2-acylglycerol O-acyltransferase 3 isoform a"
                     /EC_number="2.3.1.20"
                     /EC_number="2.3.1.22"
                     /note="acyl coenzyme A:monoacylglycerol acyltransferase 3;
                     2-acylglycerol O-acyltransferase 3;
                     acyl-CoA:monoacylglycerol acyltransferase 3;
                     diacylglycerol O-acyltransferase candidate 7;
                     diacylglycerol acyltransferase 2-like protein 7"
                     /calculated_mol_wt=38599
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VF5.1)"
     Region          45..340
                     /region_name="LPLAT"
                     /note="Lysophospholipid acyltransferases (LPLATs) of
                     glycerophospholipid biosynthesis; cl17185"
                     /db_xref="CDD:473073"
     Site            50..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VF5.1)"
     Site            order(116,119,121,142..145,193..195)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86VF5.1)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VF5.1)"
     CDS             1..341
                     /gene="MOGAT3"
                     /gene_synonym="DC7; DGAT2L2; MGAT3"
                     /coded_by="NM_178176.4:183..1208"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5714.1"
                     /db_xref="GeneID:346606"
                     /db_xref="HGNC:HGNC:23249"
                     /db_xref="MIM:610184"
ORIGIN      
        1 mgvattlqpp ttsktlqkqh leavgayqyv ltflfmgpff sllvfvllft slwpfsvfyl
       61 vwlyvdwdtp nqggrrsewi rnraiwrqlr dyypvklvkt aelppdrnyv lgahphgimc
      121 tgflcnfste sngfsqlfpg lrpwlavlag lfylpvyrdy imsfglcpvs rqsldfilsq
      181 pqlgqavvim vggahealys vpgehcltlq krkgfvrlal rhgaslvpvy sfgendifrl
      241 kafatgswqh wcqltfkklm gfspcifwgr glfsatswgl lpfavpittv vgrpipvpqr
      301 lhpteeevnh yhalymtale qlfeehkesc gvpastcltf i
//
LOCUS       NP_001077064             195 aa            linear   MAM 27-APR-2025
DEFINITION  interferon omega-1 precursor [Equus caballus].
ACCESSION   NP_001077064
VERSION     NP_001077064.1
DBSOURCE    REFSEQ: accession NM_001083595.3
KEYWORDS    RefSeq.
SOURCE      Equus caballus (horse)
  ORGANISM  Equus caballus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Himmler,A., Hauptmann,R., Adolf,G.R. and Swetly,P.
  TITLE     Molecular cloning and expression in Escherichia coli of equine type
            I interferons
  JOURNAL   DNA 5 (5), 345-356 (1986)
   PUBMED   3022999
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M14544.1.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Equus caballus"
                     /db_xref="taxon:9796"
                     /chromosome="23"
                     /map="23"
     Protein         1..195
                     /product="interferon omega-1 precursor"
                     /note="interferon alpha-II-1; IFN-omega 1; interferon
                     1BF1; interferon omega-1"
                     /calculated_mol_wt=19582
     sig_peptide     1..23
                     /note="interferon-omega-1 signal peptide"
                     /calculated_mol_wt=2318
     mat_peptide     24..195
                     /product="interferon omega-1"
                     /calculated_mol_wt=19582
     Region          26..185
                     /region_name="Interferon"
                     /note="Interferon alpha/beta domain; pfam00143"
                     /db_xref="CDD:459689"
     Site            order(28..29,32,35..36,39,42..43,100..101,103..104,
                     106..107,110,113..114,117..118,121)
                     /site_type="active"
                     /note="putative IFNAR-1 binding site [active]"
                     /db_xref="CDD:238047"
     Site            order(53..60,62..64,70..71,141..142,144..145,148..149,
                     151..152,155..160)
                     /site_type="active"
                     /note="putative IFNAR-2 binding site [active]"
                     /db_xref="CDD:238047"
     Site            101
                     /site_type="other"
                     /note="N-glycosylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238047"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05001.1)"
     CDS             1..195
                     /gene="IFN-OMEGA1"
                     /gene_synonym="IF1BF1"
                     /coded_by="NM_001083595.3:1413..2000"
                     /db_xref="GeneID:100036553"
ORIGIN      
        1 mafsvsslma lvvissspvs smscdlpasl dlrkqetlrv lhqmetispp sclkhrtdfr
       61 fpqeqldgrq fpeaqatsvl qemlqqivsl fhterssaaw nttlldrlla glhqqledln
      121 tcldeqtgee esalgtvgpt lavkryfrri rlyltekkys dcaweivrvd imrsfsssan
      181 lqgrlgmkdg dlgsp
//
LOCUS       NP_003278                204 aa            linear   PRI 27-APR-2025
DEFINITION  tumor protein D53 isoform 1 [Homo sapiens].
ACCESSION   NP_003278
VERSION     NP_003278.1
DBSOURCE    REFSEQ: accession NM_003287.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Cao,Q., Chen,J., Zhu,L., Liu,Y., Zhou,Z., Sha,J., Wang,S. and Li,J.
  TITLE     A testis-specific and testis developmentally regulated tumor
            protein D52 (TPD52)-like protein TPD52L3/hD55 interacts with TPD52
            family proteins
  JOURNAL   Biochem Biophys Res Commun 344 (3), 798-806 (2006)
   PUBMED   16631610
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Nourse,C.R., Mattei,M.G., Gunning,P. and Byrne,J.A.
  TITLE     Cloning of a third member of the D52 gene family indicates
            alternative coding sequence usage in D52-like transcripts
  JOURNAL   Biochim Biophys Acta 1443 (1-2), 155-168 (1998)
   PUBMED   9838088
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Byrne,J.A., Nourse,C.R., Basset,P. and Gunning,P.
  TITLE     Identification of homo- and heteromeric interactions between
            members of the breast carcinoma-associated D52 protein family using
            the yeast two-hybrid system
  JOURNAL   Oncogene 16 (7), 873-881 (1998)
   PUBMED   9484778
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Byrne,J.A., Mattei,M.G., Basset,P. and Gunning,P.
  TITLE     Identification and in situ hybridization mapping of a mouse Tpd52l1
            (D53) orthologue to chromosome 10A4-B2
  JOURNAL   Cytogenet Cell Genet 81 (3-4), 199-201 (1998)
   PUBMED   9730602
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Byrne,J.A., Mattei,M.G. and Basset,P.
  TITLE     Definition of the tumor protein D52 (TPD52) gene family through
            cloning of D52 homologues in human (hD53) and mouse (mD52)
  JOURNAL   Genomics 35 (3), 523-532 (1996)
   PUBMED   8812487
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Byrne,J.A., Tomasetto,C., Garnier,J.M., Rouyer,N., Mattei,M.G.,
            Bellocq,J.P., Rio,M.C. and Basset,P.
  TITLE     A screening method to identify genes commonly overexpressed in
            carcinomas and the identification of a novel complementary DNA
            sequence
  JOURNAL   Cancer Res 55 (13), 2896-2903 (1995)
   PUBMED   7796418
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U44427.1, U44429.1, AL121938.10
            and AI222450.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of a family of proteins that
            contain coiled-coil domains and may form hetero- or homomers. The
            encoded protein is involved in cell proliferation and calcium
            signaling. It also interacts with the mitogen-activated protein
            kinase kinase kinase 5 (MAP3K5/ASK1) and positively regulates
            MAP3K5-induced apoptosis. Multiple alternatively spliced transcript
            variants have been observed. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.277719.1, U44427.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000534000.6/ ENSP00000434142.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31"
     Protein         1..204
                     /product="tumor protein D53 isoform 1"
                     /note="tumor protein D53; tumor protein D52 like 1"
                     /calculated_mol_wt=22318
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16890.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     Region          44..151
                     /region_name="TPD52"
                     /note="Tumour protein D52 family; pfam04201"
                     /db_xref="CDD:461225"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     Site            133
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q16890.1)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     CDS             1..204
                     /gene="TPD52L1"
                     /gene_synonym="D53; TPD53"
                     /coded_by="NM_003287.4:180..794"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5130.1"
                     /db_xref="GeneID:7164"
                     /db_xref="HGNC:HGNC:12006"
                     /db_xref="MIM:604069"
ORIGIN      
        1 meaqaqglle teplqgtded avasadfssm lseeekeelk aelvqledei ttlrqvlsak
       61 erhlveikqk lgmnlmnelk qnfskswhdm qtttaykkth etlshagqka taafsnvgta
      121 iskkfgdmsy sirhsismpa mrnsptfksf eervettvts lktkvggtnp nggsfeevls
      181 stahasaqsl aggsrrtkee elqc
//
LOCUS       NP_001355634             899 aa            linear   ROD 27-APR-2025
DEFINITION  DNA damage-induced apoptosis suppressor protein [Mus musculus].
ACCESSION   NP_001355634 XP_006508309
VERSION     NP_001355634.1
DBSOURCE    REFSEQ: accession NM_001368705.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 899)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 899)
  AUTHORS   Nakaya,N., Hemish,J., Krasnov,P., Kim,S.Y., Stasiv,Y.,
            Michurina,T., Herman,D., Davidoff,M.S., Middendorff,R. and
            Enikolopov,G.
  TITLE     noxin, a novel stress-induced gene involved in cell cycle and
            apoptosis
  JOURNAL   Mol Cell Biol 27 (15), 5430-5444 (2007)
   PUBMED   17515607
  REMARK    GeneRIF: Noxin may be a component of the cell defense system: it is
            activated by various stress stimuli, helps cells to withdraw from
            cycling, and opposes apoptosis.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158138.13.
            
            On Feb 20, 2019 this sequence version replaced XP_006508309.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3739802.1,
                                           SRR11927938.2224177.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164139, SAMN01164142
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..899
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 51.64 cM"
     Protein         1..899
                     /product="DNA damage-induced apoptosis suppressor protein"
                     /note="nitric oxide-inducible gene protein"
                     /calculated_mol_wt=99983
     Region          8..>102
                     /region_name="Replication protein A, class 2b
                     aminoacyl-tRNA synthetases, and related proteins with
                     oligonucleotide/oligosaccharide (OB) fold."
                     /note="This superfamily includes two
                     oligonucleotide/oligosaccharide binding fold (OBF) domain
                     families. One of these contains the OBF domains of the
                     large (RPA1, 70kDa), middle (RPA2, RPA4, 32kDa) and small
                     (RPA3, 14 kDa) subunits of human heterotrimeric...;
                     cl09930"
                     /db_xref="CDD:471953"
     CDS             1..899
                     /gene="Ddias"
                     /gene_synonym="4632434I11Rik; noxin"
                     /coded_by="NM_001368705.1:294..2993"
                     /db_xref="CCDS:CCDS40022.1"
                     /db_xref="GeneID:74041"
                     /db_xref="MGI:MGI:1921291"
ORIGIN      
        1 mnkrrkflfa svlavqnwnf iypscqrcfs kiileskrft cpkcgssgdt gstnyrykls
       61 lkvaessklf fitvfgscld tffgltatgl hryledsikn letldsgrtq sllttavekc
      121 fvgqsfvfgv tnfgdvcghd sdssnfqqpc cklrgevrtl vasqiilpsp hvkgftviay
      181 lhpllhkkph cgsqehssqs ltsddsdsdl nniqgsgnts wfsessvged ffrfwepsle
      241 ltssdsqvts sddfpaskqi masgtpnqnr hcisvsevts sknchdslqs lwslhscmdk
      301 nnttgklgee lglpspvcns chesrlsdsh ffpsqmqepf eehnlecysk agkddysqyd
      361 iacyqhyevn ttpilqqrss afslsslkpe etanpsqnsd sliwddlpls eslnkflavv
      421 esevavteid aknrkqgmdk sidkchknys rlsltpwknt rplntssfsl rssqammked
      481 sgkealfsnc ksnasphiqk eskadkteaa vsiagsrsdi sedflpdtcs salftsskdr
      541 eafitqkrts gvlqqkneis crpstsisdc sdlrsryftg cgqklhsgtk gklaiqncsk
      601 kysdasdlhk lenkhrwpkk eddnfticrk ltypletlcs spesintske mpcrpsnnnl
      661 tpsssgdheg synasadlfd yiandkdigt eitkipqdnl lplevpcten ypinenrgqp
      721 sqklslqsis psrysrprsq sdsecdfees qdfvpcsqst pvagfhqrih glngaskilp
      781 siysnpnany knrknspltg qyeatsacsk nvkafrqkpe spfvssltqa nvfnhcpaae
      841 slendvdewv ppttkkvfis dilgfrvmgl rkcldlhysp dpkelprkkl ikvthktni
//
LOCUS       NP_766078                504 aa            linear   ROD 27-APR-2025
DEFINITION  O-phosphoseryl-tRNA(Sec) selenium transferase isoform 1 [Mus
            musculus].
ACCESSION   NP_766078
VERSION     NP_766078.1
DBSOURCE    REFSEQ: accession NM_172490.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Fradejas-Villar,N., Zhao,W., Reuter,U., Doengi,M., Ingold,I.,
            Bohleber,S., Conrad,M. and Schweizer,U.
  TITLE     Missense mutation in selenocysteine synthase causes
            cardio-respiratory failure and perinatal death in mice which can be
            compensated by selenium-independent GPX4
  JOURNAL   Redox Biol 48, 102188 (2021)
   PUBMED   34794077
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Mix,H., Weiler-Normann,C., Thimme,R., Ahlenstiel,G., Shin,E.C.,
            Herkel,J., David,C.S., Lohse,A.W. and Rehermann,B.
  TITLE     Identification of CD4 T-cell epitopes in soluble liver
            antigen/liver pancreas autoantigen in autoimmune hepatitis
  JOURNAL   Gastroenterology 135 (6), 2107-2118 (2008)
   PUBMED   18773898
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Ganichkin,O.M., Xu,X.M., Carlson,B.A., Mix,H., Hatfield,D.L.,
            Gladyshev,V.N. and Wahl,M.C.
  TITLE     Structure and catalytic mechanism of eukaryotic selenocysteine
            synthase
  JOURNAL   J Biol Chem 283 (9), 5849-5865 (2008)
   PUBMED   18093968
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Xu,X.M., Carlson,B.A., Mix,H., Zhang,Y., Saira,K., Glass,R.S.,
            Berry,M.J., Gladyshev,V.N. and Hatfield,D.L.
  TITLE     Biosynthesis of selenocysteine on its tRNA in eukaryotes
  JOURNAL   PLoS Biol 5 (1), e4 (2007)
   PUBMED   17194211
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Small-Howard,A., Morozova,N., Stoytcheva,Z., Forry,E.P.,
            Mansell,J.B., Harney,J.W., Carlson,B.A., Xu,X.M., Hatfield,D.L. and
            Berry,M.J.
  TITLE     Supramolecular complexes mediate selenocysteine incorporation in
            vivo
  JOURNAL   Mol Cell Biol 26 (6), 2337-2346 (2006)
   PUBMED   16508009
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Xu,X.M., Mix,H., Carlson,B.A., Grabowski,P.J., Gladyshev,V.N.,
            Berry,M.J. and Hatfield,D.L.
  TITLE     Evidence for direct roles of two additional factors, SECp43 and
            soluble liver antigen, in the selenoprotein synthesis machinery
  JOURNAL   J Biol Chem 280 (50), 41568-41575 (2005)
   PUBMED   16230358
  REMARK    GeneRIF: SECp43 and SLA have roles in selenoprotein synthesis
            [soluble liver antigen]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC120128.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK049338.1, SRR10223970.7447.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138, SAMN01164143
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 28.44 cM"
     Protein         1..504
                     /product="O-phosphoseryl-tRNA(Sec) selenium transferase
                     isoform 1"
                     /EC_number="2.9.1.2"
                     /note="O-phosphoseryl-tRNA(Sec) selenium transferase;
                     selenocysteinyl-tRNA(Sec) synthase; UGA suppressor
                     tRNA-associated protein"
                     /calculated_mol_wt=55195
     Region          1..44
                     /region_name="Tetramerization.
                     /evidence=ECO:0000269|PubMed:18093968"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P6M7.2)"
     Region          13..458
                     /region_name="selenium_SpcS"
                     /note="O-phosphoseryl-tRNA(Sec) selenium transferase;
                     TIGR03531"
                     /db_xref="CDD:211833"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9HD40; propagated from
                     UniProtKB/Swiss-Prot (Q6P6M7.2)"
     Site            74
                     /site_type="other"
                     /note="May act as a substrate filter by repelling
                     compounds with a negatively charged alpha-carboxylate.
                     /evidence=ECO:0000269|PubMed:18093968; propagated from
                     UniProtKB/Swiss-Prot (Q6P6M7.2)"
     Region          96..106
                     /region_name="Phosphate loop (P-loop).
                     /evidence=ECO:0000269|PubMed:18093968"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P6M7.2)"
     Site            284
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99742"
     CDS             1..504
                     /gene="Sepsecs"
                     /gene_synonym="D5Ertd135e; SecS; SLA"
                     /coded_by="NM_172490.4:14..1528"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS19286.1"
                     /db_xref="GeneID:211006"
                     /db_xref="MGI:MGI:1098791"
ORIGIN      
        1 mnpesfaage rrvspayvrq gcearraheh lirllleqgk cpedgwdest lelflhelav
       61 mdsnnflgnc gvgeregrva salvarrhyr fihgigrsgd isavqpkaag ssllnkitns
      121 lvlnviklag vhsvascfvv pmatgmsltl cfltlrhkrp kakyiiwpri dqkscfksmv
      181 tagfepvvie nvlegdelrt dlkaveakiq elgpehilcl hsttacfapr vpdrleelav
      241 icanydiphv vnnayglqss kcmhliqqga rvgridafvq sldknfmvpv ggaiiagfne
      301 pfiqdiskmy pgrasaspsl dvlitllslg csgyrkllke rkemfvylst qlkklaeahn
      361 erllqtphnp islamtlkti dghhdkavtq lgsmlftrqv sgaravplgn vqtvsghtfr
      421 gfmshadnyp caylnaaaai gmkmqdvdlf ikrldkclni vrkeqtrasv vsgadrnkae
      481 dadieemalk lddvlgdvgq gpal
//
LOCUS       NP_075801                144 aa            linear   ROD 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 [Mus
            musculus].
ACCESSION   NP_075801
VERSION     NP_075801.1
DBSOURCE    REFSEQ: accession NM_023312.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Ren,J., Che,Y., Li,H., Gao,H., Wang,Y., Wang,Y., Su,H., Li,Z.,
            Li,J. and Qu,P.
  TITLE     SGK3 deficiency in macrophages suppresses angiotensin II-induced
            cardiac remodeling via regulating Ndufa13-mediated mitochondrial
            oxidative stress
  JOURNAL   Cell Mol Life Sci 81 (1), 359 (2024)
   PUBMED   39158709
  REMARK    GeneRIF: SGK3 deficiency in macrophages suppresses angiotensin
            II-induced cardiac remodeling via regulating Ndufa13-mediated
            mitochondrial oxidative stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Wu,Y., Chen,S., Huang,G., Zhang,L., Zhong,L., Feng,Y., Wen,P. and
            Liu,J.
  TITLE     Transcriptome analysis reveals EBF1 ablation-induced injuries in
            cardiac system
  JOURNAL   Theranostics 14 (12), 4894-4915 (2024)
   PUBMED   39239522
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Vercellino,I. and Sazanov,L.A.
  TITLE     SCAF1 drives the compositional diversity of mammalian respirasomes
  JOURNAL   Nat Struct Mol Biol 31 (7), 1061-1071 (2024)
   PUBMED   38575788
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Wang,B., Yang,Y., Ye,J., Han,X., Yang,L., Huang,Y. and Chao,L.
  TITLE     GRIM-19 deficiency promotes macrophage polarization to the M1
            phenotype partly through glycolysis in unexplained recurrent
            spontaneous abortiondagger
  JOURNAL   Biol Reprod 110 (4), 739-749 (2024)
   PUBMED   38206868
  REMARK    GeneRIF: GRIM-19 deficiency promotes macrophage polarization to the
            M1 phenotype partly through glycolysis in unexplained recurrent
            spontaneous abortiondagger.
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Yang,L., Yang,Y., Han,X., Huang,C., Wang,Y., Jiang,D. and Chao,L.
  TITLE     GRIM19 deficiency aggravates metabolic disorder and ovarian
            dysfunction in PCOS
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (4), 167063 (2024)
   PUBMED   38360073
  REMARK    GeneRIF: GRIM19 deficiency aggravates metabolic disorder and
            ovarian dysfunction in PCOS.
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Lufei,C., Ma,J., Huang,G., Zhang,T., Novotny-Diermayr,V., Ong,C.T.
            and Cao,X.
  TITLE     GRIM-19, a death-regulatory gene product, suppresses Stat3 activity
            via functional interaction
  JOURNAL   EMBO J 22 (6), 1325-1335 (2003)
   PUBMED   12628925
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Seo,T., Lee,D., Shim,Y.S., Angell,J.E., Chidambaram,N.V.,
            Kalvakolanu,D.V. and Choe,J.
  TITLE     Viral interferon regulatory factor 1 of Kaposi's sarcoma-associated
            herpesvirus interacts with a cell death regulator, GRIM19, and
            inhibits interferon/retinoic acid-induced cell death
  JOURNAL   J Virol 76 (17), 8797-8807 (2002)
   PUBMED   12163600
  REMARK    GeneRIF: results collectively indicate that viral interferon
            regulatory factor 1 modulates interferon/retinoic acid-cell death
            signals via interactions with GRIM19
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Angell,J.E., Lindner,D.J., Shapiro,P.S., Hofmann,E.R. and
            Kalvakolanu,D.V.
  TITLE     Identification of GRIM-19, a novel cell death-regulatory gene
            induced by the interferon-beta and retinoic acid combination, using
            a genetic approach
  JOURNAL   J Biol Chem 275 (43), 33416-33426 (2000)
   PUBMED   10924506
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Moore,A.B., He,H., Yoshida,A., Rico,P.J., Haseman,J.K. and Dixon,D.
  TITLE     Transforming growth factor-alpha, epidermal growth factor receptor,
            and PCNA immunoexpression in uterine leiomyosarcomas and leiomyomas
            in B6C3F1 mice
  JOURNAL   Exp Toxicol Pathol 52 (3), 195-200 (2000)
   PUBMED   10930119
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158564.7.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034899.1, SRR7345562.3275072.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 34.03 cM"
     Protein         1..144
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 13"
                     /EC_number="7.1.1.2"
                     /note="genes associated with retinoid-IFN-induced
                     mortality 19; complex I-B16.6; cell death regulatory
                     protein GRIM-19; NADH-ubiquinone oxidoreductase B16.6
                     subunit; gene associated with retinoic-interferon-induced
                     mortality 19 protein; gene associated with retinoic and
                     IFN-induced mortality 19 protein; gene associated with
                     retinoic and interferon-induced mortality 19 protein; NADH
                     dehydrogenase (ubiquinone) 1 alpha subcomplex, 13"
                     /calculated_mol_wt=16729
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q95KV7; propagated from
                     UniProtKB/Swiss-Prot (Q9ERS2.3)"
     Region          5..128
                     /region_name="GRIM-19"
                     /note="GRIM-19 protein; pfam06212"
                     /db_xref="CDD:461852"
     Site            30..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERS2.3)"
     CDS             1..144
                     /gene="Ndufa13"
                     /gene_synonym="2700054G14Rik; CDA016; CGI-39; CI-B16.6;
                     GRIM-19; Grim19"
                     /coded_by="NM_023312.3:776..1210"
                     /db_xref="CCDS:CCDS22353.1"
                     /db_xref="GeneID:67184"
                     /db_xref="MGI:MGI:1914434"
ORIGIN      
        1 maaskvkqdm pppggygpid ykrnlprrgl sgysmfavgi galifgywrm mrwnqerrrl
       61 liedlearia lmplfqaekd rrtlqilren leeeaiimkd vpnwkvgesv fhttrwvppl
      121 igemyglrtk eemsnanfgf twyt
//
LOCUS       NP_001013210             402 aa            linear   ROD 27-APR-2025
DEFINITION  olfactomedin-like protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_001013210 XP_341900
VERSION     NP_001013210.1
DBSOURCE    REFSEQ: accession NM_001013192.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081972.1.
            
            On Mar 26, 2005 this sequence version replaced XP_341900.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081972.1, FM129944.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q33"
     Protein         1..402
                     /product="olfactomedin-like protein 1 precursor"
                     /note="olfactomedin-like protein 1"
                     /calculated_mol_wt=42709
     sig_peptide     1..28
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q66H86.1)"
                     /calculated_mol_wt=2910
     mat_peptide     29..402
                     /product="Olfactomedin-like protein 1. /id=PRO_0000020091"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H86.1)"
                     /calculated_mol_wt=42709
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H86.1)"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H86.1)"
     Region          145..395
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; pfam02191"
                     /db_xref="CDD:460482"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H86.1)"
     CDS             1..402
                     /gene="Olfml1"
                     /coded_by="NM_001013192.2:304..1512"
                     /db_xref="GeneID:361621"
                     /db_xref="RGD:1311854"
ORIGIN      
        1 mmvalpgasa slvlflaafl pplqhaqdpa mvhyiyqrfq vleqglekca qttrayiqdf
       61 qefsknlstm lgrcqthtne yrsavdnlal rveraqreid ylqylresdf cveseektsa
      121 ekvlqeaeee kkirtllnts cdnmlmaiks lkivkktvdp egswmkdags tsakvyllag
      181 srnntvwefa nlrafmedsv kpgprkltlp lswqgsgqvv yqsflffhnq gtsneiikyn
      241 lqkktvedrm llpggagrap iyqhslstyi dlavdehglw aihsgpgiqg hlvltkieag
      301 tlgiehswdt pcrsqdaeas fllcgvlyvv yssggqgphr itcvydplgt vreehlpnlf
      361 fprrarshsm ihynprdkql yawnegyqii yklqtkkklp le
//
LOCUS       NP_001357123             247 aa            linear   PRI 27-APR-2025
DEFINITION  immunoglobulin-binding protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001357123
VERSION     NP_001357123.1
DBSOURCE    REFSEQ: accession NM_001370194.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Kwon,O.C., Lee,E.J., Oh,J.S., Hong,S., Lee,C.K., Yoo,B., Park,M.C.
            and Kim,Y.G.
  TITLE     Plasma immunoglobulin binding protein 1 as a predictor of
            development of lupus nephritis
  JOURNAL   Lupus 29 (6), 547-553 (2020)
   PUBMED   32183589
  REMARK    GeneRIF: Plasma immunoglobulin binding protein 1 as a predictor of
            development of lupus nephritis.
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Liu,J., Prickett,T.D., Elliott,E., Meroni,G. and Brautigan,D.L.
  TITLE     Phosphorylation and microtubule association of the Opitz syndrome
            protein mid-1 is regulated by protein phosphatase 2A via binding to
            the regulatory subunit alpha 4
  JOURNAL   Proc Natl Acad Sci U S A 98 (12), 6650-6655 (2001)
   PUBMED   11371618
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 247)
  AUTHORS   Chung,H., Nairn,A.C., Murata,K. and Brautigan,D.L.
  TITLE     Mutation of Tyr307 and Leu309 in the protein phosphatase 2A
            catalytic subunit favors association with the alpha 4 subunit which
            promotes dephosphorylation of elongation factor-2
  JOURNAL   Biochemistry 38 (32), 10371-10376 (1999)
   PUBMED   10441131
REFERENCE   9  (residues 1 to 247)
  AUTHORS   Chen,J., Peterson,R.T. and Schreiber,S.L.
  TITLE     Alpha 4 associates with protein phosphatases 2A, 4, and 6
  JOURNAL   Biochem Biophys Res Commun 247 (3), 827-832 (1998)
   PUBMED   9647778
REFERENCE   10 (residues 1 to 247)
  AUTHORS   Onda,M., Inui,S., Maeda,K., Suzuki,M., Takahashi,E. and
            Sakaguchi,N.
  TITLE     Expression and chromosomal localization of the human alpha 4/IGBP1
            gene, the structure of which is closely related to the yeast TAP42
            protein of the rapamycin-sensitive signal transduction pathway
  JOURNAL   Genomics 46 (3), 373-378 (1997)
   PUBMED   9441740
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158141.14 and AL139111.20.
            
            Summary: The proliferation and differentiation of B cells is
            dependent upon a B-cell antigen receptor (BCR) complex. Binding of
            antigens to specific B-cell receptors results in a tyrosine
            phosphorylation reaction through the BCR complex and leads to
            multiple signal transduction pathways. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.3193.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..247
                     /product="immunoglobulin-binding protein 1 isoform 2"
                     /note="protein phosphatase 2A, regulatory subunit alpha-4;
                     B cell signal transduction molecule alpha 4; bA351K23.1
                     (immunoglobulin binding protein 1 (CD79A)); protein
                     alpha-4; CD79a-binding protein 1; immunoglobulin (CD79A)
                     binding protein 1; renal carcinoma antigen NY-REN-16;
                     protein phosphatase 2/4/6 regulatory subunit"
                     /calculated_mol_wt=28221
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P78318.1)"
     Region          12..237
                     /region_name="TAP42"
                     /note="TAP42-like family; pfam04177"
                     /db_xref="CDD:461209"
     CDS             1..247
                     /gene="IGBP1"
                     /gene_synonym="ALPHA-4; alpha4; IBP1; MRXS28"
                     /coded_by="NM_001370194.1:14..757"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:3476"
                     /db_xref="HGNC:HGNC:5461"
                     /db_xref="MIM:300139"
ORIGIN      
        1 maaedelqlp rlpelfetgr qlldevevat epagsrivqe kvfkgldlle kaaemlsqld
       61 lfsrnedlee iastdlkyll vpafqgaltm kqvnpskrld hlqrarehfi nyltqchcyh
      121 vaefelpktm nnsaenhtan ssmaypslva masqrqakiq rvfgagypsl ptmtvsdwye
      181 qhrkygalpd qgiakaapee frkaaqqqee qeekeeedde qtlhrarewd dwkdthprgy
      241 gnrqnmg
//
LOCUS       NP_110430                607 aa            linear   PRI 27-APR-2025
DEFINITION  autophagy-related protein 16-1 isoform 1 [Homo sapiens].
ACCESSION   NP_110430
VERSION     NP_110430.5
DBSOURCE    REFSEQ: accession NM_030803.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Gubas,A., Attridge,E., Jefferies,H.B., Nishimura,T., Razi,M.,
            Kunzelmann,S., Gilad,Y., Mercer,T.J., Wilson,M.M., Kimchi,A. and
            Tooze,S.A.
  TITLE     WIPI2b recruitment to phagophores and ATG16L1 binding are regulated
            by ULK1 phosphorylation
  JOURNAL   EMBO Rep 25 (9), 3789-3811 (2024)
   PUBMED   39152217
  REMARK    GeneRIF: WIPI2b recruitment to phagophores and ATG16L1 binding are
            regulated by ULK1 phosphorylation.
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Liao,F.X., Yang,S., Liu,Z.H., Bo,K.D., Xu,P.F. and Chang,J.
  TITLE     Estrogen receptor is involved in the osteoarthritis mediated by
            Atg16L1-NLRP3 activation
  JOURNAL   Jt Dis Relat Surg 35 (3), 513-520 (2024)
   PUBMED   39189559
  REMARK    GeneRIF: Estrogen receptor is involved in the osteoarthritis
            mediated by Atg16L1-NLRP3 activation.
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Cui,Y., Yu,X., Bao,J., Ping,X., Shi,S., Huang,Y., Yin,Q., Yang,H.,
            Chen,R., Yao,K., Chen,X. and Shentu,X.
  TITLE     Lens autophagy protein ATG16L1: a potential target for cataract
            treatment
  JOURNAL   Theranostics 14 (10), 3984-3996 (2024)
   PUBMED   38994020
  REMARK    GeneRIF: Lens autophagy protein ATG16L1: a potential target for
            cataract treatment.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Wang,Q., Bu,Q., Xu,Z., Liang,Y., Zhou,J., Pan,Y., Zhou,H. and Lu,L.
  TITLE     Macrophage ATG16L1 expression suppresses metabolic
            dysfunction-associated steatohepatitis progression by promoting
            lipophagy
  JOURNAL   Clin Mol Hepatol 30 (3), 515-538 (2024)
   PUBMED   38726504
  REMARK    GeneRIF: Macrophage ATG16L1 expression suppresses metabolic
            dysfunction-associated steatohepatitis progression by promoting
            lipophagy.
REFERENCE   5  (residues 1 to 607)
  AUTHORS   Schreurs,R.R.C.E., Koulis,A., Booiman,T., Boeser-Nunnink,B.,
            Cloherty,A.P.M., Rader,A.G., Patel,K.S., Kootstra,N.A. and
            Ribeiro,C.M.S.
  TITLE     Autophagy-enhancing ATG16L1 polymorphism is associated with
            improved clinical outcome and T-cell immunity in chronic HIV-1
            infection
  JOURNAL   Nat Commun 15 (1), 2465 (2024)
   PUBMED   38548722
  REMARK    GeneRIF: Autophagy-enhancing ATG16L1 polymorphism is associated
            with improved clinical outcome and T-cell immunity in chronic HIV-1
            infection.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 607)
  AUTHORS   Rioux,J.D., Xavier,R.J., Taylor,K.D., Silverberg,M.S., Goyette,P.,
            Huett,A., Green,T., Kuballa,P., Barmada,M.M., Datta,L.W.,
            Shugart,Y.Y., Griffiths,A.M., Targan,S.R., Ippoliti,A.F.,
            Bernard,E.J., Mei,L., Nicolae,D.L., Regueiro,M., Schumm,L.P.,
            Steinhart,A.H., Rotter,J.I., Duerr,R.H., Cho,J.H., Daly,M.J. and
            Brant,S.R.
  TITLE     Genome-wide association study identifies new susceptibility loci
            for Crohn disease and implicates autophagy in disease pathogenesis
  JOURNAL   Nat Genet 39 (5), 596-604 (2007)
   PUBMED   17435756
REFERENCE   7  (residues 1 to 607)
  AUTHORS   Hampe,J., Franke,A., Rosenstiel,P., Till,A., Teuber,M., Huse,K.,
            Albrecht,M., Mayr,G., De La Vega,F.M., Briggs,J., Gunther,S.,
            Prescott,N.J., Onnie,C.M., Hasler,R., Sipos,B., Folsch,U.R.,
            Lengauer,T., Platzer,M., Mathew,C.G., Krawczak,M. and Schreiber,S.
  TITLE     A genome-wide association scan of nonsynonymous SNPs identifies a
            susceptibility variant for Crohn disease in ATG16L1
  JOURNAL   Nat Genet 39 (2), 207-211 (2007)
   PUBMED   17200669
  REMARK    GeneRIF: A genome-wide association scan of nonsynonymous SNPs
            identifies a susceptibility variant for Crohn disease in ATG16L1.
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-gene interaction. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 607)
  AUTHORS   Zheng,H., Ji,C., Li,J., Jiang,H., Ren,M., Lu,Q., Gu,S., Mao,Y. and
            Xie,Y.
  TITLE     Cloning and analysis of human Apg16L
  JOURNAL   DNA Seq 15 (4), 303-305 (2004)
   PUBMED   15620219
  REMARK    GeneRIF: Contains a coiled-coil domain and a motif with seven WD
            repeats, which are also shared by mouse Apg16L.
REFERENCE   9  (residues 1 to 607)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   10 (residues 1 to 607)
  AUTHORS   Mizushima,N., Kuma,A., Kobayashi,Y., Yamamoto,A., Matsubae,M.,
            Takao,T., Natsume,T., Ohsumi,Y. and Yoshimori,T.
  TITLE     Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic
            isolation membrane with the Apg12-Apg5 conjugate
  JOURNAL   J Cell Sci 116 (Pt 9), 1679-1688 (2003)
   PUBMED   12665549
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB084962.1, AC013726.7,
            AY398617.1, BC117337.1 and AA809053.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 29, 2007 this sequence version replaced NP_110430.4.
            
            Summary: The protein encoded by this gene is part of a large
            protein complex that is necessary for autophagy, the major process
            by which intracellular components are targeted to lysosomes for
            degradation. Defects in this gene are a cause of susceptibility to
            inflammatory bowel disease type 10 (IBD10). Several transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY398617.1, SRR1803613.75084.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392017.9/ ENSP00000375872.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..607
                     /product="autophagy-related protein 16-1 isoform 1"
                     /note="WD repeat domain 30; autophagy-related protein
                     16-1; APG16L beta; ATG16 autophagy related 16-like 1"
                     /calculated_mol_wt=68134
     Region          13..43
                     /region_name="Interaction with ATG5.
                     /evidence=ECO:0000269|PubMed:25484072"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          31..206
                     /region_name="ATG16"
                     /note="Autophagy protein 16 (ATG16); pfam08614"
                     /db_xref="CDD:462536"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:26083323; propagated from
                     UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          207..230
                     /region_name="WIPI2-binding.
                     /evidence=ECO:0000269|PubMed:24954904"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          230..242
                     /region_name="RB1CC1-binding.
                     /evidence=ECO:0000269|PubMed:23392225,
                     ECO:0000269|PubMed:24954904"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          257..604
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q676U5.2)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          296..299
                     /region_name="Caspase cleavage.
                     /evidence=ECO:0000269|PubMed:24553140"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          320..359
                     /region_name="WD 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          327..364
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          364..403
                     /region_name="WD 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          370..406
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          406..445
                     /region_name="WD 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          411..448
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          447..484
                     /region_name="WD 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          456..486
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          486..525
                     /region_name="WD 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          491..527
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          532..573
                     /region_name="WD 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          537..573
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          575..607
                     /region_name="WD 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q676U5.2)"
     Region          580..604
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..607
                     /gene="ATG16L1"
                     /gene_synonym="APG16L; ATG16A; ATG16L; IBD10; WDR30"
                     /coded_by="NM_030803.7:156..1979"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2503.2"
                     /db_xref="GeneID:55054"
                     /db_xref="HGNC:HGNC:21498"
                     /db_xref="MIM:610767"
ORIGIN      
        1 mssglraadf prwkrhiseq lrrrdrlqrq afeeiilqyn klleksdlhs vlaqklqaek
       61 hdvpnrheis pghdgtwndn qlqemaqlri khqeeltelh kkrgelaqlv idlnnqmqrk
      121 dremqmneak iaeclqtisd letecldlrt klcdleranq tlkdeydalq itftalegkl
      181 rktteenqel vtrwmaekaq eanrlnaene kdsrrrqarl qkelaeaake plpveqdddi
      241 evivdetsdh teetspvrai sraatkrlsq pagglldsit nifgrrsvss fpvpqdnvdt
      301 hpgsgkevrv patalcvfda hdgevnavqf spgsrllatg gmdrrvklwe vfgekcefkg
      361 slsgsnagit siefdsagsy llaasndfas riwtvddyrl rhtltghsgk vlsakflldn
      421 arivsgshdr tlklwdlrsk vciktvfags scndivcteq cvmsghfdkk irfwdirses
      481 ivremellgk italdlnper tellscsrdd llkvidlrtn aikqtfsapg fkcgsdwtrv
      541 vfspdgsyva agsaegslyi wsvltgkvek vlskqhsssi navawspsgs hvvsvdkgck
      601 avlwaqy
//
LOCUS       NP_932129                485 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM68 isoform 1 [Mus musculus].
ACCESSION   NP_932129 XP_145747
VERSION     NP_932129.2
DBSOURCE    REFSEQ: accession NM_198012.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Wynne,C., Lazzari,E., Smith,S., McCarthy,E.M., Ni Gabhann,J.,
            Kallal,L.E., Higgs,R., Greco,A., Cryan,S.A., Biron,C.A. and
            Jefferies,C.A.
  TITLE     TRIM68 negatively regulates IFN-beta production by degrading TRK
            fused gene, a novel driver of IFN-beta downstream of anti-viral
            detection systems
  JOURNAL   PLoS One 9 (7), e101503 (2014)
   PUBMED   24999993
  REMARK    Erratum:[PLoS One. 2015 Feb 09;10(2):e0117957. doi:
            10.1371/journal.pone.0117957. Greco, Angela [added]. PMID:
            25664835]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Hatakeyama,S.
  TITLE     TRIM proteins and cancer
  JOURNAL   Nat Rev Cancer 11 (11), 792-804 (2011)
   PUBMED   21979307
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC161431.4, AK089546.1, BY014556.1, AK164544.1 and CO424835.1.
            
            On Jan 16, 2008 this sequence version replaced NP_932129.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034249.1, SRR7345562.3583214.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 54.8 cM"
     Protein         1..485
                     /product="E3 ubiquitin-protein ligase TRIM68 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 137; E3 ubiquitin-protein
                     ligase TRIM68; tripartite motif-containing protein 68;
                     RING-type E3 ubiquitin transferase TRIM68"
                     /calculated_mol_wt=56020
     Region          13..61
                     /region_name="RING-HC_TRIM68_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 68 (TRIM68) and similar proteins;
                     cd16610"
                     /db_xref="CDD:438272"
     Region          96..138
                     /region_name="Bbox_SF"
                     /note="B-box-type zinc finger superfamily; cl00034"
                     /db_xref="CDD:469587"
     Region          <112..>188
                     /region_name="Cytochrom_C552"
                     /note="Cytochrome c552; pfam02335"
                     /db_xref="CDD:426726"
     Region          304..479
                     /region_name="SPRY_PRY_C-I_1"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     (TRIM) proteins, including TRIM5, TRIM6, TRIM7, TRIM10,
                     TRIM11, TRIM17, TRIM20, TRIM21, TRIM27, TRIM35, TRIM38,
                     TRIM41, TRIM50, TRIM58, TRIM60, TRIM62, TRIM69, TRIM72,
                     NF7 and bloodthirsty; cd13733"
                     /db_xref="CDD:293968"
     CDS             1..485
                     /gene="Trim68"
                     /gene_synonym="F730114J12Rik; Rnf137; SS-56"
                     /coded_by="NM_198012.4:226..1683"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS40052.1"
                     /db_xref="GeneID:101700"
                     /db_xref="MGI:MGI:2142077"
ORIGIN      
        1 mdpavlmeai veevncpicm tflrepvsis cghtfchscl sglwklpges qnlsytcplc
       61 rapvkprklr pnwqlasvvd kvrllgfcme mglktdvcdl hkeqltmfck eddmvtceac
      121 kqspeheahs vvpikdvawe ykwklqqale hlrkeqeeaw klevsekeqa aiwktqmerr
      181 kqsirwefek yrqllkekel pcqqaeeeaa aaqasleqek getasklelr reaiirqsqv
      241 lwsmivelee rsqrpvrwml qgiqealnrs eswtlqqlep islelktdcr vlglretlkt
      301 favdvrldpd taysrlvvsk drksvhygvt qqnlpdnper fyrynivlgs qcissgrhyw
      361 evevgdrsew glgvcvenvd rkevvylspr ygfwvirlrk gteyragtde ypllpltvpp
      421 hrvgifldye ahdisfynvt dgashiftfp rypfpgrllp yfspcysidt nnttpltict
      481 lggeg
//
LOCUS       NP_055458               1163 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 516 [Homo sapiens].
ACCESSION   NP_055458 XP_496278 XP_942502
VERSION     NP_055458.1
DBSOURCE    REFSEQ: accession NM_014643.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Xie,Z.Q., Chen,F., He,J., Zhong,L., Luo,G. and Fang,M.
  TITLE     MiR-371-5p regulates trophoblast cell proliferation, migration, and
            invasion by directly targeting ZNF516
  JOURNAL   Aging (Albany NY) 16 (10), 8585-8598 (2024)
   PUBMED   38761180
  REMARK    GeneRIF: MiR-371-5p regulates trophoblast cell proliferation,
            migration, and invasion by directly targeting ZNF516.
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   4  (residues 1 to 1163)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1163)
  AUTHORS   Beck,D.B., Subramanian,T., Vijayalingam,S., Ezekiel,U.R.,
            Donkervoort,S., Yang,M.L., Dubbs,H.A., Ortiz-Gonzalez,X.R.,
            Lakhani,S., Segal,D., Au,M., Graham,J.M. Jr., Verma,S.,
            Waggoner,D., Shinawi,M., Bonnemann,C.G., Chung,W.K. and
            Chinnadurai,G.
  TITLE     A pathogenic CtBP1 missense mutation causes altered cofactor
            binding and transcriptional activity
  JOURNAL   Neurogenetics 20 (3), 129-143 (2019)
   PUBMED   31041561
REFERENCE   6  (residues 1 to 1163)
  AUTHORS   O'Brien,R.P., Phelan,P.J., Conroy,J., O'Kelly,P., Green,A.,
            Keogan,M., O'Neill,D., Jennings,S., Traynor,C., Casey,J.,
            McCormack,M., Conroy,R., Chubb,A., Ennis,S., Shields,D.C.,
            Cavalleri,G.L. and Conlon,P.J.
  TITLE     A genome-wide association study of recipient genotype and
            medium-term kidney allograft function
  JOURNAL   Clin Transplant 27 (3), 379-387 (2013)
   PUBMED   23432519
REFERENCE   7  (residues 1 to 1163)
  AUTHORS   Yang,T.L., Guo,Y., Li,J., Zhang,L., Shen,H., Li,S.M., Li,S.K.,
            Tian,Q., Liu,Y.J., Papasian,C.J. and Deng,H.W.
  TITLE     Gene-gene interaction between RBMS3 and ZNF516 influences bone
            mineral density
  JOURNAL   J Bone Miner Res 28 (4), 828-837 (2013)
   PUBMED   23045156
  REMARK    GeneRIF: one interacting gene pair (RBMS3 versus ZNF516) which,
            even after Bonferroni correction for multiple testing, showed
            consistently significant effects on hip bone mineral density.
REFERENCE   8  (residues 1 to 1163)
  AUTHORS   Shaffer,J.R., Feingold,E., Wang,X., Lee,M., Tcuenco,K., Weeks,D.E.,
            Weyant,R.J., Crout,R., McNeil,D.W. and Marazita,M.L.
  TITLE     GWAS of dental caries patterns in the permanent dentition
  JOURNAL   J Dent Res 92 (1), 38-44 (2013)
   PUBMED   23064961
REFERENCE   9  (residues 1 to 1163)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   10 (residues 1 to 1163)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018413.10, D86975.1,
            AC009716.22 and BC108287.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jul 5, 2007 this sequence version replaced
            XP_496278.2, XP_942502.1.
            
            Summary: Zinc-finger proteins bind nucleic acids and play important
            roles in various cellular functions, including cell proliferation,
            differentiation, and apoptosis. This gene encodes a zinc-finger
            protein, and belongs to the krueppel C2H2-type zinc-finger protein
            family. It may be involved in transcriptional regulation. [provided
            by RefSeq, Sep 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D86975.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000443185.7/ ENSP00000394757.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q23"
     Protein         1..1163
                     /product="zinc finger protein 516"
                     /calculated_mol_wt=124159
     Region          1..431
                     /region_name="Mediates promoter DNA-binding and activation
                     of transcription. /evidence=ECO:0000250|UniProtKB:Q7TSH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          34..56
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          36..56
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          48..73
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          64..84
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          176..194
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          202..223
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(207,209,211,213..214,217..218,222,255,257,261..262,
                     265..266,269,283,285,287,289..290,293..294,297)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          248..270
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          250..270
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          278..298
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          460..512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          533..667
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          679..730
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          838..1007
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          <915..>1037
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          1098..1120
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          1100..1120
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1126..1163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     CDS             1..1163
                     /gene="ZNF516"
                     /gene_synonym="HsT287"
                     /coded_by="NM_014643.4:371..3862"
                     /db_xref="CCDS:CCDS74234.1"
                     /db_xref="GeneID:9658"
                     /db_xref="HGNC:HGNC:28990"
                     /db_xref="MIM:615114"
ORIGIN      
        1 mdrnreaeme lrrgpsptra grghevdgdk atchtccicg ksfpfqssls qhmrkhtgek
       61 pykcpycdhr asqkgnlkih irshrtgtli qghepeagea plgemraseg ldacasptks
      121 asacnrllng asqadgarvl ngasqadsgr vllrsskkga egsacapgea kaavqcsfck
      181 sqferkkdle lhvhqahkpf kcrlcsyatl reesllshie rdhitaqgpg sgeacvengk
      241 pelspgefpc evcgqafsqt wflkahmkkh rgsfdhgchi cgrrfkepwf lknhmkahgp
      301 ktgsknrpks eldpiatinn vvqeevivag lslyevcakc gnlftnldsl nahnaihrrv
      361 easrtrapae egaegpsdtk qfflqclnlr psaagdscpg tqagrrvael dpvnsyqawq
      421 latrgkvaep aeylkygawd ealagdvafd kdrreyvlvs qekrkreqda paaqgpprkr
      481 asgpgdpapa ghldprsaar pnrraaattg qgkssecfec gkifrtyhqm vlhsrvhrra
      541 rrerdsdgdr aararcgsls egdsasqpss pgsacaaads pgsgladeaa edsgeegape
      601 papggqprrc cfseevtste lssgdqshkm gdnaserdtg eskagiaasv silenssret
      661 srrqeqhrfs mdlkmpafhp kqevpvpgdg vefpsstgae gqtghpaekl sdlhnkehsg
      721 ggkralapdl mpldlsarst rddpsnketa sslqaalvvh pcpycshkty ypevlwmhkr
      781 iwhrvscnsv appwiqpngy ksirsnlvfl srsgrtgppp alggkecqpl llarftrtqv
      841 pggmpgsksg ssplgvvtka asmpknkesh sggpcalwap gpdgyrqtkp chgqephgaa
      901 tqgplakprq easskpvpap ggggfsrsat ptptviarag aqpsanskpv ekfgvppaga
      961 gfaptnkhsa pdslkakfsa qpqgpppakg eggapplppr eppskaaqel rtlatcaags
     1021 rgdaalqaqp gvagappvlh sikqepvaeg hekrldilni fktyipkdfa tlyqgwgvsg
     1081 pglehrgtlr tqarpgefvc iecgksfhqp ghlrahmrah svvfesdgpr gsevhttsad
     1141 apkqgrdhsn tgtvqtvplr kgt
//
LOCUS       NP_000692               1023 aa            linear   PRI 27-APR-2025
DEFINITION  sodium/potassium-transporting ATPase subunit alpha-1 isoform a
            [Homo sapiens].
ACCESSION   NP_000692
VERSION     NP_000692.2
DBSOURCE    REFSEQ: accession NM_000701.8
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Cerella,C., Gajulapalli,S.R., Lorant,A., Gerard,D., Muller,F.,
            Lee,Y., Kim,K.R., Han,B.W., Christov,C., Recher,C., Sarry,J.E.,
            Dicato,M. and Diederich,M.
  TITLE     ATP1A1/BCL2L1 predicts the response of myelomonocytic and monocytic
            acute myeloid leukemia to cardiac glycosides
  JOURNAL   Leukemia 38 (1), 67-81 (2024)
   PUBMED   37904054
  REMARK    GeneRIF: ATP1A1/BCL2L1 predicts the response of myelomonocytic and
            monocytic acute myeloid leukemia to cardiac glycosides.
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Spontarelli,K., Young,V.C., Sweazey,R., Padro,A., Lee,J., Bueso,T.,
            Hernandez,R.M., Kim,J., Katz,A., Rossignol,F., Turner,C.,
            Wilczewski,C.M., Maxwell,G.L., Holmgren,M., Bailoo,J.D., Yano,S.T.
            and Artigas,P.
  TITLE     ATP1A1-linked diseases require a malfunctioning protein product
            from one allele
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (1), 119572 (2024)
   PUBMED   37659504
  REMARK    GeneRIF: ATP1A1-linked diseases require a malfunctioning protein
            product from one allele.
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Silkuniene,G., Mangalanathan,U.M., Pakhomov,A.G. and Pakhomova,O.N.
  TITLE     Silencing of ATP1A1 attenuates cell membrane disruption by
            nanosecond electric pulses
  JOURNAL   Biochem Biophys Res Commun 677, 93-97 (2023)
   PUBMED   37566922
  REMARK    GeneRIF: Silencing of ATP1A1 attenuates cell membrane disruption by
            nanosecond electric pulses.
REFERENCE   4  (residues 1 to 1023)
  AUTHORS   Sumiyoshi,S., Shiozaki,A., Kosuga,T., Simizu,H., Kudo,M.,
            Kiuchi,J., Arita,T., Konishi,H., Komatsu,S., Kuriu,Y., Kubota,T.,
            Fujiwara,H., Morinaga,Y., Konishi,E. and Otsuji,E.
  TITLE     Functional Analysis and Clinical Importance of ATP1A1 in Colon
            Cancer
  JOURNAL   Ann Surg Oncol 30 (11), 6898-6910 (2023)
   PUBMED   37407874
  REMARK    GeneRIF: Functional Analysis and Clinical Importance of ATP1A1 in
            Colon Cancer.
REFERENCE   5  (residues 1 to 1023)
  AUTHORS   Rajan,P.K., Udoh,U.S., Nakafuku,Y., Pierre,S.V. and Sanabria,J.
  TITLE     Normalization of the ATP1A1 Signalosome Rescinds Epigenetic
            Modifications and Induces Cell Autophagy in Hepatocellular
            Carcinoma
  JOURNAL   Cells 12 (19), 2367 (2023)
   PUBMED   37830582
  REMARK    GeneRIF: Normalization of the ATP1A1 Signalosome Rescinds
            Epigenetic Modifications and Induces Cell Autophagy in
            Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1023)
  AUTHORS   Shull,M.M., Pugh,D.G. and Lingrel,J.B.
  TITLE     The human Na, K-ATPase alpha 1 gene: characterization of the
            5'-flanking region and identification of a restriction fragment
            length polymorphism
  JOURNAL   Genomics 6 (3), 451-460 (1990)
   PUBMED   1970326
REFERENCE   7  (residues 1 to 1023)
  AUTHORS   Lingrel,J.B., Orlowski,J., Shull,M.M. and Price,E.M.
  TITLE     Molecular genetics of Na,K-ATPase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 38, 37-89 (1990)
   PUBMED   2158121
  REMARK    Review article
REFERENCE   8  (residues 1 to 1023)
  AUTHORS   Yang-Feng,T.L., Schneider,J.W., Lindgren,V., Shull,M.M., Benz,E.J.
            Jr., Lingrel,J.B. and Francke,U.
  TITLE     Chromosomal localization of human Na+, K+-ATPase alpha- and
            beta-subunit genes
  JOURNAL   Genomics 2 (2), 128-138 (1988)
   PUBMED   2842249
REFERENCE   9  (residues 1 to 1023)
  AUTHORS   Sverdlov,E.D., Broude,N.E., Sverdlov,V.E., Monastyrskaya,G.S.,
            Grishin,A.V., Petrukhin,K.E., Akopyanz,N.S., Modyanov,N.N. and
            Ovchinnikov,Yu.A.
  TITLE     Family of Na+,K+-ATPase genes. Intra-individual tissue-specific
            restriction fragment length polymorphism
  JOURNAL   FEBS Lett 221 (1), 129-133 (1987)
   PUBMED   2887455
  REMARK    Erratum:[FEBS Lett 1988 Jan 18;227(1):85]
REFERENCE   10 (residues 1 to 1023)
  AUTHORS   Kawakami,K., Ohta,T., Nojima,H. and Nagano,K.
  TITLE     Primary structure of the alpha-subunit of human Na,K-ATPase deduced
            from cDNA sequence
  JOURNAL   J Biochem 100 (2), 389-397 (1986)
   PUBMED   2430951
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC335233.1 and BC050359.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_000692.1.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of Na+/K+
            -ATPases. Na+/K+ -ATPase is an integral membrane protein
            responsible for establishing and maintaining the electrochemical
            gradients of Na and K ions across the plasma membrane. These
            gradients are essential for osmoregulation, for sodium-coupled
            transport of a variety of organic and inorganic molecules, and for
            electrical excitability of nerve and muscle. This enzyme is
            composed of two subunits, a large catalytic subunit (alpha) and a
            smaller glycoprotein subunit (beta). The catalytic subunit of
            Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an
            alpha 1 subunit. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, May
            2009].
            
            Transcript Variant: This variant (1) represents use of an alternate
            promoter and 5' exon, compared to variant 3. The resulting isoform
            (a) is the same length but has a distinct N-terminus, compared to
            isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050359.1, SRR11853565.1514.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295598.10/ ENSP00000295598.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.1"
     Protein         1..1023
                     /product="sodium/potassium-transporting ATPase subunit
                     alpha-1 isoform a"
                     /EC_number="7.2.2.13"
                     /note="Na, K-ATPase, alpha-A catalytic polypeptide; Na+/K+
                     ATPase 1; sodium-potassium-ATPase, alpha 1 polypeptide;
                     sodium/potassium-transporting ATPase subunit alpha-1;
                     Na,K-ATPase alpha-1 subunit; Na,K-ATPase catalytic subunit
                     alpha-A protein; sodium pump subunit alpha-1; Na(+)/K(+)
                     ATPase alpha-1 subunit; sodium-potassium ATPase catalytic
                     subunit alpha-1; ATPase, Na+/K+ transporting, alpha 1
                     polypeptide"
                     /calculated_mol_wt=112766
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDN2; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P06685; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDN2; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Region          30..1023
                     /region_name="ATPase-IIC_X-K"
                     /note="sodium or proton efflux -- potassium uptake
                     antiporter, P-type ATPase, alpha subunit; TIGR01106"
                     /db_xref="CDD:273445"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06685; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06685; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Region          82..84
                     /region_name="Phosphoinositide-3 kinase binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            132..152
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Region          216..235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDN2; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDN2; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            289..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            321..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06685; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06685; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Region          596..717
                     /region_name="Mediates interaction with SCN7A.
                     /evidence=ECO:0000250|UniProtKB:Q8VDN2"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDN2; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDN2; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            773..792
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            803..823
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            844..866
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            919..938
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            943
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P06685; propagated from
                     UniProtKB/Swiss-Prot (P05023.1)"
     Site            952..970
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     Site            986..1006
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05023.1)"
     CDS             1..1023
                     /gene="ATP1A1"
                     /gene_synonym="CMT2DD; HOMGSMR2"
                     /coded_by="NM_000701.8:269..3340"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS887.1"
                     /db_xref="GeneID:476"
                     /db_xref="HGNC:HGNC:799"
                     /db_xref="MIM:182310"
ORIGIN      
        1 mgkgvgrdky epaavseqgd kkgkkgkkdr dmdelkkevs mddhklslde lhrkygtdls
       61 rgltsaraae ilardgpnal tpppttpewi kfcrqlfggf smllwigail cflaysiqaa
      121 teeepqndnl ylgvvlsavv iitgcfsyyq eaksskimes fknmvpqqal virngekmsi
      181 naeevvvgdl vevkggdrip adlriisang ckvdnssltg esepqtrspd ftnenpletr
      241 niaffstncv egtargivvy tgdrtvmgri atlasglegg qtpiaaeieh fihiitgvav
      301 flgvsffils lileytwlea vifligiiva nvpegllatv tvcltltakr marknclvkn
      361 leavetlgst sticsdktgt ltqnrmtvah mwfdnqihea dttenqsgvs fdktsatwla
      421 lsriaglcnr avfqanqenl pilkravagd asesallkci elccgsvkem reryakivei
      481 pfnstnkyql sihknpntse pqhllvmkga perildrcss illhgkeqpl deelkdafqn
      541 aylelgglge rvlgfchlfl pdeqfpegfq fdtddvnfpi dnlcfvglis midppraavp
      601 davgkcrsag ikvimvtgdh pitakaiakg vgiisegnet vediaarlni pvsqvnprda
      661 kacvvhgsdl kdmtseqldd ilkyhteivf artspqqkli ivegcqrqga ivavtgdgvn
      721 dspalkkadi gvamgiagsd vskqaadmil lddnfasivt gveegrlifd nlkksiaytl
      781 tsnipeitpf lifiianipl plgtvtilci dlgtdmvpai slayeqaesd imkrqprnpk
      841 tdklvnerli smaygqigmi qalggfftyf vilaengflp ihllglrvdw ddrwindved
      901 sygqqwtyeq rkiveftcht affvsivvvq wadlvicktr rnsvfqqgmk nkilifglfe
      961 etalaaflsy cpgmgvalrm yplkptwwfc afpysllifv ydevrkliir rrpggwveke
     1021 tyy
//
LOCUS       NP_997245                962 aa            linear   PRI 27-APR-2025
DEFINITION  CRACD-like protein [Homo sapiens].
ACCESSION   NP_997245
VERSION     NP_997245.2
DBSOURCE    REFSEQ: accession NM_207362.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Alblooshi,H., Al Safar,H., El Kashef,A., Al Ghaferi,H., Shawky,M.,
            Hulse,G.K. and Tay,G.K.
  TITLE     Stratified analyses of genome wide association study data reveal
            haplotypes for a candidate gene on chromosome 2 (KIAA1211L) is
            associated with opioid use in patients of Arabian descent
  JOURNAL   BMC Psychiatry 20 (1), 41 (2020)
   PUBMED   32005204
  REMARK    GeneRIF: Stratified analyses of genome wide association study data
            reveal haplotypes for a candidate gene on chromosome 2 (KIAA1211L)
            is associated with opioid use in patients of Arabian descent.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Scott,L.J., Muglia,P., Kong,X.Q., Guan,W., Flickinger,M.,
            Upmanyu,R., Tozzi,F., Li,J.Z., Burmeister,M., Absher,D.,
            Thompson,R.C., Francks,C., Meng,F., Antoniades,A., Southwick,A.M.,
            Schatzberg,A.F., Bunney,W.E., Barchas,J.D., Jones,E.G., Day,R.,
            Matthews,K., McGuffin,P., Strauss,J.S., Kennedy,J.L., Middleton,L.,
            Roses,A.D., Watson,S.J., Vincent,J.B., Myers,R.M., Farmer,A.E.,
            Akil,H., Burns,D.K. and Boehnke,M.
  TITLE     Genome-wide association and meta-analysis of bipolar disorder in
            individuals of European ancestry
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7501-7506 (2009)
   PUBMED   19416921
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084377.5, BM922097.1, BC068277.1 and CF593294.1.
            
            On Oct 18, 2006 this sequence version replaced NP_997245.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068277.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397899.7/ ENSP00000380996.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..962
                     /product="CRACD-like protein"
                     /note="uncharacterized protein C2orf55; KIAA1211 like"
                     /calculated_mol_wt=102027
     Region          38..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NV74.3)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NV74.3)"
     Region          131..174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NV74.3)"
     Region          145..240
                     /region_name="DUF4592"
                     /note="Domain of unknown function (DUF4592); pfam15262"
                     /db_xref="CDD:464602"
     Region          212..871
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NV74.3)"
     Region          <305..>620
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NV74.3)"
     Region          <524..>826
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     CDS             1..962
                     /gene="CRACDL"
                     /gene_synonym="C2orf55; KIAA1211L"
                     /coded_by="NM_207362.3:299..3187"
                     /db_xref="CCDS:CCDS42720.1"
                     /db_xref="GeneID:343990"
                     /db_xref="HGNC:HGNC:33454"
ORIGIN      
        1 mistrvmdik lreaaeglge dstgkkkskf ktfkkffgkk krkespsstg sstwkqsqtr
       61 neviaiesgp vgydsedele esrgtlgsra lshdsifipe sgqdatrpvr vfsqenvcdr
      121 ikalqlkiqc nvkmgppppp gglpakrged agmsseddgl prsppemsll hdvgpgttik
      181 vsvvspdhvs dstvsarisd nslapvadfs ypaessscld nsaakhklqv kprnqrsskm
      241 rrlssraqse slsdltctpe eeeneekpll evspeerpss gqqdvapdrg pepgppaplp
      301 ppggararra rlqhssalta sveeggvpge dpssrpatpe laepesaptl rveppsppeg
      361 ppnpgpdggk qdgeappagp capatdkaee vvcapedvas pfptaipegd ttppetdpaa
      421 tseapsardg persvpkeae ptppvlpdee kgppgpapep ereaeteper gagteperig
      481 tepstapaps ppapksclkh rpaaasegpa aspplaaaes ppvepgpgsl daeaaaperp
      541 kaeraeappa gaeraaperk aerggaelrg akkfsvsscr arprpgvsrp lerasgrlpl
      601 arsgpvwrse aalddlqglp epqhakpgpr klaergpqds gdraaspagp rkspqeaaaa
      661 pgtrepcpaa qepapsedrn pfpvklrsts lslkyrdgas qevkgvkrys aevrlerslt
      721 vlpkeekcpl gtapalrgtr apsdqgkgka rppeplsskp plprkpllqs ftlphqpapp
      781 dagpgerepr keprtaekrp lrrgaekslp paatgpgadg qpappwitvt rqkrrgtldq
      841 ppnqedkpga rtlksepgkq akvpergqep vkqadfvrsk sflitpvkpa vdrkqgakln
      901 fkeglqrgis lshqnlaqsa vmmekelhql krasyastdq pswmelarkk sqawsdmpqi
      961 ik
//
LOCUS       NP_001268222             895 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 281 isoform 1 [Homo sapiens].
ACCESSION   NP_001268222
VERSION     NP_001268222.1
DBSOURCE    REFSEQ: accession NM_001281293.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Zeng,H., Hou,Y., Zhou,X., Lang,L., Luo,H., Sun,Y., Wan,X., Yuan,T.,
            Wang,R., Liu,Y., Tang,R., Cheng,S., Xu,M. and Liu,M.
  TITLE     Cancer-associated fibroblasts facilitate premetastatic niche
            formation through lncRNA SNHG5-mediated angiogenesis and vascular
            permeability in breast cancer
  JOURNAL   Theranostics 12 (17), 7351-7370 (2022)
   PUBMED   36438499
  REMARK    GeneRIF: Cancer-associated fibroblasts facilitate premetastatic
            niche formation through lncRNA SNHG5-mediated angiogenesis and
            vascular permeability in breast cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Laudadio,I., Bastianelli,A., Fulci,V., Carissimi,C., Colantoni,E.,
            Palone,F., Vitali,R., Lorefice,E., Cucchiara,S., Negroni,A. and
            Stronati,L.
  TITLE     ZNF281 Promotes Colon Fibroblast Activation in TGFbeta1-Induced Gut
            Fibrosis
  JOURNAL   Int J Mol Sci 23 (18), 10261 (2022)
   PUBMED   36142169
  REMARK    GeneRIF: ZNF281 Promotes Colon Fibroblast Activation in
            TGFbeta1-Induced Gut Fibrosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 895)
  AUTHORS   Hou,Y.M., Wang,X.P., Shen,C.C., Chen,L.T. and Zheng,X.X.
  TITLE     Cervical carcinoma progression is aggravated by lncRNA ZNF281 by
            binding KLF15
  JOURNAL   Eur Rev Med Pharmacol Sci 25 (18), 5610-5618 (2021)
   PUBMED   34604953
  REMARK    GeneRIF: Cervical carcinoma progression is aggravated by lncRNA
            ZNF281 by binding KLF15.
REFERENCE   4  (residues 1 to 895)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 895)
  AUTHORS   Zhang,Z., Yang,L., Yao,X., Yang,M. and Li,G.
  TITLE     LncRNA-ZNF281 Interacts with miR-539 to Promote Hepatocellular
            Carcinoma Cell Invasion and Migration
  JOURNAL   Cancer Biother Radiopharm 35 (2), 137-142 (2020)
   PUBMED   32073896
  REMARK    GeneRIF: LncRNA-ZNF281 Interacts with miR-539 to Promote
            Hepatocellular Carcinoma Cell Invasion and Migration.
REFERENCE   6  (residues 1 to 895)
  AUTHORS   Scharer,C.D., McCabe,C.D., Ali-Seyed,M., Berger,M.F., Bulyk,M.L.
            and Moreno,C.S.
  TITLE     Genome-wide promoter analysis of the SOX4 transcriptional network
            in prostate cancer cells
  JOURNAL   Cancer Res 69 (2), 709-717 (2009)
   PUBMED   19147588
REFERENCE   7  (residues 1 to 895)
  AUTHORS   Koch,H.B., Zhang,R., Verdoodt,B., Bailey,A., Zhang,C.D., Yates,J.R.
            3rd, Menssen,A. and Hermeking,H.
  TITLE     Large-scale identification of c-MYC-associated proteins using a
            combined TAP/MudPIT approach
  JOURNAL   Cell Cycle 6 (2), 205-217 (2007)
   PUBMED   17314511
REFERENCE   8  (residues 1 to 895)
  AUTHORS   Zhang,X., Diab,I.H. and Zehner,Z.E.
  TITLE     ZBP-89 represses vimentin gene transcription by interacting with
            the transcriptional activator, Sp1
  JOURNAL   Nucleic Acids Res 31 (11), 2900-2914 (2003)
   PUBMED   12771217
REFERENCE   9  (residues 1 to 895)
  AUTHORS   Law,D.J., Du,M., Law,G.L. and Merchant,J.L.
  TITLE     ZBP-99 defines a conserved family of transcription factors and
            regulates ornithine decarboxylase gene expression
  JOURNAL   Biochem Biophys Res Commun 262 (1), 113-120 (1999)
   PUBMED   10448078
REFERENCE   10 (residues 1 to 895)
  AUTHORS   Lisowsky,T., Polosa,P.L., Sagliano,A., Roberti,M., Gadaleta,M.N.
            and Cantatore,P.
  TITLE     Identification of human GC-box-binding zinc finger protein, a new
            Kruppel-like zinc finger protein, by the yeast one-hybrid screening
            with a GC-rich target sequence
  JOURNAL   FEBS Lett 453 (3), 369-374 (1999)
   PUBMED   10405178
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP216938.1, AJ132592.1 and AC104461.2.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' UTR compared to variant 1. Variants 1 and 2 encode the
            same protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2068957.1,
                                           SRR18074967.2892198.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367353.2/ ENSP00000356322.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..895
                     /product="zinc finger protein 281 isoform 1"
                     /note="ZNP-99 transcription factor; transcription factor
                     ZBP-99; zinc finger DNA-binding protein 99; GC-box-binding
                     zinc finger protein 1"
                     /calculated_mol_wt=96784
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Region          63..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Region          130..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Region          183..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Region          261..283
                     /region_name="zf-C2H2_4"
                     /note="C2H2-type zinc finger; pfam13894"
                     /db_xref="CDD:464025"
     Region          263..283
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(268,270,272,274..275,278..279,282,296,298,302..303,
                     306..307,310,324,326,328,330..331,334..335,338)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          275..300
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          291..311
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          319..339
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          331..356
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          347..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          377..427
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Region          638..660
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Site            651
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Region          778..817
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Site            785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Site            807
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     Site            888
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2X9.1)"
     CDS             1..895
                     /gene="ZNF281"
                     /gene_synonym="GZP1; ZBP-99; ZBP99; ZNP-99"
                     /coded_by="NM_001281293.2:110..2797"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1402.1"
                     /db_xref="GeneID:23528"
                     /db_xref="HGNC:HGNC:13075"
                     /db_xref="MIM:618703"
ORIGIN      
        1 mkigsgflsg gggtgssggs gsggggsggg ggggssgrra emeptfpqgm vmfnhrlppv
       61 tsftrpagsa apppqcvlss stsaapaaep ppppapdmtf kkepaasaaa fpsqrtswgf
      121 lqslvsikqe kpadpeeqqs hhhhhhhhyg glfagaeers pglgggeggs hgviqdlsil
      181 hqhvqqqpaq hhrdvllsss srtddhhgte epkqdtnvkk akrpkpesqg ikakrkpsas
      241 skpslvgdge gailspsqkp hicdhcsaaf rssyhlrrhv lihtgerpfq csqcsmgfiq
      301 kyllqrheki hsrekpfgcd qcsmkfiqky hmerhkrths gekpykcdtc qqyfsrtdrl
      361 lkhrrtcgev ivkgatsaep gssnhtnmgn lavlsqgnts ssrrktksks iaienkeqkt
      421 gktnesqisn ninmqsysve mptvsssggi igtgidelqk rvpklifkkg srkntdknyl
      481 nfvsplpdiv gqkslsgkps gslgivsnns vetigllqst sgkqgqissn yddamqfskk
      541 rrylptassn safsinvghm vsqqsviqsa gvsvldneap lslidssaln aeikschdks
      601 gipdevlqsi ldqysnkses qkedpfniae prvdlhtsge hselvqeenl spgtqtpsnd
      661 kasmlqeysk ylqqafekst nasftlghgf qfvslssplh nhtlfpekqi yttsplecgf
      721 gqsvtsvlps slpkppfgml fgsqpglyls aldathqqlt psqelddlid sqknletssa
      781 fqsssqklts qkeqknless tgfqipsqel asqidpqkdi eprttyqien faqafgsqfk
      841 sgsrvpmtfi tnsngevdhr vrtsvsdfsg ytnmmsdvse pcstrvktpt sqsyr
//
LOCUS       NP_000776                508 aa            linear   PRI 27-APR-2025
DEFINITION  25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial [Homo
            sapiens].
ACCESSION   NP_000776
VERSION     NP_000776.1
DBSOURCE    REFSEQ: accession NM_000785.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Murugesan,H., Sampath,P., A,V.K., R,S., Veerasamy,A.,
            Ranganathan,U.D., Paramasivam,S. and Bethunaickan,R.
  TITLE     Association of CYP27B1 gene polymorphisms with pulmonary
            tuberculosis and vitamin D levels
  JOURNAL   Gene 927, 148679 (2024)
   PUBMED   38876405
  REMARK    GeneRIF: Association of CYP27B1 gene polymorphisms with pulmonary
            tuberculosis and vitamin D levels.
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Dennis,C., Dillon,J., Cohen,D.J., Halquist,M.S., Pearcy,A.C.,
            Schwartz,Z. and Boyan,B.D.
  TITLE     Local production of active vitamin D3 metabolites in breast cancer
            cells by CYP24A1 and CYP27B1
  JOURNAL   J Steroid Biochem Mol Biol 232, 106331 (2023)
   PUBMED   37244301
  REMARK    GeneRIF: Local production of active vitamin D3 metabolites in
            breast cancer cells by CYP24A1 and CYP27B1.
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Meaux,M.N., Harambat,J., Rothenbuhler,A., Leger,J., Kamenicky,P.,
            Soskin,S., Boyer,O., Boros,E., D'Anella,P., Mignot,B., Gebhart,M.,
            Vic,P., Richard,N., Thivichon-Prince,B., Francou,B., Linglart,A.,
            Bacchetta,J. and Molin,A.
  TITLE     Genotype-phenotype Description of Vitamin D-dependent Rickets 1A:
            CYP27B1 p.(Ala129Thr) Variant Induces a Milder Disease
  JOURNAL   J Clin Endocrinol Metab 108 (4), 812-826 (2023)
   PUBMED   36321535
  REMARK    GeneRIF: Genotype-phenotype Description of Vitamin D-dependent
            Rickets 1A: CYP27B1 p.(Ala129Thr) Variant Induces a Milder Disease.
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Aftab,S., Khan,S.A., Malik,M.I., Imran,A., Anjum,M.N., Saeed,A.,
            Qureshi,A.A. and Cheema,H.A.
  TITLE     Clinical spectrum and diagnostic challenges of vitamin D dependent
            rickets type 1A (VDDR1A) caused by CYP27B1 mutation in resource
            limited countries
  JOURNAL   J Pediatr Endocrinol Metab 36 (2), 152-157 (2022)
   PUBMED   36524979
  REMARK    GeneRIF: Clinical spectrum and diagnostic challenges of vitamin D
            dependent rickets type 1A (VDDR1A) caused by CYP27B1 mutation in
            resource limited countries.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Luo,M., Liu,J., Yuan,Y., Chen,Y. and Yuan,G.
  TITLE     The role of vitamin D-synthesizing enzyme CYP27B1 in systemic lupus
            erythematosus
  JOURNAL   Turk J Med Sci 52 (4), 984-989 (2022)
   PUBMED   36326421
  REMARK    GeneRIF: The role of vitamin D-synthesizing enzyme CYP27B1 in
            systemic lupus erythematosus.
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Takeyama,K., Kitanaka,S., Sato,T., Kobori,M., Yanagisawa,J. and
            Kato,S.
  TITLE     25-Hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis
  JOURNAL   Science 277 (5333), 1827-1830 (1997)
   PUBMED   9295274
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Besancon,F., Just,J., Bourgeade,M.F., Van Weyenbergh,J.,
            Solomon,D., Guillozo,H., Wietzerbin,J. and Cayre,Y.E.
  TITLE     HIV-1 p17 and IFN-gamma both induce fructose 1,6-bisphosphatase
  JOURNAL   J Interferon Cytokine Res 17 (8), 461-467 (1997)
   PUBMED   9282826
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Szpirer,J., Szpirer,C., Riviere,M., Levan,G., Marynen,P.,
            Cassiman,J.J., Wiese,R. and DeLuca,H.F.
  TITLE     The Sp1 transcription factor gene (SP1) and the
            1,25-dihydroxyvitamin D3 receptor gene (VDR) are colocalized on
            human chromosome arm 12q and rat chromosome 7
  JOURNAL   Genomics 11 (1), 168-173 (1991)
   PUBMED   1662663
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Labuda,M., Morgan,K. and Glorieux,F.H.
  TITLE     Mapping autosomal recessive vitamin D dependency type I to
            chromosome 12q14 by linkage analysis
  JOURNAL   Am J Hum Genet 47 (1), 28-36 (1990)
   PUBMED   1971995
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Pryke,A.M., Duggan,C., White,C.P., Posen,S. and Mason,R.S.
  TITLE     Tumor necrosis factor-alpha induces vitamin D-1-hydroxylase
            activity in normal human alveolar macrophages
  JOURNAL   J Cell Physiol 142 (3), 652-656 (1990)
   PUBMED   1690216
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB005038.1 and AW449645.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            The protein encoded by this gene localizes to the inner
            mitochondrial membrane where it hydroxylates 25-hydroxyvitamin D3
            at the 1alpha position. This reaction synthesizes
            1alpha,25-dihydroxyvitamin D3, the active form of vitamin D3, which
            binds to the vitamin D receptor and regulates calcium metabolism.
            Thus this enzyme regulates the level of biologically active vitamin
            D and plays an important role in calcium homeostasis. Mutations in
            this gene can result in vitamin D-dependent rickets type I.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB005038.1, AF020192.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000228606.9/
                                                  ENSP00000228606.4
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.1"
     Protein         1..508
                     /product="25-hydroxyvitamin D-1 alpha hydroxylase,
                     mitochondrial"
                     /EC_number="1.14.15.18"
                     /note="25-OHD-1 alpha-hydroxylase; VD3 1A hydroxylase;
                     1alpha(OH)ase; 25 hydroxyvitamin D3-1-alpha hydroxylase;
                     calcidiol 1-monooxygenase; cytochrome p450 27B1;
                     cytochrome P450C1 alpha; cytochrome P450VD1-alpha;
                     cytochrome P450 subfamily XXVIIB polypeptide 1; cytochrome
                     P450, family 27, subfamily B, polypeptide 1"
                     /calculated_mol_wt=56373
     Region          68..503
                     /region_name="CYP27B1"
                     /note="cytochrome P450 family 27, subfamily B, polypeptide
                     1, also called calcidiol 1-monooxygenase; cd20648"
                     /db_xref="CDD:410741"
     Site            order(107,113,127,187..188,191,226,228..229,257,313,
                     316..317,320..321,383..388,493..494)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:410741"
     Site            order(107,126..127,134,138,314,317..318,321..322,325,
                     383..384,387,389,447..450,453..457,461)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410741"
     Site            455
                     /site_type="binding"
                     /note="heme binding site"
     CDS             1..508
                     /gene="CYP27B1"
                     /gene_synonym="CP2B; CYP1; CYP1alpha; CYP27B; P450c1;
                     PDDR; VDD1; VDDR; VDDRI; VDR"
                     /coded_by="NM_000785.4:38..1564"
                     /db_xref="CCDS:CCDS8954.1"
                     /db_xref="GeneID:1594"
                     /db_xref="HGNC:HGNC:2606"
                     /db_xref="MIM:609506"
ORIGIN      
        1 mtqtlkyasr vfhrvrwape lgaslgyrey hsarrsladi pgpstpsfla elfckgglsr
       61 lhelqvqgaa hfgpvwlasf gtvrtvyvaa palveellrq egprpercsf spwtehrrcr
      121 qracglltae geewqrlrsl laplllrpqa aaryagtlnn vvcdlvrrlr rqrgrgtgpp
      181 alvrdvagef ykfglegiaa vllgsrlgcl eaqvppdtet firavgsvfv stlltmamph
      241 wlrhlvpgpw grlcrdwdqm fafaqrhver reaeaamrng gqpekdlesg ahlthflfre
      301 elpaqsilgn vtelllagvd tvsntlswal yelsrhpevq talhseitaa lspgssayps
      361 atvlsqlpll kavvkevlrl ypvvpgnsrv pdkdihvgdy iipkntlvtl chyatsrdpa
      421 qfpepnsfrp arwlgegptp hpfaslpfgf gkrscmgrrl aelelqmala qilthfevqp
      481 epgaapvrpk trtvlvpers inlqfldr
//
LOCUS       NP_071424                331 aa            linear   PRI 27-APR-2025
DEFINITION  gamma-parvin [Homo sapiens].
ACCESSION   NP_071424
VERSION     NP_071424.1
DBSOURCE    REFSEQ: accession NM_022141.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Yoshimi,R., Yamaji,S., Suzuki,A., Mishima,W., Okamura,M., Obana,T.,
            Matsuda,C., Miwa,Y., Ohno,S. and Ishigatsubo,Y.
  TITLE     The gamma-parvin-integrin-linked kinase complex is critically
            involved in leukocyte-substrate interaction
  JOURNAL   J Immunol 176 (6), 3611-3624 (2006)
   PUBMED   16517730
  REMARK    GeneRIF: integrin-linked kinase-gamma-parvin complex is critically
            involved in the initial integrin signaling for leukocyte migration
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Alonso,M.E., Bello,M.J., de Campos,J.M., Isla,A., Vaquero,J.,
            Gutierrez,M., Sarasa,J.L. and Rey,J.A.
  TITLE     No evidence of INI1hSNF5 (SMARCB1) and PARVG point mutations in
            oligodendroglial neoplasms
  JOURNAL   Cancer Genet Cytogenet 160 (2), 169-173 (2005)
   PUBMED   15993274
  REMARK    GeneRIF: INI1hSNF5 and PARVG do not seem to be the tumor suppressor
            genes involved in oligodendroglioma development and progression
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Collins,J.E., Goward,M.E., Cole,C.G., Smink,L.J., Huckle,E.J.,
            Knowles,S., Bye,J.M., Beare,D.M. and Dunham,I.
  TITLE     Reevaluating human gene annotation: a second-generation analysis of
            chromosome 22
  JOURNAL   Genome Res 13 (1), 27-36 (2003)
   PUBMED   12529303
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Korenbaum,E., Olski,T.M. and Noegel,A.A.
  TITLE     Genomic organization and expression profile of the parvin family of
            focal adhesion proteins in mice and humans
  JOURNAL   Gene 279 (1), 69-79 (2001)
   PUBMED   11722847
  REMARK    GeneRIF: Mammalian parvins are likely to have arisen late in
            evolution from gene duplication as they share a remarkably similar
            exon/intron organization.
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Olski,T.M., Noegel,A.A. and Korenbaum,E.
  TITLE     Parvin, a 42 kDa focal adhesion protein, related to the
            alpha-actinin superfamily
  JOURNAL   J Cell Sci 114 (Pt 3), 525-538 (2001)
   PUBMED   11171322
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA673498.1, BC034406.1, AL031595.4 and AI075834.1.
            
            Summary: Members of the parvin family, including PARVG, are
            actin-binding proteins associated with focal contacts.[supplied by
            OMIM, Aug 2004].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034406.1, SRR1163657.520574.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000444313.8/ ENSP00000391583.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..331
                     /product="gamma-parvin"
                     /calculated_mol_wt=37354
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9HBI0.1)"
     Region          17..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBI0.1)"
     Region          45..150
                     /region_name="CH_PARVG_rpt1"
                     /note="first calponin homology (CH) domain found in
                     gamma-parvin; cd21305"
                     /db_xref="CDD:409154"
     Site            order(46,50,101,103..104,107..108,110,122..130,135,
                     137..138,140..141,144..145,148)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409154"
     Region          196..317
                     /region_name="CH_PARVG_rpt2"
                     /note="second calponin homology (CH) domain found in
                     gamma-parvin; cd21307"
                     /db_xref="CDD:409156"
     Site            order(212,216,270,272..273,276..277,279,288..296,301,
                     303..304,306..307,310..311,314)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409156"
     CDS             1..331
                     /gene="PARVG"
                     /coded_by="NM_022141.7:450..1445"
                     /db_xref="CCDS:CCDS14057.1"
                     /db_xref="GeneID:64098"
                     /db_xref="HGNC:HGNC:14654"
                     /db_xref="MIM:608122"
ORIGIN      
        1 mepeflydll qlpkgveppa eeelskggkk kylpptsrkd pkfeelqkvl mewinatllp
       61 ehivvrslee dmfdglilhh lfqrlaalkl eaedialtat sqkhkltvvl eavnrslqle
      121 ewqakwsves ifnkdllstl hllvalakrf qpdlslptnv qvevitiest ksglkseklv
      181 eqlteystdk deppkdvfde lfklapekvn avkeaivnfv nqkldrlgls vqnldtqfad
      241 gvilllligq legfflhlke fyltpnspae mlhnvtlale llkdegllsc pvspedivnk
      301 dakstlrvly glfckhtqka hrdrtphgap n
//
LOCUS       NP_851564                538 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-21 receptor isoform 1 precursor [Homo sapiens].
ACCESSION   NP_851564
VERSION     NP_851564.1
DBSOURCE    REFSEQ: accession NM_181078.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Zang,Z., Yin,Y., Liu,C., Zhu,Q., Huang,X., Li,H. and Yang,R.
  TITLE     IL21R hypomethylation as a biomarker for distinguishing benign and
            malignant breast tumours
  JOURNAL   Epigenetics 19 (1), 2352683 (2024)
   PUBMED   38723244
  REMARK    GeneRIF: IL21R hypomethylation as a biomarker for distinguishing
            benign and malignant breast tumours.
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Xie,Y., Huang,Y., Li,Z.Y., Jiang,W., Shi,N.X., Lu,Y., Cao,G.,
            Yin,Z. and Lin,X.J.
  TITLE     Interleukin-21 receptor signaling promotes metabolic
            dysfunction-associated steatohepatitis-driven hepatocellular
            carcinoma by inducing immunosuppressive IgA+ B cells
  JOURNAL   Mol Cancer 23 (1), 95 (2024)
   PUBMED   38720319
  REMARK    GeneRIF: Interleukin-21 receptor signaling promotes metabolic
            dysfunction-associated steatohepatitis-driven hepatocellular
            carcinoma by inducing immunosuppressive IgA[+] B cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Wu,Z., Li,H., Xu,H., Feng,F., Zhang,F., Zhang,S., Wang,L. and Li,Y.
  TITLE     ChIP-seq analysis found IL21R, a target gene of GTF2I-the
            susceptibility gene for primary biliary cholangitis in Chinese Han
  JOURNAL   Hepatol Int 18 (2), 509-516 (2024)
   PUBMED   37713154
  REMARK    GeneRIF: ChIP-seq analysis found IL21R, a target gene of GTF2I-the
            susceptibility gene for primary biliary cholangitis in Chinese Han.
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Lahmar,R., Chabchoub,E., Zemni,R., Anis,M., Ghannouchi,N. and
            Slama,F.B.H.
  TITLE     Interleukin-21 receptor gene polymorphism (rs2285452 A/G) is
            associated with susceptibility to Behcet's disease
  JOURNAL   Int J Immunogenet 50 (4), 185-193 (2023)
   PUBMED   37243939
  REMARK    GeneRIF: Interleukin-21 receptor gene polymorphism (rs2285452 A/G)
            is associated with susceptibility to Behcet's disease.
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Carreno-Saavedra,N.M., Reyes-Perez,I.V., Machado-Sulbaran,A.C.,
            Martinez-Bonilla,G.E., Ramirez-Duenas,M.G., Munoz-Valle,J.F.,
            Olaya-Valdiviezo,V., Garcia-Iglesias,T., Martinez-Garcia,E.A. and
            Sanchez-Hernandez,P.E.
  TITLE     IL-21 (rs2055979 and rs2221903)/IL-21R (rs3093301) Polymorphism and
            High Levels of IL-21 Are Associated with Rheumatoid Arthritis in
            Mexican Patients
  JOURNAL   Genes (Basel) 14 (4), 878 (2023)
   PUBMED   37107636
  REMARK    GeneRIF: IL-21 (rs2055979 and rs2221903)/IL-21R (rs3093301)
            Polymorphism and High Levels of IL-21 Are Associated with
            Rheumatoid Arthritis in Mexican Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Hecker,M., Bohnert,A., Konig,I.R., Bein,G. and Hackstein,H.
  TITLE     Novel genetic variation of human interleukin-21 receptor is
            associated with elevated IgE levels in females
  JOURNAL   Genes Immun 4 (3), 228-233 (2003)
   PUBMED   12700598
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Asao,H., Okuyama,C., Kumaki,S., Ishii,N., Tsuchiya,S., Foster,D.
            and Sugamura,K.
  TITLE     Cutting edge: the common gamma-chain is an indispensable subunit of
            the IL-21 receptor complex
  JOURNAL   J Immunol 167 (1), 1-5 (2001)
   PUBMED   11418623
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Parrish-Novak,J., Dillon,S.R., Nelson,A., Hammond,A., Sprecher,C.,
            Gross,J.A., Johnston,J., Madden,K., Xu,W., West,J., Schrader,S.,
            Burkhead,S., Heipel,M., Brandt,C., Kuijper,J.L., Kramer,J.,
            Conklin,D., Presnell,S.R., Berry,J., Shiota,F., Bort,S., Hambly,K.,
            Mudri,S., Clegg,C., Moore,M., Grant,F.J., Lofton-Day,C.,
            Gilbert,T., Rayond,F., Ching,A., Yao,L., Smith,D., Webster,P.,
            Whitmore,T., Maurer,M., Kaushansky,K., Holly,R.D. and Foster,D.
  TITLE     Interleukin 21 and its receptor are involved in NK cell expansion
            and regulation of lymphocyte function
  JOURNAL   Nature 408 (6808), 57-63 (2000)
   PUBMED   11081504
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Ozaki,K., Kikly,K., Michalovich,D., Young,P.R. and Leonard,W.J.
  TITLE     Cloning of a type I cytokine receptor most related to the IL-2
            receptor beta chain
  JOURNAL   Proc Natl Acad Sci U S A 97 (21), 11439-11444 (2000)
   PUBMED   11016959
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292663.1, BC004348.1,
            AC002303.1 and AW576566.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a cytokine receptor
            for interleukin 21 (IL21). It belongs to the type I cytokine
            receptors, and has been shown to form a heterodimeric receptor
            complex with the common gamma-chain, a receptor subunit also shared
            by the receptors for interleukin 2, 4, 7, 9, and 15. This receptor
            transduces the growth promoting signal of IL21, and is important
            for the proliferation and differentiation of T cells, B cells, and
            natural killer (NK) cells. The ligand binding of this receptor
            leads to the activation of multiple downstream signaling molecules,
            including JAK1, JAK3, STAT1, and STAT3. Knockout studies of a
            similar gene in mouse suggest a role for this gene in regulating
            immunoglobulin production. Three alternatively spliced transcript
            variants have been described. [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (2) encodes the dominant isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004348.1, AK292663.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337929.8/ ENSP00000338010.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.1"
     Protein         1..538
                     /product="interleukin-21 receptor isoform 1 precursor"
                     /note="IL-21 receptor; novel interleukin receptor"
                     /calculated_mol_wt=57098
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2050
     mat_peptide     20..538
                     /product="interleukin-21 receptor isoform 1"
                     /calculated_mol_wt=57098
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22235133; propagated from
                     UniProtKB/Swiss-Prot (Q9HBE5.1)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBE5.1)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBE5.1)"
     Region          120..225
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(120,192,213)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBE5.1)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBE5.1)"
     Region          214..218
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBE5.1)"
     Site            order(214..215,217..218)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            214
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan.
                     /evidence=ECO:0000269|PubMed:22235133; propagated from
                     UniProtKB/Swiss-Prot (Q9HBE5.1)"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBE5.1)"
     Region          266..274
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBE5.1)"
     Region          342..367
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBE5.1)"
     Region          457..487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBE5.1)"
     CDS             1..538
                     /gene="IL21R"
                     /gene_synonym="CD360; IMD56; NILR"
                     /coded_by="NM_181078.3:462..2078"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS10630.1"
                     /db_xref="GeneID:50615"
                     /db_xref="HGNC:HGNC:6006"
                     /db_xref="MIM:605383"
ORIGIN      
        1 mprgwaapll llllqggwgc pdlvcytdyl qtvicilemw nlhpstltlt wqdqyeelkd
       61 eatscslhrs ahnathatyt chmdvfhfma ddifsvnitd qsgnysqecg sfllaesikp
      121 appfnvtvtf sgqyniswrs dyedpafyml kgklqyelqy rnrgdpwavs prrklisvds
      181 rsvsllplef rkdssyelqv ragpmpgssy qgtwsewsdp vifqtqseel kegwnphlll
      241 llllvivfip afwslkthpl wrlwkkiwav psperffmpl ykgcsgdfkk wvgapftgss
      301 lelgpwspev pstlevysch pprspakrlq ltelqepael vesdgvpkps fwptaqnsgg
      361 sayseerdrp yglvsidtvt vldaegpctw pcsceddgyp aldldaglep spgledplld
      421 agttvlscgc vsagspglgg plgslldrlk ppladgedwa gglpwggrsp ggvseseags
      481 plagldmdtf dsgfvgsdcs spvecdftsp gdegpprsyl rqwvvipppl sspgpqas
//
LOCUS       NP_127491                318 aa            linear   PRI 27-APR-2025
DEFINITION  death effector domain-containing protein isoform b [Homo sapiens].
ACCESSION   NP_127491
VERSION     NP_127491.1
DBSOURCE    REFSEQ: accession NM_032998.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Hong,A.L., Guerriero,J.L., Doshi,M.B., Kynnap,B.D., Kim,W.J.,
            Schinzel,A.C., Modiste,R., Schlauch,A.J., Adam,R.M.,
            Kwiatkowski,D.J., Beroukhim,R., Letai,A., Rosenberg,J.E. and
            Hahn,W.C.
  TITLE     MCL1 and DEDD Promote Urothelial Carcinoma Progression
  JOURNAL   Mol Cancer Res 17 (6), 1294-1304 (2019)
   PUBMED   30777879
  REMARK    GeneRIF: Identify MCL1 and DEDD as genes that contribute to
            aggressive urothelial carcinomas.
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Wu,D.M., Hong,X.W., Wang,L.L., Cui,X.F., Lu,J., Chen,G.Q. and
            Zheng,Y.L.
  TITLE     MicroRNA-17 inhibition overcomes chemoresistance and suppresses
            epithelial-mesenchymal transition through a DEDD-dependent
            mechanism in gastric cancer
  JOURNAL   Int J Biochem Cell Biol 102, 59-70 (2018)
   PUBMED   29953965
  REMARK    GeneRIF: MicroRNA-17 inhibition overcomes chemoresistance and
            suppresses epithelial-mesenchymal transition through a
            DEDD-dependent mechanism in gastric cancer
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Yu,G., Jia,Z. and Dou,Z.
  TITLE     miR-24-3p regulates bladder cancer cell proliferation, migration,
            invasion and autophagy by targeting DEDD
  JOURNAL   Oncol Rep 37 (2), 1123-1131 (2017)
   PUBMED   28000900
  REMARK    GeneRIF: DEDD protein role in cell proliferation and migration of
            bladder cancer
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Lv,Q., Wang,W., Xue,J., Hua,F., Mu,R., Lin,H., Yan,J., Lv,X.,
            Chen,X. and Hu,Z.W.
  TITLE     DEDD interacts with PI3KC3 to activate autophagy and attenuate
            epithelial-mesenchymal transition in human breast cancer
  JOURNAL   Cancer Res 72 (13), 3238-3250 (2012)
   PUBMED   22719072
  REMARK    GeneRIF: Via direct interaction with the class III PI-3-kinase
            (PI3KC3)/Beclin1, DEDD activated autophagy and induced the
            degradation of Snail and Twist, two master regulators of EMT
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Zhan,Y., Hegde,R., Srinivasula,S.M., Fernandes-Alnemri,T. and
            Alnemri,E.S.
  TITLE     Death effector domain-containing proteins DEDD and FLAME-3 form
            nuclear complexes with the TFIIIC102 subunit of human transcription
            factor IIIC
  JOURNAL   Cell Death Differ 9 (4), 439-447 (2002)
   PUBMED   11965497
  REMARK    GeneRIF: DEDD forms nuclear complexes with the TFIIIC102 subunit of
            human transcription factor IIIC
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Roth,W., Stenner-Liewen,F., Pawlowski,K., Godzik,A. and Reed,J.C.
  TITLE     Identification and characterization of DEDD2, a death effector
            domain-containing protein
  JOURNAL   J Biol Chem 277 (9), 7501-7508 (2002)
   PUBMED   11741985
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Schickling,O., Stegh,A.H., Byrd,J. and Peter,M.E.
  TITLE     Nuclear localization of DEDD leads to caspase-6 activation through
            its death effector domain and inhibition of RNA polymerase I
            dependent transcription
  JOURNAL   Cell Death Differ 8 (12), 1157-1168 (2001)
   PUBMED   11753564
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Leo,C.P., Hsu,S.Y., McGee,E.A., Salanova,M. and Hsueh,A.J.
  TITLE     DEFT, a novel death effector domain-containing molecule
            predominantly expressed in testicular germ cells
  JOURNAL   Endocrinology 139 (12), 4839-4848 (1998)
   PUBMED   9832420
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Stegh,A.H., Schickling,O., Ehret,A., Scaffidi,C., Peterhansel,C.,
            Hofmann,T.G., Grummt,I., Krammer,P.H. and Peter,M.E.
  TITLE     DEDD, a novel death effector domain-containing protein, targeted to
            the nucleolus
  JOURNAL   EMBO J 17 (20), 5974-5986 (1998)
   PUBMED   9774341
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591806.16 and BC013910.2.
            
            Summary: This gene encodes a protein that contains a death effector
            domain (DED). DED is a protein-protein interaction domain shared by
            adaptors, regulators and executors of the programmed cell death
            pathway. Overexpression of this gene was shown to induce weak
            apoptosis. Upon stimulation, this protein was found to translocate
            from cytoplasm to nucleus and colocalize with UBTF, a basal factor
            required for RNA polymerase I transcription, in the nucleolus. At
            least three transcript variants encoding the same protein have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) uses an alternate in-frame
            splice junction compared to variant 5. The resulting isoform (b)
            has the same N- and C-termini but is shorter compared to isoform a.
            Variants 1, 3, and 4 all encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.129837.1,
                                           SRR1660809.54455.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368006.8/ ENSP00000356985.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..318
                     /product="death effector domain-containing protein isoform
                     b"
                     /note="death effector domain-containing protein; death
                     effector domain-containing testicular molecule"
                     /calculated_mol_wt=36663
     Region          22..118
                     /region_name="DED_DEDD"
                     /note="Death Effector Domain of DEDD; cd08790"
                     /db_xref="CDD:260058"
     Region          128..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75618.1)"
     Region          160..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75618.1)"
     CDS             1..318
                     /gene="DEDD"
                     /gene_synonym="CASP8IP1; DEDD1; DEDPro1; DEFT; FLDED-1;
                     FLDED1; KE05"
                     /coded_by="NM_032998.3:215..1171"
                     /note="isoform b is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1219.1"
                     /db_xref="GeneID:9191"
                     /db_xref="HGNC:HGNC:2755"
                     /db_xref="MIM:606841"
ORIGIN      
        1 maglkrrasq vwpeehgeqe hglyslhrmf divgthlthr dvrvlsflfv dviddhergl
       61 irngrdflla lerqgrcdes nfrqvlqllr iitrhdllpy vtlkrrravc pdlvdkylee
      121 tsiryvtpra lsdpeprppq psktvpphyp vvccptsgpq mcskrpargr atlgsqrkrr
      181 ksvtpdpkek qtcdirlrvr aeycqhetal qgnvfsnkqd plerqferfn qantilksrd
      241 lgsiicdikf seltyldafw rdyingslle alkgvfitds lkqavgheai kllvnvdeed
      301 yelgrqkllr nlmlqalp
//
LOCUS       NP_001353143             925 aa            linear   PRI 27-APR-2025
DEFINITION  disks large homolog 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001353143 XP_016861293
VERSION     NP_001353143.1
DBSOURCE    REFSEQ: accession NM_001366214.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   4  (residues 1 to 925)
  AUTHORS   Veljacic Viskovic,D., Lozic,M., Vukoja,M., Soljic,V., Vukojevic,K.,
            Glavina Durdov,M., Filipovic,N. and Lozic,B.
  TITLE     Spatio-Temporal Expression Pattern of CAKUT Candidate Genes DLG1
            and KIF12 during Human Kidney Development
  JOURNAL   Biomolecules 13 (2), 340 (2023)
   PUBMED   36830709
  REMARK    GeneRIF: Spatio-Temporal Expression Pattern of CAKUT Candidate
            Genes DLG1 and KIF12 during Human Kidney Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 925)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 925)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 925)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 925)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 925)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 925)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861293.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2147293.1,
                                           SRR11853561.21858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..925
                     /product="disks large homolog 1 isoform 11"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=103062
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..223
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          222..310
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(233..239,256,259,289,293,296..297)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          319..403
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(328..334,351,354,384,388,391..392)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          404..465
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          463..553
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(475..481,492,495,525,529,532..533)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          582..648
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(587,609..610,631)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(590,592,595,604,622..623,642,644..645)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          734..912
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..925
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366214.1:495..3272"
                     /note="isoform 11 is encoded by transcript variant 19"
                     /db_xref="CCDS:CCDS93454.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kpteavlpsp ptvpvipvlp
      181 vpaentvilp tipqanpppv lvntdsletp tyvngtdady eyeeitlerg nsglgfsiag
      241 gtdnphigdd ssifitkiit ggaaaqdgrl rvndcilrvn evdvrdvths kavealkeag
      301 sivrlyvkrr kpvsekimei klikgpkglg fsiaggvgnq hipgdnsiyv tkiieggaah
      361 kdgklqigdk llavnnvcle evtheeavta lkntsdfvyl kvakptsmym ndgyappdit
      421 nsssqpvdnh vspssflgqt pasparyspv skavlgddei treprkvvlh rgstglgfni
      481 vggedgegif isfilaggpa dlsgelrkgd riisvnsvdl raasheqaaa alknagqavt
      541 ivaqyrpeey srfeakihdl reqmmnssis sgsgslrtsq krslyvralf dydktkdsgl
      601 psqglnfkfg dilhvinasd dewwqarqvt pdgesdevgv ipskrrvekk erarlktvkf
      661 nsktrdkgsf ndkrkknlfs rkfpfyknkd qseqetsdad qhvtsnasds essyrgqeey
      721 vlsyepvnqq evnytrpvii lgpmkdrind dlisefpdkf gscvphttrp krdyevdgrd
      781 yhfvtsreqm ekdiqehkfi eagqynnhly gtsvqsvrev aekgkhcild vsgnaikrlq
      841 iaqlypisif ikpksmenim emnkrlteeq arktferamk leqeftehft aivqgdtled
      901 iynqvkqiie eqsgsyiwvp akekl
//
LOCUS       NP_001356347             273 aa            linear   PRI 27-APR-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 3 [Homo sapiens].
ACCESSION   NP_001356347 XP_016881954
VERSION     NP_001356347.1
DBSOURCE    REFSEQ: accession NM_001369418.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
            Review article
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Du,P., Li,G., Wu,L. and Huang,M.
  TITLE     Perspectives of ERCC1 in early-stage and advanced cervical cancer:
            From experiments to clinical applications
  JOURNAL   Front Immunol 13, 1065379 (2023)
   PUBMED   36713431
  REMARK    GeneRIF: Perspectives of ERCC1 in early-stage and advanced cervical
            cancer: From experiments to clinical applications.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 273)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 273)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139353.3 and AC092309.3.
            
            On Apr 9, 2019 this sequence version replaced XP_016881954.1.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.14348.1,
                                           SRR14372080.453171.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..273
                     /product="DNA excision repair protein ERCC-1 isoform 3"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=29862
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          235..264
                     /region_name="HHH"
                     /note="Helix-hairpin-helix motif; pfam00633"
                     /db_xref="CDD:425789"
     CDS             1..273
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369418.1:103..924"
                     /note="isoform 3 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS54279.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrsleqli
      241 aasredlalc pglgpqkarr lfdvlhepfl kvp
//
LOCUS       NP_766161                734 aa            linear   ROD 27-APR-2025
DEFINITION  cytosolic endo-beta-N-acetylglucosaminidase isoform 1 [Mus
            musculus].
ACCESSION   NP_766161
VERSION     NP_766161.1
DBSOURCE    REFSEQ: accession NM_172573.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Yoshida,Y., Asahina,M., Murakami,A., Kawawaki,J., Yoshida,M.,
            Fujinawa,R., Iwai,K., Tozawa,R., Matsuda,N., Tanaka,K. and
            Suzuki,T.
  TITLE     Loss of peptide:N-glycanase causes proteasome dysfunction mediated
            by a sugar-recognizing ubiquitin ligase
  JOURNAL   Proc Natl Acad Sci U S A 118 (27) (2021)
   PUBMED   34215698
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Maynard,J.C., Fujihira,H., Dolgonos,G.E., Suzuki,T. and
            Burlingame,A.L.
  TITLE     Cytosolic N-GlcNAc proteins are formed by the action of
            endo-beta-N-acetylglucosaminidase
  JOURNAL   Biochem Biophys Res Commun 530 (4), 719-724 (2020)
   PUBMED   32782141
  REMARK    GeneRIF: Cytosolic N-GlcNAc proteins are formed by the action of
            endo-beta-N-acetylglucosaminidase.
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Fujihira,H., Masahara-Negishi,Y., Akimoto,Y., Hirayama,H.,
            Lee,H.C., Story,B.A., Mueller,W.F., Jakob,P., Clauder-Munster,S.,
            Steinmetz,L.M., Radhakrishnan,S.K., Kawakami,H., Kamada,Y.,
            Miyoshi,E., Yokomizo,T. and Suzuki,T.
  TITLE     Liver-specific deletion of Ngly1 causes abnormal nuclear morphology
            and lipid metabolism under food stress
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1866 (3), 165588 (2020)
   PUBMED   31733337
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Fujihira,H., Masahara-Negishi,Y., Tamura,M., Huang,C., Harada,Y.,
            Wakana,S., Takakura,D., Kawasaki,N., Taniguchi,N., Kondoh,G.,
            Yamashita,T., Funakoshi,Y. and Suzuki,T.
  TITLE     Lethality of mice bearing a knockout of the Ngly1-gene is partially
            rescued by the additional deletion of the Engase gene
  JOURNAL   PLoS Genet 13 (4), e1006696 (2017)
   PUBMED   28426790
  REMARK    GeneRIF: These observations strongly suggest that the Ngly1- or
            Ngly1/Engase-deficient mice could serve as a valuable animal model
            for studies related to the pathogenesis of the NGLY1-deficiency,
            and that cytoplasmic ENGase represents one of the potential
            therapeutic targets for this genetic disorder.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 734)
  AUTHORS   Harada,Y., Huang,C., Yamaki,S., Dohmae,N. and Suzuki,T.
  TITLE     Non-lysosomal Degradation of Singly Phosphorylated Oligosaccharides
            Initiated by the Action of a Cytosolic
            Endo-beta-N-acetylglucosaminidase
  JOURNAL   J Biol Chem 291 (15), 8048-8058 (2016)
   PUBMED   26858256
  REMARK    GeneRIF: ENGase efficiently hydrolyzes phosphorylated
            oligosaccharides that are larger than Man4GlcNAc2-P, generating
            GlcNAc-1-P and neutral Gn1-type free oligosaccharides.
REFERENCE   6  (residues 1 to 734)
  AUTHORS   Huang,C., Harada,Y., Hosomi,A., Masahara-Negishi,Y., Seino,J.,
            Fujihira,H., Funakoshi,Y., Suzuki,T., Dohmae,N. and Suzuki,T.
  TITLE     Endo-beta-N-acetylglucosaminidase forms N-GlcNAc protein aggregates
            during ER-associated degradation in Ngly1-defective cells
  JOURNAL   Proc Natl Acad Sci U S A 112 (5), 1398-1403 (2015)
   PUBMED   25605922
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY070749.1, AK048667.1 and BC060640.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849374,
                              SAMN00849375 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 83.21 cM"
     Protein         1..734
                     /product="cytosolic endo-beta-N-acetylglucosaminidase
                     isoform 1"
                     /EC_number="3.2.1.96"
                     /note="cytosolic endo-beta-N-acetylglucosaminidase"
                     /calculated_mol_wt=82815
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BX80.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q8NFI3; propagated from
                     UniProtKB/Swiss-Prot (Q8BX80.1)"
     Region          118..428
                     /region_name="GH85_ENGase"
                     /note="Endo-beta-N-acetylglucosaminidase (ENGase)
                     hydrolyzes the N-N'-diacetylchitobiosyl core of
                     N-glycosylproteins. The beta-1,4-glycosyl bond located
                     between two N-acetylglucosamine residues is hydrolyzed
                     such that N-acetylglucosamine 1 remains with the...;
                     cd06547"
                     /db_xref="CDD:119364"
     Site            order(126,153,225,227,229,294,296..297)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:119364"
     CDS             1..734
                     /gene="Engase"
                     /gene_synonym="C130099A03; D230014K01Rik"
                     /coded_by="NM_172573.3:155..2359"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS25704.1"
                     /db_xref="GeneID:217364"
                     /db_xref="MGI:MGI:2443788"
ORIGIN      
        1 metssvltrg aarqrspaap ekqardqter rpgrrrqgrr inedqeeeav frevvsftpd
       61 plparyydkd ttrpisfyls tleellawtp lmedgfnval eplvcrrppl ssprprtllc
      121 hdmmggyled rfiqgsevqn pysfyhwqyi difvyfshht vtippvcwtn aahrhgvcvl
      181 gtfitewqeg grlceaflag depsfqavad rlvqiaqffr fdgwlinien sltpaavrnt
      241 plflqyltaq lhqqvpgglv lwydsvvqsg qlkwqdelnd qnrvffdscd gfftnynwre
      301 dhlqrmvaqa gerladvyvg vdvfarsnvv ggrfdtdksl elirkhgfsa alfapgwvye
      361 cleksdffqn qdkfwsller flpthsicsl pfvtsfclgl gtrrvcygke qavgpwyhps
      421 aqetqplfge hklagdsrgw vkthccltda whggsslllr glippevdsv avrlfslhip
      481 vppkvflsmv ykfegstdvq valelttgda sschvggmlv lnetgsrhsp rplrvpptrl
      541 arwasscgqq lsggwiqrcy evnlrgcllq dllvsfsrpp gsreeesfic rlgeiqvvda
      601 ssllaplprv qnvtisqirw lplitgsegl ptrlllsctl hwsylllrar cfrihcwkrt
      661 gssssvaesp etekptflgl afanqyrvvd laveaagfgq dgrveflvep vpregflvpq
      721 aewgkavllf svpq
//
LOCUS       NP_001207428             255 aa            linear   ROD 27-APR-2025
DEFINITION  RING finger protein 223 [Mus musculus].
ACCESSION   NP_001207428 XP_003084655 XP_003086469 XP_006538493
VERSION     NP_001207428.1
DBSOURCE    REFSEQ: accession NM_001220499.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL928667.4.
            
            On or before Nov 20, 2015 this sequence version replaced
            XP_006538493.1, XP_003084655.1, XP_003086469.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660817.139528.1,
                                           SRR11927934.52613.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 88.44 cM"
     Protein         1..255
                     /product="RING finger protein 223"
                     /calculated_mol_wt=27108
     Region          49..108
                     /region_name="RING-HC_RNF183-like"
                     /note="RING finger, HC subclass, found in RING finger
                     protein RNF183, RNF223, RNF225 and similar proteins;
                     cd16556"
                     /db_xref="CDD:438218"
     CDS             1..255
                     /gene="Rnf223"
                     /gene_synonym="9930005F22Rik"
                     /coded_by="NM_001220499.3:294..1061"
                     /db_xref="CCDS:CCDS84838.1"
                     /db_xref="GeneID:100045778"
                     /db_xref="MGI:MGI:3588193"
ORIGIN      
        1 mssghrvwra amppyrqnss tasvprspgs ggspkspstp gsvkvasple csicfsgydn
       61 ifktpkelsc shvfclecla rlaaaqpagr sgreavpcpf crqpttvpva gapalrtsrq
      121 lqaklpahlq reepvwlegt klccrplptt sgqedggfvs vdvglskpae ptlpvpvqdp
      181 apnpgwlarc warfrdwrrv alvsvlllvl fcvilwpvqc alktgnlrci nrppaatata
      241 tvttdalsfg vlann
//
LOCUS       NP_002146                643 aa            linear   PRI 27-APR-2025
DEFINITION  heat shock 70 kDa protein 6 [Homo sapiens].
ACCESSION   NP_002146 XP_001134322
VERSION     NP_002146.2
DBSOURCE    REFSEQ: accession NM_002155.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Zhu,X., Chen,X., Shen,X., Liu,Y., Fu,W., Wang,B., Zhao,L., Yang,F.,
            Mo,N., Zhong,G., Jiang,S. and Yang,Z.
  TITLE     PP4R1 accelerates the malignant progression of NSCLC via
            up-regulating HSPA6 expression and HSPA6-mediated ER stress
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (1), 119588 (2024)
   PUBMED   37739270
  REMARK    GeneRIF: PP4R1 accelerates the malignant progression of NSCLC via
            up-regulating HSPA6 expression and HSPA6-mediated ER stress.
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Guo,R., Guo,Y.Z., Zhou,Q., Li,G., Du,Z., Shi,Y. and Xing,Q.
  TITLE     ROR2 deficit may induce the tetralogy of Fallot via down-regulating
            of beta-catenin/SOX3/HSPA6 in vitro and in vivo
  JOURNAL   J Cell Mol Med 27 (22), 3539-3552 (2023)
   PUBMED   37749917
  REMARK    GeneRIF: ROR2 deficit may induce the tetralogy of Fallot via
            down-regulating of beta-catenin/SOX3/HSPA6 in vitro and in vivo.
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Huang,X., Wang,Z., Zhang,J., Ni,X., Bai,G., Cao,J., Zhang,C.,
            Han,Z. and Liu,T.
  TITLE     BARX1 promotes osteosarcoma cell proliferation and invasion by
            regulating HSPA6 expression
  JOURNAL   J Orthop Surg Res 18 (1), 211 (2023)
   PUBMED   36927457
  REMARK    GeneRIF: BARX1 promotes osteosarcoma cell proliferation and
            invasion by regulating HSPA6 expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Song,B., Shen,S., Fu,S. and Fu,J.
  TITLE     HSPA6 and its role in cancers and other diseases
  JOURNAL   Mol Biol Rep 49 (11), 10565-10577 (2022)
   PUBMED   35666422
  REMARK    GeneRIF: HSPA6 and its role in cancers and other diseases.
            Review article
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Vavilova,J.D., Boyko,A.A., Troyanova,N.I., Ponomareva,N.V.,
            Fokin,V.F., Fedotova,E.Y., Streltsova,M.A., Kust,S.A.,
            Grechikhina,M.V., Shustova,O.A., Azhikina,T.L., Kovalenko,E.I. and
            Sapozhnikov,A.M.
  TITLE     Alterations in Proteostasis System Components in Peripheral Blood
            Mononuclear Cells in Parkinson Disease: Focusing on the HSP70 and
            p62 Levels
  JOURNAL   Biomolecules 12 (4), 493 (2022)
   PUBMED   35454081
  REMARK    GeneRIF: Alterations in Proteostasis System Components in
            Peripheral Blood Mononuclear Cells in Parkinson Disease: Focusing
            on the HSP70 and p62 Levels.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Mercier,P.A., Winegarden,N.A. and Westwood,J.T.
  TITLE     Human heat shock factor 1 is predominantly a nuclear protein before
            and after heat stress
  JOURNAL   J Cell Sci 112 (Pt 16), 2765-2774 (1999)
   PUBMED   10413683
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Rensing,S.A. and Maier,U.G.
  TITLE     Phylogenetic analysis of the stress-70 protein family
  JOURNAL   J Mol Evol 39 (1), 80-86 (1994)
   PUBMED   7545947
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Leung,T.K., Hall,C., Rajendran,M., Spurr,N.K. and Lim,L.
  TITLE     The human heat-shock genes HSPA6 and HSPA7 are both expressed and
            localize to chromosome 1
  JOURNAL   Genomics 12 (1), 74-79 (1992)
   PUBMED   1346391
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Leung,T.K., Rajendran,M.Y., Monfries,C., Hall,C. and Lim,L.
  TITLE     The human heat-shock protein family. Expression of a novel
            heat-inducible HSP70 (HSP70B') and isolation of its cDNA and
            genomic DNA
  JOURNAL   Biochem J 267 (1), 125-132 (1990)
   PUBMED   2327978
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Schiller,P., Amin,J., Ananthan,J., Brown,M.E., Scott,W.A. and
            Voellmy,R.
  TITLE     Cis-acting elements involved in the regulated expression of a human
            HSP70 gene
  JOURNAL   J Mol Biol 203 (1), 97-105 (1988)
   PUBMED   3184191
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK093925.1, BC035665.1, AL590385.23 and CD366171.1.
            
            On or before Sep 20, 2006 this sequence version replaced
            XP_001134322.1, NP_002146.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR7346977.931148.1,
                                        SRR1803613.132626.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309758.6/ ENSP00000310219.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..643
                     /product="heat shock 70 kDa protein 6"
                     /note="heat shock 70kD protein 6 (HSP70B'); heat shock 70
                     kDa protein B'; heat shock 70kDa protein 6 (HSP70B');
                     epididymis secretory sperm binding protein; heat shock
                     protein family A member 6"
                     /calculated_mol_wt=70897
     Region          3..388
                     /region_name="Nucleotide-binding domain (NBD).
                     /evidence=ECO:0000250|UniProtKB:P11142"
                     /note="propagated from UniProtKB/Swiss-Prot (P17066.2)"
     Region          8..643
                     /region_name="PTZ00009"
                     /note="heat shock 70 kDa protein; Provisional"
                     /db_xref="CDD:240227"
     Region          396..511
                     /region_name="Substrate-binding domain (SBD).
                     /evidence=ECO:0000250|UniProtKB:P11142"
                     /note="propagated from UniProtKB/Swiss-Prot (P17066.2)"
     Site            563
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by METTL21A, in vitro.
                     /evidence=ECO:0000269|PubMed:23921388; propagated from
                     UniProtKB/Swiss-Prot (P17066.2)"
     Region          616..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17066.2)"
     CDS             1..643
                     /gene="HSPA6"
                     /gene_synonym="HSP70B'"
                     /coded_by="NM_002155.5:120..2051"
                     /db_xref="CCDS:CCDS1231.1"
                     /db_xref="GeneID:3310"
                     /db_xref="HGNC:HGNC:5239"
                     /db_xref="MIM:140555"
ORIGIN      
        1 mqaprelavg idlgttyscv gvfqqgrvei landqgnrtt psyvaftdte rlvgdaaksq
       61 aalnphntvf dakrligrkf adttvqsdmk hwpfrvvseg gkpkvrvcyr gedktfypee
      121 issmvlskmk etaeaylgqp vkhavitvpa yfndsqrqat kdagaiagln vlriinepta
      181 aaiaygldrr gagernvlif dlgggtfdvs vlsidagvfe vkatagdthl ggedfdnrlv
      241 nhfmeefrrk hgkdlsgnkr alrrlrtace rakrtlssst qatleidslf egvdfytsit
      301 rarfeelcsd lfrstlepve kalrdakldk aqihdvvlvg gstripkvqk llqdffngke
      361 lnksinpdea vaygaavqaa vlmgdkcekv qdlllldvap lslgletagg vmttliqrna
      421 tiptkqtqtf ttysdnqpgv fiqvyegera mtkdnnllgr felsgippap rgvpqievtf
      481 didangilsv tatdrstgka nkititndkg rlskeeverm vheaeqykae deaqrdrvaa
      541 knsleahvfh vkgslqeesl rdkipeedrr kmqdkcrevl awlehnqlae keeyehqkre
      601 leqicrpifs rlyggpgvpg gsscgtqarq gdpstgpiie evd
//
LOCUS       NP_005036               3460 aa            linear   PRI 27-APR-2025
DEFINITION  reelin isoform a precursor [Homo sapiens].
ACCESSION   NP_005036
VERSION     NP_005036.2
DBSOURCE    REFSEQ: accession NM_005045.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3460)
  AUTHORS   Serafin,D.S., Harris,N.R., Balint,L., Douglas,E.S. and Caron,K.M.
  TITLE     Proximity interactome of lymphatic VE-cadherin reveals mechanisms
            of junctional remodeling and reelin secretion
  JOURNAL   Nat Commun 15 (1), 7734 (2024)
   PUBMED   39232006
  REMARK    GeneRIF: Proximity interactome of lymphatic VE-cadherin reveals
            mechanisms of junctional remodeling and reelin secretion.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 3460)
  AUTHORS   Riva,M., Ferreira,S., Hayashi,K., Saillour,Y., Medvedeva,V.P.,
            Honda,T., Hayashi,K., Altersitz,C., Albadri,S., Rosello,M.,
            Dang,J., Serafini,M., Causeret,F., Henry,O.J., Roux,C.J.,
            Bellesme,C., Freri,E., Josifova,D., Parrini,E., Guerrini,R., Del
            Bene,F., Nakajima,K., Bahi-Buisson,N. and Pierani,A.
  TITLE     De novo monoallelic Reelin missense variants cause dominant
            neuronal migration disorders via a dominant-negative mechanism
  JOURNAL   J Clin Invest 134 (16), e153097 (2024)
   PUBMED   38980724
  REMARK    GeneRIF: De novo monoallelic Reelin missense variants cause
            dominant neuronal migration disorders via a dominant-negative
            mechanism.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 3460)
  AUTHORS   Fuentealba,L.M., Pizarro,H. and Marzolo,M.P.
  TITLE     OCRL1 Deficiency Affects the Intracellular Traffic of ApoER2 and
            Impairs Reelin-Induced Responses
  JOURNAL   Biomolecules 14 (7), 799 (2024)
   PUBMED   39062513
  REMARK    GeneRIF: OCRL1 Deficiency Affects the Intracellular Traffic of
            ApoER2 and Impairs Reelin-Induced Responses.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3460)
  AUTHORS   Afridi,T.U.K., Fatima,A., Satti,H.S., Akram,Z., Yousafzai,I.K.,
            Naeem,W.B., Fatima,N., Ali,A., Iqbal,Z., Khan,A., Shahzad,M.,
            Liu,C., Toft,M., Zhang,F., Tariq,M., Davis,E.E. and Khan,T.N.
  TITLE     Exome sequencing in four families with neurodevelopmental
            disorders: genotype-phenotype correlation and identification of
            novel disease-causing variants in VPS13B and RELN
  JOURNAL   Mol Genet Genomics 299 (1), 55 (2024)
   PUBMED   38771357
  REMARK    GeneRIF: Exome sequencing in four families with neurodevelopmental
            disorders: genotype-phenotype correlation and identification of
            novel disease-causing variants in VPS13B and RELN.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 3460)
  AUTHORS   Ping,J., Wan,J., Luo,J., Du,B., Liu,X., Jiang,T. and Zhang,J.
  TITLE     The interaction of RELN-DNMT genes involving in neurotrophin
            signaling pathway contributes to schizophrenia susceptibility
  JOURNAL   Int J Dev Neurosci 84 (2), 154-159 (2024)
   PUBMED   38296839
  REMARK    GeneRIF: The interaction of RELN-DNMT genes involving in
            neurotrophin signaling pathway contributes to schizophrenia
            susceptibility.
REFERENCE   6  (residues 1 to 3460)
  AUTHORS   Lambert de Rouvroit,C., Bernier,B., Royaux,I., de Bergeyck,V. and
            Goffinet,A.M.
  TITLE     Evolutionarily conserved, alternative splicing of reelin during
            brain development
  JOURNAL   Exp Neurol 156 (2), 229-238 (1999)
   PUBMED   10328932
REFERENCE   7  (residues 1 to 3460)
  AUTHORS   Impagnatiello,F., Guidotti,A.R., Pesold,C., Dwivedi,Y.,
            Caruncho,H., Pisu,M.G., Uzunov,D.P., Smalheiser,N.R., Davis,J.M.,
            Pandey,G.N., Pappas,G.D., Tueting,P., Sharma,R.P. and Costa,E.
  TITLE     A decrease of reelin expression as a putative vulnerability factor
            in schizophrenia
  JOURNAL   Proc Natl Acad Sci U S A 95 (26), 15718-15723 (1998)
   PUBMED   9861036
REFERENCE   8  (residues 1 to 3460)
  AUTHORS   DeSilva,U., D'Arcangelo,G., Braden,V.V., Chen,J., Miao,G.G.,
            Curran,T. and Green,E.D.
  TITLE     The human reelin gene: isolation, sequencing, and mapping on
            chromosome 7
  JOURNAL   Genome Res 7 (2), 157-164 (1997)
   PUBMED   9049633
REFERENCE   9  (residues 1 to 3460)
  AUTHORS   D'Arcangelo,G., Miao,G.G., Chen,S.C., Soares,H.D., Morgan,J.I. and
            Curran,T.
  TITLE     A protein related to extracellular matrix proteins deleted in the
            mouse mutant reeler
  JOURNAL   Nature 374 (6524), 719-723 (1995)
   PUBMED   7715726
REFERENCE   10 (residues 1 to 3460)
  AUTHORS   Michelucci,R., Pasini,E. and Dazzo,E.
  TITLE     Autosomal Dominant Epilepsy with Auditory Features
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301709
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002067.2, KF458525.1,
            AC073208.4, AC005101.2, AC000121.1, AC006316.2 and AC005064.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 31, 2002 this sequence version replaced NP_005036.1.
            
            Summary: This gene encodes a large secreted extracellular matrix
            protein thought to control cell-cell interactions critical for cell
            positioning and neuronal migration during brain development. This
            protein may be involved in schizophrenia, autism, bipolar disorder,
            major depression and in migration defects associated with temporal
            lobe epilepsy. Mutations of this gene are associated with autosomal
            recessive lissencephaly with cerebellar hypoplasia. Two transcript
            variants encoding distinct isoforms have been identified for this
            gene. Other transcript variants have been described but their full
            length nature has not been determined. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript, and encodes the longer isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U79716.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000428762.6/ ENSP00000392423.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..3460
                     /product="reelin isoform a precursor"
                     /calculated_mol_wt=385606
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2802
     Region          48..178
                     /region_name="Reeler"
                     /note="the N-terminal domain of reelin, F-spondin, and a
                     variety of other proteins; cd08544"
                     /db_xref="CDD:260081"
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          202..351
                     /region_name="Reelin_subrepeat_Nt"
                     /note="Additional N-terminal subrepeat of reelin; cd10036"
                     /db_xref="CDD:197344"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Site            305
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          421..556
                     /region_name="Reelin_subrepeat_like"
                     /note="Tandem repeat subunit of reelin and related
                     proteins; cl15240"
                     /db_xref="CDD:197448"
     Region          526..671
                     /region_name="Reelin_repeat_1_subrepeat_1"
                     /note="N-terminal subrepeat of tandem repeat unit 1 of
                     reelin and related proteins; cd10037"
                     /db_xref="CDD:197345"
     Site            order(538..539,556..557,559,563..566,598..599,646..647,
                     649)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197345"
     Site            order(571,573,634,669,671)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197345"
     Site            order(586,607,609..610,625,627..628,636,638)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197345"
     Region          592..603
                     /region_name="BNR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Site            628
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          708..862
                     /region_name="Reelin_repeat_1_subrepeat_2"
                     /note="C-terminal subrepeat of tandem repeat unit 1 of
                     reelin and related proteins; cd10045"
                     /db_xref="CDD:197353"
     Site            order(710,712,768..769,771,773,823,825..827,860)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197353"
     Site            order(730,753..754,796,798,812)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197353"
     Site            order(761,802..803,805)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197353"
     Region          798..809
                     /region_name="BNR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Region          867..1034
                     /region_name="Reelin_repeat_2_subrepeat_1"
                     /note="N-terminal subrepeat of tandem repeat unit 2 of
                     reelin and related proteins; cd10038"
                     /db_xref="CDD:197346"
     Site            order(884..885,911..912,914,918..921,957..958,1005..1006,
                     1008)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197346"
     Site            order(927,929,993,1028,1030)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197346"
     Site            order(945,966,968..969,984,986..987,995,997)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197346"
     Region          951..962
                     /region_name="BNR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Region          1037..1059
                     /region_name="EGF_2"
                     /note="EGF-like domain; pfam07974"
                     /db_xref="CDD:400365"
     Region          1065..1220
                     /region_name="Reelin_repeat_2_subrepeat_2"
                     /note="C-terminal subrepeat of tandem repeat unit 2 of
                     reelin and related proteins; cd10046"
                     /db_xref="CDD:197354"
     Site            order(1068,1070,1128..1129,1131,1133,1181,1183..1185,1218)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197354"
     Site            order(1087,1113..1114,1154,1156,1170)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197354"
     Site            order(1121,1160..1161,1163)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197354"
     Region          1156..1167
                     /region_name="BNR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Region          1240..1409
                     /region_name="Reelin_repeat_3_subrepeat_1"
                     /note="N-terminal subrepeat of tandem repeat unit 3 of
                     reelin and related proteins; cd10039"
                     /db_xref="CDD:197347"
     Site            order(1257..1258,1284..1285,1287,1291..1294,1328..1329,
                     1382..1383,1385)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197347"
     Site            1266
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Site            order(1300,1302,1370,1407,1409)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197347"
     Site            order(1316,1337,1339..1340,1361,1363..1364,1372,1374)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197347"
     Region          1322..1333
                     /region_name="BNR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Region          <1406..1440
                     /region_name="EB"
                     /note="EB module; pfam01683"
                     /db_xref="CDD:460294"
     Region          1447..1597
                     /region_name="Reelin_repeat_3_subrepeat_2"
                     /note="C-terminal subrepeat of tandem repeat unit 3 of
                     reelin and related proteins; cd10047"
                     /db_xref="CDD:197355"
     Site            order(1449,1451,1504..1505,1507,1509,1559,1561..1563,1595)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197355"
     Site            order(1466,1489..1490,1532,1534,1548)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197355"
     Site            order(1497,1538..1539,1541)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197355"
     Region          1534..1545
                     /region_name="BNR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Site            1599
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          1605..1774
                     /region_name="Reelin_repeat_4_subrepeat_1"
                     /note="N-terminal subrepeat of tandem repeat unit 4 of
                     reelin and related proteins; cd10040"
                     /db_xref="CDD:197348"
     Site            order(1621..1622,1647..1648,1650,1654..1657,1691..1692,
                     1739..1740,1742)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197348"
     Site            order(1663,1665,1727,1763,1765)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197348"
     Site            order(1679,1700,1702..1703,1713,1715..1716,1729,1731)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197348"
     Region          1685..1696
                     /region_name="BNR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Site            1749
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          1772..1794
                     /region_name="EGF_2"
                     /note="EGF-like domain; pfam07974"
                     /db_xref="CDD:400365"
     Region          1800..1949
                     /region_name="Reelin_repeat_4_subrepeat_2"
                     /note="C-terminal subrepeat of tandem repeat unit 4 of
                     reelin and related proteins; cd10048"
                     /db_xref="CDD:197356"
     Site            order(1803,1805,1860..1861,1863,1865,1908,1910..1912,1945)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197356"
     Site            order(1821,1845..1846,1881,1883,1897)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197356"
     Site            order(1853,1887..1888,1890)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197356"
     Region          1883..1894
                     /region_name="BNR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Site            1920
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          1956..2130
                     /region_name="Reelin_repeat_5_subrepeat_1"
                     /note="N-terminal subrepeat of tandem repeat unit 5 of
                     reelin and related proteins; cd10041"
                     /db_xref="CDD:197349"
     Site            order(1971..1972,2004..2005,2007,2011..2014,2048..2049,
                     2101..2102,2104)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197349"
     Site            order(2020,2022,2089,2127,2129)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197349"
     Site            order(2022,2033..2035,2057,2073..2075,2080,2083..2084,
                     2089,2091,2127,2130)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197349"
     Region          2042..2053
                     /region_name="BNR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Region          2136..2159
                     /region_name="EGF_2"
                     /note="EGF-like domain; pfam07974"
                     /db_xref="CDD:400365"
     Site            2144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          2165..2314
                     /region_name="Reelin_repeat_5_subrepeat_2"
                     /note="C-terminal subrepeat of tandem repeat unit 5 of
                     reelin and related proteins; cd10049"
                     /db_xref="CDD:197357"
     Site            order(2168,2170,2224..2225,2227,2229,2275,2277..2279,2312)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197357"
     Site            order(2186,2209..2210,2247,2249,2263)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197357"
     Site            order(2217,2253..2254,2256)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197357"
     Region          2249..2260
                     /region_name="BNR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Site            2268
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Site            2316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          2322..2478
                     /region_name="Reelin_repeat_6_subrepeat_1"
                     /note="N-terminal subrepeat of tandem repeat unit 6 of
                     reelin and related proteins; cd10042"
                     /db_xref="CDD:197350"
     Site            order(2336..2337,2361..2362,2364,2368..2371,2404..2405,
                     2452..2453,2455)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197350"
     Site            order(2344,2357..2358,2388,2467,2469)
                     /site_type="other"
                     /note="reelin receptor interface"
                     /db_xref="CDD:197350"
     Site            order(2377,2379,2440,2476,2478)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197350"
     Site            order(2392,2413,2415..2416,2431,2433..2434,2442,2444)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197350"
     Region          2398..2409
                     /region_name="BNR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Region          2514..2661
                     /region_name="Reelin_repeat_6_subrepeat_2"
                     /note="C-terminal subrepeat of tandem repeat unit 6 of
                     reelin and related proteins; cd10050"
                     /db_xref="CDD:197358"
     Site            order(2517,2519,2573..2574,2576,2578,2622,2624..2626,2659)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197358"
     Site            order(2535,2558..2559,2595,2597,2611)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197358"
     Site            order(2566,2601..2602,2604)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197358"
     Site            2568
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          2597..2608
                     /region_name="BNR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Region          2669..2853
                     /region_name="Reelin_repeat_7_subrepeat_1"
                     /note="N-terminal subrepeat of tandem repeat unit 7 of
                     reelin and related proteins; cd10043"
                     /db_xref="CDD:197351"
     Site            order(2712..2713,2738..2739,2741,2745..2748,2783..2784,
                     2828..2829,2831)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197351"
     Site            order(2754,2756,2818,2851,2853)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197351"
     Site            order(2771,2792,2794..2795,2806,2808..2809,2820,2822)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197351"
     Region          2777..2788
                     /region_name="BNR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Region          2860..2882
                     /region_name="EGF_2"
                     /note="EGF-like domain; pfam07974"
                     /db_xref="CDD:400365"
     Region          2889..3050
                     /region_name="Reelin_repeat_7_subrepeat_2"
                     /note="C-terminal subrepeat of tandem repeat unit 7 of
                     reelin and related proteins; cd10051"
                     /db_xref="CDD:197359"
     Site            order(2891,2893,2948..2949,2951,2953,3003,3005..3007,3047)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197359"
     Site            order(2910,2933..2934,2976,2978,2992)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197359"
     Site            order(2941,2982..2983,2985)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197359"
     Site            2961
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          2978..2989
                     /region_name="BNR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Site            3015
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          3055..3229
                     /region_name="Reelin_repeat_8_subrepeat_1"
                     /note="N-terminal subrepeat of tandem repeat unit 8 of
                     reelin and related proteins; cd10044"
                     /db_xref="CDD:197352"
     Site            3072
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Site            order(3074..3075,3103..3104,3106,3110..3113,3149..3150,
                     3202..3203,3205)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197352"
     Site            order(3119,3121,3190,3226,3228)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197352"
     Site            order(3136,3158,3160..3161,3176,3178..3179,3192,3194)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197352"
     Region          3142..3154
                     /region_name="BNR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Site            3184
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Region          3231..3259
                     /region_name="EGF_Tenascin"
                     /note="Tenascin EGF domain; cl46594"
                     /db_xref="CDD:480934"
     Region          3266..3426
                     /region_name="Reelin_repeat_8_subrepeat_2"
                     /note="C-terminal subrepeat of tandem repeat unit 8 of
                     reelin and related proteins; cd10052"
                     /db_xref="CDD:197360"
     Site            order(3268,3270,3328..3329,3331,3333,3387,3389..3391,3424)
                     /site_type="other"
                     /note="reelin repeat interface"
                     /db_xref="CDD:197360"
     Site            order(3287,3313..3314,3360,3362,3376)
                     /site_type="other"
                     /note="reelin subrepeat interface"
                     /db_xref="CDD:197360"
     Site            order(3321,3366..3367,3369)
                     /site_type="other"
                     /note="EGF domain interface"
                     /db_xref="CDD:197360"
     Region          3362..3373
                     /region_name="BNR 16"
                     /note="propagated from UniProtKB/Swiss-Prot (P78509.3)"
     Site            3411
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     Site            3438
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P78509.3)"
     CDS             1..3460
                     /gene="RELN"
                     /gene_synonym="ETL7; LIS2; PRO1598; RL"
                     /coded_by="NM_005045.4:303..10685"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS47680.1"
                     /db_xref="GeneID:5649"
                     /db_xref="HGNC:HGNC:9957"
                     /db_xref="MIM:600514"
ORIGIN      
        1 mersgwarqt fllalllgat lraraaagyy prfspffflc thhgelegdg eqgevlislh
       61 iagnptyyvp gqeyhvtist stffdgllvt glytstsvqa sqsiggssaf gfgimsdhqf
      121 gnqfmcsvva shvshlpttn lsfiwiappa gtgcvnfmat athrgqvifk dalaqqlceq
      181 gaptdvtvhp hlaeihsdsi ilrddfdsyh qlqlnpniwv ecnncetgeq cgaimhgnav
      241 tfcepygpre littglnttt asvlqfsigs gscrfsysdp siivlyaknn sadwiqleki
      301 rapsnvstii hilylpedak genvqfqwkq enlrvgevye acwaldnili insahrqvvl
      361 edsldpvdtg nwlffpgatv khscqsdgns iyfhgnegse fnfattrdvd lstediqeqw
      421 seefesqptg wdvlgavigt ecgtiesgls mvflkdgerk lctpsmdttg ygnlrfyfvm
      481 ggicdpgnsh endiilyaki egrkehitld tlsyssykvp slvsvvinpe lqtpatkfcl
      541 rqknhqghnr nvwavdffhv lpvlpstmsh miqfsinlgc gthqpgnsvs lefstnhgrs
      601 wsllhteclp eicagphlph stvyssenys gwnritiplp naaltrntri rwrqtgpilg
      661 nmwaidnvyi gpsclkfcsg rgqctrhgck cdpgfsgpac emasqtfpmf isesfgssrl
      721 ssyhnfysir gaevsfgcgv lasgkalvfn kdgrrqlits fldssqsrfl qftlrlgsks
      781 vlstcrapdq pgegvllhys ydngitwkll ehysylsyhe priisvelpg dakqfgiqfr
      841 wwqpyhssqr edvwaideii mtsvlfnsis ldftnlvevt qslgfylgnv qpycghdwtl
      901 cftgdsklas smryvetqsm qigasymiqf slvmgcgqky tphmdnqvkl eystnhgltw
      961 hlvqeeclps mpscqeftsa siyhaseftq wrrvivllpq ktwssatrfr wsqsyytaqd
     1021 ewaldsiyig qqcpnmcsgh gscdhgicrc dqgyqgtech peaalpstim sdfenqngwe
     1081 sdwqevigge ivkpeqgcgv issgsslyfs kagkrqlvsw dldtswvdfv qfyiqigges
     1141 ascnkpdsre egvllqysnn ggiqwhllae myfsdfskpr fvylelpaaa ktpctrfrww
     1201 qpvfsgedyd qwavddiiil sekqkqiipv inptlpqnfy ekpafdypmn qmsvwlmlan
     1261 egmvknetfc aatpsamifg ksdgdrfavt rdltlkpgyv lqfklnigca nqfsstapvl
     1321 lqyshdagms wflvkegcyp asagkgcegn srelseptmy htgdfeewtr itiviprsla
     1381 ssktrfrwiq esssqknvpp fgldgvyise pcpsycsghg dcisgvcfcd lgytaaqgtc
     1441 vsnvpnhnem fdrfegklsp lwykitgaqv gtgcgtlndg kslyfngpgk reartvpldt
     1501 rnirlvqfyi qigsktsgit cikprtrneg livqysndng ilwhllreld fmsflepqii
     1561 sidlpqdakt patafrwwqp qhgkhsaqwa lddvligmnd ssqtgfqdkf dgsidlqanw
     1621 yriqggqvdi dclsmdtali ftenigkpry aetwdfhvsa stflqfemsm gcskpfsnsh
     1681 svqlqyslnn gkdwhlvtee cvpptigclh ytessiytse rfqnwkritv ylplstispr
     1741 trfrwiqany tvgadswaid nvvlasgcpw mcsgrgicda grcvcdrgfg gpycvpvvpl
     1801 psilkddfng nlhpdlwpev ygaergnlng etiksgtsli fkgeglrmli srdldctntm
     1861 yvqfslrfia kstpershsi llqfsisggi twhlmdefyf pqttnilfin vplpytaqtn
     1921 atrfrlwqpy nngkkeeiwi vddfiidgnn vnnpvmlldt fdfgprednw ffypggnigl
     1981 ycpysskgap eedsamvfvs nevgehsitt rdlnvnenti iqfeinvgcs tdsssadpvr
     2041 lefsrdfgat whlllplcyh ssshvsslcs tehhpsstyy agtmqgwrre vvhfgklhlc
     2101 gsvrfrwyqg fypagsqpvt waidnvyigp qceemcngqg scingtkcic dpgysgptck
     2161 istknpdflk ddfegqlesd rfllmsggkp srkcgilssg nnlffnedgl rmlmtrdldl
     2221 sharfvqffm rlgcgkgvpd prsqpvllqy slngglswsl lqeflfsnss nvgryialei
     2281 plkarsgstr lrwwqpseng hfyspwvidq iliggnisgn tvleddfttl dsrkwllhpg
     2341 gtkmpvcgst gdalvfieka stryvvstdv avnedsflqi dfaascsvtd scyaieleys
     2401 vdlglswhpl vrdclptnve csryhlqril vsdtfnkwtr itlplppytr sqatrfrwhq
     2461 papfdkqqtw aidnvyigdg cidmcsghgr ciqgncvcde qwgglycddp etslptqlkd
     2521 nfnrapssqn wltvnggkls tvcgavasgm alhfsggcsr llvtvdlnlt naefiqfyfm
     2581 ygclitpnnr nqgvlleysv nggitwnllm eifydqyskp gfvnillppd akeiatrfrw
     2641 wqprhdgldq ndwaidnvli sgsadqrtvm ldtfssapvp qherspadag pvgriafdmf
     2701 medktsvneh wlfhddctve rfcdspdgvm lcgshdgrev yavthdltpt egwimqfkis
     2761 vgckvsekia qnqihvqyst dfgvswnylv pqclpadpkc sgsvsqpsvf fptkgwkrit
     2821 yplpeslvgn pvrfrfyqky sdmqwaidnf ylgpgcldnc rghgdclreq cicdpgysgp
     2881 ncylthtlkt flkerfdsee ikpdlwmsle ggstctecgi laedtalyfg gstvrqavtq
     2941 dldlrgakfl qywgrigsen nmtschrpic rkegvlldys tdggitwtll hemdyqkyis
     3001 vrhdyillpe daltnttrlr wwqpfvisng ivvsgveraq waldniligg aeinpsqlvd
     3061 tfddegtshe enwsfypnav rtagfcgnps fhlywpnkkk dkthnalssr eliiqpgymm
     3121 qfkivvgcea tscgdlhsvm leytkdarsd swqlvqtqcl psssnsigcs pfqfheatiy
     3181 nsvnssswkr itiqlpdhvs ssatqfrwiq kgeetekqsw aidhvyigea cpklcsghgy
     3241 cttgaicicd esfqgddcsv fshdlpsyik dnfesarvte anwetiqggv igsgcgqlap
     3301 yahgdslyfn gcqirqaatk pldltraski mfvlqigsms qtdscnsdls gphavdkavl
     3361 lqysvnngit whviaqhqpk dftqaqrvsy nvplearmkg vllrwwqprh ngtghdqwal
     3421 dhvevvlvst rkqnymmnfs rqhglrhfyn rrrrslrryp
//
LOCUS       NP_780569                378 aa            linear   ROD 27-APR-2025
DEFINITION  CST complex subunit STN1 [Mus musculus].
ACCESSION   NP_780569
VERSION     NP_780569.1
DBSOURCE    REFSEQ: accession NM_175360.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Nguyen,D.D., Kim,E., Le,N.T., Ding,X., Jaiswal,R.K., Kostlan,R.J.,
            Nguyen,T.N.T., Shiva,O., Le,M.T. and Chai,W.
  TITLE     Deficiency in mammalian STN1 promotes colon cancer development via
            inhibiting DNA repair
  JOURNAL   Sci Adv 9 (19), eadd8023 (2023)
   PUBMED   37163605
  REMARK    GeneRIF: Deficiency in mammalian STN1 promotes colon cancer
            development via inhibiting DNA repair.
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Miyake,Y., Nakamura,M., Nabetani,A., Shimamura,S., Tamura,M.,
            Yonehara,S., Saito,M. and Ishikawa,F.
  TITLE     RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded
            DNA and protects telomeres independently of the Pot1 pathway
  JOURNAL   Mol Cell 36 (2), 193-206 (2009)
   PUBMED   19854130
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Wan,M., Qin,J., Songyang,Z. and Liu,D.
  TITLE     OB fold-containing protein 1 (OBFC1), a human homolog of yeast
            Stn1, associates with TPP1 and is implicated in telomere length
            regulation
  JOURNAL   J Biol Chem 284 (39), 26725-26731 (2009)
   PUBMED   19648609
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Casteel,D.E., Zhuang,S., Zeng,Y., Perrino,F.W., Boss,G.R.,
            Goulian,M. and Pilz,R.B.
  TITLE     A DNA polymerase-{alpha}{middle dot}primase cofactor with homology
            to replication protein A-32 regulates DNA replication in mammalian
            cells
  JOURNAL   J Biol Chem 284 (9), 5807-5818 (2009)
   PUBMED   19119139
  REMARK    GeneRIF: OBFC1 is identical to the previously described 44 kDa
            subunit of DNA-pol-alpha/primase associated factor (AAF) which
            increases polymerase-alpha/primase template affinity and stimulate
            both DNA primase and polymerase-alpha activities in vitro.
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125075.4, AK075574.1 and AK164386.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK164386.1, AK146929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164139 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 39.64 cM"
     Protein         1..378
                     /product="CST complex subunit STN1"
                     /note="oligonucleotide/oligosaccharide-binding
                     fold-containing protein 1; alpha accessory factor 44;
                     replication protein A 32 kDa subunit; alpha-accessory
                     factor of 44 kDa; suppressor of cdc thirteen homolog;
                     oligonucleotide/oligosaccharide-binding fold containing 1"
                     /calculated_mol_wt=43355
     Region          8..195
                     /region_name="Interaction with CTC1.
                     /evidence=ECO:0000250|UniProtKB:Q9H668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2X3.2)"
     Region          65..165
                     /region_name="hOBFC1_like"
                     /note="A subfamily of OB folds similar to that found in
                     human OB fold containing protein 1 (hOBFC1). Members of
                     this group belong to the Replication protein A subunit 2
                     (RPA2) family of OB folds. RPA is a nuclear ssDNA binding
                     protein (SSB) which appears to be...; cd04483"
                     /db_xref="CDD:239929"
     Site            order(65,141,143,145,163)
                     /site_type="active"
                     /note="generic binding surface II [active]"
                     /db_xref="CDD:239929"
     Site            order(70..72,81..84,86,92..94,96,140,147..149,156..158)
                     /site_type="active"
                     /note="generic binding surface I [active]"
                     /db_xref="CDD:239929"
     Region          201..305
                     /region_name="Winged helix-turn-helix (wHTH) 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2X3.2)"
     Region          212..378
                     /region_name="STN1_2"
                     /note="CST, complex subunit STN1, C terminal; pfam09170"
                     /db_xref="CDD:462701"
     Region          306..378
                     /region_name="Winged helix-turn-helix (wHTH) 2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2X3.2)"
     CDS             1..378
                     /gene="Stn1"
                     /gene_synonym="0610009H20Rik; 2310057J23Rik; AAF-44;
                     AAF44; Obfc1; RPA-32"
                     /coded_by="NM_175360.3:329..1465"
                     /db_xref="CCDS:CCDS29892.1"
                     /db_xref="GeneID:108689"
                     /db_xref="MGI:MGI:1915581"
ORIGIN      
        1 mpqpcllmec esspreeeip plfwgldpvf lafaklyikd ilemkesqqv pgtyfynghp
       61 irrvdimgav isvkeretfy sygvddatgv incvcwkkls naesssdpai lstarelsmt
      121 sqlkklqeti eqktrigigd iirvrgsvrm freereican iyykvddpvw nmqiarmlel
      181 pklyqkvydq pfrnpalqee ealnnkdnld lagltsllse kikeflqekk mqsfyqqele
      241 tveslqslas rpvthstgsd qvelkdsgts gvaqrvfkna lqllqekglv fqrdsgsdkl
      301 yyvttkdkdl qqkiyhiike dcqkpnhmek gchllhilnc vhlnlrwdls kavlqrvlel
      361 ledqsdivst adhyyaaf
//
LOCUS       NP_001355101             210 aa            linear   PRI 27-APR-2025
DEFINITION  D-aspartate oxidase isoform e [Homo sapiens].
ACCESSION   NP_001355101
VERSION     NP_001355101.1
DBSOURCE    REFSEQ: accession NM_001368172.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Rabattoni,V., Motta,Z., Miceli,M., Molla,G., Fissore,A.,
            Adinolfi,S., Pollegioni,L. and Sacchi,S.
  TITLE     On the regulation of human D-aspartate oxidase
  JOURNAL   Protein Sci 32 (11), e4802 (2023)
   PUBMED   37805834
  REMARK    GeneRIF: On the regulation of human D-aspartate oxidase.
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Lombardo,B., Pagani,M., De Rosa,A., Nunziato,M., Migliarini,S.,
            Garofalo,M., Terrile,M., D'Argenio,V., Galbusera,A., Nuzzo,T.,
            Ranieri,A., Vitale,A., Leggiero,E., Di Maio,A., Barsotti,N.,
            Borello,U., Napolitano,F., Mandarino,A., Carotenuto,M.,
            Heresco-Levy,U., Pasqualetti,M., Malatesta,P., Gozzi,A., Errico,F.,
            Salvatore,F., Pastore,L. and Usiello,A.
  TITLE     D-aspartate oxidase gene duplication induces social recognition
            memory deficit in mice and intellectual disabilities in humans
  JOURNAL   Transl Psychiatry 12 (1), 305 (2022)
   PUBMED   35915065
  REMARK    GeneRIF: D-aspartate oxidase gene duplication induces social
            recognition memory deficit in mice and intellectual disabilities in
            humans.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Chen,A.S., Liu,H., Wu,Y., Luo,S., Patz,E.F. Jr., Glass,C., Su,L.,
            Du,M., Christiani,D.C. and Wei,Q.
  TITLE     Genetic variants in DDO and PEX5L in peroxisome-related pathways
            predict non-small cell lung cancer survival
  JOURNAL   Mol Carcinog 61 (7), 619-628 (2022)
   PUBMED   35502931
  REMARK    GeneRIF: Genetic variants in DDO and PEX5L in peroxisome-related
            pathways predict non-small cell lung cancer survival.
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Rabattoni,V., Pollegioni,L., Tedeschi,G., Maffioli,E. and Sacchi,S.
  TITLE     Cellular studies of the two main isoforms of human d-aspartate
            oxidase
  JOURNAL   FEBS J 288 (16), 4939-4954 (2021)
   PUBMED   33650155
  REMARK    GeneRIF: Cellular studies of the two main isoforms of human
            d-aspartate oxidase.
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Molla,G., Chaves-Sanjuan,A., Savinelli,A., Nardini,M. and
            Pollegioni,L.
  TITLE     Structure and kinetic properties of human d-aspartate oxidase, the
            enzyme-controlling d-aspartate levels in brain
  JOURNAL   FASEB J 34 (1), 1182-1197 (2020)
   PUBMED   31914658
  REMARK    GeneRIF: three-dimensional structural analysis contributes insights
            into the structure-function relationships of human DASPO
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Setoyama,C. and Miura,R.
  TITLE     Structural and functional characterization of the human brain
            D-aspartate oxidase
  JOURNAL   J Biochem 121 (4), 798-803 (1997)
   PUBMED   9163533
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Simonic,T., Duga,S., Negri,A., Tedeschi,G., Malcovati,M.,
            Tenchini,M.L. and Ronchi,S.
  TITLE     cDNA cloning and expression of the flavoprotein D-aspartate oxidase
            from bovine kidney cortex
  JOURNAL   Biochem J 322 (Pt 3) (Pt 3), 729-735 (1997)
   PUBMED   9148742
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Nagasaki,H.
  TITLE     Gender-related differences of mouse liver D-aspartate oxidase in
            the activity and response to administration of D-aspartate and
            peroxisome proliferators
  JOURNAL   Int J Biochem 26 (3), 415-423 (1994)
   PUBMED   8187937
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Van Veldhoven,P.P., Brees,C. and Mannaerts,G.P.
  TITLE     D-aspartate oxidase, a peroxisomal enzyme in liver of rat and man
  JOURNAL   Biochim Biophys Acta 1073 (1), 203-208 (1991)
   PUBMED   1991137
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Barker,R.F. and Hopkinson,D.A.
  TITLE     The genetic and biochemical properties of the D-amino acid oxidases
            in human tissues
  JOURNAL   Ann Hum Genet 41 (1), 27-42 (1977)
   PUBMED   21608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL050350.14.
            
            Summary: The protein encoded by this gene is a peroxisomal
            flavoprotein that catalyzes the oxidative deamination of
            D-aspartate and N-methyl D-aspartate. Flavin adenine dinucleotide
            or 6-hydroxyflavin adenine dinucleotide can serve as the cofactor
            in this reaction. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jan
            2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138525.429297.1,
                                           SRR5189664.107882.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..210
                     /product="D-aspartate oxidase isoform e"
                     /EC_number="1.4.3.1"
                     /note="aspartic oxidase; D-aspartate oxidase, DDO"
                     /calculated_mol_wt=23265
     Region          5..>192
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
     CDS             1..210
                     /gene="DDO"
                     /gene_synonym="DASOX; DASPO; DDO-1; DDO-2"
                     /coded_by="NM_001368172.1:114..746"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:8528"
                     /db_xref="HGNC:HGNC:2727"
                     /db_xref="MIM:124450"
ORIGIN      
        1 mdtariavvg agvvglstav cisklvprcs vtiisdkftp dttsdvaagm liphtypdtp
       61 ihtqkqwfre tfnhlfaian saeagdagvh lvsgwqifqs tpteevpfwa dvvlgfrkmt
      121 eaelkkfpqy vfgqafttlk cecpaylpwl ekrikgsggw tltrriedlw elhpsfdivv
      181 ncsglgsrql agdskifpni fyfflnmknn
//
LOCUS       NP_001349777             411 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-N-acetylgalactosaminidase precursor [Homo sapiens].
ACCESSION   NP_001349777 XP_005261672
VERSION     NP_001349777.1
DBSOURCE    REFSEQ: accession NM_001362848.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Yilmaz,S. and Oner,P.
  TITLE     Could low alpha-N-acetylgalactosaminidase plasma concentration
            cause schizophrenia?
  JOURNAL   World J Biol Psychiatry 24 (1), 70-77 (2023)
   PUBMED   35521802
  REMARK    GeneRIF: Could low alpha-N-acetylgalactosaminidase plasma
            concentration cause schizophrenia?
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Jafari,M., Rahimi,N., Jami,M.S., Hashemzadeh Chaleshtori,M.,
            Elahian,F. and Mirzaei,S.A.
  TITLE     Silencing of alpha-N-acetylgalactosaminidase in the gastric cancer
            cells amplified cell death and attenuated migration, while the
            multidrug resistance remained unchanged
  JOURNAL   Cell Biol Int 46 (2), 255-264 (2022)
   PUBMED   34816536
  REMARK    GeneRIF: Silencing of alpha-N-acetylgalactosaminidase in the
            gastric cancer cells amplified cell death and attenuated migration,
            while the multidrug resistance remained unchanged.
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Li,Y., Ma,C., Li,W., Yang,Y., Li,X., Liu,J., Wang,J., Li,S.,
            Liu,Y., Li,K., Li,J., Huang,D., Chen,R., Lv,L., Li,M. and Luo,X.J.
  TITLE     A missense variant in NDUFA6 confers schizophrenia risk by
            affecting YY1 binding and NAGA expression
  JOURNAL   Mol Psychiatry 26 (11), 6896-6911 (2021)
   PUBMED   33931730
  REMARK    GeneRIF: A missense variant in NDUFA6 confers schizophrenia risk by
            affecting YY1 binding and NAGA expression.
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Mohamed,F.E., Al Sorkhy,M., Ghattas,M.A., Al-Zaabi,N.,
            Al-Shamsi,A., Almansoori,T.M., Al-Gazali,L., Al-Dirbashi,O.Y.,
            Al-Jasmi,F. and Ali,B.R.
  TITLE     A Novel Homozygous Missense Variant in the NAGA Gene with Extreme
            Intrafamilial Phenotypic Heterogeneity
  JOURNAL   J Mol Neurosci 70 (1), 45-55 (2020)
   PUBMED   31468281
  REMARK    GeneRIF: A Novel Homozygous Missense Variant in the NAGA Gene with
            Extreme Intrafamilial Phenotypic Heterogeneity.
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Meshach Paul,D. and Rajasekaran,R.
  TITLE     Exploration of Structural and Functional Variations Owing to Point
            Mutations in alpha-NAGA
  JOURNAL   Interdiscip Sci 10 (1), 81-92 (2018)
   PUBMED   27138754
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Wang,A.M. and Desnick,R.J.
  TITLE     Structural organization and complete sequence of the human
            alpha-N-acetylgalactosaminidase gene: homology with the
            alpha-galactosidase A gene provides evidence for evolution from a
            common ancestral gene
  JOURNAL   Genomics 10 (1), 133-142 (1991)
   PUBMED   1646157
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Wang,A.M., Bishop,D.F. and Desnick,R.J.
  TITLE     Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide
            sequence, and expression of a full-length cDNA. Homology with human
            alpha-galactosidase A suggests evolution from a common ancestral
            gene
  JOURNAL   J Biol Chem 265 (35), 21859-21866 (1990)
   PUBMED   2174888
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Warner,T.G., Louie,A. and Potier,M.
  TITLE     Photolabeling of the alpha-neuraminidase/beta-galactosidase complex
            from human placenta with a photoreactive neuraminidase inhibitor
  JOURNAL   Biochem Biophys Res Commun 173 (1), 13-19 (1990)
   PUBMED   2256909
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Wang,A.M., Schindler,D. and Desnick,R.
  TITLE     Schindler disease: the molecular lesion in the
            alpha-N-acetylgalactosaminidase gene that causes an infantile
            neuroaxonal dystrophy
  JOURNAL   J Clin Invest 86 (5), 1752-1756 (1990)
   PUBMED   2243144
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Cantz,M. and Ulrich-Bott,B.
  TITLE     Disorders of glycoprotein degradation
  JOURNAL   J Inherit Metab Dis 13 (4), 523-537 (1990)
   PUBMED   2122119
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z99716.4.
            
            On May 1, 2018 this sequence version replaced XP_005261672.1.
            
            Summary: NAGA encodes the lysosomal enzyme
            alpha-N-acetylgalactosaminidase, which cleaves
            alpha-N-acetylgalactosaminyl moieties from glycoconjugates.
            Mutations in NAGA have been identified as the cause of  Schindler
            disease types I and II (type II also known as Kanzaki disease).
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1-3 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.22263.1,
                                           SRR11853567.20142.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..411
                     /product="alpha-N-acetylgalactosaminidase precursor"
                     /EC_number="3.2.1.49"
                     /note="Acetylgalactosaminidase, alpha-N-
                     (alpha-galactosidase B); N-acetylgalactosaminidase,
                     alpha-"
                     /calculated_mol_wt=44703
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1879
     mat_peptide     18..411
                     /product="Alpha-N-acetylgalactosaminidase.
                     /id=PRO_0000001018"
                     /note="propagated from UniProtKB/Swiss-Prot (P17050.2)"
                     /calculated_mol_wt=44703
     Region          25..308
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(33,78..79,119,154,156,188,213,217)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19683538; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19683538; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Site            201
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Region          311..394
                     /region_name="Melibiase_2_C"
                     /note="Alpha galactosidase A C-terminal beta sandwich
                     domain; pfam17450"
                     /db_xref="CDD:407508"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Site            359
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     Site            385
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19683538; propagated from
                     UniProtKB/Swiss-Prot (P17050.2)"
     CDS             1..411
                     /gene="NAGA"
                     /gene_synonym="D22S674; GALB"
                     /coded_by="NM_001362848.1:157..1392"
                     /db_xref="CCDS:CCDS14030.1"
                     /db_xref="GeneID:4668"
                     /db_xref="HGNC:HGNC:7631"
                     /db_xref="MIM:104170"
ORIGIN      
        1 mllktvlllg hvaqvlmldn gllqtppmgw lawerfrcni ncdedpknci seqlfmemad
       61 rmaqdgwrdm gytylniddc wiggrdasgr lmpdpkrfph gipfladyvh slglklgiya
      121 dmgnftcmgy pgttldkvvq daqtfaewkv dmlkldgcfs tpeeraqgyp kmaaalnatg
      181 rpiafscswp ayegglpprv nyslladicn lwrnyddiqd swwsvlsiln wfvehqdilq
      241 pvagpghwnd pdmllignfg lsleqsraqm alwtvlaapl lmstdlrtis aqnmdilqnp
      301 lmikinqdpl giqgrrihke kslievymrp lsnkasalvf fscrtdmpyr yhsslgqlnf
      361 tgsviyeaqd vysgdiisgl rdetnftvii npsgvvmwyl ypiknlemsq q
//
LOCUS       NP_001353547             467 aa            linear   PRI 27-APR-2025
DEFINITION  regulator of G-protein signaling 14 isoform 3 [Homo sapiens].
ACCESSION   NP_001353547 XP_005265852
VERSION     NP_001353547.1
DBSOURCE    REFSEQ: accession NM_001366618.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Sneddon,W.B., Ramineni,S., Van Doorn,G.E., Hepler,J.R. and
            Friedman,P.A.
  TITLE     Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport
  JOURNAL   Biochem Biophys Res Commun 733, 150700 (2024)
   PUBMED   39293332
  REMARK    GeneRIF: Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport.
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Wang,J., Guo,Y., He,Y., Qin,Y., Li,X., Yang,L., Liu,K. and Xiao,L.
  TITLE     Hepatic regulator of G protein signaling 14 ameliorates NAFLD
            through activating cAMP-AMPK signaling by targeting Gialpha1/3
  JOURNAL   Mol Metab 80, 101882 (2024)
   PUBMED   38237897
  REMARK    GeneRIF: Hepatic regulator of G protein signaling 14 ameliorates
            NAFLD through activating cAMP-AMPK signaling by targeting
            Gialpha1/3.
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Montanez-Miranda,C., Bramlett,S.N. and Hepler,J.R.
  TITLE     RGS14 expression in CA2 hippocampus, amygdala, and basal ganglia:
            Implications for human brain physiology and disease
  JOURNAL   Hippocampus 33 (3), 166-181 (2023)
   PUBMED   36541898
  REMARK    GeneRIF: RGS14 expression in CA2 hippocampus, amygdala, and basal
            ganglia: Implications for human brain physiology and disease.
            Review article
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Friedman,P.A., Sneddon,W.B., Mamonova,T., Montanez-Miranda,C.,
            Ramineni,S., Harbin,N.H., Squires,K.E., Gefter,J.V., Magyar,C.E.,
            Emlet,D.R. and Hepler,J.R.
  TITLE     RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated renal
            phosphate uptake via binding to the NHERF1 scaffolding protein
  JOURNAL   J Biol Chem 298 (5), 101836 (2022)
   PUBMED   35307350
  REMARK    GeneRIF: RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated
            renal phosphate uptake via binding to the NHERF1 scaffolding
            protein.
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Sierra,D.A., Gilbert,D.J., Householder,D., Grishin,N.V., Yu,K.,
            Ukidwe,P., Barker,S.A., He,W., Wensel,T.G., Otero,G., Brown,G.,
            Copeland,N.G., Jenkins,N.A. and Wilkie,T.M.
  TITLE     Evolution of the regulators of G-protein signaling multigene family
            in mouse and human
  JOURNAL   Genomics 79 (2), 177-185 (2002)
   PUBMED   11829488
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Kimple,R.J., De Vries,L., Tronchere,H., Behe,C.I., Morris,R.A.,
            Gist Farquhar,M. and Siderovski,D.P.
  TITLE     RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with
            guanine nucleotide dissociation inhibitor Activity
  JOURNAL   J Biol Chem 276 (31), 29275-29281 (2001)
   PUBMED   11387333
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Cho,H., Kozasa,T., Takekoshi,K., De Gunzburg,J. and Kehrl,J.H.
  TITLE     RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha-
            and G13alpha-mediated signaling pathways
  JOURNAL   Mol Pharmacol 58 (3), 569-576 (2000)
   PUBMED   10953050
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Traver,S., Bidot,C., Spassky,N., Baltauss,T., De Tand,M.F.,
            Thomas,J.L., Zalc,B., Janoueix-Lerosey,I. and Gunzburg,J.D.
  TITLE     RGS14 is a novel Rap effector that preferentially regulates the
            GTPase activity of galphao
  JOURNAL   Biochem J 350 Pt 1 (Pt 1), 19-29 (2000)
   PUBMED   10926822
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Snow,B.E., Antonio,L., Suggs,S., Gutstein,H.B. and Siderovski,D.P.
  TITLE     Molecular cloning and expression analysis of rat Rgs12 and Rgs14
  JOURNAL   Biochem Biophys Res Commun 233 (3), 770-777 (1997)
   PUBMED   9168931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC146507.2.
            
            On Oct 13, 2018 this sequence version replaced XP_005265852.1.
            
            Summary: This gene encodes a member of the regulator of G-protein
            signaling family. This protein contains one RGS domain, two
            Raf-like Ras-binding domains (RBDs), and one GoLoco domain. The
            protein attenuates the signaling activity of G-proteins by binding,
            through its GoLoco domain, to specific types of activated,
            GTP-bound G alpha subunits. Acting as a GTPase activating protein
            (GAP), the protein increases the rate of conversion of the GTP to
            GDP. This hydrolysis allows the G alpha subunits to bind G
            beta/gamma subunit heterodimers, forming inactive G-protein
            heterotrimers, thereby terminating the signal. Alternate
            transcriptional splice variants of this gene have been observed but
            have not been thoroughly characterized. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.154317.1,
                                           SRR1803616.211548.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..467
                     /product="regulator of G-protein signaling 14 isoform 3"
                     /calculated_mol_wt=51117
     Region          19..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Region          58..186
                     /region_name="RGS_RGS14"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS14 protein; cd08743"
                     /db_xref="CDD:188697"
     Site            order(88..90,92..93,130..135,137..138,165,167..169,173)
                     /site_type="other"
                     /note="putative G-alpha-3 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:188697"
     Region          192..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97492; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Region          302..372
                     /region_name="RBD1_RGS14"
                     /note="Ras-binding domain (RBD) 1 of regulator of G
                     protein signaling 14 (RGS14); cd17137"
                     /db_xref="CDD:340657"
     Site            order(334,352)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340657"
     Region          373..444
                     /region_name="RBD2_RGS14"
                     /note="Ras-binding domain (RBD) 2 of regulator of G
                     protein signaling 14 (RGS14); cd17139"
                     /db_xref="CDD:340659"
     Site            order(385,407)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340659"
     CDS             1..467
                     /gene="RGS14"
                     /coded_by="NM_001366618.1:102..1505"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:10636"
                     /db_xref="HGNC:HGNC:9996"
                     /db_xref="MIM:602513"
ORIGIN      
        1 mpgkpkhlgv pngrmvlavs dgelssttgp qgqgegrgss lsihslpsgp sspfpteeqp
       61 vaswalsfer llqdplglay fteflkkefs aenvtfwkac erfqqipasd tqqlaqearn
      121 iyqeflssqa lspvnidrqa wlgeevlaep rpdmfraqql qifnlmkfds yarfvksply
      181 recllaeaeg rplrepgssr lgspdatrkk pklkpgkslp lgveelgqlp pvegpggrpl
      241 rksfrrelgg tanaalrres qgslnssasl dlgflafvss kseshrkslg stegesesrp
      301 gkyccvylpd gtaslalarp gltirdmlag icekrglslp dikvylvgne qkalvldqdc
      361 tvladqevrl enritfelel talervvris akptkrlqea lqpilekhgl splevvlhrp
      421 gekqpldlgk lvssvaaqrl vldtlpgvki skardkspcr sqawwsc
//
LOCUS       NP_004164                635 aa            linear   PRI 27-APR-2025
DEFINITION  cationic amino acid transporter 4 [Homo sapiens].
ACCESSION   NP_004164
VERSION     NP_004164.2
DBSOURCE    REFSEQ: accession NM_004173.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Proitsi,P., Lupton,M.K., Reeves,S.J., Hamilton,G., Archer,N.,
            Martin,B.M., Iyegbe,C., Hollingworth,P., Lawlor,B., Gill,M.,
            Brayne,C., Rubinsztein,D.C., Owen,M.J., Williams,J., Lovestone,S.
            and Powell,J.F.
  TITLE     Association of serotonin and dopamine gene pathways with behavioral
            subphenotypes in dementia
  JOURNAL   Neurobiol Aging 33 (4), 791-803 (2012)
   PUBMED   20685009
  REMARK    GeneRIF: Observational study of gene-disease association, gene-gene
            interaction, gene-environment interaction, and pharmacogenomic /
            toxicogenomic. (HuGE Navigator)
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Gudayol-Ferre,E., Herrera-Guzman,I., Camarena,B.,
            Cortes-Penagos,C., Herrera-Abarca,J.E., Martinez-Medina,P.,
            Cruz,D., Hernandez,S., Genis,A., Carrillo-Guerrero,M.Y., Aviles
            Reyes,R. and Guardia-Olmos,J.
  TITLE     The role of clinical variables, neuropsychological performance and
            SLC6A4 and COMT gene polymorphisms on the prediction of early
            response to fluoxetine in major depressive disorder
  JOURNAL   J Affect Disord 127 (1-3), 343-351 (2010)
   PUBMED   20584552
  REMARK    GeneRIF: Clinical trial of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Kohlrausch,F.B., Salatino-Oliveira,A., Gama,C.S., Lobato,M.I.,
            Belmonte-de-Abreu,P. and Hutz,M.H.
  TITLE     Influence of serotonin transporter gene polymorphisms on clozapine
            response in Brazilian schizophrenics
  JOURNAL   J Psychiatr Res 44 (16), 1158-1162 (2010)
   PUBMED   20452607
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   4  (residues 1 to 635)
  AUTHORS   Kikuchi,A., Nakamura,N., Kuze,T., Sasaki,Y., Abe,M., Ohno,H.,
            Akasaka,T., Nakamura,S., Ohshima,K. and Ando,K.
  TITLE     Characterization of de novo diffuse large B-cell lymphoma with a
            translocation of c-myc and immunoglobulin genes
  JOURNAL   Leuk Res 32 (8), 1176-1182 (2008)
   PUBMED   18460403
  REMARK    GeneRIF: These results suggest a heterogeneous immunophenotype and
            genotype for c-myc/Ig DLBCL, with CD10(-)/BCL6(+)/MUM1(-) cases the
            most frequent.
REFERENCE   5  (residues 1 to 635)
  AUTHORS   Munoz,L., Lasa,A., Carricondo,M.T., Hernandez,C., Ubeda,J. and
            Nomdedeu,J.F.
  TITLE     Comparative analysis of ZAP-70 expression and Ig VH mutational
            status in B-cell chronic lymphocytic leukemia
  JOURNAL   Cytometry B Clin Cytom 72 (2), 96-102 (2007)
   PUBMED   17051526
  REMARK    GeneRIF: ZAP-70 reactivity using a T-cell marker as a control
            allows to identify the majority of patients with an unmutated Ig VH
            genotype.
REFERENCE   6  (residues 1 to 635)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   7  (residues 1 to 635)
  AUTHORS   Hammermann,R., Brunn,G. and Racke,K.
  TITLE     Analysis of the genomic organization of the human cationic amino
            acid transporters CAT-1, CAT-2 and CAT-4
  JOURNAL   Amino Acids 21 (2), 211-219 (2001)
   PUBMED   11665818
  REMARK    GeneRIF: analysis of the genomic organization
REFERENCE   8  (residues 1 to 635)
  AUTHORS   Fischer,M. and Kuppers,R.
  TITLE     Human IgA- and IgM-secreting intestinal plasma cells carry heavily
            mutated VH region genes
  JOURNAL   Eur J Immunol 28 (9), 2971-2977 (1998)
   PUBMED   9754584
REFERENCE   9  (residues 1 to 635)
  AUTHORS   Sperandeo,M.P., Borsani,G., Incerti,B., Zollo,M., Rossi,E.,
            Zuffardi,O., Castaldo,P., Taglialatela,M., Andria,G. and
            Sebastio,G.
  TITLE     The gene encoding a cationic amino acid transporter (SLC7A4) maps
            to the region deleted in the velocardiofacial syndrome
  JOURNAL   Genomics 49 (2), 230-236 (1998)
   PUBMED   9598310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002472.8, BC008814.2 and BC062565.1.
            
            On Jul 14, 2006 this sequence version replaced NP_004164.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008814.2, SRR11853560.19345.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382932.3/ ENSP00000372390.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..635
                     /product="cationic amino acid transporter 4"
                     /note="solute carrier family 7 (cationic amino acid
                     transporter, y+ system), member 4; Ig heavy chain variable
                     region; VH 3 family; solute carrier family 7 (orphan
                     transporter), member 4"
                     /calculated_mol_wt=68137
     Region          26..592
                     /region_name="2A0303"
                     /note="cationic amino acid transport permease; TIGR00906"
                     /db_xref="CDD:273330"
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            66..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43246.3)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43246.3)"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            221
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43246.3)"
     Site            229..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            270..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            365..385
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            391..411
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLQ7; propagated from
                     UniProtKB/Swiss-Prot (O43246.3)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLQ7; propagated from
                     UniProtKB/Swiss-Prot (O43246.3)"
     Site            478..498
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            500
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43246.3)"
     Site            508..528
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            539..559
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            567..587
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43246.3)"
     Site            601
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43246.3)"
     CDS             1..635
                     /gene="SLC7A4"
                     /gene_synonym="CAT-4; CAT4; HCAT3; VH"
                     /coded_by="NM_004173.3:72..1979"
                     /db_xref="CCDS:CCDS33608.1"
                     /db_xref="GeneID:6545"
                     /db_xref="HGNC:HGNC:11062"
                     /db_xref="MIM:603752"
ORIGIN      
        1 marglptias larlcqklnr lkpledstme tslrrclstl dltllgvggm vgsglyvltg
       61 avakevagpa vllsfgvaav asllaalcya efgarvprtg saylftyvsm gelwafligw
      121 nvlleyiigg aavarawsgy ldsmfshsir nftethvgsw qvpllghypd flaagiilla
      181 safvscgarv sswlnhtfsa isllvilfiv ilgfilaqph nwsadeggfa pfgfsgvmag
      241 tascfyafvg fdviaassee aqnprrsvpl aiaislaiaa gayilvstvl tlmvpwhsld
      301 pdsaladafy qrgyrwagfi vaagsicamn tvllsllfsl privyamaad glffqvfahv
      361 hprtqvpvag tlafglltaf lallldlesl vqflslgtll aytfvatsii vlrfqksspp
      421 sspgpaspgp ltkqqssfsd hlqlvgtvha svpepgelkp alrpylgfld gyspgavvtw
      481 algvmlasai tigcvlvfgn stlhlphwgy illllltsvm fllsllvlga hqqqyredlf
      541 qipmvplipa lsivlniclm lklsyltwvr fsiwllmgla vyfgygirhs kenqrelpgl
      601 nsthyvvfpr gsleetvqam qppsqapaqd pghme
//
LOCUS       NP_001035927             188 aa            linear   PRI 27-APR-2025
DEFINITION  trafficking protein particle complex subunit 5 [Homo sapiens].
ACCESSION   NP_001035927
VERSION     NP_001035927.1
DBSOURCE    REFSEQ: accession NM_001042462.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Kim,J.J., Lipatova,Z. and Segev,N.
  TITLE     TRAPP Complexes in Secretion and Autophagy
  JOURNAL   Front Cell Dev Biol 4, 20 (2016)
   PUBMED   27066478
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Scrivens,P.J., Noueihed,B., Shahrzad,N., Hul,S., Brunet,S. and
            Sacher,M.
  TITLE     C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
            early stage in ER-to-Golgi trafficking
  JOURNAL   Mol Biol Cell 22 (12), 2083-2093 (2011)
   PUBMED   21525244
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM841051.1, BU736689.1 and AC008763.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1-3 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB155196.1, SRR1803617.155745.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000596148.3/ ENSP00000470262.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..188
                     /product="trafficking protein particle complex subunit 5"
                     /note="trafficking protein particle complex 5"
                     /calculated_mol_wt=20652
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IUR0.1)"
     Region          24..175
                     /region_name="TRAPPC5_Trs31"
                     /note="Trs31 subunit of the TRAPP complex; cd14943"
                     /db_xref="CDD:271346"
     Site            order(24..29,31..32,34..35,39,53,57,61,64..65,68,95..96,
                     98..99,142)
                     /site_type="other"
                     /note="BET3 interface [polypeptide binding]"
                     /db_xref="CDD:271346"
     Site            order(64,66..67,70,76..80,153,156)
                     /site_type="other"
                     /note="sedlin interface [polypeptide binding]"
                     /db_xref="CDD:271346"
     CDS             1..188
                     /gene="TRAPPC5"
                     /gene_synonym="TRS31"
                     /coded_by="NM_001042462.2:59..625"
                     /db_xref="CCDS:CCDS42490.1"
                     /db_xref="GeneID:126003"
                     /db_xref="HGNC:HGNC:23067"
ORIGIN      
        1 mearftrgks alleralarp rtevslsafa llfselvqhc qsrvfsvael qsrlaalgrq
       61 vgarvldalv arekgarret kvlgallfvk gavwkalfgk eadkleqand dartfyiier
      121 eplintyisv pkenstlnca sftagiveav lthsgfpakv tahwhkgttl mikfeeavia
      181 rdralegr
//
LOCUS       NP_079406                917 aa            linear   PRI 27-APR-2025
DEFINITION  hexokinase HKDC1 [Homo sapiens].
ACCESSION   NP_079406
VERSION     NP_079406.4
DBSOURCE    REFSEQ: accession NM_025130.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Pang,Q., Huang,S., Wang,H. and Cao,J.
  TITLE     HKDC1 promotes autophagy and proliferation in pancreatic
            adenocarcinoma through interaction with PARP1 and
            poly(ADP-ribosyl)ation
  JOURNAL   Cell Signal 124, 111474 (2024)
   PUBMED   39424110
  REMARK    GeneRIF: HKDC1 promotes autophagy and proliferation in pancreatic
            adenocarcinoma through interaction with PARP1 and
            poly(ADP-ribosyl)ation.
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Shi,F., Jiang,J., Wang,B., Hong,L., Zhang,Y., Meng,Y., Zhang,X.,
            Gong,L., Lin,J. and Diao,H.
  TITLE     Hepatitis B virus X protein promotes tumor glycolysis by
            downregulating lncRNA OIP5-AS1/HKDC1 in HCC
  JOURNAL   Cell Signal 119, 111183 (2024)
   PUBMED   38636768
  REMARK    GeneRIF: Hepatitis B virus X protein promotes tumor glycolysis by
            downregulating lncRNA OIP5-AS1/HKDC1 in HCC.
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Chen,H.Y., Li,X.N., Yang,L., Ye,C.X., Chen,Z.L. and Wang,Z.J.
  TITLE     CircVMP1 promotes glycolysis and disease progression by
            upregulating HKDC1 in colorectal cancer
  JOURNAL   Environ Toxicol 39 (3), 1617-1630 (2024)
   PUBMED   38009649
  REMARK    GeneRIF: CircVMP1 promotes glycolysis and disease progression by
            upregulating HKDC1 in colorectal cancer.
REFERENCE   4  (residues 1 to 917)
  AUTHORS   Zhang,Y., Wang,M., Ye,L., Shen,S., Zhang,Y., Qian,X., Zhang,T.,
            Yuan,M., Ye,Z., Cai,J., Meng,X., Qiu,S., Liu,S., Liu,R., Jia,W.,
            Yang,X., Zhang,H., Zhong,X. and Gao,P.
  TITLE     HKDC1 promotes tumor immune evasion in hepatocellular carcinoma by
            coupling cytoskeleton to STAT1 activation and PD-L1 expression
  JOURNAL   Nat Commun 15 (1), 1314 (2024)
   PUBMED   38351096
  REMARK    GeneRIF: HKDC1 promotes tumor immune evasion in hepatocellular
            carcinoma by coupling cytoskeleton to STAT1 activation and PD-L1
            expression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 917)
  AUTHORS   Hu,J., Xia,F., Chen,C. and Zhao,D.
  TITLE     HKDC1 in Gastric Cancer: A New Diagnostic, Prognostic Biomarker,
            and Novel Therapeutic Target
  JOURNAL   Ann Clin Lab Sci 53 (5), 726-737 (2023)
   PUBMED   37945018
  REMARK    GeneRIF: HKDC1 in Gastric Cancer: A New Diagnostic, Prognostic
            Biomarker, and Novel Therapeutic Target.
REFERENCE   6  (residues 1 to 917)
  AUTHORS   Guo,C., Ludvik,A.E., Arlotto,M.E., Hayes,M.G., Armstrong,L.L.,
            Scholtens,D.M., Brown,C.D., Newgard,C.B., Becker,T.C., Layden,B.T.,
            Lowe,W.L. and Reddy,T.E.
  TITLE     Coordinated regulatory variation associated with gestational
            hyperglycaemia regulates expression of the novel hexokinase HKDC1
  JOURNAL   Nat Commun 6, 6069 (2015)
   PUBMED   25648650
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 917)
  AUTHORS   Hayes,M.G., Urbanek,M., Hivert,M.F., Armstrong,L.L., Morrison,J.,
            Guo,C., Lowe,L.P., Scheftner,D.A., Pluzhnikov,A., Levine,D.M.,
            McHugh,C.P., Ackerman,C.M., Bouchard,L., Brisson,D., Layden,B.T.,
            Mirel,D., Doheny,K.F., Leya,M.V., Lown-Hecht,R.N., Dyer,A.R.,
            Metzger,B.E., Reddy,T.E., Cox,N.J. and Lowe,W.L. Jr.
  CONSRTM   HAPO Study Cooperative Research Group
  TITLE     Identification of HKDC1 and BACE2 as genes influencing glycemic
            traits during pregnancy through genome-wide association studies
  JOURNAL   Diabetes 62 (9), 3282-3291 (2013)
   PUBMED   23903356
  REMARK    GeneRIF: Data identified two novel genome-wide significant
            associations: 2-h plasma glucose and HKDC1, and fasting C-peptide
            and BACE2.
            Erratum:[Diabetes. 2013 Oct;62(10):3641]
REFERENCE   8  (residues 1 to 917)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 917)
  AUTHORS   Neale,B.M., Medland,S., Ripke,S., Anney,R.J., Asherson,P.,
            Buitelaar,J., Franke,B., Gill,M., Kent,L., Holmans,P.,
            Middleton,F., Thapar,A., Lesch,K.P., Faraone,S.V., Daly,M.,
            Nguyen,T.T., Schafer,H., Steinhausen,H.C., Reif,A., Renner,T.J.,
            Romanos,M., Romanos,J., Warnke,A., Walitza,S., Freitag,C.,
            Meyer,J., Palmason,H., Rothenberger,A., Hawi,Z., Sergeant,J.,
            Roeyers,H., Mick,E. and Biederman,J.
  CONSRTM   IMAGE II Consortium Group
  TITLE     Case-control genome-wide association study of
            attention-deficit/hyperactivity disorder
  JOURNAL   J Am Acad Child Adolesc Psychiatry 49 (9), 906-920 (2010)
   PUBMED   20732627
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   10 (residues 1 to 917)
  AUTHORS   Irwin,D.M. and Tan,H.
  TITLE     Molecular evolution of the vertebrate hexokinase gene family:
            Identification of a conserved fifth vertebrate hexokinase gene
  JOURNAL   Comp Biochem Physiol Part D Genomics Proteomics 3 (1), 96-107
            (2008)
   PUBMED   20483211
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596223.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_079406.3.
            
            Summary: This gene encodes a member of the hexokinase protein
            family. The encoded protein is involved in glucose metabolism, and
            reduced expression may be associated with gestational diabetes
            mellitus. High expression of this gene may also be associated with
            poor prognosis in hepatocarcinoma. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK095086.1, AK291024.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354624.6/ ENSP00000346643.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..917
                     /product="hexokinase HKDC1"
                     /EC_number="2.7.1.1"
                     /note="putative hexokinase HKDC1; hexokinase
                     domain-containing protein 1"
                     /calculated_mol_wt=102414
     Region          1..20
                     /region_name="Mitochondrial-binding peptide (MBP).
                     /evidence=ECO:0000305|PubMed:30517626"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TB90.3)"
     Region          30..458
                     /region_name="ASKHA_NBD_HKDC1_meta_rpt1"
                     /note="nucleotide-binding domain (NBD) of the first repeat
                     of hexokinase domain-containing protein 1 (HKDC1) from
                     metazoan hexokinase (HK) domain family; cd24126"
                     /db_xref="CDD:466976"
     Region          73..207
                     /region_name="Hexokinase small subdomain 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01084"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TB90.3)"
     Region          208..447
                     /region_name="Hexokinase large subdomain 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01084"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TB90.3)"
     Region          478..910
                     /region_name="ASKHA_NBD_HKDC1_meta_rpt2"
                     /note="nucleotide-binding domain (NBD) of the second
                     repeat of hexokinase domain-containing protein 1 (HKDC1)
                     from metazoan hexokinase (HK) domain family; cd24130"
                     /db_xref="CDD:466980"
     Region          521..654
                     /region_name="Hexokinase small subdomain 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01084"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TB90.3)"
     Region          655..894
                     /region_name="Hexokinase large subdomain 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01084"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TB90.3)"
     CDS             1..917
                     /gene="HKDC1"
                     /gene_synonym="RP92"
                     /coded_by="NM_025130.4:105..2858"
                     /db_xref="CCDS:CCDS7288.1"
                     /db_xref="GeneID:80201"
                     /db_xref="HGNC:HGNC:23302"
                     /db_xref="MIM:617221"
ORIGIN      
        1 mfavhlmafy fsklkedqik kvdrflyhmr lsddtlldim rrfraemekg lakdtnptaa
       61 vkmlptfvra ipdgsengef lsldlggskf rvlkvqvaee gkrhvqmesq fyptpneiir
      121 gngtelfeyv adcladfmkt kdlkhkklpl gltfsfpcrq tkleegvlls wtkkfkargv
      181 qdtdvvsrlt kamrrhkdmd vdilalvndt vgtmmtcayd dpycevgvii gtgtnacyme
      241 dmsnidlveg degrmcinte wgafgddgal edirtefdre ldlgslnpgk qlfekmisgl
      301 ylgelvrlil lkmakagllf ggekssalht kgkietrhva amekykegla ntreilvdlg
      361 lepseadcia vqhvctivsf rsanlcaaal aailtrlren kkverlrttv gmdgtlykih
      421 pqypkrlhkv vrklvpscdv rfllsesgst kgaamvtava srvqaqrkqi drvlalfqlt
      481 reqlvdvqak mraeleyglk kkshglatvr mlptyvcglp dgtekgkfla ldlggtnfrv
      541 llvkirsgrr svrmynkifa ipleimqgtg eelfdhivqc iadfldymgl kgaslplgft
      601 fsfpcrqmsi dkgtligwtk gfkatdcege dvvdmlreai krrnefdldi vavvndtvgt
      661 mmtcgyedpn ceigliagtg snmcymedmr niemveggeg kmcintewgg fgdngciddi
      721 wtrydtevde gslnpgkqry ekmtsgmylg eivrqilidl tkqgllfrgq iserlrtrgi
      781 fetkflsqie sdrlallqvr rilqqlglds tcedsivvke vcgavsrraa qlcgaglaai
      841 vekrredqgl ehlritvgvd gtlyklhphf srilqetvke laprcdvtfm lsedgsgkga
      901 alitavakrl qqaqken
//
LOCUS       NP_056386               1112 aa            linear   PRI 27-APR-2025
DEFINITION  sentrin-specific protease 6 isoform 1 [Homo sapiens].
ACCESSION   NP_056386
VERSION     NP_056386.2
DBSOURCE    REFSEQ: accession NM_015571.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Wang,Y.W., Jia,K.G., Xing,H.J., Pan,Y., Zeng,C.S., Chen,L.,
            Su,Q.J., Shen,W.T., Chen,J., Chen,C., Cao,Q. and Wang,Y.Y.
  TITLE     [Interaction of SENP6 with PINK1 Promotes Temozolomide Resistance
            in Neuroglioma Cells via Inducing the Mitophagy]
  JOURNAL   Mol Biol (Mosk) 58 (1), 126-129 (2024)
   PUBMED   38062972
  REMARK    GeneRIF: [Interaction of SENP6 with PINK1 Promotes Temozolomide
            Resistance in Neuroglioma Cells via Inducing the Mitophagy].
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   He,Q., Chen,Z., Li,J., Liu,J., Zuo,Z., Lin,B., Song,K., Zhou,C.,
            Lai,H., Huang,Q. and Guo,X.
  TITLE     SENP6-Mediated deSUMOylation of VEGFR2 Enhances Its Cell Membrane
            Transport in Angiogenesis
  JOURNAL   Int J Mol Sci 24 (3), 2544 (2023)
   PUBMED   36768878
  REMARK    GeneRIF: SENP6-Mediated deSUMOylation of VEGFR2 Enhances Its Cell
            Membrane Transport in Angiogenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Chen,K., Wang,Q., Liu,X., Wang,F., Ma,Y., Zhang,S., Shao,Z.,
            Yang,Y. and Tian,X.
  TITLE     Single Cell RNA-Seq Identifies Immune-Related Prognostic Model and
            Key Signature-SPP1 in Pancreatic Ductal Adenocarcinoma
  JOURNAL   Genes (Basel) 13 (10), 1760 (2022)
   PUBMED   36292645
  REMARK    GeneRIF: Single Cell RNA-Seq Identifies Immune-Related Prognostic
            Model and Key Signature-SPP1 in Pancreatic Ductal Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1112)
  AUTHORS   Schick,M., Zhang,L., Maurer,S., Maurer,H.C., Isaakaidis,K.,
            Schneider,L., Patra,U., Schunck,K., Rohleder,E., Hofstetter,J.,
            Baluapuri,A., Scherger,A.K., Slotta-Huspenina,J., Hettler,F.,
            Weber,J., Engleitner,T., Maresch,R., Slawska,J., Lewis,R.,
            Istvanffy,R., Habringer,S., Steiger,K., Baiker,A.,
            Oostendorp,R.A.J., Miething,C., Lenhof,H.P., Bassermann,F.,
            Chapuy,B., Wirth,M., Wolf,E., Rad,R., Muller,S. and Keller,U.
  TITLE     Genetic alterations of the SUMO isopeptidase SENP6 drive
            lymphomagenesis and genetic instability in diffuse large B-cell
            lymphoma
  JOURNAL   Nat Commun 13 (1), 281 (2022)
   PUBMED   35022408
  REMARK    GeneRIF: Genetic alterations of the SUMO isopeptidase SENP6 drive
            lymphomagenesis and genetic instability in diffuse large B-cell
            lymphoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1112)
  AUTHORS   Mitra,S., Bodor,D.L., David,A.F., Abdul-Zani,I., Mata,J.F.,
            Neumann,B., Reither,S., Tischer,C. and Jansen,L.E.T.
  TITLE     Genetic screening identifies a SUMO protease dynamically
            maintaining centromeric chromatin
  JOURNAL   Nat Commun 11 (1), 501 (2020)
   PUBMED   31980633
  REMARK    GeneRIF: SENP6 activity is required throughout the cell cycle,
            suggesting that a dynamic SUMO cycle underlies a continuous
            surveillance of the centromere complex.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1112)
  AUTHORS   Bailey,D. and O'Hare,P.
  TITLE     Characterization of the localization and proteolytic activity of
            the SUMO-specific protease, SENP1
  JOURNAL   J Biol Chem 279 (1), 692-703 (2004)
   PUBMED   14563852
  REMARK    GeneRIF: SENP1 localization is influenced by expression and
            localization of SUMO-1-conjugated target proteins within the cell.
REFERENCE   7  (residues 1 to 1112)
  AUTHORS   Tojo,M., Matsuzaki,K., Minami,T., Honda,Y., Yasuda,H., Chiba,T.,
            Saya,H., Fujii-Kuriyama,Y. and Nakao,M.
  TITLE     The aryl hydrocarbon receptor nuclear transporter is modulated by
            the SUMO-1 conjugation system
  JOURNAL   J Biol Chem 277 (48), 46576-46585 (2002)
   PUBMED   12354770
REFERENCE   8  (residues 1 to 1112)
  AUTHORS   Goodson,M.L., Hong,Y., Rogers,R., Matunis,M.J., Park-Sarge,O.K. and
            Sarge,K.D.
  TITLE     Sumo-1 modification regulates the DNA binding activity of heat
            shock transcription factor 2, a promyelocytic leukemia nuclear body
            associated transcription factor
  JOURNAL   J Biol Chem 276 (21), 18513-18518 (2001)
   PUBMED   11278381
REFERENCE   9  (residues 1 to 1112)
  AUTHORS   Kim,K.I., Baek,S.H., Jeon,Y.J., Nishimori,S., Suzuki,T., Uchida,S.,
            Shimbara,N., Saitoh,H., Tanaka,K. and Chung,C.H.
  TITLE     A new SUMO-1-specific protease, SUSP1, that is highly expressed in
            reproductive organs
  JOURNAL   J Biol Chem 275 (19), 14102-14106 (2000)
   PUBMED   10799485
REFERENCE   10 (residues 1 to 1112)
  AUTHORS   Yeh,E.T., Gong,L. and Kamitani,T.
  TITLE     Ubiquitin-like proteins: new wines in new bottles
  JOURNAL   Gene 248 (1-2), 1-14 (2000)
   PUBMED   10806345
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL356057.12, CR990444.1, AF307849.1, AK021417.1 and AL109897.30.
            
            On Aug 17, 2007 this sequence version replaced NP_056386.1.
            
            Summary: Ubiquitin-like molecules (UBLs), such as SUMO1 (UBL1; MIM
            601912), are structurally related to ubiquitin (MIM 191339) and can
            be ligated to target proteins in a similar manner as ubiquitin.
            However, covalent attachment of UBLs does not result in degradation
            of the modified proteins. SUMO1 modification is implicated in the
            targeting of RANGAP1 (MIM 602362) to the nuclear pore complex, as
            well as in stabilization of I-kappa-B-alpha (NFKBIA; MIM 164008)
            from degradation by the 26S proteasome. Like ubiquitin, UBLs are
            synthesized as precursor proteins, with 1 or more amino acids
            following the C-terminal glycine-glycine residues of the mature UBL
            protein. Thus, the tail sequences of the UBL precursors need to be
            removed by UBL-specific proteases, such as SENP6, prior to their
            conjugation to target proteins (Kim et al., 2000 [PubMed
            10799485]). SENPs also display isopeptidase activity for
            deconjugation of SUMO-conjugated substrates (Lima and Reverter,
            2008 [PubMed 18799455]).[supplied by OMIM, Jun 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.25575.1,
                                           SRR1660805.60699.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000447266.7/ ENSP00000402527.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..1112
                     /product="sentrin-specific protease 6 isoform 1"
                     /EC_number="3.4.22.68"
                     /note="2810017C20Rik; SUMO1/sentrin specific protease 6;
                     sentrin-specific protease 6; SUMO-1-specific protease 1;
                     sentrin/SUMO-specific protease SENP6; SUMO1/sentrin
                     specific peptidase 6"
                     /calculated_mol_wt=126016
     Region          26..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Region          190..219
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Region          329..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Region          666..1112
                     /region_name="Protease"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Region          680..>792
                     /region_name="Peptidase_C48"
                     /note="Ulp1 protease family, C-terminal catalytic domain;
                     cl23802"
                     /db_xref="CDD:420019"
     Region          870..905
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Site            919
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Region          <973..1067
                     /region_name="Peptidase_C48"
                     /note="Ulp1 protease family, C-terminal catalytic domain;
                     cl23802"
                     /db_xref="CDD:420019"
     Region          1082..1112
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZR1.2)"
     Site            1111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR1.2)"
     CDS             1..1112
                     /gene="SENP6"
                     /gene_synonym="SSP1; SUSP1"
                     /coded_by="NM_015571.4:646..3984"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47454.1"
                     /db_xref="GeneID:26054"
                     /db_xref="HGNC:HGNC:20944"
                     /db_xref="MIM:605003"
ORIGIN      
        1 maagksggsa geitfleala rseskrdggf knnwsfdhee esegdtdkdg tnllsvdede
       61 dsetskgkkl nrrseivans sgefilktyv rrnksesfkt lkgnpiglnm lsnnkklsen
      121 tqntslcsgt vvhgrrfhha haqipvvkta aqssldrker keypphvqkv einpvrlsrl
      181 qgverimkkt eesesqvepe ikrkvqqkrh cstyqptppl spaskkclth ledlqrncrq
      241 aitlnestgp llrtsihqns ggqksqntgl ttkkfygnnv ekvpidiivn cddskhtylq
      301 tngkvilpga kipkitnlke rktslsdlnd piilssdddd dndrtnrres ispqpadsac
      361 sspapstgkv eaalnentcr aerelrsipe dselntvtlp rkarmkdqfg nsiintplkr
      421 rkvfsqeppd alalscqssf dsvilncrsi rvgtlfrlli epvifcldfi kiqldepdhd
      481 pveiilntsd ltkcewcnvr klpvvflqai pavyqklsiq lqmnkedkvw ndckgvnklt
      541 nleeqyiili fqngldppan mvfesiinei giknnisnff akipfeeang rlvactrtye
      601 esikgscgqk enkiktvsfe skiqlrskqe fqffdeeeet genhtifigp veklivyppp
      661 pakggisvtn edlhclnege flndviidfy lkylvleklk kedadrihif ssffykrlnq
      721 rerrnhettn lsiqqkrhgr vktwtrhvdi fekdfifvpl neaahwflav vcfpglekpk
      781 yepnphyhen aviqkcstve dscisssase mescsqnssa kpvikkmlnk khciavidsn
      841 pgqeesdpry krnicsvkys vkkinhtase neefnkgest sqkvadrtks englqnesls
      901 sthhtdglsk irlnysdesp eagkmledel vdfsedqdnq ddssddgfla ddncsseigq
      961 whlkptickq pcillmdslr gpsrsnvvki lreylevewe vkkgskrsfs kdvmkgsnpk
     1021 vpqqnnfsdc gvyvlqyves ffenpilsfe lpmnlanwfp pprmrtkree irniilklqe
     1081 dqskekrkhk dtysteaplg egteqyvnsi sd
//
LOCUS       NP_071354                454 aa            linear   PRI 27-APR-2025
DEFINITION  SH2 domain-containing protein 4A isoform a [Homo sapiens].
ACCESSION   NP_071354
VERSION     NP_071354.2
DBSOURCE    REFSEQ: accession NM_022071.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Shi,H., Luo,J., Ye,L., Duan,C., Zhang,M., Ran,H., Li,C., Wu,Q. and
            Shao,Y.
  TITLE     SH2D4A inhibits esophageal squamous cell carcinoma progression
            through FAK/PI3K/AKT signaling pathway
  JOURNAL   Cell Signal 114, 110997 (2024)
   PUBMED   38043670
  REMARK    GeneRIF: SH2D4A inhibits esophageal squamous cell carcinoma
            progression through FAK/PI3K/AKT signaling pathway.
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Matsumoto,T., Okayama,H., Nakajima,S., Saito,K., Ito,M., Kaneta,A.,
            Kanke,Y., Onozawa,H., Hayase,S., Fujita,S., Sakamoto,W., Saito,M.,
            Seze,Z., Momma,T., Mimura,K. and Kono,K.
  TITLE     SH2D4A downregulation due to loss of chromosome 8p is associated
            with poor prognosis and low T cell infiltration in colorectal
            cancer
  JOURNAL   Br J Cancer 126 (6), 917-926 (2022)
   PUBMED   34893760
  REMARK    GeneRIF: SH2D4A downregulation due to loss of chromosome 8p is
            associated with poor prognosis and low T cell infiltration in
            colorectal cancer.
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Lapinski,P.E., Oliver,J.A., Kamen,L.A., Hughes,E.D., Saunders,T.L.
            and King,P.D.
  TITLE     Genetic analysis of SH2D4A, a novel adapter protein related to T
            cell-specific adapter and adapter protein in lymphocytes of unknown
            function, reveals a redundant function in T cells
  JOURNAL   J Immunol 181 (3), 2019-2027 (2008)
   PUBMED   18641339
  REMARK    GeneRIF: SH2D4A is dispensable for TCR signal transduction in T
            cells
REFERENCE   8  (residues 1 to 454)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 454)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 454)
  AUTHORS   Dai,S., Zhao,Y. and Ding,Q.
  TITLE     [A novel member of SH(2) signaling protein family: cloning and
            characterization of SH(2)A gene]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 19 (6), 458-462 (2002)
   PUBMED   12476414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA952240.1, BC082982.1, AK024799.1 and CA418381.1.
            
            On Jun 10, 2002 this sequence version replaced NP_071354.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1 and 2
            both encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.38707.1,
                                           SRR1660809.227735.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265807.8/ ENSP00000265807.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..454
                     /product="SH2 domain-containing protein 4A isoform a"
                     /note="SH2 domain-containing protein 4A; protein SH(2)A;
                     protein phosphatase 1 regulatory subunit 38"
                     /calculated_mol_wt=52596
     Region          <19..>268
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          45..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H788.1)"
     Region          107..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H788.1)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D7V1; propagated from
                     UniProtKB/Swiss-Prot (Q9H788.1)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H788.1)"
     Region          152..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H788.1)"
     Region          237..302
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H788.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H788.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H788.1)"
     Region          339..442
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(354,373,393,395)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198213"
     Site            order(394,422)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198213"
     CDS             1..454
                     /gene="SH2D4A"
                     /gene_synonym="PPP1R38; SH2A"
                     /coded_by="NM_022071.4:336..1700"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6009.1"
                     /db_xref="GeneID:63898"
                     /db_xref="HGNC:HGNC:26102"
                     /db_xref="MIM:614968"
ORIGIN      
        1 mlkqilsemy idpdllaels eeqkqilffk mreeqirrwk ereaamerke slpvkprpkk
       61 engksvhwkl gadkevwvwv mgehhldkpy dvlcneiiae rarlkaeqea eeprkthsee
      121 ftnslktksq yhdlqapdnq qtkdiwkkva ekeeleqgsr paptleeeki rslssssrni
      181 qqmladsinr mkayafhqkk esmkkkqdee inqieeertk qickswkeds ewqaslrksk
      241 aadekrrsla kqaredykrl slgaqkgrgg erlqsplrvp qkperpplpp kpqflnsgay
      301 pqkplrnqgv vrtlsssaqe diirwfkeeq lplragyqkt sdtiapwfhg iltlkkanel
      361 llstgmpgsf lirvserikg yalsylsedg ckhflidasa daysflgvdq lqhatladlv
      421 eyhkeepits lgkelllypc gqqdqlpdyl elfe
//
LOCUS       NP_001356030             321 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 10 [Homo
            sapiens].
ACCESSION   NP_001356030
VERSION     NP_001356030.1
DBSOURCE    REFSEQ: accession NM_001369101.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.49532.1,
                                           SRR1660805.72482.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..321
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 10"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=36124
     Region          20..85
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(29,31..33,35..39,42..43,46..47,52..55)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          94..282
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..321
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369101.1:424..1389"
                     /note="isoform 10 is encoded by transcript variant 22"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mecadepcda yeveqtpqgf rstlrapsll ykhivgkrgd trkkiemetk tsisipkpgq
       61 dgeivitgqh rngvisartr idvlldtfrr kqpfthflaf flnevevqeg flrfqeevla
      121 kcsmdhgvds sifqnpkklh ltigmlvlls eeeiqqtcem lqqckeefin disggkplev
      181 emagieymnd dpgmvdvlya kvhmkdgsnr lqelvdrvle rfqasglivk ewnsvklhat
      241 vmntlfrkdp naegrynlyt aegkyifker esfdgrnilk sfallprley ndaisahcnl
      301 clpgssdspa sasqvagitv v
//
LOCUS       NP_001026881             290 aa            linear   PRI 27-APR-2025
DEFINITION  endoplasmic reticulum-Golgi intermediate compartment protein 1
            [Homo sapiens].
ACCESSION   NP_001026881
VERSION     NP_001026881.1
DBSOURCE    REFSEQ: accession NM_001031711.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Marconi,C., Lemmens,L., Masclaux,F., Mattioli,F., Fluss,J.,
            Extermann,P., Mendez,P., Leuchter,R.H., Stathaki,E., Laurent,S.,
            Hammar,E., Vannier,A., Varvagiannis,K., Guipponi,M., Sloan-Bena,F.,
            Blouin,J.L., Abramowicz,M. and Fokstuen,S.
  TITLE     Bi-allelic loss of ERGIC1 causes relatively mild arthrogryposis
  JOURNAL   Clin Genet 100 (3), 329-333 (2021)
   PUBMED   34037256
  REMARK    GeneRIF: Bi-allelic loss of ERGIC1 causes relatively mild
            arthrogryposis.
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Yoo,W., Cho,E.B., Kim,S. and Yoon,J.B.
  TITLE     The E3 ubiquitin ligase MARCH2 regulates ERGIC3-dependent
            trafficking of secretory proteins
  JOURNAL   J Biol Chem 294 (28), 10900-10912 (2019)
   PUBMED   31142615
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Wang,F., Guan,X., Yang,J., He,W., Wei,Y., Chen,H. and Li,Y.
  TITLE     Differential Expression and Significance of Endoplasmic Reticulum
            Golgi Intermediate Compartment 1 in Precancerous Gastric Lesions
            and Gastric Cancer
  JOURNAL   Am J Med Sci 355 (3), 228-234 (2018)
   PUBMED   29549924
  REMARK    GeneRIF: ERGIC1 might play an inhibitory role in the initiation and
            progression of gastric cancer.
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of gene polymorphisms with chronic kidney disease in
            Japanese individuals
  JOURNAL   Int J Mol Med 24 (4), 539-547 (2009)
   PUBMED   19724895
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Breuza,L., Halbeisen,R., Jeno,P., Otte,S., Barlowe,C., Hong,W. and
            Hauri,H.P.
  TITLE     Proteomics of endoplasmic reticulum-Golgi intermediate compartment
            (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies
            ERGIC-32, a new cycling protein that interacts with human Erv46
  JOURNAL   J Biol Chem 279 (45), 47242-47253 (2004)
   PUBMED   15308636
  REMARK    GeneRIF: ERGIC-32 functions as a modulator of the hErv41-hErv46
            complex by stabilizing hErv46
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB443891.1, AB033007.1,
            BC014490.1 and CD365875.1.
            
            Summary: This gene encodes a cycling membrane protein which is an
            endoplasmic reticulum-golgi intermediate compartment (ERGIC)
            protein which interacts with other members of this protein family
            to increase their turnover. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012766.2, SRR1803616.107162.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393784.8/ ENSP00000377374.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.1"
     Protein         1..290
                     /product="endoplasmic reticulum-Golgi intermediate
                     compartment protein 1"
                     /note="endoplasmic reticulum-golgi intermediate
                     compartment 32 kDa protein; endoplasmic reticulum-golgi
                     intermediate compartment (ERGIC) 1; ER-Golgi intermediate
                     compartment 32 kDa protein"
                     /calculated_mol_wt=32461
     Region          5..98
                     /region_name="ERGIC_N"
                     /note="Endoplasmic Reticulum-Golgi Intermediate
                     Compartment (ERGIC); pfam13850"
                     /db_xref="CDD:464000"
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X5.1)"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15308636,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q969X5.1)"
     Region          104..271
                     /region_name="COPIIcoated_ERV"
                     /note="Endoplasmic reticulum vesicle transporter;
                     pfam07970"
                     /db_xref="CDD:462327"
     Site            255..275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X5.1)"
     CDS             1..290
                     /gene="ERGIC1"
                     /gene_synonym="AMC2; AMCN; ERGIC-32; ERGIC32; NET24"
                     /coded_by="NM_001031711.3:164..1036"
                     /db_xref="CCDS:CCDS34292.1"
                     /db_xref="GeneID:57222"
                     /db_xref="HGNC:HGNC:29205"
                     /db_xref="MIM:617946"
ORIGIN      
        1 mpfdfrrfdi yrkvpkdltq ptytgaiisi ccclfilflf lseltgfitt evvnelyvdd
       61 pdkdsggkid vslnislpnl hcelvgldiq demgrhevgh idnsmkipln ngagcrfegq
      121 fsinkvpgnf hvsthsataq pqnpdmthvi hklsfgdtlq vqnihgafna lggadrltsn
      181 plashdyilk ivptvyedks gkqrysyqyt vankeyvays htgriipaiw frydlspitv
      241 kyterrqply rfitticaii ggtftvagil dsciftasea wkkiqlgkmh
//
LOCUS       NP_001355961             516 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 9 isoform 12 [Homo sapiens].
ACCESSION   NP_001355961
VERSION     NP_001355961.1
DBSOURCE    REFSEQ: accession NM_001369032.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ma,X., Yan,W., Xu,P., Ma,L., Zan,Y., Huang,L., Wang,G., Liu,L. and
            Hui,W.
  TITLE     LncRNA-p21 suppresses cell proliferation and induces apoptosis in
            gastric cancer by sponging miR-514b-3p and up-regulating ARHGEF9
            expression
  JOURNAL   Biol Chem 403 (10), 945-958 (2022)
   PUBMED   35947460
  REMARK    GeneRIF: LncRNA-p21 suppresses cell proliferation and induces
            apoptosis in gastric cancer by sponging miR-514b-3p and
            up-regulating ARHGEF9 expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Yang,H., Liao,H., Gan,S., Xiao,T. and Wu,L.
  TITLE     ARHGEF9 gene variant leads to developmental and epileptic
            encephalopathy: Genotypic phenotype analysis and treatment
            exploration
  JOURNAL   Mol Genet Genomic Med 10 (7), e1967 (2022)
   PUBMED   35638461
  REMARK    GeneRIF: ARHGEF9 gene variant leads to developmental and epileptic
            encephalopathy: Genotypic phenotype analysis and treatment
            exploration.
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Hines,D.J., Contreras,A., Garcia,B., Barker,J.S., Boren,A.J.,
            Moufawad El Achkar,C., Moss,S.J. and Hines,R.M.
  TITLE     Human ARHGEF9 intellectual disability syndrome is phenocopied by a
            mutation that disrupts collybistin binding to the GABAA receptor
            alpha2 subunit
  JOURNAL   Mol Psychiatry 27 (3), 1729-1741 (2022)
   PUBMED   35169261
  REMARK    GeneRIF: Human ARHGEF9 intellectual disability syndrome is
            phenocopied by a mutation that disrupts collybistin binding to the
            GABAA receptor alpha2 subunit.
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Ghesh,L., Besnard,T., Nizon,M., Trochu,E., Landeau-Trottier,G.,
            Breheret,F., Thauvin-Robinet,C., Bruel,A.L., Kuentz,P., Coubes,C.,
            Cuisset,L., Mignot,C., Keren,B., Bezieau,S. and Cogne,B.
  TITLE     Loss-of-function variants in ARHGEF9 are associated with an
            X-linked intellectual disability dominant disorder
  JOURNAL   Hum Mutat 42 (5), 498-505 (2021)
   PUBMED   33600053
  REMARK    GeneRIF: Loss-of-function variants in ARHGEF9 are associated with
            an X-linked intellectual disability dominant disorder.
REFERENCE   5  (residues 1 to 516)
  AUTHORS   Scala,M., Zonneveld-Huijssoon,E., Brienza,M., Mecarelli,O., van der
            Hout,A.H., Zambrelli,E., Turner,K., Zara,F., Peron,A., Vignoli,A.
            and Striano,P.
  TITLE     De novo ARHGEF9 missense variants associated with
            neurodevelopmental disorder in females: expanding the genotypic and
            phenotypic spectrum of ARHGEF9 disease in females
  JOURNAL   Neurogenetics 22 (1), 87-94 (2021)
   PUBMED   32939676
  REMARK    GeneRIF: De novo ARHGEF9 missense variants associated with
            neurodevelopmental disorder in females: expanding the genotypic and
            phenotypic spectrum of ARHGEF9 disease in females.
REFERENCE   6  (residues 1 to 516)
  AUTHORS   Harrington,A.W., Kim,J.Y. and Yoon,S.O.
  TITLE     Activation of Rac GTPase by p75 is necessary for c-jun N-terminal
            kinase-mediated apoptosis
  JOURNAL   J Neurosci 22 (1), 156-166 (2002)
   PUBMED   11756498
REFERENCE   7  (residues 1 to 516)
  AUTHORS   Grosskreutz,Y., Hermann,A., Kins,S., Fuhrmann,J.C., Betz,H. and
            Kneussel,M.
  TITLE     Identification of a gephyrin-binding motif in the GDP/GTP exchange
            factor collybistin
  JOURNAL   Biol Chem 382 (10), 1455-1462 (2001)
   PUBMED   11727829
  REMARK    GeneRIF: Here we identified residues critical for interaction with
            gephyrin in the linker region between the SH3 and the DH domains of
            collybistin.
REFERENCE   8  (residues 1 to 516)
  AUTHORS   Kins,S., Betz,H. and Kirsch,J.
  TITLE     Collybistin, a newly identified brain-specific GEF, induces
            submembrane clustering of gephyrin
  JOURNAL   Nat Neurosci 3 (1), 22-29 (2000)
   PUBMED   10607391
REFERENCE   9  (residues 1 to 516)
  AUTHORS   Reid,T., Bathoorn,A., Ahmadian,M.R. and Collard,J.G.
  TITLE     Identification and characterization of hPEM-2, a guanine nucleotide
            exchange factor specific for Cdc42
  JOURNAL   J Biol Chem 274 (47), 33587-33593 (1999)
   PUBMED   10559246
REFERENCE   10 (residues 1 to 516)
  AUTHORS   Balint,B. and Thomas,R.
  TITLE     Hereditary Hyperekplexia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL451106.9, AL355142.11 and
            AL391277.16.
            
            Summary: The protein encoded by this gene is a Rho-like GTPase that
            switches between the active (GTP-bound) state and inactive
            (GDP-bound) state to regulate CDC42 and other genes. This
            brain-specific protein also acts as an adaptor protein for the
            recruitment of gephyrin and together these proteins facilitate
            receceptor recruitement in GABAnergic and glycinergic synapses.
            Defects in this gene are the cause of startle disease with epilepsy
            (STHEE), also known as hyperekplexia with epilepsy, as well as
            several other types of cognitive disability. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.277653.1,
                                           SRR1803612.80265.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq11.1"
     Protein         1..516
                     /product="rho guanine nucleotide exchange factor 9 isoform
                     12"
                     /note="hPEM-2 collybistin; rho guanine nucleotide exchange
                     factor 9; PEM-2 homolog; rac/Cdc42 guanine nucleotide
                     exchange factor 9; Cdc42 guanine nucleotide exchange
                     factor (GEF) 9"
                     /calculated_mol_wt=60915
     Region          7..68
                     /region_name="SH3_ARHGEF9"
                     /note="Src homology 3 domain of the Rho guanine nucleotide
                     exchange factor ARHGEF9; cd11975"
                     /db_xref="CDD:212908"
     Site            order(14..16,21..22,24,60)
                     /site_type="other"
                     /note="putative DH-PH interface [polypeptide binding]"
                     /db_xref="CDD:212908"
     Site            order(17,19,22,26,44..45,58,60..61)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212908"
     Region          100..110
                     /region_name="Interaction with GPHN.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O43307.3)"
     Region          107..286
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; smart00325"
                     /db_xref="CDD:214619"
     Site            order(110,114,209,236..237,240..241,243..244,247..248,
                     251..252,255,281,285)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          291..430
                     /region_name="PH_Collybistin_ASEF"
                     /note="Collybistin/APC-stimulated guanine nucleotide
                     exchange factor pleckstrin homology (PH) domain; cd01224"
                     /db_xref="CDD:269931"
     Region          453..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43307.3)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UTH8; propagated from
                     UniProtKB/Swiss-Prot (O43307.3)"
     CDS             1..516
                     /gene="ARHGEF9"
                     /gene_synonym="COLLYBISTIN; DEE8; EIEE8; HPEM-2; PEM-2;
                     PEM2"
                     /coded_by="NM_001369032.1:808..2358"
                     /note="isoform 12 is encoded by transcript variant 14"
                     /db_xref="GeneID:23229"
                     /db_xref="HGNC:HGNC:14561"
                     /db_xref="MIM:300429"
ORIGIN      
        1 mydlitgdsi vsaeavwdhv tmanrelafk agdvikvlda snkdwwwgqi ddeegwfpas
       61 fvrlwvnqed eveegpsdvq nghldpnsdc lclgrplqnr dqmranvine imsterhyik
      121 hlkdicegyl kqcrkrrdmf sdeqlkvifg niediyrfqm gfvrdlekqy nnddphlsei
      181 gpcflehqdg fwiyseycnn hldacmelsk lmkdsryqhf feacrllqqm idiaidgfll
      241 tpvqkickyp lqlaellkyt aqdhsdyryv aaalavmrnv tqqinerkrr lenidkiaqw
      301 qasvldwege dildrsseli ytgemawiyq pygrnqqrvf flfdhqmvlc kkdlirrdil
      361 yykgridmdk yevvdiedgr dddfnvsmkn afklhnkete eihlffakkl eekirwlraf
      421 reerkmvqed ekigfeisen qkrqaamtvr kvpkqkgvns arsvppsypp pqdplnhgqy
      481 lvpdgiaqsq vfeftepkrs qspfwqnfsr ltpfkk
//
LOCUS       NP_008968                889 aa            linear   PRI 27-APR-2025
DEFINITION  A disintegrin and metalloproteinase with thrombospondin motifs 8
            preproprotein [Homo sapiens].
ACCESSION   NP_008968
VERSION     NP_008968.4
DBSOURCE    REFSEQ: accession NM_007037.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Ma,F., Liu,H., Xia,T., Zhang,Z., Ma,S., Hao,Y., Shen,J., Jiang,Y.
            and Li,N.
  TITLE     HSFAS mediates fibroblast proliferation, migration,
            trans-differentiation and apoptosis in hypertrophic scars via
            interacting with ADAMTS8
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 56 (3), 440-451 (2024)
   PUBMED   38006215
  REMARK    GeneRIF: HSFAS mediates fibroblast proliferation, migration,
            trans-differentiation and apoptosis in hypertrophic scars via
            interacting with ADAMTS8.
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Zhang,Q., Kanyomse,Q., Luo,C., Mo,Q., Zhao,X., Wang,L., Peng,W. and
            Ren,G.
  TITLE     The Prognostic Value of ADAMTS8 and Its Role as a Tumor Suppressor
            in Breast Cancer
  JOURNAL   Cancer Invest 41 (2), 119-132 (2023)
   PUBMED   36346393
  REMARK    GeneRIF: The Prognostic Value of ADAMTS8 and Its Role as a Tumor
            Suppressor in Breast Cancer.
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Zhou,B., Liu,Y., Ma,G., Wang,X., Chang,B., Lu,H. and Feng,X.
  TITLE     ADAMTS8 inhibits glioma development in vitro and in vivo
  JOURNAL   Folia Neuropathol 61 (2), 144-152 (2023)
   PUBMED   37587889
  REMARK    GeneRIF: ADAMTS8 inhibits glioma development in vitro and in vivo.
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Zhang,Y., Hu,K., Qu,Z., Xie,Z. and Tian,F.
  TITLE     ADAMTS8 inhibited lung cancer progression through suppressing VEGFA
  JOURNAL   Biochem Biophys Res Commun 598, 1-8 (2022)
   PUBMED   35149432
  REMARK    GeneRIF: ADAMTS8 inhibited lung cancer progression through
            suppressing VEGFA.
REFERENCE   5  (residues 1 to 889)
  AUTHORS   Santamaria,S., Martin,D.R., Dong,X., Yamamoto,K., Apte,S.S. and
            Ahnstrom,J.
  TITLE     Post-translational regulation and proteolytic activity of the
            metalloproteinase ADAMTS8
  JOURNAL   J Biol Chem 297 (5), 101323 (2021)
   PUBMED   34687701
  REMARK    GeneRIF: Post-translational regulation and proteolytic activity of
            the metalloproteinase ADAMTS8.
REFERENCE   6  (residues 1 to 889)
  AUTHORS   Porter,S., Span,P.N., Sweep,F.C., Tjan-Heijnen,V.C.,
            Pennington,C.J., Pedersen,T.X., Johnsen,M., Lund,L.R., Romer,J. and
            Edwards,D.R.
  TITLE     ADAMTS8 and ADAMTS15 expression predicts survival in human breast
            carcinoma
  JOURNAL   Int J Cancer 118 (5), 1241-1247 (2006)
   PUBMED   16152618
  REMARK    GeneRIF: ADAMTS8 and ADAMTS15 have emerged as novel predictors of
            survival in patients with breast carcinoma
REFERENCE   7  (residues 1 to 889)
  AUTHORS   Dunn,J.R., Panutsopulos,D., Shaw,M.W., Heighway,J., Dormer,R.,
            Salmo,E.N., Watson,S.G., Field,J.K. and Liloglou,T.
  TITLE     METH-2 silencing and promoter hypermethylation in NSCLC
  JOURNAL   Br J Cancer 91 (6), 1149-1154 (2004)
   PUBMED   15328519
  REMARK    GeneRIF: Downdownregulation of METH-2 expression in primary NSCLC,
            often associated with promoter hypermethylation, is a frequent
            event, which may be related to the development of the disease.
REFERENCE   8  (residues 1 to 889)
  AUTHORS   Collins-Racie,L.A., Flannery,C.R., Zeng,W., Corcoran,C.,
            Annis-Freeman,B., Agostino,M.J., Arai,M., DiBlasio-Smith,E.,
            Dorner,A.J., Georgiadis,K.E., Jin,M., Tan,X.Y., Morris,E.A. and
            LaVallie,E.R.
  TITLE     ADAMTS-8 exhibits aggrecanase activity and is expressed in human
            articular cartilage
  JOURNAL   Matrix Biol 23 (4), 219-230 (2004)
   PUBMED   15296936
  REMARK    GeneRIF: Ability of ADAMTS-8 to cleave aggrecan at
            aggrecanase-susceptible Glu373-Ala374 peptide bond. Presence of
            ADAMTS-8 mRNA transcripts in normal and osteoarthritic human
            cartilage. (ADAMTS-8)
REFERENCE   9  (residues 1 to 889)
  AUTHORS   Georgiadis,K.E., Hirohata,S., Seldin,M.F. and Apte,S.S.
  TITLE     ADAM-TS8, a novel metalloprotease of the ADAM-TS family located on
            mouse chromosome 9 and human chromosome 11
  JOURNAL   Genomics 62 (2), 312-315 (1999)
   PUBMED   10610729
REFERENCE   10 (residues 1 to 889)
  AUTHORS   Vazquez,F., Hastings,G., Ortega,M.A., Lane,T.F., Oikemus,S.,
            Lombardo,M. and Iruela-Arispe,M.L.
  TITLE     METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a
            new family of proteins with angio-inhibitory activity
  JOURNAL   J Biol Chem 274 (33), 23349-23357 (1999)
   PUBMED   10438512
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF060153.1, BX424609.2,
            AP002986.2 and BC089435.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 25, 2007 this sequence version replaced NP_008968.3.
            
            Summary: This gene encodes a member of the ADAMTS (a disintegrin
            and metalloproteinase with thrombospondin motifs) protein family.
            Members of the family share several distinct protein modules,
            including a propeptide region, a metalloproteinase domain, a
            disintegrin-like domain, and a thrombospondin type 1 (TS) motif.
            Individual members of this family differ in the number of
            C-terminal TS motifs, and some have unique C-terminal domains. The
            encoded preproprotein is proteolytically processed to generate the
            mature enzyme. This enzyme contains two C-terminal TS motifs, and
            disrupts angiogenesis in vivo. A number of disorders have been
            mapped in the vicinity of this gene, most notably lung neoplasms.
            Reduced expression of this gene has been observed in multiple human
            cancers and this gene has been proposed as a potential tumor
            suppressor. [provided by RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF060153.1, SRR14038196.2400245.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257359.7/ ENSP00000257359.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.3"
     Protein         1..889
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 8 preproprotein"
                     /note="a disintegrin-like and metalloprotease (reprolysin
                     type) with thrombospondin type 1 motif, 8; METH-2; METH-8;
                     ADAMTS-8"
                     /calculated_mol_wt=93662
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2817
     Region          39..148
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          138..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP79.2)"
     mat_peptide     214..889
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 8. /id=PRO_0000029179"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP79.2)"
                     /calculated_mol_wt=74087
     Region          219..426
                     /region_name="ZnMc_ADAMTS_like"
                     /note="Zinc-dependent metalloprotease, ADAMTS_like
                     subgroup. ADAMs (A Disintegrin And Metalloprotease) are
                     glycoproteins, which play roles in cell signaling, cell
                     fusion, and cell-cell interactions. This particular
                     subfamily represents domain architectures that...;
                     cd04273"
                     /db_xref="CDD:239801"
     Site            344
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UP79.2)"
     Site            order(363..364,367,373)
                     /site_type="active"
                     /db_xref="CDD:239801"
     Site            400
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UP79.2)"
     Region          440..513
                     /region_name="ADAMTS_CR_2"
                     /note="ADAMTS cysteine-rich domain 2; pfam17771"
                     /db_xref="CDD:465496"
     Site            465
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UP79.2)"
     Site            490
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UP79.2)"
     Region          529..581
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          587..689
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Site            599
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UP79.2)"
     Region          690..831
                     /region_name="Spacer"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP79.2)"
     Region          691..809
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Region          836..887
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     CDS             1..889
                     /gene="ADAMTS8"
                     /gene_synonym="ADAM-TS8; METH2"
                     /coded_by="NM_007037.6:324..2993"
                     /db_xref="CCDS:CCDS41732.1"
                     /db_xref="GeneID:11095"
                     /db_xref="HGNC:HGNC:224"
                     /db_xref="MIM:605175"
ORIGIN      
        1 mlpapaaprw ppllllllll lplargapar paaggqasel vvptrlpgsa gelalhlsaf
       61 gkgfvlrlap ddsflapefk ierlggsgra tggerglrgc ffsgtvngep eslaavslcr
      121 glsgsflldg eeftiqpqga ggslaqphrl qrwgpagarp lprgpeweve tgegqrqerg
      181 dhqedseees qeeeaegase pppplgatsr tkrfvsearf vetllvadas maafygadlq
      241 nhiltlmsva ariykhpsik nsinlmvvkv livedekwgp evsdnggltl rnfcnwqrrf
      301 nqpsdrhpeh ydtailltrq nfcgqeglcd tlgvadigti cdpnkscsvi edeglqaaht
      361 lahelghvls mphddskpct rlfgpmgkhh vmaplfvhln qtlpwspcsa myltelldgg
      421 hgdclldapa aalplptglp grmalyqldq qcrqifgpdf rhcpntsaqd vcaqlwchtd
      481 gaeplchtkn gslpwadgtp cgpghlcseg sclpeeever pkpvadggwa pwgpwgecsr
      541 tcgggvqfsh reckdpepqn ggryclgrra kyqschteec ppdgksfreq qcekynayny
      601 tdmdgnllqw vpkyagvspr drcklfcrar grsefkvfea kvidgtlcgp etlaicvrgq
      661 cvkagcdhvv dsprkldkcg vcggkgnscr kvsgsltptn ygyndivtip agatnidvkq
      721 rshpgvqndg nylalktadg qyllngnlai saieqdilvk gtilkysgsi atlerlqsfr
      781 plpepltvql ltvpgevfpp kvkytffvpn dvdfsmqssk erattniiqp llhaqwvlgd
      841 wsecsstcga gwqrrtvecr dpsgqasatc nkalkpedak pcesqlcpl
//
LOCUS       NP_001355296             286 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 59-like isoform 3 precursor [Mus musculus].
ACCESSION   NP_001355296
VERSION     NP_001355296.1
DBSOURCE    REFSEQ: accession NM_001368367.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Rutledge,E.A. and McMahon,A.P.
  TITLE     Mutational analysis of genes with ureteric progenitor cell-specific
            expression in branching morphogenesis of the mouse kidney
  JOURNAL   Dev Dyn 249 (6), 765-774 (2020)
   PUBMED   32017326
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Rutledge,E.A., Benazet,J.D. and McMahon,A.P.
  TITLE     Cellular heterogeneity in the ureteric progenitor niche and
            distinct profiles of branching morphogenesis in organ development
  JOURNAL   Development 144 (17), 3177-3188 (2017)
   PUBMED   28705898
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC157774.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3816886.1,
                                           ERR3363658.853596.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 34.15 cM"
     Protein         1..286
                     /product="transmembrane protein 59-like isoform 3
                     precursor"
                     /note="brain-specific membrane-anchored protein"
                     /calculated_mol_wt=29820
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2076
     Region          72..227
                     /region_name="BSMAP"
                     /note="Brain specific membrane anchored protein;
                     pfam12280"
                     /db_xref="CDD:463519"
     CDS             1..286
                     /gene="Tmem59l"
                     /gene_synonym="5330410G16Rik"
                     /coded_by="NM_001368367.1:32..892"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:67937"
                     /db_xref="MGI:MGI:1915187"
ORIGIN      
        1 maavalplll llaslvtptp ardpfapqlg dtqrcqqrcr qhhpgsppaq pepegpsesp
       61 nnkailisac ergcrlfsic rfvakssrpn ateteceaac teayvkaaeq racsegcwgq
      121 ipepetqleq ktqpvaenfa fqgshlqrve vtwrrshpka lelhmdpvgp ldkvrkakpr
      181 vktskakves edqqesdfls cmsrrsglpr wvlfcclfls ilimlwlscc tlvttpgqhl
      241 kfqpltaeqh kgllvesdwp lypplpppay edstppyklk ldlttl
//
LOCUS       NP_001350764             428 aa            linear   PRI 27-APR-2025
DEFINITION  rhomboid-related protein 3 isoform 3 [Homo sapiens].
ACCESSION   NP_001350764 XP_016879761
VERSION     NP_001350764.1
DBSOURCE    REFSEQ: accession NM_001363835.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Lastun,V.L., Levet,C. and Freeman,M.
  TITLE     The mammalian rhomboid protein RHBDL4 protects against endoplasmic
            reticulum stress by regulating the morphology and distribution of
            ER sheets
  JOURNAL   J Biol Chem 298 (6), 101935 (2022)
   PUBMED   35436469
  REMARK    GeneRIF: The mammalian rhomboid protein RHBDL4 protects against
            endoplasmic reticulum stress by regulating the morphology and
            distribution of ER sheets.
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Freeman,M.
  TITLE     The rhomboid-like superfamily: molecular mechanisms and biological
            roles
  JOURNAL   Annu Rev Cell Dev Biol 30, 235-254 (2014)
   PUBMED   25062361
  REMARK    Review article
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Bergbold,N. and Lemberg,M.K.
  TITLE     Emerging role of rhomboid family proteins in mammalian biology and
            disease
  JOURNAL   Biochim Biophys Acta 1828 (12), 2840-2848 (2013)
   PUBMED   23562403
  REMARK    Review article
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Lemberg,M.K.
  TITLE     Sampling the membrane: function of rhomboid-family proteins
  JOURNAL   Trends Cell Biol 23 (5), 210-217 (2013)
   PUBMED   23369641
  REMARK    Review article
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Jaszai,J. and Brand,M.
  TITLE     Cloning and expression of Ventrhoid, a novel vertebrate homologue
            of the Drosophila EGF pathway gene rhomboid
  JOURNAL   Mech Dev 113 (1), 73-77 (2002)
   PUBMED   11900977
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC100976.1 and AC005899.1.
            
            On Jun 3, 2018 this sequence version replaced XP_016879761.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100976.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149178, SAMEA2155550
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..428
                     /product="rhomboid-related protein 3 isoform 3"
                     /EC_number="3.4.21.105"
                     /note="ventrhoid transmembrane protein; rhomboid-related
                     protein 3; rhomboid, veinlet-like 4; rhomboid,
                     veinlet-like 3"
                     /calculated_mol_wt=47365
     Region          36..100
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Site            164..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P58872.1)"
     Region          205..>260
                     /region_name="Rhomboid"
                     /note="Rhomboid family; cl21536"
                     /db_xref="CDD:451297"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P58872.1)"
     CDS             1..428
                     /gene="RHBDL3"
                     /gene_synonym="RHBDL4; VRHO"
                     /coded_by="NM_001363835.1:15..1301"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:162494"
                     /db_xref="HGNC:HGNC:16502"
                     /db_xref="MIM:619017"
ORIGIN      
        1 mgehpspgpa vaacaeaeri eelepeaeer lpaapedhwk vlfdqfdpgn tgyistgkfr
       61 slleshsskl dphkrevlla ladshadgqi gyqdfvslms nkrsnsfrqa ilqgnrrlss
      121 kalleekgls lsqrlirhva yetlpreidr kwyydsytcc pppwfmitvt llevafflyn
      181 gvslgqfvlq vthprylkns lvyhpqlraq vwryltyifm hagiehlgln vvlqllvgvp
      241 lemvhgatri glvyvagvva elvrhevpvq aaadgcgpyl yehgvwagrv aplppvglsp
      301 vpspklcgal gwrgrghhpg rggpeelrae apgpvtvvdf cghvhrlrav rcllehlclh
      361 paglkaaasp lraggprsgr ggkssthrer lrgffsspaq lgradkdrrl watvmfvfrf
      421 ghtvetlf
//
LOCUS       NP_003290                803 aa            linear   PRI 27-APR-2025
DEFINITION  endoplasmin precursor [Homo sapiens].
ACCESSION   NP_003290
VERSION     NP_003290.1
DBSOURCE    REFSEQ: accession NM_003299.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Ma,M., Dubey,R., Jen,A., Pusapati,G.V., Singal,B., Shishkova,E.,
            Overmyer,K.A., Cormier-Daire,V., Fedry,J., Aravind,L., Coon,J.J.
            and Rohatgi,R.
  TITLE     Regulated N-glycosylation controls chaperone function and receptor
            trafficking
  JOURNAL   Science 386 (6722), 667-672 (2024)
   PUBMED   39509507
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Huang,X., Zhang,W., Yang,N., Zhang,Y., Qin,T., Ruan,H., Zhang,Y.,
            Tian,C., Mo,X., Tang,W., Liu,J. and Zhang,B.
  TITLE     Identification of HSP90B1 in pan-cancer hallmarks to aid
            development of a potential therapeutic target
  JOURNAL   Mol Cancer 23 (1), 19 (2024)
   PUBMED   38243263
  REMARK    GeneRIF: Identification of HSP90B1 in pan-cancer hallmarks to aid
            development of a potential therapeutic target.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Zuehlke,A. and Johnson,J.L.
  TITLE     Hsp90 and co-chaperones twist the functions of diverse client
            proteins
  JOURNAL   Biopolymers 93 (3), 211-217 (2010)
   PUBMED   19697319
  REMARK    Review article
REFERENCE   4  (residues 1 to 803)
  AUTHORS   Chen,B., Piel,W.H., Gui,L., Bruford,E. and Monteiro,A.
  TITLE     The HSP90 family of genes in the human genome: insights into their
            divergence and evolution
  JOURNAL   Genomics 86 (6), 627-637 (2005)
   PUBMED   16269234
REFERENCE   5  (residues 1 to 803)
  AUTHORS   Prasadarao,N.V., Srivastava,P.K., Rudrabhatla,R.S., Kim,K.S.,
            Huang,S.H. and Sukumaran,S.K.
  TITLE     Cloning and expression of the Escherichia coli K1 outer membrane
            protein A receptor, a gp96 homologue
  JOURNAL   Infect Immun 71 (4), 1680-1688 (2003)
   PUBMED   12654781
  REMARK    GeneRIF: OmpA of E. coli K1 interacts with a gp96-like molecule on
            HBMECs for invasion (Ecgp: 96-kDa human brain microvascular
            endothelial cell (HBMEC) glycoprotein)
REFERENCE   6  (residues 1 to 803)
  AUTHORS   Maki,R.G., Eddy,R.L. Jr., Byers,M., Shows,T.B. and Srivastava,P.K.
  TITLE     Mapping of the genes for human endoplasmic reticular heat shock
            protein gp96/grp94
  JOURNAL   Somat Cell Mol Genet 19 (1), 73-81 (1993)
   PUBMED   8460400
REFERENCE   7  (residues 1 to 803)
  AUTHORS   Schaiff,W.T., Hruska,K.A. Jr., McCourt,D.W., Green,M. and
            Schwartz,B.D.
  TITLE     HLA-DR associates with specific stress proteins and is retained in
            the endoplasmic reticulum in invariant chain negative cells
  JOURNAL   J Exp Med 176 (3), 657-666 (1992)
   PUBMED   1512535
REFERENCE   8  (residues 1 to 803)
  AUTHORS   Liu,E.S. and Lee,A.S.
  TITLE     Common sets of nuclear factors binding to the conserved promoter
            sequence motif of two coordinately regulated ER protein genes,
            GRP78 and GRP94
  JOURNAL   Nucleic Acids Res 19 (19), 5425-5431 (1991)
   PUBMED   1923827
REFERENCE   9  (residues 1 to 803)
  AUTHORS   Maki,R.G., Old,L.J. and Srivastava,P.K.
  TITLE     Human homologue of murine tumor rejection antigen gp96:
            5'-regulatory and coding regions and relationship to stress-induced
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 87 (15), 5658-5662 (1990)
   PUBMED   2377606
  REMARK    GeneRIF: a paper describing a pathway in which this gene product
            functions
REFERENCE   10 (residues 1 to 803)
  AUTHORS   Srivastava,P.K. and Old,L.J.
  TITLE     Identification of a human homologue of the murine tumor rejection
            antigen GP96
  JOURNAL   Cancer Res 49 (6), 1341-1343 (1989)
   PUBMED   2924290
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078819.24, X15187.1 and
            CA419931.1.
            
            Summary: This gene encodes a member of a family of adenosine
            triphosphate(ATP)-metabolizing molecular chaperones with roles in
            stabilizing and folding other proteins. The encoded protein is
            localized to melanosomes and the endoplasmic reticulum. Expression
            of this protein is associated with a variety of pathogenic states,
            including tumor formation. There is a microRNA gene located within
            the 5' exon of this gene. There are pseudogenes for this gene on
            chromosomes 1 and 15. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GQ900941.1, AJ890084.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299767.10/ ENSP00000299767.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..803
                     /product="endoplasmin precursor"
                     /note="tumor rejection antigen (gp96) 1; endothelial cell
                     (HBMEC) glycoprotein; endoplasmin; 94 kDa
                     glucose-regulated protein; heat shock protein 90 kDa beta
                     member 1; tumor rejection antigen 1; stress-inducible
                     tumor rejection antigen gp96; heat shock protein 90kDa
                     beta family member 1; epididymis luminal protein 35;
                     epididymis secretory sperm binding protein Li 125m; heat
                     shock protein 90kDa beta (Grp94), member 1; heat shock
                     protein family C member 4"
                     /calculated_mol_wt=90178
     sig_peptide     1..21
                     /note="/evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
                     /calculated_mol_wt=2309
     mat_peptide     22..803
                     /product="Endoplasmin. /id=PRO_0000013598"
                     /note="propagated from UniProtKB/Swiss-Prot (P14625.1)"
                     /calculated_mol_wt=90178
     Region          42..44
                     /region_name="SRT pseudosubstrate motif.
                     /evidence=ECO:0000269|PubMed:39509507"
                     /note="propagated from UniProtKB/Swiss-Prot (P14625.1)"
     Site            62
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:31296534, ECO:0000269|PubMed:39509507;
                     propagated from UniProtKB/Swiss-Prot (P14625.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Region          83..275
                     /region_name="HATPase_Hsp90-like"
                     /note="Histidine kinase-like ATPase domain of human
                     cytosolic Hsp90 and its homologs including Escherichia
                     coli HtpG, and related domains; cd16927"
                     /db_xref="CDD:340404"
     Site            order(84..85,88,92,167,195)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340404"
     Site            order(103,107..108,110..111,114,147,149,151,153..154,
                     162..163,165..171,193..199,211,213,244..245,247)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340404"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16263699,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:31296534,
                     ECO:0000269|PubMed:39509507; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Site            order(163,199)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340404"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q66HD0; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Site            217
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:31296534,
                     ECO:0000269|PubMed:39509507; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Region          257..755
                     /region_name="HSP90"
                     /note="Hsp90 protein; pfam00183"
                     /db_xref="CDD:459703"
     Region          288..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14625.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q66HD0; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Site            445
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:31296534,
                     ECO:0000269|PubMed:39509507; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Site            448
                     /site_type="other"
                     /note="Important for ATP hydrolysis.
                     /evidence=ECO:0000250|UniProtKB:P41148; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Site            479
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08113; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Site            481
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:31296534,
                     ECO:0000269|PubMed:39509507; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Site            502
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:31296534,
                     ECO:0000269|PubMed:39509507; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Region          750..803
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14625.1)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P14625.1)"
     Region          800..803
                     /region_name="Prevents secretion from ER"
                     /note="propagated from UniProtKB/Swiss-Prot (P14625.1)"
     CDS             1..803
                     /gene="HSP90B1"
                     /gene_synonym="ECGP; GP96; GRP94; HEL-S-125m; HEL35; TRA1"
                     /coded_by="NM_003299.3:107..2518"
                     /db_xref="CCDS:CCDS9094.1"
                     /db_xref="GeneID:7184"
                     /db_xref="HGNC:HGNC:12028"
                     /db_xref="MIM:191175"
ORIGIN      
        1 mralwvlglc cvlltfgsvr addevdvdgt veedlgksre gsrtddevvq reeeaiqldg
       61 lnasqirelr eksekfafqa evnrmmklii nslyknkeif lrelisnasd aldkirlisl
      121 tdenalsgne eltvkikcdk eknllhvtdt gvgmtreelv knlgtiaksg tseflnkmte
      181 aqedgqstse ligqfgvgfy saflvadkvi vtskhnndtq hiwesdsnef sviadprgnt
      241 lgrgttitlv lkeeasdyle ldtiknlvkk ysqfinfpiy vwssktetve epmeeeeaak
      301 eekeesddea aveeeeeekk pktkkvektv wdwelmndik piwqrpskev eedeykafyk
      361 sfskesddpm ayihftaege vtfksilfvp tsaprglfde ygskksdyik lyvrrvfitd
      421 dfhdmmpkyl nfvkgvvdsd dlplnvsret lqqhkllkvi rkklvrktld mikkiaddky
      481 ndtfwkefgt niklgviedh snrtrlakll rfqsshhptd itsldqyver mkekqdkiyf
      541 magssrkeae sspfverllk kgyeviylte pvdeyciqal pefdgkrfqn vakegvkfde
      601 sektkesrea vekefeplln wmkdkalkdk iekavvsqrl tespcalvas qygwsgnmer
      661 imkaqayqtg kdistnyyas qkktfeinpr hplirdmlrr ikededdktv ldlavvlfet
      721 atlrsgyllp dtkaygdrie rmlrlslnid pdakveeepe eepeetaedt tedteqdede
      781 emdvgtdeee etakestaek del
//
LOCUS       NP_115909                305 aa            linear   PRI 27-APR-2025
DEFINITION  N-acetylglucosamine-1-phosphotransferase subunit gamma precursor
            [Homo sapiens].
ACCESSION   NP_115909
VERSION     NP_115909.1
DBSOURCE    REFSEQ: accession NM_032520.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Di Lorenzo,G., Westermann,L.M., Yorgan,T.A., Sturznickel,J.,
            Ludwig,N.F., Ammer,L.S., Baranowsky,A., Ahmadi,S.,
            Pourbarkhordariesfandabadi,E., Breyer,S.R., Board,T.N., Foster,A.,
            Mercer,J., Tylee,K., Velho,R.V., Schweizer,M., Renne,T.,
            Braulke,T., Randon,D.N., Sperb-Ludwig,F., de Camargo Pinto,L.L.,
            Moreno,C.A., Cavalcanti,D.P., Amling,M., Kutsche,K., Winter,D.,
            Muschol,N.M., Schwartz,I.V.D., Rolvien,T., Danyukova,T., Schinke,T.
            and Pohl,S.
  TITLE     Pathogenic variants in GNPTAB and GNPTG encoding distinct subunits
            of GlcNAc-1-phosphotransferase differentially impact bone
            resorption in patients with mucolipidosis type II and III
  JOURNAL   Genet Med 23 (12), 2369-2377 (2021)
   PUBMED   34341521
  REMARK    GeneRIF: Pathogenic variants in GNPTAB and GNPTG encoding distinct
            subunits of GlcNAc-1-phosphotransferase differentially impact bone
            resorption in patients with mucolipidosis type II and III.
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Tiede,S., Hundt,J.E. and Paus,R.
  TITLE     UDP-GlcNAc-1-Phosphotransferase Is a Clinically Important Regulator
            of Human and Mouse Hair Pigmentation
  JOURNAL   J Invest Dermatol 141 (12), 2957-2965 (2021)
   PUBMED   34116066
  REMARK    GeneRIF: UDP-GlcNAc-1-Phosphotransferase Is a Clinically Important
            Regulator of Human and Mouse Hair Pigmentation.
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Dogan,M., Eroz,R., Terali,K., Gezdirici,A. and Bolu,S.
  TITLE     Clinical, radiological and computational studies on two novel GNPTG
            variants causing mucolipidosis III gamma phenotypes with varying
            severity
  JOURNAL   Mol Biol Rep 48 (2), 1465-1474 (2021)
   PUBMED   33507475
  REMARK    GeneRIF: Clinical, radiological and computational studies on two
            novel GNPTG variants causing mucolipidosis III gamma phenotypes
            with varying severity.
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Pasumarthi,D., Gupta,N., Sheth,J., Jain,S.J.M.N., Rungsung,I.,
            Kabra,M., Ranganath,P., Aggarwal,S., Phadke,S.R., Girisha,K.M.,
            Shukla,A., Datar,C., Verma,I.C., Puri,R.D., Bhavsar,R., Mistry,M.,
            Sankar,V.H., Gowrishankar,K., Agrawal,D., Nair,M., Danda,S.,
            Soni,J.P. and Dalal,A.
  TITLE     Identification and characterization of 30 novel pathogenic
            variations in 69 unrelated Indian patients with Mucolipidosis Type
            II and Type III
  JOURNAL   J Hum Genet 65 (11), 971-984 (2020)
   PUBMED   32651481
  REMARK    GeneRIF: Identification and characterization of 30 novel pathogenic
            variations in 69 unrelated Indian patients with Mucolipidosis Type
            II and Type III.
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Persichetti,E., Chuzhanova,N.A., Dardis,A., Tappino,B., Pohl,S.,
            Thomas,N.S., Rosano,C., Balducci,C., Paciotti,S., Dominissini,S.,
            Montalvo,A.L., Sibilio,M., Parini,R., Rigoldi,M., Di Rocco,M.,
            Parenti,G., Orlacchio,A., Bembi,B., Cooper,D.N., Filocamo,M. and
            Beccari,T.
  TITLE     Identification and molecular characterization of six novel
            mutations in the UDP-N-acetylglucosamine-1-phosphotransferase gamma
            subunit (GNPTG) gene in patients with mucolipidosis III gamma
  JOURNAL   Hum Mutat 30 (6), 978-984 (2009)
   PUBMED   19370764
  REMARK    GeneRIF: The mutational spectrum of the GNPTG gene is strongly
            influenced by the properties of the local DNA sequence environment.
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   7  (residues 1 to 305)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 305)
  AUTHORS   Raas-Rothschild,A., Cormier-Daire,V., Bao,M., Genin,E., Salomon,R.,
            Brewer,K., Zeigler,M., Mandel,H., Toth,S., Roe,B., Munnich,A. and
            Canfield,W.M.
  TITLE     Molecular basis of variant pseudo-hurler polydystrophy
            (mucolipidosis IIIC)
  JOURNAL   J Clin Invest 105 (5), 673-681 (2000)
   PUBMED   10712439
REFERENCE   9  (residues 1 to 305)
  AUTHORS   Raas-Rothschild,A. and Spiegel,R.
  TITLE     Mucolipidosis III Gamma
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301784
REFERENCE   10 (residues 1 to 305)
  AUTHORS   Ben-Yoseph,Y., Potier,M., Pack,B.A., Mitchell,D.A., Melancon,S.B.
            and Nadler,H.L.
  TITLE     Molecular size of N-acetylglucosaminylphosphotransferase and
            alpha-N-acetylglucosaminyl phosphodiesterase as determined in situ
            in Golgi membranes by radiation inactivation
  JOURNAL   Biochem J 235 (3), 883-886 (1986)
   PUBMED   3019310
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DT219524.1, BC014592.1,
            AK312067.1, AY203933.1 and AL031709.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the gamma sunbunit of the
            N-acetylglucosamine-1-phosphotransferase complex. This hexameric
            complex, composed of alpha, beta and gamma subunits, catalyzes the
            first step in synthesis of a mannose 6-phosphate lysosomal
            recognition marker. This enzyme complex is necessary for targeting
            of lysosomal hydrolases to the lysosome. Mutations in the gene
            encoding the gamma subunit have been associated with mucolipidosis
            IIIC, also known as mucolipidosis III gamma.[provided by RefSeq,
            Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK312067.1, SRR1660803.200444.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000204679.9/ ENSP00000204679.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..305
                     /product="N-acetylglucosamine-1-phosphotransferase subunit
                     gamma precursor"
                     /note="UDP-N-acetylglucosamine-1-phosphotransferase
                     subunit gamma; glcNAc-1-phosphotransferase subunit gamma;
                     N-acetylglucosamine-1-phosphate transferase gamma subunit"
                     /calculated_mol_wt=31830
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2162
     Region          69..129
                     /region_name="PRKCSH"
                     /note="Glucosidase II beta subunit-like protein;
                     pfam07915"
                     /db_xref="CDD:400321"
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9UJJ9.1)"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:15532026; propagated from
                     UniProtKB/Swiss-Prot (Q9UJJ9.1)"
     Region          267..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJJ9.1)"
     CDS             1..305
                     /gene="GNPTG"
                     /gene_synonym="C16orf27; GNPTAG; LP2537; RJD9"
                     /coded_by="NM_032520.5:36..953"
                     /db_xref="CCDS:CCDS10436.1"
                     /db_xref="GeneID:84572"
                     /db_xref="HGNC:HGNC:23026"
                     /db_xref="MIM:607838"
ORIGIN      
        1 maaglarlll llglsaggpa pagaakmkvv eepnafgvnn pflpqasrlq akrdpspvsg
       61 pvhlfrlsgk cfslvestyk yefcpfhnvt qheqtfrwna ysgilgiwhe weianntftg
      121 mwmrdgdacr srsrqskvel acgksnrlah vsepstcvya ltfetplvch phallvyptl
      181 pealqrqwdq veqdladeli tpqghekllr tlfedagylk tpeeneptql eggpdslgfe
      241 tlencrkahk elskeikrlk glltqhgipy trptetsnle hlghetprak speqlrgdpg
      301 lrgsl
//
LOCUS       NP_055282                465 aa            linear   PRI 27-APR-2025
DEFINITION  sushi repeat-containing protein SRPX2 precursor [Homo sapiens].
ACCESSION   NP_055282
VERSION     NP_055282.1
DBSOURCE    REFSEQ: accession NM_014467.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Guo,H., Liu,R., Wu,J., Li,S., Yao,W., Xu,J., Zheng,C., Lu,Y. and
            Zhang,H.
  TITLE     SRPX2 promotes cancer cell proliferation and migration of papillary
            thyroid cancer
  JOURNAL   Clin Exp Med 23 (8), 4825-4834 (2023)
   PUBMED   37306872
  REMARK    GeneRIF: SRPX2 promotes cancer cell proliferation and migration of
            papillary thyroid cancer.
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Wang,Q., Liu,J., Hu,Y., Pan,T., Xu,Y., Yu,J., Xiong,W., Zhou,Q. and
            Wang,Y.
  TITLE     Local administration of liposomal-based Srpx2 gene therapy reverses
            pulmonary fibrosis by blockading fibroblast-to-myofibroblast
            transition
  JOURNAL   Theranostics 11 (14), 7110-7125 (2021)
   PUBMED   34093874
  REMARK    GeneRIF: Local administration of liposomal-based Srpx2 gene therapy
            reverses pulmonary fibrosis by blockading
            fibroblast-to-myofibroblast transition.
            Erratum:[Theranostics. 2022 Jul 8;12(12):5330-5331. doi:
            10.7150/thno.74512. PMID: 35910799]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Li,X., Liu,J., Sun,H., Zou,Y., Chen,J., Chen,Y., Chen,C. and Wu,X.
  TITLE     SRPX2 promotes cell proliferation and invasion via activating
            FAK/SRC/ERK pathway in non-small cell lung cancer
  JOURNAL   Acta Biochim Pol 67 (2), 165-172 (2020)
   PUBMED   32550700
  REMARK    GeneRIF: SRPX2 promotes cell proliferation and invasion via
            activating FAK/SRC/ERK pathway in non-small cell lung cancer.
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Sasahira,T., Kurihara-Shimomura,M., Nishiguchi,Y., Shimomura,H. and
            Kirita,T.
  TITLE     Sushi Repeat Containing Protein X-linked 2 Is a Downstream Signal
            of LEM Domain Containing 1 and Acts as a Tumor-Promoting Factor in
            Oral Squamous Cell Carcinoma
  JOURNAL   Int J Mol Sci 21 (10), 3655 (2020)
   PUBMED   32455867
  REMARK    GeneRIF: Sushi Repeat Containing Protein X-linked 2 Is a Downstream
            Signal of LEM Domain Containing 1 and Acts as a Tumor-Promoting
            Factor in Oral Squamous Cell Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 465)
  AUTHORS   He,F., Wang,H., Li,Y., Liu,W., Gao,X., Chen,D., Wang,Q. and Shi,G.
  TITLE     SRPX2 knockdown inhibits cell proliferation and metastasis and
            promotes chemosensitivity in esophageal squamous cell carcinoma
  JOURNAL   Biomed Pharmacother 109, 671-678 (2019)
   PUBMED   30551519
  REMARK    GeneRIF: Knockdown of SRPX2 inhibits cell proliferation and
            metastasis, and promotes chemosensitivity in esophageal squamous
            cell carcinoma cells.
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Royer,B., Soares,D.C., Barlow,P.N., Bontrop,R.E., Roll,P.,
            Robaglia-Schlupp,A., Blancher,A., Levasseur,A., Cau,P.,
            Pontarotti,P. and Szepetowski,P.
  TITLE     Molecular evolution of the human SRPX2 gene that causes brain
            disorders of the Rolandic and Sylvian speech areas
  JOURNAL   BMC Genet 8, 72 (2007)
   PUBMED   17942002
  REMARK    GeneRIF: The R75K human-specific variation occurred in an important
            functional loop of the first sushi domain of SRPX2, indicating that
            this evolutionary mutation may have functional importance
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Roll,P., Rudolf,G., Pereira,S., Royer,B., Scheffer,I.E.,
            Massacrier,A., Valenti,M.P., Roeckel-Trevisiol,N., Jamali,S.,
            Beclin,C., Seegmuller,C., Metz-Lutz,M.N., Lemainque,A.,
            Delepine,M., Caloustian,C., de Saint Martin,A., Bruneau,N.,
            Depetris,D., Mattei,M.G., Flori,E., Robaglia-Schlupp,A., Levy,N.,
            Neubauer,B.A., Ravid,R., Marescaux,C., Berkovic,S.F., Hirsch,E.,
            Lathrop,M., Cau,P. and Szepetowski,P.
  TITLE     SRPX2 mutations in disorders of language cortex and cognition
  JOURNAL   Hum Mol Genet 15 (7), 1195-1207 (2006)
   PUBMED   16497722
  REMARK    GeneRIF: The involvement of SRPX2 in these disorders suggests an
            important role for SRPX2 in the perisylvian region critical for
            language and cognitive development.
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Villard,L., Nguyen,K., Cardoso,C., Martin,C.L., Weiss,A.M.,
            Sifry-Platt,M., Grix,A.W., Graham,J.M. Jr., Winter,R.M.,
            Leventer,R.J. and Dobyns,W.B.
  TITLE     A locus for bilateral perisylvian polymicrogyria maps to Xq28
  JOURNAL   Am J Hum Genet 70 (4), 1003-1008 (2002)
   PUBMED   11822025
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Kurosawa,H., Goi,K., Inukai,T., Inaba,T., Chang,K.S., Shinjyo,T.,
            Rakestraw,K.M., Naeve,C.W. and Look,A.T.
  TITLE     Two candidate downstream target genes for E2A-HLF
  JOURNAL   Blood 93 (1), 321-332 (1999)
   PUBMED   9864177
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Arlotta,P., Santori,L. and de Vecchi,A.
  TITLE     [A case of mixed tumor of the palate]
  JOURNAL   Acta Biol Med Ger 2 (3), 34 (1976)
   PUBMED   209648
  REMARK    GeneRIF: The SRPX2 protein contains the P-DUDES structural domain
            in its C-terminal region. This domain has significant albeit remote
            sequence similarity to thioredoxin-like domains, and is predicted
            to possess an oxidoreductase function.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL035608.11 and AL390040.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a secreted protein that contains three
            sushi repeat motifs. The encoded protein may play a role in the
            development of speech and language centers in the brain. This
            protein may also be involved in angiogenesis. Mutations in this
            gene are the cause of bilateral perisylvian polymicrogyria,
            rolandic epilepsy, speech dyspraxia and cognitive disability.
            [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.201156.1,
                                           SRR5189664.175439.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373004.5/ ENSP00000362095.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..465
                     /product="sushi repeat-containing protein SRPX2 precursor"
                     /note="sushi-repeat protein up-regulated in leukemia;
                     sushi repeat-containing protein SRPX2; sushi-repeat
                     protein upregulated in leukemia"
                     /calculated_mol_wt=50467
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2523
     Region          72..114
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Region          122..177
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(132,150)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          177..259
                     /region_name="HYR"
                     /note="HYR domain; pfam02494"
                     /db_xref="CDD:460572"
     Region          264..319
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(274,293)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          334..453
                     /region_name="DUF4174"
                     /note="Domain of unknown function (DUF4174); pfam13778"
                     /db_xref="CDD:463980"
     CDS             1..465
                     /gene="SRPX2"
                     /gene_synonym="BPP; CBPS; PMGX; RESDX; SRPUL"
                     /coded_by="NM_014467.3:448..1845"
                     /db_xref="CCDS:CCDS14471.1"
                     /db_xref="GeneID:27286"
                     /db_xref="HGNC:HGNC:30668"
                     /db_xref="MIM:300642"
ORIGIN      
        1 masqltqrga lfllffltpa vtptwyagsg yypdesynev yaeevpqapa ldyrvprwcy
       61 tlniqdgeat cyspkggnyh sslgtrcels cdrgfrligr rsvqclpsrr wsgtaycrqm
      121 rchalpfits gtytctngvl ldsrcdyscs sgyhlegdrs ricmedgrws ggepvcvdid
      181 ppkircphsr ekmaepeklt arvywdpplv kdsadgtitr vtlrgpepgs hfpegehvir
      241 ytaydraynr asckfivkvq vrrcptlkpp qhgyltctsa gdnygatcey hcdggydrqg
      301 tpsrvcqssr qwsgsppica pmkinvnvns aaglldqfye kqrlliisap dpsnryykmq
      361 ismlqqstcg ldlrhvtiie lvgqppqevg rireqqlsan iieelrqfqr ltrsyfnmvl
      421 idkqgidrdr ymepvtpeei ftfiddylls nqeltqrreq rdice
//
LOCUS       NP_004302                182 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-ribosylation factor-like protein 3 [Homo sapiens].
ACCESSION   NP_004302
VERSION     NP_004302.1
DBSOURCE    REFSEQ: accession NM_004311.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Zhang,X., Yao,S., Zhang,L., Yang,L., Yang,M., Guo,Q., Li,Y.,
            Wang,Z., Lei,B. and Jin,X.
  TITLE     Mechanisms underlying morphological and functional changes of cilia
            in fibroblasts derived from patients bearing ARL3T31A and
            ARL3T31A/C118F mutations
  JOURNAL   FASEB J 38 (5), e23519 (2024)
   PUBMED   38457249
  REMARK    GeneRIF: Mechanisms underlying morphological and functional changes
            of cilia in fibroblasts derived from patients bearing ARL3[T31A]
            and ARL3[T31A/C118F] mutations.
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Travis,A.M. and Pearring,J.N.
  TITLE     Human Mutations in Arl3, a Small GTPase Involved in Lipidated Cargo
            Delivery to the Cilia, Cause Retinal Dystrophy
  JOURNAL   Adv Exp Med Biol 1415, 283-288 (2023)
   PUBMED   37440046
  REMARK    GeneRIF: Human Mutations in Arl3, a Small GTPase Involved in
            Lipidated Cargo Delivery to the Cilia, Cause Retinal Dystrophy.
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Khrenova,M.G., Bulavko,E.S., Mulashkin,F.D. and Nemukhin,A.V.
  TITLE     Mechanism of Guanosine Triphosphate Hydrolysis by the Visual
            Proteins Arl3-RP2: Free Energy Reaction Profiles Computed with Ab
            Initio Type QM/MM Potentials
  JOURNAL   Molecules 26 (13), 3998 (2021)
   PUBMED   34208932
  REMARK    GeneRIF: Mechanism of Guanosine Triphosphate Hydrolysis by the
            Visual Proteins Arl3-RP2: Free Energy Reaction Profiles Computed
            with Ab Initio Type QM/MM Potentials.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Linari,M., Hanzal-Bayer,M. and Becker,J.
  TITLE     The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE
            delta, interacts with the Arf-like protein Arl3 in a GTP specific
            manner
  JOURNAL   FEBS Lett 458 (1), 55-59 (1999)
   PUBMED   10518933
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Kim,H.S.
  TITLE     Assignment of the human ADP-ribosylation factor-like 3 (ARL3) gene
            to chromosome 10 band q23.3 by radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 83 (3-4), 246 (1998)
   PUBMED   10072593
REFERENCE   8  (residues 1 to 182)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   9  (residues 1 to 182)
  AUTHORS   Cavenagh,M.M., Breiner,M., Schurmann,A., Rosenwald,A.G., Terui,T.,
            Zhang,C., Randazzo,P.A., Adams,M., Joost,H.G. and Kahn,R.A.
  TITLE     ADP-ribosylation factor (ARF)-like 3, a new member of the ARF
            family of GTP-binding proteins cloned from human and rat tissues
  JOURNAL   J Biol Chem 269 (29), 18937-18942 (1994)
   PUBMED   8034651
REFERENCE   10 (residues 1 to 182)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391121.29.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1149522.1,
                                           SRR3476690.185947.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260746.6/ ENSP00000260746.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..182
                     /product="ADP-ribosylation factor-like protein 3"
                     /note="ARF-like 3; ADP ribosylation factor like GTPase 3;
                     ADP-ribosylation factor-like 3"
                     /calculated_mol_wt=20324
     Region          3..176
                     /region_name="Arl3"
                     /note="Arf-like 3 (Arl3) GTPase; cd04155"
                     /db_xref="CDD:206721"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P36405.2)"
     Site            24..31
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206721"
     Site            order(26..27,31,35,47..54,76,81)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206721"
     Site            order(27..32,126..127,129..130,159..161)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206721"
     Site            36..51
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206721"
     Site            order(48..52,57,67,71,77,79..81)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206721"
     Site            48
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206721"
     Site            order(49..56,66,77,80..81)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206721"
     Site            order(52..58,61..66)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206721"
     Site            67..84
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206721"
     Site            67..70
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206721"
     Site            126..129
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206721"
     Site            159..161
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206721"
     CDS             1..182
                     /gene="ARL3"
                     /gene_synonym="ARFL3; JBTS35; RP83"
                     /coded_by="NM_004311.4:123..671"
                     /db_xref="CCDS:CCDS7538.1"
                     /db_xref="GeneID:403"
                     /db_xref="HGNC:HGNC:694"
                     /db_xref="MIM:604695"
ORIGIN      
        1 mgllsilrkl ksapdqevri lllgldnagk ttllkqlase dishitptqg fniksvqsqg
       61 fklnvwdigg qrkirpywkn yfentdiliy vidsadrkrf eetgqelael leeeklscvp
      121 vlifankqdl ltaapaseia eglnlhtird rvwqiqscsa ltgegvqdgm nwvcknvnak
      181 kk
//
LOCUS       NP_065170                369 aa            linear   PRI 27-APR-2025
DEFINITION  aspartate beta-hydroxylase domain-containing protein 2 [Homo
            sapiens].
ACCESSION   NP_065170
VERSION     NP_065170.2
DBSOURCE    REFSEQ: accession NM_020437.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99714.2 and AL161993.1.
            
            On Jul 19, 2008 this sequence version replaced NP_065170.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.261045.1,
                                           SRR1163658.167493.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215906.6/ ENSP00000215906.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.1"
     Protein         1..369
                     /product="aspartate beta-hydroxylase domain-containing
                     protein 2"
                     /calculated_mol_wt=41568
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ICH7.1)"
     Region          192..351
                     /region_name="Asp_Arg_Hydrox"
                     /note="Aspartyl/Asparaginyl beta-hydroxylase; pfam05118"
                     /db_xref="CDD:461552"
     Site            211
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6ICH7.1)"
     CDS             1..369
                     /gene="ASPHD2"
                     /coded_by="NM_020437.5:452..1561"
                     /db_xref="CCDS:CCDS13834.2"
                     /db_xref="GeneID:57168"
                     /db_xref="HGNC:HGNC:30437"
ORIGIN      
        1 mvwaplgppr tdcltllhtp skdspkmsle wlvawswsld glrdciatgi qsvrdcdtta
       61 vitvacllvl fvwycyhvgr eqprpyvsvn slmqaadang lqngyvycqs pecvrcthne
      121 glnqklyhnl qeyakrysws gmgrihkgir eqgrylnsrp siqkpevffl pdlpttpyfs
      181 rdaqkhdvev lernfqtilc efetlykafs ncslpqgwkm nstpsgewft fylvnqgvcv
      241 prncrkcprt yrllgslrtc ignnvfgnac isvlspgtvi tehygptnir irchlglktp
      301 ngcelvvgge pqcwaegrcl lfddsflhaa fhegsaedgp rvvfmvdlwh pnvaaaerqa
      361 ldfifapgr
//
LOCUS       NP_001346346             181 aa            linear   ROD 27-APR-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase alkB homolog 4 isoform 4
            [Mus musculus].
ACCESSION   NP_001346346
VERSION     NP_001346346.1
DBSOURCE    REFSEQ: accession NM_001359417.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Kweon,S.M., Chen,Y., Moon,E., Kvederaviciute,K., Klimasauskas,S.
            and Feldman,D.E.
  TITLE     An Adversarial DNA N6-Methyladenine-Sensor Network Preserves
            Polycomb Silencing
  JOURNAL   Mol Cell 74 (6), 1138-1147 (2019)
   PUBMED   30982744
  REMARK    GeneRIF: It has been shown that 6methyladenine (6 mA) deposition
            and removal are catalyzed by the Mettl4 methyltransferase and
            Alkbh4 dioxygenase, respectively, and that 6mA accumulation in
            genic elements corresponds with transcriptional silencing.
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Nilsen,A., Fusser,M., Greggains,G., Fedorcsak,P. and Klungland,A.
  TITLE     ALKBH4 depletion in mice leads to spermatogenic defects
  JOURNAL   PLoS One 9 (8), e105113 (2014)
   PUBMED   25153837
  REMARK    GeneRIF: ALKBH4 is essential for the development of spermatocytes
            during the prophase of meiosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Li,M.M., Nilsen,A., Shi,Y., Fusser,M., Ding,Y.H., Fu,Y., Liu,B.,
            Niu,Y., Wu,Y.S., Huang,C.M., Olofsson,M., Jin,K.X., Lv,Y., Xu,X.Z.,
            He,C., Dong,M.Q., Rendtlew Danielsen,J.M., Klungland,A. and
            Yang,Y.G.
  TITLE     ALKBH4-dependent demethylation of actin regulates actomyosin
            dynamics
  JOURNAL   Nat Commun 4, 1832 (2013)
   PUBMED   23673617
  REMARK    GeneRIF: ALKBH4-dependent actin demethylation regulates actomyosin
            function by promoting actin-non-muscle myosin II interaction.
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Lee,D.H., Jin,S.G., Cai,S., Chen,Y., Pfeifer,G.P. and O'Connor,T.R.
  TITLE     Repair of methylation damage in DNA and RNA by mammalian AlkB
            homologues
  JOURNAL   J Biol Chem 280 (47), 39448-39459 (2005)
   PUBMED   16174769
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Garcia-Frigola,C., Burgaya,F., Calbet,M., Lopez-Domenech,G., de
            Lecea,L. and Soriano,E.
  TITLE     A collection of cDNAs enriched in upper cortical layers of the
            embryonic mouse brain
  JOURNAL   Brain Res Mol Brain Res 122 (2), 133-150 (2004)
   PUBMED   15010206
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Phillips,R.L., Ernst,R.E., Brunk,B., Ivanova,N., Mahan,M.A.,
            Deanehan,J.K., Moore,K.A., Overton,G.C. and Lemischka,I.R.
  TITLE     The genetic program of hematopoietic stem cells
  JOURNAL   Science 288 (5471), 1635-1640 (2000)
   PUBMED   10834841
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087420.4 and BU698033.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence compared to variant 3. The resulting isoform (4) is
            shorter at the N-terminus compared to isoform 3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.2574021.1, BU698033.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849377, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 75.82 cM"
     Protein         1..181
                     /product="alpha-ketoglutarate-dependent dioxygenase alkB
                     homolog 4 isoform 4"
                     /EC_number="1.14.11.51"
                     /note="alkylated DNA repair protein alkB homolog 4;
                     probable alpha-ketoglutarate-dependent dioxygenase ABH4;
                     alpha-ketoglutarate-dependent dioxygenase alkB homolog 4;
                     alkB, alkylation repair homolog 4; lysine-specific
                     demethylase ALKBH4; DNA N6-methyl adenine demethylase
                     ALKBH4"
                     /calculated_mol_wt=19753
     CDS             1..181
                     /gene="Alkbh4"
                     /gene_synonym="2010004B12Rik; Abj4"
                     /coded_by="NM_001359417.1:416..961"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:72041"
                     /db_xref="MGI:MGI:1919291"
ORIGIN      
        1 magfqglpgf sqkvvqrmgl ypgledfqpv eqcnldyspe rgsaidphld dawlwgerlv
       61 slnllsatvv smspeapgsl llcsapsvrp dafedslvap srsvpcqeve vaitvprrsl
      121 lvltgaarhq wthaihrrhi karrvcatfr elsseflpgg kqqelgqell qaalsfqgrp
      181 v
//
LOCUS       NP_001352515             836 aa            linear   PRI 27-APR-2025
DEFINITION  neuroligin-4, Y-linked isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001352515 XP_011529728
VERSION     NP_001352515.1
DBSOURCE    REFSEQ: accession NM_001365586.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Nguyen,T.A., Wu,K., Pandey,S., Lehr,A.W., Li,Y., Bemben,M.A.,
            Badger,J.D. 2nd, Lauzon,J.L., Wang,T., Zaghloul,K.A., Thurm,A.,
            Jain,M., Lu,W. and Roche,K.W.
  TITLE     A Cluster of Autism-Associated Variants on X-Linked NLGN4X
            Functionally Resemble NLGN4Y
  JOURNAL   Neuron 106 (5), 759-768 (2020)
   PUBMED   32243781
  REMARK    GeneRIF: A Cluster of Autism-Associated Variants on X-Linked NLGN4X
            Functionally Resemble NLGN4Y.
REFERENCE   2  (residues 1 to 836)
  AUTHORS   Bogaert,A.F., Skorska,M.N., Wang,C., Gabrie,J., MacNeil,A.J.,
            Hoffarth,M.R., VanderLaan,D.P., Zucker,K.J. and Blanchard,R.
  TITLE     Male homosexuality and maternal immune responsivity to the Y-linked
            protein NLGN4Y
  JOURNAL   Proc Natl Acad Sci U S A 115 (2), 302-306 (2018)
   PUBMED   29229842
  REMARK    GeneRIF: Results suggest an association between a maternal immune
            response to neuroligin 4 Y-linked (NLGN4Y) and subsequent sexual
            orientation in male offspring.
            Erratum:[Proc Natl Acad Sci U S A. 2022 Aug 23;119(34):e2212767119.
            doi: 10.1073/pnas.2212767119. PMID: 35981140]
REFERENCE   3  (residues 1 to 836)
  AUTHORS   Gong,Y., Wang,L., Chippada-Venkata,U., Dai,X., Oh,W.K. and Zhu,J.
  TITLE     Constructing Bayesian networks by integrating gene expression and
            copy number data identifies NLGN4Y as a novel regulator of prostate
            cancer progression
  JOURNAL   Oncotarget 7 (42), 68688-68707 (2016)
   PUBMED   27626693
  REMARK    GeneRIF: Results suggest that NLGN4Y is an important negative
            regulator in prostate cancer progression.
REFERENCE   4  (residues 1 to 836)
  AUTHORS   Ross,J.L., Tartaglia,N., Merry,D.E., Dalva,M. and Zinn,A.R.
  TITLE     Behavioral phenotypes in males with XYY and possible role of
            increased NLGN4Y expression in autism features
  JOURNAL   Genes Brain Behav 14 (2), 137-144 (2015)
   PUBMED   25558953
  REMARK    GeneRIF: Expression of NLGN4Y, a gene that may be involved in
            synaptic function, is increased in boys with XYY
REFERENCE   5  (residues 1 to 836)
  AUTHORS   Dinamarca,M.C., Weinstein,D., Monasterio,O. and Inestrosa,N.C.
  TITLE     The synaptic protein neuroligin-1 interacts with the amyloid
            beta-peptide. Is there a role in Alzheimer's disease?
  JOURNAL   Biochemistry 50 (38), 8127-8137 (2011)
   PUBMED   21838267
REFERENCE   6  (residues 1 to 836)
  AUTHORS   Yamakawa,H., Oyama,S., Mitsuhashi,H., Sasagawa,N., Uchino,S.,
            Kohsaka,S. and Ishiura,S.
  TITLE     Neuroligins 3 and 4X interact with syntrophin-gamma2, and the
            interactions are affected by autism-related mutations
  JOURNAL   Biochem Biophys Res Commun 355 (1), 41-46 (2007)
   PUBMED   17292328
REFERENCE   7  (residues 1 to 836)
  AUTHORS   Ylisaukko-oja,T., Rehnstrom,K., Auranen,M., Vanhala,R., Alen,R.,
            Kempas,E., Ellonen,P., Turunen,J.A., Makkonen,I., Riikonen,R.,
            Nieminen-von Wendt,T., von Wendt,L., Peltonen,L. and Jarvela,I.
  TITLE     Analysis of four neuroligin genes as candidates for autism
  JOURNAL   Eur J Hum Genet 13 (12), 1285-1292 (2005)
   PUBMED   16077734
  REMARK    GeneRIF: Neuroligin mutations most probably represent rare causes
            of autism; it is unlikely that the allelic variants in any of these
            genes would be major risk factors for autism.
REFERENCE   8  (residues 1 to 836)
  AUTHORS   Skaletsky,H., Kuroda-Kawaguchi,T., Minx,P.J., Cordum,H.S.,
            Hillier,L., Brown,L.G., Repping,S., Pyntikova,T., Ali,J., Bieri,T.,
            Chinwalla,A., Delehaunty,A., Delehaunty,K., Du,H., Fewell,G.,
            Fulton,L., Fulton,R., Graves,T., Hou,S.F., Latrielle,P.,
            Leonard,S., Mardis,E., Maupin,R., McPherson,J., Miner,T., Nash,W.,
            Nguyen,C., Ozersky,P., Pepin,K., Rock,S., Rohlfing,T., Scott,K.,
            Schultz,B., Strong,C., Tin-Wollam,A., Yang,S.P., Waterston,R.H.,
            Wilson,R.K., Rozen,S. and Page,D.C.
  TITLE     The male-specific region of the human Y chromosome is a mosaic of
            discrete sequence classes
  JOURNAL   Nature 423 (6942), 825-837 (2003)
   PUBMED   12815422
REFERENCE   9  (residues 1 to 836)
  AUTHORS   Jamain,S., Quach,H., Betancur,C., Rastam,M., Colineaux,C.,
            Gillberg,I.C., Soderstrom,H., Giros,B., Leboyer,M., Gillberg,C. and
            Bourgeron,T.
  CONSRTM   Paris Autism Research International Sibpair Study
  TITLE     Mutations of the X-linked genes encoding neuroligins NLGN3 and
            NLGN4 are associated with autism
  JOURNAL   Nat Genet 34 (1), 27-29 (2003)
   PUBMED   12669065
REFERENCE   10 (residues 1 to 836)
  AUTHORS   Cantallops,I. and Cline,H.T.
  TITLE     Synapse formation: if it looks like a duck and quacks like a duck
            ...
  JOURNAL   Curr Biol 10 (17), R620-R623 (2000)
   PUBMED   10996085
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010726.4, AC010979.3,
            AC010879.2 and AC011903.4.
            
            On Sep 5, 2018 this sequence version replaced XP_011529728.1.
            
            Summary: This gene encodes a type I membrane protein that belongs
            to the family of neuroligins, which are cell adhesion molecules
            present at the postsynaptic side of the synapse, and may be
            essential for the formation of functional synapses. Alternatively
            spliced transcript variants have been found for this gene.[provided
            by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.28801.1,
                                           SRR1803611.128498.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..836
                     /product="neuroligin-4, Y-linked isoform 4 precursor"
                     /note="alternative HNL4Y"
                     /calculated_mol_wt=89576
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4646
     Region          44..610
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            order(194..196,273..275,278,419,425..426,464,510,513)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(274,395,509)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     CDS             1..836
                     /gene="NLGN4Y"
                     /gene_synonym="HNL4Y"
                     /coded_by="NM_001365586.1:438..2948"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 7"
                     /db_xref="CCDS:CCDS94714.1"
                     /db_xref="GeneID:22829"
                     /db_xref="HGNC:HGNC:15529"
                     /db_xref="MIM:400028"
ORIGIN      
        1 mlrpqgllwl pllftsvcvm lnsnvllwit alaikftlid sqaqypvvnt nygkiqglrt
       61 plpseilgpv eqylgvpyas pptgerrfqp pespsswtgi rnatqfsavc pqhlderfll
      121 hdmlpiwftt sldtlmtyvq dqnedclyln iyvpmedgtn ikrnaddits ndhgedkdih
      181 eqnskkpvmv yihggsymeg tgnmidgsil asygnvivit inyrlgilgf lstgdqaakg
      241 nyglldqiqa lrwieenvga fggdpkrvti fgsgagascv slltlshyse glfqkaiiqs
      301 gtalsswavn yqpakytril adkvgcnmld ttdmveclkn knykeliqqt itpatyhiaf
      361 gpvidgdvip ddpqilmeqg eflnydimlg vnqgeglkfv dgivdnedgv tpndfdfsvs
      421 nfvdnlygyp egkdtlreti kfmytdwadk enpetrrktl valftdhqwv apavatadlh
      481 aqygsptyfy afyhhcqsem kpswadsahg devpyvfgip migptelfsc nfskndvmls
      541 avvmtywtnf aktgdpnqpv pqdtkfihtk pnrfeevaws kynpkdqlyl higlkprvrd
      601 hyratkvafw lelvphlhnl neifqyvstt tkvpppdmts fpygtrrspa kiwpttkrpa
      661 itpannpkhs kdphktgped ttvlietkrd ystelsvtia vgasllflni lafaalyykk
      721 dkrrhethrh pspqrnttnd ithiqneeim slqmkqlehd heceslqahd tlrltcppdy
      781 tltlrrspdd ipfmtpntit mipntlmgmq plhtfktfsg gqnstnlphg hsttrv
//
LOCUS       NP_001095940             375 aa            linear   PRI 27-APR-2025
DEFINITION  alcohol dehydrogenase 6 isoform 1 [Homo sapiens].
ACCESSION   NP_001095940
VERSION     NP_001095940.1
DBSOURCE    REFSEQ: accession NM_001102470.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ostberg,L.J., Persson,B. and Hoog,J.O.
  TITLE     Computational studies of human class V alcohol dehydrogenase - the
            odd sibling
  JOURNAL   BMC Biochem 17 (1), 16 (2016)
   PUBMED   27455956
  REMARK    GeneRIF: Local structural differences between human class V ADH and
            other human ADHs includes a for class V ADH unique and conserved
            Lys51, a position directly involved in the catalytic mechanism in
            other ADHs, and nine other class V ADH-specific residues.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Jeff,J.M., Ritchie,M.D., Denny,J.C., Kho,A.N., Ramirez,A.H.,
            Crosslin,D., Armstrong,L., Basford,M.A., Wolf,W.A., Pacheco,J.A.,
            Chisholm,R.L., Roden,D.M., Hayes,M.G. and Crawford,D.C.
  TITLE     Generalization of variants identified by genome-wide association
            studies for electrocardiographic traits in African Americans
  JOURNAL   Ann Hum Genet 77 (4), 321-332 (2013)
   PUBMED   23534349
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Zuo,L., Wang,K., Zhang,X.Y., Pan,X., Wang,G., Tan,Y., Zhong,C.,
            Krystal,J.H., State,M., Zhang,H. and Luo,X.
  TITLE     Association between common alcohol dehydrogenase gene (ADH)
            variants and schizophrenia and autism
  JOURNAL   Hum Genet 132 (7), 735-743 (2013)
   PUBMED   23468174
  REMARK    GeneRIF: common ADH variants conferred risk for both schizophrenia
            in African-Americans and autism in European-Americans.
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Park,B.L., Kim,J.W., Cheong,H.S., Kim,L.H., Lee,B.C., Seo,C.H.,
            Kang,T.C., Nam,Y.W., Kim,G.B., Shin,H.D. and Choi,I.G.
  TITLE     Extended genetic effects of ADH cluster genes on the risk of
            alcohol dependence: from GWAS to replication
  JOURNAL   Hum Genet 132 (6), 657-668 (2013)
   PUBMED   23456092
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Munoz,X., Amiano,P., Celorrio,D., Dorronsoro,M., Sanchez,M.J.,
            Huerta,J.M., Barricarte,A., Arriola,L., Navarro,C.,
            Molina-Montes,E., Chirlaque,M.D., Ardanaz,E., Rodriguez,L.,
            Duell,E.J., Hijona,E., Herreros-Villanueva,M., Sala,N. and
            Bujanda,L.
  TITLE     Association of alcohol dehydrogenase polymorphisms and life-style
            factors with excessive alcohol intake within the Spanish population
            (EPIC-Spain)
  JOURNAL   Addiction 107 (12), 2117-2127 (2012)
   PUBMED   22690706
  REMARK    GeneRIF: Results show that polymorphism of ADH6 gene leads to heavy
            drinking in women.
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Sun,H.W. and Plapp,B.V.
  TITLE     Progressive sequence alignment and molecular evolution of the
            Zn-containing alcohol dehydrogenase family
  JOURNAL   J Mol Evol 34 (6), 522-535 (1992)
   PUBMED   1593644
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Chen,C.S. and Yoshida,A.
  TITLE     Enzymatic properties of the protein encoded by newly cloned human
            alcohol dehydrogenase ADH6 gene
  JOURNAL   Biochem Biophys Res Commun 181 (2), 743-747 (1991)
   PUBMED   1755855
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Yasunami,M., Chen,C.S. and Yoshida,A.
  TITLE     A human alcohol dehydrogenase gene (ADH6) encoding an additional
            class of isozyme
  JOURNAL   Proc Natl Acad Sci U S A 88 (17), 7610-7614 (1991)
   PUBMED   1881901
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Lieber,C.S.
  TITLE     Interaction of ethanol with drugs, hepatotoxic agents, carcinogens
            and vitamins
  JOURNAL   Alcohol Alcohol 25 (2-3), 157-176 (1990)
   PUBMED   2198032
  REMARK    Review article
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Lange,L.G., Sytkowski,A.J. and Vallee,B.L.
  TITLE     Human liver alcohol dehydrogenase: purification, composition, and
            catalytic features
  JOURNAL   Biochemistry 15 (21), 4687-4693 (1976)
   PUBMED   9982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK092768.1, BC039065.1 and
            AP002026.2.
            
            Summary: This gene encodes class V alcohol dehydrogenase, which is
            a member of the alcohol dehydrogenase family. Members of this
            family metabolize a wide variety of substrates, including ethanol,
            retinol, other aliphatic alcohols, hydroxysteroids, and lipid
            peroxidation products. This gene is expressed in the stomach as
            well as in the liver, and it contains a glucocorticoid response
            element upstream of its 5' UTR, which is a steroid hormone receptor
            binding site. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK092768.1, SRR5189664.128750.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394899.6/ ENSP00000378359.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..375
                     /product="alcohol dehydrogenase 6 isoform 1"
                     /EC_number="1.1.1.1"
                     /note="aldehyde reductase"
                     /calculated_mol_wt=39684
     Region          3..375
                     /region_name="alcohol_DH_class_I_II_IV"
                     /note="class I, II, IV alcohol dehydrogenases; cd08299"
                     /db_xref="CDD:176259"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28332.3)"
     Site            order(47,69,175)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176259"
     Site            order(48..49,175,179,200..204,224..225,229,269..270,
                     274..275,293..294,318..320,370)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176259"
     Site            order(49,69,95,118,142,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176259"
     Site            order(99..100,102,105,113)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176259"
     Site            order(103..104,107,112,261..262,273,286..287,292..293,
                     301..306,309..319)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176259"
     CDS             1..375
                     /gene="ADH6"
                     /gene_synonym="ADH-5"
                     /coded_by="NM_001102470.2:95..1222"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43255.1"
                     /db_xref="GeneID:130"
                     /db_xref="HGNC:HGNC:255"
                     /db_xref="MIM:103735"
ORIGIN      
        1 msttgqvirc kaailwkpga pfsieeveva ppkakevrik vvatglcgte mkvlgskhld
       61 llyptilghe gagivesige gvstvkpgdk vitlflpqcg ectsclnseg nfciqfkqsk
      121 tqlmsdgtsr ftckgksiyh fgntstfcey tvikeisvak idavaplekv cliscgfstg
      181 fgaaintakv tpgstcavfg lggvglsvvm gckaagaari igvdvnkekf kkaqelgate
      241 clnpqdlkkp iqevlfdmtd agidfcfeai gnldvlaaal ascnesygvc vvvgvlpasv
      301 qlkisgqlff sgrslkgsvf ggwksrqhip klvadymaek lnldplitht lnldkineav
      361 elmktgkcir cilll
//
LOCUS       NP_659448                456 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 25 isoform b [Homo sapiens].
ACCESSION   NP_659448
VERSION     NP_659448.1
DBSOURCE    REFSEQ: accession NM_145011.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Twine,N.A., Harkness,L., Kassem,M. and Wilkins,M.R.
  TITLE     Transcription factor ZNF25 is associated with osteoblast
            differentiation of human skeletal stem cells
  JOURNAL   BMC Genomics 17 (1), 872 (2016)
   PUBMED   27814695
  REMARK    GeneRIF: This study shows that the uncharacterized transcription
            factor, ZNF25, is associated with differentiation of hMSC to
            osteoblasts.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Guy,J., Hearn,T., Crosier,M., Mudge,J., Viggiano,L., Koczan,D.,
            Thiesen,H.J., Bailey,J.A., Horvath,J.E., Eichler,E.E.,
            Earthrowl,M.E., Deloukas,P., French,L., Rogers,J., Bentley,D. and
            Jackson,M.S.
  TITLE     Genomic sequence and transcriptional profile of the boundary
            between pericentromeric satellites and genes on human chromosome
            arm 10p
  JOURNAL   Genome Res 13 (2), 159-172 (2003)
   PUBMED   12566394
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Guy,J., Spalluto,C., McMurray,A., Hearn,T., Crosier,M.,
            Viggiano,L., Miolla,V., Archidiacono,N., Rocchi,M., Scott,C.,
            Lee,P.A., Sulston,J., Rogers,J., Bentley,D. and Jackson,M.S.
  TITLE     Genomic sequence and transcriptional profile of the boundary
            between pericentromeric satellites and genes on human chromosome
            arm 10q
  JOURNAL   Hum Mol Genet 9 (13), 2029-2042 (2000)
   PUBMED   10942432
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Tunnacliffe,A., Liu,L., Moore,J.K., Leversha,M.A., Jackson,M.S.,
            Papi,L., Ferguson-Smith,M.A., Thiesen,H.J. and Ponder,B.A.
  TITLE     Duplicated KOX zinc finger gene clusters flank the centromere of
            human chromosome 10: evidence for a pericentric inversion during
            primate evolution
  JOURNAL   Nucleic Acids Res 21 (6), 1409-1417 (1993)
   PUBMED   8464732
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Rousseau-Merck,M.F., Tunnacliffe,A., Berger,R., Ponder,B.A. and
            Thiesen,H.J.
  TITLE     A cluster of expressed zinc finger protein genes in the
            pericentromeric region of human chromosome 10
  JOURNAL   Genomics 13 (3), 845-848 (1992)
   PUBMED   1639412
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP229986.1 and AL117337.26.
            
            Transcript Variant: This variant (4) encodes isoform b, as do
            variants 5-9.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.96318.1,
                                           SRR1660803.32271.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302609.8/ ENSP00000302222.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p11.21"
     Protein         1..456
                     /product="zinc finger protein 25 isoform b"
                     /note="zinc finger protein 25 (KOX 19); zinc finger
                     protein KOX19"
                     /calculated_mol_wt=53414
     Region          8..68
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          120..140
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          144..453
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          148..168
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          176..196
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          204..224
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          232..252
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          260..280
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(265,267,269,271..272,275..276,279,293,295,299..300,
                     303..304,307,321,323,325,327..328,331..332,335)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          288..308
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          316..336
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          344..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          400..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          428..448
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..456
                     /gene="ZNF25"
                     /gene_synonym="KOX19; Zfp9"
                     /coded_by="NM_145011.4:228..1598"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS7195.1"
                     /db_xref="GeneID:219749"
                     /db_xref="HGNC:HGNC:13043"
                     /db_xref="MIM:194528"
ORIGIN      
        1 mnkfqgpvtl kdviveftke ewklltpaqr tlykdvmlen yshlvsvgyh vnkpnavfkl
       61 kqgkepwile vefphrgfpe dlwsihdlea ryqesqagns rngeltkhqk thttekacec
      121 kecgkffcqk salivhqhth skgksydcdk cgksfskned lirhqkihtr dktyeckeck
      181 kifyhlssls rhlrthagek pyecnqceks fyqkphlteh qkthtgekpf ectecgkffy
      241 vkaylmvhqk thtgekpyec kecgkafsqk shltvhqrmh tgekpykcke cgkffsrnsh
      301 lkthqrshtg ekpyeckecr kcfyqksalt vhqrthtgek pfecnkcgkt fyyksdltkh
      361 qrkhtgekpy ectecgksfa vnsvlrlhqr thtgekpyac kecgksfsqk shfiihqrkh
      421 tgekpyecqe cgetfiqksq ltahqkthtk krnaek
//
LOCUS       NP_001352355             647 aa            linear   PRI 27-APR-2025
DEFINITION  conserved oligomeric Golgi complex subunit 4 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001352355 XP_011521283
VERSION     NP_001352355.1
DBSOURCE    REFSEQ: accession NM_001365426.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Ferreira,C.R., Niiler,T., Duker,A.L., Jackson,A.P. and Bober,M.B.
  TITLE     Growth in individuals with Saul-Wilson syndrome
  JOURNAL   Am J Med Genet A 182 (9), 2110-2116 (2020)
   PUBMED   32652690
  REMARK    GeneRIF: Growth in individuals with Saul-Wilson syndrome.
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Ferreira,C.R., Xia,Z.J., Clement,A., Parry,D.A., Davids,M.,
            Taylan,F., Sharma,P., Turgeon,C.T., Blanco-Sanchez,B., Ng,B.G.,
            Logan,C.V., Wolfe,L.A., Solomon,B.D., Cho,M.T., Douglas,G.,
            Carvalho,D.R., Bratke,H., Haug,M.G., Phillips,J.B., Wegner,J.,
            Tiemeyer,M., Aoki,K., Nordgren,A., Hammarsjo,A., Duker,A.L.,
            Rohena,L., Hove,H.B., Ek,J., Adams,D., Tifft,C.J., Onyekweli,T.,
            Weixel,T., Macnamara,E., Radtke,K., Powis,Z., Earl,D., Gabriel,M.,
            Russi,A.H.S., Brick,L., Kozenko,M., Tham,E., Raymond,K.M.,
            Phillips,J.A. 3rd, Tiller,G.E., Wilson,W.G., Hamid,R.,
            Malicdan,M.C.V., Nishimura,G., Grigelioniene,G., Jackson,A.,
            Westerfield,M., Bober,M.B., Gahl,W.A. and Freeze,H.H.
  CONSRTM   Undiagnosed Diseases Network; Scottish Genome Partnership
  TITLE     A Recurrent De Novo Heterozygous COG4 Substitution Leads to
            Saul-Wilson Syndrome, Disrupted Vesicular Trafficking, and Altered
            Proteoglycan Glycosylation
  JOURNAL   Am J Hum Genet 103 (4), 553-567 (2018)
   PUBMED   30290151
  REMARK    GeneRIF: A specific heterozygous COG4 substitution as the molecular
            basis of Saul-Wilson syndrome.
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   6  (residues 1 to 647)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Ferreira,C.
  TITLE     Saul-Wilson Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32078278
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106804.4.
            
            On Jan 26, 2019 this sequence version replaced XP_011521283.1.
            
            Summary: The protein encoded by this gene is a component of an
            oligomeric protein complex involved in the structure and function
            of the Golgi apparatus. Defects in this gene may be a cause of
            congenital disorder of glycosylation type IIj. Two transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.103057.1,
                                           SRR1803614.239512.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..647
                     /product="conserved oligomeric Golgi complex subunit 4
                     isoform 3"
                     /note="complexed with Dor1p; conserved oligomeric Golgi
                     complex protein 4; COG complex subunit 4"
                     /calculated_mol_wt=73651
     Region          50..359
                     /region_name="COG4"
                     /note="COG4 transport protein; pfam08318"
                     /db_xref="CDD:462425"
     CDS             1..647
                     /gene="COG4"
                     /gene_synonym="CDG2J; COD1; SWILS"
                     /coded_by="NM_001365426.1:611..2554"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:25839"
                     /db_xref="HGNC:HGNC:18620"
                     /db_xref="MIM:606976"
ORIGIN      
        1 mdgvqtalrs edyeqaaaht hrylcldksv ielsrqgkeg smidanlkll qeaeqrlkai
       61 vaekfaiatk egdlpqverf fkifpllglh eeglrkfsey lckqvaskae enllmvlgtd
      121 msdrraavif adtltllfeg iarivethqp ivetyygpgr lytlikylqv ecdrqvekvv
      181 dkfikqrdyh qqfrhvqnnl mrnsttekie preldpilte vtlmnarsel ylrflkkris
      241 sdfevgdsma seevkqehqk cldkllnncl lsctmqelig lyvtmeeyfm retvnkaval
      301 dtyekgqlts smvddvfyiv kkcigralss ssidclcami nlattelesd frdvlcnklr
      361 mgfpattfqd iqrgvtsavn imhsslqqgk fdtkgiestd eakmsflvtl nnvevcseni
      421 stlkktlesd ctklfsqgig geqaqakfds clsdlaavsn kfrdllqegl telnstaikp
      481 qvqpwinsff svshnieeee fndyeandpw vqqfilnleq qmaefkasls pviydsltgl
      541 mtslvavele kvvlkstfnr lgglqfdkel rsliaylttv ttwtirdkfa rlsqmatiln
      601 lervteildy wgpnsgpltw rltpaevrqv lalridfrse dikrlrl
//
LOCUS       NP_001349088             549 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 382 isoform 3 [Mus musculus].
ACCESSION   NP_001349088 XP_006539937
VERSION     NP_001349088.1
DBSOURCE    REFSEQ: accession NM_001362159.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Ma,L., Yu,L., Jiang,B.C., Wang,J., Guo,X., Huang,Y., Ren,J.,
            Sun,N., Gao,D.S., Ding,H., Lu,J., Zhou,H., Zou,L., Gao,Y., Wang,L.,
            Sun,K., Ming,Y., Meng,Z., Tao,Y.X. and Yan,M.
  TITLE     ZNF382 controls mouse neuropathic pain via silencer-based
            epigenetic inhibition of Cxcl13 in DRG neurons
  JOURNAL   J Exp Med 218 (12) (2021)
   PUBMED   34762123
  REMARK    GeneRIF: ZNF382 controls mouse neuropathic pain via silencer-based
            epigenetic inhibition of Cxcl13 in DRG neurons.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC164703.3.
            
            On Apr 6, 2018 this sequence version replaced XP_006539937.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.153093.1,
                                           SRR7345562.618328.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7"
     Protein         1..549
                     /product="zinc finger protein 382 isoform 3"
                     /note="KRAB/zinc finger suppressor protein 1; multiple
                     zinc finger and krueppel-associated box protein KS1"
                     /calculated_mol_wt=63208
     Region          12..72
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          273..289
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          295..317
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          297..317
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          325..345
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          353..373
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <381..532
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          381..401
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(386,388,390,392..393,396..397,400,414,416,420..421,
                     424..425,428,442,444,446,448..449,452..453,456)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          409..429
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          437..457
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          465..485
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          493..513
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          521..541
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..549
                     /gene="Zfp382"
                     /gene_synonym="4930428B01Rik; 5930415A09Rik; KS1; Znf382"
                     /coded_by="NM_001362159.1:221..1870"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:233060"
                     /db_xref="MGI:MGI:3588204"
ORIGIN      
        1 mnchtvplqg pvsfkdvtvd ftqeewqrld paqkalyrdv mlenychfis vgfhitkpdm
       61 irkleqgeel wterifpsqs yleeeevlvk fsdyqdkppk siviikhkkl ikerssvyge
      121 algknrvvsk tlfeyksdgk vlknisefis rdinpamgkl ggskewegsi ltskqekthp
      181 asilhkqigr alssewdlaq hqktqipeqr feynkcdssf lmtgvefphg rahrgggnfn
      241 yskdditlfe ksdlgihphd lmekkcssyn kygellcrks vfvmhpssqm derpfqcpyc
      301 gnsfrrksyl ieherihtge kpyiccqcgr afrqktaltl hekthtegkp ylcvdcgksf
      361 rqkatltrhh kahtgekaye ctqcgsafgk ksylidhqrt htgekpyqct ecgkafiqkt
      421 tltvhqrtht gekpyicsec gksfcqkttl tlhqrihtge kpyicsdcgk sfrqkailtv
      481 hyrihtgeks ngcpqcgkaf srksnlirhq kihtgekpye cqecgkffsc ksnlithqkt
      541 hktetmrfq
//
LOCUS       NP_001353654             266 aa            linear   PRI 27-APR-2025
DEFINITION  GTP-binding protein Rhes precursor [Homo sapiens].
ACCESSION   NP_001353654 XP_005261499
VERSION     NP_001353654.1
DBSOURCE    REFSEQ: accession NM_001366725.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Serra,M., Pinna,A., Costa,G., Usiello,A., Pasqualetti,M.,
            Avallone,L., Morelli,M. and Napolitano,F.
  TITLE     Involvement of the Protein Ras Homolog Enriched in the Striatum,
            Rhes, in Dopaminergic Neurons' Degeneration: Link to Parkinson's
            Disease
  JOURNAL   Int J Mol Sci 22 (10), 5326 (2021)
   PUBMED   34070217
  REMARK    GeneRIF: Involvement of the Protein Ras Homolog Enriched in the
            Striatum, Rhes, in Dopaminergic Neurons' Degeneration: Link to
            Parkinson's Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Carbo,M., Brandi,V., Pascarella,G., Staid,D.S., Colotti,G.,
            Polticelli,F., Ilari,A. and Morea,V.
  TITLE     Bioinformatics analysis of Ras homologue enriched in the striatum,
            a potential target for Huntington's disease therapy
  JOURNAL   Int J Mol Med 44 (6), 2223-2233 (2019)
   PUBMED   31638189
  REMARK    GeneRIF: These regions have been used to design peptides aimed at
            inhibiting RHES interactions and, therefore, mHtt sumoylation; in
            turn, these peptides will be used to develop small molecule
            inhibitors by both rational design and virtual screening of large
            compound libraries.
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Mizuno,H. and Taketomi,A.
  TITLE     MicroRNA-101 inhibits the expression of Rhes, a striatal-enriched
            small G-protein, at the post-transcriptional level in vitro
  JOURNAL   BMC Res Notes 11 (1), 528 (2018)
   PUBMED   30064488
  REMARK    GeneRIF: results support the hypothesis that Rhes expression is
            regulated by miRNA and indicate that miR-101 may be a potent
            modulator of Rhes expression in striatal neurons.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Vitucci,D., Di Giorgio,A., Napolitano,F., Pelosi,B., Blasi,G.,
            Errico,F., Attrotto,M.T., Gelao,B., Fazio,L., Taurisano,P., Di
            Maio,A., Marsili,V., Pasqualetti,M., Bertolino,A. and Usiello,A.
  TITLE     Rasd2 Modulates Prefronto-Striatal Phenotypes in Humans and
            'Schizophrenia-Like Behaviors' in Mice
  JOURNAL   Neuropsychopharmacology 41 (3), 916-927 (2016)
   PUBMED   26228524
  REMARK    GeneRIF: Study demonstrated that variation in the gene coding for
            RASD2 (rs6518956) affects in vivo prefrontal and striatal
            phenotypes in healthy human subjects that are relevant to
            schizophrenia
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Ghiglieri,V., Napolitano,F., Pelosi,B., Schepisi,C., Migliarini,S.,
            Di Maio,A., Pendolino,V., Mancini,M., Sciamanna,G., Vitucci,D.,
            Maddaloni,G., Giampa,C., Errico,F., Nistico,R., Pasqualetti,M.,
            Picconi,B. and Usiello,A.
  TITLE     Rhes influences striatal cAMP/PKA-dependent signaling and synaptic
            plasticity in a gender-sensitive fashion
  JOURNAL   Sci Rep 5, 10933 (2015)
   PUBMED   26190541
  REMARK    GeneRIF: Rhes influences striatal cAMP/PKA-dependent signaling and
            synaptic plasticity in a gender-sensitive fashion
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Agretti,P., De Marco,G., Pinchera,A., Vitti,P., Bernal,J. and
            Tonacchera,M.
  TITLE     Ras homolog enriched in striatum inhibits the functional activity
            of wild type thyrotropin, follicle-stimulating hormone, luteinizing
            hormone receptors and activating thyrotropin receptor mutations by
            altering their expression in COS-7 cells
  JOURNAL   J Endocrinol Invest 30 (4), 279-284 (2007)
   PUBMED   17556863
  REMARK    GeneRIF: Rhes can interfere with the functional activity of wt and
            mutated TSHr and with the respective hormone-stimulated cAMP
            production of FSHr and LHr.
REFERENCE   7  (residues 1 to 266)
  AUTHORS   Taylor,J.P., Jackson,D.A., Morgan,N.G. and Chan,S.L.
  TITLE     Rhes expression in pancreatic beta-cells is regulated by efaroxan
            in a calcium-dependent process
  JOURNAL   Biochem Biophys Res Commun 349 (2), 809-815 (2006)
   PUBMED   16945334
  REMARK    GeneRIF: Rhes is an imidazoline-regulated transcript in pancreatic
            beta-cells
REFERENCE   8  (residues 1 to 266)
  AUTHORS   Vargiu,P., De Abajo,R., Garcia-Ranea,J.A., Valencia,A.,
            Santisteban,P., Crespo,P. and Bernal,J.
  TITLE     The small GTP-binding protein, Rhes, regulates signal transduction
            from G protein-coupled receptors
  JOURNAL   Oncogene 23 (2), 559-568 (2004)
   PUBMED   14724584
REFERENCE   9  (residues 1 to 266)
  AUTHORS   Chan,S.L., Monks,L.K., Gao,H., Deaville,P. and Morgan,N.G.
  TITLE     Identification of the monomeric G-protein, Rhes, as an
            efaroxan-regulated protein in the pancreatic beta-cell
  JOURNAL   Br J Pharmacol 136 (1), 31-36 (2002)
   PUBMED   11976265
REFERENCE   10 (residues 1 to 266)
  AUTHORS   St Croix,B., Rago,C., Velculescu,V., Traverso,G., Romans,K.E.,
            Montgomery,E., Lal,A., Riggins,G.J., Lengauer,C., Vogelstein,B. and
            Kinzler,K.W.
  TITLE     Genes expressed in human tumor endothelium
  JOURNAL   Science 289 (5482), 1197-1202 (2000)
   PUBMED   10947988
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL022334.1.
            
            On Oct 17, 2018 this sequence version replaced XP_005261499.1.
            
            Summary: This gene belongs to the Ras superfamily of small GTPases
            and is enriched in the striatum. The encoded protein functions as
            an E3 ligase for attachment of small ubiquitin-like modifier
            (SUMO). This protein also binds to mutant huntingtin (mHtt), the
            protein mutated in Huntington disease (HD). Sumoylation of mHTT by
            this protein may cause degeneration of the striatum. The protein
            functions as an activator of mechanistic target of rapamycin 1
            (mTOR1), which in turn plays a role in myelination, axon growth and
            regeneration. Reduced levels of mRNA expressed by this gene were
            found in HD patients. [provided by RefSeq, Jan 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1315667.1,
                                           SRR1660803.195963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2151358
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..266
                     /product="GTP-binding protein Rhes precursor"
                     /EC_number="3.6.5.2"
                     /note="tumor endothelial marker 2; Ras homolog enriched in
                     striatum; GTP-binding protein Rhes"
                     /calculated_mol_wt=30235
     mat_peptide     1..263
                     /product="GTP-binding protein Rhes. /id=PRO_0000082720"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96D21.1)"
                     /calculated_mol_wt=30024
     Region          20..266
                     /region_name="Rhes_like"
                     /note="Ras homolog enriched in striatum (Rhes) and
                     activator of G-protein signaling 1 (Dexras1/AGS1);
                     cd04143"
                     /db_xref="CDD:133343"
     Site            26..33
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133343"
     Site            order(27..28,75..76)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133343"
     Site            order(28..34,73,76,140..141,143,172..173)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133343"
     Site            order(33..34,48,50,56..57,70..71,73,75..76,174)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133343"
     Region          48..56
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96D21.1)"
     Site            order(49..50,54..57)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133343"
     Site            49..56
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133343"
     Site            51
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133343"
     Site            73..76
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133343"
     Site            order(75..76,79..93)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133343"
     Site            140..143
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133343"
     Site            172..174
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133343"
     Region          189..235
                     /region_name="Interaction with GNB1, GNB2 and GNB3.
                     /evidence=ECO:0000269|PubMed:19255495"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96D21.1)"
     Site            263..266
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:133343"
     Site            263
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q96D21.1)"
     CDS             1..266
                     /gene="RASD2"
                     /gene_synonym="Rhes; TEM2"
                     /coded_by="NM_001366725.1:64..864"
                     /db_xref="CCDS:CCDS13916.1"
                     /db_xref="GeneID:23551"
                     /db_xref="HGNC:HGNC:18229"
                     /db_xref="MIM:612842"
ORIGIN      
        1 mmktlssgnc tlsvpaknsy rmvvlgasrv gkssivsrfl ngrfedqytp tiedfhrkvy
       61 nirgdmyqld ildtsgnhpf pamrrlsilt gdvfilvfsl dnresfdevk rlqkqilevk
      121 sclknktkea aelpmvicgn kndhgelcrq vptteaellv sgdencayfe vsakkntnvd
      181 emfyvlfsma klphemspal hrkisvqygd afhprpfcmr rvkemdaygm vspfarrpsv
      241 nsdlkyikak vlregqarer dkctiq
//
LOCUS       NP_001121700             711 aa            linear   PRI 27-APR-2025
DEFINITION  taperin [Homo sapiens].
ACCESSION   NP_001121700 XP_003403877
VERSION     NP_001121700.2
DBSOURCE    REFSEQ: accession NM_001128228.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Qi,J., Tan,F., Zhang,L., Zhou,Y., Zhang,Z., Sun,Q., Li,N., Fang,Y.,
            Chen,X., Wu,Y., Zhong,G. and Chai,R.
  TITLE     Critical role of TPRN rings in the stereocilia for hearing
  JOURNAL   Mol Ther 32 (1), 204-217 (2024)
   PUBMED   37952086
  REMARK    GeneRIF: Critical role of TPRN rings in the stereocilia for
            hearing.
            Erratum:[Mol Ther. 2025 Jan 8;33(1):419-420. doi:
            10.1016/j.ymthe.2024.12.004. PMID: 39672160]
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 711)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 711)
  AUTHORS   Ferrar,T., Chamousset,D., De Wever,V., Nimick,M., Andersen,J.,
            Trinkle-Mulcahy,L. and Moorhead,G.B.
  TITLE     Taperin (c9orf75), a mutated gene in nonsyndromic deafness, encodes
            a vertebrate specific, nuclear localized protein phosphatase one
            alpha (PP1alpha) docking protein
  JOURNAL   Biol Open 1 (2), 128-139 (2012)
   PUBMED   23213405
REFERENCE   6  (residues 1 to 711)
  AUTHORS   Esteves,S.L., Domingues,S.C., da Cruz e Silva,O.A., Fardilha,M. and
            da Cruz e Silva,E.F.
  TITLE     Protein phosphatase 1alpha interacting proteins in the human brain
  JOURNAL   OMICS 16 (1-2), 3-17 (2012)
   PUBMED   22321011
REFERENCE   7  (residues 1 to 711)
  AUTHORS   Rehman,A.U., Morell,R.J., Belyantseva,I.A., Khan,S.Y., Boger,E.T.,
            Shahzad,M., Ahmed,Z.M., Riazuddin,S., Khan,S.N., Riazuddin,S. and
            Friedman,T.B.
  TITLE     Targeted capture and next-generation sequencing identifies C9orf75,
            encoding taperin, as the mutated gene in nonsyndromic deafness
            DFNB79
  JOURNAL   Am J Hum Genet 86 (3), 378-388 (2010)
   PUBMED   20170899
  REMARK    GeneRIF: Targeted capture and next-generation sequencing identifies
            C9orf75, encoding taperin, as the mutated gene in nonsyndromic
            deafness DFNB79
REFERENCE   8  (residues 1 to 711)
  AUTHORS   Li,Y., Pohl,E., Boulouiz,R., Schraders,M., Nurnberg,G., Charif,M.,
            Admiraal,R.J., von Ameln,S., Baessmann,I., Kandil,M., Veltman,J.A.,
            Nurnberg,P., Kubisch,C., Barakat,A., Kremer,H. and Wollnik,B.
  TITLE     Mutations in TPRN cause a progressive form of autosomal-recessive
            nonsyndromic hearing loss
  JOURNAL   Am J Hum Genet 86 (3), 479-484 (2010)
   PUBMED   20170898
  REMARK    GeneRIF: genome-wide homozygosity mapping in a Moroccan family;
            mapped autosomal-recessive nonsyndromic hearing loss to DFNB79
            locus on chromosome 9q34; identified a causative homozygous 11 bp
            deletion, c.42_52del, in TPRN gene in affected individuals
REFERENCE   9  (residues 1 to 711)
  AUTHORS   Khan,S.Y., Riazuddin,S., Shahzad,M., Ahmed,N., Zafar,A.U.,
            Rehman,A.U., Morell,R.J., Griffith,A.J., Ahmed,Z.M., Riazuddin,S.
            and Friedman,T.B.
  TITLE     DFNB79: reincarnation of a nonsyndromic deafness locus on
            chromosome 9q34.3
  JOURNAL   Eur J Hum Genet 18 (1), 125-129 (2010)
   PUBMED   19603065
REFERENCE   10 (residues 1 to 711)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL929554.20 and BC098411.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Aug 3, 2011 this sequence version replaced
            XP_003403877.1, NP_001121700.1.
            
            Summary: This locus encodes a sensory epithelial protein. It was
            defined by linkage analysis in three Pakistani families to lie
            between D9S1818 (centromeric) and D9SH6 (telomeric). Mutations at
            this locus have been associated with autosomal recessive deafness.
            [provided by RefSeq, Oct 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by mouse NM_175286.4 and supporting mouse transcripts.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC111500.1, BC098411.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409012.6/ ENSP00000387100.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..711
                     /product="taperin"
                     /calculated_mol_wt=75425
     Region          8..87
                     /region_name="Phostensin_N"
                     /note="PP1-regulatory protein, Phostensin N-terminal;
                     pfam13916"
                     /db_xref="CDD:464039"
     Region          134..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     Region          <238..473
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     Region          328..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     Region          414..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AI08; propagated from
                     UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AI08; propagated from
                     UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     Region          467..592
                     /region_name="Phostensin"
                     /note="Phostensin PP1-binding and SH3-binding region;
                     pfam13914"
                     /db_xref="CDD:464038"
     Region          500..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     Region          572..630
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     Region          642..662
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     Region          674..711
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KMQ1.2)"
     CDS             1..711
                     /gene="TPRN"
                     /gene_synonym="C9orf75; DFNB79"
                     /coded_by="NM_001128228.3:31..2166"
                     /db_xref="CCDS:CCDS56594.1"
                     /db_xref="GeneID:286262"
                     /db_xref="HGNC:HGNC:26894"
                     /db_xref="MIM:613354"
ORIGIN      
        1 maalgrpgsg praavpawkr eilerkrakl aalgggagpg aaepeqrvla eslgplrenp
       61 fmlleaerrr gggaagarll eryrrvpgvr alradsvlii etvpgfppap papgaaqira
      121 aevlvygapp grvsrllerf dppaaprrrg sperarpppp ppppapprpp paapsppaap
      181 gprgggaspg arrsdflqkt gsnsftvhpr glhrgagarl lsnghsapep ragpanrlag
      241 sppgsgqwkp kvesgdpslh pppspgtpsa tpasppasat psqrqcvsaa tstndsfeir
      301 papkpvmeti plgdlqaral aslransrns fmvipkskas gapppegrqs velpkgdlgp
      361 aspsqelgsq pvpggdgapa lgksplevea qwaveegacp rtataladra irwqrpsspp
      421 pflpaaseea epaeglrvpg laknsreyvr pglpvtfide vdseeapqaa klpylphpar
      481 plhparpgcv aelqprgsnt ftvvpkrkpg tlqdqhfsqa nreprpreae eeeascllgp
      541 tlkkryptvh eieviggyla lqkscltkag ssrkkmkisf ndkslqttfe ypsessleqe
      601 eevdqqeeee eeeeeeeeee egsgseekpf alflpratfv ssvrpessrl pegssglssy
      661 tpkhsvafsk wqeqaleqap reaepppvea mltpasqndl sdfrsepaly f
//
LOCUS       NP_689419                406 aa            linear   PRI 27-APR-2025
DEFINITION  sorting nexin-6 isoform b [Homo sapiens].
ACCESSION   NP_689419
VERSION     NP_689419.3
DBSOURCE    REFSEQ: accession NM_152233.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Ghosh,C., Xing,Y., Li,S., Hoyle,R.G., Sun,M., Li,J. and Sun,Y.
  TITLE     Sorting nexin 6 interacts with Cullin3 and regulates programmed
            death ligand 1 expression
  JOURNAL   FEBS Lett 595 (20), 2558-2569 (2021)
   PUBMED   34510437
  REMARK    GeneRIF: Sorting nexin 6 interacts with Cullin3 and regulates
            programmed death ligand 1 expression.
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Camargo,L.M., Collura,V., Rain,J.C., Mizuguchi,K., Hermjakob,H.,
            Kerrien,S., Bonnert,T.P., Whiting,P.J. and Brandon,N.J.
  TITLE     Disrupted in Schizophrenia 1 Interactome: evidence for the close
            connectivity of risk genes and a potential synaptic basis for
            schizophrenia
  JOURNAL   Mol Psychiatry 12 (1), 74-86 (2007)
   PUBMED   17043677
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Ishibashi,Y., Maita,H., Yano,M., Koike,N., Tamai,K., Ariga,H. and
            Iguchi-Ariga,S.M.
  TITLE     Pim-1 translocates sorting nexin 6/TRAF4-associated factor 2 from
            cytoplasm to nucleus
  JOURNAL   FEBS Lett 506 (1), 33-38 (2001)
   PUBMED   11591366
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Parks,W.T., Frank,D.B., Huff,C., Renfrew Haft,C., Martin,J.,
            Meng,X., de Caestecker,M.P., McNally,J.G., Reddi,A., Taylor,S.I.,
            Roberts,A.B., Wang,T. and Lechleider,R.J.
  TITLE     Sorting nexin 6, a novel SNX, interacts with the transforming
            growth factor-beta family of receptor serine-threonine kinases
  JOURNAL   J Biol Chem 276 (22), 19332-19339 (2001)
   PUBMED   11279102
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Wurthner,J.U., Frank,D.B., Felici,A., Green,H.M., Cao,Z.,
            Schneider,M.D., McNally,J.G., Lechleider,R.J. and Roberts,A.B.
  TITLE     Transforming growth factor-beta receptor-associated protein 1 is a
            Smad4 chaperone
  JOURNAL   J Biol Chem 276 (22), 19495-19502 (2001)
   PUBMED   11278302
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB021488.1, U83194.1,
            BI870378.1, AF121856.2, AK124315.1 and AI446034.1.
            
            On Oct 10, 2018 this sequence version replaced NP_689419.2.
            
            Summary: This gene encodes a member of the sorting nexin family.
            Members of this family contain a phox (PX) domain, which is a
            phosphoinositide binding domain, and are involved in intracellular
            trafficking. This protein associates with the long isoform of the
            leptin receptor, the transforming growth factor-beta family of
            receptor serine-threonine kinases, and with receptor tyrosine
            kinases for platelet-derived growth factor, insulin, and epidermal
            growth factor. This protein may form oligomeric complexes with
            family member proteins through interactions of both the PX domain
            and the coiled coil regions of the molecules. Translocation of this
            protein from the cytoplasm to the nucleus occurs after binding to
            proviral integration site 1 protein. This gene results in two
            transcripts encoding two distinct isoforms. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (2) encodes the longest isoform
            (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.119176.1,
                                           SRR1803617.10341.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000362031.10/ ENSP00000355217.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..406
                     /product="sorting nexin-6 isoform b"
                     /note="tumor necrosis factor receptor-associated factor
                     4(TRAF4)-associated factor 2; TRAF4-associated factor 2"
                     /calculated_mol_wt=46518
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Region          2..179
                     /region_name="Interaction with PIM1.
                     /evidence=ECO:0000269|PubMed:11591366"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in Sorting nexin-6,
                     N-terminally processed.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Region          30..170
                     /region_name="PX_SNX6"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 6; cd07292"
                     /db_xref="CDD:132825"
     Site            order(69..71,96..97,140)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:132825"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Region          182..199
                     /region_name="Membrane-binding amphipathic helix.
                     /evidence=ECO:0000303|PubMed:23085988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Region          186..403
                     /region_name="BAR_SNX6"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Sorting
                     Nexin 6; cd07662"
                     /db_xref="CDD:153346"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Site            order(216,219..220,223..224,226..227,230,233..234,237,
                     244..245,247..248,251,254..255,258..259,274,363,366..367,
                     369..371,374,377..378,380..382,384..385,388..389,391..392,
                     395..396,398..399)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153346"
     CDS             1..406
                     /gene="SNX6"
                     /gene_synonym="MSTP010; TFAF2"
                     /coded_by="NM_152233.4:33..1253"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41942.2"
                     /db_xref="GeneID:58533"
                     /db_xref="HGNC:HGNC:14970"
                     /db_xref="MIM:606098"
ORIGIN      
        1 mmeglddgpd flseedrglk ainvdlqsda alqvdisdal serdkvkftv htksslpnfk
       61 qnefsvvrqh eefiwlhdsf venedyagyi ippapprpdf dasreklqkl gegegsmtke
      121 eftkmkqele aeylaifkkt vamhevflcr vaahpilrrd lnfhvfleyn qdlsvrgknk
      181 kekledffkn mvksadgviv sgvkdvddff ehertflley hnrvkdasak sdrmtrshks
      241 aaddynrigs slyalgtqds tdickfflkv selfdktrki earvsadedl klsdllkyyl
      301 resqaakdll yrrsrslvdy enankaldka raknkdvlqa etsqqlccqk fekisesakq
      361 elidfktrrv aafrknlvel aelelkhakg nlqllqncla vlngdt
//
LOCUS       NP_003000                 87 aa            linear   PRI 27-APR-2025
DEFINITION  selenoprotein W [Homo sapiens].
ACCESSION   NP_003000
VERSION     NP_003000.1
DBSOURCE    REFSEQ: accession NM_003009.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Miao,Z., Wang,W., Miao,Z., Cao,Q. and Xu,S.
  TITLE     Role of Selenoprotein W in participating in the progression of
            non-alcoholic fatty liver disease
  JOURNAL   Redox Biol 71, 103114 (2024)
   PUBMED   38460355
  REMARK    GeneRIF: Role of Selenoprotein W in participating in the
            progression of non-alcoholic fatty liver disease.
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Kim,H., Oh,J., Kim,M.K., Lee,K.H. and Jeong,D.
  TITLE     Selenoprotein W engages in overactive osteoclast differentiation in
            multiple myeloma
  JOURNAL   Mol Biol Rep 51 (1), 587 (2024)
   PUBMED   38683225
  REMARK    GeneRIF: Selenoprotein W engages in overactive osteoclast
            differentiation in multiple myeloma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Chen,P., Wang,C., Liu,Q., Tian,J. and Liu,Q.
  TITLE     Identification of FAM96B as a novel selenoprotein W binding partner
            in the brain
  JOURNAL   Biochem Biophys Res Commun 512 (1), 137-143 (2019)
   PUBMED   30876693
  REMARK    GeneRIF: We performed a yeast two-hybrid screen on a human fetal
            brain cDNA library and identified FAM96B as a novel binding partner
            of SelW. FRET analyses confirmed the interaction between SelW' and
            FAM96B.
REFERENCE   4  (residues 1 to 87)
  AUTHORS   Tan,L., Mai,D., Zhang,B., Jiang,X., Zhang,J., Bai,R., Ye,Y., Li,M.,
            Pan,L., Su,J., Zheng,Y., Liu,Z., Zuo,Z., Zhao,Q., Li,X., Huang,X.,
            Yang,J., Tan,W., Zheng,J. and Lin,D.
  TITLE     PIWI-interacting RNA-36712 restrains breast cancer progression and
            chemoresistance by interaction with SEPW1 pseudogene SEPW1P RNA
  JOURNAL   Mol Cancer 18 (1), 9 (2019)
   PUBMED   30636640
  REMARK    GeneRIF: Functional studies demonstrated that piRNA-36,712
            interacts with RNAs produced by SEPW1P, a retroprocessed pseudogene
            of SEPW1, and subsequently inhibits SEPW1 expression through
            competition of SEPW1 mRNA with SEPW1P RNA for microRNA-7 and
            microRNA-324.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 87)
  AUTHORS   Bellingham,J., Gregory-Evans,K., Fox,M.F. and Gregory-Evans,C.Y.
  TITLE     Gene structure and tissue expression of human selenoprotein W,
            SEPW1, and identification of a retroprocessed pseudogene, SEPW1P
  JOURNAL   Biochim Biophys Acta 1627 (2-3), 140-146 (2003)
   PUBMED   12818432
  REMARK    GeneRIF: The gene lacks canonical TATA and CAAT boxes, but has
            numerous Sp1 consensus binding sites upstream of multiple
            transcription start sites. SEPW1 is expressed in all of the 22
            tissues assayed, and shows highest expression in skeletal muscle
            and heart.
REFERENCE   6  (residues 1 to 87)
  AUTHORS   Kryukov,G.V., Castellano,S., Novoselov,S.V., Lobanov,A.V.,
            Zehtab,O., Guigo,R. and Gladyshev,V.N.
  TITLE     Characterization of mammalian selenoproteomes
  JOURNAL   Science 300 (5624), 1439-1443 (2003)
   PUBMED   12775843
REFERENCE   7  (residues 1 to 87)
  AUTHORS   Whanger,P.D.
  TITLE     Selenoprotein W: a review
  JOURNAL   Cell Mol Life Sci 57 (13-14), 1846-1852 (2000)
   PUBMED   11215511
  REMARK    Review article
REFERENCE   8  (residues 1 to 87)
  AUTHORS   Smith,J.S., Tachibana,I., Pohl,U., Lee,H.K., Thanarajasingam,U.,
            Portier,B.P., Ueki,K., Ramaswamy,S., Billings,S.J.,
            Mohrenweiser,H.W., Louis,D.N. and Jenkins,R.B.
  TITLE     A transcript map of the chromosome 19q-arm glioma tumor suppressor
            region
  JOURNAL   Genomics 64 (1), 44-50 (2000)
   PUBMED   10708517
REFERENCE   9  (residues 1 to 87)
  AUTHORS   Gu,Q.P., Beilstein,M.A., Vendeland,S.C., Lugade,A., Ream,W. and
            Whanger,P.D.
  TITLE     Conserved features of selenocysteine insertion sequence (SECIS)
            elements in selenoprotein W cDNAs from five species
  JOURNAL   Gene 193 (2), 187-196 (1997)
   PUBMED   9256076
REFERENCE   10 (residues 1 to 87)
  AUTHORS   Yeh,J.Y., Beilstein,M.A., Andrews,J.S. and Whanger,P.D.
  TITLE     Tissue distribution and influence of selenium status on levels of
            selenoprotein W
  JOURNAL   FASEB J 9 (5), 392-396 (1995)
   PUBMED   7896009
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CR991097.1, BC039597.1 and
            AC008745.7.
            
            Summary: This gene encodes a selenoprotein containing a
            selenocysteine (Sec) residue, which is encoded by the UGA codon
            that normally signals translation termination. The 3' UTRs of
            selenoprotein mRNAs contain a conserved stem-loop structure, the
            Sec insertion sequence (SECIS) element that is necessary for the
            recognition of UGA as a Sec codon rather than as a stop signal.
            This protein is highly expressed in skeletal muscle, heart and
            brain. It belongs to the SelWTH family, which possesses a
            thioredoxin-like fold and a conserved CxxU (C is cysteine, U is
            Sec) motif, suggesting a redox function for this gene. Studies in
            mouse show that this selenoprotein is involved in muscle growth and
            differentiation, and in the protection of neurons from oxidative
            stress during neuronal development. A retroprocessed pseudogene of
            this locus has been identified on chromosome 1. [provided by
            RefSeq, Aug 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.162141.1,
                                           SRR5189652.186262.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: community standard
                                                (PMID:9256076)
            MANE Ensembl match               :: ENST00000601048.6/
                                                ENSP00000473185.1
            protein contains selenocysteine  :: PMID: 12818432
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..87
                     /product="selenoprotein W"
                     /note="selenoprotein W, 1"
                     /calculated_mol_wt=9317
     Region          5..78
                     /region_name="CXXU_selWTH"
                     /note="selT/selW/selH selenoprotein domain; TIGR02174"
                     /db_xref="CDD:274013"
     Site            13
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..87
                     /gene="SELENOW"
                     /gene_synonym="selW; SEPW1"
                     /coded_by="NM_003009.4:84..347"
                     /note="UGA stop codon recoded as selenocysteine"
                     /db_xref="CCDS:CCDS59402.1"
                     /db_xref="GeneID:6415"
                     /db_xref="HGNC:HGNC:10752"
                     /db_xref="MIM:603235"
ORIGIN      
        1 malavrvvyc gaugykskyl qlkkkledef pgrldicgeg tpqatgffev mvagklihsk
       61 kkgdgyvdte skflklvaai kaalaqg
//
LOCUS       NP_001352783             262 aa            linear   PRI 27-APR-2025
DEFINITION  OX-2 membrane glycoprotein isoform f precursor [Homo sapiens].
ACCESSION   NP_001352783 XP_016861945
VERSION     NP_001352783.1
DBSOURCE    REFSEQ: accession NM_001365854.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wedig,J., Jasani,S., Mukherjee,D., Lathrop,H., Matreja,P., Pfau,T.,
            D'Alesio,L., Guenther,A., Fenn,L., Kaiser,M., Torok,M.A., McGue,J.,
            Sizemore,G.M., Noonan,A.M., Dillhoff,M.E., Blaser,B.W.,
            Frankel,T.L., Culp,S., Hart,P.A., Cruz-Monserrate,Z. and Mace,T.A.
  TITLE     CD200 is overexpressed in the pancreatic tumor microenvironment and
            predictive of overall survival
  JOURNAL   Cancer Immunol Immunother 73 (6), 96 (2024)
   PUBMED   38619621
  REMARK    GeneRIF: CD200 is overexpressed in the pancreatic tumor
            microenvironment and predictive of overall survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Gonzalez-Montes,Y., Osca-Gelis,G., Rodriguez-Romanos,R.,
            Villavicencio,A., Gonzalez-Bartulos,M., Llopis,F., Clapes,V.,
            Oriol,A., Sureda,A., Escoda,L., Sarra,J., Garzo,A., Lloveras,N.,
            Gomez,B., Granada,I. and Gallardo,D.
  TITLE     CD200 genotype is associated with clinical outcome of patients with
            multiple myeloma
  JOURNAL   Front Immunol 15, 1252445 (2024)
   PUBMED   38455039
  REMARK    GeneRIF: CD200 genotype is associated with clinical outcome of
            patients with multiple myeloma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Tang,Y., Liu,W., Kadu,S., Johnson,O., Hasanali,Z.S., Kelly,A.,
            Shestov,A., Pajarillo,R., Greenblatt,E., Holmes,M., Wang,L.P.,
            Shih,N., O'Connor,R.S., Ruella,M., Garfall,A.L., Allman,D.,
            Vogl,D.T., Cohen,A., June,C.H. and Sheppard,N.C.
  TITLE     Exploiting the CD200-CD200R immune checkpoint axis in multiple
            myeloma to enhance CAR T-cell therapy
  JOURNAL   Blood 143 (2), 139-151 (2024)
   PUBMED   37616575
  REMARK    GeneRIF: Exploiting the CD200-CD200R immune checkpoint axis in
            multiple myeloma to enhance CAR T-cell therapy.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Zhang,M., Qian,X.H., Hu,J., Zhang,Y., Lin,X., Hai,W., Shi,K.,
            Jiang,X., Li,Y., Tang,H.D. and Li,B.
  TITLE     Integrating TSPO PET imaging and transcriptomics to unveil the role
            of neuroinflammation and amyloid-beta deposition in Alzheimer's
            disease
  JOURNAL   Eur J Nucl Med Mol Imaging 51 (2), 455-467 (2024)
   PUBMED   37801139
  REMARK    GeneRIF: Integrating TSPO PET imaging and transcriptomics to unveil
            the role of neuroinflammation and amyloid-beta deposition in
            Alzheimer's disease.
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Moon,S.Y., Han,M., Ryu,G., Shin,S.A., Lee,J.H. and Lee,C.S.
  TITLE     Emerging Immune Checkpoint Molecules on Cancer Cells: CD24 and
            CD200
  JOURNAL   Int J Mol Sci 24 (20), 15072 (2023)
   PUBMED   37894750
  REMARK    GeneRIF: Emerging Immune Checkpoint Molecules on Cancer Cells: CD24
            and CD200.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Chen,Z., Marsden,P.A. and Gorczynski,R.M.
  TITLE     Cloning and characterization of the human CD200 promoter region
  JOURNAL   Mol Immunol 43 (6), 579-587 (2006)
   PUBMED   15955564
  REMARK    GeneRIF: revealed a 169 bp region responsible for constitutive
            expression of CD200; positive regulatory domains were identified in
            the core promoter; and documented evidence for C/EBPbeta as being
            important in transcriptional regulation of CD200
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Preston,S., Wright,G.J., Starr,K., Barclay,A.N. and Brown,M.H.
  TITLE     The leukocyte/neuron cell surface antigen OX2 binds to a ligand on
            macrophages
  JOURNAL   Eur J Immunol 27 (8), 1911-1918 (1997)
   PUBMED   9295026
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Douglas,J., Albertson,D.G., Barclay,A.N., Davis,M. and
            Rabbitts,P.H.
  TITLE     RFLP and mapping of human MOX-1 gene on chromosome 3
  JOURNAL   Nucleic Acids Res 16 (18), 9067 (1988)
   PUBMED   2902568
REFERENCE   9  (residues 1 to 262)
  AUTHORS   McCaughan,G.W., Clark,M.J., Hurst,J., Grosveld,F. and Barclay,A.N.
  TITLE     The gene for MRC OX-2 membrane glycoprotein is localized on human
            chromosome 3
  JOURNAL   Immunogenetics 25 (2), 133-135 (1987)
   PUBMED   3817906
REFERENCE   10 (residues 1 to 262)
  AUTHORS   McCaughan,G.W., Clark,M.J. and Barclay,A.N.
  TITLE     Characterization of the human homolog of the rat MRC OX-2 membrane
            glycoprotein
  JOURNAL   Immunogenetics 25 (5), 329-335 (1987)
   PUBMED   3032785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112487.3.
            
            On Sep 20, 2018 this sequence version replaced XP_016861945.1.
            
            Summary: This gene encodes a type I membrane glycoprotein
            containing two extracellular immunoglobulin domains, a
            transmembrane and a cytoplasmic domain. This gene is expressed by
            various cell types, including B cells, a subset of T cells,
            thymocytes, endothelial cells, and neurons. The encoded protein
            plays an important role in immunosuppression and regulation of
            anti-tumor activity. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.168812.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.2"
     Protein         1..262
                     /product="OX-2 membrane glycoprotein isoform f precursor"
                     /note="CD200 antigen; antigen identified by monoclonal
                     antibody MRC OX-2; OX-2 membrane glycoprotein"
                     /calculated_mol_wt=26924
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2527
     Region          25..132
                     /region_name="IgV_1_MRC-OX-2_like"
                     /note="First immunoglobulin (Ig) variable (V) domain of
                     rat MRC OX-2 antigen, and similar domains; cd05846"
                     /db_xref="CDD:409433"
     Region          25..45
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409433"
     Region          25..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409433"
     Region          31..35
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409433"
     Region          38..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409433"
     Region          46..52
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409433"
     Region          53..62
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409433"
     Region          54..60
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409433"
     Region          63..80
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409433"
     Region          63..71
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409433"
     Region          76..80
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409433"
     Region          86..116
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409433"
     Region          86..93
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409433"
     Region          96..102
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409433"
     Region          110..117
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409433"
     Region          117..123
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409433"
     Region          123..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409433"
     Region          124..132
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409433"
     Region          <152..223
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          162..166
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          190..194
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          204..209
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          219..222
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..262
                     /gene="CD200"
                     /gene_synonym="MOX1; MOX2; MRC; OX-2"
                     /coded_by="NM_001365854.1:214..1002"
                     /note="isoform f precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:4345"
                     /db_xref="HGNC:HGNC:7203"
                     /db_xref="MIM:155970"
ORIGIN      
        1 mpfshlstys lvwvmaavvl ctaqvqvvtq dereqlytpa slkcslqnaq ealivtwqkk
       61 kavspenmvt fsenhgvviq paykdkinit qlglqnstit fwnitledeg cymclfntfg
      121 fgkisgtacl tvyvqpivsl hykfsedhln itcsatarpa pmvfwkvprs gienstvtls
      181 hpngttsvts ilhikdpknq vgkevicqvl hlgtvtdfkq tvnkgywfsv plllsivslv
      241 illvlisill ywkrhrnqdr ep
//
LOCUS       NP_001356683             141 aa            linear   PRI 27-APR-2025
DEFINITION  ATP synthase F(0) complex subunit C2, mitochondrial isoform c
            precursor [Homo sapiens].
ACCESSION   NP_001356683
VERSION     NP_001356683.1
DBSOURCE    REFSEQ: accession NM_001369754.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Tebbenkamp,A.T.N., Varela,L., Choi,J., Paredes,M.I., Giani,A.M.,
            Song,J.E., Sestan-Pesa,M., Franjic,D., Sousa,A.M.M., Liu,Z.W.,
            Li,M., Bichsel,C., Koch,M., Szigeti-Buck,K., Liu,F., Li,Z.,
            Kawasawa,Y.I., Paspalas,C.D., Mineur,Y.S., Prontera,P., Merla,G.,
            Picciotto,M.R., Arnsten,A.F.T., Horvath,T.L. and Sestan,N.
  TITLE     The 7q11.23 Protein DNAJC30 Interacts with ATP Synthase and Links
            Mitochondria to Brain Development
  JOURNAL   Cell 175 (4), 1088-1104 (2018)
   PUBMED   30318146
REFERENCE   3  (residues 1 to 141)
  AUTHORS   He,J., Ford,H.C., Carroll,J., Ding,S., Fearnley,I.M. and
            Walker,J.E.
  TITLE     Persistence of the mitochondrial permeability transition in the
            absence of subunit c of human ATP synthase
  JOURNAL   Proc Natl Acad Sci U S A 114 (13), 3409-3414 (2017)
   PUBMED   28289229
  REMARK    GeneRIF: ATP5G1, ATP5G2, and ATP5G3 of the ATP synthase are not
            involved in forming the permeability transition pore.
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Fujikawa,M., Sugawara,K., Tanabe,T. and Yoshida,M.
  TITLE     Assembly of human mitochondrial ATP synthase through two separate
            intermediates, F1-c-ring and b-e-g complex
  JOURNAL   FEBS Lett 589 (19 Pt B), 2707-2712 (2015)
   PUBMED   26297831
REFERENCE   5  (residues 1 to 141)
  AUTHORS   He,M., Xu,M., Zhang,B., Liang,J., Chen,P., Lee,J.Y., Johnson,T.A.,
            Li,H., Yang,X., Dai,J., Liang,L., Gui,L., Qi,Q., Huang,J., Li,Y.,
            Adair,L.S., Aung,T., Cai,Q., Cheng,C.Y., Cho,M.C., Cho,Y.S.,
            Chu,M., Cui,B., Gao,Y.T., Go,M.J., Gu,D., Gu,W., Guo,H., Hao,Y.,
            Hong,J., Hu,Z., Hu,Y., Huang,J., Hwang,J.Y., Ikram,M.K., Jin,G.,
            Kang,D.H., Khor,C.C., Kim,B.J., Kim,H.T., Kubo,M., Lee,J., Lee,J.,
            Lee,N.R., Li,R., Li,J., Liu,J., Longe,J., Lu,W., Lu,X., Miao,X.,
            Okada,Y., Ong,R.T., Qiu,G., Seielstad,M., Sim,X., Song,H.,
            Takeuchi,F., Tanaka,T., Taylor,P.R., Wang,L., Wang,W., Wang,Y.,
            Wu,C., Wu,Y., Xiang,Y.B., Yamamoto,K., Yang,H., Liao,M., Yokota,M.,
            Young,T., Zhang,X., Kato,N., Wang,Q.K., Zheng,W., Hu,F.B., Lin,D.,
            Shen,H., Teo,Y.Y., Mo,Z., Wong,T.Y., Lin,X., Mohlke,K.L., Ning,G.,
            Tsunoda,T., Han,B.G., Shu,X.O., Tai,E.S., Wu,T. and Qi,L.
  TITLE     Meta-analysis of genome-wide association studies of adult height in
            East Asians identifies 17 novel loci
  JOURNAL   Hum Mol Genet 24 (6), 1791-1800 (2015)
   PUBMED   25429064
REFERENCE   6  (residues 1 to 141)
  AUTHORS   Houstek,J., Andersson,U., Tvrdik,P., Nedergaard,J. and Cannon,B.
  TITLE     The expression of subunit c correlates with and thus may limit the
            biosynthesis of the mitochondrial F0F1-ATPase in brown adipose
            tissue
  JOURNAL   J Biol Chem 270 (13), 7689-7694 (1995)
   PUBMED   7706317
REFERENCE   7  (residues 1 to 141)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   8  (residues 1 to 141)
  AUTHORS   Yan,W.L., Lerner,T.J., Haines,J.L. and Gusella,J.F.
  TITLE     Sequence analysis and mapping of a novel human mitochondrial ATP
            synthase subunit 9 cDNA (ATP5G3)
  JOURNAL   Genomics 24 (2), 375-377 (1994)
   PUBMED   7698763
REFERENCE   9  (residues 1 to 141)
  AUTHORS   Dyer,M.R. and Walker,J.E.
  TITLE     Sequences of members of the human gene family for the c subunit of
            mitochondrial ATP synthase
  JOURNAL   Biochem J 293 (Pt 1) (Pt 1), 51-64 (1993)
   PUBMED   8328972
REFERENCE   10 (residues 1 to 141)
  AUTHORS   Farrell,L.B. and Nagley,P.
  TITLE     Human liver cDNA clones encoding proteolipid subunit 9 of the
            mitochondrial ATPase complex
  JOURNAL   Biochem Biophys Res Commun 144 (3), 1257-1264 (1987)
   PUBMED   2883974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073594.31.
            
            Summary: This gene encodes a subunit of mitochondrial ATP synthase.
            Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an
            electrochemical gradient of protons across the inner membrane
            during oxidative phosphorylation. ATP synthase is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, comprising the proton channel.
            The catalytic portion of mitochondrial ATP synthase consists of 5
            different subunits (alpha, beta, gamma, delta, and epsilon)
            assembled with a stoichiometry of 3 alpha, 3 beta, and single
            representatives of the gamma, delta, and epsilon subunits. The
            proton channel likely has nine subunits (a, b, c, d, e, f, g, F6
            and 8). There are three separate genes which encode subunit c of
            the proton channel and they specify precursors with different
            import sequences but identical mature proteins. The protein encoded
            by this gene is one of three precursors of subunit c. This gene has
            multiple pseudogenes. [provided by RefSeq, Jan 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK311357.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..141
                     /product="ATP synthase F(0) complex subunit C2,
                     mitochondrial isoform c precursor"
                     /note="ATP synthase, H+ transporting, mitochondrial F0
                     complex, subunit C2 (subunit 9); ATP synthase
                     lipid-binding protein, mitochondrial; ATP synthase
                     proteolipid P2; ATPase protein 9; ATPase subunit C; ATP
                     synthase c subunit; ATP synthase proton-transporting
                     mitochondrial F(0) complex subunit C2; ATP synthase, H+
                     transporting, mitochondrial Fo complex subunit C2 (subunit
                     9); ATP synthase F(0) complex subunit C2, mitochondrial;
                     dicyclohexylcarbodiimide (DCCD)-reactive proteolipid
                     subunit"
                     /calculated_mol_wt=7608
     transit_peptide 1..66
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q06055.1)"
                     /calculated_mol_wt=7047
     mat_peptide     67..141
                     /product="ATP synthase F(0) complex subunit C2,
                     mitochondrial. /id=PRO_0000002562"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
                     /calculated_mol_wt=7608
     Region          67..141
                     /region_name="ATP9"
                     /note="ATP synthase F0 subunit 9; Provisional; MTH00222"
                     /db_xref="CDD:164765"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
     Site            109
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000269|PubMed:30530489; propagated from
                     UniProtKB/Swiss-Prot (Q06055.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
     Site            124
                     /site_type="other"
                     /note="Reversibly protonated during proton transport.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q06055.1)"
     CDS             1..141
                     /gene="ATP5MC2"
                     /gene_synonym="ATP5A; ATP5G2"
                     /coded_by="NM_001369754.1:304..729"
                     /note="isoform c precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS81694.1"
                     /db_xref="GeneID:517"
                     /db_xref="HGNC:HGNC:842"
                     /db_xref="MIM:603193"
ORIGIN      
        1 mfacskfvst pslvkstsql lsrplsavvl krpeiltdes lsslavscpl tslvssrsfq
       61 tsaisrdidt aakfigagaa tvgvagsgag igtvfgslii gyarnpslkq qlfsyailgf
      121 alseamglfc lmvaflilfa m
//
LOCUS       NP_055947                957 aa            linear   PRI 27-APR-2025
DEFINITION  sorting nexin-13 isoform b [Homo sapiens].
ACCESSION   NP_055947
VERSION     NP_055947.1
DBSOURCE    REFSEQ: accession NM_015132.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 957)
  AUTHORS   Lu,A., Hsieh,F., Sharma,B.R., Vaughn,S.R., Enrich,C. and
            Pfeffer,S.R.
  TITLE     CRISPR screens for lipid regulators reveal a role for ER-bound
            SNX13 in lysosomal cholesterol export
  JOURNAL   J Cell Biol 221 (2) (2022)
   PUBMED   34936700
  REMARK    GeneRIF: CRISPR screens for lipid regulators reveal a role for
            ER-bound SNX13 in lysosomal cholesterol export.
REFERENCE   2  (residues 1 to 957)
  AUTHORS   Mas,C., Norwood,S.J., Bugarcic,A., Kinna,G., Leneva,N., Kovtun,O.,
            Ghai,R., Ona Yanez,L.E., Davis,J.L., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for different phosphoinositide specificities of
            the PX domains of sorting nexins regulating G-protein signaling
  JOURNAL   J Biol Chem 289 (41), 28554-28568 (2014)
   PUBMED   25148684
REFERENCE   3  (residues 1 to 957)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   4  (residues 1 to 957)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   5  (residues 1 to 957)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   6  (residues 1 to 957)
  AUTHORS   Kosan,C. and Kunz,J.
  TITLE     Identification and characterisation of the gene TWIST NEIGHBOR
            (TWISTNB) located in the microdeletion syndrome 7p21 region
  JOURNAL   Cytogenet Genome Res 97 (3-4), 167-170 (2002)
   PUBMED   12438708
REFERENCE   7  (residues 1 to 957)
  AUTHORS   Zheng,B., Ma,Y.C., Ostrom,R.S., Lavoie,C., Gill,G.N., Insel,P.A.,
            Huang,X.Y. and Farquhar,M.G.
  TITLE     RGS-PX1, a GAP for GalphaS and sorting nexin in vesicular
            trafficking
  JOURNAL   Science 294 (5548), 1939-1942 (2001)
   PUBMED   11729322
REFERENCE   8  (residues 1 to 957)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB050735.1, AF420470.1,
            BC045667.1 and AC073205.6.
            
            Summary: This gene encodes a PHOX domain- and RGS domain-containing
            protein that belongs to the sorting nexin (SNX) family and the
            regulator of G protein signaling (RGS) family. The PHOX domain is a
            phosphoinositide binding domain, and the SNX family members are
            involved in intracellular trafficking. The RGS family members are
            regulatory molecules that act as GTPase activating proteins for G
            alpha subunits of heterotrimeric G proteins. The RGS domain of this
            protein interacts with G alpha(s), accelerates its GTP hydrolysis,
            and attenuates G alpha(s)-mediated signaling. Overexpression of
            this protein delayes lysosomal degradation of the epidermal growth
            factor receptor. Because of its bifunctional role, this protein may
            link heterotrimeric G protein signaling and vesicular trafficking.
            [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.264128.1,
                                           SRR1803614.113921.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000428135.7/ ENSP00000398789.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.1"
     Protein         1..957
                     /product="sorting nexin-13 isoform b"
                     /note="rgs domain- and phox domain-containing protein"
                     /calculated_mol_wt=110830
     Region          97..284
                     /region_name="PXA"
                     /note="Domain associated with PX domains; smart00313"
                     /db_xref="CDD:214611"
     Region          377..511
                     /region_name="RGS_SNX13"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the Sorting Nexin 13 (SNX13) protein; cd08719"
                     /db_xref="CDD:188674"
     Region          557..676
                     /region_name="PX_SNX13"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 13; cd06873"
                     /db_xref="CDD:132783"
     Site            order(601..603,628..629,642)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132783"
     Region          792..900
                     /region_name="Nexin_C"
                     /note="Sorting nexin C terminal; pfam08628"
                     /db_xref="CDD:462541"
     CDS             1..957
                     /gene="SNX13"
                     /gene_synonym="RGS-PX1"
                     /coded_by="NM_015132.5:200..3073"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47551.1"
                     /db_xref="GeneID:23161"
                     /db_xref="HGNC:HGNC:21335"
                     /db_xref="MIM:606589"
ORIGIN      
        1 mlteaslsiw gwgslgivlf litfgpfvif yltfyilcfv ggglvvtllf gktnsekyle
       61 qcehsflppt spgvpkclee mkreartiki drrltganii deplqqviqf slrdyvqywy
      121 ytlsddesfl leirqtlqna liqfatrske idwqpyfttr ivddfgthlr vfrkaqqkit
      181 ekddqvkgta edlvdtffev evemekevcr dlvctspkde egflrdlcev llylllppgd
      241 fqnkimryfv reilargill plinqlsdpd yinqyviwmi rdsncnyeaf mniiklsdni
      301 geleavrdka aeelqylrsl dtagddinti knqinsllfv kkvcdsriqr lqsgkeintv
      361 klaanfgklc tvpldsilvd nvalqffmdy mqqtggqahl ffwmtvegyr vtaqqqlevl
      421 lsrqrdgkhq tnqtkgllra aavgiyeqyl sekasprvtv ddylvaklad tlnhedptpe
      481 ifddiqrkvy elmlrderfy psfrqnalyv rmlaeldmlk dpsfrgsddg dgesfngspt
      541 gsinlslddl snvssddsvq lhayisdtgv cndhgktyal yaitvhrrnl nseemwktyr
      601 rysdfhdfhm riteqfesls silklpgkkt fnnmdrdfle krkkdlnayl qlllapemmk
      661 aspalahyvy dflenkaysk gkgdfarkmd tfvnplrnsm rnvsnavksl pdslaegmtk
      721 msdnmgkmse rlgqdikqsf fkvpplipkt dsdpehrrvs aqlddnvddn iplrvmlllm
      781 devfdlkern qwlrrniknl lqqliratyg dtinrkivdh vdwmtspeqv adsvkrfrda
      841 fwpngilaea vpcrdksirm rtrvagktkl laimpdelkh iigaettrkg ilrvfemfqh
      901 nqlnrrmvyv flegfletlf pqykfrelfn klhsrskqmq kykqklqttq apslqkr
//
LOCUS       NP_660156                198 aa            linear   PRI 27-APR-2025
DEFINITION  GTP-binding protein Di-Ras1 [Homo sapiens].
ACCESSION   NP_660156
VERSION     NP_660156.1
DBSOURCE    REFSEQ: accession NM_145173.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Wang,Y.Y., Ye,L.H., Zhao,A.Q., Gao,W.R., Dai,N., Yin,Y. and
            Zhang,X.
  TITLE     M6A modification regulates tumor suppressor DIRAS1 expression in
            cervical cancer cells
  JOURNAL   Cancer Biol Ther 25 (1), 2306674 (2024)
   PUBMED   38372700
  REMARK    GeneRIF: M6A modification regulates tumor suppressor DIRAS1
            expression in cervical cancer cells.
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Sommerer,Y., Dobricic,V., Schilling,M., Ohlei,O., Sabet,S.S.,
            Wesse,T., Fuss,J., Franzenburg,S., Franke,A., Parkkinen,L.,
            Lill,C.M. and Bertram,L.
  TITLE     Entorhinal cortex epigenome-wide association study highlights four
            novel loci showing differential methylation in Alzheimer's disease
  JOURNAL   Alzheimers Res Ther 15 (1), 92 (2023)
   PUBMED   37149695
  REMARK    GeneRIF: Entorhinal cortex epigenome-wide association study
            highlights four novel loci showing differential methylation in
            Alzheimer's disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Liu,H., Shu,W., Liu,T., Li,Q. and Gong,M.
  TITLE     Analysis of the function and mechanism of DIRAS1 in osteosarcoma
  JOURNAL   Tissue Cell 76, 101794 (2022)
   PUBMED   35413492
  REMARK    GeneRIF: Analysis of the function and mechanism of DIRAS1 in
            osteosarcoma.
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Wielaender,F., Sarviaho,R., James,F., Hytonen,M.K., Cortez,M.A.,
            Kluger,G., Koskinen,L.L., Arumilli,M., Kornberg,M.,
            Bathen-Noethen,A., Tipold,A., Rentmeister,K., Bhatti,S.F.,
            Hulsmeyer,V., Boettcher,I.C., Tastensen,C., Flegel,T., Dietschi,E.,
            Leeb,T., Matiasek,K., Fischer,A. and Lohi,H.
  TITLE     Generalized myoclonic epilepsy with photosensitivity in juvenile
            dogs caused by a defective DIRAS family GTPase 1
  JOURNAL   Proc Natl Acad Sci U S A 114 (10), 2669-2674 (2017)
   PUBMED   28223533
  REMARK    GeneRIF: This neuronal DIRAS1 gene with a proposed role in
            cholinergic transmission provides not only a candidate for human
            myoclonic epilepsy but also insights into the disease etiology,
            while establishing a spontaneous model for future intervention
            studies and functional characterization.
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Bergom,C., Hauser,A.D., Rymaszewski,A., Gonyo,P., Prokop,J.W.,
            Jennings,B.C., Lawton,A.J., Frei,A., Lorimer,E.L.,
            Aguilera-Barrantes,I., Mackinnon,A.C., Noon,K., Fierke,C.A. and
            Williams,C.L.
  TITLE     The Tumor-suppressive Small GTPase DiRas1 Binds the Noncanonical
            Guanine Nucleotide Exchange Factor SmgGDS and Antagonizes SmgGDS
            Interactions with Oncogenic Small GTPases
  JOURNAL   J Biol Chem 291 (12), 6534-6545 (2016)
   PUBMED   26814130
  REMARK    GeneRIF: DiRas1 expression inhibits malignant features of cancers
            in part by nonproductively binding to SmgGDS and inhibiting the
            binding of other small GTPases to SmgGDS
            Erratum:[J Biol Chem. 2016 May 13;291(20):10948. doi:
            10.1074/jbc.A115.696831. PMID: 27197236]
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Deng,X., Sabino,E.C., Cunha-Neto,E., Ribeiro,A.L., Ianni,B.,
            Mady,C., Busch,M.P. and Seielstad,M.
  CONSRTM   REDSII Chagas Study Group from the NHLBI Retrovirus Epidemiology
            Donor Study-II Component International
  TITLE     Genome wide association study (GWAS) of Chagas cardiomyopathy in
            Trypanosoma cruzi seropositive subjects
  JOURNAL   PLoS One 8 (11), e79629 (2013)
   PUBMED   24324551
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Zhu,Y.H., Fu,L., Chen,L., Qin,Y.R., Liu,H., Xie,F., Zeng,T.,
            Dong,S.S., Li,J., Li,Y., Dai,Y., Xie,D. and Guan,X.Y.
  TITLE     Downregulation of the novel tumor suppressor DIRAS1 predicts poor
            prognosis in esophageal squamous cell carcinoma
  JOURNAL   Cancer Res 73 (7), 2298-2309 (2013)
   PUBMED   23436800
  REMARK    GeneRIF: DIRAS1 downregulation is associated with esophageal
            squamous cell carcinoma metastasis.
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Kontani,K., Tada,M., Ogawa,T., Okai,T., Saito,K., Araki,Y. and
            Katada,T.
  TITLE     Di-Ras, a distinct subgroup of ras family GTPases with unique
            biochemical properties
  JOURNAL   J Biol Chem 277 (43), 41070-41078 (2002)
   PUBMED   12194967
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Ellis,C.A., Vos,M.D., Howell,H., Vallecorsa,T., Fults,D.W. and
            Clark,G.J.
  TITLE     Rig is a novel Ras-related protein and potential neural tumor
            suppressor
  JOURNAL   Proc Natl Acad Sci U S A 99 (15), 9876-9881 (2002)
   PUBMED   12107278
  REMARK    GeneRIF: a novel Ras-related protein and potential neural tumor
            suppressor (RIG)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA754806.1, BC030660.1, AK124445.1 and BC017484.1.
            
            Summary: DIRAS1 belongs to a distinct branch of the functionally
            diverse Ras (see HRAS; MIM 190020) superfamily of monomeric
            GTPases.[supplied by OMIM, Apr 2004].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030660.1, SRR3476690.823811.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323469.5/ ENSP00000325836.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..198
                     /product="GTP-binding protein Di-Ras1"
                     /note="small GTP-binding tumor suppressor 1; ras-related
                     inhibitor of cell growth; distinct subgroup of the Ras
                     family member 1; DIRAS family, GTP-binding RAS-like 1"
                     /calculated_mol_wt=22198
     mat_peptide     1..195
                     /product="GTP-binding protein Di-Ras1. /id=PRO_0000191648"
                     /note="propagated from UniProtKB/Swiss-Prot (O95057.1)"
                     /calculated_mol_wt=21983
     Region          7..168
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            14..21
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206648"
     Site            order(16..22,64,121..122,124,150..152)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206648"
     Region          36..44
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95057.1)"
     Site            39
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206648"
     Site            42..44
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206648"
     Site            61..64
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206648"
     Site            order(63..64,80..81)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206648"
     Site            121..124
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     Site            150..152
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206648"
     Region          178..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95057.1)"
     Site            195
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (O95057.1)"
     CDS             1..198
                     /gene="DIRAS1"
                     /gene_synonym="Di-Ras1; GBTS1; RIG"
                     /coded_by="NM_145173.4:139..735"
                     /db_xref="CCDS:CCDS12092.1"
                     /db_xref="GeneID:148252"
                     /db_xref="HGNC:HGNC:19127"
                     /db_xref="MIM:607862"
ORIGIN      
        1 mpeqsndyrv vvfgaggvgk sslvlrfvkg tfrdtyipti edtyrqvisc dksvctlqit
       61 dttgshqfpa mqrlsiskgh afilvfsvts kqsleelgpi yklivqikgs vedipvmlvg
      121 nkcdetqrev dtreaqavaq ewkcafmets akmnynvkel fqelltletr rnmslnidgk
      181 rsgkqkrtdr vkgkctlm
//
LOCUS       NP_078933                937 aa            linear   PRI 27-APR-2025
DEFINITION  MORC family CW-type zinc finger protein 4 isoform a [Homo sapiens].
ACCESSION   NP_078933
VERSION     NP_078933.3
DBSOURCE    REFSEQ: accession NM_024657.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Liang,Y., Wu,D., Qu,Q., Li,Z. and Yin,H.
  TITLE     MORC4 plays a tumor-promoting role in colorectal cancer via
            regulating PCGF1/CDKN1A axis in vitro and in vivo
  JOURNAL   Cancer Gene Ther 30 (7), 985-996 (2023)
   PUBMED   36932196
  REMARK    GeneRIF: MORC4 plays a tumor-promoting role in colorectal cancer
            via regulating PCGF1/CDKN1A axis in vitro and in vivo.
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Yang,Z., Zhuang,Q., Hu,G. and Geng,S.
  TITLE     MORC4 is a novel breast cancer oncogene regulated by miR-193b-3p
  JOURNAL   J Cell Biochem 120 (3), 4634-4643 (2019)
   PUBMED   30320920
  REMARK    GeneRIF: These results identified MORC4 as differentially expressed
            in breast cancer cells and tissues and its downregulation by
            miR-193b-3p, as well as its roles in regulating the growth of
            breast cancer cells via regulation of apoptosis.
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Campa,D., Pastore,M., Capurso,G., Hackert,T., Di Leo,M.,
            Izbicki,J.R., Khaw,K.T., Gioffreda,D., Kupcinskas,J., Pasquali,C.,
            Macinga,P., Kaaks,R., Stigliano,S., Peeters,P.H., Key,T.J.,
            Talar-Wojnarowska,R., Vodicka,P., Valente,R., Vashist,Y.K.,
            Salvia,R., Papaconstantinou,I., Shimizu,Y., Valsuani,C.,
            Zambon,C.F., Gazouli,M., Valantiene,I., Niesen,W.,
            Mohelnikova-Duchonova,B., Hara,K., Soucek,P., Malecka-Panas,E.,
            Bueno-de-Mesquita,H.B.A., Johnson,T., Brenner,H., Tavano,F.,
            Fogar,P., Ito,H., Sperti,C., Butterbach,K., Latiano,A.,
            Andriulli,A., Cavestro,G.M., Busch,O.R.C., Dijk,F., Greenhalf,W.,
            Matsuo,K., Lombardo,C., Strobel,O., Konig,A.K., Cuk,K.,
            Strothmann,H., Katzke,V., Cantore,M., Mambrini,A., Oliverius,M.,
            Pezzilli,R., Landi,S. and Canzian,F.
  TITLE     Do pancreatic cancer and chronic pancreatitis share the same
            genetic risk factors? A PANcreatic Disease ReseArch (PANDoRA)
            consortium investigation
  JOURNAL   Int J Cancer 142 (2), 290-296 (2018)
   PUBMED   28913878
  REMARK    GeneRIF: SNP in the MORC4-rs 12837024 is associated with Chronic
            pancreatitis.
REFERENCE   4  (residues 1 to 937)
  AUTHORS   Liu,Y., Tempel,W., Zhang,Q., Liang,X., Loppnau,P., Qin,S. and
            Min,J.
  TITLE     Family-wide Characterization of Histone Binding Abilities of Human
            CW Domain-containing Proteins
  JOURNAL   J Biol Chem 291 (17), 9000-9013 (2016)
   PUBMED   26933034
REFERENCE   5  (residues 1 to 937)
  AUTHORS   Noren,E., Verma,D., Soderkvist,P., Weisselberg,T., Soderman,J.,
            Lotfi,K. and Almer,S.
  TITLE     Single Nucleotide Polymorphisms in MORC4, CD14, and TLR4 Are
            Related to Outcome of Allogeneic Stem Cell Transplantation
  JOURNAL   Ann Transplant 21, 56-67 (2016)
   PUBMED   26827181
  REMARK    GeneRIF: Genetic variation in MORC4, CD14, and TLR4 may affect the
            outcome of allogeneic stem cell transplantation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 937)
  AUTHORS   Whitcomb,D.C., LaRusch,J., Krasinskas,A.M., Klei,L., Smith,J.P.,
            Brand,R.E., Neoptolemos,J.P., Lerch,M.M., Tector,M., Sandhu,B.S.,
            Guda,N.M., Orlichenko,L., Alkaade,S., Amann,S.T., Anderson,M.A.,
            Baillie,J., Banks,P.A., Conwell,D., Cote,G.A., Cotton,P.B.,
            DiSario,J., Farrer,L.A., Forsmark,C.E., Johnstone,M., Gardner,T.B.,
            Gelrud,A., Greenhalf,W., Haines,J.L., Hartman,D.J., Hawes,R.A.,
            Lawrence,C., Lewis,M., Mayerle,J., Mayeux,R., Melhem,N.M.,
            Money,M.E., Muniraj,T., Papachristou,G.I., Pericak-Vance,M.A.,
            Romagnuolo,J., Schellenberg,G.D., Sherman,S., Simon,P., Singh,V.P.,
            Slivka,A., Stolz,D., Sutton,R., Weiss,F.U., Wilcox,C.M.,
            Zarnescu,N.O., Wisniewski,S.R., O'Connell,M.R., Kienholz,M.L.,
            Roeder,K., Barmada,M.M., Yadav,D. and Devlin,B.
  CONSRTM   Alzheimer's Disease Genetics Consortium
  TITLE     Common genetic variants in the CLDN2 and PRSS1-PRSS2 loci alter
            risk for alcohol-related and sporadic pancreatitis
  JOURNAL   Nat Genet 44 (12), 1349-1354 (2012)
   PUBMED   23143602
REFERENCE   7  (residues 1 to 937)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 937)
  AUTHORS   Liggins,A.P., Cooper,C.D., Lawrie,C.H., Brown,P.J., Collins,G.P.,
            Hatton,C.S., Pulford,K. and Banham,A.H.
  TITLE     MORC4, a novel member of the MORC family, is highly expressed in a
            subset of diffuse large B-cell lymphomas
  JOURNAL   Br J Haematol 138 (4), 479-486 (2007)
   PUBMED   17608765
REFERENCE   9  (residues 1 to 937)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   10 (residues 1 to 937)
  AUTHORS   Perry,J. and Zhao,Y.
  TITLE     The CW domain, a structural module shared amongst vertebrates,
            vertebrate-infecting parasites and higher plants
  JOURNAL   Trends Biochem Sci 28 (11), 576-580 (2003)
   PUBMED   14607086
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB989767.1, EF125209.1,
            AK300305.1, BQ101064.1 and CA448781.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 20, 2007 this sequence version replaced NP_078933.2.
            
            Summary: In human, the four current members of the microrchidia
            (morc) gene family share an N-terminal ATPase-like ATP-binding
            region and a CW four-cysteine zinc-finger motif. The protein
            encoded by this gene also has a nuclear matrix binding domain and a
            two-stranded coiled-coil motif near its C-terminus. This gene is
            widely expressed at low levels in normal tissues and has elevated
            expression in placenta and testis. Alternative splicing results in
            multiple transcript variants encoding distinct proteins. [provided
            by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355610.9/ ENSP00000347821.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.3"
     Protein         1..937
                     /product="MORC family CW-type zinc finger protein 4
                     isoform a"
                     /note="zinc finger, CW type with coiled-coil domain 2;
                     MORC family CW-type zinc finger protein 4; zinc finger
                     CW-type coiled-coil domain protein 2; zinc finger CW-type
                     domain protein 4"
                     /calculated_mol_wt=106217
     Region          39..156
                     /region_name="HATPase"
                     /note="Histidine kinase-like ATPase domain; cl00075"
                     /db_xref="CDD:469604"
     Site            order(56,60,63,86,88,90,92,122..125,138,140,149..150,152)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340391"
     Site            order(99,125)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340391"
     Region          266..400
                     /region_name="Morc6_S5"
                     /note="Morc6 ribosomal protein S5 domain 2-like;
                     pfam17942"
                     /db_xref="CDD:465579"
     Region          425..470
                     /region_name="zf-CW"
                     /note="CW-type Zinc Finger; pfam07496"
                     /db_xref="CDD:462181"
     Region          606..637
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TE76.2)"
     Region          <766..810
                     /region_name="ZapB"
                     /note="Cell division protein ZapB; pfam06005"
                     /db_xref="CDD:428718"
     CDS             1..937
                     /gene="MORC4"
                     /gene_synonym="dJ75H8.2; ZCW4; ZCWCC2"
                     /coded_by="NM_024657.5:244..3057"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14525.2"
                     /db_xref="GeneID:79710"
                     /db_xref="HGNC:HGNC:23485"
                     /db_xref="MIM:300970"
ORIGIN      
        1 mllyrgapag pgapgcglar pgggpqafgi rlstmspryl qsnssshtrp fsaiaelldn
       61 avdpdvsart vfidveevkn kscltftddg cgmtphklhr mlsfgftdkv ikksqcpigv
      121 fgngfksgsm rlgkdalvft knggtltvgl lsqtylecvq aqavivpivp fnqqnkkmii
      181 tedslpslea ilnysifnre ndllaqfdai pgkkgtrvli wnirrnkngk seldfdtdqy
      241 dilvsdfdte ekmtggvtse lpeteyslra fcgilymkpr mkiflrqkkv ttqmiaksla
      301 nveydtykpt ftnkqvritf gfscknsnqf gimmyhnnrl iksfekvgcq vkptrgegvg
      361 vigviecnfl kpaynkqdfe ytkeyrltin alaqklnayw kektsqdnfe tstvarpipk
      421 vpdqtwvqcd eclkwrklpg kidpsmlpar wfcyynshpk yrrcsvpeeq eltdedlcls
      481 kakkqeqtve ekkkmpmene nhqvfsnppk iltvqemagl nnktigyegi hspsvlpsgg
      541 eesrspslql kpldssvlqf sskykwilge epvekrrrlq nemttpsldy smpapyrrve
      601 apvaypegen shdksssers tppylfpeyp easkntgqnr evsilypgak dqrqgsllpe
      661 eledqmprlv aeesnrgstt inkeevnkgp fvavvgvakg vrdsgapiql ipfnreelae
      721 rrkaveswnp vpysvasaai paaaigekar gyeeseghnt pklknqrele elkrttekle
      781 rvlaernlfq qkveeleqer nhwqsefkkv qhelviystq eaeglywskk hmgyrqaefq
      841 ilkaelertk eekqelkekl ketethleml qkaqvsyrtp egddlerala kltrlrihvs
      901 ylltsvlphl elreigydse qvdgilytvl eanhild
//
LOCUS       NP_002199               1179 aa            linear   PRI 27-APR-2025
DEFINITION  integrin alpha-E isoform 1 precursor [Homo sapiens].
ACCESSION   NP_002199
VERSION     NP_002199.3
DBSOURCE    REFSEQ: accession NM_002208.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1179)
  AUTHORS   Akasaka,H., Sato,D., Shihoya,W., Nureki,O. and Kise,Y.
  TITLE     Cryo-EM structure of I domain-containing integrin alphaEbeta7
  JOURNAL   Biochem Biophys Res Commun 721, 150121 (2024)
   PUBMED   38781659
  REMARK    GeneRIF: Cryo-EM structure of I domain-containing integrin
            alphaEbeta7.
REFERENCE   2  (residues 1 to 1179)
  AUTHORS   Hamid,M.H.B.A., Cespedes,P.F., Jin,C., Chen,J.L., Gileadi,U.,
            Antoun,E., Liang,Z., Gao,F., Teague,R., Manoharan,N.,
            Maldonado-Perez,D., Khalid-Alham,N., Cerundolo,L., Ciaoca,R.,
            Hester,S.S., Pinto-Fernandez,A., Draganov,S.D., Vendrell,I.,
            Liu,G., Yao,X., Kvalvaag,A., Dominey-Foy,D.C.C., Nanayakkara,C.,
            Kanellakis,N., Chen,Y.L., Waugh,C., Clark,S.A., Clark,K., Sopp,P.,
            Rahman,N.M., Verrill,C., Kessler,B.M., Ogg,G., Fernandes,R.A.,
            Fisher,R., Peng,Y., Dustin,M.L. and Dong,T.
  TITLE     Unconventional human CD61 pairing with CD103 promotes TCR signaling
            and antigen-specific T cell cytotoxicity
  JOURNAL   Nat Immunol 25 (5), 834-846 (2024)
   PUBMED   38561495
  REMARK    GeneRIF: Unconventional human CD61 pairing with CD103 promotes TCR
            signaling and antigen-specific T cell cytotoxicity.
REFERENCE   3  (residues 1 to 1179)
  AUTHORS   van den Bulk,J., van der Ploeg,M., Ijsselsteijn,M.E., Ruano,D., van
            der Breggen,R., Duhen,R., Peeters,K.C.M.J., Farina-Sarasqueta,A.,
            Verdegaal,E.M.E., van der Burg,S.H., Duhen,T. and de
            Miranda,N.F.C.C.
  TITLE     CD103 and CD39 coexpression identifies neoantigen-specific
            cytotoxic T cells in colorectal cancers with low mutation burden
  JOURNAL   J Immunother Cancer 11 (2) (2023)
   PUBMED   36792124
  REMARK    GeneRIF: CD103 and CD39 coexpression identifies neoantigen-specific
            cytotoxic T cells in colorectal cancers with low mutation burden.
REFERENCE   4  (residues 1 to 1179)
  AUTHORS   Nose,Y., Saito,T., Yamamoto,K., Yamashita,K., Tanaka,K.,
            Yamamoto,K., Makino,T., Takahashi,T., Kawashima,A., Haruna,M.,
            Hirata,M., Ueyama,A., Iwahori,K., Satoh,T., Kurokawa,Y., Eguchi,H.,
            Doki,Y. and Wada,H.
  TITLE     The tissue-resident marker CD103 on peripheral blood T cells
            predicts responses to anti-PD-1 therapy in gastric cancer
  JOURNAL   Cancer Immunol Immunother 72 (1), 169-181 (2023)
   PUBMED   35776160
  REMARK    GeneRIF: The tissue-resident marker CD103 on peripheral blood T
            cells predicts responses to anti-PD-1 therapy in gastric cancer.
REFERENCE   5  (residues 1 to 1179)
  AUTHORS   Xu,W., Bergsbaken,T. and Edelblum,K.L.
  TITLE     The multifunctional nature of CD103 (alphaEbeta7 integrin)
            signaling in tissue-resident lymphocytes
  JOURNAL   Am J Physiol Cell Physiol 323 (4), C1161-C1167 (2022)
   PUBMED   36036450
  REMARK    GeneRIF: The multifunctional nature of CD103 (alphaEbeta7 integrin)
            signaling in tissue-resident lymphocytes.
            Review article
REFERENCE   6  (residues 1 to 1179)
  AUTHORS   Austrup,F., Rebstock,S., Kilshaw,P.J. and Hamann,A.
  TITLE     Transforming growth factor-beta 1-induced expression of the
            mucosa-related integrin alpha E on lymphocytes is not associated
            with mucosa-specific homing
  JOURNAL   Eur J Immunol 25 (6), 1487-1491 (1995)
   PUBMED   7614974
REFERENCE   7  (residues 1 to 1179)
  AUTHORS   Begue,B., Sarnacki,S., le Deist,F., Buc,H., Gagnon,J., Meo,T. and
            Cerf-Bensussan,N.
  TITLE     HML-1, a novel integrin made of the beta 7 chain and of a
            distinctive alpha chain, exerts an accessory function in the
            activation of human IEL via the CD3-TCR pathway
  JOURNAL   Adv Exp Med Biol 371A, 67-75 (1995)
   PUBMED   8526015
REFERENCE   8  (residues 1 to 1179)
  AUTHORS   Shaw,S.K., Cepek,K.L., Murphy,E.A., Russell,G.J., Brenner,M.B. and
            Parker,C.M.
  TITLE     Molecular cloning of the human mucosal lymphocyte integrin alpha E
            subunit. Unusual structure and restricted RNA distribution
  JOURNAL   J Biol Chem 269 (8), 6016-6025 (1994)
   PUBMED   8119947
REFERENCE   9  (residues 1 to 1179)
  AUTHORS   Parker,C.M., Cepek,K.L., Russell,G.J., Shaw,S.K., Posnett,D.N.,
            Schwarting,R. and Brenner,M.B.
  TITLE     A family of beta 7 integrins on human mucosal lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 89 (5), 1924-1928 (1992)
   PUBMED   1542691
REFERENCE   10 (residues 1 to 1179)
  AUTHORS   Cerf-Bensussan,N., Jarry,A., Brousse,N., Lisowska-Grospierre,B.,
            Guy-Grand,D. and Griscelli,C.
  TITLE     A monoclonal antibody (HML-1) defining a novel membrane molecule
            present on human intestinal lymphocytes
  JOURNAL   Eur J Immunol 17 (9), 1279-1285 (1987)
   PUBMED   3498635
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L25851.2 and AC116914.5.
            
            On Jun 8, 2007 this sequence version replaced NP_002199.2.
            
            Summary: Integrins are heterodimeric integral membrane proteins
            composed of an alpha chain and a beta chain. This gene encodes an
            I-domain-containing alpha integrin that undergoes
            post-translational cleavage in the extracellular domain, yielding
            disulfide-linked heavy and light chains. In combination with the
            beta 7 integrin, this protein forms the E-cadherin binding integrin
            known as the human mucosal lymphocyte-1 antigen. This protein is
            preferentially expressed in human intestinal intraepithelial
            lymphocytes (IEL), and in addition to a role in adhesion, it may
            serve as an accessory molecule for IEL activation. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L25851.2, BC113436.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263087.9/ ENSP00000263087.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..1179
                     /product="integrin alpha-E isoform 1 precursor"
                     /note="HML-1 antigen; integrin alpha-IEL; antigen CD103,
                     human mucosal lymphocyte antigen 1; alpha polypeptide;
                     integrin alpha-E; mucosal lymphocyte 1 antigen; integrin,
                     alpha E (antigen CD103, human mucosal lymphocyte antigen
                     1; alpha polypeptide); human mucosal lymphocyte antigen 1,
                     alpha polypeptide"
                     /calculated_mol_wt=128190
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1988
     mat_peptide     19..1179
                     /product="integrin alpha-E isoform 1"
                     /calculated_mol_wt=128190
     mat_peptide     19..177
                     /product="Integrin alpha-E light chain.
                     /id=PRO_0000016284"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
                     /calculated_mol_wt=17551
     Region          22..79
                     /region_name="FG-GAP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     Site            49
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Region          80..138
                     /region_name="FG-GAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     Region          145..199
                     /region_name="X-domain (extra domain)"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     Region          158..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     mat_peptide     179..1177
                     /product="Integrin alpha-E heavy chain.
                     /id=PRO_0000016285"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
                     /calculated_mol_wt=110258
     Region          201..378
                     /region_name="vWA_integrins_alpha_subunit"
                     /note="Integrins are a class of adhesion receptors that
                     link the extracellular matrix to the cytoskeleton and
                     cooperate with growth factor receptors to promote celll
                     survival, cell cycle progression and cell migration.
                     Integrins consist of an alpha and a beta...; cd01469"
                     /db_xref="CDD:238746"
     Site            order(201,203,224,306,308,337,367)
                     /site_type="active"
                     /note="integrin inhibitor binding pocket [active]"
                     /db_xref="CDD:238746"
     Site            order(208,210,212,279,312)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238746"
     Site            order(210..212,214,279)
                     /site_type="active"
                     /note="integrin-collagen binding site [active]"
                     /db_xref="CDD:238746"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Site            321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Region          390..442
                     /region_name="FG-GAP 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     Site            444
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Region          447..499
                     /region_name="FG-GAP 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     Region          500..560
                     /region_name="FG-GAP 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     Region          510..561
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          563..627
                     /region_name="FG-GAP 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     Region          574..633
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          631..691
                     /region_name="FG-GAP 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     Region          643..>678
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          677..>951
                     /region_name="Integrin_alpha2"
                     /note="Integrin alpha; pfam08441"
                     /db_xref="CDD:462478"
     Site            726
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Site            782
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Site            857
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Site            934
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Site            954
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Site            1065
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Site            1096
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38570.3)"
     Site            1125..1147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     Region          1150..1154
                     /region_name="GFFKR motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P38570.3)"
     CDS             1..1179
                     /gene="ITGAE"
                     /gene_synonym="CD103; HUMINAE"
                     /coded_by="NM_002208.5:45..3584"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS32531.1"
                     /db_xref="GeneID:3682"
                     /db_xref="HGNC:HGNC:6147"
                     /db_xref="MIM:604682"
ORIGIN      
        1 mwlfhtllci aslallaafn vdvarpwltp kggapfvlss llhqdpstnq twllvtsprt
       61 krtpgplhrc slvqdeilch pvehvpipkg rhrgvtvvrs hhgvliciqv lvrrphslss
      121 eltgtcsllg pdlrpqaqan ffdlenlldp darvdtgdcy snkegggedd vntarqrral
      181 ekeeeedkee eedeeeeeag teiaiildgs gsidppdfqr akdfisnmmr nfyekcfecn
      241 falvqyggvi qtefdlrdsq dvmaslarvq nitqvgsvtk tasamqhvld siftsshgsr
      301 rkaskvmvvl tdggifedpl nlttvinspk mqgverfaig vgeefksart arelnliasd
      361 pdethafkvt nymaldglls klryniisme gtvgdalhyq laqigfsaqi lderqvllga
      421 vgafdwsgga llydtrsrrg rflnqtaaaa adaeaaqysy lgyavavlhk tcslsyiaga
      481 prykhhgavf elqkegreas flpvlegeqm gsyfgselcp vdidmdgstd fllvaapfyh
      541 vhgeegrvyv yrlseqdgsf slarilsghp gftnarfgfa maamgdlsqd kltdvaigap
      601 legfgaddga sfgsvyiyng hwdglsasps qrirastvap glqyfgmsma ggfdisgdgl
      661 aditvgtlgq avvfrsrpvv rlkvsmaftp salpigfngv vnvrlcfeis svttasesgl
      721 reallnftld vdvgkqrrrl qcsdvrsclg clrewssgsq lcedlllmpt egelceedcf
      781 snasvkvsyq lqtpegqtdh pqpildryte pfaifqlpye kacknklfcv aelqlattvs
      841 qqelvvgltk eltlninltn sgedsymtsm alnyprnlql krmqkppspn iqcddpqpva
      901 svlimncrig hpvlkrssah vsvvwqleen afpnrtadit vtvtnsnerr slanethtlq
      961 frhgfvavls kpsimyvntg qglshhkefl fhvhgenlfg aeyqlqicvp tklrglqvva
     1021 vkkltrtqas tvctwsqera cayssvqhve ewhsvscvia sdkenvtvaa eiswdhseel
     1081 lkdvtelqil geisfnksly eglnaenhrt kitvvflkde kyhslpiiik gsvggllvli
     1141 vilvilfkcg ffkrkyqqln lesirkaqlk senlleeen
//
LOCUS       NP_001304714             313 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine/tyrosine-interacting-like protein 1 isoform a
            [Homo sapiens].
ACCESSION   NP_001304714 XP_011514597
VERSION     NP_001304714.1
DBSOURCE    REFSEQ: accession NM_001317785.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Smailys,J., Jiang,F., Prioleau,T., Kelley,K., Mitchell,O., Nour,S.,
            Ali,L., Buchser,W., Zavada,L. and Hinton,S.D.
  TITLE     The DUSP domain of pseudophosphatase MK-STYX interacts with G3BP1
            to decrease stress granules
  JOURNAL   Arch Biochem Biophys 744, 109702 (2023)
   PUBMED   37516290
  REMARK    GeneRIF: The DUSP domain of pseudophosphatase MK-STYX interacts
            with G3BP1 to decrease stress granules.
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Patel,S., Bhatt,A.M., Bhansali,P. and Setty,S.R.G.
  TITLE     Pseudophosphatase STYXL1 depletion enhances glucocerebrosidase
            trafficking to lysosomes via ER stress
  JOURNAL   Traffic 24 (7), 254-269 (2023)
   PUBMED   37198709
  REMARK    GeneRIF: Pseudophosphatase STYXL1 depletion enhances
            glucocerebrosidase trafficking to lysosomes via ER stress.
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Wu,J.Z., Jiang,N., Lin,J.M. and Liu,X.
  TITLE     STYXL1 promotes malignant progression of hepatocellular carcinoma
            via downregulating CELF2 through the PI3K/Akt pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (6), 2977-2985 (2020)
   PUBMED   32271415
  REMARK    GeneRIF: STYXL1 promotes malignant progression of hepatocellular
            carcinoma via downregulating CELF2 through the PI3K/Akt pathway.
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Tomar,V.S., Baral,T.K., Nagavelu,K. and Somasundaram,K.
  TITLE     Serine/threonine/tyrosine-interacting-like protein 1 (STYXL1), a
            pseudo phosphatase, promotes oncogenesis in glioma
  JOURNAL   Biochem Biophys Res Commun 515 (1), 241-247 (2019)
   PUBMED   31146910
  REMARK    GeneRIF: Silencing serine/threonine/tyrosine-interacting-like
            protein 1 (STYXL1) inhibited glioma cell growth, soft agar colony
            formation, migration, invasion, proliferation, and xenograft tumor
            growth [Review].
            Review article
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Cao,Y., Banks,D.A., Mattei,A.M., Riddick,A.T., Reed,K.M.,
            Zhang,A.M., Pickering,E.S. and Hinton,S.D.
  TITLE     Pseudophosphatase MK-STYX Alters Histone Deacetylase 6 Cytoplasmic
            Localization, Decreases Its Phosphorylation, and Increases
            Detyrosination of Tubulin
  JOURNAL   Int J Mol Sci 20 (6), 1455 (2019)
   PUBMED   30909412
  REMARK    GeneRIF: These findings show that MK-STYX decreases the number of
            HDAC6-containing aggregates and alters their localization, sustains
            microtubule acetylation, and increases detyrosination of
            microtubules, implicating MK-STYX as a signaling molecule in HDAC6
            activity.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Meier,M., Tokarz,J., Haller,F., Mindnich,R. and Adamski,J.
  TITLE     Human and zebrafish hydroxysteroid dehydrogenase like 1 (HSDL1)
            proteins are inactive enzymes but conserved among species
  JOURNAL   Chem Biol Interact 178 (1-3), 197-205 (2009)
   PUBMED   19026618
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 313)
  AUTHORS   Cheng,J., Kapranov,P., Drenkow,J., Dike,S., Brubaker,S., Patel,S.,
            Long,J., Stern,D., Tammana,H., Helt,G., Sementchenko,V.,
            Piccolboni,A., Bekiranov,S., Bailey,D.K., Ganesh,M., Ghosh,S.,
            Bell,I., Gerhard,D.S. and Gingeras,T.R.
  TITLE     Transcriptional maps of 10 human chromosomes at 5-nucleotide
            resolution
  JOURNAL   Science 308 (5725), 1149-1154 (2005)
   PUBMED   15790807
REFERENCE   9  (residues 1 to 313)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   10 (residues 1 to 313)
  AUTHORS   Wishart,M.J. and Dixon,J.E.
  TITLE     Gathering STYX: phosphatase-like form predicts functions for unique
            protein-interaction domains
  JOURNAL   Trends Biochem Sci 23 (8), 301-306 (1998)
   PUBMED   9757831
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF069762.1, BC024035.2, BM824947.1, AC006330.5 and BM972220.1.
            
            On Dec 9, 2015 this sequence version replaced XP_011514597.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC024035.2, SRR18074967.1459278.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359697.8/ ENSP00000352726.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..313
                     /product="serine/threonine/tyrosine-interacting-like
                     protein 1 isoform a"
                     /note="map kinase phosphatase-like protein MK-STYX; dual
                     specificity phosphatase 24 (putative);
                     serine/threonine/tyrosine-interacting-like protein 1; dual
                     specificity protein phosphatase 24; dual specificity
                     phosphatase inhibitor MK-STYX; inactive dual specificity
                     protein phosphatase MK-STYX"
                     /calculated_mol_wt=35687
     Region          31..139
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain; smart00450"
                     /db_xref="CDD:197731"
     Site            78
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238089"
     Region          150..304
                     /region_name="DSP_STYXL1"
                     /note="dual specificity phosphatase-like domain of
                     serine/threonine/tyrosine interacting like 1; cd14517"
                     /db_xref="CDD:350367"
     CDS             1..313
                     /gene="STYXL1"
                     /gene_synonym="DUSP24; MK-STYX; MKSTYX"
                     /coded_by="NM_001317785.2:344..1285"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5580.1"
                     /db_xref="GeneID:51657"
                     /db_xref="HGNC:HGNC:18165"
                     /db_xref="MIM:616695"
ORIGIN      
        1 mpglllcept elynilnqat klsrltdpny lclldvrskw eydeshvita lrvkkknney
       61 llpesvdlec vkycvvydnn sstleillkd ddddsdsdgd gkdlvpqaai eygriltrlt
      121 hhpvyilkgg yerfsgtyhf lrtqkiiwmp qeldafqpyp ieivpgkvfv gnfsqacdpk
      181 iqkdlkikah vnvsmdtgpf fagdadkllh iriedspeaq ilpflrhmch fieihhhlgs
      241 vilifstqgi srscaaiiay lmhsneqtlq rswayvkkck nnmcpnrglv sqllewekti
      301 lgdsitnimd ply
//
LOCUS       NP_055555                411 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic initiation factor 4A-III isoform 1 [Homo sapiens].
ACCESSION   NP_055555
VERSION     NP_055555.1
DBSOURCE    REFSEQ: accession NM_014740.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Li,J., Xin,Y., Zhang,S., Li,Y., Jiang,M., Zhang,S., Yang,L.,
            Yang,J., Cao,P. and Lu,J.
  TITLE     EIF4A3 is stabilized by the long noncoding RNA BC200 to regulate
            gene expression during Epstein-Barr virus infection
  JOURNAL   J Med Virol 96 (10), e29955 (2024)
   PUBMED   39370864
  REMARK    GeneRIF: EIF4A3 is stabilized by the long noncoding RNA BC200 to
            regulate gene expression during Epstein-Barr virus infection.
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Zhou,Q., Cai,B., Liu,K. and Chen,H.
  TITLE     EIF4A3-Induced Upregulation of hsa_circ_0049396 Attenuates the
            Tumorigenesis of Nasopharyngeal Carcinoma by Regulating the
            Hippo-YAP Pathway
  JOURNAL   DNA Cell Biol 43 (10), 510-519 (2024)
   PUBMED   39133108
  REMARK    GeneRIF: EIF4A3-Induced Upregulation of hsa_circ_0049396 Attenuates
            the Tumorigenesis of Nasopharyngeal Carcinoma by Regulating the
            Hippo-YAP Pathway.
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Jiang,X., Peng,M., Liu,Q., Peng,Q., Oyang,L., Li,S., Xu,X.,
            Shen,M., Wang,J., Li,H., Wu,N., Tan,S., Lin,J., Xia,L., Tang,Y.,
            Luo,X., Liao,Q. and Zhou,Y.
  TITLE     Circular RNA hsa_circ_0000467 promotes colorectal cancer
            progression by promoting eIF4A3-mediated c-Myc translation
  JOURNAL   Mol Cancer 23 (1), 151 (2024)
   PUBMED   39085875
  REMARK    GeneRIF: Circular RNA hsa_circ_0000467 promotes colorectal cancer
            progression by promoting eIF4A3-mediated c-Myc translation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Cao,C., Wu,X., Li,Z., Xie,Y., Xu,S., Guo,J. and Sun,W.
  TITLE     EIF4A3-Bound hsa_circ_0006847 Exerts a Tumor-Suppressive Role in
            Gastric Cancer
  JOURNAL   DNA Cell Biol 43 (5), 232-244 (2024)
   PUBMED   38513058
  REMARK    GeneRIF: EIF4A3-Bound hsa_circ_0006847 Exerts a Tumor-Suppressive
            Role in Gastric Cancer.
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Yuan,L.X., Luo,M., Liu,R.Y., Wang,H.X., Ju,L.L., Wang,F., Cao,Y.L.,
            Wang,Z.C. and Chen,L.
  TITLE     Hsa_circ_0005397 promotes hepatocellular carcinoma progression
            through EIF4A3
  JOURNAL   BMC Cancer 24 (1), 239 (2024)
   PUBMED   38383334
  REMARK    GeneRIF: Hsa_circ_0005397 promotes hepatocellular carcinoma
            progression through EIF4A3.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Palacios,I.M., Gatfield,D., St Johnston,D. and Izaurralde,E.
  TITLE     An eIF4AIII-containing complex required for mRNA localization and
            nonsense-mediated mRNA decay
  JOURNAL   Nature 427 (6976), 753-757 (2004)
   PUBMED   14973490
  REMARK    GeneRIF: identification of eIF4AIII and Barentsz as components of a
            conserved protein complex that is essential for mRNA localization
            in flies and nonsense-mediated mRNA decay in mammals
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Chan,C.C., Dostie,J., Diem,M.D., Feng,W., Mann,M., Rappsilber,J.
            and Dreyfuss,G.
  TITLE     eIF4A3 is a novel component of the exon junction complex
  JOURNAL   RNA 10 (2), 200-209 (2004)
   PUBMED   14730019
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Le Hir,H., Gatfield,D., Izaurralde,E. and Moore,M.J.
  TITLE     The exon-exon junction complex provides a binding platform for
            factors involved in mRNA export and nonsense-mediated mRNA decay
  JOURNAL   EMBO J 20 (17), 4987-4997 (2001)
   PUBMED   11532962
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Holzmann,K., Gerner,C., Poltl,A., Schafer,R., Obrist,P.,
            Ensinger,C., Grimm,R. and Sauermann,G.
  TITLE     A human common nuclear matrix protein homologous to eukaryotic
            translation initiation factor 4A
  JOURNAL   Biochem Biophys Res Commun 267 (1), 339-344 (2000)
   PUBMED   10623621
  REMARK    GeneRIF: NMP 265, a common part of the nuclear matrix, is located
            in the nucleus via an N-terminal amino acid sequence.
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Li,Q., Imataka,H., Morino,S., Rogers,G.W. Jr., Richter-Cook,N.J.,
            Merrick,W.C. and Sonenberg,N.
  TITLE     Eukaryotic translation initiation factor 4AIII (eIF4AIII) is
            functionally distinct from eIF4AI and eIF4AII
  JOURNAL   Mol Cell Biol 19 (11), 7336-7346 (1999)
   PUBMED   10523622
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA667983.1, BC004386.1 and
            AC087741.18.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the DEAD box protein family.
            DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure, such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. The protein encoded by this gene is a
            nuclear matrix protein. Its amino acid sequence is highly similar
            to the amino acid sequences of the translation initiation factors
            eIF4AI and eIF4AII, two other members of the DEAD box protein
            family. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.12526.1,
                                           SRR14038193.3358645.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000649764.2/ ENSP00000497641.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..411
                     /product="eukaryotic initiation factor 4A-III isoform 1"
                     /EC_number="3.6.4.13"
                     /note="DEAD (Asp-Glu-Ala-Asp) box polypeptide 48;
                     eukaryotic initiation factor 4A-like NUK-34; nuclear
                     matrix protein 265; ATP-dependent RNA helicase DDX48;
                     ATP-dependent RNA helicase eIF4A-3; eukaryotic initiation
                     factor 4A-III; NMP 265; DEAD box protein 48"
                     /calculated_mol_wt=46740
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P38919.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine, in Eukaryotic initiation factor
                     4A-III, N-terminally processed.
                     /evidence=ECO:0000269|Ref.8, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P38919.4)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60842; propagated from
                     UniProtKB/Swiss-Prot (P38919.4)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P38919.4)"
     Region          35..411
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          38..66
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P38919.4)"
     Site            order(40,56,58..62,65,83..90,187..188)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350803"
     Site            order(63,67,83,86,222..224,227)
                     /site_type="other"
                     /note="Mago interface [polypeptide binding]"
                     /db_xref="CDD:350803"
     Site            order(106,150..151,154..155,174,177..179,201..202,
                     205..210,230..234)
                     /site_type="other"
                     /note="Barentsz interface [polypeptide binding]"
                     /db_xref="CDD:350803"
     Site            order(114..116,142..143,163..166,169,172,197,200)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350803"
     Site            124
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60842; propagated from
                     UniProtKB/Swiss-Prot (P38919.4)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P38919.4)"
     Region          187..190
                     /region_name="DEAD box. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P38919.4)"
     Site            198
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60843; propagated from
                     UniProtKB/Swiss-Prot (P38919.4)"
     Site            296
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P38919.4)"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P38919.4)"
     CDS             1..411
                     /gene="EIF4A3"
                     /gene_synonym="DDX48; eIF-4A-III; eIF4A-III; eIF4AIII;
                     Fal1; MUK34; NMP265; NUK34; RCPS"
                     /coded_by="NM_014740.4:168..1403"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11767.1"
                     /db_xref="GeneID:9775"
                     /db_xref="HGNC:HGNC:18683"
                     /db_xref="MIM:608546"
ORIGIN      
        1 mattatmats gsarkrllke edmtkvefet seevdvtptf dtmglredll rgiyaygfek
       61 psaiqqraik qiikgrdvia qsqsgtgkta tfsisvlqcl diqvretqal ilaptrelav
      121 qiqkgllalg dymnvqchac iggtnvgedi rkldygqhvv agtpgrvfdm irrrslrtra
      181 ikmlvldead emlnkgfkeq iydvyrylpp atqvvlisat lpheilemtn kfmtdpiril
      241 vkrdeltleg ikqffvaver eewkfdtlcd lydtltitqa vifcntkrkv dwltekmrea
      301 nftvssmhgd mpqkeresim kefrsgasrv listdvwarg ldvpqvslii nydlpnnrel
      361 yihrigrsgr ygrkgvainf vknddirilr dieqyystqi dempmnvadl i
//
LOCUS       NP_001356285             880 aa            linear   ROD 27-APR-2025
DEFINITION  inner centromere protein isoform 1 [Mus musculus].
ACCESSION   NP_001356285 XP_006526775
VERSION     NP_001356285.1
DBSOURCE    REFSEQ: accession NM_001369356.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 880)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 880)
  AUTHORS   Ray,J.P., Staron,M.M., Shyer,J.A., Ho,P.C., Marshall,H.D.,
            Gray,S.M., Laidlaw,B.J., Araki,K., Ahmed,R., Kaech,S.M. and
            Craft,J.
  TITLE     The Interleukin-2-mTORc1 Kinase Axis Defines the Signaling,
            Differentiation, and Metabolism of T Helper 1 and Follicular B
            Helper T Cells
  JOURNAL   Immunity 43 (4), 690-702 (2015)
   PUBMED   26410627
REFERENCE   3  (residues 1 to 880)
  AUTHORS   Fernandez-Miranda,G., Trakala,M., Martin,J., Escobar,B.,
            Gonzalez,A., Ghyselinck,N.B., Ortega,S., Canamero,M., Perez de
            Castro,I. and Malumbres,M.
  TITLE     Genetic disruption of aurora B uncovers an essential role for
            aurora C during early mammalian development
  JOURNAL   Development 138 (13), 2661-2672 (2011)
   PUBMED   21613325
REFERENCE   4  (residues 1 to 880)
  AUTHORS   Sharif,B., Na,J., Lykke-Hartmann,K., McLaughlin,S.H., Laue,E.,
            Glover,D.M. and Zernicka-Goetz,M.
  TITLE     The chromosome passenger complex is required for fidelity of
            chromosome transmission and cytokinesis in meiosis of mouse oocytes
  JOURNAL   J Cell Sci 123 (Pt 24), 4292-4300 (2010)
   PUBMED   21123620
REFERENCE   5  (residues 1 to 880)
  AUTHORS   Trivedi,C.M., Zhu,W., Wang,Q., Jia,C., Kee,H.J., Li,L.,
            Hannenhalli,S. and Epstein,J.A.
  TITLE     Hopx and Hdac2 interact to modulate Gata4 acetylation and embryonic
            cardiac myocyte proliferation
  JOURNAL   Dev Cell 19 (3), 450-459 (2010)
   PUBMED   20833366
REFERENCE   6  (residues 1 to 880)
  AUTHORS   Uren,A.G., Wong,L., Pakusch,M., Fowler,K.J., Burrows,F.J.,
            Vaux,D.L. and Choo,K.H.
  TITLE     Survivin and the inner centromere protein INCENP show similar
            cell-cycle localization and gene knockout phenotype
  JOURNAL   Curr Biol 10 (21), 1319-1328 (2000)
   PUBMED   11084331
REFERENCE   7  (residues 1 to 880)
  AUTHORS   Cutts,S.M., Fowler,K.J., Kile,B.T., Hii,L.L., O'Dowd,R.A.,
            Hudson,D.F., Saffery,R., Kalitsis,P., Earle,E. and Choo,K.H.
  TITLE     Defective chromosome segregation, microtubule bundling and nuclear
            bridging in inner centromere protein gene (Incenp)-disrupted mice
  JOURNAL   Hum Mol Genet 8 (7), 1145-1155 (1999)
   PUBMED   10369859
REFERENCE   8  (residues 1 to 880)
  AUTHORS   Saffery,R., Irvine,D.V., Kile,B.T., Hudson,D.F., Cutts,S.M. and
            Choo,K.H.
  TITLE     Cloning, expression, and promoter structure of a mammalian inner
            centromere protein (INCENP)
  JOURNAL   Mamm Genome 10 (4), 415-418 (1999)
   PUBMED   10087305
REFERENCE   9  (residues 1 to 880)
  AUTHORS   Craig,J.M., Earnshaw,W.C. and Vagnarelli,P.
  TITLE     Mammalian centromeres: DNA sequence, protein composition, and role
            in cell cycle progression
  JOURNAL   Exp Cell Res 246 (2), 249-262 (1999)
   PUBMED   9925740
  REMARK    Review article
REFERENCE   10 (residues 1 to 880)
  AUTHORS   Fowler,K.J., Saffery,R., Kile,B.T., Irvine,D.V., Hudson,D.F.,
            Trowell,H.E. and Choo,K.H.
  TITLE     Genetic mapping of mouse centromere protein (Incenp and Cenpe)
            genes
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 67-70 (1998)
   PUBMED   9763662
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132253.5.
            
            On Apr 5, 2019 this sequence version replaced XP_006526775.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB100433.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN01164143 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..880
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 6.1 cM"
     Protein         1..880
                     /product="inner centromere protein isoform 1"
                     /calculated_mol_wt=101078
     Region          6..41
                     /region_name="INCENP_N"
                     /note="Chromosome passenger complex (CPC) protein INCENP N
                     terminal; pfam12178"
                     /db_xref="CDD:463484"
     Region          52..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Region          175..229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Region          303..322
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU62.2)"
     Region          350..461
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            450
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20571061; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Region          506..733
                     /region_name="SAH. /evidence=ECO:0000250|UniProtKB:P53352"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU62.2)"
     Region          <513..656
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          513..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU62.2)"
     Region          563..617
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU62.2)"
     Region          629..713
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU62.2)"
     Region          775..813
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU62.2)"
     Region          794..868
                     /region_name="IN box. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU62.2)"
     Region          795..849
                     /region_name="INCENP_ARK-bind"
                     /note="Inner centromere protein, ARK binding region;
                     pfam03941"
                     /db_xref="CDD:461100"
     Site            796
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            800
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKB.
                     /evidence=ECO:0000250|UniProtKB:Q9NQS7; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            862
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     Site            867
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9WU62.2)"
     CDS             1..880
                     /gene="Incenp"
                     /gene_synonym="2700067E22Rik; C130081E20"
                     /coded_by="NM_001369356.1:163..2805"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS89338.1"
                     /db_xref="GeneID:16319"
                     /db_xref="MGI:MGI:1313288"
ORIGIN      
        1 mgttapgpic lldlcdqkll dfvcnvdnkd fmwlkeieee aermfirefs nepelmpktp
       61 sqknrrkkrr vsniqdenrd pvrkrlsrrk srssqvgtrh lrskpvtive engfpvlqri
      121 trataaaaaa aaaasvasas ssstagsptv ltkkavveis tserlsaelq ltklkgslpp
      181 spvsqgtlts eeeltpkkse agkldsvtvn slkatpqspk nrgvgegrsv sklkiarasw
      241 glqdspgstd spwqervlsp illnnilptt aksplgnirs vrrslisqds qvplaskynl
      301 vakqengsrr ssrriakkag kepeasarii chsylerlln vevpqnvgle qepvevaepe
      361 eaeeeqevsk nsgcpskprs atkiaistpt skpaaagqtt tveeqeaeld qtdghreppq
      421 svrrkrsykq aisepdeeql edeelqpcqn ktpsppcpan kvvrplrtfl htvqknqmlm
      481 tptlasrssv mksfikrntp lrvdpkcsfv ekerqrlesl rrkeeaeqrr rqkveedkrr
      541 rleevklkre erlrkvlqar erveqmkeek kkqieqkfaq idektekake erlaekakkk
      601 atakkmeeve arrkqeeear rlrwlqqeee errhqemlqr kkeeeqerrk aaearrlaeq
      661 reqerrreqe rreqerreqe rreqerkeqe rreqeqerlr akremqerek alrlqkerlq
      721 keleekkrke eqqrlaeqql qeeqakkake vaaarkvlnm tvdvqspvct syqmtpqgpk
      781 sipkisvddy gmdlnsddst ddeshprkpi pswakgtqls qaivhqyyhp pnilelfgsi
      841 lpldledifk krktryhkrt ssavwnsppl katmvpssgd
//
LOCUS       NP_001357376             485 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 577 isoform a [Homo sapiens].
ACCESSION   NP_001357376 XP_006723496
VERSION     NP_001357376.1
DBSOURCE    REFSEQ: accession NM_001370447.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Lorenzo,P.M., Izquierdo,A.G., Diaz-Lagares,A., Carreira,M.C.,
            Macias-Gonzalez,M., Sandoval,J., Cueva,J., Lopez-Lopez,R.,
            Casanueva,F.F. and Crujeiras,A.B.
  TITLE     ZNF577 Methylation Levels in Leukocytes From Women With Breast
            Cancer Is Modulated by Adiposity, Menopausal State, and the
            Mediterranean Diet
  JOURNAL   Front Endocrinol (Lausanne) 11, 245 (2020)
   PUBMED   32390948
  REMARK    GeneRIF: ZNF577 Methylation Levels in Leukocytes From Women With
            Breast Cancer Is Modulated by Adiposity, Menopausal State, and the
            Mediterranean Diet.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA747815.1, AK289479.1, AI004737.1 and AC074141.3.
            
            On May 8, 2019 this sequence version replaced XP_006723496.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.199044.1,
                                           SRR1803613.162707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2162568
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..485
                     /product="zinc finger protein 577 isoform a"
                     /calculated_mol_wt=54808
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSK1.3)"
     Region          25..83
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          136..>217
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          160..180
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          188..208
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <194..399
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          216..236
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(221,223,225,227..228,231..232,235,249,251,255..256,
                     259..260,263,277,279,281,283..284,287..288,291)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          244..264
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          272..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(305,307,309,311..312,315..316,319,333,335,339..340,
                     343..344,347,361,363,365,367..368,371..372,375)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          356..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..485
                     /gene="ZNF577"
                     /coded_by="NM_001370447.1:419..1876"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS12842.2"
                     /db_xref="GeneID:84765"
                     /db_xref="HGNC:HGNC:28673"
ORIGIN      
        1 mknativmsv rreqgsssge gslsfedvav gftreewqfl dqsqkvlyke vmlenyinlv
       61 sigyrgtkpd slfkleqgep pgiaegaahs qicpgfviqs rryagkdsda fggygrsclh
      121 ikrdktltgv kyhrcvkpss pksqlndlqk icaggkphec svcgrafsrk aqliqhqrte
      181 rgekphgcge cgktfmrkiq ltehqrthtg ekphecsecg kafsrksqlm vhqrthtgek
      241 pyrcskcgka fsrkcrlnrh qrshtgekly gcsvcgkafs qkayltahqr lhtgdkpykc
      301 sdcgrtfyfk sdltrhqrih tgekpyecse cekafrsksk liqhqrthtg erpyscrecg
      361 kafahmsvli khekthiret ainsltvekp ssrshtslym seliqeqktv ntvpiempss
      421 gtppllnkse rlvgrnvviv eqpfprnqaf vvnqefeqri sltnevnvap svinyilylt
      481 divse
//
LOCUS       NP_004738               1919 aa            linear   PRI 27-APR-2025
DEFINITION  disks large homolog 5 [Homo sapiens].
ACCESSION   NP_004738
VERSION     NP_004738.3
DBSOURCE    REFSEQ: accession NM_004747.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1919)
  AUTHORS   Song,X.Q., Li,Q. and Zhang,J.
  TITLE     A double-edged sword: DLG5 in diseases
  JOURNAL   Biomed Pharmacother 162, 114611 (2023)
   PUBMED   37001186
  REMARK    GeneRIF: A double-edged sword: DLG5 in diseases.
            Review article
REFERENCE   2  (residues 1 to 1919)
  AUTHORS   Kundu,S., Nandhu,M.S., Longo,S.L., Longo,J.A., Rai,S., Chin,L.S.,
            Richardson,T.E. and Viapiano,M.S.
  TITLE     The scaffolding protein DLG5 promotes glioblastoma growth by
            controlling Sonic Hedgehog signaling in tumor stem cells
  JOURNAL   Neuro Oncol 24 (8), 1230-1242 (2022)
   PUBMED   34984467
  REMARK    GeneRIF: The scaffolding protein DLG5 promotes glioblastoma growth
            by controlling Sonic Hedgehog signaling in tumor stem cells.
REFERENCE   3  (residues 1 to 1919)
  AUTHORS   Andolfi,C., Tiribelli,C. and Pascut,D.
  TITLE     Recent Hints on the Dual Role of Discs Large MAGUK Scaffold Protein
            5 in Cancers and in Hepatocellular Carcinoma
  JOURNAL   Front Biosci (Landmark Ed) 27 (5), 164 (2022)
   PUBMED   35638431
  REMARK    GeneRIF: Recent Hints on the Dual Role of Discs Large MAGUK
            Scaffold Protein 5 in Cancers and in Hepatocellular Carcinoma.
            Review article
REFERENCE   4  (residues 1 to 1919)
  AUTHORS   Marquez,J., Mann,N., Arana,K., Deniz,E., Ji,W., Konstantino,M.,
            Mis,E.K., Deshpande,C., Jeffries,L., McGlynn,J., Hugo,H.,
            Widmeier,E., Konrad,M., Tasic,V., Morotti,R., Baptista,J.,
            Ellard,S., Lakhani,S.A., Hildebrandt,F. and Khokha,M.K.
  TITLE     DLG5 variants are associated with multiple congenital anomalies
            including ciliopathy phenotypes
  JOURNAL   J Med Genet 58 (7), 453-464 (2021)
   PUBMED   32631816
  REMARK    GeneRIF: DLG5 variants are associated with multiple congenital
            anomalies including ciliopathy phenotypes.
REFERENCE   5  (residues 1 to 1919)
  AUTHORS   Liu,J., Li,J., Li,P., Jiang,Y., Chen,H., Wang,R., Cao,F. and Liu,P.
  TITLE     DLG5 suppresses breast cancer stem cell-like characteristics to
            restore tamoxifen sensitivity by inhibiting TAZ expression
  JOURNAL   J Cell Mol Med 23 (1), 512-521 (2019)
   PUBMED   30450766
  REMARK    GeneRIF: Down-regulated DLG5 expression increases the stemness of
            breast cancer cells by enhancing TAZ expression, contributing to
            TAM resistance in breast cancer.
REFERENCE   6  (residues 1 to 1919)
  AUTHORS   Wakabayashi,M., Ito,T., Mitsushima,M., Aizawa,S., Ueda,K.,
            Amachi,T. and Kioka,N.
  TITLE     Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate
            kinase family protein, with vinexin and beta-catenin at sites of
            cell-cell contact
  JOURNAL   J Biol Chem 278 (24), 21709-21714 (2003)
   PUBMED   12657639
  REMARK    GeneRIF: findings suggest that lp-dlg/KIAA0583 is a novel
            scaffolding protein that can link the vinexin-vinculin complex and
            beta-catenin at sites of cell-cell contact
REFERENCE   7  (residues 1 to 1919)
  AUTHORS   Purmonen,S., Ahola,T.M., Pennanen,P., Aksenov,N., Zhuang,Y.H.,
            Tuohimaa,P. and Ylikomi,T.
  TITLE     HDLG5/KIAA0583, encoding a MAGUK-family protein, is a primary
            progesterone target gene in breast cancer cells
  JOURNAL   Int J Cancer 102 (1), 1-6 (2002)
   PUBMED   12353226
REFERENCE   8  (residues 1 to 1919)
  AUTHORS   Shah,G., Brugada,R., Gonzalez,O., Czernuszewicz,G., Gibbs,R.A.,
            Bachinski,L. and Roberts,R.
  TITLE     The cloning, genomic organization and tissue expression profile of
            the human DLG5 gene
  JOURNAL   BMC Genomics 3, 6 (2002)
   PUBMED   11876824
  REMARK    Erratum:[BMC Genomics. 2002 Jun 11;3:14. doi:
            10.1186/1471-2164-3-14. PMID: 12060488]
REFERENCE   9  (residues 1 to 1919)
  AUTHORS   Bowles,K.R., Abraham,S.E., Brugada,R., Zintz,C., Comeaux,J.,
            Sorajja,D., Tsubata,S., Li,H., Brandon,L., Gibbs,R.A.,
            Scherer,S.E., Bowles,N.E. and Towbin,J.A.
  TITLE     Construction of a high-resolution physical map of the chromosome
            10q22-q23 dilated cardiomyopathy locus and analysis of candidate
            genes
  JOURNAL   Genomics 67 (2), 109-127 (2000)
   PUBMED   10903836
REFERENCE   10 (residues 1 to 1919)
  AUTHORS   Nakamura,H., Sudo,T., Tsuiki,H., Miyake,H., Morisaki,T., Sasaki,J.,
            Masuko,N., Kochi,M., Ushio,Y. and Saya,H.
  TITLE     Identification of a novel human homolog of the Drosophila dlg,
            P-dlg, specifically expressed in the gland tissues and interacting
            with p55
  JOURNAL   FEBS Lett 433 (1-2), 63-67 (1998)
   PUBMED   9738934
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391421.27, AB011155.2,
            AK122931.1 and BC030250.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 10, 2006 this sequence version replaced NP_004738.2.
            
            Summary: This gene encodes a member of the family of discs large
            (DLG) homologs, a subset of the membrane-associated guanylate
            kinase (MAGUK) superfamily. The MAGUK proteins are composed of a
            catalytically inactive guanylate kinase domain, in addition to PDZ
            and SH3 domains, and are thought to function as scaffolding
            molecules at sites of cell-cell contact. The protein encoded by
            this gene localizes to the plasma membrane and cytoplasm, and
            interacts with components of adherens junctions and the
            cytoskeleton. It is proposed to function in the transmission of
            extracellular signals to the cytoskeleton and in the maintenance of
            epithelial cell structure. Alternative splice variants have been
            described but their biological nature has not been determined.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC146794.1, AB011155.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372391.7/ ENSP00000361467.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1919
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.3"
     Protein         1..1919
                     /product="disks large homolog 5"
                     /note="discs large protein LP-DLG; large type of P-DLG;
                     placenta and prostate DLG; discs large protein P-dlg;
                     discs, large homolog 5"
                     /calculated_mol_wt=213737
     Region          98..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Region          129..213
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     Region          <199..407
                     /region_name="PRK04778"
                     /note="septation ring formation regulator EzrA;
                     Provisional"
                     /db_xref="CDD:179877"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Region          <338..636
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          615..709
                     /region_name="PDZ1_DLG5-like"
                     /note="PDZ domain 1 of Discs Large 5 (Dlg5) and related
                     domains; cd06764"
                     /db_xref="CDD:467245"
     Site            order(634..640,657,660,688,692,695..696)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467245"
     Region          721..797
                     /region_name="PDZ2_DLG5-like"
                     /note="PDZ domain 2 of Discs Large 5 (Dlg5) and related
                     domains; cd06765"
                     /db_xref="CDD:467246"
     Site            order(729..735,741,744,774,778,781..782)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467246"
     Region          874..>1303
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Region          927..1122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Site            984
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Site            1000
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Site            1011
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Site            1021
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Region          1150..1187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Site            1183
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Region          1201..1230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Site            1209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Region          1245..1264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Site            1263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Region          1271..1306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Site            1334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Region          1346..1427
                     /region_name="PDZ3_DLG5-like"
                     /note="PDZ domain 3 of Discs Large 5 (Dlg5) and related
                     domains; cd06767"
                     /db_xref="CDD:467248"
     Site            order(1359..1365,1375,1378,1407,1411,1414..1415)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467248"
     Region          1427..1499
                     /region_name="dbPDZ_assoc"
                     /note="Unstructured region between two PDZ domains on
                     Dlg5; pfam16610"
                     /db_xref="CDD:465197"
     Region          1434..1493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Region          1499..1579
                     /region_name="PDZ4_DLG5-like"
                     /note="PDZ domain 4 of Discs Large 5 (Dlg5) and related
                     domains; cd06766"
                     /db_xref="CDD:467247"
     Site            order(1511..1517,1527,1530,1558,1562,1565..1566)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467247"
     Region          1597..1659
                     /region_name="SH3_DLG5"
                     /note="Src homology 3 domain of Disks Large homolog 5;
                     cd11860"
                     /db_xref="CDD:212794"
     Site            order(1599,1616..1617)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212794"
     Site            order(1602,1604,1607,1611,1633..1634,1652,1654..1655)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212794"
     Site            1666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDM6.4)"
     Region          1732..1908
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     CDS             1..1919
                     /gene="DLG5"
                     /gene_synonym="LP-DLG; P-DLG5; PDLG; YUVOB"
                     /coded_by="NM_004747.4:236..5995"
                     /db_xref="CCDS:CCDS7353.2"
                     /db_xref="GeneID:9231"
                     /db_xref="HGNC:HGNC:2904"
                     /db_xref="MIM:604090"
ORIGIN      
        1 mepqrrella qcqqslaqam teveavlgll eaagalspge rrqldeeagg akaelllkll
       61 lakerdhfqd lraalektqp hllpilylng vvgppqpaeg agstysvlst mpsdsessss
      121 lssvgttgka psppplltdq qvnekvenls iqlrlmtrer nelrkrlafa thgtafdkrp
      181 yhrlnpdyer lkiqcvrams dlqslqnqht nalkrceeva ketdfyhtlh srllsdqtrl
      241 kddvdmlrre ngqllrernl lqqswedmkr lheedqkeig dlraqqqqvl khngsseiln
      301 klydtamdkl evvkkdydal rkrysekvai hnadlsrleq lgeenqrllk qtemltqqrd
      361 taiqlqhqca lslrrfeaih helnkataqn kdlqwemell qseltelrtt qvktakesek
      421 yreerdavys eyklimserd qviseldklq tevelaeskl ksstsekkaa neemealrqi
      481 kdtvtmdagr ankeveilrk qckalcqelk ealqeadvak crrdwafqer dkivaerdsi
      541 rtlcdnlrre rdravselae alrslddtrk qkndvsrelk elkeqmesql ekearfrqlm
      601 ahsshdsaid tdsmewetev veferetedi dlkalgfdma egvnepcfpg dcgifvtkvd
      661 kgsiadgrlr vndwllrind vdlinkdkkq aikallngeg ainmvvrrrk slggkvvtpl
      721 hinlsgqkds gislengvya aavlpgspaa kegslavgdr ivaingiald nkslnecesl
      781 lrscqdsltl sllkvfpqss swsgqnifen ikdsdkmlsf rahgpevqah nkrnliqhnn
      841 stqtdifytd rledrkepgp pggsssflhk pfpggplqvc pqacpsaser slssfrsdas
      901 gdrgfglvdv rgrrpllpfe tevgpcgvge asldkadseg snsggtwpka mlsstavpek
      961 lsvykkpkqr ksifdpntfk rpqtppkidy llpgpgpahs pqpskragpl tppkpprrsd
     1021 sikfqhrlet sseseatlvg sspstsppsa lppdvdpgep mhaspprkar vriassyype
     1081 gdgdsshlpa kkscdedlts qkvdelgqkr rrpksapsfr pklapvvipa qfleeqkcvp
     1141 asgelspelq ewapyspghs srhsnpplyp srpsvgtvpr sltpsttvss ilrnpiytvr
     1201 shrvgpcssp paardagpqg lhpsvqhqgr lsldlshrtc sdysemrath gsnslpssar
     1261 lgsssnlqfk aerikipstp ryprsvvgse rgsvshsecs tppqsplnid tlsscsqsqt
     1321 sastlpriav npaslgerrk drpyveeprh vkvqkgsepl gisivsgekg giyvskvtvg
     1381 siahqagley gdqllefngi nlrsateqqa rliigqqcdt itilaqynph vhqlsshsrs
     1441 sshldpagth stlqgsgttt pehpsvidpl meqdegpstp pakqsssria gdankktlep
     1501 rvvfikksql elgvhlcggn lhgvfvaeve ddspakgpdg lvpgdliley gsldvrnktv
     1561 eevyvemlkp rdgvrlkvqy rpeeftkakg lpgdsfyira lydrladveq elsfkkddil
     1621 yvddtlpqgt fgswmawqld enaqkiqrgq ipskyvmdqe fsrrlsmsev kddnsatktl
     1681 saaarrsffr rkhkhkrsgs kdgkdllald afssdsiplf edsvslayqr vqkvdctalr
     1741 pvlilgplld vvkemlvnea pgkfcrcple vmkasqqaie rgvkdclfvd ykrrsghfdv
     1801 ttvasikeit eknrhclldi aphaierlhh mhiypivifi hyksakhike qrdpiylrdk
     1861 vtqrhskeqf eaaqkleqey sryftgviqg galssictqi lamvnqeqnk vlwipacpl
//
LOCUS       NP_115876                372 aa            linear   PRI 27-APR-2025
DEFINITION  actin-related protein T3 [Homo sapiens].
ACCESSION   NP_115876 XP_001132426
VERSION     NP_115876.3
DBSOURCE    REFSEQ: accession NM_032487.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Song,F., Amos,C.I., Lee,J.E., Lian,C.G., Fang,S., Liu,H.,
            MacGregor,S., Iles,M.M., Law,M.H., Lindeman,N.I., Montgomery,G.W.,
            Duffy,D.L., Cust,A.E., Jenkins,M.A., Whiteman,D.C., Kefford,R.F.,
            Giles,G.G., Armstrong,B.K., Aitken,J.F., Hopper,J.L., Brown,K.M.,
            Martin,N.G., Mann,G.J., Bishop,D.T., Bishop,J.A., Kraft,P.,
            Qureshi,A.A., Kanetsky,P.A., Hayward,N.K., Hunter,D.J., Wei,Q. and
            Han,J.
  CONSRTM   GenoMEL consortium
  TITLE     Identification of a melanoma susceptibility locus and somatic
            mutation in TET2
  JOURNAL   Carcinogenesis 35 (9), 2097-2101 (2014)
   PUBMED   24980573
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Figueroa,J.D., Ye,Y., Siddiq,A., Garcia-Closas,M., Chatterjee,N.,
            Prokunina-Olsson,L., Cortessis,V.K., Kooperberg,C., Cussenot,O.,
            Benhamou,S., Prescott,J., Porru,S., Dinney,C.P., Malats,N.,
            Baris,D., Purdue,M., Jacobs,E.J., Albanes,D., Wang,Z., Deng,X.,
            Chung,C.C., Tang,W., Bas Bueno-de-Mesquita,H., Trichopoulos,D.,
            Ljungberg,B., Clavel-Chapelon,F., Weiderpass,E., Krogh,V.,
            Dorronsoro,M., Travis,R., Tjonneland,A., Brenan,P.,
            Chang-Claude,J., Riboli,E., Conti,D., Gago-Dominguez,M.,
            Stern,M.C., Pike,M.C., Van Den Berg,D., Yuan,J.M., Hohensee,C.,
            Rodabough,R., Cancel-Tassin,G., Roupret,M., Comperat,E., Chen,C.,
            De Vivo,I., Giovannucci,E., Hunter,D.J., Kraft,P., Lindstrom,S.,
            Carta,A., Pavanello,S., Arici,C., Mastrangelo,G., Kamat,A.M.,
            Lerner,S.P., Barton Grossman,H., Lin,J., Gu,J., Pu,X.,
            Hutchinson,A., Burdette,L., Wheeler,W., Kogevinas,M., Tardon,A.,
            Serra,C., Carrato,A., Garcia-Closas,R., Lloreta,J., Schwenn,M.,
            Karagas,M.R., Johnson,A., Schned,A., Armenti,K.R., Hosain,G.M.,
            Andriole,G. Jr., Grubb,R. 3rd, Black,A., Ryan Diver,W.,
            Gapstur,S.M., Weinstein,S.J., Virtamo,J., Haiman,C.A., Landi,M.T.,
            Caporaso,N., Fraumeni,J.F. Jr., Vineis,P., Wu,X., Silverman,D.T.,
            Chanock,S. and Rothman,N.
  TITLE     Genome-wide association study identifies multiple loci associated
            with bladder cancer risk
  JOURNAL   Hum Mol Genet 23 (5), 1387-1398 (2014)
   PUBMED   24163127
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Hara,Y., Yamagata,K., Oguchi,K. and Baba,T.
  TITLE     Nuclear localization of profilin III-ArpM1 complex in mouse
            spermiogenesis
  JOURNAL   FEBS Lett 582 (20), 2998-3004 (2008)
   PUBMED   18692047
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Harata,M., Nishimori,K. and Hatta,S.
  TITLE     Identification of two cDNAs for human actin-related proteins (Arps)
            that have remarkable similarity to conventional actin
  JOURNAL   Biochim Biophys Acta 1522 (2), 130-133 (2001)
   PUBMED   11750065
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK055346.1, AB049117.1 and AI811210.1.
            
            On Jan 22, 2009 this sequence version replaced NP_115876.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.213651.1, AK055346.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330368.3/ ENSP00000333037.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..372
                     /product="actin-related protein T3"
                     /note="actin-related protein M1"
                     /calculated_mol_wt=40877
     Region          7..363
                     /region_name="ASKHA_NBD_actin_Arp-T1-3"
                     /note="nucleotide-binding domain (NBD) of actin,
                     actin-related proteins T1-T3 (Arp-T1-3), and similar
                     proteins; cd13397"
                     /db_xref="CDD:466848"
     CDS             1..372
                     /gene="ACTRT3"
                     /gene_synonym="ARP-T3; ARPM1"
                     /coded_by="NM_032487.5:42..1160"
                     /db_xref="CCDS:CCDS3206.1"
                     /db_xref="GeneID:84517"
                     /db_xref="HGNC:HGNC:24022"
                     /db_xref="MIM:608534"
ORIGIN      
        1 mnhcqlpvvi dngsgmikag vagcrepqfi ypniigrakg qsraaqggle lcvgdqaqdw
       61 rsslfisypv erglitswed meimwkhiyd ynlklkpcdg pvlitepaln planrqqite
      121 mffehlgvpa fymsiqavla lfaagfttgl vlnsgagvtq svpifegycl phgvqqldla
      181 gldltnylmv lmknhgimll sasdrkived ikesfcyvam nyeeemakkp dclekvyqlp
      241 dgkviqlhdq lfscpealfs pchmnleapg idkicfssim kcdtglrnsf fsniilaggs
      301 tsfpgldkrl vkdiakvapa ntavqviapp erkisvwmgg silaslsafq dmwitaaefk
      361 evgpnivhqr cf
//
LOCUS       NP_478059                370 aa            linear   PRI 27-APR-2025
DEFINITION  phosphoserine aminotransferase isoform 1 [Homo sapiens].
ACCESSION   NP_478059
VERSION     NP_478059.1
DBSOURCE    REFSEQ: accession NM_058179.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Liu,Y., Xun,W., Zhao,T., Huang,M., Sun,L., Wen,G., Kang,X., Wang,J.
            and Han,T.
  TITLE     Interplay between acetylation and ubiquitination controls PSAT1
            protein stability in lung adenocarcinoma
  JOURNAL   Commun Biol 7 (1), 1365 (2024)
   PUBMED   39433916
  REMARK    GeneRIF: Interplay between acetylation and ubiquitination controls
            PSAT1 protein stability in lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Du,X., Wang,Y. and Gao,F.
  TITLE     PSAT1 is upregulated by METTL3 to attenuate high glucose-induced
            retinal pigment epithelial cell apoptosis and oxidative stress
  JOURNAL   Diagn Pathol 19 (1), 138 (2024)
   PUBMED   39407268
  REMARK    GeneRIF: PSAT1 is upregulated by METTL3 to attenuate high
            glucose-induced retinal pigment epithelial cell apoptosis and
            oxidative stress.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Zhang,X., Wang,S., Li,W., Wang,J., Gong,Y., Chen,Q., Cao,S.,
            Pang,D. and Gao,S.
  TITLE     PSAT1 Promotes Metastasis via p-AKT/SP1/ITGA2 Axis in Estrogen
            Receptor-Negative Breast Cancer Cell
  JOURNAL   Biomolecules 14 (8), 990 (2024)
   PUBMED   39199378
  REMARK    GeneRIF: PSAT1 Promotes Metastasis via p-AKT/SP1/ITGA2 Axis in
            Estrogen Receptor-Negative Breast Cancer Cell.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Ye,J., Huang,X., Tian,S., Wang,J., Wang,H., Feng,H., Zhao,X.,
            Cao,S., Xuan,Y., Li,X., Ma,X., Huang,Y. and Zhang,X.
  TITLE     Upregulation of serine metabolism enzyme PSAT1 predicts poor
            prognosis and promotes proliferation, metastasis and drug
            resistance of clear cell renal cell carcinoma
  JOURNAL   Exp Cell Res 437 (1), 113977 (2024)
   PUBMED   38373588
  REMARK    GeneRIF: Upregulation of serine metabolism enzyme PSAT1 predicts
            poor prognosis and promotes proliferation, metastasis and drug
            resistance of clear cell renal cell carcinoma.
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Vie,N., Copois,V., Bascoul-Mollevi,C., Denis,V., Bec,N., Robert,B.,
            Fraslon,C., Conseiller,E., Molina,F., Larroque,C., Martineau,P.,
            Del Rio,M. and Gongora,C.
  TITLE     Overexpression of phosphoserine aminotransferase PSAT1 stimulates
            cell growth and increases chemoresistance of colon cancer cells
  JOURNAL   Mol Cancer 7, 14 (2008)
   PUBMED   18221502
  REMARK    GeneRIF: Overexpression of phosphoserine aminotransferase is
            associated with colorectal cancer development
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Hart,C.E., Race,V., Achouri,Y., Wiame,E., Sharrard,M., Olpin,S.E.,
            Watkinson,J., Bonham,J.R., Jaeken,J., Matthijs,G. and Van
            Schaftingen,E.
  TITLE     Phosphoserine aminotransferase deficiency: a novel disorder of the
            serine biosynthesis pathway
  JOURNAL   Am J Hum Genet 80 (5), 931-937 (2007)
   PUBMED   17436247
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Baek,J.Y., Jun,D.Y., Taub,D. and Kim,Y.H.
  TITLE     Characterization of human phosphoserine aminotransferase involved
            in the phosphorylated pathway of L-serine biosynthesis
  JOURNAL   Biochem J 373 (Pt 1), 191-200 (2003)
   PUBMED   12633500
  REMARK    GeneRIF: nucleotide sequence and enzymatic activity of two isoforms
            generated by alternative splicing; differential expression
            depending upon tissue specificity and cellular proliferation status
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Basurko,M.J., Marche,M., Darriet,M. and Cassaigne,A.
  TITLE     Phosphoserine aminotransferase, the second step-catalyzing enzyme
            for serine biosynthesis
  JOURNAL   IUBMB Life 48 (5), 525-529 (1999)
   PUBMED   10637769
REFERENCE   9  (residues 1 to 370)
  AUTHORS   van der Crabben,S.N. and de Koning,T.J.
  TITLE     Serine Deficiency Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37347880
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Misrahi,M., Atger,M. and Milgrom,E.
  TITLE     A novel progesterone-induced messenger RNA in rabbit and human
            endometria. Cloning and sequence analysis of the complementary DNA
  JOURNAL   Biochemistry 26 (13), 3975-3982 (1987)
   PUBMED   3651428
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC332195.1 and BC004863.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the class-V
            pyridoxal-phosphate-dependent aminotransferase family. The encoded
            protein is a phosphoserine aminotransferase and decreased
            expression may be associated with schizophrenia. Mutations in this
            gene are also associated with phosphoserine aminotransferase
            deficiency. Alternative splicing results in multiple transcript
            variants. Pseudogenes of this gene have been defined on chromosomes
            1, 3, and 8. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1, also known as PSAT
            beta).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.625555.1,
                                           SRR3476690.325692.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376588.4/ ENSP00000365773.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.2"
     Protein         1..370
                     /product="phosphoserine aminotransferase isoform 1"
                     /EC_number="2.6.1.52"
                     /note="endometrial progesterone-induced protein;
                     phosphohydroxythreonine aminotransferase; phosphoserine
                     transaminase"
                     /calculated_mol_wt=40292
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9Y617.2)"
     Region          8..366
                     /region_name="PSAT_like"
                     /note="Phosphoserine aminotransferase (PSAT) family. This
                     family belongs to pyridoxal phosphate (PLP)-dependent
                     aspartate aminotransferase superfamily (fold I). The major
                     group in this CD corresponds to phosphoserine
                     aminotransferase (PSAT). PSAT is active as...; cd00611"
                     /db_xref="CDD:99736"
     Site            order(9,14..15,17,76..77,80,114,117..118,205,241..243)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99736"
     Site            order(12,79..80,107,156,176,199..200,335)
                     /site_type="active"
                     /note="substrate-cofactor binding pocket [active]"
                     /db_xref="CDD:99736"
     Site            51
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y617.2)"
     Site            order(78..80,107,156,176,178,199..200)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99736"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99K85; propagated from
                     UniProtKB/Swiss-Prot (Q9Y617.2)"
     Site            200
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99736"
     Site            269
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y617.2)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y617.2)"
     Site            323
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y617.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y617.2)"
     Site            333
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y617.2)"
     CDS             1..370
                     /gene="PSAT1"
                     /gene_synonym="EPIP; NLS2; PSA; PSAT; PSATD"
                     /coded_by="NM_058179.4:87..1199"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6660.1"
                     /db_xref="GeneID:29968"
                     /db_xref="HGNC:HGNC:19129"
                     /db_xref="MIM:610936"
ORIGIN      
        1 mdaprqvvnf gpgpaklphs vlleiqkell dykgvgisvl emshrssdfa kiinntenlv
       61 rellavpdny kviflqgggc gqfsavplnl iglkagrcad yvvtgawsak aaeeakkfgt
      121 inivhpklgs ytkipdpstw nlnpdasyvy ycanetvhgv efdfipdvkg avlvcdmssn
      181 flskpvdvsk fgvifagaqk nvgsagvtvv ivrddllgfa lrecpsvley kvqagnssly
      241 ntppcfsiyv mglvlewikn nggaaamekl ssiksqtiye iidnsqgfyv cpvepqnrsk
      301 mnipfrigna kgddalekrf ldkalelnml slkghrsvgg iraslynavt iedvqklaaf
      361 mkkflemhql
//
LOCUS       NP_689740                510 aa            linear   PRI 27-APR-2025
DEFINITION  monocarboxylate transporter 14 [Homo sapiens].
ACCESSION   NP_689740
VERSION     NP_689740.2
DBSOURCE    REFSEQ: accession NM_152527.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Roshanbin,S., Lindberg,F.A., Lekholm,E., Eriksson,M.M., Perland,E.,
            Ahlund,J., Raine,A. and Fredriksson,R.
  TITLE     Histological characterization of orphan transporter MCT14
            (SLC16A14) shows abundant expression in mouse CNS and kidney
  JOURNAL   BMC Neurosci 17 (1), 43 (2016)
   PUBMED   27364523
  REMARK    GeneRIF: Study presented a phylogenetic analysis revealing that
            Slc16a14 is closely related to Slc16a2, Slc16a9 and Slc16a10;
            provided a detailed expression analysis of Slc16a14 expression,
            finding widespread expression in the mouse brain and establishing
            its expression in neurons and epithelial cells. QRT-PCR on a panel
            of mouse tissues revealed high Slc16a14 expression in the kidney
            and moderate levels in the CNS.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Halestrap,A.P. and Meredith,D.
  TITLE     The SLC16 gene family-from monocarboxylate transporters (MCTs) to
            aromatic amino acid transporters and beyond
  JOURNAL   Pflugers Arch 447 (5), 619-628 (2004)
   PUBMED   12739169
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA044472.1, BC065524.1 and AL833470.1.
            
            On Jan 26, 2004 this sequence version replaced NP_689740.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.9485.1,
                                           SRR1660807.22601.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267770 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295190.9/ ENSP00000295190.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q36.3"
     Protein         1..510
                     /product="monocarboxylate transporter 14"
                     /note="solute carrier family 16 (monocarboxylic acid
                     transporters), member 14; MCT 14; monocarboxylic acid
                     transporter 14"
                     /calculated_mol_wt=56123
     Site            28..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Region          33..492
                     /region_name="MFS_MCT14"
                     /note="Monocarboxylate transporter 14 of the Major
                     Facilitator Superfamily of transporters; cd17429"
                     /db_xref="CDD:340987"
     Site            order(44..45,48..49,52,87,138..139,141..143,146,165,
                     168..169,172,323,326..327,330..332,335,363,367,418..419,
                     423,427,442,445..446,449..450,453)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340987"
     Site            74..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Site            127..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Site            191..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Region          214..255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Site            315..335
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Site            353..373
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Site            379..399
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Site            408..428
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Site            443..463
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     Site            474..494
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTX9.1)"
     CDS             1..510
                     /gene="SLC16A14"
                     /gene_synonym="MCT14"
                     /coded_by="NM_152527.5:385..1917"
                     /db_xref="CCDS:CCDS2473.1"
                     /db_xref="GeneID:151473"
                     /db_xref="HGNC:HGNC:26417"
ORIGIN      
        1 mytshedigy dfedgpkdkk tlkphpnidg gwawmmvlss ffvhilimgs qmalgvlnve
       61 wleefhqsrg ltawvsslsm gitlivgpfi glfintcgcr qtaiigglvn slgwvlsaya
      121 anvhylfitf gvaaglgsgm aylpavvmvg ryfqkrrala qglsttgtgf gtflmtvllk
      181 ylcaeygwrn amliqgavsl nlcvcgalmr plspgknpnd pgekdvrglp ahstesvkst
      241 gqqgrteekd gglgneetlc dlqaqecpdq aghrknmcal rilktvswlt mrvrkgfedw
      301 ysgyfgtasl ftnrmfvafi fwalfayssf vipfihlpei vnlynlseqn dvfpltsiia
      361 ivhifgkvil gviadlpcis vwnvfllanf tlvlsifilp lmhtyaglav icaligfssg
      421 yfslmpvvte dlvgiehlan aygiiicang isallgppfa gwiyditqky dfsfyicgll
      481 ymigilflli qpciriieqs rrkymdgahv
//
LOCUS       NP_060753                164 aa            linear   PRI 27-APR-2025
DEFINITION  nucleotide triphosphate diphosphatase NUDT15 isoform 1 [Homo
            sapiens].
ACCESSION   NP_060753
VERSION     NP_060753.1
DBSOURCE    REFSEQ: accession NM_018283.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Sabirova,Z., Mahnoor,S., Lasfar,D., Gagne,V., Theoret,Y.,
            Leclerc,J.M., Laverdiere,C., Sinnett,D., Tran,T.H. and
            Krajinovic,M.
  TITLE     Novel variant in Nudix hydrolase 15 gene influences
            6-mercaptopurine toxicity in childhood acute lymphoblastic leukemia
            patients
  JOURNAL   Pharmacogenet Genomics 34 (5), 170-173 (2024)
   PUBMED   38682355
  REMARK    GeneRIF: Novel variant in Nudix hydrolase 15 gene influences
            6-mercaptopurine toxicity in childhood acute lymphoblastic leukemia
            patients.
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Rosdiana,D.S., Saputri,D.S., Louisa,M. and Setiabudy,R.
  TITLE     NUDT15 Polymorphism and Its Association With Mercaptopurine
            Hematotoxicity in Acute Lymphoblastic Leukemia in Indonesian
            Children
  JOURNAL   In Vivo 38 (4), 2041-2048 (2024)
   PUBMED   38936894
  REMARK    GeneRIF: NUDT15 Polymorphism and Its Association With
            Mercaptopurine Hematotoxicity in Acute Lymphoblastic Leukemia in
            Indonesian Children.
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Du,S., Huang,X., He,X., Mao,M., Chen,M., Zhang,R., Shao,H., Lv,Z.,
            Liu,X. and Chuan,J.
  TITLE     Association of NUDT15 gene polymorphism with adverse reaction,
            treatment efficacy, and dose of 6-mercaptopurine in patients with
            acute lymphoblastic leukemia: a systematic review and meta-analysis
  JOURNAL   Haematologica 109 (4), 1053-1068 (2024)
   PUBMED   37794799
  REMARK    GeneRIF: Association of NUDT15 gene polymorphism with adverse
            reaction, treatment efficacy, and dose of 6-mercaptopurine in
            patients with acute lymphoblastic leukemia: a systematic review and
            meta-analysis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 164)
  AUTHORS   von Muhlenbrock,C., Estay,C., Covarrubias,N., Miranda,J. and
            Venegas,M.
  TITLE     The c.415C>T polymorphism in NUDT15 is more frequent than the
            polymorphisms in TPMT in Chilean patients who use thiopurine drugs
  JOURNAL   Pharmacogenet Genomics 33 (7), 161-163 (2023)
   PUBMED   37556121
  REMARK    GeneRIF: The c.415C>T polymorphism in NUDT15 is more frequent than
            the polymorphisms in TPMT in Chilean patients who use thiopurine
            drugs.
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Moriyama,T., Nishii,R., Perez-Andreu,V., Yang,W., Klussmann,F.A.,
            Zhao,X., Lin,T.N., Hoshitsuki,K., Nersting,J., Kihira,K.,
            Hofmann,U., Komada,Y., Kato,M., McCorkle,R., Li,L., Koh,K.,
            Najera,C.R., Kham,S.K., Isobe,T., Chen,Z., Chiew,E.K., Bhojwani,D.,
            Jeffries,C., Lu,Y., Schwab,M., Inaba,H., Pui,C.H., Relling,M.V.,
            Manabe,A., Hori,H., Schmiegelow,K., Yeoh,A.E., Evans,W.E. and
            Yang,J.J.
  TITLE     NUDT15 polymorphisms alter thiopurine metabolism and hematopoietic
            toxicity
  JOURNAL   Nat Genet 48 (4), 367-373 (2016)
   PUBMED   26878724
  REMARK    GeneRIF: Patients with defective NUDT15 alleles showed excessive
            levels of thiopurine active metabolites and toxicity.
            [meta-analysis]
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Yang,S.K., Hong,M., Baek,J., Choi,H., Zhao,W., Jung,Y.,
            Haritunians,T., Ye,B.D., Kim,K.J., Park,S.H., Park,S.K., Yang,D.H.,
            Dubinsky,M., Lee,I., McGovern,D.P., Liu,J. and Song,K.
  TITLE     A common missense variant in NUDT15 confers susceptibility to
            thiopurine-induced leukopenia
  JOURNAL   Nat Genet 46 (9), 1017-1020 (2014)
   PUBMED   25108385
  REMARK    GeneRIF: Authros identified a nonsynonymous SNP in NUDT15 (encoding
            p.Arg139Cys) that was strongly associated with thiopurine-induced
            early leukopenia (odds ratio (OR) = 35.6; P(combined) = 4.88 x
            10(-94)).
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Takagi,Y., Setoyama,D., Ito,R., Kamiya,H., Yamagata,Y. and
            Sekiguchi,M.
  TITLE     Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine
            and deoxyguanosine diphosphates: comparison with MTH1 and MTH2
  JOURNAL   J Biol Chem 287 (25), 21541-21549 (2012)
   PUBMED   22556419
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Hori,M., Satou,K., Harashima,H. and Kamiya,H.
  TITLE     Suppression of mutagenesis by 8-hydroxy-2'-deoxyguanosine
            5'-triphosphate (7,8-dihydro-8-oxo-2'-deoxyguanosine
            5'-triphosphate) by human MTH1, MTH2, and NUDT5
  JOURNAL   Free Radic Biol Med 48 (9), 1197-1201 (2010)
   PUBMED   20144704
  REMARK    GeneRIF: human MTH1, MTH2, and NUDT5 proteins act as a defense
            against the mutagenesis induced by oxidized dGTP.
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Yu,Y., Cai,J.P., Tu,B., Wu,L., Zhao,Y., Liu,X., Li,L., McNutt,M.A.,
            Feng,J., He,Q., Yang,Y., Wang,H., Sekiguchi,M. and Zhu,W.G.
  TITLE     Proliferating cell nuclear antigen is protected from degradation by
            forming a complex with MutT Homolog2
  JOURNAL   J Biol Chem 284 (29), 19310-19320 (2009)
   PUBMED   19419956
  REMARK    GeneRIF: Data demonstrate for the first time that PCNA is protected
            by this newly identified partner molecule MTH2, which is related to
            DNA synthesis and cell cycle progression.
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Cai,J.P., Ishibashi,T., Takagi,Y., Hayakawa,H. and Sekiguchi,M.
  TITLE     Mouse MTH2 protein which prevents mutations caused by 8-oxoguanine
            nucleotides
  JOURNAL   Biochem Biophys Res Commun 305 (4), 1073-1077 (2003)
   PUBMED   12767940
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK001818.1 and BC064607.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an enzyme that belongs to the Nudix
            hydrolase superfamily. Members of this superfamily catalyze the
            hydrolysis of nucleoside diphosphates, including substrates like
            8-oxo-dGTP, which are a result of oxidative damage, and can induce
            base mispairing during DNA replication, causing transversions. The
            encoded enzyme is a negative regulator of thiopurine activation and
            toxicity. Mutations in this gene result in poor metabolism of
            thiopurines, and are associated with thiopurine-induced early
            leukopenia. Multiple pseudogenes of this gene have been identified.
            [provided by RefSeq, Apr 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064607.1, SRR5189661.70458.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258662.3/ ENSP00000258662.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..164
                     /product="nucleotide triphosphate diphosphatase NUDT15
                     isoform 1"
                     /EC_number="3.6.1.9"
                     /note="probable 7,8-dihydro-8-oxoguanine triphosphatase
                     NUDT15; nucleoside diphosphate-linked to another moiety X
                     hydrolase 15; nucleotide triphosphate diphosphatase
                     NUDT15; mutT homolog 2; 8-oxo-dGTPase NUDT15; probable
                     8-oxo-dGTP diphosphatase NUDT15; nudix (nucleoside
                     diphosphate linked moiety X)-type motif 15"
                     /calculated_mol_wt=18478
     Region          24..143
                     /region_name="NUDIX_MTH2_Nudt15"
                     /note="MutT homolog 2; cd04678"
                     /db_xref="CDD:467561"
     Region          48..69
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NV35.1)"
     Region          76..164
                     /region_name="Interaction with PCNA.
                     /evidence=ECO:0000269|PubMed:19419956"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NV35.1)"
     CDS             1..164
                     /gene="NUDT15"
                     /gene_synonym="MTH2; NUDT15D"
                     /coded_by="NM_018283.4:22..516"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9407.1"
                     /db_xref="GeneID:55270"
                     /db_xref="HGNC:HGNC:23063"
                     /db_xref="MIM:615792"
ORIGIN      
        1 mtasaqprgr rpgvgvgvvv tsckhprcvl lgkrkgsvga gsfqlpgghl efgetweeca
       61 qretweeaal hlknvhfasv vnsfiekeny hyvtilmkge vdvthdsepk nvepeknesw
      121 ewvpweelpp ldqlfwglrc lkeqgydpfk edlnhlvgyk gnhl
//
LOCUS       NP_062378                564 aa            linear   ROD 27-APR-2025
DEFINITION  diacylglycerol kinase epsilon isoform 1 [Mus musculus].
ACCESSION   NP_062378
VERSION     NP_062378.1
DBSOURCE    REFSEQ: accession NM_019505.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Traczyk,G., Hromada-Judycka,A., Swiatkowska,A., Wisniewska,J.,
            Ciesielska,A. and Kwiatkowska,K.
  TITLE     Diacylglycerol kinase-epsilon is S-palmitoylated on cysteine in the
            cytoplasmic end of its N-terminal transmembrane fragment
  JOURNAL   J Lipid Res 65 (1), 100480 (2024)
   PUBMED   38008259
  REMARK    GeneRIF: Diacylglycerol kinase-epsilon is S-palmitoylated on
            cysteine in the cytoplasmic end of its N-terminal transmembrane
            fragment.
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Nakano,T., Suzuki,A. and Goto,K.
  TITLE     Ablation of diacylglycerol kinase epsilon promotes whitening of
            brown adipose tissue under high fat diet feeding
  JOURNAL   Adv Biol Regul 91, 100994 (2024)
   PUBMED   37875386
  REMARK    GeneRIF: Ablation of diacylglycerol kinase epsilon promotes
            whitening of brown adipose tissue under high fat diet feeding.
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Wang,Z., Zhou,Z., Zhang,Y., Zuo,F., Du,J., Wang,M., Hu,M., Sun,Y.,
            Wang,X., Liu,M., Zhang,Y., Tang,W. and Yi,F.
  TITLE     Diacylglycerol kinase epsilon protects against renal
            ischemia/reperfusion injury in mice through Kruppel-like factor
            15/klotho pathway
  JOURNAL   Ren Fail 44 (1), 902-913 (2022)
   PUBMED   35616094
  REMARK    GeneRIF: Diacylglycerol kinase epsilon protects against renal
            ischemia/reperfusion injury in mice through Kruppel-like factor
            15/klotho pathway.
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Traczyk,G., Swiatkowska,A., Hromada-Judycka,A., Janikiewicz,J. and
            Kwiatkowska,K.
  TITLE     An intact zinc finger motif of the C1B domain is critical for
            stability and activity of diacylglycerol kinase-epsilon
  JOURNAL   Int J Biochem Cell Biol 152, 106295 (2022)
   PUBMED   36113832
  REMARK    GeneRIF: An intact zinc finger motif of the C1B domain is critical
            for stability and activity of diacylglycerol kinase-epsilon.
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Crotty,T., Cai,J., Sakane,F., Taketomi,A., Prescott,S.M. and
            Topham,M.K.
  TITLE     Diacylglycerol kinase delta regulates protein kinase C and
            epidermal growth factor receptor signaling
  JOURNAL   Proc Natl Acad Sci U S A 103 (42), 15485-15490 (2006)
   PUBMED   17021016
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Desai,J., Shannon,M.E., Johnson,M.D., Ruff,D.W., Hughes,L.A.,
            Kerley,M.K., Carpenter,D.A., Johnson,D.K., Rinchik,E.M. and
            Culiat,C.T.
  TITLE     Nell1-deficient mice have reduced expression of extracellular
            matrix proteins causing cranial and vertebral defects
  JOURNAL   Hum Mol Genet 15 (8), 1329-1341 (2006)
   PUBMED   16537572
REFERENCE   8  (residues 1 to 564)
  AUTHORS   Lukiw,W.J., Cui,J.G., Musto,A.E., Musto,B.C. and Bazan,N.G.
  TITLE     Epileptogenesis in diacylglycerol kinase epsilon deficiency
            up-regulates COX-2 and tyrosine hydroxylase in hippocampus
  JOURNAL   Biochem Biophys Res Commun 338 (1), 77-81 (2005)
   PUBMED   16137646
  REMARK    GeneRIF: A regulatory role is suggested for DGK epsilon, COX-2, and
            catecholamine signaling during kindling epileptogenesis.
REFERENCE   9  (residues 1 to 564)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 564)
  AUTHORS   Rodriguez de Turco,E.B., Tang,W., Topham,M.K., Sakane,F.,
            Marcheselli,V.L., Chen,C., Taketomi,A., Prescott,S.M. and
            Bazan,N.G.
  TITLE     Diacylglycerol kinase epsilon regulates seizure susceptibility and
            long-term potentiation through arachidonoyl- inositol lipid
            signaling
  JOURNAL   Proc Natl Acad Sci U S A 98 (8), 4740-4745 (2001)
   PUBMED   11287665
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK147841.1, BB635763.1, AK049335.1 and AL646096.8.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK049335.1, SRR9219381.335362.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 54.34 cM"
     Protein         1..564
                     /product="diacylglycerol kinase epsilon isoform 1"
                     /EC_number="2.7.1.107"
                     /note="DAG kinase epsilon; diglyceride kinase epsilon"
                     /calculated_mol_wt=63504
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1C6.1)"
     Region          55..108
                     /region_name="C1_DGKepsilon_typeIII_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in type III diacylglycerol kinase, DAG
                     kinase epsilon, and similar proteins; cd20801"
                     /db_xref="CDD:410351"
     Site            order(58,72,75,85,88,93,96,106)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:410351"
     Region          122..186
                     /region_name="C1_DGKepsilon_typeIII_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in type III diacylglycerol kinase, DAG
                     kinase epsilon, and similar proteins; cd20853"
                     /db_xref="CDD:410403"
     Region          218..346
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          366..521
                     /region_name="DAGKa"
                     /note="Diacylglycerol kinase accessory domain (presumed);
                     smart00045"
                     /db_xref="CDD:214486"
     CDS             1..564
                     /gene="Dgke"
                     /gene_synonym="DAGK6; DGK; DGK-epsilon"
                     /coded_by="NM_019505.4:364..2058"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS25234.1"
                     /db_xref="GeneID:56077"
                     /db_xref="MGI:MGI:1889276"
ORIGIN      
        1 megdqrsgpp aqsllpdghl vlwtlcsvll pvfitlwcsl qrsrrqlhrr difrkskhcw
       61 rdtdlfshpt yccvcaqhil qgafcdccgl rvdegclkkv dkrfpckeim lkndkaadam
      121 phhwirgnvp lcsycvfcrq qcgsqpklcd yrciwcqktv hdecmrgslr sekcdfgefr
      181 nliippsylt sinqmrkdkn tnyeglaskf gkqwtpliil ansrsgtnmg egllgefkil
      241 lnpvqvfdvt ktppikalql ctllpyysvr vlvcggdgtv gwvldaidem kikgqekyip
      301 evavlplgtg ndlsntlgwg tgyageipva qvlrnvmead gikldrwkvq vtnkgyynlr
      361 kpkeftmnny fsvgpdalma lnfhahreka pslfssriln kavylfygtk dclvqeckdl
      421 nkkieleldg ervelpnleg iivlnigywg ggcrlwegmg detyplarhd dglleivgvy
      481 gsfhcaqiqv klanpfrigq ahtvrltlkc smmpmqvdge pwaqgpctvt ithkthalml
      541 yfsgeqsddd isspsdhedv keae
//
LOCUS       NP_001356622             186 aa            linear   PRI 27-APR-2025
DEFINITION  deoxyhypusine synthase isoform g [Homo sapiens].
ACCESSION   NP_001356622 XP_024307174
VERSION     NP_001356622.1
DBSOURCE    REFSEQ: accession NM_001369693.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Liao,T.Y., Huang,Y.T., Lee,T.F., Hsueh,P.R., Yu,C.J. and Chien,J.Y.
  TITLE     Clinical significance of mutations in dihydropteroate synthase in
            Pneumocystis jirovecii pneumonia among non-HIV-infected patients
  JOURNAL   Int J Antimicrob Agents 63 (1), 107019 (2024)
   PUBMED   37925109
  REMARK    GeneRIF: Clinical significance of mutations in dihydropteroate
            synthase in Pneumocystis jirovecii pneumonia among non-HIV-infected
            patients.
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Padgett,L.R., Shinkle,M.R., Rosario,S., Stewart,T.M., Foley,J.R.,
            Casero,R.A. Jr., Park,M.H., Chung,W.K. and Mastracci,T.L.
  TITLE     Deoxyhypusine synthase mutations alter the post-translational
            modification of eukaryotic initiation factor 5A resulting in
            impaired human and mouse neural homeostasis
  JOURNAL   HGG Adv 4 (3), 100206 (2023)
   PUBMED   37333770
  REMARK    GeneRIF: Deoxyhypusine synthase mutations alter the
            post-translational modification of eukaryotic initiation factor 5A
            resulting in impaired human and mouse neural homeostasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Wator,E., Wilk,P., Biela,A., Rawski,M., Zak,K.M., Steinchen,W.,
            Bange,G., Glatt,S. and Grudnik,P.
  TITLE     Cryo-EM structure of human eIF5A-DHS complex reveals the molecular
            basis of hypusination-associated neurodegenerative disorders
  JOURNAL   Nat Commun 14 (1), 1698 (2023)
   PUBMED   36973244
  REMARK    GeneRIF: Cryo-EM structure of human eIF5A-DHS complex reveals the
            molecular basis of hypusination-associated neurodegenerative
            disorders.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Becker,A.E., Wu,P.K. and Park,J.I.
  TITLE     eIF5A-Independent Role of DHPS in p21CIP1 and Cell Fate Regulation
  JOURNAL   Int J Mol Sci 22 (24), 13187 (2021)
   PUBMED   34947982
  REMARK    GeneRIF: eIF5A-Independent Role of DHPS in p21(CIP1) and Cell Fate
            Regulation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Yan,Y.P., Tao,Y. and Chen,K.Y.
  TITLE     Molecular cloning and functional expression of human deoxyhypusine
            synthase cDNA based on expressed sequence tag information
  JOURNAL   Biochem J 315 (Pt 2) (Pt 2), 429-434 (1996)
   PUBMED   8615810
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Bevec,D., Kappel,B., Jaksche,H., Csonga,R., Hauber,J., Klier,H. and
            Steinkasserer,A.
  TITLE     Molecular characterization of a cDNA encoding functional human
            deoxyhypusine synthase and chromosomal mapping of the corresponding
            gene locus
  JOURNAL   FEBS Lett 378 (2), 195-198 (1996)
   PUBMED   8549832
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Joe,Y.A., Wolff,E.C. and Park,M.H.
  TITLE     Cloning and expression of human deoxyhypusine synthase cDNA.
            Structure-function studies with the recombinant enzyme and mutant
            proteins
  JOURNAL   J Biol Chem 270 (38), 22386-22392 (1995)
   PUBMED   7673224
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Klier,H., Csonga,R., Steinkasserer,A., Wohl,T., Lottspeich,F. and
            Eder,J.
  TITLE     Purification and characterization of human deoxyhypusine synthase
            from HeLa cells
  JOURNAL   FEBS Lett 364 (2), 207-210 (1995)
   PUBMED   7750572
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Joe,Y.A. and Park,M.H.
  TITLE     Structural features of the eIF-5A precursor required for
            posttranslational synthesis of deoxyhypusine
  JOURNAL   J Biol Chem 269 (41), 25916-25921 (1994)
   PUBMED   7929297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010422.7.
            
            On Apr 15, 2019 this sequence version replaced XP_024307174.1.
            
            Summary: This gene encodes a protein that is required for the
            formation of hypusine, a unique amino acid formed by the
            posttranslational modification of only one protein, eukaryotic
            translation initiation factor 5A. The encoded protein catalyzes the
            first step in hypusine formation by transferring the butylamine
            moiety of spermidine to a specific lysine residue of the eukaryotic
            translation initiation factor 5A precursor, forming an intermediate
            deoxyhypusine residue. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene.
            [provided by RefSeq, May 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.162140.1,
                                           SRR1803612.275609.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..186
                     /product="deoxyhypusine synthase isoform g"
                     /EC_number="2.5.1.46"
                     /note="migration-inducing gene 13"
                     /calculated_mol_wt=20518
     Region          <1..171
                     /region_name="DS"
                     /note="Deoxyhypusine synthase; pfam01916"
                     /db_xref="CDD:460382"
     CDS             1..186
                     /gene="DHPS"
                     /gene_synonym="DHS; DS; MIG13; NEDSSWI"
                     /coded_by="NM_001369693.1:629..1189"
                     /note="isoform g is encoded by transcript variant 8"
                     /db_xref="GeneID:1725"
                     /db_xref="HGNC:HGNC:2869"
                     /db_xref="MIM:600944"
ORIGIN      
        1 mpildqmvme qntegvkwtp skmiarlgke innpesvyyw aqknhipvfs paltdgslgd
       61 miffhsyknp glvldivedl rlintqaifa kctgmiilgg gvvkhhiana nlmrngadya
      121 vyintaqefd gsdsgarpde avswgkirvd aqpvkvyada slvfpllvae tfaqkmdafm
      181 hekned
//
LOCUS       NP_037490                663 aa            linear   PRI 27-APR-2025
DEFINITION  protein-arginine deiminase type-1 [Homo sapiens].
ACCESSION   NP_037490
VERSION     NP_037490.2
DBSOURCE    REFSEQ: accession NM_013358.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Padhi,A., Srivastava,A., Ramesh,A., Ehrstrom,M., Simon,M.,
            Sonkoly,E., Eidsmo,L., Bergman,P. and Lysell,J.
  TITLE     IL-22 Downregulates Peptidylarginine Deiminase-1 in Human
            Keratinocytes: Adding Another Piece to the IL-22 Puzzle in
            Epidermal Barrier Formation
  JOURNAL   J Invest Dermatol 142 (2), 333-342 (2022)
   PUBMED   34352263
  REMARK    GeneRIF: IL-22 Downregulates Peptidylarginine Deiminase-1 in Human
            Keratinocytes: Adding Another Piece to the IL-22 Puzzle in
            Epidermal Barrier Formation.
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Coassolo,S., Davidson,G., Negroni,L., Gambi,G., Daujat,S.,
            Romier,C. and Davidson,I.
  TITLE     Citrullination of pyruvate kinase M2 by PADI1 and PADI3 regulates
            glycolysis and cancer cell proliferation
  JOURNAL   Nat Commun 12 (1), 1718 (2021)
   PUBMED   33741961
  REMARK    GeneRIF: Citrullination of pyruvate kinase M2 by PADI1 and PADI3
            regulates glycolysis and cancer cell proliferation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Mechin,M.C., Takahara,H. and Simon,M.
  TITLE     Deimination and Peptidylarginine Deiminases in Skin Physiology and
            Diseases
  JOURNAL   Int J Mol Sci 21 (2), 566 (2020)
   PUBMED   31952341
  REMARK    GeneRIF: Deimination and Peptidylarginine Deiminases in Skin
            Physiology and Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Qin,H., Liu,X., Li,F., Miao,L., Li,T., Xu,B., An,X., Muth,A.,
            Thompson,P.R., Coonrod,S.A. and Zhang,X.
  TITLE     PAD1 promotes epithelial-mesenchymal transition and metastasis in
            triple-negative breast cancer cells by regulating MEK1-ERK1/2-MMP2
            signaling
  JOURNAL   Cancer Lett 409, 30-41 (2017)
   PUBMED   28844713
  REMARK    GeneRIF: Authors showed that PAD1 interacts with and citrullinates
            MEK1 thereby disrupting MEK1-catalyzed ERK1/2 phosphorylation, thus
            leading to the MMP2 overexpression.
REFERENCE   6  (residues 1 to 663)
  AUTHORS   Nachat,R., Mechin,M.C., Takahara,H., Chavanas,S., Charveron,M.,
            Serre,G. and Simon,M.
  TITLE     Peptidylarginine deiminase isoforms 1-3 are expressed in the
            epidermis and involved in the deimination of K1 and filaggrin
  JOURNAL   J Invest Dermatol 124 (2), 384-393 (2005)
   PUBMED   15675958
  REMARK    GeneRIF: PAD1 and 3 are able to modify filaggrin
REFERENCE   7  (residues 1 to 663)
  AUTHORS   Chavanas,S., Mechin,M.C., Takahara,H., Kawada,A., Nachat,R.,
            Serre,G. and Simon,M.
  TITLE     Comparative analysis of the mouse and human peptidylarginine
            deiminase gene clusters reveals highly conserved non-coding
            segments and a new human gene, PADI6
  JOURNAL   Gene 330, 19-27 (2004)
   PUBMED   15087120
REFERENCE   8  (residues 1 to 663)
  AUTHORS   Iida,A. and Nakamura,Y.
  TITLE     Identification of 45 novel SNPs in the 83-kb region containing
            peptidylarginine deiminase types 1 and 3 loci on chromosomal band
            1p36.13
  JOURNAL   J Hum Genet 49 (7), 387-390 (2004)
   PUBMED   15150696
  REMARK    GeneRIF: peptidylarginine deiminase types 1 and 3 loci map to
            chromosomal band 1p36.13
REFERENCE   9  (residues 1 to 663)
  AUTHORS   Vossenaar,E.R., Zendman,A.J., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     PAD, a growing family of citrullinating enzymes: genes, features
            and involvement in disease
  JOURNAL   Bioessays 25 (11), 1106-1118 (2003)
   PUBMED   14579251
  REMARK    Review article
REFERENCE   10 (residues 1 to 663)
  AUTHORS   Guerrin,M., Ishigami,A., Mechin,M.C., Nachat,R., Valmary,S.,
            Sebbag,M., Simon,M., Senshu,T. and Serre,G.
  TITLE     cDNA cloning, gene organization and expression analysis of human
            peptidylarginine deiminase type I
  JOURNAL   Biochem J 370 (Pt 1), 167-174 (2003)
   PUBMED   12416996
  REMARK    GeneRIF: cloning, gene organization, and expression analysis
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590644.14 and BC130574.1.
            
            On Jan 12, 2007 this sequence version replaced NP_037490.1.
            
            Summary: This gene encodes a member of the peptidyl arginine
            deiminase family of enzymes, which catalyze the post-translational
            deimination of proteins by converting arginine residues into
            citrullines in the presence of calcium ions. The family members
            have distinct substrate specificities and tissue-specific
            expression patterns. The type I enzyme is involved in the late
            stages of epidermal differentiation, where it deiminates filaggrin
            and keratin K1, which maintains hydration of the stratum corneum,
            and hence the cutaneous barrier function. This enzyme may also play
            a role in hair follicle formation. This gene exists in a cluster
            with four other paralogous genes. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026652.1, AB033768.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145893, SAMEA2147596
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375471.5/ ENSP00000364620.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..663
                     /product="protein-arginine deiminase type-1"
                     /EC_number="3.5.3.15"
                     /note="hPAD-colony 10; peptidylarginine deiminase I;
                     protein-arginine deiminase type I; peptidyl arginine
                     deiminase, type I"
                     /calculated_mol_wt=74535
     Region          1..113
                     /region_name="PAD_N"
                     /note="Protein-arginine deiminase (PAD) N-terminal domain;
                     pfam08526"
                     /db_xref="CDD:462509"
     Region          115..273
                     /region_name="PAD_M"
                     /note="Protein-arginine deiminase (PAD) middle domain;
                     pfam08527"
                     /db_xref="CDD:462510"
     Region          281..660
                     /region_name="PAD"
                     /note="Protein-arginine deiminase (PAD); pfam03068"
                     /db_xref="CDD:460794"
     CDS             1..663
                     /gene="PADI1"
                     /gene_synonym="HPAD10; PAD1; PDI; PDI1"
                     /coded_by="NM_013358.3:91..2082"
                     /db_xref="CCDS:CCDS178.1"
                     /db_xref="GeneID:29943"
                     /db_xref="HGNC:HGNC:18367"
                     /db_xref="MIM:607934"
ORIGIN      
        1 mapkrvvqls lkmpthavcv vgveahvdih sdvpkgansf rvsgssgvev fmvynrtrvk
       61 epigkarwpl dtdadmvvsv gtaskelkdf kvrvsyfgeq edqalgrsvl yltgvdisle
      121 vdtgrtgkvk rsqgdkktwr wgpegygail lvncdrdnhr saepdlthsw lmsladlqdm
      181 spmllscngp dklfdshklv lnvpfsdskr vrvfcarggn slsdykqvlg pqclsyever
      241 qpgeqeikfy vegltfpdad flglvslsvs lvdpgtlpev tlftdtvgfr mapwimtpnt
      301 qppeelyvcr vmdthgsnek fledmsyltl kancklticp qvenrndrwi qdemefgyie
      361 aphksfpvvf dsprnrglkd fpykrilgpd fgyvtreipl pgpssldsfg nldvsppvtv
      421 ggteyplgri ligssfpksg grqmaravrn flkaqqvqap velysdwlsv ghvdefltfv
      481 ptsdqkgfrl llaspsaclk lfqekkeegy geaaqfdglk hqakrsinem ladrhlqrdn
      541 lhaqkcidwn rnvlkrelgl aesdivdipq lfflknfyae affpdmvnmv vlgkylgipk
      601 pygpiingrc cleekvqsll eplglhcifi ddylsyhelq geihcgtnvr rkpfpfkwwn
      661 mvp
//
LOCUS       NP_001034965             404 aa            linear   PRI 27-APR-2025
DEFINITION  nesprin-4 isoform 1 [Homo sapiens].
ACCESSION   NP_001034965
VERSION     NP_001034965.1
DBSOURCE    REFSEQ: accession NM_001039876.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Gurusaran,M. and Davies,O.R.
  TITLE     A molecular mechanism for LINC complex branching by structurally
            diverse SUN-KASH 6:6 assemblies
  JOURNAL   Elife 10, e60175 (2021)
   PUBMED   33393904
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Cruz,V.E., Esra Demircioglu,F. and Schwartz,T.U.
  TITLE     Structural Analysis of Different LINC Complexes Reveals Distinct
            Binding Modes
  JOURNAL   J Mol Biol 432 (23), 6028-6041 (2020)
   PUBMED   33058875
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Horn,H.F., Brownstein,Z., Lenz,D.R., Shivatzki,S., Dror,A.A.,
            Dagan-Rosenfeld,O., Friedman,L.M., Roux,K.J., Kozlov,S.,
            Jeang,K.T., Frydman,M., Burke,B., Stewart,C.L. and Avraham,K.B.
  TITLE     The LINC complex is essential for hearing
  JOURNAL   J Clin Invest 123 (2), 740-750 (2013)
   PUBMED   23348741
  REMARK    GeneRIF: progressive high-frequency hearing loss in 2 families of
            Iraqi Jewish ancestry was due to homozygosity for mutation SYNE4
            c.228delAT. SYNE4, a gene not previously associated with hearing
            loss, encodes nesprin-4, a protein expressed in outer hair cells.
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Roux,K.J., Crisp,M.L., Liu,Q., Kim,D., Kozlov,S., Stewart,C.L. and
            Burke,B.
  TITLE     Nesprin 4 is an outer nuclear membrane protein that can induce
            kinesin-mediated cell polarization
  JOURNAL   Proc Natl Acad Sci U S A 106 (7), 2194-2199 (2009)
   PUBMED   19164528
REFERENCE   10 (residues 1 to 404)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002116.1, BC038360.1,
            BC052573.1, AF038458.1 and AA991508.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the nesprin family of genes, that
            encode KASH (Klarsicht, Anc-1, Syne Homology) domain-containing
            proteins. In addition to the KASH domain, this protein also
            contains a coiled-coil and leucine zipper region, a spectrin
            repeat, and a kinesin-1 binding region. This protein localizes to
            the outer nuclear membrane, and is part of the linker of
            nucleoskeleton and cytoskeleton (LINC) complex in the nuclear
            envelope. LINC complexes are formed by SUN (Sad1, UNC-84)-KASH
            pairs, and are thought to mechanically couple nuclear components to
            the cytoskeleton. Mutations in this gene have been associated with
            progressive high-frequency hearing loss. The absence of this
            protein in mice also caused hearing loss, and changes in hair cell
            morphology in the ears. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Aug 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279839.2906.1,
                                           SRR3476690.125856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159080 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324444.9/ ENSP00000316130.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..404
                     /product="nesprin-4 isoform 1"
                     /note="nesprin-4; nuclear envelope spectrin repeat protein
                     4; deafness, autosomal recessive 76; KASH
                     domain-containing protein 4"
                     /calculated_mol_wt=43381
     Region          1..91
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N205.2)"
     Region          277..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N205.2)"
     Site            356..376
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N205.2)"
     Region          <369..404
                     /region_name="KASH"
                     /note="Nuclear envelope localization domain; pfam10541"
                     /db_xref="CDD:463142"
     CDS             1..404
                     /gene="SYNE4"
                     /gene_synonym="C19orf46; DFNB76; KASH4; Nesp4"
                     /coded_by="NM_001039876.3:133..1347"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42553.1"
                     /db_xref="GeneID:163183"
                     /db_xref="HGNC:HGNC:26703"
                     /db_xref="MIM:615535"
ORIGIN      
        1 malslplgpr lgseplnhpp gapreadivg ctvcpasgee stspeqaqtl gqdslgppeh
       61 fqggprgnep aahpprwstp ssyedpaggk hcehpisgle vleaeqnslh lcllglgrrl
      121 qdleqglghw alaqsgmvql qalqvdlrga aerveallaf geglaqrsep rawaaleqil
      181 ralgayrdsi frrlwqlqaq lvsyslvfee antldqdlev egdsdwpgpg gvwgpwapss
      241 lptstelewd pagdigglgp lgqktartlg vpcelcgqrg pqgrgqglee adtshsrqdm
      301 lesglghqkr larhqrhsll rkpqdkkrqa sphlqdvrle gnpgapdpas rqpltfllil
      361 fllflllvga mfllpasggp ccshariprt pylvlsyvng lppv
//
LOCUS       NP_001124429             951 aa            linear   PRI 27-APR-2025
DEFINITION  cation channel sperm-associated auxiliary subunit epsilon isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001124429
VERSION     NP_001124429.1
DBSOURCE    REFSEQ: accession NM_001130957.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Chung,J.J., Miki,K., Kim,D., Shim,S.H., Shi,H.F., Hwang,J.Y.,
            Cai,X., Iseri,Y., Zhuang,X. and Clapham,D.E.
  TITLE     CatSperzeta regulates the structural continuity of sperm Ca2+
            signaling domains and is required for normal fertility
  JOURNAL   Elife 6, e23082 (2017)
   PUBMED   28226241
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591594.9, DB462258.1, BC032859.1, BX648685.1, BC028392.1 and
            AC099757.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028392.1, AK302609.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366534.9/ ENSP00000355492.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..951
                     /product="cation channel sperm-associated auxiliary
                     subunit epsilon isoform 1 precursor"
                     /note="uncharacterized protein C1orf101; catSperepsilon;
                     catSper-epsilon; cation channel sperm-associated protein
                     subunit epsilon; cation channel sperm-associated auxiliary
                     subunit epsilon"
                     /calculated_mol_wt=107611
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2069
     mat_peptide     20..951
                     /product="Cation channel sperm-associated auxiliary
                     subunit epsilon. /id=PRO_0000251216"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SY80.1)"
                     /calculated_mol_wt=107611
     Site            61
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Site            114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Site            414
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Site            472
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Site            487
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Site            493
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Site            535
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Region          <699..902
                     /region_name="CATSPERD"
                     /note="Cation channel sperm-associated protein subunit
                     delta; pfam15020"
                     /db_xref="CDD:464451"
     Site            796
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Site            854
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Site            881
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Site            886
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5SY80.1)"
     Site            904..924
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SY80.1)"
     CDS             1..951
                     /gene="CATSPERE"
                     /gene_synonym="C10orf101; C1orf101"
                     /coded_by="NM_001130957.2:158..3013"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS44340.1"
                     /db_xref="GeneID:257044"
                     /db_xref="HGNC:HGNC:28491"
                     /db_xref="MIM:617510"
ORIGIN      
        1 msarevavll lwlscygsal wrystnspny rifstrstik leyegtlfte wsvpetcfvl
       61 nksspttelr csspgvhaik pivtgpdeee rylfvessht cflwyyrvrh ffnnftqlit
      121 vwaydpesad pdellgnaee psinsivlst qmatlgqkpv ihtvlkrkvy ssnekmrrgt
      181 wrivvpmtkd dalkeirgnq vtfqdcfiad flilltfpll tipeipgylp issprgsqlm
      241 aswdacvvas avlvtdmetf httdsfkswt rirvppdils dderrsvahv ilsrdgivfl
      301 ingvlyiksf rgfirlggiv nlpdggitgi ssrkwcwvny llkakgrrst favwteneiy
      361 lgsillkfar lvtttelkni lslsvtatlt idrveytghp leiavflnyc tvcnvtkkif
      421 lviynedtkq wvsqdftlda pidsvtmphf tfsalpglll wnkhsiyycy hnftftgilq
      481 tpaghgnlsm lsndsiihev fidyygdilv kmennvifys kintrdavkl hlwtnyttra
      541 fiflstsgqt yflyalddgt iqiqdyplhl eaqsiafttk dkcpymafhn nvahvfyfld
      601 kgealtvwtq ivypentgly vivesygpki lqesheisfe aafgyctktl tltfyqnvdy
      661 erisdyfetq dkhtglvlvq frpseyskac piaqkvfqia vgcddkkfia ikgfskkgch
      721 hhdfsyviek sylrhqpskn lrvryiwgey gcplrldfte kfqpvvqlfd dngyvkdvea
      781 nfivweihgr ddysfnntma qsgclheaqt wksmielnkh lpleevwgpe nykhcfsyai
      841 gkpgdlnqpy eiinssngnh ifwpmghsgm yvfrvkildp nysfcnltam faietfglip
      901 spsvylvasf lfvlmllfft ilvlsyfrym riyrryiyep lhkpqrkrkk n
//
LOCUS       NP_055100                293 aa            linear   PRI 27-APR-2025
DEFINITION  exosome complex component RRP4 isoform 1 [Homo sapiens].
ACCESSION   NP_055100
VERSION     NP_055100.2
DBSOURCE    REFSEQ: accession NM_014285.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Moll,T., Odon,V., Harvey,C., Collins,M.O., Peden,A., Franklin,J.,
            Graves,E., Marshall,J.N., Dos Santos Souza,C., Zhang,S.,
            Castelli,L., Hautbergue,G., Azzouz,M., Gordon,D., Krogan,N.,
            Ferraiuolo,L., Snyder,M.P., Shaw,P.J., Rehwinkel,J. and
            Cooper-Knock,J.
  TITLE     Low expression of EXOSC2 protects against clinical COVID-19 and
            impedes SARS-CoV-2 replication
  JOURNAL   Life Sci Alliance 6 (1), e202201449 (2022)
   PUBMED   36241425
  REMARK    GeneRIF: Low expression of EXOSC2 protects against clinical
            COVID-19 and impedes SARS-CoV-2 replication.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Sterrett,M.C., Enyenihi,L., Leung,S.W., Hess,L., Strassler,S.E.,
            Farchi,D., Lee,R.S., Withers,E.S., Kremsky,I., Baker,R.E.,
            Basrai,M.A., van Hoof,A., Fasken,M.B. and Corbett,A.H.
  TITLE     A budding yeast model for human disease mutations in the EXOSC2 cap
            subunit of the RNA exosome complex
  JOURNAL   RNA 27 (9), 1046-1067 (2021)
   PUBMED   34162742
  REMARK    GeneRIF: A budding yeast model for human disease mutations in the
            EXOSC2 cap subunit of the RNA exosome complex.
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Mitchell,P., Petfalski,E., Shevchenko,A., Mann,M. and Tollervey,D.
  TITLE     The exosome: a conserved eukaryotic RNA processing complex
            containing multiple 3'-->5' exoribonucleases
  JOURNAL   Cell 91 (4), 457-466 (1997)
   PUBMED   9390555
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Adams,M.D., Dubnick,M., Kerlavage,A.R., Moreno,R., Kelley,J.M.,
            Utterback,T.R., Nagle,J.W., Fields,C. and Venter,J.C.
  TITLE     Sequence identification of 2,375 human brain genes
  JOURNAL   Nature 355 (6361), 632-634 (1992)
   PUBMED   1538749
REFERENCE   8  (residues 1 to 293)
  AUTHORS   Morris,C.M., Heisterkamp,N., Groffen,J. and Fitzgerald,P.H.
  TITLE     Entire ABL gene is joined with 5'-BCR in some patients with
            Philadelphia-positive leukemia
  JOURNAL   Blood 78 (4), 1078-1084 (1991)
   PUBMED   1868241
REFERENCE   9  (residues 1 to 293)
  AUTHORS   Soekarman,D., van Denderen,J., Hoefsloot,L., Moret,M., Meeuwsen,T.,
            van Baal,J., Hagemeijer,A. and Grosveld,G.
  TITLE     A novel variant of the bcr-abl fusion product in Philadelphia
            chromosome-positive acute lymphoblastic leukemia
  JOURNAL   Leukemia 4 (6), 397-403 (1990)
   PUBMED   2193202
REFERENCE   10 (residues 1 to 293)
  AUTHORS   Zhu,Q.S., Heisterkamp,N. and Groffen,J.
  TITLE     Characterization of the human ABL promoter regions
  JOURNAL   Oncogene 5 (6), 885-891 (1990)
   PUBMED   2163052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU934039.1, BC000747.2 and AL359092.14.
            
            On Apr 4, 2002 this sequence version replaced NP_055100.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.38231.1,
                                           SRR1660803.108578.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372358.10/ ENSP00000361433.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.12"
     Protein         1..293
                     /product="exosome complex component RRP4 isoform 1"
                     /note="homolog of yeast RRP4 (ribosomal RNA processing 4),
                     3' 5' exoribonuclease (RRP4); exosome complex exonuclease
                     RRP4; homolog of yeast RRP4 (ribosomal RNA processing 4),
                     3'-5'-exoribonuclease; exosome complex component RRP4;
                     ribosomal RNA-processing protein 4"
                     /calculated_mol_wt=32658
     Region          26..63
                     /region_name="ECR1_N"
                     /note="Exosome complex exonuclease RRP4 N-terminal region;
                     pfam14382"
                     /db_xref="CDD:464162"
     Region          75..166
                     /region_name="S1_Rrp4"
                     /note="Rrp4 S1-like RNA-binding domain. S1-like
                     RNA-binding domains are found in a wide variety of
                     RNA-associated proteins. Rrp4 protein is a subunit of the
                     exosome complex. The exosome plays a central role in 3' to
                     5' RNA processing and degradation in...; cd05789"
                     /db_xref="CDD:240215"
     Site            order(75,87,89,103)
                     /site_type="other"
                     /note="subunit interface [polypeptide binding]"
                     /db_xref="CDD:240215"
     Site            order(89,97,107,109)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:240215"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13868.2)"
     Region          169..285
                     /region_name="KH-I_Rrp4_eukar"
                     /note="type I K homology (KH) RNA-binding domain found in
                     exosome complex component Rrp4 from eukaryote; cd22525"
                     /db_xref="CDD:411953"
     Site            order(169,178,181,183..184,186,204,228,231,234..235,
                     238..239,247..248,268..269,285)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:411953"
     CDS             1..293
                     /gene="EXOSC2"
                     /gene_synonym="hRrp4p; p7; RRP4; Rrp4p; SHRF"
                     /coded_by="NM_014285.7:13..894"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6935.1"
                     /db_xref="GeneID:23404"
                     /db_xref="HGNC:HGNC:17097"
                     /db_xref="MIM:602238"
ORIGIN      
        1 mamemrlpva rkplserlgr dtkkhlvvpg dtittdtgfm rghgtymgee kliasvagsv
       61 ervnklicvk alktryigev gdivvgrite vqqkrwkvet nsrldsvlll ssmnlpggel
      121 rrrsaedela mrgflqegdl isaevqavfs dgavslhtrs lkygklgqgv lvqvspslvk
      181 rqkthfhdlp cgasvilgnn gfiwiyptpe hkeeeaggfi anlepvslad revisrlrnc
      241 iislvtqrmm lydtsilycy easlphqikd ilkpeimeei vmetrqrlle qeg
//
LOCUS       NP_001637                127 aa            linear   PRI 27-APR-2025
DEFINITION  apolipoprotein C-IV precursor [Homo sapiens].
ACCESSION   NP_001637
VERSION     NP_001637.1
DBSOURCE    REFSEQ: accession NM_001646.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Xu,S., Cheng,J., Li,N.H., Chen,Y.N., Cai,M.Y., Tang,S.S., Huang,H.,
            Zhang,B., Cen,J.M., Yang,X.L., Chen,C., Liu,X. and Xiong,X.D.
  TITLE     The association of APOC4 polymorphisms with premature coronary
            artery disease in a Chinese Han population
  JOURNAL   Lipids Health Dis 14, 63 (2015)
   PUBMED   26129832
  REMARK    GeneRIF: APOC4 rs1132899 polymorphism was associated with an
            increased risk of premature coronary artery disease in Chinese
            subjects.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Lemaitre,R.N., King,I.B., Kabagambe,E.K., Wu,J.H., McKnight,B.,
            Manichaikul,A., Guan,W., Sun,Q., Chasman,D.I., Foy,M., Wang,L.,
            Zhu,J., Siscovick,D.S., Tsai,M.Y., Arnett,D.K., Psaty,B.M.,
            Djousse,L., Chen,Y.D., Tang,W., Weng,L.C., Wu,H., Jensen,M.K.,
            Chu,A.Y., Jacobs,D.R. Jr., Rich,S.S., Mozaffarian,D., Steffen,L.,
            Rimm,E.B., Hu,F.B., Ridker,P.M., Fornage,M. and Friedlander,Y.
  TITLE     Genetic loci associated with circulating levels of very long-chain
            saturated fatty acids
  JOURNAL   J Lipid Res 56 (1), 176-184 (2015)
   PUBMED   25378659
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Middelberg,R.P., Ferreira,M.A., Henders,A.K., Heath,A.C.,
            Madden,P.A., Montgomery,G.W., Martin,N.G. and Whitfield,J.B.
  TITLE     Genetic variants in LPL, OASL and TOMM40/APOE-C1-C2-C4 genes are
            associated with multiple cardiovascular-related traits
  JOURNAL   BMC Med Genet 12, 123 (2011)
   PUBMED   21943158
  REMARK    GeneRIF: variants in LPL, OASL and TOMM40/APOE-C1-C2-C4 genes are
            associated with multiple cardiovascular-related traits
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Kotite,L., Zhang,L.H., Yu,Z., Burlingame,A.L. and Havel,R.J.
  TITLE     Human apoC-IV: isolation, characterization, and immunochemical
            quantification in plasma and plasma lipoproteins
  JOURNAL   J Lipid Res 44 (7), 1387-1394 (2003)
   PUBMED   12700345
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Mak,P.A., Laffitte,B.A., Desrumaux,C., Joseph,S.B., Curtiss,L.K.,
            Mangelsdorf,D.J., Tontonoz,P. and Edwards,P.A.
  TITLE     Regulated expression of the apolipoprotein E/C-I/C-IV/C-II gene
            cluster in murine and human macrophages. A critical role for
            nuclear liver X receptors alpha and beta
  JOURNAL   J Biol Chem 277 (35), 31900-31908 (2002)
   PUBMED   12032151
  REMARK    GeneRIF: regulated expression of gene cluster in macrophages
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Kamboh,M.I., Aston,C.E. and Hamman,R.F.
  TITLE     DNA sequence variation in human apolipoprotein C4 gene and its
            effect on plasma lipid profile
  JOURNAL   Atherosclerosis 152 (1), 193-201 (2000)
   PUBMED   10996355
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Dang,Q. and Taylor,J.
  TITLE     In vivo footprinting analysis of the hepatic control region of the
            human apolipoprotein E/C-I/C-IV/C-II gene locus
  JOURNAL   J Biol Chem 271 (45), 28667-28676 (1996)
   PUBMED   8910501
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Allan,C.M. and Taylor,J.M.
  TITLE     Expression of a novel human apolipoprotein (apoC-IV) causes
            hypertriglyceridemia in transgenic mice
  JOURNAL   J Lipid Res 37 (7), 1510-1518 (1996)
   PUBMED   8827523
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Allan,C.M., Walker,D., Segrest,J.P. and Taylor,J.M.
  TITLE     Identification and characterization of a new human gene (APOC4) in
            the apolipoprotein E, C-I, and C-II gene locus
  JOURNAL   Genomics 28 (2), 291-300 (1995)
   PUBMED   8530039
  REMARK    GeneRIF: Includes the observation of APOC4-APOC2 read-through
            transcription
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011481.4, DB185657.1,
            BC020723.1 and AV690709.1.
            
            Summary: This gene encodes a lipid-binding protein belonging to the
            apolipoprotein gene family. The protein is thought to play a role
            in lipid metabolism. Polymorphisms in this gene may influence
            circulating lipid levels and may be associated with coronary artery
            disease risk. This gene is present in a cluster with other related
            apolipoprotein genes on chromosome 19. Naturally occurring
            read-through transcription exists between this gene and the
            neighboring downstream apolipoprotein C-II (APOC2) gene. [provided
            by RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB157508.1, SRR5189664.155939.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145122
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000592954.2/ ENSP00000468236.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..127
                     /product="apolipoprotein C-IV precursor"
                     /note="apolipoprotein C-IV"
                     /calculated_mol_wt=11712
     sig_peptide     1..27
                     /note="/evidence=ECO:0000250|UniProtKB:P55057; propagated
                     from UniProtKB/Swiss-Prot (P55056.1)"
                     /calculated_mol_wt=2859
     mat_peptide     28..127
                     /product="Apolipoprotein C-IV. /id=PRO_0000002036"
                     /note="propagated from UniProtKB/Swiss-Prot (P55056.1)"
                     /calculated_mol_wt=11712
     Region          31..124
                     /region_name="APOC4"
                     /note="Apolipoprotein C4; pfam15119"
                     /db_xref="CDD:434474"
     Site            63
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P55056.1)"
     CDS             1..127
                     /gene="APOC4"
                     /gene_synonym="APO-CIV; APOC-IV"
                     /coded_by="NM_001646.3:42..425"
                     /db_xref="CCDS:CCDS12649.1"
                     /db_xref="GeneID:346"
                     /db_xref="HGNC:HGNC:611"
                     /db_xref="MIM:600745"
ORIGIN      
        1 msllrnrlqa lpalclcvlv lacigacqpe aqegtlsppp klkmsrwslv rgrmkellet
       61 vvnrtrdgwq wfwspstfrg fmqtyyddhl rdlgpltkaw fleskdsllk kthslcprlv
      121 cgdkdqg
//
LOCUS       NP_080448                335 aa            linear   ROD 27-APR-2025
DEFINITION  2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial
            precursor [Mus musculus].
ACCESSION   NP_080448
VERSION     NP_080448.1
DBSOURCE    REFSEQ: accession NM_026172.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Makela,A.M., Hohtola,E., Miinalainen,I.J., Autio,J.A., Schmitz,W.,
            Niemi,K.J., Hiltunen,J.K. and Autio,K.J.
  TITLE     Mitochondrial 2,4-dienoyl-CoA reductase (Decr) deficiency and
            impairment of thermogenesis in mouse brown adipose tissue
  JOURNAL   Sci Rep 9 (1), 12038 (2019)
   PUBMED   31427678
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Li,J., Deng,S.P., Wei,G. and Yu,P.
  TITLE     CITGeneDB: a comprehensive database of human and mouse genes
            enhancing or suppressing cold-induced thermogenesis validated by
            perturbation experiments in mice
  JOURNAL   Database (Oxford) 2018 (2018)
   PUBMED   29688375
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Zhou,L., Dai,H., Wu,J., Zhou,M., Yuan,H., Du,J., Yang,L., Wu,X.,
            Xu,H., Hua,Y., Xu,J., Zheng,L. and Shen,B.
  TITLE     Role of FEN1 S187 phosphorylation in counteracting oxygen-induced
            stress and regulating postnatal heart development
  JOURNAL   FASEB J 31 (1), 132-147 (2017)
   PUBMED   27694478
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Miinalainen,I.J., Schmitz,W., Huotari,A., Autio,K.J., Soininen,R.,
            Ver Loren van Themaat,E., Baes,M., Herzig,K.H., Conzelmann,E. and
            Hiltunen,J.K.
  TITLE     Mitochondrial 2,4-dienoyl-CoA reductase deficiency in mice results
            in severe hypoglycemia with stress intolerance and unimpaired
            ketogenesis
  JOURNAL   PLoS Genet 5 (7), e1000543 (2009)
   PUBMED   19578400
  REMARK    GeneRIF: Fasted Decr(-/-) mice displayed increased serum
            acylcarnitines and unimpaired ketogenesis.
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Brown,A.C., Olver,W.I., Donnelly,C.J., May,M.E., Naggert,J.K.,
            Shaffer,D.J. and Roopenian,D.C.
  TITLE     Searching QTL by gene expression: analysis of diabesity
  JOURNAL   BMC Genet 6, 12 (2005)
   PUBMED   15760467
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC046972.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC046972.1, AK146003.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN01164133
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 6.66 cM"
     Protein         1..335
                     /product="2,4-dienoyl-CoA reductase
                     [(3E)-enoyl-CoA-producing], mitochondrial precursor"
                     /EC_number="1.3.1.124"
                     /note="2,4-dienoyl-CoA reductase, mitochondrial;
                     2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing],
                     mitochondrial"
                     /calculated_mol_wt=32452
     transit_peptide 1..34
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9CQ62.1)"
                     /calculated_mol_wt=3780
     mat_peptide     35..335
                     /product="2,4-dienoyl-CoA reductase
                     [(3E)-enoyl-CoA-producing], mitochondrial.
                     /id=PRO_0000031966"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQ62.1)"
                     /calculated_mol_wt=32452
     Site            42
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CQ62.1)"
     Site            49
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CQ62.1)"
     Region          57..303
                     /region_name="TER_DECR_SDR_a"
                     /note="Trans-2-enoyl-CoA reductase (TER) and
                     2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR;
                     cd05369"
                     /db_xref="CDD:187627"
     Site            order(66,69..71,90..92,116..119,144..146,167,195..197,214,
                     240..243,245)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q16698; propagated from
                     UniProtKB/Swiss-Prot (Q9CQ62.1)"
     Site            order(91,119,146..149,157,159..160,163,197,199,210,242)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CQ62.1)"
     Site            106
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753,
                     ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q9CQ62.1)"
     Site            order(121,152..154,156..158,161..162,165,169..170,
                     173..174,177,181,184,189,199,203..206,208,211..212,
                     215..216,219..220,222..229,231,242,266..268,270..272,276,
                     279..280,283,288,290..295,297..303)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
     Site            order(148,199,210,214)
                     /site_type="active"
                     /db_xref="CDD:187627"
     Site            order(152..154,156,161..162,165,170,173..174,203..206,208,
                     211..212,215..216,219..220,223,226..227)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
     Site            244
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CQ62.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CQ62.1)"
     Site            315
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CQ62.1)"
     Site            319
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CQ62.1)"
     CDS             1..335
                     /gene="Decr1"
                     /gene_synonym="1200012F07Rik; Decr; Nadph"
                     /coded_by="NM_026172.4:27..1034"
                     /db_xref="CCDS:CCDS17985.1"
                     /db_xref="GeneID:67460"
                     /db_xref="MGI:MGI:1914710"
ORIGIN      
        1 mallgraffa gvsrlpcdpg pqrffsfgtk tlyqskdapq skffqpvlkp mlppdafqgk
       61 vafitgggtg lgkamttfls tlgaqcvias rnidvlkata eeissktgnk vhaircdvrd
      121 pdmvhntvle likvaghpdv vinnaagnfi spserltpng wktitdivln gtayvtleig
      181 kqlikaqkga aflaittiya esgsgfvmps ssaksgveam nkslaaewgr ygmrfniiqp
      241 gpiktkgafs rldptgrfek emidripcgr lgtmeelanl atflcsdyas wingavirfd
      301 ggeevflsge fnslkkvtke ewdiieglir ktkgs
//
LOCUS       NP_001346876             576 aa            linear   ROD 27-APR-2025
DEFINITION  TRAF-type zinc finger domain-containing protein 1 isoform 2 [Mus
            musculus].
ACCESSION   NP_001346876 XP_017176355
VERSION     NP_001346876.1
DBSOURCE    REFSEQ: accession NM_001359947.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Witwicka,H., Jia,H., Kutikov,A., Reyes-Gutierrez,P., Li,X. and
            Odgren,P.R.
  TITLE     TRAFD1 (FLN29) Interacts with Plekhm1 and Regulates Osteoclast
            Acidification and Resorption
  JOURNAL   PLoS One 10 (5), e0127537 (2015)
   PUBMED   25992615
  REMARK    GeneRIF: TRAFD1, in association with Plekhm1/Rab7-positive late
            endosomes-early lysosomes, has a previously unknown role in vesicle
            trafficking, acidification, and resorption in osteoclasts
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Sanada,T., Takaesu,G., Mashima,R., Yoshida,R., Kobayashi,T. and
            Yoshimura,A.
  TITLE     FLN29 deficiency reveals its negative regulatory role in the
            Toll-like receptor (TLR) and retinoic acid-inducible gene I
            (RIG-I)-like helicase signaling pathway
  JOURNAL   J Biol Chem 283 (49), 33858-33864 (2008)
   PUBMED   18849341
  REMARK    GeneRIF: FLN29, in addition to playing a negative regulatory role
            in the TLR4 signaling pathway, negatively regulates the RIG-I-like
            helicase signaling pathway at the level of IPS-1/TRAF6 and
            IPS-1/TRAF3 complexes
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Mashima,R., Saeki,K., Aki,D., Minoda,Y., Takaki,H., Sanada,T.,
            Kobayashi,T., Aburatani,H., Yamanashi,Y. and Yoshimura,A.
  TITLE     FLN29, a novel interferon- and LPS-inducible gene acting as a
            negative regulator of toll-like receptor signaling
  JOURNAL   J Biol Chem 280 (50), 41289-41297 (2005)
   PUBMED   16221674
  REMARK    GeneRIF: FLN29 is a new negative feedback regulator of TLR
            signaling
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC126938.2.
            
            On Jan 20, 2018 this sequence version replaced XP_017176355.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            an alternate in-frame splice site in the 3' coding region, compared
            to variant 1, that results in a protein (isoform 2) with a shorter
            C-terminus, compared to isoform 1. Variants 2 and 3 both encode the
            same isoform (2).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR13422598.496691.1,
                                           SRR13422597.287559.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 61.78 cM"
     Protein         1..576
                     /product="TRAF-type zinc finger domain-containing protein
                     1 isoform 2"
                     /note="FLN29 gene product; TRAF-type zinc finger
                     domain-containing protein 1"
                     /calculated_mol_wt=63734
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Region          <7..131
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Region          395..453
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MM4; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Region          468..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MM4; propagated from
                     UniProtKB/Swiss-Prot (Q3UDK1.1)"
     CDS             1..576
                     /gene="Trafd1"
                     /gene_synonym="1110008K06Rik; Fln29"
                     /coded_by="NM_001359947.1:120..1850"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS51639.1"
                     /db_xref="GeneID:231712"
                     /db_xref="MGI:MGI:1923551"
ORIGIN      
        1 maefrddqas rlcdnckkei pvfnftihei hcqrnigvcp vckepfpksd mdihmaaehc
       61 qvtckcnkkl ekrqlkqhae tecplrlavc qhcdlelsvv klkehedycg artelcgscg
      121 rnvlvkelkt hpevcgrvee ekrteaaipp eaydepwsqd riwiasqllr qiealdppmr
      181 lpgrplqafe adpfysrtts qrsmaaqfpv qnnlfeeqer qernrsrqsp kdsaennahl
      241 dfmlalslqn egqatsmveq gfwesvpead paragptslg dikgaadeil lpcefceely
      301 peellidhqt scnpshalrs lntgsssirg vedpgtifqn flqqatsnqf dtlmglsssa
      361 avedsiiipc efcgvqleee vlfyhqdqcd qrpatanhra vegipaqdsq pentsaelsr
      421 rrvkhqgdls sgymddvkpe svkgptysms pnrtmnnvas cnrllnlpsg prsdcqrspp
      481 gvlklnnsds qdirgqmrgs qngpiasgha pvihsiqnly penfapsfph gspgsgrseg
      541 grssrvspaa agyhsraaka kppkqqgagd aeeeee
//
LOCUS       NP_001356788             167 aa            linear   PRI 27-APR-2025
DEFINITION  protein tyrosine phosphatase type IVA 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001356788
VERSION     NP_001356788.1
DBSOURCE    REFSEQ: accession NM_001369859.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Hardy,S., Zolotarov,Y., Coleman,J., Roitman,S., Khursheed,H.,
            Aubry,I., Uetani,N. and Tremblay,M.L.
  TITLE     PRL-1/2 phosphatases control TRPM7 magnesium-dependent function to
            regulate cellular bioenergetics
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2221083120 (2023)
   PUBMED   36972446
  REMARK    GeneRIF: This study established the existence of a magnesium
            transporter protein complex (PTP4A2/CNNM3/TRPM7) governing the
            cellular uptake of this divalent cation. Moreover, PTP4A2 acts as a
            magnesium biosensor, controlling the activity of this complex to
            reprogram cellular metabolism.
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Li,Q., Bai,Y., Lyle,L.T., Yu,G., Amarasinghe,O., Nguele Meke,F.,
            Carlock,C. and Zhang,Z.Y.
  TITLE     Mechanism of PRL2 phosphatase-mediated PTEN degradation and
            tumorigenesis
  JOURNAL   Proc Natl Acad Sci U S A 117 (34), 20538-20548 (2020)
   PUBMED   32788364
  REMARK    GeneRIF: Mechanism of PRL2 phosphatase-mediated PTEN degradation
            and tumorigenesis.
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Cai,F., Huang,Y., Wang,M., Sun,M., Zhao,Y. and Hattori,M.
  TITLE     A FRET-based screening method to detect potential inhibitors of the
            binding of CNNM3 to PRL2
  JOURNAL   Sci Rep 10 (1), 12879 (2020)
   PUBMED   32733084
  REMARK    GeneRIF: A FRET-based screening method to detect potential
            inhibitors of the binding of CNNM3 to PRL2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 167)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 167)
  AUTHORS   Si,X., Zeng,Q., Ng,C.H., Hong,W. and Pallen,C.J.
  TITLE     Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase,
            with the beta-subunit of geranylgeranyltransferase II
  JOURNAL   J Biol Chem 276 (35), 32875-32882 (2001)
   PUBMED   11447212
REFERENCE   7  (residues 1 to 167)
  AUTHORS   Gjorloff-Wingren,A., Saxena,M., Han,S., Wang,X., Alonso,A.,
            Renedo,M., Oh,P., Williams,S., Schnitzer,J. and Mustelin,T.
  TITLE     Subcellular localization of intracellular protein tyrosine
            phosphatases in T cells
  JOURNAL   Eur J Immunol 30 (8), 2412-2421 (2000)
   PUBMED   10940933
REFERENCE   8  (residues 1 to 167)
  AUTHORS   Zeng,Q., Hong,W. and Tan,Y.H.
  TITLE     Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine
            phosphatases homologous to PRL-1
  JOURNAL   Biochem Biophys Res Commun 244 (2), 421-427 (1998)
   PUBMED   9514946
REFERENCE   9  (residues 1 to 167)
  AUTHORS   Cates,C.A., Michael,R.L., Stayrook,K.R., Harvey,K.A., Burke,Y.D.,
            Randall,S.K., Crowell,P.L. and Crowell,D.N.
  TITLE     Prenylation of oncogenic human PTP(CAAX) protein tyrosine
            phosphatases
  JOURNAL   Cancer Lett 110 (1-2), 49-55 (1996)
   PUBMED   9018080
REFERENCE   10 (residues 1 to 167)
  AUTHORS   Zhao,Z., Lee,C.C., Monckton,D.G., Yazdani,A., Coolbaugh,M.I.,
            Li,X., Bailey,J., Shen,Y. and Caskey,C.T.
  TITLE     Characterization and genomic mapping of genes and pseudogenes of a
            new human protein tyrosine phosphatase
  JOURNAL   Genomics 35 (1), 172-181 (1996)
   PUBMED   8661118
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136115.21, DB503104.1,
            BI549454.1 and BC070181.1.
            
            Summary: The protein encoded by this gene belongs to a small class
            of the protein tyrosine phosphatase (PTP) family. PTPs are cell
            signaling molecules that play regulatory roles in a variety of
            cellular processes. PTPs in this class contain a protein tyrosine
            phosphatase catalytic domain and a characteristic C-terminal
            prenylation motif. This PTP has been shown to primarily associate
            with plasmic and endosomal membrane through its C-terminal
            prenylation. This PTP was found to interact with the beta-subunit
            of Rab geranylgeranyltransferase II (beta GGT II), and thus may
            function as a regulator of GGT II activity. Overexpression of this
            gene in mammalian cells conferred a transformed phenotype, which
            suggested its role in tumorigenesis. Alternatively spliced
            transcript variants have been described. Related pseudogenes exist
            on chromosomes 11, 12 and 17. [provided by RefSeq, Aug 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.371452.1,
                                           SRR5189652.102244.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..167
                     /product="protein tyrosine phosphatase type IVA 2 isoform
                     1"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase IVA; phosphatase of
                     regenerating liver 2; protein tyrosine phosphatase IVA2;
                     protein tyrosine phosphatase type IVA 2; PTP(CAAXII);
                     protein-tyrosine phosphatase of regenerating liver 2;
                     protein tyrosine phosphatase type IVA, member 2"
                     /calculated_mol_wt=18996
     Region          1..155
                     /region_name="PTP-IVa2"
                     /note="protein tyrosine phosphatase type IVA 2; cd18536"
                     /db_xref="CDD:350512"
     Site            order(1..4,69..70,103,105..107,134..139,142)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:350512"
     Site            164
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q12974.1)"
     CDS             1..167
                     /gene="PTP4A2"
                     /gene_synonym="HH13; HH7-2; HU-PP-1; OV-1; PRL-2; PRL2;
                     ptp-IV1a; ptp-IV1b; PTP4A; PTPCAAX2"
                     /coded_by="NM_001369859.1:868..1371"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS348.1"
                     /db_xref="GeneID:8073"
                     /db_xref="HGNC:HGNC:9635"
                     /db_xref="MIM:601584"
ORIGIN      
        1 mnrpapveis yenmrflith nptnatlnkf teelkkygvt tlvrvcdaty dkapvekegi
       61 hvldwpfddg apppnqivdd wlnllktkfr eepgccvavh cvaglgrapv lvalaliecg
      121 mkyedavqfi rqkrrgafns kqllylekyr pkmrlrfrdt nghccvq
//
LOCUS       NP_003250                924 aa            linear   PRI 27-APR-2025
DEFINITION  intercellular adhesion molecule 5 precursor [Homo sapiens].
ACCESSION   NP_003250
VERSION     NP_003250.3
DBSOURCE    REFSEQ: accession NM_003259.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Wei,W., Guo,H., Chang,J., Yu,Y., Liu,G., Zhang,N., Willard,S.H.,
            Zheng,S. and Yu,X.F.
  TITLE     ICAM-5/Telencephalin Is a Functional Entry Receptor for Enterovirus
            D68
  JOURNAL   Cell Host Microbe 20 (5), 631-641 (2016)
   PUBMED   27923705
  REMARK    GeneRIF: Here the authors identify neuron-specific intercellular
            adhesion molecule 5 (ICAM-5/telencephalin) as a cellular receptor
            for sialic acid-dependent and -independent entry of enterovirus
            D68.
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Liu,L., Sun,M., Song,D. and Wang,Z.
  TITLE     The genetic polymorphisms of intercellular cell adhesion molecules
            and breast cancer susceptibility: a meta-analysis
  JOURNAL   Mol Biol Rep 40 (2), 1855-1860 (2013)
   PUBMED   23079714
  REMARK    GeneRIF: ICAM5 V301I and rs281439 variants may contribute to the
            susceptibility of breast cancer. [Meta-analysis]
REFERENCE   4  (residues 1 to 924)
  AUTHORS   Raemaekers,T., Peric,A., Baatsen,P., Sannerud,R., Declerck,I.,
            Baert,V., Michiels,C. and Annaert,W.
  TITLE     ARF6-mediated endosomal transport of Telencephalin affects
            dendritic filopodia-to-spine maturation
  JOURNAL   EMBO J 31 (15), 3252-3269 (2012)
   PUBMED   22781129
  REMARK    GeneRIF: A specific microenvironment facilitating ARF6-mediated
            mobilization of TLN that contributes to promotion of dendritic
            spine development.
REFERENCE   5  (residues 1 to 924)
  AUTHORS   Ho-Pun-Cheung,A., Assenat,E., Bascoul-Mollevi,C., Bibeau,F.,
            Boissiere-Michot,F., Thezenas,S., Cellier,D., Azria,D., Rouanet,P.,
            Senesse,P., Ychou,M. and Lopez-Crapez,E.
  TITLE     A large-scale candidate gene approach identifies SNPs in SOD2 and
            IL13 as predictive markers of response to preoperative
            chemoradiation in rectal cancer
  JOURNAL   Pharmacogenomics J 11 (6), 437-443 (2011)
   PUBMED   20644561
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 924)
  AUTHORS   Rieckmann,P., Turner,T., Kligannon,P. and Steinhoff,B.J.
  TITLE     Telencephalin as an indicator for temporal-lobe dysfunction
  JOURNAL   Lancet 352 (9125), 370-371 (1998)
   PUBMED   9717930
REFERENCE   7  (residues 1 to 924)
  AUTHORS   Benson,D.L., Yoshihara,Y. and Mori,K.
  TITLE     Polarized distribution and cell type-specific localization of
            telencephalin, an intercellular adhesion molecule
  JOURNAL   J Neurosci Res 52 (1), 43-53 (1998)
   PUBMED   9556028
REFERENCE   8  (residues 1 to 924)
  AUTHORS   Hayflick,J.S., Kilgannon,P. and Gallatin,W.M.
  TITLE     The intercellular adhesion molecule (ICAM) family of proteins. New
            members and novel functions
  JOURNAL   Immunol Res 17 (3), 313-327 (1998)
   PUBMED   9638475
  REMARK    Review article
REFERENCE   9  (residues 1 to 924)
  AUTHORS   Mizuno,T., Yoshihara,Y., Inazawa,J., Kagamiyama,H. and Mori,K.
  TITLE     cDNA cloning and chromosomal localization of the human
            telencephalin and its distinctive interaction with lymphocyte
            function-associated antigen-1
  JOURNAL   J Biol Chem 272 (2), 1156-1163 (1997)
   PUBMED   8995416
REFERENCE   10 (residues 1 to 924)
  AUTHORS   Yoshihara,Y. and Mori,K.
  TITLE     Telencephalin: a neuronal area code molecule?
  JOURNAL   Neurosci Res 21 (2), 119-124 (1994)
   PUBMED   7724062
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011511.12, U72671.1,
            AI199660.1, BC030132.2 and AI568610.1.
            
            On Jun 10, 2008 this sequence version replaced NP_003250.2.
            
            Summary: The protein encoded by this gene is a member of the
            intercellular adhesion molecule (ICAM) family. All ICAM proteins
            are type I transmembrane glycoproteins, contain 2-9
            immunoglobulin-like C2-type domains, and bind to the leukocyte
            adhesion LFA-1 protein. This protein is expressed on the surface of
            telencephalic neurons and displays two types of adhesion activity,
            homophilic binding between neurons and heterophilic binding between
            neurons and leukocytes. It may be a critical component in
            neuron-microglial cell interactions in the course of normal
            development or as part of neurodegenerative diseases. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026338.1, U72671.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMN02400288
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221980.5/ ENSP00000221980.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..924
                     /product="intercellular adhesion molecule 5 precursor"
                     /note="telencephalin; ICAM-5; intercellular adhesion
                     molecule 5, telencephalin"
                     /calculated_mol_wt=94156
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2979
     Region          31..103
                     /region_name="ICAM_N"
                     /note="Intercellular adhesion molecule (ICAM), N-terminal
                     domain; pfam03921"
                     /db_xref="CDD:397829"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (high mannose) asparagine.
                     /evidence=ECO:0000305|PubMed:18691975; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18691975; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          119..219
                     /region_name="IgC2_2_ICAM-1_like"
                     /note="Second immunoglobulin (Ig)-like C2-set domain of
                     intercellular cell adhesion molecule 1 (ICAM-1), and
                     similar domains; cd05755"
                     /db_xref="CDD:409413"
     Region          119..126
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409413"
     Region          137..146
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409413"
     Site            137
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18691975; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          153..159
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409413"
     Region          161..164
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409413"
     Region          179..186
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409413"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          194..201
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409413"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18691975; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          210..217
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409413"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18691975; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Site            303
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Site            316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          324..404
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Site            371
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Site            397
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          416..487
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          427..431
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          440..444
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          467..472
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          480..483
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          499..569
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          510..514
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          523..527
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          549..554
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          562..565
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          581..654
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            583
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          592..596
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          605..614
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          630..634
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          642..647
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            646
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          <694..733
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          699..703
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          722..727
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          759..831
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Site            764
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          765..769
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          778..782
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            795
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Site            796
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          797..801
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          811..816
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          822..825
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            836..856
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMF0.3)"
     Region          891..911
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMF0.3)"
     CDS             1..924
                     /gene="ICAM5"
                     /gene_synonym="TLCN; TLN"
                     /coded_by="NM_003259.4:93..2867"
                     /db_xref="CCDS:CCDS12233.1"
                     /db_xref="GeneID:7087"
                     /db_xref="HGNC:HGNC:5348"
                     /db_xref="MIM:601852"
ORIGIN      
        1 mpgpspglrr allglwaalg lglfglsavs qepfwadlqp rvafverggs lwlncstncp
       61 rpergglets lrrngtqrgl rwlarqlvdi repetqpvcf frcarrtlqa rglirtfqrp
      121 drvelmplpp wqpvgenftl scrvpgagpr asltltllrg aqelirrsfa gepprargav
      181 ltatvlarre dhganfscra eldlrphglg lfenssapre lrtfslspda prlaaprlle
      241 vgserpvsct ldglfpasea rvylalgdqn lspdvtlegd afvatatata saeqegarql
      301 vcnvtlggen retrenvtiy sfpaplltls epsvsegqmv tvtcaagaqa lvtlegvpaa
      361 vpgqpaqlql natenddrrs ffcdatldvd getliknrsa elrvlyaprl ddsdcprswt
      421 wpegpeqtlr ceargnpeps vhcarsdgga vlalgllgpv tralsgtyrc kaandqgeav
      481 kdvtltveya paldsvgcpe ritwlegtea slscvahgvp ppdvicvrsg elgaviegll
      541 rvarehagty rceatnprgs aaknvavtve ygprfeepsc psnwtwvegs grlfscevdg
      601 kpqpsvkcvg sggategvll plappdpspr apriprvlap giyvcnatnr hgsvaktvvv
      661 saesppemde stcpshqtwl egaeasalac aargrpspgv rcsregipwp eqqrvsreda
      721 gtyhcvatna hgtdsrtvtv gveyrpvvae laasppggvr pggnftltcr aeawppaqis
      781 wrappgalni glssnnstls vagamgshgg eyecaatnah grharritvr vagpwlwvav
      841 ggaaggaall aagaglafyv qstackkgey nvqeaessge avclngaggg aggaagaegg
      901 peaaggaaes paegevfaiq ltsa
//
LOCUS       NP_038804                121 aa            linear   ROD 27-APR-2025
DEFINITION  protein TCL1B5 [Mus musculus].
ACCESSION   NP_038804
VERSION     NP_038804.1
DBSOURCE    REFSEQ: accession NM_013776.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Hallas,C., Pekarsky,Y., Itoyama,T., Varnum,J., Bichi,R.,
            Rothstein,J.L. and Croce,C.M.
  TITLE     Genomic analysis of human and mouse TCL1 loci reveals a complex of
            tightly clustered genes
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14418-14423 (1999)
   PUBMED   10588720
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK139627.1 and AF195493.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF195493.1, AK139627.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 55.23 cM"
     Protein         1..121
                     /product="protein TCL1B5"
                     /calculated_mol_wt=13537
     Region          1..117
                     /region_name="TCL1_MTCP1"
                     /note="TCL1/MTCP1 family; pfam01840"
                     /db_xref="CDD:460358"
     CDS             1..121
                     /gene="Tcl1b5"
                     /gene_synonym="D12Ertd644e"
                     /coded_by="NM_013776.2:72..437"
                     /db_xref="CCDS:CCDS36546.1"
                     /db_xref="GeneID:27382"
                     /db_xref="MGI:MGI:1351635"
ORIGIN      
        1 maavsvdpqr plpvllvsvs lgiyedehhr vwiavnvets hsshgnriet cvtvhlqhmt
       61 tlpqeptpqq pinnnslptm wrlesrntyt gtdgtywrll dhsqmgdtvq ltldiiiged
      121 d
//
LOCUS       NP_689558                626 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 13B [Homo sapiens].
ACCESSION   NP_689558
VERSION     NP_689558.4
DBSOURCE    REFSEQ: accession NM_152345.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Mattioni,A., Boldt,K., Auciello,G., Komada,M., Rappoport,J.Z.,
            Ueffing,M., Castagnoli,L., Cesareni,G. and Santonico,E.
  TITLE     Ring Finger Protein 11 acts on ligand-activated EGFR via the direct
            interaction with the UIM region of ANKRD13 protein family
  JOURNAL   FEBS J 287 (16), 3526-3550 (2020)
   PUBMED   31985874
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Tanno,H., Yamaguchi,T., Goto,E., Ishido,S. and Komada,M.
  TITLE     The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor
            endocytosis from the plasma membrane
  JOURNAL   Mol Biol Cell 23 (7), 1343-1353 (2012)
   PUBMED   22298428
  REMARK    GeneRIF: overexpression of wild-type as well as truncated-mutant
            Ankrd 13A, 13B and 13D proteins strongly inhibited rapid
            endocytosis of ubiquitinated EGFR from the surface in EGF-treated
            cells
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Lango Allen,H., Estrada,K., Lettre,G., Berndt,S.I., Weedon,M.N.,
            Rivadeneira,F., Willer,C.J., Jackson,A.U., Vedantam,S.,
            Raychaudhuri,S., Ferreira,T., Wood,A.R., Weyant,R.J., Segre,A.V.,
            Speliotes,E.K., Wheeler,E., Soranzo,N., Park,J.H., Yang,J.,
            Gudbjartsson,D., Heard-Costa,N.L., Randall,J.C., Qi,L., Vernon
            Smith,A., Magi,R., Pastinen,T., Liang,L., Heid,I.M., Luan,J.,
            Thorleifsson,G., Winkler,T.W., Goddard,M.E., Sin Lo,K., Palmer,C.,
            Workalemahu,T., Aulchenko,Y.S., Johansson,A., Zillikens,M.C.,
            Feitosa,M.F., Esko,T., Johnson,T., Ketkar,S., Kraft,P., Mangino,M.,
            Prokopenko,I., Absher,D., Albrecht,E., Ernst,F., Glazer,N.L.,
            Hayward,C., Hottenga,J.J., Jacobs,K.B., Knowles,J.W., Kutalik,Z.,
            Monda,K.L., Polasek,O., Preuss,M., Rayner,N.W., Robertson,N.R.,
            Steinthorsdottir,V., Tyrer,J.P., Voight,B.F., Wiklund,F., Xu,J.,
            Zhao,J.H., Nyholt,D.R., Pellikka,N., Perola,M., Perry,J.R.,
            Surakka,I., Tammesoo,M.L., Altmaier,E.L., Amin,N., Aspelund,T.,
            Bhangale,T., Boucher,G., Chasman,D.I., Chen,C., Coin,L.,
            Cooper,M.N., Dixon,A.L., Gibson,Q., Grundberg,E., Hao,K., Juhani
            Junttila,M., Kaplan,L.M., Kettunen,J., Konig,I.R., Kwan,T.,
            Lawrence,R.W., Levinson,D.F., Lorentzon,M., McKnight,B.,
            Morris,A.P., Muller,M., Suh Ngwa,J., Purcell,S., Rafelt,S.,
            Salem,R.M., Salvi,E., Sanna,S., Shi,J., Sovio,U., Thompson,J.R.,
            Turchin,M.C., Vandenput,L., Verlaan,D.J., Vitart,V., White,C.C.,
            Ziegler,A., Almgren,P., Balmforth,A.J., Campbell,H., Citterio,L.,
            De Grandi,A., Dominiczak,A., Duan,J., Elliott,P., Elosua,R.,
            Eriksson,J.G., Freimer,N.B., Geus,E.J., Glorioso,N., Haiqing,S.,
            Hartikainen,A.L., Havulinna,A.S., Hicks,A.A., Hui,J., Igl,W.,
            Illig,T., Jula,A., Kajantie,E., Kilpelainen,T.O., Koiranen,M.,
            Kolcic,I., Koskinen,S., Kovacs,P., Laitinen,J., Liu,J., Lokki,M.L.,
            Marusic,A., Maschio,A., Meitinger,T., Mulas,A., Pare,G.,
            Parker,A.N., Peden,J.F., Petersmann,A., Pichler,I.,
            Pietilainen,K.H., Pouta,A., Ridderstrale,M., Rotter,J.I.,
            Sambrook,J.G., Sanders,A.R., Schmidt,C.O., Sinisalo,J., Smit,J.H.,
            Stringham,H.M., Bragi Walters,G., Widen,E., Wild,S.H.,
            Willemsen,G., Zagato,L., Zgaga,L., Zitting,P., Alavere,H.,
            Farrall,M., McArdle,W.L., Nelis,M., Peters,M.J., Ripatti,S., van
            Meurs,J.B., Aben,K.K., Ardlie,K.G., Beckmann,J.S., Beilby,J.P.,
            Bergman,R.N., Bergmann,S., Collins,F.S., Cusi,D., den Heijer,M.,
            Eiriksdottir,G., Gejman,P.V., Hall,A.S., Hamsten,A., Huikuri,H.V.,
            Iribarren,C., Kahonen,M., Kaprio,J., Kathiresan,S., Kiemeney,L.,
            Kocher,T., Launer,L.J., Lehtimaki,T., Melander,O., Mosley,T.H. Jr.,
            Musk,A.W., Nieminen,M.S., O'Donnell,C.J., Ohlsson,C., Oostra,B.,
            Palmer,L.J., Raitakari,O., Ridker,P.M., Rioux,J.D., Rissanen,A.,
            Rivolta,C., Schunkert,H., Shuldiner,A.R., Siscovick,D.S.,
            Stumvoll,M., Tonjes,A., Tuomilehto,J., van Ommen,G.J., Viikari,J.,
            Heath,A.C., Martin,N.G., Montgomery,G.W., Province,M.A., Kayser,M.,
            Arnold,A.M., Atwood,L.D., Boerwinkle,E., Chanock,S.J., Deloukas,P.,
            Gieger,C., Gronberg,H., Hall,P., Hattersley,A.T., Hengstenberg,C.,
            Hoffman,W., Lathrop,G.M., Salomaa,V., Schreiber,S., Uda,M.,
            Waterworth,D., Wright,A.F., Assimes,T.L., Barroso,I., Hofman,A.,
            Mohlke,K.L., Boomsma,D.I., Caulfield,M.J., Cupples,L.A.,
            Erdmann,J., Fox,C.S., Gudnason,V., Gyllensten,U., Harris,T.B.,
            Hayes,R.B., Jarvelin,M.R., Mooser,V., Munroe,P.B., Ouwehand,W.H.,
            Penninx,B.W., Pramstaller,P.P., Quertermous,T., Rudan,I.,
            Samani,N.J., Spector,T.D., Volzke,H., Watkins,H., Wilson,J.F.,
            Groop,L.C., Haritunians,T., Hu,F.B., Kaplan,R.C., Metspalu,A.,
            North,K.E., Schlessinger,D., Wareham,N.J., Hunter,D.J.,
            O'Connell,J.R., Strachan,D.P., Wichmann,H.E., Borecki,I.B., van
            Duijn,C.M., Schadt,E.E., Thorsteinsdottir,U., Peltonen,L.,
            Uitterlinden,A.G., Visscher,P.M., Chatterjee,N., Loos,R.J.,
            Boehnke,M., McCarthy,M.I., Ingelsson,E., Lindgren,C.M.,
            Abecasis,G.R., Stefansson,K., Frayling,T.M. and Hirschhorn,J.N.
  TITLE     Hundreds of variants clustered in genomic loci and biological
            pathways affect human height
  JOURNAL   Nature 467 (7317), 832-838 (2010)
   PUBMED   20881960
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11, AK092673.1, DA445860.1, BG029526.1 and AK000425.1.
            
            On Feb 7, 2007 this sequence version replaced NP_689558.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK092673.1, SRR9304719.301957.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000394859.8/
                                                ENSP00000378328.3
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..626
                     /product="ankyrin repeat domain-containing protein 13B"
                     /calculated_mol_wt=70075
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q86YJ7.4)"
     Region          <4..>103
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(13,15,19..20,23..25,27..28,32,35,45,47,49,53..54,
                     57..59,61..62,66,69,78,80,82,86..87,90..92,94..95,99,102)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          13..45
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          47..78
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          47..76
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ7.4)"
     Region          80..109
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ7.4)"
     Region          163..490
                     /region_name="GPCR_chapero_1"
                     /note="GPCR-chaperone; pfam11904"
                     /db_xref="CDD:463391"
     Region          442..474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ7.4)"
     Region          534..590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ7.4)"
     Region          595..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ7.4)"
     CDS             1..626
                     /gene="ANKRD13B"
                     /coded_by="NM_152345.5:491..2371"
                     /db_xref="CCDS:CCDS11251.1"
                     /db_xref="GeneID:124930"
                     /db_xref="HGNC:HGNC:26363"
                     /db_xref="MIM:615124"
ORIGIN      
        1 mipanasark gpegkyplhy lvwhnrhrel ekevragqvd ieqldprgrt plhlattlgh
       61 lecarvllah gadvgrenrs gwtvlqeavs trdlelvqlv lryrdyqrvv krlagipvll
      121 eklrkaqdfy vemkweftsw vplvskicps dtykvwksgq nlrvdttllg fdhmtwqrgn
      181 rsfvfrgqdt savvmeidhd rrvvytetla lagqdrelll aaaqpteeqv lsrltapvvt
      241 tqldtknisf ernktgilgw rsektemvng yeakvygasn velitrtrte hlseqhkgkv
      301 kgcktplqsf lgiaeqhggp qngtlitqtl sqanptaita eeyfnpnfel gnrdmgrpme
      361 lttktqkfka klwlceehpl slceqvapii dlmavsnalf aklrdfitlr lppgfpvkie
      421 ipifhilnar itfgnlngcd epvpsvrgsp ssetpspgsd sssvssssst tscrgceisp
      481 alfeaprgys mmggqreaat rdddddllqf aiqqslleag seydqvtiwe altnskpgth
      541 pmsyegrrqd rsapptpqrq pappasvpsp rpssgpgsgg hvfrsydeql rlamelsaqe
      601 qeerrrrarq eeeelerilr lslteq
//
LOCUS       NP_002408               3256 aa            linear   PRI 27-APR-2025
DEFINITION  proliferation marker protein Ki-67 isoform 1 [Homo sapiens].
ACCESSION   NP_002408
VERSION     NP_002408.3
DBSOURCE    REFSEQ: accession NM_002417.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3256)
  AUTHORS   Luo,H., Lian,Y., Tao,H., Zhao,Y., Wang,Z., Zhou,J., Zhang,Z. and
            Jiang,S.
  TITLE     Relationship between p16/ki67 immunoscores and PAX1/ZNF582
            methylation status in precancerous and cancerous cervical lesions
            in high-risk HPV-positive women
  JOURNAL   BMC Cancer 24 (1), 1171 (2024)
   PUBMED   39304838
  REMARK    GeneRIF: Relationship between p16/ki67 immunoscores and PAX1/ZNF582
            methylation status in precancerous and cancerous cervical lesions
            in high-risk HPV-positive women.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 3256)
  AUTHORS   Hernandez-Armendariz,A., Sorichetti,V., Hayashi,Y., Koskova,Z.,
            Brunner,A., Ellenberg,J., Saric,A. and Cuylen-Haering,S.
  TITLE     A liquid-like coat mediates chromosome clustering during mitotic
            exit
  JOURNAL   Mol Cell 84 (17), 3254-3270 (2024)
   PUBMED   39153474
REFERENCE   3  (residues 1 to 3256)
  AUTHORS   Ismael,A.T., Abdulhameed,R.A., Jalal,J.A., Tawfeeq,R.D., Ommar,A.
            and Jalal,A.
  TITLE     Expression of cytokeratin 7/20 and Ki67 in Helicobacter
            pylori-associated gastritis and intestinal metaplasia
  JOURNAL   J Infect Dev Ctries 18 (7), 1032-1040 (2024)
   PUBMED   39078783
  REMARK    GeneRIF: Expression of cytokeratin 7/20 and Ki67 in Helicobacter
            pylori-associated gastritis and intestinal metaplasia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3256)
  AUTHORS   Schmidt,M.H., Broll,R., Bruch,H.P., Finniss,S., Bogler,O. and
            Duchrow,M.
  TITLE     Proliferation marker pKi-67 occurs in different isoforms with
            various cellular effects
  JOURNAL   J Cell Biochem 91 (6), 1280-1292 (2004)
   PUBMED   15048881
REFERENCE   5  (residues 1 to 3256)
  AUTHORS   Duchrow,M., Schluter,C., Wohlenberg,C., Flad,H.D. and Gerdes,J.
  TITLE     Molecular characterization of the gene locus of the human cell
            proliferation-associated nuclear protein defined by monoclonal
            antibody Ki-67
  JOURNAL   Cell Prolif 29 (1), 1-12 (1996)
   PUBMED   8603106
REFERENCE   6  (residues 1 to 3256)
  AUTHORS   Schluter,C., Duchrow,M., Wohlenberg,C., Becker,M.H., Key,G.,
            Flad,H.D. and Gerdes,J.
  TITLE     The cell proliferation-associated antigen of antibody Ki-67: a very
            large, ubiquitous nuclear protein with numerous repeated elements,
            representing a new kind of cell cycle-maintaining proteins
  JOURNAL   J Cell Biol 123 (3), 513-522 (1993)
   PUBMED   8227122
REFERENCE   7  (residues 1 to 3256)
  AUTHORS   Landberg,G. and Roos,G.
  TITLE     Proliferating cell nuclear antigen and Ki-67 antigen expression in
            human haematopoietic cells during growth stimulation and
            differentiation
  JOURNAL   Cell Prolif 26 (5), 427-437 (1993)
   PUBMED   9087533
REFERENCE   8  (residues 1 to 3256)
  AUTHORS   Fonatsch,C., Duchrow,M., Rieder,H., Schluter,C. and Gerdes,J.
  TITLE     Assignment of the human Ki-67 gene (MK167) to 10q25-qter
  JOURNAL   Genomics 11 (2), 476-477 (1991)
   PUBMED   1769665
REFERENCE   9  (residues 1 to 3256)
  AUTHORS   Gerdes,J., Li,L., Schlueter,C., Duchrow,M., Wohlenberg,C.,
            Gerlach,C., Stahmer,I., Kloth,S., Brandt,E. and Flad,H.D.
  TITLE     Immunobiochemical and molecular biologic characterization of the
            cell proliferation-associated nuclear antigen that is defined by
            monoclonal antibody Ki-67
  JOURNAL   Am J Pathol 138 (4), 867-873 (1991)
   PUBMED   2012175
REFERENCE   10 (residues 1 to 3256)
  AUTHORS   Schonk,D.M., Kuijpers,H.J., van Drunen,E., van Dalen,C.H., Geurts
            van Kessel,A.H., Verheijen,R. and Ramaekers,F.C.
  TITLE     Assignment of the gene(s) involved in the expression of the
            proliferation-related Ki-67 antigen to human chromosome 10
  JOURNAL   Hum Genet 83 (3), 297-299 (1989)
   PUBMED   2571566
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355529.21, X65550.1,
            BU855841.1, AL390236.21 and BU632619.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 27, 2006 this sequence version replaced NP_002408.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X65550.1, SRR14038196.1751110.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368654.8/ ENSP00000357643.3
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.2"
     Protein         1..3256
                     /product="proliferation marker protein Ki-67 isoform 1"
                     /note="proliferation-related Ki-67 antigen; antigen
                     identified by monoclonal antibody Ki-67; protein
                     phosphatase 1, regulatory subunit 105; antigen Ki67;
                     proliferation marker protein Ki-67; Molecular Immunology
                     Borstel antibody 1"
                     /calculated_mol_wt=358564
     Region          6..98
                     /region_name="FHA_Ki67"
                     /note="forkhead associated (FHA) domain found in
                     proliferation marker protein Ki-67 and similar proteins;
                     cd22673"
                     /db_xref="CDD:438725"
     Site            order(9..13,18..21,23..24,31..46,66..67,91..93,95)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438725"
     Site            order(31,42..43,46,66..67,91)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438725"
     Region          101..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          271..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          495..678
                     /region_name="Positively charged patch (CP).
                     /evidence=ECO:0000269|PubMed:39153474"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          502..557
                     /region_name="PP1_bind"
                     /note="Protein phosphatase 1 binding; pfam15276"
                     /db_xref="CDD:434590"
     Region          513..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          575..632
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          674..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          853..886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1000..2928
                     /region_name="16 X 122 AA approximate repeats.
                     /evidence=ECO:0000305|PubMed:8227122"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          1001..1112
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            1017
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1045..1073
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1071
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1091
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1098
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1109..1151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1111
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1123..1234
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            1131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1167
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1176
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1193
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          1245..1356
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Region          1246..1276
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1323..1518
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1327
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1335
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1355
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1367..1477
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            1376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1383
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1420
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1437
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1488..1597
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            1496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1503
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1506
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1540
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1552
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1557
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1569
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          1597..1675
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          1609..1720
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            1617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1639
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1679
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1689..1708
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1689
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1717..1765
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1719
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1721
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1731..1842
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            1740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1747
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1764
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          1771..1790
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1784
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1801..1824
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1801
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1815
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1839..1886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1841
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1852..1964
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            1861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1869
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1897
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1906
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1923
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            1937
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          1961..2002
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            1963
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          1975..2086
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            1983
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2005
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          2017..2192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            2028
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2065
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            2072
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2085
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          2097..2204
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            2105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2113
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2146
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2203
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          2205..2400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          2215..2326
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            2223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            2231
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            2233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2268
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2285
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2325
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            2328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2333
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          2336..2447
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            2344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2352
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2389
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            2395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2406
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            2426
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          2445..2480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            2446
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          2458..2569
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            2466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          2497..2521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Site            2505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          2570..3256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46013.2)"
     Region          2580..2688
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            2588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          2700..2804
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            2708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Region          2819..2928
                     /region_name="KI67R"
                     /note="KI67R (NUC007) repeat; pfam08065"
                     /db_xref="CDD:462351"
     Site            2827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2838
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            2986
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:E9PVX6; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            3041
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     Site            3128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46013.2)"
     CDS             1..3256
                     /gene="MKI67"
                     /gene_synonym="KIA; MIB-; MIB-1; PPP1R105"
                     /coded_by="NM_002417.5:415..10185"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7659.1"
                     /db_xref="GeneID:4288"
                     /db_xref="HGNC:HGNC:7107"
                     /db_xref="MIM:176741"
ORIGIN      
        1 mwptrrlvti krsgvdgphf plslstclfg rgiecdiriq lpvvskqhck ieiheqeail
       61 hnfsstnptq vngsvidepv rlkhgdviti idrsfryene slqngrkste fprkireqep
      121 arrvsrssfs sdpdekaqds kayskitegk vsgnpqvhik nvkedstadd skdsvaqgtt
      181 nvhssehagr ngrnaadpis gdfkeissvk lvsrygelks vpttqcldns kknespfwkl
      241 yesvkkeldv ksqkenvlqy crksglqtdy atekesadgl qgetqllvsr ksrpksggsg
      301 havaepaspe qeldqnkgkg rdvesvqtps kavgasfply epakmktpvq ysqqqnspqk
      361 hknkdlyttg rresvnlgks egfkagdktl tprklstrnr tpakvedaad satkpenlss
      421 ktrgsiptdv evlpteteih nepfltlwlt qverkiqkds lskpeklgtt agqmcsglpg
      481 lssvdinnfg dsinesegip lkrrrvsfgg hlrpelfden lppntplkrg eaptkrkslv
      541 mhtppvlkki ikeqpqpsgk qesgseihve vkaqslvisp papsprktpv asdqrrrsck
      601 tapasssksq tevpkrggrk sgnlpskrvs isrsqhdilq micskrrsga seanlivaks
      661 wadvvklgak qtqtkvikhg pqrsmnkrqr rpatpkkpvg evhsqfstgh anspctiiig
      721 kahtekvhvp arpyrvlnnf isnqkmdfke dlsgiaemfk tpvkeqpqlt stchiaisns
      781 enllgkqfqg tdsgeepllp tsesfggnvf fsaqnaakqp sdkcsasppl rrqcirengn
      841 vaktprntyk mtsletktsd tetepsktvs tanrsgrste frniqklpve skseetntei
      901 vecilkrgqk atllqqrreg emkeierpfe tykenielke ndekmkamkr srtwgqkcap
      961 msdltdlksl pdtelmkdta rgqnllqtqd hakapksekg kitkmpcqsl qpepintpth
     1021 tkqqlkaslg kvgvkeella vgkftrtsge tththrepag dgksirtfke spkqildpaa
     1081 rvtgmkkwpr tpkeeaqsle dlagfkelfq tpgpseesmt dekttkiack spppesvdtp
     1141 tstkqwpkrs lrkadveeef lalrkltpsa gkamltpkpa ggdekdikaf mgtpvqkldl
     1201 agtlpgskrq lqtpkekaqa ledlagfkel fqtpghteel vaagkttkip cdspqsdpvd
     1261 tptstkqrpk rsirkadveg ellacrnlmp sagkamhtpk psvgeekdii ifvgtpvqkl
     1321 dltenltgsk rrpqtpkeea qaledltgfk elfqtpghte eavaagkttk mpcessppes
     1381 adtptstrrq pktplekrdv qkelsalkkl tqtsgettht dkvpggedks inafretakq
     1441 kldpaasvtg skrhpktkek aqpledlagl kelfqtpvct dkptthektt kiacrsqpdp
     1501 vdtptsskpq skrslrkvdv eeeffalrkr tpsagkamht pkpavsgekn iyafmgtpvq
     1561 kldltenltg skrrlqtpke kaqaledlag fkelfqtrgh teesmtndkt akvackssqp
     1621 dpdknpassk rrlktslgkv gvkeellavg kltqtsgett hthteptgdg ksmkafmesp
     1681 kqildsaasl tgskrqlrtp kgksevpedl agfielfqtp shtkesmtne kttkvsyras
     1741 qpdlvdtpts skpqpkrslr kadteeefla frkqtpsagk amhtpkpavg eekdintflg
     1801 tpvqkldqpg nlpgsnrrlq trkekaqale eltgfrelfq tpctdnpttd ekttkkilck
     1861 spqsdpadtp tntkqrpkrs lkkadveeef lafrkltpsa gkamhtpkaa vgeekdintf
     1921 vgtpvekldl lgnlpgskrr pqtpkekaka ledlagfkel fqtpghtees mtddkitevs
     1981 ckspqpdpvk tptsskqrlk islgkvgvke evlpvgkltq tsgkttqthr etagdgksik
     2041 afkesakqml dpanygtgme rwprtpkeea qsledlagfk elfqtpdhte esttddkttk
     2101 iackspppes mdtptstrrr pktplgkrdi veelsalkql tqtthtdkvp gdedkginvf
     2161 retakqkldp aasvtgskrq prtpkgkaqp ledlaglkel fqtpictdkp tthekttkia
     2221 crspqpdpvg tptifkpqsk rslrkadvee eslalrkrtp svgkamdtpk paggdekdmk
     2281 afmgtpvqkl dlpgnlpgsk rwpqtpkeka qaledlagfk elfqtpgtdk pttdekttki
     2341 ackspqpdpv dtpastkqrp krnlrkadve eeflalrkrt psagkamdtp kpavsdekni
     2401 ntfvetpvqk ldllgnlpgs krqpqtpkek aealedlvgf kelfqtpght eesmtddkit
     2461 evsckspqpe sfktsrsskq rlkiplvkvd mkeeplavsk ltrtsgettq thteptgdsk
     2521 sikafkespk qildpaasvt gsrrqlrtrk ekaraledlv dfkelfsapg hteesmtidk
     2581 ntkipckspp peltdtatst krcpktrprk evkeelsave rltqtsgqst hthkepasgd
     2641 egikvlkqra kkkpnpveee psrrrprapk ekaqpledla gftelsetsg htqesltagk
     2701 atkipcespp levvdttast krhlrtrvqk vqvkeepsav kftqtsgett dadkepaged
     2761 kgikalkesa kqtpapaasv tgsrrrprap resaqaiedl agfkdpaagh teesmtddkt
     2821 tkipcksspe ledtatsskr rprtraqkve vkeellavgk ltqtsgetth tdkepvgegk
     2881 gtkafkqpak rkldaedvig srrqprapke kaqpledlas fqelsqtpgh teelangaad
     2941 sftsapkqtp dsgkplkisr rvlrapkvep vgdvvstrdp vksqsksnts lpplpfkrgg
     3001 gkdgsvtgtk rlrcmpapee iveelpaskk qrvaprargk ssepvvimkr slrtsakrie
     3061 paeelnsndm ktnkeehklq dsvpenkgis lrsrrqnkte aeqqitevfv laerieinrn
     3121 ekkpmktspe mdiqnpddga rkpiprdkvt enkrclrsar qnessqpkva eesggqksak
     3181 vlmqnqkgkg eagnsdsmcl rsrktksqpa astlesksvq rvtrsvkrca enpkkaednv
     3241 cvkkirtrsh rdsedi
//
LOCUS       NP_001156008             390 aa            linear   PRI 27-APR-2025
DEFINITION  RNA binding motif protein, X-linked-like-1 [Homo sapiens].
ACCESSION   NP_001156008
VERSION     NP_001156008.1
DBSOURCE    REFSEQ: accession NM_001162536.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Prieto,C., Nguyen,D.T.T., Liu,Z., Wheat,J., Perez,A., Gourkanti,S.,
            Chou,T., Barin,E., Velleca,A., Rohwetter,T., Chow,A., Taggart,J.,
            Savino,A.M., Hoskova,K., Dhodapkar,M., Schurer,A., Barlowe,T.S.,
            Vu,L.P., Leslie,C., Steidl,U., Rabadan,R. and Kharas,M.G.
  TITLE     Transcriptional control of CBX5 by the RNA binding proteins RBMX
            and RBMXL1 maintains chromatin state in myeloid leukemia
  JOURNAL   Nat Cancer 2, 741-757 (2021)
   PUBMED   34458856
  REMARK    GeneRIF: Transcriptional control of CBX5 by the RNA binding
            proteins RBMX and RBMXL1 maintains chromatin state in myeloid
            leukemia.
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Martins-de-Souza,D., Gattaz,W.F., Schmitt,A., Rewerts,C.,
            Maccarrone,G., Dias-Neto,E. and Turck,C.W.
  TITLE     Prefrontal cortex shotgun proteome analysis reveals altered calcium
            homeostasis and immune system imbalance in schizophrenia
  JOURNAL   Eur Arch Psychiatry Clin Neurosci 259 (3), 151-163 (2009)
   PUBMED   19165527
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Marques,A.C., Dupanloup,I., Vinckenbosch,N., Reymond,A. and
            Kaessmann,H.
  TITLE     Emergence of young human genes after a burst of retroposition in
            primates
  JOURNAL   PLoS Biol 3 (11), e357 (2005)
   PUBMED   16201836
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Emerson,J.J., Kaessmann,H., Betran,E. and Long,M.
  TITLE     Extensive gene traffic on the mammalian X chromosome
  JOURNAL   Science 303 (5657), 537-540 (2004)
   PUBMED   14739461
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA216732.1, BC012942.1,
            BF901720.1 and AL832785.1.
            
            Summary: This gene represents a retrogene of RNA binding motif
            protein, X-linked (RBMX), which is located on chromosome X. While
            all introns in the coding sequence have been processed out compared
            to the RBMX locus, the ORF is intact and there is specific evidence
            for transcription at this location. The preservation of the ORF by
            purifying selection in all Old World monkeys carrying it suggests
            that this locus is likely to be functional, possibly during male
            meiosis when X chromosomal genes are silenced or during haploid
            stages of spermatogenesis. This gene shares 5' exon structure with
            the cysteine conjugate-beta lyase 2 locus on chromosome 1, but the
            coding sequences are non-overlapping. Alternative splicing results
            in two transcript variants. [provided by RefSeq, Jun 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            CCDS Note: This CCDS represents a retrogene of RBMX (RNA binding
            motif protein, X-linked), which is located on chromosome X. While
            all introns in the coding sequence have been processed out compared
            to the RBMX locus, the ORF is intact and there is specific evidence
            for transcription at this location. Studies in PMID:16201836
            indicate that this locus is likely to be functional because the ORF
            has been preserved by purifying selection in all six Old World
            primates carrying this retrogene. Given that X chromosomal genes in
            mammals can generate a statistically significant excess of
            autosomal retrogenes relative to genes on other chromosomes
            (PMID:14739461), it is possible that this retrogene may be
            functional during male meiosis when X chromosomal genes are
            silenced or during haploid stages of spermatogenesis
            (PMID:16201836). In addition, it should be noted that this
            retrogene shares its first non-coding exon with the cysteine
            conjugate-beta lyase 2 (CCBL2) locus on chromosome 1, but the
            coding sequences are non-overlapping.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.347574.1,
                                           SRR1803617.221530.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000652648.1/ ENSP00000498248.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.2"
     Protein         1..390
                     /product="RNA binding motif protein, X-linked-like-1"
                     /note="heterogeneous nuclear ribonucleoprotein G-like 1;
                     RNA binding motif protein, X-linked like 1"
                     /calculated_mol_wt=42011
     Region          7..86
                     /region_name="RRM_RBMX_like"
                     /note="RNA recognition motif (RRM) found in heterogeneous
                     nuclear ribonucleoprotein G (hnRNP G), Y chromosome RNA
                     recognition motif 1 (hRBMY), testis-specific heterogeneous
                     nuclear ribonucleoprotein G-T (hnRNP G-T) and similar
                     proteins; cd12382"
                     /db_xref="CDD:409816"
     Site            order(9,11,13..17,38,40..43,45..51,53,78,80,82..86)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409816"
     Region          62..390
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96E39.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q96E39.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96E39.1)"
     Region          165..>306
                     /region_name="dnaA"
                     /note="chromosomal replication initiator protein DnaA;
                     cl42516"
                     /db_xref="CDD:455861"
     Region          173..217
                     /region_name="RBM1CTR"
                     /note="RBM1CTR (NUC064) family; pfam08081"
                     /db_xref="CDD:400429"
     CDS             1..390
                     /gene="RBMXL1"
                     /gene_synonym="RBM1"
                     /coded_by="NM_001162536.3:386..1558"
                     /db_xref="CCDS:CCDS716.1"
                     /db_xref="GeneID:494115"
                     /db_xref="HGNC:HGNC:25073"
ORIGIN      
        1 mveadrpgkl figglntetn ekaletvfgk ygrivevlli kdretnksrg fafvtfespa
       61 dakdaardmn gksldgkaik veqatkpsfe rgrhgppppp rsrgpprgfg agrggsggtr
      121 gppsrgghmd dggysmnfnm sssrgplpvk rgppprsggp spkrsapsgl vrsssgmggr
      181 aplsrgrdsy ggpprreplp srrdvylspr ddgystkdsy ssrdypssrd trdyappprd
      241 ytyrdyghss srddypsrgy gdrdgygrdr dysdhpsggs yrdsyesygn srsapltrgp
      301 ppsyggssry ddysssrdgy ggsrdsysss rsdlysscdr vgrqerglpp svergypssr
      361 dsyssssrga prgagpggsr sdrgggrsry
//
LOCUS       NP_000862                440 aa            linear   PRI 27-APR-2025
DEFINITION  5-hydroxytryptamine receptor 6 [Homo sapiens].
ACCESSION   NP_000862
VERSION     NP_000862.1
DBSOURCE    REFSEQ: accession NM_000871.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Chechekhin,V.I., Ivanova,A.M., Kulebyakin,K.Y., Antropova,Y.G.,
            Karagyaur,M.N., Skryabina,M.N., Chechekhina,E.S., Basalova,N.A.,
            Grigorieva,O.A., Sysoeva,V.Y., Kalinina,N.I., Tkachuk,V.A. and
            Tyurin-Kuzmin,P.A.
  TITLE     Peripheral 5-HT/HTR6 axis is responsible for obesity-associated
            hypertension
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (2), 119651 (2024)
   PUBMED   38086448
  REMARK    GeneRIF: Peripheral 5-HT/HTR6 axis is responsible for
            obesity-associated hypertension.
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Pei,Y., Wen,X., Guo,S.C., Yang,Z.S., Zhang,R., Xiao,P. and Sun,J.P.
  TITLE     Structural insight into the selective agonist ST1936 binding of
            serotonin receptor 5-HT6
  JOURNAL   Biochem Biophys Res Commun 671, 327-334 (2023)
   PUBMED   37327704
REFERENCE   3  (residues 1 to 440)
  AUTHORS   He,L., Zhao,Q., Qi,J., Wang,Y., Han,W., Chen,Z., Cong,Y. and
            Wang,S.
  TITLE     Structural insights into constitutive activity of 5-HT6 receptor
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2209917120 (2023)
   PUBMED   36989299
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Huang,S., Xu,P., Shen,D.D., Simon,I.A., Mao,C., Tan,Y., Zhang,H.,
            Harpsoe,K., Li,H., Zhang,Y., You,C., Yu,X., Jiang,Y., Zhang,Y.,
            Gloriam,D.E. and Xu,H.E.
  TITLE     GPCRs steer Gi and Gs selectivity via TM5-TM6 switches as revealed
            by structures of serotonin receptors
  JOURNAL   Mol Cell 82 (14), 2681-2695 (2022)
   PUBMED   35714614
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Zhang,W., Li,L., Li,J., Yu,H., Zheng,F., Yan,B., Cai,W., Chen,Y.,
            Yin,L., Tang,D., Xu,Y. and Dai,Y.
  TITLE     Systematic Analysis of Neurotransmitter Receptors in Human Breast
            Cancer Reveals a Strong Association With Outcome and Uncovers HTR6
            as a Survival-Associated Gene Potentially Regulating the Immune
            Microenvironment
  JOURNAL   Front Immunol 13, 756928 (2022)
   PUBMED   35359970
  REMARK    GeneRIF: Systematic Analysis of Neurotransmitter Receptors in Human
            Breast Cancer Reveals a Strong Association With Outcome and
            Uncovers HTR6 as a Survival-Associated Gene Potentially Regulating
            the Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Lambe,E.K., Fillman,S.G., Webster,M.J. and Shannon Weickert,C.
  TITLE     Serotonin receptor expression in human prefrontal cortex: balancing
            excitation and inhibition across postnatal development
  JOURNAL   PLoS One 6 (7), e22799 (2011)
   PUBMED   21829518
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Masellis,M., Basile,V.S., Meltzer,H.Y., Lieberman,J.A., Sevy,S.,
            Goldman,D.A., Hamblin,M.W., Macciardi,F.M. and Kennedy,J.L.
  TITLE     Lack of association between the T-->C 267 serotonin 5-HT6 receptor
            gene (HTR6) polymorphism and prediction of response to clozapine in
            schizophrenia
  JOURNAL   Schizophr Res 47 (1), 49-58 (2001)
   PUBMED   11163544
  REMARK    GeneRIF: Observational study of gene-environment interaction and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Chiu,H.J., Wang,Y.C., Liou,J.H., Chao,C.H., Lee,H., Tsai,K.Y. and
            Liu,W.C.
  TITLE     Serotonin 6 receptor polymorphism in schizophrenia: frequency, age
            at onset and cognitive function
  JOURNAL   Neuropsychobiology 43 (3), 113-116 (2001)
   PUBMED   11287786
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Comings,D.E., Gade-Andavolu,R., Gonzalez,N., Wu,S., Muhleman,D.,
            Blake,H., Mann,M.B., Dietz,G., Saucier,G. and MacMurray,J.P.
  TITLE     A multivariate analysis of 59 candidate genes in personality
            traits: the temperament and character inventory
  JOURNAL   Clin Genet 58 (5), 375-385 (2000)
   PUBMED   11140838
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Kohen,R., Metcalf,M.A., Khan,N., Druck,T., Huebner,K.,
            Lachowicz,J.E., Meltzer,H.Y., Sibley,D.R., Roth,B.L. and
            Hamblin,M.W.
  TITLE     Cloning, characterization, and chromosomal localization of a human
            5-HT6 serotonin receptor
  JOURNAL   J Neurochem 66 (1), 47-56 (1996)
   PUBMED   8522988
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031727.43, L41147.1 and
            AF007141.1.
            
            Summary: This gene encodes a protein that belongs to the
            seven-transmembrane G protein-coupled receptor family of proteins.
            The encoded protein couples with the Gs alpha subunit and
            stimulates adenylate cyclase to activate the cyclic AMP-dependent
            signaling pathway. This receptor is thought to regulate cholinergic
            neuronal transmission in the brain. Several antidepressants and
            antipsychotic drugs have a high affinity for this receptor.
            [provided by RefSeq, Aug 2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L41147.1, BC074995.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000289753.2/ ENSP00000289753.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..440
                     /product="5-hydroxytryptamine receptor 6"
                     /note="serotonin receptor 6; 5-hydroxytryptamine
                     (serotonin) receptor 6, G protein-coupled"
                     /calculated_mol_wt=46823
     Region          27..331
                     /region_name="7tmA_5-HT6"
                     /note="serotonin receptor subtype 6, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15054"
                     /db_xref="CDD:320182"
     Region          28..54
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320182"
     Site            28..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50406.1)"
     Region          61..87
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320182"
     Site            63..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50406.1)"
     Site            97..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50406.1)"
     Region          99..129
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320182"
     Site            order(102,106..107,110..111,182,189,192..193,196,281,
                     284..285,288,302,306,310)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320182"
     Region          141..164
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320182"
     Site            143..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50406.1)"
     Region          185..214
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320182"
     Site            186..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50406.1)"
     Region          261..291
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320182"
     Site            267..293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50406.1)"
     Region          299..324
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320182"
     Site            300..323
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50406.1)"
     Region          346..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50406.1)"
     CDS             1..440
                     /gene="HTR6"
                     /gene_synonym="5-HT6; 5-HT6R"
                     /coded_by="NM_000871.3:880..2202"
                     /db_xref="CCDS:CCDS197.1"
                     /db_xref="GeneID:3362"
                     /db_xref="HGNC:HGNC:5301"
                     /db_xref="MIM:601109"
ORIGIN      
        1 mvpepgptan stpawgagpp sapggsgwva aalcvvialt aaansllial ictqpalrnt
       61 snfflvslft sdlmvglvvm ppamlnalyg rwvlarglcl lwtafdvmcc sasilnlcli
      121 sldryllils plryklrmtp lralalvlga wslaalasfl plllgwhelg harppvpgqc
      181 rllaslpfvl vasgltfflp sgaicftycr illaarkqav qvaslttgma sqasetlqvp
      241 rtprpgvesa dsrrlatkhs rkalkasltl gillgmffvt wlpffvaniv qavcdcispg
      301 lfdvltwlgy cnstmnpiiy plfmrdfkra lgrflpcprc prerqaslas pslrtshsgp
      361 rpglslqqvl plplppdsds dsdagsggss glrltaqlll pgeatqdppl ptraaaavnf
      421 fnidpaepel rphplgiptn
//
LOCUS       NP_542381                267 aa            linear   PRI 27-APR-2025
DEFINITION  diphthine--ammonia ligase isoform 1 [Homo sapiens].
ACCESSION   NP_542381 XP_370854
VERSION     NP_542381.1
DBSOURCE    REFSEQ: accession NM_080650.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Uthman,S., Bar,C., Scheidt,V., Liu,S., ten Have,S., Giorgini,F.,
            Stark,M.J. and Schaffrath,R.
  TITLE     The amidation step of diphthamide biosynthesis in yeast requires
            DPH6, a gene identified through mining the DPH1-DPH5 interaction
            network
  JOURNAL   PLoS Genet 9 (2), e1003334 (2013)
   PUBMED   23468660
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Su,X., Lin,Z., Chen,W., Jiang,H., Zhang,S. and Lin,H.
  TITLE     Chemogenomic approach identified yeast YLR143W as diphthamide
            synthetase
  JOURNAL   Proc Natl Acad Sci U S A 109 (49), 19983-19987 (2012)
   PUBMED   23169644
  REMARK    GeneRIF: The previously uncharacterized human gene ATPBD4 is the
            ortholog of yeast YLR143W, a diphthamide synthetase, and fully
            rescues the deletion of YLR143W in yeast.
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB250468.1, AK094007.1, BC008485.2 and AC019288.8.
            
            On Mar 22, 2004 this sequence version replaced XP_370854.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.52863.1,
                                           SRR3476690.832475.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256538.9/ ENSP00000256538.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..267
                     /product="diphthine--ammonia ligase isoform 1"
                     /EC_number="6.3.1.14"
                     /note="ATP-binding domain-containing protein 4;
                     diphthamide synthase; diphthamide synthetase;
                     diphthine--ammonia ligase; ATP binding domain 4; DPH6
                     homolog; protein DPH6 homolog"
                     /calculated_mol_wt=30176
     Region          2..219
                     /region_name="AANH_PF0828-like"
                     /note="putative ATP pyrophosphatase PF0828 and similar
                     proteins; cd01994"
                     /db_xref="CDD:467498"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ28; propagated from
                     UniProtKB/Swiss-Prot (Q7L8W6.3)"
     CDS             1..267
                     /gene="DPH6"
                     /gene_synonym="ATPBD4"
                     /coded_by="NM_080650.4:25..828"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10043.1"
                     /db_xref="GeneID:89978"
                     /db_xref="HGNC:HGNC:30543"
                     /db_xref="MIM:618391"
ORIGIN      
        1 mrvaalisgg kdscynmmqc iaaghqival anlrpaenqv gsdeldsymy qtvghhaidl
       61 yaeamalply rrtirgrsld trqvytkceg devedlyell klvkekeeve gisvgailsd
      121 yqrirvenvc krlnlqplay lwqrnqedll remissniqa miikvaalgl dpdkhlgktl
      181 dqmepyliel skkygvhvcg eggeyetftl dcplfkkkii vdssevvihs adafapvayl
      241 rflelhledk vssvpdnyrt snyiynf
//
LOCUS       NP_006701                209 aa            linear   PRI 27-APR-2025
DEFINITION  COP9 signalosome complex subunit 8 isoform 1 [Homo sapiens].
ACCESSION   NP_006701
VERSION     NP_006701.1
DBSOURCE    REFSEQ: accession NM_006710.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Liu,J., Han,D., Xuan,J., Xie,J., Wang,W., Zhou,Q. and Chen,K.
  TITLE     COP9 signalosome complex is a prognostic biomarker and corresponds
            with immune infiltration in hepatocellular carcinoma
  JOURNAL   Aging (Albany NY) 16 (6), 5264-5287 (2024)
   PUBMED   38466642
  REMARK    GeneRIF: COP9 signalosome complex is a prognostic biomarker and
            corresponds with immune infiltration in hepatocellular carcinoma.
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Sun,L.
  TITLE     COPS8 in cutaneous melanoma: an oncogene that accelerates the
            malignant development of tumor cells and predicts poor prognosis
  JOURNAL   Biosci Biotechnol Biochem 85 (2), 242-250 (2021)
   PUBMED   33604618
  REMARK    GeneRIF: COPS8 in cutaneous melanoma: an oncogene that accelerates
            the malignant development of tumor cells and predicts poor
            prognosis.
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Ju,S., Wang,F., Wang,Y. and Ju,S.
  TITLE     CSN8 is a key regulator in hypoxia-induced epithelial-mesenchymal
            transition and dormancy of colorectal cancer cells
  JOURNAL   Mol Cancer 19 (1), 168 (2020)
   PUBMED   33261601
  REMARK    GeneRIF: CSN8 is a key regulator in hypoxia-induced
            epithelial-mesenchymal transition and dormancy of colorectal cancer
            cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Cohen,H., Azriel,A., Cohen,T., Meraro,D., Hashmueli,S.,
            Bech-Otschir,D., Kraft,R., Dubiel,W. and Levi,B.Z.
  TITLE     Interaction between interferon consensus sequence-binding protein
            and COP9/signalosome subunit CSN2 (Trip15). A possible link between
            interferon regulatory factor signaling and the COP9/signalosome
  JOURNAL   J Biol Chem 275 (50), 39081-39089 (2000)
   PUBMED   10991940
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Naumann,M., Bech-Otschir,D., Huang,X., Ferrell,K. and Dubiel,W.
  TITLE     COP9 signalosome-directed c-Jun activation/stabilization is
            independent of JNK
  JOURNAL   J Biol Chem 274 (50), 35297-35300 (1999)
   PUBMED   10585392
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
REFERENCE   9  (residues 1 to 209)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
REFERENCE   10 (residues 1 to 209)
  AUTHORS   Chamovitz,D.A. and Deng,X.W.
  TITLE     The novel components of the Arabidopsis light signaling pathway may
            define a group of general developmental regulators shared by both
            animal and plant kingdoms
  JOURNAL   Cell 82 (3), 353-354 (1995)
   PUBMED   7634324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC036499.1, BC003090.1,
            AL038738.1 and AC105760.3.
            
            Summary: The protein encoded by this gene is one of the eight
            subunits of COP9 signalosome, a highly conserved protein complex
            that functions as an important regulator in multiple signaling
            pathways. The structure and function of COP9 signalosome is similar
            to that of the 19S regulatory particle of 26S proteasome. COP9
            signalosome has been shown to interact with SCF-type E3 ubiquitin
            ligases and act as a positive regulator of E3 ubiquitin ligases.
            Alternatively spliced transcript variants encoding distinct
            isoforms have been observed. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.64047.1,
                                           SRR1660803.87842.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354371.7/ ENSP00000346340.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..209
                     /product="COP9 signalosome complex subunit 8 isoform 1"
                     /note="COP9 signalosome complex subunit 8; COP9 homolog;
                     signalosome subunit 8; JAB1-containing signalosome subunit
                     8; COP9 constitutive photomorphogenic homolog subunit 8"
                     /calculated_mol_wt=23095
     Region          31..166
                     /region_name="CSN8_PSD8_EIF3K"
                     /note="CSN8/PSMD8/EIF3K family; pfam10075"
                     /db_xref="CDD:462954"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18850735,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99627.1)"
     CDS             1..209
                     /gene="COPS8"
                     /gene_synonym="COP9; CSN8; SGN8"
                     /coded_by="NM_006710.5:77..706"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2517.1"
                     /db_xref="GeneID:10920"
                     /db_xref="HGNC:HGNC:24335"
                     /db_xref="MIM:616011"
ORIGIN      
        1 mpvavmaesa fsfkklldqc enqeleapgg iatppvygql lalyllhndm nnarylwkri
       61 ppaiksanse lggiwsvgqr iwqrdfpgiy ttinahqwse tvqpimealr datrrrafal
      121 vsqaytsiia ddfaafvglp veeavkgile qgwqadsttr mvlprkpvag aldvsfnkfi
      181 plsepapvpp ipneqqlarl tdyvaflen
//
LOCUS       NP_001352707             326 aa            linear   PRI 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform 15 [Homo sapiens].
ACCESSION   NP_001352707 XP_005254694
VERSION     NP_001352707.1
DBSOURCE    REFSEQ: accession NM_001365778.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Man,Y., Yi,C., Fan,M., Yang,T., Liu,P., Liu,S. and Wang,G.
  TITLE     Identification of a novel missense mutation in the TPM1 gene via
            exome sequencing in a Chinese family with dilated cardiomyopathy: A
            case report and literature review
  JOURNAL   Medicine (Baltimore) 101 (2), e28551 (2022)
   PUBMED   35029218
  REMARK    GeneRIF: Identification of a novel missense mutation in the TPM1
            gene via exome sequencing in a Chinese family with dilated
            cardiomyopathy: A case report and literature review.
            Review article
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11 and AK131384.1.
            
            On Sep 12, 2018 this sequence version replaced XP_005254694.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..326
                     /product="tropomyosin alpha-1 chain isoform 15"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=37322
     Region          2..>159
                     /region_name="EmrA"
                     /note="Multidrug resistance efflux pump EmrA [Defense
                     mechanisms]; COG1566"
                     /db_xref="CDD:441174"
     Region          90..324
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..326
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001365778.1:84..1064"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS92009.1"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak ledelvslqk klkgtedeld kysealkdaq eklelaekka
      121 tdaeadvasl nrriqlveee ldraqerlat alqkleeaek aadesergmk viesraqkde
      181 ekmeiqeiql keakhiaeda drkyeevark lviiesdler aeeraelseg kcaeleeelk
      241 tvtnnlksle aqaekysqke dryeeeikvl sdklkeaetr aefaersvtk leksiddlee
      301 kvahakeenl smhqmldqtl lelnnm
//
LOCUS       NP_003641                145 aa            linear   PRI 27-APR-2025
DEFINITION  cystatin-F precursor [Homo sapiens].
ACCESSION   NP_003641
VERSION     NP_003641.3
DBSOURCE    REFSEQ: accession NM_003650.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Senjor,E., Perisic Nanut,M., Breznik,B., Mitrovic,A., Mlakar,J.,
            Rotter,A., Porcnik,A., Lah Turnsek,T. and Kos,J.
  TITLE     Cystatin F acts as a mediator of immune suppression in glioblastoma
  JOURNAL   Cell Oncol (Dordr) 44 (5), 1051-1063 (2021)
   PUBMED   34189679
  REMARK    GeneRIF: Cystatin F acts as a mediator of immune suppression in
            glioblastoma.
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Li,J., Durose,W.W., Ito,J., Kakita,A., Iguchi,Y., Katsuno,M.,
            Kunisawa,K., Shimizu,T. and Ikenaka,K.
  TITLE     Exploring the factors underlying remyelination arrest by studying
            the post-transcriptional regulatory mechanisms of cystatin F gene
  JOURNAL   J Neurochem 157 (6), 2070-2090 (2021)
   PUBMED   32947653
  REMARK    GeneRIF: Exploring the factors underlying remyelination arrest by
            studying the post-transcriptional regulatory mechanisms of cystatin
            F gene.
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Sawyer,A.J., Garand,M., Chaussabel,D. and Feng,C.G.
  TITLE     Transcriptomic Profiling Identifies Neutrophil-Specific
            Upregulation of Cystatin F as a Marker of Acute Inflammation in
            Humans
  JOURNAL   Front Immunol 12, 634119 (2021)
   PUBMED   33868254
  REMARK    GeneRIF: Transcriptomic Profiling Identifies Neutrophil-Specific
            Upregulation of Cystatin F as a Marker of Acute Inflammation in
            Humans.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Hamilton,G., Colbert,J.D., Schuettelkopf,A.W. and Watts,C.
  TITLE     Cystatin F is a cathepsin C-directed protease inhibitor regulated
            by proteolysis
  JOURNAL   EMBO J 27 (3), 499-508 (2008)
   PUBMED   18256700
  REMARK    GeneRIF: A latent protease inhibitor which is itself regulated by
            proteolysis in the endocytic pathway.
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Cappello,F., Gatti,E., Camossetto,V., David,A., Lelouard,H. and
            Pierre,P.
  TITLE     Cystatin F is secreted, but artificial modification of its
            C-terminus can induce its endocytic targeting
  JOURNAL   Exp Cell Res 297 (2), 607-618 (2004)
   PUBMED   15212960
  REMARK    GeneRIF: CST7 is secreted, but artificial modification of its
            C-terminus can induce its endocytic targeting.
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Morita,M., Hara,Y., Tamai,Y., Arakawa,H. and Nishimura,S.
  TITLE     Genomic construct and mapping of the gene for CMAP
            (leukocystatin/cystatin F, CST7) and identification of a proximal
            novel gene, BSCv (C20orf3)
  JOURNAL   Genomics 67 (1), 87-91 (2000)
   PUBMED   10945474
REFERENCE   7  (residues 1 to 145)
  AUTHORS   Ni,J., Fernandez,M.A., Danielsson,L., Chillakuru,R.A., Zhang,J.,
            Grubb,A., Su,J., Gentz,R. and Abrahamson,M.
  TITLE     Cystatin F is a glycosylated human low molecular weight cysteine
            proteinase inhibitor
  JOURNAL   J Biol Chem 273 (38), 24797-24804 (1998)
   PUBMED   9733783
REFERENCE   8  (residues 1 to 145)
  AUTHORS   Brown,W.M. and Dziegielewska,K.M.
  TITLE     Friends and relations of the cystatin superfamily--new members and
            their evolution
  JOURNAL   Protein Sci 6 (1), 5-12 (1997)
   PUBMED   9007972
  REMARK    Review article
REFERENCE   9  (residues 1 to 145)
  AUTHORS   Thiesse,M., Millar,S.J. and Dickinson,D.P.
  TITLE     The human type 2 cystatin gene family consists of eight to nine
            members, with at least seven genes clustered at a single locus on
            human chromosome 20
  JOURNAL   DNA Cell Biol 13 (2), 97-116 (1994)
   PUBMED   8179826
REFERENCE   10 (residues 1 to 145)
  AUTHORS   Saitoh,E., Isemura,S., Sanada,K., Kim,H.S., Smithies,O. and
            Maeda,N.
  TITLE     Cystatin superfamily. Evidence that family II cystatin genes are
            evolutionarily related to family III cystatin genes
  JOURNAL   Biol Chem Hoppe Seyler 369 Suppl, 191-197 (1988)
   PUBMED   3202964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG547285.1, AF031824.1 and
            CA449286.1.
            
            On Oct 31, 2009 this sequence version replaced NP_003641.2.
            
            Summary: The cystatin superfamily encompasses proteins that contain
            multiple cystatin-like sequences. Some of the members are active
            cysteine protease inhibitors, while others have lost or perhaps
            never acquired this inhibitory activity. There are three inhibitory
            families in the superfamily, including the type 1 cystatins
            (stefins), type 2 cystatins and the kininogens. The type 2 cystatin
            proteins are a class of cysteine proteinase inhibitors found in a
            variety of human fluids and secretions. This gene encodes a
            glycosylated cysteine protease inhibitor with a putative role in
            immune regulation through inhibition of a unique target in the
            hematopoietic system. Expression of the protein has been observed
            in various human cancer cell lines established from malignant
            tumors. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM917046.1, SRR5189655.149795.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:9733783)
            MANE Ensembl match               :: ENST00000480798.2/
                                                ENSP00000420384.1
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.21"
     Protein         1..145
                     /product="cystatin-F precursor"
                     /note="cystatin-like metastasis-associated protein;
                     cystatin-7; leukocystatin"
                     /calculated_mol_wt=14544
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1928
     mat_peptide     20..145
                     /product="cystatin-F"
                     /calculated_mol_wt=14544
     Region          36..145
                     /region_name="CY"
                     /note="Cystatin-like domain; smart00043"
                     /db_xref="CDD:214484"
     Site            order(37,81..83,85)
                     /site_type="active"
                     /note="putative proteinase inhibition site [active]"
                     /db_xref="CDD:238002"
     Site            37
                     /site_type="other"
                     /note="Reactive site; propagated from UniProtKB/Swiss-Prot
                     (O76096.1)"
     Site            62
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16601115; propagated from
                     UniProtKB/Swiss-Prot (O76096.1)"
     Region          81..85
                     /region_name="Secondary area of contact"
                     /note="propagated from UniProtKB/Swiss-Prot (O76096.1)"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16601115; propagated from
                     UniProtKB/Swiss-Prot (O76096.1)"
     CDS             1..145
                     /gene="CST7"
                     /gene_synonym="CMAP"
                     /coded_by="NM_003650.4:238..675"
                     /db_xref="CCDS:CCDS13165.2"
                     /db_xref="GeneID:8530"
                     /db_xref="HGNC:HGNC:2479"
                     /db_xref="MIM:603253"
ORIGIN      
        1 mraagtllaf cclvlsttgg pspdtcsqdl nsrvkpgfpk tiktndpgvl qaarysvekf
       61 nnctndmflf kesritralv qivkglkyml eveigrttck knqhlrlddc dfqtnhtlkq
      121 tlscysevwv vpwlqhfevp vlrch
//
LOCUS       NP_055544                526 aa            linear   PRI 27-APR-2025
DEFINITION  thymocyte selection-associated high mobility group box protein TOX
            [Homo sapiens].
ACCESSION   NP_055544 XP_376776
VERSION     NP_055544.1
DBSOURCE    REFSEQ: accession NM_014729.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Burg,M.M.L., Visser,L. and Diepstra,A.
  TITLE     TOX as a new diagnostic marker for T cell large granular
            lymphocytic leukaemia
  JOURNAL   Histopathology 84 (4), 697-701 (2024)
   PUBMED   38087646
  REMARK    GeneRIF: TOX as a new diagnostic marker for T cell large granular
            lymphocytic leukaemia.
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Ornek,S., Ozekinci,S., Ipin,T. and Kocaturk,E.
  TITLE     TOX, TWIST1, STAT4, and SATB1 protein expressions in early-stage
            mycosis fungoides
  JOURNAL   J Cutan Pathol 51 (3), 232-238 (2024)
   PUBMED   37932931
  REMARK    GeneRIF: TOX, TWIST1, STAT4, and SATB1 protein expressions in
            early-stage mycosis fungoides.
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Mohammadi,M., Asgarian-Omran,H., Najafi,B., Najafi,A., Valadan,R.,
            Karami,H., Naderisoraki,M., Alizadeforoutan,M., Shekarriz,R. and
            Tehrani,M.
  TITLE     Evaluation of mRNA Expressions of TOX and NR4As in CD8+ T cells in
            Acute Leukemia
  JOURNAL   Iran J Immunol 20 (4), 438-445 (2023)
   PUBMED   37961948
  REMARK    GeneRIF: Evaluation of mRNA Expressions of TOX and NR4As in CD8+ T
            cells in Acute Leukemia.
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Niu,H., Yan,L., Yang,L., Zhang,M., Liu,M., Ren,J., Shao,Z., Fu,R.,
            Xing,L. and Wang,H.
  TITLE     High TOX expression on CD8+ T cells in pure red cell aplasia
  JOURNAL   Ann Hematol 102 (5), 1247-1255 (2023)
   PUBMED   36933041
  REMARK    GeneRIF: High TOX expression on CD8[+] T cells in pure red cell
            aplasia.
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Niu,H. and Wang,H.
  TITLE     TOX regulates T lymphocytes differentiation and its function in
            tumor
  JOURNAL   Front Immunol 14, 990419 (2023)
   PUBMED   36969216
  REMARK    GeneRIF: TOX regulates T lymphocytes differentiation and its
            function in tumor.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Sebastiani,P., Wang,L., Nolan,V.G., Melista,E., Ma,Q., Baldwin,C.T.
            and Steinberg,M.H.
  TITLE     Fetal hemoglobin in sickle cell anemia: Bayesian modeling of
            genetic associations
  JOURNAL   Am J Hematol 83 (3), 189-195 (2008)
   PUBMED   17918249
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 526)
  AUTHORS   Stacey,S.N., Manolescu,A., Sulem,P., Rafnar,T., Gudmundsson,J.,
            Gudjonsson,S.A., Masson,G., Jakobsdottir,M., Thorlacius,S.,
            Helgason,A., Aben,K.K., Strobbe,L.J., Albers-Akkers,M.T.,
            Swinkels,D.W., Henderson,B.E., Kolonel,L.N., Le Marchand,L.,
            Millastre,E., Andres,R., Godino,J., Garcia-Prats,M.D., Polo,E.,
            Tres,A., Mouy,M., Saemundsdottir,J., Backman,V.M., Gudmundsson,L.,
            Kristjansson,K., Bergthorsson,J.T., Kostic,J., Frigge,M.L.,
            Geller,F., Gudbjartsson,D., Sigurdsson,H., Jonsdottir,T.,
            Hrafnkelsson,J., Johannsson,J., Sveinsson,T., Myrdal,G.,
            Grimsson,H.N., Jonsson,T., von Holst,S., Werelius,B., Margolin,S.,
            Lindblom,A., Mayordomo,J.I., Haiman,C.A., Kiemeney,L.A.,
            Johannsson,O.T., Gulcher,J.R., Thorsteinsdottir,U., Kong,A. and
            Stefansson,K.
  TITLE     Common variants on chromosomes 2q35 and 16q12 confer susceptibility
            to estrogen receptor-positive breast cancer
  JOURNAL   Nat Genet 39 (7), 865-869 (2007)
   PUBMED   17529974
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Aliahmad,P., O'Flaherty,E., Han,P., Goularte,O.D., Wilkinson,B.,
            Satake,M., Molkentin,J.D. and Kaye,J.
  TITLE     TOX provides a link between calcineurin activation and CD8 lineage
            commitment
  JOURNAL   J Exp Med 199 (8), 1089-1099 (2004)
   PUBMED   15078895
  REMARK    GeneRIF: expression of the HMG box protein TOX is sufficient to
            induce changes in coreceptor gene expression associated with
            beta-selection, including CD8 gene demethylation
REFERENCE   9  (residues 1 to 526)
  AUTHORS   O'Flaherty,E. and Kaye,J.
  TITLE     TOX defines a conserved subfamily of HMG-box proteins
  JOURNAL   BMC Genomics 4 (1), 13 (2003)
   PUBMED   12697058
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Wilkinson,B., Chen,J.Y., Han,P., Rufner,K.M., Goularte,O.D. and
            Kaye,J.
  TITLE     TOX: an HMG box protein implicated in the regulation of thymocyte
            selection
  JOURNAL   Nat Immunol 3 (3), 272-280 (2002)
   PUBMED   11850626
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB018351.1, CA439630.1 and
            AC091195.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 30, 2004 this sequence version replaced XP_376776.1.
            
            Summary: The protein encoded by this gene contains a HMG box DNA
            binding domain. HMG boxes are found in many eukaryotic proteins
            involved in chromatin assembly, transcription and replication. This
            protein may function to regulate T-cell development.[provided by
            RefSeq, Apr 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB018351.1, SRR1660809.135967.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361421.2/ ENSP00000354842.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..526
                     /product="thymocyte selection-associated high mobility
                     group box protein TOX"
                     /note="thymus high mobility group box protein TOX"
                     /calculated_mol_wt=57382
     Region          138..178
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94900.3)"
     Region          192..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94900.3)"
     Region          237..256
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94900.3)"
     Region          262..331
                     /region_name="HMG-box_TOX-like"
                     /note="high mobility group (HMG)-box found in the TOX high
                     mobility group box family; cd21995"
                     /db_xref="CDD:438811"
     Site            order(262..263,265..269,272..273,280,292..293,296,
                     299..300,307,311,314,318,321)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438811"
     CDS             1..526
                     /gene="TOX"
                     /gene_synonym="TOX1"
                     /coded_by="NM_014729.3:161..1741"
                     /db_xref="CCDS:CCDS34897.1"
                     /db_xref="GeneID:9760"
                     /db_xref="HGNC:HGNC:18988"
                     /db_xref="MIM:606863"
ORIGIN      
        1 mdvrfypppa qpaaapdapc lgpspcldpy ycnkfdgenm ymsmtepsqd yvpasqsypg
       61 pslesedfni ppitppslpd hslvhlneve sgyhslchpm nhngllpfhp qnmdlpeitv
      121 snmlgqdgtl lsnsisvmpd irnpegtqys shpqmaamrp rgqpadirqq pgmmphgqlt
      181 tinqsqlsaq lglnmggsnv phnspsppgs ksatpspsss vhedegddts kinggekrpa
      241 sdmgkkpktp kkkkkkdpne pqkpvsayal ffrdtqaaik gqnpnatfge vskivasmwd
      301 glgeeqkqvy kkkteaakke ylkqlaayra slvsksysep vdvktsqppq linskpsvfh
      361 gpsqahsaly lsshyhqqpg mnphltamhp slprniapkp nnqmpvtvsi anmavspppp
      421 lqispplhqh lnmqqhqplt mqqplgnqlp mqvqsalhsp tmqqgftlqp dyqtiinpts
      481 taaqvvtqam eyvrsgcrnp ppqpvdwnnd ycssggmqrd kalylt
//
LOCUS       NP_666252                363 aa            linear   ROD 27-APR-2025
DEFINITION  translocating chain-associated membrane protein 1-like 1 [Mus
            musculus].
ACCESSION   NP_666252
VERSION     NP_666252.1
DBSOURCE    REFSEQ: accession NM_146140.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114625.11.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK044115.1, AK048118.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3 54.68 cM"
     Protein         1..363
                     /product="translocating chain-associated membrane protein
                     1-like 1"
                     /calculated_mol_wt=40852
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8QZR0.1)"
     Region          50..114
                     /region_name="TRAM1"
                     /note="TRAM1-like protein; pfam08390"
                     /db_xref="CDD:462460"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8QZR0.1)"
     Region          116..324
                     /region_name="TLC"
                     /note="TRAM, LAG1 and CLN8 homology domains; smart00724"
                     /db_xref="CDD:214789"
     Site            121..141
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8QZR0.1)"
     Site            160..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8QZR0.1)"
     Site            192..214
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8QZR0.1)"
     Site            219..241
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8QZR0.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8QZR0.1)"
     Site            296..316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8QZR0.1)"
     Region          338..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8QZR0.1)"
     CDS             1..363
                     /gene="Tram1l1"
                     /gene_synonym="A830091N21Rik"
                     /coded_by="NM_146140.4:157..1248"
                     /db_xref="CCDS:CCDS17819.1"
                     /db_xref="GeneID:229801"
                     /db_xref="MGI:MGI:2443503"
ORIGIN      
        1 mglrkknarn ppvlshefmv qnhadmvscv gmffvlglmf egtsemsiaf ltlqhgvvvp
       61 aeglpsgsrt lyhygvkdla tvffymlvai iihatiqeyv ldklsrrlql tkgkqnklne
      121 agqlsvfyiv sgiwgmiila senclsdptl lwksqphnmm tfqmkffyis qlaywfhsfp
      181 elyfqkvrkq dipgqliyig lhlfhiggay llylnhlgll llmlhyavel lssvcsllyf
      241 gderyqkgls lwpivfisgr lvtlivsvvt vglhlagtnr ngnalsgnvn vlaakiavls
      301 sscsiqvyit wtlttvwlqr wledanlhvc grkrrsrark gtengvenpn ridsppkkke
      361 kap
//
LOCUS       NP_015561                567 aa            linear   PRI 27-APR-2025
DEFINITION  ran-binding protein 3 isoform RANBP3-d [Homo sapiens].
ACCESSION   NP_015561
VERSION     NP_015561.1
DBSOURCE    REFSEQ: accession NM_007322.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Tang,W., Zhu,Y., Qin,W., Zhang,H., Zhang,H., Lin,H., Zhen,X.,
            Zhuang,X., Tang,Y. and Jiang,H.
  TITLE     Ran-binding protein 3 is associated with human spermatogenesis and
            male infertility
  JOURNAL   Andrologia 52 (2), e13446 (2020)
   PUBMED   31833110
  REMARK    GeneRIF: Ran-binding protein 3 is associated with human
            spermatogenesis and male infertility.
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Koyama,M. and Matsuura,Y.
  TITLE     Crystal structure of importin-alpha3 bound to the nuclear
            localization signal of Ran-binding protein 3
  JOURNAL   Biochem Biophys Res Commun 491 (3), 609-613 (2017)
   PUBMED   28760339
  REMARK    GeneRIF: Computational docking simulation indicates that
            phosphorylation of RanBP3 at Ser58 could potentially stabilize the
            association of RanBP3 with importin-alpha through interactions
            between the phosphate moiety of phospho-Ser58 of RanBP3 and a
            cluster of basic residues (Arg96 and Lys97 in importin-alpha3) on
            armadillo repeat 1 of importin-alpha.
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Pathria,G., Garg,B., Wagner,C., Garg,K., Gschaider,M., Jalili,A.
            and Wagner,S.N.
  TITLE     RanBP3 Regulates Melanoma Cell Proliferation via Selective Control
            of Nuclear Export
  JOURNAL   J Invest Dermatol 136 (1), 264-274 (2016)
   PUBMED   26763446
  REMARK    GeneRIF: RANBP3 regulates melanoma cell proliferation and probably
            a potential target for molecular targeted therapy.
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Predicala,R. and Zhou,Y.
  TITLE     The role of Ran-binding protein 3 during influenza A virus
            replication
  JOURNAL   J Gen Virol 94 (Pt 5), 977-984 (2013)
   PUBMED   23303829
  REMARK    GeneRIF: RanBP3 is involved in vRNP nuclear export. The function of
            RanBP3 during vRNP nuclear export is regulated by phosphorylation
            at Ser58. RanBP3 phosphorylation is modulated by both PI3K/Akt and
            Ras/ERK/RSK pathways in the late phase of viral infection.
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Englmeier,L., Fornerod,M., Bischoff,F.R., Petosa,C., Mattaj,I.W.
            and Kutay,U.
  TITLE     RanBP3 influences interactions between CRM1 and its nuclear protein
            export substrates
  JOURNAL   EMBO Rep 2 (10), 926-932 (2001)
   PUBMED   11571268
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Lindsay,M.E., Holaska,J.M., Welch,K., Paschal,B.M. and Macara,I.G.
  TITLE     Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear
            protein export
  JOURNAL   J Cell Biol 153 (7), 1391-1402 (2001)
   PUBMED   11425870
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Welch,K., Franke,J., Kohler,M. and Macara,I.G.
  TITLE     RanBP3 contains an unusual nuclear localization signal that is
            imported preferentially by importin-alpha3
  JOURNAL   Mol Cell Biol 19 (12), 8400-8411 (1999)
   PUBMED   10567565
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Mueller,L., Cordes,V.C., Bischoff,F.R. and Ponstingl,H.
  TITLE     Human RanBP3, a group of nuclear RanGTP binding proteins
  JOURNAL   FEBS Lett 427 (3), 330-336 (1998)
   PUBMED   9637251
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM786367.1 and AK025300.1.
            
            Summary: This gene encodes a protein with a RanBD1 domain that is
            found in both the nucleus and cytoplasm. This protein plays a role
            in nuclear export as part of a heteromeric complex. Alternate
            transcriptional splice variants, encoding different isoforms, have
            been characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (RANBP3-d) represents the longest
            transcript and encodes the longest isoform (RANBP3-d).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK025300.1, AL050149.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340578.10/ ENSP00000341483.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..567
                     /product="ran-binding protein 3 isoform RANBP3-d"
                     /note="ran-binding protein 3; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=60079
     Region          1..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CT10; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Region          117..125
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:10567565"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18280241,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CT10; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Region          332..373
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Region          393..508
                     /region_name="RanBD_RanBP3"
                     /note="Ran-binding protein 3 Ran-binding domain; cd13180"
                     /db_xref="CDD:270001"
     Site            order(407,409..411,416..421,442,444,446..447,451..453,456,
                     458,462,466,474,476,487,491)
                     /site_type="other"
                     /note="putative RAN binding site [polypeptide binding]"
                     /db_xref="CDD:270001"
     Region          515..567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H6Z4.1)"
     CDS             1..567
                     /gene="RANBP3"
                     /coded_by="NM_007322.3:59..1762"
                     /note="isoform RANBP3-d is encoded by transcript variant
                     RANBP3-d"
                     /db_xref="CCDS:CCDS42478.1"
                     /db_xref="GeneID:8498"
                     /db_xref="HGNC:HGNC:9850"
                     /db_xref="MIM:603327"
ORIGIN      
        1 madlaneekp aiappvfvfq kdkgqkspae qknlsdsgee prgeaeaphh gtghpesage
       61 haleppapag asastppppa peaqlppfpr elagrsaggs speggedsdr edgnycppvk
      121 rertssltqf ppsqseerss gfrlkpptli hgqapsaglp sqkpkeqqrs vlrpavlqap
      181 qpkalsqtvp ssgtngvslp adctgavpaa spdtaawrsp seaadevcal eekepqknes
      241 snaseeeace kkdpatqqaf vfgqnlrdrv klinesvdea dmenaghpsa dtptatnyfl
      301 qyissslens tnsadassnk fvfgqnmser vlsppklnev ssdanrenaa aesgsesssq
      361 eatpekesla esaaaytkat arkcllekve vitgeeaesn vlqmqcklfv fdktsqswve
      421 rgrgllrlnd mastddgtlq srlvmrtqgs lrlilntklw aqmqidkase ksiritamdt
      481 edqgvkvfli sasskdtgql yaalhhrila lrsrveqeqe akmpapepga apsneeddsd
      541 dddvlapsga taagagdegd gqttgst
//
LOCUS       NP_001356801            1153 aa            linear   PRI 27-APR-2025
DEFINITION  tight junction protein 2 isoform 8 [Homo sapiens].
ACCESSION   NP_001356801 XP_016870816
VERSION     NP_001356801.1
DBSOURCE    REFSEQ: accession NM_001369872.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1153)
  AUTHORS   Ouyang,H., Wu,S., Li,W., Grey,M.J., Wu,W. and Hansen,S.H.
  TITLE     p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP
  JOURNAL   Cell Rep 42 (12), 113486 (2023)
   PUBMED   37995182
  REMARK    GeneRIF: p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP.
REFERENCE   2  (residues 1 to 1153)
  AUTHORS   Gallego-Gutierrez,H., Gonzalez-Gonzalez,L., Ramirez-Martinez,L.,
            Lopez-Bayghen,E. and Gonzalez-Mariscal,L.
  TITLE     Tight junction protein ZO-2 modulates the nuclear accumulation of
            transcription factor TEAD
  JOURNAL   Mol Biol Cell 32 (15), 1347-1358 (2021)
   PUBMED   34010016
  REMARK    GeneRIF: Tight junction protein ZO-2 modulates the nuclear
            accumulation of transcription factor TEAD.
REFERENCE   3  (residues 1 to 1153)
  AUTHORS   Wei,C.S., Becher,N., Friis,J.B., Ott,P., Vogel,I. and Gronbaek,H.
  TITLE     New tight junction protein 2 variant causing progressive familial
            intrahepatic cholestasis type 4 in adults: A case report
  JOURNAL   World J Gastroenterol 26 (5), 550-561 (2020)
   PUBMED   32089630
  REMARK    GeneRIF: New tight junction protein 2 variant causing progressive
            familial intrahepatic cholestasis type 4 in adults: A case report.
REFERENCE   4  (residues 1 to 1153)
  AUTHORS   Walsh,T., Pierce,S.B., Lenz,D.R., Brownstein,Z.,
            Dagan-Rosenfeld,O., Shahin,H., Roeb,W., McCarthy,S., Nord,A.S.,
            Gordon,C.R., Ben-Neriah,Z., Sebat,J., Kanaan,M., Lee,M.K.,
            Frydman,M., King,M.C. and Avraham,K.B.
  TITLE     Genomic duplication and overexpression of TJP2/ZO-2 leads to
            altered expression of apoptosis genes in progressive nonsyndromic
            hearing loss DFNA51
  JOURNAL   Am J Hum Genet 87 (1), 101-109 (2010)
   PUBMED   20602916
  REMARK    GeneRIF: TJP2- and GSK-3beta-mediated increased susceptibility to
            apoptosis of cells of the inner ear is the mechanism for
            adult-onset hearing loss in this kindred and may serve as one model
            for age-related hearing loss in the general population.
REFERENCE   5  (residues 1 to 1153)
  AUTHORS   Itoh,M., Morita,K. and Tsukita,S.
  TITLE     Characterization of ZO-2 as a MAGUK family member associated with
            tight as well as adherens junctions with a binding affinity to
            occludin and alpha catenin
  JOURNAL   J Biol Chem 274 (9), 5981-5986 (1999)
   PUBMED   10026224
REFERENCE   6  (residues 1 to 1153)
  AUTHORS   Denker,B.M. and Nigam,S.K.
  TITLE     Molecular structure and assembly of the tight junction
  JOURNAL   Am J Physiol 274 (1), F1-F9 (1998)
   PUBMED   9458817
  REMARK    Review article
REFERENCE   7  (residues 1 to 1153)
  AUTHORS   Beatch,M., Jesaitis,L.A., Gallin,W.J., Goodenough,D.A. and
            Stevenson,B.R.
  TITLE     The tight junction protein ZO-2 contains three PDZ
            (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced
            region
  JOURNAL   J Biol Chem 271 (42), 25723-25726 (1996)
   PUBMED   8824195
REFERENCE   8  (residues 1 to 1153)
  AUTHORS   Duclos,F., Rodius,F., Wrogemann,K., Mandel,J.L. and Koenig,M.
  TITLE     The Friedreich ataxia region: characterization of two novel genes
            and reduction of the critical region to 300 kb
  JOURNAL   Hum Mol Genet 3 (6), 909-914 (1994)
   PUBMED   7951235
REFERENCE   9  (residues 1 to 1153)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
REFERENCE   10 (residues 1 to 1153)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL358113.21.
            
            On Apr 23, 2019 this sequence version replaced XP_016870816.1.
            
            Summary: This gene encodes a zonula occluden that is a member of
            the membrane-associated guanylate kinase homolog family. The
            encoded protein functions as a component of the tight junction
            barrier in epithelial and endothelial cells and is necessary for
            proper assembly of tight junctions. Mutations in this gene have
            been identified in patients with hypercholanemia, and genomic
            duplication of a 270 kb region including this gene causes autosomal
            dominant deafness-51. Alternatively spliced transcripts encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Nov 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.103352.1,
                                           SRR1803615.8317.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.11"
     Protein         1..1153
                     /product="tight junction protein 2 isoform 8"
                     /note="Friedreich ataxia region gene X104 (tight junction
                     protein ZO-2); zona occludens 2; zonula occludens protein
                     2"
                     /calculated_mol_wt=129705
     Region          32..118
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(43..49,67,70,98,102,105..106)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          144..>226
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Region          183..>274
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Region          306..384
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(306..312,317..333,336..338,341,343..344,351,
                     359..360,362..363,375..381)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(318..324,330,333,363,367,370..371)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Region          509..590
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(520..526,536,539,568,572,575..576)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          604..666
                     /region_name="SH3_ZO-2"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 2; cd12027"
                     /db_xref="CDD:212960"
     Site            order(613,615,618,622,643..644,660,662..663)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212960"
     Region          700..879
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     CDS             1..1153
                     /gene="TJP2"
                     /gene_synonym="C9DUPq21.11; DFNA51; DUP9q21.11; FHCA1;
                     PFIC4; X104; ZO2"
                     /coded_by="NM_001369872.1:97..3558"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:9414"
                     /db_xref="HGNC:HGNC:11828"
                     /db_xref="MIM:607709"
ORIGIN      
        1 mpvrgdrgfp prrelsgwlr apgmeeliwe qytvtlqkds krgfgiavsg grdnphfeng
       61 etsivisdvl pggpadgllq endrvvmvng tpmedvlhsf avqqlrksgk vaaivvkrpr
      121 kvqvaalqas ppldqddraf evmdefdgrs frsgysersr lnshggrsrs wedspergrp
      181 herarsrerd lsrdrsrgrs lergldqdha rtrdrsrgrs lergldhdfg psrdrdrdrs
      241 rgrsidqdye rayhraydpd yerayspeyr rgarhdarsr gprsrsrehp hsrspspepr
      301 grpgpigvll mksraneeyg lrlgsqifvk emtrtglatk dgnlhegdii lkingtvten
      361 msltdarkli eksrgklqlv vlrdsqqtli nipslndsds eiediseies nrsfspeerr
      421 hqysdydyhs sseklkerps sredtpsrls rmgatptpfk stgdiagtvv petnkepryq
      481 edppapqpka aprtflrpsp edeaiygpnt kmvrfkkgds vglrlaggnd vgifvagiqe
      541 gtsaeqeglq egdqilkvnt qdfrglvred avlylleipk gemvtilaqs radvyrdila
      601 cgrgdsffir shfeceketp qslaftrgev frvvdtlydg klgnwlavri gnelekglip
      661 nksraeqmas vqnaqrdnag dradfwrmrg qrsgvkknlr ksredltavv svstkfpaye
      721 rvllreagfk rpvvlfgpia diameklane lpdwfqtakt epkdagseks tgvvrlntvr
      781 qiieqdkhal ldvtpkavdl lnytqwfpiv iffnpdsrqg vktmrqrlnp tsnkssrklf
      841 dqanklkktc ahlftatinl nsandswfgs lkdtiqhqqg eavwvsegkm egmdddpedr
      901 msyltamgad ylscdsrlis dfedtdgegg aytdneldep aeeplvssit rssepvqhee
      961 aktqnkeesy dfsksyeyks npsavagnet pgastkgypp pvaakptfgr silkpstpip
     1021 pqegeevges seeqdnapks vlgkvkifek mdhkarlqrm qelqeaqnar ieiaqkhpdi
     1081 yavpikthkp dpgtpqhtss rppepqkaps rpyqdtrgsy gsdaeeeeyr qqlsehskrg
     1141 yygqsaryrd tel
//
LOCUS       NP_079725                213 aa            linear   ROD 27-APR-2025
DEFINITION  nicolin-1 isoform 1 [Mus musculus].
ACCESSION   NP_079725
VERSION     NP_079725.1
DBSOURCE    REFSEQ: accession NM_025449.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Mulligan,M.K., Ponomarev,I., Hitzemann,R.J., Belknap,J.K.,
            Tabakoff,B., Harris,R.A., Crabbe,J.C., Blednov,Y.A., Grahame,N.J.,
            Phillips,T.J., Finn,D.A., Hoffman,P.L., Iyer,V.R., Koob,G.F. and
            Bergeson,S.E.
  TITLE     Toward understanding the genetics of alcohol drinking through
            transcriptome meta-analysis
  JOURNAL   Proc Natl Acad Sci U S A 103 (16), 6368-6373 (2006)
   PUBMED   16618939
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Janke,C., Rogowski,K., Wloga,D., Regnard,C., Kajava,A.V.,
            Strub,J.M., Temurak,N., van Dijk,J., Boucher,D., van Dorsselaer,A.,
            Suryavanshi,S., Gaertig,J. and Edde,B.
  TITLE     Tubulin polyglutamylase enzymes are members of the TTL domain
            protein family
  JOURNAL   Science 308 (5729), 1758-1762 (2005)
   PUBMED   15890843
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Garcia-Frigola,C., Burgaya,F., Calbet,M., Lopez-Domenech,G., de
            Lecea,L. and Soriano,E.
  TITLE     A collection of cDNAs enriched in upper cortical layers of the
            embryonic mouse brain
  JOURNAL   Brain Res Mol Brain Res 122 (2), 133-150 (2004)
   PUBMED   15010206
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Backofen,B., Jacob,R., Serth,K., Gossler,A., Naim,H.Y. and Leeb,T.
  TITLE     Cloning and characterization of the mammalian-specific nicolin 1
            gene (NICN1) encoding a nuclear 24 kDa protein
  JOURNAL   Eur J Biochem 269 (21), 5240-5245 (2002)
   PUBMED   12392556
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Backofen,B. and Leeb,T.
  TITLE     Genomic organization of the murine aminomethyltransferase gene
            (Amt)
  JOURNAL   DNA Seq 13 (4), 179-183 (2002)
   PUBMED   12487019
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC161260.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK146890.1, AK169135.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 59.18 cM"
     Protein         1..213
                     /product="nicolin-1 isoform 1"
                     /note="tubulin polyglutamylase complex subunit 5"
                     /calculated_mol_wt=24229
     CDS             1..213
                     /gene="Nicn1"
                     /gene_synonym="1500032A17Rik; p24; PGs5"
                     /coded_by="NM_025449.4:89..730"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS40767.1"
                     /db_xref="GeneID:66257"
                     /db_xref="MGI:MGI:1913507"
ORIGIN      
        1 msrvlvpchv kstvalqvgd mrtsqgrpgv lvvdvtfpni apfelqeimf knyytaflsi
       61 rvrqqssmht aakwvtclrd yclmpdphse egaqdyvslf khqmlcdmnr vlelrlilrq
      121 psplwlsftv eelqiyqqgp kspslafpkw lshpvsneqp aprleglpdp srvssevqqm
      181 waltemiras htstrigrfd vdgcydlnll syt
//
LOCUS       NP_001350610             890 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear factor of activated T-cells, cytoplasmic 4 isoform 8 [Homo
            sapiens].
ACCESSION   NP_001350610 XP_011535099
VERSION     NP_001350610.1
DBSOURCE    REFSEQ: accession NM_001363681.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 890)
  AUTHORS   Yu,S., Sun,Z., Ju,T., Liu,Y., Mei,Z., Wang,C., Qu,Z., Li,N., Wu,F.,
            Liu,K., Lu,M., Huang,M., Pang,X., Jia,Y., Li,Y., Zhang,Y., Dou,S.,
            Jiang,J., Dong,X., Huang,C., Li,W., Zhang,Y., Yuan,Y., Yang,B. and
            Du,W.
  TITLE     The m7G Methyltransferase Mettl1 Drives Cardiac Hypertrophy by
            Regulating SRSF9-Mediated Splicing of NFATc4
  JOURNAL   Adv Sci (Weinh) 11 (29), e2308769 (2024)
   PUBMED   38810124
  REMARK    GeneRIF: The m7G Methyltransferase Mettl1 Drives Cardiac
            Hypertrophy by Regulating SRSF9-Mediated Splicing of NFATc4.
REFERENCE   2  (residues 1 to 890)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 890)
  AUTHORS   Zhang,X., Lei,F., Wang,X.M., Deng,K.Q., Ji,Y.X., Zhang,Y., Li,H.,
            Zhang,X.D., Lu,Z. and Zhang,P.
  TITLE     NULP1 Alleviates Cardiac Hypertrophy by Suppressing NFAT3
            Transcriptional Activity
  JOURNAL   J Am Heart Assoc 9 (16), e016419 (2020)
   PUBMED   32805187
  REMARK    GeneRIF: NULP1 Alleviates Cardiac Hypertrophy by Suppressing NFAT3
            Transcriptional Activity.
REFERENCE   4  (residues 1 to 890)
  AUTHORS   Cole,A.J., Iyengar,M., Panesso-Gomez,S., O'Hayer,P., Chan,D.,
            Delgoffe,G.M., Aird,K.M., Yoon,E., Bai,S. and Buckanovich,R.J.
  TITLE     NFATC4 promotes quiescence and chemotherapy resistance in ovarian
            cancer
  JOURNAL   JCI Insight 5 (7), 131486 (2020)
   PUBMED   32182216
  REMARK    GeneRIF: NFATC4 promotes quiescence and chemotherapy resistance in
            ovarian cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 890)
  AUTHORS   Kaminuma,O., Kitamura,N., Nishito,Y., Nemoto,S., Tatsumi,H.,
            Mori,A. and Hiroi,T.
  TITLE     Downregulation of NFAT3 Due to Lack of T-Box Transcription Factor
            TBX5 Is Crucial for Cytokine Expression in T Cells
  JOURNAL   J Immunol 200 (1), 92-100 (2018)
   PUBMED   29180489
  REMARK    GeneRIF: TBX5 deficiency-mediated downregulation of NFAT3 is
            crucial for the high cytokine-producing activity of T cells
REFERENCE   6  (residues 1 to 890)
  AUTHORS   Molkentin,J.D., Lu,J.R., Antos,C.L., Markham,B., Richardson,J.,
            Robbins,J., Grant,S.R. and Olson,E.N.
  TITLE     A calcineurin-dependent transcriptional pathway for cardiac
            hypertrophy
  JOURNAL   Cell 93 (2), 215-228 (1998)
   PUBMED   9568714
REFERENCE   7  (residues 1 to 890)
  AUTHORS   Aramburu,J., Garcia-Cozar,F., Raghavan,A., Okamura,H., Rao,A. and
            Hogan,P.G.
  TITLE     Selective inhibition of NFAT activation by a peptide spanning the
            calcineurin targeting site of NFAT
  JOURNAL   Mol Cell 1 (5), 627-637 (1998)
   PUBMED   9660947
REFERENCE   8  (residues 1 to 890)
  AUTHORS   Rao,A., Luo,C. and Hogan,P.G.
  TITLE     Transcription factors of the NFAT family: regulation and function
  JOURNAL   Annu Rev Immunol 15, 707-747 (1997)
   PUBMED   9143705
  REMARK    Review article
REFERENCE   9  (residues 1 to 890)
  AUTHORS   Hoey,T., Sun,Y.L., Williamson,K. and Xu,X.
  TITLE     Isolation of two new members of the NF-AT gene family and
            functional characterization of the NF-AT proteins
  JOURNAL   Immunity 2 (5), 461-472 (1995)
   PUBMED   7749981
REFERENCE   10 (residues 1 to 890)
  AUTHORS   Vacca,A., Farina,M., Maroder,M., Alesse,E., Screpanti,I., Frati,L.
            and Gulino,A.
  TITLE     Human immunodeficiency virus type-1 tat enhances interleukin-2
            promoter activity through synergism with phorbol ester and
            calcium-mediated activation of the NF-AT cis-regulatory motif
  JOURNAL   Biochem Biophys Res Commun 205 (1), 467-474 (1994)
   PUBMED   7999066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL096870.5 and EU887644.1.
            
            On May 30, 2018 this sequence version replaced XP_011535099.1.
            
            Summary: This gene encodes a member of the nuclear factor of
            activated T cells (NFAT) protein family. The encoded protein is
            part of a DNA-binding transcription complex. This complex consists
            of at least two components: a preexisting cytosolic component that
            translocates to the nucleus upon T cell receptor stimulation and an
            inducible nuclear component. NFAT proteins are activated by the
            calmodulin-dependent phosphatase, calcineurin. The encoded protein
            plays a role in the inducible expression of cytokine genes in T
            cells, especially in the induction of interleukin-2 and
            interleukin-4. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jan 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU887644.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..890
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..890
                     /product="nuclear factor of activated T-cells, cytoplasmic
                     4 isoform 8"
                     /note="nuclear factor of activated T-cells, cytoplasmic 4;
                     T-cell transcription factor NFAT3; nuclear factor of
                     activated T-cells, cytoplasmic, calcineurin-dependent 4"
                     /calculated_mol_wt=94015
     Region          <202..401
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          395..568
                     /region_name="RHD-n_NFAT"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor of activated T-cells (NFAT)
                     proteins; cd07881"
                     /db_xref="CDD:143641"
     Site            order(418,421,423..424,426..428,475,516,518..519,533..534,
                     536,567)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143641"
     Region          573..673
                     /region_name="IPT_NFAT"
                     /note="IPT domain of the NFAT family of transcription
                     factors. NFAT transcription complexes are a target of
                     calcineurin, a calcium dependent phosphatase, and activate
                     genes mainly involved in cell-cell-interaction; cd01178"
                     /db_xref="CDD:238583"
     Site            order(597,661)
                     /site_type="DNA binding"
                     /note="DNA binding sites [nucleotide binding]"
                     /db_xref="CDD:238583"
     CDS             1..890
                     /gene="NFATC4"
                     /gene_synonym="NF-AT3; NF-ATC4; NFAT3"
                     /coded_by="NM_001363681.1:316..2988"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS86380.1"
                     /db_xref="GeneID:4776"
                     /db_xref="HGNC:HGNC:7778"
                     /db_xref="MIM:602699"
ORIGIN      
        1 mpasissifp gptlllscgs eeldsedapp ccrlalgepp pygaapigip rpppprpgmh
       61 sppprpapsp gtwesqpars vrlggpggga ggagggrvle cpsiritsis ptpeppaale
      121 dnpdawgdgs prdypppegf ggyreaggqg ggaffspspg ssslsswsff sdasdeaaly
      181 aacdevesel neaasrfglg splpsprasp rpwtpedpws lygpspggrg pedswlllsa
      241 pgptpasprp aspcgkrrys ssgtpssasp alsrrgslge egsepppppp lplardpgsp
      301 gpfdyvgapp aesipqktrr tsseqavalp rseepascng klplgaeesv appggsrkev
      361 agmdylavps plawskarig ghspifrtsa lppldwplps qyeqlelrie vqprahhrah
      421 yetegsrgav kaapgghpvv kllgysekpl tlqmfigtad ernlrphafy qvhritgkmv
      481 atasyeavvs gtkvlemtll pennmaanid cagilklrns dielrkgetd igrkntrvrl
      541 vfrvhvpqgg gkvvsvqaas vpiecsqrsa qelpqveays psacsvrgge elvltgsnfl
      601 pdskvvfier gpdgklqwee eatvnrlqsn evtltltvpe ysnkrvsrpv qvyfyvsngr
      661 rkrsptqsfr flpvickeep lpdsslrgfp sasatpfgtd mdfspprppy psyphedpac
      721 etpylsegfg ygmpplypqt gpppsyrpgl rmfpetrgtt gcaqppavsf lprpfpsdpy
      781 ggrgssfslg lpfsppapfr ppplpasppl egpfpsqsdv hplpaegynk vgpgygpgeg
      841 apeqeksrgg yssgfrdsvp iqgitleevs eiigrdlsgf pappgeeppa
//
LOCUS       NP_938017                198 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 17 [Homo sapiens].
ACCESSION   NP_938017 XP_117267
VERSION     NP_938017.2
DBSOURCE    REFSEQ: accession NM_198276.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Wang,S., Zhou,Q., Yan,S., Liu,C., Li,F., Feng,D. and He,M.
  TITLE     TMEM17 Promotes Tumor Progression in Glioblastoma by Activating the
            PI3K/AKT Pathway
  JOURNAL   Front Biosci (Landmark Ed) 29 (8), 285 (2024)
   PUBMED   39206901
  REMARK    GeneRIF: TMEM17 Promotes Tumor Progression in Glioblastoma by
            Activating the PI3K/AKT Pathway.
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Zhang,X., Zhang,Y., Miao,Y., Zhou,H., Jiang,G. and Wang,E.
  TITLE     TMEM17 depresses invasion and metastasis in lung cancer cells via
            ERK signaling pathway
  JOURNAL   Oncotarget 8 (41), 70685-70694 (2017)
   PUBMED   29050311
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Li,C., Jensen,V.L., Park,K., Kennedy,J., Garcia-Gonzalo,F.R.,
            Romani,M., De Mori,R., Bruel,A.L., Gaillard,D., Doray,B., Lopez,E.,
            Riviere,J.B., Faivre,L., Thauvin-Robinet,C., Reiter,J.F.,
            Blacque,O.E., Valente,E.M. and Leroux,M.R.
  TITLE     MKS5 and CEP290 Dependent Assembly Pathway of the Ciliary
            Transition Zone
  JOURNAL   PLoS Biol 14 (3), e1002416 (2016)
   PUBMED   26982032
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Kenny,E.E., Pe'er,I., Karban,A., Ozelius,L., Mitchell,A.A.,
            Ng,S.M., Erazo,M., Ostrer,H., Abraham,C., Abreu,M.T., Atzmon,G.,
            Barzilai,N., Brant,S.R., Bressman,S., Burns,E.R., Chowers,Y.,
            Clark,L.N., Darvasi,A., Doheny,D., Duerr,R.H., Eliakim,R.,
            Giladi,N., Gregersen,P.K., Hakonarson,H., Jones,M.R., Marder,K.,
            McGovern,D.P., Mulle,J., Orr-Urtreger,A., Proctor,D.D., Pulver,A.,
            Rotter,J.I., Silverberg,M.S., Ullman,T., Warren,S.T., Waterman,M.,
            Zhang,W., Bergman,A., Mayer,L., Katz,S., Desnick,R.J., Cho,J.H. and
            Peter,I.
  TITLE     A genome-wide scan of Ashkenazi Jewish Crohn's disease suggests
            novel susceptibility loci
  JOURNAL   PLoS Genet 8 (3), e1002559 (2012)
   PUBMED   22412388
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DR760587.1, BC047439.1 and AC093159.3.
            
            On Dec 13, 2008 this sequence version replaced NP_938017.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The extent of this RefSeq
            transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1113291.1,
                                           SRR5189667.224371.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267775 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335390.6/ ENSP00000335094.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p15"
     Protein         1..198
                     /product="transmembrane protein 17"
                     /calculated_mol_wt=22915
     Site            13
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86X19.2)"
     Site            23
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86X19.2)"
     Region          45..151
                     /region_name="Transmemb_17"
                     /note="Predicted membrane protein; pfam09799"
                     /db_xref="CDD:462907"
     Site            45..65
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X19.2)"
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X19.2)"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X19.2)"
     Site            142..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X19.2)"
     CDS             1..198
                     /gene="TMEM17"
                     /coded_by="NM_198276.3:67..663"
                     /db_xref="CCDS:CCDS1871.1"
                     /db_xref="GeneID:200728"
                     /db_xref="HGNC:HGNC:26623"
                     /db_xref="MIM:614950"
ORIGIN      
        1 melpdpvrqr lgnfsravfs dsnrtgpesn egpenemvss lalqmslyfn tyyfplwwvs
       61 simmlhmkys ilpdyykfiv itviilitli eairlylgyv gnlqekvpel agfwllslll
      121 qlplilfllf negltnlple kaihiiftlf lafqvvaafl tlrkmvnqla vrfhlqdfdr
      181 lsanrgdmrr mrscieei
//
LOCUS       NP_001348417             109 aa            linear   ROD 27-APR-2025
DEFINITION  aspartate beta-hydroxylase domain-containing protein 1 isoform 2
            [Mus musculus].
ACCESSION   NP_001348417
VERSION     NP_001348417.1
DBSOURCE    REFSEQ: accession NM_001361488.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Mattiske,T., Lee,K., Gecz,J., Friocourt,G. and Shoubridge,C.
  TITLE     Embryonic forebrain transcriptome of mice with polyalanine
            expansion mutations in the ARX homeobox gene
  JOURNAL   Hum Mol Genet 25 (24), 5433-5443 (2016)
   PUBMED   27798109
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK043553.1 and BE950878.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK043553.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164138
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 69.25 cM"
     Protein         1..109
                     /product="aspartate beta-hydroxylase domain-containing
                     protein 1 isoform 2"
                     /note="aspartate beta-hydroxylase domain-containing
                     protein 1"
                     /calculated_mol_wt=11469
     Region          <1..91
                     /region_name="Asp_Arg_Hydrox"
                     /note="Aspartyl/Asparaginyl beta-hydroxylase; pfam05118"
                     /db_xref="CDD:461552"
     CDS             1..109
                     /gene="Asphd1"
                     /gene_synonym="A830007L07Rik; Gm168"
                     /coded_by="NM_001361488.1:289..618"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS40134.1"
                     /db_xref="GeneID:233879"
                     /db_xref="MGI:MGI:2685014"
ORIGIN      
        1 msantfgnag fsvllpgarl egrcgptnar vrchlglkip pgcelvvgge pqcwaeghcl
       61 lvddsflhtv ahngspedgp rvvfivdlwh pnvagaerqa ldfvfapdp
//
LOCUS       NP_001356793             133 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 91 isoform c [Homo sapiens].
ACCESSION   NP_001356793
VERSION     NP_001356793.1
DBSOURCE    REFSEQ: accession NM_001369864.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Sallman Almen,M., Bringeland,N., Fredriksson,R. and Schioth,H.B.
  TITLE     The dispanins: a novel gene family of ancient origin that contains
            14 human members
  JOURNAL   PLoS One 7 (2), e31961 (2012)
   PUBMED   22363774
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011462.4.
            
            Transcript Variant: This variant (8), as well as variants 3 and 6,
            encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.579144.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..133
                     /product="transmembrane protein 91 isoform c"
                     /note="interferon induced transmembrane protein domain
                     containing 6; dispanin subfamily C member 3"
                     /calculated_mol_wt=14286
     Region          92..>124
                     /region_name="CD225"
                     /note="Interferon-induced transmembrane protein;
                     pfam04505"
                     /db_xref="CDD:461336"
     CDS             1..133
                     /gene="TMEM91"
                     /gene_synonym="DSPC3; IFITMD6; SynDIG3"
                     /coded_by="NM_001369864.1:436..837"
                     /note="isoform c is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS46082.1"
                     /db_xref="GeneID:641649"
                     /db_xref="HGNC:HGNC:32393"
                     /db_xref="MIM:618294"
ORIGIN      
        1 mdspslrelq qpllegtece tpaqkpgrhe lgsplreiaf aeslrglqfl spplpsvsag
       61 lgeprppdve dmsssdsdsd wdggsrlspf lphdhlglav fsmlccfwpv giaafclaqk
      121 trpscpysph cep
//
LOCUS       NP_001355304             155 aa            linear   ROD 27-APR-2025
DEFINITION  RING finger protein 122 isoform 3 [Mus musculus].
ACCESSION   NP_001355304 XP_006509253
VERSION     NP_001355304.1
DBSOURCE    REFSEQ: accession NM_001368375.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Wang,W., Jiang,M., Liu,S., Zhang,S., Liu,W., Ma,Y., Zhang,L.,
            Zhang,J. and Cao,X.
  TITLE     RNF122 suppresses antiviral type I interferon production by
            targeting RIG-I CARDs to mediate RIG-I degradation
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9581-9586 (2016)
   PUBMED   27506794
  REMARK    GeneRIF: RNF122 suppresses antiviral type I interferon production
            by targeting RIG-I caspase activation and recruitment domains to
            mediate RIG-I degradation.
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC109163.16.
            
            On Feb 8, 2019 this sequence version replaced XP_006509253.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK171823.1, AK077856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 17.97 cM"
     Protein         1..155
                     /product="RING finger protein 122 isoform 3"
                     /note="ring finger protein 122 homolog"
                     /calculated_mol_wt=17317
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BP31.1)"
     Region          91..137
                     /region_name="RING-H2_RNF122"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 122 (RNF122) and similar proteins; cd16676"
                     /db_xref="CDD:438338"
     Site            order(93,96,111,113,116,119,130,133)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:438338"
     CDS             1..155
                     /gene="Rnf122"
                     /gene_synonym="1110063C11Rik"
                     /coded_by="NM_001368375.1:322..789"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS90381.1"
                     /db_xref="GeneID:68867"
                     /db_xref="MGI:MGI:1916117"
ORIGIN      
        1 mhpfqwcngc fcglglvstn kscsmppisf qdlplniymv ifgtgifvfm lslifccyfi
       61 sklrnqaqse rygykevvlk gdakklqlyg qtcavcledf kgkdelgvlp cqhafhrkcl
      121 vkwlevrcvc pmcnkpiagp tetsqsigil ldelv
//
LOCUS       NP_950189                483 aa            linear   ROD 27-APR-2025
DEFINITION  nucleolar protein 4 isoform 2 [Mus musculus].
ACCESSION   NP_950189 XP_283513
VERSION     NP_950189.2
DBSOURCE    REFSEQ: accession NM_199024.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Toor,S.M., Wani,S. and Albagha,O.M.E.
  TITLE     Comprehensive Transcriptomic Profiling of Murine Osteoclast
            Differentiation Reveals Novel Differentially Expressed Genes and
            LncRNAs
  JOURNAL   Front Genet 12, 781272 (2021)
   PUBMED   34868271
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Takayanagi-Kiya,S., Misawa-Hojo,K., Kiya,T., Kunieda,T. and Kubo,T.
  TITLE     Splicing variants of NOL4 differentially regulate the transcription
            activity of Mlr1 and Mlr2 in cultured cells
  JOURNAL   Zoolog Sci 31 (11), 735-740 (2014)
   PUBMED   25366156
  REMARK    GeneRIF: These findings suggest that transactivation activities of
            Mlr1 and Mlr2 are differentially regulated by splicing variants of
            NOL4, which are expressed in a tissue-selective manner.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC102361.13, AC131338.4 and AC103368.7.
            
            On Jun 3, 2009 this sequence version replaced NP_950189.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, and uses an alternate splice
            site in the 3' coding region that causes a frameshift, compared to
            variant 1. The resulting isoform (2) has a distinct C-terminus and
            is shorter than isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK031008.1, SRR7652917.526343.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 11.96 cM"
     Protein         1..483
                     /product="nucleolar protein 4 isoform 2"
                     /calculated_mol_wt=53348
     Region          110..164
                     /region_name="Integrase_H2C2"
                     /note="Integrase zinc binding domain; pfam17921"
                     /db_xref="CDD:465569"
     Region          <208..369
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          210..418
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60954.2)"
     Region          435..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60954.2)"
     CDS             1..483
                     /gene="Nol4"
                     /gene_synonym="1700013J13Rik; 4930568N03Rik; Gm1262"
                     /coded_by="NM_199024.3:1640..3091"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS29093.2"
                     /db_xref="GeneID:319211"
                     /db_xref="MGI:MGI:2441684"
ORIGIN      
        1 meserdmyrq fqdwclrtyg dsgktktvtr kkyerivqll ngsessstdn akfkfwvksk
       61 gfqlgqpdev rgggggakqv lfvrvkttdg vgvdeklslr rvavvedffd iiysmhvetg
      121 pngeqirkha gqkrtykais esyaflprea vtrflmscse cqkrmhlnpd gtdhkdngkp
      181 ptlvtsmidy nmpitmaymk hmklqllnsq qdedessies defdmsdstr msavnsdlss
      241 nleermqspq tvhgqqddds aaessngnet lghssaasgg ahgrepedss sdgktgleqe
      301 eqplnlsdsp ssaqltsefr iddqgsdgkn kyknllisdl kmereareng skspahsyss
      361 ydsgknesvd rgaedlslnr gdededehde hedsekvnet dgveaerlka fnsrpipshl
      421 tsavaesila sacesesrna akrmrldkaq deaapadkqc kpeaaqatys tatvpgsqed
      481 pqi
//
LOCUS       NP_999680                260 aa            linear   INV 27-APR-2025
DEFINITION  33 kDa inner dynein arm light chain, axonemal [Strongylocentrotus
            purpuratus].
ACCESSION   NP_999680 XP_003723881 XP_011672631
VERSION     NP_999680.1
DBSOURCE    REFSEQ: accession NM_214515.2
KEYWORDS    RefSeq.
SOURCE      Strongylocentrotus purpuratus (purple sea urchin)
  ORGANISM  Strongylocentrotus purpuratus
            Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa;
            Echinoidea; Euechinoidea; Echinacea; Camarodonta; Echinidea;
            Strongylocentrotidae; Strongylocentrotus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Tu,Q., Cameron,R.A., Worley,K.C., Gibbs,R.A. and Davidson,E.H.
  TITLE     Gene structure in the sea urchin Strongylocentrotus purpuratus
            based on transcriptome analysis
  JOURNAL   Genome Res 22 (10), 2079-2087 (2012)
   PUBMED   22709795
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Gingras,D., White,D., Garin,J., Multigner,L., Job,D., Cosson,J.,
            Huitorel,P., Zingg,H., Dumas,F. and Gagnon,C.
  TITLE     Purification, cloning, and sequence analysis of a Mr = 30,000
            protein from sea urchin axonemes that is important for sperm
            motility. Relationship of the protein to a dynein light chain
  JOURNAL   J Biol Chem 271 (22), 12807-12813 (1996)
   PUBMED   8662724
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JT099654.1.
            
            On or before Apr 5, 2015 this sequence version replaced
            XP_011672631.1, XP_003723881.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JT099654.1, U47278.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMN01096960, SAMN01103178
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Strongylocentrotus purpuratus"
                     /db_xref="taxon:7668"
     Protein         1..260
                     /product="33 kDa inner dynein arm light chain, axonemal"
                     /note="p33; axonemal dynein light chain p33"
                     /calculated_mol_wt=29601
     Region          1..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q26630.1)"
     Region          67..253
                     /region_name="Ax_dynein_light"
                     /note="Axonemal dynein light chain; pfam10211"
                     /db_xref="CDD:463000"
     CDS             1..260
                     /gene="dnali1"
                     /coded_by="NM_214515.2:194..976"
                     /db_xref="EchinoBase:ECB-GENE-23175513"
                     /db_xref="GeneID:373273"
ORIGIN      
        1 mippnaslvk ydnpvlvsrn tekktprara lktspqqptn agpvpnpppk ggsklppves
       61 qkaqqtdeil nsilpprewt esgqlwvqqv sstpatrldv vnlqeqldmr lqqrqaretg
      121 icpvrrelys qcfdelirqv tiecaergll llrvrdeirm tiaayqtlye ssvafgmrka
      181 lqaeqgksdm ekkitdlgqe krelerqvne lkakceaiek reaerrqvee kkhaeeiqfl
      241 krtnqqlktq legiiapnkk
//
LOCUS       NP_037542                223 aa            linear   PRI 27-APR-2025
DEFINITION  adenylate kinase 4, mitochondrial isoform a [Homo sapiens].
ACCESSION   NP_037542 NP_001002921
VERSION     NP_037542.1
DBSOURCE    REFSEQ: accession NM_013410.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Wujak,M., Veith,C., Wu,C.Y., Wilke,T., Kanbagli,Z.I.,
            Novoyatleva,T., Guenther,A., Seeger,W., Grimminger,F., Sommer,N.,
            Schermuly,R.T. and Weissmann,N.
  TITLE     Adenylate Kinase 4-A Key Regulator of Proliferation and Metabolic
            Shift in Human Pulmonary Arterial Smooth Muscle Cells via Akt and
            HIF-1alpha Signaling Pathways
  JOURNAL   Int J Mol Sci 22 (19), 10371 (2021)
   PUBMED   34638712
  REMARK    GeneRIF: Adenylate Kinase 4-A Key Regulator of Proliferation and
            Metabolic Shift in Human Pulmonary Arterial Smooth Muscle Cells via
            Akt and HIF-1alpha Signaling Pathways.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Tan,H., Wu,C., Huang,B., Jin,L. and Jiang,X.
  TITLE     MiR-3666 serves as a tumor suppressor in ovarian carcinoma by
            down-regulating AK4 via targeting STAT3
  JOURNAL   Cancer Biomark 30 (4), 355-363 (2021)
   PUBMED   33361582
  REMARK    GeneRIF: MiR-3666 serves as a tumor suppressor in ovarian carcinoma
            by down-regulating AK4 via targeting STAT3.
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Panayiotou,C., Solaroli,N., Johansson,M. and Karlsson,A.
  TITLE     Evidence of an intact N-terminal translocation sequence of human
            mitochondrial adenylate kinase 4
  JOURNAL   Int J Biochem Cell Biol 42 (1), 62-69 (2010)
   PUBMED   19766732
  REMARK    GeneRIF: The AK4 cDNA was expressed in Escherichia coli and the
            substrate specificity and kinetic properties of the recombinant
            protein were characterized.
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Liu,R., Xu,H., Wei,Z., Wang,Y., Lin,Y. and Gong,W.
  TITLE     Crystal structure of human adenylate kinase 4 (L171P) suggests the
            role of hinge region in protein domain motion
  JOURNAL   Biochem Biophys Res Commun 379 (1), 92-97 (2009)
   PUBMED   19073142
  REMARK    GeneRIF: To investigate the role of hinge IV, crystal structure of
            human adenylate kinase 4 (AK4) L171P mutant was determined.
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Noma,T., Adachi,N. and Nakazawa,A.
  TITLE     Cloning and functional characterization of the promoter region of
            the gene encoding human adenylate kinase isozyme 3
  JOURNAL   Biochem Biophys Res Commun 264 (3), 990-997 (1999)
   PUBMED   10544043
REFERENCE   7  (residues 1 to 223)
  AUTHORS   Yoneda,T., Sato,M., Maeda,M. and Takagi,H.
  TITLE     Identification of a novel adenylate kinase system in the brain:
            cloning of the fourth adenylate kinase
  JOURNAL   Brain Res Mol Brain Res 62 (2), 187-195 (1998)
   PUBMED   9813319
REFERENCE   8  (residues 1 to 223)
  AUTHORS   Xu,G., O'Connell,P., Stevens,J. and White,R.
  TITLE     Characterization of human adenylate kinase 3 (AK3) cDNA and mapping
            of the AK3 pseudogene to an intron of the NF1 gene
  JOURNAL   Genomics 13 (3), 537-542 (1992)
   PUBMED   1639383
REFERENCE   9  (residues 1 to 223)
  AUTHORS   Robson,E.B. and Meera Khan,P.
  TITLE     Report of the committee on the genetic constitution of chromosomes
            7, 8, and 9. Oslo Conference (1981): Sixth International Workshop
            on Human Gene Mapping
  JOURNAL   Cytogenet Cell Genet 32 (1-4), 144-152 (1982)
   PUBMED   7140357
REFERENCE   10 (residues 1 to 223)
  AUTHORS   Povey,S., Slaughter,C.A., Wilson,D.E., Gormley,I.P., Buckton,K.E.,
            Perry,P. and Bobrow,M.
  TITLE     Evidence for the assignment of the loci AK1, AK3 and ACONs to
            chromosome 9 in man
  JOURNAL   Ann Hum Genet 39 (4), 413-422 (1976)
   PUBMED   182062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB061266.1, BC040224.1 and
            AL356212.13.
            
            On Jan 18, 2008 this sequence version replaced NP_001002921.1.
            
            Summary: This gene encodes a member of the adenylate kinase family
            of enzymes. The encoded protein is localized to the mitochondrial
            matrix. Adenylate kinases regulate the adenine and guanine
            nucleotide compositions within a cell by catalyzing the reversible
            transfer of phosphate group among these nucleotides. Five isozymes
            of adenylate kinase have been identified in vertebrates. Expression
            of these isozymes is tissue-specific and developmentally regulated.
            A pseudogene for this gene has been located on chromosome 17. Three
            transcript variants encoding the same protein have been identified
            for this gene. Sequence alignment suggests that the gene defined by
            NM_013410, NM_203464, and NM_001005353 is located on chromosome 1.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 all encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK025926.1, SRR1660809.187659.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000327299.8/
                                                  ENSP00000322175.7
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..223
                     /product="adenylate kinase 4, mitochondrial isoform a"
                     /EC_number="2.7.4.6"
                     /EC_number="2.7.4.4"
                     /note="adenylate kinase 3-like 1;
                     nucleoside-triphosphate-adenylate kinase; ATP-AMP
                     transphosphorylase; mitochondrial adenylate kinase-3;
                     adenylate kinase isoenzyme 4, mitochondrial; GTP:AMP
                     phosphotransferase AK4, mitochondrial; adenylate kinase 4,
                     mitochondrial; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=25137
     Region          10..188
                     /region_name="ADK"
                     /note="Adenylate kinase; pfam00406"
                     /db_xref="CDD:395329"
     Region          35..64
                     /region_name="NMP.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03170,
                     ECO:0000269|PubMed:19073142"
                     /note="propagated from UniProtKB/Swiss-Prot (P27144.1)"
     Region          125..162
                     /region_name="LID.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03170,
                     ECO:0000269|PubMed:19073142"
                     /note="propagated from UniProtKB/Swiss-Prot (P27144.1)"
     Site            175
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUR9; propagated from
                     UniProtKB/Swiss-Prot (P27144.1)"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9WUR9; propagated from
                     UniProtKB/Swiss-Prot (P27144.1)"
     Site            186
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9WUR9; propagated from
                     UniProtKB/Swiss-Prot (P27144.1)"
     CDS             1..223
                     /gene="AK4"
                     /gene_synonym="AK 4; AK3; AK3L1; AK3L2"
                     /coded_by="NM_013410.4:206..877"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS629.1"
                     /db_xref="GeneID:205"
                     /db_xref="HGNC:HGNC:363"
                     /db_xref="MIM:103030"
ORIGIN      
        1 maskllravi lgppgsgkgt vcqriaqnfg lqhlssghfl renikastev gemakqyiek
       61 sllvpdhvit rlmmselenr rgqhwlldgf prtlgqaeal dkicevdlvi slnipfetlk
      121 drlsrrwihp psgrvynldf npphvhgidd vtgeplvqqe ddkpeavaar lrqykdvakp
      181 vielyksrgv lhqfsgtetn kiwpyvytlf snkitpiqsk eay
//
LOCUS       NP_872634                699 aa            linear   PRI 27-APR-2025
DEFINITION  SRSF protein kinase 2 isoform a [Homo sapiens].
ACCESSION   NP_872634
VERSION     NP_872634.1
DBSOURCE    REFSEQ: accession NM_182692.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Yip,R.P.H., Kwok,D.C.Y., Lai,L.T.F., Ho,S.M., Wong,I.C.K.,
            Chan,C.P., Lau,W.C.Y. and Ngo,J.C.K.
  TITLE     SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid Assembly
            via Docking Interaction
  JOURNAL   PLoS Pathog 20 (2), e1011978 (2024)
   PUBMED   38324561
  REMARK    GeneRIF: SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid
            Assembly via Docking Interaction.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Yang,Z. and Ding,W.X.
  TITLE     The pre-mRNA alternative splicing regulated by SRPK2: A new player
            in alcohol-associated liver disease?
  JOURNAL   Hepatology 78 (5), 1329-1331 (2023)
   PUBMED   37183907
  REMARK    GeneRIF: The pre-mRNA alternative splicing regulated by SRPK2: A
            new player in alcohol-associated liver disease?
REFERENCE   4  (residues 1 to 699)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 699)
  AUTHORS   Fonteneau,G., Redding,A., Hoag-Lee,H., Sim,E.S., Heinrich,S.,
            Gaida,M.M. and Grabocka,E.
  TITLE     Stress Granules Determine the Development of Obesity-Associated
            Pancreatic Cancer
  JOURNAL   Cancer Discov 12 (8), 1984-2005 (2022)
   PUBMED   35674408
  REMARK    GeneRIF: Stress Granules Determine the Development of
            Obesity-Associated Pancreatic Cancer.
REFERENCE   6  (residues 1 to 699)
  AUTHORS   Koizumi,J., Okamoto,Y., Onogi,H., Mayeda,A., Krainer,A.R. and
            Hagiwara,M.
  TITLE     The subcellular localization of SF2/ASF is regulated by direct
            interaction with SR protein kinases (SRPKs)
  JOURNAL   J Biol Chem 274 (16), 11125-11131 (1999)
   PUBMED   10196197
REFERENCE   7  (residues 1 to 699)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
REFERENCE   8  (residues 1 to 699)
  AUTHORS   Kuroyanagi,N., Onogi,H., Wakabayashi,T. and Hagiwara,M.
  TITLE     Novel SR-protein-specific kinase, SRPK2, disassembles nuclear
            speckles
  JOURNAL   Biochem Biophys Res Commun 242 (2), 357-364 (1998)
   PUBMED   9446799
REFERENCE   9  (residues 1 to 699)
  AUTHORS   Bedford,M.T., Chan,D.C. and Leder,P.
  TITLE     FBP WW domains and the Abl SH3 domain bind to a specific class of
            proline-rich ligands
  JOURNAL   EMBO J 16 (9), 2376-2383 (1997)
   PUBMED   9171351
REFERENCE   10 (residues 1 to 699)
  AUTHORS   Gui,J.F., Lane,W.S. and Fu,X.D.
  TITLE     A serine kinase regulates intracellular localization of splicing
            factors in the cell cycle
  JOURNAL   Nature 369 (6482), 678-682 (1994)
   PUBMED   8208298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY031357.1, BC035214.1, CR746049.1 and BU632662.1.
            
            Transcript Variant: This variant (1) encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.145225.1,
                                           SRR1803613.111629.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393651.8/ ENSP00000377262.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..699
                     /product="SRSF protein kinase 2 isoform a"
                     /EC_number="2.7.11.1"
                     /note="SFRS protein kinase 2; serine/arginine-rich
                     splicing factor kinase 2; SR protein kinase 2;
                     serine/threonine-protein kinase SRPK2; serine kinase
                     SRPK2; SR-protein-specific kinase 2; serine/arginine-rich
                     protein-specific kinase 2"
                     /calculated_mol_wt=78898
     Region          79..>267
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(98..101,104,106,119,121,157,177..180,225,229..230,
                     232)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          <352..394
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          <515..697
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..699
                     /gene="SRPK2"
                     /gene_synonym="SFRSK2"
                     /coded_by="NM_182692.3:116..2215"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34724.1"
                     /db_xref="GeneID:6733"
                     /db_xref="HGNC:HGNC:11306"
                     /db_xref="MIM:602980"
ORIGIN      
        1 mssrkvlaiq arkrrpkrek hpkkpepqqk aplvpppppp ppppppplpd ptppepeeei
       61 lgsddeeqed padyckggyh pvkigdlfng ryhvirklgw ghfstvwlcw dmqgkrfvam
      121 kvvksaqhyt etaldeikll kcvresdpsd pnkdmvvqli ddfkisgmng ihvcmvfevl
      181 ghhllkwiik snyqglpvrc vksiirqvlq gldylhskck iihtdikpen ilmcvddayv
      241 rrmaaeatew qkagapppsg savstapqqk pigkisknkk kklkkkqkrq aellekrlqe
      301 ieelereaer kiieenitsa apsndqdgey cpevklkttg leeaaeaeta kdngeaedqe
      361 ekedaekeni ekdeddvdqe lanidptwie spktnghien gpfsleqqld dedddeedcp
      421 npeeynldep naesdytyss syeqfngelp ngrhkipesq fpefstslfs gslepvacgs
      481 vlsegsplte qeesspshdr srtvsasstg dlpkaktraa dllvnpldpr nadkirvkia
      541 dlgnacwvhk hftediqtrq yrsievliga gystpadiws tacmafelat gdylfephsg
      601 edysrdedhi ahiiellgsi prhfalsgky sreffnrrge lrhitklkpw slfdvlveky
      661 gwphedaaqf tdflipmlem vpekrasage clrhpwlns
//
LOCUS       NP_001662                291 aa            linear   PRI 27-APR-2025
DEFINITION  asialoglycoprotein receptor 1 isoform a [Homo sapiens].
ACCESSION   NP_001662
VERSION     NP_001662.1
DBSOURCE    REFSEQ: accession NM_001671.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Zhang,Z., Leng,X.K., Zhai,Y.Y., Zhang,X., Sun,Z.W., Xiao,J.Y.,
            Lu,J.F., Liu,K., Xia,B., Gao,Q., Jia,M., Xu,C.Q., Jiang,Y.N.,
            Zhang,X.G., Tao,K.S. and Wu,J.W.
  TITLE     Deficiency of ASGR1 promotes liver injury by increasing
            GP73-mediated hepatic endoplasmic reticulum stress
  JOURNAL   Nat Commun 15 (1), 1908 (2024)
   PUBMED   38459023
  REMARK    GeneRIF: Deficiency of ASGR1 promotes liver injury by increasing
            GP73-mediated hepatic endoplasmic reticulum stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Yang,X., Zheng,X., Zhu,Y., Zhao,X., Liu,J., Xun,J., Yuan,S.,
            Chen,J., Pan,H., Yang,J., Wang,J., Liang,Z., Shen,X., Liang,Y.,
            Lin,Q., Liang,H., Li,M., Peng,F., Lu,D., Xu,J., Lu,H., Jiang,S.,
            Zhao,P. and Zhu,H.
  TITLE     Asialoglycoprotein receptor 1 promotes SARS-CoV-2 infection of
            human normal hepatocytes
  JOURNAL   Signal Transduct Target Ther 9 (1), 42 (2024)
   PUBMED   38355848
  REMARK    GeneRIF: Asialoglycoprotein receptor 1 promotes SARS-CoV-2
            infection of human normal hepatocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Hoffmann,M. and Pohlmann,S.
  TITLE     Novel SARS-CoV-2 receptors: ASGR1 and KREMEN1
  JOURNAL   Cell Res 32 (1), 1-2 (2022)
   PUBMED   34903854
  REMARK    GeneRIF: Novel SARS-CoV-2 receptors: ASGR1 and KREMEN1.
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Hu,B., Yang,Y., Liu,J., Ma,Z., Huang,H., Liu,S., Yu,Y., Hao,Y.,
            Wang,B., Lu,M. and Yang,D.
  TITLE     Establishment of a functional cell line expressing both subunits of
            H1a and H2c of human hepatocyte surface molecule ASGPR
  JOURNAL   J Huazhong Univ Sci Technolog Med Sci 30 (5), 556-561 (2010)
   PUBMED   21063834
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Liu,J., Hu,B., Yang,Y., Ma,Z., Yu,Y., Liu,S., Wang,B., Zhao,X.,
            Lu,M. and Yang,D.
  TITLE     A new splice variant of the major subunit of human
            asialoglycoprotein receptor encodes a secreted form in hepatocytes
  JOURNAL   PLoS One 5 (9), e12934 (2010)
   PUBMED   20886072
  REMARK    GeneRIF: Two naturally occurring ASGPR1 splice variants are
            produced in human hepatocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Beltzer,J.P. and Spiess,M.
  TITLE     In vitro binding of the asialoglycoprotein receptor to the beta
            adaptin of plasma membrane coated vesicles
  JOURNAL   EMBO J 10 (12), 3735-3742 (1991)
   PUBMED   1935897
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Sanford,J.P., Eddy,R.L., Doyle,D. and Shows,T.B.
  TITLE     Assignment of human asialoglycoprotein receptor gene (ASGR1) to
            chromosome 17p11-13
  JOURNAL   Genomics 11 (3), 779-781 (1991)
   PUBMED   1774077
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Geffen,I., Fuhrer,C. and Spiess,M.
  TITLE     Endocytosis by the asialoglycoprotein receptor is independent of
            cytoplasmic serine residues
  JOURNAL   Proc Natl Acad Sci U S A 88 (19), 8425-8429 (1991)
   PUBMED   1924301
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Bischoff,J., Libresco,S., Shia,M.A. and Lodish,H.F.
  TITLE     The H1 and H2 polypeptides associate to form the asialoglycoprotein
            receptor in human hepatoma cells
  JOURNAL   J Cell Biol 106 (4), 1067-1074 (1988)
   PUBMED   2834401
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Spiess,M., Schwartz,A.L. and Lodish,H.F.
  TITLE     Sequence of human asialoglycoprotein receptor cDNA. An internal
            signal sequence for membrane insertion
  JOURNAL   J Biol Chem 260 (4), 1979-1982 (1985)
   PUBMED   2982798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ653541.1 and BC032130.2.
            
            Summary: This gene encodes a subunit of the asialoglycoprotein
            receptor. This receptor is a transmembrane protein that plays a
            critical role in serum glycoprotein homeostasis by mediating the
            endocytosis and lysosomal degradation of glycoproteins with exposed
            terminal galactose or N-acetylgalactosamine residues. The
            asialoglycoprotein receptor may facilitate hepatic infection by
            multiple viruses including hepatitis B, and is also a target for
            liver-specific drug delivery. The asialoglycoprotein receptor is a
            hetero-oligomeric protein composed of major and minor subunits,
            which are encoded by different genes. The protein encoded by this
            gene is the more abundant major subunit. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1), also known as H1a, represents
            the longer transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.50537.1,
                                           SRR5189664.118868.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in SARS-CoV-2 infection
            MANE Ensembl match     :: ENST00000269299.8/ ENSP00000269299.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..291
                     /product="asialoglycoprotein receptor 1 isoform a"
                     /note="hepatic lectin H1; C-type lectin domain family 4
                     member H1"
                     /calculated_mol_wt=33055
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07306.2)"
     Region          4..144
                     /region_name="Lectin_N"
                     /note="Hepatic lectin, N-terminal domain; pfam03954"
                     /db_xref="CDD:461106"
     Region          5..8
                     /region_name="Endocytosis signal. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P07306.2)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P07306.2)"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07306.2)"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P07306.2)"
     Site            147
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P07306.2)"
     Region          154..279
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Site            order(209,240,242,253,259,265..268)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(216,243,253..254)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P07306.2)"
     CDS             1..291
                     /gene="ASGR1"
                     /gene_synonym="ASGPR; ASGPR1; CLEC4H1; HL-1"
                     /coded_by="NM_001671.5:207..1082"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11089.1"
                     /db_xref="GeneID:432"
                     /db_xref="HGNC:HGNC:742"
                     /db_xref="MIM:108360"
ORIGIN      
        1 mtkeyqdlqh ldneesdhhq lrkgppppqp llqrlcsgpr llllslglsl lllvvvcvig
       61 sqnsqlqeel rglretfsnf tasteaqvkg lstqggnvgr kmkslesqle kqqkdlsedh
      121 sslllhvkqf vsdlrslscq maalqgngse rtccpvnwve herscywfsr sgkawadadn
      181 ycrledahlv vvtsweeqkf vqhhigpvnt wmglhdqngp wkwvdgtdye tgfknwrpeq
      241 pddwyghglg ggedcahftd dgrwnddvcq rpyrwvcete ldkasqeppl l
//
LOCUS       NP_037507                272 aa            linear   PRI 27-APR-2025
DEFINITION  activator of basal transcription 1 [Homo sapiens].
ACCESSION   NP_037507
VERSION     NP_037507.1
DBSOURCE    REFSEQ: accession NM_013375.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Oda,T., Kayukawa,K., Hagiwara,H., Yudate,H.T., Masuho,Y.,
            Murakami,Y., Tamura,T.A. and Muramatsu,M.A.
  TITLE     A novel TATA-binding protein-binding protein, ABT1, activates basal
            transcription and has a yeast homolog that is essential for growth
  JOURNAL   Mol Cell Biol 20 (4), 1407-1418 (2000)
   PUBMED   10648625
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513548.8.
            
            Summary: Basal transcription of genes by RNA polymerase II requires
            the interaction of TATA-binding protein (TBP) with the core region
            of class II promoters.  Studies in mouse suggest that the protein
            encoded by this gene likely activates basal transcription from
            class II promoters by interaction with TBP and the class II
            promoter DNA. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.268146.1,
                                           SRR1803612.188604.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274849.3/ ENSP00000274849.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.2"
     Protein         1..272
                     /product="activator of basal transcription 1"
                     /note="basal transcriptional activator; TATA-binding
                     protein-binding protein"
                     /calculated_mol_wt=30948
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULW3.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9ULW3.1)"
     Region          46..149
                     /region_name="RRM_ABT1_like"
                     /note="RNA recognition motif (RRM) found in activator of
                     basal transcription 1 (ABT1) and similar proteins;
                     cd12263"
                     /db_xref="CDD:409707"
     Region          198..272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULW3.1)"
     CDS             1..272
                     /gene="ABT1"
                     /gene_synonym="Esf2; hABT1"
                     /coded_by="NM_013375.4:31..849"
                     /db_xref="CCDS:CCDS4616.1"
                     /db_xref="GeneID:29777"
                     /db_xref="HGNC:HGNC:17369"
                     /db_xref="MIM:618750"
ORIGIN      
        1 meaeesekaa teqeplegte qtldaeeeqe eseeaacgsk krvvpgivyl ghipprfrpl
       61 hvrnllsayg evgrvffqae drfvrrkkka aaaaggkkrs ytkdytegwv efrdkriakr
      121 vaaslhntpm garrrspfry dlwnlkylhr ftwshlsehl aferqvrrqr lraevaqakr
      181 etdfylqsve rgqrflaadg dparpdgswt faqrpteqel rarkaarpgg rerarlataq
      241 dkarsnkgll arifgappps esmegpslvr ds
//
LOCUS       NP_001351333             449 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger CCCH domain-containing protein 14 isoform i [Mus
            musculus].
ACCESSION   NP_001351333 XP_017170724
VERSION     NP_001351333.1
DBSOURCE    REFSEQ: accession NM_001364404.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Li,Q., Yang,G., Ren,B., Liu,X., Tang,L.Q., Shi,Q., Shan,G. and
            Wang,X.
  TITLE     ZC3H14 facilitates backsplicing by binding to exon-intron boundary
            and 3' UTR
  JOURNAL   Mol Cell 84 (22), 4314-4333 (2024)
   PUBMED   39461343
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Corgiat,E.B., List,S.M., Rounds,J.C., Corbett,A.H. and Moberg,K.H.
  TITLE     The RNA-binding protein Nab2 regulates the proteome of the
            developing Drosophila brain
  JOURNAL   J Biol Chem 297 (1), 100877 (2021)
   PUBMED   34139237
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Wheeler,J.M., McMillan,P., Strovas,T.J., Liachko,N.F.,
            Amlie-Wolf,A., Kow,R.L., Klein,R.L., Szot,P., Robinson,L.,
            Guthrie,C., Saxton,A., Kanaan,N.M., Raskind,M., Peskind,E.,
            Trojanowski,J.Q., Lee,V.M.Y., Wang,L.S., Keene,C.D., Bird,T.,
            Schellenberg,G.D. and Kraemer,B.
  TITLE     Activity of the poly(A) binding protein MSUT2 determines
            susceptibility to pathological tau in the mammalian brain
  JOURNAL   Sci Transl Med 11 (523) (2019)
   PUBMED   31852801
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Rha,J., Jones,S.K., Fidler,J., Banerjee,A., Leung,S.W.,
            Morris,K.J., Wong,J.C., Inglis,G.A.S., Shapiro,L., Deng,Q.,
            Cutler,A.A., Hanif,A.M., Pardue,M.T., Schaffer,A., Seyfried,N.T.,
            Moberg,K.H., Bassell,G.J., Escayg,A., Garcia,P.S. and Corbett,A.H.
  TITLE     The RNA-binding protein, ZC3H14, is required for proper poly(A)
            tail length control, expression of synaptic proteins, and brain
            function in mice
  JOURNAL   Hum Mol Genet 26 (19), 3663-3681 (2017)
   PUBMED   28666327
  REMARK    GeneRIF: Among the proteins increased in the hippocampi of
            Zc3h14Deltaex13/Deltaex13 mice compared to control are key synaptic
            proteins including CaMK2a. This newly generated mouse serves as a
            tool to study the function of ZC3H14 in vivo.
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Watanabe,K., Takebayashi,H., Bepari,A.K., Esumi,S., Yanagawa,Y. and
            Tamamaki,N.
  TITLE     Dpy19l1, a multi-transmembrane protein, regulates the radial
            migration of glutamatergic neurons in the developing cerebral
            cortex
  JOURNAL   Development 138 (22), 4979-4990 (2011)
   PUBMED   22028030
  REMARK    Erratum:[Development. 2012 Mar;139(6):1225]
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Pak,C., Garshasbi,M., Kahrizi,K., Gross,C., Apponi,L.H., Noto,J.J.,
            Kelly,S.M., Leung,S.W., Tzschach,A., Behjati,F., Abedini,S.S.,
            Mohseni,M., Jensen,L.R., Hu,H., Huang,B., Stahley,S.N., Liu,G.,
            Williams,K.R., Burdick,S., Feng,Y., Sanyal,S., Bassell,G.J.,
            Ropers,H.H., Najmabadi,H., Corbett,A.H., Moberg,K.H. and Kuss,A.W.
  TITLE     Mutation of the conserved polyadenosine RNA binding protein,
            ZC3H14/dNab2, impairs neural function in Drosophila and humans
  JOURNAL   Proc Natl Acad Sci U S A 108 (30), 12390-12395 (2011)
   PUBMED   21734151
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Leung,S.W., Apponi,L.H., Cornejo,O.E., Kitchen,C.M.,
            Valentini,S.R., Pavlath,G.K., Dunham,C.M. and Corbett,A.H.
  TITLE     Splice variants of the human ZC3H14 gene generate multiple isoforms
            of a zinc finger polyadenosine RNA binding protein
  JOURNAL   Gene 439 (1-2), 71-78 (2009)
   PUBMED   19303045
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC159193.2.
            
            On Jun 15, 2018 this sequence version replaced XP_017170724.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.42528.1,
                                           SRR7345562.3416346.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 49.88 cM"
     Protein         1..449
                     /product="zinc finger CCCH domain-containing protein 14
                     isoform i"
                     /note="zinc finger CCCH domain-containing protein 14"
                     /calculated_mol_wt=50428
     Region          315..332
                     /region_name="zf-CCCH_2"
                     /note="RNA-binding, Nab2-type zinc finger; pfam14608"
                     /db_xref="CDD:464217"
     Region          335..353
                     /region_name="zf-CCCH_2"
                     /note="RNA-binding, Nab2-type zinc finger; pfam14608"
                     /db_xref="CDD:464217"
     CDS             1..449
                     /gene="Zc3h14"
                     /gene_synonym="1010001P15Rik; 1700016A15Rik;
                     2700069A02Rik"
                     /coded_by="NM_001364404.1:506..1855"
                     /note="isoform i is encoded by transcript variant 10"
                     /db_xref="GeneID:75553"
                     /db_xref="MGI:MGI:1919824"
ORIGIN      
        1 mstvkplrep apsedvidik pepddlided lnfvqenpls qkkptvtlty gssrpsieiy
       61 rppasrnadt gthlnrlqlh pqqssahaak qldvqssqvs eagrlceppv lssvedtysp
      121 ffrnnldkms iedenfrkrk lpvvssvvkv krfshdgeee eededygtri gslsssvsvp
      181 akperrpslp pskqanknli lkaiseaqes vtkttnysav pqkqtlpvap rtrtsqeell
      241 aemvqgqnra prisppvkee eakgdntgks qgtqqrqlls rlqidpvmve tmemsqaemt
      301 dlsvaqkpek llerckywpa ckngdecvyh hpispckafp nckfaekclf vhpnckydtk
      361 ctkadcpfth msrrasiltp kpvsspapss ngqlcryfpa ckkmecpfyh pkhcrfntqc
      421 trpdctfyhp titvpprhal kwirpqsse
//
LOCUS       NP_003738               1327 aa            linear   PRI 27-APR-2025
DEFINITION  poly [ADP-ribose] polymerase tankyrase-1 [Homo sapiens].
ACCESSION   NP_003738
VERSION     NP_003738.2
DBSOURCE    REFSEQ: accession NM_003747.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1327)
  AUTHORS   Morino,S., Mashima,T., Shirai,F., Nagayama,S., Katayama,R. and
            Seimiya,H.
  TITLE     BET protein-dependent E2F pathway activity confers bell-shaped type
            resistance to tankyrase inhibitors in APC-mutated colorectal cancer
  JOURNAL   Cancer Lett 584, 216632 (2024)
   PUBMED   38216082
  REMARK    GeneRIF: BET protein-dependent E2F pathway activity confers
            bell-shaped type resistance to tankyrase inhibitors in APC-mutated
            colorectal cancer.
REFERENCE   2  (residues 1 to 1327)
  AUTHORS   Ma,N., Wibowo,Y.C., Wirtz,P., Baltus,D., Wieland,T. and Jansen,S.
  TITLE     Tankyrase inhibition interferes with junction remodeling, induces
            leakiness, and disturbs YAP1/TAZ signaling in the endothelium
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 397 (3), 1763-1789 (2024)
   PUBMED   37741944
  REMARK    GeneRIF: Tankyrase inhibition interferes with junction remodeling,
            induces leakiness, and disturbs YAP1/TAZ signaling in the
            endothelium.
REFERENCE   3  (residues 1 to 1327)
  AUTHORS   Duan,X., Huang,T., Zhang,D., Wei,Y., Li,L., Yao,W., Cui,L.,
            Zhou,X., Yang,Y., Wang,W. and Zhao,J.
  TITLE     Effect and interaction of TNKS genetic polymorphisms and
            environmental factors on telomere damage in COEs-exposure workers
  JOURNAL   Ecotoxicol Environ Saf 250, 114489 (2023)
   PUBMED   36603485
  REMARK    GeneRIF: Effect and interaction of TNKS genetic polymorphisms and
            environmental factors on telomere damage in COEs-exposure workers.
REFERENCE   4  (residues 1 to 1327)
  AUTHORS   Xu,Y.R., Shi,M.L., Zhang,Y., Kong,N., Wang,C., Xiao,Y.F., Du,S.S.,
            Zhu,Q.Y. and Lei,C.Q.
  TITLE     Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation
  JOURNAL   Proc Natl Acad Sci U S A 119 (26), e2122805119 (2022)
   PUBMED   35733260
  REMARK    GeneRIF: Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation.
REFERENCE   5  (residues 1 to 1327)
  AUTHORS   Tang,B., Luo,H., Xie,S., Pan,C. and Fu,J.
  TITLE     Deubiquitination of TNKS1 Regulates Wnt/beta-Catenin to Affect the
            Expression of USP25 to Promote the Progression of Glioma
  JOURNAL   Dis Markers 2022, 9087190 (2022)
   PUBMED   35450028
  REMARK    GeneRIF: Deubiquitination of TNKS1 Regulates Wnt/beta-Catenin to
            Affect the Expression of USP25 to Promote the Progression of
            Glioma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1327)
  AUTHORS   Lyons,R.J., Deane,R., Lynch,D.K., Ye,Z.S., Sanderson,G.M.,
            Eyre,H.J., Sutherland,G.R. and Daly,R.J.
  TITLE     Identification of a novel human tankyrase through its interaction
            with the adaptor protein Grb14
  JOURNAL   J Biol Chem 276 (20), 17172-17180 (2001)
   PUBMED   11278563
REFERENCE   7  (residues 1 to 1327)
  AUTHORS   Chi,N.W. and Lodish,H.F.
  TITLE     Tankyrase is a golgi-associated mitogen-activated protein kinase
            substrate that interacts with IRAP in GLUT4 vesicles
  JOURNAL   J Biol Chem 275 (49), 38437-38444 (2000)
   PUBMED   10988299
REFERENCE   8  (residues 1 to 1327)
  AUTHORS   Smith,S. and de Lange,T.
  TITLE     Cell cycle dependent localization of the telomeric PARP, tankyrase,
            to nuclear pore complexes and centrosomes
  JOURNAL   J Cell Sci 112 (Pt 21), 3649-3656 (1999)
   PUBMED   10523501
REFERENCE   9  (residues 1 to 1327)
  AUTHORS   Zhu,L., Smith,S., de Lange,T. and Seldin,M.F.
  TITLE     Chromosomal mapping of the tankyrase gene in human and mouse
  JOURNAL   Genomics 57 (2), 320-321 (1999)
   PUBMED   10198177
REFERENCE   10 (residues 1 to 1327)
  AUTHORS   Smith,S., Giriat,I., Schmitt,A. and de Lange,T.
  TITLE     Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
  JOURNAL   Science 282 (5393), 1484-1487 (1998)
   PUBMED   9822378
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC021242.10, AC103877.2, AC103834.2 and AC104052.9.
            
            On Feb 14, 2006 this sequence version replaced NP_003738.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098394.1, SRR1803611.228164.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310430.11/ ENSP00000311579.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..1327
                     /product="poly [ADP-ribose] polymerase tankyrase-1"
                     /EC_number="2.4.2.30"
                     /note="tankyrase-1; TANK1; TNKS-1; tankyrase I; poly
                     [ADP-ribose] polymerase 5A; tankyrase, TRF1-interacting
                     ankyrin-related ADP-ribose polymerase;
                     ADP-ribosyltransferase diphtheria toxin-like 5;
                     TRF1-interacting ankyrin-related ADP-ribose polymerase 1;
                     protein poly-ADP-ribosyltransferase tankyrase-1"
                     /calculated_mol_wt=141909
     Region          1..91
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          112..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          181..209
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          182..504
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          215..244
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          218..246
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(221..222,225..227,229..230,234,237,246,248,250,
                     254..255,258..260,262..263,267,270,279,281,283,287..288,
                     291..293,295..296,300,303,312)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          248..279
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          248..277
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          281..312
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          281..310
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          288..628
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          335..364
                     /region_name="ANK 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          368..397
                     /region_name="ANK 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          371..399
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(374..375,378..380,382..383,387,390,399,401,403,
                     407..408,411..413,415..416,420,423,432,434,436,440..441,
                     444..446,448..449,453,456,465)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          401..432
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          401..430
                     /region_name="ANK 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          434..465
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          434..463
                     /region_name="ANK 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          521..553
                     /region_name="ANK 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Site            order(523,527..528,531..533,535,539,543,546,555,557,559,
                     563..564,567..569,571..572,576,579,588,590,592,596..597,
                     600..602,604..605,609,612)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          523..555
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          557..588
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          557..586
                     /region_name="ANK 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          590..619
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          590..619
                     /region_name="ANK 11. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          621..647
                     /region_name="ANK 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          632..953
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          649..679
                     /region_name="ANK 13. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          683..712
                     /region_name="ANK 14. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          686..714
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(689..690,693..695,697..698,702,705,714,716,718,
                     722..723,726..728,730..731,735,738,747,749,751,755..756,
                     759..761,763..764,768,771,780)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          716..747
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          716..745
                     /region_name="ANK 15. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          749..780
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          749..778
                     /region_name="ANK 16. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          782..810
                     /region_name="ANK 17. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          806..857
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
     Site            order(836,838,842..843,846..848,850..851,855,858,867,869,
                     871,875..876,879..881,883..884,888,891,900,902,904,
                     908..909,912..914,916..917,921,924,933)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          836..867
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          836..865
                     /region_name="ANK 18. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          869..900
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          869..898
                     /region_name="ANK 19. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          902..933
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          902..931
                     /region_name="ANK 20. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          935..964
                     /region_name="ANK 21. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          1024..1089
                     /region_name="SAM_tankyrase1,2"
                     /note="SAM domain of tankyrase1,2 subfamily; cd09524"
                     /db_xref="CDD:188923"
     Region          1091..1313
                     /region_name="tankyrase_like"
                     /note="Tankyrases interact with the telomere reverse
                     transcriptase complex (TERT). Tankyrase 1
                     poly-ADP-ribosylates Telomere Repeat Binding Factor 1
                     (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or
                     TRF1. The tankyrases also contain multiple ankyrin...;
                     cd01438"
                     /db_xref="CDD:238718"
     CDS             1..1327
                     /gene="TNKS"
                     /gene_synonym="ARTD5; PARP-5a; PARP5A; PARPL; pART5; TIN1;
                     TINF1; TNKS1"
                     /coded_by="NM_003747.3:29..4012"
                     /db_xref="CCDS:CCDS5974.1"
                     /db_xref="GeneID:8658"
                     /db_xref="HGNC:HGNC:11941"
                     /db_xref="MIM:603303"
ORIGIN      
        1 maasrrsqhh hhhhqqqlqp apgasapppp pppplspgla pgttpaspta sglapfaspr
       61 hglalpegdg srdppdrprs pdpvdgtscc sttstictva aapvvpavst ssaagvapnp
      121 agsgsnnsps ssssptssss sspsspgssl aespeaagvs staplgpgaa gpgtgvpavs
      181 galrelleac rngdvsrvkr lvdaanvnak dmagrksspl hfaagfgrkd vvehllqmga
      241 nvharddggl iplhnacsfg haevvslllc qgadpnardn wnytplheaa ikgkidvciv
      301 llqhgadpni rntdgksald ladpsakavl tgeykkdell eaarsgneek lmalltplnv
      361 nchasdgrks tplhlaagyn rvrivqlllq hgadvhakdk gglvplhnac syghyevtel
      421 llkhgacvna mdlwqftplh eaasknrvev cslllshgad ptlvnchgks avdmaptpel
      481 rerltyefkg hsllqaarea dlakvkktla leiinfkqpq shetalhcav aslhpkrkqv
      541 telllrkgan vneknkdfmt plhvaaerah ndvmevlhkh gakmnaldtl gqtalhraal
      601 aghlqtcrll lsygsdpsii slqgftaaqm gneavqqils estpirtsdv dyrlleaska
      661 gdletvkqlc ssqnvncrdl egrhstplhf aagynrvsvv eyllhhgadv hakdkgglvp
      721 lhnacsyghy evaellvrhg asvnvadlwk ftplheaaak gkyeicklll khgadptkkn
      781 rdgntpldlv kegdtdiqdl lrgdaallda akkgclarvq klctpeninc rdtqgrnstp
      841 lhlaagynnl evaeyllehg advnaqdkgg liplhnaasy ghvdiaalli kyntcvnatd
      901 kwaftplhea aqkgrtqlca lllahgadpt mknqegqtpl dlataddira llidamppea
      961 lptcfkpqat vvsaslispa stpsclsaas sidnltgpla elavggasna gdgaagterk
     1021 egevagldmn isqflkslgl ehlrdifete qitldvladm gheelkeigi nayghrhkli
     1081 kgverllggq qgtnpyltfh cvnqgtilld lapedkeyqs veeemqstir ehrdggnagg
     1141 ifnrynviri qkvvnkklre rfchrqkevs eenhnhhner mlfhgspfin aiihkgfder
     1201 hayiggmfga giyfaenssk snqyvygigg gtgcpthkdr scyichrqml fcrvtlgksf
     1261 lqfstmkmah appghhsvig rpsvnglaya eyviyrgeqa ypeylityqi mkpeapsqta
     1321 taaeqkt
//
LOCUS       NP_001123503             426 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 562 isoform a [Homo sapiens].
ACCESSION   NP_001123503
VERSION     NP_001123503.1
DBSOURCE    REFSEQ: accession NM_001130031.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Jia,L., Young,M.F., Powell,J., Yang,L., Ho,N.C., Hotchkiss,R.,
            Robey,P.G. and Francomano,C.A.
  TITLE     Gene expression profile of human bone marrow stromal cells:
            high-throughput expressed sequence tag sequencing analysis
  JOURNAL   Genomics 79 (1), 7-17 (2002)
   PUBMED   11827452
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP221824.1, DC405554.1, AC008759.9 and AI753280.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer protein (isoform a). Variants 1
            and 2 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP351030.1, SRR1803616.10275.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267752 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000453372.7/ ENSP00000410734.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..426
                     /product="zinc finger protein 562 isoform a"
                     /calculated_mol_wt=48432
     Region          40..81
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          <117..308
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          181..198
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          206..226
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <258..420
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          263..282
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          290..310
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          318..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(323,325,327,329..330,333..334,337,351,353,357..358,
                     361..362,365,379,381,383,385..386,389..390,393)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          346..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          374..394
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          402..422
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..426
                     /gene="ZNF562"
                     /coded_by="NM_001130031.2:217..1497"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45956.1"
                     /db_xref="GeneID:54811"
                     /db_xref="HGNC:HGNC:25950"
ORIGIN      
        1 msafdmshgf fprepicpfe ektkigtmve dhrsnsyqds vtfddvavef tpeewalldt
       61 tqkylyrdvm lenymnlasv dfffcltsew eiqprtkrss lqqgflknqi ftgiqmqtrs
      121 ysgwklcenc gevfseqfcl kthmraqngg ntfegncygk dsisvhkeas igqelskfnp
      181 cgkvftltpg lavhleilng rqpykckecg kgfkyfasld nhmgihigek lcefqecera
      241 ittsshlkqc vavhtgkkse ktkncgksft nfsqlsahak thkgeksfec kecgrsfrns
      301 ssfnvhiqih tgikphkcte cgkaftrsth ltqhvrthtg ikpyeckecg qaftqytgla
      361 ihirnhtgek pyqckecgka fnrsstltqh rrihtgekpy ecvecgktfi tsshrskhlk
      421 thsger
//
LOCUS       NP_001186180             527 aa            linear   PRI 27-APR-2025
DEFINITION  shugoshin 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001186180
VERSION     NP_001186180.1
DBSOURCE    REFSEQ: accession NM_001199251.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Yang,Z., Jiang,Y., Wang,L., Yu,B., Cai,H., Fan,J. and Zhang,M.
  TITLE     Prognosis and biological function of SGOL1 in clear cell renal cell
            carcinoma: a multiomics analysis
  JOURNAL   BMC Med Genomics 17 (1), 60 (2024)
   PUBMED   38383432
  REMARK    GeneRIF: Prognosis and biological function of SGOL1 in clear cell
            renal cell carcinoma: a multiomics analysis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Ueki,Y., Hadders,M.A., Weisser,M.B., Nasa,I., Sotelo-Parrilla,P.,
            Cressey,L.E., Gupta,T., Hertz,E.P.T., Kruse,T., Montoya,G.,
            Jeyaprakash,A.A., Kettenbach,A., Lens,S.M.A. and Nilsson,J.
  TITLE     A highly conserved pocket on PP2A-B56 is required for hSgo1 binding
            and cohesion protection during mitosis
  JOURNAL   EMBO Rep 22 (7), e52295 (2021)
   PUBMED   33973335
  REMARK    GeneRIF: A highly conserved pocket on PP2A-B56 is required for
            hSgo1 binding and cohesion protection during mitosis.
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Chetaille,P., Preuss,C., Burkhard,S., Cote,J.M., Houde,C.,
            Castilloux,J., Piche,J., Gosset,N., Leclerc,S., Wunnemann,F.,
            Thibeault,M., Gagnon,C., Galli,A., Tuck,E., Hickson,G.R., El
            Amine,N., Boufaied,I., Lemyre,E., de Santa Barbara,P., Faure,S.,
            Jonzon,A., Cameron,M., Dietz,H.C., Gallo-McFarlane,E., Benson,D.W.,
            Moreau,C., Labuda,D., Zhan,S.H., Shen,Y., Jomphe,M., Jones,S.J.,
            Bakkers,J. and Andelfinger,G.
  CONSRTM   FORGE Canada Consortium
  TITLE     Mutations in SGOL1 cause a novel cohesinopathy affecting heart and
            gut rhythm
  JOURNAL   Nat Genet 46 (11), 1245-1249 (2014)
   PUBMED   25282101
  REMARK    GeneRIF: Mutations in SGOL1 cause a novel cohesinopathy affecting
            heart and gut rhythm.
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Wang,X., Yang,Y., Duan,Q., Jiang,N., Huang,Y., Darzynkiewicz,Z. and
            Dai,W.
  TITLE     sSgo1, a major splice variant of Sgo1, functions in centriole
            cohesion where it is regulated by Plk1
  JOURNAL   Dev Cell 14 (3), 331-341 (2008)
   PUBMED   18331714
  REMARK    GeneRIF: Centriole splitting induced by Sgo1 depletion or
            expression of a dominant negative mutant is suppressed by ectopic
            expression of sSgo1 or by Plk1 knockdown.
REFERENCE   6  (residues 1 to 527)
  AUTHORS   Kitajima,T.S., Sakuno,T., Ishiguro,K., Iemura,S., Natsume,T.,
            Kawashima,S.A. and Watanabe,Y.
  TITLE     Shugoshin collaborates with protein phosphatase 2A to protect
            cohesin
  JOURNAL   Nature 441 (7089), 46-52 (2006)
   PUBMED   16541025
  REMARK    GeneRIF: a specific subtype of serine/threonine protein phosphatase
            2A (PP2A) associates with human shugoshin
REFERENCE   7  (residues 1 to 527)
  AUTHORS   Wang,X., Yang,Y. and Dai,W.
  TITLE     Differential subcellular localizations of two human Sgo1 isoforms:
            implications in regulation of sister chromatid cohesion and
            microtubule dynamics
  JOURNAL   Cell Cycle 5 (6), 635-640 (2006)
   PUBMED   16582621
REFERENCE   8  (residues 1 to 527)
  AUTHORS   McGuinness,B.E., Hirota,T., Kudo,N.R., Peters,J.M. and Nasmyth,K.
  TITLE     Shugoshin prevents dissociation of cohesin from centromeres during
            mitosis in vertebrate cells
  JOURNAL   PLoS Biol 3 (3), e86 (2005)
   PUBMED   15737064
  REMARK    GeneRIF: A shugoshin-like protein associates with centromeres
            during prophase and disappears at the onset of anaphase
REFERENCE   9  (residues 1 to 527)
  AUTHORS   Tang,Z., Sun,Y., Harley,S.E., Zou,H. and Yu,H.
  TITLE     Human Bub1 protects centromeric sister-chromatid cohesion through
            Shugoshin during mitosis
  JOURNAL   Proc Natl Acad Sci U S A 101 (52), 18012-18017 (2004)
   PUBMED   15604152
  REMARK    GeneRIF: Bub1 protects centromeric cohesion through Shugoshin in
            mitosis
REFERENCE   10 (residues 1 to 527)
  AUTHORS   Scanlan,M.J., Gout,I., Gordon,C.M., Williamson,B., Stockert,E.,
            Gure,A.O., Jager,D., Chen,Y.T., Mackay,A., O'Hare,M.J. and Old,L.J.
  TITLE     Humoral immunity to human breast cancer: antigen definition and
            quantitative analysis of mRNA expression
  JOURNAL   Cancer Immun 1, 4 (2001)
   PUBMED   12747765
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK308095.1, AB190994.1,
            AF308299.1, BC032696.1, BX648516.1 and AC099057.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            shugoshin family of proteins. This protein is thought to protect
            centromeric cohesin from cleavage during mitotic prophase by
            preventing phosphorylation of a cohesin subunit. Reduced expression
            of this gene leads to the premature loss of centromeric cohesion,
            mis-segregation of sister chromatids, and mitotic arrest. Evidence
            suggests that this protein also protects a small subset of cohesin
            found along the length of the chromosome arms during mitotic
            prophase. An isoform lacking exon 6 has been shown to play a role
            in the cohesion of centrioles (PMID: 16582621 and PMID:18331714).
            Mutations in this gene have been associated with Chronic Atrial and
            Intestinal Dysrhythmia (CAID) syndrome, characterized by the
            co-occurrence of Sick Sinus Syndrome (SSS) and Chronic Intestinal
            Pseudo-obstruction (CIPO) within the first four decades of life
            (PMID:25282101). Fibroblast cells from CAID patients exhibited both
            increased cell proliferation and higher rates of senescence.
            Pseudogenes of this gene have been found on chromosomes 1 and 7.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Both variants 1 and A1 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB190994.1, SRR9304714.96190.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267758, SAMN03267770
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000412997.6/ ENSP00000410458.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..527
                     /product="shugoshin 1 isoform 1"
                     /note="shugoshin 1AB protein; shugoshin 1CD protein;
                     shugoshin 1EF protein; shugoshin 1GH protein; shugoshin
                     1KL protein; serologically defined breast cancer antigen
                     NY-BR-85"
                     /calculated_mol_wt=59991
     Region          1..176
                     /region_name="Necessary for interaction with PPP2CA and
                     PPP2R1A. /evidence=ECO:0000269|PubMed:16580887"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK2.
                     /evidence=ECO:0000269|PubMed:17621308; propagated from
                     UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          22..66
                     /region_name="Shugoshin_N"
                     /note="Shugoshin N-terminal coiled-coil region; pfam07558"
                     /db_xref="CDD:462208"
     Region          192..200
                     /region_name="D-box 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          260..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          310..312
                     /region_name="KEN box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          348..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          438..446
                     /region_name="D-box 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          451..455
                     /region_name="PXVXL/I motif.
                     /evidence=ECO:0000305|PubMed:21346195"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          457..465
                     /region_name="D-box 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          474..495
                     /region_name="Shugoshin_C"
                     /note="Shugoshin C terminus; pfam07557"
                     /db_xref="CDD:462207"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK2.
                     /evidence=ECO:0000269|PubMed:17621308,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     CDS             1..527
                     /gene="SGO1"
                     /gene_synonym="CAID; NY-BR-85; SGO; SGOL1"
                     /coded_by="NM_001199251.3:267..1850"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46773.1"
                     /db_xref="GeneID:151648"
                     /db_xref="HGNC:HGNC:25088"
                     /db_xref="MIM:609168"
ORIGIN      
        1 makerclkks fqdsledikk rmkekrnknl aeigkrrsfi aapcqiitnt stllknyqdn
       61 nkmlvlalen ekskvkeaqd iilqlrkecy yltcqlyalk gkltsqqtve paqnqeicss
      121 gmdpnsddss rnlfvkdlpq ipleetelpg qgesfqiedq iptipqdtlg vdfdsgeaks
      181 tdnvlprtvs vrsslkkhcn sicqfdsldd fetshlagks fefervgfld plvnmhipen
      241 vqhnacqwsk dqvnlspkli qpgtftktke dileskseqt kskqrdtqer kreekrkanr
      301 rkskrmskyk enksenkktv pqkkmhksvs sndaynfnle egvhltpfrq kvsndsnree
      361 nnesevslce ssgsgddsdd lylptckyiq nptsnsdrpv trplakralk ytdeketegs
      421 kptktptttp petqqsphls lkditnvsly pvvkirrlsl spkknkaspa valpkrrcta
      481 svnykeptla sklrrgdpft dlcflnspif kqkkdlrrsk ksmkqiq
//
LOCUS       NP_904355                838 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF19A [Homo sapiens].
ACCESSION   NP_904355
VERSION     NP_904355.1
DBSOURCE    REFSEQ: accession NM_183419.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Yuan,H., Yu,J., Liu,C., Zhao,H., Xue,J., Liu,J. and Yang,Y.
  TITLE     LncRNA KCNQ10T1 shuttled by bone marrow mesenchymal stem
            cell-derived exosome inhibits sepsis via regulation of
            miR-154-3p/RNF19A axis
  JOURNAL   Cell Tissue Res 393 (3), 507-521 (2023)
   PUBMED   37326687
  REMARK    GeneRIF: LncRNA KCNQ10T1 shuttled by bone marrow mesenchymal stem
            cell-derived exosome inhibits sepsis via regulation of
            miR-154-3p/RNF19A axis.
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Zhang,N., Huang,D., Ruan,X., Ng,A.T., Tsu,J.H., Jiang,G., Huang,J.,
            Zhan,Y. and Na,R.
  TITLE     CRISPR screening reveals gleason score and castration resistance
            related oncodriver ring finger protein 19 A (RNF19A) in prostate
            cancer
  JOURNAL   Drug Resist Updat 67, 100912 (2023)
   PUBMED   36623445
  REMARK    GeneRIF: CRISPR screening reveals gleason score and castration
            resistance related oncodriver ring finger protein 19 A (RNF19A) in
            prostate cancer.
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Zhu,Q., Huang,J., Huang,H., Li,H., Yi,P., Kloeber,J.A., Yuan,J.,
            Chen,Y., Deng,M., Luo,K., Gao,M., Guo,G., Tu,X., Yin,P., Zhang,Y.,
            Su,J., Chen,J. and Lou,Z.
  TITLE     RNF19A-mediated ubiquitination of BARD1 prevents
            BRCA1/BARD1-dependent homologous recombination
  JOURNAL   Nat Commun 12 (1), 6653 (2021)
   PUBMED   34789768
  REMARK    GeneRIF: RNF19A-mediated ubiquitination of BARD1 prevents
            BRCA1/BARD1-dependent homologous recombination.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 838)
  AUTHORS   Cheng,Y., Hu,Y., Wang,H., Zhao,Z., Jiang,X., Zhang,Y., Zhang,J.,
            Tong,Y. and Qiu,X.
  TITLE     Ring finger protein 19A is overexpressed in non-small cell lung
            cancer and mediates p53 ubiquitin-degradation to promote cancer
            growth
  JOURNAL   J Cell Mol Med 25 (16), 7796-7808 (2021)
   PUBMED   34184814
  REMARK    GeneRIF: Ring finger protein 19A is overexpressed in non-small cell
            lung cancer and mediates p53 ubiquitin-degradation to promote
            cancer growth.
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Ito,T., Niwa,J., Hishikawa,N., Ishigaki,S., Doyu,M. and Sobue,G.
  TITLE     Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1
  JOURNAL   J Biol Chem 278 (31), 29106-29114 (2003)
   PUBMED   12750386
  REMARK    GeneRIF: results suggest that synphilin-1 has an important role in
            the formation of aggregates and cytotoxicity in Parkinson disease
            and that Dorfin may be involved in the pathogenic process by
            ubiquitylation of synphilin-1
REFERENCE   7  (residues 1 to 838)
  AUTHORS   Hishikawa,N., Niwa,J., Doyu,M., Ito,T., Ishigaki,S., Hashizume,Y.
            and Sobue,G.
  TITLE     Dorfin localizes to the ubiquitylated inclusions in Parkinson's
            disease, dementia with Lewy bodies, multiple system atrophy, and
            amyotrophic lateral sclerosis
  JOURNAL   Am J Pathol 163 (2), 609-619 (2003)
   PUBMED   12875980
  REMARK    GeneRIF: These results suggest that Dorfin plays a crucial role in
            the formation of ubiquitylated inclusions of alpha-synucleinopathy
            and amyotrophic lateral sclerosis.
REFERENCE   8  (residues 1 to 838)
  AUTHORS   Niwa,J., Ishigaki,S., Hishikawa,N., Yamamoto,M., Doyu,M.,
            Murata,S., Tanaka,K., Taniguchi,N. and Sobue,G.
  TITLE     Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated
            neurotoxicity
  JOURNAL   J Biol Chem 277 (39), 36793-36798 (2002)
   PUBMED   12145308
  REMARK    GeneRIF: Dorfin has a role in ubiquitylating mutant SOD1 proteins
            and targeting them for proteasomal degradation
REFERENCE   9  (residues 1 to 838)
  AUTHORS   Niwa,J., Ishigaki,S., Doyu,M., Suzuki,T., Tanaka,K. and Sobue,G.
  TITLE     A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin
            ligase activity
  JOURNAL   Biochem Biophys Res Commun 281 (3), 706-713 (2001)
   PUBMED   11237715
REFERENCE   10 (residues 1 to 838)
  AUTHORS   Gunther,M., Laithier,M. and Brison,O.
  TITLE     A set of proteins interacting with transcription factor Sp1
            identified in a two-hybrid screening
  JOURNAL   Mol Cell Biochem 210 (1-2), 131-142 (2000)
   PUBMED   10976766
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB037264.1, BC093938.1,
            AL122096.1 and BQ003778.1.
            
            Summary: This gene encodes a member of the ring between ring
            fingers (RBR) protein family, and the encoded protein contains two
            RING-finger motifs and an in between RING fingers motif. This
            protein is an E3 ubiquitin ligase that is localized to Lewy bodies,
            and ubiquitylates synphilin-1, which is an interacting protein of
            alpha synuclein in neurons. The encoded protein may be involved in
            amyotrophic lateral sclerosis and Parkinson's disease. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, 3, 4, and 5 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.209668.1,
                                           SRR1660809.91813.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341084.7/ ENSP00000342667.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.2"
     Protein         1..838
                     /product="E3 ubiquitin-protein ligase RNF19A"
                     /EC_number="2.3.2.31"
                     /note="double ring-finger protein; protein p38 interacting
                     with transcription factor Sp1; ring-IBR-ring domain
                     containing protein Dorfin; ring finger protein 19A, E3
                     ubiquitin protein ligase"
                     /calculated_mol_wt=90566
     Region          41..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NV58.3)"
     Region          128..351
                     /region_name="TRIAD supradomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NV58.3)"
     Region          130..185
                     /region_name="RING-HC_RBR_RNF19A"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 19A (RNF19A) and similar proteins; cd16775"
                     /db_xref="CDD:438431"
     Region          191..273
                     /region_name="BRcat_RBR_RNF19A"
                     /note="BRcat domain found in RING finger protein 19A
                     (RNF19A); cd20362"
                     /db_xref="CDD:439023"
     Region          295..363
                     /region_name="Rcat_RBR_RNF19"
                     /note="Rcat domain found in the RING finger protein 19
                     (RNF19) subfamily; cd20355"
                     /db_xref="CDD:439016"
     Site            368..388
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NV58.3)"
     Site            424..444
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NV58.3)"
     Region          622..685
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NV58.3)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NV58.3)"
     Region          660..838
                     /region_name="Interaction with CASR.
                     /evidence=ECO:0000269|PubMed:16513638"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NV58.3)"
     Region          700..721
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NV58.3)"
     CDS             1..838
                     /gene="RNF19A"
                     /gene_synonym="RNF19"
                     /coded_by="NM_183419.4:181..2697"
                     /db_xref="CCDS:CCDS6286.1"
                     /db_xref="GeneID:25897"
                     /db_xref="HGNC:HGNC:13432"
                     /db_xref="MIM:607119"
ORIGIN      
        1 mqeqeigfis kyneglcvnt dpvsiltsil dmslhrqmgs drdlqssass vslpsvkkap
       61 kkrrisigsl frrkkdnkrk srelnggvdg iasiesihse mctdknsifs tntssdnglt
      121 siskqigdfi ecplcllrhs kdrfpdimtc hhrscvdclr qylrieises rvniscpect
      181 erfnphdirl ilsddvlmek yeefmlrrwl vadpdcrwcp apdcgyavia fgcascpklt
      241 cgregcgtef cyhckqiwhp nqtcdaarqe raqslrlrti rsssisysqe sgaaaddikp
      301 cprcaayiik mndgscnhmt cavcgcefcw lcmkeisdlh ylspsgctfw gkkpwsrkkk
      361 ilwqlgtlvg apvgialiag iaipamiigi pvyvgrkihn ryegkdvskh krnlaiaggv
      421 tlsvivspvv aavtvgigvp imlayvygvv pislcrsggc gvsagngkgv riefddendi
      481 nvggtntavd ttsvaearhn psigegsvgg ltgslsasgs hmdrigaird nlsetastma
      541 lagasitgsl sgsamvncfn rlevqadvqk eryslsgesg tvslgtvsdn astkamagsi
      601 lnsyipldke gnsmevqvdi eskpskfrhn sgsssvddgs atrshaggss sglpegkssa
      661 tkwskeatag kksksgklrk kgnmkinetr edmdaqlleq qstnssefea pslsdsmpsv
      721 adshsshfse fscsdlesmk tscshgssdy htrfatvnil pevendrlen sphqcsisvv
      781 tqtascsevs qlnhiaeehg nngikpnvdl yfgdalketn nnhshqtmel kvaiqtei
//
LOCUS       NP_941055               1012 aa            linear   ROD 27-APR-2025
DEFINITION  isoleucine--tRNA ligase, mitochondrial precursor [Mus musculus].
ACCESSION   NP_941055 XP_355261
VERSION     NP_941055.1
DBSOURCE    REFSEQ: accession NM_198653.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK048653.1 and AK043590.1.
            
            On Nov 24, 2003 this sequence version replaced XP_355261.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK048653.1, AK043590.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 89.48 cM"
     Protein         1..1012
                     /product="isoleucine--tRNA ligase, mitochondrial
                     precursor"
                     /EC_number="6.1.1.5"
                     /note="isoleucyl-tRNA synthetase, mitochondrial; ileRS;
                     isoleucine--tRNA ligase, mitochondrial"
                     /calculated_mol_wt=107933
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q8BIJ6.1)"
                     /calculated_mol_wt=4890
     mat_peptide     49..1012
                     /product="Isoleucine--tRNA ligase, mitochondrial.
                     /id=PRO_0000233337"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BIJ6.1)"
                     /calculated_mol_wt=107933
     Region          60..1009
                     /region_name="IleS"
                     /note="Isoleucyl-tRNA synthetase [Translation, ribosomal
                     structure and biogenesis]; COG0060"
                     /db_xref="CDD:439830"
     Site            74
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q8BIJ6.1)"
     Region          116..126
                     /region_name="'HIGH' region. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BIJ6.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NSE4; propagated from
                     UniProtKB/Swiss-Prot (Q8BIJ6.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9NSE4; propagated from
                     UniProtKB/Swiss-Prot (Q8BIJ6.1)"
     Region          664..668
                     /region_name="'KMSKS' region. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BIJ6.1)"
     Site            725
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q8BIJ6.1)"
     Site            775
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q8BIJ6.1)"
     Site            781
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9NSE4; propagated from
                     UniProtKB/Swiss-Prot (Q8BIJ6.1)"
     CDS             1..1012
                     /gene="Iars2"
                     /gene_synonym="2010002H18Rik"
                     /coded_by="NM_198653.3:115..3153"
                     /db_xref="CCDS:CCDS15596.1"
                     /db_xref="GeneID:381314"
                     /db_xref="MGI:MGI:1919586"
ORIGIN      
        1 mhwglcprgp gaaavaaags fwgparlpsr lgclgmtrrl vvrsvagads pqssskggry
       61 rdtvllpqts fpmkllgrqq sdmeleiqqk cgfselyswq rerkvktefc lhdgppyang
      121 dphvghalnk ilkdianrfh mmrgskvhfv pgwdchglpi etkvlselgv daqslsamei
      181 rekarsfaqa aiekqksafv rwgvmadwnn cyytfdpkye akqlrvfyqm yekglvyrsy
      241 kpvywspssr talaeaeley npehvsrsiy vrfpllrppp klesltdass pvsvlvwttq
      301 pwtipanqai cympeakyav vkcsasghly ilaedkiapv asalettfdv vaafsgvdle
      361 ggtcshpltp dkvspllpat hvtmakgtgl vhtapahgme dysvasqhsl pmdclvdegg
      421 mftdaagpel qnkavlkegt dvvikmlqat knvlkeeniv hsypcdwrtk tpvliraskq
      481 wfvnitdika aakeslktvk fipgaalnsm tdmldrrpyw cisrqrvwgv pipvfhhktk
      541 deylinsqtt ehiiklveqh gsdvwwtlpa eqllpaevla qaggpgaley apgqdildiw
      601 fdsgtswscv lqdtqqradl ylegkdqlgg wfqsslltsv atrskapfrt vmvhgftlge
      661 kgekmskslg nvinpdtiis ggkdhskepp ygadilrwwi aesnvftevt igpsvlsaar
      721 ddisklrntl rfllgnltgf npetdsvpvk nmyvidqyml hliqdfatki tdsykqydfg
      781 kvvrllkafy trelssfyfs ivkdrlycen ekdpkrrscq talaeildvl vrafapilph
      841 laeevfqhip yvtepksvfr tgwintssiw kkpgleeave sacamrdsfl gsipgknaae
      901 yeviiviepg llfeimemlq aeetsstsql nelmmasqtt llaqeprert agdieltgtf
      961 vinleggdir eessykvivv ptarekcprc wkhtsetada lcprcaevig ak
//
LOCUS       NP_115885                731 aa            linear   PRI 27-APR-2025
DEFINITION  rho GTPase-activating protein 9 isoform 1 [Homo sapiens].
ACCESSION   NP_115885
VERSION     NP_115885.2
DBSOURCE    REFSEQ: accession NM_032496.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Sun,J., Zhao,X., Jiang,H., Yang,T., Li,D., Yang,X., Jia,A., Ma,Y.
            and Qian,Z.
  TITLE     ARHGAP9 inhibits colorectal cancer cell proliferation, invasion and
            EMT via targeting PI3K/AKT/mTOR signaling pathway
  JOURNAL   Tissue Cell 77, 101817 (2022)
   PUBMED   35679685
  REMARK    GeneRIF: ARHGAP9 inhibits colorectal cancer cell proliferation,
            invasion and EMT via targeting PI3K/AKT/mTOR signaling pathway.
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Ji,W., Zhang,L. and Zhu,H.
  TITLE     GATA binding protein 5 (GATA5) induces Rho GTPase activating
            protein 9 (ARHGAP9) to inhibit the malignant process of lung
            adenocarcinoma cells
  JOURNAL   Bioengineered 13 (2), 2878-2888 (2022)
   PUBMED   35040754
  REMARK    GeneRIF: GATA binding protein 5 (GATA5) induces Rho GTPase
            activating protein 9 (ARHGAP9) to inhibit the malignant process of
            lung adenocarcinoma cells.
REFERENCE   3  (residues 1 to 731)
  AUTHORS   He,X., Zou,H. and Wang,F.
  TITLE     SOX4-induced upregulation of ARHGAP9 promotes the progression of
            acute myeloid leukemia
  JOURNAL   Drug Dev Res 82 (8), 1227-1234 (2021)
   PUBMED   34159626
  REMARK    GeneRIF: SOX4-induced upregulation of ARHGAP9 promotes the
            progression of acute myeloid leukemia.
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Han,C., He,S., Wang,R., Gao,X., Wang,H., Qiao,J., Meng,X., Li,Y.
            and Yu,L.
  TITLE     The role of ARHGAP9: clinical implication and potential function in
            acute myeloid leukemia
  JOURNAL   J Transl Med 19 (1), 65 (2021)
   PUBMED   33579308
  REMARK    GeneRIF: The role of ARHGAP9: clinical implication and potential
            function in acute myeloid leukemia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 731)
  AUTHORS   Voss,M., Lettau,M. and Janssen,O.
  TITLE     Identification of SH3 domain interaction partners of human FasL
            (CD178) by phage display screening
  JOURNAL   BMC Immunol 10, 53 (2009)
   PUBMED   19807924
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 731)
  AUTHORS   Ceccarelli,D.F., Blasutig,I.M., Goudreault,M., Li,Z., Ruston,J.,
            Pawson,T. and Sicheri,F.
  TITLE     Non-canonical interaction of phosphoinositides with pleckstrin
            homology domains of Tiam1 and ArhGAP9
  JOURNAL   J Biol Chem 282 (18), 13864-13874 (2007)
   PUBMED   17339315
REFERENCE   8  (residues 1 to 731)
  AUTHORS   Ang,B.K., Lim,C.Y., Koh,S.S., Sivakumar,N., Taib,S., Lim,K.B.,
            Ahmed,S., Rajagopal,G. and Ong,S.H.
  TITLE     ArhGAP9, a novel MAP kinase docking protein, inhibits Erk and p38
            activation through WW domain binding
  JOURNAL   J Mol Signal 2, 1 (2007)
   PUBMED   17284314
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 731)
  AUTHORS   Peck,J., Douglas,G. 4th, Wu,C.H. and Burbelo,P.D.
  TITLE     Human RhoGAP domain-containing proteins: structure, function and
            evolutionary relationships
  JOURNAL   FEBS Lett 528 (1-3), 27-34 (2002)
   PUBMED   12297274
  REMARK    Review article
REFERENCE   10 (residues 1 to 731)
  AUTHORS   Furukawa,Y., Kawasoe,T., Daigo,Y., Nishiwaki,T., Ishiguro,H.,
            Takahashi,M., Kitayama,J. and Nakamura,Y.
  TITLE     Isolation of a novel human gene, ARHGAP9, encoding a rho-GTPase
            activating protein
  JOURNAL   Biochem Biophys Res Commun 284 (3), 643-649 (2001)
   PUBMED   11396949
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC408597.1 and AB051853.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 18, 2007 this sequence version replaced NP_115885.1.
            
            Summary: This gene encodes a member of the Rho-GAP family of GTPase
            activating proteins. The protein has substantial GAP activity
            towards several Rho-family GTPases in vitro, converting them to an
            inactive GDP-bound state. It is implicated in regulating adhesion
            of hematopoietic cells to the extracellular matrix. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB051853.1, SRR18074968.2024504.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393791.8/ ENSP00000377380.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..731
                     /product="rho GTPase-activating protein 9 isoform 1"
                     /note="rho-type GTPase-activating protein 9"
                     /calculated_mol_wt=81019
     Region          26..82
                     /region_name="SH3_ARHGAP9"
                     /note="Src Homology 3 domain of Rho GTPase-activating
                     protein 9 and similar proteins; cd12143"
                     /db_xref="CDD:213019"
     Site            order(31,33,36,42,60..61,79,81..82)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213019"
     Region          <122..>312
                     /region_name="PHA03377"
                     /note="EBNA-3C; Provisional"
                     /db_xref="CDD:177614"
     Region          324..436
                     /region_name="PH_ARHGAP9-like"
                     /note="Beta-spectrin pleckstrin homology (PH) domain;
                     cd13233"
                     /db_xref="CDD:270053"
     Site            order(332,343..345,396..398)
                     /site_type="other"
                     /note="non-cannonial phosphoinositide binding site
                     [chemical binding]"
                     /db_xref="CDD:270053"
     Region          521..725
                     /region_name="RhoGAP_ARHGAP27_15_12_9"
                     /note="GTPase-activator protein (GAP) domain for Rho-like
                     GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15,
                     12 and 9-like proteins; This subgroup of ARHGAPs are
                     multidomain proteins that contain RhoGAP, PH, SH3 and WW
                     domains. Most members that are...; cd04403"
                     /db_xref="CDD:239868"
     Site            order(559,616,620,689,692..693,716)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239868"
     Site            559
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239868"
     CDS             1..731
                     /gene="ARHGAP9"
                     /gene_synonym="10C; RGL1"
                     /coded_by="NM_032496.4:156..2351"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8941.2"
                     /db_xref="GeneID:64333"
                     /db_xref="HGNC:HGNC:14130"
                     /db_xref="MIM:610576"
ORIGIN      
        1 mlssrwwpss wgilglgprs pprgsqlcal yaftytgadg qqvslaegdr flllrktnsd
       61 wwlarrleap stsrpifvpa aymieesips qspttvipgq llwtpgpklf hgsleelsqa
      121 lpsraqasse qppplprkmc rsvstdnlsp sllkpfqegp sgrslsqedl pseasastag
      181 pqplmseppv ycnlvdlrrc prspppgpac pllqrldawe qhldpnsgrc fyinsltgck
      241 swkpprrsrs etnpgsmegt qtlkrnndvl qpqakgfrsd tgtpepldpq gslslsqrts
      301 qldppalqap rplpqllddp heveksglln mtkiaqggrk lrknwgpswv vltgnslvfy
      361 reppptapss gwgpagsrpe ssvdlrgaal ahgrhlssrr nvlhirtipg hefllqsdhe
      421 telrawhral rtvierldre nplelrlsgs gpaelsaged eeeeselvsk pllrlssrrs
      481 sirgpegteq nrvrnklkrl iakrpplqsl qergllrdqv fgcqleslcq regdtvpsfl
      541 rlciaavdkr gldvdgiyrv sgnlavvqkl rflvdrerav tsdgryvfpe qpgqegrldl
      601 dstewddihv vtgalklflr elpqplvppl llphfraala lseseqclsq iqeligsmpk
      661 pnhdtlryll ehlcrviahs dknrmtphnl givfgptlfr peqetsdpaa halypgqlvq
      721 lmltnftslf p
//
LOCUS       NP_658988                937 aa            linear   PRI 27-APR-2025
DEFINITION  guanine nucleotide exchange protein SMCR8 [Homo sapiens].
ACCESSION   NP_658988
VERSION     NP_658988.2
DBSOURCE    REFSEQ: accession NM_144775.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Tang,D., Zheng,K., Zhu,J., Jin,X., Bao,H., Jiang,L., Li,H.,
            Wang,Y., Lu,Y., Liu,J., Liu,H., Tang,C., Feng,S., Dong,X., Xu,L.,
            Yin,Y., Dang,S., Wei,X., Ren,H., Dong,B., Dai,L., Cheng,W., Wan,M.,
            Li,Z., Chen,J., Li,H., Kong,E., Wang,K., Lu,K. and Qi,S.
  TITLE     ALS-linked C9orf72-SMCR8 complex is a negative regulator of primary
            ciliogenesis
  JOURNAL   Proc Natl Acad Sci U S A 120 (50), e2220496120 (2023)
   PUBMED   38064514
  REMARK    GeneRIF: ALS-linked C9orf72-SMCR8 complex is a negative regulator
            of primary ciliogenesis.
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Su,M.Y., Fromm,S.A., Zoncu,R. and Hurley,J.H.
  TITLE     Structure of the C9orf72 ARF GAP complex that is haploinsufficient
            in ALS and FTD
  JOURNAL   Nature 585 (7824), 251-255 (2020)
   PUBMED   32848248
  REMARK    GeneRIF: Structure of the C9orf72 ARF GAP complex that is
            haploinsufficient in ALS and FTD.
REFERENCE   4  (residues 1 to 937)
  AUTHORS   Goodier,J.L., Soares,A.O., Pereira,G.C., DeVine,L.R., Sanchez,L.,
            Cole,R.N. and Garcia-Perez,J.L.
  TITLE     C9orf72-associated SMCR8 protein binds in the ubiquitin pathway and
            with proteins linked with neurological disease
  JOURNAL   Acta Neuropathol Commun 8 (1), 110 (2020)
   PUBMED   32678027
  REMARK    GeneRIF: C9orf72-associated SMCR8 protein binds in the ubiquitin
            pathway and with proteins linked with neurological disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 937)
  AUTHORS   Tang,D., Sheng,J., Xu,L., Zhan,X., Liu,J., Jiang,H., Shu,X.,
            Liu,X., Zhang,T., Jiang,L., Zhou,C., Li,W., Cheng,W., Li,Z.,
            Wang,K., Lu,K., Yan,C. and Qi,S.
  TITLE     Cryo-EM structure of C9ORF72-SMCR8-WDR41 reveals the role as a GAP
            for Rab8a and Rab11a
  JOURNAL   Proc Natl Acad Sci U S A 117 (18), 9876-9883 (2020)
   PUBMED   32303654
  REMARK    GeneRIF: Our study not only illustrates the basis of
            C9ORF72-SMCR8-WDR41 complex assembly but also reveals the GAP
            activity of the C9ORF72-SMCR8 complex
REFERENCE   6  (residues 1 to 937)
  AUTHORS   Sellier,C., Campanari,M.L., Julie Corbier,C., Gaucherot,A.,
            Kolb-Cheynel,I., Oulad-Abdelghani,M., Ruffenach,F., Page,A.,
            Ciura,S., Kabashi,E. and Charlet-Berguerand,N.
  TITLE     Loss of C9ORF72 impairs autophagy and synergizes with polyQ
            Ataxin-2 to induce motor neuron dysfunction and cell death
  JOURNAL   EMBO J 35 (12), 1276-1297 (2016)
   PUBMED   27103069
REFERENCE   7  (residues 1 to 937)
  AUTHORS   Sullivan,P.M., Zhou,X., Robins,A.M., Paushter,D.H., Kim,D.,
            Smolka,M.B. and Hu,F.
  TITLE     The ALS/FTLD associated protein C9orf72 associates with SMCR8 and
            WDR41 to regulate the autophagy-lysosome pathway
  JOURNAL   Acta Neuropathol Commun 4 (1), 51 (2016)
   PUBMED   27193190
  REMARK    GeneRIF: Study describes the identification of two binding partners
            for C9orf72: SMCR8 and WDR41 and demonstrated that
            C9orf72/SMCR8/WDR41 interacts with the FIP200/Ulk1/ATG13/ATG101
            complex.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 937)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 937)
  AUTHORS   Zhang,D., Iyer,L.M., He,F. and Aravind,L.
  TITLE     Discovery of Novel DENN Proteins: Implications for the Evolution of
            Eukaryotic Intracellular Membrane Structures and Human Disease
  JOURNAL   Front Genet 3, 283 (2012)
   PUBMED   23248642
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 937)
  AUTHORS   Bi,W., Yan,J., Stankiewicz,P., Park,S.S., Walz,K., Boerkoel,C.F.,
            Potocki,L., Shaffer,L.G., Devriendt,K., Nowaczyk,M.J., Inoue,K. and
            Lupski,J.R.
  TITLE     Genes in a refined Smith-Magenis syndrome critical deletion
            interval on chromosome 17p11.2 and the syntenic region of the mouse
  JOURNAL   Genome Res 12 (5), 713-728 (2002)
   PUBMED   11997338
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP280386.1, AF467440.1, BC101116.2, AC127537.8 and CK724925.1.
            
            On May 4, 2007 this sequence version replaced NP_658988.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.99884.1, BC142680.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000406438.5/ ENSP00000385025.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..937
                     /product="guanine nucleotide exchange protein SMCR8"
                     /note="smith-Magenis syndrome chromosomal region candidate
                     gene 8 protein; Smith-Magenis syndrome chromosome region,
                     candidate 8"
                     /calculated_mol_wt=104892
     Region          1..349
                     /region_name="Required for the homodimerization of the
                     C9orf72-SMCR8 complex.
                     /evidence=ECO:0000269|PubMed:32303654"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Region          274..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Region          384..405
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000269|PubMed:27103069; propagated from
                     UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Region          564..645
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Site            790
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Site            796
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by TBK1.
                     /evidence=ECO:0000269|PubMed:27103069; propagated from
                     UniProtKB/Swiss-Prot (Q8TEV9.2)"
     Region          862..914
                     /region_name="Interacts with WDR41 within the
                     C9orf72-SMCR8 complex.
                     /evidence=ECO:0000269|PubMed:32303654"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEV9.2)"
     CDS             1..937
                     /gene="SMCR8"
                     /gene_synonym="DENND8A"
                     /coded_by="NM_144775.3:498..3311"
                     /db_xref="CCDS:CCDS11195.2"
                     /db_xref="GeneID:140775"
                     /db_xref="HGNC:HGNC:17921"
                     /db_xref="MIM:617074"
ORIGIN      
        1 misapdvvaf tkeeeyeeep ynepalpeey svplfpfasq ganpwsklsg akfsrdfili
       61 sefseqvgpq plltipndtk vfgtfdlnyf slrimsvdyq asfvghppgs aypklnfved
      121 skvvlgdske gafayvhhlt lydleargfv rpfcmayisa dqhkimqqfq elsaefsras
      181 eclktgnrka fagelekklk dldytrtvlh teteiqkkan dkgfyssqai ekanelasve
      241 ksiiehqdll kqirsyphrk lkghdlcpge mehiqdqasq asttsnpdes adtdlytcrp
      301 aytpklikak stkcfdkklk tleelcdtey ftqtlaqlsh iehmfrgdlc ylltsqidra
      361 llkqqhitnf lfedfvevdd rmvekqesip skpsqdrpps ssleecpipk vlisvgsyks
      421 svesvlikme qelgdeeyke vevtelssfd pqenldyldm dmkgsissge sievlgteks
      481 tsvlsksdsq asltvplspq vvrskavshr tisedsievl stcpsealip ddfkasypsa
      541 ineeesypdg negairfqas isppelgete egsientpsq idssccigke sdgqlvlpst
      601 pahthsdedg vvssppqrhr qkdqgfrvdf svenanpssr dnscegfpay eldpshllas
      661 rdisktsldn ysdttsyvss vastssdrip saypaglssd rhkkragqna lkfirqypfa
      721 hpaiysllsg rtlvvlgede aivrklvtal aifvpsygcy akpvkhwass plhimdfqkw
      781 kliglqrvas pagagtlhal srysrytsil dldnktlrcp lyrgtlvprl adhrtqikrg
      841 styylhvqsm ltqlcskafl ytfchhlhlp thdketeelv asrqmsflkl tlglvnedvr
      901 vvqylaellk lhymqespgt shpmlrfdyv psflyki
//
LOCUS       NP_001356467             537 aa            linear   PRI 27-APR-2025
DEFINITION  BDNF/NT-3 growth factors receptor isoform e precursor [Homo
            sapiens].
ACCESSION   NP_001356467
VERSION     NP_001356467.1
DBSOURCE    REFSEQ: accession NM_001369538.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Gupta,R., Dittmeier,M., Wohlleben,G., Nickl,V., Bischler,T.,
            Luzak,V., Wegat,V., Doll,D., Sodmann,A., Bady,E., Langlhofer,G.,
            Wachter,B., Havlicek,S., Gupta,J., Horn,E., Luningschror,P.,
            Villmann,C., Polat,B., Wischhusen,J., Monoranu,C.M., Kuper,J. and
            Blum,R.
  TITLE     Atypical cellular responses mediated by intracellular constitutive
            active TrkB (NTRK2) kinase domains and a solely intracellular
            NTRK2-fusion oncogene
  JOURNAL   Cancer Gene Ther 31 (9), 1357-1379 (2024)
   PUBMED   39039193
  REMARK    GeneRIF: Atypical cellular responses mediated by intracellular
            constitutive active TrkB (NTRK2) kinase domains and a solely
            intracellular NTRK2-fusion oncogene.
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Zhang,X., Zhang,Y., Yan,H., Yu,H., Zhang,D., Mattay,V.S., Tan,H.Y.
            and Yue,W.
  TITLE     Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2
  JOURNAL   BMC Med 22 (1), 146 (2024)
   PUBMED   38561734
  REMARK    GeneRIF: Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Ikhlef,L., Yassine,M., Chandouri,B., Riviere,L., Naves,T.,
            Dmytruk,N., Gachard,N., Jauberteau,M.O. and Gallet,P.F.
  TITLE     Targeting the NTSR2/TrkB oncogenic pathway in chronic lymphocytic
            leukemia
  JOURNAL   Sci Rep 14 (1), 6084 (2024)
   PUBMED   38480783
  REMARK    GeneRIF: Targeting the NTSR2/TrkB oncogenic pathway in chronic
            lymphocytic leukemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Wang,Y., Liang,J., Xu,B., Yang,J., Wu,Z. and Cheng,L.
  TITLE     TrkB/BDNF signaling pathway and its small molecular agonists in CNS
            injury
  JOURNAL   Life Sci 336, 122282 (2024)
   PUBMED   38008209
  REMARK    GeneRIF: TrkB/BDNF signaling pathway and its small molecular
            agonists in CNS injury.
            Review article
REFERENCE   5  (residues 1 to 537)
  AUTHORS   Luberg,K., Wong,J., Weickert,C.S. and Timmusk,T.
  TITLE     Human TrkB gene: novel alternative transcripts, protein isoforms
            and expression pattern in the prefrontal cerebral cortex during
            postnatal development
  JOURNAL   J Neurochem 113 (4), 952-964 (2010)
   PUBMED   20193039
  REMARK    GeneRIF: Identification of 36 potential TrkB protein isoforms
            suggests high complexity in the synthesis, regulation and function
            of this important neurotrophin receptor emphasizing the need for
            further study of these novel TrkB variants.
REFERENCE   6  (residues 1 to 537)
  AUTHORS   Stoilov,P., Castren,E. and Stamm,S.
  TITLE     Analysis of the human TrkB gene genomic organization reveals novel
            TrkB isoforms, unusual gene length, and splicing mechanism
  JOURNAL   Biochem Biophys Res Commun 290 (3), 1054-1065 (2002)
   PUBMED   11798182
  REMARK    GeneRIF: analysis of TrkB gene reveals novel gene length and
            splicing mechanism
REFERENCE   7  (residues 1 to 537)
  AUTHORS   Haniu,M., Talvenheimo,J., Le,J., Katta,V., Welcher,A. and
            Rohde,M.F.
  TITLE     Extracellular domain of neurotrophin receptor trkB: disulfide
            structure, N-glycosylation sites, and ligand binding
  JOURNAL   Arch Biochem Biophys 322 (1), 256-264 (1995)
   PUBMED   7574684
REFERENCE   8  (residues 1 to 537)
  AUTHORS   Nakagawara,A., Liu,X.G., Ikegaki,N., White,P.S., Yamashiro,D.J.,
            Nycum,L.M., Biegel,J.A. and Brodeur,G.M.
  TITLE     Cloning and chromosomal localization of the human TRK-B tyrosine
            kinase receptor gene (NTRK2)
  JOURNAL   Genomics 25 (2), 538-546 (1995)
   PUBMED   7789988
REFERENCE   9  (residues 1 to 537)
  AUTHORS   Squinto,S.P., Stitt,T.N., Aldrich,T.H., Davis,S., Blanco,S.M.,
            RadzieJewski,C., Glass,D.J., Masiakowski,P., Furth,M.E.,
            Valenzuela,D.M., Distefano,P.S. and Yancopoulos,G.D.
  TITLE     trkB encodes a functional receptor for brain-derived neurotrophic
            factor and neurotrophin-3 but not nerve growth factor
  JOURNAL   Cell 65 (5), 885-893 (1991)
   PUBMED   1710174
REFERENCE   10 (residues 1 to 537)
  AUTHORS   Soppet,D., Escandon,E., Maragos,J., Middlemas,D.S., Reid,S.W.,
            Blair,J., Burton,L.E., Stanton,B.R., Kaplan,D.R., Hunter,T.,
            Nikolics,K. and Parada,L.F.
  TITLE     The neurotrophic factors brain-derived neurotrophic factor and
            neurotrophin-3 are ligands for the trkB tyrosine kinase receptor
  JOURNAL   Cell 65 (5), 895-903 (1991)
   PUBMED   1645620
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390777.13 and AL596132.7.
            
            Summary: This gene encodes a member of the neurotrophic tyrosine
            receptor kinase (NTRK) family. This kinase is a membrane-bound
            receptor that, upon neurotrophin binding, phosphorylates itself and
            members of the MAPK pathway. Signalling through this kinase leads
            to cell differentiation. Mutations in this gene have been
            associated with obesity and mood disorders. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (n), as well as variant e, encodes
            isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.122525.1,
                                           SRR1660809.25330.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..537
                     /product="BDNF/NT-3 growth factors receptor isoform e
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="BDNF/NT-3 growth factors receptor; tyrosine kinase
                     receptor B; BDNF-tropomyosine receptor kinase B;
                     tropomyosin-related kinase B; neurotrophic tyrosine kinase
                     receptor type 2"
                     /calculated_mol_wt=55488
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3697
     Region          31..60
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; pfam01462"
                     /db_xref="CDD:396168"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          92..150
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          92..113
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          96..116
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          116..137
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Region          117..139
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          140..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          151..195
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          205..283
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          214..218
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          227..230
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          245..252
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            254
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          262..268
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          276..279
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          286..379
                     /region_name="IgI_TrkB_d5"
                     /note="Fifth domain (immunoglobulin-like) of Trk receptor
                     TrkB; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05855"
                     /db_xref="CDD:409441"
     Region          286..294
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409441"
     Region          295..298
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409441"
     Region          301..309
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409441"
     Site            310
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409441"
     Region          312..319
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409441"
     Region          322..325
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409441"
     Site            325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          330..335
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409441"
     Site            order(335,349..350,353)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:409441"
     Site            338
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Region          341..349
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409441"
     Region          357..365
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409441"
     Region          368..376
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409441"
     Site            412
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7574684; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     Site            431..454
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Region          455..466
                     /region_name="Interaction with MAPK8IP3/JIP3.
                     /evidence=ECO:0000250|UniProtKB:Q63604"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Region          475..498
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            516
                     /site_type="other"
                     /note="Interaction with SHC1. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16620.1)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P15209; propagated from
                     UniProtKB/Swiss-Prot (Q16620.1)"
     CDS             1..537
                     /gene="NTRK2"
                     /gene_synonym="DEE58; EIEE58; GP145-TrkB; OBHD; trk-B;
                     TRKB"
                     /coded_by="NM_001369538.1:401..2014"
                     /note="isoform e precursor is encoded by transcript
                     variant n"
                     /db_xref="CCDS:CCDS35052.1"
                     /db_xref="GeneID:4915"
                     /db_xref="HGNC:HGNC:8032"
                     /db_xref="MIM:600456"
ORIGIN      
        1 msswirwhgp amarlwgfcw lvvgfwraaf acptsckcsa sriwcsdpsp givafprlep
       61 nsvdpenite ifianqkrle iineddveay vglrnltivd sglkfvahka flknsnlqhi
      121 nftrnkltsl srkhfrhldl selilvgnpf tcscdimwik tlqeaksspd tqdlyclnes
      181 skniplanlq ipncglpsan laapnltvee gksitlscsv agdpvpnmyw dvgnlvskhm
      241 netshtqgsl ritnissdds gkqiscvaen lvgedqdsvn ltvhfaptit flesptsdhh
      301 wcipftvkgn pkpalqwfyn gailneskyi ctkihvtnht eyhgclqldn pthmnngdyt
      361 liakneygkd ekqisahfmg wpgiddganp nypdviyedy gtaandigdt tnrsneipst
      421 dvtdktgreh lsvyavvvia svvgfcllvm lfllklarhs kfgmkgpasv isndddsasp
      481 lhhisngsnt pssseggpda viigmtkipv ienpqyfgit nsqlkpdtwp rgspkta
//
LOCUS       NP_006318                209 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim23 [Homo
            sapiens].
ACCESSION   NP_006318
VERSION     NP_006318.1
DBSOURCE    REFSEQ: accession NM_006327.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Akabane,S., Watanabe,K., Kosako,H., Yamashita,S.I., Nishino,K.,
            Kato,M., Sekine,S., Kanki,T., Matsuda,N., Endo,T. and Oka,T.
  TITLE     TIM23 facilitates PINK1 activation by safeguarding against
            OMA1-mediated degradation in damaged mitochondria
  JOURNAL   Cell Rep 42 (5), 112454 (2023)
   PUBMED   37160114
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Pandey,J., Larson-Casey,J.L., Patil,M.H., Joshi,R., Jiang,C.S.,
            Zhou,Y., He,C. and Carter,A.B.
  TITLE     NOX4-TIM23 interaction regulates NOX4 mitochondrial import and
            metabolic reprogramming
  JOURNAL   J Biol Chem 299 (5), 104695 (2023)
   PUBMED   37044213
  REMARK    GeneRIF: NOX4-TIM23 interaction regulates NOX4 mitochondrial import
            and metabolic reprogramming.
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Barchiesi,A., Bazzani,V., Tolotto,V., Elancheliyan,P.,
            Wasilewski,M., Chacinska,A. and Vascotto,C.
  TITLE     Mitochondrial Oxidative Stress Induces Rapid Intermembrane
            Space/Matrix Translocation of Apurinic/Apyrimidinic Endonuclease 1
            Protein through TIM23 Complex
  JOURNAL   J Mol Biol 432 (24), 166713 (2020)
   PUBMED   33197464
  REMARK    GeneRIF: Mitochondrial Oxidative Stress Induces Rapid Intermembrane
            Space/Matrix Translocation of Apurinic/Apyrimidinic Endonuclease 1
            Protein through TIM23 Complex.
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Muhlenbein,N., Hofmann,S., Rothbauer,U. and Bauer,M.F.
  TITLE     Organization and function of the small Tim complexes acting along
            the import pathway of metabolite carriers into mammalian
            mitochondria
  JOURNAL   J Biol Chem 279 (14), 13540-13546 (2004)
   PUBMED   14726512
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Yamamoto,H., Esaki,M., Kanamori,T., Tamura,Y., Nishikawa,Si. and
            Endo,T.
  TITLE     Tim50 is a subunit of the TIM23 complex that links protein
            translocation across the outer and inner mitochondrial membranes
  JOURNAL   Cell 111 (4), 519-528 (2002)
   PUBMED   12437925
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Moro,F., Sirrenberg,C., Schneider,H.C., Neupert,W. and Brunner,M.
  TITLE     The TIM17.23 preprotein translocase of mitochondria: composition
            and function in protein transport into the matrix
  JOURNAL   EMBO J 18 (13), 3667-3675 (1999)
   PUBMED   10393182
REFERENCE   9  (residues 1 to 209)
  AUTHORS   Bauer,M.F., Gempel,K., Reichert,A.S., Rappold,G.A., Lichtner,P.,
            Gerbitz,K.D., Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     Genetic and structural characterization of the human mitochondrial
            inner membrane translocase
  JOURNAL   J Mol Biol 289 (1), 69-82 (1999)
   PUBMED   10339406
REFERENCE   10 (residues 1 to 209)
  AUTHORS   Prashar,Y. and Weissman,S.M.
  TITLE     Analysis of differential gene expression by display of 3' end
            restriction fragments of cDNAs
  JOURNAL   Proc Natl Acad Sci U S A 93 (2), 659-663 (1996)
   PUBMED   8570611
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC062707.1, BC066951.1 and
            BU619060.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_948409.1.
            
            Summary: The protein encoded by this gene is part of a complex
            located in the inner mitochondrial membrane that mediates the
            transport of transit peptide-containing proteins across the
            membrane. Multiple transcript variants, one protein-coding and
            others not protein-coding, have been found for this gene. [provided
            by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) is the protein-coding
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.189847.1,
                                           SRR5189658.75577.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000580018.4/
                                                  ENSP00000464522.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.22"
     Protein         1..209
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim23"
                     /note="translocase of the inner mitochondrial membrane;
                     translocase of inner mitochondrial membrane 23 homolog"
                     /calculated_mol_wt=21812
     Region          46..191
                     /region_name="3a0801s02tim23"
                     /note="mitochondrial import inner membrane translocase
                     subunit tim23; TIGR00983"
                     /db_xref="CDD:130056"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14925.1)"
     Site            125..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14925.1)"
     Site            181..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14925.1)"
     CDS             1..209
                     /gene="TIMM23"
                     /gene_synonym="TIM23"
                     /coded_by="NM_006327.4:137..766"
                     /db_xref="CCDS:CCDS73091.1"
                     /db_xref="GeneID:100287932"
                     /db_xref="HGNC:HGNC:17312"
                     /db_xref="MIM:605034"
ORIGIN      
        1 meggggsgnk ttgglagffg aggagyshad lagvpltgmn plspylnvdp rylvqdtdef
       61 ilptganktr grfelaffti ggccmtgaaf gamnglrlgl ketqnmawsk prnvqilnmv
      121 trqgalwant lgslallysa fgviiektrg aeddlntvaa gtmtgmlykc tgglrgiarg
      181 gltgltltsl yalynnwehm kgsllqqsl
//
LOCUS       NP_002954                101 aa            linear   PRI 27-APR-2025
DEFINITION  protein S100-A7 [Homo sapiens].
ACCESSION   NP_002954
VERSION     NP_002954.2
DBSOURCE    REFSEQ: accession NM_002963.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Kurtovic,M., Pitesa,N., Conkas,J., Hajpek,H., Vucic,M., Musani,V.,
            Ozretic,P. and Sabol,M.
  TITLE     GLI Transcriptional Targets S100A7 and KRT16 Show Upregulated
            Expression Patterns in Epidermis Overlying the Tumor Mass in
            Melanoma Samples
  JOURNAL   Int J Mol Sci 25 (11), 6084 (2024)
   PUBMED   38892279
  REMARK    GeneRIF: GLI Transcriptional Targets S100A7 and KRT16 Show
            Upregulated Expression Patterns in Epidermis Overlying the Tumor
            Mass in Melanoma Samples.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Stolte,K.N., Danker,K., Witt,M., Ebhardt,H. and Dommisch,H.
  TITLE     Upregulation of psoriasin/S100A7 correlates with clinical severity
            in patients with oral lichen planus
  JOURNAL   Clin Oral Investig 28 (6), 318 (2024)
   PUBMED   38750317
  REMARK    GeneRIF: Upregulation of psoriasin/S100A7 correlates with clinical
            severity in patients with oral lichen planus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Li,Y., Yang,X., Jin,T., Li,Q., Li,X. and Ma,L.
  TITLE     Correlation between S100A7 and immune characteristics, methylation,
            tumor stemness and tumor heterogeneity in pan-cancer and its role
            in chemotherapy resistance in breast cancer
  JOURNAL   Aging (Albany NY) 16 (6), 5581-5600 (2024)
   PUBMED   38499391
  REMARK    GeneRIF: Correlation between S100A7 and immune characteristics,
            methylation, tumor stemness and tumor heterogeneity in pan-cancer
            and its role in chemotherapy resistance in breast cancer.
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Reddi,K.K., Zhang,W., Shahrabi-Farahani,S., Anderson,K.M., Liu,M.,
            Kakhniashvili,D., Wang,X. and Zhang,Y.H.
  TITLE     Tetraspanin CD82 Correlates with and May Regulate S100A7 Expression
            in Oral Cancer
  JOURNAL   Int J Mol Sci 25 (5), 2659 (2024)
   PUBMED   38473906
  REMARK    GeneRIF: Tetraspanin CD82 Correlates with and May Regulate S100A7
            Expression in Oral Cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Wang,H., Liu,J., Tang,R., Hu,J., Liu,M., Wang,J., Zhang,J. and
            Hou,H.
  TITLE     Deciphering the significance of anoikis in bladder cancer and
            systematic analysis of S100A7 as a potential therapeutic target
  JOURNAL   Eur J Med Res 29 (1), 52 (2024)
   PUBMED   38217031
  REMARK    GeneRIF: Deciphering the significance of anoikis in bladder cancer
            and systematic analysis of S100A7 as a potential therapeutic
            target.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Hattori,F., Kiatsurayanon,C., Okumura,K., Ogawa,H., Ikeda,S.,
            Okamoto,K. and Niyonsaba,F.
  TITLE     The antimicrobial protein S100A7/psoriasin enhances the expression
            of keratinocyte differentiation markers and strengthens the skin's
            tight junction barrier
  JOURNAL   Br J Dermatol 171 (4), 742-753 (2014)
   PUBMED   24842328
  REMARK    GeneRIF: The antimicrobial peptide psoriasin has immunoregulatory
            activities and is involved in skin innate immunity.
REFERENCE   7  (residues 1 to 101)
  AUTHORS   Schafer,B.W., Wicki,R., Engelkamp,D., Mattei,M.G. and Heizmann,C.W.
  TITLE     Isolation of a YAC clone covering a cluster of nine S100 genes on
            human chromosome 1q21: rationale for a new nomenclature of the S100
            calcium-binding protein family
  JOURNAL   Genomics 25 (3), 638-643 (1995)
   PUBMED   7759097
REFERENCE   8  (residues 1 to 101)
  AUTHORS   Hoffmann,H.J., Olsen,E., Etzerodt,M., Madsen,P., Thogersen,H.C.,
            Kruse,T. and Celis,J.E.
  TITLE     Psoriasin binds calcium and is upregulated by calcium to levels
            that resemble those observed in normal skin
  JOURNAL   J Invest Dermatol 103 (3), 370-375 (1994)
   PUBMED   8077703
REFERENCE   9  (residues 1 to 101)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 101)
  AUTHORS   Madsen,P., Rasmussen,H.H., Leffers,H., Honore,B., Dejgaard,K.,
            Olsen,E., Kiil,J., Walbum,E., Andersen,A.H., Basse,B. et al.
  TITLE     Molecular cloning, occurrence, and expression of a novel partially
            secreted protein 'psoriasin' that is highly up-regulated in
            psoriatic skin
  JOURNAL   J Invest Dermatol 97 (4), 701-712 (1991)
   PUBMED   1940442
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF090388.1, AW238300.1 and
            BX476368.1.
            
            On Sep 22, 2006 this sequence version replaced NP_002954.1.
            
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21. This protein differs from
            the other S100 proteins of known structure in its lack of calcium
            binding ability in one EF-hand at the N-terminus. The protein is
            overexpressed in hyperproliferative skin diseases, exhibits
            antimicrobial activities against bacteria and induces
            immunomodulatory activities. [provided by RefSeq, Nov 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX280362.1, BX476368.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000368723.4/
                                                  ENSP00000357712.3
            Protein has antimicrobial activity :: PMID: 24842328
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..101
                     /product="protein S100-A7"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     24842328]"
                     /note="psoriasin 1"
                     /calculated_mol_wt=11340
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:8526920; propagated from
                     UniProtKB/Swiss-Prot (P31151.4)"
     Region          4..90
                     /region_name="S-100"
                     /note="S-100 domain, which represents the largest family
                     within the superfamily of proteins carrying the Ca-binding
                     EF-hand motif. Note that this S-100 hierarchy contains
                     only S-100 EF-hand domains, other EF-hands have been
                     modeled separately. S100 proteins are...; cd00213"
                     /db_xref="CDD:238131"
     Site            order(4..21,25..26,35..36,38..40,70..73,75..76,78..81,
                     83..90)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238131"
     Site            order(21,26,31..32,63,65,67,69,71,74)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238131"
     Region          63..74
                     /region_name="calcium binding region"
     CDS             1..101
                     /gene="S100A7"
                     /gene_synonym="PSOR1; S100A7c"
                     /coded_by="NM_002963.4:62..367"
                     /db_xref="CCDS:CCDS1039.1"
                     /db_xref="GeneID:6278"
                     /db_xref="HGNC:HGNC:10497"
                     /db_xref="MIM:600353"
ORIGIN      
        1 msntqaersi igmidmfhky trrddkiekp slltmmkenf pnflsacdkk gtnyladvfe
       61 kkdknedkki dfseflsllg diatdyhkqs hgaapcsggs q
//
LOCUS       NP_005048                538 aa            linear   PRI 27-APR-2025
DEFINITION  retinoblastoma-binding protein 5 isoform 1 [Homo sapiens].
ACCESSION   NP_005048
VERSION     NP_005048.2
DBSOURCE    REFSEQ: accession NM_005057.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Xie,H., Zhao,J., Wan,J., Zhao,J., Wang,Q., Yang,X., Yang,W., Lin,P.
            and Yu,X.
  TITLE     Long non-coding RNA AC245100.4 promotes prostate cancer
            tumorigenesis via the microRNA-145-5p/RBBP5 axis
  JOURNAL   Oncol Rep 45 (2), 619-629 (2021)
   PUBMED   33416179
  REMARK    GeneRIF: Long noncoding RNA AC245100.4 promotes prostate cancer
            tumorigenesis via the microRNA1455p/RBBP5 axis.
            Erratum:[Oncol Rep. 2023 Mar;49(3):62. doi: 10.3892/or.2023.8499.
            PMID: 36799194]
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Patel,A., Dharmarajan,V., Vought,V.E. and Cosgrove,M.S.
  TITLE     On the mechanism of multiple lysine methylation by the human mixed
            lineage leukemia protein-1 (MLL1) core complex
  JOURNAL   J Biol Chem 284 (36), 24242-24256 (2009)
   PUBMED   19556245
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Southall,S.M., Wong,P.S., Odho,Z., Roe,S.M. and Wilson,J.R.
  TITLE     Structural basis for the requirement of additional factors for MLL1
            SET domain activity and recognition of epigenetic marks
  JOURNAL   Mol Cell 33 (2), 181-191 (2009)
   PUBMED   19187761
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Lee,J.H., Tate,C.M., You,J.S. and Skalnik,D.G.
  TITLE     Identification and characterization of the human Set1B histone
            H3-Lys4 methyltransferase complex
  JOURNAL   J Biol Chem 282 (18), 13419-13428 (2007)
   PUBMED   17355966
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Scacheri,P.C., Davis,S., Odom,D.T., Crawford,G.E., Perkins,S.,
            Halawi,M.J., Agarwal,S.K., Marx,S.J., Spiegel,A.M., Meltzer,P.S.
            and Collins,F.S.
  TITLE     Genome-wide analysis of menin binding provides insights into MEN1
            tumorigenesis
  JOURNAL   PLoS Genet 2 (4), e51 (2006)
   PUBMED   16604156
  REMARK    GeneRIF: analysis of menin's role as a tumor suppressor and binding
            sites of Rbbp5 and MLL1
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Goo,Y.H., Sohn,Y.C., Kim,D.H., Kim,S.W., Kang,M.J., Jung,D.J.,
            Kwak,E., Barlev,N.A., Berger,S.L., Chow,V.T., Roeder,R.G.,
            Azorsa,D.O., Meltzer,P.S., Suh,P.G., Song,E.J., Lee,K.J., Lee,Y.C.
            and Lee,J.W.
  TITLE     Activating signal cointegrator 2 belongs to a novel steady-state
            complex that contains a subset of trithorax group proteins
  JOURNAL   Mol Cell Biol 23 (1), 140-149 (2003)
   PUBMED   12482968
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Saijo,M., Sakai,Y., Kishino,T., Niikawa,N., Matsuura,Y., Morino,K.,
            Tamai,K. and Taya,Y.
  TITLE     Molecular cloning of a human protein that binds to the
            retinoblastoma protein and chromosomal mapping
  JOURNAL   Genomics 27 (3), 511-519 (1995)
   PUBMED   7558034
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA797022.1, BC075059.2,
            AL583832.14 and BQ020418.1.
            
            On Oct 4, 2004 this sequence version replaced NP_005048.1.
            
            Summary: This gene encodes a ubiquitously expressed nuclear protein
            which belongs to a highly conserved subfamily of WD-repeat
            proteins. The encoded protein binds directly to retinoblastoma
            protein, which regulates cell proliferation. It interacts
            preferentially with the underphosphorylated retinoblastoma protein
            via the E1A-binding pocket B. Three alternatively spliced
            transcript variants that encode different protein isoforms have
            been described for this gene. [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053856.1, X85134.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264515.11/ ENSP00000264515.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..538
                     /product="retinoblastoma-binding protein 5 isoform 1"
                     /note="SWD1, Set1c WD40 repeat protein, homolog; RBBP-5;
                     retinoblastoma-binding protein RBQ-3;
                     retinoblastoma-binding protein 5"
                     /calculated_mol_wt=59022
     Region          22..63
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          29..64
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <31..321
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          64..103
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          70..106
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          154..190
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          196..235
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          201..246
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          249..291
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7558034; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Region          254..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          293..331
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          298..321
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          330..366
                     /region_name="Interaction with ASH2L.
                     /evidence=ECO:0000269|PubMed:21220120"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          344..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Region          371..380
                     /region_name="Interaction with WDR5.
                     /evidence=ECO:0000269|PubMed:21220120"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Region          408..538
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7558034; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     CDS             1..538
                     /gene="RBBP5"
                     /gene_synonym="RBQ3; SWD1"
                     /coded_by="NM_005057.4:106..1722"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30983.1"
                     /db_xref="GeneID:5929"
                     /db_xref="HGNC:HGNC:9888"
                     /db_xref="MIM:600697"
ORIGIN      
        1 mnlellesfg qnypeeadgt ldcismaltc tfnrwgtlla vgcndgrivi wdfltrgiak
       61 iisahihpvc slcwsrdghk lvsastdniv sqwdvlsgdc dqrfrfpspi lkvqyhprdq
      121 nkvlvcpmks apvmltlsds khvvlpvddd sdlnvvasfd rrgeyiytgn akgkilvlkt
      181 dsqdlvasfr vttgtsntta iksiefarkg scflintadr iirvydgrei ltcgrdgepe
      241 pmqklqdlvn rtpwkkccfs gdgeyivags arqhalyiwe ksignlvkil hgtrgellld
      301 vawhpvrpii asissgvvsi waqnqvenws afapdfkeld enveyeeres efdiededks
      361 epeqtgadaa edeevdvtsv dpiaafcssd eeledskall ylpiapeved peenpygppp
      421 davqtslmde gassekkrqs sadgsqppkk kpkttnielq gvpndevhpl lgvkgdgksk
      481 kkqagrpkgs kgkekdspfk pklykgdrgl plegsakgkv qaelsqplta ggaisell
//
LOCUS       NP_067650                167 aa            linear   PRI 27-APR-2025
DEFINITION  novel acetylcholine receptor chaperone [Homo sapiens].
ACCESSION   NP_067650
VERSION     NP_067650.1
DBSOURCE    REFSEQ: accession NM_021637.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Wu,M., Liu,C.Z., Barrall,E.A., Rissman,R.A. and Joiner,W.J.
  TITLE     Unbalanced Regulation of alpha7 nAChRs by Ly6h and NACHO
            Contributes to Neurotoxicity in Alzheimer's Disease
  JOURNAL   J Neurosci 41 (41), 8461-8474 (2021)
   PUBMED   34446574
  REMARK    GeneRIF: Unbalanced Regulation of alpha7 nAChRs by Ly6h and NACHO
            Contributes to Neurotoxicity in Alzheimer's Disease.
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Mazzaferro,S., Whiteman,S.T., Alcaino,C., Beyder,A. and Sine,S.M.
  TITLE     NACHO and 14-3-3 promote expression of distinct subunit
            stoichiometries of the alpha4beta2 acetylcholine receptor
  JOURNAL   Cell Mol Life Sci 78 (4), 1565-1575 (2021)
   PUBMED   32676916
  REMARK    GeneRIF: NACHO and 14-3-3 promote expression of distinct subunit
            stoichiometries of the alpha4beta2 acetylcholine receptor.
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Kweon,H.J., Gu,S., Witham,E., Dhara,M., Yu,H., Mandon,E.D.,
            Jawhari,A. and Bredt,D.S.
  TITLE     NACHO Engages N-Glycosylation ER Chaperone Pathways for alpha7
            Nicotinic Receptor Assembly
  JOURNAL   Cell Rep 32 (6), 108025 (2020)
   PUBMED   32783947
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 167)
  AUTHORS   Deshpande,A., Vinayakamoorthy,R.M., Garg,B.K., Thummapudi,J.P.,
            Oza,G., Adhikari,K., Agarwal,A., Dalvi,P., Iyer,S., Thulasi
            Raman,S., Ramesh,V., Rameshbabu,A., Rezvaya,A., Sukumaran,S.,
            Swaminathan,S., Tilak,B., Wang,Z., Tran,P.V. and Loring,R.H.
  TITLE     Why Does Knocking Out NACHO, But Not RIC3, Completely Block
            Expression of alpha7 Nicotinic Receptors in Mouse Brain?
  JOURNAL   Biomolecules 10 (3), 470 (2020)
   PUBMED   32204458
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 167)
  AUTHORS   Matta,J.A., Gu,S., Davini,W.B., Lord,B., Siuda,E.R.,
            Harrington,A.W. and Bredt,D.S.
  TITLE     NACHO Mediates Nicotinic Acetylcholine Receptor Function throughout
            the Brain
  JOURNAL   Cell Rep 19 (4), 688-696 (2017)
   PUBMED   28445721
REFERENCE   7  (residues 1 to 167)
  AUTHORS   Rex,E.B., Shukla,N., Gu,S., Bredt,D. and DiSepio,D.
  TITLE     A Genome-Wide Arrayed cDNA Screen to Identify Functional Modulators
            of alpha7 Nicotinic Acetylcholine Receptors
  JOURNAL   SLAS Discov 22 (2), 155-165 (2017)
   PUBMED   27789755
REFERENCE   8  (residues 1 to 167)
  AUTHORS   Gu,S., Matta,J.A., Lord,B., Harrington,A.W., Sutton,S.W.,
            Davini,W.B. and Bredt,D.S.
  TITLE     Brain alpha7 Nicotinic Acetylcholine Receptor Assembly Requires
            NACHO
  JOURNAL   Neuron 89 (5), 948-955 (2016)
   PUBMED   26875622
REFERENCE   9  (residues 1 to 167)
  AUTHORS   Ross,M.T., Grafham,D.V., Coffey,A.J., Scherer,S., McLay,K.,
            Muzny,D., Platzer,M., Howell,G.R., Burrows,C., Bird,C.P.,
            Frankish,A., Lovell,F.L., Howe,K.L., Ashurst,J.L., Fulton,R.S.,
            Sudbrak,R., Wen,G., Jones,M.C., Hurles,M.E., Andrews,T.D.,
            Scott,C.E., Searle,S., Ramser,J., Whittaker,A., Deadman,R.,
            Carter,N.P., Hunt,S.E., Chen,R., Cree,A., Gunaratne,P., Havlak,P.,
            Hodgson,A., Metzker,M.L., Richards,S., Scott,G., Steffen,D.,
            Sodergren,E., Wheeler,D.A., Worley,K.C., Ainscough,R.,
            Ambrose,K.D., Ansari-Lari,M.A., Aradhya,S., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Ballabio,A., Banerjee,R., Barker,G.E.,
            Barlow,K.F., Barrett,I.P., Bates,K.N., Beare,D.M., Beasley,H.,
            Beasley,O., Beck,A., Bethel,G., Blechschmidt,K., Brady,N.,
            Bray-Allen,S., Bridgeman,A.M., Brown,A.J., Brown,M.J., Bonnin,D.,
            Bruford,E.A., Buhay,C., Burch,P., Burford,D., Burgess,J.,
            Burrill,W., Burton,J., Bye,J.M., Carder,C., Carrel,L., Chako,J.,
            Chapman,J.C., Chavez,D., Chen,E., Chen,G., Chen,Y., Chen,Z.,
            Chinault,C., Ciccodicola,A., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S., Clerc-Blankenburg,K., Clifford,K., Cobley,V., Cole,C.G.,
            Conquer,J.S., Corby,N., Connor,R.E., David,R., Davies,J., Davis,C.,
            Davis,J., Delgado,O., Deshazo,D., Dhami,P., Ding,Y., Dinh,H.,
            Dodsworth,S., Draper,H., Dugan-Rocha,S., Dunham,A., Dunn,M.,
            Durbin,K.J., Dutta,I., Eades,T., Ellwood,M., Emery-Cohen,A.,
            Errington,H., Evans,K.L., Faulkner,L., Francis,F., Frankland,J.,
            Fraser,A.E., Galgoczy,P., Gilbert,J., Gill,R., Glockner,G.,
            Gregory,S.G., Gribble,S., Griffiths,C., Grocock,R., Gu,Y.,
            Gwilliam,R., Hamilton,C., Hart,E.A., Hawes,A., Heath,P.D.,
            Heitmann,K., Hennig,S., Hernandez,J., Hinzmann,B., Ho,S., Hoffs,M.,
            Howden,P.J., Huckle,E.J., Hume,J., Hunt,P.J., Hunt,A.R.,
            Isherwood,J., Jacob,L., Johnson,D., Jones,S., de Jong,P.J.,
            Joseph,S.S., Keenan,S., Kelly,S., Kershaw,J.K., Khan,Z.,
            Kioschis,P., Klages,S., Knights,A.J., Kosiura,A., Kovar-Smith,C.,
            Laird,G.K., Langford,C., Lawlor,S., Leversha,M., Lewis,L., Liu,W.,
            Lloyd,C., Lloyd,D.M., Loulseged,H., Loveland,J.E., Lovell,J.D.,
            Lozado,R., Lu,J., Lyne,R., Ma,J., Maheshwari,M., Matthews,L.H.,
            McDowall,J., McLaren,S., McMurray,A., Meidl,P., Meitinger,T.,
            Milne,S., Miner,G., Mistry,S.L., Morgan,M., Morris,S., Muller,I.,
            Mullikin,J.C., Nguyen,N., Nordsiek,G., Nyakatura,G., O'Dell,C.N.,
            Okwuonu,G., Palmer,S., Pandian,R., Parker,D., Parrish,J.,
            Pasternak,S., Patel,D., Pearce,A.V., Pearson,D.M., Pelan,S.E.,
            Perez,L., Porter,K.M., Ramsey,Y., Reichwald,K., Rhodes,S.,
            Ridler,K.A., Schlessinger,D., Schueler,M.G., Sehra,H.K.,
            Shaw-Smith,C., Shen,H., Sheridan,E.M., Shownkeen,R., Skuce,C.D.,
            Smith,M.L., Sotheran,E.C., Steingruber,H.E., Steward,C.A.,
            Storey,R., Swann,R.M., Swarbreck,D., Tabor,P.E., Taudien,S.,
            Taylor,T., Teague,B., Thomas,K., Thorpe,A., Timms,K., Tracey,A.,
            Trevanion,S., Tromans,A.C., d'Urso,M., Verduzco,D., Villasana,D.,
            Waldron,L., Wall,M., Wang,Q., Warren,J., Warry,G.L., Wei,X.,
            West,A., Whitehead,S.L., Whiteley,M.N., Wilkinson,J.E.,
            Willey,D.L., Williams,G., Williams,L., Williamson,A.,
            Williamson,H., Wilming,L., Woodmansey,R.L., Wray,P.W., Yen,J.,
            Zhang,J., Zhou,J., Zoghbi,H., Zorilla,S., Buck,D., Reinhardt,R.,
            Poustka,A., Rosenthal,A., Lehrach,H., Meindl,A., Minx,P.J.,
            Hillier,L.W., Willard,H.F., Wilson,R.K., Waterston,R.H., Rice,C.M.,
            Vaudin,M., Coulson,A., Nelson,D.L., Weinstock,G., Sulston,J.E.,
            Durbin,R., Hubbard,T., Gibbs,R.A., Beck,S., Rogers,J. and
            Bentley,D.R.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL109952.15, BC078658.1 and BU736545.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The extent of this RefSeq transcript is based on
            transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223240.1, AK024146.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372930.5/ ENSP00000362021.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..167
                     /product="novel acetylcholine receptor chaperone"
                     /note="transmembrane protein 35; nAChR regulator;
                     nicotinic acetylcholine receptor regulator"
                     /calculated_mol_wt=18309
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53FP2.2)"
     Region          43..54
                     /region_name="Interaction with NGFR.
                     /evidence=ECO:0000250|UniProtKB:Q6JAM9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53FP2.2)"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53FP2.2)"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53FP2.2)"
     Site            115..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53FP2.2)"
     Region          136..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53FP2.2)"
     CDS             1..167
                     /gene="TMEM35A"
                     /gene_synonym="NACHO; TMEM35; TUF-1"
                     /coded_by="NM_021637.3:125..628"
                     /db_xref="CCDS:CCDS14478.1"
                     /db_xref="GeneID:59353"
                     /db_xref="HGNC:HGNC:25864"
ORIGIN      
        1 masprtvtiv alsvalglff vfmgtikltp rlskdaysem krayksyvra lpllkkmgin
       61 sillrksiga levacgivmt lvpgrpkdva nffllllvla vlffhqlvgd plkryahalv
      121 fgilltcrll iarkpedrss ekkplpgnae eqpslyekap qgkvkvs
//
LOCUS       NP_061973                467 aa            linear   PRI 27-APR-2025
DEFINITION  DNA methyltransferase 1-associated protein 1 [Homo sapiens].
ACCESSION   NP_061973
VERSION     NP_061973.1
DBSOURCE    REFSEQ: accession NM_019100.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Li,J., Hu,B., Wang,T., Huang,W., Ma,C., Zhao,Q., Zhuo,L., Zhang,T.
            and Jiang,Y.
  TITLE     C-Src confers resistance to mitotic stress through inhibition
            DMAP1/Bub3 complex formation in pancreatic cancer
  JOURNAL   Mol Cancer 17 (1), 174 (2018)
   PUBMED   30553276
  REMARK    GeneRIF: Findings reveal a regulatory role of Bub3 in
            DMAP1-mediated DNA methylation upon mitotic stress.
            Erratum:[Mol Cancer. 2019 Nov 29;18(1):172. doi:
            10.1186/s12943-019-1067-2. PMID: 31783872]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Wang,K., Liang,Q., Li,X., Tsoi,H., Zhang,J., Wang,H., Go,M.Y.,
            Chiu,P.W., Ng,E.K., Sung,J.J. and Yu,J.
  TITLE     MDGA2 is a novel tumour suppressor cooperating with DMAP1 in
            gastric cancer and is associated with disease outcome
  JOURNAL   Gut 65 (10), 1619-1631 (2016)
   PUBMED   26206665
  REMARK    GeneRIF: A novel tumour suppressor gene, MDGA2, which is frequently
            inactivated by promoter methylation in Gastric cancer, exerts a
            tumour suppressive function by cooperating with DMAP1 to activate
            the p53/p21 signalling cascade.
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Jacquet,K., Fradet-Turcotte,A., Avvakumov,N., Lambert,J.P.,
            Roques,C., Pandita,R.K., Paquet,E., Herst,P., Gingras,A.C.,
            Pandita,T.K., Legube,G., Doyon,Y., Durocher,D. and Cote,J.
  TITLE     The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1
            through Direct H4K20me Binding and H2AK15 Acetylation
  JOURNAL   Mol Cell 62 (3), 409-421 (2016)
   PUBMED   27153538
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Liu,Z. and Fisher,R.A.
  TITLE     RGS6 interacts with DMAP1 and DNMT1 and inhibits DMAP1
            transcriptional repressor activity
  JOURNAL   J Biol Chem 279 (14), 14120-14128 (2004)
   PUBMED   14734556
  REMARK    GeneRIF: RGS6 inhibited the transcriptional repressor activity of
            DMAP1.
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Xin,H., Yoon,H.G., Singh,P.B., Wong,J. and Qin,J.
  TITLE     Components of a pathway maintaining histone modification and
            heterochromatin protein 1 binding at the pericentric
            heterochromatin in Mammalian cells
  JOURNAL   J Biol Chem 279 (10), 9539-9546 (2004)
   PUBMED   14665632
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Cai,Y., Jin,J., Tomomori-Sato,C., Sato,S., Sorokina,I.,
            Parmely,T.J., Conaway,R.C. and Conaway,J.W.
  TITLE     Identification of new subunits of the multiprotein mammalian
            TRRAP/TIP60-containing histone acetyltransferase complex
  JOURNAL   J Biol Chem 278 (44), 42733-42736 (2003)
   PUBMED   12963728
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Yang,C.S. and Weiner,H.
  TITLE     Yeast two-hybrid screening identifies binding partners of human
            Tom34 that have ATPase activity and form a complex with Tom34 in
            the cytosol
  JOURNAL   Arch Biochem Biophys 400 (1), 105-110 (2002)
   PUBMED   11913976
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Rountree,M.R., Bachman,K.E. and Baylin,S.B.
  TITLE     DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex
            at replication foci
  JOURNAL   Nat Genet 25 (3), 269-277 (2000)
   PUBMED   10888872
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB123593.1, BC008053.2 and
            BU616029.1.
            
            Summary: This gene encodes a subunit of several, distinct complexes
            involved in the repression or activation of transcription. The
            encoded protein can independently repress transcription and is
            targeted to replication foci throughout S phase by interacting
            directly with the N-terminus of DNA methyltransferase 1. During
            late S phase, histone deacetylase 2 is added to this complex,
            providing a means to deacetylate histones in transcriptionally
            inactive heterochromatin following replication. The encoded protein
            is also a component of the nucleosome acetyltransferase of H4
            complex and interacts with the transcriptional corepressor tumor
            susceptibility gene 101 and the pro-apoptotic death-associated
            protein 6, among others. Alternatively spliced transcript variants
            encoding the same protein have been described. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1086660.1,
                                           SRR3476690.1166588.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372289.7/ ENSP00000361363.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..467
                     /product="DNA methyltransferase 1-associated protein 1"
                     /note="DNMT1 associated protein 1"
                     /calculated_mol_wt=52862
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPF5.1)"
     Region          124..203
                     /region_name="SANT_DAMP1_like"
                     /note="SANT/Myb-like domain of DAMP1; pfam16282"
                     /db_xref="CDD:465084"
     Region          243..402
                     /region_name="DMAP1"
                     /note="DNA methyltransferase 1-associated protein 1
                     (DMAP1); pfam05499"
                     /db_xref="CDD:398903"
     Region          258..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPF5.1)"
     Region          404..467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPF5.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NPF5.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NPF5.1)"
     CDS             1..467
                     /gene="DMAP1"
                     /gene_synonym="DNMAP1; DNMTAP1; EAF2; MEAF2; SWC4"
                     /coded_by="NM_019100.5:284..1687"
                     /db_xref="CCDS:CCDS509.1"
                     /db_xref="GeneID:55929"
                     /db_xref="HGNC:HGNC:18291"
                     /db_xref="MIM:605077"
ORIGIN      
        1 matgadvrdi lelggpegda asgtiskkdi inpdkkkskk ssetltfkrp egmhrevyal
       61 lysdkkdapp llpsdtgqgy rtvkaklgsk kvrpwkwmpf tnparkdgam ffhwrraaee
      121 gkdypfarfn ktvqvpvyse qeyqlylhdd awtkaetdhl fdlsrrfdlr fvvihdrydh
      181 qqfkkrsved lkeryyhica klanvravpg tdlkipvfda gherrrkeql erlynrtpeq
      241 vaeeeyllqe lrkiearkke rekrsqdlqk litaadttae qrrterkapk kklpqkkeae
      301 kpavpetagi kfpdfksagv tlrsqrmklp ssvgqkkika leqmllelgv elsptpteel
      361 vhmfnelrsd lvllyelkqa canceyelqm lrhrhealar agvlggpatp asgpgpasae
      421 pavtepglgp dpkdtiidvv gapltpnsrk rresasssss vkkakkp
//
LOCUS       NP_001353469             499 aa            linear   PRI 27-APR-2025
DEFINITION  inositol 1,4,5-triphosphate receptor associated 2 isoform a [Homo
            sapiens].
ACCESSION   NP_001353469
VERSION     NP_001353469.1
DBSOURCE    REFSEQ: accession NM_001366540.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Okumura,W., Tadahira,K., Kozono,T., Tamura-Nakano,M., Sato,H.,
            Matsui,H., Dohi,T., Rohrer,J., Tonozuka,T. and Nishikawa,A.
  TITLE     Jaw1/LRMP is associated with the maintenance of Golgi ribbon
            structure
  JOURNAL   J Biochem 173 (5), 383-392 (2023)
   PUBMED   36689741
  REMARK    GeneRIF: Jaw1/LRMP is associated with the maintenance of Golgi
            ribbon structure.
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Okumura,W., Kozono,T., Sato,H., Matsui,H., Takagi,T., Tonozuka,T.
            and Nishikawa,A.
  TITLE     Jaw1/LRMP increases Ca2+ influx upon GPCR stimulation with
            heterogeneous effect on the activity of each ITPR subtype
  JOURNAL   Sci Rep 12 (1), 9476 (2022)
   PUBMED   35676525
  REMARK    GeneRIF: Jaw1/LRMP increases Ca(2+) influx upon GPCR stimulation
            with heterogeneous effect on the activity of each ITPR subtype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Bataille,P., Michaud,V., Robert,M.P., Bekel,L., Leclerc-Mercier,S.,
            Harroche,A., Celerier,C., Lasseaux,E., Borgel,D.,
            Bremond-Gignac,D., Bodemer,C., Arveiler,B. and Hadj-Rabia,S.
  TITLE     Clinical variability and probable founder effect in oculocutaneous
            albinism type 7
  JOURNAL   Clin Genet 97 (3), 527-528 (2020)
   PUBMED   31694064
  REMARK    GeneRIF: Clinical variability and probable founder effect in
            oculocutaneous albinism type 7.
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Eijgelsheim,M., Newton-Cheh,C., Sotoodehnia,N., de Bakker,P.I.,
            Muller,M., Morrison,A.C., Smith,A.V., Isaacs,A., Sanna,S., Dorr,M.,
            Navarro,P., Fuchsberger,C., Nolte,I.M., de Geus,E.J., Estrada,K.,
            Hwang,S.J., Bis,J.C., Ruckert,I.M., Alonso,A., Launer,L.J.,
            Hottenga,J.J., Rivadeneira,F., Noseworthy,P.A., Rice,K.M., Perz,S.,
            Arking,D.E., Spector,T.D., Kors,J.A., Aulchenko,Y.S., Tarasov,K.V.,
            Homuth,G., Wild,S.H., Marroni,F., Gieger,C., Licht,C.M.,
            Prineas,R.J., Hofman,A., Rotter,J.I., Hicks,A.A., Ernst,F.,
            Najjar,S.S., Wright,A.F., Peters,A., Fox,E.R., Oostra,B.A.,
            Kroemer,H.K., Couper,D., Volzke,H., Campbell,H., Meitinger,T.,
            Uda,M., Witteman,J.C., Psaty,B.M., Wichmann,H.E., Harris,T.B.,
            Kaab,S., Siscovick,D.S., Jamshidi,Y., Uitterlinden,A.G.,
            Folsom,A.R., Larson,M.G., Wilson,J.F., Penninx,B.W., Snieder,H.,
            Pramstaller,P.P., van Duijn,C.M., Lakatta,E.G., Felix,S.B.,
            Gudnason,V., Pfeufer,A., Heckbert,S.R., Stricker,B.H.,
            Boerwinkle,E. and O'Donnell,C.J.
  TITLE     Genome-wide association analysis identifies multiple loci related
            to resting heart rate
  JOURNAL   Hum Mol Genet 19 (19), 3885-3894 (2010)
   PUBMED   20639392
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Kohno,T., Kunitoh,H., Suzuki,K., Yamamoto,S., Kuchiba,A.,
            Matsuno,Y., Yanagitani,N. and Yokota,J.
  TITLE     Association of KRAS polymorphisms with risk for lung adenocarcinoma
            accompanied by atypical adenomatous hyperplasias
  JOURNAL   Carcinogenesis 29 (5), 957-963 (2008)
   PUBMED   18299280
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Manenti,G., Galbiati,F., Pettinicchio,A., Spinola,M., Piconese,S.,
            Leoni,V.P., Conti,B., Ravagnani,F., Incarbone,M., Pastorino,U. and
            Dragani,T.A.
  TITLE     A V141L polymorphism of the human LRMP gene is associated with
            survival of lung cancer patients
  JOURNAL   Carcinogenesis 27 (7), 1386-1390 (2006)
   PUBMED   16410263
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Snyder,H.L., Bacik,I., Bennink,J.R., Kearns,G., Behrens,T.W.,
            Bachi,T., Orlowski,M. and Yewdell,J.W.
  TITLE     Two novel routes of transporter associated with antigen processing
            (TAP)-independent major histocompatibility complex class I antigen
            processing
  JOURNAL   J Exp Med 186 (7), 1087-1098 (1997)
   PUBMED   9314557
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Behrens,T.W., Kearns,G.M., Rivard,J.J., Bernstein,H.D.,
            Yewdell,J.W. and Staudt,L.M.
  TITLE     Carboxyl-terminal targeting and novel post-translational processing
            of JAW1, a lymphoid protein of the endoplasmic reticulum
  JOURNAL   J Biol Chem 271 (38), 23528-23534 (1996)
   PUBMED   8798562
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Behrens,T.W., Jagadeesh,J., Scherle,P., Kearns,G., Yewdell,J. and
            Staudt,L.M.
  TITLE     Jaw1, A lymphoid-restricted membrane protein localized to the
            endoplasmic reticulum
  JOURNAL   J Immunol 153 (2), 682-690 (1994)
   PUBMED   8021504
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC023510.16.
            
            Summary: The protein encode dby this gene is expressed in a
            developmentally regulated manner in lymphoid cell lines and
            tissues. The protein is localized to the cytoplasmic face of the
            endoplasmic reticulum. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.222479.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..499
                     /product="inositol 1,4,5-triphosphate receptor associated
                     2 isoform a"
                     /note="protein Jaw1; lymphoid restricted membrane protein"
                     /calculated_mol_wt=56082
     Region          4..499
                     /region_name="MRVI1"
                     /note="MRVI1 protein; pfam05781"
                     /db_xref="CDD:461738"
     CDS             1..499
                     /gene="IRAG2"
                     /gene_synonym="JAW1; LRMP"
                     /coded_by="NM_001366540.1:670..2169"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS8701.1"
                     /db_xref="GeneID:4033"
                     /db_xref="HGNC:HGNC:6690"
                     /db_xref="MIM:602003"
ORIGIN      
        1 mnddpsmeen gvervcpesl lqsreysslp lprhtsstdg titssdpgle ilnmascdld
       61 rnslckkeed trsasptiea qgtspahdni afqdstskdk tilnleakee petieehkke
      121 hasgdsvvsp lpvttvksvn lrqsentsan ekeveaeflr lslgfkcdwf tlekrvklee
      181 rsrdlaeenl kkeitnclkl lesltplced dnqaqeiikk leksikflsq caarvasrae
      241 mlgainqesr vskavevmiq hvenlkrmya kehaeleelk qvllqnersf npleddddcq
      301 ikkrsaslns kpsslrrvti aslprnigna gmvagmennd rfsrrssswr ilgskqsehr
      361 pslprfisty swadaeeekc elktkddsep sgeetvertr kpslsekknn pskwdvssvy
      421 dtiaswatnl kssirkanka lwlsiafivl faalmsfltg qlfqksvdaa ptqqedswts
      481 lehilwpftr lrhngpppv
//
LOCUS       NP_001236934             186 aa            linear   PLN 27-APR-2025
DEFINITION  pterocarpan synthase 1 precursor [Glycine max].
ACCESSION   NP_001236934
VERSION     NP_001236934.2
DBSOURCE    REFSEQ: accession NM_001250005.4
KEYWORDS    RefSeq.
SOURCE      Glycine max (soybean)
  ORGANISM  Glycine max
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
            Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50
            kb inversion clade; NPAAA clade; indigoferoid/millettioid clade;
            Phaseoleae; Glycine; Glycine subgen. Soja.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Jahan,M.A., Harris,B., Lowery,M., Coburn,K., Infante,A.M.,
            Percifield,R.J., Ammer,A.G. and Kovinich,N.
  TITLE     The NAC family transcription factor GmNAC42-1 regulates
            biosynthesis of the anticancer and neuroprotective glyceollins in
            soybean
  JOURNAL   BMC Genomics 20 (1), 149 (2019)
   PUBMED   30786857
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Uchida,K., Akashi,T. and Aoki,T.
  TITLE     The Missing Link in Leguminous Pterocarpan Biosynthesis is a
            Dirigent Domain-Containing Protein with Isoflavanol Dehydratase
            Activity
  JOURNAL   Plant Cell Physiol 58 (2), 398-408 (2017)
   PUBMED   28394400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            ACUP04001205.1.
            
            On Mar 28, 2018 this sequence version replaced NP_001236934.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BT091561.1, EV272503.1 [ECO:0000345]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Glycine max"
                     /cultivar="Williams 82"
                     /db_xref="taxon:3847"
                     /chromosome="3"
                     /map="3"
     Protein         1..186
                     /product="pterocarpan synthase 1 precursor"
                     /EC_number="4.2.1.139"
                     /note="dirigent-like protein; Pterocarpan synthase 1;
                     Dirigent protein"
                     /calculated_mol_wt=18223
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2306
     mat_peptide     22..186
                     /product="Pterocarpan synthase 1. /id=PRO_5014485865"
                     /note="propagated from UniProtKB/Swiss-Prot (I1JNN8.1)"
                     /calculated_mol_wt=18223
     Region          40..183
                     /region_name="Dirigent"
                     /note="Dirigent-like protein; pfam03018"
                     /db_xref="CDD:460780"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (I1JNN8.1)"
     CDS             1..186
                     /gene="PTS1"
                     /gene_synonym="GmPTS1"
                     /coded_by="NM_001250005.4:89..649"
                     /db_xref="GeneID:100500621"
ORIGIN      
        1 makstffvcl nlsllfslvt atyyssltpt llgfreeqft hlhfffhdvv tgpkpsmvfi
       61 aepngkakda lpfgtvvamd dpltvgpeqd sklvgkaqgi ytsisqeemg lmmvmtmaft
      121 dgdfngstis vlgrnmimse pvremaivgg tgafrfargy aqarfysvdf tkgdaiveyd
      181 vfvnhy
//
LOCUS       NP_001356528             534 aa            linear   PRI 27-APR-2025
DEFINITION  suppressor of tumorigenicity 7 protein isoform 1 [Homo sapiens].
ACCESSION   NP_001356528
VERSION     NP_001356528.1
DBSOURCE    REFSEQ: accession NM_001369599.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Liu,H., Lu,W., He,H., Wu,J., Zhang,C., Gong,H. and Yang,C.
  TITLE     Inflammation-dependent overexpression of c-Myc enhances CRL4DCAF4
            E3 ligase activity and promotes ubiquitination of ST7 in
            colitis-associated cancer
  JOURNAL   J Pathol 248 (4), 464-475 (2019)
   PUBMED   30945288
  REMARK    GeneRIF: Inflammation-dependent overexpression of c-Myc enhances
            CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7
            in colitis-associated cancer.
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Yan,F., Alinari,L., Lustberg,M.E., Martin,L.K.,
            Cordero-Nieves,H.M., Banasavadi-Siddegowda,Y., Virk,S.,
            Barnholtz-Sloan,J., Bell,E.H., Wojton,J., Jacob,N.K.,
            Chakravarti,A., Nowicki,M.O., Wu,X., Lapalombella,R., Datta,J.,
            Yu,B., Gordon,K., Haseley,A., Patton,J.T., Smith,P.L., Ryu,J.,
            Zhang,X., Mo,X., Marcucci,G., Nuovo,G., Kwon,C.H., Byrd,J.C.,
            Chiocca,E.A., Li,C., Sif,S., Jacob,S., Lawler,S., Kaur,B. and
            Baiocchi,R.A.
  TITLE     Genetic validation of the protein arginine methyltransferase PRMT5
            as a candidate therapeutic target in glioblastoma
  JOURNAL   Cancer Res 74 (6), 1752-1765 (2014)
   PUBMED   24453002
  REMARK    GeneRIF: The tumor suppressor ST7 is a key gene silenced by PRMT5.
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Hu,L., Wu,C., Zhao,X., Heist,R., Su,L., Zhao,Y., Han,B., Cao,S.,
            Chu,M., Dai,J., Dong,J., Shu,Y., Xu,L., Chen,Y., Wang,Y., Lu,F.,
            Jiang,Y., Yu,D., Chen,H., Tan,W., Ma,H., Chen,J., Jin,G., Wu,T.,
            Lu,D., Christiani,D.C., Lin,D., Hu,Z. and Shen,H.
  TITLE     Genome-wide association study of prognosis in advanced non-small
            cell lung cancer patients receiving platinum-based chemotherapy
  JOURNAL   Clin Cancer Res 18 (19), 5507-5514 (2012)
   PUBMED   22872573
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Zenklusen,J.C., Rodriguez,L.V., LaCava,M., Wang,Z., Goldstein,L.S.
            and Conti,C.J.
  TITLE     Novel susceptibility locus for mouse hepatomas: evidence for a
            conserved tumor suppressor gene
  JOURNAL   Genome Res 6 (11), 1070-1076 (1996)
   PUBMED   8938430
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Zenklusen,J.C., Weitzel,J.N., Ball,H.G. and Conti,C.J.
  TITLE     Allelic loss at 7q31.1 in human primary ovarian carcinomas suggests
            the existence of a tumor suppressor gene
  JOURNAL   Oncogene 11 (2), 359-363 (1995)
   PUBMED   7624150
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Zenklusen,J.C., Thompson,J.C., Troncoso,P., Kagan,J. and Conti,C.J.
  TITLE     Loss of heterozygosity in human primary prostate carcinomas: a
            possible tumor suppressor gene at 7q31.1
  JOURNAL   Cancer Res 54 (24), 6370-6373 (1994)
   PUBMED   7987830
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Zenklusen,J.C., Bieche,I., Lidereau,R. and Conti,C.J.
  TITLE     (C-A)n microsatellite repeat D7S522 is the most commonly deleted
            region in human primary breast cancer
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12155-12158 (1994)
   PUBMED   7991599
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Ogata,T., Ayusawa,D., Namba,M., Takahashi,E., Oshimura,M. and
            Oishi,M.
  TITLE     Chromosome 7 suppresses indefinite division of nontumorigenic
            immortalized human fibroblast cell lines KMST-6 and SUSM-1
  JOURNAL   Mol Cell Biol 13 (10), 6036-6043 (1993)
   PUBMED   8105370
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106873.3, AC002542.1 and
            AC003987.1.
            
            Summary: The gene for this product maps to a region on chromosome 7
            identified as an autism-susceptibility locus. Mutation screening of
            the entire coding region in autistic individuals failed to identify
            phenotype-specific variants, suggesting that coding mutations for
            this gene are unlikely to be involved in the etiology of autism.
            The function of this gene product has not been determined.
            Transcript variants encoding different isoforms of this protein
            have been described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.217019.1,
                                           SRR1803617.280221.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.2"
     Protein         1..534
                     /product="suppressor of tumorigenicity 7 protein isoform
                     1"
                     /note="family with sequence similarity 4, subfamily A,
                     member 1; suppression of tumorigenicity 7 (breast);
                     suppressor of tumorigenicity 7 protein"
                     /calculated_mol_wt=60811
     Region          11..498
                     /region_name="ST7"
                     /note="Suppression of tumorigenicity 7; cd11557"
                     /db_xref="CDD:211407"
     CDS             1..534
                     /gene="ST7"
                     /gene_synonym="ETS7q; FAM4A; FAM4A1; HELG; RAY1; SEN4;
                     TSG7"
                     /coded_by="NM_001369599.1:391..1995"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS94185.1"
                     /db_xref="GeneID:7982"
                     /db_xref="HGNC:HGNC:11351"
                     /db_xref="MIM:600833"
ORIGIN      
        1 mfgtesslsm flntltpkfy valtgtssli sglilifeww yfrkygtsfi eqvsvshlrp
       61 llggvdnnss nnsnssngds dsnrqsvsec kvwrnplnlf rgaeynrytw vtgrepltyy
      121 dmnlsaqdhq tfftcdsdhl rpadaimqka wrernpqari saahealein eirsrvevpl
      181 iasstiweik llpkcatayi llaeeeatti aeaeklfkqa lkagdgcyrr sqqlqhhgsq
      241 yeaqhrrdtn vlvyikrrla mcarrlgrtr eavkmmrdlm kefpllsmfn ihenlleall
      301 elqayadvqa vlakyddisl pksaticyta allkaravsd kfspeaasrr glstaemnav
      361 eaihravefn phvpkyllem kslilppehi lkrgdseaia yaffhlahwk rvegalnllh
      421 ctwegtfrmi pyplekghlf ypypicteta drellpsfhe vsvypkkelp ffilftaglc
      481 sftamlallt hqfpelmgvf akaflstlfa plnfvmekve silpsslwhq ltri
//
LOCUS       NP_689837                420 aa            linear   PRI 27-APR-2025
DEFINITION  m7GpppN-mRNA hydrolase isoform 1 [Homo sapiens].
ACCESSION   NP_689837
VERSION     NP_689837.2
DBSOURCE    REFSEQ: accession NM_152624.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Mei,Y., Lv,Q., Tan,Z., Zhang,Z., Ji,Y., Chen,S. and Shen,X.
  TITLE     Decapping enzyme 2 is a novel immune-related biomarker that
            predicts poor prognosis in glioma
  JOURNAL   Biotechnol Genet Eng Rev 40 (4), 4262-4283 (2024)
   PUBMED   37191010
  REMARK    GeneRIF: Decapping enzyme 2 is a novel immune-related biomarker
            that predicts poor prognosis in glioma.
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Liu,Q., Yi,D., Ding,J., Mao,Y., Wang,S., Ma,L., Li,Q., Wang,J.,
            Zhang,Y., Zhao,J., Guo,S., Liu,Z., Guo,F., Zhao,D., Liang,C.,
            Li,X., Peng,X. and Cen,S.
  TITLE     MOV10 recruits DCP2 to decap human LINE-1 RNA by forming large
            cytoplasmic granules with phase separation properties
  JOURNAL   EMBO Rep 24 (9), e56512 (2023)
   PUBMED   37437058
  REMARK    GeneRIF: MOV10 recruits DCP2 to decap human LINE-1 RNA by forming
            large cytoplasmic granules with phase separation properties.
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Maciej,V.D., Mateva,N., Schwarz,J., Dittmers,T., Mallick,M.,
            Urlaub,H. and Chakrabarti,S.
  TITLE     Intrinsically disordered regions of tristetraprolin and DCP2
            directly interact to mediate decay of ARE-mRNA
  JOURNAL   Nucleic Acids Res 50 (18), 10665-10679 (2022)
   PUBMED   36130271
  REMARK    GeneRIF: Intrinsically disordered regions of tristetraprolin and
            DCP2 directly interact to mediate decay of ARE-mRNA.
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 420)
  AUTHORS   van Dijk,E., Cougot,N., Meyer,S., Babajko,S., Wahle,E. and
            Seraphin,B.
  TITLE     Human Dcp2: a catalytically active mRNA decapping enzyme located in
            specific cytoplasmic structures
  JOURNAL   EMBO J 21 (24), 6915-6924 (2002)
   PUBMED   12486012
  REMARK    GeneRIF: Human Dcp2 is a catalytically active mRNA decapping enzyme
            that localizes to the cytoplasm
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Ingelfinger,D., Arndt-Jovin,D.J., Luhrmann,R. and Achsel,T.
  TITLE     The human LSm1-7 proteins colocalize with the mRNA-degrading
            enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
  JOURNAL   RNA 8 (12), 1489-1501 (2002)
   PUBMED   12515382
  REMARK    GeneRIF: LSm1-7 proteins colocalize with DCP1,DCP2 and Xrn1 in
            cytoplasmic foci
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Lykke-Andersen,J.
  TITLE     Identification of a human decapping complex associated with hUpf
            proteins in nonsense-mediated decay
  JOURNAL   Mol Cell Biol 22 (23), 8114-8121 (2002)
   PUBMED   12417715
  REMARK    GeneRIF: These data suggest that a human decapping complex
            containing decapping enzymes hDcp1a and hDcp2 may be recruited to
            mRNAs containing premature termination codons by the hUpf proteins.
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Wang,Z., Jiao,X., Carr-Schmid,A. and Kiledjian,M.
  TITLE     The hDcp2 protein is a mammalian mRNA decapping enzyme
  JOURNAL   Proc Natl Acad Sci U S A 99 (20), 12663-12668 (2002)
   PUBMED   12218187
  REMARK    GeneRIF: an mRNA decapping enzyme demonstrated to contain intrinsic
            decapping activity
REFERENCE   10 (residues 1 to 420)
  AUTHORS   Ueno,K., Kumagai,T., Kijima,T., Kishimoto,T. and Hosoe,S.
  TITLE     Cloning and tissue expression of cDNAs from chromosome 5q21-22
            which is frequently deleted in advanced lung cancer
  JOURNAL   Hum Genet 102 (1), 63-68 (1998)
   PUBMED   9490301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY146650.1, AK090564.1,
            AY135173.1, BC045596.1, DB146225.1, BX648838.1, BX537716.1,
            AL135390.1, AC008536.7, CF994730.1 and AA837315.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 9, 2003 this sequence version replaced NP_689837.1.
            
            Summary: The protein encoded by this gene is a key component of an
            mRNA-decapping complex required for degradation of mRNAs, both in
            normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). It
            removes the 7-methyl guanine cap structure from mRNA, prior to its
            degradation from the 5' end. Alternatively spliced transcript
            variants encoding different isoforms have been noted for this
            gene.[provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.181407.1,
                                           SRR1803617.205736.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389063.3/ ENSP00000373715.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..420
                     /product="m7GpppN-mRNA hydrolase isoform 1"
                     /EC_number="3.6.1.62"
                     /note="nudix (nucleoside diphosphate linked moiety X)-type
                     motif 20; mRNA-decapping enzyme 2; hDpc; m7GpppN-mRNA
                     hydrolase; DCP2 decapping enzyme homolog"
                     /calculated_mol_wt=48292
     Region          12..93
                     /region_name="DCP2"
                     /note="Dcp2, box A domain; pfam05026"
                     /db_xref="CDD:428265"
     Region          97..246
                     /region_name="NUDIX_Dcp2p_Nudt20"
                     /note="mRNA decapping enzyme 2; cd03672"
                     /db_xref="CDD:467540"
     Region          129..150
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IU60.3)"
     Region          246..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IU60.3)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IU60.3)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IU60.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IU60.3)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q8IU60.3)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IU60.3)"
     Region          313..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IU60.3)"
     CDS             1..420
                     /gene="DCP2"
                     /gene_synonym="NUDT20"
                     /coded_by="NM_152624.6:137..1399"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34210.1"
                     /db_xref="GeneID:167227"
                     /db_xref="HGNC:HGNC:24452"
                     /db_xref="MIM:609844"
ORIGIN      
        1 metkrveipg svlddlcsrf ilhipseerd nairvcfqie lahwfyldfy mqntpglpqc
       61 girdfakavf shcpfllpqg edvekvldew keykmgvpty gaiildetle nvllvqgyla
      121 ksgwgfpkgk vnkeeaphdc aarevfeetg fdikdyickd dyielrindq larlyiipgi
      181 pkdtkfnpkt rreirniewf sieklpchrn dmtpksklgl apnkffmaip firplrdwls
      241 rrfgdssdsd ngfsstgstp akptveklsr tkfrhsqqlf pdgspgdqwv khrqplqqkp
      301 ynnhsemsdl lkgknqsmrg ngrkqyqdsp nqkkrtnglq pakqqnslmk cekklhprkl
      361 qdnfetdavy dlpsssedql lehaegqpva cnghckfpfs sraflsfkfd hnaimkildl
//
LOCUS       NP_001032588              69 aa            linear   PRI 27-APR-2025
DEFINITION  beta-defensin 114 precursor [Homo sapiens].
ACCESSION   NP_001032588 XP_935255 XP_946836
VERSION     NP_001032588.1
DBSOURCE    REFSEQ: accession NM_001037499.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Yu,H., Dong,J., Gu,Y., Liu,H., Xin,A., Shi,H., Sun,F., Zhang,Y.,
            Lin,D. and Diao,H.
  TITLE     The novel human beta-defensin 114 regulates lipopolysaccharide
            (LPS)-mediated inflammation and protects sperm from motility loss
  JOURNAL   J Biol Chem 288 (17), 12270-12282 (2013)
   PUBMED   23482568
  REMARK    GeneRIF: Human beta-defensin 114 regulates lipopolysaccharide
            (LPS)-mediated inflammation and protects sperm from motility loss.
            It also has antimicrobial activity against E. coli, S. aureus, and
            C. albicans.
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Patil,A.A., Cai,Y., Sang,Y., Blecha,F. and Zhang,G.
  TITLE     Cross-species analysis of the mammalian beta-defensin gene family:
            presence of syntenic gene clusters and preferential expression in
            the male reproductive tract
  JOURNAL   Physiol Genomics 23 (1), 5-17 (2005)
   PUBMED   16033865
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Schutte,B.C., Mitros,J.P., Bartlett,J.A., Walters,J.D., Jia,H.P.,
            Welsh,M.J., Casavant,T.L. and McCray,P.B. Jr.
  TITLE     Discovery of five conserved beta -defensin gene clusters using a
            computational search strategy
  JOURNAL   Proc Natl Acad Sci U S A 99 (4), 2129-2133 (2002)
   PUBMED   11854508
  REMARK    Erratum:[Proc Natl Acad Sci U S A 2002 Oct 29;99(22):14611]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138879.10.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_935255.1, XP_946836.1.
            
            Summary: Defensins form a family of antimicrobial and cytotoxic
            peptides made by neutrophils. Defensins are short, processed
            peptide molecules that are classified by structure into three
            groups: alpha-defensins, beta-defensins and theta-defensins. All
            beta-defensin genes are densely clustered in four to five syntenic
            chromosomal regions. The protein encoded by this gene is a
            beta-defensin with antimicrobial activity against E. coli, S.
            aureus, and C. albicans. The encoded protein also binds and
            neutralizes lipopolysaccharide (LPS), a factor involved in
            inflammatory diseases and male reproductive issues. [provided by
            RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000322066.4/
                                                  ENSP00000312702.3
            Protein has antimicrobial activity :: PMID: 23482568
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.3"
     Protein         1..69
                     /product="beta-defensin 114 precursor"
                     /note="defensin, beta 14; beta-defensin 14; beta-defensin
                     114"
                     /calculated_mol_wt=5222
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3114
     mat_peptide     27..69
                     /product="beta-defensin 114"
                     /experiment="DESCRIPTION:antimicrobial
                     peptide[PMID:23482568]"
                     /calculated_mol_wt=5222
     CDS             1..69
                     /gene="DEFB114"
                     /gene_synonym="DEFB-14; DEFB14"
                     /coded_by="NM_001037499.2:60..269"
                     /db_xref="CCDS:CCDS34474.1"
                     /db_xref="GeneID:245928"
                     /db_xref="HGNC:HGNC:18095"
                     /db_xref="MIM:615243"
ORIGIN      
        1 mrifyylhfl cyvtfilpat ctlvnadrct krygrckrdc lesekqidic slprkiccte
       61 klyeeddmf
//
LOCUS       NP_951013                363 aa            linear   ROD 27-APR-2025
DEFINITION  G-protein coupled receptor 6 [Mus musculus].
ACCESSION   NP_951013 XP_006512596
VERSION     NP_951013.1
DBSOURCE    REFSEQ: accession NM_199058.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Soleilhavoup,C., Travaglio,M., Patrick,K., Garcao,P., Boobalan,E.,
            Adolfs,Y., Spriggs,R.V., Moles-Garcia,E., Dhiraj,D., Oosterveen,T.,
            Ferri,S.L., Abel,T., Brodkin,E.S., Pasterkamp,R.J., Brooks,B.P. and
            Panman,L.
  TITLE     Nolz1 expression is required in dopaminergic axon guidance and
            striatal innervation
  JOURNAL   Nat Commun 11 (1), 3111 (2020)
   PUBMED   32561725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Xu,Z., Liang,Q., Song,X., Zhang,Z., Lindtner,S., Li,Z., Wen,Y.,
            Liu,G., Guo,T., Qi,D., Wang,M., Wang,C., Li,H., You,Y., Wang,X.,
            Chen,B., Feng,H., Rubenstein,J.L. and Yang,Z.
  TITLE     SP8 and SP9 coordinately promote D2-type medium spiny neuron
            production by activating Six3 expression
  JOURNAL   Development 145 (14) (2018)
   PUBMED   29967281
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Tischfield,D.J., Saraswat,D.K., Furash,A., Fowler,S.C.,
            Fuccillo,M.V. and Anderson,S.A.
  TITLE     Loss of the neurodevelopmental gene Zswim6 alters striatal
            morphology and motor regulation
  JOURNAL   Neurobiol Dis 103, 174-183 (2017)
   PUBMED   28433741
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Oeckl,P. and Ferger,B.
  TITLE     Increased susceptibility of G-protein coupled receptor 6 deficient
            mice to MPTP neurotoxicity
  JOURNAL   Neuroscience 337, 218-223 (2016)
   PUBMED   27651149
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Zhang,Q., Zhang,Y., Wang,C., Xu,Z., Liang,Q., An,L., Li,J., Liu,Z.,
            You,Y., He,M., Mao,Y., Chen,B., Xiong,Z.Q., Rubenstein,J.L. and
            Yang,Z.
  TITLE     The Zinc Finger Transcription Factor Sp9 Is Required for the
            Development of Striatopallidal Projection Neurons
  JOURNAL   Cell Rep 16 (5), 1431-1444 (2016)
   PUBMED   27452460
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Budry,L., Balsalobre,A., Gauthier,Y., Khetchoumian,K., L'honore,A.,
            Vallette,S., Brue,T., Figarella-Branger,D., Meij,B. and Drouin,J.
  TITLE     The selector gene Pax7 dictates alternate pituitary cell fates
            through its pioneer action on chromatin remodeling
  JOURNAL   Genes Dev 26 (20), 2299-2310 (2012)
   PUBMED   23070814
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Lobo,M.K., Cui,Y., Ostlund,S.B., Balleine,B.W. and Yang,X.W.
  TITLE     Genetic control of instrumental conditioning by striatopallidal
            neuron-specific S1P receptor Gpr6
  JOURNAL   Nat Neurosci 10 (11), 1395-1397 (2007)
   PUBMED   17934457
  REMARK    GeneRIF: Gpr6 is the first striatopallidal neuron-specific genetic
            regulator of instrumental conditioning in a mammal.
REFERENCE   8  (residues 1 to 363)
  AUTHORS   Tanaka,S., Ishii,K., Kasai,K., Yoon,S.O. and Saeki,Y.
  TITLE     Neural expression of G protein-coupled receptors GPR3, GPR6, and
            GPR12 up-regulates cyclic AMP levels and promotes neurite outgrowth
  JOURNAL   J Biol Chem 282 (14), 10506-10515 (2007)
   PUBMED   17284443
REFERENCE   9  (residues 1 to 363)
  AUTHORS   Ignatov,A., Lintzel,J., Kreienkamp,H.J. and Schaller,H.C.
  TITLE     Sphingosine-1-phosphate is a high-affinity ligand for the G
            protein-coupled receptor GPR6 from mouse and induces intracellular
            Ca2+ release by activating the sphingosine-kinase pathway
  JOURNAL   Biochem Biophys Res Commun 311 (2), 329-336 (2003)
   PUBMED   14592418
  REMARK    GeneRIF: identification, characterization and cloning; identified
            sphingosine-1-phosphate as a high-affinity ligand
REFERENCE   10 (residues 1 to 363)
  AUTHORS   Chalhoub,N., Benachenhou,N. and Vacher,J.
  TITLE     Physical and transcriptional map of the mouse Chromosome 10
            proximal region syntenic to human 6q16-q21
  JOURNAL   Mamm Genome 12 (12), 887-892 (2001)
   PUBMED   11707774
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CX236691.1, AK139367.1 and AW046789.1.
            
            On Dec 30, 2017 this sequence version replaced XP_006512596.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CX236691.1, AK139367.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849377, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 22.08 cM"
     Protein         1..363
                     /product="G-protein coupled receptor 6"
                     /note="sphingosine 1-phosphate receptor GPR6"
                     /calculated_mol_wt=37954
     Site            2
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Region          29..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Region          74..341
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          76..100
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            76..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Site            108..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Region          109..130
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          143..165
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            144..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Site            187..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Region          188..204
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          224..247
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            232..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Site            279..305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Region          279..301
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          309..334
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            311..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q6YNI2.1)"
     CDS             1..363
                     /gene="Gpr6"
                     /gene_synonym="Gm233"
                     /coded_by="NM_199058.2:184..1275"
                     /db_xref="CCDS:CCDS23802.1"
                     /db_xref="GeneID:140741"
                     /db_xref="MGI:MGI:2155249"
ORIGIN      
        1 mnasaaalne sqvvavaaeg aaaaataaga pdtgewgppa asaalggggg pngslelssq
       61 lpagpsglll savnpwdvll cvsgtviage nalvvalias tpalrtpmfv lvgslatadl
      121 lagcglilhf vfqyvvpset vsllmvgflv asfaasvssl laitvdryls lynaltyysr
      181 rtllgvhlll aatwtvslgl gllpvlgwnc ladrtscsvv rpltrshval lstsffvvfg
      241 imlhlyvric qvvwrhahqi alqqhclapp hlaatrkgvg tlavvlgtfg aswlpfaiyc
      301 vvgsqedpai ytyatllpat ynsminpiiy afrnqeiqra lwllfcgcfq skvpfrsrsp
      361 sev
//
LOCUS       NP_060959               2964 aa            linear   PRI 27-APR-2025
DEFINITION  histone-lysine N-methyltransferase ASH1L isoform 2 [Homo sapiens].
ACCESSION   NP_060959
VERSION     NP_060959.2
DBSOURCE    REFSEQ: accession NM_018489.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2964)
  AUTHORS   Yancoskie,M.N., Khaleghi,R., Gururajan,A., Raghunathan,A.,
            Gupta,A., Diethelm,S., Maritz,C., Sturla,S.J., Krishnan,M. and
            Naegeli,H.
  TITLE     ASH1L guards cis-regulatory elements against cyclobutane pyrimidine
            dimer induction
  JOURNAL   Nucleic Acids Res 52 (14), 8254-8270 (2024)
   PUBMED   38884271
  REMARK    GeneRIF: ASH1L guards cis-regulatory elements against cyclobutane
            pyrimidine dimer induction.
REFERENCE   2  (residues 1 to 2964)
  AUTHORS   Xie,M., Zhang,L., Han,L., Huang,L., Huang,Y., Yang,M. and Zhang,N.
  TITLE     The ASH1L-AS1-ASH1L axis controls NME1-mediated activation of the
            RAS signaling in gastric cancer
  JOURNAL   Oncogene 42 (46), 3435-3445 (2023)
   PUBMED   37805663
  REMARK    GeneRIF: The ASH1L-AS1-ASH1L axis controls NME1-mediated activation
            of the RAS signaling in gastric cancer.
REFERENCE   3  (residues 1 to 2964)
  AUTHORS   Al-Harthi,S., Li,H., Winkler,A., Szczepski,K., Deng,J.,
            Grembecka,J., Cierpicki,T. and Jaremko,L.
  TITLE     MRG15 activates histone methyltransferase activity of ASH1L by
            recruiting it to the nucleosomes
  JOURNAL   Structure 31 (10), 1200-1207 (2023)
   PUBMED   37527654
  REMARK    GeneRIF: MRG15 activates histone methyltransferase activity of
            ASH1L by recruiting it to the nucleosomes.
REFERENCE   4  (residues 1 to 2964)
  AUTHORS   Rothrock,A.T., Stewart,J. 3rd, Li,F., Racila,E. and Amin,K.
  TITLE     Exploration of INSM1 and hASH1 as additional markers in lung
            cytology samples of high-grade neuroendocrine carcinoma with
            indeterminate neuroendocrine differentiation
  JOURNAL   Diagn Cytopathol 50 (5), 230-234 (2022)
   PUBMED   35147301
  REMARK    GeneRIF: Exploration of INSM1 and hASH1 as additional markers in
            lung cytology samples of high-grade neuroendocrine carcinoma with
            indeterminate neuroendocrine differentiation.
REFERENCE   5  (residues 1 to 2964)
  AUTHORS   Liu,W., Xu,L., Zhang,C., Shen,L., Dong,J., Zhang,H., Liu,S., Che,F.
            and Zheng,X.
  TITLE     ASH1L may contribute to the risk of Tourette syndrome: Combination
            of family-based analysis and case-control study
  JOURNAL   Brain Behav 12 (4), e2539 (2022)
   PUBMED   35307981
  REMARK    GeneRIF: ASH1L may contribute to the risk of Tourette syndrome:
            Combination of family-based analysis and case-control study.
REFERENCE   6  (residues 1 to 2964)
  AUTHORS   Gregory,G.D., Vakoc,C.R., Rozovskaia,T., Zheng,X., Patel,S.,
            Nakamura,T., Canaani,E. and Blobel,G.A.
  TITLE     Mammalian ASH1L is a histone methyltransferase that occupies the
            transcribed region of active genes
  JOURNAL   Mol Cell Biol 27 (24), 8466-8479 (2007)
   PUBMED   17923682
  REMARK    GeneRIF: These data suggest that ASH1L occupies most, if not all,
            active genes and methylates histone H3 in a nonredundant fashion at
            a subset of genes.
REFERENCE   7  (residues 1 to 2964)
  AUTHORS   Vasilescu,J., Zweitzig,D.R., Denis,N.J., Smith,J.C., Ethier,M.,
            Haines,D.S. and Figeys,D.
  TITLE     The proteomic reactor facilitates the analysis of affinity-purified
            proteins by mass spectrometry: application for identifying
            ubiquitinated proteins in human cells
  JOURNAL   J Proteome Res 6 (1), 298-305 (2007)
   PUBMED   17203973
REFERENCE   8  (residues 1 to 2964)
  AUTHORS   Kuryshev,V.Y., Vorobyov,E., Zink,D., Schmitz,J.,
            Rozhdestvensky,T.S., Munstermann,E., Ernst,U., Wellenreuther,R.,
            Moosmayer,P., Bechtel,S., Schupp,I., Horst,J., Korn,B., Poustka,A.
            and Wiemann,S.
  TITLE     An anthropoid-specific segmental duplication on human chromosome
            1q22
  JOURNAL   Genomics 88 (2), 143-151 (2006)
   PUBMED   16545939
REFERENCE   9  (residues 1 to 2964)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   10 (residues 1 to 2964)
  AUTHORS   Nakamura,T., Blechman,J., Tada,S., Rozovskaia,T., Itoyama,T.,
            Bullrich,F., Mazo,A., Croce,C.M., Geiger,B. and Canaani,E.
  TITLE     huASH1 protein, a putative transcription factor encoded by a human
            homologue of the Drosophila ash1 gene, localizes to both nuclei and
            cell-cell tight junctions
  JOURNAL   Proc Natl Acad Sci U S A 97 (13), 7284-7289 (2000)
   PUBMED   10860993
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353807.18, BQ883186.1,
            AF257305.1, AL139410.20, CN365042.1 and DA236222.1.
            
            On Jul 14, 2006 this sequence version replaced NP_060959.1.
            
            Summary: This gene encodes a member of the trithorax group of
            transcriptional activators. The protein contains four AT hooks, a
            SET domain, a PHD-finger motif, and a bromodomain. It is localized
            to many small speckles in the nucleus, and also to cell-cell tight
            junctions. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction compared to variant 1. The resulting isoform (2)
            has the same N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3350615.1,
                                           SRR14038197.1341747.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392403.8/ ENSP00000376204.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2964
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..2964
                     /product="histone-lysine N-methyltransferase ASH1L isoform
                     2"
                     /EC_number="2.1.1.359"
                     /EC_number="2.1.1.367"
                     /note="probable histone-lysine N-methyltransferase ASH1L;
                     ASH1-like protein; lysine N-methyltransferase 2H; absent
                     small and homeotic disks protein 1 homolog; ash1 (absent,
                     small, or homeotic)-like"
                     /calculated_mol_wt=332081
     Region          1..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          118..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Site            375
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          501..525
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          537..583
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          824..845
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          878..966
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          1100..1128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          1151..1231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MY8; propagated from
                     UniProtKB/Swiss-Prot (Q9NR48.2)"
     Site            1170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MY8; propagated from
                     UniProtKB/Swiss-Prot (Q9NR48.2)"
     Site            1220
                     /site_type="methylation"
                     /note="N5-methylglutamine.
                     /evidence=ECO:0000269|PubMed:26797129; propagated from
                     UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          1243..1281
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          1489..1508
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          1580..1711
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          1741..1761
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          1911..1991
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          2064..2283
                     /region_name="Catalytic domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          2087..2138
                     /region_name="AWS"
                     /note="associated with SET domains; smart00570"
                     /db_xref="CDD:197795"
     Region          2141..2281
                     /region_name="SET_ASH1L"
                     /note="SET domain (including post-SET domain) found in
                     ASH1-like protein (ASH1L) and similar proteins; cd19174"
                     /db_xref="CDD:380951"
     Site            order(2150..2152,2169,2179,2183,2191..2197,2214..2218,
                     2225..2227,2242,2253..2261,2266..2270,2279)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380951"
     Site            order(2150..2152,2191..2194,2214..2218,2255,2266..2270,
                     2279)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380951"
     Site            order(2169,2179,2183,2193..2197,2225..2227,2242,
                     2253..2257)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380951"
     Site            order(2220,2268,2270,2275)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380951"
     Region          2283..2341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Site            2312
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MY8; propagated from
                     UniProtKB/Swiss-Prot (Q9NR48.2)"
     Site            2314
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MY8; propagated from
                     UniProtKB/Swiss-Prot (Q9NR48.2)"
     Site            2318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MY8; propagated from
                     UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          2438..2543
                     /region_name="Bromo_ASH1"
                     /note="Bromodomain; ASH1_like sub-family. ASH1 (absent,
                     small, or homeotic 1) is a member of the trithorax-group
                     in Drosophila melanogaster, an epigenetic transcriptional
                     regulator of HOX genes. Drosophila ASH1 has been shown to
                     methylate specific lysines in...; cd05525"
                     /db_xref="CDD:99955"
     Site            order(2470,2475,2478,2517,2521,2527)
                     /site_type="other"
                     /note="putative acetyllysine binding site [chemical
                     binding]"
                     /db_xref="CDD:99955"
     Region          2581..2623
                     /region_name="PHD_ASH1L"
                     /note="PHD finger found in histone-lysine
                     N-methyltransferase ASH1L; cd15548"
                     /db_xref="CDD:277023"
     Site            order(2582,2593..2597,2601,2618)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277023"
     Region          2660..2794
                     /region_name="BAH_polybromo"
                     /note="BAH, or Bromo Adjacent Homology domain, as present
                     in polybromo and yeast RSC1/2. The human polybromo protein
                     (BAF180) is a component of the SWI/SNF
                     chromatin-remodeling complex PBAF. It is thought that
                     polybromo participates in transcriptional...; cd04717"
                     /db_xref="CDD:240068"
     Region          2820..2851
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     Region          2871..2914
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR48.2)"
     CDS             1..2964
                     /gene="ASH1L"
                     /gene_synonym="ASH1; ASH1L1; KMT2H; MRD52"
                     /coded_by="NM_018489.3:751..9645"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1113.2"
                     /db_xref="GeneID:55870"
                     /db_xref="HGNC:HGNC:19088"
                     /db_xref="MIM:607999"
ORIGIN      
        1 mdprntamlg lgsdsegfsr kspsaistgt lvskrevele kntkeeedlr krnrerniea
       61 gkddgltdaq qqfsvketnf segnlklkig lqakrtkkpp knlenyvcrp aikttikhpr
      121 kalksgkmtd eknehcpskr dpsklykkad dvaaiecqse evirlhsqge nnplskklsp
      181 vhsemadyin atpstllgsr dpdlkdrall nggtsvtekl aqliatcpps kssktkpkkl
      241 gtgttaglvs kdlirkagvg svagiihkdl ikkptistav glvtkdpgkk pvfnaavglv
      301 nkdsvkklgt gttavfinkn lgkkpgtitt vgllskdsgk klgigivpgl vhkesgkklg
      361 lgtvvglvnk dlgkklgstv glvakdcakk ivassamglv nkdigkklms cplagliskd
      421 ainlkaeall ptqeplkasc stninnqesq elseslkdsa tsktfeknvv rqnkesilek
      481 fsvrkeiinl ekemfnegtc iqqdsfssse kgsyetskhe kqppvyctsp dfkmggasdv
      541 stakspfsav gesnlpspsp tvsvnpltrs ppetssqlap nplllsstte lieeisesvg
      601 knqftsesth lnvghrsvgh sisieckgid kevndsktth idiprisssl gkkpsltses
      661 sihtitpsvv nftslfsnkp flklgavsas dkhcqvaesl stslqskplk krkgrkprwt
      721 kvvarstcrs pkglelerse lfknvscssl snsnsepakf mknigppsfv dhdflkrrlp
      781 klskstapsl alladsekps hksfathkls ssmcvssdll sdiykpkrgr pkskempqle
      841 gppkrtlkip askvfslqsk eeqeppilqp eieipsfkqg lsvspfpkkr grpkrqmrsp
      901 vkmkppvlsv apfvatesps klesesdnhr sssdffesed qlqdpddldd shrpsvcsms
      961 dlemepdkki tkrnngqlmk tiirkinkmk tlkrkkllnq ilsssvessn kgkvqsklhn
     1021 tvsslaatfg sklgqqinvs kkgtiyigkr rgrkpktvln gilsgsptsl avleqtaqqa
     1081 agsalgqilp pllpssasss eilpspicsq ssgtsggqsp vssdagfvep ssvpylhlhs
     1141 rqgsmiqtla mkkaskgrrr lspptllpns pshlseltsl keatpspise shsdetipsd
     1201 sgigtdnnst sdraekfcgq kkrrhsfehv slippetstv lsslkekhkh kckrrnhdyl
     1261 sydkmkrqkr krkkkypqlr nrqdpdfiae leelisrlse irithrshhf iprdllptif
     1321 rinfnsfyth psfpldplhy irkpdlkkkr grppkmream aempfmhsls fplsstgfyp
     1381 sygmpyspsp ltaapiglgy ygrypptlyp pppspsfttp lpppsymhag hlllnpakyh
     1441 kkkhkllrqe aflttsrtpl lsmstypsvp pemaygwmve hkhrhrhkhr ehrsseqpqv
     1501 smdtgssrsv leslkryrfg kdavgerykh kekhrchmsc phlspsksli nreeqwvhre
     1561 psessplalg lqtplqidcs esspslslgg ftpnsepass dehtnlftsa igscrvsnpn
     1621 ssgrkkltds pglfsaqdts lnrlhrkesl psneravqtl agsqptsdkp sqrpsestnc
     1681 sptrkrssse stsstvngvp srsprlvasg ddsvdsllqr mvqnedqepm eksidaviat
     1741 asappssspg rshskdrtlg kpdsllvpav tsdscnnsis llsekltssc sphhikrsvv
     1801 eamqrqarkm cnydkilatk knldhvnkil kakklqrqar tgnnfvkrrp grprkcplqa
     1861 vvsmqafqaa qfvnpelnrd eegaalhlsp dtvtdvieav vqsvnlnpeh kkglkrkgwl
     1921 leeqtrkkqk plpeeeeqen nksfneapve ipspsetpak psepestlqp vlsliprekk
     1981 pprppkkkyq kaglysdvyk ttdpksrliq lkkekleytp geheyglfpa pihvgkylrq
     2041 kridfqlpyd ilwqwkhnql ykkpdvplyk kirsnvyvdv kplsgyeatt cnckkpdddt
     2101 rkgcvddcln rmifaecspn tcpcgeqccn qriqrhewvq clerfraeek gwgirtkepl
     2161 kagqfiieyl gevvseqefr nrmieqyhnh sdhyclnlds gmvidsyrmg nearfinhsc
     2221 dpncemqkws vngvyrigly alkdmpagte ltydynfhsf nvekqqlckc gfekcrgiig
     2281 gksqrvnglt ssknsqpmat hkksgrskek rkskhklkkr rghlseepse nintptrltp
     2341 qlqmkpmsnr ernfvlkhhv flvrnwekir qkqeevkhts dnihsaslyt rwngicrddg
     2401 niksdvfmtq fsalqtarsv rtrrlaaaee nievaraarl aqifkeicdg iisykdssrq
     2461 alaapllnlp pkkknadyye kisdpldlit iekqiltgyy ktveafdadm lkvfrnaeky
     2521 ygrkspvgrd vcrlrkayyn arheasaqid eivgetasea dssetsvsek enghekdddv
     2581 ircicglykd eglmiqcdkc mvwqhcdcmg vnsdvehylc eqcdprpvdr evpmiprphy
     2641 aqpgcvyfic llrddlllrq gdcvylmrds rrtpdghpvr qsyrllshin rdkldifrie
     2701 klwknekeer fafghhyfrp hethhspsrr fyhnelfrvp lyeiipleav vgtccvldly
     2761 tyckgrpkgv keqdvyicdy rldksahlfy kihrnrypvc tkpyafdhfp kkltpkkdfs
     2821 phyvpdnykr nggrsswkse rskpplkdlg qeddalplie evlasqeqaa neipsleepe
     2881 regatanvse gekkteessq epqstctpee rrhnqrerln qillnlleki pgknaidvty
     2941 lleegsgrkl rrrtlfipen sfrk
//
LOCUS       NP_001041714              74 aa            linear   PRI 27-APR-2025
DEFINITION  small integral membrane protein 15 [Homo sapiens].
ACCESSION   NP_001041714 XP_931618 XP_944029
VERSION     NP_001041714.1
DBSOURCE    REFSEQ: accession NM_001048249.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Kimura,K., Wakamatsu,A., Suzuki,Y., Ota,T., Nishikawa,T.,
            Yamashita,R., Yamamoto,J., Sekine,M., Tsuritani,K., Wakaguri,H.,
            Ishii,S., Sugiyama,T., Saito,K., Isono,Y., Irie,R., Kushida,N.,
            Yoneyama,T., Otsuka,R., Kanda,K., Yokoi,T., Kondo,H., Wagatsuma,M.,
            Murakawa,K., Ishida,S., Ishibashi,T., Takahashi-Fujii,A.,
            Tanase,T., Nagai,K., Kikuchi,H., Nakai,K., Isogai,T. and Sugano,S.
  TITLE     Diversification of transcriptional modulation: large-scale
            identification and characterization of putative alternative
            promoters of human genes
  JOURNAL   Genome Res 16 (1), 55-65 (2006)
   PUBMED   16344560
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA039277.1, BX538015.1 and AC008498.3.
            
            On or before Sep 30, 2006 this sequence version replaced
            XP_931618.1, XP_944029.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.208459.1, BX538015.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000339020.8/ ENSP00000339324.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.1"
     Protein         1..74
                     /product="small integral membrane protein 15"
                     /note="UPF0542 protein C5orf43"
                     /calculated_mol_wt=8494
     Region          5..71
                     /region_name="UPF0542"
                     /note="Uncharacterized protein family UPF0542; pfam15086"
                     /db_xref="CDD:405727"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B0.1)"
     Region          55..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B0.1)"
     CDS             1..74
                     /gene="SMIM15"
                     /gene_synonym="C5orf43"
                     /coded_by="NM_001048249.4:421..645"
                     /db_xref="CCDS:CCDS34165.1"
                     /db_xref="GeneID:643155"
                     /db_xref="HGNC:HGNC:33861"
ORIGIN      
        1 mfdikawaey vvewaakdpy gflttvilal tplflasavl swklakmiea rekeqkkkqk
       61 rqeniakakr lkkd
//
LOCUS       NP_598912                528 aa            linear   ROD 27-APR-2025
DEFINITION  tyrosine--tRNA ligase, cytoplasmic [Mus musculus].
ACCESSION   NP_598912 XP_109408
VERSION     NP_598912.5
DBSOURCE    REFSEQ: accession NM_134151.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Jones,J.A., Zhou,J., Dong,J., Huitron-Resendiz,S., Boussaty,E.,
            Chavez,E., Wei,N., Dumitru,C.D., Morodomi,Y., Kanaji,T., Ryan,A.F.,
            Friedman,R., Zhou,T., Kanaji,S., Wortham,M., Schenk,S.,
            Roberts,A.J. and Yang,X.L.
  TITLE     Murine nuclear tyrosyl-tRNA synthetase deficiency leads to fat
            storage deficiency and hearing loss
  JOURNAL   J Biol Chem 300 (10), 107756 (2024)
   PUBMED   39260699
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Rhymes,E.R., Simkin,R.L., Qu,J., Villarroel-Campos,D., Surana,S.,
            Tong,Y., Shapiro,R., Burgess,R.W., Yang,X.L., Schiavo,G. and
            Sleigh,J.N.
  TITLE     Boosting BDNF in muscle rescues impaired axonal transport in a
            mouse model of DI-CMTC peripheral neuropathy
  JOURNAL   Neurobiol Dis 195, 106501 (2024)
   PUBMED   38583640
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Hines,T.J., Tadenev,A.L.D., Lone,M.A., Hatton,C.L., Bagasrawala,I.,
            Stum,M.G., Miers,K.E., Hornemann,T. and Burgess,R.W.
  TITLE     Precision mouse models of Yars/dominant intermediate
            Charcot-Marie-Tooth disease type C and Sptlc1/hereditary sensory
            and autonomic neuropathy type 1
  JOURNAL   J Anat 241 (5), 1169-1185 (2022)
   PUBMED   34875719
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Spaulding,E.L., Hines,T.J., Bais,P., Tadenev,A.L.D., Schneider,R.,
            Jewett,D., Pattavina,B., Pratt,S.L., Morelli,K.H., Stum,M.G.,
            Hill,D.P., Gobet,C., Pipis,M., Reilly,M.M., Jennings,M.J.,
            Horvath,R., Bai,Y., Shy,M.E., Alvarez-Castelao,B., Schuman,E.M.,
            Bogdanik,L.P., Storkebaum,E. and Burgess,R.W.
  TITLE     The integrated stress response contributes to tRNA
            synthetase-associated peripheral neuropathy
  JOURNAL   Science 373 (6559), 1156-1161 (2021)
   PUBMED   34516839
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Tsukahara,T., Yamagishi,S., Neyama,H. and Ueda,H.
  TITLE     Tyrosyl-tRNA synthetase: A potential kyotorphin synthetase in
            mammals
  JOURNAL   Peptides 101, 60-68 (2018)
   PUBMED   29289698
  REMARK    GeneRIF: conclusion is further supported by a positive correlation
            across brain regions between TyrRS expression and
            arginine-accelerated KTP production.
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Wei,N., Shi,Y., Truong,L.N., Fisch,K.M., Xu,T., Gardiner,E., Fu,G.,
            Hsu,Y.O., Kishi,S., Su,A.I., Wu,X. and Yang,X.L.
  TITLE     Oxidative stress diverts tRNA synthetase to nucleus for protection
            against DNA damage
  JOURNAL   Mol Cell 56 (2), 323-332 (2014)
   PUBMED   25284223
REFERENCE   9  (residues 1 to 528)
  AUTHORS   Jordanova,A., Irobi,J., Thomas,F.P., Van Dijck,P., Meerschaert,K.,
            Dewil,M., Dierick,I., Jacobs,A., De Vriendt,E., Guergueltcheva,V.,
            Rao,C.V., Tournev,I., Gondim,F.A., D'Hooghe,M., Van Gerwen,V.,
            Callaerts,P., Van Den Bosch,L., Timmermans,J.P., Robberecht,W.,
            Gettemans,J., Thevelein,J.M., De Jonghe,P., Kremensky,I. and
            Timmerman,V.
  TITLE     Disrupted function and axonal distribution of mutant tyrosyl-tRNA
            synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy
  JOURNAL   Nat Genet 38 (2), 197-202 (2006)
   PUBMED   16429158
REFERENCE   10 (residues 1 to 528)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606977.28.
            
            On Mar 18, 2019 this sequence version replaced NP_598912.4.
            
            Transcript Variant: This variant (1) represents the protein-coding
            transcript.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK145356.1, AK043837.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 63.05 cM"
     Protein         1..528
                     /product="tyrosine--tRNA ligase, cytoplasmic"
                     /EC_number="6.1.1.1"
                     /note="tyrosyl-tRNA synthetase, cytoplasmic; tyrRS;
                     tyrosyl--tRNA ligase"
                     /calculated_mol_wt=58974
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P54577; propagated from
                     UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine, in Tyrosine--tRNA ligase,
                     cytoplasmic, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P54577; propagated from
                     UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Region          8..328
                     /region_name="nt_trans"
                     /note="nucleotidyl transferase superfamily; cl00015"
                     /db_xref="CDD:469580"
     Site            order(39,41..43,49,51..52,166,170,173,182,184..185,188,
                     214..215,222..223,224)
                     /site_type="active"
                     /db_xref="CDD:173902"
     Region          44..52
                     /region_name="'HIGH' region.
                     /evidence=ECO:0000250|UniProtKB:P54577"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Site            49..52
                     /site_type="other"
                     /note="HIGH motif"
                     /db_xref="CDD:173902"
     Site            order(76,79..80,130..131,133..135,137..138,140..143,
                     145..146,162,164..165,168..169)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:173902"
     Site            197
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P54577; propagated from
                     UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54577; propagated from
                     UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Site            206
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P54577; propagated from
                     UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Region          222..226
                     /region_name="'KMSKS' region.
                     /evidence=ECO:0000250|UniProtKB:P54577"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Site            order(222..223,224..225)
                     /site_type="other"
                     /note="KMSKS motif"
                     /db_xref="CDD:173902"
     Region          242..247
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:P54577"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Region          <327..528
                     /region_name="PLN02610"
                     /note="probable methionyl-tRNA synthetase"
                     /db_xref="CDD:215329"
     Region          339..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54577; propagated from
                     UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Site            474
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P54577; propagated from
                     UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Site            482
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P54577; propagated from
                     UniProtKB/Swiss-Prot (Q91WQ3.3)"
     Site            490
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P54577; propagated from
                     UniProtKB/Swiss-Prot (Q91WQ3.3)"
     CDS             1..528
                     /gene="Yars1"
                     /gene_synonym="Yars"
                     /coded_by="NM_134151.5:114..1700"
                     /db_xref="CCDS:CCDS18685.2"
                     /db_xref="GeneID:107271"
                     /db_xref="MGI:MGI:2147627"
ORIGIN      
        1 mgdapspeek lhlitrnlqe vlgeeklkei lkerelkvyw gtattgkphv ayfvpmskia
       61 dflkagcevt ilfadlhayl dnmkapwell elrtsyyenv ikamlesigv pleklkfikg
      121 tdyqlskeyt ldvyrlssvv tqhdakkaga evvkqvehpl lsgllypglq aldeeylkvd
      181 aqfggvdqrk iftfaekylp algyskrvhl mnpmvpgltg skmssseees kidlldrked
      241 vkkklkkafc epgnvenngv lsfikhvlfp lksefvilrd ekwggnktyt vylelekdfa
      301 aevvhpgdlk nsvevalnkl ldpirekfnt palkklasaa ypdpskqkpp akgpaknsep
      361 eevipsrldi rvgkilsvek hpdadslyve kidvgeaepr tvvsglvqfv pkeelqdrlv
      421 vvlcnlkpqk mrgvdsqgml lcasvegvsr qvepldppag sapgervfvq gyekgqpdee
      481 lkpkkkvfek lqadfkisee ciaqwkqtnf mtklgfvsck slkggnis
//
LOCUS       NP_001123949             918 aa            linear   ROD 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 2 [Mus
            musculus].
ACCESSION   NP_001123949
VERSION     NP_001123949.1
DBSOURCE    REFSEQ: accession NM_001130477.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Thoren,L.A., Norgaard,G.A., Weischenfeldt,J., Waage,J.,
            Jakobsen,J.S., Damgaard,I., Bergstrom,F.C., Blom,A.M., Borup,R.,
            Bisgaard,H.C. and Porse,B.T.
  TITLE     UPF2 is a critical regulator of liver development, function and
            regeneration
  JOURNAL   PLoS One 5 (7), e11650 (2010)
   PUBMED   20657840
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 918)
  AUTHORS   Combes,A.N., Lesieur,E., Harley,V.R., Sinclair,A.H., Little,M.H.,
            Wilhelm,D. and Koopman,P.
  TITLE     Three-dimensional visualization of testis cord morphogenesis, a
            novel tubulogenic mechanism in development
  JOURNAL   Dev Dyn 238 (5), 1033-1041 (2009)
   PUBMED   19334288
REFERENCE   3  (residues 1 to 918)
  AUTHORS   Hoffman,B.G., Zavaglia,B., Witzsche,J., Ruiz de Algara,T.,
            Beach,M., Hoodless,P.A., Jones,S.J., Marra,M.A. and Helgason,C.D.
  TITLE     Identification of transcripts with enriched expression in the
            developing and adult pancreas
  JOURNAL   Genome Biol 9 (6), R99 (2008)
   PUBMED   18554416
REFERENCE   4  (residues 1 to 918)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   5  (residues 1 to 918)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 918)
  AUTHORS   Cobellis,G., Nicolaus,G., Iovino,M., Romito,A., Marra,E.,
            Barbarisi,M., Sardiello,M., Di Giorgio,F.P., Iovino,N., Zollo,M.,
            Ballabio,A. and Cortese,R.
  TITLE     Tagging genes with cassette-exchange sites
  JOURNAL   Nucleic Acids Res 33 (4), e44 (2005)
   PUBMED   15741177
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 918)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 918)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 918)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
REFERENCE   10 (residues 1 to 918)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL627185.10 and AL627078.10.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' coding region, compared to variant 1. The encoded protein
            (isoform 2) lacks 5 amino acids in the N-terminus, compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK028412.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164140 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 67.34 cM"
     Protein         1..918
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 2"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein;
                     plenty-of-prolines-101"
                     /calculated_mol_wt=103585
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          619..>816
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..918
                     /gene="Srrm1"
                     /gene_synonym="POP101; Srm160"
                     /coded_by="NM_001130477.2:30..2786"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS51329.1"
                     /db_xref="GeneID:51796"
                     /db_xref="MGI:MGI:1858303"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkeks pelpepsvrm kdssvqeats
      241 tsdilkapkp epvpepkeps peknskkeke ktrprsrsrs ksrsrtrsrs pshtrprrrh
      301 rsrsrrrpsp rrrpsprrrt pprrmppppr hrrsrspgrr rrrssaslsg ssssssssrs
      361 rsppkkppkr tsspprktrr lspsaspprr rhrpsspatp ppktrhsptp qqsnrtrksr
      421 vsvspgrtsg kvtkhkgtek respspapkp rkvelsesee dkgskmaaad svqqrrqyrr
      481 qnqqsssdsg ssstsederp krshvkngev grrrrhspsr saspsprkrq ketsprmqmg
      541 krwqspvtks srrrrspspp parrrrspsp appppppppp prrrrsptpp prrrtpsppp
      601 rrrspsprry sppiqrrysp spppkrrtas pppppkrras pspppkrrvs hspppkqrsp
      661 tvtkrrspsl sskhrkgssp grstrearsp qpnkrhspsp rprapqtssp ppvrrgasas
      721 pqgrqspsps trpirrvsrt pepkkikkaa spspqsvrrv sssrsvsgsp epaakkppap
      781 pspvqsqsps tnwspavpak kaksptpsls parnsdqegg gkkkkkkkdk khkkdkkhkk
      841 hkkhkkekav tiatpataap aavsaattts aqeepaaape prketeseae ddnlddlerh
      901 lrekalrsmr kaqvspqs
//
LOCUS       NP_001351932             667 aa            linear   PRI 27-APR-2025
DEFINITION  transcription initiation factor TFIID subunit 6 isoform delta [Homo
            sapiens].
ACCESSION   NP_001351932 XP_011514844
VERSION     NP_001351932.1
DBSOURCE    REFSEQ: accession NM_001365003.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Tuc,E., Bengur,F.B., Aykut,A., Sahin,O. and Alanay,Y.
  TITLE     The third family with TAF6-related phenotype: Alazami-Yuan syndrome
  JOURNAL   Clin Genet 97 (5), 795-796 (2020)
   PUBMED   32030742
  REMARK    GeneRIF: The third family with TAF6-related phenotype: Alazami-Yuan
            syndrome.
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Delannoy,A., Wilhelm,E., Eilebrecht,S., Alvarado-Cuevas,E.M.,
            Benecke,A.G. and Bell,B.
  TITLE     BIM and NOXA are mitochondrial effectors of TAF6delta-driven
            apoptosis
  JOURNAL   Cell Death Dis 9 (2), 70 (2018)
   PUBMED   29358700
  REMARK    GeneRIF: BIM and NOXA contribute to TAF6delta-dependent cell death.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Gupta,K., Watson,A.A., Baptista,T., Scheer,E., Chambers,A.L.,
            Koehler,C., Zou,J., Obong-Ebong,I., Kandiah,E., Temblador,A.,
            Round,A., Forest,E., Man,P., Bieniossek,C., Laue,E.D., Lemke,E.A.,
            Rappsilber,J., Robinson,C.V., Devys,D., Tora,L. and Berger,I.
  TITLE     Architecture of TAF11/TAF13/TBP complex suggests novel regulation
            properties of general transcription factor TFIID
  JOURNAL   Elife 6, e30395 (2017)
   PUBMED   29111974
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Bell,B., Scheer,E. and Tora,L.
  TITLE     Identification of hTAF(II)80 delta links apoptotic signaling
            pathways to transcription factor TFIID function
  JOURNAL   Mol Cell 8 (3), 591-600 (2001)
   PUBMED   11583621
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Hisatake,K., Ohta,T., Takada,R., Guermah,M., Horikoshi,M.,
            Nakatani,Y. and Roeder,R.G.
  TITLE     Evolutionary conservation of human
            TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and
            interactions of TAFII80 with other TAFs and with general
            transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 92 (18), 8195-8199 (1995)
   PUBMED   7667268
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Weinzierl,R.O., Ruppert,S., Dynlacht,B.D., Tanese,N. and Tjian,R.
  TITLE     Cloning and expression of Drosophila TAFII60 and human TAFII70
            reveal conserved interactions with other subunits of TFIID
  JOURNAL   EMBO J 12 (13), 5303-5309 (1993)
   PUBMED   8262073
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 667)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
REFERENCE   10 (residues 1 to 667)
  AUTHORS   Mathe,G., Schwarzenberg,L., Halle-Pannenko,O. and Simmler,M.C.
  TITLE     Discussion paper: experimental and clinical immunopharmacology data
            applicable to cancer immunotherapy
  JOURNAL   Ann N Y Acad Sci 277 (00), 467-484 (1976)
   PUBMED   826207
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073842.5.
            
            On Jul 20, 2018 this sequence version replaced XP_011514844.1.
            
            Summary: Initiation of transcription by RNA polymerase II requires
            the activities of more than 70 polypeptides. The protein that
            coordinates these activities is transcription factor IID (TFIID),
            which binds to the core promoter to position the polymerase
            properly, serves as the scaffold for assembly of the remainder of
            the transcription complex, and acts as a channel for regulatory
            signals. TFIID is composed of the TATA-binding protein (TBP) and a
            group of evolutionarily conserved proteins known as TBP-associated
            factors or TAFs. TAFs may participate in basal transcription, serve
            as coactivators, function in promoter recognition or modify general
            transcription factors (GTFs) to facilitate complex assembly and
            transcription initiation. This gene encodes one of the smaller
            subunits of TFIID that binds weakly to TBP but strongly to TAF1,
            the largest subunit of TFIID. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jun 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.943045.1,
                                           SRR1803617.249603.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..667
                     /product="transcription initiation factor TFIID subunit 6
                     isoform delta"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, E, 70/85kD; transcription initiation
                     factor TFIID subunit 6; RNA polymerase II TBP-associated
                     factor subunit E; transcription initiation factor TFIID 70
                     kDa subunit; TAF6 RNA polymerase II, TATA box binding
                     protein (TBP)-associated factor, 80kDa"
                     /calculated_mol_wt=71349
     Region          12..67
                     /region_name="HFD_TAF6"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 6 (TAF6) and similar
                     proteins; cd22931"
                     /db_xref="CDD:467055"
     Site            order(38,42,46..47,49..54,62..63,66)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467055"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          132..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Region          204..420
                     /region_name="TAF6C"
                     /note="C-terminal domain of TATA Binding Protein (TBP)
                     Associated Factor 6 (TAF6); cd08050"
                     /db_xref="CDD:381749"
     Site            order(208..210,212..213,216,227..228,231,235,238..239,245)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:381749"
     Region          208..239
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          246..281
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          291..334
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          341..373
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          375..419
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          514..564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Site            514
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          601..667
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62311; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     CDS             1..667
                     /gene="TAF6"
                     /gene_synonym="ALYUS; MGC:8964; TAF(II)70; TAF(II)80;
                     TAF2E; TAFII-70; TAFII-80; TAFII70; TAFII80; TAFII85"
                     /coded_by="NM_001365003.1:347..2350"
                     /note="isoform delta is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS94153.1"
                     /db_xref="GeneID:6878"
                     /db_xref="HGNC:HGNC:11540"
                     /db_xref="MIM:602955"
ORIGIN      
        1 maeekklkls ntvlpsesmk vvaesmgiaq iqeetcqllt dedalkfmhm gkrqklttsd
       61 idyalklknv eplygfhaqe fipfrfasgg grelyfyeek evdlsdiint plprvpldvc
      121 lkahwlsieg cqpaipenpp papkeqqkae ateplksakp gqeedgplkg kgqgattadg
      181 kgkekkappl legaplrlkp rsihelsveq qlyykeitea cvgsceakra ealqsiatdp
      241 glyqmlprfs tfisegvrvn vvqnnlalli ylmrmvkalm dnptlyleky vhelipavmt
      301 civsrqlclr pdvdnhwalr dfaarlvaqi ckhfstttnn iqsritktft kswvdektpw
      361 ttrygsiagl aelghdvikt lilprlqqeg erirsvldgp vlsnidriga dhvqslllkh
      421 capvlaklrp ppdnqdayra efgslgpllc sqvvkaraqa alqaqqvnrt tltitqprpt
      481 ltlsqapqpg prtpgllkvp gsialpvqtl vsaraaappq psppptkfiv msssssapst
      541 qqvlslstsa pgsgstttsp vtttvpsvqp ivklvstatt appstapsgp gsvqkyivvs
      601 lpptgegkgg ptshpspvpp passpsplsg salcggkqea gdspppapgt pkangsqpns
      661 gspqpap
//
LOCUS       NP_060533                838 aa            linear   PRI 27-APR-2025
DEFINITION  lymphoid-specific helicase isoform 1 [Homo sapiens].
ACCESSION   NP_060533
VERSION     NP_060533.2
DBSOURCE    REFSEQ: accession NM_018063.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Consiglio,A., Venturin,M., Briguglio,S., Rossi,C., Grillo,G.,
            Bellosta,S., Cattaneo,M.G., Licciulli,F. and Battaglia,C.
  TITLE     Lost in HELLS: Disentangling the mystery of SALNR existence in
            senescence cellular models
  JOURNAL   PLoS One 18 (5), e0286104 (2023)
   PUBMED   37252915
  REMARK    GeneRIF: Lost in HELLS: Disentangling the mystery of SALNR
            existence in senescence cellular models.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Peixoto,E., Khan,A., Lewis,Z.A., Contreras-Galindo,R. and Czaja,W.
  TITLE     The Chromatin Remodeler HELLS: A New Regulator in DNA Repair,
            Genome Maintenance, and Cancer
  JOURNAL   Int J Mol Sci 23 (16), 9313 (2022)
   PUBMED   36012581
  REMARK    GeneRIF: The Chromatin Remodeler HELLS: A New Regulator in DNA
            Repair, Genome Maintenance, and Cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Liang,X., Li,L. and Fan,Y.
  TITLE     Diagnostic, Prognostic, and Immunological Roles of HELLS in
            Pan-Cancer: A Bioinformatics Analysis
  JOURNAL   Front Immunol 13, 870726 (2022)
   PUBMED   35774795
  REMARK    GeneRIF: Diagnostic, Prognostic, and Immunological Roles of HELLS
            in Pan-Cancer: A Bioinformatics Analysis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 838)
  AUTHORS   He,C. and Liu,L.
  TITLE     Hsa_circ_0072008 regulates cell proliferation, migration, and
            invasion in cervical squamous cell carcinoma via miR-1305/helicase,
            lymphoid specific (HELLS) axis
  JOURNAL   Bioengineered 13 (4), 8311-8322 (2022)
   PUBMED   35311456
  REMARK    GeneRIF: Hsa_circ_0072008 regulates cell proliferation, migration,
            and invasion in cervical squamous cell carcinoma via
            miR-1305/helicase, lymphoid specific (HELLS) axis.
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Chen,X., Li,Y., Rubio,K., Deng,B., Li,Y., Tang,Q., Mao,C., Liu,S.,
            Xiao,D., Barreto,G. and Tao,Y.
  TITLE     Lymphoid-specific helicase in epigenetics, DNA repair and cancer
  JOURNAL   Br J Cancer 126 (2), 165-173 (2022)
   PUBMED   34493821
  REMARK    GeneRIF: Lymphoid-specific helicase in epigenetics, DNA repair and
            cancer.
            Review article
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   7  (residues 1 to 838)
  AUTHORS   Sun,L.Q., Lee,D.W., Zhang,Q., Xiao,W., Raabe,E.H., Meeker,A.,
            Miao,D., Huso,D.L. and Arceci,R.J.
  TITLE     Growth retardation and premature aging phenotypes in mice with
            disruption of the SNF2-like gene, PASG
  JOURNAL   Genes Dev 18 (9), 1035-1046 (2004)
   PUBMED   15105378
REFERENCE   8  (residues 1 to 838)
  AUTHORS   Ohira,M., Morohashi,A., Nakamura,Y., Isogai,E., Furuya,K.,
            Hamano,S., Machida,T., Aoyama,M., Fukumura,M., Miyazaki,K.,
            Suzuki,Y., Sugano,S., Hirato,J. and Nakagawara,A.
  TITLE     Neuroblastoma oligo-capping cDNA project: toward the understanding
            of the genesis and biology of neuroblastoma
  JOURNAL   Cancer Lett 197 (1-2), 63-68 (2003)
   PUBMED   12880961
  REMARK    Review article
REFERENCE   9  (residues 1 to 838)
  AUTHORS   Lee,D.W., Zhang,K., Ning,Z.Q., Raabe,E.H., Tintner,S., Wieland,R.,
            Wilkins,B.J., Kim,J.M., Blough,R.I. and Arceci,R.J.
  TITLE     Proliferation-associated SNF2-like gene (PASG): a SNF2 family
            member altered in leukemia
  JOURNAL   Cancer Res 60 (13), 3612-3622 (2000)
   PUBMED   10910076
REFERENCE   10 (residues 1 to 838)
  AUTHORS   Geiman,T.M., Durum,S.K. and Muegge,K.
  TITLE     Characterization of gene expression, genomic structure, and
            chromosomal localization of Hells (Lsh)
  JOURNAL   Genomics 54 (3), 477-483 (1998)
   PUBMED   9878251
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314485.1, AF155827.1,
            BC111789.1 and BC015477.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 22, 2002 this sequence version replaced NP_060533.1.
            
            Summary: This gene encodes a lymphoid-specific helicase. Other
            helicases function in processes involving DNA strand separation,
            including replication, repair, recombination, and transcription.
            This protein is thought to be involved with cellular proliferation
            and may play a role in leukemogenesis. Alternatively spliced
            transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, Jan 2014].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF155827.1, SRR1660805.237081.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN03267750,
                                           SAMN03267752 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000348459.10/ ENSP00000239027.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.33"
     Protein         1..838
                     /product="lymphoid-specific helicase isoform 1"
                     /note="SWI/SNF2-related, matrix-associated,
                     actin-dependent regulator of chromatin, subfamily A,
                     member 6; proliferation-associated SNF2-like protein;
                     Senescence Associated Long Non-coding RNA"
                     /calculated_mol_wt=96943
     Region          94..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRZ9.1)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRZ9.1)"
     Region          220..453
                     /region_name="DEXHc_HELLS_SMARCA6"
                     /note="DEXH-box helicase domain of HELLS; cd18009"
                     /db_xref="CDD:350767"
     Region          221..>823
                     /region_name="PLN03142"
                     /note="Probable chromatin-remodeling complex ATPase chain;
                     Provisional"
                     /db_xref="CDD:215601"
     Site            order(250..256,289,354..355)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350767"
     Region          354..357
                     /region_name="DEAH box. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRZ9.1)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRZ9.1)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60848; propagated from
                     UniProtKB/Swiss-Prot (Q9NRZ9.1)"
     CDS             1..838
                     /gene="HELLS"
                     /gene_synonym="ICF4; LSH; Nbla10143; PASG; SALNR; SMARCA6"
                     /coded_by="NM_018063.5:135..2651"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7434.1"
                     /db_xref="GeneID:3070"
                     /db_xref="HGNC:HGNC:4861"
                     /db_xref="MIM:603946"
ORIGIN      
        1 mpaerpagsg gseapamveq ldtavitpam leeeeqleaa glererkmle karmswdres
       61 teiryrrlqh lleksniysk flltkmeqqq leeqkkkekl erkkeslkvk kgknsidase
      121 ekpvmrkkrg redesynise vmskeeilsv akknkkened enssstnlcv edlqknkdsn
      181 siikdrlset vrqntkfffd pvrkcngqpv pfqqpkhftg gvmrwyqveg mewlrmlwen
      241 gingiladem glgktvqcia tialmiqrgv pgpflvcgpl stlpnwmaef krftpdiptm
      301 lyhgtqeerq klvrniykrk gtlqihpvvi tsfeiamrdr nalqhcywky livdeghrik
      361 nmkcrlirel krfnadnkll ltgtplqnnl selwsllnfl lpdvfddlks feswfditsl
      421 setaediiak ereqnvlhml hqiltpfllr rlksdvalev ppkrevvvya plskkqeify
      481 taivnrtian mfgsseketi elsptgrpkr rtrksinysk iddfpnelek lisqiqpevd
      541 reravvevni pvesevnlkl qnimmllrkc cnhpylieyp idpvtqefki deelvtnsgk
      601 flildrmlpe lkkrghkvll fsqmtsmldi lmdychlrdf nfsrldgsms ysereknmhs
      661 fntdpevfif lvstragglg inltaadtvi iydsdwnpqs dlqaqdrchr igqtkpvvvy
      721 rlvtantidq kiveraaakr klekliihkn hfkggqsgln lsknfldpke lmellksrdy
      781 ereikgsrek visdkdlell ldrsdlidqm nasgpikekm gifkilense dsspeclf
//
LOCUS       NP_002442                283 aa            linear   PRI 27-APR-2025
DEFINITION  S-methyl-5'-thioadenosine phosphorylase isoform 1 [Homo sapiens].
ACCESSION   NP_002442
VERSION     NP_002442.2
DBSOURCE    REFSEQ: accession NM_002451.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Broggi,G., Massimino,M., Failla,M., Filetti,V., Rapisarda,V.,
            Ledda,C., Lombardo,C., Loreto,C., Vigneri,P. and Caltabiano,R.
  TITLE     Concordance between CDKN2A homozygous deletion and MTAP
            immunohistochemical loss in fluoroedenite-induced pleural
            mesothelioma: An immunohistochemical and molecular study on a
            single-institution series
  JOURNAL   Pathol Res Pract 259, 155350 (2024)
   PUBMED   38781764
  REMARK    GeneRIF: Concordance between CDKN2A homozygous deletion and MTAP
            immunohistochemical loss in fluoroedenite-induced pleural
            mesothelioma: An immunohistochemical and molecular study on a
            single-institution series.
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Ngoi,N.Y.L., Tang,T.Y., Gaspar,C.F., Pavlick,D.C., Buchold,G.M.,
            Scholefield,E.L., Parimi,V., Huang,R.S.P., Janovitz,T.,
            Danziger,N., Levy,M.A., Pant,S., De Armas,A.D., Kumpula,D.,
            Ross,J.S., Javle,M. and Rodon Ahnert,J.
  TITLE     Methylthioadenosine Phosphorylase Genomic Loss in Advanced
            Gastrointestinal Cancers
  JOURNAL   Oncologist 29 (6), 493-503 (2024)
   PUBMED   38330461
  REMARK    GeneRIF: Methylthioadenosine Phosphorylase Genomic Loss in Advanced
            Gastrointestinal Cancers.
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Wang,S.N., Wang,W., Zhang,X.W., Zhang,Y.Q., Xiong,Y.L., Liu,L. and
            Teng,L.H.
  TITLE     [Methylthioadenosine phosphorylase and p16 as surrogate diagnostic
            markers for CDKN2A homozygous deletion in brain tumors]
  JOURNAL   Zhonghua Bing Li Xue Za Zhi 53 (5), 439-445 (2024)
   PUBMED   38678323
  REMARK    GeneRIF: [Methylthioadenosine phosphorylase and p16 as surrogate
            diagnostic markers for CDKN2A homozygous deletion in brain tumors].
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Lin,Z., Lei,Y., Wen,M., He,Q., Tian,D. and Xie,H.
  TITLE     MTAP-ANRIL gene fusion promotes melanoma epithelial-mesenchymal
            transition-like process by activating the JNK and p38 signaling
            pathways
  JOURNAL   Sci Rep 13 (1), 9073 (2023)
   PUBMED   37277447
  REMARK    GeneRIF: MTAP-ANRIL gene fusion promotes melanoma
            epithelial-mesenchymal transition-like process by activating the
            JNK and p38 signaling pathways.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Chen,Y., Du,X., Gao,Y., Wu,H., Zhao,H. and Su,Y.
  TITLE     Methylthioadenosine Phosphorylase and Breast Cancer 1
            Protein-Associated Protein 1 as Biomarkers for the Peritoneal
            Mesothelioma
  JOURNAL   Cancer Control 30, 10732748231220805 (2023)
   PUBMED   38092371
  REMARK    GeneRIF: Methylthioadenosine Phosphorylase and Breast Cancer 1
            Protein-Associated Protein 1 as Biomarkers for the Peritoneal
            Mesothelioma.
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Martignetti,J.A., Desnick,R.J., Aliprandis,E., Norton,K.I.,
            Hardcastle,P., Nade,S. and Gelb,B.D.
  TITLE     Diaphyseal medullary stenosis with malignant fibrous histiocytoma:
            a hereditary bone dysplasia/cancer syndrome maps to 9p21-22
  JOURNAL   Am J Hum Genet 64 (3), 801-807 (1999)
   PUBMED   10053015
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Della Ragione,F., Takabayashi,K., Mastropietro,S., Mercurio,C.,
            Oliva,A., Russo,G.L., Della Pietra,V., Borriello,A., Nobori,T.,
            Carson,D.A. and Zappia,V.
  TITLE     Purification and characterization of recombinant human
            5'-methylthioadenosine phosphorylase: definite identification of
            coding cDNA
  JOURNAL   Biochem Biophys Res Commun 223 (3), 514-519 (1996)
   PUBMED   8687427
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Nobori,T., Takabayashi,K., Tran,P., Orvis,L., Batova,A., Yu,A.L.
            and Carson,D.A.
  TITLE     Genomic cloning of methylthioadenosine phosphorylase: a purine
            metabolic enzyme deficient in multiple different cancers
  JOURNAL   Proc Natl Acad Sci U S A 93 (12), 6203-6208 (1996)
   PUBMED   8650244
REFERENCE   9  (residues 1 to 283)
  AUTHORS   Olopade,O.I., Pomykala,H.M., Hagos,F., Sveen,L.W., Espinosa,R. 3rd,
            Dreyling,M.H., Gursky,S., Stadler,W.M., Le Beau,M.M. and
            Bohlander,S.K.
  TITLE     Construction of a 2.8-megabase yeast artificial chromosome contig
            and cloning of the human methylthioadenosine phosphorylase gene
            from the tumor suppressor region on 9p21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6489-6493 (1995)
   PUBMED   7604019
REFERENCE   10 (residues 1 to 283)
  AUTHORS   Carrera,C.J., Eddy,R.L., Shows,T.B. and Carson,D.A.
  TITLE     Assignment of the gene for methylthioadenosine phosphorylase to
            human chromosome 9 by mouse-human somatic cell hybridization
  JOURNAL   Proc Natl Acad Sci U S A 81 (9), 2665-2668 (1984)
   PUBMED   6425836
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U22233.1, L40432.1, BC026106.1,
            BM994282.1, BQ220538.1, BQ232183.1, BG576334.1, AK024734.1,
            CA440131.1 and AL359922.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 12, 2004 this sequence version replaced NP_002442.1.
            
            Summary: This gene encodes an enzyme that plays a major role in
            polyamine metabolism and is important for the salvage pathway of
            both adenine and methionine. The encoded enzyme is deficient in
            many cancers. Multiple alternatively spliced transcript variants
            have been described for this gene. [provided by RefSeq, Sep 2021].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GQ891397.1, SRR1660805.213756.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000644715.2/ ENSP00000494373.1
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.3"
     Protein         1..283
                     /product="S-methyl-5'-thioadenosine phosphorylase isoform
                     1"
                     /EC_number="2.4.2.28"
                     /note="MeSAdo phosphorylase; S-methyl-5'-thioadenosine
                     phosphorylase; MTAPase; MTA phosphorylase;
                     5'-methylthioadenosine phosphorylase; epididymis luminal
                     protein 249; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=31105
     Region          12..255
                     /region_name="MTAP_SsMTAPII_like_MTIP"
                     /note="5'-deoxy-5'-methylthioadenosine phosphorylases
                     (MTAP) similar to Sulfolobus solfataricus MTAPII and
                     Pseudomonas aeruginosa PAO1 5'-methylthioinosine
                     phosphorylase (MTIP); cd09010"
                     /db_xref="CDD:350161"
     Site            order(17,60..61,69,93..96,137,172,177,194..197,219..220,
                     222,233,236)
                     /site_type="active"
                     /db_xref="CDD:350161"
     Site            order(17,60..61,93..94,197)
                     /site_type="other"
                     /note="phosphate binding site [ion binding]"
                     /db_xref="CDD:350161"
     Site            51
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ65; propagated from
                     UniProtKB/Swiss-Prot (Q13126.2)"
     Site            order(67..71,112..116,122..123,125..126,137..141,175..182,
                     185,189..190,196,203,223,233)
                     /site_type="other"
                     /note="homohexamer interface [polypeptide binding]"
                     /db_xref="CDD:350161"
     Site            178
                     /site_type="other"
                     /note="Important for substrate specificity; propagated
                     from UniProtKB/Swiss-Prot (Q13126.2)"
     Site            233
                     /site_type="other"
                     /note="Important for substrate specificity; propagated
                     from UniProtKB/Swiss-Prot (Q13126.2)"
     CDS             1..283
                     /gene="MTAP"
                     /gene_synonym="BDMF; c86fus; DMSFH; DMSMFH; HEL-249;
                     LGMBF; MSAP"
                     /coded_by="NM_002451.4:114..965"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6509.1"
                     /db_xref="GeneID:4507"
                     /db_xref="HGNC:HGNC:7413"
                     /db_xref="MIM:156540"
ORIGIN      
        1 masgttttav kigiiggtgl ddpeilegrt ekyvdtpfgk psdalilgki knvdcvllar
       61 hgrqhtimps kvnyqaniwa lkeegcthvi vttacgslre eiqpgdivii dqfidrttmr
      121 pqsfydgshs cargvchipm aepfcpktre vlietakklg lrchskgtmv tiegprfssr
      181 aesfmfrtwg advinmttvp evvlakeagi cyasiamatd ydcwkeheea vsvdrvlktl
      241 kenankaksl llttipqigs tewsetlhnl knmaqfsvll prh
//
LOCUS       NP_001352717             421 aa            linear   PRI 27-APR-2025
DEFINITION  acyl-coenzyme A thioesterase 6 isoform 1 [Homo sapiens].
ACCESSION   NP_001352717 XP_011535378
VERSION     NP_001352717.1
DBSOURCE    REFSEQ: accession NM_001365788.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Xu,B., Roos,J.L., Dexheimer,P., Boone,B., Plummer,B., Levy,S.,
            Gogos,J.A. and Karayiorgou,M.
  TITLE     Exome sequencing supports a de novo mutational paradigm for
            schizophrenia
  JOURNAL   Nat Genet 43 (9), 864-868 (2011)
   PUBMED   21822266
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Hunt,M.C., Rautanen,A., Westin,M.A., Svensson,L.T. and Alexson,S.E.
  TITLE     Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene
            clusters shows that convergent, functional evolution results in a
            reduced number of human peroxisomal ACOTs
  JOURNAL   FASEB J 20 (11), 1855-1864 (2006)
   PUBMED   16940157
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Hunt,M.C., Yamada,J., Maltais,L.J., Wright,M.W., Podesta,E.J. and
            Alexson,S.E.
  TITLE     A revised nomenclature for mammalian acyl-CoA
            thioesterases/hydrolases
  JOURNAL   J Lipid Res 46 (9), 2029-2032 (2005)
   PUBMED   16103133
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005225.2.
            
            On Sep 12, 2018 this sequence version replaced XP_011535378.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000645972.2/ ENSP00000496277.1
            RefSeq Select criteria    :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..421
                     /product="acyl-coenzyme A thioesterase 6 isoform 1"
                     /EC_number="3.1.2.2"
                     /note="putative acyl-coenzyme A thioesterase 6; putative
                     acyl-CoA thioesterase 6"
                     /calculated_mol_wt=46658
     Region          16..140
                     /region_name="Bile_Hydr_Trans"
                     /note="Acyl-CoA thioester hydrolase/BAAT N-terminal
                     region; pfam04775"
                     /db_xref="CDD:461422"
     Region          203..412
                     /region_name="BAAT_C"
                     /note="BAAT / Acyl-CoA thioester hydrolase C terminal;
                     pfam08840"
                     /db_xref="CDD:430252"
     Region          419..421
                     /region_name="Peroxisome targeting signal.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3I5F7.2)"
     CDS             1..421
                     /gene="ACOT6"
                     /gene_synonym="C14orf42; c14_5530"
                     /coded_by="NM_001365788.1:56..1321"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS91900.1"
                     /db_xref="GeneID:641372"
                     /db_xref="HGNC:HGNC:33159"
                     /db_xref="MIM:614267"
ORIGIN      
        1 maatlilepa grccwdeplr iavrglapeq pvtlrtslrd eegalfraha ryradardel
       61 dlerapalgg sfaglqpmgl lwalepekal vrlvkrdvrt pfavelevld ghdtepgrll
      121 claqnkrdfl rpgvrrepvr agpvraalfl ppdegpfpgi idlfgssrgl ceyrasllag
      181 hgfavlalay frfedlpedl ndvhleyfee avdfmlqhpk vkgpsiallg fskggdlcls
      241 masflkgita tvlinacvan tvaplhykdm iipklvddlg kvkitksgfl tfmdtwsnpl
      301 eehnhqslvp lekaqvpflf ivgmddqswk sefyaqiase rlqahgkerp qiicypetgh
      361 cidppyfpps rasvhavlge aifyggepka hskaqvdawq qiqtffhkhl ngkksvkhsk
      421 i
//
LOCUS       NP_055799               1080 aa            linear   PRI 27-APR-2025
DEFINITION  centrosomal protein of 131 kDa isoform a [Homo sapiens].
ACCESSION   NP_055799 XP_045581
VERSION     NP_055799.2
DBSOURCE    REFSEQ: accession NM_014984.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Shen,M., Li,S., Zhao,Y., Liu,Y., Liu,Z., Huan,L., Qiao,Y., Wang,L.,
            Han,L., Chen,Z. and He,X.
  TITLE     Hepatic ARID3A facilitates liver cancer malignancy by cooperating
            with CEP131 to regulate an embryonic stem cell-like gene signature
  JOURNAL   Cell Death Dis 13 (8), 732 (2022)
   PUBMED   36008383
  REMARK    GeneRIF: Hepatic ARID3A facilitates liver cancer malignancy by
            cooperating with CEP131 to regulate an embryonic stem cell-like
            gene signature.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Kim,D.H., Ahn,J.S., Han,H.J., Kim,H.M., Hwang,J., Lee,K.H.,
            Cha-Molstad,H., Ryoo,I.J., Jang,J.H., Ko,S.K., Yang,J.O., Lee,H.G.,
            Lee,S., Song,E.J., Kim,J.Y., Huh,Y.H., Kwon,Y.T., Soung,N.K. and
            Kim,B.Y.
  TITLE     Cep131 overexpression promotes centrosome amplification and colon
            cancer progression by regulating Plk4 stability
  JOURNAL   Cell Death Dis 10 (8), 570 (2019)
   PUBMED   31358734
  REMARK    GeneRIF: These findings demonstrate that Cep131 is a novel
            substrate of Plk4, and that phosphorylation or dysregulated Cep131
            overexpression promotes Plk4 stabilization and therefore centrosome
            amplification, establishing a perspective in understanding a
            relationship between centrosome amplification and cancer
            development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1080)
  AUTHORS   Denu,R.A., Sass,M.M., Johnson,J.M., Potts,G.K., Choudhary,A.,
            Coon,J.J. and Burkard,M.E.
  TITLE     Polo-like kinase 4 maintains centriolar satellite integrity by
            phosphorylation of centrosomal protein 131 (CEP131)
  JOURNAL   J Biol Chem 294 (16), 6531-6549 (2019)
   PUBMED   30804208
  REMARK    GeneRIF: PLK4 phosphorylates CEP131 at Ser-78 to maintain
            centriolar satellite integrity.
REFERENCE   5  (residues 1 to 1080)
  AUTHORS   Gupta,S.K., Luo,L. and Yen,L.
  TITLE     RNA-mediated gene fusion in mammalian cells
  JOURNAL   Proc Natl Acad Sci U S A 115 (52), E12295-E12304 (2018)
   PUBMED   30538195
  REMARK    GeneRIF: RNA of AZI1 functions as the 'initiator' RNA to induce
            TMPRSS2-ERG fusion.
REFERENCE   6  (residues 1 to 1080)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   7  (residues 1 to 1080)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   8  (residues 1 to 1080)
  AUTHORS   Aoto,H., Miyake,Y., Nakamura,M. and Tajima,S.
  TITLE     Genomic organization of the mouse AZ1 gene that encodes the protein
            localized to preacrosomes of spermatids
  JOURNAL   Genomics 40 (1), 138-141 (1997)
   PUBMED   9070930
REFERENCE   9  (residues 1 to 1080)
  AUTHORS   Aoto,H., Tsuchida,J., Nishina,Y., Nishimune,Y., Asano,A. and
            Tajima,S.
  TITLE     Isolation of a novel cDNA that encodes a protein localized to the
            pre-acrosome region of spermatids
  JOURNAL   Eur J Biochem 234 (1), 8-15 (1995)
   PUBMED   8529672
REFERENCE   10 (residues 1 to 1080)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027601.25.
            
            On Aug 11, 2006 this sequence version replaced NP_055799.1.
            
            Transcript Variant: This variant (1) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 3. This
            results in a shorter protein (isoform a), compared to isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC136578.1, DRR138512.201054.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000450824.7/ ENSP00000393583.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..1080
                     /product="centrosomal protein of 131 kDa isoform a"
                     /note="pre-acrosome localization protein 1; 5-azacytidine
                     induced 1; centrosomal protein 131 kDa;
                     5-azacytidine-induced protein 1; centrosomal protein of
                     131 kDa; centrosomal protein 131kDa"
                     /calculated_mol_wt=121717
     Region          1..250
                     /region_name="Interaction with PLK4.
                     /evidence=ECO:0000269|PubMed:30804208"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Region          1..155
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62036; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2 and PLK4.
                     /evidence=ECO:0000269|PubMed:30804208,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Region          220..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Region          301..429
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62036; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Region          <573..>1074
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26616734; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN4.3)"
     Region          1044..1080
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPN4.3)"
     CDS             1..1080
                     /gene="CEP131"
                     /gene_synonym="AZ1; AZI1; ZA1"
                     /coded_by="NM_014984.4:215..3457"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45808.1"
                     /db_xref="GeneID:22994"
                     /db_xref="HGNC:HGNC:29511"
                     /db_xref="MIM:613479"
ORIGIN      
        1 mkgtraigsv perspagvdl sltglpppvs rrpgsaattk pivrsvsvvt gseqkrkvle
       61 atgpggsqai nnlrrsnstt qvsqprsgsp rpteptdflm lfegspsgkk rpaslstaps
      121 ekgatwnvld dqprgftlps narsssalds pagprrkect valapnftan nrsnkgavgn
      181 cvttmvhnry tpserapplk ssnqtapsln niikaatceg sessgfgklp knvssathsa
      241 rnntggstgl prrkevteee aerfihqvnq atvtiqrwyr hqvqrrgaga arlehllqak
      301 reeqrqrsge gtlldlhqqk eaarrkaree karqarraai qelqqkralr aqkastaerg
      361 ppenpretrv pgmrqpaqel sptpggtahq alkanntggg lpaagpgdrc lptsdsspep
      421 qqppedrtqd vlaqdaagdn lemmapsrgs aksrgpleel lhtlqlleke pdvlprprth
      481 hrgryawase eddassltad nlekfgklsa fpeppedgtl lseaklqsim sfldemeksg
      541 qdqldsqqeg wvpeagpgpl elgsevstsv mrlkleveek kqamlllqra laqqrdltar
      601 rvketekals rqlqrqrehy eatiqrhlaf idqliedkkv lsekceavva elkqedqrct
      661 ervaqaqaqh eleikklkel msatekarre kwisektkki kevtvrglep eiqkliarhk
      721 qevrrlkslh eaellqsder asqrclrqae elreqlerek ealgqqerer arqrfqqhle
      781 qeqwalqqqr qrlysevaee rerlgqqaar qraeleelrq qleesssalt ralraefekg
      841 reeqerrhqm elntlkqqle lerqaweagr trkeeawlln reqelreeir kgrdkeielv
      901 ihrleadmal akeesekaae srikrlrdky eaelseleqs erklqercse lkgqlgeaeg
      961 enlrlqglvr qkeraledaq avneqlsser snlaqvirqe fedrlaasee etrqakaela
     1021 tlqarqqlel eevhrrvkta larkeeavss lrtqheaavk radhleelle qhrrptpstk
//
LOCUS       NP_075379                370 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane 6 superfamily member 1 isoform 1 [Homo sapiens].
ACCESSION   NP_075379
VERSION     NP_075379.2
DBSOURCE    REFSEQ: accession NM_023003.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Huang,S., Zhao,H., Lou,X., Chen,D., Shi,C. and Ren,Z.
  TITLE     TM6SF1 suppresses the progression of lung adenocarcinoma and M2
            macrophage polarization by inactivating the PI3K/AKT/mtor pathway
  JOURNAL   Biochem Biophys Res Commun 718, 149983 (2024)
   PUBMED   38718735
  REMARK    GeneRIF: TM6SF1 suppresses the progression of lung adenocarcinoma
            and M2 macrophage polarization by inactivating the PI3K/AKT/mtor
            pathway.
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Li,T.T., Cui,Y.T., Li,T.H., Xiang,Q., Chen,Y.Y., Zheng,X.L.,
            Peng,J. and Tang,Z.H.
  TITLE     TM6SF2 reduces lipid accumulation in vascular smooth muscle cells
            by inhibiting LOX-1 and CD36 expression
  JOURNAL   Exp Cell Res 429 (2), 113666 (2023)
   PUBMED   37271250
  REMARK    GeneRIF: TM6SF2 reduces lipid accumulation in vascular smooth
            muscle cells by inhibiting LOX-1 and CD36 expression.
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Tam,W.Y., Jiang,L. and Kwan,K.M.
  TITLE     Transmembrane 6 superfamily 1 (Tm6sf1) is a novel lysosomal
            transmembrane protein
  JOURNAL   Protoplasma 252 (4), 977-983 (2015)
   PUBMED   25422095
REFERENCE   5  (residues 1 to 370)
  AUTHORS   de Groot,J.S., Pan,X., Meeldijk,J., van der Wall,E., van Diest,P.J.
            and Moelans,C.B.
  TITLE     Validation of DNA promoter hypermethylation biomarkers in breast
            cancer--a short report
  JOURNAL   Cell Oncol (Dordr) 37 (4), 297-303 (2014)
   PUBMED   25123395
  REMARK    GeneRIF: Data conclude that AKR1B1 and TM6SF1 may serve as
            candidate methylation biomarkers for early breast cancer detection.
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Carim-Todd,L., Escarceller,M., Estivill,X. and Sumoy,L.
  TITLE     Cloning of the novel gene TM6SF1 reveals conservation of clusters
            of paralogous genes between human chromosomes 15q24-->q26 and
            19p13.3-->p12
  JOURNAL   Cytogenet Cell Genet 90 (3-4), 255-260 (2000)
   PUBMED   11124529
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC024270.6, AK292100.1 and BC063487.1.
            
            On Jan 29, 2009 this sequence version replaced NP_075379.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.201509.1,
                                           SRR1660805.128509.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322019.14/ ENSP00000317000.9
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..370
                     /product="transmembrane 6 superfamily member 1 isoform 1"
                     /calculated_mol_wt=41505
     Site            3..23
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZW5.2)"
     Region          6..360
                     /region_name="TM6SF1-like"
                     /note="transmembrane 6 superfamily member 1, member 2, and
                     similar proteins; cd21106"
                     /db_xref="CDD:411047"
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZW5.2)"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZW5.2)"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZW5.2)"
     Site            139..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZW5.2)"
     Site            166..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZW5.2)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZW5.2)"
     Site            268..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZW5.2)"
     Site            331..351
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZW5.2)"
     CDS             1..370
                     /gene="TM6SF1"
                     /coded_by="NM_023003.5:37..1149"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10323.1"
                     /db_xref="GeneID:53346"
                     /db_xref="HGNC:HGNC:11860"
                     /db_xref="MIM:606562"
ORIGIN      
        1 msasaatgvf vlslsaipvt yvfnhlaaqh dswtivgvaa lilflvalla rvlvkrkppr
       61 dplfyvyavf gftsvvnlii gleqdgiidg fmthylrege pylntayghm icywdgsahy
      121 lmylvmvaai aweetyrtig lywvgsiims vvvfvpgniv gkygtricpa fflsipytcl
      181 pvwagfriyn qpsenynyps kviqeaqakd llrrpfdlml vvclllatgf clfrgliald
      241 cpselcrlyt qfqepylkdp aaypkiqmla ymfysvpyfv talyglvvpg cswmpditli
      301 hagglaqaqf shigaslhar tayvyrvpee akilflalni aygvlpqlla yrciykpeff
      361 iktkaeekve
//
LOCUS       NP_001124427            1119 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 18 isoform b [Homo sapiens].
ACCESSION   NP_001124427
VERSION     NP_001124427.2
DBSOURCE    REFSEQ: accession NM_001130955.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Li,D., Sun,Y., Kong,X., Luan,C., Yu,Y., Chen,F. and Chen,P.
  TITLE     Association between a Single Nucleotide Polymorphism in the 3'-UTR
            of ARHGEF18 and the Risk of Nonidiopathic Pulmonary Arterial
            Hypertension in Chinese Population
  JOURNAL   Dis Markers 2018, 2461845 (2018)
   PUBMED   30405854
  REMARK    GeneRIF: ARHGEF18 rs3745357 variant is associated with
            nonidiopathic pulmonary arterial hypertension susceptibility in
            Chinese population.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Turton,K.B., Wilkerson,E.M., Hebert,A.S., Fogerty,F.J.,
            Schira,H.M., Botros,F.E., Coon,J.J. and Mosher,D.F.
  TITLE     Expression of novel 'LOCGEF' isoforms of ARHGEF18 in eosinophils
  JOURNAL   J Leukoc Biol 104 (1), 135-145 (2018)
   PUBMED   29601110
  REMARK    GeneRIF: We suggest that a portion of a 1361-residue isoform of
            ARHGEF18, which is unlike any other protein domain, has unique
            functions in control of polarity in activated eosinophils and other
            leukocytes
REFERENCE   4  (residues 1 to 1119)
  AUTHORS   Arno,G., Carss,K.J., Hull,S., Zihni,C., Robson,A.G., Fiorentino,A.,
            Hardcastle,A.J., Holder,G.E., Cheetham,M.E., Plagnol,V.,
            Moore,A.T., Raymond,F.L., Matter,K., Balda,M.S. and Webster,A.R.
  CONSRTM   UK Inherited Retinal Disease Consortium; NIHR Bioresource - Rare
            Diseases Consortium
  TITLE     Biallelic Mutation of ARHGEF18, Involved in the Determination of
            Epithelial Apicobasal Polarity, Causes Adult-Onset Retinal
            Degeneration
  JOURNAL   Am J Hum Genet 100 (2), 334-342 (2017)
   PUBMED   28132693
  REMARK    GeneRIF: mutation of ARHGEF18 is a likely cause of inherited
            retinal dystrophy
REFERENCE   5  (residues 1 to 1119)
  AUTHORS   Loie,E., Charrier,L.E., Sollier,K., Masson,J.Y. and Laprise,P.
  TITLE     CRB3A Controls the Morphology and Cohesion of Cancer Cells through
            Ehm2/p114RhoGEF-Dependent Signaling
  JOURNAL   Mol Cell Biol 35 (19), 3423-3435 (2015)
   PUBMED   26217016
  REMARK    GeneRIF: CRB3A recruits p114RhoGEF and its activator Ehm2 to the
            cell periphery using both functional motifs of its cytoplasmic tail
            and increases RhoA activation levels.
REFERENCE   6  (residues 1 to 1119)
  AUTHORS   Rabizadeh,S. and Bredesen,D.E.
  TITLE     Ten years on: mediation of cell death by the common neurotrophin
            receptor p75(NTR)
  JOURNAL   Cytokine Growth Factor Rev 14 (3-4), 225-239 (2003)
   PUBMED   12787561
  REMARK    Review article
REFERENCE   7  (residues 1 to 1119)
  AUTHORS   Salehi,A.H., Xanthoudakis,S. and Barker,P.A.
  TITLE     NRAGE, a p75 neurotrophin receptor-interacting protein, induces
            caspase activation and cell death through a JNK-dependent
            mitochondrial pathway
  JOURNAL   J Biol Chem 277 (50), 48043-48050 (2002)
   PUBMED   12376548
REFERENCE   8  (residues 1 to 1119)
  AUTHORS   Harrington,A.W., Kim,J.Y. and Yoon,S.O.
  TITLE     Activation of Rac GTPase by p75 is necessary for c-jun N-terminal
            kinase-mediated apoptosis
  JOURNAL   J Neurosci 22 (1), 156-166 (2002)
   PUBMED   11756498
REFERENCE   9  (residues 1 to 1119)
  AUTHORS   Acierno,J.S. Jr., Kennedy,J.C., Falardeau,J.L., Leyne,M.,
            Bromley,M.C., Colman,M.W., Sun,M., Bove,C., Ashworth,L.K.,
            Chadwick,L.H., Schiripo,T., Ma,S., Goldin,E., Schiffmann,R. and
            Slaugenhaupt,S.A.
  TITLE     A physical and transcript map of the MCOLN1 gene region on human
            chromosome 19p13.3-p13.2
  JOURNAL   Genomics 73 (2), 203-210 (2001)
   PUBMED   11318610
REFERENCE   10 (residues 1 to 1119)
  AUTHORS   Blomquist,A., Schworer,G., Schablowski,H., Psoma,A., Lehnen,M.,
            Jakobs,K.H. and Rumenapp,U.
  TITLE     Identification and characterization of a novel Rho-specific guanine
            nucleotide exchange factor
  JOURNAL   Biochem J 352 Pt 2 (Pt 2), 319-325 (2000)
   PUBMED   11085924
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK127045.1, AC008878.10,
            AB011093.1 and AA609742.1.
            
            On Dec 19, 2018 this sequence version replaced NP_001124427.1.
            
            Summary: Rho GTPases are GTP binding proteins that regulate a wide
            spectrum of cellular functions. These cellular processes include
            cytoskeletal rearrangements, gene transcription, cell growth and
            motility. Activation of Rho GTPases is under the direct control of
            guanine nucleotide exchange factors (GEFs). The protein encoded by
            this gene is a guanine nucleotide exchange factor and belongs to
            the Rho GTPase GEF family. Family members share a common feature, a
            Dbl (DH) homology domain followed by a pleckstrin (PH) homology
            domain. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Nov
            2018].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1119
                     /product="rho guanine nucleotide exchange factor 18
                     isoform b"
                     /note="Rho-specific guanine nucleotide exchange factor
                     p114; septin-associated RhoGEF; 114 kDa Rho-specific
                     guanine nucleotide exchange factor; Rho/Rac guanine
                     nucleotide exchange factor (GEF) 18"
                     /calculated_mol_wt=125309
     Region          206..400
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(212,216,323,351..352,355..356,358..359,362..363,
                     366..367,370,396,400)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          440..558
                     /region_name="PH_ARHGEF18"
                     /note="Rho guanine nucleotide exchange factor 18
                     Pleckstrin homology (PH) domain; cd15794"
                     /db_xref="CDD:275437"
     Region          <746..>892
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          842..>986
                     /region_name="PRK13729"
                     /note="conjugal transfer pilus assembly protein TraB;
                     Provisional"
                     /db_xref="CDD:184281"
     CDS             1..1119
                     /gene="ARHGEF18"
                     /gene_synonym="P114-RhoGEF; p114RhoGEF; RP78; SA-RhoGEF"
                     /coded_by="NM_001130955.2:416..3775"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45946.2"
                     /db_xref="GeneID:23370"
                     /db_xref="HGNC:HGNC:17090"
                     /db_xref="MIM:616432"
ORIGIN      
        1 mgnahsksgd rhsalpgrpe lsfygsfprk wsenvfldne lltskilsvl rpqsergfra
       61 gdlrypthfl stnsvlasvt aslkehprgt llsdgspals rnvgmtvsqk ggpqptpspa
      121 gpgtqlgpit gemdeadsaf lkfkqtadds lsltspntes ifvedpytas lrseiesdgh
      181 efeaeswsla vdaayakkqk revvkrqdvl yelmqtevhh vrtlkimlkv ysralqeelq
      241 fsskaigrlf pcaddlleth shflarlker rqesleegsd rnyviqkigd llvqqfsgen
      301 germkekygv fcsghneavs hyklllqqnk kfqnlikkig nfsivrrlgv qecillvtqr
      361 itkypvlver iiqnteagte dyedltqaln likdiisqvd akvsecekgq rlreiagkmd
      421 lksssklkng ltfrkedmlq rqlhlegmlc wkttsgrlkd ilailltdvl lllqekdqky
      481 vfasvdskpp vislqklivr evaneekamf lisaslqgpe myeiytsske drnawmahiq
      541 ravescpdee egpfslpeee rkvvearatr lrdfqerlsm kdqliaqsll ekqqiylema
      601 emggledlpq prglfrggdp setlqgelil ksamseiegi qslicrqlgs angqaedggs
      661 stgpprraet fagydctnsp tkngsfkkkv sstdprprdw rgppnspdlk lsdsdipgss
      721 eespqvveap gtesdprlpt vleselvqri qtlsqlllnl qaviahqdsy vetqraaiqe
      781 rekqfrlqst rgnllleqer qrnfekqree raaleklqsq lrheqqrwer erqwqhqele
      841 ragarlqere gearqlrerl eqeraelerq rqayqhdler lreaqraver ererlellrr
      901 lkkqntapga lppdtlaeaq ppshppsfng eglegprvsm lpsgvgpeya erpevarrds
      961 aptenrlaks dvpiqllsat nqfqrqaavq qqiptklaas tkggkdkggk srgsqrwess
     1021 asfdlkqqll lnklmgkdes tsrnrrslsp ilpgrhspap ppdpgfpaps pppadspseg
     1081 fslkaggtal lpgppapspl patplsaked askedviff
//
LOCUS       NP_808339                292 aa            linear   ROD 27-APR-2025
DEFINITION  ephrin type-A receptor 10 isoform 2 precursor [Mus musculus].
ACCESSION   NP_808339 XP_003085478 XP_003086421
VERSION     NP_808339.2
DBSOURCE    REFSEQ: accession NM_177671.6
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Agrawal,P., Wang,M., Kim,S., Lewis,A.E. and Bush,J.O.
  TITLE     Embryonic expression of EphA receptor genes in mice supports their
            candidacy for involvement in cleft lip and palate
  JOURNAL   Dev Dyn 243 (11), 1470-1476 (2014)
   PUBMED   25073978
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Thompson,C.L., Ng,L., Menon,V., Martinez,S., Lee,C.K.,
            Glattfelder,K., Sunkin,S.M., Henry,A., Lau,C., Dang,C.,
            Garcia-Lopez,R., Martinez-Ferre,A., Pombero,A., Rubenstein,J.L.R.,
            Wakeman,W.B., Hohmann,J., Dee,N., Sodt,A.J., Young,R., Smith,K.,
            Nguyen,T.N., Kidney,J., Kuan,L., Jeromin,A., Kaykas,A., Miller,J.,
            Page,D., Orta,G., Bernard,A., Riley,Z., Smith,S., Wohnoutka,P.,
            Hawrylycz,M.J., Puelles,L. and Jones,A.R.
  TITLE     A high-resolution spatiotemporal atlas of gene expression of the
            developing mouse brain
  JOURNAL   Neuron 83 (2), 309-323 (2014)
   PUBMED   24952961
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Xia,Y., Luo,C., Dai,S. and Yao,D.
  TITLE     Increased EphA/ephrinA expression in hippocampus of pilocarpine
            treated mouse
  JOURNAL   Epilepsy Res 105 (1-2), 20-29 (2013)
   PUBMED   23352741
  REMARK    GeneRIF: Ephrin A10 is significantly increased in hippocampus
            following epileptogenesis.
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Zirzow,S., Ludtke,T.H., Brons,J.F., Petry,M., Christoffels,V.M. and
            Kispert,A.
  TITLE     Expression and requirement of T-box transcription factors Tbx2 and
            Tbx3 during secondary palate development in the mouse
  JOURNAL   Dev Biol 336 (2), 145-155 (2009)
   PUBMED   19769959
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Freywald,A., Sharfe,N., Miller,C.D., Rashotte,C. and Roifman,C.M.
  TITLE     EphA receptors inhibit anti-CD3-induced apoptosis in thymocytes
  JOURNAL   J Immunol 176 (7), 4066-4074 (2006)
   PUBMED   16547242
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Corbo,J.C. and Cepko,C.L.
  TITLE     A hybrid photoreceptor expressing both rod and cone genes in a
            mouse model of enhanced S-cone syndrome
  JOURNAL   PLoS Genet 1 (2), e11 (2005)
   PUBMED   16110338
  REMARK    Erratum:[PLoS Genet. 2008 Jan;4(1):e18]
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Aasheim,H.C., Patzke,S., Hjorthaug,H.S. and Finne,E.F.
  TITLE     Characterization of a novel Eph receptor tyrosine kinase, EphA10,
            expressed in testis
  JOURNAL   Biochim Biophys Acta 1723 (1-3), 1-7 (2005)
   PUBMED   15777695
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK143168.1.
            
            On or before Jan 27, 2012 this sequence version replaced
            XP_003085478.1, XP_003086421.1, NP_808339.1.
            
            Transcript Variant: This variant (2) lacks several exons and its
            transcription extends past a splice site that is used in variant 1,
            resulting in a novel 3' coding region and 3' UTR compared to
            variant 1. It encodes isoform 2 which is shorter and has a distinct
            C-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK143168.1, SRR1660813.16647.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849379, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 57.92 cM"
     Protein         1..292
                     /product="ephrin type-A receptor 10 isoform 2 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 10"
                     /calculated_mol_wt=28455
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3156
     Region          35..210
                     /region_name="EphR_LBD"
                     /note="Ligand Binding Domain of Ephrin Receptors; cl02704"
                     /db_xref="CDD:470656"
     Site            order(47,59..62,64..65,70,72,75,108,110,161,169..171,
                     198..200,202)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198439"
     CDS             1..292
                     /gene="Epha10"
                     /gene_synonym="A330090H18"
                     /coded_by="NM_177671.6:91..969"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS18630.1"
                     /db_xref="GeneID:230735"
                     /db_xref="MGI:MGI:3586824"
ORIGIN      
        1 metgagphpl rlfvcliplc lalllgpgrp gtaeevilld skasqaelgw talpstgwee
       61 isgvdehdrp irtyqvcnvl epnqdnwlqt gwisrgrgqr ifvelqftlr dcssipgatg
      121 tcketfnayy letetdlgrg rprlggnrpr kidtiaades ftqgdlgerk mklntevrei
      181 gplsrqgfhl afqdvgacva lvsvrvyykq cratvrglaa fpataaesaf stlvevagtc
      241 vahsegepss pprmhcgadg ewlvpvgrcs csagfqehgd icegiqgprg mg
//
LOCUS       NP_066952                289 aa            linear   PRI 27-APR-2025
DEFINITION  inorganic pyrophosphatase [Homo sapiens].
ACCESSION   NP_066952
VERSION     NP_066952.1
DBSOURCE    REFSEQ: accession NM_021129.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Zheng,S., Zheng,C., Chen,S., Guo,J., Huang,L., Huang,Z., Xu,S.,
            Wu,Y., Li,S., Lin,J., You,Y. and Hu,F.
  TITLE     Structural and biochemical characterization of active sites mutant
            in human inorganic pyrophosphatase
  JOURNAL   Biochim Biophys Acta Gen Subj 1868 (5), 130594 (2024)
   PUBMED   38428647
  REMARK    GeneRIF: Structural and biochemical characterization of active
            sites mutant in human inorganic pyrophosphatase.
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Kirkbride,J.A., Nilsson,G.Y., Kim,J.I., Takeya,K., Tanaka,Y.,
            Tokumitsu,H., Suizu,F. and Eto,M.
  TITLE     PHI-1, an Endogenous Inhibitor Protein for Protein Phosphatase-1
            and a Pan-Cancer Marker, Regulates Raf-1 Proteostasis
  JOURNAL   Biomolecules 13 (12), 1741 (2023)
   PUBMED   38136612
  REMARK    GeneRIF: PHI-1, an Endogenous Inhibitor Protein for Protein
            Phosphatase-1 and a Pan-Cancer Marker, Regulates Raf-1
            Proteostasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Niu,T., Zhu,J., Dong,L., Yuan,P., Zhang,L. and Liu,D.
  TITLE     Inorganic pyrophosphatase 1 activates the phosphatidylinositol
            3-kinase/Akt signaling to promote tumorigenicity and stemness
            properties in colorectal cancer
  JOURNAL   Cell Signal 108, 110693 (2023)
   PUBMED   37141926
  REMARK    GeneRIF: Inorganic pyrophosphatase 1 activates the
            phosphatidylinositol 3-kinase/Akt signaling to promote
            tumorigenicity and stemness properties in colorectal cancer.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Troyanovsky,R.B., Indra,I., Kato,R., Mitchell,B.J. and
            Troyanovsky,S.M.
  TITLE     Basolateral protein Scribble binds phosphatase PP1 to establish a
            signaling network maintaining apicobasal polarity
  JOURNAL   J Biol Chem 297 (5), 101289 (2021)
   PUBMED   34634305
  REMARK    GeneRIF: Basolateral protein Scribble binds phosphatase PP1 to
            establish a signaling network maintaining apicobasal polarity.
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Saidy,B., Kotecha,S., Butler,A., Rakha,E.A., Ellis,I.O.,
            Green,A.R., Martin,S.G. and Storr,S.J.
  TITLE     PP1, PKA and DARPP-32 in breast cancer: A retrospective assessment
            of protein and mRNA expression
  JOURNAL   J Cell Mol Med 25 (11), 5015-5024 (2021)
   PUBMED   33991172
  REMARK    GeneRIF: PP1, PKA and DARPP-32 in breast cancer: A retrospective
            assessment of protein and mRNA expression.
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Fukami,M.H., Dangelmaier,C.A., Bauer,J.S. and Holmsen,H.
  TITLE     Secretion, subcellular localization and metabolic status of
            inorganic pyrophosphate in human platelets. A major constituent of
            the amine-storing granules
  JOURNAL   Biochem J 192 (1), 99-105 (1980)
   PUBMED   6118133
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Thuillier,L.
  TITLE     Purification and kinetic properties of human erythrocyte
            Mg2+-dependent inorganic pyrophosphatase
  JOURNAL   Biochim Biophys Acta 524 (1), 198-206 (1978)
   PUBMED   656444
REFERENCE   8  (residues 1 to 289)
  AUTHORS   McAlpine,P.J., Mohandas,T., Ray,M., Wang,H. and Hamerton,J.L.
  TITLE     Assignment of the inorganic pyrophosphatase gene locus (PP) to
            chromosome 10 in man
  JOURNAL   Cytogenet Cell Genet 16 (1-5), 201-203 (1976)
   PUBMED   975879
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Fisher,R.A., Turner,B.M., Dorkin,H.L. and Harris,H.
  TITLE     Studies on human erythrocyte inorganic pyrophosphatase
  JOURNAL   Ann Hum Genet 37 (3), 341-353 (1974)
   PUBMED   4130389
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Pynes,G.D. and Younathan,E.S.
  TITLE     Purification and some properties of inorganic pyrophosphatase from
            human erythrocytes
  JOURNAL   J Biol Chem 242 (9), 2119-2123 (1967)
   PUBMED   6022858
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL731540.4 and AB026723.1.
            
            Summary: The protein encoded by this gene is a member of the
            inorganic pyrophosphatase (PPase) family. PPases catalyze the
            hydrolysis of pyrophosphate to inorganic phosphate, which is
            important for the phosphate metabolism of cells. Studies of a
            similar protein in bovine suggested a cytoplasmic localization of
            this enzyme. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.440882.1,
                                           SRR3476690.930360.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373232.8/ ENSP00000362329.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..289
                     /product="inorganic pyrophosphatase"
                     /EC_number="3.6.1.1"
                     /note="pyrophosphate phospho-hydrolase; pyrophosphatase
                     (inorganic) 1; cytosolic inorganic pyrophosphatase;
                     diphosphate phosphohydrolase; PPase; pyrophosphatase 1;
                     epididymis secretory sperm binding protein Li 66p;
                     inorganic diphosphatase 1"
                     /calculated_mol_wt=32529
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q15181.2)"
     Region          4..241
                     /region_name="pyrophosphatase"
                     /note="Inorganic pyrophosphatase. These enzymes hydrolyze
                     inorganic pyrophosphate (PPi) to two molecules of
                     orthophosphates (Pi). The reaction requires bivalent
                     cations. The enzymes in general exist as homooligomers;
                     cl00217"
                     /db_xref="CDD:469666"
     Site            order(52..53,128..129)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238239"
     Site            order(57,79,94,193..194)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238239"
     Site            57
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15181.2)"
     Site            order(59,116,121,148,153)
                     /site_type="metal-binding"
                     /note="metal binding sites [ion binding]"
                     /db_xref="CDD:238239"
     Site            228
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15181.2)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15181.2)"
     CDS             1..289
                     /gene="PPA1"
                     /gene_synonym="HEL-S-66p; IOPPP; PP; PP1; SID6-8061"
                     /coded_by="NM_021129.4:103..972"
                     /db_xref="CCDS:CCDS7299.1"
                     /db_xref="GeneID:5464"
                     /db_xref="HGNC:HGNC:9226"
                     /db_xref="MIM:179030"
ORIGIN      
        1 msgfsteera apfsleyrvf lknekgqyis pfhdipiyad kdvfhmvvev prwsnakmei
       61 atkdplnpik qdvkkgklry vanlfpykgy iwnygaipqt wedpghndkh tgccgdndpi
      121 dvceigskvc argeiigvkv lgilamideg etdwkviain vddpdaanyn dindvkrlkp
      181 gyleatvdwf rrykvpdgkp enefafnaef kdkdfaidii ksthdhwkal vtkktngkgi
      241 scmnttlses pfkcdpdaar aivdalpppc esactvptdv dkwfhhqkn
//
LOCUS       NP_001129529             557 aa            linear   ROD 27-APR-2025
DEFINITION  copine-6 isoform a [Mus musculus].
ACCESSION   NP_001129529
VERSION     NP_001129529.1
DBSOURCE    REFSEQ: accession NM_001136057.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Liu,P., Khvotchev,M., Li,Y.C., Chanaday,N.L. and Kavalali,E.T.
  TITLE     Copine-6 Binds to SNAREs and Selectively Suppresses Spontaneous
            Neurotransmission
  JOURNAL   J Neurosci 38 (26), 5888-5899 (2018)
   PUBMED   29802203
  REMARK    GeneRIF: we identify copine-6 as a specific regulator of
            spontaneous neurotransmission
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Larimore,J., Zlatic,S.A., Arnold,M., Singleton,K.S., Cross,R.,
            Rudolph,H., Bruegge,M.V., Sweetman,A., Garza,C., Whisnant,E. and
            Faundez,V.
  TITLE     Dysbindin Deficiency Modifies the Expression of GABA Neuron and Ion
            Permeation Transcripts in the Developing Hippocampus
  JOURNAL   Front Genet 8, 28 (2017)
   PUBMED   28344592
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Reinhard,J.R., Kriz,A., Galic,M., Angliker,N., Rajalu,M., Vogt,K.E.
            and Ruegg,M.A.
  TITLE     The calcium sensor Copine-6 regulates spine structural plasticity
            and learning and memory
  JOURNAL   Nat Commun 7, 11613 (2016)
   PUBMED   27194588
  REMARK    GeneRIF: links activity-triggered calcium signals to spine
            structural plasticity necessary for learning and memory
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Perestenko,P., Watanabe,M., Beusnard-Bee,T., Guna,P. and
            McIlhinney,J.
  TITLE     The second C2-domain of copine-2, copine-6 and copine-7 is
            responsible for their calcium-dependent membrane association
  JOURNAL   FEBS J 282 (19), 3722-3736 (2015)
   PUBMED   26175110
  REMARK    GeneRIF: The second C2-domain of copine-6 is responsible for
            calcium-dependent membrane association.
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Perestenko,P.V., Pooler,A.M., Noorbakhshnia,M., Gray,A., Bauccio,C.
            and Jeffrey McIlhinney,R.A.
  TITLE     Copines-1, -2, -3, -6 and -7 show different calcium-dependent
            intracellular membrane translocation and targeting
  JOURNAL   FEBS J 277 (24), 5174-5189 (2010)
   PUBMED   21087455
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Nakayama,T., Yaoi,T., Kuwajima,G., Yoshie,O. and Sakata,T.
  TITLE     Ca2(+)-dependent interaction of N-copine, a member of the two C2
            domain protein family, with OS-9, the product of a gene frequently
            amplified in osteosarcoma
  JOURNAL   FEBS Lett 453 (1-2), 77-80 (1999)
   PUBMED   10403379
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Nakayama,T., Yaoi,T. and Kuwajima,G.
  TITLE     Localization and subcellular distribution of N-copine in mouse
            brain
  JOURNAL   J Neurochem 72 (1), 373-379 (1999)
   PUBMED   9886090
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Nakayama,T., Yaoi,T., Yasui,M. and Kuwajima,G.
  TITLE     N-copine: a novel two C2-domain-containing protein with neuronal
            activity-regulated expression
  JOURNAL   FEBS Lett 428 (1-2), 80-84 (1998)
   PUBMED   9645480
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Creutz,C.E., Tomsig,J.L., Snyder,S.L., Gautier,M.C., Skouri,F.,
            Beisson,J. and Cohen,J.
  TITLE     The copines, a novel class of C2 domain-containing,
            calcium-dependent, phospholipid-binding proteins conserved from
            Paramecium to humans
  JOURNAL   J Biol Chem 273 (3), 1393-1402 (1998)
   PUBMED   9430674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CJ143652.1, BY081897.1,
            BC050766.1 and CJ286371.1.
            
            Summary: Calcium-dependent membrane-binding proteins may regulate
            molecular events at the interface of the cell membrane and
            cytoplasm. This gene is one of several genes that encodes a
            calcium-dependent protein containing two N-terminal type II C2
            domains and an integrin A domain-like sequence in the C-terminus.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jan 2018].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1, 2 and 4
            encode the same isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.167253.1, AK144410.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 28.19 cM"
     Protein         1..557
                     /product="copine-6 isoform a"
                     /note="copine-6; N-copine; neuronal-copine"
                     /calculated_mol_wt=61650
     Region          20..137
                     /region_name="C2A_Copine"
                     /note="C2 domain first repeat in Copine; cd04048"
                     /db_xref="CDD:176013"
     Site            order(35,41,93,95,105)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176013"
     Region          152..266
                     /region_name="C2B_Copine"
                     /note="C2 domain second repeat in Copine; cd04047"
                     /db_xref="CDD:176012"
     Site            order(167,173,229,231,237)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176012"
     Region          244..303
                     /region_name="Linker region.
                     /evidence=ECO:0000269|PubMed:21087455,
                     ECO:0000269|PubMed:26175110"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z140.1)"
     Region          325..538
                     /region_name="Copine"
                     /note="pfam07002"
                     /db_xref="CDD:462064"
     CDS             1..557
                     /gene="Cpne6"
                     /coded_by="NM_001136057.3:293..1966"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS27112.1"
                     /db_xref="GeneID:12891"
                     /db_xref="MGI:MGI:1334445"
ORIGIN      
        1 msdpemgwvp eppamtlgas rvelrvschg lldrdtltkp hpcvllklys deqwvevert
       61 evlrscsspv fsrvlaieyf feekqplqfh vfdaedgats pssdtflgst ectlgqivsq
      121 tkvtkplllk ngktagksti tivaeevsgt ndyvqltfra hkldnkdlfs ksdpfmeiyk
      181 tngdqsdqlv wrtevvknnl npswepfrls lhslcscdih rplkflvydy dssgkhdfig
      241 eftstfqemq egtanpgqem qwdcinpkyr dkkknykssg tvvlaqctve kvhtfldyim
      301 ggcqisftva idftasngdp rssqslhcls prqpnhylqa lrtvggicqd ydsdkrfpaf
      361 gfgarippnf evshdfainf dpenpeceei sgviasyrrc lpqiqlygpt nvapiinrva
      421 epaqreqstg qatkysvllv ltdgvvsdma etrtaivras rlpmsiiivg vgnadfsdmr
      481 lldgddgplr cpkgvpaard ivqfvpfrdf kdaapsalak cvlaevprqv veyyasqgis
      541 pgaprpstpa mtpspsp
//
LOCUS       NP_076983                516 aa            linear   PRI 27-APR-2025
DEFINITION  nucleolar complex protein 4 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_076983 XP_947810 XP_951427
VERSION     NP_076983.1
DBSOURCE    REFSEQ: accession NM_024078.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Talebi,A., Shahidsales,S., Aliakbarian,M., Pezeshki Rad,M. and
            Kerachian,M.A.
  TITLE     Oncogenic fusion transcript analysis identified ADAP1-NOC4L,
            potentially associated with metastatic colorectal cancer
  JOURNAL   Cancer Med 12 (1), 525-540 (2023)
   PUBMED   35702822
  REMARK    GeneRIF: Oncogenic fusion transcript analysis identified
            ADAP1-NOC4L, potentially associated with metastatic colorectal
            cancer.
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Qin,Y., Li,H., Jia,L., Yan,J., Gao,G.F. and Li,X.
  TITLE     Targeted disruption of Noc4l leads to preimplantation embryonic
            lethality in mice
  JOURNAL   Protein Cell 8 (3), 230-235 (2017)
   PUBMED   28012024
  REMARK    GeneRIF: The results provide the first in vivo genetic evidence
            that Noc4l plays important roles in early embryogenesis in mice.
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 516)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 516)
  AUTHORS   Bernstein,K.A., Gallagher,J.E., Mitchell,B.M., Granneman,S. and
            Baserga,S.J.
  TITLE     The small-subunit processome is a ribosome assembly intermediate
  JOURNAL   Eukaryot Cell 3 (6), 1619-1626 (2004)
   PUBMED   15590835
REFERENCE   7  (residues 1 to 516)
  AUTHORS   Milkereit,P., Strauss,D., Bassler,J., Gadal,O., Kuhn,H., Schutz,S.,
            Gas,N., Lechner,J., Hurt,E. and Tschochner,H.
  TITLE     A Noc complex specifically involved in the formation and nuclear
            export of ribosomal 40 S subunits
  JOURNAL   J Biol Chem 278 (6), 4072-4081 (2003)
   PUBMED   12446671
REFERENCE   8  (residues 1 to 516)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY051629.1 and BC071958.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_951427.1, XP_947810.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.247707.1,
                                           SRR3476690.778572.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330579.6/ ENSP00000328854.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..516
                     /product="nucleolar complex protein 4 homolog isoform 1"
                     /note="nucleolar complex protein 4 homolog; NOC4-like
                     protein; NOC4 protein homolog; nucleolar
                     complex-associated protein 4-like protein"
                     /calculated_mol_wt=58337
     Site            297..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVI4.1)"
     Region          310..452
                     /region_name="CBF"
                     /note="CBF/Mak21 family; pfam03914"
                     /db_xref="CDD:461090"
     Site            347..367
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVI4.1)"
     Site            375..395
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVI4.1)"
     CDS             1..516
                     /gene="NOC4L"
                     /gene_synonym="NET49; NOC4; UTP19"
                     /coded_by="NM_024078.3:33..1583"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9277.1"
                     /db_xref="GeneID:79050"
                     /db_xref="HGNC:HGNC:28461"
                     /db_xref="MIM:612819"
ORIGIN      
        1 merepgaagv rralgrrlea vlasrseana vfdilavlqs edqeeiqeav rtcsrlfgal
       61 lergelfvgq lpseemvmtg sqgatrkykv wmrhryhscc nrlgellghp sfqvkelals
      121 allkfvqleg ahplekskwe gnylfprelf klvvggllsp eedqslllsq freyldyddt
      181 ryhtmqaavd avarvtgqhp evppafwnna ftllsavslp rreptvssfy vkraelwdtw
      241 kvahlkehrr vfqamwlsfl khklplslyk kvllivhdai lpqlaqptlm idfltracdl
      301 ggalsllaln glfilihkhn leypdfyrkl yglldpsvfh vkyrarffhl adlflssshl
      361 paylvaafak rlarlaltap peallmvlpf icnllrrhpa crvlvhrphg peldadpydp
      421 geedpaqsra lesslwelqa lqrhyhpevs kaasvinqal smpevsiapl leltayeife
      481 rdlkkkgpep vplefipaqg llgrpgelca qhftls
//
LOCUS       NP_006065                498 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM22 isoform 1 [Homo sapiens].
ACCESSION   NP_006065
VERSION     NP_006065.2
DBSOURCE    REFSEQ: accession NM_006074.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Yang,Y., Hao,X., Zhang,J., Gao,T., Huo,M., Liu,W., Hu,T., Ma,T.,
            Yuan,B., Zhang,M., Teng,X., Yu,H., Huang,W. and Wang,Y.
  TITLE     The E3 ligase TRIM22 functions as a tumor suppressor in breast
            cancer by targeting CCS for proteasomal degradation to inhibit
            STAT3 signaling
  JOURNAL   Cancer Lett 600, 217157 (2024)
   PUBMED   39127340
  REMARK    GeneRIF: The E3 ligase TRIM22 functions as a tumor suppressor in
            breast cancer by targeting CCS for proteasomal degradation to
            inhibit STAT3 signaling.
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Fan,L., Zhou,Y., Wei,X., Feng,W., Guo,H., Li,Y., Gao,X., Zhou,J.,
            Wen,Y., Wu,Y., Shen,X., Liu,L., Xu,G. and Zhang,Z.
  TITLE     The E3 ligase TRIM22 restricts SARS-CoV-2 replication by promoting
            proteasomal degradation of NSP8
  JOURNAL   mBio 15 (2), e0232023 (2024)
   PUBMED   38275298
  REMARK    GeneRIF: The E3 ligase TRIM22 restricts SARS-CoV-2 replication by
            promoting proteasomal degradation of NSP8.
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Kang,D., Hwang,H.J., Baek,Y., Sung,J.Y., Kim,K., Park,H.J.,
            Ko,Y.G., Kim,Y.N. and Lee,J.S.
  TITLE     TRIM22 induces cellular senescence by targeting PHLPP2 in
            hepatocellular carcinoma
  JOURNAL   Cell Death Dis 15 (1), 26 (2024)
   PUBMED   38199981
  REMARK    GeneRIF: TRIM22 induces cellular senescence by targeting PHLPP2 in
            hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Fei,X., Dou,Y.N., Sun,K., Wei,J., Guo,Q., Wang,L., Wu,X., Lv,W.,
            Jiang,X. and Fei,Z.
  TITLE     TRIM22 promotes the proliferation of glioblastoma cells by
            activating MAPK signaling and accelerating the degradation of Raf-1
  JOURNAL   Exp Mol Med 55 (6), 1203-1217 (2023)
   PUBMED   37258577
  REMARK    GeneRIF: TRIM22 promotes the proliferation of glioblastoma cells by
            activating MAPK signaling and accelerating the degradation of
            Raf-1.
REFERENCE   5  (residues 1 to 498)
  AUTHORS   Ren,Y., Dong,H., Jin,R., Jiang,J. and Zhang,X.
  TITLE     TRIM22 actives PI3K/Akt/mTOR pathway to promote psoriasis through
            enhancing cell proliferation and inflammation and inhibiting
            autophagy
  JOURNAL   Cutan Ocul Toxicol 41 (4), 304-309 (2022)
   PUBMED   36170453
  REMARK    GeneRIF: TRIM22 actives PI3K/Akt/mTOR pathway to promote psoriasis
            through enhancing cell proliferation and inflammation and
            inhibiting autophagy.
REFERENCE   6  (residues 1 to 498)
  AUTHORS   Izmailova,E., Bertley,F.M., Huang,Q., Makori,N., Miller,C.J.,
            Young,R.A. and Aldovini,A.
  TITLE     HIV-1 Tat reprograms immature dendritic cells to express
            chemoattractants for activated T cells and macrophages
  JOURNAL   Nat Med 9 (2), 191-197 (2003)
   PUBMED   12539042
REFERENCE   7  (residues 1 to 498)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   8  (residues 1 to 498)
  AUTHORS   Gongora,C., Tissot,C., Cerdan,C. and Mechti,N.
  TITLE     The interferon-inducible Staf50 gene is downregulated during T cell
            costimulation by CD2 and CD28
  JOURNAL   J Interferon Cytokine Res 20 (11), 955-961 (2000)
   PUBMED   11096452
REFERENCE   9  (residues 1 to 498)
  AUTHORS   Tissot,C., Taviaux,S.A., Diriong,S. and Mechti,N.
  TITLE     Localization of Staf50, a member of the Ring finger family, to
            11p15 by fluorescence in situ hybridization
  JOURNAL   Genomics 34 (1), 151-153 (1996)
   PUBMED   8661041
REFERENCE   10 (residues 1 to 498)
  AUTHORS   Tissot,C. and Mechti,N.
  TITLE     Molecular cloning of a new interferon-induced factor that represses
            human immunodeficiency virus type 1 long terminal repeat expression
  JOURNAL   J Biol Chem 270 (25), 14891-14898 (1995)
   PUBMED   7797467
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC364428.1, BC035582.1,
            BC022281.1 and AL360190.1.
            
            On Nov 13, 2006 this sequence version replaced NP_006065.1.
            
            Summary: The protein encoded by this gene is a member of the
            tripartite motif (TRIM) family. The TRIM motif includes three
            zinc-binding domains, a RING, a B-box type 1 and a B-box type 2,
            and a coiled-coil region. This protein localizes to the cytoplasm
            and its expression is induced by interferon. The protein is
            involved in innate immunity against different DNA and RNA viruses.
            [provided by RefSeq, Oct 2021].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.197150.1,
                                           SRR1163657.47350.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379965.8/ ENSP00000369299.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..498
                     /product="E3 ubiquitin-protein ligase TRIM22 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="stimulated trans-acting factor (50 kDa); tripartite
                     motif protein TRIM22; E3 ubiquitin-protein ligase TRIM22;
                     tripartite binding motif 22; staf-50; RING-type E3
                     ubiquitin transferase TRIM22; RING finger protein 94; 50
                     kDa-stimulated trans-acting factor; tripartite
                     motif-containing protein 22"
                     /calculated_mol_wt=56816
     Region          7..79
                     /region_name="RING-HC_TRIM5-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and
                     similar proteins; cd16591"
                     /db_xref="CDD:438253"
     Site            order(16..17,19..20,57..58,60)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438253"
     Region          95..134
                     /region_name="Bbox2_TRIM5-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34,
                     TRIM38 and similar proteins; cd19761"
                     /db_xref="CDD:380819"
     Region          135..>262
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          257..275
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYM9.1)"
     Region          299..496
                     /region_name="SPRY_PRY_TRIM22"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 22 (TRIM22), also known as RING finger protein 94
                     (RNF94) or Stimulated trans-acting factor of 50 kDa
                     (STAF50); cd15824"
                     /db_xref="CDD:293996"
     CDS             1..498
                     /gene="TRIM22"
                     /gene_synonym="GPSTAF50; RNF94; STAF50"
                     /coded_by="NM_006074.5:177..1673"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41612.1"
                     /db_xref="GeneID:10346"
                     /db_xref="HGNC:HGNC:16379"
                     /db_xref="MIM:606559"
ORIGIN      
        1 mdfsvkvdie kevtcpicle llteplsldc ghsfcqacit akikesviis rgesscpvcq
       61 trfqpgnlrp nrhlaniver vkevkmspqe gqkrdvcehh gkklqifcke dgkvicwvce
      121 lsqehqghqt frinevvkec qeklqvalqr likedqeaek leddirqert awknyiqier
      181 qkilkgfnem rvildneeqr elqkleegev nvldnlaaat dqlvqqrqda stlisdlqrr
      241 lrgssvemlq dvidvmkrse swtlkkpksv skklksvfrv pdlsgmlqvl keltdvqyyw
      301 vdvmlnpgsa tsnvaisvdq rqvktvrtct fknsnpcdfs afgvfgcqyf ssgkyywevd
      361 vsgkiawilg vhskisslnk rkssgfafdp svnyskvysr yrpqygywvi glqntceyna
      421 fedssssdpk vltlfmavpp crigvfldye agivsffnvt nhgaliykfs gcrfsrpayp
      481 yfnpwnclvp mtvcppss
//
LOCUS       NP_001597               2436 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-binding cassette sub-family A member 2 isoform a [Homo
            sapiens].
ACCESSION   NP_001597
VERSION     NP_001597.2
DBSOURCE    REFSEQ: accession NM_001606.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2436)
  AUTHORS   Inoue,Y., Tsuchida,N., Kim,C.A., de Oliveira Stephan,B.,
            Castro,M.A.A., Honjo,R.S., Bertola,D.R., Uchiyama,Y., Hamanaka,K.,
            Fujita,A., Koshimizu,E., Misawa,K., Miyatake,S., Mizuguchi,T. and
            Matsumoto,N.
  TITLE     Novel compound heterozygous ABCA2 variants cause IDPOGSA, a
            variable phenotypic syndrome with intellectual disability
  JOURNAL   J Hum Genet 69 (3-4), 163-167 (2024)
   PUBMED   38228874
  REMARK    GeneRIF: Novel compound heterozygous ABCA2 variants cause IDPOGSA,
            a variable phenotypic syndrome with intellectual disability.
REFERENCE   2  (residues 1 to 2436)
  AUTHORS   Shibata,Y., Matsumoto,N., Murase,R., Kubota,Y., Ishida,H.,
            Shimada,K. and Fujita,K.I.
  TITLE     A polymorphism in ABCA2 is associated with neutropenia induced by
            capecitabine in Japanese patients with colorectal cancer
  JOURNAL   Cancer Chemother Pharmacol 92 (6), 465-474 (2023)
   PUBMED   37653272
  REMARK    GeneRIF: A polymorphism in ABCA2 is associated with neutropenia
            induced by capecitabine in Japanese patients with colorectal
            cancer.
REFERENCE   3  (residues 1 to 2436)
  AUTHORS   Kim,M.S., Yang,S.H. and Kim,M.S.
  TITLE     Role of ABCA2 and its single nucleotide polymorphisms (4873T>A and
            4879G>C) in the regulation of multi-drug resistance in oral
            squamous carcinoma cells
  JOURNAL   Biochem Biophys Res Commun 666, 1-9 (2023)
   PUBMED   37167718
  REMARK    GeneRIF: Role of ABCA2 and its single nucleotide polymorphisms
            (4873T>A and 4879G>C) in the regulation of multi-drug resistance in
            oral squamous carcinoma cells.
REFERENCE   4  (residues 1 to 2436)
  AUTHORS   Nedoszytko,B., Sobalska-Kwapis,M., Strapagiel,D., Lange,M.,
            Gorska,A., Elberink,J.N.G.O., van Doormaal,J., Slomka,M.,
            Kalinowski,L., Gruchala-Niedoszytko,M., Nowicki,R.J., Valent,P. and
            Niedoszytko,M.
  TITLE     Results from a Genome-Wide Association Study (GWAS) in Mastocytosis
            Reveal New Gene Polymorphisms Associated with WHO Subgroups
  JOURNAL   Int J Mol Sci 21 (15), 5506 (2020)
   PUBMED   32752121
  REMARK    GeneRIF: Results from a Genome-Wide Association Study (GWAS) in
            Mastocytosis Reveal New Gene Polymorphisms Associated with WHO
            Subgroups.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2436)
  AUTHORS   Sweeney,M.D., Zhao,Z., Montagne,A., Nelson,A.R. and Zlokovic,B.V.
  TITLE     Blood-Brain Barrier: From Physiology to Disease and Back
  JOURNAL   Physiol Rev 99 (1), 21-78 (2019)
   PUBMED   30280653
  REMARK    Review article
REFERENCE   6  (residues 1 to 2436)
  AUTHORS   Kaminski,W.E., Piehler,A., Pullmann,K., Porsch-Ozcurumez,M.,
            Duong,C., Bared,G.M., Buchler,C. and Schmitz,G.
  TITLE     Complete coding sequence, promoter region, and genomic structure of
            the human ABCA2 gene and evidence for sterol-dependent regulation
            in macrophages
  JOURNAL   Biochem Biophys Res Commun 281 (1), 249-258 (2001)
   PUBMED   11178988
REFERENCE   7  (residues 1 to 2436)
  AUTHORS   Zhao,L.X., Zhou,C.J., Tanaka,A., Nakata,M., Hirabayashi,T.,
            Amachi,T., Shioda,S., Ueda,K. and Inagaki,N.
  TITLE     Cloning, characterization and tissue distribution of the rat
            ATP-binding cassette (ABC) transporter ABC2/ABCA2
  JOURNAL   Biochem J 350 Pt 3 (Pt 3), 865-872 (2000)
   PUBMED   10970803
REFERENCE   8  (residues 1 to 2436)
  AUTHORS   Klucken,J., Buchler,C., Orso,E., Kaminski,W.E.,
            Porsch-Ozcurumez,M., Liebisch,G., Kapinsky,M., Diederich,W.,
            Drobnik,W., Dean,M., Allikmets,R. and Schmitz,G.
  TITLE     ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a
            regulator of macrophage cholesterol and phospholipid transport
  JOURNAL   Proc Natl Acad Sci U S A 97 (2), 817-822 (2000)
   PUBMED   10639163
REFERENCE   9  (residues 1 to 2436)
  AUTHORS   Allikmets,R., Gerrard,B., Glavac,D., Ravnik-Glavac,M.,
            Jenkins,N.A., Gilbert,D.J., Copeland,N.G., Modi,W. and Dean,M.
  TITLE     Characterization and mapping of three new mammalian ATP-binding
            transporter genes from an EST database
  JOURNAL   Mamm Genome 6 (2), 114-117 (1995)
   PUBMED   7766993
REFERENCE   10 (residues 1 to 2436)
  AUTHORS   Luciani,M.F., Denizot,F., Savary,S., Mattei,M.G. and Chimini,G.
  TITLE     Cloning of two novel ABC transporters mapping on human chromosome 9
  JOURNAL   Genomics 21 (1), 150-159 (1994)
   PUBMED   8088782
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL807752.10, CD676110.1,
            BM921499.1, BC029282.1, BF516223.1, AF178941.1, DB168116.1,
            BE273611.1, AL525193.3 and BM474929.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 15, 2004 this sequence version replaced NP_001597.1.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intracellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White). This protein is a member of the ABC1 subfamily. Members of
            the ABC1 subfamily comprise the only major ABC subfamily found
            exclusively in multicellular eukaryotes. This protein is highly
            expressed in brain tissue and may play a role in macrophage lipid
            metabolism and neural development. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the predominant isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341511.11/ ENSP00000344155.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2436
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..2436
                     /product="ATP-binding cassette sub-family A member 2
                     isoform a"
                     /note="ATP-binding cassette, sub-family A, member 2;
                     ATP-binding cassette 2; ATP-binding cassette transporter
                     2; ATP-binding cassette, sub-family A (ABC1), member 2"
                     /calculated_mol_wt=269818
     Region          1..2368
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            14
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            55..75
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            90
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            169
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            272
                     /site_type="methylation"
                     /note="N5-methylglutamine.
                     /evidence=ECO:0000269|PubMed:26797129; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            306
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            369
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            421
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            477
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            485
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            495
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            531
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            545
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            591
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            601
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            629
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            700..720
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            751..771
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            783..803
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            814..834
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            858..878
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            894..914
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Region          1224..1244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Region          1326..1358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1409
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1457..1477
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1550
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1558
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Region          1587..1611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1613
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1678
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1776
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1793..1813
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1842..1862
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1873..1893
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1906..1926
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            1992..2012
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            2055
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     Site            2413
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BZC7.4)"
     CDS             1..2436
                     /gene="ABCA2"
                     /gene_synonym="ABC2; IDPOGSA"
                     /coded_by="NM_001606.5:98..7408"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43909.1"
                     /db_xref="GeneID:20"
                     /db_xref="HGNC:HGNC:32"
                     /db_xref="MIM:600047"
ORIGIN      
        1 mgflhqlqll lwknvtlkrr spwvlafeif iplvlffill glrqkkptis vkevsfytaa
       61 pltsagilpv mqslcpdgqr defgflqyan stvtqllerl drvveegnlf dparpslgse
      121 lealrqhlea lsagpgtsgs hldrstvssf sldsvarnpq elwrfltqnl slpnstaqal
      181 laarvdppev yhllfgpssa ldsqsglhkg qepwsrlggn plfrmeelll apalleqltc
      241 tpgsgelgri ltvpesqkga lqgyrdavcs gqaaararrf sglsaelrnq ldvakvsqql
      301 gldapngsds spqappprrl qallgdllda qkvlqdvdvl salalllpqg actgrtpgpp
      361 asgaggaang tgagavmgpn ataeegapsa aalatpdtlq gqcsafvqlw aglqpilcgn
      421 nrtiepealr rgnmsslgft skeqrnlgll vhlmtsnpki lyapagsevd rvilkanetf
      481 afvgnvthya qvwlnisaei rsfleqgrlq qhlrwlqqyv aelrlhpeal nlsldelppa
      541 lrqdnfslps gmallqqldt idnaacgwiq fmskvsvdif kgfpdeesiv nytlnqayqd
      601 nvtvfasvif qtrkdgslpp hvhykirqns sftektneir raywrpgpnt ggrfyflygf
      661 vwiqdmmera iidtfvghdv vepgsyvqmf pypcytrddf lfviehmmpl cmviswvysv
      721 amtiqhivae kehrlkevmk tmglnnavhw vawfitgfvq lsisvtalta ilkygqvlmh
      781 shvviiwlfl avyavatimf cflvsvlysk aklasacggi iyflsyvpym yvaireevah
      841 dkitafekci aslmsttafg lgskyfalye vagvgiqwht fsqspvegdd fnlllavtml
      901 mvdavvygil twyieavhpg myglprpwyf plqksywlgs grteawewsw pwartprlsv
      961 meedqacame srrfeetrgm eeepthlplv vcvdkltkvy kddkklalnk lslnlyenqv
     1021 vsflghngag ktttmsiltg lfpptsgsat iyghdirtem deirknlgmc pqhnvlfdrl
     1081 tveehlwfys rlksmaqeei rremdkmied lelsnkrhsl vqtlsggmkr klsvaiafvg
     1141 gsraiildep tagvdpyarr aiwdlilkyk pgrtillsth hmdeadllgd riaiishgkl
     1201 kccgsplflk gtygdgyrlt lvkrpaepgg pqepglassp pgraplsscs elqvsqfirk
     1261 hvascllvsd tstelsyilp seaakkgafe rlfqhlersl dalhlssfgl mdttleevfl
     1321 kvseedqsle nseadvkesr kdvlpgaegp asgeghagnl arcseltqsq aslqsassvg
     1381 sargdegagy tdvygdyrpl fdnpqdpdnv slqeveaeal srvgqgsrkl dggwlkvrqf
     1441 hgllvkrfhc arrnskalfs qillpaffvc vamtvalsvp eigdlpplvl spsqyhnytq
     1501 prgnfipyan eerreyrlrl spdaspqqlv stfrlpsgvg atcvlkspan gslgptlnls
     1561 sgesrllaar ffdsmclesf tqglplsnfv ppppspapsd spaspdedlq awnvslppta
     1621 gpemwtsaps lprlvrepvr ctcsaqgtgf scpssvgghp pqmrvvtgdi ltditghnvs
     1681 eyllftsdrf rlhrygaitf gnvlksipas fgtrappmvr kiavrraaqv fynnkgyhsm
     1741 ptylnslnna ilranlpksk gnpaaygitv tnhpmnktsa slsldyllqg tdvviaifii
     1801 vamsfvpasf vvflvaekst kakhlqfvsg cnpiiywlan yvwdmlnylv patccviilf
     1861 vfdlpaytsp tnfpavlslf llygwsitpi mypasfwfev pssayvfliv inlfigitat
     1921 vatfllqlfe hdkdlkvvns ylkscflifp nynlghglme mayneyiney yakigqfdkm
     1981 kspfewdivt rglvamaveg vvgflltimc qynflrrpqr mpvstkpved dvdvaserqr
     2041 vlrgdadndm vkienltkvy ksrkigrila vdrlclgvrp gecfgllgvn gagktstfkm
     2101 ltgdesttgg eafvnghsvl kellqvqqsl gycpqcdalf deltarehlq lytrlrgisw
     2161 kdearvvkwa lekleltkya dkpagtysgg nkrklstaia ligypafifl depttgmdpk
     2221 arrflwnlil dliktgrsvv ltshsmeece alctrlaimv ngrlrclgsi qhlknrfgdg
     2281 ymitvrtkss qsvkdvvrff nrnfpeamlk erhhtkvqyq lksehislaq vfskmeqvsg
     2341 vlgiedysvs qttldnvfvn fakkqsdnle qqeteppsal qsplgcllsl lrprsaptel
     2401 ralvadeped ldtedeglis feeeraqlsf ntdtlc
//
LOCUS       NP_848588                496 aa            linear   PRI 27-APR-2025
DEFINITION  palmitoleoyl-protein carboxylesterase NOTUM precursor [Homo
            sapiens].
ACCESSION   NP_848588
VERSION     NP_848588.3
DBSOURCE    REFSEQ: accession NM_178493.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Zhao,Q., Ren,H., Wang,N., Yuan,X., Zhao,Y. and Wen,Q.
  TITLE     NOTUM plays a bidirectionally modulatory role in the odontoblastic
            differentiation of human stem cells from the apical papilla through
            the WNT/beta-catenin signaling pathway
  JOURNAL   Arch Oral Biol 160, 105896 (2024)
   PUBMED   38278124
  REMARK    GeneRIF: NOTUM plays a bidirectionally modulatory role in the
            odontoblastic differentiation of human stem cells from the apical
            papilla through the WNT/beta-catenin signaling pathway.
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Liu,Y., Chen,H., Xiao,L., Dong,P., Ma,Y., Zhou,Y., Yang,J.,
            Bian,B., Xie,G., Chen,L. and Shen,L.
  TITLE     Notum enhances gastric cancer stem-like cell properties through
            upregulation of Sox2 by PI3K/AKT signaling pathway
  JOURNAL   Cell Oncol (Dordr) 47 (2), 463-480 (2024)
   PUBMED   37749430
  REMARK    GeneRIF: Notum enhances gastric cancer stem-like cell properties
            through upregulation of Sox2 by PI3K/AKT signaling pathway.
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Yang,P., Li,C., Zhou,Q., Zhang,X., Kou,Y., Feng,Q., Wang,H., Su,R.,
            Hasegawa,T., Liu,H. and Li,M.
  TITLE     Notum leads to potential pro-survival of OSCC through crosstalk
            between Shh and Wnt/beta-catenin signaling via p-GSK3beta
  JOURNAL   Int J Biochem Cell Biol 153, 106316 (2022)
   PUBMED   36280040
  REMARK    GeneRIF: Notum leads to potential pro-survival of OSCC through
            crosstalk between Shh and Wnt/beta-catenin signaling via
            p-GSK3beta.
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Gong,H., Niu,Q., Zhou,Y., Wang,Y.X., Xu,X.F. and Hou,K.Z.
  TITLE     Notum palmitoleoyl-protein carboxylesterase regulates Fas cell
            surface death receptor-mediated apoptosis via the Wnt signaling
            pathway in colon adenocarcinoma
  JOURNAL   Bioengineered 12 (1), 5241-5252 (2021)
   PUBMED   34402722
  REMARK    GeneRIF: Notum palmitoleoyl-protein carboxylesterase regulates Fas
            cell surface death receptor-mediated apoptosis via the Wnt
            signaling pathway in colon adenocarcinoma.
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Flanagan,D.J., Pentinmikko,N., Luopajarvi,K., Willis,N.J.,
            Gilroy,K., Raven,A.P., Mcgarry,L., Englund,J.I., Webb,A.T.,
            Scharaw,S., Nasreddin,N., Hodder,M.C., Ridgway,R.A., Minnee,E.,
            Sphyris,N., Gilchrist,E., Najumudeen,A.K., Romagnolo,B., Perret,C.,
            Williams,A.C., Clevers,H., Nummela,P., Lahde,M., Alitalo,K.,
            Hietakangas,V., Hedley,A., Clark,W., Nixon,C., Kirschner,K.,
            Jones,E.Y., Ristimaki,A., Leedham,S.J., Fish,P.V., Vincent,J.P.,
            Katajisto,P. and Sansom,O.J.
  TITLE     NOTUM from Apc-mutant cells biases clonal competition to initiate
            cancer
  JOURNAL   Nature 594 (7863), 430-435 (2021)
   PUBMED   34079124
  REMARK    GeneRIF: NOTUM from Apc-mutant cells biases clonal competition to
            initiate cancer.
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Brommage,R., Liu,J., Vogel,P., Mseeh,F., Thompson,A.Y.,
            Potter,D.G., Shadoan,M.K., Hansen,G.M., Jeter-Jones,S., Cui,J.,
            Bright,D., Bardenhagen,J.P., Doree,D.D., Moverare-Skrtic,S.,
            Nilsson,K.H., Henning,P., Lerner,U.H., Ohlsson,C., Sands,A.T.,
            Tarver,J.E., Powell,D.R., Zambrowicz,B. and Liu,Q.
  TITLE     NOTUM inhibition increases endocortical bone formation and bone
            strength
  JOURNAL   Bone Res 7, 2 (2019)
   PUBMED   30622831
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Yoon,J.H., Kim,D., Kim,J., Lee,H., Ghim,J., Kang,B.J., Song,P.,
            Suh,P.G., Ryu,S.H. and Lee,T.G.
  TITLE     NOTUM Is Involved in the Progression of Colorectal Cancer
  JOURNAL   Cancer Genomics Proteomics 15 (6), 485-497 (2018)
   PUBMED   30343282
  REMARK    GeneRIF: NOTUM expression was increased in metastatic cells.
            Proliferation was suppressed by inhibiting expression of NOTUM.
            Knockdown of NOTUM genes inhibited proliferation as well as
            migration, with possible involvement of p38 and c-JUN N-terminal
            kinase in this process.
REFERENCE   8  (residues 1 to 496)
  AUTHORS   De Robertis,M., Arigoni,M., Loiacono,L., Riccardo,F.,
            Calogero,R.A., Feodorova,Y., Tashkova,D., Belovejdov,V.,
            Sarafian,V., Cavallo,F. and Signori,E.
  TITLE     Novel insights into Notum and glypicans regulation in colorectal
            cancer
  JOURNAL   Oncotarget 6 (38), 41237-41257 (2015)
   PUBMED   26517809
  REMARK    GeneRIF: Data show that notum and glypican-1 and glypican-3 gene
            expression during colorectal cancer (CRC) development and present
            evidence to suggest them as potential new biomarkers of CRC
            pathogenesis.
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Kakugawa,S., Langton,P.F., Zebisch,M., Howell,S., Chang,T.H.,
            Liu,Y., Feizi,T., Bineva,G., O'Reilly,N., Snijders,A.P., Jones,E.Y.
            and Vincent,J.P.
  TITLE     Notum deacylates Wnt proteins to suppress signalling activity
  JOURNAL   Nature 519 (7542), 187-192 (2015)
   PUBMED   25731175
  REMARK    GeneRIF: Kinetic and mass spectrometric analyses of human proteins
            show that Notum is a carboxylesterase that removes an essential
            palmitoleate moiety from Wnt proteins and thus constitutes the
            first known extracellular protein deacylase
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Torisu,Y., Watanabe,A., Nonaka,A., Midorikawa,Y., Makuuchi,M.,
            Shimamura,T., Sugimura,H., Niida,A., Akiyama,T., Iwanari,H.,
            Kodama,T., Zeniya,M. and Aburatani,H.
  TITLE     Human homolog of NOTUM, overexpressed in hepatocellular carcinoma,
            is regulated transcriptionally by beta-catenin/TCF
  JOURNAL   Cancer Sci 99 (6), 1139-1146 (2008)
   PUBMED   18429952
  REMARK    GeneRIF: Overexpression of NOTUM is associated with hepatocellular
            carcinoma
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC145207.2, BC060882.1, BX365997.2 and BC036872.1.
            
            On Jul 24, 2008 this sequence version replaced NP_848588.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036872.1, BC060882.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409678.8/ ENSP00000387310.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..496
                     /product="palmitoleoyl-protein carboxylesterase NOTUM
                     precursor"
                     /EC_number="3.1.1.98"
                     /note="protein notum homolog; palmitoleoyl-protein
                     carboxylesterase NOTUM; notum pectinacetylesterase
                     homolog; [Wnt protein] O-palmitoleoyl-L-serine hydrolase"
                     /calculated_mol_wt=53752
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1965
     mat_peptide     20..496
                     /product="Palmitoleoyl-protein carboxylesterase NOTUM.
                     /id=PRO_0000318755"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P988.2)"
                     /calculated_mol_wt=53752
     Region          21..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P988.2)"
     Region          81..417
                     /region_name="PAE"
                     /note="Pectinacetylesterase; pfam03283"
                     /db_xref="CDD:460874"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (Q6P988.2)"
     Site            96
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PDB:4UYU, ECO:0007744|PDB:4UYW,
                     ECO:0007744|PDB:4UYZ, ECO:0007744|PDB:4UZ1,
                     ECO:0007744|PDB:4UZ5, ECO:0007744|PDB:4UZ6,
                     ECO:0007744|PDB:4UZ9, ECO:0007744|PDB:4UZA,
                     ECO:0007744|PDB:4UZL, ECO:0007744|PDB:4UZQ; propagated
                     from UniProtKB/Swiss-Prot (Q6P988.2)"
     CDS             1..496
                     /gene="NOTUM"
                     /gene_synonym="hNOTUM"
                     /coded_by="NM_178493.6:279..1769"
                     /db_xref="CCDS:CCDS32771.2"
                     /db_xref="GeneID:147111"
                     /db_xref="HGNC:HGNC:27106"
                     /db_xref="MIM:609847"
ORIGIN      
        1 mgrgvrvlll lsllhcaggs egrktwrrrg qqppppprte aapaagqpve sfpldftave
       61 gnmdsfmaqv kslaqslypc saqqlnedlr lhlllntsvt cndgspagyy lkesrgsrrw
      121 llfleggwyc fnrencdsry dtmrrlmssr dwprtrtgtg ilssqpeenp ywwnanmvfi
      181 pycssdvwsg assksekney afmgaliiqe vvrellgrgl sgakvlllag ssaggtgvll
      241 nvdrvaeqle klgypaiqvr gladsgwfld nkqyrhtdcv dtitcaptea irrgirywng
      301 vvpercrrqf qegeewncff gykvyptlrc pvfvvqwlfd eaqltvdnvh ltgqpvqegl
      361 rlyiqnlgre lrhtlkdvpa sfapaclshe iiirshwtdv qvkgtslpra lhcwdrslhd
      421 shkasktplk gcpvhlvdsc pwphcnpscp tvrdqftgqe mnvaqflmhm gfdmqtvaqp
      481 qglepsellg mlsngs
//
LOCUS       NP_003566                671 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 282 isoform 1 [Homo sapiens].
ACCESSION   NP_003566 XP_001131412 XP_001132213
VERSION     NP_003566.1
DBSOURCE    REFSEQ: accession NM_003575.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Yeo,S.Y., Ha,S.Y., Yu,E.J., Lee,K.W., Kim,J.H. and Kim,S.H.
  TITLE     ZNF282 (Zinc finger protein 282), a novel E2F1 co-activator,
            promotes esophageal squamous cell carcinoma
  JOURNAL   Oncotarget 5 (23), 12260-12272 (2014)
   PUBMED   25373738
  REMARK    GeneRIF: ZNF282 is E2F1 co-activator involved in esophageal
            squamous cell carcinoma
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Yu,E.J., Kim,S.H., Kim,M.J., Seo,W.Y., Song,K.A., Kang,M.S.,
            Yang,C.K., Stallcup,M.R. and Kim,J.H.
  TITLE     SUMOylation of ZFP282 potentiates its positive effect on estrogen
            signaling in breast tumorigenesis
  JOURNAL   Oncogene 32 (35), 4160-4168 (2013)
   PUBMED   22986521
  REMARK    GeneRIF: SUMOylation of ZFP282 potentiates its positive effect on
            estrogen signaling in breast tumorigenesis.
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Cheng,J., Kapranov,P., Drenkow,J., Dike,S., Brubaker,S., Patel,S.,
            Long,J., Stern,D., Tammana,H., Helt,G., Sementchenko,V.,
            Piccolboni,A., Bekiranov,S., Bailey,D.K., Ganesh,M., Ghosh,S.,
            Bell,I., Gerhard,D.S. and Gingeras,T.R.
  TITLE     Transcriptional maps of 10 human chromosomes at 5-nucleotide
            resolution
  JOURNAL   Science 308 (5725), 1149-1154 (2005)
   PUBMED   15790807
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Okumura,K., Sakaguchi,G., Naito,K., Tamura,T. and Igarashi,H.
  TITLE     HUB1, a novel Kruppel type zinc finger protein, represses the human
            T cell leukemia virus type I long terminal repeat-mediated
            expression
  JOURNAL   Nucleic Acids Res 25 (24), 5025-5032 (1997)
   PUBMED   9396811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D30612.1, BC073805.1 and BC041704.1.
            
            On or before Jan 25, 2007 this sequence version replaced
            XP_001132213.1, XP_001131412.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: D30612.1, BC041704.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000610704.5/ ENSP00000477841.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..671
                     /product="zinc finger protein 282 isoform 1"
                     /note="HTLV-I U5 repressive element-binding protein 1;
                     HUB-1; HTLV-I U5RE-binding protein 1"
                     /calculated_mol_wt=74165
     Region          198..260
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          239..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDV7.3)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDV7.3)"
     Region          373..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDV7.3)"
     Region          <506..651
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          520..540
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          548..568
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(553,555,557,559..560,563..564,567,581,583,587..588,
                     591..592,595,609,611,613,615..616,619..620,623)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          576..596
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          604..624
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          632..652
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          649..671
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDV7.3)"
     CDS             1..671
                     /gene="ZNF282"
                     /gene_synonym="HUB1"
                     /coded_by="NM_003575.4:45..2060"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5895.1"
                     /db_xref="GeneID:8427"
                     /db_xref="HGNC:HGNC:13076"
                     /db_xref="MIM:603397"
ORIGIN      
        1 mqfvstrpqp qqlgiqglgl dsgswswaqa lppeevchqe palrgemaeg mppmqaqewd
       61 mdarrpmpfq fppfpdrapv fpdrmmrepq lptaeislwt vvaaiqaver kvdaqasqll
      121 nlegrtgtae kkladcekta vefgnhmesk wavlgtllqe ygllqrrlen lenllrnrnf
      181 wvlrlppgsk geapkvpvtf vdiavyfsed ewknldewqk elynnlvken yktlmsldae
      241 gsvpkpdapv qaepreepcv weqrhpeere ipmdpeagae plvpaqdass qvkredtlcv
      301 rgqrgleera iptesitdsp isaqdllsri kqeehqcvwd qqdladrdip tdpnseslis
      361 ahdilswikq eeqpypwgpr dsmdgelgld sgpsdsllmv knpppappqp qpqpqppqpq
      421 lqsqpqpqsl ppiavaenpg gppsrglldd gfqvlpgerg sgeappggdr stgggggdgg
      481 gggggaeagt gagggcgscc pgglrrslll hgarskpysc pecgksfgvr ksliihhrsh
      541 tkerpyecae ceksfnchsg lirhqmthrg erpykcsece ktysrkehlq nhqrlhtger
      601 pfqcalcgks firkqnllkh qrihtgerpy tcgecgksfr ykeslkdhlr vhsggpgpga
      661 prqlpppper d
//
LOCUS       NP_476516                866 aa            linear   PRI 27-APR-2025
DEFINITION  N-alpha-acetyltransferase 15, NatA auxiliary subunit isoform 1
            [Homo sapiens].
ACCESSION   NP_476516 NP_079361
VERSION     NP_476516.1
DBSOURCE    REFSEQ: accession NM_057175.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Lyon,G.J., Vedaie,M., Beisheim,T., Park,A., Marchi,E., Gottlieb,L.,
            Hsieh,T.C., Klinkhammer,H., Sandomirsky,K., Cheng,H., Starr,L.J.,
            Preddy,I., Tseng,M., Li,Q., Hu,Y., Wang,K., Carvalho,A.,
            Martinez,F., Caro-Llopis,A., Gavin,M., Amble,K., Krawitz,P.,
            Marmorstein,R. and Herr-Israel,E.
  TITLE     Expanding the phenotypic spectrum of NAA10-related
            neurodevelopmental syndrome and NAA15-related neurodevelopmental
            syndrome
  JOURNAL   Eur J Hum Genet 31 (7), 824-833 (2023)
   PUBMED   37130971
  REMARK    GeneRIF: Expanding the phenotypic spectrum of NAA10-related
            neurodevelopmental syndrome and NAA15-related neurodevelopmental
            syndrome.
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Tian,Y., Xie,H., Yang,S., Shangguan,S., Wang,J., Jin,C., Zhang,Y.,
            Cui,X., Lyu,Y., Chen,X. and Wang,L.
  TITLE     Possible Catch-Up Developmental Trajectories for Children with Mild
            Developmental Delay Caused by NAA15 Pathogenic Variants
  JOURNAL   Genes (Basel) 13 (3), 536 (2022)
   PUBMED   35328089
  REMARK    GeneRIF: Possible Catch-Up Developmental Trajectories for Children
            with Mild Developmental Delay Caused by NAA15 Pathogenic Variants.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Ward,T., Tai,W., Morton,S., Impens,F., Van Damme,P., Van Haver,D.,
            Timmerman,E., Venturini,G., Zhang,K., Jang,M.Y., Willcox,J.A.L.,
            Haghighi,A., Gelb,B.D., Chung,W.K., Goldmuntz,E., Porter,G.A. Jr.,
            Lifton,R.P., Brueckner,M., Yost,H.J., Bruneau,B.G., Gorham,J.,
            Kim,Y., Pereira,A., Homsy,J., Benson,C.C., DePalma,S.R.,
            Varland,S., Chen,C.S., Arnesen,T., Gevaert,K., Seidman,C. and
            Seidman,J.G.
  TITLE     Mechanisms of Congenital Heart Disease Caused by NAA15
            Haploinsufficiency
  JOURNAL   Circ Res 128 (8), 1156-1169 (2021)
   PUBMED   33557580
  REMARK    GeneRIF: Mechanisms of Congenital Heart Disease Caused by NAA15
            Haploinsufficiency.
REFERENCE   5  (residues 1 to 866)
  AUTHORS   Ritter,A., Berger,J.H., Deardorff,M., Izumi,K., Lin,K.Y., Medne,L.
            and Ahrens-Nicklas,R.C.
  TITLE     Variants in NAA15 cause pediatric hypertrophic cardiomyopathy
  JOURNAL   Am J Med Genet A 185 (1), 228-233 (2021)
   PUBMED   33103328
  REMARK    GeneRIF: Variants in NAA15 cause pediatric hypertrophic
            cardiomyopathy.
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Fluge,O., Bruland,O., Akslen,L.A., Varhaug,J.E. and Lillehaug,J.R.
  TITLE     NATH, a novel gene overexpressed in papillary thyroid carcinomas
  JOURNAL   Oncogene 21 (33), 5056-5068 (2002)
   PUBMED   12140756
  REMARK    GeneRIF: NATH, a novel gene overexpressed in papillary thyroid
            carcinomas.
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
REFERENCE   8  (residues 1 to 866)
  AUTHORS   He,Y.G., Xie,Y.F., Chen,Y., Qian,W., Lai,J.H. and Tan,D.Y.
  TITLE     [Cloning and analysis of a novel gene encoding N-terminal
            acetyltransferase subunit]
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 34 (3),
            353-357 (2002)
   PUBMED   12019451
REFERENCE   9  (residues 1 to 866)
  AUTHORS   Gendron,R.L., Good,W.V., Adams,L.C. and Paradis,H.
  TITLE     Suppressed expression of tubedown-1 in retinal neovascularization
            of proliferative diabetic retinopathy
  JOURNAL   Invest Ophthalmol Vis Sci 42 (12), 3000-3007 (2001)
   PUBMED   11687548
REFERENCE   10 (residues 1 to 866)
  AUTHORS   Choi,S.C., Chang,J.Y. and Han,J.K.
  TITLE     A novel Xenopus acetyltransferase with a dynamic expression in
            early development
  JOURNAL   Biochem Biophys Res Commun 285 (5), 1338-1343 (2001)
   PUBMED   11478804
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY039242.1, BX499137.1 and
            AC097376.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 10, 2004 this sequence version replaced NP_079361.1.
            
            Summary: N-alpha-acetylation is among the most common
            post-translational protein modifications in eukaryotic cells. This
            process involves the transfer of an acetyl group from
            acetyl-coenzyme A to the alpha-amino group on a nascent polypeptide
            and is essential for normal cell function. This gene encodes the
            auxillary subunit of the N-terminal acetyltransferase A (NatA)
            complex. [provided by RefSeq, Jan 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.167745.1, AJ314788.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296543.10/ ENSP00000296543.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..866
                     /product="N-alpha-acetyltransferase 15, NatA auxiliary
                     subunit isoform 1"
                     /note="transcriptional coactivator tubedown-100; NMDA
                     receptor regulated 1; NMDA receptor-regulated protein 1;
                     gastric cancer antigen Ga19; protein tubedown-1;
                     N-terminal acetyltransferase"
                     /calculated_mol_wt=101142
     Region          12..38
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          44..283
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          46..79
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          47..74
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          80..113
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          82..108
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(84..85,88..89,91,115,118..119,122..123,125..126,149,
                     152..153,156..157,160)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          113..143
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          148..184
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          148..173
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          187..698
                     /region_name="NatA_aux_su"
                     /note="N-terminal acetyltransferase A, auxiliary subunit;
                     pfam12569"
                     /db_xref="CDD:463630"
     Region          224..257
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            262
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          374..407
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            order(378..379,382..383,385,409,412..413,416..417,
                     419..420,443,446..447,450..451,454)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          378..402
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          407..437
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          409..441
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          442..467
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          485..518
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          500..866
                     /region_name="Interaction with HYPK.
                     /evidence=ECO:0000269|PubMed:20154145"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          579..642
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          612..629
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            735
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            756
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            855
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            856
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     CDS             1..866
                     /gene="NAA15"
                     /gene_synonym="Ga19; MRD50; NARG1; NAT1P; NATH; TBDN;
                     TBDN100"
                     /coded_by="NM_057175.5:274..2874"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43270.1"
                     /db_xref="GeneID:80155"
                     /db_xref="HGNC:HGNC:30782"
                     /db_xref="MIM:608000"
ORIGIN      
        1 mpavslppke nalfkrilrc yehkqyrngl kfckqilsnp kfaehgetla mkgltlnclg
       61 kkeeayelvr rglrndlksh vcwhvygllq rsdkkydeai kcyrnalkwd kdnlqilrdl
      121 sllqiqmrdl egyretryql lqlrpaqras wigyaiayhl ledyemaaki leefrktqqt
      181 spdkvdyeys elllyqnqvl reaglyreal ehlctyekqi cdklaveetk gelllqlcrl
      241 edaadvyrgl qernpenway ykglekalkp anmlerlkiy eeawtkyprg lvprrlplnf
      301 lsgekfkecl dkflrmnfsk gcppvfntlr slykdkekva iieelvvgye tslkscrlfn
      361 pnddgkeepp ttllwvqyyl aqhydkigqp sialeyinta iestptliel flvkakiykh
      421 agnikeaarw mdeaqaldta drfinskcak ymlkanlike aeemcskftr egtsavenln
      481 emqcmwfqte caqaykamnk fgealkkche ierhfieitd dqfdfhtycm rkitlrsyvd
      541 llkledvlrq hpfyfkaari aieiylklhd npltdenkeh eadtanmsdk elkklrnkqr
      601 raqkkaqiee ekknaekekq qrnqkkkkdd ddeeiggpke elipeklakv etpleeaikf
      661 ltplknlvkn kiethlfafe iyfrkekfll mlqsvkrafa idsshpwlhe cmirlfntav
      721 ceskdlsdtv rtvlkqemnr lfgatnpknf netflkrnsd slphrlsaak mvyyldpssq
      781 kraielattl desltnrnlq tcmevlealy dgslgdckea aeiyranchk lfpyalafmp
      841 pgyeedmkit vngdssaeae elanei
//
LOCUS       NP_443204                347 aa            linear   PRI 27-APR-2025
DEFINITION  leucine-rich alpha-2-glycoprotein precursor [Homo sapiens].
ACCESSION   NP_443204
VERSION     NP_443204.1
DBSOURCE    REFSEQ: accession NM_052972.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Randen-Brady,R., Carpen,T., Hautala,L.C., Tolvanen,T., Haglund,C.,
            Joenvaara,S., Mattila,P., Makitie,A., Lehtonen,S., Hagstrom,J. and
            Silen,S.
  TITLE     LRG1 and SDR16C5 protein expressions differ according to HPV status
            in oropharyngeal squamous cell carcinoma
  JOURNAL   Sci Rep 14 (1), 14148 (2024)
   PUBMED   38898137
  REMARK    GeneRIF: LRG1 and SDR16C5 protein expressions differ according to
            HPV status in oropharyngeal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Gobel,A., Rachner,T.D., Hoffmann,O., Klotz,D.M., Kasimir-Bauer,S.,
            Kimmig,R., Hofbauer,L.C. and Bittner,A.K.
  TITLE     High serum levels of leucine-rich alpha-2 glycoprotein 1 (LRG-1)
            are associated with poor survival in patients with early breast
            cancer
  JOURNAL   Arch Gynecol Obstet 309 (6), 2789-2798 (2024)
   PUBMED   38413424
  REMARK    GeneRIF: High serum levels of leucine-rich alpha-2 glycoprotein 1
            (LRG-1) are associated with poor survival in patients with early
            breast cancer.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Chen,J., Zhang,Z., Feng,L., Liu,W., Wang,X., Chen,H. and Zou,H.
  TITLE     Lrg1 silencing attenuates ischemia-reperfusion renal injury by
            regulating autophagy and apoptosis through the TGFbeta1- Smad1/5
            signaling pathway
  JOURNAL   Arch Biochem Biophys 753, 109892 (2024)
   PUBMED   38246328
  REMARK    GeneRIF: Lrg1 silencing attenuates ischemia-reperfusion renal
            injury by regulating autophagy and apoptosis through the TGFbeta1-
            Smad1/5 signaling pathway.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Cheng,X., Wei,H., Liu,Y., Sun,Y., Ye,J., Lu,P. and Han,B.
  TITLE     Relation between LRG1 and CD4+ T cells, cognitive impairment and
            neurological function in patients with acute ischemic stroke
  JOURNAL   Biomark Med 18 (1), 5-14 (2024)
   PUBMED   38380988
  REMARK    GeneRIF: Relation between LRG1 and CD4[+] T cells, cognitive
            impairment and neurological function in patients with acute
            ischemic stroke.
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Wang,D., Pei,W., Liu,Y., Mo,R., Li,X., Gu,W., Su,Y., Ye,J., Xu,J.
            and Zhao,D.
  TITLE     Leucine rich alpha2 glycoprotein 1 derived from malignant pleural
            mesothelioma cells facilitates macrophage M2 phenotypes
  JOURNAL   Exp Lung Res 50 (1), 136-145 (2024)
   PUBMED   39033404
  REMARK    GeneRIF: Leucine rich alpha2 glycoprotein 1 derived from malignant
            pleural mesothelioma cells facilitates macrophage M2 phenotypes.
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Anderson,N.L., Polanski,M., Pieper,R., Gatlin,T., Tirumalai,R.S.,
            Conrads,T.P., Veenstra,T.D., Adkins,J.N., Pounds,J.G., Fagan,R. and
            Lobley,A.
  TITLE     The human plasma proteome: a nonredundant list developed by
            combination of four separate sources
  JOURNAL   Mol Cell Proteomics 3 (4), 311-326 (2004)
   PUBMED   14718574
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Bunkenborg,J., Pilch,B.J., Podtelejnikov,A.V. and Wisniewski,J.R.
  TITLE     Screening for N-glycosylated proteins by liquid chromatography mass
            spectrometry
  JOURNAL   Proteomics 4 (2), 454-465 (2004)
   PUBMED   14760718
REFERENCE   8  (residues 1 to 347)
  AUTHORS   O'Donnell,L.C., Druhan,L.J. and Avalos,B.R.
  TITLE     Molecular characterization and expression analysis of leucine-rich
            alpha2-glycoprotein, a novel marker of granulocytic differentiation
  JOURNAL   J Leukoc Biol 72 (3), 478-485 (2002)
   PUBMED   12223515
  REMARK    GeneRIF: cDNA clones for human leucine-rich alpha2-glycoprotein
            were isolated. LRG expression was up-regulated during neutrophil
            differentiation but down-regulated during monocytic
            differentiation. The hLRG gene was localized to chromosome 19p13.3.
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Saito,K., Tanaka,T., Kanda,H., Ebisuno,Y., Izawa,D., Kawamoto,S.,
            Okubo,K. and Miyasaka,M.
  TITLE     Gene expression profiling of mucosal addressin cell adhesion
            molecule-1+ high endothelial venule cells (HEV) and identification
            of a leucine-rich HEV glycoprotein as a HEV marker
  JOURNAL   J Immunol 168 (3), 1050-1059 (2002)
   PUBMED   11801638
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Takahashi,N., Takahashi,Y. and Putnam,F.W.
  TITLE     Periodicity of leucine and tandem repetition of a 24-amino acid
            segment in the primary structure of leucine-rich alpha
            2-glycoprotein of human serum
  JOURNAL   Proc Natl Acad Sci U S A 82 (7), 1906-1910 (1985)
   PUBMED   3856868
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011498.7, AF403428.1 and AK027382.1.
            
            Summary: The leucine-rich repeat (LRR) family of proteins,
            including LRG1, have been shown to be involved in protein-protein
            interaction, signal transduction, and cell adhesion and
            development. LRG1 is expressed during granulocyte differentiation
            (O'Donnell et al., 2002 [PubMed 12223515]).[supplied by OMIM, Mar
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027382.1, SRR5189664.113946.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306390.7/ ENSP00000302621.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..347
                     /product="leucine-rich alpha-2-glycoprotein precursor"
                     /note="2310031E04Rik; 1300008B03Rik; leucine rich alpha 2
                     glycoprotein"
                     /calculated_mol_wt=34347
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3850
     mat_peptide     36..347
                     /product="Leucine-rich alpha-2-glycoprotein.
                     /id=PRO_0000020579"
                     /note="propagated from UniProtKB/Swiss-Prot (P02750.2)"
                     /calculated_mol_wt=34347
     Site            37
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine; propagated from
                     UniProtKB/Swiss-Prot (P02750.2)"
     Region          <79..319
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19838169; propagated from
                     UniProtKB/Swiss-Prot (P02750.2)"
     Region          93..114
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P02750.2)"
     Region          94..117
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          117..138
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02750.2)"
     Region          118..141
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          141..162
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P02750.2)"
     Region          142..165
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          165..186
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P02750.2)"
     Region          166..189
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
                     ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490,
                     ECO:0000269|PubMed:19838169; propagated from
                     UniProtKB/Swiss-Prot (P02750.2)"
     Region          189..210
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P02750.2)"
     Region          190..213
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          213..234
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P02750.2)"
     Region          214..237
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          237..258
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P02750.2)"
     Region          238..261
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          261..282
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P02750.2)"
     Region          262..285
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            269
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P02750.2)"
     Region          299..346
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Site            306
                     /site_type="other"
                     /note="Not glycosylated; propagated from
                     UniProtKB/Swiss-Prot (P02750.2)"
     Site            325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (P02750.2)"
     CDS             1..347
                     /gene="LRG1"
                     /gene_synonym="HMFT1766; LRG"
                     /coded_by="NM_052972.3:24..1067"
                     /db_xref="CCDS:CCDS12130.1"
                     /db_xref="GeneID:116844"
                     /db_xref="HGNC:HGNC:29480"
                     /db_xref="MIM:611289"
ORIGIN      
        1 msswsrqrpk spggiqphvs rtlfllllla asawgvtlsp kdcqvfrsdh gssiscqppa
       61 eipgylpadt vhlaveffnl thlpanllqg asklqelhls sngleslspe flrpvpqlrv
      121 ldltrnaltg lppglfqasa tldtlvlken qlevlevswl hglkalghld lsgnrlrklp
      181 pgllanftll rtldlgenql etlppdllrg plqlerlhle gnklqvlgkd lllpqpdlry
      241 lflngnklar vaagafqglr qldmldlsnn slasvpeglw aslgqpnwdm rdgfdisgnp
      301 wicdqnlsdl yrwlqaqkdk mfsqndtrca gpeavkgqtl lavaksq
//
LOCUS       NP_001014308             779 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor SPT20 homolog isoform a [Homo sapiens].
ACCESSION   NP_001014308
VERSION     NP_001014308.2
DBSOURCE    REFSEQ: accession NM_001014286.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Arata,Y., Watanabe,A., Motosugi,R., Iemura,S.I., Natsume,T.,
            Mukai,K., Taguchi,T., Hirayama,S., Hamazaki,J. and Murata,S.
  TITLE     FAM48A mediates compensatory autophagy induced by proteasome
            impairment
  JOURNAL   Genes Cells 24 (8), 559-568 (2019)
   PUBMED   31210371
  REMARK    GeneRIF: Our results indicate that FAM48A is a kind of sensor that
            is required for compensatory autophagy induction upon proteasome
            impairment.
REFERENCE   3  (residues 1 to 779)
  AUTHORS   Lin,Y., Mallen-St Clair,J., Wang,G., Luo,J., Palma-Diaz,F., Lai,C.,
            Elashoff,D.A., Sharma,S., Dubinett,S.M. and St John,M.
  TITLE     p38 MAPK mediates epithelial-mesenchymal transition by regulating
            p38IP and Snail in head and neck squamous cell carcinoma
  JOURNAL   Oral Oncol 60, 81-89 (2016)
   PUBMED   27531877
  REMARK    GeneRIF: provide the first report that p38-p38IP is required for
            the Snail-induced E-cadherin down-regulation and cell invasion in
            HNSCC
REFERENCE   4  (residues 1 to 779)
  AUTHORS   Liu,X., Xiao,W., Wang,X.D., Li,Y.F., Han,J. and Li,Y.
  TITLE     The p38-interacting protein (p38IP) regulates G2/M progression by
            promoting alpha-tubulin acetylation via inhibiting
            ubiquitination-induced degradation of the acetyltransferase GCN5
  JOURNAL   J Biol Chem 288 (51), 36648-36661 (2013)
   PUBMED   24220028
  REMARK    GeneRIF: p38IP inhibits ubiquitination-induced GCN5 degradation and
            therefore promotes alpha-tubulin acetylation, facilitating spindle
            formation and G2/M progression.
REFERENCE   5  (residues 1 to 779)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 779)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
REFERENCE   7  (residues 1 to 779)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   8  (residues 1 to 779)
  AUTHORS   Gomes,I., Sharma,T.T., Edassery,S., Fulton,N., Mar,B.G. and
            Westbrook,C.A.
  TITLE     Novel transcription factors in human CD34 antigen-positive
            hematopoietic cells
  JOURNAL   Blood 100 (1), 107-119 (2002)
   PUBMED   12070015
  REMARK    GeneRIF: Novel transcription factors identified in human CD34
            antigen-positive hematopoietic stem cells.
REFERENCE   9  (residues 1 to 779)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   10 (residues 1 to 779)
  AUTHORS   Schmidt,U., Fiedler,U., Pilarsky,C.P., Ehlers,W., Fussel,S.,
            Haase,M., Faller,G., Sauter,G. and Wirth,M.P.
  TITLE     Identification of a novel gene on chromosome 13 between BRCA-2 and
            RB-1
  JOURNAL   Prostate 47 (2), 91-101 (2001)
   PUBMED   11340631
  REMARK    GeneRIF: mRNA is down-regulated in human prostate cancer, also
            described as C13
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL391383.15 and AL138706.9.
            
            On May 18, 2006 this sequence version replaced NP_001014308.1.
            
            Transcript Variant: This variant (1) differs in the 5' UTR, has an
            alternate splice site in the 5' coding region and an additional
            exon in the 3' coding region which results in a frameshift,
            compared to variant 2. The resulting isoform (a) is longer; it
            lacks an internal aa in the N-terminal region, but has a longer and
            distinct C-terminus, compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030686.2, SRR18074969.3685803.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000350612.11/ ENSP00000218894.10
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q13.3"
     Protein         1..779
                     /product="transcription factor SPT20 homolog isoform a"
                     /note="transcription factor (p38 interacting protein);
                     suppressor of Ty 20 homolog; tumor rejection antigen;
                     protein FAM48A; family with sequence similarity 48, member
                     A; transcription factor SPT20 homolog"
                     /calculated_mol_wt=85658
     Region          76..213
                     /region_name="Spt20"
                     /note="Spt20 family; pfam12090"
                     /db_xref="CDD:463459"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TT00; propagated from
                     UniProtKB/Swiss-Prot (Q8NEM7.2)"
     Region          373..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEM7.2)"
     Region          420..507
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEM7.2)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEM7.2)"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8NEM7.2)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TT00; propagated from
                     UniProtKB/Swiss-Prot (Q8NEM7.2)"
     Region          641..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEM7.2)"
     Region          755..779
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEM7.2)"
     CDS             1..779
                     /gene="SUPT20H"
                     /gene_synonym="C13; C13orf19; FAM48A; FP757; P38IP; SPT20"
                     /coded_by="NM_001014286.3:224..2563"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31959.1"
                     /db_xref="GeneID:55578"
                     /db_xref="HGNC:HGNC:20596"
                     /db_xref="MIM:613417"
ORIGIN      
        1 mqqalelald raeyviesar qrppkrkyls sgrksvfqkl ydlyieecek epevkklrrn
       61 vnlleklvmq etlsclvvnl ypgnegyslm lrgkngsdse tirlpyeege lleyldaeel
      121 ppilvdllek sqvnifhcgc viaeirdyrq ssnmkspgyq srhillrptm qtlicdvhsi
      181 tsdnhkwtqe dklllesqli lataeplcld psiavtctan rllynkqkmn trpmkrcfkr
      241 ysrsslnrqq dlshcppppq lrlldflqkr kerkagqhyd lkiskagncv dmwkrspcnl
      301 aipsevdvek yakveksiks ddsqptvwpa hdvkddyvfe ceagtqyqkt kltilqslgd
      361 plyygkiqpc kadeesdsqm spshsstddh snwfiigskt daervvnqyq elvqneakcp
      421 vkmshsssgs aslsqvspgk etdqtetvsv qssvlgkgvk hrpppiklps ssgnsssgny
      481 ftpqqtssfl ksptpppssk pssiprkssv dlnqvsmlsp aalspasssq rttatqvman
      541 saglnfinvv gsvcgaqalm sgsnpmlgcn tgaitpagin lsgllpsggl lpnalpsamq
      601 aasqagvpfg lkntsslrpl nllqlpggsl ifntlqqqqq qlsqftpqqp qqpttcspqq
      661 pgeqgseqgs tsqeqalsaq qaavinltgv gsfmqsqaav lsqlgsaenr peqslpqqrf
      721 qlssafqqqq qqiqqlrflq hqmamaaaaa qtaqlhhhrh tgsqskskmk rgtpttpkf
//
LOCUS       NP_061921                643 aa            linear   PRI 27-APR-2025
DEFINITION  asparagine synthetase domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_061921
VERSION     NP_061921.2
DBSOURCE    REFSEQ: accession NM_019048.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Vogel,P., Ding,Z.M., Read,R., DaCosta,C.M., Hansard,M., Small,D.L.,
            Ye,G.L., Hansen,G., Brommage,R. and Powell,D.R.
  TITLE     Progressive Degenerative Myopathy and Myosteatosis in
            ASNSD1-Deficient Mice
  JOURNAL   Vet Pathol 57 (5), 723-735 (2020)
   PUBMED   32638637
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Li,J.W., Li,K., Jiang,J., Xu,X.L. and Huang,Z.Q.
  TITLE     Construction of eukaryotic expression plasmid containing HCV NS3
            segment and protein expression in human HL-7702 hepatocytes
  JOURNAL   World J Gastroenterol 12 (7), 1038-1042 (2006)
   PUBMED   16534843
  REMARK    GeneRIF: Normal human HL-7702 hepatocytes can efficiently express
            specific HCV NS3 protein in vitro.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK000759.1, AC012488.10 and BC001243.1.
            
            On Jul 19, 2017 this sequence version replaced NP_061921.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.345878.1,
                                           SRR1660803.56066.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260952.9/ ENSP00000260952.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..643
                     /product="asparagine synthetase domain-containing protein
                     1"
                     /note="HCV NS3-transactivated protein 1"
                     /calculated_mol_wt=71949
     Region          1..179
                     /region_name="Gn_AT_II_novel"
                     /note="This asparagine synthase-related domain is present
                     in eukaryotes but its function has not yet been
                     determined. The glutaminase domain catalyzes an amide
                     nitrogen transfer from glutamine to the appropriate
                     substrate. In this process, glutamine is...; cd03766"
                     /db_xref="CDD:239735"
     Site            order(2,54,76..78,91)
                     /site_type="active"
                     /db_xref="CDD:239735"
     Region          320..608
                     /region_name="Asn_synthase_B_C"
                     /note="C-terminal domain of asparagine synthase B;
                     cd01991"
                     /db_xref="CDD:467495"
     CDS             1..643
                     /gene="ASNSD1"
                     /gene_synonym="NBLA00058; NS3TP1"
                     /coded_by="NM_019048.4:375..2306"
                     /db_xref="CCDS:CCDS2300.1"
                     /db_xref="GeneID:54529"
                     /db_xref="HGNC:HGNC:24910"
                     /db_xref="MIM:619739"
ORIGIN      
        1 mcgiccsvnf saehfsqdlk edllynlkqr gpnsskqllk sdvnyqclfs ahvlhlrgvl
       61 ttqpvederg nvflwngeif sgikveaeen dtqilfnyls sckneseils lfsevqgpws
      121 fiyyqasshy lwfgrdffgr rsllwhfsnl gksfclssvg tqtsglanqw qevpasglfr
      181 idlkstvisg ciilqlypwk yisreniiee nvnslsqisa dlpafvsvva neaklylekp
      241 vvplnmmlpq aalethcsni snvpptreil qvfltdvhmk eviqqfidvl svavkkrvlc
      301 lprdenltan evlktcdrka nvailfsggi dsmviatlad rhipldepid llnvafiaee
      361 ktmpttfnre gnkqknkcei pseefskdva aaaadspnkh vsvpdritgr aglkelqavs
      421 psriwnfvei nvsmeelqkl rrtrichlir pldtvlddsi gcavwfasrg igwlvaqegv
      481 ksyqsnakvv ltgigadeql agysrhrvrf qshgleglnk eimmelgris srnlgrddrv
      541 igdhgkearf pfldenvvsf lnslpiweka nltlprgige klllrlaave lgltasallp
      601 kramqfgsri akmekineka sdkcgrlqim slenlsieke tkl
//
LOCUS       NP_775736                540 aa            linear   PRI 27-APR-2025
DEFINITION  collagen alpha-1(XXIII) chain [Homo sapiens].
ACCESSION   NP_775736
VERSION     NP_775736.2
DBSOURCE    REFSEQ: accession NM_173465.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Naba,A., Clauser,K.R., Whittaker,C.A., Carr,S.A., Tanabe,K.K. and
            Hynes,R.O.
  TITLE     Extracellular matrix signatures of human primary metastatic colon
            cancers and their metastases to liver
  JOURNAL   BMC Cancer 14, 518 (2014)
   PUBMED   25037231
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Wade,T.D., Gordon,S., Medland,S., Bulik,C.M., Heath,A.C.,
            Montgomery,G.W. and Martin,N.G.
  TITLE     Genetic variants associated with disordered eating
  JOURNAL   Int J Eat Disord 46 (6), 594-608 (2013)
   PUBMED   23568457
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Veit,G., Zwolanek,D., Eckes,B., Niland,S., Kapyla,J., Zweers,M.C.,
            Ishada-Yamamoto,A., Krieg,T., Heino,J., Eble,J.A. and Koch,M.
  TITLE     Collagen XXIII, novel ligand for integrin alpha2beta1 in the
            epidermis
  JOURNAL   J Biol Chem 286 (31), 27804-27813 (2011)
   PUBMED   21652699
  REMARK    GeneRIF: data suggest that extracellular membrane-bound CAIV, but
            not cytosolic CAII, augments transport activity of MCT2 in a
            non-catalytic manner, possibly by facilitating a proton pathway
            other than His-88
REFERENCE   5  (residues 1 to 540)
  AUTHORS   Spivey,K.A., Banyard,J., Solis,L.M., Wistuba,I.I., Barletta,J.A.,
            Gandhi,L., Feldman,H.A., Rodig,S.J., Chirieac,L.R. and Zetter,B.R.
  TITLE     Collagen XXIII: a potential biomarker for the detection of primary
            and recurrent non-small cell lung cancer
  JOURNAL   Cancer Epidemiol Biomarkers Prev 19 (5), 1362-1372 (2010)
   PUBMED   20447926
  REMARK    GeneRIF: High COL23A1 expression is associated with recurrent
            non-small cell lung cancer.
REFERENCE   6  (residues 1 to 540)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of gene polymorphisms with chronic kidney disease in
            Japanese individuals
  JOURNAL   Int J Mol Med 24 (4), 539-547 (2009)
   PUBMED   19724895
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 540)
  AUTHORS   Veit,G., Zimina,E.P., Franzke,C.W., Kutsch,S., Siebolds,U.,
            Gordon,M.K., Bruckner-Tuderman,L. and Koch,M.
  TITLE     Shedding of collagen XXIII is mediated by furin and depends on the
            plasma membrane microenvironment
  JOURNAL   J Biol Chem 282 (37), 27424-27435 (2007)
   PUBMED   17627939
  REMARK    GeneRIF: newly synthesized collagen XXIII either is cleaved inside
            the Golgi/trans-Golgi network or reaches the cell surface, where it
            becomes protected from processing by being localized in lipid
            rafts.
REFERENCE   8  (residues 1 to 540)
  AUTHORS   Koch,M., Veit,G., Stricker,S., Bhatt,P., Kutsch,S., Zhou,P.,
            Reinders,E., Hahn,R.A., Song,R., Burgeson,R.E., Gerecke,D.R.,
            Mundlos,S. and Gordon,M.K.
  TITLE     Expression of type XXIII collagen mRNA and protein
  JOURNAL   J Biol Chem 281 (30), 21546-21557 (2006)
   PUBMED   16728390
  REMARK    GeneRIF: analysis of collagen XXIII mRNA and protein
REFERENCE   9  (residues 1 to 540)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   10 (residues 1 to 540)
  AUTHORS   Banyard,J., Bao,L. and Zetter,B.R.
  TITLE     Type XXIII collagen, a new transmembrane collagen identified in
            metastatic tumor cells
  JOURNAL   J Biol Chem 278 (23), 20989-20994 (2003)
   PUBMED   12644459
  REMARK    GeneRIF: identification and cloning; a new member of the
            transmembrane collagen family, showing structural homology with the
            transmembrane collagens XIII and XXV
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY898961.1 and AW014891.1.
            
            On Apr 10, 2003 this sequence version replaced NP_775736.1.
            
            Summary: COL23A1 is a member of the transmembrane collagens, a
            subfamily of the nonfibrillar collagens that contain a single pass
            hydrophobic transmembrane domain (Banyard et al., 2003 [PubMed
            12644459]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY158895.1, AY898961.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000390654.8/ ENSP00000375069.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..540
                     /product="collagen alpha-1(XXIII) chain"
                     /note="procollagen, type XXIII, alpha 1; collagen, type
                     XXIII, alpha 1"
                     /calculated_mol_wt=51813
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86Y22.1)"
     Site            35..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86Y22.1)"
     Region          109..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86Y22.1)"
     Region          <134..>384
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <265..533
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          316..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86Y22.1)"
     CDS             1..540
                     /gene="COL23A1"
                     /coded_by="NM_173465.4:197..1819"
                     /db_xref="CCDS:CCDS4436.1"
                     /db_xref="GeneID:91522"
                     /db_xref="HGNC:HGNC:22990"
                     /db_xref="MIM:610043"
ORIGIN      
        1 mgpgeraggg gdagkgnaag gggggrsatt agsravsalc lllsvgsaaa clllgvqaaa
       61 lqgrvaalee erellrragp pgaldawaep hlerllrekl dglakirtar eapsecvcpp
      121 gppgrrgkpg rrgdpgppgq sgrdgypgpl gldgkpglpg pkgekgapgd fgprgdqgqd
      181 gaagppgppg ppgargppgd tgkdgprgaq gpagpkgepg qdgemgpkgp pgpkgepgvp
      241 gkkgddgtps qpgppgpkge pgsmgprgen gvdgapgpkg epghrgtdga agprgapglk
      301 geqgdtvvid ydgrildalk gppgpqgppg ppgipgakge lglpgapgid gekgpkgqkg
      361 dpgepgpagl kgeagemgls glpgadglkg ekgesasdsl qeslaqlive pgppgppgpp
      421 gpmglqgiqg pkgldgakge kgasgergps glpgpvgppg liglpgtkge kgrpgepgld
      481 gfpgprgekg drsergekge rgvpgrkgvk gqkgepgppg ldqpcpvgpd glpvpgcwhk
//
LOCUS       NP_001351215             301 aa            linear   PRI 27-APR-2025
DEFINITION  aquaporin-4 isoform M23 [Homo sapiens].
ACCESSION   NP_001351215
VERSION     NP_001351215.1
DBSOURCE    REFSEQ: accession NM_001364286.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Braun,M., Sevao,M., Keil,S.A., Gino,E., Wang,M.X., Lee,J.,
            Haveliwala,M.A., Klein,E., Agarwal,S., Pedersen,T., Rhodes,C.H.,
            Jansson,D., Cook,D., Peskind,E., Perl,D.P., Piantino,J.,
            Schindler,A.G. and Iliff,J.J.
  TITLE     Macroscopic changes in aquaporin-4 underlie blast traumatic brain
            injury-related impairment in glymphatic function
  JOURNAL   Brain 147 (6), 2214-2229 (2024)
   PUBMED   38802114
  REMARK    GeneRIF: Macroscopic changes in aquaporin-4 underlie blast
            traumatic brain injury-related impairment in glymphatic function.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   De Bellis,M., Pisani,F., Mola,M.G., Rosito,S., Simone,L.,
            Buccoliero,C., Trojano,M., Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     Translational readthrough generates new astrocyte AQP4 isoforms
            that modulate supramolecular clustering, glial endfeet
            localization, and water transport
  JOURNAL   Glia 65 (5), 790-803 (2017)
   PUBMED   28206694
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   4  (residues 1 to 301)
  AUTHORS   De Bellis,M., Pisani,F., Mola,M.G., Basco,D., Catalano,F.,
            Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     A novel human aquaporin-4 splice variant exhibits a
            dominant-negative activity: a new mechanism to regulate water
            permeability
  JOURNAL   Mol Biol Cell 25 (4), 470-480 (2014)
   PUBMED   24356448
  REMARK    GeneRIF: The expression of AQP4-Delta4 may represent a new
            regulatory mechanism through which the cell-surface expression and
            therefore the activity of AQP4 can be physiologically modulated.
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Rossi,A., Pisani,F., Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     Evidences for a leaky scanning mechanism for the synthesis of the
            shorter M23 protein isoform of aquaporin-4: implication in
            orthogonal array formation and neuromyelitis optica antibody
            interaction
  JOURNAL   J Biol Chem 285 (7), 4562-4569 (2010)
   PUBMED   20007705
  REMARK    GeneRIF: In cells transiently transfected with AQP4-M1 coding
            sequence we observed besides AQP4-M1 the additional presence of the
            AQP4-M23 isoform associated with the formation of typical
            orthogonal arrays of particles.
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Umenishi,F. and Verkman,A.S.
  TITLE     Isolation and functional analysis of alternative promoters in the
            human aquaporin-4 water channel gene
  JOURNAL   Genomics 50 (3), 373-377 (1998)
   PUBMED   9676432
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Lu,M., Lee,M.D., Smith,B.L., Jung,J.S., Agre,P., Verdijk,M.A.,
            Merkx,G., Rijss,J.P. and Deen,P.M.
  TITLE     The human AQP4 gene: definition of the locus encoding two water
            channel polypeptides in brain
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10908-10912 (1996)
   PUBMED   8855281
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Yang,B., Ma,T. and Verkman,A.S.
  TITLE     cDNA cloning, gene organization, and chromosomal localization of a
            human mercurial insensitive water channel. Evidence for distinct
            transcriptional units
  JOURNAL   J Biol Chem 270 (39), 22907-22913 (1995)
   PUBMED   7559426
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Min,R., Abbink,T.E.M. and van der Knaap,M.S.
  TITLE     Megalencephalic Leukoencephalopathy with Subcortical Cysts
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HQ901095.1, AK222684.1,
            DT220791.1, DA244620.1, AC018371.10 and BU687682.1.
            
            Summary: This gene encodes a member of the aquaporin family of
            intrinsic membrane proteins that function as water-selective
            channels in the plasma membranes of many cells. This protein is the
            predominant aquaporin found in brain and has an important role in
            brain water homeostasis. Alternatively spliced transcript variants
            encoding different isoforms have been described for this gene.
            Additional isoforms, resulting from the use of alternative in-frame
            translation initiation codons, have also been described. Recent
            studies provided evidence for translational readthrough in this
            gene, and expression of C-terminally extended isoforms via the use
            of an alternative in-frame translation termination codon. [provided
            by RefSeq, Jun 2018].
            
            Transcript Variant: This variant (1, also known as hMIWC2)
            represents the predominant transcript and encodes four isoforms,
            resulting from the use of two alternative in-frame translation
            initiation codons and two alternative in-frame translation
            termination codons. This RefSeq represents isoform M23, which
            results from the use of the downstream in-frame AUG start codon and
            the upstream UGA stop codon. Isoform M23 has a shorter N-terminus
            compared to isoform M1. An alternatively spliced transcript variant
            (NM_004028.4) encodes the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.52586.1,
                                           SRR1803612.168247.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147920, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:20007705)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..301
                     /product="aquaporin-4 isoform M23"
                     /note="mercurial-insensitive water channel; aquaporin
                     type4"
                     /calculated_mol_wt=32169
     Region          9..226
                     /region_name="MIP"
                     /note="Major intrinsic protein; pfam00230"
                     /db_xref="CDD:395174"
     Site            order(55,73..75,187..188,191,194)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            order(75..77,191..193)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     CDS             1..301
                     /gene="AQP4"
                     /gene_synonym="hAQP4; MIWC; MLC4; WCH4"
                     /coded_by="NM_001364286.1:181..1086"
                     /note="isoform M23 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS58617.1"
                     /db_xref="GeneID:361"
                     /db_xref="HGNC:HGNC:637"
                     /db_xref="MIM:600308"
ORIGIN      
        1 mvafkgvwtq afwkavtaef lamlifvlls lgstinwggt ekplpvdmvl islcfglsia
       61 tmvqcfghis gghinpavtv amvctrkisi aksvfyiaaq clgaiigagi lylvtppsvv
      121 gglgvtmvhg nltaghgllv eliitfqlvf tifascdskr tdvtgsiala igfsvaighl
      181 fainytgasm nparsfgpav imgnwenhwi ywvgpiigav lagglyeyvf cpdvefkrrf
      241 keafskaaqq tkgsymeved nrsqvetddl ilkpgvvhvi dvdrgeekkg kdqsgevlss
      301 v
//
LOCUS       NP_068776                703 aa            linear   PRI 27-APR-2025
DEFINITION  glycogen [starch] synthase, liver [Homo sapiens].
ACCESSION   NP_068776
VERSION     NP_068776.2
DBSOURCE    REFSEQ: accession NM_021957.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Ilyas,M., Holzwarth,D., Ishaq,R., Ali,Y., Habiba,U., Raja,A.M.,
            Saeed,S., Abdullah,U., Khan,S.N., Ullah,A., Raja,G.K., Baig,S.M.,
            Fazeli,W., Kunz,W.S. and Shaiq,P.A.
  TITLE     Whole-Exome sequencing identifies GYS2 biallelic variants in
            individuals with suspected epilepsy
  JOURNAL   Seizure 116, 74-80 (2024)
   PUBMED   37574425
  REMARK    GeneRIF: Whole-Exome sequencing identifies GYS2 biallelic variants
            in individuals with suspected epilepsy.
REFERENCE   2  (residues 1 to 703)
  AUTHORS   A,S., Wu,H., Wang,X., Wang,X., Yang,J., Xia,L. and Xia,Y.
  TITLE     Value of glycogen synthase 2 in intrahepatic cholangiocarcinoma
            prognosis assessment and its influence on the activity of cancer
            cells
  JOURNAL   Bioengineered 12 (2), 12167-12178 (2021)
   PUBMED   34783271
  REMARK    GeneRIF: Value of glycogen synthase 2 in intrahepatic
            cholangiocarcinoma prognosis assessment and its influence on the
            activity of cancer cells.
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Arko,J.J., Debeljak,M., Tansek,M.Z., Battelino,T. and Groselj,U.
  TITLE     A patient with glycogen storage disease type 0 and a novel sequence
            variant in GYS2: a case report and literature review
  JOURNAL   J Int Med Res 48 (8), 300060520936857 (2020)
   PUBMED   32779500
  REMARK    GeneRIF: A patient with glycogen storage disease type 0 and a novel
            sequence variant in GYS2: a case report and literature review.
            Review article
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Chen,S.L., Zhang,C.Z., Liu,L.L., Lu,S.X., Pan,Y.H., Wang,C.H.,
            He,Y.F., Lin,C.S., Yang,X., Xie,D. and Yun,J.P.
  TITLE     A GYS2/p53 Negative Feedback Loop Restricts Tumor Growth in
            HBV-Related Hepatocellular Carcinoma
  JOURNAL   Cancer Res 79 (3), 534-545 (2019)
   PUBMED   30584071
  REMARK    GeneRIF: Findings suggest that GYS2 serves as a prognostic factor
            and functions as a tumor suppressor in HCC. The newly identified
            HBx/GYS2/p53 axis is responsible for the deregulation of glycogen
            metabolism.
REFERENCE   5  (residues 1 to 703)
  AUTHORS   Kasapkara,C.S., Aycan,Z., Acoglu,E., Senel,S., Oguz,M.M. and
            Ceylaner,S.
  TITLE     The variable clinical phenotype of three patients with hepatic
            glycogen synthase deficiency
  JOURNAL   J Pediatr Endocrinol Metab 30 (4), 459-462 (2017)
   PUBMED   28245189
  REMARK    GeneRIF: Mutation in GYS2 gene is associated with hepatic glycogen
            synthase deficiency.
REFERENCE   6  (residues 1 to 703)
  AUTHORS   Orho,M., Bosshard,N.U., Buist,N.R., Gitzelmann,R.,
            Aynsley-Green,A., Blumel,P., Gannon,M.C., Nuttall,F.Q. and
            Groop,L.C.
  TITLE     Mutations in the liver glycogen synthase gene in children with
            hypoglycemia due to glycogen storage disease type 0
  JOURNAL   J Clin Invest 102 (3), 507-515 (1998)
   PUBMED   9691087
REFERENCE   7  (residues 1 to 703)
  AUTHORS   Nuttall,F.Q., Gannon,M.C., Bai,G. and Lee,E.Y.
  TITLE     Primary structure of human liver glycogen synthase deduced by cDNA
            cloning
  JOURNAL   Arch Biochem Biophys 311 (2), 443-449 (1994)
   PUBMED   8203908
REFERENCE   8  (residues 1 to 703)
  AUTHORS   Nuttall,F.Q., Gannon,M.C., Kubic,V.L. and Hoyt,K.J.
  TITLE     The human liver Glycogen synthase isozyme gene is located on the
            short arm of chromosome 12
  JOURNAL   Genomics 19 (2), 404-405 (1994)
   PUBMED   8188280
REFERENCE   9  (residues 1 to 703)
  AUTHORS   Westphal,S.A. and Nuttall,F.Q.
  TITLE     Comparative characterization of human and rat liver glycogen
            synthase
  JOURNAL   Arch Biochem Biophys 292 (2), 479-486 (1992)
   PUBMED   1731614
REFERENCE   10 (residues 1 to 703)
  AUTHORS   Stalmans,W., Bollen,M., Toth,B. and Gergely,P.
  TITLE     Short-term hormonal control of protein phosphatases involved in
            hepatic glycogen metabolism
  JOURNAL   Adv Enzyme Regul 30, 305-327 (1990)
   PUBMED   2169698
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB185936.1, BC126310.1,
            AV653197.1 and AC006559.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 13, 2006 this sequence version replaced NP_068776.1.
            
            Summary: The protein encoded by this gene, liver glycogen synthase,
            catalyzes the rate-limiting step in the synthesis of glycogen - the
            transfer of a glucose molecule from UDP-glucose to a terminal
            branch of the glycogen molecule. Mutations in this gene cause
            glycogen storage disease type 0 (GSD-0) - a rare type of early
            childhood fasting hypoglycemia with decreased liver glycogen
            content. [provided by RefSeq, Dec 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D29685.1, S70004.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261195.3/ ENSP00000261195.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..703
                     /product="glycogen [starch] synthase, liver"
                     /EC_number="2.4.1.11"
                     /note="glycogen synthase 2 (liver)"
                     /calculated_mol_wt=80858
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P17625; propagated from
                     UniProtKB/Swiss-Prot (P54840.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCB3; propagated from
                     UniProtKB/Swiss-Prot (P54840.2)"
     Region          33..658
                     /region_name="Glycogen_syn"
                     /note="Glycogen synthase; pfam05693"
                     /db_xref="CDD:399009"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P54840.2)"
     Region          628..703
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54840.2)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha and GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P54840.2)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha and GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P54840.2)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha and GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P54840.2)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha and GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P54840.2)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P54840.2)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P54840.2)"
     CDS             1..703
                     /gene="GYS2"
                     /coded_by="NM_021957.4:256..2367"
                     /db_xref="CCDS:CCDS8690.1"
                     /db_xref="GeneID:2998"
                     /db_xref="HGNC:HGNC:4707"
                     /db_xref="MIM:138571"
ORIGIN      
        1 mlrgrslsvt slgglpqwev eelpveelll fevawevtnk vggiytviqt kakttadewg
       61 enyfligpyf ehnmktqveq cepvndavrr avdamnkhgc qvhfgrwlie gspyvvlfdi
      121 gysawnldrw kgdlweacsv gipyhdrean dmlifgslta wflkevtdha dgkyvvaqfh
      181 ewqagiglil srarklpiat iftthatllg rylcaanidf ynhldkfnid keagerqiyh
      241 rycmerasvh cahvfttvse itaieaehml krkpdvvtpn glnvkkfsav hefqnlhamy
      301 kariqdfvrg hfyghldfdl ektlflfiag ryefsnkgad ifleslsrln fllrmhksdi
      361 tvmvffimpa ktnnfnvetl kgqavrkqlw dvahsvkekf gkklydallr geipdlndil
      421 drddltimkr aifstqrqsl ppvtthnmid dstdpilsti rriglfnnrt drvkvilhpe
      481 flsstspllp mdyeefvrgc hlgvfpsyye pwgytpaect vmgipsvttn lsgfgcfmqe
      541 hvadptaygi yivdrrfrsp ddscnqltkf lygfckqsrr qriiqrnrte rlsdlldwry
      601 lgryyqharh ltlsrafpdk fhveltsppt tegfkyprps svppspsgsq asspqssdve
      661 devederyde eeeaerdrln ikspfslshv phgkkklhge ykn
//
LOCUS       NP_001257306             228 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 46 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001257306
VERSION     NP_001257306.1
DBSOURCE    REFSEQ: accession NM_001270377.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Cheng,L., Wang,P., Yang,S., Yang,Y., Zhang,Q., Zhang,W., Xiao,H.,
            Gao,H. and Zhang,Q.
  TITLE     Identification of genes with a correlation between copy number and
            expression in gastric cancer
  JOURNAL   BMC Med Genomics 5, 14 (2012)
   PUBMED   22559327
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Yan,L.X., Wu,Q.N., Zhang,Y., Li,Y.Y., Liao,D.Z., Hou,J.H., Fu,J.,
            Zeng,M.S., Yun,J.P., Wu,Q.L., Zeng,Y.X. and Shao,J.Y.
  TITLE     Knockdown of miR-21 in human breast cancer cell lines inhibits
            proliferation, in vitro migration and in vivo tumor growth
  JOURNAL   Breast Cancer Res 13 (1), R2 (2011)
   PUBMED   21219636
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
  REMARK    Review article
REFERENCE   5  (residues 1 to 228)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
  REMARK    Review article
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Tkatchenko,A.V., Pietu,G., Cros,N., Gannoun-Zaki,L., Auffray,C.,
            Leger,J.J. and Dechesne,C.A.
  TITLE     Identification of altered gene expression in skeletal muscles from
            Duchenne muscular dystrophy patients
  JOURNAL   Neuromuscul Disord 11 (3), 269-277 (2001)
   PUBMED   11297942
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA503253.1, AK095235.1,
            AP000424.3 and AB077205.1.
            
            Summary: This gene encodes a protein containing multiple ankyrin
            repeats. Ankyrin domains function in protein-protein interactions
            in a variety of cellular processes. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (1) encodes the shorter protein
            (isoform 1). Variants 1, 2, and 3 encode the same protein (isoform
            1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060843.1, SRR3476690.1082506.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335659.7/ ENSP00000335287.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..228
                     /product="ankyrin repeat domain-containing protein 46
                     isoform 1"
                     /note="ankyrin repeat domain-containing protein 46;
                     ankyrin repeat small protein"
                     /calculated_mol_wt=25199
     Region          11..40
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86W74.2)"
     Region          <15..>128
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          15..42
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(17..18,21..23,25..26,30,33,42,44,46,50..51,54..56,
                     58..59,63,66,75,77,79,83..84,85..86,88..89,93,96,105)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          44..75
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          44..73
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86W74.2)"
     Region          77..105
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          77..103
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86W74.2)"
     Region          107..138
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86W74.2)"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86W74.2)"
     CDS             1..228
                     /gene="ANKRD46"
                     /gene_synonym="ANK-S; GENX-115279"
                     /coded_by="NM_001270377.2:180..866"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6287.1"
                     /db_xref="GeneID:157567"
                     /db_xref="HGNC:HGNC:27229"
ORIGIN      
        1 msyvfvndss qtnvpllqac idgdfnyskr llesgfdpni rdsrgrtglh laaargnvdi
       61 cqllhkfgad llatdyqgnt alhlcghvdt iqflvsnglk idicnhqgat plvlakrrgv
      121 nkdvirlles leeqevkgfn rgthskletm qtaesesame shsllnpnlq qgegvlssfr
      181 ttwqefvedl gfwrvlllif viallslgia yyvsgvlpfv enqpelvh
//
LOCUS       NP_695001                363 aa            linear   PRI 27-APR-2025
DEFINITION  uncharacterized protein C20orf96 isoform 1 [Homo sapiens].
ACCESSION   NP_695001
VERSION     NP_695001.2
DBSOURCE    REFSEQ: accession NM_153269.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB226405.1, AK097394.1, EL734555.1, BC134417.1, DB320878.1 and
            AA921838.1.
            
            On May 21, 2011 this sequence version replaced NP_695001.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK097394.1, SRR3476690.11310.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360321.7/ ENSP00000353470.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..363
                     /product="uncharacterized protein C20orf96 isoform 1"
                     /note="uncharacterized protein C20orf96"
                     /calculated_mol_wt=42728
     Region          105..362
                     /region_name="DUF4618"
                     /note="Domain of unknown function (DUF4618); pfam15397"
                     /db_xref="CDD:464704"
     CDS             1..363
                     /gene="C20orf96"
                     /gene_synonym="dJ1103G7.2"
                     /coded_by="NM_153269.3:141..1232"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12994.1"
                     /db_xref="GeneID:140680"
                     /db_xref="HGNC:HGNC:16227"
ORIGIN      
        1 mahvlqkpkh sgthsivqef qvpdyvpwqq skqetkpstl ppvqqanslh tskmktltrv
       61 qpvfhfkptt vvtscqpknp relhrrrkld pgkmhakiwl mktslrsgra alrelrsren
      121 flsklnreli etiqemenst tlhvrallqq qdtlatiidi leysnkkrlq qlkselqewe
      181 ekkkckmsyl eqqaeqlnak iektqeevnf lstymdheys iksvqistlm rqlqqvkdsq
      241 qdelddlgem rrkvleslsd kiqkkkkkil ssvvaetqrp yeeallqkmw esqdflkcmq
      301 rfreiidqfe enmpvlraev eelqaqtrep revifedvll rrpkctpdmd vilnipveep
      361 lpf
//
LOCUS       NP_998796                608 aa            linear   PRI 27-APR-2025
DEFINITION  protein MROH8 isoform 2 [Homo sapiens].
ACCESSION   NP_998796
VERSION     NP_998796.1
DBSOURCE    REFSEQ: accession NM_213631.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Potkin,S.G., Guffanti,G., Lakatos,A., Turner,J.A., Kruggel,F.,
            Fallon,J.H., Saykin,A.J., Orro,A., Lupoli,S., Salvi,E., Weiner,M.
            and Macciardi,F.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     Hippocampal atrophy as a quantitative trait in a genome-wide
            association study identifying novel susceptibility genes for
            Alzheimer's disease
  JOURNAL   PLoS One 4 (8), e6501 (2009)
   PUBMED   19668339
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   4  (residues 1 to 608)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC030006.1, AL136172.16,
            BC057767.1 and AK093432.1.
            
            Summary: The protein encoded by this gene belongs to the maestro
            heat-like repeat family. The exact function of this gene is not
            known, however, in a genome-wide association study using
            hippocampal atrophy as a quantitative trait, this gene has been
            associated with Alzheimer's disease (PMID:19668339). Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (2) differs at the 3' end compared
            to variant 1. The encoded isoform (2) is shorter with a distinct
            C-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057767.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.23"
     Protein         1..608
                     /product="protein MROH8 isoform 2"
                     /note="maestro heat-like repeat-containing protein family
                     member 8"
                     /calculated_mol_wt=68488
     CDS             1..608
                     /gene="MROH8"
                     /gene_synonym="C20orf131; C20orf132"
                     /coded_by="NM_213631.3:69..1895"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:140699"
                     /db_xref="HGNC:HGNC:16125"
ORIGIN      
        1 mplsrrgrgs rlagsraats nlpratalsp ksagrgalsi shaqlltrrr hsseqvppes
       61 epradfrsgk wlqepatgda rdsrqalrar msskhricsq eevvipcayd sdsesvdlel
      121 snleiikkgs ssieltdldi pdipglhcep lshsprhltq qdplseaive kliqsiqkvf
      181 ngelkgelek lkflgdlssl sqalpydeta ksfihshiad ivhtlnvlvq eerphslsss
      241 mrqevfvtia dlsyqdvhll lgsedraelf sltiksiitl psvrtltqiq eimpngtcnt
      301 eclyrqtfqa fsemlqslvv kdphlenldt iikhlvpwlq svkdherera tasmaqvlkc
      361 lskhlnlklp lrfqrlghlv almallcgdp qekvaeeaae gihsllhitl rlkyithdkk
      421 dqqnlkralt kcreflelhs saakcfyncp friaqvfegf ldsnelcqfi mttfdtlktl
      481 khpciqrsag ellltlaknt esqfekvpei mgvicaqlsi isqprvrqqi intvslfisr
      541 pkytdivlsf llchpvpynr hlaevwrmls velpsttwil wrllrklqkc hnepaqekma
      601 yvavavsp
//
LOCUS       NP_001349886             809 aa            linear   ROD 27-APR-2025
DEFINITION  rab GTPase-activating protein 1 isoform b [Mus musculus].
ACCESSION   NP_001349886
VERSION     NP_001349886.1
DBSOURCE    REFSEQ: accession NM_001362957.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Oh,R.Y., Deshwar,A.R., Marwaha,A., Sabha,N., Tropak,M., Hou,H.,
            Yuki,K.E., Wilson,M.D., Rump,P., Lunsing,R., Elserafy,N.,
            Chung,C.W.T., Hewson,S., Klein-Rodewald,T., Calzada-Wack,J.,
            Sanz-Moreno,A., Kraiger,M., Marschall,S., Fuchs,H.,
            Gailus-Durner,V., Hrabe de Angelis,M., Dowling,J. and Schulze,A.
  TITLE     Biallelic loss-of-function variants in RABGAP1 cause a novel
            neurodevelopmental syndrome
  JOURNAL   Genet Med 24 (11), 2399-2407 (2022)
   PUBMED   36083289
  REMARK    GeneRIF: Biallelic loss-of-function variants in RABGAP1 cause a
            novel neurodevelopmental syndrome.
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Samarelli,A.V., Ziegler,T., Meves,A., Fassler,R. and Bottcher,R.T.
  TITLE     Rabgap1 promotes recycling of active beta1 integrins to support
            effective cell migration
  JOURNAL   J Cell Sci 133 (18) (2020)
   PUBMED   32843574
  REMARK    GeneRIF: Rabgap1 promotes recycling of active beta1 integrins to
            support effective cell migration.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 809)
  AUTHORS   Fededa,J.P., Esk,C., Mierzwa,B., Stanyte,R., Yuan,S., Zheng,H.,
            Ebnet,K., Yan,W., Knoblich,J.A. and Gerlich,D.W.
  TITLE     MicroRNA-34/449 controls mitotic spindle orientation during
            mammalian cortex development
  JOURNAL   EMBO J 35 (22), 2386-2398 (2016)
   PUBMED   27707753
REFERENCE   5  (residues 1 to 809)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL953890.7.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660811.184821.1,
                                           SRR7652917.1170162.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 24.19 cM"
     Protein         1..809
                     /product="rab GTPase-activating protein 1 isoform b"
                     /note="rab6 GTPase activating protein (GAP and
                     centrosome-associated); rab GTPase-activating protein 1;
                     GAP and centrosome-associated protein; rab6
                     GTPase-activating protein GAPCenA"
                     /calculated_mol_wt=90953
     Region          1..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2AWA9.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (A2AWA9.1)"
     Region          140..268
                     /region_name="PTB_Rab6GAP"
                     /note="GTPase activating protein for Rab 6
                     Phosphotyrosine-binding (PTB) domain; cd01211"
                     /db_xref="CDD:269922"
     Site            order(146,224,244)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269922"
     Site            order(210..215,231,252,256)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269922"
     Region          302..432
                     /region_name="DUF3694"
                     /note="Kinesin protein; pfam12473"
                     /db_xref="CDD:463599"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (A2AWA9.1)"
     Region          478..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2AWA9.1)"
     Region          558..767
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            603
                     /site_type="other"
                     /note="Arginine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (A2AWA9.1)"
     Site            644
                     /site_type="other"
                     /note="Glutamine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (A2AWA9.1)"
     CDS             1..809
                     /gene="Rabgap1"
                     /gene_synonym="Gapcena; mKIAA4104"
                     /coded_by="NM_001362957.1:223..2652"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS16003.1"
                     /db_xref="GeneID:227800"
                     /db_xref="MGI:MGI:2385139"
ORIGIN      
        1 mddkasvgki svssdsvstl nsedfvlvsr qgdetpstnn gsddektglk ivgngseqql
       61 qkeladvlmd ppmddqpger sqldgegdgp lsnqlsasst inpvplvglp kpemslpvkp
      121 gqgdsevssp ftpvadedsv vfnkltylgc asvnaprsev ealrmmsilr sqcqisldvt
      181 lsvpnvsegt vrlldpqtnt eianypiyki lfcvrghdgt pesdcfafte shynaelfri
      241 hvfrceiqea vsrilysfat afrrsakqtp lsataapqtp dsdiftfsvs leikeddgkg
      301 yfsavpkdkd rqcfklrqgi dkkivicvqq tankelaier cfglllspgk dvrnsdmhll
      361 dlesmgkssd gksyvitgsw npksphfqvv neetpkdkvl fmttavdlvi tevqepvrfl
      421 letkvrvcsp nerlfwpfsk rsttenfflk lkqikqkekk nnadtlyevv cleseserer
      481 rkttaspsvr lpqsgsqssm ipsppeddee edndepllsg fgdvskecae kiletwgell
      541 skwhlnlsvr pkqlsslvrs gvpealrgev wqllagchnn dhlvekyril itkespqdsa
      601 itrdinrtfp ahdyfkdtgg dgqdslykic kaysvydeei gycqgqsfla avlllhmpee
      661 qafsvlvkim fdyglrelfk qnfedlhckf yqlerlmqey ipdlynhfld isleahmyas
      721 qwfltlftak fplymvfhii dlllcegisv ifnvalgllk tskddllltd fegalkffrv
      781 qlpkryrsee nakrlmelac ntkvqqrll
//
LOCUS       NP_000786                443 aa            linear   PRI 27-APR-2025
DEFINITION  D(2) dopamine receptor isoform long [Homo sapiens].
ACCESSION   NP_000786
VERSION     NP_000786.1
DBSOURCE    REFSEQ: accession NM_000795.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Lambert,J., Petrovitch,D., Himes,K.P., Freiermuth,C.E., Braun,R.S.,
            Brown,J.L., Bischof,J.J., Lyons,M.S., Punches,B.E.,
            Littlefield,A.K., Kisor,D.F. and Sprague,J.E.
  TITLE     Association of genetic variants in CYP3A5, DRD2 and NK1R with
            opioid overdose
  JOURNAL   Chem Biol Interact 403, 111242 (2024)
   PUBMED   39265714
  REMARK    GeneRIF: Association of genetic variants in CYP3A5, DRD2 and NK1R
            with opioid overdose.
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Qu,K., He,Y., Zhang,Z., Cao,Y., Qin,Q., Zhou,Z. and Zhen,L.
  TITLE     Association Study Between DRD2, DRD3 Genetic Polymorphisms and
            Adverse Reactions in Chinese Patients on Amisulpride Treatment
  JOURNAL   Pharmacopsychiatry 57 (6), 283-289 (2024)
   PUBMED   39187246
  REMARK    GeneRIF: Association Study Between DRD2, DRD3 Genetic Polymorphisms
            and Adverse Reactions in Chinese Patients on Amisulpride Treatment.
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yang,Q., Zhang,X., Zhang,L., Cheng,C. and Zhao,J.
  TITLE     Exploring the influence of the DRD2 gene on mathematical ability:
            perspectives of gene association and gene-environment interaction
  JOURNAL   BMC Psychol 12 (1), 572 (2024)
   PUBMED   39425204
  REMARK    GeneRIF: Exploring the influence of the DRD2 gene on mathematical
            ability: perspectives of gene association and gene-environment
            interaction.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Ricard,J.A., Labache,L., Segal,A., Dhamala,E., Cocuzza,C.V.,
            Jones,G., Yip,S.W., Chopra,S. and Holmes,A.J.
  TITLE     A shared spatial topography links the functional connectome
            correlates of cocaine use disorder and dopamine D2/3 receptor
            densities
  JOURNAL   Commun Biol 7 (1), 1178 (2024)
   PUBMED   39300138
  REMARK    GeneRIF: A shared spatial topography links the functional
            connectome correlates of cocaine use disorder and dopamine D2/3
            receptor densities.
            Erratum:[Commun Biol. 2025 Feb 23;8(1):293. doi:
            10.1038/s42003-025-07723-7. PMID: 39988590]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Mathis,T., Baudin,F., Mariet,A.S., Augustin,S., Bricout,M.,
            Przegralek,L., Roubeix,C., Benzenine,E., Blot,G., Nous,C.,
            Kodjikian,L., Mauget-Faysse,M., Sahel,J.A., Plevin,R., Zeitz,C.,
            Delarasse,C., Guillonneau,X., Creuzot-Garcher,C., Quantin,C.,
            Hunot,S. and Sennlaub,F.
  TITLE     DRD2 activation inhibits choroidal neovascularization in patients
            with Parkinson's disease and age-related macular degeneration
  JOURNAL   J Clin Invest 134 (17), e174199 (2024)
   PUBMED   39012703
  REMARK    GeneRIF: DRD2 activation inhibits choroidal neovascularization in
            patients with Parkinson's disease and age-related macular
            degeneration.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Raymond,D., Saunders-Pullman,R. and Ozelius,L.
  TITLE     SGCE Myoclonus-Dystonia
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301587
REFERENCE   7  (residues 1 to 443)
  AUTHORS   Eubanks,J.H., Djabali,M., Selleri,L., Grandy,D.K., Civelli,O.,
            McElligott,D.L. and Evans,G.A.
  TITLE     Structure and linkage of the D2 dopamine receptor and neural cell
            adhesion molecule genes on human chromosome 11q23
  JOURNAL   Genomics 14 (4), 1010-1018 (1992)
   PUBMED   1478642
REFERENCE   8  (residues 1 to 443)
  AUTHORS   Liu,Y.F., Civelli,O., Grandy,D.K. and Albert,P.R.
  TITLE     Differential sensitivity of the short and long human dopamine D2
            receptor subtypes to protein kinase C
  JOURNAL   J Neurochem 59 (6), 2311-2317 (1992)
   PUBMED   1331329
REFERENCE   9  (residues 1 to 443)
  AUTHORS   Araki,K., Kuwano,R., Morii,K., Hayashi,S., Minoshima,S.,
            Shimizu,N., Katagiri,T., Usui,H., Kumanishi,T. and Takahashi,Y.
  TITLE     Structure and expression of human and rat D2 dopamine receptor
            genes
  JOURNAL   Neurochem Int 21 (1), 91-98 (1992)
   PUBMED   1363862
  REMARK    Erratum:[Neurochem Int 1992 Oct;21(3):465]
REFERENCE   10 (residues 1 to 443)
  AUTHORS   Dearry,A., Falardeau,P., Shores,C. and Caron,M.G.
  TITLE     D2 dopamine receptors in the human retina: cloning of cDNA and
            localization of mRNA
  JOURNAL   Cell Mol Neurobiol 11 (5), 437-453 (1991)
   PUBMED   1835903
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002840.3, DA693976.1,
            BF437994.1, X51362.1 and BC021195.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the D2 subtype of the dopamine receptor.
            This G-protein coupled receptor inhibits adenylyl cyclase activity.
            A missense mutation in this gene causes myoclonus dystonia; other
            mutations have been associated with schizophrenia. Alternative
            splicing of this gene results in two transcript variants encoding
            different isoforms. A third variant has been described, but it has
            not been determined whether this form is normal or due to aberrant
            splicing. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (long).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.202143.1, X51362.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2146411
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000362072.8/ ENSP00000354859.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.2"
     Protein         1..443
                     /product="D(2) dopamine receptor isoform long"
                     /note="d(2) dopamine receptor; seven transmembrane helix
                     receptor; dopamine D2 receptor"
                     /calculated_mol_wt=50489
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14416.2)"
     Site            17
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14416.2)"
     Site            23
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14416.2)"
     Region          35..437
                     /region_name="7tmA_D2_dopamine_R"
                     /note="D2 subtype of the D2-like family of dopamine
                     receptors, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15309"
                     /db_xref="CDD:320435"
     Region          36..62
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320435"
     Site            38..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14416.2)"
     Region          69..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320435"
     Site            71..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14416.2)"
     Region          107..137
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320435"
     Site            109..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14416.2)"
     Site            order(110,114..115,118,190,193..194,389..390,393,408,412,
                     416)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320435"
     Site            152..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14416.2)"
     Region          152..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320435"
     Region          186..211
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320435"
     Site            189..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14416.2)"
     Site            194
                     /site_type="other"
                     /note="Important for receptor activation.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P14416.2)"
     Site            197
                     /site_type="other"
                     /note="Important for receptor activation.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P14416.2)"
     Region          211..373
                     /region_name="Interaction with PPP1R9B.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P14416.2)"
     Region          281..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14416.2)"
     Region          366..396
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320435"
     Site            374..395
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14416.2)"
     Region          405..430
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320435"
     Site            410..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14416.2)"
     CDS             1..443
                     /gene="DRD2"
                     /gene_synonym="D2DR; D2R"
                     /coded_by="NM_000795.4:355..1686"
                     /note="isoform long is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8361.1"
                     /db_xref="GeneID:1813"
                     /db_xref="HGNC:HGNC:3023"
                     /db_xref="MIM:126450"
ORIGIN      
        1 mdplnlswyd ddlerqnwsr pfngsdgkad rphynyyatl ltlliavivf gnvlvcmavs
       61 rekalqtttn ylivslavad llvatlvmpw vvylevvgew kfsrihcdif vtldvmmcta
      121 silnlcaisi drytavampm lyntrysskr rvtvmisivw vlsftiscpl lfglnnadqn
      181 eciianpafv vyssivsfyv pfivtllvyi kiyivlrrrr krvntkrssr afrahlrapl
      241 kgncthpedm klctvimksn gsfpvnrrrv eaarraqele memlsstspp ertryspipp
      301 shhqltlpdp shhglhstpd spakpekngh akdhpkiaki feiqtmpngk trtslktmsr
      361 rklsqqkekk atqmlaivlg vfiicwlpff ithilnihcd cnippvlysa ftwlgyvnsa
      421 vnpiiyttfn iefrkaflki lhc
//
LOCUS       NP_000185                218 aa            linear   PRI 27-APR-2025
DEFINITION  hypoxanthine-guanine phosphoribosyltransferase [Homo sapiens].
ACCESSION   NP_000185
VERSION     NP_000185.1
DBSOURCE    REFSEQ: accession NM_000194.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Yin,J., Wang,X., Ge,X., Ding,F., Shi,Z., Ge,Z., Huang,G., Zhao,N.,
            Chen,D., Zhang,J., Agnihotri,S., Cao,Y., Ji,J., Lin,F., Wang,Q.,
            Zhou,Q., Wang,X., You,Y., Lu,Z. and Qian,X.
  TITLE     Hypoxanthine phosphoribosyl transferase 1 metabolizes temozolomide
            to activate AMPK for driving chemoresistance of glioblastomas
  JOURNAL   Nat Commun 14 (1), 5913 (2023)
   PUBMED   37737247
  REMARK    GeneRIF: Hypoxanthine phosphoribosyl transferase 1 metabolizes
            temozolomide to activate AMPK for driving chemoresistance of
            glioblastomas.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Akram,Z., Mahjabeen,I., Umair,M., Fahim,M., Kayani,M.A., Fatima,L.,
            Ahmad,M.W., Jahan,S., Afsar,T., Almajwal,A., Alruwaili,N.W.,
            Khawar,I.A. and Razak,S.
  TITLE     Expression variation of OGG1 and HPRT gene and DNA damage in
            arsenic exposed industrial workers
  JOURNAL   PLoS One 17 (9), e0273211 (2022)
   PUBMED   36178927
  REMARK    GeneRIF: Expression variation of OGG1 and HPRT gene and DNA damage
            in arsenic exposed industrial workers.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Pinho,S.A., Costa,C.F., Deus,C.M., Pinho,S.L.C., Miranda-Santos,I.,
            Afonso,G., Bagshaw,O., Stuart,J.A., Oliveira,P.J. and
            Cunha-Oliveira,T.
  TITLE     Mitochondrial and metabolic remodelling in human skin fibroblasts
            in response to glucose availability
  JOURNAL   FEBS J 289 (17), 5198-5217 (2022)
   PUBMED   35213938
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Ueda,S., Hirata,T. and Sakasegawa,S.I.
  TITLE     Hypoxanthine-guanine phosphoribosyltransferase is activated via
            positive cooperativity between guanine and IMP
  JOURNAL   FEBS Lett 596 (8), 1072-1080 (2022)
   PUBMED   35114018
  REMARK    GeneRIF: Hypoxanthine-guanine phosphoribosyltransferase is
            activated via positive cooperativity between guanine and IMP.
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Jinnah,H.A.
  TITLE     HPRT1 Disorders
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301328
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Sculley,D.G., Dawson,P.A., Emmerson,B.T. and Gordon,R.B.
  TITLE     A review of the molecular basis of hypoxanthine-guanine
            phosphoribosyltransferase (HPRT) deficiency
  JOURNAL   Hum Genet 90 (3), 195-207 (1992)
   PUBMED   1487231
  REMARK    Review article
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Sege-Peterson,K., Chambers,J., Page,T., Jones,O.W. and Nyhan,W.L.
  TITLE     Characterization of mutations in phenotypic variants of
            hypoxanthine phosphoribosyltransferase deficiency
  JOURNAL   Hum Mol Genet 1 (6), 427-432 (1992)
   PUBMED   1301916
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Lightfoot,T., Joshi,R., Nuki,G. and Snyder,F.F.
  TITLE     The point mutation of hypoxanthine-guanine
            phosphoribosyltransferase (HPRTEdinburgh) and detection by
            allele-specific polymerase chain reaction
  JOURNAL   Hum Genet 88 (6), 695-696 (1992)
   PUBMED   1551676
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Holden,J.A. and Kelley,W.N.
  TITLE     Human hypoxanthine-guanine phosphoribosyltransferase. Evidence for
            tetrameric structure
  JOURNAL   J Biol Chem 253 (12), 4459-4463 (1978)
   PUBMED   659426
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004383.1, M31642.1 and
            BC000578.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a transferase, which
            catalyzes conversion of hypoxanthine to inosine monophosphate and
            guanine to guanosine monophosphate via transfer of the
            5-phosphoribosyl group from 5-phosphoribosyl 1-pyrophosphate. This
            enzyme plays a central role in the generation of purine nucleotides
            through the purine salvage pathway. Mutations in this gene result
            in Lesch-Nyhan syndrome or gout.[provided by RefSeq, Jun 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.174892.1,
                                           SRR3476690.20350.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298556.8/ ENSP00000298556.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.2-q26.3"
     Protein         1..218
                     /product="hypoxanthine-guanine phosphoribosyltransferase"
                     /EC_number="2.4.2.8"
                     /note="HGPRTase; hypoxanthine-guanine
                     phosphoribosyltransferase 1; testicular tissue protein Li
                     89; hypoxanthine guanine phosphoribosyl transferase"
                     /calculated_mol_wt=24448
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:7107641; propagated from
                     UniProtKB/Swiss-Prot (P00492.2)"
     Region          8..218
                     /region_name="PRTases_typeI"
                     /note="Phosphoribosyl transferase (PRT)-type I domain;
                     cl00309"
                     /db_xref="CDD:444823"
     Site            order(68,70,134..136,138..142,166)
                     /site_type="active"
                     /db_xref="CDD:206754"
     Site            103
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P00493; propagated from
                     UniProtKB/Swiss-Prot (P00492.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P27605; propagated from
                     UniProtKB/Swiss-Prot (P00492.2)"
     CDS             1..218
                     /gene="HPRT1"
                     /gene_synonym="HGPRT; HPRT"
                     /coded_by="NM_000194.3:148..804"
                     /db_xref="CCDS:CCDS14641.1"
                     /db_xref="GeneID:3251"
                     /db_xref="HGNC:HGNC:5157"
                     /db_xref="MIM:308000"
ORIGIN      
        1 matrspgvvi sddepgydld lfcipnhyae dlervfiphg limdrterla rdvmkemggh
       61 hivalcvlkg gykffadlld yikalnrnsd rsipmtvdfi rlksycndqs tgdikviggd
      121 dlstltgknv livediidtg ktmqtllslv rqynpkmvkv asllvkrtpr svgykpdfvg
      181 feipdkfvvg yaldyneyfr dlnhvcvise tgkakyka
//
LOCUS       NP_001356859             679 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 8 [Homo
            sapiens].
ACCESSION   NP_001356859 XP_016884493
VERSION     NP_001356859.1
DBSOURCE    REFSEQ: accession NM_001369930.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 679)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 679)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 679)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 679)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 679)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 679)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 679)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 679)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            On Apr 24, 2019 this sequence version replaced XP_016884493.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.116333.1,
                                           SRR1803615.263526.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..679
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 8"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=77040
     Region          391..430
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..679
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369930.1:115..2154"
                     /note="isoform 8 is encoded by transcript variant 13"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mpalpldqlq ithkdpktgk lrtspalvif detlqkclds ylryvprkfd egvasapevv
       61 dmqkrlhrsv fltflrmsth keskdhfisp safgeilynn flfdipkild lcvlfgkgns
      121 pllqkmigni ftqqpsyysd ldetlptilq vfsnilqhcg lqgdganttp qkleergrlt
      181 psdmpllelk divlylcdtc ttlwafldif placqtfqkh dfcyrllgdl wqrlshsrkk
      241 lmeifhiiln qicllpiles scdniqgfie eflqifssll qekrflrdyd alfpvaedis
      301 llqqassvld etrtayilqa vesawegvdr rkatdakdps vieepngepn gvtvtaeavs
      361 qasshpense eeecmgaaaa vgpamcgvel dslisqvkdl lpdlgegfil acleyyhydp
      421 eqvinnilee rlaptlsqld rnldremkpd ptplltsrhn vfqndefdvf srdsvdlsrv
      481 hkgkstrkee ntrsllndkr avaaqrqrye qysvvveevp lqpgeslpyh svyyedeydd
      541 tydgnqvgan dadsddelis rrpftipqvl rtkvpregqe eddddeedda deeapkpdhf
      601 vqdpavlrek aearrmafla kkgyrhdsst avagsprghg qsrettqerr kkeankatra
      661 nhnrrtmadr krskgmips
//
LOCUS       NP_000199               1382 aa            linear   PRI 27-APR-2025
DEFINITION  insulin receptor isoform Long preproprotein [Homo sapiens].
ACCESSION   NP_000199
VERSION     NP_000199.2
DBSOURCE    REFSEQ: accession NM_000208.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1382)
  AUTHORS   Rasheed,R.A., Rasheed,P.H. and Ali,A.M.
  TITLE     Metabolic and hormonal profiling in polycystic ovarian syndrome:
            insights into INSR gene variations
  JOURNAL   Mol Biol Rep 51 (1), 989 (2024)
   PUBMED   39287700
  REMARK    GeneRIF: Metabolic and hormonal profiling in polycystic ovarian
            syndrome: insights into INSR gene variations.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1382)
  AUTHORS   Ciulei,G., Orasan,O.H., Cozma,A., Negrean,V., Para,I.,
            Ciumarnean,L., Leach,N., Lucaciu,R.L., Hangan,A.C. and
            Procopciuc,L.M.
  TITLE     Role of Vitamin D Receptor (BsmI-VDR) and Insulin Receptor
            (NsiI-A/G) Gene Polymorphisms in Colorectal Adenoma Susceptibility
  JOURNAL   Int J Mol Sci 25 (16), 8965 (2024)
   PUBMED   39201651
  REMARK    GeneRIF: Role of Vitamin D Receptor (BsmI-VDR) and Insulin Receptor
            (NsiI-A/G) Gene Polymorphisms in Colorectal Adenoma Susceptibility.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1382)
  AUTHORS   Schwartz,L., Simoni,A., Yan,P., Salamon,K., Turkoglu,A., Vasquez
            Martinez,G., Zepeda-Orozco,D., Eichler,T., Wang,X. and Spencer,J.D.
  TITLE     Insulin receptor orchestrates kidney antibacterial defenses
  JOURNAL   Proc Natl Acad Sci U S A 121 (29), e2400666121 (2024)
   PUBMED   38976738
  REMARK    GeneRIF: Insulin receptor orchestrates kidney antibacterial
            defenses.
REFERENCE   4  (residues 1 to 1382)
  AUTHORS   Hubbard,S.R.
  TITLE     The insulin receptor: both a prototypical and atypical receptor
            tyrosine kinase
  JOURNAL   Cold Spring Harb Perspect Biol 5 (3), a008946 (2013)
   PUBMED   23457259
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1382)
  AUTHORS   Mesika,A., Klar,A. and Falik Zaccai,T.C.
  TITLE     INSR-Related Severe Insulin Resistance Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29369573
REFERENCE   6  (residues 1 to 1382)
  AUTHORS   Gillis,D.
  TITLE     Nonsyndromic Genetic Hyperinsulinism Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301549
REFERENCE   7  (residues 1 to 1382)
  AUTHORS   Shekels,L.L., Smith,A.J., Van Etten,R.L. and Bernlohr,D.A.
  TITLE     Identification of the adipocyte acid phosphatase as a PAO-sensitive
            tyrosyl phosphatase
  JOURNAL   Protein Sci 1 (6), 710-721 (1992)
   PUBMED   1304913
REFERENCE   8  (residues 1 to 1382)
  AUTHORS   Cama,A., Quon,M.J., de la Luz Sierra,M. and Taylor,S.I.
  TITLE     Substitution of isoleucine for methionine at position 1153 in the
            beta-subunit of the human insulin receptor. A mutation that impairs
            receptor tyrosine kinase activity, receptor endocytosis, and
            insulin action
  JOURNAL   J Biol Chem 267 (12), 8383-8389 (1992)
   PUBMED   1314826
REFERENCE   9  (residues 1 to 1382)
  AUTHORS   Ullrich,A., Bell,J.R., Chen,E.Y., Herrera,R., Petruzzelli,L.M.,
            Dull,T.J., Gray,A., Coussens,L., Liao,Y.C., Tsubokawa,M. et al.
  TITLE     Human insulin receptor and its relationship to the tyrosine kinase
            family of oncogenes
  JOURNAL   Nature 313 (6005), 756-761 (1985)
   PUBMED   2983222
REFERENCE   10 (residues 1 to 1382)
  AUTHORS   Pedersen,O. and Beck-Nielsen,H.
  TITLE     A study of insulin receptors in human mononuclear leucocytes
  JOURNAL   Acta Endocrinol (Copenh) 83 (3), 556-564 (1976)
   PUBMED   185872
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125387.2, HY015976.1,
            BC117172.1, M10051.1, X02160.1, AC010606.7, AK025527.1 and
            BU684722.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 14, 2006 this sequence version replaced NP_000199.1.
            
            Summary: This gene encodes a member of the receptor tyrosine kinase
            family of proteins. The encoded preproprotein is proteolytically
            processed to generate alpha and beta subunits that form a
            heterotetrameric receptor. Binding of insulin or other ligands to
            this receptor activates the insulin signaling pathway, which
            regulates glucose uptake and release, as well as the synthesis and
            storage of carbohydrates, lipids and protein. Mutations in this
            gene underlie the inherited severe insulin resistance syndromes
            including type A insulin resistance syndrome, Donohue syndrome and
            Rabson-Mendenhall syndrome. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (Long).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M10051.1, SRR14038194.2414418.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302850.10/ ENSP00000303830.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1382
                     /product="insulin receptor isoform Long preproprotein"
                     /EC_number="2.7.10.1"
                     /note="IR"
                     /calculated_mol_wt=153932
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2420
     mat_peptide     28..758
                     /product="Insulin receptor subunit alpha.
                     /id=PRO_0000016687"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
                     /calculated_mol_wt=83643
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:23302862, ECO:0000269|PubMed:2983222;
                     propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Region          52..164
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:23302862; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            66
                     /site_type="other"
                     /note="Insulin-binding. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (P06213.4)"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:23302862; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          179..337
                     /region_name="Furin-like"
                     /note="Furin-like cysteine rich region; pfam00757"
                     /db_xref="CDD:395614"
     Site            242
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23302862;
                     propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            282
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:23302862; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          359..472
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            424
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            445
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            541
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:1472036,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          <582..>658
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          622..>665
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            633
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            651
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          686..708
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            698
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          733..741
                     /region_name="Insulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Region          746..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     mat_peptide     763..1382
                     /product="Insulin receptor subunit beta.
                     /id=PRO_0000016689"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
                     /calculated_mol_wt=69711
     Site            769
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:2983222; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            782
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          867..944
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            920
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            order(933..934,936..937)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            933
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          940..987
                     /region_name="Insulin_TMD"
                     /note="Insulin receptor trans-membrane segment; pfam17870"
                     /db_xref="CDD:465543"
     Site            957..979
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            992
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          999
                     /region_name="Important for interaction with IRS1, SHC1
                     and STAT5B. /evidence=ECO:0000269|PubMed:9428692"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            999
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:3166375; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            1011
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          1016..1303
                     /region_name="PTKc_InsR"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Insulin Receptor; cd05061"
                     /db_xref="CDD:133192"
     Site            order(1032..1033,1037,1055,1057,1104,1106,1110,1159,
                     1163..1164,1177,1192,1194..1196,1198..1199,1208..1209,
                     1211,1242)
                     /site_type="active"
                     /db_xref="CDD:133192"
     Site            order(1032..1033,1037,1055,1057,1104,1106,1110,1163..1164,
                     1166,1177)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133192"
     Site            order(1046..1049,1127,1129,1169..1170,1295,1300)
                     /site_type="other"
                     /note="PTP1B noncatalytic binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133192"
     Site            order(1163,1192,1194..1196,1198..1199,1208..1209,1211,
                     1242)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133192"
     Site            1176..1201
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133192"
     Site            order(1183,1185..1186,1188..1189)
                     /site_type="other"
                     /note="APS (SH2 domain) interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133192"
     Site            1185
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:14690593,
                     ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887,
                     ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165,
                     ECO:0000269|PubMed:26584640, ECO:0000269|PubMed:3166375,
                     ECO:0000269|PubMed:9312016; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            1189
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:14690593,
                     ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887,
                     ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165,
                     ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016;
                     propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            1190
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:14690593,
                     ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887,
                     ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165,
                     ECO:0000269|PubMed:26584640, ECO:0000269|PubMed:3166375,
                     ECO:0000269|PubMed:9312016; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            1355
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:3166375; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          1360..1382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Region          1361..1364
                     /region_name="PIK3R1-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            1361
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:3166375; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     CDS             1..1382
                     /gene="INSR"
                     /gene_synonym="CD220; HHF5"
                     /coded_by="NM_000208.4:524..4672"
                     /note="isoform Long preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12176.1"
                     /db_xref="GeneID:3643"
                     /db_xref="HGNC:HGNC:6091"
                     /db_xref="MIM:147670"
ORIGIN      
        1 matggrrgaa aapllvavaa lllgaaghly pgevcpgmdi rnnltrlhel encsvieghl
       61 qillmfktrp edfrdlsfpk limitdylll frvygleslk dlfpnltvir gsrlffnyal
      121 vifemvhlke lglynlmnit rgsvrieknn elcylatidw srildsvedn yivlnkddne
      181 ecgdicpgta kgktncpatv ingqfvercw thshcqkvcp tickshgcta eglcchsecl
      241 gncsqpddpt kcvacrnfyl dgrcvetcpp pyyhfqdwrc vnfsfcqdlh hkcknsrrqg
      301 chqyvihnnk cipecpsgyt mnssnllctp clgpcpkvch llegektids vtsaqelrgc
      361 tvingsliin irggnnlaae leanlgliee isgylkirrs yalvslsffr klrlirgetl
      421 eignysfyal dnqnlrqlwd wskhnltitq gklffhynpk lclseihkme evsgtkgrqe
      481 rndialktng dqascenell kfsyirtsfd killrwepyw ppdfrdllgf mlfykeapyq
      541 nvtefdgqda cgsnswtvvd idpplrsndp ksqnhpgwlm rglkpwtqya ifvktlvtfs
      601 derrtygaks diiyvqtdat npsvpldpis vsnsssqiil kwkppsdpng nithylvfwe
      661 rqaedselfe ldyclkglkl psrtwsppfe sedsqkhnqs eyedsagecc scpktdsqil
      721 keleessfrk tfedylhnvv fvprktssgt gaedprpsrk rrslgdvgnv tvavptvaaf
      781 pntsstsvpt speehrpfek vvnkeslvis glrhftgyri elqacnqdtp eercsvaayv
      841 sartmpeaka ddivgpvthe ifennvvhlm wqepkepngl ivlyevsyrr ygdeelhlcv
      901 srkhfalerg crlrglspgn ysvriratsl agngswtept yfyvtdyldv psniakiiig
      961 plifvflfsv vigsiylflr krqpdgplgp lyassnpeyl sasdvfpcsv yvpdewevsr
     1021 ekitllrelg qgsfgmvyeg nardiikgea etrvavktvn esaslrerie flneasvmkg
     1081 ftchhvvrll gvvskgqptl vvmelmahgd lksylrslrp eaennpgrpp ptlqemiqma
     1141 aeiadgmayl nakkfvhrdl aarncmvahd ftvkigdfgm trdiyetdyy rkggkgllpv
     1201 rwmapeslkd gvfttssdmw sfgvvlweit slaeqpyqgl sneqvlkfvm dggyldqpdn
     1261 cpervtdlmr mcwqfnpkmr ptfleivnll kddlhpsfpe vsffhseenk apeseeleme
     1321 fedmenvpld rsshcqreea ggrdggsslg fkrsyeehip ythmnggkkn griltlprsn
     1381 ps
//
LOCUS       NP_001350246             179 aa            linear   ROD 27-APR-2025
DEFINITION  iron-sulfur cluster assembly enzyme ISCU isoform 2 [Mus musculus].
ACCESSION   NP_001350246
VERSION     NP_001350246.1
DBSOURCE    REFSEQ: accession NM_001363317.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Roy,A.R., Ahmed,A., DiStefano,P.V., Chi,L., Khyzha,N., Galjart,N.,
            Wilson,M.D., Fish,J.E. and Delgado-Olguin,P.
  TITLE     The transcriptional regulator CCCTC-binding factor limits oxidative
            stress in endothelial cells
  JOURNAL   J Biol Chem 293 (22), 8449-8461 (2018)
   PUBMED   29610276
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Boniecki,M.T., Freibert,S.A., Muhlenhoff,U., Lill,R. and Cygler,M.
  TITLE     Structure and functional dynamics of the mitochondrial Fe/S cluster
            synthesis complex
  JOURNAL   Nat Commun 8 (1), 1287 (2017)
   PUBMED   29097656
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Gakh,O., Ranatunga,W., Smith,D.Y. 4th, Ahlgren,E.C.,
            Al-Karadaghi,S., Thompson,J.R. and Isaya,G.
  TITLE     Architecture of the Human Mitochondrial Iron-Sulfur Cluster
            Assembly Machinery
  JOURNAL   J Biol Chem 291 (40), 21296-21321 (2016)
   PUBMED   27519411
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Funauchi,Y., Tanikawa,C., Yi Lo,P.H., Mori,J., Daigo,Y., Takano,A.,
            Miyagi,Y., Okawa,A., Nakamura,Y. and Matsuda,K.
  TITLE     Regulation of iron homeostasis by the p53-ISCU pathway
  JOURNAL   Sci Rep 5, 16497 (2015)
   PUBMED   26560363
  REMARK    GeneRIF: ISCU expression was decreased in the majority of human
            liver cancer tissues, and its reduced expression was significantly
            associated with p53 mutation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Parent,A., Elduque,X., Cornu,D., Belot,L., Le Caer,J.P.,
            Grandas,A., Toledano,M.B. and D'Autreaux,B.
  TITLE     Mammalian frataxin directly enhances sulfur transfer of NFS1
            persulfide to both ISCU and free thiols
  JOURNAL   Nat Commun 6, 5686 (2015)
   PUBMED   25597503
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Nordin,A., Larsson,E., Thornell,L.E. and Holmberg,M.
  TITLE     Tissue-specific splicing of ISCU results in a skeletal muscle
            phenotype in myopathy with lactic acidosis, while complete loss of
            ISCU results in early embryonic death in mice
  JOURNAL   Hum Genet 129 (4), 371-378 (2011)
   PUBMED   21165651
  REMARK    GeneRIF: Data show that complete loss of ISCU results in early
            embryonic death and confirm a fundamental role for ISCU in mammals.
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Chan,S.Y., Zhang,Y.Y., Hemann,C., Mahoney,C.E., Zweier,J.L. and
            Loscalzo,J.
  TITLE     MicroRNA-210 controls mitochondrial metabolism during hypoxia by
            repressing the iron-sulfur cluster assembly proteins ISCU1/2
  JOURNAL   Cell Metab 10 (4), 273-284 (2009)
   PUBMED   19808020
  REMARK    GeneRIF: Results identify the iron-sulfur cluster assembly proteins
            (ISCU1/2) as direct targets for repression by the hypoxia-induced
            microRNA-210.
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Martelli,A., Wattenhofer-Donze,M., Schmucker,S., Bouvet,S.,
            Reutenauer,L. and Puccio,H.
  TITLE     Frataxin is essential for extramitochondrial Fe-S cluster proteins
            in mammalian tissues
  JOURNAL   Hum Mol Genet 16 (22), 2651-2658 (2007)
   PUBMED   17597094
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Canal,F., Fosset,C., Chauveau,M.J., Drapier,J.C. and Bouton,C.
  TITLE     Regulation of the cysteine desulfurase Nfs1 and the scaffold
            protein IscU in macrophages stimulated with interferon-gamma and
            lipopolysaccharide
  JOURNAL   Arch Biochem Biophys 465 (1), 282-292 (2007)
   PUBMED   17603005
  REMARK    GeneRIF: While IFN-gamma alone induced Nfs1 protein instability,
            LPS triggered a delayed decline of Nfs1, rather involving
            transcriptional events or mRNA instability.
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Rubtsov,A., Strauch,P., Digiacomo,A., Hu,J., Pelanda,R. and
            Torres,R.M.
  TITLE     Lsc regulates marginal-zone B cell migration and adhesion and is
            required for the IgM T-dependent antibody response
  JOURNAL   Immunity 23 (5), 527-538 (2005)
   PUBMED   16286020
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132939.23, AI851358.1 and AK083247.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AI851358.1, ERR3363660.1238110.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 55.55 cM"
     Protein         1..179
                     /product="iron-sulfur cluster assembly enzyme ISCU isoform
                     2"
                     /note="iron-sulfur cluster assembly enzyme ISCU,
                     mitochondrial; nifU-like N-terminal domain-containing
                     protein; IscU iron-sulfur cluster scaffold homolog"
                     /calculated_mol_wt=19255
     Region          50..170
                     /region_name="iscU"
                     /note="FeS cluster assembly scaffold IscU; TIGR01999"
                     /db_xref="CDD:188192"
     Site            order(81,107,150)
                     /site_type="active"
                     /db_xref="CDD:143480"
     CDS             1..179
                     /gene="Iscu"
                     /gene_synonym="2310020H20Rik; ISCU2; Nifu; Nifun"
                     /coded_by="NM_001363317.1:147..686"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:66383"
                     /db_xref="MGI:MGI:1913633"
ORIGIN      
        1 mggrggarti egtcrrcadh qhrgaprppl prrgrhsecp kadspegrvr vvdhyenprn
       61 vgsldktskn vgtglvgapa cgdvmklqiq vdekgkivda rfktfgcgsa iassslatew
      121 vkgktveeal tikntdiake lclppvklhc smlaedaika aladyklkqe skkeepekq
//
LOCUS       NP_000014                387 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-sarcoglycan isoform 1 precursor [Homo sapiens].
ACCESSION   NP_000014
VERSION     NP_000014.1
DBSOURCE    REFSEQ: accession NM_000023.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Faheem,A., Masud,R., Nasir,R., Awan,Z.K., Nasir,H.A., Khan,Z.K.,
            Fayyaz,H. and Raza,S.I.
  TITLE     Exome sequencing revealed variants in SGCA and SIL1 genes
            underlying limb girdle muscular dystrophy and Marinesco-Sjogren
            syndrome patients
  JOURNAL   Mol Biol Rep 51 (1), 853 (2024)
   PUBMED   39060875
  REMARK    GeneRIF: Exome sequencing revealed variants in SGCA and SIL1 genes
            underlying limb girdle muscular dystrophy and Marinesco-Sjogren
            syndrome patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Escobar,H., Krause,A., Keiper,S., Kieshauer,J., Muthel,S., de
            Paredes,M.G., Metzler,E., Kuhn,R., Heyd,F. and Spuler,S.
  TITLE     Base editing repairs an SGCA mutation in human primary muscle stem
            cells
  JOURNAL   JCI Insight 6 (10), 145994 (2021)
   PUBMED   33848270
  REMARK    GeneRIF: Base editing repairs an SGCA mutation in human primary
            muscle stem cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Kawai,H., Akaike,M., Endo,T., Adachi,K., Inui,T., Mitsui,T.,
            Kashiwagi,S., Fujiwara,T., Okuno,S., Shin,S. et al.
  TITLE     Adhalin gene mutations in patients with autosomal recessive
            childhood onset muscular dystrophy with adhalin deficiency
  JOURNAL   J Clin Invest 96 (3), 1202-1207 (1995)
   PUBMED   7657792
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Piccolo,F., Roberds,S.L., Jeanpierre,M., Leturcq,F., Azibi,K.,
            Beldjord,C., Carrie,A., Recan,D., Chaouch,M., Reghis,A. et al.
  TITLE     Primary adhalinopathy: a common cause of autosomal recessive
            muscular dystrophy of variable severity
  JOURNAL   Nat Genet 10 (2), 243-245 (1995)
   PUBMED   7663524
  REMARK    Erratum:[Nat Genet 1995 Sep 11(1):104]
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Yang,B., Jung,D., Motto,D., Meyer,J., Koretzky,G. and Campbell,K.P.
  TITLE     SH3 domain-mediated interaction of dystroglycan and Grb2
  JOURNAL   J Biol Chem 270 (20), 11711-11714 (1995)
   PUBMED   7744812
REFERENCE   8  (residues 1 to 387)
  AUTHORS   McNally,E.M., Yoshida,M., Mizuno,Y., Ozawa,E. and Kunkel,L.M.
  TITLE     Human adhalin is alternatively spliced and the gene is located on
            chromosome 17q21
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9690-9694 (1994)
   PUBMED   7937874
REFERENCE   9  (residues 1 to 387)
  AUTHORS   Roberds,S.L., Leturcq,F., Allamand,V., Piccolo,F., Jeanpierre,M.,
            Anderson,R.D., Lim,L.E., Lee,J.C., Tome,F.M., Romero,N.B. et al.
  TITLE     Missense mutations in the adhalin gene linked to autosomal
            recessive muscular dystrophy
  JOURNAL   Cell 78 (4), 625-633 (1994)
   PUBMED   8069911
REFERENCE   10 (residues 1 to 387)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015909.14.
            
            Summary: This gene encodes a component of the
            dystrophin-glycoprotein complex (DGC), which is critical to the
            stability of muscle fiber membranes and to the linking of the actin
            cytoskeleton to the extracellular matrix. Its expression is thought
            to be restricted to striated muscle. Mutations in this gene result
            in type 2D autosomal recessive limb-girdle muscular dystrophy.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.985073.1, L34355.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262018.8/ ENSP00000262018.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..387
                     /product="alpha-sarcoglycan isoform 1 precursor"
                     /note="alpha-sarcoglycan; 50kD DAG; alpha-SG;
                     dystroglycan-2; 50 kDa dystrophin-associated glycoprotein;
                     sarcoglycan, alpha (50kDa dystrophin-associated
                     glycoprotein); limb girdle muscular dystrophy 2D"
                     /calculated_mol_wt=40432
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2461
     Region          21..347
                     /region_name="Sarcoglycan_2"
                     /note="Sarcoglycan alpha/epsilon; pfam05510"
                     /db_xref="CDD:461668"
     mat_peptide     24..387
                     /product="Alpha-sarcoglycan. /id=PRO_0000031673"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16586.1)"
                     /calculated_mol_wt=40432
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16586.1)"
     Site            246
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16586.1)"
     Site            291..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16586.1)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P82350; propagated from
                     UniProtKB/Swiss-Prot (Q16586.1)"
     CDS             1..387
                     /gene="SGCA"
                     /gene_synonym="50DAG; adhalin; ADL; DAG2; DMDA2; LGMD2D;
                     LGMDR3; SCARMD1"
                     /coded_by="NM_000023.4:37..1200"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS32679.1"
                     /db_xref="GeneID:6442"
                     /db_xref="HGNC:HGNC:10805"
                     /db_xref="MIM:600119"
ORIGIN      
        1 maetlfwtpl lvvllaglgd teaqqttlhp lvgrvfvhtl dhetflslpe hvavppavhi
       61 tyhahlqghp dlprwlrytq rsphhpgfly gsatpedrgl qvievtaynr dsfdttrqrl
      121 vleigdpegp llpyqaeflv rshdaeevlp stpasrflsa lgglwepgel qllnvtsald
      181 rggrvplpie grkegvyikv gsaspfstcl kmvaspdsha rcaqgqppll scydtlaphf
      241 rvdwcnvtlv dksvpepade vptpgdgile hdpffcppte apdrdflvda lvtllvpllv
      301 allltlllay vmccrregrl krdlatsdiq mvhhctihgn teelrqmaas revprplstl
      361 pmfnvhtger lpprvdsaqv plildqh
//
LOCUS       NP_612417                213 aa            linear   PRI 27-APR-2025
DEFINITION  general transcription factor 3C polypeptide 6 [Homo sapiens].
ACCESSION   NP_612417
VERSION     NP_612417.1
DBSOURCE    REFSEQ: accession NM_138408.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Dumay-Odelot,H., Marck,C., Durrieu-Gaillard,S., Lefebvre,O.,
            Jourdain,S., Prochazkova,M., Pflieger,A. and Teichmann,M.
  TITLE     Identification, molecular cloning, and characterization of the
            sixth subunit of human transcription factor TFIIIC
  JOURNAL   J Biol Chem 282 (23), 17179-17189 (2007)
   PUBMED   17409385
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF361496.1.
            
            Summary: RNA polymerases are unable to initiate RNA synthesis in
            the absence of additional proteins called general transcription
            factors (GTFs). GTFs assemble in a complex on the DNA promoter and
            recruit the RNA polymerase. GTF3C family proteins (e.g., GTF3C1,
            MIM 603246) are essential for RNA polymerase III to make a number
            of small nuclear and cytoplasmic RNAs, including 5S RNA (MIM
            180420), tRNA, and adenovirus-associated (VA) RNA of both cellular
            and viral origin.[supplied by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF361496.1, SRR1163657.272789.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329970.8/ ENSP00000357863.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..213
                     /product="general transcription factor 3C polypeptide 6"
                     /note="transcription factor IIIC 35kDa; TFIIIC 35 kDa
                     subunit; transcription factor IIIC subunit 6;
                     transcription factor IIIC 35 kDa subunit; general
                     transcription factor IIIC, polypeptide 6, alpha 35kDa"
                     /calculated_mol_wt=23918
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969F1.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q969F1.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q969F1.1)"
     Region          28..111
                     /region_name="TFIIIC_sub6"
                     /note="TFIIIC subunit triple barrel domain; pfam10419"
                     /db_xref="CDD:463085"
     Region          191..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969F1.1)"
     CDS             1..213
                     /gene="GTF3C6"
                     /gene_synonym="bA397G5.3; C6orf51; TFIIIC35"
                     /coded_by="NM_138408.4:65..706"
                     /db_xref="CCDS:CCDS5087.1"
                     /db_xref="GeneID:112495"
                     /db_xref="HGNC:HGNC:20872"
                     /db_xref="MIM:611784"
ORIGIN      
        1 maaaadersp edgedeeeee qlvlvelsgi idsdflskce nkckvlgidt erpilqvdsc
       61 vfageyedtl gtcvifeenv ehadtegnnk tvlkykchtm kklsmtrtll tekkegeeni
      121 ggvewlqikd ndfsyrpnmi cnflhenede evvasapdks leleeeeiqm ndssnlsceq
      181 ekpmhleied sgplidipse tegsvfmetq mlp
//
LOCUS       NP_004937               1830 aa            linear   PRI 27-APR-2025
DEFINITION  dedicator of cytokinesis protein 2 [Homo sapiens].
ACCESSION   NP_004937
VERSION     NP_004937.1
DBSOURCE    REFSEQ: accession NM_004946.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1830)
  AUTHORS   Qian,G., Adeyanju,O., Cai,D., Tucker,T.A., Idell,S., Chen,S.Y. and
            Guo,X.
  TITLE     DOCK2 Promotes Atherosclerosis by Mediating the Endothelial Cell
            Inflammatory Response
  JOURNAL   Am J Pathol 194 (4), 599-611 (2024)
   PUBMED   37838011
  REMARK    GeneRIF: DOCK2 Promotes Atherosclerosis by Mediating the
            Endothelial Cell Inflammatory Response.
REFERENCE   2  (residues 1 to 1830)
  AUTHORS   Shi,N., Zhang,J. and Chen,S.Y.
  TITLE     DOCK2 Promotes Asthma Development by Eliciting Airway
            Epithelial-Mesenchymal Transition
  JOURNAL   Am J Respir Cell Mol Biol 69 (3), 310-320 (2023)
   PUBMED   36883952
  REMARK    GeneRIF: DOCK2 Promotes Asthma Development by Eliciting Airway
            Epithelial-Mesenchymal Transition.
REFERENCE   3  (residues 1 to 1830)
  AUTHORS   Li,W., Sun,Y., Yu,L., Chen,R., Gan,R., Qiu,L., Sun,G., Chen,J.,
            Zhou,L., Ding,Y., Du,H., Shu,Z., Zhang,Z., Tang,X., Chen,Y.,
            Zhao,X., Zhao,Q. and An,Y.
  TITLE     Multiple Immune Defects in Two Patients with Novel DOCK2 Mutations
            Result in Recurrent Multiple Infection Including Live Attenuated
            Virus Vaccine
  JOURNAL   J Clin Immunol 43 (6), 1193-1207 (2023)
   PUBMED   36947335
  REMARK    GeneRIF: Multiple Immune Defects in Two Patients with Novel DOCK2
            Mutations Result in Recurrent Multiple Infection Including Live
            Attenuated Virus Vaccine.
REFERENCE   4  (residues 1 to 1830)
  AUTHORS   Guo,X., Cai,D., Dong,K., Li,C., Xu,Z. and Chen,S.Y.
  TITLE     DOCK2 Deficiency Attenuates Abdominal Aortic Aneurysm
            Formation-Brief Report
  JOURNAL   Arterioscler Thromb Vasc Biol 43 (6), e210-e217 (2023)
   PUBMED   37021575
  REMARK    GeneRIF: DOCK2 Deficiency Attenuates Abdominal Aortic Aneurysm
            Formation-Brief Report.
REFERENCE   5  (residues 1 to 1830)
  AUTHORS   Scharler,C., Poupardin,R., Ebner-Peking,P., Wolf,M., Schreck,C.,
            Brachtl,G., Cronemberger Andrade,A., Krisch,L., Daheron,L.,
            Schallmoser,K., Jurchott,K., Kuchler,J., Stachelscheid,H.,
            Volk,H.D., Oostendorp,R.A.J. and Strunk,D.
  TITLE     Extra-hematopoietic immunomodulatory role of the guanine-exchange
            factor DOCK2
  JOURNAL   Commun Biol 5 (1), 1246 (2022)
   PUBMED   36380073
  REMARK    GeneRIF: Extra-hematopoietic immunomodulatory role of the
            guanine-exchange factor DOCK2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1830)
  AUTHORS   Nishihara,H., Maeda,M., Tsuda,M., Makino,Y., Sawa,H., Nagashima,K.
            and Tanaka,S.
  TITLE     DOCK2 mediates T cell receptor-induced activation of Rac2 and IL-2
            transcription
  JOURNAL   Biochem Biophys Res Commun 296 (3), 716-720 (2002)
   PUBMED   12176041
  REMARK    GeneRIF: DOCK2 mediates T cell receptor-induced activation of Rac2
            and IL-2 transcription in jurkat cells
REFERENCE   7  (residues 1 to 1830)
  AUTHORS   Reif,K. and Cyster,J.
  TITLE     The CDM protein DOCK2 in lymphocyte migration
  JOURNAL   Trends Cell Biol 12 (8), 368-373 (2002)
   PUBMED   12191913
  REMARK    Review article
REFERENCE   8  (residues 1 to 1830)
  AUTHORS   Brugnera,E., Haney,L., Grimsley,C., Lu,M., Walk,S.F.,
            Tosello-Trampont,A.C., Macara,I.G., Madhani,H., Fink,G.R. and
            Ravichandran,K.S.
  TITLE     Unconventional Rac-GEF activity is mediated through the
            Dock180-ELMO complex
  JOURNAL   Nat Cell Biol 4 (8), 574-582 (2002)
   PUBMED   12134158
REFERENCE   9  (residues 1 to 1830)
  AUTHORS   Fukui,Y., Hashimoto,O., Sanui,T., Oono,T., Koga,H., Abe,M.,
            Inayoshi,A., Noda,M., Oike,M., Shirai,T. and Sasazuki,T.
  TITLE     Haematopoietic cell-specific CDM family protein DOCK2 is essential
            for lymphocyte migration
  JOURNAL   Nature 412 (6849), 826-831 (2001)
   PUBMED   11518968
REFERENCE   10 (residues 1 to 1830)
  AUTHORS   Nishihara,H., Kobayashi,S., Hashimoto,Y., Ohba,F., Mochizuki,N.,
            Kurata,T., Nagashima,K. and Matsuda,M.
  TITLE     Non-adherent cell-specific expression of DOCK2, a member of the
            human CDM-family proteins
  JOURNAL   Biochim Biophys Acta 1452 (2), 179-187 (1999)
   PUBMED   10559471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB145764.1, BC104900.1,
            BC113457.1, BC084556.1 and AK128449.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the CDM
            protein family. It is specifically expressed in hematopoietic cells
            and is predominantly expressed in peripheral blood leukocytes. The
            protein is involved in remodeling of the actin cytoskeleton
            required for lymphocyte migration in response to chemokine
            signaling. It activates members of the Rho family of GTPases, for
            example RAC1 and RAC2, by acting as a guanine nucleotide exchange
            factor (GEF) to exchange bound GDP for free GTP. Mutations in this
            gene result in immunodeficiency 40 (IMD40), a combined form of
            immunodeficiency that affects T cell number and function, also with
            variable defects in B cell and NK cell function. [provided by
            RefSeq, May 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D86964.1, BC104900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000520908.7/ ENSP00000429283.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1830
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.1"
     Protein         1..1830
                     /product="dedicator of cytokinesis protein 2"
                     /note="dedicator of cyto-kinesis 2"
                     /calculated_mol_wt=211818
     Region          12..67
                     /region_name="SH3_DOCK2_A"
                     /note="Src Homology 3 domain of Class A Dedicator of
                     Cytokinesis protein 2; cd12050"
                     /db_xref="CDD:212983"
     Site            order(14..18,25,30..32,34,38..39,43..44,46,54,56,58,60,
                     62..63,65,67)
                     /site_type="other"
                     /note="ELMO interaction site [polypeptide binding]"
                     /db_xref="CDD:212983"
     Site            order(17,19,22,26,43..44,60,62..63)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212983"
     Region          77..414
                     /region_name="DOCK_N"
                     /note="DOCK N-terminus; pfam16172"
                     /db_xref="CDD:465040"
     Site            304
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92608.2)"
     Region          422..617
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92608.2)"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92608.2)"
     Site            738
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92608.2)"
     Region          939..1476
                     /region_name="Interaction with CRKL.
                     /evidence=ECO:0000269|PubMed:12393632"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92608.2)"
     Region          1200..1620
                     /region_name="DHR2_DOCK2"
                     /note="Dock Homology Region 2, a GEF domain, of Class A
                     Dedicator of Cytokinesis 2; cd11706"
                     /db_xref="CDD:212579"
     Site            order(1302,1309..1311,1313,1315..1316,1318..1319,
                     1322..1323,1325..1326,1329..1330,1333,1420,1424..1427,
                     1430)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:212579"
     Site            order(1368,1370..1373,1389..1391,1408..1410,1444..1447,
                     1458..1459,1462,1501,1505,1525..1526,1528..1529,
                     1533..1534,1537..1543,1546,1576,1592,1594..1595,1598,1601)
                     /site_type="other"
                     /note="Rac binding site [polypeptide binding]"
                     /db_xref="CDD:212579"
     Site            1537..1542
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212579"
     Region          1651..1704
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92608.2)"
     Site            1685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92608.2)"
     Site            1706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92608.2)"
     Site            1731
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92608.2)"
     Site            1784
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92608.2)"
     CDS             1..1830
                     /gene="DOCK2"
                     /gene_synonym="IMD40"
                     /coded_by="NM_004946.3:53..5545"
                     /db_xref="CCDS:CCDS4371.1"
                     /db_xref="GeneID:1794"
                     /db_xref="HGNC:HGNC:2988"
                     /db_xref="MIM:603122"
ORIGIN      
        1 mapwrkadke rhgvaiynfq gsgapqlslq igdvvriqet cgdwyrgyli khkmlqgifp
       61 ksfihikevt vekrrnteni ipaeiplaqe vtttlwewgs iwkqlyvask kerflqvqsm
      121 mydlmewrsq llsgtlpkde lkelkqkvts kidygnkile ldlivrdedg nildpdntsv
      181 islfhaheea tdkiterike emskdqpdya mysrissspt hslyvfvrnf vcrigedael
      241 fmslydpnkq tvisenylvr wgsrgfpkei emlnnlkvvf tdlgnkdlnr dkiylicqiv
      301 rvgkmdlkdt gakkctqglr rpfgvavmdi tdiikgkaes deekqhfipf hpvtaendfl
      361 hsllgkvias kgdsggqglw vtmkmlvgdi iqirkdyphl vdrttvvark lgfpeiimpg
      421 dvrndiyitl lqgdfdkynk ttqrnvevim cvcaedgktl pnaicvgagd kpmneyrsvv
      481 yyqvkqprwm etvkvavpie dmqrihlrfm frhrsslesk dkgeknfams yvklmkedgt
      541 tlhdgfhdlv vlkgdskkme dasayltlps yrhhvenkga tlsrssssvg glsvssrdvf
      601 sistlvcstk ltqnvgllgl lkwrmkpqll qenleklkiv dgeevvkflq dtldalfnim
      661 mehsqsdeyd ilvfdaliyi igliadrkfq hfntvleayi qqhfsatlay kklmtvlkty
      721 ldtssrgeqc epilrtlkal eyvfkfivrs rtlfsqlyeg keqmefeesm rrlfesinnl
      781 mksqykttil lqvaalkyip svlhdvemvf dakllsqlly efytcippvk lqkqkvqsmn
      841 eivqsnlfkk qecrdillpv itkelkelle qkddmqhqvl erkycvelln silevlsyqd
      901 aaftyhhiqe imvqllrtvn rtvitmgrdh ilishfvacm tailnqmgdq hysfyietfq
      961 tsselvdflm etfimfkdli gknvypgdwm amsmvqnrvf lrainkfaet mnqkflehtn
     1021 fefqlwnnyf hlavafitqd slqleqfsha kynkilnkyg dmrrligfsi rdmwyklgqn
     1081 kicfipgmvg pilemtlipe aelrkatipi ffdmmlceyq rsgdfkkfen eiilkldhev
     1141 eggrgdeqym qllesilmec aaehptiaks venfvnlvkg lleklldyrg vmtdeskdnr
     1201 msctvnllnf ykdnnreemy irylyklrdl hldcdnytea aytlllhtwl lkwsdeqcas
     1261 qvmqtgqqhp qthrqlketl yetiigyfdk gkmweeaisl ckelaeqyem eifdyellsq
     1321 nliqqakfye simkilrpkp dyfavgyygq gfpsflrnkv fiyrgkeyer redfqmqlmt
     1381 qfpnaekmnt tsapgddvkn apgqyiqcft vqpvldehpr fknkpvpdqi infyksnyvq
     1441 rfhysrpvrr gtvdpenefa smwiertsfv tayklpgilr wfevvhmsqt tisplenaie
     1501 tmstanekil mminqyqsde tlpinplsml lngivdpavm ggfakyekaf fteeyvrdhp
     1561 edqdklthlk dliawqipfl gagikihekr vsdnlrpfhd rmeecfknlk mkvekeygvr
     1621 empdfddrrv grprsmlrsy rqmsiislas mnsdcstpsk ptsesfdlel aspktprveq
     1681 eepispgstl pevklrrskk rtkrssvvfa dekaaaesdl krlsrkhefm sdtnlsehaa
     1741 iplkasvlsq msfasqsmpt ipalalsvag ipgldeants prlsqtflql sdgdkktltr
     1801 kkvnqffktm lasksaeegk qipdslstdl
//
LOCUS       NP_077284                260 aa            linear   PRI 27-APR-2025
DEFINITION  dehydrogenase/reductase SDR family member 11 precursor [Homo
            sapiens].
ACCESSION   NP_077284
VERSION     NP_077284.2
DBSOURCE    REFSEQ: accession NM_024308.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Endo,S., Morikawa,Y., Kudo,Y., Suenami,K., Matsunaga,T., Ikari,A.
            and Hara,A.
  TITLE     Human dehydrogenase/reductase SDR family member 11 (DHRS11) and
            aldo-keto reductase 1C isoforms in comparison: Substrate and
            reaction specificity in the reduction of 11-keto-C19-steroids
  JOURNAL   J Steroid Biochem Mol Biol 199, 105586 (2020)
   PUBMED   31926269
  REMARK    GeneRIF: Human dehydrogenase/reductase SDR family member 11
            (DHRS11) and aldo-keto reductase 1C isoforms in comparison:
            Substrate and reaction specificity in the reduction of
            11-keto-C19-steroids.
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Endo,S., Miyagi,N., Matsunaga,T., Hara,A. and Ikari,A.
  TITLE     Human dehydrogenase/reductase (SDR family) member 11 is a novel
            type of 17beta-hydroxysteroid dehydrogenase
  JOURNAL   Biochem Biophys Res Commun 472 (1), 231-236 (2016)
   PUBMED   26920053
  REMARK    GeneRIF: The recombinant protein (DHRS11) efficiently catalyzed the
            conversion of the 17-keto group of estrone, 4- and 5-androstenes
            and 5alpha-androstanes into their 17beta-hydroxyl metabolites with
            NADPH as a coenzyme.
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG037061.1 and AY358712.1.
            
            On Jun 29, 2006 this sequence version replaced NP_077284.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.342264.1,
                                           SRR3476690.69859.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000618403.5/ ENSP00000482704.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..260
                     /product="dehydrogenase/reductase SDR family member 11
                     precursor"
                     /EC_number="1.1.1.62"
                     /EC_number="1.1.1.270"
                     /note="short-chain dehydrogenase/reductase family 24C
                     member 1; dehydrogenase/reductase (SDR family) member 11;
                     estradiol 17-beta-dehydrogenase; 17-beta-hydroxysteroid
                     dehydrogenase; 3-beta-hydroxysteroid 3-dehydrogenase"
                     /calculated_mol_wt=25229
     sig_peptide     1..30
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWP2.1)"
                     /calculated_mol_wt=3098
     Region          6..256
                     /region_name="Mgc4172-like_SDR_c"
                     /note="human Mgc4172-like, classical (c) SDRs; cd05343"
                     /db_xref="CDD:187601"
     Site            order(18,20..23,42..44,69..72,97..99,120,149..151,166,170,
                     198..201,203..205,208)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187601"
     mat_peptide     31..260
                     /product="Dehydrogenase/reductase SDR family member 11.
                     /id=PRO_0000045490"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWP2.1)"
                     /calculated_mol_wt=25229
     Site            order(74,105..109,111,114..115,118,123,126..127,130,
                     133..134,157,164..165,168,171..172,175..176,178..183,
                     185..186,190,192,226..227,231,235,238,244..256)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187601"
     Site            order(121,151,166,170)
                     /site_type="active"
                     /db_xref="CDD:187601"
     Site            196
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187601"
     CDS             1..260
                     /gene="DHRS11"
                     /gene_synonym="ARPG836; SDR24C1; spDHRS11"
                     /coded_by="NM_024308.4:132..914"
                     /db_xref="CCDS:CCDS11315.2"
                     /db_xref="GeneID:79154"
                     /db_xref="HGNC:HGNC:28639"
                     /db_xref="MIM:616159"
ORIGIN      
        1 marpgmerwr drlalvtgas ggigaavara lvqqglkvvg cartvgniee laaecksagy
       61 pgtlipyrcd lsneedilsm fsairsqhsg vdicinnagl arpdtllsgs tsgwkdmfnv
      121 nvlalsictr eayqsmkern vddghiinin smsghrvlpl svthfysatk yavtaltegl
      181 rqelreaqth iratcispgv vetqfafklh dkdpekaaat yeqmkclkpe dvaeaviyvl
      241 stpahiqigd iqmrpteqvt
//
LOCUS       NP_080807                336 aa            linear   ROD 27-APR-2025
DEFINITION  apoptosis-enhancing nuclease isoform 1 [Mus musculus].
ACCESSION   NP_080807
VERSION     NP_080807.3
DBSOURCE    REFSEQ: accession NM_026531.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Bizen,N., Bepari,A.K., Zhou,L., Abe,M., Sakimura,K., Ono,K. and
            Takebayashi,H.
  TITLE     Ddx20, an Olig2 binding factor, governs the survival of neural and
            oligodendrocyte progenitor cells via proper Mdm2 splicing and p53
            suppression
  JOURNAL   Cell Death Differ 29 (5), 1028-1041 (2022)
   PUBMED   34974536
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Tiu,G.C., Kerr,C.H., Forester,C.M., Krishnarao,P.S.,
            Rosenblatt,H.D., Raj,N., Lantz,T.C., Zhulyn,O., Bowen,M.E.,
            Shokat,L., Attardi,L.D., Ruggero,D. and Barna,M.
  TITLE     A p53-dependent translational program directs tissue-selective
            phenotypes in a model of ribosomopathies
  JOURNAL   Dev Cell 56 (14), 2089-2102 (2021)
   PUBMED   34242585
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Ulmke,P.A., Xie,Y., Sokpor,G., Pham,L., Shomroni,O., Berulava,T.,
            Rosenbusch,J., Basu,U., Fischer,A., Nguyen,H.P., Staiger,J.F. and
            Tuoc,T.
  TITLE     Post-transcriptional regulation by the exosome complex is required
            for cell survival and forebrain development via repression of P53
            signaling
  JOURNAL   Development 148 (3) (2021)
   PUBMED   33462115
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK031972.1 and AC138376.11.
            
            On Jul 1, 2009 this sequence version replaced NP_080807.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1). Variants 1 and 3 both encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK031972.1, AK167658.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 44.83 cM"
     Protein         1..336
                     /product="apoptosis-enhancing nuclease isoform 1"
                     /EC_number="3.1.-.-"
                     /note="interferon stimulated exonuclease gene 20-like 1;
                     interferon-stimulated 20 kDa exonuclease-like 1"
                     /calculated_mol_wt=37178
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZI9.1)"
     Region          25..33
                     /region_name="Nucleolar localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZI9.1)"
     Region          56..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZI9.1)"
     Region          110..266
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Site            order(113..116,192..193,195..197,257)
                     /site_type="active"
                     /db_xref="CDD:99852"
     Site            order(113,115,197,257)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99852"
     Site            order(114..116,192..193,195..196,257)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99852"
     Region          164..187
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZI9.1)"
     Region          276..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZI9.1)"
     CDS             1..336
                     /gene="Aen"
                     /gene_synonym="2700083B06Rik; Isg20l1"
                     /coded_by="NM_026531.5:153..1163"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS39988.2"
                     /db_xref="GeneID:68048"
                     /db_xref="MGI:MGI:1915298"
ORIGIN      
        1 mvagevpest qcpsltslnt kdvvrrrhkr rsrqhqrfma rkallqeqel lstapgpglc
       61 llpspsqmpa vteasdsrrq rpkarsgsng lcskksvpre aprpgpikcv aidcemvgtg
      121 pqgrvselar csvvsysgdv lydkyirpem pivdyrtrws gitrqhmhka ipfqvaqkei
      181 lkllkgkvvv ghalhndfqa lkyvhprsqt rdttyvpnll sqpsslirtr vslkdlalnl
      241 lhkkiqvghq ghssvedamt amelyqlvev qweqqvassa qapaedrgpd sstdveqymd
      301 dqywpedltq stgaetnggp drqegeegqg arsapp
//
LOCUS       NP_001007554             798 aa            linear   PRI 27-APR-2025
DEFINITION  cold shock domain-containing protein E1 isoform 1 [Homo sapiens].
ACCESSION   NP_001007554
VERSION     NP_001007554.1
DBSOURCE    REFSEQ: accession NM_001007553.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Kakumani,P.K., Ko,Y., Ramakrishna,S., Christopher,G., Dodgson,M.,
            Shrinet,J., Harvey,L.M., Shin,C. and Simard,M.J.
  TITLE     CSDE1 promotes miR-451 biogenesis
  JOURNAL   Nucleic Acids Res 51 (17), 9385-9396 (2023)
   PUBMED   37493604
  REMARK    GeneRIF: CSDE1 promotes miR-451 biogenesis.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Liu,J., Zhang,N., Zeng,J., Wang,T., Shen,Y., Ma,C. and Yang,M.
  TITLE     N6 -methyladenosine-modified lncRNA ARHGAP5-AS1 stabilises CSDE1
            and coordinates oncogenic RNA regulons in hepatocellular carcinoma
  JOURNAL   Clin Transl Med 12 (11), e1107 (2022)
   PUBMED   36354136
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Smith,G.A., Padmanabhan,A., Lau,B.H., Pampana,A., Li,L., Lee,C.Y.,
            Pelonero,A., Nishino,T., Sadagopan,N., Xia,V.Q., Jain,R.,
            Natarajan,P., Wu,R.S., Black,B.L., Srivastava,D., Shokat,K.M. and
            Chorba,J.S.
  TITLE     Cold shock domain-containing protein E1 is a posttranscriptional
            regulator of the LDL receptor
  JOURNAL   Sci Transl Med 14 (662), eabj8670 (2022)
   PUBMED   36103516
  REMARK    GeneRIF: Cold shock domain-containing protein E1 is a
            posttranscriptional regulator of the LDL receptor.
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Kim,Y., Ko,J.Y., Lee,S.B., Oh,S., Park,J.W., Kang,H.G., Kim,D.H.,
            Chung,D., Lim,S., Kong,H., Kim,J., Yoo,K.H., Han,W., Chun,K.H. and
            Park,J.H.
  TITLE     Reduced miR-371b-5p expression drives tumor progression via
            CSDE1/RAC1 regulation in triple-negative breast cancer
  JOURNAL   Oncogene 41 (22), 3151-3161 (2022)
   PUBMED   35490208
  REMARK    GeneRIF: Reduced miR-371b-5p expression drives tumor progression
            via CSDE1/RAC1 regulation in triple-negative breast cancer.
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Avolio,R., Ingles-Ferrandiz,M., Ciocia,A., Coll,O., Bonnin,S.,
            Guitart,T., Ribo,A. and Gebauer,F.
  TITLE     Coordinated post-transcriptional control of oncogene-induced
            senescence by UNR/CSDE1
  JOURNAL   Cell Rep 38 (2), 110211 (2022)
   PUBMED   35021076
  REMARK    GeneRIF: Coordinated post-transcriptional control of
            oncogene-induced senescence by UNR/CSDE1.
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Hunt,S.L., Hsuan,J.J., Totty,N. and Jackson,R.J.
  TITLE     unr, a cellular cytoplasmic RNA-binding protein with five
            cold-shock domains, is required for internal initiation of
            translation of human rhinovirus RNA
  JOURNAL   Genes Dev 13 (4), 437-448 (1999)
   PUBMED   10049359
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Boussadia,O., Jacquemin-Sablon,H. and Dautry,F.
  TITLE     Exon skipping in the expression of the gene immediately upstream of
            N-ras (unr/NRU)
  JOURNAL   Biochim Biophys Acta 1172 (1-2), 64-72 (1993)
   PUBMED   8439573
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Nicolaiew,N., Triqueneaux,G. and Dautry,F.
  TITLE     Organization of the human N-ras locus: characterization of a gene
            located immediately upstream of N-ras
  JOURNAL   Oncogene 6 (5), 721-730 (1991)
   PUBMED   2052355
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Jeffers,M., Paciucci,R. and Pellicer,A.
  TITLE     Characterization of unr; a gene closely linked to N-ras
  JOURNAL   Nucleic Acids Res 18 (16), 4891-4899 (1990)
   PUBMED   2204029
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP202324.1, AB020692.1 and BU681634.1.
            
            Transcript Variant: This variant (1) differs in the 5' UTR and
            coding sequence compared to variant 4. The resulting isoform (1) is
            shorter at the N-terminus compared to isoform 4. Variants 1 and 5
            both encode isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.247132.1,
                                           SRR1803613.114801.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358528.9/ ENSP00000351329.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..798
                     /product="cold shock domain-containing protein E1 isoform
                     1"
                     /note="upstream of NRAS; NRAS-related; cold shock
                     domain-containing protein E1; cold shock domain containing
                     E1, RNA binding; N-ras upstream gene protein"
                     /calculated_mol_wt=88754
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:37316325; propagated from
                     UniProtKB/Swiss-Prot (O75534.2)"
     Region          26..90
                     /region_name="CSD"
                     /note="'Cold-shock' DNA-binding domain; pfam00313"
                     /db_xref="CDD:278729"
     Site            81
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75534.2)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75534.2)"
     Region          186..248
                     /region_name="CSD"
                     /note="'Cold-shock' DNA-binding domain; pfam00313"
                     /db_xref="CDD:278729"
     Site            order(192,199,210,238)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:239905"
     Site            order(197..202,209..212)
                     /site_type="active"
                     /note="RNA-binding motif [active]"
                     /db_xref="CDD:239905"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75534.2)"
     Region          350..413
                     /region_name="CSP"
                     /note="Cold shock protein domain; smart00357"
                     /db_xref="CDD:214633"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O75534.2)"
     Region          521..582
                     /region_name="CSD"
                     /note="'Cold-shock' DNA-binding domain; pfam00313"
                     /db_xref="CDD:278729"
     Site            order(530..535,542..545)
                     /site_type="active"
                     /note="RNA-binding motif [active]"
                     /db_xref="CDD:239905"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75534.2)"
     Region          674..738
                     /region_name="CSD"
                     /note="'Cold-shock' DNA-binding domain; pfam00313"
                     /db_xref="CDD:278729"
     Region          756..786
                     /region_name="SUZ-C"
                     /note="SUZ-C motif; pfam12901"
                     /db_xref="CDD:463745"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75534.2)"
     CDS             1..798
                     /gene="CSDE1"
                     /gene_synonym="D1S155E; UNR"
                     /coded_by="NM_001007553.3:448..2844"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30812.1"
                     /db_xref="GeneID:7812"
                     /db_xref="HGNC:HGNC:29905"
                     /db_xref="MIM:191510"
ORIGIN      
        1 msfdpnllhn nghngypngt saalretgvi eklltsygfi qcserqarlf fhcsqyngnl
       61 qdlkvgddve fevssdrrtg kpiavklvki kqeilpeerm ngqvvcavph nleskspaap
      121 gqsptgsvcy erngevfylt ytpedvegnv qletgdkinf vidnnkhtga vsarnimllk
      181 kkqarcqgvv camkeafgfi ergdvvkeif fhysefkgdl etlqpgddve ftikdrngke
      241 vatdvrllpq gtvifedisi ehfegtvtkv ipkvpsknqn dplpgrikvd fvipkelpfg
      301 dkdtkskvtl legdhvrfni stdrrdkler atnievlsnt fqftnearem gviaamrdgf
      361 gfikcvdrdv rmffhfseil dgnqlhiade veftvvpdml saqrnhairi kklpkgtvsf
      421 hshsdhrflg tvekeatfsn pkttspnkgk ekeaedgiia yddcgvklti afqakdvegs
      481 tspqigdkve fsisdkqrpg qqvatcvrll grnsnskrll gyvatlkdnf gfietanhdk
      541 eiffhysefs gdvdslelgd mveyslskgk gnkvsaekvn kthsvngite eadptiysgk
      601 virplrsvdp tqteyqgmie iveegdmkge vypfgivgma nkgdclqkge svkfqlcvlg
      661 qnaqtmayni tplrratvec vkdqfgfiny evgdskklff hvkevqdgie lqagdevefs
      721 vilnqrtgkc sacnvwrvce gpkavaaprp drlvnrlkni tlddasaprl mvlrqprgpd
      781 nsmgfgaerk irqagvid
//
LOCUS       NP_001353580            1303 aa            linear   PRI 27-APR-2025
DEFINITION  microtubule-associated tumor suppressor candidate 2 isoform d [Homo
            sapiens].
ACCESSION   NP_001353580
VERSION     NP_001353580.1
DBSOURCE    REFSEQ: accession NM_001366651.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1303)
  AUTHORS   Xicota,L., Cosentino,S., Vardarajan,B., Mayeux,R., Perls,T.T.,
            Andersen,S.L., Zmuda,J.M., Thyagarajan,B., Yashin,A.,
            Wojczynski,M.K., Krinsky-McHale,S., Handen,B.L., Christian,B.T.,
            Head,E., Mapstone,M.E., Schupf,N., Lee,J.H. and Barral,S.
  CONSRTM   Long-Life Family Study (LLFS); Alzheimer's Disease Genetic
            Consortium (ADGC); Alzheimer's Biomarkers Consortium-Down Syndrome
            (ABC-DS)
  TITLE     Whole genome-wide sequence analysis of long-lived families
            (Long-Life Family Study) identifies MTUS2 gene associated with
            late-onset Alzheimer's disease
  JOURNAL   Alzheimers Dement 20 (4), 2670-2679 (2024)
   PUBMED   38380866
  REMARK    GeneRIF: Whole genome-wide sequence analysis of long-lived families
            (Long-Life Family Study) identifies MTUS2 gene associated with
            late-onset Alzheimer's disease.
REFERENCE   2  (residues 1 to 1303)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 1303)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1303)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1303)
  AUTHORS   Kovacs,I.A., Luck,K., Spirohn,K., Wang,Y., Pollis,C., Schlabach,S.,
            Bian,W., Kim,D.K., Kishore,N., Hao,T., Calderwood,M.A., Vidal,M.
            and Barabasi,A.L.
  TITLE     Network-based prediction of protein interactions
  JOURNAL   Nat Commun 10 (1), 1240 (2019)
   PUBMED   30886144
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1303)
  AUTHORS   Rodrigues-Ferreira,S. and Nahmias,C.
  TITLE     An ATIPical family of angiotensin II AT2 receptor-interacting
            proteins
  JOURNAL   Trends Endocrinol Metab 21 (11), 684-690 (2010)
   PUBMED   20889352
  REMARK    Review article
REFERENCE   7  (residues 1 to 1303)
  AUTHORS   Trevino,L.R., Shimasaki,N., Yang,W., Panetta,J.C., Cheng,C.,
            Pei,D., Chan,D., Sparreboom,A., Giacomini,K.M., Pui,C.H.,
            Evans,W.E. and Relling,M.V.
  TITLE     Germline genetic variation in an organic anion transporter
            polypeptide associated with methotrexate pharmacokinetics and
            clinical effects
  JOURNAL   J Clin Oncol 27 (35), 5972-5978 (2009)
   PUBMED   19901119
REFERENCE   8  (residues 1 to 1303)
  AUTHORS   Du Puy,L., Beqqali,A., Monshouwer-Kloots,J., Haagsman,H.P.,
            Roelen,B.A. and Passier,R.
  TITLE     CAZIP, a novel protein expressed in the developing heart and
            nervous system
  JOURNAL   Dev Dyn 238 (11), 2903-2911 (2009)
   PUBMED   19806667
  REMARK    GeneRIF: These results suggest a role for CAZIP in development and
            function of the heart and nervous system in vertebrates.
REFERENCE   9  (residues 1 to 1303)
  AUTHORS   Jiang,K., Wang,J., Liu,J., Ward,T., Wordeman,L., Davidson,A.,
            Wang,F. and Yao,X.
  TITLE     TIP150 interacts with and targets MCAK at the microtubule plus ends
  JOURNAL   EMBO Rep 10 (8), 857-865 (2009)
   PUBMED   19543227
  REMARK    GeneRIF: TIP150 facilitates the EB1-dependent loading of MCAK onto
            MT plus ends and orchestrates the dynamics at the plus end of MTs.
REFERENCE   10 (residues 1 to 1303)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL359741.9, AL160255.14, AL596092.8, AL607144.5 and AL596114.10.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.3"
     Protein         1..1303
                     /product="microtubule-associated tumor suppressor
                     candidate 2 isoform d"
                     /note="+TIP of 150 kDa; cardiac zipper protein; tracking
                     protein of 150 kDa; microtubule plus-end tracking protein
                     TIP150; microtubule associated tumor suppressor candidate
                     2"
                     /calculated_mol_wt=143320
     Region          <631..927
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          924..>1257
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1303
                     /gene="MTUS2"
                     /gene_synonym="CAZIP; ICIS; KIAA0774; TIP150"
                     /coded_by="NM_001366651.1:589..4500"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:23281"
                     /db_xref="HGNC:HGNC:20595"
                     /db_xref="MIM:619358"
ORIGIN      
        1 msvpvapkks cytqlrdnrn aarnnnesil slgdtnanqi mlevssshde sktcdlgdei
       61 gntnssepen rthfhkefhq lqgfgkgsqa gsaslkdfrl sstiqrelne ehtvergtds
      121 lqttrsiqgp slsswrnvms easldvlakr daeiprhvpk dklaktldne elrrhslera
      181 sssvaavgsl tpqhpqplsl dsreargqip gggegpqktl pdhavpaafp atdstsegks
      241 vrhpkpstse skqstpsetq tvgahvlqvc sehtshsahp epalnltlas keipskleaq
      301 lgqgkgeakl dlkyvpprrv eqegkaaqeg ylgchkeenl salegrdpcg eahpeatdal
      361 ghllnsdlhh lgvgrgncee krgvnpgeqd slhttpkqgs aslggadnqp tgkispcage
      421 klgertsssf spgdshvafi pnnltdskpl dvieeerrlg sgnkdsvmvl vfnpsvgenk
      481 tevpepldpq sgrsearesk evttsvaenr nllenadkie stsaradsvl nipaplhpet
      541 tvnmtyqptt psssfqdvsv fgmdagsplv vppptdsarl lntspkvpdk ntcpsgipkp
      601 vfthskdtps sqegmenyqv ekteertetk piimpkpkhv rpkiityirr npqalgqvda
      661 slvpvglpya pptctmplph eekaaggdlk psanlyekfk pdlqkprvfs sglmvsgikp
      721 pghpfsqmse kflqevtdhp gkeefcsppy ahyevpptfy rsamllkpql glgamsrlps
      781 aksriliasq rssasaihpp gpittatsly ssdpsgstfg neeqpvlkas lpskdtpkga
      841 grvappasss vtaprrsllp apkststpag tkkdaqkdqd tnkpavsspk rvaasttklh
      901 spgypkqrta aarngfppkp dpqareaerq lvlrlkerce qqtrqlgvaq gelkraicgf
      961 dalavatqhf frknesalvk ekelsielan irdevafhta kceklqkeke elerrfedev
     1021 krlgwqqqae lqeleerlql qfeaemarlq eehgdqllsi rcqhqeqved ltashdaall
     1081 emennhtvai tilqddhdhk vqelmsthel ekkeleenfe klrlslqdqv dtltfqsqsl
     1141 rdrarrfeea lrknteeqle ialapyqhle edmkslkqvl emknqqiheq ekkilelekl
     1201 aekniileek iqvlqqqned lkaridqntv vtrqlseena nlqeyveket qekkrlsrtn
     1261 eellwklqtg dptspiklsp tspvyrgsss gpssparvst tpr
//
LOCUS       NP_776291                522 aa            linear   ROD 27-APR-2025
DEFINITION  alanine aminotransferase 2 [Mus musculus].
ACCESSION   NP_776291
VERSION     NP_776291.1
DBSOURCE    REFSEQ: accession NM_173866.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Baytas,O., Davidson,S.M., Kauer,J.A. and Morrow,E.M.
  TITLE     Loss of mitochondrial enzyme GPT2 leads to reprogramming of
            synaptic glutamate metabolism
  JOURNAL   Mol Brain 17 (1), 87 (2024)
   PUBMED   39604975
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Yiew,N.K.H., Vazquez,J.H., Martino,M.R., Kennon-McGill,S.,
            Price,J.R., Allard,F.D., Yee,E.U., Layman,A.J., James,L.P.,
            McCommis,K.S., Finck,B.N. and McGill,M.R.
  TITLE     Hepatic pyruvate and alanine metabolism are critical and
            complementary for maintenance of antioxidant capacity and
            resistance to oxidative insult
  JOURNAL   Mol Metab 77, 101808 (2023)
   PUBMED   37716594
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Yiew,N.K.H., Deja,S., Ferguson,D., Cho,K., Jarasvaraparn,C.,
            Jacome-Sosa,M., Lutkewitte,A.J., Mukherjee,S., Fu,X., Singer,J.M.,
            Patti,G.J., Burgess,S.C. and Finck,B.N.
  TITLE     Effects of hepatic mitochondrial pyruvate carrier deficiency on de
            novo lipogenesis and gluconeogenesis in mice
  JOURNAL   iScience 26 (11), 108196 (2023)
   PUBMED   37942005
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Cui,M., Peng,J., Zhou,Y., Wang,X. and Cui,D.
  TITLE     Exosomal GPT2 derived from triple-negative breast cancer cells
            promotes metastasis by activating BTRC
  JOURNAL   Thorac Cancer 14 (21), 2018-2025 (2023)
   PUBMED   37287397
  REMARK    GeneRIF: Exosomal GPT2 derived from triple-negative breast cancer
            cells promotes metastasis by activating BTRC.
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Gehlen-Breitbach,S., Schmid,T., Frob,F., Rodrian,G., Weider,M.,
            Wegner,M. and Golz,L.
  TITLE     The Tip60/Ep400 chromatin remodeling complex impacts basic cellular
            functions in cranial neural crest-derived tissue during early
            orofacial development
  JOURNAL   Int J Oral Sci 15 (1), 16 (2023)
   PUBMED   37024457
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Baytas,O., Davidson,S.M., DeBerardinis,R.J. and Morrow,E.M.
  TITLE     Mitochondrial enzyme GPT2 regulates metabolic mechanisms required
            for neuron growth and motor function in vivo
  JOURNAL   Hum Mol Genet 31 (4), 587-603 (2022)
   PUBMED   34519342
  REMARK    GeneRIF: Mitochondrial enzyme GPT2 regulates metabolic mechanisms
            required for neuron growth and motor function in vivo.
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Ouyang,Q., Nakayama,T., Baytas,O., Davidson,S.M., Yang,C.,
            Schmidt,M., Lizarraga,S.B., Mishra,S., Ei-Quessny,M., Niaz,S., Gul
            Butt,M., Imran Murtaza,S., Javed,A., Chaudhry,H.R., Vaughan,D.J.,
            Hill,R.S., Partlow,J.N., Yoo,S.Y., Lam,A.T., Nasir,R.,
            Al-Saffar,M., Barkovich,A.J., Schwede,M., Nagpal,S., Rajab,A.,
            DeBerardinis,R.J., Housman,D.E., Mochida,G.H. and Morrow,E.M.
  TITLE     Mutations in mitochondrial enzyme GPT2 cause metabolic dysfunction
            and neurological disease with developmental and progressive
            features
  JOURNAL   Proc Natl Acad Sci U S A 113 (38), E5598-E5607 (2016)
   PUBMED   27601654
  REMARK    GeneRIF: The GPT2 gene demonstrates increasing expression in brain
            in the early postnatal period, and GPT2 protein localizes to
            mitochondria. Akin to the human phenotype, Gpt2-null mice exhibit
            reduced brain growth. Through metabolomics and direct isotope
            tracing experiments, we find a number of metabolic abnormalities
            associated with loss of Gpt2
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Qian,K., Zhong,S., Xie,K., Yu,D., Yang,R. and Gong,D.W.
  TITLE     Hepatic ALT isoenzymes are elevated in gluconeogenic conditions
            including diabetes and suppressed by insulin at the protein level
  JOURNAL   Diabetes Metab Res Rev 31 (6), 562-571 (2015)
   PUBMED   25865565
  REMARK    GeneRIF: Data suggest that Alt2/Gpt2 (but not Alt1/Gpt1) is induced
            in liver of obese mice (male ob/ob mice compared to lean C57BL/6J
            mice).
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Kuninger,D., Kuzmickas,R., Peng,B., Pintar,J.E. and Rotwein,P.
  TITLE     Gene discovery by microarray: identification of novel genes induced
            during growth factor-mediated muscle cell survival and
            differentiation
  JOURNAL   Genomics 84 (5), 876-889 (2004)
   PUBMED   15475267
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Jadhao,S.B., Yang,R.Z., Lin,Q., Hu,H., Anania,F.A., Shuldiner,A.R.
            and Gong,D.W.
  TITLE     Murine alanine aminotransferase: cDNA cloning, functional
            expression, and differential gene regulation in mouse fatty liver
  JOURNAL   Hepatology 39 (5), 1297-1302 (2004)
   PUBMED   15122758
  REMARK    Erratum:[Hepatology. 2004 Jul;40(1):269. Jadaho Sanjay B [corrected
            to Jadhao Sanjay B]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC130533.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK082030.1, AK033424.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 41.61 cM"
     Protein         1..522
                     /product="alanine aminotransferase 2"
                     /EC_number="2.6.1.2"
                     /note="glutamic--alanine transaminase 2; glutamic--pyruvic
                     transaminase 2; glutamate pyruvate transaminase 2"
                     /calculated_mol_wt=57813
     Region          48..522
                     /region_name="PTZ00377"
                     /note="alanine aminotransferase; Provisional"
                     /db_xref="CDD:240391"
     Site            414
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q8BGT5.1)"
     Site            504
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q8BGT5.1)"
     Site            511
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q8BGT5.1)"
     CDS             1..522
                     /gene="Gpt2"
                     /gene_synonym="4631422C05Rik; ALT2"
                     /coded_by="NM_173866.4:137..1705"
                     /db_xref="CCDS:CCDS22499.1"
                     /db_xref="GeneID:108682"
                     /db_xref="MGI:MGI:1915391"
ORIGIN      
        1 mqraavlvrr gscprasgpw grshssaaae asaalkvrpe rsprdriltl esmnpqvkav
       61 eyavrgpivl kageiemelq rgikkpftev iranigdaha mgqqpitflr qvmalctypn
      121 llnspsfped akkrarrilq acggnslgsy sasqgvncir edvaafitrr dgvpadpdni
      181 ylttgasdgi stilkllvsg ggksrtgvmi pipqyplysa viseldavqv nyyldeencw
      241 alnvdelrra lrqakdhcdp kvlciinpgn ptgqvqsrkc iedvihfawe eklflladev
      301 yqdnvyspdc rfhsfkkvly qmgheyssnv elasfhstsk gymgecgyrg gymevinlhp
      361 eikgqlvkll svrlcppvsg qaamdivvnp pepgeesfeq fsrekefvlg nlakkaklte
      421 dlfnqvpgiq cnplqgamya fprilipaka veaaqshkma pdmfycmkll eetgicvvpg
      481 sgfgqregty hfrmtilppv dklktvlhkv kdfhlkfleq ys
//
LOCUS       NP_037485                345 aa            linear   PRI 27-APR-2025
DEFINITION  tropomodulin-4 [Homo sapiens].
ACCESSION   NP_037485
VERSION     NP_037485.2
DBSOURCE    REFSEQ: accession NM_013353.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Yuen,M., Sandaradura,S.A., Dowling,J.J., Kostyukova,A.S., Moroz,N.,
            Quinlan,K.G., Lehtokari,V.L., Ravenscroft,G., Todd,E.J.,
            Ceyhan-Birsoy,O., Gokhin,D.S., Maluenda,J., Lek,M., Nolent,F.,
            Pappas,C.T., Novak,S.M., D'Amico,A., Malfatti,E., Thomas,B.P.,
            Gabriel,S.B., Gupta,N., Daly,M.J., Ilkovski,B., Houweling,P.J.,
            Davidson,A.E., Swanson,L.C., Brownstein,C.A., Gupta,V.A., Medne,L.,
            Shannon,P., Martin,N., Bick,D.P., Flisberg,A., Holmberg,E., Van den
            Bergh,P., Lapunzina,P., Waddell,L.B., Sloboda,D.D., Bertini,E.,
            Chitayat,D., Telfer,W.R., Laquerriere,A., Gregorio,C.C.,
            Ottenheijm,C.A., Bonnemann,C.G., Pelin,K., Beggs,A.H.,
            Hayashi,Y.K., Romero,N.B., Laing,N.G., Nishino,I.,
            Wallgren-Pettersson,C., Melki,J., Fowler,V.M., MacArthur,D.G.,
            North,K.N. and Clarke,N.F.
  TITLE     Leiomodin-3 dysfunction results in thin filament disorganization
            and nemaline myopathy
  JOURNAL   J Clin Invest 124 (11), 4693-4708 (2014)
   PUBMED   25250574
  REMARK    Erratum:[J Clin Invest. 2015 Jan;125(1):456-7. doi:
            10.1172/JCI80057. PMID: 25654555]
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Cox,P.R., Siddique,T. and Zoghbi,H.Y.
  TITLE     Genomic organization of Tropomodulins 2 and 4 and unusual
            intergenic and intraexonic splicing of YL-1 and Tropomodulin 4
  JOURNAL   BMC Genomics 2, 7 (2001)
   PUBMED   11716785
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Cox,P.R. and Zoghbi,H.Y.
  TITLE     Sequencing, expression analysis, and mapping of three unique human
            tropomodulin genes and their mouse orthologs
  JOURNAL   Genomics 63 (1), 97-107 (2000)
   PUBMED   10662549
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Almenar-Queralt,A., Lee,A., Conley,C.A., Ribas de Pouplana,L. and
            Fowler,V.M.
  TITLE     Identification of a novel tropomodulin isoform, skeletal
            tropomodulin, that caps actin filament pointed ends in fast
            skeletal muscle
  JOURNAL   J Biol Chem 274 (40), 28466-28475 (1999)
   PUBMED   10497209
  REMARK    Erratum:[J Biol Chem 2000 Apr 28;275(17):13164]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF177173.2.
            
            On Aug 24, 2007 this sequence version replaced NP_037485.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017810.1, AF177173.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465413 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295314.9/ ENSP00000295314.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..345
                     /product="tropomodulin-4"
                     /note="actin-capping protein; skeletal muscle
                     tropomodulin; tropomodulin 4 (muscle); skeletal
                     tropomodulin"
                     /calculated_mol_wt=39204
     Region          4..143
                     /region_name="Tropomodulin"
                     /note="pfam03250"
                     /db_xref="CDD:460862"
     Region          42..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZQ9.1)"
     Region          <194..>285
                     /region_name="RNA1"
                     /note="Ran GTPase-activating protein (RanGAP) involved in
                     mRNA processing and transport [Translation, ribosomal
                     structure and biogenesis]; COG5238"
                     /db_xref="CDD:444072"
     CDS             1..345
                     /gene="TMOD4"
                     /gene_synonym="SK-TMOD"
                     /coded_by="NM_013353.3:101..1138"
                     /db_xref="CCDS:CCDS988.1"
                     /db_xref="GeneID:29765"
                     /db_xref="HGNC:HGNC:11874"
                     /db_xref="MIM:605834"
ORIGIN      
        1 mssyqkelek yrdidedeil rtlspeeleq ldcelqemdp enmllpaglr qrdqtkkspt
       61 gpldreallq yleqqalevk erddlvpftg ekkgkpyiqp kreipaeeqi tlepeleeal
      121 ahatdaemcd iaaildmytl msnkqyydal csgeicnteg issvvqpdky kpvpdeppnp
      181 tnieeilkrv rsndkeleev nlnniqdipi pmlselceam kantyvrsfs lvatrsgdpi
      241 anavadmlre nrslqslnie snfisstglm avlkavrena tltelrvdnq rqwpgdavem
      301 ematvleqcp sivrfgyhft qqgpraraaq amtrnnelrr qqkkr
//
LOCUS       NP_001347782             375 aa            linear   ROD 27-APR-2025
DEFINITION  serpin B5 isoform a [Mus musculus].
ACCESSION   NP_001347782
VERSION     NP_001347782.1
DBSOURCE    REFSEQ: accession NM_001360853.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Kim,S.H., Mitchel,J.A., McGill,M., Cremona,T.P., Baek,J.W.,
            Kasahara,D.I., Anathy,V., Israel,E. and Park,J.A.
  TITLE     Increased extracellular maspin levels after mechanical compression
            in vitro or allergen challenge in vivo
  JOURNAL   J Allergy Clin Immunol 144 (4), 1116-1118 (2019)
   PUBMED   31228474
  REMARK    GeneRIF: This is the first study to recognize the potential
            implication of maspin in the pathophysiology of asthma
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Mahajan,N., Hoover,B., Rajendram,M., Shi,H.Y., Kawasaki,K.,
            Weibel,D.B. and Zhang,M.
  TITLE     Maspin binds to cardiolipin in mitochondria and triggers apoptosis
  JOURNAL   FASEB J 33 (5), 6354-6364 (2019)
   PUBMED   30786218
  REMARK    GeneRIF: model of apoptosis in which maspin binds to cardiolipin,
            displaces cytochrome c from the membrane, and facilitates its
            release to the cytoplasm.
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Zhang,M., Hendrix,M.J.C., Pemberton,P.A., Sakr,W.A. and Sheng,S.
  TITLE     An Essential Role of Maspin in Embryogenesis and Tumor
            Suppression-Response
  JOURNAL   Cancer Res 77 (18), 5208-5210 (2017)
   PUBMED   28877938
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Dzinic,S.H., Bernardo,M.M., Li,X., Fernandez-Valdivia,R., Ho,Y.S.,
            Mi,Q.S., Bandyopadhyay,S., Lonardo,F., Vranic,S., Oliveira,D.S.,
            Bonfil,R.D., Dyson,G., Chen,K., Omerovic,A., Sheng,X., Han,X.,
            Wu,D., Bi,X., Cabaravdic,D., Jakupovic,U., Wahba,M., Pang,A.,
            Harajli,D., Sakr,W.A. and Sheng,S.
  TITLE     An Essential Role of Maspin in Embryogenesis and Tumor Suppression
  JOURNAL   Cancer Res 77 (4), 886-896 (2017)
   PUBMED   27923833
  REMARK    GeneRIF: maspin is a powerful context-dependent tumor suppressor.
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Kaiserman,D., Knaggs,S., Scarff,K.L., Gillard,A., Mirza,G.,
            Cadman,M., McKeone,R., Denny,P., Cooley,J., Benarafa,C.,
            Remold-O'Donnell,E., Ragoussis,J. and Bird,P.I.
  TITLE     Comparison of human chromosome 6p25 with mouse chromosome 13
            reveals a greatly expanded ov-serpin gene repertoire in the mouse
  JOURNAL   Genomics 79 (3), 349-362 (2002)
   PUBMED   11863365
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Ngamkitidechakul,C., Burke,J.M., O'Brien,W.J. and Twining,S.S.
  TITLE     Maspin: synthesis by human cornea and regulation of in vitro
            stromal cell adhesion to extracellular matrix
  JOURNAL   Invest Ophthalmol Vis Sci 42 (13), 3135-3141 (2001)
   PUBMED   11726614
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Zhang,M., Magit,D., Botteri,F., Shi,H.Y., He,K., Li,M., Furth,P.
            and Sager,R.
  TITLE     Maspin plays an important role in mammary gland development
  JOURNAL   Dev Biol 215 (2), 278-287 (1999)
   PUBMED   10545237
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Sheng,S., Truong,B., Fredrickson,D., Wu,R., Pardee,A.B. and
            Sager,R.
  TITLE     Tissue-type plasminogen activator is a target of the tumor
            suppressor gene maspin
  JOURNAL   Proc Natl Acad Sci U S A 95 (2), 499-504 (1998)
   PUBMED   9435220
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Zhang,M., Sheng,S., Maass,N. and Sager,R.
  TITLE     mMaspin: the mouse homolog of a human tumor suppressor gene
            inhibits mammary tumor invasion and motility
  JOURNAL   Mol Med 3 (1), 49-59 (1997)
   PUBMED   9132279
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK136532.1, U54705.1, AC025047.17 and AC163626.5.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1 and 2
            both encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U54705.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849387, SAMN00849389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 50.34 cM"
     Protein         1..375
                     /product="serpin B5 isoform a"
                     /note="serine (or cysteine) proteinase inhibitor, clade B,
                     member 5; serpin B5; protease inhibitor 5; peptidase
                     inhibitor 5; serine (or cysteine) proteinase inhibitor,
                     clade B (ovalbumin), member 5; serine protease inhibitor
                     7"
                     /calculated_mol_wt=41980
     Region          1..375
                     /region_name="serpinB5_maspin"
                     /note="serpin family B member 5, mammary serine proteinase
                     inhibitor; cd02057"
                     /db_xref="CDD:381013"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70124.1)"
     Site            order(181..184,186,192,235)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381013"
     Site            298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70124.1)"
     Site            327..353
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381013"
     Site            340..341
                     /site_type="other"
                     /note="Reactive bond homolog. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P70124.1)"
     Site            361
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70124.1)"
     CDS             1..375
                     /gene="Serpinb5"
                     /gene_synonym="1110036M19Rik; Maspin; ovalbumin; PI-5;
                     Spi7"
                     /coded_by="NM_001360853.1:218..1345"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35684.1"
                     /db_xref="GeneID:20724"
                     /db_xref="MGI:MGI:109579"
ORIGIN      
        1 mdalrlansa favdlfkqlc erdpagnilf spiclstsls laqvgtkgdt aneigqvlhf
       61 envkdvpfgf qtvtsdvnkl ssfyslklvk rlyidkslnp stefisstkr pyakeletvd
      121 fkdkleetkg qinssikelt dghfedilse nsisdqtkil vvnaayfvgk wmkkfpeset
      181 kecpfriskt dtkpvqmmnl eatfclgnid disckiielp fqnkhlsmli vlpkdvedes
      241 tglekieqql npetllqwtn pstmanakvk lslpkfkvek midpkasles lglkslfnes
      301 tsdfsgmset kgvslsnvih rvcleitedg gesievpgsr ilqhkdefna dhpfiyiirh
      361 nktrniiffg kfcsp
//
LOCUS       NP_001030                649 aa            linear   PRI 27-APR-2025
DEFINITION  epithelial sodium channel subunit gamma [Homo sapiens].
ACCESSION   NP_001030
VERSION     NP_001030.2
DBSOURCE    REFSEQ: accession NM_001039.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Yang,Y., Zhong,X., Lan,Y., Liang,P., Huang,Y., Wang,Y., Zhou,X.,
            Zhang,Z., Liang,Y. and Xiao,X.
  TITLE     Aberrant inactivation of SCNN1G promotes the motility of head and
            neck squamous cell carcinoma
  JOURNAL   Pathol Res Pract 240, 154175 (2022)
   PUBMED   36327816
  REMARK    GeneRIF: Aberrant inactivation of SCNN1G promotes the motility of
            head and neck squamous cell carcinoma.
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Hayakawa,T., Fukuhara,A., Saiki,A., Otsuki,M. and Shimomura,I.
  TITLE     gammaENaC/CD9 in urinary extracellular vesicles as a potential
            biomarker of MR activity
  JOURNAL   J Endocrinol 252 (2), 81-90 (2021)
   PUBMED   34755678
  REMARK    GeneRIF: gammaENaC/CD9 in urinary extracellular vesicles as a
            potential biomarker of MR activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Pierandrei,S., Truglio,G., Ceci,F., Del Porto,P., Bruno,S.M.,
            Castellani,S., Conese,M., Ascenzioni,F. and Lucarelli,M.
  TITLE     DNA Methylation Patterns Correlate with the Expression of SCNN1A,
            SCNN1B, and SCNN1G (Epithelial Sodium Channel, ENaC) Genes
  JOURNAL   Int J Mol Sci 22 (7), 3754 (2021)
   PUBMED   33916525
  REMARK    GeneRIF: DNA Methylation Patterns Correlate with the Expression of
            SCNN1A, SCNN1B, and SCNN1G (Epithelial Sodium Channel, ENaC) Genes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Noreng,S., Posert,R., Bharadwaj,A., Houser,A. and Baconguis,I.
  TITLE     Molecular principles of assembly, activation, and inhibition in
            epithelial sodium channel
  JOURNAL   Elife 9, e59038 (2020)
   PUBMED   32729833
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 649)
  AUTHORS   Azad,A.K., Rauh,R., Vermeulen,F., Jaspers,M., Korbmacher,J.,
            Boissier,B., Bassinet,L., Fichou,Y., des Georges,M., Stanke,F., De
            Boeck,K., Dupont,L., Balascakova,M., Hjelte,L., Lebecque,P.,
            Radojkovic,D., Castellani,C., Schwartz,M., Stuhrmann,M.,
            Schwarz,M., Skalicka,V., de Monestrol,I., Girodon,E., Ferec,C.,
            Claustres,M., Tummler,B., Cassiman,J.J., Korbmacher,C. and
            Cuppens,H.
  TITLE     Mutations in the amiloride-sensitive epithelial sodium channel in
            patients with cystic fibrosis-like disease
  JOURNAL   Hum Mutat 30 (7), 1093-1103 (2009)
   PUBMED   19462466
REFERENCE   6  (residues 1 to 649)
  AUTHORS   Saxena,A., Hanukoglu,I., Saxena,D., Thompson,R.J., Gardiner,R.M.
            and Hanukoglu,A.
  TITLE     Novel mutations responsible for autosomal recessive multisystem
            pseudohypoaldosteronism and sequence variants in epithelial sodium
            channel alpha-, beta-, and gamma-subunit genes
  JOURNAL   J Clin Endocrinol Metab 87 (7), 3344-3350 (2002)
   PUBMED   12107247
  REMARK    GeneRIF: Novel mutations responsible for autosomal recessive
            multisystem pseudohypoaldosteronism and sequence variants in
            epithelial sodium channel gamma-subunit gene.
REFERENCE   7  (residues 1 to 649)
  AUTHORS   Waldmann,R., Champigny,G., Bassilana,F., Voilley,N. and
            Lazdunski,M.
  TITLE     Molecular cloning and functional expression of a novel
            amiloride-sensitive Na+ channel
  JOURNAL   J Biol Chem 270 (46), 27411-27414 (1995)
   PUBMED   7499195
REFERENCE   8  (residues 1 to 649)
  AUTHORS   Hansson,J.H., Nelson-Williams,C., Suzuki,H., Schild,L.,
            Shimkets,R., Lu,Y., Canessa,C., Iwasaki,T., Rossier,B. and
            Lifton,R.P.
  TITLE     Hypertension caused by a truncated epithelial sodium channel gamma
            subunit: genetic heterogeneity of Liddle syndrome
  JOURNAL   Nat Genet 11 (1), 76-82 (1995)
   PUBMED   7550319
REFERENCE   9  (residues 1 to 649)
  AUTHORS   Voilley,N., Bassilana,F., Mignon,C., Merscher,S., Mattei,M.G.,
            Carle,G.F., Lazdunski,M. and Barbry,P.
  TITLE     Cloning, chromosomal localization, and physical linkage of the beta
            and gamma subunits (SCNN1B and SCNN1G) of the human epithelial
            amiloride-sensitive sodium channel
  JOURNAL   Genomics 28 (3), 560-565 (1995)
   PUBMED   7490094
REFERENCE   10 (residues 1 to 649)
  AUTHORS   McDonald,F.J., Price,M.P., Snyder,P.M. and Welsh,M.J.
  TITLE     Cloning and expression of the beta- and gamma-subunits of the human
            epithelial sodium channel
  JOURNAL   Am J Physiol 268 (5 Pt 1), C1157-C1163 (1995)
   PUBMED   7762608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC059391.1, X87160.1 and
            AC099482.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 9, 2004 this sequence version replaced NP_001030.1.
            
            Summary: Nonvoltage-gated, amiloride-sensitive, sodium channels
            control fluid and electrolyte transport across epithelia in many
            organs. These channels are heteromeric complexes consisting of 3
            subunits: alpha, beta, and gamma. This gene encodes the gamma
            subunit, and mutations in this gene have been associated with
            Liddle syndrome. [provided by RefSeq, Apr 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC059391.1, SRR1660805.207998.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300061.3/ ENSP00000300061.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..649
                     /product="epithelial sodium channel subunit gamma"
                     /note="amiloride-sensitive sodium channel subunit gamma;
                     amiloride-sensitive sodium channel gamma-subunit; sodium
                     channe epithelial 1 gamma subunit; ENaC gamma subunit;
                     amiloride-sensitive epithelial sodium channel gamma
                     subunit; gamma-ENaC; sodium channel epithelial 1 gamma
                     subunit; gamma-NaCH; epithelial Na(+) channel subunit
                     gamma; nonvoltage-gated sodium channel 1 subunit gamma;
                     sodium channel, nonvoltage-gated 1, gamma; sodium channel,
                     non-voltage-gated 1, gamma subunit; ENaC subunit gamma"
                     /calculated_mol_wt=74139
     Region          24..630
                     /region_name="ENaC"
                     /note="sodium channel transporter; TIGR00859"
                     /db_xref="CDD:273304"
     Site            56..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51170.4)"
     Region          135..221
                     /region_name="Gating release of inhibition by proteolysis
                     (GRIP), protease-sensitive region that is responsible for
                     the proteolytic activation of the channel.
                     /evidence=ECO:0000269|PubMed:30251954,
                     ECO:0000269|PubMed:32729833"
                     /note="propagated from UniProtKB/Swiss-Prot (P51170.4)"
     Site            138..139
                     /site_type="cleavage"
                     /note="Cleavage, by furin.
                     /evidence=ECO:0000250|UniProtKB:Q9WU39; propagated from
                     UniProtKB/Swiss-Prot (P51170.4)"
     Site            181..182
                     /site_type="cleavage"
                     /note="Cleavage, by PRSS8.
                     /evidence=ECO:0000250|UniProtKB:Q9WU39; propagated from
                     UniProtKB/Swiss-Prot (P51170.4)"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51170.4)"
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51170.4)"
     Site            542..562
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51170.4)"
     Region          623..627
                     /region_name="PY motif, recruits WW domain-containing
                     proteins and is thereby required for ubiquitination and
                     inhibition of the channel by NEDD4 and NEDD4L.
                     /evidence=ECO:0000269|PubMed:17502380"
                     /note="propagated from UniProtKB/Swiss-Prot (P51170.4)"
     CDS             1..649
                     /gene="SCNN1G"
                     /gene_synonym="BESC3; ENaCg; ENaCgamma; LDLS2; PHA1;
                     PHA1B3; SCNEG"
                     /coded_by="NM_001039.4:114..2063"
                     /db_xref="CCDS:CCDS10608.1"
                     /db_xref="GeneID:6340"
                     /db_xref="HGNC:HGNC:10602"
                     /db_xref="MIM:600761"
ORIGIN      
        1 mapgekikak ikknlpvtgp qaptikelmr wyclntnthg crrivvsrgr lrrllwigft
       61 ltavalilwq callvfsfyt vsvsikvhfr kldfpavtic ninpykystv rhlladleqe
      121 trealkslyg fpesrkrrea eswnsvsegk qprfshripl lifdqdekgk ardfftgrkr
      181 kvggsiihka snvmhieskq vvgfqlcsnd tsdcatytfs sginaiqewy klhymnimaq
      241 vplekkinms ysaeellvtc ffdgvscdar nftlfhhpmh gncytfnnre netilstsmg
      301 gseyglqvil yineeeynpf lvsstgakvi ihrqdeypfv edvgteieta mvtsigmhlt
      361 esfklsepys qctedgsdvp irniynaays lqiclhscfq tkmvekcgca qysqplppaa
      421 nycnyqqhpn wmycyyqlhr afvqeelgcq svckeacsfk ewtlttslaq wpsvvsekwl
      481 lpvltwdqgr qvnkklnktd lakllifykd lnqrsimesp ansiemllsn fggqlglwms
      541 csvvcvieii evffidffsi iarrqwqkak ewwawkqapp cpeaprspqg qdnpaldidd
      601 dlptfnsalh lppalgtqvp gtpppkyntl rlerafsnql tdtqmldel
//
LOCUS       NP_080522                166 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein mL49 [Mus musculus].
ACCESSION   NP_080522
VERSION     NP_080522.1
DBSOURCE    REFSEQ: accession NM_026246.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Cheong,A., Lingutla,R. and Mager,J.
  TITLE     Expression analysis of mammalian mitochondrial ribosomal protein
            genes
  JOURNAL   Gene Expr Patterns 38, 119147 (2020)
   PUBMED   32987154
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Yoshikawa,T., Piao,Y., Zhong,J., Matoba,R., Carter,M.G., Wang,Y.,
            Goldberg,I. and Ko,M.S.
  TITLE     High-throughput screen for genes predominantly expressed in the ICM
            of mouse blastocysts by whole mount in situ hybridization
  JOURNAL   Gene Expr Patterns 6 (2), 213-224 (2006)
   PUBMED   16325481
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK150572.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK150715.1, AK150572.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 4.34 cM"
     Protein         1..166
                     /product="large ribosomal subunit protein mL49"
                     /note="neighbor of fau 1; 39S ribosomal protein L49,
                     mitochondrial"
                     /calculated_mol_wt=19002
     Region          54..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CQ40.1)"
     Region          82..166
                     /region_name="Img2"
                     /note="Mitochondrial large subunit ribosomal protein
                     (Img2); pfam05046"
                     /db_xref="CDD:461535"
     CDS             1..166
                     /gene="Mrpl49"
                     /gene_synonym="L49mt; MRP-L49; Nof1"
                     /coded_by="NM_026246.4:20..520"
                     /db_xref="CCDS:CCDS29488.1"
                     /db_xref="GeneID:18120"
                     /db_xref="MGI:MGI:108180"
ORIGIN      
        1 maaavlraal qdwrsclgrs ygrrklsqtq gppdnpgfve svdeyqfver llpptkipep
       61 pkhkhyptps gwqpprdplp slpyfvrrsr mhnipvykei thgnrqmtli rkvegdiwal
      121 qkdveeflsp llgktpitqv nevtgtlrik gyfdeqlkaw llekgf
//
LOCUS       NP_001348933              88 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 1 [Mus musculus].
ACCESSION   NP_001348933
VERSION     NP_001348933.1
DBSOURCE    REFSEQ: accession NM_001362004.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 88)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 88)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 88)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 88)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7.
            
            Transcript Variant: This variant (14), as well as variants 1, 8-13,
            and 15-19, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660825.134467.1,
                                           SRR1660819.145380.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..88
                     /product="cAMP-regulated phosphoprotein 21 isoform 1"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=9408
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q7M2N1; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10854908,
                     ECO:0000269|PubMed:15499021; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     CDS             1..88
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362004.1:512..778"
                     /note="isoform 1 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS40786.1"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqtl
//
LOCUS       NP_006359                371 aa            linear   PRI 27-APR-2025
DEFINITION  cyclic AMP-responsive element-binding protein 3 [Homo sapiens].
ACCESSION   NP_006359
VERSION     NP_006359.3
DBSOURCE    REFSEQ: accession NM_006368.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Lee,G.E., Bang,G., Byun,J., Lee,C.J., Chen,W., Jeung,D., An,H.J.,
            Kang,H.C., Lee,J.Y., Lee,H.S., Hong,Y.S., Kim,D.J., Keniry,M.,
            Kim,J.Y., Choi,J.S., Fanto,M., Cho,S.J., Kim,K.D. and Cho,Y.Y.
  TITLE     Dysregulated CREB3 cleavage at the nuclear membrane induces
            karyoptosis-mediated cell death
  JOURNAL   Exp Mol Med 56 (3), 686-699 (2024)
   PUBMED   38480902
  REMARK    GeneRIF: Dysregulated CREB3 cleavage at the nuclear membrane
            induces karyoptosis-mediated cell death.
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Zhan,S., Qiu,M., Wei,X., Wei,J., Qin,L., Jiang,B., Wen,Q., Chen,P.,
            Lin,Q., Wei,X., Zhou,Z., Jiang,Y., Liang,X., Li,R., Liu,Y. and
            Yu,H.
  TITLE     Potentially functional genetic variants in ferroptosis-related
            CREB3 and GALNT14 genes predict survival of hepatitis B
            virus-related hepatocellular carcinoma
  JOURNAL   Cancer Med 13 (1), e6848 (2024)
   PUBMED   38151984
  REMARK    GeneRIF: Potentially functional genetic variants in
            ferroptosis-related CREB3 and GALNT14 genes predict survival of
            hepatitis B virus-related hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Yadavalli,T., Sharma,P., Wu,D., Kapoor,D. and Shukla,D.
  TITLE     CREB3 Plays an Important Role in HPSE-Facilitated HSV-1 Release in
            Human Corneal Epithelial Cells
  JOURNAL   Viruses 14 (6), 1171 (2022)
   PUBMED   35746643
  REMARK    GeneRIF: CREB3 Plays an Important Role in HPSE-Facilitated HSV-1
            Release in Human Corneal Epithelial Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Oh-Hashi,K., Yamamoto,A., Murase,R. and Hirata,Y.
  TITLE     Comparative Analysis of CREB3 and CREB3L2 Protein Expression in
            HEK293 Cells
  JOURNAL   Int J Mol Sci 22 (5), 2767 (2021)
   PUBMED   33803345
  REMARK    GeneRIF: Comparative Analysis of CREB3 and CREB3L2 Protein
            Expression in HEK293 Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Lu,R. and Misra,V.
  TITLE     Zhangfei: a second cellular protein interacts with herpes simplex
            virus accessory factor HCF in a manner similar to Luman and VP16
  JOURNAL   Nucleic Acids Res 28 (12), 2446-2454 (2000)
   PUBMED   10871379
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Mahajan,S.S. and Wilson,A.C.
  TITLE     Mutations in host cell factor 1 separate its role in cell
            proliferation from recruitment of VP16 and LZIP
  JOURNAL   Mol Cell Biol 20 (3), 919-928 (2000)
   PUBMED   10629049
REFERENCE   8  (residues 1 to 371)
  AUTHORS   Lu,R. and Misra,V.
  TITLE     Potential role for luman, the cellular homologue of herpes simplex
            virus VP16 (alpha gene trans-inducing factor), in herpesvirus
            latency
  JOURNAL   J Virol 74 (2), 934-943 (2000)
   PUBMED   10623756
REFERENCE   9  (residues 1 to 371)
  AUTHORS   Freiman,R.N. and Herr,W.
  TITLE     Viral mimicry: common mode of association with HCF by VP16 and the
            cellular protein LZIP
  JOURNAL   Genes Dev 11 (23), 3122-3127 (1997)
   PUBMED   9389645
REFERENCE   10 (residues 1 to 371)
  AUTHORS   Lu,R., Yang,P., O'Hare,P. and Misra,V.
  TITLE     Luman, a new member of the CREB/ATF family, binds to herpes simplex
            virus VP16-associated host cellular factor
  JOURNAL   Mol Cell Biol 17 (9), 5117-5126 (1997)
   PUBMED   9271389
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG701230.1 and AF211848.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 14, 2002 this sequence version replaced NP_006359.2.
            
            Summary: This gene encodes a transcription factor that is a member
            of the leucine zipper family of DNA binding proteins. This protein
            binds to the cAMP-response element and regulates cell
            proliferation. The protein interacts with host cell factor C1,
            which also associates with the herpes simplex virus (HSV) protein
            VP16 that induces transcription of HSV immediate-early genes. This
            protein and VP16 both bind to the same site on host cell factor C1.
            It is thought that the interaction between this protein and host
            cell factor C1 plays a role in the establishment of latency during
            HSV infection. This protein also plays a role in leukocyte
            migration, tumor suppression, and endoplasmic reticulum
            stress-associated protein degradation. Additional transcript
            variants have been identified, but their biological validity has
            not been determined.[provided by RefSeq, Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.967257.1, AF211848.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000353704.3/ ENSP00000342136.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..371
                     /product="cyclic AMP-responsive element-binding protein 3"
                     /note="cyclic AMP response element (CRE)-binding
                     protein/activating transcription factor 1; basic leucine
                     zipper protein; small leucine zipper protein;
                     transcription factor LZIP-alpha; leucin zipper proitein"
                     /calculated_mol_wt=41248
     Region          1..92
                     /region_name="Transcription activation (acidic).
                     /evidence=ECO:0000269|PubMed:10984507"
                     /note="propagated from UniProtKB/Swiss-Prot (O43889.2)"
     Region          13..17
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O43889.2)"
     Region          54..58
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O43889.2)"
     Region          78..81
                     /region_name="HCFC1-binding-motif (HBM)"
                     /note="propagated from UniProtKB/Swiss-Prot (O43889.2)"
     Region          151..211
                     /region_name="bZIP_CREB3"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 3 (CREB3) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14689"
                     /db_xref="CDD:269837"
     Region          152..184
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (O43889.2)"
     Region          153..204
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269837"
     Site            order(156..157,159..161,163..168,170..172)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269837"
     Site            order(171,174..175,178..179,181..182,185..186,188..189,
                     192..193,195..196,199..200,202..203)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269837"
     Region          192..213
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (O43889.2)"
     Site            231..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43889.2)"
     Site            263..264
                     /site_type="cleavage"
                     /note="Cleavage, by PS1.
                     /evidence=ECO:0000269|PubMed:12138176; propagated from
                     UniProtKB/Swiss-Prot (O43889.2)"
     Site            266..267
                     /site_type="cleavage"
                     /note="Cleavage, by PS1.
                     /evidence=ECO:0000269|PubMed:12138176; propagated from
                     UniProtKB/Swiss-Prot (O43889.2)"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43889.2)"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43889.2)"
     CDS             1..371
                     /gene="CREB3"
                     /gene_synonym="LUMAN; LZIP; sLZIP"
                     /coded_by="NM_006368.5:108..1223"
                     /db_xref="CCDS:CCDS6588.1"
                     /db_xref="GeneID:10488"
                     /db_xref="HGNC:HGNC:2347"
                     /db_xref="MIM:606443"
ORIGIN      
        1 meleldagdq dllafllees gdlgtapdea vrapldwalp lsevpsdwev ddllcsllsp
       61 paslnilsss npclvhhdht yslpretvsm dlesescrke gtqmtpqhme elaeqeiarl
      121 vltdeeksll ekeglilpet lpltkteeqi lkrvrrkirn krsaqesrrk kkvyvggles
      181 rvlkytaqnm elqnkvqlle eqnlslldql rklqamviei snktsssstc ilvllvsfcl
      241 llvpamyssd trgslpaehg vlsrqlralp sedpyqlelp alqsevpkds thqwldgsdc
      301 vlqapgntsc llhympqaps aepplewpfp dlfseplcrg pilplqanlt rkggwlptgs
      361 psvilqdrys g
//
LOCUS       NP_003802                254 aa            linear   PRI 27-APR-2025
DEFINITION  tumor necrosis factor ligand superfamily member 9 [Homo sapiens].
ACCESSION   NP_003802
VERSION     NP_003802.1
DBSOURCE    REFSEQ: accession NM_003811.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Li,Z., Gao,T., Wang,J., Zhang,X., Zhang,Y., Zhang,L., Yang,P. and
            Liu,J.
  TITLE     Ferroptosis mediated by TNFSF9 interferes in acute ischaemic stroke
            reperfusion injury with the progression of acute ischaemic stroke
  JOURNAL   J Neurochem 168 (6), 1030-1044 (2024)
   PUBMED   38344886
  REMARK    GeneRIF: Ferroptosis mediated by TNFSF9 interferes in acute
            ischaemic stroke reperfusion injury with the progression of acute
            ischaemic stroke.
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,J. and Wang,Y.
  TITLE     Role of TNFSF9 bidirectional signal transduction in antitumor
            immunotherapy
  JOURNAL   Eur J Pharmacol 928, 175097 (2022)
   PUBMED   35714694
  REMARK    GeneRIF: Role of TNFSF9 bidirectional signal transduction in
            antitumor immunotherapy.
            Review article
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Nielsen,M.A., Juul-Madsen,K., Stegmayr,J., Gao,C., Mehta,A.Y.,
            Greisen,S.R., Kragstrup,T.W., Hvid,M., Vorup-Jensen,T.,
            Cummings,R.D., Leffler,H. and Deleuran,B.W.
  TITLE     Galectin-3 Decreases 4-1BBL Bioactivity by Crosslinking Soluble and
            Membrane Expressed 4-1BB
  JOURNAL   Front Immunol 13, 915890 (2022)
   PUBMED   35812455
  REMARK    GeneRIF: Galectin-3 Decreases 4-1BBL Bioactivity by Crosslinking
            Soluble and Membrane Expressed 4-1BB.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Qiu,L., Ning,H., Zhu,Y., Yang,Q., Liu,L., Luo,L., Gao,Y. and
            Xing,Y.
  TITLE     Feedback regulation of antioxidant transcription factor NFE2L1 and
            immunostimulatory factor 41BBL mediates the crosstalk between
            oxidative stress and tumor immunity
  JOURNAL   Mol Immunol 141, 265-272 (2022)
   PUBMED   34902807
  REMARK    GeneRIF: Feedback regulation of antioxidant transcription factor
            NFE2L1 and immunostimulatory factor 41BBL mediates the crosstalk
            between oxidative stress and tumor immunity.
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Wu,J., Wang,Y., Yang,Y., Liu,F., Chen,J., Jiang,Z. and Jiang,Z.
  TITLE     TNFSF9 promotes metastasis of pancreatic cancer through Wnt/Snail
            signaling and M2 polarization of macrophages
  JOURNAL   Aging (Albany NY) 13 (17), 21571-21586 (2021)
   PUBMED   34517345
  REMARK    GeneRIF: TNFSF9 promotes metastasis of pancreatic cancer through
            Wnt/Snail signaling and M2 polarization of macrophages.
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Saoulli,K., Lee,S.Y., Cannons,J.L., Yeh,W.C., Santana,A.,
            Goldstein,M.D., Bangia,N., DeBenedette,M.A., Mak,T.W., Choi,Y. and
            Watts,T.H.
  TITLE     CD28-independent, TRAF2-dependent costimulation of resting T cells
            by 4-1BB ligand
  JOURNAL   J Exp Med 187 (11), 1849-1862 (1998)
   PUBMED   9607925
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Arch,R.H. and Thompson,C.B.
  TITLE     4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve
            growth factor receptor subfamily that bind TNF receptor-associated
            factors and activate nuclear factor kappaB
  JOURNAL   Mol Cell Biol 18 (1), 558-565 (1998)
   PUBMED   9418902
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Loo,D.T., Chalupny,N.J., Bajorath,J., Shuford,W.W., Mittler,R.S.
            and Aruffo,A.
  TITLE     Analysis of 4-1BBL and laminin binding to murine 4-1BB, a member of
            the tumor necrosis factor receptor superfamily, and comparison with
            human 4-1BB
  JOURNAL   J Biol Chem 272 (10), 6448-6456 (1997)
   PUBMED   9045669
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Alderson,M.R., Smith,C.A., Tough,T.W., Davis-Smith,T.,
            Armitage,R.J., Falk,B., Roux,E., Baker,E., Sutherland,G.R. and
            Din,W.S.
  TITLE     Molecular and biological characterization of human 4-1BB and its
            ligand
  JOURNAL   Eur J Immunol 24 (9), 2219-2227 (1994)
   PUBMED   8088337
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Goodwin,R.G., Din,W.S., Davis-Smith,T., Anderson,D.M., Gimpel,S.D.,
            Sato,T.A., Maliszewski,C.R., Brannan,C.I., Copeland,N.G.,
            Jenkins,N.A. et al.
  TITLE     Molecular cloning of a ligand for the inducible T cell gene 4-1BB:
            a member of an emerging family of cytokines with homology to tumor
            necrosis factor
  JOURNAL   Eur J Immunol 23 (10), 2631-2641 (1993)
   PUBMED   8405064
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010503.8 and BX107825.1.
            
            Summary: The protein encoded by this gene is a cytokine that
            belongs to the tumor necrosis factor (TNF) ligand family. This
            transmembrane cytokine is a bidirectional signal transducer that
            acts as a ligand for TNFRSF9/4-1BB, which is a costimulatory
            receptor molecule in T lymphocytes. This cytokine and its receptor
            are involved in the antigen presentation process and in the
            generation of cytotoxic T cells. The receptor TNFRSF9/4-1BB is
            absent from resting T lymphocytes but rapidly expressed upon
            antigenic stimulation. The ligand encoded by this gene,
            TNFSF9/4-1BBL, has been shown to reactivate anergic T lymphocytes
            in addition to promoting T lymphocyte proliferation. This cytokine
            has also been shown to be required for the optimal CD8 responses in
            CD8 T cells. This cytokine is expressed in carcinoma cell lines,
            and is thought to be involved in T cell-tumor cell
            interaction.[provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.187091.1, U03398.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000245817.5/ ENSP00000245817.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..254
                     /product="tumor necrosis factor ligand superfamily member
                     9"
                     /note="receptor 4-1BB ligand; tumor necrosis factor
                     superfamily member 9; homolog of mouse 4-1BB-L; 4-1BBL;
                     tumor necrosis factor (ligand) superfamily, member 9;
                     tumor necrosis factor ligand 5A; CD137 ligand"
                     /calculated_mol_wt=26494
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P41273.1)"
     Site            order(94,142,144,199,204,234,238)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238108"
     Region          107..240
                     /region_name="TNF"
                     /note="Tumour necrosis factor family; smart00207"
                     /db_xref="CDD:214557"
     Site            order(110..111,116,162,169,176)
                     /site_type="active"
                     /note="receptor binding sites [active]"
                     /db_xref="CDD:238108"
     CDS             1..254
                     /gene="TNFSF9"
                     /gene_synonym="4-1BB-L; CD137L; TNLG5A"
                     /coded_by="NM_003811.4:12..776"
                     /db_xref="CCDS:CCDS12169.1"
                     /db_xref="GeneID:8744"
                     /db_xref="HGNC:HGNC:11939"
                     /db_xref="MIM:606182"
ORIGIN      
        1 meyasdasld peapwppapr aracrvlpwa lvagllllll laaacavfla cpwavsgara
       61 spgsaasprl regpelspdd paglldlrqg mfaqlvaqnv llidgplswy sdpglagvsl
      121 tgglsykedt kelvvakagv yyvffqlelr rvvagegsgs vslalhlqpl rsaagaaala
      181 ltvdlppass earnsafgfq grllhlsagq rlgvhlhtea rarhawqltq gatvlglfrv
      241 tpeipaglps prse
//
LOCUS       NP_001349119             619 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 668 [Mus musculus].
ACCESSION   NP_001349119
VERSION     NP_001349119.1
DBSOURCE    REFSEQ: accession NM_001362190.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC149222.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028251.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164141 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 69.79 cM"
     Protein         1..619
                     /product="zinc finger protein 668"
                     /calculated_mol_wt=68216
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q96K58; propagated from
                     UniProtKB/Swiss-Prot (Q8K2R5.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96K58; propagated from
                     UniProtKB/Swiss-Prot (Q8K2R5.1)"
     Region          24..44
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          36..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2R5.1)"
     Region          65..419
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          86..106
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          114..134
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(231,233,235,237..238,241..242,245,259,261,265..266,
                     269..270,273,287,289,291,293..294,297..298,301)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          248..598
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96K58; propagated from
                     UniProtKB/Swiss-Prot (Q8K2R5.1)"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          491..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K2R5.1)"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(523,525,527,529..530,533..534,537,551,553,557..558,
                     561..562,565,579,581,583,585..586,589..590,593)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..619
                     /gene="Zfp668"
                     /gene_synonym="E130018B19Rik; Znf668"
                     /coded_by="NM_001362190.1:1211..3070"
                     /db_xref="CCDS:CCDS21881.1"
                     /db_xref="GeneID:244219"
                     /db_xref="MGI:MGI:2442943"
ORIGIN      
        1 meveatears pgpcykrsgr rykclfctkt fpnapraarh aathtptdct eevreaqpkv
       61 dtepkaeeas gdkvsasvak prpyacplcp kayktapelr shgrshtgek pfpcpecgrr
      121 fmqpvclrvh lashagelpf rcthcpkayg tlsklkihqr ghtgerpyac pdcgksfadp
      181 svfrkhrrth aglrpyscer cgkayaelkd lrnhershtg erpflcsecg ksfsrssslt
      241 chqrihaaqk pyrcpacgkg ftqlssyqsh erthsgekpf lcprcgrmfs dpssfrrhqr
      301 ahegvkpyrc ekcgkdfrqp adlamhrrvh tgdrpfkclq cdktfvaswd lkrhalvhsg
      361 qrpfrceecg rafaeraslt khsrmhsger pfhcnacgks fvvlsslrkh erthrsnett
      421 gaapqqelvl glalpvgvvg egsaapvaga gvgdapagll glppesggvv atqwqvvgmt
      481 vehvecqdag vgeapstlgd agevggeetd ekppqfvcre cketfstltl lrrhershpe
      541 lrpfpctqcg ksfsdraglr khsrthssvr pyscsqcpka flsasdlrkh erthpvpigt
      601 pipleplval lgmpeegsa
//
LOCUS       NP_006237                467 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
            epsilon isoform isoform a [Homo sapiens].
ACCESSION   NP_006237
VERSION     NP_006237.1
DBSOURCE    REFSEQ: accession NM_006246.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Santos,A., Cristobal,I., Carames,C., Luque,M., Sanz-Alvarez,M.,
            Madoz-Gurpide,J., Rojo,F. and Garcia-Foncillas,J.
  TITLE     Deregulation of the miR-19b/PPP2R5E Signaling Axis Shows High
            Functional Impact in Colorectal Cancer Cells
  JOURNAL   Int J Mol Sci 24 (9), 7779 (2023)
   PUBMED   37175484
  REMARK    GeneRIF: Deregulation of the miR-19b/PPP2R5E Signaling Axis Shows
            High Functional Impact in Colorectal Cancer Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Salamango,D.J., McCann,J.L., Demir,O., Becker,J.T., Wang,J.,
            Lingappa,J.R., Temiz,N.A., Brown,W.L., Amaro,R.E. and Harris,R.S.
  TITLE     Functional and Structural Insights into a Vif/PPP2R5 Complex
            Elucidated Using Patient HIV-1 Isolates and Computational Modeling
  JOURNAL   J Virol 94 (21), e00631-20 (2020)
   PUBMED   32847850
  REMARK    GeneRIF: Functional and Structural Insights into a Vif/PPP2R5
            Complex Elucidated Using Patient HIV-1 Isolates and Computational
            Modeling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Virshup,D.M. and Shenolikar,S.
  TITLE     From promiscuity to precision: protein phosphatases get a makeover
  JOURNAL   Mol Cell 33 (5), 537-545 (2009)
   PUBMED   19285938
  REMARK    Review article
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Eichhorn,P.J., Creyghton,M.P. and Bernards,R.
  TITLE     Protein phosphatase 2A regulatory subunits and cancer
  JOURNAL   Biochim Biophys Acta 1795 (1), 1-15 (2009)
   PUBMED   18588945
  REMARK    Review article
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   7  (residues 1 to 467)
  AUTHORS   McCright,B., Rivers,A.M., Audlin,S. and Virshup,D.M.
  TITLE     The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
            encodes differentiation-induced phosphoproteins that target PP2A to
            both nucleus and cytoplasm
  JOURNAL   J Biol Chem 271 (36), 22081-22089 (1996)
   PUBMED   8703017
REFERENCE   8  (residues 1 to 467)
  AUTHORS   McCright,B., Brothman,A.R. and Virshup,D.M.
  TITLE     Assignment of human protein phosphatase 2A regulatory subunit genes
            b56alpha, b56beta, b56gamma, b56delta, and b56epsilon
            (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to
            chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 --> p12
  JOURNAL   Genomics 36 (1), 168-170 (1996)
   PUBMED   8812429
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Zolnierowicz,S., Van Hoof,C., Andjelkovic,N., Cron,P., Stevens,I.,
            Merlevede,W., Goris,J. and Hemmings,B.A.
  TITLE     The variable subunit associated with protein phosphatase 2A0
            defines a novel multimember family of regulatory subunits
  JOURNAL   Biochem J 317 (Pt 1) (Pt 1), 187-194 (1996)
   PUBMED   8694763
REFERENCE   10 (residues 1 to 467)
  AUTHORS   McCright,B. and Virshup,D.M.
  TITLE     Identification of a new family of protein phosphatase 2A regulatory
            subunits
  JOURNAL   J Biol Chem 270 (44), 26123-26128 (1995)
   PUBMED   7592815
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136038.5, CB989123.1,
            BC093766.1, L76703.1, AW134792.1, CK820060.1, AA782601.1 and
            AL118555.6.
            
            Summary: The protein encoded by this gene belongs to the
            phosphatase 2A regulatory subunit B family. Protein phosphatase 2A
            is one of the four major Ser/Thr phosphatases, and it is implicated
            in the negative control of cell growth and division. It consists of
            a common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes an epsilon isoform of the regulatory subunit B56 subfamily.
            Multiple transcript variants encoding several different isoforms
            have been found for this gene. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a). Variants 1 and 2
            both encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.4272.1, L76703.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337537.8/ ENSP00000337641.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..467
                     /product="serine/threonine-protein phosphatase 2A 56 kDa
                     regulatory subunit epsilon isoform isoform a"
                     /note="PP2A, B subunit, B' epsilon; PP2A, B subunit, B56
                     epsilon; PP2A, B subunit, PR61 epsilon; PP2A, B subunit,
                     R5 epsilon; serine/threonine protein phosphatase 2A, 56
                     kDa regulatory subunit, epsilon; protein phosphatase 2
                     regulatory subunit B', epsilon"
                     /calculated_mol_wt=54568
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16537.1)"
     Region          2..>67
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); cl27532"
                     /db_xref="CDD:474937"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Region          55..435
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); pfam01603"
                     /db_xref="CDD:460264"
     CDS             1..467
                     /gene="PPP2R5E"
                     /gene_synonym="B56E; B56epsilon"
                     /coded_by="NM_006246.5:607..2010"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9758.1"
                     /db_xref="GeneID:5529"
                     /db_xref="HGNC:HGNC:9313"
                     /db_xref="MIM:601647"
ORIGIN      
        1 mssapttpps vdkvdgfsrk svrkarqkrs qsssqfrsqg kpieltplpl lkdvpsseqp
       61 elflkklqqc cvifdfmdtl sdlkmkeykr stlnelvdyi tisrgclteq typevvrmvs
      121 cnifrtlpps dsnefdpeed eptleaswph lqlvyeffir flesqefqps iakkyidqkf
      181 vlqllelfds edprerdylk tvlhriygkf lglrafirkq inniflrfvy etehfngvae
      241 lleilgsiin gfalplkaeh kqflvkvlip lhtvrslslf haqlaycivq flekdpslte
      301 pvirglmkfw pktcsqkevm flgeleeild viepsqfvki qeplfkqiak cvssphfqva
      361 eralyywnne yimslieens nvilpimfss lyriskehwn paivalvynv lkafmemnst
      421 mfdeltatyk sdrqrekkke kereelwkkl edlelkrglr rdgiipt
//
LOCUS       NP_001348153             418 aa            linear   ROD 27-APR-2025
DEFINITION  nucleolar protein 4 isoform 6 [Mus musculus].
ACCESSION   NP_001348153 XP_017173411
VERSION     NP_001348153.1
DBSOURCE    REFSEQ: accession NM_001361224.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Toor,S.M., Wani,S. and Albagha,O.M.E.
  TITLE     Comprehensive Transcriptomic Profiling of Murine Osteoclast
            Differentiation Reveals Novel Differentially Expressed Genes and
            LncRNAs
  JOURNAL   Front Genet 12, 781272 (2021)
   PUBMED   34868271
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Takayanagi-Kiya,S., Misawa-Hojo,K., Kiya,T., Kunieda,T. and Kubo,T.
  TITLE     Splicing variants of NOL4 differentially regulate the transcription
            activity of Mlr1 and Mlr2 in cultured cells
  JOURNAL   Zoolog Sci 31 (11), 735-740 (2014)
   PUBMED   25366156
  REMARK    GeneRIF: These findings suggest that transactivation activities of
            Mlr1 and Mlr2 are differentially regulated by splicing variants of
            NOL4, which are expressed in a tissue-selective manner.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC102361.13, AC131338.4 and AC103368.7.
            
            On Mar 13, 2018 this sequence version replaced XP_017173411.1.
            
            Transcript Variant: This variant (6) contains a distinct 5' UTR and
            lacks an in-frame portion of the 5' coding region, compared to
            variant 3. The resulting isoform (6) has a shorter N-terminus,
            compared to isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660813.221826.1,
                                           SRR9219380.3628.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 11.96 cM"
     Protein         1..418
                     /product="nucleolar protein 4 isoform 6"
                     /calculated_mol_wt=45238
     CDS             1..418
                     /gene="Nol4"
                     /gene_synonym="1700013J13Rik; 4930568N03Rik; Gm1262"
                     /coded_by="NM_001361224.1:2146..3402"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:319211"
                     /db_xref="MGI:MGI:2441684"
ORIGIN      
        1 mscsecqkrm hlnpdgtdhk dngkpptlvt smidynmpit maymkhmklq llnsqqdede
       61 ssiesdefdm sdstrmsavn sdlssnleer mqspqtvhgq qdddsaaess ngnetlghss
      121 aasggahgre pedsssdgkt gleqeeqpln lsdspssaql tsefriddqg sdgknkyknl
      181 lisdlkmere arengskspa hsyssydsgk nesvdrgaed lslnrgdede dehdehedse
      241 kvnetdgvea erlkafnsrp ipshltsava esilasaces esrnaakrmr ldkaqdeaap
      301 adkqckpeaa qatystatvp gsqevlying ngtysyhsyr glggllsldd tsssgptdls
      361 mkrqlatgsg ssssstsrpq lspteinavr qlvagyresa afllrsadel enlilqqn
//
LOCUS       NP_001355636             148 aa            linear   PRI 27-APR-2025
DEFINITION  core-binding factor subunit beta isoform 3 [Homo sapiens].
ACCESSION   NP_001355636 XP_006721384
VERSION     NP_001355636.1
DBSOURCE    REFSEQ: accession NM_001368707.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Beyltjens,T., Boudin,E., Revencu,N., Boeckx,N., Bertrand,M.,
            Schutz,L., Haack,T.B., Weber,A., Biliouri,E., Vinksel,M.,
            Zagozen,A., Peterlin,B., Pai,S., Telegrafi,A., Henderson,L.B.,
            Ells,C., Turner,L., Wuyts,W., Van Hul,W., Hendrickx,G. and
            Mortier,G.R.
  TITLE     Heterozygous pathogenic variants involving CBFB cause a new
            skeletal disorder resembling cleidocranial dysplasia
  JOURNAL   J Med Genet 60 (5), 498-504 (2023)
   PUBMED   36241386
  REMARK    GeneRIF: Heterozygous pathogenic variants involving CBFB cause a
            new skeletal disorder resembling cleidocranial dysplasia.
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Malik,N., Kim,Y.I., Yan,H., Tseng,Y.C., du Bois,W., Ayaz,G.,
            Tran,A.D., Vera-Ramirez,L., Yang,H., Michalowski,A.M., Kruhlak,M.,
            Lee,M., Hunter,K.W. and Huang,J.
  TITLE     Dysregulation of Mitochondrial Translation Caused by CBFB
            Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in
            Breast Cancer
  JOURNAL   Cancer Res 83 (8), 1280-1298 (2023)
   PUBMED   36799863
  REMARK    GeneRIF: Dysregulation of Mitochondrial Translation Caused by CBFB
            Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in
            Breast Cancer.
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Khan,A.S., Campbell,K.J., Cameron,E.R. and Blyth,K.
  TITLE     The RUNX/CBFbeta Complex in Breast Cancer: A Conundrum of Context
  JOURNAL   Cells 12 (4), 641 (2023)
   PUBMED   36831308
  REMARK    GeneRIF: The RUNX/CFBbeta Complex in Breast Cancer: A Conundrum of
            Context.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Jiang,Y., Chao,H.Y., Lu,X.Z., Wu,P. and Sun,X.C.
  TITLE     [Molecular Genetic Characteristics of Acute Myeloid Leukemia
            Patients with CBFbeta-MYH11 Positive]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1661-1667 (2022)
   PUBMED   36476886
  REMARK    GeneRIF: [Molecular Genetic Characteristics of Acute Myeloid
            Leukemia Patients with CBFbeta-MYH11 Positive].
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Zhao,C., Wang,S. and Wang,K.
  TITLE     Mutual exclusivity between the fusion gene CBFB::MYH11 and somatic
            mitochondrial mutations in acute myeloid leukaemia
  JOURNAL   Br J Haematol 199 (4), e25-e29 (2022)
   PUBMED   36039018
  REMARK    GeneRIF: Mutual exclusivity between the fusion gene CBFB::MYH11 and
            somatic mitochondrial mutations in acute myeloid leukaemia.
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Chiba,N., Watanabe,T., Nomura,S., Tanaka,Y., Minowa,M., Niki,M.,
            Kanamaru,R. and Satake,M.
  TITLE     Differentiation dependent expression and distinct subcellular
            localization of the protooncogene product, PEBP2beta/CBFbeta, in
            muscle development
  JOURNAL   Oncogene 14 (21), 2543-2552 (1997)
   PUBMED   9191054
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Bae,S.C., Takahashi,E., Zhang,Y.W., Ogawa,E., Shigesada,K.,
            Namba,Y., Satake,M. and Ito,Y.
  TITLE     Cloning, mapping and expression of PEBP2 alpha C, a third gene
            encoding the mammalian Runt domain
  JOURNAL   Gene 159 (2), 245-248 (1995)
   PUBMED   7622058
REFERENCE   8  (residues 1 to 148)
  AUTHORS   Liu,P., Seidel,N., Bodine,D., Speck,N., Tarle,S. and Collins,F.S.
  TITLE     Acute myeloid leukemia with Inv (16) produces a chimeric
            transcription factor with a myosin heavy chain tail
  JOURNAL   Cold Spring Harb Symp Quant Biol 59, 547-553 (1994)
   PUBMED   7587111
REFERENCE   9  (residues 1 to 148)
  AUTHORS   Liu,P., Tarle,S.A., Hajra,A., Claxton,D.F., Marlton,P.,
            Freedman,M., Siciliano,M.J. and Collins,F.S.
  TITLE     Fusion between transcription factor CBF beta/PEBP2 beta and a
            myosin heavy chain in acute myeloid leukemia
  JOURNAL   Science 261 (5124), 1041-1044 (1993)
   PUBMED   8351518
REFERENCE   10 (residues 1 to 148)
  AUTHORS   Muller,C.W. and Schulz,G.E.
  TITLE     Structure of the complex of adenylate kinase from Escherichia coli
            with the inhibitor P1,P5-di(adenosine-5'-)pentaphosphate
  JOURNAL   J Mol Biol 202 (4), 909-912 (1988)
   PUBMED   2845103
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009084.9 and AC074143.5.
            
            On Feb 19, 2019 this sequence version replaced XP_006721384.1.
            
            Summary: The protein encoded by this gene is the beta subunit of a
            heterodimeric core-binding transcription factor belonging to the
            PEBP2/CBF transcription factor family which master-regulates a host
            of genes specific to hematopoiesis (e.g., RUNX1) and osteogenesis
            (e.g., RUNX2). The beta subunit is a non-DNA binding regulatory
            subunit; it allosterically enhances DNA binding by alpha subunit as
            the complex binds to the core site of various enhancers and
            promoters, including murine leukemia virus, polyomavirus enhancer,
            T-cell receptor enhancers and GM-CSF promoters. Alternative
            splicing generates two mRNA variants, each encoding a distinct
            carboxyl terminus. In some cases, a pericentric inversion of
            chromosome 16 [inv(16)(p13q22)] produces a chimeric transcript
            consisting of the N terminus of core-binding factor beta in a
            fusion with the C-terminal portion of the smooth muscle myosin
            heavy chain 11. This chromosomal rearrangement is associated with
            acute myeloid leukemia of the M4Eo subtype. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: Variants 3 and 4 encode isoforms that are the
            same length, but have distinct protein sequences.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.714144.1,
                                           SRR14038194.1831359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..148
                     /product="core-binding factor subunit beta isoform 3"
                     /note="SL3/AKV core-binding factor beta subunit;
                     polyomavirus enhancer binding protein 2, beta subunit;
                     SL3-3 enhancer factor 1 beta subunit; CBF-beta; PEA2-beta;
                     PEBP2-beta; SL3-3 enhancer factor 1 subunit beta"
                     /calculated_mol_wt=17463
     Region          1..128
                     /region_name="CBF_beta"
                     /note="Core binding factor beta subunit; pfam02312"
                     /db_xref="CDD:396750"
     CDS             1..148
                     /gene="CBFB"
                     /gene_synonym="CLCD2; PEBP2B"
                     /coded_by="NM_001368707.1:260..706"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:865"
                     /db_xref="HGNC:HGNC:1539"
                     /db_xref="MIM:121360"
ORIGIN      
        1 mprvvpdqrs kfeneeffrk lsreceikyt gfrdrpheer qarfqnacrd grseivylka
       61 pmilngvcvi wkgwidlqrl dgmgclefde eraqqedala qqafeearrr trefedrdrs
      121 hreemearrq qdpspgsnlg ggddlklr
//
LOCUS       NP_006511                116 aa            linear   PRI 27-APR-2025
DEFINITION  dynein light chain Tctex-type 3 [Homo sapiens].
ACCESSION   NP_006511
VERSION     NP_006511.1
DBSOURCE    REFSEQ: accession NM_006520.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Wang,H., Chen,X., Jin,Y., Liu,T., Song,Y., Zhu,X. and Zhu,X.
  TITLE     The role of DYNLT3 in breast cancer proliferation, migration, and
            invasion via epithelial-to-mesenchymal transition
  JOURNAL   Cancer Med 12 (14), 15289-15303 (2023)
   PUBMED   37260179
  REMARK    GeneRIF: The role of DYNLT3 in breast cancer proliferation,
            migration, and invasion via epithelial-to-mesenchymal transition.
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Gu,X., Wang,B., Zhu,H., Zhou,Y., Horning,A.M., Huang,T.H., Chen,Y.,
            Houghton,P., Lai,Z., Michalek,J.E. and Sun,L.Z.
  TITLE     Age-associated genes in human mammary gland drive human breast
            cancer progression
  JOURNAL   Breast Cancer Res 22 (1), 64 (2020)
   PUBMED   32539762
  REMARK    GeneRIF: Age-associated genes in human mammary gland drive human
            breast cancer progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Douglas,M.W., Diefenbach,R.J., Homa,F.L., Miranda-Saksena,M.,
            Rixon,F.J., Vittone,V., Byth,K. and Cunningham,A.L.
  TITLE     Herpes simplex virus type 1 capsid protein VP26 interacts with
            dynein light chains RP3 and Tctex1 and plays a role in retrograde
            cellular transport
  JOURNAL   J Biol Chem 279 (27), 28522-28530 (2004)
   PUBMED   15117959
REFERENCE   7  (residues 1 to 116)
  AUTHORS   Wilson,M.J., Salata,M.W., Susalka,S.J. and Pfister,K.K.
  TITLE     Light chains of mammalian cytoplasmic dynein: identification and
            characterization of a family of LC8 light chains
  JOURNAL   Cell Motil Cytoskeleton 49 (4), 229-240 (2001)
   PUBMED   11746667
  REMARK    Erratum:[Cell Motil Cytoskeleton. 2002 Jul;52(3):193.]
REFERENCE   8  (residues 1 to 116)
  AUTHORS   Tai,A.W., Chuang,J.Z. and Sung,C.H.
  TITLE     Cytoplasmic dynein regulation by subunit heterogeneity and its role
            in apical transport
  JOURNAL   J Cell Biol 153 (7), 1499-1509 (2001)
   PUBMED   11425878
REFERENCE   9  (residues 1 to 116)
  AUTHORS   King,S.M., Barbarese,E., Dillman,J.F. 3rd, Benashski,S.E., Do,K.T.,
            Patel-King,R.S. and Pfister,K.K.
  TITLE     Cytoplasmic dynein contains a family of differentially expressed
            light chains
  JOURNAL   Biochemistry 37 (43), 15033-15041 (1998)
   PUBMED   9790665
REFERENCE   10 (residues 1 to 116)
  AUTHORS   Roux,A.F., Rommens,J., McDowell,C., Anson-Cartwright,L., Bell,S.,
            Schappert,K., Fishman,G.A. and Musarella,M.
  TITLE     Identification of a gene from Xp21 with similarity to the tctex-1
            gene of the murine t complex
  JOURNAL   Hum Mol Genet 3 (2), 257-263 (1994)
   PUBMED   8004092
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA342302.1 and BC000968.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of a subclass of dynein light
            chains. The encoded protein homodimerizes and forms the light chain
            component of the cytoplasmic dynein motor protein complex. This
            protein may be important for binding dynein to specific cargos
            including the spindle checkpoint protein BUB3. This protein may
            also function independently of dynein as a transcriptional
            modulator. Pseudogenes of this gene are found on chromosomes 2 and
            20.[provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U02556.1, SRR3476690.401720.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378578.9/ ENSP00000367841.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..116
                     /product="dynein light chain Tctex-type 3"
                     /note="protein 91/23"
                     /calculated_mol_wt=12931
     Region          16..112
                     /region_name="DLC-like_DYNLT3"
                     /note="dynein light chain (DLC)-like domain found in
                     dynein light chain Tctex-type 3 (DYNLT3) and similar
                     proteins; cd21463"
                     /db_xref="CDD:412011"
     CDS             1..116
                     /gene="DYNLT3"
                     /gene_synonym="RP3; TCTE1L; TCTEX1L"
                     /coded_by="NM_006520.3:62..412"
                     /db_xref="CCDS:CCDS14243.1"
                     /db_xref="GeneID:6990"
                     /db_xref="HGNC:HGNC:11694"
                     /db_xref="MIM:300302"
ORIGIN      
        1 meeyhrhcde vgfnaeeahn ivkecvdgvl ggedynhnni nqwtasiveq slthlvklgk
       61 aykyivtcav vqksaygfht asscfwdtts dgtctvrwen rtmncivnvf aiaivl
//
LOCUS       NP_001355798             513 aa            linear   ROD 27-APR-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 7
            isoform 2 [Mus musculus].
ACCESSION   NP_001355798 XP_006539078
VERSION     NP_001355798.1
DBSOURCE    REFSEQ: accession NM_001368869.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606971.22.
            
            On Mar 6, 2019 this sequence version replaced XP_006539078.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849377,
                              SAMN00849378 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 81.04 cM"
     Protein         1..513
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 7 isoform 2"
                     /note="glucose transporter type 7"
                     /calculated_mol_wt=55721
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Region          26..478
                     /region_name="MFS_GLUT_Class2"
                     /note="Class 2 Glucose transporters (GLUTs) of the Major
                     Facilitator Superfamily; cd17432"
                     /db_xref="CDD:340990"
     Site            order(38,42,173,176..177,180,295..296,300..301,304..305,
                     332,394..395,398..399,403,426..427,430)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340990"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            79..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            139..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            199..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            283..303
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            352..372
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            417..437
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Site            447..467
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     Region          494..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6A1.1)"
     CDS             1..513
                     /gene="Slc2a7"
                     /gene_synonym="GLUT-7"
                     /coded_by="NM_001368869.1:86..1627"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:435818"
                     /db_xref="MGI:MGI:3650865"
ORIGIN      
        1 medkeigtpl plphsearlq ptlvlttlsa afgsvfqygy niavintphk vlksfyndth
       61 ferhgtfmde stllllwsct vsmfplggll gslvvglmvn kwgrkgtlli nnvfaitsav
      121 lmgvskvara feliilsrvl vgicagiays tlpmylgela pqnlrgalgt mtevfviigv
      181 llaqifslqa ilgnatgwpi llaltgvpav iqllslpffp esprytliek gdeetarqal
      241 rrlrgqnynv eaemeemrte erteqaegrl svlnlftfrp lrwqlisivv lmagqqlsgi
      301 navnyyadvi ytsagvdptq sqyvtlgsgv inlvmtlvsa viierlgrri lllsgyaicc
      361 saclvltval llqstapels ylsivcvfsy ivghsigpsp vpsvvrteiv lqssrtaaft
      421 vdgavhwltn fivgltfpsi qvaigaysfl vfagvcilta ayiyvvipet kgrtfveinc
      481 afakrngvef peekevatak phtpslptke taf
//
LOCUS       NP_060347                371 aa            linear   PRI 27-APR-2025
DEFINITION  solute carrier family 35 member F6 precursor [Homo sapiens].
ACCESSION   NP_060347
VERSION     NP_060347.2
DBSOURCE    REFSEQ: accession NM_017877.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Van den Bossche,F., Tevel,V., Gilis,F., Gaussin,J.F., Boonen,M. and
            Jadot,M.
  TITLE     Residence of the Nucleotide Sugar Transporter Family Members
            SLC35F1 and SLC35F6 in the Endosomal/Lysosomal Pathway
  JOURNAL   Int J Mol Sci 25 (12), 6718 (2024)
   PUBMED   38928424
  REMARK    GeneRIF: Residence of the Nucleotide Sugar Transporter Family
            Members SLC35F1 and SLC35F6 in the Endosomal/Lysosomal Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Schroder,B.A., Wrocklage,C., Hasilik,A. and Saftig,P.
  TITLE     The proteome of lysosomes
  JOURNAL   Proteomics 10 (22), 4053-4076 (2010)
   PUBMED   20957757
  REMARK    Review article
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Kashiwaya,K., Hosokawa,M., Eguchi,H., Ohigashi,H., Ishikawa,O.,
            Shinomura,Y., Nakamura,Y. and Nakagawa,H.
  TITLE     Identification of C2orf18, termed ANT2BP (ANT2-binding protein), as
            one of the key molecules involved in pancreatic carcinogenesis
  JOURNAL   Cancer Sci 100 (3), 457-464 (2009)
   PUBMED   19154410
  REMARK    GeneRIF: C2orf18, termed ANT2-binding protein (ANT2BP), might serve
            as a candidate molecular target for pancreatic cancer therapy.
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   8  (residues 1 to 371)
  AUTHORS   Ashikov,A., Routier,F., Fuhlrott,J., Helmus,Y., Wild,M.,
            Gerardy-Schahn,R. and Bakker,H.
  TITLE     The human solute carrier gene SLC35B4 encodes a bifunctional
            nucleotide sugar transporter with specificity for UDP-xylose and
            UDP-N-acetylglucosamine
  JOURNAL   J Biol Chem 280 (29), 27230-27235 (2005)
   PUBMED   15911612
REFERENCE   9  (residues 1 to 371)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011740.7 and AY358820.1.
            
            On Jun 9, 2003 this sequence version replaced NP_060347.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.85744.1,
                                           SRR1803617.250719.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344420.10/ ENSP00000345528.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..371
                     /product="solute carrier family 35 member F6 precursor"
                     /note="transmembrane protein C2orf18; ANT2-binding
                     protein; transport and golgi organization 9 homolog"
                     /calculated_mol_wt=38189
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N357.1)"
                     /calculated_mol_wt=2044
     mat_peptide     19..371
                     /product="Solute carrier family 35 member F6.
                     /id=PRO_0000232514"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
                     /calculated_mol_wt=38189
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
     Region          <101..338
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N357.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
     Site            176..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
     Site            216..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
     Site            295..312
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
     Site            317..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
     Region          352..371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N357.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N357.1)"
     CDS             1..371
                     /gene="SLC35F6"
                     /gene_synonym="ANT2BP; C2orf18; TANGO9"
                     /coded_by="NM_017877.4:67..1182"
                     /db_xref="CCDS:CCDS1728.1"
                     /db_xref="GeneID:54978"
                     /db_xref="HGNC:HGNC:26055"
                     /db_xref="MIM:619667"
ORIGIN      
        1 mawtkyqlfl aglmlvtgsi ntlsakwadn fmaegcggsk ehsfqhpflq avgmflgefs
       61 claafyllrc raagqsdssv dpqqpfnpll flppalcdmt gtslmyvaln mtsassfqml
      121 rgaviiftgl fsvaflgrrl vlsqwlgila tiaglvvvgl adllskhdsq hklsevitgd
      181 lliimaqiiv aiqmvleekf vykhnvhplr avgteglfgf vilslllvpm yyipagsfsg
      241 nprgtledal dafcqvgqqp liavallgni ssiaffnfag isvtkelsat trmvldslrt
      301 vviwalslal gweafhalqi lgflilligt alynglhrpl lgrlsrgrpl aeeseqerll
      361 ggtrtpinda s
//
LOCUS       NP_057677                469 aa            linear   PRI 27-APR-2025
DEFINITION  24-hydroxycholesterol 7-alpha-hydroxylase isoform 1 [Homo sapiens].
ACCESSION   NP_057677
VERSION     NP_057677.2
DBSOURCE    REFSEQ: accession NM_016593.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Bell,K., Ozaki,M., Mori,K., Mizoguchi,T., Nakano,S., Porporato,N.,
            Ikeda,Y., Chihara,E., Inoue,K., Manabe,S., Hayashi,K.,
            Higashide,T., Ideta,R., Tokumo,K., Kiuchi,Y., Nakano,M., Ueno,M.,
            Kinoshita,S., Tashiro,K., Sotozono,C., Inatani,M., Sugiyama,K.,
            Kubota,T., Li,Z., Wang,Z., Khor,C.C. and Aung,T.
  TITLE     Association of the CYP39A1 G204E Genetic Variant with Increased
            Risk of Glaucoma and Blindness in Patients with Exfoliation
            Syndrome
  JOURNAL   Ophthalmology 129 (4), 406-413 (2022)
   PUBMED   34763023
  REMARK    GeneRIF: Association of the CYP39A1 G204E Genetic Variant with
            Increased Risk of Glaucoma and Blindness in Patients with
            Exfoliation Syndrome.
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Li,Z., Wang,Z., Lee,M.C., Zenkel,M., Peh,E., Ozaki,M., Topouzis,F.,
            Nakano,S., Chan,A., Chen,S., Williams,S.E.I., Orr,A., Nakano,M.,
            Kobakhidze,N., Zarnowski,T., Popa-Cherecheanu,A., Mizoguchi,T.,
            Manabe,S.I., Hayashi,K., Kazama,S., Inoue,K., Mori,Y., Miyata,K.,
            Sugiyama,K., Higashide,T., Chihara,E., Ideta,R., Ishiko,S.,
            Yoshida,A., Tokumo,K., Kiuchi,Y., Ohashi,T., Sakurai,T.,
            Sugimoto,T., Chuman,H., Aihara,M., Inatani,M., Mori,K., Ikeda,Y.,
            Ueno,M., Gaston,D., Rafuse,P., Shuba,L., Saunders,J., Nicolela,M.,
            Chichua,G., Tabagari,S., Founti,P., Sim,K.S., Meah,W.Y., Soo,H.M.,
            Chen,X.Y., Chatzikyriakidou,A., Keskini,C., Pappas,T.,
            Anastasopoulos,E., Lambropoulos,A., Panagiotou,E.S.,
            Mikropoulos,D.G., Kosior-Jarecka,E., Cheong,A., Li,Y., Lukasik,U.,
            Nongpiur,M.E., Husain,R., Perera,S.A., Alvarez,L., Garcia,M.,
            Gonzalez-Iglesias,H., Fernandez-Vega Cueto,A., Fernandez-Vega
            Cueto,L., Martinon-Torres,F., Salas,A., Oguz,C., Tamcelik,N.,
            Atalay,E., Batu,B., Irkec,M., Aktas,D., Kasim,B., Astakhov,Y.S.,
            Astakhov,S.Y., Akopov,E.L., Giessl,A., Mardin,C., Hellerbrand,C.,
            Cooke Bailey,J.N., Igo,R.P. Jr., Haines,J.L., Edward,D.P.,
            Heegaard,S., Davila,S., Tan,P., Kang,J.H., Pasquale,L.R.,
            Kruse,F.E., Reis,A., Carmichael,T.R., Hauser,M., Ramsay,M.,
            Mossbock,G., Yildirim,N., Tashiro,K., Konstas,A.G.P.,
            Coca-Prados,M., Foo,J.N., Kinoshita,S., Sotozono,C., Kubota,T.,
            Dubina,M., Ritch,R., Wiggs,J.L., Pasutto,F.,
            Schlotzer-Schrehardt,U., Ho,Y.S., Aung,T., Tam,W.L. and Khor,C.C.
  CONSRTM   Genetics of Exfoliation Syndrome Partnership
  TITLE     Association of Rare CYP39A1 Variants With Exfoliation Syndrome
            Involving the Anterior Chamber of the Eye
  JOURNAL   JAMA 325 (8), 753-764 (2021)
   PUBMED   33620406
  REMARK    GeneRIF: Association of Rare CYP39A1 Variants With Exfoliation
            Syndrome Involving the Anterior Chamber of the Eye.
            Erratum:[JAMA. 2021 Apr 6;325(13):1335. doi:
            10.1001/jama.2021.3920. PMID: 33821917]
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Matsuoka,H., Katayama,M., Ohishi,A., Miya,K., Tokunaga,R.,
            Kobayashi,S., Nishimoto,Y., Hirooka,K., Shima,A. and Michihara,A.
  TITLE     Orphan Nuclear Receptor RORalpha Regulates Enzymatic Metabolism of
            Cerebral 24S-Hydroxycholesterol through CYP39A1 Intronic Response
            Element Activation
  JOURNAL   Int J Mol Sci 21 (9), 3309 (2020)
   PUBMED   32392803
  REMARK    GeneRIF: Orphan Nuclear Receptor RORalpha Regulates Enzymatic
            Metabolism of Cerebral 24S-Hydroxycholesterol through CYP39A1
            Intronic Response Element Activation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 469)
  AUTHORS   Melchardt,T., Hufnagl,C., Magnes,T., Weiss,L., Hutarew,G.,
            Neureiter,D., Schlattau,A., Moser,G., Gaggl,A., Trankenschuh,W.,
            Greil,R. and Egle,A.
  TITLE     CYP39A1 polymorphism is associated with toxicity during intensive
            induction chemotherapy in patients with advanced head and neck
            cancer
  JOURNAL   BMC Cancer 15, 725 (2015)
   PUBMED   26475344
  REMARK    GeneRIF: The CYP39A1 polymorphism rs7761731 may help to identify
            patients at high risk for treatment related toxicity.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 469)
  AUTHORS   ten Brink,M.H., van Bavel,T., Swen,J.J., van der Straaten,T.,
            Bredius,R.G., Lankester,A.C., Zwaveling,J. and Guchelaar,H.J.
  TITLE     Effect of genetic variants GSTA1 and CYP39A1 and age on busulfan
            clearance in pediatric patients undergoing hematopoietic stem cell
            transplantation
  JOURNAL   Pharmacogenomics 14 (14), 1683-1690 (2013)
   PUBMED   24192117
  REMARK    GeneRIF: GSTA1 and CYP39A1 were found to be associated with
            busulfan clearance. When combined, the two haplotypes explained 17%
            of the variability in busulfan clearance.
REFERENCE   8  (residues 1 to 469)
  AUTHORS   Fourgeux,C., Martine,L., Bjorkhem,I., Diczfalusy,U., Joffre,C.,
            Acar,N., Creuzot-Garcher,C., Bron,A. and Bretillon,L.
  TITLE     Primary open-angle glaucoma: association with cholesterol
            24S-hydroxylase (CYP46A1) gene polymorphism and plasma
            24-hydroxycholesterol levels
  JOURNAL   Invest Ophthalmol Vis Sci 50 (12), 5712-5717 (2009)
   PUBMED   19553612
  REMARK    GeneRIF: The rs754203 SNP in CYP46A1 was associated with a risk for
            POAG. This polymorphism was not associated with changes in plasma
            24S-hydroxycholesterol.
REFERENCE   9  (residues 1 to 469)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   10 (residues 1 to 469)
  AUTHORS   Li-Hawkins,J., Lund,E.G., Bronson,A.D. and Russell,D.W.
  TITLE     Expression cloning of an oxysterol 7alpha-hydroxylase selective for
            24-hydroxycholesterol
  JOURNAL   J Biol Chem 275 (22), 16543-16549 (2000)
   PUBMED   10748047
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC336695.1, AK292263.1 and
            AL035670.29.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 27, 2003 this sequence version replaced NP_057677.1.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This endoplasmic reticulum protein is involved in the conversion of
            cholesterol to bile acids. Its substrates include the oxysterols
            25-hydroxycholesterol, 27-hydroxycholesterol and
            24-hydroxycholesterol. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.156014.1,
                                           SRR1660807.231063.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000275016.3/ ENSP00000275016.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.3"
     Protein         1..469
                     /product="24-hydroxycholesterol 7-alpha-hydroxylase
                     isoform 1"
                     /EC_number="1.14.14.26"
                     /note="cytochrome P450, subfamily XXXIX (oxysterol 7
                     alpha-hydroxylase), polypeptide 1; 24-hydroxycholesterol
                     7-alpha-hydroxylase; cytochrome P450, family 39, subfamily
                     A, polypeptide 1"
                     /calculated_mol_wt=53985
     Region          49..462
                     /region_name="CYP39A1"
                     /note="cytochrome P450 family 39, subfamily A, polypeptide
                     1; cd20635"
                     /db_xref="CDD:410728"
     Site            order(96..97,100..101,115,119,250,269,272..274,277,
                     342..346,452..453)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:410728"
     Site            order(116,123,273..274,277..278,281,342,344,406..408,412,
                     414..416,419..420,454)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410728"
     Site            267..287
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYL5.2)"
     Site            352..372
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYL5.2)"
     Site            412..432
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYL5.2)"
     CDS             1..469
                     /gene="CYP39A1"
                     /coded_by="NM_016593.5:237..1646"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4916.1"
                     /db_xref="GeneID:51302"
                     /db_xref="HGNC:HGNC:17449"
                     /db_xref="MIM:605994"
ORIGIN      
        1 melisptvii ilgclalfll lqrknlrrpp cikgwipwig vgfefgkapl efiekariky
       61 gpiftvfamg nrmtfvteee ginvflkskk vdfelavqni vyrtasipkn vflalhekly
      121 imlkgkmgtv nlhqftgqlt eelheqlenl gthgtmdlnn lvrhllypvt vnmlfnkslf
      181 stnkkkikef hqyfqvyded feygsqlpec llrnwskskk wflelfekni pdikacksak
      241 dnsmtllqat ldivetetsk enspnyglll lwaslsnavp vafwtlayvl shpdihkaim
      301 egissvfgka gkdkikvsed dlenlllikw cvletirlka pgvitrkvvk pveilnyiip
      361 sgdllmlspf wlhrnpkyfp epelfkperw kkanlekhsf ldcfmafgsg kfqcparwfa
      421 llevqmciil ilykydcsll dplpkqsylh lvgvpqpegq crieykqri
//
LOCUS       NP_005565                227 aa            linear   PRI 27-APR-2025
DEFINITION  rhombotin-2 isoform 1 [Homo sapiens].
ACCESSION   NP_005565
VERSION     NP_005565.2
DBSOURCE    REFSEQ: accession NM_005574.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Ge,J., Yue,Y., Nie,H.Y., Liu,K.G., Li,H., Lin,H.G., Zhang,T.,
            Yan,H.F., Sun,H.W., Yang,J.W., Zhou,J.L. and Cui,Y.
  TITLE     Simulated microgravity altered the gene expression profiles and
            inhibited the proliferation of Kupffer cells in the early phase by
            downregulating LMO2 and EZH2
  JOURNAL   Life Sci Space Res (Amst) 40, 21-34 (2024)
   PUBMED   38245345
  REMARK    GeneRIF: Simulated microgravity altered the gene expression
            profiles and inhibited the proliferation of Kupffer cells in the
            early phase by downregulating LMO2 and EZH2.
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Berker,N., Yegen,G., Ozluk,Y. and Dogan,O.
  TITLE     Value of GCET1, HGAL (GCET2), and LMO2 in the Determination of
            Germinal Center Phenotype in Diffuse Large B-cell Lymphoma
  JOURNAL   Turk J Haematol 40 (3), 162-173 (2023)
   PUBMED   37519110
  REMARK    GeneRIF: Value of GCET1, HGAL (GCET2), and LMO2 in the
            Determination of Germinal Center Phenotype in Diffuse Large B-cell
            Lymphoma.
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Lu,L., Wang,J., Fang,F., Guo,A., Jiang,S., Tao,Y., Zhang,Y., Li,Y.,
            Zhang,K., Zhang,Z., Zhuo,R., Chu,X., Li,X., Tian,Y., Ma,L.,
            Sang,X., Chen,Y., Yu,J., Yang,Y., Cao,H., Gao,J., Lu,J., Hu,S.,
            Pan,J. and He,H.
  TITLE     LMO2 promotes the development of AML through interaction with
            transcription co-regulator LDB1
  JOURNAL   Cell Death Dis 14 (8), 518 (2023)
   PUBMED   37573405
  REMARK    GeneRIF: LMO2 promotes the development of AML through interaction
            with transcription co-regulator LDB1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Wang,H., Wang,J., Li,R. and Zhu,Z.
  TITLE     Potential link of single nucleotide polymorphisms within LMO2 to
            the risk of cervical squamous-cell carcinoma in Chinese populations
  JOURNAL   Asian J Surg 46 (2), 1139-1141 (2023)
   PUBMED   35999096
  REMARK    GeneRIF: Potential link of single nucleotide polymorphisms within
            LMO2 to the risk of cervical squamous-cell carcinoma in Chinese
            populations.
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Pan,X., Liu,D., Ying,M., Zheng,G., Fan,C., Pan,F. and Ke,Q.
  TITLE     PAK5 is a potential target in myelodysplastic syndrome through
            interacting with LMO2 and GATA1
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 68 (9), 77-85 (2022)
   PUBMED   36905268
  REMARK    GeneRIF: PAK5 is a potential target in myelodysplastic syndrome
            through interacting with LMO2 and GATA1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Dong,W.F., Xu,Y., Hu,Q.L., Munroe,D., Minowada,J., Housman,D.E. and
            Minden,M.D.
  TITLE     Molecular characterization of a chromosome translocation breakpoint
            t(11;14)(p13;q11) from the cell line KOPT-K1
  JOURNAL   Leukemia 9 (11), 1812-1817 (1995)
   PUBMED   7475267
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Osada,H., Grutz,G., Axelson,H., Forster,A. and Rabbitts,T.H.
  TITLE     Association of erythroid transcription factors: complexes involving
            the LIM protein RBTN2 and the zinc-finger protein GATA1
  JOURNAL   Proc Natl Acad Sci U S A 92 (21), 9585-9589 (1995)
   PUBMED   7568177
REFERENCE   8  (residues 1 to 227)
  AUTHORS   Royer-Pokora,B., Loos,U. and Ludwig,W.D.
  TITLE     TTG-2, a new gene encoding a cysteine-rich protein with the LIM
            motif, is overexpressed in acute T-cell leukaemia with the
            t(11;14)(p13;q11)
  JOURNAL   Oncogene 6 (10), 1887-1893 (1991)
   PUBMED   1923511
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Boehm,T., Foroni,L., Kaneko,Y., Perutz,M.F. and Rabbitts,T.H.
  TITLE     The rhombotin family of cysteine-rich LIM-domain oncogenes:
            distinct members are involved in T-cell translocations to human
            chromosomes 11p15 and 11p13
  JOURNAL   Proc Natl Acad Sci U S A 88 (10), 4367-4371 (1991)
   PUBMED   2034676
REFERENCE   10 (residues 1 to 227)
  AUTHORS   Boehm,T., Spillantini,M.G., Sofroniew,M.V., Surani,M.A. and
            Rabbitts,T.H.
  TITLE     Developmentally regulated and tissue specific expression of mRNAs
            encoding the two alternative forms of the LIM domain oncogene
            rhombotin: evidence for thymus expression
  JOURNAL   Oncogene 6 (5), 695-703 (1991)
   PUBMED   2052354
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X61118.1, CN355348.1,
            AC132216.7 and AC113192.3.
            
            On Nov 26, 2008 this sequence version replaced NP_005565.1.
            
            Summary: LMO2 encodes a cysteine-rich, two LIM-domain protein that
            is required for yolk sac erythropoiesis. The LMO2 protein has a
            central and crucial role in hematopoietic development and is highly
            conserved. The LMO2 transcription start site is located
            approximately 25 kb downstream from the 11p13 T-cell translocation
            cluster (11p13 ttc), where a number T-cell acute lymphoblastic
            leukemia-specific translocations occur. Alternative splicing
            results in multiple transcript variants encoding different
            isoforms.[provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X61118.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257818.3/ ENSP00000257818.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..227
                     /product="rhombotin-2 isoform 1"
                     /note="T-cell translocation gene 2; rhombotin-like 1;
                     rhombotin-2; LIM domain only protein 2; cysteine-rich
                     protein TTG-2; T-cell translocation protein 2"
                     /calculated_mol_wt=24905
     Region          99..154
                     /region_name="LIM1_LMO2"
                     /note="The first LIM domain of LMO2 (LIM domain only
                     protein 2); cd09384"
                     /db_xref="CDD:188770"
     Site            order(99,102,120,123,126,129,149,152)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188770"
     Region          163..218
                     /region_name="LIM2_LMO2"
                     /note="The second LIM domain of LMO2 (LIM domain only
                     protein 2); cd09385"
                     /db_xref="CDD:188771"
     Site            order(163,166,185,188,191,194,213,216)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188771"
     CDS             1..227
                     /gene="LMO2"
                     /gene_synonym="LMO-2; RBTN2; RBTNL1; RHOM2; TTG2"
                     /coded_by="NM_005574.4:618..1301"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7888.2"
                     /db_xref="GeneID:4005"
                     /db_xref="HGNC:HGNC:6642"
                     /db_xref="MIM:180385"
ORIGIN      
        1 megsavtvle rggasspaer rskrrrrsgg dggggggara pegvrapaag qpratkgapp
       61 ppgtpppspm ssaierksld pseepvdevl qippslltcg gcqqnigdry flkaidqywh
      121 edclscdlcg crlgevgrrl yyklgrklcr rdylrlfgqd glcascdkri rayemtmrvk
      181 dkvyhlecfk caacqkhfcv gdryllinsd ivceqdiyew tkingmi
//
LOCUS       NP_001356866             643 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001356866
VERSION     NP_001356866.1
DBSOURCE    REFSEQ: accession NM_001369937.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.140393.1,
                                           SRR1803617.29975.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..643
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 9"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=73067
     Region          355..394
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..643
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369937.1:262..2193"
                     /note="isoform 9 is encoded by transcript variant 20"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mqkrlhrsvf ltflrmsthk eskdhfisps afgeilynnf lfdipkildl cvlfgkgnsp
       61 llqkmignif tqqpsyysdl detlptilqv fsnilqhcgl qgdganttpq kleergrltp
      121 sdmpllelkd ivlylcdtct tlwafldifp lacqtfqkhd fcyrlasfye aaipemesai
      181 kkrrledskl lgdlwqrlsh srkklmeifh iilnqicllp ilesscdniq gfieeflqif
      241 ssllqekrfl rdydalfpva edisllqqas svldetrtay ilqavesawe gvdrrkatda
      301 kdpsvieepn gepngvtvta eavsqasshp enseeeecmg aaaavgpamc gveldslisq
      361 vkdllpdlge gfilacleyy hydpeqvinn ileerlaptl sqldrnldre mkpdptpllt
      421 srhnvfqnde fdvfsrdsvd lsrvhkgkst rkeentrsll ndkravaaqr qryeqysvvv
      481 eevplqpges lpyhsvyyed eyddtydgnq vgandadsdd elisrrpfti pqvlrtkvpr
      541 egqeedddde eddadeeapk pdhfvqdpav lrekaearrm aflakkgyrh dsstavagsp
      601 rghgqsrett qerrkkeank atranhnrrt madrkrskgm ips
//
LOCUS       NP_001291892             164 aa            linear   PRI 27-APR-2025
DEFINITION  diphosphoinositol polyphosphate phosphohydrolase 3-alpha [Homo
            sapiens].
ACCESSION   NP_001291892 XP_005262099
VERSION     NP_001291892.1
DBSOURCE    REFSEQ: accession NM_001304963.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Chen,D., Zhang,R., Xie,A., Yuan,J., Zhang,J., Huang,Y., Zhang,H.
            and Zhang,F.
  TITLE     Clinical correlations and prognostic value of Nudix hydroxylase 10
            in patients with gastric cancer
  JOURNAL   Bioengineered 12 (2), 9779-9789 (2021)
   PUBMED   34696672
  REMARK    GeneRIF: Clinical correlations and prognostic value of Nudix
            hydroxylase 10 in patients with gastric cancer.
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Chang,B.L., Spangler,E., Gallagher,S., Haiman,C.A., Henderson,B.,
            Isaacs,W., Benford,M.L., Kidd,L.R., Cooney,K., Strom,S.,
            Ingles,S.A., Stern,M.C., Corral,R., Joshi,A.D., Xu,J., Giri,V.N.,
            Rybicki,B., Neslund-Dudas,C., Kibel,A.S., Thompson,I.M.,
            Leach,R.J., Ostrander,E.A., Stanford,J.L., Witte,J., Casey,G.,
            Eeles,R., Hsing,A.W., Chanock,S., Hu,J.J., John,E.M., Park,J.,
            Stefflova,K., Zeigler-Johnson,C. and Rebbeck,T.R.
  TITLE     Validation of genome-wide prostate cancer associations in men of
            African descent
  JOURNAL   Cancer Epidemiol Biomarkers Prev 20 (1), 23-32 (2011)
   PUBMED   21071540
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Kim,S.T., Cheng,Y., Hsu,F.C., Jin,T., Kader,A.K., Zheng,S.L.,
            Isaacs,W.B., Xu,J. and Sun,J.
  TITLE     Prostate cancer risk-associated variants reported from genome-wide
            association studies: meta-analysis and their contribution to
            genetic Variation
  JOURNAL   Prostate 70 (16), 1729-1738 (2010)
   PUBMED   20564319
  REMARK    GeneRIF: Meta-analysis of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Gudmundsson,J., Sulem,P., Rafnar,T., Bergthorsson,J.T.,
            Manolescu,A., Gudbjartsson,D., Agnarsson,B.A., Sigurdsson,A.,
            Benediktsdottir,K.R., Blondal,T., Jakobsdottir,M., Stacey,S.N.,
            Kostic,J., Kristinsson,K.T., Birgisdottir,B., Ghosh,S.,
            Magnusdottir,D.N., Thorlacius,S., Thorleifsson,G., Zheng,S.L.,
            Sun,J., Chang,B.L., Elmore,J.B., Breyer,J.P., McReynolds,K.M.,
            Bradley,K.M., Yaspan,B.L., Wiklund,F., Stattin,P., Lindstrom,S.,
            Adami,H.O., McDonnell,S.K., Schaid,D.J., Cunningham,J.M., Wang,L.,
            Cerhan,J.R., St Sauver,J.L., Isaacs,S.D., Wiley,K.E., Partin,A.W.,
            Walsh,P.C., Polo,S., Ruiz-Echarri,M., Navarrete,S., Fuertes,F.,
            Saez,B., Godino,J., Weijerman,P.C., Swinkels,D.W., Aben,K.K.,
            Witjes,J.A., Suarez,B.K., Helfand,B.T., Frigge,M.L.,
            Kristjansson,K., Ober,C., Jonsson,E., Einarsson,G.V., Xu,J.,
            Gronberg,H., Smith,J.R., Thibodeau,S.N., Isaacs,W.B.,
            Catalona,W.J., Mayordomo,J.I., Kiemeney,L.A., Barkardottir,R.B.,
            Gulcher,J.R., Thorsteinsdottir,U., Kong,A. and Stefansson,K.
  TITLE     Common sequence variants on 2p15 and Xp11.22 confer susceptibility
            to prostate cancer
  JOURNAL   Nat Genet 40 (3), 281-283 (2008)
   PUBMED   18264098
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Eeles,R.A., Kote-Jarai,Z., Giles,G.G., Olama,A.A., Guy,M.,
            Jugurnauth,S.K., Mulholland,S., Leongamornlert,D.A., Edwards,S.M.,
            Morrison,J., Field,H.I., Southey,M.C., Severi,G., Donovan,J.L.,
            Hamdy,F.C., Dearnaley,D.P., Muir,K.R., Smith,C., Bagnato,M.,
            Ardern-Jones,A.T., Hall,A.L., O'Brien,L.T., Gehr-Swain,B.N.,
            Wilkinson,R.A., Cox,A., Lewis,S., Brown,P.M., Jhavar,S.G.,
            Tymrakiewicz,M., Lophatananon,A., Bryant,S.L., Horwich,A.,
            Huddart,R.A., Khoo,V.S., Parker,C.C., Woodhouse,C.J., Thompson,A.,
            Christmas,T., Ogden,C., Fisher,C., Jamieson,C., Cooper,C.S.,
            English,D.R., Hopper,J.L., Neal,D.E. and Easton,D.F.
  CONSRTM   UK Genetic Prostate Cancer Study Collaborators; British Association
            of Urological Surgeons' Section of Oncology; UK ProtecT Study
            Collaborators
  TITLE     Multiple newly identified loci associated with prostate cancer
            susceptibility
  JOURNAL   Nat Genet 40 (3), 316-321 (2008)
   PUBMED   18264097
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Fisher,D.I., Safrany,S.T., Strike,P., McLennan,A.G. and
            Cartwright,J.L.
  TITLE     Nudix hydrolases that degrade dinucleoside and diphosphoinositol
            polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP)
            pyrophosphatase activity that generates the glycolytic activator
            ribose 1,5-bisphosphate
  JOURNAL   J Biol Chem 277 (49), 47313-47317 (2002)
   PUBMED   12370170
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Hidaka,K., Caffrey,J.J., Hua,L., Zhang,T., Falck,J.R., Nickel,G.C.,
            Carrel,L., Barnes,L.D. and Shears,S.B.
  TITLE     An adjacent pair of human NUDT genes on chromosome X are
            preferentially expressed in testis and encode two new isoforms of
            diphosphoinositol polyphosphate phosphohydrolase
  JOURNAL   J Biol Chem 277 (36), 32730-32738 (2002)
   PUBMED   12105228
  REMARK    GeneRIF: The NUDT10 gene, located on chromosome X, is
            preferentially expressed in the testis
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Leslie,N.R., McLennan,A.G. and Safrany,S.T.
  TITLE     Cloning and characterisation of hAps1 and hAps2, human diadenosine
            polyphosphate-metabolising Nudix hydrolases
  JOURNAL   BMC Biochem 3, 20 (2002)
   PUBMED   12121577
  REMARK    GeneRIF: Cloning and characterisation of NUDT10 as a diadenosine
            polyphosphate-metabolising Nudix hydrolase.
            Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX449265.2, BC050700.1,
            CN399689.1 and BC049383.1.
            
            On Feb 12, 2015 this sequence version replaced XP_005262099.1.
            
            Summary: This gene is a member of the nudix (nucleoside diphosphate
            linked moiety X)-type motif containing family. The encoded protein
            is a phosphohydrolase and may regulate the turnover of
            diphosphoinositol polyphosphates. The turnover of these high-energy
            diphosphoinositol polyphosphates represents a molecular switching
            activity with important regulatory consequences. Molecular
            switching by diphosphoinositol polyphosphates may contribute to the
            regulation of intracellular trafficking. In some populations
            putative prostate cancer susceptibility alleles have been
            identified for this gene. Alternatively spliced transcript
            variants, which differ only in the 5' UTR, have been found for this
            gene. [provided by RefSeq, Feb 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.746620.1,
                                           SRR3476690.1132745.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356450.3/ ENSP00000348831.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..164
                     /product="diphosphoinositol polyphosphate phosphohydrolase
                     3-alpha"
                     /EC_number="3.6.1.52"
                     /EC_number="3.6.1.60"
                     /note="nudix motif 10; nucleoside diphosphate-linked
                     moiety X motif 10; diadenosine 5',5'''-P1,P6-hexaphosphate
                     hydrolase 3-alpha; diadenosine hexaphosphate hydrolase
                     (AMP-forming); nudix (nucleoside diphosphate linked moiety
                     X)-type motif 10"
                     /calculated_mol_wt=18369
     Region          18..143
                     /region_name="NUDIX_DIPP2_like_Nudt4"
                     /note="diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase
                     type 2 and similar proteins; cd04666"
                     /db_xref="CDD:467551"
     Region          50..71
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFP7.1)"
     Region          144..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFP7.1)"
     CDS             1..164
                     /gene="NUDT10"
                     /gene_synonym="APS2; DIPP3-alpha; DIPP3a"
                     /coded_by="NM_001304963.2:145..639"
                     /db_xref="CCDS:CCDS35278.1"
                     /db_xref="GeneID:170685"
                     /db_xref="HGNC:HGNC:17621"
                     /db_xref="MIM:300527"
ORIGIN      
        1 mkckpnqtrt ydpegfkkra aclcfrsere devllvsssr ypdrwivpgg gmepeeepgg
       61 aavrevyeea gvkgklgrll gvfeqnqdpk hrtyvyvltv telledweds vsigrkrewf
      121 kvedaikvlq chkpvhaeyl eklklggspt ngnsmapssp dsdp
//
LOCUS       NP_861448                914 aa            linear   PRI 27-APR-2025
DEFINITION  protein O-mannosyl-transferase TMTC3 isoform 1 [Homo sapiens].
ACCESSION   NP_861448
VERSION     NP_861448.2
DBSOURCE    REFSEQ: accession NM_181783.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Yuan,H., Zhao,Z., Guo,Z., Ma,L., Han,J. and Song,Y.
  TITLE     A Novel ER Stress Mediator TMTC3 Promotes Squamous Cell Carcinoma
            Progression by Activating GRP78/PERK Signaling Pathway
  JOURNAL   Int J Biol Sci 18 (13), 4853-4868 (2022)
   PUBMED   35982901
  REMARK    GeneRIF: A Novel ER Stress Mediator TMTC3 Promotes Squamous Cell
            Carcinoma Progression by Activating GRP78/PERK Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Biyik,I., Kalkan,U. and Simsek,S.
  TITLE     The deep infiltrating endometriosis tissue has lower T-cadherin,
            E-cadherin, progesterone receptor and oestrogen receptor than
            endometrioma tissue
  JOURNAL   Taiwan J Obstet Gynecol 60 (6), 1059-1065 (2021)
   PUBMED   34794738
  REMARK    GeneRIF: The deep infiltrating endometriosis tissue has lower
            T-cadherin, E-cadherin, progesterone receptor and oestrogen
            receptor than endometrioma tissue.
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Eisenhaber,B., Sinha,S., Jadalanki,C.K., Shitov,V.A., Tan,Q.W.,
            Sirota,F.L. and Eisenhaber,F.
  TITLE     Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4,
            new O-mannosyltransferases from the GT-C/PMT clan, are rationalized
            as ligand binding sites
  JOURNAL   Biol Direct 16 (1), 4 (2021)
   PUBMED   33436046
  REMARK    GeneRIF: Conserved sequence motifs in human TMTC1, TMTC2, TMTC3,
            and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are
            rationalized as ligand binding sites.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 914)
  AUTHORS   Larsen,I.S.B., Narimatsu,Y., Joshi,H.J., Siukstaite,L.,
            Harrison,O.J., Brasch,J., Goodman,K.M., Hansen,L., Shapiro,L.,
            Honig,B., Vakhrushev,S.Y., Clausen,H. and Halim,A.
  TITLE     Discovery of an O-mannosylation pathway selectively serving
            cadherins and protocadherins
  JOURNAL   Proc Natl Acad Sci U S A 114 (42), 11163-11168 (2017)
   PUBMED   28973932
  REMARK    GeneRIF: O-mannosylation pathway dedicated to cadherins/
            protocadherins orchestrated by the four TMTC1-4 genes
REFERENCE   5  (residues 1 to 914)
  AUTHORS   Jerber,J., Zaki,M.S., Al-Aama,J.Y., Rosti,R.O., Ben-Omran,T.,
            Dikoglu,E., Silhavy,J.L., Caglar,C., Musaev,D., Albrecht,B.,
            Campbell,K.P., Willer,T., Almuriekhi,M., Caglayan,A.O., Vajsar,J.,
            Bilguvar,K., Ogur,G., Abou Jamra,R., Gunel,M. and Gleeson,J.G.
  TITLE     Biallelic Mutations in TMTC3, Encoding a Transmembrane and
            TPR-Containing Protein, Lead to Cobblestone Lissencephaly
  JOURNAL   Am J Hum Genet 99 (5), 1181-1189 (2016)
   PUBMED   27773428
REFERENCE   6  (residues 1 to 914)
  AUTHORS   Goldstein,J.I., Jarskog,L.F., Hilliard,C., Alfirevic,A., Duncan,L.,
            Fourches,D., Huang,H., Lek,M., Neale,B.M., Ripke,S., Shianna,K.,
            Szatkiewicz,J.P., Tropsha,A., van den Oord,E.J., Cascorbi,I.,
            Dettling,M., Gazit,E., Goff,D.C., Holden,A.L., Kelly,D.L.,
            Malhotra,A.K., Nielsen,J., Pirmohamed,M., Rujescu,D., Werge,T.,
            Levy,D.L., Josiassen,R.C., Kennedy,J.L., Lieberman,J.A., Daly,M.J.
            and Sullivan,P.F.
  TITLE     Clozapine-induced agranulocytosis is associated with rare HLA-DQB1
            and HLA-B alleles
  JOURNAL   Nat Commun 5, 4757 (2014)
   PUBMED   25187353
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 914)
  AUTHORS   Yun,E.J. and Vu,T.H.
  TITLE     mSmile is necessary for bronchial smooth muscle and alveolar
            myofibroblast development
  JOURNAL   Anat Rec (Hoboken) 295 (1), 167-176 (2012)
   PUBMED   21956870
  REMARK    GeneRIF: SMILE is a novel transgene specifying both bronchial
            smooth muscle and lung alveolar myofibroblast lineages,
            contributing to the understanding of the biological control of the
            development of these cells.
REFERENCE   8  (residues 1 to 914)
  AUTHORS   Racape,M., Duong Van Huyen,J.P., Danger,R., Giral,M., Bleicher,F.,
            Foucher,Y., Pallier,A., Pilet,P., Tafelmeyer,P., Ashton-Chess,J.,
            Dugast,E., Pettre,S., Charreau,B., Soulillou,J.P. and Brouard,S.
  TITLE     The involvement of SMILE/TMTC3 in endoplasmic reticulum stress
            response
  JOURNAL   PLoS One 6 (5), e19321 (2011)
   PUBMED   21603654
  REMARK    GeneRIF: that SMILE is involved in the endoplasmic reticulum stress
            response, by modulating proteasome activity and XBP-1 transcript
            expression. This function of SMILE may influence immune cell
            behavior in the context of transplantation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290436.1, BX538169.1,
            BC117175.1, CR749309.1, CR933632.1, BG287027.1 and CR737828.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 11, 2009 this sequence version replaced NP_861448.1.
            
            Summary: This gene encodes a protein that belongs to the
            transmembrane and tetratricopeptide repeat-containing protein
            family. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.255540.1,
                                           SRR1660807.161222.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000266712.11/ ENSP00000266712.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.32"
     Protein         1..914
                     /product="protein O-mannosyl-transferase TMTC3 isoform 1"
                     /EC_number="2.4.1.109"
                     /note="transmembrane and TPR repeat-containing protein 3;
                     protein O-mannosyl-transferase TMTC3; transmembrane and
                     tetratricopeptide repeat containing 3"
                     /calculated_mol_wt=103750
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            121..139
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            140..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            194..214
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          258..331
                     /region_name="TMTC_DUF1736"
                     /note="Protein O-mannosyl-transferase TMTC, DUF1736;
                     pfam08409"
                     /db_xref="CDD:462468"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            354..374
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            377..397
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            405..423
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          439..668
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          446..479
                     /region_name="TPR 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          446..474
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          479..523
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          480..513
                     /region_name="TPR 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            494
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          529..562
                     /region_name="TPR 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          530..557
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(532..533,536,538,540,564,567..568,571..572,574..575,
                     598,601..602,605..606,609)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Site            541
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          562..592
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          563..596
                     /region_name="TPR 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          566..802
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          597..625
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          668..701
                     /region_name="TPR 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          668..696
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          701..731
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          702..735
                     /region_name="TPR 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          736..765
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          737..770
                     /region_name="TPR 8.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          771..804
                     /region_name="TPR 9.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Region          771..799
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          847..891
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     Site            864
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q6ZXV5.2)"
     CDS             1..914
                     /gene="TMTC3"
                     /gene_synonym="LIS8; SMILE"
                     /coded_by="NM_181783.4:210..2954"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9032.1"
                     /db_xref="GeneID:160418"
                     /db_xref="HGNC:HGNC:26899"
                     /db_xref="MIM:617218"
ORIGIN      
        1 maninlkeit livgvvtacy wnslfcgfvf ddvsaildnk dlhpstplkt lfqndfwgtp
       61 mseershksy rpltvltfrl nyllselkpm syhllnmifh avvsviflkv cklfldnkss
      121 viasllfavh pihteavtgv vgraellssi fflaaflsyt rskgpdnsii wtpialtvfl
      181 vavatlckeq gitvvgiccv yevfiaqgyt lpllcttagq flrgkgsipf smlqtlvkli
      241 vlmfstlllv virvqviqsq lpvftrfdnp aavsptptrq ltfnyllpvn awlllnpsel
      301 ccdwtmgtip lieslldirn latftffcfl gmlgvfsiry sgdssktvlm alclmalpfi
      361 pasnlffpvg fvvaervlyv psmgfcilva hgwqkistks vfkklswicl smvilthslk
      421 tfhrnwdwes eytlfmsalk vnknnaklwn nvghalenek nferalkyfl qathvqpddi
      481 gahmnvgrty knlnrtkeae esymmakslm pqiipgkkya ariapnhlnv yinlanlira
      541 nesrleeadq lyrqaismrp dfkqayisrg elllkmnkpl kakeaylkal eldrnnadlw
      601 ynlaivhiel kepnealknf nralelnpkh klalfnsaiv mqesgevklr pearkrllsy
      661 ineepldang yfnlgmlamd dkkdneaeiw mkkaiklqad frsalfnlal lysqtakelk
      721 alpileellr yypdhikgli lkgdilmnqk kdilgakkcf erilemdpsn vqgkhnlcvv
      781 yfeekdllka erclletlal apheeyiqrh lnivrdkiss ssfiepifpt skissvegkk
      841 iptesvkeir gesrqtqivk tsdnksqsks nkqlgkngde etphkttkdi keiekkrvaa
      901 lkrleeieri lnge
//
LOCUS       NP_001180431             167 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor 24 [Homo sapiens].
ACCESSION   NP_001180431 XP_001715573 XP_001715613 XP_001732882
VERSION     NP_001180431.1
DBSOURCE    REFSEQ: accession NM_001193502.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 167)
  AUTHORS   McLellan,A.S., Langlands,K. and Kealey,T.
  TITLE     Exhaustive identification of human class II basic helix-loop-helix
            proteins by virtual library screening
  JOURNAL   Mech Dev 119 Suppl 1, S285-S291 (2002)
   PUBMED   14516699
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC110998.4, AW028708.1 and CX788264.1.
            
            On or before Jul 31, 2010 this sequence version replaced
            XP_001715573.2, XP_001715613.2, XP_001732882.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: CX788264.1, SRR12514507.445108.1
                                    [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA1968968,
                                    SAMEA1970526 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000563496.2/ ENSP00000455444.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..167
                     /product="transcription factor 24"
                     /calculated_mol_wt=17385
     Region          1..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTU0.3)"
     Region          51..105
                     /region_name="bHLH_TS_TCF24"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 24 (TCF-24) and similar proteins;
                     cd19710"
                     /db_xref="CDD:381553"
     Site            order(51,55,57..59,61,66,84..87)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381553"
     Site            order(64..65,68..69,71..72,88,91,95,97..98,102,104..105)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381553"
     CDS             1..167
                     /gene="TCF24"
                     /gene_synonym="bHLHa25; TCF-24"
                     /coded_by="NM_001193502.2:398..901"
                     /db_xref="CCDS:CCDS59103.1"
                     /db_xref="GeneID:100129654"
                     /db_xref="HGNC:HGNC:32275"
ORIGIN      
        1 mdrgrpagsp lsasaepapl aaairdsrpg rtgpgpagpg ggsrsgsgrp aaanaarers
       61 rvqtlrhafl elqrtlpsvp pdtklskldv lllattyiah ltrslqddae apadaglgal
      121 rgdgylhpvk kwpmrsrlyi gatgqflkhs vsgektnhdn tptdsqp
//
LOCUS       NP_001317517            1262 aa            linear   PRI 27-APR-2025
DEFINITION  tripeptidyl-peptidase 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001317517 XP_005254129
VERSION     NP_001317517.1
DBSOURCE    REFSEQ: accession NM_001330588.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1262)
  AUTHORS   Liao,C.L., Hu,R.C., Liao,M.S., Chen,Y.J., Chen,Y.P., Hsieh,H.H.,
            Tai,C.H., Chou,T.C., Chu,C.Y., Chen,Y.J., Lo,L.C. and Lin,J.J.
  TITLE     Unveiling a novel serpinB2-tripeptidyl peptidase II signaling axis
            during senescence
  JOURNAL   J Cell Sci 135 (10) (2022)
   PUBMED   35466366
  REMARK    GeneRIF: Unveiling a novel serpinB2-tripeptidyl peptidase II
            signaling axis during senescence.
REFERENCE   2  (residues 1 to 1262)
  AUTHORS   Atallah,I., Quinodoz,M., Campos-Xavier,B., Peter,V.G., Fouriki,A.,
            Bonvin,C., Bottani,A., Kumps,C., Angelini,F., Bellutti Enders,F.,
            Christen-Zaech,S., Rizzi,M., Renella,R., Beck-Popovic,M.,
            Poloni,C., Frossard,V., Blouin,J.L., Rivolta,C., Riccio,O.,
            Candotti,F., Hofer,M., Unger,S. and Superti-Furga,A.
  TITLE     Immune deficiency, autoimmune disease and intellectual disability:
            A pleiotropic disorder caused by biallelic variants in the TPP2
            gene
  JOURNAL   Clin Genet 99 (6), 780-788 (2021)
   PUBMED   33586135
  REMARK    GeneRIF: Immune deficiency, autoimmune disease and intellectual
            disability: A pleiotropic disorder caused by biallelic variants in
            the TPP2 gene.
REFERENCE   3  (residues 1 to 1262)
  AUTHORS   Lindas,A.C. and Tomkinson,B.
  TITLE     Characterization of the promoter of the gene encoding human
            tripeptidyl-peptidase II and identification of upstream silencer
            elements
  JOURNAL   Gene 393 (1-2), 62-69 (2007)
   PUBMED   17343995
  REMARK    GeneRIF: This investigation reveals that TPP II expression could be
            regulated through both positive and negative regulatory elements.
REFERENCE   4  (residues 1 to 1262)
  AUTHORS   York,I.A., Bhutani,N., Zendzian,S., Goldberg,A.L. and Rock,K.L.
  TITLE     Tripeptidyl peptidase II is the major peptidase needed to trim long
            antigenic precursors, but is not required for most MHC class I
            antigen presentation
  JOURNAL   J Immunol 177 (3), 1434-1443 (2006)
   PUBMED   16849449
  REMARK    GeneRIF: TPP2 plays a specialized role in antigen processing and
            one that is not essential for the generation of most presented
            peptides.
REFERENCE   5  (residues 1 to 1262)
  AUTHORS   Lindas,A.C. and Tomkinson,B.
  TITLE     Identification and characterization of the promoter for the gene
            encoding human tripeptidyl-peptidase II
  JOURNAL   Gene 345 (2), 249-257 (2005)
   PUBMED   15716107
  REMARK    GeneRIF: the promoter could be localized to a 215 bp fragment
            upstream of the initiation codon.
REFERENCE   6  (residues 1 to 1262)
  AUTHORS   Geier,E., Pfeifer,G., Wilm,M., Lucchiari-Hartz,M., Baumeister,W.,
            Eichmann,K. and Niedermann,G.
  TITLE     A giant protease with potential to substitute for some functions of
            the proteasome
  JOURNAL   Science 283 (5404), 978-981 (1999)
   PUBMED   9974389
REFERENCE   7  (residues 1 to 1262)
  AUTHORS   Tomkinson,B. and Jonsson,A.K.
  TITLE     Characterization of cDNA for human tripeptidyl peptidase II: the
            N-terminal part of the enzyme is similar to subtilisin
  JOURNAL   Biochemistry 30 (1), 168-174 (1991)
   PUBMED   1670990
REFERENCE   8  (residues 1 to 1262)
  AUTHORS   Tomkinson,B.
  TITLE     Nucleotide sequence of cDNA covering the N-terminus of human
            tripeptidyl peptidase II
  JOURNAL   Biomed Biochim Acta 50 (4-6), 727-729 (1991)
   PUBMED   1840501
REFERENCE   9  (residues 1 to 1262)
  AUTHORS   Tomkinson,B. and Zetterqvist,O.
  TITLE     Immunological cross-reactivity between human tripeptidyl peptidase
            II and fibronectin
  JOURNAL   Biochem J 267 (1), 149-154 (1990)
   PUBMED   1691635
REFERENCE   10 (residues 1 to 1262)
  AUTHORS   Tomkinson,B., Wernstedt,C., Hellman,U. and Zetterqvist,O.
  TITLE     Active site of tripeptidyl peptidase II from human erythrocytes is
            of the subtilisin type
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7508-7512 (1987)
   PUBMED   3313395
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU132468.1, BC039905.1,
            M73047.1, BX370108.2, BF514671.1, N27441.1, DB303355.1 and
            BM684792.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 27, 2016 this sequence version replaced XP_005254129.1.
            
            Summary: This gene encodes a mammalian peptidase that, at neutral
            pH, removes tripeptides from the N terminus of longer peptides. The
            protein has a specialized function that is essential for some MHC
            class I antigen presentation. The protein is a high molecular mass
            serine exopeptidase; the amino acid sequence surrounding the serine
            residue at the active site is similar to the peptidases of the
            subtilisin class rather than the trypsin class. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) contains an alternate in-frame
            exon in the 3' coding region, compared to variant 1. The encoded
            isoform (2) has the same N- and C-termini, but is longer than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.71142.1,
                                           SRR1803617.222348.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376052.5/ ENSP00000365220.3
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q33.1"
     Protein         1..1262
                     /product="tripeptidyl-peptidase 2 isoform 2"
                     /EC_number="3.4.14.10"
                     /note="tripeptidyl-peptidase II; tripeptidyl
                     aminopeptidase"
                     /calculated_mol_wt=139635
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6;
                     propagated from UniProtKB/Swiss-Prot (P29144.4)"
     Region          14..489
                     /region_name="Peptidases_S8_Tripeptidyl_Aminopeptidase_II"
                     /note="Peptidase S8 family domain in Tripeptidyl
                     aminopeptidases_II; cd04857"
                     /db_xref="CDD:173796"
     Site            order(44,264,449)
                     /site_type="active"
                     /note="putative catalytic triad [active]"
                     /db_xref="CDD:173796"
     Site            order(190,264,328..330,362,449)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:173796"
     Site            401
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q64514; propagated from
                     UniProtKB/Swiss-Prot (P29144.4)"
     Region          777..963
                     /region_name="TPPII"
                     /note="Tripeptidyl peptidase II; pfam12580"
                     /db_xref="CDD:463636"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P29144.4)"
     Region          1011..1031
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29144.4)"
     CDS             1..1262
                     /gene="TPP2"
                     /gene_synonym="IMD78; TPP-2; TPP-II; TPPII"
                     /coded_by="NM_001330588.2:54..3842"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS81777.1"
                     /db_xref="GeneID:7174"
                     /db_xref="HGNC:HGNC:12016"
                     /db_xref="MIM:190470"
ORIGIN      
        1 mataateepf pfhgllpkke tgaasflcry peydgrgvli avldtgvdpg apgmqvttdg
       61 kpkivdiidt tgsgdvntat evepkdgeiv glsgrvlkip aswtnpsgky higikngydf
      121 ypkalkeriq kerkekiwdp vhrvalaeac rkqeefdvan ngssqankli keelqsqvel
      181 lnsfekkysd pgpvydclvw hdgevwraci dsnedgdlsk stvlrnykea qeygsfgtae
      241 mlnysvniyd dgnllsivts ggahgthvas iaaghfpeep erngvapgaq ilsikigdtr
      301 lstmetgtgl iramievinh kcdlvnysyg eathwpnsgr icevineavw khniiyvssa
      361 gnngpclstv gcpggttssv igvgayvspd mmvaeyslre klpanqytws srgpsadgal
      421 gvsisapgga iasvpnwtlr gtqlmngtsm sspnacggia lilsglkann idytvhsvrr
      481 alentavkad nievfaqghg iiqvdkaydy lvqntsfank lgftvtvgnn rgiylrdpvq
      541 vaapsdhgvg iepvfpente nsekislqlh laltsnsswv qcpshlelmn qcrhinirvd
      601 prglreglhy tevcgydias pnagplfrvp itaviaakvn esshydlaft dvhfkpgqir
      661 rhfievpega twaevtvcsc ssevsakfvl havqlvkqra yrshefykfc slpekgtlte
      721 afpvlggkai efciarwwas lsdvnidyti sfhgivctap qlnihasegi nrfdvqsslk
      781 yedlapcitl knwvqtlrpv saktkplgsr dvlpnnrqly emvltynfhq pksgevtpsc
      841 pllcellyes efdsqlwiif dqnkrqmgsg dayphqyslk lekgdytirl qirheqisdl
      901 erlkdlpfiv shrlsntlsl dihenhsfal lgkkkssnlt lppkynqpff vtslpddkip
      961 kgagpgcyla gsltlsktel gkkagqsaak rqgkfkkdvi pvhyylippp tktkngskdk
     1021 ekdsekekdl keeftealrd lkiqwmtkld ssdiynelke typnylplyv arlhqldaek
     1081 ermkrlneiv daanavishi dqtalavyia mktdprpdaa tikndmdkqk stlvdalcrk
     1141 gcaladhllh tqaqdgaist daegkeeege spldslaetf wettkwtdlf dnkvltfayk
     1201 halvnkmygr glkfatklve ekptkenwkn ciqlmkllgw thcasftenw lpimyppdyc
     1261 vf
//
LOCUS       NP_065712                198 aa            linear   PRI 27-APR-2025
DEFINITION  single-stranded DNA cytosine deaminase isoform 1 [Homo sapiens].
ACCESSION   NP_065712
VERSION     NP_065712.1
DBSOURCE    REFSEQ: accession NM_020661.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Jaiswal,A., Roy,R., Tamrakar,A., Singh,A.K., Kar,P. and Kodgire,P.
  TITLE     Activation-induced cytidine deaminase an antibody diversification
            enzyme interacts with chromatin modifier UBN1 in B-cells
  JOURNAL   Sci Rep 13 (1), 19615 (2023)
   PUBMED   37949972
  REMARK    GeneRIF: Activation-induced cytidine deaminase an antibody
            diversification enzyme interacts with chromatin modifier UBN1 in
            B-cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Jiao,J., Lv,Z., Wang,Y., Fan,L. and Yang,A.
  TITLE     The off-target effects of AID in carcinogenesis
  JOURNAL   Front Immunol 14, 1221528 (2023)
   PUBMED   37600817
  REMARK    GeneRIF: The off-target effects of AID in carcinogenesis.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Xiao,J., Li,J. and Yao,X.
  TITLE     [Activation-induced cytidine deaminase (AID) involved in the
            regulation of B cell immune senescence]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 39 (5), 474-478 (2023)
   PUBMED   37248842
  REMARK    GeneRIF: [Activation-induced cytidine deaminase (AID) involved in
            the regulation of B cell immune senescence].
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Wang,Y., Miao,Y., Zhou,W., Bi,Y., Ji,Y. and Ma,Y.
  TITLE     Activation-induced cytidine deaminase displays an alternative
            co-factor for modulating PIM1 expression in diffuse large B cell
            lymphoma cell lines
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (3), 1-7 (2023)
   PUBMED   37300695
  REMARK    GeneRIF: Activation-induced cytidine deaminase displays an
            alternative co-factor for modulating PIM1 expression in diffuse
            large B cell lymphoma cell lines.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Sakhtemani,R., Perera,M.L.W., Hubschmann,D., Siebert,R.,
            Lawrence,M.S. and Bhagwat,A.S.
  TITLE     Human activation-induced deaminase lacks strong replicative strand
            bias or preference for cytosines in hairpin loops
  JOURNAL   Nucleic Acids Res 50 (9), 5145-5157 (2022)
   PUBMED   35524550
  REMARK    GeneRIF: Human activation-induced deaminase lacks strong
            replicative strand bias or preference for cytosines in hairpin
            loops.
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Noguchi,E., Shibasaki,M., Inudou,M., Kamioka,M., Yokouchi,Y.,
            Yamakawa-Kobayashi,K., Hamaguchi,H., Matsui,A. and Arinami,T.
  TITLE     Association between a new polymorphism in the activation-induced
            cytidine deaminase gene and atopic asthma and the regulation of
            total serum IgE levels
  JOURNAL   J Allergy Clin Immunol 108 (3), 382-386 (2001)
   PUBMED   11544457
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Minegishi,Y., Lavoie,A., Cunningham-Rundles,C., Bedard,P.M.,
            Hebert,J., Cote,L., Dan,K., Sedlak,D., Buckley,R.H., Fischer,A.,
            Durandy,A. and Conley,M.E.
  TITLE     Mutations in activation-induced cytidine deaminase in patients with
            hyper IgM syndrome
  JOURNAL   Clin Immunol 97 (3), 203-210 (2000)
   PUBMED   11112359
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Revy,P., Muto,T., Levy,Y., Geissmann,F., Plebani,A., Sanal,O.,
            Catalan,N., Forveille,M., Dufourcq-Labelouse,R., Gennery,A.,
            Tezcan,I., Ersoy,F., Kayserili,H., Ugazio,A.G., Brousse,N.,
            Muramatsu,M., Notarangelo,L.D., Kinoshita,K., Honjo,T., Fischer,A.
            and Durandy,A.
  TITLE     Activation-induced cytidine deaminase (AID) deficiency causes the
            autosomal recessive form of the Hyper-IgM syndrome (HIGM2)
  JOURNAL   Cell 102 (5), 565-575 (2000)
   PUBMED   11007475
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Muto,T., Muramatsu,M., Taniwaki,M., Kinoshita,K. and Honjo,T.
  TITLE     Isolation, tissue distribution, and chromosomal localization of the
            human activation-induced cytidine deaminase (AID) gene
  JOURNAL   Genomics 68 (1), 85-88 (2000)
   PUBMED   10950930
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP225441.1, AC092184.7,
            AB040431.1 and AJ577811.1.
            
            Summary: This gene encodes a RNA-editing deaminase that is a member
            of the cytidine deaminase family. AICDA is specifically expressed
            and active in germinal center-like B cells. In the germinal center,
            AICDA is involved in somatic hypermutation, gene conversion, and
            class-switch recombination of immunoglobulin genes. An epigenetic
            role in neoplastic transformation and lymphoma progression has been
            experimentally ascribed to AICDA using mouse models. Defects in
            this gene are the cause of autosomal recessive hyper-IgM
            immunodeficiency syndrome type 2 (HIGM2). [provided by RefSeq, Jul
            2020].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB040431.1, EU794587.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149876, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000229335.11/ ENSP00000229335.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..198
                     /product="single-stranded DNA cytosine deaminase isoform
                     1"
                     /EC_number="3.5.4.38"
                     /note="integrated into Burkitt's lymphoma cell line Ramos;
                     cytidine aminohydrolase; single-stranded DNA cytosine
                     deaminase; epididymis secretory protein Li 284"
                     /calculated_mol_wt=23822
     Region          1..30
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:14769937"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZX7.1)"
     Region          2..26
                     /region_name="Interaction with SUPT6H.
                     /evidence=ECO:0000269|PubMed:21518874"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZX7.1)"
     Region          5..180
                     /region_name="NAD1"
                     /note="Novel AID APOBEC clade 1; pfam18778"
                     /db_xref="CDD:465865"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000269|PubMed:16387847; propagated from
                     UniProtKB/Swiss-Prot (Q9GZX7.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:16387847,
                     ECO:0000269|PubMed:18722174; propagated from
                     UniProtKB/Swiss-Prot (Q9GZX7.1)"
     Region          39..42
                     /region_name="Important for interaction with CTNNBL1.
                     /evidence=ECO:0000269|PubMed:18722174"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZX7.1)"
     Region          88..116
                     /region_name="Required for interaction with RNF126.
                     /evidence=ECO:0000269|PubMed:23277564"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZX7.1)"
     Region          183..198
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000269|PubMed:14769937"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZX7.1)"
     CDS             1..198
                     /gene="AICDA"
                     /gene_synonym="AID; ARP2; CDA2; HEL-S-284; HIGM2"
                     /coded_by="NM_020661.4:93..689"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41747.1"
                     /db_xref="GeneID:57379"
                     /db_xref="HGNC:HGNC:13203"
                     /db_xref="MIM:605257"
ORIGIN      
        1 mdsllmnrrk flyqfknvrw akgrretylc yvvkrrdsat sfsldfgylr nkngchvell
       61 flryisdwdl dpgrcyrvtw ftswspcydc arhvadflrg npnlslrift arlyfcedrk
      121 aepeglrrlh ragvqiaimt fkdyfycwnt fvenhertfk aweglhensv rlsrqlrril
      181 lplyevddlr dafrtlgl
//
LOCUS       NP_001099009             871 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 10 isoform a [Homo
            sapiens].
ACCESSION   NP_001099009
VERSION     NP_001099009.1
DBSOURCE    REFSEQ: accession NM_001105539.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Yang,M., Cai,W., Lin,Z., Tuohuti,A. and Chen,X.
  TITLE     Intermittent Hypoxia Promotes TAM-Induced Glycolysis in Laryngeal
            Cancer Cells via Regulation of HK1 Expression through Activation of
            ZBTB10
  JOURNAL   Int J Mol Sci 24 (19), 14808 (2023)
   PUBMED   37834257
  REMARK    GeneRIF: Intermittent Hypoxia Promotes TAM-Induced Glycolysis in
            Laryngeal Cancer Cells via Regulation of HK1 Expression through
            Activation of ZBTB10.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Wang,S., Xu,Z., Li,M., Lv,M., Shen,S., Shi,Y. and Li,F.
  TITLE     Structural insights into the recognition of telomeric variant
            repeat TTGGGG by broad-complex, tramtrack and bric-a-brac - zinc
            finger protein ZBTB10
  JOURNAL   J Biol Chem 299 (3), 102918 (2023)
   PUBMED   36657642
  REMARK    GeneRIF: Structural insights into the recognition of telomeric
            variant repeat TTGGGG by broad-complex, tramtrack and bric-a-brac -
            zinc finger protein ZBTB10.
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Zhang,A., Lu,R., Lang,H. and Wu,M.
  TITLE     MiR-361-5p promotes proliferation and inhibits apoptosis of
            fibroblast-like synoviocytes via targeting ZBTB10 in rheumatoid
            arthritis
  JOURNAL   Autoimmunity 55 (5), 310-317 (2022)
   PUBMED   35608340
  REMARK    GeneRIF: MiR-361-5p promotes proliferation and inhibits apoptosis
            of fibroblast-like synoviocytes via targeting ZBTB10 in rheumatoid
            arthritis.
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Wen,Y.C., Chen,W.Y., Tram,V.T.N., Yeh,H.L., Chen,W.H., Jiang,K.C.,
            Abou-Kheir,W., Huang,J., Hsiao,M. and Liu,Y.N.
  TITLE     Pyruvate kinase L/R links metabolism dysfunction to neuroendocrine
            differentiation of prostate cancer by ZBTB10 deficiency
  JOURNAL   Cell Death Dis 13 (3), 252 (2022)
   PUBMED   35306527
  REMARK    GeneRIF: Pyruvate kinase L/R links metabolism dysfunction to
            neuroendocrine differentiation of prostate cancer by ZBTB10
            deficiency.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Lai,Y., Zhang,X., Zhang,Z., Shu,Y., Luo,X., Yang,Y., Wang,X.,
            Yang,G., Li,L. and Feng,Y.
  TITLE     The microRNA-27a: ZBTB10-specificity protein pathway is involved in
            follicle stimulating hormone-induced VEGF, Cox2 and survivin
            expression in ovarian epithelial cancer cells
  JOURNAL   Int J Oncol 42 (2), 776-784 (2013)
   PUBMED   23254909
  REMARK    GeneRIF: Collectively, these results indicated that stimulation of
            ovarian cancer cell VEGF, Cox2 and survivin expression by FSH
            involves the microRNA27a: ZBTB10-specificity protein pathway.
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Eriksson,N., Tung,J.Y., Kiefer,A.K., Hinds,D.A., Francke,U.,
            Mountain,J.L. and Do,C.B.
  TITLE     Novel associations for hypothyroidism include known autoimmune risk
            loci
  JOURNAL   PLoS One 7 (4), e34442 (2012)
   PUBMED   22493691
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Paternoster,L., Standl,M., Chen,C.M., Ramasamy,A., Bonnelykke,K.,
            Duijts,L., Ferreira,M.A., Alves,A.C., Thyssen,J.P., Albrecht,E.,
            Baurecht,H., Feenstra,B., Sleiman,P.M., Hysi,P., Warrington,N.M.,
            Curjuric,I., Myhre,R., Curtin,J.A., Groen-Blokhuis,M.M.,
            Kerkhof,M., Saaf,A., Franke,A., Ellinghaus,D., Folster-Holst,R.,
            Dermitzakis,E., Montgomery,S.B., Prokisch,H., Heim,K.,
            Hartikainen,A.L., Pouta,A., Pekkanen,J., Blakemore,A.I.,
            Buxton,J.L., Kaakinen,M., Duffy,D.L., Madden,P.A., Heath,A.C.,
            Montgomery,G.W., Thompson,P.J., Matheson,M.C., Le Souef,P., St
            Pourcain,B., Smith,G.D., Henderson,J., Kemp,J.P., Timpson,N.J.,
            Deloukas,P., Ring,S.M., Wichmann,H.E., Muller-Nurasyid,M.,
            Novak,N., Klopp,N., Rodriguez,E., McArdle,W., Linneberg,A.,
            Menne,T., Nohr,E.A., Hofman,A., Uitterlinden,A.G., van Duijn,C.M.,
            Rivadeneira,F., de Jongste,J.C., van der Valk,R.J., Wjst,M.,
            Jogi,R., Geller,F., Boyd,H.A., Murray,J.C., Kim,C., Mentch,F.,
            March,M., Mangino,M., Spector,T.D., Bataille,V., Pennell,C.E.,
            Holt,P.G., Sly,P., Tiesler,C.M., Thiering,E., Illig,T., Imboden,M.,
            Nystad,W., Simpson,A., Hottenga,J.J., Postma,D., Koppelman,G.H.,
            Smit,H.A., Soderhall,C., Chawes,B., Kreiner-Moller,E., Bisgaard,H.,
            Melen,E., Boomsma,D.I., Custovic,A., Jacobsson,B.,
            Probst-Hensch,N.M., Palmer,L.J., Glass,D., Hakonarson,H.,
            Melbye,M., Jarvis,D.L., Jaddoe,V.W., Gieger,C., Strachan,D.P.,
            Martin,N.G., Jarvelin,M.R., Heinrich,J., Evans,D.M. and
            Weidinger,S.
  CONSRTM   Australian Asthma Genetics Consortium (AAGC); Genetics of
            Overweight Young Adults (GOYA) Consortium; EArly Genetics &
            Lifecourse Epidemiology (EAGLE) Consortium
  TITLE     Meta-analysis of genome-wide association studies identifies three
            new risk loci for atopic dermatitis
  JOURNAL   Nat Genet 44 (2), 187-192 (2011)
   PUBMED   22197932
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Pathi,S.S., Jutooru,I., Chadalapaka,G., Sreevalsan,S., Anand,S.,
            Thatcher,G.R. and Safe,S.
  TITLE     GT-094, a NO-NSAID, inhibits colon cancer cell growth by activation
            of a reactive oxygen species-microRNA-27a: ZBTB10-specificity
            protein pathway
  JOURNAL   Mol Cancer Res 9 (2), 195-202 (2011)
   PUBMED   21156786
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Li,X., Mertens-Talcott,S.U., Zhang,S., Kim,K., Ball,J. and Safe,S.
  TITLE     MicroRNA-27a Indirectly Regulates Estrogen Receptor {alpha}
            Expression and Hormone Responsiveness in MCF-7 Breast Cancer Cells
  JOURNAL   Endocrinology 151 (6), 2462-2473 (2010)
   PUBMED   20382698
  REMARK    GeneRIF: Study show that miR-27a indirectly regulates
            E2-responsiveness in MCF-7 cells through suppression of ZBTB10,
            thereby enhancing expression of ERalpha.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009812.17, BC127098.1, BC050061.1 and AI627858.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.161878.1,
                                           SRR1660809.137198.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000455036.8/ ENSP00000412036.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.13"
     Protein         1..871
                     /product="zinc finger and BTB domain-containing protein 10
                     isoform a"
                     /note="zinc finger protein RINZF; zinc finger and BTB
                     domain-containing protein 10; zinc finger protein RIN ZF"
                     /calculated_mol_wt=94763
     Region          1..156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DT7.2)"
     Site            126
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q96DT7.2)"
     Region          177..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DT7.2)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96DT7.2)"
     Region          249..>316
                     /region_name="ZnF_TTF"
                     /note="zinc finger in transposases and transcription
                     factors; smart00597"
                     /db_xref="CDD:214739"
     Region          343..464
                     /region_name="BTB_POZ_ZBTB10"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 10 (ZBTB10); cd18201"
                     /db_xref="CDD:349510"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q96DT7.2)"
     Region          722..746
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          724..744
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          737..761
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          752..772
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          764..787
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          812..871
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DT7.2)"
     CDS             1..871
                     /gene="ZBTB10"
                     /gene_synonym="RINZF"
                     /coded_by="NM_001105539.3:586..3201"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47880.1"
                     /db_xref="GeneID:65986"
                     /db_xref="HGNC:HGNC:30953"
                     /db_xref="MIM:618576"
ORIGIN      
        1 msfsemnrrt lafrggglvt asgggstnnn aggeasawpp qpqprqpppp appalqppng
       61 rgadeevele glepqdleas agpaagaaee akelllpqda ggptslggga ggpllaernr
      121 rtlafrgggg gglgnngssr grpetsvwpl rhfngrgpat vdleldaleg kelmqdgasl
      181 sdstedeeeg aslgdgsgae ggscsssrrs ggdggdeveg sgvgageget vqhfplarpk
      241 slmqklqcsf qtswlkdfpw lryskdtglm scgwcqktpa dggsvdlppv ghdelsrgtr
      301 nykktlllrh hvstehklhe anaqeseips eegycdfnsr pnensycyql lrqlneqrkk
      361 gilcdvsivv sgkifkahkn ilvagsrffk tlycfsnkes pnqnntthld iaavqgfsvi
      421 ldflysgnlv ltsqnaievm tvasylqmse vvqtcrnfik dalnisikse apesvvvdyn
      481 nrkpvnrdgl sssrdqkias fwatrnltnl asnvkiendg cnvdegqien yqmndsswvq
      541 dgspemaene segqtkvfiw nnmgsqgiqe tgktrrknqt tkrfiynipp nnetnledcs
      601 vmqppvaype entllikeep dldgallsgp dgdrnvnanl laeagtsqdg gdagtshdfk
      661 yglmpgpsnd fkyglipgts ndfkyglipg asndfkygll peswpkqetw engesslimn
      721 klkcphcsyv akyrrtlkrh llihtgvrsf scdicgklft rrehvkrhsl vhkkdkkykc
      781 mvckkifmla asvgirhgsr rygvcvdcad ksqpggqegv dqgqdtefpr deeyeenevg
      841 eadeelvddg edqndpsrwd esgevcmsld d
//
LOCUS       NP_001350365             421 aa            linear   PRI 27-APR-2025
DEFINITION  UPF0415 protein C7orf25 [Homo sapiens].
ACCESSION   NP_001350365 XP_005249901
VERSION     NP_001350365.1
DBSOURCE    REFSEQ: accession NM_001363436.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Matelska,D., Steczkiewicz,K. and Ginalski,K.
  TITLE     Comprehensive classification of the PIN domain-like superfamily
  JOURNAL   Nucleic Acids Res 45 (12), 6995-7020 (2017)
   PUBMED   28575517
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Bommel,H., Xie,G., Rossoll,W., Wiese,S., Jablonka,S., Boehm,T. and
            Sendtner,M.
  TITLE     Missense mutation in the tubulin-specific chaperone E (Tbce) gene
            in the mouse mutant progressive motor neuronopathy, a model of
            human motoneuron disease
  JOURNAL   J Cell Biol 159 (4), 563-569 (2002)
   PUBMED   12446740
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX401140.2, DB483522.1, DC303669.1 and AK024820.1.
            
            On May 18, 2018 this sequence version replaced XP_005249901.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB483522.1, SRR1660807.70104.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.1"
     Protein         1..421
                     /product="UPF0415 protein C7orf25"
                     /calculated_mol_wt=46320
     Region          1..218
                     /region_name="DUF5614"
                     /note="Family of unknown function (DUF5614); pfam18474"
                     /db_xref="CDD:436527"
     Region          248..409
                     /region_name="DUF1308"
                     /note="Protein of unknown function (DUF1308); pfam07000"
                     /db_xref="CDD:399767"
     CDS             1..421
                     /gene="C7orf25"
                     /coded_by="NM_001363436.1:398..1663"
                     /db_xref="CCDS:CCDS5466.1"
                     /db_xref="GeneID:79020"
                     /db_xref="HGNC:HGNC:21703"
ORIGIN      
        1 msahsmlcer iaiakelikr aeslsrsrkg gieggaklcs klkaelkflq kveagkvaik
       61 eshlqstnlt hlraivesae nleevvsvlh vfgytdtlge kqtlvvdvva ngghtwvkai
      121 grkaealhni wlgrgqygdk siieqaedfl qashqqpvqy snphiifafy nsvsspmaek
      181 lkemgisvrg divavnalld hpeelqpses esddegpell qvtrvdreni lasvafptei
      241 kvdvckrvnl dittlityvs alsyggchfi fkekvlteqa eqerkeqvlp qleafmkdke
      301 lfacesavkd fqsildtlgg pgereratvl ikrinvvpdq pseralrlva sskinsrslt
      361 ifgtgdtlka itmtansgfv raannqgvkf svfihqpral teskealatp lpkdyttdse
      421 h
//
LOCUS       NP_079206                281 aa            linear   PRI 27-APR-2025
DEFINITION  very long chain fatty acid elongase 7 isoform 1 [Homo sapiens].
ACCESSION   NP_079206 XP_371740
VERSION     NP_079206.2
DBSOURCE    REFSEQ: accession NM_024930.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Zhou,Y., Lv,R., Ye,R.D., Ren,R. and Yu,L.
  TITLE     The 3-hydroxyacyl-CoA dehydratase 1/2 form complex with
            trans-2-enoyl-CoA reductase involved in substrates transfer in very
            long chain fatty acid elongation
  JOURNAL   Biochem Biophys Res Commun 704, 149588 (2024)
   PUBMED   38422897
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Wang,W.M., Yang,Z.G., Liu,C. and Dong,Q.
  TITLE     ELOVL fatty acid elongase 7 (ELOVL7), upregulated by Mdr2-knockout,
            predicts advanced liver fibrosis in patients with chronic hepatitis
            B
  JOURNAL   Eur Rev Med Pharmacol Sci 27 (5), 1954-1970 (2023)
   PUBMED   36930494
  REMARK    GeneRIF: ELOVL fatty acid elongase 7 (ELOVL7), upregulated by
            Mdr2-knockout, predicts advanced liver fibrosis in patients with
            chronic hepatitis B.
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Nie,L., Pascoa,T.C., Pike,A.C.W., Bushell,S.R., Quigley,A.,
            Ruda,G.F., Chu,A., Cole,V., Speedman,D., Moreira,T., Shrestha,L.,
            Mukhopadhyay,S.M.M., Burgess-Brown,N.A., Love,J.D., Brennan,P.E.
            and Carpenter,E.P.
  TITLE     The structural basis of fatty acid elongation by the ELOVL
            elongases
  JOURNAL   Nat Struct Mol Biol 28 (6), 512-520 (2021)
   PUBMED   34117479
  REMARK    GeneRIF: The structural basis of fatty acid elongation by the ELOVL
            elongases.
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Wernick,A.I., Walton,R.L., Soto-Beasley,A.I., Koga,S., Ren,Y.,
            Heckman,M.G., Milanowski,L.M., Valentino,R.R., Kondru,N.,
            Uitti,R.J., Cheshire,W.P., Wszolek,Z.K., Dickson,D.W. and Ross,O.A.
  TITLE     Investigating ELOVL7 coding variants in multiple system atrophy
  JOURNAL   Neurosci Lett 749, 135723 (2021)
   PUBMED   33600908
  REMARK    GeneRIF: Investigating ELOVL7 coding variants in multiple system
            atrophy.
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Purdy,J.G., Shenk,T. and Rabinowitz,J.D.
  TITLE     Fatty acid elongase 7 catalyzes lipidome remodeling essential for
            human cytomegalovirus replication
  JOURNAL   Cell Rep 10 (8), 1375-1385 (2015)
   PUBMED   25732827
  REMARK    GeneRIF: ELOVL7 knockdown or mTOR inhibition impairs HCMV-induced
            fatty acid elongation.
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Naganuma,T., Sato,Y., Sassa,T., Ohno,Y. and Kihara,A.
  TITLE     Biochemical characterization of the very long-chain fatty acid
            elongase ELOVL7
  JOURNAL   FEBS Lett 585 (20), 3337-3341 (2011)
   PUBMED   21959040
  REMARK    GeneRIF: progression of the VLCFA cycle enhances ELOVL7 activity.
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Ohno,Y., Suto,S., Yamanaka,M., Mizutani,Y., Mitsutake,S.,
            Igarashi,Y., Sassa,T. and Kihara,A.
  TITLE     ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid
            synthesis
  JOURNAL   Proc Natl Acad Sci U S A 107 (43), 18439-18444 (2010)
   PUBMED   20937905
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Tamura,K., Makino,A., Hullin-Matsuda,F., Kobayashi,T., Furihata,M.,
            Chung,S., Ashida,S., Miki,T., Fujioka,T., Shuin,T., Nakamura,Y. and
            Nakagawa,H.
  TITLE     Novel lipogenic enzyme ELOVL7 is involved in prostate cancer growth
            through saturated long-chain fatty acid metabolism
  JOURNAL   Cancer Res 69 (20), 8133-8140 (2009)
   PUBMED   19826053
  REMARK    GeneRIF: Overexpression of ELOVL7 is associated with prostate
            cancer growth through saturated long-chain fatty acid metabolism.
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Lehner,R. and Kuksis,A.
  TITLE     Biosynthesis of triacylglycerols
  JOURNAL   Prog Lipid Res 35 (2), 169-201 (1996)
   PUBMED   8944226
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA247166.1, AC104113.3, AB181393.1, AL137506.1 and AI769834.1.
            
            On Sep 20, 2007 this sequence version replaced NP_079206.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Both variants 1 and 2 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.191961.1,
                                           SRR1803615.27658.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000508821.6/ ENSP00000424123.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.1"
     Protein         1..281
                     /product="very long chain fatty acid elongase 7 isoform 1"
                     /EC_number="2.3.1.199"
                     /note="elongation of very long chain fatty acids protein
                     7; 3-keto acyl-CoA synthase ELOVL7; ELOVL FA elongase 7;
                     very long chain 3-oxoacyl-CoA synthase 7; ELOVL family
                     member 7, elongation of long chain fatty acids; very long
                     chain fatty acid elongase 7; very long chain
                     3-ketoacyl-CoA synthase 7"
                     /calculated_mol_wt=33225
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:34117479; propagated from
                     UniProtKB/Swiss-Prot (A1L3X0.1)"
     Site            28..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3X0.1)"
     Region          29..269
                     /region_name="ELO"
                     /note="GNS1/SUR4 family; pfam01151"
                     /db_xref="CDD:460083"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3X0.1)"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3X0.1)"
     Site            143..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3X0.1)"
     Region          147..151
                     /region_name="HxxHH motif.
                     /evidence=ECO:0000305|PubMed:34117479"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3X0.1)"
     Site            172..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3X0.1)"
     Site            207..227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3X0.1)"
     Site            237..257
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3X0.1)"
     Region          277..281
                     /region_name="Di-lysine motif.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03207"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L3X0.1)"
     CDS             1..281
                     /gene="ELOVL7"
                     /coded_by="NM_024930.3:196..1041"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34164.1"
                     /db_xref="GeneID:79993"
                     /db_xref="HGNC:HGNC:26292"
                     /db_xref="MIM:614451"
ORIGIN      
        1 mafsdltsrt vhlydnwikd adprvedwll mssplpqtil lgfyvyfvts lgpklmenrk
       61 pfelkkamit ynffivlfsv ymcyefvmsg wgigysfrcd ivdysrspta lrmartcwly
      121 yfskfielld tiffvlrkkn sqvtflhvfh htimpwtwwf gvkfaagglg tfhallntav
      181 hvvmysyygl salgpayqky lwwkkyltsl qlvqfvivai hisqfffmed ckyqfpvfac
      241 iimsysfmfl llflhfwyra ytkgqrlpkt vkngtcknkd n
//
LOCUS       NP_001346773             193 aa            linear   ROD 27-APR-2025
DEFINITION  neurocalcin-delta [Mus musculus].
ACCESSION   NP_001346773 XP_011243665
VERSION     NP_001346773.1
DBSOURCE    REFSEQ: accession NM_001359844.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Kolesova,H., Hrabalova,P., Bohuslavova,R., Abaffy,P.,
            Fabriciova,V., Sedmera,D. and Pavlinkova,G.
  TITLE     Reprogramming of the developing heart by Hif1a-deficient
            sympathetic system and maternal diabetes exposure
  JOURNAL   Front Endocrinol (Lausanne) 15, 1344074 (2024)
   PUBMED   38505753
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Ahuja,N., Hiltabidle,M.S., Rajasekhar,H., Voss,S., Lu,S.Z.,
            Barlow,H.R., Cowdin,M.A., Daniel,E., Vaddaraju,V., Anandakumar,T.,
            Black,E., Cleaver,O. and Maynard,C.
  TITLE     Endothelial Cyp26b1 restrains murine heart valve growth during
            development
  JOURNAL   Dev Biol 486, 81-95 (2022)
   PUBMED   35364055
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Del Aguila,A., Adam,M., Ullom,K., Shaw,N., Qin,S., Ehrman,J.,
            Nardini,D., Salomone,J., Gebelein,B., Lu,Q.R., Potter,S.S.,
            Waclaw,R., Campbell,K. and Nakafuku,M.
  TITLE     Olig2 defines a subset of neural stem cells that produce specific
            olfactory bulb interneuron subtypes in the subventricular zone of
            adult mice
  JOURNAL   Development 149 (5) (2022)
   PUBMED   35132995
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Upadhyay,A., Hosseinibarkooie,S., Schneider,S., Kaczmarek,A.,
            Torres-Benito,L., Mendoza-Ferreira,N., Overhoff,M., Rombo,R.,
            Grysko,V., Kye,M.J., Kononenko,N.L. and Wirth,B.
  TITLE     Neurocalcin Delta Knockout Impairs Adult Neurogenesis Whereas Half
            Reduction Is Not Pathological
  JOURNAL   Front Mol Neurosci 12, 19 (2019)
   PUBMED   30853885
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Duda,T., Pertzev,A. and Sharma,R.K.
  TITLE     Ca(2+) modulation of ANF-RGC: new signaling paradigm interlocked
            with blood pressure regulation
  JOURNAL   Biochemistry 51 (46), 9394-9405 (2012)
   PUBMED   23088492
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Brouns,M.R., De Castro,S.C., Terwindt-Rouwenhorst,E.A., Massa,V.,
            Hekking,J.W., Hirst,C.S., Savery,D., Munts,C., Partridge,D.,
            Lamers,W., Kohler,E., van Straaten,H.W., Copp,A.J. and Greene,N.D.
  TITLE     Over-expression of Grhl2 causes spina bifida in the Axial defects
            mutant mouse
  JOURNAL   Hum Mol Genet 20 (8), 1536-1546 (2011)
   PUBMED   21262862
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Kotani,T., Murata,Y., Ohnishi,H., Mori,M., Kusakari,S., Saito,Y.,
            Okazawa,H., Bixby,J.L. and Matozaki,T.
  TITLE     Expression of PTPRO in the interneurons of adult mouse olfactory
            bulb
  JOURNAL   J Comp Neurol 518 (2), 119-136 (2010)
   PUBMED   19924828
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Murias,A.R., Weruaga,E., Recio,J.S., Airado,C., Diaz,D. and
            Alonso,J.R.
  TITLE     Distribution of neurocalcin-containing neurons reveals sexual
            dimorphism in the mouse olfactory bulb
  JOURNAL   Chem Senses 32 (7), 673-680 (2007)
   PUBMED   17548529
  REMARK    GeneRIF: According to their distribution in the olfactory bulb,
            neurocalcin-immunoreactive interneurons could reflect a sexually
            dimorphic regulation of specific odorants.
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Germana,A., del Valle,M.E., Laura,R., Ciriaco,E., Vega,J.A. and
            Germana,G.
  TITLE     Effects of neurotrophin-3 gene mutation in the expression of
            neurocalcin
  JOURNAL   Ital J Anat Embryol 110 (2 Suppl 1), 37-47 (2005)
   PUBMED   16101019
  REMARK    GeneRIF: Neurocalcin-containing DRG neurons include all
            proprioceptive, and a subset of mechanoreceptive and
            proprioceptive. Furthermore, NT-3 is involved in the maturation of
            motor end-plates.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC122506.4, AC122263.5 and AC121814.3.
            
            On Jan 13, 2018 this sequence version replaced XP_011243665.1.
            
            Transcript Variant: This variant (10) differs in the 5' UTR
            compared to variant 1. Variants 1 through 11 encode the same
            protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7974084.1880.1,
                                           SRR1660817.127404.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 14.94 cM"
     Protein         1..193
                     /product="neurocalcin-delta"
                     /calculated_mol_wt=22114
     Region          21..175
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..193
                     /gene="Ncald"
                     /gene_synonym="D030020D09Rik; D15Ertd412e"
                     /coded_by="NM_001359844.1:377..958"
                     /db_xref="CCDS:CCDS27435.1"
                     /db_xref="GeneID:52589"
                     /db_xref="MGI:MGI:1196326"
ORIGIN      
        1 mgkqnsklrp evmqdllest dfteheiqew ykgflrdcps ghlsmeefkk iygnffpygd
       61 askfaehvfr tfdangdgti dfrefiials vtsrgkleqk lkwafsmydl dgngyiskae
      121 mleivqaiyk mvssvmkmpe destpekrte kifrqmdtnr dgklsleefi rgaksdpsiv
      181 rllqcdpssa gqf
//
LOCUS       NP_001356873             521 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 12 [Homo
            sapiens].
ACCESSION   NP_001356873
VERSION     NP_001356873.1
DBSOURCE    REFSEQ: accession NM_001369944.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.39102.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..521
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 12"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=59181
     Region          233..272
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..521
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369944.1:327..1892"
                     /note="isoform 12 is encoded by transcript variant 27"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mpllelkdiv lylcdtcttl wafldifpla cqtfqkhdfc yrlasfyeaa ipemesaikk
       61 rrledskllg dlwqrlshsr kklmeifhii lnqicllpil esscdniqgf ieeflqifss
      121 llqekrflrd ydalfpvaed isllqqassv ldetrtayil qavesawegv drrkatdakd
      181 psvieepnge pngvtvtaea vsqasshpen seeeecmgaa aavgpamcgv eldslisqvk
      241 dllpdlgegf ilacleyyhy dpeqvinnil eerlaptlsq ldrnldremk pdptplltsr
      301 hnvfqndefd vfsrdsvdls rvhkgkstrk eentrsllnd kravaaqrqr yeqysvvvee
      361 vplqpgeslp yhsvyyedey ddtydgnqvg andadsddel isrrpftipq vlrtkvpreg
      421 qeeddddeed dadeeapkpd hfvqdpavlr ekaearrmaf lakkgyrhds stavagsprg
      481 hgqsrettqe rrkkeankat ranhnrrtma drkrskgmip s
//
LOCUS       NP_598378                236 aa            linear   PRI 27-APR-2025
DEFINITION  rho-related GTP-binding protein RhoV [Homo sapiens].
ACCESSION   NP_598378
VERSION     NP_598378.3
DBSOURCE    REFSEQ: accession NM_133639.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Harlin,E.W., Ito,T., Nakano,S., Morikawa,K., Sato,K., Nishikawa,M.,
            Nakamura,K., Nagaoka,H., Nagase,T. and Ueda,H.
  TITLE     Regulation of RHOV signaling by interaction with SH3
            domain-containing adaptor proteins and phosphorylation by PKA
  JOURNAL   Biochem Biophys Res Commun 728, 150325 (2024)
   PUBMED   38959529
  REMARK    GeneRIF: Regulation of RHOV signaling by interaction with SH3
            domain-containing adaptor proteins and phosphorylation by PKA.
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Qin,Q. and Peng,B.
  TITLE     Prognostic significance of the rho GTPase RHOV and its role in
            tumor immune cell infiltration: a comprehensive pan-cancer analysis
  JOURNAL   FEBS Open Bio 13 (11), 2124-2146 (2023)
   PUBMED   37596964
  REMARK    GeneRIF: Prognostic significance of the rho GTPase RHOV and its
            role in tumor immune cell infiltration: a comprehensive pan-cancer
            analysis.
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Jin,M.L., Gong,Y., Ji,P., Hu,X. and Shao,Z.M.
  TITLE     In vivo CRISPR screens identify RhoV as a pro-metastasis factor of
            triple-negative breast cancer
  JOURNAL   Cancer Sci 114 (6), 2375-2385 (2023)
   PUBMED   36898847
  REMARK    GeneRIF: In vivo CRISPR screens identify RhoV as a pro-metastasis
            factor of triple-negative breast cancer.
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Luu,A.P., Yao,Z., Ramachandran,S., Azzopardi,S.A., Miles,L.A.,
            Schneider,W.M., Hoffmann,H.H., Bozzacco,L., Garcia,G. Jr., Gong,D.,
            Damoiseaux,R., Tang,H., Morizono,K., Rudin,C.M., Sun,R.,
            Arumugaswami,V., Poirier,J.T., MacDonald,M.R., Rice,C.M. and
            Li,M.M.H.
  TITLE     A CRISPR Activation Screen Identifies an Atypical Rho GTPase That
            Enhances Zika Viral Entry
  JOURNAL   Viruses 13 (11), 2113 (2021)
   PUBMED   34834920
  REMARK    GeneRIF: A CRISPR Activation Screen Identifies an Atypical Rho
            GTPase That Enhances Zika Viral Entry.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Zhang,D., Jiang,Q., Ge,X., Shi,Y., Ye,T., Mi,Y., Xie,T., Li,Q. and
            Ye,Q.
  TITLE     RHOV promotes lung adenocarcinoma cell growth and metastasis
            through JNK/c-Jun pathway
  JOURNAL   Int J Biol Sci 17 (10), 2622-2632 (2021)
   PUBMED   34326698
  REMARK    GeneRIF: RHOV promotes lung adenocarcinoma cell growth and
            metastasis through JNK/c-Jun pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Liu,J., Li,M., Ran,X., Fan,J.S. and Song,J.
  TITLE     Structural insight into the binding diversity between the human
            Nck2 SH3 domains and proline-rich proteins
  JOURNAL   Biochemistry 45 (23), 7171-7184 (2006)
   PUBMED   16752908
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Chenette,E.J., Abo,A. and Der,C.J.
  TITLE     Critical and distinct roles of amino- and carboxyl-terminal
            sequences in regulation of the biological activity of the Chp
            atypical Rho GTPase
  JOURNAL   J Biol Chem 280 (14), 13784-13792 (2005)
   PUBMED   15664990
  REMARK    GeneRIF: Data suggest that Chp is implicated in cell
            transformation, and the unique amino and carboxyl termini of Chp
            represent atypical mechanisms of regulation of Rho GTPase function.
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Katoh,M.
  TITLE     Molecular cloning and characterization of WRCH2 on human chromosome
            15q15
  JOURNAL   Int J Oncol 20 (5), 977-982 (2002)
   PUBMED   11956592
  REMARK    GeneRIF: cloning and characterization of WRCH2 on human chromosome
            15q15
REFERENCE   9  (residues 1 to 236)
  AUTHORS   Wherlock,M. and Mellor,H.
  TITLE     The Rho GTPase family: a Racs to Wrchs story
  JOURNAL   J Cell Sci 115 (Pt 2), 239-240 (2002)
   PUBMED   11839775
  REMARK    Review article
REFERENCE   10 (residues 1 to 236)
  AUTHORS   Aronheim,A., Broder,Y.C., Cohen,A., Fritsch,A., Belisle,B. and
            Abo,A.
  TITLE     Chp, a homologue of the GTPase Cdc42Hs, activates the JNK pathway
            and is implicated in reorganizing the actin cytoskeleton
  JOURNAL   Curr Biol 8 (20), 1125-1128 (1998)
   PUBMED   9778532
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025166.7 and BC112945.1.
            
            On May 7, 2009 this sequence version replaced NP_598378.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC112945.1, SRR1163655.191746.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000220507.5/ ENSP00000220507.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1"
     Protein         1..236
                     /product="rho-related GTP-binding protein RhoV"
                     /note="WRCH1-related GTPase; Wnt-1 responsive Cdc42
                     homolog 2; CDC42-like GTPase 2; Wnt-1 regulated Cdc42
                     homolog 2; Rho GTPase-like protein ARHV; WRCH-2;
                     GTP-binding protein-like 2; ras homolog gene family,
                     member V"
                     /calculated_mol_wt=26086
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L33.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L33.1)"
     Region          32..205
                     /region_name="Wrch_1"
                     /note="Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho
                     family GTPase similar to Cdc42; cd04130"
                     /db_xref="CDD:133330"
     Site            order(33,63..64,66..67,69,71,80,84..85,87..89,95,98)
                     /site_type="other"
                     /note="putative GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:133330"
     Site            38..45
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133330"
     Site            order(41..46,85..86,88,144,146,188..189)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133330"
     Site            62..68
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133330"
     Site            63
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133330"
     Site            order(64,87,95,97)
                     /site_type="active"
                     /note="putative GDI (guanine nucleotide dissociation
                     inhibitor) interaction [active]"
                     /db_xref="CDD:133330"
     Site            order(64..65,89,95)
                     /site_type="other"
                     /note="putative GAP (GTPase-activating protein)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:133330"
     Site            order(65..66,95,98)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133330"
     Site            85..88
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133330"
     Site            order(88..89,95..98,103..105)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133330"
     Site            143..146
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133330"
     Site            187..189
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133330"
     CDS             1..236
                     /gene="RHOV"
                     /gene_synonym="ARHV; CHP; WRCH2"
                     /coded_by="NM_133639.4:96..806"
                     /db_xref="CCDS:CCDS10068.1"
                     /db_xref="GeneID:171177"
                     /db_xref="HGNC:HGNC:18313"
                     /db_xref="MIM:620101"
ORIGIN      
        1 mpprelseae ppplraptpp prrrsappel gikcvlvgdg avgksslivs ytcngypary
       61 rptaldtfsv qvlvdgapvr ielwdtagqe dfdrlrslcy pdtdvflacf svvqpssfqn
      121 itekwlpeir thnpqapvll vgtqadlrdd vnvliqldqg gregpvpqpq aqglaekira
      181 ccylecsalt qknlkevfds ailsaiehka rlekklnakg vrtlsrcrwk kffcfv
//
LOCUS       NP_001035548             941 aa            linear   PRI 27-APR-2025
DEFINITION  endoplasmic reticulum aminopeptidase 1 isoform b precursor [Homo
            sapiens].
ACCESSION   NP_001035548
VERSION     NP_001035548.1
DBSOURCE    REFSEQ: accession NM_001040458.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Saad,M.A., Abdul-Sattar,A.B., Abdelal,I.T. and Barak,A.
  TITLE     Association of Endoplasmic Reticulum Aminopeptidase 1 Gene
            Polymorphism with Susceptibility and Severity of Axial
            Spondyloarthritis in Egyptian Population: A Single-center
            Case-Control Study
  JOURNAL   Ann Afr Med 23 (3), 443-451 (2024)
   PUBMED   39034571
  REMARK    GeneRIF: Association of Endoplasmic Reticulum Aminopeptidase 1 Gene
            Polymorphism with Susceptibility and Severity of Axial
            Spondyloarthritis in Egyptian Population: A Single-center
            Case-Control Study.
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Ma,C., Liu,X.W., Zheng,Y.Y. and Zhang,W.Y.
  TITLE     [Relationship between maternal and fetal ERAP-1 gene polymorphism
            and pre-eclampsia]
  JOURNAL   Zhonghua Fu Chan Ke Za Zhi 59 (6), 434-439 (2024)
   PUBMED   38951078
  REMARK    GeneRIF: [Relationship between maternal and fetal ERAP-1 gene
            polymorphism and pre-eclampsia].
REFERENCE   3  (residues 1 to 941)
  AUTHORS   Sasaki,T., Razia,S., Kimura-Kataoka,K., Araki,T., Kusaka,A.,
            Takeshita,H. and Fujihara,J.
  TITLE     Association of a single nucleotide polymorphism (rs27434) in the
            ERAP1 gene with plural tissue weight
  JOURNAL   Leg Med (Tokyo) 68, 102419 (2024)
   PUBMED   38342012
  REMARK    GeneRIF: Association of a single nucleotide polymorphism (rs27434)
            in the ERAP1 gene with plural tissue weight.
REFERENCE   4  (residues 1 to 941)
  AUTHORS   Hassan,S.H., Auda,I.G., Ali,E.N., Alosami,M.H. and Hussein,R.H.
  TITLE     Role of endoplasmic reticulum aminopeptidase-1 gene polymorphism
            (rs13167972) in occurrence susceptibility of ankylosing spondylitis
            in a sample of Iraqi male patients
  JOURNAL   Mol Biol Rep 51 (1), 462 (2024)
   PUBMED   38551779
  REMARK    GeneRIF: Role of endoplasmic reticulum aminopeptidase-1 gene
            polymorphism (rs13167972) in occurrence susceptibility of
            ankylosing spondylitis in a sample of Iraqi male patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 941)
  AUTHORS   Raja,A. and Kuiper,J.J.W.
  TITLE     Evolutionary immuno-genetics of endoplasmic reticulum
            aminopeptidase II (ERAP2)
  JOURNAL   Genes Immun 24 (6), 295-302 (2023)
   PUBMED   37925533
  REMARK    GeneRIF: Evolutionary immuno-genetics of endoplasmic reticulum
            aminopeptidase II (ERAP2).
            Review article
REFERENCE   6  (residues 1 to 941)
  AUTHORS   Cui,X., Hawari,F., Alsaaty,S., Lawrence,M., Combs,C.A., Geng,W.,
            Rouhani,F.N., Miskinis,D. and Levine,S.J.
  TITLE     Identification of ARTS-1 as a novel TNFR1-binding protein that
            promotes TNFR1 ectodomain shedding
  JOURNAL   J Clin Invest 110 (4), 515-526 (2002)
   PUBMED   12189246
  REMARK    GeneRIF: ARTS-1 has been identified as a novel TNFR1 binding
            protein that promotes TNFR1 shedding.
REFERENCE   7  (residues 1 to 941)
  AUTHORS   Yamamoto,N., Nakayama,J., Yamakawa-Kobayashi,K., Hamaguchi,H.,
            Miyazaki,R. and Arinami,T.
  TITLE     Identification of 33 polymorphisms in the adipocyte-derived leucine
            aminopeptidase (ALAP) gene and possible association with
            hypertension
  JOURNAL   Hum Mutat 19 (3), 251-257 (2002)
   PUBMED   11857741
  REMARK    GeneRIF: Association has been confirmed between the Lys528Arg
            polymorphism of the adipocyte-derived leucine aminopeptidase gene
            and essential hypertension.
REFERENCE   8  (residues 1 to 941)
  AUTHORS   Hattori,A., Matsumoto,K., Mizutani,S. and Tsujimoto,M.
  TITLE     Genomic organization of the human adipocyte-derived leucine
            aminopeptidase gene and its relationship to the placental leucine
            aminopeptidase/oxytocinase gene
  JOURNAL   J Biochem 130 (2), 235-241 (2001)
   PUBMED   11481040
REFERENCE   9  (residues 1 to 941)
  AUTHORS   Hattori,A., Kitatani,K., Matsumoto,H., Miyazawa,S., Rogi,T.,
            Tsuruoka,N., Mizutani,S., Natori,Y. and Tsujimoto,M.
  TITLE     Characterization of recombinant human adipocyte-derived leucine
            aminopeptidase expressed in Chinese hamster ovary cells
  JOURNAL   J Biochem 128 (5), 755-762 (2000)
   PUBMED   11056387
REFERENCE   10 (residues 1 to 941)
  AUTHORS   Hattori,A., Matsumoto,H., Mizutani,S. and Tsujimoto,M.
  TITLE     Molecular cloning of adipocyte-derived leucine aminopeptidase
            highly related to placental leucine aminopeptidase/oxytocinase
  JOURNAL   J Biochem 125 (5), 931-938 (1999)
   PUBMED   10220586
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA704693.1, DA327238.1,
            AF222340.1 and AC008906.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is an aminopeptidase
            involved in trimming HLA class I-binding precursors so that they
            can be presented on MHC class I molecules. The encoded protein acts
            as a monomer or as a heterodimer with ERAP2. This protein may also
            be involved in blood pressure regulation by inactivation of
            angiotensin II. Three transcript variants encoding two different
            isoforms have been found for this gene.[provided by RefSeq, Oct
            2010].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (b)
            has a shorter and distinct C-terminus compared to isoform a.
            Variants 2 and 3 both encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF183569.1, AF222340.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000443439.7/ ENSP00000406304.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q15"
     Protein         1..941
                     /product="endoplasmic reticulum aminopeptidase 1 isoform b
                     precursor"
                     /note="aminopeptidase regulator of TNFR1 shedding;
                     puromycin-insensitive leucyl-specific aminopeptidase;
                     aminopeptidase PILS; adipocyte-derived leucine
                     aminopeptidase; endoplasmic reticulum aminopeptidase
                     associated with antigen processing; type 1 tumor necrosis
                     factor receptor shedding aminopeptidase regulator"
                     /calculated_mol_wt=103696
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3557
     Site            2..21
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZ08.3)"
     Region          61..526
                     /region_name="M1_APN-Q_like"
                     /note="Peptidase M1 aminopeptidase N catalytic domain
                     family which includes aminopeptidase N (APN),
                     aminopeptidase Q (APQ), tricorn interacting factor F3, and
                     endoplasmic reticulum aminopeptidase 1 (ERAP1); cd09601"
                     /db_xref="CDD:341064"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21478864, ECO:0000269|Ref.16;
                     propagated from UniProtKB/Swiss-Prot (Q9NZ08.3)"
     Site            154
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21478864, ECO:0000269|Ref.16;
                     propagated from UniProtKB/Swiss-Prot (Q9NZ08.3)"
     Site            order(181,183,317..320,353..354,357,376,380,433,438)
                     /site_type="active"
                     /db_xref="CDD:341064"
     Site            414
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218, ECO:0000269|Ref.16;
                     propagated from UniProtKB/Swiss-Prot (Q9NZ08.3)"
     Site            438
                     /site_type="other"
                     /note="Transition state stabilizer. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9NZ08.3)"
     Region          597..916
                     /region_name="ERAP1_C"
                     /note="ERAP1-like C-terminal domain; pfam11838"
                     /db_xref="CDD:463368"
     Site            760
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21478864; propagated from
                     UniProtKB/Swiss-Prot (Q9NZ08.3)"
     Site            901
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZ08.3)"
     CDS             1..941
                     /gene="ERAP1"
                     /gene_synonym="A-LAP; ALAP; APPILS; ARTS-1; ARTS1; ERAAP;
                     ERAAP1; PILS-AP; PILSAP"
                     /coded_by="NM_001040458.3:104..2929"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS47250.1"
                     /db_xref="GeneID:51752"
                     /db_xref="HGNC:HGNC:18173"
                     /db_xref="MIM:606832"
ORIGIN      
        1 mvflplkwsl atmsfllssl lalltvstps wcqsteaspk rsdgtpfpwn kirlpeyvip
       61 vhydllihan lttltfwgtt kveitasqpt stiilhshhl qisratlrkg agerlseepl
      121 qvlehprqeq iallapepll vglpytvvih yagnlsetfh gfykstyrtk egelrilast
      181 qfeptaarma fpcfdepafk asfsikirre prhlaisnmp lvksvtvaeg liedhfdvtv
      241 kmstylvafi isdfesvski tksgvkvsvy avpdkinqad yaldaavtll efyedyfsip
      301 yplpkqdlaa ipdfqsgame nwglttyres allfdaekss assklgitmt vahelahqwf
      361 gnlvtmewwn dlwlnegfak fmefvsvsvt hpelkvgdyf fgkcfdamev dalnsshpvs
      421 tpvenpaqir emfddvsydk gacilnmlre ylsadafksg ivqylqkhsy kntknedlwd
      481 smasicptdg vkgmdgfcsr sqhssssshw hqegvdvktm mntwtlqkgf plititvrgr
      541 nvhmkqehym kgsdgapdtg ylwhvpltfi tsksdmvhrf llktktdvli lpeevewikf
      601 nvgmngyyiv hyeddgwdsl tgllkgthta vssndrasli nnafqlvsig klsiekaldl
      661 slylkhetei mpvfqglnel ipmyklmekr dmnevetqfk aflirllrdl idkqtwtdeg
      721 svsermlrsq llllacvhny qpcvqraegy frkwkesngn lslpvdvtla vfavgaqste
      781 gwdflyskyq fslssteksq iefalcrtqn keklqwllde sfkgdkiktq efpqiltlig
      841 rnpvgyplaw qflrknwnkl vqkfelgsss iahmvmgttn qfstrtrlee vkgffsslke
      901 ngsqlrcvqq tietieenig wmdknfdkir vwlqsekler m
//
LOCUS       NP_001347465             521 aa            linear   ROD 27-APR-2025
DEFINITION  occludin isoform 1 [Mus musculus].
ACCESSION   NP_001347465 XP_006517626
VERSION     NP_001347465.1
DBSOURCE    REFSEQ: accession NM_001360536.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   He,T., Zhang,M., Qin,J., Wang,Y., Li,S., Du,C., Jiao,J. and Ji,F.
  TITLE     Endothelial PD-1 Regulates Vascular Homeostasis and
            Oligodendrogenesis during Brain Development
  JOURNAL   Adv Sci (Weinh) 12 (16), e2417410 (2025)
   PUBMED   40013943
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Lin,H.H., Yu,I.S., Cheng,M.S., Chang,T.J., Lin,H.Y., Chang,Y.C.,
            Ko,C.J., Chen,P.H., Lin,S.W., Huang,T.C., Huang,S.Y., Chen,T.Y.,
            Kan,K.W., Huang,H.P. and Lee,M.S.
  TITLE     Spint1 disruption in mouse pancreas leads to glucose intolerance
            and impaired insulin production involving HEPSIN/MAFA
  JOURNAL   Nat Commun 15 (1), 10537 (2024)
   PUBMED   39627229
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Wang,Q., Zeng,S., Liang,Y., Zhou,R. and Wang,D.
  TITLE     ASH2L Mediates Epidermal Differentiation and Hair Follicle
            Morphogenesis through H3K4me3 Modification
  JOURNAL   J Invest Dermatol 144 (11), 2406-2416 (2024)
   PUBMED   38582368
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Wang,S., Ma,Y., Li,W., Zhao,Y., Gao,Y. and Wang,S.
  TITLE     LncRNA SNHG5/IGF2BP1/Occludin axis regulates Nd2O3 induced
            blood-testis barrier disruption
  JOURNAL   Environ Pollut 358, 124527 (2024)
   PUBMED   38992831
  REMARK    GeneRIF: LncRNA SNHG5/IGF2BP1/Occludin axis regulates Nd2O3 induced
            blood-testis barrier disruption.
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Zhu,Y., Huang,Y., Tang,T. and Xie,Y.
  TITLE     HDAC1 and HDAC2 orchestrate Wnt signaling to regulate neural
            progenitor transition during brain development
  JOURNAL   iScience 27 (9), 110600 (2024)
   PUBMED   39224519
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Furuse,M., Sasaki,H., Fujimoto,K. and Tsukita,S.
  TITLE     A single gene product, claudin-1 or -2, reconstitutes tight
            junction strands and recruits occludin in fibroblasts
  JOURNAL   J Cell Biol 143 (2), 391-401 (1998)
   PUBMED   9786950
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Morita,K., Itoh,M., Saitou,M., Ando-Akatsuka,Y., Furuse,M.,
            Yoneda,K., Imamura,S., Fujimoto,K. and Tsukita,S.
  TITLE     Subcellular distribution of tight junction-associated proteins
            (occludin, ZO-1, ZO-2) in rodent skin
  JOURNAL   J Invest Dermatol 110 (6), 862-866 (1998)
   PUBMED   9620290
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Saitou,M., Fujimoto,K., Doi,Y., Itoh,M., Fujimoto,T., Furuse,M.,
            Takano,H., Noda,T. and Tsukita,S.
  TITLE     Occludin-deficient embryonic stem cells can differentiate into
            polarized epithelial cells bearing tight junctions
  JOURNAL   J Cell Biol 141 (2), 397-408 (1998)
   PUBMED   9548718
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Ohsugi,M., Larue,L., Schwarz,H. and Kemler,R.
  TITLE     Cell-junctional and cytoskeletal organization in mouse blastocysts
            lacking E-cadherin
  JOURNAL   Dev Biol 185 (2), 261-271 (1997)
   PUBMED   9187087
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Ando-Akatsuka,Y., Saitou,M., Hirase,T., Kishi,M., Sakakibara,A.,
            Itoh,M., Yonemura,S., Furuse,M. and Tsukita,S.
  TITLE     Interspecies diversity of the occludin sequence: cDNA cloning of
            human, mouse, dog, and rat-kangaroo homologues
  JOURNAL   J Cell Biol 133 (1), 43-47 (1996)
   PUBMED   8601611
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158536.2.
            
            On Feb 6, 2018 this sequence version replaced XP_006517626.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U49185.1, AK033532.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 53.23 cM"
     Protein         1..521
                     /product="occludin isoform 1"
                     /EC_number="2.1.1.67"
                     /calculated_mol_wt=58869
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61146.1)"
     Region          57..261
                     /region_name="MARVEL"
                     /note="Membrane-associating domain; pfam01284"
                     /db_xref="CDD:366555"
     Site            67..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61146.1)"
     Site            134..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61146.1)"
     Site            169..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61146.1)"
     Site            242..263
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61146.1)"
     Region          300..329
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61146.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16625; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC, in vitro.
                     /evidence=ECO:0000269|PubMed:11502742; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Region          361..405
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61146.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q16625; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q16625; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q16625; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC/PRKCH.
                     /evidence=ECO:0000250|UniProtKB:Q16625; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     Region          419..518
                     /region_name="Occludin_ELL"
                     /note="Occludin homology domain; pfam07303"
                     /db_xref="CDD:462140"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16625; propagated from
                     UniProtKB/Swiss-Prot (Q61146.1)"
     CDS             1..521
                     /gene="Ocln"
                     /gene_synonym="Ocl"
                     /coded_by="NM_001360536.1:223..1788"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS26731.1"
                     /db_xref="GeneID:18260"
                     /db_xref="MGI:MGI:106183"
ORIGIN      
        1 msvrpfespp pyrpdefkpn hyapsndmyg gemhvrpmls qpaysfyped eilhfykwts
       61 ppgvirilsm liivmciaif acvastlawd rgygtglfgg slnypysgfg ygggygggyg
      121 gygygyggyt dpraakgfll amaafcfias lvifvtsvir sgmsrtrryy liviivsail
      181 gimvfiativ yimgvnptaq asgsmygsqi ymicnqfytp ggtglyvdqy lyhycvvdpq
      241 eaiaivlgfm iivafaliif favktrrkmd rydksnilwd kehiydeqpp nveewvknvs
      301 agtqdmpppp sdyaervdsp mayssngkvn gkrsypesfy kstplvpeva qeipltlsvd
      361 dfrqpryssn gnletpskra ptkgkagkgk rtdpdhyetd yttggescee leedwvreyp
      421 pitsdqqrql ykrnfdaglq eykslqaeld dvnkelsrld kelddyrees eeymaaadey
      481 nrlkqvkgsa dykskrnyck qlksklshik rmvgdydrrk p
//
LOCUS       NP_001243325             428 aa            linear   PRI 27-APR-2025
DEFINITION  ammonium transporter Rh type B isoform c [Homo sapiens].
ACCESSION   NP_001243325
VERSION     NP_001243325.1
DBSOURCE    REFSEQ: accession NM_001256396.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Mishra,S., Welch,N., Singh,S.S., Singh,K.D., Bellar,A., Kumar,A.,
            Deutz,L.N., Hanlon,M.D., Kant,S., Dastidar,S., Patel,H.,
            Agrawal,V., Attaway,A.H., Musich,R., Stark,G.R., Tedesco,F.S.,
            Truskey,G.A., Weiner,I.D., Karnik,S.S. and Dasarathy,S.
  TITLE     Ammonia transporter RhBG initiates downstream signaling and
            functional responses by activating NFkappaB
  JOURNAL   Proc Natl Acad Sci U S A 121 (31), e2314760121 (2024)
   PUBMED   39052834
  REMARK    GeneRIF: Ammonia transporter RhBG initiates downstream signaling
            and functional responses by activating NFkappaB.
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Sohet,F., Colin,Y., Genetet,S., Ripoche,P., Metral,S., Le Van
            Kim,C. and Lopez,C.
  TITLE     Phosphorylation and ankyrin-G binding of the C-terminal domain
            regulate targeting and function of the ammonium transporter RhBG
  JOURNAL   J Biol Chem 283 (39), 26557-26567 (2008)
   PUBMED   18635543
  REMARK    GeneRIF: Phosphorylation and ankyrin-G binding of the C-terminal
            domain regulate targeting and function of the ammonium transporter
            RhBG
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Huang,C.H. and Peng,J.
  TITLE     Evolutionary conservation and diversification of Rh family genes
            and proteins
  JOURNAL   Proc Natl Acad Sci U S A 102 (43), 15512-15517 (2005)
   PUBMED   16227429
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Zidi-Yahiaoui,N., Mouro-Chanteloup,I., D'Ambrosio,A.M., Lopez,C.,
            Gane,P., Le van Kim,C., Cartron,J.P., Colin,Y. and Ripoche,P.
  TITLE     Human Rhesus B and Rhesus C glycoproteins: properties of
            facilitated ammonium transport in recombinant kidney cells
  JOURNAL   Biochem J 391 (Pt 1), 33-40 (2005)
   PUBMED   15929723
  REMARK    GeneRIF: RhBG and RhCG facilitate ammonium movement across the
            plasma membrane; these results favor the hypothesis that these Rh
            glycoproteins, together with their homolog RhAG, constitute a
            family of NH3 channels in mammalian cells.
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Lopez,C., Metral,S., Eladari,D., Drevensek,S., Gane,P.,
            Chambrey,R., Bennett,V., Cartron,J.P., Le Van Kim,C. and Colin,Y.
  TITLE     The ammonium transporter RhBG: requirement of a tyrosine-based
            signal and ankyrin-G for basolateral targeting and membrane
            anchorage in polarized kidney epithelial cells
  JOURNAL   J Biol Chem 280 (9), 8221-8228 (2005)
   PUBMED   15611082
  REMARK    GeneRIF: RhBG requires a tyrosine-based signal and ankyrin-G for
            basolateral targeting and membrane
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Quentin,F., Eladari,D., Cheval,L., Lopez,C., Goossens,D., Colin,Y.,
            Cartron,J.P., Paillard,M. and Chambrey,R.
  TITLE     RhBG and RhCG, the putative ammonia transporters, are expressed in
            the same cells in the distal nephron
  JOURNAL   J Am Soc Nephrol 14 (3), 545-554 (2003)
   PUBMED   12595489
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Liu,Z., Peng,J., Mo,R., Hui,C. and Huang,C.H.
  TITLE     Rh type B glycoprotein is a new member of the Rh superfamily and a
            putative ammonia transporter in mammals
  JOURNAL   J Biol Chem 276 (2), 1424-1433 (2001)
   PUBMED   11024028
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Huang,C.H. and Liu,P.Z.
  TITLE     New insights into the Rh superfamily of genes and proteins in
            erythroid cells and nonerythroid tissues
  JOURNAL   Blood Cells Mol Dis 27 (1), 90-101 (2001)
   PUBMED   11358367
  REMARK    Review article
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Liu,Z., Chen,Y., Mo,R., Hui,C., Cheng,J.F., Mohandas,N. and
            Huang,C.H.
  TITLE     Characterization of human RhCG and mouse Rhcg as novel nonerythroid
            Rh glycoprotein homologues predominantly expressed in kidney and
            testis
  JOURNAL   J Biol Chem 275 (33), 25641-25651 (2000)
   PUBMED   10852913
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL589685.17 and AY139093.1.
            
            Summary: This gene encodes one of two non-erythroid members of the
            Rhesus (Rh) protein family. Non-erythroid Rh protein family members
            are mainly expressed in the kidney and belong to the
            methylammonium-ammonium permease/ammonia transporters superfamily.
            All Rh family proteins are predicted to be transmembrane proteins
            with 12 membrane spanning domains and intracytoplasmic N- and
            C-termini. Alternative splicing of this gene results in multiple
            transcript variants. [provided by RefSeq, Jan 2012].
            
            Transcript Variant: This variant (3) uses the same exon combination
            as variant 10 but represents the allele encoded by the GRCh38
            reference genome. The encoded isoform (c) has a frameshifted
            C-terminus compared to isoform f.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY139093.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..428
                     /product="ammonium transporter Rh type B isoform c"
                     /note="Rhesus blood group, B glycoprotein; ammonium
                     transporter Rh type B; solute carrier family 42 member 2"
                     /calculated_mol_wt=45794
     Region          28..330
                     /region_name="Ammonium_transp"
                     /note="Ammonium Transporter Family; cl03012"
                     /db_xref="CDD:445985"
     CDS             1..428
                     /gene="RHBG"
                     /gene_synonym="SLC42A2"
                     /coded_by="NM_001256396.2:203..1489"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:57127"
                     /db_xref="HGNC:HGNC:14572"
                     /db_xref="MIM:607079"
ORIGIN      
        1 mnftfatqks ltllprlecn gaisahcnlh lpgfqdvham vfvgfgflmv flqrygfssv
       61 gftfllaafa lqwstlvqgf lhsfhgghih vgvesminad fcagavlisf gavlgktgpt
      121 qlllmallev vlfginefvl lhllgvrdag gsmtihtfga yfglvlsrvl yrpqlekskh
      181 rqgsvyhsdl famigtiflw ifwpsfnaal talgagqhrt alntyyslaa stlgtfalsa
      241 lvgedgrldm vhiqnaalag gvvvgtssem mltpfgalaa gflagtvstl gykfftpile
      301 skfkvqdtcg vhnlhgmpgv lgallgvlva glatheaygd glesvfplia egqrsatsqa
      361 mhqlfglfvt lmfasvgggl gglllklpfl dsppdsqhye dqvhwqvpge hedkaqrplr
      421 veeadtqa
//
LOCUS       NP_001354506              80 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 138 isoform 12 [Homo sapiens].
ACCESSION   NP_001354506
VERSION     NP_001354506.1
DBSOURCE    REFSEQ: accession NM_001367577.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073349.11.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.171885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2146982
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..80
                     /product="zinc finger protein 138 isoform 12"
                     /note="zinc finger protein 138 (clone pHZ-32)"
                     /calculated_mol_wt=9408
     Region          4..57
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     CDS             1..80
                     /gene="ZNF138"
                     /gene_synonym="pHZ-32"
                     /coded_by="NM_001367577.1:142..384"
                     /note="isoform 12 is encoded by transcript variant 15"
                     /db_xref="GeneID:7697"
                     /db_xref="HGNC:HGNC:12922"
                     /db_xref="MIM:604080"
ORIGIN      
        1 mgpltfmdva iefsleewqc ldtaqrnvyr hvmlenyrnl vfldlitcle qgkepwnmkr
       61 hemvvakhsg lwksrtsprl
//
LOCUS       NP_006537                577 aa            linear   PRI 27-APR-2025
DEFINITION  insulin-like growth factor 2 mRNA-binding protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_006537
VERSION     NP_006537.3
DBSOURCE    REFSEQ: accession NM_006546.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Luo,J., Yang,C., Xu,S., Ji,Z., Zhang,Y., Bai,H., Deng,Z., Liang,J.,
            Huang,Y., Zhi,E., Tian,R., Li,P., Zhao,F., Zhou,Z., Li,Z. and
            Yao,C.
  TITLE     RNA-binding protein IGF2BP1 is required for spermatogenesis in an
            age-dependent manner
  JOURNAL   Commun Biol 7 (1), 1362 (2024)
   PUBMED   39433965
  REMARK    GeneRIF: RNA-binding protein IGF2BP1 is required for
            spermatogenesis in an age-dependent manner.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Bai,W., Xiao,G., Xie,G., Chen,Z., Xu,X., Zeng,J. and Xie,J.
  TITLE     METTL3/IGF2BP1 influences the development of non-small-cell lung
            cancer by mediating m6A methylation modification of TRPV1
  JOURNAL   Thorac Cancer 15 (26), 1871-1881 (2024)
   PUBMED   39090761
  REMARK    GeneRIF: METTL3/IGF2BP1 influences the development of
            non-small-cell lung cancer by mediating m6A methylation
            modification of TRPV1.
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Zhang,Q., Du,Z., Zhou,W., Li,W., Yang,Q., Yu,H. and Liu,T.
  TITLE     ZDHHC1 downregulates LIPG and inhibits colorectal cancer growth via
            IGF2BP1 Palmitoylation
  JOURNAL   Cancer Gene Ther 31 (9), 1427-1437 (2024)
   PUBMED   39069526
  REMARK    GeneRIF: ZDHHC1 downregulates LIPG and inhibits colorectal cancer
            growth via IGF2BP1 Palmitoylation.
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Leclair,N.K., Lucas,C.G., Mirchia,K., McCortney,K., Horbinski,C.M.,
            Raleigh,D.R. and Anczukow,O.
  TITLE     The RNA-binding protein IGF2BP1 regulates stability of mRNA
            transcribed from FOXM1 target genes in hypermitotic meningiomas
  JOURNAL   Acta Neuropathol 148 (1), 28 (2024)
   PUBMED   39179895
  REMARK    GeneRIF: The RNA-binding protein IGF2BP1 regulates stability of
            mRNA transcribed from FOXM1 target genes in hypermitotic
            meningiomas.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Xiao,B., Li,Y., Yang,Y., Chen,C., Gong,S., Li,H., Yao,Q. and
            Wang,L.
  TITLE     METTL3 and IGF2BP1-Mediated m6A Modification of ZHX2 Promotes Tumor
            Property of Renal Cell Carcinoma
  JOURNAL   Kidney Blood Press Res 49 (1), 787-798 (2024)
   PUBMED   39159608
  REMARK    GeneRIF: METTL3 and IGF2BP1-Mediated m6A Modification of ZHX2
            Promotes Tumor Property of Renal Cell Carcinoma.
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Runge,S., Nielsen,F.C., Nielsen,J., Lykke-Andersen,J., Wewer,U.M.
            and Christiansen,J.
  TITLE     H19 RNA binds four molecules of insulin-like growth factor II
            mRNA-binding protein
  JOURNAL   J Biol Chem 275 (38), 29562-29569 (2000)
   PUBMED   10875929
REFERENCE   7  (residues 1 to 577)
  AUTHORS   Doyle,G.A., Bourdeau-Heller,J.M., Coulthard,S., Meisner,L.F. and
            Ross,J.
  TITLE     Amplification in human breast cancer of a gene encoding a c-myc
            mRNA-binding protein
  JOURNAL   Cancer Res 60 (11), 2756-2759 (2000)
   PUBMED   10850408
REFERENCE   8  (residues 1 to 577)
  AUTHORS   Nielsen,J., Christiansen,J., Lykke-Andersen,J., Johnsen,A.H.,
            Wewer,U.M. and Nielsen,F.C.
  TITLE     A family of insulin-like growth factor II mRNA-binding proteins
            represses translation in late development
  JOURNAL   Mol Cell Biol 19 (2), 1262-1270 (1999)
   PUBMED   9891060
REFERENCE   9  (residues 1 to 577)
  AUTHORS   Doyle,G.A., Betz,N.A., Leeds,P.F., Fleisig,A.J., Prokipcak,R.D. and
            Ross,J.
  TITLE     The c-myc coding region determinant-binding protein: a member of a
            family of KH domain RNA-binding proteins
  JOURNAL   Nucleic Acids Res 26 (22), 5036-5044 (1998)
   PUBMED   9801297
REFERENCE   10 (residues 1 to 577)
  AUTHORS   Prokipcak,R.D., Herrick,D.J. and Ross,J.
  TITLE     Purification and properties of a protein that binds to the
            C-terminal coding region of human c-myc mRNA
  JOURNAL   J Biol Chem 269 (12), 9261-9269 (1994)
   PUBMED   8132663
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091133.11, BP238821.1,
            AF198254.1, AK074915.1 and AC105030.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 3, 2004 this sequence version replaced NP_006537.2.
            
            Summary: This gene encodes a member of the insulin-like growth
            factor 2 mRNA-binding protein family. The protein encoded by this
            gene contains four K homology domains and two RNA recognition
            motifs. It functions by binding to the mRNAs of certain genes,
            including insulin-like growth factor 2, beta-actin and
            beta-transducin repeat-containing protein, and regulating their
            translation. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, May 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF198254.1, AF117106.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000290341.8/ ENSP00000290341.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..577
                     /product="insulin-like growth factor 2 mRNA-binding
                     protein 1 isoform 1"
                     /note="coding region determinant-binding protein;
                     zipcode-binding protein 1; VICKZ family member 1; IGF2
                     mRNA-binding protein 1; ZBP-1; IGF-II mRNA-binding protein
                     1; insulin-like growth factor 2 mRNA binding protein 1
                     deltaN CRDBP"
                     /calculated_mol_wt=63350
     Region          1..77
                     /region_name="RRM1_IGF2BP1"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     insulin-like growth factor 2 mRNA-binding protein 1
                     (IGF2BP1); cd12625"
                     /db_xref="CDD:241069"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZI8.2)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZI8.2)"
     Region          81..156
                     /region_name="RRM2_IGF2BP1"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     insulin-like growth factor 2 mRNA-binding protein 1
                     (IGF2BP1); cd12628"
                     /db_xref="CDD:410037"
     Region          160..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZI8.2)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZI8.2)"
     Region          197..272
                     /region_name="KH-I_IGF2BP1_rpt1"
                     /note="first type I K homology (KH) RNA-binding domain
                     found in insulin-like growth factor 2 mRNA-binding protein
                     1 (IGF2BP1) and similar proteins; cd22490"
                     /db_xref="CDD:411918"
     Site            order(205,207..209,211..215,218..219,222..223,228..231)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411918"
     Region          273..369
                     /region_name="KH-I_IGF2BP1_rpt2"
                     /note="second type I K homology (KH) RNA-binding domain
                     found in insulin-like growth factor 2 mRNA-binding protein
                     1 (IGF2BP1) and similar proteins; cd22493"
                     /db_xref="CDD:411921"
     Site            order(286,288..290,292..296,299..300,303..304,309..312)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411921"
     Region          310..324
                     /region_name="Sufficient for nuclear export"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZI8.2)"
     Region          404..479
                     /region_name="KH-I_IGF2BP1_rpt3"
                     /note="third type I K homology (KH) RNA-binding domain
                     found in insulin-like growth factor 2 mRNA-binding protein
                     1 (IGF2BP1) and similar proteins; cd22496"
                     /db_xref="CDD:411924"
     Site            order(417..419,421..425,428..429,439..443,452)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:411924"
     Region          485..495
                     /region_name="Sufficient for nuclear export"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZI8.2)"
     Region          487..562
                     /region_name="KH-I_IGF2BP1_rpt4"
                     /note="fourth type I K homology (KH) RNA-binding domain
                     found in insulin-like growth factor 2 mRNA-binding protein
                     1 (IGF2BP1) and similar proteins; cd22499"
                     /db_xref="CDD:411927"
     Site            order(500..501,503..507,510,521..527)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:411927"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZI8.2)"
     CDS             1..577
                     /gene="IGF2BP1"
                     /gene_synonym="CRD-BP; CRDBP; IMP-1; IMP1; VICKZ1; ZBP1"
                     /coded_by="NM_006546.4:362..2095"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11543.1"
                     /db_xref="GeneID:10642"
                     /db_xref="HGNC:HGNC:28866"
                     /db_xref="MIM:608288"
ORIGIN      
        1 mnklyignln esvtpadlek vfaehkisys gqflvksgya fvdcpdehwa mkaietfsgk
       61 velqgkrlei ehsvpkkqrs rkiqirnipp qlrwevldsl laqygtvenc eqvnteseta
      121 vvnvtysnre qtrqaimkln ghqlenhalk vsyipdeqia qgpengrrgg fgsrgqprqg
      181 spvaagapak qqqvdiplrl lvptqyvgai igkegatirn itkqtqskid vhrkenagaa
      241 ekaisvhstp egcssackmi leimhkeakd tktadevplk ilahnnfvgr ligkegrnlk
      301 kveqdtetki tisslqdltl ynpertitvk gaienccrae qeimkkvrea yendvaamsl
      361 qshlipglnl aavglfpass savppppssv tgaapyssfm qapeqemvqv fipaqavgai
      421 igkkgqhikq lsrfasasik iappetpdsk vrmviitgpp eaqfkaqgri ygklkeenff
      481 gpkeevklet hirvpasaag rvigkggktv nelqnltaae vvvprdqtpd endqvivkii
      541 ghfyasqmaq rkirdilaqv kqqhqkgqsn qaqarrk
//
LOCUS       NP_001008543             192 aa            linear   ROD 27-APR-2025
DEFINITION  max-interacting protein 1 isoform c [Mus musculus].
ACCESSION   NP_001008543
VERSION     NP_001008543.1
DBSOURCE    REFSEQ: accession NM_001008543.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Li,X., Xiao,S., Li,F., Fang,K., Wen,J. and Gong,H.
  TITLE     Max interacting protein 1 induces IL-17-producing T
            helper/regulatory T imbalance in osteoarthritis by upregulating
            tectonic family member 2
  JOURNAL   Tissue Cell 78, 101906 (2022)
   PUBMED   36049372
  REMARK    GeneRIF: Max interacting protein 1 induces IL-17-producing T
            helper/regulatory T imbalance in osteoarthritis by upregulating
            tectonic family member 2.
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Menendez-Montes,I., Escobar,B., Palacios,B., Gomez,M.J.,
            Izquierdo-Garcia,J.L., Flores,L., Jimenez-Borreguero,L.J.,
            Aragones,J., Ruiz-Cabello,J., Torres,M. and Martin-Puig,S.
  TITLE     Myocardial VHL-HIF Signaling Controls an Embryonic Metabolic Switch
            Essential for Cardiac Maturation
  JOURNAL   Dev Cell 39 (6), 724-739 (2016)
   PUBMED   27997827
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Cui,W., Dai,X., Marcho,C., Han,Z., Zhang,K., Tremblay,K.D. and
            Mager,J.
  TITLE     Towards Functional Annotation of the Preimplantation Transcriptome:
            An RNAi Screen in Mammalian Embryos
  JOURNAL   Sci Rep 6, 37396 (2016)
   PUBMED   27869233
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Childress,P., Stayrook,K.R., Alvarez,M.B., Wang,Z., Shao,Y.,
            Hernandez-Buquer,S., Mack,J.K., Grese,Z.R., He,Y., Horan,D.,
            Pavalko,F.M., Warden,S.J., Robling,A.G., Yang,F.C., Allen,M.R.,
            Krishnan,V., Liu,Y. and Bidwell,J.P.
  TITLE     Genome-Wide Mapping and Interrogation of the Nmp4 Antianabolic Bone
            Axis
  JOURNAL   Mol Endocrinol 29 (9), 1269-1285 (2015)
   PUBMED   26244796
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Dugast-Darzacq,C., Pirity,M., Blanck,J.K., Scherl,A. and
            Schreiber-Agus,N.
  TITLE     Mxi1-SRalpha: a novel Mxi1 isoform with enhanced transcriptional
            repression potential
  JOURNAL   Oncogene 23 (55), 8887-8899 (2004)
   PUBMED   15467743
  REMARK    GeneRIF: Mxi1-SRalpha is an isoform with enhanced transcriptional
            repression potential
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Hurlin,P.J., Queva,C., Koskinen,P.J., Steingrimsson,E., Ayer,D.E.,
            Copeland,N.G., Jenkins,N.A. and Eisenman,R.N.
  TITLE     Mad3 and Mad4: novel Max-interacting transcriptional repressors
            that suppress c-myc dependent transformation and are expressed
            during neural and epidermal differentiation
  JOURNAL   EMBO J 14 (22), 5646-5659 (1995)
   PUBMED   8521822
  REMARK    Erratum:[EMBO J. 1996 Apr 15;15(8):2030. PMID: 8617250]
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Steingrimsson,E., Sawadogo,M., Gilbert,D.J., Zervos,A.S., Brent,R.,
            Blanar,M.A., Fisher,D.E., Copeland,N.G. and Jenkins,N.A.
  TITLE     Murine chromosomal location of five bHLH-Zip transcription factor
            genes
  JOURNAL   Genomics 28 (2), 179-183 (1995)
   PUBMED   8530024
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Schreiber-Agus,N., Chin,L., Chen,K., Torres,R., Rao,G., Guida,P.,
            Skoultchi,A.I. and DePinho,R.A.
  TITLE     An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic
            activity and interacts with a homolog of the yeast transcriptional
            repressor SIN3
  JOURNAL   Cell 80 (5), 777-786 (1995)
   PUBMED   7889571
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Shimizu,E., Shirasawa,H., Kodama,K., Koseki,K., Sato,T. and
            Simizu,B.
  TITLE     Cloning and sequencing of the murine Mxi1 cDNA
  JOURNAL   Gene 152 (2), 283-284 (1995)
   PUBMED   7835718
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Edelhoff,S., Ayer,D.E., Zervos,A.S., Steingrimsson,E.,
            Jenkins,N.A., Copeland,N.G., Eisenman,R.N., Brent,R. and
            Disteche,C.M.
  TITLE     Mapping of two genes encoding members of a distinct subfamily of
            MAX interacting proteins: MAD to human chromosome 2 and mouse
            chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome
            19
  JOURNAL   Oncogene 9 (2), 665-668 (1994)
   PUBMED   8290278
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC133451.14 and L38821.1.
            
            Summary: This gene encodes a protein containing a helix-loop-helix
            domain characteristic of transcription factors, which allows
            heterodimerization and sequence-specific DNA binding. The encoded
            protein is related to a family of Myc/Max/Mad proteins that are
            involved in the regulation of several cellular processes. The
            protein encoded by this gene is a transcriptional repressor thought
            to negatively regulate Myc function. Three alternatively spliced
            transcripts encoding different isoforms have been described.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3), also referred to as WR,
            differs in the 5' UTR and 5' coding region, compared to variant 1.
            The resulting isoform (c) is shorter and has a distinct N-terminus,
            compared to isoform a. This variant is supported by mRNAs and ESTs
            but the existence of the protein product has not been verified
            experimentally. Variants 3-6 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CO425181.1, L38821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849377, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 47.53 cM"
     Protein         1..192
                     /product="max-interacting protein 1 isoform c"
                     /note="max-interacting protein 1"
                     /calculated_mol_wt=21524
     Region          32..111
                     /region_name="bHLHzip_MXI1"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in Max-interacting protein 1 (MXI1) and similar
                     proteins; cd18930"
                     /db_xref="CDD:381500"
     Site            order(36..37,40..41,43..44,48,67..69)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381500"
     Site            order(47..48,50..55,57..58,70,73,77,79..81,83..84,86..87,
                     90,94,97..98,100..101,104..105,107..108)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381500"
     Site            order(47,50..51,53..54,57..58,70,73,77,79..81,83..84,
                     86..87,90,94,97..98,100..101,104..105,107..108)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381500"
     CDS             1..192
                     /gene="Mxi1"
                     /gene_synonym="bHLHc11; Gm10197; Mad2"
                     /coded_by="NM_001008543.3:229..807"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS38023.1"
                     /db_xref="GeneID:17859"
                     /db_xref="MGI:MGI:97245"
ORIGIN      
        1 mpsprlqhsk pprrlsraqk hssgssntst anrsthnele knrrahlrlc lerlkvlipl
       61 gpdctrhttl gllnkakahi kkleeaerks qhqlenlere qrflkrrleq lqgpqemeri
      121 rmdsigstis sdrsdseree ievdvestef shgeadsvst tsisdlddhs slqsvgsdeg
      181 yssasvklsf as
//
LOCUS       NP_037471                507 aa            linear   PRI 27-APR-2025
DEFINITION  dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
            [Homo sapiens].
ACCESSION   NP_037471
VERSION     NP_037471.2
DBSOURCE    REFSEQ: accession NM_013339.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Monson,E., Cideciyan,A.V., Roman,A.J., Sumaroka,A., Swider,M.,
            Wu,V., Viarbitskaya,I., Jacobson,S.G., Fliesler,S.J. and
            Pittler,S.J.
  TITLE     Inherited Retinal Degeneration Caused by Dehydrodolichyl
            Diphosphate Synthase Mutation-Effect of an ALG6 Modifier Variant
  JOURNAL   Int J Mol Sci 25 (2), 1004 (2024)
   PUBMED   38256083
  REMARK    GeneRIF: Inherited Retinal Degeneration Caused by Dehydrodolichyl
            Diphosphate Synthase Mutation-Effect of an ALG6 Modifier Variant.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Starosta,R.T., Tarnowski,J., Vairo,F.P.E., Raymond,K., Preston,G.
            and Morava,E.
  TITLE     Bosch-Boonstra-Schaaf optic atrophy syndrome (BBSOAS) initially
            diagnosed as ALG6-CDG: Functional evidence for benignity of the
            ALG6 c.391T>C (p.Tyr131His) variant and further expanding the
            BBSOAS phenotype
  JOURNAL   Eur J Med Genet 63 (7), 103941 (2020)
   PUBMED   32407885
  REMARK    GeneRIF: Bosch-Boonstra-Schaaf optic atrophy syndrome (BBSOAS)
            initially diagnosed as ALG6-CDG: Functional evidence for benignity
            of the ALG6 c.391T>C (p.Tyr131His) variant and further expanding
            the BBSOAS phenotype.
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Morava,E., Tiemes,V., Thiel,C., Seta,N., de Lonlay,P., de Klerk,H.,
            Mulder,M., Rubio-Gozalbo,E., Visser,G., van Hasselt,P.,
            Horovitz,D.D.G., de Souza,C.F.M., Schwartz,I.V.D., Green,A.,
            Al-Owain,M., Uziel,G., Sigaudy,S., Chabrol,B., van Spronsen,F.J.,
            Steinert,M., Komini,E., Wurm,D., Bevot,A., Ayadi,A., Huijben,K.,
            Dercksen,M., Witters,P., Jaeken,J., Matthijs,G., Lefeber,D.J. and
            Wevers,R.A.
  TITLE     ALG6-CDG: a recognizable phenotype with epilepsy, proximal muscle
            weakness, ataxia and behavioral and limb anomalies
  JOURNAL   J Inherit Metab Dis 39 (5), 713-723 (2016)
   PUBMED   27287710
  REMARK    GeneRIF: ALG6-CDG has been now described in 89 patients.
            Erratum:[J Inherit Metab Dis. 2016 Sep;39(5):759. doi:
            10.1007/s10545-016-9967-4. PMID: 27498540]
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Shrimal,S. and Gilmore,R.
  TITLE     Reduced expression of the oligosaccharyltransferase exacerbates
            protein hypoglycosylation in cells lacking the fully assembled
            oligosaccharide donor
  JOURNAL   Glycobiology 25 (7), 774-783 (2015)
   PUBMED   25792706
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Imbach,T., Grunewald,S., Schenk,B., Burda,P., Schollen,E.,
            Wevers,R.A., Jaeken,J., de Klerk,J.B., Berger,E.G., Matthijs,G.,
            Aebi,M. and Hennet,T.
  TITLE     Multi-allelic origin of congenital disorder of glycosylation
            (CDG)-Ic
  JOURNAL   Hum Genet 106 (5), 538-545 (2000)
   PUBMED   10914684
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Imbach,T., Burda,P., Kuhnert,P., Wevers,R.A., Aebi,M., Berger,E.G.
            and Hennet,T.
  TITLE     A mutation in the human ortholog of the Saccharomyces cerevisiae
            ALG6 gene causes carbohydrate-deficient glycoprotein syndrome
            type-Ic
  JOURNAL   Proc Natl Acad Sci U S A 96 (12), 6982-6987 (1999)
   PUBMED   10359825
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Korner,C., Knauer,R., Holzbach,U., Hanefeld,F., Lehle,L. and von
            Figura,K.
  TITLE     Carbohydrate-deficient glycoprotein syndrome type V: deficiency of
            dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase
  JOURNAL   Proc Natl Acad Sci U S A 95 (22), 13200-13205 (1998)
   PUBMED   9789065
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Burda,P., Borsig,L., de Rijk-van Andel,J., Wevers,R., Jaeken,J.,
            Carchon,H., Berger,E.G. and Aebi,M.
  TITLE     A novel carbohydrate-deficient glycoprotein syndrome characterized
            by a deficiency in glucosylation of the dolichol-linked
            oligosaccharide
  JOURNAL   J Clin Invest 102 (4), 647-652 (1998)
   PUBMED   9710431
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI819904.1, BC001253.1 and
            AL592218.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 29, 2003 this sequence version replaced NP_037471.1.
            
            Summary: This gene encodes a member of the ALG6/ALG8
            glucosyltransferase family. The encoded protein catalyzes the
            addition of the first glucose residue to the growing lipid-linked
            oligosaccharide precursor of N-linked glycosylation. Mutations in
            this gene are associated with congenital disorders of glycosylation
            type Ic. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.116787.1,
                                           SRR1803612.162459.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263440.6/ ENSP00000263440.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..507
                     /product="dolichyl pyrophosphate Man9GlcNAc2
                     alpha-1,3-glucosyltransferase"
                     /EC_number="2.4.1.267"
                     /note="Man(9)GlcNAc(2)-PP-Dol
                     alpha-1,3-glucosyltransferase; asparagine-linked
                     glycosylation 6 homolog (S. cerevisiae,
                     alpha-1,3-glucosyltransferase); asparagine-linked
                     glycosylation 6 homolog (yeast,
                     alpha-1,3-glucosyltransferase);
                     dolichyl-P-Glc:Man9GlcNAc2-PP-dolichylglucosyltransferase;
                     asparagine-linked glycosylation protein 6 homolog;
                     dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl
                     glucosyltransferase; dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol
                     alpha-1,3-glucosyltransferase; asparagine-linked
                     glycosylation 6, alpha-1,3-glucosyltransferase homolog;
                     dolichyl-P-Glc:Man(9)GlcNAc(2)-PP-dolichol alpha-
                     1->3-glucosyltransferase"
                     /calculated_mol_wt=57990
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     Region          32..488
                     /region_name="Alg6_Alg8"
                     /note="ALG6, ALG8 glycosyltransferase family; pfam03155"
                     /db_xref="CDD:460831"
     Site            59
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y672.2)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     Site            324..344
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     Site            362..382
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     Site            388..408
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     Site            438..458
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     Site            473..493
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y672.2)"
     CDS             1..507
                     /gene="ALG6"
                     /gene_synonym="CDG1C"
                     /coded_by="NM_013339.4:269..1792"
                     /db_xref="CCDS:CCDS30735.1"
                     /db_xref="GeneID:29929"
                     /db_xref="HGNC:HGNC:23157"
                     /db_xref="MIM:604566"
ORIGIN      
        1 mekwylmtvv vligltvrwt vslnsysgag kppmfgdyea qrhwqeitfn lpvkqwyfns
       61 sdnnlqywgl dyppltayhs llcayvakfi npdwialhts rgyesqahkl fmrttvliad
      121 lliyipavvl yccclkeist kkkianalci llypglilid yghfqynsvs lgfalwgvlg
      181 iscdcdllgs lafclainyk qmelyhalpf fcfllgkcfk kglkgkgfvl lvklacivva
      241 sfvlcwlpff tereqtlqvl rrlfpvdrgl fedkvaniwc sfnvflkikd ilprhiqlim
      301 sfcstflsll paciklilqp sskgfkftlv scalsfflfs fqvheksill vslpvclvls
      361 eipfmstwfl lvstfsmlpl llkdellmps vvttmaffia cvtsfsifek tseeelqlks
      421 fsisvrkylp cftflsriiq ylflisvitm vlltlmtvtl dppqklpdlf svlvcfvscl
      481 nflfflvyfn iiimwdsksg rnqkkis
//
LOCUS       NP_443084                463 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 486 [Homo sapiens].
ACCESSION   NP_443084 XP_371152 XP_943273
VERSION     NP_443084.2
DBSOURCE    REFSEQ: accession NM_052852.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC027608.1 and AC011447.7.
            
            On or before Jul 1, 2007 this sequence version replaced
            XP_371152.3, XP_943273.2, NP_443084.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA784812.1, SRR1803617.272759.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335117.9/ ENSP00000335042.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p12"
     Protein         1..463
                     /product="zinc finger protein 486"
                     /note="KRAB box only protein 2; KRAB domain only 2; KRAB
                     domain only protein 2"
                     /calculated_mol_wt=53500
     Region          13..71
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          155..176
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          188..>463
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          188..204
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          212..232
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(217,219,221,223..224,227..228,231,245,247,251..252,
                     255..256,259,273,275,277,279..280,283..284,287)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          240..260
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          268..288
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          296..316
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          324..344
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          352..372
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          380..400
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(385,387,389,391..392,395..396,399,413,415,419..420,
                     423..424,427,441,443,445,447..448,451..452,455)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          408..428
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          436..456
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..463
                     /gene="ZNF486"
                     /gene_synonym="KRBO2"
                     /coded_by="NM_052852.4:118..1509"
                     /db_xref="CCDS:CCDS46029.1"
                     /db_xref="GeneID:90649"
                     /db_xref="HGNC:HGNC:20807"
ORIGIN      
        1 mpgplrslem eslqfrdvav efsleewhcl dtaqqnlyrd vmlenyrhlv flgiivskpd
       61 litcleqgik pltmkrhemi akppvvcshf aqdlwpeqsi kdsyqkvilr kfekcghgnl
      121 hfkkgcesvd ecklhkrgyn glnqcltttq skifqcgkyv kvfhqfsnsk rhkrrhtekk
      181 plkyiegdka fnqssthtth kkidtgekpy kceecgkafn rsshltthki thtrekpykc
      241 eecgkvfkyf ssftthkkih sgekpyicee cgkafmypyt ltthkiihtg eqpykckecd
      301 kafnhpatls shkkihtgek pytcdkcgka fisssilskh ekihtgekpy kceecgkaft
      361 rsshltmhki ihtgekpykc eecgkaftws aglhkhrrth tgekpykcee cgkayttssn
      421 ltehktthtg ekpykckecg kafnwssdln khkrihigqk prt
//
LOCUS       NP_001346297             643 aa            linear   ROD 27-APR-2025
DEFINITION  cytosolic endo-beta-N-acetylglucosaminidase isoform 2 [Mus
            musculus].
ACCESSION   NP_001346297
VERSION     NP_001346297.1
DBSOURCE    REFSEQ: accession NM_001359368.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Yoshida,Y., Asahina,M., Murakami,A., Kawawaki,J., Yoshida,M.,
            Fujinawa,R., Iwai,K., Tozawa,R., Matsuda,N., Tanaka,K. and
            Suzuki,T.
  TITLE     Loss of peptide:N-glycanase causes proteasome dysfunction mediated
            by a sugar-recognizing ubiquitin ligase
  JOURNAL   Proc Natl Acad Sci U S A 118 (27) (2021)
   PUBMED   34215698
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Maynard,J.C., Fujihira,H., Dolgonos,G.E., Suzuki,T. and
            Burlingame,A.L.
  TITLE     Cytosolic N-GlcNAc proteins are formed by the action of
            endo-beta-N-acetylglucosaminidase
  JOURNAL   Biochem Biophys Res Commun 530 (4), 719-724 (2020)
   PUBMED   32782141
  REMARK    GeneRIF: Cytosolic N-GlcNAc proteins are formed by the action of
            endo-beta-N-acetylglucosaminidase.
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Fujihira,H., Masahara-Negishi,Y., Akimoto,Y., Hirayama,H.,
            Lee,H.C., Story,B.A., Mueller,W.F., Jakob,P., Clauder-Munster,S.,
            Steinmetz,L.M., Radhakrishnan,S.K., Kawakami,H., Kamada,Y.,
            Miyoshi,E., Yokomizo,T. and Suzuki,T.
  TITLE     Liver-specific deletion of Ngly1 causes abnormal nuclear morphology
            and lipid metabolism under food stress
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1866 (3), 165588 (2020)
   PUBMED   31733337
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Fujihira,H., Masahara-Negishi,Y., Tamura,M., Huang,C., Harada,Y.,
            Wakana,S., Takakura,D., Kawasaki,N., Taniguchi,N., Kondoh,G.,
            Yamashita,T., Funakoshi,Y. and Suzuki,T.
  TITLE     Lethality of mice bearing a knockout of the Ngly1-gene is partially
            rescued by the additional deletion of the Engase gene
  JOURNAL   PLoS Genet 13 (4), e1006696 (2017)
   PUBMED   28426790
  REMARK    GeneRIF: These observations strongly suggest that the Ngly1- or
            Ngly1/Engase-deficient mice could serve as a valuable animal model
            for studies related to the pathogenesis of the NGLY1-deficiency,
            and that cytoplasmic ENGase represents one of the potential
            therapeutic targets for this genetic disorder.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Harada,Y., Huang,C., Yamaki,S., Dohmae,N. and Suzuki,T.
  TITLE     Non-lysosomal Degradation of Singly Phosphorylated Oligosaccharides
            Initiated by the Action of a Cytosolic
            Endo-beta-N-acetylglucosaminidase
  JOURNAL   J Biol Chem 291 (15), 8048-8058 (2016)
   PUBMED   26858256
  REMARK    GeneRIF: ENGase efficiently hydrolyzes phosphorylated
            oligosaccharides that are larger than Man4GlcNAc2-P, generating
            GlcNAc-1-P and neutral Gn1-type free oligosaccharides.
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Huang,C., Harada,Y., Hosomi,A., Masahara-Negishi,Y., Seino,J.,
            Fujihira,H., Funakoshi,Y., Suzuki,T., Dohmae,N. and Suzuki,T.
  TITLE     Endo-beta-N-acetylglucosaminidase forms N-GlcNAc protein aggregates
            during ER-associated degradation in Ngly1-defective cells
  JOURNAL   Proc Natl Acad Sci U S A 112 (5), 1398-1403 (2015)
   PUBMED   25605922
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY070749.1, AK048667.1 and BC060640.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849374,
                              SAMN00849375 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 83.21 cM"
     Protein         1..643
                     /product="cytosolic endo-beta-N-acetylglucosaminidase
                     isoform 2"
                     /EC_number="3.2.1.96"
                     /note="cytosolic endo-beta-N-acetylglucosaminidase"
                     /calculated_mol_wt=72239
     Region          27..337
                     /region_name="GH85_ENGase"
                     /note="Endo-beta-N-acetylglucosaminidase (ENGase)
                     hydrolyzes the N-N'-diacetylchitobiosyl core of
                     N-glycosylproteins. The beta-1,4-glycosyl bond located
                     between two N-acetylglucosamine residues is hydrolyzed
                     such that N-acetylglucosamine 1 remains with the...;
                     cd06547"
                     /db_xref="CDD:119364"
     Site            order(35,62,134,136,138,203,205..206)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:119364"
     CDS             1..643
                     /gene="Engase"
                     /gene_synonym="C130099A03; D230014K01Rik"
                     /coded_by="NM_001359368.1:424..2355"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:217364"
                     /db_xref="MGI:MGI:2443788"
ORIGIN      
        1 medgfnvale plvcrrppls sprprtllch dmmggyledr fiqgsevqnp ysfyhwqyid
       61 ifvyfshhtv tippvcwtna ahrhgvcvlg tfitewqegg rlceaflagd epsfqavadr
      121 lvqiaqffrf dgwliniens ltpaavrntp lflqyltaql hqqvpgglvl wydsvvqsgq
      181 lkwqdelndq nrvffdscdg fftnynwred hlqrmvaqag erladvyvgv dvfarsnvvg
      241 grfdtdksle lirkhgfsaa lfapgwvyec leksdffqnq dkfwsllerf lpthsicslp
      301 fvtsfclglg trrvcygkeq avgpwyhpsa qetqplfgeh klagdsrgwv kthccltdaw
      361 hggsslllrg lippevdsva vrlfslhipv ppkvflsmvy kfegstdvqv alelttgdas
      421 schvggmlvl netgsrhspr plrvpptrla rwasscgqql sggwiqrcye vnlrgcllqd
      481 llvsfsrppg sreeesficr lgeiqvvdas sllaplprvq nvtisqirwl plitgseglp
      541 trlllsctlh wsylllrarc frihcwkrtg ssssvaespe tekptflgla fanqyrvvdl
      601 aveaagfgqd grveflvepv pregflvpqa ewgkavllfs vpq
//
LOCUS       NP_064601                650 aa            linear   PRI 27-APR-2025
DEFINITION  aminopeptidase B isoform a [Homo sapiens].
ACCESSION   NP_064601
VERSION     NP_064601.3
DBSOURCE    REFSEQ: accession NM_020216.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Malinauskas,M., Wallenius,V., Fandriks,L. and Casselbrant,A.
  TITLE     Local expression of AP/AngIV/IRAP and effect of AngIV on
            glucose-induced epithelial transport in human jejunal mucosa
  JOURNAL   J Renin Angiotensin Aldosterone Syst 16 (4), 1101-1108 (2015)
   PUBMED   26311161
  REMARK    GeneRIF: The substrate Angiotensin II, the enzymes
            aminopeptidases-A, B, M as well as IRAP were detected in the
            jejunal mucosa.
REFERENCE   3  (residues 1 to 650)
  AUTHORS   Fernandez-Atucha,A., Echevarria,E., Larrinaga,G., Gil,J.,
            Martinez-Cengotitabengoa,M., Gonzalez-Pinto,A.M., Irazusta,J. and
            Seco,J.
  TITLE     Plasma peptidases as prognostic biomarkers in patients with
            first-episode psychosis
  JOURNAL   Psychiatry Res 228 (2), 197-202 (2015)
   PUBMED   25997998
  REMARK    GeneRIF: these results suggest a pathophysiological involvement of
            plasma peptidases and indicate that aminopeptidase activity can
            predict the course of first-episode psychosis patients, acting as a
            prognostic indicator
REFERENCE   4  (residues 1 to 650)
  AUTHORS   Perez,I., Blanco,L., Sanz,B., Errarte,P., Ariz,U., Beitia,M.,
            Fernandez,A., Loizate,A., Candenas,M.L., Pinto,F.M., Gil,J.,
            Lopez,J.I. and Larrinaga,G.
  TITLE     Altered Activity and Expression of Cytosolic Peptidases in
            Colorectal Cancer
  JOURNAL   Int J Med Sci 12 (6), 458-467 (2015)
   PUBMED   26078706
  REMARK    GeneRIF: cytosolic peptidases(puromycin-sensitive aminopeptidase
            (PSA), aminopeptidase B (APB) and pyroglutamyl-peptidase I (PGI) )
            may be involved in colorectal carcinogenesis
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 650)
  AUTHORS   Cadel,S., Darmon,C., Pernier,J., Herve,G. and Foulon,T.
  TITLE     The M1 family of vertebrate aminopeptidases: role of evolutionarily
            conserved tyrosines in the enzymatic mechanism of aminopeptidase B
  JOURNAL   Biochimie 109, 67-77 (2015)
   PUBMED   25530263
  REMARK    GeneRIF: Data indicate that the importance of hydrogen bonds in
            aminopeptidase B (Ap-B) is verified by the Y229H substitution,
            which preserves the enzyme activity.
REFERENCE   6  (residues 1 to 650)
  AUTHORS   Foulon,T., Cadel,S. and Cohen,P.
  TITLE     Aminopeptidase B (EC 3.4.11.6)
  JOURNAL   Int J Biochem Cell Biol 31 (7), 747-750 (1999)
   PUBMED   10467730
  REMARK    Review article
REFERENCE   7  (residues 1 to 650)
  AUTHORS   Balogh,A., Cadel,S., Foulon,T., Picart,R., Der Garabedian,A.,
            Rousselet,A., Tougard,C. and Cohen,P.
  TITLE     Aminopeptidase B: a processing enzyme secreted and associated with
            the plasma membrane of rat pheochromocytoma (PC12) cells
  JOURNAL   J Cell Sci 111 (Pt 2), 161-169 (1998)
   PUBMED   9405297
REFERENCE   8  (residues 1 to 650)
  AUTHORS   Aurich-Costa,J., Cadel,S., Gouzy,C., Foulon,T., Cherif,D. and
            Cohen,P.
  TITLE     Assignment of the aminopeptidase B gene (RNPEP) to human chromosome
            1 band q32 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 143-144 (1997)
   PUBMED   9533033
REFERENCE   9  (residues 1 to 650)
  AUTHORS   Gress,T.M., Muller-Pillasch,F., Geng,M., Zimmerhackl,F.,
            Zehetner,G., Friess,H., Buchler,M., Adler,G. and Lehrach,H.
  TITLE     A pancreatic cancer-specific expression profile
  JOURNAL   Oncogene 13 (8), 1819-1830 (1996)
   PUBMED   8895530
REFERENCE   10 (residues 1 to 650)
  AUTHORS   Belhacene,N., Mari,B., Rossi,B. and Auberger,P.
  TITLE     Characterization and purification of T lymphocyte aminopeptidase B:
            a putative marker of T cell activation
  JOURNAL   Eur J Immunol 23 (8), 1948-1955 (1993)
   PUBMED   8344358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099676.2.
            
            On Dec 23, 2003 this sequence version replaced NP_064601.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001064.2, SRR1163657.562267.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295640.9/ ENSP00000295640.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..650
                     /product="aminopeptidase B isoform a"
                     /EC_number="3.4.11.6"
                     /note="aminopeptidase B; arginine aminopeptidase"
                     /calculated_mol_wt=72465
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A4.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A4.2)"
     Region          24..484
                     /region_name="M1_LTA4H"
                     /note="Peptidase M1 family including Leukotriene A4
                     hydrolase catalytic domain; cd09599"
                     /db_xref="CDD:341062"
     Site            order(169,171..172,297..301,322,325..326,329,344,348,355,
                     409,414)
                     /site_type="active"
                     /db_xref="CDD:341062"
     Site            414
                     /site_type="other"
                     /note="Transition state stabilizer. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A4.2)"
     Site            446
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A4.2)"
     Region          530..644
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..650
                     /gene="RNPEP"
                     /gene_synonym="AP-B; APB"
                     /coded_by="NM_020216.4:20..1972"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1418.1"
                     /db_xref="GeneID:6051"
                     /db_xref="HGNC:HGNC:10078"
                     /db_xref="MIM:602675"
ORIGIN      
        1 masgehspgs gaarrplhsa qavdvasasn frafellhlh ldlraefgpp gpgagsrgls
       61 gtavldlrcl epegaaelrl dshpclevta aalrrerpgs eeppaepvsf ytqpfshygq
      121 alcvsfpqpc raaerlqvll tyrvgegpgv cwlapeqtag kkkpfvytqg qavlnraffp
      181 cfdtpavkyk ysalievpdg ftavmsastw ekrgpnkfff qmcqpipsyl ialaigdlvs
      241 aevgprsrvw aepclidaak eeyngvieef latgeklfgp yvwgrydllf mppsfpfggm
      301 enpcltfvtp cllagdrsla dviiheishs wfgnlvtnan wgefwlnegf tmyaqrrist
      361 ilfgaaytcl eaatgrallr qhmditgeen plnklrvkie pgvdpddtyn etpyekgfcf
      421 vsylahlvgd qdqfdsflka yvhefkfrsi laddfldfyl eyfpelkkkr vdiipgfefd
      481 rwlntpgwpp ylpdlspgds lmkpaeelaq lwaaeeldmk aieavaispw ktyqlvyfld
      541 kilqksplpp gnvkklgdty psisnarnae lrlrwgqivl kndhqedfwk vkeflhnqgk
      601 qkytlplyha mmggsevaqt laketfasta sqlhsnvvny vqqivapkgs
//
LOCUS       NP_055766                407 aa            linear   PRI 27-APR-2025
DEFINITION  protein ZNF365 isoform A [Homo sapiens].
ACCESSION   NP_055766
VERSION     NP_055766.2
DBSOURCE    REFSEQ: accession NM_014951.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Du,X., Yu,L., Wang,L., Yan,X., Xu,B., Chai,F., Li,D., Zi,J.,
            Zhang,J. and Jiang,Y.
  TITLE     Reduced Proliferative Capacity and Defense against Staphylococcus
            aureus in Human Nasal Mucosal Epithelium Lacking ZNF365
  JOURNAL   Int Arch Allergy Immunol 185 (5), 466-479 (2024)
   PUBMED   38354721
  REMARK    GeneRIF: Reduced Proliferative Capacity and Defense against
            Staphylococcus aureus in Human Nasal Mucosal Epithelium Lacking
            ZNF365.
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Ghadamgahi,S.R., Hosseinzadeh,L., Ardalan Khales,S., Nassiri,M.,
            Alidoust,M., Etemadrezaei,S., Khorshid Shamshiri,A., Homaei
            Shandiz,F., Pasdar,A. and Afzaljavan,F.
  TITLE     Potential Role of Zinc Finger 365 rs10822013 and rs10995190 in
            Mammographic Density, Sporadic Breast Cancer Risk, and Prognosis
  JOURNAL   Iran J Med Sci 48 (6), 551-562 (2023)
   PUBMED   38094285
  REMARK    GeneRIF: Potential Role of Zinc Finger 365 rs10822013 and
            rs10995190 in Mammographic Density, Sporadic Breast Cancer Risk,
            and Prognosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Urista,J., Maldonado,M., Toscano-Marquez,F., Ramirez,R.,
            Balderas-Martinez,Y.I., Becerril,C., Romero,Y., Selman,M. and
            Pardo,A.
  TITLE     Lack of ZNF365 Drives Senescence and Exacerbates Experimental Lung
            Fibrosis
  JOURNAL   Cells 11 (18), 2848 (2022)
   PUBMED   36139424
  REMARK    GeneRIF: Lack of ZNF365 Drives Senescence and Exacerbates
            Experimental Lung Fibrosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Du,X., Zhou,Y., Song,L., Wang,X. and Zhang,S.
  TITLE     Zinc finger protein 365 is a new maternal LPS-binding protein that
            defends zebrafish embryos against gram-negative bacterial
            infections
  JOURNAL   FASEB J 32 (2), 979-994 (2018)
   PUBMED   29042450
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Wang,Q., Du,X., Meinkoth,J., Hirohashi,Y., Zhang,H., Liu,Q.,
            Richter,M. and Greene,M.I.
  TITLE     Characterization of Su48, a centrosome protein essential for cell
            division
  JOURNAL   Proc Natl Acad Sci U S A 103 (17), 6512-6517 (2006)
   PUBMED   16617106
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Gianfrancesco,F., Esposito,T., Casu,G., Maninchedda,G., Roberto,R.
            and Pirastu,M.
  TITLE     Emergence of Talanin protein associated with human uric acid
            nephrolithiasis in the Hominidae lineage
  JOURNAL   Gene 339, 131-138 (2004)
   PUBMED   15363853
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Gianfrancesco,F., Esposito,T., Ombra,M.N., Forabosco,P.,
            Maninchedda,G., Fattorini,M., Casula,S., Vaccargiu,S., Casu,G.,
            Cardia,F., Deiana,I., Melis,P., Falchi,M. and Pirastu,M.
  TITLE     Identification of a novel gene and a common variant associated with
            uric acid nephrolithiasis in a Sardinian genetic isolate
  JOURNAL   Am J Hum Genet 72 (6), 1479-1491 (2003)
   PUBMED   12740763
  REMARK    GeneRIF: A novel gene responsible for UAN was identified in an
            Italian population.
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Ombra,M.N., Forabosco,P., Casula,S., Angius,A., Maestrale,G.,
            Petretto,E., Casu,G., Colussi,G., Usai,E., Melis,P. and Pirastu,M.
  TITLE     Identification of a new candidate locus for uric acid
            nephrolithiasis
  JOURNAL   Am J Hum Genet 68 (5), 1119-1129 (2001)
   PUBMED   11309680
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC017841.1, AB020651.1,
            AC024598.7 and BC060817.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 5, 2007 this sequence version replaced NP_055766.1.
            
            Summary: This gene encodes a zinc finger protein that may play a
            role in the repair of DNA damage and maintenance of genome
            stability. The N-terminal C2H2 zinc finger motif is required to
            form a protein complex with PARP1 and MRE11, which are known to be
            involved in the restart of stalled DNA replication forks. A
            mutation in this gene may be associated with breast cancer
            susceptibility. [provided by RefSeq, Mar 2020].
            
            Transcript Variant: This variant (A) differs in the 3' coding
            region and UTR compared to variant C. The resulting protein
            (isoform A) is shorter and has a distinct C-terminus compared to
            isoform C.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070073.1, SRR1803616.176776.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395254.8/ ENSP00000378674.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.2"
     Protein         1..407
                     /product="protein ZNF365 isoform A"
                     /note="protein ZNF365; talanin; protein su48;
                     DISC1-binding zinc-finger protein"
                     /calculated_mol_wt=46411
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG89; propagated from
                     UniProtKB/Swiss-Prot (Q70YC5.3)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG89; propagated from
                     UniProtKB/Swiss-Prot (Q70YC5.3)"
     Region          <169..>290
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG89; propagated from
                     UniProtKB/Swiss-Prot (Q70YC5.3)"
     Region          347..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70YC5.3)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5PQS2; propagated from
                     UniProtKB/Swiss-Prot (Q70YC5.3)"
     CDS             1..407
                     /gene="ZNF365"
                     /gene_synonym="Su48; UAN; ZNF365D"
                     /coded_by="NM_014951.3:104..1327"
                     /note="isoform A is encoded by transcript variant A"
                     /db_xref="CCDS:CCDS31209.1"
                     /db_xref="GeneID:22891"
                     /db_xref="HGNC:HGNC:18194"
                     /db_xref="MIM:607818"
ORIGIN      
        1 mqqkafeesr ypwqesfenv avclplrcpr cgdhtrfrsl sslrahlefs hsyeertllt
       61 kcslfpslkd tdlvtssell kpgklqssgn vvkqkpsyvn lysishehsk drkpfevvae
      121 rpvsyvqtyt amdlhadsld gtrsgpglpt sdtkasfeah vrekfnrmve avdrtiekri
      181 dkltkelaqk taellevraa fvqltqkkqe vqrreralnr qvdvavemia vlrqrltese
      241 eellrkeeev vtfnhfleaa aekevqgkar lqdfienllq rvelaekqle yyqsqqasgf
      301 vrdlsghvlt dissnrkpkc lsrghphsvc nhpdlkahfh pkgrnhlkka kddrasmqpa
      361 kaiheqaess rdlcrppkkg ellgfgrkgn irpkmakkkp taivnii
//
LOCUS       NP_001138500             688 aa            linear   PRI 27-APR-2025
DEFINITION  paralemmin-3 isoform 1 [Homo sapiens].
ACCESSION   NP_001138500 XP_001726637 XP_005259948 XP_292820 XP_942391
VERSION     NP_001138500.2
DBSOURCE    REFSEQ: accession NM_001145028.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Chen,X., Wu,X., Zhao,Y., Wang,G., Feng,J., Li,Q. and Qian,G.
  TITLE     A novel binding protein of single immunoglobulin IL-1
            receptor-related molecule: Paralemmin-3
  JOURNAL   Biochem Biophys Res Commun 404 (4), 1029-1033 (2011)
   PUBMED   21187075
  REMARK    GeneRIF: These results suggest that PALM3 may function as an
            adaptor in the LPS- Toll-like receptor 4 signaling and the
            interaction of SIGIRR with PALM3 may partly account for the
            mechanism of the negatively regulatory effect of SIGIRR.
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC022098.9.
            
            On or before Nov 21, 2018 this sequence version replaced
            XP_005259948.1, NP_001138500.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2152474,
                              SAMEA2159912 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000669674.2/ ENSP00000499271.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..688
                     /product="paralemmin-3 isoform 1"
                     /calculated_mol_wt=73207
     Region          30..>102
                     /region_name="MYO6_MIU_linker"
                     /note="MIU-linker domain found in unconventional
                     myosin-VI; cl46503"
                     /db_xref="CDD:480843"
     Region          <386..>578
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          <571..>674
                     /region_name="PRK10905"
                     /note="cell division protein DamX; Validated"
                     /db_xref="CDD:236792"
     CDS             1..688
                     /gene="PALM3"
                     /coded_by="NM_001145028.2:97..2163"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46001.2"
                     /db_xref="GeneID:342979"
                     /db_xref="HGNC:HGNC:33274"
                     /db_xref="MIM:621051"
ORIGIN      
        1 malqsqvwsl atpmpmaess lyrqrlevia ekrrlqeeir aarreveeek lrverlkrks
       61 lrerwlmdga aavpepsedp tskdpqspeg qaqarirnle dslftlqsql qllqsastga
      121 qhkpsgrpsw rrqghrplsq siveagsvgq tdlnkraslp aglvgtppes psepredvlg
      181 flpgprqvpg aagdsseang pcpspiptpe qglsqravps egrvgeakgg gvvsvvwegl
      241 ratedcatga tgpeleakve evvleaigdr kgagslelpa wvkedrgive vvwegvggsd
      301 aeamgeigrv pevvqtsspr lqerleaaas iegedvpqgs pegdgqggsg geegsfiwve
      361 rvtlseewee llveglegpe vagrergdes plgaegaktg ggeetweaek rkaeesmgig
      421 seekpgtgrd eaemspvver kggekklele srgsaeklgt ereggeeplg ierkveghlr
      481 aekegdeekr gaeeeeveep lgvekkggee epeatkeple aerkggeetl eaekrggees
      541 letektqgte gdlnleqgsr egsesqaeem neagpplean tetrpekegp qpqekpvgal
      601 eeegvkpqta aegqgplgda tpllaetpap eqpaecqpll qgegpsanps ahpvptyapa
      661 rqpepsapte geeasgpkqk tcqccavm
//
LOCUS       NP_055077                736 aa            linear   PRI 27-APR-2025
DEFINITION  prolyl 3-hydroxylase 3 precursor [Homo sapiens].
ACCESSION   NP_055077
VERSION     NP_055077.2
DBSOURCE    REFSEQ: accession NM_014262.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Major,J.M., Yu,K., Chung,C.C., Weinstein,S.J., Yeager,M.,
            Wheeler,W., Snyder,K., Wright,M.E., Virtamo,J., Chanock,S. and
            Albanes,D.
  TITLE     Genome-wide association study identifies three common variants
            associated with serologic response to vitamin E supplementation in
            men
  JOURNAL   J Nutr 142 (5), 866-871 (2012)
   PUBMED   22437554
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Hosgood,H.D. 3rd, Zhang,L., Shen,M., Berndt,S.I., Vermeulen,R.,
            Li,G., Yin,S., Yeager,M., Yuenger,J., Rothman,N., Chanock,S.,
            Smith,M. and Lan,Q.
  TITLE     Association between genetic variants in VEGF, ERCC3 and
            occupational benzene haematotoxicity
  JOURNAL   Occup Environ Med 66 (12), 848-853 (2009)
   PUBMED   19773279
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Shah,R., Smith,P., Purdie,C., Quinlan,P., Baker,L., Aman,P.,
            Thompson,A.M. and Crook,T.
  TITLE     The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for
            epigenetic silencing in breast cancer
  JOURNAL   Br J Cancer 100 (10), 1687-1696 (2009)
   PUBMED   19436308
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Vranka,J.A., Sakai,L.Y. and Bachinger,H.P.
  TITLE     Prolyl 3-hydroxylase 1, enzyme characterization and identification
            of a novel family of enzymes
  JOURNAL   J Biol Chem 279 (22), 23615-23621 (2004)
   PUBMED   15044469
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Ansari-Lari,M.A., Shen,Y., Muzny,D.M., Lee,W. and Gibbs,R.A.
  TITLE     Large-scale sequencing in human chromosome 12p13: experimental and
            computational gene structure determination
  JOURNAL   Genome Res 7 (3), 268-280 (1997)
   PUBMED   9074930
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Ansari-Lari,M.A., Muzny,D.M., Lu,J., Lu,F., Lilley,C.E., Spanos,S.,
            Malley,T. and Gibbs,R.A.
  TITLE     A gene-rich cluster between the CD4 and triosephosphate isomerase
            genes at human chromosome 12p13
  JOURNAL   Genome Res 6 (4), 314-326 (1996)
   PUBMED   8723724
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ430349.1 and BQ009002.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 22, 2003 this sequence version replaced NP_055077.1.
            
            Summary: The protein encoded by this gene belongs to the leprecan
            family of proteoglycans, which function as collagen prolyl
            hydroxylases that are required for proper collagen biosynthesis,
            folding and assembly. This protein, like other family members, is
            thought to reside in the endoplasmic reticulum. Epigenetic
            inactivation of this gene is associated with breast and other
            cancers, suggesting that it may function as a tumor suppressor.
            [provided by RefSeq, Aug 2013].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK025976.1, BC017217.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000290510.10/ ENSP00000478600.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..736
                     /product="prolyl 3-hydroxylase 3 precursor"
                     /EC_number="1.14.11.7"
                     /note="gene rich cluster, B; protein B;
                     procollagen-proline 3-dioxygenase; leprecan-like 2"
                     /calculated_mol_wt=79632
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2223
     mat_peptide     21..736
                     /product="Prolyl 3-hydroxylase 3. /id=PRO_0000240360"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVL6.1)"
                     /calculated_mol_wt=79632
     Region          37..70
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVL6.1)"
     Region          154..187
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVL6.1)"
     Region          216..249
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVL6.1)"
     Region          253..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVL6.1)"
     Region          316..349
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVL6.1)"
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVL6.1)"
     Site            462
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVL6.1)"
     Region          474..674
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     Region          689..736
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVL6.1)"
     Region          733..736
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU10138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVL6.1)"
     CDS             1..736
                     /gene="P3H3"
                     /gene_synonym="GRCB; HSU47926; LEPREL2"
                     /coded_by="NM_014262.5:35..2245"
                     /db_xref="CCDS:CCDS61027.1"
                     /db_xref="GeneID:10536"
                     /db_xref="HGNC:HGNC:19318"
                     /db_xref="MIM:610342"
ORIGIN      
        1 mlrllrplll llllpppgsp eppgltqlsp gappqapdll yadglrayaa gawapavall
       61 realrsqaal grvrldcgas caadpgaalp avllgapepd sgpgptqgsw erqllraalr
      121 radcltqcaa rrlgpggaar lrvgsalrda frrrepynyl qrayyqlkkl dlaaaaahtf
      181 fvanpmhlqm redmakyrrm sgvrpqsfrd letpphwaay dtglellgrq eaglalprle
      241 ealqgslaqm escradcegp eeqqgaeeee dgaasqggly eaiaghwiqv lqcrqrcvge
      301 tatrpgrsfp vpdflpnqlr rlheahaqvg nlsqaienvl svllfypede aakralnqyq
      361 aqlgeprpgl gprediqrfi lrslgekrql yyamehlgts fkdpdpwtpa alipealrek
      421 lredqekrpw dhepvkpkpl tywkdvllle gvtltqdsrq lngseravld glltpaecgv
      481 llqlakdaag agarsgyrgr rsphtpherf egltvlkaaq laragtvgsq gaklllevse
      541 rvrtltqayf sperplhlsf thlvcrsaie geqeqrmdls hpvhadncvl dpdtgecwre
      601 ppaytyrdys gllylnddfq ggdlfftepn altvtarvrp rcgrlvafss gvenphgvwa
      661 vtrgrrcala lwhtwapehr eqewieakel lqesqeeeee eeeempskdp speppsrrhq
      721 rvqdktgrap rvreel
//
LOCUS       NP_001348529             399 aa            linear   ROD 27-APR-2025
DEFINITION  aarF domain-containing protein kinase 1 isoform d [Mus musculus].
ACCESSION   NP_001348529
VERSION     NP_001348529.1
DBSOURCE    REFSEQ: accession NM_001361600.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Rizzo,P., Tinello,C., Pearlstein,R.A. and Taniuchi,H.
  TITLE     Antibody immunodiversity: a study on the marked specificity
            difference between two anti-yeast iso-1 cytochrome c monoclonal
            antibodies whose epitopes are closely related
  JOURNAL   J Protein Chem 18 (5), 523-532 (1999)
   PUBMED   10524770
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CT485612.7, BB850741.1 and CT030260.9.
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (d) is
            shorter at the N-terminus compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189670.85931.1,
                                           SRR7345562.2850477.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 42.55 cM"
     Protein         1..399
                     /product="aarF domain-containing protein kinase 1 isoform
                     d"
                     /note="aarF domain-containing protein kinase 1"
                     /calculated_mol_wt=45631
     Region          1..243
                     /region_name="ADCK1-like"
                     /note="aarF domain containing kinase 1 and similar
                     proteins; cd13969"
                     /db_xref="CDD:270871"
     Site            order(41..45,47,57,59,118,137..140,182,186..187,189,
                     204..205)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:270871"
     CDS             1..399
                     /gene="Adck1"
                     /gene_synonym="2610005A10Rik"
                     /coded_by="NM_001361600.1:468..1667"
                     /note="isoform d is encoded by transcript variant 6"
                     /db_xref="GeneID:72113"
                     /db_xref="MGI:MGI:1919363"
ORIGIN      
        1 mqevrqvire dlgkeihdlf lsfddtplga aslaqvhkav lhdgrtvavk vqhpkvqaqs
       61 skdillmevl vlavkqlfpd fefmwlvdea kknlpleldf lnegrnaekv ahmlrhfdfl
      121 kvpqihwels tkrvllmefv eggqvndray meknqidvne ischlgkmys emifvngfvh
      181 cdphpgnvlv rkrpdtgkae ivlldhglyq vlteefrldy chlwqsliwt dmdglkqysq
      241 rlgaadlypl facmltarsw dsvkqgigqa pvsatedsei rnnaacylpe isqllnhvpr
      301 qmllilktnd llrsiettlg trssassfln msrccirala ehkkrdagsf frrtqisfse
      361 afslwqinlh elllrvralr lacwvsallg wltraphrm
//
LOCUS       NP_008868                 95 aa            linear   PRI 27-APR-2025
DEFINITION  small ubiquitin-related modifier 2 isoform a precursor [Homo
            sapiens].
ACCESSION   NP_008868
VERSION     NP_008868.3
DBSOURCE    REFSEQ: accession NM_006937.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Kaur,A., Singh,H., Kumar,D., Gahlay,G.K. and Mithu,V.S.
  TITLE     Characterizing the Conformational Dynamics of Human SUMO2: Insights
            into its Interaction with Metal Ions and SIMs
  JOURNAL   Chembiochem 25 (11), e202400045 (2024)
   PUBMED   38593270
  REMARK    GeneRIF: Characterizing the Conformational Dynamics of Human SUMO2:
            Insights into its Interaction with Metal Ions and SIMs.
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Feng,D., He,J., Yuan,M., Chen,Q., Zeng,X., Zhou,Q., Wu,J. and
            Han,B.
  TITLE     SUMO2/3 promotes the progression and oxaliplatin resistance of
            colorectal cancer through facilitating the SUMOylation at Ku80-K307
  JOURNAL   Biofactors 49 (6), 1158-1173 (2023)
   PUBMED   37338025
  REMARK    GeneRIF: SUMO2/3 promotes the progression and oxaliplatin
            resistance of colorectal cancer through facilitating the
            SUMOylation at Ku80-K307.
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Hu,Y., Chen,C., Tong,X., Chen,S., Hu,X., Pan,B., Sun,X., Chen,Z.,
            Shi,X., Hu,Y., Shen,X., Xue,X. and Lu,M.
  TITLE     NSUN2 modified by SUMO-2/3 promotes gastric cancer progression and
            regulates mRNA m5C methylation
  JOURNAL   Cell Death Dis 12 (9), 842 (2021)
   PUBMED   34504059
  REMARK    GeneRIF: NSUN2 modified by SUMO-2/3 promotes gastric cancer
            progression and regulates mRNA m5C methylation.
            Erratum:[Cell Death Dis. 2024 Jul 11;15(7):495. doi:
            10.1038/s41419-024-06859-4. PMID: 38991998]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Bouchard,D., Wang,W., Yang,W.C., He,S., Garcia,A. and Matunis,M.J.
  TITLE     SUMO paralogue-specific functions revealed through systematic
            analysis of human knockout cell lines and gene expression data
  JOURNAL   Mol Biol Cell 32 (19), 1849-1866 (2021)
   PUBMED   34232706
  REMARK    GeneRIF: SUMO paralogue-specific functions revealed through
            systematic analysis of human knockout cell lines and gene
            expression data.
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Mo,Y., Wang,Y., Zhang,S., Xiong,F., Yan,Q., Jiang,X., Deng,X.,
            Wang,Y., Fan,C., Tang,L., Zhang,S., Gong,Z., Wang,F., Liao,Q.,
            Guo,C., Li,Y., Li,X., Li,G., Zeng,Z. and Xiong,W.
  TITLE     Circular RNA circRNF13 inhibits proliferation and metastasis of
            nasopharyngeal carcinoma via SUMO2
  JOURNAL   Mol Cancer 20 (1), 112 (2021)
   PUBMED   34465340
  REMARK    GeneRIF: Circular RNA circRNF13 inhibits proliferation and
            metastasis of nasopharyngeal carcinoma via SUMO2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 95)
  AUTHORS   Saitoh,H. and Hinchey,J.
  TITLE     Functional heterogeneity of small ubiquitin-related protein
            modifiers SUMO-1 versus SUMO-2/3
  JOURNAL   J Biol Chem 275 (9), 6252-6258 (2000)
   PUBMED   10692421
REFERENCE   7  (residues 1 to 95)
  AUTHORS   Kamitani,T., Kito,K., Nguyen,H.P., Fukuda-Kamitani,T. and Yeh,E.T.
  TITLE     Characterization of a second member of the sentrin family of
            ubiquitin-like proteins
  JOURNAL   J Biol Chem 273 (18), 11349-11353 (1998)
   PUBMED   9556629
REFERENCE   8  (residues 1 to 95)
  AUTHORS   Kamitani,T., Nguyen,H.P., Kito,K., Fukuda-Kamitani,T. and Yeh,E.T.
  TITLE     Covalent modification of PML by the sentrin family of
            ubiquitin-like proteins
  JOURNAL   J Biol Chem 273 (6), 3117-3120 (1998)
   PUBMED   9452416
REFERENCE   9  (residues 1 to 95)
  AUTHORS   Lapenta,V., Chiurazzi,P., van der Spek,P., Pizzuti,A., Hanaoka,F.
            and Brahe,C.
  TITLE     SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to
            chromosome 21qter and defines a novel gene family
  JOURNAL   Genomics 40 (2), 362-366 (1997)
   PUBMED   9119407
REFERENCE   10 (residues 1 to 95)
  AUTHORS   Mannen,H., Tseng,H.M., Cho,C.L. and Li,S.S.
  TITLE     Cloning and expression of human homolog HSMT3 to yeast SMT3
            suppressor of MIF2 mutations in a centromere protein gene
  JOURNAL   Biochem Biophys Res Commun 222 (1), 178-180 (1996)
   PUBMED   8630065
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC008450.1, AK024823.1 and
            AC022211.5.
            
            On Oct 28, 2004 this sequence version replaced NP_008868.2.
            
            Summary: This gene encodes a protein that is a member of the SUMO
            (small ubiquitin-like modifier) protein family. It functions in a
            manner similar to ubiquitin in that it is bound to target proteins
            as part of a post-translational modification system. However,
            unlike ubiquitin which targets proteins for degradation, this
            protein is involved in a variety of cellular processes, such as
            nuclear transport, transcriptional regulation, apoptosis, and
            protein stability. It is not active until the last two amino acids
            of the carboxy-terminus have been cleaved off. Numerous pseudogenes
            have been reported for this gene. Alternate transcriptional splice
            variants, encoding different isoforms, have been characterized.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.564202.1,
                                           SRR1660803.197095.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000420826.7/ ENSP00000405965.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..95
                     /product="small ubiquitin-related modifier 2 isoform a
                     precursor"
                     /note="sentrin 2; SMT3 suppressor of mif two 3 homolog 2;
                     SMT3 homolog 2; ubiquitin-like protein SMT3B;
                     ubiquitin-like protein SMT3A"
                     /calculated_mol_wt=10740
     mat_peptide     1..93
                     /product="small ubiquitin-related modifier 2 isoform a"
                     /calculated_mol_wt=10609
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P61956.3)"
     Region          17..88
                     /region_name="Ubl_SUMO2_3_4"
                     /note="ubiquitin-like (Ubl) domain found in small
                     ubiquitin-related modifier SUMO-2, SUMO-3, SUMO-4, and
                     similar proteins; cd16115"
                     /db_xref="CDD:340532"
     Site            order(17,19,28..39,41..42,46..47,49..51,56,68..70,72)
                     /site_type="other"
                     /note="SUMO2 dimer-RNF4 SIM2-3 interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:340532"
     Site            order(17,26..35,42,49..51)
                     /site_type="other"
                     /note="SUMO2-TDG interaction site [polypeptide binding]"
                     /db_xref="CDD:340532"
     Site            order(17,30..35,37..39,42..43,46..47,50)
                     /site_type="other"
                     /note="SUMO3-MCAF1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340532"
     Site            order(19,23..35,38,42..43,46,50..51,53..54,56..58,61,63,
                     65,87..88)
                     /site_type="other"
                     /note="SUMO2-Rangap1-UBC9-ZNF451 complex [polypeptide
                     binding]"
                     /db_xref="CDD:340532"
     Site            order(25..33,35,42,50,59,88)
                     /site_type="other"
                     /note="SUMO2-Rangap1-UBC9-RanBP2 complex [polypeptide
                     binding]"
                     /db_xref="CDD:340532"
     Site            order(25,56,59,61,63..66,68,71,82,85,87..88)
                     /site_type="other"
                     /note="SUMO2-SENP1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340532"
     Site            order(56,59,61..64,66,68,71,76,82,85,87..88)
                     /site_type="other"
                     /note="SUMO2-SENP2 [polypeptide binding]"
                     /db_xref="CDD:340532"
     Site            order(56,59,61,63..64,66,68,71,82,85,87..88)
                     /site_type="other"
                     /note="SUMO2-SENP2-Rangap1 complex [polypeptide binding]"
                     /db_xref="CDD:340532"
     CDS             1..95
                     /gene="SUMO2"
                     /gene_synonym="HSMT3; Smt3A; SMT3B; SMT3H2; SUMO3"
                     /coded_by="NM_006937.4:126..413"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS45774.1"
                     /db_xref="GeneID:6613"
                     /db_xref="HGNC:HGNC:11125"
                     /db_xref="MIM:603042"
ORIGIN      
        1 madekpkegv ktenndhinl kvagqdgsvv qfkikrhtpl sklmkaycer qglsmrqirf
       61 rfdgqpinet dtpaqlemed edtidvfqqq tggvy
//
LOCUS       NP_001350955             530 aa            linear   PRI 27-APR-2025
DEFINITION  M-phase inducer phosphatase 3 isoform f [Homo sapiens].
ACCESSION   NP_001350955
VERSION     NP_001350955.1
DBSOURCE    REFSEQ: accession NM_001364026.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Li,Y.F., Zheng,F.Y., Miao,X.Y., Liu,H.L., Zhang,Y.Y., Chao,N.X. and
            Mo,F.R.
  TITLE     Cell division cyclin 25C knockdown inhibits hepatocellular
            carcinoma development by inducing endoplasmic reticulum stress
  JOURNAL   World J Gastroenterol 30 (19), 2564-2574 (2024)
   PUBMED   38817663
  REMARK    GeneRIF: Cell division cyclin 25C knockdown inhibits hepatocellular
            carcinoma development by inducing endoplasmic reticulum stress.
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Zhai,M., Miao,J., Zhang,R., Liu,R., Li,F., Shen,Y., Wang,T., Xu,X.,
            Gao,G., Hu,J., He,A. and Bai,J.
  TITLE     KIF22 promotes multiple myeloma progression by regulating the
            CDC25C/CDK1/cyclinB1 pathway
  JOURNAL   J Cancer Res Clin Oncol 150 (5), 239 (2024)
   PUBMED   38713252
  REMARK    GeneRIF: KIF22 promotes multiple myeloma progression by regulating
            the CDC25C/CDK1/cyclinB1 pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Xu,N., Ren,Y., Bao,Y., Shen,X., Kang,J., Wang,N., Wang,Z., Han,X.,
            Li,Z., Zuo,J., Wei,G.H., Wang,Z., Zong,W.X., Liu,W., Xie,G. and
            Wang,Y.
  TITLE     PUF60 promotes cell cycle and lung cancer progression by regulating
            alternative splicing of CDC25C
  JOURNAL   Cell Rep 42 (9), 113041 (2023)
   PUBMED   37682709
  REMARK    GeneRIF: PUF60 promotes cell cycle and lung cancer progression by
            regulating alternative splicing of CDC25C.
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Bureik,M., Rief,N., Drescher,R., Jungbluth,A., Montenarh,M. and
            Wagner,P.
  TITLE     An additional transcript of the cdc25C gene from A431 cells encodes
            a functional protein
  JOURNAL   Int J Oncol 17 (6), 1251-1258 (2000)
   PUBMED   11078813
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Wegener,S., Hampe,W., Herrmann,D. and Schaller,H.C.
  TITLE     Alternative splicing in the regulatory region of the human
            phosphatases CDC25A and CDC25C
  JOURNAL   Eur J Cell Biol 79 (11), 810-815 (2000)
   PUBMED   11139144
REFERENCE   7  (residues 1 to 530)
  AUTHORS   Sartor,H., Ehlert,F., Grzeschik,K.H., Muller,R. and Adolph,S.
  TITLE     Assignment of two human cell cycle genes, CDC25C and CCNB1, to 5q31
            and 5q12, respectively
  JOURNAL   Genomics 13 (3), 911-912 (1992)
   PUBMED   1386342
REFERENCE   8  (residues 1 to 530)
  AUTHORS   Galaktionov,K. and Beach,D.
  TITLE     Specific activation of cdc25 tyrosine phosphatases by B-type
            cyclins: evidence for multiple roles of mitotic cyclins
  JOURNAL   Cell 67 (6), 1181-1194 (1991)
   PUBMED   1836978
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Strausfeld,U., Labbe,J.C., Fesquet,D., Cavadore,J.C., Picard,A.,
            Sadhu,K., Russell,P. and Doree,M.
  TITLE     Dephosphorylation and activation of a p34cdc2/cyclin B complex in
            vitro by human CDC25 protein
  JOURNAL   Nature 351 (6323), 242-245 (1991)
   PUBMED   1828290
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Gould,K.L., Moreno,S., Tonks,N.K. and Nurse,P.
  TITLE     Complementation of the mitotic activator, p80cdc25, by a human
            protein-tyrosine phosphatase
  JOURNAL   Science 250 (4987), 1573-1576 (1990)
   PUBMED   1703321
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104116.3.
            
            Summary: This gene encodes a conserved protein that plays a key
            role in the regulation of cell division. The encoded protein
            directs dephosphorylation of cyclin B-bound CDC2 and triggers entry
            into mitosis. It also suppresses p53-induced growth arrest.
            Multiple alternatively spliced transcript variants of this gene
            have been described. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.227680.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.2"
     Protein         1..530
                     /product="M-phase inducer phosphatase 3 isoform f"
                     /EC_number="3.1.3.48"
                     /note="dual specificity phosphatase CDC25C; mitosis
                     inducer CDC25; phosphotyrosine phosphatase; protein
                     phosphatase 1, regulatory subunit 60; CDC25 homolog C;
                     M-phase inducer phosphatase 3"
                     /calculated_mol_wt=59473
     Region          <222..504
                     /region_name="MIH1"
                     /note="Mitotic inducer, protein phosphatase [Cell division
                     and chromosome partitioning]; COG5105"
                     /db_xref="CDD:227436"
     Region          367..478
                     /region_name="Cdc25"
                     /note="Cdc25 phosphatases are members of the Rhodanese
                     Homology Domain superfamily. They activate the cell
                     division kinases throughout the cell cycle progression.
                     Cdc25 phosphatases dephosphorylate phosphotyrosine and
                     phosphothreonine residues, in order to...; cd01530"
                     /db_xref="CDD:238788"
     Site            434..440
                     /site_type="active"
                     /note="oxyanion binding site [active]"
                     /db_xref="CDD:238788"
     Site            434
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238788"
     CDS             1..530
                     /gene="CDC25C"
                     /gene_synonym="CDC25; PPP1R60"
                     /coded_by="NM_001364026.1:201..1793"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:995"
                     /db_xref="HGNC:HGNC:1727"
                     /db_xref="MIM:157680"
ORIGIN      
        1 megaapcrvs lkvslgqrcw erawrfdlgm gvvssltshp lqniaesgrp qleahletrg
       61 gghvgrrfcf spgensktms telfsstree gssgsgpsfr snqrkmlnll lerdtsftvc
      121 pdvprtpvgk flgdsanlsi lsggtpkrcl dlsnlssgei tatqlttsad ldetghldss
      181 glqevhlagm nhdqhlmkcs paqllcstpn gldrghrkrd amcsssanke ndngnlvdse
      241 mkylgspitt vpkldknpnl gedqaeeisd elmefslkdq eakvsrsgly rspsmpenln
      301 rprlkqvekf kdntipdkvk kkyfsgqgkl rkglclkktv slcdititqm leedsnqghl
      361 igdfskvaal lsgkfqglie kfyvidcryp yeylgghiqg alnlysqeel fnfflkkpiv
      421 pldtqkriii vfhcefsser gprmcrclre edrslnqypa lyypelyilk ggyrdffpey
      481 melcepqsyc pmhhqdhkte llrcrsqskv qegerqlreq iallvkdmsp
//
LOCUS       NP_001001340             307 aa            linear   VRT 27-APR-2025
DEFINITION  transcriptional enhancer factor TEF-3 isoform 4 [Gallus gallus].
ACCESSION   NP_001001340
VERSION     NP_001001340.1
DBSOURCE    REFSEQ: accession NM_001001340.2
KEYWORDS    RefSeq.
SOURCE      Gallus gallus (chicken)
  ORGANISM  Gallus gallus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
            Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
            Phasianidae; Phasianinae; Gallus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Tang,H., Finn,R.D. and Thomas,P.D.
  TITLE     TreeGrafter: phylogenetic tree-based annotation of proteins with
            Gene Ontology terms and other annotations
  JOURNAL   Bioinformatics 35 (3), 518-520 (2019)
   PUBMED   30032202
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Burge,S., Kelly,E., Lonsdale,D., Mutowo-Muellenet,P., McAnulla,C.,
            Mitchell,A., Sangrador-Vegas,A., Yong,S.Y., Mulder,N. and Hunter,S.
  TITLE     Manual GO annotation of predictive protein signatures: the InterPro
            approach to GO curation
  JOURNAL   Database (Oxford) 2012, bar068 (2012)
   PUBMED   22301074
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Boardman,P.E., Sanz-Ezquerro,J., Overton,I.M., Burt,D.W., Bosch,E.,
            Fong,W.T., Tickle,C., Brown,W.R., Wilson,S.A. and Hubbard,S.J.
  TITLE     A comprehensive collection of chicken cDNAs
  JOURNAL   Curr Biol 12 (22), 1965-1969 (2002)
   PUBMED   12445392
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Farrance,I.K. and Ordahl,C.P.
  TITLE     The role of transcription enhancer factor-1 (TEF-1) related
            proteins in the formation of M-CAT binding complexes in muscle and
            non-muscle tissues
  JOURNAL   J Biol Chem 271 (14), 8266-8274 (1996)
   PUBMED   8626521
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Stewart,A.F., Larkin,S.B., Farrance,I.K., Mar,J.H., Hall,D.E. and
            Ordahl,C.P.
  TITLE     Muscle-enriched TEF-1 isoforms bind M-CAT elements from
            muscle-specific promoters and differentially activate transcription
  JOURNAL   J Biol Chem 269 (5), 3147-3150 (1994)
   PUBMED   8106348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX932327.1, BU320294.1 and
            U06851.1.
            
            Summary: This gene encodes a transcription factor which is a member
            of the transcriptional enhancer factor (TEF) family. Members of
            this family are characterized by a TEA/ATTS DNA-binding domain.
            This factor, which is highly expressed in muscle, binds to a
            promoter element called M-CAT, a motif found in promoters of muscle
            specific genes. Alternatively spliced transcripts encoding distinct
            isoforms, which are encoded through the use of a non-AUG (UUG)
            translation initiation codon, have been described. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5), also referred to as TEF-1D,
            lacks a segment in the 5' coding region, compared to variant 1.
            Translation of this transcript does not begin at a non-AUG
            translation initiation codon, compared to variant 1. The resulting
            protein (isoform 4) is shorter and has a distinct N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcripts of
            different breeds because no single transcript from the same breed
            was available for the full length of the gene. The extent of this
            transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA103992290,
                              SAMEA103992323 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Gallus gallus"
                     /db_xref="taxon:9031"
                     /chromosome="1"
                     /map="1"
                     /breed="Leghorn"
     Protein         1..307
                     /product="transcriptional enhancer factor TEF-3 isoform 4"
                     /note="M-CAT binding factor; transcriptional enhancer
                     factor TEF-3; TEA domain family member 4"
                     /calculated_mol_wt=34598
     Region          95..304
                     /region_name="YBD"
                     /note="YAP binding domain; pfam17725"
                     /db_xref="CDD:435993"
     CDS             1..307
                     /gene="TEAD4"
                     /gene_synonym="RTEF-1; TEAD-4; TEF-1; TEF-3; TEF3"
                     /coded_by="NM_001001340.2:345..1268"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CGNC:49367"
                     /db_xref="GeneID:395542"
ORIGIN      
        1 mqsiatmssa qiisatafhs kmalpglprs aypavsgfwq galpgqagss qdvkpftqqp
       61 yalqpslplp gfdsptglpp ssstpawqgr rvassklwml efsafleqqq dqdtynkhlf
      121 vhigqsnpsy sdpyleavdi rqiydkfpek kgglkelfer gpanafflvk fwadlntnie
      181 desrsfygvs sqyespenmv itcstkvcsf gkqvvekvet eyahyenghy ayrihrsplc
      241 eyminfihkl khlpekymmn svlenftilq vvtnrdtqet llciayvfev sasdhgaqhh
      301 iyrlvkd
//
LOCUS       NP_001353453            1249 aa            linear   PRI 27-APR-2025
DEFINITION  plasma membrane calcium-transporting ATPase 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001353453 XP_011536709
VERSION     NP_001353453.1
DBSOURCE    REFSEQ: accession NM_001366524.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1249)
  AUTHORS   Kobayashi,Y., Yatsu,K., Haruna,A., Kawano,R., Ozawa,M., Haze,T.,
            Komiya,S., Suzuki,S., Ohki,Y., Fujiwara,A., Saka,S., Hirawa,N.,
            Toya,Y. and Tamura,K.
  TITLE     ATP2B1 gene polymorphisms associated with resistant hypertension in
            the Japanese population
  JOURNAL   J Clin Hypertens (Greenwich) 26 (4), 355-362 (2024)
   PUBMED   38430457
  REMARK    GeneRIF: ATP2B1 gene polymorphisms associated with resistant
            hypertension in the Japanese population.
REFERENCE   2  (residues 1 to 1249)
  AUTHORS   Gao,Y., Liu,Y., Jiang,Y., Qin,M., Guan,Z., Gao,Y. and Yang,Y.
  TITLE     Association between polymorphism and haplotype of ATP2B1 gene and
            skeletal fluorosis in Han population
  JOURNAL   Int J Environ Health Res 34 (3), 1410-1420 (2024)
   PUBMED   37211801
  REMARK    GeneRIF: Association between polymorphism and haplotype of ATP2B1
            gene and skeletal fluorosis in Han population.
REFERENCE   3  (residues 1 to 1249)
  AUTHORS   Berrocal,M. and Mata,A.M.
  TITLE     The Plasma Membrane Ca2+-ATPase, a Molecular Target for Tau-induced
            Cytosolic Calcium Dysregulation
  JOURNAL   Neuroscience 518, 112-118 (2023)
   PUBMED   35469971
  REMARK    GeneRIF: The Plasma Membrane Ca[2+]-ATPase, a Molecular Target for
            Tau-induced Cytosolic Calcium Dysregulation.
            Review article
REFERENCE   4  (residues 1 to 1249)
  AUTHORS   Yang,X., Lu,L., Wu,C. and Zhang,F.
  TITLE     ATP2B1-AS1 exacerbates sepsis-induced cell apoptosis and
            inflammation by regulating miR-23a-3p/TLR4 axis
  JOURNAL   Allergol Immunopathol (Madr) 51 (2), 17-26 (2023)
   PUBMED   36916084
  REMARK    GeneRIF: ATP2B1-AS1 exacerbates sepsis-induced cell apoptosis and
            inflammation by regulating miR-23a-3p/TLR4 axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1249)
  AUTHORS   Rahimi,M.J., Urban,N., Wegler,M., Sticht,H., Schaefer,M., Popp,B.,
            Gaunitz,F., Morleo,M., Nigro,V., Maitz,S., Mancini,G.M.S.,
            Ruivenkamp,C., Suk,E.K., Bartolomaeus,T., Merkenschlager,A.,
            Koboldt,D., Bartholomew,D., Stegmann,A.P.A., Sinnema,M.,
            Duynisveld,I., Salvarinova,R., Race,S., de Vries,B.B.A.,
            Trimouille,A., Naudion,S., Marom,D., Hamiel,U., Henig,N.,
            Demurger,F., Rahner,N., Bartels,E., Hamm,J.A., Putnam,A.M.,
            Person,R., Abou Jamra,R. and Oppermann,H.
  TITLE     De novo variants in ATP2B1 lead to neurodevelopmental delay
  JOURNAL   Am J Hum Genet 109 (5), 944-952 (2022)
   PUBMED   35358416
  REMARK    GeneRIF: De novo variants in ATP2B1 lead to neurodevelopmental
            delay.
REFERENCE   6  (residues 1 to 1249)
  AUTHORS   Kessler,F., Falchetto,R., Heim,R., Meili,R., Vorherr,T.,
            Strehler,E.E. and Carafoli,E.
  TITLE     Study of calmodulin binding to the alternatively spliced C-terminal
            domain of the plasma membrane Ca2+ pump
  JOURNAL   Biochemistry 31 (47), 11785-11792 (1992)
   PUBMED   1332771
REFERENCE   7  (residues 1 to 1249)
  AUTHORS   Wang,K.K., Wright,L.C., Machan,C.L., Allen,B.G., Conigrave,A.D. and
            Roufogalis,B.D.
  TITLE     Protein kinase C phosphorylates the carboxyl terminus of the plasma
            membrane Ca(2+)-ATPase from human erythrocytes
  JOURNAL   J Biol Chem 266 (14), 9078-9085 (1991)
   PUBMED   1827443
REFERENCE   8  (residues 1 to 1249)
  AUTHORS   Olson,S., Wang,M.G., Carafoli,E., Strehler,E.E. and McBride,O.W.
  TITLE     Localization of two genes encoding plasma membrane
            Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and
            12q21-23
  JOURNAL   Genomics 9 (4), 629-641 (1991)
   PUBMED   1674727
REFERENCE   9  (residues 1 to 1249)
  AUTHORS   Strehler,E.E., Strehler-Page,M.A., Vogel,G. and Carafoli,E.
  TITLE     mRNAs for plasma membrane calcium pump isoforms differing in their
            regulatory domain are generated by alternative splicing that
            involves two internal donor sites in a single exon
  JOURNAL   Proc Natl Acad Sci U S A 86 (18), 6908-6912 (1989)
   PUBMED   2528729
REFERENCE   10 (residues 1 to 1249)
  AUTHORS   James,P.H., Pruschy,M., Vorherr,T.E., Penniston,J.T. and
            Carafoli,E.
  TITLE     Primary structure of the cAMP-dependent phosphorylation site of the
            plasma membrane calcium pump
  JOURNAL   Biochemistry 28 (10), 4253-4258 (1989)
   PUBMED   2548572
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009522.11, AC068641.18 and
            AC025034.22.
            
            On Oct 10, 2018 this sequence version replaced XP_011536709.1.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type primary ion transport ATPases characterized by the formation
            of an aspartyl phosphate intermediate during the reaction cycle.
            These enzymes remove bivalent calcium ions from eukaryotic cells
            against very large concentration gradients and play a critical role
            in intracellular calcium homeostasis. The mammalian plasma membrane
            calcium ATPase isoforms are encoded by at least four separate genes
            and the diversity of these enzymes is further increased by
            alternative splicing of transcripts. The expression of different
            isoforms and splice variants is regulated in a developmental,
            tissue- and cell type-specific manner, suggesting that these pumps
            are functionally adapted to the physiological needs of particular
            cells and tissues. This gene encodes the plasma membrane calcium
            ATPase isoform 1. Alternatively spliced transcript variants
            encoding different isoforms have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7), as well as variant 8, encodes
            isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.135633.1,
                                           SRR1660809.195419.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1249
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.33"
     Protein         1..1249
                     /product="plasma membrane calcium-transporting ATPase 1
                     isoform 2"
                     /EC_number="7.2.2.10"
                     /note="plasma membrane calcium pump; ATPase, Ca++
                     transporting, plasma membrane 1; plasma membrane
                     calcium-transporting ATPase 1"
                     /calculated_mol_wt=137674
     Region          15..1064
                     /region_name="ATPase-IIB_Ca"
                     /note="plasma-membrane calcium-translocating P-type
                     ATPase; TIGR01517"
                     /db_xref="CDD:273668"
     Region          1103..1178
                     /region_name="ATP_Ca_trans_C"
                     /note="Plasma membrane calcium transporter ATPase C
                     terminal; pfam12424"
                     /db_xref="CDD:463575"
     CDS             1..1249
                     /gene="ATP2B1"
                     /gene_synonym="MRD66; PMCA1; PMCA1kb"
                     /coded_by="NM_001366524.1:370..4119"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:490"
                     /db_xref="HGNC:HGNC:814"
                     /db_xref="MIM:108731"
ORIGIN      
        1 mgdmannsva ysgvknslke anhdgdfgit laelralmel rstdalrkiq esygdvygic
       61 tklktspneg lsgnpadler reavfgknfi ppkkpktflq lvwealqdvt liileiaaiv
      121 slglsfyqpp egdnalcgev svgeeegege tgwiegaail lsvvcvvlvt afndwskekq
      181 frglqsrieq eqkftvirgg qviqipvadi tvgdiaqvky gdllpadgil iqgndlkide
      241 ssltgesdhv kksldkdpll lsgthvmegs grmvvtavgv nsqtgiiftl lgaggeeeek
      301 kdekkkekkn kkqdgaienr nkakaqdgaa memqplksee ggdgdekdkk kanlpkkeks
      361 vlqgkltkla vqigkagllm saitviilvl yfvidtfwvq krpwlaectp iyiqyfvkff
      421 iigvtvlvva vpeglplavt islaysvkkm mkdnnlvrhl dacetmgnat aicsdktgtl
      481 tmnrmtvvqa yinekhykkv pepeaippni lsylvtgisv ncaytskilp pekegglprh
      541 vgnktecall gllldlkrdy qdvrneipee alykvytfns vrksmstvlk nsdgsyrifs
      601 kgaseiilkk cfkilsange akvfrprdrd divktviepm aseglrticl afrdfpagep
      661 epewdnendi vtgltciavv giedpvrpev pdaikkcqra gitvrmvtgd nintaraiat
      721 kcgilhpged flclegkdfn rrirnekgei eqeridkiwp klrvlarssp tdkhtlvkgi
      781 idstvsdqrq vvavtgdgtn dgpalkkadv gfamgiagtd vakeasdiil tddnftsivk
      841 avmwgrnvyd siskflqfql tvnvvaviva ftgacitqds plkavqmlwv nlimdtlasl
      901 alatepptes lllrkpygrn kplisrtmmk nilghafyql vvvftllfag ekffdidsgr
      961 naplhappse hytivfntfv lmqlfneina rkihgernvf egifnnaifc tivlgtfvvq
     1021 iiivqfggkp fscselsieq wlwsiflgmg tllwgqlist iptsrlkflk eaghgtqkee
     1081 ipeeelaedv eeidhaerel rrgqilwfrg lnriqtqmdv vnafqsgssi qgalrrqpsi
     1141 asqhhdirvv nafrsslyeg lekpesrssi hnfmthpefr iedsephipl iddtdaedda
     1201 ptkrnssppp spnknnnavd sgihltiemn ksatssspgs plhsletsl
//
LOCUS       NP_057186                477 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM17 isoform 1 [Homo sapiens].
ACCESSION   NP_057186
VERSION     NP_057186.1
DBSOURCE    REFSEQ: accession NM_016102.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Zhong,T., Zhang,J., Liu,X. and Li,H.
  TITLE     TRIM17-mediated ubiquitination and degradation of RBM38 promotes
            cisplatin resistance in non-small cell lung cancer
  JOURNAL   Cell Oncol (Dordr) 46 (5), 1493-1507 (2023)
   PUBMED   37219768
  REMARK    GeneRIF: TRIM17-mediated ubiquitination and degradation of RBM38
            promotes cisplatin resistance in non-small cell lung cancer.
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Liu,Z., Zhao,W. and Yang,R.
  TITLE     MiR-1246 is responsible for lung cancer cells-derived
            exosomes-mediated promoting effects on lung cancer stemness via
            targeting TRIM17
  JOURNAL   Environ Toxicol 37 (11), 2651-2659 (2022)
   PUBMED   35894553
  REMARK    GeneRIF: MiR-1246 is responsible for lung cancer cells-derived
            exosomes-mediated promoting effects on lung cancer stemness via
            targeting TRIM17.
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Hu,X., Xiang,D., Xie,Y., Tao,L., Zhang,Y., Jin,Y., Pinello,L.,
            Wan,Y., Yuan,G.C. and Li,Z.
  TITLE     LSD1 suppresses invasion, migration and metastasis of luminal
            breast cancer cells via activation of GATA3 and repression of
            TRIM37 expression
  JOURNAL   Oncogene 38 (44), 7017-7034 (2019)
   PUBMED   31409898
  REMARK    GeneRIF: data suggest LSD1 largely plays a tumor suppressor role in
            luminal breast cancer and the oncogenic program associated with
            LSD1-inhibition may be suppressed via TRIM37-inhibition
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 477)
  AUTHORS   Urano,T., Usui,T., Takeda,S., Ikeda,K., Okada,A., Ishida,Y.,
            Iwayanagi,T., Otomo,J., Ouchi,Y. and Inoue,S.
  TITLE     TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3
            ligase
  JOURNAL   Biochem Biophys Res Commun 383 (2), 263-268 (2009)
   PUBMED   19358823
  REMARK    GeneRIF: terf interacts with TRIM44;TRIM44 inhibited ubiquitination
            of terf, and thus stabilized the protein.
REFERENCE   7  (residues 1 to 477)
  AUTHORS   Aurino,S., Piluso,G., Saccone,V., Cacciottolo,M., D'Amico,F.,
            Dionisi,M., Totaro,A., Belsito,A., Di Vicino,U. and Nigro,V.
  TITLE     Candidate-gene testing for orphan limb-girdle muscular dystrophies
  JOURNAL   Acta Myol 27 (3), 90-97 (2008)
   PUBMED   19472918
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 477)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   9  (residues 1 to 477)
  AUTHORS   Ogawa,S., Saito,T., Matsuda,Y., Seki,N., Hayashi,A., Orimo,A.,
            Hosoi,T., Ouchi,Y., Muramatsu,M., Hori,T. and Inoue,S.
  TITLE     Chromosome mapping of RNF16 and rnf16, human, mouse and rat genes
            coding for testis RING finger protein (terf), a member of the RING
            finger family
  JOURNAL   Cytogenet Cell Genet 89 (1-2), 56-58 (2000)
   PUBMED   10894938
REFERENCE   10 (residues 1 to 477)
  AUTHORS   Ogawa,S., Goto,W., Orimo,A., Hosoi,T., Ouchi,Y., Muramatsu,M. and
            Inoue,S.
  TITLE     Molecular cloning of a novel RING finger-B box-coiled coil (RBCC)
            protein, terf, expressed in the testis
  JOURNAL   Biochem Biophys Res Commun 251 (2), 515-519 (1998)
   PUBMED   9792805
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA270450.1, DB031719.1,
            BC033788.1 and AW770403.1.
            
            Summary: The protein encoded by this gene is a member of the
            tripartite motif (TRIM) family. The TRIM motif includes three
            zinc-binding domains, a RING, a B-box type 1 and a B-box type 2,
            and a coiled-coil region. The protein localizes to cytoplasmic
            bodies. The protein is expressed almost exclusively in the testis,
            but its function is unknown. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033788.1, AF156271.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366698.7/ ENSP00000355659.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.13"
     Protein         1..477
                     /product="E3 ubiquitin-protein ligase TRIM17 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 16; RING finger protein terf;
                     testis RING finger protein; E3 ubiquitin-protein ligase
                     TRIM17; tripartite motif-containing protein 17; RING-type
                     E3 ubiquitin transferase TRIM17"
                     /calculated_mol_wt=54287
     Region          9..78
                     /region_name="RING-HC_TRIM17_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein TRIM17 and similar proteins;
                     cd16595"
                     /db_xref="CDD:438257"
     Region          98..140
                     /region_name="Bbox2_TRIM7-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins TRIM7, TRIM27 and similar
                     proteins; cd19762"
                     /db_xref="CDD:380820"
     Region          296..472
                     /region_name="SPRY_PRY_TRIM17"
                     /note="PRY/SPRY domain of tripartite motif-binding protein
                     17 (TRIM17), also known as testis RING finger protein
                     (terf); cd15812"
                     /db_xref="CDD:293984"
     CDS             1..477
                     /gene="TRIM17"
                     /gene_synonym="RBCC; RNF16; terf"
                     /coded_by="NM_016102.4:365..1798"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1571.1"
                     /db_xref="GeneID:51127"
                     /db_xref="HGNC:HGNC:13430"
                     /db_xref="MIM:606123"
ORIGIN      
        1 meavelarkl qeeatcsicl dyftdpvmtt cghnfcraci qlswekargk kgrrkrkgsf
       61 pcpecremsp qrnllpnrll tkvaemaqqh pglqkqdlcq ehheplklfc qkdqspicvv
      121 cresrehrlh rvlpaeeavq gyklkleedm eylreqitrt gnlqareeqs laewqgkvke
      181 rrerivlefe kmnlylveee qrllqalete eeetasrlre svacldrqgh slellllqle
      241 erstqgplqm lqdmkeplsr knnvsvqcpe vapptrprtv crvpgqievl rgfledvvpd
      301 atsaypylll yesrqrrylg sspegsgfcs kdrfvaypca vgqtafssgr hywevgmnit
      361 gdalwalgvc rdnvsrkdrv pkcpengfwv vqlskgtkyl stfsaltpvm lmeppshmgi
      421 fldfeagevs fysvsdgshl htysqatfpg plqpffclga pksgqmvist vtmwvkg
//
LOCUS       NP_001161713             874 aa            linear   PRI 27-APR-2025
DEFINITION  GRB2-associated and regulator of MAPK protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001161713
VERSION     NP_001161713.1
DBSOURCE    REFSEQ: accession NM_001168241.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 874)
  AUTHORS   Taniguchi,T., Tanaka,S., Ishii,A., Watanabe,M., Fujitani,N.,
            Sugeo,A., Gotoh,S., Ohta,T., Hiyoshi,M., Matsuzaki,H., Sakai,N. and
            Konishi,H.
  TITLE     A brain-specific Grb2-associated regulator of extracellular
            signal-regulated kinase (Erk)/mitogen-activated protein kinase
            (MAPK) (GAREM) subtype, GAREM2, contributes to neurite outgrowth of
            neuroblastoma cells by regulating Erk signaling
  JOURNAL   J Biol Chem 288 (41), 29934-29942 (2013)
   PUBMED   24003223
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011742.3, AB124552.1, CX759737.1 and AA736392.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript but encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB124552.1, ERR3218371.375479.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000401533.7/ ENSP00000384593.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..874
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..874
                     /product="GRB2-associated and regulator of MAPK protein 2
                     isoform 1"
                     /note="protein FAM59B; family with sequence similarity 59,
                     member B; GRB2-associated and regulator of MAPK1-like;
                     GRB2-associated and regulator of MAPK protein-like; GRB2
                     associated, regulator of MAPK1-like; GRB2 associated
                     regulator of MAPK1 2; GRB2-associated and regulator of
                     MAPK protein 2"
                     /calculated_mol_wt=92752
     Region          12..339
                     /region_name="CABIT"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75VX8.3)"
     Region          29..341
                     /region_name="CABIT"
                     /note="Cell-cycle sustaining, positive selection;
                     pfam12736"
                     /db_xref="CDD:463686"
     Region          188..207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75VX8.3)"
     Region          388..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75VX8.3)"
     Region          437..545
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75VX8.3)"
     Region          563..598
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75VX8.3)"
     Region          <568..813
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          625..742
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75VX8.3)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q75VX8.3)"
     Region          806..872
                     /region_name="SAM_GAREM"
                     /note="SAM domain of GAREM subfamily; cd09525"
                     /db_xref="CDD:188924"
     CDS             1..874
                     /gene="GAREM2"
                     /gene_synonym="FAM59B; GAREML"
                     /coded_by="NM_001168241.2:134..2758"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54336.1"
                     /db_xref="GeneID:150946"
                     /db_xref="HGNC:HGNC:27172"
                     /db_xref="MIM:617999"
ORIGIN      
        1 meklaaglag lrwsmgafpl dlivsrcrlp tlaclgpgey aegvserdil lihscrqwtt
       61 vtahtleegh yvigpkidip lqypgkfkll eqardvrepv ryfssveeva svfpdrifvm
      121 eaitfsvkvv sgefsedsev ynftlhagde ltlmgqaeil cakttkersr fttllrklgr
      181 agalagvggg gpasagaagg tggggarpvk gkmpclicmn hrtneslslp fqcqgrfstr
      241 splelqmqeg ehtvraiier vrlpvnvlvp srpprnpydl hpvreghcyk lvsiisktvv
      301 lglalrregp aplhfllltd tprfalpqgl lagdprverl vrdsasycre rfdpdeysta
      361 vreapaelae dcasprrarl clpaprapgl arapgplapa pagegdqeyv spdwaaapep
      421 aappaeipye elwahqgpeg lvrpppgldl isfgaagppr repeappppv ppkseavkee
      481 crllnappvp prggngsgrl sssppvpprf pklqpvhsps sslsyyssgl qdgagsrsgs
      541 gspspdtysl ycypctwgdc kvgesssrpa pgplpsttqp sqasraltep lsgraasllg
      601 adtpvktyhs cpplfkpshp qkrfapfgal npfsgpayps gpsaalssgp rttsgpvats
      661 gpayspgpas pgqaysaapp sscapsssss sewqepvlep fdpfelgqgs spepellrsq
      721 epravgtpgp gprlsplgps kafepeglvl hqvptplspa alqgpeagga lfltqgrleg
      781 ppasprdgat gfgvrdassw qppadlsals leevsrslrf iglsedvvsf fareridgsi
      841 fvqlsedila ddfhltklqv kkimqfikgw rpki
//
LOCUS       NP_001138461             855 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 814 [Homo sapiens].
ACCESSION   NP_001138461 XP_001725726 XP_001725760 XP_001726338
VERSION     NP_001138461.1
DBSOURCE    REFSEQ: accession NM_001144989.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK300483.1 and AC010326.7.
            
            On or before Feb 4, 2009 this sequence version replaced
            XP_001726338.1, XP_001725760.1, XP_001725726.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300483.1, SRR1163655.398248.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000435989.7/ ENSP00000410545.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..855
                     /product="zinc finger protein 814"
                     /calculated_mol_wt=97207
     Region          15..55
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          176..192
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          214..650
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          216..236
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          244..264
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          271..291
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          462..850
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          550..570
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          578..598
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(583,585,587,589..590,593..594,597,611,613,617..618,
                     621..622,625,639,641,643,645..646,649..650,653)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          606..626
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          634..654
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          662..682
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          690..710
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          718..738
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          746..766
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(751,753,755,757..758,761..762,765,779,781,785..786,
                     789..790,793,807,809,811,813..814,817..818,821)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          774..794
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          802..822
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          830..850
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..855
                     /gene="ZNF814"
                     /coded_by="NM_001144989.2:236..2803"
                     /db_xref="CCDS:CCDS46212.1"
                     /db_xref="GeneID:730051"
                     /db_xref="HGNC:HGNC:33258"
ORIGIN      
        1 maaaatlrls aqgtvtfedv avnftweewn llseaqrcly rdvtlenlal isslgcwcgv
       61 edeaapskqs iyiqretqvr tpmagvspkk ahpcemcgpi lgdilhvadh qgthhkqklh
      121 rceawgnkly dsgnfhqhqn ehigekpyrg sveealfakr cklhvsgess vfsesgkdfl
      181 prsgllqqea shtgeksnsk tecvspiqcg gahyscgesm khfstkhils qhqrlltree
      241 cyvccecgks fskyaslsnh qrvhtekkhe cgecgksfsk yvsfsnhqrv htekkhecge
      301 cgksfskyvs fsnhqrvhtg krpyecgecg ksfskyasfs nhqrvhtekk hyecgecgks
      361 fskyvsfsnh qrvhtgkrpy ecgecgksfs kyasfsnhqr vhtdkkhyec gecgksfsqk
      421 ssliqhqrfh tgekpygcee cgksfssegh lrshqrvhag erpfkcgecv ksfshkrslv
      481 hhqrvhsger pyqcgecgks fsqkgnlvlh qrvhtgarpy ecgecgksfs skghlrnhqq
      541 ihtgdrlyec gecgksfshk gtlilhqrvh prersygcge cgksfssigh lrshqrvhtg
      601 erpyecgecg ksfshkrslv hhqrmhtger pykcgdcgks fnekghlrnh qrvhtterpf
      661 kcgecgkcfs hkgnlilhqh ghtgerpyvc recgklfkkk shllvhqrih ngekpyacea
      721 cqkffrnkyq liahqrvhtg erpyecndcg ksfthsstfc vhkrihtgek pyecsecgks
      781 faesssftkh krvhtgekpy ecsecgksfa esssltkhkr vhtgekpykc ekcgklfnkk
      841 shllvhqssh wrkai
//
LOCUS       NP_077787                581 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 319 [Mus musculus].
ACCESSION   NP_077787
VERSION     NP_077787.3
DBSOURCE    REFSEQ: accession NM_024467.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Aizawa,H., Yuasa,S.,
            Nakajima,D., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: II. The complete nucleotide sequences of 400 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (1), 35-48 (2003)
   PUBMED   12693553
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Laub,F., Aldabe,R., Ou,J. and Ramirez,F.
  TITLE     Overexpression of a novel zinc-finger protein induces apoptosis in
            NIH3T3 fibroblasts
  JOURNAL   Genomics 70 (3), 375-380 (2000)
   PUBMED   11161788
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC165414.9.
            
            On Dec 20, 2003 this sequence version replaced NP_077787.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC059823.1, AK048624.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 47.12 cM"
     Protein         1..581
                     /product="zinc finger protein 319"
                     /calculated_mol_wt=65513
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERR8.1)"
     Region          77..97
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          105..125
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          133..153
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <190..348
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          203..223
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(208,210,212,214..215,218..219,222,236,238,242..243,
                     246..247,250,264,266,268,270..271,274..275,278)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          231..251
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          259..279
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2F9; propagated from
                     UniProtKB/Swiss-Prot (Q9ERR8.1)"
     Region          288..308
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          316..336
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          344..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <365..445
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          400..416
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <419..504
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          429..449
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          459..479
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(464,466,468,470..471,474..475,478,492,494,498..499,
                     502..503,506,520,522,524,526..527,530..531,534)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          487..507
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          499..524
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          515..535
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          543..563
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..581
                     /gene="Zfp319"
                     /gene_synonym="mKIAA1388; Znf319"
                     /coded_by="NM_024467.4:531..2276"
                     /db_xref="CCDS:CCDS22559.1"
                     /db_xref="GeneID:79233"
                     /db_xref="MGI:MGI:1890618"
ORIGIN      
        1 mseswqqppq tqpqqpqapq pqhhaetppa laehtlppgs aenplgcavy gillqpdpgl
       61 qppqhaplqa gepgpkcgvc ghdlahlssp hehqclaghd rsfqctqclk ifhqatdlle
      121 hqcvqaeqkp fvcgvckmgf slltslaqhh sshtgmvkcs icdktykpae aaepatttap
      181 slpsapppan iapveqpekp yscpvcqkpf khlselsrhe rihtgekpyk ctlcdksfsq
      241 sshlvhhkrt hsserpykca vcektfkhrs hlvrhmyahs gehhlfrcnv celhfkesse
      301 llqhpctpsg erpfrcgecq kafkrpsdlr qherthsaer pfkcdlcpmg fkqqyalmrh
      361 rrthkteepf kcglcekgfg qpshllyhqh vhtletlfkc pvcqkgfdqs aellrhkclp
      421 tsterpfkcp vcnkaykras alqkhqlshc aaaekplrct lcerrffsss efvqhrcdpa
      481 rekplkcpdc ekrfkyasdl qrhrrvhtge kpykcpscdk afkqrehlnk hqgvhareqq
      541 fkcvwcgerf ldvallqehs aqhsaaaaaa egayqvaacl p
//
LOCUS       NP_987095                938 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX42 [Homo sapiens].
ACCESSION   NP_987095
VERSION     NP_987095.1
DBSOURCE    REFSEQ: accession NM_203499.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Bonaventure,B. and Goujon,C.
  TITLE     [The DEAD box RNA helicase DDX42 is an intrinsic inhibitor of
            positive-strand RNA viruses]
  JOURNAL   Med Sci (Paris) 39 (4), 322-325 (2023)
   PUBMED   37094262
  REMARK    GeneRIF: [The DEAD box RNA helicase DDX42 is an intrinsic inhibitor
            of positive-strand RNA viruses].
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Yang,F., Bian,T., Zhan,X., Chen,Z., Xing,Z., Larsen,N.A., Zhang,X.
            and Shi,Y.
  TITLE     Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP
            assembly
  JOURNAL   Nat Commun 14 (1), 897 (2023)
   PUBMED   36797247
  REMARK    GeneRIF: Mechanisms of the RNA helicases DDX42 and DDX46 in human
            U2 snRNP assembly.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 938)
  AUTHORS   Bonaventure,B., Rebendenne,A., Chaves Valadao,A.L.,
            Arnaud-Arnould,M., Gracias,S., Garcia de Gracia,F., McKellar,J.,
            Labaronne,E., Tauziet,M., Vivet-Boudou,V., Bernard,E., Briant,L.,
            Gros,N., Djilli,W., Courgnaud,V., Parrinello,H., Rialle,S.,
            Blaise,M., Lacroix,L., Lavigne,M., Paillart,J.C., Ricci,E.P.,
            Schulz,R., Jouvenet,N., Moncorge,O. and Goujon,C.
  TITLE     The DEAD box RNA helicase DDX42 is an intrinsic inhibitor of
            positive-strand RNA viruses
  JOURNAL   EMBO Rep 23 (11), e54061 (2022)
   PUBMED   36161446
  REMARK    GeneRIF: The DEAD box RNA helicase DDX42 is an intrinsic inhibitor
            of positive-strand RNA viruses.
REFERENCE   5  (residues 1 to 938)
  AUTHORS   Zhao,B., Li,Z., Qian,R., Liu,G., Fan,M., Liang,Z., Hu,X. and Wan,Y.
  TITLE     Cancer-associated mutations in SF3B1 disrupt the interaction
            between SF3B1 and DDX42
  JOURNAL   J Biochem 172 (2), 117-126 (2022)
   PUBMED   35652295
  REMARK    GeneRIF: Cancer-associated mutations in SF3B1 disrupt the
            interaction between SF3B1 and DDX42.
REFERENCE   6  (residues 1 to 938)
  AUTHORS   Lin,C.W., Cheng,C.W., Yang,T.C., Li,S.W., Cheng,M.H., Wan,L.,
            Lin,Y.J., Lai,C.H., Lin,W.Y. and Kao,M.C.
  TITLE     Interferon antagonist function of Japanese encephalitis virus NS4A
            and its interaction with DEAD-box RNA helicase DDX42
  JOURNAL   Virus Res 137 (1), 49-55 (2008)
   PUBMED   18588927
  REMARK    GeneRIF: expression of N-terminal DDX42 is able to overcome
            Japanese encephalitis virus-induced antagonism of IFN responses and
            so may be important for Japanese encephalitis virus pathogenesis
REFERENCE   7  (residues 1 to 938)
  AUTHORS   Behzadnia,N., Golas,M.M., Hartmuth,K., Sander,B., Kastner,B.,
            Deckert,J., Dube,P., Will,C.L., Urlaub,H., Stark,H. and Luhrmann,R.
  TITLE     Composition and three-dimensional EM structure of double
            affinity-purified, human prespliceosomal A complexes
  JOURNAL   EMBO J 26 (6), 1737-1748 (2007)
   PUBMED   17332742
REFERENCE   8  (residues 1 to 938)
  AUTHORS   Uhlmann-Schiffler,H., Jalal,C. and Stahl,H.
  TITLE     Ddx42p--a human DEAD box protein with RNA chaperone activities
  JOURNAL   Nucleic Acids Res 34 (1), 10-22 (2006)
   PUBMED   16397294
  REMARK    GeneRIF: Ddx42p represents the first example of a human DEAD box
            protein possessing RNA helicase, protein displacement and RNA
            annealing activities.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 938)
  AUTHORS   Will,C.L., Urlaub,H., Achsel,T., Gentzel,M., Wilm,M. and
            Luhrmann,R.
  TITLE     Characterization of novel SF3b and 17S U2 snRNP proteins, including
            a human Prp5p homologue and an SF3b DEAD-box protein
  JOURNAL   EMBO J 21 (18), 4978-4988 (2002)
   PUBMED   12234937
  REMARK    GeneRIF: characterization of protein associated with the human 17S
            U2 snRNP and one of its stable subunits, SF3b; may facilitate the
            assembly of the 17S U2 snRNP
REFERENCE   10 (residues 1 to 938)
  AUTHORS   Suk,K., Kim,S., Kim,Y.H., Oh,S.H., Lee,M.K., Kim,K.W., Kim,H.D. and
            Seo,Y.S.
  TITLE     Identification of a novel human member of the DEAD box protein
            family
  JOURNAL   Biochim Biophys Acta 1501 (1), 63-69 (2000)
   PUBMED   10727850
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015651.18, DA440475.1,
            AB036090.1 and BC015505.1.
            
            Summary: This gene encodes a member of the Asp-Glu-Ala-Asp (DEAD)
            box protein family. Members of this protein family are putative RNA
            helicases, and are implicated in a number of cellular processes
            involving alteration of RNA secondary structure such as translation
            initiation, nuclear and mitochondrial splicing, and ribosome and
            spliceosome assembly. Members of this family are believed to be
            involved in embryogenesis, spermatogenesis, and cellular growth and
            division. Two transcript variants encoding the same protein have
            been identified for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an exon in the 5' UTR
            compared to variant 1. Both variants 1 and 2 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.104354.1,
                                           SRR1803612.106913.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389924.7/ ENSP00000374574.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..938
                     /product="ATP-dependent RNA helicase DDX42"
                     /EC_number="3.6.4.13"
                     /note="SF3b DEAD box protein; DEAD (Asp-Glu-Ala-Asp) box
                     helicase 42; splicing factor 3B-associated 125 kDa
                     protein; DEAD (Asp-Glu-Ala-Asp) box polypeptide 42;
                     splicing factor 3b, subunit 8"
                     /calculated_mol_wt=102844
     Region          1..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XP3.1)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q86XP3.1)"
     Site            12
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q86XP3.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86XP3.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86XP3.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86XP3.1)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q86XP3.1)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q86XP3.1)"
     Region          182..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XP3.1)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86XP3.1)"
     Region          253..281
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XP3.1)"
     Region          254..664
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          407..410
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XP3.1)"
     Region          <733..>891
                     /region_name="dermokine"
                     /note="cl42387"
                     /db_xref="CDD:455732"
     Region          737..938
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XP3.1)"
     Region          738..833
                     /region_name="Necessary for interaction with TP53BP2.
                     /evidence=ECO:0000269|PubMed:19377511"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XP3.1)"
     Site            754
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86XP3.1)"
     CDS             1..938
                     /gene="DDX42"
                     /gene_synonym="DDX42P; RHELP; RNAHP; SF3b125; SF3B8"
                     /coded_by="NM_203499.3:224..3040"
                     /db_xref="CCDS:CCDS32704.1"
                     /db_xref="GeneID:11325"
                     /db_xref="HGNC:HGNC:18676"
                     /db_xref="MIM:613369"
ORIGIN      
        1 mnwnkggpgt krgfgfggfa isagkkeepk lpqqshsafg atssssgfgk sappqlpsfy
       61 kigskranfd eenayfedee edssnvdlpy ipaensptrq qfhskpvdsd sdddpleafm
      121 aevedqaard mkrleekdke rknvkgirdd ieeeddqeay frymaenpta gvvqeeeedn
      181 leydsdgnpi aptkkiidpl ppidhseidy ppfeknfyne heeitnltpq qlidlrhkln
      241 lrvsgaappr pgssfahfgf deqlmhqirk seytqptpiq cqgvpvalsg rdmigiaktg
      301 sgktaafiwp mlihimdqke lepgdgpiav ivcptrelcq qihaeckrfg kaynlrsvav
      361 ygggsmweqa kalqegaeiv vctpgrlidh vkkkatnlqr vsylvfdead rmfdmgfeyq
      421 vrsiashvrp drqtllfsat frkkieklar dilidpirvv qgdigeaned vtqiveilhs
      481 gpskwnwltr rlveftssgs vllfvtkkan aeelannlkq eghnlgllhg dmdqsernkv
      541 isdfkkkdip vlvatdvaar gldipsiktv inydvardid ththrigrtg ragekgvayt
      601 lltpkdsnfa gdlvrnlega nqhvskelld lamqnawfrk srfkggkgkk lnigggglgy
      661 rerpglgsen mdrgnnnvms nyeaykpstg amgdrltamk aafqsqyksh fvaaslsnqk
      721 agssaagasg wtsagslnsv ptnsaqqghn spdspvtsaa kgipgfgntg nisgapvtyp
      781 sagaqgvnnt asgnnsregt ggsngkrery tenrgssrhs hgetgnrhsd sprhgdggrh
      841 gdgyrhpess srhtdghrhg enrhggsagr hgenrgandg rngesrkeaf nreskmepkm
      901 epkvdsskmd kvdsktdkta dgfavpeppk rkksrwds
//
LOCUS       NP_001161368             453 aa            linear   MAM 27-APR-2025
DEFINITION  DDB1- and CUL4-associated factor 12 [Bos taurus].
ACCESSION   NP_001161368 XP_869764
VERSION     NP_001161368.1
DBSOURCE    REFSEQ: accession NM_001167896.2
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            NKLS02000008.1.
            
            On Nov 18, 2009 this sequence version replaced XP_869764.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105241.1, SRR5571262.33831.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA6648753,
                                           SAMEA6648754 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="8"
                     /map="8"
                     /breed="Hereford"
     Protein         1..453
                     /product="DDB1- and CUL4-associated factor 12"
                     /note="WD repeat-containing protein 40A; WD repeat domain
                     40A"
                     /calculated_mol_wt=50506
     Region          1..38
                     /region_name="Required for nuclear location and
                     interaction with MOV10.
                     /evidence=ECO:0000250|UniProtKB:Q5T6F0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHH0.2)"
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHH0.2)"
     Region          <101..283
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          137..180
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          138..178
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHH0.2)"
     Region          182..220
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHH0.2)"
     Region          187..233
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          250..289
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHH0.2)"
     Region          255..292
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          300..336
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          338..375
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHH0.2)"
     CDS             1..453
                     /gene="DCAF12"
                     /gene_synonym="WDR40A"
                     /coded_by="NM_001167896.2:307..1668"
                     /db_xref="BGD:BT15988"
                     /db_xref="GeneID:525161"
                     /db_xref="VGNC:VGNC:27901"
ORIGIN      
        1 markavsrkr kapalpgags daqdpqfgwd hslhkrkrlp pvkrslvyyl knrevrlqne
       61 tsysrvlhgy aaqqlpsllk erefhlgtln kvfasqwlnh rqvvcgtkcn tlfvvdvqts
      121 qitkipilkd repgcvtqqg cgihaielnp srtllatggd npnslaiyrl ptldpvcvgd
      181 dghkdwifsi awisdtmavs gsrdgsmglw evtddvltks darhnvsrvp vyshithkal
      241 kdipkedtnp dnckvralaf nnknkelgav sldgyfhlwk tentlsklls tklpycrenv
      301 claygnewsv yavgsqahvs fldprqpsyn vksvcsrerg sgirsvsfye hiitvgtgqg
      361 sllfydiraq rfleeklsac ygskpklage nlklttgkgw lnhdetwrny fsdidffpna
      421 vythcydssg tklfvaggpl psglhgnyag lws
//
LOCUS       NP_853521                422 aa            linear   ROD 27-APR-2025
DEFINITION  G-protein coupled receptor 151 protein [Mus musculus].
ACCESSION   NP_853521
VERSION     NP_853521.1
DBSOURCE    REFSEQ: accession NM_181543.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Bielczyk-Maczynska,E., Zhao,M., Zushin,P.H., Schnurr,T.M.,
            Kim,H.J., Li,J., Nallagatla,P., Sangwung,P., Park,C.Y., Cornn,C.,
            Stahl,A., Svensson,K.J. and Knowles,J.W.
  TITLE     G protein-coupled receptor 151 regulates glucose metabolism and
            hepatic gluconeogenesis
  JOURNAL   Nat Commun 13 (1), 7408 (2022)
   PUBMED   36456565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Allain,F., Carter,M., Dumas,S., Darcq,E. and Kieffer,B.L.
  TITLE     The mu opioid receptor and the orphan receptor GPR151 contribute to
            social reward in the habenula
  JOURNAL   Sci Rep 12 (1), 20234 (2022)
   PUBMED   36424418
  REMARK    GeneRIF: The mu opioid receptor and the orphan receptor GPR151
            contribute to social reward in the habenula.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Gurtan,A., Dominy,J., Khalid,S., Vong,L., Caplan,S., Currie,T.,
            Richards,S., Lamarche,L., Denning,D., Shpektor,D., Gurinovich,A.,
            Rasheed,A., Hameed,S., Saeed,S., Saleem,I., Jalal,A., Abbas,S.,
            Sultana,R., Rasheed,S.Z., Memon,F.U., Shah,N., Ishaq,M.,
            Khera,A.V., Danesh,J., Frossard,P. and Saleheen,D.
  TITLE     Analyzing human knockouts to validate GPR151 as a therapeutic
            target for reduction of body mass index
  JOURNAL   PLoS Genet 18 (4), e1010093 (2022)
   PUBMED   35381001
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Jiang,B.C., Zhang,J., Wu,B., Jiang,M., Cao,H., Wu,H. and Gao,Y.J.
  TITLE     G protein-coupled receptor GPR151 is involved in trigeminal
            neuropathic pain through the induction of Gbetagamma/extracellular
            signal-regulated kinase-mediated neuroinflammation in the
            trigeminal ganglion
  JOURNAL   Pain 162 (5), 1434-1448 (2021)
   PUBMED   33239523
  REMARK    GeneRIF: G protein-coupled receptor GPR151 is involved in
            trigeminal neuropathic pain through the induction of
            Gbetagamma/extracellular signal-regulated kinase-mediated
            neuroinflammation in the trigeminal ganglion.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Antolin-Fontes,B., Li,K., Ables,J.L., Riad,M.H., Gorlich,A.,
            Williams,M., Wang,C., Lipford,S.M., Dao,M., Liu,J., Molina,H.,
            Heintz,N., Kenny,P.J. and Ibanez-Tallon,I.
  TITLE     The habenular G-protein-coupled receptor 151 regulates synaptic
            plasticity and nicotine intake
  JOURNAL   Proc Natl Acad Sci U S A 117 (10), 5502-5509 (2020)
   PUBMED   32098843
  REMARK    GeneRIF: These data identify GPR151 as a critical modulator of
            habenular function that controls nicotine addiction vulnerability
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Quina,L.A., Wang,S., Ng,L. and Turner,E.E.
  TITLE     Brn3a and Nurr1 mediate a gene regulatory pathway for habenula
            development
  JOURNAL   J Neurosci 29 (45), 14309-14322 (2009)
   PUBMED   19906978
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Lein,E.S., Hawrylycz,M.J., Ao,N., Ayres,M., Bensinger,A.,
            Bernard,A., Boe,A.F., Boguski,M.S., Brockway,K.S., Byrnes,E.J.,
            Chen,L., Chen,L., Chen,T.M., Chin,M.C., Chong,J., Crook,B.E.,
            Czaplinska,A., Dang,C.N., Datta,S., Dee,N.R., Desaki,A.L.,
            Desta,T., Diep,E., Dolbeare,T.A., Donelan,M.J., Dong,H.W.,
            Dougherty,J.G., Duncan,B.J., Ebbert,A.J., Eichele,G., Estin,L.K.,
            Faber,C., Facer,B.A., Fields,R., Fischer,S.R., Fliss,T.P.,
            Frensley,C., Gates,S.N., Glattfelder,K.J., Halverson,K.R.,
            Hart,M.R., Hohmann,J.G., Howell,M.P., Jeung,D.P., Johnson,R.A.,
            Karr,P.T., Kawal,R., Kidney,J.M., Knapik,R.H., Kuan,C.L.,
            Lake,J.H., Laramee,A.R., Larsen,K.D., Lau,C., Lemon,T.A.,
            Liang,A.J., Liu,Y., Luong,L.T., Michaels,J., Morgan,J.J.,
            Morgan,R.J., Mortrud,M.T., Mosqueda,N.F., Ng,L.L., Ng,R.,
            Orta,G.J., Overly,C.C., Pak,T.H., Parry,S.E., Pathak,S.D.,
            Pearson,O.C., Puchalski,R.B., Riley,Z.L., Rockett,H.R.,
            Rowland,S.A., Royall,J.J., Ruiz,M.J., Sarno,N.R., Schaffnit,K.,
            Shapovalova,N.V., Sivisay,T., Slaughterbeck,C.R., Smith,S.C.,
            Smith,K.A., Smith,B.I., Sodt,A.J., Stewart,N.N., Stumpf,K.R.,
            Sunkin,S.M., Sutram,M., Tam,A., Teemer,C.D., Thaller,C.,
            Thompson,C.L., Varnam,L.R., Visel,A., Whitlock,R.M.,
            Wohnoutka,P.E., Wolkey,C.K., Wong,V.Y., Wood,M., Yaylaoglu,M.B.,
            Young,R.C., Youngstrom,B.L., Yuan,X.F., Zhang,B., Zwingman,T.A. and
            Jones,A.R.
  TITLE     Genome-wide atlas of gene expression in the adult mouse brain
  JOURNAL   Nature 445 (7124), 168-176 (2007)
   PUBMED   17151600
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Ignatov,A., Hermans-Borgmeyer,I. and Schaller,H.C.
  TITLE     Cloning and characterization of a novel G-protein-coupled receptor
            with homology to galanin receptors
  JOURNAL   Neuropharmacology 46 (8), 1114-1120 (2004)
   PUBMED   15111018
  REMARK    GeneRIF: Galanin-receptor like (GalRL) expression is found in the
            dorsal thalamus; hybridization signals are detected in the
            striatum, the locus coeruleus, and several hindbrain nuclei.
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Berthold,M., Collin,M., Sejlitz,T., Meister,B. and Lind,P.
  TITLE     Cloning of a novel orphan G protein-coupled receptor (GPCR-2037):
            in situ hybridization reveals high mRNA expression in rat brain
            restricted to neurons of the habenular complex
  JOURNAL   Brain Res Mol Brain Res 120 (1), 22-29 (2003)
   PUBMED   14667573
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Vassilatis,D.K., Hohmann,J.G., Zeng,H., Li,F., Ranchalis,J.E.,
            Mortrud,M.T., Brown,A., Rodriguez,S.S., Weller,J.R., Wright,A.C.,
            Bergmann,J.E. and Gaitanaris,G.A.
  TITLE     The G protein-coupled receptor repertoires of human and mouse
  JOURNAL   Proc Natl Acad Sci U S A 100 (8), 4903-4908 (2003)
   PUBMED   12679517
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC121603.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AJ564167.1, BC120520.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 22.71 cM"
     Protein         1..422
                     /product="G-protein coupled receptor 151 protein"
                     /note="putative G protein-coupled receptor nGPCR-2037;
                     probable G-protein coupled receptor 151 protein;
                     GPCR-2037; G-protein coupled receptor PGR7"
                     /calculated_mol_wt=46695
     Site            14
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSN6.1)"
     Site            19
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSN6.1)"
     Region          42..321
                     /region_name="7tmA_GPR151"
                     /note="G protein-coupled receptor 151, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15002"
                     /db_xref="CDD:320133"
     Region          42..68
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320133"
     Site            46..66
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN6.1)"
     Region          77..102
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320133"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN6.1)"
     Site            order(99,102..103,115..120,122..123,126,170,172..176,203,
                     206..208,210..212,214..215,267,270..271,273..274,277,
                     288..289,291..293,296,299..300)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320133"
     Region          114..144
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320133"
     Site            124..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN6.1)"
     Region          157..178
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320133"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN6.1)"
     Region          203..232
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320133"
     Site            206..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN6.1)"
     Region          247..277
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320133"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN6.1)"
     Region          289..314
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320133"
     Site            291..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN6.1)"
     Region          339..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN6.1)"
     CDS             1..422
                     /gene="Gpr151"
                     /gene_synonym="C130082O03Rik; GalRL; nGPCR-2037; PGR7"
                     /coded_by="NM_181543.2:42..1310"
                     /db_xref="CCDS:CCDS29215.1"
                     /db_xref="GeneID:240239"
                     /db_xref="MGI:MGI:2441887"
ORIGIN      
        1 mgkamlragf adtnssnmne sfarlhfagg ylpsdskdwr tiipsllmav clvglvgnlc
       61 vigillhgvw krkpstihsl ilnlsladfs lllfsapvra aayskgvwdl gwfickssdw
      121 fthvcmaaks ltfvvvakac fayasdpakq esihsrtiws vlagiwvvas llplpewlfs
      181 ttrrhagvem clvdvpavae efmsmfgkly pllvfclpll lagvyfwray dqcktrctkt
      241 rnlrdqmrsk qltvmllsta iisallwlpe wiawlwvwhv kaggpmppqg fialsqvlmf
      301 ftstanplif lvmseefkag lkglwkwmit rkpavtsevq eapagnteal pgkapspetq
      361 tcildtdgrg spddskeksg kvvapilpdv eqfwherdav psaqdndpip wehegqeteg
      421 cn
//
LOCUS       NP_002211                461 aa            linear   PRI 27-APR-2025
DEFINITION  inositol-trisphosphate 3-kinase A [Homo sapiens].
ACCESSION   NP_002211
VERSION     NP_002211.1
DBSOURCE    REFSEQ: accession NM_002220.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Zhang,X., He,J. and Ren,D.
  TITLE     Commentary on: The actin bundling activity of ITPKA mainly accounts
            for its migration-promoting effect in lung cancer cells
  JOURNAL   Biosci Rep 43 (9) (2023)
   PUBMED   37664985
  REMARK    GeneRIF: Commentary on: The actin bundling activity of ITPKA mainly
            accounts for its migration-promoting effect in lung cancer cells.
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Kuster,L., Paraschiakos,T., Karakurt,K.E., Schumacher,U.,
            Diercks,B.P. and Windhorst,S.
  TITLE     The actin bundling activity of ITPKA mainly accounts for its
            migration-promoting effect in lung cancer cells
  JOURNAL   Biosci Rep 43 (2) (2023)
   PUBMED   36688944
  REMARK    GeneRIF: The actin bundling activity of ITPKA mainly accounts for
            its migration-promoting effect in lung cancer cells.
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Shaosheng,W., Shaochuang,W., Lichun,F., Na,X. and Xiaohong,Z.
  TITLE     ITPKA induces cell senescence, inhibits ovarian cancer
            tumorigenesis and can be downregulated by miR-203
  JOURNAL   Aging (Albany NY) 13 (8), 11822-11832 (2021)
   PUBMED   33879633
  REMARK    GeneRIF: ITPKA induces cell senescence, inhibits ovarian cancer
            tumorigenesis and can be downregulated by miR-203.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Zhang,J., Zhang,S., Li,X. and Pi,H.
  TITLE     Relationship of ITPKA expression with the prognosis of breast
            cancer
  JOURNAL   Mol Genet Genomic Med 9 (4), e1598 (2021)
   PUBMED   33624455
  REMARK    GeneRIF: Relationship of ITPKA expression with the prognosis of
            breast cancer.
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Guoren,Z., Zhaohui,F., Wei,Z., Mei,W., Yuan,W., Lin,S., Xiaoyue,X.,
            Xiaomei,Z. and Bo,S.
  TITLE     TFAP2A Induced ITPKA Serves as an Oncogene and Interacts with DBN1
            in Lung Adenocarcinoma
  JOURNAL   Int J Biol Sci 16 (3), 504-514 (2020)
   PUBMED   32015686
  REMARK    GeneRIF: TFAP2A Induced ITPKA Serves as an Oncogene and Interacts
            with DBN1 in Lung Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Erneux,C., Roeckel,N., Takazawa,K., Mailleux,P., Vassart,G. and
            Mattei,M.G.
  TITLE     Localization of the genes for human inositol 1,4,5-trisphosphate
            3-kinase A (ITPKA) and B (ITPKB) to chromosome regions 15q14-q21
            and 1q41-q43, respectively, by in situ hybridization
  JOURNAL   Genomics 14 (2), 546-547 (1992)
   PUBMED   1330886
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Takazawa,K. and Erneux,C.
  TITLE     Identification of residues essential for catalysis and binding of
            calmodulin in rat brain inositol 1,4,5-trisphosphate 3-kinase
  JOURNAL   Biochem J 280 (Pt 1) (Pt 1), 125-129 (1991)
   PUBMED   1660262
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Takazawa,K., Perret,J., Dumont,J.E. and Erneux,C.
  TITLE     Molecular cloning and expression of a new putative inositol
            1,4,5-trisphosphate 3-kinase isoenzyme
  JOURNAL   Biochem J 278 (Pt 3) (Pt 3), 883-886 (1991)
   PUBMED   1654894
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Takazawa,K., Perret,J., Dumont,J.E. and Erneux,C.
  TITLE     Molecular cloning and expression of a human brain inositol
            1,4,5-trisphosphate 3-kinase
  JOURNAL   Biochem Biophys Res Commun 174 (2), 529-535 (1991)
   PUBMED   1847047
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Lin,A.N., Barnes,S. and Wallace,R.W.
  TITLE     Phosphorylation by protein kinase C inactivates an inositol
            1,4,5-trisphosphate 3-kinase purified from human platelets
  JOURNAL   Biochem Biophys Res Commun 170 (3), 1371-1376 (1990)
   PUBMED   2167676
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087721.4, X54938.1 and
            DB543073.1.
            
            Summary: Regulates inositol phosphate metabolism by phosphorylation
            of second messenger inositol 1,4,5-trisphosphate to Ins(1,3,4,5)P4.
            The activity of the inositol 1,4,5-trisphosphate 3-kinase is
            responsible for regulating the levels of a large number of inositol
            polyphosphates that are important in cellular signaling. Both
            calcium/calmodulin and protein phosphorylation mechanisms control
            its activity. It is also a substrate for the cyclic AMP-dependent
            protein kinase, calcium/calmodulin- dependent protein kinase II,
            and protein kinase C in vitro.[provided by RefSeq, Apr 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026331.1, X54938.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260386.7/ ENSP00000260386.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1"
     Protein         1..461
                     /product="inositol-trisphosphate 3-kinase A"
                     /EC_number="2.7.1.127"
                     /note="inositol 1,4,5-trisphosphate 3-kinase A; IP3K A;
                     IP3 3-kinase A; insP 3-kinase A"
                     /calculated_mol_wt=50878
     Region          1..133
                     /region_name="Required for cytoskeleton location.
                     /evidence=ECO:0000269|PubMed:12747803"
                     /note="propagated from UniProtKB/Swiss-Prot (P23677.1)"
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23677.1)"
     Site            35
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8R071; propagated from
                     UniProtKB/Swiss-Prot (P23677.1)"
     Region          49..160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23677.1)"
     Site            55
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8R071; propagated from
                     UniProtKB/Swiss-Prot (P23677.1)"
     Site            62
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8R071; propagated from
                     UniProtKB/Swiss-Prot (P23677.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R071; propagated from
                     UniProtKB/Swiss-Prot (P23677.1)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23677.1)"
     Region          245..455
                     /region_name="IPK"
                     /note="Inositol polyphosphate kinase; pfam03770"
                     /db_xref="CDD:397715"
     Region          287..295
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P23677.1)"
     CDS             1..461
                     /gene="ITPKA"
                     /gene_synonym="IP3-3KA; IP3KA"
                     /coded_by="NM_002220.3:55..1440"
                     /db_xref="CCDS:CCDS10076.1"
                     /db_xref="GeneID:3706"
                     /db_xref="HGNC:HGNC:6178"
                     /db_xref="MIM:147521"
ORIGIN      
        1 mtlpggptgm arpggarpcs pgleraprrs vgelrllfea rcaavaaaaa ageprargak
       61 rrggqvpngl prappapvip qltvtaeepd vpptspgppe rerdclpaag sshlqqprrl
      121 stssvsstgs sslledsedd llsdsesrsr gnvqleaged vgqknhwqki rtmvnlpvis
      181 pfkkryawvq laghtgsfka agtsglilkr cseperycla rlmadalrgc vpafhgvver
      241 dgesylqlqd lldgfdgpcv ldckmgvrty leeeltkare rpklrkdmyk kmlavdpeap
      301 teeehaqrav tkprymqwre gisssttlgf riegikkadg scstdfkttr sreqvlrvfe
      361 efvqgdeevl rrylnrlqqi rdtlevseff rrhevigssl lfvhdhchra gvwlidfgkt
      421 tplpdgqild hrrpweegnr edgyllgldn ligilaslae r
//
LOCUS       NP_689474                116 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 263 isoform a [Homo sapiens].
ACCESSION   NP_689474
VERSION     NP_689474.1
DBSOURCE    REFSEQ: accession NM_152261.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Mohajeri,M.S.A., Eslahi,A., Khazaii,Z., Moradi,M.R., Pazhoomand,R.,
            Farrokhi,S., Feizabadi,M.H., Alizadeh,F. and Mojarrad,M.
  TITLE     TMEM263: a novel candidate gene implicated in human autosomal
            recessive severe lethal skeletal dysplasia
  JOURNAL   Hum Genomics 15 (1), 42 (2021)
   PUBMED   34238371
  REMARK    GeneRIF: TMEM263: a novel candidate gene implicated in human
            autosomal recessive severe lethal skeletal dysplasia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Wu,Z., Derks,M.F.L., Dibbits,B., Megens,H.J., Groenen,M.A.M. and
            Crooijmans,R.P.M.A.
  TITLE     A Novel Loss-of-Function Variant in Transmembrane Protein 263
            (TMEM263) of Autosomal Dwarfism in Chicken
  JOURNAL   Front Genet 9, 193 (2018)
   PUBMED   29930570
  REMARK    Erratum:[Front Genet. 2024 Jan 08;14:1349789. doi:
            10.3389/fgene.2023.1349789. PMID: 38259620]
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB091654.1, BC020522.1, AL117658.1 and BM979283.1.
            
            Transcript Variant: This variant (2) contains an alternate exon in
            the 5' UTR compared to variant 1. Variants 1, 2, 3, 4, and 5 encode
            isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001731.1, SRR1803612.189634.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280756.9/ ENSP00000280756.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..116
                     /product="transmembrane protein 263 isoform a"
                     /note="UPF0444 transmembrane protein C12orf23"
                     /calculated_mol_wt=11617
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUH6.1)"
     Site            2
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WUH6.1)"
     Region          25..115
                     /region_name="UPF0444"
                     /note="Transmembrane protein C12orf23, UPF0444; pfam15475"
                     /db_xref="CDD:464737"
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUH6.1)"
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUH6.1)"
     CDS             1..116
                     /gene="TMEM263"
                     /gene_synonym="C12orf23"
                     /coded_by="NM_152261.4:234..584"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9110.1"
                     /db_xref="GeneID:90488"
                     /db_xref="HGNC:HGNC:28281"
ORIGIN      
        1 mnqtdknqqe ipsylndepp egsmkdhpqq qpgmlsrvtg gifsvtkgav gatiggvawi
       61 ggkslevtkt avttvpsmgi glvkggvsav aggvtavgsa vvnkvpltgk kkdksd
//
LOCUS       NP_055292                290 aa            linear   PRI 27-APR-2025
DEFINITION  TP53-target gene 5 protein [Homo sapiens].
ACCESSION   NP_055292
VERSION     NP_055292.1
DBSOURCE    REFSEQ: accession NM_014477.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 290)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Isaka,S., Takei,Y., Tokino,T., Koyama,K., Miyoshi,Y., Suzuki,M.,
            Takahashi,E., Azuma,C., Murata,Y. and Nakamura,Y.
  TITLE     Isolation and characterization of a novel TP53-inducible gene,
            TP53TG5, which suppresses growth and shows cell cycle-dependent
            transition of expression
  JOURNAL   Genes Chromosomes Cancer 27 (4), 345-352 (2000)
   PUBMED   10719363
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021578.4, AB017802.1 and BC036785.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295308.1, SRR5189667.252014.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372726.5/ ENSP00000361811.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..290
                     /product="TP53-target gene 5 protein"
                     /note="TP53-inducible gene 5 protein"
                     /calculated_mol_wt=33888
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2B4.1)"
     Region          28..246
                     /region_name="TP53IP5"
                     /note="Cellular tumour antigen p53-inducible 5; pfam15331"
                     /db_xref="CDD:464651"
     Region          114..178
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2B4.1)"
     CDS             1..290
                     /gene="TP53TG5"
                     /gene_synonym="C20orf10; CLG01"
                     /coded_by="NM_014477.3:90..962"
                     /db_xref="CCDS:CCDS13352.1"
                     /db_xref="GeneID:27296"
                     /db_xref="HGNC:HGNC:15856"
                     /db_xref="MIM:617316"
ORIGIN      
        1 mspsakkrpk nsrvskmqde klrdeteqpv skviernrlr tvlknlsllk llkssnrriq
       61 elhklakrcw hsllsvpkil rissgensac nktkqnneef qeigcsekel kskklestgd
      121 pkkkeykewk sqvqsgmrnk ektslaampr kekhiepevp rtsrddslnp gvqgrqplte
      181 gprvifikpy rnrtpmghmk qldvadqwiw feglptrihl paprvmcrss tlrwvkrrct
      241 rfcsaslemp mwhpykvdvt wtrargasrg wrsrhqlkgr ngwrnsrvyk
//
LOCUS       NP_054757                419 aa            linear   PRI 27-APR-2025
DEFINITION  eIF5-mimic protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_054757
VERSION     NP_054757.1
DBSOURCE    REFSEQ: accession NM_014038.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Li,C., Li,Q., Li,L., Sun,S. and Lei,X.
  TITLE     The Prognostic and Immune Significance of BZW2 in Pan-Cancer and
            its Relationship with Proliferation and Apoptosis of Cervical
            Cancer
  JOURNAL   Front Biosci (Landmark Ed) 29 (3), 97 (2024)
   PUBMED   38538258
  REMARK    GeneRIF: The Prognostic and Immune Significance of BZW2 in
            Pan-Cancer and its Relationship with Proliferation and Apoptosis of
            Cervical Cancer.
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Maio,G., Smith,M., Bhawal,R., Zhang,S., Baskin,J.M., Li,J. and
            Lin,H.
  TITLE     Interactome Analysis Identifies the Role of BZW2 in Promoting
            Endoplasmic Reticulum-Mitochondria Contact and Mitochondrial
            Metabolism
  JOURNAL   Mol Cell Proteomics 23 (2), 100709 (2024)
   PUBMED   38154691
  REMARK    GeneRIF: Interactome Analysis Identifies the Role of BZW2 in
            Promoting Endoplasmic Reticulum-Mitochondria Contact and
            Mitochondrial Metabolism.
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Agarwal,S., Afaq,F., Bajpai,P., Behring,M., Kim,H.G.,
            Varambally,A., Chandrashekar,D.S., Peter,S., Diffalha,S.A.,
            Khushman,M., Seeber,A., Varambally,S. and Manne,U.
  TITLE     BZW2 Inhibition Reduces Colorectal Cancer Growth and Metastasis
  JOURNAL   Mol Cancer Res 21 (7), 698-712 (2023)
   PUBMED   37067340
  REMARK    GeneRIF: BZW2 Inhibition Reduces Colorectal Cancer Growth and
            Metastasis.
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Huang,X., Yang,Z., Li,Y. and Long,X.
  TITLE     m6A methyltransferase METTL3 facilitates multiple myeloma cell
            growth through the m6A modification of BZW2
  JOURNAL   Ann Hematol 102 (7), 1801-1810 (2023)
   PUBMED   37222774
  REMARK    GeneRIF: m6A methyltransferase METTL3 facilitates multiple myeloma
            cell growth through the m6A modification of BZW2.
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Long,X., Li,J., Wen,F., Cao,Y., Luo,Z. and Luo,C.
  TITLE     miR-140-3p attenuated the tumorigenesis of multiple myeloma via
            attenuating BZW2
  JOURNAL   Hematology 27 (1), 173-180 (2022)
   PUBMED   35068373
  REMARK    GeneRIF: miR-140-3p attenuated the tumorigenesis of multiple
            myeloma via attenuating BZW2.
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Sherva,R., Tripodis,Y., Bennett,D.A., Chibnik,L.B., Crane,P.K., de
            Jager,P.L., Farrer,L.A., Saykin,A.J., Shulman,J.M., Naj,A. and
            Green,R.C.
  CONSRTM   GENAROAD Consortium; Alzheimer's Disease Neuroimaging Initiative;
            Alzheimer's Disease Genetics Consortium
  TITLE     Genome-wide association study of the rate of cognitive decline in
            Alzheimer's disease
  JOURNAL   Alzheimers Dement 10 (1), 45-52 (2014)
   PUBMED   23535033
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Singh,C.R., Watanabe,R., Zhou,D., Jennings,M.D., Fukao,A., Lee,B.,
            Ikeda,Y., Chiorini,J.A., Campbell,S.G., Ashe,M.P., Fujiwara,T.,
            Wek,R.C., Pavitt,G.D. and Asano,K.
  TITLE     Mechanisms of translational regulation by a human eIF5-mimic
            protein
  JOURNAL   Nucleic Acids Res 39 (19), 8314-8328 (2011)
   PUBMED   21745818
  REMARK    GeneRIF: 5MP1 (BZW2) acts as a partial mimic and competitor of
            eIF5, interfering with the key steps by which eIF5 regulates eIF2
            function.
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF083246.1 and BC009597.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 4 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008453.1, SRR5189658.119037.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258761.8/ ENSP00000258761.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.1"
     Protein         1..419
                     /product="eIF5-mimic protein 1 isoform 1"
                     /note="basic leucine zipper and W2 domain-containing
                     protein 2; eIF5-mimic protein 1"
                     /calculated_mol_wt=48031
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6E2.1)"
     Site            117
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6E2.1)"
     Region          218..408
                     /region_name="W2_eIF5C_like"
                     /note="C-terminal W2 domain of the eukaryotic translation
                     initiation factor 5C and similar proteins; cd11560"
                     /db_xref="CDD:211398"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9Y6E2.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6E2.1)"
     CDS             1..419
                     /gene="BZW2"
                     /gene_synonym="5MP1; HSPC028; MST017; MSTP017"
                     /coded_by="NM_014038.3:116..1375"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5362.1"
                     /db_xref="GeneID:28969"
                     /db_xref="HGNC:HGNC:18808"
                     /db_xref="MIM:619275"
ORIGIN      
        1 mnkhqkpvlt gqrfktrkrd ekekfeptvf rdtlvqglne agddleavak fldstgsrld
       61 yrryadtlfd ilvagsmlap ggtriddgdk tkmtnhcvfs anedhetirn yaqvfnklir
      121 rykylekafe demkklllfl kafseteqtk lamlsgillg ngtlpatilt slftdslvke
      181 giaasfavkl fkawmaekda nsvtsslrka nldkrllelf pvnrqsvdhf akyftdaglk
      241 elsdflrvqq slgtrkelqk elqerlsqec pikevvlyvk eemkrndlpe tavigllwtc
      301 imnavewnkk eelvaeqalk hlkqyaplla vfssqgqsel illqkvqeyc ydnihfmkaf
      361 qkivvlfyka dvlseeailk wykeahvakg ksvfldqmkk fvewlqnaee esesegeen
//
LOCUS       NP_848638                458 aa            linear   PRI 27-APR-2025
DEFINITION  ectonucleotide pyrophosphatase/phosphodiesterase family member 7
            precursor [Homo sapiens].
ACCESSION   NP_848638
VERSION     NP_848638.3
DBSOURCE    REFSEQ: accession NM_178543.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Gorelik,A., Liu,F., Illes,K. and Nagar,B.
  TITLE     Crystal structure of the human alkaline sphingomyelinase provides
            insights into substrate recognition
  JOURNAL   J Biol Chem 292 (17), 7087-7094 (2017)
   PUBMED   28292932
  REMARK    GeneRIF: human alkaline sphingomyelinase crystal structure provides
            insights into substrate recognition
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Duan,R.D., Hindorf,U., Cheng,Y., Bergenzaun,P., Hall,M.,
            Hertervig,E. and Nilsson,A.
  TITLE     Changes of activity and isoforms of alkaline sphingomyelinase
            (nucleotide pyrophosphatase phosphodiesterase 7) in bile from
            patients undergoing endoscopic retrograde cholangiopancreatography
  JOURNAL   BMC Gastroenterol 14, 138 (2014)
   PUBMED   25100243
  REMARK    GeneRIF: NPP7 activity and the ratio of 1.4/1.2 kb products in bile
            are significantly decreased in malignancy, particularly in
            cholangiocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Parrill,A.L., Wanjala,I.W., Pham,T.C. and Baker,D.L.
  TITLE     Computational identification and experimental characterization of
            substrate binding determinants of nucleotide
            pyrophosphatase/phosphodiesterase 7
  JOURNAL   BMC Biochem 12, 65 (2011)
   PUBMED   22177013
  REMARK    GeneRIF: The F275A mutation of NPP7 showed impaired catalytic
            function whereas L107F mutation showed enhanced catalytic activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Duan,J., Wu,J., Cheng,Y. and Duan,R.D.
  TITLE     Understanding the molecular activity of alkaline sphingomyelinase
            (NPP7) by computer modeling
  JOURNAL   Biochemistry 49 (42), 9096-9105 (2010)
   PUBMED   20839774
  REMARK    GeneRIF: predict the three-dimensional structure of NPP7 by
            homology modeling using a recently crystallized NPP from bacteria.
            Using the model, we studied the substrate specificity of the enzyme
            by docking.
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Wu,J., Hansen,G.H., Nilsson,A. and Duan,R.D.
  TITLE     Functional studies of human intestinal alkaline sphingomyelinase by
            deglycosylation and mutagenesis
  JOURNAL   Biochem J 386 (Pt 1), 153-160 (2005)
   PUBMED   15458386
  REMARK    GeneRIF: alk-SMase activity is severely affected by defective
            N-glycosylation at 5 sites and by structural alterations of the
            putative metal-binding sites and the predicted active core.
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Wu,J., Liu,F., Nilsson,A. and Duan,R.D.
  TITLE     Pancreatic trypsin cleaves intestinal alkaline sphingomyelinase
            from mucosa and enhances the sphingomyelinase activity
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 287 (5), G967-G973 (2004)
   PUBMED   15205117
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Wu,J., Cheng,Y., Nilsson,A. and Duan,R.D.
  TITLE     Identification of one exon deletion of intestinal alkaline
            sphingomyelinase in colon cancer HT-29 cells and a
            differentiation-related expression of the wild-type enzyme in
            Caco-2 cells
  JOURNAL   Carcinogenesis 25 (8), 1327-1333 (2004)
   PUBMED   15016655
  REMARK    GeneRIF: intestinal alkaline sphingomyelinase may have a one-exon
            deletion in colon cancer cells
REFERENCE   9  (residues 1 to 458)
  AUTHORS   Duan,R.D., Bergman,T., Xu,N., Wu,J., Cheng,Y., Duan,J.,
            Nelander,S., Palmberg,C. and Nilsson,A.
  TITLE     Identification of human intestinal alkaline sphingomyelinase as a
            novel ecto-enzyme related to the nucleotide phosphodiesterase
            family
  JOURNAL   J Biol Chem 278 (40), 38528-38536 (2003)
   PUBMED   12885774
  REMARK    GeneRIF: identified the amino acid and cDNA sequences of human
            intestinal alk-SMase, and found that it is a novel ecto-enzyme
            related to the ecto-nucleotide phosphodiesterase family with
            specific features essential for its SMase activity
REFERENCE   10 (residues 1 to 458)
  AUTHORS   Duan,R.D., Cheng,Y., Hansen,G., Hertervig,E., Liu,J.J., Syk,I.,
            Sjostrom,H. and Nilsson,A.
  TITLE     Purification, localization, and expression of human intestinal
            alkaline sphingomyelinase
  JOURNAL   J Lipid Res 44 (6), 1241-1250 (2003)
   PUBMED   12671034
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC233701.6, DB187443.1 and
            BC041453.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 18, 2013 this sequence version replaced NP_848638.2.
            
            Summary: The protein encoded by this gene is an intestinal alkaline
            sphingomyelin phosphodiesterase that converts sphingomyelin to
            ceramide and phosphocholine. The encoded protein is anchored in the
            cell membrane, and it may function to protect the intestinal mucosa
            from inflammation and tumorigenesis. This protein is glycosylated
            and also exhibits lysophosphatidylcholine hydrolase activity.
            [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358622.1, AK126250.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2144835
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000328313.10/
                                                ENSP00000332656.5
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..458
                     /product="ectonucleotide pyrophosphatase/phosphodiesterase
                     family member 7 precursor"
                     /EC_number="3.1.4.12"
                     /note="alkaline sphingomyelinase; ectonucleotide
                     pyrophosphatase/phosphodiesterase family member 7;
                     intestinal alkaline sphingomyelinase; alkaline
                     sphingomyelin phosphodiesterase"
                     /calculated_mol_wt=49504
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1992
     mat_peptide     22..458
                     /product="Ectonucleotide pyrophosphatase/phosphodiesterase
                     family member 7. /id=PRO_0000036403"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWV6.4)"
                     /calculated_mol_wt=49504
     Region          31..396
                     /region_name="Enpp"
                     /note="Ectonucleotide pyrophosphatase/phosphodiesterase,
                     also called autotaxin; cd16018"
                     /db_xref="CDD:293742"
     Site            order(39,74..75,96,199,203,246..247,353)
                     /site_type="active"
                     /db_xref="CDD:293742"
     Site            order(39,74..75,96,199,203,247,353)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293742"
     Region          72..78
                     /region_name="Required for enzyme activity.
                     /evidence=ECO:0000269|PubMed:15458386"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWV6.4)"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15458386,
                     ECO:0000269|PubMed:28292932, ECO:0007744|PDB:5TCD,
                     ECO:0007744|PDB:5UDY; propagated from UniProtKB/Swiss-Prot
                     (Q6UWV6.4)"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15458386,
                     ECO:0000269|PubMed:28292932, ECO:0007744|PDB:5TCD,
                     ECO:0007744|PDB:5UDY; propagated from UniProtKB/Swiss-Prot
                     (Q6UWV6.4)"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15458386,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:28292932,
                     ECO:0007744|PDB:5TCD, ECO:0007744|PDB:5UDY; propagated
                     from UniProtKB/Swiss-Prot (Q6UWV6.4)"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15458386,
                     ECO:0000269|PubMed:28292932, ECO:0007744|PDB:5TCD,
                     ECO:0007744|PDB:5UDY; propagated from UniProtKB/Swiss-Prot
                     (Q6UWV6.4)"
     Site            267
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15458386,
                     ECO:0000269|PubMed:28292932, ECO:0007744|PDB:5TCD;
                     propagated from UniProtKB/Swiss-Prot (Q6UWV6.4)"
     Site            378..380
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293742"
     Site            434..454
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWV6.4)"
     CDS             1..458
                     /gene="ENPP7"
                     /gene_synonym="ALK-SMase; E-NPP 7; NPP-7; NPP7"
                     /coded_by="NM_178543.5:198..1574"
                     /db_xref="CCDS:CCDS11763.1"
                     /db_xref="GeneID:339221"
                     /db_xref="HGNC:HGNC:23764"
                     /db_xref="MIM:616997"
ORIGIN      
        1 mrgpavlltv alatllapga gapvqsqgsq nklllvsfdg frwnydqdvd tpnldamard
       61 gvkarymtpa fvtmtspchf tlvtgkyien hgvvhnmyyn ttskvklpyh atlgiqrwwd
      121 ngsvpiwita qrqglragsf fypggnvtyq gvavtrsrke giahnyknet ewranidtvm
      181 awfteedldl vtlyfgepds tghrygpesp erremvrqvd rtvgylresi arnhltdrln
      241 liitsdhgmt tvdkragdlv efhkfpnftf rdiefelldy gpngmllpke grlekvydal
      301 kdahpklhvy kkeafpeafh yannprvtpl lmysdlgyvi hgrinvqfnn gehgfdnkdm
      361 dmktifravg psfragleve pfesvhvyel mcrllgivpe andghlatll pmlhtesalp
      421 pdgrptllpk grsalppssr pllvmgllgt villseva
//
LOCUS       NP_116307                199 aa            linear   PRI 27-APR-2025
DEFINITION  ras-related and estrogen-regulated growth inhibitor isoform 1 [Homo
            sapiens].
ACCESSION   NP_116307
VERSION     NP_116307.1
DBSOURCE    REFSEQ: accession NM_032918.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Jin,S., Li,X., Dai,Y., Li,C. and Wang,D.
  TITLE     NF-kappaB-mediated miR-650 plays oncogenic roles and activates
            AKT/ERK/NF-kappaB pathways by targeting RERG in glioma cells
  JOURNAL   Cell Oncol (Dordr) 43 (6), 1035-1048 (2020)
   PUBMED   32986146
  REMARK    GeneRIF: NF-kappaB-mediated miR-650 plays oncogenic roles and
            activates AKT/ERK/NF-kappaB pathways by targeting RERG in glioma
            cells.
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Xiong,Y., Huang,H., Chen,S., Dai,H. and Zhang,L.
  TITLE     ERK5-regulated RERG expression promotes cancer progression in
            prostatic carcinoma
  JOURNAL   Oncol Rep 41 (2), 1160-1168 (2019)
   PUBMED   30431143
  REMARK    GeneRIF: Study revealed that ERK5 can inhibit Raslike
            oestrogenregulated growth inhibitor (RERG) protein expression and
            that the inhibition of RERG expression promotes prostatic carcinoma
            cell proliferation and migration.
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Zhao,W., Mo,Y., Wang,S., Midorikawa,K., Ma,N., Hiraku,Y.,
            Oikawa,S., Huang,G., Zhang,Z., Murata,M. and Takeuchi,K.
  TITLE     Quantitation of DNA methylation in Epstein-Barr virus-associated
            nasopharyngeal carcinoma by bisulfite amplicon sequencing
  JOURNAL   BMC Cancer 17 (1), 489 (2017)
   PUBMED   28716111
  REMARK    GeneRIF: In particular, methylation levels of ITGA4, RERG, and
            ZNF671 could distinguish Nasopharyngeal carcinoma (NPC) patients
            from non-cancer nasopharyngeal epithelium (NNE) subjects.  We
            identified the DNA methylation rates of previously unidentified NPC
            candidate genes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 199)
  AUTHORS   Ho,J.Y., Hsu,R.J., Liu,J.M., Chen,S.C., Liao,G.S., Gao,H.W. and
            Yu,C.P.
  TITLE     MicroRNA-382-5p aggravates breast cancer progression by regulating
            the RERG/Ras/ERK signaling axis
  JOURNAL   Oncotarget 8 (14), 22443-22459 (2017)
   PUBMED   27705918
  REMARK    GeneRIF: this study shows that miR-382-5p expression is negatively
            correlated with RERG expression, and functions as an independent
            oncomiR for the higher incidence and poorer prognosis of breast
            cancer
REFERENCE   7  (residues 1 to 199)
  AUTHORS   Monsivais,D., Dyson,M.T., Yin,P., Coon,J.S., Navarro,A., Feng,G.,
            Malpani,S.S., Ono,M., Ercan,C.M., Wei,J.J., Pavone,M.E., Su,E. and
            Bulun,S.E.
  TITLE     ERbeta- and prostaglandin E2-regulated pathways integrate cell
            proliferation via Ras-like and estrogen-regulated growth inhibitor
            in endometriosis
  JOURNAL   Mol Endocrinol 28 (8), 1304-1315 (2014)
   PUBMED   24992181
  REMARK    GeneRIF: Estradiol estrogen receptor-beta and PGE2 integrate at
            RERG, leading to increased endometriotic cell proliferation.
REFERENCE   8  (residues 1 to 199)
  AUTHORS   Chile,T., Correa-Giannella,M.L., Fortes,M.A., Bronstein,M.D.,
            Cunha-Neto,M.B., Giannella-Neto,D. and Giorgi,R.R.
  TITLE     Expression of CRABP1, GRP, and RERG mRNA in clinically
            non-functioning and functioning pituitary adenomas
  JOURNAL   J Endocrinol Invest 34 (8), e214-e218 (2011)
   PUBMED   21270509
  REMARK    GeneRIF: Results describe the mRNA expression of CRABP1, RERG, and
            GRP in pituitary adenomas.
REFERENCE   9  (residues 1 to 199)
  AUTHORS   Habashy,H.O., Powe,D.G., Glaab,E., Ball,G., Spiteri,I.,
            Krasnogor,N., Garibaldi,J.M., Rakha,E.A., Green,A.R., Caldas,C. and
            Ellis,I.O.
  TITLE     RERG (Ras-like, oestrogen-regulated, growth-inhibitor) expression
            in breast cancer: a marker of ER-positive luminal-like subtype
  JOURNAL   Breast Cancer Res Treat 128 (2), 315-326 (2011)
   PUBMED   20697807
  REMARK    GeneRIF: Loss of RERG expression is associated with breast cancer
            and distant metastasis.
REFERENCE   10 (residues 1 to 199)
  AUTHORS   Finlin,B.S., Gau,C.L., Murphy,G.A., Shao,H., Kimel,T., Seitz,R.S.,
            Chiu,Y.F., Botstein,D., Brown,P.O., Der,C.J., Tamanoi,F.,
            Andres,D.A. and Perou,C.M.
  TITLE     RERG is a novel ras-related, estrogen-regulated and
            growth-inhibitory gene in breast cancer
  JOURNAL   J Biol Chem 276 (45), 42259-42267 (2001)
   PUBMED   11533059
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC331754.1 and BC007997.1.
            
            Summary: RERG, a member of the RAS superfamily of GTPases, inhibits
            cell proliferation and tumor formation (Finlin et al., 2001 [PubMed
            11533059]).[supplied by OMIM, Mar 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007997.1, AK313881.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467147
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256953.6/ ENSP00000256953.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.3"
     Protein         1..199
                     /product="ras-related and estrogen-regulated growth
                     inhibitor isoform 1"
                     /EC_number="3.6.5.2"
                     /note="ras-related and estrogen-regulated growth
                     inhibitor"
                     /calculated_mol_wt=22477
     Region          8..169
                     /region_name="RERG_RasL11_like"
                     /note="Ras-related and Estrogen-Regulated Growth inhibitor
                     (RERG) and Ras-like 11 (RasL11)-like families; cd04146"
                     /db_xref="CDD:206713"
     Site            13..20
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206713"
     Site            order(14..15,62..63)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206713"
     Site            order(16..21,34,118..119,121,148..150)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206713"
     Site            order(20..21,35,37,43..44,57..58,60,62..63,150)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206713"
     Site            order(36..39,42..44)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206713"
     Site            order(36..37,41..44)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206713"
     Site            38
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206713"
     Site            60..63
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206713"
     Site            order(62..63,68..79)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206713"
     Site            118..121
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206713"
     Site            148..150
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206713"
     CDS             1..199
                     /gene="RERG"
                     /coded_by="NM_032918.3:338..937"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8673.1"
                     /db_xref="GeneID:85004"
                     /db_xref="HGNC:HGNC:15980"
                     /db_xref="MIM:612664"
ORIGIN      
        1 maksaevkla ifgragvgks alvvrfltkr fiweydptle styrhqatid devvsmeild
       61 tagqedtiqr eghmrwgegf vlvyditdrg sfeevlplkn ildeikkpkn vtlilvgnka
      121 dldhsrqvst eegeklatel acafyecsac tgegniteif yelcrevrrr rmvqgktrrr
      181 sstthvkqai nkmltkiss
//
LOCUS       NP_060647               1770 aa            linear   PRI 27-APR-2025
DEFINITION  NEDD4-binding protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_060647
VERSION     NP_060647.2
DBSOURCE    REFSEQ: accession NM_018177.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1770)
  AUTHORS   Leslie,E.J., Carlson,J.C., Shaffer,J.R., Buxo,C.J., Castilla,E.E.,
            Christensen,K., Deleyiannis,F.W.B., Field,L.L., Hecht,J.T.,
            Moreno,L., Orioli,I.M., Padilla,C., Vieira,A.R., Wehby,G.L.,
            Feingold,E., Weinberg,S.M., Murray,J.C. and Marazita,M.L.
  TITLE     Association studies of low-frequency coding variants in
            nonsyndromic cleft lip with or without cleft palate
  JOURNAL   Am J Med Genet A 173 (6), 1531-1538 (2017)
   PUBMED   28425186
  REMARK    GeneRIF: We found that a burden of low-frequency coding variants in
            N4BP2, CDSN, PRTG, and AHRR were associated with increased risk of
            Nonsyndromic cleft lip with or without cleft palate (NSCL/P) .
            Low-frequency variants in other genes were associated with
            decreased risk of NSCL/P. These results demonstrate that
            low-frequency variants contribute to the genetic etiology of NSCL/P
REFERENCE   2  (residues 1 to 1770)
  AUTHORS   Jeong,E.Y., Kim,T.G. and Ban,C.
  TITLE     Modulated nicking endonuclease function by the N-terminal extended
            region of the smr domain in human Bcl-3 binding protein
  JOURNAL   Proteins 80 (1), 327-332 (2012)
   PUBMED   22072629
  REMARK    GeneRIF: the N-terminal extended region of the Smr domain in the
            native B3bp may function as a regulatory region for the nicking
            endonuclease
REFERENCE   3  (residues 1 to 1770)
  AUTHORS   Diercks,T., AB,E., Daniels,M.A., de Jong,R.N., Besseling,R.,
            Kaptein,R. and Folkers,G.E.
  TITLE     Solution structure and characterization of the DNA-binding activity
            of the B3BP-Smr domain
  JOURNAL   J Mol Biol 383 (5), 1156-1170 (2008)
   PUBMED   18804481
  REMARK    GeneRIF: The solution structure of the functionally active Smr
            domain of the Bcl3-binding protein (also known as Nedd4-binding
            protein 2), a protein with unknown function that lacks other
            domains present in MutS proteins, is determined.
REFERENCE   4  (residues 1 to 1770)
  AUTHORS   Oshikawa,M., Sugai,Y., Usami,R., Ohtoko,K., Toyama,S. and Kato,S.
  TITLE     Fine expression profiling of full-length transcripts using a
            size-unbiased cDNA library prepared with the vector-capping method
  JOURNAL   DNA Res 15 (3), 123-136 (2008)
   PUBMED   18487259
REFERENCE   5  (residues 1 to 1770)
  AUTHORS   Zheng,M.Z., Qin,H.D., Yu,X.J., Zhang,R.H., Chen,L.Z., Feng,Q.S. and
            Zeng,Y.X.
  TITLE     Haplotype of gene Nedd4 binding protein 2 associated with sporadic
            nasopharyngeal carcinoma in the Southern Chinese population
  JOURNAL   J Transl Med 5, 36 (2007)
   PUBMED   17626640
  REMARK    GeneRIF: These data suggest that haplotype blocks ATTA and GTTG of
            N4BP2 is correlation with the risk of sporadic nasopharyngeal
            carcinoma in the Southern Chinese population.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1770)
  AUTHORS   Watanabe,N., Wachi,S. and Fujita,T.
  TITLE     Identification and characterization of BCL-3-binding protein:
            implications for transcription and DNA repair or recombination
  JOURNAL   J Biol Chem 278 (28), 26102-26110 (2003)
   PUBMED   12730195
  REMARK    GeneRIF: B3BP is a 5'-polynucleotide kinase
REFERENCE   7  (residues 1 to 1770)
  AUTHORS   Murillas,R., Simms,K.S., Hatakeyama,S., Weissman,A.M. and
            Kuehn,M.R.
  TITLE     Identification of developmentally expressed proteins that
            functionally interact with Nedd4 ubiquitin ligase
  JOURNAL   J Biol Chem 277 (4), 2897-2907 (2002)
   PUBMED   11717310
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098591.4, AK001542.1,
            BC126466.1, AC095057.3, AB371584.1 and AW135590.1.
            
            On Jun 13, 2003 this sequence version replaced NP_060647.1.
            
            Summary: This gene encodes a protein containing a polynucleotide
            kinase domain (PNK) near the N-terminal region, and a Small MutS
            Related (Smr) domain near the C-terminal region. The encoded
            protein can bind to both B-cell leukemia/lymphoma 3 (BCL-3) and
            neural precursor cell expressed, developmentally downregulated 4,
            (Nedd4) proteins. This protein binds and hydrolyzes ATP, may
            function as a 5'-polynucleotide kinase, and has the capacity to be
            a ubiquitylation substrate. This protein may play a role in
            transcription-coupled DNA repair or genetic recombination.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY267013.1, BC126466.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261435.11/ ENSP00000261435.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1770
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..1770
                     /product="NEDD4-binding protein 2 isoform 1"
                     /note="BCL-3-binding protein"
                     /calculated_mol_wt=198671
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          47..87
                     /region_name="CUE_N4BP2"
                     /note="CUE domain found in NEDD4-binding protein 2 (N4BP2)
                     and similar proteins; cd14365"
                     /db_xref="CDD:270548"
     Region          95..129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          449..580
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
     Region          712..756
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          795..822
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          836..862
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          890..913
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Site            906
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UW6.2)"
     Site            1210
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          1580..1606
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          1621..1682
                     /region_name="DUF1771"
                     /note="Domain of unknown function (DUF1771); pfam08590"
                     /db_xref="CDD:462528"
     Region          1688..1770
                     /region_name="SMR"
                     /note="Small MutS-related domain; smart00463"
                     /db_xref="CDD:214676"
     CDS             1..1770
                     /gene="N4BP2"
                     /gene_synonym="B3BP"
                     /coded_by="NM_018177.6:393..5705"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3457.1"
                     /db_xref="GeneID:55728"
                     /db_xref="HGNC:HGNC:29851"
                     /db_xref="MIM:619139"
ORIGIN      
        1 mprrrknlgg npfrktanpk evvvssvasr eeptttlpsm getkvdqeel ftsiseifsd
       61 ldpdvvylml secdfkvena mdcllelsat dtkieesssq sfvasenqvg aaeskimekr
      121 peeesedskm dsfldmqlte dldsliqnaf eklnsspddq vysflpsqdv nsfndssefi
      181 npdssnmtpi fstqnmnlng enlensgstl slnplpshsv lneskcfikd ntlalesnyp
      241 edsllsssln vasdsiagcs slnqkqkell esecveaqfs eapvdldase pqaclnlpgl
      301 dlpgtggdqk strvsdvflp segfnfkphk hpelptkgkd vsycpvlapl plllpppppp
      361 pmwnpmipaf dlfqgnhgfv apvvttaahw rsvnytfpps vishtsptkv wrnkdgtsay
      421 qvqetpvsqv vrkktsyvgl vlvllrglpg sgksflartl qednpsgvil stddyfying
      481 qyqfdvkylg eahewnqnra keafekkisp iiidntnlqa wemkpyvals qkhkykvlfr
      541 epdtwwkfkp kelarrnihg vskekitrml ehyqrfvsvp iimsssvpek ierielcays
      601 cedrstsprd dediisekee nilslslkhl efteeknldv tketmlpenv aylsnadlnk
      661 rrkeisdmnp siqsalilet phmyfsdses klqatdksen eqiemvavkg ysktdtdssm
      721 ervspstccs ennqedcdla nsgplqneks spgeiveera tvtkkafgkq kskstlekfp
      781 rhelsnfvgd wpvdktigqr tkrnrktekt ssvqsdkkyn ypqshklvns vsvntdcvqq
      841 rgsphesved grksqcddas eplnsykyda yknidknsfn imgdwpssds laqrehrsrm
      901 pktglsepnl eigtndkmne islstaheac wgtssqklkt lgssnlgsse mllsemtces
      961 qtclskkshg qhtslpltft nsaptvsgvv epqtlaecqe qmpkrdpgke vgmctqtepq
     1021 dfallwkiek nkisisdsik vltgrldgfk pkvfnintks dvqeaipyrv mydkstfvee
     1081 seltsadese nlnilcklfg sfslealkdl yercnkdiiw atsllldset klcedtefen
     1141 fqkscdgsqi gpfslglnlk eiisqrgtle nsnspvpefs hgigisnads qstcdaergn
     1201 seqaemravt penhesmtsi fpsaavglkn nndilpnsqe ellysskqsf pgilkattpk
     1261 dmseteknlv vtetgdnihs pshfsdifnf vsstsnleln eeiyftdsle ikrnenfpkd
     1321 yvkfsdeeef mnedekemke ilmagsslsa gvsgedktei lnptpamaks ltidclelal
     1381 ppelafqlne lfgpvgidsg sltvedcvvh idlnlakvih ekwkesvmer qrqeevscgk
     1441 fmqdpslvgh tgldnpeqks sqrtgkkllk tltasemlpl ldhwntqtkk vslreimsee
     1501 ialqekhnlk retlmfekdc atklkekqlf kifpainqnf lvdifkdhny slehtvqfln
     1561 cvlegdpvkt vvaqefvhqn envtshtgqk skekkpkklk eteetpsels fqdfeypdyd
     1621 dyraeaflhq qkrmecyska keayrigkkn vatfyaqqgt lheqkmkean hlaaieifek
     1681 vnasllpqnv ldlhglhvde alehlmrvle kkteefkqng gkpylsvitg rgnhsqggva
     1741 rikpavikyl ishsfrfsei kpgclkvmlk
//
LOCUS       NP_653195                167 aa            linear   PRI 27-APR-2025
DEFINITION  gametocyte-specific factor 1 [Homo sapiens].
ACCESSION   NP_653195
VERSION     NP_653195.2
DBSOURCE    REFSEQ: accession NM_144594.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Ipsaro,J.J., O'Brien,P.A., Bhattacharya,S., Palmer,A.G. 3rd and
            Joshua-Tor,L.
  TITLE     Asterix/Gtsf1 links tRNAs and piRNA silencing of retrotransposons
  JOURNAL   Cell Rep 34 (13), 108914 (2021)
   PUBMED   33789107
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Huntriss,J., Lu,J., Hemmings,K., Bayne,R., Anderson,R.,
            Rutherford,A., Balen,A., Elder,K. and Picton,H.M.
  TITLE     Isolation and expression of the human gametocyte-specific factor 1
            gene (GTSF1) in fetal ovary, oocytes, and preimplantation embryos
  JOURNAL   J Assist Reprod Genet 34 (1), 23-31 (2017)
   PUBMED   27646122
  REMARK    GeneRIF: To our knowledge, this report is the first to describe the
            expression of the human GTSF1 gene in human gametes and
            preimplantation embryos.
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Litvinov,I.V., Cordeiro,B., Huang,Y., Zargham,H., Pehr,K.,
            Dore,M.A., Gilbert,M., Zhou,Y., Kupper,T.S. and Sasseville,D.
  TITLE     Ectopic expression of cancer-testis antigens in cutaneous T-cell
            lymphoma patients
  JOURNAL   Clin Cancer Res 20 (14), 3799-3808 (2014)
   PUBMED   24850846
  REMARK    GeneRIF: SYCP1, cTAGE1, and GTSF1 are expressed in cutaneous T-cell
            lymphoma, but not in normal skin or benign inflammatory dermatoses.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK098819.1 and BE503352.1.
            
            On Jul 18, 2008 this sequence version replaced NP_653195.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.18635.1,
                                           SRR5189658.222449.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2148093 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305879.8/ ENSP00000304185.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..167
                     /product="gametocyte-specific factor 1"
                     /note="family with sequence similarity 112, member B;
                     asterix"
                     /calculated_mol_wt=19135
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WW33.2)"
     Region          14..38
                     /region_name="zf-U11-48K"
                     /note="U11-48K-like CHHC zinc finger; pfam05253"
                     /db_xref="CDD:461603"
     Region          48..71
                     /region_name="zf-U11-48K"
                     /note="U11-48K-like CHHC zinc finger; pfam05253"
                     /db_xref="CDD:461603"
     CDS             1..167
                     /gene="GTSF1"
                     /gene_synonym="Cue110; FAM112B"
                     /coded_by="NM_144594.3:87..590"
                     /db_xref="CCDS:CCDS8881.1"
                     /db_xref="GeneID:121355"
                     /db_xref="HGNC:HGNC:26565"
                     /db_xref="MIM:617484"
ORIGIN      
        1 meetytdsld pekllqcpyd knhqiracrf pyhlikcrkn hpdvasklat cpfnarhqvp
       61 raeishhiss cddrscieqd vvnqtrslrq etlaestwqc ppcdedwdkd lweqtstpfv
      121 wgtthysdnn spasnivteh knnlasgmrv pkslpyvlpw knngnaq
//
LOCUS       NP_001350233             328 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear distribution protein nudE-like 1 isoform 2 [Mus musculus].
ACCESSION   NP_001350233 XP_006534603
VERSION     NP_001350233.1
DBSOURCE    REFSEQ: accession NM_001363304.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Das,B.K., Gogoi,J., Kannan,A., Gao,L., Xing,W., Mohan,S. and
            Zhao,H.
  TITLE     The Cytoplasmic Dynein Associated Protein NDE1 Regulates
            Osteoclastogenesis by Modulating M-CSF and RANKL Signaling Pathways
  JOURNAL   Cells 11 (1), 13 (2021)
   PUBMED   35011575
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Amberg,N. and Hippenmeyer,S.
  TITLE     Genetic mosaic dissection of candidate genes in mice using mosaic
            analysis with double markers
  JOURNAL   STAR Protoc 2 (4), 100939 (2021)
   PUBMED   34825212
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Kim,Y.B., Hlavaty,D., Maycock,J. and Lechler,T.
  TITLE     Roles for Ndel1 in keratin organization and desmosome function
  JOURNAL   Mol Biol Cell 32 (20), ar2 (2021)
   PUBMED   34319758
  REMARK    GeneRIF: Roles for Ndel1 in keratin organization and desmosome
            function.
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Gavrilovici,C., Jiang,Y., Kiroski,I., Sterley,T.L., Vandal,M.,
            Bains,J., Park,S.K., Rho,J.M., Teskey,G.C. and Nguyen,M.D.
  TITLE     Behavioral Deficits in Mice with Postnatal Disruption of Ndel1 in
            Forebrain Excitatory Neurons: Implications for Epilepsy and
            Neuropsychiatric Disorders
  JOURNAL   Cereb Cortex Commun 2 (1), tgaa096 (2021)
   PUBMED   33615226
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Ozeki,Y., Tomoda,T., Kleiderlein,J., Kamiya,A., Bord,L., Fujii,K.,
            Okawa,M., Yamada,N., Hatten,M.E., Snyder,S.H., Ross,C.A. and
            Sawa,A.
  TITLE     Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents
            binding to NudE-like (NUDEL) and inhibits neurite outgrowth
  JOURNAL   Proc Natl Acad Sci U S A 100 (1), 289-294 (2003)
   PUBMED   12506198
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13969]
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Ko,J., Humbert,S., Bronson,R.T., Takahashi,S., Kulkarni,A.B., Li,E.
            and Tsai,L.H.
  TITLE     p35 and p39 are essential for cyclin-dependent kinase 5 function
            during neurodevelopment
  JOURNAL   J Neurosci 21 (17), 6758-6771 (2001)
   PUBMED   11517264
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Sweeney,K.J., Prokscha,A. and Eichele,G.
  TITLE     NudE-L, a novel Lis1-interacting protein, belongs to a family of
            vertebrate coiled-coil proteins
  JOURNAL   Mech Dev 101 (1-2), 21-33 (2001)
   PUBMED   11231056
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Niethammer,M., Smith,D.S., Ayala,R., Peng,J., Ko,J., Lee,M.S.,
            Morabito,M. and Tsai,L.H.
  TITLE     NUDEL is a novel Cdk5 substrate that associates with LIS1 and
            cytoplasmic dynein
  JOURNAL   Neuron 28 (3), 697-711 (2000)
   PUBMED   11163260
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Sasaki,S., Shionoya,A., Ishida,M., Gambello,M.J., Yingling,J.,
            Wynshaw-Boris,A. and Hirotsune,S.
  TITLE     A LIS1/NUDEL/cytoplasmic dynein heavy chain complex in the
            developing and adult nervous system
  JOURNAL   Neuron 28 (3), 681-696 (2000)
   PUBMED   11163259
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL603662.11 and AK146029.1.
            
            On May 17, 2018 this sequence version replaced XP_006534603.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK146029.1, SRR7652917.554496.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134, SAMN01164135
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 42.09 cM"
     Protein         1..328
                     /product="nuclear distribution protein nudE-like 1 isoform
                     2"
                     /note="nuclear distribution protein nudE-like 1; protein
                     Nudel; nuclear disribution gene E like; nuclear
                     distribution gene E-like homolog 1"
                     /calculated_mol_wt=36899
     Region          <27..>195
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          56..166
                     /region_name="Self-association"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Region          64..189
                     /region_name="Interaction with KATNB1.
                     /evidence=ECO:0000269|PubMed:16203747"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Region          114..133
                     /region_name="Required for interaction with PAFAH1B1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Region          135..309
                     /region_name="NUDE_C"
                     /note="NUDE protein, C-terminal conserved region;
                     pfam04880"
                     /db_xref="CDD:461464"
     Region          189..256
                     /region_name="Interaction with YWHAE.
                     /evidence=ECO:0000269|PubMed:12796778"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Region          195..256
                     /region_name="Interaction with KATNA1.
                     /evidence=ECO:0000269|PubMed:16203747"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Region          217..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9GZM8; propagated from
                     UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Region          241..280
                     /region_name="Interaction with DISC1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q9GZM8; propagated from
                     UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1 and MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q9GZM8; propagated from
                     UniProtKB/Swiss-Prot (Q9ERR1.2)"
     Region          256..291
                     /region_name="Required for localization to the centrosome
                     and interaction with dynein, dynactin, tubulin gamma, PCM1
                     and PCNT. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERR1.2)"
     CDS             1..328
                     /gene="Ndel1"
                     /gene_synonym="2600006O07Rik; MITAP1; mNudE-L; mNudel;
                     NUDEL"
                     /coded_by="NM_001363304.1:207..1193"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:83431"
                     /db_xref="MGI:MGI:1932915"
ORIGIN      
        1 mdgedipdfs slkeetaywk elslkykqsf qeardelvef qegsreleae leaqlvqaeq
       61 rnrdlqadnq rlkyevealk eklehqyaqs ykqvsvledd lsqtraikeq lhkyvreleq
      121 anddlerakr ativsledfe qrlnqaiern afleseldek esllvsvqrl kdeardlrqe
      181 lavrerqqev trksapsspt ldcekmdsav qaslslpatp vgkgtensfp spkaipngfg
      241 tspltpsari salnivgdll rkvgaleskl aacrnfakdq asrksyvpgs vncgvmnsng
      301 pecprsgrat ffhkgqekvi fptlfmgq
//
LOCUS       NP_001316544              98 aa            linear   PRI 27-APR-2025
DEFINITION  snRNA-activating protein complex subunit 5 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001316544
VERSION     NP_001316544.1
DBSOURCE    REFSEQ: accession NM_001329615.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Gao,Y.F., Mao,X.Y., Zhu,T., Mao,C.X., Liu,Z.X., Wang,Z.B., Li,L.,
            Li,X., Yin,J.Y., Zhang,W., Zhou,H.H. and Liu,Z.Q.
  TITLE     COL3A1 and SNAP91: novel glioblastoma markers with diagnostic and
            prognostic value
  JOURNAL   Oncotarget 7 (43), 70494-70503 (2016)
   PUBMED   27655637
  REMARK    GeneRIF: Kaplan-Meir analysis of GSE7696 indicate that COL3A1 and
            SNAP91 correlated with survival.
REFERENCE   4  (residues 1 to 98)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   5  (residues 1 to 98)
  AUTHORS   Ma,B. and Hernandez,N.
  TITLE     A map of protein-protein contacts within the small nuclear
            RNA-activating protein complex SNAPc
  JOURNAL   J Biol Chem 276 (7), 5027-5035 (2001)
   PUBMED   11056176
REFERENCE   6  (residues 1 to 98)
  AUTHORS   Henry,R.W., Mittal,V., Ma,B., Kobayashi,R. and Hernandez,N.
  TITLE     SNAP19 mediates the assembly of a functional core promoter complex
            (SNAPc) shared by RNA polymerases II and III
  JOURNAL   Genes Dev 12 (17), 2664-2672 (1998)
   PUBMED   9732265
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG764762.1, AC116913.6 and
            AK024763.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a subunit of the small nuclear RNA
            (snRNA)-activating protein complex that plays a role in the
            transcription of snRNA genes. This complex binds to the promoters
            of snRNA genes transcribed by either RNA polymerase II or III and
            recruits other regulatory factors to activate snRNA gene
            transcription. The encoded protein may play a role in stabilizing
            this complex. A pseudogene of this gene has been identified on
            chromosome 6. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (4) differs in the 3' UTR compared
            to variant 1. Both variants 1 and 4 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV715338.1, SRR1660807.340971.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316634.6/ ENSP00000319597.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..98
                     /product="snRNA-activating protein complex subunit 5
                     isoform 1"
                     /note="snRNA-activating protein complex subunit 5; SNAPc
                     subunit 5; SNAPc 19 kDa subunit; snRNA-activating protein
                     complex 19 kDa subunit"
                     /calculated_mol_wt=11197
     Region          1..83
                     /region_name="SNAPC5"
                     /note="snRNA-activating protein complex subunit 19, SNAPc
                     subunit 19; pfam15497"
                     /db_xref="CDD:464748"
     Region          73..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75971.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75971.1)"
     CDS             1..98
                     /gene="SNAPC5"
                     /gene_synonym="SNAP19"
                     /coded_by="NM_001329615.2:32..328"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS10217.1"
                     /db_xref="GeneID:10302"
                     /db_xref="HGNC:HGNC:15484"
                     /db_xref="MIM:605979"
ORIGIN      
        1 mlsrlqelrk eeetllrlka alhdqlnrlk veelalqsmi ssrrgdemls shtvpeqshd
       61 mlvhvdneas inqttlelst kshvteeeee eeeeesds
//
LOCUS       NP_001350529             205 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 179B isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001350529
VERSION     NP_001350529.1
DBSOURCE    REFSEQ: accession NM_001363600.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Gonzalez,P., Epstein,D.L. and Borras,T.
  TITLE     Characterization of gene expression in human trabecular meshwork
            using single-pass sequencing of 1060 clones
  JOURNAL   Invest Ophthalmol Vis Sci 41 (12), 3678-3693 (2000)
   PUBMED   11053263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001160.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.19153.1,
                                           SRR1163658.418013.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..205
                     /product="transmembrane protein 179B isoform 3 precursor"
                     /calculated_mol_wt=19429
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2623
     CDS             1..205
                     /gene="TMEM179B"
                     /coded_by="NM_001363600.1:31..648"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:374395"
                     /db_xref="HGNC:HGNC:33744"
ORIGIN      
        1 malswlqrve lalfaaaflc gavaaaamtr tqgsfsgrcp lygvatlngs slalsrpsap
       61 slcyfvagas gllalyclll llfwiyssci edshrgaigl rialaisaia vflvlvsaci
      121 lrfgtscsea qkipwtppgt alqfysnlhn aetsswvnlv lwcvvlvlqv vqwkseatpy
      181 rplergdpew ssetdalvgs rlshs
//
LOCUS       NP_001035523              86 aa            linear   PRI 27-APR-2025
DEFINITION  serine protease inhibitor Kazal-type 9 precursor [Homo sapiens].
ACCESSION   NP_001035523 XP_931821 XP_945179
VERSION     NP_001035523.1
DBSOURCE    REFSEQ: accession NM_001040433.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Sperrhacke,M., Fischer,J., Wu,Z., Klunder,S., Sedlacek,R.,
            Schroeder,J.M., Meyer-Hoffert,U. and Reiss,K.
  TITLE     SPINK9 stimulates metalloprotease/EGFR-dependent keratinocyte
            migration via purinergic receptor activation
  JOURNAL   J Invest Dermatol 134 (6), 1645-1654 (2014)
   PUBMED   24441102
  REMARK    GeneRIF: SPINK9 has a role in stimulating
            metalloprotease/EGFR-dependent keratinocyte migration by purinergic
            receptor pathway activation
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Brannstrom,K., Ohman,A., von Pawel Rammingen,U., Olofsson,A. and
            Brattsand,M.
  TITLE     Characterization of SPINK9, a KLK5-specific inhibitor expressed in
            palmo-plantar epidermis
  JOURNAL   Biol Chem 393 (5), 369-377 (2012)
   PUBMED   22505519
  REMARK    GeneRIF: the inhibition and binding of different SPINK9 variants
            towards KLK5, KLK7, KLK8 and KLK14
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Reiss,K., Meyer-Hoffert,U., Fischer,J., Sperrhacke,M., Wu,Z.,
            Dimitrieva,O., Krenek,P., Suchanova,S., Buryova,H., Brauer,R. and
            Sedlacek,R.
  TITLE     Expression and regulation of murine SPINK12, a potential orthologue
            of human LEKTI2
  JOURNAL   Exp Dermatol 20 (11), 905-910 (2011)
   PUBMED   21899598
  REMARK    GeneRIF: mSPINK12 shows an inhibitory activity against murine
            keratinocyte-derived trypsin-like proteolytic activity, and thus,
            appears orthologous to human LEKTI2 and may play an role in the
            regulation of epithelial cell functions.
REFERENCE   5  (residues 1 to 86)
  AUTHORS   Brattsand,M., Stefansson,K., Hubiche,T., Nilsson,S.K. and
            Egelrud,T.
  TITLE     SPINK9: a selective, skin-specific Kazal-type serine protease
            inhibitor
  JOURNAL   J Invest Dermatol 129 (7), 1656-1665 (2009)
   PUBMED   19194479
  REMARK    GeneRIF: possible role for SPINK9 in the site-specific epidermal
            differentiation of palms and soles
REFERENCE   6  (residues 1 to 86)
  AUTHORS   Meyer-Hoffert,U., Wu,Z. and Schroder,J.M.
  TITLE     Identification of lympho-epithelial Kazal-type inhibitor 2 in human
            skin as a kallikrein-related peptidase 5-specific protease
            inhibitor
  JOURNAL   PLoS One 4 (2), e4372 (2009)
   PUBMED   19190773
  REMARK    GeneRIF: A new KLK5-inhibiting peptide encoded by a member of the
            Spink family, designated as Spink9 located on chromosome 5p33.1,
            was identified.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY396740.1 and AC091948.3.
            
            On or before May 5, 2006 this sequence version replaced
            XP_931821.1, XP_945179.1.
            
            Summary: The protein encoded by this gene is a Kazal-type serine
            protease inhibitor that appears to specifically target
            kallikrein-related peptidase 5 (KLK5) in the palmo-plantar
            epidermis. KLK5 is an important initiator of skin desquamation, so
            the encoded protease inhibitor may regulate skin differentiation in
            the palms of hands and soles of feet. This cationic protein has
            also been shown to promote keratinocyte migration by activation of
            the epidermal growth factor receptor (EGFR). [provided by RefSeq,
            Dec 2015].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY396740.1, BC137530.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465418 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377906.2/ ENSP00000367139.1
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..86
                     /product="serine protease inhibitor Kazal-type 9
                     precursor"
                     /note="serine protease inhibitor Kazal-type 9;
                     lymphoepithelial Kazal-type-related inhibitor 2"
                     /calculated_mol_wt=7737
     sig_peptide     1..19
                     /note="/evidence=ECO:0000269|PubMed:19194479; propagated
                     from UniProtKB/Swiss-Prot (Q5DT21.1)"
                     /calculated_mol_wt=2037
     mat_peptide     20..86
                     /product="Serine protease inhibitor Kazal-type 9.
                     /id=PRO_0000333808"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5DT21.1)"
                     /calculated_mol_wt=7737
     Region          32..86
                     /region_name="Kazal_1"
                     /note="Kazal-type serine protease inhibitor domain;
                     pfam00050"
                     /db_xref="CDD:395004"
     Site            48..49
                     /site_type="other"
                     /note="Reactive bond.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00798; propagated
                     from UniProtKB/Swiss-Prot (Q5DT21.1)"
     CDS             1..86
                     /gene="SPINK9"
                     /gene_synonym="LEKTI2"
                     /coded_by="NM_001040433.2:56..316"
                     /db_xref="CCDS:CCDS34269.1"
                     /db_xref="GeneID:643394"
                     /db_xref="HGNC:HGNC:32951"
                     /db_xref="MIM:613511"
ORIGIN      
        1 mrataivlll altlatmfsi ecakqtkqmv dcshykklpp gqqrfchhmy dpicgsdgkt
       61 ykndcffcsk vkktdgtlkf vhfgkc
//
LOCUS       NP_001353197             122 aa            linear   PRI 27-APR-2025
DEFINITION  protein archease isoform 11 [Homo sapiens].
ACCESSION   NP_001353197
VERSION     NP_001353197.1
DBSOURCE    REFSEQ: accession NM_001366268.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Mason,C.C., Khorashad,J.S., Tantravahi,S.K., Kelley,T.W.,
            Zabriskie,M.S., Yan,D., Pomicter,A.D., Reynolds,K.R., Eiring,A.M.,
            Kronenberg,Z., Sherman,R.L., Tyner,J.W., Dalley,B.K., Dao,K.H.,
            Yandell,M., Druker,B.J., Gotlib,J., O'Hare,T. and Deininger,M.W.
  TITLE     Age-related mutations and chronic myelomonocytic leukemia
  JOURNAL   Leukemia 30 (4), 906-913 (2016)
   PUBMED   26648538
  REMARK    GeneRIF: ARCH mutation is associated with chronic myelomonocytic
            leukemia.
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Jurkin,J., Henkel,T., Nielsen,A.F., Minnich,M., Popow,J.,
            Kaufmann,T., Heindl,K., Hoffmann,T., Busslinger,M. and Martinez,J.
  TITLE     The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA
            and controls antibody secretion in plasma cells
  JOURNAL   EMBO J 33 (24), 2922-2936 (2014)
   PUBMED   25378478
  REMARK    GeneRIF: RTCB, the catalytic subunit of the tRNA ligase complex,
            and its co-factor archease mediate XBP1 mRNA splicing both in vitro
            and in vivo.
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Popow,J., Jurkin,J., Schleiffer,A. and Martinez,J.
  TITLE     Analysis of orthologous groups reveals archease and DDX1 as tRNA
            splicing factors
  JOURNAL   Nature 511 (7507), 104-107 (2014)
   PUBMED   24870230
  REMARK    GeneRIF: archease (also called ZBTB8OS), a protein of unknown
            function, is required for full activity of the human tRNA ligase
            complex and, in cooperation with DDX1, facilitates the formation of
            an RTCB-guanylate intermediate central to mammalian RNA ligation
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Popow,J., Englert,M., Weitzer,S., Schleiffer,A., Mierzwa,B.,
            Mechtler,K., Trowitzsch,S., Will,C.L., Luhrmann,R., Soll,D. and
            Martinez,J.
  TITLE     HSPC117 is the essential subunit of a human tRNA splicing ligase
            complex
  JOURNAL   Science 331 (6018), 760-764 (2011)
   PUBMED   21311021
REFERENCE   7  (residues 1 to 122)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 122)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2 and AL033529.25.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.297953.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..122
                     /product="protein archease isoform 11"
                     /note="protein archease; archease-like protein; archease
                     (ARCH); zinc finger and BTB domain-containing opposite
                     strand protein 8"
                     /calculated_mol_wt=13941
     Region          1..122
                     /region_name="Archease"
                     /note="Archease protein family (MTH1598/TM1083);
                     pfam01951"
                     /db_xref="CDD:426527"
     CDS             1..122
                     /gene="ZBTB8OS"
                     /gene_synonym="ARCH; ARCH2"
                     /coded_by="NM_001366268.1:613..981"
                     /note="isoform 11 is encoded by transcript variant 21"
                     /db_xref="GeneID:339487"
                     /db_xref="HGNC:HGNC:24094"
                     /db_xref="MIM:615891"
ORIGIN      
        1 mamfgymtdt gtveplqtve vetqgddlqs llfhfldewl ykfsadeffi prmrspyvaq
       61 avlkllgssd ppfglrkcqd yrwgeefsls khpqgtevka itysamqvyn eenpevfvii
      121 di
//
LOCUS       NP_001355297             127 aa            linear   PRI 27-APR-2025
DEFINITION  IQ domain-containing protein F6 isoform 2 [Homo sapiens].
ACCESSION   NP_001355297 XP_005265225
VERSION     NP_001355297.1
DBSOURCE    REFSEQ: accession NM_001368368.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099050.2.
            
            On Feb 9, 2019 this sequence version replaced XP_005265225.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2) is
            shorter at the N-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..127
                     /product="IQ domain-containing protein F6 isoform 2"
                     /note="IQ domain-containing protein F6"
                     /calculated_mol_wt=15330
     CDS             1..127
                     /gene="IQCF6"
                     /coded_by="NM_001368368.1:14..397"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93281.1"
                     /db_xref="GeneID:440956"
                     /db_xref="HGNC:HGNC:35158"
ORIGIN      
        1 mdtqnlekta ikiqswwrgn mvrrtllqaa lrawviqcww rsmqakmleq rrrlalrlyt
       61 cqewavvkvq aqvrmwqarr rflqarqaac iiqshwrwha sqtrglirgh yevrasrlel
      121 dieilmt
//
LOCUS       NP_001349822             690 aa            linear   ROD 27-APR-2025
DEFINITION  unconventional myosin-XIX isoform 2 [Mus musculus].
ACCESSION   NP_001349822 XP_006533992
VERSION     NP_001349822.1
DBSOURCE    REFSEQ: accession NM_001362893.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Jiao,H., Jiang,D., Hu,X., Du,W., Ji,L., Yang,Y., Li,X., Sho,T.,
            Wang,X., Li,Y., Wu,Y.T., Wei,Y.H., Hu,X. and Yu,L.
  TITLE     Mitocytosis, a migrasome-mediated mitochondrial quality-control
            process
  JOURNAL   Cell 184 (11), 2896-2910 (2021)
   PUBMED   34048705
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Jones,M.R., Dilai,S., Lingampally,A., Chao,C.M., Danopoulos,S.,
            Carraro,G., Mukhametshina,R., Wilhelm,J., Baumgart-Vogt,E., Al
            Alam,D., Chen,C., Minoo,P., Zhang,J.S. and Bellusci,S.
  TITLE     A Comprehensive Analysis of Fibroblast Growth Factor Receptor 2b
            Signaling on Epithelial Tip Progenitor Cells During Early Mouse
            Lung Branching Morphogenesis
  JOURNAL   Front Genet 9, 746 (2019)
   PUBMED   30728831
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Lu,Z., Ma,X.N., Zhang,H.M., Ji,H.H., Ding,H., Zhang,J., Luo,D.,
            Sun,Y. and Li,X.D.
  TITLE     Mouse myosin-19 is a plus-end-directed, high-duty ratio molecular
            motor
  JOURNAL   J Biol Chem 289 (26), 18535-18548 (2014)
   PUBMED   24825904
  REMARK    GeneRIF: Myo19 is a high-duty ratio molecular motor moving to the
            plus-end of the actin filament.
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL645623.13 and AK080117.1.
            
            On May 3, 2018 this sequence version replaced XP_006533992.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK080117.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 51.34 cM"
     Protein         1..690
                     /product="unconventional myosin-XIX isoform 2"
                     /note="myosin head domain containing 1; myosin head
                     domain-containing protein 1; unconventional myosin-XIX"
                     /calculated_mol_wt=77228
     Region          <18..473
                     /region_name="Motor_domain"
                     /note="Myosin and Kinesin motor domain; cl22853"
                     /db_xref="CDD:473979"
     Region          503..>528
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     CDS             1..690
                     /gene="Myo19"
                     /gene_synonym="1110055A02Rik; Myohd1"
                     /coded_by="NM_001362893.1:1145..3217"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:66196"
                     /db_xref="MGI:MGI:1913446"
ORIGIN      
        1 mkgsngtslr elpspgypiq kavwkvlagl lhlgnvhfvd sedealpcqv mddtkvsvrt
       61 salllqlpek mllesmqirt ikagkqqqvf qkpcsraecd trrdclakli yarlfdwlvs
      121 vinssicads kswtafigll dvygfesfpn nsleqlciny aneklqqhfv ahylraqqee
      181 yeveglewsf vnyqdnqtcl dllegspisi cslineecrl nrpssaaqlq triestlagr
      241 pclghnklsr epsfvvvhfa gpvryhtagl veknkdpvpp eltellqqsq dplltmlfpa
      301 npeektqeel sgqsrapalt vvskfkasle qllqvlhntt phyircikpn sqsqpqtflq
      361 eevlnqleac glvetihisa agfpirvshq nfierykllr rlgprmssgl gglepaegss
      421 eqplcakeat lqpllqdilh alpaliqtaa tpsdpakntq iplycgrtki fmtdsmlell
      481 ecgraqmleq carciqcgwr rhrlqkqekq rraavliqaa frswltrkhi rrlhiaatvi
      541 khawhkwrir maclaskeld gmeekpmpqa pgtlrssmsp ahtrflgaii hlwplglvla
      601 nsadgvrgfq rklvahaclr lpsdrpsnkv qtpqqdqagi tsiralpqgs ikfhcrkspl
      661 qyadicpdps ascvtgfnqi lleshrpvqv
//
LOCUS       NP_861460                 78 aa            linear   PRI 27-APR-2025
DEFINITION  cAMP-dependent protein kinase inhibitor beta isoform 1 [Homo
            sapiens].
ACCESSION   NP_861460
VERSION     NP_861460.1
DBSOURCE    REFSEQ: accession NM_181795.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Liu,C., Wang,H., Yang,M., Liang,Y., Jiang,L., Sun,S. and Fan,S.
  TITLE     Downregulation of cAMP-Dependent Protein Kinase Inhibitor-b
            Promotes Preeclampsia by Decreasing Phosphorylated Akt
  JOURNAL   Reprod Sci 28 (1), 178-185 (2021)
   PUBMED   32676926
  REMARK    GeneRIF: Downregulation of cAMP-Dependent Protein Kinase
            Inhibitor-b Promotes Preeclampsia by Decreasing Phosphorylated Akt.
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Dou,P., Zhang,D., Cheng,Z., Zhou,G. and Zhang,L.
  TITLE     PKIB promotes cell proliferation and the invasion-metastasis
            cascade through the PI3K/Akt pathway in NSCLC cells
  JOURNAL   Exp Biol Med (Maywood) 241 (17), 1911-1918 (2016)
   PUBMED   27325557
  REMARK    GeneRIF: results indicate that PKIB promotes cell proliferation and
            tumorigenesis by activating the PI3K/Akt pathway in non-small cell
            lung cancer (NSCLC), implying that this is an important underlying
            mechanism that affects the progression of NSCLC
REFERENCE   4  (residues 1 to 78)
  AUTHORS   Kovacs,Z., Schacht,T., Herrmann,A.K., Albrecht,P., Lefkimmiatis,K.
            and Methner,A.
  TITLE     Protein kinase inhibitor beta enhances the constitutive activity of
            G-protein-coupled zinc receptor GPR39
  JOURNAL   Biochem J 462 (1), 125-132 (2014)
   PUBMED   24869658
  REMARK    GeneRIF: mutation of the pseudosubstrate domain abolished the
            inhibitory activity of PKIB on protein kinase A activity, but had
            no effect on the interaction with GPR39, cell protection and
            induction of SRE-dependent transcription
REFERENCE   5  (residues 1 to 78)
  AUTHORS   Chung,S., Furihata,M., Tamura,K., Uemura,M., Daigo,Y., Nasu,Y.,
            Miki,T., Shuin,T., Fujioka,T., Nakamura,Y. and Nakagawa,H.
  TITLE     Overexpressing PKIB in prostate cancer promotes its aggressiveness
            by linking between PKA and Akt pathways
  JOURNAL   Oncogene 28 (32), 2849-2859 (2009)
   PUBMED   19483721
  REMARK    GeneRIF: Findings show that PKIB and PKA-C kinase can have critical
            functions of aggressive phenotype of PCs through Akt
            phosphorylation and that they should be a promising molecular
            target for PC treatment.
REFERENCE   6  (residues 1 to 78)
  AUTHORS   Qi,Z.Y., Hui,G.Z., Li,Y., Gu,S.H. and Xie,Y.
  TITLE     [Expression and characterizations of a novel full-length gene
            PKIbeta related to human glioma]
  JOURNAL   Zhonghua Yi Xue Za Zhi 88 (25), 1778-1782 (2008)
   PUBMED   19035091
  REMARK    GeneRIF: PKIbeta may be a novel full-length gene related to human
            glioma and may provide a new way to gene therapy of glioma.
REFERENCE   7  (residues 1 to 78)
  AUTHORS   Yu,J., Yu,L., Chen,Z., Zheng,L., Chen,X., Wang,X., Ren,D. and
            Zhao,S.
  TITLE     Protein inhibitor of neuronal nitric oxide synthase interacts with
            protein kinase A inhibitors
  JOURNAL   Brain Res Mol Brain Res 99 (2), 145-149 (2002)
   PUBMED   11978406
REFERENCE   8  (residues 1 to 78)
  AUTHORS   Zheng,L., Yu,L., Tu,Q., Zhang,M., He,H., Chen,W., Gao,J., Yu,J.,
            Wu,Q. and Zhao,S.
  TITLE     Cloning and mapping of human PKIB and PKIG, and comparison of
            tissue expression patterns of three members of the protein kinase
            inhibitor family, including PKIA
  JOURNAL   Biochem J 349 (Pt 2), 403-407 (2000)
   PUBMED   10880337
REFERENCE   9  (residues 1 to 78)
  AUTHORS   Scarpetta,M.A. and Uhler,M.D.
  TITLE     Evidence for two additional isoforms of the endogenous protein
            kinase inhibitor of cAMP-dependent protein kinase in mouse
  JOURNAL   J Biol Chem 268 (15), 10927-10931 (1993)
   PUBMED   7684369
  REMARK    GeneRIF: Functional studies of the mouse homolog
REFERENCE   10 (residues 1 to 78)
  AUTHORS   Van Patten,S.M., Ng,D.C., Th'ng,J.P., Angelos,K.L., Smith,A.J. and
            Walsh,D.A.
  TITLE     Molecular cloning of a rat testis form of the inhibitor protein of
            cAMP-dependent protein kinase
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5383-5387 (1991)
   PUBMED   2052616
  REMARK    GeneRIF: Functional studies of the rat homolog
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP260889.1, AK315151.1,
            AL512283.12 and BU753807.1.
            
            Summary: This gene encodes a member of the cAMP-dependent protein
            kinase inhibitor family. The encoded protein may play a role in the
            protein kinase A (PKA) pathway by interacting with the catalytic
            subunit of PKA, and overexpression of this gene may play a role in
            prostate cancer. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) encodes the shorter isoform
            (1). Variants 1, 2, 3 and 4 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.356684.1,
                                           SRR3476690.779839.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368452.7/ ENSP00000357437.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31"
     Protein         1..78
                     /product="cAMP-dependent protein kinase inhibitor beta
                     isoform 1"
                     /note="cAMP-dependent protein kinase inhibitor 2;
                     PKI-beta; protein kinase (cAMP-dependent, catalytic)
                     inhibitor beta"
                     /calculated_mol_wt=8337
     Region          1..78
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C010.1)"
     Region          9..77
                     /region_name="PKI"
                     /note="cAMP-dependent protein kinase inhibitor; pfam02827"
                     /db_xref="CDD:460716"
     Site            23
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9C010.1)"
     Site            26
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9C010.1)"
     Site            27
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9C010.1)"
     CDS             1..78
                     /gene="PKIB"
                     /gene_synonym="PRKACN2"
                     /coded_by="NM_181795.3:292..528"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5126.1"
                     /db_xref="GeneID:5570"
                     /db_xref="HGNC:HGNC:9018"
                     /db_xref="MIM:606914"
ORIGIN      
        1 mrtdsskmtd vesgvanfas saragrrnal pdiqssaatd gtsdlplkle alsvkedake
       61 kdekttqdql ekpqneek
//
LOCUS       NP_001349198             300 aa            linear   ROD 27-APR-2025
DEFINITION  retinol dehydrogenase 11 isoform 2 [Mus musculus].
ACCESSION   NP_001349198
VERSION     NP_001349198.1
DBSOURCE    REFSEQ: accession NM_001362269.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Zhang,D., Deng,W., Jiang,T., Zhao,Y., Bai,D., Tian,Y., Kong,S.,
            Zhang,L., Wang,H., Gao,S. and Lu,Z.
  TITLE     Maternal Ezh1/2 deficiency impairs the function of mitochondria in
            mouse oocytes and early embryos
  JOURNAL   J Cell Physiol 239 (6), e31244 (2024)
   PUBMED   38529784
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Wu,L., Belyaeva,O.V., Adams,M.K., Klyuyeva,A.V., Lee,S.A.,
            Goggans,K.R., Kesterson,R.A., Popov,K.M. and Kedishvili,N.Y.
  TITLE     Mice lacking the epidermal retinol dehydrogenases SDR16C5 and
            SDR16C6 display accelerated hair growth and enlarged meibomian
            glands
  JOURNAL   J Biol Chem 294 (45), 17060-17074 (2019)
   PUBMED   31562240
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Belyaeva,O.V., Wu,L., Shmarakov,I., Nelson,P.S. and Kedishvili,N.Y.
  TITLE     Retinol dehydrogenase 11 is essential for the maintenance of
            retinol homeostasis in liver and testis in mice
  JOURNAL   J Biol Chem 293 (18), 6996-7007 (2018)
   PUBMED   29567832
  REMARK    GeneRIF: results indicate that in mouse testis and liver, RDH11
            functions as an all-trans-retinaldehyde reductase essential for the
            maintenance of physiological levels of all-trans-retinol under
            reduced vitamin A availability
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Adams,M.K., Belyaeva,O.V., Wu,L. and Kedishvili,N.Y.
  TITLE     The retinaldehyde reductase activity of DHRS3 is reciprocally
            activated by retinol dehydrogenase 10 to control retinoid
            homeostasis
  JOURNAL   J Biol Chem 289 (21), 14868-14880 (2014)
   PUBMED   24733397
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Parker,R.O. and Crouch,R.K.
  TITLE     Retinol dehydrogenases (RDHs) in the visual cycle
  JOURNAL   Exp Eye Res 91 (6), 788-792 (2010)
   PUBMED   20801113
  REMARK    Review article
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Maeda,A., Maeda,T., Imanishi,Y., Golczak,M., Moise,A.R. and
            Palczewski,K.
  TITLE     Aberrant metabolites in mouse models of congenital blinding
            diseases: formation and storage of retinyl esters
  JOURNAL   Biochemistry 45 (13), 4210-4219 (2006)
   PUBMED   16566595
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Kasus-Jacobi,A., Ou,J., Birch,D.G., Locke,K.G., Shelton,J.M.,
            Richardson,J.A., Murphy,A.J., Valenzuela,D.M., Yancopoulos,G.D. and
            Edwards,A.O.
  TITLE     Functional characterization of mouse RDH11 as a retinol
            dehydrogenase involved in dark adaptation in vivo
  JOURNAL   J Biol Chem 280 (21), 20413-20420 (2005)
   PUBMED   15790565
  REMARK    GeneRIF: propose that mouse retinol dehydrogenase 11(mRDH11)
            disruption affects retinoid metabolism in photoreceptor inner
            segments and delays the kinetics of dark adaptation through
            modulation of calcium homeostasis
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Kim,T.S., Maeda,A., Maeda,T., Heinlein,C., Kedishvili,N.,
            Palczewski,K. and Nelson,P.S.
  TITLE     Delayed dark adaptation in 11-cis-retinol dehydrogenase-deficient
            mice: a role of RDH11 in visual processes in vivo
  JOURNAL   J Biol Chem 280 (10), 8694-8704 (2005)
   PUBMED   15634683
  REMARK    GeneRIF: RDH11 has a measurable role in regenerating the visual
            pigment by complementing RDH5 in retinal pigment epithelium.
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Kasus-Jacobi,A., Ou,J., Bashmakov,Y.K., Shelton,J.M.,
            Richardson,J.A., Goldstein,J.L. and Brown,M.S.
  TITLE     Characterization of mouse short-chain aldehyde reductase (SCALD),
            an enzyme regulated by sterol regulatory element-binding proteins
  JOURNAL   J Biol Chem 278 (34), 32380-32389 (2003)
   PUBMED   12807874
  REMARK    GeneRIF: characterization of catalytic properties and tissue
            distribution
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Moore,S., Pritchard,C., Lin,B., Ferguson,C. and Nelson,P.S.
  TITLE     Isolation and characterization of the murine prostate short-chain
            dehydrogenase/reductase 1 (Psdr1) gene, a new member of the
            short-chain steroid dehydrogenase/reductase family
  JOURNAL   Gene 293 (1-2), 149-160 (2002)
   PUBMED   12137953
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC154585.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB030504.1, SRR1660813.227668.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 35.51 cM"
     Protein         1..300
                     /product="retinol dehydrogenase 11 isoform 2"
                     /EC_number="1.1.1.300"
                     /note="androgen-regulated short-chain
                     dehydrogenase/reductase 1; short-chain aldehyde
                     dehydrogenase; retinal reductase 1; cell line
                     MC/9.IL4-derived protein 1; prostate short-chain
                     dehydrogenase/reductase 1; cell line MC/9.IL4 derived
                     transcript 1; all-trans and 9-cis"
                     /calculated_mol_wt=33109
     Region          22..290
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(29,31..32,34,53..55,108..110,162..164,183,187,
                     213..216)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:212495"
     Site            order(130,164,183,187)
                     /site_type="active"
                     /db_xref="CDD:212495"
     CDS             1..300
                     /gene="Rdh11"
                     /gene_synonym="2610319N22Rik; Arsdr1; CGI-82; HCBP12;
                     M42C60; Mdt1; Psdr1; ralR1; SCALD; Ube-1c; UBE-1c1"
                     /coded_by="NM_001362269.1:177..1079"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS88359.1"
                     /db_xref="GeneID:17252"
                     /db_xref="MGI:MGI:102581"
ORIGIN      
        1 mglvlrkmls sgvctsnvql pgkvaivtga ntgigketak dlaqrgarvy lacrdvdkge
       61 laareiqavt gnsqvfvrkl dladtksira fakdflaeek hlhllinnag vmmcpyskta
      121 dgfemhigvn hlghfllthl lleklkesap srivnlsslg hhlgrihfhn lqgekfysag
      181 laychsklan ilftkelakr lkgsgvttys vhpgtvhsel tryssimrwl wqlffvfikt
      241 pqegaqtsly calteglesl sgshfsdcql awvsyqgrne iiarrlwdvs cdllglpvdw
//
LOCUS       NP_776195                236 aa            linear   PRI 27-APR-2025
DEFINITION  protein YIPF6 isoform A [Homo sapiens].
ACCESSION   NP_776195
VERSION     NP_776195.2
DBSOURCE    REFSEQ: accession NM_173834.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Wang,L., Mazagova,M., Pan,C., Yang,S., Brandl,K., Liu,J.,
            Reilly,S.M., Wang,Y., Miao,Z., Loomba,R., Lu,N., Guo,Q., Liu,J.,
            Yu,R.T., Downes,M., Evans,R.M., Brenner,D.A., Saltiel,A.R.,
            Beutler,B. and Schnabl,B.
  TITLE     YIPF6 controls sorting of FGF21 into COPII vesicles and promotes
            obesity
  JOURNAL   Proc Natl Acad Sci U S A 116 (30), 15184-15193 (2019)
   PUBMED   31289229
  REMARK    GeneRIF: Levels of YIPF6 protein in human liver correlate with
            hepatic steatosis and correlate inversely with levels of FGF21 in
            serum from patients with nonalcoholic fatty liver disease.
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Djusberg,E., Jernberg,E., Thysell,E., Golovleva,I., Lundberg,P.,
            Crnalic,S., Widmark,A., Bergh,A., Brattsand,M. and Wikstrom,P.
  TITLE     High levels of the AR-V7 Splice Variant and Co-Amplification of the
            Golgi Protein Coding YIPF6 in AR Amplified Prostate Cancer Bone
            Metastases
  JOURNAL   Prostate 77 (6), 625-638 (2017)
   PUBMED   28144969
  REMARK    GeneRIF: YIPF6 overexpression in prostate cancer tumor cell lines
            resulted in reduced cell proliferation and colony formation.
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Soonthornsit,J., Sakai,N., Sasaki,Y., Watanabe,R., Osako,S. and
            Nakamura,N.
  TITLE     YIPF1, YIPF2, and YIPF6 are medial-/trans-Golgi and trans-Golgi
            network-localized Yip domain family proteins, which play a role in
            the Golgi reassembly and glycan synthesis
  JOURNAL   Exp Cell Res 353 (2), 100-108 (2017)
   PUBMED   28286305
  REMARK    GeneRIF: Knockdown of YIPF1 and YIPF2, but not that of YIPF6, also
            reduced intracellular glycans in HT-29 cells. Thus, we confirmed
            that YIPF1, YIPF2, and YIPF6 play a significant role in supporting
            normal glycan synthesis
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Ross,M.T., Grafham,D.V., Coffey,A.J., Scherer,S., McLay,K.,
            Muzny,D., Platzer,M., Howell,G.R., Burrows,C., Bird,C.P.,
            Frankish,A., Lovell,F.L., Howe,K.L., Ashurst,J.L., Fulton,R.S.,
            Sudbrak,R., Wen,G., Jones,M.C., Hurles,M.E., Andrews,T.D.,
            Scott,C.E., Searle,S., Ramser,J., Whittaker,A., Deadman,R.,
            Carter,N.P., Hunt,S.E., Chen,R., Cree,A., Gunaratne,P., Havlak,P.,
            Hodgson,A., Metzker,M.L., Richards,S., Scott,G., Steffen,D.,
            Sodergren,E., Wheeler,D.A., Worley,K.C., Ainscough,R.,
            Ambrose,K.D., Ansari-Lari,M.A., Aradhya,S., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Ballabio,A., Banerjee,R., Barker,G.E.,
            Barlow,K.F., Barrett,I.P., Bates,K.N., Beare,D.M., Beasley,H.,
            Beasley,O., Beck,A., Bethel,G., Blechschmidt,K., Brady,N.,
            Bray-Allen,S., Bridgeman,A.M., Brown,A.J., Brown,M.J., Bonnin,D.,
            Bruford,E.A., Buhay,C., Burch,P., Burford,D., Burgess,J.,
            Burrill,W., Burton,J., Bye,J.M., Carder,C., Carrel,L., Chako,J.,
            Chapman,J.C., Chavez,D., Chen,E., Chen,G., Chen,Y., Chen,Z.,
            Chinault,C., Ciccodicola,A., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S., Clerc-Blankenburg,K., Clifford,K., Cobley,V., Cole,C.G.,
            Conquer,J.S., Corby,N., Connor,R.E., David,R., Davies,J., Davis,C.,
            Davis,J., Delgado,O., Deshazo,D., Dhami,P., Ding,Y., Dinh,H.,
            Dodsworth,S., Draper,H., Dugan-Rocha,S., Dunham,A., Dunn,M.,
            Durbin,K.J., Dutta,I., Eades,T., Ellwood,M., Emery-Cohen,A.,
            Errington,H., Evans,K.L., Faulkner,L., Francis,F., Frankland,J.,
            Fraser,A.E., Galgoczy,P., Gilbert,J., Gill,R., Glockner,G.,
            Gregory,S.G., Gribble,S., Griffiths,C., Grocock,R., Gu,Y.,
            Gwilliam,R., Hamilton,C., Hart,E.A., Hawes,A., Heath,P.D.,
            Heitmann,K., Hennig,S., Hernandez,J., Hinzmann,B., Ho,S., Hoffs,M.,
            Howden,P.J., Huckle,E.J., Hume,J., Hunt,P.J., Hunt,A.R.,
            Isherwood,J., Jacob,L., Johnson,D., Jones,S., de Jong,P.J.,
            Joseph,S.S., Keenan,S., Kelly,S., Kershaw,J.K., Khan,Z.,
            Kioschis,P., Klages,S., Knights,A.J., Kosiura,A., Kovar-Smith,C.,
            Laird,G.K., Langford,C., Lawlor,S., Leversha,M., Lewis,L., Liu,W.,
            Lloyd,C., Lloyd,D.M., Loulseged,H., Loveland,J.E., Lovell,J.D.,
            Lozado,R., Lu,J., Lyne,R., Ma,J., Maheshwari,M., Matthews,L.H.,
            McDowall,J., McLaren,S., McMurray,A., Meidl,P., Meitinger,T.,
            Milne,S., Miner,G., Mistry,S.L., Morgan,M., Morris,S., Muller,I.,
            Mullikin,J.C., Nguyen,N., Nordsiek,G., Nyakatura,G., O'Dell,C.N.,
            Okwuonu,G., Palmer,S., Pandian,R., Parker,D., Parrish,J.,
            Pasternak,S., Patel,D., Pearce,A.V., Pearson,D.M., Pelan,S.E.,
            Perez,L., Porter,K.M., Ramsey,Y., Reichwald,K., Rhodes,S.,
            Ridler,K.A., Schlessinger,D., Schueler,M.G., Sehra,H.K.,
            Shaw-Smith,C., Shen,H., Sheridan,E.M., Shownkeen,R., Skuce,C.D.,
            Smith,M.L., Sotheran,E.C., Steingruber,H.E., Steward,C.A.,
            Storey,R., Swann,R.M., Swarbreck,D., Tabor,P.E., Taudien,S.,
            Taylor,T., Teague,B., Thomas,K., Thorpe,A., Timms,K., Tracey,A.,
            Trevanion,S., Tromans,A.C., d'Urso,M., Verduzco,D., Villasana,D.,
            Waldron,L., Wall,M., Wang,Q., Warren,J., Warry,G.L., Wei,X.,
            West,A., Whitehead,S.L., Whiteley,M.N., Wilkinson,J.E.,
            Willey,D.L., Williams,G., Williams,L., Williamson,A.,
            Williamson,H., Wilming,L., Woodmansey,R.L., Wray,P.W., Yen,J.,
            Zhang,J., Zhou,J., Zoghbi,H., Zorilla,S., Buck,D., Reinhardt,R.,
            Poustka,A., Rosenthal,A., Lehrach,H., Meindl,A., Minx,P.J.,
            Hillier,L.W., Willard,H.F., Wilson,R.K., Waterston,R.H., Rice,C.M.,
            Vaudin,M., Coulson,A., Nelson,D.L., Weinstock,G., Sulston,J.E.,
            Durbin,R., Hubbard,T., Gibbs,R.A., Beck,S., Rogers,J. and
            Bentley,D.R.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC012469.1 and AL928603.5.
            
            On Aug 28, 2010 this sequence version replaced NP_776195.1.
            
            Transcript Variant: This variant (A) represents the longer
            transcript and encodes the longer isoform (A).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG570565.1, SRR1660803.232025.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000462683.6/ ENSP00000417573.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq12-q13.1"
     Protein         1..236
                     /product="protein YIPF6 isoform A"
                     /note="protein YIPF6; YIP1 family member 6"
                     /calculated_mol_wt=26125
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96EC8.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4QQU5; propagated from
                     UniProtKB/Swiss-Prot (Q96EC8.2)"
     Region          <54..231
                     /region_name="YIP1"
                     /note="Rab GTPase interacting factor, Golgi membrane
                     protein [Intracellular trafficking and secretion];
                     cl46908"
                     /db_xref="CDD:481248"
     Site            85..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EC8.2)"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EC8.2)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EC8.2)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EC8.2)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EC8.2)"
     CDS             1..236
                     /gene="YIPF6"
                     /gene_synonym="FinGER6; Yip4; YIPFalpha3"
                     /coded_by="NM_173834.4:17..727"
                     /note="isoform A is encoded by transcript variant A"
                     /db_xref="CCDS:CCDS14389.1"
                     /db_xref="GeneID:286451"
                     /db_xref="HGNC:HGNC:28304"
                     /db_xref="MIM:300996"
ORIGIN      
        1 maeaeespgd pgtasprplf aglsdisisq dipvegeiti pmrsrirefd sstlnesvrn
       61 timrdlkavg kkfmhvlypr ksntllrdwd lwgplilcvt lalmlqrdsa dsekdggpqf
      121 aevfvivwfg avtitlnskl lggnisffqs lcvlgycilp ltvamlicrl vlladpgpvn
      181 fmvrlfvviv mfawsivast afladsqppn rralavypvf lfyfviswmi ltftpq
//
LOCUS       NP_001108070             283 aa            linear   PRI 27-APR-2025
DEFINITION  aspartate dehydrogenase domain-containing protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_001108070
VERSION     NP_001108070.1
DBSOURCE    REFSEQ: accession NM_001114598.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   He,X., Kang,Y. and Chen,L.
  TITLE     Identification of ASPDH as a novel NAADP-binding protein
  JOURNAL   Biochem Biophys Res Commun 621, 168-175 (2022)
   PUBMED   35841763
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008743.9, BM924033.1 and BU729215.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM924033.1, DRR138522.357387.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159080 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389208.9/ ENSP00000373860.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..283
                     /product="aspartate dehydrogenase domain-containing
                     protein isoform 1"
                     /EC_number="1.4.1.21"
                     /note="putative L-aspartate dehydrogenase; aspartate
                     dehydrogenase domain-containing protein"
                     /calculated_mol_wt=29815
     Region          13..123
                     /region_name="NAD_binding_3"
                     /note="Homoserine dehydrogenase, NAD binding domain;
                     pfam03447"
                     /db_xref="CDD:281446"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (A6ND91.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (A6ND91.2)"
     Region          173..261
                     /region_name="Asp_DH_C"
                     /note="Aspartate dehydrogenase, C-terminal; pfam01958"
                     /db_xref="CDD:426531"
     CDS             1..283
                     /gene="ASPDH"
                     /coded_by="NM_001114598.2:91..942"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46153.1"
                     /db_xref="GeneID:554235"
                     /db_xref="HGNC:HGNC:33856"
ORIGIN      
        1 madrgpwrvg vvgygrlgqs lvsrllaqgp elglelvfvw nrdpgrmags vppslqlqnl
       61 aalgerrpdl vvevahpkii hesgaqilrh anllvgspsa lsdqtterql leasqhwdha
      121 vfvargalwg aedirrldaa gglrslrvtm athpdgfrle gplaaahspg pctvlyegpv
      181 rglcpfaprn sntmaaaala apslgfdgvi gvlvadtslt dmhvvdvels gprgptgrsf
      241 avhtrrenpa epgavtgsat vtafwqslla ccqlpsrpgi hlc
//
LOCUS       NP_036205                541 aa            linear   PRI 27-APR-2025
DEFINITION  T-complex protein 1 subunit epsilon isoform a [Homo sapiens].
ACCESSION   NP_036205
VERSION     NP_036205.1
DBSOURCE    REFSEQ: accession NM_012073.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Wu,S. and Peng,L.
  TITLE     Increased CCT5 expression is a potential unfavourable factor
            promoting the growth of nasopharyngeal carcinoma
  JOURNAL   J Int Med Res 52 (9), 3000605241271754 (2024)
   PUBMED   39286844
  REMARK    GeneRIF: Increased CCT5 expression is a potential unfavourable
            factor promoting the growth of nasopharyngeal carcinoma.
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Scalia,F., Lo Bosco,G., Paladino,L., Vitale,A.M., Noori,L., Conway
            de Macario,E., Macario,A.J.L., Bucchieri,F., Cappello,F. and Lo
            Celso,F.
  TITLE     Structural and Dynamic Disturbances Revealed by Molecular Dynamics
            Simulations Predict the Impact on Function of CCT5 Chaperonin
            Mutations Associated with Rare Severe Distal Neuropathies
  JOURNAL   Int J Mol Sci 24 (3), 2018 (2023)
   PUBMED   36768350
  REMARK    GeneRIF: Structural and Dynamic Disturbances Revealed by Molecular
            Dynamics Simulations Predict the Impact on Function of CCT5
            Chaperonin Mutations Associated with Rare Severe Distal
            Neuropathies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Li,Y., Liu,C., Zhang,X., Huang,X., Liang,S., Xing,F. and Tian,H.
  TITLE     CCT5 induces epithelial-mesenchymal transition to promote gastric
            cancer lymph node metastasis by activating the Wnt/beta-catenin
            signalling pathway
  JOURNAL   Br J Cancer 126 (12), 1684-1694 (2022)
   PUBMED   35194191
  REMARK    GeneRIF: CCT5 induces epithelial-mesenchymal transition to promote
            gastric cancer lymph node metastasis by activating the
            Wnt/beta-catenin signalling pathway.
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Sergeeva,O.A., Tran,M.T., Haase-Pettingell,C. and King,J.A.
  TITLE     Biochemical characterization of mutants in chaperonin proteins CCT4
            and CCT5 associated with hereditary sensory neuropathy
  JOURNAL   J Biol Chem 289 (40), 27470-27480 (2014)
   PUBMED   25124038
  REMARK    GeneRIF: H147R CCT5 was not as efficient in chaperoning these
            substrates as wild type CCT5.
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Bouhouche,A., Benomar,A., Bouslam,N., Chkili,T. and Yahyaoui,M.
  TITLE     Mutation in the epsilon subunit of the cytosolic
            chaperonin-containing t-complex peptide-1 (Cct5) gene causes
            autosomal recessive mutilating sensory neuropathy with spastic
            paraplegia
  JOURNAL   J Med Genet 43 (5), 441-443 (2006)
   PUBMED   16399879
  REMARK    GeneRIF: A missense mutation within the CCT5 gene is associated
            with autosomal recessive mutilating sensory neuropathy with spastic
            paraplegia.
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Roperch,J.P., Lethrone,F., Prieur,S., Piouffre,L., Israeli,D.,
            Tuynder,M., Nemani,M., Pasturaud,P., Gendron,M.C., Dausset,J.,
            Oren,M., Amson,R.B. and Telerman,A.
  TITLE     SIAH-1 promotes apoptosis and tumor suppression through a network
            involving the regulation of protein folding, unfolding, and
            trafficking: identification of common effectors with p53 and
            p21(Waf1)
  JOURNAL   Proc Natl Acad Sci U S A 96 (14), 8070-8073 (1999)
   PUBMED   10393949
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Liou,A.K. and Willison,K.R.
  TITLE     Elucidation of the subunit orientation in CCT (chaperonin
            containing TCP1) from the subunit composition of CCT
            micro-complexes
  JOURNAL   EMBO J 16 (14), 4311-4316 (1997)
   PUBMED   9250675
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Roobol,A., Holmes,F.E., Hayes,N.V., Baines,A.J. and Carden,M.J.
  TITLE     Cytoplasmic chaperonin complexes enter neurites developing in vitro
            and differ in subunit composition within single cells
  JOURNAL   J Cell Sci 108 (Pt 4), 1477-1488 (1995)
   PUBMED   7615668
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Kubota,H., Hynes,G., Carne,A., Ashworth,A. and Willison,K.
  TITLE     Identification of six Tcp-1-related genes encoding divergent
            subunits of the TCP-1-containing chaperonin
  JOURNAL   Curr Biol 4 (2), 89-99 (1994)
   PUBMED   7953530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FJ224303.1.
            
            Summary: The protein encoded by this gene is a molecular chaperone
            that is a member of the chaperonin containing TCP1 complex (CCT),
            also known as the TCP1 ring complex (TRiC). This complex consists
            of two identical stacked rings, each containing eight different
            proteins. Unfolded polypeptides enter the central cavity of the
            complex and are folded in an ATP-dependent manner. The complex
            folds various proteins, including actin and tubulin. Mutations in
            this gene cause hereditary sensory and autonomic neuropathy with
            spastic paraplegia (HSNSP). Alternative splicing results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 5 and 13. [provided by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ224303.1, SRR1803615.113869.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280326.9/ ENSP00000280326.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..541
                     /product="T-complex protein 1 subunit epsilon isoform a"
                     /note="T-complex protein 1 subunit epsilon; epididymis
                     secretory protein Li 69; chaperonin containing TCP1,
                     subunit 5 (epsilon); chaperonin containing T-complex
                     polypeptide 1 subunit 5"
                     /calculated_mol_wt=59540
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P48643.1)"
     Region          10..535
                     /region_name="TCP1_epsilon"
                     /note="TCP-1 (CTT or eukaryotic type II) chaperonin
                     family, epsilon subunit. Chaperonins are involved in
                     productive folding of proteins. They share a common
                     general morphology, a double toroid of 2 stacked rings. In
                     contrast to bacterial group I chaperonins...; cd03339"
                     /db_xref="CDD:239455"
     Site            order(25,29,57..60,62,80,82,86,90,93,392,529..535)
                     /site_type="other"
                     /note="ring oligomerisation interface [polypeptide
                     binding]"
                     /db_xref="CDD:239455"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P48643.1)"
     Site            order(52..54,104,108,171,404,422,462,506,508)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239455"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48643.1)"
     Site            order(442,460,469,471..472,475)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239455"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48643.1)"
     CDS             1..541
                     /gene="CCT5"
                     /gene_synonym="CCT-epsilon; CCTE; HEL-S-69; HSNSP;
                     PNAS-102; TCP-1-epsilon"
                     /coded_by="NM_012073.5:62..1687"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3877.1"
                     /db_xref="GeneID:22948"
                     /db_xref="HGNC:HGNC:1618"
                     /db_xref="MIM:610150"
ORIGIN      
        1 masmgtlafd eygrpfliik dqdrksrlmg lealkshima akavantmrt slgpngldkm
       61 mvdkdgdvtv tndgatilsm mdvdhqiakl mvelsksqdd eigdgttgvv vlagalleea
      121 eqlldrgihp iriadgyeqa arvaiehldk isdsvlvdik dtepliqtak ttlgskvvns
      181 chrqmaeiav navltvadme rrdvdfelik vegkvggrle dtklikgviv dkdfshpqmp
      241 kkvedakiai ltcpfeppkp ktkhkldvts vedykalqky ekekfeemiq qiketganla
      301 icqwgfddea nhlllqnnlp avrwvggpei eliaiatggr ivprfselta eklgfaglvq
      361 eisfgttkdk mlvieqckns ravtifirgg nkmiieeakr slhdalcvir nlirdnrvvy
      421 gggaaeisca lavsqeadkc ptleqyamra fadalevipm alsensgmnp iqtmtevrar
      481 qvkemnpalg idclhkgtnd mkqqhvietl igkkqqisla tqmvrmilki ddirkpgese
      541 e
//
LOCUS       NP_001350710             202 aa            linear   PRI 27-APR-2025
DEFINITION  DNA dC->dU-editing enzyme APOBEC-3D isoform 2 [Homo sapiens].
ACCESSION   NP_001350710 XP_005261394
VERSION     NP_001350710.1
DBSOURCE    REFSEQ: accession NM_001363781.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Takei,H., Fukuda,H., Pan,G., Yamazaki,H., Matsumoto,T., Kazuma,Y.,
            Fujii,M., Nakayama,S., Kobayashi,I.S., Shindo,K., Yamashita,R.,
            Shirakawa,K., Takaori-Kondo,A. and Kobayashi,S.S.
  TITLE     Alternative splicing of APOBEC3D generates functional diversity and
            its role as a DNA mutator
  JOURNAL   Int J Hematol 112 (3), 395-408 (2020)
   PUBMED   32533515
  REMARK    GeneRIF: Alternative splicing of APOBEC3D generates functional
            diversity and its role as a DNA mutator.
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Desimmie,B.A., Burdick,R.C., Izumi,T., Doi,H., Shao,W.,
            Alvord,W.G., Sato,K., Koyanagi,Y., Jones,S., Wilson,E., Hill,S.,
            Maldarelli,F., Hu,W.S. and Pathak,V.K.
  TITLE     APOBEC3 proteins can copackage and comutate HIV-1 genomes
  JOURNAL   Nucleic Acids Res 44 (16), 7848-7865 (2016)
   PUBMED   27439715
  REMARK    GeneRIF: These results indicate that APOBEC3 proteins can be
            copackaged and can comutate the same genomes, and can cooperate to
            inhibit HIV replication.
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Bouzidi,M.S., Caval,V., Suspene,R., Hallez,C., Pineau,P.,
            Wain-Hobson,S. and Vartanian,J.P.
  TITLE     APOBEC3DE Antagonizes Hepatitis B Virus Restriction Factors
            APOBEC3F and APOBEC3G
  JOURNAL   J Mol Biol 428 (17), 3514-3528 (2016)
   PUBMED   27289067
  REMARK    GeneRIF: APOBEC3DE binds to itself, APOBEC3F, and APOBEC3G and
            antagonizes APOBEC3F and, to a lesser extent, APOBEC3G restriction
            of hepatitis B virus replication.
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Liang,W., Xu,J., Yuan,W., Song,X., Zhang,J., Wei,W., Yu,X.F. and
            Yang,Y.
  TITLE     APOBEC3DE Inhibits LINE-1 Retrotransposition by Interacting with
            ORF1p and Influencing LINE Reverse Transcriptase Activity
  JOURNAL   PLoS One 11 (7), e0157220 (2016)
   PUBMED   27428332
  REMARK    GeneRIF: APOBEC3DE inhibits human LINE-1 retrotransposition.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 202)
  AUTHORS   Sato,K., Takeuchi,J.S., Misawa,N., Izumi,T., Kobayashi,T.,
            Kimura,Y., Iwami,S., Takaori-Kondo,A., Hu,W.S., Aihara,K., Ito,M.,
            An,D.S., Pathak,V.K. and Koyanagi,Y.
  TITLE     APOBEC3D and APOBEC3F potently promote HIV-1 diversification and
            evolution in humanized mouse model
  JOURNAL   PLoS Pathog 10 (10), e1004453 (2014)
   PUBMED   25330146
  REMARK    GeneRIF: APOBEC3D/F and APOBEC3G fundamentally work as restriction
            factors against HIV-1 in vivo
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 202)
  AUTHORS   Conticello,S.G., Thomas,C.J., Petersen-Mahrt,S.K. and
            Neuberger,M.S.
  TITLE     Evolution of the AID/APOBEC family of polynucleotide
            (deoxy)cytidine deaminases
  JOURNAL   Mol Biol Evol 22 (2), 367-377 (2005)
   PUBMED   15496550
REFERENCE   7  (residues 1 to 202)
  AUTHORS   Harris,R.S. and Liddament,M.T.
  TITLE     Retroviral restriction by APOBEC proteins
  JOURNAL   Nat Rev Immunol 4 (11), 868-877 (2004)
   PUBMED   15516966
  REMARK    Review article
REFERENCE   8  (residues 1 to 202)
  AUTHORS   Sawyer,S.L., Emerman,M. and Malik,H.S.
  TITLE     Ancient adaptive evolution of the primate antiviral DNA-editing
            enzyme APOBEC3G
  JOURNAL   PLoS Biol 2 (9), E275 (2004)
   PUBMED   15269786
REFERENCE   9  (residues 1 to 202)
  AUTHORS   Wedekind,J.E., Dance,G.S., Sowden,M.P. and Smith,H.C.
  TITLE     Messenger RNA editing in mammals: new members of the APOBEC family
            seeking roles in the family business
  JOURNAL   Trends Genet 19 (4), 207-216 (2003)
   PUBMED   12683974
  REMARK    Review article
            Erratum:[Trends Genet. 2003 Jul;19(7):369]
REFERENCE   10 (residues 1 to 202)
  AUTHORS   Jarmuz,A., Chester,A., Bayliss,J., Gisbourne,J., Dunham,I.,
            Scott,J. and Navaratnam,N.
  TITLE     An anthropoid-specific locus of orphan C to U RNA-editing enzymes
            on chromosome 22
  JOURNAL   Genomics 79 (3), 285-296 (2002)
   PUBMED   11863358
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB121958.1, DA287097.1,
            CR456396.1, BX340829.2, AL022318.2 and BC017022.1.
            
            On Jun 3, 2018 this sequence version replaced XP_005261394.1.
            
            Summary: This gene is a member of the cytidine deaminase gene
            family. It is one of a group of related genes found in a cluster,
            thought to result from gene duplication, on chromosome 22. Members
            of the cluster encode proteins that are structurally and
            functionally related to the C to U RNA-editing cytidine deaminase
            APOBEC1 and inhibit retroviruses, such as HIV, by deaminating
            cytosine residues in nascent retroviral cDNA. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.199446.1,
                                           SRR1163657.359130.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..202
                     /product="DNA dC->dU-editing enzyme APOBEC-3D isoform 2"
                     /EC_number="3.5.4.38"
                     /note="apolipoprotein B mRNA editing enzyme, catalytic
                     polypeptide-like 3E pseudogene; probable DNA
                     dC->dU-editing enzyme APOBEC-3D; apolipoprotein B mRNA
                     editing enzyme, catalytic polypeptide-like 3D"
                     /calculated_mol_wt=24020
     Region          12..202
                     /region_name="APOBEC2"
                     /note="pfam18772"
                     /db_xref="CDD:465863"
     CDS             1..202
                     /gene="APOBEC3D"
                     /gene_synonym="A3D; A3DE; APOBEC3DE; APOBEC3E; ARP6"
                     /coded_by="NM_001363781.1:394..1002"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS87027.1"
                     /db_xref="GeneID:140564"
                     /db_xref="HGNC:HGNC:17354"
                     /db_xref="MIM:609900"
ORIGIN      
        1 mnpqirnpme rmyrdtfydn fenepilygr sytwlcyevk ikrgrsnllw dtgvfrgpvl
       61 pkrqsnhrqe vdpethchae rcflswfcdd ilspntnyev twytswspcp ecagevaefl
      121 arhsnvnlti ftarlcyfwd tdyqeglcsl sqegasvkim gykdfvscwk nfvysddepf
      181 kpwkglqtnf rllkrrlrei lq
//
LOCUS       NP_001177                736 aa            linear   PRI 27-APR-2025
DEFINITION  transcription regulator protein BACH1 [Homo sapiens].
ACCESSION   NP_001177
VERSION     NP_001177.1
DBSOURCE    REFSEQ: accession NM_001186.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Chen,Y., Zeng,Z. and Chen,J.
  TITLE     Role of BACH1 in multiple myeloma
  JOURNAL   Hematology 29 (1), 2352687 (2024)
   PUBMED   38767507
  REMARK    GeneRIF: Role of BACH1 in multiple myeloma.
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Xiao,S., Li,G., Tan,M., Liu,W. and Li,W.
  TITLE     Loss of BACH1 improves osteogenic differentiation in
            glucocorticoid-induced hBMSCs through restoring autophagy
  JOURNAL   BMC Musculoskelet Disord 25 (1), 665 (2024)
   PUBMED   39182017
  REMARK    GeneRIF: Loss of BACH1 improves osteogenic differentiation in
            glucocorticoid-induced hBMSCs through restoring autophagy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Dennis,M., Hurley,A., Bray,N., Cordero,C., Ilagan,J., Mertz,T.M.
            and Roberts,S.A.
  TITLE     Her2 amplification, Rel-A, and Bach1 can influence APOBEC3A
            expression in breast cancer cells
  JOURNAL   PLoS Genet 20 (5), e1011293 (2024)
   PUBMED   38805570
  REMARK    GeneRIF: Her2 amplification, Rel-A, and Bach1 can influence
            APOBEC3A expression in breast cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Liu,L., Matsumoto,M., Watanabe-Matsui,M., Nakagawa,T., Nagasawa,Y.,
            Pang,J., Callens,B.K.K., Muto,A., Ochiai,K., Takekawa,H., Alam,M.,
            Nishizawa,H., Shirouzu,M., Shima,H., Nakayama,K. and Igarashi,K.
  TITLE     TANK Binding Kinase 1 Promotes BACH1 Degradation through Both
            Phosphorylation-Dependent and -Independent Mechanisms without
            Relying on Heme and FBXO22
  JOURNAL   Int J Mol Sci 25 (8), 4141 (2024)
   PUBMED   38673728
  REMARK    GeneRIF: TANK Binding Kinase 1 Promotes BACH1 Degradation through
            Both Phosphorylation-Dependent and -Independent Mechanisms without
            Relying on Heme and FBXO22.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Kanezaki,R., Toki,T., Yokoyama,M., Yomogida,K., Sugiyama,K.,
            Yamamoto,M., Igarashi,K. and Ito,E.
  TITLE     Transcription factor BACH1 is recruited to the nucleus by its novel
            alternative spliced isoform
  JOURNAL   J Biol Chem 276 (10), 7278-7284 (2001)
   PUBMED   11069897
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Kobayashi,A., Yamagiwa,H., Hoshino,H., Muto,A., Sato,K., Morita,M.,
            Hayashi,N., Yamamoto,M. and Igarashi,K.
  TITLE     A combinatorial code for gene expression generated by transcription
            factor Bach2 and MAZR (MAZ-related factor) through the BTB/POZ
            domain
  JOURNAL   Mol Cell Biol 20 (5), 1733-1746 (2000)
   PUBMED   10669750
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Blouin,J.L., Duriaux Sail,G., Guipponi,M., Rossier,C.,
            Pappasavas,M.P. and Antonarakis,S.E.
  TITLE     Isolation of the human BACH1 transcription regulator gene, which
            maps to chromosome 21q22.1
  JOURNAL   Hum Genet 102 (3), 282-288 (1998)
   PUBMED   9544839
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Ohira,M., Seki,N., Nagase,T., Ishikawa,K., Nomura,N. and Ohara,O.
  TITLE     Characterization of a human homolog (BACH1) of the mouse Bach1 gene
            encoding a BTB-basic leucine zipper transcription factor and its
            mapping to chromosome 21q22.1
  JOURNAL   Genomics 47 (2), 300-306 (1998)
   PUBMED   9479503
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Oyake,T., Itoh,K., Motohashi,H., Hayashi,N., Hoshino,H.,
            Nishizawa,M., Yamamoto,M. and Igarashi,K.
  TITLE     Bach proteins belong to a novel family of BTB-basic leucine zipper
            transcription factors that interact with MafK and regulate
            transcription through the NF-E2 site
  JOURNAL   Mol Cell Biol 16 (11), 6083-6095 (1996)
   PUBMED   8887638
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Rehfuss,R.P., Walton,K.M., Loriaux,M.M. and Goodman,R.H.
  TITLE     The cAMP-regulated enhancer-binding protein ATF-1 activates
            transcription in response to cAMP-dependent protein kinase A
  JOURNAL   J Biol Chem 266 (28), 18431-18434 (1991)
   PUBMED   1655749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC063307.1, AF124731.2 and
            AI336948.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a transcription factor that belongs to
            the cap'n'collar type of basic region leucine zipper factor family
            (CNC-bZip). The encoded protein contains broad complex, tramtrack,
            bric-a-brac/poxvirus and zinc finger (BTB/POZ) domains, which is
            atypical of CNC-bZip family members. These BTB/POZ domains
            facilitate protein-protein interactions and formation of homo-
            and/or hetero-oligomers. When this encoded protein forms a
            heterodimer with MafK, it functions as a repressor of Maf
            recognition element (MARE) and transcription is repressed. Multiple
            alternatively spliced transcript variants have been identified for
            this gene. [provided by RefSeq, May 2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063307.1, SRR1660809.206118.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000286800.8/ ENSP00000286800.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..736
                     /product="transcription regulator protein BACH1"
                     /note="basic region leucine zipper transcriptional
                     regulator BACH1; BTB and CNC homology 1, basic leucine
                     zipper transcription factor 1"
                     /calculated_mol_wt=81827
     Region          7..126
                     /region_name="BTB_POZ_BACH1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in BTB and CNC
                     homolog 1 (BACH1); cd18277"
                     /db_xref="CDD:349586"
     Site            order(7..13,16..21,23..24,27,33,48,50,53..55,63,90..91,
                     94..100,117..119,122,125..126)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349586"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14867.2)"
     Region          286..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14867.2)"
     Region          349..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14867.2)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14867.2)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O14867.2)"
     Region          551..621
                     /region_name="bZIP_BACH"
                     /note="Basic leucine zipper (bZIP) domain of BTB and CNC
                     homolog (BACH) proteins: a DNA-binding and dimerization
                     domain; cd14719"
                     /db_xref="CDD:269867"
     Region          555..617
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269867"
     Region          562..578
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (O14867.2)"
     Site            order(563..564,566..568,570..575,577..579)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269867"
     Site            order(578,581..582,585..586,588..589,592..593,595..596,
                     599..600,602..603,606..607,609..610)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269867"
     Region          582..589
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (O14867.2)"
     Region          680..719
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14867.2)"
     CDS             1..736
                     /gene="BACH1"
                     /gene_synonym="BACH-1; BTBD24"
                     /coded_by="NM_001186.4:93..2303"
                     /db_xref="CCDS:CCDS13585.1"
                     /db_xref="GeneID:571"
                     /db_xref="HGNC:HGNC:935"
                     /db_xref="MIM:602751"
ORIGIN      
        1 mslsensvfa yessvhstnv llslndqrkk dvlcdvtifv egqrfrahrs vlaacssyfh
       61 srivgqadge lnitlpeevt vkgfepliqf aytaklilsk envdevckcv eflsvhniee
      121 scfqflkfkf ldstadqqec prkkcfsshc qktdlklsll dqrdletdev eeflenknvq
      181 tpqcklrryq gnakaspplq dsasqtyesm clekdaalal pslcpkyrkf qkafgtdrvr
      241 tgessvkdih asvqpnerse neclggvpec rdlqvmlkcd esklamepee tkkdpasqcp
      301 teksevtpfp hnssidphgl yslsllhtyd qygdlnfagm qnttvltekp lsgtdvqekt
      361 fgesqdlplk sdlgtredss vassdrssve revaehlakg fwsdicstdt pcqmqlspav
      421 akdgseqisq krsecpwlgi risespepgq rtfttlssvn cpfistlste gcssnleign
      481 ddyvsepqqe pcpyacvisl gddsetdteg dsescsareq ecevklpfna qriislsrnd
      541 fqsllkmhkl tpeqldcihd irrrsknria aqrcrkrkld ciqnleseie klqsekesll
      601 kerdhilstl getkqnltgl cqkvckeaal sqeqiqilak ysaadcplsf lisekdkstp
      661 dgelalpsif slsdrppavl ppcargnsep gyargqesqq mstatseqag paeqcrqsgg
      721 isdfcqqmtd kcttde
//
LOCUS       NP_001357012             320 aa            linear   PRI 27-APR-2025
DEFINITION  pro-neuregulin-3, membrane-bound isoform isoform 6 [Homo sapiens].
ACCESSION   NP_001357012
VERSION     NP_001357012.1
DBSOURCE    REFSEQ: accession NM_001370083.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Ahmad,T., Vullhorst,D., Chaudhuri,R., Guardia,C.M., Chaudhary,N.,
            Karavanova,I., Bonifacino,J.S. and Buonanno,A.
  TITLE     Transcytosis and trans-synaptic retention by postsynaptic ErbB4
            underlie axonal accumulation of NRG3
  JOURNAL   J Cell Biol 221 (7) (2022)
   PUBMED   35579602
  REMARK    GeneRIF: Transcytosis and trans-synaptic retention by postsynaptic
            ErbB4 underlie axonal accumulation of NRG3.
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kara,H.G., Erdal,M.E., Yilmaz,S.G., Sengul,C., Sengul,C.B. and
            Karakulah,K.
  TITLE     Association of NRG3 and ERBB4 gene polymorphism with nicotine
            dependence in Turkish population
  JOURNAL   Mol Biol Rep 48 (6), 5319-5326 (2021)
   PUBMED   34247340
  REMARK    GeneRIF: Association of NRG3 and ERBB4 gene polymorphism with
            nicotine dependence in Turkish population.
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Zhou,Y., Li,Y., Meng,Y., Wang,J., Wu,F., Ning,Y., Li,Y.,
            Cassidy,R.M., Li,Z. and Zhang,X.Y.
  TITLE     Neuregulin 3 rs10748842 polymorphism contributes to the effect of
            body mass index on cognitive impairment in patients with
            schizophrenia
  JOURNAL   Transl Psychiatry 10 (1), 62 (2020)
   PUBMED   32066712
  REMARK    GeneRIF: Neuregulin 3 rs10748842 polymorphism contributes to the
            effect of body mass index on cognitive impairment in patients with
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Li,Z., Liu,L., Lin,W., Zhou,Y., Zhang,G., Du,X., Li,Y., Tang,W. and
            Zhang,X.
  TITLE     NRG3 contributes to cognitive deficits in chronic patients with
            schizophrenia
  JOURNAL   Schizophr Res 215, 134-139 (2020)
   PUBMED   31753594
  REMARK    GeneRIF: NRG3 contributes to cognitive deficits in chronic patients
            with schizophrenia.
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Pinto,R., Assis,J., Nogueira,A., Pereira,C., Coelho,S., Brandao,M.,
            Dias,J., Alves,S., Pereira,D. and Medeiros,R.
  TITLE     Pharmacogenomics in epithelial ovarian cancer first-line treatment
            outcome: validation of GWAS-associated NRG3 rs1649942 and BRE
            rs7572644 variants in an independent cohort
  JOURNAL   Pharmacogenomics J 19 (1), 25-32 (2019)
   PUBMED   30287910
  REMARK    GeneRIF: The BRE rs7572644 and NRG3 rs1649942 genetic variants were
            validated in an independent cohort of EOC Portuguese patients.
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Benzel,I., Bansal,A., Browning,B.L., Galwey,N.W., Maycox,P.R.,
            McGinnis,R., Smart,D., St Clair,D., Yates,P. and Purvis,I.
  TITLE     Interactions among genes in the ErbB-Neuregulin signalling network
            are associated with increased susceptibility to schizophrenia
  JOURNAL   Behav Brain Funct 3, 31 (2007)
   PUBMED   17598910
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Carteron,C., Ferrer-Montiel,A. and Cabedo,H.
  TITLE     Characterization of a neural-specific splicing form of the human
            neuregulin 3 gene involved in oligodendrocyte survival
  JOURNAL   J Cell Sci 119 (Pt 5), 898-909 (2006)
   PUBMED   16478787
  REMARK    GeneRIF: The NRG3 protein is a new post-translationally regulated
            isoform of neuregulin 3 expressed in the developing human central
            nervous system with a role in oligodendrocyte survival.
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Hobbs,S.S., Coffing,S.L., Le,A.T., Cameron,E.M., Williams,E.E.,
            Andrew,M., Blommel,E.N., Hammer,R.P., Chang,H. and Riese,D.J. 2nd.
  TITLE     Neuregulin isoforms exhibit distinct patterns of ErbB family
            receptor activation
  JOURNAL   Oncogene 21 (55), 8442-8452 (2002)
   PUBMED   12466964
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Gizatullin,R.Z., Muravenko,O.V., Al-Amin,A.N., Wang,F.,
            Protopopov,A.I., Kashuba,V.I., Zelenin,A.V. and Zabarovsky,E.R.
  TITLE     Human NRG3 gene Map position 10q22-q23
  JOURNAL   Chromosome Res 8 (6), 560 (2000)
   PUBMED   11032326
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Zhang,D., Sliwkowski,M.X., Mark,M., Frantz,G., Akita,R., Sun,Y.,
            Hillan,K., Crowley,C., Brush,J. and Godowski,P.J.
  TITLE     Neuregulin-3 (NRG3): a novel neural tissue-enriched protein that
            binds and activates ErbB4
  JOURNAL   Proc Natl Acad Sci U S A 94 (18), 9562-9567 (1997)
   PUBMED   9275162
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL096706.10 and AL391478.14.
            
            Summary: This gene is a member of the neuregulin gene family. This
            gene family encodes ligands for the transmembrane tyrosine kinase
            receptors ERBB3 and ERBB4 - members of the epidermal growth factor
            receptor family. Ligand binding activates intracellular signaling
            cascades and the induction of cellular responses including
            proliferation, migration, differentiation, and survival or
            apoptosis. This gene encodes neuregulin 3 (NRG3). NRG3 has been
            shown to activate the tyrosine phosphorylation of its cognate
            receptor, ERBB4, and is thought to influence neuroblast
            proliferation, migration and differentiation by signalling through
            ERBB4. NRG3 also promotes mammary differentiation during
            embryogenesis. Linkage studies have implicated this gene as a
            susceptibility locus for schizophrenia and schizoaffective
            disorder. Alternative splicing results in multiple transcript
            variants encoding distinct isoforms. Additional transcript variants
            have been described but their biological validity has not been
            verified.[provided by RefSeq, Sep 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.112486.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1966682,
                                           SAMEA1968832 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..320
                     /product="pro-neuregulin-3, membrane-bound isoform isoform
                     6"
                     /note="neuregulin-3-like polypeptide"
                     /calculated_mol_wt=33000
     Region          28..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56975.1)"
     Region          119..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56975.1)"
     Region          246..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56975.1)"
     CDS             1..320
                     /gene="NRG3"
                     /gene_synonym="HRG3; pro-NRG3"
                     /coded_by="NM_001370083.1:148..1110"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:10718"
                     /db_xref="HGNC:HGNC:7999"
                     /db_xref="MIM:605533"
ORIGIN      
        1 msegaaaasp pgaasaaaas aeegtaaaaa aaaagggpdg ggegaaeppr elrcsdcivw
       61 nrqqtwlcvv plfigfiglg lslmllkwiv vgsvkeyvpt dlvdskgmgq dpfflskpss
      121 fpkametttt ttsttspatp saggaassrt pnristrltt itraptrfpg hrvpiraspr
      181 sttarntaap atvpsttapf fssstlgsrp pvpgtpstqa mpswptaaya tssylhdstp
      241 swtlspfqda asssssssss attttpetst spkfhtttys tersehfkpc rdkdlaycln
      301 dgecfvietl tgshkhcrkv
//
LOCUS       NP_001348533            1077 aa            linear   ROD 27-APR-2025
DEFINITION  adenylate cyclase type 4 [Mus musculus].
ACCESSION   NP_001348533 XP_006518386
VERSION     NP_001348533.1
DBSOURCE    REFSEQ: accession NM_001361604.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Li,G., Chen,L., Jiang,Z. and Yau,K.W.
  TITLE     Coexistence within one cell of microvillous and ciliary
            phototransductions across M1- through M6-IpRGCs
  JOURNAL   Proc Natl Acad Sci U S A 120 (52), e2315282120 (2023)
   PUBMED   38109525
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Ahuja,N., Hiltabidle,M.S., Rajasekhar,H., Voss,S., Lu,S.Z.,
            Barlow,H.R., Cowdin,M.A., Daniel,E., Vaddaraju,V., Anandakumar,T.,
            Black,E., Cleaver,O. and Maynard,C.
  TITLE     Endothelial Cyp26b1 restrains murine heart valve growth during
            development
  JOURNAL   Dev Biol 486, 81-95 (2022)
   PUBMED   35364055
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Chen,K., Wang,S. and Sun,Z.
  TITLE     In Vivo Cardiac-specific Expression of Adenylyl Cyclase 4 Gene
            Protects against Klotho Deficiency-induced Heart Failure
  JOURNAL   Transl Res 244, 101-113 (2022)
   PUBMED   35114419
  REMARK    GeneRIF: In Vivo Cardiac-specific Expression of Adenylyl Cyclase 4
            Gene Protects against Klotho Deficiency-induced Heart Failure.
REFERENCE   4  (residues 1 to 1077)
  AUTHORS   Estrada,S.M., Thagard,A.S., Dehart,M.J., Damicis,J.R.,
            Dornisch,E.M., Ippolito,D.L., Burd,I., Napolitano,P.G. and
            Ieronimakis,N.
  TITLE     The orphan nuclear receptor Nr4a1 mediates perinatal
            neuroinflammation in a murine model of preterm labor
  JOURNAL   Cell Death Dis 11 (1), 11 (2020)
   PUBMED   31907354
  REMARK    Erratum:[Cell Death Dis. 2020 Jun 30;11(6):495. doi:
            10.1038/s41419-020-2682-y. PMID: 32606386]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1077)
  AUTHORS   Kittikulsuth,W., Stuart,D. and Kohan,D.E.
  TITLE     Adenylyl cyclase 4 does not regulate collecting duct water and
            sodium handling
  JOURNAL   Physiol Rep 2 (3), e00277 (2014)
   PUBMED   24760529
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1077)
  AUTHORS   Meneray,M.A. and Lallier,T.E.
  TITLE     Differential expression of adenylyl cyclase mRNAs in lacrimal
            glands of NZB/NZW and NOD pre-autoimmune mice
  JOURNAL   Adv Exp Med Biol 506 (Pt A), 41-49 (2002)
   PUBMED   12613887
REFERENCE   7  (residues 1 to 1077)
  AUTHORS   Baker,L.P., Nielsen,M.D., Impey,S., Hacker,B.M., Poser,S.W.,
            Chan,M.Y. and Storm,D.R.
  TITLE     Regulation and immunohistochemical localization of
            betagamma-stimulated adenylyl cyclases in mouse hippocampus
  JOURNAL   J Neurosci 19 (1), 180-192 (1999)
   PUBMED   9870949
REFERENCE   8  (residues 1 to 1077)
  AUTHORS   Suzuki,Y., Shen,T., Poyard,M., Best-Belpomme,M., Hanoune,J. and
            Defer,N.
  TITLE     Expression of adenylyl cyclase mRNAs in the denervated and in the
            developing mouse skeletal muscle
  JOURNAL   Am J Physiol 274 (6), C1674-C1685 (1998)
   PUBMED   9611134
REFERENCE   9  (residues 1 to 1077)
  AUTHORS   Edelhoff,S., Villacres,E.C., Storm,D.R. and Disteche,C.M.
  TITLE     Mapping of adenylyl cyclase genes type I, II, III, IV, V, and VI in
            mouse
  JOURNAL   Mamm Genome 6 (2), 111-113 (1995)
   PUBMED   7766992
REFERENCE   10 (residues 1 to 1077)
  AUTHORS   Gao,B.N. and Gilman,A.G.
  TITLE     Cloning and expression of a widely distributed (type IV) adenylyl
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 88 (22), 10178-10182 (1991)
   PUBMED   1946437
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY346402.1, AK141767.1 and AC098877.3.
            
            On Mar 29, 2018 this sequence version replaced XP_006518386.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK141767.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 28.19 cM"
     Protein         1..1077
                     /product="adenylate cyclase type 4"
                     /EC_number="4.6.1.1"
                     /note="adenylyl cyclase 4; ATP pyrophosphate-lyase 4;
                     adenylate cyclase type IV"
                     /calculated_mol_wt=120249
     Site            29..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Region          40..453
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
     Site            61..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            94..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            120..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            141..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            170..190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Region          264..447
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(276,278..283,318,320..322,325,387..389,393..394,
                     397..398,437)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(278,322)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(283,295,298..299,302,306,318..319,375,378,388..391,
                     394,437)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     Region          479..581
                     /region_name="Adcy_cons_dom"
                     /note="Adenylate cyclase, conserved domain; pfam06327"
                     /db_xref="CDD:461877"
     Region          503..524
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P26770; propagated from
                     UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P26770; propagated from
                     UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            583..604
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            608..630
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            661..684
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            694
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            701
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            718..738
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            746..766
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Site            793..809
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91WF3.1)"
     Region          866..1065
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(878,880..885,927,929..931,934,1007..1009,1013..1014,
                     1017..1018,1054)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(880,931)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(885,901,904..905,908,912,927..928,995,998,
                     1008..1011,1014,1054)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     CDS             1..1077
                     /gene="Adcy4"
                     /gene_synonym="mKIAA4004"
                     /coded_by="NM_001361604.1:214..3447"
                     /db_xref="CCDS:CCDS27130.1"
                     /db_xref="GeneID:104110"
                     /db_xref="MGI:MGI:99674"
ORIGIN      
        1 marlfsprpp psedlfyety yslsqqypll illlvivlca lvalpavawa sgreltsdps
       61 flttvlcalg gfslllglas reqqlqrwtr plsgliwval lalgygflft ggvvsawdqv
      121 sfflfiiftv yamlplgmrd aaaagvissl shllvlglyl gwqpesqral lpqlaanavl
      181 flcgnvvgay hkalmeralr atfrealssl hsrrrldtek khqehlllsi lpaylaremk
      241 aeimarlqag qrsrpentnn fhslyvkrhq gvsvlyadiv gftrlasecs pkelvlmlne
      301 lfgkfdqiak ehecmrikil gdcyycvsgl plslpdhain cvrmgldmcr airklrvatg
      361 vdinmrvgvh sgsvlcgvig lqkwqydvws hdvtlanhme aggvpgrvhi tgatlallag
      421 ayaveradte hrdpylrelg eptylvidpr aeeedekgta kgllsslegh tmrpsllmtr
      481 yleswgaakp fahlshldsp vststplpek afspqwsldr srtprgldde ldtgdakffq
      541 vieqlnsqkq wkqskdfnll tlyfrekeme kqyrlsalpa fkyyaactfl vflsnftiqm
      601 lvttrppali itysitfllf flllfvcfse hltkcvqkgp kmlhwlpals vlvatrpgfr
      661 valgtatill vftmaiasll flpvssdclf lasnvssvtf naswempgsl plisiplisi
      721 pysmhccvlg flscslflhm sfelklllll lwlvascslf lhshawlsdc liarlyqsps
      781 dsrpgvlkep klmgaiyffi ffftllvlar qneyycrldf lwkkklrqer eetetmenlt
      841 rlllenvlpa hvapqfigqn rrnedlyhqs yecvcvlfas vpdfkefyse sninheglec
      901 lrllneiiad fdellskpkf sgvekiktig stymaatgln atsgqdtqqd serscshlgt
      961 mvefavalgs klgvinkhsf nnfrlrvgln hgpvvagvig aqkpqydiwg ntvnvasrme
     1021 stgvlgkiqv teetaralqs lgytcysrgs ikvkgkgelc tyflntdltr tgspsas
//
LOCUS       NP_002259                521 aa            linear   PRI 27-APR-2025
DEFINITION  importin subunit alpha-3 [Homo sapiens].
ACCESSION   NP_002259 NP_116160
VERSION     NP_002259.1
DBSOURCE    REFSEQ: accession NM_002268.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Ju,J., Zhang,H., Lin,M., Yan,Z., An,L., Cao,Z., Geng,D., Yue,J.,
            Tang,Y., Tian,L., Chen,F., Han,Y., Wang,W., Zhao,S., Jiao,S. and
            Zhou,Z.
  TITLE     The alanyl-tRNA synthetase AARS1 moonlights as a lactyltransferase
            to promote YAP signaling in gastric cancer
  JOURNAL   J Clin Invest 134 (10), e174587 (2024)
   PUBMED   38512451
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Yang,W., Yao,Y., Yang,S. and Ke,Y.
  TITLE     Circular RNA hsa_circ_0008003 promotes the progression of
            non-small-cell lung cancer by sponging miR-548I and regulating
            KPNA4 expression
  JOURNAL   Thorac Cancer 14 (6), 544-554 (2023)
   PUBMED   36573325
  REMARK    GeneRIF: Circular RNA hsa_circ_0008003 promotes the progression of
            non-small-cell lung cancer by sponging miR-548I and regulating
            KPNA4 expression.
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Seki,T., Tada,S., Katada,T. and Enomoto,T.
  TITLE     Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1:
            discrimination of Qip1 and Rch1 from hSrp1 by their ability to
            interact with DNA helicase Q1/RecQL
  JOURNAL   Biochem Biophys Res Commun 234 (1), 48-53 (1997)
   PUBMED   9168958
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Di Marzio,P., Choe,S., Ebright,M., Knoblauch,R. and Landau,N.R.
  TITLE     Mutational analysis of cell cycle arrest, nuclear localization and
            virion packaging of human immunodeficiency virus type 1 Vpr
  JOURNAL   J Virol 69 (12), 7909-7916 (1995)
   PUBMED   7494303
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Gallay,P., Swingler,S., Song,J., Bushman,F. and Trono,D.
  TITLE     HIV nuclear import is governed by the phosphotyrosine-mediated
            binding of matrix to the core domain of integrase
  JOURNAL   Cell 83 (4), 569-576 (1995)
   PUBMED   7585960
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Bukrinsky,M.I., Sharova,N., Dempsey,M.P., Stanwick,T.L.,
            Bukrinskaya,A.G., Haggerty,S. and Stevenson,M.
  TITLE     Active nuclear import of human immunodeficiency virus type 1
            preintegration complexes
  JOURNAL   Proc Natl Acad Sci U S A 89 (14), 6580-6584 (1992)
   PUBMED   1631159
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Sharova,N. and Bukrinskaya,A.
  TITLE     p17 and p17-containing gag precursors of input human
            immunodeficiency virus are transported into the nuclei of infected
            cells
  JOURNAL   AIDS Res Hum Retroviruses 7 (3), 303-306 (1991)
   PUBMED   2064827
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC034493.2 and AC078868.14.
            
            On Dec 4, 2002 this sequence version replaced NP_116160.1.
            
            Summary: The nuclear import of karyophilic proteins is directed by
            short amino acid sequences termed nuclear localization signals
            (NLSs). Karyopherins, or importins, are cytoplasmic proteins that
            recognize NLSs and dock NLS-containing proteins to the nuclear pore
            complex. The protein encoded by this gene shares the sequence
            similarity with Xenopus importin-alpha and Saccharomyces cerevisiae
            Srp1. This protein is found to interact with the NLSs of DNA
            helicase Q1 and SV40 T antigen. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.21922.1,
                                           SRR11853565.21203.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334256.9/ ENSP00000334373.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.33"
     Protein         1..521
                     /product="importin subunit alpha-3"
                     /note="importin subunit alpha-4; importin alpha Q1;
                     karyopherin alpha 4 (importin alpha 3)"
                     /calculated_mol_wt=57756
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O00629.1)"
     Region          11..513
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          43..52
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:29042532"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00629.1)"
     Region          66..106
                     /region_name="ARM 1, truncated"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     Region          73..98
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          107..149
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     Region          109..142
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(133,137,141,175,179,183,218,222,226)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          137..229
                     /region_name="NLS binding site (major).
                     /evidence=ECO:0000269|PubMed:29042532"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     Region          150..186
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          192..227
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          195..233
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     Region          234..278
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     Region          244..269
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          279..318
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     Region          279..311
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(302,306,310,344,348,352,386,390,394)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          306..394
                     /region_name="NLS binding site (minor).
                     /evidence=ECO:0000269|PubMed:29042532"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     Region          319..355
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          361..400
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     Region          361..395
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          401..443
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     Region          404..438
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          447..485
                     /region_name="ARM 10, atypical"
                     /note="propagated from UniProtKB/Swiss-Prot (O00629.1)"
     CDS             1..521
                     /gene="KPNA4"
                     /gene_synonym="IPOA3; QIP1; SRP3"
                     /coded_by="NM_002268.5:290..1855"
                     /db_xref="CCDS:CCDS3191.1"
                     /db_xref="GeneID:3840"
                     /db_xref="HGNC:HGNC:6397"
                     /db_xref="MIM:602970"
ORIGIN      
        1 madnekldnq rlknfknkgr dletmrrqrn evvvelrknk rdehllkrrn vphediceds
       61 didgdyrvqn tsleaivqna ssdnqgiqls avqaarklls sdrnppiddl iksgilpilv
      121 hclerddnps lqfeaawalt niasgtseqt qavvqsnavp lflrllhsph qnvceqavwa
      181 lgniigdgpq crdyvislgv vkpllsfisp sipitflrnv twvmvnlcrh kdppppmeti
      241 qeilpalcvl ihhtdvnilv dtvwalsylt dagneqiqmv idsgivphlv pllshqevkv
      301 qtaalravgn ivtgtdeqtq vvlncdalsh fpallthpke kinkeavwfl snitagnqqq
      361 vqavidanlv pmiihlldkg dfgtqkeaaw aisnltisgr kdqvayliqq nvippfcnll
      421 tvkdaqvvqv vldglsnilk maedeaetig nlieecggle kieqlqnhen ediyklayei
      481 idqffssddi dedpslvpea iqggtfgfns sanvptegfq f
//
LOCUS       NP_055909                615 aa            linear   PRI 27-APR-2025
DEFINITION  hypermethylated in cancer 2 protein [Homo sapiens].
ACCESSION   NP_055909
VERSION     NP_055909.2
DBSOURCE    REFSEQ: accession NM_015094.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Huang,P., Peslak,S.A., Shehu,V., Keller,C.A., Giardine,B., Shi,J.,
            Hardison,R.C., Blobel,G.A. and Khandros,E.
  TITLE     let-7 miRNAs repress HIC2 to regulate BCL11A transcription and
            hemoglobin switching
  JOURNAL   Blood 143 (19), 1980-1991 (2024)
   PUBMED   38364109
  REMARK    GeneRIF: let-7 miRNAs repress HIC2 to regulate BCL11A transcription
            and hemoglobin switching.
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Luo,F., Liao,Y., Cao,E., Yang,Y., Tang,K., Zhou,D., Zhou,D. and
            Cai,H.
  TITLE     Hypermethylation of HIC2 is a potential prognostic biomarker and
            tumor suppressor of glioma based on bioinformatics analysis and
            experiments
  JOURNAL   CNS Neurosci Ther 29 (4), 1154-1167 (2023)
   PUBMED   36650953
  REMARK    GeneRIF: Hypermethylation of HIC2 is a potential prognostic
            biomarker and tumor suppressor of glioma based on bioinformatics
            analysis and experiments.
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Huang,P., Peslak,S.A., Ren,R., Khandros,E., Qin,K., Keller,C.A.,
            Giardine,B., Bell,H.W., Lan,X., Sharma,M., Horton,J.R.,
            Abdulmalik,O., Chou,S.T., Shi,J., Crossley,M., Hardison,R.C.,
            Cheng,X. and Blobel,G.A.
  TITLE     HIC2 controls developmental hemoglobin switching by repressing
            BCL11A transcription
  JOURNAL   Nat Genet 54 (9), 1417-1426 (2022)
   PUBMED   35941187
  REMARK    GeneRIF: HIC2 controls developmental hemoglobin switching by
            repressing BCL11A transcription.
            Erratum:[Nat Genet. 2023 Sep;55(9):1608. doi:
            10.1038/s41588-023-01488-7. PMID: 37524792]
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Song,J.Y., Lee,S.H., Kim,M.K., Jeon,B.N., Cho,S.Y., Lee,S.H.,
            Kim,K.S. and Hur,M.W.
  TITLE     HIC2, a new transcription activator of SIRT1
  JOURNAL   FEBS Lett 593 (14), 1763-1776 (2019)
   PUBMED   31127867
  REMARK    GeneRIF: HIC2 is a pivotal transcriptional activator of SIRT1
REFERENCE   6  (residues 1 to 615)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 615)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   8  (residues 1 to 615)
  AUTHORS   Deltour,S., Pinte,S., Guerardel,C., Wasylyk,B. and Leprince,D.
  TITLE     The human candidate tumor suppressor gene HIC1 recruits CtBP
            through a degenerate GLDLSKK motif
  JOURNAL   Mol Cell Biol 22 (13), 4890-4901 (2002)
   PUBMED   12052894
REFERENCE   9  (residues 1 to 615)
  AUTHORS   Deltour,S., Pinte,S., Guerardel,C. and Leprince,D.
  TITLE     Characterization of HRG22, a human homologue of the putative tumor
            suppressor gene HIC1
  JOURNAL   Biochem Biophys Res Commun 287 (2), 427-434 (2001)
   PUBMED   11554746
  REMARK    GeneRIF: HIC1 and HRG22 define a subgroup of BTB/POZ domains unable
            to recruit repressing complexes containing a histone deacetylase
            activity.
REFERENCE   10 (residues 1 to 615)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP000552.1, AP000556.2, CN373403.1, AP000557.2, BC094787.1 and
            BM675330.1.
            
            On Apr 3, 2007 this sequence version replaced NP_055909.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB028943.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000407464.7/ ENSP00000385319.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..615
                     /product="hypermethylated in cancer 2 protein"
                     /note="hic-2; hic-3; HIC1-related gene on chromosome 22
                     protein; zinc finger and BTB domain-containing protein 30"
                     /calculated_mol_wt=66025
     Region          25..144
                     /region_name="BTB_POZ_ZBTB30_HIC2"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in hypermethylated
                     in cancer 2 protein (Hic-2); cd18334"
                     /db_xref="CDD:349643"
     Region          144..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JB3.2)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96JB3.2)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96JB3.2)"
     Region          182..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JB3.2)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96JB3.2)"
     Region          229..421
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JB3.2)"
     Region          246..250
                     /region_name="Binding to CtBP"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JB3.2)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96JB3.2)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96JB3.2)"
     Region          444..464
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(444,447,460,464)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          503..>552
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          507..527
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          507..527
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(507,510,523,527)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(512,518,525,526,534,541)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          533..555
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          535..555
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(535,538,551,555)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          535..552
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Site            order(540,542,544,546..547,550..551,554,568,570,574..575,
                     578..579,582,596,598,600,602..603,606..607,610)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          559..>613
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          563..583
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          575..600
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          591..611
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..615
                     /gene="HIC2"
                     /gene_synonym="HRG22; ZBTB30; ZNF907"
                     /coded_by="NM_015094.3:264..2111"
                     /db_xref="CCDS:CCDS13789.1"
                     /db_xref="GeneID:23119"
                     /db_xref="HGNC:HGNC:18595"
                     /db_xref="MIM:607712"
ORIGIN      
        1 mvsgplalrw cawagrgdmg pdmelpshsk qlllqlnqqr tkgflcdvii mvensifrah
       61 knvlaassiy fkslvlhdnl inldtdmvss tvfqqildfi ytgkllpsdq paepnfstll
      121 taasylqlpe laalcrrklk ragkpfgsgr agstgmgrpp rsqrlstasv iqaryqglvd
      181 grkgahapqe lpqakgsdde lflggsnqds vqglgravcp aggeaglggc ssstngssgg
      241 ceqelgldls kkspplppat pgphltpdda aqlsdsqhgs ppaasappva nsasyselgg
      301 tpdepmdleg aednhlslle apggqprksl rhstrkkewg kkepvagspf erreagpkgp
      361 cpgeegegvg drvpngilas gagpsgpyge ppypckeeee ngkdasedsa qsgseggsgh
      421 asahymyrqe gyetvsygdn lyvcipcakg fpsseqlnah vethteeelf ikeegayetg
      481 sggaeeeaed lsapsaayta eprpfkcsvc ektykdpatl rqhekthwlt rpfpcnicgk
      541 mftqrgtmtr hmrshlglkp facdecgmrf trqyrltehm rvhsgekpye cqlcggkftq
      601 qrnlishlrm htsps
//
LOCUS       NP_001008703             102 aa            linear   PRI 27-APR-2025
DEFINITION  small integral membrane protein 29 isoform 1 [Homo sapiens].
ACCESSION   NP_001008703
VERSION     NP_001008703.2
DBSOURCE    REFSEQ: accession NM_001008703.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Deng,X., Sabino,E.C., Cunha-Neto,E., Ribeiro,A.L., Ianni,B.,
            Mady,C., Busch,M.P. and Seielstad,M.
  CONSRTM   REDSII Chagas Study Group from the NHLBI Retrovirus Epidemiology
            Donor Study-II Component International
  TITLE     Genome wide association study (GWAS) of Chagas cardiomyopathy in
            Trypanosoma cruzi seropositive subjects
  JOURNAL   PLoS One 8 (11), e79629 (2013)
   PUBMED   24324551
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 102)
  AUTHORS   N'Diaye,A., Chen,G.K., Palmer,C.D., Ge,B., Tayo,B., Mathias,R.A.,
            Ding,J., Nalls,M.A., Adeyemo,A., Adoue,V., Ambrosone,C.B.,
            Atwood,L., Bandera,E.V., Becker,L.C., Berndt,S.I., Bernstein,L.,
            Blot,W.J., Boerwinkle,E., Britton,A., Casey,G., Chanock,S.J.,
            Demerath,E., Deming,S.L., Diver,W.R., Fox,C., Harris,T.B.,
            Hernandez,D.G., Hu,J.J., Ingles,S.A., John,E.M., Johnson,C.,
            Keating,B., Kittles,R.A., Kolonel,L.N., Kritchevsky,S.B., Le
            Marchand,L., Lohman,K., Liu,J., Millikan,R.C., Murphy,A.,
            Musani,S., Neslund-Dudas,C., North,K.E., Nyante,S., Ogunniyi,A.,
            Ostrander,E.A., Papanicolaou,G., Patel,S., Pettaway,C.A.,
            Press,M.F., Redline,S., Rodriguez-Gil,J.L., Rotimi,C.,
            Rybicki,B.A., Salako,B., Schreiner,P.J., Signorello,L.B.,
            Singleton,A.B., Stanford,J.L., Stram,A.H., Stram,D.O., Strom,S.S.,
            Suktitipat,B., Thun,M.J., Witte,J.S., Yanek,L.R., Ziegler,R.G.,
            Zheng,W., Zhu,X., Zmuda,J.M., Zonderman,A.B., Evans,M.K., Liu,Y.,
            Becker,D.M., Cooper,R.S., Pastinen,T., Henderson,B.E.,
            Hirschhorn,J.N., Lettre,G. and Haiman,C.A.
  TITLE     Identification, replication, and fine-mapping of Loci associated
            with adult height in individuals of african ancestry
  JOURNAL   PLoS Genet 7 (10), e1002298 (2011)
   PUBMED   21998595
  REMARK    Erratum:[PLoS Genet. 2011 Nov;7(11).
            doi:10.1371/annotation/58c67154-3f10-4155-9085-dcd6e3689008]
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Kim,J.J., Lee,H.I., Park,T., Kim,K., Lee,J.E., Cho,N.H., Shin,C.,
            Cho,Y.S., Lee,J.Y., Han,B.G., Yoo,H.W. and Lee,J.K.
  TITLE     Identification of 15 loci influencing height in a Korean population
  JOURNAL   J Hum Genet 55 (1), 27-31 (2010)
   PUBMED   19893584
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 102)
  AUTHORS   Brass,A.L., Dykxhoorn,D.M., Benita,Y., Yan,N., Engelman,A.,
            Xavier,R.J., Lieberman,J. and Elledge,S.J.
  TITLE     Identification of host proteins required for HIV infection through
            a functional genomic screen
  JOURNAL   Science 319 (5865), 921-926 (2008)
   PUBMED   18187620
REFERENCE   7  (residues 1 to 102)
  AUTHORS   Kazmierczak,B., Borrmann,L. and Bullerdiek,J.
  TITLE     Assignment of a new gene (LBH)
  JOURNAL   Genomics 56 (1), 136-137 (1999)
   PUBMED   10036196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290164.1 and BU956518.1.
            
            On Apr 17, 2018 this sequence version replaced NP_001008703.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.469308.1, AK290164.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000476320.6/ ENSP00000417604.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..102
                     /product="small integral membrane protein 29 isoform 1"
                     /note="uncharacterized protein C6orf1"
                     /calculated_mol_wt=11419
     Site            3
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86T20.3)"
     Site            21..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T20.3)"
     CDS             1..102
                     /gene="SMIM29"
                     /gene_synonym="C6orf1; LBH"
                     /coded_by="NM_001008703.4:102..410"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4790.2"
                     /db_xref="GeneID:221491"
                     /db_xref="HGNC:HGNC:1340"
                     /db_xref="MIM:611419"
ORIGIN      
        1 msnttvpnap qansdsmvgy vlgpfflitl vgvvvavvmy vqkkkrvdrl rhhllpmysy
       61 dpaeelheae qellsdmgdp kvvhgwqsgy qhkrmplldv kt
//
LOCUS       NP_001156896              57 aa            linear   PRI 27-APR-2025
DEFINITION  COP9 signalosome complex subunit 9 isoform 2 [Homo sapiens].
ACCESSION   NP_001156896
VERSION     NP_001156896.1
DBSOURCE    REFSEQ: accession NM_001163424.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 57)
  AUTHORS   Ruidiaz,S.F., Dreier,J.E., Hartmann-Petersen,R. and Kragelund,B.B.
  TITLE     The disordered PCI-binding human proteins CSNAP and DSS1 have
            diverged in structure and function
  JOURNAL   Protein Sci 30 (10), 2069-2082 (2021)
   PUBMED   34272906
  REMARK    GeneRIF: The disordered PCI-binding human proteins CSNAP and DSS1
            have diverged in structure and function.
REFERENCE   2  (residues 1 to 57)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 57)
  AUTHORS   Fuzesi-Levi,M.G., Fainer,I., Ivanov Enchev,R., Ben-Nissan,G.,
            Levin,Y., Kupervaser,M., Friedlander,G., Salame,T.M., Nevo,R.,
            Peter,M. and Sharon,M.
  TITLE     CSNAP, the smallest CSN subunit, modulates proteostasis through
            cullin-RING ubiquitin ligases
  JOURNAL   Cell Death Differ 27 (3), 984-998 (2020)
   PUBMED   31367012
  REMARK    GeneRIF: CSNAP, the smallest CSN subunit, modulates proteostasis
            through cullin-RING ubiquitin ligases.
REFERENCE   4  (residues 1 to 57)
  AUTHORS   Rozen,S., Fuzesi-Levi,M.G., Ben-Nissan,G., Mizrachi,L.,
            Gabashvili,A., Levin,Y., Ben-Dor,S., Eisenstein,M. and Sharon,M.
  TITLE     CSNAP Is a Stoichiometric Subunit of the COP9 Signalosome
  JOURNAL   Cell Rep 13 (3), 585-598 (2015)
   PUBMED   26456823
REFERENCE   5  (residues 1 to 57)
  AUTHORS   Ebina,M., Tsuruta,F., Katoh,M.C., Kigoshi,Y., Someya,A. and
            Chiba,T.
  TITLE     Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear
            localization through Nedd8 modification
  JOURNAL   PLoS One 8 (6), e65285 (2013)
   PUBMED   23776465
  REMARK    GeneRIF: Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear
            localization through Nedd8 modification.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC013469.8, AF487338.1 and CN304277.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region and an alternate splice pattern
            in the 3' coding region, compared to variant 1. The resulting
            isoform (2) lacks an internal segment near the N-terminus and has a
            shorter and distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD176791.1, HY298704.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000607357.2/ ENSP00000475979.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..57
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..57
                     /product="COP9 signalosome complex subunit 9 isoform 2"
                     /note="helicase/primase complex protein;
                     myeloma-overexpressed gene 2 protein; myeloma
                     overexpressed 2; CSN acidic protein; COP9 signalosome
                     complex subunit 9"
                     /calculated_mol_wt=6080
     Region          1..50
                     /region_name="MYEOV2"
                     /note="Myeloma-overexpressed-like; pfam15004"
                     /db_xref="CDD:464436"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WXC6.3)"
     CDS             1..57
                     /gene="COPS9"
                     /gene_synonym="CSNAP; MYEOV2"
                     /coded_by="NM_001163424.2:22..195"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS63183.1"
                     /db_xref="GeneID:150678"
                     /db_xref="HGNC:HGNC:21314"
                     /db_xref="MIM:619349"
ORIGIN      
        1 mkpavdemfp egagpyvdld eaggstgllm dlaanekavh adffndfedl fddddiq
//
LOCUS       NP_066022               2564 aa            linear   PRI 27-APR-2025
DEFINITION  spectrin beta chain, non-erythrocytic 4 isoform sigma1 [Homo
            sapiens].
ACCESSION   NP_066022
VERSION     NP_066022.2
DBSOURCE    REFSEQ: accession NM_020971.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2564)
  AUTHORS   Nassal,D.M., Shaheen,R., Patel,N.J., Yu,J., Leahy,N., Bibidakis,D.,
            Parinandi,N.L. and Hund,T.J.
  TITLE     Spectrin-Based Regulation of Cardiac Fibroblast Cell-Cell
            Communication
  JOURNAL   Cells 12 (5), 748 (2023)
   PUBMED   36899883
  REMARK    GeneRIF: Spectrin-Based Regulation of Cardiac Fibroblast Cell-Cell
            Communication.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2564)
  AUTHORS   Buelow,M., Sussmuth,D., Smith,L.D., Aryani,O., Castiglioni,C.,
            Stenzel,W., Bertini,E., Schuelke,M. and Knierim,E.
  TITLE     Novel bi-allelic variants expand the SPTBN4-related genetic and
            phenotypic spectrum
  JOURNAL   Eur J Hum Genet 29 (7), 1121-1128 (2021)
   PUBMED   33772159
  REMARK    GeneRIF: Novel bi-allelic variants expand the SPTBN4-related
            genetic and phenotypic spectrum.
REFERENCE   3  (residues 1 to 2564)
  AUTHORS   Fujishima,K., Kurisu,J., Yamada,M. and Kengaku,M.
  TITLE     betaIII spectrin controls the planarity of Purkinje cell dendrites
            by modulating perpendicular axon-dendrite interactions
  JOURNAL   Development 147 (24), 226102 (2020)
   PUBMED   33234719
  REMARK    GeneRIF: betaIII spectrin controls the planarity of Purkinje cell
            dendrites by modulating perpendicular axon-dendrite interactions.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2564)
  AUTHORS   Wang,C.C., Ortiz-Gonzalez,X.R., Yum,S.W., Gill,S.M., White,A.,
            Kelter,E., Seaver,L.H., Lee,S., Wiley,G., Gaffney,P.M.,
            Wierenga,K.J. and Rasband,M.N.
  TITLE     betaIV Spectrinopathies Cause Profound Intellectual Disability,
            Congenital Hypotonia, and Motor Axonal Neuropathy
  JOURNAL   Am J Hum Genet 102 (6), 1158-1168 (2018)
   PUBMED   29861105
  REMARK    GeneRIF: bi-allelic pathogenic SPTBN4 variants (three homozygous
            and two compound heterozygous) that cause a severe neurological
            syndrome that includes congenital hypotonia, intellectual
            disability, and motor axonal and auditory neuropathy, are reported.
REFERENCE   5  (residues 1 to 2564)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 2564)
  AUTHORS   Komada,M. and Soriano,P.
  TITLE     [Beta]IV-spectrin regulates sodium channel clustering through
            ankyrin-G at axon initial segments and nodes of Ranvier
  JOURNAL   J Cell Biol 156 (2), 337-348 (2002)
   PUBMED   11807096
REFERENCE   7  (residues 1 to 2564)
  AUTHORS   Tse,W.T., Tang,J., Jin,O., Korsgren,C., John,K.M., Kung,A.L.,
            Gwynn,B., Peters,L.L. and Lux,S.E.
  TITLE     A new spectrin, beta IV, has a major truncated isoform that
            associates with promyelocytic leukemia protein nuclear bodies and
            the nuclear matrix
  JOURNAL   J Biol Chem 276 (26), 23974-23985 (2001)
   PUBMED   11294830
REFERENCE   8  (residues 1 to 2564)
  AUTHORS   Berghs,S., Aggujaro,D., Dirkx,R. Jr., Maksimova,E., Stabach,P.,
            Hermel,J.M., Zhang,J.P., Philbrick,W., Slepnev,V., Ort,T. and
            Solimena,M.
  TITLE     betaIV spectrin, a new spectrin localized at axon initial segments
            and nodes of ranvier in the central and peripheral nervous system
  JOURNAL   J Cell Biol 151 (5), 985-1002 (2000)
   PUBMED   11086001
REFERENCE   9  (residues 1 to 2564)
  AUTHORS   Chardin,P., Camonis,J.H., Gale,N.W., van Aelst,L., Schlessinger,J.,
            Wigler,M.H. and Bar-Sagi,D.
  TITLE     Human Sos1: a guanine nucleotide exchange factor for Ras that binds
            to GRB2
  JOURNAL   Science 260 (5112), 1338-1343 (1993)
   PUBMED   8493579
REFERENCE   10 (residues 1 to 2564)
  AUTHORS   Ortiz-Gonzalez,X. and Wierenga,K.
  TITLE     SPTBN4 Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32672909
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020929.6, AF311855.1,
            AB046862.1 and AI962525.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 30, 2006 this sequence version replaced NP_066022.1.
            
            Summary: Spectrin is an actin crosslinking and molecular scaffold
            protein that links the plasma membrane to the actin cytoskeleton,
            and functions in the determination of cell shape, arrangement of
            transmembrane proteins, and organization of organelles. It is
            composed of two antiparallel dimers of alpha- and beta- subunits.
            This gene is one member of a family of beta-spectrin genes. The
            encoded protein localizes to the nuclear matrix, PML nuclear
            bodies, and cytoplasmic vesicles. A highly similar gene in the
            mouse is required for localization of specific membrane proteins in
            polarized regions of neurons. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (sigma1) represents the longer
            transcript and encodes the longer isoform (sigma1), also known as
            the 289 kDa isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF311855.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000598249.6/ ENSP00000469242.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..2564
                     /product="spectrin beta chain, non-erythrocytic 4 isoform
                     sigma1"
                     /note="spectrin beta chain, brain 3; beta-IV spectrin;
                     spectrin, non-erythroid beta chain 3; spectrin beta chain,
                     non-erythrocytic 4"
                     /calculated_mol_wt=288855
     Region          1..282
                     /region_name="Actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          20..163
                     /region_name="CH_SF"
                     /note="calponin homology (CH) domain superfamily; cl00030"
                     /db_xref="CDD:469584"
     Site            order(67,118,120..121,124..125,127,140..144,149,151..152,
                     154..155,158..159,162)
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:409031"
     Region          165..294
                     /region_name="CH_SPTBN4_rpt2"
                     /note="second calponin homology (CH) domain found in
                     spectrin beta chain, non-erythrocytic 4 (SPTBN4) and
                     similar proteins; cd21322"
                     /db_xref="CDD:409171"
     Site            order(182,186,236,238..239,242,249,254..262,271..272,
                     274..275,278..279,282)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409171"
     Region          311..418
                     /region_name="Spectrin 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          430..644
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          430..533
                     /region_name="Spectrin 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Site            534..539
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          536..641
                     /region_name="Spectrin 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          774..879
                     /region_name="Spectrin 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          775..987
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            880..885
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          884..982
                     /region_name="Spectrin 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          1089..1196
                     /region_name="Spectrin 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          1091..1195
                     /region_name="SPEC"
                     /note="Spectrin repeats; smart00150"
                     /db_xref="CDD:197544"
     Region          1201..1409
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            1304..1309
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1306..1514
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          1306..1407
                     /region_name="Spectrin 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Site            1409..1414
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1412..1512
                     /region_name="Spectrin 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          1515..1617
                     /region_name="Spectrin 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          1516..1727
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            1620..1625
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1622..1834
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          1623..1725
                     /region_name="Spectrin 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Site            1726..1731
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1728..1830
                     /region_name="Spectrin 11. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          1834..1933
                     /region_name="Spectrin"
                     /note="Spectrin repeat; pfam00435"
                     /db_xref="CDD:395348"
     Region          1835..1935
                     /region_name="Spectrin 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          1853..1872
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          1943..>2110
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          1944..2046
                     /region_name="Spectrin 13. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Site            2047..2052
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2049..2123
                     /region_name="Spectrin 14. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          2208..2439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     Region          2421..2525
                     /region_name="PH_beta_spectrin"
                     /note="Beta-spectrin pleckstrin homology (PH) domain;
                     cd10571"
                     /db_xref="CDD:269975"
     Site            order(2428,2440..2442,2488)
                     /site_type="other"
                     /note="non-cannonical phosphoinositide binding site
                     [chemical binding]"
                     /db_xref="CDD:269975"
     Region          2533..2564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H254.2)"
     CDS             1..2564
                     /gene="SPTBN4"
                     /gene_synonym="CMND; NEDHND; QV; SPNB4; SPTBN3"
                     /coded_by="NM_020971.3:321..8015"
                     /note="isoform sigma1 is encoded by transcript variant
                     sigma1"
                     /db_xref="CCDS:CCDS12559.1"
                     /db_xref="GeneID:57731"
                     /db_xref="HGNC:HGNC:14896"
                     /db_xref="MIM:606214"
ORIGIN      
        1 maqvpgevdn meglpapnnn paarwespdr gwereqpaas taaaslfecs rikaladere
       61 avqkktftkw vnshlarvgc higdlyvdlr dgfvltrlle vlsgeqlprp trgrmrihsl
      121 envdkalqfl keqrvhlenv gshdivdgnh rltlglvwti ilrfqiqvik ietednretr
      181 sakdalllwc qmktagypev niqnfttswr dglafnalih rhrpdlvdfs kltksnanyn
      241 lqrafrtaeq hlglarlldp edvnmeapde ksiityvvsf yhyfskmkal avegkrigkv
      301 ldqvlevgki ieryeelaae llawihrtvg lisnqkfans lsgvqqqlqa ftayctlekp
      361 vkfqekgnle vllfsiqskl racnrrlfvp regcgiwdid kawgelekae hereaalrae
      421 lirqeklell aqrfdhkvam reswlnenqr lvsqdnfgye lpaveaamkk heaieadiaa
      481 yeervqgvae laqalaaegy ydirrvaaqr dsvlrqwall tglvgarrtr leqnlalqkv
      541 fqemvymvdw meemqaqlls recgqhlvea ddllqkhgll egdiaaqser vealnaaalr
      601 fsqlqgyqpc dpqvicnrvn hvhgclaelq eqaarrrael easrslwall qeleeaeswa
      661 rdkerlleaa ggggaagaag aagtaggahd lsstarllaq hkilqgelgg rrallqqalr
      721 cgeelvaagg avgpgadtvh lvglaeraas arrrwqrlee aaarrerrlq earalhqfga
      781 dldglldwlr dayrlaaagd fghdeassrr larqhraltg eveahrgpvs glrrqlatlg
      841 gasgagplvv alqvrvveae qlfaevteva alrrqwlrda lavyrmfgev hacelwigek
      901 eqwllsmrvp dslddvevvq hrfesldqem nslmgrvldv nhtvqelveg ghpssdevrs
      961 cqdhlnsrwn rivelveqrk eemsavllve nhvlevaevr aqvrekrrav esapraggal
     1021 qwrlsgleaa lqaleprqaa lleeaallae rfpaqaarlh qgaeelgaew galasaaqac
     1081 geavaaagrl qrflhdldaf ldwlvraqea aggsegplpn sleeadalla rhaalkeevd
     1141 qreedyariv aaseallaad gaelgpglal dewlphlelg whkllglwea rrealvqahi
     1201 yqlflrdlrq alvvlrnqem alsgaelpgt vesveealkq hrdflttmel sqqkmqvavq
     1261 aaegllrqgn iygeqaqeav trlleknqen qlraqqwmqk lhdqlelqhf lrdcheldgw
     1321 ihekmlmard gtrednhklh krwlrhqafm aelaqnkewl ekieregqql mqekpelaas
     1381 vrkklgeirq cwaelesttq akarqlfeas kadqlvqsfa eldkkllhme sqlqdvdpgg
     1441 dlatvnsqlk klqsmesqve ewyrevgelq aqtaalplep askelvgerq navgerlvrl
     1501 leplqerrrl llaskelhqv ahdlddelaw vqerlplamq tergnglqav qqhikknqgl
     1561 rreiqahgpr leevleraga laslrspeae avrrgleqlq sawaglreaa errqqvldaa
     1621 fqveqyyfdv aeveawlgeq ellmmsedkg kdeqstlqll kkhlqleqgv enyeesiaql
     1681 srqcrallem ghpdseqisr rqsqvdrlyv alkelgeerr valeqqywly qlsrqvsele
     1741 hwiaekevva gspelgqdfe hvsvlqekfs efasetgmag rerlaavnqm vdeliecght
     1801 aaatmaewkd glneawaell elmgtraqll aasrelhkff sdarelqgqi eekrrrlprl
     1861 ttppeprpsa ssmqrtlraf ehdlqllvsq vrqlqegaaq lrtvyageha eaiasreqev
     1921 lqgwkellsa cedarlhvss tadalrfhsq vrdllswmdg iasqigaadk prdvssvevl
     1981 mnyhqglkte learvpeltt cqelgrslll nksamadeiq aqldklgtrk eevsekwdrh
     2041 wewlqqmlev hqfaqeavva dawltaqepl lqsrelgssv deveqlirrh eafrkaaaaw
     2101 eerfsslrrl ttiekikaeq skqpptpllg rkffgdptel aakaapllrp ggyerglepl
     2161 arrasdtlsa evrtrvgyvr qelkperlqp ridrlpeipg rvepaalpaa pedaaetpat
     2221 paaaeqvrpr perqesadra eelprrrrpe rqesvdqsee aarrrrperq esaeheaahs
     2281 ltlgryeqme rrrerrerrl erqesseqem pirgdlvkgk atladiveql qekeagpglp
     2341 agpslpqpre lppgrlpngl elpertprpd rprardrpkp rrrprpregg egggsrrsrs
     2401 apaqggsapa pppppthtvq hegfllrkre ldanrkssnr swvslycvls kgelgfykds
     2461 kgpasgsthg gepllslhka tsevasdykk kkhvfklqtq dgsefllqak deeemngwle
     2521 avassvaeha eiarwgqtlp ttsstdegnp kreggdrras grrk
//
LOCUS       NP_002125                316 aa            linear   PRI 27-APR-2025
DEFINITION  heme oxygenase 2 isoform b [Homo sapiens].
ACCESSION   NP_002125
VERSION     NP_002125.3
DBSOURCE    REFSEQ: accession NM_002134.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Gamage,S.M.K., Nanayakkara,S., Macfarlane,L., Hewage,D., Cheng,T.,
            Aktar,S., Lu,C.T., Dissabandara,L., Islam,F., Lam,A.K. and
            Gopalan,V.
  TITLE     Heme oxygenase-1 & 2 and their potential contribution in heme
            induced colorectal carcinogenesis
  JOURNAL   Pathol Res Pract 233, 153885 (2022)
   PUBMED   35428017
  REMARK    GeneRIF: Heme oxygenase-1 & 2 and their potential contribution in
            heme induced colorectal carcinogenesis.
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Hanna,D.A., Moore,C.M., Liu,L., Yuan,X., Dominic,I.M.,
            Fleischhacker,A.S., Hamza,I., Ragsdale,S.W. and Reddi,A.R.
  TITLE     Heme oxygenase-2 (HO-2) binds and buffers labile ferric heme in
            human embryonic kidney cells
  JOURNAL   J Biol Chem 298 (2), 101549 (2022)
   PUBMED   34973332
  REMARK    GeneRIF: Heme oxygenase-2 (HO-2) binds and buffers labile ferric
            heme in human embryonic kidney cells.
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Fernandez-Fierro,A., Funes,S.C., Rios,M., Covian,C., Gonzalez,J.
            and Kalergis,A.M.
  TITLE     Immune Modulation by Inhibitors of the HO System
  JOURNAL   Int J Mol Sci 22 (1), 294 (2020)
   PUBMED   33396647
  REMARK    GeneRIF: Immune Modulation by Inhibitors of the HO System.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Liu,L., Dumbrepatil,A.B., Fleischhacker,A.S., Marsh,E.N.G. and
            Ragsdale,S.W.
  TITLE     Heme oxygenase-2 is post-translationally regulated by heme
            occupancy in the catalytic site
  JOURNAL   J Biol Chem 295 (50), 17227-17240 (2020)
   PUBMED   33051205
  REMARK    GeneRIF: Heme oxygenase-2 is post-translationally regulated by heme
            occupancy in the catalytic site.
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Saito-Ohara,F., Ikeuchi,T., Matsumoto,M. and Kurata,S.
  TITLE     Assignment of the mouse heme oxygenase genes: heme oxygenase-1
            (Hmox1) to chromosome 10 band C1 and heme oxygenase-2 (Hmox2) to
            chromosome 16 band B1
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 180-181 (1997)
   PUBMED   9284910
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Takahashi,K., Hara,E., Suzuki,H., Sasano,H. and Shibahara,S.
  TITLE     Expression of heme oxygenase isozyme mRNAs in the human brain and
            induction of heme oxygenase-1 by nitric oxide donors
  JOURNAL   J Neurochem 67 (2), 482-489 (1996)
   PUBMED   8764571
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Ishikawa,K., Takeuchi,N., Takahashi,S., Matera,K.M., Sato,M.,
            Shibahara,S., Rousseau,D.L., Ikeda-Saito,M. and Yoshida,T.
  TITLE     Heme oxygenase-2. Properties of the heme complex of the purified
            tryptic fragment of recombinant human heme oxygenase-2
  JOURNAL   J Biol Chem 270 (11), 6345-6350 (1995)
   PUBMED   7890772
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Kutty,R.K., Kutty,G., Rodriguez,I.R., Chader,G.J. and Wiggert,B.
  TITLE     Chromosomal localization of the human heme oxygenase genes: heme
            oxygenase-1 (HMOX1) maps to chromosome 22q12 and heme oxygenase-2
            (HMOX2) maps to chromosome 16p13.3
  JOURNAL   Genomics 20 (3), 513-516 (1994)
   PUBMED   8034330
REFERENCE   10 (residues 1 to 316)
  AUTHORS   McCoubrey,W.K. Jr., Ewing,J.F. and Maines,M.D.
  TITLE     Human heme oxygenase-2: characterization and expression of a
            full-length cDNA and evidence suggesting that the two HO-2
            transcripts may differ by choice of polyadenylation signal
  JOURNAL   Arch Biochem Biophys 295 (1), 13-20 (1992)
   PUBMED   1575508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA141643.1 and BC002396.2.
            
            On May 24, 2000 this sequence version replaced NP_002125.2.
            
            Summary: Heme oxygenase, an essential enzyme in heme catabolism,
            cleaves heme to form biliverdin, which is subsequently converted to
            bilirubin by biliverdin reductase, and carbon monoxide, a putative
            neurotransmitter. Heme oxygenase activity is induced by its
            substrate heme and by various nonheme substances. Heme oxygenase
            occurs as 2 isozymes, an inducible heme oxygenase-1 and a
            constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme
            oxygenase family. Several alternatively spliced transcript variants
            encoding three different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2013].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 5. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 1, 2, 3,
            4, 6, 7, and 8 all encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.272002.1,
                                           SRR1803616.247016.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000570646.6/ ENSP00000459214.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..316
                     /product="heme oxygenase 2 isoform b"
                     /EC_number="1.14.14.18"
                     /note="heme oxygenase (decycling) 2"
                     /calculated_mol_wt=35902
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30519.2)"
     mat_peptide     2..295
                     /product="Heme oxygenase 2 soluble form.
                     /evidence=ECO:0000305|PubMed:7890772. /id=PRO_0000455626"
                     /note="propagated from UniProtKB/Swiss-Prot (P30519.2)"
                     /calculated_mol_wt=33664
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P30519.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P30519.2)"
     Region          31..236
                     /region_name="Heme_oxygenase"
                     /note="Heme oxygenase; pfam01126"
                     /db_xref="CDD:395895"
     Site            order(38,45,48..49,54,58,154..156,162..163,167,199,203,
                     227,230,234)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:350856"
     Region          147..174
                     /region_name="kinked helix"
                     /note="kinked helix [structural motif]"
                     /db_xref="CDD:350856"
     Site            160
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:P09601; propagated from
                     UniProtKB/Swiss-Prot (P30519.2)"
     Region          264..269
                     /region_name="HRM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P30519.2)"
     Region          281..286
                     /region_name="HRM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P30519.2)"
     Site            296..316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30519.2)"
     CDS             1..316
                     /gene="HMOX2"
                     /gene_synonym="HO-2"
                     /coded_by="NM_002134.4:132..1082"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS10517.1"
                     /db_xref="GeneID:3163"
                     /db_xref="HGNC:HGNC:5014"
                     /db_xref="MIM:141251"
ORIGIN      
        1 msaevetseg vdesekknsg alekenqmrm adlsellkeg tkeahdraen tqfvkdflkg
       61 nikkelfkla ttalyftysa leeemernkd hpafaplyfp melhrkealt kdmeyffgen
      121 weeqvqcpka aqkyverihy igqnepellv ahaytrymgd lsggqvlkkv aqralklpst
      181 gegtqfylfe nvdnaqqfkq lyrarmnald lnmktkeriv eeankafeyn mqifneldqa
      241 gstlaretle dgfpvhdgkg dmrkcpfyaa eqdkgalegs scpfrtamav lrkpslqfil
      301 aagvalaagl lawyym
//
LOCUS       NP_005531                913 aa            linear   PRI 27-APR-2025
DEFINITION  type II inositol 1,4,5-trisphosphate 5-phosphatase isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_005531 XP_375718
VERSION     NP_005531.2
DBSOURCE    REFSEQ: accession NM_005540.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Droubi,A., Wallis,C., Anderson,K.E., Rahman,S., de Sa,A.,
            Rahman,T., Stephens,L.R., Hawkins,P.T. and Lowe,M.
  TITLE     The inositol 5-phosphatase INPP5B regulates B cell receptor
            clustering and signaling
  JOURNAL   J Cell Biol 221 (9) (2022)
   PUBMED   35878408
  REMARK    GeneRIF: The inositol 5-phosphatase INPP5B regulates B cell
            receptor clustering and signaling.
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Nakatsu,F., Messa,M., Nandez,R., Czapla,H., Zou,Y.,
            Strittmatter,S.M. and De Camilli,P.
  TITLE     Sac2/INPP5F is an inositol 4-phosphatase that functions in the
            endocytic pathway
  JOURNAL   J Cell Biol 209 (1), 85-95 (2015)
   PUBMED   25869668
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Montjean,R., Aoidi,R., Desbois,P., Rucci,J., Trichet,M.,
            Salomon,R., Rendu,J., Faure,J., Lunardi,J., Gacon,G., Billuart,P.
            and Dorseuil,O.
  TITLE     OCRL-mutated fibroblasts from patients with Dent-2 disease exhibit
            INPP5B-independent phenotypic variability relatively to Lowe
            syndrome cells
  JOURNAL   Hum Mol Genet 24 (4), 994-1006 (2015)
   PUBMED   25305077
  REMARK    GeneRIF: OCRL-mutated fibroblasts from patients with Dent-2 disease
            exhibit INPP5B-independent phenotypic variability relatively to
            Lowe syndrome cells
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Pirruccello,M., Nandez,R., Idevall-Hagren,O., Alcazar-Roman,A.,
            Abriola,L., Berwick,S.A., Lucast,L., Morel,D. and De Camilli,P.
  TITLE     Identification of inhibitors of inositol 5-phosphatases through
            multiple screening strategies
  JOURNAL   ACS Chem Biol 9 (6), 1359-1368 (2014)
   PUBMED   24742366
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Tresaugues,L., Silvander,C., Flodin,S., Welin,M., Nyman,T.,
            Graslund,S., Hammarstrom,M., Berglund,H. and Nordlund,P.
  TITLE     Structural basis for phosphoinositide substrate recognition,
            catalysis, and membrane interactions in human inositol
            polyphosphate 5-phosphatases
  JOURNAL   Structure 22 (5), 744-755 (2014)
   PUBMED   24704254
  REMARK    GeneRIF: The crystal structures of human INPP5B in complex with
            phosphoinositide substrate analogs revealed a membrane interaction
            patch likely to assist in sequestering substrates from the lipid
            bilayer.
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Speed,C.J., Matzaris,M., Bird,P.I. and Mitchell,C.A.
  TITLE     Tissue distribution and intracellular localisation of the 75-kDa
            inositol polyphosphate 5-phosphatase
  JOURNAL   Eur J Biochem 234 (1), 216-224 (1995)
   PUBMED   8529643
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Jefferson,A.B. and Majerus,P.W.
  TITLE     Properties of type II inositol polyphosphate 5-phosphatase
  JOURNAL   J Biol Chem 270 (16), 9370-9377 (1995)
   PUBMED   7721860
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Janne,P.A., Dutra,A.S., Dracopoli,N.C., Charnas,L.R., Puck,J.M. and
            Nussbaum,R.L.
  TITLE     Localization of the 75-kDa inositol polyphosphate-5-phosphatase
            (INPP5B) to human chromosome band 1p34
  JOURNAL   Cytogenet Cell Genet 66 (3), 164-166 (1994)
   PUBMED   8125013
REFERENCE   9  (residues 1 to 913)
  AUTHORS   Ross,T.S., Jefferson,A.B., Mitchell,C.A. and Majerus,P.W.
  TITLE     Cloning and expression of human 75-kDa inositol
            polyphosphate-5-phosphatase
  JOURNAL   J Biol Chem 266 (30), 20283-20289 (1991)
   PUBMED   1718960
REFERENCE   10 (residues 1 to 913)
  AUTHORS   Mitchell,C.A., Connolly,T.M. and Majerus,P.W.
  TITLE     Identification and isolation of a 75-kDa inositol
            polyphosphate-5-phosphatase from human platelets
  JOURNAL   J Biol Chem 264 (15), 8873-8877 (1989)
   PUBMED   2542294
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA125087.1, M74161.1,
            AL603790.41, AL929472.21 and BC042529.2.
            
            On Aug 31, 2006 this sequence version replaced NP_005531.1.
            
            Summary: This gene encodes a member of a family of inositol
            polyphosphate-5-phosphatases. These enzymes function in the
            regulation of calcium signaling by inactivating inositol
            phosphates. The encoded protein is localized to the cytosol and
            mitochondria, and associates with membranes through an isoprenyl
            modification near the C-terminus. Alternatively spliced transcript
            variants of this gene have been described. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Variants 1 and 5 both encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.214807.1,
                                           SRR1803611.270451.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000373024.8/
                                                  ENSP00000362115.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..913
                     /product="type II inositol 1,4,5-trisphosphate
                     5-phosphatase isoform 1 precursor"
                     /EC_number="3.1.3.36"
                     /note="phosphoinositide 5-phosphatase; type II inositol
                     1,4,5-trisphosphate 5-phosphatase; inositol
                     polyphosphate-5-phosphatase, 75kDa"
                     /calculated_mol_wt=103857
     Region          1..146
                     /region_name="INPP5B_PH"
                     /note="Type II inositol 1,4,5-trisphosphate 5-phosphatase
                     PH domain; pfam16776"
                     /db_xref="CDD:465268"
     mat_peptide     241..913
                     /product="type II inositol 1,4,5-trisphosphate
                     5-phosphatase isoform 1"
                     /calculated_mol_wt=77477
     Region          265..558
                     /region_name="INPP5c_INPP5B"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of Type II inositol polyphosphate
                     5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and
                     related proteins; cd09093"
                     /db_xref="CDD:197327"
     Site            order(273,275,303,306,308,311,373,379..380,400,403..404,
                     447,449,451,502..503,516,518,524,548..549)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197327"
     Site            order(273,303,400,447,449,524,548..549)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197327"
     Site            order(275,303,548)
                     /site_type="other"
                     /note="Mg binding site [ion binding]"
                     /db_xref="CDD:197327"
     Site            order(303,306,308,311,373,379..380,400,403..404,451,
                     502..503,516,518,548)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197327"
     Site            order(400,449,549)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197327"
     Region          692..912
                     /region_name="RhoGAP_OCRL1"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain present in OCRL1-like proteins.
                     OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins
                     contain two conserved domains: a central inositol
                     polyphosphate 5-phosphatase domain and...; cd04380"
                     /db_xref="CDD:239845"
     Site            order(772,807,811,874,877..878,903)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239845"
     Site            772
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239845"
     Region          910
                     /region_name="isoprenylation site"
     CDS             1..913
                     /gene="INPP5B"
                     /gene_synonym="5PTase"
                     /coded_by="NM_005540.3:91..2832"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS41306.1"
                     /db_xref="GeneID:3633"
                     /db_xref="HGNC:HGNC:6077"
                     /db_xref="MIM:147264"
ORIGIN      
        1 mdqsvaiqet laegeycvia vqgvlcegds rqsrllglvr yrlehggqeh alflythrrm
       61 aitgddvsld qivpvsrdft leevspdgel yilgsdvtvq ldtaelslvf qlpfgsqtrm
      121 flhevaracp gfdsatrdpe flwlsryrca elelemptpr gcnsalvtwp gyatiggggs
      181 nfdglrpngk gvpmdqssrg qdkpeslqpr qnkskseitd mvrsstitvs dkahilsmqk
      241 fglrdtivks hllqkeedyt yiqnfrffag tynvngqspk eclrlwlsng iqapdvycvg
      301 fqeldlskea fffhdtpkee ewfkavsegl hpdakyakvk lirlvgimll lyvkqehaay
      361 iseveaetvg tgimgrmgnk ggvairfqfh ntsicvvnsh laahieeyer rnqdykdics
      421 rmqfcqpdps lppltisnhd vilwlgdlny rieeldvekv kklieekdfq mlyaydqlki
      481 qvaaktvfeg ftegeltfqp tykydtgsdd wdtsekcrap awcdrilwkg knitqlsyqs
      541 hmalktsdhk pvssvfdigv rvvndelyrk tleeivrsld kmenanipsv slskrefcfq
      601 nvkymqlkve sftihngqvp chfefinkpd eesyckqwln anpsrgfllp dsdveidlel
      661 fvnkmtatkl nsgedkiedi lvlhldrgkd yflsvsgnyl pscfgspiht lcymrepild
      721 lpletiselt lmpvwtgddg sqldspmeip kelwmmvdyl yrnavqqedl fqqpglrsef
      781 ehirdcldtg midnlsasnh svaealllfl eslpepvicy styhnclecs gnytaskqvi
      841 stlpifhknv fhylmaflre llknsaknhl denilasifg slllrnpagh qkldmtekkk
      901 aqefihqflc npl
//
LOCUS       NP_666367                559 aa            linear   ROD 27-APR-2025
DEFINITION  excitatory amino acid transporter 5 [Mus musculus].
ACCESSION   NP_666367
VERSION     NP_666367.3
DBSOURCE    REFSEQ: accession NM_146255.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Tang,F.S., Yuan,H.L., Liu,J.B., Zhang,G., Chen,S.Y. and Ke,J.B.
  TITLE     Glutamate Transporters EAAT2 and EAAT5 Differentially Shape
            Synaptic Transmission from Rod Bipolar Cell Terminals
  JOURNAL   eNeuro 9 (3) (2022)
   PUBMED   35523583
  REMARK    GeneRIF: Glutamate Transporters EAAT2 and EAAT5 Differentially
            Shape Synaptic Transmission from Rod Bipolar Cell Terminals.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Gehlen,J., Aretzweiler,C., Mataruga,A., Fahlke,C. and Muller,F.
  TITLE     Excitatory Amino Acid Transporter EAAT5 Improves Temporal
            Resolution in the Retina
  JOURNAL   eNeuro 8 (6) (2021)
   PUBMED   34772693
  REMARK    GeneRIF: Excitatory Amino Acid Transporter EAAT5 Improves Temporal
            Resolution in the Retina.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Bligard,G.W., DeBrecht,J., Smith,R.G. and Lukasiewicz,P.D.
  TITLE     Light-evoked glutamate transporter EAAT5 activation coordinates
            with conventional feedback inhibition to control rod bipolar cell
            output
  JOURNAL   J Neurophysiol 123 (5), 1828-1837 (2020)
   PUBMED   32233906
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Reichhart,N., Schoberl,S., Keckeis,S., Alfaar,A.S., Roubeix,C.,
            Cordes,M., Crespo-Garcia,S., Haeckel,A., Kociok,N., Fockler,R.,
            Fels,G., Mataruga,A., Rauh,R., Milenkovic,V.M., Zuhlke,K.,
            Klussmann,E., Schellenberger,E. and Strauss,O.
  TITLE     Anoctamin-4 is a bona fide Ca2+-dependent non-selective cation
            channel
  JOURNAL   Sci Rep 9 (1), 2257 (2019)
   PUBMED   30783137
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Valerius,M.T. and McMahon,A.P.
  TITLE     Transcriptional profiling of Wnt4 mutant mouse kidneys identifies
            genes expressed during nephron formation
  JOURNAL   Gene Expr Patterns 8 (5), 297-306 (2008)
   PUBMED   18346943
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Wersinger,E., Schwab,Y., Sahel,J.A., Rendon,A., Pow,D.V., Picaud,S.
            and Roux,M.J.
  TITLE     The glutamate transporter EAAT5 works as a presynaptic receptor in
            mouse rod bipolar cells
  JOURNAL   J Physiol 577 (Pt 1), 221-234 (2006)
   PUBMED   16973698
  REMARK    GeneRIF: These results indicate that EAAT5 acts as a major
            inhibitory presynaptic receptor at mammalian rod bipolar cell axon
            terminals.
REFERENCE   8  (residues 1 to 559)
  AUTHORS   Hasegawa,J., Obara,T., Tanaka,K. and Tachibana,M.
  TITLE     High-density presynaptic transporters are required for glutamate
            removal from the first visual synapse
  JOURNAL   Neuron 50 (1), 63-74 (2006)
   PUBMED   16600856
REFERENCE   9  (residues 1 to 559)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   10 (residues 1 to 559)
  AUTHORS   Cooper,T.G., Wagenfeld,A., Cornwall,G.A., Hsia,N., Chu,S.T.,
            Orgebin-Crist,M.C., Drevet,J., Vernet,P., Avram,C., Nieschlag,E.
            and Yeung,C.H.
  TITLE     Gene and protein expression in the epididymis of infertile c-ros
            receptor tyrosine kinase-deficient mice
  JOURNAL   Biol Reprod 69 (5), 1750-1762 (2003)
   PUBMED   12890734
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC030400.1.
            
            On Mar 22, 2019 this sequence version replaced NP_666367.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030400.1, AK044671.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: lack of evidence for use of
                                                upstream AUG
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 50.18 cM"
     Protein         1..559
                     /product="excitatory amino acid transporter 5"
                     /note="solute carrier family 1 member 7"
                     /calculated_mol_wt=59975
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Region          19..475
                     /region_name="SDF"
                     /note="Sodium:dicarboxylate symporter family; pfam00375"
                     /db_xref="CDD:425646"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Site            216..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Site            259..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Site            329..349
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Site            413..433
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZR4.1)"
     Site            456..476
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZR4.1)"
     CDS             1..559
                     /gene="Slc1a7"
                     /gene_synonym="A930031E15Rik; Eaat5"
                     /coded_by="NM_146255.3:171..1850"
                     /db_xref="CCDS:CCDS18444.3"
                     /db_xref="GeneID:242607"
                     /db_xref="MGI:MGI:2444087"
ORIGIN      
        1 mvldavlarg rtvckhngll ilsvlsvivg cllgfflrtq rlspqeisyf qfpgellmrm
       61 lkmlilplvv sslmsglasl daktssrlgi ltvayylwtt flavvvgiim vsiihpggaa
      121 qketteqsgk pvmssadall dlvrnmfpan lveatfkqyr tkttpviksp rgaaeeaprr
      181 iviygvqedn gsrvqnfald ltpppeivyk sepgtsdgmn vlgivifsat mgimlgrmgd
      241 sgtplvsfcq clnesvmkiv avagwyfpfg ivfliagkil emddpkavgk klgfyavtvv
      301 cglvvhglli lpllyflitk knpivfirgv lqallialat ssssatlpit fkcllennhi
      361 drriarfvlp vgatinmdgt alyeavaaif iaqvnnyeld fgqiitisit ataasigaag
      421 ipqaglvtmv ivltsvglpt ddinliiavd waldrfrtmi nvlgdalaag imahicrkdf
      481 aqdmgtekll pcetkpvtlq eivaaqqngc vksvaeasel tlgptcphhi pvqveqdedp
      541 aaasldhcti eiseletnv
//
LOCUS       NP_005555                198 aa            linear   PRI 27-APR-2025
DEFINITION  neutrophil gelatinase-associated lipocalin precursor [Homo
            sapiens].
ACCESSION   NP_005555
VERSION     NP_005555.2
DBSOURCE    REFSEQ: accession NM_005564.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Huang,Z., Li,Y., Qian,Y., Zhai,E., Zhao,Z., Zhang,T., Liu,Y.,
            Ye,L., Wei,R., Zhao,R., Li,Z., Liang,Z., Cai,S. and Chen,J.
  TITLE     Tumor-secreted LCN2 impairs gastric cancer progression via
            autocrine inhibition of the 24p3R/JNK/c-Jun/SPARC axis
  JOURNAL   Cell Death Dis 15 (10), 756 (2024)
   PUBMED   39424639
  REMARK    GeneRIF: Tumor-secreted LCN2 impairs gastric cancer progression via
            autocrine inhibition of the 24p3R/JNK/c-Jun/SPARC axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Yang,Y., Li,S., Liu,K., Zhang,Y., Zhu,F., Ben,T., Chen,Z. and
            Zhi,F.
  TITLE     Lipocalin-2-mediated intestinal epithelial cells pyroptosis via
            NF-kappaB/NLRP3/GSDMD signaling axis adversely affects inflammation
            in colitis
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (7), 167279 (2024)
   PUBMED   38844113
  REMARK    GeneRIF: Lipocalin-2-mediated intestinal epithelial cells
            pyroptosis via NF-kappaB/NLRP3/GSDMD signaling axis adversely
            affects inflammation in colitis.
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Qiu,R., Cai,Y., Su,Y., Fan,K., Sun,Z. and Zhang,Y.
  TITLE     Emerging insights into Lipocalin-2: Unraveling its role in
            Parkinson's Disease
  JOURNAL   Biomed Pharmacother 177, 116947 (2024)
   PUBMED   38901198
  REMARK    GeneRIF: Emerging insights into Lipocalin-2: Unraveling its role in
            Parkinson's Disease.
            Review article
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Olar,M.P., Iacobescu,M., Bolboaca,S.D., Pojoga,C., Mosteanu,O.,
            Seicean,R., Rusu,I., Banc,O., Iuga,C.A. and Seicean,A.
  TITLE     Neutrophil Gelatinase-Associated Lipocalin for the Differentiation
            of Mucinous Pancreatic Cystic Lesions
  JOURNAL   Int J Mol Sci 25 (6), 3224 (2024)
   PUBMED   38542201
  REMARK    GeneRIF: Neutrophil Gelatinase-Associated Lipocalin for the
            Differentiation of Mucinous Pancreatic Cystic Lesions.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Paparella,R., Ferraguti,G., Fiore,M., Menghi,M., Micangeli,G.,
            Tarani,F., Ligotino,A., Messina,M.P., Ceccanti,M., Minni,A.,
            Barbato,C., Lucarelli,M., Tarani,L. and Petrella,C.
  TITLE     Serum Lipocalin-2 Levels as a Biomarker in Pre- and Post-Pubertal
            Klinefelter Syndrome Patients: A Pilot Study
  JOURNAL   Int J Mol Sci 25 (4), 2214 (2024)
   PUBMED   38396890
  REMARK    GeneRIF: Serum Lipocalin-2 Levels as a Biomarker in Pre- and
            Post-Pubertal Klinefelter Syndrome Patients: A Pilot Study.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Cowland,J.B. and Borregaard,N.
  TITLE     Molecular characterization and pattern of tissue expression of the
            gene for neutrophil gelatinase-associated lipocalin from humans
  JOURNAL   Genomics 45 (1), 17-23 (1997)
   PUBMED   9339356
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Blaser,J., Triebel,S. and Tschesche,H.
  TITLE     A sandwich enzyme immunoassay for the determination of neutrophil
            lipocalin in body fluids
  JOURNAL   Clin Chim Acta 235 (2), 137-145 (1995)
   PUBMED   7554268
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Chan,P., Simon-Chazottes,D., Mattei,M.G., Guenet,J.L. and
            Salier,J.P.
  TITLE     Comparative mapping of lipocalin genes in human and mouse: the four
            genes for complement C8 gamma chain, prostaglandin-D-synthase,
            oncogene-24p3, and progestagen-associated endometrial protein map
            to HSA9 and MMU2
  JOURNAL   Genomics 23 (1), 145-150 (1994)
   PUBMED   7829063
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Kjeldsen,L., Johnsen,A.H., Sengelov,H. and Borregaard,N.
  TITLE     Isolation and primary structure of NGAL, a novel protein associated
            with human neutrophil gelatinase
  JOURNAL   J Biol Chem 268 (14), 10425-10432 (1993)
   PUBMED   7683678
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Triebel,S., Blaser,J., Reinke,H. and Tschesche,H.
  TITLE     A 25 kDa alpha 2-microglobulin-related protein is a component of
            the 125 kDa form of human gelatinase
  JOURNAL   FEBS Lett 314 (3), 386-388 (1992)
   PUBMED   1281792
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX644845.1, BC033089.1 and
            BM977724.1.
            
            On Nov 20, 2003 this sequence version replaced NP_005555.1.
            
            Summary: This gene encodes a protein that belongs to the lipocalin
            family. Members of this family transport small hydrophobic
            molecules such as lipids, steroid hormones and retinoids. The
            protein encoded by this gene is a neutrophil gelatinase-associated
            lipocalin and plays a role in innate immunity by limiting bacterial
            growth as a result of sequestering iron-containing siderophores.
            The presence of this protein in blood and urine is an early
            biomarker of acute kidney injury. This protein is thought to be be
            involved in multiple cellular processes, including maintenance of
            skin homeostasis, and suppression of invasiveness and metastasis.
            Mice lacking this gene are more susceptible to bacterial infection
            than wild type mice. [provided by RefSeq, Sep 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ686961.1, BU196396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000277480.7/ ENSP00000277480.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..198
                     /product="neutrophil gelatinase-associated lipocalin
                     precursor"
                     /note="oncogene 24p3; neutrophil gelatinase-associated
                     lipocalin; migration-stimulating factor inhibitor; 25 kDa
                     alpha-2-microglobulin-related subunit of MMP-9;
                     siderocalin LCN2"
                     /calculated_mol_wt=20548
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2059
     mat_peptide     21..198
                     /product="Neutrophil gelatinase-associated lipocalin.
                     /id=PRO_0000017933"
                     /note="propagated from UniProtKB/Swiss-Prot (P80188.2)"
                     /calculated_mol_wt=20548
     Site            21
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:7683678; propagated from
                     UniProtKB/Swiss-Prot (P80188.2)"
     Region          24..196
                     /region_name="lipocalin_2-like"
                     /note="lipocalin 2 and similar proteins; cd19457"
                     /db_xref="CDD:381232"
     Site            order(47,51,53,60..61,72,74,76,84,86,88,90..92,99,101,103,
                     112,114,126,128,130,139,141,143,145,152..154,156,158)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381232"
     Site            85
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:10684642,
                     ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:7683678, ECO:0007744|PDB:1DFV,
                     ECO:0007744|PDB:1QQS; propagated from UniProtKB/Swiss-Prot
                     (P80188.2)"
     CDS             1..198
                     /gene="LCN2"
                     /gene_synonym="24p3; MSFI; NGAL; p25"
                     /coded_by="NM_005564.5:74..670"
                     /db_xref="CCDS:CCDS6892.1"
                     /db_xref="GeneID:3934"
                     /db_xref="HGNC:HGNC:6526"
                     /db_xref="MIM:600181"
ORIGIN      
        1 mplgllwlgl allgalhaqa qdstsdlipa pplskvplqq nfqdnqfqgk wyvvglagna
       61 ilredkdpqk myatiyelke dksynvtsvl frkkkcdywi rtfvpgcqpg eftlgniksy
      121 pgltsylvrv vstnynqham vffkkvsqnr eyfkitlygr tkeltselke nfirfskslg
      181 lpenhivfpv pidqcidg
//
LOCUS       NP_004281                474 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF14 isoform 1 [Homo sapiens].
ACCESSION   NP_004281
VERSION     NP_004281.1
DBSOURCE    REFSEQ: accession NM_004290.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Zhao,S., Cordes,J., Caban,K.M., Gotz,M.J., Mackens-Kiani,T.,
            Veltri,A.J., Sinha,N.K., Weickert,P., Kaya,S., Hewitt,G.,
            Nedialkova,D.D., Frohlich,T., Beckmann,R., Buskirk,A.R., Green,R.
            and Stingele,J.
  TITLE     RNF14-dependent atypical ubiquitylation promotes
            translation-coupled resolution of RNA-protein crosslinks
  JOURNAL   Mol Cell 83 (23), 4290-4303 (2023)
   PUBMED   37951216
  REMARK    GeneRIF: RNF14-dependent atypical ubiquitylation promotes
            translation-coupled resolution of RNA-protein crosslinks.
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Suryo Rahmanto,A., Blum,C.J., Scalera,C., Heidelberger,J.B.,
            Mesitov,M., Horn-Ghetko,D., Graf,J.F., Mikicic,I., Hobrecht,R.,
            Orekhova,A., Ostermaier,M., Ebersberger,S., Mockel,M.M.,
            Krapoth,N., Da Silva Fernandes,N., Mizi,A., Zhu,Y., Chen,J.X.,
            Choudhary,C., Papantonis,A., Ulrich,H.D., Schulman,B.A., Konig,J.
            and Beli,P.
  TITLE     K6-linked ubiquitylation marks formaldehyde-induced RNA-protein
            crosslinks for resolution
  JOURNAL   Mol Cell 83 (23), 4272-4289 (2023)
   PUBMED   37951215
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Gurzeler,L.A., Link,M., Ibig,Y., Schmidt,I., Galuba,O.,
            Schoenbett,J., Gasser-Didierlaurant,C., Parker,C.N., Mao,X.,
            Bitsch,F., Schirle,M., Couttet,P., Sigoillot,F., Ziegelmuller,J.,
            Uldry,A.C., Teodorowicz,W., Schmiedeberg,N., Muhlemann,O. and
            Reinhardt,J.
  TITLE     Drug-induced eRF1 degradation promotes readthrough and reveals a
            new branch of ribosome quality control
  JOURNAL   Cell Rep 42 (9), 113056 (2023)
   PUBMED   37651229
  REMARK    Erratum:[Cell Rep. 2023 Sep 26;42(9):113159. doi:
            10.1016/j.celrep.2023.113159. PMID: 37708027]
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Oltion,K., Carelli,J.D., Yang,T., See,S.K., Wang,H.Y., Kampmann,M.
            and Taunton,J.
  TITLE     An E3 ligase network engages GCN1 to promote the degradation of
            translation factors on stalled ribosomes
  JOURNAL   Cell 186 (2), 346-362 (2023)
   PUBMED   36638793
REFERENCE   5  (residues 1 to 474)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 474)
  AUTHORS   Miyamoto,H., Rahman,M., Takatera,H., Kang,H.Y., Yeh,S., Chang,H.C.,
            Nishimura,K., Fujimoto,N. and Chang,C.
  TITLE     A dominant-negative mutant of androgen receptor coregulator ARA54
            inhibits androgen receptor-mediated prostate cancer growth
  JOURNAL   J Biol Chem 277 (7), 4609-4617 (2002)
   PUBMED   11673464
  REMARK    GeneRIF: dominant-negative AR coregulator can suppress AR
            transactivation and cell proliferation in prostate cancer cells
REFERENCE   7  (residues 1 to 474)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
REFERENCE   8  (residues 1 to 474)
  AUTHORS   Ueki,N., Seki,N., Yano,K., Masuho,Y., Saito,T. and Muramatsu,M.
  TITLE     Isolation and characterization of a novel human gene (HFB30) which
            encodes a protein with a RING finger motif
  JOURNAL   Biochim Biophys Acta 1445 (2), 232-236 (1999)
   PUBMED   10320776
REFERENCE   9  (residues 1 to 474)
  AUTHORS   Kang,H.Y., Yeh,S., Fujimoto,N. and Chang,C.
  TITLE     Cloning and characterization of human prostate coactivator ARA54, a
            novel protein that associates with the androgen receptor
  JOURNAL   J Biol Chem 274 (13), 8570-8576 (1999)
   PUBMED   10085091
REFERENCE   10 (residues 1 to 474)
  AUTHORS   Ueki,N., Oda,T., Kondo,M., Yano,K., Noguchi,T. and Muramatsu,M.
  TITLE     Selection system for genes encoding nuclear-targeted proteins
  JOURNAL   Nat Biotechnol 16 (13), 1338-1342 (1998)
   PUBMED   9853615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC402536.1, AF060544.1,
            AC005740.1 and BE042895.1.
            
            Summary: The protein encoded by this gene contains a RING zinc
            finger, a motif known to be involved in protein-protein
            interactions. This protein interacts with androgen receptor (AR)
            and may function as a coactivator that induces AR target gene
            expression in prostate. A dominant negative mutant of this gene has
            been demonstrated to inhibit the AR-mediated growth of prostate
            cancer. This protein also interacts with class III
            ubiquitin-conjugating enzymes (E2s) and may act as a
            ubiquitin-ligase (E3) in the ubiquitination of certain nuclear
            proteins. Six alternatively spliced transcript variants encoding
            two distinct isoforms have been reported. [provided by RefSeq, Jan
            2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.229101.1,
                                           SRR1660807.228946.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394520.7/ ENSP00000378028.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..474
                     /product="E3 ubiquitin-protein ligase RNF14 isoform 1"
                     /EC_number="2.3.2.31"
                     /note="androgen receptor associated protein 54; E3
                     ubiquitin-protein ligase RNF14"
                     /calculated_mol_wt=53707
     Region          9..135
                     /region_name="RWD_RNF14"
                     /note="RWD domain of RING finger protein 14 (RNF14) and
                     related proteins; cd23820"
                     /db_xref="CDD:467656"
     Region          37..45
                     /region_name="D-box.
                     /evidence=ECO:0000269|PubMed:11322894"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBS8.1)"
     Region          213..271
                     /region_name="RING-HC_RBR_RNF14"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 14 (RNF14) and similar proteins; cd16628"
                     /db_xref="CDD:438290"
     Region          216..457
                     /region_name="TRIAD supradomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBS8.1)"
     Region          300..356
                     /region_name="BRcat_RBR_RNF14"
                     /note="BRcat domain found in RING finger protein 14
                     (RNF14); cd20341"
                     /db_xref="CDD:439002"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBS8.1)"
     Region          361..474
                     /region_name="Interaction with androgen receptor.
                     /evidence=ECO:0000269|PubMed:19345326"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBS8.1)"
     Region          389..456
                     /region_name="Rcat_RBR_RNF14"
                     /note="Rcat domain found in RING finger protein 14
                     (RNF14); cd20354"
                     /db_xref="CDD:439015"
     CDS             1..474
                     /gene="RNF14"
                     /gene_synonym="ARA54; HFB30; HRIHFB2038; TRIAD2"
                     /coded_by="NM_004290.5:244..1668"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4270.1"
                     /db_xref="GeneID:9604"
                     /db_xref="HGNC:HGNC:10058"
                     /db_xref="MIM:605675"
ORIGIN      
        1 mssedreaqe dellalasiy dgdefrkaes vqggetriyl dlpqnfkifv sgnsneclqn
       61 sgfeyticfl pplvlnfelp pdypssspps ftlsgkwlsp tqlsalckhl dnlweehrgs
      121 vvlfawmqfl keetlaylni vspfelkigs qkkvqrrtaq aspnteldfg gaagsdvdqe
      181 eivderavqd veslsnliqe ildfdqaqqi kcfnsklflc sicfceklgs ecmyflecrh
      241 vyckaclkdy feiqirdgqv qclncpepkc psvatpgqvk elveaelfar ydrlllqssl
      301 dlmadvvycp rpccqlpvmq epgctmgics scnfafctlc rltyhgvspc kvtaeklmdl
      361 rneylqadea nkrlldqryg krviqkalee meskewlekn skscpccgtp iekldgcnkm
      421 tctgcmqyfc wicmgslsra npykhfndpg spcfnrlfya vdvdddiwed eved
//
LOCUS       NP_001094299             132 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 170B [Homo sapiens].
ACCESSION   NP_001094299
VERSION     NP_001094299.1
DBSOURCE    REFSEQ: accession NM_001100829.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Kang,C., Duo,Y., Zheng,L., Zhao,N., Wang,J., Liu,Z., Qiu,L. and
            Bi,F.
  TITLE     CAFs-derived exosomes promote the development of cervical cancer by
            regulating miR-18a-5p-TMEM170B signaling axis
  JOURNAL   Biochem Biophys Res Commun 694, 149403 (2024)
   PUBMED   38147699
  REMARK    GeneRIF: CAFs-derived exosomes promote the development of cervical
            cancer by regulating miR-18a-5p-TMEM170B signaling axis.
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Li,M., Han,Y., Zhou,H., Li,X., Lin,C., Zhang,E., Chi,X., Hu,J. and
            Xu,H.
  TITLE     Transmembrane protein 170B is a novel breast tumorigenesis
            suppressor gene that inhibits the Wnt/beta-catenin pathway
  JOURNAL   Cell Death Dis 9 (2), 91 (2018)
   PUBMED   29367600
  REMARK    GeneRIF: these results highlight TMEM170B as a novel tumor
            suppressor target in association with the beta-catenin pathway.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL357518.15, DB092520.1 and BE670213.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.80081.1,
                                           SRR1803615.488209.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379426.2/ ENSP00000368737.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.2"
     Protein         1..132
                     /product="transmembrane protein 170B"
                     /calculated_mol_wt=14229
     Site            12
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5T4T1.1)"
     Region          28..132
                     /region_name="Tmemb_170"
                     /note="Putative transmembrane protein 170; pfam10190"
                     /db_xref="CDD:462988"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T4T1.1)"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T4T1.1)"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T4T1.1)"
     CDS             1..132
                     /gene="TMEM170B"
                     /coded_by="NM_001100829.3:530..928"
                     /db_xref="CCDS:CCDS43425.1"
                     /db_xref="GeneID:100113407"
                     /db_xref="HGNC:HGNC:34244"
ORIGIN      
        1 mkaeggdhsm inlsvqqvls lwahgtvlrn ltemwywifl walfsslfvh gaagvlmfvm
       61 lqrhrqgrvi sviavsigfl asvtgamits aavagiyrva gknmapleal vwgvgqtvlt
      121 liisfsrila tl
//
LOCUS       NP_057340                515 aa            linear   PRI 27-APR-2025
DEFINITION  N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
            precursor [Homo sapiens].
ACCESSION   NP_057340
VERSION     NP_057340.2
DBSOURCE    REFSEQ: accession NM_016256.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Carmona,E.G., Garcia-Gimenez,J.A., Lopez-Mejias,R., Khor,C.C.,
            Lee,J.K., Taskiran,E., Ozen,S., Hocevar,A., Liu,L., Gorenjak,M.,
            Potocnik,U., Kiryluk,K., Ortego-Centeno,N., Cid,M.C.,
            Hernandez-Rodriguez,J., Castaneda,S., Gonzalez-Gay,M.A.,
            Burgner,D., Martin,J. and Marquez,A.
  CONSRTM   Spanish IgA Vasculitis Consortium;* International Kawasaki Disease
            Genetics Consortium
  TITLE     Identification of a shared genetic risk locus for Kawasaki disease
            and immunoglobulin A vasculitis by a cross-phenotype meta-analysis
  JOURNAL   Rheumatology (Oxford) 61 (3), 1204-1210 (2022)
   PUBMED   33993232
  REMARK    GeneRIF: Identification of a shared genetic risk locus for Kawasaki
            disease and immunoglobulin A vasculitis by a cross-phenotype
            meta-analysis.
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Gorelik,A., Illes,K. and Nagar,B.
  TITLE     Crystal Structure of the Mannose-6-Phosphate Uncovering Enzyme
  JOURNAL   Structure 28 (4), 426-436 (2020)
   PUBMED   32109365
  REMARK    GeneRIF: Crystal Structure of the Mannose-6-Phosphate Uncovering
            Enzyme.
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Frigerio-Domingues,C.E., Gkalitsiou,Z., Zezinka,A., Sainz,E.,
            Gutierrez,J., Byrd,C., Webster,R. and Drayna,D.
  TITLE     Genetic factors and therapy outcomes in persistent developmental
            stuttering
  JOURNAL   J Commun Disord 80, 11-17 (2019)
   PUBMED   31003007
  REMARK    GeneRIF: We evaluated 51 stuttering individuals with a mutation in
            either the GNPTAB, GNPTG, NAGPA, or AP4E1 gene. Mutation carriers
            achieved significantly less resolution in PSI following therapy,
            with PSI scores showing significantly less improvement in
            individuals who carry a mutation (p = 0.0157, RR = 1.75, OR = 2.92)
            while the group difference in DWS between carriers and non-carriers
            was statistically not significant.
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Kazemi,N., Estiar,M.A., Fazilaty,H. and Sakhinia,E.
  TITLE     Variants in GNPTAB, GNPTG and NAGPA genes are associated with
            stutterers
  JOURNAL   Gene 647, 93-100 (2018)
   PUBMED   29289611
  REMARK    GeneRIF: 14 variations were found in GNPTAB, GNPTG and NAGPA genes.
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Kang,C. and Drayna,D.
  TITLE     A role for inherited metabolic deficits in persistent developmental
            stuttering
  JOURNAL   Mol Genet Metab 107 (3), 276-280 (2012)
   PUBMED   22884963
  REMARK    GeneRIF: To date mutations in GNPTAB, GNPTG, and NAGPA have been
            associated with stuttering. These genes encode the lysosomal enzyme
            targeting pathway, defective in mucolipidosis. (Review)
            Review article
REFERENCE   6  (residues 1 to 515)
  AUTHORS   Lee,W.S., Rohrer,J., Kornfeld,R. and Kornfeld,S.
  TITLE     Multiple signals regulate trafficking of the mannose
            6-phosphate-uncovering enzyme
  JOURNAL   J Biol Chem 277 (5), 3544-3551 (2002)
   PUBMED   11723124
REFERENCE   7  (residues 1 to 515)
  AUTHORS   Rohrer,J. and Kornfeld,R.
  TITLE     Lysosomal hydrolase mannose 6-phosphate uncovering enzyme resides
            in the trans-Golgi network
  JOURNAL   Mol Biol Cell 12 (6), 1623-1631 (2001)
   PUBMED   11408573
REFERENCE   8  (residues 1 to 515)
  AUTHORS   Kornfeld,R., Bao,M., Brewer,K., Noll,C. and Canfield,W.
  TITLE     Molecular cloning and functional expression of two splice forms of
            human N-acetylglucosamine-1-phosphodiester
            alpha-N-acetylglucosaminidase
  JOURNAL   J Biol Chem 274 (46), 32778-32785 (1999)
   PUBMED   10551838
REFERENCE   9  (residues 1 to 515)
  AUTHORS   Page,T., Zhao,K.W., Tao,L. and Miller,A.L.
  TITLE     Purification and characterization of human lymphoblast
            N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
  JOURNAL   Glycobiology 6 (6), 619-626 (1996)
   PUBMED   8922957
REFERENCE   10 (residues 1 to 515)
  AUTHORS   Lee,J.K. and Pierce,M.
  TITLE     Purification and characterization of human serum
            N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
  JOURNAL   Arch Biochem Biophys 319 (2), 413-425 (1995)
   PUBMED   7786023
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA879815.1, AK025570.1 and
            AC026458.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 19, 2005 this sequence version replaced NP_057340.1.
            
            Summary: Hydrolases are transported to lysosomes after binding to
            mannose 6-phosphate receptors in the trans-Golgi network. This gene
            encodes the enzyme that catalyzes the second step in the formation
            of the mannose 6-phosphate recognition marker on lysosomal
            hydrolases. Commonly known as 'uncovering enzyme' or UCE, this
            enzyme removes N-acetyl-D-glucosamine (GlcNAc) residues from
            GlcNAc-alpha-P-mannose moieties and thereby produces the
            recognition marker. The encoded preproprotein is proteolytically
            processed by furin to generate the mature enzyme, a homotetramer of
            two disulfide-linked homodimers. Mutations in this gene are
            associated with developmental stuttering in human patients.
            [provided by RefSeq, Oct 2015].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127952.1, AK314320.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312251.8/ ENSP00000310998.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..515
                     /product="N-acetylglucosamine-1-phosphodiester
                     alpha-N-acetylglucosaminidase precursor"
                     /EC_number="3.1.4.45"
                     /note="phosphodiester alpha-GlcNAcase;
                     alpha-N-acetylglucosaminyl phosphodiesterase; lysosomal
                     alpha-N-acetylglucosaminidase; mannose
                     6-phosphate-uncovering enzyme"
                     /calculated_mol_wt=53337
     sig_peptide     1..25
                     /note="/evidence=ECO:0000269|PubMed:12058031; propagated
                     from UniProtKB/Swiss-Prot (Q9UK23.2)"
                     /calculated_mol_wt=2754
     mat_peptide     50..515
                     /product="N-acetylglucosamine-1-phosphodiester
                     alpha-N-acetylglucosaminidase. /id=PRO_0000021788"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK23.2)"
                     /calculated_mol_wt=50631
     Region          137..325
                     /region_name="NAGPA"
                     /note="Phosphodiester glycosidase; pfam09992"
                     /db_xref="CDD:430971"
     Site            208
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UK23.2)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UK23.2)"
     Site            296
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UK23.2)"
     Site            366
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UK23.2)"
     Site            388
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UK23.2)"
     Site            420
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UK23.2)"
     Site            449..469
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK23.2)"
     Region          486..493
                     /region_name="Mediates the interaction with AP4M1.
                     /evidence=ECO:0000269|PubMed:26544806"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK23.2)"
     Region          488..491
                     /region_name="Tyrosine-based internalization motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK23.2)"
     Region          511..515
                     /region_name="NPF internalization motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK23.2)"
     CDS             1..515
                     /gene="NAGPA"
                     /gene_synonym="APAA; UCE"
                     /coded_by="NM_016256.4:22..1569"
                     /db_xref="CCDS:CCDS10527.1"
                     /db_xref="GeneID:51172"
                     /db_xref="HGNC:HGNC:17378"
                     /db_xref="MIM:607985"
ORIGIN      
        1 matstgrwll lrlalfgflw easggldsga srdddlllpy prararlprd ctrvragnre
       61 heswppppat pgagglavrt fvshfrdrav aghltravep lrtfsvlepg gpggcaarrr
      121 atveetaraa dcrvaqnggf frmnsgeclg nvvsderrvs ssgglqnaqf girrdgtlvt
      181 gylseeevld tenpfvqlls gvvwlirngs iyinesqate cdetqetgsf skfvnvisar
      241 taighdrkgq lvlfhadgqt eqrginlwem aefllkqdvv nainldgggs atfvlngtla
      301 sypsdhcqdn mwrcprqvst vvcvheprcq ppdchghgtc vdghcqctgh fwrgpgcdel
      361 dcgpsncsqh glctetgcrc dagwtgsncs eecplgwhgp gcqrpckceh hcpcdpktgn
      421 csvsrvkqcl qppeatlrag elsfftrtaw laltlalafl llistaanls lllsraernr
      481 rlhgdyayhp lqemngepla aekeqpggah npfkd
//
LOCUS       NP_002255                538 aa            linear   PRI 27-APR-2025
DEFINITION  importin subunit alpha-5 [Homo sapiens].
ACCESSION   NP_002255
VERSION     NP_002255.3
DBSOURCE    REFSEQ: accession NM_002264.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Zhao,L., Wu,D., Qu,Q., Li,Z. and Yin,H.
  TITLE     Karyopherin Subunit Alpha 1 Enhances the Malignant Behaviors of
            Colon Cancer Cells via Promoting Nuclear Factor-kappaB p65 Nuclear
            Translocation
  JOURNAL   Dig Dis Sci 68 (7), 3018-3031 (2023)
   PUBMED   37038032
  REMARK    GeneRIF: Karyopherin Subunit Alpha 1 Enhances the Malignant
            Behaviors of Colon Cancer Cells via Promoting Nuclear Factor-kappaB
            p65 Nuclear Translocation.
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Jiang,L., Li,D., Wang,C., Liao,J., Liu,J., Wei,Q. and Wang,Y.
  TITLE     Decreased Expression of Karyopherin-alpha 1 is Related to the
            Malignant Degree of Cervical Cancer and is Critical for the
            Proliferation of Hela Cells
  JOURNAL   Pathol Oncol Res 28, 1610518 (2022)
   PUBMED   35991835
  REMARK    GeneRIF: Decreased Expression of Karyopherin-alpha 1 is Related to
            the Malignant Degree of Cervical Cancer and is Critical for the
            Proliferation of Hela Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Tsoi,H., Man,E.P., Leung,M.H., Mok,K.C., Chau,K.M., Wong,L.S.,
            Chan,W.L., Chan,S.Y., Luk,M.Y., Cheng,C.N. and Khoo,U.S.
  TITLE     KPNA1 regulates nuclear import of NCOR2 splice variant BQ323636.1
            to confer tamoxifen resistance in breast cancer
  JOURNAL   Clin Transl Med 11 (10), e554 (2021)
   PUBMED   34709749
  REMARK    GeneRIF: KPNA1 regulates nuclear import of NCOR2 splice variant
            BQ323636.1 to confer tamoxifen resistance in breast cancer.
REFERENCE   5  (residues 1 to 538)
  AUTHORS   de Oliveira,H.C., da Silva,T.D., Salvador,G.H.M., Moraes,I.R.,
            Fukuda,C.A., de Barros,A.C. and Fontes,M.R.M.
  TITLE     Structural and calorimetric studies reveal specific determinants
            for the binding of a high-affinity NLS to mammalian importin-alpha
  JOURNAL   Biochem J 478 (13), 2715-2732 (2021)
   PUBMED   34195786
  REMARK    GeneRIF: Structural and calorimetric studies reveal specific
            determinants for the binding of a high-affinity NLS to mammalian
            importin-alpha.
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Di Marzio,P., Choe,S., Ebright,M., Knoblauch,R. and Landau,N.R.
  TITLE     Mutational analysis of cell cycle arrest, nuclear localization and
            virion packaging of human immunodeficiency virus type 1 Vpr
  JOURNAL   J Virol 69 (12), 7909-7916 (1995)
   PUBMED   7494303
REFERENCE   7  (residues 1 to 538)
  AUTHORS   O'Neill,R.E., Jaskunas,R., Blobel,G., Palese,P. and Moroianu,J.
  TITLE     Nuclear import of influenza virus RNA can be mediated by viral
            nucleoprotein and transport factors required for protein import
  JOURNAL   J Biol Chem 270 (39), 22701-22704 (1995)
   PUBMED   7559393
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Bukrinsky,M.I., Sharova,N., Dempsey,M.P., Stanwick,T.L.,
            Bukrinskaya,A.G., Haggerty,S. and Stevenson,M.
  TITLE     Active nuclear import of human immunodeficiency virus type 1
            preintegration complexes
  JOURNAL   Proc Natl Acad Sci U S A 89 (14), 6580-6584 (1992)
   PUBMED   1631159
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Sharova,N. and Bukrinskaya,A.
  TITLE     p17 and p17-containing gag precursors of input human
            immunodeficiency virus are transported into the nuclei of infected
            cells
  JOURNAL   AIDS Res Hum Retroviruses 7 (3), 303-306 (1991)
   PUBMED   2064827
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Mukaigawa,J. and Nayak,D.P.
  TITLE     Two signals mediate nuclear localization of influenza virus
            (A/WSN/33) polymerase basic protein 2
  JOURNAL   J Virol 65 (1), 245-253 (1991)
   PUBMED   1985200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA308391.1, U20620.1,
            BC003009.1 and AC083798.14.
            
            On Jan 30, 2009 this sequence version replaced NP_002255.2.
            
            Summary: The transport of molecules between the nucleus and the
            cytoplasm in eukaryotic cells is mediated by the nuclear pore
            complex (NPC), which consists of 60-100 proteins. Small molecules
            (up to 70 kD) can pass through the nuclear pore by nonselective
            diffusion while larger molecules are transported by an active
            process. The protein encoded by this gene belongs to the importin
            alpha family, and is involved in nuclear protein import. This
            protein interacts with the recombination activating gene 1 (RAG1)
            protein and is a putative substrate of the RAG1 ubiquitin ligase.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) lacks an alternate exon
            compared to variant 2 and represents the protein-coding transcript.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.80941.1,
                                           SRR1803616.269053.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344337.11/ ENSP00000343701.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.1"
     Protein         1..538
                     /product="importin subunit alpha-5"
                     /note="importin-alpha-S1; importin alpha 5; importin
                     subunit alpha-1; recombination activating gene cohort 2;
                     nucleoprotein interactor 1; SRP1-beta; RAG cohort protein
                     2; karyopherin alpha 1 (importin alpha 5)"
                     /calculated_mol_wt=60091
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P52294.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in Importin subunit alpha-5,
                     N-terminally processed.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P52294.3)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52294.3)"
     Region          33..516
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          42..51
                     /region_name="nuclear localization signal"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P52294.3)"
     Region          77..117
                     /region_name="ARM 1, truncated"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          118..161
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          128..154
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(145,149,153,187,191,195,230,234,238)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          149..241
                     /region_name="NLS binding site (major).
                     /evidence=ECO:0000250|UniProtKB:P52293"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          162..198
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          204..239
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          207..245
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          245..437
                     /region_name="Binding to RAG1.
                     /evidence=ECO:0000269|PubMed:8052633"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          256..281
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          289..325
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          318..406
                     /region_name="NLS binding site (minor).
                     /evidence=ECO:0000250|UniProtKB:P52293"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Site            order(356,360,364,398,402,406,441,445,449)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          373..409
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          413..457
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          416..450
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          460..504
                     /region_name="ARM 10, atypical"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     CDS             1..538
                     /gene="KPNA1"
                     /gene_synonym="IPOA5; NPI-1; RCH2; SRP1"
                     /coded_by="NM_002264.4:189..1805"
                     /db_xref="CCDS:CCDS3013.1"
                     /db_xref="GeneID:3836"
                     /db_xref="HGNC:HGNC:6394"
                     /db_xref="MIM:600686"
ORIGIN      
        1 mttpgkenfr lksyknksln pdemrrrree eglqlrkqkr eeqlfkrrnv ataeeeteee
       61 vmsdggfhea qisnmemapg gvitsdmiem ifskspeqql satqkfrkll skepnppide
      121 vistpgvvar fveflkrken ctlqfesawv ltniasgnsl qtriviqaga vpifiellss
      181 efedvqeqav walgniagds tmcrdyvldc nilppllqlf skqnrltmtr navwalsnlc
      241 rgkspppefa kvspclnvls wllfvsdtdv ladacwalsy lsdgpndkiq avidagvcrr
      301 lvellmhndy kvvspalrav gnivtgddiq tqvilncsal qsllhllssp kesikkeacw
      361 tisnitagnr aqiqtvidan ifpalisilq taefrtrkea awaitnatsg gsaeqikylv
      421 elgcikplcd lltvmdskiv qvalngleni lrlgeqeakr ngtginpyca lieeaygldk
      481 ieflqshenq eiyqkafdli ehyfgteded ssiapqvdln qqqyifqqce apmegfql
//
LOCUS       NP_002109                263 aa            linear   PRI 27-APR-2025
DEFINITION  HLA class II histocompatibility antigen, DM beta chain precursor
            [Homo sapiens].
ACCESSION   NP_002109
VERSION     NP_002109.2
DBSOURCE    REFSEQ: accession NM_002118.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Suarez-Trujillo,F., Juarez,I., Jose Recio-Hoyas,M., Rey,D.,
            Palacio-Gruber,J., Gil-Martin,R., Manuel Martin-Villa,J. and
            Arnaiz-Villena,A.
  TITLE     HLA-DMB alleles and haplotypes in Ecuador (Cuenca) Amerindians:
            Importance for HLA and disease studies
  JOURNAL   Hum Immunol 84 (4), 261-262 (2023)
   PUBMED   36870854
  REMARK    GeneRIF: HLA-DMB alleles and haplotypes in Ecuador (Cuenca)
            Amerindians: Importance for HLA and disease studies.
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Yin,L., Maben,Z.J., Becerra,A. and Stern,L.J.
  TITLE     Evaluating the Role of HLA-DM in MHC Class II-Peptide Association
            Reactions
  JOURNAL   J Immunol 195 (2), 706-716 (2015)
   PUBMED   26062997
  REMARK    GeneRIF: This study provides novel insights into how HLA-DM
            efficiently catalyzes peptide loading during antigen presentation.
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Aissani,B., Boehme,A.K., Wiener,H.W., Shrestha,S., Jacobson,L.P.
            and Kaslow,R.A.
  TITLE     SNP screening of central MHC-identified HLA-DMB as a candidate
            susceptibility gene for HIV-related Kaposi's sarcoma
  JOURNAL   Genes Immun 15 (6), 424-429 (2014)
   PUBMED   25008864
  REMARK    GeneRIF: Data suggest that antigen processing by MHC class II
            HLA-DMB antigen is a target pathway in the pathogenesis of
            HIV-related Kaposi's sarcoma.
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Sherman,M.A., Weber,D.A. and Jensen,P.E.
  TITLE     DM enhances peptide binding to class II MHC by release of invariant
            chain-derived peptide
  JOURNAL   Immunity 3 (2), 197-205 (1995)
   PUBMED   7648393
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Denzin,L.K. and Cresswell,P.
  TITLE     HLA-DM induces CLIP dissociation from MHC class II alpha beta
            dimers and facilitates peptide loading
  JOURNAL   Cell 82 (1), 155-165 (1995)
   PUBMED   7606781
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Shaman,J., von Scheven,E., Morris,P., Chang,M.D. and Mellins,E.
  TITLE     Analysis of HLA-DMB mutants and -DMB genomic structure
  JOURNAL   Immunogenetics 41 (2-3), 117-124 (1995)
   PUBMED   7528727
REFERENCE   9  (residues 1 to 263)
  AUTHORS   Radley,E., Alderton,R.P., Kelly,A., Trowsdale,J. and Beck,S.
  TITLE     Genomic organization of HLA-DMA and HLA-DMB. Comparison of the gene
            organization of all six class II families in the human major
            histocompatibility complex
  JOURNAL   J Biol Chem 269 (29), 18834-18838 (1994)
   PUBMED   8034636
REFERENCE   10 (residues 1 to 263)
  AUTHORS   Kelly,A.P., Monaco,J.J., Cho,S.G. and Trowsdale,J.
  TITLE     A new human HLA class II-related locus, DM
  JOURNAL   Nature 353 (6344), 571-573 (1991)
   PUBMED   1922365
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U15085.1, EL948395.1 and
            CD742571.1.
            
            On Jul 23, 2010 this sequence version replaced NP_002109.1.
            
            Summary: HLA-DMB belongs to the HLA class II beta chain paralogues.
            This class II molecule is a heterodimer consisting of an alpha
            (DMA) and a beta (DMB) chain, both anchored in the membrane. It is
            located in intracellular vesicles. DM plays a central role in the
            peptide loading of MHC class II molecules by helping to release the
            CLIP (class II-associated invariant chain peptide) molecule from
            the peptide binding site. Class II molecules are expressed in
            antigen presenting cells (APC: B lymphocytes, dendritic cells,
            macrophages). The beta chain is approximately 26-28 kDa and its
            gene contains 6 exons. Exon one encodes the leader peptide, exons 2
            and 3 encode the two extracellular domains, exon 4 encodes the
            transmembrane domain and exon 5 encodes the cytoplasmic tail.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U15085.1, AY645722.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000418107.3/ ENSP00000398890.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..263
                     /product="HLA class II histocompatibility antigen, DM beta
                     chain precursor"
                     /note="class II histocompatibility antigen, M beta chain;
                     HLA class II histocompatibility antigen, DM beta chain;
                     MHC class II HLA-DMB; MHC class II antigen HLA-DM beta
                     chain; MHC class II antigen DMB; really interesting new
                     gene 7 protein"
                     /calculated_mol_wt=27129
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28068.2)"
                     /calculated_mol_wt=1820
     mat_peptide     19..263
                     /product="HLA class II histocompatibility antigen, DM beta
                     chain"
                     /calculated_mol_wt=27129
     Region          19..112
                     /region_name="Beta-1"
                     /note="propagated from UniProtKB/Swiss-Prot (P28068.2)"
     Region          27..106
                     /region_name="MHC_II_beta"
                     /note="Class II histocompatibility antigen, beta domain;
                     pfam00969"
                     /db_xref="CDD:425967"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P28068.2)"
     Region          112..208
                     /region_name="IgC1_MHC_II_beta_HLA-DM"
                     /note="Class II major histocompatibility complex (MHC)
                     beta chain immunoglobulin domain of histocompatibility
                     antigen (HLA) DM; member of the C1-set of Ig superfamily
                     (IgSF) domains; cd21002"
                     /db_xref="CDD:409593"
     Region          113..207
                     /region_name="Beta-2"
                     /note="propagated from UniProtKB/Swiss-Prot (P28068.2)"
     Region          114..122
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409593"
     Site            order(120,138..139,141,168..175)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409593"
     Region          132..141
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409593"
     Site            order(141,170..172,174)
                     /site_type="other"
                     /note="MHC binding domain interface [polypeptide binding]"
                     /db_xref="CDD:409593"
     Region          145..151
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409593"
     Region          153..156
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409593"
     Region          161..169
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409593"
     Region          172..182
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409593"
     Region          189..196
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409593"
     Region          203..207
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409593"
     Region          208..218
                     /region_name="Connecting peptide. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P28068.2)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28068.2)"
     Region          248..251
                     /region_name="YXXZ motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P28068.2)"
     CDS             1..263
                     /gene="HLA-DMB"
                     /gene_synonym="D6S221E; RING7"
                     /coded_by="NM_002118.5:222..1013"
                     /db_xref="CCDS:CCDS4760.1"
                     /db_xref="GeneID:3109"
                     /db_xref="HGNC:HGNC:4935"
                     /db_xref="MIM:142856"
ORIGIN      
        1 mitflplllg lslgctgagg fvahvestcl lddagtpkdf tycisfnkdl ltcwdpeenk
       61 mapcefgvln slanvlsqhl nqkdtlmqrl rnglqncath tqpfwgsltn rtrppsvqva
      121 kttpfntrep vmlacyvwgf ypaevtitwr kngklvmphs sahktaqpng dwtyqtlshl
      181 altpsygdty tcvvehtgap epilrdwtpg lspmqtlkvs vsavtlglgl iifslgvisw
      241 rraghssytp lpgsnysegw his
//
LOCUS       NP_066269                174 aa            linear   PRI 27-APR-2025
DEFINITION  gamma-crystallin C [Homo sapiens].
ACCESSION   NP_066269
VERSION     NP_066269.1
DBSOURCE    REFSEQ: accession NM_020989.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Vendra,V.P.R., Ostrowski,C., Clark,R., Dyba,M., Tarasov,S.G. and
            Hejtmancik,J.F.
  TITLE     The Y46D Mutation Destabilizes Dense Packing of the Second Greek
            Key Pair of Human gammaC-Crystallin Causing Congenital Nuclear
            Cataracts
  JOURNAL   Biochemistry 62 (12), 1864-1877 (2023)
   PUBMED   37184593
  REMARK    GeneRIF: The Y46D Mutation Destabilizes Dense Packing of the Second
            Greek Key Pair of Human gammaC-Crystallin Causing Congenital
            Nuclear Cataracts.
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Peng,Y., Zheng,Y., Deng,Z., Zhang,S., Tan,Y., Hu,Z., Tao,L. and
            Luo,Y.
  TITLE     Case Report: A de novo Variant of CRYGC Gene Associated With
            Congenital Cataract and Microphthalmia
  JOURNAL   Front Genet 13, 866246 (2022)
   PUBMED   35719371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Fu,C., Xu,J., Yang,X., Chen,X. and Yao,K.
  TITLE     Cataract-causing mutations L45P and Y46D impair the thermal
            stability of gammaC-crystallin
  JOURNAL   Biochem Biophys Res Commun 539, 70-76 (2021)
   PUBMED   33422942
  REMARK    GeneRIF: Cataract-causing mutations L45P and Y46D impair the
            thermal stability of gammaC-crystallin.
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Fu,C., Xu,J., Jia,Z., Yao,K. and Chen,X.
  TITLE     Cataract-causing mutations L45P and Y46D promote gammaC-crystallin
            aggregation by disturbing hydrogen bonds network in the second
            Greek key motif
  JOURNAL   Int J Biol Macromol 167, 470-478 (2021)
   PUBMED   33278449
  REMARK    GeneRIF: Cataract-causing mutations L45P and Y46D promote
            gammaC-crystallin aggregation by disturbing hydrogen bonds network
            in the second Greek key motif.
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Brakenhoff,R.H., Aarts,H.J., Reek,F.H., Lubsen,N.H. and
            Schoenmakers,J.G.
  TITLE     Human gamma-crystallin genes. A gene family on its way to
            extinction
  JOURNAL   J Mol Biol 216 (3), 519-532 (1990)
   PUBMED   2258929
REFERENCE   7  (residues 1 to 174)
  AUTHORS   den Dunnen,J.T., van Neck,J.W., Cremers,F.P., Lubsen,N.H. and
            Schoenmakers,J.G.
  TITLE     Nucleotide sequence of the rat gamma-crystallin gene region and
            comparison with an orthologous human region
  JOURNAL   Gene 78 (2), 201-213 (1989)
   PUBMED   2777080
REFERENCE   8  (residues 1 to 174)
  AUTHORS   Meakin,S.O., Du,R.P., Tsui,L.C. and Breitman,M.L.
  TITLE     Gamma-crystallins of the human eye lens: expression analysis of
            five members of the gene family
  JOURNAL   Mol Cell Biol 7 (8), 2671-2679 (1987)
   PUBMED   3670288
REFERENCE   9  (residues 1 to 174)
  AUTHORS   Lubsen,N.H., Renwick,J.H., Tsui,L.C., Breitman,M.L. and
            Schoenmakers,J.G.
  TITLE     A locus for a human hereditary cataract is closely linked to the
            gamma-crystallin gene family
  JOURNAL   Proc Natl Acad Sci U S A 84 (2), 489-492 (1987)
   PUBMED   3025877
REFERENCE   10 (residues 1 to 174)
  AUTHORS   Shiloh,Y., Donlon,T., Bruns,G., Breitman,M.L. and Tsui,L.C.
  TITLE     Assignment of the human gamma-crystallin gene cluster (CRYG) to the
            long arm of chromosome 2, region q33-36
  JOURNAL   Hum Genet 73 (1), 17-19 (1986)
   PUBMED   3011643
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC074954.2 and BU737104.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the beta/gamma-crystallin
            family of proteins. Crystallins constitute the major proteins of
            vertebrate eye lens and maintain the transparency and refractive
            index of the lens. This gene and several family members are present
            in a gene cluster on chromosome 2. Mutations in this gene have been
            shown to cause multiple types of cataract, including Coppock-like
            cataract and zonular pulverulent cataract, among others. [provided
            by RefSeq, Jan 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY795083.2, BC074954.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282141.4/ ENSP00000282141.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..174
                     /product="gamma-crystallin C"
                     /note="gamma-crystallin 3; gamma-crystallin 2-1"
                     /calculated_mol_wt=20748
     Region          3..82
                     /region_name="XTALbg"
                     /note="Beta/gamma crystallins; smart00247"
                     /db_xref="CDD:214583"
     Site            23
                     /site_type="methylation"
                     /note="S-methylcysteine.
                     /evidence=ECO:0000269|PubMed:12876325; propagated from
                     UniProtKB/Swiss-Prot (P07315.2)"
     Region          84..87
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P07315.2)"
     Region          89..170
                     /region_name="Crystall"
                     /note="Beta/Gamma crystallin; pfam00030"
                     /db_xref="CDD:459639"
     CDS             1..174
                     /gene="CRYGC"
                     /gene_synonym="CCL; CRYG3; CTRCT2"
                     /coded_by="NM_020989.4:37..561"
                     /db_xref="CCDS:CCDS2379.1"
                     /db_xref="GeneID:1420"
                     /db_xref="HGNC:HGNC:2410"
                     /db_xref="MIM:123680"
ORIGIN      
        1 mgkitfyedr afqgrsyett tdcpnlqpyf srcnsirves gcwmlyerpn yqgqqyllrr
       61 geypdyqqwm glsdsirscc lipqtvshrl rlyeredhkg lmmelsedcp siqdrfhlse
      121 irslhvlegc wvlyelpnyr grqyllrpqe yrrcqdwgam dakagslrrv vdly
//
LOCUS       NP_001275572             511 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 286A isoform 3 [Homo sapiens].
ACCESSION   NP_001275572
VERSION     NP_001275572.1
DBSOURCE    REFSEQ: accession NM_001288643.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Murakami,T., Sun,Z.S., Lee,C.C. and Lupski,J.R.
  TITLE     Isolation of novel genes from the CMT1A duplication/HNPP deletion
            critical region in 17p11.2-p12
  JOURNAL   Genomics 39 (1), 99-103 (1997)
   PUBMED   9027492
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005324.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.193107.1, BP219726.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..511
                     /product="zinc finger protein 286A isoform 3"
                     /note="zinc finger protein ZNF286"
                     /calculated_mol_wt=58899
     Region          35..88
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <212..351
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          235..255
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          263..283
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          290..310
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          318..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <342..497
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          346..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          374..394
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(379,381,383,385..386,389..390,393,407,409,413..414,
                     417..418,421,435,437,439,441..442,445..446,449)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          402..422
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          430..450
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          458..478
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          486..506
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..511
                     /gene="ZNF286A"
                     /gene_synonym="ZNF286"
                     /coded_by="NM_001288643.2:20..1555"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS73997.1"
                     /db_xref="GeneID:57335"
                     /db_xref="HGNC:HGNC:13501"
ORIGIN      
        1 mgalssqdsp hfqeksteeg evaalrltar sqetvtfkdv amdftpeewg kldpaqrdvm
       61 lenyrnlvsl wlpvskpesy nlengkeplk lerkapkssy sdmetrpqsk dstsvqdfsk
      121 aesckvaiid rltrnsvyds nleaalecen wlenqqgnqe rhlremfthm nslseetdhk
      181 hdvywksfnq ksvlitedrv pkgsyafhtl ekslkqksnl mkkqrtykek kphkcndcge
      241 lftyhsvlir hqrvhtgekp ytcnecgksf shranltkhq rthtrilfec seckktftes
      301 sslathqrih vgerpyecne cgkgfnrsth lvqhqlihtg vkpyecnecd kafihssali
      361 khqrthtgek pykcqecgka fshcssltkh qrvhtgekpy ecsecgktfs qsthlvqhqr
      421 ihtgekpyec necgktfsrs snfakhqrih igkkpykcse cgkafihssa liqhqrthtg
      481 ekpfrcnecg ksfkcsssli rhqrvhteeq p
//
LOCUS       NP_001340                501 aa            linear   PRI 27-APR-2025
DEFINITION  aspartate--tRNA ligase, cytoplasmic isoform 1 [Homo sapiens].
ACCESSION   NP_001340
VERSION     NP_001340.2
DBSOURCE    REFSEQ: accession NM_001349.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Xiong,H., Liao,M., Zhang,H., Li,Y., Bai,J., Zhang,J., Li,L. and
            Zhang,L.
  TITLE     DARS expression in BCR/ABL1-negative myeloproliferative neoplasms
            and its association with the immune microenvironment
  JOURNAL   Sci Rep 14 (1), 16711 (2024)
   PUBMED   39030308
  REMARK    GeneRIF: DARS expression in BCR/ABL1-negative myeloproliferative
            neoplasms and its association with the immune microenvironment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Liu,B., Katoh,H., Komura,D., Yamamoto,A., Ochi,M., Onoyama,T.,
            Abe,H., Ushiku,T., Seto,Y., Suo,J. and Ishikawa,S.
  TITLE     Functional genomics screening identifies aspartyl-tRNA synthetase
            as a novel prognostic marker and a therapeutic target for gastric
            cancers
  JOURNAL   J Pathol 258 (2), 106-120 (2022)
   PUBMED   35696251
  REMARK    GeneRIF: Functional genomics screening identifies aspartyl-tRNA
            synthetase as a novel prognostic marker and a therapeutic target
            for gastric cancers.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Klugmann,M., Kalotay,E., Delerue,F., Ittner,L.M., Bongers,A.,
            Yu,J., Morris,M.J., Housley,G.D. and Frohlich,D.
  TITLE     Developmental delay and late onset HBSL pathology in hypomorphic
            Dars1M256L mice
  JOURNAL   Neurochem Res 47 (7), 1972-1984 (2022)
   PUBMED   35357600
  REMARK    GeneRIF: Developmental delay and late onset HBSL pathology in
            hypomorphic Dars1(M256L) mice.
            Erratum:[Neurochem Res. 2022 Jul;47(7):1985-1990. doi:
            10.1007/s11064-022-03602-3. PMID: 35449376]
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Gonzalez-Serrano,L.E., Karim,L., Pierre,F., Schwenzer,H., Rotig,A.,
            Munnich,A. and Sissler,M.
  TITLE     Three human aminoacyl-tRNA synthetases have distinct
            sub-mitochondrial localizations that are unaffected by
            disease-associated mutations
  JOURNAL   J Biol Chem 293 (35), 13604-13615 (2018)
   PUBMED   30006346
  REMARK    GeneRIF: This study demonstrates that human mitochondrial AspRS,
            ArgRS, and LysRS, each have a specific sub-mitochondrial
            distribution, with ArgRS being exclusively localized in the
            membrane, LysRS exclusively in the soluble fraction, and AspRS
            being present in both.
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Rho,S.B., Kim,M.J., Lee,J.S., Seol,W., Motegi,H., Kim,S. and
            Shiba,K.
  TITLE     Genetic dissection of protein-protein interactions in multi-tRNA
            synthetase complex
  JOURNAL   Proc Natl Acad Sci U S A 96 (8), 4488-4493 (1999)
   PUBMED   10200289
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Quevillon,S., Robinson,J.C., Berthonneau,E., Siatecka,M. and
            Mirande,M.
  TITLE     Macromolecular assemblage of aminoacyl-tRNA synthetases:
            identification of protein-protein interactions and characterization
            of a core protein
  JOURNAL   J Mol Biol 285 (1), 183-195 (1999)
   PUBMED   9878398
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Reed,V.S., Wastney,M.E. and Yang,D.C.
  TITLE     Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA
            synthetase to the elongation factor 1 alpha
  JOURNAL   J Biol Chem 269 (52), 32932-32936 (1994)
   PUBMED   7806521
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Escalante,C. and Yang,D.C.
  TITLE     Expression of human aspartyl-tRNA synthetase in Escherichia coli.
            Functional analysis of the N-terminal putative amphiphilic helix
  JOURNAL   J Biol Chem 268 (8), 6014-6023 (1993)
   PUBMED   8449960
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Jacobo-Molina,A., Peterson,R. and Yang,D.C.
  TITLE     cDNA sequence, predicted primary structure, and evolving
            amphiphilic helix of human aspartyl-tRNA synthetase
  JOURNAL   J Biol Chem 264 (28), 16608-16612 (1989)
   PUBMED   2674137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA597505.1, BC000629.2,
            BU615302.1, AC011999.9 and BX101357.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 15, 2004 this sequence version replaced NP_001340.1.
            
            Summary: This gene encodes a member of a multienzyme complex that
            functions in mediating the attachment of amino acids to their
            cognate tRNAs. The encoded protein ligates L-aspartate to
            tRNA(Asp). Mutations in this gene have been found in patients
            showing hypomyelination with brainstem and spinal cord involvement
            and leg spasticity. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jun 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK129521.1, SRR3476690.947879.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264161.9/ ENSP00000264161.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.3"
     Protein         1..501
                     /product="aspartate--tRNA ligase, cytoplasmic isoform 1"
                     /EC_number="6.1.1.12"
                     /note="aspartate tRNA ligase 1, cytoplasmic; aspartyl-tRNA
                     synthetase, cytoplasmic; cell proliferation-inducing gene
                     40 protein; testicular tissue protein Li 192"
                     /calculated_mol_wt=57005
     Region          3..501
                     /region_name="PLN02850"
                     /note="aspartate-tRNA ligase"
                     /db_xref="CDD:215456"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P14868.2)"
     Site            74
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P14868.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P14868.2)"
     Region          251..254
                     /region_name="Aspartate. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P14868.2)"
     Site            374
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P14868.2)"
     Region          411..415
                     /region_name="Binding site for the 3'-end of tRNA.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P14868.2)"
     Site            500
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P14868.2)"
     CDS             1..501
                     /gene="DARS1"
                     /gene_synonym="aspRS; DARS; HBSL"
                     /coded_by="NM_001349.4:159..1664"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2180.1"
                     /db_xref="GeneID:1615"
                     /db_xref="HGNC:HGNC:2678"
                     /db_xref="MIM:603084"
ORIGIN      
        1 mpsasasrks qekpreimda aedyakeryg issmiqsqek pdrvlvrvrd ltiqkadevv
       61 wvrarvhtsr akgkqcflvl rqqqfnvqal vavgdhaskq mvkfaanink esivdvegvv
      121 rkvnqkigsc tqqdvelhvq kiyvislaep rlplqlddav rpeaegeeeg ratvnqdtrl
      181 dnrvidlrts tsqavfrlqs gichlfretl inkgfveiqt pkiisaaseg ganvftvsyf
      241 knnaylaqsp qlykqmcica dfekvfsigp vfraedsnth rhltefvgld iemafnyhyh
      301 evmeeiadtm vqifkglqer fqteiqtvnk qfpcepfkfl eptlrleyce alamlreagv
      361 emgdeddlst pnekllghlv kekydtdfyi ldkyplavrp fytmpdprnp kqsnsydmfm
      421 rgeeilsgaq rihdpqllte ralhhgidle kikayidsfr fgapphaggg iglervtmlf
      481 lglhnvrqts mfprdpkrlt p
//
LOCUS       NP_663729                289 aa            linear   PRI 27-APR-2025
DEFINITION  ATP synthase mitochondrial F1 complex assembly factor 2 [Homo
            sapiens].
ACCESSION   NP_663729
VERSION     NP_663729.1
DBSOURCE    REFSEQ: accession NM_145691.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Meulemans,A., Seneca,S., Pribyl,T., Smet,J., Alderweirldt,V.,
            Waeytens,A., Lissens,W., Van Coster,R., De Meirleir,L., di
            Rago,J.P., Gatti,D.L. and Ackerman,S.H.
  TITLE     Defining the pathogenesis of the human Atp12p W94R mutation using a
            Saccharomyces cerevisiae yeast model
  JOURNAL   J Biol Chem 285 (6), 4099-4109 (2010)
   PUBMED   19933271
  REMARK    GeneRIF: Data show that wild type human Atp12p rescues the
            respiratory defect of a yeast ATP12 deletion mutant (Deltaatp12).
REFERENCE   7  (residues 1 to 289)
  AUTHORS   De Meirleir,L., Seneca,S., Lissens,W., De Clercq,I., Eyskens,F.,
            Gerlo,E., Smet,J. and Van Coster,R.
  TITLE     Respiratory chain complex V deficiency due to a mutation in the
            assembly gene ATP12
  JOURNAL   J Med Genet 41 (2), 120-124 (2004)
   PUBMED   14757859
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Bi,W., Yan,J., Stankiewicz,P., Park,S.S., Walz,K., Boerkoel,C.F.,
            Potocki,L., Shaffer,L.G., Devriendt,K., Nowaczyk,M.J., Inoue,K. and
            Lupski,J.R.
  TITLE     Genes in a refined Smith-Magenis syndrome critical deletion
            interval on chromosome 17p11.2 and the syntenic region of the mouse
  JOURNAL   Genome Res 12 (5), 713-728 (2002)
   PUBMED   11997338
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Wang,Z.G., White,P.S. and Ackerman,S.H.
  TITLE     Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human
            mitochondria
  JOURNAL   J Biol Chem 276 (33), 30773-30778 (2001)
   PUBMED   11410595
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087163.10, BC004114.2,
            AA760883.1 and AI857387.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an assembly factor for the F(1)
            component of the mitochondrial ATP synthase. This protein binds
            specifically to the F1 alpha subunit and is thought to prevent this
            subunit from forming nonproductive homooligomers during enzyme
            assembly. This gene is located within the Smith-Magenis syndrome
            region on chromosome 17. An alternatively spliced transcript
            variant has been described, but its biological validity has not
            been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.75421.1,
                                           SRR5189655.95322.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000474627.8/
                                                  ENSP00000417190.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..289
                     /product="ATP synthase mitochondrial F1 complex assembly
                     factor 2"
                     /note="ATP12 homolog"
                     /calculated_mol_wt=32641
     Region          13..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5M1.1)"
     Region          46..265
                     /region_name="ATP12"
                     /note="ATP12 chaperone protein; cl02228"
                     /db_xref="CDD:470498"
     CDS             1..289
                     /gene="ATPAF2"
                     /gene_synonym="ATP12; ATP12p; LP3663; MC5DN1"
                     /coded_by="NM_145691.4:156..1025"
                     /db_xref="CCDS:CCDS32585.1"
                     /db_xref="GeneID:91647"
                     /db_xref="HGNC:HGNC:18802"
                     /db_xref="MIM:608918"
ORIGIN      
        1 mwrsclrlrd ggrrllnrpa ggpsasmspg ptipsparay appterkrfy qnvsitqgeg
       61 gfeinldhrk lktpqaklft vpsealaiav atewdsqqdt ikyytmhltt lcntsldnpt
      121 qrnkdqlira avkfldtdti cyrveepetl velqrnewdp iiewaekryg veissstsim
      181 gpsipaktre vlvshlasyn twalqgiefv aaqlksmvlt lglidlrltv eqavllsrle
      241 eeyqiqkwgn iewahdyelq elrartaagt lfihlcsest tvkhkllke
//
LOCUS       NP_001356635             750 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger Y-chromosomal protein isoform 5 [Homo sapiens].
ACCESSION   NP_001356635 XP_011529777
VERSION     NP_001356635.1
DBSOURCE    REFSEQ: accession NM_001369706.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Ni,W., Perez,A.A., Schreiner,S., Nicolet,C.M. and Farnham,P.J.
  TITLE     Characterization of the ZFX family of transcription factors that
            bind downstream of the start site of CpG island promoters
  JOURNAL   Nucleic Acids Res 48 (11), 5986-6000 (2020)
   PUBMED   32406922
  REMARK    GeneRIF: Characterization of the ZFX family of transcription
            factors that bind downstream of the start site of CpG island
            promoters.
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Decarpentrie,F., Vernet,N., Mahadevaiah,S.K., Longepied,G.,
            Streichemberger,E., Aknin-Seifer,I., Ojarikre,O.A., Burgoyne,P.S.,
            Metzler-Guillemain,C. and Mitchell,M.J.
  TITLE     Human and mouse ZFY genes produce a conserved testis-specific
            transcript encoding a zinc finger protein with a short acidic
            domain and modified transactivation potential
  JOURNAL   Hum Mol Genet 21 (12), 2631-2645 (2012)
   PUBMED   22407129
  REMARK    GeneRIF: Studies identified a major testis-specific ZFY transcript
            that encodes a protein with the same short acidic domain.
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Tricoli,J.V. and Bracken,R.B.
  TITLE     ZFY gene expression and retention in human prostate adenocarcinoma
  JOURNAL   Genes Chromosomes Cancer 6 (2), 65-72 (1993)
   PUBMED   7680890
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Kochoyan,M., Keutmann,H.T. and Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            refinement of the NMR structure of an even finger by selective
            deuterium labeling and implications for DNA recognition
  JOURNAL   Biochemistry 30 (29), 7063-7072 (1991)
   PUBMED   1854720
REFERENCE   8  (residues 1 to 750)
  AUTHORS   North,M., Sargent,C., O'Brien,J., Taylor,K., Wolfe,J., Affara,N.A.
            and Ferguson-Smith,M.A.
  TITLE     Comparison of ZFY and ZFX gene structure and analysis of
            alternative 3' untranslated regions of ZFY
  JOURNAL   Nucleic Acids Res 19 (10), 2579-2586 (1991)
   PUBMED   2041734
REFERENCE   9  (residues 1 to 750)
  AUTHORS   Kochoyan,M., Havel,T.F., Nguyen,D.T., Dahl,C.E., Keutmann,H.T. and
            Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            2D NMR structure of an even finger and implications for
            'jumping-linker' DNA recognition
  JOURNAL   Biochemistry 30 (14), 3371-3386 (1991)
   PUBMED   1849423
REFERENCE   10 (residues 1 to 750)
  AUTHORS   Palmer,M.S., Berta,P., Sinclair,A.H., Pym,B. and Goodfellow,P.N.
  TITLE     Comparison of human ZFY and ZFX transcripts
  JOURNAL   Proc Natl Acad Sci U S A 87 (5), 1681-1685 (1990)
   PUBMED   2308929
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006157.2.
            
            On Apr 16, 2019 this sequence version replaced XP_011529777.1.
            
            Summary: This gene encodes a zinc finger-containing protein that
            may function as a transcription factor. This gene was once a
            candidate gene for the testis-determining factor (TDF) and was
            erroneously referred to as TDF. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.209023.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yp11.2"
     Protein         1..750
                     /product="zinc finger Y-chromosomal protein isoform 5"
                     /note="zinc finger Y-chromosomal protein"
                     /calculated_mol_wt=84956
     Region          71..355
                     /region_name="Zfx_Zfy_act"
                     /note="Zfx / Zfy transcription activation region;
                     pfam04704"
                     /db_xref="CDD:461400"
     Region          <366..541
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          <372..>394
                     /region_name="ROS_MUCR"
                     /note="ROS/MUCR transcriptional regulator protein;
                     cl19880"
                     /db_xref="CDD:473244"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          403..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(440,442,444,446..447,450..451,454,500,502,506..507,
                     510..511,514,528,530,532,534..535,538..539,542)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          488..>625
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          495..515
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          507..531
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          523..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          552..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          609..629
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          664..686
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          666..686
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(671,673,675,677..678,681..682,685,699,701,705..706,
                     709..710,714,728,730,732,734..735,738..739,742)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          678..702
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          694..715
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          723..743
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..750
                     /gene="ZFY"
                     /gene_synonym="ZNF911"
                     /coded_by="NM_001369706.1:418..2670"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:7544"
                     /db_xref="HGNC:HGNC:12870"
                     /db_xref="MIM:490000"
ORIGIN      
        1 mdedefelqp qepnsffdgi gadathmdgd qivveiqeav fvsnivdsdi tvhnfvpddp
       61 dsvviqdvve dvvieedvqc sdileeadvs enviipeqvl dsdvteevsl phctvpddvl
      121 asditstsms mpehvltses mhvcdighve hmvhdsvvea eiitdpltsd ivseevlvad
      181 capeavidas gisvdqqdnd kascedylmi slddagkieh dgstgvtida esemdpckvd
      241 stcpevikvy ifkadpgedd lggtvdives ependhgvel ldqnssirvp rekmvymtvn
      301 dsqqededls nnsdgienrn gtasallhid esaglgrlak qkpkkkrrpd srqyqtaiii
      361 gpdghpltvy pcmicgkkfk srgflkrhmk nhpehlakkk yhctdcdytt nkkislhnhl
      421 eshkltskae kaiecdecgk hfshagalft hkmvhkekga nkmhkckfce yetaeqglln
      481 rhllavhskn fphicvecgk gfrhpselrk hmrihtgekp yqcqyceyrs adssnlkthi
      541 ktkhskempf kcdiclltfs dtkevqqhtl vhqeskthqc lhcdhkssns sdlkrhvisv
      601 htkdyphkce mcekgfhrps elkkhvavhk gkkmhqcrhc dfkiadpfvl srhilsvhtk
      661 dlpfrckrcr kgfrqqnelk khmkthsgrk vyqceyceys ttdasgfkrh visihtkdyp
      721 hrceyckkgf rrpseknqhi mrhhkevglp
//
LOCUS       NP_848602                273 aa            linear   PRI 27-APR-2025
DEFINITION  out at first protein homolog precursor [Homo sapiens].
ACCESSION   NP_848602
VERSION     NP_848602.1
DBSOURCE    REFSEQ: accession NM_178507.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Sanchez-Pulido,L. and Ponting,C.P.
  TITLE     OAF: a new member of the BRICHOS family
  JOURNAL   Bioinform Adv 2 (1), vbac087 (2022)
   PUBMED   36699367
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Lu,Q., Liu,J., Yu,Y., Liang,H.F., Zhang,S.Q., Li,Z.B., Chen,J.X.,
            Xu,Q.G. and Li,J.C.
  TITLE     ALB, HP, OAF and RBP4 as novel protein biomarkers for identifying
            cured patients with pulmonary tuberculosis by DIA
  JOURNAL   Clin Chim Acta 535, 82-91 (2022)
   PUBMED   35964702
  REMARK    GeneRIF: ALB, HP, OAF and RBP4 as novel protein biomarkers for
            identifying cured patients with pulmonary tuberculosis by DIA.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB480792.1, BC047726.1, AI733095.1, AA902624.1 and AP000679.7.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047726.1, ERR279833.8880.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000328965.9/ ENSP00000332613.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..273
                     /product="out at first protein homolog precursor"
                     /note="out at first protein homolog; HCV
                     NS5A-transactivated protein 13 target protein 2; OAF
                     homolog"
                     /calculated_mol_wt=27930
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2777
     mat_peptide     28..273
                     /product="Out at first protein homolog.
                     /id=PRO_0000292427"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UD1.1)"
                     /calculated_mol_wt=27930
     Region          30..268
                     /region_name="OAF"
                     /note="Transcriptional regulator, Out at first; pfam14941"
                     /db_xref="CDD:464389"
     CDS             1..273
                     /gene="OAF"
                     /gene_synonym="NS5ATP13TP2"
                     /coded_by="NM_178507.4:249..1070"
                     /db_xref="CCDS:CCDS8430.1"
                     /db_xref="GeneID:220323"
                     /db_xref="HGNC:HGNC:28752"
                     /db_xref="MIM:621070"
ORIGIN      
        1 mrlpgvplar palllllpll apllgtgapa elrvrvrlpd gqvteeslqa dsdadsisle
       61 lrkpdgtlvs ftadfkkdvk vfralilgel ekgqsqfqal cfvtqlqhne iipseamakl
      121 rqknpravrq aeevrglehl hmdvavnfsq gallsphlhn vcaeavdaiy trqedvrfwl
      181 eqgvdssvfe alpkaseqae lprcrqvgdh gkpcvcrygl slawypcmlk ychsrdrptp
      241 ykcgirscqk sysfdfyvpq rqlclwdedp ypg
//
LOCUS       NP_001350108             157 aa            linear   ROD 27-APR-2025
DEFINITION  ras-like protein family member 10A isoform 2 [Mus musculus].
ACCESSION   NP_001350108 XP_006514938
VERSION     NP_001350108.1
DBSOURCE    REFSEQ: accession NM_001363179.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Ehringer,M.A., Thompson,J., Conroy,O., Xu,Y., Yang,F., Canniff,J.,
            Beeson,M., Gordon,L., Bennett,B., Johnson,T.E. and Sikela,J.M.
  TITLE     High-throughput sequence identification of gene coding variants
            within alcohol-related QTLs
  JOURNAL   Mamm Genome 12 (8), 657-663 (2001)
   PUBMED   11471062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL645522.12.
            
            On May 10, 2018 this sequence version replaced XP_006514938.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.320317.1,
                                           ERR3363658.995152.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 3.21 cM"
     Protein         1..157
                     /product="ras-like protein family member 10A isoform 2"
                     /EC_number="3.6.5.2"
                     /note="ras-like protein family member 10A; ras-related
                     protein on chromosome 22 homolog; Ras-like protein RRP22
                     (RAS-related protein on chromosome 22)"
                     /calculated_mol_wt=16960
     Region          5..>113
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            11..18
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133342"
     Region          33..42
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K5A4.1)"
     Site            36
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133342"
     Site            40..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133342"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133342"
     Site            order(61..62,87..88)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133342"
     CDS             1..157
                     /gene="Rasl10a"
                     /gene_synonym="2210403B10Rik"
                     /coded_by="NM_001363179.1:179..652"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:75668"
                     /db_xref="MGI:MGI:1922918"
ORIGIN      
        1 mggslrvavl gapgvgktai irqflfgdyp erhrptdspc lyrpavlldg avydlsirdg
       61 dvagpgsspr sleewpdpkd wslqdtdafv lvydicspds fdyvkalrqr iaensrglaf
      121 icthgvgssg hgvsstasli sigppgrreh qrhpsww
//
LOCUS       NP_996998                172 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 580 [Homo sapiens].
ACCESSION   NP_996998
VERSION     NP_996998.1
DBSOURCE    REFSEQ: accession NM_207115.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Luo,Y., Zhao,Y., Li,X., Zhao,J. and Zhang,W.
  TITLE     ZNF580 mediates eNOS expression and endothelial cell
            migration/proliferation via the TGF-beta1/ALK5/Smad2 pathway
  JOURNAL   Mol Cell Biochem 393 (1-2), 199-207 (2014)
   PUBMED   24771066
  REMARK    GeneRIF: These results suggest that ZNF580 mediates eNOS expression
            and endothelial cell migration/proliferation via the
            TGF-b1/ALK5/Smad2 pathway, and thus plays a crucial role in
            vascular endothelial cells.
REFERENCE   4  (residues 1 to 172)
  AUTHORS   DangLi,R., HeKong,W., JiQin,L., MingHua,Z. and WenCheng,Z.
  TITLE     ROS-induced ZNF580 expression: a key role for H2O2/NF-kappaB
            signaling pathway in vascular endothelial inflammation
  JOURNAL   Mol Cell Biochem 359 (1-2), 183-191 (2012)
   PUBMED   21830064
  REMARK    GeneRIF: H2O2 upregulates the expression of ZNF580 via the
            NF-kappaB signaling pathway, and overexpression of ZNF580 plays a
            critical role in augmenting the release of pro-inflammatory
            cytokine IL-8.
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Luo,Y., Hu,W., Xu,R., Hou,B., Zhang,L. and Zhang,W.
  TITLE     ZNF580, a novel C2H2 zinc-finger transcription factor, interacts
            with the TGF-beta signal molecule Smad2
  JOURNAL   Cell Biol Int 35 (11), 1153-1157 (2011)
   PUBMED   21599657
  REMARK    GeneRIF: ZNF580 is a binding partner of Smad2 and is involved in
            the signal transduction of the transforming growth factor-beta
            signalling pathway.
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Hoffmann,C.J., Hohberg,M., Chlench,S., Maroski,J., Drab,M.,
            Siegel,G., Pries,A.R. and Zakrzewicz,A.
  TITLE     Suppression of zinc finger protein 580 by high oxLDL/LDL-ratios is
            followed by enhanced expression of endothelial IL-8
  JOURNAL   Atherosclerosis 216 (1), 103-108 (2011)
   PUBMED   21310414
  REMARK    GeneRIF: ZNF580 is a novel factor in the lipoprotein-dependent
            regulation of endothelial IL-8 expression and monocyte arrest.
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Sun,H.Y., Wei,S.P., Xu,R.C., Xu,P.X. and Zhang,W.C.
  TITLE     Sphingosine-1-phosphate induces human endothelial VEGF and MMP-2
            production via transcription factor ZNF580: novel insights into
            angiogenesis
  JOURNAL   Biochem Biophys Res Commun 395 (3), 361-366 (2010)
   PUBMED   20382120
  REMARK    GeneRIF: These results elucidate the important role that ZNF580
            plays in the process of migration and proliferation of endothelial
            cells, which provides a foundation for a novel approach to regulate
            angiogenesis.
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008735.9, AL359054.1, BU179609.1 and AF184939.1.
            
            Transcript Variant: This variant (2) represents use of an alternate
            promoter and 5' UTR, compared to variant 1. Variants 1, 2, and 3
            all encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL359054.1, SRR1163655.278522.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325333.10/ ENSP00000320050.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..172
                     /product="zinc finger protein 580"
                     /note="LDL-induced EC protein"
                     /calculated_mol_wt=18625
     Region          1..93
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK33.1)"
     Region          94..114
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(99,101,103,105..106,109..110,113,127,129,133..134,
                     137..138,141,157,159,161,163..164,167..168,171)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          120..142
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          122..142
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          152..172
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..172
                     /gene="ZNF580"
                     /coded_by="NM_207115.2:195..713"
                     /db_xref="CCDS:CCDS12931.1"
                     /db_xref="GeneID:51157"
                     /db_xref="HGNC:HGNC:29473"
                     /db_xref="MIM:617888"
ORIGIN      
        1 mlllpprpph prssspeamd ppppkappfp kaegpsstps saagprpprl grhllidang
       61 vpytytvqle eeprgppqre appgepgprk gyscpecarv fasplrlqsh rvshsdlkpf
      121 tcgacgkafk rsshlsrhra thraragpph tcplcprrfq daaelaqhvr lh
//
LOCUS       NP_000251               2215 aa            linear   PRI 27-APR-2025
DEFINITION  unconventional myosin-VIIa isoform 1 [Homo sapiens].
ACCESSION   NP_000251
VERSION     NP_000251.3
DBSOURCE    REFSEQ: accession NM_000260.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2215)
  AUTHORS   Peart,L., Gonzalez,J., Morel Swols,D., Duman,D., Saridogan,T.,
            Ramzan,M., Zafeer,M.F., Liu,X.Z., Eshraghi,A.A., Hoffer,M.E.,
            Angeli,S.I., Bademci,G., Blanton,S., Smith,C., Telischi,F.F. and
            Tekin,M.
  TITLE     Dispersed DNA variants underlie hearing loss in South Florida's
            minority population
  JOURNAL   Hum Genomics 17 (1), 103 (2023)
   PUBMED   37996878
  REMARK    GeneRIF: Dispersed DNA variants underlie hearing loss in South
            Florida's minority population.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2215)
  AUTHORS   Gilmore,W.B., Hultgren,N.W., Chadha,A., Barocio,S.B., Zhang,J.,
            Kutsyr,O., Flores-Bellver,M., Canto-Soler,M.V. and Williams,D.S.
  TITLE     Expression of two major isoforms of MYO7A in the retina:
            Considerations for gene therapy of Usher syndrome type 1B
  JOURNAL   Vision Res 212, 108311 (2023)
   PUBMED   37586294
  REMARK    GeneRIF: Expression of two major isoforms of MYO7A in the retina:
            Considerations for gene therapy of Usher syndrome type 1B.
REFERENCE   3  (residues 1 to 2215)
  AUTHORS   Baux,D., Faugere,V., Larrieu,L., Le Guedard-Mereuze,S., Hamroun,D.,
            Beroud,C., Malcolm,S., Claustres,M. and Roux,A.F.
  TITLE     UMD-USHbases: a comprehensive set of databases to record and
            analyse pathogenic mutations and unclassified variants in seven
            Usher syndrome causing genes
  JOURNAL   Hum Mutat 29 (8), E76-E87 (2008)
   PUBMED   18484607
REFERENCE   4  (residues 1 to 2215)
  AUTHORS   Inoue,A. and Ikebe,M.
  TITLE     Characterization of the motor activity of mammalian myosin VIIA
  JOURNAL   J Biol Chem 278 (7), 5478-5487 (2003)
   PUBMED   12466270
REFERENCE   5  (residues 1 to 2215)
  AUTHORS   Kelley,P.M., Weston,M.D., Chen,Z.Y., Orten,D.J., Hasson,T.,
            Overbeck,L.D., Pinnt,J., Talmadge,C.B., Ing,P., Mooseker,M.S.,
            Corey,D., Sumegi,J. and Kimberling,W.J.
  TITLE     The genomic structure of the gene defective in Usher syndrome type
            Ib (MYO7A)
  JOURNAL   Genomics 40 (1), 73-79 (1997)
   PUBMED   9070921
REFERENCE   6  (residues 1 to 2215)
  AUTHORS   Chen,Z.Y., Hasson,T., Kelley,P.M., Schwender,B.J., Schwartz,M.F.,
            Ramakrishnan,M., Kimberling,W.J., Mooseker,M.S. and Corey,D.P.
  TITLE     Molecular cloning and domain structure of human myosin-VIIa, the
            gene product defective in Usher syndrome 1B
  JOURNAL   Genomics 36 (3), 440-448 (1996)
   PUBMED   8884267
REFERENCE   7  (residues 1 to 2215)
  AUTHORS   Hasson,T., Heintzelman,M.B., Santos-Sacchi,J., Corey,D.P. and
            Mooseker,M.S.
  TITLE     Expression in cochlea and retina of myosin VIIa, the gene product
            defective in Usher syndrome type 1B
  JOURNAL   Proc Natl Acad Sci U S A 92 (21), 9815-9819 (1995)
   PUBMED   7568224
REFERENCE   8  (residues 1 to 2215)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   9  (residues 1 to 2215)
  AUTHORS   Koenekoop,R.K., Arriaga,M.A., Trzupek,K.M. and Lentz,J.J.
  TITLE     Usher Syndrome Type I
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301442
REFERENCE   10 (residues 1 to 2215)
  AUTHORS   Kimberling,W.J., Moller,C.G., Davenport,S., Priluck,I.A.,
            Beighton,P.H., Greenberg,J., Reardon,W., Weston,M.D., Kenyon,J.B.,
            Grunkemeyer,J.A. et al.
  TITLE     Linkage of Usher syndrome type I gene (USH1B) to the long arm of
            chromosome 11
  JOURNAL   Genomics 14 (4), 988-994 (1992)
   PUBMED   1478677
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000752.4, U39226.1, U34227.1,
            U55208.1 and BG108466.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 24, 2008 this sequence version replaced NP_000251.2.
            
            Summary: This gene is a member of the myosin gene family. Myosins
            are mechanochemical proteins characterized by the presence of a
            motor domain, an actin-binding domain, a neck domain that interacts
            with other proteins, and a tail domain that serves as an anchor.
            This gene encodes an unconventional myosin with a very short tail.
            Defects in this gene are associated with the mouse shaker-1
            phenotype and the human Usher syndrome 1B which are characterized
            by deafness, reduced vestibular function, and (in human) retinal
            degeneration. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The update from NM_00260.1 to NM_00260.2 was
            intended to only modify select nucleotide residues that did not
            match the reference genome; however, the update mistakenly
            represented use of an alternate splice donor and splice acceptor
            site.  NM_00260.2 was subsequently updated to version 3 to
            represent the original exon and splice site combination. The
            difference between NM_000260.1 and NM_000260.3 involve single
            residue changes to match the reference genome.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U39226.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409709.9/ ENSP00000386331.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5"
     Protein         1..2215
                     /product="unconventional myosin-VIIa isoform 1"
                     /note="myosin VIIA (Usher syndrome 1B (autosomal
                     recessive, severe)); unconventional myosin-VIIa"
                     /calculated_mol_wt=254260
     Region          79..729
                     /region_name="MYSc_Myo7"
                     /note="class VII myosin, motor domain; cd01381"
                     /db_xref="CDD:276832"
     Site            order(106..114,158..165,202..212,437..442)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276832"
     Site            106..114
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276832"
     Site            158..165
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276832"
     Site            202..212
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276832"
     Site            437..442
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276832"
     Site            466..489
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276832"
     Region          632..639
                     /region_name="Actin-binding. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13402.2)"
     Site            660..669
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276832"
     Site            order(672..697,717..729)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276832"
     Region          <766..>809
                     /region_name="CBD_MYO6-like"
                     /note="calmodulin binding domain found in unconventional
                     myosin-VI and similar proteins; cd21759"
                     /db_xref="CDD:409646"
     Site            774..784
                     /site_type="other"
                     /note="IQ motif"
                     /db_xref="CDD:409646"
     Region          <796..>966
                     /region_name="tolA"
                     /note="cell envelope integrity inner membrane protein
                     TolA; Provisional; PRK09510"
                     /db_xref="CDD:236545"
     Region          <857..933
                     /region_name="MAP7"
                     /note="MAP7 (E-MAP-115) family; pfam05672"
                     /db_xref="CDD:461709"
     Region          858..935
                     /region_name="SAH. /evidence=ECO:0000305|PubMed:25122759"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13402.2)"
     Region          1017..1253
                     /region_name="MyTH4"
                     /note="Domain in Myosin and Kinesin Tails; smart00139"
                     /db_xref="CDD:214535"
     Region          1257..1355
                     /region_name="FERM1_F1_Myosin-VII"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain 1, F1 sub-domain, found in Myosin-VIIa,
                     Myosin-VIIb, and similar proteins; cd17092"
                     /db_xref="CDD:340612"
     Region          1259..1474
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Site            order(1307..1312,1317,1325,1347)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:340612"
     Region          1468..1604
                     /region_name="FERM_C1_MyoVII"
                     /note="FERM domain C-lobe, repeat 1, of Myosin VII
                     (MyoVII/Myo7); cd13198"
                     /db_xref="CDD:270019"
     Site            order(1468..1469,1473,1475,1490,1505)
                     /site_type="other"
                     /note="CEN1 peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270019"
     Site            order(1478,1500,1502,1509)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270019"
     Site            1569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97479; propagated from
                     UniProtKB/Swiss-Prot (Q13402.2)"
     Site            1571
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P97479; propagated from
                     UniProtKB/Swiss-Prot (Q13402.2)"
     Site            1591..1602
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270019"
     Region          1605..1669
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(1612,1614,1617,1624,1647..1648,1663,1665..1666)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          1763..1896
                     /region_name="MyTH4"
                     /note="Domain in Myosin and Kinesin Tails; smart00139"
                     /db_xref="CDD:214535"
     Region          1901..1998
                     /region_name="FERM2_F1_Myosin-VII"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain 2, F1 sub-domain, found in Myosin-VIIa,
                     Myosin-VIIb, and similar proteins; cd17093"
                     /db_xref="CDD:340613"
     Region          1903..2115
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          2111..2206
                     /region_name="FERM_C2_MyoVII"
                     /note="FERM domain C-lobe, repeat 2, of Myosin VII
                     (MyoVII, Myo7); cd13199"
                     /db_xref="CDD:270020"
     Site            order(2119,2140,2142,2148)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270020"
     Site            order(2152,2156..2159,2194,2198,2201..2202)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270020"
     Site            2194..2205
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270020"
     CDS             1..2215
                     /gene="MYO7A"
                     /gene_synonym="DFNA11; DFNB2; MYOVIIA; MYU7A; NSRD2;
                     USH1B"
                     /coded_by="NM_000260.4:291..6938"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53683.1"
                     /db_xref="GeneID:4647"
                     /db_xref="HGNC:HGNC:7606"
                     /db_xref="MIM:276903"
ORIGIN      
        1 mvilqqgdhv wmdlrlgqef dvpigavvkl cdsgqvqvvd dednehwisp qnathikpmh
       61 ptsvhgvedm irlgdlneag ilrnlliryr dhliytytgs ilvavnpyql lsiyspehir
      121 qytnkkigem pphifaiadn cyfnmkrnsr dqcciisges gagktestkl ilqflaaisg
      181 qhswieqqvl eatpileafg naktirndns srfgkyidih fnkrgaiega kieqylleks
      241 rvcrqalder nyhvfycmle gmsedqkkkl glgqasdyny lamgncitce grvdsqeyan
      301 irsamkvlmf tdtenweisk llaailhlgn lqyeartfen ldacevlfsp slataaslle
      361 vnppdlmscl tsrtlitrge tvstplsreq aldvrdafvk giygrlfvwi vdkinaaiyk
      421 ppsqdvknsr rsiglldifg fenfavnsfe qlcinfaneh lqqffvrhvf kleqeeydle
      481 sidwlhieft dnqdaldmia nkpmniisli deeskfpkgt dttmlhklns qhklnanyip
      541 pknnhetqfg inhfagivyy etqgfleknr dtlhgdiiql vhssrnkfik qifqadvamg
      601 aetrkrsptl ssqfkrslel lmrtlgacqp ffvrcikpne fkkpmlfdrh lcvrqlrysg
      661 mmetirirra gypirysfve fveryrvllp gvkpaykqgd lrgtcqrmae avlgthddwq
      721 igktkiflkd hhdmllever dkaitdrvil lqkvirgfkd rsnflklkna atliqrhwrg
      781 hncrknyglm rlgflrlqal hrsrklhqqy rlarqriiqf qarcraylvr kafrhrlwav
      841 ltvqayargm iarrlhqrlr aeylwrleae kmrlaeeekl rkemsakkak eeaerkhqer
      901 laqlaredae relkekeaar rkkelleqme rarhepvnhs dmvdkmfgfl gtsgglpgqe
      961 gqapsgfedl ergrremvee dldaalplpd edeedlseyk fakfaatyfq gttthsytrr
     1021 plkqpllyhd degdqlaala vwitilrfmg dlpepkyhta msdgsekipv mtkiyetlgk
     1081 ktykrelqal qgegeaqlpe gqkkssvrhk lvhltlkkks klteevtkrl hdgestvqgn
     1141 smledrptsn leklhfiign gilrpalrde iycqiskqlt hnpskssyar gwilvslcvg
     1201 cfapsekfvk ylrnfihggp pgyapyceer lrrtfvngtr tqppswlelq atkskkpiml
     1261 pvtfmdgttk tlltdsatta kelcnaladk islkdrfgfs lyialfdkvs slgsgsdhvm
     1321 daisqceqya keqgaqerna pwrlffrkev ftpwhspsed nvatnliyqq vvrgvkfgey
     1381 rcekeddlae lasqqyfvdy gsemilerll nlvptyipdr eitplktlek waqlaiaahk
     1441 kgiyaqrrtd aqkvkedvvs yarfkwpllf srfyeaykfs gpslpkndvi vavnwtgvyf
     1501 vdeqeqvlle lsfpeimavs ssrecrvwls lgcsdlgcaa phsgwagltp agpcspcwsc
     1561 rgakttapsf tlatikgdey tftssnaedi rdlvvtfleg lrkrskyvva lqdnpnpage
     1621 esgflsfakg dliildhdtg eqvmnsgwan ginertkqrg dfptdsvyvm ptvtmpprei
     1681 valvtmtpdq rqdvvrllql rtaepevrak pytleefsyd yfrpppkhtl srvmvskarg
     1741 kdrlwshtre plkqallkkl lgseelsqea clafiavlky mgdypskrtr svneltdqif
     1801 egplkaeplk deayvqilkq ltdnhiryse ergwellwlc tglfppsnil lphvqrflqs
     1861 rkhcplaidc lqrlqkalrn gsrkypphlv eveaiqhktt qifhkvyfpd dtdeafeves
     1921 stkakdfcqn iatrlllkss egfslfvkia dkvlsvpend fffdfvrhlt dwikkarpik
     1981 dgivpsltyq vffmkklwtt tvpgkdpmad sifhyyqelp kylrgyhkct reevlqlgal
     2041 iyrvkfeedk syfpsipkll relvpqdlir qvspddwkrs ivayfnkhag kskeeaklaf
     2101 lklifkwptf gsaffevkqt tepnfpeill iainkygvsl idpktkdilt thpftkisnw
     2161 ssgntyfhit ignlvrgskl lcetslgykm ddlltsyisq mltamskqrg srsgk
//
LOCUS       NP_060225                767 aa            linear   PRI 27-APR-2025
DEFINITION  RNA cytosine C(5)-methyltransferase NSUN2 isoform 1 [Homo sapiens].
ACCESSION   NP_060225
VERSION     NP_060225.4
DBSOURCE    REFSEQ: accession NM_017755.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Zhang,X., An,K., Ge,X., Sun,Y., Wei,J., Ren,W., Wang,H., Wang,Y.,
            Du,Y., He,L., Li,O., Zhou,S., Shi,Y., Ren,T., Yang,Y.G., Kan,Q. and
            Tian,X.
  TITLE     NSUN2/YBX1 promotes the progression of breast cancer by enhancing
            HGH1 mRNA stability through m5C methylation
  JOURNAL   Breast Cancer Res 26 (1), 94 (2024)
   PUBMED   38844963
  REMARK    GeneRIF: NSUN2/YBX1 promotes the progression of breast cancer by
            enhancing HGH1 mRNA stability through m[5]C methylation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Wang,R., Xue,W., Kan,F., Zhang,H., Wang,D., Wang,L. and Wang,J.
  TITLE     NSUN2 affects diabetic retinopathy progression by regulating MUC1
            expression through RNA m5C methylation
  JOURNAL   J Transl Med 22 (1), 476 (2024)
   PUBMED   38764010
  REMARK    GeneRIF: NSUN2 affects diabetic retinopathy progression by
            regulating MUC1 expression through RNA m[5]C methylation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Du,X., Cheng,C., Yang,Y., Fan,B., Wang,P., Xia,H., Ni,X., Liu,Q.,
            Lu,L. and Wei,L.
  TITLE     NSUN2 promotes lung adenocarcinoma progression through stabilizing
            PIK3R2 mRNA in an m5C-dependent manner
  JOURNAL   Mol Carcinog 63 (5), 962-976 (2024)
   PUBMED   38411298
  REMARK    GeneRIF: NSUN2 promotes lung adenocarcinoma progression through
            stabilizing PIK3R2 mRNA in an m[5]C-dependent manner.
REFERENCE   4  (residues 1 to 767)
  AUTHORS   Wang,X., Liu,D., Hua,K. and Fang,L.
  TITLE     LncRNA HOST2 promotes NSUN2-mediated breast cancer progression via
            interaction with ELAVL1
  JOURNAL   Cell Signal 117, 111112 (2024)
   PUBMED   38387687
  REMARK    GeneRIF: LncRNA HOST2 promotes NSUN2-mediated breast cancer
            progression via interaction with ELAVL1.
REFERENCE   5  (residues 1 to 767)
  AUTHORS   Chen,Y., Jiang,Z., Zhang,C., Zhang,L., Chen,H., Xiao,N., Bai,L.,
            Liu,H. and Wan,J.
  TITLE     5-Methylcytosine transferase NSUN2 drives NRF2-mediated ferroptosis
            resistance in non-small cell lung cancer
  JOURNAL   J Biol Chem 300 (4), 106793 (2024)
   PUBMED   38403250
  REMARK    GeneRIF: 5-Methylcytosine transferase NSUN2 drives NRF2-mediated
            ferroptosis resistance in non-small cell lung cancer.
REFERENCE   6  (residues 1 to 767)
  AUTHORS   Sakita-Suto,S., Kanda,A., Suzuki,F., Sato,S., Takata,T. and
            Tatsuka,M.
  TITLE     Aurora-B regulates RNA methyltransferase NSUN2
  JOURNAL   Mol Biol Cell 18 (3), 1107-1117 (2007)
   PUBMED   17215513
  REMARK    GeneRIF: These results indicate that Aurora-B participates to
            regulate the assembly of nucleolar RNA-processing machinery and the
            RNA methyltransferase activity of NSUN2 via phosphorylation at
            Ser139 during mitosis.
REFERENCE   7  (residues 1 to 767)
  AUTHORS   Najmabadi,H., Motazacker,M.M., Garshasbi,M., Kahrizi,K.,
            Tzschach,A., Chen,W., Behjati,F., Hadavi,V., Nieh,S.E.,
            Abedini,S.S., Vazifehmand,R., Firouzabadi,S.G., Jamali,P.,
            Falah,M., Seifati,S.M., Gruters,A., Lenzner,S., Jensen,L.R.,
            Ruschendorf,F., Kuss,A.W. and Ropers,H.H.
  TITLE     Homozygosity mapping in consanguineous families reveals extreme
            heterogeneity of non-syndromic autosomal recessive mental
            retardation and identifies 8 novel gene loci
  JOURNAL   Hum Genet 121 (1), 43-48 (2007)
   PUBMED   17120046
REFERENCE   8  (residues 1 to 767)
  AUTHORS   Brzezicha,B., Schmidt,M., Makalowska,I., Jarmolowski,A.,
            Pienkowska,J. and Szweykowska-Kulinska,Z.
  TITLE     Identification of human tRNA:m5C methyltransferase catalysing
            intron-dependent m5C formation in the first position of the
            anticodon of the pre-tRNA Leu (CAA)
  JOURNAL   Nucleic Acids Res 34 (20), 6034-6043 (2006)
   PUBMED   17071714
  REMARK    GeneRIF: First report showing intron-dependent methylation of human
            pre-tRNA Leu(CAA) and identification of human gene encoding tRNA
            methylase(Trm4) responsible for this reaction.
REFERENCE   9  (residues 1 to 767)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   10 (residues 1 to 767)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF000644.1, AB255451.1 and
            BC001041.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 17, 2003 this sequence version replaced NP_060225.3.
            
            Summary: This gene encodes a methyltransferase that catalyzes the
            methylation of cytosine to 5-methylcytosine (m5C) at position 34 of
            intron-containing tRNA(Leu)(CAA) precursors. This modification is
            necessary to stabilize the anticodon-codon pairing and correctly
            translate the mRNA. Alternatively spliced transcript variants
            encoding different isoforms have been noted for this gene.[provided
            by RefSeq, Mar 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC137083.1, AK291144.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264670.11/ ENSP00000264670.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.31"
     Protein         1..767
                     /product="RNA cytosine C(5)-methyltransferase NSUN2
                     isoform 1"
                     /EC_number="2.1.1.203"
                     /note="5-methycytoisine methyltransferase; Myc-induced
                     SUN-domain-containing protein; NOL1/NOP2/Sun domain
                     family, member 2; tRNA methyltransferase 4 homolog; tRNA
                     (cytosine-5-)-methyltransferase NSUN2; tRNA
                     (cytosine(34)-C(5))-methyltransferase; NOP2/Sun RNA
                     methyltransferase family member 2; substrate of
                     AIM1/Aurora kinase B; myc-induced SUN domain-containing
                     protein; mRNA cytosine C(5)-methyltransferase; tRNA
                     cytosine C(5)-methyltransferase; RNA cytosine
                     C(5)-methyltransferase NSUN2"
                     /calculated_mol_wt=86340
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08J23.2)"
     Region          <59..431
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:17215513; propagated from
                     UniProtKB/Swiss-Prot (Q08J23.2)"
     Region          436..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08J23.2)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q08J23.2)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08J23.2)"
     Site            586
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q1HFZ0; propagated from
                     UniProtKB/Swiss-Prot (Q08J23.2)"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q08J23.2)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q1HFZ0; propagated from
                     UniProtKB/Swiss-Prot (Q08J23.2)"
     Region          719..767
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08J23.2)"
     Site            724
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q1HFZ0; propagated from
                     UniProtKB/Swiss-Prot (Q08J23.2)"
     Site            743
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q08J23.2)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q08J23.2)"
     CDS             1..767
                     /gene="NSUN2"
                     /gene_synonym="MISU; MRT5; SAKI; TRM4"
                     /coded_by="NM_017755.6:66..2369"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3869.1"
                     /db_xref="GeneID:54888"
                     /db_xref="HGNC:HGNC:25994"
                     /db_xref="MIM:610916"
ORIGIN      
        1 mgrrsrgrrl qqqqrpedae dgaegggkrg eagweggype ivkenklfeh yyqelkivpe
       61 gewgqfmdal replpatlri tgykshakei lhclknkyfk eledlevdgq kvevpqplsw
      121 ypeelawhtn lsrkilrksp hlekfhqflv setesgnisr qeavsmippl llnvrphhki
      181 ldmcaapgsk ttqliemlha dmnvpfpegf viandvdnkr cyllvhqakr lsspcimvvn
      241 hdassiprlq idvdgrkeil fydrilcdvp csgdgtmrkn idvwkkwttl nslqlhglql
      301 riatrgaeql aeggrmvyst cslnpiedea viasllekse galeladvsn elpglkwmpg
      361 itqwkvmtkd gqwftdwdav phsrhtqirp tmfppkdpek lqamhlercl rilphhqntg
      421 gffvavlvkk ssmpwnkrqp klqgksaetr estqlspadl tegkptdpsk lespsftgtg
      481 dteiahated lenngskkdg vcgpppskkm klfgfkedpf vfipeddplf ppiekfyald
      541 psfprmnllt rttegkkrql ymvskelrnv llnnsekmkv intgikvwcr nnsgeefdca
      601 frlaqegiyt lypfinsrii tvsmedvkil ltqenpffrk lssetysqak dlakgsivlk
      661 yepdsanpda lqcpivlcgw rgkasirtfv pknerlhylr mmglevlgek kkegviltne
      721 saastgqpdn dvtegqrage pnspdaeean spdvtagcdp agvhppr
//
LOCUS       NP_666423                314 aa            linear   ROD 27-APR-2025
DEFINITION  olfactory receptor 5P81 [Mus musculus].
ACCESSION   NP_666423 XP_011240111
VERSION     NP_666423.1
DBSOURCE    REFSEQ: accession NM_146311.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Olender,T., Jones,T.E.M., Bruford,E. and Lancet,D.
  TITLE     A unified nomenclature for vertebrate olfactory receptors
  JOURNAL   BMC Evol Biol 20 (1), 42 (2020)
   PUBMED   32295537
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Young,J.M., Shykind,B.M., Lane,R.P., Tonnes-Priddy,L., Ross,J.A.,
            Walker,M., Williams,E.M. and Trask,B.J.
  TITLE     Odorant receptor expressed sequence tags demonstrate olfactory
            expression of over 400 genes, extensive alternate splicing and
            unequal expression levels
  JOURNAL   Genome Biol 4 (11), R71 (2003)
   PUBMED   14611657
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Young,J.M., Friedman,C., Williams,E.M., Ross,J.A., Tonnes-Priddy,L.
            and Trask,B.J.
  TITLE     Different evolutionary processes shaped the mouse and human
            olfactory receptor gene families
  JOURNAL   Hum Mol Genet 11 (5), 535-546 (2002)
   PUBMED   11875048
  REMARK    Erratum:[Hum Mol Genet. 2002 Jul 1;11(14):1683.]
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Zhang,X. and Firestein,S.
  TITLE     The olfactory receptor gene superfamily of the mouse
  JOURNAL   Nat Neurosci 5 (2), 124-133 (2002)
   PUBMED   11802173
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116579.4.
            
            On Apr 6, 2018 this sequence version replaced XP_011240111.1.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DR065926.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 57.21 cM"
     Protein         1..314
                     /product="olfactory receptor 5P81"
                     /note="olfactory receptor MOR204-34; olfactory receptor
                     204-34; olfactory receptor 510"
                     /calculated_mol_wt=34752
     Site            8
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VEW6.1)"
     Region          28..306
                     /region_name="7tmA_OR5P-like"
                     /note="olfactory receptor subfamily 5P and related
                     proteins, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15416"
                     /db_xref="CDD:320538"
     Region          29..55
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320538"
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEW6.1)"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEW6.1)"
     Region          62..88
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320538"
     Site            order(84,87..88,100..105,107..108,111,156,158..162,198,
                     201..203,205..207,209..210,255,258..259,261..262,265,
                     271..272,274..276,279,282..283)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320538"
     Region          100..130
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320538"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEW6.1)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEW6.1)"
     Region          143..164
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320538"
     Region          198..228
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320538"
     Site            200..220
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEW6.1)"
     Region          235..265
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320538"
     Site            241..261
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEW6.1)"
     Region          272..297
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320538"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VEW6.1)"
     CDS             1..314
                     /gene="Or5p81"
                     /gene_synonym="GA_x6K02T2PBJ9-10997715-10998659;
                     MOR204-34; Olfr510"
                     /coded_by="NM_146311.2:57..1001"
                     /db_xref="CCDS:CCDS21724.1"
                     /db_xref="GeneID:258308"
                     /db_xref="MGI:MGI:3030344"
ORIGIN      
        1 mafledgnht vvtefillgl tddpvlrvil fiiilciylv tvsgnlstil lirvssqlhh
       61 pmyfflshla sidiaisssv tpnmvvnflv erssisyigc giqlgsavff gaiecfllav
      121 maydrfvaic npllystkms kqvciqllvg syiggfihas fftlsfvsfl fcgpnrinhf
      181 fcdftplvel scsdnsvlii ldsfstgtii vitvfviais ytcilitilk mhstegrhka
      241 fstctshltv vtllygtvtf iyvmpkssys tdqnkvisvf ymvvipmlnp iiyslrnnei
      301 kgalkkqlge knif
//
LOCUS       NP_001010924             890 aa            linear   PRI 27-APR-2025
DEFINITION  protein FAM171A1 precursor [Homo sapiens].
ACCESSION   NP_001010924 XP_167709
VERSION     NP_001010924.1
DBSOURCE    REFSEQ: accession NM_001010924.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 890)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 890)
  AUTHORS   Rasila,T., Saavalainen,O., Attalla,H., Lankila,P., Haglund,C.,
            Holtta,E. and Andersson,L.C.
  TITLE     Astroprincin (FAM171A1, C10orf38): A Regulator of Human Cell Shape
            and Invasive Growth
  JOURNAL   Am J Pathol 189 (1), 177-189 (2019)
   PUBMED   30312582
  REMARK    GeneRIF: APCN regulates the dynamics of the actin cytoskeletal and,
            thereby, the cell shape and invasive growth potential of tumor
            cells.
REFERENCE   3  (residues 1 to 890)
  AUTHORS   Goldstein,J.I., Jarskog,L.F., Hilliard,C., Alfirevic,A., Duncan,L.,
            Fourches,D., Huang,H., Lek,M., Neale,B.M., Ripke,S., Shianna,K.,
            Szatkiewicz,J.P., Tropsha,A., van den Oord,E.J., Cascorbi,I.,
            Dettling,M., Gazit,E., Goff,D.C., Holden,A.L., Kelly,D.L.,
            Malhotra,A.K., Nielsen,J., Pirmohamed,M., Rujescu,D., Werge,T.,
            Levy,D.L., Josiassen,R.C., Kennedy,J.L., Lieberman,J.A., Daly,M.J.
            and Sullivan,P.F.
  TITLE     Clozapine-induced agranulocytosis is associated with rare HLA-DQB1
            and HLA-B alleles
  JOURNAL   Nat Commun 5, 4757 (2014)
   PUBMED   25187353
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 890)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139338.21, AL050367.1, BX496483.1, AK022946.1 and BC034232.1.
            
            On May 5, 2005 this sequence version replaced XP_167709.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY683003.1, SRR1803612.37606.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153307 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378116.9/ ENSP00000367356.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..890
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..890
                     /product="protein FAM171A1 precursor"
                     /note="astroprincin; protein FAM171A1"
                     /calculated_mol_wt=95570
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
                     /calculated_mol_wt=2303
     mat_peptide     22..890
                     /product="Protein FAM171A1. /id=PRO_0000274263"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUB5.1)"
                     /calculated_mol_wt=95570
     Region          34..888
                     /region_name="UPF0560"
                     /note="Uncharacterized protein family UPF0560; pfam10577"
                     /db_xref="CDD:463154"
     Site            159
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:30312582; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30312582; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            304..324
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Region          730..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Region          818..890
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            849
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     Site            855
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18318008; propagated from
                     UniProtKB/Swiss-Prot (Q5VUB5.1)"
     CDS             1..890
                     /gene="FAM171A1"
                     /gene_synonym="APCN; C10orf38"
                     /coded_by="NM_001010924.2:238..2910"
                     /db_xref="CCDS:CCDS31154.1"
                     /db_xref="GeneID:221061"
                     /db_xref="HGNC:HGNC:23522"
ORIGIN      
        1 msrsatlllc llgchvwkav tktlrepgag aqevtlkvhi sdasthqpva dalieiftnq
       61 asiasgtsgt dgvafikfqy klgsqlivta skhayvpnsa pwkpirlpvf sslslgllpe
      121 rsatlmvyed vvqivsgfqg arpqprvhfq rralrlpent sysdltaflt aasspsevds
      181 fpylrgldgn gtgnstrhdl tpvtavsvhl lssngtpvlv dgpiyvtvpl atqsslrhna
      241 yvaawrfdqk lgtwlksglg lvhqegsqlt wtyiapqlgy wvaamsppip gpvvtqditt
      301 yhtvfllail ggmafillvl lclllyycrr kclkprqhhr klqlpagles skrdqstsms
      361 hinllfsrra sefpgplsvt shgrpeapgt kelmsgvhle mmspggegdl htpmlklsys
      421 tsqefssree llsckeedks qisfdnltps gtlgkdyhks vevfplkark smeregyess
      481 gnddyrgsyn tvlsqplfek qdregpastg skltiqehly papsspekeq lldrrptecm
      541 msrsvdhler ptsfprpgql iccssvdqvn dsvyrkvlpa lvipahymkl pgdhsyvsqp
      601 lvvpadqqle ierlqaelsn phagifphps sqiqpqplss qaisqqhlqd agtrewspqn
      661 asmseslsip aslndaalaq mnsevqllte kalmelgggk plphprawfv sldgrsnahv
      721 rhsyidlqra grngsndasl dsgvdmnepk sarkgrgdal slqqnyppvq ehqqkeprap
      781 dstaytqlvy lddveqsgse cgttvctped salrcllegs srrsggqlps lqeettrrta
      841 dapsepaasp hqrrsaheee eddddddqge dkkspwqkre erplmafnik
//
LOCUS       NP_065846                835 aa            linear   PRI 27-APR-2025
DEFINITION  neuroligin-2 precursor [Homo sapiens].
ACCESSION   NP_065846
VERSION     NP_065846.1
DBSOURCE    REFSEQ: accession NM_020795.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Zhang,Z., Hou,M., Ou,H., Wang,D., Li,Z., Zhang,H. and Lu,J.
  TITLE     Expression and structural analysis of human neuroligin 2 and
            neuroligin 3 implicated in autism spectrum disorders
  JOURNAL   Front Endocrinol (Lausanne) 13, 1067529 (2022)
   PUBMED   36479216
  REMARK    GeneRIF: Expression and structural analysis of human neuroligin 2
            and neuroligin 3 implicated in autism spectrum disorders.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Schafer,J., Forster,L., Mey,I., Papadopoulos,T., Brose,N. and
            Steinem,C.
  TITLE     Neuroligin-2 dependent conformational activation of collybistin
            reconstituted in supported hybrid membranes
  JOURNAL   J Biol Chem 295 (52), 18604-18613 (2020)
   PUBMED   33127642
  REMARK    GeneRIF: Neuroligin-2 dependent conformational activation of
            collybistin reconstituted in supported hybrid membranes.
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Ali,H., Marth,L. and Krueger-Burg,D.
  TITLE     Neuroligin-2 as a central organizer of inhibitory synapses in
            health and disease
  JOURNAL   Sci Signal 13 (663) (2020)
   PUBMED   33443230
  REMARK    GeneRIF: Neuroligin-2 as a central organizer of inhibitory synapses
            in health and disease.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Heshmati,M., Aleyasin,H., Menard,C., Christoffel,D.J.,
            Flanigan,M.E., Pfau,M.L., Hodes,G.E., Lepack,A.E., Bicks,L.K.,
            Takahashi,A., Chandra,R., Turecki,G., Lobo,M.K., Maze,I.,
            Golden,S.A. and Russo,S.J.
  TITLE     Cell-type-specific role for nucleus accumbens neuroligin-2 in
            depression and stress susceptibility
  JOURNAL   Proc Natl Acad Sci U S A 115 (5), 1111-1116 (2018)
   PUBMED   29339486
  REMARK    GeneRIF: nucleus accumbens neuroligin-2 has a role in depression
            and stress susceptibility
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Gangwar,S.P., Zhong,X., Seshadrinathan,S., Chen,H., Machius,M. and
            Rudenko,G.
  TITLE     Molecular Mechanism of MDGA1: Regulation of Neuroligin 2:Neurexin
            Trans-synaptic Bridges
  JOURNAL   Neuron 94 (6), 1132-1141 (2017)
   PUBMED   28641112
  REMARK    GeneRIF: MDGAs regulate the formation of neuroligin-neurexin
            trans-synaptic bridges by sterically blocking access of neurexins
            to neuroligins.
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Scheiffele,P., Fan,J., Choih,J., Fetter,R. and Serafini,T.
  TITLE     Neuroligin expressed in nonneuronal cells triggers presynaptic
            development in contacting axons
  JOURNAL   Cell 101 (6), 657-669 (2000)
   PUBMED   10892652
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Philibert,R.A., Winfield,S.L., Sandhu,H.K., Martin,B.M. and
            Ginns,E.I.
  TITLE     The structure and expression of the human neuroligin-3 gene
  JOURNAL   Gene 246 (1-2), 303-310 (2000)
   PUBMED   10767552
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Kurschner,C., Mermelstein,P.G., Holden,W.T. and Surmeier,D.J.
  TITLE     CIPP, a novel multivalent PDZ domain protein, selectively interacts
            with Kir4.0 family members, NMDA receptor subunits, neurexins, and
            neuroligins
  JOURNAL   Mol Cell Neurosci 11 (3), 161-172 (1998)
   PUBMED   9647694
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Irie,M., Hata,Y., Takeuchi,M., Ichtchenko,K., Toyoda,A., Hirao,K.,
            Takai,Y., Rosahl,T.W. and Sudhof,T.C.
  TITLE     Binding of neuroligins to PSD-95
  JOURNAL   Science 277 (5331), 1511-1515 (1997)
   PUBMED   9278515
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Ichtchenko,K., Nguyen,T. and Sudhof,T.C.
  TITLE     Structures, alternative splicing, and neurexin binding of multiple
            neuroligins
  JOURNAL   J Biol Chem 271 (5), 2676-2682 (1996)
   PUBMED   8576240
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113189.11, AF376802.1,
            BM800364.1, DR763679.1, EL949788.1, AA447769.1 and AI613237.1.
            
            Summary: This gene encodes a member of a family of neuronal cell
            surface proteins. Members of this family may act as splice
            site-specific ligands for beta-neurexins and may be involved in the
            formation and remodeling of central nervous system synapses.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF376802.1, SRR9304719.239650.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302926.7/ ENSP00000305288.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..835
                     /product="neuroligin-2 precursor"
                     /calculated_mol_wt=89408
     sig_peptide     1..14
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1431
     mat_peptide     15..835
                     /product="Neuroligin-2. /id=PRO_0000008643"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ4.1)"
                     /calculated_mol_wt=89408
     Region          42..601
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Site            order(185..187,264..266,269,419..420,455,501,504)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(265,386,500)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Site            522
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Region          623..668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Region          678..698
                     /region_name="Required for interaction with LHFPL4.
                     /evidence=ECO:0000250|UniProtKB:Q69ZK9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Site            678..698
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZK9; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZK9; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Region          790..835
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     CDS             1..835
                     /gene="NLGN2"
                     /coded_by="NM_020795.4:412..2919"
                     /db_xref="CCDS:CCDS11103.1"
                     /db_xref="GeneID:57555"
                     /db_xref="HGNC:HGNC:14290"
                     /db_xref="MIM:606479"
ORIGIN      
        1 mwllalclvg lagaqrgggg pgggapggpg lglgslgeer fpvvntaygr vrgvrrelnn
       61 eilgpvvqfl gvpyatpplg arrfqppeap aswpgvrnat tlppacpqnl hgalpaimlp
      121 vwftdnleaa atyvqnqsed clylnlyvpt edgpltkkrd eatlnppdtd irdpgkkpvm
      181 lflhggsyme gtgnmfdgsv laaygnviva tlnyrlgvlg flstgdqaak gnyglldqiq
      241 alrwlsenia hfggdperit ifgsgagasc vnllilshhs eglfqkaiaq sgtaisswsv
      301 nyqplkytrl laakvgcdre dsaeaveclr rkpsrelvdq dvqparyhia fgpvvdgdvv
      361 pddpeilmqq geflnydmli gvnqgeglkf vedsaesedg vsasafdftv snfvdnlygy
      421 pegkdvlret ikfmytdwad rdngemrrkt llalftdhqw vapavatakl hadyqspvyf
      481 ytfyhhcqae grpewadaah gdelpyvfgv pmvgatdlfp cnfskndvml savvmtywtn
      541 faktgdpnqp vpqdtkfiht kpnrfeevvw skfnskekqy lhiglkprvr dnyrankvaf
      601 wlelvphlhn lhtelftttt rlppyatrwp prppagapgt rrppppatlp pepepepgpr
      661 aydrfpgdsr dystelsvtv avgasllfln ilafaalyyk rdrrqelrcr rlsppggsgs
      721 gvpgggpllp aagrelppee elvslqlkrg ggvgadpaea lrpacppdyt lalrrapddv
      781 pllapgaltl lpsglgpppp ppppslhpfg pfppppptat shnntlphph sttrv
//
LOCUS       NP_001350315             262 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 821 isoform b [Mus musculus].
ACCESSION   NP_001350315 NP_001350316 XP_011246839
VERSION     NP_001350315.1
DBSOURCE    REFSEQ: accession NM_001363386.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Sharov,A.A., Piao,Y., Matoba,R., Dudekula,D.B., Qian,Y.,
            VanBuren,V., Falco,G., Martin,P.R., Stagg,C.A., Bassey,U.C.,
            Wang,Y., Carter,M.G., Hamatani,T., Aiba,K., Akutsu,H., Sharova,L.,
            Tanaka,T.S., Kimber,W.L., Yoshikawa,T., Jaradat,S.A., Pantano,S.,
            Nagaraja,R., Boheler,K.R., Taub,D., Hodes,R.J., Longo,D.L.,
            Schlessinger,D., Keller,J., Klotz,E., Kelsoe,G., Umezawa,A.,
            Vescovi,A.L., Rossant,J., Kunath,T., Hogan,B.L., Curci,A.,
            D'Urso,M., Kelso,J., Hide,W. and Ko,M.S.
  TITLE     Transcriptome analysis of mouse stem cells and early embryos
  JOURNAL   PLoS Biol 1 (3), E74 (2003)
   PUBMED   14691545
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132138.2, BM950913.1 and BC059014.1.
            
            On May 20, 2019 this sequence version replaced NP_001350316.1.
            
            Transcript Variant: This variant (11), as well as variants 3, 4, 9,
            and 10, encodes isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.2615511.1,
                                           ERR3363660.2907581.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 57.21 cM"
     Protein         1..262
                     /product="zinc finger protein 821 isoform b"
                     /calculated_mol_wt=30046
     Region          2..22
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <110..>184
                     /region_name="COG2433"
                     /note="Possible nuclease of RNase H fold, RuvC/YqgF family
                     [General function prediction only]"
                     /db_xref="CDD:441980"
     CDS             1..262
                     /gene="Zfp821"
                     /gene_synonym="4930566A11Rik; Znf821"
                     /coded_by="NM_001363386.1:1067..1855"
                     /note="isoform b is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS85609.1"
                     /db_xref="GeneID:75871"
                     /db_xref="MGI:MGI:1923121"
ORIGIN      
        1 mcpvcgrals spgslgrhll ihsedqrsnc avcgarftsh atfnseklpq vlnmesvpqv
       61 hsegpssaeg kdiacsppvy pagillvcnn caayrkllet qtpsvrkwal rrqneplevr
      121 lqrlererta kksrrdnetp eerevrrmrd reakrlqrmq etdeqrarrl qrdreamrlk
      181 ranetpekrq arlirereak rlkrrlekmd mmlraqfgqd psamaalaae mnffqlpvsg
      241 veldsqllgk mafeeqnnss lh
//
LOCUS       NP_004909                128 aa            linear   PRI 27-APR-2025
DEFINITION  T-cell leukemia/lymphoma protein 1B [Homo sapiens].
ACCESSION   NP_004909
VERSION     NP_004909.1
DBSOURCE    REFSEQ: accession NM_004918.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Badve,S., Collins,N.R., Bhat-Nakshatri,P., Turbin,D., Leung,S.,
            Thorat,M., Dunn,S.E., Geistlinger,T.R., Carroll,J.S., Brown,M.,
            Bose,S., Teitell,M.A. and Nakshatri,H.
  TITLE     Subcellular localization of activated AKT in estrogen receptor- and
            progesterone receptor-expressing breast cancers: potential clinical
            implications
  JOURNAL   Am J Pathol 176 (5), 2139-2149 (2010)
   PUBMED   20228224
  REMARK    GeneRIF: subcellular localization of activated AKT is dependent on
            TCL1B expression in estrogen receptor- and progesterone
            receptor-expressing breast cancer
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Laine,J., Kunstle,G., Obata,T. and Noguchi,M.
  TITLE     Differential regulation of Akt kinase isoforms by the members of
            the TCL1 oncogene family
  JOURNAL   J Biol Chem 277 (5), 3743-3751 (2002)
   PUBMED   11707444
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Pekarsky,Y., Hallas,C. and Croce,C.M.
  TITLE     The role of TCL1 in human T-cell leukemia
  JOURNAL   Oncogene 20 (40), 5638-5643 (2001)
   PUBMED   11607815
  REMARK    Review article
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Laine,J., Kunstle,G., Obata,T., Sha,M. and Noguchi,M.
  TITLE     The protooncogene TCL1 is an Akt kinase coactivator
  JOURNAL   Mol Cell 6 (2), 395-407 (2000)
   PUBMED   10983986
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Saitou,M., Sugimoto,J., Hatakeyama,T., Russo,G. and Isobe,M.
  TITLE     Identification of the TCL6 genes within the breakpoint cluster
            region on chromosome 14q32 in T-cell leukemia
  JOURNAL   Oncogene 19 (23), 2796-2802 (2000)
   PUBMED   10851082
REFERENCE   8  (residues 1 to 128)
  AUTHORS   Sugimoto,J., Hatakeyama,T., Narducci,M.G., Russo,G. and Isobe,M.
  TITLE     Identification of the TCL1/MTCP1-like 1 (TML1) gene from the region
            next to the TCL1 locus
  JOURNAL   Cancer Res 59 (10), 2313-2317 (1999)
   PUBMED   10344735
REFERENCE   9  (residues 1 to 128)
  AUTHORS   Pekarsky,Y., Hallas,C., Isobe,M., Russo,G. and Croce,C.M.
  TITLE     Abnormalities at 14q32.1 in T cell malignancies involve two
            oncogenes
  JOURNAL   Proc Natl Acad Sci U S A 96 (6), 2949-2951 (1999)
   PUBMED   10077617
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC051000.1 and AF137027.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC051000.1, AF137027.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340722.8/ ENSP00000343223.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.13"
     Protein         1..128
                     /product="T-cell leukemia/lymphoma protein 1B"
                     /note="T-cell lymphoma/leukemia 1B; TCL1/ MTCP1-like 1;
                     oncogene TCL-1B; syncytiotrophoblast-specific protein; T
                     cell leukemia/lymphoma 1B"
                     /calculated_mol_wt=14715
     Region          1..124
                     /region_name="TCL1_MTCP1"
                     /note="TCL1/MTCP1 family; pfam01840"
                     /db_xref="CDD:460358"
     CDS             1..128
                     /gene="TCL1B"
                     /gene_synonym="SYN-1; TML1"
                     /coded_by="NM_004918.4:43..429"
                     /db_xref="CCDS:CCDS32151.1"
                     /db_xref="GeneID:9623"
                     /db_xref="HGNC:HGNC:11649"
                     /db_xref="MIM:603769"
ORIGIN      
        1 maseasvrlg vppgrlwiqr pgiyedeegr twvtvvvrfn psrrewaras qgsryepsit
       61 vhlwqmavht rellssgqmp fsqlpavwql ypgrkyraad ssfweiadhg qidsmeqlvl
      121 tyqperkd
//
LOCUS       NP_001356706             246 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase MARCHF2 isoform 1 [Homo sapiens].
ACCESSION   NP_001356706
VERSION     NP_001356706.1
DBSOURCE    REFSEQ: accession NM_001369777.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Ni,D., Qi,Z., Wang,Y., Man,Y., Pang,J., Tang,W., Chen,J., Li,J. and
            Li,G.
  TITLE     KLF15-activated MARCH2 boosts cell proliferation and
            epithelial-mesenchymal transition and presents diagnostic
            significance for hepatocellular carcinoma
  JOURNAL   Exp Cell Res 440 (1), 114117 (2024)
   PUBMED   38848952
  REMARK    GeneRIF: KLF15-activated MARCH2 boosts cell proliferation and
            epithelial-mesenchymal transition and presents diagnostic
            significance for hepatocellular carcinoma.
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Seo,T., Lowery,A.M., Xu,H., Giang,W., Troyanovsky,S.M.,
            Vincent,P.A. and Kowalczyk,A.P.
  TITLE     MARCH family E3 ubiquitin ligases selectively target and degrade
            cadherin family proteins
  JOURNAL   PLoS One 19 (5), e0290485 (2024)
   PUBMED   38722959
  REMARK    GeneRIF: MARCH family E3 ubiquitin ligases selectively target and
            degrade cadherin family proteins.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Ito,K., Harada,I., Martinez,C., Sato,K., Lee,E., Port,E.,
            Byerly,J.H., Nayak,A., Tripathi,E., Zhu,J. and Irie,H.Y.
  TITLE     MARCH2, a Novel Oncogene-regulated SNAIL E3 Ligase, Suppresses
            Triple-negative Breast Cancer Metastases
  JOURNAL   Cancer Res Commun 4 (3), 946-957 (2024)
   PUBMED   38457262
  REMARK    GeneRIF: MARCH2, a Novel Oncogene-regulated SNAIL E3 Ligase,
            Suppresses Triple-negative Breast Cancer Metastases.
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Yu,C., Bai,Y., Tan,W., Bai,Y., Li,X., Zhou,Y., Zhai,J., Xue,M.,
            Tang,Y.D., Zheng,C. and Liu,Q.
  TITLE     Human MARCH1, 2, and 8 block Ebola virus envelope glycoprotein
            cleavage via targeting furin P domain
  JOURNAL   J Med Virol 96 (2), e29445 (2024)
   PUBMED   38299743
  REMARK    GeneRIF: Human MARCH1, 2, and 8 block Ebola virus envelope
            glycoprotein cleavage via targeting furin P domain.
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Chathuranga,K., Kim,T.H., Lee,H., Park,J.S., Kim,J.H.,
            Chathuranga,W.A.G., Ekanayaka,P., Choi,Y.J., Lee,C.H., Kim,C.J.,
            Jung,J.U. and Lee,J.S.
  TITLE     Negative regulation of NEMO signaling by the ubiquitin E3 ligase
            MARCH2
  JOURNAL   EMBO J 39 (21), e105139 (2020)
   PUBMED   32935379
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   8  (residues 1 to 246)
  AUTHORS   Fukuda,H., Nakamura,N. and Hirose,S.
  TITLE     MARCH-III Is a novel component of endosomes with properties similar
            to those of MARCH-II
  JOURNAL   J Biochem 139 (1), 137-145 (2006)
   PUBMED   16428329
REFERENCE   9  (residues 1 to 246)
  AUTHORS   Nakamura,N., Fukuda,H., Kato,A. and Hirose,S.
  TITLE     MARCH-II is a syntaxin-6-binding protein involved in endosomal
            trafficking
  JOURNAL   Mol Biol Cell 16 (4), 1696-1710 (2005)
   PUBMED   15689499
  REMARK    GeneRIF: Depletion of MARCH-II by small interfering RNA perturbed
            the trans-Golgi network (TGN) localization of syntaxin 6 and
            TGN38/46
REFERENCE   10 (residues 1 to 246)
  AUTHORS   Bartee,E., Mansouri,M., Hovey Nerenberg,B.T., Gouveia,K. and
            Fruh,K.
  TITLE     Downregulation of major histocompatibility complex class I by human
            ubiquitin ligases related to viral immune evasion proteins
  JOURNAL   J Virol 78 (3), 1109-1120 (2004)
   PUBMED   14722266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC136469.2.
            
            Summary: MARCH2 is a member of the MARCH family of membrane-bound
            E3 ubiquitin ligases (EC 6.3.2.19). MARCH enzymes add ubiquitin
            (see MIM 191339) to target lysines in substrate proteins, thereby
            signaling their vesicular transport between membrane compartments.
            MARCH2 reduces surface accumulation of several glycoproteins and
            appears to regulate early endosome-to-trans-Golgi network (TGN)
            trafficking (Bartee et al., 2004 [PubMed 14722266]; Nakamura et
            al., 2005 [PubMed 15689499]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 4. Variants 1, 2, and 4-7 all encode the longer isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138522.665637.1,
                                           DRR138524.115077.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..246
                     /product="E3 ubiquitin-protein ligase MARCHF2 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="membrane-associated RING-CH protein II;
                     membrane-associated ring finger (C3HC4) 2, E3 ubiquitin
                     protein ligase; membrane associated ring finger 2; E3
                     ubiquitin-protein ligase MARCH2; RING finger protein 172;
                     membrane-associated RING finger protein 2; RING-type E3
                     ubiquitin transferase MARCHF2; E3 ubiquitin-protein ligase
                     MARCHF2; RING-type E3 ubiquitin transferase MARCH2"
                     /calculated_mol_wt=26864
     Region          56..116
                     /region_name="Required for inhibition of HIV-1 virus
                     production and VSV G protein expression.
                     /evidence=ECO:0000269|PubMed:29573664"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0N8.1)"
     Region          62..113
                     /region_name="RING_CH-C4HC3_MARCH2"
                     /note="RING-CH finger, H2 subclass (C4HC3-type), found in
                     membrane-associated RING-CH2 (MARCH2); cd16808"
                     /db_xref="CDD:319722"
     Region          121..246
                     /region_name="Required for interaction with IKBKG.
                     /evidence=ECO:0000269|PubMed:32935379"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0N8.1)"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0N8.1)"
     Site            175..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0N8.1)"
     CDS             1..246
                     /gene="MARCHF2"
                     /gene_synonym="HSPC240; MARCH-II; MARCH2; RNF172"
                     /coded_by="NM_001369777.1:235..975"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS12202.1"
                     /db_xref="GeneID:51257"
                     /db_xref="HGNC:HGNC:28038"
                     /db_xref="MIM:613332"
ORIGIN      
        1 mttgdcchlp gslcdcsgsp afskvveatg lgppqyvaqv tsrdgrllst viraldtpsd
       61 gpfcricheg angecllspc gctgtlgavh ksclekwlss sntsycelch tefavekrpr
      121 pltewlkdpg prtekrtlcc dmvcflfitp laaisgwlcl rgaqdhlrlh sqleavglia
      181 ltialftiyv lwtlvsfryh cqlysewrkt nqkvrlkire adspegpqhs plaagllkkv
      241 aeetpv
//
LOCUS       NP_110415                470 aa            linear   PRI 27-APR-2025
DEFINITION  dendritic cell-specific transmembrane protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_110415
VERSION     NP_110415.1
DBSOURCE    REFSEQ: accession NM_030788.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Lee,J.J., Hsu,Y.C., Huang,W.C. and Cheng,S.P.
  TITLE     Upregulation of dendrocyte-expressed seven transmembrane protein is
            associated with unfavorable outcomes in differentiated thyroid
            cancer
  JOURNAL   Endocrine 81 (3), 513-520 (2023)
   PUBMED   37058220
  REMARK    GeneRIF: Upregulation of dendrocyte-expressed seven transmembrane
            protein is associated with unfavorable outcomes in differentiated
            thyroid cancer.
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Mullin,B.H., Zhu,K., Brown,S.J., Mullin,S., Tickner,J.,
            Pavlos,N.J., Dudbridge,F., Xu,J., Walsh,J.P. and Wilson,S.G.
  TITLE     Genetic regulatory mechanisms in human osteoclasts suggest a role
            for the STMP1 and DCSTAMP genes in Paget's disease of bone
  JOURNAL   Sci Rep 9 (1), 1052 (2019)
   PUBMED   30705363
  REMARK    GeneRIF: Genetic regulatory mechanisms in human osteoclasts suggest
            a role for the STMP1 and DCSTAMP genes in Paget's disease of bone.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Laurier,E., Amiable,N., Gagnon,E., Brown,J.P. and Michou,L.
  TITLE     Effect of a rare genetic variant of TM7SF4 gene on osteoclasts of
            patients with Paget's disease of bone
  JOURNAL   BMC Med Genet 18 (1), 133 (2017)
   PUBMED   29145829
  REMARK    GeneRIF: Our results suggest that the rare genetic variant of
            TM7SF4 gene, found in our French-Canadian cohort of patients with
            Paget's disease of bone and which encodes the DC-STAMP protein,
            increase the number of nuclei per multinucleated cells and affect
            DC-STAMP expression during osteoclastogenesis in Paget's disease of
            bone.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Yang,X., Song,X., Wang,X., Liu,X. and Peng,Z.
  TITLE     Downregulation of TM7SF4 inhibits cell proliferation and metastasis
            of A549 cells through regulating the PI3K/AKT/mTOR signaling
            pathway
  JOURNAL   Mol Med Rep 16 (5), 6122-6127 (2017)
   PUBMED   28849122
  REMARK    GeneRIF: TM7SF4 may be involved in the progression of lung cancer.
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Zeng,X.X., Chu,T.J., Yuan,J.Y., Zhang,W., Du,Y.M., Ban,Z.Y.,
            Lei,D.M., Cao,J. and Zhang,Z.
  TITLE     Transmembrane 7 superfamily member 4 regulates cell cycle
            progression in breast cancer cells
  JOURNAL   Eur Rev Med Pharmacol Sci 19 (22), 4353-4361 (2015)
   PUBMED   26636523
  REMARK    GeneRIF: TM7SF4 plays an essential role in regulating cell cycle
            progression in breast cancer.
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Jansen,B.J., Eleveld-Trancikova,D., Sanecka,A., van Hout-Kuijer,M.,
            Hendriks,I.A., Looman,M.G., Leusen,J.H. and Adema,G.J.
  TITLE     OS9 interacts with DC-STAMP and modulates its intracellular
            localization in response to TLR ligation
  JOURNAL   Mol Immunol 46 (4), 505-515 (2009)
   PUBMED   18952287
  REMARK    GeneRIF: An interaction between OS9 and DC-STAMP was confirmed by
            yeast-2-hybrid analysis and cellular colocalization.ER-to-Golgi
            translocation of DC-STAMP following TLR stimulation in CHO cells
            was demonstrated, involving the DC-STAMP/OS9 interaction. The data
            indicate that OS9 is critically involved in ER-to-Golgi transport
            of DC-STAMP, and may be important in both myeloid differentiation
            and cell fusion.
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Eleveld-Trancikova,D., Triantis,V., Moulin,V., Looman,M.W.,
            Wijers,M., Fransen,J.A., Lemckert,A.A., Havenga,M.J., Figdor,C.G.,
            Janssen,R.A. and Adema,G.J.
  TITLE     The dendritic cell-derived protein DC-STAMP is highly conserved and
            localizes to the endoplasmic reticulum
  JOURNAL   J Leukoc Biol 77 (3), 337-343 (2005)
   PUBMED   15601667
  REMARK    GeneRIF: The dendritic cell-specific transmembrane protein is a
            multimembrane-spanning protein preferentially expressed by human DC
            (hDC).
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Hartgers,F.C., Looman,M.W., van der Woning,B., Merkx,G.F.,
            Figdor,C.G. and Adema,G.J.
  TITLE     Genomic organization, chromosomal localization, and 5' upstream
            region of the human DC-STAMP gene
  JOURNAL   Immunogenetics 53 (2), 145-149 (2001)
   PUBMED   11345591
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Staege,H., Brauchlin,A., Schoedon,G. and Schaffner,A.
  TITLE     Two novel genes FIND and LIND differentially expressed in
            deactivated and Listeria-infected human macrophages
  JOURNAL   Immunogenetics 53 (2), 105-113 (2001)
   PUBMED   11345586
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Hartgers,F.C., Vissers,J.L., Looman,M.W., van Zoelen,C.,
            Huffine,C., Figdor,C.G. and Adema,G.J.
  TITLE     DC-STAMP, a novel multimembrane-spanning molecule preferentially
            expressed by dendritic cells
  JOURNAL   Eur J Immunol 30 (12), 3585-3590 (2000)
   PUBMED   11169400
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC069349.1, AP003471.2 and
            AF277290.1.
            
            Summary: This gene encodes a seven-pass transmembrane protein that
            is primarily expressed in dendritic cells. The encoded protein is
            involved in a range of immunological functions carried out by
            dendritic cells. This protein plays a role in osteoclastogenesis
            and myeloid differentiation. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Mar 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF277290.1, AF305068.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297581.2/ ENSP00000297581.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..470
                     /product="dendritic cell-specific transmembrane protein
                     isoform 1"
                     /note="IL-Four (IL-4) induced; DC-specific transmembrane
                     protein; IL-Four INDuced; Dendritic cells (DC)-specific
                     transmembrane protein; IL-4-induced protein; dendritic
                     cell-specific transmembrane protein; transmembrane 7
                     superfamily member 4; IL-four-induced protein"
                     /calculated_mol_wt=53262
     Site            35..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H295.1)"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H295.1)"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H295.1)"
     Site            210..230
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H295.1)"
     Region          242..421
                     /region_name="DC_STAMP"
                     /note="DC-STAMP-like protein; pfam07782"
                     /db_xref="CDD:462265"
     Site            293..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H295.1)"
     Site            377..397
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H295.1)"
     CDS             1..470
                     /gene="DCSTAMP"
                     /gene_synonym="FIND; hDC-STAMP; TM7SF4"
                     /coded_by="NM_030788.4:50..1462"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6301.1"
                     /db_xref="GeneID:81501"
                     /db_xref="HGNC:HGNC:18549"
                     /db_xref="MIM:605933"
ORIGIN      
        1 mgiwtsgtdi flslweiyvs prspgwmdfi qhlgvcclva lisvgllsva acwflpsiia
       61 aaaswiitcv llccskharc fillvflscg lregrnalia agtgivilgh venifhnfkg
      121 lldgmtcnlr aksfsihfpl lkkyieaiqw iyglatplsv fddlvswnqt lavslfspsh
      181 vleaqlndsk gevlsvlyqm atttevlssl gqkllafagl slvllgtglf mkrflgpcgw
      241 kyeniyitrq fvqfdererh qqrpcvlpln keerrkyvii ptfwptpker knlglfflpi
      301 lihlciwvlf aavdyllyrl ifsvskqfqs lpgfevhlkl hgekqgtqdi ihdssfnisv
      361 fepncipkpk fllsetwvpl svillilvml gllssilmql kilvsasfyp sverkriqyl
      421 hakllkkrsk qplgevkrrl slyltkihfw lpvlkmirkk qmdmasadks
//
LOCUS       NP_001193996             419 aa            linear   PRI 27-APR-2025
DEFINITION  eIF5-mimic protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001193996
VERSION     NP_001193996.1
DBSOURCE    REFSEQ: accession NM_001207067.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Zhang,W., Zhang,N., Yang,Z., Zhang,X., Sun,A., Wang,L., Song,X.,
            Geng,Z., Li,J. and Hu,J.
  TITLE     [Overexpression of BZW1 promotes invasion and metastasis of gastric
            cancer cells by regulating Wnt/beta-catenin signaling and promoting
            epithelial-mesenchymal transition]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 44 (2), 354-362 (2024)
   PUBMED   38501421
  REMARK    GeneRIF: [Overexpression of BZW1 promotes invasion and metastasis
            of gastric cancer cells by regulating Wnt/beta-catenin signaling
            and promoting epithelial-mesenchymal transition].
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Luo,A., Qiao,N., Hu,K., Xu,H., Xie,M., Jiang,Y. and Hu,J.
  TITLE     BZW1 is a prognostic and immunological biomarker in pancreatic
            adenocarcinoma
  JOURNAL   Medicine (Baltimore) 103 (5), e37092 (2024)
   PUBMED   38306570
  REMARK    GeneRIF: BZW1 is a prognostic and immunological biomarker in
            pancreatic adenocarcinoma.
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Qi,H., Zheng,Z. and Liu,Q.
  TITLE     Activation of BZW1 by CEBPB in macrophages promotes eIF2alpha
            phosphorylation-mediated metabolic reprogramming and endoplasmic
            reticulum stress in MRL/lpr lupus-prone mice
  JOURNAL   Cell Mol Biol Lett 28 (1), 79 (2023)
   PUBMED   37828427
  REMARK    GeneRIF: Activation of BZW1 by CEBPB in macrophages promotes
            eIF2alpha phosphorylation-mediated metabolic reprogramming and
            endoplasmic reticulum stress in MRL/lpr lupus-prone mice.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Li,Z., Ge,Y., Dong,J., Wang,H., Zhao,T., Wang,X., Liu,J., Gao,S.,
            Shi,L., Yang,S., Huang,C. and Hao,J.
  TITLE     BZW1 Facilitates Glycolysis and Promotes Tumor Growth in Pancreatic
            Ductal Adenocarcinoma Through Potentiating eIF2alpha
            Phosphorylation
  JOURNAL   Gastroenterology 162 (4), 1256-1271 (2022)
   PUBMED   34951995
  REMARK    GeneRIF: BZW1 Facilitates Glycolysis and Promotes Tumor Growth in
            Pancreatic Ductal Adenocarcinoma Through Potentiating eIF2alpha
            Phosphorylation.
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Singh,C.R., Glineburg,M.R., Moore,C., Tani,N., Jaiswal,R., Zou,Y.,
            Aube,E., Gillaspie,S., Thornton,M., Cecil,A., Hilgers,M.,
            Takasu,A., Asano,I., Asano,M., Escalante,C.R., Nakamura,A.,
            Todd,P.K. and Asano,K.
  TITLE     Human oncoprotein 5MP suppresses general and repeat-associated
            non-AUG translation via eIF3 by a common mechanism
  JOURNAL   Cell Rep 36 (2), 109376 (2021)
   PUBMED   34260931
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Li,S., Chai,Z., Li,Y., Liu,D., Bai,Z., Li,Y., Li,Y. and Situ,Z.
  TITLE     BZW1, a novel proliferation regulator that promotes growth of
            salivary muocepodermoid carcinoma
  JOURNAL   Cancer Lett 284 (1), 86-94 (2009)
   PUBMED   19446954
  REMARK    GeneRIF: BZW1 is a novel factor, promoting the growth of MEC cells
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Mitra,P., Vaughan,P.S., Stein,J.L., Stein,G.S. and van Wijnen,A.J.
  TITLE     Purification and functional analysis of a novel
            leucine-zipper/nucleotide-fold protein, BZAP45, stimulating cell
            cycle regulated histone H4 gene transcription
  JOURNAL   Biochemistry 40 (35), 10693-10699 (2001)
   PUBMED   11524015
  REMARK    GeneRIF: Stimulates cell cycle regulation of histone H4 gene
            transcription.
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL833518.1, AB074176.1, AC007163.3 and AC005037.2.
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.180610.1,
                                           SRR1660803.196126.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409600.6/ ENSP00000386474.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..419
                     /product="eIF5-mimic protein 2 isoform 1"
                     /note="basic leucine-zipper protein BZAP45; basic leucine
                     zipper and W2 domain-containing protein 1; putative
                     protein product of Nbla10236; eIF5-mimic protein 2"
                     /calculated_mol_wt=47912
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L1Q6.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7L1Q6.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L1Q6.1)"
     Region          217..406
                     /region_name="W2_eIF5C_like"
                     /note="C-terminal W2 domain of the eukaryotic translation
                     initiation factor 5C and similar proteins; cd11560"
                     /db_xref="CDD:211398"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q7L1Q6.1)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008; propagated from
                     UniProtKB/Swiss-Prot (Q7L1Q6.1)"
     CDS             1..419
                     /gene="BZW1"
                     /gene_synonym="5MP2; BZAP45; Nbla10236"
                     /coded_by="NM_001207067.2:92..1351"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS56156.1"
                     /db_xref="GeneID:9689"
                     /db_xref="HGNC:HGNC:18380"
                     /db_xref="MIM:619252"
ORIGIN      
        1 mnnqkqqkpt lsgqrfktrk rdekerfdpt qfqdciiqgl tetgtdleav akfldasgak
       61 ldyrryaetl fdilvaggml apggtladdm mrtdvcvfaa qedletmqaf aqvfnklirr
      121 ykylekgfed evkklllflk gfsesernkl amltgvllan gtlnasilns lynenlvkeg
      181 vsaafavklf kswinekdin avaaslrkvs mdnrlmelfp ankqsvehft kyfteaglke
      241 lseyvrnqqt igarkelqke lqeqmsrgdp fkdiilyvke emkknnipep vvigivwssv
      301 mstvewnkke elvaeqaikh lkqyspllaa fttqgqselt lllkiqeycy dnihfmkafq
      361 kivvlfykae vlseepilkw ykdahvakgk svfleqmkkf vewlknaeee seseaeegd
//
LOCUS       NP_004680                715 aa            linear   PRI 27-APR-2025
DEFINITION  metastasis-associated protein MTA1 isoform MTA1 [Homo sapiens].
ACCESSION   NP_004680
VERSION     NP_004680.2
DBSOURCE    REFSEQ: accession NM_004689.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Wanka,G., Jueckstock,J., Wild,C.M., Vattai,A., Furst,S.,
            Heidegger,H.H., Kuhn,C., Schmoeckel,E., Jeschke,U. and Dannecker,C.
  TITLE     MTA1 as negative prognostic marker in vulvar carcinoma
  JOURNAL   J Cancer Res Clin Oncol 149 (9), 6191-6201 (2023)
   PUBMED   36689059
  REMARK    GeneRIF: MTA1 as negative prognostic marker in vulvar carcinoma.
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Sun,F.Z., Wang,J.S., Li,C.X., Wang,T., Zhang,J.Y., Zhou,Y.T.,
            Wang,H.J. and Qian,H.L.
  TITLE     [The role and mechanism of tumor metastasis-associated gene 1 in
            radiosensitivity of HeLa cells]
  JOURNAL   Zhonghua Zhong Liu Za Zhi 44 (9), 962-967 (2022)
   PUBMED   36164698
  REMARK    GeneRIF: [The role and mechanism of tumor metastasis-associated
            gene 1 in radiosensitivity of HeLa cells].
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Vattem,C. and Pakala,S.B.
  TITLE     Metastasis-associated protein 1: A potential driver and regulator
            of the hallmarks of cancer
  JOURNAL   J Biosci 47 (2022)
   PUBMED   36210748
  REMARK    GeneRIF: Metastasis-associated protein 1: A potential driver and
            regulator of the hallmarks of cancer.
            Review article
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Kumar,R., Balasenthil,S., Pakala,S.B., Rayala,S.K., Sahin,A.A. and
            Ohshiro,K.
  TITLE     Metastasis-associated protein 1 short form stimulates Wnt1 pathway
            in mammary epithelial and cancer cells
  JOURNAL   Cancer Res 70 (16), 6598-6608 (2010)
   PUBMED   20710043
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Kumar,R., Balasenthil,S., Manavathi,B., Rayala,S.K. and Pakala,S.B.
  TITLE     Metastasis-associated protein 1 and its short form variant
            stimulates Wnt1 transcription through promoting its derepression
            from Six3 corepressor
  JOURNAL   Cancer Res 70 (16), 6649-6658 (2010)
   PUBMED   20682799
REFERENCE   6  (residues 1 to 715)
  AUTHORS   Singh,R.R., Kaluarachchi,K., Chen,M., Rayala,S.K., Balasenthil,S.,
            Ma,J. and Kumar,R.
  TITLE     Solution structure and antiestrogenic activity of the unique
            C-terminal, NR-box motif-containing region of MTA1s
  JOURNAL   J Biol Chem 281 (35), 25612-25621 (2006)
   PUBMED   16807247
  REMARK    GeneRIF: structure and antiestrogenic activity of the unique
            C-terminal, NR-box motif-containing region of MTA1
            Erratum:[J Biol Chem. 2013 Sep 20;288(38):27518]
REFERENCE   7  (residues 1 to 715)
  AUTHORS   Mishra,S.K., Yang,Z., Mazumdar,A., Talukder,A.H., Larose,L. and
            Kumar,R.
  TITLE     Metastatic tumor antigen 1 short form (MTA1s) associates with
            casein kinase I-gamma2, an estrogen-responsive kinase
  JOURNAL   Oncogene 23 (25), 4422-4429 (2004)
   PUBMED   15077195
  REMARK    GeneRIF: MTA1s interacts with CKI-gamma2 in vitro and in vivo and
            colocalizes in the cytoplasm
REFERENCE   8  (residues 1 to 715)
  AUTHORS   Kumar,R., Wang,R.A., Mazumdar,A., Talukder,A.H., Mandal,M.,
            Yang,Z., Bagheri-Yarmand,R., Sahin,A., Hortobagyi,G., Adam,L.,
            Barnes,C.J. and Vadlamudi,R.K.
  TITLE     A naturally occurring MTA1 variant sequesters oestrogen
            receptor-alpha in the cytoplasm
  JOURNAL   Nature 418 (6898), 654-657 (2002)
   PUBMED   12167865
  REMARK    GeneRIF: naturally occurring short form that contains a previously
            unknown sequence of 33 amino acids with an ER-binding motif,
            Leu-Arg-Ile-Leu-Leu (LRILL); MTA1s localizes in the cytoplasm,
            sequesters ER in the cytoplasm, and enhances non-genomic responses
            of ER
REFERENCE   9  (residues 1 to 715)
  AUTHORS   Toh,Y., Pencil,S.D. and Nicolson,G.L.
  TITLE     Analysis of the complete sequence of the novel
            metastasis-associated candidate gene, mta1, differentially
            expressed in mammary adenocarcinoma and breast cancer cell lines
  JOURNAL   Gene 159 (1), 97-104 (1995)
   PUBMED   7607577
REFERENCE   10 (residues 1 to 715)
  AUTHORS   Toh,Y., Pencil,S.D. and Nicolson,G.L.
  TITLE     A novel candidate metastasis-associated gene, mta1, differentially
            expressed in highly metastatic mammary adenocarcinoma cell lines.
            cDNA cloning, expression, and protein analyses
  JOURNAL   J Biol Chem 269 (37), 22958-22963 (1994)
   PUBMED   8083195
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL928654.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 4, 2006 this sequence version replaced NP_004680.1.
            
            Summary: This gene encodes a protein that was identified in a
            screen for genes expressed in metastatic cells, specifically,
            mammary adenocarcinoma cell lines. Expression of this gene has been
            correlated with the metastatic potential of at least two types of
            carcinomas although it is also expressed in many normal tissues.
            The role it plays in metastasis is unclear. It was initially
            thought to be the 70kD component of a nucleosome remodeling
            deacetylase complex, NuRD, but it is more likely that this
            component is a different but very similar protein. These two
            proteins are so closely related, though, that they share the same
            types of domains. These domains include two DNA binding domains, a
            dimerization domain, and a domain commonly found in proteins that
            methylate DNA. The profile and activity of this gene product
            suggest that it is involved in regulating transcription and that
            this may be accomplished by chromatin remodeling. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Feb 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (MTA1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC142941.1, U35113.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331320.12/ ENSP00000333633.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..715
                     /product="metastasis-associated protein MTA1 isoform MTA1"
                     /note="metastasis associated gene 1 protein"
                     /calculated_mol_wt=80655
     Region          3..188
                     /region_name="BAH_MTA"
                     /note="BAH, or Bromo Adjacent Homology domain, as present
                     in MTA1 and similar proteins. The Metastasis-associated
                     protein MTA1 is part of the NURD (nucleosome remodeling
                     and deacetylating) complex and plays a role in cellular
                     transformation and metastasis. BAH...; cd04709"
                     /db_xref="CDD:240060"
     Region          167..219
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          287..332
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(288,318..319,321..322,324..326,328..330)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Region          388..441
                     /region_name="ZnF_GATA"
                     /note="zinc finger binding to DNA consensus sequence
                     [AT]GATA[AG]; smart00401"
                     /db_xref="CDD:214648"
     Region          435..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13330.2)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13330.2)"
     Region          464..541
                     /region_name="MTA_R1"
                     /note="MTA R1 domain; pfam17226"
                     /db_xref="CDD:465388"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Region          545..552
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13330.2)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Site            626
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16617102,
                     ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:19805145;
                     propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13330.2)"
     Region          656..686
                     /region_name="Interaction with RBBP4.
                     /evidence=ECO:0000269|PubMed:24920672"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Region          673..715
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Region          696..705
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Region          711..715
                     /region_name="SUMO interaction motif 1 (SIM), crucial for
                     efficient sumoylation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     CDS             1..715
                     /gene="MTA1"
                     /coded_by="NM_004689.4:210..2357"
                     /note="isoform MTA1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32169.1"
                     /db_xref="GeneID:9112"
                     /db_xref="HGNC:HGNC:7410"
                     /db_xref="MIM:603526"
ORIGIN      
        1 maanmyrvgd yvyfensssn pylirrieel nktangnvea kvvcfyrrrd isstlialad
       61 khatlsvcyk agpgadngee geieeemenp emvdlpeklk hqlrhrelfl srqleslpat
      121 hirgkcsvtl lneteslksy leredfffys lvydpqqktl ladkgeirvg nryqaditdl
      181 lkegeedgrd qsrletqvwe ahnpltdkqi dqflvvarsv gtfaraldcs ssvrqpslhm
      241 saaaasrdit lfhamdtlhk niydiskais alvpqggpvl crdemeewsa seanlfeeal
      301 ekygkdftdi qqdflpwksl tsiieyyymw kttdryvqqk rlkaaeaesk lkqvyipnyn
      361 kpnpnqisvn nvkagvvngt gapgqspgag racescyttq syqwyswgpp nmqcrlcasc
      421 wtywkkyggl kmptrldger pgpnrsnmsp hglparssgs pkfamktrqa fylhttkltr
      481 iarrlcreil rpwhaarhpy lpinsaaika ectarlpeas qsplvlkqav rkpleavlry
      541 lethprppkp dpvksvssvl ssltpakvap vinngsptil gkrsyeqhng vdgnmkkrll
      601 mpsrglanhg qarhmgpsrn lllngksypt kvrlirggsl ppvkrrrmnw idapddvfym
      661 ateetrkirk llsssetkra arrpykpial rqsqalpprp pppapvndep ivied
//
LOCUS       NP_001354218             558 aa            linear   PRI 27-APR-2025
DEFINITION  innate immunity activator protein isoform 3 [Homo sapiens].
ACCESSION   NP_001354218
VERSION     NP_001354218.1
DBSOURCE    REFSEQ: accession NM_001367289.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Chang,D., Luong,P., Li,Q., LeBarron,J., Anderson,M., Barrett,L. and
            Lencer,W.I.
  TITLE     Small-molecule modulators of INAVA cytosolic condensate and
            cell-cell junction assemblies
  JOURNAL   J Cell Biol 220 (9) (2021)
   PUBMED   34251416
  REMARK    GeneRIF: Small-molecule modulators of INAVA cytosolic condensate
            and cell-cell junction assemblies.
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Luong,P., Hedl,M., Yan,J., Zuo,T., Fu,T.M., Jiang,X.,
            Thiagarajah,J.R., Hansen,S.H., Lesser,C.F., Wu,H., Abraham,C. and
            Lencer,W.I.
  TITLE     INAVA-ARNO complexes bridge mucosal barrier function with
            inflammatory signaling
  JOURNAL   Elife 7, e38539 (2018)
   PUBMED   30355448
  REMARK    GeneRIF: INAVA-CUPID exhibits dual functions, coordinated directly
            by ARNO, that bridge epithelial barrier function with extracellular
            signals and inflammation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 558)
  AUTHORS   Manzanillo,P., Mouchess,M., Ota,N., Dai,B., Ichikawa,R., Wuster,A.,
            Haley,B., Alvarado,G., Kwon,Y., Caothien,R., Roose-Girma,M.,
            Warming,S., McKenzie,B.S., Keir,M.E., Scherl,A., Ouyang,W. and
            Yi,T.
  TITLE     Inflammatory Bowel Disease Susceptibility Gene C1ORF106 Regulates
            Intestinal Epithelial Permeability
  JOURNAL   Immunohorizons 2 (5), 164-171 (2018)
   PUBMED   31022698
  REMARK    GeneRIF: Study identifies C1ORF106 as an epithelial cell junction
            protein, and the loss of C1ORF106 augments TNF-alpha-induced
            intestinal epithelial leakage and diarrhea that may play a critical
            role in the development of inflammatory bowel disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 558)
  AUTHORS   Jostins,L., Ripke,S., Weersma,R.K., Duerr,R.H., McGovern,D.P.,
            Hui,K.Y., Lee,J.C., Schumm,L.P., Sharma,Y., Anderson,C.A.,
            Essers,J., Mitrovic,M., Ning,K., Cleynen,I., Theatre,E.,
            Spain,S.L., Raychaudhuri,S., Goyette,P., Wei,Z., Abraham,C.,
            Achkar,J.P., Ahmad,T., Amininejad,L., Ananthakrishnan,A.N.,
            Andersen,V., Andrews,J.M., Baidoo,L., Balschun,T., Bampton,P.A.,
            Bitton,A., Boucher,G., Brand,S., Buning,C., Cohain,A., Cichon,S.,
            D'Amato,M., De Jong,D., Devaney,K.L., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Ferguson,L.R., Franchimont,D., Fransen,K.,
            Gearry,R., Georges,M., Gieger,C., Glas,J., Haritunians,T., Hart,A.,
            Hawkey,C., Hedl,M., Hu,X., Karlsen,T.H., Kupcinskas,L.,
            Kugathasan,S., Latiano,A., Laukens,D., Lawrance,I.C., Lees,C.W.,
            Louis,E., Mahy,G., Mansfield,J., Morgan,A.R., Mowat,C., Newman,W.,
            Palmieri,O., Ponsioen,C.Y., Potocnik,U., Prescott,N.J.,
            Regueiro,M., Rotter,J.I., Russell,R.K., Sanderson,J.D., Sans,M.,
            Satsangi,J., Schreiber,S., Simms,L.A., Sventoraityte,J.,
            Targan,S.R., Taylor,K.D., Tremelling,M., Verspaget,H.W., De Vos,M.,
            Wijmenga,C., Wilson,D.C., Winkelmann,J., Xavier,R.J., Zeissig,S.,
            Zhang,B., Zhang,C.K., Zhao,H., Silverberg,M.S., Annese,V.,
            Hakonarson,H., Brant,S.R., Radford-Smith,G., Mathew,C.G.,
            Rioux,J.D., Schadt,E.E., Daly,M.J., Franke,A., Parkes,M.,
            Vermeire,S., Barrett,J.C. and Cho,J.H.
  CONSRTM   International IBD Genetics Consortium (IIBDGC)
  TITLE     Host-microbe interactions have shaped the genetic architecture of
            inflammatory bowel disease
  JOURNAL   Nature 491 (7422), 119-124 (2012)
   PUBMED   23128233
REFERENCE   7  (residues 1 to 558)
  AUTHORS   Sawcer,S., Hellenthal,G., Pirinen,M., Spencer,C.C.,
            Patsopoulos,N.A., Moutsianas,L., Dilthey,A., Su,Z., Freeman,C.,
            Hunt,S.E., Edkins,S., Gray,E., Booth,D.R., Potter,S.C., Goris,A.,
            Band,G., Oturai,A.B., Strange,A., Saarela,J., Bellenguez,C.,
            Fontaine,B., Gillman,M., Hemmer,B., Gwilliam,R., Zipp,F.,
            Jayakumar,A., Martin,R., Leslie,S., Hawkins,S., Giannoulatou,E.,
            D'alfonso,S., Blackburn,H., Martinelli Boneschi,F., Liddle,J.,
            Harbo,H.F., Perez,M.L., Spurkland,A., Waller,M.J., Mycko,M.P.,
            Ricketts,M., Comabella,M., Hammond,N., Kockum,I., McCann,O.T.,
            Ban,M., Whittaker,P., Kemppinen,A., Weston,P., Hawkins,C.,
            Widaa,S., Zajicek,J., Dronov,S., Robertson,N., Bumpstead,S.J.,
            Barcellos,L.F., Ravindrarajah,R., Abraham,R., Alfredsson,L.,
            Ardlie,K., Aubin,C., Baker,A., Baker,K., Baranzini,S.E.,
            Bergamaschi,L., Bergamaschi,R., Bernstein,A., Berthele,A.,
            Boggild,M., Bradfield,J.P., Brassat,D., Broadley,S.A., Buck,D.,
            Butzkueven,H., Capra,R., Carroll,W.M., Cavalla,P., Celius,E.G.,
            Cepok,S., Chiavacci,R., Clerget-Darpoux,F., Clysters,K., Comi,G.,
            Cossburn,M., Cournu-Rebeix,I., Cox,M.B., Cozen,W., Cree,B.A.,
            Cross,A.H., Cusi,D., Daly,M.J., Davis,E., de Bakker,P.I.,
            Debouverie,M., D'hooghe,M.B., Dixon,K., Dobosi,R., Dubois,B.,
            Ellinghaus,D., Elovaara,I., Esposito,F., Fontenille,C., Foote,S.,
            Franke,A., Galimberti,D., Ghezzi,A., Glessner,J., Gomez,R.,
            Gout,O., Graham,C., Grant,S.F., Guerini,F.R., Hakonarson,H.,
            Hall,P., Hamsten,A., Hartung,H.P., Heard,R.N., Heath,S., Hobart,J.,
            Hoshi,M., Infante-Duarte,C., Ingram,G., Ingram,W., Islam,T.,
            Jagodic,M., Kabesch,M., Kermode,A.G., Kilpatrick,T.J., Kim,C.,
            Klopp,N., Koivisto,K., Larsson,M., Lathrop,M., Lechner-Scott,J.S.,
            Leone,M.A., Leppa,V., Liljedahl,U., Bomfim,I.L., Lincoln,R.R.,
            Link,J., Liu,J., Lorentzen,A.R., Lupoli,S., Macciardi,F., Mack,T.,
            Marriott,M., Martinelli,V., Mason,D., McCauley,J.L., Mentch,F.,
            Mero,I.L., Mihalova,T., Montalban,X., Mottershead,J., Myhr,K.M.,
            Naldi,P., Ollier,W., Page,A., Palotie,A., Pelletier,J., Piccio,L.,
            Pickersgill,T., Piehl,F., Pobywajlo,S., Quach,H.L., Ramsay,P.P.,
            Reunanen,M., Reynolds,R., Rioux,J.D., Rodegher,M., Roesner,S.,
            Rubio,J.P., Ruckert,I.M., Salvetti,M., Salvi,E., Santaniello,A.,
            Schaefer,C.A., Schreiber,S., Schulze,C., Scott,R.J., Sellebjerg,F.,
            Selmaj,K.W., Sexton,D., Shen,L., Simms-Acuna,B., Skidmore,S.,
            Sleiman,P.M., Smestad,C., Sorensen,P.S., Sondergaard,H.B.,
            Stankovich,J., Strange,R.C., Sulonen,A.M., Sundqvist,E.,
            Syvanen,A.C., Taddeo,F., Taylor,B., Blackwell,J.M., Tienari,P.,
            Bramon,E., Tourbah,A., Brown,M.A., Tronczynska,E., Casas,J.P.,
            Tubridy,N., Corvin,A., Vickery,J., Jankowski,J., Villoslada,P.,
            Markus,H.S., Wang,K., Mathew,C.G., Wason,J., Palmer,C.N.,
            Wichmann,H.E., Plomin,R., Willoughby,E., Rautanen,A.,
            Winkelmann,J., Wittig,M., Trembath,R.C., Yaouanq,J.,
            Viswanathan,A.C., Zhang,H., Wood,N.W., Zuvich,R., Deloukas,P.,
            Langford,C., Duncanson,A., Oksenberg,J.R., Pericak-Vance,M.A.,
            Haines,J.L., Olsson,T., Hillert,J., Ivinson,A.J., De Jager,P.L.,
            Peltonen,L., Stewart,G.J., Hafler,D.A., Hauser,S.L., McVean,G.,
            Donnelly,P. and Compston,A.
  CONSRTM   International Multiple Sclerosis Genetics Consortium; Wellcome
            Trust Case Control Consortium 2
  TITLE     Genetic risk and a primary role for cell-mediated immune mechanisms
            in multiple sclerosis
  JOURNAL   Nature 476 (7359), 214-219 (2011)
   PUBMED   21833088
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 558)
  AUTHORS   Anderson,C.A., Boucher,G., Lees,C.W., Franke,A., D'Amato,M.,
            Taylor,K.D., Lee,J.C., Goyette,P., Imielinski,M., Latiano,A.,
            Lagace,C., Scott,R., Amininejad,L., Bumpstead,S., Baidoo,L.,
            Baldassano,R.N., Barclay,M., Bayless,T.M., Brand,S., Buning,C.,
            Colombel,J.F., Denson,L.A., De Vos,M., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Fehrmann,R.S., Floyd,J.A., Florin,T.,
            Franchimont,D., Franke,L., Georges,M., Glas,J., Glazer,N.L.,
            Guthery,S.L., Haritunians,T., Hayward,N.K., Hugot,J.P., Jobin,G.,
            Laukens,D., Lawrance,I., Lemann,M., Levine,A., Libioulle,C.,
            Louis,E., McGovern,D.P., Milla,M., Montgomery,G.W., Morley,K.I.,
            Mowat,C., Ng,A., Newman,W., Ophoff,R.A., Papi,L., Palmieri,O.,
            Peyrin-Biroulet,L., Panes,J., Phillips,A., Prescott,N.J.,
            Proctor,D.D., Roberts,R., Russell,R., Rutgeerts,P., Sanderson,J.,
            Sans,M., Schumm,P., Seibold,F., Sharma,Y., Simms,L.A.,
            Seielstad,M., Steinhart,A.H., Targan,S.R., van den Berg,L.H.,
            Vatn,M., Verspaget,H., Walters,T., Wijmenga,C., Wilson,D.C.,
            Westra,H.J., Xavier,R.J., Zhao,Z.Z., Ponsioen,C.Y., Andersen,V.,
            Torkvist,L., Gazouli,M., Anagnou,N.P., Karlsen,T.H., Kupcinskas,L.,
            Sventoraityte,J., Mansfield,J.C., Kugathasan,S., Silverberg,M.S.,
            Halfvarson,J., Rotter,J.I., Mathew,C.G., Griffiths,A.M., Gearry,R.,
            Ahmad,T., Brant,S.R., Chamaillard,M., Satsangi,J., Cho,J.H.,
            Schreiber,S., Daly,M.J., Barrett,J.C., Parkes,M., Annese,V.,
            Hakonarson,H., Radford-Smith,G., Duerr,R.H., Vermeire,S.,
            Weersma,R.K. and Rioux,J.D.
  TITLE     Meta-analysis identifies 29 additional ulcerative colitis risk
            loci, increasing the number of confirmed associations to 47
  JOURNAL   Nat Genet 43 (3), 246-252 (2011)
   PUBMED   21297633
  REMARK    Erratum:[Nat Genet. 2011 Sep;43(9):919]
REFERENCE   9  (residues 1 to 558)
  AUTHORS   Franke,A., McGovern,D.P., Barrett,J.C., Wang,K.,
            Radford-Smith,G.L., Ahmad,T., Lees,C.W., Balschun,T., Lee,J.,
            Roberts,R., Anderson,C.A., Bis,J.C., Bumpstead,S., Ellinghaus,D.,
            Festen,E.M., Georges,M., Green,T., Haritunians,T., Jostins,L.,
            Latiano,A., Mathew,C.G., Montgomery,G.W., Prescott,N.J.,
            Raychaudhuri,S., Rotter,J.I., Schumm,P., Sharma,Y., Simms,L.A.,
            Taylor,K.D., Whiteman,D., Wijmenga,C., Baldassano,R.N., Barclay,M.,
            Bayless,T.M., Brand,S., Buning,C., Cohen,A., Colombel,J.F.,
            Cottone,M., Stronati,L., Denson,T., De Vos,M., D'Inca,R.,
            Dubinsky,M., Edwards,C., Florin,T., Franchimont,D., Gearry,R.,
            Glas,J., Van Gossum,A., Guthery,S.L., Halfvarson,J.,
            Verspaget,H.W., Hugot,J.P., Karban,A., Laukens,D., Lawrance,I.,
            Lemann,M., Levine,A., Libioulle,C., Louis,E., Mowat,C., Newman,W.,
            Panes,J., Phillips,A., Proctor,D.D., Regueiro,M., Russell,R.,
            Rutgeerts,P., Sanderson,J., Sans,M., Seibold,F., Steinhart,A.H.,
            Stokkers,P.C., Torkvist,L., Kullak-Ublick,G., Wilson,D.,
            Walters,T., Targan,S.R., Brant,S.R., Rioux,J.D., D'Amato,M.,
            Weersma,R.K., Kugathasan,S., Griffiths,A.M., Mansfield,J.C.,
            Vermeire,S., Duerr,R.H., Silverberg,M.S., Satsangi,J.,
            Schreiber,S., Cho,J.H., Annese,V., Hakonarson,H., Daly,M.J. and
            Parkes,M.
  TITLE     Genome-wide meta-analysis increases to 71 the number of confirmed
            Crohn's disease susceptibility loci
  JOURNAL   Nat Genet 42 (12), 1118-1125 (2010)
   PUBMED   21102463
REFERENCE   10 (residues 1 to 558)
  AUTHORS   Barrett,J.C., Lee,J.C., Lees,C.W., Prescott,N.J., Anderson,C.A.,
            Phillips,A., Wesley,E., Parnell,K., Zhang,H., Drummond,H.,
            Nimmo,E.R., Massey,D., Blaszczyk,K., Elliott,T., Cotterill,L.,
            Dallal,H., Lobo,A.J., Mowat,C., Sanderson,J.D., Jewell,D.P.,
            Newman,W.G., Edwards,C., Ahmad,T., Mansfield,J.C., Satsangi,J.,
            Parkes,M., Mathew,C.G., Donnelly,P., Peltonen,L., Blackwell,J.M.,
            Bramon,E., Brown,M.A., Casas,J.P., Corvin,A., Craddock,N.,
            Deloukas,P., Duncanson,A., Jankowski,J., Markus,H.S., Mathew,C.G.,
            McCarthy,M.I., Palmer,C.N., Plomin,R., Rautanen,A., Sawcer,S.J.,
            Samani,N., Trembath,R.C., Viswanathan,A.C., Wood,N., Spencer,C.C.,
            Barrett,J.C., Bellenguez,C., Davison,D., Freeman,C., Strange,A.,
            Donnelly,P., Langford,C., Hunt,S.E., Edkins,S., Gwilliam,R.,
            Blackburn,H., Bumpstead,S.J., Dronov,S., Gillman,M., Gray,E.,
            Hammond,N., Jayakumar,A., McCann,O.T., Liddle,J., Perez,M.L.,
            Potter,S.C., Ravindrarajah,R., Ricketts,M., Waller,M., Weston,P.,
            Widaa,S., Whittaker,P., Deloukas,P., Peltonen,L., Mathew,C.G.,
            Blackwell,J.M., Brown,M.A., Corvin,A., McCarthy,M.I., Spencer,C.C.,
            Attwood,A.P., Stephens,J., Sambrook,J., Ouwehand,W.H.,
            McArdle,W.L., Ring,S.M. and Strachan,D.P.
  CONSRTM   UK IBD Genetics Consortium; Wellcome Trust Case Control Consortium
            2
  TITLE     Genome-wide association study of ulcerative colitis identifies
            three new susceptibility loci, including the HNF4A region
  JOURNAL   Nat Genet 41 (12), 1330-1334 (2009)
   PUBMED   19915572
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099756.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1976338.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..558
                     /product="innate immunity activator protein isoform 3"
                     /note="uncharacterized protein C1orf106; innate immunity
                     activator protein"
                     /calculated_mol_wt=61444
     Region          2..131
                     /region_name="CUPID"
                     /note="Cytohesin Ubiquitin Protein Inducing Domain;
                     pfam11819"
                     /db_xref="CDD:463360"
     CDS             1..558
                     /gene="INAVA"
                     /gene_synonym="C1orf106"
                     /coded_by="NM_001367289.1:283..1959"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:55765"
                     /db_xref="HGNC:HGNC:25599"
                     /db_xref="MIM:618051"
ORIGIN      
        1 meskdevsdt dsgiilqsgp dspvspmkel thavhkqqra learleacle elrrlclrea
       61 eltgtlpaey plkpgekapk vrrrigaayk lddwalhred plsslerqla lqlqiteaar
      121 rlcleenlsr qarrqrkhsm lqeekklqel qrclverrrn sepppaaalp lgrelsasdd
      181 sslsdgllle eeesqvpkpp pespappsrp lppqtleglq ptgpeagspe rapvqnspwk
      241 etsldhpyek prkssepwse ssspattpqd gpsasslwll epasyhvvpi rgvpgqwqgr
      301 tsapatpeiq grrgqsqslr vdsfragpeg rgrsafprrr pthytvtvpd scfpatkppl
      361 phaachscse dsgsdvssis hptspgsssp disflqplsp pkthrhrgaw vpagsrelva
      421 hhpklllppg yfpagryvvv aesplppgew elrraapgpa yeeegtplry qrlvpsrsri
      481 vrtpslkdsp agrglskaav seelkwwher arlrstrphs ldrqgafrvp tvcvlrrspd
      541 gapvqvfvpe kgeiisqv
//
LOCUS       NP_055916                626 aa            linear   PRI 27-APR-2025
DEFINITION  procollagen galactosyltransferase 2 isoform 1precursor [Homo
            sapiens].
ACCESSION   NP_055916
VERSION     NP_055916.1
DBSOURCE    REFSEQ: accession NM_015101.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Kehayova,Y.S., Wilkinson,J.M., Rice,S.J. and Loughlin,J.
  TITLE     Mediation of the Same Epigenetic and Transcriptional Effect by
            Independent Osteoarthritis Risk-Conferring Alleles on a Shared
            Target Gene, COLGALT2
  JOURNAL   Arthritis Rheumatol 75 (6), 910-922 (2023)
   PUBMED   36538011
  REMARK    GeneRIF: Mediation of the Same Epigenetic and Transcriptional
            Effect by Independent Osteoarthritis Risk-Conferring Alleles on a
            Shared Target Gene, COLGALT2.
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Kehayova,Y.S., Wilkinson,J.M., Rice,S.J. and Loughlin,J.
  TITLE     Osteoarthritis genetic risk acting on the galactosyltransferase
            gene COLGALT2 has opposing functional effects in articulating joint
            tissues
  JOURNAL   Arthritis Res Ther 25 (1), 83 (2023)
   PUBMED   37208701
  REMARK    GeneRIF: Osteoarthritis genetic risk acting on the
            galactosyltransferase gene COLGALT2 has opposing functional effects
            in articulating joint tissues.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Kehayova,Y.S., Watson,E., Wilkinson,J.M., Loughlin,J. and Rice,S.J.
  TITLE     Genetic and Epigenetic Interplay Within a COLGALT2 Enhancer
            Associated With Osteoarthritis
  JOURNAL   Arthritis Rheumatol 73 (10), 1856-1865 (2021)
   PUBMED   33760386
  REMARK    GeneRIF: Genetic and Epigenetic Interplay Within a COLGALT2
            Enhancer Associated With Osteoarthritis.
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Guo,T., Li,B., Kang,Y., Gu,C., Fang,F., Chen,X., Liu,X., Lu,G.,
            Feng,C. and Xu,C.
  TITLE     COLGALT2 is overexpressed in ovarian cancer and interacts with
            PLOD3
  JOURNAL   Clin Transl Med 11 (3), e370 (2021)
   PUBMED   33783989
  REMARK    GeneRIF: COLGALT2 is overexpressed in ovarian cancer and interacts
            with PLOD3.
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Berndt,S.I., Gustafsson,S., Magi,R., Ganna,A., Wheeler,E.,
            Feitosa,M.F., Justice,A.E., Monda,K.L., Croteau-Chonka,D.C.,
            Day,F.R., Esko,T., Fall,T., Ferreira,T., Gentilini,D.,
            Jackson,A.U., Luan,J., Randall,J.C., Vedantam,S., Willer,C.J.,
            Winkler,T.W., Wood,A.R., Workalemahu,T., Hu,Y.J., Lee,S.H.,
            Liang,L., Lin,D.Y., Min,J.L., Neale,B.M., Thorleifsson,G., Yang,J.,
            Albrecht,E., Amin,N., Bragg-Gresham,J.L., Cadby,G., den Heijer,M.,
            Eklund,N., Fischer,K., Goel,A., Hottenga,J.J., Huffman,J.E.,
            Jarick,I., Johansson,A., Johnson,T., Kanoni,S., Kleber,M.E.,
            Konig,I.R., Kristiansson,K., Kutalik,Z., Lamina,C., Lecoeur,C.,
            Li,G., Mangino,M., McArdle,W.L., Medina-Gomez,C.,
            Muller-Nurasyid,M., Ngwa,J.S., Nolte,I.M., Paternoster,L.,
            Pechlivanis,S., Perola,M., Peters,M.J., Preuss,M., Rose,L.M.,
            Shi,J., Shungin,D., Smith,A.V., Strawbridge,R.J., Surakka,I.,
            Teumer,A., Trip,M.D., Tyrer,J., Van Vliet-Ostaptchouk,J.V.,
            Vandenput,L., Waite,L.L., Zhao,J.H., Absher,D., Asselbergs,F.W.,
            Atalay,M., Attwood,A.P., Balmforth,A.J., Basart,H., Beilby,J.,
            Bonnycastle,L.L., Brambilla,P., Bruinenberg,M., Campbell,H.,
            Chasman,D.I., Chines,P.S., Collins,F.S., Connell,J.M.,
            Cookson,W.O., de Faire,U., de Vegt,F., Dei,M., Dimitriou,M.,
            Edkins,S., Estrada,K., Evans,D.M., Farrall,M., Ferrario,M.M.,
            Ferrieres,J., Franke,L., Frau,F., Gejman,P.V., Grallert,H.,
            Gronberg,H., Gudnason,V., Hall,A.S., Hall,P., Hartikainen,A.L.,
            Hayward,C., Heard-Costa,N.L., Heath,A.C., Hebebrand,J., Homuth,G.,
            Hu,F.B., Hunt,S.E., Hypponen,E., Iribarren,C., Jacobs,K.B.,
            Jansson,J.O., Jula,A., Kahonen,M., Kathiresan,S., Kee,F.,
            Khaw,K.T., Kivimaki,M., Koenig,W., Kraja,A.T., Kumari,M.,
            Kuulasmaa,K., Kuusisto,J., Laitinen,J.H., Lakka,T.A.,
            Langenberg,C., Launer,L.J., Lind,L., Lindstrom,J., Liu,J.,
            Liuzzi,A., Lokki,M.L., Lorentzon,M., Madden,P.A., Magnusson,P.K.,
            Manunta,P., Marek,D., Marz,W., Mateo Leach,I., McKnight,B.,
            Medland,S.E., Mihailov,E., Milani,L., Montgomery,G.W., Mooser,V.,
            Muhleisen,T.W., Munroe,P.B., Musk,A.W., Narisu,N., Navis,G.,
            Nicholson,G., Nohr,E.A., Ong,K.K., Oostra,B.A., Palmer,C.N.,
            Palotie,A., Peden,J.F., Pedersen,N., Peters,A., Polasek,O.,
            Pouta,A., Pramstaller,P.P., Prokopenko,I., Putter,C.,
            Radhakrishnan,A., Raitakari,O., Rendon,A., Rivadeneira,F.,
            Rudan,I., Saaristo,T.E., Sambrook,J.G., Sanders,A.R., Sanna,S.,
            Saramies,J., Schipf,S., Schreiber,S., Schunkert,H., Shin,S.Y.,
            Signorini,S., Sinisalo,J., Skrobek,B., Soranzo,N., Stancakova,A.,
            Stark,K., Stephens,J.C., Stirrups,K., Stolk,R.P., Stumvoll,M.,
            Swift,A.J., Theodoraki,E.V., Thorand,B., Tregouet,D.A., Tremoli,E.,
            Van der Klauw,M.M., van Meurs,J.B., Vermeulen,S.H., Viikari,J.,
            Virtamo,J., Vitart,V., Waeber,G., Wang,Z., Widen,E., Wild,S.H.,
            Willemsen,G., Winkelmann,B.R., Witteman,J.C., Wolffenbuttel,B.H.,
            Wong,A., Wright,A.F., Zillikens,M.C., Amouyel,P., Boehm,B.O.,
            Boerwinkle,E., Boomsma,D.I., Caulfield,M.J., Chanock,S.J.,
            Cupples,L.A., Cusi,D., Dedoussis,G.V., Erdmann,J., Eriksson,J.G.,
            Franks,P.W., Froguel,P., Gieger,C., Gyllensten,U., Hamsten,A.,
            Harris,T.B., Hengstenberg,C., Hicks,A.A., Hingorani,A., Hinney,A.,
            Hofman,A., Hovingh,K.G., Hveem,K., Illig,T., Jarvelin,M.R.,
            Jockel,K.H., Keinanen-Kiukaanniemi,S.M., Kiemeney,L.A., Kuh,D.,
            Laakso,M., Lehtimaki,T., Levinson,D.F., Martin,N.G., Metspalu,A.,
            Morris,A.D., Nieminen,M.S., Njolstad,I., Ohlsson,C.,
            Oldehinkel,A.J., Ouwehand,W.H., Palmer,L.J., Penninx,B., Power,C.,
            Province,M.A., Psaty,B.M., Qi,L., Rauramaa,R., Ridker,P.M.,
            Ripatti,S., Salomaa,V., Samani,N.J., Snieder,H., Sorensen,T.I.,
            Spector,T.D., Stefansson,K., Tonjes,A., Tuomilehto,J.,
            Uitterlinden,A.G., Uusitupa,M., van der Harst,P., Vollenweider,P.,
            Wallaschofski,H., Wareham,N.J., Watkins,H., Wichmann,H.E.,
            Wilson,J.F., Abecasis,G.R., Assimes,T.L., Barroso,I., Boehnke,M.,
            Borecki,I.B., Deloukas,P., Fox,C.S., Frayling,T., Groop,L.C.,
            Haritunian,T., Heid,I.M., Hunter,D., Kaplan,R.C., Karpe,F.,
            Moffatt,M.F., Mohlke,K.L., O'Connell,J.R., Pawitan,Y., Schadt,E.E.,
            Schlessinger,D., Steinthorsdottir,V., Strachan,D.P.,
            Thorsteinsdottir,U., van Duijn,C.M., Visscher,P.M., Di Blasio,A.M.,
            Hirschhorn,J.N., Lindgren,C.M., Morris,A.P., Meyre,D., Scherag,A.,
            McCarthy,M.I., Speliotes,E.K., North,K.E., Loos,R.J. and
            Ingelsson,E.
  TITLE     Genome-wide meta-analysis identifies 11 new loci for anthropometric
            traits and provides insights into genetic architecture
  JOURNAL   Nat Genet 45 (5), 501-512 (2013)
   PUBMED   23563607
REFERENCE   7  (residues 1 to 626)
  AUTHORS   Zhao,J., Li,M., Bradfield,J.P., Zhang,H., Mentch,F.D., Wang,K.,
            Sleiman,P.M., Kim,C.E., Glessner,J.T., Hou,C., Keating,B.J.,
            Thomas,K.A., Garris,M.L., Deliard,S., Frackelton,E.C., Otieno,F.G.,
            Chiavacci,R.M., Berkowitz,R.I., Hakonarson,H. and Grant,S.F.
  TITLE     The role of height-associated loci identified in genome wide
            association studies in the determination of pediatric stature
  JOURNAL   BMC Med Genet 11, 96 (2010)
   PUBMED   20546612
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 626)
  AUTHORS   Okada,Y., Kamatani,Y., Takahashi,A., Matsuda,K., Hosono,N.,
            Ohmiya,H., Daigo,Y., Yamamoto,K., Kubo,M., Nakamura,Y. and
            Kamatani,N.
  TITLE     A genome-wide association study in 19 633 Japanese subjects
            identified LHX3-QSOX2 and IGF1 as adult height loci
  JOURNAL   Hum Mol Genet 19 (11), 2303-2312 (2010)
   PUBMED   20189936
REFERENCE   9  (residues 1 to 626)
  AUTHORS   Schegg,B., Hulsmeier,A.J., Rutschmann,C., Maag,C. and Hennet,T.
  TITLE     Core glycosylation of collagen is initiated by two
            beta(1-O)galactosyltransferases
  JOURNAL   Mol Cell Biol 29 (4), 943-952 (2009)
   PUBMED   19075007
  REMARK    GeneRIF: Two collagen beta(1-O)galactosyltransferases corresponding
            to the GLT25D1 and GLT25D2 proteins were identified.
REFERENCE   10 (residues 1 to 626)
  AUTHORS   Sood,R., Bonner,T.I., Makalowska,I., Stephan,D.A., Robbins,C.M.,
            Connors,T.D., Morgenbesser,S.D., Su,K., Faruque,M.U., Pinkett,H.,
            Graham,C., Baxevanis,A.D., Klinger,K.W., Landes,G.M., Trent,J.M.
            and Carpten,J.D.
  TITLE     Cloning and characterization of 13 novel transcripts and the human
            RGS8 gene from the 1q25 region encompassing the hereditary prostate
            cancer (HPC1) locus
  JOURNAL   Genomics 73 (2), 211-222 (2001)
   PUBMED   11318611
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC035672.1, AB011156.1 and BQ477485.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF288389.1, AB011156.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361927.9/ ENSP00000354960.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.3"
     Protein         1..626
                     /product="procollagen galactosyltransferase 2 isoform
                     1precursor"
                     /EC_number="2.4.1.50"
                     /note="procollagen galactosyltransferase 2; hydroxylysine
                     galactosyltransferase 2; glycosyltransferase 25 family
                     member 2; glycosyltransferase 25 domain containing 2"
                     /calculated_mol_wt=70100
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2842
     mat_peptide     28..626
                     /product="Procollagen galactosyltransferase 2.
                     /id=PRO_0000309541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYK4.1)"
                     /calculated_mol_wt=70100
     Site            order(60,62,90,167,169)
                     /site_type="active"
                     /db_xref="CDD:132997"
     Region          62..175
                     /region_name="Glyco_tranf_GTA_type"
                     /note="Glycosyltransferase family A (GT-A) includes
                     diverse families of glycosyl transferases with a common
                     GT-A type structural fold; cl11394"
                     /db_xref="CDD:472172"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IYK4.1)"
     Site            185
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IYK4.1)"
     Region          341..526
                     /region_name="Glyco_transf_25"
                     /note="Glycosyltransferase family 25 (LPS biosynthesis
                     protein); pfam01755"
                     /db_xref="CDD:366794"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IYK4.1)"
     Site            580
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IYK4.1)"
     Region          604..626
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYK4.1)"
     Region          623..626
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU10138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYK4.1)"
     CDS             1..626
                     /gene="COLGALT2"
                     /gene_synonym="C1orf17; ColGalT 2; GLT25D2"
                     /coded_by="NM_015101.4:372..2252"
                     /note="isoform 1precursor is encoded by transcript variant
                     1"
                     /db_xref="CCDS:CCDS1360.1"
                     /db_xref="GeneID:23127"
                     /db_xref="HGNC:HGNC:16790"
                     /db_xref="MIM:617533"
ORIGIN      
        1 maarpaatla wsllllssal lregcrarfv aerdseddge epvvfpespl qsptvlvavl
       61 arnaahtlph flgclerldy pksrmaiwaa tdhnvdntte ifrewlknvq rlyhyvewrp
      121 mdepesypde igpkhwptsr fahvmklrqa alrtarekws dyilfidvdn fltnpqtlnl
      181 liaenktiva pmlesrglys nfwcgitpkg fykrtpdyvq irewkrtgcf pvpmvhstfl
      241 idlrkeasdk ltfypphqdy twtfddiivf afssrqagiq mylcnrehyg ylpiplkphq
      301 tlqedienli hvqieamidr ppmepsqyvs vvpkypdkmg fdeifminlk rrkdrrdrml
      361 rtlyeqeiev kiveavdgka lntsqlkaln iemlpgyrdp yssrpltrge igcflshysv
      421 wkevidrele ktlvieddvr fehqfkkklm klmdnidqaq ldweliyigr krmqvkepek
      481 avpnvanlve adysywtlgy vislegaqkl vganpfgkml pvdeflpvmy nkhpvaeyke
      541 yyesrdlkaf saeplliypt hytgqpgyls dtetstiwdn etvatdwdrt hawksrkqsr
      601 iysnakntea lppptsldtv psrdel
//
LOCUS       NP_001025030             260 aa            linear   PRI 27-APR-2025
DEFINITION  BTB/POZ domain-containing protein KCTD21 [Homo sapiens].
ACCESSION   NP_001025030 XP_374915
VERSION     NP_001025030.1
DBSOURCE    REFSEQ: accession NM_001029859.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Spiombi,E., Angrisani,A., Fonte,S., De Feudis,G., Fabretti,F.,
            Cucchi,D., Izzo,M., Infante,P., Miele,E., Po,A., Di Magno,L.,
            Magliozzi,R., Guardavaccaro,D., Maroder,M., Canettieri,G.,
            Giannini,G., Ferretti,E., Gulino,A., Di Marcotullio,L., Moretti,M.
            and De Smaele,E.
  TITLE     KCTD15 inhibits the Hedgehog pathway in Medulloblastoma cells by
            increasing protein levels of the oncosuppressor KCASH2
  JOURNAL   Oncogenesis 8 (11), 64 (2019)
   PUBMED   31685809
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 260)
  AUTHORS   De Smaele,E., Di Marcotullio,L., Moretti,M., Pelloni,M.,
            Occhione,M.A., Infante,P., Cucchi,D., Greco,A., Pietrosanti,L.,
            Todorovic,J., Coni,S., Canettieri,G., Ferretti,E., Bei,R.,
            Maroder,M., Screpanti,I. and Gulino,A.
  TITLE     Identification and characterization of KCASH2 and KCASH3, 2 novel
            Cullin3 adaptors suppressing histone deacetylase and Hedgehog
            activity in medulloblastoma
  JOURNAL   Neoplasia 13 (4), 374-385 (2011)
   PUBMED   21472142
  REMARK    GeneRIF: Rescuing KCASHs expression reduces the Hedgehog-dependent
            medulloblastoma growth, suggesting that loss of members of this
            novel family of native HDAC inhibitors is crucial in sustaining Hh
            pathway-mediated tumorigenesis.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC342183.1 and AK095233.1.
            
            On Jul 27, 2005 this sequence version replaced XP_374915.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DC325444.1, BC036058.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340067.4/ ENSP00000339340.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1"
     Protein         1..260
                     /product="BTB/POZ domain-containing protein KCTD21"
                     /note="potassium channel tetramerisation domain containing
                     21; potassium channel tetramerization domain-containing
                     protein 21"
                     /calculated_mol_wt=29512
     Region          3..100
                     /region_name="BTB_POZ_KCTD21"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     channel tetramerization domain-containing protein 21
                     (KCTD21); cd18395"
                     /db_xref="CDD:349703"
     Region          107..260
                     /region_name="KCTD11_21_C"
                     /note="BTB/POZ domain-containing protein KCTD11/21
                     C-terminus; pfam19329"
                     /db_xref="CDD:466043"
     CDS             1..260
                     /gene="KCTD21"
                     /gene_synonym="KCASH2"
                     /coded_by="NM_001029859.3:84..866"
                     /db_xref="CCDS:CCDS31645.1"
                     /db_xref="GeneID:283219"
                     /db_xref="HGNC:HGNC:27452"
                     /db_xref="MIM:618790"
ORIGIN      
        1 msdpitlnvg gklyttslat ltsfpdsmlg amfsgkmptk rdsqgncfid rdgkvfryil
       61 nflrtshldl pedfqemgll rreadfyqvq pliealqeke velskaekna mlnitlnqrv
      121 qtvhftvrea pqiyslssss mevfnanifs tsclflkllg sklfycsngn lssitshlqd
      181 pnhltldwva nveglpeeey tkqnlkrlwv vpankqinsf qvfveevlki alsdgfcids
      241 shphaldfmn nkiirliryr
//
LOCUS       NP_808445                558 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial nucleoid-associated protein 1 [Mus musculus].
ACCESSION   NP_808445 XP_995940
VERSION     NP_808445.2
DBSOURCE    REFSEQ: accession NM_177777.6
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Wu,H., Zhang,W., Xu,F., Peng,K., Liu,X., Ding,W., Ma,Q., Cheng,H.
            and Wang,X.
  TITLE     C17orf80 binds the mitochondrial genome to promote its replication
  JOURNAL   J Cell Biol 222 (10) (2023)
   PUBMED   37676315
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Ko,M.S., Threat,T.A., Wang,X., Horton,J.H., Cui,Y., Wang,X.,
            Pryor,E., Paris,J., Wells-Smith,J., Kitchen,J.R., Rowe,L.B.,
            Eppig,J., Satoh,T., Brant,L., Fujiwara,H., Yotsumoto,S. and
            Nakashima,H.
  TITLE     Genome-wide mapping of unselected transcripts from extraembryonic
            tissue of 7.5-day mouse embryos reveals enrichment in the t-complex
            and under-representation on the X chromosome
  JOURNAL   Hum Mol Genet 7 (12), 1967-1978 (1998)
   PUBMED   9811942
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL603706.13.
            
            On or before May 4, 2006 this sequence version replaced
            XP_995940.1, NP_808445.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC048942.1, SRR7345562.3542185.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 79.15 cM"
     Protein         1..558
                     /product="mitochondrial nucleoid-associated protein 1"
                     /note="uncharacterized protein C17orf80 homolog"
                     /calculated_mol_wt=60145
     Region          29..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PIX9.3)"
     Region          130..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PIX9.3)"
     Region          222..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PIX9.3)"
     Site            528..548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PIX9.3)"
     CDS             1..558
                     /gene="Mtnap1"
                     /gene_synonym="D11Wsu47e; Gm57859"
                     /coded_by="NM_177777.6:385..2061"
                     /db_xref="CCDS:CCDS48976.1"
                     /db_xref="GeneID:276852"
                     /db_xref="MGI:MGI:106356"
ORIGIN      
        1 mgaaeprmev cpyckkpfkr lkshlphckm rgpsisadqn vsqskpaala qkeksptrdl
       61 trakekelev drpkravkae tsraswtaaa splpegilgs vritkaegen kdqnqfsfqa
      121 lsqakpevtl qrvttpwspa sdatspkrel tqdvseskgs pcpseteaps lvssvepfla
      181 nqdrkysstq phanpatsvg lklgtvdpqr qklrvklldv plsdrhspks gshgvqrvtp
      241 svlsreegsq dgghllgvsa hpgntktqks eslllglhtg llgkapvreh qelglgmels
      301 qskgntenrm svtnvqegag lgqggkdpit atkakphtal elrnvfmpes gnqsltspav
      361 tstpeenaqf cgqshvpait lsvgsvrdvl eptsfyqpht aqaghclmsy saqypvpktf
      421 vghvaavtsg apprsvglew fpelypayvg lgvlprrppp wslaaqvppl ptlqgrsvsk
      481 vpwwgrssad srslepltlt tsslplmrll gavhkgwvqc nttikksgvg gltmlfagyf
      541 ilccnwsfkh lklqhwrk
//
LOCUS       NP_932355                538 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 155 isoform 1 [Homo sapiens].
ACCESSION   NP_932355
VERSION     NP_932355.3
DBSOURCE    REFSEQ: accession NM_198089.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Shannon,M., Hamilton,A.T., Gordon,L., Branscomb,E. and Stubbs,L.
  TITLE     Differential expansion of zinc-finger transcription factor loci in
            homologous human and mouse gene clusters
  JOURNAL   Genome Res 13 (6A), 1097-1110 (2003)
   PUBMED   12743021
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Shannon,M., Ashworth,L.K., Mucenski,M.L., Lamerdin,J.E.,
            Branscomb,E. and Stubbs,L.
  TITLE     Comparative analysis of a conserved zinc finger gene cluster on
            human chromosome 19q and mouse chromosome 7
  JOURNAL   Genomics 33 (1), 112-120 (1996)
   PUBMED   8617494
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006213.1.
            
            On Nov 23, 2018 this sequence version replaced NP_932355.2.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3 and 4 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.200801.1,
                                           SRR1803613.93900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270014.7/ ENSP00000270014.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..538
                     /product="zinc finger protein 155 isoform 1"
                     /note="KRAB A domain"
                     /calculated_mol_wt=61950
     Region          8..67
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          178..198
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          202..>486
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          206..226
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(211,213,215,217..218,221..222,225,239,241,245..246,
                     249..250,253,267,269,271,273..274,277..278,281)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          234..254
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          262..282
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          290..310
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          318..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          346..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          374..394
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          402..422
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(407,409,411,413..414,417..418,421,435,437,441..442,
                     445..446,449,463,465,467,469..470,473..474,477)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          430..450
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          458..478
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..538
                     /gene="ZNF155"
                     /gene_synonym="pHZ-96"
                     /coded_by="NM_198089.3:144..1760"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12634.1"
                     /db_xref="GeneID:7711"
                     /db_xref="HGNC:HGNC:12940"
                     /db_xref="MIM:604086"
ORIGIN      
        1 mttfkeavtf kdvavvftee elglldpaqr klyrdvmlen frnllsvghq pfhqdtchfl
       61 reekfwmmgt atqregnsgg kiqtelesvp eagaheewsc qqiweqiakd ltrsqdsiin
      121 nsqffengdv psqveaglpt ihtgqkpsqg gkckqsisdv pifdlpqqly seeksytcde
      181 cgksicyisa lhvhqrvhvg eklfmcdvcg kefsqsshlq thqrvhtgek pfkceqcgkg
      241 fsrrsalnvh rklhtgekpy iceacgkafi hdsqlkehkr ihtgekpfkc dicgktfyfr
      301 srlkshsmvh tgekpfrcdt cdksfhqrsa lnrhcmvhtg ekpyrceqcg kgfigrldfy
      361 khqvvhtgek pynckecgks frwsscllnh qrvhsgeksf kceecgkgfy tnsqlsshqr
      421 shsgekpykc eecgkgyvtk fnldlhqrvh tgerpyncke cgknfsrass ilnhkrlhcq
      481 kkpfkcedcg krlvhrtyrk dqprdysgen pskcedcgrr ykrrlnldil lslflndt
//
LOCUS       NP_001029201             436 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-17 receptor E isoform 2 [Mus musculus].
ACCESSION   NP_001029201
VERSION     NP_001029201.1
DBSOURCE    REFSEQ: accession NM_001034029.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Wang,J., Wang,X., Wang,M., Wang,J., Wu,Y. and Qi,X.
  TITLE     Clinical significance of Interleukin 17 receptor E in diabetic
            nephropathy
  JOURNAL   Int Immunopharmacol 120, 110324 (2023)
   PUBMED   37235960
  REMARK    GeneRIF: Clinical significance of Interleukin 17 receptor E in
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Lin,X., Gaudino,S.J., Jang,K.K., Bahadur,T., Singh,A., Banerjee,A.,
            Beaupre,M., Chu,T., Wong,H.T., Kim,C.K., Kempen,C., Axelrad,J.,
            Huang,H., Khalid,S., Shah,V., Eskiocak,O., Parks,O.B., Berisha,A.,
            McAleer,J.P., Good,M., Hoshino,M., Blumberg,R., Bialkowska,A.B.,
            Gaffen,S.L., Kolls,J.K., Yang,V.W., Beyaz,S., Cadwell,K. and
            Kumar,P.
  TITLE     IL-17RA-signaling in Lgr5+ intestinal stem cells induces expression
            of transcription factor ATOH1 to promote secretory cell lineage
            commitment
  JOURNAL   Immunity 55 (2), 237-253 (2022)
   PUBMED   35081371
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Wang,J., Gong,J., Yang,Q., Wang,L., Jian,Y. and Wang,P.
  TITLE     Interleukin-17 Receptor E and C-C Motif Chemokine Receptor 10
            Identify Heterogeneous T Helper 17 Subsets in a Mouse Dry Eye
            Disease Model
  JOURNAL   Am J Pathol 192 (2), 332-343 (2022)
   PUBMED   35144761
  REMARK    GeneRIF: Interleukin-17 Receptor E and C-C Motif Chemokine Receptor
            10 Identify Heterogeneous T Helper 17 Subsets in a Mouse Dry Eye
            Disease Model.
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Hansakon,A., Jeerawattanawart,S., Pattanapanyasat,K. and
            Angkasekwinai,P.
  TITLE     IL-25 Receptor Signaling Modulates Host Defense against
            Cryptococcus neoformans Infection
  JOURNAL   J Immunol 205 (3), 674-685 (2020)
   PUBMED   32561567
  REMARK    GeneRIF: IL-25 Receptor Signaling Modulates Host Defense against
            Cryptococcus neoformans Infection.
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Vella,G., Lunding,L., Ritzmann,F., Honecker,A., Herr,C.,
            Wegmann,M., Bals,R. and Beisswenger,C.
  TITLE     The IL-17 receptor IL-17RE mediates polyIC-induced exacerbation of
            experimental allergic asthma
  JOURNAL   Respir Res 21 (1), 176 (2020)
   PUBMED   32641167
  REMARK    GeneRIF: The IL-17 receptor IL-17RE mediates polyIC-induced
            exacerbation of experimental allergic asthma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Chang,S.H., Reynolds,J.M., Pappu,B.P., Chen,G., Martinez,G.J. and
            Dong,C.
  TITLE     Interleukin-17C promotes Th17 cell responses and autoimmune disease
            via interleukin-17 receptor E
  JOURNAL   Immunity 35 (4), 611-621 (2011)
   PUBMED   21982598
  REMARK    GeneRIF: IL-17C-IL-17RE induced the expression of a nuclear IkappaB
            family member, IkappaBzeta, in Th17 cells to potentiate the Th17
            cell response
REFERENCE   7  (residues 1 to 436)
  AUTHORS   Ramirez-Carrozzi,V., Sambandam,A., Luis,E., Lin,Z., Jeet,S.,
            Lesch,J., Hackney,J., Kim,J., Zhou,M., Lai,J., Modrusan,Z., Sai,T.,
            Lee,W., Xu,M., Caplazi,P., Diehl,L., de Voss,J., Balazs,M.,
            Gonzalez,L. Jr., Singh,H., Ouyang,W. and Pappu,R.
  TITLE     IL-17C regulates the innate immune function of epithelial cells in
            an autocrine manner
  JOURNAL   Nat Immunol 12 (12), 1159-1166 (2011)
   PUBMED   21993848
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 436)
  AUTHORS   Swaidani,S., Bulek,K., Kang,Z., Liu,C., Lu,Y., Yin,W., Aronica,M.
            and Li,X.
  TITLE     The critical role of epithelial-derived Act1 in IL-17- and
            IL-25-mediated pulmonary inflammation
  JOURNAL   J Immunol 182 (3), 1631-1640 (2009)
   PUBMED   19155512
REFERENCE   9  (residues 1 to 436)
  AUTHORS   Li,T.S., Li,X.N., Chang,Z.J., Fu,X.Y. and Liu,L.
  TITLE     Identification and functional characterization of a novel
            interleukin 17 receptor: a possible mitogenic activation through
            ras/mitogen-activated protein kinase signaling pathway
  JOURNAL   Cell Signal 18 (8), 1287-1298 (2006)
   PUBMED   16310341
REFERENCE   10 (residues 1 to 436)
  AUTHORS   Maezawa,Y., Nakajima,H., Suzuki,K., Tamachi,T., Ikeda,K., Inoue,J.,
            Saito,Y. and Iwamoto,I.
  TITLE     Involvement of TNF receptor-associated factor 6 in IL-25 receptor
            signaling
  JOURNAL   J Immunol 176 (2), 1013-1018 (2006)
   PUBMED   16393988
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK044815.1, DQ092340.1 and AC153910.6.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ092340.1, SRR13422603.383317.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 52.76 cM"
     Protein         1..436
                     /product="interleukin-17 receptor E isoform 2"
                     /note="IL-17 receptor E"
                     /calculated_mol_wt=48443
     Region          <1..207
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Region          247..374
                     /region_name="SEFIR"
                     /note="SEFIR domain; pfam08357"
                     /db_xref="CDD:254756"
     CDS             1..436
                     /gene="Il17re"
                     /gene_synonym="IL-17RE; Il25r"
                     /coded_by="NM_001034029.2:712..2022"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS20421.1"
                     /db_xref="GeneID:57890"
                     /db_xref="MGI:MGI:1889371"
ORIGIN      
        1 mcieasylqe dtvrrkkcpf qswpeaygsd fwqsirftdy sqhnqmvmal tlrcplklea
       61 slcwrqdplt pcetlpnata qesegwyile nvdlhpqlcf kfsfensshv ecphqsgslp
      121 swtvsmdtqa qqltlhfssr tyatfsaaws dpglgpdtpm ppvysisqtq gsvpvtldli
      181 ipflrqenci lvwrsdvhfa wkhvlcpdvs hrhlgllila llaltalvgv vlvllgrrll
      241 pgsgrtrpvl llhaadseaq rrlvgalael lrtalgggrd vivdlwegth varigplpwl
      301 waarervare qgtvlllwnc agpstacsgd pqaaslrtll caaprpllla yfsrlcakgd
      361 iprplralpr yrllrdlprl lraldaqpat lasswshlga krclknrleq chlleleaak
      421 ddyqgstnsp cgfscl
//
LOCUS       NP_057038                318 aa            linear   PRI 27-APR-2025
DEFINITION  deoxyribose-phosphate aldolase isoform 1 [Homo sapiens].
ACCESSION   NP_057038
VERSION     NP_057038.2
DBSOURCE    REFSEQ: accession NM_015954.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Nitta,Y., Takeda,M., Fujii,T., Itami,H., Tsukamoto,S., Honoki,K.
            and Ohbayashi,C.
  TITLE     A case of pericytic neoplasm in the shoulder with a novel DERA-GLI1
            gene fusion
  JOURNAL   Histopathology 78 (3), 466-469 (2021)
   PUBMED   33067875
  REMARK    GeneRIF: A case of pericytic neoplasm in the shoulder with a novel
            DERA-GLI1 gene fusion.
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Gu,N., Dai,W., Liu,H., Ge,J., Luo,S., Cho,E., Amos,C.I., Lee,J.E.,
            Li,X., Nan,H., Yuan,H. and Wei,Q.
  TITLE     Genetic variants in TKT and DERA in the nicotinamide adenine
            dinucleotide phosphate pathway predict melanoma survival
  JOURNAL   Eur J Cancer 136, 84-94 (2020)
   PUBMED   32659474
  REMARK    GeneRIF: Genetic variants in TKT and DERA in the nicotinamide
            adenine dinucleotide phosphate pathway predict melanoma survival.
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Hoffmann,T.J., Tang,H., Thornton,T.A., Caan,B., Haan,M.,
            Millen,A.E., Thomas,F. and Risch,N.
  TITLE     Genome-wide association and admixture analysis of glaucoma in the
            Women's Health Initiative
  JOURNAL   Hum Mol Genet 23 (24), 6634-6643 (2014)
   PUBMED   25027321
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Salleron,L., Magistrelli,G., Mary,C., Fischer,N., Bairoch,A. and
            Lane,L.
  TITLE     DERA is the human deoxyribose phosphate aldolase and is involved in
            stress response
  JOURNAL   Biochim Biophys Acta 1843 (12), 2913-2925 (2014)
   PUBMED   25229427
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Andersson,J.O., Sjogren,A.M., Davis,L.A., Embley,T.M. and
            Roger,A.J.
  TITLE     Phylogenetic analyses of diplomonad genes reveal frequent lateral
            gene transfers affecting eukaryotes
  JOURNAL   Curr Biol 13 (2), 94-104 (2003)
   PUBMED   12546782
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Sgarrella,F., Poddie,F.P., Meloni,M.A., Sciola,L., Pippia,P. and
            Tozzi,M.G.
  TITLE     Channelling of deoxyribose moiety of exogenous DNA into
            carbohydrate metabolism: role of deoxyriboaldolase
  JOURNAL   Comp Biochem Physiol B Biochem Mol Biol 117 (2), 253-257 (1997)
   PUBMED   9226884
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC041328.1 and CB851336.1.
            
            On Oct 12, 2006 this sequence version replaced NP_057038.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.189350.1,
                                           SRR1660805.19903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000428559.7/ ENSP00000416583.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.3"
     Protein         1..318
                     /product="deoxyribose-phosphate aldolase isoform 1"
                     /EC_number="4.1.2.4"
                     /note="putative deoxyribose-phosphate aldolase;
                     deoxyriboaldolase; phosphodeoxyriboaldolase;
                     2-deoxy-D-ribose 5-phosphate aldolase;
                     2-deoxyribose-5-phosphate aldolase homolog;
                     deoxyribose-phosphate aldolase (putative)"
                     /calculated_mol_wt=35100
     Region          50..277
                     /region_name="DeoC"
                     /note="2-deoxyribose-5-phosphate aldolase (DERA) of the
                     DeoC family; cd00959"
                     /db_xref="CDD:188646"
     Site            order(59,61,63,103..105,129,137,142,147..150,159,161,
                     180..181,195)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:188646"
     Site            218
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188646"
     CDS             1..318
                     /gene="DERA"
                     /gene_synonym="CGI-26; DEOC"
                     /coded_by="NM_015954.4:53..1009"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44838.1"
                     /db_xref="GeneID:51071"
                     /db_xref="HGNC:HGNC:24269"
                     /db_xref="MIM:619668"
ORIGIN      
        1 msahnrgtel dlswiskiqv nhpavlrrae qiqarrtvkk ewqaawllka vtfidlttls
       61 gddtssniqr lcykakypir edllkalnmh dkgittaavc vyparvcdav kalkaagcni
      121 pvasvaagfp agqthlktrl eeirlavedg ateidvvinr slvltgqwea lydeirqfrk
      181 acgeahlkti latgelgtlt nvykasmiam magsdfikts tgketvnatf pvaivmlrai
      241 rdffwktgnk igfkpaggir sakdslawls lvkeelgdew lkpelfriga stllsdierq
      301 iyhhvtgrya ayhdlpms
//
LOCUS       NP_001352406            1086 aa            linear   PLN 27-APR-2025
DEFINITION  auxin response factor 21 [Zea mays].
ACCESSION   NP_001352406 XP_008663905
VERSION     NP_001352406.1
DBSOURCE    REFSEQ: accession NM_001365477.1
KEYWORDS    RefSeq.
SOURCE      Zea mays
  ORGANISM  Zea mays
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD
            clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
            Zea.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Schnable,P.S., Ware,D., Fulton,R.S., Stein,J.C., Wei,F.,
            Pasternak,S., Liang,C., Zhang,J., Fulton,L., Graves,T.A., Minx,P.,
            Reily,A.D., Courtney,L., Kruchowski,S.S., Tomlinson,C., Strong,C.,
            Delehaunty,K., Fronick,C., Courtney,B., Rock,S.M., Belter,E.,
            Du,F., Kim,K., Abbott,R.M., Cotton,M., Levy,A., Marchetto,P.,
            Ochoa,K., Jackson,S.M., Gillam,B., Chen,W., Yan,L.,
            Higginbotham,J., Cardenas,M., Waligorski,J., Applebaum,E.,
            Phelps,L., Falcone,J., Kanchi,K., Thane,T., Scimone,A., Thane,N.,
            Henke,J., Wang,T., Ruppert,J., Shah,N., Rotter,K., Hodges,J.,
            Ingenthron,E., Cordes,M., Kohlberg,S., Sgro,J., Delgado,B.,
            Mead,K., Chinwalla,A., Leonard,S., Crouse,K., Collura,K.,
            Kudrna,D., Currie,J., He,R., Angelova,A., Rajasekar,S., Mueller,T.,
            Lomeli,R., Scara,G., Ko,A., Delaney,K., Wissotski,M., Lopez,G.,
            Campos,D., Braidotti,M., Ashley,E., Golser,W., Kim,H., Lee,S.,
            Lin,J., Dujmic,Z., Kim,W., Talag,J., Zuccolo,A., Fan,C.,
            Sebastian,A., Kramer,M., Spiegel,L., Nascimento,L., Zutavern,T.,
            Miller,B., Ambroise,C., Muller,S., Spooner,W., Narechania,A.,
            Ren,L., Wei,S., Kumari,S., Faga,B., Levy,M.J., McMahan,L., Van
            Buren,P., Vaughn,M.W., Ying,K., Yeh,C.T., Emrich,S.J., Jia,Y.,
            Kalyanaraman,A., Hsia,A.P., Barbazuk,W.B., Baucom,R.S.,
            Brutnell,T.P., Carpita,N.C., Chaparro,C., Chia,J.M., Deragon,J.M.,
            Estill,J.C., Fu,Y., Jeddeloh,J.A., Han,Y., Lee,H., Li,P.,
            Lisch,D.R., Liu,S., Liu,Z., Nagel,D.H., McCann,M.C., SanMiguel,P.,
            Myers,A.M., Nettleton,D., Nguyen,J., Penning,B.W., Ponnala,L.,
            Schneider,K.L., Schwartz,D.C., Sharma,A., Soderlund,C.,
            Springer,N.M., Sun,Q., Wang,H., Waterman,M., Westerman,R.,
            Wolfgruber,T.K., Yang,L., Yu,Y., Zhang,L., Zhou,S., Zhu,Q.,
            Bennetzen,J.L., Dawe,R.K., Jiang,J., Jiang,N., Presting,G.G.,
            Wessler,S.R., Aluru,S., Martienssen,R.A., Clifton,S.W.,
            McCombie,W.R., Wing,R.A. and Wilson,R.K.
  TITLE     The B73 maize genome: complexity, diversity, and dynamics
  JOURNAL   Science 326 (5956), 1112-1115 (2009)
   PUBMED   19965430
  REMARK    Erratum:[Science. 2012 Aug 31;337(6098):1040]
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Emrich,S.J., Barbazuk,W.B., Li,L. and Schnable,P.S.
  TITLE     Gene discovery and annotation using LCM-454 transcriptome
            sequencing
  JOURNAL   Genome Res 17 (1), 69-73 (2007)
   PUBMED   17095711
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Verwoert,I.I., Brown,A., Slabas,A.R. and Stuitje,A.R.
  TITLE     A Zea mays GTP-binding protein of the ARF family complements an
            Escherichia coli mutant with a temperature-sensitive
            malonyl-coenzyme A:acyl carrier protein transacylase
  JOURNAL   Plant Mol Biol 27 (3), 629-633 (1995)
   PUBMED   7894026
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO533792.1, GECS01000256.1, BM501590.1, DY533360.1, BM660237.1,
            EB401482.1, EB166268.1, DR786430.1, DN215539.1, CO529039.1 and
            DW742786.1.
            
            On Aug 29, 2018 this sequence version replaced XP_008663905.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3147024.12699.1,
                                           SRR3147048.8707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00780084, SAMN00780085
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Zea mays"
                     /cultivar="B73"
                     /db_xref="taxon:4577"
                     /chromosome="1"
                     /map="1"
     Protein         1..1086
                     /product="auxin response factor 21"
                     /note="ARF transcription factor; auxin response factor 1"
                     /calculated_mol_wt=120039
     Region          131..233
                     /region_name="B3"
                     /note="B3 DNA binding domain; pfam02362"
                     /db_xref="CDD:396783"
     Site            order(133,136,144,147,149,184,195,197..198,200..201)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:197383"
     Region          263..340
                     /region_name="Auxin_resp"
                     /note="Auxin response factor; pfam06507"
                     /db_xref="CDD:428981"
     Region          <970..1048
                     /region_name="AUX_IAA"
                     /note="AUX/IAA family; pfam02309"
                     /db_xref="CDD:460529"
     CDS             1..1086
                     /gene="LOC103642400"
                     /gene_synonym="ARF1; GRMZM2G169820"
                     /coded_by="NM_001365477.1:134..3394"
                     /db_xref="GeneID:103642400"
ORIGIN      
        1 meapgtssgg aggegaggtk vneelwyaca gplvalppag slvvyfpqgh seqvaasmrk
       61 dadakipsyp nlssklicil rsvtmladpd tdevyarmtl qpvsnvthcd ketllatela
      121 lkqtrpqtef fcktltasdt sthggfsvpr raaerifphl dfsvqppaqe lqardlhdai
      181 wtfrhiyrgq pkrhllttgw slfvsgkrll agdsvlfird grqqlllgir ranrqpvnls
      241 ssvlssdsmh igilaaaaha aannsqftvf ynpraspsef vipfakyqka vysnqlslgm
      301 rfrmmfetee satrrymgti tgisdmdplr wknsqwrniq vawdeaapse rrtrvslwev
      361 epviapffiy psplftakrp rqpgvtddds semdnlfkrt mpwfgeevgk rdlstqnglv
      421 pglslvqwmn mqhnpslant vmqpellnsl agkpvqtlaa adlsrqisfq pqflqqnniq
      481 fntsllppqn qqteqlanvi atpnqlgsvi vpqkavqnss seqkqnlvtq plqvsqpmvs
      541 vaqpqlvhtq lqqpqvvlqa qpqqpqvivq aqlqqqqplv qnhttiqsgl qqiqllqqqq
      601 vqqsvqeqqq ikiqpfqvpn danmvtqlsd qmkiqllkal qpqqplvmeq qkmifdlqqq
      661 avnsqstaqq csqvatqvvg lhssstnqyp tqqktqplkt fqdfpgnavs ivkpeivtsv
      721 garslhvpgg vqsmkmdevp ssstspstnn npvilrstps ssknqclpta akapqssvvl
      781 gstleqgmkp cdstqhpmvi pklaeerpat gqdymnstql dyldtsssat svclsqadgs
      841 lqqsfppssf nqhqplreav pdsefevtda gnnflfgani dghmeplned dllgtafead
      901 kymeqmpgng isnyisskds qqelsssmis hpfgvadiaf nsidssindi qflnrnsrap
      961 gpvqqrmrty tkvhkrgavg rsidinrysg ydelkhdvar mfgiegqlsd qnrvgwklvy
     1021 edhekdvllv gddpwedfvn cvrcirilsp qeerqmrlas dygdsflgnq acsssdggrp
     1081 wrvtgd
//
LOCUS       NP_005841                424 aa            linear   PRI 27-APR-2025
DEFINITION  splicing factor 3B subunit 4 [Homo sapiens].
ACCESSION   NP_005841
VERSION     NP_005841.1
DBSOURCE    REFSEQ: accession NM_005850.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Yang,S., Ko,M., Hur,S.C., Lee,E.K. and Jeong,S.M.
  TITLE     SF3B4 Regulates Cellular Senescence and Suppresses Therapy-induced
            Senescence of Cancer Cells
  JOURNAL   Cancer Genomics Proteomics 21 (6), 622-629 (2024)
   PUBMED   39467623
  REMARK    GeneRIF: SF3B4 Regulates Cellular Senescence and Suppresses
            Therapy-induced Senescence of Cancer Cells.
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   He,G., Gu,K., Wei,J. and Zhang,J.
  TITLE     METTL3-mediated the m6A modification of SF3B4 facilitates the
            development of non-small cell lung cancer by enhancing LSM4
            expression
  JOURNAL   Thorac Cancer 15 (11), 919-928 (2024)
   PUBMED   38462740
  REMARK    GeneRIF: METTL3-mediated the m6A modification of SF3B4 facilitates
            the development of non-small cell lung cancer by enhancing LSM4
            expression.
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Yang,H., Sui,L., Cai,C., Chu,H. and Diao,Y.
  TITLE     SETDB1 promotes progression through upregulation of SF3B4
            expression and regulates the immunity in ovarian cancer
  JOURNAL   J Ovarian Res 17 (1), 34 (2024)
   PUBMED   38317200
  REMARK    GeneRIF: SETDB1 promotes progression through upregulation of SF3B4
            expression and regulates the immunity in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Yang,F., Bian,T., Zhan,X., Chen,Z., Xing,Z., Larsen,N.A., Zhang,X.
            and Shi,Y.
  TITLE     Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP
            assembly
  JOURNAL   Nat Commun 14 (1), 897 (2023)
   PUBMED   36797247
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Will,C.L., Schneider,C., MacMillan,A.M., Katopodis,N.F.,
            Neubauer,G., Wilm,M., Luhrmann,R. and Query,C.C.
  TITLE     A novel U2 and U11/U12 snRNP protein that associates with the
            pre-mRNA branch site
  JOURNAL   EMBO J 20 (16), 4536-4546 (2001)
   PUBMED   11500380
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Das,R., Zhou,Z. and Reed,R.
  TITLE     Functional association of U2 snRNP with the ATP-independent
            spliceosomal complex E
  JOURNAL   Mol Cell 5 (5), 779-787 (2000)
   PUBMED   10882114
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Das,B.K., Xia,L., Palandjian,L., Gozani,O., Chyung,Y. and Reed,R.
  TITLE     Characterization of a protein complex containing spliceosomal
            proteins SAPs 49, 130, 145, and 155
  JOURNAL   Mol Cell Biol 19 (10), 6796-6802 (1999)
   PUBMED   10490618
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Champion-Arnaud,P. and Reed,R.
  TITLE     The prespliceosome components SAP 49 and SAP 145 interact in a
            complex implicated in tethering U2 snRNP to the branch site
  JOURNAL   Genes Dev 8 (16), 1974-1983 (1994)
   PUBMED   7958871
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA535996.1, BC004273.1 and
            AI925089.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes one of four subunits of the splicing
            factor 3B. The protein encoded by this gene cross-links to a region
            in the pre-mRNA immediately upstream of the branchpoint sequence in
            pre-mRNA in the prespliceosomal complex A. It also may be involved
            in the assembly of the B, C and E spliceosomal complexes. In
            addition to RNA-binding activity, this protein interacts directly
            and highly specifically with subunit 2 of the splicing factor 3B.
            This protein contains two N-terminal RNA-recognition motifs (RRMs),
            consistent with the observation that it binds directly to pre-mRNA.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223322.1, AK097315.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000271628.9/ ENSP00000271628.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..424
                     /product="splicing factor 3B subunit 4"
                     /note="spliceosome-associated protein (U2 snRNP);
                     spliceosomal protein; SAP 49; SF3b50;
                     spliceosome-associated protein 49; splicing factor 3b,
                     subunit 4, 49kD; splicing factor 3b, subunit 4, 49kDa;
                     pre-mRNA-splicing factor SF3b 49 kDa subunit"
                     /calculated_mol_wt=44255
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q15427.1)"
     Region          15..88
                     /region_name="RRM1_SF3B4"
                     /note="RNA recognition motif 1 (RRM1) found in splicing
                     factor 3B subunit 4 (SF3B4) and similar proteins; cd12334"
                     /db_xref="CDD:409771"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q15427.1)"
     Region          99..181
                     /region_name="RRM2_SF3B4"
                     /note="RNA recognition motif 2 (RRM2) found in splicing
                     factor 3B subunit 4 (SF3B4) and similar proteins; cd12335"
                     /db_xref="CDD:409772"
     Region          207..424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15427.1)"
     CDS             1..424
                     /gene="SF3B4"
                     /gene_synonym="AFD1; Hsh49; SAP49; SF3b49"
                     /coded_by="NM_005850.5:45..1319"
                     /db_xref="CCDS:CCDS72900.1"
                     /db_xref="GeneID:10262"
                     /db_xref="HGNC:HGNC:10771"
                     /db_xref="MIM:605593"
ORIGIN      
        1 maagpisern qdatvyvggl dekvsepllw elflqagpvv nthmpkdrvt gqhqgygfve
       61 flseedadya ikimnmikly gkpirvnkas ahnknldvga nifignldpe idekllydtf
      121 safgvilqtp kimrdpdtgn skgyafinfa sfdasdaaie amngqylcnr pitvsyafkk
      181 dskgerhgsa aerllaaqnp lsqadrphql fadappppsa pnpvvsslgs glpppgmppp
      241 gsfpppvppp galppgippa mppppmppga aghgppsagt pgaghpghgh shphpfppgg
      301 mphpgmsqmq lahhgphglg hphagppgsg gqppprpppg mphpgpppmg mpprgppfgs
      361 pmghpgpmpp hgmrgppplm pphgytgppr pppygyqrgp lppprptprp pvpprgplrg
      421 plpq
//
LOCUS       NP_001356426             446 aa            linear   PRI 27-APR-2025
DEFINITION  carabin isoform 1 [Homo sapiens].
ACCESSION   NP_001356426 XP_006718603
VERSION     NP_001356426.1
DBSOURCE    REFSEQ: accession NM_001369497.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Qiao,H., Lv,R., Pang,Y., Yao,Z., Zhou,X., Zhu,W. and Zhou,W.
  TITLE     Weighted Gene Coexpression Network Analysis Identifies TBC1D10C as
            a New Prognostic Biomarker for Breast Cancer
  JOURNAL   Anal Cell Pathol (Amst) 2022, 5259187 (2022)
   PUBMED   35425695
  REMARK    GeneRIF: Weighted Gene Coexpression Network Analysis Identifies
            TBC1D10C as a New Prognostic Biomarker for Breast Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Jiang,W., Zhou,X., Li,Z., Liu,K., Wang,W., Tan,R., Cong,X.,
            Shan,J., Zhan,Y., Cui,Z., Jiang,L., Li,Q., Shen,S., Bai,M.,
            Cheng,Y., Li,B., Tan,M., Ma,D.K., Liu,J.O. and Dang,Y.
  TITLE     Prolyl 4-hydroxylase 2 promotes B-cell lymphoma progression via
            hydroxylation of Carabin
  JOURNAL   Blood 131 (12), 1325-1336 (2018)
   PUBMED   29437589
  REMARK    GeneRIF: identify prolyl 4-hydroxylase 2 (P4HA2) as a specific
            proline hydroxylase of Carabin. Carabin hydroxylation leads to its
            proteasomal degradation, thereby activating the Ras/extracellular
            signal-regulated kinase pathway and increasing B-cell lymphoma
            proliferation.
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Schickel,J.N., Pasquali,J.L., Soley,A., Knapp,A.M., Decossas,M.,
            Kern,A., Fauny,J.D., Marcellin,L., Korganow,A.S., Martin,T. and
            Soulas-Sprauel,P.
  TITLE     Carabin deficiency in B cells increases BCR-TLR9
            costimulation-induced autoimmunity
  JOURNAL   EMBO Mol Med 4 (12), 1261-1275 (2012)
   PUBMED   23109291
  REMARK    GeneRIF: Carabin as a new negative regulator of B-cell function,
            whose deficiency in B cells speeds up early B-cell responses
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Hsu,C., Morohashi,Y., Yoshimura,S., Manrique-Hoyos,N., Jung,S.,
            Lauterbach,M.A., Bakhti,M., Gronborg,M., Mobius,W., Rhee,J.,
            Barr,F.A. and Simons,M.
  TITLE     Regulation of exosome secretion by Rab35 and its GTPase-activating
            proteins TBC1D10A-C
  JOURNAL   J Cell Biol 189 (2), 223-232 (2010)
   PUBMED   20404108
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Datta,D., Contreras,A.G., Basu,A., Dormond,O., Flynn,E.,
            Briscoe,D.M. and Pal,S.
  TITLE     Calcineurin inhibitors activate the proto-oncogene Ras and promote
            protumorigenic signals in renal cancer cells
  JOURNAL   Cancer Res 69 (23), 8902-8909 (2009)
   PUBMED   19903851
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Fuchs,E., Haas,A.K., Spooner,R.A., Yoshimura,S., Lord,J.M. and
            Barr,F.A.
  TITLE     Specific Rab GTPase-activating proteins define the Shiga toxin and
            epidermal growth factor uptake pathways
  JOURNAL   J Cell Biol 177 (6), 1133-1143 (2007)
   PUBMED   17562788
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Pan,F., Sun,L., Kardian,D.B., Whartenby,K.A., Pardoll,D.M. and
            Liu,J.O.
  TITLE     Feedback inhibition of calcineurin and Ras by a dual inhibitory
            protein Carabin
  JOURNAL   Nature 445 (7126), 433-436 (2007)
   PUBMED   17230191
  REMARK    GeneRIF: Carabin is a negative feedback inhibitor of the
            calcineurin signalling pathway that also mediates crosstalk between
            calcineurin and Ras
            GeneRIF: Carabin inhibits calcineurin and Ras and was identified by
            a yeast-two-hybrid screen with calcineurin
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003419.3.
            
            On Apr 10, 2019 this sequence version replaced XP_006718603.1.
            
            Summary: The protein encoded by this gene has an N-terminal
            Rab-GTPase domain and a binding site at the C-terminus for
            calcineurin, and is an inhibitor of both the Ras signaling pathway
            and calcineurin, a phosphatase regulated by calcium and calmodulin.
            Genes encoding similar proteins are located on chromosomes 16 and
            22. Multiple transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, Jan 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.252836.1,
                                           SRR1163658.376441.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..446
                     /product="carabin isoform 1"
                     /calculated_mol_wt=49582
     Region          1..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IV04.1)"
     Region          89..294
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            137
                     /site_type="other"
                     /note="Arginine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q8IV04.1)"
     Site            178
                     /site_type="other"
                     /note="Glutamine finger. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q8IV04.1)"
     Region          384..446
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IV04.1)"
     Region          406..446
                     /region_name="Interaction with calcineurin"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IV04.1)"
     CDS             1..446
                     /gene="TBC1D10C"
                     /gene_synonym="CARABIN; EPI64C"
                     /coded_by="NM_001369497.1:24..1364"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS8162.1"
                     /db_xref="GeneID:374403"
                     /db_xref="HGNC:HGNC:24702"
                     /db_xref="MIM:610831"
ORIGIN      
        1 maqalgedlv qppelqddss slgsdselsg pgpyrqadry gfiggssaep gpghppadli
       61 rqremkwvem tshwektmsr rykkvkmqcr kgipsalrar cwpllcgahv cqknspgtyq
      121 elaeapgdpq wmetigrdlh rqfplhemfv spqghgqqgl lqvlkaytly rpeqgycqaq
      181 gpvaavllmh lppeeafwcl vqicevylpg yygphmeavr ldaevfmall rrllphvhkh
      241 lqqvgvgpll ylpewflclf arslpfptvl rvwdaflseg arvlfrvglt lvrlalgtae
      301 qrgacpglle tlgalraipp aqlqeeafms qvhsvvlser dlqreikaql aqlpdsapgp
      361 pprpqvrlag aqaifeaqql agvrrgakpe vprivvqppe eprpprrkpq trgktfhgll
      421 trargppieg pprpqrgsts fldtrf
//
LOCUS       NP_002203                245 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 6 isoform a [Homo
            sapiens].
ACCESSION   NP_002203
VERSION     NP_002203.1
DBSOURCE    REFSEQ: accession NM_002212.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Huang,C.G., Zhou,X.Q., Zheng,A.F., Luo,X., Shen,J., Xiao,Z.G.,
            Yang,Z.H. and Dai,Q.
  TITLE     eIF6 Promotes Gastric Cancer Proliferation and Invasion by
            Regulating Cell Cycle
  JOURNAL   Dig Dis Sci 69 (9), 3249-3260 (2024)
   PUBMED   38987443
  REMARK    GeneRIF: eIF6 Promotes Gastric Cancer Proliferation and Invasion by
            Regulating Cell Cycle.
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Yi,D., Zhang,D., Zeng,Z., Zhang,S., Song,B., He,C., Li,M. and He,J.
  TITLE     Circular RNA eukaryotic translation initiation factor 6 facilitates
            TPC-1 cell proliferation and invasion through the
            microRNA-138-5p/lipase H axis
  JOURNAL   Funct Integr Genomics 23 (4), 313 (2023)
   PUBMED   37776372
  REMARK    GeneRIF: Circular RNA eukaryotic translation initiation factor 6
            facilitates TPC-1 cell proliferation and invasion through the
            microRNA-138-5p/lipase H axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Elliff,J., Biswas,A., Roshan,P., Kuppa,S., Patterson,A.,
            Mattice,J., Chinnaraj,M., Burd,R., Walker,S.E., Pozzi,N.,
            Antony,E., Bothner,B. and Origanti,S.
  TITLE     Dynamic states of eIF6 and SDS variants modulate interactions with
            uL14 of the 60S ribosomal subunit
  JOURNAL   Nucleic Acids Res 51 (4), 1803-1822 (2023)
   PUBMED   36651285
  REMARK    GeneRIF: Dynamic states of eIF6 and SDS variants modulate
            interactions with uL14 of the 60S ribosomal subunit.
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Scagliola,A., Miluzio,A., Mori,G., Ricciardi,S., Oliveto,S.,
            Manfrini,N. and Biffo,S.
  TITLE     Inhibition of eIF6 Activity Reduces Hepatocellular Carcinoma
            Growth: An In Vivo and In Vitro Study
  JOURNAL   Int J Mol Sci 23 (14), 7720 (2022)
   PUBMED   35887068
  REMARK    GeneRIF: Inhibition of eIF6 Activity Reduces Hepatocellular
            Carcinoma Growth: An In Vivo and In Vitro Study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Keen,A.N., Payne,L.A., Mehta,V., Rice,A., Simpson,L.J., Pang,K.L.,
            Del Rio Hernandez,A., Reader,J.S. and Tzima,E.
  TITLE     Eukaryotic initiation factor 6 regulates mechanical responses in
            endothelial cells
  JOURNAL   J Cell Biol 221 (2) (2022)
   PUBMED   35024764
  REMARK    GeneRIF: Eukaryotic initiation factor 6 regulates mechanical
            responses in endothelial cells.
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Sanvito,F., Piatti,S., Villa,A., Bossi,M., Lucchini,G.,
            Marchisio,P.C. and Biffo,S.
  TITLE     The beta4 integrin interactor p27(BBP/eIF6) is an essential nuclear
            matrix protein involved in 60S ribosomal subunit assembly
  JOURNAL   J Cell Biol 144 (5), 823-837 (1999)
   PUBMED   10085284
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Sanvito,F., Arrigo,G., Zuffardi,O., Agnelli,M., Marchisio,P.C. and
            Biffo,S.
  TITLE     Localization of p27 beta4 binding protein gene (ITGB4BP) to human
            chromosome region 20q11.2
  JOURNAL   Genomics 52 (1), 111-112 (1998)
   PUBMED   9740680
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Si,K., Chaudhuri,J., Chevesich,J. and Maitra,U.
  TITLE     Molecular cloning and functional expression of a human cDNA
            encoding translation initiation factor 6
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14285-14290 (1997)
   PUBMED   9405604
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Biffo,S., Sanvito,F., Costa,S., Preve,L., Pignatelli,R.,
            Spinardi,L. and Marchisio,P.C.
  TITLE     Isolation of a novel beta4 integrin-binding protein (p27(BBP))
            highly expressed in epithelial cells
  JOURNAL   J Biol Chem 272 (48), 30314-30321 (1997)
   PUBMED   9374518
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC001119.2 and BM851166.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Hemidesmosomes are structures which link the basal lamina
            to the intermediate filament cytoskeleton. An important functional
            component of hemidesmosomes is the integrin beta-4 subunit (ITGB4),
            a protein containing two fibronectin type III domains. The protein
            encoded by this gene binds to the fibronectin type III domains of
            ITGB4 and may help link ITGB4 to the intermediate filament
            cytoskeleton. The encoded protein, which is insoluble and found
            both in the nucleus and in the cytoplasm, can function as a
            translation initiation factor and prevent the association of the
            40S and 60S ribosomal subunits. Multiple non-protein coding
            transcript variants and variants encoding two different isoforms
            have been found for this gene. [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a). Variants 1, 2, and 6 all encode isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.153922.1,
                                           SRR5189658.109685.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374450.8/ ENSP00000363574.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..245
                     /product="eukaryotic translation initiation factor 6
                     isoform a"
                     /EC_number="3.6.5.3"
                     /note="B4 integrin interactor; p27 beta-4 integrin-binding
                     protein; eukaryotic translation initiation factor 3A"
                     /calculated_mol_wt=26468
     Region          1..244
                     /region_name="PTZ00136"
                     /note="eukaryotic translation initiation factor 6-like
                     protein; Provisional"
                     /db_xref="CDD:185471"
     Site            order(2..4,203..207)
                     /site_type="other"
                     /note="'Velcro' closure"
                     /db_xref="CDD:238292"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P56537.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O55135,
                     ECO:0000255|HAMAP-Rule:MF_03132; propagated from
                     UniProtKB/Swiss-Prot (P56537.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55135,
                     ECO:0000255|HAMAP-Rule:MF_03132; propagated from
                     UniProtKB/Swiss-Prot (P56537.1)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03132,
                     ECO:0000269|PubMed:12917340, ECO:0000269|PubMed:21084295;
                     propagated from UniProtKB/Swiss-Prot (P56537.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03132,
                     ECO:0000269|PubMed:12917340, ECO:0000269|PubMed:21084295;
                     propagated from UniProtKB/Swiss-Prot (P56537.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03132,
                     ECO:0000269|PubMed:14654845; propagated from
                     UniProtKB/Swiss-Prot (P56537.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P56537.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P56537.1)"
     CDS             1..245
                     /gene="EIF6"
                     /gene_synonym="b(2)gcn; CAB; eIF-6; EIF3A; ITGB4BP;
                     p27(BBP); p27BBP"
                     /coded_by="NM_002212.4:53..790"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13249.1"
                     /db_xref="GeneID:3692"
                     /db_xref="HGNC:HGNC:6159"
                     /db_xref="MIM:602912"
ORIGIN      
        1 mavrasfenn ceigcfaklt ntyclvaigg senfysvfeg elsdtipvvh asiagcriig
       61 rmcvgnrhgl lvpnnttdqe lqhirnslpd tvqirrveer lsalgnvttc ndyvalvhpd
      121 ldreteeila dvlkvevfrq tvadqvlvgs ycvfsnqggl vhpktsiedq delssllqvp
      181 lvagtvnrgs eviaagmvvn dwcafcgldt tstelsvves vfklneaqps tiatsmrdsl
      241 idslt
//
LOCUS       NP_036419                778 aa            linear   PRI 27-APR-2025
DEFINITION  arf-GAP with coiled-coil, ANK repeat and PH domain-containing
            protein 2 [Homo sapiens].
ACCESSION   NP_036419
VERSION     NP_036419.3
DBSOURCE    REFSEQ: accession NM_012287.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Zhang,G., Liu,Z., Zhong,J. and Lin,L.
  TITLE     Circ-ACAP2 facilitates the progression of colorectal cancer through
            mediating miR-143-3p/FZD4 axis
  JOURNAL   Eur J Clin Invest 51 (12), e13607 (2021)
   PUBMED   34085707
  REMARK    GeneRIF: Circ-ACAP2 facilitates the progression of colorectal
            cancer through mediating miR-143-3p/FZD4 axis.
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Zhao,B., Song,X. and Guan,H.
  TITLE     CircACAP2 promotes breast cancer proliferation and metastasis by
            targeting miR-29a/b-3p-COL5A1 axis
  JOURNAL   Life Sci 244, 117179 (2020)
   PUBMED   31863774
  REMARK    GeneRIF: Elevated expression of circACAP2 in breast cancer tissues
            leads to malignant phenotype upon cancerous cells.
            CircACAP2-miR-29a/b-3p-COL5A1 axis leads to breast cancer
            tumorigenesis
REFERENCE   5  (residues 1 to 778)
  AUTHORS   Lin,L., Shi,Y., Wang,M., Wang,C., Zhu,J. and Zhang,R.
  TITLE     Rab35/ACAP2 and Rab35/RUSC2 Complex Structures Reveal Molecular
            Basis for Effector Recognition by Rab35 GTPase
  JOURNAL   Structure 27 (5), 729-740 (2019)
   PUBMED   30905672
  REMARK    GeneRIF: analysis of structural basis for effector recognition in
            Rab35/ACAP2 and Rab35/RUSC2 complexes
REFERENCE   6  (residues 1 to 778)
  AUTHORS   Cuthbert,E.J., Davis,K.K. and Casanova,J.E.
  TITLE     Substrate specificities and activities of AZAP family Arf GAPs in
            vivo
  JOURNAL   Am J Physiol Cell Physiol 294 (1), C263-C270 (2008)
   PUBMED   18003747
  REMARK    GeneRIF: ACAP2 has robust, constitutive Arf6 GAP activity in vivo,
            with little activity toward Arf1.
REFERENCE   7  (residues 1 to 778)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   8  (residues 1 to 778)
  AUTHORS   Jackson,T.R., Brown,F.D., Nie,Z., Miura,K., Foroni,L., Sun,J.,
            Hsu,V.W., Donaldson,J.G. and Randazzo,P.A.
  TITLE     ACAPs are arf6 GTPase-activating proteins that function in the cell
            periphery
  JOURNAL   J Cell Biol 151 (3), 627-638 (2000)
   PUBMED   11062263
REFERENCE   9  (residues 1 to 778)
  AUTHORS   Dowler,S., Currie,R.A., Campbell,D.G., Deak,M., Kular,G.,
            Downes,C.P. and Alessi,D.R.
  TITLE     Identification of pleckstrin-homology-domain-containing proteins
            with novel phosphoinositide-binding specificities
  JOURNAL   Biochem J 351 (Pt 1), 19-31 (2000)
   PUBMED   11001876
REFERENCE   10 (residues 1 to 778)
  AUTHORS   Jackson,T.R., Kearns,B.G. and Theibert,A.B.
  TITLE     Cytohesins and centaurins: mediators of PI 3-kinase-regulated Arf
            signaling
  JOURNAL   Trends Biochem Sci 25 (10), 489-495 (2000)
   PUBMED   11050434
  REMARK    GeneRIF: Centaurin beta2/KIAA0041, is a member of the centaurin
            family of ADP-ribosylation factor directed GTPase-activating
            proteins. Binding of phosphoinositides to a pleckstrin homology
            domain may regulate subcellular localisation and activity.
            Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB087306.1, D26069.3, AC090018.12, BC017120.1 and CA413842.1.
            
            On May 7, 2008 this sequence version replaced NP_036419.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D26069.3, BC060767.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326793.11/ ENSP00000324287.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..778
                     /product="arf-GAP with coiled-coil, ANK repeat and PH
                     domain-containing protein 2"
                     /note="Arf GAP with coiled coil, ANK repeat and PH domains
                     2; centaurin-beta-2"
                     /calculated_mol_wt=87898
     Region          18..217
                     /region_name="BAR_ACAP2"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with
                     Coiled-coil, ANK repeat and PH domain containing protein
                     2; cd07638"
                     /db_xref="CDD:153322"
     Site            order(27,30..31,35,37..38,41..42,44..45,55..56,58..59,
                     62..63,65..66,69,83,86..87,178,181..182,184,189,192..193,
                     195..196,199..200,203..204,206..207,210..211,213..214)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153322"
     Region          269..365
                     /region_name="PH_ACAP"
                     /note="ArfGAP with coiled-coil, ankyrin repeat and PH
                     domains Pleckstrin homology (PH) domain; cd13250"
                     /db_xref="CDD:270070"
     Region          371..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15057.3)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15057.3)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZQK5; propagated from
                     UniProtKB/Swiss-Prot (Q15057.3)"
     Region          399..513
                     /region_name="ArfGap_ACAP2"
                     /note="ArfGAP domain of ACAP2 (ArfGAP with Coiled-coil,
                     ANK repeat and PH domains 2); cd08851"
                     /db_xref="CDD:350076"
     Site            order(414,417,434,437,442)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350076"
     Site            order(414,417,434,437)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350076"
     Site            order(439,442..443,452,456..457,496)
                     /site_type="other"
                     /note="putative ANK repeat binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350076"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15057.3)"
     Region          540..599
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15057.3)"
     Site            581
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15057.3)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZQK5; propagated from
                     UniProtKB/Swiss-Prot (Q15057.3)"
     Region          <610..741
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(615..617,619..620,624,627,636,638,642,646..647,
                     650..652,654..655,659,662,671,673,675,679..680,683..685,
                     687..688,692,695,704)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          638..671
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          640..669
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15057.3)"
     Region          673..704
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          673..702
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15057.3)"
     Region          706..735
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15057.3)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q15057.3)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15057.3)"
     CDS             1..778
                     /gene="ACAP2"
                     /gene_synonym="CENTB2; CNT-B2"
                     /coded_by="NM_012287.6:174..2510"
                     /db_xref="CCDS:CCDS33924.1"
                     /db_xref="GeneID:23527"
                     /db_xref="HGNC:HGNC:16469"
                     /db_xref="MIM:607766"
ORIGIN      
        1 mkmtvdfeec lkdsprfraa leevegdvae lelkldklvk lciamidtgk afcvankqfm
       61 ngirdlaqys sndavvetsl tkfsdslqem infhtilfdq tqrsikaqlq nfvkedlrkf
      121 kdakkqfekv seekenalvk naqvqrnkqh eveeatnilt atrkcfrhia ldyvlqinvl
      181 qskrrseilk smlsfmyahl affhqgydlf selgpymkdl gaqldrlvvd aakekremeq
      241 khstiqqkdf ssddskleyn vdaangivme gylfkrasna fktwnrrwfs iqnnqlvyqk
      301 kfkdnptvvv edlrlctvkh cedierrfcf evvsptkscm lqadseklrq awikavqtsi
      361 atayrekgde sekldkkssp stgsldsgne skekllkges alqrvqcipg nasccdcgla
      421 dprwasinlg itlciecsgi hrslgvhfsk vrsltldtwe pellklmcel gndvinrvye
      481 anvekmgikk pqpgqrqeke ayirakyver kfvdkysisl sppeqqkkfv sksseekrls
      541 iskfgpgdqv rasaqssvrs ndsgiqqssd dgreslpstv sanslyepeg erqdssmfld
      601 skhlnpglql yrasyeknlp kmaealahga dvnwanseen katpliqavl ggslvtcefl
      661 lqnganvnqr dvqgrgplhh atvlghtgqv clflkrganq hatdeegkdp lsiaveaana
      721 divtllrlar mneemreseg lygqpgdety qdifrdfsqm asnnpeklnr fqqdsqkf
//
LOCUS       NP_004991                116 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
            isoform 1 [Homo sapiens].
ACCESSION   NP_004991
VERSION     NP_004991.1
DBSOURCE    REFSEQ: accession NM_005000.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Tensing,K., Pata,I., Wittig,I., Wehnert,M. and Metspalu,A.
  TITLE     Genomic organization of the human complex I 13-kDa subunit gene
            NDUFA5
  JOURNAL   Cytogenet Cell Genet 84 (1-2), 125-127 (1999)
   PUBMED   10343126
REFERENCE   7  (residues 1 to 116)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   8  (residues 1 to 116)
  AUTHORS   Emahazion,T., Beskow,A., Gyllensten,U. and Brookes,A.J.
  TITLE     Intron based radiation hybrid mapping of 15 complex I genes of the
            human electron transport chain
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 115-119 (1998)
   PUBMED   9763677
REFERENCE   9  (residues 1 to 116)
  AUTHORS   Pata,I., Tensing,K. and Metspalu,A.
  TITLE     A human cDNA encoding the homologue of NADH: ubiquinone
            oxidoreductase subunit B13
  JOURNAL   Biochim Biophys Acta 1350 (2), 115-118 (1997)
   PUBMED   9048877
REFERENCE   10 (residues 1 to 116)
  AUTHORS   Russell,M.W., du Manoir,S., Collins,F.S. and Brody,L.C.
  TITLE     Cloning of the human NADH: ubiquinone oxidoreductase subunit B13:
            localization to chromosome 7q32 and identification of a pseudogene
            on 11p15
  JOURNAL   Mamm Genome 8 (1), 60-61 (1997)
   PUBMED   9021153
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC000813.1, AC073323.5 and
            CR933664.1.
            
            Summary: This nuclear gene encodes a conserved protein that
            comprises the B13 subunit of complex I of the mitochondrial
            respiratory chain. The encoded protein localizes to the inner
            mitochondrial membrane, where it is thought to aid in the transfer
            of electrons from NADH to ubiquinone. Alternative splicing results
            in multiple transcript variants. There are numerous pseudogenes of
            this gene on chromosomes 1, 3, 6, 8, 9, 11, 12, and 16. [provided
            by RefSeq, Apr 2014].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.580536.1,
                                           SRR14038192.3596408.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188, SAMN03568911
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000355749.7/
                                                  ENSP00000347988.2
            RefSeq Select criteria             :: based on manual assertion,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.32"
     Protein         1..116
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 5 isoform 1"
                     /EC_number="7.1.1.2"
                     /EC_number="1.6.99.3"
                     /note="ubiquinone reductase; type I dehydrogenase; complex
                     I 13kDa subunit B; NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 5; complex I subunit B13;
                     NADH-ubiquinone oxidoreductase 13 kDa-B subunit; NADH
                     dehydrogenase (ubiquinone) 1 alpha subcomplex, 5, 13kDa"
                     /calculated_mol_wt=13328
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P23935; propagated from
                     UniProtKB/Swiss-Prot (Q16718.3)"
     Region          13..79
                     /region_name="ETC_C1_NDUFA5"
                     /note="ETC complex I subunit conserved region; pfam04716"
                     /db_xref="CDD:461407"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q16718.3)"
     Site            46
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CPP6; propagated from
                     UniProtKB/Swiss-Prot (Q16718.3)"
     Site            60
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q16718.3)"
     Site            98
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CPP6; propagated from
                     UniProtKB/Swiss-Prot (Q16718.3)"
     CDS             1..116
                     /gene="NDUFA5"
                     /gene_synonym="B13; CI-13kB; CI-13KD-B; NUFM; UQOR13"
                     /coded_by="NM_005000.5:24..374"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5788.1"
                     /db_xref="GeneID:4698"
                     /db_xref="HGNC:HGNC:7688"
                     /db_xref="MIM:601677"
ORIGIN      
        1 magvlkkttg lvglavcntp herlrilytk ildvleeipk naayrkyteq itneklamvk
       61 aepdvkkled qlqggqleev ilqaehelnl arkmrewklw eplveeppad qwkwpi
//
LOCUS       NP_065134                925 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear pore complex protein Nup107 isoform 1 [Homo sapiens].
ACCESSION   NP_065134
VERSION     NP_065134.1
DBSOURCE    REFSEQ: accession NM_020401.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Han,Y., Sha,H., Yang,Y., Yu,Z., Zhou,L., Wang,Y., Yang,F., Qiu,L.,
            Zhang,Y. and Zhou,J.
  TITLE     Mutations in the NUP93, NUP107 and NUP160 genes cause
            steroid-resistant nephrotic syndrome in Chinese children
  JOURNAL   Ital J Pediatr 50 (1), 81 (2024)
   PUBMED   38650033
  REMARK    GeneRIF: Mutations in the NUP93, NUP107 and NUP160 genes cause
            steroid-resistant nephrotic syndrome in Chinese children.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 925)
  AUTHORS   Braun,D.A., Lovric,S., Schapiro,D., Schneider,R., Marquez,J.,
            Asif,M., Hussain,M.S., Daga,A., Widmeier,E., Rao,J., Ashraf,S.,
            Tan,W., Lusk,C.P., Kolb,A., Jobst-Schwan,T., Schmidt,J.M.,
            Hoogstraten,C.A., Eddy,K., Kitzler,T.M., Shril,S., Moawia,A.,
            Schrage,K., Khayyat,A.I.A., Lawson,J.A., Gee,H.Y., Warejko,J.K.,
            Hermle,T., Majmundar,A.J., Hugo,H., Budde,B., Motameny,S.,
            Altmuller,J., Noegel,A.A., Fathy,H.M., Gale,D.P., Waseem,S.S.,
            Khan,A., Kerecuk,L., Hashmi,S., Mohebbi,N., Ettenger,R.,
            Serdaroglu,E., Alhasan,K.A., Hashem,M., Goncalves,S., Ariceta,G.,
            Ubetagoyena,M., Antonin,W., Baig,S.M., Alkuraya,F.S., Shen,Q.,
            Xu,H., Antignac,C., Lifton,R.P., Mane,S., Nurnberg,P., Khokha,M.K.
            and Hildebrandt,F.
  TITLE     Mutations in multiple components of the nuclear pore complex cause
            nephrotic syndrome
  JOURNAL   J Clin Invest 128 (10), 4313-4328 (2018)
   PUBMED   30179222
REFERENCE   5  (residues 1 to 925)
  AUTHORS   Ren,Y., Diao,F., Katari,S., Yatsenko,S., Jiang,H.,
            Wood-Trageser,M.A. and Rajkovic,A.
  TITLE     Functional study of a novel missense single-nucleotide variant of
            NUP107 in two daughters of Mexican origin with premature ovarian
            insufficiency
  JOURNAL   Mol Genet Genomic Med 6 (2), 276-281 (2018)
   PUBMED   29363275
  REMARK    GeneRIF: Whole exome sequencing identified a novel and rare
            missense variant in the NUP107 gene (c.1063C>T, p.R355C) in both
            sisters with HH.
REFERENCE   6  (residues 1 to 925)
  AUTHORS   Le Rouzic,E., Mousnier,A., Rustum,C., Stutz,F., Hallberg,E.,
            Dargemont,C. and Benichou,S.
  TITLE     Docking of HIV-1 Vpr to the nuclear envelope is mediated by the
            interaction with the nucleoporin hCG1
  JOURNAL   J Biol Chem 277 (47), 45091-45098 (2002)
   PUBMED   12228227
REFERENCE   7  (residues 1 to 925)
  AUTHORS   Vasu,S., Shah,S., Orjalo,A., Park,M., Fischer,W.H. and Forbes,D.J.
  TITLE     Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA
            export
  JOURNAL   J Cell Biol 155 (3), 339-354 (2001)
   PUBMED   11684705
REFERENCE   8  (residues 1 to 925)
  AUTHORS   Belgareh,N., Rabut,G., Bai,S.W., van Overbeek,M., Beaudouin,J.,
            Daigle,N., Zatsepina,O.V., Pasteau,F., Labas,V., Fromont-Racine,M.,
            Ellenberg,J. and Doye,V.
  TITLE     An evolutionarily conserved NPC subcomplex, which redistributes in
            part to kinetochores in mammalian cells
  JOURNAL   J Cell Biol 154 (6), 1147-1160 (2001)
   PUBMED   11564755
REFERENCE   9  (residues 1 to 925)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   10 (residues 1 to 925)
  AUTHORS   Bastos,R., Ribas de Pouplana,L., Enarson,M., Bodoor,K. and Burke,B.
  TITLE     Nup84, a novel nucleoporin that is associated with CAN/Nup214 on
            the cytoplasmic face of the nuclear pore complex
  JOURNAL   J Cell Biol 137 (5), 989-1000 (1997)
   PUBMED   9166401
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ295745.1, AC124890.8 and
            BE326877.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the nucleoporin family. The
            protein is localized to the nuclear rim and is an essential
            component of the nuclear pore complex (NPC). All molecules entering
            or leaving the nucleus either diffuse through or are actively
            transported by the NPC. Alternate transcriptional splice variants
            of this gene have been observed but have not been thoroughly
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.92806.1,
                                           SRR1803617.198004.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000229179.9/ ENSP00000229179.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..925
                     /product="nuclear pore complex protein Nup107 isoform 1"
                     /note="nuclear pore complex protein Nup107; nucleoporin
                     107kDa"
                     /calculated_mol_wt=106243
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P57740.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P57740.1)"
     Region          20..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P57740.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            60
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BH74;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            68
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BH74; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P57740.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P57740.1)"
     Region          209..908
                     /region_name="Nup84_Nup100"
                     /note="Nuclear pore protein 84 / 107; pfam04121"
                     /db_xref="CDD:461184"
     CDS             1..925
                     /gene="NUP107"
                     /gene_synonym="GAMOS7; NPHS11; NUP84; ODG6"
                     /coded_by="NM_020401.4:89..2866"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8985.1"
                     /db_xref="GeneID:57122"
                     /db_xref="HGNC:HGNC:29914"
                     /db_xref="MIM:607617"
ORIGIN      
        1 mdrsgfgeis spvireaevt rtarkqsaqk rvllqasqde nfgnttprnq viprtpssfr
       61 qpftptsrsl lrqpdiscil gtggksprlt qssgffgnls mvtnlddsnw aaafssqrsg
      121 lftntephsi tedvtisavm lreddpgeaa smsmfsdflq sflkhssstv fdlveeyeni
      181 cgsqvnilsk ivsratpglq kfsktasmlw llqqemvtwr llaslyrdri qsaleeesvf
      241 avtavnasek tvvealfqrd slvrqsqlvv dwlesiakde igefsdnief yaksvywent
      301 lhtlkqrqlt syvgsvrplv teldpdapir qkmplddldr edevrllkyl ftliragmte
      361 eaqrlckrcg qawraatleg wklyhdpnvn ggtelepveg npyrriwkis cwrmaedelf
      421 nryeraiyaa lsgnlkqllp vcdtwedtvw ayfrvmvdsl veqeiqtsva tldeteelpr
      481 eylganwtle kvfeelqatd kkrvleenqe hyhivqkfli lgdidglmde fskwlsksrn
      541 nlpghllrfm thlilffrtl glqtkeevsi evlktyiqll irekhtnlia fytchlpqdl
      601 avaqyalfle svtefeqrhh clelakeadl dvatitktvv enirkkdnge fshhdlapal
      661 dtgtteedrl kidvidwlvf dpaqraealk qgnaimrkfl askkheaake vfvkipqdsi
      721 aeiynqceeq gmesplpaed dnairehlci rayleahetf newfkhmnsv pqkpalipqp
      781 tftekvaheh kekkyemdfg iwkghldalt advkekmynv llfvdggwmv dvredakedh
      841 erthqmvllr klclpmlcfl lhtilhstgq yqeclqladm vsserhklyl vfskeelrkl
      901 lqklresslm lldqgldplg yeiql
//
LOCUS       NP_009197                374 aa            linear   PRI 27-APR-2025
DEFINITION  GPN-loop GTPase 1 isoform a [Homo sapiens].
ACCESSION   NP_009197
VERSION     NP_009197.3
DBSOURCE    REFSEQ: accession NM_007266.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Mendez-Hernandez,L.E., Robledo-Rivera,A.Y., Macias-Silva,M.,
            Calera,M.R. and Sanchez-Olea,R.
  TITLE     Gpn3 is polyubiquitinated on lysine 216 and degraded by the
            proteasome in the cell nucleus in a Gpn1-inhibitable manner
  JOURNAL   FEBS Lett 591 (22), 3757-3770 (2017)
   PUBMED   29029378
  REMARK    GeneRIF: Results show that Gpn1-inhibitable, nuclear
            polyubiquitination on lysine 216 regulates the half-life of Gpn3 by
            tagging it for proteasomal degradation.
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Reyes-Pardo,H., Barbosa-Camacho,A.A., Perez-Mejia,A.E.,
            Lara-Chacon,B., Salas-Estrada,L.A., Robledo-Rivera,A.Y.,
            Montero-Moran,G.M., Lara-Gonzalez,S., Calera,M.R. and
            Sanchez-Olea,R.
  TITLE     A nuclear export sequence in GPN-loop GTPase 1, an essential
            protein for nuclear targeting of RNA polymerase II, is necessary
            and sufficient for nuclear export
  JOURNAL   Biochim Biophys Acta 1823 (10), 1756-1766 (2012)
   PUBMED   22796641
  REMARK    GeneRIF: A highly active, evolutionarily conserved nuclear export
            sequences in XAB1/Gpn1, was identified.
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Carre,C. and Shiekhattar,R.
  TITLE     Human GTPases associate with RNA polymerase II to mediate its
            nuclear import
  JOURNAL   Mol Cell Biol 31 (19), 3953-3962 (2011)
   PUBMED   21768307
  REMARK    GeneRIF: Data show that GPN1/GPN3 define a new family of small
            GTPases that are specialized for the transport of RNA polymerase II
            into the nucleus.
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Kraja,A.T., Vaidya,D., Pankow,J.S., Goodarzi,M.O., Assimes,T.L.,
            Kullo,I.J., Sovio,U., Mathias,R.A., Sun,Y.V., Franceschini,N.,
            Absher,D., Li,G., Zhang,Q., Feitosa,M.F., Glazer,N.L.,
            Haritunians,T., Hartikainen,A.L., Knowles,J.W., North,K.E.,
            Iribarren,C., Kral,B., Yanek,L., O'Reilly,P.F., McCarthy,M.I.,
            Jaquish,C., Couper,D.J., Chakravarti,A., Psaty,B.M., Becker,L.C.,
            Province,M.A., Boerwinkle,E., Quertermous,T., Palotie,L.,
            Jarvelin,M.R., Becker,D.M., Kardia,S.L., Rotter,J.I., Chen,Y.D. and
            Borecki,I.B.
  TITLE     A bivariate genome-wide approach to metabolic syndrome: STAMPEED
            consortium
  JOURNAL   Diabetes 60 (4), 1329-1339 (2011)
   PUBMED   21386085
REFERENCE   8  (residues 1 to 374)
  AUTHORS   Forget,D., Lacombe,A.A., Cloutier,P., Al-Khoury,R., Bouchard,A.,
            Lavallee-Adam,M., Faubert,D., Jeronimo,C., Blanchette,M. and
            Coulombe,B.
  TITLE     The protein interaction network of the human transcription
            machinery reveals a role for the conserved GTPase RPAP4/GPN1 and
            microtubule assembly in nuclear import and biogenesis of RNA
            polymerase II
  JOURNAL   Mol Cell Proteomics 9 (12), 2827-2839 (2010)
   PUBMED   20855544
  REMARK    GeneRIF: RPAP4/GPN1 is a member of a newly discovered GTPase family
            that contains a highly conserved GPN loop motif that is essential,
            along with its GTP-binding motifs, for nuclear localization of
            POLR2A/RPB1 in a process that also requires microtubule assembly
REFERENCE   9  (residues 1 to 374)
  AUTHORS   Lembo,F., Pero,R., Angrisano,T., Vitiello,C., Iuliano,R.,
            Bruni,C.B. and Chiariotti,L.
  TITLE     MBDin, a novel MBD2-interacting protein, relieves MBD2 repression
            potential and reactivates transcription from methylated promoters
  JOURNAL   Mol Cell Biol 23 (5), 1656-1665 (2003)
   PUBMED   12588985
  REMARK    GeneRIF: relieves MBD2-mediated transcriptional repression and
            reactivates transcription from methylated promoters
REFERENCE   10 (residues 1 to 374)
  AUTHORS   Nitta,M., Saijo,M., Kodo,N., Matsuda,T., Nakatsu,Y., Tamai,H. and
            Tanaka,K.
  TITLE     A novel cytoplasmic GTPase XAB1 interacts with DNA repair protein
            XPA
  JOURNAL   Nucleic Acids Res 28 (21), 4212-4218 (2000)
   PUBMED   11058119
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK298866.1, BC007451.2,
            AJ010842.1 and AC074091.6.
            
            On Aug 31, 2018 this sequence version replaced NP_009197.2.
            
            Summary: This gene encodes a guanosine triphosphatase enzyme. The
            encoded protein may play a role in DNA repair and may function in
            activation of transcription. Alternatively spliced transcript
            variants have been described. [provided by RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.128275.1,
                                           SRR1803614.247358.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000610189.2/ ENSP00000476446.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..374
                     /product="GPN-loop GTPase 1 isoform a"
                     /note="MBD2-interacting protein; ATP(GTP)-binding protein;
                     XPA binding protein 1, GTPase; RNA polymerase II
                     associated protein 4; RNAPII-associated protein 4"
                     /calculated_mol_wt=41609
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9HCN4.1)"
     Region          20..259
                     /region_name="GPN1"
                     /note="GPN-loop GTPase 1; cd17870"
                     /db_xref="CDD:349779"
     Site            order(27..34,189..190,192..193,244..246)
                     /site_type="active"
                     /db_xref="CDD:349779"
     Region          86..88
                     /region_name="Gly-Pro-Asn (GPN)-loop, involved in dimer
                     interface. /evidence=ECO:0000250|UniProtKB:Q9UYR9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCN4.1)"
     Site            88
                     /site_type="other"
                     /note="Stabilizes the phosphate intermediate, shared with
                     dimeric partner. /evidence=ECO:0000250|UniProtKB:Q9UYR9;
                     propagated from UniProtKB/Swiss-Prot (Q9HCN4.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCN4.1)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9HCN4.1)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCN4.1)"
     Region          326..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCN4.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9HCN4.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9HCN4.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9HCN4.1)"
     CDS             1..374
                     /gene="GPN1"
                     /gene_synonym="ATPBD1A; MBDIN; NTPBP; RPAP4; XAB1"
                     /coded_by="NM_007266.4:10..1134"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1760.3"
                     /db_xref="GeneID:11321"
                     /db_xref="HGNC:HGNC:17030"
                     /db_xref="MIM:611479"
ORIGIN      
        1 maasaaaael qasggprhpv cllvlgmags gkttfvqrlt ghlhaqgtpp yvinldpavh
       61 evpfpanidi rdtvkykevm kqyglgpngg ivtslnlfat rfdqvmkfie kaqnmskyvl
      121 idtpgqievf twsasgtiit ealassfptv viyvmdtsrs tnpvtfmsnm lyacsilykt
      181 klpfivvmnk tdiidhsfav ewmqdfeafq dalnqettyv snltrsmslv ldefysslrv
      241 vgvsavlgtg ldelfvqvts aaeeyereyr peyerlkksl anaesqqqre qlerlrkdmg
      301 svaldagtak dslspvlhps dliltrgtld eedeeadsdt ddidhrvtee sheepafqnf
      361 mqesmaqywk rnnk
//
LOCUS       NP_060873                582 aa            linear   PRI 27-APR-2025
DEFINITION  mRNA-decapping enzyme 1A isoform a [Homo sapiens].
ACCESSION   NP_060873
VERSION     NP_060873.4
DBSOURCE    REFSEQ: accession NM_018403.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Wu,H., Zhang,J., Bai,Y., Zhang,S., Zhang,Z., Tong,W., Han,P.,
            Fu,B., Zhang,Y. and Shen,Z.
  TITLE     DCP1A is an unfavorable prognostic-related enhancer RNA in
            hepatocellular carcinoma
  JOURNAL   Aging (Albany NY) 13 (19), 23020-23035 (2021)
   PUBMED   34609335
  REMARK    GeneRIF: DCP1A is an unfavorable prognostic-related enhancer RNA in
            hepatocellular carcinoma.
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Leonard,D., Ajuh,P., Lamond,A.I. and Legerski,R.J.
  TITLE     hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA
            splicing
  JOURNAL   Biochem Biophys Res Commun 308 (4), 793-801 (2003)
   PUBMED   12927788
REFERENCE   7  (residues 1 to 582)
  AUTHORS   Ingelfinger,D., Arndt-Jovin,D.J., Luhrmann,R. and Achsel,T.
  TITLE     The human LSm1-7 proteins colocalize with the mRNA-degrading
            enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
  JOURNAL   RNA 8 (12), 1489-1501 (2002)
   PUBMED   12515382
REFERENCE   8  (residues 1 to 582)
  AUTHORS   Lykke-Andersen,J.
  TITLE     Identification of a human decapping complex associated with hUpf
            proteins in nonsense-mediated decay
  JOURNAL   Mol Cell Biol 22 (23), 8114-8121 (2002)
   PUBMED   12417715
  REMARK    GeneRIF: These data suggest that a human decapping complex
            containing decapping enzymes hDcp1a and hDcp2 may be recruited to
            mRNAs containing premature termination codons by the hUpf proteins.
REFERENCE   9  (residues 1 to 582)
  AUTHORS   Callebaut,I.
  TITLE     An EVH1/WH1 domain as a key actor in TGFbeta signalling
  JOURNAL   FEBS Lett 519 (1-3), 178-180 (2002)
   PUBMED   12023040
REFERENCE   10 (residues 1 to 582)
  AUTHORS   Bai,R.Y., Koester,C., Ouyang,T., Hahn,S.A., Hammerschmidt,M.,
            Peschel,C. and Duyster,J.
  TITLE     SMIF, a Smad4-interacting protein that functions as a co-activator
            in TGFbeta signalling
  JOURNAL   Nat Cell Biol 4 (3), 181-190 (2002)
   PUBMED   11836524
  REMARK    GeneRIF: Overexpression of wild-type SMIF enhanced expression of
            TGFbeta/BMP regulated genes, whereas a dominant-negative SMIF
            mutant suppressed expression.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY146651.1, AC112218.2 and
            CD676826.1.
            
            On Mar 23, 2010 this sequence version replaced NP_060873.3.
            
            Summary: Decapping is a key step in general and regulated mRNA
            decay. The protein encoded by this gene is a decapping enzyme. This
            protein and another decapping enzyme form a decapping complex,
            which interacts with the nonsense-mediated decay factor hUpf1 and
            may be recruited to mRNAs containing premature termination codons.
            This protein also participates in the TGF-beta signaling pathway.
            Alternative splicing of this gene results in multiple transcript
            variants. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB075507.1, SRR1803612.205466.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000610213.6/ ENSP00000476386.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.1"
     Protein         1..582
                     /product="mRNA-decapping enzyme 1A isoform a"
                     /EC_number="3.6.1.62"
                     /note="transcription factor SMIF; Smad4-interacting
                     transcriptional co-activator; mRNA-decapping enzyme 1A;
                     decapping enzyme hDcp1a; putative protein product of
                     Nbla00360; DCP1 decapping enzyme homolog A; DCP1 decapping
                     enzyme-like protein A"
                     /calculated_mol_wt=63148
     Region          6..126
                     /region_name="Dcp1"
                     /note="mRNA decapping enzyme 1 (Dcp1); cd09804"
                     /db_xref="CDD:197362"
     Site            order(7..8,12,14..15,18..19,29,31,53,70..72,75,77)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:197362"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Region          132..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Region          172..214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YD3; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Region          <268..532
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            376
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Region          513..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q91YD3; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NPI6.3)"
     Region          539..581
                     /region_name="mRNA_decap_C"
                     /note="mRNA-decapping enzyme C-terminus; pfam16741"
                     /db_xref="CDD:465253"
     CDS             1..582
                     /gene="DCP1A"
                     /gene_synonym="HSA275986; Nbla00360; SMAD4IP1; SMIF"
                     /coded_by="NM_018403.7:27..1775"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46847.2"
                     /db_xref="GeneID:55802"
                     /db_xref="HGNC:HGNC:18714"
                     /db_xref="MIM:607010"
ORIGIN      
        1 mealsragqe mslaalkqhd pyitsiadlt gqvalytfcp kanqwektdi egtlfvyrrs
       61 aspyhgftiv nrlnmhnlve pvnkdlefql hepfllyrna slsiysiwfy dkndchriak
      121 lmadvveeet rrsqqaardk qspsqangcs dhrpidilem lsrakdeyer nqmgdsniss
      181 pglqpstqls nlgstetlee mpsgsqdksa psghkhltve elfgtslpke qpavvgldse
      241 emerlpgdas qkepnsflpf pfeqlggapq setlgvpsaa hhsvqpeitt pvlitpasit
      301 qsnekhapty tiplspvlsp tlpaeaptaq vppslprnst mmqavkttpr qrspllnqpv
      361 pelshaslia nqspfrapln vtntagtslp svdllqklrl tpqhdqiqtq plgkgamvas
      421 fspaagqlat pesfieppsk taaarvaasa slsnmvlapl qsmqqnqdpe vfvqpkvlss
      481 aipvagaplv tatttavssv llapsvfqqt vtrssdlerk asspspltig tpesqrkpsi
      541 ilsksqlqdt lihlikndss flstlhevyl qvltknkdnh nl
//
LOCUS       NP_009168                867 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear body protein SP140 isoform 1 [Homo sapiens].
ACCESSION   NP_009168
VERSION     NP_009168.4
DBSOURCE    REFSEQ: accession NM_007237.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 867)
  AUTHORS   Nakamura,H., Hikichi,H., Seto,S., Hijikata,M. and Keicho,N.
  TITLE     Transcriptional regulators SP110 and SP140 modulate inflammatory
            response genes in Mycobacterium tuberculosis-infected human
            macrophages
  JOURNAL   Microbiol Spectr 12 (10), e0010124 (2024)
   PUBMED   39162523
  REMARK    GeneRIF: Transcriptional regulators SP110 and SP140 modulate
            inflammatory response genes in Mycobacterium tuberculosis-infected
            human macrophages.
REFERENCE   2  (residues 1 to 867)
  AUTHORS   Tanagala,K.K.K., Morin-Baxter,J., Carvajal,R., Cheema,M., Dubey,S.,
            Nakagawa,H., Yoon,A., Cheng,Y.L., Taylor,A., Nickerson,J., Mintz,A.
            and Momen-Heravi,F.
  TITLE     SP140 inhibits STAT1 signaling, induces IFN-gamma in
            tumor-associated macrophages, and is a predictive biomarker of
            immunotherapy response
  JOURNAL   J Immunother Cancer 10 (12) (2022)
   PUBMED   36600652
  REMARK    GeneRIF: SP140 inhibits STAT1 signaling, induces IFN-gamma in
            tumor-associated macrophages, and is a predictive biomarker of
            immunotherapy response.
REFERENCE   3  (residues 1 to 867)
  AUTHORS   Fraschilla,I., Amatullah,H., Rahman,R.U. and Jeffrey,K.L.
  TITLE     Immune chromatin reader SP140 regulates microbiota and risk for
            inflammatory bowel disease
  JOURNAL   Cell Host Microbe 30 (10), 1370-1381 (2022)
   PUBMED   36130593
  REMARK    GeneRIF: Immune chromatin reader SP140 regulates microbiota and
            risk for inflammatory bowel disease.
REFERENCE   4  (residues 1 to 867)
  AUTHORS   Amatullah,H., Fraschilla,I., Digumarthi,S., Huang,J.,
            Adiliaghdam,F., Bonilla,G., Wong,L.P., Rivard,M.E., Beauchamp,C.,
            Mercier,V., Goyette,P., Sadreyev,R.I., Anthony,R.M., Rioux,J.D. and
            Jeffrey,K.L.
  TITLE     Epigenetic reader SP140 loss of function drives Crohn's disease due
            to uncontrolled macrophage topoisomerases
  JOURNAL   Cell 185 (17), 3232-3247 (2022)
   PUBMED   35952671
  REMARK    GeneRIF: Epigenetic reader SP140 loss of function drives Crohn's
            disease due to uncontrolled macrophage topoisomerases.
REFERENCE   5  (residues 1 to 867)
  AUTHORS   Zucchelli,C., Tamburri,S., Quilici,G., Palagano,E., Berardi,A.,
            Saare,M., Peterson,P., Bachi,A. and Musco,G.
  TITLE     Structure of human Sp140 PHD finger: an atypical fold interacting
            with Pin1
  JOURNAL   FEBS J 281 (1), 216-231 (2014)
   PUBMED   24267382
REFERENCE   6  (residues 1 to 867)
  AUTHORS   Granito,A., Yang,W.H., Muratori,L., Lim,M.J., Nakajima,A.,
            Ferri,S., Pappas,G., Quarneti,C., Bianchi,F.B., Bloch,D.B. and
            Muratori,P.
  TITLE     PML nuclear body component Sp140 is a novel autoantigen in primary
            biliary cirrhosis
  JOURNAL   Am J Gastroenterol 105 (1), 125-131 (2010)
   PUBMED   19861957
REFERENCE   7  (residues 1 to 867)
  AUTHORS   Di Bernardo,M.C., Crowther-Swanepoel,D., Broderick,P., Webb,E.,
            Sellick,G., Wild,R., Sullivan,K., Vijayakrishnan,J., Wang,Y.,
            Pittman,A.M., Sunter,N.J., Hall,A.G., Dyer,M.J., Matutes,E.,
            Dearden,C., Mainou-Fowler,T., Jackson,G.H., Summerfield,G.,
            Harris,R.J., Pettitt,A.R., Hillmen,P., Allsup,D.J., Bailey,J.R.,
            Pratt,G., Pepper,C., Fegan,C., Allan,J.M., Catovsky,D. and
            Houlston,R.S.
  TITLE     A genome-wide association study identifies six susceptibility loci
            for chronic lymphocytic leukemia
  JOURNAL   Nat Genet 40 (10), 1204-1210 (2008)
   PUBMED   18758461
REFERENCE   8  (residues 1 to 867)
  AUTHORS   Madani,N., Millette,R., Platt,E.J., Marin,M., Kozak,S.L.,
            Bloch,D.B. and Kabat,D.
  TITLE     Implication of the lymphocyte-specific nuclear body protein Sp140
            in an innate response to human immunodeficiency virus type 1
  JOURNAL   J Virol 76 (21), 11133-11138 (2002)
   PUBMED   12368356
  REMARK    GeneRIF: the nuclear body protein Sp140, was found specifically in
            all NP cells (n = 12 cell lines tested; P < or = 0.001), and HIV-1
            infection induced its partial dispersal from nuclear bodies into
            cytosolic colocalization with Vif
REFERENCE   9  (residues 1 to 867)
  AUTHORS   Bloch,D.B., de la Monte,S.M., Guigaouri,P., Filippov,A. and
            Bloch,K.D.
  TITLE     Identification and characterization of a leukocyte-specific
            component of the nuclear body
  JOURNAL   J Biol Chem 271 (46), 29198-29204 (1996)
   PUBMED   8910577
REFERENCE   10 (residues 1 to 867)
  AUTHORS   Dent,A.L., Yewdell,J., Puvion-Dutilleul,F., Koken,M.H., de The,H.
            and Staudt,L.M.
  TITLE     LYSP100-associated nuclear domains (LANDs): description of a new
            class of subnuclear structures and their relationship to PML
            nuclear bodies
  JOURNAL   Blood 88 (4), 1423-1426 (1996)
   PUBMED   8695863
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301267.1, BC038091.1,
            BC105960.1, U36500.1 and AC009949.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 12, 2008 this sequence version replaced NP_009168.3.
            
            Summary: This gene encodes a member of the SP100 family of
            proteins, which are share common domains including an N-terminal
            homogeneously staining region domain followed by a SP100/autoimmune
            regulator/NucP41/P75/deformed epidermal autoregulatory factor
            domain, a plant homeobox zinc finger, and a bromodomain. The
            encoded protein is interferon-inducible and is expressed at high
            levels in the nuclei of leukocytes. Variants of this gene have been
            associated with multiple sclerosis, Crohn's disease, and chronic
            lymphocytic leukemia. Alternative splicing results in multiple
            variants. [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The extent of this RefSeq
            transcript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U36500.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392045.8/ ENSP00000375899.3
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..867
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..867
                     /product="nuclear body protein SP140 isoform 1"
                     /note="lymphoid-specific SP100 homolog; speckled 140 kDa;
                     nuclear autoantigen Sp-140; lymphoid-restricted homolog of
                     Sp100"
                     /calculated_mol_wt=98093
     Region          38..136
                     /region_name="HSR"
                     /note="HSR domain; pfam03172"
                     /db_xref="CDD:460835"
     Region          260..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13342.2)"
     Region          268..>479
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     Region          365..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13342.2)"
     Region          486..580
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13342.2)"
     Region          495..514
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13342.2)"
     Region          584..660
                     /region_name="SAND"
                     /note="SAND domain; pfam01342"
                     /db_xref="CDD:460167"
     Region          692..733
                     /region_name="PHD_SP110_140"
                     /note="PHD finger found in the Sp100/Sp140 family of
                     nuclear body components; cd15626"
                     /db_xref="CDD:277096"
     Site            order(692,697..698,701..706,713)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:277096"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24267382; propagated from
                     UniProtKB/Swiss-Prot (Q13342.2)"
     Region          757..860
                     /region_name="Bromo_SP100C_like"
                     /note="Bromodomain, SP100C_like subfamily. The SP100C
                     protein is a splice variant of SP100, a major component of
                     PML-SP100 nuclear bodies (NBs), which are poorly
                     understood. It is covalently modified by SUMO-1 and may
                     play a role in processes at the chromatin...; cd05501"
                     /db_xref="CDD:99933"
     Site            order(783,788,791,830,834,839)
                     /site_type="other"
                     /note="putative acetyllysine binding site [chemical
                     binding]"
                     /db_xref="CDD:99933"
     CDS             1..867
                     /gene="SP140"
                     /gene_synonym="LYSP100; LYSP100-A; LYSP100-B"
                     /coded_by="NM_007237.5:110..2713"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42831.1"
                     /db_xref="GeneID:11262"
                     /db_xref="HGNC:HGNC:17133"
                     /db_xref="MIM:608602"
ORIGIN      
        1 maqqgqqgqm asgdsnlnfr mvaeiqnveg qnlqeqvcpe pifrffrenk veiasaitrp
       61 fpflmglrdr sfiseqmyeh fqeafrnlvp vtrvmycvls elektfgwsh lealfsrinl
      121 maypdlneiy rsfqnvcyeh splqmnnvnd ledrprllpy gkqensnach emddiavpqe
      181 alsssprcep gfssesceql alpkagggda edapsllpgg gvscklaiqi degeseempk
      241 llpydtevle sngmidaart ystapgekqg eeegrnsprk rnqdkekyqe spegrdketf
      301 dlktpqvtne gepekglcll pgegeegsdd csemcdgeep qeassslarc gsvsclsaet
      361 fdlktpqvtn egepekelsl lpgegeegsd dcsemcdgee rqeassslar rgsvsselen
      421 hpmneegese elassllydn vpgaeqsaye nekcscvmcf seevpgspea rtesdqacgt
      481 mdtvdianns tlgkpkrkrr kkrghgwsrm rmrrqensqq ndnskadgqv vssekkanvn
      541 lkdlskirgr krgkpgtrft qsdraaqkrv rsrasrkhkd etvdfkapll pvtcggvkgi
      601 lhkkklqqgi lvkciqtedg kwftptefei kggharsknw rlsvrcggwp lrwlmengfl
      661 pdppriryrk kkrilksqnn ssvdpcmrnl decevcrdgg elfccdtcsr vfhedchipp
      721 veaertpwnc ifcrmkespg sqqccqesev lerqmcpeeq lkceflllkv yccsessffa
      781 kipyyyyire acqglkepmw ldkikkrlne hgypqvegfv qdmrlifqnh rasykykdfg
      841 qmgfrleaef eknfkevfai qetngnn
//
LOCUS       NP_001356107             758 aa            linear   ROD 27-APR-2025
DEFINITION  endothelin-converting enzyme 1 isoform b [Mus musculus].
ACCESSION   NP_001356107
VERSION     NP_001356107.1
DBSOURCE    REFSEQ: accession NM_001369178.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Chen,L., Lu,Y., Zhao,M., Xu,J., Wang,Y., Xu,Q., Cao,Y. and Liu,H.
  TITLE     A non-canonical role of endothelin converting enzyme 1 (ECE1) in
            promoting lung cancer development via directly targeting protein
            kinase B (AKT)
  JOURNAL   J Gene Med 26 (1), e3612 (2024)
   PUBMED   37897251
  REMARK    GeneRIF: A non-canonical role of endothelin converting enzyme 1
            (ECE1) in promoting lung cancer development via directly targeting
            protein kinase B (AKT).
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Eckman,E.A., Clausen,D.M., Sole-Domenech,S., Lee,C.W.,
            Sinobas-Pereira,C., Domalewski,R.J., Nichols,M.R. and
            Pacheco-Quinto,J.
  TITLE     Nascent Abeta42 Fibrillization in Synaptic Endosomes Precedes
            Plaque Formation in a Mouse Model of Alzheimer's-like
            beta-Amyloidosis
  JOURNAL   J Neurosci 43 (50), 8812-8824 (2023)
   PUBMED   37884349
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Ahuja,N., Hiltabidle,M.S., Rajasekhar,H., Voss,S., Lu,S.Z.,
            Barlow,H.R., Cowdin,M.A., Daniel,E., Vaddaraju,V., Anandakumar,T.,
            Black,E., Cleaver,O. and Maynard,C.
  TITLE     Endothelial Cyp26b1 restrains murine heart valve growth during
            development
  JOURNAL   Dev Biol 486, 81-95 (2022)
   PUBMED   35364055
REFERENCE   4  (residues 1 to 758)
  AUTHORS   Arfian,N., Suzuki,Y., Hartopo,A.B., Anggorowati,N.,
            Nugrahaningsih,D.A.A. and Emoto,N.
  TITLE     Endothelin converting enzyme-1 (ECE-1) deletion in association with
            Endothelin-1 downregulation ameliorates kidney fibrosis in mice
  JOURNAL   Life Sci 258, 118223 (2020)
   PUBMED   32768584
  REMARK    GeneRIF: Endothelin converting enzyme-1 (ECE-1) deletion in
            association with Endothelin-1 downregulation ameliorates kidney
            fibrosis in mice.
REFERENCE   5  (residues 1 to 758)
  AUTHORS   Poltavski,D.M., Colombier,P., Hu,J., Duron,A., Black,B.L. and
            Makita,T.
  TITLE     Venous endothelin modulates responsiveness of cardiac sympathetic
            axons to arterial semaphorin
  JOURNAL   Elife 8, e42528 (2019)
   PUBMED   30735130
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 758)
  AUTHORS   Kuwaki,T., Ling,G.Y., Onodera,M., Ishii,T., Nakamura,A., Ju,K.H.,
            Cao,W.H., Kumada,M., Kurihara,H., Kurihara,Y., Yazaki,Y.,
            Ohuchi,T., Yanagisawa,M. and Fukuda,Y.
  TITLE     Endothelin in the central control of cardiovascular and respiratory
            functions
  JOURNAL   Clin Exp Pharmacol Physiol 26 (12), 989-994 (1999)
   PUBMED   10626068
  REMARK    Review article
REFERENCE   7  (residues 1 to 758)
  AUTHORS   Yanagisawa,H., Hammer,R.E., Richardson,J.A., Williams,S.C.,
            Clouthier,D.E. and Yanagisawa,M.
  TITLE     Role of Endothelin-1/Endothelin-A receptor-mediated signaling
            pathway in the aortic arch patterning in mice
  JOURNAL   J Clin Invest 102 (1), 22-33 (1998)
   PUBMED   9649553
REFERENCE   8  (residues 1 to 758)
  AUTHORS   Yanagisawa,H., Yanagisawa,M., Kapur,R.P., Richardson,J.A.,
            Williams,S.C., Clouthier,D.E., de Wit,D., Emoto,N. and Hammer,R.E.
  TITLE     Dual genetic pathways of endothelin-mediated intercellular
            signaling revealed by targeted disruption of endothelin converting
            enzyme-1 gene
  JOURNAL   Development 125 (5), 825-836 (1998)
   PUBMED   9449665
REFERENCE   9  (residues 1 to 758)
  AUTHORS   Hanania,E.G., Au,W.W., Ullrich,R.L. and Papaconstantinou,J.
  TITLE     Regulation of retinoblastoma gene expression in a mouse mammary
            tumor model
  JOURNAL   Cancer Gene Ther 2 (4), 251-261 (1995)
   PUBMED   8548579
REFERENCE   10 (residues 1 to 758)
  AUTHORS   Xu,D., Emoto,N., Giaid,A., Slaughter,C., Kaw,S., deWit,D. and
            Yanagisawa,M.
  TITLE     ECE-1: a membrane-bound metalloprotease that catalyzes the
            proteolytic activation of big endothelin-1
  JOURNAL   Cell 78 (3), 473-485 (1994)
   PUBMED   8062389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK163790.1 and AL807764.9.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK163790.1, SRR7974084.23047.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 70.02 cM"
     Protein         1..758
                     /product="endothelin-converting enzyme 1 isoform b"
                     /EC_number="3.4.24.71"
                     /note="endothelin-converting enzyme-1b;
                     endothelin-converting enzyme-1d; endothelin-converting
                     enzyme-1a; endothelin-converting enzyme-1c1"
                     /calculated_mol_wt=85670
     Region          107..756
                     /region_name="M13"
                     /note="Peptidase family M13 includes neprilysin and
                     endothelin-converting enzyme I; cd08662"
                     /db_xref="CDD:341056"
     Site            order(137,548,553..556,575,591..592,595..596,599,655,698,
                     701..702,719..720,726)
                     /site_type="active"
                     /db_xref="CDD:341056"
     CDS             1..758
                     /gene="Ece1"
                     /gene_synonym="ECE-1; ECE-1a; ECE-1b; ECE-1c1; ECE-1d"
                     /coded_by="NM_001369178.1:127..2403"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:230857"
                     /db_xref="MGI:MGI:1101357"
ORIGIN      
        1 mppqslglqr gsfflgkrgp glmvslplla sslqvnfrss rsgqrcwaar tsvekrlvvl
       61 vtllaaglva claalgiqyq trtppvclte acvsvtssil nsmdptvdpc qdffsyacgg
      121 wikanpvpdg hsrwgtfsnl wehnqavikh llenatasvs eaerkaqvyy racmnetrie
      181 elrakplmel ieklggwnit gpwakdnfqd tlqvvtahyr tspffsvyvs adsknsnsnv
      241 iqvdqsglgl psrdyylnkt enekvltgyl nymvqlgkll gggdedairp qmqqildfet
      301 alanitipqe krrdeeliyh kvtaaelqtl apainwlpfl ntifypvein esepivvydk
      361 eylrqvstli nntdkcllnn ymmwnlvrkt ssfldqrfqd adekfmevmy gtkktciprw
      421 kfcvsdtenn lgfalgpmfv katfaedskn iaseiimeik kafeeslstl kwmdeetrrs
      481 akekadaiyn migypnfimd pkeldkvfnd ytavpdlyfe namrffnfsw rvtadqlrka
      541 pnrdqwsmtp pmvnayyspt kneivfpagi lqapfytrss pnalnfggig vvvgheltha
      601 fddqgreydk dgnlrpwwkn ssveafkqqt ecmvqqysny svngepvngr htlgeniadn
      661 gglkaayray qnwvkkngae qtlptlglts nqlfflgfaq vwcsvrtpes sheglitdph
      721 spsrfrvigs lsnskefseh frcppgspmn phhkcevw
//
LOCUS       NP_005630                422 aa            linear   PRI 27-APR-2025
DEFINITION  synaptotagmin-1 isoform 1 [Homo sapiens].
ACCESSION   NP_005630
VERSION     NP_005630.1
DBSOURCE    REFSEQ: accession NM_005639.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Stephan,G., Haddock,S., Wang,S., Erdjument-Bromage,H., Liu,W.,
            Ravn-Boess,N., Frenster,J.D., Bready,D., Cai,J., Ronnen,R.,
            Sabio-Ortiz,J., Fenyo,D., Neubert,T.A. and Placantonakis,D.G.
  TITLE     Modulation of GPR133 (ADGRD1) signaling by its intracellular
            interaction partner extended synaptotagmin 1
  JOURNAL   Cell Rep 43 (5), 114229 (2024)
   PUBMED   38758649
  REMARK    GeneRIF: Modulation of GPR133 (ADGRD1) signaling by its
            intracellular interaction partner extended synaptotagmin 1.
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Zhang,J., Ren,G., Huang,T., Sang,Y., Zhong,Y. and Yi,Y.
  TITLE     miRNA-363-3p Hinders Proliferation, Migration, Invasion and
            Autophagy of Thyroid Cancer Cells by Controlling SYT1 Transcription
            to affect NF-kappaB
  JOURNAL   Endocr Metab Immune Disord Drug Targets 24 (1), 153-162 (2024)
   PUBMED   37150983
  REMARK    GeneRIF: miRNA-363-3p Hinders Proliferation, Migration, Invasion
            and Autophagy of Thyroid Cancer Cells by Controlling SYT1
            Transcription to affect NF-kappaB.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Yamada,K., Motohashi,S., Oikawa,T., Tago,N., Koizumi,R., Ono,M.,
            Tachibana,T., Yoshida,A., Yoshida,S., Shimoda,M., Oka,M., Yoneda,Y.
            and Yoshida,K.
  TITLE     Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B+ vesicle pathway in liver cancer
  JOURNAL   Proc Natl Acad Sci U S A 119 (36), e2202730119 (2022)
   PUBMED   36044553
  REMARK    GeneRIF: Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B(+) vesicle pathway in liver cancer.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Thibord,F., Chan,M.V., Chen,M.H. and Johnson,A.D.
  TITLE     A year of COVID-19 GWAS results from the GRASP portal reveals
            potential genetic risk factors
  JOURNAL   HGG Adv 3 (2), 100095 (2022)
   PUBMED   35224516
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Melland,H., Bumbak,F., Kolesnik-Taylor,A., Ng-Cordell,E., John,A.,
            Constantinou,P., Joss,S., Larsen,M., Fagerberg,C., Laulund,L.W.,
            Thies,J., Emslie,F., Willemsen,M., Kleefstra,T., Pfundt,R.,
            Barrick,R., Chang,R., Loong,L., Alfadhel,M., van der Smagt,J.,
            Nizon,M., Kurian,M.A., Scott,D.J., Ziarek,J.J., Gordon,S.L. and
            Baker,K.
  TITLE     Expanding the genotype and phenotype spectrum of SYT1-associated
            neurodevelopmental disorder
  JOURNAL   Genet Med 24 (4), 880-893 (2022)
   PUBMED   35101335
  REMARK    GeneRIF: Expanding the genotype and phenotype spectrum of
            SYT1-associated neurodevelopmental disorder.
REFERENCE   6  (residues 1 to 422)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Chowdhury,D., Travis,G.H., Sutcliffe,J.G. and Burton,F.H.
  TITLE     Synaptotagmin I and 1B4 are identical: implications for
            synaptotagmin distribution in the primate brain
  JOURNAL   Neurosci Lett 190 (1), 9-12 (1995)
   PUBMED   7624059
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Mochly-Rosen,D., Miller,K.G., Scheller,R.H., Khaner,H., Lopez,J.
            and Smith,B.L.
  TITLE     p65 fragments, homologous to the C2 region of protein kinase C,
            bind to the intracellular receptors for protein kinase C
  JOURNAL   Biochemistry 31 (35), 8120-8124 (1992)
   PUBMED   1326322
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Perin,M.S., Johnston,P.A., Ozcelik,T., Jahn,R., Francke,U. and
            Sudhof,T.C.
  TITLE     Structural and functional conservation of synaptotagmin (p65) in
            Drosophila and humans
  JOURNAL   J Biol Chem 266 (1), 615-622 (1991)
   PUBMED   1840599
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Blaustein,R.O., Germann,W.J., Finkelstein,A. and DasGupta,B.R.
  TITLE     The N-terminal half of the heavy chain of botulinum type A
            neurotoxin forms channels in planar phospholipid bilayers
  JOURNAL   FEBS Lett 226 (1), 115-120 (1987)
   PUBMED   2446925
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073606.19, AC073616.17,
            AC073572.19, AC078917.14 and AC027288.26.
            
            Summary: This gene encodes a member of the synaptotagmin protein
            family. The synaptotagmins are integral membrane proteins of
            synaptic vesicles that serve as calcium sensors in the process of
            vesicular trafficking and exocytosis. The encoded protein
            participates in triggering neurotransmitter release at the synapse
            in response to calcium binding. Mutations in this gene are
            associated with Baker-Gordon syndrome. [provided by RefSeq, Jan
            2023].
            
            Transcript Variant: This variant (1) encodes isoform 1. Variants 1,
            2, and 3 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.24033.1,
                                           SRR1660803.197773.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: locus in the vicinity of
                                      disease-associated variant(s)
            MANE Ensembl match     :: ENST00000261205.9/ ENSP00000261205.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..422
                     /product="synaptotagmin-1 isoform 1"
                     /note="sytI; synaptotagmin I"
                     /calculated_mol_wt=47442
     Region          6..113
                     /region_name="Syt1_N"
                     /note="N-terminal domain of synaptotagmin-1 (Syt1) and
                     similar proteins; cd21963"
                     /db_xref="CDD:409248"
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            order(40,43..44,46..48,50..51)
                     /site_type="other"
                     /note="Botolinum neurotoxin B binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409248"
     Site            58..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          113..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          136..382
                     /region_name="Phospholipid binding. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          143..265
                     /region_name="C2A_Synaptotagmin-1-5-6-9-10"
                     /note="C2A domain first repeat present in Synaptotagmins
                     1, 5, 6, 9, and 10; cd08385"
                     /db_xref="CDD:176031"
     Site            order(173,179,231,233,239)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176031"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          274..409
                     /region_name="C2B_Synaptotagmin-1"
                     /note="C2 domain second repeat present in Synaptotagmin 1;
                     cd08402"
                     /db_xref="CDD:176047"
     Site            order(304,310,364,366,372)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176047"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     CDS             1..422
                     /gene="SYT1"
                     /gene_synonym="BAGOS; P65; SVP65; SYT"
                     /coded_by="NM_005639.3:553..1821"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9017.1"
                     /db_xref="GeneID:6857"
                     /db_xref="HGNC:HGNC:11509"
                     /db_xref="MIM:185605"
ORIGIN      
        1 mvseshheal aappvttvat vlpsnatepa spgegkedaf sklkekfmne lhkiplppwa
       61 liaiaivavl lvltccfcic kkclfkkknk kkgkekggkn ainmkdvkdl gktmkdqalk
      121 dddaetgltd geekeepkee eklgklqysl dydfqnnqll vgiiqaaelp aldmggtsdp
      181 yvkvfllpdk kkkfetkvhr ktlnpvfneq ftfkvpysel ggktlvmavy dfdrfskhdi
      241 igefkvpmnt vdfghvteew rdlqsaekee qeklgdicfs lryvptagkl tvvileaknl
      301 kkmdvgglsd pyvkihlmqn gkrlkkkktt ikkntlnpyy nesfsfevpf eqiqkvqvvv
      361 tvldydkigk ndaigkvfvg ynstgaelrh wsdmlanprr piaqwhtlqv eeevdamlav
      421 kk
//
LOCUS       NP_001347007            1080 aa            linear   ROD 27-APR-2025
DEFINITION  importin-4 isoform 2 [Mus musculus].
ACCESSION   NP_001347007 XP_006519716
VERSION     NP_001347007.1
DBSOURCE    REFSEQ: accession NM_001360078.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Young,J.C., Major,A.T., Miyamoto,Y., Loveland,K.L. and Jans,D.A.
  TITLE     Distinct effects of importin alpha2 and alpha4 on Oct3/4
            localization and expression in mouse embryonic stem cells
  JOURNAL   FASEB J 25 (11), 3958-3965 (2011)
   PUBMED   21840941
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wang,J., Sarkar,T.R., Zhou,M., Sharan,S., Ritt,D.A., Veenstra,T.D.,
            Morrison,D.K., Huang,A.M. and Sterneck,E.
  TITLE     CCAAT/enhancer binding protein delta (C/EBPdelta, CEBPD)-mediated
            nuclear import of FANCD2 by IPO4 augments cellular response to DNA
            damage
  JOURNAL   Proc Natl Acad Sci U S A 107 (37), 16131-16136 (2010)
   PUBMED   20805509
  REMARK    GeneRIF: report a function of IPO4 and nuclear import in the
            Fanconi anemia pathway of DNA repair
REFERENCE   4  (residues 1 to 1080)
  AUTHORS   Pradeepa,M.M., Manjunatha,S., Sathish,V., Agrawal,S. and Rao,M.R.
  TITLE     Involvement of importin-4 in the transport of transition protein 2
            into the spermatid nucleus
  JOURNAL   Mol Cell Biol 28 (13), 4331-4341 (2008)
   PUBMED   17682055
REFERENCE   5  (residues 1 to 1080)
  AUTHORS   Wesselkamper,S.C., McDowell,S.A., Medvedovic,M., Dalton,T.P.,
            Deshmukh,H.S., Sartor,M.A., Case,L.M., Henning,L.N., Borchers,M.T.,
            Tomlinson,C.R., Prows,D.R. and Leikauf,G.D.
  TITLE     The role of metallothionein in the pathogenesis of acute lung
            injury
  JOURNAL   Am J Respir Cell Mol Biol 34 (1), 73-82 (2006)
   PUBMED   16166738
  REMARK    GeneRIF: Metallothionein deficient mice have a marked decrease in
            Importin 4 transcripts during acute lung injury
REFERENCE   6  (residues 1 to 1080)
  AUTHORS   Corbo,J.C. and Cepko,C.L.
  TITLE     A hybrid photoreceptor expressing both rod and cone genes in a
            mouse model of enhanced S-cone syndrome
  JOURNAL   PLoS Genet 1 (2), e11 (2005)
   PUBMED   16110338
  REMARK    Erratum:[PLoS Genet. 2008 Jan;4(1):e18]
REFERENCE   7  (residues 1 to 1080)
  AUTHORS   Jakel,S., Mingot,J.M., Schwarzmaier,P., Hartmann,E. and Gorlich,D.
  TITLE     Importins fulfil a dual function as nuclear import receptors and
            cytoplasmic chaperones for exposed basic domains
  JOURNAL   EMBO J 21 (3), 377-386 (2002)
   PUBMED   11823430
REFERENCE   8  (residues 1 to 1080)
  AUTHORS   Chu,C.C. and Paul,W.E.
  TITLE     Expressed genes in interleukin-4 treated B cells identified by cDNA
            representational difference analysis
  JOURNAL   Mol Immunol 35 (8), 487-502 (1998)
   PUBMED   9798653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK030490.1, BM950244.1 and AK147086.1.
            
            On Jan 26, 2018 this sequence version replaced XP_006519716.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR13862062.216210.1,
                                           SRR1660811.176148.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 28.19 cM"
     Protein         1..1080
                     /product="importin-4 isoform 2"
                     /note="importin 4a; imp4; ran-binding protein 4"
                     /calculated_mol_wt=118974
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q8TEX9; propagated from
                     UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          24..90
                     /region_name="IBN_N"
                     /note="Importin-beta N-terminal domain; smart00913"
                     /db_xref="CDD:197981"
     Region          348..385
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          <353..>620
                     /region_name="KAP95"
                     /note="Karyopherin (importin) beta [Intracellular
                     trafficking and secretion]; COG5215"
                     /db_xref="CDD:227540"
     Region          353..381
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(370..371,374,377..378,381,412..413,416,419..420,423,
                     456..457,460,463..464,498..499,502,505..506)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          390..427
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          394..424
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          431..471
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          435..464
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          475..513
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          477..507
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          894..931
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          899..927
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          935..973
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI75.1)"
     Region          940..970
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..1080
                     /gene="Ipo4"
                     /gene_synonym="8430408O15Rik; Imp4a; RanBP4"
                     /coded_by="NM_001360078.1:87..3329"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:75751"
                     /db_xref="MGI:MGI:1923001"
ORIGIN      
        1 mepagleqil kelllpdter irrateqlqt ilrdpaalpa lfdllatatd sqirqfaavl
       61 trrrlnnrwr rlapeqresl kslvltalqk etvhsvsvsl aqlsatifrk eglqgwpqfm
      121 nllqhsthss hspekevgll llsvvvssqp eafhahqhel lqllnetlsd vsfpgvlfys
      181 lrtltaiary vrpddvslar mlvpkvvtal rtlipldevk acealealde mletelpiin
      241 phlsevltfc levaknvalg eplrvrvlcc ltflvkvksk allknrlvpp llhalfplma
      301 aeppmgqldp edqdsddddl eiglmgetpk hfavqvvdml alhlppeklc phvmpmleea
      361 lrsedpyqrk agflvlavls dgagdhirqr llypllqivc kglddpsqiv rnaalfalgq
      421 fsenlqphis syseevmpll lsylksvpmg nthhlakacy alenfvenlg pkvqpylpel
      481 mecmlqplkn pskartkela vsaigaiata aqdsllpyfp timdllrefl ltghedfhlv
      541 qiqsletlgv laralgesmk plaeeccqlg lglcihiddp dvrrctyslf aalsglmgeg
      601 lgpylpqitt lmllslrste givpqydgis sfllfdddse aeeeeelmde dmeeegddse
      661 isgysvenaf fdekedtcta lgeismntcv aflpfmdatf devykllecp hmnvrksaye
      721 algqfccalh kasqrsssdp ssilqtslar vmpaymqavk vererpvvma vlesltgvlr
      781 tcgslalqpp grlselcnvl kavlqkktac qdaeeddded ddqaeydaml lehageaipv
      841 laatagghaf apffatflpl llcktkqsct vaeksfavgt laesiqglgt asaqfvsrlf
      901 pvllnnarea dpevrsnaif glgvlaehgg cpaqdhfpkl lglllpllar erhdrvrdni
      961 cgalarvlma spvgktepqv latllralpl kedmeewlti ghlfsflhqn npeqvvdvas
     1021 ellricslil pdnrippdtk aallllltfl akqhtdsfht algslpndka qelqammglt
//
LOCUS       NP_000995                115 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein P2 [Homo sapiens].
ACCESSION   NP_000995
VERSION     NP_000995.1
DBSOURCE    REFSEQ: accession NM_001004.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Horbowicz-Drozdzal,P., Kamel,K., Kmiecik,S., Borkiewicz,L.,
            Tumer,N.E., Shaw,P.C., Tchorzewski,M. and Grela,P.
  TITLE     Phosphorylation of the conserved C-terminal domain of ribosomal
            P-proteins impairs the mode of interaction with plant toxins
  JOURNAL   FEBS Lett 595 (17), 2221-2236 (2021)
   PUBMED   34328639
  REMARK    GeneRIF: Phosphorylation of the conserved C-terminal domain of
            ribosomal P-proteins impairs the mode of interaction with plant
            toxins.
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Cai,Z., Wu,Y., Zhang,F. and Wu,H.
  TITLE     A three-gene signature and clinical outcome in pediatric acute
            myeloid leukemia
  JOURNAL   Clin Transl Oncol 23 (4), 866-873 (2021)
   PUBMED   32862280
  REMARK    GeneRIF: A three-gene signature and clinical outcome in pediatric
            acute myeloid leukemia.
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Campos,R.K., Wijeratne,H.R.S., Shah,P., Garcia-Blanco,M.A. and
            Bradrick,S.S.
  TITLE     Ribosomal stalk proteins RPLP1 and RPLP2 promote biogenesis of
            flaviviral and cellular multi-pass transmembrane proteins
  JOURNAL   Nucleic Acids Res 48 (17), 9872-9885 (2020)
   PUBMED   32890404
  REMARK    GeneRIF: Ribosomal stalk proteins RPLP1 and RPLP2 promote
            biogenesis of flaviviral and cellular multi-pass transmembrane
            proteins.
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Jiang,D., Izumi,K., Ueda,T., Oshima,K., Nakashima,T. and Kimura,M.
  TITLE     Functional characterization of archaeal homologs of human nuclear
            RNase P proteins Rpp21 and Rpp29 provides insights into the
            molecular basis of their cooperativity in catalysis
  JOURNAL   Biochem Biophys Res Commun 482 (1), 68-74 (2017)
   PUBMED   27810361
  REMARK    GeneRIF: Collectively, the present results suggest that PhoRpp21
            binds the loop between P11 and P12 helices through overall
            positively charged clusters on the surface of the complex and
            serves as a scaffold for PhoRpp29 to optimize structural
            conformation of its N-terminal helix (alpha2) in PhoRpp21, as well
            as C-terminal residues in PhoRpp29, for RNase P activity.
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Artero-Castro,A., Perez-Alea,M., Feliciano,A., Leal,J.A.,
            Genestar,M., Castellvi,J., Peg,V., Ramon Y Cajal,S. and
            Lleonart,M.E.
  TITLE     Disruption of the ribosomal P complex leads to stress-induced
            autophagy
  JOURNAL   Autophagy 11 (9), 1499-1519 (2015)
   PUBMED   26176264
  REMARK    GeneRIF: absence of RPLP0, RPLP1, or RPLP2 resulted in reactive
            oxygen species (ROS) accumulation and MAPK1/ERK2 signaling pathway
            activation.
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   7  (residues 1 to 115)
  AUTHORS   Matoba,R., Okubo,K., Hori,N., Fukushima,A. and Matsubara,K.
  TITLE     The addition of 5'-coding information to a 3'-directed cDNA library
            improves analysis of gene expression
  JOURNAL   Gene 146 (2), 199-207 (1994)
   PUBMED   8076819
REFERENCE   8  (residues 1 to 115)
  AUTHORS   Hochstrasser,D.F., Frutiger,S., Paquet,N., Bairoch,A., Ravier,F.,
            Pasquali,C., Sanchez,J.C., Tissot,J.D., Bjellqvist,B., Vargas,R. et
            al.
  TITLE     Human liver protein map: a reference database established by
            microsequencing and gel comparison
  JOURNAL   Electrophoresis 13 (12), 992-1001 (1992)
   PUBMED   1286669
REFERENCE   9  (residues 1 to 115)
  AUTHORS   Sharp,M.G., Adams,S.M., Elvin,P., Walker,R.A., Brammar,W.J. and
            Varley,J.M.
  TITLE     A sequence previously identified as metastasis-related encodes an
            acidic ribosomal phosphoprotein, P2
  JOURNAL   Br J Cancer 61 (1), 83-88 (1990)
   PUBMED   2153399
REFERENCE   10 (residues 1 to 115)
  AUTHORS   Rich,B.E. and Steitz,J.A.
  TITLE     Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
            cDNA clones, in vitro synthesis, and assembly
  JOURNAL   Mol Cell Biol 7 (11), 4065-4074 (1987)
   PUBMED   3323886
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC005354.1 and BC007573.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            phosphoprotein that is a component of the 60S subunit. The protein,
            which is a functional equivalent of the E. coli L7/L12 ribosomal
            protein, belongs to the L12P family of ribosomal proteins. It plays
            an important role in the elongation step of protein synthesis.
            Unlike most ribosomal proteins, which are basic, the encoded
            protein is acidic. Its C-terminal end is nearly identical to the
            C-terminal ends of the ribosomal phosphoproteins P0 and P1. The P2
            protein can interact with P0 and P1 to form a pentameric complex
            consisting of P1 and P2 dimers, and a P0 monomer. The protein is
            located in the cytoplasm. As is typical for genes encoding
            ribosomal proteins, there are multiple processed pseudogenes of
            this gene dispersed through the genome. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB152601.1, DB577310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321153.9/ ENSP00000322419.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..115
                     /product="large ribosomal subunit protein P2"
                     /note="60S acidic ribosomal protein P2; acidic ribosomal
                     phosphoprotein P2; renal carcinoma antigen NY-REN-44;
                     ribosomal protein, large, P2"
                     /calculated_mol_wt=11534
     Region          1..>66
                     /region_name="Ribosomal_P2"
                     /note="Ribosomal protein P2. This subfamily represents the
                     eukaryotic large ribosomal protein P2. Eukaryotic P1 and
                     P2 are functionally equivalent to the bacterial protein
                     L7/L12, but are not homologous to L7/L12. P2 is located in
                     the L12 stalk, with proteins...; cd05833"
                     /db_xref="CDD:100111"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P05387.1)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05387.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05387.1)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P05387.1)"
     Region          78..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05387.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P05387.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P05387.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14997482; propagated from
                     UniProtKB/Swiss-Prot (P05387.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P99027; propagated from
                     UniProtKB/Swiss-Prot (P05387.1)"
     CDS             1..115
                     /gene="RPLP2"
                     /gene_synonym="D11S2243E; LP2; P2; RPP2"
                     /coded_by="NM_001004.4:75..422"
                     /db_xref="CCDS:CCDS7717.1"
                     /db_xref="GeneID:6181"
                     /db_xref="HGNC:HGNC:10377"
                     /db_xref="MIM:180530"
ORIGIN      
        1 mryvasylla alggnsspsa kdikkildsv gieadddrln kviselngkn iedviaqgig
       61 klasvpagga vavsaapgsa apaagsapaa aeekkdekke eseesdddmg fglfd
//
LOCUS       NP_705694                458 aa            linear   PRI 27-APR-2025
DEFINITION  keratin, type I cytoskeletal 13 isoform a [Homo sapiens].
ACCESSION   NP_705694
VERSION     NP_705694.3
DBSOURCE    REFSEQ: accession NM_153490.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Goda,H., Nakashiro,K.I., Sano,Y., Adachi,T., Tokuzen,N.,
            Kuribayashi,N., Hino,S. and Uchida,D.
  TITLE     KRT13 and UPK1B for differential diagnosis between metastatic lung
            carcinoma from oral squamous cell carcinoma and lung squamous cell
            carcinoma
  JOURNAL   Sci Rep 13 (1), 22626 (2023)
   PUBMED   38114532
  REMARK    GeneRIF: KRT13 and UPK1B for differential diagnosis between
            metastatic lung carcinoma from oral squamous cell carcinoma and
            lung squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Takenaka,W., Yokoyama,Y., Ikehata,K., Kouda,S., Hirose,H.,
            Minami,K., Hamada,Y., Mori,S., Koizumi,M. and Yamamoto,H.
  TITLE     KRT13 is upregulated in pancreatic cancer stem-like cells and
            associated with radioresistance
  JOURNAL   J Radiat Res 64 (2), 284-293 (2023)
   PUBMED   36610719
  REMARK    GeneRIF: KRT13 is upregulated in pancreatic cancer stem-like cells
            and associated with radioresistance.
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Lennartz,M., Ullmann,V.S., Gorbokon,N., Uhlig,R., Rico,S.D.,
            Kind,S., Reiswich,V., Viehweger,F., Kluth,M., Hube-Magg,C.,
            Bernreuther,C., Buscheck,F., Putri,D., Clauditz,T.S., Fraune,C.,
            Hinsch,A., Jacobsen,F., Krech,T., Lebock,P., Steurer,S.,
            Burandt,E., Minner,S., Marx,A.H., Simon,R., Sauter,G. and Menz,A.
  TITLE     Cytokeratin 13 (CK13) expression in cancer: a tissue microarray
            study on 10,439 tumors
  JOURNAL   APMIS 131 (2), 77-91 (2023)
   PUBMED   36269681
  REMARK    GeneRIF: Cytokeratin 13 (CK13) expression in cancer: a tissue
            microarray study on 10,439 tumors.
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Yin,L., Li,Q., Mrdenovic,S., Chu,G.C., Wu,B.J., Bu,H., Duan,P.,
            Kim,J., You,S., Lewis,M.S., Liang,G., Wang,R., Zhau,H.E. and
            Chung,L.W.K.
  TITLE     KRT13 promotes stemness and drives metastasis in breast cancer
            through a plakoglobin/c-Myc signaling pathway
  JOURNAL   Breast Cancer Res 24 (1), 7 (2022)
   PUBMED   35078507
  REMARK    GeneRIF: KRT13 promotes stemness and drives metastasis in breast
            cancer through a plakoglobin/c-Myc signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Vinores,S.A., Van Niel,E., Kim,H.J. and Campochiaro,P.A.
  TITLE     Simultaneous expression of keratin and glial fibrillary acidic
            protein by the same cells in epiretinal membranes
  JOURNAL   Invest Ophthalmol Vis Sci 33 (12), 3361-3366 (1992)
   PUBMED   1385351
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Romano,V., Raimondi,E., Bosco,P., Feo,S., Di Pietro,C., Leube,R.E.,
            Troyanovsky,S.M. and Ceratto,N.
  TITLE     Chromosomal mapping of human cytokeratin 13 gene (KRT13)
  JOURNAL   Genomics 14 (2), 495-497 (1992)
   PUBMED   1385306
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Mischke,D., Wachter,E., Hochstrasser,K., Wild,A.G. and Schulz,P.
  TITLE     The N-, but not the C-terminal domains of human keratins 13 and 15
            are closely related
  JOURNAL   Nucleic Acids Res 17 (19), 7984 (1989)
   PUBMED   2477803
REFERENCE   9  (residues 1 to 458)
  AUTHORS   Schulz,P., Wachter,E., Hochstrasser,K., Wild,A.G. and Mischke,D.
  TITLE     Sequence of a human keratin 13 specific cDNA encompassing coil 1B
            through the 3' end
  JOURNAL   Biochem Biophys Res Commun 162 (3), 1522-1527 (1989)
   PUBMED   2475110
REFERENCE   10 (residues 1 to 458)
  AUTHORS   Turyk,M.E., Golub,T.R., Wood,N.B., Hawkins,J.L. and Wilbanks,G.D.
  TITLE     Growth and characterization of epithelial cells from normal human
            uterine ectocervix and endocervix
  JOURNAL   In Vitro Cell Dev Biol 25 (6), 544-556 (1989)
   PUBMED   2472374
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Michael Rogers. The reference sequence was
            derived from AC019349.28.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_705694.2.
            
            Summary: The protein encoded by this gene is a member of the
            keratin gene family. The keratins are intermediate filament
            proteins responsible for the structural integrity of epithelial
            cells and are subdivided into cytokeratins and hair keratins. Most
            of the type I cytokeratins consist of acidic proteins which are
            arranged in pairs of heterotypic keratin chains. This type I
            cytokeratin is paired with keratin 4 and expressed in the
            suprabasal layers of non-cornified stratified epithelia. Mutations
            in this gene and keratin 4 have been associated with the autosomal
            dominant disorder White Sponge Nevus. The type I cytokeratins are
            clustered in a region of chromosome 17q21.2. Alternative splicing
            of this gene results in multiple transcript variants; however, not
            all variants have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223077.1, ERR279827.5455.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147975, SAMEA2156670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000246635.8/ ENSP00000246635.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..458
                     /product="keratin, type I cytoskeletal 13 isoform a"
                     /note="cytokeratin 13; keratin, type I cytoskeletal 13;
                     CK-13; keratin 13, type I"
                     /calculated_mol_wt=49457
     Region          1..103
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P13646.4)"
     Site            27
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P13646.4)"
     Site            35
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P13646.4)"
     Region          103..415
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          104..139
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P13646.4)"
     Region          140..158
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P13646.4)"
     Region          159..250
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P13646.4)"
     Region          251..273
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P13646.4)"
     Region          274..412
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P13646.4)"
     Region          413..458
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P13646.4)"
     Region          420..458
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13646.4)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P13646.4)"
     CDS             1..458
                     /gene="KRT13"
                     /gene_synonym="CK13; K13; WSN2"
                     /coded_by="NM_153490.3:63..1439"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11396.1"
                     /db_xref="GeneID:3860"
                     /db_xref="HGNC:HGNC:6415"
                     /db_xref="MIM:148065"
ORIGIN      
        1 mslrlqsssa sygggfgggs cqlgggrgvs tcstrfvsgg saggygggvs cgfgggagsg
       61 fgggyggglg ggyggglggg fgggfaggfv dfgacdggll tgnekitmqn lndrlasyle
      121 kvraleeana dlevkirdwh lkqspasper dyspyyktie elrdkiltat iennrvilei
      181 dnarlaaddf rlkyenelal rqsveading lrrvldeltl sktdlemqie slneelaymk
      241 knheeemkef snqvvgqvnv emdatpgidl trvlaemreq yeamaernrr daeewfhtks
      301 aelnkevstn tamiqtskte itelrrtlqg leielqsqls mkaglentva etecryalql
      361 qqiqglissi eaqlselrse mecqnqeykm lldiktrleq eiatyrslle gqdakmigfp
      421 ssagsvsprs tsvtttssas vtttsnasgr rtsdvrrp
//
LOCUS       NP_694545                514 aa            linear   PRI 27-APR-2025
DEFINITION  protein APCDD1 precursor [Homo sapiens].
ACCESSION   NP_694545
VERSION     NP_694545.1
DBSOURCE    REFSEQ: accession NM_153000.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Skopelitou,D., Miao,B., Srivastava,A., Kumar,A., Kuswick,M.,
            Dymerska,D., Paramasivam,N., Schlesner,M., Lubinski,J.,
            Hemminki,K., Forsti,A. and Bandapalli,O.R.
  TITLE     Whole Exome Sequencing Identifies APCDD1 and HDAC5 Genes as
            Potentially Cancer Predisposing in Familial Colorectal Cancer
  JOURNAL   Int J Mol Sci 22 (4), 1837 (2021)
   PUBMED   33673279
  REMARK    GeneRIF: Whole Exome Sequencing Identifies APCDD1 and HDAC5 Genes
            as Potentially Cancer Predisposing in Familial Colorectal Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Lin,L., Huang,M., Shi,X., Mayakonda,A., Hu,K., Jiang,Y.Y., Guo,X.,
            Chen,L., Pang,B., Doan,N., Said,J.W., Xie,J., Gery,S., Cheng,X.,
            Lin,Z., Li,J., Berman,B.P., Yin,D., Lin,D.C. and Koeffler,H.P.
  TITLE     Super-enhancer-associated MEIS1 promotes transcriptional
            dysregulation in Ewing sarcoma in co-operation with EWS-FLI1
  JOURNAL   Nucleic Acids Res 47 (3), 1255-1267 (2019)
   PUBMED   30496486
  REMARK    GeneRIF: Through integrative analysis, we identify MEIS1 as a
            super-enhancer-driven oncogene, which co-operates with EWS-FLI1 in
            transcriptional regulation, and plays a key pro-survival role in
            Ewing sarcoma. Moreover, APCDD1, another super-enhancer-associated
            gene, acting as a downstream target of both MEIS1 and EWS-FLI1, is
            also characterized as a novel tumor-promoting factor in this
            malignancy
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Han,W. and Liu,J.
  TITLE     Epigenetic silencing of the Wnt antagonist APCDD1 by promoter DNA
            hyper-methylation contributes to osteosarcoma cell invasion and
            metastasis
  JOURNAL   Biochem Biophys Res Commun 491 (1), 91-97 (2017)
   PUBMED   28698141
  REMARK    GeneRIF: Thus, we have provided the first evidence that APCDD1
            expression is epigenetically silenced in OS, which may facilitate
            invasion and metastasis of OS cells.
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Yiew,N.K.H., Chatterjee,T.K., Tang,Y.L., Pellenberg,R.,
            Stansfield,B.K., Bagi,Z., Fulton,D.J., Stepp,D.W., Chen,W.,
            Patel,V., Kamath,V.M., Litwin,S.E., Hui,D.Y., Rudich,S.M., Kim,H.W.
            and Weintraub,N.L.
  TITLE     A novel role for the Wnt inhibitor APCDD1 in adipocyte
            differentiation: Implications for diet-induced obesity
  JOURNAL   J Biol Chem 292 (15), 6312-6324 (2017)
   PUBMED   28242765
  REMARK    GeneRIF: these novel findings suggest that APCDD1 positively
            regulates adipogenic differentiation and that its down-regulation
            by miR-130 during diet-induced obesity may contribute to impaired
            adipogenic differentiation and obesity-related metabolic disease.
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Li,M., Cheng,R., Zhuang,Y. and Yao,Z.
  TITLE     A recurrent mutation in the APCDD1 gene responsible for hereditary
            hypotrichosis simplex in a large Chinese family
  JOURNAL   Br J Dermatol 167 (4), 952-954 (2012)
   PUBMED   22512811
  REMARK    GeneRIF: mutation in the APCDD1 gene is responsible for hereditary
            hypotrichosis simplex in a large Chinese family.
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Ahn,M.J., Won,H.H., Lee,J., Lee,S.T., Sun,J.M., Park,Y.H.,
            Ahn,J.S., Kwon,O.J., Kim,H., Shim,Y.M., Kim,J., Kim,K., Kim,Y.H.,
            Park,J.Y., Kim,J.W. and Park,K.
  TITLE     The 18p11.22 locus is associated with never smoker non-small cell
            lung cancer susceptibility in Korean populations
  JOURNAL   Hum Genet 131 (3), 365-372 (2012)
   PUBMED   21866343
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Tsui,D.W., Lam,Y.M., Lee,W.S., Leung,T.Y., Lau,T.K., Lau,E.T.,
            Tang,M.H., Akolekar,R., Nicolaides,K.H., Chiu,R.W., Lo,Y.M. and
            Chim,S.S.
  TITLE     Systematic identification of placental epigenetic signatures for
            the noninvasive prenatal detection of Edwards syndrome
  JOURNAL   PLoS One 5 (11), e15069 (2010)
   PUBMED   21152411
  REMARK    GeneRIF: Data show that the methylated VAPA-APCDD1 DNA in maternal
            plasma is predominantly derived from the fetus, and this novel
            fetal epigenetic marker in maternal plasma is useful for the
            noninvasive detection of fetal trisomy 18.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Shimomura,Y., Agalliu,D., Vonica,A., Luria,V., Wajid,M., Baumer,A.,
            Belli,S., Petukhova,L., Schinzel,A., Brivanlou,A.H., Barres,B.A.
            and Christiano,A.M.
  TITLE     APCDD1 is a novel Wnt inhibitor mutated in hereditary hypotrichosis
            simplex
  JOURNAL   Nature 464 (7291), 1043-1047 (2010)
   PUBMED   20393562
  REMARK    GeneRIF: APCDD1 is a novel inhibitor of the Wnt signalling pathway
            with an essential role in human hair growth
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Takahashi,M., Fujita,M., Furukawa,Y., Hamamoto,R., Shimokawa,T.,
            Miwa,N., Ogawa,M. and Nakamura,Y.
  TITLE     Isolation of a novel human gene, APCDD1, as a direct target of the
            beta-Catenin/T-cell factor 4 complex with probable involvement in
            colorectal carcinogenesis
  JOURNAL   Cancer Res 62 (20), 5651-5656 (2002)
   PUBMED   12384519
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Baumer,A., Belli,S., Trueb,R.M. and Schinzel,A.
  TITLE     An autosomal dominant form of hereditary hypotrichosis simplex maps
            to 18p11.32-p11.23 in an Italian family
  JOURNAL   Eur J Hum Genet 8 (6), 443-448 (2000)
   PUBMED   10878665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB056722.1, BC053324.1 and
            AP001099.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This locus encodes an inhibitor of the Wnt signaling
            pathway. Mutations at this locus have been associated with
            hereditary hypotrichosis simplex. Increased expression of this gene
            may also be associated with colorectal carcinogenesis.[provided by
            RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB056722.1, AB104887.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355285.10/ ENSP00000347433.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.22"
     Protein         1..514
                     /product="protein APCDD1 precursor"
                     /note="protein APCDD1; adenomatosis polyposis coli
                     down-regulated 1 protein; hypoptrichosis simplex"
                     /calculated_mol_wt=55847
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2968
     Region          51..282
                     /region_name="APCDDC"
                     /note="Adenomatosis polyposis coli down-regulated 1;
                     pfam14921"
                     /db_xref="CDD:464377"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8J025.1)"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8J025.1)"
     Region          267..463
                     /region_name="APCDDC"
                     /note="Adenomatosis polyposis coli down-regulated 1;
                     pfam14921"
                     /db_xref="CDD:464377"
     Site            319
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8J025.1)"
     Region          438..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8J025.1)"
     Site            493..512
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8J025.1)"
     CDS             1..514
                     /gene="APCDD1"
                     /gene_synonym="B7323; DRAPC1; FP7019; HHS; HTS; HYPT1"
                     /coded_by="NM_153000.5:348..1892"
                     /db_xref="CCDS:CCDS11849.1"
                     /db_xref="GeneID:147495"
                     /db_xref="HGNC:HGNC:15718"
                     /db_xref="MIM:607479"
ORIGIN      
        1 mswprrlllr ylfpalllhg lgegsallhp dsrshprsle ksawrafkes qchhmlkhlh
       61 ngaritvqmp ptieghwvst gcevrsgpef itrsyrfyhn ntfkayqfyy gsnrctnpty
      121 tliirgkirl rqaswiirgg teadyqlhnv qvichteava eklgqqvnrt cpgfladggp
      181 wvqdvaydlw reengcectk avnfamhelq lirvekqylh hnldhlveel flgdihtdat
      241 qrmfyrpssy qpplqnaknh dhaciacrii yrsdehhppi lppkadltig lhgewvsqrc
      301 evrpevlflt rhfifhdnnn tweghyyhys dpvckhptfs iyargrysrg vlssrvmggt
      361 efvfkvnhmk vtpmdaatas llnvfngnec gaegswqvgi qqdvthtngc valgiklpht
      421 eyeifkmeqd argryllfng qrpsdgsspd rpekratsyq mplvqcasss praedlaeds
      481 gsslygrapg rhtwslllaa laclvpllhw nirr
//
LOCUS       NP_001347241             480 aa            linear   PLN 27-APR-2025
DEFINITION  uDP-glycosyltransferase 708D1 [Glycine max].
ACCESSION   NP_001347241 XP_003534077
VERSION     NP_001347241.1
DBSOURCE    REFSEQ: accession NM_001360312.1
KEYWORDS    RefSeq.
SOURCE      Glycine max (soybean)
  ORGANISM  Glycine max
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
            Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50
            kb inversion clade; NPAAA clade; indigoferoid/millettioid clade;
            Phaseoleae; Glycine; Glycine subgen. Soja.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Hirade,Y., Kotoku,N., Terasaka,K., Saijo-Hamano,Y., Fukumoto,A. and
            Mizukami,H.
  TITLE     Identification and functional analysis of 2-hydroxyflavanone
            C-glucosyltransferase in soybean (Glycine max)
  JOURNAL   FEBS Lett 589 (15), 1778-1786 (2015)
   PUBMED   25979175
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Umezawa,T., Sakurai,T., Totoki,Y., Toyoda,A., Seki,M., Ishiwata,A.,
            Akiyama,K., Kurotani,A., Yoshida,T., Mochida,K., Kasuga,M.,
            Todaka,D., Maruyama,K., Nakashima,K., Enju,A., Mizukado,S.,
            Ahmed,S., Yoshiwara,K., Harada,K., Tsubokura,Y., Hayashi,M.,
            Sato,S., Anai,T., Ishimoto,M., Funatsuki,H., Teraishi,M., Osaki,M.,
            Shinano,T., Akashi,R., Sakaki,Y., Yamaguchi-Shinozaki,K. and
            Shinozaki,K.
  TITLE     Sequencing and analysis of approximately 40,000 soybean cDNA clones
            from a full-length-enriched cDNA library
  JOURNAL   DNA Res 15 (6), 333-346 (2008)
   PUBMED   18927222
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            ACUP04003333.1 and LC003312.1.
            
            On Feb 1, 2018 this sequence version replaced XP_003534077.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: LC003312.1, BT097680.1 [ECO:0000345]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Glycine max"
                     /cultivar="Williams 82"
                     /db_xref="taxon:3847"
                     /chromosome="9"
                     /map="9"
     Protein         1..480
                     /product="uDP-glycosyltransferase 708D1"
                     /EC_number="2.4.1.360"
                     /note="Glyma.09g162400; UDP-glycosyltransferase
                     708A6-like"
                     /calculated_mol_wt=52384
     Region          9..464
                     /region_name="GT1_Gtf-like"
                     /note="UDP-glycosyltransferases and similar proteins;
                     cd03784"
                     /db_xref="CDD:340817"
     Site            order(19..20,22,181,184..185,189,216,291,371,373,375..376,
                     379)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(19,291,371,373,375..376)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            20
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
     Region          291..292
                     /region_name="UDP.
                     /evidence=ECO:0000250|UniProtKB:A0A0A1HA03"
                     /note="propagated from UniProtKB/Swiss-Prot (I1L3T1.1)"
     CDS             1..480
                     /gene="UGT708D1"
                     /coded_by="NM_001360312.1:127..1569"
                     /db_xref="GeneID:100776116"
ORIGIN      
        1 msssegvvhv aflpsagmgh lnpflrlaat firygckvtl itpkptvsla esnlisrfcs
       61 sfphqvtqld lnlvsvdptt vdtidpfflq fetirrslhl lppilsllst plsafiydit
      121 litpllsvie klscpsylyf tssarmfsff arvsvlsasn pgqtpssfig ddgvkipgft
      181 spiprssvpp ailqassnlf qrimledsan vtklnngvfi nsfeelegea laalnggkvl
      241 eglppvygvg plmaceyekg deegqkgcms sivkwldeqs kgsvvyvslg nrtetrreqi
      301 kdmalgliec gygflwvvkl krvdkedeeg leevlgsels skvkekgvvv kefvdqveil
      361 ghpsvggfls hggwnsvtet vwkgvpclsw pqhsdqkmsa evirmsgmgi wpeewgwgtq
      421 dvvkgdeiak rikemmsnes lrvkagelke aalkaagvgg scevtikrqi eewkrnaqan
//
LOCUS       NP_004916                292 aa            linear   PRI 27-APR-2025
DEFINITION  aquaporin-3 isoform 1 [Homo sapiens].
ACCESSION   NP_004916
VERSION     NP_004916.1
DBSOURCE    REFSEQ: accession NM_004925.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Edamana,S., Login,F.H., Riishede,A., Dam,V.S., Kirkegaard,T. and
            Nejsum,L.N.
  TITLE     The water channels aquaporin-1 and aquaporin-3 interact with and
            affect the cell polarity protein Scribble in 3D in vitro models of
            breast cancer
  JOURNAL   Am J Physiol Cell Physiol 327 (5), C1323-C1334 (2024)
   PUBMED   39279492
  REMARK    GeneRIF: The water channels aquaporin-1 and aquaporin-3 interact
            with and affect the cell polarity protein Scribble in 3D in vitro
            models of breast cancer.
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Liang,Y., Chen,P., Wang,S., Cai,L., Zhu,F., Jiang,Y., Li,L.,
            Zhu,L., Heng,Y., Zhang,W., Pan,Y., Wei,W. and Jia,L.
  TITLE     SCFFBXW5-mediated degradation of AQP3 suppresses autophagic cell
            death through the PDPK1-AKT-MTOR axis in hepatocellular carcinoma
            cells
  JOURNAL   Autophagy 20 (9), 1984-1999 (2024)
   PUBMED   38726865
  REMARK    GeneRIF: SCF[FBXW5]-mediated degradation of AQP3 suppresses
            autophagic cell death through the PDPK1-AKT-MTOR axis in
            hepatocellular carcinoma cells.
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Ziehe,D., Marko,B., Thon,P., Rahmel,T., Palmowski,L., Nowak,H., von
            Busch,A., Wolf,A., Witowski,A., Vonheder,J., Ellger,B., Wappler,F.,
            Schwier,E., Henzler,D., Kohler,T., Zarbock,A., Ehrentraut,S.F.,
            Putensen,C., Frey,U.H., Anft,M., Babel,N., Adamzik,M., Koos,B.,
            Bergmann,L., Unterberg,M. and Rump,K.
  CONSRTM   SepsisDataNet.NRW Research Group
  TITLE     The Aquaporin 3 Polymorphism (rs17553719) Is Associated with Sepsis
            Survival and Correlated with IL-33 Secretion
  JOURNAL   Int J Mol Sci 25 (3), 1400 (2024)
   PUBMED   38338680
  REMARK    GeneRIF: The Aquaporin 3 Polymorphism (rs17553719) Is Associated
            with Sepsis Survival and Correlated with IL-33 Secretion.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Thon,P., Rahmel,T., Ziehe,D., Palmowski,L., Marko,B., Nowak,H.,
            Wolf,A., Witowski,A., Orlowski,J., Ellger,B., Wappler,F.,
            Schwier,E., Henzler,D., Kohler,T., Zarbock,A., Ehrentraut,S.F.,
            Putensen,C., Frey,U.H., Anft,M., Babel,N., Sitek,B., Adamzik,M.,
            Bergmann,L., Unterberg,M., Koos,B. and Rump,K.
  CONSRTM   SepsisDataNet.NRW Research Group
  TITLE     AQP3 and AQP9-Contrary Players in Sepsis?
  JOURNAL   Int J Mol Sci 25 (2), 1209 (2024)
   PUBMED   38279209
  REMARK    GeneRIF: AQP3 and AQP9-Contrary Players in Sepsis?
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Roudier,N., Ripoche,P., Gane,P., Le Pennec,P.Y., Daniels,G.,
            Cartron,J.P. and Bailly,P.
  TITLE     AQP3 deficiency in humans and the molecular basis of a novel blood
            group system, GIL
  JOURNAL   J Biol Chem 277 (48), 45854-45859 (2002)
   PUBMED   12239222
  REMARK    GeneRIF: first reported cases of AQP3 deficiency in humans and
            provide the molecular basis of a new blood group system, GIL,
            encoded by the AQP3 protein
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Inase,N., Fushimi,K., Ishibashi,K., Uchida,S., Ichioka,M.,
            Sasaki,S. and Marumo,F.
  TITLE     Isolation of human aquaporin 3 gene
  JOURNAL   J Biol Chem 270 (30), 17913-17916 (1995)
   PUBMED   7543093
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Ishibashi,K., Sasaki,S., Saito,F., Ikeuchi,T. and Marumo,F.
  TITLE     Structure and chromosomal localization of a human water channel
            (AQP3) gene
  JOURNAL   Genomics 27 (2), 352-354 (1995)
   PUBMED   7558005
  REMARK    Erratum:[Genomics 1995 Dec 10;30(3):633]
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Raina,S., Preston,G.M., Guggino,W.B. and Agre,P.
  TITLE     Molecular cloning and characterization of an aquaporin cDNA from
            salivary, lacrimal, and respiratory tissues
  JOURNAL   J Biol Chem 270 (4), 1908-1912 (1995)
   PUBMED   7530250
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK315760.1 and BC013566.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the water channel protein aquaporin 3.
            Aquaporins are a family of small integral membrane proteins related
            to the major intrinsic protein, also known as aquaporin 0.
            Aquaporin 3 is localized at the basal lateral membranes of
            collecting duct cells in the kidney. In addition to its water
            channel function, aquaporin 3 has been found to facilitate the
            transport of nonionic small solutes such as urea and glycerol, but
            to a smaller degree. It has been suggested that water channels can
            be functionally heterogeneous and possess water and solute
            permeation mechanisms. Alternative splicing of this gene results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.212200.1,
                                           SRR5189655.178129.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297991.6/ ENSP00000297991.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..292
                     /product="aquaporin-3 isoform 1"
                     /note="aquaporin 3 (GIL blood group); aquaglyceroporin-3"
                     /calculated_mol_wt=31413
     Region          23..264
                     /region_name="MIP"
                     /note="Major intrinsic protein (MIP) superfamily. Members
                     of the MIP superfamily function as membrane channels that
                     selectively transport water, small neutral molecules, and
                     ions out of and between cells. The channel proteins share
                     a common fold: the N-terminal...; cd00333"
                     /db_xref="CDD:238204"
     Site            25..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92482.2)"
     Site            57..74
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92482.2)"
     Site            order(63,81..83,211..212,215,218)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            63
                     /site_type="other"
                     /note="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:O14520; propagated from
                     UniProtKB/Swiss-Prot (Q92482.2)"
     Site            order(83..85,215..217)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     Region          83..85
                     /region_name="NPA 1.
                     /evidence=ECO:0000250|UniProtKB:O14520"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92482.2)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92482.2)"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92482.2)"
     Site            160..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92482.2)"
     Site            190..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92482.2)"
     Site            212
                     /site_type="other"
                     /note="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:O14520; propagated from
                     UniProtKB/Swiss-Prot (Q92482.2)"
     Region          215..217
                     /region_name="NPA 2.
                     /evidence=ECO:0000250|UniProtKB:O14520"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92482.2)"
     Site            218
                     /site_type="other"
                     /note="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:O14520; propagated from
                     UniProtKB/Swiss-Prot (Q92482.2)"
     Site            243..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92482.2)"
     CDS             1..292
                     /gene="AQP3"
                     /gene_synonym="AQP-3; GIL"
                     /coded_by="NM_004925.5:64..942"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6542.1"
                     /db_xref="GeneID:360"
                     /db_xref="HGNC:HGNC:636"
                     /db_xref="MIM:600170"
ORIGIN      
        1 mgrqkelvsr cgemlhiryr llrqalaecl gtlilvmfgc gsvaqvvlsr gthggfltin
       61 lafgfavtlg iliagqvsga hlnpavtfam cflarepwik lpiytlaqtl gaflgagivf
      121 glyydaiwhf adnqlfvsgp ngtagifaty psghldming ffdqfigtas livcvlaivd
      181 pynnpvprgl eaftvglvvl vigtsmgfns gyavnpardf gprlftalag wgsavfttgq
      241 hwwwvpivsp llgsiagvfv yqlmigchle qpppsneeen vklahvkhke qi
//
LOCUS       NP_078930                702 aa            linear   PRI 27-APR-2025
DEFINITION  polynucleotide 5'-hydroxyl-kinase NOL9 [Homo sapiens].
ACCESSION   NP_078930
VERSION     NP_078930.4
DBSOURCE    REFSEQ: accession NM_024654.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Gordon,J., Pillon,M.C. and Stanley,R.E.
  TITLE     Nol9 Is a Spatial Regulator for the Human ITS2 Pre-rRNA
            Endonuclease-Kinase Complex
  JOURNAL   J Mol Biol 431 (19), 3771-3786 (2019)
   PUBMED   31288032
  REMARK    GeneRIF: a Nol9-encoded nucleolar localization sequence that is
            responsible for nucleolar transport of the assembled Las1L-Nol9
            complex, is reported.
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Bielczyk-Maczynska,E., Lam Hung,L., Ferreira,L., Fleischmann,T.,
            Weis,F., Fernandez-Pevida,A., Harvey,S.A., Wali,N., Warren,A.J.,
            Barroso,I., Stemple,D.L. and Cvejic,A.
  TITLE     The Ribosome Biogenesis Protein Nol9 Is Essential for Definitive
            Hematopoiesis and Pancreas Morphogenesis in Zebrafish
  JOURNAL   PLoS Genet 11 (12), e1005677 (2015)
   PUBMED   26624285
  REMARK    GeneRIF: we present the nol9sa1022/sa1022 mutant, a novel zebrafish
            ribosomopathy model, which recapitulates key human disease
            characteristics.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 702)
  AUTHORS   Heindl,K. and Martinez,J.
  TITLE     Nol9 is a novel polynucleotide 5'-kinase involved in ribosomal RNA
            processing
  JOURNAL   EMBO J 29 (24), 4161-4171 (2010)
   PUBMED   21063389
  REMARK    GeneRIF: The polynucleotide kinase activity of Nol9 is required for
            efficient generation of the 5.8S and 28S ribosomal RNAs from the
            32S precursor.
REFERENCE   5  (residues 1 to 702)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 702)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   7  (residues 1 to 702)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 702)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591866.13.
            
            On Nov 23, 2018 this sequence version replaced NP_078930.3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK091284.1, SRR1660803.101026.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377705.6/ ENSP00000366934.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.31"
     Protein         1..702
                     /product="polynucleotide 5'-hydroxyl-kinase NOL9"
                     /EC_number="2.7.1.78"
                     /note="polynucleotide 5'-kinase"
                     /calculated_mol_wt=79192
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q5SY16.1)"
     Region          31..47
                     /region_name="Nucleolar localization signal.
                     /evidence=ECO:0000269|PubMed:31288032"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SY16.1)"
     Region          69..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SY16.1)"
     Region          298..635
                     /region_name="Clp1"
                     /note="Pre-mRNA cleavage complex II protein Clp1; cl42059"
                     /db_xref="CDD:477931"
     Region          306..>415
                     /region_name="CLP1_P"
                     /note="mRNA cleavage and polyadenylation factor CLP1
                     P-loop; pfam16575"
                     /db_xref="CDD:406878"
     Region          480..702
                     /region_name="Interaction with LAS1L.
                     /evidence=ECO:0000269|PubMed:31288032"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SY16.1)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5SY16.1)"
     Region          680..702
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SY16.1)"
     CDS             1..702
                     /gene="NOL9"
                     /gene_synonym="Grc3; NET6"
                     /coded_by="NM_024654.5:12..2120"
                     /db_xref="CCDS:CCDS80.1"
                     /db_xref="GeneID:79707"
                     /db_xref="HGNC:HGNC:26265"
                     /db_xref="MIM:620304"
ORIGIN      
        1 madsglllkr gscrstwlrv rkarpqlils rrprrrlgsl rwcgrrrlrw rllqaqasgv
       61 dwregarqvs raaaarrpnt atpspipspt pasepesepe lesasschrp llippvrpvg
      121 pgrallllpv eqgftfsgic rvtclygqvq vfgftisqgq paqdifsvyt hsclsihalh
      181 ysqpekskke lkrearnllk shlnlddrrw smqnfspqcs ivllehlkta tvnfitsypg
      241 ssyifvqesp tpqikpeyla lrsvgirrek krkglqltes tlsaleelvn vsceevdgcp
      301 vilvcgsqdv gkstfnryli nhllnslpcv dylecdlgqt eftppgcisl lnitepvlgp
      361 pfthlrtpqk mvyygkpsck nnyenyidiv kyvfsaykre splivntmgw vsdqglllli
      421 dlirllspsh vvqfrsdhsk ympdltpqyv ddmdglytks ktkmrnrrfr laafadalef
      481 adeekespve ftghkligvy tdfafritpr nreshnkilr dlsilsylsq lqppmpkpls
      541 plhsltpyqv pfnavalrit hsdvapthil yavnaswvgl ckiqddvrgy tngpillaqt
      601 picdclgfgi crgidmekrl yhiltpvppe elrtvncllv gaiaiphcvl kcqrgiegtv
      661 pyvttdynfk lpgasekiga repeeahkek pyrrpkfcrk mk
//
LOCUS       NP_001349794             276 aa            linear   ROD 27-APR-2025
DEFINITION  ARL14 effector protein [Mus musculus].
ACCESSION   NP_001349794 XP_006499149
VERSION     NP_001349794.1
DBSOURCE    REFSEQ: accession NM_001362865.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Sansom,S.N., Griffiths,D.S., Faedo,A., Kleinjan,D.J., Ruan,Y.,
            Smith,J., van Heyningen,V., Rubenstein,J.L. and Livesey,F.J.
  TITLE     The level of the transcription factor Pax6 is essential for
            controlling the balance between neural stem cell self-renewal and
            neurogenesis
  JOURNAL   PLoS Genet 5 (6), e1000511 (2009)
   PUBMED   19521500
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX649348.8 and BX890640.4.
            
            On May 1, 2018 this sequence version replaced XP_006499149.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 3. All four variants encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.2354174.1,
                                           ERR3363660.765763.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 55.97 cM"
     Protein         1..276
                     /product="ARL14 effector protein"
                     /note="ARF7 effector protein"
                     /calculated_mol_wt=30880
     Region          145..248
                     /region_name="ARF7EP_C"
                     /note="ARF7 effector protein C-terminus; pfam14949"
                     /db_xref="CDD:464395"
     Region          158..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BIX3.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N8R7; propagated from
                     UniProtKB/Swiss-Prot (Q8BIX3.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355; propagated from
                     UniProtKB/Swiss-Prot (Q8BIX3.1)"
     CDS             1..276
                     /gene="Arl14ep"
                     /gene_synonym="2700007P21Rik; 4930448O08Rik; ARF7EP"
                     /coded_by="NM_001362865.1:161..991"
                     /db_xref="CCDS:CCDS16503.1"
                     /db_xref="GeneID:212772"
                     /db_xref="MGI:MGI:1926020"
ORIGIN      
        1 mdpcsvgvql rtthdchktf ytrhtgfktl kelssndmll lqlrtgmtls gnnticlhhv
       61 kiyidrfedl qksccdpfni hkklakknlh vidlddatfl sakfgrqlvp gwklcpkctq
      121 iingsvdvds ddrqrrkpds dgrtakalrs lqftnpgkqt efapeggkre krkltkatsa
      181 asdrqiipak skvydsqgll ifsgmdlcdc ldedclgcfy acptcgstkc gaecrcdrkw
      241 lyeqieiegg eiihnkhagk aygllspchp ydilqk
//
LOCUS       NP_001355613            1007 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein 26 isoform 2 [Mus musculus].
ACCESSION   NP_001355613
VERSION     NP_001355613.1
DBSOURCE    REFSEQ: accession NM_001368684.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Kogo,H., Kowa-Sugiyama,H., Yamada,K., Bolor,H., Tsutsumi,M.,
            Ohye,T., Inagaki,H., Taniguchi,M., Toda,T. and Kurahashi,H.
  TITLE     Screening of genes involved in chromosome segregation during
            meiosis I: toward the identification of genes responsible for
            infertility in humans
  JOURNAL   J Hum Genet 55 (5), 293-299 (2010)
   PUBMED   20339383
REFERENCE   4  (residues 1 to 1007)
  AUTHORS   Guo,G., Huss,M., Tong,G.Q., Wang,C., Li Sun,L., Clarke,N.D. and
            Robson,P.
  TITLE     Resolution of cell fate decisions revealed by single-cell gene
            expression analysis from zygote to blastocyst
  JOURNAL   Dev Cell 18 (4), 675-685 (2010)
   PUBMED   20412781
REFERENCE   5  (residues 1 to 1007)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   6  (residues 1 to 1007)
  AUTHORS   McKee,A.E., Minet,E., Stern,C., Riahi,S., Stiles,C.D. and
            Silver,P.A.
  TITLE     A genome-wide in situ hybridization map of RNA-binding proteins
            reveals anatomically restricted expression in the developing mouse
            brain
  JOURNAL   BMC Dev Biol 5, 14 (2005)
   PUBMED   16033648
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1007)
  AUTHORS   Peterson,K.A., King,B.L., Hagge-Greenberg,A., Roix,J.J., Bult,C.J.
            and O'Brien,T.P.
  TITLE     Functional and comparative genomic analysis of the piebald deletion
            region of mouse chromosome 14
  JOURNAL   Genomics 80 (2), 172-184 (2002)
   PUBMED   12160731
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113125.8 and AC146601.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14777535.1871125.1,
                                           SRR1660811.223400.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 55.36 cM"
     Protein         1..1007
                     /product="RNA-binding protein 26 isoform 2"
                     /note="RNA-binding protein 26; cutaneous T-cell lymphoma
                     tumor antigen se70-2; protein expressed in male leptotene
                     and zygotene spermatocytes 393"
                     /calculated_mol_wt=113456
     Region          11..76
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          106..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          <294..314
                     /region_name="ZnF_C3H1"
                     /note="zinc finger; smart00356"
                     /db_xref="CDD:214632"
     Region          334..404
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          460..515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T8P6; propagated from
                     UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Site            510
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T8P6; propagated from
                     UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          531..606
                     /region_name="RRM1_RBM26"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     RNA-binding protein 26 (RBM26); cd12516"
                     /db_xref="CDD:409938"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          642..662
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          <720..>841
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Region          853..884
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     Region          886..957
                     /region_name="RRM2_RBM26_like"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     RNA-binding protein 26 (RBM26) and similar proteins;
                     cd12258"
                     /db_xref="CDD:409703"
     Region          965..1007
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZN0.2)"
     CDS             1..1007
                     /gene="Rbm26"
                     /gene_synonym="1700009P03Rik; C230097K14Rik; MLZ-393;
                     Pro1777; Se70-2"
                     /coded_by="NM_001368684.1:463..3486"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS88725.1"
                     /db_xref="GeneID:74213"
                     /db_xref="MGI:MGI:1921463"
ORIGIN      
        1 mvskmiienf ealkswlskt lepicdadps alakyvlalv kkdksekelk alcidqldvf
       61 lqketqifve klfdavntks ylpppeqpss gslkvdflqh qekdikkeel tkeeerekkf
      121 srrlnhsppq sssryrdnrs rderkkddrs rkrdydrnpp rrdsyrdryn rrrgrsrsys
      181 rsrsrswske rlrdrdrdrs rtrsrsrtrs rerdlvkpky dldrtdplen nytpvssvsn
      241 issghypvpt lsstitviap thhgnnttes wsefhedqvd hnsyvrppmp kkrcrdydek
      301 gfcmrgdmcp fdhgsdpvvv edvnlpgmlp fpaqppvveg ppppglpppp piltpppvnl
      361 rppvpppgpl ppslppvtgp ppplpplqps gmdappnsat ssvptvvttg ihhqpppapp
      421 slftadtydt dgynpeapsi tntsrpmyrh rvhaqrpnli gltsgdmdlp prekppnkss
      481 mrivvdsesr krtigsgepg vstkktwfdk pnfnrtnspg fqkkvqfgne ntklelrkvp
      541 pelnniskln ehfsrfgtlv nlqvayngdp egaliqfaty eeakkaisst eavlnnrfik
      601 vywhregttq qlqttspkvi qplvqqpilp vvkqsvkerl gpvpsattep aeaqsatsel
      661 pqnvtklsvk drlgfvskps vsatekvlst stgltktvyn paalkaaqkt lsvstpavdn
      721 neaqkkkqea lklqqdvrkr kqeilekhie tqkmliskle knktmksedk aeimktleil
      781 tknitklkde vkstspgrcl pksiktktqm qkelldteld lykkmqagee vtelrrkyte
      841 lqleaakrgi lssgrgrgih trgrgtahgr grgrgrgrgv pghavvdhrp raleisafte
      901 sdredllphf aqygeiedcq iddaslhaii tfktraeaea aaihgarfkg qdlklawnkp
      961 ianmsavdte eaepdeeefq eeslvddsll qdddeeeedn esrswrr
//
LOCUS       NP_004528                391 aa            linear   PRI 27-APR-2025
DEFINITION  nucleosome assembly protein 1-like 1 isoform 1 [Homo sapiens].
ACCESSION   NP_004528 NP_071743
VERSION     NP_004528.1
DBSOURCE    REFSEQ: accession NM_004537.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Zhu,X., Li,Y., Shao,Z., Lu,X. and Chen,Y.
  TITLE     NAP1L1 Promotes Endometrial Cancer Progression via EP300-Mediated
            DDX5 Promoter Acetylation
  JOURNAL   Mol Cancer Res 22 (11), 1011-1021 (2024)
   PUBMED   38953887
  REMARK    GeneRIF: NAP1L1 Promotes Endometrial Cancer Progression via
            EP300-Mediated DDX5 Promoter Acetylation.
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Gul,G., Aydin,M.A., Algul,S., Kiziltan,R. and Kemik,O.
  TITLE     Nucleosome assembly protein 1-like 1 (NAP1L1) in gastric cancer
            patients: a potential biomarker with diagnostic and prognostic
            utility
  JOURNAL   Biomarkers 29 (1), 30-35 (2024)
   PUBMED   38258494
  REMARK    GeneRIF: Nucleosome assembly protein 1-like 1 (NAP1L1) in gastric
            cancer patients: a potential biomarker with diagnostic and
            prognostic utility.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Ohtomo,H., Yamane,T., Oda,T., Kodera,N., Kurita,J.I., Tsunaka,Y.,
            Amyot,R., Ikeguchi,M. and Nishimura,Y.
  TITLE     Dynamic Solution Structures of Whole Human NAP1 Dimer Bound to One
            and Two Histone H2A-H2B Heterodimers Obtained by Integrative
            Methods
  JOURNAL   J Mol Biol 435 (15), 168189 (2023)
   PUBMED   37380014
  REMARK    GeneRIF: Dynamic Solution Structures of Whole Human NAP1 Dimer
            Bound to One and Two Histone H2A-H2B Heterodimers Obtained by
            Integrative Methods.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Freitag,M. and Schwertz,H.
  TITLE     A New Role of NAP1L1 in Megakaryocytes and Human Platelets
  JOURNAL   Int J Mol Sci 23 (23), 14694 (2022)
   PUBMED   36499021
  REMARK    GeneRIF: A New Role of NAP1L1 in Megakaryocytes and Human
            Platelets.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Xiaohua,Zhu., Xie,Y., Huang,W., Chen,Z. and Guo,S.
  TITLE     NAP1L1 promotes tumor proliferation through HDGF/C-JUN signaling in
            ovarian cancer
  JOURNAL   BMC Cancer 22 (1), 339 (2022)
   PUBMED   35351053
  REMARK    GeneRIF: NAP1L1 promotes tumor proliferation through HDGF/C-JUN
            signaling in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Kho,Y., Kim,S.C., Jiang,C., Barma,D., Kwon,S.W., Cheng,J.,
            Jaunbergs,J., Weinbaum,C., Tamanoi,F., Falck,J. and Zhao,Y.
  TITLE     A tagging-via-substrate technology for detection and proteomics of
            farnesylated proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (34), 12479-12484 (2004)
   PUBMED   15308774
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Rehtanz,M., Schmidt,H.M., Warthorst,U. and Steger,G.
  TITLE     Direct interaction between nucleosome assembly protein 1 and the
            papillomavirus E2 proteins involved in activation of transcription
  JOURNAL   Mol Cell Biol 24 (5), 2153-2168 (2004)
   PUBMED   14966293
  REMARK    GeneRIF: These results suggest that the binding of
            sequence-specific DNA binding proteins to human nucleosome assembly
            protein 1 may be an important step contributing to the activation
            of transcription.
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Tomarev,S.I., Wistow,G., Raymond,V., Dubois,S. and Malyukova,I.
  TITLE     Gene expression profile of the human trabecular meshwork: NEIBank
            sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 44 (6), 2588-2596 (2003)
   PUBMED   12766061
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Asahara,H., Tartare-Deckert,S., Nakagawa,T., Ikehara,T., Hirose,F.,
            Hunter,T., Ito,T. and Montminy,M.
  TITLE     Dual roles of p300 in chromatin assembly and transcriptional
            activation in cooperation with nucleosome assembly protein 1 in
            vitro
  JOURNAL   Mol Cell Biol 22 (9), 2974-2983 (2002)
   PUBMED   11940655
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Simon,H.U., Mills,G.B., Kozlowski,M., Hogg,D., Branch,D., Ishimi,Y.
            and Siminovitch,K.A.
  TITLE     Molecular characterization of hNRP, a cDNA encoding a human
            nucleosome-assembly-protein-I-related gene product involved in the
            induction of cell proliferation
  JOURNAL   Biochem J 297 (Pt 2) (Pt 2), 389-397 (1994)
   PUBMED   8297347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU183927.1, AL162068.1,
            DA512918.1, AW950481.1, AF300335.2, DA137494.1, CD000987.1,
            CD678271.1, DB546929.1, AC011611.26 and AA057019.1.
            
            On Sep 24, 2001 this sequence version replaced NP_071743.1.
            
            Summary: This gene encodes a member of the nucleosome assembly
            protein (NAP) family. This protein participates in DNA replication
            and may play a role in modulating chromatin formation and
            contribute to the regulation of cell proliferation. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms; however, not all have been fully described. [provided by
            RefSeq, Apr 2015].
            
            Transcript Variant: This variant (2) represents the longest
            transcript and encodes the longer isoform (1). Variants 1, 2 and 4
            encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL162068.1, SRR11853565.7328.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000618691.5/ ENSP00000477538.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..391
                     /product="nucleosome assembly protein 1-like 1 isoform 1"
                     /note="HSP22-like protein interacting protein;
                     NAP-1-related protein"
                     /calculated_mol_wt=45243
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55209.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P55209.1)"
     mat_peptide     2..388
                     /product="Nucleosome assembly protein 1-like 1.
                     /id=PRO_0000185652"
                     /note="propagated from UniProtKB/Swiss-Prot (P55209.1)"
                     /calculated_mol_wt=44859
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P55209.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P55209.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55209.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P28656; propagated from
                     UniProtKB/Swiss-Prot (P55209.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55209.1)"
     Region          76..343
                     /region_name="NAP"
                     /note="Nucleosome assembly protein (NAP); pfam00956"
                     /db_xref="CDD:460010"
     Site            116
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P55209.1)"
     Region          125..150
                     /region_name="NAP1L motif.
                     /evidence=ECO:0000269|PubMed:21211722"
                     /note="propagated from UniProtKB/Swiss-Prot (P55209.1)"
     Region          132..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55209.1)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P55209.1)"
     Region          273..279
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P55209.1)"
     Region          346..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55209.1)"
     Site            388
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P55209.1)"
     CDS             1..391
                     /gene="NAP1L1"
                     /gene_synonym="NAP1; NAP1L; NRP"
                     /coded_by="NM_004537.7:140..1315"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9013.1"
                     /db_xref="GeneID:4673"
                     /db_xref="HGNC:HGNC:7637"
                     /db_xref="MIM:164060"
ORIGIN      
        1 madidnkeqs eldqdlddve eveeeetgee tklkarqltv qmmqnpqila alqerldglv
       61 etptgyiesl prvvkrrvna lknlqvkcaq ieakfyeevh dlerkyavly qplfdkrfei
      121 inaiyeptee ecewkpdeed eiseelkeka kiedekkdee kedpkgipef wltvfknvdl
      181 lsdmvqehde pilkhlkdik vkfsdagqpm sfvlefhfep neyftnevlt ktyrmrsepd
      241 dsdpfsfdgp eimgctgcqi dwkkgknvtl ktikkkqkhk grgtvrtvtk tvsndsffnf
      301 fappevpesg dldddaeail aadfeighfl reriiprsvl yftgeaiedd dddydeegee
      361 adeegeeegd eendpdydpk kdqnpaeckq q
//
LOCUS       NP_839943               1631 aa            linear   PRI 27-APR-2025
DEFINITION  ras GTPase-activating-like protein IQGAP3 [Homo sapiens].
ACCESSION   NP_839943
VERSION     NP_839943.3
DBSOURCE    REFSEQ: accession NM_178229.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1631)
  AUTHORS   Tang,M., Zhang,S., Yang,M., Feng,R., Lin,J., Chen,X., Xu,Y., Yu,R.,
            Liao,X., Li,Z., Li,X., Li,M., Zhang,Q., Chen,S., Qian,W., Liu,Y.,
            Song,L. and Li,J.
  TITLE     Infiltrative Vessel Co-optive Growth Pattern Induced by IQGAP3
            Overexpression Promotes Microvascular Invasion in Hepatocellular
            Carcinoma
  JOURNAL   Clin Cancer Res 30 (10), 2206-2224 (2024)
   PUBMED   38470497
  REMARK    GeneRIF: Infiltrative Vessel Co-optive Growth Pattern Induced by
            IQGAP3 Overexpression Promotes Microvascular Invasion in
            Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 1631)
  AUTHORS   Zolotarenko,A. and Bruskin,S.
  TITLE     IQGAP3 Is an Important Mediator of Skin Inflammatory Diseases
  JOURNAL   Int J Mol Sci 25 (8), 4545 (2024)
   PUBMED   38674130
  REMARK    GeneRIF: IQGAP3 Is an Important Mediator of Skin Inflammatory
            Diseases.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1631)
  AUTHORS   Su,Z., Wang,Y., Cao,J., Ma,J., Wang,G., Ren,H., Zhang,Y., Sheng,K.,
            Zhu,X. and Wang,Y.
  TITLE     Identification and validation of non-coding RNA-mediated high
            expression of IQGAP3 in poor prognosis of lung adenocarcinoma
  JOURNAL   J Gene Med 26 (1), e3664 (2024)
   PUBMED   38282143
  REMARK    GeneRIF: Identification and validation of non-coding RNA-mediated
            high expression of IQGAP3 in poor prognosis of lung adenocarcinoma.
REFERENCE   4  (residues 1 to 1631)
  AUTHORS   Mei,W., Dong,Y., Gu,Y., Kapoor,A., Lin,X., Su,Y., Vega Neira,S. and
            Tang,D.
  TITLE     IQGAP3 is relevant to prostate cancer: A detailed presentation of
            potential pathomechanisms
  JOURNAL   J Adv Res 54, 195-210 (2023)
   PUBMED   36681115
  REMARK    GeneRIF: IQGAP3 is relevant to prostate cancer: A detailed
            presentation of potential pathomechanisms.
REFERENCE   5  (residues 1 to 1631)
  AUTHORS   Li,W., Wang,Z., Wang,H., Zhang,J., Wang,X., Xing,S. and Chen,S.
  TITLE     IQGAP3 in clear cell renal cell carcinoma contributes to drug
            resistance and genome stability
  JOURNAL   PeerJ 10, e14201 (2022)
   PUBMED   36275458
  REMARK    GeneRIF: IQGAP3 in clear cell renal cell carcinoma contributes to
            drug resistance and genome stability.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1631)
  AUTHORS   Adachi,M., Kawasaki,A., Nojima,H., Nishida,E. and Tsukita,S.
  TITLE     Involvement of IQGAP family proteins in the regulation of mammalian
            cell cytokinesis
  JOURNAL   Genes Cells 19 (11), 803-820 (2014)
   PUBMED   25229330
  REMARK    GeneRIF: Mammalian IQGAP proteins may play a role in cytokinesis by
            regulating the localization of key cytokinesis regulatory proteins
            to the contractile apparatus during mitosis.
REFERENCE   7  (residues 1 to 1631)
  AUTHORS   Yang,Y., Zhao,W., Xu,Q.W., Wang,X.S., Zhang,Y. and Zhang,J.
  TITLE     IQGAP3 promotes EGFR-ERK signaling and the growth and metastasis of
            lung cancer cells
  JOURNAL   PLoS One 9 (5), e97578 (2014)
   PUBMED   24849319
  REMARK    GeneRIF: IQGAP3 may contribute to the pathogenesis of lung cancer
            by modulating EGFR-ERK signaling
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1631)
  AUTHORS   Atcheson,E., Hamilton,E., Pathmanathan,S., Greer,B., Harriott,P.
            and Timson,D.J.
  TITLE     IQ-motif selectivity in human IQGAP2 and IQGAP3: binding of
            calmodulin and myosin essential light chain
  JOURNAL   Biosci Rep 31 (5), 371-379 (2011)
   PUBMED   21299499
  REMARK    GeneRIF: The first IQ-motifs from IQGAP2 and IQGAP3 form transient
            interactions with calmodulin in the absence of calcium.
REFERENCE   9  (residues 1 to 1631)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 1631)
  AUTHORS   Wang,S., Watanabe,T., Noritake,J., Fukata,M., Yoshimura,T.,
            Itoh,N., Harada,T., Nakagawa,M., Matsuura,Y., Arimura,N. and
            Kaibuchi,K.
  TITLE     IQGAP3, a novel effector of Rac1 and Cdc42, regulates neurite
            outgrowth
  JOURNAL   J Cell Sci 120 (Pt 4), 567-577 (2007)
   PUBMED   17244649
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL365181.24.
            
            On Nov 23, 2018 this sequence version replaced NP_839943.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB105103.1, BC131536.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361170.7/ ENSP00000354451.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1631
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1631
                     /product="ras GTPase-activating-like protein IQGAP3"
                     /calculated_mol_wt=184568
     Region          28..179
                     /region_name="CH_SF"
                     /note="calponin homology (CH) domain superfamily; cl00030"
                     /db_xref="CDD:469584"
     Site            order(40,101,103..104,107..108,110,124..128,134,136..137,
                     139..140,143..144,147)
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:409031"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKF1; propagated from
                     UniProtKB/Swiss-Prot (Q86VI3.2)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q86VI3.2)"
     Region          <734..>957
                     /region_name="COG5022"
                     /note="Myosin heavy chain [General function prediction
                     only]"
                     /db_xref="CDD:227355"
     Region          <861..1631
                     /region_name="IQG1"
                     /note="Protein involved in regulation of cellular
                     morphogenesis/cytokinesis [Cell division and chromosome
                     partitioning / Signal transduction mechanisms]; COG5261"
                     /db_xref="CDD:227586"
     Region          987..1336
                     /region_name="RasGAP_IQGAP3"
                     /note="Ras-GTPase Activating Domain of IQ motif containing
                     GTPase activating protein 3; cd12207"
                     /db_xref="CDD:213346"
     Site            order(1031,1062,1064,1066..1067,1070,1073,1077,1169,
                     1177..1178,1181..1182,1185,1210,1213..1214,1217,1221,1223,
                     1228..1229)
                     /site_type="other"
                     /note="putative RAS interface [polypeptide binding]"
                     /db_xref="CDD:213346"
     Site            1424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86VI3.2)"
     CDS             1..1631
                     /gene="IQGAP3"
                     /coded_by="NM_178229.5:37..4932"
                     /db_xref="CCDS:CCDS1144.1"
                     /db_xref="GeneID:128239"
                     /db_xref="HGNC:HGNC:20669"
                     /db_xref="MIM:621092"
ORIGIN      
        1 merraagpgw aayerltaee mdeqrrqnva yqylcrleea krwmeaclke elpspvelee
       61 slrngvllak lghcfapsvv plkkiydveq lryqatglhf rhtdninfwl saiahiglps
      121 tffpettdiy dkknmprvvy cihalslflf rlglapqihd lygkvkftae elsnmasela
      181 kyglqlpafs kiggilanel svdeaavhaa vlaineaver gvvedtlaal qnpsallenl
      241 replaavyqe mlaqakmeka anarnhddre sqdiydhylt qaeiqgninh vnvhgalevv
      301 ddalerqspe allkalqdpa lalrgvrrdf adwyleqlns dreqkaqelg lvellekeev
      361 qagvaaantk gdqeqamlha vqrinkairr rvaadtvkel mcpeaqlppv ypvassmyql
      421 elavlqqqqg elgqeelfva vemlsavvli nraleardas gfwsslvnpa tglaevegen
      481 aqryfdallk lrqergmged flswndlqat vsqvnaqtqe etdrvlavsl inealdkgsp
      541 ektlsalllp aaglddvslp vapryhlllv aakrqkaqvt gdpgavlwle eirqgvvran
      601 qdtntaqrma lgvaainqai kegkaaqter vlrnpavalr gvvpdcangy qralesamak
      661 kqrpadtafw vqhdmkdgta yyfhlqtfqg iweqppgcpl ntshltreei qsavtkvtaa
      721 ydrqqlwkan vgfviqlqar lrgflvrqkf aehshflrtw lpavikiqah wrgyrqrkiy
      781 lewlqyfkan ldaiikiqaw armwaarrqy lrrlhyfqkn vnsivkiqaf frarkaqddy
      841 rilvhaphpp lsvvrrfahl lnqsqqdfla eaellklqee vvrkirsnqq leqdlnimdi
      901 kigllvknri tlqevvshck kltkrnkeql sdmmvldkqk glkslskekr qkleayqhlf
      961 yllqtqpiyl aklifqmpqn kttkfmeavi fslynyassr reaylllqlf ktalqeeiks
     1021 kveqpqdvvt gnptvvrlvv rfyrngrgqs alqeilgkvi qdvledkvls vhtdpvhlyk
     1081 nwinqteaqt gqrshlpydv tpeqalshpe vqrrldialr nllamtdkfl laitssvdqi
     1141 pygmryvakv lkatlaekfp datdsevykv vgnllyyrfl npavvapdaf divamaagga
     1201 laapqrhalg avaqllqhaa agkafsgqsq hlrvlndyle ethlkfrkfi hracqvpepe
     1261 erfavdeysd mvavakpmvy itvgelvnth rlllehqdci apdhqdplhe lledlgelpt
     1321 ipdligesia adghtdlskl evsltltnkf egleadadds ntrslllstk qlladiiqfh
     1381 pgdtlkeils lsasreqeaa hkqlmsrrqa ctaqtpeplr rhrsltahsl lplaekqrrv
     1441 lrnlrrleal glvsarngyq glvdelakdi rnqhrhrhrr kaelvklqat lqglstkttf
     1501 yeeqgdyysq yiracldhla pdskssgkgk kqpslhytaa qllekgvlve iedlpashfr
     1561 nvifditpgd eagkfevnak flgvdmerfq lhyqdllqlq yegvavmklf nkakvnvnll
     1621 ifllnkkflr k
//
LOCUS       NP_009129                275 aa            linear   PRI 27-APR-2025
DEFINITION  pyridoxal phosphate homeostasis protein isoform 2 [Homo sapiens].
ACCESSION   NP_009129
VERSION     NP_009129.1
DBSOURCE    REFSEQ: accession NM_007198.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Ciapaite,J., van Roermund,C.W.T., Bosma,M., Gerrits,J.,
            Houten,S.M., IJlst,L., Waterham,H.R., van Karnebeek,C.D.M.,
            Wanders,R.J.A., Zwartkruis,F.J.T., Jans,J.J. and
            Verhoeven-Duif,N.M.
  TITLE     Maintenance of cellular vitamin B6 levels and mitochondrial
            oxidative function depend on pyridoxal 5'-phosphate homeostasis
            protein
  JOURNAL   J Biol Chem 299 (9), 105047 (2023)
   PUBMED   37451483
  REMARK    GeneRIF: Maintenance of cellular vitamin B6 levels and
            mitochondrial oxidative function depend on pyridoxal 5'-phosphate
            homeostasis protein.
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Plecko,B., Zweier,M., Begemann,A., Mathis,D., Schmitt,B.,
            Striano,P., Baethmann,M., Vari,M.S., Beccaria,F., Zara,F.,
            Crowther,L.M., Joset,P., Sticht,H., Papuc,S.M. and Rauch,A.
  TITLE     Confirmation of mutations in PROSC as a novel cause of vitamin B 6
            -dependent epilepsy
  JOURNAL   J Med Genet 54 (12), 809-814 (2017)
   PUBMED   28391250
  REMARK    GeneRIF: We therefore confirm PROSC as a novel gene for
            vitamin-B6-dependent epilepsy and delineate a non-specific plasma
            vitamin B6 profile under pyridoxine treatment.
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Tremino,L., Forcada-Nadal,A., Contreras,A. and Rubio,V.
  TITLE     Studies on cyanobacterial protein PipY shed light on structure,
            potential functions, and vitamin B6 -dependent epilepsy
  JOURNAL   FEBS Lett 591 (20), 3431-3442 (2017)
   PUBMED   28914444
  REMARK    GeneRIF: Exploiting the universality of the Synechococcus elongatus
            COG0325 (PiPY) functions, it has been used in site-directed
            mutagenesis studies to shed light on disease causation by
            epilepsy-associated mutations in the human COG0325 gene PROSC.
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Darin,N., Reid,E., Prunetti,L., Samuelsson,L., Husain,R.A.,
            Wilson,M., El Yacoubi,B., Footitt,E., Chong,W.K., Wilson,L.C.,
            Prunty,H., Pope,S., Heales,S., Lascelles,K., Champion,M.,
            Wassmer,E., Veggiotti,P., de Crecy-Lagard,V., Mills,P.B. and
            Clayton,P.T.
  TITLE     Mutations in PROSC Disrupt Cellular Pyridoxal Phosphate Homeostasis
            and Cause Vitamin-B6-Dependent Epilepsy
  JOURNAL   Am J Hum Genet 99 (6), 1325-1337 (2016)
   PUBMED   27912044
  REMARK    GeneRIF: studies suggest that PROSC is involved in intracellular
            homeostatic regulation of pyridoxal 5'-phosphate, supplying this
            cofactor to apoenzymes while minimizing any toxic side reactions
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Roessler,S., Long,E.L., Budhu,A., Chen,Y., Zhao,X., Ji,J.,
            Walker,R., Jia,H.L., Ye,Q.H., Qin,L.X., Tang,Z.Y., He,P.,
            Hunter,K.W., Thorgeirsson,S.S., Meltzer,P.S. and Wang,X.W.
  TITLE     Integrative genomic identification of genes on 8p associated with
            hepatocellular carcinoma progression and patient survival
  JOURNAL   Gastroenterology 142 (4), 957-966 (2012)
   PUBMED   22202459
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Bowling,F.G.
  TITLE     Pyridoxine supply in human development
  JOURNAL   Semin Cell Dev Biol 22 (6), 611-618 (2011)
   PUBMED   21664474
  REMARK    Review article
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Ikegawa,S., Isomura,M., Koshizuka,Y. and Nakamura,Y.
  TITLE     Cloning and characterization of human and mouse PROSC (proline
            synthetase co-transcribed) genes
  JOURNAL   J Hum Genet 44 (5), 337-342 (1999)
   PUBMED   10496079
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Al-Shekaili,H., Ciapaite,J., van Karnebeek,C. and Pena,I.
  TITLE     PLPBP Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36795901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012334.1, AL136616.1 and
            BM984988.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a pyridoxal 5'-phosphate binding protein
            involved in the homeostatic regulation of intracellular pyridoxal
            5'-phosphate. This gene has a tumor suppressive effect on
            hepatocellular carcinoma and other solid tumors of epithelial
            origin. Naturally occurring mutations in this gene are associated
            with a pyridoxine-dependent epilepsy. [provided by RefSeq, Mar
            2017].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region compared to variant 1. The encoded isoform
            (2) is shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012334.1, AK291135.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000328195.8/ ENSP00000333551.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.23"
     Protein         1..275
                     /product="pyridoxal phosphate homeostasis protein isoform
                     2"
                     /note="proline synthetase co-transcribed bacterial homolog
                     protein; proline synthase co-transcribed bacterial homolog
                     protein; PLP homeostasis protein; pyridoxal phosphate
                     homeostasis protein"
                     /calculated_mol_wt=30213
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94903.1)"
     Region          17..248
                     /region_name="PLPDE_III_YBL036c_euk"
                     /note="Pyridoxal 5-phosphate (PLP)-binding TIM barrel
                     domain of Type III PLP-Dependent Enzymes, Eukaryotic
                     YBL036c-like proteins; cd06822"
                     /db_xref="CDD:143496"
     Site            order(45,47,68,94,181,183,225..226,241..244)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143496"
     Site            47
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:143496"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2Y8; propagated from
                     UniProtKB/Swiss-Prot (O94903.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94903.1)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94903.1)"
     Region          251..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94903.1)"
     CDS             1..275
                     /gene="PLPBP"
                     /gene_synonym="EPEO1; EPVB6D; PROSC"
                     /coded_by="NM_007198.4:16..843"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6096.1"
                     /db_xref="GeneID:11212"
                     /db_xref="HGNC:HGNC:9457"
                     /db_xref="MIM:604436"
ORIGIN      
        1 mwragsmsae lgvgcalrav nervqqavar rprdlpaiqp rlvavsktkp admvieaygh
       61 gqrtfgenyv qellekasnp kilslcpeik whfighlqkq nvnklmavpn lfmletvdsv
      121 kladkvnssw qrkgsperlk vmvqintsge eskhglppse tiaivehina kcpnlefvgl
      181 mtigsfghdl sqgpnpdfql llslreelck klnipadqve lsmgmsadfq havevgstnv
      241 rigstifger dyskkptpdk caadvkaple vaqeh
//
LOCUS       NP_001351626             293 aa            linear   ROD 27-APR-2025
DEFINITION  triadin isoform 3 [Mus musculus].
ACCESSION   NP_001351626
VERSION     NP_001351626.1
DBSOURCE    REFSEQ: accession NM_001364697.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Zhao,Y., Riching,A.S., Knight,W.E., Chi,C., Broadwell,L.J., Du,Y.,
            Abdel-Hafiz,M., Ambardekar,A.V., Irwin,D.C., Proenza,C., Xu,H.,
            Leinwand,L.A., Walker,L.A., Woulfe,K.C., Bristow,M.R.,
            Buttrick,P.M. and Song,K.
  TITLE     Cardiomyocyte-Specific Long Noncoding RNA Regulates Alternative
            Splicing of the Triadin Gene in the Heart
  JOURNAL   Circulation 146 (9), 699-714 (2022)
   PUBMED   35862102
  REMARK    GeneRIF: Cardiomyocyte-Specific Long Noncoding RNA Regulates
            Alternative Splicing of the Triadin Gene in the Heart.
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Manno,C., Tammineni,E., Figueroa,L., Marty,I. and Rios,E.
  TITLE     Quantification of the calcium signaling deficit in muscles devoid
            of triadin
  JOURNAL   PLoS One 17 (2), e0264146 (2022)
   PUBMED   35213584
  REMARK    GeneRIF: Quantification of the calcium signaling deficit in muscles
            devoid of triadin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Seo,M.H., Lim,S. and Yeo,S.
  TITLE     Association of decreased triadin expression level with apoptosis of
            dopaminergic cells in Parkinson's disease mouse model
  JOURNAL   BMC Neurosci 22 (1), 65 (2021)
   PUBMED   34736417
  REMARK    GeneRIF: Association of decreased triadin expression level with
            apoptosis of dopaminergic cells in Parkinson's disease mouse model.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Sebastien,M., Aubin,P., Brocard,J., Brocard,J., Marty,I. and
            Faure,J.
  TITLE     Dynamics of triadin, a muscle-specific triad protein, within
            sarcoplasmic reticulum subdomains
  JOURNAL   Mol Biol Cell 31 (4), 261-272 (2020)
   PUBMED   31877066
  REMARK    GeneRIF: Dynamics of triadin, a muscle-specific triad protein,
            within sarcoplasmic reticulum subdomains.
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Zhang,L., Salgado-Somoza,A., Vausort,M., Leszek,P. and Devaux,Y.
  CONSRTM   Cardiolinctrade mark network. Electronic address:
            https://www.cardiolinc.org
  TITLE     A heart-enriched antisense long non-coding RNA regulates the
            balance between cardiac and skeletal muscle triadin
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1865 (2), 247-258 (2018)
   PUBMED   29126880
  REMARK    GeneRIF: The lncRNA TRDN-AS regulates the balance between cardiac
            and skeletal isoforms of triadin.
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Arvanitis,D.A., Vafiadaki,E., Fan,G.C., Mitton,B.A., Gregory,K.N.,
            Del Monte,F., Kontrogianni-Konstantopoulos,A., Sanoudou,D. and
            Kranias,E.G.
  TITLE     Histidine-rich Ca-binding protein interacts with sarcoplasmic
            reticulum Ca-ATPase
  JOURNAL   Am J Physiol Heart Circ Physiol 293 (3), H1581-H1589 (2007)
   PUBMED   17526652
  REMARK    GeneRIF: Histidine-rich Ca-binding protein may play a key role in
            the regulation of SR Ca cycling through its direct interactions
            with SERCA2 and triadin, mediating a fine cross talk between SR Ca
            uptake and release in the heart.
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Kirchhof,P., Klimas,J., Fabritz,L., Zwiener,M., Jones,L.R.,
            Schafers,M., Hermann,S., Boknik,P., Schmitz,W., Breithardt,G.,
            Kirchhefer,U. and Neumann,J.
  TITLE     Stress and high heart rate provoke ventricular tachycardia in mice
            expressing triadin
  JOURNAL   J Mol Cell Cardiol 42 (5), 962-971 (2007)
   PUBMED   17408688
  REMARK    GeneRIF: Triadin(TRD)xjunctin(JCN) mice were studied to compensate
            the down-regulation of junctin expression in triadin-expressing
            mice; exercise or stress provoked repetitive ventricular
            tachycardia in freely roaming TRDxJCN mice.
REFERENCE   8  (residues 1 to 293)
  AUTHORS   Hong,S., Kim,T.W., Choi,I., Woo,J.M., Oh,J., Park,W.J., Kim,D.H.
            and Cho,C.
  TITLE     Complementary DNA cloning, genomic characterization and expression
            analysis of a mammalian gene encoding histidine-rich calcium
            binding protein
  JOURNAL   Biochim Biophys Acta 1727 (3), 188-196 (2005)
   PUBMED   15777620
REFERENCE   9  (residues 1 to 293)
  AUTHORS   Kirchhefer,U., Baba,H.A., Kobayashi,Y.M., Jones,L.R., Schmitz,W.
            and Neumann,J.
  TITLE     Altered function in atrium of transgenic mice overexpressing
            triadin 1
  JOURNAL   Am J Physiol Heart Circ Physiol 283 (4), H1334-H1343 (2002)
   PUBMED   12234783
  REMARK    GeneRIF: triadin 1 overexpression triggered time-dependent
            alterations in SR protein expression, Ca(2+) homeostasis, and
            contractility, indicating for the first time an inhibitory function
            of triadin 1 on SR-Ca(2+) release in vivo.
REFERENCE   10 (residues 1 to 293)
  AUTHORS   Hong,C.S., Ji,J.H., Kim,J.P., Jung,D.H. and Kim,D.H.
  TITLE     Molecular cloning and characterization of mouse cardiac triadin
            isoforms
  JOURNAL   Gene 278 (1-2), 193-199 (2001)
   PUBMED   11707337
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC153965.4 and AC157017.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF223416.1, SRR5189679.119112.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164133, SAMN01766820
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 18.37 cM"
     Protein         1..293
                     /product="triadin isoform 3"
                     /note="cardiac triadin"
                     /calculated_mol_wt=32959
     Region          45..>74
                     /region_name="Asp-B-Hydro_N"
                     /note="Aspartyl beta-hydroxylase N-terminal region;
                     pfam05279"
                     /db_xref="CDD:428406"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9Q9K5.1)"
     Region          117..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9Q9K5.1)"
     CDS             1..293
                     /gene="Trdn"
                     /gene_synonym="2310045H21Rik; EG432451; TDN"
                     /coded_by="NM_001364697.1:219..1100"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS87985.1"
                     /db_xref="GeneID:76757"
                     /db_xref="MGI:MGI:1924007"
ORIGIN      
        1 mteitaegna sttttvidnk ngcipkspgk vlkrsvtedi vttfsspaaw llvialiitw
       61 savaivmfdl vdyknfsass iakigsdplk lvndaveett dwiygffsll sdiissegde
      121 ddedadedid kgeieepplk rkeihqekae keekpekkiq tkashrerek gkeklkgekp
      181 ektathkekl ekkerpetkm makedkkikt kekteekakk emkvgkqekv kptaakaket
      241 pktppkarkk ddkempavhe qkdqyafcry midmfvhgdl kpgipnnsyc cls
//
LOCUS       NP_001355825             628 aa            linear   PRI 27-APR-2025
DEFINITION  collagen alpha-1(XIII) chain isoform 29 [Homo sapiens].
ACCESSION   NP_001355825 XP_016871183
VERSION     NP_001355825.1
DBSOURCE    REFSEQ: accession NM_001368896.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Kim,H., Choi,N., Kim,D.Y., Kim,S.Y., Song,S.Y. and Sung,J.H.
  TITLE     TGF-beta2 and collagen play pivotal roles in the spheroid formation
            and anti-aging of human dermal papilla cells
  JOURNAL   Aging (Albany NY) 13 (16), 19978-19995 (2021)
   PUBMED   34404755
  REMARK    GeneRIF: TGF-beta2 and collagen play pivotal roles in the spheroid
            formation and anti-aging of human dermal papilla cells.
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Koivunen,J., Kemppainen,A.V., Finnila,M.A., Keski-Filppula,R.,
            Haronen,H., Tu,H., Pellikka,H., Heikkinen,A., Kylmaoja,E.,
            Sormunen,R., Miinalainen,I., Saarakkala,S., Izzi,V. and
            Pihlajaniemi,T.
  TITLE     Collagen XIII-derived ectodomain regulates bone angiogenesis and
            intracortical remodeling
  JOURNAL   Matrix Biol 83, 6-25 (2019)
   PUBMED   31220558
  REMARK    GeneRIF: Data suggest that ColXIII has a role in age-dependent
            cortical bone deterioration with possible implications for
            osteoporosis and fracture risk.
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Rodriguez Cruz,P.M., Cossins,J., Estephan,E.P., Munell,F.,
            Selby,K., Hirano,M., Maroofin,R., Mehrjardi,M.Y.V., Chow,G.,
            Carr,A., Manzur,A., Robb,S., Munot,P., Wei Liu,W., Banka,S.,
            Fraser,H., De Goede,C., Zanoteli,E., Conti Reed,U., Sage,A.,
            Gratacos,M., Macaya,A., Dusl,M., Senderek,J., Topf,A., Hofer,M.,
            Knight,R., Ramdas,S., Jayawant,S., Lochmuller,H., Palace,J. and
            Beeson,D.
  TITLE     The clinical spectrum of the congenital myasthenic syndrome
            resulting from COL13A1 mutations
  JOURNAL   Brain 142 (6), 1547-1560 (2019)
   PUBMED   31081514
  REMARK    GeneRIF: patients with COL13A1 mutations present mostly with severe
            early-onset myasthenic syndrome with feeding and breathing
            difficulties
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Juvonen,M., Sandberg,M. and Pihlajaniemi,T.
  TITLE     Patterns of expression of the six alternatively spliced exons
            affecting the structures of the COL1 and NC2 domains of the alpha
            1(XIII) collagen chain in human tissues and cell lines
  JOURNAL   J Biol Chem 267 (34), 24700-24707 (1992)
   PUBMED   1447210
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Juvonen,M. and Pihlajaniemi,T.
  TITLE     Characterization of the spectrum of alternative splicing of alpha 1
            (XIII) collagen transcripts in HT-1080 cells and calvarial tissue
            resulted in identification of two previously unidentified
            alternatively spliced sequences, one previously unidentified exon,
            and nine new mRNA variants
  JOURNAL   J Biol Chem 267 (34), 24693-24699 (1992)
   PUBMED   1447209
REFERENCE   7  (residues 1 to 628)
  AUTHORS   Tikka,L., Elomaa,O., Pihlajaniemi,T. and Tryggvason,K.
  TITLE     Human alpha 1 (XIII) collagen gene. Multiple forms of the gene
            transcripts are generated through complex alternative splicing of
            several short exons
  JOURNAL   J Biol Chem 266 (26), 17713-17719 (1991)
   PUBMED   1894651
REFERENCE   8  (residues 1 to 628)
  AUTHORS   Pihlajaniemi,T. and Tamminen,M.
  TITLE     The alpha 1 chain of type XIII collagen consists of three
            collagenous and four noncollagenous domains, and its primary
            transcript undergoes complex alternative splicing
  JOURNAL   J Biol Chem 265 (28), 16922-16928 (1990)
   PUBMED   1698771
REFERENCE   9  (residues 1 to 628)
  AUTHORS   Shows,T.B., Tikka,L., Byers,M.G., Eddy,R.L., Haley,L.L.,
            Henry,W.M., Prockop,D.J. and Tryggvason,K.
  TITLE     Assignment of the human collagen alpha 1 (XIII) chain gene
            (COL13A1) to the q22 region of chromosome 10
  JOURNAL   Genomics 5 (1), 128-133 (1989)
   PUBMED   2767682
REFERENCE   10 (residues 1 to 628)
  AUTHORS   Tikka,L., Pihlajaniemi,T., Henttu,P., Prockop,D.J. and
            Tryggvason,K.
  TITLE     Gene structure for the alpha 1 chain of a human short-chain
            collagen (type XIII) with alternatively spliced transcripts and
            translation termination codon at the 5' end of the last exon
  JOURNAL   Proc Natl Acad Sci U S A 85 (20), 7491-7495 (1988)
   PUBMED   2459707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC025426.11, AL138925.17 and
            AC024601.9.
            
            On Mar 7, 2019 this sequence version replaced XP_016871183.1.
            
            Summary: This gene encodes the alpha chain of one of the
            nonfibrillar collagens. The function of this gene product is not
            known, however, it has been detected at low levels in all
            connective tissue-producing cells so it may serve a general
            function in connective tissues. Unlike most of the collagens, which
            are secreted into the extracellular matrix, collagen XIII contains
            a transmembrane domain and the protein has been localized to the
            plasma membrane. The transcripts for this gene undergo complex and
            extensive splicing involving at least eight exons. Like other
            collagens, collagen XIII is a trimer; it is not known whether this
            trimer is composed of one or more than one alpha chain isomer. A
            number of alternatively spliced transcript variants have been
            described, but the full length nature of some of them has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.191528.1,
                                           SRR3476690.306759.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155550, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..628
                     /product="collagen alpha-1(XIII) chain isoform 29"
                     /note="collagen alpha-1(XIII) chain; collagen, type XIII,
                     alpha 1"
                     /calculated_mol_wt=61425
     Region          <131..>383
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <358..>605
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     CDS             1..628
                     /gene="COL13A1"
                     /gene_synonym="CMS19; COLXIIIA1"
                     /coded_by="NM_001368896.1:519..2405"
                     /note="isoform 29 is encoded by transcript variant 29"
                     /db_xref="CCDS:CCDS91254.1"
                     /db_xref="GeneID:1305"
                     /db_xref="HGNC:HGNC:2190"
                     /db_xref="MIM:120350"
ORIGIN      
        1 mvaerthkaa atgargpgel gapgtvalva araergarlp spgscglltl alcslalsll
       61 ahfrtaelqa rvlrleaerg eqqmetailg rvnqlldekw klhsrrrrea pktspgcncp
      121 pgppgqpgtr gfpgfpgpig ldgkpghpgp kgdmgltgpp gqpgpqgqkg ekgqcgeyph
      181 rllpllnsvr lapppvikrr tfqgeqsqas iqgppgppgp pgpsgplghp glpgpmgppg
      241 lpgppgpkgd pgiqgyhgrk gergmpgmpg khgakgapgi avagmkgepg ipgtkgekga
      301 egspglpgll gqkgekgdag nsigggrgep gppglpgppg pkgeagvdgq vgppgqpgdk
      361 gergaageqg pdgpkgskge pgkgemvdyn gninealqei rtlalmgppg lpgqigppga
      421 pgipgqkgei glpgppghdg ekgprgkpgd mgppgpqgpp gkdgppgvkg enghpgspge
      481 kgekgetgqa gspglqgvpg pkgeagldga kgekgfqgek gdrgplglpg asgldgrpgp
      541 pgtpgpigvp gpagpkgerg skgdpgmtgp tgaaglpglh gppgdkgnrg hrgfkgekge
      601 pglpgldgld apcplgedgl pvqgcwnk
//
LOCUS       NP_001193770             453 aa            linear   PRI 27-APR-2025
DEFINITION  trans-Golgi network integral membrane protein 2 isoform 3 precursor
            [Homo sapiens].
ACCESSION   NP_001193770
VERSION     NP_001193770.1
DBSOURCE    REFSEQ: accession NM_001206841.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Gerashchenko,T., Skitchenko,R., Korobeynikova,A., Kuanysheva,K.,
            Khozyainova,A., Vorobiev,R., Rodionov,E., Miller,S.,
            Topolnitsky,E., Shefer,N., Anisimenko,M., Zhuikova,L., Vashisth,M.,
            Pankova,O., Perelmuter,V., Rezapova,V., Artomov,M. and Denisov,E.
  TITLE     Whole-exome sequencing reveals an association of rs112065068 in
            TGOLN2 gene with distant metastasis of non-small cell lung cancer
  JOURNAL   Gene 920, 148507 (2024)
   PUBMED   38670394
  REMARK    GeneRIF: Whole-exome sequencing reveals an association of
            rs112065068 in TGOLN2 gene with distant metastasis of non-small
            cell lung cancer.
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Lujan,P., Garcia-Cabau,C., Wakana,Y., Vera Lillo,J.,
            Rodilla-Ramirez,C., Sugiura,H., Malhotra,V., Salvatella,X.,
            Garcia-Parajo,M.F. and Campelo,F.
  TITLE     Sorting of secretory proteins at the trans-Golgi network by human
            TGN46
  JOURNAL   Elife 12, 91708 (2024)
   PUBMED   38466628
  REMARK    GeneRIF: Sorting of secretory proteins at the trans-Golgi network
            by human TGN46.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Liang,X.H., Nichols,J.G., De Hoyos,C.L., Sun,H., Zhang,L. and
            Crooke,S.T.
  TITLE     Golgi-58K can re-localize to late endosomes upon cellular uptake of
            PS-ASOs and facilitates endosomal release of ASOs
  JOURNAL   Nucleic Acids Res 49 (14), 8277-8293 (2021)
   PUBMED   34244781
  REMARK    GeneRIF: Golgi-58K can re-localize to late endosomes upon cellular
            uptake of PS-ASOs and facilitates endosomal release of ASOs.
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Yeaman,C., Ayala,M.I., Wright,J.R., Bard,F., Bossard,C., Ang,A.,
            Maeda,Y., Seufferlein,T., Mellman,I., Nelson,W.J. and Malhotra,V.
  TITLE     Protein kinase D regulates basolateral membrane protein exit from
            trans-Golgi network
  JOURNAL   Nat Cell Biol 6 (2), 106-112 (2004)
   PUBMED   14743217
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Wang,J. and Howell,K.E.
  TITLE     The luminal domain of TGN38 interacts with integrin beta 1 and is
            involved in its trafficking
  JOURNAL   Traffic 1 (9), 713-723 (2000)
   PUBMED   11208159
REFERENCE   7  (residues 1 to 453)
  AUTHORS   Stephens,D.J. and Banting,G.
  TITLE     Direct interaction of the trans-Golgi network membrane protein,
            TGN38, with the F-actin binding protein, neurabin
  JOURNAL   J Biol Chem 274 (42), 30080-30086 (1999)
   PUBMED   10514494
REFERENCE   8  (residues 1 to 453)
  AUTHORS   Stephens,D.J. and Banting,G.
  TITLE     Specificity of interaction between adaptor-complex medium chains
            and the tyrosine-based sorting motifs of TGN38 and lgp120
  JOURNAL   Biochem J 335 (Pt 3) (Pt 3), 567-572 (1998)
   PUBMED   9794796
REFERENCE   9  (residues 1 to 453)
  AUTHORS   Kain,R., Angata,K., Kerjaschki,D. and Fukuda,M.
  TITLE     Molecular cloning and expression of a novel human trans-Golgi
            network glycoprotein, TGN51, that contains multiple
            tyrosine-containing motifs
  JOURNAL   J Biol Chem 273 (2), 981-988 (1998)
   PUBMED   9422759
REFERENCE   10 (residues 1 to 453)
  AUTHORS   Ponnambalam,S., Girotti,M., Yaspo,M.L., Owen,C.E., Perry,A.C.,
            Suganuma,T., Nilsson,T., Fried,M., Banting,G. and Warren,G.
  TITLE     Primate homologues of rat TGN38: primary structure, expression and
            functional implications
  JOURNAL   J Cell Sci 109 (Pt 3), 675-685 (1996)
   PUBMED   8907712
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL710137.1, BC008461.1,
            BY798185.2, AC093162.5 and AA723637.1.
            
            Summary: This gene encodes a type I integral membrane protein that
            is localized to the trans-Golgi network, a major sorting station
            for secretory and membrane proteins. The encoded protein cycles
            between early endosomes and the trans-Golgi network, and may play a
            role in exocytic vesicle formation. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (3, A allele) uses an alternate
            splice site in the 3' coding region, which results in a frameshift,
            compared to variant 1. The encoded isoform (3) has a longer and
            distinct C-terminus, compared to isoform 1. This variant (3, A
            allele) differs at 1 nt position compared to variant 3, B allele.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF027515.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..453
                     /product="trans-Golgi network integral membrane protein 2
                     isoform 3 precursor"
                     /note="trans-Golgi network integral membrane protein 2;
                     TGN38 homolog; trans-Golgi network protein TGN51;
                     trans-Golgi network glycoprotein 46; trans-Golgi network
                     glycoprotein 48; trans-Golgi network glycoprotein 51"
                     /calculated_mol_wt=46061
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1715
     mat_peptide     18..453
                     /product="trans-Golgi network integral membrane protein 2
                     isoform 3"
                     /calculated_mol_wt=46061
     Region          27..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43493.4)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Region          <44..383
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          54..249
                     /region_name="14 X 14 AA tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (O43493.4)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43493.4)"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            96
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            180
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            208
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            373
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            377
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43493.4)"
     Site            382..402
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43493.4)"
     Region          395..398
                     /region_name="Endocytosis signal, in isoform TGN51"
                     /note="propagated from UniProtKB/Swiss-Prot (O43493.4)"
     Region          418..421
                     /region_name="Endocytosis signal, in isoform TGN51"
                     /note="propagated from UniProtKB/Swiss-Prot (O43493.4)"
     Region          430..433
                     /region_name="Endocytosis signal, in isoform TGN46 and
                     isoform TGN48"
                     /note="propagated from UniProtKB/Swiss-Prot (O43493.4)"
     CDS             1..453
                     /gene="TGOLN2"
                     /gene_synonym="hTGN46; hTGN48; hTGN51; TGN38; TGN46;
                     TGN48; TGN51; TTGN2"
                     /coded_by="NM_001206841.2:28..1389"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3, A allele"
                     /db_xref="GeneID:10618"
                     /db_xref="HGNC:HGNC:15450"
                     /db_xref="MIM:603062"
ORIGIN      
        1 mrfvvalvll nvaaagavpl latesvkqee agvrpsagnv sthpslsqrp ggstkshpep
       61 qtpkdspsks saeaqtpedt pnksgaeakt qkdssnksga eaktqkgsts ksgseaqttk
      121 dstskshpel qtpkdstgks gaeaqtpeds pnrsgaeakt qkdspsksgs eaqttkdvpn
      181 ksgadgqtpk dgssksgaed qtpkdvpnks gaekqtpkdg snksgaeeqg pidgpsksga
      241 eeqtskdspn kvvpeqpsrk dhskpisnps dnkelpkadt nqladkgkls phafktesge
      301 etdlisppqe evkssepted vepkeaeddd tgpeegsppk eekekmsgsa ssenregtls
      361 dstgsekddl ypngsgngsa esshffaylv taailvavly iahhnkrkii afvlegkrsk
      421 vtrrpkasdy qrldqkiffp pspnrmvyss gkr
//
LOCUS       NP_077819                538 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein with KRAB and SCAN domains 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_077819
VERSION     NP_077819.2
DBSOURCE    REFSEQ: accession NM_024493.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Nonoyama,K., Matsuo,Y., Sugita,S., Eguchi,Y., Denda,Y., Murase,H.,
            Kato,T., Imafuji,H., Saito,K., Morimoto,M., Ogawa,R., Takahashi,H.,
            Mitsui,A., Kimura,M. and Takiguchi,S.
  TITLE     Expression of ZKSCAN3 protein suppresses proliferation, migration,
            and invasion of pancreatic cancer through autophagy
  JOURNAL   Cancer Sci 115 (6), 1964-1978 (2024)
   PUBMED   38671550
  REMARK    GeneRIF: Expression of ZKSCAN3 protein suppresses proliferation,
            migration, and invasion of pancreatic cancer through autophagy.
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Li,X.M., Wen,J.H., Feng,Z.S., Wu,Y.S., Li,D.Y., Liang,S., Wu,D.,
            Wu,H.L., Li,S.M., Ye,Z.N., Yang,C., Sun,L., Tang,J.X. and Liu,H.F.
  TITLE     Effect of Lacking ZKSCAN3 on Autophagy, Lysosomal Biogenesis and
            Senescence
  JOURNAL   Int J Mol Sci 24 (9), 7786 (2023)
   PUBMED   37175493
  REMARK    GeneRIF: Effect of Lacking ZKSCAN3 on Autophagy, Lysosomal
            Biogenesis and Senescence.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Yang,Z., Lemacon,D.S., Li,S., Cheruiyot,A., Kong,L., Tan,K.,
            Cheng,C., Turkay,E., He,D. and You,Z.
  TITLE     Context-dependent pro- and anti-resection roles of ZKSCAN3 in the
            regulation of fork processing during replication stress
  JOURNAL   J Biol Chem 298 (8), 102215 (2022)
   PUBMED   35779634
  REMARK    GeneRIF: Context-dependent pro- and anti-resection roles of ZKSCAN3
            in the regulation of fork processing during replication stress.
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Zhang,X., Bai,Y., Huang,L., Liu,S., Mo,Y., Cheng,W., Wang,G.,
            Cao,Z., Chen,X., Cui,H., Qi,L., Ma,L., Liu,M., Guan,X.Y. and
            Ma,N.F.
  TITLE     CHD1L augments autophagy-mediated migration of hepatocellular
            carcinoma through targeting ZKSCAN3
  JOURNAL   Cell Death Dis 12 (10), 950 (2021)
   PUBMED   34654797
  REMARK    GeneRIF: CHD1L augments autophagy-mediated migration of
            hepatocellular carcinoma through targeting ZKSCAN3.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Pan,H.Y. and Valapala,M.
  TITLE     Role of the Transcriptional Repressor Zinc Finger with KRAB and
            SCAN Domains 3 (ZKSCAN3) in Retinal Pigment Epithelial Cells
  JOURNAL   Cells 10 (10), 2504 (2021)
   PUBMED   34685484
  REMARK    GeneRIF: Role of the Transcriptional Repressor Zinc Finger with
            KRAB and SCAN Domains 3 (ZKSCAN3) in Retinal Pigment Epithelial
            Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Yang,L., Zhang,L., Wu,Q. and Boyd,D.D.
  TITLE     Unbiased screening for transcriptional targets of ZKSCAN3
            identifies integrin beta 4 and vascular endothelial growth factor
            as downstream targets
  JOURNAL   J Biol Chem 283 (50), 35295-35304 (2008)
   PUBMED   18940803
  REMARK    GeneRIF: ZKSCAN3 regulates the expression of several genes favoring
            tumor progression including integrin beta 4 and VEGF
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Yang,L., Hamilton,S.R., Sood,A., Kuwai,T., Ellis,L., Sanguino,A.,
            Lopez-Berestein,G. and Boyd,D.D.
  TITLE     The previously undescribed ZKSCAN3 (ZNF306) is a novel 'driver' of
            colorectal cancer progression
  JOURNAL   Cancer Res 68 (11), 4321-4330 (2008)
   PUBMED   18519692
  REMARK    GeneRIF: ZKSCAN3 adds to an expanding set of encoded products
            contributing to the progression of colorectal cancer
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Wang,H., Yang,L., Jamaluddin,M.S. and Boyd,D.D.
  TITLE     The Kruppel-like KLF4 transcription factor, a novel regulator of
            urokinase receptor expression, drives synthesis of this binding
            site in colonic crypt luminal surface epithelial cells
  JOURNAL   J Biol Chem 279 (21), 22674-22683 (2004)
   PUBMED   15031282
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Petroni,D., Bartolini,E., Chiaramonte,R., Ottolenghi,S. and Comi,P.
  TITLE     Computer sequence analysis of human highly conserved zinc finger
            modules
  JOURNAL   DNA Seq 9 (3), 163-169 (1998)
   PUBMED   10520746
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA440043.1, BC006118.1, AL021997.1 and AL358785.10.
            
            On Apr 2, 2008 this sequence version replaced NP_077819.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.54547.1,
                                           SRR1803611.56846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252211.7/ ENSP00000252211.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..538
                     /product="zinc finger protein with KRAB and SCAN domains 3
                     isoform 1"
                     /note="zinc finger protein 306; zinc finger protein zfp47;
                     zinc finger protein 309; zinc finger protein with KRAB and
                     SCAN domains 3; zinc finger protein 47 homolog; zinc
                     finger and SCAN domain-containing protein 13"
                     /calculated_mol_wt=60510
     Region          42..154
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91VW9; propagated from
                     UniProtKB/Swiss-Prot (Q9BRR0.2)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BRR0.2)"
     Region          214..274
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          226..274
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRR0.2)"
     Region          314..336
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          316..336
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          329..351
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          342..364
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          344..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <368..515
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(377,379,381,383..384,387..388,391,405,407,411..412,
                     415..416,419,433,435,437,439..440,443..444,447)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          400..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          428..448
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BRR0.2)"
     Region          482..502
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          508..530
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          510..530
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..538
                     /gene="ZKSCAN3"
                     /gene_synonym="dJ874C20.1; dJ874C20.1.; ZF47; zfp-47;
                     ZFP306; Zfp47; ZNF306; ZNF309; ZSCAN13; ZSCAN35"
                     /coded_by="NM_024493.4:184..1800"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4650.1"
                     /db_xref="GeneID:80317"
                     /db_xref="HGNC:HGNC:13853"
                     /db_xref="MIM:612791"
ORIGIN      
        1 marelsesta ldaqstedqm ellvikveee eagfpsspdl gsegsrerfr gfrypeaagp
       61 realsrlrel crqwlqpemh skeqilellv leqfltilpg nlqswvreqh pesgeevvvl
      121 leylerqlde papqvsgvdq gqellcckma lltpapgsqs sqfqlmkall khesvgsqpl
      181 qdrvlqvpvl ahggccredk vvasrltpes qgllkvedva ltltpewtqq dssqgnlcrd
      241 ekqenhgslv slgdekqtks rdlppaeelp ekehgkisch lrediaqipt caeageqegr
      301 lqrkqknatg grrhichecg ksfaqssgls khrrihtgek pyeceecgka figssalvih
      361 qrvhtgekpy eceecgkafs hssdlikhqr thtgekpyec ddcgktfsqs csllehhrih
      421 tgekpyqcsm cgkafrrssh llrhqrihtg dknvqepeqg eawksrmesq lenvetpmsy
      481 kcnecersft qntgliehqk ihtgekpyqc nacgkgftri sylvqhqrsh vgknilsq
//
LOCUS       NP_001357305             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357305 XP_016881646
VERSION     NP_001357305.1
DBSOURCE    REFSEQ: accession NM_001370376.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            On May 7, 2019 this sequence version replaced XP_016881646.1.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.151468.1,
                                           SRR1660807.21639.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370376.1:1624..3273"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_001352080             686 aa            linear   ROD 27-APR-2025
DEFINITION  dihydropyrimidinase-related protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001352080 XP_006251146
VERSION     NP_001352080.1
DBSOURCE    REFSEQ: accession NM_001365151.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Zhang,J., Li,X., Zhang,Z., Zhang,J., Ma,L., Wang,S., Guo,X., Li,H.,
            Pan,B. and Niu,Q.
  TITLE     Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced PC12 cells
            necroptosis
  JOURNAL   Ecotoxicol Environ Saf 270, 115860 (2024)
   PUBMED   38142589
  REMARK    GeneRIF: Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced
            PC12 cells necroptosis.
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Liu,Y. and Xu,Y.J.
  TITLE     LKB1 and CRMP1 cooperatively promote the repair of the sciatic
            nerve injury
  JOURNAL   Dev Neurobiol 84 (1), 18-31 (2024)
   PUBMED   38105470
  REMARK    GeneRIF: LKB1 and CRMP1 cooperatively promote the repair of the
            sciatic nerve injury.
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Cruz Hernandez,J.H., Rosado Loman,W.N., Gomez-Crisostomo,N.P., De
            la Cruz-Hernandez,E.N., Guzman Garcia,L.M., Gomez Gomez,M.,
            Hernandez Del Angel,N.A., Aguilar Gamas,C.F., Cruz Hernandez,V.S.
            and Martinez-Abundis,E.
  TITLE     High sugar but not high fat diet consumption induces hepatic
            metabolic disruption and up-regulation of mitochondrial
            fission-associated protein Drp1 in a model of moderate obesity
  JOURNAL   Arch Physiol Biochem 129 (1), 233-240 (2023)
   PUBMED   32880477
  REMARK    GeneRIF: High sugar but not high fat diet consumption induces
            hepatic metabolic disruption and up-regulation of mitochondrial
            fission-associated protein Drp1 in a model of moderate obesity.
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Chua,J.Y., Ng,S.J., Yagensky,O., Wanker,E.E. and Chua,J.J.E.
  TITLE     FEZ1 Forms Complexes with CRMP1 and DCC to Regulate Axon and
            Dendrite Development
  JOURNAL   eNeuro 8 (2) (2021)
   PUBMED   33771901
  REMARK    GeneRIF: FEZ1 Forms Complexes with CRMP1 and DCC to Regulate Axon
            and Dendrite Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Nakamura,F., Kumeta,K., Hida,T., Isono,T., Nakayama,Y.,
            Kuramata-Matsuoka,E., Yamashita,N., Uchida,Y., Ogura,K.,
            Gengyo-Ando,K., Mitani,S., Ogino,T. and Goshima,Y.
  TITLE     Amino- and carboxyl-terminal domains of Filamin-A interact with
            CRMP1 to mediate Sema3A signalling
  JOURNAL   Nat Commun 5, 5325 (2014)
   PUBMED   25358863
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Chen,T.C., Lee,S.A., Hong,T.M., Shih,J.Y., Lai,J.M., Chiou,H.Y.,
            Yang,S.C., Chan,C.H., Kao,C.Y., Yang,P.C. and Huang,C.Y.
  TITLE     From midbody protein-protein interaction network construction to
            novel regulators in cytokinesis
  JOURNAL   J Proteome Res 8 (11), 4943-4953 (2009)
   PUBMED   19799413
REFERENCE   7  (residues 1 to 686)
  AUTHORS   Bevers,M.B., Lawrence,E., Maronski,M., Starr,N., Amesquita,M. and
            Neumar,R.W.
  TITLE     Knockdown of m-calpain increases survival of primary hippocampal
            neurons following NMDA excitotoxicity
  JOURNAL   J Neurochem 108 (5), 1237-1250 (2009)
   PUBMED   19141074
REFERENCE   8  (residues 1 to 686)
  AUTHORS   Bretin,S., Reibel,S., Charrier,E., Maus-Moatti,M., Auvergnon,N.,
            Thevenoux,A., Glowinski,J., Rogemond,V., Premont,J., Honnorat,J.
            and Gauchy,C.
  TITLE     Differential expression of CRMP1, CRMP2A, CRMP2B, and CRMP5 in
            axons or dendrites of distinct neurons in the mouse brain
  JOURNAL   J Comp Neurol 486 (1), 1-17 (2005)
   PUBMED   15834957
REFERENCE   9  (residues 1 to 686)
  AUTHORS   Fukada,M., Watakabe,I., Yuasa-Kawada,J., Kawachi,H., Kuroiwa,A.,
            Matsuda,Y. and Noda,M.
  TITLE     Molecular characterization of CRMP5, a novel member of the
            collapsin response mediator protein family
  JOURNAL   J Biol Chem 275 (48), 37957-37965 (2000)
   PUBMED   10956643
REFERENCE   10 (residues 1 to 686)
  AUTHORS   Wang,L.H. and Strittmatter,S.M.
  TITLE     A family of rat CRMP genes is differentially expressed in the
            nervous system
  JOURNAL   J Neurosci 16 (19), 6197-6207 (1996)
   PUBMED   8815901
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Aug 1, 2018 this sequence version replaced XP_006251146.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.57286.1,
                                           SRR22399481.2524281.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..686
                     /product="dihydropyrimidinase-related protein 1 isoform 1"
                     /note="dihydropyrimidinase-related protein 1; DRP-1;
                     CRMP-1; inactive dihydropyrimidinase"
                     /calculated_mol_wt=74118
     Region          131..580
                     /region_name="D-HYD"
                     /note="D-hydantoinases (D-HYD) also called
                     dihydropyrimidases (DHPase) and related proteins; DHPases
                     are a family of enzymes that catalyze the reversible
                     hydrolytic ring opening of the amide bond in five- or
                     six-membered cyclic diamides, like dihydropyrimidine...;
                     cd01314"
                     /db_xref="CDD:238639"
     Site            order(142..143,145,158..159,294,315,318,321,344,348,352,
                     355,382..383,385..386,504,509,514)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238639"
     Site            order(187,189,279,312,368,446)
                     /site_type="active"
                     /db_xref="CDD:238639"
     CDS             1..686
                     /gene="Crmp1"
                     /coded_by="NM_001365151.1:95..2155"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25415"
                     /db_xref="RGD:2407"
ORIGIN      
        1 maerrrawnt eddlpvylar pgsaaqtprq kyggmfaave gayenktidf daysvgrrgs
       61 artprsagrp davglpcpgg sedtasdvse psgsavsspg drddrppalr ircpaprdlp
      121 lgrdngqsdr llirggriin ddqsfyadvy ledglikqig enlivpggvk tieangrmvi
      181 pggidvntyl qkpsqgmtsa ddffqgtraa laggttmiid hvvpepgssl ltsfekwhea
      241 adtksccdys lhvditswyd gvreelevlv qdkgvnsfqv ymaykdlyqm sdsqlyeaft
      301 flkglgavil vhaengdlia qeqkrilemg itgpeghals rpeeleaeav fraiaiagri
      361 ncpvyitkvm sksaadiial arkkgplvfg epiaaslgtd gthywsknwa kaaafvtspp
      421 lspdpttpdy ltsllacgdl qvtgsghcpy staqkavgkd nftlipegvn gieermtvvw
      481 dkavatgkmd enqfvavtst naakifnlyp rkgriavgsd advviwdpdk mktltakshk
      541 stveynifeg mechgsplvv isqgkivfed gnisvskgmg rfiprkpfpe hlyqrvrirs
      601 kvfglhsvsr gmydgpvyev patpkhaapa psaksspskh qpppirnlhq snfslsgaqi
      661 ddnnprrtgh rivappggrs nitslg
//
LOCUS       NP_000031                 99 aa            linear   PRI 27-APR-2025
DEFINITION  apolipoprotein C-III precursor [Homo sapiens].
ACCESSION   NP_000031
VERSION     NP_000031.1
DBSOURCE    REFSEQ: accession NM_000040.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Xiao,Q., Wang,L., Wang,J., Wang,M., Wang,D.W. and Ding,H.
  TITLE     A novel lncRNA GM47544 modulates triglyceride metabolism by
            inducing ubiquitination-dependent protein degradation of APOC3
  JOURNAL   Mol Metab 88, 102011 (2024)
   PUBMED   39173944
  REMARK    GeneRIF: A novel lncRNA GM47544 modulates triglyceride metabolism
            by inducing ubiquitination-dependent protein degradation of APOC3.
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Naber,A., Demus,D., Slieker,R.C., Nicolardi,S., Beulens,J.W.J.,
            Elders,P.J.M., Lieverse,A.G., Sijbrands,E.J.G., 't Hart,L.M.,
            Wuhrer,M. and van Hoek,M.
  TITLE     Apolipoprotein-CIII O-Glycosylation Is Associated with Micro- and
            Macrovascular Complications of Type 2 Diabetes
  JOURNAL   Int J Mol Sci 25 (10), 5365 (2024)
   PUBMED   38791405
  REMARK    GeneRIF: Apolipoprotein-CIII O-Glycosylation Is Associated with
            Micro- and Macrovascular Complications of Type 2 Diabetes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Packard,C.J., Pirillo,A., Tsimikas,S., Ference,B.A. and
            Catapano,A.L.
  TITLE     Exploring apolipoprotein C-III: pathophysiological and
            pharmacological relevance
  JOURNAL   Cardiovasc Res 119 (18), 2843-2857 (2024)
   PUBMED   38039351
  REMARK    GeneRIF: Exploring apolipoprotein C-III: pathophysiological and
            pharmacological relevance.
            Review article
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Pu,Z., Wang,W., Xie,H. and Wang,W.
  TITLE     Apolipoprotein C3 (ApoC3) facilitates NLRP3 mediated pyroptosis of
            macrophages through mitochondrial damage by accelerating of the
            interaction between SCIMP and SYK pathway in acute lung injury
  JOURNAL   Int Immunopharmacol 128, 111537 (2024)
   PUBMED   38232538
  REMARK    GeneRIF: Apolipoprotein C3 (ApoC3) facilitates NLRP3 mediated
            pyroptosis of macrophages through mitochondrial damage by
            accelerating of the interaction between SCIMP and SYK pathway in
            acute lung injury.
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Yan,S., Ding,Z.Y., Gao,Y., Mao,W.J. and Cheng,X.Y.
  TITLE     [The role of apolipoprotein C3 in the regulation of nonalcoholic
            fatty liver disease, glucose and lipid metabolism, and islet beta
            cell function]
  JOURNAL   Sheng Li Xue Bao 75 (6), 767-778 (2023)
   PUBMED   38151342
  REMARK    GeneRIF: [The role of apolipoprotein C3 in the regulation of
            nonalcoholic fatty liver disease, glucose and lipid metabolism, and
            islet beta cell function].
            Review article
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Norata,G.D., Tsimikas,S., Pirillo,A. and Catapano,A.L.
  TITLE     Apolipoprotein C-III: From Pathophysiology to Pharmacology
  JOURNAL   Trends Pharmacol Sci 36 (10), 675-687 (2015)
   PUBMED   26435212
  REMARK    Review article
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Sehayek,E. and Eisenberg,S.
  TITLE     Mechanisms of inhibition by apolipoprotein C of apolipoprotein
            E-dependent cellular metabolism of human triglyceride-rich
            lipoproteins through the low density lipoprotein receptor pathway
  JOURNAL   J Biol Chem 266 (27), 18259-18267 (1991)
   PUBMED   1917954
REFERENCE   8  (residues 1 to 99)
  AUTHORS   von Eckardstein,A., Holz,H., Sandkamp,M., Weng,W., Funke,H. and
            Assmann,G.
  TITLE     Apolipoprotein C-III(Lys58----Glu). Identification of an
            apolipoprotein C-III variant in a family with
            hyperalphalipoproteinemia
  JOURNAL   J Clin Invest 87 (5), 1724-1731 (1991)
   PUBMED   2022742
REFERENCE   9  (residues 1 to 99)
  AUTHORS   Karathanasis,S.K., Zannis,V.I. and Breslow,J.L.
  TITLE     Isolation and characterization of cDNA clones corresponding to two
            different human apoC-III alleles
  JOURNAL   J Lipid Res 26 (4), 451-456 (1985)
   PUBMED   2989400
REFERENCE   10 (residues 1 to 99)
  AUTHORS   Kinnunen,P.K. and Ehnolm,C.
  TITLE     Effect of serum and C-apoproteins from very low density
            lipoproteins on human postheparin plasma hepatic lipase
  JOURNAL   FEBS Lett 65 (3), 354-357 (1976)
   PUBMED   182536
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from H74029.1, X01388.1 and
            AV657170.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein component of triglyceride
            (TG)-rich lipoproteins (TRLs) including very low density
            lipoproteins (VLDL), high density lipoproteins (HDL) and
            chylomicrons. The encoded protein plays a role in role in the
            metabolism of these TRLs through multiple modes. This protein has
            been shown to promote the secretion of VLDL1, inhibit lipoprotein
            lipase enzyme activity, and delay catabolism of TRL remnants.
            Mutations in this gene are associated with low plasma triglyceride
            levels and reduced risk of ischemic cardiovascular disease, and
            hyperalphalipoproteinemia, which is characterized by elevated
            levels of high density lipoprotein (HDL) and HDL cholesterol in
            human patients. This gene and other related genes comprise an
            apolipoprotein gene cluster on chromosome 11. [provided by RefSeq,
            Sep 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC027977.1, X01388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000227667.8/ ENSP00000227667.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..99
                     /product="apolipoprotein C-III precursor"
                     /note="apolipoprotein C-III"
                     /calculated_mol_wt=8765
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2106
     mat_peptide     21..99
                     /product="Apolipoprotein C-III.
                     /evidence=ECO:0000269|PubMed:3949020. /id=PRO_0000002031"
                     /note="propagated from UniProtKB/Swiss-Prot (P02656.1)"
                     /calculated_mol_wt=8765
     Region          22..90
                     /region_name="Apo-CIII"
                     /note="Apolipoprotein CIII (Apo-CIII); pfam05778"
                     /db_xref="CDD:461737"
     Site            37
                     /site_type="other"
                     /note="May interact with the LDL receptor.
                     /evidence=ECO:0000305|PubMed:18408013; propagated from
                     UniProtKB/Swiss-Prot (P02656.1)"
     Site            41
                     /site_type="other"
                     /note="May interact with the LDL receptor.
                     /evidence=ECO:0000305|PubMed:18408013; propagated from
                     UniProtKB/Swiss-Prot (P02656.1)"
     Site            44
                     /site_type="other"
                     /note="May interact with the LDL receptor.
                     /evidence=ECO:0000305|PubMed:18408013; propagated from
                     UniProtKB/Swiss-Prot (P02656.1)"
     Region          68..99
                     /region_name="Lipid-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P02656.1)"
     Site            94
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19838169,
                     ECO:0000269|PubMed:23527852, ECO:0000269|PubMed:3123586.
                     /id=CAR_000168; propagated from UniProtKB/Swiss-Prot
                     (P02656.1)"
     CDS             1..99
                     /gene="APOC3"
                     /gene_synonym="Apo-C3; ApoC-3; APOCIII"
                     /coded_by="NM_000040.3:48..347"
                     /db_xref="CCDS:CCDS8377.1"
                     /db_xref="GeneID:345"
                     /db_xref="HGNC:HGNC:610"
                     /db_xref="MIM:107720"
ORIGIN      
        1 mqprvllvva llallasara seaedaslls fmqgymkhat ktakdalssv qesqvaqqar
       61 gwvtdgfssl kdywstvkdk fsefwdldpe vrptsavaa
//
LOCUS       NP_060541               1519 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 40 isoform 1 [Homo sapiens].
ACCESSION   NP_060541 XP_370737
VERSION     NP_060541.3
DBSOURCE    REFSEQ: accession NM_018071.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1519)
  AUTHORS   Gu,J., Zhang,X., Jiang,G., Li,Q., Wang,E. and Yu,J.
  TITLE     ARHGEF40 promotes non-small cell lung cancer proliferation and
            invasion via the AKT-Wnt axis by binding to RhoA
  JOURNAL   Mol Carcinog 61 (11), 1016-1030 (2022)
   PUBMED   36000254
  REMARK    GeneRIF: ARHGEF40 promotes non-small cell lung cancer proliferation
            and invasion via the AKT-Wnt axis by binding to RhoA.
REFERENCE   2  (residues 1 to 1519)
  AUTHORS   Campos,C., Fragoso,S., Luis,R., Pinto,F., Brito,C., Esteves,S.,
            Pataco,M., Santos,S., Machado,P., Vicente,J.B., Rosa,J.C.,
            Cavaco,B.M., Moura,C. and Pojo,M.
  TITLE     High-Throughput Sequencing Identifies 3 Novel Susceptibility Genes
            for Hereditary Melanoma
  JOURNAL   Genes (Basel) 11 (4), 403 (2020)
   PUBMED   32276436
  REMARK    GeneRIF: High-Throughput Sequencing Identifies 3 Novel
            Susceptibility Genes for Hereditary Melanoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1519)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1519)
  AUTHORS   Fujiwara,S., Matsui,T.S., Ohashi,K., Mizuno,K. and Deguchi,S.
  TITLE     Keratin-binding ability of the N-terminal Solo domain of Solo is
            critical for its function in cellular mechanotransduction
  JOURNAL   Genes Cells 24 (5), 390-402 (2019)
   PUBMED   30929300
  REMARK    GeneRIF: Keratin binding domain is critical for Solo localization
            and its function in regulating mechanotransduction.
REFERENCE   5  (residues 1 to 1519)
  AUTHORS   Tse,S.W., Broderick,J.A., Wei,M.L., Luo,M.H., Smith,D.,
            McCaffery,P., Stamm,S. and Andreadis,A.
  TITLE     Identification, expression analysis, genomic organization and
            cellular location of a novel protein with a RhoGEF domain
  JOURNAL   Gene 359, 63-72 (2005)
   PUBMED   16143467
  REMARK    GeneRIF: Solo mRNA is ubiquitously expressed but enriched in brain,
            and it undergoes extensive alternative splicing.
REFERENCE   6  (residues 1 to 1519)
  AUTHORS   Jikuya,H., Takano,J., Kikuno,R., Hirosawa,M., Nagase,T., Nomura,N.
            and Ohara,O.
  TITLE     Characterization of long cDNA clones from human adult spleen. II.
            The complete sequences of 81 cDNA clones
  JOURNAL   DNA Res 10 (1), 49-57 (2003)
   PUBMED   12693554
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY010070.1, AK074057.1,
            BC142692.1, AL161668.6 and HY277017.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Aug 30, 2004 this sequence version replaced
            XP_370737.3, NP_060541.2.
            
            Summary: This gene encodes a protein similar to guanosine
            nucleotide exchange factors for Rho GTPases. The encoded protein
            contains in its C-terminus a GEF domain involved in exchange
            activity and a pleckstrin homology domain. Alternatively spliced
            transcripts that encode different proteins have been described.
            [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK074057.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298694.9/ ENSP00000298694.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..1519
                     /product="rho guanine nucleotide exchange factor 40
                     isoform 1"
                     /note="protein SOLO; Rho guanine nucleotide exchange
                     factor (GEF) 40"
                     /calculated_mol_wt=164527
     Region          194..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TER5.3)"
     Region          253..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TER5.3)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TER5.3)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TER5.3)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TER5.3)"
     Region          786..964
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Site            871..876
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Site            931
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TER5.3)"
     Region          955..1031
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TER5.3)"
     Site            961
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TER5.3)"
     Site            1082
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8TER5.3)"
     Region          1090..1245
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          1244..1379
                     /region_name="PH_puratrophin-1"
                     /note="Puratrophin-1 pleckstrin homology (PH) domain;
                     cd13242"
                     /db_xref="CDD:270062"
     Site            1433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TER5.3)"
     Site            1438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TER5.3)"
     Region          1466..1519
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TER5.3)"
     Site            1474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TER5.3)"
     Site            1492
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TER5.3)"
     CDS             1..1519
                     /gene="ARHGEF40"
                     /gene_synonym="SOLO"
                     /coded_by="NM_018071.5:94..4653"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32041.1"
                     /db_xref="GeneID:55701"
                     /db_xref="HGNC:HGNC:25516"
                     /db_xref="MIM:610018"
ORIGIN      
        1 mepepvedcv qstlaalypp feataptllg qvfqvverty redalrytld flvpakhlla
       61 kvqqeacaqy sgflffhegw plclheqvvv qlaalpwqll rpgdfylqvv psaaqaprla
      121 lkclapgggr vqevpvpnea caylftpewl qginkdrptg rlstcllsap sgiqrlpwae
      181 licprfvhke glmvghqpst lppelpsgpp glpspplpee algtrspgdg hnapvegpeg
      241 eyvellevtl pvrgsptdae gspglsrvrt vptrkgaggk grhrrhrawm hqkglgprgq
      301 dgarppgegs stgaspespp gaeavpeaav levseppaea vgeasgscpl rpgelrgggg
      361 ggqgaegppg tprrtgkgnr rkkraagrga lsrggdsapl spgdkedash qealgnlpsp
      421 sehklpechl vkeeyegsgk pesepkelkt agekepqlse acgpteegag erelegpgll
      481 cmaghtgpeg plsdtptppl etvqegkgdn ipeealavsv sdhpdvawdl masgfliltg
      541 gvdqsgrall titppcppee pppsrdtlnt tlhylhsllr pdlqtlglsv lldlrqappl
      601 ppalipalsq lqdsgdpplv qrllilihdd lptelcgfqg aevlsendlk rvakpeelqw
      661 elgghrdpsp shwveihqev vrlcrlcqgv lgsvrqaiee legaaepeee eavgmpkplq
      721 kvladprlta lqrdggailm rlrstpsskl egqgpatlyq evdeaihqlv rlsnlhvqqq
      781 eqrqclrrlq qvlqwlsgpg eeqlasfamp gdtlsalqet elrfrafsae vqerlaqare
      841 alaleenats qkvldifeqr leqvesglhr alrlqrffqq ahewvdegfa rlagagpgre
      901 avlaalalrr apepsagtfq emralaldlg spaalrewgr cqarcqeler riqqhvgeea
      961 sprgyrrrra dgassggaqw gprspspsls slllpsspgp rpapshcsla pcgedyeeeg
     1021 pelapeaegr ppravlirgl evtstevvdr tcsprehvll grargpdgpw gvgtprmerk
     1081 rsisaqqrlv seliaceqdy vatlsepvpp pgpeltpelr gtwaaalsar erlrsfhrth
     1141 flrelqgcat hplrigacfl rhgdqfslya qyvkhrhkle nglaalspls kgsmeagpyl
     1201 pralqqpleq ltrygrllee llreagpels secralgaav qllreqearg rdllaveavr
     1261 gceidlkeqg qllhrdpftv icgrkkclrh vflfehlllf sklkgpeggs emfvykqafk
     1321 tadmglteni gdsglcfelw frrrrareay tlqatspeik lkwtssiaql lwrqaahnke
     1381 lrvqqmvsmg ignkpfldik algertlsal ltgraartra svavssfeha gpslpglspg
     1441 acslparvee eawdldvkqi slapetldss gdvspgprns pslqpphpgs stptlasrgi
     1501 lglsrqshar alsdpttpl
//
LOCUS       NP_004059                435 aa            linear   PRI 27-APR-2025
DEFINITION  AP-2 complex subunit mu isoform a [Homo sapiens].
ACCESSION   NP_004059
VERSION     NP_004059.2
DBSOURCE    REFSEQ: accession NM_004068.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Lee,H.J., Fenollar-Ferrer,C., Isgrig,K., Wang,Y.X., Valente,K.,
            Eide,J., Honda,K., Chien,W.W., Petralia,R.S., Dong,L.,
            Friedman,T.B., Bonifacino,J.S., Griffith,A.J. and Roux,I.
  TITLE     SLC26A4-AP-2 mu2 interaction regulates SLC26A4 plasma membrane
            abundance in the endolymphatic sac
  JOURNAL   Sci Adv 10 (41), eadm8663 (2024)
   PUBMED   39383236
  REMARK    GeneRIF: SLC26A4-AP-2 mu2 interaction regulates SLC26A4 plasma
            membrane abundance in the endolymphatic sac.
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Mihalic,F., Simonetti,L., Giudice,G., Sander,M.R., Lindqvist,R.,
            Peters,M.B.A., Benz,C., Kassa,E., Badgujar,D., Inturi,R., Ali,M.,
            Krystkowiak,I., Sayadi,A., Andersson,E., Aronsson,H., Soderberg,O.,
            Dobritzsch,D., Petsalaki,E., Overby,A.K., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Large-scale phage-based screening reveals extensive pan-viral
            mimicry of host short linear motifs
  JOURNAL   Nat Commun 14 (1), 2409 (2023)
   PUBMED   37100772
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Liu,X., Zhao,X., Yang,J., Wang,H., Piao,Y. and Wang,L.
  TITLE     High expression of AP2M1 correlates with worse prognosis by
            regulating immune microenvironment and drug resistance to R-CHOP in
            diffuse large B cell lymphoma
  JOURNAL   Eur J Haematol 110 (2), 198-208 (2023)
   PUBMED   36335584
  REMARK    GeneRIF: High expression of AP2M1 correlates with worse prognosis
            by regulating immune microenvironment and drug resistance to R-CHOP
            in diffuse large B cell lymphoma.
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Ohno,H., Stewart,J., Fournier,M.C., Bosshart,H., Rhee,I.,
            Miyatake,S., Saito,T., Gallusser,A., Kirchhausen,T. and
            Bonifacino,J.S.
  TITLE     Interaction of tyrosine-based sorting signals with
            clathrin-associated proteins
  JOURNAL   Science 269 (5232), 1872-1875 (1995)
   PUBMED   7569928
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Liu,Q., Feng,Y. and Forgac,M.
  TITLE     Activity and in vitro reassembly of the coated vesicle (H+)-ATPase
            requires the 50-kDa subunit of the clathrin assembly complex AP-2
  JOURNAL   J Biol Chem 269 (50), 31592-31597 (1994)
   PUBMED   7989329
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Pauloin,A. and Thurieau,C.
  TITLE     The 50 kDa protein subunit of assembly polypeptide (AP) AP-2
            adaptor from clathrin-coated vesicles is phosphorylated on
            threonine-156 by AP-1 and a soluble AP50 kinase which co-purifies
            with the assembly polypeptides
  JOURNAL   Biochem J 296 (Pt 2) (Pt 2), 409-415 (1993)
   PUBMED   8257432
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Chang,M.P., Mallet,W.G., Mostov,K.E. and Brodsky,F.M.
  TITLE     Adaptor self-aggregation, adaptor-receptor recognition and binding
            of alpha-adaptin subunits to the plasma membrane contribute to
            recruitment of adaptor (AP2) components of clathrin-coated pits
  JOURNAL   EMBO J 12 (5), 2169-2180 (1993)
   PUBMED   8491205
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Garcia,J.V. and Miller,A.D.
  TITLE     Serine phosphorylation-independent downregulation of cell-surface
            CD4 by nef
  JOURNAL   Nature 350 (6318), 508-511 (1991)
   PUBMED   2014052
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI461415.1 and BC004996.1.
            
            On Jul 19, 2001 this sequence version replaced NP_004059.1.
            
            Summary: This gene encodes a subunit of the heterotetrameric coat
            assembly protein complex 2 (AP2), which belongs to the adaptor
            complexes medium subunits family. The encoded protein is required
            for the activity of a vacuolar ATPase, which is responsible for
            proton pumping occurring in the acidification of endosomes and
            lysosomes. The encoded protein may also play an important role in
            regulating the intracellular trafficking and function of CTLA-4
            protein. Three transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, Jul 2015].
            
            Transcript Variant: This variant (1) lacks two alternate in-frame
            exons compared to variant 3. The resulting isoform (a) has the same
            N- and C-termini but is shorter compared to isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.179990.1,
                                           SRR3476690.1004436.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000292807.9/ ENSP00000292807.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..435
                     /product="AP-2 complex subunit mu isoform a"
                     /note="clathrin-associated/assembly/adaptor protein,
                     medium 1; plasma membrane adaptor AP-2 50kDA protein;
                     clathrin coat adaptor protein AP50; clathrin adaptor
                     complex AP2, mu subunit; HA2 50 kDA subunit; clathrin
                     assembly protein complex 2 medium chain; AP-2 mu 2 chain;
                     AP-2 complex subunit mu; adaptin-mu2; clathrin coat
                     assembly protein AP50; clathrin coat-associated protein
                     AP50; adaptor protein complex AP-2 subunit mu; plasma
                     membrane adaptor AP-2 50 kDa protein; clathrin assembly
                     protein complex 2 mu medium chain; adaptor-related protein
                     complex 2 subunit mu; adaptor related protein complex 2 mu
                     1 subunit"
                     /calculated_mol_wt=49524
     Region          1..140
                     /region_name="AP2_Mu_N"
                     /note="AP-2 complex subunit mu N-terminal domain; cd14836"
                     /db_xref="CDD:341440"
     Site            order(1,18..19,21..22,45..49,52,54,56,58,60,71..77,79..81,
                     83..84,105,109..110,113..114,117..118,120..123,125,
                     131..132,134..136)
                     /site_type="other"
                     /note="AP2 beta interface [polypeptide binding]"
                     /db_xref="CDD:341440"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q96CW1.2)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AAK1.
                     /evidence=ECO:0000269|PubMed:11877457,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96CW1.2)"
     Region          168..434
                     /region_name="AP-2_Mu2_Cterm"
                     /note="C-terminal domain of medium Mu2 subunit in
                     ubiquitously expressed clathrin-associated adaptor protein
                     (AP) complex AP-2; cd09251"
                     /db_xref="CDD:271159"
     Site            order(174..176,203,318,391,393,401..402,420..423,425)
                     /site_type="signal peptide"
                     /note="signal peptide binding site [polypeptide binding]"
                     /db_xref="CDD:271159"
     Site            order(192..193,245..250,254..255,276,278,382,384,430,432)
                     /site_type="other"
                     /note="AP-2 beta subunit interface [polypeptide binding]"
                     /db_xref="CDD:271159"
     CDS             1..435
                     /gene="AP2M1"
                     /gene_synonym="AP50; CLAPM1; MRD60; mu2"
                     /coded_by="NM_004068.4:149..1456"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43177.1"
                     /db_xref="GeneID:1173"
                     /db_xref="HGNC:HGNC:564"
                     /db_xref="MIM:601024"
ORIGIN      
        1 migglfiynh kgevlisrvy rddigrnavd afrvnvihar qqvrspvtni artsffhvkr
       61 sniwlaavtk qnvnaamvfe flykmcdvma ayfgkiseen iknnfvliye lldeildfgy
      121 pqnsetgalk tfitqqgiks qhqtkeeqsq itsqvtgqig wrregikyrr nelfldvles
      181 vnllmspqgq vlsahvsgrv vmksylsgmp eckfgmndki viekqgkgta detsksgkqs
      241 iaiddctfhq cvrlskfdse rsisfippdg efelmryrtt kdiilpfrvi plvrevgrtk
      301 levkvviksn fkpsllaqki evriptplnt sgvqvicmkg kakykasena ivwkikrmag
      361 mkesqisaei ellptndkkk warppismnf evpfapsglk vrylkvfepk lnysdhdvik
      421 wvryigrsgi yetrc
//
LOCUS       NP_001356309             386 aa            linear   PRI 27-APR-2025
DEFINITION  nucleosome assembly protein 1-like 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001356309
VERSION     NP_001356309.1
DBSOURCE    REFSEQ: accession NM_001369380.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Tan,L., Cheng,W., Liu,F., Wang,D.O., Wu,L., Cao,N. and Wang,J.
  TITLE     Positive natural selection of N6-methyladenosine on the RNAs of
            processed pseudogenes
  JOURNAL   Genome Biol 22 (1), 180 (2021)
   PUBMED   34120636
  REMARK    GeneRIF: Positive natural selection of N6-methyladenosine on the
            RNAs of processed pseudogenes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Mizuhashi,S., Fukushima,S., Ishibashi,T., Kuriyama,H., Kimura,T.,
            Kanemaru,H., Kajihara,I., Makino,K., Miyashita,A., Aoi,J., Kita,K.
            and Ihn,H.
  TITLE     Nucleosome assembly protein 1-like 4, a new therapeutic target for
            proliferation and invasion of melanoma cells
  JOURNAL   J Dermatol Sci 102 (1), 16-24 (2021)
   PUBMED   33583643
  REMARK    GeneRIF: Nucleosome assembly protein 1-like 4, a new therapeutic
            target for proliferation and invasion of melanoma cells.
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Tanaka,T., Hozumi,Y., Martelli,A.M., Iino,M. and Goto,K.
  TITLE     Nucleosome assembly proteins NAP1L1 and NAP1L4 modulate p53
            acetylation to regulate cell fate
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1866 (12), 118560 (2019)
   PUBMED   31634504
  REMARK    GeneRIF: The NAP1L4 regulates cell fate by controlling the
            expression of p53-responsive proarrest and proapoptotic genes
            through selective modulation of p53 acetylation at specific sites
            during normal homeostasis and in stress-induced responses.
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Tanaka,T., Hozumi,Y., Iino,M. and Goto,K.
  TITLE     NAP1L1 regulates NF-kappaB signaling pathway acting on
            anti-apoptotic Mcl-1 gene expression
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1864 (10), 1759-1768 (2017)
   PUBMED   28687276
  REMARK    GeneRIF: knockdown of NAP1L1 suppresses IkappaBalpha degradation
            and nuclear transport of p65 subunit after treatment with TNF-a
            stimulation, leading to attenuation of the NF-kappaB
            transcriptional activity, whereas NAP1L4 knockdown remains
            silent.results of this study suggest that NAP1L1 downregulation
            renders the cell vulnerable to apoptotic cell death through
            attenuation of NF-kappaB transcriptional activity on the
            anti-apop...
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Ruiz,M.T., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2 is part of multi-protein complexes in HeLa cells
  JOURNAL   J Cell Biochem 93 (2), 398-408 (2004)
   PUBMED   15368365
  REMARK    GeneRIF: NAP-2 is in complex(es) with other proteins, which are
            distinct from histones
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Shikama,N., Chan,H.M., Krstic-Demonacos,M., Smith,L., Lee,C.W.,
            Cairns,W. and La Thangue,N.B.
  TITLE     Functional interaction between nucleosome assembly proteins and
            p300/CREB-binding protein family coactivators
  JOURNAL   Mol Cell Biol 20 (23), 8933-8943 (2000)
   PUBMED   11073993
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Pelletier,J., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2: histone chaperone function and phosphorylation state through
            the cell cycle
  JOURNAL   J Mol Biol 298 (2), 225-238 (2000)
   PUBMED   10764593
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Munroe,D., Prawitt,D., Chu,L.L., Bric,E., Kim,J.,
            Reid,L.H., Davies,C., Nakagama,H., Loebbert,R., Winterpacht,A.,
            Petruzzi,M.J., Higgins,M.J., Nowak,N., Evans,G., Shows,T.,
            Weissman,B.E., Zabel,B., Housman,D.E. and Pelletier,J.
  TITLE     Functional characterization of human nucleosome assembly protein-2
            (NAP1L4) suggests a role as a histone chaperone
  JOURNAL   Genomics 44 (3), 253-265 (1997)
   PUBMED   9325046
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Hu,R.J., Lee,M.P., Johnson,L.A. and Feinberg,A.P.
  TITLE     A novel human homologue of yeast nucleosome assembly protein, 65 kb
            centromeric to the p57KIP2 gene, is biallelically expressed in
            fetal and adult tissues
  JOURNAL   Hum Mol Genet 5 (11), 1743-1748 (1996)
   PUBMED   8923002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC131971.9.
            
            Summary: This gene encodes a member of the nucleosome assembly
            protein (NAP) family which can interact with both core and linker
            histones. It can shuttle between the cytoplasm and nucleus,
            suggesting a role as a histone chaperone. This gene is one of
            several located near the imprinted gene domain of 11p15.5, an
            important tumor-suppressor gene region. Alterations in this region
            have been associated with the Beckwith-Wiedemann syndrome, Wilms
            tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung,
            ovarian, and breast cancer. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.73699.1,
                                           SRR1803614.162565.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..386
                     /product="nucleosome assembly protein 1-like 4 isoform 2"
                     /note="nucleosome assembly protein 2; nucleosome assembly
                     protein 1-like 4b; NAP-2"
                     /calculated_mol_wt=43948
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          65..338
                     /region_name="NAP"
                     /note="Nucleosome assembly protein (NAP); pfam00956"
                     /db_xref="CDD:460010"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P28656; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          116..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          265..271
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     CDS             1..386
                     /gene="NAP1L4"
                     /gene_synonym="hNAP2; NAP1L4b; NAP2; NAP2L"
                     /coded_by="NM_001369380.1:94..1254"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS91410.1"
                     /db_xref="GeneID:4676"
                     /db_xref="HGNC:HGNC:7640"
                     /db_xref="MIM:601651"
ORIGIN      
        1 madhsfsdgv psdsveaakn asntekltdq vmqnprvlaa lqerldnvph tpssyietlp
       61 kavkrrinal kqlqvrcahi eakfyeevhd lerkyaalyq plfdkrrefi tgdveptdae
      121 sewhseneee eklagdmksk vvvtekaaat aeepdpkgip efwftifrnv dmlselvqey
      181 depilkhlqd ikvkfsdpgq pmsfvlefhf epndyftnsv ltktykmkse pdkadpfsfe
      241 gpeivdcdgc tidwkkgknv tvktikkkqk hkgrgtvrti tkqvpnesff nffnplkasg
      301 dgesldedse ftlasdfeig hffrerivpr avlyftgeai edddnfeege egeeeelegd
      361 eegededdae inpkkepsqp aeckqq
//
LOCUS       NP_001353502             833 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 10 [Homo
            sapiens].
ACCESSION   NP_001353502
VERSION     NP_001353502.1
DBSOURCE    REFSEQ: accession NM_001366573.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 833)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 833)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 833)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 833)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 833)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 833)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 833)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.100580.1,
                                           SRR1660803.80269.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..833
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 10"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=93988
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <535..>669
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..833
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366573.1:2344..4845"
                     /note="isoform 10 is encoded by transcript variant 13"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsvtkhkgt
      361 ekrespspap kprkvelses eedkggkmaa adsvqqrrqy rrqnqqsssd sgsssssede
      421 rpkrshvkng evgrrrrhsp srsaspsprk rqketsprmq mgkrwqspvt ksgrrrrsps
      481 ppptrrrrsp spappprrrr tptppprrrt psppprrrsp sprrysppiq rryspspppk
      541 rrtasppppp krraspsppp krrvshsppp kqrsspvtkr rspslsskhr kgsspsrstr
      601 earspqpnkr hspsprprap qtssspppvr rgassspqrr qspspstrpi rrvsrtpepk
      661 kikkaaspsp qsvrrvsssr svsgspepaa kkppappspv qsqspstnws pavpvkkaks
      721 ptpspspprn sdqegggkkk kkkkdkkhkk dkkhkkhkkh kkekavaaaa aaavtpaaia
      781 aatttlaqee pvaapepkke teseaednld dlekhlreka lrsmrkaqvs pqs
//
LOCUS       NP_001344224             257 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF170 isoform 1 [Mus musculus].
ACCESSION   NP_001344224 XP_006509279
VERSION     NP_001344224.2
DBSOURCE    REFSEQ: accession NM_001357295.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Song,X., Liu,S., Wang,W., Ma,Z., Cao,X. and Jiang,M.
  TITLE     E3 ubiquitin ligase RNF170 inhibits innate immune responses by
            targeting and degrading TLR3 in murine cells
  JOURNAL   Cell Mol Immunol 17 (8), 865-874 (2020)
   PUBMED   31076723
  REMARK    GeneRIF: E3 ubiquitin ligase RNF170 inhibits innate immune
            responses by targeting and degrading TLR3 in murine cells.
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Kim,Y., Kim,S.H., Kim,K.H., Chae,S., Kim,C., Kim,J., Shin,H.S.,
            Lee,M.S. and Kim,D.
  TITLE     Age-dependent gait abnormalities in mice lacking the Rnf170 gene
            linked to human autosomal-dominant sensory ataxia
  JOURNAL   Hum Mol Genet 24 (25), 7196-7206 (2015)
   PUBMED   26433933
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Lu,J.P., Wang,Y., Sliter,D.A., Pearce,M.M. and Wojcikiewicz,R.J.
  TITLE     RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase,
            mediates inositol 1,4,5-trisphosphate receptor ubiquitination and
            degradation
  JOURNAL   J Biol Chem 286 (27), 24426-24433 (2011)
   PUBMED   21610068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093366.9.
            
            On May 14, 2019 this sequence version replaced NP_001344224.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660813.95711.1,
                                           SRR7652917.244715.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 14.38 cM"
     Protein         1..257
                     /product="E3 ubiquitin-protein ligase RNF170 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF170; RING-type E3
                     ubiquitin transferase RNF170"
                     /calculated_mol_wt=29687
     Region          84..139
                     /region_name="RING-HC_RNF170"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 170 (RNF170) and similar proteins; cd16553"
                     /db_xref="CDD:438215"
     Region          203..238
                     /region_name="DUF1232"
                     /note="Protein of unknown function (DUF1232); pfam06803"
                     /db_xref="CDD:462011"
     CDS             1..257
                     /gene="Rnf170"
                     /gene_synonym="6720407G21Rik"
                     /coded_by="NM_001357295.2:462..1235"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS22207.1"
                     /db_xref="GeneID:77733"
                     /db_xref="MGI:MGI:1924983"
ORIGIN      
        1 maryysegqs lqqddsfieg vsdqvlvavv vslaltatll yallrnvqqn ihpenqelvr
       61 vlreqfqteq dvpaparqqf ytemycpicl hqasfpvetn cghlfcgsci iaywrygswl
      121 gaiscpicrq tvtllltvfg eddqsqdvir lrqdvndynr rfsgqprsim erimdlptll
      181 rhafrevfsv gglfwmfrir imlclmgaff ylispldfvp ealfgilgfl ddffviflll
      241 iyisimyrev itqrltr
//
LOCUS       NP_114437               1053 aa            linear   PRI 27-APR-2025
DEFINITION  EMILIN-2 precursor [Homo sapiens].
ACCESSION   NP_114437
VERSION     NP_114437.2
DBSOURCE    REFSEQ: accession NM_032048.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Broniarczyk,J., Trejo-Cerro,O., Massimi,P., Kavcic,N., Myers,M.P.
            and Banks,L.
  TITLE     HPV-18 E6 enhances the interaction between EMILIN2 and SNX27 to
            promote WNT signaling
  JOURNAL   J Virol 98 (7), e0073524 (2024)
   PUBMED   38874360
  REMARK    GeneRIF: HPV-18 E6 enhances the interaction between EMILIN2 and
            SNX27 to promote WNT signaling.
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Tang,X. and Li,F.
  TITLE     Decreased EMILIN2 correlates to metabolism phenotype and poor
            prognosis of ovarian cancer
  JOURNAL   J Biochem 172 (2), 89-97 (2022)
   PUBMED   35588228
  REMARK    GeneRIF: Decreased EMILIN2 correlates to metabolism phenotype and
            poor prognosis of ovarian cancer.
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wang,L.C., Cui,W.Y., Zhang,Z., Tan,Z.L., Lv,Q.L., Chen,S.H. and
            Shen,X.L.
  TITLE     Expression, methylation and prognostic feature of EMILIN2 in
            Low-Grade-Glioma
  JOURNAL   Brain Res Bull 175, 26-36 (2021)
   PUBMED   34280481
  REMARK    GeneRIF: Expression, methylation and prognostic feature of EMILIN2
            in Low-Grade-Glioma.
REFERENCE   4  (residues 1 to 1053)
  AUTHORS   Andreuzzi,E., Capuano,A., Pellicani,R., Poletto,E., Doliana,R.,
            Maiero,S., Fornasarig,M., Magris,R., Colombatti,A., Cannizzaro,R.,
            Spessotto,P. and Mongiat,M.
  TITLE     Loss of Multimerin-2 and EMILIN-2 Expression in Gastric Cancer
            Associate with Altered Angiogenesis
  JOURNAL   Int J Mol Sci 19 (12), 3983 (2018)
   PUBMED   30544909
  REMARK    GeneRIF: Loss of Multimerin-2 and EMILIN-2 Expression in Gastric
            Cancer Associate with Altered Angiogenesis
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1053)
  AUTHORS   Paulitti,A., Andreuzzi,E., Bizzotto,D., Pellicani,R.,
            Tarticchio,G., Marastoni,S., Pastrello,C., Jurisica,I.,
            Ligresti,G., Bucciotti,F., Doliana,R., Colladel,R., Braghetta,P.,
            Poletto,E., Di Silvestre,A., Bressan,G., Colombatti,A., Bonaldo,P.
            and Mongiat,M.
  TITLE     The ablation of the matricellular protein EMILIN2 causes defective
            vascularization due to impaired EGFR-dependent IL-8 production
            affecting tumor growth
  JOURNAL   Oncogene 37 (25), 3399-3414 (2018)
   PUBMED   29483644
  REMARK    GeneRIF: High EMILIN2 expression is associated with angiogenesis in
            B16 melanoma.
REFERENCE   6  (residues 1 to 1053)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1053)
  AUTHORS   Doliana,R., Veljkovic,V., Prljic,J., Veljkovic,N., De Lorenzo,E.,
            Mongiat,M., Ligresti,G., Marastoni,S. and Colombatti,A.
  TITLE     EMILINs interact with anthrax protective antigen and inhibit toxin
            action in vitro
  JOURNAL   Matrix Biol 27 (2), 96-106 (2008)
   PUBMED   17988845
  REMARK    GeneRIF: EMILIN1 interacts with anthrax protective antigen and
            inhibits toxin action in vitro. EMILIN1 may be a potential target
            and/or a protein useful for countermeasures against B. anthracis
            toxin lethality.
REFERENCE   8  (residues 1 to 1053)
  AUTHORS   Mongiat,M., Ligresti,G., Marastoni,S., Lorenzon,E., Doliana,R. and
            Colombatti,A.
  TITLE     Regulation of the extrinsic apoptotic pathway by the extracellular
            matrix glycoprotein EMILIN2
  JOURNAL   Mol Cell Biol 27 (20), 7176-7187 (2007)
   PUBMED   17698584
  REMARK    GeneRIF: Results suggest that the expression of EMILIN2 triggers
            the apoptosis of different cell lines by activation of death
            receptors.
REFERENCE   9  (residues 1 to 1053)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 1053)
  AUTHORS   Doliana,R., Bot,S., Mungiguerra,G., Canton,A., Cilli,S.P. and
            Colombatti,A.
  TITLE     Isolation and characterization of EMILIN-2, a new component of the
            growing EMILINs family and a member of the EMI domain-containing
            superfamily
  JOURNAL   J Biol Chem 276 (15), 12003-12011 (2001)
   PUBMED   11278945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001011.6, AF270513.1, AI356740.1, AL552384.3, BX398832.2,
            AK090519.1 and AP000919.6.
            
            On Mar 4, 2005 this sequence version replaced NP_114437.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF270513.1, BC136541.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254528.4/ ENSP00000254528.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.32-p11.31"
     Protein         1..1053
                     /product="EMILIN-2 precursor"
                     /note="extracellular glycoprotein EMILIN-2; elastin
                     microfibril interface-located protein 2"
                     /calculated_mol_wt=112197
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3509
     mat_peptide     31..1053
                     /product="EMILIN-2. /id=PRO_0000007817"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXX0.3)"
                     /calculated_mol_wt=112197
     Region          45..115
                     /region_name="EMI"
                     /note="EMI domain; pfam07546"
                     /db_xref="CDD:462204"
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXX0.3)"
     Region          120..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXX0.3)"
     Region          212..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXX0.3)"
     Region          <270..732
                     /region_name="PRK01156"
                     /note="chromosome segregation protein; Provisional"
                     /db_xref="CDD:100796"
     Site            275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXX0.3)"
     Site            458
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXX0.3)"
     Site            510
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXX0.3)"
     Site            587
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXX0.3)"
     Site            616
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9BXX0.3)"
     Site            745
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXX0.3)"
     Region          783..901
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXX0.3)"
     Region          849..901
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          908..1046
                     /region_name="C1q"
                     /note="C1q domain; cl23878"
                     /db_xref="CDD:420072"
     Site            974
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BXX0.3)"
     CDS             1..1053
                     /gene="EMILIN2"
                     /gene_synonym="EMILIN-2; FOAP-10"
                     /coded_by="NM_032048.3:184..3345"
                     /db_xref="CCDS:CCDS11828.1"
                     /db_xref="GeneID:84034"
                     /db_xref="HGNC:HGNC:19881"
                     /db_xref="MIM:608928"
ORIGIN      
        1 mwqprrpwpr vpwrwalall alvgaglcha gpqpgyparp sarnknwcay ivnknvscsv
       61 legsesfiqa qyncawnqmp cpsalvyrvn frpryvtryk tvtqlewrcc pgfrggdcqe
      121 gpkdpvktlr ptparprnsl kkatdnepsq fseprktlsp tgtaqpswgv dpkegpqelq
      181 ekkiqvleek vlrltrtvld lqsslagvse nlkhatqdda srtrapglss qhpkpdttvs
      241 gdtetgqspg vfntkesgmk dikselaevk dtlknksdkl eeldgkvkgy egqlrqlqea
      301 aqgptvtmtt nelyqayvds kidalreelm egmdrkladl knsceykltg lqqqcddygs
      361 sylgvielig eketslrkei nnlrarlqep saqanccdse kngdigqqik tldqkierva
      421 eatrmlngrl dnefdrlivp epdvdfdakw neldarinvt eknaeehcfy ieetlrgain
      481 gevgdlkqlv dqkiqsledr lgsvllqmtn ntgaelsppg aaalpgvsgs gdervmmeln
      541 hlkdkvqvve dicllniqgk phgmegalpn redravrdsl hllkslndtm hrkfqeteqt
      601 iqklqqdfsf lysqlnhten dvthlqkems ncragenagm grftkvgeqe rtvdtlpspq
      661 hpvahccsql eerwqrlqsq viseldacke ctqgvqrevs mvegrvshme ktcskldsis
      721 gnlqrikegl nkhvsslwnc vrqmngtlrs hsrdisglkn svqqfyshvf qistdlqdlv
      781 kfqpsakaps ppppaeapke plqpepappr psgpataedp grrpvlpqrp peerppqppg
      841 stgviaetgq agppagagvs grglprgvdg qtgsgtvpga egfagapgyp ksppvaspga
      901 pvpslvsfsa gltqkpfpsd ggvvlfnkvl vndgdvynps tgvftapydg rylitatltp
      961 erdayveavl svsnasvaql htagyrrefl eyhrppgalh tcggpgafhl ivhlkagdav
     1021 nvvvtggkla htdfdemyst fsgvflypfl shl
//
LOCUS       NP_001353452            1176 aa            linear   PRI 27-APR-2025
DEFINITION  plasma membrane calcium-transporting ATPase 1 isoform 1a [Homo
            sapiens].
ACCESSION   NP_001353452 XP_024304760
VERSION     NP_001353452.1
DBSOURCE    REFSEQ: accession NM_001366523.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1176)
  AUTHORS   Kobayashi,Y., Yatsu,K., Haruna,A., Kawano,R., Ozawa,M., Haze,T.,
            Komiya,S., Suzuki,S., Ohki,Y., Fujiwara,A., Saka,S., Hirawa,N.,
            Toya,Y. and Tamura,K.
  TITLE     ATP2B1 gene polymorphisms associated with resistant hypertension in
            the Japanese population
  JOURNAL   J Clin Hypertens (Greenwich) 26 (4), 355-362 (2024)
   PUBMED   38430457
  REMARK    GeneRIF: ATP2B1 gene polymorphisms associated with resistant
            hypertension in the Japanese population.
REFERENCE   2  (residues 1 to 1176)
  AUTHORS   Gao,Y., Liu,Y., Jiang,Y., Qin,M., Guan,Z., Gao,Y. and Yang,Y.
  TITLE     Association between polymorphism and haplotype of ATP2B1 gene and
            skeletal fluorosis in Han population
  JOURNAL   Int J Environ Health Res 34 (3), 1410-1420 (2024)
   PUBMED   37211801
  REMARK    GeneRIF: Association between polymorphism and haplotype of ATP2B1
            gene and skeletal fluorosis in Han population.
REFERENCE   3  (residues 1 to 1176)
  AUTHORS   Berrocal,M. and Mata,A.M.
  TITLE     The Plasma Membrane Ca2+-ATPase, a Molecular Target for Tau-induced
            Cytosolic Calcium Dysregulation
  JOURNAL   Neuroscience 518, 112-118 (2023)
   PUBMED   35469971
  REMARK    GeneRIF: The Plasma Membrane Ca[2+]-ATPase, a Molecular Target for
            Tau-induced Cytosolic Calcium Dysregulation.
            Review article
REFERENCE   4  (residues 1 to 1176)
  AUTHORS   Yang,X., Lu,L., Wu,C. and Zhang,F.
  TITLE     ATP2B1-AS1 exacerbates sepsis-induced cell apoptosis and
            inflammation by regulating miR-23a-3p/TLR4 axis
  JOURNAL   Allergol Immunopathol (Madr) 51 (2), 17-26 (2023)
   PUBMED   36916084
  REMARK    GeneRIF: ATP2B1-AS1 exacerbates sepsis-induced cell apoptosis and
            inflammation by regulating miR-23a-3p/TLR4 axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1176)
  AUTHORS   Rahimi,M.J., Urban,N., Wegler,M., Sticht,H., Schaefer,M., Popp,B.,
            Gaunitz,F., Morleo,M., Nigro,V., Maitz,S., Mancini,G.M.S.,
            Ruivenkamp,C., Suk,E.K., Bartolomaeus,T., Merkenschlager,A.,
            Koboldt,D., Bartholomew,D., Stegmann,A.P.A., Sinnema,M.,
            Duynisveld,I., Salvarinova,R., Race,S., de Vries,B.B.A.,
            Trimouille,A., Naudion,S., Marom,D., Hamiel,U., Henig,N.,
            Demurger,F., Rahner,N., Bartels,E., Hamm,J.A., Putnam,A.M.,
            Person,R., Abou Jamra,R. and Oppermann,H.
  TITLE     De novo variants in ATP2B1 lead to neurodevelopmental delay
  JOURNAL   Am J Hum Genet 109 (5), 944-952 (2022)
   PUBMED   35358416
  REMARK    GeneRIF: De novo variants in ATP2B1 lead to neurodevelopmental
            delay.
REFERENCE   6  (residues 1 to 1176)
  AUTHORS   Kessler,F., Falchetto,R., Heim,R., Meili,R., Vorherr,T.,
            Strehler,E.E. and Carafoli,E.
  TITLE     Study of calmodulin binding to the alternatively spliced C-terminal
            domain of the plasma membrane Ca2+ pump
  JOURNAL   Biochemistry 31 (47), 11785-11792 (1992)
   PUBMED   1332771
REFERENCE   7  (residues 1 to 1176)
  AUTHORS   Wang,K.K., Wright,L.C., Machan,C.L., Allen,B.G., Conigrave,A.D. and
            Roufogalis,B.D.
  TITLE     Protein kinase C phosphorylates the carboxyl terminus of the plasma
            membrane Ca(2+)-ATPase from human erythrocytes
  JOURNAL   J Biol Chem 266 (14), 9078-9085 (1991)
   PUBMED   1827443
REFERENCE   8  (residues 1 to 1176)
  AUTHORS   Olson,S., Wang,M.G., Carafoli,E., Strehler,E.E. and McBride,O.W.
  TITLE     Localization of two genes encoding plasma membrane
            Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and
            12q21-23
  JOURNAL   Genomics 9 (4), 629-641 (1991)
   PUBMED   1674727
REFERENCE   9  (residues 1 to 1176)
  AUTHORS   Strehler,E.E., Strehler-Page,M.A., Vogel,G. and Carafoli,E.
  TITLE     mRNAs for plasma membrane calcium pump isoforms differing in their
            regulatory domain are generated by alternative splicing that
            involves two internal donor sites in a single exon
  JOURNAL   Proc Natl Acad Sci U S A 86 (18), 6908-6912 (1989)
   PUBMED   2528729
REFERENCE   10 (residues 1 to 1176)
  AUTHORS   James,P.H., Pruschy,M., Vorherr,T.E., Penniston,J.T. and
            Carafoli,E.
  TITLE     Primary structure of the cAMP-dependent phosphorylation site of the
            plasma membrane calcium pump
  JOURNAL   Biochemistry 28 (10), 4253-4258 (1989)
   PUBMED   2548572
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009522.11, AC068641.18 and
            AC025034.22.
            
            On Oct 10, 2018 this sequence version replaced XP_024304760.1.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type primary ion transport ATPases characterized by the formation
            of an aspartyl phosphate intermediate during the reaction cycle.
            These enzymes remove bivalent calcium ions from eukaryotic cells
            against very large concentration gradients and play a critical role
            in intracellular calcium homeostasis. The mammalian plasma membrane
            calcium ATPase isoforms are encoded by at least four separate genes
            and the diversity of these enzymes is further increased by
            alternative splicing of transcripts. The expression of different
            isoforms and splice variants is regulated in a developmental,
            tissue- and cell type-specific manner, suggesting that these pumps
            are functionally adapted to the physiological needs of particular
            cells and tissues. This gene encodes the plasma membrane calcium
            ATPase isoform 1. Alternatively spliced transcript variants
            encoding different isoforms have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (6), as well as variant 1, encodes
            isoform 1a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.53806.1,
                                           SRR1803611.213452.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.33"
     Protein         1..1176
                     /product="plasma membrane calcium-transporting ATPase 1
                     isoform 1a"
                     /EC_number="7.2.2.10"
                     /note="plasma membrane calcium pump; ATPase, Ca++
                     transporting, plasma membrane 1; plasma membrane
                     calcium-transporting ATPase 1"
                     /calculated_mol_wt=129386
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Region          15..1064
                     /region_name="ATPase-IIB_Ca"
                     /note="plasma-membrane calcium-translocating P-type
                     ATPase; TIGR01517"
                     /db_xref="CDD:273668"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            155..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Region          297..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G5E829; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Site            367..386
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            419..439
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            856..876
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            883..903
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            928..948
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            972..991
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            1006..1027
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Site            1040..1060
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Region          1100..1117
                     /region_name="Calmodulin-binding subdomain A.
                     /evidence=ECO:0000305|PubMed:1332771"
                     /note="propagated from UniProtKB/Swiss-Prot (P20020.4)"
     Region          1103..1142
                     /region_name="ATP_Ca_trans_C"
                     /note="Plasma membrane calcium transporter ATPase C
                     terminal; pfam12424"
                     /db_xref="CDD:463575"
     Site            1116
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000269|PubMed:1827443; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     Site            1142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11505; propagated from
                     UniProtKB/Swiss-Prot (P20020.4)"
     CDS             1..1176
                     /gene="ATP2B1"
                     /gene_synonym="MRD66; PMCA1; PMCA1kb"
                     /coded_by="NM_001366523.1:465..3995"
                     /note="isoform 1a is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS41817.1"
                     /db_xref="GeneID:490"
                     /db_xref="HGNC:HGNC:814"
                     /db_xref="MIM:108731"
ORIGIN      
        1 mgdmannsva ysgvknslke anhdgdfgit laelralmel rstdalrkiq esygdvygic
       61 tklktspneg lsgnpadler reavfgknfi ppkkpktflq lvwealqdvt liileiaaiv
      121 slglsfyqpp egdnalcgev svgeeegege tgwiegaail lsvvcvvlvt afndwskekq
      181 frglqsrieq eqkftvirgg qviqipvadi tvgdiaqvky gdllpadgil iqgndlkide
      241 ssltgesdhv kksldkdpll lsgthvmegs grmvvtavgv nsqtgiiftl lgaggeeeek
      301 kdekkkekkn kkqdgaienr nkakaqdgaa memqplksee ggdgdekdkk kanlpkkeks
      361 vlqgkltkla vqigkagllm saitviilvl yfvidtfwvq krpwlaectp iyiqyfvkff
      421 iigvtvlvva vpeglplavt islaysvkkm mkdnnlvrhl dacetmgnat aicsdktgtl
      481 tmnrmtvvqa yinekhykkv pepeaippni lsylvtgisv ncaytskilp pekegglprh
      541 vgnktecall gllldlkrdy qdvrneipee alykvytfns vrksmstvlk nsdgsyrifs
      601 kgaseiilkk cfkilsange akvfrprdrd divktviepm aseglrticl afrdfpagep
      661 epewdnendi vtgltciavv giedpvrpev pdaikkcqra gitvrmvtgd nintaraiat
      721 kcgilhpged flclegkdfn rrirnekgei eqeridkiwp klrvlarssp tdkhtlvkgi
      781 idstvsdqrq vvavtgdgtn dgpalkkadv gfamgiagtd vakeasdiil tddnftsivk
      841 avmwgrnvyd siskflqfql tvnvvaviva ftgacitqds plkavqmlwv nlimdtlasl
      901 alatepptes lllrkpygrn kplisrtmmk nilghafyql vvvftllfag ekffdidsgr
      961 naplhappse hytivfntfv lmqlfneina rkihgernvf egifnnaifc tivlgtfvvq
     1021 iiivqfggkp fscselsieq wlwsiflgmg tllwgqlist iptsrlkflk eaghgtqkee
     1081 ipeeelaedv eeidhaerel rrgqilwfrg lnriqtqmdv vnafqsgssi qgalrrqpsi
     1141 asqhhdvtni stpthvvfss stasttvgys sgecis
//
LOCUS       NP_002130                391 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding motif protein, X chromosome isoform 1 [Homo sapiens].
ACCESSION   NP_002130
VERSION     NP_002130.2
DBSOURCE    REFSEQ: accession NM_002139.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Johansson,J., Lideus,S., Frykholm,C., Gunnarsson,C., Mihalic,F.,
            Gudmundsson,S., Ekvall,S., Molin,A.M., Pham,M., Vihinen,M.,
            Lagerstedt-Robinson,K., Nordgren,A., Jemth,P., Ameur,A.,
            Anneren,G., Wilbe,M. and Bondeson,M.L.
  TITLE     Gustavson syndrome is caused by an in-frame deletion in RBMX
            associated with potentially disturbed SH3 domain interactions
  JOURNAL   Eur J Hum Genet 32 (3), 333-341 (2024)
   PUBMED   37277488
  REMARK    GeneRIF: Gustavson syndrome is caused by an in-frame deletion in
            RBMX associated with potentially disturbed SH3 domain interactions.
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Yan,Q., Zeng,P., Huang,S., Tan,C., Zhou,X., Qiao,J., Zhao,X.,
            Feng,L., Zhu,Z., Zhang,G., Hu,H. and Chen,C.
  TITLE     [RBMX overexpression inhibits proliferation, migration, invasion
            and glycolysis of human bladder cancer cells by downregulating
            PKM2]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 44 (1), 9-16 (2024)
   PUBMED   38293971
  REMARK    GeneRIF: [RBMX overexpression inhibits proliferation, migration,
            invasion and glycolysis of human bladder cancer cells by
            downregulating PKM2].
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Sheng,Y., Lei,K., Sun,C., Liu,J., Tu,Z., Zhu,X. and Huang,K.
  TITLE     Aberrant RBMX expression is relevant for cancer prognosis and
            immunotherapy response
  JOURNAL   Aging (Albany NY) 16 (1), 226-245 (2024)
   PUBMED   38214653
  REMARK    GeneRIF: Aberrant RBMX expression is relevant for cancer prognosis
            and immunotherapy response.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Liu,J., Zheng,T., Chen,D., Huang,J., Zhao,Y., Ma,W. and Liu,H.
  TITLE     RBMX involves in telomere stability maintenance by regulating TERRA
            expression
  JOURNAL   PLoS Genet 19 (9), e1010937 (2023)
   PUBMED   37756323
  REMARK    GeneRIF: RBMX involves in telomere stability maintenance by
            regulating TERRA expression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Zheng,Y., Niu,X., Xue,W., Li,L., Geng,Q., Fan,Z. and Zhao,J.
  TITLE     The Role of Alternative Splicing Factors hnRNP G and Fox-2 in the
            Progression and Prognosis of Esophageal Cancer
  JOURNAL   Dis Markers 2022, 3043737 (2022)
   PUBMED   36466711
  REMARK    GeneRIF: The Role of Alternative Splicing Factors hnRNP G and Fox-2
            in the Progression and Prognosis of Esophageal Cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Mazeyrat,S., Saut,N., Mattei,M.G. and Mitchell,M.J.
  TITLE     RBMY evolved on the Y chromosome from a ubiquitously transcribed
            X-Y identical gene
  JOURNAL   Nat Genet 22 (3), 224-226 (1999)
   PUBMED   10391207
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Delbridge,M.L., Lingenfelter,P.A., Disteche,C.M. and Graves,J.A.
  TITLE     The candidate spermatogenesis gene RBMY has a homologue on the
            human X chromosome
  JOURNAL   Nat Genet 22 (3), 223-224 (1999)
   PUBMED   10391206
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Venables,J.P., Vernet,C., Chew,S.L., Elliott,D.J., Cowmeadow,R.B.,
            Wu,J., Cooke,H.J., Artzt,K. and Eperon,I.C.
  TITLE     T-STAR/ETOILE: a novel relative of SAM68 that interacts with an
            RNA-binding protein implicated in spermatogenesis
  JOURNAL   Hum Mol Genet 8 (6), 959-969 (1999)
   PUBMED   10332027
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Soulard,M., Della Valle,V., Siomi,M.C., Pinol-Roma,S., Codogno,P.,
            Bauvy,C., Bellini,M., Lacroix,J.C., Monod,G., Dreyfuss,G. et al.
  TITLE     hnRNP G: sequence and characterization of a glycosylated
            RNA-binding protein
  JOURNAL   Nucleic Acids Res 21 (18), 4210-4217 (1993)
   PUBMED   7692398
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Le Coniat,M., Soulard,M., Della Valle,V., Larsen,C.J. and Berger,R.
  TITLE     Localization of the human gene encoding heterogeneous nuclear RNA
            ribonucleoprotein G (hnRNP-G) to chromosome 6p12
  JOURNAL   Hum Genet 88 (5), 593-595 (1992)
   PUBMED   1551662
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM147410.1, DC337568.1 and
            BC007435.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 17, 2004 this sequence version replaced NP_002130.1.
            
            Summary: This gene belongs to the RBMY gene family which includes
            candidate Y chromosome spermatogenesis genes. This gene, an active
            X chromosome homolog of the Y chromosome RBMY gene, is widely
            expressed whereas the RBMY gene evolved a male-specific function in
            spermatogenesis. Pseudogenes of this gene, found on chromosomes 1,
            4, 9, 11, and 6, were likely derived by retrotransposition from the
            original gene. Alternatively spliced transcript variants encoding
            different isoforms have been identified. A snoRNA gene (SNORD61) is
            found in one of its introns. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) represents the more frequently
            occurring transcript and it encodes the longer protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.785239.1,
                                           SRR3476690.256439.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000320676.11/ ENSP00000359645.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.3"
     Protein         1..391
                     /product="RNA-binding motif protein, X chromosome isoform
                     1"
                     /note="heterogeneous nuclear ribonucleoprotein G; hnRNP G;
                     glycoprotein p43; RNA-binding motif protein, X chromosome"
                     /calculated_mol_wt=42201
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in Heterogeneous nuclear
                     ribonucleoprotein G, alternate.
                     /evidence=ECO:0000269|Ref.9; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylvaline, in Heterogeneous nuclear
                     ribonucleoprotein G, N-terminally processed.
                     /evidence=ECO:0000269|Ref.9; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Region          7..86
                     /region_name="RRM_RBMX_like"
                     /note="RNA recognition motif (RRM) found in heterogeneous
                     nuclear ribonucleoprotein G (hnRNP G), Y chromosome RNA
                     recognition motif 1 (hRBMY), testis-specific heterogeneous
                     nuclear ribonucleoprotein G-T (hnRNP G-T) and similar
                     proteins; cd12382"
                     /db_xref="CDD:409816"
     Site            order(9,11,13..17,38,40..43,45..51,53,78,80,82..86)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409816"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Region          61..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P38159.3)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Site            125
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV02; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Site            144
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV02; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Site            164
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV02; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Region          165..>306
                     /region_name="dnaA"
                     /note="chromosomal replication initiator protein DnaA;
                     cl42516"
                     /db_xref="CDD:455861"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Site            172
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV02; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Region          173..217
                     /region_name="RBM1CTR"
                     /note="RBM1CTR (NUC064) family; pfam08081"
                     /db_xref="CDD:400429"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Region          186..236
                     /region_name="Necessary for the association to nascent
                     RNAPII transcripts and nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (P38159.3)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P38159.3)"
     Region          333..391
                     /region_name="Necessary for RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P38159.3)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P38159.3)"
     CDS             1..391
                     /gene="RBMX"
                     /gene_synonym="hnRNP-G; HNRNPG; HNRPG; MRXS11; MRXSG;
                     MRXSH; RBMXP1; RBMXRT; RNMX"
                     /coded_by="NM_002139.4:156..1331"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14661.1"
                     /db_xref="GeneID:27316"
                     /db_xref="HGNC:HGNC:9910"
                     /db_xref="MIM:300199"
ORIGIN      
        1 mveadrpgkl figglntetn ekaleavfgk ygrivevllm kdretnksrg fafvtfespa
       61 dakdaardmn gksldgkaik veqatkpsfe sgrrgppppp rsrgpprglr ggrggsggtr
      121 gppsrgghmd dggysmnfnm sssrgplpvk rgppprsggp ppkrsapsgp vrsssgmggr
      181 apvsrgrdsy ggpprreplp srrdvylspr ddgystkdsy ssrdypssrd trdyappprd
      241 ytyrdyghss srddypsrgy sdrdgygrdr dysdhpsggs yrdsyesygn srsapptrgp
      301 ppsyggssry ddysssrdgy ggsrdsysss rsdlyssgrd rvgrqerglp psmergyppp
      361 rdsyssssrg aprgggrggs rsdrgggrsr y
//
LOCUS       NP_001356186            1500 aa            linear   PRI 27-APR-2025
DEFINITION  carbamoyl-phosphate synthase [ammonia], mitochondrial isoform b
            precursor [Homo sapiens].
ACCESSION   NP_001356186
VERSION     NP_001356186.1
DBSOURCE    REFSEQ: accession NM_001369257.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1500)
  AUTHORS   Dong,H., Sang,T., Ma,X., Song,J., Chen,Z., Zhang,H., Jin,Y., Li,M.,
            Dong,D., Sun,L., Zhu,Z., Zhang,Y. and Yang,Y.
  TITLE     Clinical features and CPS1 variants in Chinese patients with
            carbamoyl phosphate synthetase 1 deficiency
  JOURNAL   BMC Pediatr 24 (1), 539 (2024)
   PUBMED   39174957
  REMARK    GeneRIF: Clinical features and CPS1 variants in Chinese patients
            with carbamoyl phosphate synthetase 1 deficiency.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1500)
  AUTHORS   Kwan,R., Chen,L., Park,M.J., Su,Z., Weerasinghe,S.V.W., Lee,W.M.,
            Durkalski-Mauldin,V.L., Fontana,R.J. and Omary,M.B.
  TITLE     The Role of Carbamoyl Phosphate Synthetase 1 as a Prognostic
            Biomarker in Patients With Acetaminophen-induced Acute Liver
            Failure
  JOURNAL   Clin Gastroenterol Hepatol 21 (12), 3060-3069 (2023)
   PUBMED   37054752
  REMARK    GeneRIF: The Role of Carbamoyl Phosphate Synthetase 1 as a
            Prognostic Biomarker in Patients With Acetaminophen-induced Acute
            Liver Failure.
REFERENCE   3  (residues 1 to 1500)
  AUTHORS   Gragnaniello,V., Gueraldi,D., Puma,A., Commone,A., Loro,C.,
            Cazzorla,C., Haberle,J. and Burlina,A.B.
  TITLE     Variant in the allosteric domain of CPS1 protein associated with
            effectiveness of N-carbamoyl glutamate therapy in neonatal onset
            CPS1 deficiency
  JOURNAL   J Pediatr Endocrinol Metab 36 (9), 873-878 (2023)
   PUBMED   37427576
  REMARK    GeneRIF: Variant in the allosteric domain of CPS1 protein
            associated with effectiveness of N-carbamoyl glutamate therapy in
            neonatal onset CPS1 deficiency.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1500)
  AUTHORS   Huo,R., Zhu,H., Lu,L., Ying,L., Xu,M., Xu,Z., Li,J., Zhou,Z. and
            Sha,J.
  TITLE     Molecular cloning, identification and characteristics of a novel
            isoform of carbamyl phosphate synthetase I in human testis
  JOURNAL   J Biochem Mol Biol 38 (1), 28-33 (2005)
   PUBMED   15715943
REFERENCE   5  (residues 1 to 1500)
  AUTHORS   Hoshide,R., Soejima,H., Ohta,T., Niikawa,N., Haraguchi,Y.,
            Matsuura,T., Endo,F. and Matsuda,I.
  TITLE     Assignment of the human carbamyl phosphate synthetase I gene (CPS1)
            to 2q35 by fluorescence in situ hybridization
  JOURNAL   Genomics 28 (1), 124-125 (1995)
   PUBMED   7590739
REFERENCE   6  (residues 1 to 1500)
  AUTHORS   Hoshide,R., Matsuura,T., Haraguchi,Y., Endo,F., Yoshinaga,M. and
            Matsuda,I.
  TITLE     Carbamyl phosphate synthetase I deficiency. One base substitution
            in an exon of the CPS I gene causes a 9-basepair deletion due to
            aberrant splicing
  JOURNAL   J Clin Invest 91 (5), 1884-1887 (1993)
   PUBMED   8486760
REFERENCE   7  (residues 1 to 1500)
  AUTHORS   Ah Mew,N., Simpson,K.L., Gropman,A.L., Lanpher,B.C., Chapman,K.A.
            and Summar,M.L.
  TITLE     Urea Cycle Disorders Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301396
REFERENCE   8  (residues 1 to 1500)
  AUTHORS   Haraguchi,Y., Uchino,T., Takiguchi,M., Endo,F., Mori,M. and
            Matsuda,I.
  TITLE     Cloning and sequence of a cDNA encoding human carbamyl phosphate
            synthetase I: molecular analysis of hyperammonemia
  JOURNAL   Gene 107 (2), 335-340 (1991)
   PUBMED   1840546
REFERENCE   9  (residues 1 to 1500)
  AUTHORS   Liu,T.H., Li,D.C., Gu,C.F. and Ye,S.F.
  TITLE     Carbamyl phosphate synthetase I. A novel marker for gastric
            carcinoma
  JOURNAL   Chin Med J (Engl) 102 (8), 630-638 (1989)
   PUBMED   2517620
REFERENCE   10 (residues 1 to 1500)
  AUTHORS   Pierson,D.L. and Brien,J.M.
  TITLE     Human carbamylphosphate synthetase I. Stabilization, purification,
            and partial characterization of the enzyme from human liver
  JOURNAL   J Biol Chem 255 (16), 7891-7895 (1980)
   PUBMED   6249820
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007970.3 and AC008172.2.
            
            Summary: The mitochondrial enzyme encoded by this gene catalyzes
            synthesis of carbamoyl phosphate from ammonia and bicarbonate. This
            reaction is the first committed step of the urea cycle, which is
            important in the removal of excess urea from cells. The encoded
            protein may also represent a core mitochondrial nucleoid protein.
            Three transcript variants encoding different isoforms have been
            found for this gene. The shortest isoform may not be localized to
            the mitochondrion. Mutations in this gene have been associated with
            carbamoyl phosphate synthetase deficiency, susceptibility to
            persistent pulmonary hypertension, and susceptibility to
            venoocclusive disease after bone marrow transplantation.[provided
            by RefSeq, May 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.248665.1,
                                           SRR1660803.140911.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1500
                     /product="carbamoyl-phosphate synthase [ammonia],
                     mitochondrial isoform b precursor"
                     /EC_number="6.3.4.16"
                     /note="carbamoylphosphate synthetase I;
                     carbamoyl-phosphate synthase 1, mitochondrial;
                     carbamoyl-phosphate synthase (ammonia)"
                     /calculated_mol_wt=160550
     transit_peptide 1..38
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P31327.2)"
                     /calculated_mol_wt=4408
     mat_peptide     39..1500
                     /product="Carbamoyl-phosphate synthase [ammonia],
                     mitochondrial. /id=PRO_0000029897"
                     /note="propagated from UniProtKB/Swiss-Prot (P31327.2)"
                     /calculated_mol_wt=160550
     Region          39..218
                     /region_name="Anthranilate phosphoribosyltransferase
                     homolog"
                     /note="propagated from UniProtKB/Swiss-Prot (P31327.2)"
     Region          46..400
                     /region_name="CPSaseIIsmall"
                     /note="carbamoyl-phosphate synthase, small subunit;
                     TIGR01368"
                     /db_xref="CDD:273580"
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            57
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            119
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            157
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            182
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            197
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            207
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            210
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            214
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            219
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            228
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            280
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            287
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            307
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            310
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            412
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Region          419..1477
                     /region_name="CPSaseII_lrg"
                     /note="carbamoyl-phosphate synthase, large subunit;
                     TIGR01369"
                     /db_xref="CDD:273581"
     Site            453
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            458
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            522
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            527
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            532
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            537
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07756; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            553
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            560
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            575
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            612
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            630
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            751
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            757
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            772
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            793
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            811
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            831
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            841
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            856
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            875
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            889
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            892
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07756; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07756; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            908
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            915
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            919
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            935
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1036
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1074
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1079
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07756; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1093
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07756; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1100
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1168
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1183
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1222
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1232
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1269
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1291
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1331
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P31327.2)"
     Site            1332
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P31327.2)"
     Site            1356
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1444
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1471
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1479
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     Site            1486
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P31327.2)"
     CDS             1..1500
                     /gene="CPS1"
                     /gene_synonym="CPSASE1; GATD6; PHN"
                     /coded_by="NM_001369257.1:218..4720"
                     /note="isoform b precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS2393.1"
                     /db_xref="GeneID:1373"
                     /db_xref="HGNC:HGNC:2323"
                     /db_xref="MIM:608307"
ORIGIN      
        1 mtriltafkv vrtlktgfgf tnvtahqkwk fsrpgirlls vkaqtahivl edgtkmkgys
       61 fghpssvage vvfntglggy peaitdpayk gqiltmanpi ignggapdtt aldelglsky
      121 lesngikvsg llvldyskdy nhwlatkslg qwlqeekvpa iygvdtrmlt kiirdkgtml
      181 gkiefegqpv dfvdpnkqnl iaevstkdvk vygkgnptkv vavdcgiknn virllvkrga
      241 evhlvpwnhd ftkmeydgil iaggpgnpal aepliqnvrk ilesdrkepl fgistgnlit
      301 glaagaktyk msmanrgqnq pvlnitnkqa fitaqnhgya ldntlpagwk plfvnvndqt
      361 negimheskp ffavqfhpev tpgpidteyl fdsffslikk gkattitsvl pkpalvasrv
      421 evskvlilgs gglsigqage fdysgsqavk amkeenvktv lmnpniasvq tnevglkqad
      481 tvyflpitpq fvtevikaeq pdglilgmgg qtalncgvel fkrgvlkeyg vkvlgtsves
      541 imatedrqlf sdklneinek iapsfavesi edalkaadti gypvmirsay algglgsgic
      601 pnretlmdls tkafamtnqi lveksvtgwk eieyevvrda ddncvtvcnm envdamgvht
      661 gdsvvvapaq tlsnaefqml rrtsinvvrh lgivgecniq falhptsmey ciievnarls
      721 rssalaskat gyplafiaak ialgiplpei knvvsgktsa cfepsldymv tkiprwdldr
      781 fhgtssrigs smksvgevma igrtfeesfq kalrmchpsi egftprlpmn kewpsnldlr
      841 kelsepsstr iyaiakaidd nmsldeiekl tyidkwflyk mrdilnmekt lkglnsesmt
      901 eetlkrakei gfsdkqiskc lglteaqtre lrlkknihpw vkqidtlaae ypsvtnylyv
      961 tyngqehdvn fddhgmmvlg cgpyhigssv efdwcavssi rtlrqlgkkt vvvncnpetv
     1021 stdfdecdkl yfeelsleri ldiyhqeacg gciisvggqi pnnlavplyk ngvkimgtsp
     1081 lqidraedrs ifsavldelk vaqapwkavn tlnealefak svdypcllrp syvlsgsamn
     1141 vvfsedemkk fleeatrvsq ehpvvltkfv egarevemda vgkdgrvish aisehvedag
     1201 vhsgdatlml ptqtisqgai ekvkdatrki akafaisgpf nvqflvkgnd vlviecnlra
     1261 srsfpfvskt lgvdfidvat kvmigenvde khlptldhpi ipadyvaika pmfswprlrd
     1321 adpilrcema stgevacfge gihtaflkam lstgfkipqk giligiqqsf rprflgvaeq
     1381 lhnegfklfa teatsdwlna nnvpatpvaw psqegqnpsl ssirklirdg sidlvinlpn
     1441 nntkfvhdny virrtavdsg iplltnfqvt klfaeavqks rkvdskslfh yrqysagkaa
//
LOCUS       NP_071452                646 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-binding cassette sub-family G member 4 isoform a [Homo
            sapiens].
ACCESSION   NP_071452
VERSION     NP_071452.2
DBSOURCE    REFSEQ: accession NM_022169.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Yang,A., Alrosan,A.Z., Sharpe,L.J., Brown,A.J., Callaghan,R. and
            Gelissen,I.C.
  TITLE     Regulation of ABCG4 transporter expression by sterols and LXR
            ligands
  JOURNAL   Biochim Biophys Acta Gen Subj 1865 (1), 129769 (2021)
   PUBMED   33141061
  REMARK    GeneRIF: Regulation of ABCG4 transporter expression by sterols and
            LXR ligands.
            Erratum:[Biochim Biophys Acta Gen Subj. 2022 Aug;1866(8):130169.
            doi: 10.1016/j.bbagen.2022.130169. PMID: 35599093]
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Mallappa,S., Neeli,P.K., Karnewar,S. and Kotamraju,S.
  TITLE     Doxorubicin induces prostate cancer drug resistance by upregulation
            of ABCG4 through GSH depletion and CREB activation: Relevance of
            statins in chemosensitization
  JOURNAL   Mol Carcinog 58 (7), 1118-1133 (2019)
   PUBMED   30834613
  REMARK    GeneRIF: Intriguingly, DU-145 cells with stably depleted ABCG4
            levels not only significantly delayed the development of the tumor
            but also greatly sensitized the tumor to a low dose of doxorubicin
            that resulted in complete tumor regression. Collectively, this data
            reinforces a novel function of ABCG4 in doxorubicin-mediated
            chemoresistance, and as a potential therapeutic target in
            drug-induced prostate cancer chemoresistance.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Alrosan,A., Aleidi,S.M., Yang,A., Brown,A.J. and Gelissen,I.C.
  TITLE     The Adaptor Protein Alix is Involved in the Interaction Between the
            Ubiquitin Ligase NEDD4-1 and its Targets, ABCG1 and ABCG4
  JOURNAL   Int J Mol Sci 20 (11), 2714 (2019)
   PUBMED   31159502
  REMARK    GeneRIF: Alix serves as a co-factor for the interaction between the
            E3-ubiquitin ligase NEDD4-1 and the ABC transporter targets, ABCG1
            and ABCG4.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Oldfield,S., Lowry,C., Ruddick,J. and Lightman,S.
  TITLE     ABCG4: a novel human white family ABC-transporter expressed in the
            brain and eye
  JOURNAL   Biochim Biophys Acta 1591 (1-3), 175-179 (2002)
   PUBMED   12183068
  REMARK    GeneRIF: ABCG4 is expressed specifically in the brain and the eye.
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Yoshikawa,M., Yabuuchi,H., Kuroiwa,A., Ikegami,Y., Sai,Y.,
            Tamai,I., Tsuji,A., Matsuda,Y., Yoshida,H. and Ishikawa,T.
  TITLE     Molecular and cytogenetic characterization of the mouse ATP-binding
            cassette transporter Abcg4
  JOURNAL   Gene 293 (1-2), 67-75 (2002)
   PUBMED   12137944
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Engel,T., Lorkowski,S., Lueken,A., Rust,S., Schluter,B., Berger,G.,
            Cullen,P. and Assmann,G.
  TITLE     The human ABCG4 gene is regulated by oxysterols and retinoids in
            monocyte-derived macrophages
  JOURNAL   Biochem Biophys Res Commun 288 (2), 483-488 (2001)
   PUBMED   11606068
  REMARK    GeneRIF: ABCG4 may be involved in macrophage lipid homeostasis.
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Dean,M., Rzhetsky,A. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Genome Res 11 (7), 1156-1166 (2001)
   PUBMED   11435397
  REMARK    Review article
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Annilo,T., Tammur,J., Hutchinson,A., Rzhetsky,A., Dean,M. and
            Allikmets,R.
  TITLE     Human and mouse orthologs of a new ATP-binding cassette gene, ABCG4
  JOURNAL   Cytogenet Cell Genet 94 (3-4), 196-201 (2001)
   PUBMED   11856881
  REMARK    GeneRIF: Human and mouse orthologs of a new ATP-binding cassette
            gene, ABCG4: maps to human chromosome 11, is expressed abundantly
            in brain, and has alternatively-spliced isoforms
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC041091.1 and DA093690.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 12, 2002 this sequence version replaced NP_071452.1.
            
            Summary: The protein encoded by this gene is a member of the
            ATP-binding cassette (ABC) transporter superfamily. ABC proteins
            transport various molecules across extra- and intra-cellular
            membranes. ABC genes are divided into seven distinct subfamilies
            (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). The encoded protein
            is a member of the White subfamily and plays an important role in
            cellular cholesterol homeostasis. This protein functions as either
            a homodimer or as a heterodimer with another ABC subfamily protein
            such as ABCG1. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1, 2, and 3
            all encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC041091.1, SRR1803615.75799.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000619701.5/ ENSP00000481728.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..646
                     /product="ATP-binding cassette sub-family G member 4
                     isoform a"
                     /note="putative ABC transporter; ATP-binding cassette,
                     sub-family G (WHITE), member 4"
                     /calculated_mol_wt=71765
     Region          44..646
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     Site            394..414
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H172.2)"
     Site            422
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H172.2)"
     Site            426..446
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H172.2)"
     Site            473..493
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H172.2)"
     Site            504..524
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H172.2)"
     Site            533..553
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H172.2)"
     Site            618..638
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H172.2)"
     CDS             1..646
                     /gene="ABCG4"
                     /gene_synonym="WHITE2"
                     /coded_by="NM_022169.5:325..2265"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8415.1"
                     /db_xref="GeneID:64137"
                     /db_xref="HGNC:HGNC:13884"
                     /db_xref="MIM:607784"
ORIGIN      
        1 maekaleavg cglgpgavam avtledgaep pvltthlkkv enhiteaqrf shlpkrsavd
       61 iefvelsysv regpcwrkrg yktllkclsg kfcrreligi mgpsgagkst fmnilagyre
      121 sgmkgqilvn grprelrtfr kmscyimqdd mllphltvle ammvsanlkl sekqevkkel
      181 vteiltalgl mscshtrtal lsggqrkrla ialelvnnpp vmffdeptsg ldsascfqvv
      241 slmkslaqgg rtiictihqp saklfemfdk lyilsqgqci fkgvvtnlip ylkglglhcp
      301 tyhnpadfii evasgeygdl npmlfravqn glcamaekks speknevpap cppcppevdp
      361 ieshtfatst ltqfcilfkr tflsilrdtv lthlrfmshv vigvliglly lhigddaskv
      421 fnntgclffs mlflmfaalm ptvltfplem avfmrehlny wyslkayyla ktmadvpfqv
      481 vcpvvycsiv ywmtgqpaet srfllfsala tatalvaqsl glligaasns lqvatfvgpv
      541 taipvllfsg ffvsfktipt ylqwssylsy vrygfegvil tiygmergdl tcleercpfr
      601 epqsilrald vedaklymdf lvlgifflal rllaylvlry rvkser
//
LOCUS       NP_001347944             889 aa            linear   ROD 27-APR-2025
DEFINITION  TBC1 domain family member 30 isoform 2 [Mus musculus].
ACCESSION   NP_001347944
VERSION     NP_001347944.1
DBSOURCE    REFSEQ: accession NM_001361015.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC140264.2, AC135360.3 and BC059081.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10"
     Protein         1..889
                     /product="TBC1 domain family member 30 isoform 2"
                     /note="TBC1 domain family member 30-like"
                     /calculated_mol_wt=98627
     Region          208..429
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Region          598..726
                     /region_name="DUF4682"
                     /note="Domain of unknown function (DUF4682); pfam15733"
                     /db_xref="CDD:464830"
     CDS             1..889
                     /gene="Tbc1d30"
                     /gene_synonym="4930505D03Rik; 9530013E20Rik"
                     /coded_by="NM_001361015.1:268..2937"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:74694"
                     /db_xref="MGI:MGI:1921944"
ORIGIN      
        1 mevlpagrtw dpqqseeaag hpadegdlep qpdgrtsrta slvsglltel yscteeeeva
       61 aggdrasqgr plrrdsldss tetsgsdafl ggrgagdsrv lqelrerpsl rlqmqylqrk
      121 dsselktvlr elkyrigiqs akllrqlkqk drllhkvqkn cdivtaclqa vsqkrrvdtk
      181 lkftlepslg qngfqqwyda lkavarlstg ipkewrrkvw ltladhylhs iaidwdktmr
      241 ftfnersnpd ddsmgiqivk dlhrtgcssy cgqeaeqdrv vlkrvllaya rwnknvgycq
      301 gfnilaalil evmegnegda lkimiylidk vlpesyfvnn lralsvdmav frdllrlklp
      361 elsqhldtlq rtankesggg yeppltnvft mqwfltlfat clpnhtvlki wdsvffegse
      421 iilrvslaiw aklgeqiecc etadefygtm grltqemleq dllqshelmq tvysmapfpf
      481 pqlaelreky tynitpfpat ikptsvsgrh skardsdden gpddedavas avgclgplsg
      541 llapelqkyq kqikeateeq tlrsnniael spgainscrs eyhaafnsmm mermttdina
      601 lkrqysrikk kqqqqlhqvy iradkgpvts ilpsqanssp vinhlllgkk mkitnraakn
      661 avihvpghpg gkispvpyed iktklnspwr thirvhkknm prtkshlgcg dtvglieeqs
      721 egckasslga aeefpsgrtv tahsegssgd gdgggstprt iegqspepvf gdadvdvaav
      781 qvklealeln qrdaaaetep kvhfpcqrha seladapgen qtaikllpgs tsktpifspf
      841 psvkplrksa tarnlglygp tertpnvhfp qmsrgfnksg ignsstkkr
//
LOCUS       NP_057461                348 aa            linear   PRI 27-APR-2025
DEFINITION  A-kinase anchoring protein 7 isoform gamma [Homo sapiens].
ACCESSION   NP_057461
VERSION     NP_057461.2
DBSOURCE    REFSEQ: accession NM_016377.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 348)
  AUTHORS   O'Connell,G.C., Treadway,M.B., Petrone,A.B., Tennant,C.S.,
            Lucke-Wold,N., Chantler,P.D. and Barr,T.L.
  TITLE     Peripheral blood AKAP7 expression as an early marker for
            lymphocyte-mediated post-stroke blood brain barrier disruption
  JOURNAL   Sci Rep 7 (1), 1172 (2017)
   PUBMED   28446746
  REMARK    GeneRIF: AKAP7 expression levels may have clinical utility as a
            prognostic biomarker for post-stroke blood brain complications
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Bjerregaard-Andersen,K., Ostensen,E., Scott,J.D., Tasken,K. and
            Morth,J.P.
  TITLE     Malonate in the nucleotide-binding site traps human
            AKAP18gamma/delta in a novel conformational state
  JOURNAL   Acta Crystallogr F Struct Biol Commun 72 (Pt 8), 591-597 (2016)
   PUBMED   27487922
  REMARK    GeneRIF: Malonate in the nucleotide-binding site traps human
            AKAP18-gamma in a novel conformational state.
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Burgers,P.P., van der Heyden,M.A., Kok,B., Heck,A.J. and
            Scholten,A.
  TITLE     A systematic evaluation of protein kinase A-A-kinase anchoring
            protein interaction motifs
  JOURNAL   Biochemistry 54 (1), 11-21 (2015)
   PUBMED   25097019
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Greenwald,E.C., Redden,J.M., Dodge-Kafka,K.L. and Saucerman,J.J.
  TITLE     Scaffold state switching amplifies, accelerates, and insulates
            protein kinase C signaling
  JOURNAL   J Biol Chem 289 (4), 2353-2360 (2014)
   PUBMED   24302730
  REMARK    GeneRIF: PKC tethered to AKAP7alpha was less susceptible to
            inhibition from the ATP-competitive inhibitor Go6976 and the
            substrate-competitive inhibitor PKC 20-28, but not the
            activation-competitive inhibitor calphostin C.
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Brown,R.L., August,S.L., Williams,C.J. and Moss,S.B.
  TITLE     AKAP7gamma is a nuclear RI-binding AKAP
  JOURNAL   Biochem Biophys Res Commun 306 (2), 394-401 (2003)
   PUBMED   12804576
  REMARK    GeneRIF: AKAP7gamma is the first nuclear AKAP to bind RI and may be
            responsible for positioning PKA via RI and/or RII to regulate
            PKA-mediated gene transcription in both somatic cells and oocytes
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Alto,N.M., Soderling,S.H., Hoshi,N., Langeberg,L.K., Fayos,R.,
            Jennings,P.A. and Scott,J.D.
  TITLE     Bioinformatic design of A-kinase anchoring protein-in silico: a
            potent and selective peptide antagonist of type II protein kinase A
            anchoring
  JOURNAL   Proc Natl Acad Sci U S A 100 (8), 4445-4450 (2003)
   PUBMED   12672969
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Potet,F., Scott,J.D., Mohammad-Panah,R., Escande,D. and Baro,I.
  TITLE     AKAP proteins anchor cAMP-dependent protein kinase to KvLQT1/IsK
            channel complex
  JOURNAL   Am J Physiol Heart Circ Physiol 280 (5), H2038-H2045 (2001)
   PUBMED   11299204
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Trotter,K.W., Fraser,I.D., Scott,G.K., Stutts,M.J., Scott,J.D. and
            Milgram,S.L.
  TITLE     Alternative splicing regulates the subcellular localization of
            A-kinase anchoring protein 18 isoforms
  JOURNAL   J Cell Biol 147 (7), 1481-1492 (1999)
   PUBMED   10613906
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Fraser,I.D., Tavalin,S.J., Lester,L.B., Langeberg,L.K.,
            Westphal,A.M., Dean,R.A., Marrion,N.V. and Scott,J.D.
  TITLE     A novel lipid-anchored A-kinase Anchoring Protein facilitates
            cAMP-responsive membrane events
  JOURNAL   EMBO J 17 (8), 2261-2272 (1998)
   PUBMED   9545239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL137222.17, DN998807.1,
            AK300587.1 and BC110897.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 28, 2011 this sequence version replaced NP_057461.1.
            
            Summary: This gene encodes a member of the A-kinase anchoring
            protein (AKAP) family, a group of functionally related proteins
            that bind to a regulatory subunit (RII) of cAMP-dependent protein
            kinase A (PKA) and target the enzyme to specific subcellular
            compartments. AKAPs have a common RII-binding domain, but contain
            different targeting motifs responsible for directing PKA to
            distinct intracellular locations. Three alternatively spliced
            transcript variants encoding different isoforms have been
            described.[provided by RefSeq, Apr 2011].
            
            Transcript Variant: This variant (gamma) differs in he 5' UTR and
            has multiple difference in the coding region, compared to variant
            alpha. The encoded isoform (gamma) is longer and has a distinct
            N-terminus, compared to isoform alpha.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.16846.1,
                                           SRR1803615.246646.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000431975.7/
                                                ENSP00000405252.2
            RefSeq Select criteria           :: based on manual assertion,
                                                conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.2"
     Protein         1..348
                     /product="A-kinase anchoring protein 7 isoform gamma"
                     /note="A-kinase anchor protein 9 kDa; AKAP 18; A-kinase
                     anchor protein 18 kDa; A kinase (PRKA) anchor protein 7"
                     /calculated_mol_wt=39387
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0M2.2)"
     Region          85..283
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     Region          290..345
                     /region_name="AKAP7_RIRII_bdg"
                     /note="PKA-RI-RII subunit binding domain of A-kinase
                     anchor protein; pfam10470"
                     /db_xref="CDD:463101"
     Region          294..348
                     /region_name="PKA-RII-alpha subunit binding domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0M2.2)"
     Region          295..319
                     /region_name="RI-alpha-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0M2.2)"
     Region          296..309
                     /region_name="RII-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0M2.2)"
     Region          316..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0M2.2)"
     CDS             1..348
                     /gene="AKAP7"
                     /gene_synonym="AKAP15; AKAP18"
                     /coded_by="NM_016377.4:298..1344"
                     /note="isoform gamma is encoded by transcript variant
                     gamma"
                     /db_xref="CCDS:CCDS5142.2"
                     /db_xref="GeneID:9465"
                     /db_xref="HGNC:HGNC:377"
                     /db_xref="MIM:604693"
ORIGIN      
        1 merpeaggin snecenvsrk kkmseefean tmdslvdmpf atvdiqddcg itdepqinlk
       61 rsqenewvks dqvkkrkkkr kdyqpnyfls ipitnkeiik gikilqnaii qqderlakam
      121 vsdgsfhitl lvmqllnede vnigidalle lkpfieellq gkhltlpfqg igtfgnqvgf
      181 vklaegdhvn slleiaetan rtfqekgilv gesrsfkphl tfmklskspw lrkngvkkid
      241 pdlyekfish rfgeeilyri dlcsmlkkkq sngyyhcess ivigekngge pddaelvrls
      301 krlvenavlk avqqyleetq nknkpgegss vkteaadqng ndnennrk
//
LOCUS       NP_783597                126 aa            linear   ROD 27-APR-2025
DEFINITION  histone H2B type 2-B [Mus musculus].
ACCESSION   NP_783597
VERSION     NP_783597.2
DBSOURCE    REFSEQ: accession NM_175666.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Doyle,H.A., Aswad,D.W. and Mamula,M.J.
  TITLE     Autoimmunity to isomerized histone H2B in systemic lupus
            erythematosus
  JOURNAL   Autoimmunity 46 (1), 6-13 (2013)
   PUBMED   22967069
  REMARK    GeneRIF: Autoimmunity to isoAsp H2B suggests that this form of the
            autoantigen may be critical in the induction of anti-histone
            autoantibodies in murine models of human SLE.
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Santoro,S.W. and Dulac,C.
  TITLE     The activity-dependent histone variant H2BE modulates the life span
            of olfactory neurons
  JOURNAL   Elife 1, e00070 (2012)
   PUBMED   23240083
  REMARK    GeneRIF: The activity-dependent histone variant H2BE modulates the
            life span of olfactory neurons.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Das,R., Burke,T. and Plow,E.F.
  TITLE     Histone H2B as a functionally important plasminogen receptor on
            macrophages
  JOURNAL   Blood 110 (10), 3763-3772 (2007)
   PUBMED   17690254
  REMARK    GeneRIF: H2B plays a very prominent and functionally important role
            as plasminogen receptor.
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Kim,S.C., Sprung,R., Chen,Y., Xu,Y., Ball,H., Pei,J., Cheng,T.,
            Kho,Y., Xiao,H., Xiao,L., Grishin,N.V., White,M., Yang,X.J. and
            Zhao,Y.
  TITLE     Substrate and functional diversity of lysine acetylation revealed
            by a proteomics survey
  JOURNAL   Mol Cell 23 (4), 607-618 (2006)
   PUBMED   16916647
REFERENCE   5  (residues 1 to 126)
  AUTHORS   Odegard,V.H., Kim,S.T., Anderson,S.M., Shlomchik,M.J. and
            Schatz,D.G.
  TITLE     Histone modifications associated with somatic hypermutation
  JOURNAL   Immunity 23 (1), 101-110 (2005)
   PUBMED   16039583
REFERENCE   6  (residues 1 to 126)
  AUTHORS   Fernandez-Capetillo,O., Allis,C.D. and Nussenzweig,A.
  TITLE     Phosphorylation of histone H2B at DNA double-strand breaks
  JOURNAL   J Exp Med 199 (12), 1671-1677 (2004)
   PUBMED   15197225
REFERENCE   7  (residues 1 to 126)
  AUTHORS   Marzluff,W.F., Gongidi,P., Woods,K.R., Jin,J. and Maltais,L.J.
  TITLE     The human and mouse replication-dependent histone genes
  JOURNAL   Genomics 80 (5), 487-498 (2002)
   PUBMED   12408966
REFERENCE   8  (residues 1 to 126)
  AUTHORS   Bolognese,F., Imbriano,C., Caretti,G. and Mantovani,R.
  TITLE     Cloning and characterization of the histone-fold proteins YBL1 and
            YCL1
  JOURNAL   Nucleic Acids Res 28 (19), 3830-3838 (2000)
   PUBMED   11000277
REFERENCE   9  (residues 1 to 126)
  AUTHORS   Wang,Z.F., Tisovec,R., Debry,R.W., Frey,M.R., Matera,A.G. and
            Marzluff,W.F.
  TITLE     Characterization of the 55-kb mouse histone gene cluster on
            chromosome 3
  JOURNAL   Genome Res 6 (8), 702-714 (1996)
   PUBMED   8858345
REFERENCE   10 (residues 1 to 126)
  AUTHORS   Ko,M.S.
  TITLE     An 'equalized cDNA library' by the reassociation of short
            double-stranded cDNAs
  JOURNAL   Nucleic Acids Res 18 (19), 5705-5711 (1990)
   PUBMED   2216762
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125099.3.
            
            On Jun 25, 2005 this sequence version replaced NP_783597.1.
            
            Summary: Histones are basic nuclear proteins that are responsible
            for the nucleosome structure of the chromosomal fiber in
            eukaryotes. Two molecules of each of the four core histones (H2A,
            H2B, H3, and H4) form an octamer, around which approximately 146 bp
            of DNA is wrapped in repeating units, called nucleosomes. The
            linker histone, H1, interacts with linker DNA between nucleosomes
            and functions in the compaction of chromatin into higher order
            structures. This gene encodes a replication-dependent histone that
            is a member of the histone H2B family. [provided by RefSeq, Aug
            2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR7345562.2184524.1,
                                        ERR3363658.5692255.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria        :: based on single protein-coding
                                             transcript
            replication-dependent histone :: PMID: 12408966
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3 41.71 cM"
     Protein         1..126
                     /product="histone H2B type 2-B"
                     /note="H2b 616; histone 2, H2bb; histone cluster 2, H2bb"
                     /calculated_mol_wt=13789
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64525.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylproline.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            12
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            13
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P33778; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by STK4/MST1.
                     /evidence=ECO:0000269|PubMed:15197225,
                     ECO:0000269|PubMed:16039583; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            16
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P33778; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            17
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            24
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P33778; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Region          30..123
                     /region_name="HFD_H2B"
                     /note="histone-fold domain found in histone H2B and
                     similar proteins; cd22910"
                     /db_xref="CDD:467035"
     Site            order(31,33,36,38,40..42,44..46,49..56,58..59,62..63,
                     66..67,69..71,73..75,79,89..90,92,95..96,99,102..104,107,
                     110..112,114..115,118..119,122..123)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            order(31..37,40..41,43,54..56,89)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:467035"
     Site            order(35,39..41,43..44,47..49,54..56,60,96,100,109..110,
                     112..113,116..117,119..120,123)
                     /site_type="other"
                     /note="Hif1 binding site [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:20647423,
                     ECO:0000269|PubMed:32822587; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            47
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            58
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            order(62,65..66,68..69,72,77,80,83..85,93..94,97,101..102)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            80
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            86
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            86
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            87
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            93
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            109
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            113
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q00729; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     Site            117
                     /site_type="methylation"
                     /note="N6-methylated lysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00729; propagated from
                     UniProtKB/Swiss-Prot (Q64525.3)"
     CDS             1..126
                     /gene="H2bc18"
                     /gene_synonym="H2b-616; Hist2h2bb"
                     /coded_by="NM_175666.3:53..433"
                     /db_xref="CCDS:CCDS57243.1"
                     /db_xref="GeneID:319189"
                     /db_xref="MGI:MGI:2448413"
ORIGIN      
        1 mpdpaksapa pkkgskkavt kvqkkdgkkr krsrkesysv yvykvlkqvh pdtgisskam
       61 gimnsfvndi feriageasr lahynkrsti tsreiqtavr lllpgelakh avsegtkavt
      121 kytssk
//
LOCUS       NP_002950                831 aa            linear   PRI 27-APR-2025
DEFINITION  sortilin isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_002950
VERSION     NP_002950.3
DBSOURCE    REFSEQ: accession NM_002959.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Vukolova,Y., Gubareva,I., Galati,G. and Germanova,O.
  TITLE     Diagnostic utility of sortilin & other biomarkers in the diagnosis
            of carotid & coronary atherosclerosis in individuals with arterial
            hypertension
  JOURNAL   Indian J Med Res 159 (5), 511-518 (2024)
   PUBMED   39382416
  REMARK    GeneRIF: Diagnostic utility of sortilin & other biomarkers in the
            diagnosis of carotid & coronary atherosclerosis in individuals with
            arterial hypertension.
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Bolduan,F., Wetzel,A., Giesecke,Y., Eichhorn,I., Alenina,N.,
            Bader,M., Willnow,T.E., Wiedenmann,B. and Sigal,M.
  TITLE     Elevated sortilin expression discriminates functional from
            non-functional neuroendocrine tumors and enables therapeutic
            targeting
  JOURNAL   Front Endocrinol (Lausanne) 15, 1331231 (2024)
   PUBMED   38694940
  REMARK    GeneRIF: Elevated sortilin expression discriminates functional from
            non-functional neuroendocrine tumors and enables therapeutic
            targeting.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Atak,M., Sevim Nalkiran,H., Bostan,M. and Uydu,H.A.
  TITLE     The association of Sort1 expression with LDL subfraction and
            inflammation in patients with coronary artery disease
  JOURNAL   Acta Cardiol 79 (2), 159-166 (2024)
   PUBMED   38095557
  REMARK    GeneRIF: The association of Sort1 expression with LDL subfraction
            and inflammation in patients with coronary artery disease.
REFERENCE   4  (residues 1 to 831)
  AUTHORS   Georgoula,M., Ntavaroukas,P., Androutsopoulou,A., Xiromerisiou,G.,
            Kalala,F., Speletas,M., Asprodini,E., Vasilaki,A. and
            Papoutsopoulou,S.
  TITLE     Sortilin Expression Levels and Peripheral Immunity: A Potential
            Biomarker for Segregation between Parkinson's Disease Patients and
            Healthy Controls
  JOURNAL   Int J Mol Sci 25 (3), 1791 (2024)
   PUBMED   38339069
  REMARK    GeneRIF: Sortilin Expression Levels and Peripheral Immunity: A
            Potential Biomarker for Segregation between Parkinson's Disease
            Patients and Healthy Controls.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 831)
  AUTHORS   Carlo,A.S., Nykjaer,A. and Willnow,T.E.
  TITLE     Sorting receptor sortilin-a culprit in cardiovascular and
            neurological diseases
  JOURNAL   J Mol Med (Berl) 92 (9), 905-911 (2014)
   PUBMED   24838608
  REMARK    GeneRIF: This article describes the molecular mechanisms of
            sortilin action in protein sorting and signaling and how modulation
            of receptor function may offer therapeutic strategies for treatment
            of diseases of the cardiovascular and nervous systems. [review]
            Review article
REFERENCE   6  (residues 1 to 831)
  AUTHORS   Mazella,J., Zsurger,N., Navarro,V., Chabry,J., Kaghad,M., Caput,D.,
            Ferrara,P., Vita,N., Gully,D., Maffrand,J.P. and Vincent,J.P.
  TITLE     The 100-kDa neurotensin receptor is gp95/sortilin, a
            non-G-protein-coupled receptor
  JOURNAL   J Biol Chem 273 (41), 26273-26276 (1998)
   PUBMED   9756851
REFERENCE   7  (residues 1 to 831)
  AUTHORS   Tauris,J., Ellgaard,L., Jacobsen,C., Nielsen,M.S., Madsen,P.,
            Thogersen,H.C., Gliemann,J., Petersen,C.M. and Moestrup,S.K.
  TITLE     The carboxy-terminal domain of the receptor-associated protein
            binds to the Vps10p domain of sortilin
  JOURNAL   FEBS Lett 429 (1), 27-30 (1998)
   PUBMED   9657377
REFERENCE   8  (residues 1 to 831)
  AUTHORS   Lin,B.Z., Pilch,P.F. and Kandror,K.V.
  TITLE     Sortilin is a major protein component of Glut4-containing vesicles
  JOURNAL   J Biol Chem 272 (39), 24145-24147 (1997)
   PUBMED   9305862
REFERENCE   9  (residues 1 to 831)
  AUTHORS   Petersen,C.M., Nielsen,M.S., Nykjaer,A., Jacobsen,L., Tommerup,N.,
            Rasmussen,H.H., Roigaard,H., Gliemann,J., Madsen,P. and
            Moestrup,S.K.
  TITLE     Molecular identification of a novel candidate sorting receptor
            purified from human brain by receptor-associated protein affinity
            chromatography
  JOURNAL   J Biol Chem 272 (6), 3599-3605 (1997)
   PUBMED   9013611
REFERENCE   10 (residues 1 to 831)
  AUTHORS   Zsurger,N., Mazella,J. and Vincent,J.P.
  TITLE     Solubilization and purification of a high affinity neurotensin
            receptor from newborn human brain
  JOURNAL   Brain Res 639 (2), 245-252 (1994)
   PUBMED   8205478
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC023542.1, DB045034.1,
            DA023768.1 and AL390252.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 29, 2001 this sequence version replaced NP_002950.2.
            
            Summary: This gene encodes a member of the VPS10-related sortilin
            family of proteins. The encoded preproprotein is proteolytically
            processed by furin to generate the mature receptor. This receptor
            plays a role in the trafficking of different proteins to either the
            cell surface, or subcellular compartments such as lysosomes and
            endosomes. Expression levels of this gene may influence the risk of
            myocardial infarction in human patients. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.167059.1,
                                           SRR1660803.40652.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256637.8/ ENSP00000256637.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..831
                     /product="sortilin isoform 1 preproprotein"
                     /note="neurotensin receptor 3; glycoprotein 95; 100 kDa NT
                     receptor"
                     /calculated_mol_wt=88490
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3596
     Region          50..61
                     /region_name="Intrachain binding of the propeptide and the
                     extracellular domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     mat_peptide     78..831
                     /product="Sortilin. /id=PRO_0000033163"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
                     /calculated_mol_wt=83862
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q99523.3)"
     Region          133..741
                     /region_name="VPS10"
                     /note="VPS10 domain; smart00602"
                     /db_xref="CDD:214740"
     Region          145..156
                     /region_name="BNR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16263699,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q99523.3)"
     Region          198..209
                     /region_name="BNR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Region          240..251
                     /region_name="BNR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Site            274
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99523.3)"
     Region          287..298
                     /region_name="BNR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Region          328..339
                     /region_name="BNR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Region          377..388
                     /region_name="BNR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19122660; propagated from
                     UniProtKB/Swiss-Prot (Q99523.3)"
     Region          428..439
                     /region_name="BNR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Region          506..517
                     /region_name="BNR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Region          548..559
                     /region_name="BNR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Site            582
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19122660; propagated from
                     UniProtKB/Swiss-Prot (Q99523.3)"
     Region          612..756
                     /region_name="Interactions with LRPAP1 and NGFB"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Site            684
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99523.3)"
     Site            756..778
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Region          779..831
                     /region_name="Golgi to endosome transport and interactions
                     with GGA1 and GGA2. /evidence=ECO:0000269|PubMed:16787399"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Region          787..792
                     /region_name="Endocytosis signal. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99523.3)"
     Site            819
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q99523.3)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     Region          826..830
                     /region_name="DXXLL motif involved in the interaction with
                     GGA1. /evidence=ECO:0000269|PubMed:20015111"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99523.3)"
     CDS             1..831
                     /gene="SORT1"
                     /gene_synonym="Gp95; LDLCQ6; NT3; NTR3"
                     /coded_by="NM_002959.7:27..2522"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS798.1"
                     /db_xref="GeneID:6272"
                     /db_xref="HGNC:HGNC:11186"
                     /db_xref="MIM:602458"
ORIGIN      
        1 merpwgaadg lsrwphglgl llllqllpps tlsqdrldap pppaaplprw sgpigvswgl
       61 raaaaggafp rggrwrrsap gedeecgrvr dfvaklannt hqhvfddlrg svslswvgds
      121 tgvilvlttf hvplvimtfg qsklyrsedy gknfkditdl inntfirtef gmaigpensg
      181 kvvltaevsg gsrggrifrs sdfaknfvqt dlpfhpltqm myspqnsdyl lalstenglw
      241 vsknfggkwe eihkavclak wgsdntifft tyangsckad lgalelwrts dlgksfktig
      301 vkiysfglgg rflfasvmad kdttrrihvs tdqgdtwsma qlpsvgqeqf ysilaanddm
      361 vfmhvdepgd tgfgtiftsd drgivysksl drhlytttgg etdftnvtsl rgvyitsvls
      421 ednsiqtmit fdqggrwthl rkpensecda taknknecsl hihasysisq klnvpmapls
      481 epnavgivia hgsvgdaisv mvpdvyisdd ggyswtkmle gphyytilds ggiivaiehs
      541 srpinvikfs tdegqcwqty tftrdpiyft glasepgars mnisiwgfte sfltsqwvsy
      601 tidfkdiler nceekdytiw lahstdpedy edgcilgyke qflrlrkssv cqngrdyvvt
      661 kqpsiclcsl edflcdfgyy rpendskcve qpelkghdle fclygreehl ttngyrkipg
      721 dkcqggvnpv revkdlkkkc tsnflspekq nsksnsvpii laivglmlvt vvagvlivkk
      781 yvcggrflvh rysvlqqhae angvdgvdal dtashtnksg yhddsdedll e
//
LOCUS       NP_001354461             510 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 25 [Homo sapiens].
ACCESSION   NP_001354461 XP_016872222
VERSION     NP_001354461.1
DBSOURCE    REFSEQ: accession NM_001367532.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 510)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 510)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_016872222.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.297217.1,
                                           SRR3476690.48584.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..510
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 25"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=57361
     Region          12..295
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..22,33,35,66,82..85,89,91,127..128,130,132..133,
                     135,148..149,152,167..171,173)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..22,33,35,66,82..85,89,132..133,135,148..149)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(89,91,127..128,130,132,152,167..171,173)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(148..158,161..171)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(286,288..295)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          378..505
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..510
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367532.1:95..1627"
                     /note="isoform 25 is encoded by transcript variant 25"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkcvkktstq eyaakiintk klsardhqkl erearicrll
       61 khpnivrlhd siseegfhyl vfdlvtggel fedivareyy seadashcih qilesvnhih
      121 qhdivhrdlk penlllaskc kgaavkladf glaievqgeq qawfgfagtp gylspevlrk
      181 dpygkpvdiw acgvilyill vgyppfwded qhklyqqika gaydfpspew dtvtpeaknl
      241 inqmltinpa kritadqalk hpwvcqrstv asmmhrqetv eclrkfnarr klkgailttm
      301 lvsrnfsaak sllnkksdgg vkpqsnnkns lvspaqepap lqtamepqtt vvhnatdgik
      361 gstescnttt ededlkvrkq eiikiteqli eainngdfea ytkicdpglt sfepealgnl
      421 vegmdfhkfy fenllsknsk pihttilnph vhvigedaac iayirltqyi dgqgrprtsq
      481 seetrvwhrr dgkwlnvhyh csgapaaplq
//
LOCUS       NP_000894                274 aa            linear   PRI 27-APR-2025
DEFINITION  NAD(P)H dehydrogenase [quinone] 1 isoform a [Homo sapiens].
ACCESSION   NP_000894
VERSION     NP_000894.1
DBSOURCE    REFSEQ: accession NM_000903.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Zhou,Y., Chen,Y., Xuan,C., Li,X., Tan,Y., Yang,M., Cao,M., Chen,C.,
            Huang,X. and Hu,R.
  TITLE     DPP9 regulates NQO1 and ROS to promote resistance to chemotherapy
            in liver cancer cells
  JOURNAL   Redox Biol 75, 103292 (2024)
   PUBMED   39094401
  REMARK    GeneRIF: DPP9 regulates NQO1 and ROS to promote resistance to
            chemotherapy in liver cancer cells.
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Chen,H., Li,H., He,M., Lai,Z., Huang,L., Wen,D., Shi,M. and Kan,A.
  TITLE     UBA2 SUMOylates NQO1 and promotes the proliferation of
            hepatocellular carcinoma by modulating the MAPK pathway
  JOURNAL   Cancer Sci 115 (9), 2998-3012 (2024)
   PUBMED   39013843
  REMARK    GeneRIF: UBA2 SUMOylates NQO1 and promotes the proliferation of
            hepatocellular carcinoma by modulating the MAPK pathway.
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Wang,M., Shen,Y., Gao,Y., Chen,H., Duan,F., Li,S. and Wang,G.
  TITLE     NQO1 polymorphism and susceptibility to ischemic stroke in a
            Chinese population
  JOURNAL   BMC Med Genomics 17 (1), 219 (2024)
   PUBMED   39174970
  REMARK    GeneRIF: NQO1 polymorphism and susceptibility to ischemic stroke in
            a Chinese population.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Zhang,X., Yang,Y., Zhao,H., Tian,Z., Cao,Q., Li,Y., Gu,Y., Song,Q.,
            Hu,X., Jin,M. and Jiang,X.
  TITLE     Correlation of PD-L1 expression with CD8+ T cells and oxidative
            stress-related molecules NRF2 and NQO1 in esophageal squamous cell
            carcinoma
  JOURNAL   J Pathol Clin Res 10 (4), e12390 (2024)
   PUBMED   38992928
  REMARK    GeneRIF: Correlation of PD-L1 expression with CD8+ T cells and
            oxidative stress-related molecules NRF2 and NQO1 in esophageal
            squamous cell carcinoma.
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Matsumoto,H., Sasai,H., Kawamoto,N., Katsuyama,M., Minamiyama,M.,
            Kuru,S., Fukao,T. and Ohnishi,H.
  CONSRTM   SMON Research Group Members
  TITLE     Loss-of-function polymorphisms in NQO1 are not associated with the
            development of subacute myelo-optico-neuropathy
  JOURNAL   Mol Genet Genomic Med 12 (6), e2470 (2024)
   PUBMED   38860482
  REMARK    GeneRIF: Loss-of-function polymorphisms in NQO1 are not associated
            with the development of subacute myelo-optico-neuropathy.
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Li,Y. and Jaiswal,A.K.
  TITLE     Regulation of human NAD(P)H:quinone oxidoreductase gene. Role of
            AP1 binding site contained within human antioxidant response
            element
  JOURNAL   J Biol Chem 267 (21), 15097-15104 (1992)
   PUBMED   1340765
  REMARK    Erratum:[J Biol Chem. 1993 Oct 5;268(28):21454. PMID: 8407991]
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Traver,R.D., Horikoshi,T., Danenberg,K.D., Stadlbauer,T.H.,
            Danenberg,P.V., Ross,D. and Gibson,N.W.
  TITLE     NAD(P)H:quinone oxidoreductase gene expression in human colon
            carcinoma cells: characterization of a mutation which modulates
            DT-diaphorase activity and mitomycin sensitivity
  JOURNAL   Cancer Res 52 (4), 797-802 (1992)
   PUBMED   1737339
REFERENCE   8  (residues 1 to 274)
  AUTHORS   Jaiswal,A.K.
  TITLE     Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and
            induction by dioxin
  JOURNAL   Biochemistry 30 (44), 10647-10653 (1991)
   PUBMED   1657151
REFERENCE   9  (residues 1 to 274)
  AUTHORS   Chen,L.Z., Harris,P.C., Apostolou,S., Baker,E., Holman,K.,
            Lane,S.A., Nancarrow,J.K., Whitmore,S.A., Stallings,R.L.,
            Hildebrand,C.E. et al.
  TITLE     A refined physical map of the long arm of human chromosome 16
  JOURNAL   Genomics 10 (2), 308-312 (1991)
   PUBMED   2071140
REFERENCE   10 (residues 1 to 274)
  AUTHORS   Jaiswal,A.K., McBride,O.W., Adesnik,M. and Nebert,D.W.
  TITLE     Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase.
            cDNA sequence and localization of gene to chromosome 16
  JOURNAL   J Biol Chem 263 (27), 13572-13578 (1988)
   PUBMED   2843525
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM452267.1, BC007659.2,
            BM052991.1, BM787983.1, BM828301.1 and AV729122.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the NAD(P)H dehydrogenase
            (quinone) family and encodes a cytoplasmic 2-electron reductase.
            This FAD-binding protein forms homodimers and reduces quinones to
            hydroquinones. This protein's enzymatic activity prevents the one
            electron reduction of quinones that results in the production of
            radical species. Mutations in this gene have been associated with
            tardive dyskinesia (TD), an increased risk of hematotoxicity after
            exposure to benzene, and susceptibility to various forms of cancer.
            Altered expression of this protein has been seen in many tumors and
            is also associated with Alzheimer's disease (AD). Alternate
            transcriptional splice variants, encoding different isoforms, have
            been characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.15706.1,
                                           SRR1803614.237687.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153946, SAMEA2154405
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000320623.10/ ENSP00000319788.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..274
                     /product="NAD(P)H dehydrogenase [quinone] 1 isoform a"
                     /EC_number="1.6.5.2"
                     /note="diaphorase (NADH/NADPH) (cytochrome b-5 reductase);
                     NAD(P)H:Quinone acceptor oxidoreductase type 1; quinone
                     reductase 1; DT-diaphorase; azoreductase; phylloquinone
                     reductase; menadione reductase; NAD(P)H:quinone
                     oxireductase; dioxin-inducible 1; NAD(P)H:menadione
                     oxidoreductase 1; diaphorase-4; NAD(P)H dehydrogenase,
                     quinone 1; NAD(P)H:quinone oxidoreductase 1;
                     NAD(P)H-quinone oxidoreductase"
                     /calculated_mol_wt=30737
     Region          5..216
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15559.1)"
     Region          225..274
                     /region_name="Important for apoenzyme conformational
                     stability. /evidence=ECO:0000269|PubMed:28291250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15559.1)"
     CDS             1..274
                     /gene="NQO1"
                     /gene_synonym="DHQU; DIA4; DTD; NMOR1; NMORI; QR1"
                     /coded_by="NM_000903.3:122..946"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10883.1"
                     /db_xref="GeneID:1728"
                     /db_xref="HGNC:HGNC:2874"
                     /db_xref="MIM:125860"
ORIGIN      
        1 mvgrralivl ahsertsfny amkeaaaaal kkkgwevves dlyamnfnpi isrkditgkl
       61 kdpanfqypa esvlaykegh lspdivaeqk kleaadlvif qfplqwfgvp ailkgwferv
      121 figefaytya amydkgpfrs kkavlsittg gsgsmyslqg ihgdmnvilw piqsgilhfc
      181 gfqvlepqlt ysightpada riqilegwkk rleniwdetp lyfapsslfd lnfqagflmk
      241 kevqdeeknk kfglsvghhl gksiptdnqi kark
//
LOCUS       NP_001355260             594 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 90 isoform 5 [Mus musculus].
ACCESSION   NP_001355260
VERSION     NP_001355260.1
DBSOURCE    REFSEQ: accession NM_001368331.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Yu,C.Y., Han,J.X., Zhang,J., Jiang,P., Shen,C., Guo,F., Tang,J.,
            Yan,T., Tian,X., Zhu,X., Ma,D., Hu,Y., Xie,Y., Du,W., Zhong,M.,
            Chen,J., Liu,Q., Sun,D., Chen,Y., Zou,W., Hong,J., Chen,H. and
            Fang,J.Y.
  TITLE     A 16q22.1 variant confers susceptibility to colorectal cancer as a
            distal regulator of ZFP90
  JOURNAL   Oncogene 39 (6), 1347-1360 (2020)
   PUBMED   31641208
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Liu,T., Kong,W.X., Tang,X.Y., Xu,M., Wang,Q.H., Zhang,B., Hu,L.D.
            and Chen,H.
  TITLE     The transcription factor Zfp90 regulates the self-renewal and
            differentiation of hematopoietic stem cells
  JOURNAL   Cell Death Dis 9 (6), 677 (2018)
   PUBMED   29880802
  REMARK    GeneRIF: Zfp90 was highly expressed in hematopoietic stem cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Taher,L., Collette,N.M., Murugesh,D., Maxwell,E., Ovcharenko,I. and
            Loots,G.G.
  TITLE     Global gene expression analysis of murine limb development
  JOURNAL   PLoS One 6 (12), e28358 (2011)
   PUBMED   22174793
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
REFERENCE   7  (residues 1 to 594)
  AUTHORS   Marine,J.C., Gilbert,D.J., Bellefroid,E.J., Martial,J.A.,
            Ihle,J.N., Copeland,N.G. and Jenkins,N.A.
  TITLE     Chromosomal location of fifteen unique mouse KRAB-containing zinc
            finger loci
  JOURNAL   Mamm Genome 7 (6), 413-416 (1996)
   PUBMED   8662221
REFERENCE   8  (residues 1 to 594)
  AUTHORS   Bellefroid,E.J., Marine,J.C., Matera,A.G., Bourguignon,C.,
            Desai,T., Healy,K.C., Bray-Ward,P., Martial,J.A., Ihle,J.N. and
            Ward,D.C.
  TITLE     Emergence of the ZNF91 Kruppel-associated box-containing zinc
            finger gene family in the last common ancestor of anthropoidea
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10757-10761 (1995)
   PUBMED   7479878
REFERENCE   9  (residues 1 to 594)
  AUTHORS   Lange,R., Christoph,A., Thiesen,H.J., Vopper,G., Johnson,K.R.,
            Lemaire,L., Plomann,M., Cremer,H., Barthels,D. and Heinlein,U.A.
  TITLE     Developmentally regulated mouse gene NK10 encodes a zinc finger
            repressor protein with differential DNA-binding domains
  JOURNAL   DNA Cell Biol 14 (11), 971-981 (1995)
   PUBMED   7576184
REFERENCE   10 (residues 1 to 594)
  AUTHORS   Ihle,J.N., Smith-White,B., Sisson,B., Parker,D., Blair,D.G.,
            Schultz,A., Kozak,C., Lunsford,R.D., Askew,D., Weinstein,Y. et al.
  TITLE     Activation of the c-H-ras proto-oncogene by retrovirus insertion
            and chromosomal rearrangement in a Moloney leukemia virus-induced
            T-cell leukemia
  JOURNAL   J Virol 63 (7), 2959-2966 (1989)
   PUBMED   2542606
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC134615.5 and AC164096.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.4493457.1,
                                           SRR17253014.3821464.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849376
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 53.14 cM"
     Protein         1..594
                     /product="zinc finger protein 90 isoform 5"
                     /note="zinc finger protein 90 homolog; zfp-90; zinc finger
                     protein NK10; Nk10 expressed protein; zinc finger protein
                     83"
                     /calculated_mol_wt=67489
     Region          <1..32
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          168..188
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..230
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          234..590
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          238..258
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          266..286
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(271,273,275,277..278,281..282,285,299,301,305..306,
                     309..310,313,327,329,331,333..334,337..338,341)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          294..314
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          322..342
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          350..370
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          406..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          454..474
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          482..502
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(487,489,491,493..494,497..498,501,515,517,521..522,
                     525..526,529,543,545,547,549..550,553..554,557)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          510..530
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          538..558
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          566..586
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..594
                     /gene="Zfp90"
                     /gene_synonym="6430515L01Rik; KRAB17; mKIAA1954; NK10;
                     Zfp64; Zfp83"
                     /coded_by="NM_001368331.1:612..2396"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:22751"
                     /db_xref="MGI:MGI:104786"
ORIGIN      
        1 mlenynhlvs lgyqvskpev ifkleqgeep wisekeiqrp fcpdwktrpe ssrspqqgvs
       61 evflrtnvls httigdiwnv aiqghqesgr rhlgpeassq kkittlekki eqnkvgedss
      121 lstdlvpqld isssirpsdc ktfgnnlehn selvtqsnil akkkpykcdk crksfihrss
      181 lnkhekihkg dpysngtdqg aqsgrkhhec adcgktflwr tqltehqrih tgekpfecnv
      241 cgkafrhsss lgqhenahtg ekpyqcslcg kafqrssslv qhqrihtgek pyrcnlcgrs
      301 frhstsltqh evthsgekpf qckecgkafs rcsslvqher thtgekpfec sicgrafgqs
      361 pslykhmrih krskpyqsnn fslafvpntp lpqgegllte vksyhcndcg kdfghitdfs
      421 ehqrlhagen sygseqtllg qqslshprek pyqcnvcgka fkrstsfieh hrihtgekpy
      481 ecnecgeafs rlssltqher thtgekpyec idcgkafsqs ssliqherth tgekpyecne
      541 cgrafrkktn lhdhqrthtg ekpyackecg rnfsrssalt khhrvharnk lqes
//
LOCUS       NP_060136                737 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 280C [Homo sapiens].
ACCESSION   NP_060136
VERSION     NP_060136.1
DBSOURCE    REFSEQ: accession NM_017666.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Ying,Y., Wang,M., Chen,Y., Li,M., Ma,C., Zhang,J., Huang,X.,
            Jia,M., Zeng,J., Wang,Y., Li,L., Wang,X., Tao,Q. and Shu,X.S.
  TITLE     Zinc finger protein 280C contributes to colorectal tumorigenesis by
            maintaining epigenetic repression at H3K27me3-marked loci
  JOURNAL   Proc Natl Acad Sci U S A 119 (22), e2120633119 (2022)
   PUBMED   35605119
  REMARK    GeneRIF: Zinc finger protein 280C contributes to colorectal
            tumorigenesis by maintaining epigenetic repression at
            H3K27me3-marked loci.
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 737)
  AUTHORS   Moquin,D.M., Genois,M.M., Zhang,J.M., Ouyang,J., Yadav,T.,
            Buisson,R., Yazinski,S.A., Tan,J., Boukhali,M., Gagne,J.P.,
            Poirier,G.G., Lan,L., Haas,W. and Zou,L.
  TITLE     Localized protein biotinylation at DNA damage sites identifies
            ZPET, a repressor of homologous recombination
  JOURNAL   Genes Dev 33 (1-2), 75-89 (2019)
   PUBMED   30567999
  REMARK    GeneRIF: ZPET binds ssDNA and localizes to DNA double-strand breaks
            (DSBs) and stalled replication forks.
            Erratum:[Genes Dev. 2019 Feb 1;33(3-4):253. doi:
            10.1101/gad.324053.119. PMID: 30709902]
REFERENCE   6  (residues 1 to 737)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   7  (residues 1 to 737)
  AUTHORS   Kroncke,K.D. and Klotz,L.O.
  TITLE     Zinc fingers as biologic redox switches?
  JOURNAL   Antioxid Redox Signal 11 (5), 1015-1027 (2009)
   PUBMED   19132878
  REMARK    Review article
REFERENCE   8  (residues 1 to 737)
  AUTHORS   Brayer,K.J. and Segal,D.J.
  TITLE     Keep your fingers off my DNA: protein-protein interactions mediated
            by C2H2 zinc finger domains
  JOURNAL   Cell Biochem Biophys 50 (3), 111-131 (2008)
   PUBMED   18253864
  REMARK    Review article
REFERENCE   9  (residues 1 to 737)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   10 (residues 1 to 737)
  AUTHORS   Iuchi,S.
  TITLE     Three classes of C2H2 zinc finger proteins
  JOURNAL   Cell Mol Life Sci 58 (4), 625-635 (2001)
   PUBMED   11361095
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC051728.1, DA441065.1 and AL139234.19.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the zinc finger
            domain-containing protein family. This family member contains
            multiple Cys2-His2(C2H2)-type zinc finger domains, the most common
            type of zinc finger domain that self-folds to form a
            beta-beta-alpha structure that binds a zinc ion. [provided by
            RefSeq, Aug 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC051728.1, SRR1660807.109014.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370978.9/ ENSP00000360017.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..737
                     /product="zinc finger protein 280C"
                     /note="zinc finger protein 633; suppressor of hairy wing
                     homolog 3; zinc finger protein proximal to RAD eighteen"
                     /calculated_mol_wt=82965
     Region          46..227
                     /region_name="DUF4195"
                     /note="Domain of unknown function (DUF4195); pfam13836"
                     /db_xref="CDD:463993"
     Region          57..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND82.1)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8ND82.1)"
     Region          176..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND82.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8ND82.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8ND82.1)"
     Region          355..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(360,362,364,366..367,370..371,375,390,392,396..397,
                     400..401,405,420,422,424,426..427,430..431)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          385..406
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          415..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          535..602
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND82.1)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8ND82.1)"
     CDS             1..737
                     /gene="ZNF280C"
                     /gene_synonym="SUHW3; ZNF633; ZPET"
                     /coded_by="NM_017666.5:155..2368"
                     /db_xref="CCDS:CCDS14622.1"
                     /db_xref="GeneID:55609"
                     /db_xref="HGNC:HGNC:25955"
ORIGIN      
        1 mdddkpfqpk niskmaelfm eceeeelepw qkkveetqde dddelifvge issskpaisn
       61 ilnrghssss skgiksephs pgipeifrta sqrcrdppsn pvaasprfhl vskssqssvt
      121 venaskpdft knsqvgsdns sillfdstqe slppsqdipa ifregmknts yvlkhpstsk
      181 vnsvtpkkpk tsedvpqinp stslpligsp pvtssqvmls kgtntsspyd agadylracp
      241 kcnvqfnlld plkyhmkhcc pdmitkflgv ivkserpcde dktdsetgkl imlvnefyyg
      301 rhegvtekep ktyttfkcfs cskvlknnir fmnhmkhhle lekqnneswe nhttcqhcyr
      361 qyptpfqlqc hiesthtphe fstickicel sfetehillq hmkdthkpge mpyvcqvcqf
      421 rsstfsdvea hfraahentk nllcpfclkv skmatpymnh ymkhqkkgvh rcpkcrlqfl
      481 tskekaehka qhrtfikpke leglppgakv tiraslgplq sklptapfgc apgtsflqvt
      541 pptsqnttar nprksnasrs ktsklhatts taskvntskp rgriakskak psykqkrqrn
      601 rknkmslalk nircrrgihk ciechskikd fashfsiyih csfckyntnc nkafvnhmms
      661 shsnhpgkrf cifkkhsgtl rgitlvclkc dfladssgld rmakhlsqrk thtcqviien
      721 vskststsep ttgcslk
//
LOCUS       NP_057438                722 aa            linear   PRI 27-APR-2025
DEFINITION  solute carrier organic anion transporter family member 4A1 [Homo
            sapiens].
ACCESSION   NP_057438
VERSION     NP_057438.3
DBSOURCE    REFSEQ: accession NM_016354.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Li,S., Li,Z., Huang,L., Geng,Z., Li,F., Wu,B., Sheng,Y., Xu,Y.,
            Li,B., Xu,Y., Gu,Z. and Qi,Y.
  TITLE     SLCO4A1, as a novel prognostic biomarker of non-small cell lung
            cancer, promotes cell proliferation and migration
  JOURNAL   Int J Oncol 64 (3) (2024)
   PUBMED   38275113
  REMARK    GeneRIF: SLCO4A1, as a novel prognostic biomarker of non-small cell
            lung cancer, promotes cell proliferation and migration.
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Ontsouka,E., Epstein,A., Kallol,S., Zaugg,J., Baumann,M.,
            Schneider,H. and Albrecht,C.
  TITLE     Placental Expression of Bile Acid Transporters in Intrahepatic
            Cholestasis of Pregnancy
  JOURNAL   Int J Mol Sci 22 (19), 10434 (2021)
   PUBMED   34638773
  REMARK    GeneRIF: Placental Expression of Bile Acid Transporters in
            Intrahepatic Cholestasis of Pregnancy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Buxhofer-Ausch,V., Sheikh,M., Ausch,C., Zotter,S., Bauer,H.,
            Mollik,M., Reiner,A., Gleiss,A., Jager,W., Sebesta,C., Kriwanek,S.
            and Thalhammer,T.
  TITLE     Abundance of the Organic Anion-transporting Polypeptide OATP4A1 in
            Early-Stage Colorectal Cancer Patients: Association With Disease
            Relapse
  JOURNAL   Appl Immunohistochem Mol Morphol 27 (3), 185-194 (2019)
   PUBMED   29734253
  REMARK    GeneRIF: Abundance of the Organic Anion-transporting Polypeptide
            OATP4A1 in Early-Stage Colorectal Cancer Patients: Association With
            Disease Relapse.
REFERENCE   5  (residues 1 to 722)
  AUTHORS   Ban,M.J., Ji,S.H., Lee,C.K., Bae,S.B., Kim,H.J., Ahn,T.S.,
            Lee,M.S., Baek,M.J. and Jeong,D.
  TITLE     Solute carrier organic anion transporter family member 4A1
            (SLCO4A1) as a prognosis marker of colorectal cancer
  JOURNAL   J Cancer Res Clin Oncol 143 (8), 1437-1447 (2017)
   PUBMED   28378090
  REMARK    GeneRIF: SLCO4A1 may be a valuable marker of poor prognostic for
            colorectal cancer (CRC). Furthermore, SLCO4A1 plays an important
            role in CRC cell proliferation, migration, invasion, and
            carcinogenesis
REFERENCE   6  (residues 1 to 722)
  AUTHORS   Hagenbuch,B. and Meier,P.J.
  TITLE     Organic anion transporting polypeptides of the OATP/ SLC21 family:
            phylogenetic classification as OATP/ SLCO superfamily, new
            nomenclature and molecular/functional properties
  JOURNAL   Pflugers Arch 447 (5), 653-665 (2004)
   PUBMED   14579113
  REMARK    Review article
REFERENCE   7  (residues 1 to 722)
  AUTHORS   Pizzagalli,F., Varga,Z., Huber,R.D., Folkers,G., Meier,P.J. and
            St-Pierre,M.V.
  TITLE     Identification of steroid sulfate transport processes in the human
            mammary gland
  JOURNAL   J Clin Endocrinol Metab 88 (8), 3902-3912 (2003)
   PUBMED   12915686
REFERENCE   8  (residues 1 to 722)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   9  (residues 1 to 722)
  AUTHORS   Fujiwara,K., Adachi,H., Nishio,T., Unno,M., Tokui,T., Okabe,M.,
            Onogawa,T., Suzuki,T., Asano,N., Tanemoto,M., Seki,M., Shiiba,K.,
            Suzuki,M., Kondo,Y., Nunoki,K., Shimosegawa,T., Iinuma,K., Ito,S.,
            Matsuno,S. and Abe,T.
  TITLE     Identification of thyroid hormone transporters in humans: different
            molecules are involved in a tissue-specific manner
  JOURNAL   Endocrinology 142 (5), 2005-2012 (2001)
   PUBMED   11316767
REFERENCE   10 (residues 1 to 722)
  AUTHORS   Tamai,I., Nezu,J., Uchino,H., Sai,Y., Oku,A., Shimane,M. and
            Tsuji,A.
  TITLE     Molecular identification and characterization of novel members of
            the human organic anion transporter (OATP) family
  JOURNAL   Biochem Biophys Res Commun 273 (1), 251-260 (2000)
   PUBMED   10873595
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM846201.1, AB031051.1, BC015727.1, AI660559.1 and AF205072.1.
            
            On Dec 12, 2003 this sequence version replaced NP_057438.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015727.1, SRR1803611.122216.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000217159.6/ ENSP00000217159.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..722
                     /product="solute carrier organic anion transporter family
                     member 4A1"
                     /note="solute carrier family 21 (organic anion
                     transporter), member 12; organic anion transporting
                     polypeptide E; sodium-independent organic anion
                     transporter E; organic anion transporter
                     polypeptide-related protein 1; colon organic anion
                     transporter; solute carrier family 21 member 12; OATP-RP1"
                     /calculated_mol_wt=77063
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96BD0.2)"
     Region          102..604
                     /region_name="MFS_SLCO4A_OATP4A"
                     /note="Solute carrier organic anion transporter 4A
                     subfamily of the Major Facilitator Superfamily of
                     transporters; cd17462"
                     /db_xref="CDD:341020"
     Site            104..124
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            order(116..117,120..121,124,157,241..242,244..246,249,269,
                     272..273,276,392,395..396,399..401,404,433,437,477..478,
                     482,486,548,551..552,555..556,559)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341020"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            171..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            223..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            273..293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            308..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            379..400
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            421..444
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            449..471
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            499
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            557
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            581..603
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            613..638
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Site            672..689
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     Region          703..722
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD0.2)"
     CDS             1..722
                     /gene="SLCO4A1"
                     /gene_synonym="OATP-E; OATP1; OATP4A1; OATPE; OATPRP1;
                     POAT; SLC21A12"
                     /coded_by="NM_016354.4:148..2316"
                     /db_xref="CCDS:CCDS13501.1"
                     /db_xref="GeneID:28231"
                     /db_xref="HGNC:HGNC:10953"
                     /db_xref="MIM:612436"
ORIGIN      
        1 mplhqlgdkp ltfpspnsam engldhtpps rraspgtpls pgslrsaahs pldtskqplc
       61 qlwaekhgar gthevryvsa gqsvacgwwa fappclqvln tpkgilfflc aaaflqgmtv
      121 ngfintvits lerrydlhsy qsgliassyd iaaclcltfv syfggsghkp rwlgwgvllm
      181 gtgslvfalp hftagryeve ldagvrtcpa npgavcadst sglsryqlvf mlgqflhgvg
      241 atplytlgvt yldenvkssc spvyiaifyt aailgpaagy liggallniy temgrrtelt
      301 tesplwvgaw wvgflgsgaa afftavpilg yprqlpgsqr yavmraaemh qlkdssrgea
      361 snpdfgktir dlplsiwlll knptfillcl agateatlit gmstfspkfl esqfslsase
      421 aatlfgylvv paggggtflg gffvnklrlr gsavikfclf ctvvsllgil vfslhcpsvp
      481 magvtasygg sllpeghlnl tapcnaacsc qpehyspvcg sdglmyfslc hagcpaatet
      541 nvdgqkvyrd cscipqnlss gfghatagkc tstcqrkpll lvfifvviff tflssipalt
      601 atlrcvrdpq rsfalgiqwi vvrilggipg piafgwvidk acllwqdqcg qqgsclvyqn
      661 samsryilim gllykvlgvl ffaiacflyk plsessdgle tclpsqssap dsatdsqlqs
      721 sv
//
LOCUS       NP_001349958             278 aa            linear   ROD 27-APR-2025
DEFINITION  syntaxin-16 isoform e [Mus musculus].
ACCESSION   NP_001349958
VERSION     NP_001349958.1
DBSOURCE    REFSEQ: accession NM_001363029.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Hara,Y., Katsuyama,T., Fukaya,M., Sugawara,T., Shiroshima,T.,
            Sadakata,T., Osumi,N. and Sakagami,H.
  TITLE     ADP Ribosylation Factor 4 (Arf4) Regulates Radial Migration through
            N-Cadherin Trafficking during Cerebral Cortical Development
  JOURNAL   eNeuro 10 (11) (2023)
   PUBMED   37848288
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Sundberg,J.P., Dadras,S.S., Silva,K.A., Kennedy,V.E., Garland,G.,
            Murray,S.A., Sundberg,B.A., Schofield,P.N. and Pratt,C.H.
  TITLE     Systematic screening for skin, hair, and nail abnormalities in a
            large-scale knockout mouse program
  JOURNAL   PLoS One 12 (7), e0180682 (2017)
   PUBMED   28700664
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Beaton,N., Rudigier,C., Moest,H., Muller,S., Mrosek,N., Roder,E.,
            Rudofsky,G., Rulicke,T., Ukropec,J., Ukropcova,B., Augustin,R.,
            Neubauer,H. and Wolfrum,C.
  TITLE     TUSC5 regulates insulin-mediated adipose tissue glucose uptake by
            modulation of GLUT4 recycling
  JOURNAL   Mol Metab 4 (11), 795-810 (2015)
   PUBMED   26629404
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Chua,C.E. and Tang,B.L.
  TITLE     Syntaxin 16 is enriched in neuronal dendrites and may have a role
            in neurite outgrowth
  JOURNAL   Mol Membr Biol 25 (1), 35-45 (2008)
   PUBMED   17852734
  REMARK    GeneRIF: Syntaxin 16 may thus play a role in neurite outgrowth and
            perhaps other specific dendritic anterograde/retrograde traffic.
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Frohlich,L.F., Bastepe,M., Ozturk,D., Abu-Zahra,H. and Juppner,H.
  TITLE     Lack of Gnas epigenetic changes and pseudohypoparathyroidism type
            Ib in mice with targeted disruption of syntaxin-16
  JOURNAL   Endocrinology 148 (6), 2925-2935 (2007)
   PUBMED   17317779
  REMARK    GeneRIF: Mice genetically altered to carry the equivalent of
            STX16del4-6 contributing to pseudohypoparathyroidism type 1b.
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Nishimura,M., Yokoi,N., Miki,T., Horikawa,Y., Yoshioka,H.,
            Takeda,J., Ohara,O. and Seino,S.
  TITLE     Construction of a multi-functional cDNA library specific for mouse
            pancreatic islets and its application to microarray
  JOURNAL   DNA Res 11 (5), 315-323 (2004)
   PUBMED   15747579
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL669896.7.
            
            Transcript Variant: This variant (5) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (e) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG866605.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849377, SAMN00849379
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 97.85 cM"
     Protein         1..278
                     /product="syntaxin-16 isoform e"
                     /calculated_mol_wt=31346
     Region          73..254
                     /region_name="COG5325"
                     /note="t-SNARE complex subunit, syntaxin [Intracellular
                     trafficking and secretion]"
                     /db_xref="CDD:227635"
     Region          <217..244
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            217
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     CDS             1..278
                     /gene="Stx16"
                     /gene_synonym="4930401D03; 5430410K23Rik; 6330500A18Rik;
                     Syn16"
                     /coded_by="NM_001363029.1:8..844"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:228960"
                     /db_xref="MGI:MGI:1923396"
ORIGIN      
        1 matrrltdaf lllrnnsiqt rqllaeqvss httssplhsr siaaeldela ddrmalvsgi
       61 sldpeaaigv tkrsppkwvd gvdeiqydvg rikqkmkela slhdkhlnrp tlddsseeeh
      121 aieittqevt qlfhrcqrav qalpsrarra cseqeerllr nvvaslaqal qelstsfrha
      181 qsdylkrmkn reersqhffd tpvplmddgd datlygqgtv ldridynveq scvktedglk
      241 qlhkaeqyqk knrkmlvivi lvaviivllv alvavksr
//
LOCUS       NP_001351601            1163 aa            linear   PRI 27-APR-2025
DEFINITION  uncharacterized protein SPEM3 isoform 2 [Homo sapiens].
ACCESSION   NP_001351601 XP_011522099 XP_024308362
VERSION     NP_001351601.1
DBSOURCE    REFSEQ: accession NM_001364672.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113189.11 and HY033016.1.
            
            On or before Jun 28, 2018 this sequence version replaced
            XP_024308362.1, XP_011522099.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY033016.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..1163
                     /product="uncharacterized protein SPEM3 isoform 2"
                     /calculated_mol_wt=124976
     Region          <184..>654
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          <222..405
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..1163
                     /gene="SPEM3"
                     /coded_by="NM_001364672.1:47..3538"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:107983988"
                     /db_xref="HGNC:HGNC:53651"
ORIGIN      
        1 mgerayhgaq vcsgtnprkc qdlgdsilll lgsfillnvw invvtllwkh lksslrilfr
       61 hffpkgfllr rvnhldswip dtndekvsac ccvppkcgha gvpresargl ykagmmggge
      121 apqvtaskaq asllsrpets sqfpkmskld tgpchlpqes ktktpdcapa eapaqaqvhs
      181 pthtpvctpt hpwtrstdht avhtpahswt hskartpegt hsqaqdtsaq aqahtsaptp
      241 aqtpahiqah tpaptpakas ahtkahtsaq aqthspphtp eythsqahsp ehtsahspaq
      301 apmpvpahpq ahapeytsah apayipdhsh lvrssvpvpt sapappgtla pattpvlapt
      361 papvpasaps papalvmalt ttpvpdpvpa ttpapiitpi pstppafshd lstghvvyda
      421 rrekqnffhm sspqnpeysr kdlatlfrpq egqdlvssgi seqtkqcsgd saklpagsil
      481 gylelrnmew knsddakdkf pqtktspycs fhpcsseknt dsqapfypkf laysrdtaca
      541 ktcfhsatta qssvctlppp ftlslplvpp rsfvppqptn hqrpstliqt ptvlptsksp
      601 qsiltsqfpi pslfatisqp liqpqcpech eslgltqdsg lqrtpgpskd srvprnldla
      661 qnpdlyknpg ltqdpglhen pglapnqglh efpglpqdsy lcqnpspsqd fglhknsgit
      721 qdshpqkntg ltqeagilrs pcltqspglh kktpftqtsd lqrssgftqd sgiyrnlepn
      781 qetviyknqd lsqatdhqkn lgsskdsggh kntgnvqdpg vcstaglted sgsqkgpyvp
      841 qdsevnkssg viqesflhks pglvqtsglp kcsgltqnsg dyknpgliqd cgghkvkglt
      901 qdsnlpsltq atkverrfsl pqdvgvyrss ehsqdsnlhk cpginqdpgp hkdpalvqds
      961 glpkisgltq esgpyksscl ipdpslyknp spalgsdfvq llsllqtpks tlslmkssvp
     1021 ekaaqkedaq rhvlwarvql nenscpskaq vvsndlqtfs evpvlielqs sswragsqhg
     1081 ayrpvdtvps gyqnyrqmsm pthinwkshc pgpgtqaghv vfdarqrrla vgkdkceals
     1141 prrlhqeaps nsgkpsrsgd irm
//
LOCUS       NP_001355770             426 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 8B isoform 4 [Mus musculus].
ACCESSION   NP_001355770
VERSION     NP_001355770.1
DBSOURCE    REFSEQ: accession NM_001368841.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL732626.8.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660817.155500.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 23.05 cM"
     Protein         1..426
                     /product="transmembrane protein 8B isoform 4"
                     /calculated_mol_wt=46302
     Region          285..>401
                     /region_name="DUF3522"
                     /note="Protein of unknown function (DUF3522); pfam12036"
                     /db_xref="CDD:463441"
     CDS             1..426
                     /gene="Tmem8b"
                     /gene_synonym="4930500O05Rik"
                     /coded_by="NM_001368841.1:1243..2523"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:242409"
                     /db_xref="MGI:MGI:2441680"
ORIGIN      
        1 mwlywflavp qskpfppiiv qpctkcpqps lsralvpgaa mnmpqslgtq plppeppslg
       61 tpiegsgaia ptehcwpvrp tlrneldtfs vhfyiffgps valpperpav falrllpvld
      121 sggvlslelq lnasslrqen vtvfgclthe vplslgdaav tcskeslagf llsvsatsrv
      181 arlripfpqt gtwfltlrsl cgvgprfvrc rnataevrlr tflspcvddc gpygqckllr
      241 thnylyaace ckagwrgwgc tdsadaltyg fqllstlllc lsnlmflppv vlairsryvl
      301 eaavytftmf fstfyhacdq pgivvfcimd ydvlqfcdfl gslmsvwvtv iamarlqpvi
      361 kqvlyllgam llsmalqldr hglwnllgps lfalgilata wfaasgagtv thrhgaagfs
      421 tcvpaa
//
LOCUS       NP_780517                216 aa            linear   ROD 27-APR-2025
DEFINITION  MOB kinase activator 3C [Mus musculus].
ACCESSION   NP_780517
VERSION     NP_780517.1
DBSOURCE    REFSEQ: accession NM_175308.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Harrow,J.L., Steward,C.A., Frankish,A., Gilbert,J.G.,
            Gonzalez,J.M., Loveland,J.E., Mudge,J., Sheppard,D., Thomas,M.,
            Trevanion,S. and Wilming,L.G.
  TITLE     The Vertebrate Genome Annotation browser 10 years on
  JOURNAL   Nucleic Acids Res 42 (Database issue), D771-D779 (2014)
   PUBMED   24316575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL626806.14 and AL627085.13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK084014.1, BC099740.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 53.06 cM"
     Protein         1..216
                     /product="MOB kinase activator 3C"
                     /note="mob1 homolog 2C; MOB1, Mps One Binder kinase
                     activator-like 2C"
                     /calculated_mol_wt=25389
     Region          35..207
                     /region_name="Mob1_phocein"
                     /note="Mob1/phocein family; pfam03637"
                     /db_xref="CDD:461000"
     CDS             1..216
                     /gene="Mob3c"
                     /gene_synonym="D130076I06Rik; Mobkl2c"
                     /coded_by="NM_175308.5:212..862"
                     /db_xref="CCDS:CCDS18497.1"
                     /db_xref="GeneID:100465"
                     /db_xref="MGI:MGI:2140623"
ORIGIN      
        1 malclkqvfa kdktfrprkr fepgtqrfel ykkaqaslks gldlrsvvrl ppgesiddwi
       61 avhvvdffnr inliygtmae hcsesscpvm aggpryeyrw qderqyrrpa klsaprymal
      121 lmdwieglin dedvfptrvg vpfpknfqqv ctkiltrlfr vfvhvyihhf dsilsmgaea
      181 hvntcykhfy yfiqefslvd qreleplrem terich
//
LOCUS       NP_002381                769 aa            linear   PRI 27-APR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 11
            isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_002381 NP_067625
VERSION     NP_002381.2
DBSOURCE    REFSEQ: accession NM_002390.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Barallobre-Barreiro,J., Didangelos,A., Schoendube,F.A., Drozdov,I.,
            Yin,X., Fernandez-Caggiano,M., Willeit,P., Puntmann,V.O.,
            Aldama-Lopez,G., Shah,A.M., Domenech,N. and Mayr,M.
  TITLE     Proteomics analysis of cardiac extracellular matrix remodeling in a
            porcine model of ischemia/reperfusion injury
  JOURNAL   Circulation 125 (6), 789-802 (2012)
   PUBMED   22261194
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Fu,G.K., Wang,J.T., Yang,J., Au-Young,J. and Stuve,L.L.
  TITLE     Circular rapid amplification of cDNA ends for high-throughput
            extension cloning of partial genes
  JOURNAL   Genomics 84 (1), 205-210 (2004)
   PUBMED   15203218
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Shea,S.H., Wall,T.L., Carr,L.G. and Li,T.K.
  TITLE     ADH2 and alcohol-related phenotypes in Ashkenazic Jewish American
            college students
  JOURNAL   Behav Genet 31 (2), 231-239 (2001)
   PUBMED   11545539
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 769)
  AUTHORS   Sagane,K., Ohya,Y., Hasegawa,Y. and Tanaka,I.
  TITLE     Metalloproteinase-like, disintegrin-like, cysteine-rich proteins
            MDC2 and MDC3: novel human cellular disintegrins highly expressed
            in the brain
  JOURNAL   Biochem J 334 (Pt 1) (Pt 1), 93-98 (1998)
   PUBMED   9693107
REFERENCE   6  (residues 1 to 769)
  AUTHORS   Wolfsberg,T.G., Primakoff,P., Myles,D.G. and White,J.M.
  TITLE     ADAM, a novel family of membrane proteins containing A Disintegrin
            And Metalloprotease domain: multipotential functions in cell-cell
            and cell-matrix interactions
  JOURNAL   J Cell Biol 131 (2), 275-278 (1995)
   PUBMED   7593158
  REMARK    Review article
REFERENCE   7  (residues 1 to 769)
  AUTHORS   Katagiri,T., Harada,Y., Emi,M. and Nakamura,Y.
  TITLE     Human metalloprotease/disintegrin-like (MDC) gene: exon-intron
            organization and alternative splicing
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 39-44 (1995)
   PUBMED   7956356
REFERENCE   8  (residues 1 to 769)
  AUTHORS   Emi,M., Katagiri,T., Harada,Y., Saito,H., Inazawa,J., Ito,I.,
            Kasumi,F. and Nakamura,Y.
  TITLE     A novel metalloprotease/disintegrin-like gene at 17q21.3 is
            somatically rearranged in two primary breast cancers
  JOURNAL   Nat Genet 5 (2), 151-157 (1993)
   PUBMED   8252040
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005180.3, BC144550.1,
            AB009675.1, CD630831.1, CD630842.1, CN418442.1, BM557705.1 and
            BM681070.1.
            
            On or before Aug 24, 2005 this sequence version replaced
            NP_067625.1, NP_002381.1.
            
            Summary: This gene encodes a member of the ADAM (a disintegrin and
            metalloprotease) protein family. Members of this family are
            membrane-anchored proteins structurally related to snake venom
            disintegrins, and have been implicated in a variety of biological
            processes involving cell-cell and cell-matrix interactions,
            including fertilization, muscle development, and neurogenesis. The
            encoded preproprotein is proteolytically processed to generate the
            mature protease. This gene represents a candidate tumor suppressor
            gene for human breast cancer based on its location within a minimal
            region of chromosome 17q21 previously defined by tumor deletion
            mapping. Alternative splicing results in multiple transcript
            variants, at least one of which encodes an isoform that is
            proteolytically processed. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB009675.1, SRR1660803.156588.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000200557.11/ ENSP00000200557.6
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..769
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 11 isoform 1 preproprotein"
                     /note="disintegrin and metalloproteinase domain-containing
                     protein 11; ADAM 11; metalloproteinase-like,
                     disintegrin-like, and cysteine-rich protein"
                     /calculated_mol_wt=80871
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2566
     Region          40..78
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75078.3)"
     Region          62..189
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Site            96
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75078.3)"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75078.3)"
     mat_peptide     226..769
                     /product="Disintegrin and metalloproteinase
                     domain-containing protein 11. /id=PRO_0000029075"
                     /note="propagated from UniProtKB/Swiss-Prot (O75078.3)"
                     /calculated_mol_wt=58990
     Region          239..438
                     /region_name="Reprolysin"
                     /note="Reprolysin (M12B) family zinc metalloprotease;
                     pfam01421"
                     /db_xref="CDD:426256"
     Region          332..769
                     /region_name="Required for localization to cerebellar
                     cortex basket cell terminals. Also required for
                     localization of KCNA1, KCNA2, DLG4 and ADAM22 to
                     cerebellar cortex basket cell terminal perisomatic axons
                     and pinceaux. /evidence=ECO:0000250|UniProtKB:Q9R1V4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75078.3)"
     Region          453..526
                     /region_name="Disintegrin"
                     /note="pfam00200"
                     /db_xref="CDD:459709"
     Region          530..668
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     Site            605
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75078.3)"
     Site            673
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75078.3)"
     Site            735..755
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75078.3)"
     CDS             1..769
                     /gene="ADAM11"
                     /gene_synonym="MDC"
                     /coded_by="NM_002390.6:213..2522"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS11486.1"
                     /db_xref="GeneID:4185"
                     /db_xref="HGNC:HGNC:189"
                     /db_xref="MIM:155120"
ORIGIN      
        1 mrllrrwafa alllsllptp glgtqgpaga lrwgglpqlg gpgapevtep srlvressgg
       61 evrkqqldtr vrqeppggpp vhlaqvsfvi pafnsnftld lelnhhllss qyverhfsre
      121 gttqhstgag dhcyyqgklr gnphsfaals tcqglhgvfs dgnltyivep qevagpwgap
      181 qgplphliyr tpllpdplgc repgclfavp aqsappnrpr lrrkrqvrrg hptvhsetky
      241 velivindhq lfeqmrqsvv ltsnfaksvv nladviykeq lntrivlvam etwadgdkiq
      301 vqddlletla rlmvyrregl pepsdathlf sgrtfqstss gaayvggics lshgggvney
      361 gnmgamavtl aqtlgqnlgm mwnkhrssag dckcpdiwlg cimedtgfyl prkfsrcsid
      421 eynqflqegg gsclfnkplk lldppecgng fveageecdc gsvqecsrag gncckkctlt
      481 hdamcsdglc crrckyeprg vscreavnec diaetctgds sqcppnlhkl dgyycdheqg
      541 rcyggrcktr drqcqvlwgh aaadrfcyek lnvegtergs cgrkgsgwvq cskqdvlcgf
      601 llcvnisgap rlgdlvgdis svtfyhqgke ldcrgghvql adgsdlsyve dgtacgpnml
      661 cldhrclpas afnfstcpgs gerricshhg vcsnegkcic qpdwtgkdcs ihnplptspp
      721 tgeterykgp sgtniiigsi agavlvaaiv lggtgwgfkn irrgrsgga
//
LOCUS       NP_689504                377 aa            linear   PRI 27-APR-2025
DEFINITION  mucin-7 precursor [Homo sapiens].
ACCESSION   NP_689504
VERSION     NP_689504.2
DBSOURCE    REFSEQ: accession NM_152291.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Zhang,J. and Li,Z.
  TITLE     Diagnostic accuracy of MUC7 expression for bladder cancer: A
            systematic review and meta-analysis
  JOURNAL   Medicine (Baltimore) 102 (35), e34828 (2023)
   PUBMED   37657056
  REMARK    GeneRIF: Diagnostic accuracy of MUC7 expression for bladder cancer:
            A systematic review and meta-analysis.
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Saad,E.A., Elsaid,A.M., Shoaib,R.M.S., Megahed,K.F. and
            Elsharawy,A.N.
  TITLE     MUC7 VNTR polymorphism and association with bronchial asthma in
            Egyptian children
  JOURNAL   Sci Rep 12 (1), 18910 (2022)
   PUBMED   36344553
  REMARK    GeneRIF: MUC7 VNTR polymorphism and association with bronchial
            asthma in Egyptian children.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Chahal,G., Quintana-Hayashi,M.P., Gaytan,M.O., Benktander,J.,
            Padra,M., King,S.J. and Linden,S.K.
  TITLE     Streptococcus oralis Employs Multiple Mechanisms of Salivary Mucin
            Binding That Differ Between Strains
  JOURNAL   Front Cell Infect Microbiol 12, 889711 (2022)
   PUBMED   35782137
  REMARK    GeneRIF: Streptococcus oralis Employs Multiple Mechanisms of
            Salivary Mucin Binding That Differ Between Strains.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Hertel,S., Hannig,M., Hannig,C. and Sterzenbach,T.
  TITLE     Mucins 5b and 7 and secretory IgA in the oral acquired pellicle of
            children with caries and caries-free children
  JOURNAL   Arch Oral Biol 134, 105314 (2022)
   PUBMED   34861462
  REMARK    GeneRIF: Mucins 5b and 7 and secretory IgA in the oral acquired
            pellicle of children with caries and caries-free children.
REFERENCE   5  (residues 1 to 377)
  AUTHORS   McQuaid,I.K., Dorfman,J.R. and Mall,A.S.
  TITLE     The comparative inhibitory potency of salivary mucins against human
            immunodeficiency virus type 1
  JOURNAL   Virology 553, 1-8 (2021)
   PUBMED   33190061
  REMARK    GeneRIF: The comparative inhibitory potency of salivary mucins
            against human immunodeficiency virus type 1.
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Bobek,L.A. and Situ,H.
  TITLE     MUC7 20-Mer: investigation of antimicrobial activity, secondary
            structure, and possible mechanism of antifungal action
  JOURNAL   Antimicrob Agents Chemother 47 (2), 643-652 (2003)
   PUBMED   12543672
  REMARK    GeneRIF: MUC7 is a salivary mucin with antimicrobial activity
            against bacteria and fungi.
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Prakobphol,A., Thomsson,K.A., Hansson,G.C., Rosen,S.D.,
            Singer,M.S., Phillips,N.J., Medzihradszky,K.F., Burlingame,A.L.,
            Leffler,H. and Fisher,S.J.
  TITLE     Human low-molecular-weight salivary mucin expresses the sialyl
            lewisx determinant and has L-selectin ligand activity
  JOURNAL   Biochemistry 37 (14), 4916-4927 (1998)
   PUBMED   9538010
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Troxler,R.F., Iontcheva,I., Oppenheim,F.G., Nunes,D.P. and
            Offner,G.D.
  TITLE     Molecular characterization of a major high molecular weight mucin
            from human sublingual gland
  JOURNAL   Glycobiology 7 (7), 965-973 (1997)
   PUBMED   9363439
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Bobek,L.A., Liu,J., Sait,S.N., Shows,T.B., Bobek,Y.A. and
            Levine,M.J.
  TITLE     Structure and chromosomal localization of the human salivary mucin
            gene, MUC7
  JOURNAL   Genomics 31 (3), 277-282 (1996)
   PUBMED   8838308
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Bobek,L.A., Tsai,H., Biesbrock,A.R. and Levine,M.J.
  TITLE     Molecular cloning, sequence, and specificity of expression of the
            gene encoding the low molecular weight human salivary mucin (MUC7)
  JOURNAL   J Biol Chem 268 (27), 20563-20569 (1993)
   PUBMED   7690757
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC108518.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 3, 2009 this sequence version replaced NP_689504.1.
            
            Summary: This gene encodes a small salivary mucin, which is thought
            to play a role in facilitating the clearance of bacteria in the
            oral cavity and to aid in mastication, speech, and swallowing. The
            central domain of this glycoprotein contains tandem repeats, each
            composed of 23 amino acids. This antimicrobial protein has
            antibacterial and antifungal activity. The most common allele
            contains 6 repeats, and some alleles may be associated with
            susceptibility to asthma. Alternatively spliced transcript variants
            with different 5' UTR, but encoding the same protein, have been
            found for this gene. [provided by RefSeq, Oct 2014].
            
            Transcript Variant: This variant (3) represents the shortest
            transcript and has a different 5' UTR compared to transcript
            variant 1. Transcript variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025688.1, AK312855.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000304887.6/
                                                  ENSP00000302021.5
            Protein has antimicrobial activity :: PMID: 12543672
            RefSeq Select criteria             :: based on expression, longest
                                                  protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.3"
     Protein         1..377
                     /product="mucin-7 precursor"
                     /note="mucin 7, salivary; mucin-7; MUC-7; apo-MG2;
                     salivary mucin-7; mucin MG2"
                     /calculated_mol_wt=36809
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2368
     mat_peptide     23..377
                     /product="mucin-7"
                     /calculated_mol_wt=36809
     mat_peptide     52..71
                     /product="MUC7 20-Mer"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     12543672]"
                     /calculated_mol_wt=2513
     Region          70..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Region          <141..358
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Region          150..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            176
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000269|PubMed:12407114; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            182
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) serine, by GALNT13.
                     /evidence=ECO:0000269|PubMed:12407114; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            183
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) serine, by GALNT13.
                     /evidence=ECO:0000269|PubMed:12407114; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            188
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000269|PubMed:12407114; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            189
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000269|PubMed:12407114; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     CDS             1..377
                     /gene="MUC7"
                     /gene_synonym="MG2"
                     /coded_by="NM_152291.3:111..1244"
                     /db_xref="CCDS:CCDS3541.1"
                     /db_xref="GeneID:4589"
                     /db_xref="HGNC:HGNC:7518"
                     /db_xref="MIM:158375"
ORIGIN      
        1 mktlplfvci calsacfsfs egrerdhelr hrrhhhqspk shfelphypg llahqkpfir
       61 ksykclhkrc rpklppspnn ppkfpnphqp pkhpdknssv vnptlvattq ipsvtfpsas
      121 tkittlpnvt flpqnattis srenvntsss vatlapvnsp apqdttaapp tpsattpapp
      181 sssappetta apptpsattq appsssappe ttaapptppa ttpappsssa ppettaappt
      241 psattpapls ssappettav pptpsattld pssasappet taapptpsat tpappsspap
      301 qettaapitt pnsspttlap dtsetsaapt hqtttsvttq ttttkqptsa pgqnkisrfl
      361 lymknllnri iddmveq
//
LOCUS       NP_001034936             227 aa            linear   PRI 27-APR-2025
DEFINITION  phospholipid hydroperoxide glutathione peroxidase GPX4 isoform B
            precursor [Homo sapiens].
ACCESSION   NP_001034936
VERSION     NP_001034936.1
DBSOURCE    REFSEQ: accession NM_001039847.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Ye,H., Ding,X., Lv,X., Du,Y., Guo,R., Qiu,J., Li,R. and Cao,L.
  TITLE     KLF14 directly downregulates the expression of GPX4 to exert
            antitumor effects by promoting ferroptosis in cervical cancer
  JOURNAL   J Transl Med 22 (1), 923 (2024)
   PUBMED   39390559
  REMARK    GeneRIF: KLF14 directly downregulates the expression of GPX4 to
            exert antitumor effects by promoting ferroptosis in cervical
            cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Sok,S.P.M., Pipkin,K., Popescu,N.I., Reidy,M., Li,B., Van
            Remmen,H., Kinter,M., Sun,X.H., Fan,Z. and Zhao,M.
  TITLE     Gpx4 Regulates Invariant NKT Cell Homeostasis and Function by
            Preventing Lipid Peroxidation and Ferroptosis
  JOURNAL   J Immunol 213 (7), 941-951 (2024)
   PUBMED   39158281
  REMARK    GeneRIF: Gpx4 Regulates Invariant NKT Cell Homeostasis and Function
            by Preventing Lipid Peroxidation and Ferroptosis.
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Li,X., He,J., Gao,X., Zheng,G., Chen,C., Chen,Y., Xing,Z., Wang,T.,
            Tang,J., Guo,Y. and He,Y.
  TITLE     GPX4 restricts ferroptosis of NKp46+ILC3s to control intestinal
            inflammation
  JOURNAL   Cell Death Dis 15 (9), 687 (2024)
   PUBMED   39300068
  REMARK    GeneRIF: GPX4 restricts ferroptosis of NKp46[+]ILC3s to control
            intestinal inflammation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Liu,C., Tian,W. and Lei,D.
  TITLE     GSTO2 ameliorates human neuroblastoma cell apoptosis, inflammation,
            ferroptosis, and oxidative stress by upregulating GPX4 expression
            in intracerebral hemorrhage
  JOURNAL   Drug Dev Res 85 (6), e22245 (2024)
   PUBMED   39154227
  REMARK    GeneRIF: GSTO2 ameliorates human neuroblastoma cell apoptosis,
            inflammation, ferroptosis, and oxidative stress by upregulating
            GPX4 expression in intracerebral hemorrhage.
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Sneddon,A.A., Wu,H.C., Farquharson,A., Grant,I., Arthur,J.R.,
            Rotondo,D., Choe,S.N. and Wahle,K.W.
  TITLE     Regulation of selenoprotein GPx4 expression and activity in human
            endothelial cells by fatty acids, cytokines and antioxidants
  JOURNAL   Atherosclerosis 171 (1), 57-65 (2003)
   PUBMED   14642406
  REMARK    GeneRIF: lipids, cytokines and antioxidants modulate GPx4 in a
            complex manner that in the presence of adequate selenium, may
            favour protection against potentially proatherogenic processes.
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Roveri,A., Flohe,L., Maiorino,M. and Ursini,F.
  TITLE     Phospholipid-hydroperoxide glutathione peroxidase in sperm
  JOURNAL   Methods Enzymol 347, 208-212 (2002)
   PUBMED   11898409
  REMARK    GeneRIF: Glutathione peroxidase is a moonlighting protein that
            functions both as a peroxidase as well as a structural protein in
            mature spermatozoa.
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Kelner,M.J. and Montoya,M.A.
  TITLE     Structural organization of the human selenium-dependent
            phospholipid hydroperoxide glutathione peroxidase gene (GPX4):
            chromosomal localization to 19p13.3
  JOURNAL   Biochem Biophys Res Commun 249 (1), 53-55 (1998)
   PUBMED   9705830
REFERENCE   8  (residues 1 to 227)
  AUTHORS   Opalenik,S.R., Ding,Q., Mallery,S.R. and Thompson,J.A.
  TITLE     Glutathione depletion associated with the HIV-1 TAT protein
            mediates the extracellular appearance of acidic fibroblast growth
            factor
  JOURNAL   Arch Biochem Biophys 351 (1), 17-26 (1998)
   PUBMED   9501919
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Esworthy,R.S., Doan,K., Doroshow,J.H. and Chu,F.F.
  TITLE     Cloning and sequencing of the cDNA encoding a human testis
            phospholipid hydroperoxide glutathione peroxidase
  JOURNAL   Gene 144 (2), 317-318 (1994)
   PUBMED   8039723
REFERENCE   10 (residues 1 to 227)
  AUTHORS   Chu,F.F.
  TITLE     The human glutathione peroxidase genes GPX2, GPX3, and GPX4 map to
            chromosomes 14, 5, and 19, respectively
  JOURNAL   Cytogenet Cell Genet 66 (2), 96-98 (1994)
   PUBMED   8287691
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC039849.1 and AL558552.3.
            
            Summary: The protein encoded by this gene belongs to the
            glutathione peroxidase family, members of which catalyze the
            reduction of hydrogen peroxide, organic hydroperoxides and lipid
            hydroperoxides, and thereby protect cells against oxidative damage.
            Several isozymes of this gene family exist in vertebrates, which
            vary in cellular location and substrate specificity. This isozyme
            has a high preference for lipid hydroperoxides and protects cells
            against membrane lipid peroxidation and cell death. It is also
            required for normal sperm development; thus, it has been identified
            as a 'moonlighting' protein because of its ability to serve dual
            functions as a peroxidase, as well as a structural protein in
            mature spermatozoa. Mutations in this gene are associated with
            Sedaghatian type of spondylometaphyseal dysplasia (SMDS). This
            isozyme is also a selenoprotein, containing the rare amino acid
            selenocysteine (Sec) at its active site. Sec is encoded by the UGA
            codon, which normally signals translation termination. The 3' UTRs
            of selenoprotein mRNAs contain a conserved stem-loop structure,
            designated the Sec insertion sequence (SECIS) element, that is
            necessary for the recognition of UGA as a Sec codon, rather than as
            a stop signal. Transcript variants resulting from alternative
            splicing or use of alternate promoters have been described to
            encode isoforms with different subcellular localization. [provided
            by RefSeq, Dec 2018].
            
            Transcript Variant: This variant (2) uses an alternate acceptor
            splice site in the 3' coding region, which causes a frame-shift,
            compared to variant 1. The resulting isoform (B) has a longer and a
            distinct C-terminus compared to isoform A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1940041.1, AL558552.3
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            multifunctional gene product(s)    :: PMID: 11898409
            protein contains selenocysteine    :: PMID: 8039723
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..227
                     /product="phospholipid hydroperoxide glutathione
                     peroxidase GPX4 isoform B precursor"
                     /EC_number="1.11.1.9"
                     /EC_number="1.11.1.12"
                     /note="phospholipid hydroperoxidase; sperm nucleus
                     glutathione peroxidase; phospholipid hydroperoxide
                     glutathione peroxidase, mitochondrial; epididymis
                     secretory sperm binding protein; selenoprotein GPX4;
                     phospholipid hydroperoxide glutathione peroxidase GPX4"
                     /calculated_mol_wt=22556
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2509
     Region          40..168
                     /region_name="GSH_Peroxidase"
                     /note="Glutathione (GSH) peroxidase family; tetrameric
                     selenoenzymes that catalyze the reduction of a variety of
                     hydroperoxides including lipid peroxidases, using GSH as a
                     specific electron donor substrate. GSH peroxidase contains
                     one selenocysteine residue per...; cd00340"
                     /db_xref="CDD:238207"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P36970; propagated from
                     UniProtKB/Swiss-Prot (P36969.3)"
     Site            order(73,108,163)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238207"
     Site            73
                     /site_type="other"
                     /note="Selenocysteine"
     Site            order(107,110,112,115,118,122)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238207"
     CDS             1..227
                     /gene="GPX4"
                     /gene_synonym="GPx-4; GSHPx-4; MCSP; PHGPx; SMDS; snGPx;
                     snPHGPx"
                     /coded_by="NM_001039847.3:51..734"
                     /note="UGA stop codon recoded as selenocysteine; isoform B
                     precursor is encoded by transcript variant 2"
                     /db_xref="GeneID:2879"
                     /db_xref="HGNC:HGNC:4556"
                     /db_xref="MIM:138322"
ORIGIN      
        1 mslgrlcrll kpallcgala apglagtmca srddwrcars mhefsakdid ghmvnldkyr
       61 gfvcivtnva squgktevny tqlvdlhary aecglrilaf pcnqfgkqep gsneeikefa
      121 agynvkfdmf skicvngdda hplwkwmkiq pkgkgilgna ikwnftkfgh rlstvphrqe
      181 rlrgealrth ggapgdregp aplflapqvc gparapahal gafhrhs
//
LOCUS       NP_068745                411 aa            linear   PRI 27-APR-2025
DEFINITION  homeobox protein aristaless-like 4 [Homo sapiens].
ACCESSION   NP_068745
VERSION     NP_068745.2
DBSOURCE    REFSEQ: accession NM_021926.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Peled,A., Sarig,O., Mohamad,J., Eskin-Schwartz,M., Vodo,D.,
            Bochner,R., Malchin,N., Isakov,O., Shomron,N., Fainberg,G.,
            Bertolini,M., Paus,R. and Sprecher,E.
  TITLE     Dominant frontonasal dysplasia with ectodermal defects results from
            increased activity of ALX4
  JOURNAL   Am J Med Genet A 191 (12), 2806-2812 (2023)
   PUBMED   37724761
  REMARK    GeneRIF: Dominant frontonasal dysplasia with ectodermal defects
            results from increased activity of ALX4.
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Fonteles,C.S., Finnell,R.H., Lei,Y., Zurita-Jimenez,M.E.,
            Monteiro,A.J., George,T.M. and Harshbarger,R.J.
  TITLE     De novo ALX4 variant detected in child with non-syndromic
            craniosynostosis
  JOURNAL   Braz J Med Biol Res 54 (11), e11396 (2021)
   PUBMED   34586326
  REMARK    GeneRIF: De novo ALX4 variant detected in child with non-syndromic
            craniosynostosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Walters,M.E., Lacassie,Y., Azamian,M., Franciskovich,R., Zapata,G.,
            Hernandez,P.P., Liu,P., Campbell,I.M., Bostwick,B.L. and
            Lalani,S.R.
  TITLE     Vertical transmission of a large calvarial ossification defect due
            to heterozygous variants of ALX4 and TWIST1
  JOURNAL   Am J Med Genet A 185 (3), 916-922 (2021)
   PUBMED   33369125
  REMARK    GeneRIF: Vertical transmission of a large calvarial ossification
            defect due to heterozygous variants of ALX4 and TWIST1.
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Xu,Q., Zhou,L., Yang,G., Meng,F., Wan,Y., Wang,L. and Zhang,L.
  TITLE     Overexpression of circ_0001445 decelerates hepatocellular carcinoma
            progression by regulating miR-942-5p/ALX4 axis
  JOURNAL   Biotechnol Lett 42 (12), 2735-2747 (2020)
   PUBMED   32856218
  REMARK    GeneRIF: Overexpression of circ_0001445 decelerates hepatocellular
            carcinoma progression by regulating miR-942-5p/ALX4 axis.
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Chen,C.H., Bournat,J.C., Wilken,N., Rosenfeld,J.A., Zhang,J.,
            Seth,A. and Jorgez,C.J.
  TITLE     Variants in ALX4 and their association with genitourinary defects
  JOURNAL   Andrology 8 (5), 1243-1255 (2020)
   PUBMED   32385972
  REMARK    GeneRIF: Variants in ALX4 and their association with genitourinary
            defects.
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Wu,Y.Q., Badano,J.L., McCaskill,C., Vogel,H., Potocki,L. and
            Shaffer,L.G.
  TITLE     Haploinsufficiency of ALX4 as a potential cause of parietal
            foramina in the 11p11.2 contiguous gene-deletion syndrome
  JOURNAL   Am J Hum Genet 67 (5), 1327-1332 (2000)
   PUBMED   11017806
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Qu,S., Tucker,S.C., Zhao,Q., deCrombrugghe,B. and Wisdom,R.
  TITLE     Physical and genetic interactions between Alx4 and Cart1
  JOURNAL   Development 126 (2), 359-369 (1999)
   PUBMED   9847249
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Bartsch,O., Wuyts,W., Van Hul,W., Hecht,J.T., Meinecke,P.,
            Hogue,D., Werner,W., Zabel,B., Hinkel,G.K., Powell,C.M.,
            Shaffer,L.G. and Willems,P.J.
  TITLE     Delineation of a contiguous gene syndrome with multiple exostoses,
            enlarged parietal foramina, craniofacial dysostosis, and mental
            retardation, caused by deletions in the short arm of chromosome 11
  JOURNAL   Am J Hum Genet 58 (4), 734-742 (1996)
   PUBMED   8644736
REFERENCE   9  (residues 1 to 411)
  AUTHORS   McGaughran,J.M., Ward,H.B. and Evans,D.G.
  TITLE     WAGR syndrome and multiple exostoses in a patient with
            del(11)(p11.2p14.2)
  JOURNAL   J Med Genet 32 (10), 823-824 (1995)
   PUBMED   8558565
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Mavrogiannis,L.A. and Wilkie,A.O.M.
  TITLE     Enlarged Parietal Foramina
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301307
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC103854.2 and AJ404888.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 15, 2004 this sequence version replaced NP_068745.1.
            
            Summary: This gene encodes a paired-like homeodomain transcription
            factor expressed in the mesenchyme of developing bones, limbs,
            hair, teeth, and mammary tissue. Mutations in this gene cause
            parietal foramina 2 (PFM2); an autosomal dominant disease
            characterized by deficient ossification of the parietal bones.
            Mutations in this gene also cause a form of frontonasal dysplasia
            with alopecia and hypogonadism; suggesting a role for this gene in
            craniofacial development, mesenchymal-epithelial communication, and
            hair follicle development. Deletion of a segment of chromosome 11
            containing this gene, del(11)(p11p12), causes Potocki-Shaffer
            syndrome (PSS); a syndrome characterized by craniofacial anomalies,
            cognitive disability, multiple exostoses, and genital abnormalities
            in males. In mouse, this gene has been shown to use dual
            translation initiation sites located 16 codons apart. [provided by
            RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB058691.1, AJ404888.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000652299.1/ ENSP00000498217.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..411
                     /product="homeobox protein aristaless-like 4"
                     /note="homeodomain transcription factor ALX4;
                     aristaless-like homeobox 4"
                     /calculated_mol_wt=44110
     Region          75..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H161.2)"
     Region          184..219
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H161.2)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H161.2)"
     Region          215..271
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          387..405
                     /region_name="OAR"
                     /note="OAR motif; pfam03826"
                     /db_xref="CDD:461067"
     Region          391..404
                     /region_name="OAR.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H161.2)"
     CDS             1..411
                     /gene="ALX4"
                     /gene_synonym="CRS5; FND2"
                     /coded_by="NM_021926.4:78..1313"
                     /db_xref="CCDS:CCDS31468.1"
                     /db_xref="GeneID:60529"
                     /db_xref="HGNC:HGNC:450"
                     /db_xref="MIM:605420"
ORIGIN      
        1 mnaetcvsyc espaaamday yspvsqsreg sspfrafpgg dkfgttflsa aakaqgfgda
       61 ksrarygagq qdlatplesg agargsfnkf qpqpstpqpq pppqpqpqqq qpqpqppaqp
      121 hlylqrgack tppdgslklq egssghsaal qvpcyakess lgepelppds dtvgmdssyl
      181 svkeagvkgp qdrassdlps plekadsesn kgkkrrnrtt ftsyqleele kvfqkthypd
      241 vyareqlamr tdltearvqv wfqnrrakwr krerfgqmqq vrthfstaye lplltraeny
      301 aqiqnpswlg nngaaspvpa cvvpcdpvpa cmsphahppg sgassvtdfl svsgagshvg
      361 qthmgslfga aslspglngy elngepdrkt ssiaalrmka kehsaaiswa t
//
LOCUS       NP_032665                353 aa            linear   ROD 27-APR-2025
DEFINITION  melatonin receptor type 1A [Mus musculus].
ACCESSION   NP_032665 XP_996424
VERSION     NP_032665.1
DBSOURCE    REFSEQ: accession NM_008639.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Bisikirska,B., Labella,R., Cuesta-Dominguez,A., Luo,N., De
            Angelis,J., Mosialou,I., Lin,C.S., Beck,D., Lata,S., Shyu,P.T.,
            McMahon,D.J., Guo,E., Hagen,J., Chung,W.K., Shane,E., Cohen,A. and
            Kousteni,S.
  TITLE     Melatonin receptor 1A variants as genetic cause of idiopathic
            osteoporosis
  JOURNAL   Sci Transl Med 16 (769), eadj0085 (2024)
   PUBMED   39413162
  REMARK    GeneRIF: Melatonin receptor 1A variants as genetic cause of
            idiopathic osteoporosis.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Pistono,C., Zimmermann,A., Morel,C., Herbeaux,K., Heraud,C.,
            Dumont-Kientzy,S., Pevet,P., Felder-Schmittbuhl,M.P. and Mathis,C.
  TITLE     Major role of MT2 receptors in the beneficial effect of melatonin
            on long-term recognition memory in C57BL/6J male mice
  JOURNAL   Horm Behav 136, 105076 (2021)
   PUBMED   34634697
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Zhao,H., Feng,L., Zhong,W., Zhen,H., Chi,Q. and Wang,X.
  TITLE     Hyperphosphorylation of Tau Due to the Interference of Protein
            Phosphatase Methylesterase-1 Overexpression by MiR-125b-5p in
            Melatonin Receptor Knockout Mice
  JOURNAL   Int J Mol Sci 22 (21), 11850 (2021)
   PUBMED   34769281
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Huang,Y.S., Lu,K.C., Chao,H.W., Chen,A., Chao,T.K., Guo,C.Y.,
            Hsieh,H.Y., Shih,H.M., Sytwu,H.K. and Wu,C.C.
  TITLE     The MTNR1A mRNA is stabilized by the cytoplasmic hnRNPL in renal
            tubular cells
  JOURNAL   J Cell Physiol 236 (3), 2023-2035 (2021)
   PUBMED   32730662
  REMARK    GeneRIF: The MTNR1A mRNA is stabilized by the cytoplasmic hnRNPL in
            renal tubular cells.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Martinez-Aguila,A., Fonseca,B., Perez de Lara,M.J.,
            Miras-Portugal,M.T., Gomez-Villafuertes,R., Carracedo,G. and
            Pintor,J.
  TITLE     Changes in melatonin receptor expression in a murine model of
            glaucoma
  JOURNAL   Mol Vis 26, 530-539 (2020)
   PUBMED   32818016
  REMARK    GeneRIF: Changes in melatonin receptor expression in a murine model
            of glaucoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Liu,C., Weaver,D.R., Jin,X., Shearman,L.P., Pieschl,R.L.,
            Gribkoff,V.K. and Reppert,S.M.
  TITLE     Molecular dissection of two distinct actions of melatonin on the
            suprachiasmatic circadian clock
  JOURNAL   Neuron 19 (1), 91-102 (1997)
   PUBMED   9247266
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Weaver,D.R., Liu,C. and Reppert,S.M.
  TITLE     Nature's knockout: the Mel1b receptor is not necessary for
            reproductive and circadian responses to melatonin in Siberian
            hamsters
  JOURNAL   Mol Endocrinol 10 (11), 1478-1487 (1996)
   PUBMED   8923472
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Roca,A.L., Godson,C., Weaver,D.R. and Reppert,S.M.
  TITLE     Structure, characterization, and expression of the gene encoding
            the mouse Mel1a melatonin receptor
  JOURNAL   Endocrinology 137 (8), 3469-3477 (1996)
   PUBMED   8754776
  REMARK    Erratum:[Endocrinology 1997 Jun;138(6):2307]
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Bermingham,N.A., Martin,J.E. and Fisher,E.M.
  TITLE     The mouse lysosomal membrane protein 1 gene as a candidate for the
            motorneuron degeneration (mnd) locus
  JOURNAL   Genomics 32 (2), 266-271 (1996)
   PUBMED   8833154
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Slaugenhaupt,S.A., Roca,A.L., Liebert,C.B., Altherr,M.R.,
            Gusella,J.F. and Reppert,S.M.
  TITLE     Mapping of the gene for the Mel1a-melatonin receptor to human
            chromosome 4 (MTNR1A) and mouse chromosome 8 (Mtnr1a)
  JOURNAL   Genomics 27 (2), 355-357 (1995)
   PUBMED   7558006
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158352.5.
            
            On May 4, 2006 this sequence version replaced XP_996424.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U52222.1, BC119313.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849378, SAMN00849384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 24.95 cM"
     Protein         1..353
                     /product="melatonin receptor type 1A"
                     /note="mel-1A-R; Mel1a receptor"
                     /calculated_mol_wt=39706
     Site            4
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q61184.1)"
     Site            10
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q61184.1)"
     Region          31..309
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          33..57
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61184.1)"
     Region          66..88
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61184.1)"
     Region          104..126
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61184.1)"
     Site            146..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61184.1)"
     Region          149..165
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          188..211
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            191..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61184.1)"
     Region          240..262
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61184.1)"
     Region          277..302
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61184.1)"
     CDS             1..353
                     /gene="Mtnr1a"
                     /gene_synonym="MelR; MR"
                     /coded_by="NM_008639.3:104..1165"
                     /db_xref="CCDS:CCDS22273.1"
                     /db_xref="GeneID:17773"
                     /db_xref="MGI:MGI:102967"
ORIGIN      
        1 mkgnvselln atqqapggge ggrprpswla stlafilift ivvdilgnll vilsvyrnkk
       61 lrnsgnifvv slavadlvva vypyplvlts ilnngwnlgy lhcqvsaflm glsvigsifn
      121 itgiamnryc yichslkydk iysnknslcy vfliwmltli aimpnlqtgt lqydpriysc
      181 tftqsvssay tiavvvfhfi vpmiivifcy lriwvlvlqv rrrvkpdnkp klkpqdfrnf
      241 vtmfvvfvlf aicwaplnli glivasdpat mvpripewlf vasyylayfn sclnaiiygl
      301 lnqnfrkeyk kiivslctak mffvessnee adkikckpsp lipnnnlikv dsv
//
LOCUS       NP_775798                340 aa            linear   PRI 27-APR-2025
DEFINITION  GTP-binding protein REM 2 [Homo sapiens].
ACCESSION   NP_775798
VERSION     NP_775798.2
DBSOURCE    REFSEQ: accession NM_173527.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Royer,L., Herzog,J.J., Kenny,K., Tzvetkova,B., Cochrane,J.C.,
            Marr,M.T. 2nd and Paradis,S.
  TITLE     The Ras-like GTPase Rem2 is a potent inhibitor of
            calcium/calmodulin-dependent kinase II activity
  JOURNAL   J Biol Chem 293 (38), 14798-14811 (2018)
   PUBMED   30072381
  REMARK    GeneRIF: report that substitution of two key amino acid residues in
            the Rem2 N terminus (Arg-79 and Arg-80) completely abolishes its
            ability to inhibit CaMKII
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Chai,S., Wan,X., Ramirez-Navarro,A., Tesar,P.J., Kaufman,E.S.,
            Ficker,E., George,A.L. Jr. and Deschenes,I.
  TITLE     Physiological genomics identifies genetic modifiers of long QT
            syndrome type 2 severity
  JOURNAL   J Clin Invest 128 (3), 1043-1056 (2018)
   PUBMED   29431731
  REMARK    GeneRIF: 2 novel gene variants in REM2 and KCNK17 that provide a
            physiologically plausible explanation for variable expressivity in
            a large subset of patients in a multigenerational long QT syndrome
            type 2 family
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Moore,A.R., Ghiretti,A.E. and Paradis,S.
  TITLE     A loss-of-function analysis reveals that endogenous Rem2 promotes
            functional glutamatergic synapse formation and restricts dendritic
            complexity
  JOURNAL   PLoS One 8 (8), e74751 (2013)
   PUBMED   23991227
  REMARK    GeneRIF: conclude that endogenous Rem2 is a positive regulator of
            functional, excitatory synapse development and a negative regulator
            of dendritic complexity
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Ghiretti,A.E. and Paradis,S.
  TITLE     The GTPase Rem2 regulates synapse development and dendritic
            morphology
  JOURNAL   Dev Neurobiol 71 (5), 374-389 (2011)
   PUBMED   21485012
  REMARK    GeneRIF: our results suggest that Rem2 regulates dendritic
            branching and synapse development
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Edel,M.J., Menchon,C., Menendez,S., Consiglio,A., Raya,A. and
            Izpisua Belmonte,J.C.
  TITLE     Rem2 GTPase maintains survival of human embryonic stem cells as
            well as enhancing reprogramming by regulating p53 and cyclin D1
  JOURNAL   Genes Dev 24 (6), 561-573 (2010)
   PUBMED   20231315
  REMARK    GeneRIF: Rem2 mediates the fibroblastic growth factor 2 (FGF2)
            signaling pathway to maintain proliferation of hESCsby suppressing
            the transcriptional activity of p53 and cyclin D(1)
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Bierings,R., Beato,M. and Edel,M.J.
  TITLE     An endothelial cell genetic screen identifies the GTPase Rem2 as a
            suppressor of p19ARF expression that promotes endothelial cell
            proliferation and angiogenesis
  JOURNAL   J Biol Chem 283 (7), 4408-4416 (2008)
   PUBMED   18056257
  REMARK    GeneRIF: data unravel a possible molecular mechanism for
            Rem2-induced angiogenesis and suggests Rem2 as a potential novel
            target for treating pathological angiogenesis
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Finlin,B.S., Mosley,A.L., Crump,S.M., Correll,R.N., Ozcan,S.,
            Satin,J. and Andres,D.A.
  TITLE     Regulation of L-type Ca2+ channel activity and insulin secretion by
            the Rem2 GTPase
  JOURNAL   J Biol Chem 280 (51), 41864-41871 (2005)
   PUBMED   15728182
  REMARK    GeneRIF: inhibition of L-type Ca2+ channels by Rem2 signaling may
            represent a new and potentially important mechanism for regulating
            Ca2+-triggered exocytosis in hormone-secreting cells, including
            insulin secretion in pancreatic beta-cells
REFERENCE   10 (residues 1 to 340)
  AUTHORS   Finlin,B.S., Shao,H., Kadono-Okuda,K., Guo,N. and Andres,D.A.
  TITLE     Rem2, a new member of the Rem/Rad/Gem/Kir family of Ras-related
            GTPases
  JOURNAL   Biochem J 347 Pt 1 (Pt 1), 223-231 (2000)
   PUBMED   10727423
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL135998.6, AK096283.1 and BC035663.1.
            
            On Jan 27, 2007 this sequence version replaced NP_775798.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096283.1, BC035663.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267396.9/ ENSP00000267396.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..340
                     /product="GTP-binding protein REM 2"
                     /EC_number="3.6.5.2"
                     /note="Rad and Gem-related 2 (rat homolog); rad and
                     Gem-like GTP-binding protein 2; RAS-like GTP binding 2;
                     RAS (RAD and GEM)-like GTP binding 2"
                     /calculated_mol_wt=37008
     Region          1..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYK8.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTY2; propagated from
                     UniProtKB/Swiss-Prot (Q8IYK8.2)"
     Region          115..340
                     /region_name="RGK"
                     /note="Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras
                     GTPases; cd04148"
                     /db_xref="CDD:206715"
     Site            121..128
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206715"
     Site            order(122..123,171..172)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(123..129,169,172,229..230,232,259..260)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206715"
     Site            order(128..129,141,143,152..153,166..167,169,171..172,261)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(142..143,150..153)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206715"
     Site            order(142..147,149..152)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206715"
     Site            144
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206715"
     Site            169..172
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206715"
     Site            order(171..172,181..184,187..190)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206715"
     Site            229..232
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206715"
     Site            259..261
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206715"
     Region          283..308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYK8.2)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTY2; propagated from
                     UniProtKB/Swiss-Prot (Q8IYK8.2)"
     Site            334..337
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:206715"
     CDS             1..340
                     /gene="REM2"
                     /coded_by="NM_173527.3:67..1089"
                     /db_xref="CCDS:CCDS45082.1"
                     /db_xref="GeneID:161253"
                     /db_xref="HGNC:HGNC:20248"
                     /db_xref="MIM:616955"
ORIGIN      
        1 mhtdldtdmd mdtettalcp sgsrrasppg tptpeadatl lkksekllae ldrsglpsap
       61 gaprrrgsmp vpykhqlrra qavdeldwpp qasssgssds lgsgeaapaq kdgifkvmlv
      121 gesgvgkstl agtfgglqgd sahepenped tyerrimvdk eevtlvvydi weqgdaggwl
      181 rdhclqtgda flivfsvtdr rsfskvpetl lrlragrphh dlpvilvgnk sdlarsrevs
      241 leegrhlagt lsckhietsa alhhntrelf egavrqirlr rgrnhaggqr pdpgspegpa
      301 pparresltk kakrflanlv prnakffkqr srschdlsvl
//
LOCUS       NP_478129                329 aa            linear   PRI 27-APR-2025
DEFINITION  beta-tectorin precursor [Homo sapiens].
ACCESSION   NP_478129
VERSION     NP_478129.1
DBSOURCE    REFSEQ: accession NM_058222.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,M., Eng,C., Hawk,E.T., Huang,M., Lin,J., Gu,J., Ellis,L.M. and
            Wu,X.
  TITLE     Identification of polymorphisms in ultraconserved elements
            associated with clinical outcomes in locally advanced colorectal
            adenocarcinoma
  JOURNAL   Cancer 118 (24), 6188-6198 (2012)
   PUBMED   22673945
  REMARK    GeneRIF: Single nucleotide polymorphism in the ultraconserved
            elements of TECTB gene is associated with recurrence in colorectal
            adenocarcinoma.
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kammerer,R., Ruttiger,L., Riesenberg,R., Schauble,C., Krupar,R.,
            Kamp,A., Sunami,K., Eisenried,A., Hennenberg,M., Grunert,F.,
            Bress,A., Battaglia,S., Schrewe,H., Knipper,M., Schneider,M.R. and
            Zimmermann,W.
  TITLE     Loss of mammal-specific tectorial membrane component
            carcinoembryonic antigen cell adhesion molecule 16 (CEACAM16) leads
            to hearing impairment at low and high frequencies
  JOURNAL   J Biol Chem 287 (26), 21584-21598 (2012)
   PUBMED   22544735
  REMARK    GeneRIF: CEACAM16 can probably form higher order structures with
            other tectorial membrane proteins such as alpha-tectorin and
            beta-tectorin and influences the physical properties of the
            tectorial membrane
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Legan,P.K., Rau,A., Keen,J.N. and Richardson,G.P.
  TITLE     The mouse tectorins. Modular matrix proteins of the inner ear
            homologous to components of the sperm-egg adhesion system
  JOURNAL   J Biol Chem 272 (13), 8791-8801 (1997)
   PUBMED   9079715
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL391986.12 and BC113499.1.
            
            Summary: This gene encodes a non-collagenous glycoprotein component
            of the tectorial membrane, which covers the auditory hair cells in
            the cochlea of the inner ear. A similar protein in mouse functions
            in low-frequency hearing. [provided by RefSeq, Jul 2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.20874.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA2144835 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000646139.2/ ENSP00000494896.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q25.2"
     Protein         1..329
                     /product="beta-tectorin precursor"
                     /note="beta-tectorin"
                     /calculated_mol_wt=35192
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1782
     mat_peptide     18..305
                     /product="Beta-tectorin. /id=PRO_0000041741"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PL2.1)"
                     /calculated_mol_wt=32512
     Region          32..283
                     /region_name="ZP"
                     /note="Zona pellucida (ZP) domain; smart00241"
                     /db_xref="CDD:214579"
     Site            80
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PL2.1)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PL2.1)"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PL2.1)"
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PL2.1)"
     CDS             1..329
                     /gene="TECTB"
                     /coded_by="NM_058222.3:185..1174"
                     /db_xref="CCDS:CCDS7571.1"
                     /db_xref="GeneID:6975"
                     /db_xref="HGNC:HGNC:11721"
                     /db_xref="MIM:602653"
ORIGIN      
        1 mvtkafvlla ifaeasaksc apnkadvilv fcypktiitk ipecpygwev hqlalgglcy
       61 ngvheggyyq fvipdlspkn ksycgtqsey kppiyhfysh ivsndttviv knqpvnysfs
      121 ctyhstylvn qaafdqrvat vhvkngsmgt fesqlslnfy tnakfsikke apfvleasei
      181 gsdlfagvea kglsirfkvv lnscwatpsa dfmyplqwql inkgcptdet vlvhengrdh
      241 ratfqfnafr fqnipklskv wlhcetficd seklscpvtc dkrkrllrdq tggvlvvels
      301 lrsrgfssly sfsdvlhhli mmlgicavl
//
LOCUS       NP_001265488            1004 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 316 [Homo sapiens].
ACCESSION   NP_001265488 XP_003959965 XP_003960047 XP_003960424 XP_003960977
VERSION     NP_001265488.1
DBSOURCE    REFSEQ: accession NM_001278559.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073343.6.
            
            On or before Jun 22, 2013 this sequence version replaced
            XP_003960977.1, XP_003959965.1, XP_003960047.1, XP_003960424.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000382252.6/ ENSP00000477706.1
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..1004
                     /product="zinc finger protein 316"
                     /calculated_mol_wt=108307
     Region          1..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NFI3.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (A6NFI3.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (A6NFI3.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (A6NFI3.1)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (A6NFI3.1)"
     Region          158..218
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <345..506
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          347..367
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          375..395
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(380,382,384,386..387,390..391,394,408,410,414..415,
                     418..419,422,436,438,440,442..443,446..447,450)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          403..423
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          431..451
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          459..479
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          487..505
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          508..574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NFI3.1)"
     Region          693..713
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(698,700,702,704..705,708..709,712,726,728,732..733,
                     736..737,740,754,756,758,760..761,764..765,768)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          705..730
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          721..741
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <746..933
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          749..769
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          777..797
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          805..825
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          833..853
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(838,840,842,844..845,848..849,852,866,868,872..873,
                     876..877,880,894,896,898,900..901,904..905,908)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          861..881
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          889..909
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          917..937
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          936..976
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NFI3.1)"
     CDS             1..1004
                     /gene="ZNF316"
                     /gene_synonym="MZF-3"
                     /coded_by="NM_001278559.2:561..3575"
                     /db_xref="CCDS:CCDS75563.1"
                     /db_xref="GeneID:100131017"
                     /db_xref="HGNC:HGNC:13843"
ORIGIN      
        1 maalhttpds paaqleraed gsecdpdqee eeeeeekgee vqeveeeeee ivveeeeegv
       61 aevvqdaqve avaevevead veeedvkevl aeeecpalgt qerlsrggda kspvlqekgl
      121 qasrapatpr dedleeeeee eedededdll tagcqelvtf edvavyfsle ewerleadqr
      181 glyqevmqen ygilvslgyp ipkpdlifrl eqgeepwvpd sprpeegdiv tgvytgawfw
      241 tddiedheee ddedflaeva eeeneppglw saaygvgdvp gtwgpddsds aqtpegwgpd
      301 pgglgvladg seakpflpgr epganllspw afpaavappa grpettcdvc gkvfphrsrl
      361 akhqryhaav kpfgceecgk gfvyrshlai hqrthtgekp fpcpdcgkrf vykshlvthr
      421 rihtgerpyr cafcgagfgr rsylvthqrt htgerpypcs hcgrsfsqss alarhqavht
      481 adrphccpdc gqafrlradf qrhrrgggca eaggdgprre pgetaaaagp edtdpgpegs
      541 evgeadgeae aaaeereeaa vaaptpsgkv dpaperrfle lgnglgegeg psshplgfhf
      601 pvhpkswlhp dsfpilglpd frerlpvdgr plpaplggpl slvegtglac dpfggggaag
      661 gggglrafgp aiggllaepa paalaeeesp wicsdcgktf grraalakhq ryhagerphr
      721 cadcgksfvy gshlarhrrt htgerpfpcp ecgarfargs hlaahvrght gekpfvcgvc
      781 gagfsrrahl tahgrahtge rpyacgecgr rfgqsaaltr hqwahaeekp hrcpdcgkgf
      841 ghssdfkrhr rthtgekpfr cadcgrgfaq rsnlakhrrg htgerpfpcp ecgkrfsqrs
      901 vlvthqrtht gerpyacanc grrfsqsshl lthmkthrga taapgsgsap apapkpeaaa
      961 kgpssagpge rgsallefag gtsfgsehqa afagpsgayr egvl
//
LOCUS       NP_660335                443 aa            linear   PRI 27-APR-2025
DEFINITION  inactive polypeptide N-acetylgalactosaminyltransferase-like protein
            5 [Homo sapiens].
ACCESSION   NP_660335
VERSION     NP_660335.2
DBSOURCE    REFSEQ: accession NM_145292.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Hagiuda,J., Takasaki,N., Oya,M., Ishikawa,H. and Narimatsu,H.
  TITLE     Mutation of GALNTL5 gene identified in patients diagnosed with
            asthenozoospermia
  JOURNAL   Hum Fertil (Camb) 23 (4), 226-233 (2020)
   PUBMED   30628500
  REMARK    GeneRIF: Mutation of GALNTL5 gene identified in patients diagnosed
            with asthenozoospermia.
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Takasaki,N., Tachibana,K., Ogasawara,S., Matsuzaki,H., Hagiuda,J.,
            Ishikawa,H., Mochida,K., Inoue,K., Ogonuki,N., Ogura,A., Noce,T.,
            Ito,C., Toshimori,K. and Narimatsu,H.
  TITLE     A heterozygous mutation of GALNTL5 affects male infertility with
            impairment of sperm motility
  JOURNAL   Proc Natl Acad Sci U S A 111 (3), 1120-1125 (2014)
   PUBMED   24398516
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC022021.2, AC074257.5 and AW103179.1.
            
            On Dec 23, 2009 this sequence version replaced NP_660335.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the functional protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022021.2, HM005684.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392800.7/ ENSP00000376548.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..443
                     /product="inactive polypeptide
                     N-acetylgalactosaminyltransferase-like protein 5"
                     /note="putative polypeptide
                     N-acetylgalactosaminyltransferase-like protein 5;
                     galNAc-T15; pp-GaNTase 15; polypeptide GalNAc transferase
                     15; UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase-like 5; polypeptide
                     GalNAc transferase-like 5; protein-UDP
                     acetylgalactosaminyltransferase 15; UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase 15; testis tissue
                     sperm-binding protein Li 61n"
                     /calculated_mol_wt=51297
     Site            5..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z4T8.3)"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4T8.3)"
     Region          133..243
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z4T8.3)"
     Region          137..433
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(141..143,145,174,204,207,211,227..229,309..310,
                     332..333,335,360,363,370)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(227,229,360)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          301..363
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z4T8.3)"
     CDS             1..443
                     /gene="GALNTL5"
                     /gene_synonym="GalNAc-T5L; GALNACT19; GALNT15"
                     /coded_by="NM_145292.4:204..1535"
                     /db_xref="CCDS:CCDS5929.1"
                     /db_xref="GeneID:168391"
                     /db_xref="HGNC:HGNC:21725"
                     /db_xref="MIM:615133"
ORIGIN      
        1 mrnaiiqglf ygsltfgiwt allfiylhhn hvsswqkksq eplsawspgk kvhqqiiygs
       61 eqipkphviv krtdedkaks mlgtdfnhtn pelhkellky gfnviisrsl gierevpdtr
      121 skmclqkhyp arlptasivi cfyneecnal fqtmssvtnl tphyfleeii lvddmskvdd
      181 lkekldyhle tfrgkvkiir nkkreglira rligashasg dvlvfldshc evnrvwlepl
      241 lhaiakdpkm vvcplidvid drtleykpsp lvrgtfdwnl qfkwdnvfsy emdgpegstk
      301 pirspamsgg ifairrhyfn eigqydkdmd fwgrenlels lriwmcggql fiipcsrvgh
      361 iskkqtgkps tiisamthny lrlvhvwlde ykeqfflrkp glkyvtygni rervelrkrl
      421 gcksfqwyld nvfpeleasv nsl
//
LOCUS       NP_001352732             415 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 641 isoform 3 [Homo sapiens].
ACCESSION   NP_001352732 XP_016874286
VERSION     NP_001352732.1
DBSOURCE    REFSEQ: accession NM_001365803.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Yan,H., He,N. and He,S.
  TITLE     HCG15 is a hypoxia-responsive lncRNA and facilitates hepatocellular
            carcinoma cell proliferation and invasion by enhancing ZNF641
            transcription
  JOURNAL   Biochem Biophys Res Commun 608, 170-176 (2022)
   PUBMED   35427894
  REMARK    GeneRIF: HCG15 is a hypoxia-responsive lncRNA and facilitates
            hepatocellular carcinoma cell proliferation and invasion by
            enhancing ZNF641 transcription.
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Qi,X., Li,Y., Xiao,J., Yuan,W., Yan,Y., Wang,Y., Liang,S., Zhu,C.,
            Chen,Y., Liu,M. and Wu,X.
  TITLE     Activation of transcriptional activities of AP-1 and SRE by a new
            zinc-finger protein ZNF641
  JOURNAL   Biochem Biophys Res Commun 339 (4), 1155-1164 (2006)
   PUBMED   16343441
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC024257.25.
            
            On Sep 12, 2018 this sequence version replaced XP_016874286.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.326774.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..415
                     /product="zinc finger protein 641 isoform 3"
                     /calculated_mol_wt=46394
     Region          <2..90
                     /region_name="PLN03206"
                     /note="phosphoribosylformylglycinamidine synthase;
                     Provisional"
                     /db_xref="CDD:178745"
     Region          243..263
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(243,246,259,263)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(248,250,252,254..255,258..259,262,276,278,282..283,
                     286..287,290,304,306,308,310..311,314..315,318)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          267..>321
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          271..296
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          271..291
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(276,282,289,295,298,305)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          299..319
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          299..319
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          328..>407
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          351..371
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          379..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..415
                     /gene="ZNF641"
                     /coded_by="NM_001365803.1:160..1407"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS53787.1"
                     /db_xref="GeneID:121274"
                     /db_xref="HGNC:HGNC:31834"
                     /db_xref="MIM:613906"
ORIGIN      
        1 mlseqtaalg tgwesmnvql dgaepqverg sqeerpwrtv pgplehlccd leeepqslqe
       61 kaqsapwvpa ipqegntgdw emaaallaag sqvssaslgv scgpitaafv llshqpidel
      121 ahmiingfpi pkldmlsqle ggeeqwvpdp qdleerdilr vtytgdgseh egdtpeleae
      181 pprmlssvse dtvlwnpehd eswdsmpsss rgmllgppfl qedsfsnllc stemdsllrp
      241 htcpqcgkqf vwgshlarhq qthtgerpys clkcektfgr rhhlirhqkt hlhdktsrcs
      301 ecgknfrcns hlashqrvha egksckgqev gespgtrkrq rappvpkchv ctecgksfgr
      361 rhhlvrhwlt htgekpfqcp rceksfgrkh hldrhllthq gqsprnswdr gtsvf
//
LOCUS       NP_001160                261 aa            linear   PRI 27-APR-2025
DEFINITION  aquaporin-8 [Homo sapiens].
ACCESSION   NP_001160
VERSION     NP_001160.2
DBSOURCE    REFSEQ: accession NM_001169.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Shen,Z., Sheng,H., Zhao,J., Xu,J., Cai,Z., Zhang,H., Guo,Z.,
            Liu,J., Liang,H., Tan,L., Gan,S., Huang,J. and Zhu,S.
  TITLE     AQP8 Modulates Mitochondrial H2O2 Transport to Influence Glioma
            Proliferation
  JOURNAL   Cancer Invest 42 (4), 345-356 (2024)
   PUBMED   38742677
  REMARK    GeneRIF: AQP8 Modulates Mitochondrial H2O2 Transport to Influence
            Glioma Proliferation.
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Lin,C., He,H., Kim,J.J., Zheng,X., Huang,Z. and Dai,N.
  TITLE     Osmotic pressure induces translocation of aquaporin-8 by P38 and
            JNK MAPK signaling pathways in patients with functional
            constipation
  JOURNAL   Dig Liver Dis 55 (8), 1049-1059 (2023)
   PUBMED   36792433
  REMARK    GeneRIF: Osmotic pressure induces translocation of aquaporin-8 by
            P38 and JNK MAPK signaling pathways in patients with functional
            constipation.
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Capiglioni,A.M., Capitani,M.C., Marrone,J. and Marinelli,R.A.
  TITLE     Adenoviral Transfer of Human Aquaporin-8 Gene to Mouse Liver
            Improves Ammonia-Derived Ureagenesis
  JOURNAL   Cells 12 (11), 1535 (2023)
   PUBMED   37296655
  REMARK    GeneRIF: Adenoviral Transfer of Human Aquaporin-8 Gene to Mouse
            Liver Improves Ammonia-Derived Ureagenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Cai,Z., Shen,Z., Zhao,J., Zhang,H., Guo,Z., Xia,Q., Liang,H.,
            Liu,J., Tan,L., Sheng,H. and Zhu,S.
  TITLE     AQP8 may affect glioma proliferation and growth by regulating
            GSK-3beta phosphorylation and nuclear transport of beta-catenin
  JOURNAL   Int J Dev Neurosci 83 (4), 333-345 (2023)
   PUBMED   37081713
  REMARK    GeneRIF: AQP8 may affect glioma proliferation and growth by
            regulating GSK-3beta phosphorylation and nuclear transport of
            beta-catenin.
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Capiglioni,A.M., Muller,G.L., Marrone,J., Alvarez,M.L. and
            Marinelli,R.A.
  TITLE     Enhanced ammonia detoxification to urea in hepatocytes transduced
            with human aquaporin-8 gene
  JOURNAL   Biotechnol Bioeng 118 (11), 4331-4337 (2021)
   PUBMED   34292591
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Kuwahara,M., Gu,Y., Ishibashi,K., Marumo,F. and Sasaki,S.
  TITLE     Mercury-sensitive residues and pore site in AQP3 water channel
  JOURNAL   Biochemistry 36 (46), 13973-13978 (1997)
   PUBMED   9369468
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Harrington,D.J., Adachi,K. and Royer,W.E. Jr.
  TITLE     The high resolution crystal structure of deoxyhemoglobin S
  JOURNAL   J Mol Biol 272 (3), 398-407 (1997)
   PUBMED   9325099
  REMARK    GeneRIF: The crystal structure of deoxyhemoglobin S, 2HBS,
            demonstrates the interaction of the mutant valine with another
            hemoglobin tetramer and provides insights into formation of the
            intracellular sickle cell fiber.
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Raina,S., Preston,G.M., Guggino,W.B. and Agre,P.
  TITLE     Molecular cloning and characterization of an aquaporin cDNA from
            salivary, lacrimal, and respiratory tissues
  JOURNAL   J Biol Chem 270 (4), 1908-1912 (1995)
   PUBMED   7530250
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008741.7, AB013456.1 and
            BC040630.1.
            
            On Mar 15, 2004 this sequence version replaced NP_001160.1.
            
            Summary: Aquaporin 8 (AQP8) is a water channel protein. Aquaporins
            are a family of small integral membrane proteins related to the
            major intrinsic protein (MIP or AQP0).  Aquaporin 8 mRNA is found
            in pancreas and colon but not other tissues. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF067797.1, AB013456.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219660.6/ ENSP00000219660.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.1"
     Protein         1..261
                     /product="aquaporin-8"
                     /calculated_mol_wt=27250
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94778.2)"
     Region          38..231
                     /region_name="MIP"
                     /note="Major intrinsic protein (MIP) superfamily. Members
                     of the MIP superfamily function as membrane channels that
                     selectively transport water, small neutral molecules, and
                     ions out of and between cells. The channel proteins share
                     a common fold: the N-terminal...; cl00200"
                     /db_xref="CDD:444743"
     Site            59
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94778.2)"
     Site            order(72,90..92,206..207,210,213)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            85..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94778.2)"
     Site            order(92..94,210..212)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     Region          92..94
                     /region_name="NPA 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O94778.2)"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94778.2)"
     Site            139
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O94778.2)"
     Site            157..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94778.2)"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94778.2)"
     Region          210..212
                     /region_name="NPA 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O94778.2)"
     Site            229..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94778.2)"
     CDS             1..261
                     /gene="AQP8"
                     /gene_synonym="AQP-8"
                     /coded_by="NM_001169.3:100..885"
                     /db_xref="CCDS:CCDS10626.1"
                     /db_xref="GeneID:343"
                     /db_xref="HGNC:HGNC:642"
                     /db_xref="MIM:603750"
ORIGIN      
        1 msgeiamcep efgndkarep svggrwrvsw yerfvqpclv ellgsalfif igclsvieng
       61 tdtgllqpal ahglalglvi atlgnisggh fnpavslaam ligglnlvml lpywvsqllg
      121 gmlgaalaka vspeerfwna sgaafvtvqe qgqvagalva eiilttllal avcmgainek
      181 tkgplapfsi gfavtvdila ggpvsggcmn parafgpavv anhwnfhwiy wlgpllagll
      241 vgllircfig dgktrlilka r
//
LOCUS       NP_003137                709 aa            linear   PRI 27-APR-2025
DEFINITION  FACT complex subunit SSRP1 [Homo sapiens].
ACCESSION   NP_003137
VERSION     NP_003137.1
DBSOURCE    REFSEQ: accession NM_003146.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Lyu,Y., Yang,Y., Talwar,V., Lu,H., Chen,C., Salman,S., Wicks,E.E.,
            Huang,T.Y., Drehmer,D., Wang,Y., Zuo,Q., Datan,E., Jackson,W. 3rd,
            Dordai,D., Wang,R. and Semenza,G.L.
  TITLE     Hypoxia-inducible factor 1 recruits FACT and RNF20/40 to mediate
            histone ubiquitination and transcriptional activation of target
            genes
  JOURNAL   Cell Rep 43 (4), 113972 (2024)
   PUBMED   38517892
  REMARK    GeneRIF: Hypoxia-inducible factor 1 recruits FACT and RNF20/40 to
            mediate histone ubiquitination and transcriptional activation of
            target genes.
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Chen,X., Li,M., Wang,D., Wang,Q., Wei,X., Liu,X., Yang,J.,
            Kalvakolanu,D.V., Guo,B. and Zhang,L.
  TITLE     Histone chaperone SSRP1 is required for apoptosis inhibition and
            mitochondrial function in HCC via transcriptional promotion of
            TRAP1
  JOURNAL   Biochem Cell Biol 101 (4), 361-376 (2023)
   PUBMED   37084412
  REMARK    GeneRIF: Histone chaperone SSRP1 is required for apoptosis
            inhibition and mitochondrial function in HCC via transcriptional
            promotion of TRAP1.
REFERENCE   3  (residues 1 to 709)
  AUTHORS   McCauley,M.J., Morse,M., Becker,N., Hu,Q., Botuyan,M.V.,
            Navarrete,E., Huo,R., Muthurajan,U.M., Rouzina,I., Luger,K.,
            Mer,G., Maher,L.J. 3rd and Williams,M.C.
  TITLE     Human FACT subunits coordinate to catalyze both disassembly and
            reassembly of nucleosomes
  JOURNAL   Cell Rep 41 (13), 111858 (2022)
   PUBMED   36577379
  REMARK    GeneRIF: Human FACT subunits coordinate to catalyze both
            disassembly and reassembly of nucleosomes.
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Sivkina,A.L., Karlova,M.G., Valieva,M.E., McCullough,L.L.,
            Formosa,T., Shaytan,A.K., Feofanov,A.V., Kirpichnikov,M.P.,
            Sokolova,O.S. and Studitsky,V.M.
  TITLE     Electron microscopy analysis of ATP-independent nucleosome
            unfolding by FACT
  JOURNAL   Commun Biol 5 (1), 2 (2022)
   PUBMED   35013515
  REMARK    GeneRIF: Electron microscopy analysis of ATP-independent nucleosome
            unfolding by FACT.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Dyer,M.A., Hayes,P.J. and Baron,M.H.
  TITLE     The HMG domain protein SSRP1/PREIIBF is involved in activation of
            the human embryonic beta-like globin gene
  JOURNAL   Mol Cell Biol 18 (5), 2617-2628 (1998)
   PUBMED   9566881
REFERENCE   7  (residues 1 to 709)
  AUTHORS   Orphanides,G., LeRoy,G., Chang,C.H., Luse,D.S. and Reinberg,D.
  TITLE     FACT, a factor that facilitates transcript elongation through
            nucleosomes
  JOURNAL   Cell 92 (1), 105-116 (1998)
   PUBMED   9489704
REFERENCE   8  (residues 1 to 709)
  AUTHORS   Nagulapalli,S., Pongubala,J.M. and Atchison,M.L.
  TITLE     Multiple proteins physically interact with PU.1. Transcriptional
            synergy with NF-IL6 beta (C/EBP delta, CRP3)
  JOURNAL   J Immunol 155 (9), 4330-4338 (1995)
   PUBMED   7594592
REFERENCE   9  (residues 1 to 709)
  AUTHORS   Bruhn,S.L., Pil,P.M., Essigmann,J.M., Housman,D.E. and Lippard,S.J.
  TITLE     Isolation and characterization of human cDNA clones encoding a high
            mobility group box protein that recognizes structural distortions
            to DNA caused by binding of the anticancer agent cisplatin
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2307-2311 (1992)
   PUBMED   1372440
REFERENCE   10 (residues 1 to 709)
  AUTHORS   Toney,J.H., Donahue,B.A., Kellett,P.J., Bruhn,S.L., Essigmann,J.M.
            and Lippard,S.J.
  TITLE     Isolation of cDNAs encoding a human protein that binds selectively
            to DNA modified by the anticancer drug
            cis-diamminedichloroplatinum(II)
  JOURNAL   Proc Natl Acad Sci U S A 86 (21), 8328-8332 (1989)
   PUBMED   2530581
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1990 Feb;87(4):1625]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000781.6.
            
            Summary: The protein encoded by this gene is a subunit of a
            heterodimer that, along with SUPT16H, forms chromatin
            transcriptional elongation factor FACT. FACT interacts specifically
            with histones H2A/H2B to effect nucleosome disassembly and
            transcription elongation. FACT and cisplatin-damaged DNA may be
            crucial to the anticancer mechanism of cisplatin. This encoded
            protein contains a high mobility group box which most likely
            constitutes the structure recognition element for
            cisplatin-modified DNA. This protein also functions as a
            co-activator of the transcriptional activator p63. An alternatively
            spliced transcript variant of this gene has been described, but its
            full-length nature is not known. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.5331.1,
                                           SRR11853560.5239.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278412.7/ ENSP00000278412.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..709
                     /product="FACT complex subunit SSRP1"
                     /note="chromatin-specific transcription elongation factor
                     80 kDa subunit; high mobility group box; facilitates
                     chromatin remodeling 80 kDa subunit; cisplatin-DNA SSRP;
                     hSSRP1; FACTp80; FACT 80 kDa subunit; recombination signal
                     sequence recognition protein 1; facilitates chromatin
                     transcription complex subunit SSRP1; facilitates chromatin
                     transcription complex 80 kDa subunit"
                     /calculated_mol_wt=80944
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.3,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Region          21..480
                     /region_name="POB3"
                     /note="Nucleosome-binding factor SPN, POB3 subunit
                     [Transcription / DNA replication, recombination, and
                     repair / Chromatin structure and dynamics]; COG5165"
                     /db_xref="CDD:227494"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            413
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q08943; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            450..451
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3 and/or caspase-7; propagated
                     from UniProtKB/Swiss-Prot (Q08945.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q08943; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Region          458..709
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08945.1)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000305|PubMed:15659405; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            542
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q08943; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Region          549..615
                     /region_name="HMG-box_SSRP1-like"
                     /note="high mobility group (HMG)-box found in
                     structure-specific recognition protein 1 (SSRP1) and
                     similar proteins; cd21994"
                     /db_xref="CDD:438810"
     Site            order(549,551..552,554..555,558..559,562,566,574..575,
                     578..579,582,585..586,607,611,615)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438810"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15659405,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q08945.1)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000305|PubMed:15659405; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     CDS             1..709
                     /gene="SSRP1"
                     /gene_synonym="FACT; FACT80; T160"
                     /coded_by="NM_003146.3:283..2412"
                     /db_xref="CCDS:CCDS7952.1"
                     /db_xref="GeneID:6749"
                     /db_xref="HGNC:HGNC:11327"
                     /db_xref="MIM:604328"
ORIGIN      
        1 maetlefndv yqevkgsmnd grlrlsrqgi ifknsktgkv dniqagelte giwrrvalgh
       61 glklltkngh vykydgfres efeklsdffk thyrlelmek dlcvkgwnwg tvkfggqlls
      121 fdigdqpvfe iplsnvsqct tgknevtlef hqnddaevsl mevrfyvppt qedgvdpvea
      181 faqnvlskad viqatgdaic ifrelqcltp rgrydiriyp tflhlhgktf dykipyttvl
      241 rlfllphkdq rqmffvisld ppikqgqtry hflillfskd edisltlnmn eeevekrfeg
      301 rltknmsgsl yemvsrvmka lvnrkitvpg nfqghsgaqc itcsykassg llyplergfi
      361 yvhkppvhir fdeisfvnfa rgttttrsfd feietkqgtq ytfssieree ygklfdfvna
      421 kklniknrgl kegmnpsyde yadsdedqhd aylermkeeg kireenands sddsgeetde
      481 sfnpgeeeed vaeefdsnas assssnegds drdekkrkql kkakmakdrk srkkpvevkk
      541 gkdpnapkrp msaymlwlna srekiksdhp gisitdlskk ageiwkgmsk ekkeewdrka
      601 edarrdyeka mkeyeggrge sskrdkskkk kkvkvkmekk stpsrgsssk sssrqlsesf
      661 kskefvssde sssgenkskk krrrsedsee eelastppss edsasgsde
//
LOCUS       NP_006491                646 aa            linear   PRI 27-APR-2025
DEFINITION  cell surface glycoprotein MUC18 precursor [Homo sapiens].
ACCESSION   NP_006491
VERSION     NP_006491.2
DBSOURCE    REFSEQ: accession NM_006500.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Chen,J.M., He,J., Qiu,J.M., Yang,G.G., Wang,D. and Shen,Z.
  TITLE     Netrin-1-CD146 and netrin-1-S100A9 are associated with early stage
            of lymph node metastasis in colorectal cancer
  JOURNAL   BMC Gastroenterol 24 (1), 308 (2024)
   PUBMED   39261771
  REMARK    GeneRIF: Netrin-1-CD146 and netrin-1-S100A9 are associated with
            early stage of lymph node metastasis in colorectal cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Wei,N., Wu,X., Yu,Y., Zhou,H., Cui,K., Zhao,X. and Zhang,X.
  TITLE     CD146 Promotes EMT-Mediated Migration and Invasion of NSCLC via
            PI3K/Akt Signaling Pathway
  JOURNAL   Front Biosci (Landmark Ed) 29 (4), 140 (2024)
   PUBMED   38682195
  REMARK    GeneRIF: CD146 Promotes EMT-Mediated Migration and Invasion of
            NSCLC via PI3K/Akt Signaling Pathway.
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Boutin,L., Roger,E., Gayat,E., Depret,F., Blot-Chabaud,M. and
            Chadjichristos,C.E.
  TITLE     The role of CD146 in renal disease: from experimental nephropathy
            to clinics
  JOURNAL   J Mol Med (Berl) 102 (1), 11-21 (2024)
   PUBMED   37993561
  REMARK    GeneRIF: The role of CD146 in renal disease: from experimental
            nephropathy to clinics.
            Review article
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Chen,J., Xu,Q., Liu,D., Li,X., Guo,M., Chen,X., Liao,J., Lei,R.,
            Li,W., Huang,H., Saw,P.E., Song,E., Yan,X. and Nie,Y.
  TITLE     CD146 promotes malignant progression of breast phyllodes tumor
            through suppressing DCBLD2 degradation and activating the AKT
            pathway
  JOURNAL   Cancer Commun (Lond) 43 (11), 1244-1266 (2023)
   PUBMED   37856423
  REMARK    GeneRIF: CD146 promotes malignant progression of breast phyllodes
            tumor through suppressing DCBLD2 degradation and activating the AKT
            pathway.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Li,Y., Chai,J.L., Shi,X., Feng,Y., Li,J.J., Zhou,L.N., Cao,C. and
            Li,K.R.
  TITLE     Galphai1/3 mediate Netrin-1-CD146-activated signaling and
            angiogenesis
  JOURNAL   Theranostics 13 (7), 2319-2336 (2023)
   PUBMED   37153740
  REMARK    GeneRIF: Galphai1/3 mediate Netrin-1-CD146-activated signaling and
            angiogenesis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Bardin,N., Frances,V., Lesaule,G., Horschowski,N., George,F. and
            Sampol,J.
  TITLE     Identification of the S-Endo 1 endothelial-associated antigen
  JOURNAL   Biochem Biophys Res Commun 218 (1), 210-216 (1996)
   PUBMED   8573133
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Shih,I.M., Elder,D.E., Speicher,D., Johnson,J.P. and Herlyn,M.
  TITLE     Isolation and functional characterization of the A32
            melanoma-associated antigen
  JOURNAL   Cancer Res 54 (9), 2514-2520 (1994)
   PUBMED   8162602
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Johnson,J.P., Rothbacher,U. and Sers,C.
  TITLE     The progression associated antigen MUC18: a unique member of the
            immunoglobulin supergene family
  JOURNAL   Melanoma Res 3 (5), 337-340 (1993)
   PUBMED   8292890
  REMARK    Review article
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Sers,C., Kirsch,K., Rothbacher,U., Riethmuller,G. and Johnson,J.P.
  TITLE     Genomic organization of the melanoma-associated glycoprotein MUC18:
            implications for the evolution of the immunoglobulin domains
  JOURNAL   Proc Natl Acad Sci U S A 90 (18), 8514-8518 (1993)
   PUBMED   8378324
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Lehmann,J.M., Riethmuller,G. and Johnson,J.P.
  TITLE     MUC18, a marker of tumor progression in human melanoma, shows
            sequence similarity to the neural cell adhesion molecules of the
            immunoglobulin superfamily
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9891-9895 (1989)
   PUBMED   2602381
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AU076908.1, BC056418.1, AB209925.1 and AP002956.1.
            
            On Jul 27, 2005 this sequence version replaced NP_006491.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF089868.1, SRR1803614.131276.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264036.6/ ENSP00000264036.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..646
                     /product="cell surface glycoprotein MUC18 precursor"
                     /note="Gicerin; melanoma adhesion molecule; cell surface
                     glycoprotein MUC18; cell surface glycoprotein P1H12;
                     melanoma-associated antigen A32; melanoma-associated
                     antigen MUC18; S-endo 1 endothelial-associated antigen"
                     /calculated_mol_wt=69258
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2368
     mat_peptide     24..646
                     /product="Cell surface glycoprotein MUC18.
                     /id=PRO_0000014891"
                     /note="propagated from UniProtKB/Swiss-Prot (P43121.2)"
                     /calculated_mol_wt=69258
     Region          35..132
                     /region_name="CD19_double_Ig"
                     /note="CD19 (Cluster of Differentiation 19), a unique
                     double immunoglobulin (Ig)-fold domain; cl49627"
                     /db_xref="CDD:483967"
     Region          35..86
                     /region_name="protodomain 1+3"
                     /note="protodomain 1+3 [structural motif]"
                     /db_xref="CDD:467824"
     Region          35..39
                     /region_name="strand A'"
                     /note="strand A' [structural motif]"
                     /db_xref="CDD:467824"
     Region          41..48
                     /region_name="strand B"
                     /note="strand B [structural motif]"
                     /db_xref="CDD:467824"
     Site            order(43,45,47,86,100,102,104,109,128)
                     /site_type="other"
                     /note="CD81 binding site [polypeptide binding]"
                     /db_xref="CDD:467824"
     Region          49..58
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:467824"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     Region          58..65
                     /region_name="strand C"
                     /note="strand C [structural motif]"
                     /db_xref="CDD:467824"
     Site            order(65,115)
                     /site_type="other"
                     /note="antibody binding site [polypeptide binding]"
                     /db_xref="CDD:467824"
     Region          72..85
                     /region_name="strand C'"
                     /note="strand C' [structural motif]"
                     /db_xref="CDD:467824"
     Region          86..89
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:467824"
     Region          89..132
                     /region_name="protodomain 2+4"
                     /note="protodomain 2+4 [structural motif]"
                     /db_xref="CDD:467824"
     Region          89..93
                     /region_name="strand D"
                     /note="strand D [structural motif]"
                     /db_xref="CDD:467824"
     Region          99..104
                     /region_name="strand E"
                     /note="strand E [structural motif]"
                     /db_xref="CDD:467824"
     Region          110..119
                     /region_name="strand F"
                     /note="strand F [structural motif]"
                     /db_xref="CDD:467824"
     Region          119..127
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:467824"
     Region          127..132
                     /region_name="strand G"
                     /note="strand G [structural motif]"
                     /db_xref="CDD:467824"
     Region          139..234
                     /region_name="C2-set_2"
                     /note="CD80-like C2-set immunoglobulin domain; pfam08205"
                     /db_xref="CDD:400489"
     Region          171..175
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          192..196
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          261..321
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          278..299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43121.2)"
     Region          346..410
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            418
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     Region          443..510
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          446..452
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     Region          461..465
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            467
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     Region          496..501
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            508
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     Site            518
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     Region          525..554
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43121.2)"
     Site            527
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     Site            544
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     Site            560..583
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43121.2)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R2Y2; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     Region          620..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43121.2)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P43121.2)"
     CDS             1..646
                     /gene="MCAM"
                     /gene_synonym="CD146; HEMCAM; MelCAM; METCAM; MUC18"
                     /coded_by="NM_006500.3:30..1970"
                     /db_xref="CCDS:CCDS31690.1"
                     /db_xref="GeneID:4162"
                     /db_xref="HGNC:HGNC:6934"
                     /db_xref="MIM:155735"
ORIGIN      
        1 mglprlvcaf llaaccccpr vagvpgeaeq papelvevev gstallkcgl sqsqgnlshv
       61 dwfsvhkekr tlifrvrqgq gqsepgeyeq rlslqdrgat laltqvtpqd eriflcqgkr
      121 prsqeyriql rvykapeepn iqvnplgipv nskepeevat cvgrngypip qviwykngrp
      181 lkeeknrvhi qssqtvessg lytlqsilka qlvkedkdaq fycelnyrlp sgnhmkesre
      241 vtvpvfypte kvwlevepvg mlkegdrvei rcladgnppp hfsiskqnps treaeeettn
      301 dngvlvlepa rkehsgryec qgldldtmis llsepqellv nyvsdvrvsp aaperqegss
      361 ltltceaess qdlefqwlre etgqvlergp vlqlhdlkre agggyrcvas vpsipglnrt
      421 qlvnvaifgp pwmafkerkv wvkenmvlnl sceasghprp tiswnvngta seqdqdpqrv
      481 lstlnvlvtp elletgvect asndlgknts ilflelvnlt tltpdsnttt glststasph
      541 transtster klpepesrgv vivavivcil vlavlgavly flykkgklpc rrsgkqeitl
      601 ppsrkselvv evksdklpee mgllqgssgd krapgdqgek yidlrh
//
LOCUS       NP_001350287             813 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 3B
            isoform 2 [Mus musculus].
ACCESSION   NP_001350287
VERSION     NP_001350287.1
DBSOURCE    REFSEQ: accession NM_001363358.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Chang,W.H., Choi,S.H., Moon,B.S., Cai,M., Lyu,J., Bai,J., Gao,F.,
            Hajjali,I., Zhao,Z., Campbell,D.B., Weiner,L.P. and Lu,W.
  TITLE     Smek1/2 is a nuclear chaperone and cofactor for cleaved Wnt
            receptor Ryk, regulating cortical neurogenesis
  JOURNAL   Proc Natl Acad Sci U S A 114 (50), E10717-E10725 (2017)
   PUBMED   29180410
  REMARK    GeneRIF: Smek1 and Smek2 (Smek1/2) are key factors in the Ryk
            signaling pathway
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Moon,B.S., Yun,H.M., Chang,W.H., Steele,B.H., Cai,M., Choi,S.H. and
            Lu,W.
  TITLE     Smek promotes corticogenesis through regulating Mbd3's stability
            and Mbd3/NuRD complex recruitment to genes associated with
            neurogenesis
  JOURNAL   PLoS Biol 15 (5), e2001220 (2017)
   PUBMED   28467410
  REMARK    GeneRIF: Smek/Mbd3 interaction regulates neuronal gene expression
            and neuronal differentiation during cortical development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 813)
  AUTHORS   Lee,D.H., Acharya,S.S., Kwon,M., Drane,P., Guan,Y., Adelmant,G.,
            Kalev,P., Shah,J., Pellman,D., Marto,J.A. and Chowdhury,D.
  TITLE     Dephosphorylation enables the recruitment of 53BP1 to double-strand
            DNA breaks
  JOURNAL   Mol Cell 54 (3), 512-525 (2014)
   PUBMED   24703952
REFERENCE   5  (residues 1 to 813)
  AUTHORS   Krol,A.J., Roellig,D., Dequeant,M.L., Tassy,O., Glynn,E.,
            Hattem,G., Mushegian,A., Oates,A.C. and Pourquie,O.
  TITLE     Evolutionary plasticity of segmentation clock networks
  JOURNAL   Development 138 (13), 2783-2792 (2011)
   PUBMED   21652651
REFERENCE   6  (residues 1 to 813)
  AUTHORS   Lyu,J., Jho,E.H. and Lu,W.
  TITLE     Smek promotes histone deacetylation to suppress transcription of
            Wnt target gene brachyury in pluripotent embryonic stem cells
  JOURNAL   Cell Res 21 (6), 911-921 (2011)
   PUBMED   21423269
  REMARK    GeneRIF: the Smek-containing protein phosphatase 4 complex
            represses transcription of Wnt-responsive development-related genes
            through histone deacetylation, and that this complex is essential
            for embryonic stem cell pluripotency maintenance
REFERENCE   7  (residues 1 to 813)
  AUTHORS   Thiagarajan,R.D., Georgas,K.M., Rumballe,B.A., Lesieur,E.,
            Chiu,H.S., Taylor,D., Tang,D.T., Grimmond,S.M. and Little,M.H.
  TITLE     Identification of anchor genes during kidney development defines
            ontological relationships, molecular subcompartments and regulatory
            pathways
  JOURNAL   PLoS One 6 (2), e17286 (2011)
   PUBMED   21386911
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 813)
  AUTHORS   Yoon,Y.S., Lee,M.W., Ryu,D., Kim,J.H., Ma,H., Seo,W.Y., Kim,Y.N.,
            Kim,S.S., Lee,C.H., Hunter,T., Choi,C.S., Montminy,M.R. and
            Koo,S.H.
  TITLE     Suppressor of MEK null (SMEK)/protein phosphatase 4 catalytic
            subunit (PP4C) is a key regulator of hepatic gluconeogenesis
  JOURNAL   Proc Natl Acad Sci U S A 107 (41), 17704-17709 (2010)
   PUBMED   20876121
REFERENCE   9  (residues 1 to 813)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
REFERENCE   10 (residues 1 to 813)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX000351.17 and BX294116.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660817.39015.1,
                                           SRR7345562.1889020.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 16.46 cM"
     Protein         1..813
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 3B isoform 2"
                     /note="serine/threonine-protein phosphatase 4 regulatory
                     subunit 3B; SMEK homolog 2, suppressor of mek1"
                     /calculated_mol_wt=93051
     Region          7..>65
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q922R5.2)"
     Region          168..359
                     /region_name="PP4R3"
                     /note="Phosphatase 4 regulatory subunit 3; pfam04802"
                     /db_xref="CDD:461435"
     Region          680..813
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q922R5.2)"
     Site            804
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5MIZ7; propagated from
                     UniProtKB/Swiss-Prot (Q922R5.2)"
     CDS             1..813
                     /gene="Ppp4r3b"
                     /gene_synonym="mKIAA1387; Smek2"
                     /coded_by="NM_001363358.1:331..2772"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:104570"
                     /db_xref="MGI:MGI:2144474"
ORIGIN      
        1 msdtrrrvkv ytlnedrqwd drgtghvsst yveelkgmsl lvraesdgsl lleskinpnt
       61 ayqkqqdtli vwseaenydl alsfqekagc deiwekicqv qgkdpsvevt qdlideseee
      121 rfeempetsh lidlpacels kleeiadlvt svlsspirre klalaleneg yikkllqlfq
      181 acenlenteg lhhlyeiirg ilflnkatlf evmfsdecim dvvgcleydp alaqpkrhre
      241 fltktakfke vipitdselr qkihqtyrvq yiqdiilptp svfeenflst ltsfiffnkv
      301 eivsmlqede kflsevfaql tdeatdddkr relvnffkef cafsqtlqpq nrdaffktla
      361 klgilpalei vmgmddlqvr saatdifsyl vefspsmvre fvmqeaqqsd ddvllinvvi
      421 eqmicdtdpe lggavqlmgl lrtlidpenm lattnkteks eflnffynhc mhvltapllt
      481 ntsedkcekd nmlgsnttnt icpdnyqtaq llalilellt fcvehhtyhi knyimnkdll
      541 rrvlvlmnsk htflalcalr fmrriiglkd efynryitkg nlfepvinal ldngtrynll
      601 nsavielfef irvedikslt ahivenfyka lesieyvqtf kglktkyeqe kdrqnqklns
      661 nrfrrdakal eedeemwfne dddeegkavi tpvekskted dfpdsyekfm etkkakesed
      721 kenlpkrass ggfkftfshs psatngtnst nsksvvsqtt passnvassk ttslatsvta
      781 tkgnlvglvd ypddeeedee eessprkrpr lgs
//
LOCUS       NP_001035362            1762 aa            linear   PRI 27-APR-2025
DEFINITION  ADAMTS-like protein 1 isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001035362
VERSION     NP_001035362.3
DBSOURCE    REFSEQ: accession NM_001040272.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1762)
  AUTHORS   Kantaputra,P.N., Pruksametanan,A., Phondee,N., Hutsadaloi,A.,
            Intachai,W., Kawasaki,K., Ohazama,A., Ngamphiw,C., Tongsima,S.,
            Ketudat Cairns,J.R. and Tripuwabhrut,P.
  TITLE     ADAMTSL1 and mandibular prognathism
  JOURNAL   Clin Genet 95 (4), 507-515 (2019)
   PUBMED   30714143
  REMARK    GeneRIF: This explains why the patients with ADAMTSL1 mutations had
            abnormal mandibles but normal long bones. This is the first report
            that mutations in ADAMTSL1 are responsible for the pathogenesis of
            mandibular prognathism.
REFERENCE   2  (residues 1 to 1762)
  AUTHORS   Kadalayil,L., Khan,S., Nevanlinna,H., Fasching,P.A., Couch,F.J.,
            Hopper,J.L., Liu,J., Maishman,T., Durcan,L., Gerty,S.,
            Blomqvist,C., Rack,B., Janni,W., Collins,A., Eccles,D. and
            Tapper,W.
  TITLE     Germline variation in ADAMTSL1 is associated with prognosis
            following breast cancer treatment in young women
  JOURNAL   Nat Commun 8 (1), 1632 (2017)
   PUBMED   29158497
  REMARK    GeneRIF: ADAMTSL1 are associated with breast cancer prognosis and
            may involve an interaction with AREG expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1762)
  AUTHORS   Hendee,K., Wang,L.W., Reis,L.M., Rice,G.M., Apte,S.S. and
            Semina,E.V.
  TITLE     Identification and functional analysis of an ADAMTSL1 variant
            associated with a complex phenotype including congenital glaucoma,
            craniofacial, and other systemic features in a three-generation
            human pedigree
  JOURNAL   Hum Mutat 38 (11), 1485-1490 (2017)
   PUBMED   28722276
  REMARK    GeneRIF: These data imply a multisystem role for ADAMTSL1 and
            present the first disease-associated variant affecting a
            C-mannosylation motif.
REFERENCE   4  (residues 1 to 1762)
  AUTHORS   Singh,A., Babyak,M.A., Nolan,D.K., Brummett,B.H., Jiang,R.,
            Siegler,I.C., Kraus,W.E., Shah,S.H., Williams,R.B. and Hauser,E.R.
  TITLE     Gene by stress genome-wide interaction analysis and path analysis
            identify EBF1 as a cardiovascular and metabolic risk gene
  JOURNAL   Eur J Hum Genet 23 (6), 854-862 (2015)
   PUBMED   25271088
REFERENCE   5  (residues 1 to 1762)
  AUTHORS   Xie,T., Deng,L., Mei,P., Zhou,Y., Wang,B., Zhang,J., Lin,J.,
            Wei,Y., Zhang,X. and Xu,R.
  TITLE     Genome-wide association study combining pathway analysis for
            typical sporadic amyotrophic lateral sclerosis in Chinese Han
            populations
  JOURNAL   Neurobiol Aging 35 (7), 1778 (2014)
   PUBMED   24529757
REFERENCE   6  (residues 1 to 1762)
  AUTHORS   Wang,L.W., Leonhard-Melief,C., Haltiwanger,R.S. and Apte,S.S.
  TITLE     Post-translational modification of thrombospondin type-1 repeats in
            ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan
  JOURNAL   J Biol Chem 284 (44), 30004-30015 (2009)
   PUBMED   19671700
  REMARK    GeneRIF: thrombospondin type-1 repeats from punctin-1 carries
            C-mannosylation in close proximity to O-linked fucose
REFERENCE   7  (residues 1 to 1762)
  AUTHORS   Wang,L.W., Dlugosz,M., Somerville,R.P., Raed,M., Haltiwanger,R.S.
            and Apte,S.S.
  TITLE     O-fucosylation of thrombospondin type 1 repeats in
            ADAMTS-like-1/punctin-1 regulates secretion: implications for the
            ADAMTS superfamily
  JOURNAL   J Biol Chem 282 (23), 17024-17031 (2007)
   PUBMED   17395588
  REMARK    GeneRIF: data define a critical role for N-glycosylation and
            O-fucosylation in the biosynthesis of punctin-1
REFERENCE   8  (residues 1 to 1762)
  AUTHORS   Fu,G.K., Wang,J.T., Yang,J., Au-Young,J. and Stuve,L.L.
  TITLE     Circular rapid amplification of cDNA ends for high-throughput
            extension cloning of partial genes
  JOURNAL   Genomics 84 (1), 205-210 (2004)
   PUBMED   15203218
REFERENCE   9  (residues 1 to 1762)
  AUTHORS   Hall,N.G., Klenotic,P., Anand-Apte,B. and Apte,S.S.
  TITLE     ADAMTSL-3/punctin-2, a novel glycoprotein in extracellular matrix
            related to the ADAMTS family of metalloproteases
  JOURNAL   Matrix Biol 22 (6), 501-510 (2003)
   PUBMED   14667842
REFERENCE   10 (residues 1 to 1762)
  AUTHORS   Hirohata,S., Wang,L.W., Miyagi,M., Yan,L., Seldin,M.F., Keene,D.R.,
            Crabb,J.W. and Apte,S.S.
  TITLE     Punctin, a novel ADAMTS-like molecule, ADAMTSL-1, in extracellular
            matrix
  JOURNAL   J Biol Chem 277 (14), 12182-12189 (2002)
   PUBMED   11805097
  REMARK    GeneRIF: Punctin, a novel ADAMTS-like molecule, ADAMTSL-1, in
            extracellular matrix
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA598045.1, CX758410.1, AF251058.1, DA549329.1, AL591423.7,
            AI750970.1, BX640951.1, BC100790.2, AL158150.14 and BU626040.1.
            
            On Jul 31, 2007 this sequence version replaced NP_001035362.2.
            
            Summary: This gene encodes a secreted protein and member of the
            ADAMTS (a disintegrin and metalloproteinase with thrombospondin
            motif) family. This protein lacks the metalloproteinase and
            disintegrin-like domains, which are typical of the ADAMTS family,
            but contains other ADAMTS domains, including the thrombospondin
            type 1 motif. This protein may have important functions in the
            extracellular matrix. Alternative splicing results in multiple
            transcript variants encoding distinct proteins. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) encodes the longer isoform
            (4).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968189,
                              SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380548.9/ ENSP00000369921.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1762
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p22.2-p22.1"
     Protein         1..1762
                     /product="ADAMTS-like protein 1 isoform 4 precursor"
                     /note="ADAM-TS related protein 1; ADAMTS-like protein 1;
                     punctin-1"
                     /calculated_mol_wt=190301
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3128
     mat_peptide     29..1762
                     /product="ADAMTS-like protein 1. /id=PRO_0000035860"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6G6.4)"
                     /calculated_mol_wt=190301
     Region          36..82
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            36
                     /site_type="other"
                     /note="Not glycosylated.
                     /evidence=ECO:0000269|PubMed:19671700; propagated from
                     UniProtKB/Swiss-Prot (Q8N6G6.4)"
     Site            39
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan.
                     /evidence=ECO:0000269|PubMed:19671700; propagated from
                     UniProtKB/Swiss-Prot (Q8N6G6.4)"
     Site            42
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan.
                     /evidence=ECO:0000269|PubMed:19671700; propagated from
                     UniProtKB/Swiss-Prot (Q8N6G6.4)"
     Site            48
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000269|PubMed:19671700; propagated from
                     UniProtKB/Swiss-Prot (Q8N6G6.4)"
     Region          87..185
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Region          204..296
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17395588; propagated from
                     UniProtKB/Swiss-Prot (Q8N6G6.4)"
     Region          301..359
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            312
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000269|PubMed:17395588; propagated from
                     UniProtKB/Swiss-Prot (Q8N6G6.4)"
     Region          380..437
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            391
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) serine.
                     /evidence=ECO:0000269|PubMed:17395588; propagated from
                     UniProtKB/Swiss-Prot (Q8N6G6.4)"
     Region          440..492
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            451
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000269|PubMed:17395588; propagated from
                     UniProtKB/Swiss-Prot (Q8N6G6.4)"
     Region          531..583
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          611..666
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          670..728
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          732..788
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          792..849
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          895..949
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          895..899
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          908..912
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          930..934
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          944..949
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1120..1164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6G6.4)"
     Region          1187..1266
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1198..1202
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409570"
     Region          1211..1215
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409570"
     Region          1233..1237
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409570"
     Region          1247..1252
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409570"
     Region          1260..1263
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409570"
     Region          1279..1368
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1304..1308
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409570"
     Region          1317..1321
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409570"
     Region          1336..1340
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409570"
     Region          1350..1355
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409570"
     Region          1363..1366
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409570"
     Region          1409..1488
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1414..1418
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1427..1431
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1452..1456
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1466..1471
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1481..1484
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1549..1607
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1610..1666
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1670..1725
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1730..1759
                     /region_name="PLAC"
                     /note="PLAC (protease and lacunin) domain; pfam08686"
                     /db_xref="CDD:462560"
     CDS             1..1762
                     /gene="ADAMTSL1"
                     /gene_synonym="ADAMTSL-1; ADAMTSR1; C9orf94; PUNCTIN"
                     /coded_by="NM_001040272.6:81..5369"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS47954.1"
                     /db_xref="GeneID:92949"
                     /db_xref="HGNC:HGNC:14632"
                     /db_xref="MIM:609198"
ORIGIN      
        1 meccrratpg tlllflafll lssrtarsee drdglwdawg pwsecsrtcg ggasyslrrc
       61 lsskscegrn iryrtcsnvd cppeagdfra qqcsahndvk hhgqfyewlp vsndpdnpcs
      121 lkcqakgttl vvelapkvld gtrcytesld mcisglcqiv gcdhqlgstv kedncgvcng
      181 dgstcrlvrg qyksqlsatk sddtvvaipy gsrhirlvlk gpdhlyletk tlqgtkgens
      241 lsstgtflvd nssvdfqkfp dkeilrmagp ltadfivkir nsgsadstvq fifyqpiihr
      301 wretdffpcs atcgggyqlt saecydlrsn rvvadqychy ypenikpkpk lqecnldpcp
      361 asdgykqimp ydlyhplprw eatpwtacss scgggiqsra vscveediqg hvtsveewkc
      421 mytpkmpiaq pcnifdcpkw laqewspctv tcgqglryrv vlcidhrgmh tggcspktkp
      481 hikeecivpt pcykpkeklp veaklpwfkq aqeleegaav seepsfipea wsactvtcgv
      541 gtqvrivrcq vllsfsqsva dlpidecegp kpasqracya gpcsgeipef npdetdglfg
      601 glqdfdelyd weyegftkcs escgggvqea vvsclnkqtr epaeenlcvt srrppqllks
      661 cnldpcparw eigkwspcsl tcgvglqtrd vfcshllsre mnetvilade lcrqpkpstv
      721 qacnrfncpp awypaqwqpc srtcgggvqk revlckqrma dgsflelpet fcsaskpacq
      781 qackkddcps ewllsdwtec stscgegtqt rsaicrkmlk tglstvvnst lcpplpfsss
      841 irpcmlatca rpgrpstkhs phiaaarkvy iqtrrqrklh fvvggfayll pktavvlrcp
      901 arrvrkplit wekdgqhlis sthvtvapfg ylkihrlkps dagvytcsag parehfvikl
      961 iggnrklvar plsprseeev lagrkggpke alqthkhqng ifsngskaek rglaanpgsr
     1021 yddlvsrlle qggwpgella sweaqdsaer nttseedpga eqvllhlpft mvteqrrldd
     1081 ilgnlsqqpe elrdlyskhl vaqlaqeifr shlehqdtll kpserrtspv tlsphkhvsg
     1141 fssslrtsst gdagggsrrp hrkptilrki saaqqlsase vvthlgqtva lasgtlsvll
     1201 hceaighprp tiswarngee vqfsdrillq pddslqilap veadvgfytc natnalgyds
     1261 vsiavtlagk plvktsrmtv intekpavtv digstiktvq gvnvtincqv agvpeaevtw
     1321 frnksklgsp hhlhegslll tnvsssdqgl yscraanlhg eltestqlli ldppqvptql
     1381 edirallaat gpnlpsvlts plgtqlvldp gnsallgcpi kghpvpnitw fhggqpivta
     1441 tglthhilaa gqilqvanls ggsqgefscl aqneagvlmq kaslviqdyw wsvdrlatcs
     1501 ascgnrgvqq prlrcllnst evnpahcagk vrpavqpiac nrrdcpsrwm vtswsactrs
     1561 cgggvqtrrv tcqklkasgi stpvsndmct qvakrpvdtq acnqqlcvew afsswgqcng
     1621 pcigphlavq hrqvfcqtrd gitlpseqcs alprpvstqn cwseacsvhw rvslwtlcta
     1681 tcgnygfqsr rvecvhartn kavpehlcsw gprpanwqrc nitpcenmec rdttrycekv
     1741 kqlklcqlsq fksrccgtcg ka
//
LOCUS       NP_000032                317 aa            linear   PRI 27-APR-2025
DEFINITION  apolipoprotein E isoform b precursor [Homo sapiens].
ACCESSION   NP_000032
VERSION     NP_000032.1
DBSOURCE    REFSEQ: accession NM_000041.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Chen,L., He,X., Mao,L. and Liu,P.
  TITLE     APOE contributes to longitudinal impulse control disorders
            progression in Parkinson's disease
  JOURNAL   BMC Psychiatry 24 (1), 632 (2024)
   PUBMED   39334114
  REMARK    GeneRIF: APOE contributes to longitudinal impulse control disorders
            progression in Parkinson's disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Toral-Rios,D., Pichardo-Rojas,P., Ruiz-Sanchez,E.,
            Rosas-Carrasco,O., Carvajal-Garcia,R., Galvez-Coutino,D.C.,
            Martinez-Rodriguez,N.L., Rubio-Chavez,A.D., Alcantara-Flores,M.,
            Lopez-Ramirez,A., Martinez-Rosas,A.R., Ruiz-Chow,A.A.,
            Alonso-Vanegas,M. and Campos-Pena,V.
  TITLE     Synergistic Effect between the APOE epsilon4 Allele with Genetic
            Variants of GSK3B and MAPT: Differential Profile between Refractory
            Epilepsy and Alzheimer Disease
  JOURNAL   Int J Mol Sci 25 (18), 10228 (2024)
   PUBMED   39337715
  REMARK    GeneRIF: Synergistic Effect between the APOE epsilon4 Allele with
            Genetic Variants of GSK3B and MAPT: Differential Profile between
            Refractory Epilepsy and Alzheimer Disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Han,J.S., Yoo,S.G., Lee,S.J., Lee,H.J., Choi,I.Y. and Park,K.H.
  TITLE     The biphasic impact of apolipoprotein E epsilon4 allele on
            age-related hearing loss
  JOURNAL   Sci Rep 14 (1), 21420 (2024)
   PUBMED   39271694
  REMARK    GeneRIF: The biphasic impact of apolipoprotein E epsilon4 allele on
            age-related hearing loss.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Wei,G., Li,B., Wang,H., Chen,L., Chen,W., Chen,K., Wang,W.,
            Wang,S., Zeng,H., Liu,Y., Zeng,Y. and Rao,H.
  TITLE     Apolipoprotein E E3/E4 genotype is associated with an increased
            risk of coronary atherosclerosis in patients with hypertension
  JOURNAL   BMC Cardiovasc Disord 24 (1), 486 (2024)
   PUBMED   39261765
  REMARK    GeneRIF: Apolipoprotein E E3/E4 genotype is associated with an
            increased risk of coronary atherosclerosis in patients with
            hypertension.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Greyshock,N., Guyton,J.R., Sebastian,S. and Okorodudu,D.
  TITLE     APOE p.Leu167del-Related Lipid Disorders - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24921113
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Bird,T.D.
  TITLE     Alzheimer Disease Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301340
REFERENCE   7  (residues 1 to 317)
  AUTHORS   McLean,J.W., Elshourbagy,N.A., Chang,D.J., Mahley,R.W. and
            Taylor,J.M.
  TITLE     Human apolipoprotein E mRNA. cDNA cloning and nucleotide sequencing
            of a new variant
  JOURNAL   J Biol Chem 259 (10), 6498-6504 (1984)
   PUBMED   6327682
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Utermann,G., Pruin,N. and Steinmetz,A.
  TITLE     Polymorphism of apolipoprotein E. III. Effect of a single
            polymorphic gene locus on plasma lipid levels in man
  JOURNAL   Clin Genet 15 (1), 63-72 (1979)
   PUBMED   759055
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Innerarity,T.L., Mahley,R.W., Weisgraber,K.H. and Bersot,T.P.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. II.
            Receptor binding activity of a high density lipoprotein subfraction
            modulated by the apo(E--A-II) complex
  JOURNAL   J Biol Chem 253 (17), 6289-6295 (1978)
   PUBMED   210175
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Weisgraber,K.H. and Mahley,R.W.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. I.
            Characterization of this mixed disulfide and its identification in
            a high density lipoprotein subfraction
  JOURNAL   J Biol Chem 253 (17), 6281-6288 (1978)
   PUBMED   210174
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY056112.1 and BC003557.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a major apoprotein of
            the chylomicron. It binds to a specific liver and peripheral cell
            receptor, and is essential for the normal catabolism of
            triglyceride-rich lipoprotein constituents. This gene maps to
            chromosome 19 in a cluster with the related apolipoprotein C1 and
            C2 genes. Mutations in this gene result in familial
            dysbetalipoproteinemia, or type III hyperlipoproteinemia (HLP III),
            in which increased plasma cholesterol and triglycerides are the
            consequence of impaired clearance of chylomicron and VLDL remnants.
            [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (2) contains an alternate 5'
            terminal exon, and it thus differs in the 5' UTR and initiates
            translation at a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (b) is shorter at the N-terminus,
            compared to isoform a. Variants 2, 3, 4 and 5 all encode isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.95821.1, M12529.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252486.9/ ENSP00000252486.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..317
                     /product="apolipoprotein E isoform b precursor"
                     /note="apolipoprotein E3"
                     /calculated_mol_wt=34237
     sig_peptide     1..18
                     /note="/evidence=ECO:0000269|PubMed:7068630; propagated
                     from UniProtKB/Swiss-Prot (P02649.1)"
                     /calculated_mol_wt=1935
     mat_peptide     19..317
                     /product="Apolipoprotein E. /id=PRO_0000001987"
                     /note="propagated from UniProtKB/Swiss-Prot (P02649.1)"
                     /calculated_mol_wt=34237
     Site            26
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:23234360; propagated from
                     UniProtKB/Swiss-Prot (P02649.1)"
     Site            36
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:23234360; propagated from
                     UniProtKB/Swiss-Prot (P02649.1)"
     Region          80..255
                     /region_name="8 X 22 AA approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P02649.1)"
     Region          81..266
                     /region_name="Apolipoprotein"
                     /note="Apolipoprotein A1/A4/E domain; pfam01442"
                     /db_xref="CDD:460211"
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (Glc) (glycation) lysine.
                     /evidence=ECO:0000269|PubMed:10452964; propagated from
                     UniProtKB/Swiss-Prot (P02649.1)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02649.1)"
     Region          158..168
                     /region_name="LDL and other lipoprotein receptors binding.
                     /evidence=ECO:0000269|PubMed:20030366,
                     ECO:0000269|PubMed:2063194"
                     /note="propagated from UniProtKB/Swiss-Prot (P02649.1)"
     Region          210..290
                     /region_name="Lipid-binding and lipoprotein association.
                     /evidence=ECO:0000269|PubMed:2280190,
                     ECO:0000269|PubMed:8071364"
                     /note="propagated from UniProtKB/Swiss-Prot (P02649.1)"
     Site            212
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19838169,
                     ECO:0000269|PubMed:2498325; propagated from
                     UniProtKB/Swiss-Prot (P02649.1)"
     Region          266..317
                     /region_name="Homooligomerization.
                     /evidence=ECO:0000269|PubMed:8340399"
                     /note="propagated from UniProtKB/Swiss-Prot (P02649.1)"
     Region          278..290
                     /region_name="Specificity for association with VLDL.
                     /evidence=ECO:0000269|PubMed:8071364"
                     /note="propagated from UniProtKB/Swiss-Prot (P02649.1)"
     Site            307
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19838169; propagated from
                     UniProtKB/Swiss-Prot (P02649.1)"
     Site            308
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:19838169,
                     ECO:0000269|PubMed:20511397; propagated from
                     UniProtKB/Swiss-Prot (P02649.1)"
     Site            314
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:23234360; propagated from
                     UniProtKB/Swiss-Prot (P02649.1)"
     CDS             1..317
                     /gene="APOE"
                     /gene_synonym="AD2; APO-E; ApoE4; LDLCQ5; LPG"
                     /coded_by="NM_000041.4:70..1023"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS12647.1"
                     /db_xref="GeneID:348"
                     /db_xref="HGNC:HGNC:613"
                     /db_xref="MIM:107741"
ORIGIN      
        1 mkvlwaallv tflagcqakv eqavetepep elrqqtewqs gqrwelalgr fwdylrwvqt
       61 lseqvqeell ssqvtqelra lmdetmkelk aykseleeql tpvaeetrar lskelqaaqa
      121 rlgadmedvc grlvqyrgev qamlgqstee lrvrlashlr klrkrllrda ddlqkrlavy
      181 qagaregaer glsairerlg plveqgrvra atvgslagqp lqeraqawge rlrarmeemg
      241 srtrdrldev keqvaevrak leeqaqqirl qaeafqarlk swfeplvedm qrqwaglvek
      301 vqaavgtsaa pvpsdnh
//
LOCUS       NP_001032895            1334 aa            linear   PRI 27-APR-2025
DEFINITION  nck-associated protein 5-like [Homo sapiens].
ACCESSION   NP_001032895 NP_065992 XP_374976
VERSION     NP_001032895.2
DBSOURCE    REFSEQ: accession NM_001037806.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1334)
  AUTHORS   Shintomi,M., Shiratori,M., Negishi,L. and Terada,Y.
  TITLE     Identification of Cep169-interacting proteins and the in vivo
            modification sites of Cep169 via proteomic analysis
  JOURNAL   Biochem Biophys Res Commun 495 (3), 2275-2281 (2018)
   PUBMED   29269292
  REMARK    GeneRIF: Our findings suggest that Cep169 regulates cell growth by
            interacting with multiple proteins.
REFERENCE   2  (residues 1 to 1334)
  AUTHORS   Mori,Y., Inoue,Y., Taniyama,Y., Tanaka,S. and Terada,Y.
  TITLE     Phosphorylation of the centrosomal protein, Cep169, by Cdk1
            promotes its dissociation from centrosomes in mitosis
  JOURNAL   Biochem Biophys Res Commun 468 (4), 642-646 (2015)
   PUBMED   26549230
  REMARK    GeneRIF: These data suggest that the dissociation of Cep169 from
            centrosomes is controlled by Cdk1/Cyclin B during mitosis, and that
            Cep169 might regulate MT dynamics of mitotic spindle.
REFERENCE   3  (residues 1 to 1334)
  AUTHORS   Mori,Y., Inoue,Y., Tanaka,S., Doda,S., Yamanaka,S., Fukuchi,H. and
            Terada,Y.
  TITLE     Cep169, a Novel Microtubule Plus-End-Tracking Centrosomal Protein,
            Binds to CDK5RAP2 and Regulates Microtubule Stability
  JOURNAL   PLoS One 10 (10), e0140968 (2015)
   PUBMED   26485573
  REMARK    GeneRIF: These results show that Cep169 targets microtubule tips
            and regulates stability of microtubules with CDK5RAP2.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN359946.1, CN359941.1, AC131157.4, BC033253.1, BX327000.2 and
            BU617503.1.
            
            On or before Oct 2, 2008 this sequence version replaced
            NP_065992.1, NP_001032895.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by same species and orthologous transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335999.7/ ENSP00000337998.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..1334
                     /product="nck-associated protein 5-like"
                     /note="NCKAP5-like; centrosomal protein of 169 kDa"
                     /calculated_mol_wt=139331
     Region          1..139
                     /region_name="Mediates interaction with CDK5RAP2 and is
                     required for homodimerization and microtubule bundle
                     formation. /evidence=ECO:0000269|PubMed:26482847,
                     ECO:0000269|PubMed:26485573"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          115..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          210..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          <214..663
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          266..316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          349..711
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          484..487
                     /region_name="(S/T)X(I/L)P motif 1.
                     /evidence=ECO:0000269|PubMed:26482847,
                     ECO:0000269|PubMed:26485573"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            577
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          750..1146
                     /region_name="Mediates interaction with beta-tubulin and
                     is required for microtubule bundle formation.
                     /evidence=ECO:0000269|PubMed:26482847"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:26549230,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          782..884
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          816..819
                     /region_name="(S/T)X(I/L)P motif 2.
                     /evidence=ECO:0000269|PubMed:26482847,
                     ECO:0000269|PubMed:26485573"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          879..1181
                     /region_name="NCKAP5"
                     /note="Nck-associated protein 5, Peripheral clock protein;
                     pfam15246"
                     /db_xref="CDD:464586"
     Region          926..929
                     /region_name="(S/T)X(I/L)P motif 3, required for
                     interaction with MAPRE1.
                     /evidence=ECO:0000269|PubMed:26482847,
                     ECO:0000269|PubMed:26485573"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          931..953
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          986..1015
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          1030..1183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Site            1194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH0.4)"
     Region          1197..1334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH0.4)"
     CDS             1..1334
                     /gene="NCKAP5L"
                     /gene_synonym="Cep169; FP1193; KIAA1602"
                     /coded_by="NM_001037806.4:191..4195"
                     /db_xref="CCDS:CCDS41781.2"
                     /db_xref="GeneID:57701"
                     /db_xref="HGNC:HGNC:29321"
                     /db_xref="MIM:615104"
ORIGIN      
        1 mseamdqpag gpgnprpgeg ddgsmepgtc qellhrlrel eaensalaqa nenqretyer
       61 cldevanhvv qallnqkdlr eeciklkkrv fdlerqnqml salfqqklql ttgslpqipl
      121 tplqppsepp aspslssteg paaplplghc agqrevcweq qlrpggpgpp aapppaldal
      181 spflrkkaqi levlraleet dplllcspat pwrppgqgpg spepingelc gppqpepspw
      241 apclllgpgn lggllhwerl lgglggeedt grpwgpsrgp pqaqgtssgp ncapgsssss
      301 ssdeagdpne apspdtllga larrqlnlgq lledtesylq aflagaagpl ngdhpgpgqs
      361 sspdqappql skskglpksa wgggtpeahr pgfgatsegq gplpflsmfm gagdaplgsr
      421 pghphsssqv ksklqigpps pgeaqgpllp sparglkflk lpptseksps pggpqlspql
      481 prnsripcrn sgsdgspspl larrglggge lspegaqglp tspspcyttp dstqlrppqs
      541 alsttlspgp vvspcyenil dlsrstfrgp spepppsplq vptypqltle vpqapevlrs
      601 pgvppspclp esypygspqe ksldkagses phpgrrtpgn sskkpsqgsg rrpgdpgstp
      661 lrdrlaalgk lktgpegalg sekngvparp gtektrgpgk sgesagdmvp sihrpleqle
      721 akggirgava lgtnslkqqe pglmgdpgar vysshsmgar vdlepvsprs cltkvelaks
      781 rlagalcpqv prtpakvpts apslgkpnks phssptklps ksptkvvprp gaplvtkesp
      841 kpdkgkgppw adcgsttaqs tplvpgptdp sqgpeglaph saieekvmkg ieenvlrlqg
      901 qerapgaevk hrntssiasw fglkksklpa lnrrteatkn kegagggspl rrevkmeark
      961 leaeslnisk lmakaedlrr aleeekayls srarprpggp apgpntglgq vqgqlagmyq
     1021 gadtfmqqll nrvdgkelps kswrepkpey gdfqpvssdp kspwpacgpr nglvgplqgc
     1081 gkppgkpsse pgrreempse dslaepvpts hftacgsltr tldsgigtfp ppdhgssgtp
     1141 sknlpktkpp rldpppgvpp arpppltkvp rrahtlerev pgieellvsg rhpsmpafpa
     1201 llpaapghrg hetcpddpce dpgptppvql aknwtfpntr aagsssdplm cpprqleglp
     1261 rtpmalpvdr krsqepsrps ptpqgppfgg srtpstsdma eegrvasggp pgletsesls
     1321 dslydslssc gsqg
//
LOCUS       NP_037493                482 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 223 [Homo sapiens].
ACCESSION   NP_037493
VERSION     NP_037493.3
DBSOURCE    REFSEQ: accession NM_013361.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Shannon,M., Hamilton,A.T., Gordon,L., Branscomb,E. and Stubbs,L.
  TITLE     Differential expansion of zinc-finger transcription factor loci in
            homologous human and mouse gene clusters
  JOURNAL   Genome Res 13 (6A), 1097-1110 (2003)
   PUBMED   12743021
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Rosati,M., Franze,A., Matarazzo,M.R. and Grimaldi,G.
  TITLE     Coding region intron/exon organization, alternative splicing, and
            X-chromosome inactivation of the KRAB/FPB-domain-containing human
            zinc finger gene ZNF41
  JOURNAL   Cytogenet Cell Genet 85 (3-4), 291-296 (1999)
   PUBMED   10449920
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Shannon,M., Ashworth,L.K., Mucenski,M.L., Lamerdin,J.E.,
            Branscomb,E. and Stubbs,L.
  TITLE     Comparative analysis of a conserved zinc finger gene cluster on
            human chromosome 19q and mouse chromosome 7
  JOURNAL   Genomics 33 (1), 112-120 (1996)
   PUBMED   8617494
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC022466.1, DR761157.1, AF187989.1, AC092072.2 and HY311227.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 28, 2007 this sequence version replaced NP_037493.2.
            
            Summary: This gene encodes a protein containing a
            Kruppel-associated box domain and multiple zinc finger domains. The
            function of this protein has yet to be determined. [provided by
            RefSeq, Mar 2014].
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA626060.1, SRR1803612.91965.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000434772.8/ ENSP00000401947.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..482
                     /product="zinc finger protein 223"
                     /note="Homo sapiens zinc finger protein 223; KRAB A
                     domain"
                     /calculated_mol_wt=55632
     Region          8..67
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <139..380
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          150..170
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          178..198
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(183,185,187,189..190,193..194,197,211,213,217..218,
                     221..222,225,239,241,243,245..246,249..250,253)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          206..226
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          234..254
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          262..282
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          294..310
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          322..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          346..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(351,353,355,357..358,361..362,365,379,381,385..386,
                     389..390,393,407,409,411,413..414,417..418,421)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <368..436
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          374..394
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          402..422
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          430..450
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..482
                     /gene="ZNF223"
                     /coded_by="NM_013361.6:229..1677"
                     /db_xref="CCDS:CCDS12635.1"
                     /db_xref="GeneID:7766"
                     /db_xref="HGNC:HGNC:13016"
ORIGIN      
        1 mtmskeavtf kdvavvftee elglldlaqr klyrdvmlen frnllsvghq pfhrdtfhfl
       61 reekfwmmdi atqregnsgg kiqpemktfp eagphegwsc qqiweeiasd ltrpqdstik
      121 ssqffeqgda hsqveeglsi mhtgqkpsnc gkckqsfsdm sifdlpqqir saekshscde
      181 cgksfcyisa lhihqrvhlg eklfkcdvcg kefsqslhlq thqrvhtgek pfkceqcgrg
      241 frcrsaltvh cklhmgekhy nceacgrafi hdfqlqkhqr ihtgekpfkc eicsvsfrlr
      301 sslnrhcvvh tgkkpnstge ygkgfirrld lckhqtihtg ekpynckecg ksfrrssyll
      361 ihqrvhtgek pykcdkcgks yitksgldlh hrahtgerpy ncddcgksfr qassilnhkr
      421 lhcrkkpfkc edcgkklvyr syrkdqqknh sgenpskced cgkrykrrln ldiilslfln
      481 dt
//
LOCUS       NP_001356865             643 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001356865
VERSION     NP_001356865.1
DBSOURCE    REFSEQ: accession NM_001369936.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.18532.1,
                                           SRR1803613.226600.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..643
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 9"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=73067
     Region          355..394
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..643
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369936.1:200..2131"
                     /note="isoform 9 is encoded by transcript variant 19"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mqkrlhrsvf ltflrmsthk eskdhfisps afgeilynnf lfdipkildl cvlfgkgnsp
       61 llqkmignif tqqpsyysdl detlptilqv fsnilqhcgl qgdganttpq kleergrltp
      121 sdmpllelkd ivlylcdtct tlwafldifp lacqtfqkhd fcyrlasfye aaipemesai
      181 kkrrledskl lgdlwqrlsh srkklmeifh iilnqicllp ilesscdniq gfieeflqif
      241 ssllqekrfl rdydalfpva edisllqqas svldetrtay ilqavesawe gvdrrkatda
      301 kdpsvieepn gepngvtvta eavsqasshp enseeeecmg aaaavgpamc gveldslisq
      361 vkdllpdlge gfilacleyy hydpeqvinn ileerlaptl sqldrnldre mkpdptpllt
      421 srhnvfqnde fdvfsrdsvd lsrvhkgkst rkeentrsll ndkravaaqr qryeqysvvv
      481 eevplqpges lpyhsvyyed eyddtydgnq vgandadsdd elisrrpfti pqvlrtkvpr
      541 egqeedddde eddadeeapk pdhfvqdpav lrekaearrm aflakkgyrh dsstavagsp
      601 rghgqsrett qerrkkeank atranhnrrt madrkrskgm ips
//
LOCUS       NP_001915                165 aa            linear   PRI 27-APR-2025
DEFINITION  growth arrest and DNA damage-inducible protein GADD45 alpha isoform
            1 [Homo sapiens].
ACCESSION   NP_001915
VERSION     NP_001915.1
DBSOURCE    REFSEQ: accession NM_001924.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Zhou,L., Bai,G., Song,Y., Liu,X., Li,X., Deng,Y., Si,Y., Shi,Y. and
            Li,H.
  TITLE     AGEs induce MMP-9 promoter demethylation through the
            GADD45alpha-mediated BER pathway to promote breast cancer
            metastasis in patients with diabetes
  JOURNAL   Endocr Relat Cancer 31 (9), e230330 (2024)
   PUBMED   38904412
  REMARK    GeneRIF: AGEs induce MMP-9 promoter demethylation through the
            GADD45alpha-mediated BER pathway to promote breast cancer
            metastasis in patients with diabetes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Hassan,N., Yi,H., Malik,B., Gaspard-Boulinc,L., Samaraweera,S.E.,
            Casolari,D.A., Seneviratne,J., Balachandran,A., Chew,T., Duly,A.,
            Carter,D.R., Cheung,B.B., Norris,M., Haber,M., Kavallaris,M.,
            Marshall,G.M., Zhang,X.D., Liu,T., Wang,J., Liebermann,D.A.,
            D'Andrea,R.J. and Wang,J.Y.
  TITLE     Loss of the stress sensor GADD45A promotes stem cell activity and
            ferroptosis resistance in LGR4/HOXA9-dependent AML
  JOURNAL   Blood 144 (1), 84-98 (2024)
   PUBMED   38579286
  REMARK    GeneRIF: Loss of the stress sensor GADD45A promotes stem cell
            activity and ferroptosis resistance in LGR4/HOXA9-dependent AML.
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Yu,L.R., Han,X.Z., Tang,Y.Z., Liu,D., Luo,X.Q., Qiu,X.W., Feng,J.,
            Yuan,W.X. and Ding,J.Y.
  TITLE     Activation of the MEK/ERK Pathway Mediates the Inhibitory Effects
            of Silvestrol on Nasopharyngeal Carcinoma Cells via RAP1A, HK2, and
            GADD45A
  JOURNAL   Front Biosci (Landmark Ed) 29 (4), 160 (2024)
   PUBMED   38682208
  REMARK    GeneRIF: Activation of the MEK/ERK Pathway Mediates the Inhibitory
            Effects of Silvestrol on Nasopharyngeal Carcinoma Cells via RAP1A,
            HK2, and GADD45A.
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Marcotte,G.R., Miller,M.J., Kunz,H.E., Ryan,Z.C., Strub,M.D.,
            Vanderboom,P.M., Heppelmann,C.J., Chau,S., Von Ruff,Z.D.,
            Kilroe,S.P., McKeen,A.T., Dierdorff,J.M., Stern,J.I., Nath,K.A.,
            Grueter,C.E., Lira,V.A., Judge,A.R., Rasmussen,B.B., Nair,K.S.,
            Lanza,I.R., Ebert,S.M. and Adams,C.M.
  TITLE     GADD45A is a mediator of mitochondrial loss, atrophy, and weakness
            in skeletal muscle
  JOURNAL   JCI Insight 8 (22), e171772 (2023)
   PUBMED   37815864
  REMARK    GeneRIF: GADD45A is a mediator of mitochondrial loss, atrophy, and
            weakness in skeletal muscle.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Gebert,M., Bartoszewska,S., Opalinski,L., Collawn,J.F. and
            Bartoszewski,R.
  TITLE     IRE1-mediated degradation of pre-miR-301a promotes apoptosis
            through upregulation of GADD45A
  JOURNAL   Cell Commun Signal 21 (1), 322 (2023)
   PUBMED   37946177
  REMARK    GeneRIF: IRE1-mediated degradation of pre-miR-301a promotes
            apoptosis through upregulation of GADD45A.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Chen,I.T., Smith,M.L., O'Connor,P.M. and Fornace,A.J. Jr.
  TITLE     Direct interaction of Gadd45 with PCNA and evidence for competitive
            interaction of Gadd45 and p21Waf1/Cip1 with PCNA
  JOURNAL   Oncogene 11 (10), 1931-1937 (1995)
   PUBMED   7478510
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Kearsey,J.M., Coates,P.J., Prescott,A.R., Warbrick,E. and Hall,P.A.
  TITLE     Gadd45 is a nuclear cell cycle regulated protein which interacts
            with p21Cip1
  JOURNAL   Oncogene 11 (9), 1675-1683 (1995)
   PUBMED   7478594
REFERENCE   8  (residues 1 to 165)
  AUTHORS   Carrier,F., Smith,M.L., Bae,I., Kilpatrick,K.E., Lansing,T.J.,
            Chen,C.Y., Engelstein,M., Friend,S.H., Henner,W.D., Gilmer,T.M. et
            al.
  TITLE     Characterization of human Gadd45, a p53-regulated protein
  JOURNAL   J Biol Chem 269 (51), 32672-32677 (1994)
   PUBMED   7798274
REFERENCE   9  (residues 1 to 165)
  AUTHORS   Smith,M.L., Chen,I.T., Zhan,Q., Bae,I., Chen,C.Y., Gilmer,T.M.,
            Kastan,M.B., O'Connor,P.M. and Fornace,A.J. Jr.
  TITLE     Interaction of the p53-regulated protein Gadd45 with proliferating
            cell nuclear antigen
  JOURNAL   Science 266 (5189), 1376-1380 (1994)
   PUBMED   7973727
REFERENCE   10 (residues 1 to 165)
  AUTHORS   Papathanasiou,M.A., Kerr,N.C., Robbins,J.H., McBride,O.W., Alamo,I.
            Jr., Barrett,S.F., Hickson,I.D. and Fornace,A.J. Jr.
  TITLE     Induction by ionizing radiation of the gadd45 gene in cultured
            human cells: lack of mediation by protein kinase C
  JOURNAL   Mol Cell Biol 11 (2), 1009-1016 (1991)
   PUBMED   1990262
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314991.1 and M60974.1.
            
            Summary: This gene is a member of a group of genes whose transcript
            levels are increased following stressful growth arrest conditions
            and treatment with DNA-damaging agents. The protein encoded by this
            gene responds to environmental stresses by mediating activation of
            the p38/JNK pathway via MTK1/MEKK4 kinase. The DNA damage-induced
            transcription of this gene is mediated by both p53-dependent and
            -independent mechanisms. Alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene.[provided
            by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.705608.1,
                                           SRR1163658.469431.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370986.9/ ENSP00000360025.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..165
                     /product="growth arrest and DNA damage-inducible protein
                     GADD45 alpha isoform 1"
                     /note="DNA damage-inducible transcript-1; growth arrest
                     and DNA damage-inducible protein GADD45 alpha; growth
                     arrest and DNA-damage-inducible 45 alpha; DDIT-1; DNA
                     damage-inducible transcript 1 protein"
                     /calculated_mol_wt=18205
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P24522.1)"
     Region          21..123
                     /region_name="Ribosomal_L7Ae"
                     /note="Ribosomal protein L7Ae/L30e/S12e/Gadd45 family;
                     pfam01248"
                     /db_xref="CDD:426153"
     CDS             1..165
                     /gene="GADD45A"
                     /gene_synonym="DDIT1; GADD45"
                     /coded_by="NM_001924.4:295..792"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS640.1"
                     /db_xref="GeneID:1647"
                     /db_xref="HGNC:HGNC:4095"
                     /db_xref="MIM:126335"
ORIGIN      
        1 mtleefsage qktermdkvg daleevlska lsqrtitvgv yeaakllnvd pdnvvlclla
       61 adedddrdva lqihftliqa fccendinil rvsnpgrlae lllletdagp aasegaeqpp
      121 dlhcvlvtnp hssqwkdpal sqlicfcres rymdqwvpvi nlper
//
LOCUS       NP_001356475             464 aa            linear   PRI 27-APR-2025
DEFINITION  BDNF/NT-3 growth factors receptor isoform f precursor [Homo
            sapiens].
ACCESSION   NP_001356475
VERSION     NP_001356475.1
DBSOURCE    REFSEQ: accession NM_001369546.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Gupta,R., Dittmeier,M., Wohlleben,G., Nickl,V., Bischler,T.,
            Luzak,V., Wegat,V., Doll,D., Sodmann,A., Bady,E., Langlhofer,G.,
            Wachter,B., Havlicek,S., Gupta,J., Horn,E., Luningschror,P.,
            Villmann,C., Polat,B., Wischhusen,J., Monoranu,C.M., Kuper,J. and
            Blum,R.
  TITLE     Atypical cellular responses mediated by intracellular constitutive
            active TrkB (NTRK2) kinase domains and a solely intracellular
            NTRK2-fusion oncogene
  JOURNAL   Cancer Gene Ther 31 (9), 1357-1379 (2024)
   PUBMED   39039193
  REMARK    GeneRIF: Atypical cellular responses mediated by intracellular
            constitutive active TrkB (NTRK2) kinase domains and a solely
            intracellular NTRK2-fusion oncogene.
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Zhang,X., Zhang,Y., Yan,H., Yu,H., Zhang,D., Mattay,V.S., Tan,H.Y.
            and Yue,W.
  TITLE     Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2
  JOURNAL   BMC Med 22 (1), 146 (2024)
   PUBMED   38561734
  REMARK    GeneRIF: Childhood urbanicity is associated with emotional episodic
            memory-related striatal function and common variation in NTRK2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Ikhlef,L., Yassine,M., Chandouri,B., Riviere,L., Naves,T.,
            Dmytruk,N., Gachard,N., Jauberteau,M.O. and Gallet,P.F.
  TITLE     Targeting the NTSR2/TrkB oncogenic pathway in chronic lymphocytic
            leukemia
  JOURNAL   Sci Rep 14 (1), 6084 (2024)
   PUBMED   38480783
  REMARK    GeneRIF: Targeting the NTSR2/TrkB oncogenic pathway in chronic
            lymphocytic leukemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Wang,Y., Liang,J., Xu,B., Yang,J., Wu,Z. and Cheng,L.
  TITLE     TrkB/BDNF signaling pathway and its small molecular agonists in CNS
            injury
  JOURNAL   Life Sci 336, 122282 (2024)
   PUBMED   38008209
  REMARK    GeneRIF: TrkB/BDNF signaling pathway and its small molecular
            agonists in CNS injury.
            Review article
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Luberg,K., Wong,J., Weickert,C.S. and Timmusk,T.
  TITLE     Human TrkB gene: novel alternative transcripts, protein isoforms
            and expression pattern in the prefrontal cerebral cortex during
            postnatal development
  JOURNAL   J Neurochem 113 (4), 952-964 (2010)
   PUBMED   20193039
  REMARK    GeneRIF: Identification of 36 potential TrkB protein isoforms
            suggests high complexity in the synthesis, regulation and function
            of this important neurotrophin receptor emphasizing the need for
            further study of these novel TrkB variants.
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Stoilov,P., Castren,E. and Stamm,S.
  TITLE     Analysis of the human TrkB gene genomic organization reveals novel
            TrkB isoforms, unusual gene length, and splicing mechanism
  JOURNAL   Biochem Biophys Res Commun 290 (3), 1054-1065 (2002)
   PUBMED   11798182
  REMARK    GeneRIF: analysis of TrkB gene reveals novel gene length and
            splicing mechanism
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Haniu,M., Talvenheimo,J., Le,J., Katta,V., Welcher,A. and
            Rohde,M.F.
  TITLE     Extracellular domain of neurotrophin receptor trkB: disulfide
            structure, N-glycosylation sites, and ligand binding
  JOURNAL   Arch Biochem Biophys 322 (1), 256-264 (1995)
   PUBMED   7574684
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Nakagawara,A., Liu,X.G., Ikegaki,N., White,P.S., Yamashiro,D.J.,
            Nycum,L.M., Biegel,J.A. and Brodeur,G.M.
  TITLE     Cloning and chromosomal localization of the human TRK-B tyrosine
            kinase receptor gene (NTRK2)
  JOURNAL   Genomics 25 (2), 538-546 (1995)
   PUBMED   7789988
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Squinto,S.P., Stitt,T.N., Aldrich,T.H., Davis,S., Blanco,S.M.,
            RadzieJewski,C., Glass,D.J., Masiakowski,P., Furth,M.E.,
            Valenzuela,D.M., Distefano,P.S. and Yancopoulos,G.D.
  TITLE     trkB encodes a functional receptor for brain-derived neurotrophic
            factor and neurotrophin-3 but not nerve growth factor
  JOURNAL   Cell 65 (5), 885-893 (1991)
   PUBMED   1710174
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Soppet,D., Escandon,E., Maragos,J., Middlemas,D.S., Reid,S.W.,
            Blair,J., Burton,L.E., Stanton,B.R., Kaplan,D.R., Hunter,T.,
            Nikolics,K. and Parada,L.F.
  TITLE     The neurotrophic factors brain-derived neurotrophic factor and
            neurotrophin-3 are ligands for the trkB tyrosine kinase receptor
  JOURNAL   Cell 65 (5), 895-903 (1991)
   PUBMED   1645620
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390777.13.
            
            Summary: This gene encodes a member of the neurotrophic tyrosine
            receptor kinase (NTRK) family. This kinase is a membrane-bound
            receptor that, upon neurotrophin binding, phosphorylates itself and
            members of the MAPK pathway. Signalling through this kinase leads
            to cell differentiation. Mutations in this gene have been
            associated with obesity and mood disorders. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (x), as well as variant f, encodes
            isoform f.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.6331.1,
                                           SRR1803617.114122.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..464
                     /product="BDNF/NT-3 growth factors receptor isoform f
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="BDNF/NT-3 growth factors receptor; tyrosine kinase
                     receptor B; BDNF-tropomyosine receptor kinase B;
                     tropomyosin-related kinase B; neurotrophic tyrosine kinase
                     receptor type 2"
                     /calculated_mol_wt=48028
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3697
     Region          31..60
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; pfam01462"
                     /db_xref="CDD:396168"
     Region          92..150
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          96..116
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          117..139
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          140..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          151..195
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Region          205..283
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          214..218
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          227..230
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          245..252
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          262..268
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          276..279
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          286..366
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          288..292
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..305
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..335
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          345..350
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          358..361
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..464
                     /gene="NTRK2"
                     /gene_synonym="DEE58; EIEE58; GP145-TrkB; OBHD; trk-B;
                     TRKB"
                     /coded_by="NM_001369546.1:491..1885"
                     /note="isoform f precursor is encoded by transcript
                     variant x"
                     /db_xref="CCDS:CCDS94428.1"
                     /db_xref="GeneID:4915"
                     /db_xref="HGNC:HGNC:8032"
                     /db_xref="MIM:600456"
ORIGIN      
        1 msswirwhgp amarlwgfcw lvvgfwraaf acptsckcsa sriwcsdpsp givafprlep
       61 nsvdpenite ifianqkrle iineddveay vglrnltivd sglkfvahka flknsnlqhi
      121 nftrnkltsl srkhfrhldl selilvgnpf tcscdimwik tlqeaksspd tqdlyclnes
      181 skniplanlq ipncglpsan laapnltvee gksitlscsv agdpvpnmyw dvgnlvskhm
      241 netshtqgsl ritnissdds gkqiscvaen lvgedqdsvn ltvhyhhwci pftvkgnpkp
      301 alqwfyngai lneskyictk ihvtnhteyh gclqldnpth mnngdytlia kneygkdekq
      361 isahfmgwpg iddganpnyp dviyedygta andigdttnr sneipstdvt dktgrehlsv
      421 yavvviasvv gfcllvmlfl lklarhskfg mkgfvlfhki pldg
//
LOCUS       NP_057093                365 aa            linear   PRI 27-APR-2025
DEFINITION  endophilin-B1 isoform 1 [Homo sapiens].
ACCESSION   NP_057093
VERSION     NP_057093.1
DBSOURCE    REFSEQ: accession NM_016009.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Bhatt,V.S., Ashley,R. and Sundborger-Lunna,A.
  TITLE     Amphipathic Motifs Regulate N-BAR Protein Endophilin B1
            Auto-inhibition and Drive Membrane Remodeling
  JOURNAL   Structure 29 (1), 61-69 (2021)
   PUBMED   33086035
  REMARK    GeneRIF: Amphipathic Motifs Regulate N-BAR Protein Endophilin B1
            Auto-inhibition and Drive Membrane Remodeling.
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Frangez,Z., Seyed Jafari,S.M., Hunger,R.E. and Simon,H.U.
  TITLE     Loss of Concurrent Regulation of the Expression of BIF-1, BAX, and
            Beclin-1 in Primary and Metastatic Melanoma
  JOURNAL   Biochemistry (Mosc) 85 (10), 1227-1234 (2020)
   PUBMED   33202207
  REMARK    GeneRIF: Loss of Concurrent Regulation of the Expression of BIF-1,
            BAX, and Beclin-1 in Primary and Metastatic Melanoma.
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Karbowski,M., Jeong,S.Y. and Youle,R.J.
  TITLE     Endophilin B1 is required for the maintenance of mitochondrial
            morphology
  JOURNAL   J Cell Biol 166 (7), 1027-1039 (2004)
   PUBMED   15452144
  REMARK    GeneRIF: Double knockdown of endophilin B1 and Drp1 leads to a
            mitochondrial phenotype identical to that of the Drp1 single
            knockdown, a result consistent with Drp1 acting upstream of
            endophilin B1 in the maintenance of morphological dynamics of
            mitochondria.
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Lee,S.Y., Wenk,M.R., Kim,Y., Nairn,A.C. and De Camilli,P.
  TITLE     Regulation of synaptojanin 1 by cyclin-dependent kinase 5 at
            synapses
  JOURNAL   Proc Natl Acad Sci U S A 101 (2), 546-551 (2004)
   PUBMED   14704270
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Modregger,J., Schmidt,A.A., Ritter,B., Huttner,W.B. and Plomann,M.
  TITLE     Characterization of Endophilin B1b, a brain-specific
            membrane-associated lysophosphatidic acid acyl transferase with
            properties distinct from endophilin A1
  JOURNAL   J Biol Chem 278 (6), 4160-4167 (2003)
   PUBMED   12456676
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Cuddeback,S.M., Yamaguchi,H., Komatsu,K., Miyashita,T., Yamada,M.,
            Wu,C., Singh,S. and Wang,H.G.
  TITLE     Molecular cloning and characterization of Bif-1. A novel Src
            homology 3 domain-containing protein that associates with Bax
  JOURNAL   J Biol Chem 276 (23), 20559-20565 (2001)
   PUBMED   11259440
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Pierrat,B., Simonen,M., Cueto,M., Mestan,J., Ferrigno,P. and
            Heim,J.
  TITLE     SH3GLB, a new endophilin-related protein family featuring an SH3
            domain
  JOURNAL   Genomics 71 (2), 222-234 (2001)
   PUBMED   11161816
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Howard,L., Nelson,K.K., Maciewicz,R.A. and Blobel,C.P.
  TITLE     Interaction of the metalloprotease disintegrins MDC9 and MDC15 with
            two SH3 domain-containing proteins, endophilin I and SH3PX1
  JOURNAL   J Biol Chem 274 (44), 31693-31699 (1999)
   PUBMED   10531379
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB038227.1, AF350371.1,
            AL049597.29 and AI936794.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a SRC homology 3 domain-containing
            protein. The encoded protein interacts with the proapoptotic member
            of the Bcl-2 family, Bcl-2-associated X protein (Bax) and may be
            involved in regulating apoptotic signaling pathways. This protein
            may also be involved in maintaining mitochondrial morphology.
            Alternate splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) is a predominant transcript
            and encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.82142.1,
                                           SRR1660803.103847.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370558.8/ ENSP00000473267.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.3"
     Protein         1..365
                     /product="endophilin-B1 isoform 1"
                     /note="Bax-interacting factor 1; SH3-containing protein
                     SH3GLB1; SH3 domain-containing GRB2-like protein B1;
                     SH3-domain GRB2 like endophilin B1; protein phosphatase 1,
                     regulatory subunit 70; testicular tissue protein Li 172"
                     /calculated_mol_wt=40665
     Region          1..37
                     /region_name="Required for membrane binding.
                     /evidence=ECO:0000269|PubMed:21068542"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y371.1)"
     Region          1..30
                     /region_name="Membrane-binding amphipathic helix"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y371.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9Y371.1)"
     Region          24..252
                     /region_name="BAR_Endophilin_B1"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of
                     Endophilin-B1; cd07616"
                     /db_xref="CDD:153300"
     Site            order(48,51..52,56,58..59,62..63,65..66,93..94,96..97,
                     100..101,103..104,107,121,124..125,214,217..218,220,224,
                     227..228,230..231,234..235,238..239,241..242,245..246,
                     248..249)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153300"
     Site            order(74,156,160,163,168..169,178,181,196)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153300"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK5.
                     /evidence=ECO:0000269|PubMed:21499257; propagated from
                     UniProtKB/Swiss-Prot (Q9Y371.1)"
     Region          305..365
                     /region_name="SH3_Endophilin_B1"
                     /note="Src homology 3 domain of Endophilin-B1; cd11945"
                     /db_xref="CDD:212878"
     Site            order(314,316,319,323,343..344,357,359..360)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212878"
     CDS             1..365
                     /gene="SH3GLB1"
                     /gene_synonym="Bif-1; CGI-61; dJ612B15.2; PPP1R70"
                     /coded_by="NM_016009.5:325..1422"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS710.1"
                     /db_xref="GeneID:51100"
                     /db_xref="HGNC:HGNC:10833"
                     /db_xref="MIM:609287"
ORIGIN      
        1 mnimdfnvkk laadagtfls ravqfteekl gqaektelda hlenllskae ctkiwtekim
       61 kqtevllqpn pnarieefvy ekldrkapsr innpellgqy midagtefgp gtaygnalik
      121 cgetqkrigt adreliqtsa lnfltplrnf iegdyktiak erkllqnkrl dldaaktrlk
      181 kakaaetrns seqelritqs efdrqaeitr lllegissth ahhlrclndf veaqmtyyaq
      241 cyqymldlqk qlgsfpsnyl snnnqtsvtp vpsvlpnaig ssamastsgl vitspsnlsd
      301 lkecsgsrka rvlydydaan stelsllade vitvfsvvgm dsdwlmgerg nqkgkvpity
      361 lelln
//
LOCUS       NP_001192446             394 aa            linear   MAM 27-APR-2025
DEFINITION  RNA demethylase ALKBH5 [Bos taurus].
ACCESSION   NP_001192446 XP_001790649
VERSION     NP_001192446.2
DBSOURCE    REFSEQ: accession NM_001205517.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            NKLS02000019.1.
            
            On May 30, 2018 this sequence version replaced NP_001192446.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GGVC01076889.1, GGUY01100852.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA6648756,
                                           SAMEA6648764 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="19"
                     /map="19"
                     /breed="Hereford"
     Protein         1..394
                     /product="RNA demethylase ALKBH5"
                     /EC_number="1.14.11.53"
                     /note="alkylated DNA repair protein alkB homolog 5;
                     alpha-ketoglutarate-dependent dioxygenase alkB homolog 5;
                     alkB, alkylation repair homolog 5; AlkB family member 5,
                     RNA demethylase"
                     /calculated_mol_wt=43938
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E1BH29.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (E1BH29.1)"
     Region          48..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E1BH29.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (E1BH29.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (E1BH29.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (E1BH29.1)"
     Site            132
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (E1BH29.1)"
     Region          <136..270
                     /region_name="2OG-FeII_Oxy"
                     /note="2OG-Fe(II) oxygenase superfamily; cl21496"
                     /db_xref="CDD:473886"
     Site            235
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (E1BH29.1)"
     Region          298..394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E1BH29.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (E1BH29.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TSG4; propagated from
                     UniProtKB/Swiss-Prot (E1BH29.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TSG4; propagated from
                     UniProtKB/Swiss-Prot (E1BH29.1)"
     CDS             1..394
                     /gene="ALKBH5"
                     /coded_by="NM_001205517.3:1..1185"
                     /db_xref="GeneID:533303"
                     /db_xref="VGNC:VGNC:25836"
ORIGIN      
        1 maaasgytdl reklksmtsr dnykagsrea aaaaaaavaa aaaaaaaaep yaapgakrky
       61 pedsdpersd feeqqlqkee earkvksgir qmrlfsqdec akiearidev vsraekglyn
      121 ehtvdraplr nkyffgegyt ygaqlqkrgp gqerlyppgd vdeipewvhq lviqklvehr
      181 vipegfvnsa vindyqpggc ivshvdpihi ferpivsvsf fsdsalcfgc kfqfkpirvs
      241 epvlslpvrr gsvtvlsgya adeithcirp qdikerravi ilrktrldap rletkslsss
      301 vlppsyasdr lsgnnrdpal kpkrshrkad pdaahrpril emdkeenrrs vllpahrrag
      361 rfssenyrrk syepgedcse aagsparkvk mrrh
//
LOCUS       NP_001353499             832 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 8 [Homo
            sapiens].
ACCESSION   NP_001353499 XP_016855513
VERSION     NP_001353499.1
DBSOURCE    REFSEQ: accession NM_001366570.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 832)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 832)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 832)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 832)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 832)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 832)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 832)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 832)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 832)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 832)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855513.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.158779.1,
                                           SRR1660807.233502.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..832
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..832
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 8"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=93859
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <298..658
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..832
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366570.1:2055..4553"
                     /note="isoform 8 is encoded by transcript variant 10"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsvtkhkgt
      361 ekrespspap kprkvelses edkggkmaaa dsvqqrrqyr rqnqqsssds gssssseder
      421 pkrshvknge vgrrrrhsps rsaspsprkr qketsprmqm gkrwqspvtk sgrrrrspsp
      481 pptrrrrsps pappprrrrt ptppprrrtp sppprrrsps prrysppiqr ryspspppkr
      541 rtaspppppk rraspspppk rrvshspppk qrsspvtkrr spslsskhrk gsspsrstre
      601 arspqpnkrh spsprprapq tssspppvrr gassspqrrq spspstrpir rvsrtpepkk
      661 ikkaaspspq svrrvsssrs vsgspepaak kppappspvq sqspstnwsp avpvkkaksp
      721 tpspspprns dqegggkkkk kkkdkkhkkd kkhkkhkkhk kekavaaaaa aavtpaaiaa
      781 atttlaqeep vaapepkket eseaednldd lekhlrekal rsmrkaqvsp qs
//
LOCUS       NP_060553                568 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 358 [Homo sapiens].
ACCESSION   NP_060553
VERSION     NP_060553.4
DBSOURCE    REFSEQ: accession NM_018083.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Wride,M.A., Mansergh,F.C., Somani,J.M., Winkfein,R.J. and
            Rancourt,D.E.
  TITLE     Characterization and in silico mapping of a novel murine zinc
            finger transcription factor
  JOURNAL   Gene 289 (1-2), 49-59 (2002)
   PUBMED   12036583
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Bassi,M.T., Manzoni,M., Monti,E., Pizzo,M.T., Ballabio,A. and
            Borsani,G.
  TITLE     Cloning of the gene encoding a novel integral membrane protein,
            mucolipidin-and identification of the two major founder mutations
            causing mucolipidosis type IV
  JOURNAL   Am J Hum Genet 67 (5), 1110-1120 (2000)
   PUBMED   11013137
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008878.10, BI601846.1, AK001252.2 and BC003585.1.
            
            On Mar 22, 2007 this sequence version replaced NP_060553.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279839.2952.1,
                                           SRR1163657.353982.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000597229.2/ ENSP00000472305.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..568
                     /product="zinc finger protein 358"
                     /calculated_mol_wt=59156
     Region          1..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW07.2)"
     Region          <35..339
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          153..173
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(158,160,162,164..165,168..169,172,186,188,192..193,
                     196..197,200,214,216,218,220..221,224..225,228)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          166..190
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          181..201
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          209..229
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          237..257
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          265..285
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          293..313
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(298,300,302,304..305,308..309,312,326,328,332..333,
                     336..337,340,354,356,358,360..361,364..365,368)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          321..341
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          333..356
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          349..369
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          361..384
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          375..397
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          377..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          448..568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW07.2)"
     CDS             1..568
                     /gene="ZNF358"
                     /gene_synonym="ZFEND"
                     /coded_by="NM_018083.5:186..1892"
                     /db_xref="CCDS:CCDS32890.2"
                     /db_xref="GeneID:140467"
                     /db_xref="HGNC:HGNC:16838"
                     /db_xref="MIM:619496"
ORIGIN      
        1 mrrsvlvrnp ghkglrpvye eldsdsedld pnpedldpvs edpepdpedl ntvpedvdps
       61 yedlepvsed ldpdaeapgs epqdpdpmss sfdldpdvig pvplildpns dtlspgdpkv
      121 dpissgltat pqvlatspav lpapaspprp fscpdcgraf rrssglsqhr rthsgekpyr
      181 cpdcgksfsh gatlaqhrgi htgarpyqca acgkafgwrs tllkhrsshs gekphhcpvc
      241 gkafghgsll aqhlrthggp rphkcpvcak gfgqgsallk hlrthtgerp ypcpqcgkaf
      301 gqssallqhq rthtaerpyr cphcgkafgq ssnlqhhlri htgerpyacp hcskafgqss
      361 allqhlhvhs gerpyrcqlc gkafgqassl tkhkrvhega aaaaaaaaaa aaaaaaglgl
      421 gpglspasmm rpgqvsllgp davsvlgsgl glspgtssgr npdpgsgpgt lpdpsskplp
      481 gsrstpsptp vessdpkagh dagpdlvpsp dldpvpspdp dpvpspdpnp vscpdpcspt
      541 rgtvspalpt gespewvqeq gallgpdg
//
LOCUS       NP_998783               1137 aa            linear   PRI 27-APR-2025
DEFINITION  DENN domain-containing protein 2B isoform 1 [Homo sapiens].
ACCESSION   NP_998783
VERSION     NP_998783.1
DBSOURCE    REFSEQ: accession NM_213618.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Kumar,R., Francis,V., Ioannou,M.S., Aguila,A., Khan,M., Banks,E.,
            Kulasekaran,G. and McPherson,P.S.
  TITLE     DENND2B activates Rab35 at the intercellular bridge, regulating
            cytokinetic abscission and tetraploidy
  JOURNAL   Cell Rep 42 (7), 112795 (2023)
   PUBMED   37454296
  REMARK    GeneRIF: DENND2B activates Rab35 at the intercellular bridge,
            regulating cytokinetic abscission and tetraploidy.
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Kim,M.K., Kim,B., Kwon,J.O., Song,M.K., Jung,S., Lee,Z.H. and
            Kim,H.H.
  TITLE     ST5 Positively Regulates Osteoclastogenesis via Src/Syk/calcium
            Signaling Pathways
  JOURNAL   Mol Cells 42 (11), 810-819 (2019)
   PUBMED   31707778
  REMARK    GeneRIF: Findings provide evidence of suppression of tumorigenicity
            5 (ST5) involvement in positive regulation of osteoclastogenesis
            via src Kinases (Src)/Syk Kinase (Syk)/calcium signaling.
REFERENCE   4  (residues 1 to 1137)
  AUTHORS   Ioannou,M.S., Kulasekaran,G., Fotouhi,M., Morein,J.J., Han,C.,
            Tse,S., Nossova,N., Han,T., Mannard,E. and McPherson,P.S.
  TITLE     Intersectin-s interaction with DENND2B facilitates recycling of
            epidermal growth factor receptor
  JOURNAL   EMBO Rep 18 (12), 2119-2130 (2017)
   PUBMED   29030480
  REMARK    GeneRIF: Here, we discover that intersectin-s binds DENND2B, a
            guanine nucleotide exchange factor for the exocytic GTPase Rab13,
            and this interaction promotes recycling of ligand-free EGFR to the
            cell surface.  Our study thus reveals a novel mechanism controlling
            the fate of internalized EGFR with important implications for
            cancer.
REFERENCE   5  (residues 1 to 1137)
  AUTHORS   Ioannou,M.S., Bell,E.S., Girard,M., Chaineau,M., Hamlin,J.N.,
            Daubaras,M., Monast,A., Park,M., Hodgson,L. and McPherson,P.S.
  TITLE     DENND2B activates Rab13 at the leading edge of migrating cells and
            promotes metastatic behavior
  JOURNAL   J Cell Biol 208 (5), 629-648 (2015)
   PUBMED   25713415
  REMARK    GeneRIF: DENND2B interacts with the Rab13 effector MICAL-L2 at the
            cell periphery, and this interaction is required for the dynamic
            remodeling of the cell's leading edge.
REFERENCE   6  (residues 1 to 1137)
  AUTHORS   Majidi,M., Gutkind,J.S. and Lichy,J.H.
  TITLE     Deletion of the COOH terminus converts the ST5 p70 protein from an
            inhibitor of RAS signaling to an activator with transforming
            activity in NIH-3T3 cells
  JOURNAL   J Biol Chem 275 (9), 6560-6565 (2000)
   PUBMED   10692462
REFERENCE   7  (residues 1 to 1137)
  AUTHORS   Hubbs,A.E., Majidi,M. and Lichy,J.H.
  TITLE     Expression of an isoform of the novel signal transduction protein
            ST5 is linked to cell morphology
  JOURNAL   Oncogene 18 (15), 2519-2525 (1999)
   PUBMED   10229203
REFERENCE   8  (residues 1 to 1137)
  AUTHORS   Majidi,M., Hubbs,A.E. and Lichy,J.H.
  TITLE     Activation of extracellular signal-regulated kinase 2 by a novel
            Abl-binding protein, ST5
  JOURNAL   J Biol Chem 273 (26), 16608-16614 (1998)
   PUBMED   9632734
REFERENCE   9  (residues 1 to 1137)
  AUTHORS   Lichy,J.H., Majidi,M., Elbaum,J. and Tsai,M.M.
  TITLE     Differential expression of the human ST5 gene in HeLa-fibroblast
            hybrid cell lines mediated by YY1: evidence that YY1 plays a part
            in tumor suppression
  JOURNAL   Nucleic Acids Res 24 (23), 4700-4708 (1996)
   PUBMED   8972856
REFERENCE   10 (residues 1 to 1137)
  AUTHORS   Lichy,J.H., Modi,W.S., Seuanez,H.N. and Howley,P.M.
  TITLE     Identification of a human chromosome 11 gene which is
            differentially regulated in tumorigenic and nontumorigenic somatic
            cell hybrids of HeLa cells
  JOURNAL   Cell Growth Differ 3 (8), 541-548 (1992)
   PUBMED   1390339
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX647431.1, BC036655.1,
            U15131.1 and U15780.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene was identified by its ability to suppress the
            tumorigenicity of Hela cells in nude mice. The protein encoded by
            this gene contains a C-terminal region that shares similarity with
            the Rab 3 family of small GTP binding proteins. This protein
            preferentially binds to the SH3 domain of c-Abl kinase, and acts as
            a regulator of MAPK1/ERK2 kinase, which may contribute to its
            ability to reduce the tumorigenic phenotype in cells. Three
            alternatively spliced transcript variants of this gene encoding
            distinct isoforms are identified. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647431.1, AK312305.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313726.11/ ENSP00000319678.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..1137
                     /product="DENN domain-containing protein 2B isoform 1"
                     /note="DENN/MADD domain containing 2B; suppression of
                     tumorigenicity 5 protein; heLa tumor suppression 1"
                     /calculated_mol_wt=126354
     Region          1..99
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78524.3)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29030480; propagated from
                     UniProtKB/Swiss-Prot (P78524.3)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q924W7; propagated from
                     UniProtKB/Swiss-Prot (P78524.3)"
     Region          <46..411
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q924W7; propagated from
                     UniProtKB/Swiss-Prot (P78524.3)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q924W7; propagated from
                     UniProtKB/Swiss-Prot (P78524.3)"
     Region          293..573
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78524.3)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P78524.3)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P78524.3)"
     Region          401..447
                     /region_name="Interaction with ABL1.
                     /evidence=ECO:0000269|PubMed:9632734"
                     /note="propagated from UniProtKB/Swiss-Prot (P78524.3)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q924W7; propagated from
                     UniProtKB/Swiss-Prot (P78524.3)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q924W7; propagated from
                     UniProtKB/Swiss-Prot (P78524.3)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q924W7; propagated from
                     UniProtKB/Swiss-Prot (P78524.3)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P78524.3)"
     Region          641..661
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78524.3)"
     Region          697..784
                     /region_name="uDENN"
                     /note="Domain always found upstream of DENN domain, found
                     in a variety of signalling proteins; smart00800"
                     /db_xref="CDD:214824"
     Region          791..975
                     /region_name="DENN"
                     /note="DENN (AEX-3) domain; pfam02141"
                     /db_xref="CDD:460461"
     Region          1023..1089
                     /region_name="dDENN"
                     /note="Domain always found downstream of DENN domain,
                     found in a variety of signalling proteins; smart00801"
                     /db_xref="CDD:129037"
     CDS             1..1137
                     /gene="DENND2B"
                     /gene_synonym="HTS1; p126; ST5"
                     /coded_by="NM_213618.2:184..3597"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS7791.1"
                     /db_xref="GeneID:6764"
                     /db_xref="HGNC:HGNC:11350"
                     /db_xref="MIM:140750"
ORIGIN      
        1 mtmtanknss ithgaggtka prgtlsrsqs vspppvlspp rspiyplsds etsacrypsh
       61 sssrvllkdr hppapspqnp qdpspdtspp tcpfktasfg yldrspsack rdaqkesvqg
      121 aaqdvagvaa clplaqstpf pgpaagprgv lltrtgtrah slgirekisa wegrreaspr
      181 msmcgekreg sgsewaaseg cpslgcpsvv pspcssektf dfkglrrmsr tfsecsypet
      241 eeegealpvr dsfyrlekrl grsepsaflr ghgsrkessa vlsriqkieq vlkeqpgrgl
      301 pqlpsscysv drgkrktgtl gsleepagga svsagsravg vagvageagp pperegsgst
      361 kpgtpgnsps sqrlpskssl dpavnpvpkp krtfeyeadk npkskpsngl ppsptpaapp
      421 plpstpappv trrpkkdmrg hrksqsrksf efedasslqs lypsspteng tenqpkfgsk
      481 stleenayed ivgdlpkenp yedvdlksrr agrksqqlse nsldslhrmw spqdrkynsp
      541 ptqlslkpns qslrsgnwse rkshrlprlp krhshddmll laqlslpssp sslnedslst
      601 tsellssrra rripklvqri nsiynakrgk krlkklsmss ietaslrden sesesdsddr
      661 fkahtqrlvh iqsmlkraps yrtlelelle wqerelfeyf vvvslkkkps rntylpevsy
      721 qfpkldrptk qmreaeerlk aipqfcfpda kdwlpvseys setfsfmltg edgsrrfgyc
      781 rrllpsgkgp rlpevycvis rlgcfglfsk vldeverrrg isaalvypfm rslmespfpa
      841 pgktikvktf lpgagnevle lrrpmdsrle hvdfeclftc lsvrqlirif aslllerrvi
      901 fvadklstls scshavvall ypfswqhtfi pvlpasmidi vccptpflvg llssslpklk
      961 elpveealmv nlgsdrfirq mddedtllpr klqaaleqal erknelisqd sdsdsddecn
     1021 tlnglvsevf irffvetvgh yslfltqsek gerafqreaf rksvasksir rflevfmesq
     1081 mfagfiqdre lrkcrakglf eqrveqylee lpdteqsgmn kflrglgnkm kflhkkn
//
LOCUS       NP_006627                350 aa            linear   PRI 27-APR-2025
DEFINITION  bifunctional methylenetetrahydrofolate
            dehydrogenase/cyclohydrolase, mitochondrial isoform A precursor
            [Homo sapiens].
ACCESSION   NP_006627
VERSION     NP_006627.2
DBSOURCE    REFSEQ: accession NM_006636.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Mo,H.Y., Wang,R.B., Ma,M.Y., Zhang,Y., Li,X.Y., Wen,W.R., Han,Y.
            and Tian,T.
  TITLE     MTHFD2-mediated redox homeostasis promotes gastric cancer
            progression under hypoxic conditions
  JOURNAL   Redox Rep 29 (1), 2345455 (2024)
   PUBMED   38723197
  REMARK    GeneRIF: MTHFD2-mediated redox homeostasis promotes gastric cancer
            progression under hypoxic conditions.
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Silva,R.V.N., Berzotti,L.A., Laia,M.G., Araujo,L.S., Silva,C.A.,
            Ribeiro,K.B., Brandao,M., Michelleti,A.M.R., Machado,J.R. and
            Lira,R.C.P.
  TITLE     Implications of MTHFD2 expression in renal cell carcinoma
            aggressiveness
  JOURNAL   PLoS One 19 (2), e0299353 (2024)
   PUBMED   38422037
  REMARK    GeneRIF: Implications of MTHFD2 expression in renal cell carcinoma
            aggressiveness.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Wang,J., Yu,Z., Jiang,Y., Le,T., Wu,Y., Li,Z., Zhang,G., Wu,F. and
            Ma,H.
  TITLE     Downregulation of MTHFD2 Inhibits Proliferation and Enhances
            Chemosensitivity in Hepatocellular Carcinoma via PI3K/AKT Pathway
  JOURNAL   Front Biosci (Landmark Ed) 29 (1), 35 (2024)
   PUBMED   38287824
  REMARK    GeneRIF: Downregulation of MTHFD2 Inhibits Proliferation and
            Enhances Chemosensitivity in Hepatocellular Carcinoma via PI3K/AKT
            Pathway.
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Wu,S., Cai,W., Li,Y., Tan,W., Yuan,Y., Zhou,Z., Shi,J., Liu,X. and
            Gao,H.
  TITLE     SNHG3/hsa-miR-455-5p Axis-mediated High Expression of MTHFD2
            Correlates with Tumor Immune Infiltration and Endometrial Carcinoma
            Progression
  JOURNAL   Int J Med Sci 20 (8), 1097-1113 (2023)
   PUBMED   37484807
  REMARK    GeneRIF: SNHG3/hsa-miR-455-5p Axis-mediated High Expression of
            MTHFD2 Correlates with Tumor Immune Infiltration and Endometrial
            Carcinoma Progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Deng,X., Liu,X., Hu,B., Liu,J., Fu,B. and Zhang,W.
  TITLE     Upregulation of MTHFD2 is associated with PD-L1 activation in
            bladder cancer via the PI3K/AKT pathway
  JOURNAL   Int J Mol Med 51 (2) (2023)
   PUBMED   36601741
  REMARK    GeneRIF: Upregulation of MTHFD2 is associated with PDL1 activation
            in bladder cancer via the PI3K/AKT pathway.
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Di Pietro,E., Wang,X.L. and MacKenzie,R.E.
  TITLE     The expression of mitochondrial methylenetetrahydrofolate
            dehydrogenase-cyclohydrolase supports a role in rapid cell growth
  JOURNAL   Biochim Biophys Acta 1674 (1), 78-84 (2004)
   PUBMED   15342116
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Pawelek,P.D. and MacKenzie,R.E.
  TITLE     Methenyltetrahydrofolate cyclohydrolase is rate limiting for the
            enzymatic conversion of 10-formyltetrahydrofolate to
            5,10-methylenetetrahydrofolate in bifunctional
            dehydrogenase-cyclohydrolase enzymes
  JOURNAL   Biochemistry 37 (4), 1109-1115 (1998)
   PUBMED   9454603
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Kokame,K., Kato,H. and Miyata,T.
  TITLE     Homocysteine-respondent genes in vascular endothelial cells
            identified by differential display analysis. GRP78/BiP and novel
            genes
  JOURNAL   J Biol Chem 271 (47), 29659-29665 (1996)
   PUBMED   8939898
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Yang,X.M. and MacKenzie,R.E.
  TITLE     NAD-dependent methylenetetrahydrofolate
            dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the
            mammalian homolog of the mitochondrial enzyme encoded by the yeast
            MIS1 gene
  JOURNAL   Biochemistry 32 (41), 11118-11123 (1993)
   PUBMED   8218174
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Peri,K.G., Belanger,C. and Mackenzie,R.E.
  TITLE     Nucleotide sequence of the human NAD-dependent methylene
            tetrahydrofolate dehydrogenase-cyclohydrolase
  JOURNAL   Nucleic Acids Res 17 (21), 8853 (1989)
   PUBMED   2587219
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX475613.1, BC017054.1,
            CB124593.1 and AC073263.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 5, 2006 this sequence version replaced NP_006627.1.
            
            Summary: This gene encodes a nuclear-encoded mitochondrial
            bifunctional enzyme with methylenetetrahydrofolate dehydrogenase
            and methenyltetrahydrofolate cyclohydrolase activities. The enzyme
            functions as a homodimer and is unique in its absolute requirement
            for magnesium and inorganic phosphate. Formation of the
            enzyme-magnesium complex allows binding of NAD. Alternative
            splicing results in two different transcripts, one protein-coding
            and the other not protein-coding. This gene has a pseudogene on
            chromosome 7. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and is the protein-coding transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK130664.1, SRR1803612.261966.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000394053.7/
                                                  ENSP00000377617.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..350
                     /product="bifunctional methylenetetrahydrofolate
                     dehydrogenase/cyclohydrolase, mitochondrial isoform A
                     precursor"
                     /EC_number="3.5.4.9"
                     /EC_number="1.5.1.15"
                     /note="NAD-dependent methylene tetrahydrofolate
                     dehydrogenase cyclohydrolase; bifunctional
                     methylenetetrahydrofolate dehydrogenase/cyclohydrolase,
                     mitochondrial"
                     /calculated_mol_wt=34762
     transit_peptide 1..29
                     /calculated_mol_wt=3151
     mat_peptide     30..350
                     /product="bifunctional methylenetetrahydrofolate
                     dehydrogenase/cyclohydrolase, mitochondrial isoform A"
                     /calculated_mol_wt=34762
     Region          37..335
                     /region_name="FolD"
                     /note="5,10-methylene-tetrahydrofolate
                     dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase
                     [Coenzyme transport and metabolism]; COG0190"
                     /db_xref="CDD:439960"
     Site            50
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P13995.2)"
     CDS             1..350
                     /gene="MTHFD2"
                     /gene_synonym="NMDMC"
                     /coded_by="NM_006636.4:28..1080"
                     /note="isoform A precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1935.2"
                     /db_xref="GeneID:10797"
                     /db_xref="HGNC:HGNC:7434"
                     /db_xref="MIM:604887"
ORIGIN      
        1 maatslmsal aarllqpahs cslrlrpfhl aavrneavvi sgrklaqqik qevrqeveew
       61 vasgnkrphl svilvgenpa shsyvlnktr aaavvginse timkpasise eellnlinkl
      121 nnddnvdgll vqlplpehid erricnavsp dkdvdgfhvi nvgrmcldqy smlpatpwgv
      181 weiikrtgip tlgknvvvag rsknvgmpia mllhtdgahe rpggdatvti shrytpkeql
      241 kkhtiladiv isaagipnli tadmikegaa vidvginrvh dpvtakpklv gdvdfegvrq
      301 kagyitpvpg gvgpmtvaml mkntiiaakk vlrleerevl kskelgvatn
//
LOCUS       NP_055037                172 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8
            isoform 1 [Homo sapiens].
ACCESSION   NP_055037
VERSION     NP_055037.1
DBSOURCE    REFSEQ: accession NM_014222.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Xiang,H., Tang,H., He,Q., Sun,J., Yang,Y., Kong,L. and Wang,Y.
  TITLE     NDUFA8 is transcriptionally regulated by EP300/H3K27ac and promotes
            mitochondrial respiration to support proliferation and inhibit
            apoptosis in cervical cancer
  JOURNAL   Biochem Biophys Res Commun 693, 149374 (2024)
   PUBMED   38096616
  REMARK    GeneRIF: NDUFA8 is transcriptionally regulated by EP300/H3K27ac and
            promotes mitochondrial respiration to support proliferation and
            inhibit apoptosis in cervical cancer.
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Qiu,L., Sheng,P. and Wang,X.
  TITLE     Identification of Metabolic Syndrome-Related miRNA-mRNA Regulatory
            Networks and Key Genes Based on Bioinformatics Analysis
  JOURNAL   Biochem Genet 61 (1), 428-447 (2023)
   PUBMED   35877019
  REMARK    GeneRIF: Identification of Metabolic Syndrome-Related miRNA-mRNA
            Regulatory Networks and Key Genes Based on Bioinformatics Analysis.
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Tort,F., Barredo,E., Parthasarathy,R., Ugarteburu,O.,
            Ferrer-Cortes,X., Garcia-Villoria,J., Gort,L.,
            Gonzalez-Quintana,A., Martin,M.A., Fernandez-Vizarra,E., Zeviani,M.
            and Ribes,A.
  TITLE     Biallelic mutations in NDUFA8 cause complex I deficiency in two
            siblings with favorable clinical evolution
  JOURNAL   Mol Genet Metab 131 (3), 349-357 (2020)
   PUBMED   33153867
  REMARK    GeneRIF: Biallelic mutations in NDUFA8 cause complex I deficiency
            in two siblings with favorable clinical evolution.
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Triepels,R., van den Heuvel,L., Loeffen,J., Smeets,R., Trijbels,F.
            and Smeitink,J.
  TITLE     The nuclear-encoded human NADH:ubiquinone oxidoreductase NDUFA8
            subunit: cDNA cloning, chromosomal localization, tissue
            distribution, and mutation detection in complex-I-deficient
            patients
  JOURNAL   Hum Genet 103 (5), 557-563 (1998)
   PUBMED   9860297
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Smeitink,J., Loeffen,J., Smeets,R., Triepels,R., Ruitenbeek,W.,
            Trijbels,F. and van den Heuvel,L.
  TITLE     Molecular characterization and mutational analysis of the human B17
            subunit of the mitochondrial respiratory chain complex I
  JOURNAL   Hum Genet 103 (2), 245-250 (1998)
   PUBMED   9760212
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Emahazion,T., Beskow,A., Gyllensten,U. and Brookes,A.J.
  TITLE     Intron based radiation hybrid mapping of 15 complex I genes of the
            human electron transport chain
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 115-119 (1998)
   PUBMED   9763677
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Sarto,C., Marocchi,A., Sanchez,J.C., Giannone,D., Frutiger,S.,
            Golaz,O., Wilkins,M.R., Doro,G., Cappellano,F., Hughes,G.,
            Hochstrasser,D.F. and Mocarelli,P.
  TITLE     Renal cell carcinoma and normal kidney protein expression
  JOURNAL   Electrophoresis 18 (3-4), 599-604 (1997)
   PUBMED   9150947
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314135.1 and BC001016.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the complex I
            19 kDa subunit family. Mammalian complex I is composed of 45
            different subunits. This protein has NADH dehydrogenase activity
            and oxidoreductase activity. It plays an important role in
            transfering electrons from NADH to the respiratory chain. The
            immediate electron acceptor for the enzyme is believed to be
            ubiquinone. Alternative splicing of this gene results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.4286.1,
                                           SRR5189664.130104.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000373768.4/
                                                  ENSP00000362873.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.2"
     Protein         1..172
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 8 isoform 1"
                     /EC_number="7.1.1.2"
                     /EC_number="1.6.99.3"
                     /note="NADH-ubiquinone oxidoreductase 19 kDa subunit;
                     NADH:ubiquinone oxidoreductase PGIV subunit; NADH
                     dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;
                     complex I-19kD; complex I-PGIV; NADH dehydrogenase
                     (ubiquinone) 1 alpha subcomplex, 8, 19kDa"
                     /calculated_mol_wt=19974
     Region          36..46
                     /region_name="Cx9C motif 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (P51970.3)"
     Region          56..66
                     /region_name="Cx9C motif 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (P51970.3)"
     Region          78..111
                     /region_name="CHCH"
                     /note="CHCH domain; pfam06747"
                     /db_xref="CDD:429096"
     Region          78..88
                     /region_name="Cx9C motif 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (P51970.3)"
     Region          100..110
                     /region_name="Cx9C motif 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (P51970.3)"
     Region          133..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51970.3)"
     CDS             1..172
                     /gene="NDUFA8"
                     /gene_synonym="CI-19KD; CI-PGIV; MC1DN37; PGIV"
                     /coded_by="NM_014222.3:103..621"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6835.1"
                     /db_xref="GeneID:4702"
                     /db_xref="HGNC:HGNC:7692"
                     /db_xref="MIM:603359"
ORIGIN      
        1 mpgivelptl eelkvdevki ssavlkaaah hygaqcdkpn kefmlcrwee kdprrcleeg
       61 klvnkcaldf frqikrhcae pfteywtcid ytgqqlfrhc rkqqakfdec vldklgwvrp
      121 dlgelskvtk vktdrplpen pyhsrprpdp speiegdlqp athgsrfyfw tk
//
LOCUS       NP_001353457            1140 aa            linear   PRI 27-APR-2025
DEFINITION  plasma membrane calcium-transporting ATPase 1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001353457
VERSION     NP_001353457.1
DBSOURCE    REFSEQ: accession NM_001366528.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1140)
  AUTHORS   Kobayashi,Y., Yatsu,K., Haruna,A., Kawano,R., Ozawa,M., Haze,T.,
            Komiya,S., Suzuki,S., Ohki,Y., Fujiwara,A., Saka,S., Hirawa,N.,
            Toya,Y. and Tamura,K.
  TITLE     ATP2B1 gene polymorphisms associated with resistant hypertension in
            the Japanese population
  JOURNAL   J Clin Hypertens (Greenwich) 26 (4), 355-362 (2024)
   PUBMED   38430457
  REMARK    GeneRIF: ATP2B1 gene polymorphisms associated with resistant
            hypertension in the Japanese population.
REFERENCE   2  (residues 1 to 1140)
  AUTHORS   Gao,Y., Liu,Y., Jiang,Y., Qin,M., Guan,Z., Gao,Y. and Yang,Y.
  TITLE     Association between polymorphism and haplotype of ATP2B1 gene and
            skeletal fluorosis in Han population
  JOURNAL   Int J Environ Health Res 34 (3), 1410-1420 (2024)
   PUBMED   37211801
  REMARK    GeneRIF: Association between polymorphism and haplotype of ATP2B1
            gene and skeletal fluorosis in Han population.
REFERENCE   3  (residues 1 to 1140)
  AUTHORS   Berrocal,M. and Mata,A.M.
  TITLE     The Plasma Membrane Ca2+-ATPase, a Molecular Target for Tau-induced
            Cytosolic Calcium Dysregulation
  JOURNAL   Neuroscience 518, 112-118 (2023)
   PUBMED   35469971
  REMARK    GeneRIF: The Plasma Membrane Ca[2+]-ATPase, a Molecular Target for
            Tau-induced Cytosolic Calcium Dysregulation.
            Review article
REFERENCE   4  (residues 1 to 1140)
  AUTHORS   Yang,X., Lu,L., Wu,C. and Zhang,F.
  TITLE     ATP2B1-AS1 exacerbates sepsis-induced cell apoptosis and
            inflammation by regulating miR-23a-3p/TLR4 axis
  JOURNAL   Allergol Immunopathol (Madr) 51 (2), 17-26 (2023)
   PUBMED   36916084
  REMARK    GeneRIF: ATP2B1-AS1 exacerbates sepsis-induced cell apoptosis and
            inflammation by regulating miR-23a-3p/TLR4 axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1140)
  AUTHORS   Rahimi,M.J., Urban,N., Wegler,M., Sticht,H., Schaefer,M., Popp,B.,
            Gaunitz,F., Morleo,M., Nigro,V., Maitz,S., Mancini,G.M.S.,
            Ruivenkamp,C., Suk,E.K., Bartolomaeus,T., Merkenschlager,A.,
            Koboldt,D., Bartholomew,D., Stegmann,A.P.A., Sinnema,M.,
            Duynisveld,I., Salvarinova,R., Race,S., de Vries,B.B.A.,
            Trimouille,A., Naudion,S., Marom,D., Hamiel,U., Henig,N.,
            Demurger,F., Rahner,N., Bartels,E., Hamm,J.A., Putnam,A.M.,
            Person,R., Abou Jamra,R. and Oppermann,H.
  TITLE     De novo variants in ATP2B1 lead to neurodevelopmental delay
  JOURNAL   Am J Hum Genet 109 (5), 944-952 (2022)
   PUBMED   35358416
  REMARK    GeneRIF: De novo variants in ATP2B1 lead to neurodevelopmental
            delay.
REFERENCE   6  (residues 1 to 1140)
  AUTHORS   Kessler,F., Falchetto,R., Heim,R., Meili,R., Vorherr,T.,
            Strehler,E.E. and Carafoli,E.
  TITLE     Study of calmodulin binding to the alternatively spliced C-terminal
            domain of the plasma membrane Ca2+ pump
  JOURNAL   Biochemistry 31 (47), 11785-11792 (1992)
   PUBMED   1332771
REFERENCE   7  (residues 1 to 1140)
  AUTHORS   Wang,K.K., Wright,L.C., Machan,C.L., Allen,B.G., Conigrave,A.D. and
            Roufogalis,B.D.
  TITLE     Protein kinase C phosphorylates the carboxyl terminus of the plasma
            membrane Ca(2+)-ATPase from human erythrocytes
  JOURNAL   J Biol Chem 266 (14), 9078-9085 (1991)
   PUBMED   1827443
REFERENCE   8  (residues 1 to 1140)
  AUTHORS   Olson,S., Wang,M.G., Carafoli,E., Strehler,E.E. and McBride,O.W.
  TITLE     Localization of two genes encoding plasma membrane
            Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and
            12q21-23
  JOURNAL   Genomics 9 (4), 629-641 (1991)
   PUBMED   1674727
REFERENCE   9  (residues 1 to 1140)
  AUTHORS   Strehler,E.E., Strehler-Page,M.A., Vogel,G. and Carafoli,E.
  TITLE     mRNAs for plasma membrane calcium pump isoforms differing in their
            regulatory domain are generated by alternative splicing that
            involves two internal donor sites in a single exon
  JOURNAL   Proc Natl Acad Sci U S A 86 (18), 6908-6912 (1989)
   PUBMED   2528729
REFERENCE   10 (residues 1 to 1140)
  AUTHORS   James,P.H., Pruschy,M., Vorherr,T.E., Penniston,J.T. and
            Carafoli,E.
  TITLE     Primary structure of the cAMP-dependent phosphorylation site of the
            plasma membrane calcium pump
  JOURNAL   Biochemistry 28 (10), 4253-4258 (1989)
   PUBMED   2548572
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009522.11, AC068641.18 and
            AC025034.22.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type primary ion transport ATPases characterized by the formation
            of an aspartyl phosphate intermediate during the reaction cycle.
            These enzymes remove bivalent calcium ions from eukaryotic cells
            against very large concentration gradients and play a critical role
            in intracellular calcium homeostasis. The mammalian plasma membrane
            calcium ATPase isoforms are encoded by at least four separate genes
            and the diversity of these enzymes is further increased by
            alternative splicing of transcripts. The expression of different
            isoforms and splice variants is regulated in a developmental,
            tissue- and cell type-specific manner, suggesting that these pumps
            are functionally adapted to the physiological needs of particular
            cells and tissues. This gene encodes the plasma membrane calcium
            ATPase isoform 1. Alternatively spliced transcript variants
            encoding different isoforms have been identified. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.252185.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.33"
     Protein         1..1140
                     /product="plasma membrane calcium-transporting ATPase 1
                     isoform 4"
                     /EC_number="7.2.2.10"
                     /note="plasma membrane calcium pump; ATPase, Ca++
                     transporting, plasma membrane 1; plasma membrane
                     calcium-transporting ATPase 1"
                     /calculated_mol_wt=125318
     Region          15..1023
                     /region_name="ATPase-IIB_Ca"
                     /note="plasma-membrane calcium-translocating P-type
                     ATPase; TIGR01517"
                     /db_xref="CDD:273668"
     Region          1067..1106
                     /region_name="ATP_Ca_trans_C"
                     /note="Plasma membrane calcium transporter ATPase C
                     terminal; pfam12424"
                     /db_xref="CDD:463575"
     CDS             1..1140
                     /gene="ATP2B1"
                     /gene_synonym="MRD66; PMCA1; PMCA1kb"
                     /coded_by="NM_001366528.1:370..3792"
                     /note="isoform 4 is encoded by transcript variant 11"
                     /db_xref="GeneID:490"
                     /db_xref="HGNC:HGNC:814"
                     /db_xref="MIM:108731"
ORIGIN      
        1 mgdmannsva ysgvknslke anhdgdfgit laelralmel rstdalrkiq esygdvygic
       61 tklktspneg lsgnpadler reavfgknfi ppkkpktflq lvwealqdvt liileiaaiv
      121 slglsfyqpp egdnalcgev svgeeegege tgwiegaail lsvvcvvlvt afndwskekq
      181 frglqsrieq eqkftvirgg qviqipvadi tvgdiaqvky gdllpadgil iqgndlkide
      241 ssltgesdhv kksldkdpll lsgthvmegs grmvvtavgv nsqtgiiftl lgaggeeeek
      301 kdekkkekkn kkqdgaienr nkakaqdgaa memqplksee ggdgdekdkk kanlpkkeks
      361 vlqgkltkla vqigkagllm saitviilvl yfvidtfwvq krpwlaectp iyiqyfvkff
      421 iigvtvlvva vpeglplavt islaysvkkm mkdnnlvrhl dacetmgnat aicsdktgtl
      481 tmnrmtvvqa yinekhykkv pepeaippni lsylvtgisv ncaytskilp pekegglprh
      541 vgnktecall gllldlkrdy qdvrneipee alykvytfns vrksmstvlk nsdgsyrifs
      601 kgaseiilkk cfkilsange akvfrprdrd divktviepm aseglrticl afrdfpagep
      661 epewdnendi vtgltciavv giedpvrpev pdaikkcqra gitvrmvtgd nintaraiat
      721 kcgilhpged flclegkdfn rrirnekgei eqeridkiwp klrvlarssp tdkhtlvkgi
      781 idstvsdqrq vvavtgdgtn dgpalkkadv gfamgiagtd vakeasdiil tddnftsivk
      841 avmwgrnvyd siskflqfql tvnvvaviva ftgacitqds plkavqmlwv nlimdtlasl
      901 alatepptes lllrkpygrn kplisrtmmk nilghafyql vvvftllfag ekffdidsgr
      961 naplhappse hytivfntfv lmqlfneina rkihgernvf egifnnaifc tivlgtfvvq
     1021 listiptsrl kflkeaghgt qkeeipeeel aedveeidha erelrrgqil wfrglnriqt
     1081 qmdvvnafqs gssiqgalrr qpsiasqhhd vtnistpthv vfssstastt vgyssgecis
//
LOCUS       NP_001347949             617 aa            linear   ROD 27-APR-2025
DEFINITION  D-glutamate cyclase, mitochondrial isoform 2 precursor [Mus
            musculus].
ACCESSION   NP_001347949 XP_006515800
VERSION     NP_001347949.1
DBSOURCE    REFSEQ: accession NM_001361020.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Ariyoshi,M., Katane,M., Hamase,K., Miyoshi,Y., Nakane,M.,
            Hoshino,A., Okawa,Y., Mita,Y., Kaimoto,S., Uchihashi,M., Fukai,K.,
            Ono,K., Tateishi,S., Hato,D., Yamanaka,R., Honda,S., Fushimura,Y.,
            Iwai-Kanai,E., Ishihara,N., Mita,M., Homma,H. and Matoba,S.
  TITLE     D-Glutamate is metabolized in the heart mitochondria
  JOURNAL   Sci Rep 7, 43911 (2017)
   PUBMED   28266638
  REMARK    GeneRIF: Further analysis of D-glutamate metabolism indicated that
            9030617O03Rik is a D-glutamate cyclase that converts D-glutamate to
            5-oxo-D-proline.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Nishimura,M., Yokoi,N., Miki,T., Horikawa,Y., Yoshioka,H.,
            Takeda,J., Ohara,O. and Seino,S.
  TITLE     Construction of a multi-functional cDNA library specific for mouse
            pancreatic islets and its application to microarray
  JOURNAL   DNA Res 11 (5), 315-323 (2004)
   PUBMED   15747579
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC159818.2 and AC126262.4.
            
            On Feb 27, 2018 this sequence version replaced XP_006515800.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 1.  The encoded isoform
            (2) has a shorter N-terminus than isoform 1. Both variants 2 and 3
            encode the same isoform (2).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC066161.1, SRR13948564.2401208.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 28266638; reported by
                                                  MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 51.1 cM"
     Protein         1..617
                     /product="D-glutamate cyclase, mitochondrial isoform 2
                     precursor"
                     /EC_number="4.2.1.48"
                     /note="UPF0317 protein C14orf159 homolog, mitochondrial;
                     D-glutamate cyclase, mitochondrial"
                     /calculated_mol_wt=63467
     transit_peptide 1..26
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q8BH86.1)"
                     /calculated_mol_wt=2918
     mat_peptide     27..617
                     /product="D-glutamate cyclase, mitochondrial.
                     /id=PRO_0000036293"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH86.1)"
                     /calculated_mol_wt=63467
     Site            93
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q8BH86.1)"
     Region          115..255
                     /region_name="D-Glu_cyclase"
                     /note="D-glutamate cyclase; pfam07286"
                     /db_xref="CDD:462133"
     Region          299..610
                     /region_name="DUF4392"
                     /note="Domain of unknown function (DUF4392); pfam14336"
                     /db_xref="CDD:464140"
     CDS             1..617
                     /gene="Dglucy"
                     /gene_synonym="9030617O03Rik"
                     /coded_by="NM_001361020.1:342..2195"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS26108.1"
                     /db_xref="GeneID:217830"
                     /db_xref="MGI:MGI:2444813"
ORIGIN      
        1 mtisfllrsc lrsavrslpk aalirntssm teglqpasvv vlprslapaf esfcqgnrgp
       61 lpllgqseav ktlpqlsavs dirticpqlq kykfgtctgi ltsleehseq lkemvtfiid
      121 csfsieeale qagiprrdlt gpshagaykt tvpcatiagf ccplvvtmrp ipkdklerll
      181 qathairgqq gqpihigdpg llgiealskp dygsyvecrp edvpvfwpsp ltsleavisc
      241 kaplafaspp gcmvmvpkdt assascltpe mvpevhaisk dplhysivsa paaqkvrele
      301 stiavdpgnr gighlllkde llqaalslsh arsvlvttgf pthfnheppe etdgppgaia
      361 laaflqalgk etamvvdqra lnlhmrived airqgvlktp ipiltyqgrs medaraflck
      421 dgdpksprfd hlvaieragr aadgnyynar kmnikhlvdp iddiflaaqk ipgisstgvg
      481 dggnelgmgk vkaavkkhir ngdviacdve adfaviagvs nwggyalaca lyilnscqvh
      541 erylrratgp srrageqswi qalpsvakee kmlgilvenq vrsgvsgivg mevdglpfhd
      601 vhaemirklv gattvhm
//
LOCUS       NP_001020262             845 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-binding cassette sub-family F member 1 isoform a [Homo
            sapiens].
ACCESSION   NP_001020262
VERSION     NP_001020262.1
DBSOURCE    REFSEQ: accession NM_001025091.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 845)
  AUTHORS   Yin,X., Xia,K., Peng,S., Tan,B., Huang,Y., Wang,M. and He,M.
  TITLE     ABCF1/CXCL12/CXCR4 Enhances Glioblastoma Cell Proliferation,
            Migration, and Invasion by Activating the PI3K/AKT Signal Pathway
  JOURNAL   Dev Neurosci 46 (3), 210-220 (2024)
   PUBMED   37757768
  REMARK    GeneRIF: ABCF1/CXCL12/CXCR4 Enhances Glioblastoma Cell
            Proliferation, Migration, and Invasion by Activating the PI3K/AKT
            Signal Pathway.
REFERENCE   2  (residues 1 to 845)
  AUTHORS   Choi,E.B., Vodnala,M., Zerbato,M., Wang,J., Ho,J.J., Inouye,C.,
            Ding,L. and Fong,Y.W.
  TITLE     ATP-binding cassette protein ABCF1 couples transcription and genome
            surveillance in embryonic stem cells through low-complexity domain
  JOURNAL   Sci Adv 7 (44), eabk2775 (2021)
   PUBMED   34714667
  REMARK    GeneRIF: ABCF1 functions as a transcriptional coactivator for OCT4
            and SOX2 to stimulate transciption of pluripotency-associated genes
            in embryonic stem cells.
REFERENCE   3  (residues 1 to 845)
  AUTHORS   Fassler,J.S., Skuodas,S., Weeks,D.L. and Phillips,B.T.
  TITLE     Protein Aggregation and Disaggregation in Cells and Development
  JOURNAL   J Mol Biol 433 (21), 167215 (2021)
   PUBMED   34450138
  REMARK    Review article
REFERENCE   4  (residues 1 to 845)
  AUTHORS   Cao,Q.T., Aguiar,J.A., Tremblay,B.J., Abbas,N., Tiessen,N.,
            Revill,S., Makhdami,N., Ayoub,A., Cox,G., Ask,K., Doxey,A.C. and
            Hirota,J.A.
  TITLE     ABCF1 Regulates dsDNA-induced Immune Responses in Human Airway
            Epithelial Cells
  JOURNAL   Front Cell Infect Microbiol 10, 487 (2020)
   PUBMED   33042865
  REMARK    GeneRIF: ABCF1 Regulates dsDNA-induced Immune Responses in Human
            Airway Epithelial Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 845)
  AUTHORS   Fung,S.W., Cheung,P.F., Yip,C.W., Ng,L.W., Cheung,T.T., Chong,C.C.,
            Lee,C., Lai,P.B., Chan,A.W., Tsao,G.S., Wong,C.H., Chan,S.L.,
            Lo,K.W. and Cheung,S.T.
  TITLE     The ATP-binding cassette transporter ABCF1 is a hepatic oncofetal
            protein that promotes chemoresistance, EMT and cancer stemness in
            hepatocellular carcinoma
  JOURNAL   Cancer Lett 457, 98-109 (2019)
   PUBMED   31100412
  REMARK    GeneRIF: The ATP-binding cassette transporter ABCF1 is a hepatic
            oncofetal protein that promotes chemoresistance, epithelial
            mesenchymal transformation and cancer stemness in hepatocellular
            carcinoma cells.
REFERENCE   6  (residues 1 to 845)
  AUTHORS   Qu,L., Jiang,Y., Cheng,C., Wu,D., Meng,B., Chen,Z., Zhu,Y.,
            Shaw,N., Ouyang,S. and Liu,Z.J.
  TITLE     Crystal Structure of ATP-Bound Human ABCF1 Demonstrates a Unique
            Conformation of ABC Proteins
  JOURNAL   Structure 26 (9), 1259-1265 (2018)
   PUBMED   30017566
  REMARK    GeneRIF: Study solves the crystal structure of an ATP-bound
            wild-type human ABCF1 at 2.3-A resolution. The comparative studies
            indicate that the structure is in a pre-activation intermediate
            conformation. This conformation is stabilized by the interaction
            between ATP and protein suggesting that this conformation is an
            important step in the activation of ABCF1.
REFERENCE   7  (residues 1 to 845)
  AUTHORS   Mancarella,C., Pasello,M., Ventura,S., Grilli,A., Calzolari,L.,
            Toracchio,L., Lollini,P.L., Donati,D.M., Picci,P., Ferrari,S. and
            Scotlandi,K.
  TITLE     Insulin-Like Growth Factor 2 mRNA-Binding Protein 3 is a Novel
            Post-Transcriptional Regulator of Ewing Sarcoma Malignancy
  JOURNAL   Clin Cancer Res 24 (15), 3704-3716 (2018)
   PUBMED   29703820
  REMARK    GeneRIF: The combined assessment of IGF2BP3 and ABCF1 predicts
            recurrence in Ewing sarcoma patients.
REFERENCE   8  (residues 1 to 845)
  AUTHORS   Klein,I., Sarkadi,B. and Varadi,A.
  TITLE     An inventory of the human ABC proteins
  JOURNAL   Biochim Biophys Acta 1461 (2), 237-262 (1999)
   PUBMED   10581359
  REMARK    Review article
REFERENCE   9  (residues 1 to 845)
  AUTHORS   Richard,M., Drouin,R. and Beaulieu,A.D.
  TITLE     ABC50, a novel human ATP-binding cassette protein found in tumor
            necrosis factor-alpha-stimulated synoviocytes
  JOURNAL   Genomics 53 (2), 137-145 (1998)
   PUBMED   9790762
REFERENCE   10 (residues 1 to 845)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI547952.1, BC034488.2,
            AF027302.1, BM556481.1 and BU620927.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the GCN20 subfamily. Unlike other members of
            the superfamily, this protein lacks the transmembrane domains which
            are characteristic of most ABC transporters. This protein may be
            regulated by tumor necrosis factor-alpha and play a role in
            enhancement of protein synthesis and the inflammation process.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC112923.1, SRR1803615.5546.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326195.13/ ENSP00000313603.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..845
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..845
                     /product="ATP-binding cassette sub-family F member 1
                     isoform a"
                     /note="ATP-binding cassette 50 (TNF-alpha stimulated);
                     TNFalpha-inducible ATP-binding protein;
                     TNF-alpha-stimulated ABC protein; ATP-binding cassette,
                     sub-family F (GCN20), member 1"
                     /calculated_mol_wt=95795
     Region          1..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NE71.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NE71.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NE71.2)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NE71.2)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NE71.2)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:17894550,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NE71.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:17894550,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NE71.2)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NE71.2)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NE71.2)"
     Region          306..829
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          559..602
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NE71.2)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NE71.2)"
     CDS             1..845
                     /gene="ABCF1"
                     /gene_synonym="ABC27; ABC50"
                     /coded_by="NM_001025091.2:47..2584"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34380.1"
                     /db_xref="GeneID:23"
                     /db_xref="HGNC:HGNC:70"
                     /db_xref="MIM:603429"
ORIGIN      
        1 mpkapkqqpp epewigdges tspsdkvvkk gkkdkkikkt ffeelavedk qageeekvlk
       61 ekeqqqqqqq qqqkkkrdtr kgrrkkdvdd dgeekelmer lkklsvptsd eedevpapkp
      121 rggkktkggn vfaaliqdqs eeeeeeekhp pkpakpeknr inkavseeqq palkgkkgke
      181 ekskgkakpq nkfaaldnee edkeeeiike keppkqgkek akkaeqgsee egegeeeeee
      241 ggeskaddpy ahlskkekkk lkkqmeyerq vaslkaanaa endfsvsqae mssrqamlen
      301 asdiklekfs isahgkelfv nadlyivagr ryglvgpngk gkttllkhia nralsippni
      361 dvllceqevv adetpavqav lradtkrlkl leeerrlqgq leqgddtaae rlekvyeelr
      421 atgaaaaeak arrilaglgf dpemqnrptq kfsggwrmrv slaralfmep tllmldeptn
      481 hldlnaviwl nnylqgwrkt llivshdqgf lddvctdiih ldaqrlhyyr gnymtfkkmy
      541 qqkqkellkq yekqekklke lkaggkstkq aekqtkealt rkqqkcrrkn qdeesqeape
      601 llkrpkeytv rftfpdpppl sppvlglhgv tfgyqgqkpl fknldfgidm dsricivgpn
      661 gvgkstllll ltgkltpthg emrknhrlki gffnqqyaeq lrmeetptey lqrgfnlpyq
      721 darkclgrfg leshahtiqi cklsggqkar vvfaelacre pdvlildept nnldiesida
      781 lgeaineykg avivvshdar litetncqlw vveeqsvsqi dgdfedykre vlealgevmv
      841 srpre
//
LOCUS       NP_001632                318 aa            linear   PRI 27-APR-2025
DEFINITION  DNA repair nuclease/redox regulator APEX1 [Homo sapiens].
ACCESSION   NP_001632
VERSION     NP_001632.2
DBSOURCE    REFSEQ: accession NM_001641.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Vemulapalli,S., Hashemi,M., Chen,Y., Pramanik,S., Bhakat,K.K. and
            Lyubchenko,Y.L.
  TITLE     Nanoscale Interaction of Endonuclease APE1 with DNA
  JOURNAL   Int J Mol Sci 25 (10), 5145 (2024)
   PUBMED   38791183
  REMARK    GeneRIF: Nanoscale Interaction of Endonuclease APE1 with DNA.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Cao,X., Zheng,J., Zhang,R., Sun,Y. and Zhao,M.
  TITLE     Live-cell imaging of human apurinic/apyrimidinic endonuclease 1 in
            the nucleus and nucleolus using a chaperone@DNA probe
  JOURNAL   Nucleic Acids Res 52 (8), e41 (2024)
   PUBMED   38554110
  REMARK    GeneRIF: Live-cell imaging of human apurinic/apyrimidinic
            endonuclease 1 in the nucleus and nucleolus using a chaperone@DNA
            probe.
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Du,Y., Zhou,Y., Yan,X., Pan,F., He,L., Guo,Z. and Hu,Z.
  TITLE     APE1 inhibition enhances ferroptotic cell death and contributes to
            hepatocellular carcinoma therapy
  JOURNAL   Cell Death Differ 31 (4), 431-446 (2024)
   PUBMED   38418695
  REMARK    GeneRIF: APE1 inhibition enhances ferroptotic cell death and
            contributes to hepatocellular carcinoma therapy.
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Mao,S., Xie,C., Liu,Y., Zhao,Y., Li,M., Gao,H., Xiao,Y., Zou,Y.,
            Zheng,Z., Gao,Y., Xie,J., Tian,B., Wang,L., Hua,Y. and Xu,H.
  TITLE     Apurinic/apyrimidinic endodeoxyribonuclease 1 (APE1) promotes
            stress granule formation via YBX1 phosphorylation in ovarian cancer
  JOURNAL   Cell Mol Life Sci 81 (1), 113 (2024)
   PUBMED   38436697
  REMARK    GeneRIF: Apurinic/apyrimidinic endodeoxyribonuclease 1 (APE1)
            promotes stress granule formation via YBX1 phosphorylation in
            ovarian cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Rostami,M., Yalin,S.F., Altiparmak,M.R. and Guven,M.
  TITLE     Investigation of APE1 and OGG1 expression in chronic hemodialysis
            patients
  JOURNAL   Mol Biol Rep 51 (1), 144 (2024)
   PUBMED   38236479
  REMARK    GeneRIF: Investigation of APE1 and OGG1 expression in chronic
            hemodialysis patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Harrison,L., Ascione,G., Menninger,J.C., Ward,D.C. and Demple,B.
  TITLE     Human apurinic endonuclease gene (APE): structure and genomic
            mapping (chromosome 14q11.2-12)
  JOURNAL   Hum Mol Genet 1 (9), 677-680 (1992)
   PUBMED   1284593
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Robson,C.N., Hochhauser,D., Craig,R., Rack,K., Buckle,V.J. and
            Hickson,I.D.
  TITLE     Structure of the human DNA repair gene HAP1 and its localisation to
            chromosome 14q 11.2-12
  JOURNAL   Nucleic Acids Res 20 (17), 4417-4421 (1992)
   PUBMED   1383925
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Xanthoudakis,S., Miao,G., Wang,F., Pan,Y.C. and Curran,T.
  TITLE     Redox activation of Fos-Jun DNA binding activity is mediated by a
            DNA repair enzyme
  JOURNAL   EMBO J 11 (9), 3323-3335 (1992)
   PUBMED   1380454
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Zhao,B., Grandy,D.K., Hagerup,J.M., Magenis,R.E., Smith,L.,
            Chauhan,B.C. and Henner,W.D.
  TITLE     The human gene for apurinic/apyrimidinic endonuclease (HAP1):
            sequence and localization to chromosome 14 band q12
  JOURNAL   Nucleic Acids Res 20 (15), 4097-4098 (1992)
   PUBMED   1380694
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Cheng,X.B., Bunville,J. and Patterson,T.A.
  TITLE     Nucleotide sequence of a cDNA for an apurinic/apyrimidinic
            endonuclease from HeLa cells
  JOURNAL   Nucleic Acids Res 20 (2), 370 (1992)
   PUBMED   1371347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK291100.1 and AI554786.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 25, 2002 this sequence version replaced NP_001632.1.
            
            Summary: The APEX gene encodes the major AP endonuclease in human
            cells. It encodes the APEX endonuclease, a DNA repair enzyme with
            apurinic/apyrimidinic (AP) activity. Such AP activity sites occur
            frequently in DNA molecules by spontaneous hydrolysis, by DNA
            damaging agents or by DNA glycosylases that remove specific
            abnormal bases. The AP sites are the most frequent pre-mutagenic
            lesions that can prevent normal DNA replication. Splice variants
            have been found for this gene; all encode the same protein.
            Disruptions in the biological functions related to APEX are
            associated with many various malignancies and neurodegenerative
            diseases.[provided by RefSeq, Dec 2019].
            
            Transcript Variant: This variant (1) contains the full-length first
            exon and is the longest transcript.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.441507.1,
                                           SRR3476690.1071603.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000216714.8/
                                                  ENSP00000216714.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..318
                     /product="DNA repair nuclease/redox regulator APEX1"
                     /EC_number="3.1.11.2"
                     /note="AP endonuclease class I; deoxyribonuclease
                     (apurinic or apyrimidinic); AP lyase; DNA-(apurinic or
                     apyrimidinic site) lyase; apurinic/apyrimidinic (abasic)
                     endonuclease; protein REF-1; apurinic-apyrimidinic
                     endonuclease 1; redox factor-1; APEX nuclease
                     (multifunctional DNA repair enzyme) 1; DNA-(apurinic or
                     apyrimidinic site) endonuclease"
                     /calculated_mol_wt=35423
     Region          1..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
     Region          2..33
                     /region_name="Necessary for interaction with YBX1, binding
                     to RNA, NPM1-dependent association with rRNA,
                     endoribonuclease activity on abasic RNA and localization
                     in the nucleoli. /evidence=ECO:0000269|PubMed:18809583"
                     /note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000269|PubMed:14633989; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000269|PubMed:14633989; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Region          8..13
                     /region_name="Nuclear localization signal (NLS)"
                     /note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
     Region          23..33
                     /region_name="Necessary for interaction with NPM1 and for
                     efficient rRNA binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
     Site            27
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:20699270; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Site            31..32
                     /site_type="cleavage"
                     /note="Cleavage, by granzyme A; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Site            31
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:20699270; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     mat_peptide     32..318
                     /product="DNA repair nuclease/redox regulator APEX1,
                     mitochondrial. /evidence=ECO:0000250. /id=PRO_0000402572"
                     /note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
                     /calculated_mol_wt=32245
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:20699270; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:20699270; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Region          62..316
                     /region_name="Ape1-like_AP-endo"
                     /note="Human Ape1-like subfamily of the ExoIII family
                     apurinic/apyrimidinic (AP) endonucleases; cd09087"
                     /db_xref="CDD:197321"
     Region          64..80
                     /region_name="Nuclear export signal (NES)"
                     /note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
     Site            order(68,70..74,78,96,98,103,127..128,171,174,210,212,222,
                     224,226,229..230,266,268..270,276,278,280,282..283,309)
                     /site_type="active"
                     /db_xref="CDD:197321"
     Site            order(68,70..74,78,96,98,103,127..128,171,174,210,212,222,
                     224,226,229..230,266,268..270,276,278,280,282,309)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:197321"
     Site            order(68,96,171,174,210,212,309)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197321"
     Site            order(68,96,171,210,212,283,308..309)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197321"
     Site            order(70,96,308)
                     /site_type="metal-binding"
                     /note="metal binding site A [ion binding]"
                     /db_xref="CDD:197321"
     Site            order(171,174,210,212,230,266,280,282,309)
                     /site_type="other"
                     /note="AP binding site [nucleotide binding]"
                     /db_xref="CDD:197321"
     Site            197
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Site            order(210,212,309)
                     /site_type="metal-binding"
                     /note="metal binding site B [ion binding]"
                     /db_xref="CDD:197321"
     Site            212
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000269|PubMed:8932375; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK5.
                     /evidence=ECO:0000250|UniProtKB:P28352; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Site            283
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000269|PubMed:21762700,
                     ECO:0000269|PubMed:9804799; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     Region          289..318
                     /region_name="Mitochondrial targeting sequence (MTS)"
                     /note="propagated from UniProtKB/Swiss-Prot (P27695.2)"
     Site            309
                     /site_type="other"
                     /note="Interaction with DNA substrate; propagated from
                     UniProtKB/Swiss-Prot (P27695.2)"
     CDS             1..318
                     /gene="APEX1"
                     /gene_synonym="APE; APE1; APEN; APEX; APX; HAP1; REF1"
                     /coded_by="NM_001641.4:238..1194"
                     /db_xref="CCDS:CCDS9550.1"
                     /db_xref="GeneID:328"
                     /db_xref="HGNC:HGNC:587"
                     /db_xref="MIM:107748"
ORIGIN      
        1 mpkrgkkgav aedgdelrte peakksktaa kkndkeaage gpalyedppd qktspsgkpa
       61 tlkicswnvd glrawikkkg ldwvkeeapd ilclqetkcs enklpaelqe lpglshqyws
      121 apsdkegysg vgllsrqcpl kvsygigdee hdqegrviva efdsfvlvta yvpnagrglv
      181 rleyrqrwde afrkflkgla srkplvlcgd lnvaheeidl rnpkgnkkna gftpqerqgf
      241 gellqavpla dsfrhlypnt pyaytfwtym mnarsknvgw rldyfllshs llpalcdski
      301 rskalgsdhc pitlylal
//
LOCUS       NP_005594               1251 aa            linear   PRI 27-APR-2025
DEFINITION  phospholipid-transporting ATPase IC isoform 1 [Homo sapiens].
ACCESSION   NP_005594
VERSION     NP_005594.2
DBSOURCE    REFSEQ: accession NM_005603.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1251)
  AUTHORS   Dieudonne,T., Kummerer,F., Laursen,M.J., Stock,C., Flygaard,R.K.,
            Khalid,S., Lenoir,G., Lyons,J.A., Lindorff-Larsen,K. and Nissen,P.
  TITLE     Activation and substrate specificity of the human P4-ATPase ATP8B1
  JOURNAL   Nat Commun 14 (1), 7492 (2023)
   PUBMED   37980352
  REMARK    GeneRIF: Activation and substrate specificity of the human
            P4-ATPase ATP8B1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1251)
  AUTHORS   Chen,L.C., Huang,S.P., Shih,C.T., Li,C.Y., Chen,Y.T., Huang,C.Y.,
            Yu,C.C., Lin,V.C., Lee,C.H., Geng,J.H. and Bao,B.Y.
  TITLE     ATP8B1: A prognostic prostate cancer biomarker identified via
            genetic analysis
  JOURNAL   Prostate 83 (6), 602-611 (2023)
   PUBMED   36794287
  REMARK    GeneRIF: ATP8B1: A prognostic prostate cancer biomarker identified
            via genetic analysis.
REFERENCE   3  (residues 1 to 1251)
  AUTHORS   Gomez-Mellado,V.E., Chang,J.C., Ho-Mok,K.S., Bernardino
            Morcillo,C., Kersten,R.H.J., Oude Elferink,R.P.J., Verhoeven,A.J.
            and Paulusma,C.C.
  TITLE     ATP8B1 Deficiency Results in Elevated Mitochondrial
            Phosphatidylethanolamine Levels and Increased Mitochondrial
            Oxidative Phosphorylation in Human Hepatoma Cells
  JOURNAL   Int J Mol Sci 23 (20), 12344 (2022)
   PUBMED   36293199
  REMARK    GeneRIF: ATP8B1 Deficiency Results in Elevated Mitochondrial
            Phosphatidylethanolamine Levels and Increased Mitochondrial
            Oxidative Phosphorylation in Human Hepatoma Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1251)
  AUTHORS   Nayagam,J.S., Foskett,P., Strautnieks,S., Agarwal,K., Miquel,R.,
            Joshi,D. and Thompson,R.J.
  TITLE     Clinical phenotype of adult-onset liver disease in patients with
            variants in ABCB4, ABCB11, and ATP8B1
  JOURNAL   Hepatol Commun 6 (10), 2654-2664 (2022)
   PUBMED   35894240
  REMARK    GeneRIF: Clinical phenotype of adult-onset liver disease in
            patients with variants in ABCB4, ABCB11, and ATP8B1.
REFERENCE   5  (residues 1 to 1251)
  AUTHORS   Bull,L.N., van Eijk,M.J., Pawlikowska,L., DeYoung,J.A., Juijn,J.A.,
            Liao,M., Klomp,L.W., Lomri,N., Berger,R., Scharschmidt,B.F.,
            Knisely,A.S., Houwen,R.H. and Freimer,N.B.
  TITLE     A gene encoding a P-type ATPase mutated in two forms of hereditary
            cholestasis
  JOURNAL   Nat Genet 18 (3), 219-224 (1998)
   PUBMED   9500542
REFERENCE   6  (residues 1 to 1251)
  AUTHORS   Carlton,V.E., Knisely,A.S. and Freimer,N.B.
  TITLE     Mapping of a locus for progressive familial intrahepatic
            cholestasis (Byler disease) to 18q21-q22, the benign recurrent
            intrahepatic cholestasis region
  JOURNAL   Hum Mol Genet 4 (6), 1049-1053 (1995)
   PUBMED   7655458
REFERENCE   7  (residues 1 to 1251)
  AUTHORS   Houwen,R.H., Baharloo,S., Blankenship,K., Raeymaekers,P., Juyn,J.,
            Sandkuijl,L.A. and Freimer,N.B.
  TITLE     Genome screening by searching for shared segments: mapping a gene
            for benign recurrent intrahepatic cholestasis
  JOURNAL   Nat Genet 8 (4), 380-386 (1994)
   PUBMED   7894490
REFERENCE   8  (residues 1 to 1251)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
REFERENCE   9  (residues 1 to 1251)
  AUTHORS   Bull,L.N., Morotti,R. and Squires,J.E.
  TITLE     ATP8B1 Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301474
REFERENCE   10 (residues 1 to 1251)
  AUTHORS   Clayton,R.J., Iber,F.L., Ruebner,B.H. and McKusick,V.A.
  TITLE     Byler disease. Fatal familial intrahepatic cholestasis in an Amish
            kindred
  JOURNAL   Am J Dis Child 117 (1), 112-124 (1969)
   PUBMED   5762004
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022724.8 and AC027097.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 4, 2018 this sequence version replaced NP_005594.1.
            
            Summary: This gene encodes a member of the P-type cation transport
            ATPase family, which belongs to the subfamily of
            aminophospholipid-transporting ATPases. The aminophospholipid
            translocases transport phosphatidylserine and
            phosphatidylethanolamine from one side of a bilayer to another.
            Mutations in this gene may result in progressive familial
            intrahepatic cholestasis type 1 and in benign recurrent
            intrahepatic cholestasis. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF038007.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.31"
     Protein         1..1251
                     /product="phospholipid-transporting ATPase IC isoform 1"
                     /EC_number="7.6.2.1"
                     /note="ATPase, class I, type 8B, member 1;
                     phospholipid-transporting ATPase IC; E1-E2 ATPase;
                     probable phospholipid-transporting ATPase IC; familial
                     intrahepatic cholestasis type 1; ATPase, aminophospholipid
                     transporter, class I, type 8B, member 1; P4-ATPase
                     flippase complex alpha subunit ATP8B1"
                     /calculated_mol_wt=143565
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Region          94..1051
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            109..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Site            137..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Site            341..362
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Site            390..411
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Site            order(454..456,596,619..621,685,732..734,867,870,873,893,
                     896)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            950..970
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Region          <959..>1171
                     /region_name="DUF2339"
                     /note="Predicted membrane protein (DUF2339); pfam10101"
                     /db_xref="CDD:431054"
     Site            983..1002
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Site            1033..1054
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Site            1069..1091
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Site            1098..1118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Site            1139..1163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43520.3)"
     Site            1223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q148W0; propagated from
                     UniProtKB/Swiss-Prot (O43520.3)"
     CDS             1..1251
                     /gene="ATP8B1"
                     /gene_synonym="ATPIC; BRIC; FIC1; ICP1; PFIC; PFIC1"
                     /coded_by="NM_005603.6:341..4096"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11965.1"
                     /db_xref="GeneID:5205"
                     /db_xref="HGNC:HGNC:3706"
                     /db_xref="MIM:602397"
ORIGIN      
        1 msterdsett fdedsqpnde vvpysddete delddqgsav epeqnrvnre aeenrepfrk
       61 ectwqvkand rkyheqphfm ntkflcikes kyannaikty kynaftfipm nlfeqfkraa
      121 nlyflallil qavpqistla wyttlvpllv vlgvtaikdl vddvarhkmd keinnrtcev
      181 ikdgrfkvak wkeiqvgdvi rlkkndfvpa dilllsssep nslcyvetae ldgetnlkfk
      241 msleitdqyl qredtlatfd gfieceepnn rldkftgtlf wrntsfplda dkillrgcvi
      301 rntdfchglv ifagadtkim knsgktrfkr tkidylmnym vytifvvlil lsaglaigha
      361 yweaqvgnss wylydgeddt psyrgflifw gyiivlntmv pislyvsvev irlgqshfin
      421 wdlqmyyaek dtpakarttt lneqlgqihy ifsdktgtlt qnimtfkkcc ingqiygdhr
      481 dasqhnhnki eqvdfswnty adgklafydh ylieqiqsgk epevrqfffl lavchtvmvd
      541 rtdgqlnyqa aspdegalvn aarnfgfafl artqntitis elgtertynv laildfnsdr
      601 krmsiivrtp egniklyckg adtviyerlh rmnptkqetq daldifanet lrtlclcyke
      661 ieekeftewn kkfmaasvas tnrdealdkv yeeiekdlil lgataiedkl qdgvpetisk
      721 lakadikiwv ltgdkketae nigfacellt edtticyged insllharme nqrnrggvya
      781 kfappvqesf fppggnrali itgswlneil lekktkrnki lklkfprtee errmrtqskr
      841 rleakkeqrq knfvdlacec saviccrvtp kqkamvvdlv krykkaitla igdgandvnm
      901 iktahigvgi sgqegmqavm ssdysfaqfr ylqrlllvhg rwsyirmckf lryffyknfa
      961 ftlvhfwysf fngysaqtay edwfitlynv lytslpvllm glldqdvsdk lslrfpglyi
     1021 vgqrdllfny krffvsllhg vltsmilffi plgaylqtvg qdgeapsdyq sfavtiasal
     1081 vitvnfqigl dtsywtfvna fsifgsialy fgimfdfhsa gihvlfpsaf qftgtasnal
     1141 rqpyiwltii lavavcllpv vairflsmti wpsesdkiqk hrkrlkaeeq wqrrqqvfrr
     1201 gvstrrsaya fshqrgyadl issgrsirkk rspldaivad gtaeyrrtgd s
//
LOCUS       NP_001357323             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357323
VERSION     NP_001357323.1
DBSOURCE    REFSEQ: accession NM_001370394.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1910897.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370394.1:1226..2875"
                     /note="isoform 1 is encoded by transcript variant 23"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_065705               1050 aa            linear   PRI 27-APR-2025
DEFINITION  sentrin-specific protease 7 isoform 1 [Homo sapiens].
ACCESSION   NP_065705
VERSION     NP_065705.3
DBSOURCE    REFSEQ: accession NM_020654.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Wu,Z., Huang,H., Han,Q., Hu,Z., Teng,X.L., Ding,R., Ye,Y., Yu,X.,
            Zhao,R., Wang,Z. and Zou,Q.
  TITLE     SENP7 senses oxidative stress to sustain metabolic fitness and
            antitumor functions of CD8+ T cells
  JOURNAL   J Clin Invest 132 (7) (2022)
   PUBMED   35143421
  REMARK    GeneRIF: SENP7 senses oxidative stress to sustain metabolic fitness
            and antitumor functions of CD8+ T cells.
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Suhail,A., Rizvi,Z.A., Mujagond,P., Ali,S.A., Gaur,P., Singh,M.,
            Ahuja,V., Awasthi,A. and Srikanth,C.V.
  TITLE     DeSUMOylase SENP7-Mediated Epithelial Signaling Triggers Intestinal
            Inflammation via Expansion of Gamma-Delta T Cells
  JOURNAL   Cell Rep 29 (11), 3522-3538 (2019)
   PUBMED   31825833
  REMARK    GeneRIF: DeSUMOylase SENP7-Mediated Epithelial Signaling Triggers
            Intestinal Inflammation via Expansion of Gamma-Delta T Cells.
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Ji,P., Liang,S., Li,P., Xie,C., Li,J., Zhang,K., Zheng,X., Feng,M.,
            Li,Q., Jiao,H., Chi,X., Zhao,W., Zhang,S. and Wang,X.
  TITLE     Speckle-type POZ protein suppresses hepatocellular carcinoma cell
            migration and invasion via ubiquitin-dependent proteolysis of
            SUMO1/sentrin specific peptidase 7
  JOURNAL   Biochem Biophys Res Commun 502 (1), 30-42 (2018)
   PUBMED   29777712
  REMARK    GeneRIF: SPOP inhibits hepatocellular carcinoma (HCC) cell
            metastasis via ubiquitin-dependent SENP7 proteolysis and may thus
            serve as a new opinion for the prevention of HCC metastasis.
REFERENCE   4  (residues 1 to 1050)
  AUTHORS   Karami,S., Lin,F.M., Kumar,S., Bahnassy,S., Thangavel,H.,
            Quttina,M., Li,Y., Ren,J. and Bawa-Khalfe,T.
  TITLE     Novel SUMO-Protease SENP7S Regulates beta-catenin Signaling and
            Mammary Epithelial Cell Transformation
  JOURNAL   Sci Rep 7, 46477 (2017)
   PUBMED   28429743
  REMARK    GeneRIF: non-tumorigenic MCF10-2A cells with reduced SENP7S exhibit
            greater cell proliferation and anchorage-dependent growth. SENP7S
            depletion directly potentiates tumorigenic properties of MCF10-2A
            cells with induction of anchorage-independent growth and
            self-renewal in 3D-spheroid conditions. Collectively, the results
            identify SENP7S as a novel mediator of beta-catenin signaling and
            normal mammary epithelial cell physiology.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1050)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   6  (residues 1 to 1050)
  AUTHORS   Bawa-Khalfe,T., Lu,L.S., Zuo,Y., Huang,C., Dere,R., Lin,F.M. and
            Yeh,E.T.
  TITLE     Differential expression of SUMO-specific protease 7 variants
            regulates epithelial-mesenchymal transition
  JOURNAL   Proc Natl Acad Sci U S A 109 (43), 17466-17471 (2012)
   PUBMED   23045645
  REMARK    GeneRIF: differential splicing of the SENP7 regulates either tumor
            suppression or progression
REFERENCE   7  (residues 1 to 1050)
  AUTHORS   Alegre,K.O. and Reverter,D.
  TITLE     Swapping small ubiquitin-like modifier (SUMO) isoform specificity
            of SUMO proteases SENP6 and SENP7
  JOURNAL   J Biol Chem 286 (41), 36142-36151 (2011)
   PUBMED   21878624
  REMARK    GeneRIF: Loop 1 insertion in SENP6 and SENP7 as a platform to
            discriminate between SUMO1 and SUMO2/3 isoforms in this subclass of
            the SUMO protease family.
REFERENCE   8  (residues 1 to 1050)
  AUTHORS   Nozawa,R.S., Nagao,K., Masuda,H.T., Iwasaki,O., Hirota,T.,
            Nozaki,N., Kimura,H. and Obuse,C.
  TITLE     Human POGZ modulates dissociation of HP1alpha from mitotic
            chromosome arms through Aurora B activation
  JOURNAL   Nat Cell Biol 12 (7), 719-727 (2010)
   PUBMED   20562864
REFERENCE   9  (residues 1 to 1050)
  AUTHORS   Lima,C.D. and Reverter,D.
  TITLE     Structure of the human SENP7 catalytic domain and poly-SUMO
            deconjugation activities for SENP6 and SENP7
  JOURNAL   J Biol Chem 283 (46), 32045-32055 (2008)
   PUBMED   18799455
  REMARK    GeneRIF: SENP6 and SENP7 exhibit lower rates for processing
            pre-SUMO1, pre-SUMO2, or pre-SUMO3 in comparison with SENP2
REFERENCE   10 (residues 1 to 1050)
  AUTHORS   Gong,L., Millas,S., Maul,G.G. and Yeh,E.T.
  TITLE     Differential regulation of sentrinized proteins by a novel
            sentrin-specific protease
  JOURNAL   J Biol Chem 275 (5), 3355-3359 (2000)
   PUBMED   10652325
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136599.1, BC129988.1 and AI858732.1.
            
            On Oct 14, 2006 this sequence version replaced NP_065705.2.
            
            Summary: The reversible posttranslational modification of proteins
            by the addition of small ubiquitin-like SUMO proteins (see SUMO1;
            MIM 601912) is required for many cellular processes. SUMO-specific
            proteases, such as SENP7, process SUMO precursors to generate a
            C-terminal diglycine motif required for the conjugation reaction.
            They also display isopeptidase activity for deconjugation of
            SUMO-conjugated substrates (Lima and Reverter, 2008 [PubMed
            18799455]).[supplied by OMIM, Jun 2009].
            
            Transcript Variant: This variant (1, also known as SENP7L)
            represents the longest transcript and encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC129988.1, SRR18074969.1161413.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394095.7/ ENSP00000377655.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q12.3"
     Protein         1..1050
                     /product="sentrin-specific protease 7 isoform 1"
                     /EC_number="3.4.22.68"
                     /note="sentrin-specific protease 7; SUMO-1-specific
                     protease 2; sentrin/SUMO-specific protease SENP7;
                     SUMO1/sentrin specific peptidase 7"
                     /calculated_mol_wt=119527
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BUH8; propagated from
                     UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZF42; propagated from
                     UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Region          183..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Region          304..365
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Region          443..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Region          760..1050
                     /region_name="Protease.
                     /evidence=ECO:0000250|UniProtKB:Q9HC62"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQF6.4)"
     Region          774..1011
                     /region_name="Peptidase_C48"
                     /note="Ulp1 protease family, C-terminal catalytic domain;
                     cl23802"
                     /db_xref="CDD:420019"
     CDS             1..1050
                     /gene="SENP7"
                     /coded_by="NM_020654.5:83..3235"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2941.2"
                     /db_xref="GeneID:57337"
                     /db_xref="HGNC:HGNC:30402"
                     /db_xref="MIM:612846"
ORIGIN      
        1 mdkrklgrrp ssseiitegk rkksssdlse irkmlnakpe dvhvqsplsk frsserwtlp
       61 lqwerslrnk visldhknkk hirgcpvtsk ssperqlkvm ltnvlwtdlg rkfrktlprn
      121 danlcdankv qsdslpstsv dsletcqkle plrqslnlse riprviltnv lgtelgrkyi
      181 rtppvtegsl sdtdnlqseq lssssdgsle syqnlnphks cylsergsqr sktvddnsak
      241 qtahnkekrr kddgisllis dtqpedlnsg srgcdhleqe srnkdvkysd skveltlisr
      301 ktkrrlrnnl pdsqyctsld ksteqtkkqe ddstistefe kpsenyhqdp klpeeittkp
      361 tksdftklss lnsqeltlsn atksasagst tetvensnsi divgisslve kdenelntie
      421 kpilrghneg nqslisaepi vvssdeegpv ehksseilkl qskqdrettn enestsesal
      481 lelplitces vqmsselcpy npvmenissi mpsnemdlql dfiftsvyig kikgaskgcv
      541 titkkyikip fqvslneisl lvdtthlkrf glwkskddnh skrshailff wvssdylqei
      601 qtqlehsvls qqskssefif lelhnpvsqr eelklkdimt eisiisgele lsyplswvqa
      661 fplfqnlssk essfihyycv stcsfpagva vaeemklksv sqpsntdaak ptytflqkqs
      721 sgcyslsits npdeewrevr htglvqkliv ypppptkggl gvtnedlecl eegeflndvi
      781 idfylkylil ekasdelver shifssffyk cltrkennlt ednpnlsmaq rrhkrvrtwt
      841 rhinifnkdy ifvpvnessh wylavicfpw leeavyedfp qtvsqqsqaq qsqndnktid
      901 ndlrttstls lsaedsqste snmsvpkkmc krpcililds lkaasvqntv qnlreyleve
      961 wevklkthrq fsktnmvdlc pkvpkqdnss dcgvyllqyv esffkdpivn felpihlekw
     1021 fprhviktkr edirelilkl hlqqqkgsss
//
LOCUS       NP_001103348             520 aa            linear   PRI 27-APR-2025
DEFINITION  T-box transcription factor TBX22 isoform 1 [Homo sapiens].
ACCESSION   NP_001103348
VERSION     NP_001103348.1
DBSOURCE    REFSEQ: accession NM_001109878.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Slavec,L., Gersak,K., Eberlinc,A., Hovnik,T., Lovrecic,L.,
            Mlinaric-Rascan,I. and Karas Kuzelicki,N.
  TITLE     A Comprehensive Genetic Analysis of Slovenian Families with
            Multiple Cases of Orofacial Clefts Reveals Novel Variants in the
            Genes IRF6, GRHL3, and TBX22
  JOURNAL   Int J Mol Sci 24 (5), 4262 (2023)
   PUBMED   36901693
  REMARK    GeneRIF: A Comprehensive Genetic Analysis of Slovenian Families
            with Multiple Cases of Orofacial Clefts Reveals Novel Variants in
            the Genes IRF6, GRHL3, and TBX22.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Dai,J., Xu,C., Wang,G., Liang,Y., Wan,T., Zhang,Y., Xu,X., Yu,L.,
            Che,Z., Han,Q., Wu,D. and Yang,Y.
  TITLE     Novel TBX22 mutations in Chinese nonsyndromic cleft lip/palate
            families
  JOURNAL   J Genet 97 (2), 411-417 (2018)
   PUBMED   29932061
  REMARK    GeneRIF: Findings indicate the important role of T-box 22 protein
            (TBX22) in familial cases with X-linked cleft palate.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Marcano,A.C., Doudney,K., Braybrook,C., Squires,R., Patton,M.A.,
            Lees,M.M., Richieri-Costa,A., Lidral,A.C., Murray,J.C., Moore,G.E.
            and Stanier,P.
  TITLE     TBX22 mutations are a frequent cause of cleft palate
  JOURNAL   J Med Genet 41 (1), 68-74 (2004)
   PUBMED   14729838
  REMARK    GeneRIF: Four novel TBX22 splice site mutations in North American
            and Brazilian cleft palate families.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Packham,E.A. and Brook,J.D.
  TITLE     T-box genes in human disorders
  JOURNAL   Hum Mol Genet 12 Spec No 1, R37-R44 (2003)
   PUBMED   12668595
  REMARK    Review article
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Braybrook,C., Lisgo,S., Doudney,K., Henderson,D., Marcano,A.C.,
            Strachan,T., Patton,M.A., Villard,L., Moore,G.E., Stanier,P. and
            Lindsay,S.
  TITLE     Craniofacial expression of human and murine TBX22 correlates with
            the cleft palate and ankyloglossia phenotype observed in CPX
            patients
  JOURNAL   Hum Mol Genet 11 (22), 2793-2804 (2002)
   PUBMED   12374769
  REMARK    GeneRIF: Craniofacial expression of human and murine TBX22
            correlates with the cleft palate and ankyloglossia (CPX) phenotype
            observed in CPX patients.
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Aldred,M.A.
  TITLE     Cleft lip and palate: new genetic clues
  JOURNAL   Trends Mol Med 7 (12), 539-540 (2001)
   PUBMED   11733204
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Braybrook,C., Doudney,K., Marcano,A.C., Arnason,A., Bjornsson,A.,
            Patton,M.A., Goodfellow,P.J., Moore,G.E. and Stanier,P.
  TITLE     The T-box transcription factor gene TBX22 is mutated in X-linked
            cleft palate and ankyloglossia
  JOURNAL   Nat Genet 29 (2), 179-183 (2001)
   PUBMED   11559848
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Laugier-Anfossi,F. and Villard,L.
  TITLE     Molecular characterization of a new human T-box gene (TBX22)
            located in xq21.1 encoding a protein containing a truncated
            T-domain
  JOURNAL   Gene 255 (2), 289-296 (2000)
   PUBMED   11024289
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031000.1, AK097514.1,
            DB456367.1 and AY035371.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of a phylogenetically conserved
            family of genes that share a common DNA-binding domain, the T-box.
            T-box genes encode transcription factors involved in the regulation
            of developmental processes. Mutations in this gene have been
            associated with the inherited X-linked disorder, Cleft palate with
            ankyloglossia, and it is believed to play a major role in human
            palatogenesis. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Both variants 1 and
            2 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.204827.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373296.8/ ENSP00000362393.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq21.1"
     Protein         1..520
                     /product="T-box transcription factor TBX22 isoform 1"
                     /note="T-box transcription factor TBX22; T-box protein 22;
                     T-box 22"
                     /calculated_mol_wt=57779
     Region          1..91
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y458.3)"
     Region          90..283
                     /region_name="T-box_TBX22-like"
                     /note="DNA-binding domain of T-box transcription factor 22
                     and related T-box proteins; cd20200"
                     /db_xref="CDD:410326"
     Site            order(119..120,153,200,203,216..217,260..263,268,271..272,
                     275..281)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410326"
     CDS             1..520
                     /gene="TBX22"
                     /gene_synonym="ABERS; CLPA; CPX; dJ795G23.1; TBXX"
                     /coded_by="NM_001109878.2:138..1700"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14445.1"
                     /db_xref="GeneID:50945"
                     /db_xref="HGNC:HGNC:11600"
                     /db_xref="MIM:300307"
ORIGIN      
        1 malssraraf svealvgrps krklqdpiqa eqpelrekkg geeeeerrss aagkseplek
       61 qpktepstsa ssgcgsdsgy gnssesleek diqmelqgse lwkrfhdigt emiitkagrr
      121 mfpsvrvkvk gldpgkqyhv aidvvpvdsk ryryvyhssq wmvagntdhl ciiprfyvhp
      181 dspcsgetwm rqiisfdrmk ltnnemddkg hiilqsmhky kprvhvieqg ssvdlsqiqs
      241 lptegvktfs fketefttvt ayqnqqitkl kiernpfakg frdtgrnrgv ldglletypw
      301 rpsftldfkt fgadtqsgss gsspvtssgg apsplnslls plcfspmfhl ptsslgmpcp
      361 eaylpnvnlp lcykicptnf wqqqplvlpa perlassnss qslaplmmev pmlsslgvtn
      421 sksgssedss dqylqapnst nqmlyglqsp gniflpnsit pealscsfhp sydfyrynfs
      481 mpsrlisgsn hlkvnddsqv sfgegkcnhv hwypainhyl
//
LOCUS       NP_775913                391 aa            linear   PRI 27-APR-2025
DEFINITION  N-acetylaspartylglutamate synthase A [Homo sapiens].
ACCESSION   NP_775913
VERSION     NP_775913.2
DBSOURCE    REFSEQ: accession NM_173642.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Yan,H., Liu,W., Xiang,R., Li,X., Hou,S., Xu,L., Wang,L., Zhao,D.,
            Liu,X., Wang,G., Chi,Y. and Yang,J.
  TITLE     Ribosomal modification protein rimK-like family member A activates
            betaine-homocysteine S-methyltransferase 1 to ameliorate hepatic
            steatosis
  JOURNAL   Signal Transduct Target Ther 9 (1), 214 (2024)
   PUBMED   39117631
  REMARK    GeneRIF: Ribosomal modification protein rimK-like family member A
            activates betaine-homocysteine S-methyltransferase 1 to ameliorate
            hepatic steatosis.
            Erratum:[Signal Transduct Target Ther. 2024 Dec 11;9(1):360. doi:
            10.1038/s41392-024-02054-1. PMID: 39663370]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Lodder-Gadaczek,J., Becker,I., Gieselmann,V., Wang-Eckhardt,L. and
            Eckhardt,M.
  TITLE     N-acetylaspartylglutamate synthetase II synthesizes
            N-acetylaspartylglutamylglutamate
  JOURNAL   J Biol Chem 286 (19), 16693-16706 (2011)
   PUBMED   21454531
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Collard,F., Stroobant,V., Lamosa,P., Kapanda,C.N., Lambert,D.M.,
            Muccioli,G.G., Poupaert,J.H., Opperdoes,F. and Van Schaftingen,E.
  TITLE     Molecular identification of N-acetylaspartylglutamate synthase and
            beta-citrylglutamate synthase
  JOURNAL   J Biol Chem 285 (39), 29826-29833 (2010)
   PUBMED   20657015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL513331.17, DR000262.1, BC039737.1 and BX094947.1.
            
            On Jan 12, 2008 this sequence version replaced NP_775913.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.219787.1,
                                           SRR1660805.253151.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000431473.4/ ENSP00000414330.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..391
                     /product="N-acetylaspartylglutamate synthase A"
                     /EC_number="6.3.2.41"
                     /EC_number="6.3.2.42"
                     /note="family with sequence similarity 80, member A;
                     ribosomal protein S6 modification-like protein A;
                     N-acetylaspartyl-glutamate synthetase A; NAAG synthetase
                     A; N-acetylaspartylglutamate synthetase II; RP11-157D18.1;
                     N-acetylaspartylglutamylglutamate synthase A"
                     /calculated_mol_wt=42733
     Region          5..298
                     /region_name="CPSase_L_D2"
                     /note="Carbamoyl-phosphate synthase L chain, ATP binding
                     domain; cl17255"
                     /db_xref="CDD:473076"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFX8; propagated from
                     UniProtKB/Swiss-Prot (Q8IXN7.2)"
     Region          341..379
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXN7.2)"
     CDS             1..391
                     /gene="RIMKLA"
                     /gene_synonym="FAM80A; NAAGS; NAAGS-II; NAAGS2"
                     /coded_by="NM_173642.4:144..1319"
                     /db_xref="CCDS:CCDS466.2"
                     /db_xref="GeneID:284716"
                     /db_xref="HGNC:HGNC:28725"
                     /db_xref="MIM:618949"
ORIGIN      
        1 mcsqlwfltd rriredypqv qilralrqrc seqdvrfrav lmdqiavtiv gghlglqlnq
       61 kalttfpdvv lvrvptpsvq sdsditvlrh leklgcrlvn rpqsilncin kfwtfqelag
      121 hgvpmpdtfs ygghedfskm ideaeplgyp vvvkstrghr gkavflardk hhlsdichli
      181 rhdvpylfqk yvkeshgkdi rvvvvggqvi gsmlrcstdg rmqsncslgg vgvkcplteq
      241 gkqlaiqvsn ilgmdfcgid llimddgsfv vceananvgf lafdqacnld vggiiadytm
      301 sllpnrqtgk mavlpglssp reknepdgca saqgvaesvy tinsgstsse sepelgeird
      361 ssastmgapp smlpepgyni nnriaselkl k
//
LOCUS       NP_999185               1214 aa            linear   MAM 27-APR-2025
DEFINITION  pro-epidermal growth factor precursor [Sus scrofa].
ACCESSION   NP_999185
VERSION     NP_999185.1
DBSOURCE    REFSEQ: accession NM_214020.2
KEYWORDS    RefSeq.
SOURCE      Sus scrofa (pig)
  ORGANISM  Sus scrofa
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae;
            Sus.
REFERENCE   1  (residues 1 to 1214)
  AUTHORS   Zhu,M., Iwano,T. and Takeda,S.
  TITLE     Estrogen and EGFR Pathways Regulate Notch Signaling in Opposing
            Directions for Multi-Ciliogenesis in the Fallopian Tube
  JOURNAL   Cells 8 (8), 933 (2019)
   PUBMED   31430961
  REMARK    GeneRIF: The authors show that the differentiation of
            multi-ciliated cells in the fallopian tube depends on the balance
            of EGF and estrogen signaling, either of which inhibits or
            stimulates the Notch signaling pathway respectively.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1214)
  AUTHORS   Hunyadi-Bagi,A., Balogh,P., Nagy,K. and Kusza,S.
  TITLE     Association and polymorphism study of seven candidate genes with
            reproductive traits in three pig breeds in Hungary
  JOURNAL   Acta Biochim Pol 63 (2), 359-364 (2016)
   PUBMED   27119729
  REMARK    GeneRIF: Interval between litters and litter size may be linked
            with EGF polymorphisms in pigs.
REFERENCE   3  (residues 1 to 1214)
  AUTHORS   Jeong,W., Kim,J., Bazer,F.W. and Song,G.
  TITLE     Epidermal growth factor stimulates proliferation and migration of
            porcine trophectoderm cells through protooncogenic protein kinase 1
            and extracellular-signal-regulated kinases 1/2 mitogen-activated
            protein kinase signal transduction cascades during early pregnancy
  JOURNAL   Mol Cell Endocrinol 381 (1-2), 302-311 (2013)
   PUBMED   24012778
  REMARK    GeneRIF: EGF coordinately activates multiple cell signaling
            pathways critical to proliferation, migration and survival of
            trophectoderm cells.
REFERENCE   4  (residues 1 to 1214)
  AUTHORS   Wang,X., Zheng,F., Liu,O., Zheng,S., Liu,Y., Wang,Y., Tang,Z. and
            Zhong,L.
  TITLE     Epidermal growth factor can optimize a serum-free culture system
            for bone marrow stem cell proliferation in a miniature pig model
  JOURNAL   In Vitro Cell Dev Biol Anim 49 (10), 815-825 (2013)
   PUBMED   24002665
  REMARK    GeneRIF: 10 nM/L EGF was the optimal dose for serum-free culture,
            which can replace traditional standard serum medium for in vitro
            expansion of miniature pig bone marrow-derived mesenchymal stem
            cells.
REFERENCE   5  (residues 1 to 1214)
  AUTHORS   Yamashita,Y., Kawashima,I., Gunji,Y., Hishinuma,M. and Shimada,M.
  TITLE     Progesterone is essential for maintenance of Tace/Adam17 mRNA
            expression, but not EGF-like factor, in cumulus cells, which
            enhances the EGF receptor signaling pathway during in vitro
            maturation of porcine COCs
  JOURNAL   J Reprod Dev 56 (3), 315-323 (2010)
   PUBMED   20168049
  REMARK    GeneRIF: progesterone-induced TACE/ADAM17 leads to production of
            soluble EGF domain from cumulus cells, which enhances functional
            changes of cumulus cells and progresses meiotic maturation of
            oocytes
REFERENCE   6  (residues 1 to 1214)
  AUTHORS   Lechner,J., Malloth,N.A., Jennings,P., Heckl,D., Pfaller,W. and
            Seppi,T.
  TITLE     Opposing roles of EGF in IFN-alpha-induced epithelial barrier
            destabilization and tissue repair
  JOURNAL   Am J Physiol Cell Physiol 293 (6), C1843-C1850 (2007)
   PUBMED   17913840
  REMARK    GeneRIF: EGF appears to sensitize epithelial cells to the
            detrimental effects of IFN-alpha but also helps to restore barrier
            function in the healing phase.
REFERENCE   7  (residues 1 to 1214)
  AUTHORS   Andronowska,A., Postek,A. and Doboszynska,T.
  TITLE     Epidermal growth factor and epidermal growth factor receptor
            immunoreactivity in the endothelial cells of the uterine artery and
            its branches during different stages of the estrous cycle in the
            pig
  JOURNAL   Pol J Vet Sci 9 (3), 165-170 (2006)
   PUBMED   17020010
  REMARK    GeneRIF: The phase-related expression of EGF and EGFR in the
            endothelium of the uterine artery and its branches suggest the
            modulatory effect of EGF and its receptor on the uterine artery and
            the region supplying these vessels.
REFERENCE   8  (residues 1 to 1214)
  AUTHORS   Kim,J.G., Vallet,J.L. and Christenson,R.K.
  TITLE     Characterization of uterine epidermal growth factor during early
            pregnancy in pigs
  JOURNAL   Domest Anim Endocrinol 20 (4), 253-265 (2001)
   PUBMED   11518619
REFERENCE   9  (residues 1 to 1214)
  AUTHORS   Jorgensen,P.E., Jensen,L.G., Sorensen,B.S., Poulsen,S.S. and
            Nexo,E.
  TITLE     Pig epidermal growth factor precursor contains segments that are
            highly conserved among species
  JOURNAL   Scand J Clin Lab Invest 58 (4), 287-298 (1998)
   PUBMED   9741816
REFERENCE   10 (residues 1 to 1214)
  AUTHORS   Pascall,J.C., Jones,D.S., Doel,S.M., Clements,J.M., Hunter,M.,
            Fallon,T., Edwards,M. and Brown,K.D.
  TITLE     Cloning and characterization of a gene encoding pig epidermal
            growth factor
  JOURNAL   J Mol Endocrinol 6 (1), 63-70 (1991)
   PUBMED   2015058
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF336151.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF336151.1, SRR5275317.55657.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA103886111, SAMEA103886112
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1214
                     /organism="Sus scrofa"
                     /db_xref="taxon:9823"
                     /chromosome="8"
                     /map="8"
     Protein         1..1214
                     /product="pro-epidermal growth factor precursor"
                     /note="pro-epidermal growth factor"
                     /calculated_mol_wt=131061
     sig_peptide     1..22
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00968.2)"
                     /calculated_mol_wt=2464
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00968.2)"
     Region          47..194
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          86..127
                     /region_name="LDL-receptor class B 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00968.2)"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00968.2)"
     Region          128..169
                     /region_name="LDL-receptor class B 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00968.2)"
     Region          151..189
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          170..211
                     /region_name="LDL-receptor class B 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     Region          212..258
                     /region_name="LDL-receptor class B 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     Region          <331..393
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Site            404
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00968.2)"
     Region          408..436
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          439..476
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          483..523
                     /region_name="LDL-receptor class B 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     Region          504..546
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          524..566
                     /region_name="LDL-receptor class B 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     Region          547..589
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          567..609
                     /region_name="LDL-receptor class B 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     Region          590..633
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          610..653
                     /region_name="LDL-receptor class B 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     Region          634..676
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          654..696
                     /region_name="LDL-receptor class B 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     Region          677..718
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          745..780
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            815
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00968.2)"
     Region          870..902
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF domain; pfam07645"
                     /db_xref="CDD:429571"
     Site            order(870,873,890)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          916..>940
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Site            926
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00968.2)"
     mat_peptide     970..1022
                     /product="pro-epidermal growth factor"
                     /calculated_mol_wt=6149
     Region          <975..>1013
                     /region_name="PHA03099"
                     /note="epidermal growth factor-like protein (EGF-like
                     protein); Provisional"
                     /db_xref="CDD:165381"
     Site            1032..1051
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     Region          1193..1214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00968.2)"
     CDS             1..1214
                     /gene="EGF"
                     /coded_by="NM_214020.2:437..4081"
                     /db_xref="GeneID:397083"
                     /db_xref="RGD:13916117"
                     /db_xref="VGNC:VGNC:98921"
ORIGIN      
        1 mllflilllp vvlkfsfvsl saparwncpe gspsgngnat cvgpapflif shgnsifrid
       61 legtnheqlv adagisvlmd fhyneeriyw vdlerqllqr vflngtrqek vcnleknvsg
      121 mainwineel iwsnqqegti tvtdmkgnns rvllsalkyp anvavdpver lmfwssvvag
      181 slhradvtgv evrllletse eiaavsldvl dkrlfwiqyn reggssrics cdydggsvhf
      241 skhltqhnvf amslfgdhif ystwkkktiw vankhtgkdm vkmnlnpafv ppggikvvhp
      301 lvqpkaegda wasdqklckl rkgncrgsmc gqepkshvct caegytlsqd grkcedvnec
      361 afwnhgctlg centpgsyyc tcpagfvllp dgkrchqlis cpsnvsecsh dcvltsdgpi
      421 cfcpedsvle adgktcsgcs spdnggcsql clplspvtwe cgcfpgydlq ldkkscrasg
      481 pppfllfans qdirhmhfdg tdyetllnqq igmvlaldhd pvenkvyfah talkwieran
      541 mdgsqrerlf eeavdvpegl aidwigrkfy wtdrgrslie gsdlngkyre iiikedisqp
      601 rgiavhpvak rlfwtdmgtn priessslqg igrqviassd lvwpsgitid yltdklywcd
      661 akqsviemsn ldgsrrqrla qndvghpfav avfedhvwfs dwtmpsvirv nkrtgknrvr
      721 lrgsmlkpss lvvvhplakp gtnpclhqng gcehickesf gtaqclcheg flkapdgkmc
      781 lalngqeila grgkdlsdgv mpvdtlprsr elednltesq hilvaeimvs ddedcgaagc
      841 saqarcvteg edatcqclkg fagdgnlcsd idecelgtsv cpptssecin tegghvcrcs
      901 egyqgdgihc ldidecqlgv htcgenatct ntegnytctc agrpsepgri cpdptppshl
      961 gedgrysvrn sysecppshd gyclhggvcm yieavdsyac ncvfgyvger cqhrdlkwwe
     1021 lrhaglgrqw nvtvvavcvv vlvlllllgl wgahyyrtqk llsknpknpy eesgrdvsgi
     1081 rpadgeagms scpqpwfvvi kehqnlrngs qpgapkdglg advgqfssle pgslqptswr
     1141 kepqmymdte qgccipsssd kgsgpqgigy sfhlpsygar siavgveksh sllsanplrq
     1201 qrapdpphqm eltq
//
LOCUS       NP_002402                 93 aa            linear   PRI 27-APR-2025
DEFINITION  mammaglobin-A precursor [Homo sapiens].
ACCESSION   NP_002402
VERSION     NP_002402.1
DBSOURCE    REFSEQ: accession NM_002411.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Kusumastuti,R., Kumagai,Y., Ishihara,S., Enomoto,A., Murakami,T.,
            Yasuda,M. and Haga,H.
  TITLE     Mammaglobin 1 mediates progression of trastuzumab-resistant breast
            cancer cells through regulation of cyclins and NF-kappaB
  JOURNAL   FEBS Open Bio 12 (10), 1797-1813 (2022)
   PUBMED   35945910
  REMARK    GeneRIF: Mammaglobin 1 mediates progression of
            trastuzumab-resistant breast cancer cells through regulation of
            cyclins and NF-kappaB.
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Talaat,I.M., Hachim,M.Y., Hachim,I.Y., Ibrahim,R.A.E.,
            Ahmed,M.A.E.R. and Tayel,H.Y.
  TITLE     Bone marrow mammaglobin-1 (SCGB2A2) immunohistochemistry expression
            as a breast cancer specific marker for early detection of bone
            marrow micrometastases
  JOURNAL   Sci Rep 10 (1), 13061 (2020)
   PUBMED   32747636
  REMARK    GeneRIF: Bone marrow mammaglobin-1 (SCGB2A2) immunohistochemistry
            expression as a breast cancer specific marker for early detection
            of bone marrow micrometastases.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Soares,C.D., de Lima Morais,T.M., Carlos,R., Martins,M.D., de
            Almeida,O.P., Mariano,F.V. and Altemani,A.
  TITLE     Immunohistochemical expression of mammaglobin in salivary duct
            carcinomas de novo and salivary duct carcinoma ex pleomorphic
            adenoma
  JOURNAL   Hum Pathol 92, 59-66 (2019)
   PUBMED   31400353
  REMARK    GeneRIF: This study has confirmed that the mammaglobin is commonly
            expressed in salivary duct carcinoma de novo and secretory
            carcinomas.
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Ni,Y.B., Tsang,J.Y.S., Shao,M.M., Chan,S.K., Cheung,S.Y., Tong,J.,
            To,K.F. and Tse,G.M.
  TITLE     GATA-3 is superior to GCDFP-15 and mammaglobin to identify primary
            and metastatic breast cancer
  JOURNAL   Breast Cancer Res Treat 169 (1), 25-32 (2018)
   PUBMED   29340880
  REMARK    GeneRIF: GATA-3 expression was the highest in luminal breast
            carcinomas, and showed higher sensitivity than GCDFP-15 and MGB.
            However, in the poorly differentiated IBC, its utility was still
            limited. One should be aware of the possible GATA-3 expression in
            lung carcinomas.
REFERENCE   5  (residues 1 to 93)
  AUTHORS   Yang,Y., Lu,S., Zeng,W., Xie,S. and Xiao,S.
  TITLE     GATA3 expression in clinically useful groups of breast carcinoma: a
            comparison with GCDFP15 and mammaglobin for identifying paired
            primary and metastatic tumors
  JOURNAL   Ann Diagn Pathol 26, 1-5 (2017)
   PUBMED   28038704
  REMARK    GeneRIF: good coincidence was observed between primary and
            metastatic tumor GATA3 expression (kappa value = 0.826 >0.75) as
            compared with the coincidence of GCDFP15 (kappa value =0.492 <0.75)
            and mammaglobin (kappa value =0.593 <0.75)
REFERENCE   6  (residues 1 to 93)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   7  (residues 1 to 93)
  AUTHORS   Fischer,M. and Kuppers,R.
  TITLE     Human IgA- and IgM-secreting intestinal plasma cells carry heavily
            mutated VH region genes
  JOURNAL   Eur J Immunol 28 (9), 2971-2977 (1998)
   PUBMED   9754584
REFERENCE   8  (residues 1 to 93)
  AUTHORS   Watson,M.A., Darrow,C., Zimonjic,D.B., Popescu,N.C. and
            Fleming,T.P.
  TITLE     Structure and transcriptional regulation of the human mammaglobin
            gene, a breast cancer associated member of the uteroglobin gene
            family localized to chromosome 11q13
  JOURNAL   Oncogene 16 (6), 817-824 (1998)
   PUBMED   9488047
REFERENCE   9  (residues 1 to 93)
  AUTHORS   Wilson,P.C., de Bouteiller,O., Liu,Y.J., Potter,K., Banchereau,J.,
            Capra,J.D. and Pascual,V.
  TITLE     Somatic hypermutation introduces insertions and deletions into
            immunoglobulin V genes
  JOURNAL   J Exp Med 187 (1), 59-70 (1998)
   PUBMED   9419211
REFERENCE   10 (residues 1 to 93)
  AUTHORS   Watson,M.A. and Fleming,T.P.
  TITLE     Mammaglobin, a mammary-specific member of the uteroglobin gene
            family, is overexpressed in human breast cancer
  JOURNAL   Cancer Res 56 (4), 860-865 (1996)
   PUBMED   8631025
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U33147.1 and BG207094.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AW972474.1, U33147.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000227918.3/ ENSP00000227918.2
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..93
                     /product="mammaglobin-A precursor"
                     /note="mammaglobin 1; mammaglobin-A; prostatic steroid
                     binding protein 1"
                     /calculated_mol_wt=8481
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2037
     Region          15..90
                     /region_name="Uteroglobin"
                     /note="Uteroglobin family; pfam01099"
                     /db_xref="CDD:460063"
     mat_peptide     19..93
                     /product="Mammaglobin-A. /id=PRO_0000036372"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13296.1)"
                     /calculated_mol_wt=8481
     Site            order(24..25,28,42,46,49,54..59,61..62,65,73,75..77,
                     79..80,83)
                     /site_type="other"
                     /note="Dimer interface [polypeptide binding]"
                     /db_xref="CDD:238346"
     Site            order(25,32,42,59,62,77,80..81)
                     /site_type="other"
                     /note="Hydrophobic pocket - steroid binding site [chemical
                     binding]"
                     /db_xref="CDD:238346"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13296.1)"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13296.1)"
     CDS             1..93
                     /gene="SCGB2A2"
                     /gene_synonym="MGB1; PSBP1; UGB2"
                     /coded_by="NM_002411.4:60..341"
                     /db_xref="CCDS:CCDS8018.1"
                     /db_xref="GeneID:4250"
                     /db_xref="HGNC:HGNC:7050"
                     /db_xref="MIM:605562"
ORIGIN      
        1 mkllmvlmla alsqhcyags gcpllenvis ktinpqvskt eykellqefi ddnattnaid
       61 elkecflnqt detlsnvevf mqliydsslc dlf
//
LOCUS       NP_056203                350 aa            linear   PRI 27-APR-2025
DEFINITION  protein YIPF3 [Homo sapiens].
ACCESSION   NP_056203
VERSION     NP_056203.2
DBSOURCE    REFSEQ: accession NM_015388.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Soonthornsit,J., Sakai,N., Sasaki,Y., Watanabe,R., Osako,S. and
            Nakamura,N.
  TITLE     YIPF1, YIPF2, and YIPF6 are medial-/trans-Golgi and trans-Golgi
            network-localized Yip domain family proteins, which play a role in
            the Golgi reassembly and glycan synthesis
  JOURNAL   Exp Cell Res 353 (2), 100-108 (2017)
   PUBMED   28286305
  REMARK    GeneRIF: Knockdown of YIPF1 and YIPF2, but not that of YIPF6, also
            reduced intracellular glycans in HT-29 cells. Thus, we confirmed
            that YIPF1, YIPF2, and YIPF6 play a significant role in supporting
            normal glycan synthesis
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Kranjc,T., Dempsey,E., Cagney,G., Nakamura,N., Shields,D.C. and
            Simpson,J.C.
  TITLE     Functional characterisation of the YIPF protein family in mammalian
            cells
  JOURNAL   Histochem Cell Biol 147 (4), 439-451 (2017)
   PUBMED   27999994
  REMARK    GeneRIF: The significance of YIPF3 protein for the maintenance of
            the morphology of the Golgi was tested by RNA interference,
            revealing a number of specific morphological changes to this
            organelle on their depletion.
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Tanimoto,K., Suzuki,K., Jokitalo,E., Sakai,N., Sakaguchi,T.,
            Tamura,D., Fujii,G., Aoki,K., Takada,S., Ishida,R., Tanabe,M.,
            Itoh,H., Yoneda,Y., Sohda,M., Misumi,Y. and Nakamura,N.
  TITLE     Characterization of YIPF3 and YIPF4, cis-Golgi Localizing Yip
            domain family proteins
  JOURNAL   Cell Struct Funct 36 (2), 171-185 (2011)
   PUBMED   21757827
  REMARK    GeneRIF: YIPF3 is synthesized in the ER as a N-glycosylated form
            (40 kDa), is then O-glycosylated in the Golgi apparatus to become a
            lower mobility form (46 kDa) and finally becomes a higher mobility
            form cleaved at its C-terminal luminal domain (36 kDa).
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC019297.1.
            
            On Jun 30, 2004 this sequence version replaced NP_056203.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC019297.1, SRR1660803.123200.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372422.7/ ENSP00000361499.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..350
                     /product="protein YIPF3"
                     /note="killer lineage protein 1; natural killer
                     cell-specific antigen KLIP1"
                     /calculated_mol_wt=38117
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            188..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            215..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            241..263
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            333
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:21757827; propagated from
                     UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            334
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:21757827; propagated from
                     UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21757827; propagated from
                     UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            339
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:23234360; propagated from
                     UniProtKB/Swiss-Prot (Q9GZM5.1)"
     Site            346
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:21757827,
                     ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360;
                     propagated from UniProtKB/Swiss-Prot (Q9GZM5.1)"
     CDS             1..350
                     /gene="YIPF3"
                     /gene_synonym="C6orf109; dJ337H4.3; FinGER3; KLIP1; Yip5b;
                     YIPFbeta2"
                     /coded_by="NM_015388.4:120..1172"
                     /db_xref="CCDS:CCDS4899.1"
                     /db_xref="GeneID:25844"
                     /db_xref="HGNC:HGNC:21023"
                     /db_xref="MIM:609775"
ORIGIN      
        1 mattaapagg arngagpewg gfeeniqggg savidmenmd dtsgssfedm gelhqrlree
       61 evdadaadaa aaeeedgefl gmkgfkgqls rqvadqmwqa gkrqasrafs lyanidilrp
      121 yfdvepaqvr srllesmipi kmvnfpqkia gelygplmlv ftlvaillhg mktsdtiire
      181 gtlmgtaigt cfgywlgvss fiyflaylcn aqitmlqmla llgyglfghc ivlfitynih
      241 lhalfylfwl lvgglstlrm vavlvsrtvg ptqrlllcgt laalhmlfll ylhfayhkvv
      301 egildtlegp nippiqrvpr dipamlpaar lpttvlnata kavavtlqsh
//
LOCUS       NP_112214                628 aa            linear   PRI 27-APR-2025
DEFINITION  NUAK family SNF1-like kinase 2 [Homo sapiens].
ACCESSION   NP_112214
VERSION     NP_112214.3
DBSOURCE    REFSEQ: accession NM_030952.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Guo,Z. and Guo,L.
  TITLE     OTUD7B deubiquitinates and stabilizes YAP1 to upregulate NUAK2
            expression, thus accelerating gastric cancer procession
  JOURNAL   Dig Liver Dis 56 (2), 352-362 (2024)
   PUBMED   37429790
  REMARK    GeneRIF: OTUD7B deubiquitinates and stabilizes YAP1 to upregulate
            NUAK2 expression, thus accelerating gastric cancer procession.
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Prasad,V., Cerikan,B., Stahl,Y., Kopp,K., Magg,V.,
            Acosta-Rivero,N., Kim,H., Klein,K., Funaya,C., Haselmann,U.,
            Cortese,M., Heigwer,F., Bageritz,J., Bitto,D., Jargalsaikhan,S.,
            Neufeldt,C., Pahmeier,F., Boutros,M., Yamauchi,Y., Ruggieri,A. and
            Bartenschlager,R.
  TITLE     Enhanced SARS-CoV-2 entry via UPR-dependent AMPK-related kinase
            NUAK2
  JOURNAL   Mol Cell 83 (14), 2559-2577 (2023)
   PUBMED   37421942
  REMARK    GeneRIF: Enhanced SARS-CoV-2 entry via UPR-dependent AMPK-related
            kinase NUAK2.
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Dai,Y., Shi,W., Qiu,Y., Xu,T., Lin,J. and Su,Y.
  TITLE     Circ_0000033 up-regulates NUAK2 by sequestering miR-378a-3p to
            promote breast tumorigenesis
  JOURNAL   Environ Mol Mutagen 64 (6), 359-370 (2023)
   PUBMED   37357410
  REMARK    GeneRIF: Circ_0000033 up-regulates NUAK2 by sequestering
            miR-378a-3p to promote breast tumorigenesis.
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Lin,R., Wu,W., Chen,H., Gao,H., Wu,X., Li,G., He,Q., Lu,H., Sun,M.
            and Liu,Z.
  TITLE     GPR65 promotes intestinal mucosal Th1 and Th17 cell differentiation
            and gut inflammation through downregulating NUAK2
  JOURNAL   Clin Transl Med 12 (3), e771 (2022)
   PUBMED   35343079
  REMARK    GeneRIF: GPR65 promotes intestinal mucosal Th1 and Th17 cell
            differentiation and gut inflammation through downregulating NUAK2.
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Legembre,P., Schickel,R., Barnhart,B.C. and Peter,M.E.
  TITLE     Identification of SNF1/AMP kinase-related kinase as an
            NF-kappaB-regulated anti-apoptotic kinase involved in CD95-induced
            motility and invasiveness
  JOURNAL   J Biol Chem 279 (45), 46742-46747 (2004)
   PUBMED   15345718
  REMARK    GeneRIF: SNARK is an NF-kappaB-regulated anti-apoptotic gene that
            contributes to the tumor-promoting activity of CD95 in
            apoptosis-resistant tumor cells
REFERENCE   7  (residues 1 to 628)
  AUTHORS   Lizcano,J.M., Goransson,O., Toth,R., Deak,M., Morrice,N.A.,
            Boudeau,J., Hawley,S.A., Udd,L., Makela,T.P., Hardie,D.G. and
            Alessi,D.R.
  TITLE     LKB1 is a master kinase that activates 13 kinases of the AMPK
            subfamily, including MARK/PAR-1
  JOURNAL   EMBO J 23 (4), 833-843 (2004)
   PUBMED   14976552
REFERENCE   8  (residues 1 to 628)
  AUTHORS   Suzuki,A., Kusakai,G., Kishimoto,A., Minegichi,Y., Ogura,T. and
            Esumi,H.
  TITLE     Induction of cell-cell detachment during glucose starvation through
            F-actin conversion by SNARK, the fourth member of the AMP-activated
            protein kinase catalytic subunit family
  JOURNAL   Biochem Biophys Res Commun 311 (1), 156-161 (2003)
   PUBMED   14575707
REFERENCE   9  (residues 1 to 628)
  AUTHORS   Lefebvre,D.L., Bai,Y., Shahmolky,N., Sharma,M., Poon,R.,
            Drucker,D.J. and Rosen,C.F.
  TITLE     Identification and characterization of a novel
            sucrose-non-fermenting protein kinase/AMP-activated protein
            kinase-related protein kinase, SNARK
  JOURNAL   Biochem J 355 (Pt 2), 297-305 (2001)
   PUBMED   11284715
  REMARK    GeneRIF: This study describes the cloning and characterization of
            the rat SNARK homolog, mapping of the human SNARK gene to 1q32, and
            a potential functional role as mediator of the cellular response to
            metabolic stress.
REFERENCE   10 (residues 1 to 628)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC098933.2.
            
            On Dec 20, 2018 this sequence version replaced NP_112214.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017306.2, AL136891.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367157.6/ ENSP00000356125.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..628
                     /product="NUAK family SNF1-like kinase 2"
                     /EC_number="2.7.11.1"
                     /note="SNF1/AMP activated protein kinase; NUAK family,
                     SNF1-like kinase, 2; SNF1/AMP kinase-related kinase;
                     omphalocele kinase 2"
                     /calculated_mol_wt=69481
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H093.1)"
     Region          49..303
                     /region_name="STKc_NUAK2"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     novel (nua) kinase family NUAK 2; cd14161"
                     /db_xref="CDD:271063"
     Site            order(59..63,67,79,81,113,129..132,136,138..139,141,
                     174..175,177,179..180,182,192..193,196,209..214,216,
                     246..249,251)
                     /site_type="active"
                     /db_xref="CDD:271063"
     Site            order(59..62,67,79,81,113,129..132,136,179..180,182,
                     192..193)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271063"
     Site            order(136,138..139,141,175,177,179,196,209..214,216,
                     246..249,251)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271063"
     Site            192..214
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271063"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by LKB1.
                     /evidence=ECO:0000269|PubMed:14976552,
                     ECO:0000269|PubMed:32845958; propagated from
                     UniProtKB/Swiss-Prot (Q9H093.1)"
     Region          355..493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H093.1)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q9H093.1)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q9H093.1)"
     Region          531..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H093.1)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q9H093.1)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q9H093.1)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZN4; propagated from
                     UniProtKB/Swiss-Prot (Q9H093.1)"
     CDS             1..628
                     /gene="NUAK2"
                     /gene_synonym="ANPH2; SNARK"
                     /coded_by="NM_030952.3:118..2004"
                     /db_xref="CCDS:CCDS1453.3"
                     /db_xref="GeneID:81788"
                     /db_xref="HGNC:HGNC:29558"
                     /db_xref="MIM:608131"
ORIGIN      
        1 meslvfarrs gptpsaaela rplaegliks pkplmkkqav krhhhkhnlr hryefletlg
       61 kgtygkvkka ressgrlvai ksirkdkikd eqdlmhirre ieimsslnhp hiiaihevfe
      121 nsskivivme yasrgdlydy iserqqlser earhffrqiv savhychqnr vvhrdlklen
      181 illdangnik iadfglsnly hqgkflqtfc gsplyaspei vngkpytgpe vdswslgvll
      241 yilvhgtmpf dghdhkilvk qisngayrep pkpsdacgli rwllmvnptr ratledvash
      301 wwvnwgyatr vgeqeapheg ghpgsdsara smadwlrrss rpllengakv csffkqhapg
      361 ggsttpgler qhslkksrke ndmaqslhsd taddtahrpg ksnlklpkgi lkkkvsasae
      421 gvqedppels pipaspgqaa pllpkkgilk kprqresgyy sspepsesge lldagdvfvs
      481 gdpkeqkppq asglllhrkg ilklngkfsq talelaaptt fgsldelapp rplarasrps
      541 gavsedsils sesfdqldlp erlpepplrg cvsvdnltgl eeppsegpgs clrrwrqdpl
      601 gdscfsltdc qevtatyrqa lrvcsklt
//
LOCUS       NP_001349828             399 aa            linear   ROD 27-APR-2025
DEFINITION  actin-related protein 2 isoform 1 [Mus musculus].
ACCESSION   NP_001349828 XP_006514843
VERSION     NP_001349828.1
DBSOURCE    REFSEQ: accession NM_001362899.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Aloisio,F.M. and Barber,D.L.
  TITLE     Arp2/3 complex activity is necessary for mouse ESC differentiation,
            times formative pluripotency, and enables lineage specification
  JOURNAL   Stem Cell Reports 17 (6), 1318-1333 (2022)
   PUBMED   35658973
  REMARK    GeneRIF: Arp2/3 complex activity is necessary for mouse ESC
            differentiation, times formative pluripotency, and enables lineage
            specification.
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Longatti,A., Ponzoni,L., Moretto,E., Giansante,G., Lattuada,N.,
            Colombo,M.N., Francolini,M., Sala,M., Murru,L. and Passafaro,M.
  TITLE     Arhgap22 Disruption Leads to RAC1 Hyperactivity Affecting
            Hippocampal Glutamatergic Synapses and Cognition in Mice
  JOURNAL   Mol Neurobiol 58 (12), 6092-6110 (2021)
   PUBMED   34455539
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Figueiredo,A.M., Barbacena,P., Russo,A., Vaccaro,S., Ramalho,D.,
            Pena,A., Lima,A.P., Ferreira,R.R., Fidalgo,M.A., El-Marjou,F.,
            Carvalho,Y., Vasconcelos,F.F., Lennon-Dumenil,A.M., Vignjevic,D.M.
            and Franco,C.A.
  TITLE     Endothelial cell invasion is controlled by dactylopodia
  JOURNAL   Proc Natl Acad Sci U S A 118 (18) (2021)
   PUBMED   33903241
  REMARK    GeneRIF: Endothelial cell invasion is controlled by dactylopodia.
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Ma,W., Chang,J., Tong,J., Ho,U., Yau,B., Kebede,M.A. and Thorn,P.
  TITLE     Arp2/3 nucleates F-actin coating of fusing insulin granules in
            pancreatic beta cells to control insulin secretion
  JOURNAL   J Cell Sci 133 (6) (2020)
   PUBMED   32079655
  REMARK    GeneRIF: Arp2/3 nucleates F-actin coating of fusing insulin
            granules in pancreatic beta cells to control insulin secretion.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Tessier,S., Doolittle,A.C., Sao,K., Rotty,J.D., Bear,J.E.,
            Ulici,V., Loeser,R.F., Shapiro,I.M., Diekman,B.O. and Risbud,M.V.
  TITLE     Arp2/3 inactivation causes intervertebral disc and cartilage
            degeneration with dysregulated TonEBP-mediated osmoadaptation
  JOURNAL   JCI Insight 5 (4), 131382 (2020)
   PUBMED   31961823
  REMARK    GeneRIF: Arp2/3 inactivation causes intervertebral disc and
            cartilage degeneration with dysregulated TonEBP-mediated
            osmoadaptation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Strasser,G.A., Rahim,N.A., VanderWaal,K.E., Gertler,F.B. and
            Lanier,L.M.
  TITLE     Arp2/3 is a negative regulator of growth cone translocation
  JOURNAL   Neuron 43 (1), 81-94 (2004)
   PUBMED   15233919
  REMARK    GeneRIF: Arp2/3 inhibition in growth cones doesn't affect actin
            organization or inhibit lamellipodia protrusion or filopodia
            formation. Arp2/3 inhibition enhances axon elongation and causes
            defects in growth cone guidance.
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Merrifield,C.J., Qualmann,B., Kessels,M.M. and Almers,W.
  TITLE     Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3
            complex are recruited to sites of clathrin-mediated endocytosis in
            cultured fibroblasts
  JOURNAL   Eur J Cell Biol 83 (1), 13-18 (2004)
   PUBMED   15085951
  REMARK    GeneRIF: N-WASP and the Arp2/3 complex trigger actin polymerization
            during a late step in clathrin-mediated endocytosis
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Vyas,A., Saha,B., Lai,E. and Tole,S.
  TITLE     Paleocortex is specified in mice in which dorsal telencephalic
            patterning is severely disrupted
  JOURNAL   J Comp Neurol 466 (4), 545-553 (2003)
   PUBMED   14566948
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Magdalena,J., Millard,T.H., Etienne-Manneville,S., Launay,S.,
            Warwick,H.K. and Machesky,L.M.
  TITLE     Involvement of the Arp2/3 complex and Scar2 in Golgi polarity in
            scratch wound models
  JOURNAL   Mol Biol Cell 14 (2), 670-684 (2003)
   PUBMED   12589062
  REMARK    GeneRIF: Scar2 and the Arp2/3 complex appear to be involved in the
            establishment and maintenance of Golgi polarity during directed
            migration
REFERENCE   10 (residues 1 to 399)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606522.6 and BP753259.1.
            
            On May 3, 2018 this sequence version replaced XP_006514843.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR3363658.5710234.1,
                                           SRR10662774.1592634.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 12.88 cM"
     Protein         1..399
                     /product="actin-related protein 2 isoform 1"
                     /note="actin-like protein 2; ARP2 actin-related protein 2
                     homolog"
                     /calculated_mol_wt=45246
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P61160; propagated from
                     UniProtKB/Swiss-Prot (P61161.1)"
     Region          7..393
                     /region_name="ASKHA_NBD_Arp2"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein2 (Arp2) and similar proteins; cd10220"
                     /db_xref="CDD:466821"
     Site            304
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P61160; propagated from
                     UniProtKB/Swiss-Prot (P61161.1)"
     Site            327
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P61160; propagated from
                     UniProtKB/Swiss-Prot (P61161.1)"
     CDS             1..399
                     /gene="Actr2"
                     /gene_synonym="4921510D23Rik; Arp2; D6Ertd746e"
                     /coded_by="NM_001362899.1:100..1299"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:66713"
                     /db_xref="MGI:MGI:1913963"
ORIGIN      
        1 mdsqgrkvvv cdngtgfvkc gyagsnfpeh ifpalvgrpi irsttkvgni eiknnkkmdl
       61 mvgdeaselr smlevnypme ngivrnwddm khlwdytfgp eklnidtrnc killteppmn
      121 ptknrekive vmfetyqfsg vyvaiqavlt lyaqglltgv vvdsgdgvth icpvyegfsl
      181 phltrrldia grditrylik llllrgyafn hsadfetvrm ikeklcyvgy nieqeqklal
      241 ettvlvesyt lpdgriikvg gerfeapeal fqphlinveg vgvaellfnt iqaadidtrs
      301 efykhivlsg gstmypglps rlerelkqly lervlkgdve klskfkirie dpprrkhmvf
      361 lggavladim kdkdnfwmtr qeyqekgvrv leklgvtvr
//
LOCUS       NP_689650                261 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 664 [Homo sapiens].
ACCESSION   NP_689650
VERSION     NP_689650.1
DBSOURCE    REFSEQ: accession NM_152437.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Zhang,T.X., Haller,G., Lin,P., Alvarado,D.M., Hecht,J.T.,
            Blanton,S.H., Stephens Richards,B., Rice,J.P., Dobbs,M.B. and
            Gurnett,C.A.
  TITLE     Genome-wide association study identifies new disease loci for
            isolated clubfoot
  JOURNAL   J Med Genet 51 (5), 334-339 (2014)
   PUBMED   24667120
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Wu,Y., Gao,H., Li,H., Tabara,Y., Nakatochi,M., Chiu,Y.F.,
            Park,E.J., Wen,W., Adair,L.S., Borja,J.B., Cai,Q., Chang,Y.C.,
            Chen,P., Croteau-Chonka,D.C., Fogarty,M.P., Gan,W., He,C.T.,
            Hsiung,C.A., Hwu,C.M., Ichihara,S., Igase,M., Jo,J., Kato,N.,
            Kawamoto,R., Kuzawa,C.W., Lee,J.J., Liu,J., Lu,L., McDade,T.W.,
            Osawa,H., Sheu,W.H., Teo,Y., Vadlamudi,S., Van Dam,R.M., Wang,Y.,
            Xiang,Y.B., Yamamoto,K., Ye,X., Young,T.L., Zheng,W., Zhu,J.,
            Shu,X.O., Shin,C., Jee,S.H., Chuang,L.M., Miki,T., Yokota,M.,
            Lin,X., Mohlke,K.L. and Tai,E.S.
  TITLE     A meta-analysis of genome-wide association studies for adiponectin
            levels in East Asians identifies a novel locus near WDR11-FGFR2
  JOURNAL   Hum Mol Genet 23 (4), 1108-1119 (2014)
   PUBMED   24105470
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Shi,Y., Li,Y., Zhang,D., Zhang,H., Li,Y., Lu,F., Liu,X., He,F.,
            Gong,B., Cai,L., Li,R., Liao,S., Ma,S., Lin,H., Cheng,J., Zheng,H.,
            Shan,Y., Chen,B., Hu,J., Jin,X., Zhao,P., Chen,Y., Zhang,Y.,
            Lin,Y., Li,X., Fan,Y., Yang,H., Wang,J. and Yang,Z.
  TITLE     Exome sequencing identifies ZNF644 mutations in high myopia
  JOURNAL   PLoS Genet 7 (6), e1002084 (2011)
   PUBMED   21695231
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Teslovich,T.M., Musunuru,K., Smith,A.V., Edmondson,A.C.,
            Stylianou,I.M., Koseki,M., Pirruccello,J.P., Ripatti,S.,
            Chasman,D.I., Willer,C.J., Johansen,C.T., Fouchier,S.W., Isaacs,A.,
            Peloso,G.M., Barbalic,M., Ricketts,S.L., Bis,J.C., Aulchenko,Y.S.,
            Thorleifsson,G., Feitosa,M.F., Chambers,J., Orho-Melander,M.,
            Melander,O., Johnson,T., Li,X., Guo,X., Li,M., Shin Cho,Y., Jin
            Go,M., Jin Kim,Y., Lee,J.Y., Park,T., Kim,K., Sim,X., Twee-Hee
            Ong,R., Croteau-Chonka,D.C., Lange,L.A., Smith,J.D., Song,K., Hua
            Zhao,J., Yuan,X., Luan,J., Lamina,C., Ziegler,A., Zhang,W.,
            Zee,R.Y., Wright,A.F., Witteman,J.C., Wilson,J.F., Willemsen,G.,
            Wichmann,H.E., Whitfield,J.B., Waterworth,D.M., Wareham,N.J.,
            Waeber,G., Vollenweider,P., Voight,B.F., Vitart,V.,
            Uitterlinden,A.G., Uda,M., Tuomilehto,J., Thompson,J.R., Tanaka,T.,
            Surakka,I., Stringham,H.M., Spector,T.D., Soranzo,N., Smit,J.H.,
            Sinisalo,J., Silander,K., Sijbrands,E.J., Scuteri,A., Scott,J.,
            Schlessinger,D., Sanna,S., Salomaa,V., Saharinen,J., Sabatti,C.,
            Ruokonen,A., Rudan,I., Rose,L.M., Roberts,R., Rieder,M.,
            Psaty,B.M., Pramstaller,P.P., Pichler,I., Perola,M., Penninx,B.W.,
            Pedersen,N.L., Pattaro,C., Parker,A.N., Pare,G., Oostra,B.A.,
            O'Donnell,C.J., Nieminen,M.S., Nickerson,D.A., Montgomery,G.W.,
            Meitinger,T., McPherson,R., McCarthy,M.I., McArdle,W., Masson,D.,
            Martin,N.G., Marroni,F., Mangino,M., Magnusson,P.K., Lucas,G.,
            Luben,R., Loos,R.J., Lokki,M.L., Lettre,G., Langenberg,C.,
            Launer,L.J., Lakatta,E.G., Laaksonen,R., Kyvik,K.O., Kronenberg,F.,
            Konig,I.R., Khaw,K.T., Kaprio,J., Kaplan,L.M., Johansson,A.,
            Jarvelin,M.R., Janssens,A.C., Ingelsson,E., Igl,W., Kees
            Hovingh,G., Hottenga,J.J., Hofman,A., Hicks,A.A., Hengstenberg,C.,
            Heid,I.M., Hayward,C., Havulinna,A.S., Hastie,N.D., Harris,T.B.,
            Haritunians,T., Hall,A.S., Gyllensten,U., Guiducci,C., Groop,L.C.,
            Gonzalez,E., Gieger,C., Freimer,N.B., Ferrucci,L., Erdmann,J.,
            Elliott,P., Ejebe,K.G., Doring,A., Dominiczak,A.F., Demissie,S.,
            Deloukas,P., de Geus,E.J., de Faire,U., Crawford,G., Collins,F.S.,
            Chen,Y.D., Caulfield,M.J., Campbell,H., Burtt,N.P.,
            Bonnycastle,L.L., Boomsma,D.I., Boekholdt,S.M., Bergman,R.N.,
            Barroso,I., Bandinelli,S., Ballantyne,C.M., Assimes,T.L.,
            Quertermous,T., Altshuler,D., Seielstad,M., Wong,T.Y., Tai,E.S.,
            Feranil,A.B., Kuzawa,C.W., Adair,L.S., Taylor,H.A. Jr.,
            Borecki,I.B., Gabriel,S.B., Wilson,J.G., Holm,H.,
            Thorsteinsdottir,U., Gudnason,V., Krauss,R.M., Mohlke,K.L.,
            Ordovas,J.M., Munroe,P.B., Kooner,J.S., Tall,A.R., Hegele,R.A.,
            Kastelein,J.J., Schadt,E.E., Rotter,J.I., Boerwinkle,E.,
            Strachan,D.P., Mooser,V., Stefansson,K., Reilly,M.P., Samani,N.J.,
            Schunkert,H., Cupples,L.A., Sandhu,M.S., Ridker,P.M., Rader,D.J.,
            van Duijn,C.M., Peltonen,L., Abecasis,G.R., Boehnke,M. and
            Kathiresan,S.
  TITLE     Biological, clinical and population relevance of 95 loci for blood
            lipids
  JOURNAL   Nature 466 (7307), 707-713 (2010)
   PUBMED   20686565
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Rivolta,M.N., Negrini,C. and Wilcox,E.R.
  TITLE     A novel zinc finger gene preferentially expressed in the retina and
            the organ of Corti localizes to human chromosome 12q24.3
  JOURNAL   Biochim Biophys Acta 1306 (2-3), 127-132 (1996)
   PUBMED   8634327
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA304849.1, BX647762.1, AK056034.1, BC051696.1, AC068790.36 and
            BQ185193.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA326356.1, SRR1803616.40783.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337815.9/ ENSP00000337320.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..261
                     /product="zinc finger protein 664"
                     /note="zinc finger Organ of Corti 1; zinc finger protein
                     176; zinc finger protein from organ of Corti"
                     /calculated_mol_wt=30153
     Region          5..25
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          33..53
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          61..81
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          74..97
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          89..109
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <94..256
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          117..137
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          145..165
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          173..193
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(178,180,182,184..185,188..189,192,206,208,212..213,
                     216..217,220,234,236,238,240..241,244..245,248)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          201..221
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          229..249
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..261
                     /gene="ZNF664"
                     /gene_synonym="ZFOC1; ZNF176"
                     /coded_by="NM_152437.3:1030..1815"
                     /db_xref="CCDS:CCDS9257.1"
                     /db_xref="GeneID:144348"
                     /db_xref="HGNC:HGNC:25406"
                     /db_xref="MIM:617890"
ORIGIN      
        1 miykcpmcre ffseradlfm hqkihtaekp hkcdkcdkgf fhiselhihw rdhtgekvyk
       61 cddcgkdfst ttklnrhkki htvekpykcy ecgkafnwss hlqihmrvht gekpyvcsec
      121 grgfsnssnl cmhqrvhtge kpfkceecgk afrhtsslcm hqrvhtgekp ykcyecgkaf
      181 sqssslcihq rvhtgekpyr ccgcgkafsq ssslcihqrv htgekpfkcd ecgkafsqst
      241 slcihqrvht kernhlkisv i
//
LOCUS       NP_001355758             808 aa            linear   ROD 27-APR-2025
DEFINITION  protein phosphatase 1 regulatory subunit 12B isoform 3 [Mus
            musculus].
ACCESSION   NP_001355758
VERSION     NP_001355758.1
DBSOURCE    REFSEQ: accession NM_001368829.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Ye,Z., Okamoto,R., Ito,H., Ito,R., Moriwaki,K., Ichikawa,M.,
            Kimena,L., Ali,Y., Ito,M., Gomez-Sanchez,C.E. and Dohi,K.
  TITLE     Myosin Light Chain Phosphatase Plays an Important Role in Cardiac
            Fibrosis in a Model of Mineralocorticoid Receptor-Associated
            Hypertension
  JOURNAL   J Am Heart Assoc 13 (5), e032828 (2024)
   PUBMED   38420846
  REMARK    GeneRIF: Myosin Light Chain Phosphatase Plays an Important Role in
            Cardiac Fibrosis in a Model of Mineralocorticoid
            Receptor-Associated Hypertension.
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Lee,E., May,H., Kazmierczak,K., Liang,J., Nguyen,N., Hill,J.A.,
            Gillette,T.G., Szczesna-Cordary,D. and Chang,A.N.
  TITLE     The MYPT2-regulated striated muscle-specific myosin light chain
            phosphatase limits cardiac myosin phosphorylation in vivo
  JOURNAL   J Biol Chem 300 (2), 105652 (2024)
   PUBMED   38224947
  REMARK    GeneRIF: The MYPT2-regulated striated muscle-specific myosin light
            chain phosphatase limits cardiac myosin phosphorylation in vivo.
REFERENCE   4  (residues 1 to 808)
  AUTHORS   Hu,T., Kalyanaraman,H., Pilz,R.B. and Casteel,D.E.
  TITLE     Phosphatase regulatory subunit MYPT2 knockout partially compensates
            for the cardiac dysfunction in mice caused by lack of myosin light
            chain kinase 3
  JOURNAL   J Biol Chem 299 (4), 104584 (2023)
   PUBMED   36889588
  REMARK    GeneRIF: Phosphatase regulatory subunit MYPT2 knockout partially
            compensates for the cardiac dysfunction in mice caused by lack of
            myosin light chain kinase 3.
REFERENCE   5  (residues 1 to 808)
  AUTHORS   Liu,K., Zhao,J., Chen,C., Xu,J., Bell,R.L., Hall,F.S., Koob,G.F.,
            Volkow,N.D., Qing,H. and Lin,Z.
  TITLE     Epistatic evidence for gender-dependant slow neurotransmission
            signalling in substance use disorders: PPP1R12B versus PPP1R1B
  JOURNAL   EBioMedicine 61, 103066 (2020)
   PUBMED   33096475
  REMARK    GeneRIF: Epistatic evidence for gender-dependant slow
            neurotransmission signalling in substance use disorders: PPP1R12B
            versus PPP1R1B.
REFERENCE   6  (residues 1 to 808)
  AUTHORS   Hughes,J.J., Alkhunaizi,E., Kruszka,P., Pyle,L.C., Grange,D.K.,
            Berger,S.I., Payne,K.K., Masser-Frye,D., Hu,T., Christie,M.R.,
            Clegg,N.J., Everson,J.L., Martinez,A.F., Walsh,L.E., Bedoukian,E.,
            Jones,M.C., Harris,C.J., Riedhammer,K.M., Choukair,D.,
            Fechner,P.Y., Rutter,M.M., Hufnagel,S.B., Roifman,M., Kletter,G.B.,
            Delot,E., Vilain,E., Lipinski,R.J., Vezina,C.M., Muenke,M. and
            Chitayat,D.
  TITLE     Loss-of-Function Variants in PPP1R12A: From Isolated Sex Reversal
            to Holoprosencephaly Spectrum and Urogenital Malformations
  JOURNAL   Am J Hum Genet 106 (1), 121-128 (2020)
   PUBMED   31883643
REFERENCE   7  (residues 1 to 808)
  AUTHORS   Mizutani,H., Okamoto,R., Moriki,N., Konishi,K., Taniguchi,M.,
            Fujita,S., Dohi,K., Onishi,K., Suzuki,N., Satoh,S., Makino,N.,
            Itoh,T., Hartshorne,D.J. and Ito,M.
  TITLE     Overexpression of myosin phosphatase reduces Ca(2+) sensitivity of
            contraction and impairs cardiac function
  JOURNAL   Circ J 74 (1), 120-128 (2010)
   PUBMED   19966500
  REMARK    GeneRIF: MYPT2 is truly the regulatory subunit of cardiac myosin
            phosphatase in-vivo and plays a significant role in modulating
            cardiac function.
REFERENCE   8  (residues 1 to 808)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   9  (residues 1 to 808)
  AUTHORS   Arimura,T., Suematsu,N., Zhou,Y.B., Nishimura,J., Satoh,S.,
            Takeshita,A., Kanaide,H. and Kimura,A.
  TITLE     Identification, characterization, and functional analysis of
            heart-specific myosin light chain phosphatase small subunit
  JOURNAL   J Biol Chem 276 (9), 6073-6082 (2001)
   PUBMED   11067852
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC117827.6 and AC131591.13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164139
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 58.24 cM"
     Protein         1..808
                     /product="protein phosphatase 1 regulatory subunit 12B
                     isoform 3"
                     /EC_number="3.1.3.53"
                     /note="myosin phosphatase target subunit 2; myosin
                     phosphatase-targeting subunit 2; protein phosphatase 1,
                     regulatory (inhibitor) subunit 12B"
                     /calculated_mol_wt=90636
     Region          <45..137
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          48..79
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          81..112
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          442..494
                     /region_name="IPD_PPP1R12"
                     /note="inhibitory phosphorylation domain of protein
                     phosphatase 1 regulatory subunit 12 (PPP1R12) family;
                     cl40436"
                     /db_xref="CDD:424067"
     Region          707..808
                     /region_name="PRKG1_interact"
                     /note="cGMP-dependent protein kinase interacting domain;
                     pfam15898"
                     /db_xref="CDD:464927"
     CDS             1..808
                     /gene="Ppp1r12b"
                     /gene_synonym="1810037O03Rik; 9530009M10Rik; Mypt2"
                     /coded_by="NM_001368829.1:532..2958"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:329251"
                     /db_xref="MGI:MGI:1916417"
ORIGIN      
        1 mkdllleqvk kqgvdleqsr keeeqqmlqd arqwlnsgri edvrqarsga talhvaaakg
       61 ysevlrlliq agyelnvqdh dgwtplhaaa hwgvkeacsi laealcdmdi rnklgqtpfd
      121 vadeglvehl emlqkkqdvl rseketrnkl iesdlnskfq sglfknkekm lyeeeipksq
      181 dteeenkess sssseeeege devsesetek eadkkpeatv nhsnseiksr imeqipapaq
      241 ntfsassarr lsslfnkaee pkdespsswr lglrktgshn mlsevansre alrdrgssiy
      301 rssssprisa llddkdkere nksyfsmlvp rrlsstsdie ekenresavn lvrsgshtrq
      361 lwrdeakgse tpqtiapsty tstylkrtpy ksqadstaek tadsvssstp lcvitnrpap
      421 stangvpaat vfssagtdps vearekrrsy ltpvrdeeae slrkarsrqa rqtrrstqgv
      481 tltdlqeaek tfsrsraerq aqeqpgekle dpgglegstk kqepsaaptk gagegrslee
      541 epiyhrlryp tqpdkpttpv spsasrpsly tgshllrtsr asgpdsense tsthataake
      601 mdtsekgead lddqssnrls vrerrrakdr rrgtginfwt ndedetdvse evkealherl
      661 srlesggtnp tssdsysdra sararreare arlasltsrv eedsnrdykk lyesaltenq
      721 klktklqeaq leladikakl ekmaqqkqek tsdrssvlev ekrerraler kmsemeeemk
      781 vltelksdnq rlkdengali rvisklsk
//
LOCUS       NP_438171                525 aa            linear   PRI 27-APR-2025
DEFINITION  coronin-2A [Homo sapiens].
ACCESSION   NP_438171
VERSION     NP_438171.1
DBSOURCE    REFSEQ: accession NM_052820.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Kase-Kato,I., Asai,S., Minemura,C., Tsuneizumi,K., Oshima,S.,
            Koma,A., Kasamatsu,A., Hanazawa,T., Uzawa,K. and Seki,N.
  TITLE     Molecular Pathogenesis of the Coronin Family: CORO2A Facilitates
            Migration and Invasion Abilities in Oral Squamous Cell Carcinoma
  JOURNAL   Int J Mol Sci 22 (23), 12684 (2021)
   PUBMED   34884487
  REMARK    GeneRIF: Molecular Pathogenesis of the Coronin Family: CORO2A
            Facilitates Migration and Invasion Abilities in Oral Squamous Cell
            Carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Lim,K.H., Choi,J.H., Park,J.H., Cho,H.J., Park,J.J., Lee,E.J.,
            Li,L., Choi,Y.K. and Baek,K.H.
  TITLE     Ubiquitin specific protease 19 involved in transcriptional
            repression of retinoic acid receptor by stabilizing CORO2A
  JOURNAL   Oncotarget 7 (23), 34759-34772 (2016)
   PUBMED   27129179
  REMARK    GeneRIF: The regulation of CORO2A through the deubiquitinating
            activity of USP19 affected the transcriptional repression activity
            of the retinoic acid receptor (RAR), suggesting that USP19 may be
            involved in the regulation of RAR-mediated adipogenesis.
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Rastetter,R.H., Blomacher,M., Drebber,U., Marko,M., Behrens,J.,
            Solga,R., Hojeili,S., Bhattacharya,K., Wunderlich,C.M.,
            Wunderlich,F.T., Odenthal,M., Ziemann,A., Eichinger,L. and
            Clemen,C.S.
  TITLE     Coronin 2A (CRN5) expression is associated with colorectal
            adenoma-adenocarcinoma sequence and oncogenic signalling
  JOURNAL   BMC Cancer 15, 638 (2015)
   PUBMED   26373535
  REMARK    GeneRIF: increased expression of coronin 2A is associated with the
            malignant phenotype of human colon carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Marshall,T.W., Aloor,H.L. and Bear,J.E.
  TITLE     Coronin 2A regulates a subset of focal-adhesion-turnover events
            through the cofilin pathway
  JOURNAL   J Cell Sci 122 (Pt 17), 3061-3069 (2009)
   PUBMED   19654210
  REMARK    GeneRIF: Coronin 2A and cofilin regulate a subset of
            focal-adhesion-turnover events.
REFERENCE   7  (residues 1 to 525)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 525)
  AUTHORS   Yoon,H.G., Chan,D.W., Reynolds,A.B., Qin,J. and Wong,J.
  TITLE     N-CoR mediates DNA methylation-dependent repression through a
            methyl CpG binding protein Kaiso
  JOURNAL   Mol Cell 12 (3), 723-734 (2003)
   PUBMED   14527417
REFERENCE   9  (residues 1 to 525)
  AUTHORS   Yoon,H.G., Chan,D.W., Huang,Z.Q., Li,J., Fondell,J.D., Qin,J. and
            Wong,J.
  TITLE     Purification and functional characterization of the human N-CoR
            complex: the roles of HDAC3, TBL1 and TBLR1
  JOURNAL   EMBO J 22 (6), 1336-1346 (2003)
   PUBMED   12628926
  REMARK    GeneRIF: This protein is one of 10-12 associated proteins in the
            purified N-CoR complex.
REFERENCE   10 (residues 1 to 525)
  AUTHORS   Zaphiropoulos,P.G. and Toftgard,R.
  TITLE     cDNA cloning of a novel WD repeat protein mapping to the 9q22.3
            chromosomal region
  JOURNAL   DNA Cell Biol 15 (12), 1049-1056 (1996)
   PUBMED   8985118
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC011690.2, AK292788.1,
            AL137073.13 and BM976925.1.
            
            Summary: This gene encodes a member of the WD repeat protein
            family. WD repeats are minimally conserved regions of approximately
            40 amino acids typically bracketed by gly-his and trp-asp (GH-WD),
            which may facilitate formation of heterotrimeric or multiprotein
            complexes. Members of this family are involved in a variety of
            cellular processes, including cell cycle progression, signal
            transduction, apoptosis, and gene regulation. This protein contains
            5 WD repeats, and has a structural similarity with actin-binding
            proteins: the D. discoideum coronin and the human p57 protein,
            suggesting that this protein may also be an actin-binding protein
            that regulates cell motility. Alternative splicing of this gene
            generates 2 transcript variants. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) contains a distinct 5' UTR
            transcribed from an alternate exon, as compared to variant 1.
            Variants 1 and 2 encode the same protein and contain the same 3'
            UTR.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011690.2, AK292788.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375077.5/ ENSP00000364218.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.33"
     Protein         1..525
                     /product="coronin-2A"
                     /note="WD protein IR10; coronin-like protein B; WD-repeat
                     protein 2; WD repeat-containing protein 2; coronin, actin
                     binding protein, 2A"
                     /calculated_mol_wt=59632
     Region          10..518
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          24..71
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92828.2)"
     Region          40..80
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          72..122
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92828.2)"
     Region          86..130
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          130..170
                     /region_name="WD repeat"
     Region          135..170
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..214
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92828.2)"
     Region          184..219
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          220..263
                     /region_name="WD repeat"
     Region          225..266
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          269..308
                     /region_name="WD repeat"
     Region          273..312
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..525
                     /gene="CORO2A"
                     /gene_synonym="CLIPINB; IR10; WDR2"
                     /coded_by="NM_052820.4:80..1657"
                     /db_xref="CCDS:CCDS6735.1"
                     /db_xref="GeneID:7464"
                     /db_xref="HGNC:HGNC:2255"
                     /db_xref="MIM:602159"
ORIGIN      
        1 mswhpqyrss kfrhvfgkpa skencydsvp itrsvhdnhf cavnphfiav vtecagggaf
       61 lviplhqtgk ldphypkvcg hrgnvldvkw npfddfeias csedatikiw sipkqlltrn
      121 ltayrkelvg harrvglvew hptaanilfs agydykvmiw nldtkesvit spmstischq
      181 dvilsmsfnt ngsllattck drkirvidpr agtvlqeasy kghraskvlf lgnlkklmst
      241 gtsrwnnrqv alwdqdnlsv plmeedldgs sgvlfpfyda dtsmlyvvgk gdgniryyev
      301 sadkphlsyl teyrsynpqk gigvmpkrgl dvssceifrf yklittksli epismivprr
      361 sesyqediyp ptagaqpslt aqewlsgmnr dpilvslrpg sellrphplp aerpifnsma
      421 pasprllnqt eklaaedgwr ssslleekmp rwaaehrlee kktwltngfd vfecpppkte
      481 nellqmfyrq qeeirrlrel ltqrevqakq leleiknlrm gseql
//
LOCUS       NP_031405               2433 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-binding cassette sub-family A member 2 isoform 1 [Mus
            musculus].
ACCESSION   NP_031405
VERSION     NP_031405.2
DBSOURCE    REFSEQ: accession NM_007379.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 2433)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 2433)
  AUTHORS   Davis,W. Jr.
  TITLE     The ATP-Binding Cassette Transporter-2 (ABCA2) Overexpression
            Modulates Sphingosine Levels and Transcription of the Amyloid
            Precursor Protein (APP) Gene
  JOURNAL   Curr Alzheimer Res 12 (9), 847-859 (2015)
   PUBMED   26510981
  REMARK    GeneRIF: Study suggests that ABCA2 modulation of sphingolipid
            metabolism activates a signaling pathway that regulates amyloid
            precursor protein transcription
REFERENCE   3  (residues 1 to 2433)
  AUTHORS   Thompson,C.L., Ng,L., Menon,V., Martinez,S., Lee,C.K.,
            Glattfelder,K., Sunkin,S.M., Henry,A., Lau,C., Dang,C.,
            Garcia-Lopez,R., Martinez-Ferre,A., Pombero,A., Rubenstein,J.L.R.,
            Wakeman,W.B., Hohmann,J., Dee,N., Sodt,A.J., Young,R., Smith,K.,
            Nguyen,T.N., Kidney,J., Kuan,L., Jeromin,A., Kaykas,A., Miller,J.,
            Page,D., Orta,G., Bernard,A., Riley,Z., Smith,S., Wohnoutka,P.,
            Hawrylycz,M.J., Puelles,L. and Jones,A.R.
  TITLE     A high-resolution spatiotemporal atlas of gene expression of the
            developing mouse brain
  JOURNAL   Neuron 83 (2), 309-323 (2014)
   PUBMED   24952961
REFERENCE   4  (residues 1 to 2433)
  AUTHORS   Haller,J.F., Cavallaro,P., Hernandez,N.J., Dolat,L., Soscia,S.J.,
            Welti,R., Grabowski,G.A., Fitzgerald,M.L. and Freeman,M.W.
  TITLE     Endogenous beta-glucocerebrosidase activity in Abca12/epidermis
            elevates ceramide levels after topical lipid application but does
            not restore barrier function
  JOURNAL   J Lipid Res 55 (3), 493-503 (2014)
   PUBMED   24293640
REFERENCE   5  (residues 1 to 2433)
  AUTHORS   Davis,W. Jr.
  TITLE     The ATP-binding cassette transporter-2 (ABCA2) regulates
            esterification of plasma membrane cholesterol by modulation of
            sphingolipid metabolism
  JOURNAL   Biochim Biophys Acta 1841 (1), 168-179 (2014)
   PUBMED   24201375
  REMARK    GeneRIF: control of ABCA2 expression level may be a key locus of
            regulation for esterification of plasma membrane-derived
            cholesterol through modulation of sphingolipid metabolism.
REFERENCE   6  (residues 1 to 2433)
  AUTHORS   Kasahara,M., Hayashi,M., Tanaka,K., Inoko,H., Sugaya,K., Ikemura,T.
            and Ishibashi,T.
  TITLE     Chromosomal localization of the proteasome Z subunit gene reveals
            an ancient chromosomal duplication involving the major
            histocompatibility complex
  JOURNAL   Proc Natl Acad Sci U S A 93 (17), 9096-9101 (1996)
   PUBMED   8799160
REFERENCE   7  (residues 1 to 2433)
  AUTHORS   Allikmets,R., Gerrard,B., Glavac,D., Ravnik-Glavac,M.,
            Jenkins,N.A., Gilbert,D.J., Copeland,N.G., Modi,W. and Dean,M.
  TITLE     Characterization and mapping of three new mammalian ATP-binding
            transporter genes from an EST database
  JOURNAL   Mamm Genome 6 (2), 114-117 (1995)
   PUBMED   7766993
REFERENCE   8  (residues 1 to 2433)
  AUTHORS   Pilz,A., Woodward,K., Povey,S. and Abbott,C.
  TITLE     Comparative mapping of 50 human chromosome 9 loci in the laboratory
            mouse
  JOURNAL   Genomics 25 (1), 139-149 (1995)
   PUBMED   7774911
REFERENCE   9  (residues 1 to 2433)
  AUTHORS   Luciani,M.F., Denizot,F., Savary,S., Mattei,M.G. and Chimini,G.
  TITLE     Cloning of two novel ABC transporters mapping on human chromosome 9
  JOURNAL   Genomics 21 (1), 150-159 (1994)
   PUBMED   8088782
REFERENCE   10 (residues 1 to 2433)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: from microorganisms to man
  JOURNAL   Annu Rev Cell Biol 8, 67-113 (1992)
   PUBMED   1282354
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CJ126415.1, AK169438.1, AL732557.4 and CJ263864.1.
            
            On Jul 7, 2006 this sequence version replaced NP_031405.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK169438.1, X75927.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2433
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 17.25 cM"
     Protein         1..2433
                     /product="ATP-binding cassette sub-family A member 2
                     isoform 1"
                     /note="ATP-binding cassette transporter 2; ATP-binding
                     cassette 2; ATP-binding cassette, sub-family A (ABC1),
                     member 2"
                     /calculated_mol_wt=270395
     Region          1..2367
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     CDS             1..2433
                     /gene="Abca2"
                     /gene_synonym="Abc2; D2H0S1474E; mKIAA1062"
                     /coded_by="NM_007379.3:172..7473"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS15773.1"
                     /db_xref="GeneID:11305"
                     /db_xref="MGI:MGI:99606"
ORIGIN      
        1 mgflhqlqll lwknvtlkrr spwvlafeif iplvlffill glrqkkptis vkeafytaap
       61 ltsagilpvm qslcpdgqrd efgflqyans tvtqllerlh rvveegnlfd pvrpslgsel
      121 ealrqrleal ssgpgtwesh sarpavssfs ldsvardqre lwrflmqnls lpnstaqall
      181 aarvdpsevy rllfgplpdl dgklgflrkq epwsrlgsnp llqmeellla palleqltca
      241 pgsgelgril tmpeghqvdl qgyrdavcsg qataraqrfs dlaaelrnql dtakiaqqlg
      301 fdvpngsdpq pqapspqslp allgdlldaq kllqdvdvls alalllpqga cagqasapqa
      361 sslnglanst gigansgsnt tveegtqspv spaspdtlqg qcsafvqlwa glqpilcgnn
      421 rtiepealrr gnmsslgfts keqrnlgllv hlmtsnpkil yapvgseadr vilkanetfa
      481 fvgnvthyaq vwlnisteir sfleqgrlqq hlqwlqqyva dlqlhpeamn lsleelppal
      541 rqdfslpngt allqqldtid naacgwiqfm skvsvdifkg fpdeesivny tlnqayqdnv
      601 tvfasvifqt rkdgslpphv hykirqnssf tektneirra ywrpgpntgg rfyflygfvw
      661 iqdmmeraii ntfvghdvve pgnyvqmfpy pcytrddflf viehmmplcm viswvysvam
      721 tiqhivaeke hrlkevmktm glnnavhwva wfitgfvqls isvtaltail kygqvlmhsh
      781 vliiwlflav yavatimfcf lvsvlyskak lasacggiiy flsyvpymyv aireevahdk
      841 itafekcias lmsttafglg skyfalyeva gvgiqwhtfs qspvegddfn lllavtmlmv
      901 dtvvygvltw yieavhpgmy glprpwyfpl qksywlgsgr teawewswpw ahtprlsvme
      961 edqacamesr hfeetrgmee epthlplvvc vdkltkvykn dkkmalnkls lnlyenqvvs
     1021 flghngagkt ttmsiltglf pptsgsatiy ghdirtemde irknlgmcpq hnvlfdrltv
     1081 eehlwfysrl ksmaqeeirk etdkmiedle lsnkrhslvq tlsggmkrkl svaiafvggs
     1141 raiildepta gvdpyarrai wdlilkykpg rtillsthhm deadllgdri aiishgklkc
     1201 cgsplflkga ygdgyrltlv kqpaepgtsq epglasspsg cprlsscsep qvsqfirkhv
     1261 assllvsdts telsyilpse avkkgaferl fqqlehslda lhlssfglmd ttleevflkv
     1321 seedqslens eadvkesrkd vlpgaeglta vggqagnlar cselaqsqas lqsassvgsa
     1381 rgeegtgysd gygdyrplfd nlqdpdnvsl qeaemealaq vgqgsrkleg wwlkmrqfhg
     1441 llvkrfhcar rnskalcsqi llpaffvcva mtvalsvpei gdlpplvlsp sqyhnytqpr
     1501 gnfipyanee rqeyrlrlsp daspqqlvst frlpsgvgat cvlkspangs lgpmlnlssg
     1561 esrllaarff dsmclesftq glplsnfvpp ppspapsdsp vspdedslqa wnmslpptag
     1621 petwtsapsl prlvhepvrc tcsaqgtgfs cpssvgghpp qmrvvtgdil tditghnvse
     1681 yllftsdrfr lhrygaitfg nvqksipasf garvppmvrk iavrrvaqvl ynnkgyhsmp
     1741 tylnslnnai lranlpkskg npaaygitvt nhpmnktsas lsldyllqgt dvviaifiiv
     1801 amsfvpasfv vflvaekstk akhlqfvsgc npviywlany vwdmlnylvp atccviilfv
     1861 fdlpaytspt nfpavlslfl lygwsitpim ypasfwfevp ssayvflivi nlfigitatv
     1921 atfllqlfeh dkdlkvvnsy lkscflifpn ynlghglmem ayneyineyy akigqfdkmk
     1981 spfewdivtr glvamtvegf vgffltimcq ynflrqpqrl pvstkpvedd vdvaserqrv
     2041 lrgdadndmv kienltkvyk srkigrilav drlclgvrpg ecfgllgvng agktstfkml
     2101 tgdesttgge afvnghsvlk dllqvqqslg ycpqfdalfd eltarehlql ytrlrgipwk
     2161 deaqvvkwal ekleltkyad kpagtysggn krklstaial igypafifld epttgmdpka
     2221 rrflwnlild liktgrsvvl tshsmeecea lctrlaimvn grlrclgsiq hlknrfgdgy
     2281 mitvrtkssq nvkdvvrffn rnfpeamlke rhhtkvqyql ksehislaqv fskmeqvvgv
     2341 lgiedysvsq ttldnvfvnf akkqsdnveq qeaepsslps plgllsllrp rpaptelral
     2401 vadepedldt edeglisfee eraqlsfntd tlc
//
LOCUS       NP_778236                666 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX51 [Homo sapiens].
ACCESSION   NP_778236
VERSION     NP_778236.2
DBSOURCE    REFSEQ: accession NM_175066.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Wang,X., Liu,H., Zhao,C., Li,W., Xu,H. and Chen,Y.
  TITLE     The DEAD-box RNA helicase 51 controls non-small cell lung cancer
            proliferation by regulating cell cycle progression via multiple
            pathways
  JOURNAL   Sci Rep 6, 26108 (2016)
   PUBMED   27198888
  REMARK    GeneRIF: these data suggest that DDX51 aids cell cancer
            proliferation by regulating multiple signaling pathways
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 666)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK097078.1, AC138466.12, BC029279.1, BC040185.2 and BC063603.1.
            
            On Aug 4, 2007 this sequence version replaced NP_778236.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040185.2, AK097078.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397333.4/ ENSP00000380495.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..666
                     /product="ATP-dependent RNA helicase DDX51"
                     /EC_number="3.6.4.13"
                     /note="DEAD box protein 51; DEAD (Asp-Glu-Ala-Asp) box
                     polypeptide 51"
                     /calculated_mol_wt=72326
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Region          9..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Region          <78..149
                     /region_name="LGT"
                     /note="Prolipoprotein diacylglyceryl transferase; cl00478"
                     /db_xref="CDD:469786"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Region          209..453
                     /region_name="DEADc_DDX51"
                     /note="DEAD-box helicase domain of DEAD box protein 51;
                     cd17956"
                     /db_xref="CDD:350714"
     Site            order(217..218,220..222,225,257..264)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350714"
     Region          221..229
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Region          371..374
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Region          479..609
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(568,570,595,598..599)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     CDS             1..666
                     /gene="DDX51"
                     /coded_by="NM_175066.4:24..2024"
                     /db_xref="CCDS:CCDS41865.1"
                     /db_xref="GeneID:317781"
                     /db_xref="HGNC:HGNC:20082"
ORIGIN      
        1 malfyvaryp gpdaaaaagp egaeagahgr arallerlqs rarerqqqre paqteaaast
       61 epatrrrrrp rrrrrvndae pgspeapqgk rrkadgedag aesneeapge psagsseeap
      121 gepsagssee apgerstsas aeaapdgpal eeaagplvpg lvlggfgkrk apkvqpflpr
      181 wlaepncvrr nvtedlvpie dipdvhpdlq kqlrahgiss yfpvqaavip allesaacgf
      241 lvgrggyrps dlcvsaptgs gktlafvipv vqallsrvvc hiralvvlpt kelaqqvskv
      301 fniytdatpl rvslvtgqks lakeqeslvq ktadgyrcla divvatpgrl vdhidqtpgf
      361 slqqlrflii deadrmidsm hqswlprvva aafqsedpad pcallqrrqa qavtaastcc
      421 pqmplqkllf satltqnpek lqqlglhqpr lfstglahrg ledtdgdgds gkyafpvglt
      481 hhyvpcslss kplvvlhlvl emgfsrvlcf tnsrenshrl fllvqafggv dvaefssryg
      541 pgqrrmilkq feqgkiqlli stdatargid vqgvelvvny dapqylrtyv hrvgrtarag
      601 ktgqaftlll kvqerrflrm lteagapelq rhelsskllq plvpryeeal sqleesvkee
      661 rkqraa
//
LOCUS       NP_004929               1430 aa            linear   PRI 27-APR-2025
DEFINITION  death-associated protein kinase 1 [Homo sapiens].
ACCESSION   NP_004929
VERSION     NP_004929.2
DBSOURCE    REFSEQ: accession NM_004938.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1430)
  AUTHORS   Fu,M., Gu,J., Yu,D., Wang,M., Zhang,J., Ji,R., Jiang,P. and
            Zhang,X.
  TITLE     Circ1811 suppresses gastric cancer progression by regulating the
            miR-632/DAPK1 axis
  JOURNAL   Gene 910, 148331 (2024)
   PUBMED   38438055
  REMARK    GeneRIF: Circ1811 suppresses gastric cancer progression by
            regulating the miR-632/DAPK1 axis.
REFERENCE   2  (residues 1 to 1430)
  AUTHORS   Yang,J., Liu,Y., Geng,Q. and Wang,B.
  TITLE     Death associated protein kinase 1 predicts the prognosis and the
            immunotherapy response of various cancers
  JOURNAL   Mol Biol Rep 51 (1), 670 (2024)
   PUBMED   38787485
  REMARK    GeneRIF: Death associated protein kinase 1 predicts the prognosis
            and the immunotherapy response of various cancers.
            Erratum:[Mol Biol Rep. 2024 Jul 23;51(1):846. doi:
            10.1007/s11033-024-09709-w. PMID: 39042224]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1430)
  AUTHORS   Wang,F., Hu,D., Lou,X., Wang,Y., Wang,L., Zhang,T., Yan,Z., Meng,N.
            and Zou,Y.
  TITLE     BNIP3 and DAPK1 methylation in peripheral blood leucocytes are
            noninvasive biomarkers for gastric cancer
  JOURNAL   Gene 898, 148109 (2024)
   PUBMED   38142898
  REMARK    GeneRIF: BNIP3 and DAPK1 methylation in peripheral blood leucocytes
            are noninvasive biomarkers for gastric cancer.
REFERENCE   4  (residues 1 to 1430)
  AUTHORS   Luo,Q.Q., Tian,Y., Qu,G.J., Huang,K., Hu,P.P., Xue,Y., Hu,B.F. and
            Luo,S.S.
  TITLE     The targeting of DAPK1 with miR-190a-3p promotes autophagy in
            trophoblast cells
  JOURNAL   Mol Reprod Dev 91 (1), e23724 (2024)
   PUBMED   38282318
  REMARK    GeneRIF: The targeting of DAPK1 with miR-190a-3p promotes autophagy
            in trophoblast cells.
REFERENCE   5  (residues 1 to 1430)
  AUTHORS   Takata,K., Miyata-Takata,T. and Sato,Y.
  TITLE     Frequent CDKN2B/P15 and DAPK1 methylation in duodenal follicular
            lymphoma is related to duodenal reactive lymphoid hyperplasia
  JOURNAL   J Clin Exp Hematop 64 (2), 129-137 (2024)
   PUBMED   38925973
  REMARK    GeneRIF: Frequent CDKN2B/P15 and DAPK1 methylation in duodenal
            follicular lymphoma is related to duodenal reactive lymphoid
            hyperplasia.
REFERENCE   6  (residues 1 to 1430)
  AUTHORS   Jin,Y., Blue,E.K., Dixon,S., Hou,L., Wysolmerski,R.B. and
            Gallagher,P.J.
  TITLE     Identification of a new form of death-associated protein kinase
            that promotes cell survival
  JOURNAL   J Biol Chem 276 (43), 39667-39678 (2001)
   PUBMED   11485996
REFERENCE   7  (residues 1 to 1430)
  AUTHORS   Tereshko,V., Teplova,M., Brunzelle,J., Watterson,D.M. and Egli,M.
  TITLE     Crystal structures of the catalytic domain of human protein kinase
            associated with apoptosis and tumor suppression
  JOURNAL   Nat Struct Biol 8 (10), 899-907 (2001)
   PUBMED   11573098
REFERENCE   8  (residues 1 to 1430)
  AUTHORS   Inbal,B., Shani,G., Cohen,O., Kissil,J.L. and Kimchi,A.
  TITLE     Death-associated protein kinase-related protein 1, a novel
            serine/threonine kinase involved in apoptosis
  JOURNAL   Mol Cell Biol 20 (3), 1044-1054 (2000)
   PUBMED   10629061
REFERENCE   9  (residues 1 to 1430)
  AUTHORS   Feinstein,E., Druck,T., Kastury,K., Berissi,H., Goodart,S.A.,
            Overhauser,J., Kimchi,A. and Huebner,K.
  TITLE     Assignment of DAP1 and DAPK--genes that positively mediate
            programmed cell death triggered by IFN-gamma--to chromosome regions
            5p12.2 and 9q34.1, respectively
  JOURNAL   Genomics 29 (1), 305-307 (1995)
   PUBMED   8530096
REFERENCE   10 (residues 1 to 1430)
  AUTHORS   Deiss,L.P., Feinstein,E., Berissi,H., Cohen,O. and Kimchi,A.
  TITLE     Identification of a novel serine/threonine kinase and a novel 15-kD
            protein as potential mediators of the gamma interferon-induced cell
            death
  JOURNAL   Genes Dev 9 (1), 15-30 (1995)
   PUBMED   7828849
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR002874.1, AK295119.1,
            BC113660.1, CX872304.1, BG110813.1 and H77515.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 10, 2006 this sequence version replaced NP_004929.1.
            
            Summary: Death-associated protein kinase 1 is a positive mediator
            of gamma-interferon induced programmed cell death. DAPK1 encodes a
            structurally unique 160-kD calmodulin dependent serine-threonine
            kinase that carries 8 ankyrin repeats and 2 putative P-loop
            consensus sites. It is a tumor suppressor candidate. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Dec 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, 3 and 4 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.202596.1,
                                           SRR1803617.102821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000408954.8/ ENSP00000386135.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1430
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..1430
                     /product="death-associated protein kinase 1"
                     /EC_number="2.7.11.1"
                     /note="DAP kinase 1"
                     /calculated_mol_wt=159916
     Region          7..275
                     /region_name="STKc_DAPK1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Death-Associated Protein Kinase 1; cd14194"
                     /db_xref="CDD:271096"
     Site            order(18,21,23..24,53..54,100,103,106..107,222)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:271096"
     Site            order(19..25,27,40,42,77,93..94,96,100,102,139,141,
                     143..144,146,160..161,164,179..182)
                     /site_type="active"
                     /db_xref="CDD:271096"
     Site            order(19..25,27,40,42,77,93..94,96,100,139,143..144,146,
                     160..161)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271096"
     Site            order(23,100,102,139,141,143,164,179..182)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271096"
     Site            160..182
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271096"
     Region          267..334
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1 and RPS6KA3.
                     /evidence=ECO:0000269|PubMed:16213824; propagated from
                     UniProtKB/Swiss-Prot (P53355.6)"
     Region          292..301
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:11579085,
                     ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:17056602;
                     propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P53355.6)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P53355.6)"
     Region          <338..409
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          378..409
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          378..407
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Region          392..668
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          411..440
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Region          412..442
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(413,417..418,421..423,425..426,430,433,442,444,446,
                     450..451,454..456,458..459,463,466,475,477,479,483..484,
                     487..489,491..492,496,499,508)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          444..475
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          444..473
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Region          477..508
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          477..506
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Region          510..541
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          510..539
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Site            order(543,545,549..550,553..555,557..558,562,565,574,576,
                     578,582..583,586..588,590..591,595,598,607,609,611,
                     615..616,619..621,623..624,628,631)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          543..574
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          543..572
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Region          576..607
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          576..605
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Region          609..638
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          609..638
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Site            734
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:15616583; propagated from
                     UniProtKB/Swiss-Prot (P53355.6)"
     Region          875..904
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Site            1115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YE7; propagated from
                     UniProtKB/Swiss-Prot (P53355.6)"
     Region          1162..1196
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P53355.6)"
     Region          1308..1393
                     /region_name="Death_DAPK1"
                     /note="Death domain found in death-associated protein
                     kinase 1; cd08782"
                     /db_xref="CDD:260052"
     CDS             1..1430
                     /gene="DAPK1"
                     /gene_synonym="DAPK; ROCO3"
                     /coded_by="NM_004938.4:350..4642"
                     /db_xref="CCDS:CCDS43842.1"
                     /db_xref="GeneID:1612"
                     /db_xref="HGNC:HGNC:2674"
                     /db_xref="MIM:600831"
ORIGIN      
        1 mtvfrqenvd dyydtgeelg sgqfavvkkc rekstglqya akfikkrrtk ssrrgvsred
       61 ierevsilke iqhpnvitlh evyenktdvi lilelvagge lfdflaekes lteeeatefl
      121 kqilngvyyl hslqiahfdl kpenimlldr nvpkprikii dfglahkidf gnefknifgt
      181 pefvapeivn yeplgleadm wsigvityil lsgaspflgd tkqetlanvs avnyefedey
      241 fsntsalakd firrllvkdp kkrmtiqdsl qhpwikpkdt qqalsrkasa vnmekfkkfa
      301 arkkwkqsvr lislcqrlsr sflsrsnmsv arsddtldee dsfvmkaiih ainddnvpgl
      361 qhllgslsny dvnqpnkhgt pplliaagcg niqilqllik rgsridvqdk ggsnavywaa
      421 rhghvdtlkf lsenkcpldv kdksgemalh vaaryghadv aqllcsfgsn pniqdkeeet
      481 plhcaawhgy ysvakalcea gcnvniknre getplltasa rgyhdivecl aehgadlnac
      541 dkdghialhl avrrcqmevi ktllsqgcfv dyqdrhgntp lhvackdgnm pivvalcean
      601 cnldisnkyg rtplhlaann gildvvrylc lmgasvealt tdgktaedla rseqhehvag
      661 llarlrkdth rglfiqqlrp tqnlqprikl klfghsgsgk ttlveslkcg llrsffrrrr
      721 prlsstnssr fppsplaskp tvsvsinnly pgcenvsvrs rsmmfepglt kgmlevfvap
      781 thhphcsadd qstkaidiqn aylngvgdfs vwefsgnpvy fccydyfaan dptsihvvvf
      841 sleepyeiql nqvifwlsfl kslvpveepi afggklknpl qvvlvathad imnvprpagg
      901 efgydkdtsl lkeirnrfgn dlhisnklfv ldagasgskd mkvlrnhlqe irsqivsvcp
      961 pmthlcekii stlpswrkln gpnqlmslqq fvydvqdqln plaseedlrr iaqqlhstge
     1021 inimqsetvq dvllldprwl ctnvlgklls vetpralhhy rgrytvediq rlvpdsdvee
     1081 llqildamdi cardlssgtm vdvpaliktd nlhrswadee devmvyggvr ivpvehltpf
     1141 pcgifhkvqv nlcrwihqqs tegdadirlw vngcklanrg aellvllvnh gqgievqvrg
     1201 letekikccl lldsvcstie nvmattlpgl ltvkhylspq qlrehhepvm iyqprdffra
     1261 qtlketsltn tmggykesfs simcfgchdv ysqaslgmdi hasdlnlltr rklsrlldpp
     1321 dplgkdwcll amnlglpdlv akyntsngap kdflpsplha llrewttype stvgtlmskl
     1381 relgrrdaad fllkassvfk inldgngqea yasscnsgts ynsissvvsr
//
LOCUS       NP_002167                187 aa            linear   PRI 27-APR-2025
DEFINITION  interferon beta precursor [Homo sapiens].
ACCESSION   NP_002167
VERSION     NP_002167.1
DBSOURCE    REFSEQ: accession NM_002176.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Xu,Z., Tian,M., Tan,Q., Hao,P., Gao,Z., Li,C. and Jin,N.
  TITLE     FHL2 Inhibits SARS-CoV-2 Replication by Enhancing IFN-beta
            Expression through Regulating IRF-3
  JOURNAL   Int J Mol Sci 25 (1), 353 (2023)
   PUBMED   38203523
  REMARK    GeneRIF: FHL2 Inhibits SARS-CoV-2 Replication by Enhancing IFN-beta
            Expression through Regulating IRF-3.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Wright,O., Harris,A., Nguyen,V.D., Zhou,Y., Durand,M.,
            Jayyaratnam,A., Gormley,D., O'Neill,L.A.J., Triantafilou,K.,
            Nichols,E.M. and Booty,L.M.
  TITLE     C5aR2 Regulates STING-Mediated Interferon Beta Production in Human
            Macrophages
  JOURNAL   Cells 12 (23), 2707 (2023)
   PUBMED   38067135
  REMARK    GeneRIF: C5aR2 Regulates STING-Mediated Interferon Beta Production
            in Human Macrophages.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Schwanke,H., Stempel,M. and Brinkmann,M.M.
  TITLE     Of Keeping and Tipping the Balance: Host Regulation and Viral
            Modulation of IRF3-Dependent IFNB1 Expression
  JOURNAL   Viruses 12 (7), 733 (2020)
   PUBMED   32645843
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Teles,R.M., Graeber,T.G., Krutzik,S.R., Montoya,D., Schenk,M.,
            Lee,D.J., Komisopoulou,E., Kelly-Scumpia,K., Chun,R., Iyer,S.S.,
            Sarno,E.N., Rea,T.H., Hewison,M., Adams,J.S., Popper,S.J.,
            Relman,D.A., Stenger,S., Bloom,B.R., Cheng,G. and Modlin,R.L.
  TITLE     Type I interferon suppresses type II interferon-triggered human
            anti-mycobacterial responses
  JOURNAL   Science 339 (6126), 1448-1453 (2013)
   PUBMED   23449998
  REMARK    GeneRIF: IFN-gamma and its downstream antimicrobial genes were
            preferentially expressed in self-healing tuberculoid lesions and
            mediated antimicrobial activity against M.leprae in vitro; IFN-beta
            and its downstream genes,including IL-10, were induced in monocytes
            by M.leprae and preferentially expressed in disseminated and
            progressive lepromatous lesions
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Karpusas,M., Nolte,M., Benton,C.B., Meier,W., Lipscomb,W.N. and
            Goelz,S.
  TITLE     The crystal structure of human interferon beta at 2.2-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 94 (22), 11813-11818 (1997)
   PUBMED   9342320
REFERENCE   6  (residues 1 to 187)
  AUTHORS   Flores,I., Mariano,T.M. and Pestka,S.
  TITLE     Human interferon omega (omega) binds to the alpha/beta receptor
  JOURNAL   J Biol Chem 266 (30), 19875-19877 (1991)
   PUBMED   1834641
REFERENCE   7  (residues 1 to 187)
  AUTHORS   Silverman,R.H. and Sengupta,D.N.
  TITLE     Translational regulation by HIV leader RNA, TAT, and
            interferon-inducible enzymes
  JOURNAL   J Exp Pathol 5 (2), 69-77 (1990)
   PUBMED   1708818
REFERENCE   8  (residues 1 to 187)
  AUTHORS   Shepard,H.M., Leung,D., Stebbing,N. and Goeddel,D.V.
  TITLE     A single amino acid change in IFN-beta1 abolishes its antiviral
            activity
  JOURNAL   Nature 294 (5841), 563-565 (1981)
   PUBMED   6171735
REFERENCE   9  (residues 1 to 187)
  AUTHORS   Ohno,S. and Taniguchi,T.
  TITLE     Structure of a chromosomal gene for human interferon beta
  JOURNAL   Proc Natl Acad Sci U S A 78 (9), 5305-5309 (1981)
   PUBMED   16593086
REFERENCE   10 (residues 1 to 187)
  AUTHORS   Derynck,R., Content,J., DeClercq,E., Volckaert,G., Tavernier,J.,
            Devos,R. and Fiers,W.
  TITLE     Isolation and structure of a human fibroblast interferon gene
  JOURNAL   Nature 285 (5766), 542-547 (1980)
   PUBMED   6157094
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M28622.1 and AL390882.12.
            
            Summary: This gene encodes a cytokine that belongs to the
            interferon family of signaling proteins, which are released as part
            of the innate immune response to pathogens. The protein encoded by
            this gene belongs to the type I class of interferons, which are
            important for defense against viral infections. In addition, type I
            interferons are involved in cell differentiation and anti-tumor
            defenses. Following secretion in response to a pathogen, type I
            interferons bind a homologous receptor complex and induce
            transcription of genes such as those encoding inflammatory
            cytokines and chemokines. Overactivation of type I interferon
            secretion is linked to autoimmune diseases. Mice deficient for this
            gene display several phenotypes including defects in B cell
            maturation and increased susceptibility to viral infection.
            [provided by RefSeq, Sep 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: M28622.1, V00546.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in cytokine storm inflammatory
                                      response
            MANE Ensembl match     :: ENST00000380232.4/ ENSP00000369581.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.3"
     Protein         1..187
                     /product="interferon beta precursor"
                     /note="fibroblast interferon; interferon, beta 1,
                     fibroblast; interferon-beta"
                     /calculated_mol_wt=20027
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2285
     mat_peptide     22..187
                     /product="Interferon beta. /id=PRO_0000016400"
                     /note="propagated from UniProtKB/Swiss-Prot (P01574.1)"
                     /calculated_mol_wt=20027
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P70499; propagated from
                     UniProtKB/Swiss-Prot (P01574.1)"
     Region          27..185
                     /region_name="Interferon"
                     /note="Interferon alpha/beta domain; pfam00143"
                     /db_xref="CDD:459689"
     Site            order(29..30,33,36..37,40,43..44,100..101,103..104,
                     106..107,110,113..114,117..118,121)
                     /site_type="active"
                     /note="putative IFNAR-1 binding site [active]"
                     /db_xref="CDD:238047"
     Site            order(53..60,62..64,70..71,141..142,144..145,148..149,
                     151..152,155..160)
                     /site_type="active"
                     /note="putative IFNAR-2 binding site [active]"
                     /db_xref="CDD:238047"
     Site            101
                     /site_type="other"
                     /note="N-glycosylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238047"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:9342320; propagated from
                     UniProtKB/Swiss-Prot (P01574.1)"
     CDS             1..187
                     /gene="IFNB1"
                     /gene_synonym="IFB; IFF; IFN-beta; IFNB"
                     /coded_by="NM_002176.4:74..637"
                     /db_xref="CCDS:CCDS6495.1"
                     /db_xref="GeneID:3456"
                     /db_xref="HGNC:HGNC:5434"
                     /db_xref="MIM:147640"
ORIGIN      
        1 mtnkcllqia lllcfsttal smsynllgfl qrssnfqcqk llwqlngrle yclkdrmnfd
       61 ipeeikqlqq fqkedaalti yemlqnifai frqdssstgw netivenlla nvyhqinhlk
      121 tvleekleke dftrgklmss lhlkryygri lhylkakeys hcawtivrve ilrnfyfinr
      181 ltgylrn
//
LOCUS       NP_116106                434 aa            linear   PRI 27-APR-2025
DEFINITION  glycerol-3-phosphate acyltransferase 3 [Homo sapiens].
ACCESSION   NP_116106
VERSION     NP_116106.2
DBSOURCE    REFSEQ: accession NM_032717.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Fan,G., Li,Y., Zong,Y., Suo,X., Jia,Y., Gao,M. and Yang,X.
  TITLE     GPAT3 regulates the synthesis of lipid intermediate LPA and
            exacerbates Kupffer cell inflammation mediated by the ERK signaling
            pathway
  JOURNAL   Cell Death Dis 14 (3), 208 (2023)
   PUBMED   36964139
  REMARK    GeneRIF: GPAT3 regulates the synthesis of lipid intermediate LPA
            and exacerbates Kupffer cell inflammation mediated by the ERK
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Tanigawa,K., Hayashi,Y., Hama,K., Yamashita,A., Yokoyama,K.,
            Luo,Y., Kawashima,A., Maeda,Y., Nakamura,Y., Harada,A., Kiriya,M.,
            Karasawa,K. and Suzuki,K.
  TITLE     Mycobacterium leprae promotes triacylglycerol de novo synthesis
            through induction of GPAT3 expression in human premonocytic THP-1
            cells
  JOURNAL   PLoS One 16 (3), e0249184 (2021)
   PUBMED   33770127
  REMARK    GeneRIF: Mycobacterium leprae promotes triacylglycerol de novo
            synthesis through induction of GPAT3 expression in human
            premonocytic THP-1 cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Sim,M.F.M., Persiani,E., Talukder,M.M.U., Mcilroy,G.D., Roumane,A.,
            Edwardson,J.M. and Rochford,J.J.
  TITLE     Oligomers of the lipodystrophy protein seipin may co-ordinate GPAT3
            and AGPAT2 enzymes to facilitate adipocyte differentiation
  JOURNAL   Sci Rep 10 (1), 3259 (2020)
   PUBMED   32094408
  REMARK    GeneRIF: Oligomers of the lipodystrophy protein seipin may
            co-ordinate GPAT3 and AGPAT2 enzymes to facilitate adipocyte
            differentiation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Fan,S.H., Wang,Y.Y., Wu,Z.Y., Zhang,Z.F., Lu,J., Li,M.Q., Shan,Q.,
            Wu,D.M., Sun,C.H., Hu,B. and Zheng,Y.L.
  TITLE     AGPAT9 suppresses cell growth, invasion and metastasis by
            counteracting acidic tumor microenvironment through
            KLF4/LASS2/V-ATPase signaling pathway in breast cancer
  JOURNAL   Oncotarget 6 (21), 18406-18417 (2015)
   PUBMED   26110566
  REMARK    GeneRIF: Data show that 1-acylglycerol-3-phosphate
            O-acyltransferase 9 (AGPAT9) inhibit cell growth by regulating
            expression of KLF4/LASS2/V-ATPase proteins in breast cancer.
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Cao,J., Li,J.L., Li,D., Tobin,J.F. and Gimeno,R.E.
  TITLE     Molecular identification of microsomal
            acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de
            novo triacylglycerol synthesis
  JOURNAL   Proc Natl Acad Sci U S A 103 (52), 19695-19700 (2006)
   PUBMED   17170135
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Tang,W., Yuan,J., Chen,X., Gu,X., Luo,K., Li,J., Wan,B., Wang,Y.
            and Yu,L.
  TITLE     Identification of a novel human lysophosphatidic acid
            acyltransferase, LPAAT-theta, which activates mTOR pathway
  JOURNAL   J Biochem Mol Biol 39 (5), 626-635 (2006)
   PUBMED   17002884
  REMARK    GeneRIF: LPAAT-theta gene consisted of 12 exons and 11 introns, and
            mapped to chromosome 4q21.23, was ubiquitously expressed in 18
            human tissues and overexpression of LPAAT-theta can induce
            mTOR-dependent p70S6K and 4EBP1 phosphorylation in HEK293T cells.
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC096768.3, DA673378.1, AY358100.1 and BM841009.1.
            
            On Jun 10, 2002 this sequence version replaced NP_116106.1.
            
            Summary: This gene encodes a member of the lysophosphatidic acid
            acyltransferase protein family. The encoded protein is an enzyme
            which catalyzes the conversion of glycerol-3-phosphate to
            lysophosphatidic acid in the synthesis of triacylglycerol. Multiple
            alternatively spliced variants, encoding the same protein, have
            been identified. [provided by RefSeq, Jan 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ345298.1, SRR1660809.33345.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264409.5/ ENSP00000264409.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.23"
     Protein         1..434
                     /product="glycerol-3-phosphate acyltransferase 3"
                     /EC_number="2.3.1.51"
                     /EC_number="2.3.1.15"
                     /note="1-acylglycerol-3-phosphate O-acyltransferase 8;
                     lysophosphatidic acid acyltransferase theta; MAG-1;
                     GPAT-3; hGPAT3; 1-AGPAT 9; 1-AGP acyltransferase 9; lung
                     cancer metastasis-associated protein 1;
                     acyl-CoA:glycerol-3-phosphate acyltransferase 3;
                     endoplasmic reticulum associated GPAT;
                     1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9; testis
                     secretory sperm-binding protein Li 213e;
                     1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10;
                     1-acylglycerol-3-phosphate O-acyltransferase 9"
                     /calculated_mol_wt=48574
     Site            14..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53EU6.2)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53EU6.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53EU6.2)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53EU6.2)"
     Site            161..181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53EU6.2)"
     Region          199..408
                     /region_name="LPLAT_LPCAT1-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: LPCAT1-like; cd07991"
                     /db_xref="CDD:153253"
     Site            order(229,232,234,248..251,304..306)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153253"
     Region          229..234
                     /region_name="HXXXXD motif.
                     /evidence=ECO:0000250|UniProtKB:Q9D517"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53EU6.2)"
     CDS             1..434
                     /gene="GPAT3"
                     /gene_synonym="AGPAT 10; AGPAT10; AGPAT8; AGPAT9;
                     HMFN0839; LPAAT-theta; MAG1"
                     /coded_by="NM_032717.5:516..1820"
                     /db_xref="CCDS:CCDS3606.1"
                     /db_xref="GeneID:84803"
                     /db_xref="HGNC:HGNC:28157"
                     /db_xref="MIM:610958"
ORIGIN      
        1 megaelagki lstwltlvlg fillpsvfgv slgiseiymk ilvktlewat iriekgtpke
       61 silknsasvg iiqrdespme kglsglrgrd felsdvfyfs kkgleaived evtqrfssee
      121 lvswnlltrt nvnfqyislr ltmvwvlgvi vrycvllplr vtlafigisl lvigttlvgq
      181 lpdsslknwl selvhltccr icvralsgti hyhnkqyrpq kggicvanht spidvliltt
      241 dgcyamvgqv hgglmgiiqr amvkacphvw fersemkdrh lvtkrlkehi adkkklpili
      301 fpegtcinnt svmmfkkgsf eiggtihpva ikynpqfgda fwnsskynmv syllrmmtsw
      361 aivcdvwymp pmtreegeda vqfanrvksa iaiqggltel pwdgglkrak vkdifkeeqq
      421 knyskmivgn gsls
//
LOCUS       NP_001124506             297 aa            linear   PRI 27-APR-2025
DEFINITION  probable E3 SUMO-protein ligase RNF212 isoform a [Homo sapiens].
ACCESSION   NP_001124506
VERSION     NP_001124506.1
DBSOURCE    REFSEQ: accession NM_001131034.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Riera-Escamilla,A., Enguita-Marruedo,A., Moreno-Mendoza,D.,
            Chianese,C., Sleddens-Linkels,E., Contini,E., Benelli,M.,
            Natali,A., Colpi,G.M., Ruiz-Castane,E., Maggi,M., Baarends,W.M. and
            Krausz,C.
  TITLE     Sequencing of a 'mouse azoospermia' gene panel in azoospermic men:
            identification of RNF212 and STAG3 mutations as novel genetic
            causes of meiotic arrest
  JOURNAL   Hum Reprod 34 (6), 978-988 (2019)
   PUBMED   31125047
  REMARK    GeneRIF: For the first time, study reports biallelic variants in
            STAG3, in one sporadic patient, and a homozygous RNF212 variant, in
            the two brothers, as the genetic cause of non-obstructive
            azoospermia. Meiotic studies allowed the detection of the
            functional consequences of the mutations and provided information
            on the role of STAG3 and RNF212 in human male meiosis.
            Erratum:[Hum Reprod. 2020 Aug 1;35(8):1945-1946. doi:
            10.1093/humrep/deaa179. PMID: 32715309]
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Yu,C.H., Xie,T., Zhang,R.P. and A,Z.C.
  TITLE     Association of the common SNPs in RNF212, STAG3 and RFX2 gene with
            male infertility with azoospermia in Chinese population
  JOURNAL   Eur J Obstet Gynecol Reprod Biol 221, 109-112 (2018)
   PUBMED   29277047
  REMARK    GeneRIF: The polymorphism of SNP rs4045481 in RNF212 gene might be
            associated with azoospermia and genotype CC of this SNP may be a
            risk factor of azoospermia.
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Reynolds,A., Qiao,H., Yang,Y., Chen,J.K., Jackson,N., Biswas,K.,
            Holloway,J.K., Baudat,F., de Massy,B., Wang,J., Hoog,C., Cohen,P.E.
            and Hunter,N.
  TITLE     RNF212 is a dosage-sensitive regulator of crossing-over during
            mammalian meiosis
  JOURNAL   Nat Genet 45 (3), 269-278 (2013)
   PUBMED   23396135
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Kong,A., Thorleifsson,G., Stefansson,H., Masson,G., Helgason,A.,
            Gudbjartsson,D.F., Jonsdottir,G.M., Gudjonsson,S.A., Sverrisson,S.,
            Thorlacius,T., Jonasdottir,A., Hardarson,G.A., Palsson,S.T.,
            Frigge,M.L., Gulcher,J.R., Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Sequence variants in the RNF212 gene associate with genome-wide
            recombination rate
  JOURNAL   Science 319 (5868), 1398-1401 (2008)
   PUBMED   18239089
  REMARK    GeneRIF: genome search identified sequence variants in the 4p16.3
            region correlated with recombination rate in males & females;
            variants are located in the RNF212 gene, a putative ortholog of
            ZHP-3 gene essential for recombination & chiasma formation in C
            elegans
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Jantsch,V., Pasierbek,P., Mueller,M.M., Schweizer,D., Jantsch,M.
            and Loidl,J.
  TITLE     Targeted gene knockout reveals a role in meiotic recombination for
            ZHP-3, a Zip3-related protein in Caenorhabditis elegans
  JOURNAL   Mol Cell Biol 24 (18), 7998-8006 (2004)
   PUBMED   15340062
  REMARK    GeneRIF: This paper describes a partial transcript of the human
            RNF212 gene.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG701603.1, AK096160.1,
            BC101260.1, AC019103.8 and BC050356.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a RING finger protein that may function
            as a ubiquitin ligase. The encoded protein may be involved in
            meiotic recombination. This gene is located within a linkage
            disequilibrium block and polymorphisms in this gene may influence
            recombination rates. Alternate splicing results in multiple
            transcript variants.[provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC101260.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000433731.7/ ENSP00000389709.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..297
                     /product="probable E3 SUMO-protein ligase RNF212 isoform
                     a"
                     /note="probable E3 SUMO-protein ligase RNF212; probable E3
                     SUMO-protein transferase RNF212"
                     /calculated_mol_wt=33234
     Region          4..50
                     /region_name="RING-HC_RNF212"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 212 (RNF212) and similar proteins; cd16746"
                     /db_xref="CDD:438404"
     CDS             1..297
                     /gene="RNF212"
                     /gene_synonym="SPGF62; ZHP3"
                     /coded_by="NM_001131034.4:101..994"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46996.1"
                     /db_xref="GeneID:285498"
                     /db_xref="HGNC:HGNC:27729"
                     /db_xref="MIM:612041"
ORIGIN      
        1 manwvfcnrc fqpphrtscf sltncghvyc daclgkgkkn eclickapcr tvllskhtda
       61 diqaffmsid slckkysret sqilefqekh rkrllafyre kisrleeslr ksvlqieqlq
      121 smrssqqtaf stikssvstk phgcllpphs sapdrlesme vdlspspirk seiaagpari
      181 smisppqdgr mgphltasfc fipwltlskp pvpgecvisr gspcfcidvc phwllllafs
      241 sgrhgeltns ktlpiyaevq ravlfpfqqa egtldtfrtp avsvvfplcq ferkksf
//
LOCUS       NP_003755                287 aa            linear   PRI 27-APR-2025
DEFINITION  syntaxin-11 [Homo sapiens].
ACCESSION   NP_003755
VERSION     NP_003755.2
DBSOURCE    REFSEQ: accession NM_003764.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Kogl,T., Chang,H.F., Staniek,J., Chiang,S.C.C., Thoulass,G.,
            Lao,J., Weissert,K., Dettmer-Monaco,V., Geiger,K., Manna,P.T.,
            Beziat,V., Momenilandi,M., Tu,S.M., Keppler,S.J., Pattu,V.,
            Wolf,P., Kupferschmid,L., Tholen,S., Covill,L.E., Ebert,K.,
            Straub,T., Gross,M., Gather,R., Engel,H., Salzer,U., Schell,C.,
            Maier,S., Lehmberg,K., Cornu,T.I., Pircher,H., Shahrooei,M.,
            Parvaneh,N., Elling,R., Rizzi,M., Bryceson,Y.T., Ehl,S., Aichele,P.
            and Ammann,S.
  TITLE     Patients and mice with deficiency in the SNARE protein SYNTAXIN-11
            have a secondary B cell defect
  JOURNAL   J Exp Med 221 (7) (2024)
   PUBMED   38722309
  REMARK    GeneRIF: Patients and mice with deficiency in the SNARE protein
            SYNTAXIN-11 have a secondary B cell defect.
            Erratum:[J Exp Med. 2024 Jul 1;221(7):e2022112205142024c. doi:
            10.1084/jem.2022112205142024c. PMID: 38771261]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wang,J., Li,D.L., Zheng,L.F., Ren,S., Huang,Z.Q., Tao,Y., Liu,Z.,
            Shang,Y., Pang,D., Guo,H., Zeng,T., Wang,H.R., Huang,H., Du,X.,
            Ye,H., Zhou,H.M., Li,P. and Zhao,T.J.
  TITLE     Dynamic palmitoylation of STX11 controls injury-induced fatty acid
            uptake to promote muscle regeneration
  JOURNAL   Dev Cell 59 (3), 384-399 (2024)
   PUBMED   38198890
  REMARK    GeneRIF: Dynamic palmitoylation of STX11 controls injury-induced
            fatty acid uptake to promote muscle regeneration.
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Ganesan,S., Alvarez,N.N., Steiner,S., Fowler,K.M., Corona,A.K. and
            Roy,C.R.
  TITLE     Syntaxin 11 Contributes to the Interferon-Inducible Restriction of
            Coxiella burnetii Intracellular Infection
  JOURNAL   mBio 14 (1), e0354522 (2023)
   PUBMED   36728431
  REMARK    GeneRIF: Syntaxin 11 Contributes to the Interferon-Inducible
            Restriction of Coxiella burnetii Intracellular Infection.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Bahadir,A., Kader,S., Cebi,A.H., Erduran,E., Mutlu,M. and Aslan,Y.
  TITLE     Familial Hemophagocytic Lymphohistiocytosis With Heterozygous STX11
            and Homozygous UNC13D Mutations Diagnosed in the Neonatal Period
  JOURNAL   J Pediatr Hematol Oncol 44 (4), e866-e868 (2022)
   PUBMED   35293882
  REMARK    GeneRIF: Familial Hemophagocytic Lymphohistiocytosis With
            Heterozygous STX11 and Homozygous UNC13D Mutations Diagnosed in the
            Neonatal Period.
REFERENCE   5  (residues 1 to 287)
  AUTHORS   zur Stadt,U., Schmidt,S., Kasper,B., Beutel,K., Diler,A.S.,
            Henter,J.I., Kabisch,H., Schneppenheim,R., Nurnberg,P., Janka,G.
            and Hennies,H.C.
  TITLE     Linkage of familial hemophagocytic lymphohistiocytosis (FHL) type-4
            to chromosome 6q24 and identification of mutations in syntaxin 11
  JOURNAL   Hum Mol Genet 14 (6), 827-834 (2005)
   PUBMED   15703195
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Valdez,A.C., Cabaniols,J.P., Brown,M.J. and Roche,P.A.
  TITLE     Syntaxin 11 is associated with SNAP-23 on late endosomes and the
            trans-Golgi network
  JOURNAL   J Cell Sci 112 (Pt 6), 845-854 (1999)
   PUBMED   10036234
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Advani,R.J., Bae,H.R., Bock,J.B., Chao,D.S., Doung,Y.C.,
            Prekeris,R., Yoo,J.S. and Scheller,R.H.
  TITLE     Seven novel mammalian SNARE proteins localize to distinct membrane
            compartments
  JOURNAL   J Biol Chem 273 (17), 10317-10324 (1998)
   PUBMED   9553086
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Tang,B.L., Low,D.Y. and Hong,W.
  TITLE     Syntaxin 11: a member of the syntaxin family without a carboxyl
            terminal transmembrane domain
  JOURNAL   Biochem Biophys Res Commun 245 (2), 627-632 (1998)
   PUBMED   9571206
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Zhang,K., Astigarraga,I., Bryceson,Y., Lehmberg,K., Machowicz,R.,
            Marsh,R., Sieni,E., Wang,Z. and Nichols,K.E.
  TITLE     Familial Hemophagocytic Lymphohistiocytosis
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM150302.1, BC033519.1,
            BQ030324.1, AL135917.15, CR739089.1, AI791689.1 and BF941242.1.
            
            On Aug 15, 2003 this sequence version replaced NP_003755.1.
            
            Summary: This gene encodes a member of the syntaxin family.
            Syntaxins have been implicated in the targeting and fusion of
            intracellular transport vesicles. This family member may regulate
            protein transport among late endosomes and the trans-Golgi network.
            Mutations in this gene have been associated with familial
            hemophagocytic lymphohistiocytosis. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.380161.1,
                                           SRR1660809.237270.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367568.5/ ENSP00000356540.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.2"
     Protein         1..287
                     /product="syntaxin-11"
                     /calculated_mol_wt=33065
     Region          43..238
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          207..273
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(235,242,245)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            238
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     CDS             1..287
                     /gene="STX11"
                     /gene_synonym="FHL4; HLH4; HPLH4"
                     /coded_by="NM_003764.4:193..1056"
                     /db_xref="CCDS:CCDS5205.1"
                     /db_xref="GeneID:8676"
                     /db_xref="HGNC:HGNC:11429"
                     /db_xref="MIM:605014"
ORIGIN      
        1 mkdrlaelld lskqydqqfp dgddefdsph edivfetdhi leslyrdird iqdenqllva
       61 dvkrlgkqna rfltsmrrls sikrdtnsia kaikargevi hcklramkel seaaeaqhgp
      121 hsavarisra qynaltltfq ramhdynqae mkqrdnckir iqrqleimgk evsgdqiedm
      181 feqgkwdvfs enlladvkga raalneiesr hrellrlesr irdvhelflq mavlvekqad
      241 tlnvielnvq ktvdytgqak aqvrkavqye eknpcrtlcc fccpclk
//
LOCUS       NP_057060                451 aa            linear   PRI 27-APR-2025
DEFINITION  sorting nexin-7 isoform a [Homo sapiens].
ACCESSION   NP_057060
VERSION     NP_057060.2
DBSOURCE    REFSEQ: accession NM_015976.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Anton,Z., Betin,V.M.S., Simonetti,B., Traer,C.J., Attar,N.,
            Cullen,P.J. and Lane,J.D.
  TITLE     A heterodimeric SNX4--SNX7 SNX-BAR autophagy complex coordinates
            ATG9A trafficking for efficient autophagosome assembly
  JOURNAL   J Cell Sci 133 (14) (2020)
   PUBMED   32513819
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Xu,S., Zhang,L. and Brodin,L.
  TITLE     Overexpression of SNX7 reduces Abeta production by enhancing
            lysosomal degradation of APP
  JOURNAL   Biochem Biophys Res Commun 495 (1), 12-19 (2018)
   PUBMED   29080748
  REMARK    GeneRIF: Overexpression of SNX7 in HEK293T cells reduces the levels
            of secreted Abeta and beta-cleaved N-terminal APP fragments
            (sAPPbeta). Moreover, SNX7 overexpression caused a significant
            reduction of the steady-state levels of APP as well as of the cell
            surface APP levels.
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Zhang,X., Bocca,S., Franchi,A., Anderson,S., Kaur,M., Bajic,V.B.
            and Oehninger,S.
  TITLE     Do GnRH analogues directly affect human endometrial epithelial cell
            gene expression?
  JOURNAL   Mol Hum Reprod 16 (5), 347-360 (2010)
   PUBMED   20203127
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Orlacchio,A., Kawarai,T., Gaudiello,F., St George-Hyslop,P.H.,
            Floris,R. and Bernardi,G.
  TITLE     New locus for hereditary spastic paraplegia maps to chromosome
            1p31.1-1p21.1
  JOURNAL   Ann Neurol 58 (3), 423-429 (2005)
   PUBMED   16130112
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627442.10.
            
            On Jul 17, 2008 this sequence version replaced NP_057060.1.
            
            Summary: This gene encodes a member of the sorting nexin family.
            Members of this family contain a phox (PX) domain, which is a
            phosphoinositide binding domain, and are involved in intracellular
            trafficking. This protein does not contain a coiled coil region
            like some family members, and its exact function is unknown.
            Alternative splicing results in multiple transcript variants. A
            related pseudogene has been identified on chromosome 11. [provided
            by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.906165.1,
                                           SRR1660803.41473.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306121.8/ ENSP00000304429.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.3"
     Protein         1..451
                     /product="sorting nexin-7 isoform a"
                     /calculated_mol_wt=51488
     Region          96..211
                     /region_name="PX_SNX7"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 7; cd07284"
                     /db_xref="CDD:132817"
     Site            order(137..139,163..164,181)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132817"
     Region          195..437
                     /region_name="BAR_SNX7"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Sorting
                     Nexin 7; cd07666"
                     /db_xref="CDD:153350"
     Site            order(256,259..260,263..264,266..267,270,273..274,277,
                     284..285,287..288,291,294..295,298..299,313,399,402..403,
                     405..407,410,413..414,416..418,420..421,424..425,427..428,
                     431..432,434..435)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153350"
     CDS             1..451
                     /gene="SNX7"
                     /coded_by="NM_015976.5:12..1367"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS755.2"
                     /db_xref="GeneID:51375"
                     /db_xref="HGNC:HGNC:14971"
                     /db_xref="MIM:614904"
ORIGIN      
        1 megerrasqa pssglpagga ngespgggap fpgssgssal lqaevldlde deddlevfsk
       61 daslmdmnsf spmmptspls minqikfede pdlkdlfitv depeshvtti etfityriit
      121 ktsrgefdss efevrrryqd flwlkgklee ahptliippl pekfivkgmv erfnddfiet
      181 rrkalhkfln riadhptltf nedfkiflta qawelsshkk qgpgllsrmg qtvravassm
      241 rgvknrpeef memnnfielf sqkinlidki sqriykeere yfdemkeygp ihilwsasee
      301 dlvdtlkdva scidrcckat ekrmsglsea llpvvheyvl ysemlmgvmk rrdqiqaeld
      361 skvevltykk adtdllpeei gkledkveca nnalkadwer wkqnmqndik laftdmaeen
      421 ihyyeqclat wesfltsqtn lhleeasedk p
//
LOCUS       NP_940849                132 aa            linear   PRI 27-APR-2025
DEFINITION  vesicle transport protein GOT1A [Homo sapiens].
ACCESSION   NP_940849 XP_059186
VERSION     NP_940849.1
DBSOURCE    REFSEQ: accession NM_198447.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Zhang,L., Cheng,A., Yu,Y., Zou,N., Wang,W., Lv,L., Guo,X., Chen,M.
            and Zhang,Y.
  TITLE     GOLT1A-KISS1 fusion is associated with metastasis in adenoid cystic
            carcinomas
  JOURNAL   Biochem Biophys Res Commun 526 (1), 70-77 (2020)
   PUBMED   32192769
  REMARK    GeneRIF: GOLT1A-KISS1 fusion is associated with metastasis in
            adenoid cystic carcinomas.
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Ikeda,K., Horie-Inoue,K., Ueno,T., Suzuki,T., Sato,W.,
            Shigekawa,T., Osaki,A., Saeki,T., Berezikov,E., Mano,H. and
            Inoue,S.
  TITLE     miR-378a-3p modulates tamoxifen sensitivity in breast cancer MCF-7
            cells through targeting GOLT1A
  JOURNAL   Sci Rep 5, 13170 (2015)
   PUBMED   26255816
  REMARK    GeneRIF: GOLT1A knockdown restored tamoxifen resistance and low
            GOLT1A levels correlate with better survival in patients with
            breast cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Conchon,S., Cao,X., Barlowe,C. and Pelham,H.R.
  TITLE     Got1p and Sft2p: membrane proteins involved in traffic to the Golgi
            complex
  JOURNAL   EMBO J 18 (14), 3934-3946 (1999)
   PUBMED   10406798
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK124645.1.
            
            On Dec 17, 2003 this sequence version replaced XP_059186.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.21467.1, BC058832.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308302.4/ ENSP00000308535.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..132
                     /product="vesicle transport protein GOT1A"
                     /calculated_mol_wt=14756
     Region          4..109
                     /region_name="Got1"
                     /note="Got1/Sft2-like family; cl02130"
                     /db_xref="CDD:470475"
     Site            10..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVE7.1)"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVE7.1)"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVE7.1)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVE7.1)"
     CDS             1..132
                     /gene="GOLT1A"
                     /gene_synonym="CGI-141; GOT1; GOT1B; hGOT1b; HMFN1187;
                     YMR292W"
                     /coded_by="NM_198447.2:83..481"
                     /db_xref="CCDS:CCDS1443.1"
                     /db_xref="GeneID:127845"
                     /db_xref="HGNC:HGNC:24766"
                     /db_xref="MIM:620633"
ORIGIN      
        1 misitewqki gvgitgfgif filfgtllyf dsvllafgnl lfltglslii glrktfwfff
       61 qrhklkgtsf llggvvivll rwpllgmfle tygffslfkg ffpvafgflg nvcnipflga
      121 lfrrlqgtss mv
//
LOCUS       NP_005979                 72 aa            linear   PRI 27-APR-2025
DEFINITION  small proline-rich protein 2A [Homo sapiens].
ACCESSION   NP_005979
VERSION     NP_005979.1
DBSOURCE    REFSEQ: accession NM_005988.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Hu,Z., Zhang,C., Sifuentes-Dominguez,L., Zarek,C.M.,
            Propheter,D.C., Kuang,Z., Wang,Y., Pendse,M., Ruhn,K.A.,
            Hassell,B., Behrendt,C.L., Zhang,B., Raj,P., Harris-Tryon,T.A.,
            Reese,T.A. and Hooper,L.V.
  TITLE     Small proline-rich protein 2A is a gut bactericidal protein
            deployed during helminth infection
  JOURNAL   Science 374 (6568), eabe6723 (2021)
   PUBMED   34735226
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Xu,X., Wei,S., Chen,Y., Yu,D., Wang,X. and Dong,X.
  TITLE     Serum Small Proline-Rich Protein 2A (SPRR2A) Is a Noninvasive
            Biomarker in Gastric Cancer
  JOURNAL   Dis Markers 2020, 8493796 (2020)
   PUBMED   32908616
  REMARK    GeneRIF: Serum Small Proline-Rich Protein 2A (SPRR2A) Is a
            Noninvasive Biomarker in Gastric Cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 72)
  AUTHORS   Nisa,L., Barras,D., Medova,M., Aebersold,D.M., Medo,M.,
            Poliakova,M., Koch,J., Bojaxhiu,B., Elicin,O., Dettmer,M.S.,
            Angelino,P., Giger,R., Borner,U., Caversaccio,M.D., Carey,T.E.,
            Ho,L., McKee,T.A., Delorenzi,M. and Zimmer,Y.
  TITLE     Comprehensive Genomic Profiling of Patient-matched Head and Neck
            Cancer Cells: A Preclinical Pipeline for Metastatic and Recurrent
            Disease
  JOURNAL   Mol Cancer Res 16 (12), 1912-1926 (2018)
   PUBMED   30108165
  REMARK    GeneRIF: Assessment of SPRR2A protein expression in a clinical
            cohort of patients with head and neck squamous cell carcinoma
            (HNSCC) confirmed common SPRR2A downregulation in primary tumors
            and lymph node metastases, but not in normal tissue. High
            expression of SPRR2A in lymph node metastases was, along with
            nonoropharyngeal location of the primary tumor, an independent
            prognostic factor for regional disease recurrence.
REFERENCE   4  (residues 1 to 72)
  AUTHORS   Ramakrishnan,V.R., Gonzalez,J.R., Cooper,S.E., Barham,H.P.,
            Anderson,C.B., Larson,E.D., Cool,C.D., Diller,J.D., Jones,K. and
            Kinnamon,S.C.
  TITLE     RNA sequencing and pathway analysis identify tumor necrosis factor
            alpha driven small proline-rich protein dysregulation in chronic
            rhinosinusitis
  JOURNAL   Am J Rhinol Allergy 31 (5), 283-288 (2017)
   PUBMED   28859701
  REMARK    GeneRIF: Expression of SPRR1 and of SPRR2A is increased in mucosal
            samples from patients with chronic rhinosinusitis and appeared as a
            downstream result of TNF alpha modulation, which possibly resulted
            in epithelial barrier dysfunction.
REFERENCE   5  (residues 1 to 72)
  AUTHORS   Mizuguchi,Y., Isse,K., Specht,S., Lunz,J.G. 3rd, Corbitt,N.,
            Takizawa,T. and Demetris,A.J.
  TITLE     Small proline rich protein 2a in benign and malignant liver disease
  JOURNAL   Hepatology 59 (3), 1130-1143 (2014)
   PUBMED   24123265
  REMARK    GeneRIF: SPRR2a modulates ZEB-1 signaling by way of
            miR-200c/141-associated epithelial mesenchyme transition through
            SH3-domain networks and contributes to benign and malignant
            wound-healing responses.
REFERENCE   6  (residues 1 to 72)
  AUTHORS   Fischer,D.F., van Drunen,C.M., Winkler,G.S., van de Putte,P. and
            Backendorf,C.
  TITLE     Involvement of a nuclear matrix association region in the
            regulation of the SPRR2A keratinocyte terminal differentiation
            marker
  JOURNAL   Nucleic Acids Res 26 (23), 5288-5294 (1998)
   PUBMED   9826750
REFERENCE   7  (residues 1 to 72)
  AUTHORS   Steinert,P.M. and Marekov,L.N.
  TITLE     Direct evidence that involucrin is a major early isopeptide
            cross-linked component of the keratinocyte cornified cell envelope
  JOURNAL   J Biol Chem 272 (3), 2021-2030 (1997)
   PUBMED   8999895
REFERENCE   8  (residues 1 to 72)
  AUTHORS   Fischer,D.F., Gibbs,S., van De Putte,P. and Backendorf,C.
  TITLE     Interdependent transcription control elements regulate the
            expression of the SPRR2A gene during keratinocyte terminal
            differentiation
  JOURNAL   Mol Cell Biol 16 (10), 5365-5374 (1996)
   PUBMED   8816448
REFERENCE   9  (residues 1 to 72)
  AUTHORS   Gibbs,S., Fijneman,R., Wiegant,J., van Kessel,A.G., van De Putte,P.
            and Backendorf,C.
  TITLE     Molecular characterization and evolution of the SPRR family of
            keratinocyte differentiation markers encoding small proline-rich
            proteins
  JOURNAL   Genomics 16 (3), 630-637 (1993)
   PUBMED   8325635
REFERENCE   10 (residues 1 to 72)
  AUTHORS   Gibbs,S., Lohman,F., Teubel,W., van de Putte,P. and Backendorf,C.
  TITLE     Characterization of the human spr2 promoter: induction after UV
            irradiation or TPA treatment and regulation during differentiation
            of cultured primary keratinocytes
  JOURNAL   Nucleic Acids Res 18 (15), 4401-4407 (1990)
   PUBMED   2388825
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BE710686.1, X53064.1 and CA433267.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA766540.1, DA763239.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392653.3/ ENSP00000376423.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..72
                     /product="small proline-rich protein 2A"
                     /note="2-1; SPR-2A"
                     /calculated_mol_wt=7834
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35326.1)"
     Region          21..47
                     /region_name="3 X 9 AA tandem repeats of
                     P-K-C-P-[EQ]-P-C-P-P. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35326.1)"
     Region          42..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35326.1)"
     CDS             1..72
                     /gene="SPRR2A"
                     /coded_by="NM_005988.3:62..280"
                     /db_xref="CCDS:CCDS1034.1"
                     /db_xref="GeneID:6700"
                     /db_xref="HGNC:HGNC:11261"
                     /db_xref="MIM:182267"
ORIGIN      
        1 msyqqqqckq pcqpppvcpt pkcpepcppp kcpepcpppk cpqpcppqqc qqkyppvtps
       61 ppcqskyppk sk
//
LOCUS       NP_081757                643 aa            linear   ROD 27-APR-2025
DEFINITION  SURP and G-patch domain-containing protein 1 [Mus musculus].
ACCESSION   NP_081757
VERSION     NP_081757.1
DBSOURCE    REFSEQ: accession NM_027481.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Benbarche,S., Pineda,J.M.B., Galvis,L.B., Biswas,J., Liu,B.,
            Wang,E., Zhang,Q., Hogg,S.J., Lyttle,K., Dahi,A., Lewis,A.M.,
            Sarchi,M., Rahman,J., Fox,N., Ai,Y., Mehta,S., Garippa,R.,
            Ortiz-Pacheco,J., Li,Z., Monetti,M., Stanley,R.F., Doulatov,S.,
            Bradley,R.K. and Abdel-Wahab,O.
  TITLE     GPATCH8 modulates mutant SF3B1 mis-splicing and pathogenicity in
            hematologic malignancies
  JOURNAL   Mol Cell 84 (10), 1886-1903 (2024)
   PUBMED   38688280
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Kim,M.J., Yu,C.Y., Theusch,E., Naidoo,D., Stevens,K., Kuang,Y.L.,
            Schuetz,E., Chaudhry,A.S. and Medina,M.W.
  TITLE     SUGP1 is a novel regulator of cholesterol metabolism
  JOURNAL   Hum Mol Genet 25 (14), 3106-3116 (2016)
   PUBMED   27206982
  REMARK    GeneRIF: Our results strongly support a role for SUGP1 as a novel
            regulator of cholesterol metabolism and suggest that it contributes
            to the relationship between rs10401969 and plasma cholesterol
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Sampson,N.D. and Hewitt,J.E.
  TITLE     SF4 and SFRS14, two related putative splicing factors on human
            chromosome 19p13.11
  JOURNAL   Gene 305 (1), 91-100 (2003)
   PUBMED   12594045
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC167132.12.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK017736.1, AF521129.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 34.15 cM"
     Protein         1..643
                     /product="SURP and G-patch domain-containing protein 1"
                     /note="splicing factor 4"
                     /calculated_mol_wt=72518
     Region          48..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          97..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWZ8; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          186..237
                     /region_name="Surp"
                     /note="Surp module; pfam01805"
                     /db_xref="CDD:460339"
     Region          187..229
                     /region_name="SURP motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWZ8; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          261..312
                     /region_name="Surp"
                     /note="Surp module; pfam01805"
                     /db_xref="CDD:460339"
     Region          262..305
                     /region_name="SURP motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          293..>416
                     /region_name="kgd"
                     /note="multifunctional oxoglutarate
                     decarboxylase/oxoglutarate dehydrogenase thiamine
                     pyrophosphate-binding subunit/dihydrolipoyllysine-residue
                     succinyltransferase subunit; cl39092"
                     /db_xref="CDD:476867"
     Region          316..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWZ8; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          360..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          378..384
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWZ8; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CH02.1)"
     Region          561..605
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     CDS             1..643
                     /gene="Sugp1"
                     /gene_synonym="5730496N02Rik; Sf4"
                     /coded_by="NM_027481.3:261..2192"
                     /db_xref="CCDS:CCDS22356.1"
                     /db_xref="GeneID:70616"
                     /db_xref="MGI:MGI:1917866"
ORIGIN      
        1 mslkmdnrdv agkanrwfgm aqpksgkmnm nilhqeelia qkkreiearm eqkarqshvp
       61 spqpphpgei adahnscisn kfandgsflq qflklqkaqt stdsaprapp smptpsslkk
      121 plvlskrtgl glssptgpvk nyshakqlpv ahrpsvfqsp dddeeedyeq wleikvsppe
      181 gaetrrviek larfvaeggp elekvamedy kdnpaftflh dknsreflyy rrkvaeirke
      241 aqkpqaatqk vsppedeeak nlaeklarfi adggpeveti alqnnrenqa fsflydpnsq
      301 gyryyrqkld efrkakagst gsfpapapnp slrrksapea lsgavppita cptpvapapa
      361 vnptpsipgk ptataavkrk rksrwgpeed kvelppaela qrdidaspsp lsvqdlkglg
      421 yekgkpvglv gvtelsdaqk kqlkeqqemq qmydmimqhk ramqdmqllw ekalqqhqhg
      481 ydsdeevdse lgtwehqlrr memdktrewa eqltqmgrgk hfigdflppd elekfmetfk
      541 alkegrepdy seykefkltv enigyqmlmk mgwkegeglg tegqgiknpv nkgattidga
      601 gfgidrpael skeddeyeaf rkrmmlayrf rpnplnnprr pyy
//
LOCUS       NP_003074                334 aa            linear   PRI 27-APR-2025
DEFINITION  snRNA-activating protein complex subunit 2 [Homo sapiens].
ACCESSION   NP_003074
VERSION     NP_003074.1
DBSOURCE    REFSEQ: accession NM_003083.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Harrigan,J.A., Belotserkovskaya,R., Coates,J., Dimitrova,D.S.,
            Polo,S.E., Bradshaw,C.R., Fraser,P. and Jackson,S.P.
  TITLE     Replication stress induces 53BP1-containing OPT domains in G1 cells
  JOURNAL   J Cell Biol 193 (1), 97-108 (2011)
   PUBMED   21444690
  REMARK    GeneRIF: The findings invoke a model wherein incomplete DNA
            synthesis during S phase leads to a DNA damage response and
            formation of 53BP1-OPT domains in the subsequent G1.
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Shanmugam,M. and Hernandez,N.
  TITLE     Mitotic functions for SNAP45, a subunit of the small nuclear
            RNA-activating protein complex SNAPc
  JOURNAL   J Biol Chem 283 (21), 14845-14856 (2008)
   PUBMED   18356157
  REMARK    GeneRIF: SNAP45 plays two roles in the cell, one as a subunit of
            the transcription factor SNAP(c) and another as a factor required
            for proper mitotic progression
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Emran,F., Florens,L., Ma,B., Swanson,S.K., Washburn,M.P. and
            Hernandez,N.
  TITLE     A role for Yin Yang-1 (YY1) in the assembly of snRNA transcription
            complexes
  JOURNAL   Gene 377, 96-108 (2006)
   PUBMED   16769183
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Hinkley,C.S., Hirsch,H.A., Gu,L., LaMere,B. and Henry,R.W.
  TITLE     The small nuclear RNA-activating protein 190 Myb DNA binding domain
            stimulates TATA box-binding protein-TATA box recognition
  JOURNAL   J Biol Chem 278 (20), 18649-18657 (2003)
   PUBMED   12621023
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Acierno,J.S. Jr., Kennedy,J.C., Falardeau,J.L., Leyne,M.,
            Bromley,M.C., Colman,M.W., Sun,M., Bove,C., Ashworth,L.K.,
            Chadwick,L.H., Schiripo,T., Ma,S., Goldin,E., Schiffmann,R. and
            Slaugenhaupt,S.A.
  TITLE     A physical and transcript map of the MCOLN1 gene region on human
            chromosome 19p13.3-p13.2
  JOURNAL   Genomics 73 (2), 203-210 (2001)
   PUBMED   11318610
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Wong,M.W., Henry,R.W., Ma,B., Kobayashi,R., Klages,N., Matthias,P.,
            Strubin,M. and Hernandez,N.
  TITLE     The large subunit of basal transcription factor SNAPc is a Myb
            domain protein that interacts with Oct-1
  JOURNAL   Mol Cell Biol 18 (1), 368-377 (1998)
   PUBMED   9418884
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Henry,R.W., Ma,B., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     Cloning and characterization of SNAP50, a subunit of the
            snRNA-activating protein complex SNAPc
  JOURNAL   EMBO J 15 (24), 7129-7136 (1996)
   PUBMED   9003788
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Sadowski,C.L., Henry,R.W., Kobayashi,R. and Hernandez,N.
  TITLE     The SNAP45 subunit of the small nuclear RNA (snRNA) activating
            protein complex is required for RNA polymerase II and III snRNA
            gene transcription and interacts with the TATA box binding protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (9), 4289-4293 (1996)
   PUBMED   8633057
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Yoon,J.B. and Roeder,R.G.
  TITLE     Cloning of two proximal sequence element-binding transcription
            factor subunits (gamma and delta) that are required for
            transcription of small nuclear RNA genes by RNA polymerases II and
            III and interact with the TATA-binding protein
  JOURNAL   Mol Cell Biol 16 (1), 1-9 (1996)
   PUBMED   8524284
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Henry,R.W., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     A TBP-TAF complex required for transcription of human snRNA genes
            by RNA polymerase II and III
  JOURNAL   Nature 374 (6523), 653-656 (1995)
   PUBMED   7715707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U44755.1 and AC010336.8.
            
            Summary: This gene encodes a subunit of the snRNA-activating
            protein complex which is associated with the TATA box-binding
            protein. The encoded protein is necessary for RNA polymerase II and
            III dependent small-nuclear RNA gene transcription. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U44755.1, SRR3476690.130996.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221573.11/ ENSP00000221573.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..334
                     /product="snRNA-activating protein complex subunit 2"
                     /note="proximal sequence element-binding transcription
                     factor subunit delta; PSE-binding factor subunit delta;
                     PTF subunit delta; SNAPC 45 kDa subunit; SNAPc subunit 2;
                     snRNA-activating protein complex 45 kDa subunit; small
                     nuclear RNA activating complex, polypeptide 2, 45kD; small
                     nuclear RNA activating complex, polypeptide 2, 45kDa"
                     /calculated_mol_wt=35425
     Region          14..334
                     /region_name="SNAPC2"
                     /note="Small nuclear RNA activating complex (SNAPc),
                     subunit 2; pfam11035"
                     /db_xref="CDD:463210"
     Region          137..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13487.1)"
     Region          271..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13487.1)"
     CDS             1..334
                     /gene="SNAPC2"
                     /gene_synonym="PTFDELTA; SNAP45"
                     /coded_by="NM_003083.4:30..1034"
                     /db_xref="CCDS:CCDS12190.1"
                     /db_xref="GeneID:6618"
                     /db_xref="HGNC:HGNC:11135"
                     /db_xref="MIM:605076"
ORIGIN      
        1 mkppprrraa parylgevtg patwsarekr qlvrllqarq gqpepdatel arelrgrsea
       61 eirvflqqlk grvareaiqk vhpgglqgpr rreaqppapi evwtdlaeki tgpleealav
      121 afsqvltiaa tepvtllhsk ppkptqargk plllsapggq edpapeipss apaapssapr
      181 tpdpapekps essagpstee dfavdfekiy kylssvsrsg rspelsaaes avvldllmsl
      241 peelpllpct alvehmtety lrltapqpip aggslgpaae gdgagskape etppatekae
      301 hselkspwqa agicplnpfl vplellgraa tpar
//
LOCUS       NP_036336                822 aa            linear   PRI 27-APR-2025
DEFINITION  general transcription factor 3C polypeptide 4 [Homo sapiens].
ACCESSION   NP_036336
VERSION     NP_036336.2
DBSOURCE    REFSEQ: accession NM_012204.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Joubert,B.R., Lange,E.M., Franceschini,N., Mwapasa,V., North,K.E.
            and Meshnick,S.R.
  CONSRTM   NIAID Center for HIV/AIDS Vaccine Immunology
  TITLE     A whole genome association study of mother-to-child transmission of
            HIV in Malawi
  JOURNAL   Genome Med 2 (3), 17 (2010)
   PUBMED   20487506
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
            Erratum:[Genome Med. 2010;2(10):76]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Dumay-Odelot,H., Marck,C., Durrieu-Gaillard,S., Lefebvre,O.,
            Jourdain,S., Prochazkova,M., Pflieger,A. and Teichmann,M.
  TITLE     Identification, molecular cloning, and characterization of the
            sixth subunit of human transcription factor TFIIIC
  JOURNAL   J Biol Chem 282 (23), 17179-17189 (2007)
   PUBMED   17409385
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Hsieh,Y.J., Kundu,T.K., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     The TFIIIC90 subunit of TFIIIC interacts with multiple components
            of the RNA polymerase III machinery and contains a histone-specific
            acetyltransferase activity
  JOURNAL   Mol Cell Biol 19 (11), 7697-7704 (1999)
   PUBMED   10523658
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Hsieh,Y.J., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of two evolutionarily conserved
            subunits (TFIIIC102 and TFIIIC63) of human TFIIIC and their
            involvement in functional interactions with TFIIIB and RNA
            polymerase III
  JOURNAL   Mol Cell Biol 19 (7), 4944-4952 (1999)
   PUBMED   10373544
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC060821.1, BC112245.1, AK027509.1, AL160165.17 and AB072895.1.
            
            On Aug 18, 2007 this sequence version replaced NP_036336.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the functional protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF142328.1, BC094774.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372146.5/ ENSP00000361219.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..822
                     /product="general transcription factor 3C polypeptide 4"
                     /EC_number="2.3.1.48"
                     /note="general transcription factor 3C 4; TFIIIC 90 kDa
                     subunit; transcription factor IIIC subunit delta;
                     transcription factor IIIC 90 kDa subunit; general
                     transcription factor IIIC, polypeptide 4, 90kDa"
                     /calculated_mol_wt=91852
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN8.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9UKN8.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKN8.2)"
     Region          64..254
                     /region_name="TFIIIC_delta"
                     /note="Transcription factor IIIC subunit delta N-term;
                     pfam12657"
                     /db_xref="CDD:463658"
     Region          265..719
                     /region_name="DUF5921"
                     /note="Domain of unknown function (DUF5921); pfam19336"
                     /db_xref="CDD:466046"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKN8.2)"
     Region          608..663
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKN8.2)"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKN8.2)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKN8.2)"
     Region          745..817
                     /region_name="zf-TFIIIC"
                     /note="Putative zinc-finger of transcription factor IIIC
                     complex; pfam12660"
                     /db_xref="CDD:372246"
     CDS             1..822
                     /gene="GTF3C4"
                     /gene_synonym="KAT12; TF3C-delta; TFIII90; TFIIIC290;
                     TFIIIC90; TFIIICDELTA"
                     /coded_by="NM_012204.4:136..2604"
                     /db_xref="CCDS:CCDS6953.1"
                     /db_xref="GeneID:9329"
                     /db_xref="HGNC:HGNC:4667"
                     /db_xref="MIM:604892"
ORIGIN      
        1 mntadqarvg paddgpapsg eeegegggea ggkepaadaa pgpsaafrlm vtrrepavkl
       61 qyavsglepl awsedhrvsv starsiavle licdvhnpgq dlvihrtsvp aplnscllkv
      121 gsktevaeck ekfaaskdpt vsqtfmldrv fnpegkalpp mrgfkytsws pmgcdangrc
      181 llaaltmdnr ltiqanlnrl qwvqlvdlte iygerlyets yrlskneape gnlgdfaefq
      241 rrhsmqtpvr mewsgicttq qvkhnnecrd vgsvllavlf engniavwqf qlpfvgkesi
      301 sscntiesgi tspsvlfwwe yehnnrkmsg livgsafgpi kilpvnlkav kgyftlrqpv
      361 ilwkemdqlp vhsikcvply hpyqkcscsl vvaargsyvf wcllliskag lnvhnshvtg
      421 lhslpivsmt adkqngtvyt cssdgkvrql ipiftdvalk fehqliklsd vfgsvrthgi
      481 avspcgayla iittegming lhpvnknyqv qfvtlktfee aaaqllessv qnlfkqvdli
      541 dlvrwkilkd khipqflqea lekkiessgv tyfwrfklfl lrilyqsmqk tpsealwkpt
      601 hedskillvd spgmgnadde qqeegtsskq vvkqglqers kegdveeptd dslpttgdag
      661 grepmeekll eiqgkieave mhltrehmkr vlgevylhtw itentsiptr glcnflmsde
      721 eyddrtarvl ighiskkmnk qtfpehcslc keilpftdrk qavcsnghiw lrcfltyqsc
      781 qsliyrrcll hdsiarhpap edpdwikrll qspcpfcdsp vf
//
LOCUS       NP_001355202             318 aa            linear   PRI 27-APR-2025
DEFINITION  serine palmitoyltransferase 1 isoform e [Homo sapiens].
ACCESSION   NP_001355202 XP_011516441
VERSION     NP_001355202.1
DBSOURCE    REFSEQ: accession NM_001368273.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Rochat,J., Blavier,A., Ruet,S., Vasseur,S., Puma,A., Desnous,B.,
            Chan,V., Delmont,E., Attarian,S., Juntas Morales,R., Quadrio,I.,
            Vidoni,L., Bonello-Palot,N. and Cheillan,D.
  TITLE     Functional and Molecular Characterization of New SPTLC1 Missense
            Variants in Patients with Hereditary Sensory and Autonomic
            Neuropathy Type 1 (HSAN1)
  JOURNAL   Genes (Basel) 15 (6), 692 (2024)
   PUBMED   38927628
  REMARK    GeneRIF: Functional and Molecular Characterization of New SPTLC1
            Missense Variants in Patients with Hereditary Sensory and Autonomic
            Neuropathy Type 1 (HSAN1).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Li,C., Hou,Y., Wei,Q., Lin,J., Jiang,Z., Jiang,Q., Yang,T.,
            Xiao,Y., Huang,J., Cheng,Y., Ou,R., Liu,K., Chen,X., Song,W.,
            Zhao,B., Wu,Y., Cao,B., Chen,Y. and Shang,H.
  TITLE     Mutation screening of SPTLC1 and SPTLC2 in amyotrophic lateral
            sclerosis
  JOURNAL   Hum Genomics 17 (1), 28 (2023)
   PUBMED   36966328
  REMARK    GeneRIF: Mutation screening of SPTLC1 and SPTLC2 in amyotrophic
            lateral sclerosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Jagle,S., Hsu,H.H., Juratli,H.A., Zimmer,A.D., Prieschl,A.,
            Alter,S., Wiedenhofer,B., Metze,D., Emmert,S. and Fischer,J.
  TITLE     Pathogenic variants in the SPTLC1 gene cause hyperkeratosis
            lenticularis perstans
  JOURNAL   Br J Dermatol 188 (1), 94-99 (2023)
   PUBMED   36689507
  REMARK    GeneRIF: Pathogenic variants in the SPTLC1 gene cause
            hyperkeratosis lenticularis perstans.
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Wang,P., Wei,Q., Li,H. and Wu,Z.Y.
  TITLE     Clinical feature difference between juvenile amyotrophic lateral
            sclerosis with SPTLC1 and FUS mutations
  JOURNAL   Chin Med J (Engl) 136 (2), 176-183 (2023)
   PUBMED   36801857
  REMARK    GeneRIF: Clinical feature difference between juvenile amyotrophic
            lateral sclerosis with SPTLC1 and FUS mutations.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Fiorillo,C., Capodivento,G., Geroldi,A., Tozza,S., Moroni,I.,
            Mohassel,P., Cataldi,M., Campana,C., Morando,S., Panicucci,C.,
            Pedemonte,M., Brolatti,N., Siliquini,S., Traverso,M., Baratto,S.,
            Debellis,D., Magri,S., Prada,V., Bellone,E., Salpietro,V.,
            Donkervoort,S., Gable,K., Gupta,S.D., Dunn,T.M., Bonnemann,C.G.,
            Taroni,F., Bruno,C., Schenone,A., Mandich,P., Nobbio,L. and
            Nolano,M.
  TITLE     The SPTLC1 p.S331 mutation bridges sensory neuropathy and motor
            neuron disease and has implications for treatment
  JOURNAL   Neuropathol Appl Neurobiol 48 (7), e12842 (2022)
   PUBMED   35904184
  REMARK    GeneRIF: The SPTLC1 p.S331 mutation bridges sensory neuropathy and
            motor neuron disease and has implications for treatment.
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Perry,D.K., Carton,J., Shah,A.K., Meredith,F., Uhlinger,D.J. and
            Hannun,Y.A.
  TITLE     Serine palmitoyltransferase regulates de novo ceramide generation
            during etoposide-induced apoptosis
  JOURNAL   J Biol Chem 275 (12), 9078-9084 (2000)
   PUBMED   10722759
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Hanada,K., Hara,T. and Nishijima,M.
  TITLE     Purification of the serine palmitoyltransferase complex responsible
            for sphingoid base synthesis by using affinity peptide
            chromatography techniques
  JOURNAL   J Biol Chem 275 (12), 8409-8415 (2000)
   PUBMED   10722674
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Gable,K., Slife,H., Bacikova,D., Monaghan,E. and Dunn,T.M.
  TITLE     Tsc3p is an 80-amino acid protein associated with serine
            palmitoyltransferase and required for optimal enzyme activity
  JOURNAL   J Biol Chem 275 (11), 7597-7603 (2000)
   PUBMED   10713067
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Weiss,B. and Stoffel,W.
  TITLE     Human and murine serine-palmitoyl-CoA transferase--cloning,
            expression and characterization of the key enzyme in sphingolipid
            synthesis
  JOURNAL   Eur J Biochem 249 (1), 239-247 (1997)
   PUBMED   9363775
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Nicholson,G.A.
  TITLE     SPTLC1-Related Hereditary Sensory Neuropathy
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301564
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354751.7 and AL391219.12.
            
            On Feb 2, 2019 this sequence version replaced XP_011516441.1.
            
            Summary: This gene encodes a member of the class-II
            pyridoxal-phosphate-dependent aminotransferase family. The encoded
            protein is the long chain base subunit 1 of serine
            palmitoyltransferase. Serine palmitoyltransferase converts L-serine
            and palmitoyl-CoA to 3-oxosphinganine with pyridoxal 5'-phosphate
            and is the key enzyme in sphingolipid biosynthesis. Mutations in
            this gene were identified in patients with hereditary sensory
            neuropathy type 1. Alternatively spliced variants encoding
            different isoforms have been identified. Pseudogenes of this gene
            have been defined on chromosomes 1, 6, 10, and 13. [provided by
            RefSeq, Jul 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.159469.1,
                                           SRR1803617.63245.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.31"
     Protein         1..318
                     /product="serine palmitoyltransferase 1 isoform e"
                     /EC_number="2.3.1.50"
                     /note="long chain base biosynthesis protein 1;
                     serine-palmitoyl-CoA transferase 1; serine
                     C-palmitoyltransferase"
                     /calculated_mol_wt=35135
     Region          <1..317
                     /region_name="AAT_I"
                     /note="Aspartate aminotransferase (AAT) superfamily (fold
                     type I) of pyridoxal phosphate (PLP)-dependent enzymes.
                     PLP combines with an alpha-amino acid to form a compound
                     called a Schiff base or aldimine intermediate, which
                     depending on the reaction, is the...; cl18945"
                     /db_xref="CDD:450240"
     Site            order(12..13,16,90,119,122,151,154)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:99747"
     Site            154
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99747"
     CDS             1..318
                     /gene="SPTLC1"
                     /gene_synonym="ALS27; HSAN1; HSN1; LBC1; LCB1; SPT1; SPTI"
                     /coded_by="NM_001368273.1:654..1610"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:10558"
                     /db_xref="HGNC:HGNC:11277"
                     /db_xref="MIM:605712"
ORIGIN      
        1 mkteeaiiys ygfatiasai payskrgdiv fvdraacfai qkglqasrsd iklfkhndma
       61 dlerllkeqe iedqknprka rvtrrfivve glymntgtic plpelvklky kykariflee
      121 slsfgvlgeh grgvtehygi niddidlisa nmenalasig gfccgrsfvi dhqrlsgqgy
      181 cfsaslppll aaaaiealni meenpgifav lkekcgqihk alqgisglkv vgeslspafh
      241 lqleestgsr eqdvrllqei vdqcmnrsia ltqaryleke ekclpppsir vvvtveqtee
      301 eleraastik evaqavll
//
LOCUS       NP_001357517             124 aa            linear   PRI 27-APR-2025
DEFINITION  tudor-interacting repair regulator protein isoform 6 [Homo
            sapiens].
ACCESSION   NP_001357517
VERSION     NP_001357517.1
DBSOURCE    REFSEQ: accession NM_001370588.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Parnandi,N., Rendo,V., Cui,G., Botuyan,M.V., Remisova,M.,
            Nguyen,H., Drane,P., Beroukhim,R., Altmeyer,M., Mer,G. and
            Chowdhury,D.
  TITLE     TIRR inhibits the 53BP1-p53 complex to alter cell-fate programs
  JOURNAL   Mol Cell 81 (12), 2583-2595 (2021)
   PUBMED   33961797
  REMARK    GeneRIF: TIRR inhibits the 53BP1-p53 complex to alter cell-fate
            programs.
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Avolio,R., Jarvelin,A.I., Mohammed,S., Agliarulo,I., Condelli,V.,
            Zoppoli,P., Calice,G., Sarnataro,D., Bechara,E., Tartaglia,G.G.,
            Landriscina,M., Castello,A., Esposito,F. and Matassa,D.S.
  TITLE     Protein Syndesmos is a novel RNA-binding protein that regulates
            primary cilia formation
  JOURNAL   Nucleic Acids Res 46 (22), 12067-12086 (2018)
   PUBMED   30260431
  REMARK    GeneRIF: Identification of a small subset of mRNAs responsible for
            the biogenesis of primary cilium that have been linked to
            developmental and degenerative diseases, known as ciliopathies, and
            cancer. SDOS binds and regulates the translation of several of
            these mRNAs, controlling cilia development.
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Zhang,A., Peng,B., Huang,P., Chen,J. and Gong,Z.
  TITLE     The p53-binding protein 1-Tudor-interacting repair regulator
            complex participates in the DNA damage response
  JOURNAL   J Biol Chem 292 (16), 6461-6467 (2017)
   PUBMED   28213517
  REMARK    GeneRIF: TIRR is a novel 53BP1-interacting protein that
            participates in the DNA damage response
REFERENCE   7  (residues 1 to 124)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 124)
  AUTHORS   Song,M.G., Li,Y. and Kiledjian,M.
  TITLE     Multiple mRNA decapping enzymes in mammalian cells
  JOURNAL   Mol Cell 40 (3), 423-432 (2010)
   PUBMED   21070968
REFERENCE   9  (residues 1 to 124)
  AUTHORS   Taylor,M.J. and Peculis,B.A.
  TITLE     Evolutionary conservation supports ancient origin for Nudt16, a
            nuclear-localized, RNA-binding, RNA-decapping enzyme
  JOURNAL   Nucleic Acids Res 36 (18), 6021-6034 (2008)
   PUBMED   18820299
REFERENCE   10 (residues 1 to 124)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023830.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.45422.1,
                                           SRR9304715.369676.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..124
                     /product="tudor-interacting repair regulator protein
                     isoform 6"
                     /note="protein syndesmos; NUDT16-like protein 1; nudix
                     (nucleoside diphosphate linked moiety X)-type motif
                     16-like 1; tudor-interacting repair regulator protein"
                     /calculated_mol_wt=13442
     Region          23..107
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     CDS             1..124
                     /gene="NUDT16L1"
                     /gene_synonym="SDOS; TIRR"
                     /coded_by="NM_001370588.1:10..384"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:84309"
                     /db_xref="HGNC:HGNC:28154"
                     /db_xref="MIM:617338"
ORIGIN      
        1 mstaavpelk qisrveamrl gpgwshscha mlyaanpgql fgripmrfsv lvlglvrvpl
       61 ytqkdrvggf pnflsnafvs takcqllfal kvlnmmpeek lvealaaate kqkkalekll
      121 pass
//
LOCUS       NP_080430                262 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL10m isoform 1 precursor [Mus
            musculus].
ACCESSION   NP_080430
VERSION     NP_080430.1
DBSOURCE    REFSEQ: accession NM_026154.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Cheong,A., Lingutla,R. and Mager,J.
  TITLE     Expression analysis of mammalian mitochondrial ribosomal protein
            genes
  JOURNAL   Gene Expr Patterns 38, 119147 (2020)
   PUBMED   32987154
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Yang,Y., Cimen,H., Han,M.J., Shi,T., Deng,J.H., Koc,H.,
            Palacios,O.M., Montier,L., Bai,Y., Tong,Q. and Koc,E.C.
  TITLE     NAD+-dependent deacetylase SIRT3 regulates mitochondrial protein
            synthesis by deacetylation of the ribosomal protein MRPL10
  JOURNAL   J Biol Chem 285 (10), 7417-7429 (2010)
   PUBMED   20042612
  REMARK    GeneRIF: Data describe the regulation of mitochondrial protein
            synthesis by the reversible acetylation of the mitochondrial
            ribosome and characterize MRPL10 as a novel substrate of the
            NAD(+)-dependent deacetylase, SIRT3.
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Mu,X., Zhao,S., Pershad,R., Hsieh,T.F., Scarpa,A., Wang,S.W.,
            White,R.A., Beremand,P.D., Thomas,T.L., Gan,L. and Klein,W.H.
  TITLE     Gene expression in the developing mouse retina by EST sequencing
            and microarray analysis
  JOURNAL   Nucleic Acids Res 29 (24), 4983-4993 (2001)
   PUBMED   11812828
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
REFERENCE   9  (residues 1 to 262)
  AUTHORS   Goldschmidt-Reisin,S., Kitakawa,M., Herfurth,E.,
            Wittmann-Liebold,B., Grohmann,L. and Graack,H.R.
  TITLE     Mammalian mitochondrial ribosomal proteins. N-terminal amino acid
            sequencing, characterization, and identification of corresponding
            gene sequences
  JOURNAL   J Biol Chem 273 (52), 34828-34836 (1998)
   PUBMED   9857009
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD561609.1, AK150774.1 and BF458354.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK002865.1, AK078463.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 60.69 cM"
     Protein         1..262
                     /product="large ribosomal subunit protein uL10m isoform 1
                     precursor"
                     /EC_number="3.6.5.3"
                     /note="39S ribosomal protein L10, mitochondrial; large
                     ribosomal subunit protein uL10m"
                     /calculated_mol_wt=26489
     transit_peptide 1..28
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q3TBW2.2)"
                     /calculated_mol_wt=2925
     mat_peptide     29..262
                     /product="Large ribosomal subunit protein uL10m.
                     /id=PRO_0000273076"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3TBW2.2)"
                     /calculated_mol_wt=26489
     Region          81..228
                     /region_name="Ribosomal_L10"
                     /note="Ribosomal protein L10 family, L10 subfamily;
                     composed of bacterial 50S ribosomal protein and eukaryotic
                     mitochondrial 39S ribosomal protein, L10. L10 occupies the
                     L7/L12 stalk of the ribosome. The N-terminal domain (NTD)
                     of L10 interacts with L11 protein...; cd05797"
                     /db_xref="CDD:240223"
     Site            order(162,181,184,200,203..204,207..208,210..215,217..219,
                     222..223,225..226,228)
                     /site_type="other"
                     /note="Interface with L7/L12 ribosomal proteins
                     [polypeptide binding]"
                     /db_xref="CDD:240223"
     Region          243..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3TBW2.2)"
     CDS             1..262
                     /gene="Mrpl10"
                     /gene_synonym="0610040E02Rik; L10mt; MRP-L8; Rpml8"
                     /coded_by="NM_026154.3:20..808"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS25312.1"
                     /db_xref="GeneID:107732"
                     /db_xref="MGI:MGI:1333801"
ORIGIN      
        1 maaavagilr gglppraawl ptlqtvrhgs kavtrhwrvm hfqrqklmai teyippkpai
       61 nprclppppk ppkeesglvr llrqdivavf rdnrmiavcq nvalsaedkl llrhqlrkhk
      121 ifikvfpsqv lkpflensky rnllplfvgh nlllvseepk vkemvrvlks vpflpllggc
      181 vddtilsrqg lvdyaklpsl dqlqgqlvgg lthlmaqtry llqhqpvqlt slldqyvkeq
      241 negdcatsan eklhppdpap da
//
LOCUS       NP_055185                567 aa            linear   PRI 27-APR-2025
DEFINITION  SRSF protein kinase 3 isoform 1 [Homo sapiens].
ACCESSION   NP_055185
VERSION     NP_055185.2
DBSOURCE    REFSEQ: accession NM_014370.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Roychaudhury,A., Lee,Y.R., Choi,T.I., Thomas,M.G., Khan,T.N.,
            Yousaf,H., Skinner,C., Maconachie,G., Crosier,M., Horak,H.,
            Constantinescu,C.S., Kim,T.Y., Lee,K.H., Kyung,J.J., Wang,T.,
            Ku,B., Chodirker,B.N., Hammer,M.F., Gottlob,I., Norton,W.H.J.,
            Gerlai,R., Kim,H.G., Graziano,C., Pippucci,T., Iovino,E.,
            Montanari,F., Severi,G., Toro,C., Boerkoel,C.F., Cha,H.S.,
            Choi,C.Y., Kim,S., Yoon,J.H., Gilmore,K., Vora,N.L., Davis,E.E.,
            Chudley,A.E., Schwartz,C.E. and Kim,C.H.
  TITLE     SRPK3 Is Essential for Cognitive and Ocular Development in Humans
            and Zebrafish, Explaining X-Linked Intellectual Disability
  JOURNAL   Ann Neurol 96 (5), 914-931 (2024)
   PUBMED   39073169
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Wang,Y. and Tatakis,D.N.
  TITLE     Human gingiva transcriptome during wound healing
  JOURNAL   J Clin Periodontol 44 (4), 394-402 (2017)
   PUBMED   28005267
  REMARK    GeneRIF: SRPK3 expression is significantly downregulated in human
            masticatory mucosa during wound healing
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Zhang,M., Zhu,B. and Davie,J.
  TITLE     Alternative splicing of MEF2C pre-mRNA controls its activity in
            normal myogenesis and promotes tumorigenicity in rhabdomyosarcoma
            cells
  JOURNAL   J Biol Chem 290 (1), 310-324 (2015)
   PUBMED   25404735
  REMARK    GeneRIF: Alternative splicing of the alpha-exon of MEF2C regulates
            myogenesis. Loss of SRPK3 in rhabdomyosarcoma cells inhibits this
            splicing and blocks differentiation.
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Nakagawa,O., Arnold,M., Nakagawa,M., Hamada,H., Shelton,J.M.,
            Kusano,H., Harris,T.M., Childs,G., Campbell,K.P., Richardson,J.A.,
            Nishino,I. and Olson,E.N.
  TITLE     Centronuclear myopathy in mice lacking a novel muscle-specific
            protein kinase transcriptionally regulated by MEF2
  JOURNAL   Genes Dev 19 (17), 2066-2077 (2005)
   PUBMED   16140986
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Grunau,C., Hindermann,W. and Rosenthal,A.
  TITLE     Large-scale methylation analysis of human genomic DNA reveals
            tissue-specific differences between the methylation profiles of
            genes and pseudogenes
  JOURNAL   Hum Mol Genet 9 (18), 2651-2663 (2000)
   PUBMED   11063724
  REMARK    Erratum:[Hum Mol Genet 2001 Jan 1;10(1):85-7]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52111.3 and BC092416.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 4, 2005 this sequence version replaced NP_055185.1.
            
            Summary: This gene encodes a protein kinase similar to a protein
            kinase which is specific for the SR (serine/arginine-rich domain)
            family of splicing factors. A highly similar protein has been shown
            to play a role in muscle development in mice. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301749.1, BC092416.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370101.8/ ENSP00000359119.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..567
                     /product="SRSF protein kinase 3 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="SFRS protein kinase 3; serine/threonine kinase 23;
                     muscle-specific serine kinase 1; serine arginine rich
                     protein-specific kinase 3; serine/threonine-protein kinase
                     SRPK3; SR-protein-specific kinase 3;
                     serine/threonine-protein kinase 23"
                     /calculated_mol_wt=61883
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPE1.2)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0G2; propagated from
                     UniProtKB/Swiss-Prot (Q9UPE1.2)"
     Region          68..565
                     /region_name="STKc_SRPK3"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Serine-aRginine Protein Kinase 3; cd14218"
                     /db_xref="CDD:271120"
     Site            order(85..89,93,106,108,122,144,164..167,170,172..173,212,
                     214,216..217,219,409,412,421,423..426,428,465)
                     /site_type="active"
                     /db_xref="CDD:271120"
     Site            order(85..89,93,106,108,144,164..167,170,212,214,216..217,
                     219,409)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271120"
     Site            order(122,172,212,214,412,421,423..426,428,465)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271120"
     Site            order(180..181,458,460,462,471,476,479..480,483..484,512,
                     516,518,527..528)
                     /site_type="other"
                     /note="kinase-docking site [polypeptide binding]"
                     /db_xref="CDD:271120"
     Region          238..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPE1.2)"
     Region          298..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPE1.2)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0G2; propagated from
                     UniProtKB/Swiss-Prot (Q9UPE1.2)"
     Site            408..428
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271120"
     CDS             1..567
                     /gene="SRPK3"
                     /gene_synonym="MSSK-1; MSSK1; STK23; XLID114"
                     /coded_by="NM_014370.4:47..1750"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35441.1"
                     /db_xref="GeneID:26576"
                     /db_xref="HGNC:HGNC:11402"
                     /db_xref="MIM:301002"
ORIGIN      
        1 msastggggd sggsggssss sqascgpess gselalatpv pqmlqgllgs ddeeqedpkd
       61 yckggyhpvk igdvfngryh vvrklgwghf stvwlcwdiq rkrfvalkvv ksaghyteta
      121 vdeikllkcv rdsdpsdpkr etivqliddf risgvngvhv cmvlevlghq llkwiiksny
      181 qglpvpcvks ivrqvlhgld ylhtkckiih tdikpenill cvgdayirrl aaeatewqqa
      241 gapppsrsiv stapqevlqt gklsknkrkk mrrkrkqqkr lleerlrdlq rleameaatq
      301 aedsglrldg gsgstsssgc hpggaragps passspapgg grslsagsqt sgfsgslfsp
      361 ascsilsgss nqretgglls pstpfgasnl lvnplepqna dkikikiadl gnacwvhkhf
      421 tediqtrqyr avevligaey gppadiwsta cmafelatgd ylfephsged ysrdedhiah
      481 ivellgdipp afalsgrysr effnrrgelr hihnlkhwgl yevlmekyew pleqatqfsa
      541 fllpmmeyip ekrasaadcl qhpwlnp
//
LOCUS       NP_054745                337 aa            linear   PRI 27-APR-2025
DEFINITION  m7GpppX diphosphatase isoform 2 [Homo sapiens].
ACCESSION   NP_054745
VERSION     NP_054745.1
DBSOURCE    REFSEQ: accession NM_014026.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Masoudi,M., Bereshneh,A.H., Rasoulinezhad,M., Ashrafi,M.R.,
            Garshasbi,M. and Tavasoli,A.R.
  TITLE     Leukoencephalopathy in Al-Raqad syndrome: Expanding the clinical
            and neuroimaging features caused by a biallelic novel missense
            variant in DCPS
  JOURNAL   Am J Med Genet A 182 (10), 2391-2398 (2020)
   PUBMED   32770650
  REMARK    GeneRIF: Leukoencephalopathy in Al-Raqad syndrome: Expanding the
            clinical and neuroimaging features caused by a biallelic novel
            missense variant in DCPS.
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Fuchs,A.L., Wurm,J.P., Neu,A. and Sprangers,R.
  TITLE     Molecular basis of the selective processing of short mRNA
            substrates by the DcpS mRNA decapping enzyme
  JOURNAL   Proc Natl Acad Sci U S A 117 (32), 19237-19244 (2020)
   PUBMED   32723815
  REMARK    GeneRIF: Molecular basis of the selective processing of short mRNA
            substrates by the DcpS mRNA decapping enzyme.
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Gopalsamy,A., Narayanan,A., Liu,S., Parikh,M.D., Kyne,R.E. Jr.,
            Fadeyi,O., Tones,M.A., Cherry,J.J., Nabhan,J.F., LaRosa,G.,
            Petersen,D.N., Menard,C., Foley,T.L., Noell,S., Ren,Y., Loria,P.M.,
            Maglich-Goodwin,J., Rong,H. and Jones,L.H.
  TITLE     Design of Potent mRNA Decapping Scavenger Enzyme (DcpS) Inhibitors
            with Improved Physicochemical Properties To Investigate the
            Mechanism of Therapeutic Benefit in Spinal Muscular Atrophy (SMA)
  JOURNAL   J Med Chem 60 (7), 3094-3108 (2017)
   PUBMED   28257199
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Milac,A.L., Bojarska,E. and Wypijewska del Nogal,A.
  TITLE     Decapping Scavenger (DcpS) enzyme: advances in its structure,
            activity and roles in the cap-dependent mRNA metabolism
  JOURNAL   Biochim Biophys Acta 1839 (6), 452-462 (2014)
   PUBMED   24742626
  REMARK    Review article
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Gu,M., Fabrega,C., Liu,S.W., Liu,H., Kiledjian,M. and Lima,C.D.
  TITLE     Insights into the structure, mechanism, and regulation of scavenger
            mRNA decapping activity
  JOURNAL   Mol Cell 14 (1), 67-80 (2004)
   PUBMED   15068804
  REMARK    GeneRIF: Structural and biochemical analysis suggests an
            autoregulatory mechanism whereby premature decapping mRNA is
            prevented by blocking the conformational changes that are required
            to form a closed productive active site capable of cap hydrolysis.
REFERENCE   7  (residues 1 to 337)
  AUTHORS   van Dijk,E., Le Hir,H. and Seraphin,B.
  TITLE     DcpS can act in the 5'-3' mRNA decay pathway in addition to the
            3'-5' pathway
  JOURNAL   Proc Natl Acad Sci U S A 100 (21), 12081-12086 (2003)
   PUBMED   14523240
  REMARK    GeneRIF: m7GDP breakdown by DcpS should prevent misincorporation of
            methylated nucleotides in nucleic acids and could generate a unique
            indicator allowing the cell to monitor mRNA decay.
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Kwasnicka,D.A., Krakowiak,A., Thacker,C., Brenner,C. and
            Vincent,S.R.
  TITLE     Coordinate expression of NADPH-dependent flavin reductase, Fre-1,
            and Hint-related 7meGMP-directed hydrolase, DCS-1
  JOURNAL   J Biol Chem 278 (40), 39051-39058 (2003)
   PUBMED   12871939
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Liu,H., Rodgers,N.D., Jiao,X. and Kiledjian,M.
  TITLE     The scavenger mRNA decapping enzyme DcpS is a member of the HIT
            family of pyrophosphatases
  JOURNAL   EMBO J 21 (17), 4699-4708 (2002)
   PUBMED   12198172
  REMARK    GeneRIF: The central histidine within the DcpS HIT motif is
            critical for decapping activity and defines the HIT motif as a new
            mRNA decapping domain, making DcpS the first member of the HIT
            family of proteins with a defined biological function.
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Wang,Z. and Kiledjian,M.
  TITLE     Functional link between the mammalian exosome and mRNA decapping
  JOURNAL   Cell 107 (6), 751-762 (2001)
   PUBMED   11747811
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF532613.1, BE382749.1,
            AY040771.1, AP001318.6 and BM998313.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the histidine triad family
            of pyrophosphatases that removes short mRNA fragments containing
            the 5' mRNA cap structure, which appear in the 3' -> 5' mRNA decay
            pathway, following deadenylation and exosome-mediated turnover.
            This enzyme hydrolyzes the triphosphate linkage of the cap
            structure (7-methylguanosine nucleoside triphosphate) to yield
            7-methylguanosine monophosphate and nucleoside diphosphate. It
            protects the cell from the potentially toxic accumulation of these
            short, capped mRNA fragments, and regulates the activity of other
            cap-binding proteins, which are inhibited by their accumulation. It
            also acts as a transcript-specific modulator of pre-mRNA splicing
            and microRNA turnover. [provided by RefSeq, Apr 2017].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1. The
            encoded isoform (2) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.506890.1, AY040771.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263579.5/ ENSP00000263579.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.2"
     Protein         1..337
                     /product="m7GpppX diphosphatase isoform 2"
                     /EC_number="3.6.1.59"
                     /note="homolog of C. elegans 7meGMP-directed hydrolase
                     dcs-1; mRNA decapping enzyme; scavenger mRNA-decapping
                     enzyme DcpS; heat shock-like protein 1; 5'-(N(7)-methyl
                     5'-triphosphoguanosine)-[mRNA] diphosphatase; histidine
                     triad protein member 5; hint-related 7meGMP-directed
                     hydrolase; m7GpppX diphosphatase; decapping scavenger
                     enzyme; histidine triad nucleotide-binding protein 5;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=38478
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C86.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96C86.2)"
     Region          10..13
                     /region_name="nuclear localization signal (NLS)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C86.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C86.2)"
     Region          47..329
                     /region_name="COG5075"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:227407"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DAR7; propagated from
                     UniProtKB/Swiss-Prot (Q96C86.2)"
     Site            138
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96C86.2)"
     Region          142..154
                     /region_name="nuclear export sequence (NES)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C86.2)"
     Site            142
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96C86.2)"
     Region          275..279
                     /region_name="Histidine triad motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C86.2)"
     CDS             1..337
                     /gene="DCPS"
                     /gene_synonym="ARS; DCS1; HINT-5; HINT5; HSL1; HSPC015"
                     /coded_by="NM_014026.6:22..1035"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8473.1"
                     /db_xref="GeneID:28960"
                     /db_xref="HGNC:HGNC:29812"
                     /db_xref="MIM:610534"
ORIGIN      
        1 madaapqlgk rkreldveea haasteekea gvgngtcapv rlpfsgfrlq kvlresardk
       61 iiflhgkvne asgdgdgeda vvilektpfq veqvaqlltg spelqlqfsn diystyhlfp
      121 prqlndvktt vvypatekhl qkylrqdlrl iretgddyrn itlphlesqs lsiqwvynil
      181 dkkaeadriv fenpdpsdgf vlipdlkwnq qqlddlylia ichrrgirsl rdltpehlpl
      241 lrnilhqgqe ailqryrmkg dhlrvylhyl psyyhlhvhf talgfeapgs gverahllae
      301 vienlecdpr hyqqrtltfa lraddpllkl lqeaqqs
//
LOCUS       NP_060189                765 aa            linear   PRI 27-APR-2025
DEFINITION  SNF-related serine/threonine-protein kinase isoform 1 [Homo
            sapiens].
ACCESSION   NP_060189
VERSION     NP_060189.3
DBSOURCE    REFSEQ: accession NM_017719.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Xie,Z., Tang,J., Chen,Z., Wei,L., Chen,J. and Liu,Q.
  TITLE     Human bone marrow mesenchymal stem cell-derived extracellular
            vesicles reduce inflammation and pyroptosis in acute kidney injury
            via miR-223-3p/HDAC2/SNRK
  JOURNAL   Inflamm Res 72 (3), 553-576 (2023)
   PUBMED   36640195
  REMARK    GeneRIF: Human bone marrow mesenchymal stem cell-derived
            extracellular vesicles reduce inflammation and pyroptosis in acute
            kidney injury via miR-223-3p/HDAC2/SNRK.
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Wang,Y.L., Wang,J., Chen,X., Wang,Z.X. and Wu,J.W.
  TITLE     Crystal structure of the kinase and UBA domains of SNRK reveals a
            distinct UBA binding mode in the AMPK family
  JOURNAL   Biochem Biophys Res Commun 495 (1), 1-6 (2018)
   PUBMED   29061304
  REMARK    GeneRIF: Report the crystal structure of an N-terminal SNRK
            fragment containing kinase and adjacent ubiquitin-associated (UBA)
            domains. This structure shows that the UBA domain binds between the
            N- and C-lobes of the kinase domain. The mode of UBA binding in
            SNRK largely resembles that in AMPK and brain specific kinase
            (BRSK), however, unique interactions play vital roles in
            stabilizing the KD-UBA interface of SNRK.
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Hopp,E.E., Cossette,S.M., Kumar,S.N., Eastwood,D., Ramchandran,R.
            and Bishop,E.
  TITLE     Sucrose Non-Fermenting Related Kinase Expression in Ovarian Cancer
            and Correlation with Clinical Features
  JOURNAL   Cancer Invest 35 (7), 456-462 (2017)
   PUBMED   28722495
  REMARK    GeneRIF: Differential expression of SNRK in early versus late stage
            disease suggests specific roles for SNRK in ovarian cancer
            metastasis.
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Rines,A.K., Chang,H.C., Wu,R., Sato,T., Khechaduri,A., Kouzu,H.,
            Shapiro,J., Shang,M., Burke,M.A., Abdelwahid,E., Jiang,X., Chen,C.,
            Rawlings,T.A., Lopaschuk,G.D., Schumacker,P.T., Abel,E.D. and
            Ardehali,H.
  TITLE     Snf1-related kinase improves cardiac mitochondrial efficiency and
            decreases mitochondrial uncoupling
  JOURNAL   Nat Commun 8, 14095 (2017)
   PUBMED   28117339
  REMARK    GeneRIF: Study shows that TRIB3 binds to SNRK, and downregulates
            UCP3 through PPARalpha. SNRK is increased in cardiomyopathy
            patients, and SNRK reduces infarct size after
            ischaemia/reperfusion. SNRK also decreases cardiac cell death in a
            UCP3-dependent manner.
            Erratum:[Nat Commun. 2017 Aug 30;8:16155. doi: 10.1038/ncomms16155.
            PMID: 28853433]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 765)
  AUTHORS   Cossette,S.M., Bhute,V.J., Bao,X., Harmann,L.M., Horswill,M.A.,
            Sinha,I., Gastonguay,A., Pooya,S., Bordas,M., Kumar,S.N.,
            Mirza,S.P., Palecek,S.P., Strande,J.L. and Ramchandran,R.
  TITLE     Sucrose Nonfermenting-Related Kinase Enzyme-Mediated Rho-Associated
            Kinase Signaling is Responsible for Cardiac Function
  JOURNAL   Circ Cardiovasc Genet 9 (6), 474-486 (2016)
   PUBMED   27780848
  REMARK    GeneRIF: SNRK in cardiomyocytes is responsible for maintaining
            cardiac metabolic homeostasis, which is mediated in part by ROCK,
            and alteration of this homeostasis influences cardiac function in
            the adult heart.
REFERENCE   6  (residues 1 to 765)
  AUTHORS   Bower,K.E., Zeller,R.W., Wachsman,W., Martinez,T. and McGuire,K.L.
  TITLE     Correlation of transcriptional repression by p21(SNFT) with changes
            in DNA.NF-AT complex interactions
  JOURNAL   J Biol Chem 277 (38), 34967-34977 (2002)
   PUBMED   12087103
REFERENCE   7  (residues 1 to 765)
  AUTHORS   Kertesz,N., Samson,J., Debacker,C., Wu,H. and Labastie,M.C.
  TITLE     Cloning and characterization of human and mouse SNRK sucrose
            non-fermenting protein (SNF-1)-related kinases
  JOURNAL   Gene 294 (1-2), 13-24 (2002)
   PUBMED   12234663
REFERENCE   8  (residues 1 to 765)
  AUTHORS   Yoshida,K., Yamada,M., Nishio,C., Konishi,A. and Hatanaka,H.
  TITLE     SNRK, a member of the SNF1 family, is related to low K(+)-induced
            apoptosis of cultured rat cerebellar granule neurons
  JOURNAL   Brain Res 873 (2), 274-282 (2000)
   PUBMED   10930554
REFERENCE   9  (residues 1 to 765)
  AUTHORS   Iacobelli,M., Wachsman,W. and McGuire,K.L.
  TITLE     Repression of IL-2 promoter activity by the novel basic leucine
            zipper p21SNFT protein
  JOURNAL   J Immunol 165 (2), 860-868 (2000)
   PUBMED   10878360
REFERENCE   10 (residues 1 to 765)
  AUTHORS   Becker,W., Heukelbach,J., Kentrup,H. and Joost,H.G.
  TITLE     Molecular cloning and characterization of a novel mammalian protein
            kinase harboring a homology domain that defines a subfamily of
            serine/threonine kinases
  JOURNAL   Eur J Biochem 235 (3), 736-743 (1996)
   PUBMED   8654423
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP281284.1, D43636.2, DB080037.1 and AK025449.1.
            
            On Aug 17, 2007 this sequence version replaced NP_060189.2.
            
            Summary: SNRK is a member of the sucrose nonfermenting
            (SNF)-related kinase family of serine/threonine kinases (Kertesz et
            al., 2002 [PubMed 12234663]).[supplied by OMIM, Apr 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.140063.1,
                                           SRR1660809.65309.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296088.12/ ENSP00000296088.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.1"
     Protein         1..765
                     /product="SNF-related serine/threonine-protein kinase
                     isoform 1"
                     /EC_number="2.7.11.1"
                     /note="SNF-1 related kinase; SNF-related
                     serine/threonine-protein kinase; SNF1-related kinase"
                     /calculated_mol_wt=84145
     Region          12..269
                     /region_name="STKc_SNRK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     SNF1-related kinase; cd14074"
                     /db_xref="CDD:270976"
     Site            order(22..26,30,43,45,76,92..95,99,101..102,104,138..139,
                     141,143..144,146,157..158,161,175..179,181,211..214)
                     /site_type="active"
                     /db_xref="CDD:270976"
     Site            order(22..25,30,43,45,76,92..95,99,143..144,146,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270976"
     Site            order(99,101..102,104,139,141,143,161,175..179,181,
                     211..214)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270976"
     Site            157..179
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270976"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NRH2.2)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by LKB1.
                     /evidence=ECO:0000269|PubMed:15733851; propagated from
                     UniProtKB/Swiss-Prot (Q9NRH2.2)"
     Region          288..335
                     /region_name="UBA_SNRK"
                     /note="UBA domain of SNF-related serine/threonine-protein
                     kinase (SNRK) and similar proteins mainly found in
                     metazoa; cd14339"
                     /db_xref="CDD:270524"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NRH2.2)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NRH2.2)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NRH2.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63553; propagated from
                     UniProtKB/Swiss-Prot (Q9NRH2.2)"
     Region          512..634
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRH2.2)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRH2.2)"
     Site            534
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NRH2.2)"
     Site            607
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRH2.2)"
     CDS             1..765
                     /gene="SNRK"
                     /gene_synonym="HSNFRK"
                     /coded_by="NM_017719.5:305..2602"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43075.1"
                     /db_xref="GeneID:54861"
                     /db_xref="HGNC:HGNC:30598"
                     /db_xref="MIM:612760"
ORIGIN      
        1 magfkrgydg kiaglydldk tlgrghfavv klarhvftge kvavkvidkt kldtlatghl
       61 fqevrcmklv qhpnivrlye vidtqtklyl ilelgdggdm fdyimkheeg lnedlakkyf
      121 aqivhaisyc hklhvvhrdl kpenvvffek qglvkltdfg fsnkfqpgkk lttscgslay
      181 sapeillgde ydapavdiws lgvilfmlvc gqppfqeand setltmimdc kytvpshvsk
      241 eckdlitrml qrdpkrrasl eeienhpwlq gvdpspatky niplvsyknl seeehnsiiq
      301 rmvlgdiadr daivealetn rynhitatyf llaerilrek qekeiqtrsa spsnikaqfr
      361 qswptkidvp qdleddltat plshatvpqs paraadsvln ghrskglcds akkddlpela
      421 gpalstvppa slkptasgrk clfrveedee edeedkkpms lstqvvlrrk psvtnrltsr
      481 ksapvlnqif eegesddefd mdenlppkls rlkmniaspg tvhkryhrrk sqgrgsscss
      541 setsdddses rrrldkdsgf tyswhrrdss egppgsegdg ggqskpsnas ggvdkaspse
      601 nnagggspss gsggnptnts gttrrcagps nsmqlasrsa gelveslklm slclgsqlhg
      661 stkyiidpqn glsfssvkvq ekstwkmcis stgnagqvpa vggikffsdh madttteler
      721 iksknlknnv lqlplcekti svniqrnpke gllcasspas cchvi
//
LOCUS       NP_001116151            2765 aa            linear   PRI 27-APR-2025
DEFINITION  teneurin-2 isoform 1 [Homo sapiens].
ACCESSION   NP_001116151
VERSION     NP_001116151.1
DBSOURCE    REFSEQ: accession NM_001122679.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2765)
  AUTHORS   Vysokov,N.V., Silva,J.P., Lelianova,V.G., Suckling,J., Cassidy,J.,
            Blackburn,J.K., Yankova,N., Djamgoz,M.B., Kozlov,S.V.,
            Tonevitsky,A.G. and Ushkaryov,Y.A.
  TITLE     Proteolytically released Lasso/teneurin-2 induces axonal attraction
            by interacting with latrophilin-1 on axonal growth cones
  JOURNAL   Elife 7, e37935 (2018)
   PUBMED   30457553
  REMARK    GeneRIF: These findings reveal a novel mechanism of axonal
            pathfinding, whereby latrophilin-1 and Lasso mediate both
            short-range interaction that supports synaptogenesis, and
            long-range signaling that induces axonal attraction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2765)
  AUTHORS   Tews,D., Fromme,T., Keuper,M., Hofmann,S.M., Debatin,K.M.,
            Klingenspor,M., Wabitsch,M. and Fischer-Posovszky,P.
  TITLE     Teneurin-2 (TENM2) deficiency induces UCP1 expression in
            differentiating human fat cells
  JOURNAL   Mol Cell Endocrinol 443, 106-113 (2017)
   PUBMED   28088466
  REMARK    GeneRIF: TENM2 knockdown induces both UCP1 mRNA and protein
            expression upon adipogenic differentiation without affecting
            mitochondrial mass.
REFERENCE   3  (residues 1 to 2765)
  AUTHORS   Perry,J.R., Day,F., Elks,C.E., Sulem,P., Thompson,D.J.,
            Ferreira,T., He,C., Chasman,D.I., Esko,T., Thorleifsson,G.,
            Albrecht,E., Ang,W.Q., Corre,T., Cousminer,D.L., Feenstra,B.,
            Franceschini,N., Ganna,A., Johnson,A.D., Kjellqvist,S.,
            Lunetta,K.L., McMahon,G., Nolte,I.M., Paternoster,L., Porcu,E.,
            Smith,A.V., Stolk,L., Teumer,A., Tsernikova,N., Tikkanen,E.,
            Ulivi,S., Wagner,E.K., Amin,N., Bierut,L.J., Byrne,E.M.,
            Hottenga,J.J., Koller,D.L., Mangino,M., Pers,T.H.,
            Yerges-Armstrong,L.M., Zhao,J.H., Andrulis,I.L., Anton-Culver,H.,
            Atsma,F., Bandinelli,S., Beckmann,M.W., Benitez,J., Blomqvist,C.,
            Bojesen,S.E., Bolla,M.K., Bonanni,B., Brauch,H., Brenner,H.,
            Buring,J.E., Chang-Claude,J., Chanock,S., Chen,J.,
            Chenevix-Trench,G., Collee,J.M., Couch,F.J., Couper,D.,
            Coveillo,A.D., Cox,A., Czene,K., D'adamo,A.P., Smith,G.D., De
            Vivo,I., Demerath,E.W., Dennis,J., Devilee,P., Dieffenbach,A.K.,
            Dunning,A.M., Eiriksdottir,G., Eriksson,J.G., Fasching,P.A.,
            Ferrucci,L., Flesch-Janys,D., Flyger,H., Foroud,T., Franke,L.,
            Garcia,M.E., Garcia-Closas,M., Geller,F., de Geus,E.E., Giles,G.G.,
            Gudbjartsson,D.F., Gudnason,V., Guenel,P., Guo,S., Hall,P.,
            Hamann,U., Haring,R., Hartman,C.A., Heath,A.C., Hofman,A.,
            Hooning,M.J., Hopper,J.L., Hu,F.B., Hunter,D.J., Karasik,D.,
            Kiel,D.P., Knight,J.A., Kosma,V.M., Kutalik,Z., Lai,S.,
            Lambrechts,D., Lindblom,A., Magi,R., Magnusson,P.K., Mannermaa,A.,
            Martin,N.G., Masson,G., McArdle,P.F., McArdle,W.L., Melbye,M.,
            Michailidou,K., Mihailov,E., Milani,L., Milne,R.L., Nevanlinna,H.,
            Neven,P., Nohr,E.A., Oldehinkel,A.J., Oostra,B.A., Palotie,A.,
            Peacock,M., Pedersen,N.L., Peterlongo,P., Peto,J., Pharoah,P.D.,
            Postma,D.S., Pouta,A., Pylkas,K., Radice,P., Ring,S.,
            Rivadeneira,F., Robino,A., Rose,L.M., Rudolph,A., Salomaa,V.,
            Sanna,S., Schlessinger,D., Schmidt,M.K., Southey,M.C., Sovio,U.,
            Stampfer,M.J., Stockl,D., Storniolo,A.M., Timpson,N.J., Tyrer,J.,
            Visser,J.A., Vollenweider,P., Volzke,H., Waeber,G.,
            Waldenberger,M., Wallaschofski,H., Wang,Q., Willemsen,G.,
            Winqvist,R., Wolffenbuttel,B.H., Wright,M.J., Boomsma,D.I.,
            Econs,M.J., Khaw,K.T., Loos,R.J., McCarthy,M.I., Montgomery,G.W.,
            Rice,J.P., Streeten,E.A., Thorsteinsdottir,U., van Duijn,C.M.,
            Alizadeh,B.Z., Bergmann,S., Boerwinkle,E., Boyd,H.A., Crisponi,L.,
            Gasparini,P., Gieger,C., Harris,T.B., Ingelsson,E., Jarvelin,M.R.,
            Kraft,P., Lawlor,D., Metspalu,A., Pennell,C.E., Ridker,P.M.,
            Snieder,H., Sorensen,T.I., Spector,T.D., Strachan,D.P.,
            Uitterlinden,A.G., Wareham,N.J., Widen,E., Zygmunt,M., Murray,A.,
            Easton,D.F., Stefansson,K., Murabito,J.M. and Ong,K.K.
  CONSRTM   Australian Ovarian Cancer Study; GENICA Network; kConFab; LifeLines
            Cohort Study; InterAct Consortium; Early Growth Genetics (EGG)
            Consortium
  TITLE     Parent-of-origin-specific allelic associations among 106 genomic
            loci for age at menarche
  JOURNAL   Nature 514 (7520), 92-97 (2014)
   PUBMED   25231870
REFERENCE   4  (residues 1 to 2765)
  AUTHORS   Scannell Bryan,M., Argos,M., Pierce,B., Tong,L., Rakibuz-Zaman,M.,
            Ahmed,A., Rahman,M., Islam,T., Yunus,M., Parvez,F., Roy,S.,
            Jasmine,F., Baron,J.A., Kibriya,M.G. and Ahsan,H.
  TITLE     Genome-wide association studies and heritability estimates of body
            mass index related phenotypes in Bangladeshi adults
  JOURNAL   PLoS One 9 (8), e105062 (2014)
   PUBMED   25133637
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2765)
  AUTHORS   Tanaka,T., Ngwa,J.S., van Rooij,F.J., Zillikens,M.C.,
            Wojczynski,M.K., Frazier-Wood,A.C., Houston,D.K., Kanoni,S.,
            Lemaitre,R.N., Luan,J., Mikkila,V., Renstrom,F., Sonestedt,E.,
            Zhao,J.H., Chu,A.Y., Qi,L., Chasman,D.I., de Oliveira Otto,M.C.,
            Dhurandhar,E.J., Feitosa,M.F., Johansson,I., Khaw,K.T.,
            Lohman,K.K., Manichaikul,A., McKeown,N.M., Mozaffarian,D.,
            Singleton,A., Stirrups,K., Viikari,J., Ye,Z., Bandinelli,S.,
            Barroso,I., Deloukas,P., Forouhi,N.G., Hofman,A., Liu,Y.,
            Lyytikainen,L.P., North,K.E., Dimitriou,M., Hallmans,G.,
            Kahonen,M., Langenberg,C., Ordovas,J.M., Uitterlinden,A.G.,
            Hu,F.B., Kalafati,I.P., Raitakari,O., Franco,O.H., Johnson,A.,
            Emilsson,V., Schrack,J.A., Semba,R.D., Siscovick,D.S., Arnett,D.K.,
            Borecki,I.B., Franks,P.W., Kritchevsky,S.B., Lehtimaki,T.,
            Loos,R.J., Orho-Melander,M., Rotter,J.I., Wareham,N.J.,
            Witteman,J.C., Ferrucci,L., Dedoussis,G., Cupples,L.A. and
            Nettleton,J.A.
  TITLE     Genome-wide meta-analysis of observational studies shows common
            genetic variants associated with macronutrient intake
  JOURNAL   Am J Clin Nutr 97 (6), 1395-1402 (2013)
   PUBMED   23636237
REFERENCE   6  (residues 1 to 2765)
  AUTHORS   Vinatzer,U., Gollinger,M., Mullauer,L., Raderer,M., Chott,A. and
            Streubel,B.
  TITLE     Mucosa-associated lymphoid tissue lymphoma: novel translocations
            including rearrangements of ODZ2, JMJD2C, and CNN3
  JOURNAL   Clin Cancer Res 14 (20), 6426-6431 (2008)
   PUBMED   18927281
  REMARK    GeneRIF: Gene rearrangements of ODZ2 is associated with
            mucosa-associated lymphoid tissue lymphoma.
REFERENCE   7  (residues 1 to 2765)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   8  (residues 1 to 2765)
  AUTHORS   Bagutti,C., Forro,G., Ferralli,J., Rubin,B. and
            Chiquet-Ehrismann,R.
  TITLE     The intracellular domain of teneurin-2 has a nuclear function and
            represses zic-1-mediated transcription
  JOURNAL   J Cell Sci 116 (Pt 14), 2957-2966 (2003)
   PUBMED   12783990
  REMARK    GeneRIF: intracellular domain of teneurin-2 has a nuclear function
            and role in repressing zic-1-mediated transcription
REFERENCE   9  (residues 1 to 2765)
  AUTHORS   Ben-Zur,T., Feige,E., Motro,B. and Wides,R.
  TITLE     The mammalian Odz gene family: homologs of a Drosophila pair-rule
            gene with expression implying distinct yet overlapping
            developmental roles
  JOURNAL   Dev Biol 217 (1), 107-120 (2000)
   PUBMED   10625539
REFERENCE   10 (residues 1 to 2765)
  AUTHORS   Oohashi,T., Zhou,X.H., Feng,K., Richter,B., Morgelin,M.,
            Perez,M.T., Su,W.D., Chiquet-Ehrismann,R., Rauch,U. and Fassler,R.
  TITLE     Mouse ten-m/Odz is a new family of dimeric type II transmembrane
            proteins expressed in many tissues
  JOURNAL   J Cell Biol 145 (3), 563-577 (1999)
   PUBMED   10225957
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008607.5, AC008642.5, AC008601.7, AC093304.4, AC008464.7,
            AC008705.6, AC011369.4, AC008637.7 and AC026689.6.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN03465403,
                              SAMN03465404 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2765
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..2765
                     /product="teneurin-2 isoform 1"
                     /note="odd Oz/ten-m homolog 2; teneurin-2; neurestin
                     alpha; odz, odd Oz/ten-m homolog 2; tenascin-M2; protein
                     Odd Oz/ten-m homolog 2"
                     /calculated_mol_wt=306756
     Region          10..374
                     /region_name="Ten_N"
                     /note="Teneurin Intracellular Region; pfam06484"
                     /db_xref="CDD:461932"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTS5; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          111..271
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHK6; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9R1K2; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R1K2; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            380..400
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            443
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            482
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            528..529
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          575..734
                     /region_name="DUF5885"
                     /note="Family of unknown function (DUF5885); pfam19232"
                     /db_xref="CDD:437064"
     Region          756..798
                     /region_name="DSL"
                     /note="Delta serrate ligand; cl19567"
                     /db_xref="CDD:473190"
     Region          798..831
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          834..864
                     /region_name="acid_disulf_rpt"
                     /note="acidic double-disulfide repeat; NF033662"
                     /db_xref="CDD:411265"
     Site            916
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            939
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1231..1561
                     /region_name="NHL"
                     /note="NHL repeat unit of beta-propeller proteins;
                     cl18310"
                     /db_xref="CDD:302697"
     Region          1231..1270
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Site            1258
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1263..1307
                     /region_name="NHL 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1282..1325
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1333..1377
                     /region_name="NHL 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1349..1387
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1392..1443
                     /region_name="NHL 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1403..1444
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1465..1492
                     /region_name="NHL 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1467..1500
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1521..1564
                     /region_name="NHL 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1522..2458
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          1535..1561
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1574..1593
                     /region_name="YD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            1607
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1610..1630
                     /region_name="YD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1673..1692
                     /region_name="YD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1693..1715
                     /region_name="YD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            1703
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            1740
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            1764
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            1798
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            1883
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1886..1905
                     /region_name="YD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1927..1945
                     /region_name="YD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1946..1966
                     /region_name="YD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1973..1990
                     /region_name="YD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            1984
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          1991..2012
                     /region_name="YD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2013..2030
                     /region_name="YD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2033..2053
                     /region_name="YD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2056..2076
                     /region_name="YD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2084..2104
                     /region_name="YD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2110..2127
                     /region_name="YD 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2128..2154
                     /region_name="YD 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2156..2169
                     /region_name="YD 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2170..2193
                     /region_name="YD 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            2188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2196..2216
                     /region_name="YD 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2217..2237
                     /region_name="YD 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2239..2259
                     /region_name="YD 20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2271..2291
                     /region_name="YD 21"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2293..2313
                     /region_name="YD 22"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            2328
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2339..2380
                     /region_name="YD 23"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT68.3)"
     Site            2639
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT68.3)"
     Region          2681..2758
                     /region_name="Tox-GHH"
                     /note="GHH signature containing HNH/Endo VII superfamily
                     nuclease toxin; pfam15636"
                     /db_xref="CDD:464783"
     CDS             1..2765
                     /gene="TENM2"
                     /gene_synonym="ODZ2; ten-2; TEN-M2; TEN2; TNM2"
                     /coded_by="NM_001122679.2:190..8487"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:57451"
                     /db_xref="HGNC:HGNC:29943"
                     /db_xref="MIM:610119"
ORIGIN      
        1 mdvkdrrhrs ltrgrcgkec rytsssldse dcrvptqksy sssetlkayd hdsrmhygnr
       61 vtdlihresd efprqgtnft laelgiceps phrsgycsdm gilhqgysls tgsdadsdte
      121 ggmspehair lwgrgiksrr ssglssrens altltdsdne nksddengrp ipptsspsll
      181 psaqlpsshn pppvscqmpl ldsntshqim dtnpdeefsp nsyllracsg pqqasssgpp
      241 nhhsqstlrp plppphnhtl shhhssansl nrnsltnrrs qihapapapn dlattpesvq
      301 lqdswvlnsn vpletrhflf ktssgstplf sssspgyplt sgtvytpppr llprntfsrk
      361 afklkkpsky cswkcaalsa iaaalllail layfiamhll glnwqlqpad ghtfnngirt
      421 glpgnddvat mpsggkvpws lknssidsge aevgrrvtqe vppgvfwrsq ihisqpqflk
      481 fnislgkdal fgvyirrglp pshaqydfme rldgkekwsv vesprerrsi qtlvqneavf
      541 vqyldvglwh lafyndgkdk emvsfntvvl dsvqdcprnc hgngecvsgv chcfpgflga
      601 dcakaacpvl csgngqyskg tcqcysgwkg aecdvpmnqc idpscgghgs cidgncvcsa
      661 gykgehceev dcldptcssh gvcvngeclc spgwgglnce larvqcpdqc sghgtylpdt
      721 glcscdpnwm gpdcsvevcs vdcgthgvci ggacrceegw tgaacdqrvc hprciehgtc
      781 kdgkcecreg wngehctidg cpdlcngngr ctlgqnswqc vcqtgwrgpg cnvametsca
      841 dnkdnegdgl vdcldpdccl qsacqnsllc rgsrdpldii qqgqtdwpav ksfydrikll
      901 agkdsthiip genpfnsslv slirgqvvtt dgtplvgvnv sfvkypkygy titrqdgtfd
      961 lianggaslt lhferapfms qertvwlpwn sfyamdtlvm kteensipsc dlsgfvrpdp
     1021 iiissplstf fsaapgqnpi vpetqvlhee ielpgsnvkl rylssrtagy ksllkitmtq
     1081 stvplnlirv hlmvaveghl fqksfqaspn laytfiwdkt daygqrvygl sdavvsvgfe
     1141 yetcpslilw ekrtallqgf eldpsnlggw sldkhhilnv ksgilhkgtg enqfltqqpa
     1201 iitsimgngr rrsiscpscn glaegnklla pvalavgidg slyvgdfnyi rrifpsrnvt
     1261 silelrnkef khsnnpahky ylavdpvsgs lyvsdtnsrr iyrvkslsgt kdlagnsevv
     1321 agtgeqclpf dearcgdggk aidatlmspr giavdknglm yfvdatmirk vdqngiistl
     1381 lgsndltavr plscdssmdv aqvrlewptd lavnpmdnsl yvlennvilr itenhqvsii
     1441 agrpmhcqvp gidyslskla ihsalesasa iaishtgvly itetdekkin rlrqvttnge
     1501 icllagaasd cdckndvncn cysgddayat dailnspssl avapdgtiyi adlgnirira
     1561 vsknkpvlna fnqyeaaspg eqelyvfnad gihqytvslv tgeylynfty stdndvteli
     1621 dnngnslkir rdssgmprhl lmpdnqiitl tvgtngglkv vstqnlelgl mtydgntgll
     1681 atksdetgwt tfydydhegr ltnvtrptgv vtslhremek sitidiensn rdddvtvitn
     1741 lssveasytv vqdqvrnsyq lcnngtlrvm yangmgisfh sephvlagti tptigrcnis
     1801 lpmenglnsi ewrlrkeqik gkvtifgrkl rvhgrnllsi dydrnirtek iyddhrkftl
     1861 riiydqvgrp flwlpssgla avnvsyffng rlaglqrgam sertdidkqg rivsrmfadg
     1921 kvwsysyldk smvlllqsqr qyifeydssd rllavtmpsv arhsmsthts igyirniynp
     1981 pesnasvifd ysddgrilkt sflgtgrqvf ykygklskls eivydstavt fgydettgvl
     2041 kmvnlqsggf sctiryrkig plvdkqiyrf seegmvnarf dytyhdnsfr iasikpvise
     2101 tplpvdlyry deisgkvehf gkfgviyydi nqiittavmt lskhfdthgr ikevqyemfr
     2161 slmywmtvqy dsmgrvikre lklgpyantt kytydydgdg qlqsvavndr ptwrysydln
     2221 gnlhllnpgn svrlmplryd lrdritrlgd vqykidddgy lcqrgsdife ynskglltra
     2281 ynkasgwsvq yrydgvgrra syktnlghhl qyfysdlhnp trithvynhs nseitslyyd
     2341 lqghlfames ssgeeyyvas dntgtplavf singlmikql qytaygeiyy dsnpdfqmvi
     2401 gfhgglydpl tklvhftqrd ydvlagrwts pdytmwknvg kepapfnlym fksnnplsse
     2461 ldlknyvtdv kswlvmfgfq lsniipgfpr akmyfvpppy elsesqasen gqlitgvqqt
     2521 terhnqafma legqvitkkl hasirekagh wfatttpiig kgimfaikeg rvttgvssia
     2581 sedsrkvasv lnnayyldkm hysiegkdth yfvkigsadg dlvtlgttig rkvlesgvnv
     2641 tvsqptllvn grtrrftnie fqystlllsi rygltpdtld eekarvldqa rqralgtawa
     2701 keqqkardgr egsrlwtege kqqllstgrv qgyegyyvlp veqypelads ssniqflrqn
     2761 emgkr
//
LOCUS       NP_064425                540 aa            linear   PRI 27-APR-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 9
            isoform 1 [Homo sapiens].
ACCESSION   NP_064425
VERSION     NP_064425.2
DBSOURCE    REFSEQ: accession NM_020041.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Quinlivan,R., Murphy,E., Pula,S., Pain,A., Brain,H., Scopes,G.,
            Gjika,F., Ahmadouk,N., Manole,A. and Houlden,H.
  TITLE     Raised CK and acute kidney injury following intense exercise in
            three patients with a history of exercise intolerance due to
            homozygous mutations in SLC2A9
  JOURNAL   Neuromuscul Disord 34, 49-53 (2024)
   PUBMED   38150892
  REMARK    GeneRIF: Raised CK and acute kidney injury following intense
            exercise in three patients with a history of exercise intolerance
            due to homozygous mutations in SLC2A9.
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Ueda,M., Fukui,K., Kamatani,N., Kamitsuji,S., Matsuo,A., Sasase,T.,
            Nishiu,J. and Matsushita,M.
  TITLE     GLUT9 as a potential drug target for chronic kidney disease: Drug
            target validation by a Mendelian randomization study
  JOURNAL   J Hum Genet 68 (10), 699-704 (2023)
   PUBMED   37308567
  REMARK    GeneRIF: GLUT9 as a potential drug target for chronic kidney
            disease: Drug target validation by a Mendelian randomization study.
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Perdomo-Ramirez,A., Cordoba-Lanus,E., Trujillo-Frias,C.J.,
            Gonzalez-Navasa,C., Ramos-Trujillo,E., Luis-Yanes,M.I.,
            Garcia-Nieto,V. and Claverie-Martin,F.
  CONSRTM   RenalTube
  TITLE     Pathogenic Variants of SLC22A12 (URAT1) and SLC2A9 (GLUT9) in
            Spanish Patients with Renal Hypouricemia: Founder Effect of SLC2A9
            Variant c.374C>T; p.(T125M)
  JOURNAL   Int J Mol Sci 24 (9), 8455 (2023)
   PUBMED   37176161
  REMARK    GeneRIF: Pathogenic Variants of SLC22A12 (URAT1) and SLC2A9 (GLUT9)
            in Spanish Patients with Renal Hypouricemia: Founder Effect of
            SLC2A9 Variant c.374C>T; p.(T125M).
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Toyoda,Y., Miyata,H., Uchida,N., Morimoto,K., Shigesawa,R.,
            Kassai,H., Nakao,K., Tomioka,N.H., Matsuo,H., Ichida,K.,
            Hosoyamada,M., Aiba,A., Suzuki,H. and Takada,T.
  TITLE     Vitamin C transporter SVCT1 serves a physiological role as a urate
            importer: functional analyses and in vivo investigations
  JOURNAL   Pflugers Arch 475 (4), 489-504 (2023)
   PUBMED   36749388
REFERENCE   5  (residues 1 to 540)
  AUTHORS   Cachau,R., Shahsavari,S. and Cho,S.K.
  TITLE     The in-silico evaluation of important GLUT9 residue for uric acid
            transport based on renal hypouricemia type 2
  JOURNAL   Chem Biol Interact 373, 110378 (2023)
   PUBMED   36736875
  REMARK    GeneRIF: The in-silico evaluation of important GLUT9 residue for
            uric acid transport based on renal hypouricemia type 2.
REFERENCE   6  (residues 1 to 540)
  AUTHORS   Richardson,S., Neama,G., Phillips,T., Bell,S., Carter,S.D.,
            Moley,K.H., Moley,J.F., Vannucci,S.J. and Mobasheri,A.
  TITLE     Molecular characterization and partial cDNA cloning of facilitative
            glucose transporters expressed in human articular chondrocytes;
            stimulation of 2-deoxyglucose uptake by IGF-I and elevated MMP-2
            secretion by glucose deprivation
  JOURNAL   Osteoarthritis Cartilage 11 (2), 92-101 (2003)
   PUBMED   12554125
REFERENCE   7  (residues 1 to 540)
  AUTHORS   Mobasheri,A., Neama,G., Bell,S., Richardson,S. and Carter,S.D.
  TITLE     Human articular chondrocytes express three facilitative glucose
            transporter isoforms: GLUT1, GLUT3 and GLUT9
  JOURNAL   Cell Biol Int 26 (3), 297-300 (2002)
   PUBMED   11991658
  REMARK    GeneRIF: GLUT9 is expressed by normal articular chondrocytes.
REFERENCE   8  (residues 1 to 540)
  AUTHORS   Shikhman,A.R., Brinson,D.C., Valbracht,J. and Lotz,M.K.
  TITLE     Cytokine regulation of facilitated glucose transport in human
            articular chondrocytes
  JOURNAL   J Immunol 167 (12), 7001-7008 (2001)
   PUBMED   11739520
REFERENCE   9  (residues 1 to 540)
  AUTHORS   Doege,H., Bocianski,A., Joost,H.G. and Schurmann,A.
  TITLE     Activity and genomic organization of human glucose transporter 9
            (GLUT9), a novel member of the family of sugar-transport
            facilitators predominantly expressed in brain and leucocytes
  JOURNAL   Biochem J 350 Pt 3 (Pt 3), 771-776 (2000)
   PUBMED   10970791
  REMARK    Erratum:[Biochem J 2001 Sep 15;358(Pt 3):791-2]
REFERENCE   10 (residues 1 to 540)
  AUTHORS   Phay,J.E., Hussain,H.B. and Moley,J.F.
  TITLE     Cloning and expression analysis of a novel member of the
            facilitative glucose transporter family, SLC2A9 (GLUT9)
  JOURNAL   Genomics 66 (2), 217-220 (2000)
   PUBMED   10860667
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005674.11, BI821650.1,
            CD629819.1, CD629822.1, BC018897.2 and AL572022.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 2, 2004 this sequence version replaced NP_064425.1.
            
            Summary: This gene encodes a member of the SLC2A facilitative
            glucose transporter family. Members of this family play a
            significant role in maintaining glucose homeostasis. The encoded
            protein may play a role in the development and survival of
            chondrocytes in cartilage matrices. Two transcript variants
            encoding distinct isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript, and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110414.1, SRR1803615.94999.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264784.8/ ENSP00000264784.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.1"
     Protein         1..540
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 9 isoform 1"
                     /note="urate voltage-driven efflux transporter 1; human
                     glucose transporter-like protein-9; GLUT-9; glucose
                     transporter type 9; solute carrier family 2 (facilitated
                     glucose transporter), member 9; urate transporter"
                     /calculated_mol_wt=58571
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Region          59..510
                     /region_name="MFS_GLUT_Class2"
                     /note="Class 2 Glucose transporters (GLUTs) of the Major
                     Facilitator Superfamily; cd17432"
                     /db_xref="CDD:340990"
     Site            order(71,75,206,209..210,213,327..328,332..333,336..337,
                     364,426..427,430..431,435,458..459,462)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340990"
     Site            90
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            172..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            201..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            317..337
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            355..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            382..402
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            416..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            452..472
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            479..499
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NRM0.2)"
     Region          519..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM0.2)"
     CDS             1..540
                     /gene="SLC2A9"
                     /gene_synonym="GLUT9; GLUTX; UAQTL2; URATv1"
                     /coded_by="NM_020041.3:69..1691"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3407.1"
                     /db_xref="GeneID:56606"
                     /db_xref="HGNC:HGNC:13446"
                     /db_xref="MIM:606142"
ORIGIN      
        1 markqnrnsk elglvpltdd tshagppgpg rallecdhlr sgvpggrrrk dwscsllvas
       61 lagafgssfl ygynlsvvna ptpyikafyn eswerrhgrp idpdtltllw svtvsifaig
      121 glvgtlivkm igkvlgrkht llanngfais aallmacslq agafemlivg rfimgidggv
      181 alsvlpmyls eispkeirgs lgqvtaific igvftgqllg lpellgkest wpylfgvivv
      241 pavvqllslp flpdspryll lekhnearav kafqtflgka dvsqeveevl aesrvqrsir
      301 lvsvlellra pyvrwqvvtv ivtmacyqlc glnaiwfytn sifgkagipp akipyvtlst
      361 ggietlaavf sglviehlgr rplliggfgl mglffgtlti tltlqdhapw vpylsivgil
      421 aiiasfcsgp ggipfiltge ffqqsqrpaa fiiagtvnwl snfavgllfp fiqksldtyc
      481 flvfaticit gaiylyfvlp etknrtyaei sqafskrnka yppeekidsa vtdgkingrp
//
LOCUS       NP_065161                706 aa            linear   PRI 27-APR-2025
DEFINITION  choline transporter-like protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_065161
VERSION     NP_065161.3
DBSOURCE    REFSEQ: accession NM_020428.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Song,T., Zhao,S., Luo,S., Chen,C., Liu,X., Wu,X., Sun,Z., Cao,J.,
            Wang,Z., Wang,Y., Yu,B., Zhang,Z., Du,X., Li,X., Han,Z., Chen,H.,
            Chen,F., Wang,L., Wang,H., Sun,K., Han,Y., Xie,L. and Ji,Y.
  TITLE     SLC44A2 regulates vascular smooth muscle cell phenotypic switching
            and aortic aneurysm
  JOURNAL   J Clin Invest 134 (16), e173690 (2024)
   PUBMED   38916960
  REMARK    GeneRIF: SLC44A2 regulates vascular smooth muscle cell phenotypic
            switching and aortic aneurysm.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Koehl,B., Vrignaud,C., Mikdar,M., Nair,T.S., Yang,L., Landry,S.,
            Laiguillon,G., Giroux-Lathuile,C., Anselme-Martin,S., El Kenz,H.,
            Hermine,O., Mohandas,N., Cartron,J.P., Colin,Y., Detante,O.,
            Marlu,R., Le Van Kim,C., Carey,T.E., Azouzi,S. and Peyrard,T.
  TITLE     Lack of the human choline transporter-like protein SLC44A2 causes
            hearing impairment and a rare red blood phenotype
  JOURNAL   EMBO Mol Med 15 (3), e16320 (2023)
   PUBMED   36695047
  REMARK    GeneRIF: Lack of the human choline transporter-like protein SLC44A2
            causes hearing impairment and a rare red blood phenotype.
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Zirka,G., Robert,P., Tilburg,J., Tishkova,V., Maracle,C.X.,
            Legendre,P., van Vlijmen,B.J.M., Alessi,M.C., Lenting,P.J.,
            Morange,P.E. and Thomas,G.M.
  TITLE     Impaired adhesion of neutrophils expressing Slc44a2/HNA-3b to VWF
            protects against NETosis under venous shear rates
  JOURNAL   Blood 137 (16), 2256-2266 (2021)
   PUBMED   33556175
  REMARK    GeneRIF: Impaired adhesion of neutrophils expressing Slc44a2/HNA-3b
            to VWF protects against NETosis under venous shear rates.
REFERENCE   4  (residues 1 to 706)
  AUTHORS   Fujita,Y., Nagakura,T., Uchino,H., Inazu,M. and Yamanaka,T.
  TITLE     Functional Expression of Choline Transporters in Human Neural Stem
            Cells and Its Link to Cell Proliferation, Cell Viability, and
            Neurite Outgrowth
  JOURNAL   Cells 10 (2), 453 (2021)
   PUBMED   33672580
  REMARK    GeneRIF: Functional Expression of Choline Transporters in Human
            Neural Stem Cells and Its Link to Cell Proliferation, Cell
            Viability, and Neurite Outgrowth.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 706)
  AUTHORS   Taylor,A., Grapentine,S., Ichhpuniani,J. and Bakovic,M.
  TITLE     Choline transporter-like proteins 1 and 2 are newly identified
            plasma membrane and mitochondrial ethanolamine transporters
  JOURNAL   J Biol Chem 296, 100604 (2021)
   PUBMED   33789160
  REMARK    GeneRIF: Choline transporter-like proteins 1 and 2 are newly
            identified plasma membrane and mitochondrial ethanolamine
            transporters.
REFERENCE   6  (residues 1 to 706)
  AUTHORS   Kommareddi,P.K., Nair,T.S., Raphael,Y., Telian,S.A., Kim,A.H.,
            Arts,H.A., El-Kashlan,H.K. and Carey,T.E.
  TITLE     Cochlin isoforms and their interaction with CTL2 (SLC44A2) in the
            inner ear
  JOURNAL   J Assoc Res Otolaryngol 8 (4), 435-446 (2007)
   PUBMED   17926100
  REMARK    GeneRIF: CTL2 is more widely distributed than previously described,
            and its prominent expression on cells facing the scala media
            suggests a possible role in homeostasis.
REFERENCE   7  (residues 1 to 706)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   8  (residues 1 to 706)
  AUTHORS   Traiffort,E., Ruat,M., O'Regan,S. and Meunier,F.M.
  TITLE     Molecular characterization of the family of choline
            transporter-like proteins and their splice variants
  JOURNAL   J Neurochem 92 (5), 1116-1125 (2005)
   PUBMED   15715662
REFERENCE   9  (residues 1 to 706)
  AUTHORS   Nair,T.S., Kozma,K.E., Hoefling,N.L., Kommareddi,P.K., Ueda,Y.,
            Gong,T.W., Lomax,M.I., Lansford,C.D., Telian,S.A., Satar,B.,
            Arts,H.A., El-Kashlan,H.K., Berryhill,W.E., Raphael,Y. and
            Carey,T.E.
  TITLE     Identification and characterization of choline transporter-like
            protein 2, an inner ear glycoprotein of 68 and 72 kDa that is the
            target of antibody-induced hearing loss
  JOURNAL   J Neurosci 24 (7), 1772-1779 (2004)
   PUBMED   14973250
REFERENCE   10 (residues 1 to 706)
  AUTHORS   O'Regan,S., Traiffort,E., Ruat,M., Cha,N., Compaore,D. and
            Meunier,F.M.
  TITLE     An electric lobe suppressor for a yeast choline transport mutation
            belongs to a new family of transporter-like proteins
  JOURNAL   Proc Natl Acad Sci U S A 97 (4), 1835-1840 (2000)
   PUBMED   10677542
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA749803.1, DA673268.1, BC040556.1 and AC011475.6.
            
            On Feb 6, 2009 this sequence version replaced NP_065161.2.
            
            Transcript Variant: This variant encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042692.1, FN668568.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335757.10/ ENSP00000336888.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..706
                     /product="choline transporter-like protein 2 isoform 1"
                     /note="choline transporter-like protein 2; solute carrier
                     family 44 (choline transporter), member 2; testicular
                     tissue protein Li 47"
                     /calculated_mol_wt=79993
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            187
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            200
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            316..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Region          337..676
                     /region_name="Choline_transpo"
                     /note="Plasma-membrane choline transporter; pfam04515"
                     /db_xref="CDD:461337"
     Site            365..385
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            417
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            458..480
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            505..525
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            564..584
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            600..620
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWA5.3)"
     Site            639..659
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWA5.3)"
     CDS             1..706
                     /gene="SLC44A2"
                     /gene_synonym="CTL2; PP1292"
                     /coded_by="NM_020428.4:82..2202"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12245.1"
                     /db_xref="GeneID:57153"
                     /db_xref="HGNC:HGNC:17292"
                     /db_xref="MIM:606106"
ORIGIN      
        1 mgderphyyg khgtpqkydp tfkgpiynrg ctdiiccvfl llaivgyvav giiawthgdp
       61 rkviyptdsr gefcgqkgtk nenkpylfyf nivkcasplv llefqcptpq icvekcpdry
      121 ltylnarssr dfeyykqfcv pgfknnkgva evlqdgdcpa vlipskplar rcfpaihayk
      181 gvlmvgnett yedghgsrkn itdlvegakk angvlearql amrifedytv swywiiiglv
      241 iamamsllfi illrflagim vwvmiimvil vlgygifhcy meysrlrgea gsdvslvdlg
      301 fqtdfrvylh lrqtwlafmi ilsileviii llliflrkri liaialikea sravgyvmcs
      361 llyplvtffl lclciaywas tavflstsne avykifddsp cpftaktcnp etfpssnesr
      421 qcpnarcqfa fyggesgyhr allglqifna fmffwlanfv lalgqvtlag afasyywalr
      481 kpddlpafpl fsafgralry htgslafgal ilaivqiirv ileyldqrlk aaenkfakcl
      541 mtclkccfwc lekfikflnr nayimiaiyg tnfctsarna ffllmrniir vavldkvtdf
      601 lfllgklliv gsvgilafff fthririvqd tapplnyywv piltvivgsy liahgffsvy
      661 gmcvdtlflc fledlerndg saerpyfmss tlkkllnktn kkaaes
//
LOCUS       NP_036161                901 aa            linear   ROD 27-APR-2025
DEFINITION  sperm-associated antigen 1 isoform 3 [Mus musculus].
ACCESSION   NP_036161
VERSION     NP_036161.2
DBSOURCE    REFSEQ: accession NM_012031.4
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Huang,C., Wu,D., Khan,F.A., Jiao,X., Guan,K. and Huo,L.
  TITLE     The GTPase SPAG-1 orchestrates meiotic program by dictating meiotic
            resumption and cytoskeleton architecture in mouse oocytes
  JOURNAL   Mol Biol Cell 27 (11), 1776-1785 (2016)
   PUBMED   27053660
  REMARK    GeneRIF: Findings broaden our knowledge of SPAG-1, showing that it
            exerts a role in oocyte meiotic execution via its involvement in
            AMPK and MAPK signaling pathways.
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Hayashida,K., Omagari,K., Masuda,J. and Kohno,S.
  TITLE     An integrase of endogenous retrovirus is involved in maternal
            mitochondrial DNA inheritance of the mouse
  JOURNAL   Biochem Biophys Res Commun 366 (1), 206-211 (2008)
   PUBMED   18054325
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Hayashida,K., Omagari,K., Masuda,J., Hazama,H., Kadokawa,Y.,
            Ohba,K. and Kohno,S.
  TITLE     The sperm mitochondria-specific translocator has a key role in
            maternal mitochondrial inheritance
  JOURNAL   Cell Biol Int 29 (6), 472-481 (2005)
   PUBMED   15979907
  REMARK    GeneRIF: The number of PCR positives of sperm mtDNA in two-cell
            embryos was significantly increased following sperm incubation with
            anti-tetratricopeptide repeat-containing protein involved in
            spermatogenesis (tpis).
REFERENCE   4  (residues 1 to 901)
  AUTHORS   Yamashita,H., Avraham,S., Jiang,S., London,R., Van Veldhoven,P.P.,
            Subramani,S., Rogers,R.A. and Avraham,H.
  TITLE     Characterization of human and murine PMP20 peroxisomal proteins
            that exhibit antioxidant activity in vitro
  JOURNAL   J Biol Chem 274 (42), 29897-29904 (1999)
   PUBMED   10514471
REFERENCE   5  (residues 1 to 901)
  AUTHORS   Takaishi,M. and Huh,Nh.
  TITLE     A tetratricopeptide repeat-containing protein gene, tpis, whose
            expression is induced with differentiation of spermatogenic cells
  JOURNAL   Biochem Biophys Res Commun 264 (1), 81-85 (1999)
   PUBMED   10527845
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC046313.1, BB706348.1 and AI843673.1.
            
            On Jun 10, 2007 this sequence version replaced NP_036161.1.
            
            Transcript Variant: This variant (3) contains an alternate exon in
            the 5' UTR, lacks a portion of the 5' coding region, and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (3) has a distinct N-terminus and is shorter than
            isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC046313.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849384 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 14.46 cM"
     Protein         1..901
                     /product="sperm-associated antigen 1 isoform 3"
                     /note="infertility-related sperm protein Spag-1;
                     TPR-containing protein involved in spermatogenesis"
                     /calculated_mol_wt=100539
     Region          202..686
                     /region_name="3a0801s09"
                     /note="mitochondrial precursor proteins import receptor
                     (72 kDa mitochondrial outermembrane protein)
                     (mitochondrial import receptor for the ADP/ATP carrier)
                     (translocase of outermembrane tom70); TIGR00990"
                     /db_xref="CDD:273380"
     Region          213..246
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Site            order(217..218,221..222,224,247,250..251,254..255,
                     257..258,281,284..285,288..289,292)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          217..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          218..>331
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          246..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..279
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Region          280..313
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Region          280..308
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          322..437
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Region          430..464
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Region          433..459
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(434..435,438..439,441,473,476..477,480..481,
                     483..484,507,510..511,514..515,518)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          471..501
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          472..505
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Region          506..534
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          507..539
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Region          606..639
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Site            order(607,610..611,614..615,617,641,644..645,648..649,
                     651..652,675,678..679,682..683,686)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          607..634
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          619..>795
                     /region_name="PLN03088"
                     /note="SGT1, suppressor of G2 allele of SKP1; Provisional"
                     /db_xref="CDD:215568"
     Region          639..669
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          640..673
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Region          694..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Site            703
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5U2X2; propagated from
                     UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07617; propagated from
                     UniProtKB/Swiss-Prot (Q80ZX8.1)"
     Region          778..869
                     /region_name="RPAP3_C"
                     /note="Potential Monad-binding region of RPAP3; pfam13877"
                     /db_xref="CDD:464012"
     CDS             1..901
                     /gene="Spag1"
                     /gene_synonym="tpis"
                     /coded_by="NM_012031.4:235..2940"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS37061.1"
                     /db_xref="GeneID:26942"
                     /db_xref="MGI:MGI:1349387"
ORIGIN      
        1 mtakakdcps lwgfgttktf kipiehldfk yiencsdvkh lekilyvlrs geegyypelt
       61 efcekcltnl apksralrkd kpaetassfs aeewekidsd lkswvseikr eentchfhdp
      121 enhpgvedpl ppvrgstccp hsgketysks ktakkriprd yaewdkfdve kecskidedy
      181 kektvinnka hlskietkie tagltekeks flanrekgkg neafysgdye eavmyytrsl
      241 salptaiayn nraqaeiklq rwssaledce kaleldpgnv kallrratty khqnklqeav
      301 ddlrkvlqve pdndlakktl severdlkns epvselqtkg krmvieeven sgdeggkgsa
      361 deredggsde aamgniqkkl mvrrseggrr srrgrtpgpr aeqqgglret atastgdshy
      421 peepraadnp sglkrrgnel frggqfaeaa aqysvaiaql eptgsanade lsilysnraa
      481 cylkegncrd ciqdcnrale lhpfsvkpll rramayetle qyrnayvdyk tvlqidcgiq
      541 lasdsanria rilteldgsk wrerlppipa vptseplrvw lpaaetpdqd pcpnncmpsi
      601 tdekmfqalk eegnqlvkdk nykdaiskyn eclkinskac aiytnralcy lklgqfeeak
      661 ldceqalqid genvkashrl alaqkglenc resgvdpsqv llspdsseaa rhldtkndta
      721 ppskgrerrr iqvqevdgss deeperpaea satsapardg vedggsaepa ekldvskptn
      781 ayefgqvlst isarkdeeac ahllaitapk dlplllsnkl egdtfllliq slkshlvakd
      841 pslvyehlly lskaerfktm ltlinkgqke qmaqlfdgls dtqsdgltae dvqalrrqye
      901 l
//
LOCUS       NP_001032229             275 aa            linear   MAM 27-APR-2025
DEFINITION  autophagy protein 5 [Sus scrofa].
ACCESSION   NP_001032229 XP_020946137
VERSION     NP_001032229.2
DBSOURCE    REFSEQ: accession NM_001037152.2
KEYWORDS    RefSeq.
SOURCE      Sus scrofa (pig)
  ORGANISM  Sus scrofa
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae;
            Sus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Kim,S.H., Min,K.S., Kim,N.H. and Yoon,J.T.
  TITLE     Differential expression of programmed cell death on the follicular
            development in normal and miniature pig ovary
  JOURNAL   PLoS One 7 (10), e46194 (2012)
   PUBMED   23056260
  REMARK    GeneRIF: Data indicate that the expression of MAP1LC3A, B and
            autophagy-associated genes (ATG5, mTOR, Beclin-1) was increased in
            normal pigs, while decreased in miniature pigs.
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Uenishi,H., Eguchi-Ogawa,T., Shinkai,H., Okumura,N., Suzuki,K.,
            Toki,D., Hamasima,N. and Awata,T.
  TITLE     PEDE (Pig EST Data Explorer) has been expanded into Pig Expression
            Data Explorer, including 10 147 porcine full-length cDNA sequences
  JOURNAL   Nucleic Acids Res 35 (Database issue), D650-D653 (2007)
   PUBMED   17145712
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Uenishi,H., Eguchi,T., Suzuki,K., Sawazaki,T., Toki,D., Shinkai,H.,
            Okumura,N., Hamasima,N. and Awata,T.
  TITLE     PEDE (Pig EST Data Explorer): construction of a database for ESTs
            derived from porcine full-length cDNA libraries
  JOURNAL   Nucleic Acids Res 32 (Database issue), D484-D488 (2004)
   PUBMED   14681463
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK389447.1 and AEMK02000001.1.
            
            On or before Mar 28, 2018 this sequence version replaced
            XP_020946137.1, NP_001032229.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5250920.112078.1,
                                           SRR5120059.131421.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA103886111, SAMEA103886112
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Sus scrofa"
                     /db_xref="taxon:9823"
                     /chromosome="1"
                     /map="1"
     Protein         1..275
                     /product="autophagy protein 5"
                     /note="autophagy related 5-like protein; ATG5 autophagy
                     related 5 homolog"
                     /calculated_mol_wt=32298
     Region          79..270
                     /region_name="APG5"
                     /note="Autophagy protein Apg5; pfam04106"
                     /db_xref="CDD:461175"
     CDS             1..275
                     /gene="ATG5"
                     /coded_by="NM_001037152.2:345..1172"
                     /db_xref="GeneID:100739102"
                     /db_xref="RGD:14213958"
                     /db_xref="VGNC:VGNC:103029"
ORIGIN      
        1 mtddkdvlrd vwfgriptcf tlyqdeiter eaepyylllp rvsyltlvtd kvkkhfqkvm
       61 rqediseiwf eyegtplkwh ypigllfdll asssalpwni tvhfksfpek dllhcpskdv
      121 ieahfmscvk eadalkhksq vinemqkkdh kqlwmglqnd rfdqfwainr klmeypaeen
      181 gfryipfriy qttterpfiq klfrpvasdg qlhtlgdllk evcpsavape dgerknqvmi
      241 hgiepmletp lqwlsehlsy pdnflhisii pqptd
//
LOCUS       NP_037425                282 aa            linear   PRI 27-APR-2025
DEFINITION  transformer-2 protein homolog alpha isoform 1 [Homo sapiens].
ACCESSION   NP_037425
VERSION     NP_037425.1
DBSOURCE    REFSEQ: accession NM_013293.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Cao,W., Lei,S., Zeng,Z., Xiao,C., Sun,B., Xie,P., Li,Y., Luo,D. and
            Yu,W.
  TITLE     Transformer 2 alpha homolog is a downstream gene of
            hypoxia-inducible factor 1 subunit alpha and is involved in the
            progression of pancreatic cancer
  JOURNAL   Bioengineered 13 (5), 13238-13251 (2022)
   PUBMED   35635094
  REMARK    GeneRIF: Transformer 2 alpha homolog is a downstream gene of
            hypoxia-inducible factor 1 subunit alpha and is involved in the
            progression of pancreatic cancer.
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Liu,Q., Zhu,L., Liu,X., Zheng,J., Liu,Y., Ruan,X., Cao,S., Cai,H.,
            Li,Z. and Xue,Y.
  TITLE     TRA2A-induced upregulation of LINC00662 regulates blood-brain
            barrier permeability by affecting ELK4 mRNA stability in
            Alzheimer's microenvironment
  JOURNAL   RNA Biol 17 (9), 1293-1308 (2020)
   PUBMED   32372707
  REMARK    GeneRIF: TRA2A-induced upregulation of LINC00662 regulates
            blood-brain barrier permeability by affecting ELK4 mRNA stability
            in Alzheimer's microenvironment.
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Gevaert,K., Staes,A., Van Damme,J., De Groot,S., Hugelier,K.,
            Demol,H., Martens,L., Goethals,M. and Vandekerckhove,J.
  TITLE     Global phosphoproteome analysis on human HepG2 hepatocytes using
            reversed-phase diagonal LC
  JOURNAL   Proteomics 5 (14), 3589-3599 (2005)
   PUBMED   16097034
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Shin,C., Feng,Y. and Manley,J.L.
  TITLE     Dephosphorylated SRp38 acts as a splicing repressor in response to
            heat shock
  JOURNAL   Nature 427 (6974), 553-558 (2004)
   PUBMED   14765198
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Tacke,R., Tohyama,M., Ogawa,S. and Manley,J.L.
  TITLE     Human Tra2 proteins are sequence-specific activators of pre-mRNA
            splicing
  JOURNAL   Cell 93 (1), 139-148 (1998)
   PUBMED   9546399
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Dauwalder,B., Amaya-Manzanares,F. and Mattox,W.
  TITLE     A human homologue of the Drosophila sex determination factor
            transformer-2 has conserved splicing regulatory functions
  JOURNAL   Proc Natl Acad Sci U S A 93 (17), 9004-9009 (1996)
   PUBMED   8799144
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP376263.1, U53209.1 and
            AB097048.1.
            
            Summary: This gene is a member of the transformer 2 homolog family
            and encodes a protein with several RRM (RNA recognition motif)
            domains. This phosphorylated nuclear protein binds to specific RNA
            sequences and plays a role in the regulation of pre-mRNA splicing.
            Alternatively spliced transcript variants have been found for this
            gene. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.463285.1,
                                           SRR5189655.158764.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297071.9/ ENSP00000297071.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.3"
     Protein         1..282
                     /product="transformer-2 protein homolog alpha isoform 1"
                     /note="transformer-2 protein homolog alpha; htra-2 alpha;
                     putative MAPK activating protein PM24; transformer-2
                     alpha; Tra2alpha; TRA2-alpha; TRA-2 alpha; transformer-2
                     protein homolog A"
                     /calculated_mol_wt=32558
     Region          1..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13595.1)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13595.1)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13595.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13595.1)"
     Region          118..197
                     /region_name="RRM_TRA2"
                     /note="RNA recognition motif (RRM) found in transformer-2
                     protein homolog TRA2-alpha, TRA2-beta and similar
                     proteins; cd12363"
                     /db_xref="CDD:409798"
     Site            order(120,124..125,149,151,160,162,164,166,188..191,
                     194..197)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409798"
     Region          198..225
                     /region_name="Linker"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Region          201..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     Site            232
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFR5; propagated from
                     UniProtKB/Swiss-Prot (Q13595.1)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13595.1)"
     Region          260..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13595.1)"
     CDS             1..282
                     /gene="TRA2A"
                     /gene_synonym="AWMS1; HSU53209"
                     /coded_by="NM_013293.5:158..1006"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5383.1"
                     /db_xref="GeneID:29896"
                     /db_xref="HGNC:HGNC:16645"
                     /db_xref="MIM:602718"
ORIGIN      
        1 msdveennfe gresrsqsks ptgtparvks esrsgsrsps rvskhseshs rsrsksrsrs
       61 rrhshrrytr srshshshrr rsrsrsytpe yrrrrsrshs pmsnrrrhtg sranpdpntc
      121 lgvfglslyt terdlrevfs rygplsgvnv vydqrtgrsr gfafvyferi ddskeamera
      181 ngmeldgrri rvdysitkra htptpgiymg rpthsggggg gggggggggg grrrdsyydr
      241 gydrgydrye dydyryrrrs pspyysryrs rsrsrsyspr ry
//
LOCUS       NP_000683                517 aa            linear   PRI 27-APR-2025
DEFINITION  aldehyde dehydrogenase X, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_000683
VERSION     NP_000683.3
DBSOURCE    REFSEQ: accession NM_000692.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Wang,Y., Popovic,Z., Charkoftaki,G., Garcia-Milian,R., Lam,T.T.,
            Thompson,D.C., Chen,Y. and Vasiliou,V.
  TITLE     Multi-omics profiling reveals cellular pathways and functions
            regulated by ALDH1B1 in colon cancer cells
  JOURNAL   Chem Biol Interact 384, 110714 (2023)
   PUBMED   37716420
  REMARK    GeneRIF: Multi-omics profiling reveals cellular pathways and
            functions regulated by ALDH1B1 in colon cancer cells.
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Feng,Z., Hom,M.E., Bearrood,T.E., Rosenthal,Z.C., Fernandez,D.,
            Ondrus,A.E., Gu,Y., McCormick,A.K., Tomaske,M.G., Marshall,C.R.,
            Kline,T., Chen,C.H., Mochly-Rosen,D., Kuo,C.J. and Chen,J.K.
  TITLE     Targeting colorectal cancer with small-molecule inhibitors of
            ALDH1B1
  JOURNAL   Nat Chem Biol 18 (10), 1065-1075 (2022)
   PUBMED   35788181
  REMARK    GeneRIF: Targeting colorectal cancer with small-molecule inhibitors
            of ALDH1B1.
            Erratum:[Nat Chem Biol. 2025 Feb;21(2):309. doi:
            10.1038/s41589-024-01810-2. PMID: 39653787]
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Tsochantaridis,I., Kontopoulos,A., Voulgaridou,G.P.,
            Tsifintaris,M., Triantafyllou,C. and Pappa,A.
  TITLE     Aldehyde Dehydrogenase 1B1 Is Implicated in DNA Damage Response in
            Human Colorectal Adenocarcinoma
  JOURNAL   Cells 11 (13), 2017 (2022)
   PUBMED   35805102
  REMARK    GeneRIF: Aldehyde Dehydrogenase 1B1 Is Implicated in DNA Damage
            Response in Human Colorectal Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Baek,S.H. and Jang,Y.K.
  TITLE     AMBRA1 Negatively Regulates the Function of ALDH1B1, a Cancer Stem
            Cell Marker, by Controlling Its Ubiquitination
  JOURNAL   Int J Mol Sci 22 (21), 12079 (2021)
   PUBMED   34769507
  REMARK    GeneRIF: AMBRA1 Negatively Regulates the Function of ALDH1B1, a
            Cancer Stem Cell Marker, by Controlling Its Ubiquitination.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Stewart,M.J., Malek,K., Xiao,Q., Dipple,K.M. and Crabb,D.W.
  TITLE     The novel aldehyde dehydrogenase gene, ALDH5, encodes an active
            aldehyde dehydrogenase enzyme
  JOURNAL   Biochem Biophys Res Commun 211 (1), 144-151 (1995)
   PUBMED   7779080
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Hiraoka,L.R., Hsu,L. and Hsieh,C.L.
  TITLE     Assignment of ALDH3 to human chromosome 17p11.2 and ALDH5 to human
            chromosome 9p13
  JOURNAL   Genomics 25 (1), 323-325 (1995)
   PUBMED   7774944
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Sherman,D., Dave,V., Hsu,L.C., Peters,T.J. and Yoshida,A.
  TITLE     Diverse polymorphism within a short coding region of the human
            aldehyde dehydrogenase-5 (ALDH5) gene
  JOURNAL   Hum Genet 92 (5), 477-480 (1993)
   PUBMED   8244338
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Yoshida,A.
  TITLE     Molecular genetics of human aldehyde dehydrogenase
  JOURNAL   Pharmacogenetics 2 (4), 139-147 (1992)
   PUBMED   1306115
  REMARK    Review article
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Hsu,L.C. and Chang,W.C.
  TITLE     Cloning and characterization of a new functional human aldehyde
            dehydrogenase gene
  JOURNAL   J Biol Chem 266 (19), 12257-12265 (1991)
   PUBMED   2061311
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB256700.1, DA599259.1,
            AK313344.1, AL135785.10 and AI803741.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 27, 2002 this sequence version replaced NP_000683.2.
            
            Summary: This protein belongs to the aldehyde dehydrogenases family
            of proteins. Aldehyde dehydrogenase is the second enzyme of the
            major oxidative pathway of alcohol metabolism. This gene does not
            contain introns in the coding sequence. The variation of this locus
            may affect the development of alcohol-related problems. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001619.1, SRR1803614.55344.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000377698.4/
                                                  ENSP00000366927.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.1"
     Protein         1..517
                     /product="aldehyde dehydrogenase X, mitochondrial
                     precursor"
                     /EC_number="1.2.1.3"
                     /note="aldehyde dehydrogenase 5; acetaldehyde
                     dehydrogenase 5; ALDH class 2; aldehyde dehydrogenase X,
                     mitochondrial; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=55324
     transit_peptide 1..17
                     /calculated_mol_wt=1943
     mat_peptide     18..517
                     /product="aldehyde dehydrogenase X, mitochondrial"
                     /calculated_mol_wt=55324
     Region          31..511
                     /region_name="ALDH_F1AB_F2_RALDH1"
                     /note="NAD+-dependent retinal dehydrogenase 1, ALDH
                     families 1A, 1B, and 2-like; cd07141"
                     /db_xref="CDD:143459"
     Site            51
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CZS1; propagated from
                     UniProtKB/Swiss-Prot (P30837.4)"
     Site            52
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CZS1; propagated from
                     UniProtKB/Swiss-Prot (P30837.4)"
     Site            order(89..90,94,97,99,103,144,147..148,152,154..155,
                     158..162,164..165,168..175,268,271,274..275,278..279,281,
                     286,451,453,460,463,465..472,479..481,484..487,489,492,
                     497,504..509,511)
                     /site_type="other"
                     /note="homotetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143459"
     Site            order(182..185,209,212,242,246..247,260,263,266,286..287,
                     319,366,369,416)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143459"
     Site            order(186,285,316,319)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143459"
     Site            186
                     /site_type="other"
                     /note="Transition state stabilizer. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P30837.4)"
     Site            364
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CZS1; propagated from
                     UniProtKB/Swiss-Prot (P30837.4)"
     Site            383
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CZS1; propagated from
                     UniProtKB/Swiss-Prot (P30837.4)"
     Site            399
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CZS1; propagated from
                     UniProtKB/Swiss-Prot (P30837.4)"
     Site            414
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CZS1; propagated from
                     UniProtKB/Swiss-Prot (P30837.4)"
     Site            426
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CZS1; propagated from
                     UniProtKB/Swiss-Prot (P30837.4)"
     Site            429
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CZS1; propagated from
                     UniProtKB/Swiss-Prot (P30837.4)"
     CDS             1..517
                     /gene="ALDH1B1"
                     /gene_synonym="ALDH5; ALDHX"
                     /coded_by="NM_000692.5:116..1669"
                     /db_xref="CCDS:CCDS6615.1"
                     /db_xref="GeneID:219"
                     /db_xref="HGNC:HGNC:407"
                     /db_xref="MIM:100670"
ORIGIN      
        1 mlrflaprll slqgrtarys saaalpspil npdipynqlf innewqdavs kktfptvnpt
       61 tgevighvae gdradvdrav kaareafrlg spwrrmdase rgrllnrlad lverdrvyla
      121 sletldngkp fqesyaldld evikvyryfa gwadkwhgkt ipmdgqhfcf trhepvgvcg
      181 qiipwnfplv mqgwklapal atgntvvmkv aeqtplsaly laslikeagf ppgvvniitg
      241 ygptagaaia qhvdvdkvaf tgstevghli qkaagdsnlk rvtlelggks psivladadm
      301 ehaveqchea lffnmgqccc agsrtfvees iyneflertv ekakqrkvgn pfeldtqqgp
      361 qvdkeqferv lgyiqlgqke gakllcgger fgergffikp tvfggvqddm riakeeifgp
      421 vqplfkfkki eevverannt ryglaaavft rdldkamyft qalqagtvwv ntynivtcht
      481 pfggfkesgn grelgedglk aytevktvti kvpqkns
//
LOCUS       NP_001129047              91 aa            linear   PRI 27-APR-2025
DEFINITION  small integral membrane protein 13 [Homo sapiens].
ACCESSION   NP_001129047 XP_001720466 XP_001725041 XP_001725413
VERSION     NP_001129047.1
DBSOURCE    REFSEQ: accession NM_001135575.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Cai,D.C., Fonteijn,H., Guadalupe,T., Zwiers,M., Wittfeld,K.,
            Teumer,A., Hoogman,M., Arias-Vasquez,A., Yang,Y., Buitelaar,J.,
            Fernandez,G., Brunner,H.G., van Bokhoven,H., Franke,B.,
            Hegenscheid,K., Homuth,G., Fisher,S.E., Grabe,H.J., Francks,C. and
            Hagoort,P.
  TITLE     A genome-wide search for quantitative trait loci affecting the
            cortical surface area and thickness of Heschl's gyrus
  JOURNAL   Genes Brain Behav 13 (7), 675-685 (2014)
   PUBMED   25130324
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136139.6, BC032356.1 and AA724884.1.
            
            On or before Oct 2, 2008 this sequence version replaced
            XP_001725041.1, XP_001720466.1, XP_001725413.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.170665.1,
                                           SRR1803616.132444.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000416247.4/ ENSP00000451866.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.2"
     Protein         1..91
                     /product="small integral membrane protein 13"
                     /note="UPF0766 protein C6orf228"
                     /calculated_mol_wt=10220
     Region          1..46
                     /region_name="DUF4750"
                     /note="Domain of unknown function (DUF4750); pfam15938"
                     /db_xref="CDD:464949"
     Site            10..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DJ93.1)"
     Region          47..91
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DJ93.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q942; propagated from
                     UniProtKB/Swiss-Prot (P0DJ93.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q942; propagated from
                     UniProtKB/Swiss-Prot (P0DJ93.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:E9Q942; propagated from
                     UniProtKB/Swiss-Prot (P0DJ93.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q942; propagated from
                     UniProtKB/Swiss-Prot (P0DJ93.1)"
     CDS             1..91
                     /gene="SMIM13"
                     /gene_synonym="C6orf228"
                     /coded_by="NM_001135575.2:481..756"
                     /db_xref="CCDS:CCDS56396.1"
                     /db_xref="GeneID:221710"
                     /db_xref="HGNC:HGNC:27356"
ORIGIN      
        1 mwhsvgltll vfvatllivl llmvcgwyfv whlflskfkf lrelvgdtgs qegdhepsgs
       61 eteedtsssp hrirsarqrr apadeghrpl t
//
LOCUS       NP_001071428             787 aa            linear   MAM 27-APR-2025
DEFINITION  zinc finger protein 227 [Bos taurus].
ACCESSION   NP_001071428 XP_602431
VERSION     NP_001071428.1
DBSOURCE    REFSEQ: accession NM_001077960.2
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC126592.1.
            
            On Nov 21, 2006 this sequence version replaced XP_602431.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC126592.1, SRR5571257.48133.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA6648753, SAMEA6648754
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="18"
                     /map="18"
                     /breed="Hereford"
     Protein         1..787
                     /product="zinc finger protein 227"
                     /calculated_mol_wt=89230
     Region          23..83
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          245..279
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <296..482
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          314..334
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          342..362
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          370..390
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(375,377,379,381..382,385..386,389,403,405,409..410,
                     413..414,417,431,433,435,437..438,441..442,445)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          394..774
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          398..418
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          426..446
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          454..474
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          482..502
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          510..530
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(515,517,519,521..522,525..526,529,543,545,549..550,
                     553..554,557,571,573,575,577..578,581..582,585)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          538..558
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          566..586
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          594..614
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          622..642
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(627,629,631,633..634,637..638,641,655,657,661..662,
                     665..666,669,683,685,687,689..690,693..694,697)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          650..670
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          678..698
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          706..726
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          734..754
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          762..782
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..787
                     /gene="ZNF227"
                     /coded_by="NM_001077960.2:229..2592"
                     /db_xref="BGD:BT18878"
                     /db_xref="GeneID:524111"
                     /db_xref="VGNC:VGNC:58349"
ORIGIN      
        1 mpsqdsdfpq kehekmtefq eavtfkdvav vfteeelgll dsaqrklyqd vmvenfrnlv
       61 svghvpfkad mvsqleteek lwtmeretqr nghsseihsa vtsgskipne metlgkvmfk
      121 ylsceelscw qiwkhttndl tlqrksswfl hgdslqvsed enhimnhkgd hfgclenqef
      181 liptaqascg srclsesenp srgkqmsvkn hlhvcegftk nsplsdpgkt dakqtpckge
      241 rphpcrvcge gfshgavlpv hqvdpgekcs hlqthqrihp ggtvnkcpks gdgfhqnsfh
      301 phhsnptgek syrcdscgka fgsstgliih yrthtgekpy rceacgkcfs qssnfqchqr
      361 vhteekpykc eecgkgfgws vnlrvhqrvh rgekpykcee cgkgftqaah yhihqrvhtg
      421 ekpykcdvcg kgfshnspli chrrvhtgek pyrceacgkg ftrntdlhih frvhtgekpy
      481 tckecgkgfs qasnlqvhqn vhtgekrfkc etcgkgfsqs sklqthqrvh tgekpyrcdv
      541 cgkdfsyssn lklhqvihtg ekpytceacg kgfswrsnlh ahqrvhsgek pykceacdks
      601 fsqaidfrvh qrvhtgekpy kcgvcgkgfs qssglqshqr vhtgekpykc dvcgkgfrys
      661 sqfiyhqrgh tgekpykcee cgkgfgrsln lrhhqrvhtg ekphkceecg kafslpsnlr
      721 vhlsvhtrek lfkcedcgkg fsqssrlqah qrvhtgekpy kcnicgkdfs hrsrltyhqk
      781 vhtgknl
//
LOCUS       NP_004696                761 aa            linear   PRI 27-APR-2025
DEFINITION  52 kDa repressor of the inhibitor of the protein kinase [Homo
            sapiens].
ACCESSION   NP_004696
VERSION     NP_004696.2
DBSOURCE    REFSEQ: accession NM_004705.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Now,H. and Yoo,J.Y.
  TITLE     A protein-kinase, IFN-inducible double-stranded RNA dependent
            inhibitor and repressor of p58 (PRKRIR) enhances type I
            IFN-mediated antiviral response through the stability control of
            RIG-I protein
  JOURNAL   Biochem Biophys Res Commun 413 (3), 487-493 (2011)
   PUBMED   21910972
  REMARK    GeneRIF: PRKRIR provides a novel positive regulator controlling the
            RIG-I-IFN production system through protein stability control.
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Silva,L.K., Blanton,R.E., Parrado,A.R., Melo,P.S., Morato,V.G.,
            Reis,E.A., Dias,J.P., Castro,J.M., Vasconcelos,P.F., Goddard,K.A.,
            Barreto,M.L., Reis,M.G. and Teixeira,M.G.
  TITLE     Dengue hemorrhagic fever is associated with polymorphisms in JAK1
  JOURNAL   Eur J Hum Genet 18 (11), 1221-1227 (2010)
   PUBMED   20588308
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Johnatty,S.E., Beesley,J., Chen,X., Macgregor,S., Duffy,D.L.,
            Spurdle,A.B., deFazio,A., Gava,N., Webb,P.M., Rossing,M.A.,
            Doherty,J.A., Goodman,M.T., Lurie,G., Thompson,P.J., Wilkens,L.R.,
            Ness,R.B., Moysich,K.B., Chang-Claude,J., Wang-Gohrke,S.,
            Cramer,D.W., Terry,K.L., Hankinson,S.E., Tworoger,S.S.,
            Garcia-Closas,M., Yang,H., Lissowska,J., Chanock,S.J.,
            Pharoah,P.D., Song,H., Whitemore,A.S., Pearce,C.L., Stram,D.O.,
            Wu,A.H., Pike,M.C., Gayther,S.A., Ramus,S.J., Menon,U.,
            Gentry-Maharaj,A., Anton-Culver,H., Ziogas,A., Hogdall,E.,
            Kjaer,S.K., Hogdall,C., Berchuck,A., Schildkraut,J.M.,
            Iversen,E.S., Moorman,P.G., Phelan,C.M., Sellers,T.A.,
            Cunningham,J.M., Vierkant,R.A., Rider,D.N., Goode,E.L., Haviv,I.
            and Chenevix-Trench,G.
  CONSRTM   Ovarian Cancer Association Consortium; Australian Ovarian Cancer
            Study Group; Australian Cancer Study (Ovarian Cancer)
  TITLE     Evaluation of candidate stromal epithelial cross-talk genes
            identifies association between risk of serous ovarian cancer and
            TERT, a cancer susceptibility 'hot-spot'
  JOURNAL   PLoS Genet 6 (7), e1001016 (2010)
   PUBMED   20628624
  REMARK    GeneRIF: Meta-analysis of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Lu,J., O'Hara,E.B., Trieselmann,B.A., Romano,P.R. and Dever,T.E.
  TITLE     The interferon-induced double-stranded RNA-activated protein kinase
            PKR will phosphorylate serine, threonine, or tyrosine at residue 51
            in eukaryotic initiation factor 2alpha
  JOURNAL   J Biol Chem 274 (45), 32198-32203 (1999)
   PUBMED   10542257
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Shi,Y., Vattem,K.M., Sood,R., An,J., Liang,J., Stramm,L. and
            Wek,R.C.
  TITLE     Identification and characterization of pancreatic eukaryotic
            initiation factor 2 alpha-subunit kinase, PEK, involved in
            translational control
  JOURNAL   Mol Cell Biol 18 (12), 7499-7509 (1998)
   PUBMED   9819435
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Gale,M. Jr., Blakely,C.M., Hopkins,D.A., Melville,M.W., Wambach,M.,
            Romano,P.R. and Katze,M.G.
  TITLE     Regulation of interferon-induced protein kinase PKR: modulation of
            P58IPK inhibitory function by a novel protein, P52rIPK
  JOURNAL   Mol Cell Biol 18 (2), 859-871 (1998)
   PUBMED   9447982
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Polyak,S.J., Tang,N., Wambach,M., Barber,G.N. and Katze,M.G.
  TITLE     The P58 cellular inhibitor complexes with the interferon-induced,
            double-stranded RNA-dependent protein kinase, PKR, to regulate its
            autophosphorylation and activity
  JOURNAL   J Biol Chem 271 (3), 1702-1707 (1996)
   PUBMED   8576172
REFERENCE   10 (residues 1 to 761)
  AUTHORS   Mellor,H. and Proud,C.G.
  TITLE     A synthetic peptide substrate for initiation factor-2 kinases
  JOURNAL   Biochem Biophys Res Commun 178 (2), 430-437 (1991)
   PUBMED   1677563
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP002360.4, DR005363.1, AF081567.1 and AA765102.1.
            
            On Apr 4, 2002 this sequence version replaced NP_004696.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110304.1, SRR1803613.154733.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2142348,
                                           SAMEA2146411 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260045.8/ ENSP00000260045.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5"
     Protein         1..761
                     /product="52 kDa repressor of the inhibitor of the protein
                     kinase"
                     /note="death-associated protein 4; inhibitor of protein
                     kinase PKR; P58IPK-regulatory protein; p58IPK-interacting
                     protein; THAP domain-containing protein 0; 58 kDa
                     interferon-induced protein kinase-interacting protein;
                     protein-kinase, interferon-inducible double stranded RNA
                     dependent inhibitor, repressor of (P58 repressor);
                     testicular tissue protein Li 133; THAP domain-containing
                     protein 12"
                     /calculated_mol_wt=87573
     Region          5..86
                     /region_name="THAP"
                     /note="THAP domain; pfam05485"
                     /db_xref="CDD:461662"
     Region          116..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43422.2)"
     Region          <157..330
                     /region_name="DUF4371"
                     /note="Domain of unknown function (DUF4371); cl46273"
                     /db_xref="CDD:480613"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43422.2)"
     Region          <672..729
                     /region_name="Dimer_Tnp_hAT"
                     /note="hAT family C-terminal dimerization region;
                     pfam05699"
                     /db_xref="CDD:399013"
     CDS             1..761
                     /gene="THAP12"
                     /gene_synonym="DAP4; P52rIPK; PRKRIR; THAP0"
                     /coded_by="NM_004705.4:297..2582"
                     /db_xref="CCDS:CCDS8243.1"
                     /db_xref="GeneID:5612"
                     /db_xref="HGNC:HGNC:9440"
                     /db_xref="MIM:607374"
ORIGIN      
        1 mpnfcaapnc trkstqsdla ffrfprdpar cqkwvencrr adledktpdq lnkhyrlcak
       61 hfetsmicrt spyrtvlrdn aiptifdlts hlnnphsrhr krikelsede irtlkqkkid
      121 etseqeqkhk etnnsnaqnp seeegegqde dilpltleek enkeylkslf eililmgkqn
      181 ipldgheade ipeglftpdn fqallecrin sgeevlrkrf ettavntlfc sktqqrqmle
      241 icescireet lrevrdshff siitddvvdi ageehlpvlv rfvdeshnlr eefigflpye
      301 adaeilavkf htmitekwgl nmeycrgqay ivssgfsskm kvvasrllek ypqaiytlcs
      361 scalnmwlak svpvmgvsva lgtieevcsf fhrspqllle ldnvisvlfq nskergkelk
      421 eichsqwtgr hdafeilvel lqalvlcldg insdtnirwn nyiagrafvl csavsdfdfi
      481 vtivvlknvl sftrafgknl qgqtsdvffa agsltavlhs lnevmeniev yhefwfeeat
      541 nlatkldiqm klpgkfrrah qgnlesqlts esyyketlsv ptvehiiqel kdifseqhlk
      601 alkclslvps vmgqlkfnts eehhadmyrs dlpnpdtlsa elhcwrikwk hrgkdielps
      661 tiyealhlpd ikffpnvyal lkvlcilpvm kveneryeng rkrlkaylrn tltdqrssnl
      721 allninfdik hdldlmvdty iklytsksel ptdnsetven t
//
LOCUS       NP_001351364             684 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial inner membrane m-AAA protease component paraplegin
            isoform 2 precursor [Mus musculus].
ACCESSION   NP_001351364
VERSION     NP_001351364.1
DBSOURCE    REFSEQ: accession NM_001364435.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Montoro-Gamez,C., Nolte,H., Molinie,T., Evangelista,G.,
            Troder,S.E., Barth,E., Popovic,M., Trifunovic,A., Zevnik,B.,
            Langer,T. and Rugarli,E.I.
  TITLE     SARM1 deletion delays cerebellar but not spinal cord degeneration
            in an enhanced mouse model of SPG7 deficiency
  JOURNAL   Brain 146 (10), 4117-4131 (2023)
   PUBMED   37086482
  REMARK    GeneRIF: SARM1 deletion delays cerebellar but not spinal cord
            degeneration in an enhanced mouse model of SPG7 deficiency.
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Sambri,I., Massa,F., Gullo,F., Meneghini,S., Cassina,L.,
            Carraro,M., Dina,G., Quattrini,A., Patanella,L., Carissimo,A.,
            Iuliano,A., Santorelli,F., Codazzi,F., Grohovaz,F., Bernardi,P.,
            Becchetti,A. and Casari,G.
  TITLE     Impaired flickering of the permeability transition pore causes SPG7
            spastic paraplegia
  JOURNAL   EBioMedicine 61, 103050 (2020)
   PUBMED   33045469
  REMARK    GeneRIF: Impaired flickering of the permeability transition pore
            causes SPG7 spastic paraplegia.
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Schatton,D., Pla-Martin,D., Marx,M.C., Hansen,H., Mourier,A.,
            Nemazanyy,I., Pessia,A., Zentis,P., Corona,T., Kondylis,V.,
            Barth,E., Schauss,A.C., Velagapudi,V. and Rugarli,E.I.
  TITLE     CLUH regulates mitochondrial metabolism by controlling translation
            and decay of target mRNAs
  JOURNAL   J Cell Biol 216 (3), 675-693 (2017)
   PUBMED   28188211
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Mancuso,G., Barth,E., Crivello,P. and Rugarli,E.I.
  TITLE     Alternative splicing of Spg7, a gene involved in hereditary spastic
            paraplegia, encodes a variant of paraplegin targeted to the
            endoplasmic reticulum
  JOURNAL   PLoS One 7 (5), e36337 (2012)
   PUBMED   22563492
  REMARK    GeneRIF: Studies indicate that both mouse and human SPG7 ESTs
            containing alternative first exons.
REFERENCE   5  (residues 1 to 684)
  AUTHORS   Koppen,M., Bonn,F., Ehses,S. and Langer,T.
  TITLE     Autocatalytic processing of m-AAA protease subunits in mitochondria
  JOURNAL   Mol Biol Cell 20 (19), 4216-4224 (2009)
   PUBMED   19656850
  REMARK    GeneRIF: Data show that Afg3l1 or Afg3l2 are required for
            maturation of newly imported paraplegin subunits after their
            cleavage by MPP.
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Pirozzi,M., Quattrini,A., Andolfi,G., Dina,G., Malaguti,M.C.,
            Auricchio,A. and Rugarli,E.I.
  TITLE     Intramuscular viral delivery of paraplegin rescues peripheral
            axonopathy in a model of hereditary spastic paraplegia
  JOURNAL   J Clin Invest 116 (1), 202-208 (2006)
   PUBMED   16357941
  REMARK    Erratum:[J Clin Invest. 2014 Feb;124(2):871]
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Nolden,M., Ehses,S., Koppen,M., Bernacchia,A., Rugarli,E.I. and
            Langer,T.
  TITLE     The m-AAA protease defective in hereditary spastic paraplegia
            controls ribosome assembly in mitochondria
  JOURNAL   Cell 123 (2), 277-289 (2005)
   PUBMED   16239145
REFERENCE   8  (residues 1 to 684)
  AUTHORS   Nishimura,M., Yokoi,N., Miki,T., Horikawa,Y., Yoshioka,H.,
            Takeda,J., Ohara,O. and Seino,S.
  TITLE     Construction of a multi-functional cDNA library specific for mouse
            pancreatic islets and its application to microarray
  JOURNAL   DNA Res 11 (5), 315-323 (2004)
   PUBMED   15747579
REFERENCE   9  (residues 1 to 684)
  AUTHORS   Ferreirinha,F., Quattrini,A., Pirozzi,M., Valsecchi,V., Dina,G.,
            Broccoli,V., Auricchio,A., Piemonte,F., Tozzi,G., Gaeta,L.,
            Casari,G., Ballabio,A. and Rugarli,E.I.
  TITLE     Axonal degeneration in paraplegin-deficient mice is associated with
            abnormal mitochondria and impairment of axonal transport
  JOURNAL   J Clin Invest 113 (2), 231-242 (2004)
   PUBMED   14722615
REFERENCE   10 (residues 1 to 684)
  AUTHORS   Molla,A., Rouard-Talbot,L. and Block,M.R.
  TITLE     Cotranscription of two RNA coding for the cell adhesion regulator
            and its variant in Reh leukemia cells
  JOURNAL   Biochim Biophys Acta 1315 (1), 6-8 (1996)
   PUBMED   8611648
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC121819.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.335407.1,
                                           SRR11927935.2883692.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 72.04 cM"
     Protein         1..684
                     /product="mitochondrial inner membrane m-AAA protease
                     component paraplegin isoform 2 precursor"
                     /note="paraplegin; cell matrix adhesion regulator; spastic
                     paraplegia 7 protein; spastic paraplegia 7 homolog;
                     mitochondrial inner membrane m-AAA protease component
                     paraplegin"
                     /calculated_mol_wt=70168
     transit_peptide 1..43
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:19656850; propagated from
                     UniProtKB/Swiss-Prot (Q3ULF4.1)"
                     /calculated_mol_wt=4551
     Region          22..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ULF4.1)"
     Region          103..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ULF4.1)"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ULF4.1)"
     Region          147..646
                     /region_name="HflB"
                     /note="ATP-dependent Zn proteases [Posttranslational
                     modification, protein turnover, chaperones]; COG0465"
                     /db_xref="CDD:440233"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ULF4.1)"
     CDS             1..684
                     /gene="Spg7"
                     /gene_synonym="Cmar; PGN"
                     /coded_by="NM_001364435.1:20..2074"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:234847"
                     /db_xref="MGI:MGI:2385906"
ORIGIN      
        1 maaallllrg lrpgpeprpr rlwgllsgrg pglssgagar rpyaargtpv gpaaagghap
       61 qslllriltp sfegisglll kqhivpnavr lwplsgstly fntsrmkqkn kdndkpkgkt
      121 peddeeekrr keredqmyre rlrtlfiial vmsllnslst sggsiswadf vnemlakgev
      181 qrvqvvpesd vvevylhpga vvfgrprlal myrmqvanid kfeeklraae delnieskdr
      241 ipvsykrtgf fgnalyalgm tavglailwy vfrlagmtgr eggfsafnql kmarftivdg
      301 ktgkgvsfqd vagmheakle vrefvdylks perflqlgak vpkgalllgp pgcgktllak
      361 avateaqvpf lamagpefve vigglgaarv rslfkearar apcivyidei davgkkrsts
      421 msgfsnteee qtlnqllvem dgmgttdhvi vlastnradv ldnalmrpgr ldrhvfidlp
      481 tlqerreife qhlkglkltq pssfysqrla eltpgfsgad ianicneaal haareghtsv
      541 htfnfeyave rviagtakks kilskeeqrv vafhesghal vgwllehtea vmkvsiaprt
      601 naalgfsqml prdqylftke qlfermcmal ggraaeaisf srvtsgskaa ggqslqthre
      661 gaarqpgqaa gvgecpsgkg sdkl
//
LOCUS       NP_083152                229 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane emp24 domain-containing protein 5 isoform 1 precursor
            [Mus musculus].
ACCESSION   NP_083152 NP_082721 XP_915835
VERSION     NP_083152.1
DBSOURCE    REFSEQ: accession NM_028876.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Nagae,M., Liebschner,D., Yamada,Y., Morita-Matsumoto,K.,
            Matsugaki,N., Senda,T., Fujita,M., Kinoshita,T. and Yamaguchi,Y.
  TITLE     Crystallographic analysis of murine p24gamma2 Golgi dynamics domain
  JOURNAL   Proteins 85 (4), 764-770 (2017)
   PUBMED   28066915
  REMARK    GeneRIF: Crystallographic analysis of murine p24gamma2 Golgi
            dynamics domain has been reported.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC159996.7, AK014490.1, BB764499.1 and BB376243.1.
            
            On or before Dec 7, 2005 this sequence version replaced
            XP_915835.1, NP_082721.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK014490.1, AK033463.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 52.49 cM"
     Protein         1..229
                     /product="transmembrane emp24 domain-containing protein 5
                     isoform 1 precursor"
                     /note="transmembrane emp24 domain-containing protein 5;
                     p24 family protein gamma-2; transmembrane emp24 protein
                     transport domain containing 5"
                     /calculated_mol_wt=23411
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2779
     mat_peptide     28..229
                     /product="Transmembrane emp24 domain-containing protein 5.
                     /id=PRO_0000010390"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CXE7.1)"
                     /calculated_mol_wt=23411
     Region          35..222
                     /region_name="EMP24_GP25L"
                     /note="emp24/gp25L/p24 family/GOLD; pfam01105"
                     /db_xref="CDD:426051"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CXE7.1)"
     CDS             1..229
                     /gene="Tmed5"
                     /gene_synonym="3110020O18Rik; 4432412D15Rik; p24gamma2"
                     /coded_by="NM_028876.3:197..886"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS19508.1"
                     /db_xref="GeneID:73130"
                     /db_xref="MGI:MGI:1921586"
ORIGIN      
        1 mggrmwlpfp vlllsalpaa llrgaagftp sldsdftftl pagrkecfyq pmplkaslei
       61 eyqvldggel didfhltspe grtlvfeqrk sdgvhtiete dgdymfcfdn tfstisekvi
      121 ffelildnmg eevqgqedwk kyitntdvle mkledilesi nsiksrlsks ghiqtllraf
      181 eardrniqes nfdrvnfwsv vnlmvmvvvs aiqvytlksl fedkrksrt
//
LOCUS       NP_775099               2595 aa            linear   PRI 27-APR-2025
DEFINITION  glucosylceramide transporter ABCA12 isoform a [Homo sapiens].
ACCESSION   NP_775099
VERSION     NP_775099.2
DBSOURCE    REFSEQ: accession NM_173076.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2595)
  AUTHORS   Noda,T., Takeichi,T., Tanahashi,K., Ogawa,Y., Takeuchi,S.,
            Yoshikawa,T., Toriyama,E., Ashida,M., Imakado,S., Tsuchihashi,H.,
            Okamoto,T., Okuno,Y., Ogi,T., Sugiura,K., Kubo,A., Muro,Y.,
            Suga,Y., Ishida-Yamamoto,A. and Akiyama,M.
  TITLE     Updated mutational spectrum and genotype-phenotype correlations in
            ichthyosis patients with ABCA12 pathogenic variants
  JOURNAL   Exp Dermatol 33 (4), e15072 (2024)
   PUBMED   38576105
  REMARK    GeneRIF: Updated mutational spectrum and genotype-phenotype
            correlations in ichthyosis patients with ABCA12 pathogenic
            variants.
REFERENCE   2  (residues 1 to 2595)
  AUTHORS   Hotz,A., Folster-Holst,R., Oji,V., Bourrat,E., Frank,J.,
            Marrakchi,S., Ennouri,M., Wankner,L., Komlosi,K., Alter,S. and
            Fischer,J.
  TITLE     Erythrokeratodermia Variabilis-like Phenotype in Patients Carrying
            ABCA12 Mutations
  JOURNAL   Genes (Basel) 15 (3), 288 (2024)
   PUBMED   38540347
  REMARK    GeneRIF: Erythrokeratodermia Variabilis-like Phenotype in Patients
            Carrying ABCA12 Mutations.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2595)
  AUTHORS   Liu,Y., Mo,R., Chen,Z. and Yang,Y.
  TITLE     Novel variants in ABCA12 cause erythrokeratodermia variabilis
  JOURNAL   Br J Dermatol 190 (3), 454 (2024)
   PUBMED   38085035
  REMARK    GeneRIF: Novel variants in ABCA12 cause erythrokeratodermia
            variabilis.
REFERENCE   4  (residues 1 to 2595)
  AUTHORS   Takeichi,T., Hamada,T., Yamamoto,M., Ito,Y., Kawaguchi,A.,
            Kobashi,H., Yoshikawa,T., Koga,H., Ishii,N., Nakama,T., Muro,Y.,
            Ogi,T. and Akiyama,M.
  TITLE     Patients with keratinization disorders due to ABCA12 variants
            showing pityriasis rubra pilaris phenotypes
  JOURNAL   J Dermatol 51 (1), 101-105 (2024)
   PUBMED   37752865
  REMARK    GeneRIF: Patients with keratinization disorders due to ABCA12
            variants showing pityriasis rubra pilaris phenotypes.
REFERENCE   5  (residues 1 to 2595)
  AUTHORS   Terrinoni,A., Sala,G., Bruno,E., Pitolli,C., Minieri,M., Pieri,M.,
            Gambacurta,A., Campione,E., Belardi,R. and Bernardini,S.
  TITLE     Partial Loss of Function ABCA12 Mutations Generate Reduced
            Deposition of Glucosyl-Ceramide, Leading to Patchy Ichthyosis and
            Erythrodermia Resembling Erythrokeratodermia Variabilis et
            Progressiva (EKVP)
  JOURNAL   Int J Mol Sci 24 (18), 13962 (2023)
   PUBMED   37762265
  REMARK    GeneRIF: Partial Loss of Function ABCA12 Mutations Generate Reduced
            Deposition of Glucosyl-Ceramide, Leading to Patchy Ichthyosis and
            Erythrodermia Resembling Erythrokeratodermia Variabilis et
            Progressiva (EKVP).
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2595)
  AUTHORS   Dean,M., Rzhetsky,A. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Genome Res 11 (7), 1156-1166 (2001)
   PUBMED   11435397
  REMARK    Review article
REFERENCE   7  (residues 1 to 2595)
  AUTHORS   Parmentier,L., Clepet,C., Boughdene-Stambouli,O., Lakhdar,H.,
            Blanchet-Bardon,C., Dubertret,L., Wunderle,E., Pulcini,F.,
            Fizames,C. and Weissenbach,J.
  TITLE     Lamellar ichthyosis: further narrowing, physical and expression
            mapping of the chromosome 2 candidate locus
  JOURNAL   Eur J Hum Genet 7 (1), 77-87 (1999)
   PUBMED   10094194
REFERENCE   8  (residues 1 to 2595)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
REFERENCE   9  (residues 1 to 2595)
  AUTHORS   Parmentier,L., Lakhdar,H., Blanchet-Bardon,C., Marchand,S.,
            Dubertret,L. and Weissenbach,J.
  TITLE     Mapping of a second locus for lamellar ichthyosis to chromosome
            2q33-35
  JOURNAL   Hum Mol Genet 5 (4), 555-559 (1996)
   PUBMED   8845852
  REMARK    Erratum:[Hum Mol Genet 1996 Jun;5(6):862-3]
REFERENCE   10 (residues 1 to 2595)
  AUTHORS   Richard,G.
  TITLE     Autosomal Recessive Congenital Ichthyosis
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301593
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC072062.3, AY219711.1,
            BC144073.1, AF418105.1, AK123578.1 and AK096597.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 16, 2003 this sequence version replaced NP_775099.1.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intracellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            and White). This encoded protein is a member of the ABC1 subfamily,
            which is the only major ABC subfamily found exclusively in
            multicellular eukaryotes. Alternative splicing of this gene results
            in multiple transcript variants. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY219711.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000272895.12/ ENSP00000272895.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2595
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..2595
                     /product="glucosylceramide transporter ABCA12 isoform a"
                     /EC_number="7.6.2.1"
                     /note="ATP-binding cassette transporter 12; ATP-binding
                     cassette, sub-family A (ABC1), member 12; glucosylceramide
                     transporter ABCA12"
                     /calculated_mol_wt=293107
     Region          7..>86
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            23..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            367
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            383
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            412
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            435
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            528
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            543
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            577
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            608
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            623
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            648
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Region          752..2576
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            752
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            826
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            920
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            963
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1065..1085
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1112..1132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1145..1165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1170
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1174..1194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1200..1220
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1250..1270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1524
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1663
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1704
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1747..1767
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1769
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1819
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1835
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1876
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1921
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1952
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            1979..1999
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2035..2055
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2072..2092
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2103..2123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2187..2207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2208
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2270..2290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2542
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Site            2547
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UK0.3)"
     Region          2571..2595
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UK0.3)"
     CDS             1..2595
                     /gene="ABCA12"
                     /gene_synonym="ARCI4A; ARCI4B; ICR2B; LI2"
                     /coded_by="NM_173076.3:419..8206"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33372.1"
                     /db_xref="GeneID:26154"
                     /db_xref="HGNC:HGNC:14637"
                     /db_xref="MIM:607800"
ORIGIN      
        1 maslfhqlqi lvwknwlgvk rqplwtlvli lwpviifiil aitrtkfppt akptcylapr
       61 nlpstgffpf lqtllcdtds kckdtpygpq dllrrkgidd alfkdseilr kssnldkdss
      121 lsfqstqvpe rrhaslatvf pspssdleip gtytfngsqv larilglekl lkqnstsedi
      181 rrelcdsysg yivddafswt flgrnvfnkf clsnmtlles slqelnkqfs qlssdpnnqk
      241 ivfqeivrml sffsqvqeqk avwqllssfp nvfqndtsls nlfdvlrkan svllvvqkvy
      301 prfatnegfr tlqksvkhll ytldspaqgd sdnithvwne ddgqtlspss laaqllilen
      361 fedallnisa nspyipylac vrnvtdslar gspenlrllq stirfkksfl rngsyedyfp
      421 pvpevlkskl sqlrnltell cesetfslie kscqlsdmsf gslceesefd lqlleaaelg
      481 teiaasllyh dnviskkvrd lltgdpskin lnmdqfleqa lqmnylenit qlipiieaml
      541 hvnnsadase kpgqllemfk nveelkedlr rttgmsnrti dkllaipipd nraeiisqvf
      601 wlhscdtnit tpkledamke fcnlslsers rqsyligltl lhylniynft ykvffprkdq
      661 kpvekmmelf irlkeilnqm asgthplldk mrslkqmhlp rsvpltqamy rsnrmntpqg
      721 sfstisqalc sqgitteylt amlpssqrpk gnhtkdflty kltkeqiask ygipinstpf
      781 cfslykdiin mpagpviwaf lkpmllgril yapynpvtka imeksnvtlr qlaelreksq
      841 ewmdksplfm nsfhllnqai pmlqntlrnp fvqvfvkfsv gldavellkq ideldilrlk
      901 lennidiidq lntlssltvn isscvlydri qaaktideme reakrlyksn elfgsvifkl
      961 psnrswhrgy dsgnvflppv ikytirmslk taqttrslrt kiwapgphns pshnqiygra
     1021 fiylqdsier aiielqtgrn sqeiavqvqa ipypcfmkdn fltsvsyslp ivlmvawvvf
     1081 iaafvkklvy ekdlrlheym kmmgvnscsh ffawliesvg fllvtivili iilkfgnilp
     1141 ktngfilfly fsdysfsvia msylisvffn ntniaaligs liyiiaffpf ivlvtvenel
     1201 syvlkvfmsl lsptafsyas qyiaryeeqg iglqwenmyt spvqddttsf gwlcclilad
     1261 sfiyfliawy vrnvfpgtyg maapwyfpil psywkerfgc aevkpeksng lmftnimmqn
     1321 tnpsaspeym fssniepepk dltvgvalhg vtkiygskva vdnlnlnfye ghitsllgpn
     1381 gagktttism ltglfgasag tifvygkdik tdlhtvrknm gvcmqhdvlf sylttkehll
     1441 lygsikvphw tkkqlheevk rtlkdtglys hrhkrvgtls ggmkrklsis ialiggsrvv
     1501 ildepstgvd pcsrrsiwdv isknktarti ilsthhldea evlsdriafl eqgglrccgs
     1561 pfylkeafgd gyhltltkkk spnlnanavc dtmavtamiq shlpeaylke diggelvyvl
     1621 ppfstkvsga ylsllraldn gmgdlnigcy gisdttveev flnltkesqk nsamslehlt
     1681 qkkignsnan gistpddlsv sssnftdrdd kiltrgerld gfglllkkim ailikrfhht
     1741 rrnwkgliaq vilpivfvtt amglgtlrns snsypeiqis pslygtseqt afyanyhpst
     1801 ealvsamwdf pgidnmclnt sdlqclnkds lekwntsgep itnfgvcscs envqecpkfn
     1861 yspphrrtys sqviynltgq rvenylista nefvqkrygg wsfglpltkd lrfditgvpa
     1921 nrtlakvwyd pegyhslpay lnslnnfllr vnmskydaar hgiimyshpy pgvqdqeqat
     1981 isslidilva lsilmgysvt tasfvtyvvr ehqtkakqlq hisgigvtcy wvtnfiydmv
     2041 fylvpvafsi giiaifklpa fysennlgav slllllfgya tfswmyllag lfhetgmafi
     2101 tyvcvnlffg insivslsvv yflskekpnd ptlelisetl kriflifpqf cfgygliels
     2161 qqqsvldflk aygveypnet femnklgamf valvsqgtmf fslrllines likklrlffr
     2221 kfnsshvret idededvrae rlrvesgaae fdlvqlyclt ktyqlihkki iavnnisigi
     2281 pagecfgllg vngagkttif kmltgdiips sgnilirnkt gslghvdshs slvgycpqed
     2341 alddlvtvee hlyfyarvhg ipekdiketv hkllrrlhlm pfkdratsmc sygtkrklst
     2401 alaligkpsi llldepssgm dpkskrhlwk iiseevqnkc sviltshsme ecealctrla
     2461 imvngkfqci gslqhiksrf grgftvkvhl knnkvtmetl tkfmqlhfpk tylkdqhlsm
     2521 leyhvpvtag gvanifdlle tnktalnitn flvsqttlee vfinfakdqk syetadtssq
     2581 gstisvdsqd dqmes
//
LOCUS       NP_060666                421 aa            linear   PRI 27-APR-2025
DEFINITION  trimethyllysine dioxygenase, mitochondrial isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_060666 XP_943796
VERSION     NP_060666.1
DBSOURCE    REFSEQ: accession NM_018196.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Wang,Y., Reddy,Y.V., Al Temimi,A.H.K., Venselaar,H.,
            Nelissen,F.H.T., Lenstra,D.C. and Mecinovic,J.
  TITLE     Investigating the active site of human trimethyllysine hydroxylase
  JOURNAL   Biochem J 476 (7), 1109-1119 (2019)
   PUBMED   30898847
  REMARK    GeneRIF: This work demonstrates the importance of the recognition
            sites that contribute to the enzymatic activity of TMLH: the
            Fe(II)-binding H242-D244-H389 residues, R391-R398 involved in 2OG
            binding and several residues (D231, N334 and the aromatic cage
            comprised of W221, Y217 and Y234) associated with binding of (2S)-N
            (epsilon)-trimethyllysine.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Chen,C., Xie,X., Wu,X., Lu,Y., Wang,X., Wu,W., Hu,Y. and Ding,Q.
  TITLE     Complex recombination with deletion in the F8 and duplication in
            the TMLHE mediated by int22h copies during early embryogenesis
  JOURNAL   Thromb Haemost 117 (8), 1478-1485 (2017)
   PUBMED   28492696
  REMARK    GeneRIF: Case Report: complex recombination with deletion in the F8
            and duplication in the TMLHE mediated by int22h copies during early
            embryogenesis in proband's mother.
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Floyd,B.J., Wilkerson,E.M., Veling,M.T., Minogue,C.E., Xia,C.,
            Beebe,E.T., Wrobel,R.L., Cho,H., Kremer,L.S., Alston,C.L.,
            Gromek,K.A., Dolan,B.K., Ulbrich,A., Stefely,J.A., Bohl,S.L.,
            Werner,K.M., Jochem,A., Westphall,M.S., Rensvold,J.W., Taylor,R.W.,
            Prokisch,H., Kim,J.P., Coon,J.J. and Pagliarini,D.J.
  TITLE     Mitochondrial Protein Interaction Mapping Identifies Regulators of
            Respiratory Chain Function
  JOURNAL   Mol Cell 63 (4), 621-632 (2016)
   PUBMED   27499296
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Nava,C., Lamari,F., Heron,D., Mignot,C., Rastetter,A., Keren,B.,
            Cohen,D., Faudet,A., Bouteiller,D., Gilleron,M., Jacquette,A.,
            Whalen,S., Afenjar,A., Perisse,D., Laurent,C., Dupuits,C.,
            Gautier,C., Gerard,M., Huguet,G., Caillet,S., Leheup,B.,
            Leboyer,M., Gillberg,C., Delorme,R., Bourgeron,T., Brice,A. and
            Depienne,C.
  TITLE     Analysis of the chromosome X exome in patients with autism spectrum
            disorders identified novel candidate genes, including TMLHE
  JOURNAL   Transl Psychiatry 2 (10), e179 (2012)
   PUBMED   23092983
  REMARK    GeneRIF: Study found 3 mutations in TMLHE to be associated with
            autism spectrum disorder, c.229C>T/p.Arg77X, c.730G>C/p.Asp244His,
            and c.1107G>T/p.Glu369Asp.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Celestino-Soper,P.B., Shaw,C.A., Sanders,S.J., Li,J., Murtha,M.T.,
            Ercan-Sencicek,A.G., Davis,L., Thomson,S., Gambin,T.,
            Chinault,A.C., Ou,Z., German,J.R., Milosavljevic,A.,
            Sutcliffe,J.S., Cook,E.H. Jr., Stankiewicz,P., State,M.W. and
            Beaudet,A.L.
  TITLE     Use of array CGH to detect exonic copy number variants throughout
            the genome in autism families detects a novel deletion in TMLHE
  JOURNAL   Hum Mol Genet 20 (22), 4360-4370 (2011)
   PUBMED   21865298
  REMARK    GeneRIF: Use of array CGH to detect exonic copy number variants
            throughout the genome in autism families detects a novel deletion
            in TMLHE.
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Monfregola,J., Napolitano,G., Conte,I., Cevenini,A., Migliaccio,C.,
            D'Urso,M. and Ursini,M.V.
  TITLE     Functional characterization of the TMLH gene: promoter analysis, in
            situ hybridization, identification and mapping of alternative
            splicing variants
  JOURNAL   Gene 395 (1-2), 86-97 (2007)
   PUBMED   17408883
  REMARK    GeneRIF: By 5' and 3' RACE, we identified and mapped two
            alternative 5' TMLH first exons and seven alternative 3'-splice
            variants.
REFERENCE   8  (residues 1 to 421)
  AUTHORS   Monfregola,J., Cevenini,A., Terracciano,A., van Vlies,N.,
            Arbucci,S., Wanders,R.J., D'Urso,M., Vaz,F.M. and Ursini,M.V.
  TITLE     Functional analysis of TMLH variants and definition of domains
            required for catalytic activity and mitochondrial targeting
  JOURNAL   J Cell Physiol 204 (3), 839-847 (2005)
   PUBMED   15754339
  REMARK    GeneRIF: C-terminal region of trimethyllysine hydroxylase, epsilon
            contains the main determinants for its enzymatic activity including
            a key H389 residue
REFERENCE   9  (residues 1 to 421)
  AUTHORS   Vaz,F.M., Ofman,R., Westinga,K., Back,J.W. and Wanders,R.J.
  TITLE     Molecular and Biochemical Characterization of Rat epsilon
            -N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine
            Biosynthesis
  JOURNAL   J Biol Chem 276 (36), 33512-33517 (2001)
   PUBMED   11431483
REFERENCE   10 (residues 1 to 421)
  AUTHORS   Rogner,U.C., Heiss,N.S., Kioschis,P., Wiemann,S., Korn,B. and
            Poustka,A.
  TITLE     Transcriptional analysis of the candidate region for incontinentia
            pigmenti (IP2) in Xq28
  JOURNAL   Genome Res 6 (10), 922-934 (1996)
   PUBMED   8908511
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB174485.1, AK001589.1 and
            BX571846.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_943796.1.
            
            Summary: This gene encodes the protein trimethyllysine dioxygenase
            which is the first enzyme in the carnitine biosynthesis pathway.
            Carnitine play an essential role in the transport of activated
            fatty acids across the inner mitochondrial membrane. The encoded
            protein converts trimethyllysine into hydroxytrimethyllysine. A
            pseudogene of this gene is found on chromosome X. Alternate
            splicing results in multiple transcript variants.[provided by
            RefSeq, May 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.2538.1, SRR1803611.712.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000334398.8/
                                                  ENSP00000335261.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..421
                     /product="trimethyllysine dioxygenase, mitochondrial
                     isoform 1 precursor"
                     /EC_number="1.14.11.8"
                     /note="butyrobetaine (gamma), 2-oxoglutarate dioxygenase
                     (gamma-butyrobetaine hydroxylase) 2; trimethyllysine
                     dioxygenase, mitochondrial; TML hydroxylase;
                     TML-alpha-ketoglutarate dioxygenase;
                     epsilon-trimethyllysine 2-oxoglutarate dioxygenase;
                     epsilon-trimethyllysine hydroxylase"
                     /calculated_mol_wt=47557
     transit_peptide 1..15
                     /calculated_mol_wt=1979
     mat_peptide     16..421
                     /product="trimethyllysine dioxygenase, mitochondrial
                     isoform 1"
                     /calculated_mol_wt=47557
     Region          70..419
                     /region_name="carnitine_TMLD"
                     /note="trimethyllysine dioxygenase; TIGR02410"
                     /db_xref="CDD:274119"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q91ZE0; propagated from
                     UniProtKB/Swiss-Prot (Q9NVH6.1)"
     Site            order(211..212,245,247,252,302,402,404)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238154"
     Site            236
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NVH6.1)"
     Site            order(242,244,269,389,398)
                     /site_type="active"
                     /db_xref="CDD:238154"
     Site            order(242,244,389)
                     /site_type="other"
                     /note="iron coordination sites [ion binding]"
                     /db_xref="CDD:238154"
     CDS             1..421
                     /gene="TMLHE"
                     /gene_synonym="AUTSX6; BBOX2; TMLD; TMLH; TMLHED; XAP130"
                     /coded_by="NM_018196.4:163..1428"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS14768.1"
                     /db_xref="GeneID:55217"
                     /db_xref="HGNC:HGNC:18308"
                     /db_xref="MIM:300777"
ORIGIN      
        1 mwyhrlshlh srlqdllkgg viypalpqpn fksllplavh whhtaskslt cawqqhedhf
       61 elkyantvmr fdyvwlrdhc rsascynskt hqrsldtasv dlcikpktir ldettlfftw
      121 pdghvtkydl nwlvknsyeg qkqkviqpri lwnaeiyqqa qvpsvdcqsf letneglkkf
      181 lqnfllygia fvenvpptqe hteklaeris liretiygrm wyftsdfsrg dtaytklald
      241 rhtdttyfqe pcgiqvfhcl khegtggrtl lvdgfyaaeq vlqkapeefe llskvplkhe
      301 yiedvgechn hmigigpvln iypwnkelyl irynnydrav intvpydvvh rwytahrtlt
      361 ielrrpenef wvklkpgrvl fidnwrvlhg recftgyrql cgcyltrddv lntarllglq
      421 a
//
LOCUS       NP_000034                335 aa            linear   PRI 27-APR-2025
DEFINITION  tumor necrosis factor receptor superfamily member 6 isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_000034
VERSION     NP_000034.1
DBSOURCE    REFSEQ: accession NM_000043.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Bartels,N., van der Voort,N.T.M., Opanasyuk,O., Felekyan,S.,
            Greife,A., Shang,X., Bister,A., Wiek,C., Seidel,C.A.M. and
            Monzel,C.
  TITLE     Advanced multiparametric image spectroscopy and super-resolution
            microscopy reveal a minimal model of CD95 signal initiation
  JOURNAL   Sci Adv 10 (35), eadn3238 (2024)
   PUBMED   39213362
  REMARK    GeneRIF: Advanced multiparametric image spectroscopy and
            super-resolution microscopy reveal a minimal model of CD95 signal
            initiation.
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Liu,Y., Sardana,R., Nemirovsky,D., Frosina,D., Jungbluth,A.,
            Johnson,W.T., Vardhana,S., Arcila,M., Horwitz,S.M., Derkach,A.,
            Dogan,A. and Xiao,W.
  TITLE     Somatic mutations in FAS pathway increase hemophagocytic
            lymphohistiocytosis risk in patients with T- and/or NK-cell
            lymphoma
  JOURNAL   Blood Adv 8 (12), 3064-3075 (2024)
   PUBMED   38593227
  REMARK    GeneRIF: Somatic mutations in FAS pathway increase hemophagocytic
            lymphohistiocytosis risk in patients with T- and/or NK-cell
            lymphoma.
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Yang,Z., Zhang,X., Zhang,X., Liu,Y., Zhang,J. and Yuan,X.
  TITLE     [Porphyromonas gingivalis infection facilitates immune escape of
            esophageal cancer by enhancing YTHDF2-mediated Fas degradation]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 44 (6), 1159-1165 (2024)
   PUBMED   38977346
  REMARK    GeneRIF: [Porphyromonas gingivalis infection facilitates immune
            escape of esophageal cancer by enhancing YTHDF2-mediated Fas
            degradation].
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Staniek,J., Kalina,T., Andrieux,G., Boerries,M., Janowska,I.,
            Fuentes,M., Diez,P., Bakardjieva,M., Stancikova,J., Raabe,J.,
            Neumann,J., Schwenk,S., Arpesella,L., Stuchly,J., Benes,V., Garcia
            Valiente,R., Fernandez Garcia,J., Carsetti,R., Piano Mortari,E.,
            Catala,A., de la Calle,O., Sogkas,G., Neven,B., Rieux-Laucat,F.,
            Magerus,A., Neth,O., Olbrich,P., Voll,R.E., Alsina,L.,
            Allende,L.M., Gonzalez-Granado,L.I., Bohler,C., Thiel,J.,
            Venhoff,N., Lorenzetti,R., Warnatz,K., Unger,S., Seidl,M.,
            Mielenz,D., Schneider,P., Ehl,S., Rensing-Ehl,A., Smulski,C.R. and
            Rizzi,M.
  TITLE     Non-apoptotic FAS signaling controls mTOR activation and
            extrafollicular maturation in human B cells
  JOURNAL   Sci Immunol 9 (91), eadj5948 (2024)
   PUBMED   38215192
  REMARK    GeneRIF: Non-apoptotic FAS signaling controls mTOR activation and
            extrafollicular maturation in human B cells.
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Jenkins,M., Keir,M. and McCune,J.M.
  TITLE     A membrane-bound Fas decoy receptor expressed by human thymocytes
  JOURNAL   J Biol Chem 275 (11), 7988-7993 (2000)
   PUBMED   10713117
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Cascino,I., Papoff,G., Eramo,A. and Ruberti,G.
  TITLE     Soluble Fas/Apo-1 splicing variants and apoptosis
  JOURNAL   Front Biosci 1, d12-d18 (1996)
   PUBMED   9159204
  REMARK    GeneRIF: A review of alternative spliced APO-1 variants and their
            possible biological roles.
            Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Cheng,J., Zhou,T., Liu,C., Shapiro,J.P., Brauer,M.J., Kiefer,M.C.,
            Barr,P.J. and Mountz,J.D.
  TITLE     Protection from Fas-mediated apoptosis by a soluble form of the Fas
            molecule
  JOURNAL   Science 263 (5154), 1759-1762 (1994)
   PUBMED   7510905
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Bleesing,J.J.H., Nagaraj,C.B. and Zhang,K.
  TITLE     Autoimmune Lymphoproliferative Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301287
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Inazawa,J., Itoh,N., Abe,T. and Nagata,S.
  TITLE     Assignment of the human Fas antigen gene (Fas) to 10q24.1
  JOURNAL   Genomics 14 (3), 821-822 (1992)
   PUBMED   1385309
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Oehm,A., Behrmann,I., Falk,W., Pawlita,M., Maier,G., Klas,C.,
            Li-Weber,M., Richards,S., Dhein,J., Trauth,B.C. et al.
  TITLE     Purification and molecular cloning of the APO-1 cell surface
            antigen, a member of the tumor necrosis factor/nerve growth factor
            receptor superfamily. Sequence identity with the Fas antigen
  JOURNAL   J Biol Chem 267 (15), 10709-10715 (1992)
   PUBMED   1375228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012479.1, AK290978.1,
            AL157394.15, AK026195.1 and BU620333.1.
            
            Summary: The protein encoded by this gene is a member of the
            TNF-receptor superfamily. This receptor contains a death domain. It
            has been shown to play a central role in the physiological
            regulation of programmed cell death, and has been implicated in the
            pathogenesis of various malignancies and diseases of the immune
            system. The interaction of this receptor with its ligand allows the
            formation of a death-inducing signaling complex that includes
            Fas-associated death domain protein (FADD), caspase 8, and caspase
            10. The autoproteolytic processing of the caspases in the complex
            triggers a downstream caspase cascade, and leads to apoptosis. This
            receptor has been also shown to activate NF-kappaB, MAPK3/ERK1, and
            MAPK8/JNK, and is found to be involved in transducing the
            proliferating signals in normal diploid fibroblast and T cells.
            Several alternatively spliced transcript variants have been
            described, some of which are candidates for nonsense-mediated mRNA
            decay (NMD). The isoforms lacking the transmembrane domain may
            negatively regulate the apoptosis mediated by the full length
            isoform. [provided by RefSeq, Mar 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.69751.1,
                                           SRR1163657.562566.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000652046.1/ ENSP00000498466.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.31"
     Protein         1..335
                     /product="tumor necrosis factor receptor superfamily
                     member 6 isoform 1 precursor"
                     /note="tumor necrosis factor receptor superfamily, member
                     6; APO-1 cell surface antigen; apoptosis antigen 1; Fas
                     AMA; CD95 antigen; FASLG receptor; apoptosis-mediating
                     surface antigen FAS; apoptosis signaling receptor FAS; Fas
                     (TNF receptor superfamily, member 6); TNF receptor
                     superfamily member 6; mutant tumor necrosis receptor
                     superfamily member 6"
                     /calculated_mol_wt=35080
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2670
     mat_peptide     26..335
                     /product="Tumor necrosis factor receptor superfamily
                     member 6. /id=PRO_0000034563"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
                     /calculated_mol_wt=35080
     Site            28
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:22171320; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Region          39..167
                     /region_name="TNFRSF6"
                     /note="Tumor necrosis factor receptor superfamily member 6
                     (TNFRSF6), also known as fas cell surface death receptor
                     (Fas); cd10579"
                     /db_xref="CDD:276905"
     Region          47..83
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Region          48..82
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276905"
     Site            order(59..65,94..97,102)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276905"
     Region          84..127
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Region          85..127
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276905"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Region          128..166
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Region          129..149
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276905"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Site            174..190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Region          212..317
                     /region_name="Interaction with HIPK3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P25446; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Region          226..319
                     /region_name="Death_FAS_TNFRSF6"
                     /note="Death domain of FAS or TNF receptor superfamily
                     member 6; cd08316"
                     /db_xref="CDD:260028"
     Site            order(228..229,231..232,235..236,238..239,251,284..286,
                     288..289,291,294..296,298..300,302,305..309,311,314..315)
                     /site_type="other"
                     /note="FAS-FADD heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:260028"
     Region          230..254
                     /region_name="Interaction with CALM.
                     /evidence=ECO:0000269|PubMed:24914971"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Site            250
                     /site_type="glycosylation"
                     /note="(Microbial infection) N-beta-linked (GlcNAc)
                     arginine. /evidence=ECO:0000269|PubMed:30979585,
                     ECO:0000305|PubMed:23955153; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Site            order(251,307..308,311,315,318..319)
                     /site_type="other"
                     /note="octamer interface [polypeptide binding]"
                     /db_xref="CDD:260028"
     Site            order(296,299,303,306..307,314,317..318)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:260028"
     CDS             1..335
                     /gene="FAS"
                     /gene_synonym="ALPS1A; APO-1; APT1; CD95; FAS1; FASTM;
                     TNFRSF6"
                     /coded_by="NM_000043.6:80..1087"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS7393.1"
                     /db_xref="GeneID:355"
                     /db_xref="HGNC:HGNC:11920"
                     /db_xref="MIM:134637"
ORIGIN      
        1 mlgiwtllpl vltsvarlss ksvnaqvtdi nskglelrkt vttvetqnle glhhdgqfch
       61 kpcppgerka rdctvngdep dcvpcqegke ytdkahfssk crrcrlcdeg hgleveinct
      121 rtqntkcrck pnffcnstvc ehcdpctkce hgiikectlt sntkckeegs rsnlgwlcll
      181 llpiplivwv krkevqktcr khrkenqgsh esptlnpetv ainlsdvdls kyittiagvm
      241 tlsqvkgfvr kngvneakid eikndnvqdt aeqkvqllrn whqlhgkkea ydtlikdlkk
      301 anlctlaeki qtiilkdits dsensnfrne iqslv
//
LOCUS       NP_001103824             424 aa            linear   PRI 27-APR-2025
DEFINITION  zona pellucida sperm-binding protein 3 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001103824 XP_001130779
VERSION     NP_001103824.1
DBSOURCE    REFSEQ: accession NM_001110354.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Sun,L., Tong,K., Liu,W., Tian,Y., Liu,D., Huang,G. and Li,J.
  TITLE     Novel variants in ZP1, ZP2 and ZP3 associated with empty follicle
            syndrome and abnormal zona pellucida
  JOURNAL   Reprod Biomed Online 46 (5), 847-855 (2023)
   PUBMED   36931917
  REMARK    GeneRIF: Novel variants in ZP1, ZP2 and ZP3 associated with empty
            follicle syndrome and abnormal zona pellucida.
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Li,W., Li,Q., Xu,X., Wang,C., Hu,K. and Xu,J.
  TITLE     Novel mutations in TUBB8 and ZP3 cause human oocyte maturation
            arrest and female infertility
  JOURNAL   Eur J Obstet Gynecol Reprod Biol 279, 132-139 (2022)
   PUBMED   36335766
  REMARK    GeneRIF: Novel mutations in TUBB8 and ZP3 cause human oocyte
            maturation arrest and female infertility.
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Jia,W., Xi,Q., Zhu,L., Luo,Y., Li,Z., Hou,M., Zhang,D., Yang,X.,
            Hu,J., Jin,L. and Zhang,X.
  TITLE     Novel mutations in ZP2 and ZP3 cause female infertility in three
            patients
  JOURNAL   J Assist Reprod Genet 39 (5), 1205-1215 (2022)
   PUBMED   35366744
  REMARK    GeneRIF: Novel mutations in ZP2 and ZP3 cause female infertility in
            three patients.
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Zhang,Z., Guo,Q., Jia,L., Zhou,C., He,S., Fang,C., Zhang,M.,
            Sun,P., Zeng,Z., Wang,M., Wang,D. and Liang,X.
  TITLE     A novel gene mutation in ZP3 loop region identified in patients
            with empty follicle syndrome
  JOURNAL   Hum Mutat 43 (2), 180-188 (2022)
   PUBMED   34816529
  REMARK    GeneRIF: A novel gene mutation in ZP3 loop region identified in
            patients with empty follicle syndrome.
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Pulawska,K., Ponikwicka-Tyszko,D., Lebiedzinska,W., Guo,P.,
            Bernaczyk,P., Pilaszewicz-Puza,A., Li,X., Chrusciel,M., Lupu,O.,
            Leskinen,S., Makela,J.A., Toppari,J., Wolczynski,S., Coelingh
            Bennink,H.J.T., Huhtaniemi,I. and Rahman,N.A.
  TITLE     Novel expression of zona pellucida 3 protein in normal testis;
            potential functional implications
  JOURNAL   Mol Cell Endocrinol 539, 111502 (2022)
   PUBMED   34736966
  REMARK    GeneRIF: Novel expression of zona pellucida 3 protein in normal
            testis; potential functional implications.
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Kipersztok,S., Osawa,G.A., Liang,L.F., Modi,W.S. and Dean,J.
  TITLE     POM-ZP3, a bipartite transcript derived from human ZP3 and a POM121
            homologue
  JOURNAL   Genomics 25 (2), 354-359 (1995)
   PUBMED   7789967
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Miller,D.J., Gong,X. and Shur,B.D.
  TITLE     Sperm require beta-N-acetylglucosaminidase to penetrate through the
            egg zona pellucida
  JOURNAL   Development 118 (4), 1279-1289 (1993)
   PUBMED   8269854
REFERENCE   8  (residues 1 to 424)
  AUTHORS   van Duin,M., Polman,J.E., Suikerbuijk,R.F., Geurts-van Kessel,A.H.
            and Olijve,W.
  TITLE     The human gene for the zona pellucida glycoprotein ZP3 and a second
            polymorphic locus are located on chromosome 7
  JOURNAL   Cytogenet Cell Genet 63 (2), 111-113 (1993)
   PUBMED   8467708
REFERENCE   9  (residues 1 to 424)
  AUTHORS   van Duin,M., Polman,J.E., Verkoelen,C.C., Bunschoten,H.,
            Meyerink,J.H., Olijve,W. and Aitken,R.J.
  TITLE     Cloning and characterization of the human sperm receptor ligand
            ZP3: evidence for a second polymorphic allele with a different
            frequency in the Caucasian and Japanese populations
  JOURNAL   Genomics 14 (4), 1064-1070 (1992)
   PUBMED   1478648
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Chamberlin,M.E. and Dean,J.
  TITLE     Human homolog of the mouse sperm receptor
  JOURNAL   Proc Natl Acad Sci U S A 87 (16), 6014-6018 (1990)
   PUBMED   2385582
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005522.2, M60504.1,
            DB328313.1 and BC113949.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 17, 2007 this sequence version replaced XP_001130779.1.
            
            Summary: The zona pellucida is an extracellular matrix that
            surrounds the oocyte and early embryo. It is composed primarily of
            three or four glycoproteins with various functions during
            fertilization and preimplantation development. The protein encoded
            by this gene is a structural component of the zona pellucida and
            functions in primary binding and induction of the sperm acrosome
            reaction. The nascent protein contains a N-terminal signal peptide
            sequence, a conserved ZP domain, a C-terminal consensus furin
            cleavage site, and a transmembrane domain. It is hypothesized that
            furin cleavage results in release of the mature protein from the
            plasma membrane for subsequent incorporation into the zona
            pellucida matrix. However, the requirement for furin cleavage in
            this process remains controversial based on mouse studies. A
            variation in the last exon of this gene has previously served as
            the basis for an additional ZP3 locus; however, sequence and
            literature review reveals that there is only one full-length ZP3
            locus in the human genome. Another locus encoding a bipartite
            transcript designated POMZP3 contains a duplication of the last
            four exons of ZP3, including the above described variation, and
            maps closely to this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M60504.1, SRR14038194.3340216.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394857.8/ ENSP00000378326.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..424
                     /product="zona pellucida sperm-binding protein 3 isoform 1
                     precursor"
                     /note="zona pellucida protein C; zona pellucida
                     sperm-binding protein 3; zona pellucida glycoprotein 3B;
                     ZP3A/ZP3B; sperm receptor; zona pellucida glycoprotein
                     ZP3"
                     /calculated_mol_wt=44386
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2651
     mat_peptide     23..424
                     /product="zona pellucida sperm-binding protein 3 isoform
                     1"
                     /calculated_mol_wt=44386
     Site            23
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:15379548; propagated from
                     UniProtKB/Swiss-Prot (P21754.2)"
     Region          45..303
                     /region_name="ZP"
                     /note="Zona pellucida (ZP) domain; smart00241"
                     /db_xref="CDD:214579"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15379548; propagated from
                     UniProtKB/Swiss-Prot (P21754.2)"
     Site            147
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15379548; propagated from
                     UniProtKB/Swiss-Prot (P21754.2)"
     Site            156
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P21754.2)"
     Site            162
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P21754.2)"
     Site            163
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P21754.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15379548; propagated from
                     UniProtKB/Swiss-Prot (P21754.2)"
     Region          330..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21754.2)"
     Site            388..408
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21754.2)"
     CDS             1..424
                     /gene="ZP3"
                     /gene_synonym="OOMD3; OZEMA3; Zp-3; ZP3A; ZP3B; ZPC"
                     /coded_by="NM_001110354.2:16..1290"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS47618.1"
                     /db_xref="GeneID:7784"
                     /db_xref="HGNC:HGNC:13189"
                     /db_xref="MIM:182889"
ORIGIN      
        1 melsyrlfic lllwgstelc ypqplwllqg gashpetsvq pvlvecqeat lmvmvskdlf
       61 gtgkliraad ltlgpeacep lvsmdtedvv rfevglhecg nsmqvtddal vystfllhdp
      121 rpvgnlsivr tnraeipiec ryprqgnvss qailptwlpf rttvfseekl tfslrlmeen
      181 wnaekrsptf hlgdaahlqa eihtgshvpl rlfvdhcvat ptpdqnaspy htivdfhgcl
      241 vdgltdassa fkvprpgpdt lqftvdvfhf andsrnmiyi tchlkvtlae qdpdelnkac
      301 sfskpsnswf pvegsadicq ccnkgdcgtp shsrrqphvm sqwsrsasrn rrhvteeadv
      361 tvgplifldr rgdheveqwa lpsdtsvvll gvglavvvsl tltavilvlt rrcrtashpv
      421 sase
//
LOCUS       NP_542395                168 aa            linear   PRI 27-APR-2025
DEFINITION  D-aminoacyl-tRNA deacylase 2 [Homo sapiens].
ACCESSION   NP_542395
VERSION     NP_542395.1
DBSOURCE    REFSEQ: accession NM_080664.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Kuncha,S.K., Mazeed,M., Singh,R., Kattula,B., Routh,S.B. and
            Sankaranarayanan,R.
  TITLE     A chiral selectivity relaxed paralog of DTD for proofreading tRNA
            mischarging in Animalia
  JOURNAL   Nat Commun 9 (1), 511 (2018)
   PUBMED   29410408
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Havugimana,P.C., Hart,G.T., Nepusz,T., Yang,H., Turinsky,A.L.,
            Li,Z., Wang,P.I., Boutz,D.R., Fong,V., Phanse,S., Babu,M.,
            Craig,S.A., Hu,P., Wan,C., Vlasblom,J., Dar,V.U., Bezginov,A.,
            Clark,G.W., Wu,G.C., Wodak,S.J., Tillier,E.R., Paccanaro,A.,
            Marcotte,E.M. and Emili,A.
  TITLE     A census of human soluble protein complexes
  JOURNAL   Cell 150 (5), 1068-1081 (2012)
   PUBMED   22939629
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL163973.1, BI553940.1, AK055367.1, AL139353.3 and BU675173.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.971230.1, AK055367.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146, SAMN03267755
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310850.9/ ENSP00000312224.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..168
                     /product="D-aminoacyl-tRNA deacylase 2"
                     /EC_number="3.1.1.96"
                     /note="probable D-tyrosyl-tRNA(Tyr) deacylase 2; putative
                     D-tyrosyl-tRNA deacylase 2; putative D-tyrosyl-tRNA(Tyr)
                     deacylase 2; L-alanyl-tRNA deacylase; animalia-specifc
                     tRNA deacylase; animalia-specific tRNA deacylase;
                     D-tyrosyl-tRNA deacylase 2 (putative)"
                     /calculated_mol_wt=18529
     Region          11..167
                     /region_name="Tyr_Deacylase"
                     /note="D-Tyr-tRNA(Tyr) deacylase; pfam02580"
                     /db_xref="CDD:460603"
     Region          160..161
                     /region_name="Gly-transPro motif, allows the protein to
                     recognize chirality of D-amino acids.
                     /evidence=ECO:0000250|UniProtKB:Q8BHA3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FN9.1)"
     CDS             1..168
                     /gene="DTD2"
                     /gene_synonym="ATD; C14orf126"
                     /coded_by="NM_080664.3:114..620"
                     /db_xref="CCDS:CCDS9643.1"
                     /db_xref="GeneID:112487"
                     /db_xref="HGNC:HGNC:20277"
ORIGIN      
        1 maegsripqa rallqqclha rlqirpadgd vaaqwvevqr glviyvcffk gadkellpkm
       61 vntllnvkls etengkhvsi ldlpgnilii pqatlggrlk grnmqyhsns gkeegfelys
      121 qfvtlcekev aanskcaear vvvehgtygn rqvlkldtng pfthlief
//
LOCUS       NP_001355074            2615 aa            linear   PRI 27-APR-2025
DEFINITION  teneurin-2 isoform 3 [Homo sapiens].
ACCESSION   NP_001355074 XP_016865155
VERSION     NP_001355074.1
DBSOURCE    REFSEQ: accession NM_001368145.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2615)
  AUTHORS   Vysokov,N.V., Silva,J.P., Lelianova,V.G., Suckling,J., Cassidy,J.,
            Blackburn,J.K., Yankova,N., Djamgoz,M.B., Kozlov,S.V.,
            Tonevitsky,A.G. and Ushkaryov,Y.A.
  TITLE     Proteolytically released Lasso/teneurin-2 induces axonal attraction
            by interacting with latrophilin-1 on axonal growth cones
  JOURNAL   Elife 7, e37935 (2018)
   PUBMED   30457553
  REMARK    GeneRIF: These findings reveal a novel mechanism of axonal
            pathfinding, whereby latrophilin-1 and Lasso mediate both
            short-range interaction that supports synaptogenesis, and
            long-range signaling that induces axonal attraction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2615)
  AUTHORS   Tews,D., Fromme,T., Keuper,M., Hofmann,S.M., Debatin,K.M.,
            Klingenspor,M., Wabitsch,M. and Fischer-Posovszky,P.
  TITLE     Teneurin-2 (TENM2) deficiency induces UCP1 expression in
            differentiating human fat cells
  JOURNAL   Mol Cell Endocrinol 443, 106-113 (2017)
   PUBMED   28088466
  REMARK    GeneRIF: TENM2 knockdown induces both UCP1 mRNA and protein
            expression upon adipogenic differentiation without affecting
            mitochondrial mass.
REFERENCE   3  (residues 1 to 2615)
  AUTHORS   Perry,J.R., Day,F., Elks,C.E., Sulem,P., Thompson,D.J.,
            Ferreira,T., He,C., Chasman,D.I., Esko,T., Thorleifsson,G.,
            Albrecht,E., Ang,W.Q., Corre,T., Cousminer,D.L., Feenstra,B.,
            Franceschini,N., Ganna,A., Johnson,A.D., Kjellqvist,S.,
            Lunetta,K.L., McMahon,G., Nolte,I.M., Paternoster,L., Porcu,E.,
            Smith,A.V., Stolk,L., Teumer,A., Tsernikova,N., Tikkanen,E.,
            Ulivi,S., Wagner,E.K., Amin,N., Bierut,L.J., Byrne,E.M.,
            Hottenga,J.J., Koller,D.L., Mangino,M., Pers,T.H.,
            Yerges-Armstrong,L.M., Zhao,J.H., Andrulis,I.L., Anton-Culver,H.,
            Atsma,F., Bandinelli,S., Beckmann,M.W., Benitez,J., Blomqvist,C.,
            Bojesen,S.E., Bolla,M.K., Bonanni,B., Brauch,H., Brenner,H.,
            Buring,J.E., Chang-Claude,J., Chanock,S., Chen,J.,
            Chenevix-Trench,G., Collee,J.M., Couch,F.J., Couper,D.,
            Coveillo,A.D., Cox,A., Czene,K., D'adamo,A.P., Smith,G.D., De
            Vivo,I., Demerath,E.W., Dennis,J., Devilee,P., Dieffenbach,A.K.,
            Dunning,A.M., Eiriksdottir,G., Eriksson,J.G., Fasching,P.A.,
            Ferrucci,L., Flesch-Janys,D., Flyger,H., Foroud,T., Franke,L.,
            Garcia,M.E., Garcia-Closas,M., Geller,F., de Geus,E.E., Giles,G.G.,
            Gudbjartsson,D.F., Gudnason,V., Guenel,P., Guo,S., Hall,P.,
            Hamann,U., Haring,R., Hartman,C.A., Heath,A.C., Hofman,A.,
            Hooning,M.J., Hopper,J.L., Hu,F.B., Hunter,D.J., Karasik,D.,
            Kiel,D.P., Knight,J.A., Kosma,V.M., Kutalik,Z., Lai,S.,
            Lambrechts,D., Lindblom,A., Magi,R., Magnusson,P.K., Mannermaa,A.,
            Martin,N.G., Masson,G., McArdle,P.F., McArdle,W.L., Melbye,M.,
            Michailidou,K., Mihailov,E., Milani,L., Milne,R.L., Nevanlinna,H.,
            Neven,P., Nohr,E.A., Oldehinkel,A.J., Oostra,B.A., Palotie,A.,
            Peacock,M., Pedersen,N.L., Peterlongo,P., Peto,J., Pharoah,P.D.,
            Postma,D.S., Pouta,A., Pylkas,K., Radice,P., Ring,S.,
            Rivadeneira,F., Robino,A., Rose,L.M., Rudolph,A., Salomaa,V.,
            Sanna,S., Schlessinger,D., Schmidt,M.K., Southey,M.C., Sovio,U.,
            Stampfer,M.J., Stockl,D., Storniolo,A.M., Timpson,N.J., Tyrer,J.,
            Visser,J.A., Vollenweider,P., Volzke,H., Waeber,G.,
            Waldenberger,M., Wallaschofski,H., Wang,Q., Willemsen,G.,
            Winqvist,R., Wolffenbuttel,B.H., Wright,M.J., Boomsma,D.I.,
            Econs,M.J., Khaw,K.T., Loos,R.J., McCarthy,M.I., Montgomery,G.W.,
            Rice,J.P., Streeten,E.A., Thorsteinsdottir,U., van Duijn,C.M.,
            Alizadeh,B.Z., Bergmann,S., Boerwinkle,E., Boyd,H.A., Crisponi,L.,
            Gasparini,P., Gieger,C., Harris,T.B., Ingelsson,E., Jarvelin,M.R.,
            Kraft,P., Lawlor,D., Metspalu,A., Pennell,C.E., Ridker,P.M.,
            Snieder,H., Sorensen,T.I., Spector,T.D., Strachan,D.P.,
            Uitterlinden,A.G., Wareham,N.J., Widen,E., Zygmunt,M., Murray,A.,
            Easton,D.F., Stefansson,K., Murabito,J.M. and Ong,K.K.
  CONSRTM   Australian Ovarian Cancer Study; GENICA Network; kConFab; LifeLines
            Cohort Study; InterAct Consortium; Early Growth Genetics (EGG)
            Consortium
  TITLE     Parent-of-origin-specific allelic associations among 106 genomic
            loci for age at menarche
  JOURNAL   Nature 514 (7520), 92-97 (2014)
   PUBMED   25231870
REFERENCE   4  (residues 1 to 2615)
  AUTHORS   Scannell Bryan,M., Argos,M., Pierce,B., Tong,L., Rakibuz-Zaman,M.,
            Ahmed,A., Rahman,M., Islam,T., Yunus,M., Parvez,F., Roy,S.,
            Jasmine,F., Baron,J.A., Kibriya,M.G. and Ahsan,H.
  TITLE     Genome-wide association studies and heritability estimates of body
            mass index related phenotypes in Bangladeshi adults
  JOURNAL   PLoS One 9 (8), e105062 (2014)
   PUBMED   25133637
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2615)
  AUTHORS   Tanaka,T., Ngwa,J.S., van Rooij,F.J., Zillikens,M.C.,
            Wojczynski,M.K., Frazier-Wood,A.C., Houston,D.K., Kanoni,S.,
            Lemaitre,R.N., Luan,J., Mikkila,V., Renstrom,F., Sonestedt,E.,
            Zhao,J.H., Chu,A.Y., Qi,L., Chasman,D.I., de Oliveira Otto,M.C.,
            Dhurandhar,E.J., Feitosa,M.F., Johansson,I., Khaw,K.T.,
            Lohman,K.K., Manichaikul,A., McKeown,N.M., Mozaffarian,D.,
            Singleton,A., Stirrups,K., Viikari,J., Ye,Z., Bandinelli,S.,
            Barroso,I., Deloukas,P., Forouhi,N.G., Hofman,A., Liu,Y.,
            Lyytikainen,L.P., North,K.E., Dimitriou,M., Hallmans,G.,
            Kahonen,M., Langenberg,C., Ordovas,J.M., Uitterlinden,A.G.,
            Hu,F.B., Kalafati,I.P., Raitakari,O., Franco,O.H., Johnson,A.,
            Emilsson,V., Schrack,J.A., Semba,R.D., Siscovick,D.S., Arnett,D.K.,
            Borecki,I.B., Franks,P.W., Kritchevsky,S.B., Lehtimaki,T.,
            Loos,R.J., Orho-Melander,M., Rotter,J.I., Wareham,N.J.,
            Witteman,J.C., Ferrucci,L., Dedoussis,G., Cupples,L.A. and
            Nettleton,J.A.
  TITLE     Genome-wide meta-analysis of observational studies shows common
            genetic variants associated with macronutrient intake
  JOURNAL   Am J Clin Nutr 97 (6), 1395-1402 (2013)
   PUBMED   23636237
REFERENCE   6  (residues 1 to 2615)
  AUTHORS   Vinatzer,U., Gollinger,M., Mullauer,L., Raderer,M., Chott,A. and
            Streubel,B.
  TITLE     Mucosa-associated lymphoid tissue lymphoma: novel translocations
            including rearrangements of ODZ2, JMJD2C, and CNN3
  JOURNAL   Clin Cancer Res 14 (20), 6426-6431 (2008)
   PUBMED   18927281
  REMARK    GeneRIF: Gene rearrangements of ODZ2 is associated with
            mucosa-associated lymphoid tissue lymphoma.
REFERENCE   7  (residues 1 to 2615)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   8  (residues 1 to 2615)
  AUTHORS   Bagutti,C., Forro,G., Ferralli,J., Rubin,B. and
            Chiquet-Ehrismann,R.
  TITLE     The intracellular domain of teneurin-2 has a nuclear function and
            represses zic-1-mediated transcription
  JOURNAL   J Cell Sci 116 (Pt 14), 2957-2966 (2003)
   PUBMED   12783990
  REMARK    GeneRIF: intracellular domain of teneurin-2 has a nuclear function
            and role in repressing zic-1-mediated transcription
REFERENCE   9  (residues 1 to 2615)
  AUTHORS   Ben-Zur,T., Feige,E., Motro,B. and Wides,R.
  TITLE     The mammalian Odz gene family: homologs of a Drosophila pair-rule
            gene with expression implying distinct yet overlapping
            developmental roles
  JOURNAL   Dev Biol 217 (1), 107-120 (2000)
   PUBMED   10625539
REFERENCE   10 (residues 1 to 2615)
  AUTHORS   Oohashi,T., Zhou,X.H., Feng,K., Richter,B., Morgelin,M.,
            Perez,M.T., Su,W.D., Chiquet-Ehrismann,R., Rauch,U. and Fassler,R.
  TITLE     Mouse ten-m/Odz is a new family of dimeric type II transmembrane
            proteins expressed in many tissues
  JOURNAL   J Cell Biol 145 (3), 563-577 (1999)
   PUBMED   10225957
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008634.5, AC093304.4, AC008464.7, AC008705.6, AC011369.4,
            AC008637.7 and AC026689.6.
            
            On Jan 17, 2019 this sequence version replaced XP_016865155.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145743,
                              SAMN03465403 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2615
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..2615
                     /product="teneurin-2 isoform 3"
                     /note="odd Oz/ten-m homolog 2; teneurin-2; neurestin
                     alpha; odz, odd Oz/ten-m homolog 2; tenascin-M2; protein
                     Odd Oz/ten-m homolog 2"
                     /calculated_mol_wt=289682
     Region          <10..222
                     /region_name="Ten_N"
                     /note="Teneurin Intracellular Region; pfam06484"
                     /db_xref="CDD:461932"
     Region          423..582
                     /region_name="DUF5885"
                     /note="Family of unknown function (DUF5885); pfam19232"
                     /db_xref="CDD:437064"
     Region          <587..668
                     /region_name="C_rich_MXAN6577"
                     /note="MXAN_6577-like cysteine-rich domain; NF041328"
                     /db_xref="CDD:469225"
     Region          691..721
                     /region_name="acid_disulf_rpt"
                     /note="acidic double-disulfide repeat; NF033662"
                     /db_xref="CDD:411265"
     Region          1088..1411
                     /region_name="NHL"
                     /note="NHL repeat unit of beta-propeller proteins;
                     cl18310"
                     /db_xref="CDD:302697"
     Region          1126..1175
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1199..1237
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1253..1294
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1317..1350
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1372..2308
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          1385..1411
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          2531..2608
                     /region_name="Tox-GHH"
                     /note="GHH signature containing HNH/Endo VII superfamily
                     nuclease toxin; pfam15636"
                     /db_xref="CDD:464783"
     CDS             1..2615
                     /gene="TENM2"
                     /gene_synonym="ODZ2; ten-2; TEN-M2; TEN2; TNM2"
                     /coded_by="NM_001368145.1:323..8170"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:57451"
                     /db_xref="HGNC:HGNC:29943"
                     /db_xref="MIM:610119"
ORIGIN      
        1 mlhaankgrk psaeagrpip ptsspsllps aqlpsshnpp pvscqmplld sntshqimdt
       61 npdeefspns yllracsgpq qasssgppnh hsqstlrppl ppphnhtlsh hhssanslnr
      121 nsltnrrsqi hapapapndl attpesvqlq dswvlnsnvp letrhflfkt ssgstplfss
      181 sspgypltsg tvytppprll prntfsrkaf klkkpskycs wkcaalsaia aalllailla
      241 yfiamhllgl nwqlqpadgh tfnngirtgl pgnddvatmp sggkvpwslk nssidsgeae
      301 vgrrvtqevp pgvfwrsqih isqpqflkfn islgkdalfg vyirrglpps haqydfmerl
      361 dgkekwsvve sprerrsiqt lvqneavfvq yldvglwhla fyndgkdkem vsfntvvlds
      421 vqdcprnchg ngecvsgvch cfpgflgadc akaacpvlcs gngqyskgtc qcysgwkgae
      481 cdvpmnqcid pscgghgsci dgncvcsagy kgehceevdc ldptcsshgv cvngeclcsp
      541 gwgglncela rvqcpdqcsg hgtylpdtgl cscdpnwmgp dcsvevcsvd cgthgvcigg
      601 acrceegwtg aacdqrvchp rciehgtckd gkcecregwn gehctigrqt agtetdgcpd
      661 lcngngrctl gqnswqcvcq tgwrgpgcnv ametscadnk dnegdglvdc ldpdcclqsa
      721 cqnsllcrgs rdpldiiqqg qtdwpavksf ydrikllagk dsthiipgen pfnsslvsli
      781 rgqvvttdgt plvgvnvsfv kypkygytit rqdgtfdlia nggasltlhf erapfmsqer
      841 tvwlpwnsfy amdtlvmkte ensipscdls gfvrpdpiii ssplstffsa apgqnpivpe
      901 tqvlheeiel pgsnvklryl ssrtagyksl lkitmtqstv plnlirvhlm vaveghlfqk
      961 sfqaspnlay tfiwdktday gqrvyglsda vvsvgfeyet cpslilwekr tallqgfeld
     1021 psnlggwsld khhilnvksg ilhkgtgenq fltqqpaiit simgngrrrs iscpscngla
     1081 egnkllapva lavgidgsly vgdfnyirri fpsrnvtsil elrnnpahky ylavdpvsgs
     1141 lyvsdtnsrr iyrvkslsgt kdlagnsevv agtgeqclpf dearcgdggk aidatlmspr
     1201 giavdknglm yfvdatmirk vdqngiistl lgsndltavr plscdssmdv aqvrlewptd
     1261 lavnpmdnsl yvlennvilr itenhqvsii agrpmhcqvp gidyslskla ihsalesasa
     1321 iaishtgvly itetdekkin rlrqvttnge icllagaasd cdckndvncn cysgddayat
     1381 dailnspssl avapdgtiyi adlgnirira vsknkpvlna fnqyeaaspg eqelyvfnad
     1441 gihqytvslv tgeylynfty stdndvteli dnngnslkir rdssgmprhl lmpdnqiitl
     1501 tvgtngglkv vstqnlelgl mtydgntgll atksdetgwt tfydydhegr ltnvtrptgv
     1561 vtslhremek sitidiensn rdddvtvitn lssveasytv vqdqvrnsyq lcnngtlrvm
     1621 yangmgisfh sephvlagti tptigrcnis lpmenglnsi ewrlrkeqik gkvtifgrkl
     1681 rvhgrnllsi dydrnirtek iyddhrkftl riiydqvgrp flwlpssgla avnvsyffng
     1741 rlaglqrgam sertdidkqg rivsrmfadg kvwsysyldk smvlllqsqr qyifeydssd
     1801 rllavtmpsv arhsmsthts igyirniynp pesnasvifd ysddgrilkt sflgtgrqvf
     1861 ykygklskls eivydstavt fgydettgvl kmvnlqsggf sctiryrkig plvdkqiyrf
     1921 seegmvnarf dytyhdnsfr iasikpvise tplpvdlyry deisgkvehf gkfgviyydi
     1981 nqiittavmt lskhfdthgr ikevqyemfr slmywmtvqy dsmgrvikre lklgpyantt
     2041 kytydydgdg qlqsvavndr ptwrysydln gnlhllnpgn svrlmplryd lrdritrlgd
     2101 vqykidddgy lcqrgsdife ynskglltra ynkasgwsvq yrydgvgrra syktnlghhl
     2161 qyfysdlhnp trithvynhs nseitslyyd lqghlfames ssgeeyyvas dntgtplavf
     2221 singlmikql qytaygeiyy dsnpdfqmvi gfhgglydpl tklvhftqrd ydvlagrwts
     2281 pdytmwknvg kepapfnlym fksnnplsse ldlknyvtdv kswlvmfgfq lsniipgfpr
     2341 akmyfvpppy elsesqasen gqlitgvqqt terhnqafma legqvitkkl hasirekagh
     2401 wfatttpiig kgimfaikeg rvttgvssia sedsrkvasv lnnayyldkm hysiegkdth
     2461 yfvkigsadg dlvtlgttig rkvlesgvnv tvsqptllvn grtrrftnie fqystlllsi
     2521 rygltpdtld eekarvldqa rqralgtawa keqqkardgr egsrlwtege kqqllstgrv
     2581 qgyegyyvlp veqypelads ssniqflrqn emgkr
//
LOCUS       NP_001353380             256 aa            linear   PRI 27-APR-2025
DEFINITION  rab GTPase-activating protein 1-like isoform L [Homo sapiens].
ACCESSION   NP_001353380
VERSION     NP_001353380.1
DBSOURCE    REFSEQ: accession NM_001366451.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Anttila,V., Winsvold,B.S., Gormley,P., Kurth,T., Bettella,F.,
            McMahon,G., Kallela,M., Malik,R., de Vries,B., Terwindt,G.,
            Medland,S.E., Todt,U., McArdle,W.L., Quaye,L., Koiranen,M.,
            Ikram,M.A., Lehtimaki,T., Stam,A.H., Ligthart,L., Wedenoja,J.,
            Dunham,I., Neale,B.M., Palta,P., Hamalainen,E., Schurks,M.,
            Rose,L.M., Buring,J.E., Ridker,P.M., Steinberg,S., Stefansson,H.,
            Jakobsson,F., Lawlor,D.A., Evans,D.M., Ring,S.M., Farkkila,M.,
            Artto,V., Kaunisto,M.A., Freilinger,T., Schoenen,J., Frants,R.R.,
            Pelzer,N., Weller,C.M., Zielman,R., Heath,A.C., Madden,P.A.F.,
            Montgomery,G.W., Martin,N.G., Borck,G., Gobel,H., Heinze,A.,
            Heinze-Kuhn,K., Williams,F.M.K., Hartikainen,A.L., Pouta,A., van
            den Ende,J., Uitterlinden,A.G., Hofman,A., Amin,N., Hottenga,J.J.,
            Vink,J.M., Heikkila,K., Alexander,M., Muller-Myhsok,B.,
            Schreiber,S., Meitinger,T., Wichmann,H.E., Aromaa,A.,
            Eriksson,J.G., Traynor,B., Trabzuni,D., Rossin,E., Lage,K.,
            Jacobs,S.B.R., Gibbs,J.R., Birney,E., Kaprio,J., Penninx,B.W.,
            Boomsma,D.I., van Duijn,C., Raitakari,O., Jarvelin,M.R.,
            Zwart,J.A., Cherkas,L., Strachan,D.P., Kubisch,C., Ferrari,M.D.,
            van den Maagdenberg,A.M.J.M., Dichgans,M., Wessman,M., Smith,G.D.,
            Stefansson,K., Daly,M.J., Nyholt,D.R., Chasman,D. and Palotie,A.
  CONSRTM   North American Brain Expression Consortium; UK Brain Expression
            Consortium
  TITLE     Genome-wide meta-analysis identifies new susceptibility loci for
            migraine
  JOURNAL   Nat Genet 45 (8), 912-917 (2013)
   PUBMED   23793025
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Kim,J.H., Jung,S.H., Bae,J.S., Lee,H.S., Yim,S.H., Park,S.Y.,
            Bang,S.Y., Hu,H.J., Shin,H.D., Bae,S.C. and Chung,Y.J.
  TITLE     Deletion variants of RABGAP1L, 10q21.3, and C4 are associated with
            the risk of systemic lupus erythematosus in Korean women
  JOURNAL   Arthritis Rheum 65 (4), 1055-1063 (2013)
   PUBMED   23335107
  REMARK    GeneRIF: Deletion variants of RABGAP1L were found to be
            significantly associated with SLE in Korean women.
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB019493.1, AB019490.1 and Z99127.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB019490.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1"
     Protein         1..256
                     /product="rab GTPase-activating protein 1-like isoform L"
                     /note="TBC1 domain family, member 18; expressed in
                     hematopoietic cells, heart, liver (HLL); rab
                     GTPase-activating protein 1-like"
                     /calculated_mol_wt=29166
     Region          <8..>223
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..256
                     /gene="RABGAP1L"
                     /gene_synonym="HHL; TBC1D18"
                     /coded_by="NM_001366451.1:1185..1955"
                     /note="isoform L is encoded by transcript variant 15"
                     /db_xref="GeneID:9910"
                     /db_xref="HGNC:HGNC:24663"
                     /db_xref="MIM:609238"
ORIGIN      
        1 mlkipthleg kikitkrenr rlqeasmrle qenddlahel vtskialrnd ldqaedkadv
       61 lnkellltkq rlveteeekr kqeeetaqlk evfrkqleka eyeikkttai iaeykqicsq
      121 lstrlekqqa askeelevvk gkmmackhcs difskegalk laatgredqg ietddekdsl
      181 kkqlremele laqtklqlve akckiqeleh qrgalmneiq aaknswfskt lnsiktatgt
      241 qplqpapvtq ppkest
//
LOCUS       NP_001353922             122 aa            linear   PRI 27-APR-2025
DEFINITION  interferon alpha-inducible protein 27, mitochondrial isoform 1
            [Homo sapiens].
ACCESSION   NP_001353922
VERSION     NP_001353922.1
DBSOURCE    REFSEQ: accession NM_001366993.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Oguz,A.K., Oygur,C.S., Tasir,S., Ozdag,H. and Akar,M.N.
  TITLE     Behcet syndrome: The disturbed balance between anti- (CLEC12A, CLC)
            and proinflammatory (IFI27) gene expressions
  JOURNAL   Immun Inflamm Dis 11 (4), e836 (2023)
   PUBMED   37102643
  REMARK    GeneRIF: Behcet syndrome: The disturbed balance between anti-
            (CLEC12A, CLC) and proinflammatory (IFI27) gene expressions.
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Jiang,C., He,C., Kan,J., Guan,H., Zhou,T. and Yang,Y.
  TITLE     Integrative bulk and single-cell transcriptome profiling analysis
            reveals IFI27 as a novel interferon-stimulated gene in dengue
  JOURNAL   J Med Virol 95 (4), e28706 (2023)
   PUBMED   36971141
  REMARK    GeneRIF: Integrative bulk and single-cell transcriptome profiling
            analysis reveals IFI27 as a novel interferon-stimulated gene in
            dengue.
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Shojaei,M., Shamshirian,A., Monkman,J., Grice,L., Tran,M.,
            Tan,C.W., Teo,S.M., Rodrigues Rossi,G., McCulloch,T.R., Nalos,M.,
            Raei,M., Razavi,A., Ghasemian,R., Gheibi,M., Roozbeh,F., Sly,P.D.,
            Spann,K.M., Chew,K.Y., Zhu,Y., Xia,Y., Wells,T.J., Senegaglia,A.C.,
            Kuniyoshi,C.L., Franck,C.L., Dos Santos,A.F.R., de Noronha,L.,
            Motamen,S., Valadan,R., Amjadi,O., Gogna,R., Madan,E.,
            Alizadeh-Navaei,R., Lamperti,L., Zuniga,F., Nova-Lamperti,E.,
            Labarca,G., Knippenberg,B., Herwanto,V., Wang,Y., Phu,A., Chew,T.,
            Kwan,T., Kim,K., Teoh,S., Pelaia,T.M., Kuan,W.S., Jee,Y.,
            Iredell,J., O'Byrne,K., Fraser,J.F., Davis,M.J., Belz,G.T.,
            Warkiani,M.E., Gallo,C.S., Souza-Fonseca-Guimaraes,F., Nguyen,Q.,
            Mclean,A., Kulasinghe,A., Short,K.R. and Tang,B.
  TITLE     IFI27 transcription is an early predictor for COVID-19 outcomes, a
            multi-cohort observational study
  JOURNAL   Front Immunol 13, 1060438 (2023)
   PUBMED   36685600
  REMARK    GeneRIF: IFI27 transcription is an early predictor for COVID-19
            outcomes, a multi-cohort observational study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Saini,J., Thapa,U., Bandyopadhyay,B., Vrati,S. and Banerjee,A.
  TITLE     Knockdown of NEAT1 restricts dengue virus replication by augmenting
            interferon alpha-inducible protein 27 via the RIG-I pathway
  JOURNAL   J Gen Virol 104 (1) (2023)
   PUBMED   36748518
  REMARK    GeneRIF: Knockdown of NEAT1 restricts dengue virus replication by
            augmenting interferon alpha-inducible protein 27 via the RIG-I
            pathway.
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Guo,M., Cao,W., Chen,S., Tian,R., Xue,B., Wang,L., Liu,Q., Deng,R.,
            Wang,X., Wang,Z., Zhang,Y., Yang,D., Zuo,C., Li,G., Tang,S. and
            Zhu,H.
  TITLE     TRIM21 Regulates Virus-Induced Cell Pyroptosis through
            Polyubiquitination of ISG12a
  JOURNAL   J Immunol 209 (10), 1987-1998 (2022)
   PUBMED   36426955
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Izmailova,E., Bertley,F.M., Huang,Q., Makori,N., Miller,C.J.,
            Young,R.A. and Aldovini,A.
  TITLE     HIV-1 Tat reprograms immature dendritic cells to express
            chemoattractants for activated T cells and macrophages
  JOURNAL   Nat Med 9 (2), 191-197 (2003)
   PUBMED   12539042
REFERENCE   7  (residues 1 to 122)
  AUTHORS   Martensen,P.M., Sogaard,T.M., Gjermandsen,I.M., Buttenschon,H.N.,
            Rossing,A.B., Bonnevie-Nielsen,V., Rosada,C., Simonsen,J.L. and
            Justesen,J.
  TITLE     The interferon alpha induced protein ISG12 is localized to the
            nuclear membrane
  JOURNAL   Eur J Biochem 268 (22), 5947-5954 (2001)
   PUBMED   11722583
REFERENCE   8  (residues 1 to 122)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 122)
  AUTHORS   Taules,M., Rius,E., Talaya,D., Lopez-Girona,A., Bachs,O. and
            Agell,N.
  TITLE     Calmodulin is essential for cyclin-dependent kinase 4 (Cdk4)
            activity and nuclear accumulation of cyclin D1-Cdk4 during G1
  JOURNAL   J Biol Chem 273 (50), 33279-33286 (1998)
   PUBMED   9837900
REFERENCE   10 (residues 1 to 122)
  AUTHORS   Rasmussen,U.B., Wolf,C., Mattei,M.G., Chenard,M.P., Bellocq,J.P.,
            Chambon,P., Rio,M.C. and Basset,P.
  TITLE     Identification of a new interferon-alpha-inducible gene (p27) on
            human chromosome 14q32 and its expression in breast carcinoma
  JOURNAL   Cancer Res 53 (17), 4096-4101 (1993)
   PUBMED   8358738
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL121838.4 and KF573698.1.
            
            Transcript Variant: This variant (11) differs in the 5' UTR
            compared to variant 1. This variant represents an allele commonly
            found in the human population and corresponds to the allele present
            in the GRC reference assembly. Variants 1, 3, 5, 11 and 12 encode
            the same isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015492.1, BE888281.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..122
                     /product="interferon alpha-inducible protein 27,
                     mitochondrial isoform 1"
                     /note="2310061N23Rik; interferon alpha-inducible protein
                     27, mitochondrial; ISG12(a); interferon-stimulated gene
                     12a protein; interferon alpha-induced 11.5 kDa protein"
                     /calculated_mol_wt=8318
     transit_peptide 1..33
                     /note="Mitochondrion.
                     /evidence=ECO:0000305|PubMed:18330707; propagated from
                     UniProtKB/Swiss-Prot (P40305.4)"
                     /calculated_mol_wt=3242
     mat_peptide     34..122
                     /product="Interferon alpha-inducible protein 27,
                     mitochondrial. /id=PRO_0000147372"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
                     /calculated_mol_wt=8318
     Site            34..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
     Region          37..115
                     /region_name="Ifi-6-16"
                     /note="Interferon-induced 6-16 family; pfam06140"
                     /db_xref="CDD:461837"
     Site            71..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
     Region          76..122
                     /region_name="Mediates interaction with SKP2 and hepatitis
                     C virus non-structural protein NS5A.
                     /evidence=ECO:0000269|PubMed:27194766"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
     Region          103..112
                     /region_name="Required for hepatitis C virus
                     non-structural protein NS5A degradation.
                     /evidence=ECO:0000269|PubMed:27194766"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
     CDS             1..122
                     /gene="IFI27"
                     /gene_synonym="FAM14D; ISG12; ISG12A; P27"
                     /coded_by="NM_001366993.1:189..557"
                     /note="isoform 1 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS32148.1"
                     /db_xref="GeneID:3429"
                     /db_xref="HGNC:HGNC:5397"
                     /db_xref="MIM:600009"
ORIGIN      
        1 measaltssa vtsvakvvrv asgsavvlpl ariatvvigg vvamaavpmv lsamgftaag
       61 iasssiaakm msaaaiangg gvasgslvat lqslgatgls gltkfilgsi gsaiaaviar
      121 fy
//
LOCUS       NP_004219                399 aa            linear   PRI 27-APR-2025
DEFINITION  cytohesin-2 isoform 2 [Homo sapiens].
ACCESSION   NP_004219
VERSION     NP_004219.3
DBSOURCE    REFSEQ: accession NM_004228.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Viegas,A., Yin,D.M., Borggrafe,J., Viennet,T., Falke,M.,
            Schmitz,A., Famulok,M. and Etzkorn,M.
  TITLE     Molecular Architecture of a Network of Potential Intracellular EGFR
            Modulators: ARNO, CaM, Phospholipids, and the Juxtamembrane Segment
  JOURNAL   Structure 28 (1), 54-62 (2020)
   PUBMED   31780432
  REMARK    GeneRIF: Molecular Architecture of a Network of Potential
            Intracellular EGFR Modulators: ARNO, CaM, Phospholipids, and the
            Juxtamembrane Segment.
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Luong,P., Hedl,M., Yan,J., Zuo,T., Fu,T.M., Jiang,X.,
            Thiagarajah,J.R., Hansen,S.H., Lesser,C.F., Wu,H., Abraham,C. and
            Lencer,W.I.
  TITLE     INAVA-ARNO complexes bridge mucosal barrier function with
            inflammatory signaling
  JOURNAL   Elife 7, e38539 (2018)
   PUBMED   30355448
  REMARK    GeneRIF: INAVA-CUPID exhibits dual functions, coordinated directly
            by ARNO, that bridge epithelial barrier function with extracellular
            signals and inflammation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Manzanillo,P., Mouchess,M., Ota,N., Dai,B., Ichikawa,R., Wuster,A.,
            Haley,B., Alvarado,G., Kwon,Y., Caothien,R., Roose-Girma,M.,
            Warming,S., McKenzie,B.S., Keir,M.E., Scherl,A., Ouyang,W. and
            Yi,T.
  TITLE     Inflammatory Bowel Disease Susceptibility Gene C1ORF106 Regulates
            Intestinal Epithelial Permeability
  JOURNAL   Immunohorizons 2 (5), 164-171 (2018)
   PUBMED   31022698
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Mossessova,E., Gulbis,J.M. and Goldberg,J.
  TITLE     Structure of the guanine nucleotide exchange factor Sec7 domain of
            human arno and analysis of the interaction with ARF GTPase
  JOURNAL   Cell 92 (3), 415-423 (1998)
   PUBMED   9476900
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Frank,S., Upender,S., Hansen,S.H. and Casanova,J.E.
  TITLE     ARNO is a guanine nucleotide exchange factor for ADP-ribosylation
            factor 6
  JOURNAL   J Biol Chem 273 (1), 23-27 (1998)
   PUBMED   9417041
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Meacci,E., Tsai,S.C., Adamik,R., Moss,J. and Vaughan,M.
  TITLE     Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for
            ADP-ribosylation factor
  JOURNAL   Proc Natl Acad Sci U S A 94 (5), 1745-1748 (1997)
   PUBMED   9050849
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Chardin,P., Paris,S., Antonny,B., Robineau,S., Beraud-Dufour,S.,
            Jackson,C.L. and Chabre,M.
  TITLE     A human exchange factor for ARF contains Sec7- and
            pleckstrin-homology domains
  JOURNAL   Nature 384 (6608), 481-484 (1996)
   PUBMED   8945478
REFERENCE   10 (residues 1 to 399)
  AUTHORS   Kolanus,W., Nagel,W., Schiller,B., Zeitlmann,L., Godar,S.,
            Stockinger,H. and Seed,B.
  TITLE     Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by
            cytohesin-1, a cytoplasmic regulatory molecule
  JOURNAL   Cell 86 (2), 233-242 (1996)
   PUBMED   8706128
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC344850.1, X99753.1,
            AC008403.8 and BC012771.2.
            
            On Aug 9, 2008 this sequence version replaced NP_004219.2.
            
            Summary: The protein encoded by this gene is a member of the PSCD
            family. Members of this family have identical structural
            organization that consists of an N-terminal coiled-coil motif, a
            central Sec7 domain, and a C-terminal pleckstrin homology (PH)
            domain. The coiled-coil motif is involved in homodimerization, the
            Sec7 domain contains guanine-nucleotide exchange protein (GEP)
            activity, and the PH domain interacts with phospholipids and is
            responsible for association of PSCDs with membranes. Members of
            this family appear to mediate the regulation of protein sorting and
            membrane trafficking. The encoded protein exhibits GEP activity in
            vitro with ARF1, ARF3, and ARF6 and is 83% homologous to CYTH1. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Transcript Variant: This variant (2) lacks a 3-nucleotide exon in
            the PH domain region, compared to variant 1. This results in a
            protein (isoform 2)  missing a single glycine residue, compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.194741.1,
                                           SRR3476690.267525.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000452733.7/ ENSP00000408236.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..399
                     /product="cytohesin-2 isoform 2"
                     /note="pleckstrin homology, Sec7 and coiled/coil domains 2
                     (cytohesin-2); ARF nucleotide-binding site opener; ARF
                     exchange factor; PH, SEC7 and coiled-coil
                     domain-containing protein 2; pleckstrin homology, Sec7 and
                     coiled-coil domains 2; CTC-273B12.8"
                     /calculated_mol_wt=46358
     Region          61..243
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          258..377
                     /region_name="PH_GRP1-like"
                     /note="General Receptor for Phosphoinositides-1-like
                     Pleckstrin homology (PH) domain; cd01252"
                     /db_xref="CDD:269954"
     Site            order(258,285,287,289,299,302,304,335..337,339,342..347,
                     377)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:269954"
     Site            order(268,271,275,277,279,290,300,338,349..350)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269954"
     Region          386..394
                     /region_name="C-terminal autoinhibitory region.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99418.2)"
     CDS             1..399
                     /gene="CYTH2"
                     /gene_synonym="ARNO; CTS18; CTS18.1; cytohesin-2; PSCD2;
                     PSCD2L; SEC7L; Sec7p-L; Sec7p-like"
                     /coded_by="NM_004228.7:140..1339"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12722.1"
                     /db_xref="GeneID:9266"
                     /db_xref="HGNC:HGNC:9502"
                     /db_xref="MIM:602488"
ORIGIN      
        1 medgvyeppd ltpeermele nirrrkqell veiqrlreel seamsevegl eanegsktlq
       61 rnrkmamgrk kfnmdpkkgi qflvenellq ntpeeiarfl ykgeglnkta igdylgeree
      121 lnlavlhafv dlheftdlnl vqalrqflws frlpgeaqki drmmeafaqr yclcnpgvfq
      181 stdtcyvlsf avimlntslh npnvrdkpgl erfvamnrgi neggdlpeel lrnlydsirn
      241 epfkipeddg ndlthtffnp dregwllklg grvktwkrrw filtdnclyy feyttdkepr
      301 giiplenlsi revddprkpn cfelyipnnk gqlikackte adgrvvegnh mvyrisaptq
      361 eekdewiksi qaavsvdpfy emlaarkkri svkkkqeqp
//
LOCUS       NP_665872                417 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat and SAM domain-containing protein 4B [Homo sapiens].
ACCESSION   NP_665872
VERSION     NP_665872.2
DBSOURCE    REFSEQ: accession NM_145865.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Graves,M.J., Matoo,S., Choi,M.S., Storad,Z.A., El Sheikh
            Idris,R.A., Pickles,B.K., Acharya,P., Shinder,P.E., Arvay,T.O. and
            Crawley,S.W.
  TITLE     A cryptic sequence targets the adhesion complex scaffold ANKS4B to
            apical microvilli to promote enterocyte brush border assembly
  JOURNAL   J Biol Chem 295 (36), 12588-12604 (2020)
   PUBMED   32636301
  REMARK    GeneRIF: A cryptic sequence targets the adhesion complex scaffold
            ANKS4B to apical microvilli to promote enterocyte brush border
            assembly.
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Choi,M.S., Graves,M.J., Matoo,S., Storad,Z.A., El Sheikh
            Idris,R.A., Weck,M.L., Smith,Z.B., Tyska,M.J. and Crawley,S.W.
  TITLE     The small EF-hand protein CALML4 functions as a critical myosin
            light chain within the intermicrovillar adhesion complex
  JOURNAL   J Biol Chem 295 (28), 9281-9296 (2020)
   PUBMED   32209652
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 417)
  AUTHORS   He,Y., Li,J. and Zhang,M.
  TITLE     Myosin VII, USH1C, and ANKS4B or USH1G Together Form Condensed
            Molecular Assembly via Liquid-Liquid Phase Separation
  JOURNAL   Cell Rep 29 (4), 974-986 (2019)
   PUBMED   31644917
  REMARK    GeneRIF: Myosin VII, USH1C, and ANKS4B or USH1G Together Form
            Condensed Molecular Assembly via Liquid-Liquid Phase Separation.
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Tomkins,J.E., Dihanich,S., Beilina,A., Ferrari,R., Ilacqua,N.,
            Cookson,M.R., Lewis,P.A. and Manzoni,C.
  TITLE     Comparative Protein Interaction Network Analysis Identifies Shared
            and Distinct Functions for the Human ROCO Proteins
  JOURNAL   Proteomics 18 (10), e1700444 (2018)
   PUBMED   29513927
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Crawley,S.W., Weck,M.L., Grega-Larson,N.E., Shifrin,D.A. Jr. and
            Tyska,M.J.
  TITLE     ANKS4B Is Essential for Intermicrovillar Adhesion Complex Formation
  JOURNAL   Dev Cell 36 (2), 190-200 (2016)
   PUBMED   26812018
  REMARK    GeneRIF: ankyrin repeat and sterile alpha motif domain containing
            4B (ANKS4B) localizes to the tips of adherent brush border
            microvilli and is essential for intermicrovillar adhesion
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Reyniers,L., Del Giudice,M.G., Civiero,L., Belluzzi,E.,
            Lobbestael,E., Beilina,A., Arrigoni,G., Derua,R., Waelkens,E.,
            Li,Y., Crosio,C., Iaccarino,C., Cookson,M.R., Baekelandt,V.,
            Greggio,E. and Taymans,J.M.
  TITLE     Differential protein-protein interactions of LRRK1 and LRRK2
            indicate roles in distinct cellular signaling pathways
  JOURNAL   J Neurochem 131 (2), 239-250 (2014)
   PUBMED   24947832
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Sato,Y., Hatta,M., Karim,M.F., Sawa,T., Wei,F.Y., Sato,S.,
            Magnuson,M.A., Gonzalez,F.J., Tomizawa,K., Akaike,T., Yoshizawa,T.
            and Yamagata,K.
  TITLE     Anks4b, a novel target of HNF4alpha protein, interacts with GRP78
            protein and regulates endoplasmic reticulum stress-induced
            apoptosis in pancreatic beta-cells
  JOURNAL   J Biol Chem 287 (27), 23236-23245 (2012)
   PUBMED   22589549
REFERENCE   9  (residues 1 to 417)
  AUTHORS   Johnston,A.M., Naselli,G., Niwa,H., Brodnicki,T., Harrison,L.C. and
            Gonez,L.J.
  TITLE     Harp (harmonin-interacting, ankyrin repeat-containing protein), a
            novel protein that interacts with harmonin in epithelial tissues
  JOURNAL   Genes Cells 9 (10), 967-982 (2004)
   PUBMED   15461667
REFERENCE   10 (residues 1 to 417)
  AUTHORS   Weil,D., El-Amraoui,A., Masmoudi,S., Mustapha,M., Kikkawa,Y.,
            Laine,S., Delmaghani,S., Adato,A., Nadifi,S., Zina,Z.B., Hamel,C.,
            Gal,A., Ayadi,H., Yonekawa,H. and Petit,C.
  TITLE     Usher syndrome type I G (USH1G) is caused by mutations in the gene
            encoding SANS, a protein that associates with the USH1C protein,
            harmonin
  JOURNAL   Hum Mol Genet 12 (5), 463-471 (2003)
   PUBMED   12588794
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK096138.1, BC112368.1 and AF001550.1.
            
            On Jun 7, 2007 this sequence version replaced NP_665872.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096138.1, BC111784.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311620.7/ ENSP00000308772.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..417
                     /product="ankyrin repeat and SAM domain-containing protein
                     4B"
                     /note="harmonin-interacting ankyrin-repeat containing
                     protein"
                     /calculated_mol_wt=46466
     Region          1..252
                     /region_name="Mediates localization to microvilli.
                     /evidence=ECO:0000269|PubMed:26812018"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8V4.2)"
     Region          <1..163
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          3..29
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(6..7,10..12,14..15,19,22,29,31,33,37..38,41..43,
                     45..46,50,53,62,64,66,70..71,74..76,78..79,83,86,95)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          31..62
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          64..95
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          97..125
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          151..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8V4.2)"
     Region          253..346
                     /region_name="Mediates interaction with MYO7B.
                     /evidence=ECO:0000269|PubMed:26812018"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8V4.2)"
     Region          255..>281
                     /region_name="CEN_ANKS4B"
                     /note="central domain found in ankyrin repeat and SAM
                     domain-containing protein 4B; cd21802"
                     /db_xref="CDD:409641"
     Site            order(264..265,268..269,271..276)
                     /site_type="other"
                     /note="myosin tail binding site [polypeptide binding]"
                     /db_xref="CDD:409641"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N8V4.2)"
     Region          305..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8V4.2)"
     Region          345..410
                     /region_name="SAM_HARP"
                     /note="SAM domain of HARP subfamily; cd09587"
                     /db_xref="CDD:188986"
     Site            order(345,347,349..351,353..354,356,401..402,406)
                     /site_type="other"
                     /note="putative polypeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:188986"
     Region          415..417
                     /region_name="PDZ-binding, mediates interaction with
                     USH1C. /evidence=ECO:0000269|PubMed:26812018"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8V4.2)"
     CDS             1..417
                     /gene="ANKS4B"
                     /gene_synonym="HARP"
                     /coded_by="NM_145865.3:40..1293"
                     /db_xref="CCDS:CCDS42130.1"
                     /db_xref="GeneID:257629"
                     /db_xref="HGNC:HGNC:26795"
                     /db_xref="MIM:609901"
ORIGIN      
        1 mstryhqaas dsylellkea tkrdlnlsde dgmtptllaa yhgnlealei icsrggdpdr
       61 cdiwgntplh faasnghahc vsflvnfgan ifaldndlqt pldaaasreq necvalldka
      121 ataqnimnpk kvtrlkeqaq knarrqikec erlqekhqnk mahtyskees gtlssskgtf
      181 srsspsnasa pgtfgslskg ikdtfkikfk knkdtaeqvg kegrsgqrnv mevfreeeed
      241 sfsgdfkekl qlsaeedgsv hhesilnrpg lgsivfrrnr isspedisds krefgfklps
      301 ellqrqgase adegaadeeg eenglkddlp wdddevewee dvvdatplev fllsqhleef
      361 lpifkreqid lealllcsde dlqsiqmqlg prkkvlnain rrkqvlqqpg qlvdtsl
//
LOCUS       NP_000331                524 aa            linear   PRI 27-APR-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 2
            isoform 1 [Homo sapiens].
ACCESSION   NP_000331
VERSION     NP_000331.1
DBSOURCE    REFSEQ: accession NM_000340.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Fu,H., Vuononvirta,J., Fanti,S., Bonacina,F., D'Amati,A., Wang,G.,
            Poobalasingam,T., Fankhaenel,M., Lucchesi,D., Coleby,R.,
            Tarussio,D., Thorens,B., Hearnden,R.J., Longhi,M.P., Grevitt,P.,
            Sheikh,M.H., Solito,E., Godinho,S.A., Bombardieri,M., Smith,D.M.,
            Cooper,D., Iqbal,A.J., Rathmell,J.C., Schaefer,S., Morales,V.,
            Bianchi,K., Norata,G.D. and Marelli-Berg,F.M.
  TITLE     The glucose transporter 2 regulates CD8+ T cell function via
            environment sensing
  JOURNAL   Nat Metab 5 (11), 1969-1985 (2023)
   PUBMED   37884694
  REMARK    GeneRIF: The glucose transporter 2 regulates CD8[+] T cell function
            via environment sensing.
            Erratum:[Nat Metab. 2025 Mar;7(3):634. doi:
            10.1038/s42255-025-01256-3. PMID: 40000839]
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Liu,L., Ma,F., Liu,Q., Yu,X. and Zeng,X.
  TITLE     Association Between the SLC2A2 Gene rs1499821 Polymorphism and
            Caries Susceptibility
  JOURNAL   Genet Test Mol Biomarkers 27 (5), 149-156 (2023)
   PUBMED   37257183
  REMARK    GeneRIF: Association Between the SLC2A2 Gene rs1499821 Polymorphism
            and Caries Susceptibility.
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Chen,H., Zhang,X., Liao,N., Ji,Y., Mi,L., Gan,Y., Su,Y. and Wen,F.
  TITLE     Decreased expression of Glucagon-like peptide-1 receptor and
            Sodium-glucose co-transporter 2 in patients with proliferative
            diabetic retinopathy
  JOURNAL   Front Endocrinol (Lausanne) 13, 1020252 (2022)
   PUBMED   36465606
  REMARK    GeneRIF: Decreased expression of Glucagon-like peptide-1 receptor
            and Sodium-glucose co-transporter 2 in patients with proliferative
            diabetic retinopathy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Grunert,S.C., Schumann,A., Baronio,F., Tsiakas,K., Murko,S.,
            Spiekerkoetter,U. and Santer,R.
  TITLE     Evidence for a Genotype-Phenotype Correlation in Patients with
            Pathogenic GLUT2 (SLC2A2) Variants
  JOURNAL   Genes (Basel) 12 (11), 1785 (2021)
   PUBMED   34828390
  REMARK    GeneRIF: Evidence for a Genotype-Phenotype Correlation in Patients
            with Pathogenic GLUT2 (SLC2A2) Variants.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Ban,N., Yamada,Y., Someya,Y., Miyawaki,K., Ihara,Y., Hosokawa,M.,
            Toyokuni,S., Tsuda,K. and Seino,Y.
  TITLE     Hepatocyte nuclear factor-1alpha recruits the transcriptional
            co-activator p300 on the GLUT2 gene promoter
  JOURNAL   Diabetes 51 (5), 1409-1418 (2002)
   PUBMED   11978637
  REMARK    GeneRIF: Hepatocyte nuclear factor-1alpha recruits the
            transcriptional co-activator p300 on the GLUT2 gene promoter.
REFERENCE   6  (residues 1 to 524)
  AUTHORS   De Leon,D.D. and Pinney,S.E.
  TITLE     Permanent Neonatal Diabetes Mellitus
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301620
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Patel,P., Lo,Y.M., Bell,G.I., Turner,R.C. and Wainscoat,J.S.
  TITLE     Dinucleotide repeat polymorphism at the human GLUT2 locus
  JOURNAL   Nucleic Acids Res 19 (14), 4017 (1991)
   PUBMED   1862003
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Froguel,P., Zouali,H., Sun,F., Velho,G., Fukumoto,H., Passa,P. and
            Cohen,D.
  TITLE     CA repeat polymorphism in the glucose transporter GLUT 2 gene
  JOURNAL   Nucleic Acids Res 19 (13), 3754 (1991)
   PUBMED   1852621
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Fukumoto,H., Kayano,T., Buse,J.B., Edwards,Y., Pilch,P.F.,
            Bell,G.I. and Seino,S.
  TITLE     Cloning and characterization of the major insulin-responsive
            glucose transporter expressed in human skeletal muscle and other
            insulin-responsive tissues
  JOURNAL   J Biol Chem 264 (14), 7776-7779 (1989)
   PUBMED   2656669
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Fukumoto,H., Seino,S., Imura,H., Seino,Y., Eddy,R.L., Fukushima,Y.,
            Byers,M.G., Shows,T.B. and Bell,G.I.
  TITLE     Sequence, tissue distribution, and chromosomal localization of mRNA
            encoding a human glucose transporter-like protein
  JOURNAL   Proc Natl Acad Sci U S A 85 (15), 5434-5438 (1988)
   PUBMED   3399500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092918.6, J03810.1 and
            AC061708.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an integral plasma membrane glycoprotein
            of the liver, islet beta cells, intestine, and kidney epithelium.
            The encoded protein mediates facilitated bidirectional glucose
            transport. Because of its low affinity for glucose, it has been
            suggested as a glucose sensor. Mutations in this gene are
            associated with susceptibility to diseases, including
            Fanconi-Bickel syndrome and noninsulin-dependent diabetes mellitus
            (NIDDM). Alternative splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments and
            experimental data in the literature (PMID: 11978637).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313622.1, J03810.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000314251.8/ ENSP00000323568.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..524
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 2 isoform 1"
                     /note="glucose transporter type 2, liver; solute carrier
                     family 2 (facilitated glucose transporter), member 2"
                     /calculated_mol_wt=57359
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Region          12..490
                     /region_name="MFS_GLUT_Class1"
                     /note="Class 1 Glucose transporters (GLUTs) of the Major
                     Facilitator Superfamily; cd17431"
                     /db_xref="CDD:340989"
     Site            order(24,28,193,196..197,200,314..315,319..320,323,349,
                     411..412,416,420,443,447)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340989"
     Site            62
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11168.1)"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            128..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            188..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            304..324
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            339..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            369..389
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            401..421
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            434..454
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            462..482
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11168.1)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P11168.1)"
     CDS             1..524
                     /gene="SLC2A2"
                     /gene_synonym="GLUT2"
                     /coded_by="NM_000340.2:51..1625"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3215.1"
                     /db_xref="GeneID:6514"
                     /db_xref="HGNC:HGNC:11006"
                     /db_xref="MIM:138160"
ORIGIN      
        1 mtedkvtgtl vftvitavlg sfqfgydigv inapqqviis hyrhvlgvpl ddrkainnyv
       61 instdelpti sysmnpkptp waeeetvaaa qlitmlwsls vssfavggmt asffggwlgd
      121 tlgrikamlv anilslvgal lmgfsklgps hiliiagrsi sglycglisg lvpmyigeia
      181 ptalrgalgt fhqlaivtgi lisqiiglef ilgnydlwhi llglsgvrai lqslllffcp
      241 esprylyikl deevkakqsl krlrgyddvt kdinemrker eeasseqkvs iiqlftnssy
      301 rqpilvalml hvaqqfsgin gifyystsif qtagiskpvy atigvgavnm vftavsvflv
      361 ekagrrslfl igmsgmfvca ifmsvglvll nkfswmsyvs miaiflfvsf feigpgpipw
      421 fmvaeffsqg prpaalaiaa fsnwtcnfiv alcfqyiadf cgpyvfflfa gvllaftlft
      481 ffkvpetkgk sfeeiaaefq kksgsahrpk aavemkflga tetv
//
LOCUS       NP_001349359             242 aa            linear   ROD 27-APR-2025
DEFINITION  lysosomal membrane ascorbate-dependent ferrireductase CYB561A3
            isoform 1 [Mus musculus].
ACCESSION   NP_001349359 XP_017173639
VERSION     NP_001349359.1
DBSOURCE    REFSEQ: accession NM_001362430.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Zhang,D.L., Su,D., Berczi,A., Vargas,A. and Asard,H.
  TITLE     An ascorbate-reducible cytochrome b561 is localized in macrophage
            lysosomes
  JOURNAL   Biochim Biophys Acta 1760 (12), 1903-1913 (2006)
   PUBMED   16996694
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Su,D. and Asard,H.
  TITLE     Three mammalian cytochromes b561 are ascorbate-dependent
            ferrireductases
  JOURNAL   FEBS J 273 (16), 3722-3734 (2006)
   PUBMED   16911521
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125093.4.
            
            On May 3, 2018 this sequence version replaced XP_017173639.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.192970.1,
                                           SRR1660817.111582.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 6.6 cM"
     Protein         1..242
                     /product="lysosomal membrane ascorbate-dependent
                     ferrireductase CYB561A3 isoform 1"
                     /EC_number="7.2.1.3"
                     /note="cytochrome b ascorbate-dependent protein 3;
                     lysosomal cytochrome b; lysosomal membrane
                     ascorbate-dependent ferrireductase CYB561A3"
                     /calculated_mol_wt=26955
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     Region          10..188
                     /region_name="Cytochrome_b_N"
                     /note="Cytochrome b (N-terminus)/b6/petB: Cytochrome b is
                     a subunit of cytochrome bc1, an 11-subunit mitochondrial
                     respiratory enzyme. Cytochrome b spans the mitochondrial
                     membrane with 8 transmembrane helices (A-H) in eukaryotes.
                     In plants and cyanobacteria; cl23723"
                     /db_xref="CDD:474033"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     Site            order(47,83,117,156)
                     /site_type="other"
                     /note="putative heme binding sites [chemical binding]"
                     /db_xref="CDD:176489"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     Site            120..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     Site            155..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     Site            203..223
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1H1.1)"
     CDS             1..242
                     /gene="Cyb561a3"
                     /gene_synonym="2310004G04Rik; Cybasc3; Lcytb"
                     /coded_by="NM_001362430.1:1043..1771"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS29582.1"
                     /db_xref="GeneID:225912"
                     /db_xref="MGI:MGI:2686925"
ORIGIN      
        1 masgwfylsc mvlgslgsmc ilftaywmqy wrggfawdgt vlmfnwhpvl mvagmvvlyg
       61 aaslvyrlps swvgprlpwk vlhaalhlla ftctvvglia vfrfhnhsri ahlyslhswl
      121 gittvvlfac qwflgfavfl lpwasqwlrs llkplhvffg acilslsits visgineklf
      181 fvlknatkpy sslpgeavfa nstgllvvaf gllvlyvlla sswkrpdpga ltdrqpllhd
      241 re
//
LOCUS       NP_001355283             317 aa            linear   ROD 27-APR-2025
DEFINITION  N-lysine methyltransferase SETD6 isoform 2 [Mus musculus].
ACCESSION   NP_001355283
VERSION     NP_001355283.1
DBSOURCE    REFSEQ: accession NM_001368354.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Elsen,G.E., Bedogni,F., Hodge,R.D., Bammler,T.K., MacDonald,J.W.,
            Lindtner,S., Rubenstein,J.L.R. and Hevner,R.F.
  TITLE     The Epigenetic Factor Landscape of Developing Neocortex Is
            Regulated by Transcription Factors Pax6--> Tbr2--> Tbr1
  JOURNAL   Front Neurosci 12, 571 (2018)
   PUBMED   30186101
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Carmona-Mora,P., Widagdo,J., Tomasetig,F., Canales,C.P., Cha,Y.,
            Lee,W., Alshawaf,A., Dottori,M., Whan,R.M., Hardeman,E.C. and
            Palmer,S.J.
  TITLE     The nuclear localization pattern and interaction partners of
            GTF2IRD1 demonstrate a role in chromatin regulation
  JOURNAL   Hum Genet 134 (10), 1099-1115 (2015)
   PUBMED   26275350
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Binda,O., Sevilla,A., LeRoy,G., Lemischka,I.R., Garcia,B.A. and
            Richard,S.
  TITLE     SETD6 monomethylates H2AZ on lysine 7 and is required for the
            maintenance of embryonic stem cell self-renewal
  JOURNAL   Epigenetics 8 (2), 177-183 (2013)
   PUBMED   23324626
  REMARK    GeneRIF: SETD6 monomethylates H2AZ on lysine 7 and is required for
            the maintenance of embryonic stem cell self-renewal.
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113951.13.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3305798.1,
                                           SRR10662772.1873505.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 47.17 cM"
     Protein         1..317
                     /product="N-lysine methyltransferase SETD6 isoform 2"
                     /note="SET domain-containing protein 6; N-lysine
                     methyltransferase SETD6"
                     /calculated_mol_wt=36443
     Region          <1..146
                     /region_name="SET_SETD6"
                     /note="SET domain found in SET domain-containing protein 6
                     (SETD6) and similar proteins; cd19178"
                     /db_xref="CDD:380955"
     Site            order(64..69,92..96,104,127..130)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380955"
     Region          178..309
                     /region_name="Rubis-subs-bind"
                     /note="Rubisco LSMT substrate-binding; pfam09273"
                     /db_xref="CDD:462737"
     CDS             1..317
                     /gene="Setd6"
                     /gene_synonym="0610039J04Rik; 3110004G14Rik"
                     /coded_by="NM_001368354.1:186..1139"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:66083"
                     /db_xref="MGI:MGI:1913333"
ORIGIN      
        1 mfwpeeerlr llkgtgvpea vekdlvnirs eyysivlpfm eahsdlfsps vrslelyqql
       61 valvmaysfq epleedddek epnsplmvpa adilnhianh nanleysady lrmvatqpil
      121 egheifntyg qmanwqlihm ygfaepypnn tddtadiqmv tvrdaalqgt kdetekllvc
      181 erwdflckqe mvgeegafvi gceevlteee lattlkvlcm paeefrdyke ragwgeeete
      241 ddslaitdip klqeswkrll rnsvlltlqt yttdlktdqd llsnkeayat lswreqqalq
      301 vrygqkmilh rvleltn
//
LOCUS       NP_006764                670 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX18 [Homo sapiens].
ACCESSION   NP_006764
VERSION     NP_006764.3
DBSOURCE    REFSEQ: accession NM_006773.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Feng,B., Wang,X., Qiu,D., Sun,H., Deng,J., Tan,Y., Ji,K., Xu,S.,
            Zhang,S. and Tang,C.
  TITLE     DDX18 Facilitates the Tumorigenesis of Lung Adenocarcinoma by
            Promoting Cell Cycle Progression through the Upregulation of CDK4
  JOURNAL   Int J Mol Sci 25 (9), 4953 (2024)
   PUBMED   38732173
  REMARK    GeneRIF: DDX18 Facilitates the Tumorigenesis of Lung Adenocarcinoma
            by Promoting Cell Cycle Progression through the Upregulation of
            CDK4.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Guo,C., Liu,Z. and Zhang,H.
  TITLE     DNA 6mA demethylase ALKBH1 regulates DDX18 expression to promote
            proliferation of human head and neck squamous cell carcinoma
  JOURNAL   Cell Oncol (Dordr) 46 (4), 1097-1111 (2023)
   PUBMED   36976498
  REMARK    GeneRIF: DNA 6mA demethylase ALKBH1 regulates DDX18 expression to
            promote proliferation of human head and neck squamous cell
            carcinoma.
REFERENCE   3  (residues 1 to 670)
  AUTHORS   Redmond,A.M., Byrne,C., Bane,F.T., Brown,G.D., Tibbitts,P.,
            O'Brien,K., Hill,A.D., Carroll,J.S. and Young,L.S.
  TITLE     Genomic interaction between ER and HMGB2 identifies DDX18 as a
            novel driver of endocrine resistance in breast cancer cells
  JOURNAL   Oncogene 34 (29), 3871-3880 (2015)
   PUBMED   25284587
  REMARK    GeneRIF: Data show that odulation of RNA helicase DDX18 directly
            affects growth of tamoxifen-resistant cells, suggesting that it may
            be a critical downstream effector of the estrogen receptors (ERs)
            and high mobility group box 2 (HMGB2) complex.
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 670)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 670)
  AUTHORS   Dubaele,S. and Chene,P.
  TITLE     Cellular studies of MrDb (DDX18)
  JOURNAL   Oncol Res 16 (12), 549-556 (2007)
   PUBMED   18351129
  REMARK    GeneRIF: findings suggest that MrDb is important for cell
            proliferation and that its inhibition could prevent tumor cell
            proliferation.
REFERENCE   8  (residues 1 to 670)
  AUTHORS   Sekiguchi,T., Hayano,T., Yanagida,M., Takahashi,N. and Nishimoto,T.
  TITLE     NOP132 is required for proper nucleolus localization of DEAD-box
            RNA helicase DDX47
  JOURNAL   Nucleic Acids Res 34 (16), 4593-4608 (2006)
   PUBMED   16963496
REFERENCE   9  (residues 1 to 670)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
REFERENCE   10 (residues 1 to 670)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU599536.1, BC024739.1 and
            AK091227.1.
            
            On Nov 14, 2003 this sequence version replaced NP_006764.2.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. This gene encodes a DEAD box protein,
            and it is activated by Myc protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC024739.1, SRR1803613.252788.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263239.7/ ENSP00000263239.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.1"
     Protein         1..670
                     /product="ATP-dependent RNA helicase DDX18"
                     /EC_number="3.6.4.13"
                     /note="DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 18
                     (Myc-regulated); Myc-regulated DEAD box protein; DEAD box
                     protein 18; DEAD (Asp-Glu-Ala-Asp) box polypeptide 18;
                     Helicase Associated with Set1 homolog"
                     /calculated_mol_wt=75276
     Region          31..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVP1.2)"
     Region          179..207
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVP1.2)"
     Region          190..387
                     /region_name="DEADc_DDX18"
                     /note="DEAD-box helicase domain of DEAD box protein 18;
                     cd17942"
                     /db_xref="CDD:350700"
     Site            order(198..199,201..203,206,224..231)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350700"
     Region          333..336
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVP1.2)"
     Region          400..530
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(488,490,515,518..519)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     Region          562..619
                     /region_name="DUF4217"
                     /note="Domain of unknown function (DUF4217); pfam13959"
                     /db_xref="CDD:464056"
     CDS             1..670
                     /gene="DDX18"
                     /gene_synonym="Has1; MrDb"
                     /coded_by="NM_006773.4:88..2100"
                     /db_xref="CCDS:CCDS2120.1"
                     /db_xref="GeneID:8886"
                     /db_xref="HGNC:HGNC:2741"
                     /db_xref="MIM:606355"
ORIGIN      
        1 mshlpmkllr kkiekrnlkl rqrnlkfqga snltlsetqn gdvseetmgs rkvkkskqkp
       61 mnvglsetqn ggmsqeavgn ikvtkspqks tvltngeaam qssnseskkk kkkkrkmvnd
      121 aepdtkkakt enkgkseees aettketenn vekpdndede sevpslplgl tgafedtsfa
      181 slcnlvnent lkaikemgft nmteiqhksi rpllegrdll aaaktgsgkt laflipavel
      241 ivklrfmprn gtgvlilspt relamqtfgv lkelmthhvh tyglimggsn rsaeaqklgn
      301 giniivatpg rlldhmqntp gfmyknlqcl videadrild vgfeeelkqi ikllptrrqt
      361 mlfsatqtrk vedlarislk keplyvgvdd dkanatvdgl eqgyvvcpse krflllftfl
      421 kknrkkklmv ffsscmsvky hyellnyidl pvlaihgkqk qnkrtttffq fcnadsgtll
      481 ctdvaargld ipevdwivqy dppddpkeyi hrvgrtargl ngrghallil rpeelgflry
      541 lkqskvplse fdfswskisd iqsqleklie knyflhksaq eayksyiray dshslkqifn
      601 vnnlnlpqva lsfgfkvppf vdlnvnsneg kqkkrggggg fgyqktkkve kskifkhisk
      661 kssdsrqfsh
//
LOCUS       NP_060302                181 aa            linear   PRI 27-APR-2025
DEFINITION  protein Abitram isoform 1 [Homo sapiens].
ACCESSION   NP_060302
VERSION     NP_060302.1
DBSOURCE    REFSEQ: accession NM_017832.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Derlig,K., Ehrhardt,T., Giessl,A., Brandstatter,J.H., Enz,R. and
            Dahlhaus,R.
  TITLE     Simiate is an Actin binding protein involved in filopodia dynamics
            and arborization of neurons
  JOURNAL   Front Cell Neurosci 8, 99 (2014)
   PUBMED   24782708
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Derlig,K., Giessl,A., Brandstatter,J.H., Enz,R. and Dahlhaus,R.
  TITLE     Identification and characterisation of Simiate, a novel protein
            linked to the fragile X syndrome
  JOURNAL   PLoS One 8 (12), e83007 (2013)
   PUBMED   24349419
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Ahn,J., Chung,K.S., Kim,D.U., Won,M., Kim,L., Kim,K.S., Nam,M.,
            Choi,S.J., Kim,H.C., Yoon,M., Chae,S.K. and Hoe,K.L.
  TITLE     Systematic identification of hepatocellular proteins interacting
            with NS5A of the hepatitis C virus
  JOURNAL   J Biochem Mol Biol 37 (6), 741-748 (2004)
   PUBMED   15607035
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC015795.1 and AK000464.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.281482.1, BC015795.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322940.11/ ENSP00000363753.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..181
                     /product="protein Abitram isoform 1"
                     /note="protein FAM206A; protein Simiate; family with
                     sequence similarity 206 member A; protein Abitram"
                     /calculated_mol_wt=20247
     Region          <115..171
                     /region_name="Biotinyl_lipoyl_domains"
                     /note="Biotinyl_lipoyl_domains are present in
                     biotin-dependent carboxylases/decarboxylases, the
                     dihydrolipoyl acyltransferase component (E2) of 2-oxo acid
                     dehydrogenases, and the H-protein of the glycine cleavage
                     system (GCS). These domains transport CO2, acyl; cl11404"
                     /db_xref="CDD:448245"
     CDS             1..181
                     /gene="ABITRAM"
                     /gene_synonym="C9orf6; CG-8; FAM206A; Simiate"
                     /coded_by="NM_017832.4:88..633"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6774.1"
                     /db_xref="GeneID:54942"
                     /db_xref="HGNC:HGNC:1364"
                     /db_xref="MIM:620392"
ORIGIN      
        1 matepeaaep vvpslvdryf trwykpdvkg kfcedhcilq hsnricvitl aeshpvlqsg
       61 ktiksisyqi stncsrlqnk vsgkfkrgaq fltelaplck iycsdgeeyt vsscvrgrlm
      121 evnenilhkp silqekpste gyiavvlpkf eesksitegl ltqkqyeevm vkrinattat
      181 s
//
LOCUS       NP_061891                356 aa            linear   PRI 27-APR-2025
DEFINITION  inactive ubiquitin thioesterase OTULINL [Homo sapiens].
ACCESSION   NP_061891
VERSION     NP_061891.1
DBSOURCE    REFSEQ: accession NM_019018.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Taneera,J., Khalique,A., Salima,A., Mohammed,A.K., Sawan,A.S.,
            Aneis,H., Habib,P., Abdrabh,S., Elemam,N.M., Sharif-Askari,N.S.,
            Abu-Gharbieh,E., Saber-Ayad,M. and El-Huneidi,W.
  TITLE     Disrupting of family with sequence similarity 105, member A
            (Fam105a) deteriorates pancreatic beta-cell physiology and insulin
            secretion in INS-1 cells
  JOURNAL   Mol Cell Endocrinol 574, 111987 (2023)
   PUBMED   37311518
  REMARK    GeneRIF: Disrupting of family with sequence similarity 105, member
            A (Fam105a) deteriorates pancreatic beta-cell physiology and
            insulin secretion in INS-1 cells.
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Weinelt,N. and van Wijk,S.J.L.
  TITLE     Ubiquitin-dependent and -independent functions of OTULIN in cell
            fate control and beyond
  JOURNAL   Cell Death Differ 28 (2), 493-504 (2021)
   PUBMED   33288901
  REMARK    Review article
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Ceccarelli,D.F., Ivantsiv,S., Mullin,A.A., Coyaud,E., Manczyk,N.,
            Maisonneuve,P., Kurinov,I., Zhao,L., Go,C., Gingras,A.C.,
            Raught,B., Cordes,S. and Sicheri,F.
  TITLE     FAM105A/OTULINL Is a Pseudodeubiquitinase of the OTU-Class that
            Localizes to the ER Membrane
  JOURNAL   Structure 27 (6), 1000-1012 (2019)
   PUBMED   31056421
  REMARK    GeneRIF: The crystal structure of FAM105A/OTULINL indicated that
            the OTU domain possesses structural deficiencies in both active
            site and substrate-binding infrastructure predicted to impair
            normal deubiquitinase (DUB) function.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX342178.2, BC011524.1, AC010627.7 and AF052146.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.146705.1,
                                           SRR1803614.104134.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274217.4/ ENSP00000274217.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..356
                     /product="inactive ubiquitin thioesterase OTULINL"
                     /note="protein FAM105A; inactive ubiquitin thioesterase
                     FAM105A; family with sequence similarity 105 member A"
                     /calculated_mol_wt=42065
     Region          1..83
                     /region_name="Required for membrane binding.
                     /evidence=ECO:0000269|PubMed:31056421"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUU6.1)"
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUU6.1)"
     Region          95..355
                     /region_name="OTU_OTULL"
                     /note="OTU (ovarian tumor) domain of inactive ubiquitin
                     thioesterase Otulinl; cd22798"
                     /db_xref="CDD:438619"
     CDS             1..356
                     /gene="OTULINL"
                     /gene_synonym="FAM105A; NET20"
                     /coded_by="NM_019018.3:104..1174"
                     /db_xref="CCDS:CCDS3884.1"
                     /db_xref="GeneID:54491"
                     /db_xref="HGNC:HGNC:25629"
ORIGIN      
        1 maatrsptra rerersgapa agsdqvhswm latsqaldtv wrmakgfvml avsflvaaic
       61 yfrrlhlysg hklkwwigyl qrkfkrnlsv eaevdllsyc arewkgetpr nklmrkayee
      121 lfwrhhikcv rqvrrdnyda lrsvlfqifs qgisfpswmk ekdivklpek llfsqgcnwi
      181 qqysfgpeky tgsnvfgklr kyvellktqw tefngirdyh krgsmcntlf sdaileykly
      241 ealkfimlyq vtevyeqmkt kkvipslfrl lfsretssdp lsfmmnhlns vgdtcgleqi
      301 dmfilgysle vkikvfrlfk fnsrdfevcy peeplrdwpe islltendrh yhipvf
//
LOCUS       NP_001354466             429 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 30 [Homo sapiens].
ACCESSION   NP_001354466
VERSION     NP_001354466.1
DBSOURCE    REFSEQ: accession NM_001367537.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22 and AC022400.9.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..429
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 30"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=47699
     Region          <11..199
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          297..424
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..429
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367537.1:286..1575"
                     /note="isoform 30 is encoded by transcript variant 30"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mstsetskhr hcihqilesv nhihqhdivh rdlkpenlll askckgaavk ladfglaiev
       61 qgeqqawfgf agtpgylspe vlrkdpygkp vdiwacgvil yillvgyppf wdedqhklyq
      121 qikagaydfp spewdtvtpe aknlinqmlt inpakritad qalkhpwvcq rstvasmmhr
      181 qetveclrkf narrklkgai lttmlvsrnf saaksllnkk sdggvkepqt tvvhnatdgi
      241 kgstescntt tededlkaap lrtgngssvp egrssrdrta psagmqpqps lcssamrkqe
      301 iikiteqlie ainngdfeay tkicdpglts fepealgnlv egmdfhkfyf enllsknskp
      361 ihttilnphv hvigedaaci ayirltqyid gqgrprtsqs eetrvwhrrd gkwlnvhyhc
      421 sgapaaplq
//
LOCUS       NP_001352520             816 aa            linear   PRI 27-APR-2025
DEFINITION  neuroligin-4, Y-linked isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001352520 XP_016885524
VERSION     NP_001352520.1
DBSOURCE    REFSEQ: accession NM_001365591.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Nguyen,T.A., Wu,K., Pandey,S., Lehr,A.W., Li,Y., Bemben,M.A.,
            Badger,J.D. 2nd, Lauzon,J.L., Wang,T., Zaghloul,K.A., Thurm,A.,
            Jain,M., Lu,W. and Roche,K.W.
  TITLE     A Cluster of Autism-Associated Variants on X-Linked NLGN4X
            Functionally Resemble NLGN4Y
  JOURNAL   Neuron 106 (5), 759-768 (2020)
   PUBMED   32243781
  REMARK    GeneRIF: A Cluster of Autism-Associated Variants on X-Linked NLGN4X
            Functionally Resemble NLGN4Y.
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Bogaert,A.F., Skorska,M.N., Wang,C., Gabrie,J., MacNeil,A.J.,
            Hoffarth,M.R., VanderLaan,D.P., Zucker,K.J. and Blanchard,R.
  TITLE     Male homosexuality and maternal immune responsivity to the Y-linked
            protein NLGN4Y
  JOURNAL   Proc Natl Acad Sci U S A 115 (2), 302-306 (2018)
   PUBMED   29229842
  REMARK    GeneRIF: Results suggest an association between a maternal immune
            response to neuroligin 4 Y-linked (NLGN4Y) and subsequent sexual
            orientation in male offspring.
            Erratum:[Proc Natl Acad Sci U S A. 2022 Aug 23;119(34):e2212767119.
            doi: 10.1073/pnas.2212767119. PMID: 35981140]
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Gong,Y., Wang,L., Chippada-Venkata,U., Dai,X., Oh,W.K. and Zhu,J.
  TITLE     Constructing Bayesian networks by integrating gene expression and
            copy number data identifies NLGN4Y as a novel regulator of prostate
            cancer progression
  JOURNAL   Oncotarget 7 (42), 68688-68707 (2016)
   PUBMED   27626693
  REMARK    GeneRIF: Results suggest that NLGN4Y is an important negative
            regulator in prostate cancer progression.
REFERENCE   4  (residues 1 to 816)
  AUTHORS   Ross,J.L., Tartaglia,N., Merry,D.E., Dalva,M. and Zinn,A.R.
  TITLE     Behavioral phenotypes in males with XYY and possible role of
            increased NLGN4Y expression in autism features
  JOURNAL   Genes Brain Behav 14 (2), 137-144 (2015)
   PUBMED   25558953
  REMARK    GeneRIF: Expression of NLGN4Y, a gene that may be involved in
            synaptic function, is increased in boys with XYY
REFERENCE   5  (residues 1 to 816)
  AUTHORS   Dinamarca,M.C., Weinstein,D., Monasterio,O. and Inestrosa,N.C.
  TITLE     The synaptic protein neuroligin-1 interacts with the amyloid
            beta-peptide. Is there a role in Alzheimer's disease?
  JOURNAL   Biochemistry 50 (38), 8127-8137 (2011)
   PUBMED   21838267
REFERENCE   6  (residues 1 to 816)
  AUTHORS   Yamakawa,H., Oyama,S., Mitsuhashi,H., Sasagawa,N., Uchino,S.,
            Kohsaka,S. and Ishiura,S.
  TITLE     Neuroligins 3 and 4X interact with syntrophin-gamma2, and the
            interactions are affected by autism-related mutations
  JOURNAL   Biochem Biophys Res Commun 355 (1), 41-46 (2007)
   PUBMED   17292328
REFERENCE   7  (residues 1 to 816)
  AUTHORS   Ylisaukko-oja,T., Rehnstrom,K., Auranen,M., Vanhala,R., Alen,R.,
            Kempas,E., Ellonen,P., Turunen,J.A., Makkonen,I., Riikonen,R.,
            Nieminen-von Wendt,T., von Wendt,L., Peltonen,L. and Jarvela,I.
  TITLE     Analysis of four neuroligin genes as candidates for autism
  JOURNAL   Eur J Hum Genet 13 (12), 1285-1292 (2005)
   PUBMED   16077734
  REMARK    GeneRIF: Neuroligin mutations most probably represent rare causes
            of autism; it is unlikely that the allelic variants in any of these
            genes would be major risk factors for autism.
REFERENCE   8  (residues 1 to 816)
  AUTHORS   Skaletsky,H., Kuroda-Kawaguchi,T., Minx,P.J., Cordum,H.S.,
            Hillier,L., Brown,L.G., Repping,S., Pyntikova,T., Ali,J., Bieri,T.,
            Chinwalla,A., Delehaunty,A., Delehaunty,K., Du,H., Fewell,G.,
            Fulton,L., Fulton,R., Graves,T., Hou,S.F., Latrielle,P.,
            Leonard,S., Mardis,E., Maupin,R., McPherson,J., Miner,T., Nash,W.,
            Nguyen,C., Ozersky,P., Pepin,K., Rock,S., Rohlfing,T., Scott,K.,
            Schultz,B., Strong,C., Tin-Wollam,A., Yang,S.P., Waterston,R.H.,
            Wilson,R.K., Rozen,S. and Page,D.C.
  TITLE     The male-specific region of the human Y chromosome is a mosaic of
            discrete sequence classes
  JOURNAL   Nature 423 (6942), 825-837 (2003)
   PUBMED   12815422
REFERENCE   9  (residues 1 to 816)
  AUTHORS   Jamain,S., Quach,H., Betancur,C., Rastam,M., Colineaux,C.,
            Gillberg,I.C., Soderstrom,H., Giros,B., Leboyer,M., Gillberg,C. and
            Bourgeron,T.
  CONSRTM   Paris Autism Research International Sibpair Study
  TITLE     Mutations of the X-linked genes encoding neuroligins NLGN3 and
            NLGN4 are associated with autism
  JOURNAL   Nat Genet 34 (1), 27-29 (2003)
   PUBMED   12669065
REFERENCE   10 (residues 1 to 816)
  AUTHORS   Cantallops,I. and Cline,H.T.
  TITLE     Synapse formation: if it looks like a duck and quacks like a duck
            ...
  JOURNAL   Curr Biol 10 (17), R620-R623 (2000)
   PUBMED   10996085
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010726.4, AC010979.3,
            AC010879.2 and AC011903.4.
            
            On Sep 5, 2018 this sequence version replaced XP_016885524.1.
            
            Summary: This gene encodes a type I membrane protein that belongs
            to the family of neuroligins, which are cell adhesion molecules
            present at the postsynaptic side of the synapse, and may be
            essential for the formation of functional synapses. Alternatively
            spliced transcript variants have been found for this gene.[provided
            by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.199279.1,
                                           SRR1803615.276657.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..816
                     /product="neuroligin-4, Y-linked isoform 1 precursor"
                     /note="alternative HNL4Y"
                     /calculated_mol_wt=87194
     sig_peptide     1..43
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ3.1)"
                     /calculated_mol_wt=4845
     mat_peptide     44..816
                     /product="Neuroligin-4, Y-linked. /id=PRO_0000008649"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ3.1)"
                     /calculated_mol_wt=87194
     Region          44..590
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     Site            order(174..176,253..255,258,399,405..406,444,490,493)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(254,375,489)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Region          359..364
                     /region_name="Interaction with NRXN1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     Site            511
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     Region          636..659
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     Site            677..697
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     Site            712
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62889; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ3.1)"
     CDS             1..816
                     /gene="NLGN4Y"
                     /gene_synonym="HNL4Y"
                     /coded_by="NM_001365591.1:438..2888"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 10"
                     /db_xref="CCDS:CCDS14788.1"
                     /db_xref="GeneID:22829"
                     /db_xref="HGNC:HGNC:15529"
                     /db_xref="MIM:400028"
ORIGIN      
        1 mlrpqgllwl pllftsvcvm lnsnvllwit alaikftlid sqaqypvvnt nygkiqglrt
       61 plpseilgpv eqylgvpyas pptgerrfqp pespsswtgi rnatqfsavc pqhlderfll
      121 hdmlpiwftt sldtlmtyvq dqnedclyln iyvpmeddih eqnskkpvmv yihggsymeg
      181 tgnmidgsil asygnvivit inyrlgilgf lstgdqaakg nyglldqiqa lrwieenvga
      241 fggdpkrvti fgsgagascv slltlshyse glfqkaiiqs gtalsswavn yqpakytril
      301 adkvgcnmld ttdmveclkn knykeliqqt itpatyhiaf gpvidgdvip ddpqilmeqg
      361 eflnydimlg vnqgeglkfv dgivdnedgv tpndfdfsvs nfvdnlygyp egkdtlreti
      421 kfmytdwadk enpetrrktl valftdhqwv apavatadlh aqygsptyfy afyhhcqsem
      481 kpswadsahg devpyvfgip migptelfsc nfskndvmls avvmtywtnf aktgdpnqpv
      541 pqdtkfihtk pnrfeevaws kynpkdqlyl higlkprvrd hyratkvafw lelvphlhnl
      601 neifqyvstt tkvpppdmts fpygtrrspa kiwpttkrpa itpannpkhs kdphktgped
      661 ttvlietkrd ystelsvtia vgasllflni lafaalyykk dkrrhethrh pspqrnttnd
      721 ithiqneeim slqmkqlehd heceslqahd tlrltcppdy tltlrrspdd ipfmtpntit
      781 mipntlmgmq plhtfktfsg gqnstnlphg hsttrv
//
LOCUS       NP_001092764             199 aa            linear   PRI 27-APR-2025
DEFINITION  protein shisa-like-1 precursor [Homo sapiens].
ACCESSION   NP_001092764 XP_376018
VERSION     NP_001092764.1
DBSOURCE    REFSEQ: accession NM_001099294.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     Unexpected diversity in Shisa-like proteins suggests the importance
            of their roles as transmembrane adaptors
  JOURNAL   Cell Signal 24 (3), 758-769 (2012)
   PUBMED   22120523
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Hirosawa,M., Nagase,T., Murahashi,Y., Kikuno,R. and Ohara,O.
  TITLE     Identification of novel transcribed sequences on human chromosome
            22 by expressed sequence tag mapping
  JOURNAL   DNA Res 8 (1), 1-9 (2001)
   PUBMED   11258795
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL671760.9, AL591914.3, AL022339.1 and AL031595.4.
            
            On Jun 29, 2007 this sequence version replaced XP_376018.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR3476690.1153780.1, BC104183.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2155974 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381176.5/ ENSP00000370568.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..199
                     /product="protein shisa-like-1 precursor"
                     /note="protein shisa-like-1"
                     /calculated_mol_wt=19962
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2629
     mat_peptide     26..199
                     /product="Protein shisa-like-1. /id=PRO_0000318951"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SXP7.2)"
                     /calculated_mol_wt=19962
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3SXP7.2)"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3SXP7.2)"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SXP7.2)"
     Region          146..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SXP7.2)"
     CDS             1..199
                     /gene="SHISAL1"
                     /gene_synonym="KIAA1644"
                     /coded_by="NM_001099294.2:234..833"
                     /db_xref="CCDS:CCDS43025.1"
                     /db_xref="GeneID:85352"
                     /db_xref="HGNC:HGNC:29335"
                     /db_xref="MIM:620220"
ORIGIN      
        1 mtscgqqsln vlavlfsllf savlsahfrv cepytdhkgr yhfgfhcprl sdnktfilcc
       61 hhnntvfkyc cnetefqavm qanltasseg ymhnnytall gvwiygffvl mllvldllyy
      121 samnydickv ylarwgiqgr wmkqdprrwg nparaprpgq rapqpqpppg plpqapqavh
      181 tlrgdahspp lmtfqsssa
//
LOCUS       NP_001346928              76 aa            linear   MAM 27-APR-2025
DEFINITION  cAMP-dependent protein kinase inhibitor alpha [Bos taurus].
ACCESSION   NP_001346928
VERSION     NP_001346928.1
DBSOURCE    REFSEQ: accession NM_001359999.1
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000014.1, EH141155.1, EV617339.1, EV614528.1 and EE913121.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DV934602.1, SRR5571255.21355.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03145412, SAMN03145418
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="14"
                     /map="14"
                     /breed="Hereford"
     Protein         1..76
                     /product="cAMP-dependent protein kinase inhibitor alpha"
                     /note="PKI-alpha; protein kinase (cAMP-dependent,
                     catalytic) inhibitor alpha"
                     /calculated_mol_wt=7884
     Region          2..70
                     /region_name="PKI"
                     /note="cAMP-dependent protein kinase inhibitor; pfam02827"
                     /db_xref="CDD:460716"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0000250|UniProtKB:P61925; propagated from
                     UniProtKB/Swiss-Prot (Q3SX13.3)"
     Site            16
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q3SX13.3)"
     Site            19
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q3SX13.3)"
     Site            20
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q3SX13.3)"
     Region          49..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SX13.3)"
     CDS             1..76
                     /gene="PKIA"
                     /coded_by="NM_001359999.1:109..339"
                     /db_xref="BGD:BT29271"
                     /db_xref="GeneID:613524"
                     /db_xref="VGNC:VGNC:32940"
ORIGIN      
        1 mtdvettyad fiasgrtgrr naihdilvss asgnsnelal klagldinkt egeedaqrns
       61 teqsgeaqge aakses
//
LOCUS       NP_001355750            1584 aa            linear   ROD 27-APR-2025
DEFINITION  deleted in lung and esophageal cancer protein 1 homolog isoform 3
            [Mus musculus].
ACCESSION   NP_001355750 XP_006512220
VERSION     NP_001355750.1
DBSOURCE    REFSEQ: accession NM_001368821.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1584)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1584)
  AUTHORS   Okitsu,Y., Nagano,M., Yamagata,T., Ito,C., Toshimori,K., Dohra,H.,
            Fujii,W. and Yogo,K.
  TITLE     Dlec1 is required for spermatogenesis and male fertility in mice
  JOURNAL   Sci Rep 10 (1), 18883 (2020)
   PUBMED   33144677
  REMARK    GeneRIF: Dlec1 is required for spermatogenesis and male fertility
            in mice.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1584)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   4  (residues 1 to 1584)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC055818.9.
            
            On Feb 28, 2019 this sequence version replaced XP_006512220.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC145277.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1584
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 71.32 cM"
     Protein         1..1584
                     /product="deleted in lung and esophageal cancer protein 1
                     homolog isoform 3"
                     /note="deleted in lung and esophageal cancer protein 1
                     homolog"
                     /calculated_mol_wt=176143
     CDS             1..1584
                     /gene="Dlec1"
                     /gene_synonym="D630005C06Rik"
                     /coded_by="NM_001368821.1:7..4761"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:320256"
                     /db_xref="MGI:MGI:2443671"
ORIGIN      
        1 mdseskeeqq ctassavmss letqflsvph qlesaslsws irkslhsstv lmddchfgfp
       61 trslragfha lpplpepqtl rlrpaslrtq eishllarvf rnlytaqvig ddlsdslika
      121 rgsedarhee fldqlqqara iykqrldeaa mlerhimqar ardiaeteht tkqsrlqvve
      181 tpvklppvkt afrwcldskl mrkhhliste dyytdpvpfc papkdkstlg cskltfsceq
      241 rflrkseldr eaeehcrqlt ecddfeytvd slgsiskake rttdsvktsr pknkkwmehl
      301 qvpqraldrr llasmenrnh flknprffpp ntphggksli vplskperra slnaepewsc
      361 tdapvflakp svgfftdyei gpvyemvial qnttstsrfl rvlppsspyf alglgmfpgk
      421 ggivapgmtc qyivqfipdc lgdfddfilv etqsphtlvi plqarrpppv ltlspvldcg
      481 hcliggvkit kficknvgfs vgkfcimpqk swpppsfrav attgfveqpp fgvmpsvfel
      541 apgyaillev lflptglgqa eetfiivcdn cqikevvvvg tgqlvaldli hisggknepd
      601 pgelkdltaq yfirfepenv qstakkqlii rnathvelaf hwqimkpnlq plmpgethss
      661 dsikchpdre tafsiipekg ileshsdqef ilsfspyklk cfhsvlqmvl eavpeplssg
      721 lenlgdysys vddmivleie vkglaepfqv llepyaliip genyigitvk kdfkmwnnsk
      781 spirymwgki shchiievep ctgviepnev gdfelnltgg vpgptsqdle ceikdspcpv
      841 vlhieasfkg paltidvpal qfgllrlgkk asisiqirnv sqlsavwhlk espvclaerd
      901 edvspfdiep fcgqllplge crvtitleas qcqrlqtvle levengsgsy lpvyaevqqp
      961 hvylknshle fsnlylgvst ksrttlvngt llptrfhwgk llgpqadlct mtvsptqgll
     1021 gpseelqltl eltthteekl tnlvllchvs gmekplvlgi sgkplglqvt isivesdgst
     1081 tsttqeelrl dfgskvplrt pvirhiiltn cspiqtpftl tleyfgssqd slykktsvpd
     1141 vppallktar iqqhvakker ldfvesmlsh rkgaaflphi sqgmlgayqe lciditgcan
     1201 mwgeywdell cvvgdlpvtv ipvymavvgc pisslrntcy svapfqkepi trfgtqisgg
     1261 dtvtrslrly nsshcdirld wetyipeeka drllellvfy gppfplrdqd gseivcpets
     1321 easlpgspcp snvsvsshtv pstgscsggg ggtraeeqim svilqrheav paghiyrisp
     1381 kqlvipagdh rtiyisftpt vldpgvmhkv gytgyalgfm sldketdrqi pgrmrrlqdf
     1441 avsplrldln ghvrhaqlhv eldssgylef wcqasdlipq npcsgvlsdr ittrhlkltn
     1501 tteilydfqa rvsrpffisq ggaswdsrap hqceegtast gqwlmirpqd nmlvsagver
     1561 lphhprlyrq htgtscphlg tryk
//
LOCUS       NP_055091                517 aa            linear   PRI 27-APR-2025
DEFINITION  recombining binding protein suppressor of hairless-like protein
            isoform 1 [Homo sapiens].
ACCESSION   NP_055091
VERSION     NP_055091.2
DBSOURCE    REFSEQ: accession NM_014276.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Nair,A.K., Sutherland,J.R., Traurig,M., Piaggi,P., Chen,P.,
            Kobes,S., Hanson,R.L., Bogardus,C. and Baier,L.J.
  TITLE     Functional and association analysis of an Amerindian-derived
            population-specific p.(Thr280Met) variant in RBPJL, a component of
            the PTF1 complex
  JOURNAL   Eur J Hum Genet 26 (2), 238-246 (2018)
   PUBMED   29302047
  REMARK    GeneRIF: Amerindian-derived population-specific Thr280Met variant
            may modify risk of diabetes mellitus by regulating exocrine enzyme
            expression.
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Beres,T.M., Masui,T., Swift,G.H., Shi,L., Henke,R.M. and
            MacDonald,R.J.
  TITLE     PTF1 is an organ-specific and Notch-independent basic
            helix-loop-helix complex containing the mammalian Suppressor of
            Hairless (RBP-J) or its paralogue, RBP-L
  JOURNAL   Mol Cell Biol 26 (1), 117-130 (2006)
   PUBMED   16354684
  REMARK    GeneRIF: P48 interacts with the RBP-L and RBP-J subunits primarily
            through two short conserved tryptophan-containing motifs, similar
            to the motif of the Notch intracellular domain (NotchIC) that
            interacts with RBP-J.
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Tani,S., Taniwaki,M., Taniguchi,Y., Minoguchi,S., Kuroda,K.,
            Han,H., Aoki,T., Miyatake,S., Hashimoto,N. and Honjo,T.
  TITLE     Chromosomal mapping of two RBP-J-related genes: Kyo-T and RBP-L
  JOURNAL   J Hum Genet 44 (1), 73-75 (1999)
   PUBMED   9929984
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Minoguchi,S., Taniguchi,Y., Kato,H., Okazaki,T., Strobl,L.J.,
            Zimber-Strobl,U., Bornkamm,G.W. and Honjo,T.
  TITLE     RBP-L, a transcription factor related to RBP-Jkappa
  JOURNAL   Mol Cell Biol 17 (5), 2679-2687 (1997)
   PUBMED   9111338
  REMARK    GeneRIF: In mouse, there is cooperative transcriptional activity of
            RBP-L with EBNA-2.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL021578.4, DA045470.1,
            CA950939.1, AB024964.1 and BC030213.1.
            
            On Sep 11, 2003 this sequence version replaced NP_055091.1.
            
            Summary: This gene encodes a member of the suppressor of hairless
            protein family. A similar protein in mouse is a transcription
            factor that binds to DNA sequences almost identical to that bound
            by the Notch receptor signaling pathway transcription factor
            recombining binding protein J. The mouse protein has been shown to
            activate transcription in concert with Epstein-Barr virus nuclear
            antigen-2. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. There are no
            full-length human transcripts supporting this exon combination;
            inferred from partial human transcripts and full-length transcript
            support from the mouse ortholog (GeneID: 19668, AK131814.1).
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2151405,
                              SAMEA2153347 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000343694.8/ ENSP00000341243.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..517
                     /product="recombining binding protein suppressor of
                     hairless-like protein isoform 1"
                     /note="recombining binding protein suppressor of
                     hairless-like protein; transcription factor RBP-L"
                     /calculated_mol_wt=56620
     Region          26..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBG7.3)"
     Region          69..206
                     /region_name="LAG1-DNAbind"
                     /note="LAG1, DNA binding; pfam09271"
                     /db_xref="CDD:462735"
     Region          78..88
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q06330"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBG7.3)"
     Region          193..198
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q06330"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBG7.3)"
     Region          220..225
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q06330"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBG7.3)"
     Region          234..359
                     /region_name="BTD"
                     /note="Beta-trefoil DNA-binding domain; pfam09270"
                     /db_xref="CDD:462734"
     Region          381..477
                     /region_name="IPT_RBP-Jkappa"
                     /note="IPT domain of the recombination signal Jkappa
                     binding protein (RBP-Jkappa). RBP-J kappa, was initially
                     considered to be involved in V(D)J recombination because
                     of its DNA binding specificity and structural similarity
                     to site-specific recombinases known...; cd01176"
                     /db_xref="CDD:238581"
     CDS             1..517
                     /gene="RBPJL"
                     /gene_synonym="RBPL; RBPSUHL; SUHL"
                     /coded_by="NM_014276.4:84..1637"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13349.1"
                     /db_xref="GeneID:11317"
                     /db_xref="HGNC:HGNC:13761"
                     /db_xref="MIM:616104"
ORIGIN      
        1 mdpagaadps vppnplthls lqdrsemqlq seadrrslpg twtrsspeht tilrggvrrc
       61 lqqqceqtvr ilhakvaqks ygnekrffcp ppcvylsgpg wrvkpgqdqa hqagetgptv
      121 cgymgldsas gsatetqkln feqqpdsref gcaktlyisd adkrkhfrlv lrlvlrggre
      181 lgtfhsrlik viskpsqkkq slkntdlcis sgskvslfnr lrsqtvstry lsvedgafva
      241 sarqwaaftl hladghsaqg dfppregyvr ygslvqlvct vtgitlppmi irkvakqcal
      301 ldvdepisql hkcafqfpgs ppggggtylc latekvvqfq aspcpkeanr allndsscwt
      361 iigtesvefs fstslactle pvtpvplist lelsgggdva tlelhgenfh aglkvwfgdv
      421 eaetmyrspr slvcvvpdva afcsdwrwlr apitipmslv radglfypsa fsftytpeys
      481 vrpghpgvpe patdadalle sihqeftrtn fhlfiqt
//
LOCUS       NP_001004067            1222 aa            linear   PRI 27-APR-2025
DEFINITION  BOS complex subunit NOMO3 precursor [Homo sapiens].
ACCESSION   NP_001004067
VERSION     NP_001004067.1
DBSOURCE    REFSEQ: accession NM_001004067.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1222)
  AUTHORS   Sundaram,A., Yamsek,M., Zhong,F., Hooda,Y., Hegde,R.S. and
            Keenan,R.J.
  TITLE     Substrate-driven assembly of a translocon for multipass membrane
            proteins
  JOURNAL   Nature 611 (7934), 167-172 (2022)
   PUBMED   36261522
REFERENCE   2  (residues 1 to 1222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1222)
  AUTHORS   McGilvray,P.T., Anghel,S.A., Sundaram,A., Zhong,F., Trnka,M.J.,
            Fuller,J.R., Hu,H., Burlingame,A.L. and Keenan,R.J.
  TITLE     An ER translocon for multi-pass membrane protein biogenesis
  JOURNAL   Elife 9, e56889 (2020)
   PUBMED   32820719
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1222)
  AUTHORS   Pfefferle,S., Schopf,J., Kogl,M., Friedel,C.C., Muller,M.A.,
            Carbajo-Lozoya,J., Stellberger,T., von Dall'Armi,E., Herzog,P.,
            Kallies,S., Niemeyer,D., Ditt,V., Kuri,T., Zust,R., Pumpor,K.,
            Hilgenfeld,R., Schwarz,F., Zimmer,R., Steffen,I., Weber,F.,
            Thiel,V., Herrler,G., Thiel,H.J., Schwegmann-Wessels,C.,
            Pohlmann,S., Haas,J., Drosten,C. and von Brunn,A.
  TITLE     The SARS-coronavirus-host interactome: identification of
            cyclophilins as target for pan-coronavirus inhibitors
  JOURNAL   PLoS Pathog 7 (10), e1002331 (2011)
   PUBMED   22046132
REFERENCE   5  (residues 1 to 1222)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   6  (residues 1 to 1222)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   7  (residues 1 to 1222)
  AUTHORS   Haffner,C., Frauli,M., Topp,S., Irmler,M., Hofmann,K., Regula,J.T.,
            Bally-Cuif,L. and Haass,C.
  TITLE     Nicalin and its binding partner Nomo are novel Nodal signaling
            antagonists
  JOURNAL   EMBO J 23 (15), 3041-3050 (2004)
   PUBMED   15257293
REFERENCE   8  (residues 1 to 1222)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
REFERENCE   9  (residues 1 to 1222)
  AUTHORS   van Soest,S., Swart,J., Tijmes,N., Sandkuijl,L.A., Rommers,J. and
            Bergen,A.A.
  TITLE     A locus for autosomal recessive pseudoxanthoma elasticum, with
            penetrance of vascular symptoms in carriers, maps to chromosome
            16p13.1
  JOURNAL   Genome Res 7 (8), 830-834 (1997)
   PUBMED   9267806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136624.3, DB461977.1,
            DR760717.1, CD653707.1, BC006531.2 and BQ948282.1.
            
            Summary: This gene encodes a protein originally thought to be
            related to the collagenase gene family. This gene is one of three
            highly similar genes in a duplicated region on the short arm of
            chromosome 16. These three genes encode closely related proteins
            that may have the same function. The protein encoded by one of
            these genes has been identified as part of a protein complex that
            participates in the Nodal signaling pathway during vertebrate
            development. Mutations in ABCC6, which is located nearby, rather
            than mutations in this gene are associated with pseudoxanthoma
            elasticum. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399336.9/ ENSP00000382274.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.11"
     Protein         1..1222
                     /product="BOS complex subunit NOMO3 precursor"
                     /note="pM5 protein, middle copy; pM5 protein 3; BOS
                     complex subunit NOMO3"
                     /calculated_mol_wt=131343
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2809
     mat_peptide     32..1222
                     /product="BOS complex subunit NOMO3. /id=PRO_0000021821"
                     /note="propagated from UniProtKB/Swiss-Prot (P69849.2)"
                     /calculated_mol_wt=131343
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P69849.2)"
     Region          102..>556
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
     Site            218
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P69849.2)"
     Site            618
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P69849.2)"
     Region          <811..>1011
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
     Site            1156..1176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P69849.2)"
     Region          1198..1222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P69849.2)"
     CDS             1..1222
                     /gene="NOMO3"
                     /gene_synonym="Nomo"
                     /coded_by="NM_001004067.4:140..3808"
                     /db_xref="CCDS:CCDS42123.1"
                     /db_xref="GeneID:408050"
                     /db_xref="HGNC:HGNC:25242"
                     /db_xref="MIM:609159"
ORIGIN      
        1 mlvgqgagpl gpavvtaavv lllsgvgpah gsedivvgcg gfvksdvein yslieiklyt
       61 khgtlkyqtd capnngyfmi plydkgdfil kiepplgwsf epttvelhvd gvsdictkgg
      121 dinfvftgfs vngkvlskgq plgpagvqvs lrntgteaki qstvtqpggk faffkvlpgd
      181 yeilathptw alkeasttvr vtnsnanaas plivagynvs gsvrsdgepm kgvkfllfss
      241 lvtkedvlgc nvspvpgfqp qdeslvylcy tvsredgsfs fyslpsggyt vipfyrgeri
      301 tfdvapsrld ftvehdslki epvfhvmgfs vtgrvlngpe gdgvpeavvt lnnqikvktk
      361 adgsfrleni ttgtytihaq kehlyfetvt ikiapntpql adivatgfsv cgqisiirfp
      421 dtvkqmnkyk vvlssqdkdk slvtvetdah gsfcfkanpg tykvqvmvpe aetragltlk
      481 pqtfpltvtd rpvmdvafvq flasvsgkvs cldtcgdllv tlqslsrqge krslqlsgkv
      541 namtftfdnv lpgkykisim hedwcwknks levevleddv savefrqtgy mlrcslshai
      601 tlefyqdgng renvgiynls kgvnrfclsk pgvykvtprs chrfeqafyt ydtsspsilt
      661 ltairhhvlg tittdkmmdv tvtikssids epalvlgplk svqelrreqq laeiearrqe
      721 rekngneege ermtkppvqe mvdelqgpfs ydfsywarsg ekitvtpssk ellfyppsme
      781 avvsgescpg klieihgkag lflegqihpe legveivise kgassplitv ftddkgaysv
      841 gplhsdleyt vtsqkegyvl tavegtigdf kayalagvsf eikaeddqpl pgvllslsgg
      901 lfrsnlltqd ngiltfsnls pgqyyfkpmm kefrfepssq mievqegqnl kititgyrta
      961 yscygtvssl ngepeqgvam eavgqndcsi ygedtvtdee gkfrlrgllp gcvyhvqlka
     1021 egndhieral phhrvievgn ndiddvniiv frqinqfdls gnvitsseyl ptlwvklyks
     1081 enldnpiqtv slgqslffhf ppllrdgeny vvlldstlpr sqydyilpqv sftavgyhkh
     1141 itlifnptrk lpeqdiaqgs yialpltllv llagynhdkl iplllqltsr lqgvgalgqa
     1201 asdnsgpeda krqakkqktr rt
//
LOCUS       NP_689539                317 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 9 [Homo sapiens].
ACCESSION   NP_689539
VERSION     NP_689539.1
DBSOURCE    REFSEQ: accession NM_152326.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Hayward,D., Kouznetsova,V.L., Pierson,H.E., Hasan,N.M.,
            Guzman,E.R., Tsigelny,I.F. and Lutsenko,S.
  TITLE     ANKRD9 is a metabolically-controlled regulator of IMPDH2 abundance
            and macro-assembly
  JOURNAL   J Biol Chem 294 (39), 14454-14466 (2019)
   PUBMED   31337707
  REMARK    GeneRIF: ANKRD9 regulates IMPDH2 abundance and macro-assembly in
            response to metabolic changes.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Lee,Y., Lim,B., Lee,S.W., Lee,W.R., Kim,Y.I., Kim,M., Ju,H.,
            Kim,M.Y., Kang,S.J., Song,J.J., Lee,J.E. and Kang,C.
  TITLE     ANKRD9 is associated with tumor suppression as a substrate receptor
            subunit of ubiquitin ligase
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1864 (10), 3145-3153 (2018)
   PUBMED   30293565
  REMARK    GeneRIF: show that ANKRD9 is genetically and functionally
            associated with tumor suppression by acting as a substrate receptor
            subunit of a CUL5-based E3 ubiquitin ligase that ubiquitinates
            substrate proteins as IMPDH2 and presumably IMPDH1, marking them
            for proteasomal degradation and turnover. Furthermore, ANKRD9
            accomplishes its anti-proliferative and tumor-suppressive function
            via IMPDH2 degradation.
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Arking,D.E., Pulit,S.L., Crotti,L., van der Harst,P., Munroe,P.B.,
            Koopmann,T.T., Sotoodehnia,N., Rossin,E.J., Morley,M., Wang,X.,
            Johnson,A.D., Lundby,A., Gudbjartsson,D.F., Noseworthy,P.A.,
            Eijgelsheim,M., Bradford,Y., Tarasov,K.V., Dorr,M.,
            Muller-Nurasyid,M., Lahtinen,A.M., Nolte,I.M., Smith,A.V.,
            Bis,J.C., Isaacs,A., Newhouse,S.J., Evans,D.S., Post,W.S.,
            Waggott,D., Lyytikainen,L.P., Hicks,A.A., Eisele,L., Ellinghaus,D.,
            Hayward,C., Navarro,P., Ulivi,S., Tanaka,T., Tester,D.J.,
            Chatel,S., Gustafsson,S., Kumari,M., Morris,R.W., Naluai,A.T.,
            Padmanabhan,S., Kluttig,A., Strohmer,B., Panayiotou,A.G.,
            Torres,M., Knoflach,M., Hubacek,J.A., Slowikowski,K.,
            Raychaudhuri,S., Kumar,R.D., Harris,T.B., Launer,L.J.,
            Shuldiner,A.R., Alonso,A., Bader,J.S., Ehret,G., Huang,H.,
            Kao,W.H., Strait,J.B., Macfarlane,P.W., Brown,M., Caulfield,M.J.,
            Samani,N.J., Kronenberg,F., Willeit,J., Smith,J.G., Greiser,K.H.,
            Meyer Zu Schwabedissen,H., Werdan,K., Carella,M., Zelante,L.,
            Heckbert,S.R., Psaty,B.M., Rotter,J.I., Kolcic,I., Polasek,O.,
            Wright,A.F., Griffin,M., Daly,M.J., Arnar,D.O., Holm,H.,
            Thorsteinsdottir,U., Denny,J.C., Roden,D.M., Zuvich,R.L.,
            Emilsson,V., Plump,A.S., Larson,M.G., O'Donnell,C.J., Yin,X.,
            Bobbo,M., D'Adamo,A.P., Iorio,A., Sinagra,G., Carracedo,A.,
            Cummings,S.R., Nalls,M.A., Jula,A., Kontula,K.K., Marjamaa,A.,
            Oikarinen,L., Perola,M., Porthan,K., Erbel,R., Hoffmann,P.,
            Jockel,K.H., Kalsch,H., Nothen,M.M., den Hoed,M., Loos,R.J.,
            Thelle,D.S., Gieger,C., Meitinger,T., Perz,S., Peters,A.,
            Prucha,H., Sinner,M.F., Waldenberger,M., de Boer,R.A., Franke,L.,
            van der Vleuten,P.A., Beckmann,B.M., Martens,E., Bardai,A.,
            Hofman,N., Wilde,A.A., Behr,E.R., Dalageorgou,C., Giudicessi,J.R.,
            Medeiros-Domingo,A., Barc,J., Kyndt,F., Probst,V., Ghidoni,A.,
            Insolia,R., Hamilton,R.M., Scherer,S.W., Brandimarto,J.,
            Margulies,K., Moravec,C.E., del Greco,M. F, Fuchsberger,C.,
            O'Connell,J.R., Lee,W.K., Watt,G.C., Campbell,H., Wild,S.H., El
            Mokhtari,N.E., Frey,N., Asselbergs,F.W., Mateo Leach,I., Navis,G.,
            van den Berg,M.P., van Veldhuisen,D.J., Kellis,M., Krijthe,B.P.,
            Franco,O.H., Hofman,A., Kors,J.A., Uitterlinden,A.G.,
            Witteman,J.C., Kedenko,L., Lamina,C., Oostra,B.A., Abecasis,G.R.,
            Lakatta,E.G., Mulas,A., Orru,M., Schlessinger,D., Uda,M.,
            Markus,M.R., Volker,U., Snieder,H., Spector,T.D., Arnlov,J.,
            Lind,L., Sundstrom,J., Syvanen,A.C., Kivimaki,M., Kahonen,M.,
            Mononen,N., Raitakari,O.T., Viikari,J.S., Adamkova,V., Kiechl,S.,
            Brion,M., Nicolaides,A.N., Paulweber,B., Haerting,J.,
            Dominiczak,A.F., Nyberg,F., Whincup,P.H., Hingorani,A.D.,
            Schott,J.J., Bezzina,C.R., Ingelsson,E., Ferrucci,L., Gasparini,P.,
            Wilson,J.F., Rudan,I., Franke,A., Muhleisen,T.W., Pramstaller,P.P.,
            Lehtimaki,T.J., Paterson,A.D., Parsa,A., Liu,Y., van Duijn,C.M.,
            Siscovick,D.S., Gudnason,V., Jamshidi,Y., Salomaa,V., Felix,S.B.,
            Sanna,S., Ritchie,M.D., Stricker,B.H., Stefansson,K., Boyer,L.A.,
            Cappola,T.P., Olsen,J.V., Lage,K., Schwartz,P.J., Kaab,S.,
            Chakravarti,A., Ackerman,M.J., Pfeufer,A., de Bakker,P.I. and
            Newton-Cheh,C.
  CONSRTM   CARe Consortium; COGENT Consortium; DCCT/EDIC; eMERGE Consortium;
            HRGEN Consortium
  TITLE     Genetic association study of QT interval highlights role for
            calcium signaling pathways in myocardial repolarization
  JOURNAL   Nat Genet 46 (8), 826-836 (2014)
   PUBMED   24952745
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Malinouski,M., Hasan,N.M., Zhang,Y., Seravalli,J., Lin,J.,
            Avanesov,A., Lutsenko,S. and Gladyshev,V.N.
  TITLE     Genome-wide RNAi ionomics screen reveals new genes and regulation
            of human trace element metabolism
  JOURNAL   Nat Commun 5, 3301 (2014)
   PUBMED   24522796
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX161460.1, AL136293.5 and AW138815.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All three variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX161460.1, BX354128.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2152474
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000286918.9/ ENSP00000286918.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.31"
     Protein         1..317
                     /product="ankyrin repeat domain-containing protein 9"
                     /calculated_mol_wt=34164
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BM1.1)"
     Region          71..100
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BM1.1)"
     Region          <75..207
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          109..110
                     /region_name="Important role in both nutrient sensing and
                     binding/regulation of IMPDH2.
                     /evidence=ECO:0000269|PubMed:31337707"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BM1.1)"
     Region          112..141
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BM1.1)"
     Region          158..189
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          158..187
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BM1.1)"
     CDS             1..317
                     /gene="ANKRD9"
                     /coded_by="NM_152326.4:583..1536"
                     /db_xref="CCDS:CCDS9973.1"
                     /db_xref="GeneID:122416"
                     /db_xref="HGNC:HGNC:20096"
                     /db_xref="MIM:618605"
ORIGIN      
        1 mpwdarrpgg gadggpeasg aarsraqkqc rkssfafyqa vrdllpvwll edmraseafh
       61 wdergraaay spseallyal vhdhqayahy llatfprral appsagfrcc aapgphvala
      121 vrynrvgilr rilrtlrdfp aeerarvldr rgcsrveggg tslhvacela rpeclflllg
      181 hgaspglrdg ggltplelll rqlgrdagat psaagapasa pgeprqrrll lldllalytp
      241 vgaagsarqe llgdrprwqr llgedkfqwl aglappslfa ramqvlvtai spgrfpeald
      301 elplppflqp ldltgkg
//
LOCUS       NP_001356728              88 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome c oxidase subunit 6B2 [Homo sapiens].
ACCESSION   NP_001356728
VERSION     NP_001356728.1
DBSOURCE    REFSEQ: accession NM_001369799.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Shen,M., Zhao,N., Deng,X. and Deng,M.
  TITLE     [High expression of COX6B2 in gastric cancer is associated with
            poor long-term prognosis and promotes cell proliferation and cell
            cycle progression by inhibiting p53 signaling]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 44 (2), 289-297 (2024)
   PUBMED   38501414
  REMARK    GeneRIF: [High expression of COX6B2 in gastric cancer is associated
            with poor long-term prognosis and promotes cell proliferation and
            cell cycle progression by inhibiting p53 signaling].
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Cheng,C.C., Wooten,J., Gibbs,Z.A., McGlynn,K., Mishra,P. and
            Whitehurst,A.W.
  TITLE     Sperm-specific COX6B2 enhances oxidative phosphorylation,
            proliferation, and survival in human lung adenocarcinoma
  JOURNAL   Elife 9, e58108 (2020)
   PUBMED   32990599
  REMARK    GeneRIF: Sperm-specific COX6B2 enhances oxidative phosphorylation,
            proliferation, and survival in human lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Huttemann,M., Jaradat,S. and Grossman,L.I.
  TITLE     Cytochrome c oxidase of mammals contains a testes-specific isoform
            of subunit VIb--the counterpart to testes-specific cytochrome c?
  JOURNAL   Mol Reprod Dev 66 (1), 8-16 (2003)
   PUBMED   12874793
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Taanman,J.W., Schrage,C., Ponne,N.J., Das,A.T., Bolhuis,P.A., de
            Vries,H. and Agsteribbe,E.
  TITLE     Isolation of cDNAs encoding subunit VIb of cytochrome c oxidase and
            steady-state levels of coxVIb mRNA in different tissues
  JOURNAL   Gene 93 (2), 285-291 (1990)
   PUBMED   2172092
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020922.9.
            
            Transcript Variant: This variant (3) differs in the 3' UTR compared
            to variant 1. All four variants encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: HY032431.1, DB450411.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2148093, SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..88
                     /product="cytochrome c oxidase subunit 6B2"
                     /note="cytochrome c oxidase subunit VIb, testes-specific;
                     cancer/testis antigen 59; COX VIb-2; cytochrome c oxidase
                     subunit VIb polypeptide 2 (testis)"
                     /calculated_mol_wt=10398
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YFQ2.1)"
     Region          10..87
                     /region_name="Cyt_c_Oxidase_VIb"
                     /note="Cytochrome c oxidase subunit VIb. Cytochrome c
                     oxidase (CcO), the terminal oxidase in the respiratory
                     chains of eukaryotes and most bacteria, is a multi-chain
                     transmembrane protein located in the inner membrane of
                     mitochondria and the cell membrane of...; cd00926"
                     /db_xref="CDD:238466"
     Site            order(14..17,26..29,61,64..70)
                     /site_type="other"
                     /note="Subunit VIb/II interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Site            26
                     /site_type="other"
                     /note="Subunit VIb/I interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Site            order(30,33,85)
                     /site_type="other"
                     /note="Subunit VIb/III interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Region          32..42
                     /region_name="Cx9C motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YFQ2.1)"
     Site            order(49,51..56)
                     /site_type="other"
                     /note="Subunit VIb/VIb interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Region          56..67
                     /region_name="Cx10C motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YFQ2.1)"
     Site            order(78,81..83)
                     /site_type="other"
                     /note="Subunit VIb/VIa interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     CDS             1..88
                     /gene="COX6B2"
                     /gene_synonym="COXVIB2; CT59"
                     /coded_by="NM_001369799.1:89..355"
                     /db_xref="CCDS:CCDS42630.1"
                     /db_xref="GeneID:125965"
                     /db_xref="HGNC:HGNC:24380"
                     /db_xref="MIM:618127"
ORIGIN      
        1 mldveaqepp kgkwstppfd prfpsqnqir ncyqnfldyh rclktrtrrg kstqpceyyf
       61 rvyhslcpis wveswneqik ngifagki
//
LOCUS       NP_001353516             805 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 20 [Homo
            sapiens].
ACCESSION   NP_001353516
VERSION     NP_001353516.1
DBSOURCE    REFSEQ: accession NM_001366587.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 805)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 805)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 805)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 805)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 805)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 805)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 805)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.231354.1,
                                           SRR1803617.52389.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..805
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 20"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=90455
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <38..126
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <507..>641
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..805
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366587.1:2344..4761"
                     /note="isoform 20 is encoded by transcript variant 25"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rtksrspspa pekkektpel pepsvkvkep
      121 svqeatstsd ilkvpkpepi pepkepspek nskkekekek trprsrsrsk srsrtrsrsp
      181 shtrprrrhr srsrsysprr rpsprrrpsp rrrtpprrmp ppprhrrsrs pvrrrrrssa
      241 slsgssssss ssrsrsppkk ppkrtssppr ktrrlspsas pprrrhrpsp patpppktrh
      301 sptpqqsnrt rksrvsvspg rtsgkvtkhk gtekrespsp apkprkvels eseedkggkm
      361 aaadsvqqrr qyrrqnqqss sdsgssssse derpkrshvk ngevgrrrrh spsrsaspsp
      421 rkrqketspr mqmgkrwqsp vtksgrrrrs psppptrrrr spspappprr rrtptppprr
      481 rtpsppprrr spsprryspp iqrryspspp pkrrtasppp ppkrraspsp ppkrrvshsp
      541 ppkqrsspvt krrspslssk hrkgsspsrs trearspqpn krhspsprpr apqtsssppp
      601 vrrgassspq rrqspspstr pirrvsrtpe pkkikkaasp spqsvrrvss srsvsgspep
      661 aakkppapps pvqsqspstn wspavpvkka ksptpspspp rnsdqegggk kkkkkkdkkh
      721 kkdkkhkkhk khkkekavaa aaaaavtpaa iaaatttlaq eepvaapepk keteseaedn
      781 lddlekhlre kalrsmrkaq vspqs
//
LOCUS       NP_079140                353 aa            linear   PRI 27-APR-2025
DEFINITION  rRNA methyltransferase 1, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_079140
VERSION     NP_079140.2
DBSOURCE    REFSEQ: accession NM_024864.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Rebelo-Guiomar,P., Pellegrino,S., Dent,K.C., Sas-Chen,A.,
            Miller-Fleming,L., Garone,C., Van Haute,L., Rogan,J.F., Dinan,A.,
            Firth,A.E., Andrews,B., Whitworth,A.J., Schwartz,S., Warren,A.J.
            and Minczuk,M.
  TITLE     A late-stage assembly checkpoint of the human mitochondrial
            ribosome large subunit
  JOURNAL   Nat Commun 13 (1), 929 (2022)
   PUBMED   35177605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Lee,K.W., Okot-Kotber,C., LaComb,J.F. and Bogenhagen,D.F.
  TITLE     Mitochondrial ribosomal RNA (rRNA) methyltransferase family members
            are positioned to modify nascent rRNA in foci near the
            mitochondrial DNA nucleoid
  JOURNAL   J Biol Chem 288 (43), 31386-31399 (2013)
   PUBMED   24036117
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC243732.3, CB137408.1 and BC009416.1.
            
            On Dec 18, 2003 this sequence version replaced NP_079140.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.119175.1,
                                           SRR1163658.151192.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000614766.5/
                                                  ENSP00000481559.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..353
                     /product="rRNA methyltransferase 1, mitochondrial
                     precursor"
                     /note="rRNA methyltransferase 1, mitochondrial;
                     mitochondrial large ribosomal RNA ribose methylase; 16S
                     rRNA [Gm1145] 2'-O-methyltransferase; 16S rRNA
                     (guanosine(1145)-2'-O)-methyltransferase; CTB-75G16.3;
                     mitochondrial rRNA methyltransferase 1 homolog"
                     /calculated_mol_wt=36384
     transit_peptide 1..20
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q6IN84.1)"
                     /calculated_mol_wt=2273
     mat_peptide     21..353
                     /product="rRNA methyltransferase 1, mitochondrial.
                     /id=PRO_0000273202"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN84.1)"
                     /calculated_mol_wt=36384
     Region          51..127
                     /region_name="SpoU_sub_bind"
                     /note="RNA 2'-O ribose methyltransferase substrate
                     binding; pfam08032"
                     /db_xref="CDD:429793"
     Region          146..303
                     /region_name="SpoU-like_MRM1"
                     /note="SAM-dependent rRNA methylase related to MRM1;
                     cd18105"
                     /db_xref="CDD:349978"
     Site            order(161,164..165,167..170,243..244,277..280,288..291,
                     294,297..298,301..302)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:349978"
     Site            order(224,226,256..259,262,276..277,279,289..290,292,295)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349978"
     Region          311..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN84.1)"
     CDS             1..353
                     /gene="MRM1"
                     /coded_by="NM_024864.5:229..1290"
                     /db_xref="CCDS:CCDS32631.1"
                     /db_xref="GeneID:79922"
                     /db_xref="HGNC:HGNC:26202"
                     /db_xref="MIM:618099"
ORIGIN      
        1 mallstvrga twgrlvtrhf shaarhgerp ggeelsrlll ddlvptsrle llfgmtpcll
       61 alqaarrsva rlllqagkag lqgkraellr maeardipvl rprrqkldtm cryqvhqgvc
      121 mevsplrprp wreageaspg ddpqqlwlvl dgiqdprnfg avlrsahflg vdkvitsrrn
      181 scpltpvvsk ssagamevmd vfstddltgf lqtkaqqgwl vagtvgcpst edpqsseipi
      241 mscleflwer ptllvlgneg sglsqevqas cqllltilpr rqlppglesl nvsvaagill
      301 hsicsqrkgf ptegerrqll qdpqepsars eglsmaqhpg lssgpekerq neg
//
LOCUS       NP_001017915            1189 aa            linear   PRI 27-APR-2025
DEFINITION  phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 isoform a
            [Homo sapiens].
ACCESSION   NP_001017915
VERSION     NP_001017915.1
DBSOURCE    REFSEQ: accession NM_001017915.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1189)
  AUTHORS   Lu,G., Liu,H., Wang,H., Tang,X., Luo,S., Du,M., Christiani,D.C. and
            Wei,Q.
  TITLE     Potentially functional variants of INPP5D and EXOSC3 in immunity B
            cell-related genes are associated with non-small cell lung cancer
            survival
  JOURNAL   Front Immunol 15, 1440454 (2024)
   PUBMED   39176091
  REMARK    GeneRIF: Potentially functional variants of INPP5D and EXOSC3 in
            immunity B cell-related genes are associated with non-small cell
            lung cancer survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1189)
  AUTHORS   Ramakrishnan,G.S., Berry,W.L., Pacherille,A., Kerr,W.G.,
            Chisholm,J.D., Pedicone,C. and Humphrey,M.B.
  TITLE     SHIP inhibition mediates select TREM2-induced microglial functions
  JOURNAL   Mol Immunol 170, 35-45 (2024)
   PUBMED   38613944
  REMARK    GeneRIF: SHIP inhibition mediates select TREM2-induced microglial
            functions.
REFERENCE   3  (residues 1 to 1189)
  AUTHORS   Bradshaw,W.J., Kennedy,E.C., Moreira,T., Smith,L.A., Chalk,R.,
            Katis,V.L., Benesch,J.L.P., Brennan,P.E., Murphy,E.J. and
            Gileadi,O.
  TITLE     Regulation of inositol 5-phosphatase activity by the C2 domain of
            SHIP1 and SHIP2
  JOURNAL   Structure 32 (4), 453-466 (2024)
   PUBMED   38309262
  REMARK    GeneRIF: Regulation of inositol 5-phosphatase activity by the C2
            domain of SHIP1 and SHIP2.
REFERENCE   4  (residues 1 to 1189)
  AUTHORS   Nalaskowski,M.M., Metzner,A., Brehm,M.A., Labiadh,S., Brauer,H.,
            Grabinski,N., Mayr,G.W. and Jucker,M.
  TITLE     The inositol 5-phosphatase SHIP1 is a nucleo-cytoplasmic shuttling
            protein and enzymatically active in cell nuclei
  JOURNAL   Cell Signal 24 (3), 621-628 (2012)
   PUBMED   21864674
  REMARK    GeneRIF: The identification of SHIP1 as a nuclear inositol 5
            phosphatase adds another member of the phosphoinositide and
            inositol modulating molecules to the emerging network of inositide
            signaling in the nucleus.
REFERENCE   5  (residues 1 to 1189)
  AUTHORS   Kerr,W.G.
  TITLE     Inhibitor and activator: dual functions for SHIP in immunity and
            cancer
  JOURNAL   Ann N Y Acad Sci 1217, 1-17 (2011)
   PUBMED   21155837
  REMARK    GeneRIF: This review summarizes how SHIP participates in normal
            immune physiology or the pathologies that result when SHIP is
            mutated. SHIP can have either inhibitory or activating roles in
            cell signaling.
            Review article
REFERENCE   6  (residues 1 to 1189)
  AUTHORS   Ware,M.D., Rosten,P., Damen,J.E., Liu,L., Humphries,R.K. and
            Krystal,G.
  TITLE     Cloning and characterization of human SHIP, the 145-kD inositol
            5-phosphatase that associates with SHC after cytokine stimulation
  JOURNAL   Blood 88 (8), 2833-2840 (1996)
   PUBMED   8874179
REFERENCE   7  (residues 1 to 1189)
  AUTHORS   Drayer,A.L., Pesesse,X., De Smedt,F., Woscholski,R., Parker,P. and
            Erneux,C.
  TITLE     Cloning and expression of a human placenta inositol
            1,3,4,5-tetrakisphosphate and phosphatidylinositol
            3,4,5-trisphosphate 5-phosphatase
  JOURNAL   Biochem Biophys Res Commun 225 (1), 243-249 (1996)
   PUBMED   8769125
REFERENCE   8  (residues 1 to 1189)
  AUTHORS   Lioubin,M.N., Algate,P.A., Tsai,S., Carlberg,K., Aebersold,A. and
            Rohrschneider,L.R.
  TITLE     p150Ship, a signal transduction molecule with inositol
            polyphosphate-5-phosphatase activity
  JOURNAL   Genes Dev 10 (9), 1084-1095 (1996)
   PUBMED   8654924
REFERENCE   9  (residues 1 to 1189)
  AUTHORS   Kavanaugh,W.M., Pot,D.A., Chin,S.M., Deuter-Reinhard,M.,
            Jefferson,A.B., Norris,F.A., Masiarz,F.R., Cousens,L.S.,
            Majerus,P.W. and Williams,L.T.
  TITLE     Multiple forms of an inositol polyphosphate 5-phosphatase form
            signaling complexes with Shc and Grb2
  JOURNAL   Curr Biol 6 (4), 438-445 (1996)
   PUBMED   8723348
REFERENCE   10 (residues 1 to 1189)
  AUTHORS   Damen,J.E., Liu,L., Rosten,P., Humphries,R.K., Jefferson,A.B.,
            Majerus,P.W. and Krystal,G.
  TITLE     The 145-kDa protein induced to associate with Shc by multiple
            cytokines is an inositol tetraphosphate and phosphatidylinositol
            3,4,5-triphosphate 5-phosphatase
  JOURNAL   Proc Natl Acad Sci U S A 93 (4), 1689-1693 (1996)
   PUBMED   8643691
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AW503130.1, U53470.1 and
            BC099920.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the inositol
            polyphosphate-5-phosphatase (INPP5) family and encodes a protein
            with an N-terminal SH2 domain, an inositol phosphatase domain, and
            two C-terminal protein interaction domains. Expression of this
            protein is restricted to hematopoietic cells where its movement
            from the cytosol to the plasma membrane is mediated by tyrosine
            phosphorylation. At the plasma membrane, the protein hydrolyzes the
            5' phosphate from phosphatidylinositol (3,4,5)-trisphosphate and
            inositol-1,3,4,5-tetrakisphosphate, thereby affecting multiple
            signaling pathways. The protein is also partly localized to the
            nucleus, where it may be involved in nuclear inositol phosphate
            signaling processes. Overall, the protein functions as a negative
            regulator of myeloid cell proliferation and survival. Mutations in
            this gene are associated with defects and cancers of the immune
            system. Deficiencies in the encoded protein, SHIP1, have been
            associated with Inflammatory Bowel Disease types such as Crohn's
            Disease and Ulcerative Colitis. Alternative splicing of this gene
            results in multiple transcript variants. [provided by RefSeq, Jul
            2020].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.38964.1, U84400.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000445964.6/ ENSP00000405338.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..1189
                     /product="phosphatidylinositol 3,4,5-trisphosphate
                     5-phosphatase 1 isoform a"
                     /EC_number="3.1.3.56"
                     /EC_number="3.1.3.36"
                     /EC_number="3.1.3.86"
                     /note="signaling inositol polyphosphate 5 phosphatase
                     SIP-145; inositol polyphosphate-5-phosphatase, 145kDa; SH2
                     domain-containing inositol 5'-phosphatase 1;
                     phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1;
                     signaling inositol polyphosphate phosphatase SHIP II;
                     phosphatidylinositol 4,5-bisphosphate 5-phosphatase"
                     /calculated_mol_wt=133162
     Region          1..102
                     /region_name="SH2_SHIP"
                     /note="Src homology 2 (SH2) domain found in SH2-containing
                     inositol-5'-phosphatase (SHIP) and SLAM-associated protein
                     (SAP); cd10343"
                     /db_xref="CDD:198206"
     Site            order(12,31,52,54)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198206"
     Site            order(52..53,65..66,71,74,90..92)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198206"
     Region          103..132
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92835.2)"
     Region          124..129
                     /region_name="SH3-binding 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92835.2)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ES52; propagated from
                     UniProtKB/Swiss-Prot (Q92835.2)"
     Region          404..710
                     /region_name="INPP5c_SHIP1-INPP5D"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of SH2 domain containing inositol
                     polyphosphate 5-phosphatase-1 and related proteins;
                     cd09100"
                     /db_xref="CDD:197334"
     Site            order(412,414,453,520..521,541,544..545,587,589,591,
                     644..645,667,673,700..701)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197334"
     Site            order(412,453,541,587,589,673,700..701)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197334"
     Site            order(453,520..521,541,544..545,591,644..645,667,700)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197334"
     Site            order(453,700)
                     /site_type="other"
                     /note="putative Mg binding site [ion binding]"
                     /db_xref="CDD:197334"
     Site            order(541,589,701)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197334"
     Region          870..906
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92835.2)"
     Region          899..>1127
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          912..915
                     /region_name="NPXY motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92835.2)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q92835.2)"
     Region          922..1189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92835.2)"
     Site            934
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ES52; propagated from
                     UniProtKB/Swiss-Prot (Q92835.2)"
     Site            944
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9ES52; propagated from
                     UniProtKB/Swiss-Prot (Q92835.2)"
     Site            960
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92835.2)"
     Site            963
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92835.2)"
     Region          969..974
                     /region_name="SH3-binding 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92835.2)"
     Site            971
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92835.2)"
     Region          1016..1030
                     /region_name="Interaction with DAB2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92835.2)"
     Region          1019..1022
                     /region_name="NPXY motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92835.2)"
     Site            1022
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9ES52; propagated from
                     UniProtKB/Swiss-Prot (Q92835.2)"
     Region          1040..1051
                     /region_name="SH3-binding 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92835.2)"
     CDS             1..1189
                     /gene="INPP5D"
                     /gene_synonym="hp51CN; p150Ship; SHIP; SHIP-1; SHIP1;
                     SIP-145"
                     /coded_by="NM_001017915.3:138..3707"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS74672.1"
                     /db_xref="GeneID:3635"
                     /db_xref="HGNC:HGNC:6079"
                     /db_xref="MIM:601582"
ORIGIN      
        1 mvpcwnhgni trskaeells rtgkdgsflv rasesisray alcvlyrncv ytyrilpned
       61 dkftvqaseg vsmrfftkld qliefykken mglvthlqyp vpleeedtgd dpeedtvesv
      121 vsppelpprn ipltasscea kevpfsnenp ratetsrpsl setlfqrlqs mdtsglpeeh
      181 lkaiqdylst qlaqdsefvk tgssslphlk klttllckel ygevirtlps leslqrlfdq
      241 qlspglrprp qvpgeanpin mvsklsqlts llssiedkvk allhegpesp hrpslippvt
      301 fevkaeslgi pqkmqlkvdv esgkliikks kdgsedkfys hkkilqliks qkflnklvil
      361 vetekekilr keyvfadskk regfcqllqq mknkhseqpe pdmitifigt wnmgnapppk
      421 kitswflskg qgktrddsad yiphdiyvig tqedplseke wleilkhslq eitsvtfktv
      481 aihtlwniri vvlakpehen rishictdnv ktgiantlgn kgavgvsfmf ngtslgfvns
      541 hltsgsekkl rrnqnymnil rflalgdkkl spfnithrft hlfwfgdlny rvdlptweae
      601 tiiqkikqqq yadllshdql lterreqkvf lhfeeeeitf aptyrferlt rdkyaytkqk
      661 atgmkynlps wcdrvlwksy plvhvvcqsy gstsdimtsd hspvfatfea gvtsqfvskn
      721 gpgtvdsqgq ieflrcyatl ktksqtkfyl efhssclesf vksqegenee gsegelvvkf
      781 getlpklkpi isdpeylldq hilisikssd sdesygegci alrleatetq lpiytplthh
      841 geltghfqge iklqtsqgkt reklydfvkt erdessgpkt lksltshdpm kqwevtsrap
      901 pcsgssitei inpnymgvgp fgppmplhvk qtlspdqqpt awsydqppkd splgpcrges
      961 pptppgqppi spkkflpsta nrglpprtqe srpsdlgkna gdtlpqedlp ltkpemfenp
     1021 lygslssfpk paprkdqesp kmprkepppc pepgilspsi vltkaqeadr gegpgkqvpa
     1081 prlrsftcss saegraaggd ksqgkpktpv ssqapvpakr pikpsrsein qqtpptptpr
     1141 pplpvkspav lhlqhskgrd yrdntelphh gkhrpeegpp gplgrtamq
//
LOCUS       NP_004410                384 aa            linear   PRI 27-APR-2025
DEFINITION  dual specificity protein phosphatase 5 [Homo sapiens].
ACCESSION   NP_004410
VERSION     NP_004410.3
DBSOURCE    REFSEQ: accession NM_004419.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Chen,P., Wang,J., Yao,Y., Qu,Y., Ji,M. and Hou,P.
  TITLE     Targeting DUSP5 suppresses malignant phenotypes of BRAF-mutant
            thyroid cancer cells and improves their response to sorafenib
  JOURNAL   Endocrine 85 (3), 1268-1277 (2024)
   PUBMED   38564084
  REMARK    GeneRIF: Targeting DUSP5 suppresses malignant phenotypes of
            BRAF-mutant thyroid cancer cells and improves their response to
            sorafenib.
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Song,G., Zhao,F., Ni,R., Deng,B., Chen,S., Hu,R., Zheng,J.,
            Peng,Y., Liu,H., Luo,Y., Zhou,Z., Huang,G. and Shen,W.
  TITLE     Epithelial cells derived exosomal miR-203a-3p facilitates stromal
            inflammation of type IIIA chronic prostatitis/chronic pelvic pain
            syndrome by targeting DUSP5 and increasing MCP-1 generation
  JOURNAL   J Nanobiotechnology 22 (1), 236 (2024)
   PUBMED   38724995
  REMARK    GeneRIF: Epithelial cells derived exosomal miR-203a-3p facilitates
            stromal inflammation of type IIIA chronic prostatitis/chronic
            pelvic pain syndrome by targeting DUSP5 and increasing MCP-1
            generation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Yang,Z., Huang,D., Meng,M., Wang,W., Feng,J., Fang,L., Chen,H. and
            Zou,S.
  TITLE     BAF53A drives colorectal cancer development by regulating
            DUSP5-mediated ERK phosphorylation
  JOURNAL   Cell Death Dis 13 (12), 1049 (2022)
   PUBMED   36526622
  REMARK    GeneRIF: BAF53A drives colorectal cancer development by regulating
            DUSP5-mediated ERK phosphorylation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Altan,Z. and Sahin,Y.
  TITLE     miR-203 suppresses pancreatic cancer cell proliferation and
            migration by modulating DUSP5 expression
  JOURNAL   Mol Cell Probes 66, 101866 (2022)
   PUBMED   36183924
  REMARK    GeneRIF: miR-203 suppresses pancreatic cancer cell proliferation
            and migration by modulating DUSP5 expression.
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Chen,H.D., Li,F., Chen,S., Zhong,Z.H., Gao,P.F. and Gao,W.Z.
  TITLE     METTL3-mediated N6-methyladenosine modification of DUSP5 mRNA
            promotes gallbladder-cancer progression
  JOURNAL   Cancer Gene Ther 29 (7), 1012-1020 (2022)
   PUBMED   34799724
  REMARK    GeneRIF: METTL3-mediated N6-methyladenosine modification of DUSP5
            mRNA promotes gallbladder-cancer progression.
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Ueda,K., Arakawa,H. and Nakamura,Y.
  TITLE     Dual-specificity phosphatase 5 (DUSP5) as a direct transcriptional
            target of tumor suppressor p53
  JOURNAL   Oncogene 22 (36), 5586-5591 (2003)
   PUBMED   12944906
  REMARK    GeneRIF: DUSP5 is a direct target of p53.
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Kwak,S.P. and Dixon,J.E.
  TITLE     Multiple dual specificity protein tyrosine phosphatases are
            expressed and regulated differentially in liver cell lines
  JOURNAL   J Biol Chem 270 (3), 1156-1160 (1995)
   PUBMED   7836374
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Ishibashi,T., Bottaro,D.P., Michieli,P., Kelley,C.A. and
            Aaronson,S.A.
  TITLE     A novel dual specificity phosphatase induced by serum stimulation
            and heat shock
  JOURNAL   J Biol Chem 269 (47), 29897-29902 (1994)
   PUBMED   7961985
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Martell,K.J., Kwak,S., Hakes,D.J., Dixon,J.E. and Trent,J.M.
  TITLE     Chromosomal localization of four human VH1-like protein-tyrosine
            phosphatases
  JOURNAL   Genomics 22 (2), 462-464 (1994)
   PUBMED   7806236
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF979291.1, CB991409.1,
            U15932.2, AL355512.22, BC062545.1 and BI495660.1.
            
            On Apr 22, 2005 this sequence version replaced NP_004410.2.
            
            Summary:  The protein encoded by this gene is a member of the dual
            specificity protein phosphatase subfamily.  These phosphatases
            inactivate their target kinases by dephosphorylating both the
            phosphoserine/threonine and phosphotyrosine residues.  They
            negatively regulate members of the mitogen-activated protein (MAP)
            kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated
            with cellular proliferation and differentiation.  Different members
            of the family of dual specificity phosphatases show distinct
            substrate specificities for various MAP kinases, different tissue
            distribution and subcellular localization, and different modes of
            inducibility of their expression by extracellular stimuli.  This
            gene product inactivates ERK1, is expressed in a variety of tissues
            with the highest levels in pancreas and brain, and is localized in
            the nucleus. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.419819.1, AB209823.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369583.4/ ENSP00000358596.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q25.2"
     Protein         1..384
                     /product="dual specificity protein phosphatase 5"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="serine/threonine specific protein phosphatase;
                     VH1-like phosphatase 3; dual specificity protein
                     phosphatase hVH3"
                     /calculated_mol_wt=41916
     Region          5..140
                     /region_name="DSP_MapKP"
                     /note="N-terminal regulatory rhodanese domain of dual
                     specificity phosphatases (DSP), such as Mapk Phosphatase.
                     This domain is believed to determine substrate specificity
                     by binding the substrate, such as ERK2, and activating the
                     C-terminal catalytic domain by...; cd01446"
                     /db_xref="CDD:238723"
     Site            52..54
                     /site_type="active"
                     /note="putative substrate binding residues [active]"
                     /db_xref="CDD:238723"
     Region          53..74
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16690.2)"
     Region          179..316
                     /region_name="DSP_DUSP5"
                     /note="dual specificity phosphatase domain of dual
                     specificity protein phosphatase 5; cd14639"
                     /db_xref="CDD:350487"
     CDS             1..384
                     /gene="DUSP5"
                     /gene_synonym="DUSP; HVH3"
                     /coded_by="NM_004419.4:216..1370"
                     /db_xref="CCDS:CCDS7566.1"
                     /db_xref="GeneID:1847"
                     /db_xref="HGNC:HGNC:3071"
                     /db_xref="MIM:603069"
ORIGIN      
        1 mkvtsldgrq lrkmlrkeaa arcvvldcrp ylafaasnvr gslnvnlnsv vlrrarggav
       61 saryvlpdea ararllqegg ggvaavvvld qgsrhwqklr eesaarvvlt sllaclpagp
      121 rvyflkggye tfyseypecc vdvkpisqek ieseralisq cgkpvvnvsy rpaydqggpv
      181 eilpflylgs ayhaskcefl anlhitalln vsrrtseaca thlhykwipv edshtadiss
      241 hfqeaidfid cvrekggkvl vhceagisrs pticmaylmk tkqfrlkeaf dyikqrrsmv
      301 spnfgfmgql lqyeseilps tpnpqppscq geaagsslig hlqtlspdmq gayctfpasv
      361 lapvpthstv selsrspvat atsc
//
LOCUS       NP_004955                482 aa            linear   PRI 27-APR-2025
DEFINITION  histone deacetylase 1 [Homo sapiens].
ACCESSION   NP_004955
VERSION     NP_004955.2
DBSOURCE    REFSEQ: accession NM_004964.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Chen,W., Chu,J., Miao,Y., Jiang,W., Wang,F., Zhang,N., Jin,J. and
            Cai,Y.
  TITLE     MOF-mediated acetylation of CDK9 promotes global transcription by
            modulating P-TEFb complex formation
  JOURNAL   FEBS J 291 (21), 4796-4812 (2024)
   PUBMED   39250546
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Kanojia,A., Roy,G., Madhubala,R. and Muthuswami,R.
  TITLE     Interplay between DOT1L and HDAC1 regulates Leishmania donovani
            infection in human THP-1 cells
  JOURNAL   Acta Trop 258, 107352 (2024)
   PUBMED   39103111
  REMARK    GeneRIF: Interplay between DOT1L and HDAC1 regulates Leishmania
            donovani infection in human THP-1 cells.
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Di Giorgio,E., Dalla,E., Tolotto,V., D'Este,F., Paluvai,H.,
            Ranzino,L. and Brancolini,C.
  TITLE     HDAC4 influences the DNA damage response and counteracts senescence
            by assembling with HDAC1/HDAC2 to control H2BK120 acetylation and
            homology-directed repair
  JOURNAL   Nucleic Acids Res 52 (14), 8218-8240 (2024)
   PUBMED   38874468
  REMARK    GeneRIF: HDAC4 influences the DNA damage response and counteracts
            senescence by assembling with HDAC1/HDAC2 to control H2BK120
            acetylation and homology-directed repair.
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Kong,Y., Jiang,R., Zhou,H., Ge,M., Lin,H., Wang,Y., Yao,R.,
            Wang,Q., Liang,X., Li,J. and Zhou,X.
  TITLE     PHF12 regulates HDAC1 to promote tumorigenesis via EGFR/AKT
            signaling pathway in non-small cell lung cancer
  JOURNAL   J Transl Med 22 (1), 689 (2024)
   PUBMED   39075515
  REMARK    GeneRIF: PHF12 regulates HDAC1 to promote tumorigenesis via
            EGFR/AKT signaling pathway in non-small cell lung cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Xiong,F., Wang,D., Xiong,W., Wang,X., Huang,W.H., Wu,G.H.,
            Liu,W.Z., Wang,Q., Chen,J.S., Kuai,Y.Y., Wang,B. and Chen,Y.J.
  TITLE     Unveiling the role of HP1alpha-HDAC1-STAT1 axis as a therapeutic
            target for HP1alpha-positive intrahepatic cholangiocarcinoma
  JOURNAL   J Exp Clin Cancer Res 43 (1), 152 (2024)
   PUBMED   38812060
  REMARK    GeneRIF: Unveiling the role of HP1alpha-HDAC1-STAT1 axis as a
            therapeutic target for HP1alpha-positive intrahepatic
            cholangiocarcinoma.
            Erratum:[J Exp Clin Cancer Res. 2024 Jul 5;43(1):186. doi:
            10.1186/s13046-024-03112-w. PMID: 38965576]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Taunton,J., Hassig,C.A. and Schreiber,S.L.
  TITLE     A mammalian histone deacetylase related to the yeast
            transcriptional regulator Rpd3p
  JOURNAL   Science 272 (5260), 408-411 (1996)
   PUBMED   8602529
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Wolffe,A.P.
  TITLE     Histone deacetylase: a regulator of transcription
  JOURNAL   Science 272 (5260), 371-372 (1996)
   PUBMED   8602525
  REMARK    Review article
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Furukawa,Y., Kawakami,T., Sudo,K., Inazawa,J., Matsumine,A.,
            Akiyama,T. and Nakamura,Y.
  TITLE     Isolation and mapping of a human gene (RPD3L1) that is homologous
            to RPD3, a transcription factor in Saccharomyces cerevisiae
  JOURNAL   Cytogenet Cell Genet 73 (1-2), 130-133 (1996)
   PUBMED   8646880
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Hijmans,E.M., Voorhoeve,P.M., Beijersbergen,R.L., van 't Veer,L.J.
            and Bernards,R.
  TITLE     E2F-5, a new E2F family member that interacts with p130 in vivo
  JOURNAL   Mol Cell Biol 15 (6), 3082-3089 (1995)
   PUBMED   7760804
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Margolis,D.M., Somasundaran,M. and Green,M.R.
  TITLE     Human transcription factor YY1 represses human immunodeficiency
            virus type 1 transcription and virion production
  JOURNAL   J Virol 68 (2), 905-910 (1994)
   PUBMED   8289393
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109945.15.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 26, 2001 this sequence version replaced NP_004955.1.
            
            Summary: Histone acetylation and deacetylation, catalyzed by
            multisubunit complexes, play a key role in the regulation of
            eukaryotic gene expression. The protein encoded by this gene
            belongs to the histone deacetylase/acuc/apha family and is a
            component of the histone deacetylase complex. It also interacts
            with retinoblastoma tumor-suppressor protein and this complex is a
            key element in the control of cell proliferation and
            differentiation. Together with metastasis-associated protein-2, it
            deacetylates p53 and modulates its effect on cell growth and
            apoptosis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.10339.1,
                                           SRR1803611.177301.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373548.8/ ENSP00000362649.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2-p35.1"
     Protein         1..482
                     /product="histone deacetylase 1"
                     /EC_number="3.5.1.98"
                     /note="reduced potassium dependency, yeast homolog-like 1;
                     protein deacetylase HDAC1; protein decrotonylase HDAC1;
                     protein deacylase HDAC1"
                     /calculated_mol_wt=54972
     Region          4..374
                     /region_name="HDAC1"
                     /note="Histone deacetylase 1 (HDAC1); cd10010"
                     /db_xref="CDD:212534"
     Region          9..321
                     /region_name="Histone deacetylase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13547.1)"
     Site            74
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Site            order(140..141,149..150,176,178,264,271,301,303)
                     /site_type="active"
                     /db_xref="CDD:212534"
     Site            220
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Region          390..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13547.1)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92769; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:11602581,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13547.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:11602581,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Site            432
                     /site_type="methylation"
                     /note="N6-methylated lysine, by EHMT2.
                     /evidence=ECO:0000269|PubMed:18438403; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     CDS             1..482
                     /gene="HDAC1"
                     /gene_synonym="GON-10; HD1; KDAC1; RPD3; RPD3L1"
                     /coded_by="NM_004964.3:88..1536"
                     /db_xref="CCDS:CCDS360.1"
                     /db_xref="GeneID:3065"
                     /db_xref="HGNC:HGNC:4852"
                     /db_xref="MIM:601241"
ORIGIN      
        1 maqtqgtrrk vcyyydgdvg nyyygqghpm kphrirmthn lllnyglyrk meiyrphkan
       61 aeemtkyhsd dyikflrsir pdnmseyskq mqrfnvgedc pvfdglfefc qlstggsvas
      121 avklnkqqtd iavnwagglh hakkseasgf cyvndivlai lellkyhqrv lyididihhg
      181 dgveeafytt drvmtvsfhk ygeyfpgtgd lrdigagkgk yyavnyplrd giddesyeai
      241 fkpvmskvme mfqpsavvlq cgsdslsgdr lgcfnltikg hakcvefvks fnlpmlmlgg
      301 ggytirnvar cwtyetaval dteipnelpy ndyfeyfgpd fklhispsnm tnqntneyle
      361 kikqrlfenl rmlphapgvq mqaipedaip eesgdededd pdkrisicss dkriaceeef
      421 sdseeegegg rknssnfkka krvktedeke kdpeekkevt eeektkeekp eakgvkeevk
      481 la
//
LOCUS       NP_004752                777 aa            linear   PRI 27-APR-2025
DEFINITION  ral guanine nucleotide dissociation stimulator-like 2 isoform 1
            [Homo sapiens].
ACCESSION   NP_004752
VERSION     NP_004752.1
DBSOURCE    REFSEQ: accession NM_004761.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   2  (residues 1 to 777)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   3  (residues 1 to 777)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 777)
  AUTHORS   Hershkovitz,D., Gross,Y., Nahum,S., Yehezkel,S., Sarig,O., Uitto,J.
            and Sprecher,E.
  TITLE     Functional characterization of SAMD9, a protein deficient in
            normophosphatemic familial tumoral calcinosis
  JOURNAL   J Invest Dermatol 131 (3), 662-669 (2011)
   PUBMED   21160498
  REMARK    GeneRIF: SAMD9, an IFN-gamma-responsive protein, interacts with
            RGL2 to diminish the expression of EGR1, a protein of direct
            relevance to the pathogenesis of ectopic calcification and
            inflammation.
REFERENCE   5  (residues 1 to 777)
  AUTHORS   Bandyopadhyay,S., Chiang,C.Y., Srivastava,J., Gersten,M., White,S.,
            Bell,R., Kurschner,C., Martin,C., Smoot,M., Sahasrabudhe,S.,
            Barber,D.L., Chanda,S.K. and Ideker,T.
  TITLE     A human MAP kinase interactome
  JOURNAL   Nat Methods 7 (10), 801-805 (2010)
   PUBMED   20936779
REFERENCE   6  (residues 1 to 777)
  AUTHORS   Ando,A., Kikuti,Y.Y., Abe,K., Shigenari,A., Kawata,H., Ikemura,T.,
            Kimura,M. and Inoko,H.
  TITLE     cDNA cloning, northern hybridization, and mapping analysis of a
            putative GDS-related protein gene at the centromeric ends of the
            human and mouse MHC regions
  JOURNAL   Immunogenetics 49 (4), 354-356 (1999)
   PUBMED   10079301
REFERENCE   7  (residues 1 to 777)
  AUTHORS   Herberg,J.A., Beck,S. and Trowsdale,J.
  TITLE     TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form
            a dense cluster at the centromeric end of the MHC
  JOURNAL   J Mol Biol 277 (4), 839-857 (1998)
   PUBMED   9545376
REFERENCE   8  (residues 1 to 777)
  AUTHORS   Herberg,J.A., Sgouros,J., Jones,T., Copeman,J., Humphray,S.J.,
            Sheer,D., Cresswell,P., Beck,S. and Trowsdale,J.
  TITLE     Genomic analysis of the Tapasin gene, located close to the TAP loci
            in the MHC
  JOURNAL   Eur J Immunol 28 (2), 459-467 (1998)
   PUBMED   9521053
REFERENCE   9  (residues 1 to 777)
  AUTHORS   Peterson,S.N., Trabalzini,L., Brtva,T.R., Fischer,T.,
            Altschuler,D.L., Martelli,P., Lapetina,E.G., Der,C.J. and
            White,G.C. 2nd.
  TITLE     Identification of a novel RalGDS-related protein as a candidate
            effector for Ras and Rap1
  JOURNAL   J Biol Chem 271 (47), 29903-29908 (1996)
   PUBMED   8939933
REFERENCE   10 (residues 1 to 777)
  AUTHORS   Isomura,M., Okui,K., Fujiwara,T., Shin,S. and Nakamura,Y.
  TITLE     Isolation and mapping of RAB2L, a human cDNA that encodes a protein
            homologous to RalGDS
  JOURNAL   Cytogenet Cell Genet 74 (4), 263-265 (1996)
   PUBMED   8976381
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL050259.1 and BX648015.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL050259.1, BC032681.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000497454.6/ ENSP00000420211.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..777
                     /product="ral guanine nucleotide dissociation
                     stimulator-like 2 isoform 1"
                     /note="GDS-related protein; ralGDS-like factor;
                     ras-associated protein RAB2L; ralGDS-like 2"
                     /calculated_mol_wt=83418
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15211.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15211.1)"
     Region          90..212
                     /region_name="RasGEFN"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     GTPases; N-terminal motif; smart00229"
                     /db_xref="CDD:214571"
     Region          239..513
                     /region_name="RasGEF"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     small GTPases; smart00147"
                     /db_xref="CDD:214539"
     Site            order(272..274,287..288,290..292,294..295,298..299,302,
                     349,352..353,355..357,359..362,364..365,385,388,393..395,
                     398,431..433,436..438,440..442,444..447,462,466,501,
                     504..505)
                     /site_type="other"
                     /note="Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:238087"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15211.1)"
     Region          581..644
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15211.1)"
     Region          647..733
                     /region_name="RA_RGL2"
                     /note="Ras-associating (RA) domain found in Ral guanine
                     nucleotide dissociation stimulator-like 2 (RalGDS-like 2)
                     and similar proteins; cd17211"
                     /db_xref="CDD:340731"
     Site            order(647..651,653,661..669,673..674,682,685..686,688)
                     /site_type="other"
                     /note="putative RA-Ras interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340731"
     Region          734..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15211.1)"
     CDS             1..777
                     /gene="RGL2"
                     /gene_synonym="HKE1.5; KE1.5; RAB2L"
                     /coded_by="NM_004761.5:115..2448"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4774.1"
                     /db_xref="GeneID:5863"
                     /db_xref="HGNC:HGNC:9769"
                     /db_xref="MIM:602306"
ORIGIN      
        1 mlprplrlll dtsppggvvl ssfrsrdpee gggpgglvvg ggqeeeeeee eeapvsvwde
       61 eedgavftvt srqyrpldpl vpmppprssr rlragtleal vrhlldtrts gtdvsfmsaf
      121 lathraftst pallglmadr lealeshptd elerttevai svlstwlash pedfgseakg
      181 qldrlesfll qtgyaagkgv gggsadlirn lrsrvdpqap dlpkplalpg dppadptdvl
      241 vfladhlaeq ltlldaelfl nlipsqclgg lwghrdrpgh shlcpsvrat vtqfnkvaga
      301 vvssvlgats tgegpgevti rplrppqrar llekwirvae ecrllrnfss vyavvsalqs
      361 spihrlraaw geatrdslrv fsslcqifse ednysqsrel lvqevklqsp lephskkapr
      421 sgsrgggvvp ylgtflkdlv mldaaskdel engyinfdkr rkefavlsel rrlqnecrgy
      481 nlqpdhdiqr wlqglrplte aqshrvscev eppgssdppa prvlrptlvi sqwtevlgsv
      541 gvptplvscd rpstggdeap ttpaplltrl aqhmkwpsvs sldsalessp slhspadpsh
      601 lsppassprp srghrrsasc gsplsggaee asggtgygge gsgpgasdcr iirvqmelge
      661 dgsvyksilv tsqdkapsvi srvlkknnrd savaseyelv qllpgerelt ipasanvfya
      721 mdgashdfll rqrrrsstat pgvtsgpsas gtppsegggg sfprikatgr kiaralf
//
LOCUS       NP_001269862             854 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 341 isoform 1 [Homo sapiens].
ACCESSION   NP_001269862
VERSION     NP_001269862.1
DBSOURCE    REFSEQ: accession NM_001282933.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Beziat,V., Fieschi,C., Momenilandi,M., Migaud,M., Belaid,B.,
            Djidjik,R. and Puel,A.
  TITLE     Inherited human ZNF341 deficiency
  JOURNAL   Curr Opin Immunol 82, 102326 (2023)
   PUBMED   37080116
  REMARK    GeneRIF: Inherited human ZNF341 deficiency.
            Review article
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Cekic,S., Huriyet,H., Hortoglu,M., Kasap,N., Ozen,A.,
            Karakoc-Aydiner,E., Metin,A., Ocakoglu,G., Demiroz Abakay,C.,
            Temel,S.G., Ozemri Sag,S., Baris,S., Cavas,T. and Sebnem Kilic,S.
  TITLE     Increased radiosensitivity and impaired DNA repair in patients with
            STAT3-LOF and ZNF341 deficiency, potentially contributing to
            malignant transformations
  JOURNAL   Clin Exp Immunol 209 (1), 83-89 (2022)
   PUBMED   35511492
  REMARK    GeneRIF: Increased radiosensitivity and impaired DNA repair in
            patients with STAT3-LOF and ZNF341 deficiency, potentially
            contributing to malignant transformations.
REFERENCE   3  (residues 1 to 854)
  AUTHORS   Lachover-Roth,I., Lagovsky,I., Shtorch-Asor,A., Confino-Cohen,R.,
            Reinstein,E. and Garty,B.Z.
  TITLE     Hyper IgE Syndrome in an Isolated Population in Israel
  JOURNAL   Front Immunol 13, 829239 (2022)
   PUBMED   35185921
  REMARK    GeneRIF: Hyper IgE Syndrome in an Isolated Population in Israel.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 854)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 854)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 854)
  AUTHORS   Beziat,V., Li,J., Lin,J.X., Ma,C.S., Li,P., Bousfiha,A.,
            Pellier,I., Zoghi,S., Baris,S., Keles,S., Gray,P., Du,N., Wang,Y.,
            Zerbib,Y., Levy,R., Leclercq,T., About,F., Lim,A.I., Rao,G.,
            Payne,K., Pelham,S.J., Avery,D.T., Deenick,E.K., Pillay,B.,
            Chou,J., Guery,R., Belkadi,A., Guerin,A., Migaud,M., Rattina,V.,
            Ailal,F., Benhsaien,I., Bouaziz,M., Habib,T., Chaussabel,D.,
            Marr,N., El-Benna,J., Grimbacher,B., Wargon,O., Bustamante,J.,
            Boisson,B., Muller-Fleckenstein,I., Fleckenstein,B.,
            Chandesris,M.O., Titeux,M., Fraitag,S., Alyanakian,M.A.,
            Leruez-Ville,M., Picard,C., Meyts,I., Di Santo,J.P., Hovnanian,A.,
            Somer,A., Ozen,A., Rezaei,N., Chatila,T.A., Abel,L., Leonard,W.J.,
            Tangye,S.G., Puel,A. and Casanova,J.L.
  TITLE     A recessive form of hyper-IgE syndrome by disruption of
            ZNF341-dependent STAT3 transcription and activity
  JOURNAL   Sci Immunol 3 (24) (2018)
   PUBMED   29907691
  REMARK    GeneRIF: Human ZNF341 is essential for the STAT3
            transcription-dependent autoinduction and sustained activity of
            STAT3.
REFERENCE   7  (residues 1 to 854)
  AUTHORS   Frey-Jakobs,S., Hartberger,J.M., Fliegauf,M., Bossen,C.,
            Wehmeyer,M.L., Neubauer,J.C., Bulashevska,A., Proietti,M.,
            Frobel,P., Noltner,C., Yang,L., Rojas-Restrepo,J., Langer,N.,
            Winzer,S., Engelhardt,K.R., Glocker,C., Pfeifer,D., Klein,A.,
            Schaffer,A.A., Lagovsky,I., Lachover-Roth,I., Beziat,V., Puel,A.,
            Casanova,J.L., Fleckenstein,B., Weidinger,S., Kilic,S.S.,
            Garty,B.Z., Etzioni,A. and Grimbacher,B.
  TITLE     ZNF341 controls STAT3 expression and thereby immunocompetence
  JOURNAL   Sci Immunol 3 (24) (2018)
   PUBMED   29907690
  REMARK    GeneRIF: Study reports two distinct homozygous nonsense mutations
            in exons 6 and 8 of ZNF341 in four consanguineous families with
            recurrent bacterial and fungal infections. ZNF341 mutations
            segregate with a phenotype resembling hyper-immunoglobulin E
            syndrome. Authors describe ZNF341 as a positive regulator of STAT3
            expression and report the clinical and laboratory phenotype of
            individuals lacking ZNF341.
REFERENCE   8  (residues 1 to 854)
  AUTHORS   Lango Allen,H., Estrada,K., Lettre,G., Berndt,S.I., Weedon,M.N.,
            Rivadeneira,F., Willer,C.J., Jackson,A.U., Vedantam,S.,
            Raychaudhuri,S., Ferreira,T., Wood,A.R., Weyant,R.J., Segre,A.V.,
            Speliotes,E.K., Wheeler,E., Soranzo,N., Park,J.H., Yang,J.,
            Gudbjartsson,D., Heard-Costa,N.L., Randall,J.C., Qi,L., Vernon
            Smith,A., Magi,R., Pastinen,T., Liang,L., Heid,I.M., Luan,J.,
            Thorleifsson,G., Winkler,T.W., Goddard,M.E., Sin Lo,K., Palmer,C.,
            Workalemahu,T., Aulchenko,Y.S., Johansson,A., Zillikens,M.C.,
            Feitosa,M.F., Esko,T., Johnson,T., Ketkar,S., Kraft,P., Mangino,M.,
            Prokopenko,I., Absher,D., Albrecht,E., Ernst,F., Glazer,N.L.,
            Hayward,C., Hottenga,J.J., Jacobs,K.B., Knowles,J.W., Kutalik,Z.,
            Monda,K.L., Polasek,O., Preuss,M., Rayner,N.W., Robertson,N.R.,
            Steinthorsdottir,V., Tyrer,J.P., Voight,B.F., Wiklund,F., Xu,J.,
            Zhao,J.H., Nyholt,D.R., Pellikka,N., Perola,M., Perry,J.R.,
            Surakka,I., Tammesoo,M.L., Altmaier,E.L., Amin,N., Aspelund,T.,
            Bhangale,T., Boucher,G., Chasman,D.I., Chen,C., Coin,L.,
            Cooper,M.N., Dixon,A.L., Gibson,Q., Grundberg,E., Hao,K., Juhani
            Junttila,M., Kaplan,L.M., Kettunen,J., Konig,I.R., Kwan,T.,
            Lawrence,R.W., Levinson,D.F., Lorentzon,M., McKnight,B.,
            Morris,A.P., Muller,M., Suh Ngwa,J., Purcell,S., Rafelt,S.,
            Salem,R.M., Salvi,E., Sanna,S., Shi,J., Sovio,U., Thompson,J.R.,
            Turchin,M.C., Vandenput,L., Verlaan,D.J., Vitart,V., White,C.C.,
            Ziegler,A., Almgren,P., Balmforth,A.J., Campbell,H., Citterio,L.,
            De Grandi,A., Dominiczak,A., Duan,J., Elliott,P., Elosua,R.,
            Eriksson,J.G., Freimer,N.B., Geus,E.J., Glorioso,N., Haiqing,S.,
            Hartikainen,A.L., Havulinna,A.S., Hicks,A.A., Hui,J., Igl,W.,
            Illig,T., Jula,A., Kajantie,E., Kilpelainen,T.O., Koiranen,M.,
            Kolcic,I., Koskinen,S., Kovacs,P., Laitinen,J., Liu,J., Lokki,M.L.,
            Marusic,A., Maschio,A., Meitinger,T., Mulas,A., Pare,G.,
            Parker,A.N., Peden,J.F., Petersmann,A., Pichler,I.,
            Pietilainen,K.H., Pouta,A., Ridderstrale,M., Rotter,J.I.,
            Sambrook,J.G., Sanders,A.R., Schmidt,C.O., Sinisalo,J., Smit,J.H.,
            Stringham,H.M., Bragi Walters,G., Widen,E., Wild,S.H.,
            Willemsen,G., Zagato,L., Zgaga,L., Zitting,P., Alavere,H.,
            Farrall,M., McArdle,W.L., Nelis,M., Peters,M.J., Ripatti,S., van
            Meurs,J.B., Aben,K.K., Ardlie,K.G., Beckmann,J.S., Beilby,J.P.,
            Bergman,R.N., Bergmann,S., Collins,F.S., Cusi,D., den Heijer,M.,
            Eiriksdottir,G., Gejman,P.V., Hall,A.S., Hamsten,A., Huikuri,H.V.,
            Iribarren,C., Kahonen,M., Kaprio,J., Kathiresan,S., Kiemeney,L.,
            Kocher,T., Launer,L.J., Lehtimaki,T., Melander,O., Mosley,T.H. Jr.,
            Musk,A.W., Nieminen,M.S., O'Donnell,C.J., Ohlsson,C., Oostra,B.,
            Palmer,L.J., Raitakari,O., Ridker,P.M., Rioux,J.D., Rissanen,A.,
            Rivolta,C., Schunkert,H., Shuldiner,A.R., Siscovick,D.S.,
            Stumvoll,M., Tonjes,A., Tuomilehto,J., van Ommen,G.J., Viikari,J.,
            Heath,A.C., Martin,N.G., Montgomery,G.W., Province,M.A., Kayser,M.,
            Arnold,A.M., Atwood,L.D., Boerwinkle,E., Chanock,S.J., Deloukas,P.,
            Gieger,C., Gronberg,H., Hall,P., Hattersley,A.T., Hengstenberg,C.,
            Hoffman,W., Lathrop,G.M., Salomaa,V., Schreiber,S., Uda,M.,
            Waterworth,D., Wright,A.F., Assimes,T.L., Barroso,I., Hofman,A.,
            Mohlke,K.L., Boomsma,D.I., Caulfield,M.J., Cupples,L.A.,
            Erdmann,J., Fox,C.S., Gudnason,V., Gyllensten,U., Harris,T.B.,
            Hayes,R.B., Jarvelin,M.R., Mooser,V., Munroe,P.B., Ouwehand,W.H.,
            Penninx,B.W., Pramstaller,P.P., Quertermous,T., Rudan,I.,
            Samani,N.J., Spector,T.D., Volzke,H., Watkins,H., Wilson,J.F.,
            Groop,L.C., Haritunians,T., Hu,F.B., Kaplan,R.C., Metspalu,A.,
            North,K.E., Schlessinger,D., Wareham,N.J., Hunter,D.J.,
            O'Connell,J.R., Strachan,D.P., Wichmann,H.E., Borecki,I.B., van
            Duijn,C.M., Schadt,E.E., Thorsteinsdottir,U., Peltonen,L.,
            Uitterlinden,A.G., Visscher,P.M., Chatterjee,N., Loos,R.J.,
            Boehnke,M., McCarthy,M.I., Ingelsson,E., Lindgren,C.M.,
            Abecasis,G.R., Stefansson,K., Frayling,T.M. and Hirschhorn,J.N.
  TITLE     Hundreds of variants clustered in genomic loci and biological
            pathways affect human height
  JOURNAL   Nature 467 (7317), 832-838 (2010)
   PUBMED   20881960
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC132873.1, BC094738.1 and AK027550.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC146811.1, SRR1660803.184316.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375200.6/ ENSP00000364346.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..854
                     /product="zinc finger protein 341 isoform 1"
                     /calculated_mol_wt=92598
     Region          152..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYN7.2)"
     Region          <237..>374
                     /region_name="KREPA"
                     /note="Kinetoplastid RNA Editing Protein A (KREPA);
                     cl49620"
                     /db_xref="CDD:483960"
     Region          323..729
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          324..344
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          352..372
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          399..434
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYN7.2)"
     Region          447..467
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(452,454,456,458..459,462..463,466,482,484,488..489,
                     492..493,496,510,512,514,516..517,520..521,524)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          475..497
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          505..525
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          542..562
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          568..588
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(573,575,577,579..580,583..584,587,601,603,607..608,
                     611..612,615,629,631,633,635..636,639..640,643)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          596..616
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          624..644
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          652..677
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          685..705
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          713..730
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          731..763
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYN7.2)"
     CDS             1..854
                     /gene="ZNF341"
                     /gene_synonym="HIES3"
                     /coded_by="NM_001282933.2:27..2591"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS74719.1"
                     /db_xref="GeneID:84905"
                     /db_xref="HGNC:HGNC:15992"
                     /db_xref="MIM:618269"
ORIGIN      
        1 maqaifeale gmdnqtvlav qslldgqgav pdptgqsvna ppaiqpldde dvflcgkckk
       61 qfnslpafmt hkreqcqgna palatvslat nsiyppsaap tavqqaptpa nrqistyitv
      121 ppspliqtlv qgnilvsddv lmsamsafts ldqpmpqgpp pvqsslnmhs vpsyltqppp
      181 ppppppplpp ppppqppppp pqslgppgrp npggngvvev ysaaaplags gtveiqalgm
      241 qpypplevpn qcveppvypt ptvyspgkqg fkpkgpnpaa pmtsatggtv atfdspatlk
      301 trrakgargl peaagkpkaq klkcsycdks ftknfdlqqh irshtgekpf qciacgrafa
      361 qksnvkkhmq thkvwppghs ggtvsrnsvt vqvmalnpsr qedeestglg qplpgapqpq
      421 alstageeeg dkpeskqvvl idssylcqfc pskfstyfql kshmtqhkne qvykcvvksc
      481 aqtfpkldtf lehikshqee lsyrchlcgk dfpslydlgv hqyshsllpq hspkkdnavy
      541 kcvkcvnkys tpealehhlq tathnfpcph cqkvfpcery lrrhlpthgs ggrfkcqvck
      601 kffrrehylk lhahihsgek pykcsvcesa fnrkdklkrh mlihepfkky kcpfsthtgc
      661 skefnrpdkl kahilshsgm klhkcalcsk sfsrrahlae hqrahtgnyk frcagcakgf
      721 srhkylkdhr crlgpqkdkd lqtrrppqrr aaprscgsgg rkvltplpdp lgleelkdtg
      781 aglvpeavpg kppfaepdav lsivvggavg aetelvvpgh aeglgsnlal aelqagaegp
      841 camlavpvyi qase
//
LOCUS       NP_001092909            1008 aa            linear   PRI 27-APR-2025
DEFINITION  ephrin type-A receptor 10 isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001092909
VERSION     NP_001092909.1
DBSOURCE    REFSEQ: accession NM_001099439.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Huang,S., Ma,L., Liu,X., He,C., Li,J., Hu,Z., Jiang,L., Liu,Y.,
            Liu,X., Feng,Y. and Cai,X.
  TITLE     A non-coding variant in 5' untranslated region drove up-regulation
            of pseudo-kinase EPHA10 and caused non-syndromic hearing loss in
            humans
  JOURNAL   Hum Mol Genet 32 (5), 720-731 (2023)
   PUBMED   36048850
  REMARK    GeneRIF: A non-coding variant in 5' untranslated region drove
            up-regulation of pseudo-kinase EPHA10 and caused non-syndromic
            hearing loss in humans.
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Zhao,W., Liu,L., Li,X. and Xu,S.
  TITLE     EphA10 drives tumor progression and immune evasion by regulating
            the MAPK/ERK cascade in lung adenocarcinoma
  JOURNAL   Int Immunopharmacol 110, 109031 (2022)
   PUBMED   35839564
  REMARK    GeneRIF: EphA10 drives tumor progression and immune evasion by
            regulating the MAPK/ERK cascade in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Peng,J. and Zhang,D.
  TITLE     Coexpression of EphA10 and Gli3 promotes breast cancer cell
            proliferation, invasion and migration
  JOURNAL   J Investig Med 69 (6), 1215-1221 (2021)
   PUBMED   33990369
  REMARK    GeneRIF: Coexpression of EphA10 and Gli3 promotes breast cancer
            cell proliferation, invasion and migration.
REFERENCE   4  (residues 1 to 1008)
  AUTHORS   Chen,Y.L., Yen,Y.C., Jang,C.W., Wang,S.H., Huang,H.T., Chen,C.H.,
            Hsiao,J.R., Chang,J.Y. and Chen,Y.W.
  TITLE     Ephrin A4-ephrin receptor A10 signaling promotes cell migration and
            spheroid formation by upregulating NANOG expression in oral
            squamous cell carcinoma cells
  JOURNAL   Sci Rep 11 (1), 644 (2021)
   PUBMED   33436772
  REMARK    GeneRIF: Ephrin A4-ephrin receptor A10 signaling promotes cell
            migration and spheroid formation by upregulating NANOG expression
            in oral squamous cell carcinoma cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1008)
  AUTHORS   Shrestha,S., Byrne,D.P., Harris,J.A., Kannan,N. and Eyers,P.A.
  TITLE     Cataloguing the dead: breathing new life into pseudokinase research
  JOURNAL   FEBS J 287 (19), 4150-4169 (2020)
   PUBMED   32053275
  REMARK    GeneRIF: Cataloguing the dead: breathing new life into pseudokinase
            research.
            Review article
REFERENCE   6  (residues 1 to 1008)
  AUTHORS   Cheng,C.Y., Schache,M., Ikram,M.K., Young,T.L., Guggenheim,J.A.,
            Vitart,V., MacGregor,S., Verhoeven,V.J., Barathi,V.A., Liao,J.,
            Hysi,P.G., Bailey-Wilson,J.E., St Pourcain,B., Kemp,J.P.,
            McMahon,G., Timpson,N.J., Evans,D.M., Montgomery,G.W., Mishra,A.,
            Wang,Y.X., Wang,J.J., Rochtchina,E., Polasek,O., Wright,A.F.,
            Amin,N., van Leeuwen,E.M., Wilson,J.F., Pennell,C.E., van
            Duijn,C.M., de Jong,P.T., Vingerling,J.R., Zhou,X., Chen,P., Li,R.,
            Tay,W.T., Zheng,Y., Chew,M., Burdon,K.P., Craig,J.E., Iyengar,S.K.,
            Igo,R.P. Jr., Lass,J.H. Jr., Chew,E.Y., Haller,T., Mihailov,E.,
            Metspalu,A., Wedenoja,J., Simpson,C.L., Wojciechowski,R., Hohn,R.,
            Mirshahi,A., Zeller,T., Pfeiffer,N., Lackner,K.J., Bettecken,T.,
            Meitinger,T., Oexle,K., Pirastu,M., Portas,L., Nag,A.,
            Williams,K.M., Yonova-Doing,E., Klein,R., Klein,B.E.,
            Hosseini,S.M., Paterson,A.D., Makela,K.M., Lehtimaki,T.,
            Kahonen,M., Raitakari,O., Yoshimura,N., Matsuda,F., Chen,L.J.,
            Pang,C.P., Yip,S.P., Yap,M.K., Meguro,A., Mizuki,N., Inoko,H.,
            Foster,P.J., Zhao,J.H., Vithana,E., Tai,E.S., Fan,Q., Xu,L.,
            Campbell,H., Fleck,B., Rudan,I., Aung,T., Hofman,A.,
            Uitterlinden,A.G., Bencic,G., Khor,C.C., Forward,H., Parssinen,O.,
            Mitchell,P., Rivadeneira,F., Hewitt,A.W., Williams,C., Oostra,B.A.,
            Teo,Y.Y., Hammond,C.J., Stambolian,D., Mackey,D.A., Klaver,C.C.,
            Wong,T.Y., Saw,S.M. and Baird,P.N.
  CONSRTM   Consortium for Refractive Error and Myopia; Fuchs' Genetics
            Multi-Center Study Group; Wellcome Trust Case Control Consortium 2;
            Diabetes Control and Complications Trial/Epidemiology of Diabetes
            Interventions, and Complications Research Group
  TITLE     Nine loci for ocular axial length identified through genome-wide
            association studies, including shared loci with refractive error
  JOURNAL   Am J Hum Genet 93 (2), 264-277 (2013)
   PUBMED   24144296
REFERENCE   7  (residues 1 to 1008)
  AUTHORS   Tao,S., Wang,Z., Feng,J., Hsu,F.C., Jin,G., Kim,S.T., Zhang,Z.,
            Gronberg,H., Zheng,L.S., Isaacs,W.B., Xu,J. and Sun,J.
  TITLE     A genome-wide search for loci interacting with known prostate
            cancer risk-associated genetic variants
  JOURNAL   Carcinogenesis 33 (3), 598-603 (2012)
   PUBMED   22219177
REFERENCE   8  (residues 1 to 1008)
  AUTHORS   Fox,B.P. and Kandpal,R.P.
  TITLE     A paradigm shift in EPH receptor interaction: biological relevance
            of EPHB6 interaction with EPHA2 and EPHB2 in breast carcinoma cell
            lines
  JOURNAL   Cancer Genomics Proteomics 8 (4), 185-193 (2011)
   PUBMED   21737611
  REMARK    GeneRIF: EPHA10 does not interact with EPHB6 in breast neoplasms
REFERENCE   9  (residues 1 to 1008)
  AUTHORS   Alonso-C,L.M., Trinidad,E.M., de Garcillan,B., Ballesteros,M.,
            Castellanos,M., Cotillo,I., Munoz,J.J. and Zapata,A.G.
  TITLE     Expression profile of Eph receptors and ephrin ligands in healthy
            human B lymphocytes and chronic lymphocytic leukemia B-cells
  JOURNAL   Leuk Res 33 (3), 395-406 (2009)
   PUBMED   18819711
  REMARK    GeneRIF: CLL B-cells showed a more heterogeneous Eph/EFN profile,
            specially EFNA4, EphB6 and EphA10.
REFERENCE   10 (residues 1 to 1008)
  AUTHORS   Aasheim,H.C., Patzke,S., Hjorthaug,H.S. and Finne,E.F.
  TITLE     Characterization of a novel Eph receptor tyrosine kinase, EphA10,
            expressed in testis
  JOURNAL   Biochim Biophys Acta 1723 (1-3), 1-7 (2005)
   PUBMED   15777695
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AJ872185.1, BC041360.1, AC104336.2 and BC039363.1.
            
            Summary: Ephrin receptors, the largest subfamily of receptor
            tyrosine kinases (RTKs), and their ephrin ligands are important
            mediators of cell-cell communication regulating cell attachment,
            shape, and mobility in neuronal and epithelial cells (Aasheim et
            al., 2005 [PubMed 15777695]). See MIM 179610 for additional
            background on Eph receptors and ephrins.[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (3) represents the longer
            transcript and encodes the longer isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373048.9/ ENSP00000362139.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..1008
                     /product="ephrin type-A receptor 10 isoform 3 precursor"
                     /EC_number="2.7.10.1"
                     /note="EphA10s protein; Ephrin type-A receptor 10"
                     /calculated_mol_wt=106068
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3667
     mat_peptide     34..1008
                     /product="Ephrin type-A receptor 10. /id=PRO_0000042157"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JZY3.2)"
                     /calculated_mol_wt=106068
     Region          35..210
                     /region_name="EphR_LBD_A10"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 10;
                     cd10487"
                     /db_xref="CDD:198455"
     Site            order(59,61..65,72..73,75,77,108,110,115..116,161,
                     165..166,169..171,198..200,202)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198455"
     Site            311
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5JZY3.2)"
     Region          322..342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JZY3.2)"
     Site            order(338,417,430)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          339..431
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(431..432,434..435)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          451..531
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Site            486
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5JZY3.2)"
     Site            566..586
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JZY3.2)"
     Region          569..642
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          639..904
                     /region_name="PTKc_EphR_A10"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Ephrin Receptor A10; cd05064"
                     /db_xref="CDD:133195"
     Site            order(651,653..655,659,675,677,723..724,726,770,774..775,
                     777,788,805..809,818,852)
                     /site_type="active"
                     /db_xref="CDD:133195"
     Site            order(651,654..655,675,677,723..724,726,775,777,788)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133195"
     Site            order(770,774,805..809,818,852)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133195"
     Site            787..811
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133195"
     Region          929..998
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     CDS             1..1008
                     /gene="EPHA10"
                     /gene_synonym="DFNA88"
                     /coded_by="NM_001099439.2:55..3081"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS41305.1"
                     /db_xref="GeneID:284656"
                     /db_xref="HGNC:HGNC:19987"
                     /db_xref="MIM:611123"
ORIGIN      
        1 metcagphpl rlflcrmqlc lalllgpwrp gtaeevilld skasqaelgw talpsngwee
       61 isgvdehdrp irtyqvcnvl epnqdnwlqt gwisrgrgqr ifvelqftlr dcssipgaag
      121 tcketfnvyy leteadlgrg rprlggsrpr kidtiaades ftqgdlgerk mklntevrei
      181 gplsrrgfhl afqdvgacva lvsvrvyykq cratvrglat fpataaesaf stlvevagtc
      241 vahsegepgs pprmhcgadg ewlvpvgrcs csagfqergd fceacppgfy kvsprrplcs
      301 pcpehsrale nastfcvcqd syarsptdpp sasctrppsa prdlqyslsr splvlrlrwl
      361 ppadsggrsd vtysllclrc gregpagace pcgprvaflp rqaglreraa tllhlrpgar
      421 ytvrvaalng vsgpaaaagt tyaqvtvstg pgapweedei rrdrvepqsv slswrepipa
      481 gapgandtey eiryyekgqs eqtysmvktg aptvtvtnlk patryvfqir aaspgpswea
      541 qsfnpsievq tlgeaasgsr dqspaivvtv vtisallvlg svmsvlaiwr rpcsygkggg
      601 dahdeeelyf hfkvptrrtf ldpqscgdll qavhlfakel daksvtlers lgggrfgelc
      661 cgclqlpgrq ellvavhmlr dsasdsqrlg flaealtlgq fdhshivrle gvvtrgstlm
      721 ivteymshga ldgflrrheg qlvagqlmgl lpglasamky lsemgyvhrg laarhvlvss
      781 dlvckisgfg rgprdrseav yttmsgrspa lwaapetlqf ghfssasdvw sfgiimwevm
      841 afgerpywdm sgqdvikave dgfrlppprn cpnllhrlml dcwqkdpger prfsqihsil
      901 skmvqdpepp kcalttcprp ptpladrafs tfpsfgsvga wlealdlcry kdsfaaagyg
      961 sleavaemta qdlvslgisl aehreallsg isalqarvlq lqgqgvqv
//
LOCUS       NP_001188291              95 aa            linear   PRI 27-APR-2025
DEFINITION  high mobility group nucleosome-binding domain-containing protein 3
            isoform c [Homo sapiens].
ACCESSION   NP_001188291
VERSION     NP_001188291.1
DBSOURCE    REFSEQ: accession NM_001201362.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Bian,Y., Li,J., Shen,H., Li,Y., Hou,Y., Huang,L., Song,G. and
            Qiao,C.
  TITLE     WTAP dysregulation-mediated HMGN3-m6A modification inhibited
            trophoblast invasion in early-onset preeclampsia
  JOURNAL   FASEB J 36 (12), e22617 (2022)
   PUBMED   36412513
  REMARK    GeneRIF: WTAP dysregulation-mediated HMGN3-m6A modification
            inhibited trophoblast invasion in early-onset preeclampsia.
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Sorin,S., Kubota,S., Hamidi,S., Yokomizo-Nakano,T.,
            Vaeteewoottacharn,K., Wongkham,S., Waraasawapati,S., Pairojkul,C.,
            Bai,J., Morii,M., Sheng,G., Sawanyawisuth,K. and Sashida,G.
  TITLE     HMGN3 represses transcription of epithelial regulators to promote
            migration of cholangiocarcinoma in a SNAI2-dependent manner
  JOURNAL   FASEB J 36 (7), e22345 (2022)
   PUBMED   35635715
  REMARK    GeneRIF: HMGN3 represses transcription of epithelial regulators to
            promote migration of cholangiocarcinoma in a SNAI2-dependent
            manner.
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Koh,M., Ahmad,I., Ko,Y., Zhang,Y., Martinez,T.F., Diedrich,J.K.,
            Chu,Q., Moresco,J.J., Erb,M.A., Saghatelian,A., Schultz,P.G. and
            Bollong,M.J.
  TITLE     A short ORF-encoded transcriptional regulator
  JOURNAL   Proc Natl Acad Sci U S A 118 (4) (2021)
   PUBMED   33468658
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Lei,S.F., Shen,H., Yang,T.L., Guo,Y., Dong,S.S., Xu,X.H.,
            Deng,F.Y., Tian,Q., Liu,Y.J., Liu,Y.Z., Li,J. and Deng,H.W.
  TITLE     Genome-wide association study identifies HMGN3 locus for spine bone
            size variation in Chinese
  JOURNAL   Hum Genet 131 (3), 463-469 (2012)
   PUBMED   21947420
  REMARK    GeneRIF: The SNPs in the region of HMGN3 gene formed a tightly
            combined haplotype block in both Chinese and Caucasians. The
            results suggest that the genomic region containing HMGN3 gene may
            be associated with spine BS in Chinese.
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Ueda,T., Furusawa,T., Kurahashi,T., Tessarollo,L. and Bustin,M.
  TITLE     The nucleosome binding protein HMGN3 modulates the transcription
            profile of pancreatic beta cells and affects insulin secretion
  JOURNAL   Mol Cell Biol 29 (19), 5264-5276 (2009)
   PUBMED   19651901
  REMARK    GeneRIF: loss of HMGN3 impairs glucose-stimulated insulin secretion
            and leads to a diabetic phenotype.
REFERENCE   6  (residues 1 to 95)
  AUTHORS   West,K.L., Castellini,M.A., Duncan,M.K. and Bustin,M.
  TITLE     Chromosomal proteins HMGN3a and HMGN3b regulate the expression of
            glycine transporter 1
  JOURNAL   Mol Cell Biol 24 (9), 3747-3756 (2004)
   PUBMED   15082770
REFERENCE   7  (residues 1 to 95)
  AUTHORS   Leong,P.W., Liew,K., Lim,W. and Chow,V.T.
  TITLE     Differential display RT-PCR analysis of enterovirus-71-infected
            rhabdomyosarcoma cells reveals mRNA expression responses of
            multiple human genes with known and novel functions
  JOURNAL   Virology 295 (1), 147-159 (2002)
   PUBMED   12033773
REFERENCE   8  (residues 1 to 95)
  AUTHORS   West,K.L., Ito,Y., Birger,Y., Postnikov,Y., Shirakawa,H. and
            Bustin,M.
  TITLE     HMGN3a and HMGN3b, two protein isoforms with a tissue-specific
            expression pattern, expand the cellular repertoire of
            nucleosome-binding proteins
  JOURNAL   J Biol Chem 276 (28), 25959-25969 (2001)
   PUBMED   11356838
REFERENCE   9  (residues 1 to 95)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX641808.1, AL355796.11,
            BU619570.1 and AI028183.1.
            
            Summary: The protein encoded by this gene binds thyroid hormone
            receptor beta in the presence of thyroid hormone. The encoded
            protein, a member of the HMGN protein family, is thought to reduce
            the compactness of the chromatin fiber in nucleosomes, thereby
            enhancing transcription from chromatin templates. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. There is a related pseudogene on chromosome 1.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) retains an alternate segment
            in the 3' region compared to variant 1, which results in a
            different 3' coding region and 3' UTR. The resulting isoform (c) is
            shorter and has a distinct C-terminus compared to isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.451805.1,
                                           SRR1660803.305524.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267752, SAMN03267760
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..95
                     /product="high mobility group nucleosome-binding
                     domain-containing protein 3 isoform c"
                     /note="thyroid hormone receptor interacting protein 7;
                     high mobility group nucleosome-binding domain-containing
                     protein 3; TR-interacting protein 7"
                     /calculated_mol_wt=10098
     Region          2..87
                     /region_name="HMG17"
                     /note="domain in high mobilty group proteins HMG14 and HMG
                     17; smart00527"
                     /db_xref="CDD:197773"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15651.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q15651.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15651.2)"
     CDS             1..95
                     /gene="HMGN3"
                     /gene_synonym="PNAS-24; PNAS-25; TRIP7"
                     /coded_by="NM_001201362.2:123..410"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:9324"
                     /db_xref="HGNC:HGNC:12312"
                     /db_xref="MIM:604502"
ORIGIN      
        1 mpkrkspent egkdgskvtk qeptrrsarl sakpappkpe pkprktsakk epgakisrga
       61 kgkkeekqea gkegtapsen getkaeevls intsh
//
LOCUS       NP_001009158             140 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-synuclein [Pan troglodytes].
ACCESSION   NP_001009158 XP_001162256 XP_001162295 XP_001162335 XP_001162370
            XP_001162416 XP_001162454 XP_001162500 XP_001162542 XP_001162591
            XP_001162634 XP_009446185 XP_517341
VERSION     NP_001009158.1
DBSOURCE    REFSEQ: accession NM_001009158.4
KEYWORDS    RefSeq.
SOURCE      Pan troglodytes (chimpanzee)
  ORGANISM  Pan troglodytes
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Pan.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Hamilton,B.A.
  TITLE     alpha-Synuclein A53T substitution associated with Parkinson disease
            also marks the divergence of Old World and New World primates
  JOURNAL   Genomics 83 (4), 739-742 (2004)
   PUBMED   15028296
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAQQLN020000003.1.
            
            On or before Apr 16, 2016 this sequence version replaced
            XP_009446185.1, XP_001162416.1, XP_001162454.1, XP_001162500.1,
            XP_001162542.1, XP_001162591.1, XP_001162634.1, XP_517341.2,
            XP_001162335.1, XP_001162295.1, XP_001162370.1, XP_001162256.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GABF01003734.1,
                                           SRR22306524.1832552.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02045701 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Pan troglodytes"
                     /db_xref="taxon:9598"
                     /chromosome="3"
                     /map="3"
     Protein         1..140
                     /product="alpha-synuclein"
                     /note="synuclein, alpha (non A4 component of amyloid
                     precursor)"
                     /calculated_mol_wt=14329
     Region          1..131
                     /region_name="Synuclein"
                     /note="pfam01387"
                     /db_xref="CDD:460186"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P37840; propagated from
                     UniProtKB/Swiss-Prot (P61145.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P37840; propagated from
                     UniProtKB/Swiss-Prot (P61145.1)"
     Region          100..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61145.1)"
     Region          111..140
                     /region_name="Interaction with SERF1A.
                     /evidence=ECO:0000250|UniProtKB:P37840"
                     /note="propagated from UniProtKB/Swiss-Prot (P61145.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FYN.
                     /evidence=ECO:0000250|UniProtKB:P37840; propagated from
                     UniProtKB/Swiss-Prot (P61145.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:P37840; propagated from
                     UniProtKB/Swiss-Prot (P61145.1)"
     CDS             1..140
                     /gene="SNCA"
                     /coded_by="NM_001009158.4:119..541"
                     /db_xref="GeneID:461375"
                     /db_xref="VGNC:VGNC:1998"
ORIGIN      
        1 mdvfmkglsk akegvvaaae ktkqgvaeaa gktkegvlyv gsktkegvvh gvatvaektk
       61 eqvtnvggav vtgvtavaqk tvegagsiaa atgfvkkdql gkneegapqe giledmpvdp
      121 dneayempse egyqdyepea
//
LOCUS       NP_001653                180 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-ribosylation factor 5 [Homo sapiens].
ACCESSION   NP_001653
VERSION     NP_001653.1
DBSOURCE    REFSEQ: accession NM_001662.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Kulasekaran,G., Chaineau,M., Piscopo,V.E.C., Verginelli,F.,
            Fotouhi,M., Girard,M., Tang,Y., Dali,R., Lo,R., Stifani,S. and
            McPherson,P.S.
  TITLE     An Arf/Rab cascade controls the growth and invasiveness of
            glioblastoma
  JOURNAL   J Cell Biol 220 (2) (2021)
   PUBMED   33443570
  REMARK    GeneRIF: An Arf/Rab cascade controls the growth and invasiveness of
            glioblastoma.
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Fernandez-Chamorro,J., Francisco-Velilla,R., Ramajo,J. and
            Martinez-Salas,E.
  TITLE     Rab1b and ARF5 are novel RNA-binding proteins involved in FMDV
            IRES-driven RNA localization
  JOURNAL   Life Sci Alliance 2 (1), e201800131 (2019)
   PUBMED   30655362
  REMARK    GeneRIF: ARF5 and Rab1b exhibit RNA-binding capacity, suggesting a
            role for domain 3 of the IRES in RNA localization into specific
            cellular compartments.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Egerer,J., Emmerich,D., Fischer-Zirnsak,B., Chan,W.L.,
            Meierhofer,D., Tuysuz,B., Marschner,K., Sauer,S., Barr,F.A.,
            Mundlos,S. and Kornak,U.
  TITLE     GORAB Missense Mutations Disrupt RAB6 and ARF5 Binding and Golgi
            Targeting
  JOURNAL   J Invest Dermatol 135 (10), 2368-2376 (2015)
   PUBMED   26000619
  REMARK    GeneRIF: GORAB missense mutation disrupt ARF5 binding in Golgi
            apparatus in patients, with genetic skin diseases.
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Yu,J., Chia,J., Canning,C.A., Jones,C.M., Bard,F.A. and
            Virshup,D.M.
  TITLE     WLS retrograde transport to the endoplasmic reticulum during Wnt
            secretion
  JOURNAL   Dev Cell 29 (3), 277-291 (2014)
   PUBMED   24768165
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Helms,J.B., Palmer,D.J. and Rothman,J.E.
  TITLE     Two distinct populations of ARF bound to Golgi membranes
  JOURNAL   J Cell Biol 121 (4), 751-760 (1993)
   PUBMED   8491770
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Lee,F.J., Moss,J. and Vaughan,M.
  TITLE     Human and Giardia ADP-ribosylation factors (ARFs) complement ARF
            function in Saccharomyces cerevisiae
  JOURNAL   J Biol Chem 267 (34), 24441-24445 (1992)
   PUBMED   1447192
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Tsuchiya,M., Price,S.R., Tsai,S.C., Moss,J. and Vaughan,M.
  TITLE     Molecular identification of ADP-ribosylation factor mRNAs and their
            expression in mammalian cells
  JOURNAL   J Biol Chem 266 (5), 2772-2777 (1991)
   PUBMED   1993656
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Stearns,T., Willingham,M.C., Botstein,D. and Kahn,R.A.
  TITLE     ADP-ribosylation factor is functionally and physically associated
            with the Golgi complex
  JOURNAL   Proc Natl Acad Sci U S A 87 (3), 1238-1242 (1990)
   PUBMED   2105501
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000357.1.
            
            Summary: This gene is a member of the human ADP-ribosylation factor
            (ARF) gene family. These genes encode small guanine
            nucleotide-binding proteins that stimulate the
            ADP-ribosyltransferase activity of cholera toxin and play a role in
            vesicular trafficking and as activators of phospholipase D. The
            gene products include 6 ARF proteins and 11 ARF-like proteins and
            constitute 1 family of the RAS superfamily. The ARF proteins are
            categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and
            ARF5) and class III (ARF6). The members of each class share a
            common gene organization. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033104.1, SRR3476690.883380.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000000233.10/ ENSP00000000233.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q32.1"
     Protein         1..180
                     /product="ADP-ribosylation factor 5"
                     /note="ADP ribosylation factor 5"
                     /calculated_mol_wt=20399
     Region          1..180
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            24..31
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206717"
     Site            order(26..32,126..127,129,159..161)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206717"
     Site            order(26..27,31,35,47..54,76,81)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206717"
     Site            36..51
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206717"
     Site            order(48..52,57,67,71,73,77,79..81)
                     /site_type="other"
                     /note="GEF interaction site [polypeptide binding]"
                     /db_xref="CDD:206717"
     Site            48
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206717"
     Site            order(49..51,73,80)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:206717"
     Site            51..66
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206717"
     Site            67..70
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206717"
     Site            69..86
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206717"
     Site            126..129
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206717"
     Site            159..161
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206717"
     CDS             1..180
                     /gene="ARF5"
                     /coded_by="NM_001662.4:89..631"
                     /db_xref="CCDS:CCDS34745.1"
                     /db_xref="GeneID:381"
                     /db_xref="HGNC:HGNC:658"
                     /db_xref="MIM:103188"
ORIGIN      
        1 mgltvsalfs rifgkkqmri lmvgldaagk ttilyklklg eivttiptig fnvetveykn
       61 icftvwdvgg qdkirplwrh yfqntqglif vvdsndrerv qesadelqkm lqedelrdav
      121 llvfankqdm pnampvselt dklglqhlrs rtwyvqatca tqgtglydgl dwlshelskr
//
LOCUS       NP_001356315             386 aa            linear   PRI 27-APR-2025
DEFINITION  nucleosome assembly protein 1-like 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001356315
VERSION     NP_001356315.1
DBSOURCE    REFSEQ: accession NM_001369386.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Tan,L., Cheng,W., Liu,F., Wang,D.O., Wu,L., Cao,N. and Wang,J.
  TITLE     Positive natural selection of N6-methyladenosine on the RNAs of
            processed pseudogenes
  JOURNAL   Genome Biol 22 (1), 180 (2021)
   PUBMED   34120636
  REMARK    GeneRIF: Positive natural selection of N6-methyladenosine on the
            RNAs of processed pseudogenes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Mizuhashi,S., Fukushima,S., Ishibashi,T., Kuriyama,H., Kimura,T.,
            Kanemaru,H., Kajihara,I., Makino,K., Miyashita,A., Aoi,J., Kita,K.
            and Ihn,H.
  TITLE     Nucleosome assembly protein 1-like 4, a new therapeutic target for
            proliferation and invasion of melanoma cells
  JOURNAL   J Dermatol Sci 102 (1), 16-24 (2021)
   PUBMED   33583643
  REMARK    GeneRIF: Nucleosome assembly protein 1-like 4, a new therapeutic
            target for proliferation and invasion of melanoma cells.
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Tanaka,T., Hozumi,Y., Martelli,A.M., Iino,M. and Goto,K.
  TITLE     Nucleosome assembly proteins NAP1L1 and NAP1L4 modulate p53
            acetylation to regulate cell fate
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1866 (12), 118560 (2019)
   PUBMED   31634504
  REMARK    GeneRIF: The NAP1L4 regulates cell fate by controlling the
            expression of p53-responsive proarrest and proapoptotic genes
            through selective modulation of p53 acetylation at specific sites
            during normal homeostasis and in stress-induced responses.
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Tanaka,T., Hozumi,Y., Iino,M. and Goto,K.
  TITLE     NAP1L1 regulates NF-kappaB signaling pathway acting on
            anti-apoptotic Mcl-1 gene expression
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1864 (10), 1759-1768 (2017)
   PUBMED   28687276
  REMARK    GeneRIF: knockdown of NAP1L1 suppresses IkappaBalpha degradation
            and nuclear transport of p65 subunit after treatment with TNF-a
            stimulation, leading to attenuation of the NF-kappaB
            transcriptional activity, whereas NAP1L4 knockdown remains
            silent.results of this study suggest that NAP1L1 downregulation
            renders the cell vulnerable to apoptotic cell death through
            attenuation of NF-kappaB transcriptional activity on the
            anti-apop...
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Ruiz,M.T., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2 is part of multi-protein complexes in HeLa cells
  JOURNAL   J Cell Biochem 93 (2), 398-408 (2004)
   PUBMED   15368365
  REMARK    GeneRIF: NAP-2 is in complex(es) with other proteins, which are
            distinct from histones
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Shikama,N., Chan,H.M., Krstic-Demonacos,M., Smith,L., Lee,C.W.,
            Cairns,W. and La Thangue,N.B.
  TITLE     Functional interaction between nucleosome assembly proteins and
            p300/CREB-binding protein family coactivators
  JOURNAL   Mol Cell Biol 20 (23), 8933-8943 (2000)
   PUBMED   11073993
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Pelletier,J., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2: histone chaperone function and phosphorylation state through
            the cell cycle
  JOURNAL   J Mol Biol 298 (2), 225-238 (2000)
   PUBMED   10764593
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Munroe,D., Prawitt,D., Chu,L.L., Bric,E., Kim,J.,
            Reid,L.H., Davies,C., Nakagama,H., Loebbert,R., Winterpacht,A.,
            Petruzzi,M.J., Higgins,M.J., Nowak,N., Evans,G., Shows,T.,
            Weissman,B.E., Zabel,B., Housman,D.E. and Pelletier,J.
  TITLE     Functional characterization of human nucleosome assembly protein-2
            (NAP1L4) suggests a role as a histone chaperone
  JOURNAL   Genomics 44 (3), 253-265 (1997)
   PUBMED   9325046
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Hu,R.J., Lee,M.P., Johnson,L.A. and Feinberg,A.P.
  TITLE     A novel human homologue of yeast nucleosome assembly protein, 65 kb
            centromeric to the p57KIP2 gene, is biallelically expressed in
            fetal and adult tissues
  JOURNAL   Hum Mol Genet 5 (11), 1743-1748 (1996)
   PUBMED   8923002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC131971.9.
            
            Summary: This gene encodes a member of the nucleosome assembly
            protein (NAP) family which can interact with both core and linker
            histones. It can shuttle between the cytoplasm and nucleus,
            suggesting a role as a histone chaperone. This gene is one of
            several located near the imprinted gene domain of 11p15.5, an
            important tumor-suppressor gene region. Alterations in this region
            have been associated with the Beckwith-Wiedemann syndrome, Wilms
            tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung,
            ovarian, and breast cancer. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803611.245387.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..386
                     /product="nucleosome assembly protein 1-like 4 isoform 2"
                     /note="nucleosome assembly protein 2; nucleosome assembly
                     protein 1-like 4b; NAP-2"
                     /calculated_mol_wt=43948
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          65..338
                     /region_name="NAP"
                     /note="Nucleosome assembly protein (NAP); pfam00956"
                     /db_xref="CDD:460010"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P28656; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          116..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          265..271
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     CDS             1..386
                     /gene="NAP1L4"
                     /gene_synonym="hNAP2; NAP1L4b; NAP2; NAP2L"
                     /coded_by="NM_001369386.1:417..1577"
                     /note="isoform 2 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS91410.1"
                     /db_xref="GeneID:4676"
                     /db_xref="HGNC:HGNC:7640"
                     /db_xref="MIM:601651"
ORIGIN      
        1 madhsfsdgv psdsveaakn asntekltdq vmqnprvlaa lqerldnvph tpssyietlp
       61 kavkrrinal kqlqvrcahi eakfyeevhd lerkyaalyq plfdkrrefi tgdveptdae
      121 sewhseneee eklagdmksk vvvtekaaat aeepdpkgip efwftifrnv dmlselvqey
      181 depilkhlqd ikvkfsdpgq pmsfvlefhf epndyftnsv ltktykmkse pdkadpfsfe
      241 gpeivdcdgc tidwkkgknv tvktikkkqk hkgrgtvrti tkqvpnesff nffnplkasg
      301 dgesldedse ftlasdfeig hffrerivpr avlyftgeai edddnfeege egeeeelegd
      361 eegededdae inpkkepsqp aeckqq
//
LOCUS       NP_061198               1742 aa            linear   PRI 27-APR-2025
DEFINITION  unconventional myosin-Vc [Homo sapiens].
ACCESSION   NP_061198
VERSION     NP_061198.2
DBSOURCE    REFSEQ: accession NM_018728.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1742)
  AUTHORS   Holthenrich,A., Terglane,J., Nass,J., Mietkowska,M., Kerkhoff,E.
            and Gerke,V.
  TITLE     Spire1 and Myosin Vc promote Ca2+-evoked externalization of von
            Willebrand factor in endothelial cells
  JOURNAL   Cell Mol Life Sci 79 (2), 96 (2022)
   PUBMED   35084586
  REMARK    GeneRIF: Spire1 and Myosin Vc promote Ca(2+)-evoked externalization
            of von Willebrand factor in endothelial cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1742)
  AUTHORS   Tesolin,P., Fiorino,S., Lenarduzzi,S., Rubinato,E., Cattaruzzi,E.,
            Ammar,L., Castro,V., Orzan,E., Granata,C., Dell'Orco,D., Morgan,A.
            and Girotto,G.
  TITLE     Pendred Syndrome, or Not Pendred Syndrome? That Is the Question
  JOURNAL   Genes (Basel) 12 (10), 1569 (2021)
   PUBMED   34680964
  REMARK    GeneRIF: Pendred Syndrome, or Not Pendred Syndrome? That Is the
            Question.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1742)
  AUTHORS   Dolce,L.G., Ohbayashi,N., Silva,D.F.C.D., Ferrari,A.J.R.,
            Pirolla,R.A.S., Schwarzer,A.C.A.P., Zanphorlin,L.M., Cabral,L.,
            Fioramonte,M., Ramos,C.H.I., Gozzo,F.C., Fukuda,M., Giuseppe,P.O.
            and Murakami,M.T.
  TITLE     Unveiling the interaction between the molecular motor Myosin Vc and
            the small GTPase Rab3A
  JOURNAL   J Proteomics 212, 103549 (2020)
   PUBMED   31698103
  REMARK    GeneRIF: Unveiling the interaction between the molecular motor
            Myosin Vc and the small GTPase Rab3A.
REFERENCE   4  (residues 1 to 1742)
  AUTHORS   Sladewski,T.E., Krementsova,E.B. and Trybus,K.M.
  TITLE     Myosin Vc Is Specialized for Transport on a Secretory Superhighway
  JOURNAL   Curr Biol 26 (16), 2202-2207 (2016)
   PUBMED   27498562
  REMARK    GeneRIF: MyoVc is unique in taking variable size steps, which are
            frequently in the backward direction. Results obtained with
            chimeric constructs implicate the lever arm/rod of MyoVc as being
            responsible for these properties. Actin bundles allow single MyoVc
            motors to move processively.
REFERENCE   5  (residues 1 to 1742)
  AUTHORS   Wulf,S.F., Ropars,V., Fujita-Becker,S., Oster,M., Hofhaus,G.,
            Trabuco,L.G., Pylypenko,O., Sweeney,H.L., Houdusse,A.M. and
            Schroder,R.R.
  TITLE     Force-producing ADP state of myosin bound to actin
  JOURNAL   Proc Natl Acad Sci U S A 113 (13), E1844-E1852 (2016)
   PUBMED   26976594
  REMARK    GeneRIF: The myosin V structure reveals the detailed rearrangements
            underlying myosin force generation as well as the basis of
            strain-dependent ADP release that is essential for processive
            myosins, such as myosin V.
REFERENCE   6  (residues 1 to 1742)
  AUTHORS   Roland,J.T., Lapierre,L.A. and Goldenring,J.R.
  TITLE     Alternative splicing in class V myosins determines association with
            Rab10
  JOURNAL   J Biol Chem 284 (2), 1213-1223 (2009)
   PUBMED   19008234
  REMARK    GeneRIF: related Rab protein, Rab10, can interact with myosin Va,
            myosin Vb, and myosin Vc
REFERENCE   7  (residues 1 to 1742)
  AUTHORS   Watanabe,S., Watanabe,T.M., Sato,O., Awata,J., Homma,K., Umeki,N.,
            Higuchi,H., Ikebe,R. and Ikebe,M.
  TITLE     Human myosin Vc is a low duty ratio nonprocessive motor
  JOURNAL   J Biol Chem 283 (16), 10581-10592 (2008)
   PUBMED   18079121
  REMARK    GeneRIF: myosin Vc is a low duty ratio nonprocessive motor
REFERENCE   8  (residues 1 to 1742)
  AUTHORS   Takagi,Y., Yang,Y., Fujiwara,I., Jacobs,D., Cheney,R.E.,
            Sellers,J.R. and Kovacs,M.
  TITLE     Human myosin Vc is a low duty ratio, nonprocessive molecular motor
  JOURNAL   J Biol Chem 283 (13), 8527-8537 (2008)
   PUBMED   18201966
  REMARK    GeneRIF: Kinetic simulations reveal that the high ADP affinity of
            actomyosin Vc may lead to elevations of the duty ratio of myosin Vc
            to as high as 64% under possible physiological ADP concentrations
REFERENCE   9  (residues 1 to 1742)
  AUTHORS   Rodriguez,O.C. and Cheney,R.E.
  TITLE     Human myosin-Vc is a novel class V myosin expressed in epithelial
            cells
  JOURNAL   J Cell Sci 115 (Pt 5), 991-1004 (2002)
   PUBMED   11870218
REFERENCE   10 (residues 1 to 1742)
  AUTHORS   Bement,W.M., Hasson,T., Wirth,J.A., Cheney,R.E. and Mooseker,M.S.
  TITLE     Identification and overlapping expression of multiple
            unconventional myosin genes in vertebrate cell types
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6549-6553 (1994)
   PUBMED   8022818
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11767. doi:
            10.1073/pnas.91.24.11767-c. PMID: 7972138]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010674.11.
            
            On Jul 26, 2007 this sequence version replaced NP_061198.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF272390.1, SRR7346977.2792627.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261839.12/ ENSP00000261839.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1742
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.2"
     Protein         1..1742
                     /product="unconventional myosin-Vc"
                     /note="myosin 5C; myosin-Vc"
                     /calculated_mol_wt=202680
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.4;
                     propagated from UniProtKB/Swiss-Prot (Q9NQX4.2)"
     Region          81..741
                     /region_name="MYSc_Myo5"
                     /note="class V myosin, motor domain; cd01380"
                     /db_xref="CDD:276831"
     Site            order(109..117,161..168,207..217,435..440)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276831"
     Site            109..117
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276831"
     Site            161..168
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276831"
     Site            207..217
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276831"
     Site            435..443
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276831"
     Site            order(464..475,478..487)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276831"
     Region          632..654
                     /region_name="Actin-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00782"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQX4.2)"
     Site            674..684
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276831"
     Site            order(695..705,726..741)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276831"
     Region          810..828
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     Region          831..851
                     /region_name="IQ"
                     /note="IQ calmodulin-binding motif; pfam00612"
                     /db_xref="CDD:459869"
     Region          <886..>1356
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1369..1736
                     /region_name="Myo5c_CBD"
                     /note="Cargo binding domain of myosin 5C; cd15476"
                     /db_xref="CDD:271260"
     CDS             1..1742
                     /gene="MYO5C"
                     /coded_by="NM_018728.4:169..5397"
                     /db_xref="CCDS:CCDS42036.1"
                     /db_xref="GeneID:55930"
                     /db_xref="HGNC:HGNC:7604"
                     /db_xref="MIM:610022"
ORIGIN      
        1 mavaelytqy nrvwipdpee vwksaeiakd yrvgdkvlrl lledgteldy svnpeslppl
       61 rnpdilvgen dltalsylhe pavlhnlrir faeskliyty sgiilvamnp ykqlpiygda
      121 iihaysgqnm gdmdphifav aeeaykqmar nnrnqsiivs gesgagktvs aryamryfat
      181 vsksgsnahv edkvlasnpi teavgnaktt rndnssrfgk yteisfdeqn qiiganmsty
      241 lleksrvvfq senernyhif yqlcasaqqs efkhlklgsa eefnytrmgg ntviegvndr
      301 aemvetqktf tllgfkedfq mdvfkilaai lhlgnvqita vgnerssvse ddshlkvfce
      361 llglesgrva qwlcnrkivt ssetvvkpmt rpqavnarda lakkiyahlf dfiverinqa
      421 lqfsgkqhtf igvldiygfe tfdvnsfeqf cinyaneklq qqfnmhvfkl eqeeymkedi
      481 pwtlidfydn qpvidlieak mgilelldee cllphgtden wlqklynnfv nrnplfekpr
      541 msntsfviqh fadkveykce gfleknrdtv ydmlveilra skfhlcanff qenptppspf
      601 gsmitvksak qvikpnskhf rttvgskfrs slyllmetln attphyvrci kpndeklpfe
      661 fdskrivqql racgvletir isaqsypsrw tyiefysryg ilmtkqelsf sdkkevckvv
      721 lhrliqdsnq yqfgktkiff ragqvaylek lrldklrqsc vmvqkhmrgw lqrkkflrer
      781 raaliiqqyf rgqqtvrkai tavalkeawa aiiiqkhcrg ylvrslyqli rmatitmqay
      841 srgflarrry rkmleehkav ilqkyarawl arrrfqsirr fvlniqltyr vqrlqkkled
      901 qnkenhglve kltslaalra gdvekiqkle aelekaathr rnyeekgkry rdaveeklak
      961 lqkhnselet qkeqiqlklq ekteelkekm dnltkqlfdd vqkeerqrml leksfelktq
     1021 dyekqiqslk eeikalkdek mqlqhlvege hvtsdglkae varlskqvkt isefekeiel
     1081 lqaqkidvek hvqsqkremr ekmseitkql lesydiedvr srlsvedleh lnedgelwfa
     1141 yeglkkatrv leshfqsqkd cyekeiealn fkvvhlsqei nhlqklfree ndinesirhe
     1201 vtrltsenmm ipdfkqqise lekqkqdlei rlneqaekmk gkleelsnql hrsqeeegtq
     1261 rkaleaqnei htkekeklid kiqemqeasd hlkkqfetes evkcnfrqea srltlenrdl
     1321 eeeldmkdrv ikklqdqvkt lsktigkand vhsssgpkey lgmlqykred eakliqnlil
     1381 dlkprgvvvn mipglpahil fmcvryadsl ndanmlkslm nstingikqv vkehledfem
     1441 lsfwlsntch flnclkqysg eeefmkhnsp qqnknclnnf dlseyrqils dvairiyhqf
     1501 iiimekniqp iivpgmleye slqgisglkp tgfrkrsssi ddtdgytmts vlqqlsyfyt
     1561 tmcqngldpe lvrqavkqlf fligavtlns lflrkdmcsc rkgmqircni syleewlkdk
     1621 nlqnslaket leplsqaawl lqvkkttdsd akeiyercts lsavqiikil nsytpiddfe
     1681 krvtpsfvrk vqallnsred ssqlmldtky lfqvtfpftp sphalemiqi pssfklgfln
     1741 rl
//
LOCUS       NP_776504                552 aa            linear   MAM 27-APR-2025
DEFINITION  hyaluronan synthase 2 [Bos taurus].
ACCESSION   NP_776504
VERSION     NP_776504.2
DBSOURCE    REFSEQ: accession NM_174079.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Lopes,E.F., Marques,L.S., Duranti,R.G., de Oliveira,A.T.,
            Lopes,R.F. and Rodrigues,J.L.
  TITLE     Gene Expression of Monocarboxylate Transporters and Oocyte-secreted
            Factors in Bovine Cumulus-oocyte Complexes Selected by Brilliant
            Cresyl Blue
  JOURNAL   Reprod Domest Anim 50 (5), 763-770 (2015)
   PUBMED   26280459
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Usui,T., Suzuki,K., Kaji,Y., Amano,S., Miyata,K., Heldin,P. and
            Yamashita,H.
  TITLE     Hyaluronan synthase expression in bovine eyes
  JOURNAL   Invest Ophthalmol Vis Sci 40 (3), 563-567 (1999)
   PUBMED   10067958
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000014.1.
            
            On Jan 18, 2018 this sequence version replaced NP_776504.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ004951.1, SRR5721698.14185.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA6648753, SAMEA6648754
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="14"
                     /map="14"
                     /breed="Hereford"
     Protein         1..552
                     /product="hyaluronan synthase 2"
                     /EC_number="2.4.1.212"
                     /note="HA synthase 2; hyaluronate synthase 2; hyaluronic
                     acid synthase 2"
                     /calculated_mol_wt=63352
     Site            12..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O97711.1)"
     Site            46..66
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O97711.1)"
     Region          84..361
                     /region_name="GT2_HAS"
                     /note="Hyaluronan synthases catalyze polymerization of
                     hyaluronan; cd06434"
                     /db_xref="CDD:133056"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q92819; propagated from
                     UniProtKB/Swiss-Prot (O97711.1)"
     Site            212..214
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133056"
     Site            221
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:Q92819; propagated from
                     UniProtKB/Swiss-Prot (O97711.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q92819; propagated from
                     UniProtKB/Swiss-Prot (O97711.1)"
     Site            375..395
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O97711.1)"
     Site            403..423
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O97711.1)"
     Site            430..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O97711.1)"
     Site            476..496
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O97711.1)"
     Site            511..531
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O97711.1)"
     CDS             1..552
                     /gene="HAS2"
                     /coded_by="NM_174079.3:544..2202"
                     /db_xref="BGD:BT12058"
                     /db_xref="GeneID:281220"
                     /db_xref="VGNC:VGNC:29755"
ORIGIN      
        1 mhcerflcil riigttlfgv slllgitaay ivgyqfiqtd nyyfsfglyg aflashliiq
       61 slfaflehrk mkksletpik lnktvalcia ayqedpdylr kclqsvkrlt ypgikvvmvi
      121 dgnseddlym mdifsevmgr dksatyiwkn nyhvkgpget deshkessqh vtqlvlsnks
      181 icimqkwggk revmytafra lgrsvdyvqv cdsdtmldpa ssvemvkvle edpmvggvgg
      241 dvqilnkyds wisflssvry wmafnierac qsyfgcvqci sgplgmyrns llhefvedwy
      301 nqefmgsqcs fgddrhltnr vlslgyatky tarskcltet pieylrwlnq qtrwsksyfr
      361 ewlynamwfh khhlwmtyea vitgffpffl iatviqlfyr gkiwnillfl ltvqlvglik
      421 ssfasclrgn ivmvfmslys vlymssllpa kmfaiatink agwgtsgrkt ivvnfiglip
      481 vsvwftillg gviftiykes kkpfseskqt vlivgtllya cywvmlltly vvlinkcgrr
      541 kkgqqydmvl dv
//
LOCUS       NP_057153                125 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit TIM16 [Homo
            sapiens].
ACCESSION   NP_057153
VERSION     NP_057153.8
DBSOURCE    REFSEQ: accession NM_016069.11
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Waingankar,T.P. and D'Silva,P.
  TITLE     Multiple variants of the human presequence translocase motor
            subunit Magmas govern the mitochondrial import
  JOURNAL   J Biol Chem 297 (6), 101349 (2021)
   PUBMED   34715125
  REMARK    GeneRIF: Multiple variants of the human presequence translocase
            motor subunit Magmas govern the mitochondrial import.
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Di,K., Lomeli,N., Bota,D.A. and Das,B.C.
  TITLE     Magmas inhibition as a potential treatment strategy in malignant
            glioma
  JOURNAL   J Neurooncol 141 (2), 267-276 (2019)
   PUBMED   30414099
  REMARK    GeneRIF: Findings demonstrate that Magmas is overexpressed in
            tissue sections from glioma patients and xenografts. In vivo
            studies showed that a novel Magmas small molecule inhibitor, BT#9,
            could cross the BBB in mice. In vitro studies revealed that BT#9
            significantly decreased cell proliferation, induced apoptosis, and
            blocked migration and invasion.
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Sinha,D., Joshi,N., Chittoor,B., Samji,P. and D'Silva,P.
  TITLE     Role of Magmas in protein transport and human mitochondria
            biogenesis
  JOURNAL   Hum Mol Genet 19 (7), 1248-1262 (2010)
   PUBMED   20053669
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Elsner,S., Simian,D., Iosefson,O., Marom,M. and Azem,A.
  TITLE     The mitochondrial protein translocation motor: structural
            conservation between the human and yeast Tim14/Pam18-Tim16/Pam16
            co-chaperones
  JOURNAL   Int J Mol Sci 10 (5), 2041-2053 (2009)
   PUBMED   19564938
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Jubinsky,P.T., Short,M.K., Mutema,G., Morris,R.E., Ciraolo,G.M. and
            Li,M.
  TITLE     Magmas expression in neoplastic human prostate
  JOURNAL   J Mol Histol 36 (1-2), 69-75 (2005)
   PUBMED   15704001
  REMARK    GeneRIF: Magmas expression in prostate cancer.
REFERENCE   9  (residues 1 to 125)
  AUTHORS   Jubinsky,P.T., Messer,A., Bender,J., Morris,R.E., Ciraolo,G.M.,
            Witte,D.P., Hawley,R.G. and Short,M.K.
  TITLE     Identification and characterization of Magmas, a novel
            mitochondria-associated protein involved in granulocyte-macrophage
            colony-stimulating factor signal transduction
  JOURNAL   Exp Hematol 29 (12), 1392-1402 (2001)
   PUBMED   11750097
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Bauer,M.F., Gempel,K., Reichert,A.S., Rappold,G.A., Lichtner,P.,
            Gerbitz,K.D., Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     Genetic and structural characterization of the human mitochondrial
            inner membrane translocase
  JOURNAL   J Mol Biol 289 (1), 69-82 (1999)
   PUBMED   10339406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG715429.1 and AK026514.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 23, 2002 this sequence version replaced NP_057153.7.
            
            Summary: This gene encodes a mitochondrial protein involved in
            granulocyte-macrophage colony-stimulating factor (GM-CSF)
            signaling. This protein also plays a role in the import of
            nuclear-encoded mitochondrial proteins into the mitochondrial
            matrix and may be important in reactive oxygen species (ROS)
            homeostasis. Mutations in this gene cause Megarbane-Dagher-Melike
            type spondylometaphyseal dysplasia, an early lethal skeletal
            dysplasia characterized by short stature, developmental delay and
            other skeletal abnormalities. [provided by RefSeq, May 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026514.1, BP317921.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000318059.8/
                                                  ENSP00000315693.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..125
                     /product="mitochondrial import inner membrane translocase
                     subunit TIM16"
                     /note="mitochondria associated protein involved in
                     granulocyte macrophage colony stimulating factor signal
                     transduction; magmas-like protein; mitochondria-associated
                     granulocyte macrophage CSF-signaling molecule; presequence
                     translocase associated motor 16 homolog"
                     /calculated_mol_wt=13694
     Region          1..125
                     /region_name="Pam16"
                     /note="pfam03656"
                     /db_xref="CDD:252088"
     Region          58..110
                     /region_name="J-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3D7.2)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQV1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3D7.2)"
     CDS             1..125
                     /gene="PAM16"
                     /gene_synonym="CGI-136; MAGMAS; SMDMDM; TIM16; TIMM16"
                     /coded_by="NM_016069.11:88..465"
                     /db_xref="CCDS:CCDS10512.1"
                     /db_xref="GeneID:51025"
                     /db_xref="HGNC:HGNC:29679"
                     /db_xref="MIM:614336"
ORIGIN      
        1 makylaqiiv mgvqvvgraf aralrqefaa sraaadargr aghrsaaasn lsglslqeaq
       61 qilnvsklsp eevqknyehl fkvndksvgg sfylqskvvr akerldeelk iqaqedrekg
      121 qmpht
//
LOCUS       NP_001350477             406 aa            linear   PRI 27-APR-2025
DEFINITION  sialic acid-binding Ig-like lectin 8 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001350477 XP_011525037
VERSION     NP_001350477.1
DBSOURCE    REFSEQ: accession NM_001363548.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Li,T.A., Gonzalez-Gil,A., Awol,A.K., Ackerman,S.J., Orsburn,B.C.
            and Schnaar,R.L.
  TITLE     Sialylated keratan sulfates on MUC5B are Siglec-8 ligands in the
            human esophagus
  JOURNAL   Glycobiology 34 (10) (2024)
   PUBMED   39173029
  REMARK    GeneRIF: Sialylated keratan sulfates on MUC5B are Siglec-8 ligands
            in the human esophagus.
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Lee,H.S., Gonzalez-Gil,A., Drake,V., Li,T.A., Schnaar,R.L. and
            Kim,J.
  TITLE     Induction of the endogenous sialoglycan ligand for eosinophil death
            receptor Siglec-8 in chronic rhinosinusitis with hyperplastic nasal
            polyposis
  JOURNAL   Glycobiology 31 (8), 1026-1036 (2021)
   PUBMED   33755113
  REMARK    GeneRIF: Induction of the endogenous sialoglycan ligand for
            eosinophil death receptor Siglec-8 in chronic rhinosinusitis with
            hyperplastic nasal polyposis.
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Trebo,A., Ditsch,N., Degenhardt,T., Kuhn,C., Rahmeh,M.,
            Schmoeckel,E., Mayr,D., Czogalla,B., Kolben,T., Meister,S.,
            Mahner,S., Jeschke,U. and Hester,A.
  TITLE     First Evidence for a Role of Siglec-8 in Breast Cancer
  JOURNAL   Int J Mol Sci 22 (4), 2000 (2021)
   PUBMED   33670444
  REMARK    GeneRIF: First Evidence for a Role of Siglec-8 in Breast Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Sajay-Asbaghi,M., Sadeghi-Shabestrai,M., Monfaredan,A.,
            Seyfizadeh,N., Razavi,A. and Kazemi,T.
  TITLE     Promoter region single nucleotide polymorphism of siglec-8 gene
            associates with susceptibility to allergic asthma
  JOURNAL   Per Med 17 (3), 195-201 (2020)
   PUBMED   32077788
  REMARK    GeneRIF: Promoter region single nucleotide polymorphism of siglec-8
            gene associates with susceptibility to allergic asthma.
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Legrand,F., Cao,Y., Wechsler,J.B., Zhu,X., Zimmermann,N.,
            Rampertaap,S., Monsale,J., Romito,K., Youngblood,B.A., Brock,E.C.,
            Makiya,M.A., Tomasevic,N., Bebbington,C., Maric,I., Metcalfe,D.D.,
            Bochner,B.S. and Klion,A.D.
  TITLE     Sialic acid-binding immunoglobulin-like lectin (Siglec) 8 in
            patients with eosinophilic disorders: Receptor expression and
            targeting using chimeric antibodies
  JOURNAL   J Allergy Clin Immunol 143 (6), 2227-2237 (2019)
   PUBMED   30543818
  REMARK    GeneRIF: Siglec-8 is highly expressed on blood eosinophils from
            eosinophilic donors and normal donors and represents a potential
            therapeutic target for eosinophilic disorders
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Nutku,E., Aizawa,H., Hudson,S.A. and Bochner,B.S.
  TITLE     Ligation of Siglec-8: a selective mechanism for induction of human
            eosinophil apoptosis
  JOURNAL   Blood 101 (12), 5014-5020 (2003)
   PUBMED   12609831
  REMARK    GeneRIF: Sialic acid binding immunoglobulin-like lectin 8
            (Siglec-8) cross-linking with antibodies rapidly generated
            caspase-3-like activity and reduced eosinophil viability through
            induction of apoptosis
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Munday,J., Kerr,S., Ni,J., Cornish,A.L., Zhang,J.Q., Nicoll,G.,
            Floyd,H., Mattei,M.G., Moore,P., Liu,D. and Crocker,P.R.
  TITLE     Identification, characterization and leucocyte expression of
            Siglec-10, a novel human sialic acid-binding receptor
  JOURNAL   Biochem J 355 (Pt 2), 489-497 (2001)
   PUBMED   11284738
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Foussias,G., Yousef,G.M. and Diamandis,E.P.
  TITLE     Molecular characterization of a Siglec8 variant containing
            cytoplasmic tyrosine-based motifs, and mapping of the Siglec8 gene
  JOURNAL   Biochem Biophys Res Commun 278 (3), 775-781 (2000)
   PUBMED   11095983
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Kikly,K.K., Bochner,B.S., Freeman,S.D., Tan,K.B., Gallagher,K.T.,
            D'alessio,K.J., Holmes,S.D., Abrahamson,J.A., Erickson-Miller,C.L.,
            Murdock,P.R., Tachimoto,H., Schleimer,R.P. and White,J.R.
  TITLE     Identification of SAF-2, a novel siglec expressed on eosinophils,
            mast cells, and basophils
  JOURNAL   J Allergy Clin Immunol 105 (6 Pt 1), 1093-1100 (2000)
   PUBMED   10856141
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Floyd,H., Ni,J., Cornish,A.L., Zeng,Z., Liu,D., Carter,K.C.,
            Steel,J. and Crocker,P.R.
  TITLE     Siglec-8. A novel eosinophil-specific member of the immunoglobulin
            superfamily
  JOURNAL   J Biol Chem 275 (2), 861-866 (2000)
   PUBMED   10625619
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA388103.1, BC053319.1, BP309940.1 and AF195092.1.
            
            On May 24, 2018 this sequence version replaced XP_011525037.1.
            
            Summary: Sialic acid-binding immunoglobulin (Ig)-like lectins, or
            SIGLECs (e.g., CD33 (MIM 159590)), are a family of type 1
            transmembrane proteins each having a unique expression pattern,
            mostly in hemopoietic cells. SIGLEC8 is a member of the CD33-like
            subgroup of SIGLECs, which are localized to 19q13.3-q13.4 and have
            2 conserved cytoplasmic tyrosine-based motifs: an immunoreceptor
            tyrosine-based inhibitory motif, or ITIM (see MIM 604964), and a
            motif homologous to one identified in signaling lymphocyte
            activation molecule (SLAM; MIM 603492) that mediates an association
            with SLAM-associated protein (SAP; MIM 300490) (summarized by
            Foussias et al., 2000 [PubMed 11095983]).[supplied by OMIM, May
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.592987.1,
                                           SRR1803613.128924.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..406
                     /product="sialic acid-binding Ig-like lectin 8 isoform 2
                     precursor"
                     /note="SAF-2; CDw329; sialoadhesin family member 2"
                     /calculated_mol_wt=42584
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1794
     Region          27..151
                     /region_name="IgV_CD33"
                     /note="Immunoglobulin Variable (IgV) domain at the
                     N-terminus of CD33 and related Siglecs (sialic
                     acid-binding Ig-like lectins); cd05712"
                     /db_xref="CDD:409377"
     Region          27..51
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409377"
     Region          27..31
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409377"
     Region          34..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409377"
     Region          40..51
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409377"
     Region          52..61
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409377"
     Region          62..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409377"
     Region          62..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409377"
     Region          70..93
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409377"
     Region          80..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409377"
     Region          94..127
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409377"
     Region          95..99
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409377"
     Region          105..113
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409377"
     Region          120..128
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409377"
     Site            order(125,133..134)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409377"
     Region          128..131
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409377"
     Region          132..151
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409377"
     Region          132..151
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409377"
     Region          175..253
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          186..190
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          199..203
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          221..225
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          232..237
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          247..250
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..406
                     /gene="SIGLEC8"
                     /gene_synonym="SAF2; SIGLEC-8; SIGLEC8L"
                     /coded_by="NM_001363548.1:68..1288"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS86797.1"
                     /db_xref="GeneID:27181"
                     /db_xref="HGNC:HGNC:10877"
                     /db_xref="MIM:605639"
ORIGIN      
        1 mlllllllpl lwgtkgmegd rqygdgyllq vqelvtvqeg lcvhvpcsfs ypqdgwtdsd
       61 pvhgywfrag drpyqdapva tnnpdrevqa etqgrfqllg diwsndcsls irdarkrdkg
      121 syffrlergs mkwsyksqln yktkqlsvfv tdppwnltmt vfqgdatast algngsslsv
      181 legqslrlvc avnsnpparl swtrgsltlc psrssnpgll elprvhvrde geftcraqna
      241 qgsqhislsl slqnegtgts rpvsqvtlaa vggagatala flsfciifii vrscrkksar
      301 paagvgdtgm edakairgsa sqgplteswk dgnplkkppp avapssgeeg elhyatlsfh
      361 kvkpqdpqgq eatdseysei kihkretaet qaclrnhnps skevrg
//
LOCUS       NP_002483                189 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5,
            mitochondrial isoform 1 precursor [Homo sapiens].
ACCESSION   NP_002483
VERSION     NP_002483.1
DBSOURCE    REFSEQ: accession NM_002492.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Wang,T., Li,X., Tao,Y., Wang,X., Li,L. and Liu,J.
  TITLE     METTL3-mediated NDUFB5 m6A modification promotes cell migration and
            mitochondrial respiration to promote the wound healing of diabetic
            foot ulcer
  JOURNAL   J Transl Med 22 (1), 643 (2024)
   PUBMED   38982516
  REMARK    GeneRIF: METTL3-mediated NDUFB5 m6A modification promotes cell
            migration and mitochondrial respiration to promote the wound
            healing of diabetic foot ulcer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Kang,K., Li,J., Li,R., Xu,X., Liu,J., Qin,L., Huang,T., Wu,J.,
            Jiao,M., Wei,M., Wang,H., Wang,T. and Zhang,Q.
  TITLE     Potentially Critical Roles of NDUFB5, TIMMDC1, and VDAC3 in the
            Progression of Septic Cardiomyopathy Through Integrated
            Bioinformatics Analysis
  JOURNAL   DNA Cell Biol 39 (1), 105-117 (2020)
   PUBMED   31794266
  REMARK    GeneRIF: Data suggest that the hub genes NADH:ubiquinone
            oxidoreductase subunit B5 (NDUFB5), translocase of inner
            mitochondrial membrane domain containing 1 (TIMMDC1), and
            voltage-dependent anion channel 3 (VDAC3) might serve as potential
            biomarkers for diagnosis and/or therapeutic targets for precise
            treatment of septic cardiomyopathy (SC) .
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Starr,J.M., Shiels,P.G., Harris,S.E., Pattie,A., Pearce,M.S.,
            Relton,C.L. and Deary,I.J.
  TITLE     Oxidative stress, telomere length and biomarkers of physical aging
            in a cohort aged 79 years from the 1932 Scottish Mental Survey
  JOURNAL   Mech Ageing Dev 129 (12), 745-751 (2008)
   PUBMED   18977241
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 189)
  AUTHORS   Harris,S.E., Fox,H., Wright,A.F., Hayward,C., Starr,J.M.,
            Whalley,L.J. and Deary,I.J.
  TITLE     A genetic association analysis of cognitive ability and cognitive
            ageing using 325 markers for 109 genes associated with oxidative
            stress or cognition
  JOURNAL   BMC Genet 8, 43 (2007)
   PUBMED   17601350
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 189)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   9  (residues 1 to 189)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   10 (residues 1 to 189)
  AUTHORS   Ton,C., Hwang,D.M., Dempsey,A.A. and Liew,C.C.
  TITLE     Identification and primary structure of five human NADH-ubiquinone
            oxidoreductase subunits
  JOURNAL   Biochem Biophys Res Commun 241 (2), 589-594 (1997)
   PUBMED   9425316
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA112751.1, BC009796.1,
            CD364869.1 and AC090425.15.
            
            Summary: The protein encoded by this gene is a subunit of the
            multisubunit NADH:ubiquinone oxidoreductase (complex I). Mammalian
            complex I is composed of 45 different subunits. It locates at the
            mitochondrial inner membrane. This protein has NADH dehydrogenase
            activity and oxidoreductase activity. It transfers electrons from
            NADH to the respiratory chain. The immediate electron acceptor for
            the enzyme is believed to be ubiquinone. Three transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BF575756.1, SRR1803615.98981.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000259037.8/
                                                  ENSP00000259037.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.33"
     Protein         1..189
                     /product="NADH dehydrogenase [ubiquinone] 1 beta
                     subcomplex subunit 5, mitochondrial isoform 1 precursor"
                     /EC_number="7.1.1.2"
                     /EC_number="1.6.99.3"
                     /note="complex I SGDH subunit; NADH-ubiquinone
                     oxidoreductase SGDH subunit; complex I-SGDH; NADH
                     dehydrogenase (ubiquinone) 1 beta subcomplex, 5, 16kDa"
                     /calculated_mol_wt=17002
     Region          1..189
                     /region_name="NDUF_B5"
                     /note="NADH:ubiquinone oxidoreductase, NDUFB5/SGDH
                     subunit; pfam09781"
                     /db_xref="CDD:430820"
     transit_peptide 1..46
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (O43674.1)"
                     /calculated_mol_wt=4767
     mat_peptide     47..189
                     /product="NADH dehydrogenase [ubiquinone] 1 beta
                     subcomplex subunit 5, mitochondrial. /id=PRO_0000020052"
                     /note="propagated from UniProtKB/Swiss-Prot (O43674.1)"
                     /calculated_mol_wt=17002
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43674.1)"
     CDS             1..189
                     /gene="NDUFB5"
                     /gene_synonym="CISGDH; SGDH"
                     /coded_by="NM_002492.4:23..592"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3234.1"
                     /db_xref="GeneID:4711"
                     /db_xref="HGNC:HGNC:7700"
                     /db_xref="MIM:603841"
ORIGIN      
        1 maamsllrrv svtavaalsg rplgtrlgfg gfltrgfpka aapvrhsgdh gkrlfvirps
       61 rfydrrflkl lrfyialtgi pvaifitlvn vfigqaelae ipegyvpehw eyykhpisrw
      121 iarnfydspe kiyertmavl qieaekaelr vkelevrklm hvrgdgpwyy yetidkelid
      181 hspkatpdn
//
LOCUS       NP_061946                488 aa            linear   PRI 27-APR-2025
DEFINITION  spermatogenesis-associated protein 6 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_061946
VERSION     NP_061946.1
DBSOURCE    REFSEQ: accession NM_019073.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Wang,X., Jiang,C., Dai,S., Shen,G., Yang,Y. and Shen,Y.
  TITLE     Identification of nonfunctional SPATA20 causing acephalic
            spermatozoa syndrome in humans
  JOURNAL   Clin Genet 103 (3), 310-319 (2023)
   PUBMED   36415156
  REMARK    GeneRIF: Identification of nonfunctional SPATA20 causing acephalic
            spermatozoa syndrome in humans.
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Sujit,K.M., Singh,V., Trivedi,S., Singh,K., Gupta,G. and
            Rajender,S.
  TITLE     Increased DNA methylation in the spermatogenesis-associated (SPATA)
            genes correlates with infertility
  JOURNAL   Andrology 8 (3), 602-609 (2020)
   PUBMED   31838782
  REMARK    GeneRIF: Increased DNA methylation in the
            spermatogenesis-associated (SPATA) genes correlates with
            infertility.
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Huo,S., Du,W., Shi,P., Si,Y. and Zhao,S.
  TITLE     The role of spermatogenesis-associated protein 6 in testicular germ
            cell tumors
  JOURNAL   Int J Clin Exp Pathol 8 (8), 9119-9125 (2015)
   PUBMED   26464655
  REMARK    GeneRIF: SPATA6 may play an important role in testicular germ cell
            tumors, and down-regulation of SPATA6 could lead to apoptosis of
            testicular germ cell tumors.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 488)
  AUTHORS   Ficarro,S., Chertihin,O., Westbrook,V.A., White,F., Jayes,F.,
            Kalab,P., Marto,J.A., Shabanowitz,J., Herr,J.C., Hunt,D.F. and
            Visconti,P.E.
  TITLE     Phosphoproteome analysis of capacitated human sperm. Evidence of
            tyrosine phosphorylation of a kinase-anchoring protein 3 and
            valosin-containing protein/p97 during capacitation
  JOURNAL   J Biol Chem 278 (13), 11579-11589 (2003)
   PUBMED   12509440
REFERENCE   7  (residues 1 to 488)
  AUTHORS   Yamano,Y., Ohyama,K., Sano,T., Ohta,M., Shimada,A., Hirakawa,Y.,
            Sugimoto,M. and Morishima,I.
  TITLE     A novel spermatogenesis-related factor-1 gene expressed in maturing
            rat testis
  JOURNAL   Biochem Biophys Res Commun 289 (4), 888-893 (2001)
   PUBMED   11735130
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL356968.41, AK000869.1, AL359959.9 and BC040655.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.218080.1,
                                           SRR1660803.42446.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371847.8/ ENSP00000360913.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p33"
     Protein         1..488
                     /product="spermatogenesis-associated protein 6 isoform 1
                     precursor"
                     /note="spermatogenesis-associated protein 6;
                     spermatogenesis-related factor-1; testicular tissue
                     protein Li 178"
                     /calculated_mol_wt=53902
     sig_peptide     1..20
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
                     /calculated_mol_wt=2106
     Region          11..149
                     /region_name="SPATA6"
                     /note="Spermatogenesis-assoc protein 6; pfam14909"
                     /db_xref="CDD:464365"
     mat_peptide     21..488
                     /product="Spermatogenesis-associated protein 6.
                     /id=PRO_0000278441"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWH7.1)"
                     /calculated_mol_wt=53902
     Region          176..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:12509440; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:12509440; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Region          256..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U6K5; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MU5; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH7.1)"
     CDS             1..488
                     /gene="SPATA6"
                     /gene_synonym="HASH; SRF-1; SRF1"
                     /coded_by="NM_019073.4:197..1663"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS551.1"
                     /db_xref="GeneID:54558"
                     /db_xref="HGNC:HGNC:18309"
                     /db_xref="MIM:613947"
ORIGIN      
        1 mpkvkalqca laleissvtc pgvvlkdked iylsicvfgq ykktqcvpat fplvfnarmv
       61 fekvfpdavd pgdvvtqley dtavfeliql vppvgetlst ydentrdfmf pgpnqmsghh
      121 dsnrqvtmrr isglrgnapr lefsttsvit eclissrkch tqdkfiyhla pvekshgrlq
      181 nrtsrsqkkk sksperskyc inaknyeqpt isskshspsp ytkrrmcels edtrrrlahl
      241 nlgpyefkke tdkppfvirh vdppspradt llgssgrdce rdgwsrvhnd hshlgccrpk
      301 dykvirtphg rdfddslekc eeylsprscs kprhsartll vhsapstmpk hspspvlnra
      361 slrerfhsdw cspsncdeih drvknvlksh qahqrhlyde rdlekddele lkrsllcrds
      421 aydsdpeyss cqqprgtfhl ddgeywsnra asykgkshrp ifensmdkmy rnlykkacss
      481 ashtqesf
//
LOCUS       NP_766115                170 aa            linear   ROD 27-APR-2025
DEFINITION  nucleotide triphosphate diphosphatase NUDT15 [Mus musculus].
ACCESSION   NP_766115 XP_919600
VERSION     NP_766115.1
DBSOURCE    REFSEQ: accession NM_172527.3
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Wang,J., Zhang,Y., Li,L., Wang,L., Sun,S., Wang,B., Ge,Y. and
            Zhang,Z.
  TITLE     Nudt15-mediated inflammatory signaling contributes to divergent
            outcomes in leukemogenesis and hematopoiesis
  JOURNAL   Leukemia 38 (9), 1958-1970 (2024)
   PUBMED   39025986
  REMARK    GeneRIF: Nudt15-mediated inflammatory signaling contributes to
            divergent outcomes in leukemogenesis and hematopoiesis.
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Yamashita,N., Kawahara,M., Imai,T., Tatsumi,G., Asai-Nishishita,A.
            and Andoh,A.
  TITLE     Loss of Nudt15 thiopurine detoxification increases direct DNA
            damage in hematopoietic stem cells
  JOURNAL   Sci Rep 13 (1), 11908 (2023)
   PUBMED   37488179
  REMARK    GeneRIF: Loss of Nudt15 thiopurine detoxification increases direct
            DNA damage in hematopoietic stem cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Imai,T., Kawahara,M., Tatsumi,G., Yamashita,N., Nishishita-Asai,A.,
            Inatomi,O., Masamune,A., Kakuta,Y. and Andoh,A.
  TITLE     Thiopurine Use During Pregnancy Has Deleterious Effects on
            Offspring in Nudt15R138C Knock-In Mice
  JOURNAL   Cell Mol Gastroenterol Hepatol 12 (1), 335-337 (2021)
   PUBMED   33766784
  REMARK    Review article
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Tatsumi,G., Kawahara,M., Imai,T., Nishishita-Asai,A., Nishida,A.,
            Inatomi,O., Yokoyama,A., Kakuta,Y., Kito,K. and Andoh,A.
  TITLE     Thiopurine-mediated impairment of hematopoietic stem and leukemia
            cells in Nudt15R138C knock-in mice
  JOURNAL   Leukemia 34 (3), 882-894 (2020)
   PUBMED   31645647
  REMARK    GeneRIF: Thiopurine-mediated impairment of hematopoietic stem and
            leukemia cells in Nudt15(R138C) knock-in mice.
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Zheng,J.D., Hei,A.L., Zuo,P.P., Dong,Y.L., Song,X.N., Takagi,Y.,
            Sekiguchi,M. and Cai,J.P.
  TITLE     Age-related alterations in the expression of MTH2 in the
            hippocampus of the SAMP8 mouse with learning and memory
            deterioration
  JOURNAL   J Neurol Sci 287 (1-2), 188-196 (2009)
   PUBMED   19735921
  REMARK    GeneRIF: These results suggest that the MTH2 deficiency might be
            one of the causative factors for accelerated aging.
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Lau,N.C., Seto,A.G., Kim,J., Kuramochi-Miyagawa,S., Nakano,T.,
            Bartel,D.P. and Kingston,R.E.
  TITLE     Characterization of the piRNA complex from rat testes
  JOURNAL   Science 313 (5785), 363-367 (2006)
   PUBMED   16778019
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Cai,J.P., Ishibashi,T., Takagi,Y., Hayakawa,H. and Sekiguchi,M.
  TITLE     Mouse MTH2 protein which prevents mutations caused by 8-oxoguanine
            nucleotides
  JOURNAL   Biochem Biophys Res Commun 305 (4), 1073-1077 (2003)
   PUBMED   12767940
  REMARK    GeneRIF: MTH2 has a potential to protect the genetic material from
            the untoward effects of endogenous oxygen radicals; MTH2 could act
            as an MTH1 redundancy factor [MTH2]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK040749.1, AK032657.1, AC113198.15 and AK043196.1.
            
            On Dec 7, 2005 this sequence version replaced XP_919600.1.
            
            Transcript Variant: This variant (2) differs in its 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK040749.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN01164132
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 39.06 cM"
     Protein         1..170
                     /product="nucleotide triphosphate diphosphatase NUDT15"
                     /EC_number="3.6.1.9"
                     /note="MutT homolog 2; probable 7,8-dihydro-8-oxoguanine
                     triphosphatase NUDT15; nudix motif 15; 8-oxo-dGTPase
                     NUDT15; nucleoside diphosphate-linked moiety X motif 15;
                     nudix (nucleoside diphosphate linked moiety X)-type motif
                     15; 7,8-dihydro-8-oxoguanine-triphosphatase NUDT15;
                     probable 8-oxo-dGTP diphosphatase NUDT15; nucleoside
                     diphosphate-linked to another moiety X hydrolase 15"
                     /calculated_mol_wt=19445
     Region          27..142
                     /region_name="NUDIX_MTH2_Nudt15"
                     /note="MutT homolog 2; cd04678"
                     /db_xref="CDD:467561"
     Region          47..68
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG93.1)"
     Region          75..163
                     /region_name="Interaction with PCNA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG93.1)"
     CDS             1..170
                     /gene="Nudt15"
                     /gene_synonym="6530403O17; A730068G11Rik; MTH2"
                     /coded_by="NM_172527.3:430..942"
                     /db_xref="CCDS:CCDS27270.1"
                     /db_xref="GeneID:214254"
                     /db_xref="MGI:MGI:2443366"
ORIGIN      
        1 maanaeprrr pgvgvgvvvl scehprcvll gkrkgsfgag sfqlpgghle fgetweecaq
       61 retweeaglh lknvcfasvv nsfvekenyh yvtilmkgev dmthdseprn mepekneswe
      121 wvpweefppl dqlfwalrcl keqgydpfke dlnhlegyrg ehlerttktp
//
LOCUS       NP_775754                531 aa            linear   PRI 27-APR-2025
DEFINITION  ultra-long-chain fatty acid omega-hydroxylase [Homo sapiens].
ACCESSION   NP_775754
VERSION     NP_775754.2
DBSOURCE    REFSEQ: accession NM_173483.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Nohara,T., Ohno,Y. and Kihara,A.
  TITLE     Impaired production of the skin barrier lipid acylceramide by
            CYP4F22 ichthyosis mutations
  JOURNAL   J Dermatol Sci 101 (1), 69-71 (2021)
   PUBMED   33067036
  REMARK    GeneRIF: Impaired production of the skin barrier lipid acylceramide
            by CYP4F22 ichthyosis mutations.
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Esperon-Moldes,U., Ginarte-Val,M., Rodriguez-Pazos,L., Fachal,L.,
            Martin-Santiago,A., Vicente,A., Jimenez-Gallo,D.,
            Guillen-Navarro,E., Sampol,L.M., Gonzalez-Ensenat,M.A. and Vega,A.
  TITLE     Novel CYP4F22 mutations associated with autosomal recessive
            congenital ichthyosis (ARCI). Study of the CYP4F22 c.1303C>T
            founder mutation
  JOURNAL   PLoS One 15 (2), e0229025 (2020)
   PUBMED   32069299
  REMARK    GeneRIF: The present study reports five CYP4F22 mutations, two of
            them novel, increasing the number of CYP4F22 mutations currently
            listed. Additionally, our results suggest that the recurrent
            c.1303C>T change has a founder effect in Spanish population and
            c.1303C>T carrier families originated from a single ancestor with
            probable African ancestry.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Sayeb,M., Riahi,Z., Laroussi,N., Bonnet,C., Romdhane,L.,
            Mkaouar,R., Zaouak,A., Marrakchi,J., Abdessalem,G., Messaoud,O.,
            Bouchniba,O., Ghilane,N., Mokni,M., Besbes,G., Yacoub-Youssef,H.,
            Petit,C. and Abdelhak,S.
  TITLE     A Tunisian family with a novel mutation in the gene CYP4F22 for
            lamellar ichthyosis and co-occurrence of hearing loss in a child
            due to mutation in the SLC26A4 gene
  JOURNAL   Int J Dermatol 58 (12), 1439-1443 (2019)
   PUBMED   31020658
  REMARK    GeneRIF: Study reports a consanguineous family from Southern
            Tunisia including three members affected with congenital ichthyosis
            likely due to a novel missense mutation c.728G>T (p.Arg243Leu) in
            exon 8 of CYP4F2.
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Elias,P.M., Williams,M.L., Holleran,W.M., Jiang,Y.J. and Schmuth,M.
  TITLE     Pathogenesis of permeability barrier abnormalities in the
            ichthyoses: inherited disorders of lipid metabolism
  JOURNAL   J Lipid Res 49 (4), 697-714 (2008)
   PUBMED   18245815
  REMARK    Review article
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Lefevre,C., Bouadjar,B., Ferrand,V., Tadini,G., Megarbane,A.,
            Lathrop,M., Prud'homme,J.F. and Fischer,J.
  TITLE     Mutations in a new cytochrome P450 gene in lamellar ichthyosis type
            3
  JOURNAL   Hum Mol Genet 15 (5), 767-776 (2006)
   PUBMED   16436457
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Virolainen,E., Wessman,M., Hovatta,I., Niemi,K.M., Ignatius,J.,
            Kere,J., Peltonen,L. and Palotie,A.
  TITLE     Assignment of a novel locus for autosomal recessive congenital
            ichthyosis to chromosome 19p13.1-p13.2
  JOURNAL   Am J Hum Genet 66 (3), 1132-1137 (2000)
   PUBMED   10712223
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Fischer,J., Faure,A., Bouadjar,B., Blanchet-Bardon,C.,
            Karaduman,A., Thomas,I., Emre,S., Cure,S., Ozguc,M., Weissenbach,J.
            and Prud'homme,J.F.
  TITLE     Two new loci for autosomal recessive ichthyosis on chromosomes 3p21
            and 19p12-q12 and evidence for further genetic heterogeneity
  JOURNAL   Am J Hum Genet 66 (3), 904-913 (2000)
   PUBMED   10712205
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Richard,G.
  TITLE     Autosomal Recessive Congenital Ichthyosis
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301593
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA874258.1, BC069351.1,
            AC011492.8 and AI341068.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 11, 2007 this sequence version replaced NP_775754.1.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This gene is part of a cluster of cytochrome P450 genes on
            chromosome 19 and encodes an enzyme thought to play a role in the
            12(R)-lipoxygenase pathway. Mutations in this gene are the cause of
            ichthyosis lamellar type 3. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096820.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269703.8/ ENSP00000269703.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..531
                     /product="ultra-long-chain fatty acid omega-hydroxylase"
                     /EC_number="1.14.14.177"
                     /note="cytochrome P450 4F22; cytochrome P450, family 2,
                     subfamily E, polypeptide 2 homolog; cytochrome P450,
                     family 4, subfamily F, polypeptide 22"
                     /calculated_mol_wt=61827
     Site            23..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT55.1)"
     Region          82..523
                     /region_name="CYP4F"
                     /note="cytochrome P450 family 4, subfamily F; cd20679"
                     /db_xref="CDD:410772"
     Site            order(125,144..145,152,156,163,332,335..336,339,401..402,
                     405,467..469,473..477,480..481,485)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410772"
     Site            order(145,334..335,339,402,404,406,513)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:410772"
     CDS             1..531
                     /gene="CYP4F22"
                     /gene_synonym="ARCI5; INLNE; LI3"
                     /coded_by="NM_173483.4:168..1763"
                     /db_xref="CCDS:CCDS12331.1"
                     /db_xref="GeneID:126410"
                     /db_xref="HGNC:HGNC:26820"
                     /db_xref="MIM:611495"
ORIGIN      
        1 mlpitdrllh llglektafr iyavstlllf llfflfrlll rflrlcrsfy itcrrlrcfp
       61 qpprrnwllg hlgmylpnea glqdekkvld nmhhvllvwm gpvlpllvlv hpdyikpllg
      121 asaaiapkdd lfygflkpwl gdglllskgd kwsrhrrllt pafhfdilkp ymkifnqsad
      181 imhakwrhla egsavsldmf ehislmtlds lqkcvfsyns ncqekmsdyi saiielsals
      241 vrrqyrlhhy ldfiyyrsad grrfrqacdm vhhftteviq errralrqqg aeawlkakqg
      301 ktldfidvll lardedgkel sdediraead tfmfeghdtt ssgiswmlfn lakypeyqek
      361 creeiqevmk greleelewd dltqlpfttm cikeslrqyp pvtlvsrqct ediklpdgri
      421 ipkgiiclvs iygthhnptv wpdskvynpy rfdpdnpqqr splayvpfsa gprncigqsf
      481 amaelrvvva ltllrfrlsv drtrkvrrkp elilrtengl wlkveplppr a
//
LOCUS       NP_001878                252 aa            linear   PRI 27-APR-2025
DEFINITION  beta-crystallin B1 [Homo sapiens].
ACCESSION   NP_001878
VERSION     NP_001878.1
DBSOURCE    REFSEQ: accession NM_001887.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Jing,X., Zhu,M., Lu,X., Wei,P., Shi,L., Zhang,B.Y., Xu,Y.,
            Tang,Y.P., Xiang,D.M. and Gong,P.
  TITLE     Cataract-causing Y204X mutation of crystallin protein CRYbetaB1
            promotes its C-terminal degradation and higher-order
            oligomerization
  JOURNAL   J Biol Chem 299 (8), 104953 (2023)
   PUBMED   37356717
  REMARK    GeneRIF: Cataract-causing Y204X mutation of crystallin protein
            CRYbetaB1 promotes its C-terminal degradation and higher-order
            oligomerization.
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Liu,J., Xu,W., Wang,K., Chen,F., Ren,L., Xu,J., Yao,K. and Chen,X.
  TITLE     Congenital cataract-causing mutation betaB1-L116P is prone to
            amyloid fibrils aggregation and protease degradation with low
            structural stability
  JOURNAL   Int J Biol Macromol 195, 475-482 (2022)
   PUBMED   34896472
  REMARK    GeneRIF: Congenital cataract-causing mutation betaB1-L116P is prone
            to amyloid fibrils aggregation and protease degradation with low
            structural stability.
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Ji,Y., Zhao,X., Zhang,J., Zhang,D., Tian,C., Zhang,L., Zhao,Y. and
            Zhao,J.
  TITLE     A novel missense mutation of CRYBB1 causes congenital cataract in a
            Chinese family
  JOURNAL   Eur J Ophthalmol 31 (3), 1064-1069 (2021)
   PUBMED   32223445
  REMARK    GeneRIF: A novel missense mutation of CRYBB1 causes congenital
            cataract in a Chinese family.
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Jin,A., Zhang,Y., Xiao,D., Xiang,M., Jin,K. and Zeng,M.
  TITLE     A Novel Mutation p.S93R in CRYBB1 Associated with Dominant
            Congenital Cataract and Microphthalmia
  JOURNAL   Curr Eye Res 45 (4), 483-489 (2020)
   PUBMED   31566446
  REMARK    GeneRIF: A Novel Mutation p.S93R in CRYBB1 Associated with Dominant
            Congenital Cataract and Microphthalmia.
REFERENCE   6  (residues 1 to 252)
  AUTHORS   MacCoss,M.J., McDonald,W.H., Saraf,A., Sadygov,R., Clark,J.M.,
            Tasto,J.J., Gould,K.L., Wolters,D., Washburn,M., Weiss,A.,
            Clark,J.I. and Yates,J.R. 3rd.
  TITLE     Shotgun identification of protein modifications from protein
            complexes and lens tissue
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 7900-7905 (2002)
   PUBMED   12060738
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   8  (residues 1 to 252)
  AUTHORS   Lampi,K.J., Ma,Z., Hanson,S.R., Azuma,M., Shih,M., Shearer,T.R.,
            Smith,D.L., Smith,J.B. and David,L.L.
  TITLE     Age-related changes in human lens crystallins identified by
            two-dimensional electrophoresis and mass spectrometry
  JOURNAL   Exp Eye Res 67 (1), 31-43 (1998)
   PUBMED   9702176
REFERENCE   9  (residues 1 to 252)
  AUTHORS   David,L.L., Lampi,K.J., Lund,A.L. and Smith,J.B.
  TITLE     The sequence of human betaB1-crystallin cDNA allows mass
            spectrometric detection of betaB1 protein missing portions of its
            N-terminal extension
  JOURNAL   J Biol Chem 271 (8), 4273-4279 (1996)
   PUBMED   8626774
REFERENCE   10 (residues 1 to 252)
  AUTHORS   Hulsebos,T.J., Gilbert,D.J., Delattre,O., Smink,L.J., Dunham,I.,
            Westerveld,A., Thomas,G., Jenkins,N.A. and Copeland,N.G.
  TITLE     Assignment of the beta B1 crystallin gene (CRYBB1) to human
            chromosome 22 and mouse chromosome 5
  JOURNAL   Genomics 29 (3), 712-718 (1995)
   PUBMED   8575764
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U35340.1 and BM669750.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Crystallins are separated into two classes:
            taxon-specific, or enzyme, and ubiquitous. The latter class
            constitutes the major proteins of vertebrate eye lens and maintains
            the transparency and refractive index of the lens. Since lens
            central fiber cells lose their nuclei during development, these
            crystallins are made and then retained throughout life, making them
            extremely stable proteins. Mammalian lens crystallins are divided
            into alpha, beta, and gamma families; beta and gamma crystallins
            are also considered as a superfamily. Alpha and beta families are
            further divided into acidic and basic groups. Seven protein regions
            exist in crystallins: four homologous motifs, a connecting peptide,
            and N- and C-terminal extensions. Beta-crystallins, the most
            heterogeneous, differ by the presence of the C-terminal extension
            (present in the basic group, none in the acidic group).
            Beta-crystallins form aggregates of different sizes and are able to
            self-associate to form dimers or to form heterodimers with other
            beta-crystallins. This gene, a beta basic group member, undergoes
            extensive cleavage at its N-terminal extension during lens
            maturation. It is also a member of a gene cluster with beta-A4,
            beta-B2, and beta-B3. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY794960.2, U35340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000647684.1/ ENSP00000497249.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.1"
     Protein         1..252
                     /product="beta-crystallin B1"
                     /note="eye lens structural protein; beta-B1 crystallin"
                     /calculated_mol_wt=27892
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53674.2)"
     Region          2..58
                     /region_name="N-terminal arm"
                     /note="propagated from UniProtKB/Swiss-Prot (P53674.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:8626774; propagated from
                     UniProtKB/Swiss-Prot (P53674.2)"
     Region          60..142
                     /region_name="Crystall"
                     /note="Beta/Gamma crystallin; pfam00030"
                     /db_xref="CDD:459639"
     Region          144..148
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P53674.2)"
     Region          150..232
                     /region_name="Crystall"
                     /note="Beta/Gamma crystallin; pfam00030"
                     /db_xref="CDD:459639"
     Region          235..252
                     /region_name="C-terminal arm"
                     /note="propagated from UniProtKB/Swiss-Prot (P53674.2)"
     CDS             1..252
                     /gene="CRYBB1"
                     /gene_synonym="CATCN3; CTRCT17"
                     /coded_by="NM_001887.4:71..829"
                     /db_xref="CCDS:CCDS13840.1"
                     /db_xref="GeneID:1414"
                     /db_xref="HGNC:HGNC:2397"
                     /db_xref="MIM:600929"
ORIGIN      
        1 msqaakasas atvavnpgpd tkgkgappag tspspgttla pttvpitsak aaelppgnyr
       61 lvvfelenfq grraefsgec snladrgfdr vrsiivsagp wvafeqsnfr gemfilekge
      121 yprwntwsss yrsdrlmsfr pikmdaqehk islfeganfk gntieiqgdd apslwvygfs
      181 drvgsvkvss gtwvgyqypg yrgyqyllep gdfrhwnewg afqpqmqslr rlrdkqwhle
      241 gsfpvlatep pk
//
LOCUS       NP_001108239             393 aa            linear   MAM 27-APR-2025
DEFINITION  bone morphogenetic protein 15 precursor [Ovis aries].
ACCESSION   NP_001108239
VERSION     NP_001108239.1
DBSOURCE    REFSEQ: accession NM_001114767.2
KEYWORDS    RefSeq.
SOURCE      Ovis aries (sheep)
  ORGANISM  Ovis aries
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Caprinae; Ovis.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Zamani,P., Rabiei,F., Hadiei,E., Abdoli,R., Ahmadi,A. and Rabiei,S.
  TITLE     Screening for causative mutations in ovine BMPR1B and BMP15 genes
            and their homologous fragments in human
  JOURNAL   J Assist Reprod Genet 40 (8), 1973-1982 (2023)
   PUBMED   37455267
  REMARK    GeneRIF: Screening for causative mutations in ovine BMPR1B and
            BMP15 genes and their homologous fragments in human.
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Khan,J.M., Tahir,M.F., Qamar,M.F., Naz,S., Rauf,M., Noreen,R.,
            Ayaz,M.M., Khan,M., Ahmad,M., Khurshid,U., Saeed,S., Iqbal,M.J.,
            Younas,Q.U.A. and Hameed,Y.
  TITLE     Mutations in the bone morphogenetic protein 15 gene causing
            defective protein secretion in Cholistani infertile sheep
  JOURNAL   Braz J Biol 84, e256923 (2022)
   PUBMED   35137843
  REMARK    GeneRIF: Mutations in the bone morphogenetic protein 15 gene
            causing defective protein secretion in Cholistani infertile sheep.
            Erratum:[Braz J Biol. 2022 May 20;84:e256923er. doi:
            10.1590/1519-6984.256923er. PMID: 35584463]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Perez-Ruiz,E., Gallegos-Sanchez,J., Cortez-Romero,C.,
            Segura-Leon,O.L., Salinas-Ruiz,J. and Salazar-Ortiz,J.
  TITLE     FecGE mutation in pelibuey sheep
  JOURNAL   Anim Genet 51 (2), 346-347 (2020)
   PUBMED   31961953
  REMARK    GeneRIF: No polymorphisms were found in exon 2 of the BMP15 gene in
            Pelibuey sheep.
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Lassoued,N., Benkhlil,Z., Woloszyn,F., Rejeb,A., Aouina,M.,
            Rekik,M., Fabre,S. and Bedhiaf-Romdhani,S.
  TITLE     FecX Bar a Novel BMP15 mutation responsible for prolificacy and
            female sterility in Tunisian Barbarine Sheep
  JOURNAL   BMC Genet 18 (1), 43 (2017)
   PUBMED   28506298
  REMARK    GeneRIF: BMP15 mutation is associated with prolificacy and female
            sterility.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Estienne,A., Lahoz,B., Jarrier,P., Bodin,L., Folch,J.,
            Alabart,J.L., Fabre,S. and Monniaux,D.
  TITLE     BMP15 regulates the inhibin/activin system independently of
            ovulation rate control in sheep
  JOURNAL   Reproduction 153 (4), 395-404 (2017)
   PUBMED   28069901
  REMARK    GeneRIF: activin can explain that the effects of BMP15 mutations
            differ when present in different genetic backgrounds
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Martinez-Royo,A., Jurado,J.J., Smulders,J.P., Marti,J.I.,
            Alabart,J.L., Roche,A., Fantova,E., Bodin,L., Mulsant,P.,
            Serrano,M., Folch,J. and Calvo,J.H.
  TITLE     A deletion in the bone morphogenetic protein 15 gene causes
            sterility and increased prolificacy in Rasa Aragonesa sheep
  JOURNAL   Anim Genet 39 (3), 294-297 (2008)
   PUBMED   18355397
  REMARK    GeneRIF: in BMP15, this new mutation is associated with increased
            prolificacy and sterility in heterozygous and homozygous ewes
            respectively
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Feary,E.S., Juengel,J.L., Smith,P., French,M.C., O'Connell,A.R.,
            Lawrence,S.B., Galloway,S.M., Davis,G.H. and McNatty,K.P.
  TITLE     Patterns of expression of messenger RNAs encoding GDF9, BMP15,
            TGFBR1, BMPR1B, and BMPR2 during follicular development and
            characterization of ovarian follicular populations in ewes carrying
            the Woodlands FecX2W mutation
  JOURNAL   Biol Reprod 77 (6), 990-998 (2007)
   PUBMED   17715428
  REMARK    GeneRIF: sequence of the complete coding region of BMP15 gene and
            determination of the patterns of expression of mRNAs encoding BMP15
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Chu,M.X., Liu,Z.H., Jiao,C.L., He,Y.Q., Fang,L., Ye,S.C., Chen,G.H.
            and Wang,J.Y.
  TITLE     Mutations in BMPR-IB and BMP-15 genes are associated with litter
            size in Small Tailed Han sheep (Ovis aries)
  JOURNAL   J Anim Sci 85 (3), 598-603 (2007)
   PUBMED   17040942
  REMARK    GeneRIF: Small Tailed Han ewes carrying mutations in both BMPR-IB
            and BMP-15 genes had greater litter size than those with either
            mutation alone.
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Bodin,L., Di Pasquale,E., Fabre,S., Bontoux,M., Monget,P.,
            Persani,L. and Mulsant,P.
  TITLE     A novel mutation in the bone morphogenetic protein 15 gene causing
            defective protein secretion is associated with both increased
            ovulation rate and sterility in Lacaune sheep
  JOURNAL   Endocrinology 148 (1), 393-400 (2007)
   PUBMED   17038554
  REMARK    GeneRIF: BMP15 has an essential role in ovarian folliculogenesis
            and the control of ovulation rate in sheep.
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Galloway,S.M., McNatty,K.P., Cambridge,L.M., Laitinen,M.P.,
            Juengel,J.L., Jokiranta,T.S., McLaren,R.J., Luiro,K., Dodds,K.G.,
            Montgomery,G.W., Beattie,A.E., Davis,G.H. and Ritvos,O.
  TITLE     Mutations in an oocyte-derived growth factor gene (BMP15) cause
            increased ovulation rate and infertility in a dosage-sensitive
            manner
  JOURNAL   Nat Genet 25 (3), 279-283 (2000)
   PUBMED   10888873
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            KT853038.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KT853038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5077168, SAMEA5298418
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Ovis aries"
                     /db_xref="taxon:9940"
                     /chromosome="X"
                     /map="X"
     Protein         1..393
                     /product="bone morphogenetic protein 15 precursor"
                     /note="growth/differentiation factor 9B"
                     /calculated_mol_wt=41905
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9MZE2.1)"
                     /calculated_mol_wt=3013
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9MZE2.1)"
     Site            237
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9MZE2.1)"
     mat_peptide     269..393
                     /product="Bone morphogenetic protein 15.
                     /id=PRO_0000033897"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9MZE2.1)"
                     /calculated_mol_wt=13905
     Region          290..393
                     /region_name="TGF_beta_GDF9B"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in growth/differentiation factor 9B (GDF-9B)
                     and similar proteins; cd19402"
                     /db_xref="CDD:381672"
     Site            order(297,299,303..304,306,316,318..320,337..338,341..342,
                     344..345,348,353..354,357,359..360,363,383..385,387,393)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381672"
     Site            374
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9MZE2.1)"
     CDS             1..393
                     /gene="BMP15"
                     /gene_synonym="BMP-15; GDF-9B; GDF9B"
                     /coded_by="NM_001114767.2:1..1182"
                     /db_xref="GeneID:100141303"
ORIGIN      
        1 mvllsilril lwglvlfmeh rvqmtqvgqp siahlpeapt lpliqellee apgkqqrkpr
       61 vlghplryml elyqrsadas ghprenrtig atmvrlvrpl asvarplrgs whiqtldfpl
      121 rpnrvayqlv ratvvyrhql hlthshlsch vepwvqkspt nhfpssgrgs skpsllpktw
      181 temdimehvg qklwnhkgrr vlrlrfvcqq prgsevlefw whgtssldtv flllyfndtq
      241 svqktkplpk glkeftekdp slllrrarqa gsiasevpgp srehdgpesn qcslhpfqvs
      301 fqqlgwdhwi iaphlytpny ckgvcprvlh yglnspnhai iqnlvselvd qnvpqpscvp
      361 ykyvpisill ieangsilyk eyegmiaqsc tcr
//
LOCUS       NP_001348848             189 aa            linear   ROD 27-APR-2025
DEFINITION  testis-expressed protein 22 [Mus musculus].
ACCESSION   NP_001348848 XP_006516402
VERSION     NP_001348848.1
DBSOURCE    REFSEQ: accession NM_001361919.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Miyata,H., Castaneda,J.M., Fujihara,Y., Yu,Z., Archambeault,D.R.,
            Isotani,A., Kiyozumi,D., Kriseman,M.L., Mashiko,D., Matsumura,T.,
            Matzuk,R.M., Mori,M., Noda,T., Oji,A., Okabe,M.,
            Prunskaite-Hyyrylainen,R., Ramirez-Solis,R., Satouh,Y., Zhang,Q.,
            Ikawa,M. and Matzuk,M.M.
  TITLE     Genome engineering uncovers 54 evolutionarily conserved and
            testis-enriched genes that are not required for male fertility in
            mice
  JOURNAL   Proc Natl Acad Sci U S A 113 (28), 7704-7710 (2016)
   PUBMED   27357688
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Neesen,J., Hartwich,T., Brandhorst,G., Aumuller,G., Glaser,B.,
            Burfeind,P. and Mendoza-Lujambio,I.
  TITLE     Tep22, a novel testicular expressed gene, is involved in the
            biogenesis of the acrosome and the midpiece of the sperm tail
  JOURNAL   Biochem Biophys Res Commun 297 (4), 737-748 (2002)
   PUBMED   12359214
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073562.6, AK006471.1 and BX631150.1.
            
            On Mar 30, 2018 this sequence version replaced XP_006516402.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK006471.1, BC048634.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 61.57 cM"
     Protein         1..189
                     /product="testis-expressed protein 22"
                     /note="testis-expressed sequence 22 protein;
                     testis-expressed protein of 22 kDa"
                     /calculated_mol_wt=21371
     Region          1..120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D9U4.1)"
     CDS             1..189
                     /gene="Tex22"
                     /gene_synonym="1700028O09Rik; Tep22"
                     /coded_by="NM_001361919.1:396..965"
                     /db_xref="CCDS:CCDS26203.1"
                     /db_xref="GeneID:75671"
                     /db_xref="MGI:MGI:1922921"
ORIGIN      
        1 mdsrqqrpqr ktlqwqlaqe qrqqsppqgl avassqpdtk skpqddlqtq dwvcepqelr
       61 rpgsrwnisi derrrlalqr mqertdtara psgdplglhp egqqtetsps tqsvptpplq
      121 acetmadplq diahvlaelm segverdvli sqplrstens nafqdflaqd aplwkdenfe
      181 aqtsrwphs
//
LOCUS       NP_005640                605 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 354A isoform 1 [Homo sapiens].
ACCESSION   NP_005640
VERSION     NP_005640.2
DBSOURCE    REFSEQ: accession NM_005649.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Wang,W., Cai,J., Wu,Y., Hu,L., Chen,Z., Hu,J., Chen,Z., Li,W.,
            Guo,M. and Huang,Z.
  TITLE     Novel activity of KRAB domain that functions to reinforce nuclear
            localization of KRAB-containing zinc finger proteins by interacting
            with KAP1
  JOURNAL   Cell Mol Life Sci 70 (20), 3947-3958 (2013)
   PUBMED   23665872
REFERENCE   2  (residues 1 to 605)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 605)
  AUTHORS   Johnatty,S.E., Beesley,J., Chen,X., Macgregor,S., Duffy,D.L.,
            Spurdle,A.B., deFazio,A., Gava,N., Webb,P.M., Rossing,M.A.,
            Doherty,J.A., Goodman,M.T., Lurie,G., Thompson,P.J., Wilkens,L.R.,
            Ness,R.B., Moysich,K.B., Chang-Claude,J., Wang-Gohrke,S.,
            Cramer,D.W., Terry,K.L., Hankinson,S.E., Tworoger,S.S.,
            Garcia-Closas,M., Yang,H., Lissowska,J., Chanock,S.J.,
            Pharoah,P.D., Song,H., Whitemore,A.S., Pearce,C.L., Stram,D.O.,
            Wu,A.H., Pike,M.C., Gayther,S.A., Ramus,S.J., Menon,U.,
            Gentry-Maharaj,A., Anton-Culver,H., Ziogas,A., Hogdall,E.,
            Kjaer,S.K., Hogdall,C., Berchuck,A., Schildkraut,J.M.,
            Iversen,E.S., Moorman,P.G., Phelan,C.M., Sellers,T.A.,
            Cunningham,J.M., Vierkant,R.A., Rider,D.N., Goode,E.L., Haviv,I.
            and Chenevix-Trench,G.
  CONSRTM   Ovarian Cancer Association Consortium; Australian Ovarian Cancer
            Study Group; Australian Cancer Study (Ovarian Cancer)
  TITLE     Evaluation of candidate stromal epithelial cross-talk genes
            identifies association between risk of serous ovarian cancer and
            TERT, a cancer susceptibility 'hot-spot'
  JOURNAL   PLoS Genet 6 (7), e1001016 (2010)
   PUBMED   20628624
  REMARK    GeneRIF: Meta-analysis of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 605)
  AUTHORS   Navarro-Lerida,I., Martinez Moreno,M., Roncal,F., Gavilanes,F.,
            Albar,J.P. and Rodriguez-Crespo,I.
  TITLE     Proteomic identification of brain proteins that interact with
            dynein light chain LC8
  JOURNAL   Proteomics 4 (2), 339-346 (2004)
   PUBMED   14760703
REFERENCE   5  (residues 1 to 605)
  AUTHORS   Bugert,P., Pesti,T. and Kovacs,G.
  TITLE     The tcf17 gene at chromosome 5q is not involved in the development
            of conventional renal cell carcinoma
  JOURNAL   Int J Cancer 86 (6), 806-810 (2000)
   PUBMED   10842194
REFERENCE   6  (residues 1 to 605)
  AUTHORS   Jacob,A.N., Manjunath,N.A., Bray-Ward,P. and Kandpal,R.P.
  TITLE     Molecular cloning of a zinc finger gene eZNF from a human inner ear
            cDNA library, and in situ expression pattern of its mouse homologue
            in mouse inner ear
  JOURNAL   Somat Cell Mol Genet 24 (2), 121-129 (1998)
   PUBMED   9919311
REFERENCE   7  (residues 1 to 605)
  AUTHORS   Omori,Y., Kyushiki,H., Takeda,S., Suzuki,M., Kawai,A., Fujiwara,T.,
            Takahashi,E. and Nakamura,Y.
  TITLE     Cloning, expression and mapping of a novel human zinc-finger gene
            TCF17 homologous to rodent Kid1
  JOURNAL   Cytogenet Cell Genet 78 (3-4), 285-288 (1997)
   PUBMED   9465904
REFERENCE   8  (residues 1 to 605)
  AUTHORS   Witzgall,R., O'Leary,E., Gessner,R., Ouellette,A.J. and
            Bonventre,J.V.
  TITLE     Kid-1, a putative renal transcription factor: regulation during
            ontogeny and in response to ischemia and toxic injury
  JOURNAL   Mol Cell Biol 13 (3), 1933-1942 (1993)
   PUBMED   8382778
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF116030.1, BC036517.1, BU685427.1 and AC113348.2.
            
            On Oct 7, 2003 this sequence version replaced NP_005640.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.65893.1, EU794664.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335815.7/ ENSP00000337122.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..605
                     /product="zinc finger protein 354A isoform 1"
                     /note="transcription factor 17; zinc finger protein eZNF;
                     epididymis luminal protein 104"
                     /calculated_mol_wt=69106
     Region          14..73
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          74..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60765.2)"
     Region          189..208
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..600
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          216..236
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          244..264
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(249,251,253,255..256,259..260,263,277,279,283..284,
                     287..288,291,305,307,309,311..312,315..316,319)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          272..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          356..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(361,363,365,367..368,371..372,375,389,391,395..396,
                     399..400,403,417,419,421,423..424,427..428,431)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          384..404
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          412..432
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          440..460
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          468..488
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          496..516
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(501,503,505,507..508,511..512,515,529,531,535..536,
                     539..540,543,557,559,561,563..564,567..568,571)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          524..544
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          552..572
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          580..600
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..605
                     /gene="ZNF354A"
                     /gene_synonym="EZNF; HEL104; HKL1; KID-1; KID1; TCF17"
                     /coded_by="NM_005649.3:156..1973"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4438.1"
                     /db_xref="GeneID:6940"
                     /db_xref="HGNC:HGNC:11628"
                     /db_xref="MIM:602444"
ORIGIN      
        1 maagqrearp qvsltfedva vlftrdewrk lapsqrnlyr dvmlenyrnl vslglpftkp
       61 kvisllqqge dpwevekdgs gvsslgskss hkttkstqtq dssfqglilk rsnrnvpwdl
      121 klekpyiyeg rlekkqdkkg sfqivsathk kiptiershk ntelsqnfsp ksvlirqqil
      181 prektppkce iqgnslkqns qllnqpkita dkrykcslce ktfintsslr kheknhsgek
      241 lfkckecska fsqssaliqh qithtgekpy ickecgkaft lstslykhlr thtveksyrc
      301 kecgksfsrr sglfihqkih aeenpckynp grkasscsts lsgcqrihsr kksylcnecg
      361 ntfksssslr yhqrihtgek pfkcsecgra fsqsasliqh erihtgekpy rcnecgkgft
      421 sisrlnrhri ihtgekfync necgkalssh stliiherih tgekpckckv cgkafrqssa
      481 liqhqrmhtg erpykcnecg ktfrcnssls nhqrihtgek pyrceecgis fgqssaliqh
      541 rrihtgekpf kcntcgktfr qsssriahqr ihtgekpyec ntcgklfnhr ssltnhykih
      601 ieedp
//
LOCUS       NP_079108                985 aa            linear   PRI 27-APR-2025
DEFINITION  ras and Rab interactor 3 isoform 1 [Homo sapiens].
ACCESSION   NP_079108
VERSION     NP_079108.3
DBSOURCE    REFSEQ: accession NM_024832.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Bhattacharyya,R., Teves,C.A.F., Long,A., Hofert,M. and Tanzi,R.E.
  TITLE     The neuronal-specific isoform of BIN1 regulates beta-secretase
            cleavage of APP and Abeta generation in a RIN3-dependent manner
  JOURNAL   Sci Rep 12 (1), 3486 (2022)
   PUBMED   35241726
  REMARK    GeneRIF: The neuronal-specific isoform of BIN1 regulates
            beta-secretase cleavage of APP and Abeta generation in a
            RIN3-dependent manner.
            Erratum:[Sci Rep. 2022 Apr 6;12(1):5739. doi:
            10.1038/s41598-022-09896-1. PMID: 35388126]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Shen,R., Zhao,X., He,L., Ding,Y., Xu,W., Lin,S., Fang,S., Yang,W.,
            Sung,K., Spencer,B., Rissman,R.A., Lei,M., Ding,J. and Wu,C.
  TITLE     Upregulation of RIN3 induces endosomal dysfunction in Alzheimer's
            disease
  JOURNAL   Transl Neurodegener 9 (1), 26 (2020)
   PUBMED   32552912
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 985)
  AUTHORS   De Ridder,R., Boudin,E., Vandeweyer,G., Devogelaer,J.P.,
            Fransen,E., Mortier,G. and Van Hul,W.
  TITLE     Genetic Variation in RIN3 in the Belgian Population Supports Its
            Involvement in the Pathogenesis of Paget's Disease of Bone and
            Modifies the Age of Onset
  JOURNAL   Calcif Tissue Int 104 (6), 613-621 (2019)
   PUBMED   30726512
  REMARK    GeneRIF: Genetic Variation in RIN3 in the Belgian Population
            Supports Its Involvement in the Pathogenesis of Paget's Disease of
            Bone and Modifies the Age of Onset.
REFERENCE   5  (residues 1 to 985)
  AUTHORS   Kunkle,B.W., Vardarajan,B.N., Naj,A.C., Whitehead,P.L., Rolati,S.,
            Slifer,S., Carney,R.M., Cuccaro,M.L., Vance,J.M., Gilbert,J.R.,
            Wang,L.S., Farrer,L.A., Reitz,C., Haines,J.L., Beecham,G.W.,
            Martin,E.R., Schellenberg,G.D., Mayeux,R.P. and Pericak-Vance,M.A.
  TITLE     Early-Onset Alzheimer Disease and Candidate Risk Genes Involved in
            Endolysosomal Transport
  JOURNAL   JAMA Neurol 74 (9), 1113-1122 (2017)
   PUBMED   28738127
  REMARK    GeneRIF: RIN3 may be involved in endolysosomal transport-a process
            known to be important to development of early onset AD.
REFERENCE   6  (residues 1 to 985)
  AUTHORS   Yoshikawa,M., Kajiho,H., Sakurai,K., Minoda,T., Nakagawa,S.,
            Kontani,K. and Katada,T.
  TITLE     Tyr-phosphorylation signals translocate RIN3, the small GTPase
            Rab5-GEF, to early endocytic vesicles
  JOURNAL   Biochem Biophys Res Commun 372 (1), 168-172 (2008)
   PUBMED   18486601
  REMARK    GeneRIF: Tyrosine-phosphorylation signals are involved in the RIN3
            activation and translocation to early endocytic vesicles.
REFERENCE   7  (residues 1 to 985)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   8  (residues 1 to 985)
  AUTHORS   Kajiho,H., Saito,K., Tsujita,K., Kontani,K., Araki,Y., Kurosu,H.
            and Katada,T.
  TITLE     RIN3: a novel Rab5 GEF interacting with amphiphysin II involved in
            the early endocytic pathway
  JOURNAL   J Cell Sci 116 (Pt 20), 4159-4168 (2003)
   PUBMED   12972505
  REMARK    GeneRIF: RIN3 biochemically characterized as the stimulator and
            stabilizer for GTP-Rab5 plays an important role in the transport
            pathway from plasma membrane to early endosomes
REFERENCE   9  (residues 1 to 985)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
REFERENCE   10 (residues 1 to 985)
  AUTHORS   Saito,K., Murai,J., Kajiho,H., Kontani,K., Kurosu,H. and Katada,T.
  TITLE     A novel binding protein composed of homophilic tetramer exhibits
            unique properties for the small GTPase Rab5
  JOURNAL   J Biol Chem 277 (5), 3412-3418 (2002)
   PUBMED   11733506
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DR003779.1, BX248258.1, BC025248.1, BC070062.1, AB081753.1 and
            AK026092.1.
            
            On Dec 24, 2003 this sequence version replaced NP_079108.2.
            
            Summary: Summary: This protein encoded by this gene is a member of
            the RIN family of Ras interaction-interference proteins, which are
            binding partners to the RAB5 small GTPases. The protein functions
            as a guanine nucleotide exchange for RAB5B and RAB31. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB081753.1, BX248258.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216487.12/ ENSP00000216487.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..985
                     /product="ras and Rab interactor 3 isoform 1"
                     /note="RAB5 interacting protein 3; ras
                     interaction/interference protein 3"
                     /calculated_mol_wt=107723
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TB24.4)"
     Region          52..153
                     /region_name="SH2_RIN3"
                     /note="Src homology 2 (SH2) domain found in Ras and Rab
                     interactor 3 (RIN3)-like proteins; cd10395"
                     /db_xref="CDD:198258"
     Site            order(70,88,114,116)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198258"
     Site            order(115,143)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198258"
     Region          183..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TB24.4)"
     Region          <240..525
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          251..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TB24.4)"
     Region          315..531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TB24.4)"
     Region          587..732
                     /region_name="Interaction with RAB5B.
                     /evidence=ECO:0000269|PubMed:12972505"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TB24.4)"
     Region          739..842
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     Region          877..964
                     /region_name="RA_Rin3"
                     /note="Ras-associating (RA) domain found in Ras and Rab
                     interactor 3 (Rin3); cd16130"
                     /db_xref="CDD:340547"
     CDS             1..985
                     /gene="RIN3"
                     /coded_by="NM_024832.5:153..3110"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32144.1"
                     /db_xref="GeneID:79890"
                     /db_xref="HGNC:HGNC:18751"
                     /db_xref="MIM:610223"
ORIGIN      
        1 mirhagapar gdptgpvpvv gkgeeeeeed gmrlclpanp knclphrrgi silekliktc
       61 pvwlqlslgq aevarilhrv vagmflvrrd ssskqlvlcv hfpslnessa evleytikee
      121 ksilylegsa lvfedifrli afycvsrdll pftlrlpqai leassftdle tianlglgfw
      181 dsslnppqer gkpaepprdr apgfplvssl rptahdanca ceielsvgnd rlwfvnpifi
      241 edcssalptd qpplgncpar plpptsdats ptsrwaprrp pppppvlplq pcspaqppvl
      301 palapapacp lptsppvpap hvtphapgpp dhpnqppmmt cerlpcptag lgplreeamk
      361 pgaassplqq vpapplpakk nlptapprrr vservsledq spgmaaegdq lslppqgtsd
      421 gpedtprest eqgqdtevka sdphsmpelp rtakqppvpp prkkrisrql astlpaplen
      481 aelctqamal etptpgppre gqspasqagt qhppaqatah sqsspefkgs laslsdslgv
      541 svmatdqdsy stssteeele qfsspsvkkk psmilgkarh rlsfasfssm fhaflsnnrk
      601 lykkvvelaq dkgsyfgslv qdykvyslem marqtsstem lqeirtmmtq lksyllqste
      661 lkalvdpalh seeeleaive salykcvlkp lkeainsclh qihskdgslq qlkenqlvil
      721 attttdlgvt tsvpevpmme kilqkftsmh kayspekkis illktckliy dsmalgnpgk
      781 pygaddflpv lmyvlarsnl temllnveym melmdpalql gegsyylttt ygalehiksy
      841 dkitvtrqls vevqdsihrw errrtlnkar asrssvqdfi cvsylepeqq artlasradt
      901 qaqalcaqca ekfaverpqa hrlfvlvdgr cfqladdalp hcikgyllrs epkrdfhfvy
      961 rpldgggggg ggsppclvvr epnfl
//
LOCUS       NP_073747                532 aa            linear   PRI 27-APR-2025
DEFINITION  5' exonuclease Apollo isoform a [Homo sapiens].
ACCESSION   NP_073747
VERSION     NP_073747.1
DBSOURCE    REFSEQ: accession NM_022836.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Sonmez,C., Toia,B., Eickhoff,P., Matei,A.M., El Beyrouthy,M.,
            Wallner,B., Douglas,M.E., de Lange,T. and Lottersberger,F.
  TITLE     DNA-PK controls Apollo's access to leading-end telomeres
  JOURNAL   Nucleic Acids Res 52 (8), 4313-4327 (2024)
   PUBMED   38407308
  REMARK    GeneRIF: DNA-PK controls Apollo's access to leading-end telomeres.
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Bories,C., Lejour,T., Adolphe,F., Kermasson,L., Couve,S.,
            Tanguy,L., Luszczewska,G., Watzky,M., Poillerat,V., Garnier,P.,
            Groisman,R., Ferlicot,S., Richard,S., Saparbaev,M., Revy,P., Gad,S.
            and Renaud,F.
  TITLE     DCLRE1B/Apollo germline mutations associated with renal cell
            carcinoma impair telomere protection
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (4), 167107 (2024)
   PUBMED   38430974
  REMARK    GeneRIF: DCLRE1B/Apollo germline mutations associated with renal
            cell carcinoma impair telomere protection.
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Li,L., Wang,F., Deng,Z., Zhang,G., Zhu,L., Zhao,Z. and Liu,R.
  TITLE     DCLRE1B promotes tumor progression and predicts immunotherapy
            response through METTL3-mediated m6A modification in pancreatic
            cancer
  JOURNAL   BMC Cancer 23 (1), 1073 (2023)
   PUBMED   37936074
  REMARK    GeneRIF: DCLRE1B promotes tumor progression and predicts
            immunotherapy response through METTL3-mediated m6A modification in
            pancreatic cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Yosaatmadja,Y., Baddock,H.T., Newman,J.A., Bielinski,M.,
            Gavard,A.E., Mukhopadhyay,S.M.M., Dannerfjord,A.A., Schofield,C.J.,
            McHugh,P.J. and Gileadi,O.
  TITLE     Structural and mechanistic insights into the Artemis endonuclease
            and strategies for its inhibition
  JOURNAL   Nucleic Acids Res 49 (16), 9310-9326 (2021)
   PUBMED   34387696
  REMARK    GeneRIF: Structural and mechanistic insights into the Artemis
            endonuclease and strategies for its inhibition.
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Baddock,H.T., Newman,J.A., Yosaatmadja,Y., Bielinski,M.,
            Schofield,C.J., Gileadi,O. and McHugh,P.J.
  TITLE     A phosphate binding pocket is a key determinant of exo- versus
            endo-nucleolytic activity in the SNM1 nuclease family
  JOURNAL   Nucleic Acids Res 49 (16), 9294-9309 (2021)
   PUBMED   34387694
  REMARK    GeneRIF: A phosphate binding pocket is a key determinant of exo-
            versus endo-nucleolytic activity in the SNM1 nuclease family.
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Lenain,C., Bauwens,S., Amiard,S., Brunori,M., Giraud-Panis,M.J. and
            Gilson,E.
  TITLE     The Apollo 5' exonuclease functions together with TRF2 to protect
            telomeres from DNA repair
  JOURNAL   Curr Biol 16 (13), 1303-1310 (2006)
   PUBMED   16730175
  REMARK    GeneRIF: SNM1B (Apollo) protein exhibits a 5'-to-3' DNA exonuclease
            activity and functions together with TRF2 to protect telomeres from
            damage and fusion.
REFERENCE   7  (residues 1 to 532)
  AUTHORS   Freibaum,B.D. and Counter,C.M.
  TITLE     hSnm1B is a novel telomere-associated protein
  JOURNAL   J Biol Chem 281 (22), 15033-15036 (2006)
   PUBMED   16606622
  REMARK    GeneRIF: the C terminus of Snm1B was shown to interact with the TRF
            homology domain of TRF2 indicating that Snm1B is likely recruited
            to the telomere via interaction with the double-stranded
            telomere-binding protein TRF2
REFERENCE   8  (residues 1 to 532)
  AUTHORS   Ishiai,M., Kimura,M., Namikoshi,K., Yamazoe,M., Yamamoto,K.,
            Arakawa,H., Agematsu,K., Matsushita,N., Takeda,S., Buerstedde,J.M.
            and Takata,M.
  TITLE     DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear
            focus formation
  JOURNAL   Mol Cell Biol 24 (24), 10733-10741 (2004)
   PUBMED   15572677
REFERENCE   9  (residues 1 to 532)
  AUTHORS   Demuth,I., Digweed,M. and Concannon,P.
  TITLE     Human SNM1B is required for normal cellular response to both DNA
            interstrand crosslink-inducing agents and ionizing radiation
  JOURNAL   Oncogene 23 (53), 8611-8618 (2004)
   PUBMED   15467758
  REMARK    GeneRIF: siRNA knockdown of hSNM1B rendered cells sensitive to
            ionizing radiation, suggesting the possibility of hSNM1B
            involvement in homologous recombination repair of double-strand
            breaks arising as intermediates of ICL repair
REFERENCE   10 (residues 1 to 532)
  AUTHORS   Dronkert,M.L., de Wit,J., Boeve,M., Vasconcelos,M.L., van Steeg,H.,
            Tan,T.L., Hoeijmakers,J.H. and Kanaar,R.
  TITLE     Disruption of mouse SNM1 causes increased sensitivity to the DNA
            interstrand cross-linking agent mitomycin C
  JOURNAL   Mol Cell Biol 20 (13), 4553-4561 (2000)
   PUBMED   10848582
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR005221.1, BC029687.1 and
            AI669133.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: DNA interstrand cross-links prevent strand separation,
            thereby physically blocking transcription, replication, and
            segregation of DNA. DCLRE1B is one of several evolutionarily
            conserved genes involved in repair of interstrand cross-links
            (Dronkert et al., 2000 [PubMed 10848582]).[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.162258.1,
                                           SRR1803614.276786.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000650450.2/ ENSP00000498042.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..532
                     /product="5' exonuclease Apollo isoform a"
                     /EC_number="3.5.2.6"
                     /note="DNA cross-link repair 1B (PSO2 homolog, S.
                     cerevisiae); 5' exonuclease Apollo; SNM1 homolog B;
                     beta-lactamase DCLRE1B"
                     /calculated_mol_wt=59871
     Region          6..151
                     /region_name="SNM1A-1C-like_MBL-fold"
                     /note="SNM1A, artemis/SNM1C, yeast Pso2p, and related
                     proteins; MBL-fold metallo-hydrolase domain; cd16273"
                     /db_xref="CDD:293831"
     Site            order(31,33,35..36,99..100,120,145)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293831"
     Region          216..299
                     /region_name="DRMBL"
                     /note="DNA repair metallo-beta-lactamase; pfam07522"
                     /db_xref="CDD:429512"
     Region          350..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H816.1)"
     Region          453..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H816.1)"
     Region          496..529
                     /region_name="apollo_TRF2_binding"
                     /note="TRF2-binding region of apollo and similar proteins;
                     cd11662"
                     /db_xref="CDD:212560"
     Region          496..511
                     /region_name="TBM"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H816.1)"
     Site            order(498,500..510)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:212560"
     CDS             1..532
                     /gene="DCLRE1B"
                     /gene_synonym="APOLLO; DKCB8; SNM1B; SNMIB"
                     /coded_by="NM_022836.4:262..1860"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS866.1"
                     /db_xref="GeneID:64858"
                     /db_xref="HGNC:HGNC:17641"
                     /db_xref="MIM:609683"
ORIGIN      
        1 mngvliphtp iavdfwslrr agtarlffls hmhsdhtvgl sstwarplyc spitahllhr
       61 hlqvskqwiq alevgeshvl pldeigqetm tvtlldanhc pgsvmflfeg yfgtilytgd
      121 frytpsmlke paltlgkqih tlyldntncn palvlpsrqe aahqivqlir khpqhnikig
      181 lyslgkesll eqlalefqtw vvlsprrlel vqllgladvf tveekagrih avdhmeichs
      241 nmlrwnqthp tiailptsrk ihsshpdihv ipysdhssys elrafvaalk pcqvvpivsr
      301 rpcggfqdsl sprisvplip dsvqqymsss srkpsllwll errlkrprtq gvvfespees
      361 adqsqadrds kkakkeklsp wpadlekqps hhplrikkql fpdlyskewn kavpfcesqk
      421 rvtmltaplg fsvhlrstde efisqktree iglgsplvpm gdddggpeat gnqsawmghg
      481 splshsskgt pllatefrgl alkylltpvn ffqagyssrr fdqqvekyhk pc
//
LOCUS       NP_059995               1551 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein kinase MRCK gamma [Homo sapiens].
ACCESSION   NP_059995 XP_290516
VERSION     NP_059995.2
DBSOURCE    REFSEQ: accession NM_017525.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1551)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   2  (residues 1 to 1551)
  AUTHORS   Yasukochi,Y., Sakuma,J., Takeuchi,I., Kato,K., Oguri,M.,
            Fujimaki,T., Horibe,H. and Yamada,Y.
  TITLE     Identification of CDC42BPG as a novel susceptibility locus for
            hyperuricemia in a Japanese population
  JOURNAL   Mol Genet Genomics 293 (2), 371-379 (2018)
   PUBMED   29124443
  REMARK    GeneRIF: Findings indicate that CDC42BPG may be a susceptibility
            locus for hyperuricemia.
REFERENCE   3  (residues 1 to 1551)
  AUTHORS   Gagliardi,P.A., Somale,D., Puliafito,A., Chiaverina,G., di
            Blasio,L., Oneto,M., Bianchini,P., Bussolino,F. and Primo,L.
  TITLE     MRCKalpha is activated by caspase cleavage to assemble an apical
            actin ring for epithelial cell extrusion
  JOURNAL   J Cell Biol 217 (1), 231-249 (2018)
   PUBMED   29162624
REFERENCE   4  (residues 1 to 1551)
  AUTHORS   Tin,A., Woodward,O.M., Kao,W.H., Liu,C.T., Lu,X., Nalls,M.A.,
            Shriner,D., Semmo,M., Akylbekova,E.L., Wyatt,S.B., Hwang,S.J.,
            Yang,Q., Zonderman,A.B., Adeyemo,A.A., Palmer,C., Meng,Y.,
            Reilly,M., Shlipak,M.G., Siscovick,D., Evans,M.K., Rotimi,C.N.,
            Flessner,M.F., Kottgen,M., Cupples,L.A., Fox,C.S. and Kottgen,A.
  CONSRTM   CARe and CHARGE Consortia
  TITLE     Genome-wide association study for serum urate concentrations and
            gout among African Americans identifies genomic risk loci and a
            novel URAT1 loss-of-function allele
  JOURNAL   Hum Mol Genet 20 (20), 4056-4068 (2011)
   PUBMED   21768215
REFERENCE   5  (residues 1 to 1551)
  AUTHORS   Li,S., Wang,L., Berman,M., Kong,Y.Y. and Dorf,M.E.
  TITLE     Mapping a dynamic innate immunity protein interaction network
            regulating type I interferon production
  JOURNAL   Immunity 35 (3), 426-440 (2011)
   PUBMED   21903422
  REMARK    Erratum:[Immunity. 2011 Oct 28;35(4):647-8]
REFERENCE   6  (residues 1 to 1551)
  AUTHORS   Ng,Y., Tan,I., Lim,L. and Leung,T.
  TITLE     Expression of the human myotonic dystrophy kinase-related
            Cdc42-binding kinase gamma is regulated by promoter DNA methylation
            and Sp1 binding
  JOURNAL   J Biol Chem 279 (33), 34156-34164 (2004)
   PUBMED   15194684
  REMARK    GeneRIF: CDC42BPG expression is regulated by promoter methylation
            and Sp1 binding.
REFERENCE   7  (residues 1 to 1551)
  AUTHORS   Kedra,D., Seroussi,E., Fransson,I., Trifunovic,J., Clark,M.,
            Lagercrantz,J., Blennow,E., Mehlin,H. and Dumanski,J.
  TITLE     The germinal center kinase gene and a novel CDC25-like gene are
            located in the vicinity of the PYGM gene on 11q13
  JOURNAL   Hum Genet 100 (5-6), 611-619 (1997)
   PUBMED   9341881
REFERENCE   8  (residues 1 to 1551)
  AUTHORS   Guru,S.C., Agarwal,S.K., Manickam,P., Olufemi,S.E., Crabtree,J.S.,
            Weisemann,J.M., Kester,M.B., Kim,Y.S., Wang,Y., Emmert-Buck,M.R.,
            Liotta,L.A., Spiegel,A.M., Boguski,M.S., Roe,B.A., Collins,F.S.,
            Marx,S.J., Burns,L. and Chandrasekharappa,S.C.
  TITLE     A transcript map for the 2.8-Mb region containing the multiple
            endocrine neoplasia type 1 locus
  JOURNAL   Genome Res 7 (7), 725-735 (1997)
   PUBMED   9253601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001187.5, AY648038.1 and BI793270.1.
            
            On Sep 5, 2007 this sequence version replaced NP_059995.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY648038.1, SRR7346977.2430426.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342711.6/ ENSP00000345133.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..1551
                     /product="serine/threonine-protein kinase MRCK gamma"
                     /EC_number="2.7.11.1"
                     /note="myotonic dystrophy protein kinase like protein;
                     MRCK gamma; DMPK-like gamma; CDC42 binding protein kinase
                     gamma (DMPK-like); myotonic dystrophy protein kinase-like
                     alpha; myotonic dystrophy protein kinase-like gamma;
                     myotonic dystrophy kinase-related CDC42-binding kinase
                     gamma"
                     /calculated_mol_wt=172329
     Region          69..399
                     /region_name="STKc_DMPK_like"
                     /note="Catalytic domain of Myotonic Dystrophy protein
                     kinase (DMPK)-like Serine/Threonine Kinases; cd05597"
                     /db_xref="CDD:270748"
     Site            order(77..81,85,98,100,132,148..149,151,155,157,195,197,
                     199..200,202,212..213,216,231..236,268,274,277)
                     /site_type="active"
                     /db_xref="CDD:270748"
     Site            order(77..81,85,98,100,132,149..151,155,195,197,199..200,
                     202,212..213)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270748"
     Site            order(81,155,157,195,197,199,216,231..236,268,274,277)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270748"
     Site            order(212..222,225..236)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270748"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q6DT37.2)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q6DT37.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q6DT37.2)"
     Site            393..398
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270748"
     Region          <444..805
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          467..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DT37.2)"
     Region          655..675
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DT37.2)"
     Region          801..849
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DT37.2)"
     Region          863..886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DT37.2)"
     Region          879..921
                     /region_name="C1_MRCKgamma"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in myotonic dystrophy kinase-related Cdc42-binding
                     kinase gamma (MRCK gamma) and similar proteins; cd20866"
                     /db_xref="CDD:410416"
     Site            order(884..890,898..902,905)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410416"
     Region          938..1070
                     /region_name="PH_MRCK"
                     /note="MRCK (myotonic dystrophy-related Cdc42-binding
                     kinase) pleckstrin homology (PH) domain; cd01243"
                     /db_xref="CDD:269949"
     Region          1102..1360
                     /region_name="CNH"
                     /note="CNH domain; pfam00780"
                     /db_xref="CDD:459938"
     Region          1442..1551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DT37.2)"
     Site            1482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6DT37.2)"
     CDS             1..1551
                     /gene="CDC42BPG"
                     /gene_synonym="DMPK2; HSMDPKIN; KAPPA-200; MRCKG;
                     MRCKgamma"
                     /coded_by="NM_017525.3:85..4740"
                     /db_xref="CCDS:CCDS31601.1"
                     /db_xref="GeneID:55561"
                     /db_xref="HGNC:HGNC:29829"
                     /db_xref="MIM:613991"
ORIGIN      
        1 merrlraleq largeaggcp gldglldlll alhhelssgp lrrersvaqf lswaspfvsk
       61 vkelrlqrdd feilkvigrg afgevtvvrq rdtgqifamk mlhkwemlkr aetacfreer
      121 dvlvkgdsrw vttlhyafqd eeylylvmdy yaggdlltll srfedrlppe laqfylaemv
      181 laihslhqlg yvhrdvkpdn vlldvnghir ladfgsclrl ntngmvdssv avgtpdyisp
      241 eilqameegk ghygpqcdww slgvcayell fgetpfyaes lvetygkimn hedhlqfppd
      301 vpdvpasaqd lirqllcrqe erlgrggldd frnhpffegv dwerlassta pyipelrgpm
      361 dtsnfdvddd tlnhpgtlpp pshgafsghh lpfvgftyts gshspessse awaalerklq
      421 cleqekvels rkhqealhap tdhreleqlr kevqtlrdrl pemlrdkasl sqtdgppags
      481 pgqdsdlrqe ldrlhrelae graglqaqeq elcraqgqqe ellqrlqeaq ereaatasqt
      541 ralssqleea raaqreleaq vsslsrqvtq lqgqweqrle essqaktiht asetngmgpp
      601 eggpqeaqlr kevaalreql eqahshrpsg keealcqlqe enrrlsreqe rleaelaqeq
      661 eskqrleger retesnweaq ladilswvnd ekvsrgylqa latkmaeele slrnvgtqtl
      721 parpldhqwk arrlqkmeas arlelqsale aeirakqglq erltqvqeaq lqaerrlqea
      781 ekqsqalqqe lamlreelra rgpvdtkpsn slipflsfrs sekdsakdpg isgeatrhgg
      841 epdlrpegrr slrmgavfpr aptantaste glpakpgsht lrprsfpspt kclrctslml
      901 glgrqglgcd acgyfchttc apqappcpvp pdllrtalgv hpetgtgtay egflsvprps
      961 gvrrgwqrvf aalsdsrlll fdapdlrlsp psgallqvld lrdpqfsatp vlasdvihaq
     1021 srdlprifrv ttsqlavppt tctvlllaes egererwlqv lgelqrllld arprprpvyt
     1081 lkeaydnglp llphtlcaai ldqdrlalgt eeglfvihlr sndifqvgec rrvqqltlsp
     1141 sagllvvlcg rgpsvrlfal aelenievag akipesrgcq vlaagsilqa rtpvlcvavk
     1201 rqvlcyqlgp gpgpwqrrir elqapatvqs lgllgdrlcv gaaggfalyp llneaaplal
     1261 gaglvpeelp psrgglgeal gavelslsef lllfttagiy vdgagrksrg hellwpaapm
     1321 gwgyaapylt vfsensidvf dvrraewvqt vplkkvrpln pegslflygt ekvrltylrn
     1381 qlaekdefdi pdltdnsrrq lfrtkskrrf ffrvseeqqk qqrremlkdp fvrsklispp
     1441 tnfnhlvhvg pangrpgard kspapeekgr vargsgpqrp hsfsealrrp asmgseglgg
     1501 dadpmkrkpw tslssesvsc pqgslspats lmqvserprs lplspeless p
//
LOCUS       NP_000431                860 aa            linear   PRI 27-APR-2025
DEFINITION  rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
            isoform 1 [Homo sapiens].
ACCESSION   NP_000431
VERSION     NP_000431.2
DBSOURCE    REFSEQ: accession NM_000440.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Kuehlewein,L., Strasser,T., Blumenstock,G., Stingl,K.,
            Fischer,M.D., Wilhelm,B., Zrenner,E., Wissinger,B., Kohl,S.,
            Weisschuh,N. and Zobor,D.
  CONSRTM   RD-CURE Consortium
  TITLE     Central Visual Function and Genotype-Phenotype Correlations in
            PDE6A-Associated Retinitis Pigmentosa
  JOURNAL   Invest Ophthalmol Vis Sci 63 (5), 9 (2022)
   PUBMED   35533076
  REMARK    GeneRIF: Central Visual Function and Genotype-Phenotype
            Correlations in PDE6A-Associated Retinitis Pigmentosa.
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Li,Y., Li,R., Dai,H. and Li,G.
  TITLE     Novel variants in PDE6A and PDE6B genes and its phenotypes in
            patients with retinitis pigmentosa in Chinese families
  JOURNAL   BMC Ophthalmol 22 (1), 27 (2022)
   PUBMED   35033039
  REMARK    GeneRIF: Novel variants in PDE6A and PDE6B genes and its phenotypes
            in patients with retinitis pigmentosa in Chinese families.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Cote,R.H., Gupta,R., Irwin,M.J. and Wang,X.
  TITLE     Photoreceptor Phosphodiesterase (PDE6): Structure, Regulatory
            Mechanisms, and Implications for Treatment of Retinal Diseases
  JOURNAL   Adv Exp Med Biol 1371, 33-59 (2022)
   PUBMED   34170501
  REMARK    GeneRIF: Photoreceptor Phosphodiesterase (PDE6): Structure,
            Regulatory Mechanisms, and Implications for Treatment of Retinal
            Diseases.
            Review article
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Kuehlewein,L., Zobor,D., Andreasson,S.O., Ayuso,C., Banfi,S.,
            Bocquet,B., Bernd,A.S., Biskup,S., Boon,C.J.F., Downes,S.M.,
            Fischer,M.D., Holz,F.G., Kellner,U., Leroy,B.P., Meunier,I.,
            Nasser,F., Rosenberg,T., Rudolph,G., Stingl,K., Thiadens,A.A.H.J.,
            Wilhelm,B., Wissinger,B., Zrenner,E., Kohl,S. and Weisschuh,N.
  CONSRTM   RD-CURE Consortium
  TITLE     Clinical Phenotype and Course of PDE6A-Associated Retinitis
            Pigmentosa Disease, Characterized in Preparation for a Gene
            Supplementation Trial
  JOURNAL   JAMA Ophthalmol 138 (12), 1241-1250 (2020)
   PUBMED   33057649
  REMARK    GeneRIF: Clinical Phenotype and Course of PDE6A-Associated
            Retinitis Pigmentosa Disease, Characterized in Preparation for a
            Gene Supplementation Trial.
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Khateb,S., Nassisi,M., Bujakowska,K.M., Mejecase,C., Condroyer,C.,
            Antonio,A., Foussard,M., Demontant,V., Mohand-Said,S., Sahel,J.A.,
            Zeitz,C. and Audo,I.
  TITLE     Longitudinal Clinical Follow-up and Genetic Spectrum of Patients
            With Rod-Cone Dystrophy Associated With Mutations in PDE6A and
            PDE6B
  JOURNAL   JAMA Ophthalmol 137 (6), 669-679 (2019)
   PUBMED   30998820
  REMARK    GeneRIF: Mutations in PDE6A and PDE6B accounted for 1.6% and 2.4%,
            respectively, in a cohort of French patients with rod-cone
            dystrophy (RCD)
REFERENCE   6  (residues 1 to 860)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   7  (residues 1 to 860)
  AUTHORS   Catty,P., Pfister,C., Bruckert,F. and Deterre,P.
  TITLE     The cGMP phosphodiesterase-transducin complex of retinal rods.
            Membrane binding and subunits interactions
  JOURNAL   J Biol Chem 267 (27), 19489-19493 (1992)
   PUBMED   1326553
REFERENCE   8  (residues 1 to 860)
  AUTHORS   Pittler,S.J. and Baehr,W.
  TITLE     The molecular genetics of retinal photoreceptor proteins involved
            in cGMP metabolism
  JOURNAL   Prog Clin Biol Res 362, 33-66 (1991)
   PUBMED   1672236
  REMARK    Review article
REFERENCE   9  (residues 1 to 860)
  AUTHORS   Pittler,S.J., Baehr,W., Wasmuth,J.J., McConnell,D.G.,
            Champagne,M.S., vanTuinen,P., Ledbetter,D. and Davis,R.L.
  TITLE     Molecular characterization of human and bovine rod photoreceptor
            cGMP phosphodiesterase alpha-subunit and chromosomal localization
            of the human gene
  JOURNAL   Genomics 6 (2), 272-283 (1990)
   PUBMED   2155175
REFERENCE   10 (residues 1 to 860)
  AUTHORS   Takemoto,D.J. and Cunnick,J.M.
  TITLE     Visual transduction in rod outer segments
  JOURNAL   Cell Signal 2 (2), 99-104 (1990)
   PUBMED   2169289
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M26061.1, BC035909.1,
            AC008427.9, AC008545.3 and BU734142.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 21, 2008 this sequence version replaced NP_000431.1.
            
            Summary: This gene encodes the cyclic-GMP (cGMP)-specific
            phosphodiesterase 6A alpha subunit, expressed in cells of the
            retinal rod outer segment. The phosphodiesterase 6 holoenzyme is a
            heterotrimer composed of an alpha, beta, and two gamma subunits.
            cGMP is an important regulator of rod cell membrane current, and
            its dynamic concentration is established by phosphodiesterase 6A
            cGMP hydrolysis and guanylate cyclase cGMP synthesis. The protein
            is a subunit of a key phototransduction enzyme and participates in
            processes of transmission and amplification of the visual signal.
            Mutations in this gene have been identified as one cause of
            autosomal recessive retinitis pigmentosa. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M26061.1, BC035909.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000255266.10/ ENSP00000255266.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..860
                     /product="rod cGMP-specific 3',5'-cyclic phosphodiesterase
                     subunit alpha isoform 1"
                     /EC_number="3.1.4.35"
                     /note="rod cGMP-specific 3',5'-cyclic phosphodiesterase
                     subunit alpha; cGMP phosphodiesterase alpha subunit; rod
                     photoreceptor cGMP phosphodiesterase alpha subunit; PDE
                     V-B1; GMP-PDE alpha; phosphodiesterase 6A, cGMP-specific,
                     rod, alpha; retinitis pigmentosa type 43"
                     /calculated_mol_wt=99417
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0000250|UniProtKB:P11541; propagated from
                     UniProtKB/Swiss-Prot (P16499.4)"
     Region          75..232
                     /region_name="GAF"
                     /note="Domain present in phytochromes and cGMP-specific
                     phosphodiesterases; smart00065"
                     /db_xref="CDD:214500"
     Region          254..441
                     /region_name="GAF"
                     /note="Domain present in phytochromes and cGMP-specific
                     phosphodiesterases; smart00065"
                     /db_xref="CDD:214500"
     Region          558..802
                     /region_name="PDEase_I"
                     /note="3'5'-cyclic nucleotide phosphodiesterase;
                     pfam00233"
                     /db_xref="CDD:459723"
     Region          821..860
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16499.4)"
     Site            857
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P16499.4)"
     CDS             1..860
                     /gene="PDE6A"
                     /gene_synonym="CGPR-A; PDEA; RP43"
                     /coded_by="NM_000440.3:121..2703"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4299.1"
                     /db_xref="GeneID:5145"
                     /db_xref="HGNC:HGNC:8785"
                     /db_xref="MIM:180071"
ORIGIN      
        1 mgevtaeeve kfldsnigfa kqyynlhyra klisdllgak eaavdfsnyh spssmeesei
       61 ifdllrdfqe nlqtekcifn vmkklcfllq adrmslfmyr trngiaelat rlfnvhkdav
      121 ledclvmpdq eivfpldmgi vghvahskki anvpnteede hfcdfvdilt eyktknilas
      181 pimngkdvva iimavnkvdg shftkrdeei llkylnfanl imkvyhlsyl hncetrrgqi
      241 llwsgskvfe eltdierqfh kalytvrafl ncdrysvgll dmtkqkeffd vwpvlmgevp
      301 pysgprtpdg reinfykvid yilhgkedik vipnpppdhw alvsglpayv aqnglicnim
      361 napaedffaf qkepldesgw miknvlsmpi vnkkeeivgv atfynrkdgk pfdemdetlm
      421 esltqflgws vlnpdtyesm nklenrkdif qdivkyhvkc dneeiqkilk trevygkepw
      481 eceeeelaei lqaelpdadk yeinkfhfsd lpltelelvk cgiqmyyelk vvdkfhipqe
      541 alvrfmysls kgyrkityhn wrhgfnvgqt mfsllvtgkl kryftdleal amvtaafchd
      601 idhrgtnnly qmksqnplak lhgssilerh hlefgktllr deslnifqnl nrrqhehaih
      661 mmdiaiiatd lalyfkkrtm fqkivdqskt yeseqewtqy mmleqtrkei vmammmtacd
      721 lsaitkpwev qsqvallvaa efweqgdler tvlqqnpipm mdrnkadelp klqvgfidfv
      781 ctfvykefsr fheeitpmld gitnnrkewk aladeydakm kvqeekkqkq qsaksaaagn
      841 qpggnpspgg attskscciq
//
LOCUS       NP_001356861             643 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001356861 XP_016884496
VERSION     NP_001356861.1
DBSOURCE    REFSEQ: accession NM_001369932.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            On Apr 24, 2019 this sequence version replaced XP_016884496.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.81772.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..643
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 9"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=73067
     Region          355..394
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..643
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369932.1:545..2476"
                     /note="isoform 9 is encoded by transcript variant 15"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mqkrlhrsvf ltflrmsthk eskdhfisps afgeilynnf lfdipkildl cvlfgkgnsp
       61 llqkmignif tqqpsyysdl detlptilqv fsnilqhcgl qgdganttpq kleergrltp
      121 sdmpllelkd ivlylcdtct tlwafldifp lacqtfqkhd fcyrlasfye aaipemesai
      181 kkrrledskl lgdlwqrlsh srkklmeifh iilnqicllp ilesscdniq gfieeflqif
      241 ssllqekrfl rdydalfpva edisllqqas svldetrtay ilqavesawe gvdrrkatda
      301 kdpsvieepn gepngvtvta eavsqasshp enseeeecmg aaaavgpamc gveldslisq
      361 vkdllpdlge gfilacleyy hydpeqvinn ileerlaptl sqldrnldre mkpdptpllt
      421 srhnvfqnde fdvfsrdsvd lsrvhkgkst rkeentrsll ndkravaaqr qryeqysvvv
      481 eevplqpges lpyhsvyyed eyddtydgnq vgandadsdd elisrrpfti pqvlrtkvpr
      541 egqeedddde eddadeeapk pdhfvqdpav lrekaearrm aflakkgyrh dsstavagsp
      601 rghgqsrett qerrkkeank atranhnrrt madrkrskgm ips
//
LOCUS       NP_001531                205 aa            linear   PRI 27-APR-2025
DEFINITION  heat shock protein beta-1 [Homo sapiens].
ACCESSION   NP_001531
VERSION     NP_001531.1
DBSOURCE    REFSEQ: accession NM_001540.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Meng,J., Fang,J., Bao,Y., Chen,H., Hu,X., Wang,Z., Li,M., Cheng,Q.,
            Dong,Y., Yang,X., Zou,Y., Zhao,D., Tang,J., Zhang,W. and Chen,C.
  TITLE     The biphasic role of Hspb1 on ferroptotic cell death in Parkinson's
            disease
  JOURNAL   Theranostics 14 (12), 4643-4666 (2024)
   PUBMED   39239519
  REMARK    GeneRIF: The biphasic role of Hspb1 on ferroptotic cell death in
            Parkinson's disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Tieliwaerdi,A., Aini,A., Amuti,M., Aierken,Y., Nijiati,M. and
            Luo,B.
  TITLE     STUB1 promotes the degradation of HSPB1 and induces ferroptosis in
            lung cancer cells
  JOURNAL   Environ Toxicol 39 (8), 4156-4170 (2024)
   PUBMED   38661247
  REMARK    GeneRIF: STUB1 promotes the degradation of HSPB1 and induces
            ferroptosis in lung cancer cells.
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Xu,Z.Y., Han,J., Yang,K., Zhang,G.M., Jiao,M.N., Liang,S.X.,
            Yan,Y.B. and Chen,W.
  TITLE     HSP27 promotes vasculogenic mimicry formation in human salivary
            adenoid cystic carcinoma via the AKT-MMP-2/9 pathway
  JOURNAL   Oral Surg Oral Med Oral Pathol Oral Radiol 137 (5), 515-528 (2024)
   PUBMED   38553306
  REMARK    GeneRIF: HSP27 promotes vasculogenic mimicry formation in human
            salivary adenoid cystic carcinoma via the AKT-MMP-2/9 pathway.
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Homa,K. and Zur-Wyrozumska,K.
  TITLE     HSPB1 mutation causing distal Hereditary Motor Neuropathy type 2B
            in a Polish family
  JOURNAL   Folia Med Cracov 63 (4), 57-61 (2023)
   PUBMED   38578345
  REMARK    GeneRIF: HSPB1 mutation causing distal Hereditary Motor Neuropathy
            type 2B in a Polish family.
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Stokoe,D., Engel,K., Campbell,D.G., Cohen,P. and Gaestel,M.
  TITLE     Identification of MAPKAP kinase 2 as a major enzyme responsible for
            the phosphorylation of the small mammalian heat shock proteins
  JOURNAL   FEBS Lett 313 (3), 307-313 (1992)
   PUBMED   1332886
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Kato,K., Shinohara,H., Goto,S., Inaguma,Y., Morishita,R. and
            Asano,T.
  TITLE     Copurification of small heat shock protein with alpha B crystallin
            from human skeletal muscle
  JOURNAL   J Biol Chem 267 (11), 7718-7725 (1992)
   PUBMED   1560006
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Landry,J., Lambert,H., Zhou,M., Lavoie,J.N., Hickey,E., Weber,L.A.
            and Anderson,C.W.
  TITLE     Human HSP27 is phosphorylated at serines 78 and 82 by heat shock
            and mitogen-activated kinases that recognize the same amino acid
            motif as S6 kinase II
  JOURNAL   J Biol Chem 267 (2), 794-803 (1992)
   PUBMED   1730670
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP231480.1 and BC012768.2.
            
            Summary: This gene encodes a member of the small heat shock protein
            (HSP20) family of proteins. In response to environmental stress,
            the encoded protein translocates from the cytoplasm to the nucleus
            and functions as a molecular chaperone that promotes the correct
            folding of other proteins. This protein plays an important role in
            the differentiation of a wide variety of cell types. Expression of
            this gene is correlated with poor clinical outcome in multiple
            human cancers, and the encoded protein may promote cancer cell
            proliferation and metastasis, while protecting cancer cells from
            apoptosis. Mutations in this gene have been identified in human
            patients with Charcot-Marie-Tooth disease and distal hereditary
            motor neuropathy. [provided by RefSeq, Aug 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012292.1, X54079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248553.7/ ENSP00000248553.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..205
                     /product="heat shock protein beta-1"
                     /note="heat shock 27kD protein 1; stress-responsive
                     protein 27; epididymis secretory protein Li 102;
                     estrogen-regulated 24 kDa protein; 28 kDa heat shock
                     protein; heat shock 27 kDa protein; heat shock 27kDa
                     protein 1; heat shock protein family B member 1"
                     /calculated_mol_wt=22651
     Site            12
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2 and MAPKAPK3.
                     /evidence=ECO:0000269|PubMed:10383393,
                     ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:8774846,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P04792.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42930; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Region          70..205
                     /region_name="Interaction with TGFB1I1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04792.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2, MAPKAPK3 and MAPKAPK5.
                     /evidence=ECO:0000269|PubMed:10383393,
                     ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:15976317,
                     ECO:0000269|PubMed:1730670, ECO:0000269|PubMed:19166925,
                     ECO:0000269|PubMed:8774846, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P04792.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2, MAPKAPK3 and MAPKAPK5.
                     /evidence=ECO:0000269|PubMed:10383393,
                     ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:15976317,
                     ECO:0000269|PubMed:1730670, ECO:0000269|PubMed:19166925,
                     ECO:0000269|PubMed:8774846, ECO:0000269|Ref.14,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Region          84..169
                     /region_name="ACD_HspB1_like"
                     /note="Alpha crystallin domain (ACD) found in mammalian
                     small (s)heat shock protein (Hsp)-27 (also denoted HspB1
                     in human) and similar proteins. sHsps are molecular
                     chaperones that suppress protein aggregation and protect
                     against cell stress, and are generally...; cd06475"
                     /db_xref="CDD:107230"
     Site            order(84..88,98,100,102..103,140,161..162)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:107230"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P04792.2)"
     CDS             1..205
                     /gene="HSPB1"
                     /gene_synonym="CMT2F; HEL-S-102; HMN2B; HMND3; HS.76067;
                     Hsp25; HSP27; HSP28; SRP27"
                     /coded_by="NM_001540.5:41..658"
                     /db_xref="CCDS:CCDS5583.1"
                     /db_xref="GeneID:3315"
                     /db_xref="HGNC:HGNC:5246"
                     /db_xref="MIM:602195"
ORIGIN      
        1 mterrvpfsl lrgpswdpfr dwyphsrlfd qafglprlpe ewsqwlggss wpgyvrplpp
       61 aaiespavaa paysralsrq lssgvseirh tadrwrvsld vnhfapdelt vktkdgvvei
      121 tgkheerqde hgyisrcftr kytlppgvdp tqvssslspe gtltveapmp klatqsneit
      181 ipvtfesraq lggpeaaksd etaak
//
LOCUS       NP_001344835             327 aa            linear   ROD 27-APR-2025
DEFINITION  G protein pathway suppressor 2 [Mus musculus].
ACCESSION   NP_001344835 XP_006533850
VERSION     NP_001344835.1
DBSOURCE    REFSEQ: accession NM_001357906.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   English,J., Orofino,J., Cederquist,C.T., Paul,I., Li,H., Auwerx,J.,
            Emili,A., Belkina,A., Cardamone,D. and Perissi,V.
  TITLE     GPS2-mediated regulation of the adipocyte secretome modulates
            adipose tissue remodeling at the onset of diet-induced obesity
  JOURNAL   Mol Metab 69, 101682 (2023)
   PUBMED   36731652
  REMARK    GeneRIF: GPS2-mediated regulation of the adipocyte secretome
            modulates adipose tissue remodeling at the onset of diet-induced
            obesity.
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Huang,Z., Efthymiadou,A., Liang,N., Fan,R. and Treuter,E.
  TITLE     Antagonistic action of GPS2 and KDM1A at enhancers governs
            alternative macrophage activation by interleukin 4
  JOURNAL   Nucleic Acids Res 51 (3), 1067-1086 (2023)
   PUBMED   36610795
  REMARK    GeneRIF: Antagonistic action of GPS2 and KDM1A at enhancers governs
            alternative macrophage activation by interleukin 4.
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Huang,Z., Liang,N., Goni,S., Damdimopoulos,A., Wang,C.,
            Ballaire,R., Jager,J., Niskanen,H., Han,H., Jakobsson,T.,
            Bracken,A.P., Aouadi,M., Venteclef,N., Kaikkonen,M.U., Fan,R. and
            Treuter,E.
  TITLE     The corepressors GPS2 and SMRT control enhancer and silencer
            remodeling via eRNA transcription during inflammatory activation of
            macrophages
  JOURNAL   Mol Cell 81 (5), 953-968 (2021)
   PUBMED   33503407
  REMARK    GeneRIF: The corepressors GPS2 and SMRT control enhancer and
            silencer remodeling via eRNA transcription during inflammatory
            activation of macrophages.
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Drareni,K., Ballaire,R., Alzaid,F., Goncalves,A., Chollet,C.,
            Barilla,S., Nguewa,J.L., Dias,K., Lemoine,S., Riveline,J.P.,
            Roussel,R., Dalmas,E., Velho,G., Treuter,E., Gautier,J.F. and
            Venteclef,N.
  TITLE     Adipocyte Reprogramming by the Transcriptional Coregulator GPS2
            Impacts Beta Cell Insulin Secretion
  JOURNAL   Cell Rep 32 (11), 108141 (2020)
   PUBMED   32937117
  REMARK    GeneRIF: Adipocyte Reprogramming by the Transcriptional Coregulator
            GPS2 Impacts Beta Cell Insulin Secretion.
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Ma,W.B., Wang,X.H., Li,C.Y., Tian,H.H., Zhang,J., Bi,J.J.,
            Ren,G.M., Tao,S.S., Liu,X., Zhang,W., Li,D.X., Chen,H., Zhan,Y.Q.,
            Yu,M., Ge,C.H., Yang,X.M. and Yin,R.H.
  TITLE     GPS2 promotes erythroid differentiation by control of the stability
            of EKLF protein
  JOURNAL   Blood 135 (25), 2302-2315 (2020)
   PUBMED   32384137
  REMARK    GeneRIF: GPS2 promotes erythroid differentiation by control of the
            stability of EKLF protein.
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Cardamone,M.D., Krones,A., Tanasa,B., Taylor,H., Ricci,L.,
            Ohgi,K.A., Glass,C.K., Rosenfeld,M.G. and Perissi,V.
  TITLE     A protective strategy against hyperinflammatory responses requiring
            the nontranscriptional actions of GPS2
  JOURNAL   Mol Cell 46 (1), 91-104 (2012)
   PUBMED   22424771
  REMARK    GeneRIF: GPS2 as a molecular guardian required for precise control
            of inflammatory responses involved in immunity and homeostasis.
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Venteclef,N., Jakobsson,T., Ehrlund,A., Damdimopoulos,A.,
            Mikkonen,L., Ellis,E., Nilsson,L.M., Parini,P., Janne,O.A.,
            Gustafsson,J.A., Steffensen,K.R. and Treuter,E.
  TITLE     GPS2-dependent corepressor/SUMO pathways govern anti-inflammatory
            actions of LRH-1 and LXRbeta in the hepatic acute phase response
  JOURNAL   Genes Dev 24 (4), 381-395 (2010)
   PUBMED   20159957
  REMARK    GeneRIF: metabolically important coregulator GPS2 functions as a
            hitherto unrecognized transrepression mediator of interactions
            between SUMOylated nuclear receptors and the N-CoR corepressor
            complex
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Zhang,D., Harry,G.J., Blackshear,P.J. and Zeldin,D.C.
  TITLE     G-protein pathway suppressor 2 (GPS2) interacts with the regulatory
            factor X4 variant 3 (RFX4_v3) and functions as a transcriptional
            co-activator
  JOURNAL   J Biol Chem 283 (13), 8580-8590 (2008)
   PUBMED   18218630
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Ishizuka,T. and Lazar,M.A.
  TITLE     The nuclear receptor corepressor deacetylase activating domain is
            essential for repression by thyroid hormone receptor
  JOURNAL   Mol Endocrinol 19 (6), 1443-1451 (2005)
   PUBMED   15695367
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL596185.12, BC138880.1 and AW046264.1.
            
            On May 1, 2018 this sequence version replaced XP_006533850.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF153696.1, SRR7345562.2232034.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 42.92 cM"
     Protein         1..327
                     /product="G protein pathway suppressor 2"
                     /calculated_mol_wt=36607
     Region          5..292
                     /region_name="G_path_suppress"
                     /note="G-protein pathway suppressor; pfam15991"
                     /db_xref="CDD:464961"
     Region          26..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q921N8.1)"
     Region          61..94
                     /region_name="interaction with SUMO.
                     /evidence=ECO:0000250|UniProtKB:Q13227"
                     /note="propagated from UniProtKB/Swiss-Prot (Q921N8.1)"
     Region          178..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q921N8.1)"
     Region          253..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q921N8.1)"
     Region          300..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q921N8.1)"
     Site            312
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:26070566,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q921N8.1)"
     Site            323
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:26070566,
                     ECO:0007744|PubMed:24129315; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0000250|UniProtKB:Q13227;
                     propagated from UniProtKB/Swiss-Prot (Q921N8.1)"
     CDS             1..327
                     /gene="Gps2"
                     /gene_synonym="GPS-2"
                     /coded_by="NM_001357906.2:119..1102"
                     /db_xref="CCDS:CCDS24922.1"
                     /db_xref="GeneID:56310"
                     /db_xref="MGI:MGI:1891751"
ORIGIN      
        1 mpallerpkl snamaralhr himmererkr qeeeevdkmm eqkmkeeqer rkkkemeerm
       61 sleetkeqil klqeklsalq eekhqlflql kkvlheeekr rrkeqsdltt ltsaayqqsl
      121 tvhtgthlls mqgspgghnr pgtlmaadra kqmfgpqvlt trhyvgsaaa fagtpehgqf
      181 qgspggaygt aqppphygpt qpayspsqql rapsafpavq ylsqpqpqpy avhghfqptq
      241 tgflqpgstl slqkqmehan qqtsfsdsss lrpmhpqalh papgllaspq lpvqiqaagk
      301 sgfattsqpg prlpfiqhsq nprfyhk
//
LOCUS       NP_996662                 82 aa            linear   PRI 27-APR-2025
DEFINITION  diphthamide biosynthesis protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_996662 XP_376210
VERSION     NP_996662.1
DBSOURCE    REFSEQ: accession NM_206831.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Denisova,E., Heidenreich,B., Nagore,E., Rachakonda,P.S., Hosen,I.,
            Akrap,I., Traves,V., Garcia-Casado,Z., Lopez-Guerrero,J.A.,
            Requena,C., Sanmartin,O., Serra-Guillen,C., Llombart,B.,
            Guillen,C., Ferrando,J., Gimeno,E., Nordheim,A., Hemminki,K. and
            Kumar,R.
  TITLE     Frequent DPH3 promoter mutations in skin cancers
  JOURNAL   Oncotarget 6 (34), 35922-35930 (2015)
   PUBMED   26416425
  REMARK    GeneRIF: The results from this study show occurrence of frequent
            somatic non-coding mutations adjacent to a pre-existing binding
            site for Ets transcription factors within the directional promoter
            of DPH3 and OXNAD1 genes in three major skin cancers.
REFERENCE   5  (residues 1 to 82)
  AUTHORS   Wu,F., Zhang,J., Sun,J., Huang,H., Ji,P., Chu,W., Yu,M., Yang,F.,
            Wu,Z., Wu,J. and Shi,Y.
  TITLE     Solution structure of human DESR1, a CSL zinc-binding protein
  JOURNAL   Proteins 71 (1), 514-518 (2008)
   PUBMED   18214955
  REMARK    GeneRIF: Solution structure of human DESR1, a CSL zinc-binding
            protein.
REFERENCE   6  (residues 1 to 82)
  AUTHORS   Liu,S., Wiggins,J.F., Sreenath,T., Kulkarni,A.B., Ward,J.M. and
            Leppla,S.H.
  TITLE     Dph3, a small protein required for diphthamide biosynthesis, is
            essential in mouse development
  JOURNAL   Mol Cell Biol 26 (10), 3835-3841 (2006)
   PUBMED   16648478
REFERENCE   7  (residues 1 to 82)
  AUTHORS   Liu,S., Milne,G.T., Kuremsky,J.G., Fink,G.R. and Leppla,S.H.
  TITLE     Identification of the proteins required for biosynthesis of
            diphthamide, the target of bacterial ADP-ribosylating toxins on
            translation elongation factor 2
  JOURNAL   Mol Cell Biol 24 (21), 9487-9497 (2004)
   PUBMED   15485916
REFERENCE   8  (residues 1 to 82)
  AUTHORS   Sjolinder,M., Uhlmann,J. and Ponstingl,H.
  TITLE     Characterisation of an evolutionary conserved protein interacting
            with the putative guanine nucleotide exchange factor DelGEF and
            modulating secretion
  JOURNAL   Exp Cell Res 294 (1), 68-76 (2004)
   PUBMED   14980502
  REMARK    GeneRIF: DelGIP1is a binding partner of deafness locus putative
            guanine nucleotide exchange factor; downregulation of DelGIP1
            induced increased extracellular secretion of proteoglycans
            indicating a possible role for DelGIP1 in the secretion process
REFERENCE   9  (residues 1 to 82)
  AUTHORS   Liu,S. and Leppla,S.H.
  TITLE     Retroviral insertional mutagenesis identifies a small protein
            required for synthesis of diphthamide, the target of bacterial
            ADP-ribosylating toxins
  JOURNAL   Mol Cell 12 (3), 603-613 (2003)
   PUBMED   14527407
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA875039.1 and AC090953.2.
            
            On Mar 22, 2004 this sequence version replaced XP_376210.1.
            
            Summary: This gene encodes a CSL zinc finger-containing protein
            that is required for dipthamide biosynthesis. The encoded protein
            is necessary for the initial step in the modification of a
            histidine residue in elongation factor-2 to diphthamide. This
            modified residue is a target for ADP ribosylation by the bacterial
            toxins diphtheria toxin and Pseudomonas exotoxin A. Alternative
            splicing results in multiple transcript variants that encode the
            same isoform. [provided by RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.235986.1,
                                           SRR1803613.12890.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000488423.2/ ENSP00000419599.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..82
                     /product="diphthamide biosynthesis protein 3 isoform 1"
                     /note="deafness locus putative guanine nucleotide exchange
                     factor interacting protein 1; zinc finger, CSL domain
                     containing 2; DPH3 homolog (KTI11, S. cerevisiae); zinc
                     finger, CSL-type containing 2; DPH3A, KTI11 homolog A;
                     Del-GEF interacting protein; DPH3, KTI11 homolog;
                     diphtheria toxin and Pseudomonas exotoxin A sensitivity
                     required gene 1; delGEF-interacting protein 1; CSL-type
                     zinc finger-containing protein 2; diphthamide biosynthesis
                     protein 3"
                     /calculated_mol_wt=9109
     Region          6..60
                     /region_name="zf-CSL"
                     /note="CSL zinc finger; pfam05207"
                     /db_xref="CDD:398744"
     CDS             1..82
                     /gene="DPH3"
                     /gene_synonym="DELGIP; DELGIP1; DESR1; DPH3A; KTI11;
                     ZCSL2"
                     /coded_by="NM_206831.3:68..316"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2629.1"
                     /db_xref="GeneID:285381"
                     /db_xref="HGNC:HGNC:27717"
                     /db_xref="MIM:608959"
ORIGIN      
        1 mavfhdevei edfqydedse tyfypcpcgd nfsitkedle ngedvatcps csliikviyd
       61 kdqfvcgetv papsankelv kc
//
LOCUS       NP_001356316             381 aa            linear   PRI 27-APR-2025
DEFINITION  guanine nucleotide-binding protein G(olf) subunit alpha isoform 2
            [Homo sapiens].
ACCESSION   NP_001356316 XP_024306932
VERSION     NP_001356316.1
DBSOURCE    REFSEQ: accession NM_001369387.1
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Sarva,H., Trosch,R., Kiss,Z.H.T., Furtado,S., Luciano,M.S.,
            Glickman,A., Raymond,D., Ozelius,L.J., Bressman,S.B. and
            Saunders-Pullman,R.
  TITLE     Deep Brain Stimulation in Isolated Dystonia With a GNAL Mutation
  JOURNAL   Mov Disord 34 (2), 301-303 (2019)
   PUBMED   30536916
  REMARK    GeneRIF: cases extend and support prior limited literature that
            suggested that cervical dystonia from GNAL mutations may
            significantly improve with GPi deep brain stimulation
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Putzel,G.G., Fuchs,T., Battistella,G., Rubien-Thomas,E.,
            Frucht,S.J., Blitzer,A., Ozelius,L.J. and Simonyan,K.
  TITLE     GNAL mutation in isolated laryngeal dystonia
  JOURNAL   Mov Disord 31 (5), 750-755 (2016)
   PUBMED   27093447
  REMARK    GeneRIF: GNAL mutation may represent one of the rare causative
            genetic factors of isolated laryngeal dystonia.
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Dos Santos,C.O., Masuho,I., da Silva-Junior,F.P., Barbosa,E.R.,
            Silva,S.M., Borges,V., Ferraz,H.B., Rocha,M.S., Limongi,J.C.,
            Martemyanov,K.A. and de Carvalho Aguiar,P.
  TITLE     Screening of GNAL variants in Brazilian patients with isolated
            dystonia reveals a novel mutation with partial loss of function
  JOURNAL   J Neurol 263 (4), 665-668 (2016)
   PUBMED   26810727
  REMARK    GeneRIF: GNAL mutations are not a common cause of dystonia in the
            Brazilian population
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Carecchio,M., Panteghini,C., Reale,C., Barzaghi,C., Monti,V.,
            Romito,L., Sasanelli,F. and Garavaglia,B.
  TITLE     Novel GNAL mutation with intra-familial clinical heterogeneity:
            Expanding the phenotype
  JOURNAL   Parkinsonism Relat Disord 23, 66-71 (2016)
   PUBMED   26725140
  REMARK    GeneRIF: We report a novel GNAL mutation in Italian family with
            adult-onset, dominantly-inherited dystonia
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Vuoristo,J.T., Berrettini,W.H., Overhauser,J., Prockop,D.J.,
            Ferraro,T.N. and Ala-Kokko,L.
  TITLE     Sequence and genomic organization of the human G-protein Golfalpha
            gene (GNAL) on chromosome 18p11, a susceptibility region for
            bipolar disorder and schizophrenia
  JOURNAL   Mol Psychiatry 5 (5), 495-501 (2000)
   PUBMED   11032382
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Kleuss,C., Raw,A.S., Lee,E., Sprang,S.R. and Gilman,A.G.
  TITLE     Mechanism of GTP hydrolysis by G-protein alpha subunits
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9828-9831 (1994)
   PUBMED   7937899
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Zigman,J.M., Westermark,G.T., LaMendola,J., Boel,E. and
            Steiner,D.F.
  TITLE     Human G(olf) alpha: complementary deoxyribonucleic acid structure
            and expression in pancreatic islets and other tissues outside the
            olfactory neuroepithelium and central nervous system
  JOURNAL   Endocrinology 133 (6), 2508-2514 (1993)
   PUBMED   8243272
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Deutschlander,A.B. and Wszolek,Z.K.
  TITLE     DYT-GNAL
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30605297
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Wilkie,T.M., Gilbert,D.J., Olsen,A.S., Chen,X.N., Amatruda,T.T.,
            Korenberg,J.R., Trask,B.J., de Jong,P., Reed,R.R., Simon,M.I. et
            al.
  TITLE     Evolution of the mammalian G protein alpha subunit multigene family
  JOURNAL   Nat Genet 1 (2), 85-91 (1992)
   PUBMED   1302014
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001120.5, DC414694.1,
            L10665.1, DA151077.1, BC050021.1, AI024119.1 and AP001269.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 8, 2019 this sequence version replaced XP_024306932.1.
            
            Summary: This gene encodes a stimulatory G protein alpha subunit
            which mediates odorant signaling in the olfactory epithelium. This
            protein couples dopamine type 1 receptors and adenosine A2A
            receptors and is widely expressed in the central nervous system.
            Mutations in this gene have been associated with dystonia 25 and
            this gene is located in a susceptibility region for bipolar
            disorder and schizophrenia. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.136758.1,
                                           SRR1660803.208199.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match :: ENST00000423027.8/ ENSP00000408489.2
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..381
                     /product="guanine nucleotide-binding protein G(olf)
                     subunit alpha isoform 2"
                     /note="guanine nucleotide-binding protein G(olf) subunit
                     alpha; guanine nucleotide binding protein (G protein),
                     alpha activating activity polypeptide, olfactory type;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide, olfactory type;
                     adenylate cyclase-stimulating G alpha protein, olfactory
                     type; heterotrimeric guanine nucleotide-binding protein
                     1O"
                     /calculated_mol_wt=44178
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P38405.1)"
     Region          43..375
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Region          44..57
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P38405.1)"
     Site            order(49,54..56,191,210,213,279..280,282,352..353)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            49..56
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(50..52,80,84,88,91,94..95,115,118,159,188,213,221,
                     225)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGK7; propagated from
                     UniProtKB/Swiss-Prot (P38405.1)"
     Region          183..191
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P38405.1)"
     Site            186..194
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            191
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(192,194,196,207,209,213..215,217,220..221,223..226)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(194,219,222..223,226)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Region          206..215
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P38405.1)"
     Site            210..213
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            211..227
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Region          275..282
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P38405.1)"
     Site            279..282
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(344..355,357..360)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Region          351..356
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P38405.1)"
     Site            352..354
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..381
                     /gene="GNAL"
                     /gene_synonym="DYT25; HG1O"
                     /coded_by="NM_001369387.1:350..1495"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS11852.1"
                     /db_xref="GeneID:2774"
                     /db_xref="HGNC:HGNC:4388"
                     /db_xref="MIM:139312"
ORIGIN      
        1 mgclggnskt tedqgvdeke rreankkiek qlqkerlayk athrllllga gesgkstivk
       61 qmrilhvngf npeekkqkil dirknvkdai vtivsamsti ippvplanpe nqfrsdyiks
      121 iapitdfeys qeffdhvkkl wddegvkacf ersneyqlid caqyflerid svslvdytpt
      181 dqdllrcrvl tsgifetrfq vdkvnfhmfd vggqrderrk wiqcfndvta iiyvaacssy
      241 nmvirednnt nrlresldlf esiwnnrwlr tisiilflnk qdmlaekvla gkskiedyfp
      301 eyanytvped atpdagedpk vtrakffird lflristatg dgkhycyphf tcavdtenir
      361 rvfndcrdii qrmhlkqyel l
//
LOCUS       NP_001347095             897 aa            linear   ROD 27-APR-2025
DEFINITION  3-hydroxy-3-methylglutaryl-coenzyme A reductase isoform 2 [Mus
            musculus].
ACCESSION   NP_001347095 XP_006517593
VERSION     NP_001347095.1
DBSOURCE    REFSEQ: accession NM_001360166.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 897)
  AUTHORS   Liepinsh,E., Zvejniece,L., Clemensson,L., Ozola,M., Vavers,E.,
            Cirule,H., Korzh,S., Skuja,S., Groma,V., Briviba,M., Grinberga,S.,
            Liu,W., Olszewski,P., Gentreau,M., Fredriksson,R., Dambrova,M. and
            Schioth,H.B.
  TITLE     Hydroxymethylglutaryl-CoA reductase activity is essential for
            mitochondrial beta-oxidation of fatty acids to prevent lethal
            accumulation of long-chain acylcarnitines in the mouse liver
  JOURNAL   Br J Pharmacol 181 (16), 2750-2773 (2024)
   PUBMED   38641905
  REMARK    GeneRIF: Hydroxymethylglutaryl-CoA reductase activity is essential
            for mitochondrial beta-oxidation of fatty acids to prevent lethal
            accumulation of long-chain acylcarnitines in the mouse liver.
REFERENCE   2  (residues 1 to 897)
  AUTHORS   Guo,C.G., Sun,R., Wang,X., Yuan,Y., Xu,Y., Li,S., Sun,X., Wang,J.,
            Hu,X., Guo,T., Chen,X.W., Xiao,R.P. and Zhang,X.
  TITLE     Intestinal SURF4 is essential for apolipoprotein transport and
            lipoprotein secretion
  JOURNAL   Mol Metab 79, 101847 (2024)
   PUBMED   38042368
REFERENCE   3  (residues 1 to 897)
  AUTHORS   Kobayashi,K., Iwasa,K., Azuma-Suzuki,R., Kawauchi,T. and
            Nabeshima,Y.I.
  TITLE     Feto-maternal cholesterol transport regulated by beta-Klotho-FGF15
            axis is essential for fetal growth
  JOURNAL   Life Sci Alliance 6 (10), e202301916 (2023)
   PUBMED   37541847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 897)
  AUTHORS   Edwards,W., Greco,T.M., Miner,G.E., Barker,N.K., Herring,L.,
            Cohen,S., Cristea,I.M. and Conlon,F.L.
  TITLE     Quantitative proteomic profiling identifies global protein network
            dynamics in murine embryonic heart development
  JOURNAL   Dev Cell 58 (12), 1087-1105 (2023)
   PUBMED   37148880
REFERENCE   5  (residues 1 to 897)
  AUTHORS   Yogev,Y., Shorer,Z., Koifman,A., Wormser,O., Drabkin,M.,
            Halperin,D., Dolgin,V., Proskorovski-Ohayon,R., Hadar,N.,
            Davidov,G., Nudelman,H., Zarivach,R., Shelef,I., Perez,Y. and
            Birk,O.S.
  TITLE     Limb girdle muscular disease caused by HMGCR mutation and statin
            myopathy treatable with mevalonolactone
  JOURNAL   Proc Natl Acad Sci U S A 120 (7), e2217831120 (2023)
   PUBMED   36745799
  REMARK    GeneRIF: Limb girdle muscular disease caused by HMGCR mutation and
            statin myopathy treatable with mevalonolactone.
REFERENCE   6  (residues 1 to 897)
  AUTHORS   Goodrum,J.F., Bouldin,T.W., Zhang,S.H., Maeda,N. and Popko,B.
  TITLE     Nerve regeneration and cholesterol reutilization occur in the
            absence of apolipoproteins E and A-I in mice
  JOURNAL   J Neurochem 64 (1), 408-416 (1995)
   PUBMED   7798939
REFERENCE   7  (residues 1 to 897)
  AUTHORS   Myohanen,S., Wahlfors,J., Alhonen,L. and Janne,J.
  TITLE     Nucleotide sequence of mouse spermidine synthase cDNA
  JOURNAL   DNA Seq 4 (5), 343-346 (1994)
   PUBMED   7803821
REFERENCE   8  (residues 1 to 897)
  AUTHORS   Hwa,J.J., Zollman,S., Warden,C.H., Taylor,B.A., Edwards,P.A.,
            Fogelman,A.M. and Lusis,A.J.
  TITLE     Genetic and dietary interactions in the regulation of HMG-CoA
            reductase gene expression
  JOURNAL   J Lipid Res 33 (5), 711-725 (1992)
   PUBMED   1352323
REFERENCE   9  (residues 1 to 897)
  AUTHORS   Helmberg,A., Fassler,R., Geley,S., Johrer,K., Kroemer,G., Bock,G.
            and Kofler,R.
  TITLE     Glucocorticoid-regulated gene expression in the immune system.
            Analysis of glucocorticoid-regulated transcripts from the mouse
            macrophage-like cell line P388D1
  JOURNAL   J Immunol 145 (12), 4332-4337 (1990)
   PUBMED   2258621
REFERENCE   10 (residues 1 to 897)
  AUTHORS   Sundaresan,S., Yang-Feng,T.L. and Francke,U.
  TITLE     Genes for HMG-CoA reductase and serotonin 1a receptor are on mouse
            chromosome 13
  JOURNAL   Somat Cell Mol Genet 15 (5), 465-469 (1989)
   PUBMED   2781417
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC154851.3.
            
            On Jan 27, 2018 this sequence version replaced XP_006517593.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.76641.1,
                                           SRR11927932.3285963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..897
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 50.65 cM"
     Protein         1..897
                     /product="3-hydroxy-3-methylglutaryl-coenzyme A reductase
                     isoform 2"
                     /EC_number="1.1.1.34"
                     /note="HMG-CoA reductase; 3-hydroxy-3-methylglutaryl-CoA
                     reductase"
                     /calculated_mol_wt=97988
     Region          11..897
                     /region_name="2A060605"
                     /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase;
                     TIGR00920"
                     /db_xref="CDD:273339"
     CDS             1..897
                     /gene="Hmgcr"
                     /gene_synonym="HMG-CoAR; Red"
                     /coded_by="NM_001360166.1:530..3223"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:15357"
                     /db_xref="MGI:MGI:96159"
ORIGIN      
        1 mrgskdceat mlsrlfrmhg lfvashpwev ivgtvtltic mmsmnmftgn nkicgwnyec
       61 pkfeedvlss diiiltitrc iailyiyfqf qnlrqlgsky ilgiaglfti fssfvfstvv
      121 ihfldkeltg lnealpffll lidlsrasal akfalssnsq devreniarg mailgptftl
      181 dalveclvig vgtmsgvrql eimccfgcms vlanyfvfmt ffpacvslvl elsresregr
      241 piwqlshfar vleeeenkpn pvtqrvkmim slglvlvhah srwiadpspq nstaeqakvs
      301 lgldedvskr iepsvslwqf ylskmismdi eqvitlslaf llavkyiffe qaetestlsl
      361 knpitspvvt skkaqdnccr repllvrrnq klssveedpg anqerkvevi kplvveaett
      421 sratfvlgas vasppsalgt qepgielpie prpneeclqi lenaekgakf lsdaeiiqlv
      481 nakhipaykl etlmetherg vsirrqllst klaepsslqy lpyrdynysl vmgaccenvi
      541 gympipvgva gplcldgkey qvpmattegc lvastnrgcr aislgggass rvladgmtrg
      601 pvvrlpracd saevktwlet pegfavikea fdstsrfarl qklhvtmagr nlyirfqsrt
      661 gdamgmnmis kgtekallkl qeffpdmqil avsgnyctdk kpaainwieg rgktvvceav
      721 ipakvvrevl kttteamvdv ninknlvgsa magsiggyna haanivtaiy iacgqdaaqn
      781 vgssncitlm easgptnedl yisctmpsie igtvgggtnl lpqqaclqml gvqgackdnp
      841 genarqlari vcgtvmagel slmaalaagh lvrshmvhnr skinlqdlqg tctkkaa
//
LOCUS       NP_001008221             134 aa            linear   PRI 27-APR-2025
DEFINITION  complexin-2 [Homo sapiens].
ACCESSION   NP_001008221
VERSION     NP_001008221.1
DBSOURCE    REFSEQ: accession NM_001008220.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Chen,Y., Ning,J., Shu,L., Wen,L., Yan,B., Wang,Z., Hu,J., Zhou,X.,
            Tao,Y., Xia,X. and Huang,J.
  TITLE     CPLX2 is a novel tumor suppressor and improves the prognosis in
            glioma
  JOURNAL   J Neurooncol 167 (1), 63-74 (2024)
   PUBMED   38427133
  REMARK    GeneRIF: CPLX2 is a novel tumor suppressor and improves the
            prognosis in glioma.
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Li,H., Zhao,J., Zhong,X.L., Xu,P.Y., Du,L.J., Fang,P., Tan,L.J.,
            Li,M.J., Zhang,C.F. and Cao,T.S.
  TITLE     CPLX2 Regulates Ferroptosis and Apoptosis Through NRF2 Pathway in
            Human Hepatocellular Carcinoma Cells
  JOURNAL   Appl Biochem Biotechnol 195 (1), 597-609 (2023)
   PUBMED   36107387
  REMARK    GeneRIF: CPLX2 Regulates Ferroptosis and Apoptosis Through NRF2
            Pathway in Human Hepatocellular Carcinoma Cells.
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Ramos-Miguel,A., Sawada,K., Jones,A.A., Thornton,A.E., Barr,A.M.,
            Leurgans,S.E., Schneider,J.A., Bennett,D.A. and Honer,W.G.
  TITLE     Presynaptic proteins complexin-I and complexin-II differentially
            influence cognitive function in early and late stages of
            Alzheimer's disease
  JOURNAL   Acta Neuropathol 133 (3), 395-407 (2017)
   PUBMED   27866231
  REMARK    GeneRIF: This study demonstrated that complexin-II differentially
            influence cognitive function in early and late stages of
            Alzheimer's disease.
REFERENCE   5  (residues 1 to 134)
  AUTHORS   Kurokawa,A., Narukawa,M., Ohmoto,M., Yoshimoto,J., Abe,K. and
            Misaka,T.
  TITLE     Expression of the synaptic exocytosis-regulating molecule complexin
            2 in taste buds and its participation in peripheral taste
            transduction
  JOURNAL   J Neurochem 133 (6), 806-814 (2015)
   PUBMED   25692331
  REMARK    GeneRIF: These results suggested that CPLX2 participated in
            synaptic taste transduction.
REFERENCE   6  (residues 1 to 134)
  AUTHORS   Yamada,M., Saisu,H., Ishizuka,T., Takahashi,H. and Abe,T.
  TITLE     Immunohistochemical distribution of the two isoforms of
            synaphin/complexin involved in neurotransmitter release:
            localization at the distinct central nervous system regions and
            synaptic types
  JOURNAL   Neuroscience 93 (1), 7-18 (1999)
   PUBMED   10430466
REFERENCE   7  (residues 1 to 134)
  AUTHORS   Harrison,P.J. and Eastwood,S.L.
  TITLE     Preferential involvement of excitatory neurons in medial temporal
            lobe in schizophrenia
  JOURNAL   Lancet 352 (9141), 1669-1673 (1998)
   PUBMED   9853440
  REMARK    Erratum:[Lancet 1999 Jan 9;353(9147):154]
REFERENCE   8  (residues 1 to 134)
  AUTHORS   Morgans,C.W., Brandstatter,J.H., Kellerman,J., Betz,H. and
            Wassle,H.
  TITLE     A SNARE complex containing syntaxin 3 is present in ribbon synapses
            of the retina
  JOURNAL   J Neurosci 16 (21), 6713-6721 (1996)
   PUBMED   8824312
REFERENCE   9  (residues 1 to 134)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   10 (residues 1 to 134)
  AUTHORS   Christensen,V.L. and Johnston,N.P.
  TITLE     Effect of time of day of insemination and the position of the egg
            in the oviduct on the fertility of turkeys
  JOURNAL   Poult Sci 56 (2), 458-462 (1977)
   PUBMED   605033
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY576870.1, U35100.1,
            BI197868.1, AK124837.1 and AC138965.2.
            
            Summary: Proteins encoded by the complexin/synaphin gene family are
            cytosolic proteins that function in synaptic vesicle exocytosis.
            These proteins bind syntaxin, part of the SNAP receptor. The
            protein product of this gene binds to the SNAP receptor complex and
            disrupts it, allowing transmitter release. Two transcript variants
            encoding the same protein have been found for this gene. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BN000500.2, SRR1803617.207302.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393745.8/ ENSP00000377346.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..134
                     /product="complexin-2"
                     /note="synaphin 1; CPX II; complexin II"
                     /calculated_mol_wt=15263
     Region          1..133
                     /region_name="Synaphin"
                     /note="Synaphin protein; pfam05835"
                     /db_xref="CDD:461755"
     Region          1..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PUV4.2)"
     Region          41..97
                     /region_name="Interaction with the SNARE complex.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PUV4.2)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P84087; propagated from
                     UniProtKB/Swiss-Prot (Q6PUV4.2)"
     CDS             1..134
                     /gene="CPLX2"
                     /gene_synonym="921-L; CPX-2; CPX2; Hfb1"
                     /coded_by="NM_001008220.2:217..621"
                     /db_xref="CCDS:CCDS4396.1"
                     /db_xref="GeneID:10814"
                     /db_xref="HGNC:HGNC:2310"
                     /db_xref="MIM:605033"
ORIGIN      
        1 mdfvmkqalg gatkdmgkml ggeeekdpda qkkeeerqea lrqqeeerka kharmeaere
       61 kvrqqirdky glkkkeekea eekaaleqpc egsltrpkka ipagcgdeee eeeesildtv
      121 lkylpgplqd mfkk
//
LOCUS       NP_001354460             529 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 24 [Homo sapiens].
ACCESSION   NP_001354460 XP_005270260
VERSION     NP_001354460.1
DBSOURCE    REFSEQ: accession NM_001367531.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_005270260.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.219725.1,
                                           SRR3476690.807601.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..529
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 24"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=59476
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          397..524
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..529
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367531.1:95..1684"
                     /note="isoform 24 is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS91267.1"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk krkssssvhl mpqsnnknsl vspaqepapl
      361 qtamepqttv vhnatdgikg stescnttte dedlkvrkqe iikiteqlie ainngdfeay
      421 tkicdpglts fepealgnlv egmdfhkfyf enllsknskp ihttilnphv hvigedaaci
      481 ayirltqyid gqgrprtsqs eetrvwhrrd gkwlnvhyhc sgapaaplq
//
LOCUS       NP_001036694             240 aa            linear   PRI 27-APR-2025
DEFINITION  citrate synthase-lysine N-methyltransferase CSKMT, mitochondrial
            precursor [Homo sapiens].
ACCESSION   NP_001036694
VERSION     NP_001036694.1
DBSOURCE    REFSEQ: accession NM_001043229.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Malecki,J., Jakobsson,M.E., Ho,A.Y.Y., Moen,A., Rustan,A.C. and
            Falnes,P.O.
  TITLE     Uncovering human METTL12 as a mitochondrial methyltransferase that
            modulates citrate synthase activity through metabolite-sensitive
            lysine methylation
  JOURNAL   J Biol Chem 292 (43), 17950-17962 (2017)
   PUBMED   28887308
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Rhein,V.F., Carroll,J., Ding,S., Fearnley,I.M. and Walker,J.E.
  TITLE     Human METTL12 is a mitochondrial methyltransferase that modifies
            citrate synthase
  JOURNAL   FEBS Lett 591 (12), 1641-1652 (2017)
   PUBMED   28391595
  REMARK    GeneRIF: Data suggest that METTL12, localized in mitochondrial
            matrix, modifies/methylates Lys368 of citrate synthase in external
            surface region close to its catalytic site; addition/removal of
            methylation has no effect on citrate synthase activity; Lys368
            occurs in highly conserved sequence of amino acid residues of
            citrate synthase.
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Weber,M.J.
  TITLE     Mammalian small nucleolar RNAs are mobile genetic elements
  JOURNAL   PLoS Genet 2 (12), e205 (2006)
   PUBMED   17154719
  REMARK    Erratum:[PLoS Genet. 2007 Feb;3(2):e36]
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Taylor,T.D., Noguchi,H., Totoki,Y., Toyoda,A., Kuroki,Y., Dewar,K.,
            Lloyd,C., Itoh,T., Takeda,T., Kim,D.W., She,X., Barlow,K.F.,
            Bloom,T., Bruford,E., Chang,J.L., Cuomo,C.A., Eichler,E.,
            FitzGerald,M.G., Jaffe,D.B., LaButti,K., Nicol,R., Park,H.S.,
            Seaman,C., Sougnez,C., Yang,X., Zimmer,A.R., Zody,M.C.,
            Birren,B.W., Nusbaum,C., Fujiyama,A., Hattori,M., Rogers,J.,
            Lander,E.S. and Sakaki,Y.
  TITLE     Human chromosome 11 DNA sequence and analysis including novel gene
            identification
  JOURNAL   Nature 440 (7083), 497-500 (2006)
   PUBMED   16554811
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Choy,K.W., Wang,C.C., Ogura,A., Lau,T.K., Rogers,M.S., Ikeo,K.,
            Gojobori,T., Lam,D.S. and Pang,C.P.
  TITLE     Genomic annotation of 15,809 ESTs identified from pooled early
            gestation human eyes
  JOURNAL   Physiol Genomics 25 (1), 9-15 (2006)
   PUBMED   16368877
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001458.6, BY796224.2, BX348415.2 and BG676615.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.241705.1,
                                           SRR1803611.81617.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144335, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000532971.2/
                                                  ENSP00000431287.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..240
                     /product="citrate synthase-lysine N-methyltransferase
                     CSKMT, mitochondrial precursor"
                     /EC_number="2.1.1.-"
                     /note="methyltransferase-like protein 12, mitochondrial;
                     methyltransferase like 12; citrate synthase-lysine
                     N-methyltransferase CSKMT, mitochondrial"
                     /calculated_mol_wt=22893
     transit_peptide 1..28
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:28887308; propagated from
                     UniProtKB/Swiss-Prot (A8MUP2.1)"
                     /calculated_mol_wt=3035
     mat_peptide     29..240
                     /product="Citrate synthase-lysine N-methyltransferase
                     CSKMT, mitochondrial. /id=PRO_0000349199"
                     /note="propagated from UniProtKB/Swiss-Prot (A8MUP2.1)"
                     /calculated_mol_wt=22893
     Region          75..>207
                     /region_name="Methyltransf_31"
                     /note="Methyltransferase domain; pfam13847"
                     /db_xref="CDD:463998"
     CDS             1..240
                     /gene="CSKMT"
                     /gene_synonym="CS-KMT; METTL12; U99HG"
                     /coded_by="NM_001043229.2:255..977"
                     /db_xref="CCDS:CCDS41657.1"
                     /db_xref="GeneID:751071"
                     /db_xref="HGNC:HGNC:33113"
                     /db_xref="MIM:617897"
ORIGIN      
        1 maalrrmlhl pslmmgtcrp fagsladscl adrclwdrlh aqprlgtvpt fdwffgydev
       61 qglllpllqe aqaasplrvl dvgcgtsslc tglytksphp vdvlgvdfsp vavahmnsll
      121 eggpgqtplc pghpasslhf mhadaqnlga vassgsfqll ldkgtwdava rgglprayql
      181 lseclrvlnp qgtliqfsde dpdvrlpcle qgsygwtvtv qelgpfrgit yfayliqgsh
//
LOCUS       NP_001346399             351 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 19 isoform 1 [Mus musculus].
ACCESSION   NP_001346399 XP_017169556
VERSION     NP_001346399.1
DBSOURCE    REFSEQ: accession NM_001359470.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Lu,Y., Oura,S., Matsumura,T., Oji,A., Sakurai,N., Fujihara,Y.,
            Shimada,K., Miyata,H., Tobita,T., Noda,T., Castaneda,J.M.,
            Kiyozumi,D., Zhang,Q., Larasati,T., Young,S.A.M., Kodani,M.,
            Huddleston,C.A., Robertson,M.J., Coarfa,C., Isotani,A.,
            Aitken,R.J., Okabe,M., Matzuk,M.M., Garcia,T.X. and Ikawa,M.
  TITLE     CRISPR/Cas9-mediated genome editing reveals 30 testis-enriched
            genes dispensable for male fertility in micedagger
  JOURNAL   Biol Reprod 101 (2), 501-511 (2019)
   PUBMED   31201419
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BB636118.1, AK034298.1, AK138931.1 and AC153497.8.
            
            On Jan 13, 2018 this sequence version replaced XP_017169556.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK036228.1, AK042426.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 63.51 cM"
     Protein         1..351
                     /product="transmembrane protein 19 isoform 1"
                     /calculated_mol_wt=37759
     Region          74..337
                     /region_name="DUF92"
                     /note="Integral membrane protein DUF92; pfam01940"
                     /db_xref="CDD:460391"
     CDS             1..351
                     /gene="Tmem19"
                     /gene_synonym="2810428F02Rik"
                     /coded_by="NM_001359470.1:267..1322"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS88087.1"
                     /db_xref="GeneID:67226"
                     /db_xref="MGI:MGI:1914476"
ORIGIN      
        1 mlsipppqvl valfsmtdsd dttckryikm itnivilsli icislafwim smtastyygn
       61 frpvspwrwl fsvvvpvvia cngfkkksld hsgalgglvv gfiltianfs fftslmtffl
      121 ssskltkwrg nikkqldsey keggqrnwvq vfcngavpte lallymieng pgempidfsk
      181 qhtaswmcls llaalassag dtwasevapv lskssprlit twekvpvgtn ggvtavglas
      241 sllggtfvgl ayfltqlvfv ndldisapqw piiafggvag lfgslvdsfl gatmqfsgld
      301 ertglvvssp tqetkhiagk pildnnavnl fssvlvalll ptaasgfwpr e
//
LOCUS       NP_056197               2610 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 1 [Homo sapiens].
ACCESSION   NP_056197
VERSION     NP_056197.3
DBSOURCE    REFSEQ: accession NM_015382.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2610)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2610)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2610)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2610)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 2610)
  AUTHORS   Harris,L.D., Le Pen,J., Scholz,N., Mieszczanek,J., Vaughan,N.,
            Davis,S., Berridge,G., Kessler,B.M., Bienz,M. and Licchesi,J.D.F.
  TITLE     The deubiquitinase TRABID stabilizes the K29/K48-specific E3
            ubiquitin ligase HECTD1
  JOURNAL   J Biol Chem 296, 100246 (2021)
   PUBMED   33853758
  REMARK    GeneRIF: The deubiquitinase TRABID stabilizes the K29/K48-specific
            E3 ubiquitin ligase HECTD1.
REFERENCE   6  (residues 1 to 2610)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2610)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2610)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2610)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2610)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, DA509926.1, DA818448.1, DA440215.1, AY254380.1,
            AB032957.2 and BM977042.1.
            
            On Apr 16, 2014 this sequence version replaced NP_056197.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.155868.1,
                                           SRR1803612.230324.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399332.6/ ENSP00000382269.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2610
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2610
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 1"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=289239
     Region          246..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          395..424
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          426..455
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          459..491
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          489..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          579..612
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          627..657
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          707..748
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..1335
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Region          1343..1406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1433..1483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1496..1515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1592..1611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1674..1757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1760
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1777..1797
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1893..1958
                     /region_name="BTHB_HectD1"
                     /note="basic tilted helix bundle (BTHB) domain found in
                     HECT domain-containing protein 1 (HectD1) and similar
                     proteins; cd21062"
                     /db_xref="CDD:439138"
     Region          2029..2103
                     /region_name="K-box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          2131..2608
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(2137,2166,2176,2263,2541,2573..2574,2577..2581,2601,
                     2607)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          2297..2318
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            2318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            order(2356,2359..2360,2362..2363,2366,2408,2410,
                     2414..2415,2417,2423,2428,2445,2449)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2610
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_015382.4:800..8632"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41939.1"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhngwi dvtwdaggsn
     1321 syrmgaegkf dlklapgydp dtvaspkpvs stvsgttqsw sslvknncpd ktsaaagsss
     1381 rkgssssvcs vasssdislg stkterrsei vmehsivsga dvhepivvls saenvpqtev
     1441 gssssastst ltaetgsena erklgpdssv rtpgessais mgivsvsspd vssvseltnk
     1501 eaasqrplss sasnrlsvss llaagapmss sasvpnlssr etsslesfvr rvaniartna
     1561 tnnmnlsrss sdnntntlgr nvmstatspl mgaqsfpnlt tpgttstvtm stssvtsssn
     1621 vatattvlsv gqslsntltt sltstssesd tgqeaeysly dfldscrast llaelddded
     1681 lpepdeedde neddnqedqe yeevmilrrp slqrragsrs dvthhavtsq lpqvpagags
     1741 rpigeqeeee yetkggrrrt wdddyvlkrq fsalvpafdp rpgrtnvqqt tdleipppgt
     1801 phselleeve ctpsprlalt lkvtglgttr evelpltnfr stifyyvqkl lqlscngnvk
     1861 sdklrriwep tytimyremk dsdkekengk mgcwsiehve qylgtdelpk ndlitylqkn
     1921 adaaflrhwk ltgtnksirk nrncsqliaa ykdfcehgtk sglnqgaist lqssdilnlt
     1981 keqpqakagn gqnscgvedv lqllrilyiv asdpysrisq edgdeqpqft fppdeftskk
     2041 ittkilqqie eplalasgal pdwceqltsk cpflipfetr qlyftctafg asraivwlqn
     2101 rreatvertr ttssvrrddp gefrvgrlkh ervkvprges lmewaenvmq ihadrksvle
     2161 veflgeegtg lgptlefyal vaaefqrtdl gawlcddnfp ddesrhvdlg gglkppgyyv
     2221 qrscglftap fpqdsdeler itklfhflgi flakciqdnr lvdlpiskpf fklmcmgdik
     2281 snmskliyes rgdrdlhcte sqseasteeg hdslsvgsfe edsksefild ppkpkppawf
     2341 ngiltwedfe lvnphrarfl keikdlaikr rqilsnkgls edekntklqe lvlknpsgsg
     2401 pplsiedlgl nfqfcpssri ygftavdlkp sgedemitmd naeeyvdlmf dfcmhtgiqk
     2461 qmeafrdgfn kvfpmeklss fsheevqmil cgnqspswaa ediinytepk lgytrdspgf
     2521 lrfvrvlcgm ssderkaflq fttgcstlpp gglanlhprl tvvrkvdatd asypsvntcv
     2581 hylklpeyss eeimrerlla atmekgfhln
//
LOCUS       NP_001115                185 aa            linear   PRI 27-APR-2025
DEFINITION  pro-adrenomedullin precursor [Homo sapiens].
ACCESSION   NP_001115
VERSION     NP_001115.1
DBSOURCE    REFSEQ: accession NM_001124.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Goetze,J.P., Voiosu,A., Wiese,S., Schulte,J., Kaufmann,P.,
            Bergmann,A., Bartels,E.D. and Moller,S.
  TITLE     Peptidylglycine alpha-amidating monooxygenase and adrenomedullin
            measurement in patients with hepatic cirrhosis
  JOURNAL   Biomark Med 17 (13), 577-583 (2023)
   PUBMED   37812053
  REMARK    GeneRIF: Peptidylglycine alpha-amidating monooxygenase and
            adrenomedullin measurement in patients with hepatic cirrhosis.
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Ersahan,S., Ozcelik,F., Sirin,D.A., Hepsenoglu,Y.E., Ozcelik,I.K.
            and Topbas,C.
  TITLE     Is adrenomedullin upregulation due to apical periodontitis
            independent of periodontal disease?
  JOURNAL   Odontology 111 (3), 708-718 (2023)
   PUBMED   36414882
  REMARK    GeneRIF: Is adrenomedullin upregulation due to apical periodontitis
            independent of periodontal disease?
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Dong,Y., Vipin,V.A., Blesson,C.S. and Yallampalli,C.
  TITLE     Impact of adrenomedullin on mitochondrial respiratory capacity in
            human adipocyte
  JOURNAL   Sci Rep 13 (1), 9578 (2023)
   PUBMED   37311963
  REMARK    GeneRIF: Impact of adrenomedullin on mitochondrial respiratory
            capacity in human adipocyte.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Balint,L., Nelson-Maney,N.P., Tian,Y., Serafin,S.D. and Caron,K.M.
  TITLE     Clinical Potential of Adrenomedullin Signaling in the
            Cardiovascular System
  JOURNAL   Circ Res 132 (9), 1185-1202 (2023)
   PUBMED   37104556
  REMARK    GeneRIF: Clinical Potential of Adrenomedullin Signaling in the
            Cardiovascular System.
            Review article
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Dou,W., Xie,J., Chen,J., Zhou,J., Xu,Z., Wang,Z. and Zhu,Q.
  TITLE     Overexpression of adrenomedullin (ADM) alleviates the senescence of
            human dental pulp stem cells by regulating the miR-152/CCNA2
            pathway
  JOURNAL   Cell Cycle 22 (5), 565-579 (2023)
   PUBMED   36310381
  REMARK    GeneRIF: Overexpression of adrenomedullin (ADM) alleviates the
            senescence of human dental pulp stem cells by regulating the
            miR-152/CCNA2 pathway.
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Allaker,R.P., Zihni,C. and Kapas,S.
  TITLE     An investigation into the antimicrobial effects of adrenomedullin
            on members of the skin, oral, respiratory tract and gut microflora
  JOURNAL   FEMS Immunol Med Microbiol 23 (4), 289-293 (1999)
   PUBMED   10225288
  REMARK    GeneRIF: Adrenomedullin has broad bacteriocidal activity against
            gram-positive and gram-negative bacteria.
REFERENCE   7  (residues 1 to 185)
  AUTHORS   Satoh,F., Takahashi,K., Murakami,O., Totsune,K., Sone,M.,
            Ohneda,M., Abe,K., Miura,Y., Hayashi,Y., Sasano,H. et al.
  TITLE     Adrenomedullin in human brain, adrenal glands and tumor tissues of
            pheochromocytoma, ganglioneuroblastoma and neuroblastoma
  JOURNAL   J Clin Endocrinol Metab 80 (5), 1750-1752 (1995)
   PUBMED   7745031
REFERENCE   8  (residues 1 to 185)
  AUTHORS   Ishimitsu,T., Kojima,M., Kangawa,K., Hino,J., Matsuoka,H.,
            Kitamura,K., Eto,T. and Matsuo,H.
  TITLE     Genomic structure of human adrenomedullin gene
  JOURNAL   Biochem Biophys Res Commun 203 (1), 631-639 (1994)
   PUBMED   8074714
REFERENCE   9  (residues 1 to 185)
  AUTHORS   Kitamura,K., Kangawa,K., Ishiyama,Y., Washimine,H., Ichiki,Y.,
            Kawamoto,M., Minamino,N., Matsuo,H. and Eto,T.
  TITLE     Identification and hypotensive activity of proadrenomedullin
            N-terminal 20 peptide (PAMP)
  JOURNAL   FEBS Lett 351 (1), 35-37 (1994)
   PUBMED   8076689
REFERENCE   10 (residues 1 to 185)
  AUTHORS   Kitamura,K., Sakata,J., Kangawa,K., Kojima,M., Matsuo,H. and Eto,T.
  TITLE     Cloning and characterization of cDNA encoding a precursor for human
            adrenomedullin
  JOURNAL   Biochem Biophys Res Commun 194 (2), 720-725 (1993)
   PUBMED   7688224
  REMARK    Erratum:[Biochem Biophys Res Commun 1994 Jul 15;202(1):643]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY105655.1, D14874.1 and
            BQ021632.1.
            
            Summary: The protein encoded by this gene is a preprohormone which
            is cleaved to form two biologically active peptides, adrenomedullin
            and proadrenomedullin N-terminal 20 peptide. Adrenomedullin is a 52
            aa peptide with several functions, including vasodilation,
            regulation of hormone secretion, promotion of angiogenesis, and
            antimicrobial activity. The antimicrobial activity is
            antibacterial, as the peptide has been shown to kill E. coli and S.
            aureus at low concentration. [provided by RefSeq, Aug 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.638.1,
                                           SRR3476690.854615.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000278175.10/
                                                  ENSP00000278175.5
            Protein has antimicrobial activity :: PMID: 10225288
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..185
                     /product="pro-adrenomedullin precursor"
                     /note="preproadrenomedullin; proadrenomedullin N-20
                     terminal peptide; pro-adrenomedullin"
                     /calculated_mol_wt=18238
     Region          1..150
                     /region_name="Calc_CGRP_IAPP"
                     /note="Calcitonin / CGRP / IAPP family; pfam00214"
                     /db_xref="CDD:459715"
     sig_peptide     1..21
                     /note="/evidence=ECO:0000250|UniProtKB:P53366; propagated
                     from UniProtKB/Swiss-Prot (P35318.1)"
                     /calculated_mol_wt=2201
     mat_peptide     22..41
                     /product="Proadrenomedullin N-20 terminal peptide.
                     /evidence=ECO:0000250|UniProtKB:P43145.
                     /id=PRO_0000000961"
                     /note="propagated from UniProtKB/Swiss-Prot (P35318.1)"
                     /calculated_mol_wt=2462
     Site            41
                     /site_type="amidation"
                     /note="Arginine amide.
                     /evidence=ECO:0000269|PubMed:16315141; propagated from
                     UniProtKB/Swiss-Prot (P35318.1)"
     Region          60..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35318.1)"
     mat_peptide     95..146
                     /product="adrenomedullin"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     10225288]"
                     /calculated_mol_wt=6032
     Site            116
                     /site_type="other"
                     /note="Required for CALCRL receptor interaction.
                     /evidence=ECO:0000269|PubMed:32296767; propagated from
                     UniProtKB/Swiss-Prot (P35318.1)"
     Site            125
                     /site_type="other"
                     /note="Required for CALCRL receptor interaction.
                     /evidence=ECO:0000269|PubMed:32296767; propagated from
                     UniProtKB/Swiss-Prot (P35318.1)"
     Region          133..185
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35318.1)"
     Site            146
                     /site_type="amidation"
                     /note="Tyrosine amide.
                     /evidence=ECO:0000269|PubMed:8387282; propagated from
                     UniProtKB/Swiss-Prot (P35318.1)"
     CDS             1..185
                     /gene="ADM"
                     /gene_synonym="AM; PAMP"
                     /coded_by="NM_001124.3:179..736"
                     /db_xref="CCDS:CCDS7801.1"
                     /db_xref="GeneID:133"
                     /db_xref="HGNC:HGNC:259"
                     /db_xref="MIM:103275"
ORIGIN      
        1 mklvsvalmy lgslaflgad tarldvasef rkkwnkwals rgkrelrmss syptgladvk
       61 agpaqtlirp qdmkgasrsp edsspdaari rvkryrqsmn nfqglrsfgc rfgtctvqkl
      121 ahqiyqftdk dkdnvaprsk ispqgygrrr rrslpeagpg rtlvsskpqa hgapappsgs
      181 aphfl
//
LOCUS       NP_005098                368 aa            linear   PRI 27-APR-2025
DEFINITION  nuclease EXOG, mitochondrial isoform 1 precursor [Homo sapiens].
ACCESSION   NP_005098
VERSION     NP_005098.2
DBSOURCE    REFSEQ: accession NM_005107.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Szymanski,M.R., Karlowicz,A., Herrmann,G.K., Cen,Y. and Yin,Y.W.
  TITLE     Human EXOG Possesses Strong AP Hydrolysis Activity: Implication on
            Mitochondrial DNA Base Excision Repair
  JOURNAL   J Am Chem Soc 144 (51), 23543-23550 (2022)
   PUBMED   36516439
  REMARK    GeneRIF: Human EXOG Possesses Strong AP Hydrolysis Activity:
            Implication on Mitochondrial DNA Base Excision Repair.
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Karlowicz,A., Dubiel,A.B., Czerwinska,J., Bledea,A., Purzycki,P.,
            Grzelewska,M., McAuley,R.J., Szczesny,R.J., Brzuska,G., Krol,E.,
            Szczesny,B. and Szymanski,M.R.
  TITLE     In vitro reconstitution reveals a key role of human mitochondrial
            EXOG in RNA primer processing
  JOURNAL   Nucleic Acids Res 50 (14), 7991-8007 (2022)
   PUBMED   35819194
  REMARK    GeneRIF: In vitro reconstitution reveals a key role of human
            mitochondrial EXOG in RNA primer processing.
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Wu,C.C., Lin,J.L.J., Yang-Yen,H.F. and Yuan,H.S.
  TITLE     A unique exonuclease ExoG cleaves between RNA and DNA in
            mitochondrial DNA replication
  JOURNAL   Nucleic Acids Res 47 (10), 5405-5419 (2019)
   PUBMED   30949702
  REMARK    GeneRIF: ExoG has a role as a unique 5'-exonuclease to mediate the
            flap-independent RNA primer removal process during mtDNA
            replication to maintain mitochondrial genome integrity
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Cymerman,I.A., Chung,I., Beckmann,B.M., Bujnicki,J.M. and Meiss,G.
  TITLE     EXOG, a novel paralog of Endonuclease G in higher eukaryotes
  JOURNAL   Nucleic Acids Res 36 (4), 1369-1379 (2008)
   PUBMED   18187503
  REMARK    GeneRIF: Human endonuclease G-like-1 is a dimeric mitochondrial
            enzyme that displays 5'-3' exonuclease activity and further differs
            from EndoG in substrate specificity
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Moritani,M., Nomura,K., Tanahashi,T., Osabe,D., Fujita,Y.,
            Shinohara,S., Yamaguchi,Y., Keshavarz,P., Kudo,E., Nakamura,N.,
            Yoshikawa,T., Ichiishi,E., Takata,Y., Yasui,N., Shiota,H.,
            Kunika,K., Inoue,H. and Itakura,M.
  TITLE     Genetic association of single nucleotide polymorphisms in
            endonuclease G-like 1 gene with type 2 diabetes in a Japanese
            population
  JOURNAL   Diabetologia 50 (6), 1218-1227 (2007)
   PUBMED   17415550
  REMARK    GeneRIF: ENDOGL1 is a candidate disease-susceptibility gene for
            type 2 diabetes in a Japanese population
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Daigo,Y., Isomura,M., Nishiwaki,T., Tamari,M., Ishikawa,S., Kai,M.,
            Murata,Y., Takeuchi,K., Yamane,Y., Hayashi,R., Minami,M.,
            Fujino,M.A., Hojo,Y., Uchiyama,I., Takagi,T. and Nakamura,Y.
  TITLE     Characterization of a 1200-kb genomic segment of chromosome
            3p22-p21.3
  JOURNAL   DNA Res 6 (1), 37-44 (1999)
   PUBMED   10231028
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290107.1, AB020523.1,
            AK301067.1, AP006241.1 and AA993872.1.
            
            On Feb 28, 2009 this sequence version replaced NP_005098.1.
            
            Summary: This gene encodes an endo/exonuclease with 5'-3'
            exonuclease activity. The encoded enzyme catalyzes the hydrolysis
            of ester linkages at the 5' end of a nucleic acid chain. This
            enzyme is localized to the mitochondria and may play a role in
            programmed cell death. Alternatively spliced transcript variants
            have been described. A pseudogene exists on chromosome 18.
            [provided by RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.15394.1,
                                           SRR1660809.103462.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000287675.10/
                                                  ENSP00000287675.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..368
                     /product="nuclease EXOG, mitochondrial isoform 1
                     precursor"
                     /EC_number="3.1.30.-"
                     /note="endonuclease G-like 2; endonuclease G-like 1;
                     nuclease EXOG, mitochondrial; endo G-like 1;
                     endo/exonuclease (5'-3'), endonuclease G-like"
                     /calculated_mol_wt=36934
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9Y2C4.2)"
                     /calculated_mol_wt=4169
     mat_peptide     42..368
                     /product="Nuclease EXOG, mitochondrial.
                     /id=PRO_0000178669"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2C4.2)"
                     /calculated_mol_wt=36934
     Region          77..286
                     /region_name="NUC"
                     /note="DNA/RNA non-specific endonuclease; smart00477"
                     /db_xref="CDD:214683"
     Site            order(137..138,140,171,179,183)
                     /site_type="active"
                     /db_xref="CDD:238043"
     Site            order(137..138,183)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238043"
     Site            171
                     /site_type="other"
                     /note="Mg2+ binding site [ion binding]"
                     /db_xref="CDD:238043"
     Region          302..350
                     /region_name="Exog_C"
                     /note="Endo/exonuclease (EXOG) C-terminal domain;
                     pfam18026"
                     /db_xref="CDD:465620"
     CDS             1..368
                     /gene="EXOG"
                     /gene_synonym="ENDOGL1; ENDOGL2; ENGL; ENGL-a; ENGL-b;
                     ENGLA; ENGLB"
                     /coded_by="NM_005107.4:29..1135"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2680.1"
                     /db_xref="GeneID:9941"
                     /db_xref="HGNC:HGNC:3347"
                     /db_xref="MIM:604051"
ORIGIN      
        1 maiksiasrl rgsrrflsgf vagavvgaag aglaalqffr sqgaegaltg kqpdgsaeka
       61 vleqfgfplt gtearcytnh alsydqakrv prwvlehisk skimgdadrk hckfkpdpni
      121 pptfsafned yvgsgwsrgh mapagnnkfs skamaetfyl snivpqdfdn nsgywnriem
      181 ycrelterfe dvwvvsgplt lpqtrgdgkk ivsyqviged nvavpshlyk vilarrssvs
      241 teplalgafv vpneaigfqp qltefqvslq dleklsglvf fphldrtsdi rnicsvdtck
      301 lldfqeftly lstrkiegar svlrlekime nlknaeiepd dyfmsryekk leelkakeqs
      361 gtqirkps
//
LOCUS       NP_001137160            1054 aa            linear   PRI 27-APR-2025
DEFINITION  DIS3-like exonuclease 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001137160
VERSION     NP_001137160.1
DBSOURCE    REFSEQ: accession NM_001143688.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 1054)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   5  (residues 1 to 1054)
  AUTHORS   Marcon,E., Ni,Z., Pu,S., Turinsky,A.L., Trimble,S.S., Olsen,J.B.,
            Silverman-Gavrila,R., Silverman-Gavrila,L., Phanse,S., Guo,H.,
            Zhong,G., Guo,X., Young,P., Bailey,S., Roudeva,D., Zhao,D.,
            Hewel,J., Li,J., Graslund,S., Paduch,M., Kossiakoff,A.A.,
            Lupien,M., Emili,A., Wodak,S.J. and Greenblatt,J.
  TITLE     Human-chromatin-related protein interactions identify a demethylase
            complex required for chromosome segregation
  JOURNAL   Cell Rep 8 (1), 297-310 (2014)
   PUBMED   24981860
REFERENCE   6  (residues 1 to 1054)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1054)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 1054)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 1054)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 1054)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.129073.1,
                                           SRR1660807.228454.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319212.9/ ENSP00000321711.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..1054
                     /product="DIS3-like exonuclease 1 isoform 1"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=120657
     Region          11..188
                     /region_name="PIN_Rrp44-like"
                     /note="VapC-like PIN domain of yeast exosome subunit Rrp44
                     endoribonuclease and other eukaryotic homologs; cd09862"
                     /db_xref="CDD:350211"
     Site            order(22..26,28,30,88,92..93,100,104,118,121)
                     /site_type="other"
                     /note="exosome subunit interface [polypeptide binding]"
                     /db_xref="CDD:350211"
     Site            order(33,38,41,153)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:350211"
     Region          238..866
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Region          881..956
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     Site            989
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TF46.2)"
     CDS             1..1054
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_001143688.3:30..3194"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45286.1"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mlqkrekvll lrtfqgrtlr ivrehylrpc vpchsplcpq paacshdgkl lssdvthyvi
       61 pdwkvvqdyl eilefpelkg iifmqtacqa vqhqrgrrqy nklrnllkda rhdcilfane
      121 fqqccylpre rgesmekwqt rsiynaavwy yhhcqdrmpi vmvtedeeai qqygsetegv
      181 fvitfknyld nfwpdlkaah elcdsilqsr rerenesqes hgkeypehlp levleagiks
      241 gryiqgilnv nkhraqieaf vrlqgasskd sdlvsdilih gmkarnrsih gdvvvvellp
      301 knewkgrtva lcendcddka sgespsepmp tgrvvgilqk nwrdyvvtfp skeevqsqgk
      361 naqkilvtpw dyripkiris tqqaetlqdf rvvvridswe stsvypnghf vrvlgrigdl
      421 egeiatilve nsisvipfse aqmcempvnt pespwkvspe eeqkrkdlrk shlvfsidpk
      481 gcedvddtls vrtlnngnle lgvhiadvth fvapnsyidi eartrattyy ladrrydmlp
      541 svlsadlcsl lggvdryavs imweldkasy eikkvwygrt iirsayklfy eaaqelldgn
      601 lsvvddipef kdldeksrqa kleelvwaig kltdiarhvr akrdgcgale legvevcvql
      661 ddkknihdli pkqplevhet vaecmilanh wvakkiwesf phqallrqhp pphqeffsel
      721 recakakgff idtrsnktla dsldnandph dpivnrllrs matqamsnal yfstgscaee
      781 efhhyglald kythftspir rysdivvhrl lmaaiskdkk meikgnlfsn kdleelcrhi
      841 nnrnqaaqhs qkqstelfqc myfkdkdpat eercisdgvi ysirtngvll fiprfgikga
      901 aylknkdglv iscgpdscse wkpgslqrfq nkitstttdg esvtfhlfdh vtvrisiqas
      961 rchsdtirle iisnkpykip ntelihqssp llkselvkev tksveeaqla qevkvniiqe
     1021 eyqeyrqtkg rslytlleei rdlalldvsn nygi
//
LOCUS       NP_055878                921 aa            linear   PRI 27-APR-2025
DEFINITION  sodium/calcium exchanger 2 precursor [Homo sapiens].
ACCESSION   NP_055878 XP_375633
VERSION     NP_055878.1
DBSOURCE    REFSEQ: accession NM_015063.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Liu,H., Yu,J., Yang,L., He,P. and Li,Z.
  TITLE     NCX2 Regulates Intracellular Calcium Homeostasis and Translocation
            of HIF-1alpha into the Nucleus to Inhibit Glioma Invasion
  JOURNAL   Biochem Genet 61 (3), 979-994 (2023)
   PUBMED   36334237
  REMARK    GeneRIF: NCX2 Regulates Intracellular Calcium Homeostasis and
            Translocation of HIF-1alpha into the Nucleus to Inhibit Glioma
            Invasion.
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Xia,Z., Wang,C. and Zhang,H.
  TITLE     The downregulation of NCXs is positively correlated with the
            prognosis of stage II-IV colon cancer
  JOURNAL   World J Surg Oncol 19 (1), 177 (2021)
   PUBMED   34127021
  REMARK    GeneRIF: The downregulation of NCXs is positively correlated with
            the prognosis of stage II-IV colon cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 921)
  AUTHORS   Valsecchi,V., Anzilotti,S., Serani,A., Laudati,G., Brancaccio,P.,
            Guida,N., Cuomo,O., Pignataro,G. and Annunziato,L.
  TITLE     miR-206 Reduces the Severity of Motor Neuron Degeneration in the
            Facial Nuclei of the Brainstem in a Mouse Model of SMA
  JOURNAL   Mol Ther 28 (4), 1154-1166 (2020)
   PUBMED   32075715
  REMARK    GeneRIF: miR-206 Reduces the Severity of Motor Neuron Degeneration
            in the Facial Nuclei of the Brainstem in a Mouse Model of SMA.
REFERENCE   4  (residues 1 to 921)
  AUTHORS   Huai,C., Wei,Y., Li,M., Zhang,X., Wu,H., Qiu,X., Shen,L., Chen,L.,
            Zhou,W., Zhang,N., Zhu,G., Zhang,Y., Zhang,Z., He,L. and Qin,S.
  TITLE     Genome-Wide Analysis of DNA Methylation and Antituberculosis
            Drug-Induced Liver Injury in the Han Chinese Population
  JOURNAL   Clin Pharmacol Ther 106 (6), 1389-1397 (2019)
   PUBMED   31247120
  REMARK    GeneRIF: Methylation on SLC8A2 is associated with the development
            of anti-tuberculosis drug-induced liver injury.
REFERENCE   5  (residues 1 to 921)
  AUTHORS   Sweeney,M.D., Zhao,Z., Montagne,A., Nelson,A.R. and Zlokovic,B.V.
  TITLE     Blood-Brain Barrier: From Physiology to Disease and Back
  JOURNAL   Physiol Rev 99 (1), 21-78 (2019)
   PUBMED   30280653
  REMARK    Review article
REFERENCE   6  (residues 1 to 921)
  AUTHORS   Qu,M., Jiao,H., Zhao,J., Ren,Z.P., Smits,A., Kere,J. and Nister,M.
  TITLE     Molecular genetic and epigenetic analysis of NCX2/SLC8A2 at 19q13.3
            in human gliomas
  JOURNAL   Neuropathol Appl Neurobiol 36 (3), 198-210 (2010)
   PUBMED   20132488
  REMARK    GeneRIF: The aim of this study was to investigate if NCX2 might be
            a tumour suppressor gene involved in glioma. Results indicate that
            DNA methylation may play a key role in the transcriptional
            silencing of NCX2.
REFERENCE   7  (residues 1 to 921)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 921)
  AUTHORS   Pulina,M.V., Rizzuto,R., Brini,M. and Carafoli,E.
  TITLE     Inhibitory interaction of the plasma membrane Na+/Ca2+ exchangers
            with the 14-3-3 proteins
  JOURNAL   J Biol Chem 281 (28), 19645-19654 (2006)
   PUBMED   16679322
  REMARK    GeneRIF: plasma membrane Na+/Ca2+ exchangers have inhibitory
            interactions with the 14-3-3 proteins
REFERENCE   9  (residues 1 to 921)
  AUTHORS   Katanosaka,Y., Iwata,Y., Kobayashi,Y., Shibasaki,F., Wakabayashi,S.
            and Shigekawa,M.
  TITLE     Calcineurin inhibits Na+/Ca2+ exchange in phenylephrine-treated
            hypertrophic cardiomyocytes
  JOURNAL   J Biol Chem 280 (7), 5764-5772 (2005)
   PUBMED   15557343
REFERENCE   10 (residues 1 to 921)
  AUTHORS   Li,Z., Matsuoka,S., Hryshko,L.V., Nicoll,D.A., Bersohn,M.M.,
            Burke,E.P., Lifton,R.P. and Philipson,K.D.
  TITLE     Cloning of the NCX2 isoform of the plasma membrane Na(+)-Ca2+
            exchanger
  JOURNAL   J Biol Chem 269 (26), 17434-17439 (1994)
   PUBMED   8021246
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC401065.1, AB029010.1 and AC073548.5.
            
            On Jan 7, 2005 this sequence version replaced XP_375633.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic and transcript sequence to make the sequence consistent
            with the reference genome assembly. The extent of this transcript
            is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB029010.1, AK302552.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000236877.11/ ENSP00000236877.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..921
                     /product="sodium/calcium exchanger 2 precursor"
                     /note="Na+/Ca2+-exchanging protein Nac2; sodium/calcium
                     exchanger 2; Na(+)/Ca(2+)-exchange protein 2; solute
                     carrier family 8 (sodium/calcium exchanger), member 2;
                     solute carrier family 8 member 2"
                     /calculated_mol_wt=98492
     Region          1..921
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1894
     mat_peptide     21..921
                     /product="Sodium/calcium exchanger 2. /id=PRO_0000019382"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
                     /calculated_mol_wt=98492
     Region          22..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            69..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            131..152
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Region          135..175
                     /region_name="Alpha-1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            165..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            197..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            223..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Region          248..267
                     /region_name="Putative calmodulin-binding region.
                     /evidence=ECO:0000250|UniProtKB:P23685"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K596; propagated from
                     UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            721..740
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            748..770
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            773..791
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Region          790..826
                     /region_name="Alpha-2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            817
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            823..843
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            855..875
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     Site            893..909
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPR5.2)"
     CDS             1..921
                     /gene="SLC8A2"
                     /gene_synonym="NCX2"
                     /coded_by="NM_015063.3:122..2887"
                     /db_xref="CCDS:CCDS33065.1"
                     /db_xref="GeneID:6543"
                     /db_xref="HGNC:HGNC:11069"
                     /db_xref="MIM:601901"
ORIGIN      
        1 maplalvgvt lllaappcsg aatptpslpp ppandsdtst ggcqgsyrcq pgvllpvwep
       61 ddpslgdkaa ravvyfvamv ymflgvsiia drfmaaievi tskekeitit kangetsvgt
      121 vriwnetvsn ltlmalgssa peillsviev cghnfqagel gpgtivgsaa fnmfvviavc
      181 iyvipagesr kikhlrvffv taswsifayv wlylilavfs pgvvqvweal ltlvffpvcv
      241 vfawmadkrl lfykyvykry rtdprsgiii gaegdppksi eldgtfvgae apgelgglgp
      301 gpaearelda srreviqilk dlkqkhpdkd leqlvgiany yallhqqksr afyriqatrl
      361 mtgagnvlrr haadasrraa paegageded dgasriffep slyhclencg svllsvtcqg
      421 gegnstfyvd yrtedgsaka gsdyeysegt lvfkpgetqk elrigiiddd ifeedehffv
      481 rllnlrvgda qgmfepdggg rpkgrlvapl latvtilddd hagifsfqdr llhvsecmgt
      541 vdvrvvrssg argtvrlpyr tvdgtarggg vhyedacgel efgddetmkt lqvkivddee
      601 yekkdnffie lgqpqwlkrg isalllnqgd gdrkltaeee earriaemgk pvlgencrle
      661 viieesydfk ntvdklikkt nlalvigths wreqfleait vsagdeeeee dgsreerlps
      721 cfdyvmhflt vfwkvlfacv ppteychgwa cfgvsilvig lltaligdla shfgctvglk
      781 dsvnavvfva lgtsipdtfa skvaalqdqc adasignvtg snavnvflgl gvawsvaavy
      841 wavqgrpfev rtgtlafsvt lftvfafvgi avllyrrrph iggelggprg pklattalfl
      901 glwllyilfa sleaychirg f
//
LOCUS       NP_001349956             924 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM37 isoform 4 [Mus musculus].
ACCESSION   NP_001349956
VERSION     NP_001349956.1
DBSOURCE    REFSEQ: accession NM_001363027.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Ge,Y., Zhao,R., Li,B., Xiao,B., Zhou,L. and Zuo,S.
  TITLE     Aerobic glycolysis and tumor progression of hepatocellular
            carcinoma are mediated by ubiquitin of P53 K48-linked regulated by
            TRIM37
  JOURNAL   Exp Cell Res 421 (2), 113377 (2022)
   PUBMED   36252649
  REMARK    GeneRIF: Aerobic glycolysis and tumor progression of hepatocellular
            carcinoma are mediated by ubiquitin of P53 K48-linked regulated by
            TRIM37.
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Liu,J., Li,S., Fei,X., Nan,X., Shen,Y., Xiu,H., Cormier,S.A.,
            Lu,C., Guo,C., Wang,S., Cai,Z. and Wang,P.
  TITLE     Increased alveolar epithelial TRAF6 via autophagy-dependent TRIM37
            degradation mediates particulate matter-induced lung metastasis
  JOURNAL   Autophagy 18 (5), 971-989 (2022)
   PUBMED   34524943
  REMARK    GeneRIF: Increased alveolar epithelial TRAF6 via
            autophagy-dependent TRIM37 degradation mediates particulate
            matter-induced lung metastasis.
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Zhao,L., Hao,Y., Song,Z., Fan,Y. and Li,S.
  TITLE     TRIM37 negatively regulates inflammatory responses induced by virus
            infection via controlling TRAF6 ubiquitination
  JOURNAL   Biochem Biophys Res Commun 556, 87-92 (2021)
   PUBMED   33839419
  REMARK    GeneRIF: TRIM37 negatively regulates inflammatory responses induced
            by virus infection via controlling TRAF6 ubiquitination.
REFERENCE   4  (residues 1 to 924)
  AUTHORS   Han,C., Xia,X., Jiao,S., Li,G., Ran,Q. and Yao,S.
  TITLE     Tripartite motif containing protein 37 involves in thrombin
            stimulated BV-2 microglial cell apoptosis and interleukin 1beta
            release
  JOURNAL   Biochem Biophys Res Commun 516 (4), 1252-1257 (2019)
   PUBMED   31301768
  REMARK    GeneRIF: TRIM37 has a role in apoptosis and IL-1beta release in
            mouse BV-2 microglia that involves PPARgamma ubiquitination; it is
            increased in mononuclear leukocytes of intracerebral hemorrhage
            patients
REFERENCE   5  (residues 1 to 924)
  AUTHORS   Bhatnagar,S., Gazin,C., Chamberlain,L., Ou,J., Zhu,X., Tushir,J.S.,
            Virbasius,C.M., Lin,L., Zhu,L.J., Wajapeyee,N. and Green,M.R.
  TITLE     TRIM37 is a new histone H2A ubiquitin ligase and breast cancer
            oncoprotein
  JOURNAL   Nature 516 (7529), 116-120 (2014)
   PUBMED   25470042
REFERENCE   6  (residues 1 to 924)
  AUTHORS   Wajapeyee,N., Malonia,S.K., Palakurthy,R.K. and Green,M.R.
  TITLE     Oncogenic RAS directs silencing of tumor suppressor genes through
            ordered recruitment of transcriptional repressors
  JOURNAL   Genes Dev 27 (20), 2221-2226 (2013)
   PUBMED   24105743
REFERENCE   7  (residues 1 to 924)
  AUTHORS   Kallijarvi,J., Hamalainen,R.H., Karlberg,N., Sainio,K. and
            Lehesjoki,A.E.
  TITLE     Tissue expression of the mulibrey nanism-associated Trim37 protein
            in embryonic and adult mouse tissues
  JOURNAL   Histochem Cell Biol 126 (3), 325-334 (2006)
   PUBMED   16514549
  REMARK    GeneRIF: We here show that the mouse Trim37 gene presents several
            alternative splice variants, including a testis-specific transcript
            with an additional 3' exon.
REFERENCE   8  (residues 1 to 924)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Hara,Y., Nagase,T.,
            Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: I. The complete nucleotide sequences of 100 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 9 (5), 179-188 (2002)
   PUBMED   12465718
REFERENCE   9  (residues 1 to 924)
  AUTHORS   Lehesjoki,A.E., Reed,V.A., Mark Gardiner,R. and Greene,N.D.
  TITLE     Expression of MUL, a gene encoding a novel RBCC family ring-finger
            protein, in human and mouse embryogenesis
  JOURNAL   Mech Dev 108 (1-2), 221-225 (2001)
   PUBMED   11578880
REFERENCE   10 (residues 1 to 924)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL713917.6, BX000355.5 and
            AL596130.13.
            
            Summary: The protein encoded by this gene is part of the
            tripartite-motif containing family (TRIM), which is typified by the
            RING, B-box type 1, B-box type 2, and coiled-coil region domains.
            In mouse this protein is proposed to oligomerize through its coiled
            coil domain and has been reported to be expressed in neural
            crest-derived tissues as well as in tissues whose development is
            regulated by mesenchymal-epithelial interactions. In humans,
            mutations in this gene are associated with mulibrey
            (muscle-liver-brain-eye) nanism, an autosomal recessive disorder
            characterized by prenatal onset growth failure, cardiomyopathy and
            dysmorphic features. [provided by RefSeq, Jan 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.177568.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN00849380,
                                           SAMN00849381 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 51.93 cM"
     Protein         1..924
                     /product="E3 ubiquitin-protein ligase TRIM37 isoform 4"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase TRIM37; tripartite
                     motif-containing protein 37; TRAF encompassing factor 3;
                     RING-type E3 ubiquitin transferase TRIM37"
                     /calculated_mol_wt=103444
     Region          13..55
                     /region_name="mRING-HC-C4C4_TRIM37_C-VIII"
                     /note="Modified RING finger, HC subclass (C4C4-type),
                     found in tripartite motif-containing protein 37 (TRIM37)
                     and similar proteins; cd16619"
                     /db_xref="CDD:438281"
     Region          93..132
                     /region_name="Bbox2_TRIM37_C-VIII"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 37 (TRIM37) and similar proteins;
                     cd19779"
                     /db_xref="CDD:380837"
     Region          132..254
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Region          273..406
                     /region_name="MATH_TRIM37"
                     /note="Tripartite motif containing protein 37 (TRIM37)
                     family, MATH domain; TRIM37 is a peroxisomal protein and
                     is a member of the tripartite motif (TRIM) protein
                     subfamily, also known as the RING-B-box-coiled-coil (RBCC)
                     subfamily of zinc-finger proteins; cd03773"
                     /db_xref="CDD:239742"
     Site            322
                     /site_type="active"
                     /note="Mulibrey nanism-associated mutation residue
                     [active]"
                     /db_xref="CDD:239742"
     Site            order(328,372..374)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:239742"
     CDS             1..924
                     /gene="Trim37"
                     /gene_synonym="1110032A10Rik; 2810004E07Rik; MUL; TEF3"
                     /coded_by="NM_001363027.1:400..3174"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:68729"
                     /db_xref="MGI:MGI:2153072"
ORIGIN      
        1 mdeqsvesia evfrcficme klrdarlcph csklccfsci rrwlteqraq cphcraplql
       61 relvncrwae evtqqldtlq lcsltkheen ekdkcenhhe klsvfcwtck kcichqcalw
      121 ggmhgghtfk plaeiyeqhv tkvneevakl rrrlmelisl vqevernvea vrnakdervr
      181 eirnavemmi arldtqlknk litlmgqkts ltqetelles llqevehqlr scskselisk
      241 sseilmmfqq vhrkpmasfv ttpvppdfts elvpsydsat fvlenfstlr qradpvyspp
      301 lqvsglcwrl kvypdgngvv rgyylsvfle lsaglpetsk yeyrvemvhq scndptknii
      361 refasdfevg ecwgynrffr ldllanegyl nrqndtvilr fqvrsptffq kcrdqhwyit
      421 qleaaqtgyi qqinnlkerl tielsrtqks rdlsppdnhl spqnddspet rtkkagscsd
      481 mlleggptca svretkeded eeekiqnedy hhelsdgdld ldlvgedevn hldgssssas
      541 statsnteen dideetmsge ndveynsmel eegelmedaa aagppgsshs yvgassrmsr
      601 rthlcsaats slldidplil ihlldlkdrs smenlwglqp rpsasllqpt asysrkdkdq
      661 rkqqamwrvp sdlkmlkrlk tqmaevrcmk tdvkttlsdi kgssvastdm qtnlfcadqa
      721 alttcgpens grlqdlgmel lakssvagcy irnptnkkns pksaraiags lslrravdsg
      781 ensrskgdcq vlaegssgss qsgsrhsspr althgiigdl lpksedrqck aldsdavvva
      841 vfnglptvek rrkmvtlgtn akggrlegmq madleshsea gevqptlpeg asaapeedsh
      901 ssfpdgeqid penlhfnpde gggr
//
LOCUS       NP_079472                217 aa            linear   PRI 27-APR-2025
DEFINITION  grpE protein homolog 1, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_079472
VERSION     NP_079472.1
DBSOURCE    REFSEQ: accession NM_025196.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Manjunath,P., Stojkovic,G., Euro,L., Konovalova,S., Wanrooij,S.,
            Koski,K. and Tyynismaa,H.
  TITLE     Preferential binding of ADP-bound mitochondrial HSP70 to the
            nucleotide exchange factor GRPEL1 over GRPEL2
  JOURNAL   Protein Sci 33 (11), e5190 (2024)
   PUBMED   39445986
  REMARK    GeneRIF: Preferential binding of ADP-bound mitochondrial HSP70 to
            the nucleotide exchange factor GRPEL1 over GRPEL2.
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Chen,P., Wang,B., Mo,Q., Wu,P., Fang,Y., Tian,Y., Jin,X., Gao,Y.,
            Wu,Y., Cao,Y., Zhang,Y., Xi,L., Wang,S., Hu,J., Ma,D., Zhou,J.,
            Gao,Q. and Chen,G.
  TITLE     The LIV-1-GRPEL1 axis adjusts cell fate during anti-mitotic
            agent-damaged mitosis
  JOURNAL   EBioMedicine 49, 26-39 (2019)
   PUBMED   31636012
  REMARK    GeneRIF: These data demonstrate that LIV-1-GRPEL1 axis dually
            regulates mitotic exit as well as apoptosis by interacting with
            PP2A B55alpha and AIF.
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Borges,J.C., Fischer,H., Craievich,A.F., Hansen,L.D. and Ramos,C.H.
  TITLE     Free human mitochondrial GrpE is a symmetric dimer in solution
  JOURNAL   J Biol Chem 278 (37), 35337-35344 (2003)
   PUBMED   12840016
  REMARK    GeneRIF: The low resolution structure of human GrpE presented
            suggests that GrpE is a symmetric dimer when not bound to DnaK
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Choglay,A.A., Chapple,J.P., Blatch,G.L. and Cheetham,M.E.
  TITLE     Identification and characterization of a human mitochondrial
            homologue of the bacterial co-chaperone GrpE
  JOURNAL   Gene 267 (1), 125-134 (2001)
   PUBMED   11311562
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Bauer,M.F., Gempel,K., Reichert,A.S., Rappold,G.A., Lichtner,P.,
            Gerbitz,K.D., Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     Genetic and structural characterization of the human mitochondrial
            inner membrane translocase
  JOURNAL   J Mol Biol 289 (1), 69-82 (1999)
   PUBMED   10339406
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC024242.2, AF070525.1 and AC097382.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.54823.1,
                                           SRR1660803.222171.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000264954.5/
                                                  ENSP00000264954.4
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.1"
     Protein         1..217
                     /product="grpE protein homolog 1, mitochondrial precursor"
                     /note="GrpE-like protein cochaperone; grpE protein homolog
                     1, mitochondrial"
                     /calculated_mol_wt=21337
     transit_peptide 1..27
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9HAV7.2)"
                     /calculated_mol_wt=2961
     mat_peptide     28..217
                     /product="GrpE protein homolog 1, mitochondrial.
                     /id=PRO_0000013049"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAV7.2)"
                     /calculated_mol_wt=21337
     Region          29..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAV7.2)"
     Region          72..213
                     /region_name="GrpE"
                     /note="nucleotide exchange factor GrpE; cd00446"
                     /db_xref="CDD:271355"
     Region          72..122
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
     Site            order(74,77..78,81..82,84..85,88..90,92,95..96,99..100,
                     103..104,106..107,110..112,114..118,120..121,143..144,
                     146..148,151,157..158)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271355"
     Site            order(90,98,120,123,170,172..173,175..179,195,204,208,210,
                     213)
                     /site_type="other"
                     /note="Hsp70 (ATPase domain) interactions [polypeptide
                     binding]"
                     /db_xref="CDD:271355"
     Site            94
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LP6; propagated from
                     UniProtKB/Swiss-Prot (Q9HAV7.2)"
     Site            100
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LP6; propagated from
                     UniProtKB/Swiss-Prot (Q9HAV7.2)"
     Region          143..158
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
     Site            215
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9HAV7.2)"
     CDS             1..217
                     /gene="GRPEL1"
                     /gene_synonym="GrpE; HMGE; mt-GrpE#1"
                     /coded_by="NM_025196.4:33..686"
                     /db_xref="CCDS:CCDS3396.1"
                     /db_xref="GeneID:80273"
                     /db_xref="HGNC:HGNC:19696"
                     /db_xref="MIM:606173"
ORIGIN      
        1 maaqcvrlar rslpalalsl rpsprllcta tkqknsgqnl eedmgqseqk adppatektl
       61 leekvkleeq lketvekykr aladtenlrq rsqklveeak lygiqafckd llevadvlek
      121 atqcvpkeei kddnphlknl yeglvmtevq iqkvftkhgl lklnpvgakf dpyehealfh
      181 tpvegkepgt valvskvgyk lhgrtlrpal vgvvkea
//
LOCUS       NP_115702                504 aa            linear   PRI 27-APR-2025
DEFINITION  endosomal/lysosomal proton channel TMEM175 isoform 1 [Homo
            sapiens].
ACCESSION   NP_115702
VERSION     NP_115702.1
DBSOURCE    REFSEQ: accession NM_032326.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Zhang,J., Zeng,W., Han,Y., Lee,W.R., Liou,J. and Jiang,Y.
  TITLE     Lysosomal LAMP proteins regulate lysosomal pH by direct inhibition
            of the TMEM175 channel
  JOURNAL   Mol Cell 83 (14), 2524-2539 (2023)
   PUBMED   37390818
  REMARK    GeneRIF: Lysosomal LAMP proteins regulate lysosomal pH by direct
            inhibition of the TMEM175 channel.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Hu,M., Li,P., Wang,C., Feng,X., Geng,Q., Chen,W., Marthi,M.,
            Zhang,W., Gao,C., Reid,W., Swanson,J., Du,W., Hume,R.I. and Xu,H.
  TITLE     Parkinson's disease-risk protein TMEM175 is a proton-activated
            proton channel in lysosomes
  JOURNAL   Cell 185 (13), 2292-2308 (2022)
   PUBMED   35750034
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Zheng,W., Shen,C., Wang,L., Rawson,S., Xie,W.J., Nist-Lund,C.,
            Wu,J., Shen,Z., Xia,S., Holt,J.R., Wu,H. and Fu,T.M.
  TITLE     pH regulates potassium conductance and drives a constitutive proton
            current in human TMEM175
  JOURNAL   Sci Adv 8 (12), eabm1568 (2022)
   PUBMED   35333573
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Wie,J., Liu,Z., Song,H., Tropea,T.F., Yang,L., Wang,H., Liang,Y.,
            Cang,C., Aranda,K., Lohmann,J., Yang,J., Lu,B., Chen-Plotkin,A.S.,
            Luk,K.C. and Ren,D.
  TITLE     A growth-factor-activated lysosomal K+ channel regulates
            Parkinson's pathology
  JOURNAL   Nature 591 (7850), 431-437 (2021)
   PUBMED   33505021
  REMARK    GeneRIF: A growth-factor-activated lysosomal K(+) channel regulates
            Parkinson's pathology.
            Erratum:[Nature. 2021 Apr;592(7855):E10. doi:
            10.1038/s41586-021-03438-x. PMID: 33790472]
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Oh,S., Paknejad,N. and Hite,R.K.
  TITLE     Gating and selectivity mechanisms for the lysosomal K+ channel
            TMEM175
  JOURNAL   Elife 9, e53430 (2020)
   PUBMED   32228865
  REMARK    GeneRIF: Gating and selectivity mechanisms for the lysosomal K(+)
            channel TMEM175.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Nalls,M.A., Pankratz,N., Lill,C.M., Do,C.B., Hernandez,D.G.,
            Saad,M., DeStefano,A.L., Kara,E., Bras,J., Sharma,M., Schulte,C.,
            Keller,M.F., Arepalli,S., Letson,C., Edsall,C., Stefansson,H.,
            Liu,X., Pliner,H., Lee,J.H., Cheng,R., Ikram,M.A., Ioannidis,J.P.,
            Hadjigeorgiou,G.M., Bis,J.C., Martinez,M., Perlmutter,J.S.,
            Goate,A., Marder,K., Fiske,B., Sutherland,M., Xiromerisiou,G.,
            Myers,R.H., Clark,L.N., Stefansson,K., Hardy,J.A., Heutink,P.,
            Chen,H., Wood,N.W., Houlden,H., Payami,H., Brice,A., Scott,W.K.,
            Gasser,T., Bertram,L., Eriksson,N., Foroud,T. and Singleton,A.B.
  CONSRTM   International Parkinson's Disease Genomics Consortium (IPDGC);
            Parkinson's Study Group (PSG) Parkinson's Research: The Organized
            GENetics Initiative (PROGENI); 23andMe; GenePD; NeuroGenetics
            Research Consortium (NGRC); Hussman Institute of Human Genomics
            (HIHG); Ashkenazi Jewish Dataset Investigator; Cohorts for Health
            and Aging Research in Genetic Epidemiology (CHARGE); North American
            Brain Expression Consortium (NABEC); United Kingdom Brain
            Expression Consortium (UKBEC); Greek Parkinson's Disease
            Consortium; Alzheimer Genetic Analysis Group
  TITLE     Large-scale meta-analysis of genome-wide association data
            identifies six new risk loci for Parkinson's disease
  JOURNAL   Nat Genet 46 (9), 989-993 (2014)
   PUBMED   25064009
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Ng,M.C., Shriner,D., Chen,B.H., Li,J., Chen,W.M., Guo,X., Liu,J.,
            Bielinski,S.J., Yanek,L.R., Nalls,M.A., Comeau,M.E.,
            Rasmussen-Torvik,L.J., Jensen,R.A., Evans,D.S., Sun,Y.V., An,P.,
            Patel,S.R., Lu,Y., Long,J., Armstrong,L.L., Wagenknecht,L.,
            Yang,L., Snively,B.M., Palmer,N.D., Mudgal,P., Langefeld,C.D.,
            Keene,K.L., Freedman,B.I., Mychaleckyj,J.C., Nayak,U., Raffel,L.J.,
            Goodarzi,M.O., Chen,Y.D., Taylor,H.A. Jr., Correa,A., Sims,M.,
            Couper,D., Pankow,J.S., Boerwinkle,E., Adeyemo,A., Doumatey,A.,
            Chen,G., Mathias,R.A., Vaidya,D., Singleton,A.B., Zonderman,A.B.,
            Igo,R.P. Jr., Sedor,J.R., Kabagambe,E.K., Siscovick,D.S.,
            McKnight,B., Rice,K., Liu,Y., Hsueh,W.C., Zhao,W., Bielak,L.F.,
            Kraja,A., Province,M.A., Bottinger,E.P., Gottesman,O., Cai,Q.,
            Zheng,W., Blot,W.J., Lowe,W.L., Pacheco,J.A., Crawford,D.C.,
            Grundberg,E., Rich,S.S., Hayes,M.G., Shu,X.O., Loos,R.J.,
            Borecki,I.B., Peyser,P.A., Cummings,S.R., Psaty,B.M., Fornage,M.,
            Iyengar,S.K., Evans,M.K., Becker,D.M., Kao,W.H., Wilson,J.G.,
            Rotter,J.I., Sale,M.M., Liu,S., Rotimi,C.N. and Bowden,D.W.
  CONSRTM   FIND Consortium; eMERGE Consortium; DIAGRAM Consortium; MuTHER
            Consortium; MEta-analysis of type 2 DIabetes in African Americans
            Consortium
  TITLE     Meta-analysis of genome-wide association studies in African
            Americans provides insights into the genetic architecture of type 2
            diabetes
  JOURNAL   PLoS Genet 10 (8), e1004517 (2014)
   PUBMED   25102180
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Do,C.B., Tung,J.Y., Dorfman,E., Kiefer,A.K., Drabant,E.M.,
            Francke,U., Mountain,J.L., Goldman,S.M., Tanner,C.M.,
            Langston,J.W., Wojcicki,A. and Eriksson,N.
  TITLE     Web-based genome-wide association study identifies two novel loci
            and a substantial genetic component for Parkinson's disease
  JOURNAL   PLoS Genet 7 (6), e1002141 (2011)
   PUBMED   21738487
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Nalls,M.A., Plagnol,V., Hernandez,D.G., Sharma,M., Sheerin,U.M.,
            Saad,M., Simon-Sanchez,J., Schulte,C., Lesage,S.,
            Sveinbjornsdottir,S., Stefansson,K., Martinez,M., Hardy,J.,
            Heutink,P., Brice,A., Gasser,T., Singleton,A.B. and Wood,N.W.
  CONSRTM   International Parkinson Disease Genomics Consortium
  TITLE     Imputation of sequence variants for identification of genetic risks
            for Parkinson's disease: a meta-analysis of genome-wide association
            studies
  JOURNAL   Lancet 377 (9766), 641-649 (2011)
   PUBMED   21292315
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA168151.1, BC005158.2 and BC047738.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.23441.1,
                                           SRR3476690.921379.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264771.9/ ENSP00000264771.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..504
                     /product="endosomal/lysosomal proton channel TMEM175
                     isoform 1"
                     /note="endosomal/lysomomal potassium channel TMEM175;
                     endosomal/lysosomal potassium channel TMEM175;
                     endosomal/lysosomal proton channel TMEM175"
                     /calculated_mol_wt=55484
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            34..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Region          35..124
                     /region_name="TMEM175"
                     /note="Endosomal/lysosomal potassium channel TMEM175;
                     pfam06736"
                     /db_xref="CDD:429088"
     Region          35..41
                     /region_name="RxxxFSD motif 1.
                     /evidence=ECO:0000269|PubMed:26317472"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            46
                     /site_type="other"
                     /note="Hydrophobic filter residue 1-1.
                     /evidence=ECO:0000269|PubMed:28723891; propagated from
                     UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            50
                     /site_type="other"
                     /note="Hydrophobic filter residue 2-1.
                     /evidence=ECO:0000250|UniProtKB:K9UJK2; propagated from
                     UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            53
                     /site_type="other"
                     /note="Hydrophobic filter residue 3-1.
                     /evidence=ECO:0000250|UniProtKB:K9UJK2; propagated from
                     UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Region          58..63
                     /region_name="Short helix H1-1.
                     /evidence=ECO:0000250|UniProtKB:K9UJK2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Region          65..71
                     /region_name="Short helix H2-1.
                     /evidence=ECO:0000250|UniProtKB:K9UJK2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            78..100
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            107..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            139..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            211..230
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            258..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Region          260..356
                     /region_name="TMEM175"
                     /note="Endosomal/lysosomal potassium channel TMEM175;
                     pfam06736"
                     /db_xref="CDD:429088"
     Region          260..266
                     /region_name="RxxxFSD motif 2.
                     /evidence=ECO:0000305|PubMed:26317472"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            271
                     /site_type="other"
                     /note="Hydrophobic filter residue 1-2.
                     /evidence=ECO:0000269|PubMed:28723891; propagated from
                     UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            275
                     /site_type="other"
                     /note="Hydrophobic filter residue 2-2.
                     /evidence=ECO:0000250|UniProtKB:K9UJK2; propagated from
                     UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            278
                     /site_type="other"
                     /note="Hydrophobic filter residue 3-2.
                     /evidence=ECO:0000250|UniProtKB:K9UJK2; propagated from
                     UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Region          288..296
                     /region_name="Short helix H1-2.
                     /evidence=ECO:0000250|UniProtKB:K9UJK2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Region          298..304
                     /region_name="Short helix H2-2.
                     /evidence=ECO:0000250|UniProtKB:K9UJK2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            310..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            339..360
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            376..396
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            417..440
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Site            443..469
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     Region          483..504
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSA9.1)"
     CDS             1..504
                     /gene="TMEM175"
                     /gene_synonym="hTMEM175"
                     /coded_by="NM_032326.4:113..1627"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3341.1"
                     /db_xref="GeneID:84286"
                     /db_xref="HGNC:HGNC:28709"
                     /db_xref="MIM:616660"
ORIGIN      
        1 msqprtpeqa ldtpgdcppg rrdedagegi qcsqrmlsfs dallsiiatv milpvthtei
       61 speqqfdrsv qrllatriav ylmtflivtv awaahtrlfq vvgktddtla llnlacmmti
      121 tflpytfslm vtfpdvplgi flfcvcviai gvvqalivgy afhfphllsp qiqrsahral
      181 yrrhvlgivl qgpalcfaaa ifslffvpls yllmvtvill pyvskvtgwc rdrllghrep
      241 sahpvevfsf dlheplsker veafsdgvya ivatllildi cednvpdpkd vkerfsgslv
      301 aalsatgprf layfgsfatv gllwfahhsl flhvrkatra mgllntlsla fvgglplayq
      361 qtsafarqpr delervrvsc tiiflasifq lamwttallh qaetlqpsvw fggrehvlmf
      421 aklalypcas llafastcll srfsvgifhl mqiavpcafl llrllvglal atlrvlrgla
      481 rpehpppapt gqddpqsqll papc
//
LOCUS       NP_057571                240 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial transcription rescue factor 1 isoform a [Homo
            sapiens].
ACCESSION   NP_057571
VERSION     NP_057571.1
DBSOURCE    REFSEQ: accession NM_016487.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Desai,N., Yang,H., Chandrasekaran,V., Kazi,R., Minczuk,M. and
            Ramakrishnan,V.
  TITLE     Elongational stalling activates mitoribosome-associated quality
            control
  JOURNAL   Science 370 (6520), 1105-1110 (2020)
   PUBMED   33243891
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Gopalakrishna,S., Pearce,S.F., Dinan,A.M., Schober,F.A.,
            Cipullo,M., Spahr,H., Khawaja,A., Maffezzini,C., Freyer,C.,
            Wredenberg,A., Atanassov,I., Firth,A.E. and Rorbach,J.
  TITLE     C6orf203 is an RNA-binding protein involved in mitochondrial
            protein synthesis
  JOURNAL   Nucleic Acids Res 47 (17), 9386-9399 (2019)
   PUBMED   31396629
  REMARK    GeneRIF: Although mitoribosome stability is not affected in
            C6orf203-depleted cells, mitoribosome profiling analysis revealed a
            global disruption of the association of mt-mRNAs with the
            mitoribosome, suggesting that C6orf203 may be required for the
            proper maturation and functioning of the mitoribosome.
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Kotrys,A.V., Cysewski,D., Czarnomska,S.D., Pietras,Z.,
            Borowski,L.S., Dziembowski,A. and Szczesny,R.J.
  TITLE     Quantitative proteomics revealed C6orf203/MTRES1 as a factor
            preventing stress-induced transcription deficiency in human
            mitochondria
  JOURNAL   Nucleic Acids Res 47 (14), 7502-7517 (2019)
   PUBMED   31226201
  REMARK    GeneRIF: Data show that mitochondrial transcription rescue factor 1
            (MTRES1) is elevated in cells under stress and that this
            upregulation of MTRES1 prevents mitochondrial transcript loss under
            perturbed mitochondrial gene expression.
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   8  (residues 1 to 240)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 240)
  AUTHORS   Reymond,A., Friedli,M., Henrichsen,C.N., Chapot,F., Deutsch,S.,
            Ucla,C., Rossier,C., Lyle,R., Guipponi,M. and Antonarakis,S.E.
  TITLE     From PREDs and open reading frames to cDNA isolation: revisiting
            the human chromosome 21 transcription map
  JOURNAL   Genomics 78 (1-2), 46-54 (2001)
   PUBMED   11707072
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB499205.1, DA167160.1, AF151064.1, AI693246.1, AL355586.27 and
            CD673918.1.
            
            Transcript Variant: This variant (1) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 3. Variants 1 and 2
            encode the same isoform (a), which has a shorter N-terminus
            compared to isoform b.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.9177.1,
                                           SRR5189652.47709.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000311381.8/
                                                  ENSP00000310951.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..240
                     /product="mitochondrial transcription rescue factor 1
                     isoform a"
                     /note="uncharacterized protein C6orf203"
                     /calculated_mol_wt=18353
     transit_peptide 1..84
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:31226201; propagated from
                     UniProtKB/Swiss-Prot (Q9P0P8.1)"
                     /calculated_mol_wt=9607
     mat_peptide     85..240
                     /product="Mitochondrial transcription rescue factor 1.
                     /id=PRO_0000089559"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0P8.1)"
                     /calculated_mol_wt=18353
     Region          95..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0P8.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9P0P8.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9P0P8.1)"
     CDS             1..240
                     /gene="MTRES1"
                     /gene_synonym="C6orf203; HSPC230; PRED31"
                     /coded_by="NM_016487.5:86..808"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5058.1"
                     /db_xref="GeneID:51250"
                     /db_xref="HGNC:HGNC:17971"
                     /db_xref="MIM:618583"
ORIGIN      
        1 mamasvklla gvlrkpdawi glwgvlrgtp ssyklctswn rylyfsstkl rapnyktlfy
       61 nifslrlpgl llspecifpf svrlksnirs tkstkkslqk vdeedsdees hhdemseqee
      121 eleddptvvk nykdlekavq sfrydvvlkt gldigrnkve dafykgelrl neeklwkksr
      181 tvkvgdtldl ligedkeagt etvmrillkk vfeektesek yrvvlrrwks lklpkkrmsk
//
LOCUS       NP_001193583            2504 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear receptor corepressor 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001193583
VERSION     NP_001193583.1
DBSOURCE    REFSEQ: accession NM_001206654.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2504)
  AUTHORS   Patton,A., Ilaslan,H., Armstrong,S.M., Bakhshwin,A., Cheng,Y.W.,
            Minhas,F. and Fritchie,K.J.
  TITLE     Keratin-Positive Giant Cell-Rich Tumor of Bone Harboring an
            HMGA2::NCOR2 Fusion: Two Cases, Including a Patient With Metastatic
            Disease, and Review of the Literature
  JOURNAL   Int J Surg Pathol 32 (3), 556-564 (2024)
   PUBMED   37461232
  REMARK    GeneRIF: Keratin-Positive Giant Cell-Rich Tumor of Bone Harboring
            an HMGA2::NCOR2 Fusion: Two Cases, Including a Patient With
            Metastatic Disease, and Review of the Literature.
            Review article
REFERENCE   2  (residues 1 to 2504)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   3  (residues 1 to 2504)
  AUTHORS   Lee,R.D., Knutson,T.P., Munro,S.A., Miller,J.T.,
            Heltemes-Harris,L.M., Mullighan,C.G., Jepsen,K. and Farrar,M.A.
  TITLE     Nuclear corepressors NCOR1/NCOR2 regulate B cell development,
            maintain genomic integrity and prevent transformation
  JOURNAL   Nat Immunol 23 (12), 1763-1776 (2022)
   PUBMED   36316474
  REMARK    GeneRIF: Nuclear corepressors NCOR1/NCOR2 regulate B cell
            development, maintain genomic integrity and prevent transformation.
REFERENCE   4  (residues 1 to 2504)
  AUTHORS   Tsai,K.K., Huang,S.S., Northey,J.J., Liao,W.Y., Hsu,C.C.,
            Cheng,L.H., Werner,M.E., Chuu,C.P., Chatterjee,C., Lakins,J.N. and
            Weaver,V.M.
  TITLE     Screening of organoids derived from patients with breast cancer
            implicates the repressor NCOR2 in cytotoxic stress response and
            antitumor immunity
  JOURNAL   Nat Cancer 3 (6), 734-752 (2022)
   PUBMED   35618935
  REMARK    GeneRIF: Screening of organoids derived from patients with breast
            cancer implicates the repressor NCOR2 in cytotoxic stress response
            and antitumor immunity.
REFERENCE   5  (residues 1 to 2504)
  AUTHORS   Jiang,Q., Galiegue-Zouitina,S., Roumier,C., Hildebrand,M.P.,
            Thomas,S. and Coignet,L.J.
  TITLE     Genomic organization and refined mapping of the human nuclear
            corepressor 2 (NCOR2)/ silencing mediator of retinoid and thyroid
            hormone receptor (SMRT) gene on chromosome 12q24.3
  JOURNAL   Cytogenet Cell Genet 92 (3-4), 217-220 (2001)
   PUBMED   11435691
REFERENCE   6  (residues 1 to 2504)
  AUTHORS   Ordentlich,P., Downes,M., Xie,W., Genin,A., Spinner,N.B. and
            Evans,R.M.
  TITLE     Unique forms of human and mouse nuclear receptor corepressor SMRT
  JOURNAL   Proc Natl Acad Sci U S A 96 (6), 2639-2644 (1999)
   PUBMED   10077563
REFERENCE   7  (residues 1 to 2504)
  AUTHORS   Margolis,R.L., Abraham,M.R., Gatchell,S.B., Li,S.H., Kidwai,A.S.,
            Breschel,T.S., Stine,O.C., Callahan,C., McInnis,M.G. and Ross,C.A.
  TITLE     cDNAs with long CAG trinucleotide repeats from human brain
  JOURNAL   Hum Genet 100 (1), 114-122 (1997)
   PUBMED   9225980
REFERENCE   8  (residues 1 to 2504)
  AUTHORS   Sande,S. and Privalsky,M.L.
  TITLE     Identification of TRACs (T3 receptor-associating cofactors), a
            family of cofactors that associate with, and modulate the activity
            of, nuclear hormone receptors
  JOURNAL   Mol Endocrinol 10 (7), 813-825 (1996)
   PUBMED   8813722
REFERENCE   9  (residues 1 to 2504)
  AUTHORS   Chen,J.D. and Evans,R.M.
  TITLE     A transcriptional co-repressor that interacts with nuclear hormone
            receptors
  JOURNAL   Nature 377 (6548), 454-457 (1995)
   PUBMED   7566127
REFERENCE   10 (residues 1 to 2504)
  AUTHORS   Horlein,A.J., Naar,A.M., Heinzel,T., Torchia,J., Gloss,B.,
            Kurokawa,R., Ryan,A., Kamei,Y., Soderstrom,M., Glass,C.K. et al.
  TITLE     Ligand-independent repression by the thyroid hormone receptor
            mediated by a nuclear receptor co-repressor
  JOURNAL   Nature 377 (6548), 397-404 (1995)
   PUBMED   7566114
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073592.11, AC069261.37 and
            AC073916.41.
            
            Summary: This gene encodes a nuclear receptor co-repressor that
            mediates transcriptional silencing of certain target genes. The
            encoded protein is a member of a family of thyroid hormone- and
            retinoic acid receptor-associated co-repressors. This protein acts
            as part of a multisubunit complex which includes histone
            deacetylases to modify chromatin structure that prevents basal
            transcriptional activity of target genes. Aberrant expression of
            this gene is associated with certain cancers. Alternate splicing
            results in multiple transcript variants encoding different
            isoforms.[provided by RefSeq, Apr 2011].
            
            Transcript Variant: This variant (3) has multiple difference in the
            coding region, but maintains the reading frame, compared to variant
            1. The resulting isoform (3) has the same N- and C-termini but is
            shorter than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF125672.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..2504
                     /product="nuclear receptor corepressor 2 isoform 3"
                     /note="silencing mediator for retinoid and thyroid hormone
                     receptors; CTG repeat protein 26; T3 receptor-associating
                     factor; thyroid-, retinoic-acid-receptor-associated
                     corepressor"
                     /calculated_mol_wt=272693
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            18
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WU42; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          <100..457
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          120..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          141..229
                     /region_name="GPS2_interact"
                     /note="G-protein pathway suppressor 2-interacting domain;
                     pfam15784"
                     /db_xref="CDD:464868"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          190..220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          254..312
                     /region_name="Interaction with SIN3A/B.
                     /evidence=ECO:0000250|UniProtKB:Q60974"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          388..479
                     /region_name="Deacetylase activation domain (DAD).
                     /evidence=ECO:0000269|PubMed:22230954"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          431..474
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cl21498"
                     /db_xref="CDD:473887"
     Site            order(431,460..461,463..464,466..468,470..472)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          486..621
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          <540..>648
                     /region_name="RSC8"
                     /note="RSC chromatin remodeling complex subunit RSC8
                     [Chromatin structure and dynamics / Transcription];
                     COG5259"
                     /db_xref="CDD:227584"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          613..656
                     /region_name="Myb_DNA-binding"
                     /note="Myb-like DNA-binding domain; pfam00249"
                     /db_xref="CDD:459731"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          <740..1209
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            860
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            921
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            928
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            941
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          1155..1176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1200
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1230
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          1277..1297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1373
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          1430..1472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          1496..1599
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WU42; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1643
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          1753..1857
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1765
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1768
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1851
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          <1875..2252
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1927..2114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1949
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            1995
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2016
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2036
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2047
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2048
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2050
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WU42; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2052
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2067
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          2118..2121
                     /region_name="Required for interaction with RARA in the
                     absence of its ligand.
                     /evidence=ECO:0000269|PubMed:20543827"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          2126..2130
                     /region_name="CORNR box of ID1.
                     /evidence=ECO:0000250|UniProtKB:Q60974"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          2164..2225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          2238..2259
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          2329..2333
                     /region_name="CORNR box of ID2.
                     /evidence=ECO:0000250|UniProtKB:Q60974"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Region          2374..2490
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y618.3)"
     Site            2403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y618.3)"
     CDS             1..2504
                     /gene="NCOR2"
                     /gene_synonym="CTG26; N-CoR2; SMAP270; SMRT; SMRTE;
                     SMRTE-tau; TNRC14; TRAC; TRAC-1; TRAC1"
                     /coded_by="NM_001206654.2:470..7984"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55892.1"
                     /db_xref="GeneID:9612"
                     /db_xref="HGNC:HGNC:7673"
                     /db_xref="MIM:600848"
ORIGIN      
        1 msgstqpvaq twratepryp phslsypvqi arthtdvgll eyqhhsrdya shlspgsiiq
       61 pqrrrpslls efqpgnersq elhlrpeshs ylpelgksem efieskrprl ellpdpllrp
      121 spllatgqpa gsedltkdrs ltgklepvsp pspphtdpel elvpprlske eliqnmdrvd
      181 reitmveqqi sklkkkqqql eeeaakppep ekpvspppie skhrslvqii ydenrkkaea
      241 ahrileglgp qvelplynqp sdtrqyheni kinqamrkkl ilyfkrrnha rkqweqkfcq
      301 rydqlmeawe kkveriennp rrrakeskvr eyyekqfpei rkqrelqerm qrvgqrgsgl
      361 smsaarsehe vseiidglse qenlekqmrq lavippmlyd adqqrikfin mnglmadpmk
      421 vykdrqvmnm wseqeketfr ekfmqhpknf gliasflerk tvaecvlyyy ltkknenyks
      481 lvrrsyrrrg ksqqqqqqqq qqqqqqqqqp mprssqeekd ekekekeaek eeekpevend
      541 kedllkektd dtsgedndek eavaskgrkt ansqgrrkgr itrsmanean seeaitpqqs
      601 aelasmelne ssrwteeeme takkgllehg rnwsaiarmv gsktvsqckn fyfnykkrqn
      661 ldeilqqhkl kmekernarr kkkkapaaas eeaafppvve deemeasgvs gneeemveea
      721 eatvnnssdt esipsphtea akdtgqngpk ppatlgadgp ppgpptpppe dipapteptp
      781 aseatgaptp ppappspsap ppvvpkeeke eetaaappve egeeqkppaa eelavdtgka
      841 eepvksecte eaeegpakgk daeaaeatae galkaekkeg gsgrattaks sgapqdsdss
      901 atcsadevde aeggdknrll sprpslltpt gdpranaspq kpldlkqlkq raaaippiqv
      961 tkvheppred aaptkpappa ppppqnlqpe sdapqqpgss prgksrspap padkeaekpv
     1021 ffpafaaeaq klpgdppcwt sglpfpvppr evikasphap dpsafsyapp ghplplglhd
     1081 tarpvlprpp tisnppplis sakhpsvler qigaisqgms vqlhvpyseh akapvgpvtm
     1141 glplpmdpkk lapfsgvkqe qlsprgqagp peslgvptaq easvlrgtal gsvpggsitk
     1201 gipstrvpsd saityrgsit hgtpadvlyk gtitriiged spsrldrgre dslpkghviy
     1261 egkkghvlsy eggmsvtqcs kedgrsssgp phetaapkrt ydmmegrvgr aissasiegl
     1321 mgraipperh sphhlkeqhh irgsitqgip rsyveaqedy lrreakllkr egtpppppps
     1381 rdlteayktq algplklkpa heglvatvke agrsiheipr eelrhtpelp laprplkegs
     1441 itqgtplkyd tgasttgskk hdvrsligsp grtfppvhpl dvmadarale racyeeslks
     1501 rpgtasssgg siargapviv pelgkprqsp ltyedhgapf aghlprgspv ttreptprlq
     1561 egslssskas qdrkltstpr eiaksphstv pehhphpisp yehllrgvsg vdlyrshipl
     1621 afdptsiprg ipldaaaayy lprhlapnpt yphlyppyli rgypdtaale nrqtiindyi
     1681 tsqqmhhnaa tamaqradml rglspressl alnyaagprg iidlsqvphl pvlvpptpgt
     1741 patamdrlay lptapqpfss rhsssplspg gpthltkptt tsssererdr drerdrdrer
     1801 eksiltsttt vehapiwrpg teqssgssgg gggsssrpas hshahqhspi sprtqdalqq
     1861 rpsvlhntgm kgiitaveps tptvlrstst sspvrpaatf ppathcplgg tldgvyptlm
     1921 epvllpkeap rvarperpra dtghaflakp parsglepas spskgseprp lvppvsghat
     1981 iartpaknla phhaspdppa ppasasdphr ektqskpfsi qelelrslgy hgssyspegv
     2041 epvspvssps lthdkglpkh leeldkshle gelrpkqpgp vklggeaahl phlrplpesq
     2101 pssspllqta pgvkghqrvv tlaqhisevi tqdytrhhpq qlsaplpapl ysfpgascpv
     2161 ldlrrppsdl ylpppdhgap argsphsegg krspepnkts vlgggedgie pvsppegmte
     2221 pghsrsavyp llyrdgeqte psrmgskspg ntsqppaffs kltesnsamv kskkqeinkk
     2281 lnthnrnepe ynisqpgtei fnmpaitgtg lmtyrsqavq ehastnmgle aiirkalmgk
     2341 ydqweesppl sanafnplna saslpaampi taadgrsdht ltspggggka kvsgrpssrk
     2401 akspapglas gdrppsvssv hsegdcnrrt pltnrvwedr pssagstpfp ynplimrlqa
     2461 gvmasppppg lpagsgplag phhawdeepk pllcsqyetl sdse
//
LOCUS       NP_004292                429 aa            linear   PRI 27-APR-2025
DEFINITION  actin-like protein 6A isoform 1 [Homo sapiens].
ACCESSION   NP_004292
VERSION     NP_004292.1
DBSOURCE    REFSEQ: accession NM_004301.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Liu,Y., Liu,Y., Li,Y., Wang,T., Li,B., Kong,X. and Li,C.
  TITLE     High expression of ACTL6A leads to poor prognosis of oral squamous
            cell carcinoma patients through promoting malignant progression
  JOURNAL   Head Neck 46 (6), 1450-1467 (2024)
   PUBMED   38523407
  REMARK    GeneRIF: High expression of ACTL6A leads to poor prognosis of oral
            squamous cell carcinoma patients through promoting malignant
            progression.
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Liu,F., Liao,Z., Qin,L., Zhang,Z., Zhang,Q., Han,S., Zeng,W.,
            Zhang,H., Liu,Y., Song,J., Chen,W., Zhu,H., Liang,H., Chen,X.,
            Zhang,B. and Zhang,Z.
  TITLE     Targeting VPS72 inhibits ACTL6A/MYC axis activity in HCC
            progression
  JOURNAL   Hepatology 78 (5), 1384-1401 (2023)
   PUBMED   36631007
  REMARK    GeneRIF: Targeting VPS72 inhibits ACTL6A/MYC axis activity in HCC
            progression.
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Chen,P.M., Wong,C.N., Wong,C.N. and Chu,P.Y.
  TITLE     Actin-like Protein 6A Expression Correlates with Cancer Stem
            Cell-like Features and Poor Prognosis in Ovarian Cancer
  JOURNAL   Int J Mol Sci 24 (3), 2016 (2023)
   PUBMED   36768349
  REMARK    GeneRIF: Actin-like Protein 6A Expression Correlates with Cancer
            Stem Cell-like Features and Poor Prognosis in Ovarian Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Yang,Z., Huang,D., Meng,M., Wang,W., Feng,J., Fang,L., Chen,H. and
            Zou,S.
  TITLE     BAF53A drives colorectal cancer development by regulating
            DUSP5-mediated ERK phosphorylation
  JOURNAL   Cell Death Dis 13 (12), 1049 (2022)
   PUBMED   36526622
  REMARK    GeneRIF: BAF53A drives colorectal cancer development by regulating
            DUSP5-mediated ERK phosphorylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Zhao,K., Wang,W., Rando,O.J., Xue,Y., Swiderek,K., Kuo,A. and
            Crabtree,G.R.
  TITLE     Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF
            complex to chromatin after T lymphocyte receptor signaling
  JOURNAL   Cell 95 (5), 625-636 (1998)
   PUBMED   9845365
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Cho,H., Orphanides,G., Sun,X., Yang,X.J., Ogryzko,V., Lees,E.,
            Nakatani,Y. and Reinberg,D.
  TITLE     A human RNA polymerase II complex containing factors that modify
            chromatin structure
  JOURNAL   Mol Cell Biol 18 (9), 5355-5363 (1998)
   PUBMED   9710619
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Reyes,J.C., Muchardt,C. and Yaniv,M.
  TITLE     Components of the human SWI/SNF complex are enriched in active
            chromatin and are associated with the nuclear matrix
  JOURNAL   J Cell Biol 137 (2), 263-274 (1997)
   PUBMED   9128241
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Wang,W., Cote,J., Xue,Y., Zhou,S., Khavari,P.A., Biggar,S.R.,
            Muchardt,C., Kalpana,G.V., Goff,S.P., Yaniv,M., Workman,J.L. and
            Crabtree,G.R.
  TITLE     Purification and biochemical heterogeneity of the mammalian SWI-SNF
            complex
  JOURNAL   EMBO J 15 (19), 5370-5382 (1996)
   PUBMED   8895581
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB041143.1, BC036371.1 and
            AC090425.15.
            
            Summary: This gene encodes a family member of actin-related
            proteins (ARPs), which share significant amino acid sequence
            identity to conventional actins. Both actins and ARPs have an actin
            fold, which is an ATP-binding cleft, as a common feature. The ARPs
            are involved in diverse cellular processes, including vesicular
            transport, spindle orientation, nuclear migration and chromatin
            remodeling. This gene encodes a 53 kDa subunit protein of the BAF
            (BRG1/brm-associated factor) complex in mammals, which is
            functionally related to SWI/SNF complex in S. cerevisiae and
            Drosophila; the latter is thought to facilitate transcriptional
            activation of specific genes by antagonizing chromatin-mediated
            transcriptional repression. Together with beta-actin, it is
            required for maximal ATPase activity of BRG1, and for the
            association of the BAF complex with chromatin/matrix. Three
            transcript variants that encode two different protein isoforms have
            been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a), which is also referred to as hArpNbeta/Baf53. Isoform a is
            found mostly in the nucleus.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.157103.1,
                                           SRR5189661.114987.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000429709.7/ ENSP00000397552.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.33"
     Protein         1..429
                     /product="actin-like protein 6A isoform 1"
                     /note="hArpN beta; BAF53; INO80 complex subunit K;
                     actin-related protein 4; BAF complex 53 kDa subunit;
                     actin-like protein 6A; arpNbeta; BRG1-associated factor
                     53A; actin-related protein Baf53a; 53 kDa BRG1-associated
                     factor A"
                     /calculated_mol_wt=47330
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O96019.1)"
     Region          8..420
                     /region_name="ASKHA_NBD_Arp4_ACTL6-like"
                     /note="nucleotide-binding domain (NBD) of the
                     actin-related protein 4 (Arp4)-like subfamily; cd13395"
                     /db_xref="CDD:466846"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O96019.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O96019.1)"
     CDS             1..429
                     /gene="ACTL6A"
                     /gene_synonym="ACTL6; Arp4; ARPN-BETA; BAF53A; INO80K;
                     SMARCN1"
                     /coded_by="NM_004301.5:168..1457"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3231.1"
                     /db_xref="GeneID:86"
                     /db_xref="HGNC:HGNC:24124"
                     /db_xref="MIM:604958"
ORIGIN      
        1 msggvyggde vgalvfdigs ytvragyage dcpkvdfpta igmvverddg stlmeidgdk
       61 gkqggptyyi dtnalrvpre nmeaisplkn gmvedwdsfq aildhtykmh vkseaslhpv
      121 lmseapwntr akrekltelm fehynipaff lcktavltaf angrstglil dsgathttai
      181 pvhdgyvlqq givksplagd fitmqcrelf qemnielvpp ymiaskeavr egspanwkrk
      241 eklpqvtrsw hnymcncviq dfqasvlqvs dstydeqvaa qmptvhyefp ngyncdfgae
      301 rlkipeglfd psnvkglsgn tmlgvshvvt tsvgmcdidi rpglygsviv aggntliqsf
      361 tdrlnrelsq ktppsmrlkl iannttverr fsswiggsil aslgtfqqmw iskqeyeegg
      421 kqcverkcp
//
LOCUS       NP_001356673             200 aa            linear   PRI 27-APR-2025
DEFINITION  integrin beta-1-binding protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001356673 XP_005246240
VERSION     NP_001356673.1
DBSOURCE    REFSEQ: accession NM_001369744.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Su,V.L., Simon,B., Draheim,K.M. and Calderwood,D.A.
  TITLE     Serine phosphorylation of the small phosphoprotein ICAP1 inhibits
            its nuclear accumulation
  JOURNAL   J Biol Chem 295 (10), 3269-3284 (2020)
   PUBMED   32005669
  REMARK    GeneRIF: Serine phosphorylation of the small phosphoprotein ICAP1
            inhibits its nuclear accumulation.
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Bouin,A.P., Kyumurkov,A., Regent-Kloeckner,M., Ribba,A.S.,
            Faurobert,E., Fournier,H.N., Bourrin-Reynard,I., Manet-Dupe,S.,
            Oddou,C., Balland,M., Planus,E. and Albiges-Rizo,C.
  TITLE     ICAP-1 monoubiquitylation coordinates matrix density and rigidity
            sensing for cell migration through ROCK2-MRCKalpha balance
  JOURNAL   J Cell Sci 130 (3), 626-636 (2017)
   PUBMED   28049720
  REMARK    GeneRIF: ICAP-1 monoubiquitylation helps in switching from
            ROCK2-mediated to MRCKalpha-mediated cell contractility.
            Erratum:[J Cell Sci. 2017 Mar 15;130(6):1195. doi:
            10.1242/jcs.202218. PMID: 28298614]
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Chang,D.D., Hoang,B.Q., Liu,J. and Springer,T.A.
  TITLE     Molecular basis for interaction between Icap1 alpha PTB domain and
            beta 1 integrin
  JOURNAL   J Biol Chem 277 (10), 8140-8145 (2002)
   PUBMED   11741908
  REMARK    GeneRIF: Site-directed mutagenesis showed that Leu(135), Ile(138),
            and Ile(139) of Icap1 alpha, and Leu(82) and Tyr(144), are required
            for the Icap1 alpha-beta(1) integrin interaction
REFERENCE   7  (residues 1 to 200)
  AUTHORS   Zhang,J., Clatterbuck,R.E., Rigamonti,D., Chang,D.D. and Dietz,H.C.
  TITLE     Interaction between krit1 and icap1alpha infers perturbation of
            integrin beta1-mediated angiogenesis in the pathogenesis of
            cerebral cavernous malformation
  JOURNAL   Hum Mol Genet 10 (25), 2953-2960 (2001)
   PUBMED   11741838
REFERENCE   8  (residues 1 to 200)
  AUTHORS   Gotthardt,M., Trommsdorff,M., Nevitt,M.F., Shelton,J.,
            Richardson,J.A., Stockinger,W., Nimpf,J. and Herz,J.
  TITLE     Interactions of the low density lipoprotein receptor gene family
            with cytosolic adaptor and scaffold proteins suggest diverse
            biological functions in cellular communication and signal
            transduction
  JOURNAL   J Biol Chem 275 (33), 25616-25624 (2000)
   PUBMED   10827173
REFERENCE   9  (residues 1 to 200)
  AUTHORS   Bouvard,D. and Block,M.R.
  TITLE     Calcium/calmodulin-dependent protein kinase II controls integrin
            alpha5beta1-mediated cell adhesion through the integrin cytoplasmic
            domain associated protein-1alpha
  JOURNAL   Biochem Biophys Res Commun 252 (1), 46-50 (1998)
   PUBMED   9813144
REFERENCE   10 (residues 1 to 200)
  AUTHORS   Chang,D.D., Wong,C., Smith,H. and Liu,J.
  TITLE     ICAP-1, a novel beta1 integrin cytoplasmic domain-associated
            protein, binds to a conserved and functionally important NPXY
            sequence motif of beta1 integrin
  JOURNAL   J Cell Biol 138 (5), 1149-1157 (1997)
   PUBMED   9281591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC080162.7.
            
            On Apr 17, 2019 this sequence version replaced XP_005246240.1.
            
            Summary: The cytoplasmic domains of integrins are essential for
            cell adhesion. The protein encoded by this gene binds to the beta1
            integrin cytoplasmic domain. The interaction between this protein
            and beta1 integrin is highly specific. Two isoforms of this protein
            are derived from alternatively spliced transcripts. The shorter
            form of this protein does not interact with the beta1 integrin
            cytoplasmic domain. The longer form is a phosphoprotein and the
            extent of its phosphorylation is regulated by the cell-matrix
            interaction, suggesting an important role of this protein during
            integrin-dependent cell adhesion. Several transcript variants, some
            protein-coding and some non-protein coding, have been found for
            this gene. [provided by RefSeq, Jan 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.283900.1,
                                           SRR1803616.177765.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..200
                     /product="integrin beta-1-binding protein 1 isoform 1"
                     /note="integrin cytoplasmic domain-associated protein
                     1-beta; integrin cytoplasmic domain-associated protein
                     1-alpha; bodenin; integrin beta-1-binding protein 1"
                     /calculated_mol_wt=21651
     Region          1..200
                     /region_name="ICAP-1_inte_bdg"
                     /note="Beta-1 integrin binding protein; pfam10480"
                     /db_xref="CDD:119000"
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14713.1)"
     Region          6..7
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (O14713.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CaMK2.
                     /evidence=ECO:0000269|PubMed:9813144; propagated from
                     UniProtKB/Swiss-Prot (O14713.1)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35671; propagated from
                     UniProtKB/Swiss-Prot (O14713.1)"
     Site            order(66,153,173)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269985"
     Region          136..139
                     /region_name="Interaction with KRIT1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14713.1)"
     Site            order(139..144,160,184,188)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269985"
     Region          139..141
                     /region_name="Interaction with ITGB1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14713.1)"
     CDS             1..200
                     /gene="ITGB1BP1"
                     /gene_synonym="ICAP-1A; ICAP-1alpha; ICAP-1B; ICAP1;
                     ICAP1A; ICAP1B"
                     /coded_by="NM_001369744.1:329..931"
                     /note="isoform 1 is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS1662.1"
                     /db_xref="GeneID:9270"
                     /db_xref="HGNC:HGNC:23927"
                     /db_xref="MIM:607153"
ORIGIN      
        1 mfrkgkkrhs ssssqsseis tksksvdssl gglsrsstva sldtdstkss gqsnnnsdtc
       61 aefrikyvga ieklklsegk glegpldlin yidvaqqdgk lpfvppeeef imgvskygik
      121 vstsdqydvl hrhalyliir mvcyddglga gksllalktt dasneeyslw vyqcnsleqa
      181 qaickvlsta fdsvltsekp
//
LOCUS       NP_006814                 76 aa            linear   PRI 27-APR-2025
DEFINITION  cAMP-dependent protein kinase inhibitor alpha [Homo sapiens].
ACCESSION   NP_006814
VERSION     NP_006814.1
DBSOURCE    REFSEQ: accession NM_006823.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Xu,B., Zhang,J., Chen,W. and Cai,W.
  TITLE     Exploring the methylation status of CFTR and PKIA genes as
            potential biomarkers for lung adenocarcinoma
  JOURNAL   Orphanet J Rare Dis 18 (1), 246 (2023)
   PUBMED   37644544
  REMARK    GeneRIF: Exploring the methylation status of CFTR and PKIA genes as
            potential biomarkers for lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Fung,H.Y., Fu,S.C., Brautigam,C.A. and Chook,Y.M.
  TITLE     Structural determinants of nuclear export signal orientation in
            binding to exportin CRM1
  JOURNAL   Elife 4, e10034 (2015)
   PUBMED   26349033
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Estrada,K., Styrkarsdottir,U., Evangelou,E., Hsu,Y.H., Duncan,E.L.,
            Ntzani,E.E., Oei,L., Albagha,O.M., Amin,N., Kemp,J.P., Koller,D.L.,
            Li,G., Liu,C.T., Minster,R.L., Moayyeri,A., Vandenput,L.,
            Willner,D., Xiao,S.M., Yerges-Armstrong,L.M., Zheng,H.F.,
            Alonso,N., Eriksson,J., Kammerer,C.M., Kaptoge,S.K., Leo,P.J.,
            Thorleifsson,G., Wilson,S.G., Wilson,J.F., Aalto,V., Alen,M.,
            Aragaki,A.K., Aspelund,T., Center,J.R., Dailiana,Z., Duggan,D.J.,
            Garcia,M., Garcia-Giralt,N., Giroux,S., Hallmans,G., Hocking,L.J.,
            Husted,L.B., Jameson,K.A., Khusainova,R., Kim,G.S., Kooperberg,C.,
            Koromila,T., Kruk,M., Laaksonen,M., Lacroix,A.Z., Lee,S.H.,
            Leung,P.C., Lewis,J.R., Masi,L., Mencej-Bedrac,S., Nguyen,T.V.,
            Nogues,X., Patel,M.S., Prezelj,J., Rose,L.M., Scollen,S.,
            Siggeirsdottir,K., Smith,A.V., Svensson,O., Trompet,S., Trummer,O.,
            van Schoor,N.M., Woo,J., Zhu,K., Balcells,S., Brandi,M.L.,
            Buckley,B.M., Cheng,S., Christiansen,C., Cooper,C., Dedoussis,G.,
            Ford,I., Frost,M., Goltzman,D., Gonzalez-Macias,J., Kahonen,M.,
            Karlsson,M., Khusnutdinova,E., Koh,J.M., Kollia,P., Langdahl,B.L.,
            Leslie,W.D., Lips,P., Ljunggren,O., Lorenc,R.S., Marc,J.,
            Mellstrom,D., Obermayer-Pietsch,B., Olmos,J.M.,
            Pettersson-Kymmer,U., Reid,D.M., Riancho,J.A., Ridker,P.M.,
            Rousseau,F., Slagboom,P.E., Tang,N.L., Urreizti,R., Van Hul,W.,
            Viikari,J., Zarrabeitia,M.T., Aulchenko,Y.S.,
            Castano-Betancourt,M., Grundberg,E., Herrera,L., Ingvarsson,T.,
            Johannsdottir,H., Kwan,T., Li,R., Luben,R., Medina-Gomez,C.,
            Palsson,S.T., Reppe,S., Rotter,J.I., Sigurdsson,G., van Meurs,J.B.,
            Verlaan,D., Williams,F.M., Wood,A.R., Zhou,Y., Gautvik,K.M.,
            Pastinen,T., Raychaudhuri,S., Cauley,J.A., Chasman,D.I.,
            Clark,G.R., Cummings,S.R., Danoy,P., Dennison,E.M., Eastell,R.,
            Eisman,J.A., Gudnason,V., Hofman,A., Jackson,R.D., Jones,G.,
            Jukema,J.W., Khaw,K.T., Lehtimaki,T., Liu,Y., Lorentzon,M.,
            McCloskey,E., Mitchell,B.D., Nandakumar,K., Nicholson,G.C.,
            Oostra,B.A., Peacock,M., Pols,H.A., Prince,R.L., Raitakari,O.,
            Reid,I.R., Robbins,J., Sambrook,P.N., Sham,P.C., Shuldiner,A.R.,
            Tylavsky,F.A., van Duijn,C.M., Wareham,N.J., Cupples,L.A.,
            Econs,M.J., Evans,D.M., Harris,T.B., Kung,A.W., Psaty,B.M.,
            Reeve,J., Spector,T.D., Streeten,E.A., Zillikens,M.C.,
            Thorsteinsdottir,U., Ohlsson,C., Karasik,D., Richards,J.B.,
            Brown,M.A., Stefansson,K., Uitterlinden,A.G., Ralston,S.H.,
            Ioannidis,J.P., Kiel,D.P. and Rivadeneira,F.
  TITLE     Genome-wide meta-analysis identifies 56 bone mineral density loci
            and reveals 14 loci associated with risk of fracture
  JOURNAL   Nat Genet 44 (5), 491-501 (2012)
   PUBMED   22504420
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Tao,S., Wang,Z., Feng,J., Hsu,F.C., Jin,G., Kim,S.T., Zhang,Z.,
            Gronberg,H., Zheng,L.S., Isaacs,W.B., Xu,J. and Sun,J.
  TITLE     A genome-wide search for loci interacting with known prostate
            cancer risk-associated genetic variants
  JOURNAL   Carcinogenesis 33 (3), 598-603 (2012)
   PUBMED   22219177
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Olsen,S.R. and Uhler,M.D.
  TITLE     Inhibition of protein kinase-A by overexpression of the cloned
            human protein kinase inhibitor
  JOURNAL   Mol Endocrinol 5 (9), 1246-1256 (1991)
   PUBMED   1770951
REFERENCE   7  (residues 1 to 76)
  AUTHORS   Knighton,D.R., Zheng,J.H., Ten Eyck,L.F., Xuong,N.H., Taylor,S.S.
            and Sowadski,J.M.
  TITLE     Structure of a peptide inhibitor bound to the catalytic subunit of
            cyclic adenosine monophosphate-dependent protein kinase
  JOURNAL   Science 253 (5018), 414-420 (1991)
   PUBMED   1862343
REFERENCE   8  (residues 1 to 76)
  AUTHORS   Olsen,S.R. and Uhler,M.D.
  TITLE     Isolation and characterization of cDNA clones for an inhibitor
            protein of cAMP-dependent protein kinase
  JOURNAL   J Biol Chem 266 (17), 11158-11162 (1991)
   PUBMED   1710219
REFERENCE   9  (residues 1 to 76)
  AUTHORS   Van Patten,S.M., Heisermann,G.J., Cheng,H.C. and Walsh,D.A.
  TITLE     Tyrosine kinase catalyzed phosphorylation and inactivation of the
            inhibitor protein of the cAMP-dependent protein kinase
  JOURNAL   J Biol Chem 262 (7), 3398-3403 (1987)
   PUBMED   2434500
REFERENCE   10 (residues 1 to 76)
  AUTHORS   Scott,J.D., Fischer,E.H., Demaille,J.G. and Krebs,E.G.
  TITLE     Identification of an inhibitory region of the heat-stable protein
            inhibitor of the cAMP-dependent protein kinase
  JOURNAL   Proc Natl Acad Sci U S A 82 (13), 4379-4383 (1985)
   PUBMED   2989819
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI597731.1, BC022265.2,
            DR763580.1, BX419914.2 and CR744438.1.
            
            Summary: The protein encoded by this gene is a member of the
            cAMP-dependent protein kinase (PKA) inhibitor family. This protein
            was demonstrated to interact with and inhibit the activities of
            both C alpha and C beta catalytic subunits of the PKA.
            Alternatively spliced transcript variants encoding the same protein
            have been reported. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) differs the in the 5' UTR, as
            compared to variant 2. Both variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.274429.1,
                                           SRR1803616.154936.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396418.7/ ENSP00000379696.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.13"
     Protein         1..76
                     /product="cAMP-dependent protein kinase inhibitor alpha"
                     /note="PKI-alpha; protein kinase (cAMP-dependent,
                     catalytic) inhibitor alpha"
                     /calculated_mol_wt=7857
     Region          2..70
                     /region_name="PKI"
                     /note="cAMP-dependent protein kinase inhibitor; pfam02827"
                     /db_xref="CDD:460716"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P61925.2)"
     Site            16
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P61925.2)"
     Site            19
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P61925.2)"
     Site            20
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P61925.2)"
     Region          49..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61925.2)"
     CDS             1..76
                     /gene="PKIA"
                     /gene_synonym="PRKACN1"
                     /coded_by="NM_006823.4:286..516"
                     /db_xref="CCDS:CCDS6222.1"
                     /db_xref="GeneID:5569"
                     /db_xref="HGNC:HGNC:9017"
                     /db_xref="MIM:606059"
ORIGIN      
        1 mtdvettyad fiasgrtgrr naihdilvss asgnsnelal klagldinkt egeedaqrss
       61 teqsgeaqge aakses
//
LOCUS       NP_001357556             215 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 267 [Mus musculus].
ACCESSION   NP_001357556
VERSION     NP_001357556.1
DBSOURCE    REFSEQ: accession NM_001370627.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Cajigas,I., Chakraborty,A., Swyter,K.R., Luo,H., Bastidas,M.,
            Nigro,M., Morris,E.R., Chen,S., VanGompel,M.J.W., Leib,D.,
            Kohtz,S.J., Martina,M., Koh,S., Ay,F. and Kohtz,J.D.
  TITLE     The Evf2 Ultraconserved Enhancer lncRNA Functionally and Spatially
            Organizes Megabase Distant Genes in the Developing Forebrain
  JOURNAL   Mol Cell 71 (6), 956-972 (2018)
   PUBMED   30146317
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC163689.3 and AC241593.3.
            
            Transcript Variant: This variant (4) represents the longest
            transcript. All four variants encode the same protein.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN00849375, SAMN00849381
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 67.25 cM"
     Protein         1..215
                     /product="transmembrane protein 267"
                     /note="transmembrane protein C5orf28 homolog"
                     /calculated_mol_wt=24021
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDR5.1)"
     Site            114..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDR5.1)"
     Site            178..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDR5.1)"
     CDS             1..215
                     /gene="Tmem267"
                     /gene_synonym="EG633640; Gm7120"
                     /coded_by="NM_001370627.1:697..1344"
                     /db_xref="GeneID:633640"
                     /db_xref="MGI:MGI:3648543"
ORIGIN      
        1 maskvektha lppccstesl issiglgifc lvadrllrfp iiqhndwlra isdnivhgvi
       61 gmwswavvtg irkksdfgev llagflasvi dvdhffqars lslqaaltlp rrpflhcstv
      121 ipiavlsvkl avhlfklrds wrflpwmilv swtshhirdg irhglwicpf gktpplpssf
      181 yvistlslph lcsflmyltg trqtvsskyg mridv
//
LOCUS       NP_006617                424 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 6 [Homo sapiens].
ACCESSION   NP_006617
VERSION     NP_006617.1
DBSOURCE    REFSEQ: accession NM_006626.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Bardwell,V.J. and Treisman,R.
  TITLE     The POZ domain: a conserved protein-protein interaction motif
  JOURNAL   Genes Dev 8 (14), 1664-1677 (1994)
   PUBMED   7958847
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU600946.1, BX641237.1, BC037282.2 and BX390688.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037282.2, SRR1660809.155653.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373659.4/ ENSP00000362763.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.2"
     Protein         1..424
                     /product="zinc finger and BTB domain-containing protein 6"
                     /note="zinc finger protein with interaction domain; zinc
                     finger protein 482"
                     /calculated_mol_wt=48105
     Region          8..123
                     /region_name="BTB_POZ_ZBTB6"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 6 (ZBTB6); cd18197"
                     /db_xref="CDD:349506"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15916.1)"
     Region          303..323
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..348
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(333,335,337,339..340,343..344,347,361,363,367..368,
                     371..372,375,389,391,393,395..396,399..400)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          340..364
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          356..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          384..401
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          402..424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15916.1)"
     CDS             1..424
                     /gene="ZBTB6"
                     /gene_synonym="ZID; ZNF482"
                     /coded_by="NM_006626.6:83..1357"
                     /db_xref="CCDS:CCDS6846.1"
                     /db_xref="GeneID:10773"
                     /db_xref="HGNC:HGNC:16764"
                     /db_xref="MIM:605976"
ORIGIN      
        1 maaesdvlhf qfeqqgdvvl qkmnllrqqn lfcdvsiyin dtefqghkvi laacstfmrd
       61 qflltqskhv ritilqsaev grklllscyt galevkrkel lkyltaasyl qmvhivekct
      121 ealskyleid lsmknnnqht dlcqssdpdv knedensdkd ceiieiseds pvnidfhvke
      181 eesnalqstv esltserkem kspelstvdi gfkdneicil hvesistagv engqfsqpct
      241 sskasmyfse tqhslinstv esrvaevpgn qdqglfcent egsygtvsei qnleegyslr
      301 hqcprcprgf lhvenylrhl kmhklflclq cgktftqkkn lnrhirghmg irpfqctvcl
      361 ktftakstlq dhlnihsgdr pykchccdmd fkhksalkkh ltsvhgrssg eklsrpdlkr
      421 qsll
//
LOCUS       NP_001351199             408 aa            linear   ROD 27-APR-2025
DEFINITION  actin-histidine N-methyltransferase isoform 6 [Mus musculus].
ACCESSION   NP_001351199 XP_006516146
VERSION     NP_001351199.1
DBSOURCE    REFSEQ: accession NM_001364270.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Alganatay,C., Balbasi,E., Tuncbag,N., Sezginmert,D. and Terzi
            Cizmecioglu,N.
  TITLE     SETD3 regulates endoderm differentiation of mouse embryonic stem
            cells through canonical Wnt signaling pathway
  JOURNAL   FASEB J 38 (4), e23463 (2024)
   PUBMED   38334393
  REMARK    GeneRIF: SETD3 regulates endoderm differentiation of mouse
            embryonic stem cells through canonical Wnt signaling pathway.
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Hoye,M.L., Calviello,L., Poff,A.J., Ejimogu,N.E., Newman,C.R.,
            Montgomery,M.D., Ou,J., Floor,S.N. and Silver,D.L.
  TITLE     Aberrant cortical development is driven by impaired cell cycle and
            translational control in a DDX3X syndrome model
  JOURNAL   Elife 11, e78203 (2022)
   PUBMED   35762573
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Diep,J., Ooi,Y.S., Wilkinson,A.W., Peters,C.E., Foy,E.,
            Johnson,J.R., Zengel,J., Ding,S., Weng,K.F., Laufman,O., Jang,G.,
            Xu,J., Young,T., Verschueren,E., Kobluk,K.J., Elias,J.E.,
            Sarnow,P., Greenberg,H.B., Huttenhain,R., Nagamine,C.M., Andino,R.,
            Krogan,N.J., Gozani,O. and Carette,J.E.
  TITLE     Enterovirus pathogenesis requires the host methyltransferase SETD3
  JOURNAL   Nat Microbiol 4 (12), 2523-2537 (2019)
   PUBMED   31527793
  REMARK    GeneRIF: Enterovirus pathogenesis requires the host
            methyltransferase SETD3. SETD3 is essential for in vivo replication
            and pathogenesis in multiple mouse models for EV infection,
            including CV-A10, EV-A71 and EV-D68.
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Xu,L., Wang,P., Feng,X., Tang,J., Li,L., Zheng,X., Zhang,J., Hu,Y.,
            Lan,T., Yuan,K., Zhang,Y., Ren,S., Hao,X., Zhang,M. and Xu,M.
  TITLE     SETD3 is regulated by a couple of microRNAs and plays opposing
            roles in proliferation and metastasis of hepatocellular carcinoma
  JOURNAL   Clin Sci (Lond) 133 (20), 2085-2105 (2019)
   PUBMED   31654063
  REMARK    GeneRIF: SETD3 is regulated by a couple of microRNAs and plays
            opposing roles in proliferation and metastasis of hepatocellular
            carcinoma.
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Wilkinson,A.W., Diep,J., Dai,S., Liu,S., Ooi,Y.S., Song,D.,
            Li,T.M., Horton,J.R., Zhang,X., Liu,C., Trivedi,D.V., Ruppel,K.M.,
            Vilches-Moure,J.G., Casey,K.M., Mak,J., Cowan,T., Elias,J.E.,
            Nagamine,C.M., Spudich,J.A., Cheng,X., Carette,J.E. and Gozani,O.
  TITLE     SETD3 is an actin histidine methyltransferase that prevents primary
            dystocia
  JOURNAL   Nature 565 (7739), 372-376 (2019)
   PUBMED   30626964
  REMARK    GeneRIF: results identify a mammalian histidine methyltransferase
            and uncover a pivotal role for SETD3 and actin His73 methylation in
            the regulation of smooth muscle contractility; data also support
            the broader hypothesis that protein histidine methylation acts as a
            common regulatory mechanism
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Eom,G.H., Kim,K.B., Kim,J.H., Kim,J.Y., Kim,J.R., Kee,H.J.,
            Kim,D.W., Choe,N., Park,H.J., Son,H.J., Choi,S.Y., Kook,H. and
            Seo,S.B.
  TITLE     Histone methyltransferase SETD3 regulates muscle differentiation
  JOURNAL   J Biol Chem 286 (40), 34733-34742 (2011)
   PUBMED   21832073
  REMARK    GeneRIF: SETD3 is a H3K4/K36 methyltransferase and plays an
            important role in the transcriptional regulation of muscle cell
            differentiation
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Ishii,H., Mimori,K., Mori,M. and Vecchione,A.
  TITLE     Differentially expressed genes in endothelial differentiation
  JOURNAL   DNA Cell Biol 24 (7), 432-437 (2005)
   PUBMED   16008511
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC152059.4 and AL583892.13.
            
            On Jun 13, 2018 this sequence version replaced XP_006516146.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057968.1, SRR7345562.4209896.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 59.23 cM"
     Protein         1..408
                     /product="actin-histidine N-methyltransferase isoform 6"
                     /EC_number="2.1.1.85"
                     /note="SET domain-containing protein 3; histone-lysine
                     N-methyltransferase setd3; endothelial differentiation
                     inhibitory protein D10; actin-histidine
                     N-methyltransferase; protein-L-histidine
                     N-tele-methyltransferase"
                     /calculated_mol_wt=45941
     Region          1..143
                     /region_name="SET_SETD3"
                     /note="SET domain found in SET domain-containing protein 3
                     (SETD3) and similar proteins; cd19176"
                     /db_xref="CDD:380953"
     Region          158..289
                     /region_name="Rubis-subs-bind"
                     /note="Rubisco LSMT substrate-binding; pfam09273"
                     /db_xref="CDD:462737"
     CDS             1..408
                     /gene="Setd3"
                     /gene_synonym="2610102I01Rik; 2610305M23Rik;
                     6030490B17Rik; D12Ertd771e"
                     /coded_by="NM_001364270.1:332..1558"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:52690"
                     /db_xref="MGI:MGI:1289184"
ORIGIN      
        1 mtvesaknsv lgplysqdri lqamgniala fhllcerasp nsfwqpyiqt lpseydtply
       61 feeeevrclq stqaihdvfs qykntarqya yfykviqitt gynleddrce cvalqdfqag
      121 dqiyifygtr snaefvihsg fffdnnshdr vkiklgvsks drlyamkaev laragiptss
      181 vfalhstepp isaqllaflr vfcmteeelk ehllgdsaid riftlgnaef pvswdnevkl
      241 wtfledrasl llktykttie edkivlknpd lsvratmaik lrlgekeile kavksaavnr
      301 eyyrkhmeer aplpryeesd lglleggvgd srlplvlrkl eeeagvqesl sltetvskvk
      361 aaenglvnge nlipngtrse neslspeese nvtgeessgs makvkerl
//
LOCUS       NP_001018857             627 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 805 isoform 1 [Homo sapiens].
ACCESSION   NP_001018857 XP_372753
VERSION     NP_001018857.2
DBSOURCE    REFSEQ: accession NM_001023563.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Lasky-Su,J., Neale,B.M., Franke,B., Anney,R.J., Zhou,K.,
            Maller,J.B., Vasquez,A.A., Chen,W., Asherson,P., Buitelaar,J.,
            Banaschewski,T., Ebstein,R., Gill,M., Miranda,A., Mulas,F.,
            Oades,R.D., Roeyers,H., Rothenberger,A., Sergeant,J.,
            Sonuga-Barke,E., Steinhausen,H.C., Taylor,E., Daly,M., Laird,N.,
            Lange,C. and Faraone,S.V.
  TITLE     Genome-wide association scan of quantitative traits for attention
            deficit hyperactivity disorder identifies novel associations and
            confirms candidate gene associations
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 147B (8), 1345-1354 (2008)
   PUBMED   18821565
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005261.2.
            
            On Feb 9, 2009 this sequence version replaced NP_001018857.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.229101.1,
                                           SRR1803616.21427.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000414468.3/ ENSP00000412999.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..627
                     /product="zinc finger protein 805 isoform 1"
                     /note="CTC-444N24.8"
                     /calculated_mol_wt=71013
     Region          13..73
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          71..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5CZA5.3)"
     Region          113..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5CZA5.3)"
     Region          205..225
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(210,212,214,216..217,220..221,224,238,240,244..245,
                     248..249,252,266,268,270,272..273,276..277,280)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          218..242
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          233..253
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          257..>580
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          261..281
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          289..309
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          317..337
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          345..365
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          373..393
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          401..421
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(406,408,410,412..413,416..417,420,434,436,440..441,
                     444..445,448,462,464,466,468..469,472..473,476)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          429..449
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          457..477
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          485..505
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(490,492,494,496..497,500..501,504,518,520,524..525,
                     528..529,532,546,548,550,552..553,556..557,560)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          513..533
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          541..561
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..627
                     /gene="ZNF805"
                     /coded_by="NM_001023563.4:261..2144"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46207.1"
                     /db_xref="GeneID:390980"
                     /db_xref="HGNC:HGNC:23272"
ORIGIN      
        1 mamaltdpaq vsvtfddvav tftqeewgql dlaqrtlyqe vmlencgllv slgcpvprpe
       61 liyhlehgqe pwtrkedlsq gtcpgdkgkp kstepttcel alsegisfwg qltqgasgds
      121 qlgqpkdqdg fsemqgerlr pgldsqkekl pgkmspkhdg lgtadsvcsr iiqdrvslgd
      181 dvhdcdshgs gknpviqeee nifkcnecek vfnkkrllar herihsgvkp yectecgktf
      241 skstyllqhh mvhtgekpyk cmecgkafnr kshltqhqri hsgekpykcs ecgkafthrs
      301 tfvlhnrsht gekpfvckec gkafrdrpgf irhyiihsge npyecfecgk vfkhrsylmw
      361 hqqthtgekp yecsecgkaf cesaalihhy vihtgekpfe clecgkafnh rsylkrhqri
      421 htgekpyvcs ecgkafthcs tfilhkraht gekpfeckec gkafsnradl irhfsihtge
      481 kpyecmecgk afnrrsgltr hqrihsgekp yeciecgktf cwstnlirhs iihtgekpye
      541 csecgkafsr sssltqhqrm htgrnpisvt dvgrpftsgq tsvniqelll gknflnvtte
      601 enllqeeasy masdrtyqre tpqvssl
//
LOCUS       NP_085152                834 aa            linear   PRI 27-APR-2025
DEFINITION  arf-GAP with coiled-coil, ANK repeat and PH domain-containing
            protein 3 [Homo sapiens].
ACCESSION   NP_085152
VERSION     NP_085152.2
DBSOURCE    REFSEQ: accession NM_030649.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Zhan,F., Zhang,R., Qiu,L. and Ren,Y.
  TITLE     ACAP3 negatively regulated by HDAC2 inhibits the malignant
            development of papillary thyroid carcinoma cells
  JOURNAL   Int J Biochem Cell Biol 174, 106635 (2024)
   PUBMED   39098591
  REMARK    GeneRIF: ACAP3 negatively regulated by HDAC2 inhibits the malignant
            development of papillary thyroid carcinoma cells.
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Suchkova,I.O., Borisova,E.V. and Patkin,E.L.
  TITLE     Length Polymorphism and Methylation Status of UPS29 Minisatellite
            of the ACAP3 Gene as Molecular Biomarker of Epilepsy. Sex
            Differences in Seizure Types and Symptoms
  JOURNAL   Int J Mol Sci 21 (23), 9206 (2020)
   PUBMED   33276684
  REMARK    GeneRIF: Length Polymorphism and Methylation Status of UPS29
            Minisatellite of the ACAP3 Gene as Molecular Biomarker of Epilepsy.
            Sex Differences in Seizure Types and Symptoms.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 834)
  AUTHORS   Miura,Y. and Kanaho,Y.
  TITLE     ACAP3, the GTPase-activating protein specific to the small GTPase
            Arf6, regulates neuronal migration in the developing cerebral
            cortex
  JOURNAL   Biochem Biophys Res Commun 493 (2), 1089-1094 (2017)
   PUBMED   28919417
REFERENCE   6  (residues 1 to 834)
  AUTHORS   Miura,Y., Hongu,T., Yamauchi,Y., Funakoshi,Y., Katagiri,N.,
            Ohbayashi,N. and Kanaho,Y.
  TITLE     ACAP3 regulates neurite outgrowth through its GAP activity specific
            to Arf6 in mouse hippocampal neurons
  JOURNAL   Biochem J 473 (17), 2591-2602 (2016)
   PUBMED   27330119
REFERENCE   7  (residues 1 to 834)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 834)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 834)
  AUTHORS   Shubina,D.M., Suchkova,I.O., Slominskaia,N.A., Alenina,N., Bader,M.
            and Patkin,E.L.
  TITLE     [CENTB5 gene expression in human and mouse]
  JOURNAL   Mol Biol (Mosk) 43 (3), 407-413 (2009)
   PUBMED   19548526
  REMARK    GeneRIF: minisatellite locus UPS29 can regulate an activity of
            CENTB5, SCNN1D and ACOT7 in nervous system cells.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139287.24, BC051194.1 and AB051503.1.
            
            On Dec 20, 2008 this sequence version replaced NP_085152.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC051194.1, SRR7346977.1849310.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354700.10/ ENSP00000346733.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..834
                     /product="arf-GAP with coiled-coil, ANK repeat and PH
                     domain-containing protein 3"
                     /note="cnt-b5; centaurin-beta-5"
                     /calculated_mol_wt=92364
     Region          16..215
                     /region_name="BAR_ACAP3"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with
                     Coiled-coil, ANK repeat and PH domain containing protein
                     3; cd07637"
                     /db_xref="CDD:153321"
     Site            order(25,28..29,33,35..36,39..40,42..43,53..54,56..57,
                     60..61,63..64,67,81,84..85,176,179..180,182,187,190..191,
                     193..194,197..198,201..202,204..205,208..209,211..212)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153321"
     Region          271..367
                     /region_name="PH_ACAP"
                     /note="ArfGAP with coiled-coil, ankyrin repeat and PH
                     domains Pleckstrin homology (PH) domain; cd13250"
                     /db_xref="CDD:270070"
     Region          375..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P50.2)"
     Region          403..518
                     /region_name="ArfGap_ACAP3"
                     /note="ArfGAP domain of ACAP3 (ArfGAP with Coiled-coil,
                     ANK repeat and PH domains 3); cd08850"
                     /db_xref="CDD:350075"
     Site            order(418,421,438,441,446)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350075"
     Site            order(418,421,438,441)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350075"
     Site            order(443,446..447,456,460..461,501)
                     /site_type="other"
                     /note="putative ANK repeat binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350075"
     Region          633..653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P50.2)"
     Region          <701..>788
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(702,704,708..709,712..714,716..717,721,724,733,735,
                     737,741..742,745..747,749..750,754,757,766,768,770,
                     774..775,778..780,782..783,787)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          702..733
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          702..731
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P50.2)"
     Region          735..766
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          735..764
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P50.2)"
     Region          768..797
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96P50.2)"
     CDS             1..834
                     /gene="ACAP3"
                     /gene_synonym="CENTB5"
                     /coded_by="NM_030649.3:116..2620"
                     /db_xref="CCDS:CCDS19.2"
                     /db_xref="GeneID:116983"
                     /db_xref="HGNC:HGNC:16754"
ORIGIN      
        1 mtvefeecvk dsprfratid evetdvveie akldklvklc sgmveagkay vstsrlfvsg
       61 vrdlsqqcqg dtviseclqr fadslqevvn yhmilfdqaq rsvrqqlqsf vkedvrkfke
      121 tkkqfdkvre dlelslvrna qaprhrphev eeatgaltlt rkcfrhlald yvlqinvlqa
      181 kkkfeildsm lsfmhaqssf fqqgysllhq ldpymkklaa eldqlvidsa vekremerkh
      241 aaiqqrtllq dfsydeskve fdvdapsgvv megylfkras nafktwnrrw fsiqnsqlvy
      301 qkklkdaltv vvddlrlcsv kpcedierrf cfevlsptks cmlqadsekl rqawvqavqa
      361 siasayresp dscyserldr taspstssid satdtrergv kgesvlqrvq svagnsqcgd
      421 cgqpdprwas inlgvllcie csgihrslgv hcskvrsltl dswepellkl mcelgnsavn
      481 qiyeaqcega gsrkptasss rqdkeawikd kyvekkflrk apmapaleap rrwrvqkclr
      541 phssprapta rrkvrlepvl pcvaalssvg tldrkfrrds lfcpdeldsl fsyfdagaag
      601 agprslssds glggssdgss dvlafgsgsv vdsvteeega eseessgead gdteaeawgl
      661 advrelhpgl lahraarard lpalaaalah gaevnwadae degktplvqa vlggslivce
      721 fllqngadvn qrdsrgrapl hhatllgrtg qvclflkrga dqhaldqeqr dplaiavqaa
      781 nadivtllrl armaeemrea eaapgppgal agsptelqfr rciqefislh lees
//
LOCUS       NP_000680                501 aa            linear   PRI 27-APR-2025
DEFINITION  aldehyde dehydrogenase 1A1 [Homo sapiens].
ACCESSION   NP_000680
VERSION     NP_000680.2
DBSOURCE    REFSEQ: accession NM_000689.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Huang,Y.K., Wang,T.M., Chen,C.Y., Li,C.Y., Wang,S.C., Irshad,K.,
            Pan,Y. and Chang,K.C.
  TITLE     The role of ALDH1A1 in glioblastoma proliferation and invasion
  JOURNAL   Chem Biol Interact 402, 111202 (2024)
   PUBMED   39128802
  REMARK    GeneRIF: The role of ALDH1A1 in glioblastoma proliferation and
            invasion.
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Lai,W., Zhao,Y., Chen,Y., Dai,Z., Chen,R., Niu,Y., Chen,X.,
            Chen,S., Huang,G., Shan,Z., Zheng,J., Hu,Y., Chen,Q., Gong,S.,
            Kang,S., Guo,H., Ma,X., Song,Y., Xia,K., Wang,J., Zhou,L., So,K.F.,
            Wang,K., Qiu,S., Zhang,L., Chen,J. and Shi,L.
  TITLE     Autism patient-derived SHANK2BY29X mutation affects the development
            of ALDH1A1 negative dopamine neuron
  JOURNAL   Mol Psychiatry 29 (10), 3180-3194 (2024)
   PUBMED   38704506
  REMARK    GeneRIF: Autism patient-derived SHANK2B[Y29X] mutation affects the
            development of ALDH1A1 negative dopamine neuron.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Wang,M., Wang,T., Wang,J., Yang,Y., Li,X., Chen,H. and Liao,J.
  TITLE     ALDH1A1 promotes immune escape of tumor cells through
            ZBTB7B-glycolysis pathway
  JOURNAL   Cell Death Dis 15 (8), 568 (2024)
   PUBMED   39107297
  REMARK    GeneRIF: ALDH1A1 promotes immune escape of tumor cells through
            ZBTB7B-glycolysis pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Yaghjyan,L., Heng,Y.J., Baker,G.M., Murthy,D., Mahoney,M.B.,
            Rosner,B. and Tamimi,R.M.
  TITLE     Associations of stem cell markers CD44, CD24 and ALDH1A1 with
            mammographic breast density in women with benign breast biopsies
  JOURNAL   Br J Cancer 131 (2), 325-333 (2024)
   PUBMED   38849477
  REMARK    GeneRIF: Associations of stem cell markers CD44, CD24 and ALDH1A1
            with mammographic breast density in women with benign breast
            biopsies.
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Mousa,N.A., Hussein,A., Elemam,N.M., Mohammed,G., Elwany,M.,
            Basha,T., AlHammadi,A.A., Majzob,R.S. and Talaat,I.M.
  TITLE     Are embryonic stem cell markers and ALDH1A1 relevant in the context
            of breast cancer estrogen positivity?
  JOURNAL   Cancer Med 13 (3), e7004 (2024)
   PUBMED   38400679
  REMARK    GeneRIF: Are embryonic stem cell markers and ALDH1A1 relevant in
            the context of breast cancer estrogen positivity?
            Erratum:[Cancer Med. 2024 Apr;13(8):e7171. doi: 10.1002/cam4.7171.
            PMID: 38629223]
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Pereira,F., Rosenmann,E., Nylen,E., Kaufman,M., Pinsky,L. and
            Wrogemann,K.
  TITLE     The 56 kDa androgen binding protein is an aldehyde dehydrogenase
  JOURNAL   Biochem Biophys Res Commun 175 (3), 831-838 (1991)
   PUBMED   1709013
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Hsu,L.C., Chang,W.C. and Yoshida,A.
  TITLE     Genomic structure of the human cytosolic aldehyde dehydrogenase
            gene
  JOURNAL   Genomics 5 (4), 857-865 (1989)
   PUBMED   2591967
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Agarwal,D.P., Cohn,P., Goedde,H.W. and Hempel,J.
  TITLE     Aldehyde dehydrogenase from human erythrocytes: structural
            relationship to the liver cytosolic isozyme
  JOURNAL   Enzyme 42 (1), 47-52 (1989)
   PUBMED   2776714
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Inoue,K., Nishimukai,H. and Yamasawa,K.
  TITLE     Purification and partial characterization of aldehyde dehydrogenase
            from human erythrocytes
  JOURNAL   Biochim Biophys Acta 569 (2), 117-123 (1979)
   PUBMED   224930
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Harada,S., Agarwal,D.P. and Goedde,H.W.
  TITLE     Isozyme variations in acetaldehyde dehydrogenase (e.c.1.2.1.3) in
            human tissues
  JOURNAL   Hum Genet 44 (2), 181-185 (1978)
   PUBMED   730161
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC398835.1, BC001505.2 and
            AI074764.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_000680.1.
            
            Summary: The protein encoded by this gene belongs to the aldehyde
            dehydrogenase family. Aldehyde dehydrogenase is the next enzyme
            after alcohol dehydrogenase in the major pathway of alcohol
            metabolism. There are two major aldehyde dehydrogenase isozymes in
            the liver, cytosolic and mitochondrial, which are encoded by
            distinct genes, and can be distinguished by their electrophoretic
            mobility, kinetic properties, and subcellular localization. This
            gene encodes the cytosolic isozyme. Studies in mice show that
            through its role in retinol metabolism, this gene may also be
            involved in the regulation of the metabolic responses to high-fat
            diet. [provided by RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ224286.1, SRR3476690.103954.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162895, SAMEA2467144
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297785.8/ ENSP00000297785.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.13"
     Protein         1..501
                     /product="aldehyde dehydrogenase 1A1"
                     /EC_number="1.2.1.3"
                     /EC_number="1.2.1.19"
                     /EC_number="1.2.1.36"
                     /EC_number="1.2.1.28"
                     /note="retinaldehyde dehydrogenase 1; aldehyde
                     dehydrogenase 1, soluble; aldehyde dehydrogenase, liver
                     cytosolic; ALDH class 1; acetaldehyde dehydrogenase 1;
                     retinal dehydrogenase 1; ALHDII; RALDH 1; epididymis
                     luminal protein 12; epididymis secretory sperm binding
                     protein Li 53e; epididymis luminal protein 9;
                     3-deoxyglucosone dehydrogenase"
                     /calculated_mol_wt=54731
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:6723659,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Region          15..495
                     /region_name="ALDH_F1AB_F2_RALDH1"
                     /note="NAD+-dependent retinal dehydrogenase 1, ALDH
                     families 1A, 1B, and 2-like; cd07141"
                     /db_xref="CDD:143459"
     Site            order(73..74,78,81,83,87,128,131..132,136,138..139,
                     142..146,148..149,152..159,252,255,258..259,262..263,265,
                     270,435,437,444,447,449..456,463..465,468..471,473,476,
                     481,488..493,495)
                     /site_type="other"
                     /note="homotetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143459"
     Site            91
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Site            order(166..169,193,196,226,230..231,244,247,250,270..271,
                     303,350,353,400)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143459"
     Site            order(170,269,300,303)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143459"
     Site            170
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P20000; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Site            252
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Region          336..501
                     /region_name="Mediates interaction with PRMT3.
                     /evidence=ECO:0000269|PubMed:33495566"
                     /note="propagated from UniProtKB/Swiss-Prot (P00352.2)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Site            353
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Site            367
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Site            410
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Site            419
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Site            435
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     Site            495
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00352.2)"
     CDS             1..501
                     /gene="ALDH1A1"
                     /gene_synonym="ALDC; ALDH-E1; ALDH1; ALDH11; HEL-9;
                     HEL-S-53e; HEL12; PUMB1; RALDH1"
                     /coded_by="NM_000689.5:54..1559"
                     /db_xref="CCDS:CCDS6644.1"
                     /db_xref="GeneID:216"
                     /db_xref="HGNC:HGNC:402"
                     /db_xref="MIM:100640"
ORIGIN      
        1 msssgtpdlp vlltdlkiqy tkifinnewh dsvsgkkfpv fnpateeelc qveegdkedv
       61 dkavkaarqa fqigspwrtm dasergrlly kladlierdr lllatmesmn ggklysnayl
      121 ndlagciktl rycagwadki qgrtipidgn fftytrhepi gvcgqiipwn fplvmliwki
      181 gpalscgntv vvkpaeqtpl talhvaslik eagfppgvvn ivpgygptag aaisshmdid
      241 kvaftgstev gklikeaagk snlkrvtlel ggkspcivla dadldnavef ahhgvfyhqg
      301 qcciaasrif veesiydefv rrsverakky ilgnpltpgv tqgpqidkeq ydkildlies
      361 gkkegaklec gggpwgnkgy fvqptvfsnv tdemriakee ifgpvqqimk fkslddvikr
      421 anntfyglsa gvftkdidka itissalqag tvwvncygvv saqcpfggfk msgngrelge
      481 ygfheytevk tvtvkisqkn s
//
LOCUS       NP_068773                435 aa            linear   PRI 27-APR-2025
DEFINITION  gap junction alpha-3 protein [Homo sapiens].
ACCESSION   NP_068773
VERSION     NP_068773.2
DBSOURCE    REFSEQ: accession NM_021954.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Goyal,S., Singh,R., Singh,J.R. and Vanita,V.
  TITLE     Novel and known variants in GJA3 and LIM2 in congenital cataract
            families from North India
  JOURNAL   BMC Genomics 25 (1), 31 (2024)
   PUBMED   38178039
  REMARK    GeneRIF: Novel and known variants in GJA3 and LIM2 in congenital
            cataract families from North India.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Leon-Fuentes,I.M., Salgado-Gil,M.G., Novoa,M.S. and Retamal,M.A.
  TITLE     Connexins in Cancer, the Possible Role of Connexin46 as a Cancer
            Stem Cell-Determining Protein
  JOURNAL   Biomolecules 13 (10), 1460 (2023)
   PUBMED   37892142
  REMARK    GeneRIF: Connexins in Cancer, the Possible Role of Connexin46 as a
            Cancer Stem Cell-Determining Protein.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Boese,E.A., Drack,A.V., Roos,B.R., Alward,W.L.M., Tollefson,M.R.,
            Schnieders,M.J., Scheetz,T.E., Boldt,H.C., Stone,E.M. and
            Fingert,J.H.
  TITLE     GJA3 Genetic Variation and Autosomal Dominant Congenital Cataracts
            and Glaucoma Following Cataract Surgery
  JOURNAL   JAMA Ophthalmol 141 (9), 872-879 (2023)
   PUBMED   37589989
  REMARK    GeneRIF: GJA3 Genetic Variation and Autosomal Dominant Congenital
            Cataracts and Glaucoma Following Cataract Surgery.
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Acuna,R.A., Varas-Godoy,M., Herrera-Sepulveda,D. and Retamal,M.A.
  TITLE     Connexin46 Expression Enhances Cancer Stem Cell and
            Epithelial-to-Mesenchymal Transition Characteristics of Human
            Breast Cancer MCF-7 Cells
  JOURNAL   Int J Mol Sci 22 (22), 12604 (2021)
   PUBMED   34830485
  REMARK    GeneRIF: Connexin46 Expression Enhances Cancer Stem Cell and
            Epithelial-to-Mesenchymal Transition Characteristics of Human
            Breast Cancer MCF-7 Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Gong,X.D., Wang,Y., Hu,X.B., Zheng,S.Y., Fu,J.L., Nie,Q., Wang,L.,
            Hou,M., Xiang,J.W., Xiao,Y., Gao,Q., Bai,Y.Y., Liu,Y.Z. and Li,D.W.
  TITLE     Aging-dependent loss of GAP junction proteins Cx46 and Cx50 in the
            fiber cells of human and mouse lenses accounts for the diminished
            coupling conductance
  JOURNAL   Aging (Albany NY) 13 (13), 17568-17591 (2021)
   PUBMED   34226295
  REMARK    GeneRIF: Aging-dependent loss of GAP junction proteins Cx46 and
            Cx50 in the fiber cells of human and mouse lenses accounts for the
            diminished coupling conductance.
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Gong,X., Li,E., Klier,G., Huang,Q., Wu,Y., Lei,H., Kumar,N.M.,
            Horwitz,J. and Gilula,N.B.
  TITLE     Disruption of alpha3 connexin gene leads to proteolysis and
            cataractogenesis in mice
  JOURNAL   Cell 91 (6), 833-843 (1997)
   PUBMED   9413992
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Mackay,D., Ionides,A., Berry,V., Moore,A., Bhattacharya,S. and
            Shiels,A.
  TITLE     A new locus for dominant 'zonular pulverulent' cataract, on
            chromosome 13
  JOURNAL   Am J Hum Genet 60 (6), 1474-1478 (1997)
   PUBMED   9199569
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Hsieh,C.L., Kumar,N.M., Gilula,N.B. and Francke,U.
  TITLE     Distribution of genes for gap junction membrane channel proteins on
            human and mouse chromosomes
  JOURNAL   Somat Cell Mol Genet 17 (2), 191-200 (1991)
   PUBMED   1849321
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Willecke,K., Jungbluth,S., Dahl,E., Hennemann,H., Heynkes,R. and
            Grzeschik,K.H.
  TITLE     Six genes of the human connexin gene family coding for gap
            junctional proteins are assigned to four different human
            chromosomes
  JOURNAL   Eur J Cell Biol 53 (2), 275-280 (1990)
   PUBMED   1964417
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Rosenberg,A.M. and Gole,G.A.
  TITLE     Morning Glory Syndrome: a report of two cases
  JOURNAL   Aust J Ophthalmol 9 (4), 263-265 (1981)
   PUBMED   7342922
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138688.27, DR003755.1 and
            BF726530.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 11, 2002 this sequence version replaced NP_068773.1.
            
            Summary: The protein encoded by this gene is a connexin and is a
            component of lens fiber gap junctions. Defects in this gene are a
            cause of zonular pulverulent cataract type 3 (CZP3). [provided by
            RefSeq, Jan 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DR003755.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000241125.4/ ENSP00000241125.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..435
                     /product="gap junction alpha-3 protein"
                     /note="connexin-46; gap junction alpha 3; gap junction
                     protein, alpha 3, 46kDa"
                     /calculated_mol_wt=47279
     Region          3..227
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6H8.4)"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6H8.4)"
     Region          108..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6H8.4)"
     Site            153..173
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6H8.4)"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6H8.4)"
     Region          291..435
                     /region_name="Connexin40_C"
                     /note="Connexin 40 C-terminal domain; cl46284"
                     /db_xref="CDD:480624"
     Region          332..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6H8.4)"
     CDS             1..435
                     /gene="GJA3"
                     /gene_synonym="CTRCT14; CX46; CZP3"
                     /coded_by="NM_021954.4:181..1488"
                     /db_xref="CCDS:CCDS9289.1"
                     /db_xref="GeneID:2700"
                     /db_xref="HGNC:HGNC:4277"
                     /db_xref="MIM:121015"
ORIGIN      
        1 mgdwsflgrl lenaqehstv igkvwltvlf ifrilvlgaa aedvwgdeqs dftcntqqpg
       61 cenvcydraf pishirfwal qiifvstptl iylghvlhiv rmeekkkere eeeqlkresp
      121 spkeppqdnp ssrddrgrvr magallrtyv fniifktlfe vgfiagqyfl ygfelkplyr
      181 cdrwpcpntv dcfisrptek tifiifmlav acaslllnml eiyhlgwkkl kqgvtsrlgp
      241 daseaplgta dppplppssr ppavaigfpp yyahtaaplg qaravgypga pppaadfkll
      301 alteargkgq saklynghhh llmteqnwan qaaerqppal kaypaastpa apspvgsssp
      361 plaheaeaga apllldgsgs slegsalagt peeeeqavtt aaqmhqpplp lgdpgraska
      421 srassgrarp edlai
//
LOCUS       NP_001354509             314 aa            linear   PRI 27-APR-2025
DEFINITION  cytohesin-3 isoform b [Homo sapiens].
ACCESSION   NP_001354509
VERSION     NP_001354509.1
DBSOURCE    REFSEQ: accession NM_001367580.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Fu,Y., Li,J., Feng,M.X., Yang,X.M., Wang,Y.H., Zhang,Y.L., Qin,W.,
            Xia,Q. and Zhang,Z.G.
  TITLE     Cytohesin-3 is upregulated in hepatocellular carcinoma and
            contributes to tumor growth and vascular invasion
  JOURNAL   Int J Clin Exp Pathol 7 (5), 2123-2132 (2014)
   PUBMED   24966920
  REMARK    GeneRIF: Cytohesin-3 was upregulated in hepatocellular carcinoma
            tissues, correlating with overall survival/relapse-free survival
            and tumor size/vascular invasion.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Malaby,A.W., van den Berg,B. and Lambright,D.G.
  TITLE     Structural basis for membrane recruitment and allosteric activation
            of cytohesin family Arf GTPase exchange factors
  JOURNAL   Proc Natl Acad Sci U S A 110 (35), 14213-14218 (2013)
   PUBMED   23940353
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Nevrivy,D.J., Peterson,V.J., Avram,D., Ishmael,J.E., Hansen,S.G.,
            Dowell,P., Hruby,D.E., Dawson,M.I. and Leid,M.
  TITLE     Interaction of GRASP, a protein encoded by a novel retinoic
            acid-induced gene, with members of the cytohesin family of guanine
            nucleotide exchange factors
  JOURNAL   J Biol Chem 275 (22), 16827-16836 (2000)
   PUBMED   10828067
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Ogasawara,M., Kim,S.C., Adamik,R., Togawa,A., Ferrans,V.J.,
            Takeda,K., Kirby,M., Moss,J. and Vaughan,M.
  TITLE     Similarities in function and gene structure of cytohesin-4 and
            cytohesin-1, guanine nucleotide-exchange proteins for
            ADP-ribosylation factors
  JOURNAL   J Biol Chem 275 (5), 3221-3230 (2000)
   PUBMED   10652308
REFERENCE   8  (residues 1 to 314)
  AUTHORS   Venkateswarlu,K., Gunn-Moore,F., Oatey,P.B., Tavare,J.M. and
            Cullen,P.J.
  TITLE     Nerve growth factor- and epidermal growth factor-stimulated
            translocation of the ADP-ribosylation factor-exchange factor GRP1
            to the plasma membrane of PC12 cells requires activation of
            phosphatidylinositol 3-kinase and the GRP1 pleckstrin homology
            domain
  JOURNAL   Biochem J 335 (Pt 1) (Pt 1), 139-146 (1998)
   PUBMED   9742223
REFERENCE   9  (residues 1 to 314)
  AUTHORS   Franco,M., Boretto,J., Robineau,S., Monier,S., Goud,B., Chardin,P.
            and Chavrier,P.
  TITLE     ARNO3, a Sec7-domain guanine nucleotide exchange factor for ADP
            ribosylation factor 1, is involved in the control of Golgi
            structure and function
  JOURNAL   Proc Natl Acad Sci U S A 95 (17), 9926-9931 (1998)
   PUBMED   9707577
REFERENCE   10 (residues 1 to 314)
  AUTHORS   Klarlund,J.K., Guilherme,A., Holik,J.J., Virbasius,J.V., Chawla,A.
            and Czech,M.P.
  TITLE     Signaling by phosphoinositide-3,4,5-trisphosphate through proteins
            containing pleckstrin and Sec7 homology domains
  JOURNAL   Science 275 (5308), 1927-1930 (1997)
   PUBMED   9072969
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009412.6 and AC004895.3.
            
            Summary: This gene encodes a member of the PSCD (pleckstrin
            homology, Sec7 and coiled-coil domains) family. PSCD family members
            have identical structural organization that consists of an
            N-terminal coiled-coil motif, a central Sec7 domain, and a
            C-terminal pleckstrin homology (PH) domain. The coiled-coil motif
            is involved in homodimerization, the Sec7 domain contains
            guanine-nucleotide exchange protein (GEP) activity, and the PH
            domain interacts with phospholipids and is responsible for
            association of PSCDs with membranes. Members of this family appear
            to mediate the regulation of protein sorting and membrane
            trafficking. This encoded protein is involved in the control of
            Golgi structure and function, and it may have a physiological role
            in regulating ADP-ribosylation factor protein 6 (ARF) functions, in
            addition to acting on ARF1. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AK295163.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..314
                     /product="cytohesin-3 isoform b"
                     /note="pleckstrin homology, Sec7 and coiled-coil domains
                     3; ARF nucleotide-binding site opener 3; general receptor
                     of phosphoinositides 1; PH, SEC7 and coiled-coil
                     domain-containing protein 3"
                     /calculated_mol_wt=36662
     Region          <66..163
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          178..297
                     /region_name="PH_GRP1-like"
                     /note="General Receptor for Phosphoinositides-1-like
                     Pleckstrin homology (PH) domain; cd01252"
                     /db_xref="CDD:269954"
     Site            order(178,205,207,209,219,222,224,255..257,259,262..267,
                     297)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:269954"
     Site            order(188,191,195,197,199,210,220,258,269..270)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269954"
     CDS             1..314
                     /gene="CYTH3"
                     /gene_synonym="ARNO3; cytohesin-3; GRP1; PSCD3"
                     /coded_by="NM_001367580.1:1295..2239"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:9265"
                     /db_xref="HGNC:HGNC:9504"
                     /db_xref="MIM:605081"
ORIGIN      
        1 malpqlqtam laaflwdprd vvltaqpgae qcaessqhir ilqpqfrlir lrfwklyiqr
       61 rvqawqflws frlpgeaqki drmmeafasr yclcnpgvfq stdtcyvlsf aiimlntslh
      121 nhnvrdkpta erfiamnrgi neggdlpeel lrnlyesikn epfkipeddg ndlthtffnp
      181 dregwllklg grvktwkrrw filtdnclyy feyttdkepr giiplenlsi revedprkpn
      241 cfelynpshk gqvikackte adgrvvegnh vvyrisapsp eekeewmksi kasisrdpfy
      301 dmlatrkrri ankk
//
LOCUS       NP_001348391             186 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein mL62 isoform 3 precursor [Mus
            musculus].
ACCESSION   NP_001348391
VERSION     NP_001348391.1
DBSOURCE    REFSEQ: accession NM_001361462.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Cheong,A., Lingutla,R. and Mager,J.
  TITLE     Expression analysis of mammalian mitochondrial ribosomal protein
            genes
  JOURNAL   Gene Expr Patterns 38, 119147 (2020)
   PUBMED   32987154
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Feaga,H.A., Quickel,M.D., Hankey-Giblin,P.A. and Keiler,K.C.
  TITLE     Human Cells Require Non-stop Ribosome Rescue Activity in
            Mitochondria
  JOURNAL   PLoS Genet 12 (3), e1005964 (2016)
   PUBMED   27029019
  REMARK    GeneRIF: Because ICT1 is essential in human cells, these results
            suggest that ribosome rescue activity in mitochondria is required
            in humans
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Handa,Y., Hikawa,Y., Tochio,N., Kogure,H., Inoue,M., Koshiba,S.,
            Guntert,P., Inoue,Y., Kigawa,T., Yokoyama,S. and Nameki,N.
  TITLE     Solution structure of the catalytic domain of the mitochondrial
            protein ICT1 that is essential for cell vitality
  JOURNAL   J Mol Biol 404 (2), 260-273 (2010)
   PUBMED   20869366
  REMARK    GeneRIF: solution structure of the catalytic domain of the ICT1
            protein that lacks an N-terminal mitochondrial targeting signal and
            an unstructured C-terminal basic-residue-rich extension
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY137982.1, BC079614.1 and AW495606.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079614.1, CD355003.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 80.84 cM"
     Protein         1..186
                     /product="large ribosomal subunit protein mL62 isoform 3
                     precursor"
                     /EC_number="3.1.1.29"
                     /note="peptidyl-tRNA hydrolase ICT1, mitochondrial; large
                     ribosomal subunit protein mL62; immature colon carcinoma
                     transcript 1 protein homolog; 39S ribosomal protein L58,
                     mitochondrial"
                     /calculated_mol_wt=21226
     CDS             1..186
                     /gene="Mrpl58"
                     /gene_synonym="1110001A02Rik; 1110002E03Rik; Ict1;
                     MRP-L58"
                     /coded_by="NM_001361462.1:24..584"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS88282.1"
                     /db_xref="GeneID:68572"
                     /db_xref="MGI:MGI:1915822"
ORIGIN      
        1 matawglrwg lsrtgtllla pparcarral hrqvdgttfq siysldklyp eskgadtawk
       61 vpehakqass yiplvnskae vrfhlasadw ieepvrqkia lthknkinka gelvltsess
      121 ryqfrnlaec lqkirdmiae asqvpkepsk edarlqrlri ekmnrerlrq krlnsalkts
      181 rrmtmd
//
LOCUS       NP_001306145             483 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome P450 1A1 isoform 2 [Homo sapiens].
ACCESSION   NP_001306145
VERSION     NP_001306145.1
DBSOURCE    REFSEQ: accession NM_001319216.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Guo,L., Zhang,X., Li,X., Wang,K., Wang,Y., Abulikemu,A., Su,X.,
            Shu,M., Li,H., Cui,S., Xu,Z., Tian,H., Niu,Y., Yuan,H., He,Z.,
            Sun,X. and Duan,H.
  TITLE     Polycyclic aromatic hydrocarbon and its adducts in peripheral
            blood: Gene and environment interaction among Chinese population
  JOURNAL   Environ Int 190, 108922 (2024)
   PUBMED   39128373
  REMARK    GeneRIF: Polycyclic aromatic hydrocarbon and its adducts in
            peripheral blood: Gene and environment interaction among Chinese
            population.
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Xu,J. and Tan,C.
  TITLE     Interaction between CYP1A1 gene polymorphism and environment
            factors on risk of endometrial cancer
  JOURNAL   Environ Health Prev Med 29, 54 (2024)
   PUBMED   39384367
  REMARK    GeneRIF: Interaction between CYP1A1 gene polymorphism and
            environment factors on risk of endometrial cancer.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Datkhile,K.D., Patil,S.R., Patil,M.N., Durgawale,P.P.,
            Jagdale,N.J., Deshmukh,V.N., More,A.L., Gudur,R.A. and Gudur,A.K.
  TITLE     Genetic polymorphisms of CYP1A, CYP1B, CYP2C and risk of cervical
            cancer among rural population of Maharashtra: Findings from a
            hospital-based case-control study
  JOURNAL   J Cancer Res Ther 19 (7), 1925-1930 (2023)
   PUBMED   38376298
  REMARK    GeneRIF: Genetic polymorphisms of CYP1A, CYP1B, CYP2C and risk of
            cervical cancer among rural population of Maharashtra: Findings
            from a hospital-based case-control study.
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Dutkiewicz,Z. and Mikstacka,R.
  TITLE     Hydration and Structural Adaptations of the Human CYP1A1, CYP1A2,
            and CYP1B1 Active Sites by Molecular Dynamics Simulations
  JOURNAL   Int J Mol Sci 24 (14), 11481 (2023)
   PUBMED   37511239
  REMARK    GeneRIF: Hydration and Structural Adaptations of the Human CYP1A1,
            CYP1A2, and CYP1B1 Active Sites by Molecular Dynamics Simulations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Jiang,Z., Dragin,N., Jorge-Nebert,L.F., Martin,M.V.,
            Guengerich,F.P., Aklillu,E., Ingelman-Sundberg,M., Hammons,G.J.,
            Lyn-Cook,B.D., Kadlubar,F.F., Saldana,S.N., Sorter,M., Vinks,A.A.,
            Nassr,N., von Richter,O., Jin,L. and Nebert,D.W.
  TITLE     Search for an association between the human CYP1A2 genotype and
            CYP1A2 metabolic phenotype
  JOURNAL   Pharmacogenet Genomics 16 (5), 359-367 (2006)
   PUBMED   16609368
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Jiang,Z., Dalton,T.P., Jin,L., Wang,B., Tsuneoka,Y., Shertzer,H.G.,
            Deka,R. and Nebert,D.W.
  TITLE     Toward the evaluation of function in genetic variability:
            characterizing human SNP frequencies and establishing
            BAC-transgenic mice carrying the human CYP1A1_CYP1A2 locus
  JOURNAL   Hum Mutat 25 (2), 196-206 (2005)
   PUBMED   15643613
  REMARK    GeneRIF: Determination of SNP frequencies in the CYP1A1_CYP1A2
            locus.
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Hayashi,S., Watanabe,J., Nakachi,K. and Kawajiri,K.
  TITLE     Genetic linkage of lung cancer-associated MspI polymorphisms with
            amino acid replacement in the heme binding region of the human
            cytochrome P450IA1 gene
  JOURNAL   J Biochem 110 (3), 407-411 (1991)
   PUBMED   1722803
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Kubota,M., Sogawa,K., Kaizu,Y., Sawaya,T., Watanabe,J.,
            Kawajiri,K., Gotoh,O. and Fujii-Kuriyama,Y.
  TITLE     Xenobiotic responsive element in the 5'-upstream region of the
            human P-450c gene
  JOURNAL   J Biochem 110 (2), 232-236 (1991)
   PUBMED   1761516
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Kawajiri,K., Nakachi,K., Imai,K., Yoshii,A., Shinoda,N. and
            Watanabe,J.
  TITLE     Identification of genetically high risk individuals to lung cancer
            by DNA polymorphisms of the cytochrome P450IA1 gene
  JOURNAL   FEBS Lett 263 (1), 131-133 (1990)
   PUBMED   1691986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091230.23.
            
            Summary: This gene, CYP1A1, encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This protein localizes to the endoplasmic reticulum and its
            expression is induced by some polycyclic aromatic hydrocarbons
            (PAHs), some of which are found in cigarette smoke. The enzyme's
            endogenous substrate is unknown; however, it is able to metabolize
            some PAHs to carcinogenic intermediates. The gene has been
            associated with lung cancer risk. A related family member, CYP1A2,
            is located approximately 25 kb away from CYP1A1 on chromosome 15.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            lacks an in-frame coding exon, compared to variant 1, and encodes a
            shorter isoform (2), compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY871801.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2142586 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..483
                     /product="cytochrome P450 1A1 isoform 2"
                     /EC_number="1.14.14.1"
                     /EC_number="4.2.1.152"
                     /note="flavoprotein-linked monooxygenase; cytochrome
                     P1-450, dioxin-inducible; xenobiotic monooxygenase; aryl
                     hydrocarbon hydroxylase; cytochrome P450, subfamily I
                     (aromatic compound-inducible), polypeptide 1; cytochrome
                     P450 1A1; cytochrome P450-C; cytochrome P450-P1;
                     cytochrome P450 form 6; cytochrome P450, family 1,
                     subfamily A, polypeptide 1; hydroperoxy icosatetraenoate
                     dehydratase"
                     /calculated_mol_wt=54669
     Region          70..476
                     /region_name="cytochrome_P450"
                     /note="cytochrome P450 (CYP) superfamily; cl41757"
                     /db_xref="CDD:477761"
     Site            order(131,135,142,198,313..314,317..318,321..322,325,376,
                     386,388,420..422,426..430,433..434)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410651"
     Site            order(224..225,313,316..317,321,384..387)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410651"
     CDS             1..483
                     /gene="CYP1A1"
                     /gene_synonym="AHH; AHRR; CP11; CYP1; CYPIA1; P1-450;
                     P450-C; P450DX"
                     /coded_by="NM_001319216.2:118..1569"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS81906.1"
                     /db_xref="GeneID:1543"
                     /db_xref="HGNC:HGNC:2595"
                     /db_xref="MIM:108330"
ORIGIN      
        1 mlfpismsat efllasvifc lvfwvirasr pqvpkglknp pgpwgwplig hmltlgknph
       61 lalsrmsqqy gdvlqirigs tpvvvlsgld tirqalvrqg ddfkgrpdly tftlisngqs
      121 msfspdsgpv waarrrlaqn glksfsiasd passtscyle ehvskeaevl istlqelmag
      181 pghfnpyryv vvsvtnvica icfgrrydhn hqellslvnl nnnfgevvgs gnpadfipil
      241 rylpnpslna fkdlnekfys fmqkmvkehy ktfekghird itdsliehcq ekqldenanv
      301 qlsdekiini vldlfgagfd tvttaiswsl mylvmnprvq rkiqeeldtv igrsrrprls
      361 drshlpymea filetfrhss fvpftiphrk lwvnpseflp erfltpdgai dkvlsekvii
      421 fgmgkrkcig etiarwevfl flaillqrve fsvplgvkvd mtpiygltmk haccehfqmq
      481 lrs
//
LOCUS       NP_065863               2047 aa            linear   PRI 27-APR-2025
DEFINITION  dedicator of cytokinesis protein 6 isoform 1 [Homo sapiens].
ACCESSION   NP_065863
VERSION     NP_065863.2
DBSOURCE    REFSEQ: accession NM_020812.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2047)
  AUTHORS   Swiderska,M.K., Mostowska,A., Skrypnik,D., Bogdanski,P.,
            Jagodzinski,P.P. and Grzegorzewska,A.E.
  TITLE     Associations of ANGPTL6, DOCK6, FABP1, and PCSK9 single-nucleotide
            variants with hypercholesterolemia in the Polish population: a
            cross-sectional study
  JOURNAL   Pol Arch Intern Med 133 (2) (2023)
   PUBMED   36601873
  REMARK    GeneRIF: Associations of ANGPTL6, DOCK6, FABP1, and PCSK9
            single-nucleotide variants with hypercholesterolemia in the Polish
            population: a cross-sectional study.
REFERENCE   2  (residues 1 to 2047)
  AUTHORS   Dessay,M., Couture,E., Maaroufi,H., Fournier,F., Gagnon,E.,
            Droit,A., Brown,J.P. and Michou,L.
  TITLE     Attenuated clinical and osteoclastic phenotypes of Paget's disease
            of bone linked to the p.Pro392Leu/SQSTM1 mutation by a rare variant
            in the DOCK6 gene
  JOURNAL   BMC Med Genomics 15 (1), 41 (2022)
   PUBMED   35241069
  REMARK    GeneRIF: Attenuated clinical and osteoclastic phenotypes of Paget's
            disease of bone linked to the p.Pro392Leu/SQSTM1 mutation by a rare
            variant in the DOCK6 gene.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2047)
  AUTHORS   Zhang,Z.Y., Sun,Y.Y., Wang,H.C., Fu,W.N. and Sun,C.F.
  TITLE     Overexpression of DOCK6 in oral squamous cell cancer promotes
            cellular migration and invasion and is associated with poor
            prognosis
  JOURNAL   Arch Oral Biol 133, 105297 (2022)
   PUBMED   34742001
  REMARK    GeneRIF: Overexpression of DOCK6 in oral squamous cell cancer
            promotes cellular migration and invasion and is associated with
            poor prognosis.
REFERENCE   4  (residues 1 to 2047)
  AUTHORS   Muller,P.M., Rademacher,J., Bagshaw,R.D., Wortmann,C., Barth,C.,
            van Unen,J., Alp,K.M., Giudice,G., Eccles,R.L., Heinrich,L.E.,
            Pascual-Vargas,P., Sanchez-Castro,M., Brandenburg,L., Mbamalu,G.,
            Tucholska,M., Spatt,L., Czajkowski,M.T., Welke,R.W., Zhang,S.,
            Nguyen,V., Rrustemi,T., Trnka,P., Freitag,K., Larsen,B., Popp,O.,
            Mertins,P., Gingras,A.C., Roth,F.P., Colwill,K., Bakal,C.,
            Pertz,O., Pawson,T., Petsalaki,E. and Rocks,O.
  TITLE     Systems analysis of RhoGEF and RhoGAP regulatory proteins reveals
            spatially organized RAC1 signalling from integrin adhesions
  JOURNAL   Nat Cell Biol 22 (4), 498-511 (2020)
   PUBMED   32203420
REFERENCE   5  (residues 1 to 2047)
  AUTHORS   Shaheen,R., Faqeih,E., Sunker,A., Morsy,H., Al-Sheddi,T.,
            Shamseldin,H.E., Adly,N., Hashem,M. and Alkuraya,F.S.
  TITLE     Recessive mutations in DOCK6, encoding the guanidine nucleotide
            exchange factor DOCK6, lead to abnormal actin cytoskeleton
            organization and Adams-Oliver syndrome
  JOURNAL   Am J Hum Genet 89 (2), 328-333 (2011)
   PUBMED   21820096
  REMARK    GeneRIF: A homozygous truncating mutation in dedicator of
            cytokinesis 6 gene (DOCK6) which encodes an atypical guanidine
            exchange factor (GEF) known to activate two members of the Rho
            GTPase family: Cdc42 and Rac1, was identified.
REFERENCE   6  (residues 1 to 2047)
  AUTHORS   Wang,K.S., Liu,X.F. and Aragam,N.
  TITLE     A genome-wide meta-analysis identifies novel loci associated with
            schizophrenia and bipolar disorder
  JOURNAL   Schizophr Res 124 (1-3), 192-199 (2010)
   PUBMED   20889312
REFERENCE   7  (residues 1 to 2047)
  AUTHORS   Miyamoto,Y., Yamauchi,J., Sanbe,A. and Tanoue,A.
  TITLE     Dock6, a Dock-C subfamily guanine nucleotide exchanger, has the
            dual specificity for Rac1 and Cdc42 and regulates neurite outgrowth
  JOURNAL   Exp Cell Res 313 (4), 791-804 (2007)
   PUBMED   17196961
REFERENCE   8  (residues 1 to 2047)
  AUTHORS   Cheng,J., Kapranov,P., Drenkow,J., Dike,S., Brubaker,S., Patel,S.,
            Long,J., Stern,D., Tammana,H., Helt,G., Sementchenko,V.,
            Piccolboni,A., Bekiranov,S., Bailey,D.K., Ganesh,M., Ghosh,S.,
            Bell,I., Gerhard,D.S. and Gingeras,T.R.
  TITLE     Transcriptional maps of 10 human chromosomes at 5-nucleotide
            resolution
  JOURNAL   Science 308 (5725), 1149-1154 (2005)
   PUBMED   15790807
REFERENCE   9  (residues 1 to 2047)
  AUTHORS   Cote,J.F. and Vuori,K.
  TITLE     Identification of an evolutionarily conserved superfamily of
            DOCK180-related proteins with guanine nucleotide exchange activity
  JOURNAL   J Cell Sci 115 (Pt 24), 4901-4913 (2002)
   PUBMED   12432077
REFERENCE   10 (residues 1 to 2047)
  AUTHORS   Lehman,A., Wuyts,W. and Patel,M.S.
  TITLE     Adams-Oliver Syndrome - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27077170
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011472.7, CV571923.1,
            AB037816.2, DC333132.1, AK316063.1, CX759906.1 and BC008335.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 22, 2007 this sequence version replaced NP_065863.1.
            
            Summary: This gene encodes a member of the dedicator of cytokinesis
            (DOCK) family of atypical guanine nucleotide exchange factors.
            Guanine nucleotide exchange factors interact with small GTPases and
            are components of intracellular signaling networks. The encoded
            protein is a group C DOCK protein and plays a role in actin
            cytoskeletal reorganization by activating the Rho GTPases Cdc42 and
            Rac1. Mutations in this gene are associated with Adams-Oliver
            syndrome 2. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC146786.1, AB037816.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294618.12/ ENSP00000294618.6
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2047
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..2047
                     /product="dedicator of cytokinesis protein 6 isoform 1"
                     /note="dedicator of cytokinesis protein 6"
                     /calculated_mol_wt=229428
     Region          20..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HP0.3)"
     Region          48..157
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          136..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HP0.3)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDR9; propagated from
                     UniProtKB/Swiss-Prot (Q96HP0.3)"
     Region          213..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HP0.3)"
     Region          410..444
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HP0.3)"
     Region          547..724
                     /region_name="C2_Dock-C"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08696"
                     /db_xref="CDD:176078"
     Site            865
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDR9; propagated from
                     UniProtKB/Swiss-Prot (Q96HP0.3)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96HP0.3)"
     Site            880
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96HP0.3)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDR9; propagated from
                     UniProtKB/Swiss-Prot (Q96HP0.3)"
     Region          1068..1090
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HP0.3)"
     Site            1308
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96HP0.3)"
     Region          1592..2014
                     /region_name="DHR2_DOCK6"
                     /note="Dock Homology Region 2, a GEF domain, of Class C
                     Dedicator of Cytokinesis 6; cd11702"
                     /db_xref="CDD:212575"
     Site            order(1708,1718,1720..1721,1723..1724,1727..1728,
                     1730..1731,1734..1735)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212575"
     Site            order(1750,1752,1775,1778..1781,1783..1784,1803..1805,
                     1822..1824,1852..1855,1865..1866,1869,1871,1908..1909,
                     1912,1928..1929,1931..1932,1935..1937,1940..1942,
                     1945..1946,1949,1977,1999,2002)
                     /site_type="other"
                     /note="Rac/Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212575"
     Site            1940..1945
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212575"
     Region          2025..2047
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HP0.3)"
     Site            2036
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96HP0.3)"
     CDS             1..2047
                     /gene="DOCK6"
                     /gene_synonym="AOS2; ZIR1"
                     /coded_by="NM_020812.4:85..6228"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45975.1"
                     /db_xref="GeneID:57572"
                     /db_xref="HGNC:HGNC:19189"
                     /db_xref="MIM:614194"
ORIGIN      
        1 maaserrafa hkinrtvaae vrkqvsrers gsphssrrcs sslgvpltev vepldfedvl
       61 lsrppdaepg plrdlvefpa ddlelllqpr ecrttepgip kdekldaqvr aavemyiedw
      121 vivhrryqyl saayspvttd tqrerqkglp rqvfeqdasg dersgpedsn dsrrgsgspe
      181 dtprssgass ifdlrnlaad sllpsllera apedvdrrne tlrrqhrppa lltlypapde
      241 deavercsrp epprehfgqr ilvkclslkf eieiepifgi lalydvrekk kisenfyfdl
      301 nsdsmkgllr ahgthpaist larsaifsvt ypspdiflvi klekvlqqgd iseccepymv
      361 lkevdtaknk ekleklrlaa eqfctrlgry rmpfawtavh lanivssagq ldrdsdsege
      421 rrpawtdrrr rgpqdrassg ddacsfsgfr patltvtnff kqeaerlsde dlfkfladmr
      481 rpssllrrlr pvtaqlkidi spapenphfc lspellhikp ypdprgrptk eilefparev
      541 yaphtsyrnl lyvyphslnf ssrqgsvrnl avrvqymtge dpsqalpvif gksscseftr
      601 eaftpvvyhn kspefyeefk lhlpacvten hhllftfyhv scqprpgtal etpvgftwip
      661 llqhgrlrtg pfclpvsvdq pppsysvltp dvalpgmrwv dghkgvfsve ltavssvhpq
      721 dpyldkfftl vhvleegafp frlkdtvlse gnveqelras laalrlaspe plvafshhvl
      781 dklvrlvirp piisgqivnl grgafeamah vvslvhrsle aaqdarghcp qlaayvhyaf
      841 rlpgtepslp dgappvtvqa atlargsgrp aslylarsks isssnpdlav apgsvddevs
      901 rilaskllhe elalqwvvss savreailqh awfffqlmvk smalhlllgq rldtprklrf
      961 pgrflddita lvgsvglevi trvhkdvela ehlnaslaff lsdllslvdr gfvfslvrah
     1021 ykqvatrlqs spnpaalltl rmeftrilcs hehyvtlnlp ccplsppasp spsvssttsq
     1081 sstfssqapd pkvtsmfels gpfrqqhfla gllltelala lepeaegafl lhkkaisavh
     1141 sllcghdtdp ryaeatvkar vaelylplls iardtlprlh dfaegpgqrs rlasmldsdt
     1201 egegdiagti npsvamaiag gplapgsras isqgpptasr agcalsaess rtllacvlwv
     1261 lkntepallq rwatdltlpq lgrlldllyl claafeykgk kaferinslt fkksldmkar
     1321 leeailgtig arqemvrrsr erspfgnpen vrwrksvthw kqtsdrvdkt kdemehealv
     1381 egnlateasl vvldtleiiv qtvmlseare svlgavlkvv lyslgsaqsa lflqhglatq
     1441 ralvskfpel lfeedtelca dlclrllrhc gsristirth asaslyllmr qnfeighnfa
     1501 rvkmqvtmsl sslvgttqnf seehlrrslk tiltyaeedm glrdstfaeq vqdlmfnlhm
     1561 iltdtvkmke hqedpemlid lmyriargyq gspdlrltwl qnmagkhael gnhaeaaqcm
     1621 vhaaalvaey lalledhrhl pvgcvsfqni ssnvleesai sddilspdee gfcsgkhfte
     1681 lglvglleqa agyftmggly eavnevyknl ipileahrdy kklaavhgkl qeaftkimhq
     1741 ssgwervfgt yfrvgfygah fgdldeqefv ykepsitkla eishrleefy terfgddvve
     1801 iikdsnpvdk skldsqkayi qityvepyfd tyelkdrvty fdrnyglrtf lfctpftpdg
     1861 rahgelpeqh krktllstdh afpyiktrir vchreetvlt pvevaiedmq kktrelafat
     1921 eqdppdakml qmvlqgsvgp tvnqgpleva qvflaeiped pklfrhhnkl rlcfkdfckk
     1981 cedalrknka ligpdqkeyh relernycrl realqplltq rlpqlmaptp pglrnslnra
     2041 sfrkadl
//
LOCUS       NP_006757               2004 aa            linear   PRI 27-APR-2025
DEFINITION  histone acetyltransferase KAT6A isoform 1 [Homo sapiens].
ACCESSION   NP_006757
VERSION     NP_006757.2
DBSOURCE    REFSEQ: accession NM_006766.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2004)
  AUTHORS   Olbromski,M., Mrozowska,M., Smolarz,B., Romanowicz,H., Rusak,A. and
            Piotrowska,A.
  TITLE     ERalpha status of invasive ductal breast carcinoma as a result of
            regulatory interactions between lysine deacetylases KAT6A and KAT6B
  JOURNAL   Sci Rep 14 (1), 26935 (2024)
   PUBMED   39505971
  REMARK    GeneRIF: ERalpha status of invasive ductal breast carcinoma as a
            result of regulatory interactions between lysine deacetylases KAT6A
            and KAT6B.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2004)
  AUTHORS   Tan,K., Wang,J., Su,X., Zheng,Y. and Li,W.
  TITLE     KAT6A/YAP/TEAD4 pathway modulates osteoclastogenesis by regulating
            the RANKL/OPG ratio on the compression side during orthodontic
            tooth movement
  JOURNAL   Prog Orthod 25 (1), 29 (2024)
   PUBMED   39129034
  REMARK    GeneRIF: KAT6A/YAP/TEAD4 pathway modulates osteoclastogenesis by
            regulating the RANKL/OPG ratio on the compression side during
            orthodontic tooth movement.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2004)
  AUTHORS   Tham,E., Lindstrand,A., Santani,A., Malmgren,H., Nesbitt,A.,
            Dubbs,H.A., Zackai,E.H., Parker,M.J., Millan,F., Rosenbaum,K.,
            Wilson,G.N. and Nordgren,A.
  TITLE     Dominant mutations in KAT6A cause intellectual disability with
            recognizable syndromic features
  JOURNAL   Am J Hum Genet 96 (3), 507-513 (2015)
   PUBMED   25728777
  REMARK    GeneRIF: Heterozygous truncating mutations in KAT6A, as well as
            deletions of the same locus, cause a syndrome characterized by
            intellectual disability, craniosynostosis, cardiac defects, feeding
            difficulties, and distinct facial features.
REFERENCE   4  (residues 1 to 2004)
  AUTHORS   Dreveny,I., Deeves,S.E., Fulton,J., Yue,B., Messmer,M.,
            Bhattacharya,A., Collins,H.M. and Heery,D.M.
  TITLE     The double PHD finger domain of MOZ/MYST3 induces alpha-helical
            structure of the histone H3 tail to facilitate acetylation and
            methylation sampling and modification
  JOURNAL   Nucleic Acids Res 42 (2), 822-835 (2014)
   PUBMED   24150941
  REMARK    GeneRIF: The double PHD finger domain of MOZ/MYST3 induces
            alpha-helical structure of the histone H3 tail to facilitate
            acetylation and methylation sampling and modification.
REFERENCE   5  (residues 1 to 2004)
  AUTHORS   Ali,M., Yan,K., Lalonde,M.E., Degerny,C., Rothbart,S.B.,
            Strahl,B.D., Cote,J., Yang,X.J. and Kutateladze,T.G.
  TITLE     Tandem PHD fingers of MORF/MOZ acetyltransferases display
            selectivity for acetylated histone H3 and are required for the
            association with chromatin
  JOURNAL   J Mol Biol 424 (5), 328-338 (2012)
   PUBMED   23063713
  REMARK    GeneRIF: These data suggest that the tandem of plant homeodomain
            1/2 fingers play a role in MOZ and MORF histone acetyltransferase
            association with histon H3 regions enriched in acetylated marks.
REFERENCE   6  (residues 1 to 2004)
  AUTHORS   Qiu,Y., Liu,L., Zhao,C., Han,C., Li,F., Zhang,J., Wang,Y., Li,G.,
            Mei,Y., Wu,M., Wu,J. and Shi,Y.
  TITLE     Combinatorial readout of unmodified H3R2 and acetylated H3K14 by
            the tandem PHD finger of MOZ reveals a regulatory mechanism for
            HOXA9 transcription
  JOURNAL   Genes Dev 26 (12), 1376-1391 (2012)
   PUBMED   22713874
  REMARK    GeneRIF: PHD12 facilitates the localization of MOZ onto the
            promoter locus of the HOXA9 gene, thereby promoting the H3
            acetylation around the promoter region.
REFERENCE   7  (residues 1 to 2004)
  AUTHORS   Qin,S., Jin,L., Zhang,J., Liu,L., Ji,P., Wu,M., Wu,J. and Shi,Y.
  TITLE     Recognition of unmodified histone H3 by the first PHD finger of
            bromodomain-PHD finger protein 2 provides insights into the
            regulation of histone acetyltransferases monocytic leukemic
            zinc-finger protein (MOZ) and MOZ-related factor (MORF)
  JOURNAL   J Biol Chem 286 (42), 36944-36955 (2011)
   PUBMED   21880731
  REMARK    GeneRIF: Recognition of unmodified histone H3 by the first PHD
            finger of bromodomain-PHD finger protein 2 provides insights into
            the regulation of histone acetyltransferases monocytic leukemic
            zinc-finger protein (MOZ) and MOZ-related factor (MORF).
REFERENCE   8  (residues 1 to 2004)
  AUTHORS   Champagne,N., Pelletier,N. and Yang,X.J.
  TITLE     The monocytic leukemia zinc finger protein MOZ is a histone
            acetyltransferase
  JOURNAL   Oncogene 20 (3), 404-409 (2001)
   PUBMED   11313971
REFERENCE   9  (residues 1 to 2004)
  AUTHORS   Borrow,J., Stanton,V.P. Jr., Andresen,J.M., Becher,R., Behm,F.G.,
            Chaganti,R.S., Civin,C.I., Disteche,C., Dube,I., Frischauf,A.M.,
            Horsman,D., Mitelman,F., Volinia,S., Watmore,A.E. and Housman,D.E.
  TITLE     The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses
            a putative acetyltransferase to the CREB-binding protein
  JOURNAL   Nat Genet 14 (1), 33-41 (1996)
   PUBMED   8782817
REFERENCE   10 (residues 1 to 2004)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA442995.1, BC142659.1,
            U47742.1, AA310750.1, CB216817.1, AC090571.5 and AJ420560.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 3, 2007 this sequence version replaced NP_006757.1.
            
            Summary: This gene encodes a member of the MOZ, YBFR2, SAS2, TIP60
            family of histone acetyltransferases. The protein is composed of a
            nuclear localization domain, a double C2H2 zinc finger domain that
            binds to acetylated histone tails, a histone acetyl-transferase
            domain, a glutamate/aspartate-rich region, and a serine- and
            methionine-rich transactivation domain. It is part of a complex
            that acetylates lysine-9 residues in histone 3, and in addition, it
            acts as a co-activator for several transcription factors. Allelic
            variants of this gene are associated with an autosomal dominant
            form of cognitive disability. Chromosomal translocations of this
            gene are associated with acute myeloid leukemia. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: MW032476.1, U47742.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265713.8/ ENSP00000265713.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2004
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..2004
                     /product="histone acetyltransferase KAT6A isoform 1"
                     /EC_number="2.3.1.48"
                     /note="MYST histone acetyltransferase (monocytic leukemia)
                     3; zinc finger protein 220; monocytic leukemia zinc finger
                     protein; runt-related transcription factor binding protein
                     2; histone acetyltransferase MYST3; MOZ, YBF2/SAS3, SAS2
                     and TIP60 protein 3; histone acetyltransferase KAT6A;
                     K(lysine) acetyltransferase 6A"
                     /calculated_mol_wt=224898
     Region          1..144
                     /region_name="Required for activation of RUNX1-1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Region          52..166
                     /region_name="Required for nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Region          85..162
                     /region_name="H15"
                     /note="Domain in histone families 1 and 5; smart00526"
                     /db_xref="CDD:197772"
     Region          144..664
                     /region_name="Interaction with PML.
                     /evidence=ECO:0000269|PubMed:23431171"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Site            172
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZ21; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Region          205..262
                     /region_name="PHD1_MOZ_MORF"
                     /note="PHD finger 1 found in monocytic leukemia
                     zinc-finger protein (MOZ) and its factor (MORF); cd15618"
                     /db_xref="CDD:277090"
     Site            order(208,210..211,213,230,235..237,242..244,257,259..261)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:277090"
     Site            order(244,248,251..252,255,257..258,260,262)
                     /site_type="other"
                     /note="PHD2 interface [polypeptide binding]"
                     /db_xref="CDD:277090"
     Region          264..310
                     /region_name="PHD2_KAT6A_6B"
                     /note="PHD finger 2 found in monocytic leukemia
                     zinc-finger protein (MOZ) and its factor (MORF); cd15527"
                     /db_xref="CDD:277002"
     Site            order(264,269,282..286)
                     /site_type="other"
                     /note="PHD1 interface [polypeptide binding]"
                     /db_xref="CDD:277002"
     Site            order(276..282,285,300..303)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:277002"
     Region          312..664
                     /region_name="Interaction with RUNX1-1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Region          334..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Site            350
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            355
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:23431171; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Region          441..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Region          488..778
                     /region_name="Catalytic"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Region          <504..778
                     /region_name="PLN00104"
                     /note="MYST -like histone acetyltransferase; Provisional"
                     /db_xref="CDD:215056"
     Region          507..810
                     /region_name="Mediates interaction with BRPF1, required
                     for histone H3 acetyltransferase activity.
                     /evidence=ECO:0000269|PubMed:18794358"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Site            604
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000269|Ref.27; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Region          785..1445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZ21; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            813..814
                     /site_type="other"
                     /note="Breakpoint for translocation to form KAT6A-ASXL2;
                     propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Site            815
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZ21; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            899
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q5TKR9; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            941
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            954
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            974
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            1007
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            1089
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            1090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            1113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92794.2)"
     Site            1117..1118
                     /site_type="other"
                     /note="Breakpoint for translocation to form KAT6A-EP300
                     and KAT6A-NCOA2; propagated from UniProtKB/Swiss-Prot
                     (Q92794.2)"
     Region          1461..1621
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Region          1517..1741
                     /region_name="Interaction with PML.
                     /evidence=ECO:0000269|PubMed:23431171"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Region          1517..1642
                     /region_name="Interaction with RUNX1-2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Site            1546..1547
                     /site_type="other"
                     /note="Breakpoint for translocation to form KAT6A-CREBBP;
                     propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Region          1637..1721
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     Region          1913..1948
                     /region_name="Required for activation of RUNX1-2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92794.2)"
     CDS             1..2004
                     /gene="KAT6A"
                     /gene_synonym="ARTHS; MOZ; MRD32; MYST-3; MYST3; RUNXBP2;
                     ZC2HC6A; ZNF220"
                     /coded_by="NM_006766.5:413..6427"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6124.1"
                     /db_xref="GeneID:7994"
                     /db_xref="HGNC:HGNC:13013"
                     /db_xref="MIM:601408"
ORIGIN      
        1 mvklanplyt ewileaikkv kkqkqrpsee ricnavsssh gldrktvleq lelsvkdgti
       61 lkvsnkglns ykdpdnpgri alpkprnhgk ldnkqnvdwn klikravegl aesggstlks
      121 ierflkgqkd vsalfggsaa sgfhqqlrla ikraighgrl lkdgplyrln tkatnvdgke
      181 sceslsclpp vsllphekdk pvaepipics fclgtkeqnr ekkpeelisc adcgnsghps
      241 clkfspeltv rvkalrwqci ecktcsscrd qgknadnmlf cdscdrgfhm eccdppltrm
      301 pkgmwicqic rprkkgrkll qkkaaqikrr ytnpigrpkn rlkkqntvsk gpfskvrtgp
      361 grgrkrkitl ssqsasssse egyleridgl dfcrdsnvsl kfnkktkgli dgltkfftps
      421 pdgrkargev vdyseqyrir krgnrkssts dwptdnqdgw dgkqeneerl fgsqeimtek
      481 dmelfrdiqe qalqkvgvtg ppdpqvrcps viefgkyeih twysspypqe ysrlpklylc
      541 efclkymksr tilqqhmkkc gwfhppanei yrknnisvfe vdgnvstiyc qnlcllaklf
      601 ldhktlyydv epflfyvltq ndvkgchlvg yfskekhcqq kynvscimil pqyqrkgygr
      661 flidfsylls kregqagspe kplsdlgrls ymaywksvil eclyhqndkq isikklsklt
      721 gicpqditst lhhlrmldfr sdqfviirre kliqdhmakl qlnlrpvdvd peclrwtpvi
      781 vsnsvvseee eeeaeegene epqcqerele isvgksvshe nkeqdsysve sekkpevmap
      841 vsstrlskqv lphdslpans qpsrrgrwgr knrktqerfg dkdsklllee tssapqeqyg
      901 ecgekseatq eqyteseeql vaseeqpsqd gkpdlpkrrl segvepwrgq lkkspealkc
      961 rltegserlp rrysegdrav lrgfsessee eeepesprss sppiltkptl krkkpflhrr
     1021 rrvrkrkhhn ssvvtetise ttevldepfe dsdserpmpr leptfeidee eeeedenelf
     1081 preyfrrlss qdvlrcqsss krkskdeeed eesddaddtp ilkpvsllrk rdvknsplep
     1141 dtstplkkkk gwpkgksrkp ihwkkrpgrk pgfklsreim pvstqacvie pivsipkagr
     1201 kpkiqeseet vepkedmplp eerkeeeemq aeaeeaeege eedaassevp aaspadssns
     1261 petetkepev eeeeekprvs eeqrqseeeq qeleepepee eedaaaetaq nddhdadded
     1321 dghlestkkk eleeqptred vkeepgvqes fldanmqksr ekikdkeete ldseeeqpsh
     1381 dtsvvseqma gseddheeds htkeelielk eeeeiphsel dletvqavqs ltqeessehe
     1441 gayqdceetl aacqtlqsyt qadedpqmsm vedchasehn spissvqshp sqsvrsvssp
     1501 nvpalesgyt qispeqgsls apsmqnmets pmmdvpsvsd hsqqvvdsgf sdlgsiestt
     1561 enyenpssyd stmggsicgn sssqsscsyg glsssssltq sscvvtqqma smgsscsmmq
     1621 qssvqpaanc sikspqscvv erppsnqqqq ppppppqqpq ppppqpqpap qppppqqqpq
     1681 qqpqpqpqqp ppppppqqqp plsqcsmnns ftpapmimei pesgstgnis iyeripgdfg
     1741 agsysqpsat fslaklqqlt ntimdphamp yshspavtsy atsvslsntg laqlapshpl
     1801 agtpqaqatm tpppnlastt mnltspllqc nmsatnigip htqrlqgqmp vkghisirsk
     1861 saplpsaaah qqqlygrsps avamqagpra lavqrgmnmg vnlmptpayn vnsmnmntln
     1921 amnsyrmtqp mmnssyhsnp aymnqtaqyp mqmqmgmmgs qaytqqpmqp nphgnmmytg
     1981 pshhsymnaa gvpkqslngp ymrr
//
LOCUS       NP_002709               1150 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein phosphatase 2A regulatory subunit B''
            subunit alpha isoform 1 [Homo sapiens].
ACCESSION   NP_002709
VERSION     NP_002709.2
DBSOURCE    REFSEQ: accession NM_002718.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Jiao,N., Ji,W.S., Zhang,B., Shang,Y.K., Zhang,Y.C., Yu,W.Q.,
            Jin,H.L., Li,C., Zhang,C.Y., Yan,C., Yue,W. and Zhang,Q.
  TITLE     Overexpression of Protein Phosphatase 2 Regulatory Subunit B'Alpha
            Promotes Glycolysis by Regulating Hexokinase 1 in Hepatocellular
            Carcinoma
  JOURNAL   Biomed Environ Sci 35 (7), 622-632 (2022)
   PUBMED   35945177
  REMARK    GeneRIF: Overexpression of Protein Phosphatase 2 Regulatory Subunit
            B''Alpha Promotes Glycolysis by Regulating Hexokinase 1 in
            Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Zheng,J., Tian,N., Liu,F., Zhang,Y., Su,J., Gao,Y., Deng,M.,
            Wei,L., Ye,J., Li,H. and Wang,J.Z.
  TITLE     A novel dephosphorylation targeting chimera selectively promoting
            tau removal in tauopathies
  JOURNAL   Signal Transduct Target Ther 6 (1), 269 (2021)
   PUBMED   34262014
  REMARK    GeneRIF: A novel dephosphorylation targeting chimera selectively
            promoting tau removal in tauopathies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Dzulko,M., Pons,M., Henke,A., Schneider,G. and Kramer,O.H.
  TITLE     The PP2A subunit PR130 is a key regulator of cell development and
            oncogenic transformation
  JOURNAL   Biochim Biophys Acta Rev Cancer 1874 (2), 188453 (2020)
   PUBMED   33068647
  REMARK    GeneRIF: The PP2A subunit PR130 is a key regulator of cell
            development and oncogenic transformation.
            Review article
REFERENCE   4  (residues 1 to 1150)
  AUTHORS   Dmitriev,A.A., Beniaminov,A.D., Melnikova,N.V., Pushkova,E.N.,
            Gerashchenko,G.V., Kudryavtseva,A.V. and Kashuba,V.I.
  TITLE     [Functional Hypermethylation of ALDH1L1, PLCL2, and PPP2R3A in
            Colon Cancer]
  JOURNAL   Mol Biol (Mosk) 54 (2), 204-211 (2020)
   PUBMED   32392189
  REMARK    GeneRIF: [Functional Hypermethylation of ALDH1L1, PLCL2, and
            PPP2R3A in Colon Cancer].
REFERENCE   5  (residues 1 to 1150)
  AUTHORS   Reynhout,S., Jansen,S., Haesen,D., van Belle,S., de Munnik,S.A.,
            Bongers,E.M.H.F., Schieving,J.H., Marcelis,C., Amiel,J., Rio,M.,
            Mclaughlin,H., Ladda,R., Sell,S., Kriek,M.,
            Peeters-Scholte,C.M.P.C.D., Terhal,P.A., van Gassen,K.L.,
            Verbeek,N., Henry,S., Scott Schwoerer,J., Malik,S., Revencu,N.,
            Ferreira,C.R., Macnamara,E., Braakman,H.M.H., Brimble,E.,
            Ruzhnikov,M.R.Z., Wagner,M., Harrer,P., Wieczorek,D., Kuechler,A.,
            Tziperman,B., Barel,O., de Vries,B.B.A., Gordon,C.T., Janssens,V.
            and Vissers,L.E.L.M.
  TITLE     De Novo Mutations Affecting the Catalytic Calpha Subunit of PP2A,
            PPP2CA, Cause Syndromic Intellectual Disability Resembling Other
            PP2A-Related Neurodevelopmental Disorders
  JOURNAL   Am J Hum Genet 104 (1), 139-156 (2019)
   PUBMED   30595372
  REMARK    Erratum:[Am J Hum Genet. 2019 Feb 7;104(2):357. doi:
            10.1016/j.ajhg.2019.01.003. PMID: 30735662]
REFERENCE   6  (residues 1 to 1150)
  AUTHORS   Ruediger,R., Fields,K. and Walter,G.
  TITLE     Binding specificity of protein phosphatase 2A core enzyme for
            regulatory B subunits and T antigens
  JOURNAL   J Virol 73 (1), 839-842 (1999)
   PUBMED   9847399
REFERENCE   7  (residues 1 to 1150)
  AUTHORS   Ruediger,R., Brewis,N., Ohst,K. and Walter,G.
  TITLE     Increasing the ratio of PP2A core enzyme to holoenzyme inhibits
            Tat-stimulated HIV-1 transcription and virus production
  JOURNAL   Virology 238 (2), 432-443 (1997)
   PUBMED   9400615
REFERENCE   8  (residues 1 to 1150)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   9  (residues 1 to 1150)
  AUTHORS   Hendrix,P., Mayer-Jackel,R.E., Cron,P., Goris,J., Hofsteenge,J.,
            Merlevede,W. and Hemmings,B.A.
  TITLE     Structure and expression of a 72-kDa regulatory subunit of protein
            phosphatase 2A. Evidence for different size forms produced by
            alternative splicing
  JOURNAL   J Biol Chem 268 (20), 15267-15276 (1993)
   PUBMED   8392071
REFERENCE   10 (residues 1 to 1150)
  AUTHORS   Mayer,R.E., Hendrix,P., Cron,P., Matthies,R., Stone,S.R., Goris,J.,
            Merlevede,W., Hofsteenge,J. and Hemmings,B.A.
  TITLE     Structure of the 55-kDa regulatory subunit of protein phosphatase
            2A: evidence for a neuronal-specific isoform
  JOURNAL   Biochemistry 30 (15), 3589-3597 (1991)
   PUBMED   1849734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK293012.1, AL389975.1 and
            DB378665.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_002709.1.
            
            Summary: This gene encodes one of the regulatory subunits of the
            protein phosphatase 2. Protein phosphatase 2 (formerly named type
            2A) is one of the four major Ser/Thr phosphatases and is implicated
            in the negative control of cell growth and division. Protein
            phosphatase 2 holoenzymes are heterotrimeric proteins composed of a
            structural subunit A, a catalytic subunit C, and a regulatory
            subunit B. The regulatory subunit is encoded by a diverse set of
            genes that have been grouped into the B/PR55, B'/PR61, and B''/PR72
            families. These different regulatory subunits confer distinct
            enzymatic specificities and intracellular localizations to the
            holozenzyme. The product of this gene belongs to the B'' family.
            The B'' family has been further divided into subfamilies. The
            product of this gene belongs to the alpha subfamily of regulatory
            subunit B''. Alternative splicing results in multiple transcript
            variants encoding different isoforms.[provided by RefSeq, Jun
            2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1), also known as
            isoform beta or isoform PR130.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.163327.1,
                                           SRR1803612.161424.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264977.8/ ENSP00000264977.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.2-q22.3"
     Protein         1..1150
                     /product="serine/threonine-protein phosphatase 2A
                     regulatory subunit B'' subunit alpha isoform 1"
                     /EC_number="3.1.3.16"
                     /note="serine/threonine-protein phosphatase 2A 72/130 kDa
                     regulatory subunit B; protein phosphatase 2, regulatory
                     subunit B'', alpha; PR130/B''alpha1 subunit;
                     PR72/B''alpha2 subuit"
                     /calculated_mol_wt=130147
     Region          661..693
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06190.1)"
     Region          787..1070
                     /region_name="PPP2R3A"
                     /note="serine/threonine protein phosphatase 2A regulatory
                     subunit B' subunit alpha; cd21506"
                     /db_xref="CDD:410339"
     Region          1105..1132
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06190.1)"
     CDS             1..1150
                     /gene="PPP2R3A"
                     /gene_synonym="PPP2R3; PR130; PR72"
                     /coded_by="NM_002718.5:563..4015"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3087.1"
                     /db_xref="GeneID:5523"
                     /db_xref="HGNC:HGNC:9307"
                     /db_xref="MIM:604944"
ORIGIN      
        1 maatyrlvvs tvnhyssvvi drrfeqaihy ctgtchtfth gidcivvhhs vcadllhipv
       61 sqfkdadlns mflphengls saegdypqqa ftgiprvkrg stfqntynlk diageaisfa
      121 sgkikefsfe klknsnhaay rkgrkvksds fnrrsvdldl lcghynndgn apsfgllrss
      181 sveekplshr nsldtnltsm flqnfseedl vtqilekhki dnfssgtdik mcldillkcs
      241 edlkkctdii kqcikkksgs sisegsgndt isssetvymn vmtrlasylk klpfefmqsg
      301 nnealdltel isnmpslqlt pfspvfgteq ppkyedvvql sasdsgrfqt ielqndkpns
      361 rkmdtvqsip nnstnslynl evndprtlka vqvqsqsltm nplenvssdd lmetlyieee
      421 sdgkkaldkg qktengpshe llkvnehrae fpehathlkk cptpmqneig kifeksfvnl
      481 pkedckskvs kfeegdqrdf tnsssqeeid kllmdlesfs qkmetslrep lakgknsnfl
      541 nshsqltgqt lvdlepkskv sspiekvsps cltriietng hkieeedral llrilesied
      601 faqelvecks srgslsqeke mmqilqetlt tssqanlsvc rspvgdkakd ttsavliqqt
      661 pevikiqnkp ekkpgtplpp patspssprp lspvphvnnv vnaplsinip rfyfpeglpd
      721 tcsnheqtls rietafmdie eqkadiyemg kiakvcgcpl ywkapmfraa ggektgfvta
      781 qsfiamwrkl lnnhhddask ficllakpnc ssleqedfip llqdvvdthp gltflkdape
      841 fhsryittvi qrifytvnrs wsgkitstei rksnflqtla lleeeedinq itdyfsyehf
      901 yviyckfwel dtdhdlyisq adlsryndqa sssriierif sgavtrgkti qkegrmsyad
      961 fvwfliseed krnptsieyw frcmdvdgdg vlsmyeleyf yeeqcermea mgieplpfhd
     1021 llcqmldlvk pavdgkitlr dlkrcrmahi fydtffnlek yldheqrdpf avqkdvendg
     1081 pepsdwdrfa aeeyetlvae esaqaqfqeg fedyetdepa spsefgnksn kilsaslpek
     1141 cgklqsvdee
//
LOCUS       NP_079904                 86 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome c oxidase subunit 6B1 [Mus musculus].
ACCESSION   NP_079904 XP_914756
VERSION     NP_079904.1
DBSOURCE    REFSEQ: accession NM_025628.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Vercellino,I. and Sazanov,L.A.
  TITLE     SCAF1 drives the compositional diversity of mammalian respirasomes
  JOURNAL   Nat Struct Mol Biol 31 (7), 1061-1071 (2024)
   PUBMED   38575788
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Vercellino,I. and Sazanov,L.A.
  TITLE     Structure and assembly of the mammalian mitochondrial supercomplex
            CIII2CIV
  JOURNAL   Nature 598 (7880), 364-367 (2021)
   PUBMED   34616041
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Yao,Y., Liu,Q., Adrianto,I., Wu,X., Glassbrook,J., Khalasawi,N.,
            Yin,C., Yi,Q., Dong,Z., Geissmann,F., Zhou,L. and Mi,Q.S.
  TITLE     Histone deacetylase 3 controls lung alveolar macrophage development
            and homeostasis
  JOURNAL   Nat Commun 11 (1), 3822 (2020)
   PUBMED   32732898
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 86)
  AUTHORS   Cui,X.S., Li,X.Y., Jeong,Y.J., Jun,J.H. and Kim,N.H.
  TITLE     Gene expression of cox5a, 5b, or 6b1 and their roles in
            preimplantation mouse embryos
  JOURNAL   Biol Reprod 74 (3), 601-610 (2006)
   PUBMED   16291927
  REMARK    GeneRIF: gene expression of the Cox subunits, Cox5a, 5b, and 6b1 is
            not required for embryo developmental events up to the blastocyst
            stage
REFERENCE   6  (residues 1 to 86)
  AUTHORS   Grossman,L.I. and Lomax,M.I.
  TITLE     Nuclear genes for cytochrome c oxidase
  JOURNAL   Biochim Biophys Acta 1352 (2), 174-192 (1997)
   PUBMED   9199249
  REMARK    Review article
REFERENCE   7  (residues 1 to 86)
  AUTHORS   Stubbs,L., Carver,E.A., Shannon,M.E., Kim,J., Geisler,J.,
            Generoso,E.E., Stanford,B.G., Dunn,W.C., Mohrenweiser,H.,
            Zimmermann,W., Watt,S.M. and Ashworth,L.K.
  TITLE     Detailed comparative map of human chromosome 19q and related
            regions of the mouse genome
  JOURNAL   Genomics 35 (3), 499-508 (1996)
   PUBMED   8812484
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK007996.1 and AW047421.1.
            
            On Dec 7, 2005 this sequence version replaced XP_914756.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV449586.1, BQ747274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 18.84 cM"
     Protein         1..86
                     /product="cytochrome c oxidase subunit 6B1"
                     /EC_number="7.1.1.9"
                     /note="cytochrome c oxidase, subunit VIb polypeptide 1"
                     /calculated_mol_wt=9940
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P00429; propagated from
                     UniProtKB/Swiss-Prot (P56391.2)"
     Region          8..85
                     /region_name="Cyt_c_Oxidase_VIb"
                     /note="Cytochrome c oxidase subunit VIb. Cytochrome c
                     oxidase (CcO), the terminal oxidase in the respiratory
                     chains of eukaryotes and most bacteria, is a multi-chain
                     transmembrane protein located in the inner membrane of
                     mitochondria and the cell membrane of...; cd00926"
                     /db_xref="CDD:238466"
     Site            order(12..15,24..27,59,62..68)
                     /site_type="other"
                     /note="Subunit VIb/II interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Site            24
                     /site_type="other"
                     /note="Subunit VIb/I interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Site            order(28,31,83)
                     /site_type="other"
                     /note="Subunit VIb/III interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Region          30..40
                     /region_name="Cx9C motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (P56391.2)"
     Site            order(47,49..54)
                     /site_type="other"
                     /note="Subunit VIb/VIb interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Region          54..65
                     /region_name="Cx10C motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (P56391.2)"
     Site            62
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (P56391.2)"
     Site            order(76,79..81)
                     /site_type="other"
                     /note="Subunit VIb/VIa interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     CDS             1..86
                     /gene="Cox6b1"
                     /gene_synonym="2010000G05Rik; COX VIb-1; Cox6b"
                     /coded_by="NM_025628.3:73..333"
                     /db_xref="CCDS:CCDS39887.1"
                     /db_xref="GeneID:110323"
                     /db_xref="MGI:MGI:107460"
ORIGIN      
        1 maediktkik nyktapfdsr fpnqnqtknc wqnyldfhrc ekamtakggd vsvcewyrrv
       61 ykslcpvswv sawddriaeg tfpgki
//
LOCUS       NP_078945                614 aa            linear   PRI 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 55 [Homo sapiens].
ACCESSION   NP_078945
VERSION     NP_078945.2
DBSOURCE    REFSEQ: accession NM_024669.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Yazdanpanah,M., Jalilian,N., Abdollah Zadeh,R., Sahraian,M.A. and
            Noori-Daloii,M.R.
  TITLE     Investigating the association of polymorphisms of ANKRD55 and MMEL1
            with susceptibility to multiple sclerosis in Iranian population
  JOURNAL   Int J Neurosci 132 (10), 1037-1042 (2022)
   PUBMED   33491520
  REMARK    GeneRIF: Investigating the association of polymorphisms of ANKRD55
            and MMEL1 with susceptibility to multiple sclerosis in Iranian
            population.
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Mena,J., Alloza,I., Tulloch Navarro,R., Aldekoa,A., Diez Garcia,J.,
            Villanueva Etxebarria,A., Lindskog,C., Antiguedad,A., Boyero,S.,
            Mendibe-Bilbao,M.D.M., Alvarez de Arcaya,A., Sanchez Menoyo,J.L.,
            Midaglia,L., Villarrubia,N., Malhotra,S., Montalban,X.,
            Villar,L.M., Comabella,M. and Vandenbroeck,K.
  TITLE     Genomic Multiple Sclerosis Risk Variants Modulate the Expression of
            the ANKRD55-IL6ST Gene Region in Immature Dendritic Cells
  JOURNAL   Front Immunol 12, 816930 (2022)
   PUBMED   35111166
  REMARK    GeneRIF: Genomic Multiple Sclerosis Risk Variants Modulate the
            Expression of the ANKRD55-IL6ST Gene Region in Immature Dendritic
            Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Korshunov,A., Okonechnikov,K., Schmitt-Hoffner,F., Ryzhova,M.,
            Sahm,F., Stichel,D., Schrimpf,D., Reuss,D.E., Sievers,P.,
            Suwala,A.K., Kumirova,E., Zheludkova,O., Golanov,A., Jones,D.T.W.,
            Pfister,S.M., Kool,M. and von Deimling,A.
  TITLE     Molecular analysis of pediatric CNS-PNET revealed nosologic
            heterogeneity and potent diagnostic markers for CNS neuroblastoma
            with FOXR2-activation
  JOURNAL   Acta Neuropathol Commun 9 (1), 20 (2021)
   PUBMED   33536079
  REMARK    GeneRIF: Molecular analysis of pediatric CNS-PNET revealed
            nosologic heterogeneity and potent diagnostic markers for CNS
            neuroblastoma with FOXR2-activation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 614)
  AUTHORS   Ugidos,N., Mena,J., Baquero,S., Alloza,I., Azkargorta,M.,
            Elortza,F. and Vandenbroeck,K.
  TITLE     Interactome of the Autoimmune Risk Protein ANKRD55
  JOURNAL   Front Immunol 10, 2067 (2019)
   PUBMED   31620119
  REMARK    GeneRIF: Interactome of the Autoimmune Risk Protein ANKRD55.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 614)
  AUTHORS   Zhernakova,A., Stahl,E.A., Trynka,G., Raychaudhuri,S., Festen,E.A.,
            Franke,L., Westra,H.J., Fehrmann,R.S., Kurreeman,F.A., Thomson,B.,
            Gupta,N., Romanos,J., McManus,R., Ryan,A.W., Turner,G., Brouwer,E.,
            Posthumus,M.D., Remmers,E.F., Tucci,F., Toes,R., Grandone,E.,
            Mazzilli,M.C., Rybak,A., Cukrowska,B., Coenen,M.J., Radstake,T.R.,
            van Riel,P.L., Li,Y., de Bakker,P.I., Gregersen,P.K.,
            Worthington,J., Siminovitch,K.A., Klareskog,L., Huizinga,T.W.,
            Wijmenga,C. and Plenge,R.M.
  TITLE     Meta-analysis of genome-wide association studies in celiac disease
            and rheumatoid arthritis identifies fourteen non-HLA shared loci
  JOURNAL   PLoS Genet 7 (2), e1002004 (2011)
   PUBMED   21383967
REFERENCE   7  (residues 1 to 614)
  AUTHORS   Teslovich,T.M., Musunuru,K., Smith,A.V., Edmondson,A.C.,
            Stylianou,I.M., Koseki,M., Pirruccello,J.P., Ripatti,S.,
            Chasman,D.I., Willer,C.J., Johansen,C.T., Fouchier,S.W., Isaacs,A.,
            Peloso,G.M., Barbalic,M., Ricketts,S.L., Bis,J.C., Aulchenko,Y.S.,
            Thorleifsson,G., Feitosa,M.F., Chambers,J., Orho-Melander,M.,
            Melander,O., Johnson,T., Li,X., Guo,X., Li,M., Shin Cho,Y., Jin
            Go,M., Jin Kim,Y., Lee,J.Y., Park,T., Kim,K., Sim,X., Twee-Hee
            Ong,R., Croteau-Chonka,D.C., Lange,L.A., Smith,J.D., Song,K., Hua
            Zhao,J., Yuan,X., Luan,J., Lamina,C., Ziegler,A., Zhang,W.,
            Zee,R.Y., Wright,A.F., Witteman,J.C., Wilson,J.F., Willemsen,G.,
            Wichmann,H.E., Whitfield,J.B., Waterworth,D.M., Wareham,N.J.,
            Waeber,G., Vollenweider,P., Voight,B.F., Vitart,V.,
            Uitterlinden,A.G., Uda,M., Tuomilehto,J., Thompson,J.R., Tanaka,T.,
            Surakka,I., Stringham,H.M., Spector,T.D., Soranzo,N., Smit,J.H.,
            Sinisalo,J., Silander,K., Sijbrands,E.J., Scuteri,A., Scott,J.,
            Schlessinger,D., Sanna,S., Salomaa,V., Saharinen,J., Sabatti,C.,
            Ruokonen,A., Rudan,I., Rose,L.M., Roberts,R., Rieder,M.,
            Psaty,B.M., Pramstaller,P.P., Pichler,I., Perola,M., Penninx,B.W.,
            Pedersen,N.L., Pattaro,C., Parker,A.N., Pare,G., Oostra,B.A.,
            O'Donnell,C.J., Nieminen,M.S., Nickerson,D.A., Montgomery,G.W.,
            Meitinger,T., McPherson,R., McCarthy,M.I., McArdle,W., Masson,D.,
            Martin,N.G., Marroni,F., Mangino,M., Magnusson,P.K., Lucas,G.,
            Luben,R., Loos,R.J., Lokki,M.L., Lettre,G., Langenberg,C.,
            Launer,L.J., Lakatta,E.G., Laaksonen,R., Kyvik,K.O., Kronenberg,F.,
            Konig,I.R., Khaw,K.T., Kaprio,J., Kaplan,L.M., Johansson,A.,
            Jarvelin,M.R., Janssens,A.C., Ingelsson,E., Igl,W., Kees
            Hovingh,G., Hottenga,J.J., Hofman,A., Hicks,A.A., Hengstenberg,C.,
            Heid,I.M., Hayward,C., Havulinna,A.S., Hastie,N.D., Harris,T.B.,
            Haritunians,T., Hall,A.S., Gyllensten,U., Guiducci,C., Groop,L.C.,
            Gonzalez,E., Gieger,C., Freimer,N.B., Ferrucci,L., Erdmann,J.,
            Elliott,P., Ejebe,K.G., Doring,A., Dominiczak,A.F., Demissie,S.,
            Deloukas,P., de Geus,E.J., de Faire,U., Crawford,G., Collins,F.S.,
            Chen,Y.D., Caulfield,M.J., Campbell,H., Burtt,N.P.,
            Bonnycastle,L.L., Boomsma,D.I., Boekholdt,S.M., Bergman,R.N.,
            Barroso,I., Bandinelli,S., Ballantyne,C.M., Assimes,T.L.,
            Quertermous,T., Altshuler,D., Seielstad,M., Wong,T.Y., Tai,E.S.,
            Feranil,A.B., Kuzawa,C.W., Adair,L.S., Taylor,H.A. Jr.,
            Borecki,I.B., Gabriel,S.B., Wilson,J.G., Holm,H.,
            Thorsteinsdottir,U., Gudnason,V., Krauss,R.M., Mohlke,K.L.,
            Ordovas,J.M., Munroe,P.B., Kooner,J.S., Tall,A.R., Hegele,R.A.,
            Kastelein,J.J., Schadt,E.E., Rotter,J.I., Boerwinkle,E.,
            Strachan,D.P., Mooser,V., Stefansson,K., Reilly,M.P., Samani,N.J.,
            Schunkert,H., Cupples,L.A., Sandhu,M.S., Ridker,P.M., Rader,D.J.,
            van Duijn,C.M., Peltonen,L., Abecasis,G.R., Boehnke,M. and
            Kathiresan,S.
  TITLE     Biological, clinical and population relevance of 95 loci for blood
            lipids
  JOURNAL   Nature 466 (7307), 707-713 (2010)
   PUBMED   20686565
REFERENCE   8  (residues 1 to 614)
  AUTHORS   Stahl,E.A., Raychaudhuri,S., Remmers,E.F., Xie,G., Eyre,S.,
            Thomson,B.P., Li,Y., Kurreeman,F.A., Zhernakova,A., Hinks,A.,
            Guiducci,C., Chen,R., Alfredsson,L., Amos,C.I., Ardlie,K.G.,
            Barton,A., Bowes,J., Brouwer,E., Burtt,N.P., Catanese,J.J.,
            Coblyn,J., Coenen,M.J., Costenbader,K.H., Criswell,L.A.,
            Crusius,J.B., Cui,J., de Bakker,P.I., De Jager,P.L., Ding,B.,
            Emery,P., Flynn,E., Harrison,P., Hocking,L.J., Huizinga,T.W.,
            Kastner,D.L., Ke,X., Lee,A.T., Liu,X., Martin,P., Morgan,A.W.,
            Padyukov,L., Posthumus,M.D., Radstake,T.R., Reid,D.M.,
            Seielstad,M., Seldin,M.F., Shadick,N.A., Steer,S., Tak,P.P.,
            Thomson,W., van der Helm-van Mil,A.H., van der Horst-Bruinsma,I.E.,
            van der Schoot,C.E., van Riel,P.L., Weinblatt,M.E., Wilson,A.G.,
            Wolbink,G.J., Wordsworth,B.P., Wijmenga,C., Karlson,E.W.,
            Toes,R.E., de Vries,N., Begovich,A.B., Worthington,J.,
            Siminovitch,K.A., Gregersen,P.K., Klareskog,L. and Plenge,R.M.
  CONSRTM   BIRAC Consortium; YEAR Consortium
  TITLE     Genome-wide association study meta-analysis identifies seven new
            rheumatoid arthritis risk loci
  JOURNAL   Nat Genet 42 (6), 508-514 (2010)
   PUBMED   20453842
REFERENCE   9  (residues 1 to 614)
  AUTHORS   Xu,J., Zheng,S.L., Isaacs,S.D., Wiley,K.E., Wiklund,F., Sun,J.,
            Kader,A.K., Li,G., Purcell,L.D., Kim,S.T., Hsu,F.C., Stattin,P.,
            Hugosson,J., Adolfsson,J., Walsh,P.C., Trent,J.M., Duggan,D.,
            Carpten,J., Gronberg,H. and Isaacs,W.B.
  TITLE     Inherited genetic variant predisposes to aggressive but not
            indolent prostate cancer
  JOURNAL   Proc Natl Acad Sci U S A 107 (5), 2136-2140 (2010)
   PUBMED   20080650
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 614)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK123389.1, DA292581.1 and AW269928.1.
            
            On Mar 22, 2006 this sequence version replaced NP_078945.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK123389.1, SRR1803616.37820.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341048.9/ ENSP00000342295.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q11.2"
     Protein         1..614
                     /product="ankyrin repeat domain-containing protein 55"
                     /calculated_mol_wt=68283
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          26..55
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          27..267
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(60,62,66..67,70..72,74..75,79,82,91,93,95,99..100,
                     103..105,107..108,112,115,124,126,128,167..168,171..173,
                     175..176,180,183,192)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          60..91
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          60..89
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          93..125
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          93..124
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          126..192
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          126..157
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          130..159
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          161..190
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          194..262
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          194..223
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          230..260
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          230..255
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          236..317
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          264..295
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          264..293
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          297..326
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          319..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          354..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          454..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLD6; propagated from
                     UniProtKB/Swiss-Prot (Q3KP44.3)"
     Region          564..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP44.3)"
     CDS             1..614
                     /gene="ANKRD55"
                     /coded_by="NM_024669.3:124..1968"
                     /db_xref="CCDS:CCDS34161.1"
                     /db_xref="GeneID:79722"
                     /db_xref="HGNC:HGNC:25681"
                     /db_xref="MIM:615189"
ORIGIN      
        1 mmrqatmdfs tpsvfdqqrg dsseevdltm vyqaasngdv naltavired psileccdse
       61 gctplmhavs grqadtvkll lkmganinmq daygrtslcl atylgwlegc vsllrngakh
      121 nipdkngrlp lhaataepdm rlltvllqqs niseinhqdn egmtplhwaa fhnqpqhtqm
      181 llkkgadptl vdkdfktalh wavqsgnril csiilshhqg psiinyddes gktcvhiaaa
      241 agfsdiihel arvpecnlqa ldvddrtplh waaaagkaec vqsllelgmd snlrdinest
      301 playalycgh tacvkllsqe srteptrppp sqssrpqkke rrfnvlnqif cknkkeeqra
      361 hqkdpsrdry reedtsevnd iittfdsivg tncqeqpgdq vamvefkkkt sdnskyllpe
      421 kkplarkglp pirtqslppi tlgnnfltas hratshagls saphhmaqrs qksrseqdll
      481 nnrtgcqmll dnpwksdsnq vfsykvwtvs ssdklldrll svrpghqevs vpphlrhlhn
      541 pssgqnfqhl spnrhkirdl pftrnnlapl pdqkflsgep lrtnrvlpai psqrrhstaa
      601 eesehsanpt sden
//
LOCUS       NP_001346378             373 aa            linear   ROD 27-APR-2025
DEFINITION  probable G-protein coupled receptor 173 [Mus musculus].
ACCESSION   NP_001346378 XP_006529044
VERSION     NP_001346378.1
DBSOURCE    REFSEQ: accession NM_001359449.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 373)
  AUTHORS   He,L., Shi,H., Zhang,G., Peng,Y., Ghosh,A., Zhang,M., Hu,X.,
            Liu,C., Shao,Y., Wang,S., Chen,L., Sun,W., Su,J., Chen,X.,
            Zhang,L., Chan,Y.S., Pei,D., Tortorella,M., Guo,Y., Yan,H. and
            He,J.
  TITLE     A Novel CCK Receptor GPR173 Mediates Potentiation of GABAergic
            Inhibition
  JOURNAL   J Neurosci 43 (13), 2305-2325 (2023)
   PUBMED   36813575
  REMARK    GeneRIF: A Novel CCK Receptor GPR173 Mediates Potentiation of
            GABAergic Inhibition.
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 373)
  AUTHORS   McIlwraith,E.K., Loganathan,N. and Belsham,D.D.
  TITLE     Regulation of Gpr173 expression, a putative phoenixin receptor, by
            saturated fatty acid palmitate and endocrine-disrupting chemical
            bisphenol A through a p38-mediated mechanism in immortalized
            hypothalamic neurons
  JOURNAL   Mol Cell Endocrinol 485, 54-60 (2019)
   PUBMED   30716364
  REMARK    GeneRIF: Study reports that Gpr173 is downregulated by palmitate
            and BPA in hypothalamic neuronal cell lines and primary culture,
            both partially mediated by MAPK p38 pathway. Also, palmitate
            impairs the capacity of the GPR173 putative ligand, PNX, to
            activate signaling in hypothalamic neurons. These findings
            contribute to the understanding of how fats and endocrine
            disruptors affect reproductive function.
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Larco,D.O., Cho-Clark,M., Mani,S.K. and Wu,T.J.
  TITLE     The metabolite GnRH-(1-5) inhibits the migration of immortalized
            GnRH neurons
  JOURNAL   Endocrinology 154 (2), 783-795 (2013)
   PUBMED   23321696
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Vassilatis,D.K., Hohmann,J.G., Zeng,H., Li,F., Ranchalis,J.E.,
            Mortrud,M.T., Brown,A., Rodriguez,S.S., Weller,J.R., Wright,A.C.,
            Bergmann,J.E. and Gaitanaris,G.A.
  TITLE     The G protein-coupled receptor repertoires of human and mouse
  JOURNAL   Proc Natl Acad Sci U S A 100 (8), 4903-4908 (2003)
   PUBMED   12679517
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL731727.18 and CK627285.1.
            
            On Jan 4, 2018 this sequence version replaced XP_006529044.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR9219380.86491.1,
                                           SRR1660825.138951.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164142 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="X"
                     /map="X 68.46 cM"
     Protein         1..373
                     /product="probable G-protein coupled receptor 173"
                     /note="super conserved receptor expressed in brain 3; G
                     protein-coupled receptor SREB3"
                     /calculated_mol_wt=41381
     Site            3
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PI62.1)"
     Region          23..351
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          25..49
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI62.1)"
     Region          58..80
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI62.1)"
     Region          97..119
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI62.1)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI62.1)"
     Region          142..158
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          184..207
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            184
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PI62.1)"
     Site            189..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI62.1)"
     Region          285..307
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            288..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI62.1)"
     Region          319..344
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI62.1)"
     CDS             1..373
                     /gene="Gpr173"
                     /gene_synonym="3230401K02Rik; Sreb3"
                     /coded_by="NM_001359449.1:1005..2126"
                     /db_xref="CCDS:CCDS30475.1"
                     /db_xref="GeneID:70771"
                     /db_xref="MGI:MGI:1918021"
ORIGIN      
        1 manttgepee vsgalslpsa sayvklvllg limcvslagn ailsllvlke ralhkapyyf
       61 lldlcladgi rsaicfpfvl asvrhgsswt fsalsckiva fmavlfcfha afmlfcisvt
      121 rymaiahhrf yakrmtlwtc aavicmawtl svamafppvf dvgtykfire edqcifehry
      181 fkandtlgfm lmlavlmaat havygklllf eyrhrkmkpv qmvpaisqnw tfhgpgatgq
      241 aaanwiagfg rgpmpptllg irqnghaasr rllgmdevkg ekqlgrmfya itllflllws
      301 pyivacywrv fvkacavphr ylatavwmsf aqaavnpivc fllnkdlkkc lrthapcwgt
      361 ggapaprepy cvm
//
LOCUS       NP_660334                765 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 49 [Homo sapiens].
ACCESSION   NP_660334
VERSION     NP_660334.3
DBSOURCE    REFSEQ: accession NM_145291.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   5  (residues 1 to 765)
  AUTHORS   Jeon,B.N., Yoon,J.H., Han,D., Kim,M.K., Kim,Y., Choi,S.H., Song,J.,
            Kim,K.S., Kim,K. and Hur,M.W.
  TITLE     ZNF509S1 downregulates PUMA by inhibiting p53K382 acetylation and
            p53-DNA binding
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1860 (9), 962-972 (2017)
   PUBMED   28757384
  REMARK    GeneRIF: ZNF509S1 modulation of p53 activity.
REFERENCE   6  (residues 1 to 765)
  AUTHORS   Jeon,B.N., Kim,M.K., Yoon,J.H., Kim,M.Y., An,H., Noh,H.J.,
            Choi,W.I., Koh,D.I. and Hur,M.W.
  TITLE     Two ZNF509 (ZBTB49) isoforms induce cell-cycle arrest by activating
            transcription of p21/CDKN1A and RB upon exposure to genotoxic
            stress
  JOURNAL   Nucleic Acids Res 42 (18), 11447-11461 (2014)
   PUBMED   25245946
  REMARK    GeneRIF: Two major ZNF509 isoforms are induced by p53 and act as
            downstream executioners of cell-cycle arrest by inducing expression
            of p21 and RB.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK292551.1, BC109087.1 and CA435417.1.
            
            On Feb 24, 2009 this sequence version replaced NP_660334.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Both variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127560.1, SRR1660805.89189.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337872.9/ ENSP00000338807.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..765
                     /product="zinc finger and BTB domain-containing protein
                     49"
                     /note="zinc finger protein 509"
                     /calculated_mol_wt=84931
     Region          7..118
                     /region_name="BTB_POZ_ZBTB49"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 49 (ZBTB49); cd18233"
                     /db_xref="CDD:349542"
     Region          165..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSB9.3)"
     Region          275..294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZSB9.3)"
     Region          <384..542
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          397..417
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(402,404,406,408..409,412..413,416,430,432,436..437,
                     440..441,444,458,460,462,464..465,468..469,472)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          409..434
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          425..445
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          453..473
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          481..501
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          509..529
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(514,516,518,520..521,524..525,528,542,544,548..549,
                     552..553,556,570,572,574,576..577,580..581,584)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          537..557
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          549..574
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          565..585
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..765
                     /gene="ZBTB49"
                     /gene_synonym="ZNF509"
                     /coded_by="NM_145291.4:122..2419"
                     /db_xref="CCDS:CCDS3375.1"
                     /db_xref="GeneID:166793"
                     /db_xref="HGNC:HGNC:19883"
                     /db_xref="MIM:616238"
ORIGIN      
        1 mdpvathsch llqqlheqri qgllcdcmlv vkgvcfkahk nvlaafsqyf rslfqnsssq
       61 kndvfhldvk nvsgigqild fmytshldln qdniqvmldt aqclqvqnvl slchtflksa
      121 tvvqppgmpc nstlslqstl tpdatcvise nypphllqec sadaqqnktl deshphasps
      181 vnrhhsagei skqapdtsdg sctelpfkqp nyyyklrnfy skqyhkhaag psqervveqp
      241 fafststdlt tvesqpcavs hsecilespe hlpsnflaqp vndsaphpes datcqqpvkq
      301 mrlkkaihlk klnflksqky aeqvsepksd dgltkrlesa skntlekass qsaeekesee
      361 vvscenfnci seterpedpa aledqsqtlq sqrqyacelc gkpfkhpsnl elhkrshtge
      421 kpfecnicgk hfsqagnlqt hlrrhsgekp yiceicgkrf aasgdvqrhi iihsgekphl
      481 cdicgrgfsn fsnlkehkkt htadkvftcd ecgksfnmqr klvkhrirht gerpyscsac
      541 gkcfggsgdl rrhvrthtge kpytceicnk cftrsavlrr hkkmhckagd espdvleels
      601 qaietsdlek sqssdsfsqd tsvtlmpvsv klpvhpvens vaefdshsgg sycklrsmiq
      661 phgvsdqekl sldpgklakp qmqqtqpqay aysdvdtpag geplqadgma mirsslaald
      721 nhggdplgsr assttyrnse gqffssmtlw glamktlqne neldq
//
LOCUS       NP_001001790              51 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial import receptor subunit TOM5 homolog isoform 1 [Homo
            sapiens].
ACCESSION   NP_001001790 XP_939053 XP_939056 XP_950638 XP_950639
VERSION     NP_001001790.1
DBSOURCE    REFSEQ: accession NM_001001790.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 51)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 51)
  AUTHORS   Kato,H. and Mihara,K.
  TITLE     Identification of Tom5 and Tom6 in the preprotein translocase
            complex of human mitochondrial outer membrane
  JOURNAL   Biochem Biophys Res Commun 369 (3), 958-963 (2008)
   PUBMED   18331822
  REMARK    GeneRIF: The human counterparts of Tom5 and Tom6, together with the
            other components including Tom7, were identified in the preprotein
            translocase complex.
REFERENCE   3  (residues 1 to 51)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB451927.1, BC034247.1 and BC029423.1.
            
            On or before Jul 26, 2007 this sequence version replaced
            XP_939053.1, XP_939056.1, XP_950638.1, XP_950639.1.
            
            Transcript Variant: This variant (1) represents the shortest
            transcript and encodes the shortest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279834.3473.1,
                                           SRR1163655.670005.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000321301.7/
                                                  ENSP00000313584.6
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..51
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.2"
     Protein         1..51
                     /product="mitochondrial import receptor subunit TOM5
                     homolog isoform 1"
                     /note="mitochondrial import receptor subunit TOM5 homolog;
                     mitochondrial outer membrane protein TOM5; translocase of
                     outer mitochondrial membrane 5 homolog"
                     /calculated_mol_wt=5904
     Region          1..50
                     /region_name="Tom5"
                     /note="Mitochondrial import receptor subunit or
                     translocase; pfam10642"
                     /db_xref="CDD:431410"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q8N4H5.1)"
     Site            27..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4H5.1)"
     CDS             1..51
                     /gene="TOMM5"
                     /gene_synonym="bA613M10.3; C9orf105; Tom5"
                     /coded_by="NM_001001790.3:66..221"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43803.1"
                     /db_xref="GeneID:401505"
                     /db_xref="HGNC:HGNC:31369"
                     /db_xref="MIM:616169"
ORIGIN      
        1 mfrieglapk ldpeemkrkm redvissirn fliyvallrv tpfilkklds i
//
LOCUS       NP_055333                825 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 229 isoform 1 [Homo sapiens].
ACCESSION   NP_055333 XP_371175
VERSION     NP_055333.3
DBSOURCE    REFSEQ: accession NM_014518.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Thye,T., Vannberg,F.O., Wong,S.H., Owusu-Dabo,E., Osei,I.,
            Gyapong,J., Sirugo,G., Sisay-Joof,F., Enimil,A., Chinbuah,M.A.,
            Floyd,S., Warndorff,D.K., Sichali,L., Malema,S., Crampin,A.C.,
            Ngwira,B., Teo,Y.Y., Small,K., Rockett,K., Kwiatkowski,D.,
            Fine,P.E., Hill,P.C., Newport,M., Lienhardt,C., Adegbola,R.A.,
            Corrah,T., Ziegler,A., Morris,A.P., Meyer,C.G., Horstmann,R.D. and
            Hill,A.V.S.
  CONSRTM   African TB Genetics Consortium; Wellcome Trust Case Control
            Consortium
  TITLE     Genome-wide association analyses identifies a susceptibility locus
            for tuberculosis on chromosome 18q11.2
  JOURNAL   Nat Genet 42 (9), 739-741 (2010)
   PUBMED   20694014
  REMARK    Erratum:[Nat Genet. 2011 Oct;43(10):1040]
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Shannon,M., Hamilton,A.T., Gordon,L., Branscomb,E. and Stubbs,L.
  TITLE     Differential expansion of zinc-finger transcription factor loci in
            homologous human and mouse gene clusters
  JOURNAL   Genome Res 13 (6A), 1097-1110 (2003)
   PUBMED   12743021
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF192979.1, AC245748.2 and BM663713.1.
            
            On Mar 27, 2014 this sequence version replaced NP_055333.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.105737.1,
                                           SRR1660805.135560.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000614049.5/ ENSP00000479884.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..825
                     /product="zinc finger protein 229 isoform 1"
                     /calculated_mol_wt=93637
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJW7.4)"
     Region          33..74
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          351..371
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          375..787
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          379..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(384,386,388,390..391,394..395,398,412,414,418..419,
                     422..423,426,440,442,444,446..447,450..451,454)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          407..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          463..483
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          491..511
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          519..539
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          547..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          602..622
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(607,609,611,613..614,617..618,621,635,637,641..642,
                     645..646,649,663,665,667,669..670,673..674,677)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          630..650
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          658..678
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          686..706
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          714..734
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          742..762
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(747,749,751,753..754,757..758,761,775,777,781..782,
                     785..786,789,803,805,807,809..810,813..814,817)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          770..790
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          798..818
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..825
                     /gene="ZNF229"
                     /coded_by="NM_014518.4:430..2907"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42574.1"
                     /db_xref="GeneID:7772"
                     /db_xref="HGNC:HGNC:13022"
                     /db_xref="MIM:620827"
ORIGIN      
        1 metltsrhek ralhsqasai sqdreekims qeplsfkdva vvfteeelel ldstqrqlyq
       61 dvmqenfrnl lsvgernplg dkngkdteyi qdeelrffsh kelssckiwe evagelpgsq
      121 dcrvnlqgkd fqfsedaaph qgwegastpc fpienfldsl qgdgliglen qqfpawrair
      181 pipiqgswak afvnqlgdvq ercknldted tvykcnwddd sfcwischvd hrfpeidkpc
      241 gcnkcrkdci knsvlhrinp genglksney rngfrddadl pphprvplke klcqydefse
      301 glrhsahlnr hqrvptgeks vkslergrgv rqnthirnhp rapvgdmpyr cdvcgkgfry
      361 ksvllihqgv htgrrpykce ecgkafgrss nllvhqrvht gekpykcsec gkgfsyssvl
      421 qvhqrlhtge kpytcsecgk gfcaksalhk hqhihpgekp yscgecgkgf scsshlsshq
      481 kthtgerpyq cdkcgkgfsh nsylqahqrv hmgqhlykcn vcgksfsyss gllmhqrlht
      541 gekpykcecg ksfgrssdlh ihqrvhtgek pykcsecgkg frrnsdlhsh qrvhtgerpy
      601 vcdvcgkgfi yssdllihqr vhtgekpykc aecgkgfsys sgllihqrvh tgekpyrcqe
      661 cgkgfrctss lhkhqrvhtg kkpytcdqcg kgfsygsnlr thqrlhtgek pytccecgkg
      721 frygsgllsh krvhtgekpy rchvcgkgys qsshlqghqr vhtgekpykc eecgkgfgrn
      781 sclhvhqrvh tgekpytcgv cgkgfsytsg lrnhqrvhlg enpyk
//
LOCUS       NP_078876                226 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 204 [Homo sapiens].
ACCESSION   NP_078876
VERSION     NP_078876.2
DBSOURCE    REFSEQ: accession NM_024600.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Kearsey,J., Petit,S., De Oliveira,C. and Schweighoffer,F.
  TITLE     A novel four transmembrane spanning protein, CLP24. A hypoxically
            regulated cell junction protein
  JOURNAL   Eur J Biochem 271 (13), 2584-2592 (2004)
   PUBMED   15206924
  REMARK    GeneRIF: suggests that CLP24 is a novel, hypoxically regulated
            tetraspan adherens junction protein that modulates cell adhesion,
            paracellular permeability and angiogenesis
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Kutsenko,A.S., Gizatullin,R.Z., Al-Amin,A.N., Wang,F., Kvasha,S.M.,
            Podowski,R.M., Matushkin,Y.G., Gyanchandani,A., Muravenko,O.V.,
            Levitsky,V.G., Kolchanov,N.A., Protopopov,A.I., Kashuba,V.I.,
            Kisselev,L.L., Wasserman,W., Wahlestedt,C. and Zabarovsky,E.R.
  TITLE     NotI flanking sequences: a tool for gene discovery and verification
            of the human genome
  JOURNAL   Nucleic Acids Res 30 (14), 3163-3170 (2002)
   PUBMED   12136098
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Daniels,R.J., Peden,J.F., Lloyd,C., Horsley,S.W., Clark,K.,
            Tufarelli,C., Kearney,L., Buckle,V.J., Doggett,N.A., Flint,J. and
            Higgs,D.R.
  TITLE     Sequence, structure and pathology of the fully annotated terminal 2
            Mb of the short arm of human chromosome 16
  JOURNAL   Hum Mol Genet 10 (4), 339-352 (2001)
   PUBMED   11157797
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY676494.1 and BC105785.1.
            
            On Aug 19, 2006 this sequence version replaced NP_078876.1.
            
            Summary: C16ORF30 plays a role in cell adhesion and cellular
            permeability at adherens junctions (Kearsey et al., 2004 [PubMed
            15206924]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.76690.1, AY676494.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000566264.2/ ENSP00000454945.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..226
                     /product="transmembrane protein 204"
                     /note="claudin-like protein 24; claudin-like protein of 24
                     kDa"
                     /calculated_mol_wt=24409
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSN7.1)"
     Site            104..124
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSN7.1)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSN7.1)"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BSN7.1)"
     Site            171..191
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSN7.1)"
     CDS             1..226
                     /gene="TMEM204"
                     /gene_synonym="C16orf30; CLP24"
                     /coded_by="NM_024600.6:611..1291"
                     /db_xref="CCDS:CCDS42098.1"
                     /db_xref="GeneID:79652"
                     /db_xref="HGNC:HGNC:14158"
                     /db_xref="MIM:611002"
ORIGIN      
        1 mtvqrlvaaa vlvalvslil nnvaaftsnw vcqtledgrr rsvglwrscw lvdrtrggps
       61 pgaragqvda hdcealgwgs eaagfqesrg tvklqfdmmr acnlvataal tagqltfllg
      121 lvglpllspd apcweeamaa afqlasfvlv iglvtfyrig pytnlswscy lnigacllat
      181 laaamliwni lhkredcmap rvivisrslt arfrrgldnd yvespc
//
LOCUS       NP_036228                709 aa            linear   PRI 27-APR-2025
DEFINITION  DCC-interacting protein 13-alpha [Homo sapiens].
ACCESSION   NP_036228
VERSION     NP_036228.1
DBSOURCE    REFSEQ: accession NM_012096.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Du,Y., Duan,Y., Zhao,J., Liu,C., Zhang,Z., Zhang,J., Meng,Z.,
            Wang,X., Lau,W.B., Xie,D., Lopez,B.L., Christopher,T.A., Gao,E.,
            Koch,W.W., Liu,H., Liu,D., Ma,X.L., Gu,G. and Wang,Y.
  TITLE     Dysfunctional APPL1-Mediated Epigenetic Regulation in Diabetic
            Vascular Injury
  JOURNAL   Arterioscler Thromb Vasc Biol 43 (12), e491-e508 (2023)
   PUBMED   37795615
  REMARK    GeneRIF: Dysfunctional APPL1-Mediated Epigenetic Regulation in
            Diabetic Vascular Injury.
            Erratum:[Arterioscler Thromb Vasc Biol. 2024 May;44(5):e171. doi:
            10.1161/ATV.0000000000000171. PMID: 38657036]
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Yuan,W., Liu,W., Zhang,Y., Wang,X., Xu,C., Li,Q., Ji,P., Wang,J.,
            Feng,P., Wu,Y., Shen,H. and Wang,P.
  TITLE     Reduced APPL1 impairs osteogenic differentiation of mesenchymal
            stem cells by facilitating MGP expression to disrupt the BMP2
            pathway in osteoporosis
  JOURNAL   J Biol Chem 299 (6), 104823 (2023)
   PUBMED   37187293
  REMARK    GeneRIF: Reduced APPL1 impairs osteogenic differentiation of
            mesenchymal stem cells by facilitating MGP expression to disrupt
            the BMP2 pathway in osteoporosis.
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Yang,M., Gong,C., Song,K., Huang,N., Chen,H., Gong,H., Yang,Y.,
            Guo,S. and Xiao,H.
  TITLE     APPL1 Is a Prognostic Biomarker and Correlated with Treg Cell
            Infiltration via Oxygen-Consuming Metabolism in Renal Clear Cell
            Carcinoma
  JOURNAL   Oxid Med Cell Longev 2023, 5885203 (2023)
   PUBMED   36846720
  REMARK    GeneRIF: APPL1 Is a Prognostic Biomarker and Correlated with Treg
            Cell Infiltration via Oxygen-Consuming Metabolism in Renal Clear
            Cell Carcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Martini,C., Logan,J.M., Sorvina,A., Gordon,C., Beck,A.R., S-Y
            Ung,B., Caruso,M.C., Moore,C., Hocking,A., Johnson,I.R.D., Li,K.L.,
            Karageorgos,L., Hopkins,A.M., Esterman,A.J., Huzzell,C.,
            Brooks,R.D., Lazniewska,J., Hickey,S.M., Bader,C.,
            Parkinson-Lawrence,E., Weigert,R., Sorich,M.J., Tewari,P.,
            Martin,C., O'Toole,S., Bates,M., Ward,M., Mohammed,B., Keegan,H.,
            Watson,W., Prendergast,S., Heffernan,S., NiMhaolcatha,S.,
            O'Connor,R., Malone,V., Carter,M., Ryan,K., Brady,N., Clarke,A.,
            Sokol,F., Prabhakaran,S., Stahl,J., Klebe,S., Samaratunga,H.,
            Delahunt,B., Selemidis,S., Moretti,K.L., Butler,L.M., O'Leary,J.J.
            and Brooks,D.A.
  TITLE     Aberrant protein expression of Appl1, Sortilin and Syndecan-1
            during the biological progression of prostate cancer
  JOURNAL   Pathology 55 (1), 40-51 (2023)
   PUBMED   36089417
  REMARK    GeneRIF: Aberrant protein expression of Appl1, Sortilin and
            Syndecan-1 during the biological progression of prostate cancer.
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Zhang,Y., Liu,W., Yuan,W., Cai,Z., Ye,G., Zheng,G., Xu,C., Wang,X.,
            Zeng,C., Mi,R., Feng,P., Chen,F., Wu,Y., Shen,H. and Wang,P.
  TITLE     Impairment of APPL1/Myoferlin facilitates adipogenic
            differentiation of mesenchymal stem cells by blocking autophagy
            flux in osteoporosis
  JOURNAL   Cell Mol Life Sci 79 (9), 488 (2022)
   PUBMED   35984564
  REMARK    GeneRIF: Impairment of APPL1/Myoferlin facilitates adipogenic
            differentiation of mesenchymal stem cells by blocking autophagy
            flux in osteoporosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Miaczynska,M., Christoforidis,S., Giner,A., Shevchenko,A.,
            Uttenweiler-Joseph,S., Habermann,B., Wilm,M., Parton,R.G. and
            Zerial,M.
  TITLE     APPL proteins link Rab5 to nuclear signal transduction via an
            endosomal compartment
  JOURNAL   Cell 116 (3), 445-456 (2004)
   PUBMED   15016378
  REMARK    GeneRIF: identification of a pathway directly linking the small
            GTPase Rab5, a key regulator of endocytosis, to signal transduction
            and mitogenesis via APPL1 and APPL2, two Rab5 effectors
REFERENCE   7  (residues 1 to 709)
  AUTHORS   Yang,L., Lin,H.K., Altuwaijri,S., Xie,S., Wang,L. and Chang,C.
  TITLE     APPL suppresses androgen receptor transactivation via potentiating
            Akt activity
  JOURNAL   J Biol Chem 278 (19), 16820-16827 (2003)
   PUBMED   12621049
REFERENCE   8  (residues 1 to 709)
  AUTHORS   Liu,J., Yao,F., Wu,R., Morgan,M., Thorburn,A., Finley,R.L. Jr. and
            Chen,Y.Q.
  TITLE     Mediation of the DCC apoptotic signal by DIP13 alpha
  JOURNAL   J Biol Chem 277 (29), 26281-26285 (2002)
   PUBMED   12011067
REFERENCE   9  (residues 1 to 709)
  AUTHORS   Mitsuuchi,Y., Johnson,S.W., Sonoda,G., Tanno,S., Golemis,E.A. and
            Testa,J.R.
  TITLE     Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an
            adaptor molecule that interacts with the
            oncoprotein-serine/threonine kinase AKT2
  JOURNAL   Oncogene 18 (35), 4891-4898 (1999)
   PUBMED   10490823
REFERENCE   10 (residues 1 to 709)
  AUTHORS   Naylor,R., Knight Johnson,A. and del Gaudio,D.
  TITLE     Maturity-Onset Diabetes of the Young Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29792621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093928.2, BC028599.2 and
            AF169797.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene has been shown to be
            involved in the regulation of cell proliferation, and in the
            crosstalk between the adiponectin signalling and insulin signalling
            pathways. The encoded protein binds many other proteins, including
            RAB5A, DCC, AKT2, PIK3CA, adiponectin receptors, and proteins of
            the NuRD/MeCP1 complex. This protein is found associated with
            endosomal membranes, but can be released by EGF and translocated to
            the nucleus. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.53167.1,
                                           SRR1660805.136161.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000288266.8/ ENSP00000288266.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     Protein         1..709
                     /product="DCC-interacting protein 13-alpha"
                     /note="signaling adaptor protein DIP13alpha; adaptor
                     protein containing pH domain, PTB domain and leucine
                     zipper motif 1; AKT2 interactor; adapter protein
                     containing PH domain, PTB domain and leucine zipper motif
                     1; dip13-alpha; adaptor protein, phosphotyrosine
                     interaction, PH domain and leucine zipper containing 1"
                     /calculated_mol_wt=79533
     Region          1..428
                     /region_name="Required for RAB5A binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKG1.1)"
     Region          20..234
                     /region_name="BAR_APPL1"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Adaptor
                     protein, Phosphotyrosine interaction, PH domain and
                     Leucine zipper containing 1; cd07631"
                     /db_xref="CDD:153315"
     Site            order(20,45..46,119,121,124,130,146,149,152,154,158,173)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153315"
     Site            order(29,32..33,37,40,43..44,47,57..58,60..61,64..65,
                     67..68,71,89,186,189..190,192,197..198,200..201,204..205,
                     207..208,211..212,214..215,219,222)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153315"
     Region          252..376
                     /region_name="BAR-PH_APPL"
                     /note="Adaptor protein containing PH domain, PTB domain,
                     and Leucine zipper motif Bin1/amphiphysin/Rvs167
                     (BAR)-Pleckstrin homology (PH) domain; cd13247"
                     /db_xref="CDD:270067"
     Region          397..434
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKG1.1)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKG1.1)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UKG1.1)"
     Region          403..414
                     /region_name="F&H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKG1.1)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:17765681; propagated from
                     UniProtKB/Swiss-Prot (Q9UKG1.1)"
     Region          467..491
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKG1.1)"
     Region          490..625
                     /region_name="PTB_APPL"
                     /note="Adaptor protein containing PH domain, PTB domain,
                     and Leucine zipper motif (APPL; also called
                     DCC-interacting protein (DIP)-13alpha)
                     Phosphotyrosine-binding (PTB) domain; cd13158"
                     /db_xref="CDD:269980"
     Site            order(505,582,607)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269980"
     Site            order(571..576,589,616,620)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269980"
     Region          645..709
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKG1.1)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K3H0; propagated from
                     UniProtKB/Swiss-Prot (Q9UKG1.1)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K3H0; propagated from
                     UniProtKB/Swiss-Prot (Q9UKG1.1)"
     CDS             1..709
                     /gene="APPL1"
                     /gene_synonym="APPL; DIP13alpha; MODY14"
                     /coded_by="NM_012096.3:156..2285"
                     /db_xref="CCDS:CCDS2882.1"
                     /db_xref="GeneID:26060"
                     /db_xref="HGNC:HGNC:24035"
                     /db_xref="MIM:604299"
ORIGIN      
        1 mpgidklpie etledspqtr sllgvfeeda taisnymnql yqamhriyda qnelsaathl
       61 tskllkeyek qrfplggdde vmsstlqqfs kvidelssch avlstqlada mmfpitqfke
      121 rdlkeiltlk evfqiasndh daainrysrl skkrendkvk yevtedvyts rkkqhqtmmh
      181 yfcalntlqy kkkiallepl lgymqaqisf fkmgsenlne qleeflanig tsvqnvrrem
      241 dsdietmqqt iedlevasdp lyvpdpdptk fpvnrnltrk agylnarnkt glvsstwdrq
      301 fyftqggnlm sqargdvagg lamdidncsv mavdcedrry cfqitsfdgk kssilqaesk
      361 kdheewicti nniskqiyls enpeetaarv nqsaleavtp spsfqqrhes lrpaagqsrp
      421 ptartsssgs lgsestnlaa lsldslvapd tpiqfdiisp vcedqpgqak afgqggrrtn
      481 pfgesggstk setedsilhq lfivrflgsm evksddhpdv vyetmrqila araihnifrm
      541 teshllvtcd clklidpqtq vtrltfplpc vvlyathqen krlfgfvlrt ssgrsesnls
      601 svcyifesnn egekicdsvg lakqialhae ldrrasekqk eiervkekqq kelnkqkqie
      661 kdleeqsrli aassrpnqas segqfvvlss sqseesdlge ggkkresea
//
LOCUS       NP_001035536             747 aa            linear   PRI 27-APR-2025
DEFINITION  myotubularin-related protein 12 isoform 1 [Homo sapiens].
ACCESSION   NP_001035536
VERSION     NP_001035536.1
DBSOURCE    REFSEQ: accession NM_001040446.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 747)
  AUTHORS   St-Denis,N., Gupta,G.D., Lin,Z.Y., Gonzalez-Badillo,B., Veri,A.O.,
            Knight,J.D.R., Rajendran,D., Couzens,A.L., Currie,K.W., Tkach,J.M.,
            Cheung,S.W.T., Pelletier,L. and Gingras,A.C.
  TITLE     Phenotypic and Interaction Profiling of the Human Phosphatases
            Identifies Diverse Mitotic Regulators
  JOURNAL   Cell Rep 17 (9), 2488-2501 (2016)
   PUBMED   27880917
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Gupta,V.A., Hnia,K., Smith,L.L., Gundry,S.R., McIntire,J.E.,
            Shimazu,J., Bass,J.R., Talbot,E.A., Amoasii,L., Goldman,N.E.,
            Laporte,J. and Beggs,A.H.
  TITLE     Loss of catalytically inactive lipid phosphatase
            myotubularin-related protein 12 impairs myotubularin stability and
            promotes centronuclear myopathy in zebrafish
  JOURNAL   PLoS Genet 9 (6), e1003583 (2013)
   PUBMED   23818870
  REMARK    GeneRIF: Analysis of human XLMTM patient myotubes showed that
            mutations that disrupt the interaction between myotubularin and
            MTMR12 proteins result in reduction of both myotubularin and MTMR12
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Ritter,B.P., Angelo,G.W., Durner,M., Rossy-Fullana,E.,
            Carrion-Baralt,J., Silverman,J.M. and Bespalova,I.N.
  TITLE     Mutation screening of PDZD2, GOLPH3, and MTMR12 genes in patients
            with schizophrenia
  JOURNAL   Psychiatr Genet 22 (1), 51-52 (2012)
   PUBMED   21451436
  REMARK    GeneRIF: This study does not support the association of PDZD2,
            GOLPH3, and MTMR12 genes with schizophrenia.
REFERENCE   5  (residues 1 to 747)
  AUTHORS   Lorenzo,O., Urbe,S. and Clague,M.J.
  TITLE     Systematic analysis of myotubularins: heteromeric interactions,
            subcellular localisation and endosome related functions
  JOURNAL   J Cell Sci 119 (Pt 14), 2953-2959 (2006)
   PUBMED   16787938
REFERENCE   6  (residues 1 to 747)
  AUTHORS   Nandurkar,H.H., Layton,M., Laporte,J., Selan,C., Corcoran,L.,
            Caldwell,K.K., Mochizuki,Y., Majerus,P.W. and Mitchell,C.A.
  TITLE     Identification of myotubularin as the lipid phosphatase catalytic
            subunit associated with the 3-phosphatase adapter protein, 3-PAP
  JOURNAL   Proc Natl Acad Sci U S A 100 (15), 8660-8665 (2003)
   PUBMED   12847286
  REMARK    GeneRIF: Identification of myotubularin as the lipid phosphatase
            catalytic subunit associated with the 3-phosphatase adapter
            protein, 3-PAP.
REFERENCE   7  (residues 1 to 747)
  AUTHORS   Wishart,M.J. and Dixon,J.E.
  TITLE     PTEN and myotubularin phosphatases: from 3-phosphoinositide
            dephosphorylation to disease
  JOURNAL   Trends Cell Biol 12 (12), 579-585 (2002)
   PUBMED   12495846
  REMARK    Review article
REFERENCE   8  (residues 1 to 747)
  AUTHORS   Nandurkar,H.H., Caldwell,K.K., Whisstock,J.C., Layton,M.J.,
            Gaudet,E.A., Norris,F.A., Majerus,P.W. and Mitchell,C.A.
  TITLE     Characterization of an adapter subunit to a phosphatidylinositol
            (3)P 3-phosphatase: identification of a myotubularin-related
            protein lacking catalytic activity
  JOURNAL   Proc Natl Acad Sci U S A 98 (17), 9499-9504 (2001)
   PUBMED   11504939
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY028703.1, AC025181.8 and
            BC057393.1.
            
            Summary: Phosphatidylinositide 3-kinase-derived membrane-anchored
            phosphatidylinositides, such as phosphatidylinositol 3-phosphate
            (PtdIns(3)P), regulate diverse cellular processes. The protein
            encoded by this gene functions as an adaptor subunit in a complex
            with an active PtdIns(3)P 3-phosphatase. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jun 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.223827.1,
                                           SRR1660807.61944.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382142.8/ ENSP00000371577.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.3"
     Protein         1..747
                     /product="myotubularin-related protein 12 isoform 1"
                     /note="phosphatidylinositol-3 phosphate 3-phosphatase
                     adaptor subunit; inactive phosphatidylinositol
                     3-phosphatase 12; 3-phosphatase adapter subunit;
                     phosphatidylinositol-3-phosphate associated protein;
                     3-phosphatase adapter protein; phosphatidylinositol 3
                     phosphate 3-phosphatase adapter subunit"
                     /calculated_mol_wt=86017
     Region          26..202
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          260..462
                     /region_name="PTP-MTMR12"
                     /note="protein tyrosine phosphatase-like pseudophosphatase
                     domain of myotubularin related phosphoinositide
                     phosphatase 12; cd14594"
                     /db_xref="CDD:350442"
     Region          449..558
                     /region_name="Interaction with MTM1.
                     /evidence=ECO:0000269|PubMed:12847286"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0I1.2)"
     Region          559..687
                     /region_name="3-PAP"
                     /note="Myotubularin-associated protein; pfam12578"
                     /db_xref="CDD:463634"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0I1.2)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5FVM6; propagated from
                     UniProtKB/Swiss-Prot (Q9C0I1.2)"
     Site            716
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0I1.2)"
     CDS             1..747
                     /gene="MTMR12"
                     /gene_synonym="3-PAP; PIP3AP"
                     /coded_by="NM_001040446.3:102..2345"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34138.1"
                     /db_xref="GeneID:54545"
                     /db_xref="HGNC:HGNC:18191"
                     /db_xref="MIM:606501"
ORIGIN      
        1 mlgkgvvggg ggtkapkpsf vsyvrpeeih tnekevteke vtlhllpgeq llceastvlk
       61 yvqedscqhg vygrlvctdf kiaflgddes aldndetqfk nkvigendit lhcvdqiygv
      121 fdekkktlfg qlkkypekli ihckdlrvfq fclrytkeee vkrivsgiih htqapkllkr
      181 lflfsyataa qnntvtdpkn htvmfdtlkd wcwelertkg nmkykavsvn egykvcerlp
      241 ayfvvptplp eenvqrfqgh gipiwcwsch ngsallkmsa lpkeqddgil qiqksfldgi
      301 yktihrppye ivktedlssn flslqeiqta yskfkqlfli dnstefwdtd ikwfslless
      361 swldiirrcl kkaieitecm eaqnmnvlll eenasdlccl isslvqlmmd phcrtrigfq
      421 sliqkewvmg ghcfldrcnh lrqndkeevp vfllfldcvw qlvhqhppaf eftetyltvl
      481 sdslyipifs tfffnsphqk dtnmgregqd tqskplnllt vwdwsvqfep kaqtllknpl
      541 yvekpkldkg qrkgmrfkhq rqlslpltqs ksspkrgffr eetdhliknl lgkrisklin
      601 ssdelqdnfr efydswhsks tdyhglllph iegpeikvwa qrylrwipea qilgggqvat
      661 lskllemmee vqslqekide rhhsqqapqa eapcllrnsa rlsslfpfal lqrhsskpvl
      721 ptsgwkalgd eddlakrede fvdlgdv
//
LOCUS       NP_001351994             258 aa            linear   PRI 27-APR-2025
DEFINITION  adenosine receptor A1 isoform 2 [Homo sapiens].
ACCESSION   NP_001351994 XP_016855831
VERSION     NP_001351994.1
DBSOURCE    REFSEQ: accession NM_001365065.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Zhu,W., Hong,Y., Tong,Z., He,X., Li,Y., Wang,H., Gao,X., Song,P.,
            Zhang,X., Wu,X., Tan,Z., Huang,W., Liu,Z., Bao,Y., Ma,J., Zheng,N.,
            Xie,C., Ke,X., Zhou,W., Jia,W., Li,M., Zhong,J., Sheng,L. and Li,H.
  TITLE     Activation of hepatic adenosine A1 receptor ameliorates MASH via
            inhibiting SREBPs maturation
  JOURNAL   Cell Rep Med 5 (3), 101477 (2024)
   PUBMED   38508143
  REMARK    GeneRIF: Activation of hepatic adenosine A1 receptor ameliorates
            MASH via inhibiting SREBPs maturation.
            Erratum:[Cell Rep Med. 2024 May 21;5(5):101563. doi:
            10.1016/j.xcrm.2024.101563. PMID: 38718795]
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Tzortzini,E., Corey,R.A. and Kolocouris,A.
  TITLE     Comparative Study of Receptor-, Receptor State-, and
            Membrane-Dependent Cholesterol Binding Sites in A2A and A1
            Adenosine Receptors Using Coarse-Grained Molecular Dynamics
            Simulations
  JOURNAL   J Chem Inf Model 63 (3), 928-949 (2023)
   PUBMED   36637988
  REMARK    GeneRIF: Comparative Study of Receptor-, Receptor State-, and
            Membrane-Dependent Cholesterol Binding Sites in A2A and A1
            Adenosine Receptors Using Coarse-Grained Molecular Dynamics
            Simulations.
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Sarasola,L.I., Del Torrent,C.L., Perez-Arevalo,A., Argerich,J.,
            Casajuana-Martin,N., Chevigne,A., Fernandez-Duenas,V., Ferre,S.,
            Pardo,L. and Ciruela,F.
  TITLE     The ADORA1 mutation linked to early-onset Parkinson's disease
            alters adenosine A1-A2A receptor heteromer formation and function
  JOURNAL   Biomed Pharmacother 156, 113896 (2022)
   PUBMED   36279718
  REMARK    GeneRIF: The ADORA1 mutation linked to early-onset Parkinson's
            disease alters adenosine A1-A2A receptor heteromer formation and
            function.
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Deluigi,M., Morstein,L., Schuster,M., Klenk,C., Merklinger,L.,
            Cridge,R.R., de Zhang,L.A., Klipp,A., Vacca,S., Vaid,T.M.,
            Mittl,P.R.E., Egloff,P., Eberle,S.A., Zerbe,O., Chalmers,D.K.,
            Scott,D.J. and Pluckthun,A.
  TITLE     Crystal structure of the alpha1B-adrenergic receptor reveals
            molecular determinants of selective ligand recognition
  JOURNAL   Nat Commun 13 (1), 382 (2022)
   PUBMED   35046410
  REMARK    GeneRIF: Crystal structure of the alpha1B-adrenergic receptor
            reveals molecular determinants of selective ligand recognition.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Tian,D., Li,J., Zou,L., Lin,M., Shi,X., Hu,Y., Lang,J., Xu,L.,
            Ye,W., Li,X. and Chen,L.
  TITLE     Adenosine A1 Receptor Deficiency Aggravates Extracellular Matrix
            Accumulation in Diabetic Nephropathy through Disturbance of
            Peritubular Microenvironment
  JOURNAL   J Diabetes Res 2021, 5584871 (2021)
   PUBMED   34671682
  REMARK    GeneRIF: Adenosine A1 Receptor Deficiency Aggravates Extracellular
            Matrix Accumulation in Diabetic Nephropathy through Disturbance of
            Peritubular Microenvironment.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Townsend-Nicholson,A. and Shine,J.
  TITLE     Molecular cloning and characterisation of a human brain A1
            adenosine receptor cDNA
  JOURNAL   Brain Res Mol Brain Res 16 (3-4), 365-370 (1992)
   PUBMED   1339301
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Libert,F., Van Sande,J., Lefort,A., Czernilofsky,A., Dumont,J.E.,
            Vassart,G., Ensinger,H.A. and Mendla,K.D.
  TITLE     Cloning and functional characterization of a human A1 adenosine
            receptor
  JOURNAL   Biochem Biophys Res Commun 187 (2), 919-926 (1992)
   PUBMED   1530647
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Stiles,G.L.
  TITLE     Adenosine receptors
  JOURNAL   J Biol Chem 267 (10), 6451-6454 (1992)
   PUBMED   1551861
  REMARK    Review article
REFERENCE   9  (residues 1 to 258)
  AUTHORS   Libert,F., Passage,E., Parmentier,M., Simons,M.J., Vassart,G. and
            Mattei,M.G.
  TITLE     Chromosomal mapping of A1 and A2 adenosine receptors, VIP receptor,
            and a new subtype of serotonin receptor
  JOURNAL   Genomics 11 (1), 225-227 (1991)
   PUBMED   1662665
  REMARK    Erratum:[Genomics 1994 Sep 1;23(1):305]
REFERENCE   10 (residues 1 to 258)
  AUTHORS   Libert,F., Parmentier,M., Lefort,A., Dinsart,C., Van Sande,J.,
            Maenhaut,C., Simons,M.J., Dumont,J.E. and Vassart,G.
  TITLE     Selective amplification and cloning of four new members of the G
            protein-coupled receptor family
  JOURNAL   Science 244 (4904), 569-572 (1989)
   PUBMED   2541503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105940.2.
            
            On Jul 24, 2018 this sequence version replaced XP_016855831.1.
            
            Summary: The protein encoded by this gene is an adenosine receptor
            that belongs to the G-protein coupled receptor 1 family. There are
            3 types of adenosine receptors, each with a specific pattern of
            ligand binding and tissue distribution, and together they regulate
            a diverse set of physiologic functions. The type A1 receptors
            inhibit adenylyl cyclase, and play a role in the fertilization
            process. Animal studies also suggest a role for A1 receptors in
            kidney function and ethanol intoxication. Transcript variants with
            alternative splicing in the 5' UTR have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.74583.1,
                                           SRR7410570.115002.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..258
                     /product="adenosine receptor A1 isoform 2"
                     /calculated_mol_wt=29276
     Region          <46..231
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          58..74
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          110..133
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          165..187
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          199..224
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..258
                     /gene="ADORA1"
                     /gene_synonym="RDC7"
                     /coded_by="NM_001365065.1:670..1446"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:134"
                     /db_xref="HGNC:HGNC:262"
                     /db_xref="MIM:102775"
ORIGIN      
        1 mhlpthrale eegaplrgpw rpgvpqrgls rqlggrsshs allsprykmv vtprraavai
       61 agcwilsfvv gltpmfgwnn lsaverawaa ngsmgepvik cefekvisme ymvyfnffvw
      121 vlpplllmvl iylevfylir kqlnkkvsas sgdpqkyygk elkiakslal ilflfalswl
      181 plhilncitl fcpschkpsi ltyiaiflth gnsamnpivy afriqkfrvt flkiwndhfr
      241 cqpappided lpeerpdd
//
LOCUS       NP_997278                544 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 324B [Homo sapiens].
ACCESSION   NP_997278
VERSION     NP_997278.2
DBSOURCE    REFSEQ: accession NM_207395.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R.,
            Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H.,
            Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T.,
            Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y.,
            Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M.,
            Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H.,
            Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T.,
            Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K.,
            Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H.,
            Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M.,
            Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S.,
            Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A.,
            Hara,H., Tanase,T.O., Nomura,Y., Togiya,S., Komai,F., Hara,R.,
            Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A.,
            Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T.,
            Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S.,
            Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H.,
            Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T.,
            Sugiyama,A., Takemoto,M., Kawakami,B., Yamazaki,M., Watanabe,K.,
            Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M.,
            Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y.,
            Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N.,
            Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T.,
            Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K.,
            Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T.,
            Oyama,M., Hata,H., Watanabe,M., Komatsu,T., Mizushima-Sugano,J.,
            Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K.,
            Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R.,
            Nakai,K., Yada,T., Nakamura,Y., Ohara,O., Isogai,T. and Sugano,S.
  TITLE     Complete sequencing and characterization of 21,243 full-length
            human cDNAs
  JOURNAL   Nat Genet 36 (1), 40-45 (2004)
   PUBMED   14702039
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
REFERENCE   4  (residues 1 to 544)
  AUTHORS   Bonaldo,M.F., Lennon,G. and Soares,M.B.
  TITLE     Normalization and subtraction: two approaches to facilitate gene
            discovery
  JOURNAL   Genome Res 6 (9), 791-806 (1996)
   PUBMED   8889548
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK127750.1, BC140881.1, BM714371.1 and AC012313.7.
            
            On Jul 10, 2008 this sequence version replaced NP_997278.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127750.1, BX648711.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336614.9/ ENSP00000337473.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..544
                     /product="zinc finger protein 324B"
                     /calculated_mol_wt=60471
     Region          1..61
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          184..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AW86.1)"
     Region          259..279
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(264,266,268,270..271,274..275,278,292,294,298..299,
                     302..303,306,320,322,324,326..327,330..331,334)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <268..499
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          287..307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          315..335
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          343..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          371..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          399..419
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          427..447
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          455..475
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          483..503
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          508..544
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AW86.1)"
     CDS             1..544
                     /gene="ZNF324B"
                     /coded_by="NM_207395.3:90..1724"
                     /db_xref="CCDS:CCDS33138.1"
                     /db_xref="GeneID:388569"
                     /db_xref="HGNC:HGNC:33107"
ORIGIN      
        1 mtfedvavyf sqeewglldt aqralyrhvm lenftlvtsl glstsrprvv iqlergeepw
       61 vpsgkdmtla rntygrlnsg swsltedrdv sgewprafpd tppgmttsvf pvadachsvk
      121 slqrqpgasp sqerkptgvs viywerlllg srsdqasisl rltsplrppk ssrprektft
      181 eyrvpgrqpr tperqkpcaq evpgrafgna sdlkaasggr drrmgaawqe phrllggqep
      241 stwdelgeal hageksfecr acskvfvkss dllkhlrtht gerpyectqc gkafsqtshl
      301 tqhqrihsge tpyacpvcgk afrhssslvr hqrihtaeks frcsecgkaf shgsnlsqhr
      361 kihaggrpya caqcgrrfcr nshliqhert htgekpfvca lcgaafsqgs slflhqrvht
      421 gekpfacaqc grsfsrssnl tqhqllhtge rpfrcvdcgk gfakgavlls hrrihtgekp
      481 fvctqcgraf rerpallhhq rihttektna aapdctpgpg flqghhrkvr rggkpspvlk
      541 pakv
//
LOCUS       NP_006746                337 aa            linear   PRI 27-APR-2025
DEFINITION  transaldolase [Homo sapiens].
ACCESSION   NP_006746 XP_943790
VERSION     NP_006746.1
DBSOURCE    REFSEQ: accession NM_006755.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Grammatikopoulos,T., Hadzic,N., Foskett,P., Strautnieks,S.,
            Samyn,M., Vara,R., Dhawan,A., Hertecant,J., Al Jasmi,F., Rahman,O.,
            Deheragoda,M., Bull,L.N. and Thompson,R.J.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Liver Disease and Risk of Hepatocellular Carcinoma in Children With
            Mutations in TALDO1
  JOURNAL   Hepatol Commun 6 (3), 473-479 (2022)
   PUBMED   34677006
  REMARK    GeneRIF: Liver Disease and Risk of Hepatocellular Carcinoma in
            Children With Mutations in TALDO1.
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Alfarsi,L.H., El Ansari,R., Craze,M.L., Mohammed,O.J., Masisi,B.K.,
            Ellis,I.O., Rakha,E.A. and Green,A.R.
  TITLE     SLC1A5 co-expression with TALDO1 associates with endocrine therapy
            failure in estrogen receptor-positive breast cancer
  JOURNAL   Breast Cancer Res Treat 189 (2), 317-331 (2021)
   PUBMED   34282517
  REMARK    GeneRIF: SLC1A5 co-expression with TALDO1 associates with endocrine
            therapy failure in estrogen receptor-positive breast cancer.
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Shayota,B.J., Donti,T.R., Xiao,J., Gijavanekar,C., Kennedy,A.D.,
            Hubert,L., Rodan,L., Vanderpluym,C., Nowak,C., Bjornsson,H.T.,
            Ganetzky,R., Berry,G.T., Pappan,K.L., Sutton,V.R., Sun,Q. and
            Elsea,S.H.
  TITLE     Untargeted metabolomics as an unbiased approach to the diagnosis of
            inborn errors of metabolism of the non-oxidative branch of the
            pentose phosphate pathway
  JOURNAL   Mol Genet Metab 131 (1-2), 147-154 (2020)
   PUBMED   32828637
  REMARK    GeneRIF: Untargeted metabolomics as an unbiased approach to the
            diagnosis of inborn errors of metabolism of the non-oxidative
            branch of the pentose phosphate pathway.
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Ding,Y., Gong,C., Huang,D., Chen,R., Sui,P., Lin,K.H., Liang,G.,
            Yuan,L., Xiang,H., Chen,J., Yin,T., Alexander,P.B., Wang,Q.F.,
            Song,E.W., Li,Q.J., Wood,K.C. and Wang,X.F.
  TITLE     Synthetic lethality between HER2 and transaldolase in intrinsically
            resistant HER2-positive breast cancers
  JOURNAL   Nat Commun 9 (1), 4274 (2018)
   PUBMED   30323337
  REMARK    GeneRIF: these results pinpoint transaldolase as a novel metabolic
            enzyme possessing synthetic lethality with HER2 inhibition.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Kusuda,J., Hirai,M., Toyoda,A., Tanuma,R., Nomura-Kitabayashi,A.
            and Hashimoto,K.
  TITLE     Cloning and chromosomal localization of a paralog and a mouse
            homolog of the human transaldolase gene
  JOURNAL   Gene 209 (1-2), 13-21 (1998)
   PUBMED   9524206
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Banki,K., Eddy,R.L., Shows,T.B., Halladay,D.L., Bullrich,F.,
            Croce,C.M., Jurecic,V., Baldini,A. and Perl,A.
  TITLE     The human transaldolase gene (TALDO1) is located on chromosome 11
            at p15.4-p15.5
  JOURNAL   Genomics 45 (1), 233-238 (1997)
   PUBMED   9339383
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Kusuda,J., Hirai,M., Toyoda,A. and Hashimoto,K.
  TITLE     Localization of the human transaldolase gene (TALDO) to chromosome
            1p33-p34.1 by fluorescence in situ hybridization and PCR analysis
            of somatic cell hybirds
  JOURNAL   Genomics 40 (2), 378-381 (1997)
   PUBMED   9119412
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Banki,K., Colombo,E., Sia,F., Halladay,D., Mattson,D.H.,
            Tatum,A.H., Massa,P.T., Phillips,P.E. and Perl,A.
  TITLE     Oligodendrocyte-specific expression and autoantigenicity of
            transaldolase in multiple sclerosis
  JOURNAL   J Exp Med 180 (5), 1649-1663 (1994)
   PUBMED   7964452
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Banki,K., Halladay,D. and Perl,A.
  TITLE     Cloning and expression of the human gene for transaldolase. A novel
            highly repetitive element constitutes an integral part of the
            coding sequence
  JOURNAL   J Biol Chem 269 (4), 2847-2851 (1994)
   PUBMED   8300619
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L19437.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_943790.1.
            
            Summary: Transaldolase 1 is a key enzyme of the nonoxidative
            pentose phosphate pathway providing ribose-5-phosphate for nucleic
            acid synthesis and NADPH for lipid biosynthesis. This pathway can
            also maintain glutathione at a reduced state and thus protect
            sulfhydryl groups and cellular integrity from oxygen radicals. The
            functional gene of transaldolase 1 is located on chromosome 11 and
            a pseudogene is identified on chromosome 1 but there are
            conflicting map locations. The second and third exon of this gene
            were developed by insertion of a retrotransposable element. This
            gene is thought to be involved in multiple sclerosis. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.691487.1,
                                           SRR1163658.234642.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319006.8/ ENSP00000321259.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..337
                     /product="transaldolase"
                     /EC_number="2.2.1.2"
                     /note="glycerone transferase; dihydroxyacetone
                     transferase; testicular secretory protein Li 56"
                     /calculated_mol_wt=37409
     Region          1..10
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q93092"
                     /note="propagated from UniProtKB/Swiss-Prot (P37837.2)"
     Region          11..329
                     /region_name="PRK05269"
                     /note="transaldolase B; Provisional"
                     /db_xref="CDD:235381"
     Site            order(27,43,45..46,104,106,142,165,167,187,192)
                     /site_type="active"
                     /db_xref="CDD:188644"
     Site            order(114,292,295,299..300,306,309,313)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188644"
     Site            115
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q93092; propagated from
                     UniProtKB/Swiss-Prot (P37837.2)"
     Site            142
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188644"
     Site            219
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P37837.2)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P37837.2)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P37837.2)"
     Site            269
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P37837.2)"
     Site            286
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P37837.2)"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P37837.2)"
     CDS             1..337
                     /gene="TALDO1"
                     /gene_synonym="TAL; TAL-H; TALDOR; TALH"
                     /coded_by="NM_006755.2:19..1032"
                     /db_xref="CCDS:CCDS7712.1"
                     /db_xref="GeneID:6888"
                     /db_xref="HGNC:HGNC:11559"
                     /db_xref="MIM:602063"
ORIGIN      
        1 mssspvkrqr mesaldqlkq fttvvadtgd fhaideykpq dattnpslil aaaqmpayqe
       61 lveeaiaygr klggsqedqi knaidklfvl fgaeilkkip grvstevdar lsfdkdamva
      121 rarrlielyk eagiskdril iklsstwegi qagkeleeqh gihcnmtllf sfaqavacae
      181 agvtlispfv grildwhvan tdkksyeple dpgvksvtki ynyykkfsyk tivmgasfrn
      241 tgeikalagc dfltispkll gellqdnakl vpvlsakaaq asdlekihld eksfrwlhne
      301 dqmaveklsd girkfaadav klermlterm fnaengk
//
LOCUS       NP_001356875             521 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 12 [Homo
            sapiens].
ACCESSION   NP_001356875
VERSION     NP_001356875.1
DBSOURCE    REFSEQ: accession NM_001369946.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.112923.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..521
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 12"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=59181
     Region          233..272
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..521
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369946.1:879..2444"
                     /note="isoform 12 is encoded by transcript variant 29"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mpllelkdiv lylcdtcttl wafldifpla cqtfqkhdfc yrlasfyeaa ipemesaikk
       61 rrledskllg dlwqrlshsr kklmeifhii lnqicllpil esscdniqgf ieeflqifss
      121 llqekrflrd ydalfpvaed isllqqassv ldetrtayil qavesawegv drrkatdakd
      181 psvieepnge pngvtvtaea vsqasshpen seeeecmgaa aavgpamcgv eldslisqvk
      241 dllpdlgegf ilacleyyhy dpeqvinnil eerlaptlsq ldrnldremk pdptplltsr
      301 hnvfqndefd vfsrdsvdls rvhkgkstrk eentrsllnd kravaaqrqr yeqysvvvee
      361 vplqpgeslp yhsvyyedey ddtydgnqvg andadsddel isrrpftipq vlrtkvpreg
      421 qeeddddeed dadeeapkpd hfvqdpavlr ekaearrmaf lakkgyrhds stavagsprg
      481 hgqsrettqe rrkkeankat ranhnrrtma drkrskgmip s
//
LOCUS       NP_079048               1142 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger MYM-type protein 1 isoform a [Homo sapiens].
ACCESSION   NP_079048
VERSION     NP_079048.3
DBSOURCE    REFSEQ: accession NM_024772.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1142)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL607089.16.
            
            On Aug 26, 2006 this sequence version replaced NP_079048.2.
            
            Transcript Variant: This variant (5) differs in the 5' UTR,
            compared to variant 1. Variants 1, 4, and 5 encode the same protein
            (isoform a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.130621.1, BX537537.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359858.9/ ENSP00000352920.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..1142
                     /product="zinc finger MYM-type protein 1 isoform a"
                     /note="zinc finger, MYM domain containing 1; zinc finger
                     MYM-type protein 1; zinc finger, MYM-type 1"
                     /calculated_mol_wt=128586
     Region          131..171
                     /region_name="zf-FCS"
                     /note="MYM-type Zinc finger with FCS sequence motif;
                     pfam06467"
                     /db_xref="CDD:428958"
     Region          385..413
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SVZ6.1)"
     Region          452..531
                     /region_name="ZnF_TTF"
                     /note="zinc finger in transposases and transcription
                     factors; smart00597"
                     /db_xref="CDD:214739"
     Region          494..727
                     /region_name="DUF4371"
                     /note="Domain of unknown function (DUF4371); cl46273"
                     /db_xref="CDD:480613"
     Region          1029..1118
                     /region_name="Dimer_Tnp_hAT"
                     /note="hAT family C-terminal dimerization region;
                     pfam05699"
                     /db_xref="CDD:399013"
     CDS             1..1142
                     /gene="ZMYM1"
                     /gene_synonym="MYM"
                     /coded_by="NM_024772.5:133..3561"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS41302.1"
                     /db_xref="GeneID:79830"
                     /db_xref="HGNC:HGNC:26253"
ORIGIN      
        1 mkepllggec dkavasqlgl ldeiktepdn aqeychrqqs rtqenelkin avfsesasql
       61 tagiqlslas sgvnkmlpsv sttaiqvsca gckkilqkgq tayqrkgsaq lfcsipcite
      121 yissasspvp skrtcsncsk dilnpkdvis vqledttsck tfcslsclss yeekrkpfvt
      181 ictnsiltkc smcqktaiiq yevkyqnvkh nlcsnaclsk fhsannfimn ccencgtycy
      241 tssslshilq megqshyfns sksitaykqk pakplisvpc kplkpsdemi ettsdlgkte
      301 lfcsincfsa yskakmesss vsvvsvvhdt stellspkkd ttpvisnivs ladtdvalpi
      361 mntdvlqdtv ssvtatadvi vdlsksspse psnavassst eqpsvspsss vfsqhaigss
      421 tevqkdnmks mkisdelchp kctskvqkvk gksrsikksc cadfeclens kkdvafcysc
      481 qlfcqkyfsc gresfathgt snwkktlekf rkheksemhl kslefwreyq fcdgavsddl
      541 sihskqiegn kkylkliien ilflgkqclp lrgndqsvss vnkgnflell emrakdkgee
      601 tfrlmnsqvd fynstqiqsd iieiikteml qdivneinds safsiicdet insamkeqls
      661 icvrypqkss kailikerfl gfvdteemtg thlhrtikty lqqigvdmdk ihgqaydstt
      721 nlkikfnkia aefkkeepra lyihcyahfl dlsiirfcke vkelrsalkt lsslfnticm
      781 sgemlanfrn iyrlsqnktc kkhisqscwt vhdrtllsvi dslpeiietl eviashssnt
      841 sfadelshll tlvskfefvf clkflyrvls vtgilskelq nktidifsls skieailecl
      901 sserndvyfk tiwdgteeic qkitckgfkv ekpslqkrrk iqksvdlgns dnmffptste
      961 eqykiniyyq gldtilqnlk lcfsefdyck ikqisellfk wneplnetta khvqefykld
     1021 ediipelrfy rhyaklnfvi ddscinfvsl gclfiqhglh snipclskll yialswpits
     1081 astensfstl prlktylcnt mgqekltgpa lmaveqelvn klmeperlne ivekfisqmk
     1141 ei
//
LOCUS       NP_851313                122 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein mL52 isoform c [Homo sapiens].
ACCESSION   NP_851313
VERSION     NP_851313.1
DBSOURCE    REFSEQ: accession NM_180982.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Li,X., Wang,M., Li,S., Chen,Y., Wang,M., Wu,Z., Sun,X., Yao,L.,
            Dong,H., Song,Y. and Xu,Y.
  TITLE     HIF-1-induced mitochondrial ribosome protein L52: a mechanism for
            breast cancer cellular adaptation and metastatic initiation in
            response to hypoxia
  JOURNAL   Theranostics 11 (15), 7337-7359 (2021)
   PUBMED   34158854
  REMARK    GeneRIF: HIF-1-induced mitochondrial ribosome protein L52: a
            mechanism for breast cancer cellular adaptation and metastatic
            initiation in response to hypoxia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 122)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 122)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   9  (residues 1 to 122)
  AUTHORS   O'Brien,T.W.
  TITLE     Evolution of a protein-rich mitochondrial ribosome: implications
            for human genetic disease
  JOURNAL   Gene 286 (1), 73-79 (2002)
   PUBMED   11943462
REFERENCE   10 (residues 1 to 122)
  AUTHORS   Koc,E.C., Burkhart,W., Blackburn,K., Moyer,M.B., Schlatzer,D.M.,
            Moseley,A. and Spremulli,L.L.
  TITLE     The large subunit of the mammalian mitochondrial ribosome. Analysis
            of the complement of ribosomal proteins present
  JOURNAL   J Biol Chem 276 (47), 43958-43969 (2001)
   PUBMED   11551941
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ082981.1, BX248749.1 and
            AA282747.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein which has no
            bacterial homolog. Multiple transcript variants encoding different
            protein isoforms were identified through sequence analysis.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1,
            resulting in a shorter protein (isoform c) compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.161862.1,
                                           ERR279865.2896.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000397496.7/
                                                  ENSP00000380633.3
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..122
                     /product="large ribosomal subunit protein mL52 isoform c"
                     /note="39S ribosomal protein L52, mitochondrial; L52mt;
                     MRP-L52; mitochondrial large ribosomal subunit protein
                     mL52"
                     /calculated_mol_wt=13461
     Region          23..112
                     /region_name="MRPL52"
                     /note="Mitoribosomal protein mL52; pfam18699"
                     /db_xref="CDD:465836"
     Region          98..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TS9.2)"
     CDS             1..122
                     /gene="MRPL52"
                     /gene_synonym="mL52"
                     /coded_by="NM_180982.3:27..395"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS9575.1"
                     /db_xref="GeneID:122704"
                     /db_xref="HGNC:HGNC:16655"
                     /db_xref="MIM:611856"
ORIGIN      
        1 maalgtvlfs vrrlhcsvaa waggqwrlqq glaanpsgyg pltelpdwsy adgrpappmk
       61 gqlrrkaere tfarrvvlls qemdaglqaw qlrqqklqee qrkqenalkp kgaslksplp
      121 sq
//
LOCUS       NP_004829                361 aa            linear   PRI 27-APR-2025
DEFINITION  homer protein homolog 3 isoform 1 [Homo sapiens].
ACCESSION   NP_004829
VERSION     NP_004829.3
DBSOURCE    REFSEQ: accession NM_004838.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Chen,L., Shan,X., Wan,X., Zha,W. and Fan,R.
  TITLE     HOMER3 promotes liver hepatocellular carcinoma cancer progression
            by -upregulating EZH2 and mediating miR-361/GPNMB axis
  JOURNAL   Pathol Res Pract 254, 155150 (2024)
   PUBMED   38266459
  REMARK    GeneRIF: HOMER3 promotes liver hepatocellular carcinoma cancer
            progression by -upregulating EZH2 and mediating miR-361/GPNMB axis.
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Peixoto,A., Ferreira,D., Azevedo,R., Freitas,R., Fernandes,E.,
            Relvas-Santos,M., Gaiteiro,C., Soares,J., Cotton,S., Teixeira,B.,
            Paulo,P., Lima,L., Palmeira,C., Martins,G., Oliveira,M.J.,
            Silva,A.M.N., Santos,L.L. and Ferreira,J.A.
  TITLE     Glycoproteomics identifies HOMER3 as a potentially targetable
            biomarker triggered by hypoxia and glucose deprivation in bladder
            cancer
  JOURNAL   J Exp Clin Cancer Res 40 (1), 191 (2021)
   PUBMED   34108014
  REMARK    GeneRIF: Glycoproteomics identifies HOMER3 as a potentially
            targetable biomarker triggered by hypoxia and glucose deprivation
            in bladder cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Liu,Q., He,L., Li,S., Li,F., Deng,G., Huang,X., Yang,M., Xiao,Y.,
            Chen,X., Ouyang,Y., Chen,J., Wu,X., Wang,X., Song,L. and Lin,C.
  TITLE     HOMER3 facilitates growth factor-mediated beta-Catenin tyrosine
            phosphorylation and activation to promote metastasis in triple
            negative breast cancer
  JOURNAL   J Hematol Oncol 14 (1), 6 (2021)
   PUBMED   33407765
  REMARK    GeneRIF: HOMER3 facilitates growth factor-mediated beta-Catenin
            tyrosine phosphorylation and activation to promote metastasis in
            triple negative breast cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Ishiguro,K. and Xavier,R.
  TITLE     Homer-3 regulates activation of serum response element in T cells
            via its EVH1 domain
  JOURNAL   Blood 103 (6), 2248-2256 (2004)
   PUBMED   14645007
  REMARK    GeneRIF: Homer-3 may be involved in the regulation of SRE
            activation in T cells via interaction between its EVH1 domain and
            C/EBP beta.
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Norton,N., Williams,H.J., Williams,N.M., Spurlock,G., Zammit,S.,
            Jones,G., Jones,S., Owen,R., O'Donovan,M.C. and Owen,M.J.
  TITLE     Mutation screening of the Homer gene family and association
            analysis in schizophrenia
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 120B (1), 18-21 (2003)
   PUBMED   12815733
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Soloviev,M.M., Ciruela,F., Chan,W.Y. and McIlhinney,R.A.
  TITLE     Molecular characterisation of two structurally distinct groups of
            human homers, generated by extensive alternative splicing
  JOURNAL   J Mol Biol 295 (5), 1185-1200 (2000)
   PUBMED   10653696
REFERENCE   9  (residues 1 to 361)
  AUTHORS   Tu,J.C., Xiao,B., Yuan,J.P., Lanahan,A.A., Leoffert,K., Li,M.,
            Linden,D.J. and Worley,P.F.
  TITLE     Homer binds a novel proline-rich motif and links group 1
            metabotropic glutamate receptors with IP3 receptors
  JOURNAL   Neuron 21 (4), 717-726 (1998)
   PUBMED   9808459
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Xiao,B., Tu,J.C., Petralia,R.S., Yuan,J.P., Doan,A., Breder,C.D.,
            Ruggiero,A., Lanahan,A.A., Wenthold,R.J. and Worley,P.F.
  TITLE     Homer regulates the association of group 1 metabotropic glutamate
            receptors with multivalent complexes of homer-related, synaptic
            proteins
  JOURNAL   Neuron 21 (4), 707-716 (1998)
   PUBMED   9808458
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002985.1, BC012113.1 and
            CN284196.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 11, 2009 this sequence version replaced NP_004829.2.
            
            Summary: This gene encodes a member of the HOMER family of
            postsynaptic density scaffolding proteins that share a similar
            domain structure consisting of an N-terminal
            Enabled/vasodilator-stimulated phosphoprotein homology 1 domain
            which mediates protein-protein interactions, and a carboxy-terminal
            coiled-coil domain and two leucine zipper motifs that are involved
            in self-oligomerization. The encoded protein binds numerous other
            proteins including group I metabotropic glutamate receptors,
            inositol 1,4,5-trisphosphate receptors and amyloid precursor
            proteins and has been implicated in diverse biological functions
            such as neuronal signaling, T-cell activation and trafficking of
            amyloid beta peptides. Alternative splicing results in multiple
            transcript variants.[provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (2), termed Homer-3A01, differs in
            the 5' UTR compared to variant 1. Both variants 1 and 2 encode the
            same protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012113.1, SRR3476690.354747.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392351.8/ ENSP00000376162.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..361
                     /product="homer protein homolog 3 isoform 1"
                     /note="Homer, neuronal immediate early gene, 3; homer
                     protein homolog 3; homer homolog 3; homer scaffolding
                     protein 3"
                     /calculated_mol_wt=39705
     Region          1..80
                     /region_name="Required for interaction with NFATC2.
                     /evidence=ECO:0000269|PubMed:18218901"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Region          6..114
                     /region_name="EVH1_Homer_Vesl"
                     /note="Homer/Vesl family proteins EVH1 domain; cd01206"
                     /db_xref="CDD:269917"
     Site            order(27,73,77,92)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269917"
     Region          114..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2X5; propagated from
                     UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JP6; propagated from
                     UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Region          <166..>360
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..361
                     /gene="HOMER3"
                     /gene_synonym="HOMER-3; VESL3"
                     /coded_by="NM_004838.4:235..1320"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12391.1"
                     /db_xref="GeneID:9454"
                     /db_xref="HGNC:HGNC:17514"
                     /db_xref="MIM:604800"
ORIGIN      
        1 mstareqpif strahvfqid patkrnwipa gkhaltvsyf ydatrnvyri isiggakaii
       61 nstvtpnmtf tktsqkfgqw adsrantvyg lgfaseqhlt qfaekfqevk eaarlareks
      121 qdggeltspa lglashqvpp splvsangpg eeklfrsqsa dapgpterer lkkmlsegsv
      181 gevqweaeff alqdsnnkla galreanaaa aqwrqqleaq raeaerlrqr vaeleaqaas
      241 evtptgekeg lgqgqsleql ealvqtkdqe iqtlksqtgg prealeaaer eetqqkvqdl
      301 etrnaelehq lramerslee araererara evgraaqlld vslfelselr eglarlaeaa
      361 p
//
LOCUS       NP_776159                402 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger CCHC domain-containing protein 12 [Homo sapiens].
ACCESSION   NP_776159
VERSION     NP_776159.1
DBSOURCE    REFSEQ: accession NM_173798.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Cho,G., Lim,Y. and Golden,J.A.
  TITLE     XLMR candidate mouse gene, Zcchc12 (Sizn1) is a novel marker of
            Cajal-Retzius cells
  JOURNAL   Gene Expr Patterns 11 (3-4), 216-220 (2011)
   PUBMED   21172456
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Cho,G., Lim,Y. and Golden,J.A.
  TITLE     SUMO interaction motifs in Sizn1 are required for promyelocytic
            leukemia protein nuclear body localization and for transcriptional
            activation
  JOURNAL   J Biol Chem 284 (29), 19592-19600 (2009)
   PUBMED   19416967
  REMARK    GeneRIF: Data indicate that the SIMs in Sizn1 are required for its
            PML-NB localization and for the full transcriptional co-activation
            function in BMP signaling.
REFERENCE   8  (residues 1 to 402)
  AUTHORS   Li,H., Liu,Q., Hu,X., Feng,D., Xiang,S., He,Z., Hu,X., Zhou,J.,
            Ding,X., Zhou,C. and Zhang,J.
  TITLE     Human ZCCHC12 activates AP-1 and CREB signaling as a
            transcriptional co-activator
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 41 (7), 535-544 (2009)
   PUBMED   19578717
  REMARK    GeneRIF: ZCCHC12 enhanced the transcriptional activities of
            activator protein 1 (AP-1) and cAMP response element binding
            protein (CREB) as a coactivator
REFERENCE   9  (residues 1 to 402)
  AUTHORS   Cho,G., Bhat,S.S., Gao,J., Collins,J.S., Rogers,R.C.,
            Simensen,R.J., Schwartz,C.E., Golden,J.A. and Srivastava,A.K.
  TITLE     Evidence that SIZN1 is a candidate X-linked mental retardation gene
  JOURNAL   Am J Med Genet A 146A (20), 2644-2650 (2008)
   PUBMED   18798319
  REMARK    GeneRIF: data implicate SIZN1 as a candidate gene for X-linked
            mental retardation and/or as a neurocognitive functional modifier
REFERENCE   10 (residues 1 to 402)
  AUTHORS   Cho,G., Lim,Y., Zand,D. and Golden,J.A.
  TITLE     Sizn1 is a novel protein that functions as a transcriptional
            coactivator of bone morphogenic protein signaling
  JOURNAL   Mol Cell Biol 28 (5), 1565-1572 (2008)
   PUBMED   18160706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK122676.1 and AW002115.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a downstream effector of bone
            morphogenetic protein (BMP) signalling. This protein contains a
            zinc finger domain and functions as a transcriptional coactivator.
            Variation in this gene may be associated with X-linked cognitive
            disability. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Aug 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC031241.1, BC036572.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310164.3/ ENSP00000308921.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq24"
     Protein         1..402
                     /product="zinc finger CCHC domain-containing protein 12"
                     /note="smad-interacting zinc finger protein 1;
                     paraneoplastic Ma antigen family member 7A; zinc finger,
                     CCHC domain containing 12"
                     /calculated_mol_wt=45239
     Region          <9..212
                     /region_name="PNMA"
                     /note="pfam14893"
                     /db_xref="CDD:464357"
     Region          308..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PEW1.2)"
     CDS             1..402
                     /gene="ZCCHC12"
                     /gene_synonym="PNMA7A; SIZN; SIZN1"
                     /coded_by="NM_173798.4:474..1682"
                     /db_xref="CCDS:CCDS14574.1"
                     /db_xref="GeneID:170261"
                     /db_xref="HGNC:HGNC:27273"
                     /db_xref="MIM:300701"
ORIGIN      
        1 masiiarvgn srrlnaplpp wahsmlrslg rslgpimasm adrnmklfsg rvvpaqgeet
       61 fenwltqvng vlpdwnmsee eklkrlmktl rgparevmrv lqatnpnlsv adflramklv
      121 fgesessvta hgkffntlqa qgekaslyvi rlevqlqnai qagiiaekda nrtrlqqlll
      181 ggelsrdlrl rlkdflrmya neqerlpnfl elirmvreee dwddafikrk rpkrsesmve
      241 ravspvafqg sppivigsad cnvieiddtl ddsdedvilv esqdpplpsw gapplrdrar
      301 pqdevlvids phnsraqfps tsggsgyknn gpgemrrark rkhtircsyc geeghsketc
      361 dnesdkaqvf enliitlqel thtemersrv apgeyndfse pl
//
LOCUS       NP_006738               1042 aa            linear   PRI 27-APR-2025
DEFINITION  signal-induced proliferation-associated protein 1 [Homo sapiens].
ACCESSION   NP_006738
VERSION     NP_006738.3
DBSOURCE    REFSEQ: accession NM_006747.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Guo,L., Zhang,W., Zhang,X., Wang,J., Nie,J., Jin,X., Ma,Y.,
            Wang,S., Zhou,X., Zhang,Y., Xu,Y., Tanaka,Y., Yuan,J., Liao,X.H.,
            Gong,Y. and Su,L.
  TITLE     A novel transcription factor SIPA1: identification and verification
            in triple-negative breast cancer
  JOURNAL   Oncogene 42 (35), 2641-2654 (2023)
   PUBMED   37500797
  REMARK    GeneRIF: A novel transcription factor SIPA1: identification and
            verification in triple-negative breast cancer.
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Ma,Y., Weng,J., Wang,N., Zhang,Y., Minato,N. and Su,L.
  TITLE     A novel nuclear localization region in SIPA1 determines protein
            nuclear distribution and epirubicin-sensitivity of breast cancer
            cells
  JOURNAL   Int J Biol Macromol 180, 718-728 (2021)
   PUBMED   33753200
  REMARK    GeneRIF: A novel nuclear localization region in SIPA1 determines
            protein nuclear distribution and epirubicin-sensitivity of breast
            cancer cells.
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wang,N., Weng,J., Xia,J., Zhu,Y., Chen,Q., Hu,D., Zhang,X., Sun,R.,
            Feng,J., Minato,N., Gong,Y. and Su,L.
  TITLE     SIPA1 enhances SMAD2/3 expression to maintain stem cell features in
            breast cancer cells
  JOURNAL   Stem Cell Res 49, 102099 (2020)
   PUBMED   33296812
  REMARK    GeneRIF: SIPA1 enhances SMAD2/3 expression to maintain stem cell
            features in breast cancer cells.
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Li,J.Y., Wang,J.B., Liu,C.B., Ma,D.L. and Ma,J.H.
  TITLE     Dynamic relationship between SIPA1 gene and protein expression and
            the development of gastric cancer
  JOURNAL   Genet Mol Res 16 (1) (2017)
   PUBMED   28362978
  REMARK    GeneRIF: Study shows that SIPA1 mRNA and protein expression are
            down-regulated in gastric cancer cells and correlate with tumor
            grading, invasion and lymph node metastasis as well as higher
            expression of VEGFA. Low SIPA1 levels in gastric cancer may then
            accelerate tumor development and progression by promoting VEGFA
            expression to increase vascular density.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Takahara,T., Kasamatsu,A., Yamatoji,M., Iyoda,M., Kasama,H.,
            Saito,T., Takeuchi,S., Endo-Sakamoto,Y., Shiiba,M., Tanzawa,H. and
            Uzawa,K.
  TITLE     SIPA1 promotes invasion and migration in human oral squamous cell
            carcinoma by ITGB1 and MMP7
  JOURNAL   Exp Cell Res 352 (2), 357-363 (2017)
   PUBMED   28237246
  REMARK    GeneRIF: SIPA1 promotes oral squamous cell carcinoma metastasis by
            regulating the ITGB1 and MMP7.
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Ebrahimi,S., Wang,E., Udar,N., Arnold,E., Burbee,D., Small,K. and
            Sawicki,M.P.
  TITLE     Genomic organization and cloning of the human homologue of murine
            Sipa-1
  JOURNAL   Gene 214 (1-2), 215-221 (1998)
   PUBMED   9651531
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   Kurachi,H., Wada,Y., Tsukamoto,N., Maeda,M., Kubota,H., Hattori,M.,
            Iwai,K. and Minato,N.
  TITLE     Human SPA-1 gene product selectively expressed in lymphoid tissues
            is a specific GTPase-activating protein for Rap1 and Rap2.
            Segregate expression profiles from a rap1GAP gene product
  JOURNAL   J Biol Chem 272 (44), 28081-28088 (1997)
   PUBMED   9346962
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Wada,Y., Kubota,H., Maeda,M., Taniwaki,M., Hattori,M., Imamura,S.,
            Iwai,K. and Minato,N.
  TITLE     Mitogen-inducible SIPA1 is mapped to the conserved syntenic groups
            of chromosome 19 in mouse and chromosome 11q13.3 centromeric to
            BCL1 in human
  JOURNAL   Genomics 39 (1), 66-73 (1997)
   PUBMED   9027487
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   Minato,N.
  TITLE     [Regulatory mechanisms of lymphocyte proliferation: roles of Spa-1
            gene]
  JOURNAL   Hum Cell 9 (1), 11-16 (1996)
   PUBMED   9183624
  REMARK    Review article
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Hattori,M., Tsukamoto,N., Nur-e-Kamal,M.S., Rubinfeld,B., Iwai,K.,
            Kubota,H., Maruta,H. and Minato,N.
  TITLE     Molecular cloning of a novel mitogen-inducible nuclear protein with
            a Ran GTPase-activating domain that affects cell cycle progression
  JOURNAL   Mol Cell Biol 15 (1), 552-560 (1995)
   PUBMED   7799964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001362.5.
            
            On Sep 26, 2008 this sequence version replaced NP_006738.2.
            
            Summary: The product of this gene is a mitogen induced GTPase
            activating protein (GAP). It exhibits a specific GAP activity for
            Ras-related regulatory proteins Rap1 and Rap2, but not for Ran or
            other small GTPases. This protein may also hamper mitogen-induced
            cell cycle progression when abnormally or prematurely expressed. It
            is localized to the perinuclear region. Two alternatively spliced
            variants encoding the same isoform have been characterized to date.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110353.1, AF029789.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000534313.6/ ENSP00000436269.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..1042
                     /product="signal-induced proliferation-associated protein
                     1"
                     /note="signal-induced proliferation-associated gene 1;
                     GTPase-activating protein Spa-1; p130 SPA-1; sipa-1"
                     /calculated_mol_wt=112018
     Region          1..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FS4.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96FS4.1)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96FS4.1)"
     Region          132..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FS4.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96FS4.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96FS4.1)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96FS4.1)"
     Region          351..532
                     /region_name="Rap_GAP"
                     /note="Rap/ran-GAP; pfam02145"
                     /db_xref="CDD:460463"
     Region          687..759
                     /region_name="PDZ_SIPA1-like"
                     /note="PDZ domain of signal-induced
                     proliferation-associated protein 1 (SIPA1), and related
                     domains; cd06745"
                     /db_xref="CDD:467227"
     Site            order(697..703,709,712,741,745,748..749)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467227"
     Site            817
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96FS4.1)"
     Region          830..903
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FS4.1)"
     Site            839
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96FS4.1)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96FS4.1)"
     Region          946..980
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FS4.1)"
     Region          974..1030
                     /region_name="ZapB"
                     /note="Cell division protein ZapB; pfam06005"
                     /db_xref="CDD:428718"
     CDS             1..1042
                     /gene="SIPA1"
                     /gene_synonym="SPA1"
                     /coded_by="NM_006747.4:174..3302"
                     /db_xref="CCDS:CCDS8108.1"
                     /db_xref="GeneID:6494"
                     /db_xref="HGNC:HGNC:10885"
                     /db_xref="MIM:602180"
ORIGIN      
        1 mpmwaggvgs prrgmapast ddlfarklrq parppltpht feprpvrgpl lrsgsdagea
       61 rpptpaspra rahsheeasr paatstrlft dplallglpa eepepafppv leprwfahyd
      121 vqsllfdwap rsqgmgshse assgtlasae dqaassdllh gapgfvcelg gegelglggp
      181 asppvppalp naavsileep qnrtsaysle hadlgagyyr kyfygkehqn ffgmdeslgp
      241 vavslrreek egsgggtlhs yrvivrttql rtlrgtised alppgpprgl sprkllehva
      301 pqlspsclrl gsaspkvprt lltldeqvls fqrkvgilyc ragqgseeem ynnqeagpaf
      361 mqfltllgdv vrlkgfesyr aqldtktdst gthslyttyq dheimfhvst mlpytpnnqq
      421 qllrkrhign divtivfqep gskpfcptti rshfqhvflv vrahtpctph ttyrvavsrt
      481 qdtpafgpal pagggpfaan adfrafllak alngeqaagh arqfhamatr trqqylqdla
      541 tnevtttsld sasrfglpsl ggrrraaprg pgaelqaags lvwgvraapg arvaagaqas
      601 gpegievpcl lgisaealvl vaprdgrvvf ncacrdvlaw tfseqqldly hgrgeaitlr
      661 fdgspgqavg evvarlqlvs rgcetrelal prdgqgrlgf evdaegfvth verftfaeta
      721 glrpgarllr vcgqtlpslr peaaaqllrs apkvcvtvlp pdesgrprrs fselytlslq
      781 epsrrgapdp vqdevqgvtl lpttkqllhl clqdggsppg pgdlaeerte flhsqnslsp
      841 rsslsdeapv lpnttpdlll attakpsvps adsetpltqd rpgspsgsed kgnpapelra
      901 sflprtlslr nsisrimsea gsgtledewq aiseiastcn tileslsreg qpipesgdpk
      961 gtpksdaepe pgnlsekvsh lesmlrklqe dlqkekadra aleeevrslr hnnrrlqaes
     1021 esaatrllla skqlgsptad la
//
LOCUS       NP_075566                274 aa            linear   PRI 27-APR-2025
DEFINITION  pyrroline-5-carboxylate reductase 3 isoform 1 [Homo sapiens].
ACCESSION   NP_075566
VERSION     NP_075566.3
DBSOURCE    REFSEQ: accession NM_023078.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Zhuang,F., Huang,S. and Liu,L.
  TITLE     PYCR3 modulates mtDNA copy number to drive proliferation and
            doxorubicin resistance in triple-negative breast cancer
  JOURNAL   Int J Biochem Cell Biol 171, 106581 (2024)
   PUBMED   38642827
  REMARK    GeneRIF: PYCR3 modulates mtDNA copy number to drive proliferation
            and doxorubicin resistance in triple-negative breast cancer.
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Meeks,K.R. and Tanner,J.J.
  TITLE     Expression and kinetic characterization of PYCR3
  JOURNAL   Arch Biochem Biophys 733, 109468 (2023)
   PUBMED   36414121
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Kirin,M., Chandra,A., Charteris,D.G., Hayward,C., Campbell,S.,
            Celap,I., Bencic,G., Vatavuk,Z., Kirac,I., Richards,A.J.,
            Tenesa,A., Snead,M.P., Fleck,B.W., Singh,J., Harsum,S.,
            Maclaren,R.E., den Hollander,A.I., Dunlop,M.G., Hoyng,C.B.,
            Wright,A.F., Campbell,H., Vitart,V. and Mitry,D.
  TITLE     Genome-wide association study identifies genetic risk underlying
            primary rhegmatogenous retinal detachment
  JOURNAL   Hum Mol Genet 22 (15), 3174-3185 (2013)
   PUBMED   23585552
REFERENCE   5  (residues 1 to 274)
  AUTHORS   De Ingeniis,J., Ratnikov,B., Richardson,A.D., Scott,D.A.,
            Aza-Blanc,P., De,S.K., Kazanov,M., Pellecchia,M., Ronai,Z.,
            Osterman,A.L. and Smith,J.W.
  TITLE     Functional specialization in proline biosynthesis of melanoma
  JOURNAL   PLoS One 7 (9), e45190 (2012)
   PUBMED   23024808
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Merrill,M.J., Yeh,G.C. and Phang,J.M.
  TITLE     Purified human erythrocyte pyrroline-5-carboxylate reductase.
            Preferential oxidation of NADPH
  JOURNAL   J Biol Chem 264 (16), 9352-9358 (1989)
   PUBMED   2722838
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA629534.1, BC007993.1 and
            AC067930.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 13, 2018 this sequence version replaced NP_075566.2.
            
            Summary: This gene encodes a protein that belongs to the
            pyrroline-5-carboxylate reductase family of enzymes. Members of
            this family catalyze the final step in proline biosynthesis,
            converting pyrroline-5-carboxylate to proline. Glutamate and
            ornithine are precursors in the synthesis of proline. The protein
            encoded by this gene is a cytoplasmic enzyme involved in the
            biosynthesis of proline from ornithine. [provided by RefSeq, Aug
            2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.29245.1,
                                           SRR1803612.51706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000495276.6/ ENSP00000480945.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..274
                     /product="pyrroline-5-carboxylate reductase 3 isoform 1"
                     /EC_number="1.5.1.2"
                     /note="P5CR 3; P5C reductase 3; pyrroline-5-carboxylate
                     reductase-like"
                     /calculated_mol_wt=28532
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q53H96.3)"
     Region          7..273
                     /region_name="ProC"
                     /note="Pyrroline-5-carboxylate reductase [Amino acid
                     transport and metabolism]; COG0345"
                     /db_xref="CDD:440114"
     CDS             1..274
                     /gene="PYCR3"
                     /gene_synonym="PYCRL"
                     /coded_by="NM_023078.6:28..852"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6407.3"
                     /db_xref="GeneID:65263"
                     /db_xref="HGNC:HGNC:25846"
                     /db_xref="MIM:616408"
ORIGIN      
        1 maaaepsprr vgfvgagrma gaiaqglira gkveaqhila saptdrnlch fqalgcrtth
       61 snqevlqscl lvifatkphv lpavlaevap vvttehilvs vaagvslstl eellppntrv
      121 lrvlpnlpcv vqegaivmar grhvgssetk llqhlleacg rceevpeayv dihtglsgsg
      181 vafvcafsea laegavkmgm psslahriaa qtllgtakml lhegqhpaql rsdvctpggt
      241 tiyglhaleq gglraatmsa veaatcrake lsrk
//
LOCUS       NP_056391                957 aa            linear   PRI 27-APR-2025
DEFINITION  ERC protein 2 [Homo sapiens].
ACCESSION   NP_056391
VERSION     NP_056391.1
DBSOURCE    REFSEQ: accession NM_015576.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 957)
  AUTHORS   Cheng,P., Chen,K., Zhang,S., Mu,K.T., Liang,S. and Zhang,Y.
  TITLE     IDH1 R132C and ERC2 L309I Mutations Contribute to the Development
            of Maffucci's Syndrome
  JOURNAL   Front Endocrinol (Lausanne) 12, 763349 (2021)
   PUBMED   34790172
  REMARK    GeneRIF: IDH1 R132C and ERC2 L309I Mutations Contribute to the
            Development of Maffucci's Syndrome.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 957)
  AUTHORS   Arancibia,D., Lira,M., Cruz,Y., Barrera,D.P.,
            Montenegro-Venegas,C., Godoy,J.A., Garner,C.C., Inestrosa,N.C.,
            Gundelfinger,E.D., Zamorano,P. and Torres,V.I.
  TITLE     Serine-Arginine Protein Kinase SRPK2 Modulates the Assembly of the
            Active Zone Scaffolding Protein CAST1/ERC2
  JOURNAL   Cells 8 (11), 1333 (2019)
   PUBMED   31671734
  REMARK    GeneRIF: Serine-Arginine Protein Kinase SRPK2 Modulates the
            Assembly of the Active Zone Scaffolding Protein CAST1/ERC2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 957)
  AUTHORS   Teumer,A., Holtfreter,B., Volker,U., Petersmann,A., Nauck,M.,
            Biffar,R., Volzke,H., Kroemer,H.K., Meisel,P., Homuth,G. and
            Kocher,T.
  TITLE     Genome-wide association study of chronic periodontitis in a general
            German population
  JOURNAL   J Clin Periodontol 40 (11), 977-985 (2013)
   PUBMED   24024966
REFERENCE   4  (residues 1 to 957)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   5  (residues 1 to 957)
  AUTHORS   Curtis,D., Vine,A.E., McQuillin,A., Bass,N.J., Pereira,A.,
            Kandaswamy,R., Lawrence,J., Anjorin,A., Choudhury,K., Datta,S.R.,
            Puri,V., Krasucki,R., Pimm,J., Thirumalai,S., Quested,D. and
            Gurling,H.M.
  TITLE     Case-case genome-wide association analysis shows markers
            differentially associated with schizophrenia and bipolar disorder
            and implicates calcium channel genes
  JOURNAL   Psychiatr Genet 21 (1), 1-4 (2011)
   PUBMED   21057379
REFERENCE   6  (residues 1 to 957)
  AUTHORS   Takao-Rikitsu,E., Mochida,S., Inoue,E., Deguchi-Tawarada,M.,
            Inoue,M., Ohtsuka,T. and Takai,Y.
  TITLE     Physical and functional interaction of the active zone proteins,
            CAST, RIM1, and Bassoon, in neurotransmitter release
  JOURNAL   J Cell Biol 164 (2), 301-311 (2004)
   PUBMED   14734538
REFERENCE   7  (residues 1 to 957)
  AUTHORS   Deguchi-Tawarada,M., Inoue,E., Takao-Rikitsu,E., Inoue,M.,
            Ohtsuka,T. and Takai,Y.
  TITLE     CAST2: identification and characterization of a protein
            structurally related to the presynaptic cytomatrix protein CAST
  JOURNAL   Genes Cells 9 (1), 15-23 (2004)
   PUBMED   14723704
REFERENCE   8  (residues 1 to 957)
  AUTHORS   Ko,J., Na,M., Kim,S., Lee,J.R. and Kim,E.
  TITLE     Interaction of the ERC family of RIM-binding proteins with the
            liprin-alpha family of multidomain proteins
  JOURNAL   J Biol Chem 278 (43), 42377-42385 (2003)
   PUBMED   12923177
  REMARK    GeneRIF: In vitro results indicate that ERC2/CAST, an active
            zone-specific isoform, interacts with all of the known isoforms of
            liprin-alpha and that liprin-alpha1 associates with both ERC2 and
            ERC1b
REFERENCE   9  (residues 1 to 957)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   10 (residues 1 to 957)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098478.2, AB002376.2,
            AA826430.1 and BC060881.1.
            
            Summary: This gene encodes a protein that belongs to the
            Rab3-interacting molecule (RIM)-binding protein family. Members of
            this protein family form part of the cytomatrix at the active zone
            (CAZ) complex and function as regulators of neurotransmitter
            release. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the supported protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB002376.2, BC112391.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000288221.11/ ENSP00000288221.6
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     Protein         1..957
                     /product="ERC protein 2"
                     /note="CAZ-associated structural protein; cytomatrix
                     protein p110"
                     /calculated_mol_wt=110427
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15083.3)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PH08; propagated from
                     UniProtKB/Swiss-Prot (O15083.3)"
     Region          150..911
                     /region_name="Cast"
                     /note="RIM-binding protein of the cytomatrix active zone;
                     pfam10174"
                     /db_xref="CDD:431111"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PH08; propagated from
                     UniProtKB/Swiss-Prot (O15083.3)"
     Region          918..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15083.3)"
     CDS             1..957
                     /gene="ERC2"
                     /gene_synonym="CAST; CAST1; ELKSL; SPBC110; Spc110"
                     /coded_by="NM_015576.3:361..3234"
                     /db_xref="CCDS:CCDS46851.1"
                     /db_xref="GeneID:26059"
                     /db_xref="HGNC:HGNC:31922"
                     /db_xref="MIM:617250"
ORIGIN      
        1 mygsartitn legspsrspr lprsprlghr rtssgggggt gktlsmeniq slnaayatsg
       61 pmylsdhegv asttypkgtm tlgratnrav yggrvtamgs spniasagls htdvlsytdq
      121 hggltgsshh hhhqvpsmlr qvrdstmldl qaqlkelqre ndllrkeldi kdsklgssmn
      181 siktfwspel kkervlrkee aarmsvlkeq mrvsheenqh lqltiqalqd elrtqrdlnh
      241 llqqesgnrg aehftielte enfrrlqaeh drqakelfll rktleemelr ietqkqtlna
      301 rdesikklle mlqskglpsk sleddnertr rmaeaesqvs hlevildqke kenihlreel
      361 hrrsqlqpep aktkalqtvi emkdtkiasl ernirdlede iqmlkangvl ntedreeeik
      421 qievykshsk fmktkidqlk qelskkesel lalqtkletl snqnsdckqh ievlkeslta
      481 keqraailqt evdalrlrle ekesflnkkt kqlqdlteek gtlageirdm kdmlevkerk
      541 invlqkkien lqeqlrdkdk qltnlkdrvk slqtdssntd talatleeal sekeriierl
      601 keqrerddre rleeiesfrk enkdlkekvn alqaelteke sslidlkeha sslasaglkr
      661 dsklksleia ieqkkeecsk leaqlkkahn ieddsrmnpe fadqikqldk easyyrdecg
      721 kaqaevdrll eilkevenek ndkdkkiael esltlrhmkd qnkkvanlkh nqqlekkkna
      781 qlleevrrre dsmadnsqhl qieelmnale ktrqeldatk arlastqqsl aekeahlanl
      841 rierrkqlee ilemkqeall aaisekdani allelsaskk kktqeevmal krekdrlvhq
      901 lkqqtqnrmk lmadnydddh hhyhhhhhhh hhrspgrsqh snhrpspdqd deegiwa
//
LOCUS       NP_660215                468 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM11 [Homo sapiens].
ACCESSION   NP_660215
VERSION     NP_660215.1
DBSOURCE    REFSEQ: accession NM_145214.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Xuan,T.
  TITLE     Tripartite Motif-containing Protein 11 Silencing Inhibits
            Proliferation and Glycolysis and Promotes Apoptosis of Esophageal
            Squamous Cell Carcinoma Cells by Inactivating Signal Transduction
            and Activation of Transcription Factor 3/c-Myc Signaling
  JOURNAL   J Physiol Investig 67 (1), 37-46 (2024)
   PUBMED   38780271
  REMARK    GeneRIF: Tripartite Motif-containing Protein 11 Silencing Inhibits
            Proliferation and Glycolysis and Promotes Apoptosis of Esophageal
            Squamous Cell Carcinoma Cells by Inactivating Signal Transduction
            and Activation of Transcription Factor 3/c-Myc Signaling.
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Yu,T., Yang,X., Fu,Q., Liang,J., Wu,X., Sheng,J., Chen,Y., Xiao,L.,
            Wu,Y., Nie,D., You,X., Mai,H., Chen,K. and Hu,S.
  TITLE     TRIM11 attenuates Treg cell differentiation by p62-selective
            autophagic degradation of AIM2
  JOURNAL   Cell Rep 42 (10), 113231 (2023)
   PUBMED   37804507
  REMARK    GeneRIF: TRIM11 attenuates Treg cell differentiation by
            p62-selective autophagic degradation of AIM2.
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Liang,Z., Li,J., Zhang,G. and Chen,M.
  TITLE     TRIM11 promotes cell proliferation of non-small cell lung cancer
            through the inhibition of ferroptosis by AMPK
  JOURNAL   Clin Respir J 17 (10), 1006-1016 (2023)
   PUBMED   37604203
  REMARK    GeneRIF: TRIM11 promotes cell proliferation of non-small cell lung
            cancer through the inhibition of ferroptosis by AMPK.
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Zhang,Z.Y., Harischandra,D.S., Wang,R., Ghaisas,S., Zhao,J.Y.,
            McMonagle,T.P., Zhu,G., Lacuarta,K.D., Song,J., Trojanowski,J.Q.,
            Xu,H., Lee,V.M. and Yang,X.
  TITLE     TRIM11 protects against tauopathies and is down-regulated in
            Alzheimer's disease
  JOURNAL   Science 381 (6656), eadd6696 (2023)
   PUBMED   37499037
  REMARK    GeneRIF: TRIM11 protects against tauopathies and is down-regulated
            in Alzheimer's disease.
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Pan,Y., Yu,H. and Lu,F.
  TITLE     TRIM11 Posttranscriptionally Modulated by miR-5193 Facilitates
            Tumor Growth and Metastasis of Prostate Cancer
  JOURNAL   Technol Cancer Res Treat 22, 15330338231178639 (2023)
   PUBMED   37248611
  REMARK    GeneRIF: TRIM11 Posttranscriptionally Modulated by miR-5193
            Facilitates Tumor Growth and Metastasis of Prostate Cancer.
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Uchil,P.D., Quinlan,B.D., Chan,W.T., Luna,J.M. and Mothes,W.
  TITLE     TRIM E3 ligases interfere with early and late stages of the
            retroviral life cycle
  JOURNAL   PLoS Pathog 4 (2), e16 (2008)
   PUBMED   18248090
  REMARK    GeneRIF: Downregulation of TRIM11 and TRIM15 enhanced virus release
            suggesting that these proteins contribute to the endogenous
            restriction of retroviruses in cells.
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Ishikawa,H., Tachikawa,H., Miura,Y. and Takahashi,N.
  TITLE     TRIM11 binds to and destabilizes a key component of the
            activator-mediated cofactor complex (ARC105) through the
            ubiquitin-proteasome system
  JOURNAL   FEBS Lett 580 (20), 4784-4792 (2006)
   PUBMED   16904669
  REMARK    GeneRIF: These results suggest that TRIM11, with the
            ubiquitin-proteasome pathway, regulates ARC105 function in TGFbeta
            signaling.
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Cooper,S.T. and Hanson,I.M.
  TITLE     A screen for proteins that interact with PAX6: C-terminal mutations
            disrupt interaction with HOMER3, DNCL1 and TRIM11
  JOURNAL   BMC Genet 6, 43 (2005)
   PUBMED   16098226
  REMARK    GeneRIF: PAX6 interacts with HOMER3, DNCL1, and TRIM11. Three
            C-terminal PAX6 mutations, previously identified in patients with
            eye malformations, all reduced or abolished the interactions.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Niikura,T., Hashimoto,Y., Tajima,H., Ishizaka,M., Yamagishi,Y.,
            Kawasumi,M., Nawa,M., Terashita,K., Aiso,S. and Nishimoto,I.
  TITLE     A tripartite motif protein TRIM11 binds and destabilizes Humanin, a
            neuroprotective peptide against Alzheimer's disease-relevant
            insults
  JOURNAL   Eur J Neurosci 17 (6), 1150-1158 (2003)
   PUBMED   12670303
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL670729.19.
            
            Summary: The protein encoded by this gene is a member of the
            tripartite motif (TRIM) family. The TRIM motif includes three
            zinc-binding domains, a RING, a B-box type 1 and a B-box type 2,
            and a coiled-coil region. This protein localizes to the nucleus and
            the cytoplasm. Its function has not been identified. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC069227.1, CA916721.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000284551.11/ ENSP00000284551.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.13"
     Protein         1..468
                     /product="E3 ubiquitin-protein ligase TRIM11"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 11; RING finger
                     protein 92; RING-type E3 ubiquitin transferase TRIM11"
                     /calculated_mol_wt=52643
     Region          9..69
                     /region_name="RING-HC_TRIM7-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins, TRIM7, TRIM11 and TRIM27, and
                     similar proteins; cd16594"
                     /db_xref="CDD:438256"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96F44.2)"
     Region          90..133
                     /region_name="Bbox2_TRIM11_C-IV"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 11 (TRIM11) and similar proteins;
                     cd19766"
                     /db_xref="CDD:380824"
     Region          288..456
                     /region_name="SPRY_PRY_TRIM11"
                     /note="PRY/SPRY domain of tripartite motif-binding protein
                     11 (TRIM11), also known as RING finger protein 92 (RNF92);
                     cd15811"
                     /db_xref="CDD:293983"
     CDS             1..468
                     /gene="TRIM11"
                     /gene_synonym="BIA1; RNF92"
                     /coded_by="NM_145214.3:275..1681"
                     /db_xref="CCDS:CCDS31048.1"
                     /db_xref="GeneID:81559"
                     /db_xref="HGNC:HGNC:16281"
                     /db_xref="MIM:607868"
ORIGIN      
        1 maapdlstnl qeeatcaicl dyftdpvmtd cghnfcreci rrcwgqpegp yacpecrels
       61 pqrnlrpnrp lakmaemarr lhppspvpqg vcpahrepla afcgdelrll caacersgeh
      121 wahrvrplqd aaedlkakle kslehlrkqm qdallfqaqa detcvlwqkm vesqrqnvlg
      181 eferlrrlla eeeqqllqrl eeeelevlpr lregaahlgq qsahlaelia elegrcqlpa
      241 lgllqdikda lrrvqdvklq ppevvpmelr tvcrvpglve tlrrfrgdvt ldpdtanpel
      301 ilsedrrsvq rgdlrqalpd sperfdpgpc vlgqerftsg rhywevevgd rtswalgvcr
      361 envnrkekge lsagngfwil vflgsyynss eralaplrdp prrvgifldy eaghlsfysa
      421 tdgsllfifp eipfsgtlrp lfsplssspt pmticrpkgg sgdtlapq
//
LOCUS       NP_001139812             310 aa            linear   PRI 27-APR-2025
DEFINITION  NK1 transcription factor-related protein 2 [Homo sapiens].
ACCESSION   NP_001139812 XP_001724169 XP_372331 XP_945791
VERSION     NP_001139812.1
DBSOURCE    REFSEQ: accession NM_001146340.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Costain,G., Lionel,A.C., Ogura,L., Marshall,C.R., Scherer,S.W.,
            Silversides,C.K. and Bassett,A.S.
  TITLE     Genome-wide rare copy number variations contribute to genetic risk
            for transposition of the great arteries
  JOURNAL   Int J Cardiol 204, 115-121 (2016)
   PUBMED   26655555
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Rovescalli,A.C., Cinquanta,M., Ferrante,J., Kozak,C.A. and
            Nirenberg,M.
  TITLE     The mouse Nkx-1.2 homeobox gene: alternative RNA splicing at
            canonical and noncanonical splice sites
  JOURNAL   Proc Natl Acad Sci U S A 97 (5), 1982-1987 (2000)
   PUBMED   10681422
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445237.16 and BX092002.1.
            
            On or before Apr 9, 2009 this sequence version replaced
            XP_945791.2, XP_372331.4, XP_001724169.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            CCDS Note: This CCDS representation lacks full-length human
            transcript support. Its exon combination is therefore inferred, but
            it is supported by the full-length orthologous transcript in mouse
            (AF222444.1).
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2153733,
                              SAMEA2153932 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000451024.5/ ENSP00000451945.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..310
                     /product="NK1 transcription factor-related protein 2"
                     /note="homeobox protein SAX-1; NK1 transcription factor
                     related, locus 2"
                     /calculated_mol_wt=32250
     Region          36..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UD57.3)"
     Region          164..220
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          217..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UD57.3)"
     CDS             1..310
                     /gene="NKX1-2"
                     /gene_synonym="bB238F13.2; C10orf121; NKX-1.1; SAX1"
                     /coded_by="NM_001146340.3:93..1025"
                     /db_xref="CCDS:CCDS59221.1"
                     /db_xref="GeneID:390010"
                     /db_xref="HGNC:HGNC:31652"
                     /db_xref="MIM:621058"
ORIGIN      
        1 mlawqdggak aapshhkisf svldildpqk ftraalpavr paprearksl aeveagkdas
       61 srdpvrqlet pdaagpgagq asplegseae eeedaedprr prlreraarl lpglarspda
      121 pagalasgep cedggggpvr sppgspgspr prrrrlepnc akprrartaf tyeqlvalen
      181 kfratrylsv cerlnlalsl sltetqvkiw fqnrrtkwkk qnpgadgaaq vgggapqpga
      241 agggggggsg gspgppgtga lhfqtfpsys aanvlfpsaa sfpltaaapg spfapflgps
      301 yltpfyaprl
//
LOCUS       NP_001354452             554 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 16 [Homo sapiens].
ACCESSION   NP_001354452
VERSION     NP_001354452.1
DBSOURCE    REFSEQ: accession NM_001367523.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.214633.1,
                                           SRR1803617.69158.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..554
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 16"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=61406
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          395..>450
                     /region_name="NTF2_like"
                     /note="Nuclear transport factor 2 (NTF2-like) superfamily.
                     This family includes members of the NTF2 family,
                     Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases,
                     and the beta subunit of Ring hydroxylating dioxygenases.
                     This family is a classic example of...; cl09109"
                     /db_xref="CDD:471850"
     CDS             1..554
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367523.1:95..1759"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmepqttvvh natdgikgst escntttede dlkvrkqeii kiteqlieai nngdfeaytk
      421 icdpgltsfe pealgnlveg mdfhkfyfen rewvraadil lpaplplclc llltfssqlp
      481 tfplfdlraa lllcmlvplc pdgcrqaplk alllsskchs fcscfvavpv ttikltyflp
      541 gavayacnpn tlgg
//
LOCUS       NP_612474                376 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein GLI4 [Homo sapiens].
ACCESSION   NP_612474
VERSION     NP_612474.1
DBSOURCE    REFSEQ: accession NM_138465.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Kas,K., Wlodarska,I., Meyen,E., Van den Berghe,H. and Van de
            Ven,W.J.
  TITLE     Assignment of the gene encoding human Kruppel-related zinc finger
            protein 4 (GLI4) to 8q24.3 by fluorescent in situ hybridization
  JOURNAL   Cytogenet Cell Genet 72 (4), 297-298 (1996)
   PUBMED   8641133
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Ruppert,J.M., Kinzler,K.W., Wong,A.J., Bigner,S.H., Kao,F.T.,
            Law,M.L., Seuanez,H.N., O'Brien,S.J. and Vogelstein,B.
  TITLE     The GLI-Kruppel family of human genes
  JOURNAL   Mol Cell Biol 8 (8), 3104-3113 (1988)
   PUBMED   2850480
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI761835.1, BC014165.2 and AI829114.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014165.2, SRR1163657.330683.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340042.2/ ENSP00000345024.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..376
                     /product="zinc finger protein GLI4"
                     /note="GLI-Kruppel family member GLI4 (oncogene HKR4);
                     glioma-associated oncogene family zinc finger 4;
                     krueppel-related zinc finger protein 4"
                     /calculated_mol_wt=41014
     Region          1..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10075.2)"
     Region          <74..>182
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P10075.2)"
     Region          113..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10075.2)"
     Region          <181..343
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          185..205
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(185,188,201,205)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          213..233
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(213,216,229,233)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          241..261
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(241,244,257,261)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(246,248,250,252..253,256..257,260,274,276,280..281,
                     284..285,288,302,304,306,308..309,312..313,316)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          269..289
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          297..317
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          325..345
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          337..360
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          353..373
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..376
                     /gene="GLI4"
                     /gene_synonym="HKR4; ZNF928"
                     /coded_by="NM_138465.4:78..1208"
                     /db_xref="CCDS:CCDS6398.1"
                     /db_xref="GeneID:2738"
                     /db_xref="HGNC:HGNC:4320"
                     /db_xref="MIM:165280"
ORIGIN      
        1 maalgdiqes psvpspvsls spgtpgtqhh epqlhlhghq hgspgsspkv lsqpsdldlq
       61 dveeveigrd tfwpdsepkp eqaprspgsq apdegaggal rsllrslprr arcsagfgpe
      121 ssaerpagqp pgavpcaqpr gawrvtlvqq aaagpegape raaelgvnfg rsrqgsarga
      181 kphrceacgk sfkynslllk hqrihtgekp yachecgkrf rgwsgfiqhh rihtgekpye
      241 cgqcgrafsh sshftqhlri hngekpykcg ecgqafsqss nlvrhqrlht gekpyacsqc
      301 gkafiwssvl iehqrihtge kpyecsdcgk afrgrshffr hlrthtgekp facgacgkaf
      361 gqssqliqhq rvhyre
//
LOCUS       NP_001035492             292 aa            linear   PRI 27-APR-2025
DEFINITION  DCN1-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001035492
VERSION     NP_001035492.1
DBSOURCE    REFSEQ: accession NM_001040402.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Keuss,M.J., Thomas,Y., Mcarthur,R., Wood,N.T., Knebel,A. and
            Kurz,T.
  TITLE     Characterization of the mammalian family of DCN-type NEDD8 E3
            ligases
  JOURNAL   J Cell Sci 129 (7), 1441-1454 (2016)
   PUBMED   26906416
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Monda,J.K., Scott,D.C., Miller,D.J., Lydeard,J., King,D.,
            Harper,J.W., Bennett,E.J. and Schulman,B.A.
  TITLE     Structural conservation of distinctive N-terminal
            acetylation-dependent interactions across a family of mammalian
            NEDD8 ligation enzymes
  JOURNAL   Structure 21 (1), 42-53 (2013)
   PUBMED   23201271
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Khadka,S., Vangeloff,A.D., Zhang,C., Siddavatam,P., Heaton,N.S.,
            Wang,L., Sengupta,R., Sahasrabudhe,S., Randall,G., Gribskov,M.,
            Kuhn,R.J., Perera,R. and LaCount,D.J.
  TITLE     A physical interaction network of dengue virus and human proteins
  JOURNAL   Mol Cell Proteomics 10 (12), M111.012187 (2011)
   PUBMED   21911577
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Kurz,T., Ozlu,N., Rudolf,F., O'Rourke,S.M., Luke,B., Hofmann,K.,
            Hyman,A.A., Bowerman,B. and Peter,M.
  TITLE     The conserved protein DCN-1/Dcn1p is required for cullin
            neddylation in C. elegans and S. cerevisiae
  JOURNAL   Nature 435 (7046), 1257-1261 (2005)
   PUBMED   15988528
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK124346.1, D87466.1 and BC053897.1.
            
            Transcript Variant: This variant (1) has an alternate exon in place
            of the first exon compared to variant 3. The resulting isoform (1)
            has a shorter and distinct N-terminus compared to isoform 3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX537944.1, SRR1660803.94473.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334635.10/ ENSP00000334625.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..292
                     /product="DCN1-like protein 4 isoform 1"
                     /note="DCN1-like protein 4; DCUN1 domain-containing
                     protein 4; defective in cullin neddylation protein 1-like
                     protein 4; DCN1, defective in cullin neddylation 1, domain
                     containing 4"
                     /calculated_mol_wt=33937
     Region          43..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92564.2)"
     Region          175..285
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     CDS             1..292
                     /gene="DCUN1D4"
                     /gene_synonym="DCNL4"
                     /coded_by="NM_001040402.3:91..969"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33982.1"
                     /db_xref="GeneID:23142"
                     /db_xref="HGNC:HGNC:28998"
                     /db_xref="MIM:612977"
ORIGIN      
        1 mhsdaaavnf qlnshlstla nihkiyhtln klnltedigq ddhqtgslrs csssdcfnkv
       61 mpprkkrrpa sgddlsakks rhdsmyrkyd strikteeea fsskrclewf yeyagtddvv
      121 gpegmekfce digvepenvv mlvlawklda qnmgyftlqe wlkgmtslqc dtteklrntl
      181 dylrsflnds tnfkliyrya fdfarekdqr sldintakcm lglllgkiwp lfpvfhqfle
      241 qskykvinkd qwcnvlefsr tinldlsnyd edgawpvlld efvewykdkq ms
//
LOCUS       NP_002547                807 aa            linear   PRI 27-APR-2025
DEFINITION  oxysterol-binding protein 1 [Homo sapiens].
ACCESSION   NP_002547
VERSION     NP_002547.1
DBSOURCE    REFSEQ: accession NM_002556.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Lin,Y., Ran,L., Du,X., Yang,H. and Wu,Y.
  TITLE     Oxysterol-Binding Protein: new insights into lipid transport
            functions and human diseases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1868 (9), 159365 (2023)
   PUBMED   37455011
  REMARK    GeneRIF: Oxysterol-Binding Protein: new insights into lipid
            transport functions and human diseases.
            Review article
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 807)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 807)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 807)
  AUTHORS   Peresse,T., Kovacs,D., Subra,M., Bigay,J., Tsai,M.C., Polidori,J.,
            Gautier,R., Desrat,S., Fleuriot,L., Debayle,D., Litaudon,M.,
            Pham,V.C., Bignon,J., Antonny,B., Roussi,F. and Mesmin,B.
  TITLE     Molecular and cellular dissection of the oxysterol-binding protein
            cycle through a fluorescent inhibitor
  JOURNAL   J Biol Chem 295 (13), 4277-4288 (2020)
   PUBMED   32075908
  REMARK    GeneRIF: Molecular and cellular dissection of the oxysterol-binding
            protein cycle through a fluorescent inhibitor.
REFERENCE   6  (residues 1 to 807)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   7  (residues 1 to 807)
  AUTHORS   Moreira,E.F., Jaworski,C., Li,A. and Rodriguez,I.R.
  TITLE     Molecular and biochemical characterization of a novel
            oxysterol-binding protein (OSBP2) highly expressed in retina
  JOURNAL   J Biol Chem 276 (21), 18570-18578 (2001)
   PUBMED   11278871
REFERENCE   8  (residues 1 to 807)
  AUTHORS   Laitinen,S., Olkkonen,V.M., Ehnholm,C. and Ikonen,E.
  TITLE     Family of human oxysterol binding protein (OSBP) homologues. A
            novel member implicated in brain sterol metabolism
  JOURNAL   J Lipid Res 40 (12), 2204-2211 (1999)
   PUBMED   10588946
REFERENCE   9  (residues 1 to 807)
  AUTHORS   Ridgway,N.D., Dawson,P.A., Ho,Y.K., Brown,M.S. and Goldstein,J.L.
  TITLE     Translocation of oxysterol binding protein to Golgi apparatus
            triggered by ligand binding
  JOURNAL   J Cell Biol 116 (2), 307-319 (1992)
   PUBMED   1730758
REFERENCE   10 (residues 1 to 807)
  AUTHORS   Levanon,D., Hsieh,C.L., Francke,U., Dawson,P.A., Ridgway,N.D.,
            Brown,M.S. and Goldstein,J.L.
  TITLE     cDNA cloning of human oxysterol-binding protein and localization of
            the gene to human chromosome 11 and mouse chromosome 19
  JOURNAL   Genomics 7 (1), 65-74 (1990)
   PUBMED   1970801
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF185696.1 and AP000442.6.
            
            Summary: Oxysterol binding protein is an intracellular protein that
            is believed to transport sterols from lysosomes to the nucleus
            where the sterol down-regulates the genes for the LDL receptor,
            HMG-CoA reductase, and HMG synthetase [provided by RefSeq, Jul
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF185696.1, SRR1803617.223496.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263847.6/ ENSP00000263847.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..807
                     /product="oxysterol-binding protein 1"
                     /calculated_mol_wt=89290
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Region          61..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22059.1)"
     Region          91..189
                     /region_name="PH_OSBP_ORP4"
                     /note="Human Oxysterol binding protein and OSBP-related
                     protein 4 Pleckstrin homology (PH) domain; cd13284"
                     /db_xref="CDD:270101"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22059.1)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Region          329..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22059.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3B7Z2; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22059.1)"
     Region          358..364
                     /region_name="FFAT. /evidence=ECO:0000269|PubMed:24209621"
                     /note="propagated from UniProtKB/Swiss-Prot (P22059.1)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22059.1)"
     Region          418..796
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     Region          710..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22059.1)"
     CDS             1..807
                     /gene="OSBP"
                     /gene_synonym="OSBP1"
                     /coded_by="NM_002556.3:111..2534"
                     /db_xref="CCDS:CCDS7974.1"
                     /db_xref="GeneID:5007"
                     /db_xref="HGNC:HGNC:8503"
                     /db_xref="MIM:167040"
ORIGIN      
        1 maatelrgvv gpgpaaiaal ggggagppvv gggggrgdag pgsgaasgtv vaaaaggpgp
       61 gaggvaaagp apapptggsg gsgaggsgsa regwlfkwtn yikgyqrrwf vlsngllsyy
      121 rskaemrhtc rgtinlatan itvedscnfi isnggaqtyh lkasseverq rwvtalelak
      181 akavkmlaes desgdeesvs qtdktelqnt lrtlsskved lstcndliak hgtalqrsls
      241 eleslklpae snekikqvne ratlfritsn aminacrdfl mlaqthskkw qkslqyerdq
      301 rirleetleq lakqhnhler afrgatvlpa ntpgnvgsgk dqccsgkgdm sdeddeneff
      361 dapeiitmpe nlghkrtgsn isgassdisl deqykhqlee tkkekrtrip ykpnyslnlw
      421 simkncigke lskipmpvnf neplsmlqrl tedleyhell draakcensl eqlcyvaaft
      481 vssysttvfr tskpfnpllg etfeldrlee ngyrslceqv shhppaaahh aeskngwtlr
      541 qeikitskfr gkylsimplg tihcifhatg hhytwkkvtt tvhniivgkl widqsgeidi
      601 vnhktgdkcn lkfvpysyfs rdvarkvtge vtdpsgkvhf allgtwdekm ecfkvqpvig
      661 enggdarqrg heaeesrvml wkrnplpkna enmyyfsela ltlnawesgt aptdsrlrpd
      721 qrlmengrwd eanaekqrle ekqrlsrkkr eaeamkated gtpydpykal wferkkdpvt
      781 kelthiyrge yweckekqdw sscpdif
//
LOCUS       NP_003483                261 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 187 [Homo sapiens].
ACCESSION   NP_003483
VERSION     NP_003483.1
DBSOURCE    REFSEQ: accession NM_003492.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Hernangomez-Laderas,A., Cilleros-Portet,A., Martinez Velasco,S.,
            Mari,S., Legarda,M., Gonzalez-Garcia,B.P., Tutau,C.,
            Garcia-Santisteban,I., Irastorza,I., Fernandez-Jimenez,N. and
            Bilbao,J.R.
  TITLE     Sex bias in celiac disease: XWAS and monocyte eQTLs in women
            identify TMEM187 as a functional candidate gene
  JOURNAL   Biol Sex Differ 14 (1), 86 (2023)
   PUBMED   38072919
  REMARK    GeneRIF: Sex bias in celiac disease: XWAS and monocyte eQTLs in
            women identify TMEM187 as a functional candidate gene.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Zaghloul,H.M., Abdelshafy,S.S., Abdelaleem,E.A., Ali,H.M. and
            Khattab,R.A.M.
  TITLE     Transmembrane Protein 187 (TMEM187) and Interleukin 1 Receptor
            Associated Kinase (IRAK1) gene polymorphism association with
            rheumatoid arthritis susceptibility in Egyptian patients
  JOURNAL   Egypt J Immunol 30 (3), 171-179 (2023)
   PUBMED   37440666
  REMARK    GeneRIF: Transmembrane Protein 187 (TMEM187) and Interleukin 1
            Receptor Associated Kinase (IRAK1) gene polymorphism association
            with rheumatoid arthritis susceptibility in Egyptian patients.
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Khalifa,O., Balandraud,N., Lambert,N., Auger,I., Roudier,J.,
            Senechal,A., Genevieve,D., Picard,C., Lefranc,G., Touitou,I.,
            Mrenda,B.M., Benedito,C., Pardoux,E., Gagez,A.L., Pers,Y.M.,
            Jorgensen,C., Mahjoub,T. and Apparailly,F.
  TITLE     TMEM187-IRAK1 Polymorphisms Associated with Rheumatoid Arthritis
            Susceptibility in Tunisian and French Female Populations: Influence
            of Geographic Origin
  JOURNAL   J Immunol Res 2017, 4915950 (2017)
   PUBMED   28271077
  REMARK    GeneRIF: study investigated association between 3 polymorphisms in
            the Xq28 region containing TMEM187 and IRAK1 (rs13397, rs1059703,
            and rs1059702) with rheumatoid arthritis (RA)susceptibility;
            results replicated association of the 3 Xq28 polymorphisms with RA
            risk in Tunisian and French populations and suggested that RA
            susceptibility is associated with TMEM187-IRAK1 polymorphisms in
            women
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Denoeud,F., Kapranov,P., Ucla,C., Frankish,A., Castelo,R.,
            Drenkow,J., Lagarde,J., Alioto,T., Manzano,C., Chrast,J., Dike,S.,
            Wyss,C., Henrichsen,C.N., Holroyd,N., Dickson,M.C., Taylor,R.,
            Hance,Z., Foissac,S., Myers,R.M., Rogers,J., Hubbard,T., Harrow,J.,
            Guigo,R., Gingeras,T.R., Antonarakis,S.E. and Reymond,A.
  TITLE     Prominent use of distal 5' transcription start sites and discovery
            of a large number of additional exons in ENCODE regions
  JOURNAL   Genome Res 17 (6), 746-759 (2007)
   PUBMED   17567994
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Faranda,S., Frattini,A., Zucchi,I., Patrosso,C., Milanesi,L.,
            Montagna,C. and Vezzoni,P.
  TITLE     Characterization and fine localization of two new genes in Xq28
            using the genomic sequence/EST database screening approach
  JOURNAL   Genomics 34 (3), 323-327 (1996)
   PUBMED   8786131
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Zoppe,M., Frattini,A., Faranda,S. and Vezzoni,P.
  TITLE     The complete sequence of the host cell factor 1 (HCFC1) gene and
            its promoter: a role for YY1 transcription factor in the regulation
            of its expression
  JOURNAL   Genomics 34 (1), 85-91 (1996)
   PUBMED   8661027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52112.2 and BC008203.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene consists of two exons and encodes a multi-pass
            membrane protein. An alternatively spliced transcript variant
            encoding the same protein has been found, but its biological
            validity is not determined. [provided by RefSeq, May 2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008203.1, SRR3476690.546291.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369982.5/ ENSP00000358999.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..261
                     /product="transmembrane protein 187"
                     /calculated_mol_wt=29017
     Region          8..245
                     /region_name="TMEM187"
                     /note="TMEM187 protein family; pfam15100"
                     /db_xref="CDD:464502"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14656.1)"
     Site            43..63
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14656.1)"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14656.1)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14656.1)"
     Site            140..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14656.1)"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14656.1)"
     CDS             1..261
                     /gene="TMEM187"
                     /gene_synonym="CXorf12; DXS9878E; ITBA1"
                     /coded_by="NM_003492.3:321..1106"
                     /db_xref="CCDS:CCDS14739.1"
                     /db_xref="GeneID:8269"
                     /db_xref="HGNC:HGNC:13705"
                     /db_xref="MIM:300059"
ORIGIN      
        1 mnpewgqafv hvavagglca vavftgifds vsvqvgyehy aeapvaglpa flampfnslv
       61 nmaytllgls wlhrggamgl gprylkdvfa amallygpvq wlrlwtqwrr aavldqwltl
      121 pifawpvawc lyldrgwrpw lflslecvsl asyglallhp qgfevalgah vvaavgqalr
      181 thrhygstts atylalgvls clgfvvlklc dhqlarwrlf qcltghfwsk vcdvlqfhfa
      241 flflthfnth prfhpsggkt r
//
LOCUS       NP_032944                100 aa            linear   ROD 27-APR-2025
DEFINITION  pancreatic polypeptide prohormone precursor [Mus musculus].
ACCESSION   NP_032944
VERSION     NP_032944.1
DBSOURCE    REFSEQ: accession NM_008918.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Ortiz,J.A., Ghazalli,N., Lopez,K., Rawson,J., McCown,E.M., Oh,E.,
            Irimia,J.M., Jou,K., Mares,J., Chen,M.H., Wu,X., Zook,H.N.,
            Quijano,J.C., Erdem,N., Lizarraga,A., Kandeel,F., Fueger,P.T.,
            Thurmond,D.C. and Ku,H.T.
  TITLE     Trefoil Factor 2 Expressed by the Murine Pancreatic Acinar Cells Is
            Required for the Development of Islets and for beta-Cell Function
            During Aging
  JOURNAL   Diabetes 73 (9), 1447-1461 (2024)
   PUBMED   38905124
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Kane,E., Mak,T.C.S. and Latreille,M.
  TITLE     MicroRNA-7 regulates endocrine progenitor delamination and
            endocrine cell mass in developing pancreatic islets
  JOURNAL   iScience 27 (7), 110332 (2024)
   PUBMED   39055950
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Sun,J., Wang,Y., Fu,H., Kang,F., Song,J., Xu,M., Ning,G., Wang,J.,
            Wang,W. and Wang,Q.
  TITLE     Mettl3-Mediated m6A Methylation Controls Pancreatic Bipotent
            Progenitor Fate and Islet Formation
  JOURNAL   Diabetes 73 (2), 237-249 (2024)
   PUBMED   37963393
REFERENCE   5  (residues 1 to 100)
  AUTHORS   Zhou,Y., Liu,K., Tang,W., Zhang,Y., Sun,Y., Wu,Y., Shi,Y., Yao,Z.,
            Li,Y., Bai,R., Liang,R., Sun,P., Chang,X., Wang,S., Zhu,Y. and
            Han,X.
  TITLE     beta-Cell miRNA-503-5p Induced by Hypomethylation and Inflammation
            Promotes Insulin Resistance and beta-Cell Decompensation
  JOURNAL   Diabetes 73 (1), 57-74 (2024)
   PUBMED   37847900
REFERENCE   6  (residues 1 to 100)
  AUTHORS   Gregor,P., Millham,M.L., Feng,Y., DeCarr,L.B., McCaleb,M.L. and
            Cornfield,L.J.
  TITLE     Cloning and characterization of a novel receptor to pancreatic
            polypeptide, a member of the neuropeptide Y receptor family
  JOURNAL   FEBS Lett 381 (1-2), 58-62 (1996)
   PUBMED   8641440
REFERENCE   7  (residues 1 to 100)
  AUTHORS   Guz,Y., Montminy,M.R., Stein,R., Leonard,J., Gamer,L.W.,
            Wright,C.V. and Teitelman,G.
  TITLE     Expression of murine STF-1, a putative insulin gene transcription
            factor, in beta cells of pancreas, duodenal epithelium and
            pancreatic exocrine and endocrine progenitors during ontogeny
  JOURNAL   Development 121 (1), 11-18 (1995)
   PUBMED   7867492
REFERENCE   8  (residues 1 to 100)
  AUTHORS   Gittes,G.K. and Rutter,W.J.
  TITLE     Onset of cell-specific gene expression in the developing mouse
            pancreas
  JOURNAL   Proc Natl Acad Sci U S A 89 (3), 1128-1132 (1992)
   PUBMED   1371010
REFERENCE   9  (residues 1 to 100)
  AUTHORS   Herrera,P.L., Huarte,J., Sanvito,F., Meda,P., Orci,L. and
            Vassalli,J.D.
  TITLE     Embryogenesis of the murine endocrine pancreas; early expression of
            pancreatic polypeptide gene
  JOURNAL   Development 113 (4), 1257-1265 (1991)
   PUBMED   1811941
REFERENCE   10 (residues 1 to 100)
  AUTHORS   Yonekura,H., Nata,K., Watanabe,T., Kurashina,Y., Yamamoto,H. and
            Okamoto,H.
  TITLE     Mosaic evolution of prepropancreatic polypeptide. II. Structural
            conservation and divergence in pancreatic polypeptide gene
  JOURNAL   J Biol Chem 263 (6), 2990-2997 (1988)
   PUBMED   3343236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK131852.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131852.1, AK136736.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849378, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 65.48 cM"
     Protein         1..100
                     /product="pancreatic polypeptide prohormone precursor"
                     /note="pancreatic prohormone; pancreatic polypeptide
                     prohormone"
                     /calculated_mol_wt=7853
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3185
     mat_peptide     30..65
                     /product="Pancreatic polypeptide. /id=PRO_0000025368"
                     /note="propagated from UniProtKB/Swiss-Prot (P10601.1)"
                     /calculated_mol_wt=4335
     Region          30..65
                     /region_name="PAH"
                     /note="Pancreatic hormones / neuropeptide F / peptide YY
                     family; smart00309"
                     /db_xref="CDD:197643"
     Site            order(46,50,53,57,59..61)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238072"
     Site            order(49,53,56,60..62,64..65)
                     /site_type="active"
                     /note="receptor binding site [active]"
                     /db_xref="CDD:238072"
     Site            65
                     /site_type="amidation"
                     /note="Tyrosine amide. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P10601.1)"
     mat_peptide     69..100
                     /product="C-terminal peptide. /id=PRO_0000025369"
                     /note="propagated from UniProtKB/Swiss-Prot (P10601.1)"
                     /calculated_mol_wt=3195
     CDS             1..100
                     /gene="Ppy"
                     /gene_synonym="IGSPP; PP"
                     /coded_by="NM_008918.2:55..357"
                     /db_xref="CCDS:CCDS25486.1"
                     /db_xref="GeneID:19064"
                     /db_xref="MGI:MGI:97753"
ORIGIN      
        1 mavaycclsl flvstwvall lqplqgtwga plepmypgdy atpeqmaqye tqlrryintl
       61 trprygkrae eentgglpgv qlspctsppv glipcsapws
//
LOCUS       NP_067027                261 aa            linear   PRI 27-APR-2025
DEFINITION  enolase-phosphatase E1 isoform 1 [Homo sapiens].
ACCESSION   NP_067027
VERSION     NP_067027.1
DBSOURCE    REFSEQ: accession NM_021204.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Bu,Y., Hao,J., He,J., Li,X., Liu,Y. and Ma,L.
  TITLE     Tumor-promoting properties of enolase-phosphatase 1 in breast
            cancer via activating the NF-kappaB signaling pathway
  JOURNAL   Mol Biol Rep 50 (2), 993-1004 (2023)
   PUBMED   36378417
  REMARK    GeneRIF: Tumor-promoting properties of enolase-phosphatase 1 in
            breast cancer via activating the NF-kappaB signaling pathway.
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Wang,B., Xu,X., Liu,X., Wang,D., Zhuang,H., He,X., Han,T. and
            Hong,J.
  TITLE     Enolase-phosphatase 1 acts as an oncogenic driver in glioma
  JOURNAL   J Cell Physiol 236 (2), 1184-1194 (2021)
   PUBMED   32654229
  REMARK    GeneRIF: Enolase-phosphatase 1 acts as an oncogenic driver in
            glioma.
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Zhuang,H., Qiang,Z., Shao,X., Wang,H., Dang,Y., Wang,Z., Wu,F.,
            Wei,W. and Li,Y.
  TITLE     Integration of metabolomics and expression of enolase-phosphatase 1
            links to hepatocellular carcinoma progression
  JOURNAL   Theranostics 9 (12), 3639-3652 (2019)
   PUBMED   31281503
  REMARK    GeneRIF: Taken together, these findings illustrate that ENOPH1
            promotes hepatocellular carcinoma progression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Su,L., Yang,K., Li,S., Liu,C., Han,J., Zhang,Y. and Xu,G.
  TITLE     Enolase-phosphatase 1 as a novel potential malignant glioma
            indicator promotes cell proliferation and migration
  JOURNAL   Oncol Rep 40 (4), 2233-2241 (2018)
   PUBMED   30066900
  REMARK    GeneRIF: High ENOPH1 expression is associated with malignant
            glioma.
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Wang,H., Pang,H., Bartlam,M. and Rao,Z.
  TITLE     Crystal structure of human E1 enzyme and its complex with a
            substrate analog reveals the mechanism of its phosphatase/enolase
            activity
  JOURNAL   J Mol Biol 348 (4), 917-926 (2005)
   PUBMED   15843022
  REMARK    GeneRIF: the crystal structure of MASA and its complex with a
            substrate analog
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA067292.1, BC065815.1, AW470971.1 and AC067942.6.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.271742.1,
                                           SRR1660803.204736.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000273920.8/ ENSP00000273920.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..261
                     /product="enolase-phosphatase E1 isoform 1"
                     /EC_number="3.1.3.77"
                     /note="acireductone synthase;
                     2,3-diketo-5-methylthio-1-phosphopentane phosphatase;
                     enolase-phosphatase E1"
                     /calculated_mol_wt=28802
     Region          12..234
                     /region_name="HAD_EP"
                     /note="Enolase-phosphatase similar to human
                     enolase-phosphatase E1 and and Xanthomonas oryzae pv.
                     Oryzae enolase-phosphatase Xep; cd01629"
                     /db_xref="CDD:319768"
     Site            order(16..20,27,31..32,118,153..155,159,187,211..212,
                     216..217)
                     /site_type="active"
                     /db_xref="CDD:319768"
     CDS             1..261
                     /gene="ENOPH1"
                     /gene_synonym="E1; MASA; MST145; mtnC"
                     /coded_by="NM_021204.5:241..1026"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3594.1"
                     /db_xref="GeneID:58478"
                     /db_xref="HGNC:HGNC:24599"
ORIGIN      
        1 mvvlsvpaev tvilldiegt ttpiafvkdi lfpyieenvk eylqthweee ecqqdvsllr
       61 kqaeedahld gavpipaasg ngvddlqqmi qavvdnvcwq msldrkttal kqlqghmwra
      121 aftagrmkae ffadvvpavr kwreagmkvy iyssgsveaq kllfghsteg dilelvdghf
      181 dtkighkves esyrkiadsi gcstnnilfl tdvtreasaa eeadvhvavv vrpgnagltd
      241 dektyyslit sfselylpss t
//
LOCUS       NP_004892                616 aa            linear   PRI 27-APR-2025
DEFINITION  ectonucleoside triphosphate diphosphohydrolase 4 isoform a [Homo
            sapiens].
ACCESSION   NP_004892
VERSION     NP_004892.1
DBSOURCE    REFSEQ: accession NM_004901.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Gorelik,A., Labriola,J.M., Illes,K. and Nagar,B.
  TITLE     Crystal structure of the nucleotide-metabolizing enzyme NTPDase4
  JOURNAL   Protein Sci 29 (10), 2054-2061 (2020)
   PUBMED   32767432
  REMARK    GeneRIF: Crystal structure of the nucleotide-metabolizing enzyme
            NTPDase4.
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Avital-Shacham,M., Sharf,R. and Kleinberger,T.
  TITLE     NTPDASE4 gene products cooperate with the adenovirus E4orf4 protein
            through PP2A-dependent and -independent mechanisms and contribute
            to induction of cell death
  JOURNAL   J Virol 88 (11), 6318-6328 (2014)
   PUBMED   24672025
  REMARK    GeneRIF: NTPDASE4 gene products cooperate with the adenovirus
            E4orf4 protein through PP2A-dependent and -independent mechanisms
            and contribute to induction of cell death.
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Saito,A., Fujikura-Ouchi,Y., Ito,C., Matsuoka,H., Shimoda,K. and
            Akiyama,K.
  TITLE     An association study on polymorphisms in the PEA15, ENTPD4, and
            GAS2L1 genes and schizophrenia
  JOURNAL   Psychiatry Res 185 (1-2), 9-15 (2011)
   PUBMED   20537721
  REMARK    GeneRIF: The present study fails to provide evidence for the
            contribution of ENTPD4 genes to the etiology of schizophrenia in
            the Japanese population.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Biederbick,A., Rosser,R., Storre,J. and Elsasser,H.P.
  TITLE     The VSFASSQQ motif confers calcium sensitivity to the intracellular
            apyrase LALP70
  JOURNAL   BMC Biochem 5, 8 (2004)
   PUBMED   15200686
  REMARK    GeneRIF: The VSFASSQQ motif confers calcium sensitivity to LALP70
            during UDP cleavage.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Biederbick,A., Kosan,C., Kunz,J. and Elsasser,H.P.
  TITLE     First apyrase splice variants have different enzymatic properties
  JOURNAL   J Biol Chem 275 (25), 19018-19024 (2000)
   PUBMED   10858452
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Biederbick,A., Rose,S. and Elsasser,H.P.
  TITLE     A human intracellular apyrase-like protein, LALP70, localizes to
            lysosomal/autophagic vacuoles
  JOURNAL   J Cell Sci 112 (Pt 15), 2473-2484 (1999)
   PUBMED   10393803
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Wang,T.F. and Guidotti,G.
  TITLE     Golgi localization and functional expression of human uridine
            diphosphatase
  JOURNAL   J Biol Chem 273 (18), 11392-11399 (1998)
   PUBMED   9556635
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC341200.1, AJ131358.1,
            CN313716.1, CN313713.1 and AC104561.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the apyrase protein family.
            Apyrases are enzymes that catalyze the hydrolysis of nucleotide
            diphosphates and triphosphates in a calcium or magnesium-dependent
            manner. The encoded protein is an endo-apyrase and may play a role
            in salvaging nucleotides from lysosomes. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene, and these isoforms may differ in divalent cation
            dependence and substrate specificity. [provided by RefSeq, Sep
            2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2739600.1, AJ131358.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358689.9/ ENSP00000351520.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..616
                     /product="ectonucleoside triphosphate diphosphohydrolase 4
                     isoform a"
                     /EC_number="3.6.1.6"
                     /EC_number="3.6.1.15"
                     /EC_number="3.6.1.42"
                     /note="lysosomal apyrase-like 1; guanosine-diphosphatase
                     like protein; uridine-diphosphatase; lysosomal
                     apyrase-like protein of 70 kDa; golgi luminal UDPase;
                     Golgi UDPase"
                     /calculated_mol_wt=70125
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y227.1)"
     Region          88..544
                     /region_name="ASKHA_NBD_NTPDase4-like"
                     /note="nucleotide-binding domain (NBD) of the
                     ectonucleoside triphosphate diphosphohydrolase 4
                     (NTPDase4)-like subfamily; cd24045"
                     /db_xref="CDD:466895"
     Site            404
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:32767432; propagated from
                     UniProtKB/Swiss-Prot (Q9Y227.1)"
     Site            407
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:32767432; propagated from
                     UniProtKB/Swiss-Prot (Q9Y227.1)"
     Site            560..580
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y227.1)"
     CDS             1..616
                     /gene="ENTPD4"
                     /gene_synonym="LALP70; LAP70; LYSAL1; NTPDase-4; UDPase"
                     /coded_by="NM_004901.5:189..2039"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6041.1"
                     /db_xref="GeneID:9583"
                     /db_xref="HGNC:HGNC:14573"
                     /db_xref="MIM:607577"
ORIGIN      
        1 mgrigisclf paswhfsisp vgcprilntn lrqimvisvl aaavsllyfs vviirnkygr
       61 ltrdkkfqry larvtdieat dtnnpnvnyg ivvdcgssgs rvfvycwprh ngnphdlldi
      121 rqmrdknrkp vvmkikpgis efatspekvs dyispllnfa aehvprakhk etplyilcta
      181 gmrilpesqq kailedlltd ipvhfdflfs dshaevisgk qegvyawigi nfvlgrfehi
      241 edddeavvev nipgsessea ivrkrtagil dmggvstqia yevpktvsfa ssqqeevakn
      301 llaefnlgcd vhqtehvyrv yvatflgfgg naarqryedr ifantiqknr llgkqtgltp
      361 dmpyldpclp ldikdeiqqn gqtiylrgtg dfdlcretiq pfmnktnetq tslngvyqpp
      421 ihfqnsefyg fsefyycted vlrmggdyna akftkaakdy catkwsilre rfdrglyash
      481 adlhrlkyqc fksawmfevf hrgfsfpvny kslktalqvy dkevqwtlga ilyrtrflpl
      541 rdiqqeafra shthwrgvsf vynhylfsgc flvvllaill yllrlrrihr rtprsssaaa
      601 lwmeeglpaq napgtl
//
LOCUS       NP_001353438             478 aa            linear   PRI 27-APR-2025
DEFINITION  repulsive guidance molecule B isoform 2 [Homo sapiens].
ACCESSION   NP_001353438 XP_016864879
VERSION     NP_001353438.1
DBSOURCE    REFSEQ: accession NM_001366509.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Novak,R., Ahmad,Y.A., Timaner,M., Bitman-Lotan,E.,
            Oknin-Vaisman,A., Horwitz,R., Hartmann,O., Reissland,M., Buck,V.,
            Rosenfeldt,M., Nikomarov,D., Diefenbacher,M.E., Shaked,Y. and
            Orian,A.
  TITLE     RNF4 RGMb BMP6 axis required for osteogenic differentiation and
            cancer cell survival
  JOURNAL   Cell Death Dis 13 (9), 820 (2022)
   PUBMED   36153321
  REMARK    GeneRIF: RNF4~RGMb~BMP6 axis required for osteogenic
            differentiation and cancer cell survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Malinauskas,T., Peer,T.V., Bishop,B., Mueller,T.D. and Siebold,C.
  TITLE     Repulsive guidance molecules lock growth differentiation factor 5
            in an inhibitory complex
  JOURNAL   Proc Natl Acad Sci U S A 117 (27), 15620-15631 (2020)
   PUBMED   32576689
  REMARK    GeneRIF: Repulsive guidance molecules lock growth differentiation
            factor 5 in an inhibitory complex.
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Sekiya,T. and Takaki,S.
  TITLE     RGMB enhances the suppressive activity of the monomeric secreted
            form of CTLA-4
  JOURNAL   Sci Rep 9 (1), 6984 (2019)
   PUBMED   31061392
  REMARK    GeneRIF: RGMB enhances the suppressive activity of the monomeric
            secreted form of CTLA-4.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Li,J., Ye,L., Shi,X., Chen,J., Feng,F., Chen,Y., Xiao,Y., Shen,J.,
            Li,P., Jiang,W.G. and He,J.
  TITLE     Repulsive guidance molecule B inhibits metastasis and is associated
            with decreased mortality in non-small cell lung cancer
  JOURNAL   Oncotarget 7 (13), 15678-15689 (2016)
   PUBMED   26910889
  REMARK    GeneRIF: Our results demonstrate that RGMB is an important
            inhibitor of non-small cell lung cancer metastasis and that low
            RGMB expression is a novel predictor or a poor prognosis.
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Li,P., Li,J., Yang,R., Zhang,F., Wang,H., Chu,H., Lu,Y., Dun,S.,
            Wang,Y., Zang,W., Du,Y., Chen,X., Zhao,G. and Zhang,G.
  TITLE     Study on expression of lncRNA RGMB-AS1 and repulsive guidance
            molecule b in non-small cell lung cancer
  JOURNAL   Diagn Pathol 10, 63 (2015)
   PUBMED   26055877
  REMARK    GeneRIF: RGMB was down-regulation in non-small cell lung cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Li,J., Ye,L., Mansel,R.E. and Jiang,W.G.
  TITLE     Potential prognostic value of repulsive guidance molecules in
            breast cancer
  JOURNAL   Anticancer Res 31 (5), 1703-1711 (2011)
   PUBMED   21617229
  REMARK    GeneRIF: Reduced expression of RGMB in breast cancer was associated
            with breast cancer.
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Salyakina,D., Ma,D.Q., Jaworski,J.M., Konidari,I., Whitehead,P.L.,
            Henson,R., Martinez,D., Robinson,J.L., Sacharow,S., Wright,H.H.,
            Abramson,R.K., Gilbert,J.R., Cuccaro,M.L. and Pericak-Vance,M.A.
  TITLE     Variants in several genomic regions associated with asperger
            disorder
  JOURNAL   Autism Res 3 (6), 303-310 (2010)
   PUBMED   21182207
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Liu,X., Hashimoto,M., Horii,H., Yamaguchi,A., Naito,K. and
            Yamashita,T.
  TITLE     Repulsive guidance molecule b inhibits neurite growth and is
            increased after spinal cord injury
  JOURNAL   Biochem Biophys Res Commun 382 (4), 795-800 (2009)
   PUBMED   19324014
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Samad,T.A., Rebbapragada,A., Bell,E., Zhang,Y., Sidis,Y.,
            Jeong,S.J., Campagna,J.A., Perusini,S., Fabrizio,D.A.,
            Schneyer,A.L., Lin,H.Y., Brivanlou,A.H., Attisano,L. and Woolf,C.J.
  TITLE     DRAGON, a bone morphogenetic protein co-receptor
  JOURNAL   J Biol Chem 280 (14), 14122-14129 (2005)
   PUBMED   15671031
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Samad,T.A., Srinivasan,A., Karchewski,L.A., Jeong,S.J.,
            Campagna,J.A., Ji,R.R., Fabrizio,D.A., Zhang,Y., Lin,H.Y., Bell,E.
            and Woolf,C.J.
  TITLE     DRAGON: a member of the repulsive guidance molecule-related family
            of neuronal- and muscle-expressed membrane proteins is regulated by
            DRG11 and has neuronal adhesive properties
  JOURNAL   J Neurosci 24 (8), 2027-2036 (2004)
   PUBMED   14985445
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008522.6.
            
            On Oct 10, 2018 this sequence version replaced XP_016864879.1.
            
            Summary: RGMB is a glycosylphosphatidylinositol (GPI)-anchored
            member of the repulsive guidance molecule family (see RGMA, MIM
            607362) and contributes to the patterning of the developing nervous
            system (Samad et al., 2005 [PubMed 15671031]).[supplied by OMIM,
            Apr 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.69230.1,
                                           SRR1803614.75728.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q15"
     Protein         1..478
                     /product="repulsive guidance molecule B isoform 2"
                     /note="repulsive guidance molecule B; DRG11-responsive
                     axonal guidance and outgrowth of neurite; RGM domain
                     family, member B; repulsive guidance molecule family
                     member b"
                     /calculated_mol_wt=51794
     Region          95..262
                     /region_name="RGM_N"
                     /note="Repulsive guidance molecule (RGM) N-terminus;
                     pfam06535"
                     /db_xref="CDD:461940"
     Region          267..441
                     /region_name="RGM_C"
                     /note="Repulsive guidance molecule (RGM) C-terminus;
                     pfam06534"
                     /db_xref="CDD:461939"
     CDS             1..478
                     /gene="RGMB"
                     /gene_synonym="DRAGON"
                     /coded_by="NM_001366509.1:507..1943"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47251.1"
                     /db_xref="GeneID:285704"
                     /db_xref="HGNC:HGNC:26896"
                     /db_xref="MIM:612687"
ORIGIN      
        1 mirkkrkrsa ppgpcrshgp rpatapappp speptrpawt gmglraapss aaaaaaeveq
       61 rrspglcppp lellllllfs lgllhagdcq qpaqcriqkc ttdfvsltsh lnsavdgfds
      121 efckalraya gctqrtskac rgnlvyhsav lgisdlmsqr ncskdgptss tnpevthdpc
      181 nyhshagare hrrgdqnpps ylfcglfgdp hlrtfkdnfq tckvegawpl idnnylsvqv
      241 tnvpvvpgss atatnkitii fkahhectdq kvyqavtddl paafvdgtts ggdsdakslr
      301 iveresghyv emharyigtt vfvrqvgryl tlairmpedl amsyeesqdl qlcvngcpls
      361 eriddgqgqv sailghslpr tslvqawpgy tletantqch ekmpvkdiyf qscvfdlltt
      421 gdanftaaah saledvealh prkerwhifp ssgngtprgg sdlsvslglt clilivfl
//
LOCUS       NP_000777                509 aa            linear   PRI 27-APR-2025
DEFINITION  lanosterol 14-alpha demethylase isoform 1 [Homo sapiens].
ACCESSION   NP_000777
VERSION     NP_000777.1
DBSOURCE    REFSEQ: accession NM_000786.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Kaluzhskiy,L., Yablokov,E., Gnedenko,O., Burkatovskii,D.,
            Maslov,I., Bogorodskiy,A., Ershov,P., Tsybruk,T., Zelepuga,E.,
            Rutckova,T., Kozlovskaya,E., Dmitrenok,P., Gilep,A.,
            Borshchevskiy,V., Strushkevich,N. and Ivanov,A.
  TITLE     The effect of membrane composition on the interaction between human
            CYP51 and its flavonoid inhibitor - luteolin 7,3'-disulfate
  JOURNAL   Biochim Biophys Acta Biomembr 1866 (3), 184286 (2024)
   PUBMED   38272204
  REMARK    GeneRIF: The effect of membrane composition on the interaction
            between human CYP51 and its flavonoid inhibitor - luteolin
            7,3'-disulfate.
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Yin,J., Fu,J., Shao,Y., Xu,J., Li,H., Chen,C., Zhao,Y., Zheng,Z.,
            Yu,C., Zheng,L. and Wang,B.
  TITLE     CYP51-mediated cholesterol biosynthesis is required for the
            proliferation of CD4+ T cells in Sjogren's syndrome
  JOURNAL   Clin Exp Med 23 (5), 1691-1711 (2023)
   PUBMED   36413274
  REMARK    GeneRIF: CYP51-mediated cholesterol biosynthesis is required for
            the proliferation of CD4[+] T cells in Sjogren's syndrome.
REFERENCE   3  (residues 1 to 509)
  AUTHORS   McCarty,K.D., Sullivan,M.E., Tateishi,Y., Hargrove,T.Y.,
            Lepesheva,G.I. and Guengerich,F.P.
  TITLE     Processive kinetics in the three-step lanosterol
            14alpha-demethylation reaction catalyzed by human cytochrome P450
            51A1
  JOURNAL   J Biol Chem 299 (7), 104841 (2023)
   PUBMED   37209823
  REMARK    GeneRIF: Processive kinetics in the three-step lanosterol
            14alpha-demethylation reaction catalyzed by human cytochrome P450
            51A1.
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Jing,Y., Usai,R., Liu,Y. and Kincaid,J.R.
  TITLE     Revealing substrate-induced structural changes in active site of
            human CYP51 in the presence of its physiological substrates
  JOURNAL   J Inorg Biochem 242, 112167 (2023)
   PUBMED   36870163
  REMARK    GeneRIF: Revealing substrate-induced structural changes in active
            site of human CYP51 in the presence of its physiological
            substrates.
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Lamb,D.C., Hargrove,T.Y., Zhao,B., Wawrzak,Z., Goldstone,J.V.,
            Nes,W.D., Kelly,S.L., Waterman,M.R., Stegeman,J.J. and
            Lepesheva,G.I.
  TITLE     Concerning P450 Evolution: Structural Analyses Support Bacterial
            Origin of Sterol 14alpha-Demethylases
  JOURNAL   Mol Biol Evol 38 (3), 952-967 (2021)
   PUBMED   33031537
  REMARK    GeneRIF: Concerning P450 Evolution: Structural Analyses Support
            Bacterial Origin of Sterol 14alpha-Demethylases.
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Rozman,D., Stromstedt,M. and Waterman,M.R.
  TITLE     The three human cytochrome P450 lanosterol 14 alpha-demethylase
            (CYP51) genes reside on chromosomes 3, 7, and 13: structure of the
            two retrotransposed pseudogenes, association with a line-1 element,
            and evolution of the human CYP51 family
  JOURNAL   Arch Biochem Biophys 333 (2), 466-474 (1996)
   PUBMED   8809088
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Stromstedt,M., Rozman,D. and Waterman,M.R.
  TITLE     The ubiquitously expressed human CYP51 encodes lanosterol 14
            alpha-demethylase, a cytochrome P450 whose expression is regulated
            by oxysterols
  JOURNAL   Arch Biochem Biophys 329 (1), 73-81 (1996)
   PUBMED   8619637
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Aoyama,Y., Noshiro,M., Gotoh,O., Imaoka,S., Funae,Y., Kurosawa,N.,
            Horiuchi,T. and Yoshida,Y.
  TITLE     Sterol 14-demethylase P450 (P45014DM*) is one of the most ancient
            and conserved P450 species
  JOURNAL   J Biochem 119 (5), 926-933 (1996)
   PUBMED   8797093
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Aoyama,Y., Funae,Y., Noshiro,M., Horiuchi,T. and Yoshida,Y.
  TITLE     Occurrence of a P450 showing high homology to yeast lanosterol
            14-demethylase (P450(14DM)) in the rat liver
  JOURNAL   Biochem Biophys Res Commun 201 (3), 1320-1326 (1994)
   PUBMED   8024575
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U23942.1 and AC000120.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This endoplasmic reticulum protein participates in the synthesis of
            cholesterol by catalyzing the removal of the 14alpha-methyl group
            from lanosterol. Homologous genes are found in all three eukaryotic
            phyla, fungi, plants, and animals, suggesting that this is one of
            the oldest cytochrome P450 genes. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.163286.1, U23942.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000003100.13/ ENSP00000003100.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..509
                     /product="lanosterol 14-alpha demethylase isoform 1"
                     /EC_number="1.14.14.154"
                     /note="sterol 14-alpha demethylase; cytochrome P450, 51
                     (lanosterol 14-alpha-demethylase); lanosterol 14-alpha
                     demethylase; CYPLI; cytochrome P450LI; cytochrome
                     P45014DM; cytochrome P450 51A1; cytochrome P450-14DM;
                     cytochrome P450, family 51, subfamily A, polypeptide 1"
                     /calculated_mol_wt=57147
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16850.4)"
     Region          94..505
                     /region_name="CYP51-like"
                     /note="cytochrome P450 family 51 and similar cytochrome
                     P450s; cd11042"
                     /db_xref="CDD:410668"
     Site            order(137,159,162,169,314,317..318,321..322,325,377,382,
                     386,388,447..449,452..457,460..461)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410668"
     Site            order(137,139..140,144,240,313,316..317,320..321,385,387)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410668"
     CDS             1..509
                     /gene="CYP51A1"
                     /gene_synonym="CP51; CYP51; CYPL1; LDM; P450-14DM; P450L1"
                     /coded_by="NM_000786.4:114..1643"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5623.1"
                     /db_xref="GeneID:1595"
                     /db_xref="HGNC:HGNC:2649"
                     /db_xref="MIM:601637"
ORIGIN      
        1 maaaagmlll gllqaggsvl gqamekvtgg nllsmlliac aftlslvyli rlaaghlvql
       61 pagvksppyi fspipflgha iafgkspief lenayekygp vfsftmvgkt ftyllgsdaa
      121 allfnskned lnaedvysrl ttpvfgkgva ydvpnpvfle qkkmlksgln iahfkqhvsi
      181 ieketkeyfe swgesgeknv fealseliil tashclhgke irsqlnekva qlyadldggf
      241 shaawllpgw lplpsfrrrd rahreikdif ykaiqkrrqs qekiddilqt lldatykdgr
      301 pltddevagm liglllagqh tssttsawmg fflardktlq kkcyleqktv cgenlpplty
      361 dqlkdlnlld rciketlrlr ppimimmrma rtpqtvagyt ippghqvcvs ptvnqrlkds
      421 wverldfnpd rylqdnpasg ekfayvpfga grhrcigenf ayvqiktiws tmlrlyefdl
      481 idgyfptvny ttmihtpenp virykrrsk
//
LOCUS       NP_001265525            1003 aa            linear   PRI 27-APR-2025
DEFINITION  anoctamin-2 isoform 1 [Homo sapiens].
ACCESSION   NP_001265525
VERSION     NP_001265525.1
DBSOURCE    REFSEQ: accession NM_001278596.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Sala-Rabanal,M., Yurtsever,Z., Berry,K.N., McClenaghan,C.,
            Foy,A.J., Hanson,A., Steinberg,D.F., Greven,J.A., Kluender,C.E.,
            Alexander-Brett,J.M., Nichols,C.G. and Brett,T.J.
  TITLE     Modulation of TMEM16B channel activity by the calcium-activated
            chloride channel regulator 4 (CLCA4) in human cells
  JOURNAL   J Biol Chem 300 (7), 107432 (2024)
   PUBMED   38825009
  REMARK    GeneRIF: Modulation of TMEM16B channel activity by the
            calcium-activated chloride channel regulator 4 (CLCA4) in human
            cells.
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Auer,F., Franco Taveras,E., Klein,U., Kesenheimer,C.,
            Fleischhauer,D., Mohrlen,F. and Frings,S.
  TITLE     Anoctamin 2-chloride channels reduce simple spike activity and
            mediate inhibition at elevated calcium concentration in cerebellar
            Purkinje cells
  JOURNAL   PLoS One 16 (3), e0247801 (2021)
   PUBMED   33651839
  REMARK    GeneRIF: Anoctamin 2-chloride channels reduce simple spike activity
            and mediate inhibition at elevated calcium concentration in
            cerebellar Purkinje cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Tengvall,K., Huang,J., Hellstrom,C., Kammer,P., Bistrom,M.,
            Ayoglu,B., Lima Bomfim,I., Stridh,P., Butt,J., Brenner,N.,
            Michel,A., Lundberg,K., Padyukov,L., Lundberg,I.E., Svenungsson,E.,
            Ernberg,I., Olafsson,S., Dilthey,A.T., Hillert,J., Alfredsson,L.,
            Sundstrom,P., Nilsson,P., Waterboer,T., Olsson,T. and Kockum,I.
  TITLE     Molecular mimicry between Anoctamin 2 and Epstein-Barr virus
            nuclear antigen 1 associates with multiple sclerosis risk
  JOURNAL   Proc Natl Acad Sci U S A 116 (34), 16955-16960 (2019)
   PUBMED   31375628
  REMARK    GeneRIF: a hypothesis where immune reactivity toward EBNA1 through
            molecular mimicry with ANO2 contributes to the etiopathogenesis of
            Multiple sclerosis.
REFERENCE   4  (residues 1 to 1003)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1003)
  AUTHORS   Pifferi,S.
  TITLE     Permeation Mechanisms in the TMEM16B Calcium-Activated Chloride
            Channels
  JOURNAL   PLoS One 12 (1), e0169572 (2017)
   PUBMED   28046119
  REMARK    GeneRIF: residues facing the putative channel pore are responsible
            both for controlling the ion selectivity and the gating of the
            channel, providing an initial understanding of molecular mechanism
            of ion permeation in TMEM16B
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1003)
  AUTHORS   Stohr,H., Heisig,J.B., Benz,P.M., Schoberl,S., Milenkovic,V.M.,
            Strauss,O., Aartsen,W.M., Wijnholds,J., Weber,B.H. and Schulz,H.L.
  TITLE     TMEM16B, a novel protein with calcium-dependent chloride channel
            activity, associates with a presynaptic protein complex in
            photoreceptor terminals
  JOURNAL   J Neurosci 29 (21), 6809-6818 (2009)
   PUBMED   19474308
  REMARK    GeneRIF: This study suggested that TMEM16B to be a strong candidate
            for the long sought-after Ca(2+)-dependent chloride channel in the
            photoreceptor synapse.
REFERENCE   7  (residues 1 to 1003)
  AUTHORS   Hartzell,H.C., Yu,K., Xiao,Q., Chien,L.T. and Qu,Z.
  TITLE     Anoctamin/TMEM16 family members are Ca2+-activated Cl- channels
  JOURNAL   J Physiol 587 (Pt 10), 2127-2139 (2009)
   PUBMED   19015192
  REMARK    Review article
REFERENCE   8  (residues 1 to 1003)
  AUTHORS   Schneppenheim,R., Castaman,G., Federici,A.B., Kreuz,W.,
            Marschalek,R., Oldenburg,J., Oyen,F. and Budde,U.
  TITLE     A common 253-kb deletion involving VWF and TMEM16B in German and
            Italian patients with severe von Willebrand disease type 3
  JOURNAL   J Thromb Haemost 5 (4), 722-728 (2007)
   PUBMED   17371490
  REMARK    GeneRIF: VWF and TMEM16B deletions may have a role in severe von
            Willebrand disease type 3
REFERENCE   9  (residues 1 to 1003)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of TMEM16E and TMEM16F genes in
            silico
  JOURNAL   Int J Oncol 24 (5), 1345-1349 (2004)
   PUBMED   15067359
REFERENCE   10 (residues 1 to 1003)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     FLJ10261 gene, located within the CCND1-EMS1 locus on human
            chromosome 11q13, encodes the eight-transmembrane protein
            homologous to C12orf3, C11orf25 and FLJ34272 gene products
  JOURNAL   Int J Oncol 22 (6), 1375-1381 (2003)
   PUBMED   12739008
  REMARK    GeneRIF: C12orf3, FLJ10261 (ORAOV2), C11orf25 and FLJ34272
            constitute a family of eight-transmembrane proteins with N- and
            C-terminal tails facing the cytoplasm.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB593159.1, AC006431.9, FJ384095.1, AK024010.1 and BE645295.1.
            
            Summary: ANO2 belongs to a family of calcium-activated chloride
            channels (CaCCs) (reviewed by Hartzell et al., 2009 [PubMed
            19015192]).[supplied by OMIM, Jan 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ384095.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..1003
                     /product="anoctamin-2 isoform 1"
                     /note="transmembrane protein 16B (eight membrane-spanning
                     domains); anoctamin 2, calcium activated chloride channel"
                     /calculated_mol_wt=113839
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Region          91..349
                     /region_name="Anoct_dimer"
                     /note="dimerization domain of Ca+-activated
                     chloride-channel, anoctamin; pfam16178"
                     /db_xref="CDD:465044"
     Region          352..942
                     /region_name="Anoctamin"
                     /note="Calcium-activated chloride channel; pfam04547"
                     /db_xref="CDD:461349"
     Site            366..386
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            422
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            435..455
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            539..559
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            583..603
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            624..644
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            749..769
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            802..822
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            841
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            849
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            856
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Site            908..928
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Region          961..1003
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     Region          1001..1003
                     /region_name="DLG4 binding (PDZ)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ90.2)"
     CDS             1..1003
                     /gene="ANO2"
                     /gene_synonym="C12orf3; TMEM16B"
                     /coded_by="NM_001278596.3:43..3054"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS91643.1"
                     /db_xref="GeneID:57101"
                     /db_xref="HGNC:HGNC:1183"
                     /db_xref="MIM:610109"
ORIGIN      
        1 matpgprdip llpgsprrls pqagsrggqg pkhgqqclkm pgprapglqg gsnrdpgqpc
       61 ggestrsssv innyldanep vslearlsrm hfhdsqrkvd yvlayhyrkr gvhlaqgfpg
      121 hslaivsnge tgkephaggp gdielgplda leeerkeqre efehnlmeag lelekdlenk
      181 sqgsifvrih apwqvlarea eflkikvptk kemyeikagg siakkfsaal qklsshlqpr
      241 vpehsnnkmk nlsypfsrek mylyniqekd tffdnatrsr ivheilkrta csranntmgi
      301 nslianniye aayplhdgey dspeddmndr kllyqewary gvfykfqpid lirkyfgeki
      361 glyfawlgly tsflipssvi gvivflygca tieedipsre mcdqqnaftm cplcdkscdy
      421 wnlssacgta qashlfdnpa tvffsifmal watmflenwk rlqmrlgyfw dltgieeeee
      481 raqehsrpey etkvrekmlk esnqsavqkl etnttecgde ddedkltwkd rfpgylmnfa
      541 silfmialtf sivfgvivyr ittaaalsln katrsnvrvt vtataviinl vvilildeiy
      601 gavakwltki evpkteqtfe erlilkafll kfvnayspif yvaffkgrfv grpgsyvyvf
      661 dgyrmeecap ggclmelciq lsiimlgkql iqnnifeigv pklkklfrkl kdeteagetd
      721 sahskhpeqw dldyslepyt gltpeymemi iqfgfvtlfv asfplapvfa llnnvievrl
      781 dakkfvtelr rpdavrtkdi giwfdilsgi gkfsvisnaf viaitsdfip rlvyqysysh
      841 ngtlhgfvnh tlsffnvsql kegtqpensq fdqevqfcrf kdyreppwap npyefskqyw
      901 filsarlafv iifqnlvmfl svlvdwmipd iptdisdqik keksllvdff lkeeheklkl
      961 mdepalrspg ggdrsrsraa ssapsgqsql gsmmssgsqh tnv
//
LOCUS       NP_653214                 88 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome c oxidase subunit 6B2 [Homo sapiens].
ACCESSION   NP_653214
VERSION     NP_653214.2
DBSOURCE    REFSEQ: accession NM_144613.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Shen,M., Zhao,N., Deng,X. and Deng,M.
  TITLE     [High expression of COX6B2 in gastric cancer is associated with
            poor long-term prognosis and promotes cell proliferation and cell
            cycle progression by inhibiting p53 signaling]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 44 (2), 289-297 (2024)
   PUBMED   38501414
  REMARK    GeneRIF: [High expression of COX6B2 in gastric cancer is associated
            with poor long-term prognosis and promotes cell proliferation and
            cell cycle progression by inhibiting p53 signaling].
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Cheng,C.C., Wooten,J., Gibbs,Z.A., McGlynn,K., Mishra,P. and
            Whitehurst,A.W.
  TITLE     Sperm-specific COX6B2 enhances oxidative phosphorylation,
            proliferation, and survival in human lung adenocarcinoma
  JOURNAL   Elife 9, e58108 (2020)
   PUBMED   32990599
  REMARK    GeneRIF: Sperm-specific COX6B2 enhances oxidative phosphorylation,
            proliferation, and survival in human lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Huttemann,M., Jaradat,S. and Grossman,L.I.
  TITLE     Cytochrome c oxidase of mammals contains a testes-specific isoform
            of subunit VIb--the counterpart to testes-specific cytochrome c?
  JOURNAL   Mol Reprod Dev 66 (1), 8-16 (2003)
   PUBMED   12874793
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Taanman,J.W., Schrage,C., Ponne,N.J., Das,A.T., Bolhuis,P.A., de
            Vries,H. and Agsteribbe,E.
  TITLE     Isolation of cDNAs encoding subunit VIb of cytochrome c oxidase and
            steady-state levels of coxVIb mRNA in different tissues
  JOURNAL   Gene 93 (2), 285-291 (1990)
   PUBMED   2172092
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG717038.1 and BC026123.2.
            
            On Aug 26, 2003 this sequence version replaced NP_653214.1.
            
            Transcript Variant: This variant (2) differs in the 3' UTR compared
            to variant 1. All four variants encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026123.2, BG716978.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326529.9/ ENSP00000320672.3
            NMD candidate          :: translation inferred from conservation
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..88
                     /product="cytochrome c oxidase subunit 6B2"
                     /note="cytochrome c oxidase subunit VIb, testes-specific;
                     cancer/testis antigen 59; COX VIb-2; cytochrome c oxidase
                     subunit VIb polypeptide 2 (testis)"
                     /calculated_mol_wt=10398
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YFQ2.1)"
     Region          10..87
                     /region_name="Cyt_c_Oxidase_VIb"
                     /note="Cytochrome c oxidase subunit VIb. Cytochrome c
                     oxidase (CcO), the terminal oxidase in the respiratory
                     chains of eukaryotes and most bacteria, is a multi-chain
                     transmembrane protein located in the inner membrane of
                     mitochondria and the cell membrane of...; cd00926"
                     /db_xref="CDD:238466"
     Site            order(14..17,26..29,61,64..70)
                     /site_type="other"
                     /note="Subunit VIb/II interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Site            26
                     /site_type="other"
                     /note="Subunit VIb/I interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Site            order(30,33,85)
                     /site_type="other"
                     /note="Subunit VIb/III interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Region          32..42
                     /region_name="Cx9C motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YFQ2.1)"
     Site            order(49,51..56)
                     /site_type="other"
                     /note="Subunit VIb/VIb interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     Region          56..67
                     /region_name="Cx10C motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YFQ2.1)"
     Site            order(78,81..83)
                     /site_type="other"
                     /note="Subunit VIb/VIa interface [polypeptide binding]"
                     /db_xref="CDD:238466"
     CDS             1..88
                     /gene="COX6B2"
                     /gene_synonym="COXVIB2; CT59"
                     /coded_by="NM_144613.5:89..355"
                     /db_xref="CCDS:CCDS42630.1"
                     /db_xref="GeneID:125965"
                     /db_xref="HGNC:HGNC:24380"
                     /db_xref="MIM:618127"
ORIGIN      
        1 mldveaqepp kgkwstppfd prfpsqnqir ncyqnfldyh rclktrtrrg kstqpceyyf
       61 rvyhslcpis wveswneqik ngifagki
//
LOCUS       NP_003577                400 aa            linear   PRI 27-APR-2025
DEFINITION  double C2-like domain-containing protein alpha [Homo sapiens].
ACCESSION   NP_003577
VERSION     NP_003577.2
DBSOURCE    REFSEQ: accession NM_003586.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Hu,X., Tang,J., Lan,X. and Mi,X.
  TITLE     Increased expression of DOC2A in human and rat temporal lobe
            epilepsy
  JOURNAL   Epilepsy Res 151, 78-84 (2019)
   PUBMED   30844661
  REMARK    GeneRIF: This study demonstrated that the DOCA2 increase expression
            in temporal lobe in temporal lobe epilepsy.
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Ramirez,D.M.O., Crawford,D.C., Chanaday,N.L., Trauterman,B.,
            Monteggia,L.M. and Kavalali,E.T.
  TITLE     Loss of Doc2-Dependent Spontaneous Neurotransmission Augments
            Glutamatergic Synaptic Strength
  JOURNAL   J Neurosci 37 (26), 6224-6230 (2017)
   PUBMED   28539418
  REMARK    GeneRIF: this study, members of the Doc2 family of presynaptic
            proteins were eliminated, which caused a reduction in spontaneous
            neurotransmission, whereas action potential-evoked
            neurotransmission remained relatively normal.
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Mochida,S., Orita,S., Sakaguchi,G., Sasaki,T. and Takai,Y.
  TITLE     Role of the Doc2 alpha-Munc13-1 interaction in the neurotransmitter
            release process
  JOURNAL   Proc Natl Acad Sci U S A 95 (19), 11418-11422 (1998)
   PUBMED   9736751
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Orita,S., Naito,A., Sakaguchi,G., Maeda,M., Igarashi,H., Sasaki,T.
            and Takai,Y.
  TITLE     Physical and functional interactions of Doc2 and Munc13 in
            Ca2+-dependent exocytotic machinery
  JOURNAL   J Biol Chem 272 (26), 16081-16084 (1997)
   PUBMED   9195900
REFERENCE   8  (residues 1 to 400)
  AUTHORS   Verhage,M., de Vries,K.J., Roshol,H., Burbach,J.P., Gispen,W.H. and
            Sudhof,T.C.
  TITLE     DOC2 proteins in rat brain: complementary distribution and proposed
            function as vesicular adapter proteins in early stages of secretion
  JOURNAL   Neuron 18 (3), 453-461 (1997)
   PUBMED   9115738
REFERENCE   9  (residues 1 to 400)
  AUTHORS   Sakaguchi,G., Orita,S., Maeda,M., Igarashi,H. and Takai,Y.
  TITLE     Molecular cloning of an isoform of Doc2 having two C2-like domains
  JOURNAL   Biochem Biophys Res Commun 217 (3), 1053-1061 (1995)
   PUBMED   8554557
REFERENCE   10 (residues 1 to 400)
  AUTHORS   Orita,S., Sasaki,T., Naito,A., Komuro,R., Ohtsuka,T., Maeda,M.,
            Suzuki,H., Igarashi,H. and Takai,Y.
  TITLE     Doc2: a novel brain protein having two repeated C2-like domains
  JOURNAL   Biochem Biophys Res Commun 206 (2), 439-448 (1995)
   PUBMED   7826360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC055284.1.
            
            On May 7, 2004 this sequence version replaced NP_003577.1.
            
            Summary: There are at least two protein isoforms of the Double C2
            protein, namely alpha (DOC2A) and beta (DOC2B), which contain two
            C2-like domains. DOC2A and DOC2B are encoded by different genes;
            these genes are at times confused with the unrelated DAB2 gene
            which was initially named DOC-2. DOC2A is mainly expressed in brain
            and is suggested to be involved in Ca(2+)-dependent
            neurotransmitter release. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (3) lacks an alternate exon and
            uses an alternate splice site in the 5' UTR compared to variant 1.
            Variants 1 through 4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC055284.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000350119.9/ ENSP00000340017.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..400
                     /product="double C2-like domain-containing protein alpha"
                     /note="doc2-alpha; double C2-like domains, alpha"
                     /calculated_mol_wt=43828
     Region          1..89
                     /region_name="Interaction with UNC13D and DYNLT1.
                     /evidence=ECO:0000269|PubMed:18354201,
                     ECO:0000269|PubMed:9804756"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14183.5)"
     Region          90..213
                     /region_name="C2A_Rabphilin_Doc2"
                     /note="C2 domain first repeat present in Rabphilin and
                     Double C2 domain; cd04035"
                     /db_xref="CDD:176000"
     Site            order(120,126,181,183,189)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176000"
     Region          215..400
                     /region_name="Interaction with UNC13D.
                     /evidence=ECO:0000269|PubMed:18354201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14183.5)"
     Region          254..386
                     /region_name="C2B_Rabphilin_Doc2"
                     /note="C2 domain second repeat present in Rabphilin and
                     Double C2 domain; cd08384"
                     /db_xref="CDD:176030"
     Site            order(282,288,342,344,350)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176030"
     CDS             1..400
                     /gene="DOC2A"
                     /gene_synonym="Doc2"
                     /coded_by="NM_003586.3:139..1341"
                     /db_xref="CCDS:CCDS10666.1"
                     /db_xref="GeneID:8448"
                     /db_xref="HGNC:HGNC:2985"
                     /db_xref="MIM:604567"
ORIGIN      
        1 mrgrrgdrmt iniqehmain vcpgpirpir qisdyfprgp gpeggggggg eapahlvpla
       61 lappaallga ttpedgaevd sydsddatal gtlefdllyd rasctlhcsi lrakglkpmd
      121 fngladpyvk lhllpgacka nklktktqrn tlnpvwnedl tysgitdddi thkvlriavc
      181 dedklshnef igeirvplrr lkpsqkkhfn iclerqvpla spssmsaalr giscylkele
      241 qaeqgqglle ergrillsls yssrrrgllv gilrcahlaa mdvngysdpy vktylrpdvd
      301 kkskhktcvk kktlnpefne effyeielst latktlevtv wdydigksnd figgvslgpg
      361 argearkhws dclqqpdaal erwhtltsel ppaagalssa
//
LOCUS       NP_001074433             612 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor Sp2 isoform 2 [Mus musculus].
ACCESSION   NP_001074433
VERSION     NP_001074433.1
DBSOURCE    REFSEQ: accession NM_001080964.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Johnson,C.A. and Ghashghaei,H.T.
  TITLE     Sp2 regulates late neurogenic but not early expansive divisions of
            neural stem cells underlying population growth in the mouse cortex
  JOURNAL   Development 147 (4) (2020)
   PUBMED   32001437
  REMARK    GeneRIF: there is a stage-specific requirement for Sp2 in neural
            stem and progenitor cells in the mouse cortex
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Norrie,J.L., Lupo,M.S., Xu,B., Al Diri,I., Valentine,M., Putnam,D.,
            Griffiths,L., Zhang,J., Johnson,D., Easton,J., Shao,Y., Honnell,V.,
            Frase,S., Miller,S., Stewart,V., Zhou,X., Chen,X. and Dyer,M.A.
  TITLE     Nucleome Dynamics during Retinal Development
  JOURNAL   Neuron 104 (3), 512-528 (2019)
   PUBMED   31493975
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Volkel,S., Stielow,B., Finkernagel,F., Berger,D., Stiewe,T.,
            Nist,A. and Suske,G.
  TITLE     Transcription factor Sp2 potentiates binding of the TALE
            homeoproteins Pbx1:Prep1 and the histone-fold domain protein Nf-y
            to composite genomic sites
  JOURNAL   J Biol Chem 293 (50), 19250-19262 (2018)
   PUBMED   30337366
  REMARK    GeneRIF: a mechanism by which the DNA binding-independent activity
            of Sp2 potentiates genomic loading of Pbx1:Prep1 and Nf-y to
            composite motifs present in many promoters of highly expressed
            genes
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Wegener,A., Kuspert,M., Sock,E., Philipsen,S., Suske,G. and
            Wegner,M.
  TITLE     Sp2 is the only glutamine-rich specificity protein with minor
            impact on development and differentiation in myelinating glia
  JOURNAL   J Neurochem 140 (2), 245-256 (2017)
   PUBMED   27889927
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Zschemisch,N.H., Brusch,I., Hambusch,A.S. and Bleich,A.
  TITLE     Transcription Factor SP2 Enhanced the Expression of Cd14 in
            Colitis-Susceptible C3H/HeJBir
  JOURNAL   PLoS One 11 (5), e0155821 (2016)
   PUBMED   27191968
  REMARK    GeneRIF: SP2 as important factor responsible for higher Cd14
            expression and reduced IBD susceptibility mediated by the C3Bir
            allele.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 612)
  AUTHORS   Suske,G., Bruford,E. and Philipsen,S.
  TITLE     Mammalian SP/KLF transcription factors: bring in the family
  JOURNAL   Genomics 85 (5), 551-556 (2005)
   PUBMED   15820306
REFERENCE   7  (residues 1 to 612)
  AUTHORS   Moorefield,K.S., Fry,S.J. and Horowitz,J.M.
  TITLE     Sp2 DNA binding activity and trans-activation are negatively
            regulated in mammalian cells
  JOURNAL   J Biol Chem 279 (14), 13911-13924 (2004)
   PUBMED   14726517
REFERENCE   8  (residues 1 to 612)
  AUTHORS   Hammer,F., Compagnone,N.A., Vigne,J.L., Bair,S.R. and Mellon,S.H.
  TITLE     Transcriptional regulation of P450scc gene expression in the
            embryonic rodent nervous system
  JOURNAL   Endocrinology 145 (2), 901-912 (2004)
   PUBMED   14576192
REFERENCE   9  (residues 1 to 612)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 612)
  AUTHORS   Bakovic,M., Waite,K.A. and Vance,D.E.
  TITLE     Functional significance of Sp1, Sp2, and Sp3 transcription factors
            in regulation of the murine CTP:phosphocholine cytidylyltransferase
            alpha promoter
  JOURNAL   J Lipid Res 41 (4), 583-594 (2000)
   PUBMED   10744779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL596384.17, BC086457.1, BP765918.1 and AA267604.1.
            
            Summary: This gene encodes a member of the Sp subfamily of Sp/XKLF
            transcription factors. Sp family proteins are sequence-specific
            DNA-binding proteins characterized by an amino-terminal
            trans-activation domain and three carboxy-terminal zinc finger
            motifs. This protein contains the least conserved DNA-binding
            domain within the Sp subfamily of proteins, and its DNA sequence
            specificity differs from the other Sp proteins. The protein can act
            as a transcriptional activator or repressor, depending on the
            promoter and cell type. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK172877.1, BC021759.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 60.17 cM"
     Protein         1..612
                     /product="transcription factor Sp2 isoform 2"
                     /note="transcription factor Sp2"
                     /calculated_mol_wt=64777
     Region          9..525
                     /region_name="SP2_N"
                     /note="N-terminal domain of transcription factor
                     Specificity Protein (SP) 2; cd22540"
                     /db_xref="CDD:411776"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02086; propagated from
                     UniProtKB/Swiss-Prot (Q9D2H6.2)"
     Region          166..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D2H6.2)"
     Region          226..250
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D2H6.2)"
     Region          360..368
                     /region_name="9aaTAD, inactive.
                     /evidence=ECO:0000250|UniProtKB:Q02086"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D2H6.2)"
     Region          529..548
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(533,535,537,539..540,543..544,547,563,565,569..570,
                     573..574,577,591,593,595,597..598,601..602,605)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          541..567
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          556..578
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          570..593
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          584..606
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          586..606
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..612
                     /gene="Sp2"
                     /gene_synonym="4930480I16Rik; mKIAA0048"
                     /coded_by="NM_001080964.2:62..1900"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:78912"
                     /db_xref="MGI:MGI:1926162"
ORIGIN      
        1 msdpqmsmaa taavspsdyl qpaaattqds qpsplallaa tcskigppav eaavtppapp
       61 qptprklvpi kpaplplspc knsfsilssk gnilqiqgsq lstsypggqf vfaiqnptli
      121 nkgsrsnasi qyqvpqiqgn ssqtiqvqps ltnqiqvipg tnqaittpst sghkpvpikp
      181 apvqkssttt tpvqsganvv kltgggsnmt ltlplnnlvn tsdiggpaql ltespptpls
      241 ktnkkarkks lpvsqpsvav aeqvetvlie ttadniiqag nnllivqspg ggqpavvqqv
      301 qvvppkaeqq qvvqipqqal rvvqaasatl ptvpqkpsqn fqiqtteptp tqvyirtpsg
      361 evqtvlvqds ppataattst vtcnspalra phlsgtskkh saailrkerp lpkiapagsi
      421 islnaaqlaa aaqamqtini ngvqvqgvpv titntggqqq ltvqnvsgnn ltisglsptq
      481 iqlqmeqala geaqpgekrr rmactcpnck dgekrsgeqg kkkhvchipd cgktfrktsl
      541 lrahvrlhtg erpfvcnwff cgkrftrsde lqrharthtg dkrfecaqcq krfmrsdhlt
      601 khykthlgtk gl
//
LOCUS       NP_001353522             834 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 18 [Homo
            sapiens].
ACCESSION   NP_001353522 XP_016855512
VERSION     NP_001353522.1
DBSOURCE    REFSEQ: accession NM_001366593.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 834)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 834)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 834)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 834)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 834)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 834)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855512.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.56473.1,
                                           SRR1803613.25179.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..834
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 18"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=94044
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <331..660
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..834
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366593.1:2055..4559"
                     /note="isoform 18 is encoded by transcript variant 36"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels esedkggkma aadsvqqrrq yrrqnqqsss dsgsssssed
      421 erpkrshvkn gevgrrrrhs psrsaspspr krqketsprm qmgkrwqspv tksgrrrrsp
      481 sppptrrrrs pspappprrr rtptppprrr tpsppprrrs psprrysppi qrryspsppp
      541 krrtaspppp pkrraspspp pkrrvshspp pkqrsspvtk rrspslsskh rkgsspsrst
      601 rearspqpnk rhspsprpra pqtssspppv rrgassspqr rqspspstrp irrvsrtpep
      661 kkikkaasps pqsvrrvsss rsvsgspepa akkppappsp vqsqspstnw spavpvkkak
      721 sptpspsppr nsdqegggkk kkkkkdkkhk kdkkhkkhkk hkkekavaaa aaaavtpaai
      781 aaatttlaqe epvaapepkk eteseaednl ddlekhlrek alrsmrkaqv spqs
//
LOCUS       NP_004586                366 aa            linear   PRI 27-APR-2025
DEFINITION  spermine synthase isoform 1 [Homo sapiens].
ACCESSION   NP_004586
VERSION     NP_004586.2
DBSOURCE    REFSEQ: accession NM_004595.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Tao,X., Liu,J., Diaz-Perez,Z., Foley,J.R., Nwafor,A., Stewart,T.M.,
            Casero,R.A. Jr. and Zhai,R.G.
  TITLE     Reduction of spermine synthase enhances autophagy to suppress Tau
            accumulation
  JOURNAL   Cell Death Dis 15 (5), 333 (2024)
   PUBMED   38740758
  REMARK    GeneRIF: Reduction of spermine synthase enhances autophagy to
            suppress Tau accumulation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Cressman,A., Morales,D., Zhang,Z., Le,B., Foley,J.,
            Murray-Stewart,T., Genetos,D.C. and Fierro,F.A.
  TITLE     Effects of Spermine Synthase Deficiency in Mesenchymal Stromal
            Cells Are Rescued by Upstream Inhibition of Ornithine Decarboxylase
  JOURNAL   Int J Mol Sci 25 (5), 2463 (2024)
   PUBMED   38473716
  REMARK    GeneRIF: Effects of Spermine Synthase Deficiency in Mesenchymal
            Stromal Cells Are Rescued by Upstream Inhibition of Ornithine
            Decarboxylase.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Qazi,T.J., Wu,Q., Aierken,A., Lu,D., Bukhari,I., Hussain,H.M.J.,
            Yang,J., Mir,A. and Qing,H.
  TITLE     Whole-exome sequencing identifies a novel mutation in spermine
            synthase gene (SMS) associated with Snyder-Robinson Syndrome
  JOURNAL   BMC Med Genet 21 (1), 168 (2020)
   PUBMED   32838743
  REMARK    GeneRIF: Whole-exome sequencing identifies a novel mutation in
            spermine synthase gene (SMS) associated with Snyder-Robinson
            Syndrome.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Becerra-Solano,L.E., Butler,J., Castaneda-Cisneros,G.,
            McCloskey,D.E., Wang,X., Pegg,A.E., Schwartz,C.E.,
            Sanchez-Corona,J. and Garcia-Ortiz,J.E.
  TITLE     A missense mutation, p.V132G, in the X-linked spermine synthase
            gene (SMS) causes Snyder-Robinson syndrome
  JOURNAL   Am J Med Genet A 149A (3), 328-335 (2009)
   PUBMED   19206178
  REMARK    GeneRIF: A missense mutation, p. V132G, in the X-linked SMS gene
            causes Snyder-Robinson syndrome.
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Wu,H., Min,J., Zeng,H., McCloskey,D.E., Ikeguchi,Y., Loppnau,P.,
            Michael,A.J., Pegg,A.E. and Plotnikov,A.N.
  TITLE     Crystal structure of human spermine synthase: implications of
            substrate binding and catalytic mechanism
  JOURNAL   J Biol Chem 283 (23), 16135-16146 (2008)
   PUBMED   18367445
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Cason,A.L., Ikeguchi,Y., Skinner,C., Wood,T.C., Holden,K.R.,
            Lubs,H.A., Martinez,F., Simensen,R.J., Stevenson,R.E., Pegg,A.E.
            and Schwartz,C.E.
  TITLE     X-linked spermine synthase gene (SMS) defect: the first polyamine
            deficiency syndrome
  JOURNAL   Eur J Hum Genet 11 (12), 937-944 (2003)
   PUBMED   14508504
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Arena,J.F., Schwartz,C., Ouzts,L., Stevenson,R., Miller,M.,
            Garza,J., Nance,M. and Lubs,H.
  TITLE     X-linked mental retardation with thin habitus, osteoporosis, and
            kyphoscoliosis: linkage to Xp21.3-p22.12
  JOURNAL   Am J Med Genet 64 (1), 50-58 (1996)
   PUBMED   8826448
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Korhonen,V.P., Halmekyto,M., Kauppinen,L., Myohanen,S.,
            Wahlfors,J., Keinanen,T., Hyvonen,T., Alhonen,L., Eloranta,T. and
            Janne,J.
  TITLE     Molecular cloning of a cDNA encoding human spermine synthase
  JOURNAL   DNA Cell Biol 14 (10), 841-847 (1995)
   PUBMED   7546290
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Schwartz,C.E., Peron,A. and Kutler,M.J.
  TITLE     Snyder-Robinson Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23805436
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Snyder,R.D. and Robinson,A.
  TITLE     Recessive sex-linked mental retardation in the absence of other
            recognizable abnormalities. Report of a family
  JOURNAL   Clin Pediatr (Phila) 8 (11), 669-674 (1969)
   PUBMED   5823961
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U73023.1, AD001528.1 and
            BC009898.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 30, 2002 this sequence version replaced NP_004586.1.
            
            Summary: This gene encodes a protein belonging to the
            spermidine/spermin synthase family and catalyzes the production of
            spermine from spermidine. Pseudogenes of this gene are located on
            chromosomes 1, 5, 6 and X. Mutations in this gene cause an X-linked
            intellectual disability called Snyder-Robinson Syndrome (SRS).
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1167824.1,
                                           SRR1660809.231072.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000404933.7/ ENSP00000385746.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.11"
     Protein         1..366
                     /product="spermine synthase isoform 1"
                     /EC_number="2.5.1.22"
                     /note="spermidine aminopropyltransferase"
                     /calculated_mol_wt=41137
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P52788.2)"
     Region          21..117
                     /region_name="SpmSyn_N"
                     /note="S-adenosylmethionine decarboxylase N -terminal;
                     pfam17950"
                     /db_xref="CDD:465581"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52788.2)"
     Region          123..172
                     /region_name="Spermine_synt_N"
                     /note="Spermidine synthase tetramerization domain;
                     pfam17284"
                     /db_xref="CDD:407397"
     Region          175..365
                     /region_name="Spermine_synth"
                     /note="Spermine/spermidine synthase domain; pfam01564"
                     /db_xref="CDD:396237"
     CDS             1..366
                     /gene="SMS"
                     /gene_synonym="MRSR; MRXSSR; SPMSY; SpS; SRS"
                     /coded_by="NM_004595.5:117..1217"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14203.1"
                     /db_xref="GeneID:6611"
                     /db_xref="HGNC:HGNC:11123"
                     /db_xref="MIM:300105"
ORIGIN      
        1 maaarhstld fmlgakadge tilkglqsif qeqgmaesvh twqdhgylat ytnkngsfan
       61 lriyphglvl ldlqsydgda qgkeeidsil nkveermkel sqdstgrvkr lppivrggai
      121 drywptadgr lveydidevv ydedspyqni kilhskqfgn ililsgdvnl aesdlaytra
      181 imgsgkedyt gkdvlilggg dggilceivk lkpkmvtmve idqmvidgck kymrktcgdv
      241 ldnlkgdcyq vliedcipvl kryakegref dyvindltav pistspeeds tweflrlild
      301 lsmkvlkqdg kyftqgncvn ltealslyee qlgrlycpve fskeivcvps ylelwvfytv
      361 wkkakp
//
LOCUS       NP_001352141             594 aa            linear   PRI 27-APR-2025
DEFINITION  aspartate--tRNA ligase, mitochondrial isoform 2 [Homo sapiens].
ACCESSION   NP_001352141 XP_006711490
VERSION     NP_001352141.1
DBSOURCE    REFSEQ: accession NM_001365212.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Bostanova,F.M., Tsygankova,P.G., Larshina,E.A., Nagornov,I.O.,
            Evseeva,Y.V., Krutikhina,I.L., Dzhentemirova,M.E., Kashlakova,M.N.,
            Petukhova,M.S., Sharkova,I.V. and Zakharova,E.Y.
  TITLE     Identification of a Novel Indel Variant in the DARS2 Gene in
            Russian Patients with Leukoencephalopathy with Brainstem and Spinal
            Cord Involvement and Lactate Elevation
  JOURNAL   Genes (Basel) 15 (5), 615 (2024)
   PUBMED   38790244
  REMARK    GeneRIF: Identification of a Novel Indel Variant in the DARS2 Gene
            in Russian Patients with Leukoencephalopathy with Brainstem and
            Spinal Cord Involvement and Lactate Elevation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Liu,X.S., Liu,Z.Y., Zeng,D.B., Hu,J., Chen,X.L., Gu,J.L., Gao,Y.
            and Pei,Z.J.
  TITLE     Functional enrichment analysis reveals the involvement of DARS2 in
            multiple biological pathways and its potential as a therapeutic
            target in esophageal carcinoma
  JOURNAL   Aging (Albany NY) 16 (4), 3934-3954 (2024)
   PUBMED   38382106
  REMARK    GeneRIF: Functional enrichment analysis reveals the involvement of
            DARS2 in multiple biological pathways and its potential as a
            therapeutic target in esophageal carcinoma.
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Fang,T., Jiang,J., Yu,W., Li,R. and Tian,H.
  TITLE     DARS2 promotes the occurrence of lung adenocarcinoma via the
            ERK/c-Myc signaling pathway
  JOURNAL   Thorac Cancer 14 (36), 3511-3521 (2023)
   PUBMED   37950542
  REMARK    GeneRIF: DARS2 promotes the occurrence of lung adenocarcinoma via
            the ERK/c-Myc signaling pathway.
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Liu,X.S., Yuan,L.L., Gao,Y., Ming,X., Zhang,Y.H., Zhang,Y.,
            Liu,Z.Y., Yang,Y. and Pei,Z.J.
  TITLE     DARS2 overexpression is associated with PET/CT metabolic parameters
            and affects glycolytic activity in lung adenocarcinoma
  JOURNAL   J Transl Med 21 (1), 574 (2023)
   PUBMED   37626419
  REMARK    GeneRIF: DARS2 overexpression is associated with PET/CT metabolic
            parameters and affects glycolytic activity in lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Isohanni,P., Linnankivi,T., Buzkova,J., Lonnqvist,T., Pihko,H.,
            Valanne,L., Tienari,P.J., Elovaara,I., Pirttila,T., Reunanen,M.,
            Koivisto,K., Marjavaara,S. and Suomalainen,A.
  TITLE     DARS2 mutations in mitochondrial leucoencephalopathy and multiple
            sclerosis
  JOURNAL   J Med Genet 47 (1), 66-70 (2010)
   PUBMED   19592391
  REMARK    GeneRIF: DARS2 mutations cause childhood-to-adolescence onset
            leucoencephalopathy, but they do not seem to be associated with
            multiple sclerosis.
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Reiling,E., van Vliet-Ostaptchouk,J.V., van 't Riet,E., van
            Haeften,T.W., Arp,P.A., Hansen,T., Kremer,D., Groenewoud,M.J., van
            Hove,E.C., Romijn,J.A., Smit,J.W., Nijpels,G., Heine,R.J.,
            Uitterlinden,A.G., Pedersen,O., Slagboom,P.E., Maassen,J.A.,
            Hofker,M.H., 't Hart,L.M. and Dekker,J.M.
  TITLE     Genetic association analysis of 13 nuclear-encoded mitochondrial
            candidate genes with type II diabetes mellitus: the DAMAGE study
  JOURNAL   Eur J Hum Genet 17 (8), 1056-1062 (2009)
   PUBMED   19209188
  REMARK    GeneRIF: Meta-analysis of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 594)
  AUTHORS   Scheper,G.C., van der Klok,T., van Andel,R.J., van Berkel,C.G.,
            Sissler,M., Smet,J., Muravina,T.I., Serkov,S.V., Uziel,G.,
            Bugiani,M., Schiffmann,R., Krageloh-Mann,I., Smeitink,J.A.,
            Florentz,C., Van Coster,R., Pronk,J.C. and van der Knaap,M.S.
  TITLE     Mitochondrial aspartyl-tRNA synthetase deficiency causes
            leukoencephalopathy with brain stem and spinal cord involvement and
            lactate elevation
  JOURNAL   Nat Genet 39 (4), 534-539 (2007)
   PUBMED   17384640
  REMARK    GeneRIF: Mutations in DARS2, which encodes mitochondrial
            aspartyl-tRNA synthetase, in affected individuals with
            leukoencephalopathy with brain stem and spinal cord involvement and
            lactate elevation.
REFERENCE   8  (residues 1 to 594)
  AUTHORS   Bonnefond,L., Fender,A., Rudinger-Thirion,J., Giege,R., Florentz,C.
            and Sissler,M.
  TITLE     Toward the full set of human mitochondrial aminoacyl-tRNA
            synthetases: characterization of AspRS and TyrRS
  JOURNAL   Biochemistry 44 (12), 4805-4816 (2005)
   PUBMED   15779907
  REMARK    GeneRIF: The gene for mitochondrial aspartyl-tRNA synthetase is
            described and the initial characterization of the enzyme is
            reported. Genes for the remaining missing human synthetases have
            also been found with the exception of glutaminyl-tRNA synthetase.
REFERENCE   9  (residues 1 to 594)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 594)
  AUTHORS   Engelen,M., Abbink,T.E.M., Salomons,G.S. and van der Knaap,M.S.
  TITLE     Leukoencephalopathy with Brain Stem and Spinal Cord Involvement and
            Lactate Elevation
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20506600
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109921.21.
            
            On Aug 7, 2018 this sequence version replaced XP_006711490.1.
            
            Summary: The protein encoded by this gene belongs to the class-II
            aminoacyl-tRNA synthetase family. It is a mitochondrial enzyme that
            specifically aminoacylates aspartyl-tRNA. Mutations in this gene
            are associated with leukoencephalopathy with brainstem and spinal
            cord involvement and lactate elevation (LBSL). [provided by RefSeq,
            Nov 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.226068.1,
                                           SRR1803616.88977.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1"
     Protein         1..594
                     /product="aspartate--tRNA ligase, mitochondrial isoform 2"
                     /EC_number="6.1.1.12"
                     /note="aspartate tRNA ligase 2, mitochondrial;
                     aspartyl-tRNA synthetase, mitochondrial; aspartate--tRNA
                     ligase, mitochondrial"
                     /calculated_mol_wt=67555
     Region          50..585
                     /region_name="AspS"
                     /note="Aspartyl-tRNA synthetase [Translation, ribosomal
                     structure and biogenesis]; COG0173"
                     /db_xref="CDD:439943"
     CDS             1..594
                     /gene="DARS2"
                     /gene_synonym="ASPRS; LBSL; MT-ASPRS; mtAspRS"
                     /coded_by="NM_001365212.1:558..2342"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS91109.1"
                     /db_xref="GeneID:55157"
                     /db_xref="HGNC:HGNC:25538"
                     /db_xref="MIM:610956"
ORIGIN      
        1 myfpswlsql yrglsrpirr ttqpiwgsly rsllqssqrr ipefssfvvr tntcgelrss
       61 hlgqevtlcg wiqyrrqntf lvlrdfdglv qviipqdesa asvkkilcea pvesvvqvsg
      121 tvisrpagqe npkmptgeie ikvktaelln ackklpfeik nfvkktealr lqyryldlrs
      181 fqmqynlrlr sqmvmkmrey lcnlhgfvdi etptlfkrtp ggakeflvps repgkfyslp
      241 qspqqfkqll mvggldryfq varcyrdegs rpdrqpeftq idiemsfvdq tgiqsliegl
      301 lqyswpndkd pvvvpfptmt faevlatygt dkpdtrfgmk iidisdvfrn teigflqdal
      361 skphgtvkai cipegakylk rkdiesirnf aadhfnqcsl lgklrlecad lletrgvvlr
      421 dptlfsflwv vdfplflpke enprelesah hpftaphpsd ihllytepkk arsqhydlvl
      481 ngneigggsi rihnaelqry ilatllkedv kmlshllqal dygapphggi algldrlicl
      541 vtgspsirdv iafpksfrgh dlmsntpdsv ppeelkpyhi rvskptdska erah
//
LOCUS       NP_001357319             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357319
VERSION     NP_001357319.1
DBSOURCE    REFSEQ: accession NM_001370390.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.75871.1,
                                           SRR7346977.1561026.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370390.1:1354..3003"
                     /note="isoform 1 is encoded by transcript variant 19"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_078868                318 aa            linear   PRI 27-APR-2025
DEFINITION  polyprenal reductase isoform 1 [Homo sapiens].
ACCESSION   NP_078868
VERSION     NP_078868.1
DBSOURCE    REFSEQ: accession NM_024592.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lu,Y., Liu,Z., Zheng,Y., Liu,X., Liu,X., Chen,N., Mao,K. and Lin,W.
  TITLE     Analysis of the implication of steroid 5 alpha-reductase 3 on
            prognosis and immune microenvironment in Liver Hepatocellular
            Carcinoma
  JOURNAL   Ann Med 56 (1), 2408463 (2024)
   PUBMED   39340288
  REMARK    GeneRIF: Analysis of the implication of steroid 5 alpha-reductase 3
            on prognosis and immune microenvironment in Liver Hepatocellular
            Carcinoma.
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Wilson,M.P., Kentache,T., Althoff,C.R., Schulz,C., de
            Bettignies,G., Mateu Cabrera,G., Cimbalistiene,L., Burnyte,B.,
            Yoon,G., Costain,G., Vuillaumier-Barrot,S., Cheillan,D., Rymen,D.,
            Rychtarova,L., Hansikova,H., Bury,M., Dewulf,J.P., Caligiore,F.,
            Jaeken,J., Cantagrel,V., Van Schaftingen,E., Matthijs,G.,
            Foulquier,F. and Bommer,G.T.
  TITLE     A pseudoautosomal glycosylation disorder prompts the revision of
            dolichol biosynthesis
  JOURNAL   Cell 187 (14), 3585-3601 (2024)
   PUBMED   38821050
  REMARK    Erratum:[Cell. 2024 Jul 11;187(14):3784. doi:
            10.1016/j.cell.2024.06.004. PMID: 38870945]
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Zhang,Y.P., Na,W.T., Dai,X.Q., Li,R.F., Wang,J.X., Gao,T.,
            Zhang,W.B. and Xiang,C.
  TITLE     Over-expression of SRD5A3 and its prognostic significance in breast
            cancer
  JOURNAL   World J Surg Oncol 19 (1), 260 (2021)
   PUBMED   34465365
  REMARK    GeneRIF: Over-expression of SRD5A3 and its prognostic significance
            in breast cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Ben Ayed,I., Ouarda,W., Frikha,F., Kammoun,F., Souissi,A., Ben
            Said,M., Bouzid,A., Elloumi,I., Hamdani,T.M., Gharbi,N.,
            Baklouti,N., Guirat,M., Mejdoub,F., Kharrat,N., Boujelbene,I.,
            Abdelhedi,F., Belguith,N., Keskes,L., Gibriel,A.A., Kamoun,H.,
            Triki,C., Alimi,A.M. and Masmoudi,S.
  TITLE     SRD5A3-CDG: 3D structure modeling, clinical spectrum, and
            computer-based dysmorphic facial recognition
  JOURNAL   Am J Med Genet A 185 (4), 1081-1090 (2021)
   PUBMED   33403770
  REMARK    GeneRIF: SRD5A3-CDG: 3D structure modeling, clinical spectrum, and
            computer-based dysmorphic facial recognition.
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Mai,Q., Sheng,D., Chen,C., Gou,Q., Chen,M., Huang,X., Yin,H.,
            Chen,X. and Chen,Z.
  TITLE     Steroid 5 alpha-reductase 3 (SRD5A3) promotes tumor growth and
            predicts poor survival of human hepatocellular carcinoma (HCC)
  JOURNAL   Aging (Albany NY) 12 (24), 25395-25411 (2020)
   PUBMED   33229626
  REMARK    GeneRIF: Steroid 5 alpha-reductase 3 (SRD5A3) promotes tumor growth
            and predicts poor survival of human hepatocellular carcinoma (HCC).
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Kahrizi,K., Hu,C.H., Garshasbi,M., Abedini,S.S., Ghadami,S.,
            Kariminejad,R., Ullmann,R., Chen,W., Ropers,H.H., Kuss,A.W.,
            Najmabadi,H. and Tzschach,A.
  TITLE     Next generation sequencing in a family with autosomal recessive
            Kahrizi syndrome (OMIM 612713) reveals a homozygous frameshift
            mutation in SRD5A3
  JOURNAL   Eur J Hum Genet 19 (1), 115-117 (2011)
   PUBMED   20700148
  REMARK    GeneRIF: Next generation sequencing identified a homozygous
            frameshift mutation (c.203dupC; p.Phe69LeufsX2) SRD5A3 as the
            disease-causing change in Kahrizi syndrome.
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Cantagrel,V., Lefeber,D.J., Ng,B.G., Guan,Z., Silhavy,J.L.,
            Bielas,S.L., Lehle,L., Hombauer,H., Adamowicz,M., Swiezewska,E., De
            Brouwer,A.P., Blumel,P., Sykut-Cegielska,J., Houliston,S.,
            Swistun,D., Ali,B.R., Dobyns,W.B., Babovic-Vuksanovic,D., van
            Bokhoven,H., Wevers,R.A., Raetz,C.R., Freeze,H.H., Morava,E.,
            Al-Gazali,L. and Gleeson,J.G.
  TITLE     SRD5A3 is required for converting polyprenol to dolichol and is
            mutated in a congenital glycosylation disorder
  JOURNAL   Cell 142 (2), 203-217 (2010)
   PUBMED   20637498
  REMARK    GeneRIF: Study of a large consanguineous Emirati family showed that
            loss of function mutations of the SRD5A3 gene cause a multisystemic
            syndrome with eye malformations, cerebellar vermis hypoplasia, and
            psychomotor delay.
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Uemura,M., Tamura,K., Chung,S., Honma,S., Okuyama,A., Nakamura,Y.
            and Nakagawa,H.
  TITLE     Novel 5 alpha-steroid reductase (SRD5A3, type-3) is overexpressed
            in hormone-refractory prostate cancer
  JOURNAL   Cancer Sci 99 (1), 81-86 (2008)
   PUBMED   17986282
  REMARK    GeneRIF: Findings indicate that a novel type 3 5 alpha-steroid
            reductase, SRD5A3, is associated with DHT production and
            maintenance of androgen-androgen receptor-pathway activation in
            prostate cancer.
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Payne,A.H. and Hales,D.B.
  TITLE     Overview of steroidogenic enzymes in the pathway from cholesterol
            to active steroid hormones
  JOURNAL   Endocr Rev 25 (6), 947-970 (2004)
   PUBMED   15583024
  REMARK    Review article
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CX763068.1, AK023414.1,
            AC069200.6 and DB532427.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the steroid
            5-alpha reductase family, and polyprenol reductase subfamily. It is
            involved in the production of androgen 5-alpha-dihydrotestosterone
            (DHT) from testosterone, and maintenance of the androgen-androgen
            receptor activation pathway. This protein is also necessary for the
            conversion of polyprenol into dolichol, which is required for the
            synthesis of dolichol-linked monosaccharides and the
            oligosaccharide precursor used for N-linked glycosylation of
            proteins. Mutations in this gene are associated with congenital
            disorder of glycosylation type Iq. [provided by RefSeq, Mar 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL526960.3, SRR1803617.157348.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264228.9/ ENSP00000264228.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..318
                     /product="polyprenal reductase isoform 1"
                     /EC_number="1.3.1.22"
                     /EC_number="1.3.1.94"
                     /note="3-oxo-5-alpha-steroid 4-dehydrogenase 3; probable
                     polyprenol reductase; SR type 3; 3-oxo-5-alpha-steroid
                     4-dehydrogenase (NADP(+)); polyprenal reductase"
                     /calculated_mol_wt=36390
     Site            12..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8P0.1)"
     Region          69..318
                     /region_name="ICMT"
                     /note="Isoprenylcysteine carboxyl methyltransferase (ICMT)
                     family; cl21511"
                     /db_xref="CDD:473892"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8P0.1)"
     Site            118..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8P0.1)"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8P0.1)"
     Site            195..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8P0.1)"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8P0.1)"
     CDS             1..318
                     /gene="SRD5A3"
                     /gene_synonym="CDG1P; CDG1Q; KRIZI; S5AR; S5AR 3; SRD5A2L;
                     SRD5A2L1"
                     /coded_by="NM_024592.5:96..1052"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3498.1"
                     /db_xref="GeneID:79644"
                     /db_xref="HGNC:HGNC:25812"
                     /db_xref="MIM:611715"
ORIGIN      
        1 mapwaeaehs alnplravwl tltaaflltl llqllppgll pgcaifqdli rygktkcgep
       61 srpaacrafd vpkryfshfy iisvlwngfl lwcltqslfl gapfpswlhg llrilgaaqf
      121 qggelalsaf lvlvflwlhs lrrlfeclyv svfsnvmihv vqycfglvyy vlvgltvlsq
      181 vpmdgrnayi tgknllmqar wfhilgmmmf iwssahqykc hvilgnlrkn kagvvihcnh
      241 ripfgdwfey vsspnylael miyvsmavtf gfhnltwwlv vtnvffnqal saflshqfyk
      301 skfvsypkhr kaflpflf
//
LOCUS       NP_068572                198 aa            linear   PRI 27-APR-2025
DEFINITION  dnaJ homolog subfamily C member 12 isoform a [Homo sapiens].
ACCESSION   NP_068572
VERSION     NP_068572.1
DBSOURCE    REFSEQ: accession NM_021800.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Shen,M., Cao,S., Long,X., Xiao,L., Yang,L., Zhang,P., Li,L.,
            Chen,F., Lei,T., Gao,H., Ye,F. and Bu,H.
  TITLE     DNAJC12 causes breast cancer chemotherapy resistance by repressing
            doxorubicin-induced ferroptosis and apoptosis via activation of AKT
  JOURNAL   Redox Biol 70, 103035 (2024)
   PUBMED   38306757
  REMARK    GeneRIF: DNAJC12 causes breast cancer chemotherapy resistance by
            repressing doxorubicin-induced ferroptosis and apoptosis via
            activation of AKT.
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Deng,I.B., Follett,J., Bu,M. and Farrer,M.J.
  TITLE     DNAJC12 in Monoamine Metabolism, Neurodevelopment, and
            Neurodegeneration
  JOURNAL   Mov Disord 39 (2), 249-258 (2024)
   PUBMED   38014588
  REMARK    GeneRIF: DNAJC12 in Monoamine Metabolism, Neurodevelopment, and
            Neurodegeneration.
            Review article
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Gunes,D. and Senturk,L.
  TITLE     A rare cause of hyperphenylalaninemia: four cases from a single
            family with DNAJC12 deficiency
  JOURNAL   J Pediatr Endocrinol Metab 36 (8), 791-797 (2023)
   PUBMED   37283250
  REMARK    GeneRIF: A rare cause of hyperphenylalaninemia: four cases from a
            single family with DNAJC12 deficiency.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Porta,F., Neirotti,A. and Spada,M.
  TITLE     Restless legs syndrome in DNAJC12 deficiency
  JOURNAL   Neurol Sci 44 (6), 2167-2172 (2023)
   PUBMED   36897462
  REMARK    GeneRIF: Restless legs syndrome in DNAJC12 deficiency.
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Ciki,K., Yildiz,Y., Yucel Yilmaz,D., Pektas,E., Tokatli,A.,
            Ozgul,R.K., Sivri,H.S. and Dursun,A.
  TITLE     DNACJ12 deficiency in patients with unexplained
            hyperphenylalaninemia: two new patients and a novel variant
  JOURNAL   Metab Brain Dis 36 (6), 1405-1410 (2021)
   PUBMED   34014443
  REMARK    GeneRIF: DNACJ12 deficiency in patients with unexplained
            hyperphenylalaninemia: two new patients and a novel variant.
            Erratum:[Metab Brain Dis. 2021 Aug;36(6):1411. doi:
            10.1007/s11011-021-00759-8. PMID: 34106389]
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   7  (residues 1 to 198)
  AUTHORS   De Bessa,S.A., Salaorni,S., Patrao,D.F., Neto,M.M., Brentani,M.M.
            and Nagai,M.A.
  TITLE     JDP1 (DNAJC12/Hsp40) expression in breast cancer and its
            association with estrogen receptor status
  JOURNAL   Int J Mol Med 17 (2), 363-367 (2006)
   PUBMED   16391838
  REMARK    GeneRIF: JDP1 is a estrogen target gene and that its expression
            might be used as a marker of the estrogen transactivation activity
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Lee,J., Hahn,Y., Yun,J.H., Mita,K. and Chung,J.H.
  TITLE     Characterization of JDP genes, an evolutionarily conserved J
            domain-only protein family, from human and moths
  JOURNAL   Biochim Biophys Acta 1491 (1-3), 355-363 (2000)
   PUBMED   10760603
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133551.13, CB121724.1 and
            AF176012.1.
            
            Summary: This gene encodes a member of a subclass of the HSP40/DnaJ
            protein family. Members of this family of proteins are associated
            with complex assembly, protein folding, and export. Two transcript
            variants encoding distinct isoforms have been identified for this
            gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript, and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.130065.1,
                                           SRR1803612.41108.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267761 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000225171.7/ ENSP00000225171.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..198
                     /product="dnaJ homolog subfamily C member 12 isoform a"
                     /note="J domain protein 1; dnaJ homolog subfamily C member
                     12; J domain containing protein 1 (JDP1); j
                     domain-containing protein 1; DnaJ (Hsp40) homolog,
                     subfamily C, member 12"
                     /calculated_mol_wt=23284
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UKB3.1)"
     Region          14..76
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(42..44,53,56..57,60..61)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     Region          114..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKB3.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKB3.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R022; propagated from
                     UniProtKB/Swiss-Prot (Q9UKB3.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R022; propagated from
                     UniProtKB/Swiss-Prot (Q9UKB3.1)"
     CDS             1..198
                     /gene="DNAJC12"
                     /gene_synonym="HPANBH4; JDP1"
                     /coded_by="NM_021800.3:178..774"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7271.1"
                     /db_xref="GeneID:56521"
                     /db_xref="HGNC:HGNC:28908"
                     /db_xref="MIM:606060"
ORIGIN      
        1 mdailnyrse dtedyytllg cdelssveqi laefkvrale chpdkhpenp kavetfqklq
       61 kakeiltnee srarydhwrr sqmsmpfqqw ealndsvkts mhwvvrgkkd lmleesdkth
      121 ttkmeneecn eqrerkkeel astaekteqk epkpleksvs pqnsdssgfa dvngwhlrfr
      181 wskdapsell rkfrnyei
//
LOCUS       NP_997723                235 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 215 [Homo sapiens].
ACCESSION   NP_997723
VERSION     NP_997723.2
DBSOURCE    REFSEQ: accession NM_212558.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Liu,Y., Zheng,Q., He,G., Zhang,M., Yan,X., Yang,Z., Zhang,P.,
            Wang,L., Liu,J., Liang,L. and Han,H.
  TITLE     Transmembrane protein 215 promotes angiogenesis by maintaining
            endothelial cell survival
  JOURNAL   J Cell Physiol 234 (6), 9525-9534 (2019)
   PUBMED   30370660
  REMARK    GeneRIF: These results identified TMEM215 as a novel molecule
            involved in angiogenesis by regulating the survival of endothelial
            cells.
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Pajewski,N.M., Shrestha,S., Quinn,C.P., Parker,S.D., Wiener,H.,
            Aissani,B., McKinney,B.A., Poland,G.A., Edberg,J.C., Kimberly,R.P.,
            Tang,J. and Kaslow,R.A.
  TITLE     A genome-wide association study of host genetic determinants of the
            antibody response to Anthrax Vaccine Adsorbed
  JOURNAL   Vaccine 30 (32), 4778-4784 (2012)
   PUBMED   22658931
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX647550.1, AL157884.9 and BM681172.1.
            
            On Aug 18, 2007 this sequence version replaced NP_997723.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647550.1, AK125320.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342743.6/ ENSP00000345468.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..235
                     /product="transmembrane protein 215"
                     /calculated_mol_wt=25675
     Region          1..235
                     /region_name="TMEM215"
                     /note="TMEM215 family; pfam15746"
                     /db_xref="CDD:374072"
     Site            12..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68D42.1)"
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68D42.1)"
     Region          99..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68D42.1)"
     CDS             1..235
                     /gene="TMEM215"
                     /coded_by="NM_212558.3:325..1032"
                     /db_xref="CCDS:CCDS6530.1"
                     /db_xref="GeneID:401498"
                     /db_xref="HGNC:HGNC:33816"
ORIGIN      
        1 mrpddinprt glvvalvsvf lvfgfmftvs gmkgetlgni pllaigpaic lpgiaaiala
       61 rktegctkwp enellwvrkl pcfrkpkdke vvellrtpsd lesgkgssde lakkaglrgk
      121 pppqsqgevs vassinsptp teegecqslv qnghqeetsr yldgycpsgs sltysaldvk
      181 csardrsecp epedsiffvp qdsiivcsyk qnspydrycc yinqiqgrwd hetiv
//
LOCUS       NP_036476                410 aa            linear   PRI 27-APR-2025
DEFINITION  neurotensin receptor type 2 [Homo sapiens].
ACCESSION   NP_036476 XP_944391
VERSION     NP_036476.2
DBSOURCE    REFSEQ: accession NM_012344.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Ikhlef,L., Yassine,M., Chandouri,B., Riviere,L., Naves,T.,
            Dmytruk,N., Gachard,N., Jauberteau,M.O. and Gallet,P.F.
  TITLE     Targeting the NTSR2/TrkB oncogenic pathway in chronic lymphocytic
            leukemia
  JOURNAL   Sci Rep 14 (1), 6084 (2024)
   PUBMED   38480783
  REMARK    GeneRIF: Targeting the NTSR2/TrkB oncogenic pathway in chronic
            lymphocytic leukemia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Yang,Y., Zhang,W., Wei,K., Hu,F., Wu,S., Ma,Y. and Ouyang,Q.
  TITLE     Physiological and Pathological Roles of NTSR2 in Several Organs and
            Diseases (Review)
  JOURNAL   Protein Pept Lett 31 (1), 3-10 (2024)
   PUBMED   37962046
  REMARK    GeneRIF: Physiological and Pathological Roles of NTSR2 in Several
            Organs and Diseases (Review).
            Review article
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Qiu,S., Nikolaou,S., Zhu,J., Jeffery,P., Goldin,R., Kinross,J.,
            Alexander,J.L., Rasheed,S., Tekkis,P. and Kontovounisios,C.
  TITLE     Characterisation of the Expression of Neurotensin and Its Receptors
            in Human Colorectal Cancer and Its Clinical Implications
  JOURNAL   Biomolecules 10 (8), 1145 (2020)
   PUBMED   32764278
  REMARK    GeneRIF: Characterisation of the Expression of Neurotensin and Its
            Receptors in Human Colorectal Cancer and Its Clinical Implications.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Zhu,S., Tian,H., Niu,X., Wang,J., Li,X., Jiang,N., Wen,S., Chen,X.,
            Ren,S., Xu,C., Chang,C., Flores-Morales,A., Shang,Z., Sun,Y. and
            Niu,Y.
  TITLE     Neurotensin and its receptors mediate neuroendocrine
            transdifferentiation in prostate cancer
  JOURNAL   Oncogene 38 (24), 4875-4884 (2019)
   PUBMED   30770901
  REMARK    GeneRIF: A novel role of NTS in the development of
            Castration-resistant prostate cancer with Neuroendocrine
            differentiation (NED), and a possible strategy to prevent the onset
            of NED by targeting the NTS signaling pathway.
            Erratum:[Oncogene. 2019 Jun;38(24):4885. doi:
            10.1038/s41388-019-0827-1. PMID: 31048775]
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Abbaci,A., Talbot,H., Saada,S., Gachard,N., Abraham,J., Jaccard,A.,
            Bordessoule,D., Fauchais,A.L., Naves,T. and Jauberteau,M.O.
  TITLE     Neurotensin receptor type 2 protects B-cell chronic lymphocytic
            leukemia cells from apoptosis
  JOURNAL   Oncogene 37 (6), 756-767 (2018)
   PUBMED   29059151
  REMARK    GeneRIF: High NTSR2 expression is associated with B-cell chronic
            lymphocytic leukemia.
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Martin,S., Vincent,J.P. and Mazella,J.
  TITLE     Recycling ability of the mouse and the human neurotensin type 2
            receptors depends on a single tyrosine residue
  JOURNAL   J Cell Sci 115 (Pt 1), 165-173 (2002)
   PUBMED   11801734
  REMARK    GeneRIF: Recycling ability depends on a single tyrosine residue
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Ramez,M., Bagot,M., Nikolova,M., Boumsell,L., Vita,N., Chalon,P.,
            Caput,D., Ferrara,P. and Bensussan,A.
  TITLE     Functional characterization of neurotensin receptors in human
            cutaneous T cell lymphoma malignant lymphocytes
  JOURNAL   J Invest Dermatol 117 (3), 687-693 (2001)
   PUBMED   11564178
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Vincent,J.P., Mazella,J. and Kitabgi,P.
  TITLE     Neurotensin and neurotensin receptors
  JOURNAL   Trends Pharmacol Sci 20 (7), 302-309 (1999)
   PUBMED   10390649
  REMARK    Review article
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Vita,N., Oury-Donat,F., Chalon,P., Guillemot,M., Kaghad,M.,
            Bachy,A., Thurneyssen,O., Garcia,S., Poinot-Chazel,C., Casellas,P.,
            Keane,P., Le Fur,G., Maffrand,J.P., Soubrie,P., Caput,D. and
            Ferrara,P.
  TITLE     Neurotensin is an antagonist of the human neurotensin NT2 receptor
            expressed in Chinese hamster ovary cells
  JOURNAL   Eur J Pharmacol 360 (2-3), 265-272 (1998)
   PUBMED   9851594
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Chalon,P., Vita,N., Kaghad,M., Guillemot,M., Bonnin,J., Delpech,B.,
            Le Fur,G., Ferrara,P. and Caput,D.
  TITLE     Molecular cloning of a levocabastine-sensitive neurotensin binding
            site
  JOURNAL   FEBS Lett 386 (2-3), 91-94 (1996)
   PUBMED   8647296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106875.5 and AC110754.3.
            
            On Nov 23, 2018 this sequence version replaced NP_036476.1.
            
            Summary: The protein encoded by this gene belongs to the G
            protein-coupled receptor family that activate a
            phosphatidylinositol-calcium second messenger system. Binding and
            pharmacological studies demonstrate that this receptor binds
            neurotensin as well as several other ligands already described for
            neurotensin NT1 receptor. However, unlike NT1 receptor, this gene
            recognizes, with high affinity, levocabastine, a histamine H1
            receptor antagonist previously shown to compete with neurotensin
            for low-affinity binding sites in brain. These activities suggest
            that this receptor may be of physiological importance and that a
            natural agonist for the receptor may exist. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.9445.1,
                                           SRR3476690.1178643.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306928.6/ ENSP00000303686.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..410
                     /product="neurotensin receptor type 2"
                     /note="neurotensin receptor, type 2;
                     levocabastine-sensitive neurotensin receptor; NT-R-2"
                     /calculated_mol_wt=45254
     Region          33..369
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Site            33..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95665.2)"
     Region          35..59
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            65..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95665.2)"
     Region          69..91
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          109..131
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            110..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95665.2)"
     Region          154..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            155..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95665.2)"
     Region          204..227
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            218..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95665.2)"
     Region          296..318
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95665.2)"
     Region          337..362
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            338..358
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95665.2)"
     Region          381..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95665.2)"
     CDS             1..410
                     /gene="NTSR2"
                     /gene_synonym="NTR2"
                     /coded_by="NM_012344.4:67..1299"
                     /db_xref="CCDS:CCDS1681.1"
                     /db_xref="GeneID:23620"
                     /db_xref="HGNC:HGNC:8040"
                     /db_xref="MIM:605538"
ORIGIN      
        1 metssprppr pssnpglsld arlgvdtrlw akvlftalya liwalgaagn alsahvvlka
       61 ragragrlrh hvlslalagl llllvgvpve lysfvwfhyp wvfgdlgcrg yyfvhelcay
      121 atvlsvagls aerclavcqp lrarslltpr rtrwlvalsw aaslglalpm avimgqkhel
      181 etadgepepa srvctvlvsr talqvfiqvn vlvsfvlpla ltaflngvtv shllalcsqv
      241 pststpgsst psrlellsee gllsfivwkk tfiqggqvsl vrhkdvrrir slqrsvqvlr
      301 aivvmyvicw lpyharrlmy cyvpddawtd plynfyhyfy mvtntlfyvs savtpllyna
      361 vsssfrklfl eavsslcgeh hpmkrlppkp qsptlmdtas gfgdppetrt
//
LOCUS       NP_001129580             440 aa            linear   PRI 27-APR-2025
DEFINITION  R3H and coiled-coil domain-containing protein 1 isoform a [Homo
            sapiens].
ACCESSION   NP_001129580 XP_001716473 XP_114618 XP_944412
VERSION     NP_001129580.2
DBSOURCE    REFSEQ: accession NM_001136108.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Kanesada,K., Tsunedomi,R., Hazama,S., Ogihara,H., Hamamoto,Y.,
            Shindo,Y., Matsui,H., Tokumitsu,Y., Yoshida,S., Iida,M., Suzuki,N.,
            Takeda,S., Ioka,T. and Nagano,H.
  TITLE     Association between a single nucleotide polymorphism in the R3HCC1
            gene and irinotecan toxicity
  JOURNAL   Cancer Med 12 (4), 4294-4305 (2023)
   PUBMED   36308049
  REMARK    GeneRIF: Association between a single nucleotide polymorphism in
            the R3HCC1 gene and irinotecan toxicity.
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Lee,S., Liu,B., Lee,S., Huang,S.X., Shen,B. and Qian,S.B.
  TITLE     Global mapping of translation initiation sites in mammalian cells
            at single-nucleotide resolution
  JOURNAL   Proc Natl Acad Sci U S A 109 (37), E2424-E2432 (2012)
   PUBMED   22927429
  REMARK    GeneRIF: Ribosome profiling indicates that this gene can use a
            non-AUG (CUG) start codon in both human HEK293 and mouse embryonic
            fibroblast cells.
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Diaz,M., Lopez-Bermejo,A., Petry,C.J., de Zegher,F. and Ibanez,L.
  TITLE     Efficacy of metformin therapy in adolescent girls with androgen
            excess: relation to sex hormone-binding globulin and androgen
            receptor polymorphisms
  JOURNAL   Fertil Steril 94 (7), 2800-3 (2010)
   PUBMED   20691435
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Kashima,I., Jonas,S., Jayachandran,U., Buchwald,G., Conti,E.,
            Lupas,A.N. and Izaurralde,E.
  TITLE     SMG6 interacts with the exon junction complex via two conserved
            EJC-binding motifs (EBMs) required for nonsense-mediated mRNA decay
  JOURNAL   Genes Dev 24 (21), 2440-2450 (2010)
   PUBMED   20930030
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC143829.1 and BC032421.1.
            
            On Aug 28, 2014 this sequence version replaced NP_001129580.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.870080.1,
                                           SRR1660803.152523.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match       :: ENST00000265806.12/ ENSP00000265806.8
            non-AUG initiation codon :: PMID: 22927429
            RefSeq Select criteria   :: based on conservation, expression,
                                        longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..440
                     /product="R3H and coiled-coil domain-containing protein 1
                     isoform a"
                     /note="R3H and coiled-coil domain-containing protein 1"
                     /calculated_mol_wt=48961
     Region          19..80
                     /region_name="R3H_unknown_1"
                     /note="R3H domain of a group of eukaryotic proteins with
                     unknown function. The name of the R3H domain comes from
                     the characteristic spacing of the most conserved arginine
                     and histidine residues. The function of the domain is
                     predicted to bind ssDNA or ssRNA in...; cd02638"
                     /db_xref="CDD:100067"
     Site            order(49,53)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100067"
     Region          154..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3T6.3)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3T6.3)"
     Region          254..276
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3T6.3)"
     Region          318..382
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..440
                     /gene="R3HCC1"
                     /coded_by="NM_001136108.3:69..1391"
                     /note="isoform a is encoded by transcript variant 1;
                     non-AUG (CUG) translation initiation codon"
                     /db_xref="CCDS:CCDS47826.2"
                     /db_xref="GeneID:203069"
                     /db_xref="HGNC:HGNC:27329"
ORIGIN      
        1 mallcldgvf lssaendfvh riqeeldrfl lqkqlskvll fpplssrlry lihrtaenfd
       61 llssfsvgeg wkrrtvichq dirvpssdgl sgpcrapasc psryhgprpi snqgaaavpr
      121 garagrwyrg rkpdqplyvp rvlrrqeewg ltstsvlkre apagrdpeep gdvgagdpns
      181 dqglpvlmtq gtedlkgpgq rceneplldp vgpeplgpes qsgkgdmvem atrfgstlql
      241 dlekgkesll ekrlvaeeee deeeveedgp sscseddyse llqeitdnlt kkeiqiekih
      301 ldtssfveel pgekdlahvv eiydfepalk tedllatfse fqekgfriqw vddthalgif
      361 pclasaaeal trefsvlkir pltqgtkqsk lkalqrpkll rlvkerpqtn atvarrlvar
      421 alglqhkkke rpavrgplpp
//
LOCUS       NP_055431               1177 aa            linear   PRI 27-APR-2025
DEFINITION  phospholipid-transporting ATPase IF [Homo sapiens].
ACCESSION   NP_055431 XP_087254
VERSION     NP_055431.1
DBSOURCE    REFSEQ: accession NM_014616.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1177)
  AUTHORS   Dong,N., Qi,W., Wu,L., Li,J., Zhang,X., Wu,H., Zhang,W., Jiang,J.,
            Zhang,S., Fu,W., Liu,Q., Qi,G., Wang,L., Lu,Y., Luo,J., Kong,Y.,
            Liu,Y., Zhao,R.C. and Wang,J.
  TITLE     LINC00606 promotes glioblastoma progression through sponge
            miR-486-3p and interaction with ATP11B
  JOURNAL   J Exp Clin Cancer Res 43 (1), 139 (2024)
   PUBMED   38725030
  REMARK    GeneRIF: LINC00606 promotes glioblastoma progression through sponge
            miR-486-3p and interaction with ATP11B.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1177)
  AUTHORS   Yu,W.K., Wang,Y.C., Gao,Y., Shi,C.H., Fan,Y., Yu,L.L., Zhao,Z.C.,
            Li,S.S., Xu,Y.M. and Li,Y.S.
  TITLE     Genetic analysis of the ATP11B gene in Chinese Han population with
            cerebral small vessel disease
  JOURNAL   BMC Genomics 23 (1), 822 (2022)
   PUBMED   36510145
  REMARK    GeneRIF: Genetic analysis of the ATP11B gene in Chinese Han
            population with cerebral small vessel disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1177)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1177)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   5  (residues 1 to 1177)
  AUTHORS   Tone,T., Nakayama,K., Takatsu,H. and Shin,H.W.
  TITLE     ATPase reaction cycle of P4-ATPases affects their transport from
            the endoplasmic reticulum
  JOURNAL   FEBS Lett 594 (3), 412-423 (2020)
   PUBMED   31571211
REFERENCE   6  (residues 1 to 1177)
  AUTHORS   Muzny,D.M., Scherer,S.E., Kaul,R., Wang,J., Yu,J., Sudbrak,R.,
            Buhay,C.J., Chen,R., Cree,A., Ding,Y., Dugan-Rocha,S., Gill,R.,
            Gunaratne,P., Harris,R.A., Hawes,A.C., Hernandez,J., Hodgson,A.V.,
            Hume,J., Jackson,A., Khan,Z.M., Kovar-Smith,C., Lewis,L.R.,
            Lozado,R.J., Metzker,M.L., Milosavljevic,A., Miner,G.R.,
            Morgan,M.B., Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z.,
            Steffen,D., Wei,S., Wheeler,D.A., Wright,M.W., Worley,K.C.,
            Yuan,Y., Zhang,Z., Adams,C.Q., Ansari-Lari,M.A., Ayele,M.,
            Brown,M.J., Chen,G., Chen,Z., Clendenning,J.,
            Clerc-Blankenburg,K.P., Chen,R., Chen,Z., Davis,C., Delgado,O.,
            Dinh,H.H., Dong,W., Draper,H., Ernst,S., Fu,G.,
            Gonzalez-Garay,M.L., Garcia,D.K., Gillett,W., Gu,J., Hao,B.,
            Haugen,E., Havlak,P., He,X., Hennig,S., Hu,S., Huang,W.,
            Jackson,L.R., Jacob,L.S., Kelly,S.H., Kube,M., Levy,R., Li,Z.,
            Liu,B., Liu,J., Liu,W., Lu,J., Maheshwari,M., Nguyen,B.V.,
            Okwuonu,G.O., Palmeiri,A., Pasternak,S., Perez,L.M., Phelps,K.A.,
            Plopper,F.J., Qiang,B., Raymond,C., Rodriguez,R.,
            Saenphimmachak,C., Santibanez,J., Shen,H., Shen,Y., Subramanian,S.,
            Tabor,P.E., Verduzco,D., Waldron,L., Wang,J., Wang,J., Wang,Q.,
            Williams,G.A., Wong,G.K., Yao,Z., Zhang,J., Zhang,X., Zhao,G.,
            Zhou,J., Zhou,Y., Nelson,D., Lehrach,H., Reinhardt,R., Naylor,S.L.,
            Yang,H., Olson,M., Weinstock,G. and Gibbs,R.A.
  TITLE     The DNA sequence, annotation and analysis of human chromosome 3
  JOURNAL   Nature 440 (7088), 1194-1198 (2006)
   PUBMED   16641997
REFERENCE   7  (residues 1 to 1177)
  AUTHORS   Paulusma,C.C. and Oude Elferink,R.P.
  TITLE     The type 4 subfamily of P-type ATPases, putative aminophospholipid
            translocases with a role in human disease
  JOURNAL   Biochim Biophys Acta 1741 (1-2), 11-24 (2005)
   PUBMED   15919184
  REMARK    Review article
REFERENCE   8  (residues 1 to 1177)
  AUTHORS   Kuhlbrandt,W.
  TITLE     Biology, structure and mechanism of P-type ATPases
  JOURNAL   Nat Rev Mol Cell Biol 5 (4), 282-295 (2004)
   PUBMED   15071553
  REMARK    Review article
REFERENCE   9  (residues 1 to 1177)
  AUTHORS   Halleck,M.S., Schlegel,R.A. and Williamson,P.L.
  TITLE     Reanalysis of ATP11B, a type IV P-type ATPase
  JOURNAL   J Biol Chem 277 (12), 9736-9740 (2002)
   PUBMED   11790799
  REMARK    GeneRIF: the region containing transmembrane domain 4,
            corresponding to exon 12, is present in the human homolog of the
            gene, ATP11B
REFERENCE   10 (residues 1 to 1177)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI861412.1, DR000074.1, AK296750.1, AF156548.1, BX489704.1,
            AK304855.1, AL133061.1 and AB023173.1.
            
            On Apr 21, 2005 this sequence version replaced XP_087254.5.
            
            Summary: P-type ATPases, such as ATP11B, are phosphorylated in
            their intermediate state and drive uphill transport of ions across
            membranes. Several subfamilies of P-type ATPases have been
            identified. One subfamily transports heavy metal ions, such as
            Cu(2+) or Cd(2+). Another subfamily transports non-heavy metal
            ions, such as H(+), Na(+), K(+), or Ca(+). A third subfamily
            transports amphipaths, such as phosphatidylserine.[supplied by
            OMIM, Feb 2005].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.242189.1,
                                           SRR1803613.136294.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323116.10/ ENSP00000321195.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.33"
     Protein         1..1177
                     /product="phospholipid-transporting ATPase IF"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase IF;
                     ATPase IR; P4-ATPase flippase complex alpha subunit
                     ATP11B; ATPase, class VI, type 11B"
                     /calculated_mol_wt=134059
     Region          41..979
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            56..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     Site            83..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     Site            290..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     Site            342..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     Site            order(407..409,572,595..597,659,706..708,794,797,800,821,
                     824)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            407..413
                     /site_type="other"
                     /note="P-type ATPase signature motif"
                     /db_xref="CDD:319770"
     Site            407
                     /site_type="phosphorylation"
                     /note="phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:319770"
     Site            877..898
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     Site            911..930
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     Site            961..982
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     Site            998..1020
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     Site            1026..1047
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     Site            1066..1090
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     Site            1154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9Y2G3.2)"
     CDS             1..1177
                     /gene="ATP11B"
                     /gene_synonym="ATPIF; ATPIR"
                     /coded_by="NM_014616.3:257..3790"
                     /db_xref="CCDS:CCDS33896.1"
                     /db_xref="GeneID:23200"
                     /db_xref="HGNC:HGNC:13553"
                     /db_xref="MIM:605869"
ORIGIN      
        1 mwrwirqqlg fdpphqsdtr tiyvanrfpq nglytpqkfi dnriisskyt vwnfvpknlf
       61 eqfrrvanfy fliiflvqlm idtptspvts glplffvitv taikqgyedw lrhnsdnevn
      121 gapvyvvrsg glvktrskni rvgdivriak deifpadlvl lssdrldgsc hvttasldge
      181 tnlkthvavp etallqtvan ldtlvaviec qqpeadlyrf mgrmiitqqm eeivrplgpe
      241 slllrgarlk ntkeifgvav ytgmetkmal nyksksqkrs aveksmntfl iiylvilise
      301 avistilkyt wqaeekwdep wynqktehqr nsskilrfis dflaflvlyn fiipislyvt
      361 vemqkflgsf figwdldlyh eesdqkaqvn tsdlneelgq veyvftdktg tltenemqfr
      421 ecsingmkyq eingrlvpeg ptpdssegnl sylsslshln nlshlttsss frtspenete
      481 likehdlffk avslchtvqi snvqtdctgd gpwqsnlaps qleyyasspd ekalveaaar
      541 igivfignse etmevktlgk lerykllhil efdsdrrrms vivqapsgek llfakgaess
      601 ilpkciggei ektrihvdef alkglrtlci ayrkftskey eeidkrifea rtalqqreek
      661 laavfqfiek dlillgatav edrlqdkvre tiealrmagi kvwvltgdkh etavsvslsc
      721 ghfhrtmnil elinqksdse caeqlrqlar ritedhviqh glvvdgtsls lalreheklf
      781 mevcrncsav lccrmaplqk akvirlikis pekpitlavg dgandvsmiq eahvgigimg
      841 kegrqaarns dyaiarfkfl skllfvhghf yyiriatlvq yffyknvcfi tpqflyqfyc
      901 lfsqqtlyds vyltlynicf tslpiliysl leqhvdphvl qnkptlyrdi sknrllsikt
      961 flywtilgfs hafifffgsy lligkdtsll gngqmfgnwt fgtlvftvmv itvtvkmale
     1021 thfwtwinhl vtwgsiifyf vfslfyggil wpflgsqnmy fvfiqllssg sawfaiilmv
     1081 vtclfldiik kvfdrhlhpt stekaqltet nagikcldsm ccfpegeaac asvgrmlerv
     1141 igrcspthis rswsasdpfy tndrsiltls tmdsstc
//
LOCUS       NP_291020                156 aa            linear   PRI 27-APR-2025
DEFINITION  protein SYS1 homolog isoform a [Homo sapiens].
ACCESSION   NP_291020
VERSION     NP_291020.1
DBSOURCE    REFSEQ: accession NM_033542.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Behnia,R., Panic,B., Whyte,J.R. and Munro,S.
  TITLE     Targeting of the Arf-like GTPase Arl3p to the Golgi requires
            N-terminal acetylation and the membrane protein Sys1p
  JOURNAL   Nat Cell Biol 6 (5), 405-413 (2004)
   PUBMED   15077113
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA526637.1 and AL591714.1.
            
            Summary: SYS1 forms a complex with ADP-ribosylation factor-related
            protein ARFRP1 (MIM 604699) and targets ARFRP1 to the Golgi
            apparatus (Behnia et al., 2004 [PubMed 15077113]).[supplied by
            OMIM, Aug 2009].
            
            Transcript Variant: This variant encodes the longer isoform (a).
            Both variants 1 and 3 encode the same isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL591714.1, AK075264.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000243918.10/ ENSP00000243918.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..156
                     /product="protein SYS1 homolog isoform a"
                     /note="protein SYS1 homolog; SYS1 Golgi-localized integral
                     membrane protein homolog"
                     /calculated_mol_wt=17484
     Region          5..148
                     /region_name="SYS1"
                     /note="Integral membrane protein S linking to the trans
                     Golgi network; pfam09801"
                     /db_xref="CDD:370705"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N2H4.1)"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N2H4.1)"
     Site            91..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N2H4.1)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N2H4.1)"
     CDS             1..156
                     /gene="SYS1"
                     /gene_synonym="C20orf169; dJ453C12.4; dJ453C12.4.1"
                     /coded_by="NM_033542.4:164..634"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13351.1"
                     /db_xref="GeneID:90196"
                     /db_xref="HGNC:HGNC:16162"
                     /db_xref="MIM:612979"
ORIGIN      
        1 magqfrsyvw dpllilsqiv lmqtvyygsl glwlalvdgl vrsspsldqm fdaeilgfst
       61 ppgrlsmmsf ilnaltcalg llyfirrgkq cldftvtvhf fhllgcwfys srfpsaltww
      121 lvqavcialm avigeylcmr telkeiplns apksnv
//
LOCUS       NP_001077362             797 aa            linear   PRI 27-APR-2025
DEFINITION  striatin-3 isoform 1 [Homo sapiens].
ACCESSION   NP_001077362
VERSION     NP_001077362.1
DBSOURCE    REFSEQ: accession NM_001083893.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Zhu,J., Tang,W., Fang,P., Wang,C., Gu,M., Yang,W., Pan,B., Wang,B.
            and Guo,W.
  TITLE     STRN3 promotes tumour growth in hepatocellular carcinoma by
            inhibiting the hippo pathway
  JOURNAL   J Cell Mol Med 28 (6), e18147 (2024)
   PUBMED   38429901
  REMARK    GeneRIF: STRN3 promotes tumour growth in hepatocellular carcinoma
            by inhibiting the hippo pathway.
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Liu,L., Weber,A., Linne,U., Shehata,M., Pleschka,S., Kracht,M. and
            Schmitz,M.L.
  TITLE     Phosphorylation of Influenza A Virus Matrix Protein 1 at Threonine
            108 Controls Its Multimerization State and Functional Association
            with the STRIPAK Complex
  JOURNAL   mBio 14 (1), e0323122 (2023)
   PUBMED   36602306
  REMARK    GeneRIF: Phosphorylation of Influenza A Virus Matrix Protein 1 at
            Threonine 108 Controls Its Multimerization State and Functional
            Association with the STRIPAK Complex.
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Bisoyi,P., Devi,P., Besra,K., Prasad,A., Jain,B.P. and Goswami,S.K.
  TITLE     The profile of expression of the scaffold protein SG2NA(s) differs
            between cancer types and its interactome in normal vis-a-vis breast
            tumor tissues suggests its wide roles in regulating multiple
            cellular pathways
  JOURNAL   Mol Cell Biochem 477 (6), 1653-1668 (2022)
   PUBMED   35230605
  REMARK    GeneRIF: The profile of expression of the scaffold protein SG2NA(s)
            differs between cancer types and its interactome in normal
            vis-a-vis breast tumor tissues suggests its wide roles in
            regulating multiple cellular pathways.
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 797)
  AUTHORS   Baillat,G., Moqrich,A., Castets,F., Baude,A., Bailly,Y.,
            Benmerah,A. and Monneron,A.
  TITLE     Molecular cloning and characterization of phocein, a protein found
            from the Golgi complex to dendritic spines
  JOURNAL   Mol Biol Cell 12 (3), 663-673 (2001)
   PUBMED   11251078
REFERENCE   7  (residues 1 to 797)
  AUTHORS   Castets,F., Rakitina,T., Gaillard,S., Moqrich,A., Mattei,M.G. and
            Monneron,A.
  TITLE     Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat
            proteins principally expressed in the brain
  JOURNAL   J Biol Chem 275 (26), 19970-19977 (2000)
   PUBMED   10748158
REFERENCE   8  (residues 1 to 797)
  AUTHORS   Moreno,C.S., Park,S., Nelson,K., Ashby,D., Hubalek,F., Lane,W.S.
            and Pallas,D.C.
  TITLE     WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are
            members of a novel family of calmodulin-binding proteins that
            associate with protein phosphatase 2A
  JOURNAL   J Biol Chem 275 (8), 5257-5263 (2000)
   PUBMED   10681496
REFERENCE   9  (residues 1 to 797)
  AUTHORS   Muro,Y., Chan,E.K., Landberg,G. and Tan,E.M.
  TITLE     A cell-cycle nuclear autoantigen containing WD-40 motifs expressed
            mainly in S and G2 phase cells
  JOURNAL   Biochem Biophys Res Commun 207 (3), 1029-1037 (1995)
   PUBMED   7864889
REFERENCE   10 (residues 1 to 797)
  AUTHORS   Landberg,G. and Tan,E.M.
  TITLE     Characterization of a DNA-binding nuclear autoantigen mainly
            associated with S phase and G2 cells
  JOURNAL   Exp Cell Res 212 (2), 255-261 (1994)
   PUBMED   7910562
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA854600.1, BC132673.1, AF243424.1, AL049830.3 and AA572712.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1), also known as the
            beta isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2689399.1,
                                           SRR11853567.8877.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357479.10/ ENSP00000350071.5
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..797
                     /product="striatin-3 isoform 1"
                     /note="nuclear autoantigen; cell cycle S/G2 nuclear
                     autoantigen; s/G2 antigen; cell cycle autoantigen SG2NA;
                     striatin, calmodulin binding protein 3; protein
                     phosphatase 2 regulatory subunit B'''beta"
                     /calculated_mol_wt=87079
     Region          1..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13033.3)"
     Region          65..190
                     /region_name="Striatin"
                     /note="Striatin family; pfam08232"
                     /db_xref="CDD:462401"
     Region          71..79
                     /region_name="Caveolin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P58405; propagated from
                     UniProtKB/Swiss-Prot (Q13033.3)"
     Region          166..183
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG2; propagated from
                     UniProtKB/Swiss-Prot (Q13033.3)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13033.3)"
     Region          224..278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Region          313..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG2; propagated from
                     UniProtKB/Swiss-Prot (Q13033.3)"
     Region          475..796
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          478..517
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Site            order(479,497,501,507..508,531..532,550,554,560..561,
                     584..585,602,607,613..614,631,649,653,659..660,672..673,
                     698,702,708..709,721..722,739,744,750..751,763..764,786,
                     790,796)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          485..531
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          531..570
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Region          537..584
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          584..623
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Region          589..626
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          635..671
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          679..718
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Region          684..720
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          721..760
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Region          726..765
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          767..797
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13033.3)"
     Region          772..796
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..797
                     /gene="STRN3"
                     /gene_synonym="PPP2R6B; S/G2NA; SG2NA"
                     /coded_by="NM_001083893.2:195..2588"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41938.1"
                     /db_xref="GeneID:29966"
                     /db_xref="HGNC:HGNC:15720"
                     /db_xref="MIM:614766"
ORIGIN      
        1 mdelaggggg gpgmaapprq qqgpggnlgl spggngaagg ggppasegag paagpelsrp
       61 qqytipgilh yiqhewarfe merahwever aelqariafl qgerkgqenl kkdlvrrikm
      121 leyalkqera kyhklkygte lnqgdlkmpt feseetkdte aptapqnsql twkqgrqllr
      181 qylqevgytd tildvrsqrv rsllglsnse pngsvetknl eqilnggesp kqkgqeikrs
      241 sgdvletfnf lenaddsded eendmiegip egkdkhrmnk hkigneglaa dltddpdtee
      301 alkefdflvt aedgegagea rssgdgtewd kddlsptaev wdvdqglisk lkeqykkerk
      361 gkkgvkranr tklydmiadl gddelphips giinqsrsas trmtdhegar aeeaepitfp
      421 sgggksfimg sddvllsvlg lgdladltvt ndadysydlp ankdafrktw npkytlrshf
      481 dgvralafhp vepvlvtase dhtlklwnlq ktvpakksas ldvepiytfr ahigpvlsla
      541 issngeqcfs ggidatiqww nmpspsvdpy dtyepnvlag tlvghtdavw glaysgiknq
      601 llscsadgtv rlwnpqeklp cictyngdkk hgiptsvdfi gcdpahmvts fntgsaviyd
      661 letsqslvil ssqvdsglqs nnhinrvvsh ptlpvtitah edrhikffdn ktgkmihsmv
      721 ahldavtsla vdpngiylms gshdcsirlw nldsktcvqe itahrkklde siydvafhss
      781 kayiasagad alakvfv
//
LOCUS       NP_001940                465 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor E2F3 isoform 1 [Homo sapiens].
ACCESSION   NP_001940
VERSION     NP_001940.1
DBSOURCE    REFSEQ: accession NM_001949.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Xie,W., Shao,Y., Bo,Q., Li,Z., Yu,Q., Wang,L. and Wu,G.
  TITLE     FTO promotes the progression of retinoblastoma through
            YTHDF2-dependent N6-methyladenosine modification in E2F3
  JOURNAL   Mol Carcinog 63 (5), 926-937 (2024)
   PUBMED   38380957
  REMARK    GeneRIF: FTO promotes the progression of retinoblastoma through
            YTHDF2-dependent N6-methyladenosine modification in E2F3.
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Zhang,X.B., Song,Y., Lai,Y.T., Qiu,S.Z., Hu,A.K., Li,D.X.,
            Zheng,N.S., Zeng,H.Q. and Lin,Q.C.
  TITLE     MiR-210-3p enhances intermittent hypoxia-induced tumor progression
            via inhibition of E2F3
  JOURNAL   Sleep Breath 28 (2), 607-617 (2024)
   PUBMED   37775619
  REMARK    GeneRIF: MiR-210-3p enhances intermittent hypoxia-induced tumor
            progression via inhibition of E2F3.
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Pan,X., Xu,C., Cheng,G., Chen,Z., Liu,M. and Mei,Y.
  TITLE     Transcription factor E2F3 activates CDC25B to regulate DNA damage
            and promote mitoxantrone resistance in stomach adenocarcinoma
  JOURNAL   Mol Biol Rep 51 (1), 90 (2024)
   PUBMED   38194158
  REMARK    GeneRIF: Transcription factor E2F3 activates CDC25B to regulate DNA
            damage and promote mitoxantrone resistance in stomach
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Chen,H.Z., Tsai,S.Y. and Leone,G.
  TITLE     Emerging roles of E2Fs in cancer: an exit from cell cycle control
  JOURNAL   Nat Rev Cancer 9 (11), 785-797 (2009)
   PUBMED   19851314
  REMARK    Review article
REFERENCE   5  (residues 1 to 465)
  AUTHORS   He,Y., Armanious,M.K., Thomas,M.J. and Cress,W.D.
  TITLE     Identification of E2F-3B, an alternative form of E2F-3 lacking a
            conserved N-terminal region
  JOURNAL   Oncogene 19 (30), 3422-3433 (2000)
   PUBMED   10918599
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Leone,G., Nuckolls,F., Ishida,S., Adams,M., Sears,R., Jakoi,L.,
            Miron,A. and Nevins,J.R.
  TITLE     Identification of a novel E2F3 product suggests a mechanism for
            determining specificity of repression by Rb proteins
  JOURNAL   Mol Cell Biol 20 (10), 3626-3632 (2000)
   PUBMED   10779352
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Magae,J., Wu,C.L., Illenye,S., Harlow,E. and Heintz,N.H.
  TITLE     Nuclear localization of DP and E2F transcription factors by
            heterodimeric partners and retinoblastoma protein family members
  JOURNAL   J Cell Sci 109 (Pt 7), 1717-1726 (1996)
   PUBMED   8832394
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Karlseder,J., Rotheneder,H. and Wintersberger,E.
  TITLE     Interaction of Sp1 with the growth- and cell cycle-regulated
            transcription factor E2F
  JOURNAL   Mol Cell Biol 16 (4), 1659-1667 (1996)
   PUBMED   8657141
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Wu,C.L., Zukerberg,L.R., Ngwu,C., Harlow,E. and Lees,J.A.
  TITLE     In vivo association of E2F and DP family proteins
  JOURNAL   Mol Cell Biol 15 (5), 2536-2546 (1995)
   PUBMED   7739537
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Lees,J.A., Saito,M., Vidal,M., Valentine,M., Look,T., Harlow,E.,
            Dyson,N. and Helin,K.
  TITLE     The retinoblastoma protein binds to a family of E2F transcription
            factors
  JOURNAL   Mol Cell Biol 13 (12), 7813-7825 (1993)
   PUBMED   8246996
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL132775.29, Y10479.1,
            AL136303.15 and BU633769.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of a small family of
            transcription factors that function through binding of DP
            interaction partner proteins. The encoded protein recognizes a
            specific sequence motif in DNA and interacts directly with the
            retinoblastoma protein (pRB) to regulate the expression of genes
            involved in the cell cycle. Altered copy number and activity of
            this gene have been observed in a number of human cancers. There
            are pseudogenes for this gene on chromosomes 2 and 17. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Mar 2013].
            
            Transcript Variant: This variant (1, also known as a) represents
            the longer transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y10479.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000346618.8/ ENSP00000262904.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.3"
     Protein         1..465
                     /product="transcription factor E2F3 isoform 1"
                     /note="transcription factor E2F3"
                     /calculated_mol_wt=49031
     Region          96..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00716.1)"
     Region          101..153
                     /region_name="Cyclin A/CDK2 binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00716.1)"
     Region          102
                     /region_name="Alternative start codon"
                     /note="reported in PMID: 10918599."
     Region          179..243
                     /region_name="E2F_TDP"
                     /note="E2F/DP family winged-helix DNA-binding domain;
                     pfam02319"
                     /db_xref="CDD:460530"
     Region          204..225
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (O00716.1)"
     Region          209..245
                     /region_name="DEF box"
                     /note="propagated from UniProtKB/Swiss-Prot (O00716.1)"
     Region          246..337
                     /region_name="Dimerization. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00716.1)"
     Region          254..354
                     /region_name="E2F_DD"
                     /note="Dimerization domain of E2F transcription factors;
                     cd14660"
                     /db_xref="CDD:271137"
     Region          254..289
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:271137"
     Site            order(255..256,259..260,262..263,266..267,269..270,
                     273..274,276..277,279..281,283..284,287,295..300,303..304,
                     307,311..319,334..341,343..346,348,354)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271137"
     Site            order(321..330,332..333,335)
                     /site_type="other"
                     /note="RbC binding site [polypeptide binding]"
                     /db_xref="CDD:271137"
     Region          357..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00716.1)"
     Region          391..465
                     /region_name="Transactivation. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00716.1)"
     Region          432..449
                     /region_name="Retinoblastoma protein binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00716.1)"
     CDS             1..465
                     /gene="E2F3"
                     /gene_synonym="E2F-3"
                     /coded_by="NM_001949.5:355..1752"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4545.1"
                     /db_xref="GeneID:1871"
                     /db_xref="HGNC:HGNC:3115"
                     /db_xref="MIM:600427"
ORIGIN      
        1 mrkgiqpale qylvtaggge gaavvaaaaa asmdkralla spgfaaaaaa aaapgayiqi
       61 lttntsttsc ssslqsgava agpllpsapg aeqtagslly ttphgpssra gllqqppalg
      121 rggsgggggp pakrrlelge sghqylsdgl ktpkgkgraa lrspdspktp kspsektryd
      181 tslglltkkf iqllsqspdg vldlnkaaev lkvqkrriyd itnvlegihl ikkksknnvq
      241 wmgcslsedg gmlaqcqgls kevtelsqee kkldeliqsc tldlkllted senqrlayvt
      301 yqdirkisgl kdqtvivvka ppetrlevpd sieslqihla stqgpievyl cpeetethsp
      361 mktnnqdhng nipkpaskdl astnsghsdc svsmgnlspl aspanllqqt edqipsnleg
      421 pfvnllppll qedyllslge eegisdlfda ydleklplve dfmcs
//
LOCUS       NP_066363               1918 aa            linear   PRI 27-APR-2025
DEFINITION  NFX1-type zinc finger-containing protein 1 [Homo sapiens].
ACCESSION   NP_066363
VERSION     NP_066363.1
DBSOURCE    REFSEQ: accession NM_021035.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1918)
  AUTHORS   Wang,Z., She,D., Liu,L., Hua,X., Zhu,H., Yu,L., Wang,H., Zhu,Y.,
            Fan,G., Wang,Y., Xu,M. and Zhou,G.
  TITLE     Circular RNA CircSATB2 facilitates osteosarcoma progression through
            regulating the miR-661/FUS-mediated mRNA of ZNFX1
  JOURNAL   Cell Signal 114, 110977 (2024)
   PUBMED   37984605
  REMARK    GeneRIF: Circular RNA CircSATB2 facilitates osteosarcoma
            progression through regulating the miR-661/FUS-mediated mRNA of
            ZNFX1.
REFERENCE   2  (residues 1 to 1918)
  AUTHORS   Gu,Y., Wang,G. and Xu,H.
  TITLE     Long non-coding RNA ZNFX1 antisense 1 (ZFAS1) suppresses
            anti-oxidative stress in chondrocytes during osteoarthritis by
            sponging microRNA-1323
  JOURNAL   Bioengineered 13 (5), 13188-13200 (2022)
   PUBMED   35635081
  REMARK    GeneRIF: Long non-coding RNA ZNFX1 antisense 1 (ZFAS1) suppresses
            anti-oxidative stress in chondrocytes during osteoarthritis by
            sponging microRNA-1323.
REFERENCE   3  (residues 1 to 1918)
  AUTHORS   Alawbathani,S., Westenberger,A., Ordonez-Herrera,N., Al-Hilali,M.,
            Al Hebby,H., Alabbas,F., Alhashem,A.M., Elyamany,G., Megarbane,A.,
            Kose,M., Alhashmi,N., Al Sukaiti,N., Al-Raqad,M., Al-Tawalbeh,S.,
            Abu Adas Blanco,O., Alkhattabi,F., Sng,D., Al-Ali,R., Khan,S.,
            Tawamie,H., Tripolszki,K., Karageorgou,V., Trunzo,R., Al
            Mutairi,F., Reversade,B., Bauer,P. and Bertoli-Avella,A.M.
  TITLE     Biallelic ZNFX1 variants are associated with a spectrum of
            immuno-hematological abnormalities
  JOURNAL   Clin Genet 101 (2), 247-254 (2022)
   PUBMED   34708404
  REMARK    GeneRIF: Biallelic ZNFX1 variants are associated with a spectrum of
            immuno-hematological abnormalities.
REFERENCE   4  (residues 1 to 1918)
  AUTHORS   Vavassori,S., Chou,J., Faletti,L.E., Haunerdinger,V., Opitz,L.,
            Joset,P., Fraser,C.J., Prader,S., Gao,X., Schuch,L.A., Wagner,M.,
            Hoefele,J., Maccari,M.E., Zhu,Y., Elakis,G., Gabbett,M.T.,
            Forstner,M., Omran,H., Kaiser,T., Kessler,C., Olbrich,H., Frosk,P.,
            Almutairi,A., Platt,C.D., Elkins,M., Weeks,S., Rubin,T., Planas,R.,
            Marchetti,T., Koovely,D., Klambt,V., Soliman,N.A., von
            Hardenberg,S., Klemann,C., Baumann,U., Lenz,D., Klein-Franke,A.,
            Schwemmle,M., Huber,M., Sturm,E., Hartleif,S., Haffner,K.,
            Gimpel,C., Brotschi,B., Laube,G., Gungor,T., Buckley,M.F.,
            Kottke,R., Staufner,C., Hildebrandt,F., Reu-Hofer,S., Moll,S.,
            Weber,A., Kaur,H., Ehl,S., Hiller,S., Geha,R., Roscioli,T.,
            Griese,M. and Pachlopnik Schmid,J.
  TITLE     Multisystem inflammation and susceptibility to viral infections in
            human ZNFX1 deficiency
  JOURNAL   J Allergy Clin Immunol 148 (2), 381-393 (2021)
   PUBMED   33872655
  REMARK    GeneRIF: Multisystem inflammation and susceptibility to viral
            infections in human ZNFX1 deficiency.
REFERENCE   5  (residues 1 to 1918)
  AUTHORS   Le Voyer,T., Neehus,A.L., Yang,R., Ogishi,M., Rosain,J., Alroqi,F.,
            Alshalan,M., Blumental,S., Al Ali,F., Khan,T., Ata,M., Rozen,L.,
            Demulder,A., Bastard,P., Gruber,C., Roynard,M., Seeleuthener,Y.,
            Rapaport,F., Bigio,B., Chrabieh,M., Sng,D., Berteloot,L.,
            Boddaert,N., Rozenberg,F., Al-Muhsen,S., Bertoli-Avella,A.,
            Abel,L., Bogunovic,D., Marr,N., Mansouri,D., Al Mutairi,F.,
            Beziat,V., Weil,D., Mahdaviani,S.A., Ferster,A., Zhang,S.Y.,
            Reversade,B., Boisson-Dupuis,S., Casanova,J.L. and Bustamante,J.
  TITLE     Inherited deficiency of stress granule ZNFX1 in patients with
            monocytosis and mycobacterial disease
  JOURNAL   Proc Natl Acad Sci U S A 118 (15) (2021)
   PUBMED   33876776
  REMARK    GeneRIF: Inherited deficiency of stress granule ZNFX1 in patients
            with monocytosis and mycobacterial disease.
REFERENCE   6  (residues 1 to 1918)
  AUTHORS   Lango Allen,H., Estrada,K., Lettre,G., Berndt,S.I., Weedon,M.N.,
            Rivadeneira,F., Willer,C.J., Jackson,A.U., Vedantam,S.,
            Raychaudhuri,S., Ferreira,T., Wood,A.R., Weyant,R.J., Segre,A.V.,
            Speliotes,E.K., Wheeler,E., Soranzo,N., Park,J.H., Yang,J.,
            Gudbjartsson,D., Heard-Costa,N.L., Randall,J.C., Qi,L., Vernon
            Smith,A., Magi,R., Pastinen,T., Liang,L., Heid,I.M., Luan,J.,
            Thorleifsson,G., Winkler,T.W., Goddard,M.E., Sin Lo,K., Palmer,C.,
            Workalemahu,T., Aulchenko,Y.S., Johansson,A., Zillikens,M.C.,
            Feitosa,M.F., Esko,T., Johnson,T., Ketkar,S., Kraft,P., Mangino,M.,
            Prokopenko,I., Absher,D., Albrecht,E., Ernst,F., Glazer,N.L.,
            Hayward,C., Hottenga,J.J., Jacobs,K.B., Knowles,J.W., Kutalik,Z.,
            Monda,K.L., Polasek,O., Preuss,M., Rayner,N.W., Robertson,N.R.,
            Steinthorsdottir,V., Tyrer,J.P., Voight,B.F., Wiklund,F., Xu,J.,
            Zhao,J.H., Nyholt,D.R., Pellikka,N., Perola,M., Perry,J.R.,
            Surakka,I., Tammesoo,M.L., Altmaier,E.L., Amin,N., Aspelund,T.,
            Bhangale,T., Boucher,G., Chasman,D.I., Chen,C., Coin,L.,
            Cooper,M.N., Dixon,A.L., Gibson,Q., Grundberg,E., Hao,K., Juhani
            Junttila,M., Kaplan,L.M., Kettunen,J., Konig,I.R., Kwan,T.,
            Lawrence,R.W., Levinson,D.F., Lorentzon,M., McKnight,B.,
            Morris,A.P., Muller,M., Suh Ngwa,J., Purcell,S., Rafelt,S.,
            Salem,R.M., Salvi,E., Sanna,S., Shi,J., Sovio,U., Thompson,J.R.,
            Turchin,M.C., Vandenput,L., Verlaan,D.J., Vitart,V., White,C.C.,
            Ziegler,A., Almgren,P., Balmforth,A.J., Campbell,H., Citterio,L.,
            De Grandi,A., Dominiczak,A., Duan,J., Elliott,P., Elosua,R.,
            Eriksson,J.G., Freimer,N.B., Geus,E.J., Glorioso,N., Haiqing,S.,
            Hartikainen,A.L., Havulinna,A.S., Hicks,A.A., Hui,J., Igl,W.,
            Illig,T., Jula,A., Kajantie,E., Kilpelainen,T.O., Koiranen,M.,
            Kolcic,I., Koskinen,S., Kovacs,P., Laitinen,J., Liu,J., Lokki,M.L.,
            Marusic,A., Maschio,A., Meitinger,T., Mulas,A., Pare,G.,
            Parker,A.N., Peden,J.F., Petersmann,A., Pichler,I.,
            Pietilainen,K.H., Pouta,A., Ridderstrale,M., Rotter,J.I.,
            Sambrook,J.G., Sanders,A.R., Schmidt,C.O., Sinisalo,J., Smit,J.H.,
            Stringham,H.M., Bragi Walters,G., Widen,E., Wild,S.H.,
            Willemsen,G., Zagato,L., Zgaga,L., Zitting,P., Alavere,H.,
            Farrall,M., McArdle,W.L., Nelis,M., Peters,M.J., Ripatti,S., van
            Meurs,J.B., Aben,K.K., Ardlie,K.G., Beckmann,J.S., Beilby,J.P.,
            Bergman,R.N., Bergmann,S., Collins,F.S., Cusi,D., den Heijer,M.,
            Eiriksdottir,G., Gejman,P.V., Hall,A.S., Hamsten,A., Huikuri,H.V.,
            Iribarren,C., Kahonen,M., Kaprio,J., Kathiresan,S., Kiemeney,L.,
            Kocher,T., Launer,L.J., Lehtimaki,T., Melander,O., Mosley,T.H. Jr.,
            Musk,A.W., Nieminen,M.S., O'Donnell,C.J., Ohlsson,C., Oostra,B.,
            Palmer,L.J., Raitakari,O., Ridker,P.M., Rioux,J.D., Rissanen,A.,
            Rivolta,C., Schunkert,H., Shuldiner,A.R., Siscovick,D.S.,
            Stumvoll,M., Tonjes,A., Tuomilehto,J., van Ommen,G.J., Viikari,J.,
            Heath,A.C., Martin,N.G., Montgomery,G.W., Province,M.A., Kayser,M.,
            Arnold,A.M., Atwood,L.D., Boerwinkle,E., Chanock,S.J., Deloukas,P.,
            Gieger,C., Gronberg,H., Hall,P., Hattersley,A.T., Hengstenberg,C.,
            Hoffman,W., Lathrop,G.M., Salomaa,V., Schreiber,S., Uda,M.,
            Waterworth,D., Wright,A.F., Assimes,T.L., Barroso,I., Hofman,A.,
            Mohlke,K.L., Boomsma,D.I., Caulfield,M.J., Cupples,L.A.,
            Erdmann,J., Fox,C.S., Gudnason,V., Gyllensten,U., Harris,T.B.,
            Hayes,R.B., Jarvelin,M.R., Mooser,V., Munroe,P.B., Ouwehand,W.H.,
            Penninx,B.W., Pramstaller,P.P., Quertermous,T., Rudan,I.,
            Samani,N.J., Spector,T.D., Volzke,H., Watkins,H., Wilson,J.F.,
            Groop,L.C., Haritunians,T., Hu,F.B., Kaplan,R.C., Metspalu,A.,
            North,K.E., Schlessinger,D., Wareham,N.J., Hunter,D.J.,
            O'Connell,J.R., Strachan,D.P., Wichmann,H.E., Borecki,I.B., van
            Duijn,C.M., Schadt,E.E., Thorsteinsdottir,U., Peltonen,L.,
            Uitterlinden,A.G., Visscher,P.M., Chatterjee,N., Loos,R.J.,
            Boehnke,M., McCarthy,M.I., Ingelsson,E., Lindgren,C.M.,
            Abecasis,G.R., Stefansson,K., Frayling,T.M. and Hirschhorn,J.N.
  TITLE     Hundreds of variants clustered in genomic loci and biological
            pathways affect human height
  JOURNAL   Nature 467 (7317), 832-838 (2010)
   PUBMED   20881960
REFERENCE   7  (residues 1 to 1918)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   8  (residues 1 to 1918)
  AUTHORS   Dunphy,E.J. and McNeel,D.G.
  TITLE     Antigen-specific IgG elicited in subjects with prostate cancer
            treated with flt3 ligand
  JOURNAL   J Immunother 28 (3), 268-275 (2005)
   PUBMED   15838384
  REMARK    GeneRIF: MAD-CaP-5 (KIAA1404) is a novel prostate cancer antigen.
REFERENCE   9  (residues 1 to 1918)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 1918)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK096594.1, AB037825.2, DA809204.1, AU140771.1 and AL049766.14.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB037825.2, SRR14038194.859988.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396105.6/ ENSP00000379412.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1918
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.13"
     Protein         1..1918
                     /product="NFX1-type zinc finger-containing protein 1"
                     /calculated_mol_wt=220097
     Region          1..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2E3.2)"
     Region          75..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2E3.2)"
     Region          543..>636
                     /region_name="RecD"
                     /note="ATPase/5#-3# helicase helicase subunit RecD of the
                     DNA repair enzyme RecBCD (exonuclease V) [Replication,
                     recombination and repair]; COG0507"
                     /db_xref="CDD:440273"
     Region          598..>681
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            621..627
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          796..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2E3.2)"
     Region          876..896
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2E3.2)"
     Region          <978..1073
                     /region_name="EEXXEc_NFX1"
                     /note="EEXXE-box helicase domain of NFX1; cd17936"
                     /db_xref="CDD:350694"
     Region          1075..1251
                     /region_name="SF1_C_Upf1"
                     /note="C-terminal helicase domain of Upf1-like family
                     helicases; cd18808"
                     /db_xref="CDD:350195"
     Site            order(1159..1161,1183,1185..1186,1201)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350195"
     Site            order(1189,1191,1223)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350195"
     Region          1372..1417
                     /region_name="NF-X1-zinc-finger"
                     /note="Presumably a zinc binding domain, which has been
                     shown to bind to DNA in the human nuclear transcriptional
                     repressor NF-X1. The zinc finger can be characterized by
                     the pattern
                     C-X(1-6)-H-X-C-X3-C(H/C)-X(3-4)-(H/C)-X(1-10)-C. The NF-X1
                     zinc finger...; cd06008"
                     /db_xref="CDD:100116"
     Region          1461..1505
                     /region_name="NF-X1-zinc-finger"
                     /note="Presumably a zinc binding domain, which has been
                     shown to bind to DNA in the human nuclear transcriptional
                     repressor NF-X1. The zinc finger can be characterized by
                     the pattern
                     C-X(1-6)-H-X-C-X3-C(H/C)-X(3-4)-(H/C)-X(1-10)-C. The NF-X1
                     zinc finger...; cd06008"
                     /db_xref="CDD:100116"
     Region          1484..1561
                     /region_name="LELP1"
                     /note="Late cornified envelope-like proline-rich protein
                     1; pfam15042"
                     /db_xref="CDD:464464"
     Region          1843..1889
                     /region_name="DUF6539"
                     /note="Family of unknown function (DUF6539); pfam20173"
                     /db_xref="CDD:466324"
     CDS             1..1918
                     /gene="ZNFX1"
                     /gene_synonym="IMD91"
                     /coded_by="NM_021035.3:86..5842"
                     /db_xref="CCDS:CCDS13417.1"
                     /db_xref="GeneID:57169"
                     /db_xref="HGNC:HGNC:29271"
                     /db_xref="MIM:618931"
ORIGIN      
        1 meerrphlda rprnshtnhr gpvdgelppr arnqannppa nalrggashp grhprannhp
       61 aaywqreerf ramgrnphqg rrnqeghasd eardqrhdqe ndtrwrngnq dcrnrrppws
      121 ndnfqqwrtp hqkpteqpqq akklgykfle sllqkdpsev vitlatslgl kellshssmk
      181 snflelicqv lrkacsskmd rqsvlhvlgi lknskflkvc lpayvvgmit epipdirnqy
      241 pehisniisl lqdlvsvfpa ssvqetsmlv sllptslnal rasgvdieee teknlekvqt
      301 iiehlqekrr egtlrvdtyt lvqpeaedhv esyrtmpiyp tynevhlder pflrpniisg
      361 kydstaiyld thfrllredf vrplregile llqsfedqgl rkrkfddiri yfdtriitpm
      421 csssgivykv qfdtkplkfv rwqnskrlly gslvcmskdn fetflfatvs nreqedlcrg
      481 ivqlcfneqs qqllaevqps dsflmvetta yfeayrhvle glqevqeedv pfqrnivecn
      541 shvkepryll mggrydftpl ienpsatgef lrnveglrhp rinvldpgqw pskealkldd
      601 sqmealqfal trelaiiqgp pgtgktyvgl kivqalltne svwqislqkf pilvvcytnh
      661 aldqflegiy ncqktsivrv ggrsnseilk qftlrelrnk refrrnlpmh lrraymsimt
      721 qmkeseqelh egaktlectm rgvlreqylq kyispqhwes lmngpvqdse wicfqhwkhs
      781 mmlewlglgv gsftqsvspa gpentaqaeg deeeegeees slieiaeead liqadrviee
      841 eevvrpqrrk keesgadqel akmllamrld hcgtgtaagq eqatgewqtq rnqkkkmkkr
      901 vkdelrklnt mtaaeaneie dvwqldlssr wqlyrlwlql yqadtrrkil syerqyrtsa
      961 ermaelrlqe dlhilkdaqv vgmtttgaak yrqilqkvep riviveeaae vleahtiatl
     1021 skacqhlili gdhqqlrpsa nvydlaknfn levslferlv kvnipfvrln yqhrmcpeia
     1081 rlltphiyqd lenhpsvlky ekikgvssnl ffvehnfpeq eiqegkshqn qheahfvvel
     1141 ckyflcqeyl psqitiltty tgqlfclrkl mpaktfagvr vhvvdkyqge endiillslv
     1201 rsnqegkvgf lqisnricva lsrakkgmyc ignmqmlakv plwskiihtl rennqigpml
     1261 rlccqnhpet htlvskasdf qkvpeggcsl pcefrlgcgh vctrachpyd sshkefqcmk
     1321 pcqkvicqeg hrcplvcfqe cqpcqvkvpk tiprcgheqm vpcsvpesdf ccqepcsksl
     1381 rcghrcshpc gedcvqlcse mvtiklkcgh sqpvkcghve gllyggllvk cttkcgtild
     1441 cghpcpgsch scfegrfher cqqpckrlli cshkcqepci gecppcqrtc qnrcvhsqck
     1501 kkcgelcspc vepcvwrcqh yqctklcsep cnrppcyvpc tkllvcghpc iglcgepcpk
     1561 kcrichmdev tqiffgfede pdarfvqled cshifevqal drymneqkdd evairlkvcp
     1621 icqvpirknl rygtsikqrl eeieiikeki qgsageiats qerlkaller ksllhqllpe
     1681 dflmlkekla qknlsvkdlg lvenyisfyd hlaslwdslk kmhvleekrv rtrleqvhew
     1741 lakkrlsfts qelsdlrsei qrltylvnll trykiaekkv kdsiavevys vqnilektck
     1801 ftqedeqlvq ekmealkatl pcsglgisee ervqivsaig yprghwfkcr nghiyvigdc
     1861 ggamergtcp dckeviggtn htlersnqla semdgaqhaa wsdtannlmn feeiqgmm
//
LOCUS       NP_776993                636 aa            linear   MAM 27-APR-2025
DEFINITION  polyadenylate-binding protein 1 [Bos taurus].
ACCESSION   NP_776993 XP_001255740
VERSION     NP_776993.1
DBSOURCE    REFSEQ: accession NM_174568.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Cosson,B., Berkova,N., Couturier,A., Chabelskaya,S., Philippe,M.
            and Zhouravleva,G.
  TITLE     Poly(A)-binding protein and eRF3 are associated in vivo in human
            and Xenopus cells
  JOURNAL   Biol Cell 94 (4-5), 205-216 (2002)
   PUBMED   12489690
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EH131059.1, EE252928.1, EV617074.1, DV806286.1, EE252871.1 and
            DV850814.1.
            
            On Jan 14, 2007 this sequence version replaced XP_001255740.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5721699.47.1, GGVC01087092.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA6648753, SAMEA6648754
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="14"
                     /map="14"
                     /breed="Hereford"
     Protein         1..636
                     /product="polyadenylate-binding protein 1"
                     /note="poly(A)-binding protein 1"
                     /calculated_mol_wt=70540
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Region          11..615
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Region          166..289
                     /region_name="CSDE1-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P61286.1)"
     Site            299
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            385
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            419
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            432
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            436
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            455
                     /site_type="methylation"
                     /note="Omega-N-methylated arginine, by CARM1.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            460
                     /site_type="methylation"
                     /note="Omega-N-methylated arginine, by CARM1.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            475
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P29341; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            481
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            493
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11940; Dimethylated
                     arginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11940;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            506
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            512
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     Site            518
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (P61286.1)"
     CDS             1..636
                     /gene="PABPC1"
                     /gene_synonym="PABP-1"
                     /coded_by="NM_174568.3:515..2425"
                     /db_xref="GeneID:282296"
                     /db_xref="VGNC:VGNC:53870"
ORIGIN      
        1 mnpsapsypm aslyvgdlhp dvteamlyek fspagpilsi rvcrdmitrr slgyayvnfq
       61 qpadaerald tmnfdvikgk pvrimwsqrd pslrksgvgn ifiknldksi dnkalydtfs
      121 afgnilsckv vcdengskgy gfvhfetqea aeraiekmng mllndrkvfv grfksrkere
      181 aelgarakef tnvyiknfge dmdderlkdl fgkfgpalsv kvmtdesgks kgfgfvsfer
      241 hedaqkavde mngkelngkq iyvgraqkkv erqtelkrkf eqmkqdritr yqgvnlyvkn
      301 lddgidderl rkefspfgti tsakvmmegg rskgfgfvcf sspeeatkav temngrivat
      361 kplyvalaqr keerqahltn qymqrmasvr avpnpvinpy qpappsgyfm aaipqtqnra
      421 ayyppsqiaq lrpsprwtaq garphpfqnm pgairpaapr ppfstmrpas sqvprvmstq
      481 rvantstqtm gprpaaaaaa atpavrtvpq ykyaagvrnp qqhlnaqpqv tmqqpavhvq
      541 gqepltasml asappqeqkq mlgerlfpli qamhptlagk itgmlleidn sellhmlesp
      601 eslrskvdea vavlqahqak eaaqkavnsa tgvptv
//
LOCUS       NP_001231682             233 aa            linear   PRI 27-APR-2025
DEFINITION  low affinity immunoglobulin gamma Fc region receptor III-B isoform
            2 precursor [Homo sapiens].
ACCESSION   NP_001231682
VERSION     NP_001231682.2
DBSOURCE    REFSEQ: accession NM_001244753.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Aslam,M.M., John,P., Fan,K.H., Malik,J.M., Feingold,E.,
            Demirci,F.Y. and Kamboh,M.I.
  TITLE     Association of Fc Gamma Receptor 3B Gene Copy Number Variation with
            Rheumatoid Arthritis Susceptibility
  JOURNAL   Genes (Basel) 13 (12), 2238 (2022)
   PUBMED   36553504
  REMARK    GeneRIF: Association of Fc Gamma Receptor 3B Gene Copy Number
            Variation with Rheumatoid Arthritis Susceptibility.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Minguela,A., Salido,E.J., Soto-Ramirez,M.F., Olga,M.A., Leal,J.D.,
            Garcia-Garay,M.C., Periago,A., Berenguer,M., Blanque,M. and
            Campillo,J.A.
  TITLE     Low-affinity immunoglobulin gamma Fc region receptor III-B
            (FcgammaRIIIB, CD16B) deficiency in patients with blood and immune
            system disorders
  JOURNAL   Br J Haematol 195 (5), 743-747 (2021)
   PUBMED   34544201
  REMARK    GeneRIF: Low-affinity immunoglobulin gamma Fc region receptor III-B
            (FcgammaRIIIB, CD16B) deficiency in patients with blood and immune
            system disorders.
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Nasr,A., Aljada,A., Hamid,O., Elsheikh,H.A., Masuadi,E.,
            Al-Bawab,A., Alenazi,T.H., Abushouk,A. and Salah,A.M.
  TITLE     Significant differences in FcgammaRIIa, FcgammaRIIIa and
            FcgammaRIIIb genes polymorphism and anti-malarial IgG subclass
            pattern are associated with severe Plasmodium falciparum malaria in
            Saudi children
  JOURNAL   Malar J 20 (1), 376 (2021)
   PUBMED   34551786
  REMARK    GeneRIF: Significant differences in FcgammaRIIa, FcgammaRIIIa and
            FcgammaRIIIb genes polymorphism and anti-malarial IgG subclass
            pattern are associated with severe Plasmodium falciparum malaria in
            Saudi children.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Moraru,M., Perez-Portilla,A., Al-Akioui Sanz,K.,
            Blazquez-Moreno,A., Arnaiz-Villena,A., Reyburn,H.T. and Vilches,C.
  TITLE     FCGR Genetic Variation in Two Populations From Ecuador
            Highlands-Extensive Copy-Number Variation, Distinctive Distribution
            of Functional Polymorphisms, and a Novel, Locally Common, Chimeric
            FCGR3B/A (CD16B/A) Gene
  JOURNAL   Front Immunol 12, 615645 (2021)
   PUBMED   34108956
  REMARK    GeneRIF: FCGR Genetic Variation in Two Populations From Ecuador
            Highlands-Extensive Copy-Number Variation, Distinctive Distribution
            of Functional Polymorphisms, and a Novel, Locally Common, Chimeric
            FCGR3B/A (CD16B/A) Gene.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Lanier,L.L., Yu,G. and Phillips,J.H.
  TITLE     Analysis of Fc gamma RIII (CD16) membrane expression and
            association with CD3 zeta and Fc epsilon RI-gamma by site-directed
            mutation
  JOURNAL   J Immunol 146 (5), 1571-1576 (1991)
   PUBMED   1825220
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Qiu,W.Q., de Bruin,D., Brownstein,B.H., Pearse,R. and Ravetch,J.V.
  TITLE     Organization of the human and mouse low-affinity Fc gamma R genes:
            duplication and recombination
  JOURNAL   Science 248 (4956), 732-735 (1990)
   PUBMED   2139735
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Ravetch,J.V. and Perussia,B.
  TITLE     Alternative membrane forms of Fc gamma RIII(CD16) on human natural
            killer cells and neutrophils. Cell type-specific expression of two
            genes that differ in single nucleotide substitutions
  JOURNAL   J Exp Med 170 (2), 481-497 (1989)
   PUBMED   2526846
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Scallon,B.J., Scigliano,E., Freedman,V.H., Miedel,M.C., Pan,Y.C.,
            Unkeless,J.C. and Kochan,J.P.
  TITLE     A human immunoglobulin G receptor exists in both
            polypeptide-anchored and phosphatidylinositol-glycan-anchored forms
  JOURNAL   Proc Natl Acad Sci U S A 86 (13), 5079-5083 (1989)
   PUBMED   2525780
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Peltz,G.A., Grundy,H.O., Lebo,R.V., Yssel,H., Barsh,G.S. and
            Moore,K.W.
  TITLE     Human Fc gamma RIII: cloning, expression, and identification of the
            chromosomal locus of two Fc receptors for IgG
  JOURNAL   Proc Natl Acad Sci U S A 86 (3), 1013-1017 (1989)
   PUBMED   2521732
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Simmons,D. and Seed,B.
  TITLE     The Fc gamma receptor of natural killer cells is a
            phospholipid-linked membrane protein
  JOURNAL   Nature 333 (6173), 568-570 (1988)
   PUBMED   2967436
  REMARK    Erratum:[Nature 1989 Aug 24;340(6235):662]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M24854.1, AL451067.12, X16863.1
            and AJ581669.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 31, 2018 this sequence version replaced NP_001231682.1.
            
            Summary: The protein encoded by this gene is a low affinity
            receptor for the Fc region of gamma immunoglobulins (IgG). The
            encoded protein acts as a monomer and can bind either monomeric or
            aggregated IgG. This gene may function to capture immune complexes
            in the peripheral circulation. Several transcript variants encoding
            different isoforms have been found for this gene. A highly-similar
            gene encoding a related protein is also found on chromosome 1.
            [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (2). Variants 1 and 2 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ581669.1, SRR1660805.239720.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000650385.1/ ENSP00000497461.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..233
                     /product="low affinity immunoglobulin gamma Fc region
                     receptor III-B isoform 2 precursor"
                     /note="low affinity immunoglobulin gamma Fc region
                     receptor III-B; Fc fragment of IgG receptor IIIb;
                     FcgammaRIIIb; Fc fragment of IgG, low affinity IIIb,
                     receptor (CD16b); Fc-gamma receptor IIIb (CD 16); Fc gamma
                     receptor III-B; fc-gamma RIIIb; fc-gamma RIII-beta; igG Fc
                     receptor III-1"
                     /calculated_mol_wt=24479
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1782
     mat_peptide     17..200
                     /product="Low affinity immunoglobulin gamma Fc region
                     receptor III-B. /id=PRO_0000015151"
                     /note="propagated from UniProtKB/Swiss-Prot (O75015.3)"
                     /calculated_mol_wt=20852
     Region          26..104
                     /region_name="Ig1_FcgammaR_like"
                     /note="First immunoglobulin (Ig)-like domain of
                     Fcgamma-receptors (FcgammaRs), and similar domains;
                     cd05752"
                     /db_xref="CDD:409410"
     Region          27..30
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409410"
     Site            order(29..30,48,56..59)
                     /site_type="other"
                     /note="pentraxin binding site [polypeptide binding]"
                     /db_xref="CDD:409410"
     Region          35..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409410"
     Region          42..48
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409410"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75015.3)"
     Region          58..63
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409410"
     Site            63
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75015.3)"
     Region          65..67
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409410"
     Region          72..77
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409410"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75015.3)"
     Region          85..90
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409410"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75015.3)"
     Region          98..104
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409410"
     Region          108..190
                     /region_name="Ig2_FcgammaR_like"
                     /note="Second immunoglobulin (Ig)-like domain of
                     Fcgamma-receptors (FcgammaRs), and similar domains;
                     cd05753"
                     /db_xref="CDD:409411"
     Site            order(108,131,137..138)
                     /site_type="other"
                     /note="Fc binding site [polypeptide binding]"
                     /db_xref="CDD:409411"
     Region          108..112
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409411"
     Region          117..119
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409411"
     Site            order(121..123,132,137,176)
                     /site_type="other"
                     /note="pentraxin binding site [polypeptide binding]"
                     /db_xref="CDD:409411"
     Region          123..130
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409411"
     Region          137..143
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409411"
     Region          146..151
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409411"
     Region          155..159
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409411"
     Region          169..174
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409411"
     Region          180..190
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409411"
     Site            180
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75015.3)"
     Site            187
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75015.3)"
     CDS             1..233
                     /gene="FCGR3B"
                     /gene_synonym="CD16; CD16-I; CD16A; CD16b; FCG3; FCGR3;
                     FCGR3A; FCR-10; FCRIII; FCRIIIb"
                     /coded_by="NM_001244753.2:83..784"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS41433.1"
                     /db_xref="GeneID:2215"
                     /db_xref="HGNC:HGNC:3620"
                     /db_xref="MIM:610665"
ORIGIN      
        1 mwqlllptal lllvsagmrt edlpkavvfl epqwysvlek dsvtlkcqga yspednstqw
       61 fhnenlissq assyfidaat vndsgeyrcq tnlstlsdpv qlevhigwll lqaprwvfke
      121 edpihlrchs wkntalhkvt ylqngkdrky fhhnsdfhip katlkdsgsy fcrglvgskn
      181 vssetvniti tqglavstis sfsppgyqvs fclvmvllfa vdtglyfsvk tni
//
LOCUS       NP_666148                338 aa            linear   ROD 27-APR-2025
DEFINITION  activator of 90 kDa heat shock protein ATPase homolog 1 isoform 1
            [Mus musculus].
ACCESSION   NP_666148
VERSION     NP_666148.1
DBSOURCE    REFSEQ: accession NM_146036.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Woodford,M.R., Sager,R.A., Marris,E., Dunn,D.M., Blanden,A.R.,
            Murphy,R.L., Rensing,N., Shapiro,O., Panaretou,B., Prodromou,C.,
            Loh,S.N., Gutmann,D.H., Bourboulia,D., Bratslavsky,G., Wong,M. and
            Mollapour,M.
  TITLE     Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates
            folding of kinase and non-kinase clients
  JOURNAL   EMBO J 36 (24), 3650-3665 (2017)
   PUBMED   29127155
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Desjardins,F., Delisle,C. and Gratton,J.P.
  TITLE     Modulation of the cochaperone AHA1 regulates heat-shock protein 90
            and endothelial NO synthase activation by vascular endothelial
            growth factor
  JOURNAL   Arterioscler Thromb Vasc Biol 32 (10), 2484-2492 (2012)
   PUBMED   22859491
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Xu,W., Mollapour,M., Prodromou,C., Wang,S., Scroggins,B.T.,
            Palchick,Z., Beebe,K., Siderius,M., Lee,M.J., Couvillon,A.,
            Trepel,J.B., Miyata,Y., Matts,R. and Neckers,L.
  TITLE     Dynamic tyrosine phosphorylation modulates cycling of the
            HSP90-P50(CDC37)-AHA1 chaperone machine
  JOURNAL   Mol Cell 47 (3), 434-443 (2012)
   PUBMED   22727666
  REMARK    GeneRIF: Hsp90 phosphorylation on tyrosine313 promotes recruitment
            of AHA1, which stimulates Hsp90 ATPase activity, furthering the
            chaperoning process.
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Echeverria,P.C., Bernthaler,A., Dupuis,P., Mayer,B. and Picard,D.
  TITLE     An interaction network predicted from public data as a discovery
            tool: application to the Hsp90 molecular chaperone machine
  JOURNAL   PLoS One 6 (10), e26044 (2011)
   PUBMED   22022502
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC151967.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025552.1, AK076069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 41.47 cM"
     Protein         1..338
                     /product="activator of 90 kDa heat shock protein ATPase
                     homolog 1 isoform 1"
                     /note="activator of 90 kDa heat shock protein ATPase
                     homolog 1; AHA1, activator of heat shock 90kDa protein
                     ATPase homolog 1; AHA1, activator of heat shock protein
                     ATPase homolog 1"
                     /calculated_mol_wt=37986
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O95433; propagated from
                     UniProtKB/Swiss-Prot (Q8BK64.2)"
     Region          29..158
                     /region_name="Aha1_N"
                     /note="Activator of Hsp90 ATPase, N-terminal; smart01000"
                     /db_xref="CDD:214964"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95433; propagated from
                     UniProtKB/Swiss-Prot (Q8BK64.2)"
     Region          208..333
                     /region_name="SRPBCC_Aha1"
                     /note="Putative hydrophobic ligand-binding SRPBCC domain
                     of the Hsp90 co-chaperone Aha1 and related proteins;
                     cd08892"
                     /db_xref="CDD:176901"
     Site            order(209,211,213,222..224,226..227,232,240,248,250,252,
                     254,256,258..259,261,264,270,272..273,286..287,289,291,
                     301,303,305,307,311..319,322..324,327)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176901"
     Site            212
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O95433; propagated from
                     UniProtKB/Swiss-Prot (Q8BK64.2)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL.
                     /evidence=ECO:0000250|UniProtKB:O95433; propagated from
                     UniProtKB/Swiss-Prot (Q8BK64.2)"
     Site            order(261,273,286,296..297)
                     /site_type="other"
                     /note="putative Hsp90 binding residues [polypeptide
                     binding]"
                     /db_xref="CDD:176901"
     CDS             1..338
                     /gene="Ahsa1"
                     /gene_synonym="p38"
                     /coded_by="NM_146036.2:115..1131"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS26075.1"
                     /db_xref="GeneID:217737"
                     /db_xref="MGI:MGI:2387603"
ORIGIN      
        1 makwgegdpr wiveeradat nvnnwhwter dasnwstekl ktlflavrve neegkcevte
       61 vnkldgeasi nnrkgkliff yewtiklnwt gtsksgvqyk ghveipnlsd ensvdeveis
      121 vslakdepdt nlvalmkedg vkllreavgi yistlkteft qgmilptvng esvdpvgqpa
      181 lktetckaks apsksqakpv gvkiptckit lketfltspe elyrvfttqe lvqafthapa
      241 aleadrggkf hmvdgnvtge ftdlvpekhi amkwrfkswp eghfatitlt fidkngetel
      301 cmegrgipap eeertrqgwq ryyfegikqt fgygarlf
//
LOCUS       NP_277040                397 aa            linear   PRI 27-APR-2025
DEFINITION  ethanolaminephosphotransferase 1 [Homo sapiens].
ACCESSION   NP_277040 XP_371484
VERSION     NP_277040.1
DBSOURCE    REFSEQ: accession NM_033505.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Li,F., Shi,Z., Cheng,M., Zhou,Z., Chu,M., Sun,L. and Zhou,J.C.
  TITLE     Biology and Roles in Diseases of Selenoprotein I Characterized by
            Ethanolamine Phosphotransferase Activity and Antioxidant Potential
  JOURNAL   J Nutr 153 (11), 3164-3172 (2023)
   PUBMED   36963501
  REMARK    GeneRIF: Biology and Roles in Diseases of Selenoprotein I
            Characterized by Ethanolamine Phosphotransferase Activity and
            Antioxidant Potential.
            Review article
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Sarma,A.S., Siddardha,B., T,P.L., Ranganath,P. and Dalal,A.
  TITLE     A novel homozygous synonymous splicing variant in SELENOI gene
            causes spastic paraplegia 81
  JOURNAL   J Gene Med 25 (7), e3501 (2023)
   PUBMED   36942482
  REMARK    GeneRIF: A novel homozygous synonymous splicing variant in SELENOI
            gene causes spastic paraplegia 81.
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Nunes,L.G.A., Pitts,M.W. and Hoffmann,P.R.
  TITLE     Selenoprotein I (selenoi) as a critical enzyme in the central
            nervous system
  JOURNAL   Arch Biochem Biophys 729, 109376 (2022)
   PUBMED   36007576
  REMARK    GeneRIF: Selenoprotein I (selenoi) as a critical enzyme in the
            central nervous system.
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Ma,C., Martinez-Rodriguez,V. and Hoffmann,P.R.
  TITLE     Roles for Selenoprotein I and Ethanolamine Phospholipid Synthesis
            in T Cell Activation
  JOURNAL   Int J Mol Sci 22 (20), 11174 (2021)
   PUBMED   34681834
  REMARK    GeneRIF: Roles for Selenoprotein I and Ethanolamine Phospholipid
            Synthesis in T Cell Activation.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Varlamova,E.G., Goltyaev,M.V., Novoselov,V.I. and Fesenko,E.E.
  TITLE     Cloning, intracellular localization, and expression of the
            mammalian selenocysteine-containing protein SELENOI (SelI) in tumor
            cell lines
  JOURNAL   Dokl Biochem Biophys 476 (1), 320-322 (2017)
   PUBMED   29101747
  REMARK    GeneRIF: intracellular localization of human selenoprotein SelI and
            the degree of expression of its gene in different human tumor cell
            lines
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Ahmed,M.Y., Al-Khayat,A., Al-Murshedi,F., Al-Futaisi,A.,
            Chioza,B.A., Pedro Fernandez-Murray,J., Self,J.E., Salter,C.G.,
            Harlalka,G.V., Rawlins,L.E., Al-Zuhaibi,S., Al-Azri,F.,
            Al-Rashdi,F., Cazenave-Gassiot,A., Wenk,M.R., Al-Salmi,F.,
            Patton,M.A., Silver,D.L., Baple,E.L., McMaster,C.R. and Crosby,A.H.
  TITLE     A mutation of EPT1 (SELENOI) underlies a new disorder of Kennedy
            pathway phospholipid biosynthesis
  JOURNAL   Brain 140 (3), 547-554 (2017)
   PUBMED   28052917
  REMARK    GeneRIF: These studies define the first human disorder arising due
            to defective CDP-ethanolamine biosynthesis and provide new insight
            into the role of Kennedy pathway components in human neurological
            function
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   8  (residues 1 to 397)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 397)
  AUTHORS   Horibata,Y. and Hirabayashi,Y.
  TITLE     Identification and characterization of human
            ethanolaminephosphotransferase1
  JOURNAL   J Lipid Res 48 (3), 503-508 (2007)
   PUBMED   17132865
REFERENCE   10 (residues 1 to 397)
  AUTHORS   Kryukov,G.V., Castellano,S., Novoselov,S.V., Lobanov,A.V.,
            Zehtab,O., Guigo,R. and Gladyshev,V.N.
  TITLE     Characterization of mammalian selenoproteomes
  JOURNAL   Science 300 (5624), 1439-1443 (2003)
   PUBMED   12775843
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010896.15.
            
            On Aug 30, 2004 this sequence version replaced XP_371484.1.
            
            Summary: The multi-pass transmembrane protein encoded by this gene
            belongs to the CDP-alcohol phosphatidyltransferase class-I family.
            It catalyzes the transfer of phosphoethanolamine from
            CDP-ethanolamine to diacylglycerol to produce
            phosphatidylethanolamine, which is involved in the formation and
            maintenance of vesicular membranes, regulation of lipid metabolism,
            and protein folding. This protein is a selenoprotein, containing
            the rare selenocysteine (Sec) amino acid at its active site. Sec is
            encoded by the UGA codon, which normally signals translation
            termination. The 3' UTRs of selenoprotein mRNAs contain a conserved
            stem-loop structure, designated the Sec insertion sequence (SECIS)
            element, that is necessary for the recognition of UGA as a Sec
            codon rather than as a stop signal. Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Jul 2016].
            
            Transcript Variant: This variant (1) represents the
            selenoprotein-encoding transcript.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK001426.1, AB051511.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match              :: ENST00000260585.12/
                                               ENSP00000260585.7
            protein contains selenocysteine :: PMID: 12775843
            RefSeq Select criteria          :: based on single protein-coding
                                               transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..397
                     /product="ethanolaminephosphotransferase 1"
                     /EC_number="2.7.8.1"
                     /note="hEPT1; ethanolaminephosphotransferase 1
                     (CDP-ethanolamine-specific)"
                     /calculated_mol_wt=45098
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Region          6..382
                     /region_name="PRK10832"
                     /note="CDP-diacylglycerol--glycerol-3-phosphate
                     3-phosphatidyltransferase; cl00453"
                     /db_xref="CDD:469774"
     Site            47..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Site            84..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Site            123..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Site            150..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Site            179..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Site            221..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Site            256..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Site            291..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Site            317..339
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Site            344..366
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D9.3)"
     Site            387
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..397
                     /gene="SELENOI"
                     /gene_synonym="EPT1; SELI; SEPI; SPG81"
                     /coded_by="NM_033505.4:91..1284"
                     /note="UGA stop codon recoded as selenocysteine"
                     /db_xref="CCDS:CCDS46240.1"
                     /db_xref="GeneID:85465"
                     /db_xref="HGNC:HGNC:29361"
                     /db_xref="MIM:607915"
ORIGIN      
        1 magyeyvspe qlagfdkyky savdtnplsl yvmhpfwnti vkvfptwlap nlitfsgfll
       61 vvfnfllmay fdpdfyasap ghkhvpdwvw ivvgilnfva ytldgvdgkq arrtnsstpl
      121 gelfdhglds wscvyfvvtv ysifgrgstg vsvfvlylll wvvlfsfils hwekyntgil
      181 flpwgydisq vtisfvyivt avvgveawye pflfnflyrd lftamiigca lcvtlpmsll
      241 nffrsyknnt lklnsvyeam vplfspcllf ilstawilws psdilelhpr vfyfmvgtaf
      301 anstcqlivc qmsstrcptl nwllvplflv vlvvnlgvas yvesillytl ttaftlahih
      361 ygvrvvkqls shfqiypfsl rkpnsdulgm eeknigl
//
LOCUS       NP_004868                142 aa            linear   PRI 27-APR-2025
DEFINITION  glia maturation factor gamma isoform 1 [Homo sapiens].
ACCESSION   NP_004868
VERSION     NP_004868.1
DBSOURCE    REFSEQ: accession NM_004877.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Zhao,Y., Wei,X., Li,J., Diao,Y., Shan,C., Li,W., Zhang,S. and Wu,F.
  TITLE     High Level of GMFG Correlated to Poor Clinical Outcome and Promoted
            Cell Migration and Invasion through EMT Pathway in Triple-Negative
            Breast Cancer
  JOURNAL   Genes (Basel) 14 (6), 1157 (2023)
   PUBMED   37372337
  REMARK    GeneRIF: High Level of GMFG Correlated to Poor Clinical Outcome and
            Promoted Cell Migration and Invasion through EMT Pathway in
            Triple-Negative Breast Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Tang,H., Liu,J. and Huang,J.
  TITLE     GMFG (glia maturation factor gamma) inhibits lung cancer growth by
            activating p53 signaling pathway
  JOURNAL   Bioengineered 13 (4), 9284-9293 (2022)
   PUBMED   35383531
  REMARK    GeneRIF: GMFG (glia maturation factor gamma) inhibits lung cancer
            growth by activating p53 signaling pathway.
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Zhang,Y.L., Cao,J.L., Zhang,Y., Liao,L., Deng,L., Yang,S.Y.,
            Hu,S.Y., Ning,Y., Zhang,F.L. and Li,D.Q.
  TITLE     RNF144A exerts tumor suppressor function in breast cancer through
            targeting YY1 for proteasomal degradation to downregulate GMFG
            expression
  JOURNAL   Med Oncol 39 (4), 48 (2022)
   PUBMED   35103856
  REMARK    GeneRIF: RNF144A exerts tumor suppressor function in breast cancer
            through targeting YY1 for proteasomal degradation to downregulate
            GMFG expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Lan,A., Ren,C., Wang,X., Tong,G. and Yang,G.
  TITLE     Bioinformatics and survival analysis of glia maturation
            factor-gamma in pan-cancers
  JOURNAL   BMC Cancer 21 (1), 423 (2021)
   PUBMED   33863293
  REMARK    GeneRIF: Bioinformatics and survival analysis of glia maturation
            factor-gamma in pan-cancers.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Gerlach,B.D., Tubbesing,K., Liao,G., Rezey,A.C., Wang,R.,
            Barroso,M. and Tang,D.D.
  TITLE     Phosphorylation of GMFgamma by c-Abl Coordinates Lamellipodial and
            Focal Adhesion Dynamics to Regulate Airway Smooth Muscle Cell
            Migration
  JOURNAL   Am J Respir Cell Mol Biol 61 (2), 219-231 (2019)
   PUBMED   30811945
  REMARK    GeneRIF: GMFgamma phosphorylation by c-Abl has an important role in
            coordinating lamellipodial and focal adhesion dynamics to regulate
            cell migration
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Asai,K., Fujita,K., Yamamoto,M., Hotta,T., Morikawa,M., Kokubo,M.,
            Moriyama,A. and Kato,T.
  TITLE     Isolation of novel human cDNA (hGMF-gamma) homologous to Glia
            Maturation Factor-beta gene
  JOURNAL   Biochim Biophys Acta 1396 (3), 242-244 (1998)
   PUBMED   9545571
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Lim,R. and Zaheer,A.
  TITLE     In vitro enhancement of p38 mitogen-activated protein kinase
            activity by phosphorylated glia maturation factor
  JOURNAL   J Biol Chem 271 (38), 22953-22956 (1996)
   PUBMED   8798479
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Zaheer,A. and Lim,R.
  TITLE     In vitro inhibition of MAP kinase (ERK1/ERK2) activity by
            phosphorylated glia maturation factor (GMF)
  JOURNAL   Biochemistry 35 (20), 6283-6288 (1996)
   PUBMED   8639570
REFERENCE   10 (residues 1 to 142)
  AUTHORS   Lim,R. and Zaheer,A.
  TITLE     Phorbol ester stimulates rapid intracellular phosphorylation of
            glia maturation factor
  JOURNAL   Biochem Biophys Res Commun 211 (3), 928-934 (1995)
   PUBMED   7598724
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF974742.1 and BC080180.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BF974742.1, BU687769.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159764 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000597595.6/ ENSP00000472249.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..142
                     /product="glia maturation factor gamma isoform 1"
                     /calculated_mol_wt=16670
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (O60234.1)"
     Region          9..130
                     /region_name="ADF_GMF-beta_like"
                     /note="ADF-homology domain of glia maturation factor beta
                     and related proteins; cd11283"
                     /db_xref="CDD:200439"
     CDS             1..142
                     /gene="GMFG"
                     /gene_synonym="GMF-GAMMA"
                     /coded_by="NM_004877.4:68..496"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12532.1"
                     /db_xref="GeneID:9535"
                     /db_xref="HGNC:HGNC:4374"
                     /db_xref="MIM:604104"
ORIGIN      
        1 msdslvvcev dpelteklrk frfrketdna aiimkvdkdr qmvvleeefq nispeelkme
       61 lperqprfvv ysykyvhddg rvsyplcfif sspvgckpeq qmmyagsknr lvqtaeltkv
      121 feirttddlt eawlqeklsf fr
//
LOCUS       NP_001346506             722 aa            linear   ROD 27-APR-2025
DEFINITION  BTB/POZ domain-containing protein KCTD3 isoform 3 [Mus musculus].
ACCESSION   NP_001346506 XP_006497207
VERSION     NP_001346506.1
DBSOURCE    REFSEQ: accession NM_001359577.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Cao-Ehlker,X., Zong,X., Hammelmann,V., Gruner,C., Fenske,S.,
            Michalakis,S., Wahl-Schott,C. and Biel,M.
  TITLE     Up-regulation of hyperpolarization-activated cyclic
            nucleotide-gated channel 3 (HCN3) by specific interaction with K+
            channel tetramerization domain-containing protein 3 (KCTD3)
  JOURNAL   J Biol Chem 288 (11), 7580-7589 (2013)
   PUBMED   23382386
  REMARK    GeneRIF: KCTD3 is an accessory subunit of native HCN3 complexes
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC129312.6.
            
            On Jan 13, 2018 this sequence version replaced XP_006497207.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3533950.1,
                                           SRR13948564.4383840.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 93.51 cM"
     Protein         1..722
                     /product="BTB/POZ domain-containing protein KCTD3 isoform
                     3"
                     /note="BTB/POZ domain-containing protein KCTD3"
                     /calculated_mol_wt=78852
     Region          17..119
                     /region_name="BTB_POZ_SHKBP1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in SH3KBP1-binding
                     protein 1 (SHKBP1); cd18393"
                     /db_xref="CDD:349701"
     CDS             1..722
                     /gene="Kctd3"
                     /gene_synonym="4930438A20Rik; 9330185B06; E330032J19Rik;
                     NY-REN-45"
                     /coded_by="NM_001359577.1:229..2397"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:226823"
                     /db_xref="MGI:MGI:2444629"
ORIGIN      
        1 magghcgsfa asaassgeiv qlnvggtrfs tsrqtlmwip dsffssllsg ristlrdetg
       61 aifidrdpaa fapilnflrt keldlrgvsi nvlrheaefy gitplvrrll lceelerssc
      121 gsvlfhgylp ppgipsrkvt ntarssvdar nglnsmegea rgngtqpvla gngedtirlg
      181 vpvdprkvli vaghhnwiva ayahfavcyr cvqprrscrc sllhwkpagg heshgeggrv
      241 erchaaladm qkfplrmkdn dllvtelyhd psndavtals vyltpktsvs gnwieiaygt
      301 ssgavrvivq hpetvgsgpq lfqtftvhrs pvtkimlsek hlvsvcadnn hvrtwtvtrf
      361 rgmistqpgs tplasfkils leeteshgsy ssgndigpfg erddqqvfiq kvvpitnklf
      421 vrlsstgkri ceiqavdctt issftvrece gssrmgsrpr rylftghtng siqmwdltta
      481 mdmvnktedk daggpteeel lklldqcdls tsrcatpnis patsvlqhsr lresssslql
      541 qhhetiheaa tygatrpyre spllararrt esfhsyrdfq tlnlnrsier pvpenghmgp
      601 aqtevkgaag ecamserrsp gtevrcgres dgglevhrta eglsepkkrs aedenehkve
      661 frkkgfeagg flgrkkvpyl asspstsdgg tdspgtasps ptkttpsprh kksdssgqey
      721 sl
//
LOCUS       NP_001295049            1773 aa            linear   PRI 27-APR-2025
DEFINITION  TOG array regulator of axonemal microtubules protein 1 isoform 1
            [Homo sapiens].
ACCESSION   NP_001295049 XP_005267508
VERSION     NP_001295049.1
DBSOURCE    REFSEQ: accession NM_001308120.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1773)
  AUTHORS   Latour,B.L., Van De Weghe,J.C., Rusterholz,T.D., Letteboer,S.J.,
            Gomez,A., Shaheen,R., Gesemann,M., Karamzade,A., Asadollahi,M.,
            Barroso-Gil,M., Chitre,M., Grout,M.E., van Reeuwijk,J., van
            Beersum,S.E., Miller,C.V., Dempsey,J.C., Morsy,H., Bamshad,M.J.,
            Nickerson,D.A., Neuhauss,S.C., Boldt,K., Ueffing,M.,
            Keramatipour,M., Sayer,J.A., Alkuraya,F.S., Bachmann-Gagescu,R.,
            Roepman,R. and Doherty,D.
  CONSRTM   University of Washington Center for Mendelian Genomics; Genomics
            England Research Consortium
  TITLE     Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes
            Joubert syndrome
  JOURNAL   J Clin Invest 130 (8), 4423-4439 (2020)
   PUBMED   32453716
REFERENCE   2  (residues 1 to 1773)
  AUTHORS   Das,A., Dickinson,D.J., Wood,C.C., Goldstein,B. and Slep,K.C.
  TITLE     Crescerin uses a TOG domain array to regulate microtubules in the
            primary cilium
  JOURNAL   Mol Biol Cell 26 (23), 4248-4264 (2015)
   PUBMED   26378256
REFERENCE   3  (residues 1 to 1773)
  AUTHORS   Hepner,F., Myung,J.K., Ulfig,N., Pollak,A. and Lubec,G.
  TITLE     Detection of hypothetical proteins in human fetal perireticular
            nucleus
  JOURNAL   J Proteome Res 4 (6), 2379-2385 (2005)
   PUBMED   16335990
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK295185.1, BX648723.1, BC065234.1 and AA911186.1.
            
            On Apr 22, 2015 this sequence version replaced XP_005267508.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.226658.1,
                                           SRR1660807.155435.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361462.7/ ENSP00000354917.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1773
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q21.2"
     Protein         1..1773
                     /product="TOG array regulator of axonemal microtubules
                     protein 1 isoform 1"
                     /note="protein FAM179B; crescerin-1; family with sequence
                     similarity 179 member B; TOG array regulator of axonemal
                     microtubules protein 1"
                     /calculated_mol_wt=195133
     Site            order(369..370,373,376,378,412..413,416,419..420,423,
                     453..454,457,460..461,464,488..489,497,500..501,528..529,
                     532,535..536)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          395..423
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          435..465
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          470..501
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          512..537
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..1773
                     /gene="TOGARAM1"
                     /gene_synonym="FAM179B; JBTS37; KIAA0423"
                     /coded_by="NM_001308120.2:233..5554"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS76676.1"
                     /db_xref="GeneID:23116"
                     /db_xref="HGNC:HGNC:19959"
                     /db_xref="MIM:617618"
ORIGIN      
        1 maaapsalll lppfpvlsty rlqsrsrpsa petddsrvgg imrgeknyyf rgaagdhgsc
       61 ptttsplasa llmpseavss swsesgggls ggdeedtrll qllrtardps eafqalqaal
      121 prrggrlgfp rrkealyral grvlveggsd ekrlclqlls dvlrgqgeag qleeafslal
      181 lpqlvvslre enpalrkdal qilhiclkrs pgevlrtliq qglestdarl rastalllpi
      241 llttedlllg ldlteviisl arklgdqete eesetafsal qqigerlgqd rfqsyisrlp
      301 salrrhynrr lesqfgsqvp yyleleasgf pedplpcavt lsnsnlkfgi ipqelhsrll
      361 dqedyknrtq aveelkqvlg kfnpsstphs slvgfislly nllddsnfkv vhgtlevlhl
      421 lvirlgeqvq qflgpviaas vkvladnklv ikqeymkifl klmkevgpqq vlclllehlk
      481 hkhsrvreev vnicicsllt ypsedfdlpk lsfdlapalv dskrrvrqaa leafavlass
      541 mgsgktsilf kavdtvelqd ngdgvmnavq arlarktlpr lteqgfveya vlmpssaggr
      601 snhlahgadt dwllagnrtq sahchcgdhv rdsmhiygsy sptictrrvl sagkgknklp
      661 weneqpgimg enqtstskdi eqfstydfip saklklsqgm pvnddlcfsr krvsrnlfqn
      721 srdfnpdclp lcaagttgth qtnlsgkcaq lgfsqicgkt gsvgsdlqfl gttsshqekv
      781 yaslnfgskt qqtfgsqtec tssngqnpsp gayilpsypv ssprtspkht spliispkks
      841 qdnsvnfsns wplksfegls kpspqkklvs qkssdptgrn hgensqekpp vqltpalvrs
      901 pssrrglngt kpvppiprgi sllpdkadls tvghkkkepd diwkcekdsl pidlselnfk
      961 dkdldqeemh sslrslrnsa akkraklsgs tsdlespdsa mkldltmdsp slssspnins
     1021 ysesgvysqe sltsslsttp qgkrimsdif ptfgskpcpt rlssakkkis hiaeqspsag
     1081 sssnpqqiss fdftttkals edsvvvvgkg vfgslssapa tcsqsvissv engdtfsikq
     1141 sieppsgiyg rsvqqnissy ldvenekdak vsiskstynk mrqkrkeeke lfhnkdcekk
     1201 eknswermrh tgtekmases etptgaisqy kermpsvths peimdlselr pfskpeialt
     1261 ealrlladed wekkieglnf irclaafhse ilntklhetn favvqevknl rsgvsraavv
     1321 clsdlftylk ksmdqeldtt vkvllhkage sntfiredvd kalramvnnv tparavvsli
     1381 nggqshlhia vrrctaqhls dvlefmeper ilsaakdmae rilpaaakfa qdssqetryy
     1441 grkmlffmmc hpnfekmlek yvpskdlpyi kdsvrnlqqk glgeipldtp sakgrrshtg
     1501 svgntrsssv srdafnsaer avtevrevtr ksvprnsles aeylklitgl lnakdfrdri
     1561 ngikqllsdt ennqdlvvgn ivkifdafks rlhdsnskvn lvaletmhkm ipllrdhlsp
     1621 iinmlipaiv dnnlnsknpg iyaaatnvvq alsqhvdnyl llqpfctkaq flngkakqdm
     1681 tekladivte lyqrkphate qkvlvvlwhl lgnmtnsgsl pgaggnirta taklskalfa
     1741 qmgqnllnqa asqpphikks leelldmtil nel
//
LOCUS       NP_001244103             370 aa            linear   PRI 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX19B isoform 3 [Homo sapiens].
ACCESSION   NP_001244103
VERSION     NP_001244103.1
DBSOURCE    REFSEQ: accession NM_001257174.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Banerjee,P., Markande,S., Kalarikkal,M. and Joseph,J.
  TITLE     SUMOylation modulates the function of DDX19 in mRNA export
  JOURNAL   J Cell Sci 135 (4) (2022)
   PUBMED   35080244
  REMARK    GeneRIF: SUMOylation modulates the function of DDX19 in mRNA
            export.
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Park,Y., Park,J., Hwang,H.J., Kim,L., Jeong,K., Song,H.K.,
            Rufener,S.C., Muhlemann,O. and Kim,Y.K.
  TITLE     Translation mediated by the nuclear cap-binding complex is confined
            to the perinuclear region via a CTIF-DDX19B interaction
  JOURNAL   Nucleic Acids Res 49 (14), 8261-8276 (2021)
   PUBMED   34232997
  REMARK    GeneRIF: Translation mediated by the nuclear cap-binding complex is
            confined to the perinuclear region via a CTIF-DDX19B interaction.
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Arul Nambi Rajan,A. and Montpetit,B.
  TITLE     Emerging molecular functions and novel roles for the DEAD-box
            protein Dbp5/DDX19 in gene expression
  JOURNAL   Cell Mol Life Sci 78 (5), 2019-2030 (2021)
   PUBMED   33205304
  REMARK    GeneRIF: Emerging molecular functions and novel roles for the
            DEAD-box protein Dbp5/DDX19 in gene expression.
            Review article
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Yin,L., Li,J., Zhu,H., Lin,M., Cheng,L., Wang,Y., Zhou,Z. and
            Sha,J.
  TITLE     Identification and characterization of a gene coding a novel
            isoform of DEAD-box protein
  JOURNAL   Reprod Fertil Dev 14 (3-4), 185-189 (2002)
   PUBMED   12219940
  REMARK    GeneRIF: identification and characterization of a gene coding a
            novel isoform
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Schmitt,C., von Kobbe,C., Bachi,A., Pante,N., Rodrigues,J.P.,
            Boscheron,C., Rigaut,G., Wilm,M., Seraphin,B., Carmo-Fonseca,M. and
            Izaurralde,E.
  TITLE     Dbp5, a DEAD-box protein required for mRNA export, is recruited to
            the cytoplasmic fibrils of nuclear pore complex via a conserved
            interaction with CAN/Nup159p
  JOURNAL   EMBO J 18 (15), 4332-4347 (1999)
   PUBMED   10428971
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Mattioni,T., Hume,C.R., Konigorski,S., Hayes,P., Osterweil,Z. and
            Lee,J.S.
  TITLE     A cDNA clone for a novel nuclear protein with DNA binding activity
  JOURNAL   Chromosoma 101 (10), 618-624 (1992)
   PUBMED   1424986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012184.7 and AF353720.1.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. This gene encodes a DEAD box protein,
            which exhibits RNA-dependent ATPase and ATP-dependent RNA-unwinding
            activities. This protein is recruited to the cytoplasmic fibrils of
            the nuclear pore complex, where it participates in the export of
            mRNA from the nucleus. Multiple alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF353720.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119, SAMEA2161674
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..370
                     /product="ATP-dependent RNA helicase DDX19B isoform 3"
                     /EC_number="3.6.4.13"
                     /note="DEAD-box protein 5; yeast Dbp5 homolog; DEAD/H
                     (Asp-Glu-Ala-Asp/His) box polypeptide 19 (Dbp5, yeast,
                     homolog); ATP-dependent RNA helicase DDX19; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 19B; ATP-dependent RNA
                     helicase DDX19B; DEAD-box RNA helicase DEAD5; DEAD box
                     protein 19B; DEAD (Asp-Glu-Ala-As) box polypeptide 19B;
                     dead box protein 5 homolog"
                     /calculated_mol_wt=41648
     Region          1..187
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            order(31..37,133)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          198..334
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(287,289,320,323..324)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     CDS             1..370
                     /gene="DDX19B"
                     /gene_synonym="DBP5; DDX19; RNAh"
                     /coded_by="NM_001257174.2:410..1522"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS42187.1"
                     /db_xref="GeneID:11269"
                     /db_xref="HGNC:HGNC:2742"
                     /db_xref="MIM:605812"
ORIGIN      
        1 mgfnrpskiq enalplmlae ppqnliaqsq sgtgktaafv lamlsqvepa nkypqclcls
       61 ptyelalqtg kvieqmgkfy pelklayavr gnklergqki seqivigtpg tvldwcsklk
      121 fidpkkikvf vldeadvmia tqghqdqsir iqrmlprncq mllfsatfed svwkfaqkvv
      181 pdpnviklkr eeetldtikq yyvlcssrde kfqalcnlyg aitiaqamif chtrktaswl
      241 aaelskeghq vallsgemmv eqraavierf regkekvlvt tnvcargidv eqvsvvinfd
      301 lpvdkdgnpd netylhrigr tgrfgkrgla vnmvdskhsm nilnriqehf nkkierldtd
      361 dldeiekian
//
LOCUS       NP_001093205             419 aa            linear   PRI 27-APR-2025
DEFINITION  creatine kinase S-type, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_001093205
VERSION     NP_001093205.1
DBSOURCE    REFSEQ: accession NM_001099735.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Rizo-Roca,D., Guimaraes,D.S.P.S.F., Pendergrast,L.A., Di Leo,N.,
            Chibalin,A.V., Maqdasy,S., Ryden,M., Naslund,E., Zierath,J.R. and
            Krook,A.
  TITLE     Decreased mitochondrial creatine kinase 2 impairs skeletal muscle
            mitochondrial function independently of insulin in type 2 diabetes
  JOURNAL   Sci Transl Med 16 (768), eado3022 (2024)
   PUBMED   39383244
  REMARK    GeneRIF: Decreased mitochondrial creatine kinase 2 impairs skeletal
            muscle mitochondrial function independently of insulin in type 2
            diabetes.
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Lin,W., Zhou,J., Ma,Y., Ge,L., Luo,Y., Wang,Y. and Zhou,S.
  TITLE     Prognostic value of mitochondrial CKMT2 in Pan-cancer and its tumor
            immune correlation analysis
  JOURNAL   Sci Rep 14 (1), 342 (2024)
   PUBMED   38172162
  REMARK    GeneRIF: Prognostic value of mitochondrial CKMT2 in Pan-cancer and
            its tumor immune correlation analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Payne,R.M. and Strauss,A.W.
  TITLE     Expression of the mitochondrial creatine kinase genes
  JOURNAL   Mol Cell Biochem 133-134, 235-243 (1994)
   PUBMED   7808456
  REMARK    Review article
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Richard,I., Devaud,C., Cherif,D., Cohen,D. and Beckmann,J.S.
  TITLE     The gene for creatine kinase, mitochondrial 2 (sarcomeric; CKMT2),
            maps to chromosome 5q13.3
  JOURNAL   Genomics 18 (1), 134-136 (1993)
   PUBMED   8276398
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Klein,S.C., Haas,R.C., Perryman,M.B., Billadello,J.J. and
            Strauss,A.W.
  TITLE     Regulatory element analysis and structural characterization of the
            human sarcomeric mitochondrial creatine kinase gene
  JOURNAL   J Biol Chem 266 (27), 18058-18065 (1991)
   PUBMED   1917943
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Haas,R.C. and Strauss,A.W.
  TITLE     Separate nuclear genes encode sarcomere-specific and ubiquitous
            human mitochondrial creatine kinase isoenzymes
  JOURNAL   J Biol Chem 265 (12), 6921-6927 (1990)
   PUBMED   2324105
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Haas,R.C., Korenfeld,C., Zhang,Z.F., Perryman,B., Roman,D. and
            Strauss,A.W.
  TITLE     Isolation and characterization of the gene and cDNA encoding human
            mitochondrial creatine kinase
  JOURNAL   J Biol Chem 264 (5), 2890-2897 (1989)
   PUBMED   2914937
  REMARK    Erratum:[J Biol Chem 1989 Sep 25;264(27):16332]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB479765.1, BC029140.1 and
            AW300490.1.
            
            Summary: Mitochondrial creatine kinase (MtCK) is responsible for
            the transfer of high energy phosphate from mitochondria to the
            cytosolic carrier, creatine. It belongs to the creatine kinase
            isoenzyme family. It exists as two isoenzymes, sarcomeric MtCK and
            ubiquitous MtCK, encoded by separate genes. Mitochondrial creatine
            kinase occurs in two different oligomeric forms: dimers and
            octamers, in contrast to the exclusively dimeric cytosolic creatine
            kinase isoenzymes. Sarcomeric mitochondrial creatine kinase has 80%
            homology with the coding exons of ubiquitous mitochondrial creatine
            kinase. This gene contains sequences homologous to several motifs
            that are shared among some nuclear genes encoding mitochondrial
            proteins and thus may be essential for the coordinated activation
            of these genes during mitochondrial biogenesis. Three transcript
            variants encoding the same protein have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All three variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.63632.1,
                                           SRR5189655.117948.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000254035.9/
                                                  ENSP00000254035.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..419
                     /product="creatine kinase S-type, mitochondrial precursor"
                     /EC_number="2.7.3.2"
                     /note="basic-type mitochondrial creatine kinase; creatine
                     kinase S-type, mitochondrial; S-MtCK; mib-CK; sarcomeric
                     mitochondrial creatine kinase; creatine kinase,
                     mitochondrial 2 (sarcomeric)"
                     /calculated_mol_wt=43344
     transit_peptide 1..39
                     /calculated_mol_wt=4179
     mat_peptide     40..419
                     /product="creatine kinase S-type, mitochondrial"
                     /calculated_mol_wt=43344
     Region          40..64
                     /region_name="Cardiolipin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P17540.2)"
     Region          50..407
                     /region_name="creatine_kinase_like"
                     /note="Phosphagen (guanidino) kinases such as creatine
                     kinase and similar enzymes; cd00716"
                     /db_xref="CDD:153076"
     Site            order(106,235,266,317,319)
                     /site_type="other"
                     /note="creatine binding site [chemical binding]"
                     /db_xref="CDD:153076"
     Site            order(162,164,166,225,262,270,326,328..330,354,356,
                     358..359,369)
                     /site_type="other"
                     /note="ADP binding site [chemical binding]"
                     /db_xref="CDD:153076"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P09605; propagated from
                     UniProtKB/Swiss-Prot (P17540.2)"
     Site            order(351..360,363..372)
                     /site_type="active"
                     /note="substrate specificity loop [active]"
                     /db_xref="CDD:153076"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6P8J7; propagated from
                     UniProtKB/Swiss-Prot (P17540.2)"
     CDS             1..419
                     /gene="CKMT2"
                     /gene_synonym="SMTCK"
                     /coded_by="NM_001099735.2:77..1336"
                     /db_xref="CCDS:CCDS4053.1"
                     /db_xref="GeneID:1160"
                     /db_xref="HGNC:HGNC:1996"
                     /db_xref="MIM:123295"
ORIGIN      
        1 masifskllt grnasllfat mgtsvlttgy llnrqkvcae vreqprlfpp sadypdlrkh
       61 nncmaecltp aiyaklrnkv tpngytldqc iqtgvdnpgh pfiktvgmva gdeesyevfa
      121 dlfdpviklr hngydprvmk httdldaski tqgqfdehyv lssrvrtgrs irglslppac
      181 traerreven vaitaleglk gdlagryykl semteqdqqr liddhflfdk pvsplltcag
      241 mardwpdarg iwhnydktfl iwineedhtr vismekggnm krvferfcrg lkeverliqe
      301 rgwefmwner lgyiltcpsn lgtglragvh vripklskdp rfskilenlr lqkrgtggvd
      361 taavadvydi snidrigrse velvqividg vnylvdcekk lergqdikvp pplpqfgkk
//
LOCUS       NP_001094068             371 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 707 isoform a [Homo sapiens].
ACCESSION   NP_001094068
VERSION     NP_001094068.1
DBSOURCE    REFSEQ: accession NM_001100598.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Rual,J.F., Hirozane-Kishikawa,T., Hao,T., Bertin,N., Li,S.,
            Dricot,A., Li,N., Rosenberg,J., Lamesch,P., Vidalain,P.O.,
            Clingingsmith,T.R., Hartley,J.L., Esposito,D., Cheo,D., Moore,T.,
            Simmons,B., Sequerra,R., Bosak,S., Doucette-Stamm,L., Le Peuch,C.,
            Vandenhaute,J., Cusick,M.E., Albala,J.S., Hill,D.E. and Vidal,M.
  TITLE     Human ORFeome version 1.1: a platform for reverse proteomics
  JOURNAL   Genome Res 14 (10B), 2128-2135 (2004)
   PUBMED   15489335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB249556.1, DA007942.1, AK001126.1, CV023324.1, BC014894.1,
            AK055263.1 and AW294133.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 4. Variants 1, 2, 3, 4, and 5 encode the same
            protein (isoform a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290432.1, DA474624.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358656.9/ ENSP00000351482.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..371
                     /product="zinc finger protein 707 isoform a"
                     /calculated_mol_wt=42957
     Region          8..68
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          71..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C28.2)"
     Region          178..198
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <187..366
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          206..226
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          234..254
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          262..282
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(267,269,271,273..274,277..278,281,295,297,301..302,
                     305..306,309,323,325,327,329..330,333..334,337)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          290..310
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          318..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          346..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..371
                     /gene="ZNF707"
                     /coded_by="NM_001100598.2:215..1330"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47932.1"
                     /db_xref="GeneID:286075"
                     /db_xref="HGNC:HGNC:27815"
ORIGIN      
        1 mdmaqepvtf rdvaiyfsre ewaclepsqr alyrdvmldn fssvaalgfc sprpdlvsrl
       61 eqweepwved rerpefqavq rgprpgarks adpkrpcdhp awahkkthvr reraregssf
      121 rkgfrldtdd gqlpraaper tdakptafpc qvltqrcgrr pgrrerrkqr avelsficgt
      181 cgkalschsr llahqtvhtg tkafecpecg qtfrwasnlq rhqknhtrek pfcceacgqa
      241 fslkdrlaqh rkvhtehrpy scgdcgkafk qksnllrhql vhtgerpfyc adcgkafrtk
      301 enlshhqrvh sgekpytcae cgksfrwpkg fsihrrlhlt krfyecghcg kgfrhlgfft
      361 rhqrthrhge v
//
LOCUS       NP_001353142             892 aa            linear   PRI 27-APR-2025
DEFINITION  disks large homolog 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001353142 XP_011510805
VERSION     NP_001353142.1
DBSOURCE    REFSEQ: accession NM_001366213.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 892)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   2  (residues 1 to 892)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 892)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   4  (residues 1 to 892)
  AUTHORS   Veljacic Viskovic,D., Lozic,M., Vukoja,M., Soljic,V., Vukojevic,K.,
            Glavina Durdov,M., Filipovic,N. and Lozic,B.
  TITLE     Spatio-Temporal Expression Pattern of CAKUT Candidate Genes DLG1
            and KIF12 during Human Kidney Development
  JOURNAL   Biomolecules 13 (2), 340 (2023)
   PUBMED   36830709
  REMARK    GeneRIF: Spatio-Temporal Expression Pattern of CAKUT Candidate
            Genes DLG1 and KIF12 during Human Kidney Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 892)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 892)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 892)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 892)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 892)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 892)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_011510805.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.24776.1,
                                           SRR1660809.45487.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..892
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..892
                     /product="disks large homolog 1 isoform 3"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=99683
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          701..879
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..892
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366213.1:495..3173"
                     /note="isoform 3 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS75072.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgsfndk rkknlfsrkf pfyknkdqse
      661 qetsdadqhv tsnasdsess yrgqeeyvls yepvnqqevn ytrpviilgp mkdrinddli
      721 sefpdkfgsc vphttrpkrd yevdgrdyhf vtsreqmekd iqehkfieag qynnhlygts
      781 vqsvrevaek gkhcildvsg naikrlqiaq lypisifikp ksmenimemn krlteeqark
      841 tferamkleq eftehftaiv qgdtlediyn qvkqiieeqs gsyiwvpake kl
//
LOCUS       NP_057467                313 aa            linear   PRI 27-APR-2025
DEFINITION  leucine zipper protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_057467
VERSION     NP_057467.1
DBSOURCE    REFSEQ: accession NM_016383.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Viphakone,N., Cumberbatch,M.G., Livingstone,M.J., Heath,P.R.,
            Dickman,M.J., Catto,J.W. and Wilson,S.A.
  TITLE     Luzp4 defines a new mRNA export pathway in cancer cells
  JOURNAL   Nucleic Acids Res 43 (4), 2353-2366 (2015)
   PUBMED   25662211
  REMARK    GeneRIF: Luzp4 is an RNA-binding protein which associates with the
            TREX mRNA export complex subunit Uap56. Luzp4 also binds the
            principal mRNA export receptor Nxf1, enhances its RNA binding
            activity and complements Alyref knockdown in vivo. Luzp4 displays
            all features of an mRNA export adaptor. Whilst Luzp4 is
            up-regulated in a range of tumours, it appears preferentially
            expressed in melanoma cells where it is required for growth.
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Tureci,O., Sahin,U., Koslowski,M., Buss,B., Bell,C., Ballweber,P.,
            Zwick,C., Eberle,T., Zuber,M., Villena-Heinsen,C., Seitz,G. and
            Pfreundschuh,M.
  TITLE     A novel tumour associated leucine zipper protein targeting to sites
            of gene transcription and splicing
  JOURNAL   Oncogene 21 (24), 3879-3888 (2002)
   PUBMED   12032826
  REMARK    GeneRIF: A novel tumour associated leucine zipper protein targeting
            to sites of gene transcription and splicing.
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Sahin,U., Koslowski,M., Tureci,O., Eberle,T., Zwick,C., Romeike,B.,
            Moringlane,J.R., Schwechheimer,K., Feiden,W. and Pfreundschuh,M.
  TITLE     Expression of cancer testis genes in human brain tumors
  JOURNAL   Clin Cancer Res 6 (10), 3916-3922 (2000)
   PUBMED   11051238
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC239923.3, DB035084.1,
            AF124430.1 and AK093369.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a leucine-zipper protein that was first
            defined as a cancer testis antigens. The encoded protein is an RNA
            binding protein that interacts with the mRNA export receptor
            nuclear RNA export factor 2. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.364378.1,
                                           SRR5189667.137125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371920.4/ ENSP00000360988.3
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq23"
     Protein         1..313
                     /product="leucine zipper protein 4 isoform 1"
                     /note="HOM-TES-85 tumor antigen; cancer/testis antigen 28;
                     tumor antigen HOM-TES-85"
                     /calculated_mol_wt=35806
     Region          1..238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          1..119
                     /region_name="Interaction with DDX39B/UAP56.
                     /evidence=ECO:0000269|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          22..40
                     /region_name="UAP56-binding motif (UBM), required for
                     proper nuclear localization.
                     /evidence=ECO:0000269|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          51..80
                     /region_name="Arg-rich, required for RNA-binding.
                     /evidence=ECO:0000303|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          <110..>255
                     /region_name="PHA00430"
                     /note="tail fiber protein"
                     /db_xref="CDD:222790"
     Region          178..236
                     /region_name="RS-containing His-rich (RS-H), necessary for
                     nuclear localization.
                     /evidence=ECO:0000269|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          238..287
                     /region_name="Leucine-zipper, required for RNA-binding and
                     for its relocalization to the cytoplasm during cell
                     division. /evidence=ECO:0000269|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          241..313
                     /region_name="Interaction with NXF1.
                     /evidence=ECO:0000269|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          290..313
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     CDS             1..313
                     /gene="LUZP4"
                     /gene_synonym="CT-28; CT-8; CT28; HOM-TES-85"
                     /coded_by="NM_016383.5:46..987"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14567.1"
                     /db_xref="GeneID:51213"
                     /db_xref="HGNC:HGNC:24971"
                     /db_xref="MIM:300616"
ORIGIN      
        1 masfrkltls ekvppnhpsr kkvnfldmsl ddiiiykele gtnaeeeknk rqnhskkesp
       61 srqqskahrh rhrrgysrcr snseegnhdk kpsqkpsgfk sgqhplngqp lieqekcsdn
      121 yeaqaeknqg qsegnqhqse gnpdkseesq gqpeenhhse rsrnhlersl sqsdrsqgql
      181 krhhpqyers hgqykrshgq sershghser shghsershg hsershghsk rsrsqgdlvd
      241 tqsdliatqr dliatqkdli atqrdliatq rdlivtqrdl vaterdlinq sgrshgqser
      301 hqrystgknt itt
//
LOCUS       NP_038876                566 aa            linear   ROD 27-APR-2025
DEFINITION  erythroid membrane-associated protein isoform a precursor [Mus
            musculus].
ACCESSION   NP_038876
VERSION     NP_038876.3
DBSOURCE    REFSEQ: accession NM_013848.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Su,M., Lin,Y., Cui,C., Tian,X. and Lai,L.
  TITLE     ERMAP is a B7 family-related molecule that negatively regulates T
            cell and macrophage responses
  JOURNAL   Cell Mol Immunol 18 (8), 1920-1933 (2021)
   PUBMED   32620788
  REMARK    GeneRIF: ERMAP is a B7 family-related molecule that negatively
            regulates T cell and macrophage responses.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   McClelland,K.S., Bell,K., Larney,C., Harley,V.R., Sinclair,A.H.,
            Oshlack,A., Koopman,P. and Bowles,J.
  TITLE     Purification and Transcriptomic Analysis of Mouse Fetal Leydig
            Cells Reveals Candidate Genes for Specification of Gonadal
            Steroidogenic Cells
  JOURNAL   Biol Reprod 92 (6), 145 (2015)
   PUBMED   25855264
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Xu,H., Foltz,L., Sha,Y., Madlansacay,M.R., Cain,C., Lindemann,G.,
            Vargas,J., Nagy,D., Harriman,B., Mahoney,W. and Schueler,P.A.
  TITLE     Cloning and characterization of human erythroid membrane-associated
            protein, human ERMAP
  JOURNAL   Genomics 76 (1-3), 2-4 (2001)
   PUBMED   11549310
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Ye,T.Z., Gordon,C.T., Lai,Y.H., Fujiwara,Y., Peters,L.L.,
            Perkins,A.C. and Chui,D.H.
  TITLE     Ermap, a gene coding for a novel erythroid specific
            adhesion/receptor membrane protein
  JOURNAL   Gene 242 (1-2), 337-345 (2000)
   PUBMED   10721728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606975.9.
            
            On Mar 15, 2019 this sequence version replaced NP_038876.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF153906.1, SRR13422598.207958.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135, SAMN01164140
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 55.34 cM"
     Protein         1..566
                     /product="erythroid membrane-associated protein isoform a
                     precursor"
                     /note="erythroid membrane-associated protein"
                     /calculated_mol_wt=60397
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3133
     Region          26..141
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     mat_peptide     30..566
                     /product="Erythroid membrane-associated protein.
                     /id=PRO_0000226089"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLN5.2)"
                     /calculated_mol_wt=60397
     Region          43..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          106..110
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          120..125
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          133..136
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JLN5.2)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JLN5.2)"
     Site            247..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLN5.2)"
     Region          321..503
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9JLN5.2)"
     CDS             1..566
                     /gene="Ermap"
                     /coded_by="NM_013848.3:281..1981"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS18571.2"
                     /db_xref="GeneID:27028"
                     /db_xref="MGI:MGI:1349816"
ORIGIN      
        1 merpspcgsw lvgclftiav fqppvqvlgd agkvyiaplr dtanlpcplf lwpnmvlsem
       61 rwyrpghlpr tqavhvfrdg qdrdedlmpe ykgrtalvrd ahkesyilqi snvrledrgl
      121 yqcqvwvgns srednvtlqv avlgsdpyih vkgydagwie llcqsvgwfp kpwtewrdtt
      181 grallslsev hsldenglfr tavssrirdn algnvsctih nealgqektt amiigaperg
      241 slsspavals vvlpvlglli llgiwlickq kkskekllye qamevenlle dhakekgrlh
      301 kalkklrsel klkraaanag wrrarlhfva vtldpdtahp klilsedrrc vrlgdrkrpv
      361 pdnperfdfv vsvlgseyft tgchywevyv gektkwilgv csesvsrkgk vtaspanghw
      421 lvrqsrgney ealtspqtsf rlkespkcvg ifldyeagii sfynvtdksh iftfthsfss
      481 plrpffepcl hdegkntapl iictelqkse esivpkqegk drangdvslk mnpsllspqg
      541 selfllndtw psnlgpalkg lkvpsl
//
LOCUS       NP_001348497             203 aa            linear   ROD 27-APR-2025
DEFINITION  ras-like protein family member 10B isoform 1 [Mus musculus].
ACCESSION   NP_001348497 XP_006533548
VERSION     NP_001348497.1
DBSOURCE    REFSEQ: accession NM_001361568.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Shigesawa,I., Nakamura,A., Yamauchi,Y., Kawata,S., Miyazaki,A.,
            Nomoto,H., Kameda,H., Terauchi,Y. and Atsumi,T.
  TITLE     Effects of glucokinase haploinsufficiency on the pancreatic
            beta-cell mass and function of long-term high-fat, high-sucrose
            diet-fed mice
  JOURNAL   J Diabetes Investig 15 (12), 1732-1742 (2024)
   PUBMED   39305123
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Rybkin,I.I., Kim,M.S., Bezprozvannaya,S., Qi,X., Richardson,J.A.,
            Plato,C.F., Hill,J.A., Bassel-Duby,R. and Olson,E.N.
  TITLE     Regulation of atrial natriuretic peptide secretion by a novel
            Ras-like protein
  JOURNAL   J Cell Biol 179 (3), 527-537 (2007)
   PUBMED   17984325
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK045997.1, BE995698.1, AK158941.1 and AW456843.1.
            
            On Mar 29, 2018 this sequence version replaced XP_006533548.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI202455.1, BE995698.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849376
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 50.3 cM"
     Protein         1..203
                     /product="ras-like protein family member 10B isoform 1"
                     /EC_number="3.6.5.2"
                     /note="ras-like protein family member 10B"
                     /calculated_mol_wt=23098
     Region          1..203
                     /region_name="Small GTPase-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
     mat_peptide     1..200
                     /product="Ras-like protein family member 10B.
                     /id=PRO_0000280801"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
                     /calculated_mol_wt=22914
     Region          5..203
                     /region_name="RRP22"
                     /note="Ras-related protein on chromosome 22 (RRP22)
                     family; cd04142"
                     /db_xref="CDD:133342"
     Site            11..18
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133342"
     Site            order(12..13,61..62)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133342"
     Site            order(13..19,59,62,128..129,131,159..160)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133342"
     Site            order(18..19,33,35,42..43,56..57,59,61..62,161)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133342"
     Region          33..42
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
     Site            order(34..35,40..43)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133342"
     Site            order(34..38,40..42)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133342"
     Site            36
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133342"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133342"
     Site            order(61..62,72..77,84..87)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133342"
     Site            128..131
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133342"
     Site            159..161
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133342"
     Site            200..203
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:133342"
     Site            200
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q5SSG5.1)"
     CDS             1..203
                     /gene="Rasl10b"
                     /gene_synonym="B230331P10Rik; Gm729; VTS58635"
                     /coded_by="NM_001361568.1:336..947"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS25163.1"
                     /db_xref="GeneID:276952"
                     /db_xref="MGI:MGI:2685575"
ORIGIN      
        1 mvstyrvavl gargvgksai vrqflynefs evcvptttrr lylpavvmng hvhdlqildf
       61 ppisafpvnt lqewadaccr glrsvhayil vydiccfdsf eyvktirqqi letrvigtse
      121 tpiiivgnkr dlqrgrvipr wnvshlvrkt wkcgyvecsa kynwhilllf sellksvgca
      181 rckhvhaalr fqgalrrnrc aim
//
LOCUS       NP_002449               5762 aa            linear   PRI 27-APR-2025
DEFINITION  mucin-5B precursor [Homo sapiens].
ACCESSION   NP_002449 XP_001126093 XP_001129427
VERSION     NP_002449.2
DBSOURCE    REFSEQ: accession NM_002458.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 5762)
  AUTHORS   Li,T.A., Gonzalez-Gil,A., Awol,A.K., Ackerman,S.J., Orsburn,B.C.
            and Schnaar,R.L.
  TITLE     Sialylated keratan sulfates on MUC5B are Siglec-8 ligands in the
            human esophagus
  JOURNAL   Glycobiology 34 (10) (2024)
   PUBMED   39173029
  REMARK    GeneRIF: Sialylated keratan sulfates on MUC5B are Siglec-8 ligands
            in the human esophagus.
REFERENCE   2  (residues 1 to 5762)
  AUTHORS   Ueda,Y., Mogami,H., Chigusa,Y., Kawamura,Y., Inohaya,A.,
            Takakura,M., Yasuda,E., Matsuzaka,Y., Shimada,M., Ito,S.,
            Morita,S., Mandai,M. and Kondoh,E.
  TITLE     Hyposecretion of cervical MUC5B is related to preterm birth in
            pregnant women after cervical excisional surgery
  JOURNAL   Am J Reprod Immunol 91 (3), e13832 (2024)
   PUBMED   38462543
  REMARK    GeneRIF: Hyposecretion of cervical MUC5B is related to preterm
            birth in pregnant women after cervical excisional surgery.
REFERENCE   3  (residues 1 to 5762)
  AUTHORS   Dhooria,S., Bal,A., Sharma,R., Prabhakar,N., Arora,S., Sehgal,I.S.,
            Kashyap,D., Garg,M., Bhalla,A., Aggarwal,A.N. and Agarwal,R.
  TITLE     Association of MUC5B promoter polymorphism with interstitial lung
            changes after COVID-19: A preliminary observation
  JOURNAL   Indian J Med Res 159 (1), 109-113 (2024)
   PUBMED   38344913
  REMARK    GeneRIF: Association of MUC5B promoter polymorphism with
            interstitial lung changes after COVID-19: A preliminary
            observation.
REFERENCE   4  (residues 1 to 5762)
  AUTHORS   Chen,Y., Zhao,Y.H., Di,Y.P. and Wu,R.
  TITLE     Characterization of human mucin 5B gene expression in airway
            epithelium and the genomic clone of the amino-terminal and
            5'-flanking region
  JOURNAL   Am J Respir Cell Mol Biol 25 (5), 542-553 (2001)
   PUBMED   11713095
REFERENCE   5  (residues 1 to 5762)
  AUTHORS   Desseyn,J.L., Buisine,M.P., Porchet,N., Aubert,J.P. and Laine,A.
  TITLE     Genomic organization of the human mucin gene MUC5B. cDNA and
            genomic sequences upstream of the large central exon
  JOURNAL   J Biol Chem 273 (46), 30157-30164 (1998)
   PUBMED   9804771
REFERENCE   6  (residues 1 to 5762)
  AUTHORS   Desseyn,J.L., Guyonnet-Duperat,V., Porchet,N., Aubert,J.P. and
            Laine,A.
  TITLE     Human mucin gene MUC5B, the 10.7-kb large central exon encodes
            various alternate subdomains resulting in a super-repeat.
            Structural evidence for a 11p15.5 gene family
  JOURNAL   J Biol Chem 272 (6), 3168-3178 (1997)
   PUBMED   9013550
REFERENCE   7  (residues 1 to 5762)
  AUTHORS   Troxler,R.F., Offner,G.D., Zhang,F., Iontcheva,I. and
            Oppenheim,F.G.
  TITLE     Molecular cloning of a novel high molecular weight mucin (MG1) from
            human sublingual gland
  JOURNAL   Biochem Biophys Res Commun 217 (3), 1112-1119 (1995)
   PUBMED   8554565
REFERENCE   8  (residues 1 to 5762)
  AUTHORS   Meezaman,D., Charles,P., Daskal,E., Polymeropoulos,M.H.,
            Martin,B.M. and Rose,M.C.
  TITLE     Cloning and analysis of cDNA encoding a major airway glycoprotein,
            human tracheobronchial mucin (MUC5)
  JOURNAL   J Biol Chem 269 (17), 12932-12939 (1994)
   PUBMED   7513696
REFERENCE   9  (residues 1 to 5762)
  AUTHORS   Dufosse,J., Porchet,N., Audie,J.P., Guyonnet Duperat,V., Laine,A.,
            Van-Seuningen,I., Marrakchi,S., Degand,P. and Aubert,J.P.
  TITLE     Degenerate 87-base-pair tandem repeats create
            hydrophilic/hydrophobic alternating domains in human mucin peptides
            mapped to 11p15
  JOURNAL   Biochem J 293 (Pt 2) (Pt 2), 329-337 (1993)
   PUBMED   7916618
REFERENCE   10 (residues 1 to 5762)
  AUTHORS   Douglas,W.H., Reeh,E.S., Ramasubbu,N., Raj,P.A., Bhandary,K.K. and
            Levine,M.J.
  TITLE     Statherin: a major boundary lubricant of human saliva
  JOURNAL   Biochem Biophys Res Commun 180 (1), 91-97 (1991)
   PUBMED   1718282
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC061979.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 24, 2010 this sequence version replaced NP_002449.1.
            
            Summary: This gene encodes a member of the mucin family of
            proteins, which are highly glycosylated macromolecular components
            of mucus secretions. This family member is the major gel-forming
            mucin in mucus. It is a major contributor to the lubricating and
            viscoelastic properties of whole saliva, normal lung mucus and
            cervical mucus. This gene has been found to be up-regulated in some
            human diseases, including sinus mucosa of chronic rhinosinusitis
            (CRS), CRS with nasal polyposis, chronic obstructive pulmonary
            disease (COPD) and H. pylori-associated gastric disease, and it may
            be involved in the pathogenesis of these diseases. [provided by
            RefSeq, Jul 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on partial transcript alignments that tile across
            this locus.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968832 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000529681.5/ ENSP00000436812.1
            RefSeq Select criteria    :: based on single protein-coding
                                         transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..5762
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..5762
                     /product="mucin-5B precursor"
                     /note="mucin 5, subtype B, tracheobronchial; cervical
                     mucin MUC5B; sublingual gland mucin; high molecular weight
                     salivary mucin MG1"
                     /calculated_mol_wt=593848
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2514
     Region          27..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          70..223
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            201
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            254
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          261..325
                     /region_name="C8"
                     /note="C8 domain; pfam08742"
                     /db_xref="CDD:462584"
     Region          329..385
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            order(338,342,355,359)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          387..>432
                     /region_name="VWC_out"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00215"
                     /db_xref="CDD:214565"
     Site            401
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          425..579
                     /region_name="VWD"
                     /note="von Willebrand factor type D domain; pfam00094"
                     /db_xref="CDD:459671"
     Site            515
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          615..685
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Region          695..752
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(704,708,722,726)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          794..855
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            order(803,815,826,831)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            805
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          884..1041
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Site            929
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1078..1152
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Site            1276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            1292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1333..4228
                     /region_name="7 X Cys-rich subdomain repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1340..1426
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            1340
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1437..1462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1480..1502
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1509..1597
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            1509
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            1556
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1607..1783
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1630..>1767
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     Site            1774
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1790..1878
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            1790
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1890..2199
                     /region_name="11 X approximate tandem repeats,
                     Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          1890..2019
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          <1928..2313
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          2031..2100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          2114..2211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          2242..2302
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          2320..2408
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            2320
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          2419..2756
                     /region_name="11 X approximate tandem repeats,
                     Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          2443..2462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          2473..2522
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          2556..2861
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          2644..>2868
                     /region_name="Chi1"
                     /note="Chitinase [Carbohydrate transport and metabolism];
                     COG3469"
                     /db_xref="CDD:442692"
     Site            2749
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          2877..2965
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            2877
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          2976..3456
                     /region_name="17 X approximate tandem repeats,
                     Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          3001..3049
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          3256..3357
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          3371..3469
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          3375..>3573
                     /region_name="Chi1"
                     /note="Chitinase [Carbohydrate transport and metabolism];
                     COG3469"
                     /db_xref="CDD:442692"
     Site            3449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          3481..3561
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          3577..3665
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            3577
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          3676..4013
                     /region_name="11 X approximate tandem repeats,
                     Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          3699..3779
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          3813..3917
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          3878..>4080
                     /region_name="Chi1"
                     /note="Chitinase [Carbohydrate transport and metabolism];
                     COG3469"
                     /db_xref="CDD:442692"
     Region          3956..4118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            4006
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          4134..4222
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Site            4134
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          4233..4879
                     /region_name="23 X approximate tandem repeats,
                     Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          4259..4389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          4428..4447
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          4458..4527
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          4541..4750
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            4804
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            4960
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5017
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5024
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5046
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          5064..5237
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Site            5096
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          5290..5351
                     /region_name="C8"
                     /note="C8 domain; pfam08742"
                     /db_xref="CDD:462584"
     Region          5359..5414
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            5486
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          5523..5586
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Site            5526
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5565
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5566
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5602
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5612
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Region          5660..5742
                     /region_name="CT"
                     /note="C-terminal cystine knot-like domain (CTCK);
                     smart00041"
                     /db_xref="CDD:214482"
     Site            5663
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5677
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     Site            5721
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HC84.3)"
     CDS             1..5762
                     /gene="MUC5B"
                     /gene_synonym="MG1; MUC-5B; MUC5; MUC9"
                     /coded_by="NM_002458.3:59..17347"
                     /db_xref="CCDS:CCDS44515.2"
                     /db_xref="GeneID:727897"
                     /db_xref="HGNC:HGNC:7516"
                     /db_xref="MIM:600770"
ORIGIN      
        1 mgapsacrtl vlalaamlvv pqaetqgpve pswenaghtm dggaptsspt rrvsfvppvt
       61 vfpslsplnp ahngrvcstw gdfhyktfdg dvfrfpglcn yvfsehcraa yedfnvqlrr
      121 glvgsrpvvt rvvikaqglv leasngsvli ngqreelpys rtgllveqsg dyikvsirlv
      181 ltflwngeds alleldpkya nqtcglcgdf nglpafnefy ahnarltplq fgnlqkldgp
      241 teqcpdplpl pagnctdeeg ichrtllgpa faechalvds taylaacaqd lcrcptcpca
      301 tfveysrqca haggqprnwr cpelcprtcp lnmqhqecgs pctdtcsnpq raqlcedhcv
      361 dgcfcppgtv lddithsgcl plgqcpcthg grtyspgtsf nttcssctcs gglwqcqdlp
      421 cpgtcsvqgg ahistydekl ydlhgdcsyv lskkcadssf tvlaelrkcg ltdnenclka
      481 vtlsldggdt airvqadggv flnsiytqlp lsaanitlft pssffivvqt glglqllvql
      541 vplmqvfvrl dpahqgqmcg lcgnfnqnqa ddftalsgvv eatgaafant wkaqaacana
      601 rnsfedpcsl svenenyarh wcsrltdpns afsrchsiin pkpfhsncmf dtcncersed
      661 clcaalssyv hacaakgvql sdwrdgvctk ymqncpksqr yayvvdacqp tcrglseadv
      721 tcsvsfvpvd gctcpagtfl ndagacvpaq ecpcyahgtv lapgevvhde gavcsctggk
      781 lsclgaslqk stgcaapmvy ldcsnssagt pgaeclrsch tldvgcfsth cvsgcvcppg
      841 lvsdgsggci aeedcpcvhn eatykpgeti rvdcntctcr nrrwecshrl clgtcvaygd
      901 ghfitfdgdr ysfegsceyi laqdycgdnt thgtfrivte nipcgttgtt cskaiklfve
      961 syelilqegt fkavargpgg dppykirymg iflviethgm avswdrktsv firlhqdykg
     1021 rvcglcgnfd dnaindfatr srsvvgdale fgnswklsps cpdalapkdp ctanpfrksw
     1081 aqkqcsilhg ptfaacrsqv dstkyyeacv ndacacdsgg dcecfctava ayaqachdag
     1141 lcvswrtpdt cplfcdfynp hggcewhyqp cgapclktcr npsghclvdl pglegcypkc
     1201 ppsqpffned qmkcvaqcgc ydkdgnyydv garvptaenc qscnctpsgi qcahsleact
     1261 ctyedrtysy qdviynttdg lgacliaicg sngtiirkav acpgtpattp ftfttawvph
     1321 sttspalpvs tvcvrevcrw sswynghrpe pglgggdfet fenlrqrgyq vcpvladiec
     1381 raaqlpdmpl eelgqqvdcd rmrglmcans qqspplchdy elrvlcceyv pcgpspapgt
     1441 spqpslsast epavptptqt tatekttlwv tpsirstaal tsqtgsssgp vtvtpsapgt
     1501 ttcqprcqwt ewfdedypks eqlggdvesy dkiraagghl cqqpkdiecq aesfpnwtla
     1561 qvgqkvhcdv hfglvcrnwe qegvfkmcyn yrirvlccsd dhcrgrattp pptteletat
     1621 ttttqalfst pqptsspglt rappasttav ptlsegltsp rytstlgtat tggpttpags
     1681 teptvpgvat stlptrsalp gttgslgtwr psqpptlapt tmatsrarpt gtastaskep
     1741 lttslaptlt selstsqaet stprtettms pltntttsqg ttrcqpkcew tewfdvdfpt
     1801 sgvaggdmet feniraaggk mcwapksiec raenypevsi dqvgqvltcs letgltckne
     1861 dqtgrfnmcf nynvrvlccd dyshcpstpa tsstatpsst pgttwiltkp tttatttast
     1921 gstatptstl rtapppkvlt ttattptvts skatpssspg tatalpalrs tattptatsv
     1981 tpipssslgt twtrlsqttt ptatmstatp sstpetahts tvltatattt gatgsvatps
     2041 stpgtahttk vptttttgft atpssspgta ltppvwistt ttpttrgstv tpssipgtth
     2101 tatvlttttt tvatgsmatp ssstqtsgtp psltttatti tatgsttnps stpgttpipp
     2161 vltttattpa atsntvtpss algtthtppv pntmatthgr slppssphtv rtawtsatsg
     2221 ilgtthitep stvtshtlaa ttgttqhstp alssphpssr ttesppspgt ttpghttats
     2281 rttatatpsk trtstllpss ptsapittvv tmgcepqcaw sewldysypm pgpsggdfdt
     2341 ysniraagga vceqplglec raqaqpgvpl relgqvvecs ldfglvcrnr eqvgkfkmcf
     2401 nyeirvfccn yghcpstpat sstampsstp gttwiltelt ttatttestg statpsstpg
     2461 ttwiltepst tatvtvptgs tatasstqat agtphvstta ttptvtsska tpfsspgtat
     2521 alpalrstat tptatsftai pssslgttwt rlsqtttpta tmstatpsst petvhtstvl
     2581 tttatttgat gsvatpsstp gtahttkvlt ttttgftatp ssspgtartl pvwisttttp
     2641 ttrgstvtps sipgtthtpt vlttttttva tgsmatpsss tqtsgtppsl tttattitat
     2701 gsttnpsstp gttpippvlt ttattpaats stvtpssalg tthtppvpnt tatthgrsls
     2761 pssphtvrta wtsatsgtlg tthitepstg tshtpaattg ttqhstpals sphpssrtte
     2821 sppspgtttp ghtratsrtt atatpsktrt stllpsspts apittvvtmg cepqcawsew
     2881 ldysypmpgp sggdfdtysn iraaggavce qplglecraq aqpgvplrel gqvvecsldf
     2941 glvcrnreqv gkfkmcfnye irvfccnygh cpstpatsst atpsstpgtt wilteqttaa
     3001 tttattgsta ipsstpgtap ppkvltstat tptatsskat ssssprtatt lpvltstatk
     3061 statsftpip sftlgttgtl peqtttpmat mstihpsstp etthtstvlt tkatttrats
     3121 smstpsstpg ttwilteltt aatttaatgp tatpsstpgt twiltepstt atvtvptgst
     3181 atasstrata gtlkvltsta ttptvissra tpssspgtat alpalrstat tptatsvtai
     3241 pssslgtawt rlsqtttpta tmstatpsst petvhtstvl tttttttrat gsvatpsstp
     3301 gtahttkvpt ttttgftatp ssspgtaltp pvwisttttp ttrgstvtps sipgtthtat
     3361 vlttttttva tgsmatpsss tqtsgtppsl tttattitat gsttnpsstp gttpippvlt
     3421 ttattpaats stvtpssalg tthtppvpnt tatthgrslp pssphtvrta wtsatsgilg
     3481 tthitepstv tshtpaatts ttqhstpals sphpssrtte sppspgtttp ghtrgtsrtt
     3541 atatpsktrt stllpsspts apittvvttg cepqcawsew ldysypmpgp sggdfdtysn
     3601 iraaggavce qplglecraq aqpgvplrel gqvvecsldf glvcrnreqv gkfkmcfnye
     3661 irvfccnygh cpstpatsst atpsstpgtt wiltklttta tttestgsta tpsstpgttw
     3721 iltepsttat vtvptgstat asstqatagt phvsttattp tvtsskatpf sspgtatalp
     3781 alrstattpt atsftaipss slgttwtrls qtttptatms tatpsstpet ahtstvlttt
     3841 atttratgsv atpsstpgta httkvptttt tgftvtpsss pgtartppvw isttttptts
     3901 gstvtpssvp gtthtptvlt tttttvatgs matpssstqt sgtppslitt attitatgst
     3961 tnpsstpgtt pippvlttta ttpaatsstv tpssalgtth tppvpnttat thgrslspss
     4021 phtvrtawts atsgtlgtth itepstgtsh tpaattgttq hstpalssph pssrttespp
     4081 spgtttpght tatsrttata tpsktrtstl lpssptsapi ttvvttgcep qcawsewldy
     4141 sypmpgpsgg dfdtysnira aggavceqpl glecraqaqp gvplgelgqv vecsldfglv
     4201 crnreqvgkf kmcfnyeirv fccnyghcps tpatsstamp sstpgttwil teltttattt
     4261 astgstatps stpgtapppk vltspattpt atsskatsss sprtattlpv ltstatksta
     4321 tsvtpipsst lgttgtlpeq tttpvatmst ihpsstpett htstvlttka tttratssts
     4381 tpsstpgttw iltelttaat ttaatgptat psstpgttwi lteltttatt tastgstatp
     4441 sstpgttwil tepsttatvt vptgstatas stqatagtph vsttattptv tsskatpsss
     4501 pgtatalpal rstattptat sftaipsssl gttwtrlsqt ttptatmsta tpsstpetvh
     4561 tstvltatat ttgatgsvat psstpgtaht tkvptttttg ftatpssspg taltppvwis
     4621 ttttpttttp ttsgstvtps sipgtthtar vlttttttva tgsmatpsss tqtsgtppsl
     4681 tttattitat gsttnpsstp gttpitpvlt stattpaats skatsssspr tattlpvlts
     4741 tatkstatsf tpipsstlwt twtvpaqttt pmstmstiht sstpetthts tvltttatmt
     4801 ratnstatps stlgttrilt eltttattta atgstatlss tpgttwilte pstiatvmvp
     4861 tgstatasst lgtahtpkvv ttmatmptat astvpssstv gttrtpavlp sslptfsvst
     4921 vsssvlttlr ptgfpsshfs tpcfcrafgq ffspgeviyn ktdragchfy avcnqhcdid
     4981 rfqgacptsp ppvssaplss pspapgcdna iplrqvnetw tlenctvarc vgdnrvvlld
     5041 pkpvanvtcv nkhlpikvsd psqpcdfhye cecicsmwgg shystfdgts ytfrgnctyv
     5101 lmreiharfg nlslyldnhy ctasataaaa rcpralsihy ksmdivltvt mvhgkeegli
     5161 lfdqipvssg fskngvlvsv lgtttmrvdi palgvsvtfn gqvfqarlpy slfhnntegq
     5221 cgtctnnqrd dclqrdgtta asckdmaktw lvpdsrkdgc waptgtppta spaapvsstp
     5281 tptpcppqpl cdlmlsqvfa echnlvppgp ffnacisdhc rgrlevpcqs leayaelcra
     5341 rgvcsdwrga tgglcdltcp ptkvykpcgp iqpatcnsrn qspqlegmae gcfcpedqil
     5401 fnahmgicvq acpcvgpdgf pkfpgerwvs ncqscvcdeg svsvqckplp cdaqgqpppc
     5461 nrpgfvtvtr praenpccpe tvcvcntttc pqslpvcppg qesictqeeg dccptfrcrp
     5521 qlcsyngtfy gvgatfpgal pchmctclsg dtqdptvqcq edacnnttcp qgfeykrvag
     5581 qccgecvqta cltpdgqpvq lnetwvnshv dnctvylcea eggvhlltpq pascpdvssc
     5641 rgslrktgcc ysceedscqv rinttilwhq gcetevnitf cegscpgask ysaeaqamqh
     5701 qctccqerrv heetvplhcp ngsailhtyt hvdecgctpf cvpapmapph trgfpaqeat
     5761 av
//
LOCUS       NP_001353505             887 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 12 [Homo
            sapiens].
ACCESSION   NP_001353505 XP_016855509
VERSION     NP_001353505.1
DBSOURCE    REFSEQ: accession NM_001366576.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 887)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 887)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 887)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 887)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 887)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 887)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 887)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855509.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.118736.1,
                                           SRR1803611.29489.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..887
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 12"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=100003
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <121..209
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <384..713
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <589..>723
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..887
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366576.1:26..2689"
                     /note="isoform 12 is encoded by transcript variant 16"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrtksrsp
      181 spapekkekt pelpepsvkv kepsvqeats tsdilkvpkp epipepkeps peknskkeke
      241 kektrprsrs rsksrsrtrs rspshtrprr rhrsrsrsys prrrpsprrr psprrrtppr
      301 rmpppprhrr srspvrrrrr ssaslsgsss sssssrsrsp pkkppkrtss pprktrrlsp
      361 saspprrrhr psppatpppk trhsptpqqs nrtrksrvsv spgrtsgkvt khkgtekres
      421 pspapkprkv elsesedkgg kmaaadsvqq rrqyrrqnqq sssdsgssss sederpkrsh
      481 vkngevgrrr rhspsrsasp sprkrqkets prmqmgkrwq spvtksgrrr rspsppptrr
      541 rrspspappp rrrrtptppp rrrtpspppr rrspsprrys ppiqrrysps pppkrrtasp
      601 ppppkrrasp spppkrrvsh spppkqrssp vtkrrspsls skhrkgssps rstrearspq
      661 pnkrhspspr prapqtsssp ppvrrgasss pqrrqspsps trpirrvsrt pepkkikkaa
      721 spspqsvrrv sssrsvsgsp epaakkppap pspvqsqsps tnwspavpvk kaksptpsps
      781 pprnsdqegg gkkkkkkkdk khkkdkkhkk hkkhkkekav aaaaaaavtp aaiaaatttl
      841 aqeepvaape pkketeseae dnlddlekhl rekalrsmrk aqvspqs
//
LOCUS       NP_001664                561 aa            linear   PRI 27-APR-2025
DEFINITION  asparagine synthetase [glutamine-hydrolyzing] isoform a [Homo
            sapiens].
ACCESSION   NP_001664
VERSION     NP_001664.3
DBSOURCE    REFSEQ: accession NM_001673.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Jung,A.R., Shin,S., Kim,M.Y., Ha,U.S., Hong,S.H., Lee,J.Y.,
            Kim,S.W., Chung,Y.J. and Park,Y.H.
  TITLE     Integrated Bioinformatics Analysis Identified ASNS and DDIT3 as the
            Therapeutic Target in Castrate-Resistant Prostate Cancer
  JOURNAL   Int J Mol Sci 25 (5), 2836 (2024)
   PUBMED   38474084
  REMARK    GeneRIF: Integrated Bioinformatics Analysis Identified ASNS and
            DDIT3 as the Therapeutic Target in Castrate-Resistant Prostate
            Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Wu,Z., Wu,Z., Zeng,J., Liu,Y., Wang,Y., Li,H., Xia,T., Liu,W.,
            Lin,Z. and Xu,W.
  TITLE     An endoplasmic reticulum stress-related signature featuring ASNS
            for predicting prognosis and immune landscape in prostate cancer
  JOURNAL   Aging (Albany NY) 16 (1), 43-65 (2024)
   PUBMED   38206293
  REMARK    GeneRIF: An endoplasmic reticulum stress-related signature
            featuring ASNS for predicting prognosis and immune landscape in
            prostate cancer.
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Cai,D.J., Zhang,Z.Y., Bu,Y., Li,L., Deng,Y.Z., Sun,L.Q., Hu,C.P.
            and Li,M.
  TITLE     Asparagine synthetase regulates lung-cancer metastasis by
            stabilizing the beta-catenin complex and modulating mitochondrial
            response
  JOURNAL   Cell Death Dis 13 (6), 566 (2022)
   PUBMED   35739087
  REMARK    GeneRIF: Asparagine synthetase regulates lung-cancer metastasis by
            stabilizing the beta-catenin complex and modulating mitochondrial
            response.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Liu,L., Wang,J., Li,H., Dong,Y., Li,Y., Xia,L., Yang,B., Wang,H.,
            Xu,Y., Cheng,G., Du,K., Zhang,X., Zhu,C., Cui,S. and Ren,C.
  TITLE     An intractable epilepsy phenotype of ASNS novel mutation in two
            patients with asparagine synthetase deficiency
  JOURNAL   Clin Chim Acta 531, 331-336 (2022)
   PUBMED   35469797
  REMARK    GeneRIF: An intractable epilepsy phenotype of ASNS novel mutation
            in two patients with asparagine synthetase deficiency.
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Heng,H.H., Shi,X.M., Scherer,S.W., Andrulis,I.L. and Tsui,L.C.
  TITLE     Refined localization of the asparagine synthetase gene (ASNS) to
            chromosome 7, region q21.3, and characterization of the somatic
            cell hybrid line 4AF/106/KO15
  JOURNAL   Cytogenet Cell Genet 66 (2), 135-138 (1994)
   PUBMED   7904551
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Alfadhel,M. and El-Hattab,A.W.
  TITLE     Asparagine Synthetase Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30234940
REFERENCE   7  (residues 1 to 561)
  AUTHORS   Van Heeke,G. and Schuster,S.M.
  TITLE     The N-terminal cysteine of human asparagine synthetase is essential
            for glutamine-dependent activity
  JOURNAL   J Biol Chem 264 (33), 19475-19477 (1989)
   PUBMED   2573597
REFERENCE   8  (residues 1 to 561)
  AUTHORS   Greco,A., Gong,S.S., Ittmann,M. and Basilico,C.
  TITLE     Organization and expression of the cell cycle gene, ts11, that
            encodes asparagine synthetase
  JOURNAL   Mol Cell Biol 9 (6), 2350-2359 (1989)
   PUBMED   2569668
REFERENCE   9  (residues 1 to 561)
  AUTHORS   Van Heeke,G. and Schuster,S.M.
  TITLE     Expression of human asparagine synthetase in Escherichia coli
  JOURNAL   J Biol Chem 264 (10), 5503-5509 (1989)
   PUBMED   2564390
REFERENCE   10 (residues 1 to 561)
  AUTHORS   Zhang,Y.P., Lambert,M.A., Cairney,A.E., Wills,D., Ray,P.N. and
            Andrulis,I.L.
  TITLE     Molecular structure of the human asparagine synthetase gene
  JOURNAL   Genomics 4 (3), 259-265 (1989)
   PUBMED   2565875
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC014621.2, AA948141.1 and
            AC005326.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 21, 2008 this sequence version replaced NP_001664.2.
            
            Summary: The protein encoded by this gene is involved in the
            synthesis of asparagine. This gene complements a mutation in the
            temperature-sensitive hamster mutant ts11, which blocks progression
            through the G1 phase of the cell cycle at nonpermissive
            temperature. Alternatively spliced transcript variants have been
            described for this gene. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, and 7 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014621.2, M27396.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394308.8/ ENSP00000377845.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.3"
     Protein         1..561
                     /product="asparagine synthetase [glutamine-hydrolyzing]
                     isoform a"
                     /EC_number="6.3.5.4"
                     /note="glutamine-dependent asparagine synthetase; TS11
                     cell cycle control protein"
                     /calculated_mol_wt=64239
     Region          1..555
                     /region_name="asnB"
                     /note="asparagine synthetase B; Provisional; PRK09431"
                     /db_xref="CDD:236513"
     Site            365
                     /site_type="other"
                     /note="Important for beta-aspartyl-AMP intermediate
                     formation. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P08243.4)"
     Site            385
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08243.4)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08243.4)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08243.4)"
     CDS             1..561
                     /gene="ASNS"
                     /gene_synonym="ASNSD; TS11"
                     /coded_by="NM_001673.5:118..1803"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5652.1"
                     /db_xref="GeneID:440"
                     /db_xref="HGNC:HGNC:753"
                     /db_xref="MIM:108370"
ORIGIN      
        1 mcgiwalfgs ddclsvqcls amkiahrgpd afrfenvngy tnccfgfhrl avvdplfgmq
       61 pirvkkypyl wlcyngeiyn hkkmqqhfef eyqtkvdgei ilhlydkggi eqticmldgv
      121 fafvlldtan kkvflgrdty gvrplfkamt edgflavcse akglvtlkhs atpflkvepf
      181 lpghyevldl kpngkvasve mvkyhhcrdv plhalydnve klfpgfeiet vknnlrilfn
      241 navkkrlmtd rrigcllsgg ldsslvaatl lkqlkeaqvq yplqtfaigm edspdllaar
      301 kvadhigseh yevlfnseeg iqaldevifs letydittvr asvgmylisk yirkntdsvv
      361 ifsgegsdel tqgyiyfhka pspekaeees erllrelylf dvlradrtta ahglelrvpf
      421 ldhrfssyyl slppemripk ngiekhllre tfedsnlipk eilwrpkeaf sdgitsvkns
      481 wfkilqeyve hqvddamman aaqkfpfntp ktkegyyyrq vferhypgra dwlshywmpk
      541 winatdpsar tlthyksavk a
//
LOCUS       NP_055939                578 aa            linear   PRI 27-APR-2025
DEFINITION  GRAM domain-containing protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_055939 XP_005261455 XP_027105
VERSION     NP_055939.1
DBSOURCE    REFSEQ: accession NM_015124.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Zhang,J., Tu,K., Zhou,Z., Zheng,X., Gao,J., Yao,Y. and Liu,Q.
  TITLE     [Expression and clinicopathological significance of GRAMD4 in
            hepatocellular carcinoma]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 29 (2), 190-193 (2013)
   PUBMED   23388340
  REMARK    GeneRIF: The expression of GRAMD4 is up-regulated in hepatocellular
            carcinoma cell(HCC cell) lines and HCC tissues, and the increased
            expression is correlated with the clinicopathological
            characteristics of HCC.
REFERENCE   3  (residues 1 to 578)
  AUTHORS   John,K., Alla,V., Meier,C. and Putzer,B.M.
  TITLE     GRAMD4 mimics p53 and mediates the apoptotic function of p73 at
            mitochondria
  JOURNAL   Cell Death Differ 18 (5), 874-886 (2011)
   PUBMED   21127500
  REMARK    GeneRIF: GRAMD4 induces changes in Bcl-2 and Bax protein levels
            Erratum:[Cell Death Differ. 2012 Mar;19(3):552]
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Stanelle,J., Tu-Rapp,H. and Putzer,B.M.
  TITLE     A novel mitochondrial protein DIP mediates E2F1-induced apoptosis
            independently of p53
  JOURNAL   Cell Death Differ 12 (4), 347-357 (2005)
   PUBMED   15565177
  REMARK    GeneRIF: localizes to the mitochondria, upregulated following E2F1
            induction
            GeneRIF: DIP induces p53-independent caspase-dependent and
            -independent apoptosis. DIP is localized in the mitochondria. DIP
            accumulates upon E2F1 activation.
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Stanelle,J., Stiewe,T., Theseling,C.C., Peter,M. and Putzer,B.M.
  TITLE     Gene expression changes in response to E2F1 activation
  JOURNAL   Nucleic Acids Res 30 (8), 1859-1867 (2002)
   PUBMED   11937641
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021392.5 and AL096766.12.
            
            On or before Dec 16, 2015 this sequence version replaced
            XP_005261455.1, XP_027105.2.
            
            Summary: GRAMD4 is a mitochondrial effector of E2F1 (MIM
            189971)-induced apoptosis (Stanelle et al., 2005 [PubMed
            15565177]).[supplied by OMIM, Jan 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB018310.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000406902.6/ ENSP00000385689.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..578
                     /product="GRAM domain-containing protein 4 isoform 1"
                     /note="GRAM domain-containing protein 4;
                     death-inducing-protein"
                     /calculated_mol_wt=66277
     Region          23..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IC98.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6IC98.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6IC98.1)"
     Region          95..>213
                     /region_name="tolA_full"
                     /note="TolA protein; TIGR02794"
                     /db_xref="CDD:274303"
     Region          96..>151
                     /region_name="tolA"
                     /note="cell envelope integrity inner membrane protein
                     TolA; Provisional; PRK09510"
                     /db_xref="CDD:236545"
     Region          136..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IC98.1)"
     Site            240..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IC98.1)"
     Site            334..354
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IC98.1)"
     Site            356..376
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IC98.1)"
     Region          415..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IC98.1)"
     Region          460..565
                     /region_name="PH-GRAM_GRAMDC4"
                     /note="GRAM domain-containing protein 4 (GRAMDC4)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13221"
                     /db_xref="CDD:270041"
     CDS             1..578
                     /gene="GRAMD4"
                     /gene_synonym="DIP"
                     /coded_by="NM_015124.5:230..1966"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33672.1"
                     /db_xref="GeneID:23151"
                     /db_xref="HGNC:HGNC:29113"
                     /db_xref="MIM:613691"
ORIGIN      
        1 mlrrldkirf rghkrddfld laespnasdt ecsdeiplkv prtsprdsee lrdpagpgtl
       61 imatgvqdfn rtefdrlnei kghleialle khflqeelrk lreetnaeml rqeldrerqr
      121 rmeleqkvqe vlkarteeqm aqqppkgqaq asngaerrsq glssrlqkwf yerfgeyved
      181 frfqpeentv eteeplsarr ltenmrrlkr gakpvtnfvk nlsalsdwys vytsaiaftv
      241 ymnavwhgwa iplflflail rlslnyliar gwriqwsivp evsepveppk edltvsekfq
      301 lvldvaqkaq nlfgkmadil ekiknlfmwv qpeitqklyv alwaaflasc ffpyrlvgla
      361 vglyagikff lidfifkrcp rlrakydtpy iiwrslptdp qlkerssaav srrlqttssr
      421 syvpsapagl gkeedagrfh stkkgnfhei fnltenerpl avcengwrcc linrdrkmpt
      481 dyirngvlyv tenylcfess ksgsskrnkv iklvditdiq kykvlsvlpg sgmgiavstp
      541 stqkplvfga mvhrdeafet ilsqyikits aaasggds
//
LOCUS       NP_001350149             443 aa            linear   ROD 27-APR-2025
DEFINITION  gasdermin-A2 isoform 1 [Mus musculus].
ACCESSION   NP_001350149 XP_006534519
VERSION     NP_001350149.1
DBSOURCE    REFSEQ: accession NM_001363220.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Fattinger,S.A., Maurer,L., Geiser,P., Bernard,E.M., Enz,U.,
            Ganguillet,S., Gul,E., Kroon,S., Demarco,B., Mack,V., Furter,M.,
            Barthel,M., Pelczar,P., Shao,F., Broz,P., Sellin,M.E. and
            Hardt,W.D.
  TITLE     Gasdermin D is the only Gasdermin that provides protection against
            acute Salmonella gut infection in mice
  JOURNAL   Proc Natl Acad Sci U S A 120 (48), e2315503120 (2023)
   PUBMED   37988464
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Tamura,M., Tanaka,S., Fujii,T., Aoki,A., Komiyama,H., Ezawa,K.,
            Sumiyama,K., Sagai,T. and Shiroishi,T.
  TITLE     Members of a novel gene family, Gsdm, are expressed exclusively in
            the epithelium of the skin and gastrointestinal tract in a highly
            tissue-specific manner
  JOURNAL   Genomics 89 (5), 618-629 (2007)
   PUBMED   17350798
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Runkel,F., Marquardt,A., Stoeger,C., Kochmann,E., Simon,D.,
            Kohnke,B., Korthaus,D., Wattler,F., Fuchs,H., Hrabe de Angelis,M.,
            Stumm,G., Nehls,M., Wattler,S., Franz,T. and Augustin,M.
  TITLE     The dominant alopecia phenotypes Bareskin, Rex-denuded, and Reduced
            Coat 2 are caused by mutations in gasdermin 3
  JOURNAL   Genomics 84 (5), 824-835 (2004)
   PUBMED   15475261
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Evolutionary recombination hotspot around GSDML-GSDM locus is
            closely linked to the oncogenomic recombination hotspot around the
            PPP1R1B-ERBB2-GRB7 amplicon
  JOURNAL   Int J Oncol 24 (4), 757-763 (2004)
   PUBMED   15010812
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591125.20 and BC109335.1.
            
            On May 12, 2018 this sequence version replaced XP_006534519.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC109335.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849376, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 62.28 cM"
     Protein         1..443
                     /product="gasdermin-A2 isoform 1"
                     /note="gasdermin-2; gasderminA-2"
                     /calculated_mol_wt=49713
     Region          1..249
                     /region_name="Triggers pyroptosis.
                     /evidence=ECO:0000250|UniProtKB:Q96QA5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32M21.1)"
     Region          3..233
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Site            78..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32M21.1)"
     Site            99..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32M21.1)"
     Site            164..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32M21.1)"
     Site            183..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32M21.1)"
     Region          252..416
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..443
                     /gene="Gsdma2"
                     /gene_synonym="2200001G21Rik; 2210006M16Rik;
                     2210009F20Rik; 2210411P14Rik; Gsdm2; GsdmA-2; Gsdml2"
                     /coded_by="NM_001363220.1:102..1433"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS36301.1"
                     /db_xref="GeneID:76758"
                     /db_xref="MGI:MGI:1921490"
ORIGIN      
        1 msmfedvtra larqlnprgd ltpldslidf krfhpfclvl rkrkstlfwg aryvrtdytl
       61 ldvlepgssp sdptllgnfs fknmldvrve gdvevptmmk vkgtvglsqs stlevqmlsv
      121 aptalenlhm erklsadhpf lkemreykqn lyvvmevvka kqevtlkras naiskfslnl
      181 pslglqgsvn hkeavtipkg cvlayrvrql iiygkdewgi pyictdnmpt fnplcvlqrq
      241 gstvqmisge mhedfktlkk evqqetqeve klspvgrssl ltslshllgk kkelqdleqm
      301 legaldkghe vtlealpkdv lllkdamdai lyflgaltel seeqlkilvk slenkvlpvq
      361 lklvesileq nflqdkedvf plrpdllssl geedqiltea lvglsglevq rsgpqytwnp
      421 dtchnlcaly aglsllhlls rds
//
LOCUS       NP_001091988            1346 aa            linear   PRI 27-APR-2025
DEFINITION  adhesion G protein-coupled receptor F5 precursor [Homo sapiens].
ACCESSION   NP_001091988
VERSION     NP_001091988.1
DBSOURCE    REFSEQ: accession NM_001098518.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1346)
  AUTHORS   Xiang,Q., Li,N., Zhang,Y., Wang,T., Wang,Y. and Bian,J.
  TITLE     GPR116 alleviates acetaminophen-induced liver injury in mice by
            inhibiting endoplasmic reticulum stress
  JOURNAL   Cell Mol Life Sci 81 (1), 299 (2024)
   PUBMED   39001944
  REMARK    GeneRIF: GPR116 alleviates acetaminophen-induced liver injury in
            mice by inhibiting endoplasmic reticulum stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1346)
  AUTHORS   Wu,Y., Liu,H., Sun,Z., Liu,J., Li,K., Fan,R., Dai,F., Tang,H.,
            Hou,Q., Li,J. and Tang,X.
  TITLE     The adhesion-GPCR ADGRF5 fuels breast cancer progression by
            suppressing the MMP8-mediated antitumorigenic effects
  JOURNAL   Cell Death Dis 15 (6), 455 (2024)
   PUBMED   38937435
  REMARK    GeneRIF: The adhesion-GPCR ADGRF5 fuels breast cancer progression
            by suppressing the MMP8-mediated antitumorigenic effects.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1346)
  AUTHORS   Jacenik,D., Hikisz,P., Beswick,E.J. and Fichna,J.
  TITLE     The clinical relevance of the adhesion G protein-coupled receptor
            F5 for human diseases and cancers
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1869 (5), 166683 (2023)
   PUBMED   36878303
  REMARK    GeneRIF: The clinical relevance of the adhesion G protein-coupled
            receptor F5 for human diseases and cancers.
            Review article
REFERENCE   4  (residues 1 to 1346)
  AUTHORS   Kang,H., Fichna,J., Matlawska-Wasowska,K. and Jacenik,D.
  TITLE     The Expression Pattern of Adhesion G Protein-Coupled Receptor F5 Is
            Related to Cell Adhesion and Metastatic Pathways in Colorectal
            Cancer-Comprehensive Study Based on In Silico Analysis
  JOURNAL   Cells 11 (23), 3876 (2022)
   PUBMED   36497132
  REMARK    GeneRIF: The Expression Pattern of Adhesion G Protein-Coupled
            Receptor F5 Is Related to Cell Adhesion and Metastatic Pathways in
            Colorectal Cancer-Comprehensive Study Based on In Silico Analysis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1346)
  AUTHORS   Georgiadi,A., Lopez-Salazar,V., Merahbi,R.E., Karikari,R.A., Ma,X.,
            Mourao,A., Klepac,K., Buhler,L., Alfaro,A.J., Kaczmarek,I.,
            Linford,A., Bosma,M., Shilkova,O., Ritvos,O., Nakamura,N.,
            Hirose,S., Lassi,M., Teperino,R., Machado,J., Scheideler,M.,
            Dietrich,A., Geerlof,A., Feuchtinger,A., Blutke,A., Fischer,K.,
            Muller,T.D., Kessler,K., Schoneberg,T., Thor,D., Hornemann,S.,
            Kruse,M., Nawroth,P., Pivovarova-Ramich,O., Pfeiffer,A.F.H.,
            Sattler,M., Bluher,M. and Herzig,S.
  TITLE     Orphan GPR116 mediates the insulin sensitizing effects of the
            hepatokine FNDC4 in adipose tissue
  JOURNAL   Nat Commun 12 (1), 2999 (2021)
   PUBMED   34016966
  REMARK    GeneRIF: Orphan GPR116 mediates the insulin sensitizing effects of
            the hepatokine FNDC4 in adipose tissue.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1346)
  AUTHORS   Sandberg,A., Johansson,D.G., Macao,B. and Hard,T.
  TITLE     SEA domain autoproteolysis accelerated by conformational strain:
            energetic aspects
  JOURNAL   J Mol Biol 377 (4), 1117-1129 (2008)
   PUBMED   18308334
  REMARK    GeneRIF: SEA domain autoproteolysis accelerated by conformational
            strain.
            Erratum:[J Mol Biol. 2008 Jun 27;380(1):264]
REFERENCE   7  (residues 1 to 1346)
  AUTHORS   Liu,T., Qian,W.J., Gritsenko,M.A., Camp,D.G. 2nd, Monroe,M.E.,
            Moore,R.J. and Smith,R.D.
  TITLE     Human plasma N-glycoproteome analysis by immunoaffinity
            subtraction, hydrazide chemistry, and mass spectrometry
  JOURNAL   J Proteome Res 4 (6), 2070-2080 (2005)
   PUBMED   16335952
REFERENCE   8  (residues 1 to 1346)
  AUTHORS   Bjarnadottir,T.K., Fredriksson,R., Hoglund,P.J., Gloriam,D.E.,
            Lagerstrom,M.C. and Schioth,H.B.
  TITLE     The human and mouse repertoire of the adhesion family of
            G-protein-coupled receptors
  JOURNAL   Genomics 84 (1), 23-33 (2004)
   PUBMED   15203201
REFERENCE   9  (residues 1 to 1346)
  AUTHORS   Vassilatis,D.K., Hohmann,J.G., Zeng,H., Li,F., Ranchalis,J.E.,
            Mortrud,M.T., Brown,A., Rodriguez,S.S., Weller,J.R., Wright,A.C.,
            Bergmann,J.E. and Gaitanaris,G.A.
  TITLE     The G protein-coupled receptor repertoires of human and mouse
  JOURNAL   Proc Natl Acad Sci U S A 100 (8), 4903-4908 (2003)
   PUBMED   12679517
REFERENCE   10 (residues 1 to 1346)
  AUTHORS   Fredriksson,R., Lagerstrom,M.C., Hoglund,P.J. and Schioth,H.B.
  TITLE     Novel human G protein-coupled receptors with long N-terminals
            containing GPS domains and Ser/Thr-rich regions
  JOURNAL   FEBS Lett 531 (3), 407-414 (2002)
   PUBMED   12435584
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB230925.1, AB018301.2, AL096772.5, AY498875.1 and AY140958.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.261933.1,
                                           SRR1660807.130135.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283296.12/ ENSP00000283296.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.3"
     Protein         1..1346
                     /product="adhesion G protein-coupled receptor F5
                     precursor"
                     /note="probable G-protein coupled receptor 116; Ig-Hepta
                     homolog"
                     /calculated_mol_wt=147030
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2446
     mat_peptide     22..1346
                     /product="Adhesion G protein-coupled receptor F5.
                     /id=PRO_0000012896"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
                     /calculated_mol_wt=147030
     Site            51..52
                     /site_type="cleavage"
                     /note="Cleavage, by furin.
                     /evidence=ECO:0000250|UniProtKB:Q9WVT0; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          179..281
                     /region_name="SEA"
                     /note="SEA domain; cl02507"
                     /db_xref="CDD:470595"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            226..227
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250|UniProtKB:Q9WVT0;
                     propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          285..361
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          289..293
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..305
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            301
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            315
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            328
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          333..337
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          347..351
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            398
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            472
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          477..562
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Site            487
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            505
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            540
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            627
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            649
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            666
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            820
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            931
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          953..996
                     /region_name="GPS"
                     /note="GPCR proteolysis site, GPS, motif; pfam01825"
                     /db_xref="CDD:460350"
     Region          954..1003
                     /region_name="GPS.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            963
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            982
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            990..991
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098,
                     ECO:0000305|PubMed:36073784; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          991..1006
                     /region_name="Tethered agonist.
                     /evidence=ECO:0000269|PubMed:28570277,
                     ECO:0000269|PubMed:36073784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            1007..1027
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          1009..1283
                     /region_name="7tmB2_GPR116_Ig-Hepta"
                     /note="The immunoglobulin-repeat-containing receptor
                     Ig-hepta/GPR116, member of the class B2 family of
                     seven-transmembrane G protein-coupled receptors; cd15254"
                     /db_xref="CDD:320382"
     Region          1011..1036
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320382"
     Site            order(1016,1020,1068,1071..1072,1075,1087,1094,1171..1172,
                     1174,1176,1232,1235,1248,1252)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320382"
     Region          1051..1073
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320382"
     Site            1054..1074
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          1087..1110
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320382"
     Site            1091..1111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            1129..1149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          1130..1146
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320382"
     Region          1168..1191
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320382"
     Site            1174..1194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          1215..1240
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320382"
     Site            1221..1241
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          1245..1270
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320382"
     Site            1245..1265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            1300
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:G5E8Q8; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Site            1307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G5E8Q8; propagated from
                     UniProtKB/Swiss-Prot (Q8IZF2.3)"
     Region          1327..1346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZF2.3)"
     CDS             1..1346
                     /gene="ADGRF5"
                     /gene_synonym="GPR116; KPG_001"
                     /coded_by="NM_001098518.2:251..4291"
                     /db_xref="CCDS:CCDS4919.1"
                     /db_xref="GeneID:221395"
                     /db_xref="HGNC:HGNC:19030"
                     /db_xref="MIM:620874"
ORIGIN      
        1 mksprrttlc lmfiviyssk aalnwnyest ihplslhehe pageealrqk ravatkspta
       61 eeytvnieis fenasfldpi kaylnslsfp ihgnntdqit dilsinvttv crpagneiwc
      121 scetgygwpr erclhnlicq erdvflpghh csclkelppn gpfcllqedv tlnmrvrlnv
      181 gfqedlmnts salyrsyktd letafrkgyg ilpgfkgvtv tgfksgsvvv tyevkttpps
      241 lelihkaneq vvqslnqtyk mdynsfqavt inesnffvtp eiifegdtvs lvcekevlss
      301 nvswryeeqq leiqnssrfs iytalfnnmt svskltihni tpgdageyvc klildifeye
      361 ckkkidvmpi qilaneemkv mcdnnpvsln ccsqgnvnws kvewkqegki nipgtpetdi
      421 dsscsrytlk adgtqcpsgs sgttviytce fisaygargs anikvtfisv anltitpdpi
      481 svsegqnfsi kcisdvsnyd evywntsagi kiyqrfyttr ryldgaesvl tvktstrewn
      541 gtyhcifryk nsysiatkdv ivhplplkln imvdpleatv scsgshhikc cieedgdykv
      601 tfhtgssslp aakevnkkqv cykhnfnass vswcsktvdv cchftnaann svwspsmkln
      661 lvpgenitcq dpvigvgepg kviqklcrfs nvpsspespi ggtitykcvg sqweekrndc
      721 isapinsllq makaliksps qdemlptylk dlsisidkae heissspgsl gaiinildll
      781 stvptqvnse mmthvlstvn vilgkpvlnt wkvlqqqwtn qssqllhsve rfsqalqsgd
      841 spplsfsqtn vqmssmviks shpetyqqrf vfpyfdlwgn vvidksylen lqsdssivtm
      901 afptlqaila qdiqennfae slvmtttvsh nttmpfrism tfknnspsgg etkcvfwnfr
      961 lanntggwds sgcyveegdg dnvtcicdhl tsfsilmspd spdpssllgi lldiisyvgv
     1021 gfsilslaac lvveavvwks vtknrtsymr htcivniaas llvantwfiv vaaiqdnryi
     1081 lcktacvaat ffihffylsv ffwmltlglm lfyrlvfilh etsrstqkai afclgygcpl
     1141 aisvitlgat qprevytrkn vcwlnwedtk allafaipal iivvvnitit ivvitkilrp
     1201 sigdkpckqe ksslfqisks igvltpllgl twgfglttvf pgtnlvfhii failnvfqgl
     1261 fillfgclwd lkvqeallnk fslsrwssqh skstslgsst pvfsmsspis rrfnnlfgkt
     1321 gtynvstpea tssslensss asslln
//
LOCUS       NP_060506               2078 aa            linear   PRI 27-APR-2025
DEFINITION  autophagy-related protein 2 homolog B [Homo sapiens].
ACCESSION   NP_060506
VERSION     NP_060506.6
DBSOURCE    REFSEQ: accession NM_018036.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2078)
  AUTHORS   Wei,G., Chen,X., Ruan,T., Ma,X., Zhu,X., Wen,W., He,D., Tao,K. and
            Wu,C.
  TITLE     Human gastric cancer progression and stabilization of ATG2B through
            RNF5 binding facilitated by autophagy-associated CircDHX8
  JOURNAL   Cell Death Dis 15 (6), 410 (2024)
   PUBMED   38866787
  REMARK    GeneRIF: Human gastric cancer progression and stabilization of
            ATG2B through RNF5 binding facilitated by autophagy-associated
            CircDHX8.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2078)
  AUTHORS   Wen,J., Wan,L. and Dong,X.
  TITLE     The prognostic value of autophagy related genes with potential
            protective function in Ewing sarcoma
  JOURNAL   BMC Bioinformatics 23 (1), 306 (2022)
   PUBMED   35902797
  REMARK    GeneRIF: The prognostic value of autophagy related genes with
            potential protective function in Ewing sarcoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2078)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 2078)
  AUTHORS   Sakai,S.S., Hasegawa,A., Ishimura,R., Tamura,N., Kageyama,S.,
            Komatsu-Hirota,S., Abe,M., Ling,Y., Okuda,S., Funayama,M.,
            Kikkawa,M., Miura,Y., Sakimura,K., Narita,I., Waguri,S., Shimizu,R.
            and Komatsu,M.
  TITLE     Loss of Atg2b and Gskip Impairs the Maintenance of the
            Hematopoietic Stem Cell Pool Size
  JOURNAL   Mol Cell Biol 42 (1), e0002421 (2022)
   PUBMED   34748402
  REMARK    GeneRIF: Loss of Atg2b and Gskip Impairs the Maintenance of the
            Hematopoietic Stem Cell Pool Size.
REFERENCE   5  (residues 1 to 2078)
  AUTHORS   Saliba,J., Saint-Martin,C., Di Stefano,A., Lenglet,G., Marty,C.,
            Keren,B., Pasquier,F., Valle,V.D., Secardin,L., Leroy,G.,
            Mahfoudhi,E., Grosjean,S., Droin,N., Diop,M., Dessen,P.,
            Charrier,S., Palazzo,A., Merlevede,J., Meniane,J.C.,
            Delaunay-Darivon,C., Fuseau,P., Isnard,F., Casadevall,N.,
            Solary,E., Debili,N., Bernard,O.A., Raslova,H., Najman,A.,
            Vainchenker,W., Bellanne-Chantelot,C. and Plo,I.
  TITLE     Germline duplication of ATG2B and GSKIP predisposes to familial
            myeloid malignancies
  JOURNAL   Nat Genet 47 (10), 1131-1140 (2015)
   PUBMED   26280900
  REMARK    GeneRIF: demonstrate that overexpression of ATG2B and GSKIP
            enhances hematopoietic progenitor differentiation, including of
            megakaryocytes, by increasing progenitor sensitivity to
            thrombopoietin
REFERENCE   6  (residues 1 to 2078)
  AUTHORS   Velikkakath,A.K., Nishimura,T., Oita,E., Ishihara,N. and
            Mizushima,N.
  TITLE     Mammalian Atg2 proteins are essential for autophagosome formation
            and important for regulation of size and distribution of lipid
            droplets
  JOURNAL   Mol Biol Cell 23 (5), 896-909 (2012)
   PUBMED   22219374
  REMARK    GeneRIF: Depletion of both Atg2A and Atg2B causes clustering of
            enlarged lipid droplets in an autophagy-independent manner. These
            data suggest that mammalian Atg2 proteins function both in
            autophagosome formation and regulation of lipid droplet morphology
            and dispersion.
REFERENCE   7  (residues 1 to 2078)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   8  (residues 1 to 2078)
  AUTHORS   Kang,M.R., Kim,M.S., Oh,J.E., Kim,Y.R., Song,S.Y., Kim,S.S.,
            Ahn,C.H., Yoo,N.J. and Lee,S.H.
  TITLE     Frameshift mutations of autophagy-related genes ATG2B, ATG5, ATG9B
            and ATG12 in gastric and colorectal cancers with microsatellite
            instability
  JOURNAL   J Pathol 217 (5), 702-706 (2009)
   PUBMED   19197948
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 2078)
  AUTHORS   Xie,H., Diber,A., Pollock,S., Nemzer,S., Safer,H., Meloon,B.,
            Olson,A., Hwang,J.J., Endress,G.A., Savitsky,K. and Gill-More,R.
  TITLE     Bridging expressed sequence alignments through targeted cDNA
            sequencing
  JOURNAL   Genomics 83 (4), 572-576 (2004)
   PUBMED   15028280
REFERENCE   10 (residues 1 to 2078)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359240.4 and AL355102.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_060506.5.
            
            Summary: This gene encodes a protein required for autophagy. The
            encoded protein is involved in autophagosome formation. A germline
            duplication of a region that includes this gene is associated with
            predisposition to myeloid malignancies. [provided by RefSeq, Jul
            2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3938885.1,
                                           SRR14038194.3786590.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359933.6/ ENSP00000353010.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2078
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.2"
     Protein         1..2078
                     /product="autophagy-related protein 2 homolog B"
                     /note="ATG2 autophagy related 2 homolog B; bridge-like
                     lipid transfer protein family member 4B"
                     /calculated_mol_wt=232633
     Region          11..113
                     /region_name="Chorein_N"
                     /note="N-terminal region of Chorein or VPS13; pfam12624"
                     /db_xref="CDD:463646"
     Region          17..>234
                     /region_name="MRS6"
                     /note="Vacuolar protein sorting-associated protein
                     [Intracellular trafficking and secretion]; COG5043"
                     /db_xref="CDD:227376"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XK6; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Region          473..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            840
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Region          868..888
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            899
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            1008
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XK6; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            1012
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q80XK6; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            1016
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XK6; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            1018
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            1022
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q80XK6; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Region          1375..1405
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BY7.5)"
     Site            1526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96BY7.5)"
     Region          1980..2074
                     /region_name="ATG_C"
                     /note="Autophagy-related protein C terminal domain;
                     pfam09333"
                     /db_xref="CDD:462761"
     CDS             1..2078
                     /gene="ATG2B"
                     /gene_synonym="BLTP4B; C14orf103"
                     /coded_by="NM_018036.7:366..6602"
                     /db_xref="CCDS:CCDS9944.2"
                     /db_xref="GeneID:55102"
                     /db_xref="HGNC:HGNC:20187"
                     /db_xref="MIM:616226"
ORIGIN      
        1 mpwpfsesik kracryllqr ylghflqekl sleqlsldly qgtgslaqvp ldkwclneil
       61 esadaplevt egfiqsisls vpwgsllqdn calevrglem vfrprprpat gsepmywssf
      121 mtssmqlake clsqkltdeq gegsqpfegl ekfaetietv lrrvkvtfid tvlriehvpe
      181 nsktgtalei riertvycde tadessginv hqptafahkl lqlsgvslfw defsasakss
      241 pvcstapvet epklspswnp kiiyephpql trnlpeiaps dpvqigrlig rlelsltlkq
      301 nevlpgakld vdgqidsihl llsprqvhll ldmlaaiagp ensskiglan kdrknrpmqq
      361 edeyriqmel nryylrkdsl svgvsseqsf yetetartps sreeevffsm admdmshsls
      421 slpplgdppn mdlelsltst ytntpagspl satvlqptwg efldhhkeqp vrgstfpsnl
      481 vhptplqkts lpsrsvsvde srpelifrla vgtfsisvlh idplsppets qnlnpltpma
      541 vafftcieki dparfstedf ksfravfaea cshdhlrfig tgikvsyeqr qrsasryfst
      601 dmsigqmefl eclfptdfhs vpphytellt fhskeetgsh spvclqlhyk hsenrgpqgn
      661 qarlssvphk aelqiklnpv cceldisivd rlnsllqpqk latvemmash mytsynkhis
      721 lhkaftevfl ddshspancr isvqvatpal nlsvrfpipd lrsdqergpw fkkslqkeil
      781 ylaftdlefk tefiggstpe qikleltfre ligsfqeekg dpsikffhvs sgvdgdttss
      841 ddfdwprivl kinppamhsi leriaaeeee endghyqeee eggahslkdv cdlrrpapsp
      901 fssrrvmfen eqmvmpgdpv emtefqdkai snshyvlelt lpniyvtlpn ksfyeklynr
      961 ifndlllwep tapspvetfe nisygiglsv asqlintfnk dsfsafksav hydeesgsee
     1021 etlqyfstvd pnyrsrrkkk ldsqnknsqs flsvllninh gliavftdvk qdngdllenk
     1081 hgefwlefns gslfcvtkye gfddkhyicl hsssfslyhk givngvilpt etrlpsstrp
     1141 hwleptiyss eedglsktss dgvggdslnm lsvavkilsd ksesntkefl iavglkgatl
     1201 qhrmlpsgls wheqilyfln iadepvlgyn pptsfttfhv hlwscaldyr plylpirsll
     1261 tvetfsvsss valdkssstl riildeaalh lsdkcntvti nlsrdyvrvm dmglleltit
     1321 avksdsdgeq teprfelhcs sdvvhirtcs dscaalmnli qyiasygdlq tpnkadmkpg
     1381 afqrrskvds sgrsssrgpv lpeadqqmlr dlmsdameei dmqqgtssvk pqangvldek
     1441 sqiqepccsd lflfpdesgn vsqesgptya sfshhfisda mtgvptendd fcilfapkaa
     1501 mqekeeepvi kimvddaivi rdnyfslpvn ktdtskaplh fpipviryvv kevslvwhly
     1561 ggkdfgivpp tspaksyisp hsspshtptr hgrntvcggk grnhdflmei qlskvkfqhe
     1621 vyppckpdcd sslsehpvsr qvfivqdlei rdrlatsqmn kflylycske mprkahsnml
     1681 tvkalhvcpe sgrspqeccl rvslmplrln idqdalfflk dfftslsaev elqmtpdpev
     1741 kkspgadvtc slprhlstsk epnlvisfsg pkqpsqndsa nsvevvngme eknfsaeeas
     1801 frdqpvffre frftsevpir ldyhgkhvsm dqgtlagili glaqlncsel klkrlsyrhg
     1861 llgvdklfsy aitewlndik knqlpgilgg vgpmhslvql vqglkdlvwl pieqyrkdgr
     1921 ivrgfqrgaa sfgtstamaa leltnrmvqt iqaaaetayd mvspgtlsie pkktkrfphh
     1981 rlahqpvdlr egvakaysvv kegitdtaqt iyetaarehe srgvtgavge vlrqippavv
     2041 kplivateat snvlggmrnq irpdvrqdes qkwrhgdd
//
LOCUS       NP_542408                 89 aa            linear   PRI 27-APR-2025
DEFINITION  dynein light chain 2, cytoplasmic [Homo sapiens].
ACCESSION   NP_542408
VERSION     NP_542408.1
DBSOURCE    REFSEQ: accession NM_080677.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Day,C.L., Puthalakath,H., Skea,G., Strasser,A., Barsukov,I.,
            Lian,L.Y., Huang,D.C. and Hinds,M.G.
  TITLE     Localization of dynein light chains 1 and 2 and their pro-apoptotic
            ligands
  JOURNAL   Biochem J 377 (Pt 3), 597-605 (2004)
   PUBMED   14561217
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Lei,K. and Davis,R.J.
  TITLE     JNK phosphorylation of Bim-related members of the Bcl2 family
            induces Bax-dependent apoptosis
  JOURNAL   Proc Natl Acad Sci U S A 100 (5), 2432-2437 (2003)
   PUBMED   12591950
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Fuhrmann,J.C., Kins,S., Rostaing,P., El Far,O., Kirsch,J.,
            Sheng,M., Triller,A., Betz,H. and Kneussel,M.
  TITLE     Gephyrin interacts with Dynein light chains 1 and 2, components of
            motor protein complexes
  JOURNAL   J Neurosci 22 (13), 5393-5402 (2002)
   PUBMED   12097491
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Puthalakath,H., Villunger,A., O'Reilly,L.A., Beaumont,J.G.,
            Coultas,L., Cheney,R.E., Huang,D.C. and Strasser,A.
  TITLE     Bmf: a proapoptotic BH3-only protein regulated by interaction with
            the myosin V actin motor complex, activated by anoikis
  JOURNAL   Science 293 (5536), 1829-1832 (2001)
   PUBMED   11546872
  REMARK    Erratum:[Science 2002 Aug 16;297(5584):1122]
REFERENCE   10 (residues 1 to 89)
  AUTHORS   Naisbitt,S., Valtschanoff,J., Allison,D.W., Sala,C., Kim,E.,
            Craig,A.M., Weinberg,R.J. and Sheng,M.
  TITLE     Interaction of the postsynaptic density-95/guanylate kinase
            domain-associated protein complex with a light chain of myosin-V
            and dynein
  JOURNAL   J Neurosci 20 (12), 4524-4534 (2000)
   PUBMED   10844022
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA140058.1, BF528423.1, BC010744.1, DB022843.1, CN280282.1 and
            AC015813.12.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA140058.1, SRR3476690.1025326.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000579991.3/ ENSP00000477310.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q22"
     Protein         1..89
                     /product="dynein light chain 2, cytoplasmic"
                     /note="radial spoke 22 homolog; DLC8b; 8 kDa dynein light
                     chain b"
                     /calculated_mol_wt=10219
     Region          5..88
                     /region_name="DLC-like_DYNLL1_DYNLL2"
                     /note="dynein light chain (DLC)-like domain found in the
                     cytoplasmic dynein light chain 1 (DYNLL1) family; cd21452"
                     /db_xref="CDD:412000"
     Site            41
                     /site_type="other"
                     /note="Interaction with myosin V motor complex.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q96FJ2.1)"
     CDS             1..89
                     /gene="DYNLL2"
                     /gene_synonym="Dlc2; DNCL1B; RSPH22"
                     /coded_by="NM_080677.3:275..544"
                     /db_xref="CCDS:CCDS11601.1"
                     /db_xref="GeneID:140735"
                     /db_xref="HGNC:HGNC:24596"
                     /db_xref="MIM:608942"
ORIGIN      
        1 msdrkavikn admsedmqqd avdcatqame kyniekdiaa yikkefdkky nptwhcivgr
       61 nfgsyvthet khfiyfylgq vaillfksg
//
LOCUS       NP_004081                185 aa            linear   PRI 27-APR-2025
DEFINITION  dual specificity protein phosphatase 3 [Homo sapiens].
ACCESSION   NP_004081
VERSION     NP_004081.1
DBSOURCE    REFSEQ: accession NM_004090.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Ferruzo,P.Y.M., Boell,V.K., Russo,L.C., Oliveira,C.C. and
            Forti,F.L.
  TITLE     DUSP3 modulates IRES-dependent translation of mRNAs through
            dephosphorylation of the HNRNPC protein in cells under genotoxic
            stimulus
  JOURNAL   Biol Cell 116 (5), e2300128 (2024)
   PUBMED   38538536
  REMARK    GeneRIF: DUSP3 modulates IRES-dependent translation of mRNAs
            through dephosphorylation of the HNRNPC protein in cells under
            genotoxic stimulus.
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Chousakos,E., Katsoulas,N., Kavantzas,N., Stratigos,A. and
            Lazaris,A.C.
  TITLE     The role of dual-specificity phosphatase 3 in melanocytic
            oncogenesis
  JOURNAL   Exp Dermatol 31 (10), 1466-1476 (2022)
   PUBMED   35899430
  REMARK    GeneRIF: The role of dual-specificity phosphatase 3 in melanocytic
            oncogenesis.
            Review article
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Kim,B.R., Ha,J., Kang,E. and Cho,S.
  TITLE     Regulation of signal transducer and activator of transcription 3
            activation by dual-specificity phosphatase 3
  JOURNAL   BMB Rep 53 (6), 335-340 (2020)
   PUBMED   32475380
  REMARK    GeneRIF: Regulation of signal transducer and activator of
            transcription 3 activation by dual-specificity phosphatase 3.
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Russo,L.C., Farias,J.O. and Forti,F.L.
  TITLE     DUSP3 maintains genomic stability and cell proliferation by
            modulating NER pathway and cell cycle regulatory proteins
  JOURNAL   Cell Cycle 19 (12), 1545-1561 (2020)
   PUBMED   32380926
  REMARK    GeneRIF: DUSP3 maintains genomic stability and cell proliferation
            by modulating NER pathway and cell cycle regulatory proteins.
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Beaumont,V.A., Reiss,K., Qu,Z., Allen,B., Batista,V.S. and
            Loria,J.P.
  TITLE     Allosteric Impact of the Variable Insert Loop in Vaccinia
            H1-Related (VHR) Phosphatase
  JOURNAL   Biochemistry 59 (20), 1896-1908 (2020)
   PUBMED   32348128
  REMARK    GeneRIF: Allosteric Impact of the Variable Insert Loop in Vaccinia
            H1-Related (VHR) Phosphatase.
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Denu,J.M., Zhou,G., Wu,L., Zhao,R., Yuvaniyama,J., Saper,M.A. and
            Dixon,J.E.
  TITLE     The purification and characterization of a human dual-specific
            protein tyrosine phosphatase
  JOURNAL   J Biol Chem 270 (8), 3796-3803 (1995)
   PUBMED   7876121
  REMARK    Erratum:[J Biol Chem 1995 Apr 28;270(17):10358]
REFERENCE   7  (residues 1 to 185)
  AUTHORS   Jones,K.A., Black,D.M., Brown,M.A., Griffiths,B.L., Nicolai,H.M.,
            Chambers,J.A., Bonjardim,M., Xu,C.F., Boyd,M., McFarlane,R. et al.
  TITLE     The detailed characterisation of a 400 kb cosmid walk in the BRCA1
            region: identification and localisation of 10 genes including a
            dual-specificity phosphatase
  JOURNAL   Hum Mol Genet 3 (11), 1927-1934 (1994)
   PUBMED   7874108
REFERENCE   8  (residues 1 to 185)
  AUTHORS   Folander,K., Douglass,J. and Swanson,R.
  TITLE     Confirmation of the assignment of the gene encoding Kv1.3, a
            voltage-gated potassium channel (KCNA3) to the proximal short arm
            of human chromosome 1
  JOURNAL   Genomics 23 (1), 295-296 (1994)
   PUBMED   7829094
REFERENCE   9  (residues 1 to 185)
  AUTHORS   Kamb,A., Futreal,P.A., Rosenthal,J., Cochran,C., Harshman,K.D.,
            Liu,Q., Phelps,R.S., Tavtigian,S.V., Tran,T., Hussey,C. et al.
  TITLE     Localization of the VHR phosphatase gene and its analysis as a
            candidate for BRCA1
  JOURNAL   Genomics 23 (1), 163-167 (1994)
   PUBMED   7829067
REFERENCE   10 (residues 1 to 185)
  AUTHORS   Ishibashi,T., Bottaro,D.P., Chan,A., Miki,T. and Aaronson,S.A.
  TITLE     Expression cloning of a human dual-specificity phosphatase
  JOURNAL   Proc Natl Acad Sci U S A 89 (24), 12170-12174 (1992)
   PUBMED   1281549
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA104250.1, BC002682.1,
            AK129822.1, AC055813.9, DB171573.1, AK055834.1, DA167802.1,
            DA075379.1, BQ652984.1 and BQ575811.1.
            
            Summary: The protein encoded by this gene is a member of the dual
            specificity protein phosphatase subfamily. These phosphatases
            inactivate their target kinases by dephosphorylating both the
            phosphoserine/threonine and phosphotyrosine residues. They
            negatively regulate members of the mitogen-activated protein (MAP)
            kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated
            with cellular proliferation and differentiation. Different members
            of the family of dual specificity phosphatases show distinct
            substrate specificities for various MAP kinases, different tissue
            distribution and subcellular localization, and different modes of
            inducibility of their expression by extracellular stimuli. This
            gene maps in a region that contains the BRCA1 locus which confers
            susceptibility to breast and ovarian cancer. Although DUSP3 is
            expressed in both breast and ovarian tissues, mutation screening in
            breast cancer pedigrees and in sporadic tumors was negative,
            leading to the conclusion that this gene is not BRCA1. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.105724.1,
                                           SRR1803611.73793.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000226004.8/ ENSP00000226004.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..185
                     /product="dual specificity protein phosphatase 3"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="serine/threonine specific protein phosphatase;
                     vaccinia virus phosphatase VH1-related; dual specificity
                     protein phosphatase VHR; vaccinia H1-related phosphatase"
                     /calculated_mol_wt=20347
     Region          10..177
                     /region_name="DUSP3"
                     /note="dual specificity protein phosphatase 3; cd14579"
                     /db_xref="CDD:350427"
     CDS             1..185
                     /gene="DUSP3"
                     /gene_synonym="VHR"
                     /coded_by="NM_004090.4:54..611"
                     /db_xref="CCDS:CCDS11469.1"
                     /db_xref="GeneID:1845"
                     /db_xref="HGNC:HGNC:3069"
                     /db_xref="MIM:600183"
ORIGIN      
        1 msgsfelsvq dlndllsdgs gcyslpsqpc nevtpriyvg nasvaqdipk lqklgithvl
       61 naaegrsfmh vntnanfykd sgitylgika ndtqefnlsa yferaadfid qalaqkngrv
      121 lvhcregysr sptlviaylm mrqkmdvksa lsivrqnrei gpndgflaql cqlndrlake
      181 gklkp
//
LOCUS       NP_004246                150 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome c oxidase subunit 5A, mitochondrial precursor [Homo
            sapiens].
ACCESSION   NP_004246
VERSION     NP_004246.2
DBSOURCE    REFSEQ: accession NM_004255.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Cai,M., Qin,Y., Wan,A., Jin,H., Tang,J. and Chen,Z.
  TITLE     COX5A as a potential biomarker for disease activity and organ
            damage in lupus
  JOURNAL   Clin Exp Med 23 (8), 4745-4756 (2023)
   PUBMED   37891386
  REMARK    GeneRIF: COX5A as a potential biomarker for disease activity and
            organ damage in lupus.
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Zhang,P., Lu,H., Wu,Y., Lu,D., Li,C., Yang,X., Chen,Z., Qian,J. and
            Ge,J.
  TITLE     COX5A Alleviates Doxorubicin-Induced Cardiotoxicity by Suppressing
            Oxidative Stress, Mitochondrial Dysfunction and Cardiomyocyte
            Apoptosis
  JOURNAL   Int J Mol Sci 24 (12), 10400 (2023)
   PUBMED   37373547
  REMARK    GeneRIF: COX5A Alleviates Doxorubicin-Induced Cardiotoxicity by
            Suppressing Oxidative Stress, Mitochondrial Dysfunction and
            Cardiomyocyte Apoptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Zeng,J., Li,G., Xia,Y., Wang,F., Wang,Y., Xu,S., Zhou,Y., Liu,X.,
            Xie,X. and Zhang,J.
  TITLE     miR-204/COX5A axis contributes to invasion and chemotherapy
            resistance in estrogen receptor-positive breast cancers
  JOURNAL   Cancer Lett 492, 185-196 (2020)
   PUBMED   32758616
  REMARK    GeneRIF: miR-204/COX5A axis contributes to invasion and
            chemotherapy resistance in estrogen receptor-positive breast
            cancers.
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 150)
  AUTHORS   Oswald,C., Krause-Buchholz,U. and Rodel,G.
  TITLE     Knockdown of human COX17 affects assembly and supramolecular
            organization of cytochrome c oxidase
  JOURNAL   J Mol Biol 389 (3), 470-479 (2009)
   PUBMED   19393246
REFERENCE   7  (residues 1 to 150)
  AUTHORS   Uddin,M., Opazo,J.C., Wildman,D.E., Sherwood,C.C., Hof,P.R.,
            Goodman,M. and Grossman,L.I.
  TITLE     Molecular evolution of the cytochrome c oxidase subunit 5A gene in
            primates
  JOURNAL   BMC Evol Biol 8, 8 (2008)
   PUBMED   18197981
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 150)
  AUTHORS   Williams,S.L., Valnot,I., Rustin,P. and Taanman,J.W.
  TITLE     Cytochrome c oxidase subassemblies in fibroblast cultures from
            patients carrying mutations in COX10, SCO1, or SURF1
  JOURNAL   J Biol Chem 279 (9), 7462-7469 (2004)
   PUBMED   14607829
  REMARK    GeneRIF: study points to a role for surfeit 1(SURF1) in promoting
            the association of cytochrome c oxidase II with the cytochrome c
            oxidase I.cytochrome c oxidase subunit 4.cytochrome c oxidase
            subunit 5A subassembly
REFERENCE   9  (residues 1 to 150)
  AUTHORS   Hofmann,S., Lichtner,P., Schuffenhauer,S., Gerbitz,K.D. and
            Meitinger,T.
  TITLE     Assignment of the human genes coding for cytochrome c oxidase
            subunits Va (COX5A), VIc (COX6C) and VIIc (COX7C) to chromosome
            bands 15q25, 8q22-->q23 and 5q14 and of three pseudogenes (COX5AP1,
            COX6CP1, COX7CP1) to 14q22, 16p12 and 13q14-->q21 by FISH and
            radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 83 (3-4), 226-227 (1998)
   PUBMED   10072584
REFERENCE   10 (residues 1 to 150)
  AUTHORS   Rizzuto,R., Nakase,H., Zeviani,M., DiMauro,S. and Schon,E.A.
  TITLE     Subunit Va of human and bovine cytochrome c oxidase is highly
            conserved
  JOURNAL   Gene 69 (2), 245-256 (1988)
   PUBMED   2853101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AI815421.1, AK026623.1 and
            AC125435.8.
            
            On Jun 20, 2008 this sequence version replaced NP_004246.1.
            
            Summary: Cytochrome c oxidase (COX) is the terminal enzyme of the
            mitochondrial respiratory chain. It is a multi-subunit enzyme
            complex that couples the transfer of electrons from cytochrome c to
            molecular oxygen and contributes to a proton electrochemical
            gradient across the inner mitochondrial membrane. The complex
            consists of 13 mitochondrial- and nuclear-encoded subunits. The
            mitochondrially-encoded subunits perform the electron transfer of
            proton pumping activities. The functions of the nuclear-encoded
            subunits are unknown but they may play a role in the regulation and
            assembly of the complex. This gene encodes the nuclear-encoded
            subunit Va of the human mitochondrial respiratory chain enzyme. A
            pseudogene COX5AP1 has been found in chromosome 14q22. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.40972.1,
                                           SRR1163655.347096.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000322347.11/
                                                  ENSP00000317780.6
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..150
                     /product="cytochrome c oxidase subunit 5A, mitochondrial
                     precursor"
                     /EC_number="7.1.1.9"
                     /note="cytochrome c oxidase polypeptide, mitochondrial;
                     cytochrome c oxidase subunit 5A, mitochondrial; cytochrome
                     c oxidase subunit Va; mitochondrial cytochrome c oxidase
                     subunit Va; cytochrome c oxidase polypeptide Va"
                     /calculated_mol_wt=12501
     sig_peptide     1..41
                     /calculated_mol_wt=4279
     Region          2..17
                     /region_name="SIFI-degron.
                     /evidence=ECO:0000269|PubMed:38297121"
                     /note="propagated from UniProtKB/Swiss-Prot (P20674.2)"
     mat_peptide     42..150
                     /product="cytochrome c oxidase subunit 5A, mitochondrial"
                     /calculated_mol_wt=12501
     Region          45..146
                     /region_name="Cyt_c_Oxidase_Va"
                     /note="Cytochrome c oxidase subunit Va. Cytochrome c
                     oxidase (CcO), the terminal oxidase in the respiratory
                     chains of eukaryotes and most bacteria, is a multi-chain
                     transmembrane protein located in the inner membrane of
                     mitochondria and the cell membrane of...; cd00923"
                     /db_xref="CDD:238463"
     Site            order(49,52..53,81..85,119,122,125,128)
                     /site_type="other"
                     /note="Subunit Va/VIc interface [polypeptide binding]"
                     /db_xref="CDD:238463"
     Site            order(68,72)
                     /site_type="other"
                     /note="Subunit Va/Vb interface [polypeptide binding]"
                     /db_xref="CDD:238463"
     Site            order(71,75,97,100..104,107,110..111,114,138,140)
                     /site_type="other"
                     /note="Subunit Va/IV interface [polypeptide binding]"
                     /db_xref="CDD:238463"
     Site            order(79,81,115)
                     /site_type="other"
                     /note="Subunit Va/II interface [polypeptide binding]"
                     /db_xref="CDD:238463"
     Site            87
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P12787; propagated from
                     UniProtKB/Swiss-Prot (P20674.2)"
     Site            113
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P12787; propagated from
                     UniProtKB/Swiss-Prot (P20674.2)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P20674.2)"
     CDS             1..150
                     /gene="COX5A"
                     /gene_synonym="COX; COX-VA; MC4DN20; VA"
                     /coded_by="NM_004255.4:60..512"
                     /db_xref="CCDS:CCDS10273.1"
                     /db_xref="GeneID:9377"
                     /db_xref="HGNC:HGNC:2267"
                     /db_xref="MIM:603773"
ORIGIN      
        1 mlgaalrrca vaattradpr gllhsartpg pavaiqsvrc yshgsqetde efdarwvtyf
       61 nkpdidawel rkgintlvty dmvpepkiid aalracrrln dfastvrile vvkdkagphk
      121 eiypyviqel rptlnelgis tpeelgldkv
//
LOCUS       NP_940878                351 aa            linear   PRI 27-APR-2025
DEFINITION  actin maturation protease isoform 1 [Homo sapiens].
ACCESSION   NP_940878 XP_209143
VERSION     NP_940878.3
DBSOURCE    REFSEQ: accession NM_198476.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Haahr,P., Galli,R.A., van den Hengel,L.G., Bleijerveld,O.B.,
            Kazokaite-Adomaitiene,J., Song,J.Y., Kroese,L.J., Krimpenfort,P.,
            Baltissen,M.P., Vermeulen,M., Ottenheijm,C.A.C. and
            Brummelkamp,T.R.
  TITLE     Actin maturation requires the ACTMAP/C19orf54 protease
  JOURNAL   Science 377 (6614), 1533-1537 (2022)
   PUBMED   36173861
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020945.6, BC020262.1, DA073426.1 and AI250667.1.
            
            On Feb 7, 2008 this sequence version replaced NP_940878.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020262.1, SRR1803615.138769.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378313.7/ ENSP00000367564.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..351
                     /product="actin maturation protease isoform 1"
                     /note="UPF0692 protein C19orf54; actin aminopeptidase
                     ACTMAP"
                     /calculated_mol_wt=37648
     Region          1..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKX5.2)"
     Region          124..244
                     /region_name="Peptidase C39-like.
                     /evidence=ECO:0000303|PubMed:36173861"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKX5.2)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5BKX5.2)"
     CDS             1..351
                     /gene="ACTMAP"
                     /gene_synonym="C19orf54"
                     /coded_by="NM_198476.5:675..1730"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12564.2"
                     /db_xref="GeneID:284325"
                     /db_xref="HGNC:HGNC:24758"
                     /db_xref="MIM:620093"
ORIGIN      
        1 mtspcspplk ppisppktpv pqassipspp lppspldfsa lpsppwsqqt pvppplplpp
       61 ppaatgpapr hvfgleksql lkeafdkagp vpkgredvkr llklhkdrfr gdlrwilfca
      121 dlpsliqegp qcglvalwma gtllsppsgv plerlirvat ergytaqgem fsvadmgrla
      181 qevlgcqakl lsgglggpnr dlvlqhlvtg hpllipyded fnhepcqrkg hkahwavsag
      241 vllgvravps lgytedpelp glfhpvlgtp cqppslpeeg spgavyllsk qgkswhyqlw
      301 dydqvresnl qltdfspsra tdgrvyvvpv ggvraglcgq allltpqdcs h
//
LOCUS       NP_055928               2961 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger ZZ-type and EF-hand domain-containing protein 1 [Homo
            sapiens].
ACCESSION   NP_055928 XP_001127649 XP_001719669 XP_001723950
VERSION     NP_055928.3
DBSOURCE    REFSEQ: accession NM_015113.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2961)
  AUTHORS   Yu,Y., Tencer,A., Xuan,H., Kutateladze,T.G. and Shi,X.
  TITLE     ZZEF1 is a Histone Reader and Transcriptional Coregulator of
            Kruppel-Like Factors
  JOURNAL   J Mol Biol 433 (2), 166722 (2021)
   PUBMED   33227311
REFERENCE   2  (residues 1 to 2961)
  AUTHORS   McGrath,L.M., Cornelis,M.C., Lee,P.H., Robinson,E.B., Duncan,L.E.,
            Barnett,J.H., Huang,J., Gerber,G., Sklar,P., Sullivan,P.,
            Perlis,R.H. and Smoller,J.W.
  TITLE     Genetic predictors of risk and resilience in psychiatric disorders:
            a cross-disorder genome-wide association study of functional
            impairment in major depressive disorder, bipolar disorder, and
            schizophrenia
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 162B (8), 779-788 (2013)
   PUBMED   24039173
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087292.14, AB007859.4, AK127482.1, BC047285.1 and BC067099.1.
            
            On or before Jun 11, 2008 this sequence version replaced
            XP_001723950.1, XP_001719669.1, XP_001127649.2, NP_055928.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC151836.1, AB007859.4 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381638.7/ ENSP00000371051.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2961
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..2961
                     /product="zinc finger ZZ-type and EF-hand
                     domain-containing protein 1"
                     /note="zinc finger, ZZ-type with EF hand domain 1"
                     /calculated_mol_wt=330946
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43149.6)"
     Region          <95..141
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Region          251..380
                     /region_name="APC10-ZZEF1"
                     /note="APC10/DOC1-like domain of uncharacterized Zinc
                     finger ZZ-type and EF-hand domain-containing protein 1
                     (ZZEF1) and homologs; cd08667"
                     /db_xref="CDD:176488"
     Site            order(276,304,310,312,372)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:176488"
     Region          <1119..1189
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cl00049"
                     /db_xref="CDD:412131"
     Region          1446..1531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43149.6)"
     Site            1475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSH7; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Site            1509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Site            1512
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Site            1518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Site            1521
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSH7; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Site            1523
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Site            1537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Site            1540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Region          1781..1828
                     /region_name="ZZ_EF"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     proteins with an EF_hand motif. The ZZ motif coordinates
                     two zinc ions and most likely participates in ligand
                     binding or molecular scaffolding; cd02343"
                     /db_xref="CDD:239083"
     Site            order(1783,1786,1797,1800,1806,1809,1819,1823)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239083"
     Site            order(1783,1786,1806,1809)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239083"
     Site            order(1784,1794,1796,1802,1804)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239083"
     Site            order(1795,1810,1825,1828)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239083"
     Site            order(1797,1800,1819,1823)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239083"
     Region          1830..1877
                     /region_name="ZZ"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin, CBP/p300 and many other proteins. The ZZ motif
                     coordinates one or two zinc ions and most likely
                     participates in ligand binding or molecular scaffolding.
                     Many proteins containing ZZ motifs have...; cd02249"
                     /db_xref="CDD:239069"
     Site            order(1832,1835,1846,1849,1855,1858,1868,1872)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239069"
     Site            order(1832,1835,1855,1858)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239069"
     Site            order(1833,1843,1845,1851,1853)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239069"
     Site            order(1844,1859,1874,1877)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239069"
     Site            order(1846,1849,1868,1872)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239069"
     Region          1994..2078
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43149.6)"
     Region          2426..2455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43149.6)"
     Site            2444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     Site            2667
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O43149.6)"
     CDS             1..2961
                     /gene="ZZEF1"
                     /gene_synonym="ZZZ4"
                     /coded_by="NM_015113.4:136..9021"
                     /db_xref="CCDS:CCDS11043.1"
                     /db_xref="GeneID:23140"
                     /db_xref="HGNC:HGNC:29027"
                     /db_xref="MIM:619459"
ORIGIN      
        1 mgnapshsse deaaaaggeg wgphqdwaav sgttpgpgva apalppaaal leparlreaa
       61 aallptppce slvsrhrgal frwleerlgr geesvtleqf relleargag csseqfeeaf
      121 aqfdaegdgt vdaenmleal knssganlqg elshiirqlq acslvpgftd ifseskegld
      181 ihssmilrfl hrnrlssavm pypmlehcnn mctmrssvlk esldqlvqke kespgdltrs
      241 pemdklksva kcyayietss nsadidkmtn getssywqsd gsacshwirl kmkpdvvlrh
      301 lsiavaatdq sympqqvtva vgrnasdlqe vrdvhipsnv tgyvtllena nvsqlyvqin
      361 ikrclsdgcd trihglravg fqrvkksgvs vsdasaiwyw slltslvtas metnpafvqt
      421 vlhntqkalr hmpplslspg stdfstflsp nvleevdsfl iritsccstp eveltllafa
      481 largsvakvm sslctitdhl dtqydassli lsmasvrqnl llkygkplql tlqacdvkgk
      541 edksgpenll vepwtrdgfl tetgktrast ifstgtesaf qvtqirimvr rggigaqcgl
      601 vfaynsssdk fcaeehfkrf ekydkwklqe lrqfvksrig cssddlgedd pigwfeleee
      661 wdeadvklqq crvakylmvk flctrqesae rlgvqgltis gylrparaea eqsvtcahcr
      721 kdteesvcga tlllrtlqfi qqlahdlvqq kesglkyksf ldfagldlqi fwnfysklkq
      781 npreecvsaq tlllqllqsc fsvlqgdvla aseeekapiq spkgveaake lythlcdvvd
      841 kvdgdsvpme ilkqevrntl lngaaiffpn rqtrrnhlft mmnvteqehk qslqltfrsl
      901 ctyfsdkdpg gllllpeknd lakmnisevl avmdtlvsva arecellmls gapgevgsvl
      961 fslfwsvqgs llswcylqlk stdsgakdla vdliekyvgq flasmraile slfsqysgkt
     1021 iverlcnsvf smaarqlvif lldfctldip hcvllrefsv ltellkklcs gpegglrkld
     1081 vetwqqeqpv vlhtwtkesa hnyennchev svfvspgaty fevefddrce tekrydylef
     1141 tdargrktry dtkvgtdkwp kkvtfkagpr lqflfhsdss hnewgykftv tacglpdvav
     1201 swgldlqllv srlmgrlasq cmalksvrql gsnmvvpqak malvlssplw kpvfrhqvcp
     1261 eleleaswpt hphrnskevk nipddpcrhf lldfaqsepa qnfcgpysel fkgfiqacrk
     1321 qapktdivag stidqavnat faalvyrtpd lyeklqkyvn sggkialsee faqvysladg
     1381 iriwmlemkq kslmslgnea eekhsseate vnpeslakec ieksllllkf lptgisskes
     1441 cekletadet shlqplnkrq rtssvveehf qasvspteaa ppatgdqspg lgtqpklpss
     1501 sglpaadvsp ataeeplsps tptrrppftr grlrllsfrs meearlvptv kekypvlkdv
     1561 mdfikdqsls hrsvvkvlsl rkaqaqsile vlkitqhcae slgqphcfhp pfilfllell
     1621 tcqkdftnyf ghlegcgadl hkeirdtyyq lvlflvkavk gfsslndrsl lpalscvqta
     1681 llhlldmgwe pndlaffvdi qlpdllmkms qenisvhdsv isqwseedel adakqnsewm
     1741 decqdgmfea wyekiaqedp ekqrkmhmfi arycdllnvd iscdgcdeia pwhryrclqc
     1801 sdmdlcktcf lggvkpeghg ddhemvnmef tcdhcqglii grrmncnvcd dfdlcygcya
     1861 akkysyghlp thsitahpmv tirisdrqrl iqpyihnysw llfaalalys ahlasaedvd
     1921 gekldpqtrs sattlrsqcm qlvgdclmka hqgkglkala llgvlpdgds sledqalpvt
     1981 vptgaseeql ekkavqgael seagngkrav heeirpvdfk qrnkadkgvs lskdpscqtq
     2041 isdspadasp ptglpdaeds evssqkpiee kavtpspeqv faecsqkril gllaamlppl
     2101 ksgptvplid lehvlplmfq vvisnaghln etyhltlgll gqliirllpa evdaavikvl
     2161 sakhnlfaag dssivpdgwk tthllfslga vcldsrvgld wacsmaeilr slnsaplwrd
     2221 viatftdhci kqlpfqlkht niftllvlvg fpqvlcvgtr cvymdnanep hnviilkhft
     2281 eknravivdv ktrkrktvkd yqlvqkgggq ecgdsraqls qysqhfafia shllqssmds
     2341 hcpeaveatw vlslalkgly ktlkahgfee iratflqtdl lkllvkkcsk gtgfsktwll
     2401 rdleilsiml ysskkeinal aehgdlelde rgdreeever pvsspgdpeq kkldplegld
     2461 eptricflma hdalnaplhi lraiyelqmk ktdyfflevq krfdgdeltt derirslaqr
     2521 wqpskslrle eqsakavdtd miilpclsrp arcdqataes npvtqkliss teselqqsya
     2581 kqrrsksaal lhkelncksk ravrdylfrv neatavlyar hvlasllaew pshvpvsedi
     2641 lelsgpahmt yildmfmqle ekhewekilq kvlqgcredm lgtmalaacq fmeepgmevq
     2701 vreskhpynn ntnfedkvhi pgaiylsikf dsqcnteegc delamssssd fqqdrhsfsg
     2761 sqqkwkdfel pgdtlyyrft sdmsntewgy rftvtaghlg rfqtgfeilk qmlseervvp
     2821 hlplakiwew lvgvacrqtg hqrlkaihll lrivrccghs dlcdlallkp lwqlfthmey
     2881 glfedvtqpg illplhralt elffvtenra qelgvlqdyl lalttddhll rcaaqalqni
     2941 aaislainyp nkatrlwnve c
//
LOCUS       NP_001353119             434 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 565 isoform 2 [Homo sapiens].
ACCESSION   NP_001353119 XP_016881831
VERSION     NP_001353119.1
DBSOURCE    REFSEQ: accession NM_001366190.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012617.7 and AC008848.9.
            
            On Sep 25, 2018 this sequence version replaced XP_016881831.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            lacks a portion of the 5' coding region compared to variant 1. The
            encoded isoform (2) has a shorter N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.231341.1, AK308212.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..434
                     /product="zinc finger protein 565 isoform 2"
                     /calculated_mol_wt=50322
     Region          103..433
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          104..124
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(109,111,113,115..116,119..120,123,137,139,143..144,
                     147..148,151,165,167,169,171..172,175..176,179)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          132..152
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          160..180
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          188..208
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          216..236
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          244..264
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(249,251,253,255..256,259..260,263,277,279,283..284,
                     287..288,291,305,307,309,311..312,315..316,319)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          272..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          356..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          384..404
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          412..432
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..434
                     /gene="ZNF565"
                     /coded_by="NM_001366190.1:231..1535"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:147929"
                     /db_xref="HGNC:HGNC:26726"
                     /db_xref="MIM:614275"
ORIGIN      
        1 miandvtgpw cpdlesrcek flqkdifeig afnweimesl kcsdlegsdf radwecegqf
       61 erqvneecyf kqvnvtyghm pvfqhhtsht vrqsretgek lmechecgka fsrgshliqh
      121 qkihtgekpf gckecgkafs rashlvqhqr ihtgekpydc kdcgkafgrt selilhqrlh
      181 tgvkpyecke cgktfrqhsq lilhqrthtg ekpyvckdcg kafirgsqlt vhrrihtgar
      241 pyeckecgka frqhsqltvh qrihtgekpy eckecgkgfi hssevtrhqr ihsgekpyec
      301 kecgkafrqh aqltrhqrvh tgdrpyeckd cgkafsrssy liqhqrihtg dkpyeckecg
      361 kafirvsqlt hhqrihtcek pyecrecgma firssqlteh qrihpgikpy ecrecgqafi
      421 lgsqliehyr ihtg
//
LOCUS       NP_002475                320 aa            linear   PRI 27-APR-2025
DEFINITION  cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_002475
VERSION     NP_002475.2
DBSOURCE    REFSEQ: accession NM_002484.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Bargagna,B., Matteucci,S., Ciofi-Baffoni,S., Camponeschi,F. and
            Banci,L.
  TITLE     Unraveling the mechanism of [4Fe-4S] cluster assembly on the
            N-terminal cluster binding site of NUBP1
  JOURNAL   Protein Sci 32 (5), e4625 (2023)
   PUBMED   36916754
  REMARK    GeneRIF: Unraveling the mechanism of [4Fe-4S] cluster assembly on
            the N-terminal cluster binding site of NUBP1.
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Camponeschi,F., Prusty,N.R., Heider,S.A.E., Ciofi-Baffoni,S. and
            Banci,L.
  TITLE     GLRX3 Acts as a [2Fe-2S] Cluster Chaperone in the Cytosolic
            Iron-Sulfur Assembly Machinery Transferring [2Fe-2S] Clusters to
            NUBP1
  JOURNAL   J Am Chem Soc 142 (24), 10794-10805 (2020)
   PUBMED   32429669
  REMARK    GeneRIF: GLRX3 Acts as a [2Fe-2S] Cluster Chaperone in the
            Cytosolic Iron-Sulfur Assembly Machinery Transferring [2Fe-2S]
            Clusters to NUBP1.
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Hosgood,H.D. 3rd, Menashe,I., He,X., Chanock,S. and Lan,Q.
  TITLE     PTEN identified as important risk factor of chronic obstructive
            pulmonary disease
  JOURNAL   Respir Med 103 (12), 1866-1870 (2009)
   PUBMED   19625176
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Shen,M., Vermeulen,R., Rajaraman,P., Menashe,I., He,X.,
            Chapman,R.S., Yeager,M., Thomas,G., Burdett,L., Hutchinson,A.,
            Yuenger,J., Chanock,S. and Lan,Q.
  TITLE     Polymorphisms in innate immunity genes and lung cancer risk in
            Xuanwei, China
  JOURNAL   Environ Mol Mutagen 50 (4), 285-290 (2009)
   PUBMED   19170196
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Hosgood,H.D. 3rd, Menashe,I., Shen,M., Yeager,M., Yuenger,J.,
            Rajaraman,P., He,X., Chatterjee,N., Caporaso,N.E., Zhu,Y.,
            Chanock,S.J., Zheng,T. and Lan,Q.
  TITLE     Pathway-based evaluation of 380 candidate genes and lung cancer
            susceptibility suggests the importance of the cell cycle pathway
  JOURNAL   Carcinogenesis 29 (10), 1938-1943 (2008)
   PUBMED   18676680
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Stehling,O., Netz,D.J., Niggemeyer,B., Rosser,R., Eisenstein,R.S.,
            Puccio,H., Pierik,A.J. and Lill,R.
  TITLE     Human Nbp35 is essential for both cytosolic iron-sulfur protein
            assembly and iron homeostasis
  JOURNAL   Mol Cell Biol 28 (17), 5517-5528 (2008)
   PUBMED   18573874
  REMARK    GeneRIF: The cytosolic soluble P-loop NTPase termed huNbp35 (also
            known as Nubp1) was identified as an Fe/S protein, and its role in
            the maturation of Fe/S proteins in HeLa cells, is defined.
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Taniguchi,N., Taniura,H., Niinobe,M., Takayama,C.,
            Tominaga-Yoshino,K., Ogura,A. and Yoshikawa,K.
  TITLE     The postmitotic growth suppressor necdin interacts with a
            calcium-binding protein (NEFA) in neuronal cytoplasm
  JOURNAL   J Biol Chem 275 (41), 31674-31681 (2000)
   PUBMED   10915798
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Nakashima,H., Grahovac,M.J., Mazzarella,R., Fujiwara,H.,
            Kitchen,J.R., Threat,T.A. and Ko,M.S.
  TITLE     Two novel mouse genes--Nubp2, mapped to the t-complex on chromosome
            17, and Nubp1, mapped to chromosome 16--establish a new gene family
            of nucleotide-binding proteins in eukaryotes
  JOURNAL   Genomics 60 (2), 152-160 (1999)
   PUBMED   10486206
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Shahrestanifar,M., Saha,D.P., Scala,L.A., Basu,A. and Howells,R.D.
  TITLE     Cloning of a human cDNA encoding a putative nucleotide-binding
            protein related to Escherichia coli MinD
  JOURNAL   Gene 147 (2), 281-285 (1994)
   PUBMED   7926816
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP225034.1 and AK223204.1.
            
            On Dec 1, 2006 this sequence version replaced NP_002475.1.
            
            Summary: NUBP1 is a member of the NUBP/MRP subfamily of ATP-binding
            proteins (Nakashima et al., 1999 [PubMed 10486206]).[supplied by
            OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.94264.1,
                                           SRR5189667.235878.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283027.10/ ENSP00000283027.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.13"
     Protein         1..320
                     /product="cytosolic Fe-S cluster assembly factor NUBP1
                     isoform 1"
                     /note="nucleotide binding protein 1 (MinD homolog, E.
                     coli); nucleotide binding protein 1 (E.coli MinD like);
                     cytosolic Fe-S cluster assembly factor NUBP1; nucleotide
                     binding protein (e.coli MinD like); NBP 1;
                     nucleotide-binding protein 1"
                     /calculated_mol_wt=34404
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P53384.2)"
     Region          53..303
                     /region_name="ParA"
                     /note="NUBPL iron-transfer P-loop NTPase; pfam10609"
                     /db_xref="CDD:431392"
     Site            order(63..70,202,204,229..230,268..270,273..274)
                     /site_type="active"
                     /db_xref="CDD:349757"
     Site            order(63..65,95..96,98,101..102,145..146,176,178,181,208,
                     211,269,271..272,274)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349757"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5I0L4; propagated from
                     UniProtKB/Swiss-Prot (P53384.2)"
     CDS             1..320
                     /gene="NUBP1"
                     /gene_synonym="CIAO5; NBP; NBP1; NBP35"
                     /coded_by="NM_002484.4:23..985"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10543.1"
                     /db_xref="GeneID:4682"
                     /db_xref="HGNC:HGNC:8041"
                     /db_xref="MIM:600280"
ORIGIN      
        1 meevphdcpg adsaqagrga scqgcpnqrl casgagatpd taieeikekm ktvkhkilvl
       61 sgkggvgkst fsahlahgla edentqiall didicgpsip kimglegeqv hqsgsgwspv
      121 yvednlgvms vgfllsspdd aviwrgpkkn gmikqflrdv dwgevdyliv dtppgtsdeh
      181 lsvvrylata hidgaviitt pqevslqdvr keinfcrkvk lpiigvvenm sgficpkckk
      241 esqifppttg gaelmcqdle vpllgrvpld pligkncdkg qsffidapds patlayrsii
      301 qriqefcnlh qskeenliss
//
LOCUS       NP_001003818             516 aa            linear   PRI 27-APR-2025
DEFINITION  tripartite motif-containing protein 6 isoform 1 [Homo sapiens].
ACCESSION   NP_001003818
VERSION     NP_001003818.1
DBSOURCE    REFSEQ: accession NM_001003818.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Zhou,J., Zhou,Y., Wei,X.F., Fan,L., Gao,X., Li,Y., Wu,Y., Feng,W.,
            Shen,X., Liu,L., Xu,G. and Zhang,Z.
  TITLE     TRIM6 facilitates SARS-CoV-2 proliferation by catalyzing the
            K29-typed ubiquitination of NP to enhance the ability to bind viral
            genomes
  JOURNAL   J Med Virol 96 (3), e29531 (2024)
   PUBMED   38515377
  REMARK    GeneRIF: TRIM6 facilitates SARS-CoV-2 proliferation by catalyzing
            the K29-typed ubiquitination of NP to enhance the ability to bind
            viral genomes.
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Liao,L., Tao,P., Xu,Q., Chen,W., Chen,J., Liu,W., Liu,W., Hu,J. and
            Lu,J.
  TITLE     TRIM6 Promotes ROS-Mediated Inflammasome Activation and Pyroptosis
            in Renal Tubular Epithelial Cells via Ubiquitination and
            Degradation of GPX3 Protein
  JOURNAL   Front Biosci (Landmark Ed) 29 (2), 58 (2024)
   PUBMED   38420829
  REMARK    GeneRIF: TRIM6 Promotes ROS-Mediated Inflammasome Activation and
            Pyroptosis in Renal Tubular Epithelial Cells via Ubiquitination and
            Degradation of GPX3 Protein.
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Liu,X., Zhao,J., Dong,P., Du,X., Lu,W., Feng,Y. and Wang,L.
  TITLE     TRIM6 silencing for inhibiting growth and angiogenesis of gliomas
            by regulating VEGFA
  JOURNAL   J Chem Neuroanat 132, 102291 (2023)
   PUBMED   37236551
  REMARK    GeneRIF: TRIM6 silencing for inhibiting growth and angiogenesis of
            gliomas by regulating VEGFA.
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Guo,J., Feng,S., Liu,H., Chen,Z., Ding,C., Jin,Y., Chen,X.,
            Ling,Y., Zeng,Y., Long,H. and Qiu,H.
  TITLE     TRIM6: An Upregulated Biomarker with Prognostic Significance and
            Immune Correlations in Gliomas
  JOURNAL   Biomolecules 13 (9), 1298 (2023)
   PUBMED   37759698
  REMARK    GeneRIF: TRIM6: An Upregulated Biomarker with Prognostic
            Significance and Immune Correlations in Gliomas.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 516)
  AUTHORS   Zhang,Y., Yuan,L., Cui,S. and Wu,S.
  TITLE     Tripartite motif protein 6 promotes hepatocellular carcinoma
            progression via multiple pathways
  JOURNAL   Turk J Med Sci 53 (5), 1032-1044 (2023)
   PUBMED   38813007
  REMARK    GeneRIF: Tripartite motif protein 6 promotes hepatocellular
            carcinoma progression via multiple pathways.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 516)
  AUTHORS   Li,X., Gold,B., O'hUigin,C., Diaz-Griffero,F., Song,B., Si,Z.,
            Li,Y., Yuan,W., Stremlau,M., Mische,C., Javanbakht,H., Scally,M.,
            Winkler,C., Dean,M. and Sodroski,J.
  TITLE     Unique features of TRIM5alpha among closely related human TRIM
            family members
  JOURNAL   Virology 360 (2), 419-433 (2007)
   PUBMED   17156811
REFERENCE   7  (residues 1 to 516)
  AUTHORS   Li,X., Li,Y., Stremlau,M., Yuan,W., Song,B., Perron,M. and
            Sodroski,J.
  TITLE     Functional replacement of the RING, B-box 2, and coiled-coil
            domains of tripartite motif 5alpha (TRIM5alpha) by heterologous
            TRIM domains
  JOURNAL   J Virol 80 (13), 6198-6206 (2006)
   PUBMED   16775307
  REMARK    GeneRIF: heterologous RING, B-box 2, and CC domains from related
            TRIM proteins can functionally substitute for TRIM5alpha(rh)
            domains.
REFERENCE   8  (residues 1 to 516)
  AUTHORS   Woo,J.S., Imm,J.H., Min,C.K., Kim,K.J., Cha,S.S. and Oh,B.H.
  TITLE     Structural and functional insights into the B30.2/SPRY domain
  JOURNAL   EMBO J 25 (6), 1353-1363 (2006)
   PUBMED   16498413
REFERENCE   9  (residues 1 to 516)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   10 (residues 1 to 516)
  AUTHORS   Orimo,A., Tominaga,N., Yoshimura,K., Yamauchi,Y., Nomura,M.,
            Sato,M., Nogi,Y., Suzuki,M., Suzuki,H., Ikeda,K., Inoue,S. and
            Muramatsu,M.
  TITLE     Molecular cloning of ring finger protein 21
            (RNF21)/interferon-responsive finger protein (ifp1), which
            possesses two RING-B box-coiled coil domains in tandem
  JOURNAL   Genomics 69 (1), 143-149 (2000)
   PUBMED   11013086
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290172.1, BC047564.1,
            AK316178.1 and AF220030.1.
            
            Summary: The protein encoded by this gene is a member of the
            tripartite motif (TRIM) family. The TRIM motif includes three
            zinc-binding domains, a RING, B-box type 1 and B-box type 2 domain,
            and a coiled-coil region. The protein localizes to the nucleus, but
            its specific function has not been identified. This gene is mapped
            to chromosome 11p15, where it resides within a TRIM gene cluster.
            Alternative splicing results in multiple transcript variants. A
            read-through transcript from this gene into the downstream TRIM34
            gene has also been observed, which results in a fusion product from
            these neighboring family members. [provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047564.1, SRR1803611.47676.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380097.8/ ENSP00000369440.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..516
                     /product="tripartite motif-containing protein 6 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="RING finger protein 89; RING-type E3 ubiquitin
                     transferase TRIM6"
                     /calculated_mol_wt=59222
     Region          35..107
                     /region_name="RING-HC_TRIM5-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and
                     similar proteins; cd16591"
                     /db_xref="CDD:438253"
     Site            order(44..45,47..48,85..86,88)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438253"
     Region          124..162
                     /region_name="Bbox2_TRIM5-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34,
                     TRIM38 and similar proteins; cd19761"
                     /db_xref="CDD:380819"
     Region          159..>270
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          327..514
                     /region_name="SPRY_PRY_TRIM6"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     6 (TRIM6), also known as RING finger protein 89 (RNF89);
                     cd15823"
                     /db_xref="CDD:293995"
     CDS             1..516
                     /gene="TRIM6"
                     /gene_synonym="RNF89"
                     /coded_by="NM_001003818.3:262..1812"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31389.1"
                     /db_xref="GeneID:117854"
                     /db_xref="HGNC:HGNC:16277"
                     /db_xref="MIM:607564"
ORIGIN      
        1 mcgserilqa gnileirvgq agarrvatmt spvlvdiree vtcpiclell teplsidcgh
       61 sfcqacitpn gresvigqeg erscpvcqts yqpgnlrpnr hlanivrrlr evvlgpgkql
      121 kavlcadhge klqlfcqedg kvicwlcers qehrghhtfl veevaqeyqe kfqeslkklk
      181 neeqeaeklt afirekktsw knqmepercr iqtefnqlrn ildrveqrel kkleqeekkg
      241 lriieeaend lvhqtqslre lisdlerrcq gstmellqdv sdvtersefw tlrkpealpt
      301 klrsmfrapd lkrmlrvcre ltdvqsywvd vtlnphtanl nlvlaknrrq vrfvgakvsg
      361 psclekhydc svlgsqhfss gkhywevdva kktawilgvc snslgptfsf nhfaqnhsay
      421 sryqpqsgyw viglqhnhey rayedsspsl llsmtvpprr vgvfldyeag tvsfynvtnh
      481 gfpiytfsky yfpttlcpyf npcncvipmt lrrpss
//
LOCUS       NP_001352711             248 aa            linear   PRI 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform 19 [Homo sapiens].
ACCESSION   NP_001352711
VERSION     NP_001352711.1
DBSOURCE    REFSEQ: accession NM_001365782.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Man,Y., Yi,C., Fan,M., Yang,T., Liu,P., Liu,S. and Wang,G.
  TITLE     Identification of a novel missense mutation in the TPM1 gene via
            exome sequencing in a Chinese family with dilated cardiomyopathy: A
            case report and literature review
  JOURNAL   Medicine (Baltimore) 101 (2), e28551 (2022)
   PUBMED   35029218
  REMARK    GeneRIF: Identification of a novel missense mutation in the TPM1
            gene via exome sequencing in a Chinese family with dilated
            cardiomyopathy: A case report and literature review.
            Review article
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.181617.1,
                                           SRR1803612.245481.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..248
                     /product="tropomyosin alpha-1 chain isoform 19"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=28467
     Region          12..246
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..248
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001365782.1:88..834"
                     /note="isoform 19 is encoded by transcript variant 19"
                     /db_xref="CCDS:CCDS92012.1"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeeragt lqreldherk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egkcaeleee lktvtnnlks leaqaekysq
      181 kedryeeeik vlsdklkeae traefaersv tkleksiddl edelyaqklk ykaiseeldh
      241 alndmtsm
//
LOCUS       NP_057235               1235 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein kinase TAO2 isoform 1 [Homo sapiens].
ACCESSION   NP_057235
VERSION     NP_057235.2
DBSOURCE    REFSEQ: accession NM_016151.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1235)
  AUTHORS   Ma,X., Mandausch,F.J., Wu,Y., Sahoo,V.K., Ma,W., Leoni,G.,
            Hostiuc,M., Wintgens,J.P., Qiu,J., Kannaiyan,N., Rossner,M.J. and
            Wehr,M.C.
  TITLE     Comprehensive split TEV based protein-protein interaction screening
            reveals TAOK2 as a key modulator of Hippo signalling to limit
            growth
  JOURNAL   Cell Signal 113, 110917 (2024)
   PUBMED   37813295
  REMARK    GeneRIF: Comprehensive split TEV based protein-protein interaction
            screening reveals TAOK2 as a key modulator of Hippo signalling to
            limit growth.
REFERENCE   2  (residues 1 to 1235)
  AUTHORS   Yang,Q., Li,Y., Wang,Y., Qiao,X., Liu,T., Wang,H. and Shen,H.
  TITLE     The circRNA circSIAE Inhibits Replication of Coxsackie Virus B3 by
            Targeting miR-331-3p and Thousand and One Amino-Acid Kinase 2
  JOURNAL   Front Cell Infect Microbiol 11, 779919 (2022)
   PUBMED   35141166
  REMARK    GeneRIF: The circRNA circSIAE Inhibits Replication of Coxsackie
            Virus B3 by Targeting miR-331-3p and Thousand and One Amino-Acid
            Kinase 2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1235)
  AUTHORS   Nourbakhsh,K., Ferreccio,A.A., Bernard,M.J. and Yadav,S.
  TITLE     TAOK2 is an ER-localized kinase that catalyzes the dynamic
            tethering of ER to microtubules
  JOURNAL   Dev Cell 56 (24), 3321-3333 (2021)
   PUBMED   34879262
  REMARK    GeneRIF: TAOK2 is an ER-localized kinase that catalyzes the dynamic
            tethering of ER to microtubules.
REFERENCE   4  (residues 1 to 1235)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1235)
  AUTHORS   Koo,C.Y., Giacomini,C., Reyes-Corral,M., Olmos,Y., Tavares,I.A.,
            Marson,C.M., Linardopoulos,S., Tutt,A.N. and Morris,J.D.H.
  TITLE     Targeting TAO Kinases Using a New Inhibitor Compound Delays Mitosis
            and Induces Mitotic Cell Death in Centrosome Amplified Breast
            Cancer Cells
  JOURNAL   Mol Cancer Ther 16 (11), 2410-2421 (2017)
   PUBMED   28830982
  REMARK    GeneRIF: we characterize a compound that inhibits TAOK1 and TAOK2
            activity with IC50 values of 11 to 15 nmol/L, is ATP-competitive,
            and targets these kinases selectively. TAOK inhibition or depletion
            in centrosome-amplified SKBR3 or BT549 breast cancer cell models
            increases the mitotic population, the percentages of mitotic cells
            displaying amplified centrosomes and multipolar spindles, induces
            cell death, and inhibits cell growt
REFERENCE   6  (residues 1 to 1235)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   7  (residues 1 to 1235)
  AUTHORS   Chen,Z. and Cobb,M.H.
  TITLE     Regulation of stress-responsive mitogen-activated protein (MAP)
            kinase pathways by TAO2
  JOURNAL   J Biol Chem 276 (19), 16070-16075 (2001)
   PUBMED   11279118
REFERENCE   8  (residues 1 to 1235)
  AUTHORS   Moore,T.M., Garg,R., Johnson,C., Coptcoat,M.J., Ridley,A.J. and
            Morris,J.D.
  TITLE     PSK, a novel STE20-like kinase derived from prostatic carcinoma
            that activates the c-Jun N-terminal kinase mitogen-activated
            protein kinase pathway and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 275 (6), 4311-4322 (2000)
   PUBMED   10660600
REFERENCE   9  (residues 1 to 1235)
  AUTHORS   Chen,Z., Hutchison,M. and Cobb,M.H.
  TITLE     Isolation of the protein kinase TAO2 and identification of its
            mitogen-activated protein kinase/extracellular signal-regulated
            kinase kinase binding domain
  JOURNAL   J Biol Chem 274 (40), 28803-28807 (1999)
   PUBMED   10497253
REFERENCE   10 (residues 1 to 1235)
  AUTHORS   Hutchison,M., Berman,K.S. and Cobb,M.H.
  TITLE     Isolation of TAO1, a protein kinase that activates MEKs in
            stress-activated protein kinase cascades
  JOURNAL   J Biol Chem 273 (44), 28625-28632 (1998)
   PUBMED   9786855
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP233788.1, BC136653.1 and
            BC151221.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 17, 2004 this sequence version replaced NP_057235.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1, also known as PSK1-alpha).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF061943.1, BC136653.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308893.9/ ENSP00000310094.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..1235
                     /product="serine/threonine-protein kinase TAO2 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="prostate derived STE20-like kinase PSK;
                     serine/threonine-protein kinase TAO2; PSK-1; hKFC-C;
                     kinase from chicken homolog C; prostate-derived STE20-like
                     kinase 1; prostate-derived sterile 20-like kinase 1;
                     thousand and one amino acid protein kinase 2"
                     /calculated_mol_wt=138121
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Region          12..319
                     /region_name="STKc_TAO2"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Thousand-and-One Amino acids 2; cd06634"
                     /db_xref="CDD:270804"
     Site            order(34..38,42,55,57,89,105..108,110..111,114,155..156,
                     158,169,314)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270804"
     Site            order(34..38,42,55,57,89,105..108,110..111,114,151,
                     153..156,158,168..169,172,182..185,187,217,226)
                     /site_type="active"
                     /db_xref="CDD:270804"
     Site            order(37..38,151,153..155,172,182..185,187,217,226)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270804"
     Site            168..187
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270804"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17158878,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q9UL54.2)"
     Region          318..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UL54.2)"
     Region          <467..>803
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZQ29; propagated from
                     UniProtKB/Swiss-Prot (Q9UL54.2)"
     Region          732..777
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            777
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9UL54.2)"
     Region          804..835
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UL54.2)"
     Region          891..939
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            965..985
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            987..1007
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            1011
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            1012..1032
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            1031
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            1043..1063
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Site            1166..1186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     Region          1198..1235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL54.2)"
     CDS             1..1235
                     /gene="TAOK2"
                     /gene_synonym="MAP3K17; PSK; PSK1; PSK1-BETA; TAO1; TAO2;
                     Tao2beta"
                     /coded_by="NM_016151.4:817..4524"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10663.1"
                     /db_xref="GeneID:9344"
                     /db_xref="HGNC:HGNC:16835"
                     /db_xref="MIM:613199"
ORIGIN      
        1 mpaggragsl kdpdvaelff kddpeklfsd lreighgsfg avyfardvrn sevvaikkms
       61 ysgkqsnekw qdiikevrfl qklrhpntiq yrgcylreht awlvmeyclg sasdllevhk
      121 kplqeveiaa vthgalqgla ylhshnmihr dvkagnills epglvklgdf gsasimapan
      181 sfvgtpywma pevilamdeg qydgkvdvws lgitcielae rkpplfnmna msalyhiaqn
      241 espvlqsghw seyfrnfvds clqkipqdrp tsevllkhrf vlrerpptvi mdliqrtkda
      301 vreldnlqyr kmkkilfqea pngpgaeape eeeeaepymh ragtltsles shsvpsmsis
      361 assqsssvns ladasdneee eeeeeeeeee eegpearema mmqegehtvt shssiihrlp
      421 gsdnlyddpy qpeitpsplq ppaapaptst tssarrrayc rnrdhfatir taslvsrqiq
      481 eheqdsalre qlsgykrmrr qhqkqllale srlrgereeh sarlqrelea qragfgaeae
      541 klarrhqaig ekearaaqae erkfqqhilg qqkkelaall eaqkrtyklr keqlkeelqe
      601 npstpkreka ewllrqkeql qqcqaeeeag llrrqrqyfe lqcrqykrkm llarhsldqd
      661 llredlnkkq tqkdlecall lrqheatrel elrqlqavqr traeltrlqh qtelgnqley
      721 nkrreqelrq khaaqvrqqp kslkvragqr ppglplpipg algppntgtp ieqqpcspgq
      781 eavldqrmlg eeeeavgerr ilgkegatle pkqqrilgee sgapspspqk hgslvdeevw
      841 glpeeieelr vpslvpqers ivgqeeagtw slwgkedesl ldeefelgwv qgpaltpvpe
      901 eeeeeeegap igtprdpgdg cpspdippep ppthlrpcpa sqlpgllshg llaglsfavg
      961 sssgllplll llllpllaaq gggglqaall alevglvglg asylllctal hlpsslflll
     1021 aqgtalgavl glswrrglmg vplglgaawl lawpglalpl vamaaggrwv rqqgprvrrg
     1081 isrlwlrvll rlspmafral qgcgavgdrg lfalypktnk dgfrsrlpvp gprrrnprtt
     1141 qhplallarv wvlckgwnwr larasqglas hlppwaihtl aswgllrger ptriprllpr
     1201 sqrqlgppas rqplpgtlag rrsrtrqsra lppwr
//
LOCUS       NP_055716                432 aa            linear   PRI 27-APR-2025
DEFINITION  RING finger protein 44 [Homo sapiens].
ACCESSION   NP_055716
VERSION     NP_055716.1
DBSOURCE    REFSEQ: accession NM_014901.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Stolk,L., Perry,J.R., Chasman,D.I., He,C., Mangino,M., Sulem,P.,
            Barbalic,M., Broer,L., Byrne,E.M., Ernst,F., Esko,T.,
            Franceschini,N., Gudbjartsson,D.F., Hottenga,J.J., Kraft,P.,
            McArdle,P.F., Porcu,E., Shin,S.Y., Smith,A.V., van Wingerden,S.,
            Zhai,G., Zhuang,W.V., Albrecht,E., Alizadeh,B.Z., Aspelund,T.,
            Bandinelli,S., Lauc,L.B., Beckmann,J.S., Boban,M., Boerwinkle,E.,
            Broekmans,F.J., Burri,A., Campbell,H., Chanock,S.J., Chen,C.,
            Cornelis,M.C., Corre,T., Coviello,A.D., d'Adamo,P., Davies,G., de
            Faire,U., de Geus,E.J., Deary,I.J., Dedoussis,G.V., Deloukas,P.,
            Ebrahim,S., Eiriksdottir,G., Emilsson,V., Eriksson,J.G.,
            Fauser,B.C., Ferreli,L., Ferrucci,L., Fischer,K., Folsom,A.R.,
            Garcia,M.E., Gasparini,P., Gieger,C., Glazer,N., Grobbee,D.E.,
            Hall,P., Haller,T., Hankinson,S.E., Hass,M., Hayward,C.,
            Heath,A.C., Hofman,A., Ingelsson,E., Janssens,A.C., Johnson,A.D.,
            Karasik,D., Kardia,S.L., Keyzer,J., Kiel,D.P., Kolcic,I.,
            Kutalik,Z., Lahti,J., Lai,S., Laisk,T., Laven,J.S., Lawlor,D.A.,
            Liu,J., Lopez,L.M., Louwers,Y.V., Magnusson,P.K., Marongiu,M.,
            Martin,N.G., Klaric,I.M., Masciullo,C., McKnight,B., Medland,S.E.,
            Melzer,D., Mooser,V., Navarro,P., Newman,A.B., Nyholt,D.R.,
            Onland-Moret,N.C., Palotie,A., Pare,G., Parker,A.N., Pedersen,N.L.,
            Peeters,P.H., Pistis,G., Plump,A.S., Polasek,O., Pop,V.J.,
            Psaty,B.M., Raikkonen,K., Rehnberg,E., Rotter,J.I., Rudan,I.,
            Sala,C., Salumets,A., Scuteri,A., Singleton,A., Smith,J.A.,
            Snieder,H., Soranzo,N., Stacey,S.N., Starr,J.M., Stathopoulou,M.G.,
            Stirrups,K., Stolk,R.P., Styrkarsdottir,U., Sun,Y.V., Tenesa,A.,
            Thorand,B., Toniolo,D., Tryggvadottir,L., Tsui,K., Ulivi,S., van
            Dam,R.M., van der Schouw,Y.T., van Gils,C.H., van Nierop,P.,
            Vink,J.M., Visscher,P.M., Voorhuis,M., Waeber,G., Wallaschofski,H.,
            Wichmann,H.E., Widen,E., Wijnands-van Gent,C.J., Willemsen,G.,
            Wilson,J.F., Wolffenbuttel,B.H., Wright,A.F.,
            Yerges-Armstrong,L.M., Zemunik,T., Zgaga,L., Zillikens,M.C.,
            Zygmunt,M., Arnold,A.M., Boomsma,D.I., Buring,J.E., Crisponi,L.,
            Demerath,E.W., Gudnason,V., Harris,T.B., Hu,F.B., Hunter,D.J.,
            Launer,L.J., Metspalu,A., Montgomery,G.W., Oostra,B.A.,
            Ridker,P.M., Sanna,S., Schlessinger,D., Spector,T.D.,
            Stefansson,K., Streeten,E.A., Thorsteinsdottir,U., Uda,M.,
            Uitterlinden,A.G., van Duijn,C.M., Volzke,H., Murray,A.,
            Murabito,J.M., Visser,J.A. and Lunetta,K.L.
  CONSRTM   LifeLines Cohort Study
  TITLE     Meta-analyses identify 13 loci associated with age at menopause and
            highlight DNA repair and immune pathways
  JOURNAL   Nat Genet 44 (3), 260-268 (2012)
   PUBMED   22267201
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Auffray,C., Behar,G., Bois,F., Bouchier,C., Da Silva,C.,
            Devignes,M.D., Duprat,S., Houlgatte,R., Jumeau,M.N., Lamy,B. et al.
  TITLE     [IMAGE: molecular integration of the analysis of the human genome
            and its expression]
  JOURNAL   C R Acad Sci III 318 (2), 263-272 (1995)
   PUBMED   7757816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC063297.1 and BC039833.1.
            
            Summary: The protein encoded by this gene contains a RING finger, a
            motif present in a variety of functionally distinct proteins and
            known to be involved in protein-protein and protein-DNA
            interactions. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063297.1, AB029023.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274811.9/ ENSP00000274811.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..432
                     /product="RING finger protein 44"
                     /calculated_mol_wt=47597
     Region          1..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L0R7.1)"
     Region          371..432
                     /region_name="RING-H2_RNF44"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 44 (RNF44) and similar proteins; cd16680"
                     /db_xref="CDD:438342"
     CDS             1..432
                     /gene="RNF44"
                     /coded_by="NM_014901.5:508..1806"
                     /db_xref="CCDS:CCDS4404.1"
                     /db_xref="GeneID:22838"
                     /db_xref="HGNC:HGNC:19180"
                     /db_xref="MIM:619283"
ORIGIN      
        1 mrpwalavtr wppsapvgqr rfsagpgstp gqlwgspgle gplasppard erlpsqqpps
       61 rpphlpveer rasapaggsp rmlhpatqqs pfmvdlheqv hqgpvplsyt vttvttqgfp
      121 lptgqhipgc saqqlpacsv mfsgqhyplc clpppliqac tmqqlpvpyq ayphlissdh
      181 yilhppppap ppqpthmapl gqfvslqtqh prmplqrldn dvdlrgdqps lgsftystsa
      241 pgpalspsvp lhylphdplh qelsfgvpys hmmprrlstq ryrlqqplpp pppppppppy
      301 ypsflpyfls mlpmsptamg ptisldldvd dvemenyeal lnlaerlgda kprgltkadi
      361 eqlpsyrfnp dshqseqtlc vvcfsdfear qllrvlpcnh efhtkcvdkw lkanrtcpic
      421 radasevpre ae
//
LOCUS       NP_116237                269 aa            linear   PRI 27-APR-2025
DEFINITION  RBPJ-interacting and tubulin-associated protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_116237
VERSION     NP_116237.1
DBSOURCE    REFSEQ: accession NM_032848.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Tang,H., Li,X., Jiang,L., Liu,Z., Chen,L., Chen,J., Deng,M.,
            Zhou,F., Zheng,X. and Liu,Z.
  TITLE     RITA1 drives the growth of bladder cancer cells by recruiting
            TRIM25 to facilitate the proteasomal degradation of RBPJ
  JOURNAL   Cancer Sci 113 (9), 3071-3084 (2022)
   PUBMED   35701858
  REMARK    GeneRIF: RITA1 drives the growth of bladder cancer cells by
            recruiting TRIM25 to facilitate the proteasomal degradation of
            RBPJ.
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Wildner,J.M., Friemel,A., Jennewein,L., Roth,S., Ritter,A.,
            Schuttler,C., Chen,Q., Louwen,F., Yuan,J. and Kreis,N.N.
  TITLE     RITA Is Expressed in Trophoblastic Cells and Is Involved in
            Differentiation Processes of the Placenta
  JOURNAL   Cells 8 (12), 1484 (2019)
   PUBMED   31766533
  REMARK    GeneRIF: RITA Is Expressed in Trophoblastic Cells and Is Involved
            in Differentiation Processes of the Placenta.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Hoock,S.C., Ritter,A., Steinhauser,K., Roth,S., Behrends,C.,
            Oswald,F., Solbach,C., Louwen,F., Kreis,N.N. and Yuan,J.
  TITLE     RITA modulates cell migration and invasion by affecting focal
            adhesion dynamics
  JOURNAL   Mol Oncol 13 (10), 2121-2141 (2019)
   PUBMED   31353815
  REMARK    GeneRIF: This study identifies RITA as a novel crucial player in
            cell migration and invasion by affecting the turnover of focal
            adhesions through its interference with the dynamics of actin
            filaments and microtubules. Its deregulation may contribute to
            malignant progression.
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Brockmann,B., Mastel,H., Oswald,F. and Maier,D.
  TITLE     Analysis of the interaction between human RITA and Drosophila
            Suppressor of Hairless
  JOURNAL   Hereditas 151 (6), 209-219 (2014)
   PUBMED   25588307
  REMARK    GeneRIF: human RITA, binding to Drosophila Su(H) and tubulin,
            cannot influence the Notch signalling pathway in the fly
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Wang,H., Yang,Z., Liu,C., Huang,S., Wang,H., Chen,Y. and Chen,G.
  TITLE     RBP-J-interacting and tubulin-associated protein induces apoptosis
            and cell cycle arrest in human hepatocellular carcinoma by
            activating the p53-Fbxw7 pathway
  JOURNAL   Biochem Biophys Res Commun 454 (1), 71-77 (2014)
   PUBMED   25445601
  REMARK    GeneRIF: RITA overexpression increased expression of p53 and Fbxw7
            and downregulated expression of cyclin D1, cyclin E, CDK2, Hes-1
            and NF-kappaB p65. These changes led to growth inhibition and
            induced G0/G1 cell cycle arrest and apoptosis in SMMC7721 and HepG2
            cells.
REFERENCE   8  (residues 1 to 269)
  AUTHORS   Wang,H., Chen,G., Wang,H. and Liu,C.
  TITLE     RITA inhibits growth of human hepatocellular carcinoma through
            induction of apoptosis
  JOURNAL   Oncol Res 20 (10), 437-445 (2013)
   PUBMED   24308154
  REMARK    GeneRIF: RITA might suppress tumor growth and induce apoptosis in
            hepatocellular carcinoma.
REFERENCE   9  (residues 1 to 269)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   10 (residues 1 to 269)
  AUTHORS   Wacker,S.A., Alvarado,C., von Wichert,G., Knippschild,U.,
            Wiedenmann,J., Clauss,K., Nienhaus,G.U., Hameister,H., Baumann,B.,
            Borggrefe,T., Knochel,W. and Oswald,F.
  TITLE     RITA, a novel modulator of Notch signalling, acts via nuclear
            export of RBP-J
  JOURNAL   EMBO J 30 (1), 43-56 (2011)
   PUBMED   21102556
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA207985.1, AK027733.1 and AA594422.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the shorter isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.684349.1,
                                           SRR3476690.1160026.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000548278.2/ ENSP00000449841.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.13"
     Protein         1..269
                     /product="RBPJ-interacting and tubulin-associated protein
                     1 isoform 1"
                     /note="RBPJ-interacting and tubulin-associated protein 1"
                     /calculated_mol_wt=28488
     Region          2..269
                     /region_name="RITA"
                     /note="RBPJ-interacting and tubulin associated protein;
                     pfam17066"
                     /db_xref="CDD:465342"
     Region          5..17
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K30.1)"
     Region          66..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K30.1)"
     Region          92..108
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K30.1)"
     Region          128..156
                     /region_name="Interaction with RBPJ/RBPSUH.
                     /evidence=ECO:0000269|PubMed:21102556"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K30.1)"
     Region          141..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K30.1)"
     Region          156..269
                     /region_name="Interaction with tubulin"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K30.1)"
     CDS             1..269
                     /gene="RITA1"
                     /gene_synonym="C12orf52; RITA"
                     /coded_by="NM_032848.3:498..1307"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9166.1"
                     /db_xref="GeneID:84934"
                     /db_xref="HGNC:HGNC:25925"
                     /db_xref="MIM:620696"
ORIGIN      
        1 mktpvelavs gmqtlglqhr crggyrvkar tsyvdetlfg spagtrptpp dfdppwveka
       61 nrtrgvgkea skalgakgsc ettpsrgstp tltprkknky rpishtpsyc deslfgsrse
      121 gasfgaprma kgdaaklral lwtppptprg shsprpreap lraihpagps ktepgpaads
      181 qklsmgglhs srplkrglsh slthlnvpst ghpatsapht ngpqdlrpst sgvtfrsplv
      241 tsrarsvsis vpstprrgga tqkpkppwk
//
LOCUS       NP_001353510             886 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 15 [Homo
            sapiens].
ACCESSION   NP_001353510 XP_016855510
VERSION     NP_001353510.1
DBSOURCE    REFSEQ: accession NM_001366581.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 886)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 886)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 886)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 886)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 886)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 886)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 886)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 886)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 886)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 886)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855510.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.152893.1,
                                           SRR1803612.144788.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..886
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..886
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 15"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=99947
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <121..209
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <588..>722
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..886
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366581.1:26..2686"
                     /note="isoform 15 is encoded by transcript variant 20"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrtksrsp
      181 spapekkekt pelpepsvkv kepsvqeats tsdilkvpkp epipepkeps peknskkeke
      241 kektrprsrs rsksrsrtrs rspshtrprr rhrsrsrsys prrrpsprrr psprrrtppr
      301 rmpppprhrr srspvrrrrr ssaslsgsss sssssrsrsp pkkppkrtss pprktrrlsp
      361 saspprrrhr psppatpppk trhsptpqqs nrtrksrvsv spgrtsvtkh kgtekresps
      421 papkprkvel seseedkggk maaadsvqqr rqyrrqnqqs ssdsgsssss ederpkrshv
      481 kngevgrrrr hspsrsasps prkrqketsp rmqmgkrwqs pvtksgrrrr spsppptrrr
      541 rspspapppr rrrtptpppr rrtpsppprr rspsprrysp piqrryspsp ppkrrtaspp
      601 pppkrrasps pppkrrvshs pppkqrsspv tkrrspslss khrkgsspsr strearspqp
      661 nkrhspsprp rapqtssspp pvrrgasssp qrrqspspst rpirrvsrtp epkkikkaas
      721 pspqsvrrvs ssrsvsgspe paakkppapp spvqsqspst nwspavpvkk aksptpspsp
      781 prnsdqeggg kkkkkkkdkk hkkdkkhkkh kkhkkekava aaaaaavtpa aiaaatttla
      841 qeepvaapep kketeseaed nlddlekhlr ekalrsmrka qvspqs
//
LOCUS       NP_001353137             871 aa            linear   PRI 27-APR-2025
DEFINITION  disks large homolog 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001353137 XP_016861307
VERSION     NP_001353137.1
DBSOURCE    REFSEQ: accession NM_001366208.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Veljacic Viskovic,D., Lozic,M., Vukoja,M., Soljic,V., Vukojevic,K.,
            Glavina Durdov,M., Filipovic,N. and Lozic,B.
  TITLE     Spatio-Temporal Expression Pattern of CAKUT Candidate Genes DLG1
            and KIF12 during Human Kidney Development
  JOURNAL   Biomolecules 13 (2), 340 (2023)
   PUBMED   36830709
  REMARK    GeneRIF: Spatio-Temporal Expression Pattern of CAKUT Candidate
            Genes DLG1 and KIF12 during Human Kidney Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 871)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861307.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.21818.1,
                                           SRR14038195.797519.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 21595829
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..871
                     /product="disks large homolog 1 isoform 8"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=96945
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          680..858
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..871
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366208.1:227..2842"
                     /note="isoform 8 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS93452.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt snasdsessy
      661 rgqeeyvlsy epvnqqevny trpviilgpm kdrinddlis efpdkfgscv phttrpkrdy
      721 evdgrdyhfv tsreqmekdi qehkfieagq ynnhlygtsv qsvrevaekg khcildvsgn
      781 aikrlqiaql ypisifikpk smenimemnk rlteeqarkt feramkleqe ftehftaivq
      841 gdtlediynq vkqiieeqsg syiwvpakek l
//
LOCUS       NP_001355194             247 aa            linear   PRI 27-APR-2025
DEFINITION  myosin-IIIa isoform 2 [Homo sapiens].
ACCESSION   NP_001355194
VERSION     NP_001355194.1
DBSOURCE    REFSEQ: accession NM_001368265.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Cirilo,J.A. Jr., Liao,X., Perrin,B.J. and Yengo,C.M.
  TITLE     The dynamics of actin protrusions can be controlled by
            tip-localized myosin motors
  JOURNAL   J Biol Chem 300 (1), 105516 (2024)
   PUBMED   38042485
  REMARK    GeneRIF: The dynamics of actin protrusions can be controlled by
            tip-localized myosin motors.
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Gunther,L.K., Cirilo,J.A. Jr., Desetty,R. and Yengo,C.M.
  TITLE     Deafness mutation in the MYO3A motor domain impairs actin
            protrusion elongation mechanism
  JOURNAL   Mol Biol Cell 33 (1), ar5 (2022)
   PUBMED   34788109
  REMARK    GeneRIF: Deafness mutation in the MYO3A motor domain impairs actin
            protrusion elongation mechanism.
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Bueno,A.S., Nunes,K., Dias,A.M.M., Alves,L.U., Mendes,B.C.A.,
            Sampaio-Silva,J., Smits,J., Yntema,H.G., Meyer,D., Lezirovitz,K.
            and Mingroni-Netto,R.C.
  TITLE     Frequency and origin of the c.2090T>G p.(Leu697Trp) MYO3A variant
            associated with autosomal dominant hearing loss
  JOURNAL   Eur J Hum Genet 30 (1), 13-21 (2022)
   PUBMED   33953343
  REMARK    GeneRIF: Frequency and origin of the c.2090T>G p.(Leu697Trp) MYO3A
            variant associated with autosomal dominant hearing loss.
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Souissi,A., Abdelmalek Driss,D., Chakchouk,I., Ben Said,M., Ben
            Ayed,I., Mosrati,M.A., Elloumi,I., Tlili,A., Aifa,S. and
            Masmoudi,S.
  TITLE     Molecular insights into MYO3A kinase domain variants explain
            variability in both severity and progression of DFNB30 hearing
            impairment
  JOURNAL   J Biomol Struct Dyn 40 (21), 10940-10951 (2022)
   PUBMED   34423747
  REMARK    GeneRIF: Molecular insights into MYO3A kinase domain variants
            explain variability in both severity and progression of DFNB30
            hearing impairment.
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Wonkam,A., Manyisa,N., Bope,C.D., Dandara,C. and Chimusa,E.R.
  TITLE     Whole exome sequencing reveals pathogenic variants in MYO3A, MYO15A
            and COL9A3 and differential frequencies in ancestral alleles in
            hearing impairment genes among individuals from Cameroon
  JOURNAL   Hum Mol Genet 29 (23), 3729-3743 (2021)
   PUBMED   33078831
  REMARK    GeneRIF: Whole exome sequencing reveals pathogenic variants in
            MYO3A, MYO15A and COL9A3 and differential frequencies in ancestral
            alleles in hearing impairment genes among individuals from
            Cameroon.
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Komaba,S., Inoue,A., Maruta,S., Hosoya,H. and Ikebe,M.
  TITLE     Determination of human myosin III as a motor protein having a
            protein kinase activity
  JOURNAL   J Biol Chem 278 (24), 21352-21360 (2003)
   PUBMED   12672820
  REMARK    GeneRIF: class III myosin is an actin-based motor protein having a
            protein kinase activity
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Walsh,T., Walsh,V., Vreugde,S., Hertzano,R., Shahin,H., Haika,S.,
            Lee,M.K., Kanaan,M., King,M.C. and Avraham,K.B.
  TITLE     From flies' eyes to our ears: mutations in a human class III myosin
            cause progressive nonsyndromic hearing loss DFNB30
  JOURNAL   Proc Natl Acad Sci U S A 99 (11), 7518-7523 (2002)
   PUBMED   12032315
  REMARK    GeneRIF: mutation in humans causes progressive nonsyndromic hearing
            loss DFNB30
REFERENCE   8  (residues 1 to 247)
  AUTHORS   Dose,A.C. and Burnside,B.
  TITLE     Cloning and chromosomal localization of a human class III myosin
  JOURNAL   Genomics 67 (3), 333-342 (2000)
   PUBMED   10936054
REFERENCE   9  (residues 1 to 247)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 247)
  AUTHORS   Wallace,H. and Maden,M.
  TITLE     Irradiation inhibits the regeneration of aneurogenic limbs
  JOURNAL   J Exp Zool 195 (3), 353-358 (1976)
   PUBMED   1262820
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL358612.9 and BC036079.1.
            
            Summary: The protein encoded by this gene belongs to the myosin
            superfamily. Myosins are actin-dependent motor proteins and are
            categorized into conventional myosins (class II) and unconventional
            myosins (classes I and III through XV) based on their variable
            C-terminal cargo-binding domains. Class III myosins, such as this
            one, have a kinase domain N-terminal to the conserved N-terminal
            motor domains and are expressed in photoreceptors. The protein
            encoded by this gene plays an important role in hearing in humans.
            Three different recessive, loss of function mutations in the
            encoded protein have been shown to cause nonsyndromic progressive
            hearing loss. Expression of this gene is highly restricted, with
            the strongest expression in retina and cochlea. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036079.1, SRR18074967.3723321.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..247
                     /product="myosin-IIIa isoform 2"
                     /EC_number="2.7.11.1"
                     /note="myosin-IIIa; epididymis secretory sperm binding
                     protein"
                     /calculated_mol_wt=27547
     Region          2..245
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(27..30,33,35,48,50,79,100..103,150,154..155,157,
                     167..168)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..247
                     /gene="MYO3A"
                     /gene_synonym="DFNA90; DFNB30"
                     /coded_by="NM_001368265.1:205..948"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS91223.1"
                     /db_xref="GeneID:53904"
                     /db_xref="HGNC:HGNC:7601"
                     /db_xref="MIM:606808"
ORIGIN      
        1 mfpligktii fdnfpdpsdt weitetigkg tygkvfkvln kkngqkaavk ildpihdide
       61 eieaeynilk alsdhpnvvr fygiyfkkdk vngdklwlvl elcsggsvtd lvkgflkrge
      121 rmsepliayi lhealmglqh lhnnktihrd vkgnnilltt eggvklvdfg vsaqltstrh
      181 rrntsvgtpf wmapeviace qqldttydar cdtwslgita ielgdgdppl adlhpmralf
      241 kiprsdd
//
LOCUS       NP_071753                330 aa            linear   PRI 27-APR-2025
DEFINITION  potassium channel subfamily K member 15 [Homo sapiens].
ACCESSION   NP_071753
VERSION     NP_071753.2
DBSOURCE    REFSEQ: accession NM_022358.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Rinne,S., Schick,F., Vowinkel,K., Schutte,S., Krasel,C.,
            Kauferstein,S., Schafer,M.K., Kiper,A.K., Muller,T. and Decher,N.
  TITLE     Potassium channel TASK-5 forms functional heterodimers with TASK-1
            and TASK-3 to break its silence
  JOURNAL   Nat Commun 15 (1), 7548 (2024)
   PUBMED   39215006
  REMARK    GeneRIF: Potassium channel TASK-5 forms functional heterodimers
            with TASK-1 and TASK-3 to break its silence.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Goldstein,S.A., Bayliss,D.A., Kim,D., Lesage,F., Plant,L.D. and
            Rajan,S.
  TITLE     International Union of Pharmacology. LV. Nomenclature and molecular
            relationships of two-P potassium channels
  JOURNAL   Pharmacol Rev 57 (4), 527-540 (2005)
   PUBMED   16382106
  REMARK    Review article
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Karschin,C., Wischmeyer,E., Preisig-Muller,R., Rajan,S., Derst,C.,
            Grzeschik,K.H., Daut,J. and Karschin,A.
  TITLE     Expression pattern in brain of TASK-1, TASK-3, and a tandem pore
            domain K(+) channel subunit, TASK-5, associated with the central
            auditory nervous system
  JOURNAL   Mol Cell Neurosci 18 (6), 632-648 (2001)
   PUBMED   11749039
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Ashmole,I., Goodwin,P.A. and Stanfield,P.R.
  TITLE     TASK-5, a novel member of the tandem pore K+ channel family
  JOURNAL   Pflugers Arch 442 (6), 828-833 (2001)
   PUBMED   11680614
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Vega-Saenz de Miera,E., Lau,D.H., Zhadina,M., Pountney,D.,
            Coetzee,W.A. and Rudy,B.
  TITLE     KT3.2 and KT3.3, two novel human two-pore K(+) channels closely
            related to TASK-1
  JOURNAL   J Neurophysiol 86 (1), 130-142 (2001)
   PUBMED   11431495
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Kim,D. and Gnatenco,C.
  TITLE     TASK-5, a new member of the tandem-pore K(+) channel family
  JOURNAL   Biochem Biophys Res Commun 284 (4), 923-930 (2001)
   PUBMED   11409881
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF257081.1, AF294351.1 and
            BC082981.1.
            
            On May 19, 2011 this sequence version replaced NP_071753.1.
            
            Summary: This gene encodes one of the members of the superfamily of
            potassium channel proteins containing two pore-forming P domains.
            The product of this gene has not been shown to be a functional
            channel, however, it may require other non-pore-forming proteins
            for activity. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF257081.1, AF294350.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372861.5/ ENSP00000361952.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..330
                     /product="potassium channel subfamily K member 15"
                     /note="potassium channel, subfamily K, member 14; two pore
                     potassium channel KT3.3; two pore K(+) channel KT3.3;
                     TWIK-related acid-sensitive K(+) channel 5; acid-sensitive
                     potassium channel protein TASK-5; potassium channel, two
                     pore domain subfamily K, member 15; TWIK-related
                     acid-sensitive K+ 5"
                     /calculated_mol_wt=36091
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H427.3)"
     Region          <73..132
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H427.3)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H427.3)"
     Region          177..243
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Site            223..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H427.3)"
     Region          256..276
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H427.3)"
     CDS             1..330
                     /gene="KCNK15"
                     /gene_synonym="dJ781B1.1; K2p15.1; KCNK11; KCNK14; KT3.3;
                     TASK-5; TASK5"
                     /coded_by="NM_022358.4:47..1039"
                     /db_xref="CCDS:CCDS13337.1"
                     /db_xref="GeneID:60598"
                     /db_xref="HGNC:HGNC:13814"
                     /db_xref="MIM:607368"
ORIGIN      
        1 mrrpsvraag lvlctlcyll vgaavfdale seaesgrqrl lvqkrgalrr kfgfsaedyr
       61 elerlalqae phragrqwkf pgsfyfaitv ittieyghaa pgtdsgkvfc mfyallgipl
      121 tlvtfqslge rlnavvrrll laakcclglr wtcvstenlv vagllacaat lalgavafsh
      181 fegwtffhay yycfitltti gfgdfvalqs gealqrklpy vafsflyill gltvigafln
      241 lvvlrflvas adwperaart psprppgape srglwlprrp arsvgsasvf chvhklerca
      301 rdnlgfspps spgvvrggqa prlgarwksi
//
LOCUS       NP_001356854             709 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001356854 XP_011528751
VERSION     NP_001356854.1
DBSOURCE    REFSEQ: accession NM_001369925.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 709)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 709)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 709)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 709)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            On Apr 24, 2019 this sequence version replaced XP_011528751.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.141905.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..709
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 5"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=80513
     Region          416..455
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..709
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369925.1:115..2244"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mpalpldqlq ithkdpktgk lrtspalvif detlqkclds ylryvprkfd egvasapevv
       61 dmqkrlhrsv fltflrmsth keskdhfisp safgeilynn flfdipkild lcvlfgkgns
      121 pllqkmigni ftqqpsyysd ldetlptilq vfsnilqhcg lqgdganttp qkleergrlt
      181 psdmpllelk divlylcdtc ttlwafldif placqtfqkh dfcyrlasfy eaaipemesa
      241 ikkrrledsk llgdlwqrls hsrkklmeif hiilnqicll pilesscdni qgfieeflqi
      301 fssllqekrf lrdydalfpv aedisllqqa ssvldetrta yilqavesaw egvdrrkatd
      361 akdpsvieep ngepngvtvt aeavsqassh penseeeecm gaaaavgpam cgveldslis
      421 qvkdllpdlg egfilacley yhydpeqvin nileerlapt lsqldrnldr emkpdptpll
      481 tsrhnvfqnd efdvfsrdsv dlsrvhkgks trkeentrsl lndkravaaq rqryeqysvv
      541 veevplqpge slpyhsvyye deyddtydgn qvgandadsd delisrrpft ipqvlrtkvp
      601 regqeedddd eeddadeeap kvppwqpdhf vqdpavlrek aearrmafla kkgyrhdsst
      661 avagsprghg qsrettqerr kkeankatra nhnrrtmadr krskgmips
//
LOCUS       NP_001070667             624 aa            linear   PRI 27-APR-2025
DEFINITION  splicing regulatory glutamine/lysine-rich protein 1 isoform a [Homo
            sapiens].
ACCESSION   NP_001070667
VERSION     NP_001070667.1
DBSOURCE    REFSEQ: accession NM_001077199.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Chang,C., Rajasekaran,M., Qiao,Y., Dong,H., Wang,Y., Xia,H.,
            Deivasigamani,A., Wu,M., Sekar,K., Gao,H., Sun,M., Niu,Y., Li,Q.,
            Tao,L., Yan,Z., Wang,M., Chen,S., Zhao,S., Chen,D., Li,L., Yang,F.,
            Gao,H., Chen,B., Su,L., Xu,L., Chen,Y., Seshachalam,V.P., Chen,G.,
            Gunaratne,J., Hong,W., Shi,J., Chen,G., Grierson,D.S., Chabot,B.,
            Xie,T., Hui,K.M. and Chen,J.
  TITLE     The aberrant upregulation of exon 10-inclusive SREK1 through SRSF10
            acts as an oncogenic driver in human hepatocellular carcinoma
  JOURNAL   Nat Commun 13 (1), 1363 (2022)
   PUBMED   35296659
  REMARK    GeneRIF: The aberrant upregulation of exon 10-inclusive SREK1
            through SRSF10 acts as an oncogenic driver in human hepatocellular
            carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Abudureheman,Z., Li,L., Zhong,X., Xu,J., Gong,H., Yilamujiang,S.,
            Ren,J., Xie,C., Zheng,A., Tuerxun,D., Abudukadeer,A., Aini,P.,
            Xu,A. and Zou,X.
  TITLE     The rs74794265 SNP of the SREK1 Gene is Associated with COPD in
            Kashi, China
  JOURNAL   Int J Chron Obstruct Pulmon Dis 16, 2631-2636 (2021)
   PUBMED   34556983
  REMARK    GeneRIF: The rs74794265 SNP of the SREK1 Gene is Associated with
            COPD in Kashi, China.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Hernandez,I.H., Cabrera,J.R., Santos-Galindo,M., Sanchez-Martin,M.,
            Dominguez,V., Garcia-Escudero,R., Perez-Alvarez,M.J., Pintado,B.
            and Lucas,J.J.
  TITLE     Pathogenic SREK1 decrease in Huntington's disease lowers TAF1
            mimicking X-linked dystonia parkinsonism
  JOURNAL   Brain 143 (7), 2207-2219 (2020)
   PUBMED   32533168
  REMARK    GeneRIF: Pathogenic SREK1 decrease in Huntington's disease lowers
            TAF1 mimicking X-linked dystonia parkinsonism.
REFERENCE   6  (residues 1 to 624)
  AUTHORS   Heese,K., Fujita,M., Akatsu,H., Yamamoto,T., Kosaka,K., Nagai,Y.
            and Sawada,T.
  TITLE     The splicing regulatory protein p18SRP is down-regulated in
            Alzheimer's disease brain
  JOURNAL   J Mol Neurosci 24 (2), 269-276 (2004)
   PUBMED   15456940
  REMARK    GeneRIF: p18SRP is a lysine-rich zinc finger domain-containing
            protein that interacts with the serine-arginine-rich splicing
            regulatory protein SRrp86; it is downregulated in brain of
            Alzheimer disease patients.
REFERENCE   7  (residues 1 to 624)
  AUTHORS   Li,J., Hawkins,I.C., Harvey,C.D., Jennings,J.L., Link,A.J. and
            Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 and its interacting
            proteins
  JOURNAL   Mol Cell Biol 23 (21), 7437-7447 (2003)
   PUBMED   14559993
REFERENCE   8  (residues 1 to 624)
  AUTHORS   Li,J., Barnard,D.C. and Patton,J.G.
  TITLE     A unique glutamic acid-lysine (EK) domain acts as a splicing
            inhibitor
  JOURNAL   J Biol Chem 277 (42), 39485-39492 (2002)
   PUBMED   12183448
  REMARK    GeneRIF: the unique glutamic acid-lysine domain of SRrp86 plays a
            modulatory role controlling serine-arginine domain function
REFERENCE   9  (residues 1 to 624)
  AUTHORS   Barnard,D.C., Li,J., Peng,R. and Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 through coactivation
            and repression of specific SR proteins
  JOURNAL   RNA 8 (4), 526-533 (2002)
   PUBMED   11991645
  REMARK    GeneRIF: SRrp86 can activate SRp20 and repress SC35 in a
            dose-dependent manner both in vitro and in vivo
REFERENCE   10 (residues 1 to 624)
  AUTHORS   Barnard,D.C. and Patton,J.G.
  TITLE     Identification and characterization of a novel serine-arginine-rich
            splicing regulatory protein
  JOURNAL   Mol Cell Biol 20 (9), 3049-3057 (2000)
   PUBMED   10757789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD706234.1, BC047322.1,
            BC112343.1 and AC008772.6.
            
            Summary: This gene encodes a member of a family of
            serine/arginine-rich (SR) splicing proteins containing RNA
            recognition motif (RRM) domains. The encoded protein interacts with
            other SR proteins to modulate splice site selection. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.256286.1,
                                           SRR1803614.241324.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334121.11/ ENSP00000334538.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..624
                     /product="splicing regulatory glutamine/lysine-rich
                     protein 1 isoform a"
                     /note="splicing factor, arginine/serine-rich 12;
                     serine-arginine-rich splicing regulatory protein 508;
                     serine/arginine-rich-splicing regulatory protein 86;
                     splicing regulatory glutamine/lysine-rich protein 1;
                     splicing regulatory glutamic acid/lysine-rich protein 1"
                     /calculated_mol_wt=71519
     Region          20..99
                     /region_name="RRM1_SREK1"
                     /note="RNA recognition motif 1 (RRM1) found in splicing
                     regulatory glutamine/lysine-rich protein 1 (SREK1) and
                     similar proteins; cd12519"
                     /db_xref="CDD:409941"
     Region          178..263
                     /region_name="RRM2_SREK1"
                     /note="RNA recognition motif 2 (RRM2) found in splicing
                     regulatory glutamine/lysine-rich protein 1 (SREK1) and
                     similar proteins; cd12260"
                     /db_xref="CDD:409705"
     CDS             1..624
                     /gene="SREK1"
                     /gene_synonym="SFRS12; SRrp508; SRrp86"
                     /coded_by="NM_001077199.3:78..1952"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43323.1"
                     /db_xref="GeneID:140890"
                     /db_xref="HGNC:HGNC:17882"
                     /db_xref="MIM:609268"
ORIGIN      
        1 mnsgggfglg lgfgltptsv iqvtnlssav tseqmrtlfs flgeieelrl yppdnaplaf
       61 sskvcyvkfr dpssvgvaqh ltntvfidra livvpcaegk ipeeskalsl lapaptmtsl
      121 mpgagllpip tpnplttlgv slsslgaipa aaldpniatl geipqpplmg nvdpskidei
      181 rrtvyvgnln sqtttadqll effkqvgevk fvrmagdetq ptrfafvefa dqnsvprala
      241 fngvmfgdrp lkinhsnnai vkppemtpqa aakeleevmk rvreaqsfis aaiepesgks
      301 nerkggrsrs htrsksrsss kshsrrkrsq skhrsrshnr srsrqkdrrr sksphkkrsk
      361 srerrksrsr shsrdkrkdt rekikekerv kekdrekere rekerekeke rgknkdrdke
      421 rekdrekdke kdrerereke hekdrdkeke keqdkekere kdrskeidek rkkdkksrtp
      481 prsynasrrs rsssrerrrr rsrsssrspr tsktikrkss rspsprsrnk kdkkrekerd
      541 hiserrerer stsmrkssnd rdgkeklekn stslkekehn kepdssvske vddkdaprte
      601 enkiqhngnc qlneenlstk teav
//
LOCUS       NP_079009                678 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 665 isoform 3 [Homo sapiens].
ACCESSION   NP_079009
VERSION     NP_079009.3
DBSOURCE    REFSEQ: accession NM_024733.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Wan,Y.I., Shrine,N.R., Soler Artigas,M., Wain,L.V., Blakey,J.D.,
            Moffatt,M.F., Bush,A., Chung,K.F., Cookson,W.O., Strachan,D.P.,
            Heaney,L., Al-Momani,B.A., Mansur,A.H., Manney,S., Thomson,N.C.,
            Chaudhuri,R., Brightling,C.E., Bafadhel,M., Singapuri,A., Niven,R.,
            Simpson,A., Holloway,J.W., Howarth,P.H., Hui,J., Musk,A.W.,
            James,A.L., Brown,M.A., Baltic,S., Ferreira,M.A., Thompson,P.J.,
            Tobin,M.D., Sayers,I. and Hall,I.P.
  CONSRTM   Australian Asthma Genetics Consortium
  TITLE     Genome-wide association study to identify genetic determinants of
            severe asthma
  JOURNAL   Thorax 67 (9), 762-768 (2012)
   PUBMED   22561531
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092070.2.
            
            On Mar 29, 2007 this sequence version replaced NP_079009.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832507.1, SRR3476690.839333.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396424.5/ ENSP00000379702.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..678
                     /product="zinc finger protein 665 isoform 3"
                     /calculated_mol_wt=77509
     Region          8..61
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          164..552
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          180..200
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          208..228
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          236..256
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          264..284
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          292..312
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(297,299,301,303..304,307..308,311,325,327,331..332,
                     335..336,339,353,355,357,359..360,363..364,367)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          320..340
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          348..368
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          376..396
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          404..424
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          432..452
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          460..480
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          488..508
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          516..536
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          544..564
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(549,551,553,555..556,559..560,563,577,579,583..584,
                     587..588,591,605,607,609,611..612,615..616,619)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          556..580
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          572..592
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          584..609
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          600..620
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          612..636
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          628..648
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          641..665
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          656..676
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..678
                     /gene="ZNF665"
                     /gene_synonym="ZFP160L"
                     /coded_by="NM_024733.5:93..2129"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS46169.1"
                     /db_xref="GeneID:79788"
                     /db_xref="HGNC:HGNC:25885"
ORIGIN      
        1 malpqgqltf kdvaiefsqe ewtcldpaqk tlyrdvmlen yrnlvsldis ckcvntdlpp
       61 kgknnmgeaf ytvklerles cdtvglsfqe vqkntydfec qwkddegnyk tvlmlqkenl
      121 pgrraqrdrr aagnrhienq lgvsfqshlp elqqfqhegk iyeynqveks pnnrgkhykc
      181 decgkvfsqn srltshkrih tgekpyqcnk cgkaftvrsn ltihqvihtg ekpykcnecg
      241 kvfsqpsnla ghqrihtgek pykcnecgka frahskltth qvihtgekpy kckecgkcft
      301 qnshlashrr ihtgekpykc necgkafsvr ssltthqtih tgekpykcne cgkvfrhnsy
      361 lakhrrihtg ekpykcnecg kafsmhsnlt khqiihtgek pfkcnecvkv ftqyshlanh
      421 rrihtgekpy rcdecgkafs vrssltthqa ihtgekpykc ndcgkvftqn shlashrgih
      481 sgekpykcde cgkafsqtsq larhwrvhtg ekpykcnecg kafsvhsslt ihqtihtgqk
      541 pykcndcgkv frhnsylaih qrihtgekpy kcnecgkafs vhsnlathqv ihtgekpykc
      601 necgkvftqn shlanhrrih tgekpyrcne cgkafsvrst ltthmavhtg dkpykcnqcg
      661 kvftqnsnla khrrihsg
//
LOCUS       NP_006846                214 aa            linear   PRI 27-APR-2025
DEFINITION  ER lumen protein-retaining receptor 3 isoform a [Homo sapiens].
ACCESSION   NP_006846
VERSION     NP_006846.1
DBSOURCE    REFSEQ: accession NM_006855.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Bauer,A., Santen,L., Schmitt,M.J., Shaebani,M.R. and Becker,B.
  TITLE     Cell-type-specific differences in KDEL receptor clustering in
            mammalian cells
  JOURNAL   PLoS One 15 (7), e0235864 (2020)
   PUBMED   32645101
  REMARK    GeneRIF: Cell-type-specific differences in KDEL receptor clustering
            in mammalian cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Raykhel,I., Alanen,H., Salo,K., Jurvansuu,J., Nguyen,V.D.,
            Latva-Ranta,M. and Ruddock,L.
  TITLE     A molecular specificity code for the three mammalian KDEL receptors
  JOURNAL   J Cell Biol 179 (6), 1193-1204 (2007)
   PUBMED   18086916
  REMARK    Erratum:[J Cell Biol. 2008 Feb 11;180(3):645]
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   5  (residues 1 to 214)
  AUTHORS   Collins,J.E., Goward,M.E., Cole,C.G., Smink,L.J., Huckle,E.J.,
            Knowles,S., Bye,J.M., Beare,D.M. and Dunham,I.
  TITLE     Reevaluating human gene annotation: a second-generation analysis of
            chromosome 22
  JOURNAL   Genome Res 13 (1), 27-36 (2003)
   PUBMED   12529303
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Jia,L., Young,M.F., Powell,J., Yang,L., Ho,N.C., Hotchkiss,R.,
            Robey,P.G. and Francomano,C.A.
  TITLE     Gene expression profile of human bone marrow stromal cells:
            high-throughput expressed sequence tag sequencing analysis
  JOURNAL   Genomics 79 (1), 7-17 (2002)
   PUBMED   11827452
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   8  (residues 1 to 214)
  AUTHORS   Pelham,H.R.
  TITLE     The dynamic organisation of the secretory pathway
  JOURNAL   Cell Struct Funct 21 (5), 413-419 (1996)
   PUBMED   9118249
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z97056.1, AL035081.1 and
            AI753246.1.
            
            Summary: This gene encodes a member of the KDEL endoplasmic
            reticulum protein retention receptor family. Retention of resident
            soluble proteins in the lumen of the endoplasmic reticulum (ER) is
            achieved in both yeast and animal cells by their continual
            retrieval from the cis-Golgi, or a pre-Golgi compartment. Sorting
            of these proteins is dependent on a C-terminal tetrapeptide signal,
            usually lys-asp-glu-leu (KDEL) in animal cells, and his-asp-glu-leu
            (HDEL) in S. cerevisiae. This process is mediated by a receptor
            that recognizes, and binds the tetrapeptide-containing protein, and
            returns it to the ER. In yeast, the sorting receptor encoded by a
            single gene, ERD2, is a seven-transmembrane protein. Unlike yeast,
            several human homologs of the ERD2 gene, constituting the KDEL
            receptor gene family, have been described. KDELR3 was the third
            member of the family to be identified. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001277.1, SRR5189661.53921.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216014.9/ ENSP00000216014.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..214
                     /product="ER lumen protein-retaining receptor 3 isoform a"
                     /note="KDEL receptor 3; ER lumen protein-retaining
                     receptor 3; KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum
                     protein retention receptor 3"
                     /calculated_mol_wt=24896
     Site            5..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Site            5
                     /site_type="other"
                     /note="Interaction with the K-D-E-L motif on target
                     proteins. /evidence=ECO:0000250|UniProtKB:Q5ZKX9;
                     propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Region          29..169
                     /region_name="ER_lumen_recept"
                     /note="ER lumen protein retaining receptor; pfam00810"
                     /db_xref="CDD:459945"
     Site            33..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Region          47..48
                     /region_name="Interaction with the K-D-E-L motif on target
                     proteins. /evidence=ECO:0000250|UniProtKB:Q5ZKX9"
                     /note="propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Site            93..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Site            117..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Site            117
                     /site_type="other"
                     /note="Interaction with the K-D-E-L motif on target
                     proteins. /evidence=ECO:0000250|UniProtKB:Q5ZKX9;
                     propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Site            150..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Region          159..169
                     /region_name="Interaction with the K-D-E-L motif on target
                     proteins. /evidence=ECO:0000250|UniProtKB:Q5ZKX9"
                     /note="propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Site            193
                     /site_type="other"
                     /note="Important for recycling of cargo proteins with the
                     sequence motif K-D-E-L from the Golgi to the endoplasmic
                     reticulum. /evidence=ECO:0000250|UniProtKB:P24390;
                     propagated from UniProtKB/Swiss-Prot (O43731.1)"
     Region          204..207
                     /region_name="Important for recycling of cargo proteins
                     with the sequence motif K-D-E-L from the Golgi to the
                     endoplasmic reticulum.
                     /evidence=ECO:0000250|UniProtKB:P24390"
                     /note="propagated from UniProtKB/Swiss-Prot (O43731.1)"
     CDS             1..214
                     /gene="KDELR3"
                     /gene_synonym="ERD23; ERD2L3"
                     /coded_by="NM_006855.4:139..783"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13972.1"
                     /db_xref="GeneID:11015"
                     /db_xref="HGNC:HGNC:6306"
                     /db_xref="MIM:619900"
ORIGIN      
        1 mnvfrilgdl shllamilll gkiwrskcck gisgksqilf alvfttryld lftnfisiyn
       61 tvmkvvfllc ayvtvymiyg kfrktfdsen dtfrlefllv pviglsflen ysftlleilw
      121 tfsiylesva ilpqlfmisk tgeaetitth ylfflglyra lylanwirry qtenfydqia
      181 vvsgvvqtif ycdffylyvt kvlkgkklsl pmpi
//
LOCUS       NP_000604                462 aa            linear   PRI 27-APR-2025
DEFINITION  hemopexin precursor [Homo sapiens].
ACCESSION   NP_000604
VERSION     NP_000604.1
DBSOURCE    REFSEQ: accession NM_000613.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Greite,R., Schott,S., Wang,L., Gohlke,L., Kreimann,K., Derlin,K.,
            Gutberlet,M., Schmidbauer,M., Leffler,A., Tudorache,I., Salman,J.,
            Ius,F., Natanov,R., Fegbeutel,C., Haverich,A., Lichtinghagen,R.,
            Husing,A.M., von Vietinghoff,S., Schmitt,R., Shushakova,N.,
            Rong,S., Haller,H., Schmidt-Ott,K.M., Gram,M., Vijayan,V.,
            Scheffner,I., Gwinner,W. and Immenschuh,S.
  TITLE     Free heme and hemopexin in acute kidney injury after
            cardiopulmonary bypass and transient renal ischemia
  JOURNAL   Clin Transl Sci 16 (12), 2729-2743 (2023)
   PUBMED   37899696
  REMARK    GeneRIF: Free heme and hemopexin in acute kidney injury after
            cardiopulmonary bypass and transient renal ischemia.
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Liu,W., Lu,L., Pan,H., He,X., Zhang,M., Wang,N., Zhu,J., Yi,H. and
            Tang,S.
  TITLE     Heme oxygenase-1 and hemopexin gene polymorphisms and the risk of
            anti-tuberculosis drug-induced hepatotoxicity in China
  JOURNAL   Pharmacogenomics 23 (7), 431-441 (2022)
   PUBMED   35470713
  REMARK    GeneRIF: Heme oxygenase-1 and hemopexin gene polymorphisms and the
            risk of anti-tuberculosis drug-induced hepatotoxicity in China.
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yildirim,N., Unal,S., Yalcinkaya,A., Karahan,F. and Oztas,Y.
  TITLE     Evaluation of the relationship between intravascular hemolysis and
            clinical manifestations in sickle cell disease: decreased hemopexin
            during vaso-occlusive crises and increased inflammation in acute
            chest syndrome
  JOURNAL   Ann Hematol 101 (1), 35-41 (2022)
   PUBMED   34564750
  REMARK    GeneRIF: Evaluation of the relationship between intravascular
            hemolysis and clinical manifestations in sickle cell disease:
            decreased hemopexin during vaso-occlusive crises and increased
            inflammation in acute chest syndrome.
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Law,M.L., Cai,G.Y., Hartz,J.A., Jones,C. and Kao,F.T.
  TITLE     The hemopexin gene maps to the same location as the beta-globin
            gene cluster on human chromosome 11
  JOURNAL   Genomics 3 (1), 48-52 (1988)
   PUBMED   3220477
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Morgan,W.T., Alam,J., Deaciuc,V., Muster,P., Tatum,F.M. and
            Smith,A.
  TITLE     Interaction of hemopexin with Sn-protoporphyrin IX, an inhibitor of
            heme oxygenase. Role for hemopexin in hepatic uptake of
            Sn-protoporphyrin IX and induction of mRNA for heme oxygenase
  JOURNAL   J Biol Chem 263 (17), 8226-8231 (1988)
   PUBMED   3372522
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Smith,A., Tatum,F.M., Muster,P., Burch,M.K. and Morgan,W.T.
  TITLE     Importance of ligand-induced conformational changes in hemopexin
            for receptor-mediated heme transport
  JOURNAL   J Biol Chem 263 (11), 5224-5229 (1988)
   PUBMED   2833500
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Altruda,F., Poli,V., Restagno,G. and Silengo,L.
  TITLE     Structure of the human hemopexin gene and evidence for
            intron-mediated evolution
  JOURNAL   J Mol Evol 27 (2), 102-108 (1988)
   PUBMED   2842511
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Taketani,S., Kohno,H., Naitoh,Y. and Tokunaga,R.
  TITLE     Isolation of the hemopexin receptor from human placenta
  JOURNAL   J Biol Chem 262 (18), 8668-8671 (1987)
   PUBMED   3036819
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Altruda,F., Poli,V., Restagno,G., Argos,P., Cortese,R. and
            Silengo,L.
  TITLE     The primary structure of human hemopexin deduced from cDNA
            sequence: evidence for internal, repeating homology
  JOURNAL   Nucleic Acids Res 13 (11), 3841-3859 (1985)
   PUBMED   2989777
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Takahashi,N., Takahashi,Y. and Putnam,F.W.
  TITLE     Complete amino acid sequence of human hemopexin, the heme-binding
            protein of serum
  JOURNAL   Proc Natl Acad Sci U S A 82 (1), 73-77 (1985)
   PUBMED   3855550
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC005395.1, AK313648.1 and
            AV655383.1.
            
            Summary: This gene encodes a plasma glycoprotein that binds heme
            with high affinity. The encoded protein is an acute phase protein
            that transports heme from the plasma to the liver and may be
            involved in protecting cells from oxidative stress. [provided by
            RefSeq, Apr 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.81928.1,
                                           SRR5189658.89065.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265983.8/ ENSP00000265983.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..462
                     /product="hemopexin precursor"
                     /EC_number="3.2.1.35"
                     /note="beta-1B-glycoprotein; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=49296
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2399
     mat_peptide     24..462
                     /product="hemopexin"
                     /calculated_mol_wt=49296
     Site            24
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:19838169,
                     ECO:0000269|PubMed:6371807, ECO:0000269|PubMed:6510521;
                     propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Region          29..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Site            29
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:23234360; propagated from
                     UniProtKB/Swiss-Prot (P02790.2)"
     Region          30..40
                     /region_name="O-glycosylated at one site"
                     /note="propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Region          47..231
                     /region_name="HX"
                     /note="Hemopexin-like repeats.; Hemopexin is a
                     heme-binding protein that transports heme to the liver.
                     Hemopexin-like repeats occur in vitronectin and some
                     matrix metalloproteinases family (matrixins). The HX
                     repeats of some matrixins bind tissue inhibitor of...;
                     cd00094"
                     /db_xref="CDD:238046"
     Region          53..93
                     /region_name="Hemopexin 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Site            order(57,59,98,100,144,146,189,191)
                     /site_type="metal-binding"
                     /note="Metal binding sites [ion binding]"
                     /db_xref="CDD:238046"
     Site            64
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:6371807;
                     propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Region          94..139
                     /region_name="Hemopexin 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Region          140..184
                     /region_name="Hemopexin 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Region          185..231
                     /region_name="Hemopexin 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Site            187
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
                     ECO:0000269|PubMed:6371807; propagated from
                     UniProtKB/Swiss-Prot (P02790.2)"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:6371807, ECO:0000269|PubMed:6510521;
                     propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Site            246
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:6371807, ECO:0000269|PubMed:6510521;
                     propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Region          256..460
                     /region_name="HX"
                     /note="Hemopexin-like repeats.; Hemopexin is a
                     heme-binding protein that transports heme to the liver.
                     Hemopexin-like repeats occur in vitronectin and some
                     matrix metalloproteinases family (matrixins). The HX
                     repeats of some matrixins bind tissue inhibitor of...;
                     cd00094"
                     /db_xref="CDD:238046"
     Region          259..304
                     /region_name="Hemopexin 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Site            order(264,266,309,311,361,363,404,406)
                     /site_type="metal-binding"
                     /note="Metal binding sites [ion binding]"
                     /db_xref="CDD:238046"
     Region          305..352
                     /region_name="Hemopexin 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Region          357..396
                     /region_name="Hemopexin 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Region          400..450
                     /region_name="Hemopexin 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P02790.2)"
     Site            453
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:15084671,
                     ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
                     ECO:0000269|PubMed:6371807; propagated from
                     UniProtKB/Swiss-Prot (P02790.2)"
     CDS             1..462
                     /gene="HPX"
                     /gene_synonym="HX"
                     /coded_by="NM_000613.3:25..1413"
                     /db_xref="CCDS:CCDS7763.1"
                     /db_xref="GeneID:3263"
                     /db_xref="HGNC:HGNC:5171"
                     /db_xref="MIM:142290"
ORIGIN      
        1 marvlgapva lglwslcwsl aiatplppts ahgnvaeget kpdpdvterc sdgwsfdatt
       61 lddngtmlff kgefvwkshk wdreliserw knfpspvdaa frqghnsvfl ikgdkvwvyp
      121 pekkekgypk llqdefpgip spldaavech rgecqaegvl ffqgdrewfw dlatgtmker
      181 swpavgncss alrwlgryyc fqgnqflrfd pvrgevppry prdvrdyfmp cpgrghghrn
      241 gtghgnsthh gpeymrcsph lvlsaltsdn hgatyafsgt hywrldtsrd gwhswpiahq
      301 wpqgpsavda afsweeklyl vqgtqvyvfl tkggytlvsg ypkrlekevg tphgiildsv
      361 daaficpgss rlhimagrrl wwldlksgaq atwtelpwph ekvdgalcme kslgpnscsa
      421 ngpglylihg pnlycysdve klnaakalpq pqnvtsllgc th
//
LOCUS       NP_659441                787 aa            linear   PRI 27-APR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 32
            isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_659441 XP_945593
VERSION     NP_659441.4
DBSOURCE    REFSEQ: accession NM_145004.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   3  (residues 1 to 787)
  AUTHORS   Choi,I., Woo,J.M., Hong,S., Jung,Y.K., Kim,D.H. and Cho,C.
  TITLE     Identification and characterization of ADAM32 with
            testis-predominant gene expression
  JOURNAL   Gene 304, 151-162 (2003)
   PUBMED   12568724
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105091.3 and AC105185.5.
            
            On Nov 23, 2018 this sequence version replaced NP_659441.3.
            
            Summary: This gene encodes a member of the disintegrin family of
            membrane-anchored proteins that play a role in diverse biological
            processes such as brain development, fertilization, tumor
            development and inflammation. This gene is predominantly expressed
            in the testis. The encoded protein undergoes proteolytic processing
            to generate a mature polypeptide comprised of an metalloprotease,
            disintegrin and epidermal growth factor-like domains. This gene is
            located in a cluster of other disintegrin and metallopeptidase
            family genes on chromosome 8. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034975.2, BC026169.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379907.9/ ENSP00000369238.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.22"
     Protein         1..787
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 32 isoform 1 preproprotein"
                     /note="a disintegrin and metalloprotease domain 32; a
                     disintegrin and metalloproteinase domain 32; disintegrin
                     and metalloproteinase domain-containing protein 32;
                     metalloproteinase 12-like protein; testicular tissue
                     protein Li 13"
                     /calculated_mol_wt=86176
     sig_peptide     1..16
                     /note="/evidence=ECO:0000269|PubMed:15340161; propagated
                     from UniProtKB/Swiss-Prot (Q8TC27.2)"
                     /calculated_mol_wt=1790
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8TC27.2)"
     Region          27..144
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TC27.2)"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TC27.2)"
     mat_peptide     175..787
                     /product="Disintegrin and metalloproteinase
                     domain-containing protein 32. /id=PRO_0000029139"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC27.2)"
                     /calculated_mol_wt=67854
     Region          187..381
                     /region_name="ZnMc_adamalysin_II_like"
                     /note="Zinc-dependent metalloprotease; adamalysin_II_like
                     subfamily. Adamalysin II is a snake venom zinc
                     endopeptidase. This subfamily contains other snake venom
                     metalloproteinases, as well as membrane-anchored
                     metalloproteases belonging to the ADAM family; cd04269"
                     /db_xref="CDD:239797"
     Site            order(321..322,325,331)
                     /site_type="active"
                     /db_xref="CDD:239797"
     Region          400..474
                     /region_name="Disintegrin"
                     /note="pfam00200"
                     /db_xref="CDD:459709"
     Site            465
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TC27.2)"
     Region          479..616
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     Site            598
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TC27.2)"
     Site            683..703
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC27.2)"
     Region          714..786
                     /region_name="SEEEED"
                     /note="Serine-rich region of AP3B1, clathrin-adaptor
                     complex; pfam14797"
                     /db_xref="CDD:434218"
     Region          715..787
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC27.2)"
     CDS             1..787
                     /gene="ADAM32"
                     /coded_by="NM_145004.7:43..2406"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS47846.1"
                     /db_xref="GeneID:203102"
                     /db_xref="HGNC:HGNC:15479"
                     /db_xref="MIM:618602"
ORIGIN      
        1 mfrlwlllag lcgllasrpg fqnsllqivi pekiqtntnd sseieyeqis yiipidekly
       61 tvhlkqryfl adnfmiylyn qgsmntyssd iqtqcyyqgn iegypdsmvt lstcsglrgi
      121 lqfenvsygi eplesavefq hvlyklkned ndiaifidrs lkeqpmddni fiseksepav
      181 pdlfplylem hivvdktlyd ywgsdsmivt nkvieivgla nsmftqfkvt ivlsslelws
      241 denkistvge adellqkfle wkqsylnlrp hdiaylliym dyprylgavf pgtmcitrys
      301 agvalypkei tleafavivt qmlalslgis yddpkkcqcs estcimnpev vqsngvktfs
      361 scslrsfqnf isnvgvkclq nkpqmqkksp kpvcgngrle gneicdcgte aqcgpasccd
      421 frtcvlkdga kcykglcckd cqilqsgvec rpkahpecdi aencngtspe cgpditling
      481 lscknnkfic ydgdchdlda rcesvfgkgs rnapfacyee iqsqsdrfgn cgrdrnnkyv
      541 fcgwrnlicg rlvctyptrk pfhqengdvi yafvrdsvci tvdyklprtv pdplavkngs
      601 qcdigrvcvn recvesriik asahvcsqqc sghgvcdsrn kchcspgykp pncqirskgf
      661 sifpeedmgs imerasgkte ntwllgflia lpilivttai vlarkqlkkw fakeeefpss
      721 esksegstqt yasqsssegs tqtyasqtrs esssqadtsk sksedsaeay tsrsksqdst
      781 qtqsssn
//
LOCUS       NP_001154801             703 aa            linear   ROD 27-APR-2025
DEFINITION  nucleolar protein 11 isoform 2 [Mus musculus].
ACCESSION   NP_001154801
VERSION     NP_001154801.1
DBSOURCE    REFSEQ: accession NM_001161329.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK076704.1, AK078524.1 and AL596116.14.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK076704.1, AK038696.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 70.19 cM"
     Protein         1..703
                     /product="nucleolar protein 11 isoform 2"
                     /calculated_mol_wt=78426
     Region          200..243
                     /region_name="NUC205"
                     /note="NUC205 domain; pfam08168"
                     /db_xref="CDD:429856"
     CDS             1..703
                     /gene="Nol11"
                     /gene_synonym="1500002M01Rik"
                     /coded_by="NM_001161329.2:125..2236"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS48965.1"
                     /db_xref="GeneID:68979"
                     /db_xref="MGI:MGI:1916229"
ORIGIN      
        1 matleeeftl stgvlgagpe gflgveqtdk adqflvtdsg rtvvlykvsd qkplgswsvk
       61 qgqsitcpav cnfqtgeyim vhdhkvlriw nnddvnvdkv fkatlsaevh rihsvqrtep
      121 lvlfrggaar gleallvepq qniesvipde evivwsevfm lfkqpvlifi tenhghyyay
      181 vrlckshsls kytlllekee ksvkpnftar vdgkfislvs lssdgciyet lipiyssdte
      241 qnqrlvralm lksvvsggvr ngvaltildq dhiavlgppl saskeclsiw nikfqtlqts
      301 kelpqgtsgq lwyhgevlfm lhgksltvip ykceesslag algklkhtqe sgthsvphfv
      361 nwetcsgyel gssgaeqsrt lrrkkvetnl qpevpgfkql lsiikkdsek hievelrkfl
      421 akstpafhti igdlvaglvg rckaepsfyp rncltqliqt hvlsyslcpd lmeialehtd
      481 vqmlqlclqq fpdipesttc aclklflsds tqdekkemee qieivqngfg pedgncseds
      541 qqlndkpadt ahepgsfpvt scpvapkraa llnavlhsay sepfllphlk dipakhvtlf
      601 lqylyflylk ctgsatmtlp gvnpptvsqi mdwiclllda nftvllmipe akrlllilyn
      661 fvksqisiys elnkiavsfr elqrlnreks srglysievl elf
//
LOCUS       NP_061154                224 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger C4H2 domain-containing protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_061154
VERSION     NP_061154.1
DBSOURCE    REFSEQ: accession NM_018684.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Wongkittichote,P., Choi,T.I., Kim,O.H., Riley,K., Koeberl,D.,
            Narayanan,V., Ramsey,K., Balak,C., Schwartz,C.E.,
            Cueto-Gonzalez,A.M., Casadesus,F.M., Kim,C.H. and Shinawi,M.S.
  TITLE     Expanding allelic and phenotypic spectrum of ZC4H2-related
            disorder: A novel hypomorphic variant and high prevalence of
            tethered cord
  JOURNAL   Clin Genet 103 (2), 167-178 (2023)
   PUBMED   36250278
  REMARK    GeneRIF: Expanding allelic and phenotypic spectrum of ZC4H2-related
            disorder: A novel hypomorphic variant and high prevalence of
            tethered cord.
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Li,Y., Yang,C., Wang,H., Zhao,L., Kong,Q., Cang,Y., Zhao,S., Lv,L.,
            Li,Y., Mao,B. and Ma,P.
  TITLE     Sequential stabilization of RNF220 by RLIM and ZC4H2 during
            cerebellum development and Shh-group medulloblastoma progression
  JOURNAL   J Mol Cell Biol 14 (1) (2022)
   PUBMED   35040952
  REMARK    GeneRIF: Sequential stabilization of RNF220 by RLIM and ZC4H2
            during cerebellum development and Shh-group medulloblastoma
            progression.
            Erratum:[J Mol Cell Biol. 2022 May 25;14(2):mjac030. doi:
            10.1093/jmcb/mjac030. PMID: 35639540]
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Godfrey,D., Torres,A., Heidary,G., Zahoor,H., Lee,A., Berry,G. and
            Engle,E.
  TITLE     A 7-year old female with arthrogryposis multiplex congenita, Duane
            retraction syndrome, and Marcus Gunn phenomenon due to a ZC4H2 gene
            mutation: a clinical presentation of the Wieacker-Wolff syndrome
  JOURNAL   Ophthalmic Genet 42 (5), 612-614 (2021)
   PUBMED   33949289
  REMARK    GeneRIF: A 7-year old female with arthrogryposis multiplex
            congenita, Duane retraction syndrome, and Marcus Gunn phenomenon
            due to a ZC4H2 gene mutation: a clinical presentation of the
            Wieacker-Wolff syndrome.
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Lombard,Z., Park,C., Makova,K.D. and Ramsay,M.
  TITLE     A computational approach to candidate gene prioritization for
            X-linked mental retardation using annotation-based binary filtering
            and motif-based linear discriminatory analysis
  JOURNAL   Biol Direct 6, 30 (2011)
   PUBMED   21668950
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Kroncke,K.D. and Klotz,L.O.
  TITLE     Zinc fingers as biologic redox switches?
  JOURNAL   Antioxid Redox Signal 11 (5), 1015-1027 (2009)
   PUBMED   19132878
  REMARK    Review article
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Wang,Y., Han,K.J., Pang,X.W., Vaughan,H.A., Qu,W., Dong,X.Y.,
            Peng,J.R., Zhao,H.T., Rui,J.A., Leng,X.S., Cebon,J., Burgess,A.W.
            and Chen,W.F.
  TITLE     Large scale identification of human hepatocellular
            carcinoma-associated antigens by autoantibodies
  JOURNAL   J Immunol 169 (2), 1102-1109 (2002)
   PUBMED   12097419
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Mulley,J.C., Kerr,B., Stevenson,R. and Lubs,H.
  TITLE     Nomenclature guidelines for X-linked mental retardation
  JOURNAL   Am J Med Genet 43 (1-2), 383-391 (1992)
   PUBMED   1605216
  REMARK    Review article
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Miles,J.H. and Carpenter,N.J.
  TITLE     Unique X-linked mental retardation syndrome with fingertip arches
            and contractures linked to Xq21.31
  JOURNAL   Am J Med Genet 38 (2-3), 215-223 (1991)
   PUBMED   2018061
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC004411.1 and AK001547.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the zinc finger
            domain-containing protein family. This family member has a
            C-terminal zinc finger domain that is characterized by four
            cysteine residues and two histidine residues, and it also includes
            a coiled-coil region. This protein has been detected as an
            autoantigen in hepatocellular carcinoma patients. This gene has
            been identified as a potential candidate for X-linked cognitive
            disability. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1570751.1, BC004411.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374839.8/ ENSP00000363972.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq11.2"
     Protein         1..224
                     /product="zinc finger C4H2 domain-containing protein
                     isoform 1"
                     /note="hepatocellular carcinoma-associated antigen 127;
                     zinc finger C4H2 domain-containing protein; zinc finger,
                     C4H2 domain containing"
                     /calculated_mol_wt=26113
     Region          13..221
                     /region_name="zf-C4H2"
                     /note="Zinc finger-containing protein; pfam10146"
                     /db_xref="CDD:462963"
     CDS             1..224
                     /gene="ZC4H2"
                     /gene_synonym="HCA127; KIAA1166; MCS; MRXS4; WRWF; WRWFFR;
                     WWS"
                     /coded_by="NM_018684.4:74..748"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14380.1"
                     /db_xref="GeneID:55906"
                     /db_xref="HGNC:HGNC:24931"
                     /db_xref="MIM:300897"
ORIGIN      
        1 madeqeimck lesikeirnk tlqmekikar lkaefeales eerhlkeykq emdlllqekm
       61 ahveelrlih adinvmenti kqsendlnkl lestrrlhde ykplkehvda lrmtlglqrl
      121 pdlceeeekl sldyfekqka ewqtepqepp ipeslaaaaa aaqqlqvark qdtrqtatfr
      181 qqpppmkacl schqqihrna picplckaks rsrnpkkpkr kqde
//
LOCUS       NP_001349140             623 aa            linear   ROD 27-APR-2025
DEFINITION  kelch repeat and BTB domain-containing protein 2 isoform a [Mus
            musculus].
ACCESSION   NP_001349140 XP_006505909
VERSION     NP_001349140.1
DBSOURCE    REFSEQ: accession NM_001362211.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Ding,J., Gao,W., Yang,H., Duan,L., Sun,D., Liu,L., Qu,X., Yu,H.,
            Xu,B., Zhao,S., Wang,L. and Chai,J.
  TITLE     KBTBD2 promotes proliferation and migration of gastric cancer via
            activating EGFR signaling pathway
  JOURNAL   Pathol Res Pract 254, 155095 (2024)
   PUBMED   38237399
  REMARK    GeneRIF: KBTBD2 promotes proliferation and migration of gastric
            cancer via activating EGFR signaling pathway.
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Zhang,Z., Gallagher,T., Scherer,P.E. and Beutler,B.
  TITLE     Tissue-specific disruption of Kbtbd2 uncovers adipocyte-intrinsic
            and -extrinsic features of the teeny lipodystrophy syndrome
  JOURNAL   Proc Natl Acad Sci U S A 117 (21), 11829-11835 (2020)
   PUBMED   32381739
  REMARK    GeneRIF: Tissue-specific disruption of Kbtbd2 uncovers
            adipocyte-intrinsic and -extrinsic features of the teeny
            lipodystrophy syndrome.
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Dai,K., Huang,Y., Chen,Z., Sun,X., Yang,L. and Jiang,Y.
  TITLE     Kbtbd2 inhibits the cytotoxic activity of immortalized NK cells
            through down-regulating mTOR signaling in a mouse hepatocellular
            carcinoma model
  JOURNAL   Eur J Immunol 48 (4), 683-695 (2018)
   PUBMED   29331106
  REMARK    GeneRIF: This investigation indicates that Kbtbd2 is an inhibitory
            molecule for the tumoricidal activity of KIL C.2 Natural killer
            cells and perhaps intratumoral Natural killer cells.
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Zhang,Z., Turer,E., Li,X., Zhan,X., Choi,M., Tang,M., Press,A.,
            Smith,S.R., Divoux,A., Moresco,E.M. and Beutler,B.
  TITLE     Insulin resistance and diabetes caused by genetic or diet-induced
            KBTBD2 deficiency in mice
  JOURNAL   Proc Natl Acad Sci U S A 113 (42), E6418-E6426 (2016)
   PUBMED   27708159
  REMARK    GeneRIF: KBTBD2 is an essential regulator of the insulin-signaling
            pathway, modulating insulin sensitivity by limiting p85alpha
            abundance.
REFERENCE   5  (residues 1 to 623)
  AUTHORS   Wang,T., Zhan,X., Bu,C.H., Lyon,S., Pratt,D., Hildebrand,S.,
            Choi,J.H., Zhang,Z., Zeng,M., Wang,K.W., Turer,E., Chen,Z.,
            Zhang,D., Yue,T., Wang,Y., Shi,H., Wang,J., Sun,L., SoRelle,J.,
            McAlpine,W., Hutchins,N., Zhan,X., Fina,M., Gobert,R., Quan,J.,
            Kreutzer,M., Arnett,S., Hawkins,K., Leach,A., Tate,C., Daniel,C.,
            Reyna,C., Prince,L., Davis,S., Purrington,J., Bearden,R.,
            Weatherly,J., White,D., Russell,J., Sun,Q., Tang,M., Li,X.,
            Scott,L., Moresco,E.M., McInerney,G.M., Karlsson Hedestam,G.B.,
            Xie,Y. and Beutler,B.
  TITLE     Real-time resolution of point mutations that cause phenovariance in
            mice
  JOURNAL   Proc Natl Acad Sci U S A 112 (5), E440-E449 (2015)
   PUBMED   25605905
REFERENCE   6  (residues 1 to 623)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
REFERENCE   7  (residues 1 to 623)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC115003.18.
            
            On Apr 10, 2018 this sequence version replaced XP_006505909.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1-5 all encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.4021.1,
                                           SRR1660811.50248.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849386 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 27.73 cM"
     Protein         1..623
                     /product="kelch repeat and BTB domain-containing protein 2
                     isoform a"
                     /note="BTB and kelch domain containing 1; kelch repeat and
                     BTB domain-containing protein 2"
                     /calculated_mol_wt=71155
     Region          5..137
                     /region_name="BTB_POZ_KBTBD2_BKLHD1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch repeat
                     and BTB domain-containing protein 2 (KBTBD2); cd18270"
                     /db_xref="CDD:349579"
     Region          23..516
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          128..223
                     /region_name="BACK_KBTBD2"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch repeat and BTB domain-containing protein 2 (KBTBD2);
                     cd18479"
                     /db_xref="CDD:350554"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IY47; propagated from
                     UniProtKB/Swiss-Prot (G3X9X1.1)"
     Region          310..366
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          317..380
                     /region_name="Kelch 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3X9X1.1)"
     Region          374..415
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          381..429
                     /region_name="Kelch 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3X9X1.1)"
     Region          419..456
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          431..469
                     /region_name="Kelch 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3X9X1.1)"
     Region          459..516
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          470..529
                     /region_name="Kelch 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3X9X1.1)"
     Region          519..568
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          535..581
                     /region_name="Kelch 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3X9X1.1)"
     CDS             1..623
                     /gene="Kbtbd2"
                     /gene_synonym="Bklhd1; mKIAA1489"
                     /coded_by="NM_001362211.1:852..2723"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS51790.1"
                     /db_xref="GeneID:210973"
                     /db_xref="MGI:MGI:2384811"
ORIGIN      
        1 mstqeerqin teyavslleq lklfyeqqlf tdivlivegt efpchkmvla tcssyframf
       61 msglseskqt hvhlrnvdaa alqmiiayay tgnlavndst veqlyetacf lqvedvlqrc
      121 reylikkina encvrllsfa dlfsceelkq sakrmvehkf tavyrqeafm qlshdllidi
      181 lssdnlnvek eetvreaaml wleyntesrs qylssvlsqi ridalsevtq rawfqglppn
      241 dksvvvqgly ksmpkffkpr lgmtkeemmi fieassenpc slyssvcysp qaekvyklcs
      301 ppadlhkvgt vvtpdndiyi aggqvplknt ktnhsktskl qtafrtvncf ywfdaqqntw
      361 fpktpmlfvr vkpslvcceg yiyaiggdsv ggelnrrtve rydtekdewt mvsplpcawq
      421 wsaavvvhdc iyvmtlnlmy cyfprsdswv emamrqtsrs fasaaafgdk ifyigglhia
      481 tnsgirlpsg tvdgssvtve iydvnknewk maanipakry sdpcvravvi snslcvfmre
      541 thlnerakyv tyqydleldr wslrqhiser vlwdlgrdfr ctvgklypsc leespwkppt
      601 ylfspdgtee feldgemval ppv
//
LOCUS       NP_001036148            1683 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase SHPRH isoform a [Homo sapiens].
ACCESSION   NP_001036148
VERSION     NP_001036148.2
DBSOURCE    REFSEQ: accession NM_001042683.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1683)
  AUTHORS   Nagelberg,A.L., Sihota,T.S., Chuang,Y.C., Shi,R., Chow,J.L.M.,
            English,J., MacAulay,C., Lam,S., Lam,W.L. and Lockwood,W.W.
  TITLE     Integrative genomics identifies SHPRH as a tumor suppressor gene in
            lung adenocarcinoma that regulates DNA damage response
  JOURNAL   Br J Cancer 131 (3), 534-550 (2024)
   PUBMED   38890444
  REMARK    GeneRIF: Integrative genomics identifies SHPRH as a tumor
            suppressor gene in lung adenocarcinoma that regulates DNA damage
            response.
REFERENCE   2  (residues 1 to 1683)
  AUTHORS   Gao,J., Pan,H., Li,J., Jiang,J. and Wang,W.
  TITLE     A peptide encoded by the circular form of the SHPRH gene induces
            apoptosis in neuroblastoma cells
  JOURNAL   PeerJ 12, e16806 (2024)
   PUBMED   38282862
  REMARK    GeneRIF: A peptide encoded by the circular form of the SHPRH gene
            induces apoptosis in neuroblastoma cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1683)
  AUTHORS   Chen,W., Zhong,M., Yu,J., Xie,R., Zhou,T., Zhang,S., Xiong,C. and
            Huang,D.
  TITLE     KMT2B promotes SHPRH expression to regulate 131I sensitivity in
            thyroid carcinoma cells by affecting FYN protein stability
  JOURNAL   Cell Signal 88, 110165 (2021)
   PUBMED   34606908
  REMARK    GeneRIF: KMT2B promotes SHPRH expression to regulate (131)I
            sensitivity in thyroid carcinoma cells by affecting FYN protein
            stability.
REFERENCE   4  (residues 1 to 1683)
  AUTHORS   Seelinger,M., Sogaard,C.K. and Otterlei,M.
  TITLE     The Human RAD5 Homologs, HLTF and SHPRH, Have Separate Functions in
            DNA Damage Tolerance Dependent on The DNA Lesion Type
  JOURNAL   Biomolecules 10 (3), 463 (2020)
   PUBMED   32192191
  REMARK    GeneRIF: The Human RAD5 Homologs, HLTF and SHPRH, Have Separate
            Functions in DNA Damage Tolerance Dependent on The DNA Lesion Type.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1683)
  AUTHORS   Seelinger,M. and Otterlei,M.
  TITLE     Helicase-Like Transcription Factor HLTF and E3 Ubiquitin Ligase
            SHPRH Confer DNA Damage Tolerance through Direct Interactions with
            Proliferating Cell Nuclear Antigen (PCNA)
  JOURNAL   Int J Mol Sci 21 (3), 693 (2020)
   PUBMED   31973093
  REMARK    GeneRIF: Helicase-Like Transcription Factor HLTF and E3 Ubiquitin
            Ligase SHPRH Confer DNA Damage Tolerance through Direct
            Interactions with Proliferating Cell Nuclear Antigen (PCNA).
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1683)
  AUTHORS   Lin,J.R., Zeman,M.K., Chen,J.Y., Yee,M.C. and Cimprich,K.A.
  TITLE     SHPRH and HLTF act in a damage-specific manner to coordinate
            different forms of postreplication repair and prevent mutagenesis
  JOURNAL   Mol Cell 42 (2), 237-249 (2011)
   PUBMED   21396873
  REMARK    GeneRIF: HLTF and SHPRH suppress mutagenesis in a damage-specific
            manner, preventing mutations induced by UV rays and methyl
            methanesulfonate.
REFERENCE   7  (residues 1 to 1683)
  AUTHORS   Motegi,A., Liaw,H.J., Lee,K.Y., Roest,H.P., Maas,A., Wu,X.,
            Moinova,H., Markowitz,S.D., Ding,H., Hoeijmakers,J.H. and Myung,K.
  TITLE     Polyubiquitination of proliferating cell nuclear antigen by HLTF
            and SHPRH prevents genomic instability from stalled replication
            forks
  JOURNAL   Proc Natl Acad Sci U S A 105 (34), 12411-12416 (2008)
   PUBMED   18719106
  REMARK    GeneRIF: HLTF and SHPRH are functional homologues of yeast Rad5
            that cooperatively mediate PCNA polyubiquitination and maintain
            genomic stability.
REFERENCE   8  (residues 1 to 1683)
  AUTHORS   Motegi,A., Sood,R., Moinova,H., Markowitz,S.D., Liu,P.P. and
            Myung,K.
  TITLE     Human SHPRH suppresses genomic instability through proliferating
            cell nuclear antigen polyubiquitination
  JOURNAL   J Cell Biol 175 (5), 703-708 (2006)
   PUBMED   17130289
  REMARK    GeneRIF: We report that a putative tumor suppressor gene, SHPRH, is
            a human orthologue of yeast RAD5.The yRad5/SHPRH-dependent pathway
            is a conserved and fundamental DNA repair mechanism that protects
            the genome from genotoxic stress.
REFERENCE   9  (residues 1 to 1683)
  AUTHORS   Unk,I., Hajdu,I., Fatyol,K., Szakal,B., Blastyak,A., Bermudez,V.,
            Hurwitz,J., Prakash,L., Prakash,S. and Haracska,L.
  TITLE     Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
            polyubiquitylation of proliferating cell nuclear antigen
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18107-18112 (2006)
   PUBMED   17108083
  REMARK    GeneRIF: SHPRH function is an important deterrent to mutagenesis
            and carcinogenesis in humans
REFERENCE   10 (residues 1 to 1683)
  AUTHORS   Sood,R., Makalowska,I., Galdzicki,M., Hu,P., Eddings,E.,
            Robbins,C.M., Moses,T., Namkoong,J., Chen,S. and Trent,J.M.
  TITLE     Cloning and characterization of a novel gene, SHPRH, encoding a
            conserved putative protein with SNF2/helicase and PHD-finger
            domains from the 6q24 region
  JOURNAL   Genomics 82 (2), 153-161 (2003)
   PUBMED   12837266
  REMARK    GeneRIF: SHPRH maps to 6q24 and is a possible candidate for the
            tumor suppressor gene reported from that region.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL451145.15, AY163808.1, AY161136.1, BC117686.1, AK126959.1,
            AA315737.1 and BX648322.1.
            
            On Feb 24, 2010 this sequence version replaced NP_001036148.1.
            
            Summary: SHPRH is a ubiquitously expressed protein that contains
            motifs characteristics of several DNA repair proteins,
            transcription factors, and helicases. SHPRH is a functional homolog
            of S. cerevisiae RAD5 (Unk et al., 2006 [PubMed
            17108083]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC117686.1, AY161136.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000275233.12/ ENSP00000275233.7
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.3"
     Protein         1..1683
                     /product="E3 ubiquitin-protein ligase SHPRH isoform a"
                     /EC_number="2.3.2.27"
                     /note="2610103K11Rik; E3 ubiquitin-protein ligase SHPRH;
                     SNF2, histone-linker, PHD and RING finger
                     domain-containing helicase; SNF2 histone linker PHD RING
                     helicase, E3 ubiquitin protein ligase; RING-type E3
                     ubiquitin transferase SHPRH"
                     /calculated_mol_wt=192949
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          <298..>388
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          304..>409
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            375..381
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          440..508
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          525..607
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPQ3; propagated from
                     UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          660..706
                     /region_name="PHD_SHPRH"
                     /note="PHD finger found in E3 ubiquitin-protein ligase
                     SHPRH; cd15547"
                     /db_xref="CDD:277022"
     Site            order(660,673..677,681,701)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277022"
     Region          <702..903
                     /region_name="DEXQc_SHPRH"
                     /note="DEXQ-box helicase domain of SHPRH; cd18070"
                     /db_xref="CDD:350828"
     Region          819..822
                     /region_name="DEAQ box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          1429..1482
                     /region_name="RING-HC_SHPRH-like"
                     /note="RING finger, HC subclass, found in SNF2
                     histone-linker PHD finger RING finger helicase (SHPRH) and
                     similar proteins; cd16569"
                     /db_xref="CDD:438231"
     Region          1508..1633
                     /region_name="SF2_C_SNF"
                     /note="C-terminal helicase domain of the SNF family
                     helicases; cd18793"
                     /db_xref="CDD:350180"
     Site            order(1537..1538,1546,1585,1606..1607)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350180"
     Site            order(1591..1592,1594,1617,1620)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350180"
     CDS             1..1683
                     /gene="SHPRH"
                     /gene_synonym="bA545I5.2; RAD5"
                     /coded_by="NM_001042683.3:661..5712"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43513.2"
                     /db_xref="GeneID:257218"
                     /db_xref="HGNC:HGNC:19336"
                     /db_xref="MIM:608048"
ORIGIN      
        1 mssrrkrapp vrvdeekrqq lhwnmhedrr nepiiisddd eqpcpgsdts sahyiilsds
       61 lkeevahrdk krcskvvsfs kpiekeetvg ifsplsvkln ivispyhfdn swkaflgelt
      121 lqllpaqsli enfsersitl mssessnqfl iyvhskgedv ekqkkepmsi cdkgilvess
      181 fsgemledlg wlqkkrrikl yqkpegnhii kvgiylleag lakldflsda nsrmkkfnql
      241 mkkvmeklhn siipdvleed eddpesepeg qdidelyhfv kqthqqetqs iqvdvqhpal
      301 ipvlrpyqre avnwmlqqec frsspatesa lhflwreivt seglklyynp ytgciireyp
      361 nsgpqllggi lademglgkt vevlalilth trqdvkqdal tlpegkvvny fipshyfggk
      421 lkkteiqnie fepkekvqcp ptrvmiltav kemngkkgvs ilsiykyvss iyrydvqrnr
      481 sllkrmlkcl ifeglvkqik ghgfsgtftl gknykeedic dktkkqavgs prkiqketrk
      541 sgnkdtdsey lpsdtsdddd dpyyyyyksr rnrsklrkkl vpstkkgksq pfinpdsqgh
      601 cpatsdsgit dvamskstci sefnqehete dcaeslnhad sdvppsntms pfntsdyrfe
      661 cicgeldqid rkprvqclkc hlwqhakcvn ydeknlkikp fycphclvam epvstratli
      721 ispssichqw vdeinrhvrs sslrvlvyqg vkkdgflqph flaeqdivii tydvlrseln
      781 yvdiphsnse dgrrlrnqkr ymaipsplva vewwriclde aqmvecptvk aaemaqrlsg
      841 inrwcisgtp vqrgledlfg lvvflgiepy cvkhwwvrll yrpyckknpq hlysfiakil
      901 wrsakkdvid qiqippqtee ihwlhfspve rhfyhrqhev ccqdvvvklr kisdwalkls
      961 sldrrtvtsi lypllrlrqa cchpqavrge flplqkstmt meelltslqk kcgteceeah
     1021 rqlvcalngl agihiikgey alaaelyrev lrsseehkgk lktdslqrlh athnlmelli
     1081 arhpgipptl rdgrleeeak qlrehymskc ntevaeaqqa lypvqqtihe lqrkihsnsp
     1141 wwlnvihrai eftideelvq rvrneitsny kqqtgklsms ekfrdcrglq fllttqmeel
     1201 nkcqklvrea vknlegppsr nviesatvch lrparlplnc cvfckadelf teyesklfsn
     1261 tvkgqtaife emiedeeglv ddraptttrg lwaiseters mkailsfaks hrfdvefvde
     1321 gstsmdlfea wkkeykllhe ywmalrnrvs avdelamate rlrvrdprep kpnppvlhii
     1381 epheveqnri kllndkavat sqlqkklgql lyltnleksq dktsggvnpe pcpicarqlg
     1441 kqwavltcgh cfcnecisii ieqysvgshr ssikcaicrq ttshkeisyv ftsekanqee
     1501 dipvkgshst kveavvrtlm kiqlrdpgak alvfstwqdv ldiiskaltd nnmefaqisr
     1561 vktfqenlsa fkrdpqinil llplhtgsng ltiieathvl lvepilnpah elqaigrvhr
     1621 igqtkptivh rflikatiee rmqamlktae rshtnssakh seasvltvad ladlftkete
     1681 ele
//
LOCUS       NP_001124538             210 aa            linear   PRI 27-APR-2025
DEFINITION  Rieske domain-containing protein isoform 1 [Homo sapiens].
ACCESSION   NP_001124538
VERSION     NP_001124538.1
DBSOURCE    REFSEQ: accession NM_001131066.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Volik,S., Raphael,B.J., Huang,G., Stratton,M.R., Bignel,G.,
            Murnane,J., Brebner,J.H., Bajsarowicz,K., Paris,P.L., Tao,Q.,
            Kowbel,D., Lapuk,A., Shagin,D.A., Shagina,I.A., Gray,J.W.,
            Cheng,J.F., de Jong,P.J., Pevzner,P. and Collins,C.
  TITLE     Decoding the fine-scale structure of a breast cancer genome and
            transcriptome
  JOURNAL   Genome Res 16 (3), 394-404 (2006)
   PUBMED   16461635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN914641.1, BI551847.1, BC035110.2, BX114571.1 and AC008547.6.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 3 encode the same protein
            (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.478011.1,
                                           SRR1803614.78625.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380005.9/ ENSP00000369341.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q15"
     Protein         1..210
                     /product="Rieske domain-containing protein isoform 1"
                     /note="rieske domain-containing protein"
                     /calculated_mol_wt=23571
     Region          69..187
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
     CDS             1..210
                     /gene="RFESD"
                     /coded_by="NM_001131066.2:177..809"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47248.1"
                     /db_xref="GeneID:317671"
                     /db_xref="HGNC:HGNC:29587"
ORIGIN      
        1 mlkcfrnclr psslstlplq ygilfpklla clvhlhfghf ssavisvtsf ylsmnldgsa
       61 qdpekreyss vcvgreddik ksermtavvh drevvifyhk geyhamdirc yhsggplhlg
      121 diedfdgrpc ivcpwhkyki tlatgeglyq sinpkdpsak pkwcskgikq rihtvtvdng
      181 niyvtlsnep fkcdsdfyat gdfkviksss
//
LOCUS       NP_078850                568 aa            linear   PRI 27-APR-2025
DEFINITION  protein NDNF precursor [Homo sapiens].
ACCESSION   NP_078850
VERSION     NP_078850.3
DBSOURCE    REFSEQ: accession NM_024574.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Liu,Y., Ren,J., Bai,R., He,S., Peng,Z., Yin,W., Guo,R., Niu,J.,
            Zhang,W., Xia,Z., Fan,X., Yang,K., Li,B., Yang,H., Song,H. and
            Xie,J.
  TITLE     Overexpression of NDNF Improves the Cytoprotective Effects of Aged
            Human Bone Marrow Mesenchymal Stem Cells by Modulating Oxidative
            Stress and Apoptosis
  JOURNAL   Stem Cells Dev 33 (15-16), 432-437 (2024)
   PUBMED   38801165
  REMARK    GeneRIF: Overexpression of NDNF Improves the Cytoprotective Effects
            of Aged Human Bone Marrow Mesenchymal Stem Cells by Modulating
            Oxidative Stress and Apoptosis.
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Yang,S., Wu,X., Daoutidou,E.I., Zhang,Y., Shimell,M., Chuang,K.H.,
            Peterson,A.J., O'Connor,M.B. and Zheng,X.
  TITLE     The NDNF-like factor Nord is a Hedgehog-induced extracellular BMP
            modulator that regulates Drosophila wing patterning and growth
  JOURNAL   Elife 11, e73357 (2022)
   PUBMED   35037619
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Messina,A., Pulli,K., Santini,S., Acierno,J., Kansakoski,J.,
            Cassatella,D., Xu,C., Casoni,F., Malone,S.A., Ternier,G., Conte,D.,
            Sidis,Y., Tommiska,J., Vaaralahti,K., Dwyer,A., Gothilf,Y.,
            Merlo,G.R., Santoni,F., Niederlander,N.J., Giacobini,P., Raivio,T.
            and Pitteloud,N.
  TITLE     Neuron-Derived Neurotrophic Factor Is Mutated in Congenital
            Hypogonadotropic Hypogonadism
  JOURNAL   Am J Hum Genet 106 (1), 58-70 (2020)
   PUBMED   31883645
  REMARK    GeneRIF: Neuron-Derived Neurotrophic Factor Is Mutated in
            Congenital Hypogonadotropic Hypogonadism.
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Zhang,Y., Wu,X., Kai,Y., Lee,C.H., Cheng,F., Li,Y., Zhuang,Y.,
            Ghaemmaghami,J., Chuang,K.H., Liu,Z., Meng,Y., Keswani,M.,
            Gough,N.R., Wu,X., Zhu,W., Tzatsos,A., Peng,W., Seto,E.,
            Sotomayor,E.M. and Zheng,X.
  TITLE     Secretome profiling identifies neuron-derived neurotrophic factor
            as a tumor-suppressive factor in lung cancer
  JOURNAL   JCI Insight 4 (24), 129344 (2019)
   PUBMED   31852841
  REMARK    GeneRIF: Secretome profiling identifies neuron-derived neurotrophic
            factor as a tumor-suppressive factor in lung cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Ohashi,K., Enomoto,T., Joki,Y., Shibata,R., Ogura,Y., Kataoka,Y.,
            Shimizu,Y., Kambara,T., Uemura,Y., Yuasa,D., Matsuo,K.,
            Hayakawa,S., Hiramatsu-Ito,M., Murohara,T. and Ouchi,N.
  TITLE     Neuron-derived neurotrophic factor functions as a novel modulator
            that enhances endothelial cell function and revascularization
            processes
  JOURNAL   J Biol Chem 289 (20), 14132-14144 (2014)
   PUBMED   24706764
  REMARK    GeneRIF: NDNF acts as an endogenous modulator that promotes
            endothelial cell function and ischemia-induced revascularization
            through eNOS-dependent mechanisms
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Kuang,X.L., Zhao,X.M., Xu,H.F., Shi,Y.Y., Deng,J.B. and Sun,G.T.
  TITLE     Spatio-temporal expression of a novel neuron-derived neurotrophic
            factor (NDNF) in mouse brains during development
  JOURNAL   BMC Neurosci 11, 137 (2010)
   PUBMED   20969804
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 568)
  AUTHORS   Kalsi,G., Kuo,P.H., Aliev,F., Alexander,J., McMichael,O.,
            Patterson,D.G., Walsh,D., Zhao,Z., Schuckit,M., Nurnberger,J. Jr.,
            Edenberg,H., Kramer,J., Hesselbrock,V., Tischfield,J.A.,
            Vladimirov,V., Prescott,C.A., Dick,D.M., Kendler,K.S. and
            Riley,B.P.
  TITLE     A systematic gene-based screen of chr4q22-q32 identifies
            association of a novel susceptibility gene, DKK2, with the
            quantitative trait of alcohol dependence symptom counts
  JOURNAL   Hum Mol Genet 19 (12), 2497-2506 (2010)
   PUBMED   20332099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Erratum:[Hum Mol Genet. 2010 Oct 15;19(20):4121. Hesselbrock,
            Victor [added]; Tischfield, Jay A [added]]
REFERENCE   8  (residues 1 to 568)
  AUTHORS   Utine,G.E. and Aktas,D.
  TITLE     Mosaicism for terminal deletion of 4q
  JOURNAL   Genet Couns 17 (2), 205-209 (2006)
   PUBMED   16970039
  REMARK    GeneRIF: direct duplication of chromosome 4q27q31.3 de novo results
            in partial trisomy of its long arm.
REFERENCE   9  (residues 1 to 568)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC105254.3, BX359842.2, BC019351.1, AY358821.1, DA807168.1 and
            AK026844.1.
            
            On Jun 29, 2006 this sequence version replaced NP_078850.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC019351.1, SRR1803615.220308.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379692.9/ ENSP00000369014.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q27"
     Protein         1..568
                     /product="protein NDNF precursor"
                     /note="fibronectin type-III domain-containing protein
                     C4orf31; protein NDNF"
                     /calculated_mol_wt=62362
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2329
     mat_peptide     20..568
                     /product="Protein NDNF. /id=PRO_0000301965"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TB73.2)"
                     /calculated_mol_wt=62362
     Region          192..335
                     /region_name="NDNF"
                     /note="Neuron-derived neurotrophic factor, first Fn(III)
                     domain; pfam10179"
                     /db_xref="CDD:462981"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TB73.2)"
     Region          394..568
                     /region_name="NDNF_C"
                     /note="Neuron-derived Neurotrophic Factor C-terminal;
                     pfam19433"
                     /db_xref="CDD:466079"
     CDS             1..568
                     /gene="NDNF"
                     /gene_synonym="C4orf31; HH25; NORD"
                     /coded_by="NM_024574.4:545..2251"
                     /db_xref="CCDS:CCDS3717.2"
                     /db_xref="GeneID:79625"
                     /db_xref="HGNC:HGNC:26256"
                     /db_xref="MIM:616506"
ORIGIN      
        1 mvllhwcllw llfplssrtq klptrdeelf qmqirdkaff hdssvipdga eissylfrdt
       61 pkryffvvee dntplsvtvt pcdaplewkl slqelpedrs gegsgdlepl eqqkqqiine
      121 egtelfsykg ndveyfisss spsglyqldl lstekdthfk vyatttpesd qpypelpydp
      181 rvdvtslgrt tvtlawkpsp tasllkqpiq ycvvinkehn fkslcaveak lsaddafmma
      241 pkpgldfspf dfahfgfpsd nsgkersfqa kpspklgrhv ysrpkvdiqk icignknift
      301 vsdlkpdtqy yfdvfvvnin snmstayvgt fartkeeakq ktvelkdgki tdvfvkrkga
      361 kflrfapvss hqkvtffihs cldavqiqvr rdgklllsqn vegiqqfqlr gkpkakylvr
      421 lkgnkkgasm lkilattrpt kqsfpslped trikafdklr tcssatvawl gtqernkfci
      481 ykkevddnyn edqkkreqnq clgpdirkks ekvlckyfhs qnlqkavtte tikglqpgks
      541 ylldvyvigh gghsvkyqsk vvktrkfc
//
LOCUS       NP_203752               1861 aa            linear   PRI 27-APR-2025
DEFINITION  protein TANC1 isoform 1 [Homo sapiens].
ACCESSION   NP_203752 XP_043492
VERSION     NP_203752.2
DBSOURCE    REFSEQ: accession NM_033394.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1861)
  AUTHORS   Wu,D., Li,Y., Ren,Q., Pei,S., Wang,L., Yang,L., Chong,Y., Sun,S.,
            Hao,J. and Feng,F.
  TITLE     TANC1 methylation as a novel biomarker for the diagnosis of
            patients with anti-tuberculosis drug-induced liver injury
  JOURNAL   Sci Rep 11 (1), 17423 (2021)
   PUBMED   34465797
  REMARK    GeneRIF: TANC1 methylation as a novel biomarker for the diagnosis
            of patients with anti-tuberculosis drug-induced liver injury.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1861)
  AUTHORS   Yang,Q., Liu,H., Li,Z., Wang,Y. and Liu,W.
  TITLE     Purification and mutagenesis studies of TANC1 ankyrin repeats
            domain provide clues to understand mis-sense variants from diseases
  JOURNAL   Biochem Biophys Res Commun 514 (2), 358-364 (2019)
   PUBMED   31040020
  REMARK    GeneRIF: mis-sense variants tested in this study may either affect
            protein folding or disrupt the interaction between TANC1/2 AR
            domains and their binding partners
REFERENCE   3  (residues 1 to 1861)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1861)
  AUTHORS   Fachal,L., Gomez-Caamano,A., Barnett,G.C., Peleteiro,P.,
            Carballo,A.M., Calvo-Crespo,P., Kerns,S.L., Sanchez-Garcia,M.,
            Lobato-Busto,R., Dorling,L., Elliott,R.M., Dearnaley,D.P.,
            Sydes,M.R., Hall,E., Burnet,N.G., Carracedo,A., Rosenstein,B.S.,
            West,C.M., Dunning,A.M. and Vega,A.
  TITLE     A three-stage genome-wide association study identifies a
            susceptibility locus for late radiotherapy toxicity at 2q24.1
  JOURNAL   Nat Genet 46 (8), 891-894 (2014)
   PUBMED   24974847
REFERENCE   5  (residues 1 to 1861)
  AUTHORS   Avirneni-Vadlamudi,U., Galindo,K.A., Endicott,T.R., Paulson,V.,
            Cameron,S. and Galindo,R.L.
  TITLE     Drosophila and mammalian models uncover a role for the myoblast
            fusion gene TANC1 in rhabdomyosarcoma
  JOURNAL   J Clin Invest 122 (1), 403-407 (2012)
   PUBMED   22182840
REFERENCE   6  (residues 1 to 1861)
  AUTHORS   Granot-Hershkovitz,E., Raas-Rothschild,A., Frumkin,A., Granot,D.,
            Silverstein,S. and Abeliovich,D.
  TITLE     Complex chromosomal rearrangement in a girl with
            psychomotor-retardation and a de novo inversion: inv(2)(p15;q24.2)
  JOURNAL   Am J Med Genet A 155A (8), 1825-1832 (2011)
   PUBMED   21739571
REFERENCE   7  (residues 1 to 1861)
  AUTHORS   Aouizerat,B.E., Vittinghoff,E., Musone,S.L., Pawlikowska,L.,
            Kwok,P.Y., Olgin,J.E. and Tseng,Z.H.
  TITLE     GWAS for discovery and replication of genetic loci associated with
            sudden cardiac arrest in patients with coronary artery disease
  JOURNAL   BMC Cardiovasc Disord 11, 29 (2011)
   PUBMED   21658281
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1861)
  AUTHORS   Suzuki,T., Li,W., Zhang,J.P., Tian,Q.B., Sakagami,H., Usuda,N.,
            Kondo,H., Fujii,T. and Endo,S.
  TITLE     A novel scaffold protein, TANC, possibly a rat homolog of
            Drosophila rolling pebbles (rols), forms a multiprotein complex
            with various postsynaptic density proteins
  JOURNAL   Eur J Neurosci 21 (2), 339-350 (2005)
   PUBMED   15673434
  REMARK    GeneRIF: Discusses cloning and expression of Rat TANC1 and
            preliminary cloning of human TANC1, which resulted in recovery of a
            partial cDNA.
            Erratum:[Eur J Neurosci. 2005 Feb;21(3):825. Usada, Nobuteru
            [corrected to Usuda, Nobuteru]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC037329.1, AK128859.1, AC009307.4, BC150597.1, BX648327.1 and
            AL833258.1.
            
            On Mar 21, 2009 this sequence version replaced NP_203752.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.84494.1,
                                           SRR1660805.205801.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263635.8/ ENSP00000263635.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.2"
     Protein         1..1861
                     /product="protein TANC1 isoform 1"
                     /note="rolling pebbles homolog B; TPR domain,
                     ankyrin-repeat and coiled-coil-containing; protein TANC1;
                     tetratricopeptide repeat, ankyrin repeat and coiled-coil
                     domain-containing protein 1"
                     /calculated_mol_wt=202089
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          63..99
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          206..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          257..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          439..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          <521..>822
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
     Region          896..928
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          934..963
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          939..965
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(940..941,944..946,948..949,953,956,965,967,969,
                     973..974,977..979,981..982,986,989,998,1000,1002,
                     1006..1007,1010..1012,1014..1015,1019)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          948..>1205
                     /region_name="PHA03100"
                     /note="ankyrin repeat protein; Provisional; cl39094"
                     /db_xref="CDD:476869"
     Region          967..998
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          967..996
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1000..1029
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1040..1069
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1078..1107
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1079..1285
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1079..1109
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1111..1140
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1115..1142
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1144..1173
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1145..1175
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1146,1150..1151,1154..1156,1158..1159,1163,1166,
                     1175,1177,1179,1183..1184,1187..1189,1191..1192,1196,1199,
                     1208,1210,1212,1216..1217,1220..1222,1224..1225,1229,1232,
                     1241)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1177..1208
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1177..1206
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1210..1241
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1210..1239
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1243..1272
                     /region_name="ANK 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1243..1268
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1273..>1410
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          1289..1322
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1292..1317
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(1293..1294,1297..1298,1300,1337,1340..1341,
                     1344..1345,1347..1348,1371,1374..1375,1378..1379,1382)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1335..1365
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1336..1369
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1370..1398
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1371..1403
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1421..1485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6F6B3; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1636..1696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1676
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q0VGY8; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q0VGY8; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     CDS             1..1861
                     /gene="TANC1"
                     /gene_synonym="ROLSB; TANC"
                     /coded_by="NM_033394.3:269..5854"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42766.1"
                     /db_xref="GeneID:85461"
                     /db_xref="HGNC:HGNC:29364"
                     /db_xref="MIM:611397"
ORIGIN      
        1 mlkavlkksr eggkggkkea gsdfgpetsp vlhldhsads pvsslptaed tyrvslakgv
       61 smslpsspll prqshlvqsr vnkkspgpvr kpkyvesprv pgdavimpfr evakptepde
      121 heakadneps cspaaqellt rlgfllgegi psathitied knetmctals qgispcstlt
      181 sstaspstds pcstlnscvs ktaankspce tisspsstle skdsgiiati tsssenddrs
      241 gsslewnkdg nlrlgvqkgv lhdrradncs pvaeeettgs aestlpkaes sagdgpvpys
      301 qgssslimpr pnsvaatsst kledlsyldg qrnaplrtsi rlpwhntagg raqevkarfa
      361 pykpqdillk pllfevpsit tdsvfvgrdw lfhqieenlr ntelaenrga vvvgnvgfgk
      421 taiisklval schgsrmrqi asnspgsspk tsdptqdlhf tpllspssst sasstaktpl
      481 gsisaenqrp redavkylas kvvayhycqa dntytclvpe fvhsiaallc rshqlaayrd
      541 llikepqlqs mlslrscvqd pvaafkrgvl epltnlrneq kipeeeyiil idglneaefh
      601 kpdygdtlss fitkiiskfp awlklivtvr anfqeiisal pfvklslddf pdnkdihsdl
      661 hayvqhrvhs sqdilsnisl ngkadatlig kvsshlvlrs lgsylylklt ldlfqrghlv
      721 iksasykvvp vslselyllq cnmkfmtqsa feralpilnv alaslhpmtd eqifqainag
      781 hiqgeqgwed fqqrmdalsc flikrrdktr mfchpsfrew lvwradgent aflceprngh
      841 allafmfsrq egklnrqqtm elghhilkah ifkglskktg issshlqalw igysteglsa
      901 alaslrnlyt pnvkvsrlli lgganvnyrt evlnnapilc vqshlgheev vtlllefgac
      961 ldgtsengmt alcyaaaagh mklvclltkk gvrvdhldkk gqcalvhsal rghgdilqyl
     1021 ltcewspgpp qpgtlrksha lqqaltaaas mghssvvqcl lgmekeheve vngtdtlwge
     1081 taltaaagrg klevcelllg hgaavsrtnr rgvpplfcaa rqghwqivrl llergcdvnl
     1141 sdkqgrtplm vaaceghlst vefllskgaa lssldkegls alswaclkgh ravvqylvee
     1201 gaaidqtdkn grtpldlaaf ygdaetvlyl vekgaviehv dhsgmrpldr aigcrntsvv
     1261 vallrkgakl gnaawamats kpdiliillq klmeegnvmy kkgkmkeaaq ryqyalrkfp
     1321 regfgedmrp fnelrvslyl nlsrcrrktn dfgmaeefas kalelkpksy eafyararak
     1381 rnsrqfvaal adlqeavklc ptnqevkrll arveeeckql qrsqqqkqqg plpaplndse
     1441 needtptpgl sdhfhseete eeetspqees vsptprsqps ssvpssyirn lqeglqskgr
     1501 pvspqsragi gkslrepvaq pglllqpskq aqivktsqhl gsgqsavrng smkvqissqn
     1561 pppspmpgri aatpagsrtq hlegtgtftt ragcghfgdr lgpsqnvrlq cgengpahpl
     1621 psktktterl lshssvavda appnqgglat csdvrhpasl tssgssgsps ssikmsssts
     1681 sltssssfsd gfkvqgpdtr ikdkvvthvq sgtaehrprn tpfmgimdkt arfqqqsnpp
     1741 srswhcpape glltntssaa glqsantekp slmqvggynn qaktcsvstl sasvhngaqv
     1801 keleeskcqi pvhsqenrit ktvshlyqes iskqqphisn eahrshltaa kpkrsfiesn
     1861 v
//
LOCUS       NP_115984                817 aa            linear   PRI 27-APR-2025
DEFINITION  neurabin-2 [Homo sapiens].
ACCESSION   NP_115984
VERSION     NP_115984.3
DBSOURCE    REFSEQ: accession NM_032595.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Verdugo-Sivianes,E.M., Rojas,A.M., Munoz-Galvan,S., Otero-Albiol,D.
            and Carnero,A.
  TITLE     Mutation of SPINOPHILIN (PPP1R9B) found in human tumors promotes
            the tumorigenic and stemness properties of cells
  JOURNAL   Theranostics 11 (7), 3452-3471 (2021)
   PUBMED   33537097
  REMARK    GeneRIF: Mutation of SPINOPHILIN (PPP1R9B) found in human tumors
            promotes the tumorigenic and stemness properties of cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Chen,Y., Booth,C., Wang,H., Wang,R.X., Terzi,D., Zachariou,V.,
            Jiao,K., Zhang,J. and Wang,Q.
  TITLE     Effective Attenuation of Adenosine A1R Signaling by Neurabin
            Requires Oligomerization of Neurabin
  JOURNAL   Mol Pharmacol 92 (6), 630-639 (2017)
   PUBMED   28954816
  REMARK    GeneRIF: homo-oligomerization of neurabin is required for
            stabilizing RGS4 on the plasma membrane to attenuate A1R signaling
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Hiday,A.C., Edler,M.C., Salek,A.B., Morris,C.W., Thang,M.,
            Rentz,T.J., Rose,K.L., Jones,L.M. and Baucum,A.J. 2nd.
  TITLE     Mechanisms and Consequences of Dopamine Depletion-Induced
            Attenuation of the Spinophilin/Neurofilament Medium Interaction
  JOURNAL   Neural Plast 2017, 4153076 (2017)
   PUBMED   28634551
  REMARK    GeneRIF: Study determined that spinophilin binding to neurofilament
            medium required overexpression of the catalytic subunit of protein
            kinase A and was decreased by cyclin-dependent protein kinase 5.
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Stephens,D.J. and Banting,G.
  TITLE     Direct interaction of the trans-Golgi network membrane protein,
            TGN38, with the F-actin binding protein, neurabin
  JOURNAL   J Biol Chem 274 (42), 30080-30086 (1999)
   PUBMED   10514494
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Smith,F.D., Oxford,G.S. and Milgram,S.L.
  TITLE     Association of the D2 dopamine receptor third cytoplasmic loop with
            spinophilin, a protein phosphatase-1-interacting protein
  JOURNAL   J Biol Chem 274 (28), 19894-19900 (1999)
   PUBMED   10391935
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Hsieh-Wilson,L.C., Allen,P.B., Watanabe,T., Nairn,A.C. and
            Greengard,P.
  TITLE     Characterization of the neuronal targeting protein spinophilin and
            its interactions with protein phosphatase-1
  JOURNAL   Biochemistry 38 (14), 4365-4373 (1999)
   PUBMED   10194355
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Burnett,P.E., Blackshaw,S., Lai,M.M., Qureshi,I.A., Burnett,A.F.,
            Sabatini,D.M. and Snyder,S.H.
  TITLE     Neurabin is a synaptic protein linking p70 S6 kinase and the
            neuronal cytoskeleton
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8351-8356 (1998)
   PUBMED   9653190
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Allen,P.B., Ouimet,C.C. and Greengard,P.
  TITLE     Spinophilin, a novel protein phosphatase 1 binding protein
            localized to dendritic spines
  JOURNAL   Proc Natl Acad Sci U S A 94 (18), 9956-9961 (1997)
   PUBMED   9275233
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002401.2, BF448737.1,
            AJ401189.1, ABBA01041227.1, AL713642.1 and BM991997.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 5, 2007 this sequence version replaced NP_115984.2.
            
            Summary: This gene encodes a scaffold protein that functions as a
            regulatory subunit of protein phosphatase 1a. Expression of this
            gene is particularly high in dendritic spines, suggesting that the
            encoded protein may play a role in receiving signals from the
            central nervous system. The encoded protein has putative tumor
            suppressor function and decreased expression has been observed in
            tumors. [provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL713642.1, SRR3476690.867667.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000612501.2/ ENSP00000478767.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..817
                     /product="neurabin-2"
                     /note="protein phosphatase 1, regulatory subunit 9B,
                     spinophilin; protein phosphatase 1, regulatory (inhibitor)
                     subunit 9B; neurabin-II"
                     /calculated_mol_wt=89203
     Region          1..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          1..154
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6R891; propagated from
                     UniProtKB/Swiss-Prot (Q96SB3.3)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6R891; propagated from
                     UniProtKB/Swiss-Prot (Q96SB3.3)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6R891; propagated from
                     UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          100..371
                     /region_name="Interaction with D(2) dopamine receptor.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35274; propagated from
                     UniProtKB/Swiss-Prot (Q96SB3.3)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35274; propagated from
                     UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          164..283
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          169..255
                     /region_name="Interaction with ADRA2A, ADRA2B and ADRA2C.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96SB3.3)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96SB3.3)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          216..447
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          417..494
                     /region_name="Interaction with protein phosphatase 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          426..489
                     /region_name="PDZ_5"
                     /note="PDZ domain; pfam17817"
                     /db_xref="CDD:465518"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          447..451
                     /region_name="PP1-binding motif.
                     /evidence=ECO:0000250|UniProtKB:O35274"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          480..525
                     /region_name="Interaction with RGS2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          493..582
                     /region_name="PDZ_neurabin-like"
                     /note="PDZ domain of neurabin-1 and neurabin-2, and
                     related domains; cd06790"
                     /db_xref="CDD:467252"
     Site            order(505..511,529,532,562,566,569..570)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467252"
     Region          595..816
                     /region_name="Interaction with TGN38.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SB3.3)"
     Region          651..>813
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96SB3.3)"
     CDS             1..817
                     /gene="PPP1R9B"
                     /gene_synonym="PPP1R6; PPP1R9; SPINO; Spn"
                     /coded_by="NM_032595.5:165..2618"
                     /db_xref="CCDS:CCDS74102.1"
                     /db_xref="GeneID:84687"
                     /db_xref="HGNC:HGNC:9298"
                     /db_xref="MIM:603325"
ORIGIN      
        1 mmkteprgpg gplrsasphr sayeagiqal kppdapgpde apkgahhkky gsnvhriksm
       61 flqmgttagp sgeagggagl aeapraserg vrlslprass lnenvdhsal lklgtsvser
      121 vsrfdskpap saqpappphp psrlqetrkl fersapaaag gdkeaaarrl lrqeraglqd
      181 rkldvvvrfn gstealdkld adavsptvsq lsavfekads rtglhrgpgl praagvpqvn
      241 sklvskrsrv fqpppppppa psgdapaeke rcpagqqppq hrvaparppp kprevrkikp
      301 veveesgese aesapgeviq aevtvhaale ngstvataas papeepkaqa apekeaaava
      361 ppergvgngr apdvapeevd eskkedfsea dlvdvsaysg lgedsagsal eeddeddeed
      421 geppyepesg cveipglsee edpapsrkih fstapiqvfs tysnedydrr nedvdpmaas
      481 aeyelekrve rlelfpvele kdseglgisi igmgagadmg leklgifvkt vteggaahrd
      541 griqvndllv evdgtslvgv tqsfaasvlr ntkgrvrfmi grerpgeqse vaqliqqtle
      601 qerwqremme qryaqygedd eetgeyatde deelsptfpg gemaievfel aenedalspv
      661 dmepeklvhk fkelqikhav teaeiqqlkr klqsleqekg rwrvekaqle qsveenkerm
      721 eklegywgea qslcqavdeh lretqaqyqa lerkyskakr likdyqqkei eflkketaqr
      781 rvleeselar keemdklldk iselegnlqt lrnsnst
//
LOCUS       NP_001357555             215 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 267 [Mus musculus].
ACCESSION   NP_001357555
VERSION     NP_001357555.1
DBSOURCE    REFSEQ: accession NM_001370626.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Cajigas,I., Chakraborty,A., Swyter,K.R., Luo,H., Bastidas,M.,
            Nigro,M., Morris,E.R., Chen,S., VanGompel,M.J.W., Leib,D.,
            Kohtz,S.J., Martina,M., Koh,S., Ay,F. and Kohtz,J.D.
  TITLE     The Evf2 Ultraconserved Enhancer lncRNA Functionally and Spatially
            Organizes Megabase Distant Genes in the Developing Forebrain
  JOURNAL   Mol Cell 71 (6), 956-972 (2018)
   PUBMED   30146317
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC163689.3 and AC241593.3.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 4. All four variants encode the same protein.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN00849374, SAMN00849375
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 67.25 cM"
     Protein         1..215
                     /product="transmembrane protein 267"
                     /note="transmembrane protein C5orf28 homolog"
                     /calculated_mol_wt=24021
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDR5.1)"
     Site            114..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDR5.1)"
     Site            178..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDR5.1)"
     CDS             1..215
                     /gene="Tmem267"
                     /gene_synonym="EG633640; Gm7120"
                     /coded_by="NM_001370626.1:593..1240"
                     /db_xref="GeneID:633640"
                     /db_xref="MGI:MGI:3648543"
ORIGIN      
        1 maskvektha lppccstesl issiglgifc lvadrllrfp iiqhndwlra isdnivhgvi
       61 gmwswavvtg irkksdfgev llagflasvi dvdhffqars lslqaaltlp rrpflhcstv
      121 ipiavlsvkl avhlfklrds wrflpwmilv swtshhirdg irhglwicpf gktpplpssf
      181 yvistlslph lcsflmyltg trqtvsskyg mridv
//
LOCUS       NP_060926                260 aa            linear   PRI 27-APR-2025
DEFINITION  ELL-associated factor 2 isoform 1 [Homo sapiens].
ACCESSION   NP_060926
VERSION     NP_060926.2
DBSOURCE    REFSEQ: accession NM_018456.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Feng,M.L., Sun,M.J., Xu,B.Y., Liu,M.Y., Zhang,H.J. and Wu,C.
  TITLE     Mechanism of ELL-associated factor 2 and vasohibin 1 regulating
            invasion, migration, and angiogenesis in colorectal cancer
  JOURNAL   World J Gastroenterol 29 (24), 3770-3792 (2023)
   PUBMED   37426316
  REMARK    GeneRIF: Mechanism of ELL-associated factor 2 and vasohibin 1
            regulating invasion, migration, and angiogenesis in colorectal
            cancer.
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Zhao,C.X., Yan,Z.X., Wen,J.J., Fu,D., Xu,P.P., Wang,L., Cheng,S.,
            Hu,J.D. and Zhao,W.L.
  TITLE     CircEAF2 counteracts Epstein-Barr virus-positive diffuse large
            B-cell lymphoma progression via miR-BART19-3p/APC/beta-catenin axis
  JOURNAL   Mol Cancer 20 (1), 153 (2021)
   PUBMED   34852843
  REMARK    GeneRIF: CircEAF2 counteracts Epstein-Barr virus-positive diffuse
            large B-cell lymphoma progression via
            miR-BART19-3p/APC/beta-catenin axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Han,W. and Shen,G.L.
  TITLE     Systematic expression analysis of EAF family reveals the importance
            of EAF2 in melanoma
  JOURNAL   Int Immunopharmacol 88, 106958 (2020)
   PUBMED   33182068
  REMARK    GeneRIF: Systematic expression analysis of EAF family reveals the
            importance of EAF2 in melanoma.
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Liu,R., Chen,C., Li,Y., Huang,Q. and Xue,Y.
  TITLE     ELL-associated factors EAF1/2 negatively regulate HIV-1
            transcription through inhibition of Super Elongation Complex
            formation
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1863 (5), 194508 (2020)
   PUBMED   32087315
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Xiao,W., Jiang,F. and Wang,Z.
  TITLE     ELL binding regulates U19/Eaf2 intracellular localization,
            stability, and transactivation
  JOURNAL   Prostate 66 (1), 1-12 (2006)
   PUBMED   16114057
  REMARK    GeneRIF: ELL may be an important factor required for U19/Eaf2
            function because U19/Eaf2 nuclear localization and transactivation
            activity are essential for its function as a transcription factor.
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Kong,S.E., Banks,C.A., Shilatifard,A., Conaway,J.W. and
            Conaway,R.C.
  TITLE     ELL-associated factors 1 and 2 are positive regulators of RNA
            polymerase II elongation factor ELL
  JOURNAL   Proc Natl Acad Sci U S A 102 (29), 10094-10098 (2005)
   PUBMED   16006523
  REMARK    GeneRIF: ELL-associated factors 1 and 2 are positive regulators of
            RNA polymerase II elongation factor ELL.
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Xiao,W., Zhang,Q., Jiang,F., Pins,M., Kozlowski,J.M. and Wang,Z.
  TITLE     Suppression of prostate tumor growth by U19, a novel
            testosterone-regulated apoptosis inducer
  JOURNAL   Cancer Res 63 (15), 4698-4704 (2003)
   PUBMED   12907652
  REMARK    GeneRIF: U19 is growth inhibitory and tumor suppressive and that
            the disruption of androgen-dependent growth inhibition via U19
            down-regulation is commonly associated with prostate cancer
            progression.
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Saso,K., Ito,T., Natori,S. and Sekimizu,K.
  TITLE     Identification of a novel tissue-specific transcriptional activator
            FESTA as a protein that interacts with the transcription elongation
            factor S-II
  JOURNAL   J Biochem 133 (4), 493-500 (2003)
   PUBMED   12761297
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Simone,F., Luo,R.T., Polak,P.E., Kaberlein,J.J. and Thirman,M.J.
  TITLE     ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with
            alternative ELL binding properties
  JOURNAL   Blood 101 (6), 2355-2362 (2003)
   PUBMED   12446457
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY005912.1 and AY049020.1.
            
            On Jun 10, 2002 this sequence version replaced NP_060926.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.47926.1,
                                           SRR5189667.268300.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000273668.7/ ENSP00000273668.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.33"
     Protein         1..260
                     /product="ELL-associated factor 2 isoform 1"
                     /note="testosterone-regulated apoptosis inducer and tumor
                     suppressor protein"
                     /calculated_mol_wt=28661
     Region          17..113
                     /region_name="EAF"
                     /note="RNA polymerase II transcription elongation factor;
                     pfam09816"
                     /db_xref="CDD:462913"
     Region          17..104
                     /region_name="Necessary for interaction with ELL.
                     /evidence=ECO:0000269|PubMed:12446457"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CJ1.1)"
     Region          116..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CJ1.1)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96CJ1.1)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96CJ1.1)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96CJ1.1)"
     Region          170..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CJ1.1)"
     Region          177..260
                     /region_name="Necessary for transactivation activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CJ1.1)"
     Region          246..260
                     /region_name="Necessary for interaction with TCEA1 and
                     transactivation activity. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CJ1.1)"
     CDS             1..260
                     /gene="EAF2"
                     /gene_synonym="BM040; TRAITS; U19"
                     /coded_by="NM_018456.6:78..860"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3006.1"
                     /db_xref="GeneID:55840"
                     /db_xref="HGNC:HGNC:23115"
                     /db_xref="MIM:607659"
ORIGIN      
        1 mnsaagfshl drrervlklg esfekqprca fhtvrydfkp asidtssegy levgegeqvt
       61 itlpniegst ppvtvfkgsk kpylkecili inhdtgecrl eklssnitvk ktrvegsski
      121 qyrkeqqqqq mwnsartpnl vkhspsedkm spaspiddie relkaeaslm dqmsscdsss
      181 dsksssssss edsssdsede dcksstsdtg ncvsghptmt qyripdidas hnrfrdnsgl
      241 lmntlrndlq lsesgsdsdd
//
LOCUS       NP_115540                561 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 394 isoform 1 [Homo sapiens].
ACCESSION   NP_115540
VERSION     NP_115540.2
DBSOURCE    REFSEQ: accession NM_032164.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Huang,C., Wang,Y., Li,D., Li,Y., Luo,J., Yuan,W., Ou,Y., Zhu,C.,
            Zhang,Y., Wang,Z., Liu,M. and Wu,X.
  TITLE     Inhibition of transcriptional activities of AP-1 and c-Jun by a new
            zinc finger protein ZNF394
  JOURNAL   Biochem Biophys Res Commun 320 (4), 1298-1305 (2004)
   PUBMED   15249231
  REMARK    GeneRIF: Overexpression of ZNF394 in the cell inhibits the
            transcriptional activities of c-Jun and AP-1 reporters.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA962329.1 and BC051847.1.
            
            On Jun 19, 2003 this sequence version replaced NP_115540.1.
            
            Summary: The protein encoded by this gene is a zinc finger protein
            that inhibits the transcription of mitogen-activated protein kinase
            signaling pathways. The encoded protein may be involved in cardiac
            function. [provided by RefSeq, Sep 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022360.1, SRR3476690.169910.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337673.7/ ENSP00000337363.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..561
                     /product="zinc finger protein 394 isoform 1"
                     /note="zinc finger protein 99; zinc finger protein with
                     KRAB and SCAN domains 14"
                     /calculated_mol_wt=64125
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GI3.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53GI3.2)"
     Region          60..170
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          155..214
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          182..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GI3.2)"
     Region          231..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GI3.2)"
     Region          337..353
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          356..>420
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          360..380
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(365,367,369,371..372,375..376,379,393,395,399..400,
                     403..404,407,421,423,425,427..428,431..432,435)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          388..408
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          414..436
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          416..436
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          444..463
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <464..543
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          471..491
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(476,478,480,482..483,486..487,490,504,506,510..511,
                     514..515,518,532,534,536,538..539,542..543,546)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          499..519
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          527..547
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..561
                     /gene="ZNF394"
                     /gene_synonym="ZKSCAN14; ZSCAN46"
                     /coded_by="NM_032164.4:189..1874"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5666.1"
                     /db_xref="GeneID:84124"
                     /db_xref="HGNC:HGNC:18832"
                     /db_xref="MIM:619300"
ORIGIN      
        1 mnssltaqrr gsdaelgpwv maarskdaap sqrdgllpvk veedspgswe pnypaaspdp
       61 etsrlhfrql ryqevagpee alsrlrelcr rwlrpellsk eqilellvle qfltilpeel
      121 qawvrehcpe sgeeavavvr alqraldgts sqgmvtfedt avsltweewe rldparrdfc
      181 resaqkdsgs tvppslesrv enkelipmqq ileeaepqgq lqeafqgkrp lfskcgsthe
      241 drvekqsgdp lplklenspe aeglnsisdv nkngsieged sknnelqnsa rcsnlvlcqh
      301 ipkaerptds eehgnkckqs fhmvtwhvlk phksdsgdsf hhsslfetqr qlheerpykc
      361 gncgksfkqr sdlfrhqrih tgekpygcqe cgksfsqsaa ltkhqrthtg ekpytclkcg
      421 erfrqnshln rhqsthsrdk hfkceecget chisnlfrhq rlhkgerpyk ceeceksfkq
      481 rsdlfkhhri htgekpygcs vcgkrfnqsa tlikhqriht gekpykclec gerfrqsthl
      541 irhqrihqnk vlsagrggsr l
//
LOCUS       NP_002563                229 aa            linear   PRI 27-APR-2025
DEFINITION  platelet-activating factor acetylhydrolase IB subunit alpha2
            isoform a [Homo sapiens].
ACCESSION   NP_002563
VERSION     NP_002563.1
DBSOURCE    REFSEQ: accession NM_002572.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Tanigawa,K., Kiriya,M., Hayashi,Y., Shinden,Y., Kijima,Y.,
            Natsugoe,S., Sumimoto,T., Morimoto-Kamata,R., Yui,S., Hama,K.,
            Yokoyama,K., Nakamura,Y., Suzuki,K., Nojiri,H., Inoue,K. and
            Karasawa,K.
  TITLE     Cathepsin G-induced malignant progression of MCF-7 cells involves
            suppression of PAF signaling through induced expression of PAFAH1B2
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1867 (8), 159164 (2022)
   PUBMED   35462067
  REMARK    GeneRIF: Cathepsin G-induced malignant progression of MCF-7 cells
            involves suppression of PAF signaling through induced expression of
            PAFAH1B2.
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Ma,C., Guo,Y., Zhang,Y., Duo,A., Jia,Y., Liu,C. and Li,B.
  TITLE     PAFAH1B2 is a HIF1a target gene and promotes metastasis in
            pancreatic cancer
  JOURNAL   Biochem Biophys Res Commun 501 (3), 654-660 (2018)
   PUBMED   29758199
  REMARK    GeneRIF: PAFAH1B2 overexpression in pancreatic ductal
            adenocarcinoma cells was directly mediated by HIF1a.
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Scott,B.T., Olson,N., Long,G.L. and Bovill,E.G.
  TITLE     Novel isoforms of intracellular platelet activating factor
            acetylhydrolase (PAFAH1b2) in human testis; encoded by
            alternatively spliced mRNAs
  JOURNAL   Prostaglandins Other Lipid Mediat 85 (3-4), 69-80 (2008)
   PUBMED   18155631
  REMARK    GeneRIF: splice variants of the Pafah1b2 gene transcript retain
            exons 1-5 and replace exon 6 with alternative exons derived from
            genomic sequence 3' to exon 6. Splice variants encode two proteins
            with different novel carboxy termini
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Sweeney,K.J., Clark,G.D., Prokscha,A., Dobyns,W.B. and Eichele,G.
  TITLE     Lissencephaly associated mutations suggest a requirement for the
            PAFAH1B heterotrimeric complex in brain development
  JOURNAL   Mech Dev 92 (2), 263-271 (2000)
   PUBMED   10727864
REFERENCE   8  (residues 1 to 229)
  AUTHORS   Moro,F., Arrigo,G., Fogli,A., Bernard,L. and Carrozzo,R.
  TITLE     The beta and gamma subunits of the human platelet-activating factor
            acetyl hydrolase isoform Ib (PAFAH1B2 and PAFAH1B3) map to
            chromosome 11q23 and 19q13.1, respectively
  JOURNAL   Genomics 51 (1), 157-159 (1998)
   PUBMED   9693049
REFERENCE   9  (residues 1 to 229)
  AUTHORS   Adachi,H., Tsujimoto,M., Hattori,M., Arai,H. and Inoue,K.
  TITLE     Differential tissue distribution of the beta- and gamma-subunits of
            human cytosolic platelet-activating factor acetylhydrolase (isoform
            I)
  JOURNAL   Biochem Biophys Res Commun 233 (1), 10-13 (1997)
   PUBMED   9144386
REFERENCE   10 (residues 1 to 229)
  AUTHORS   Albrecht,U., Abu-Issa,R., Ratz,B., Hattori,M., Aoki,J., Arai,H.,
            Inoue,K. and Eichele,G.
  TITLE     Platelet-activating factor acetylhydrolase expression and activity
            suggest a link between neuronal migration and platelet-activating
            factor
  JOURNAL   Dev Biol 180 (2), 579-593 (1996)
   PUBMED   8954729
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP005018.1, D63390.1 and DQ836743.1.
            
            Summary: Platelet-activating factor acetylhydrolase (PAFAH)
            inactivates platelet-activating factor (PAF) into acetate and
            LYSO-PAF. This gene encodes the beta subunit of PAFAH, the other
            subunits are alpha and gamma. Multiple alternatively spliced
            transcript variants have been described for this gene. [provided by
            RefSeq, Jan 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and it encodes the longest protein (isoform a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ836743.1, SRR3476690.714208.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000527958.6/ ENSP00000435289.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..229
                     /product="platelet-activating factor acetylhydrolase IB
                     subunit alpha2 isoform a"
                     /EC_number="3.1.1.47"
                     /note="PAF-AH1b alpha 2 subunit; epididymis secretory
                     protein Li 303; intracellular platelet-activating factor
                     acetylhydrolase alpha 2 subunit; platelet-activating
                     factor acetylhydrolase IB subunit beta; PAFAH subunit
                     beta; PAF-AH subunit beta; PAF-AH 30 kDa subunit; PAF
                     acetylhydrolase 30 kDa subunit; platelet-activating factor
                     acetylhydrolase 1b, catalytic subunit 2 (30kDa);
                     epididymis secretory sperm binding protein;
                     platelet-activating factor acetylhydrolase IB subunit
                     alpha2"
                     /calculated_mol_wt=25438
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P68402.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P68402.1)"
     Region          8..217
                     /region_name="PAF_acetylesterase_like"
                     /note="PAF_acetylhydrolase (PAF-AH)_like subfamily of
                     SGNH-hydrolases. Platelet-activating factor (PAF) and
                     PAF-AH are key players in inflammation and in
                     atherosclerosis. PAF-AH is a calcium independent
                     phospholipase A2 which exhibits strong substrate...;
                     cd01820"
                     /db_xref="CDD:238858"
     Site            order(48,75,105,193,196)
                     /site_type="active"
                     /db_xref="CDD:238858"
     Site            order(48,193,196)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238858"
     Site            order(48,75,105)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238858"
     Site            order(49,104,195)
                     /site_type="active"
                     /note="specificity pocket [active]"
                     /db_xref="CDD:238858"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P68402.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q61206; propagated from
                     UniProtKB/Swiss-Prot (P68402.1)"
     CDS             1..229
                     /gene="PAFAH1B2"
                     /gene_synonym="HEL-S-303"
                     /coded_by="NM_002572.4:140..829"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8380.1"
                     /db_xref="GeneID:5049"
                     /db_xref="HGNC:HGNC:8575"
                     /db_xref="MIM:602508"
ORIGIN      
        1 msqgdsnpaa iphaaediqg ddrwmsqhnr fvldckdkep dvlfvgdsmv qlmqqyeiwr
       61 elfsplhaln fgiggdttrh vlwrlkngel enikpkvivv wvgtnnhent aeevaggiea
      121 ivqlintrqp qakiivlgll prgekpnplr qknakvnqll kvslpklanv qlldtdggfv
      181 hsdgaischd mfdflhltgg gyakickplh elimqlleet peekqttia
//
LOCUS       NP_054899                206 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein uL22m isoform a [Homo sapiens].
ACCESSION   NP_054899
VERSION     NP_054899.2
DBSOURCE    REFSEQ: accession NM_014180.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   7  (residues 1 to 206)
  AUTHORS   O'Brien,T.W.
  TITLE     Evolution of a protein-rich mitochondrial ribosome: implications
            for human genetic disease
  JOURNAL   Gene 286 (1), 73-79 (2002)
   PUBMED   11943462
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Koc,E.C., Burkhart,W., Blackburn,K., Moyer,M.B., Schlatzer,D.M.,
            Moseley,A. and Spremulli,L.L.
  TITLE     The large subunit of the mammalian mitochondrial ribosome. Analysis
            of the complement of ribosomal proteins present
  JOURNAL   J Biol Chem 276 (47), 43958-43969 (2001)
   PUBMED   11551941
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Goldschmidt-Reisin,S., Kitakawa,M., Herfurth,E.,
            Wittmann-Liebold,B., Grohmann,L. and Graack,H.R.
  TITLE     Mammalian mitochondrial ribosomal proteins. N-terminal amino acid
            sequencing, characterization, and identification of corresponding
            gene sequences
  JOURNAL   J Biol Chem 273 (52), 34828-34836 (1998)
   PUBMED   9857009
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP372420.1, AK000601.1,
            AC008410.6 and CR933679.1.
            
            On May 30, 2002 this sequence version replaced NP_054899.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein that belongs to
            the L22 ribosomal protein family. A pseudogene corresponding to
            this gene is found on chromosome 4q. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.267279.1,
                                           SRR1803611.38860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000523037.6/
                                                  ENSP00000431040.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.2"
     Protein         1..206
                     /product="large ribosomal subunit protein uL22m isoform a"
                     /note="39S ribosomal protein L22, mitochondrial; L25mt;
                     39S ribosomal protein L25, mitochondrial; mitochondrial
                     large ribosomal subunit protein uL22m"
                     /calculated_mol_wt=23510
     Region          69..172
                     /region_name="Ribosomal_L22"
                     /note="Ribosomal protein L22p/L17e; pfam00237"
                     /db_xref="CDD:459725"
     CDS             1..206
                     /gene="MRPL22"
                     /gene_synonym="HSPC158; L22mt; MRP-L22; MRP-L25; RPML25;
                     uL22m"
                     /coded_by="NM_014180.4:39..659"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4331.1"
                     /db_xref="GeneID:29093"
                     /db_xref="HGNC:HGNC:14480"
                     /db_xref="MIM:611835"
ORIGIN      
        1 maaavlgqlg alwihnlrsr gklalgvlpq syihtsasld isrkwekknk ivyppqlpge
       61 prrpaeiyhc rrqikyskdk mwylaklirg msidqalaql efndkkgaki ikevlleaqd
      121 mavrdhnvef rsnlyiaest sgrgqclkri ryhgrgrfgi mekvychyfv klvegppppp
      181 eppktavaha keyiqqlrsr tivhtl
//
LOCUS       NP_079422                169 aa            linear   PRI 27-APR-2025
DEFINITION  N-alpha-acetyltransferase 50 isoform 1 [Homo sapiens].
ACCESSION   NP_079422
VERSION     NP_079422.1
DBSOURCE    REFSEQ: accession NM_025146.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Reddi,R., Saddanapu,V., Chinthapalli,D.K., Sankoju,P., Sripadi,P.
            and Addlagatta,A.
  TITLE     Human Naa50 Protein Displays Broad Substrate Specificity for
            Amino-terminal Acetylation: DETAILED STRUCTURAL AND BIOCHEMICAL
            ANALYSIS USING TETRAPEPTIDE LIBRARY
  JOURNAL   J Biol Chem 291 (39), 20530-20538 (2016)
   PUBMED   27484799
  REMARK    GeneRIF: Because Naa10 is reported to acetylate all amino termini
            that are devoid of methionine and Naa50 acetylates all other
            peptides that are followed by methionine
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Rong,Z., Ouyang,Z., Magin,R.S., Marmorstein,R. and Yu,H.
  TITLE     Opposing Functions of the N-terminal Acetyltransferases Naa50 and
            NatA in Sister-chromatid Cohesion
  JOURNAL   J Biol Chem 291 (36), 19079-19091 (2016)
   PUBMED   27422821
  REMARK    GeneRIF: co-depletion of NatA, a heterodimeric NAT complex that
            physically interacts with Naa50, rescues the sister-chromatid
            cohesion defects and the resulting mitotic arrest caused by Naa50
            depletion, indicating that NatA and Naa50 play antagonistic roles
            in cohesion.
REFERENCE   6  (residues 1 to 169)
  AUTHORS   Starheim,K.K., Gromyko,D., Evjenth,R., Ryningen,A., Varhaug,J.E.,
            Lillehaug,J.R. and Arnesen,T.
  TITLE     Knockdown of human N alpha-terminal acetyltransferase complex C
            leads to p53-dependent apoptosis and aberrant human Arl8b
            localization
  JOURNAL   Mol Cell Biol 29 (13), 3569-3581 (2009)
   PUBMED   19398576
  REMARK    GeneRIF: Data show that with MAK3 knockdown, p53 is stabilized and
            phosphorylated and there is a significant transcriptional
            activation of proapoptotic genes downstream of p53, and that
            localization of Arl8b is altered, suggesting that Arl8b is a Mak3
            substrate.
REFERENCE   7  (residues 1 to 169)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 169)
  AUTHORS   Hou,F., Chu,C.W., Kong,X., Yokomori,K. and Zou,H.
  TITLE     The acetyltransferase activity of San stabilizes the mitotic
            cohesin at the centromeres in a shugoshin-independent manner
  JOURNAL   J Cell Biol 177 (4), 587-597 (2007)
   PUBMED   17502424
  REMARK    GeneRIF: May be specifically required for the maintenance of
            centromeric cohesion in mitosis.
REFERENCE   9  (residues 1 to 169)
  AUTHORS   Arnesen,T., Anderson,D., Torsvik,J., Halseth,H.B., Varhaug,J.E. and
            Lillehaug,J.R.
  TITLE     Cloning and characterization of hNAT5/hSAN: an evolutionarily
            conserved component of the NatA protein N-alpha-acetyltransferase
            complex
  JOURNAL   Gene 371 (2), 291-295 (2006)
   PUBMED   16507339
  REMARK    GeneRIF: The first description of the human homologue of Nat5p/San,
            hNAT5, the third component of the human NatA
            N-alpha-acetyltransferase complex
REFERENCE   10 (residues 1 to 169)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM831426.1, BC012731.2, DB198553.1, DB096143.1, DA408894.1,
            DA599265.1, HX784836.1, AW954963.1, H15889.1, H39948.1, BX102492.1
            and AC108693.5.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023256.1, SRR1803612.19842.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000240922.8/ ENSP00000240922.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.31"
     Protein         1..169
                     /product="N-alpha-acetyltransferase 50 isoform 1"
                     /EC_number="2.3.1.258"
                     /note="N-acetyltransferase 5; N-acetyltransferase 13
                     (GCN5-related); N-acetyltransferase san homolog; natE
                     catalytic subunit; N-epsilon-acetyltransferase 50"
                     /calculated_mol_wt=19267
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Site            34
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; N6-acetyllysine, by
                     autocatalysis. /evidence=ECO:0000269|PubMed:19744929,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Site            37
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:19744929,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Region          57..155
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:19744929; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     CDS             1..169
                     /gene="NAA50"
                     /gene_synonym="hNaa50p; MAK3; NAT13; NAT13P; NAT5; NAT5P;
                     SAN"
                     /coded_by="NM_025146.4:301..810"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2975.1"
                     /db_xref="GeneID:80218"
                     /db_xref="HGNC:HGNC:29533"
                     /db_xref="MIM:610834"
ORIGIN      
        1 mkgsrielgd vtphnikqlk rlnqvifpvs yndkfykdvl evgelaklay fndiavgavc
       61 crvdhsqnqk rlyimtlgcl apyrrlgigt kmlnhvlnic ekdgtfdniy lhvqisnesa
      121 idfyrkfgfe iietkknyyk riepadahvl qknlkvpsgq nadvqktdn
//
LOCUS       NP_004539                172 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 [Homo
            sapiens].
ACCESSION   NP_004539
VERSION     NP_004539.1
DBSOURCE    REFSEQ: accession NM_004548.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Arroum,T., Borowski,M.T., Marx,N., Schmelter,F., Scholz,M.,
            Psathaki,O.E., Hippler,M., Enriquez,J.A. and Busch,K.B.
  TITLE     Loss of respiratory complex I subunit NDUFB10 affects complex I
            assembly and supercomplex formation
  JOURNAL   Biol Chem 404 (5), 399-415 (2023)
   PUBMED   36952351
  REMARK    GeneRIF: Loss of respiratory complex I subunit NDUFB10 affects
            complex I assembly and supercomplex formation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Yano,M., Terada,K. and Mori,M.
  TITLE     AIP is a mitochondrial import mediator that binds to both import
            receptor Tom20 and preproteins
  JOURNAL   J Cell Biol 163 (1), 45-56 (2003)
   PUBMED   14557246
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Daniels,R.J., Peden,J.F., Lloyd,C., Horsley,S.W., Clark,K.,
            Tufarelli,C., Kearney,L., Buckle,V.J., Doggett,N.A., Flint,J. and
            Higgs,D.R.
  TITLE     Sequence, structure and pathology of the fully annotated terminal 2
            Mb of the short arm of human chromosome 16
  JOURNAL   Hum Mol Genet 10 (4), 339-352 (2001)
   PUBMED   11157797
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Emahazion,T., Beskow,A., Gyllensten,U. and Brookes,A.J.
  TITLE     Intron based radiation hybrid mapping of 15 complex I genes of the
            human electron transport chain
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 115-119 (1998)
   PUBMED   9763677
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP319067.1 and BC005829.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF088991.1, SRR1163655.207088.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000268668.11/
                                                  ENSP00000268668.6
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..172
                     /product="NADH dehydrogenase [ubiquinone] 1 beta
                     subcomplex subunit 10"
                     /EC_number="7.1.1.2"
                     /note="complex I PDSW subunit; NADH ubiquinone
                     oxidoreductase PDSW subunit (RH 16p13.3); CI-PDSW; complex
                     I-PDSW; NADH-ubiquinone oxidoreductase PDSW subunit; NADH
                     dehydrogenase (ubiquinone) 1 beta subcomplex, 10, 22kDa"
                     /calculated_mol_wt=20646
     Region          36..161
                     /region_name="NDUFB10"
                     /note="NADH-ubiquinone oxidoreductase subunit 10;
                     pfam10249"
                     /db_xref="CDD:431170"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O96000.3)"
     CDS             1..172
                     /gene="NDUFB10"
                     /gene_synonym="MC1DN35; PDSW"
                     /coded_by="NM_004548.3:88..606"
                     /db_xref="CCDS:CCDS10451.1"
                     /db_xref="GeneID:4716"
                     /db_xref="HGNC:HGNC:7696"
                     /db_xref="MIM:603843"
ORIGIN      
        1 mpdswdkdvy pepprrtpvq pnpivymmka fdlivdrpvt lvrefierqh aknryyyyhr
       61 qyrrvpdite ckeedimcmy eaemqwkrdy kvdqeiinim qdrlkacqqr egqnyqqnci
      121 keveqftqva kayqdryqdl gayssarkcl akqrqrmlqe rkaakeaaaa ts
//
LOCUS       NP_005613                586 aa            linear   PRI 27-APR-2025
DEFINITION  acyl-coenzyme A synthetase ACSM3, mitochondrial isoform 1 [Homo
            sapiens].
ACCESSION   NP_005613
VERSION     NP_005613.2
DBSOURCE    REFSEQ: accession NM_005622.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Zhu,W., Wei,X. and Fang,M.
  TITLE     Acyl-CoA Medium-Chain Synthetase-3 (ACSM3) Is Regulated by Insulin
            Like Growth Factor 2 mRNA Binding Protein 3 (IGF2BP3) and Inhibits
            Proliferation, Motility and Stem Cell Properties of Breast Invasive
            Carcinoma
  JOURNAL   Ann Clin Lab Sci 53 (4), 539-547 (2023)
   PUBMED   37625834
  REMARK    GeneRIF: Acyl-CoA Medium-Chain Synthetase-3 (ACSM3) Is Regulated by
            Insulin Like Growth Factor 2 mRNA Binding Protein 3 (IGF2BP3) and
            Inhibits Proliferation, Motility and Stem Cell Properties of Breast
            Invasive Carcinoma.
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Yang,X., Wu,G., Zhang,Q., Chen,X., Li,J., Han,Q., Yang,L., Wang,C.,
            Huang,M., Li,Y., Chen,J., LiLi, Wang,H. and Liu,K.
  TITLE     ACSM3 suppresses the pathogenesis of high-grade serous ovarian
            carcinoma via promoting AMPK activity
  JOURNAL   Cell Oncol (Dordr) 45 (1), 151-161 (2022)
   PUBMED   35124784
  REMARK    GeneRIF: ACSM3 suppresses the pathogenesis of high-grade serous
            ovarian carcinoma via promoting AMPK activity.
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Gopal,R., Selvarasu,K., Pandian,P.P. and Ganesan,K.
  TITLE     Integrative transcriptome analysis of liver cancer profiles
            identifies upstream regulators and clinical significance of ACSM3
            gene expression
  JOURNAL   Cell Oncol (Dordr) 40 (3), 219-233 (2017)
   PUBMED   28390038
  REMARK    GeneRIF: Our data provide evidence for a differential expression
            and regulation of the ACSM3 gene in hepatocellular carcinoma
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Gumprecht,J., Zychma,M.J., Grzeszczak,W. and
            Zukowska-Szczechowska,E.
  CONSRTM   End-stage Renal Disease Study Group
  TITLE     Human SA gene Pst1 polymorphism and chronic renal failure: results
            of the family-based study
  JOURNAL   Nephrol Dial Transplant 16 (2), 387-390 (2001)
   PUBMED   11158418
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Nabika,T., Bonnardeaux,A., James,M., Julier,C., Jeunemaitre,X.,
            Corvol,P., Lathrop,M. and Soubrier,F.
  TITLE     Evaluation of the SA locus in human hypertension
  JOURNAL   Hypertension 25 (1), 6-13 (1995)
   PUBMED   7843754
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Samani,N.J., Whitmore,S.A., Kaiser,M.A., Harris,J., See,C.G.,
            Callen,D.F. and Lodwick,D.
  TITLE     Chromosomal assignment of the human SA gene to 16p13.11 and
            demonstration of its expression in the kidney
  JOURNAL   Biochem Biophys Res Commun 199 (2), 862-868 (1994)
   PUBMED   8135833
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Iwai,N., Ohmichi,N., Hanai,K., Nakamura,Y. and Kinoshita,M.
  TITLE     Human SA gene locus as a candidate locus for essential hypertension
  JOURNAL   Hypertension 23 (3), 375-380 (1994)
   PUBMED   7907320
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI770558.1, X80062.1, D16350.1, BU170035.1, BM828310.1 and
            AC004381.1.
            
            On Feb 13, 2004 this sequence version replaced NP_005613.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.169679.1,
                                           SRR5189661.67996.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000289416.10/ ENSP00000289416.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..586
                     /product="acyl-coenzyme A synthetase ACSM3, mitochondrial
                     isoform 1"
                     /EC_number="6.2.1.2"
                     /EC_number="6.2.1.17"
                     /note="SA (rat hypertension-associated) homolog;
                     acyl-coenzyme A synthetase ACSM3, mitochondrial; SA
                     hypertension-associated homolog; protein SA homolog;
                     butyrate--CoA ligase 3; butyryl-coenzyme A synthetase 3;
                     middle-chain acyl-CoA synthetase 3; propionate--CoA
                     ligase"
                     /calculated_mol_wt=63010
     transit_peptide 1..27
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q53FZ2.2)"
                     /calculated_mol_wt=3161
     mat_peptide     28..586
                     /product="Acyl-coenzyme A synthetase ACSM3, mitochondrial.
                     /id=PRO_0000306097"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53FZ2.2)"
                     /calculated_mol_wt=63010
     Region          54..583
                     /region_name="MACS_euk"
                     /note="Eukaryotic Medium-chain acyl-CoA synthetase (MACS
                     or ACSM); cd05928"
                     /db_xref="CDD:341251"
     Site            order(153,280..282,306,326,328,332,352..355,374..379,
                     382..383,398,461,473,476,482,484..487,516,547,552..553,
                     555,557)
                     /site_type="active"
                     /db_xref="CDD:341251"
     Site            157
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q3UNX5; propagated from
                     UniProtKB/Swiss-Prot (Q53FZ2.2)"
     Site            order(232,235..240,242..243)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341251"
     Site            order(276,328..329,332,352,484..486,547,553)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341251"
     Site            order(352..355,374..379,398,461,473,476,482,487)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341251"
     CDS             1..586
                     /gene="ACSM3"
                     /gene_synonym="SA; SAH"
                     /coded_by="NM_005622.4:164..1924"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10589.1"
                     /db_xref="GeneID:6296"
                     /db_xref="HGNC:HGNC:10522"
                     /db_xref="MIM:145505"
ORIGIN      
        1 mlarvtrkml rhakcfqrla ifgsvralhk dnrtatpqnf snyesmkqdf klgipeyfnf
       61 akdvldqwtd kekagkkpsn pafwwinrng eemrwsfeel gslsrkfani lseacslqrg
      121 drvililprv pewwlanvac lrtgtvlipg ttqltqkdil yrlqsskanc iitndvlapa
      181 vdavaskcen lhsklivsen sregwgnlke lmkhasdsht cvktkhneim aifftsgtsg
      241 ypkmtahths sfglglsvng rfwldltpsd vmwntsdtgw aksawssvfs pwiqgacvft
      301 hhlprfepts ilqtlskypi tvfcsaptvy rmlvqndits ykfkslkhcv sagepitpdv
      361 tekwrnktgl diyegygqte tvlicgnfkg mkikpgsmgk pspafdvkiv dvngnvlppg
      421 qegdigiqvl pnrpfglfth yvdnpsktas tlrgnfyitg drgymdkdgy fwfvaraddv
      481 ilssgyrigp fevenalneh psvaesavvs spdpirgevv kafvvlnpdy kshdqeqlik
      541 eiqehvkktt apykyprkve fiqelpktis gktkrnelrk kewkti
//
LOCUS       NP_005104                731 aa            linear   PRI 27-APR-2025
DEFINITION  golgin subfamily A member 5 [Homo sapiens].
ACCESSION   NP_005104
VERSION     NP_005104.4
DBSOURCE    REFSEQ: accession NM_005113.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Christian,J.G., Heymann,J., Paschen,S.A., Vier,J., Schauenburg,L.,
            Rupp,J., Meyer,T.F., Hacker,G. and Heuer,D.
  TITLE     Targeting of a chlamydial protease impedes intracellular bacterial
            growth
  JOURNAL   PLoS Pathog 7 (9), e1002283 (2011)
   PUBMED   21990969
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Sohda,M., Misumi,Y., Yamamoto,A., Nakamura,N., Ogata,S.,
            Sakisaka,S., Hirose,S., Ikehara,Y. and Oda,K.
  TITLE     Interaction of Golgin-84 with the COG complex mediates the
            intra-Golgi retrograde transport
  JOURNAL   Traffic 11 (12), 1552-1566 (2010)
   PUBMED   20874812
  REMARK    GeneRIF: Golgin-84 on coat protein I vesicles interacts with the
            conserved oligomeric Golgi complex before SNARE assembly.
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Heuer,D., Rejman Lipinski,A., Machuy,N., Karlas,A., Wehrens,A.,
            Siedler,F., Brinkmann,V. and Meyer,T.F.
  TITLE     Chlamydia causes fragmentation of the Golgi compartment to ensure
            reproduction
  JOURNAL   Nature 457 (7230), 731-735 (2009)
   PUBMED   19060882
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Malsam,J., Satoh,A., Pelletier,L. and Warren,G.
  TITLE     Golgin tethers define subpopulations of COPI vesicles
  JOURNAL   Science 307 (5712), 1095-1098 (2005)
   PUBMED   15718469
REFERENCE   6  (residues 1 to 731)
  AUTHORS   Satoh,A., Wang,Y., Malsam,J., Beard,M.B. and Warren,G.
  TITLE     Golgin-84 is a rab1 binding partner involved in Golgi structure
  JOURNAL   Traffic 4 (3), 153-161 (2003)
   PUBMED   12656988
  REMARK    GeneRIF: involved in generating and maintaining the architecture of
            the Golgi apparatus
REFERENCE   7  (residues 1 to 731)
  AUTHORS   Diao,A., Rahman,D., Pappin,D.J., Lucocq,J. and Lowe,M.
  TITLE     The coiled-coil membrane protein golgin-84 is a novel rab effector
            required for Golgi ribbon formation
  JOURNAL   J Cell Biol 160 (2), 201-212 (2003)
   PUBMED   12538640
REFERENCE   8  (residues 1 to 731)
  AUTHORS   Bascom,R.A., Srinivasan,S. and Nussbaum,R.L.
  TITLE     Identification and characterization of golgin-84, a novel Golgi
            integral membrane protein with a cytoplasmic coiled-coil domain
  JOURNAL   J Biol Chem 274 (5), 2953-2962 (1999)
   PUBMED   9915833
  REMARK    Erratum:[J Biol Chem 1999 Apr 30;274(18):12950]
REFERENCE   9  (residues 1 to 731)
  AUTHORS   Klugbauer,S., Demidchik,E.P., Lengfelder,E. and Rabes,H.M.
  TITLE     Detection of a novel type of RET rearrangement (PTC5) in thyroid
            carcinomas after Chernobyl and analysis of the involved RET-fused
            gene RFG5
  JOURNAL   Cancer Res 58 (2), 198-203 (1998)
   PUBMED   9443391
REFERENCE   10 (residues 1 to 731)
  AUTHORS   Ishizaka,Y., Ochiai,M., Tahira,T., Sugimura,T. and Nagao,M.
  TITLE     Activation of the ret-II oncogene without a sequence encoding a
            transmembrane domain and transforming activity of two ret-II
            oncogene products differing in carboxy-termini due to alternative
            splicing
  JOURNAL   Oncogene 4 (6), 789-794 (1989)
   PUBMED   2734021
  REMARK    Erratum:[Oncogene 1989 Nov;4(11):1415]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL132987.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_005104.3.
            
            Summary: The Golgi apparatus, which participates in glycosylation
            and transport of proteins and lipids in the secretory pathway,
            consists of a series of stacked cisternae (flattened membrane
            sacs). Interactions between the Golgi and microtubules are thought
            to be important for the reorganization of the Golgi after it
            fragments during mitosis. This gene encodes one of the golgins, a
            family of proteins localized to the Golgi. This protein is a
            coiled-coil membrane protein that has been postulated to play a
            role in vesicle tethering and docking. Translocations involving
            this gene and the ret proto-oncogene have been found in tumor
            tissues; the chimeric sequences have been designated RET-II and
            PTC5. A pseudogene of this gene is located on the short arm of
            chromosome 5. [provided by RefSeq, Jul 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.122087.1,
                                           SRR1803611.169184.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000163416.7/ ENSP00000163416.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..731
                     /product="golgin subfamily A member 5"
                     /note="golgi integral membrane protein 5; golgi
                     autoantigen, golgin subfamily a, 5; golgin-84; RET-fused
                     gene 5 protein; cell proliferation-inducing gene 31
                     protein"
                     /calculated_mol_wt=82894
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q8TBA6.3)"
     Site            89
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q3ZU82; propagated from
                     UniProtKB/Swiss-Prot (Q8TBA6.3)"
     Region          93..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBA6.3)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TBA6.3)"
     Region          <219..570
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          420..724
                     /region_name="Golgin_A5"
                     /note="Golgin subfamily A member 5; pfam09787"
                     /db_xref="CDD:462900"
     Site            497..498
                     /site_type="other"
                     /note="Breakpoint for translocation to form RET-GOLGA5
                     oncogene; propagated from UniProtKB/Swiss-Prot (Q8TBA6.3)"
     Site            699..719
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBA6.3)"
     CDS             1..731
                     /gene="GOLGA5"
                     /gene_synonym="GOLIM5; ret-II; RFG5"
                     /coded_by="NM_005113.4:183..2378"
                     /db_xref="CCDS:CCDS9905.1"
                     /db_xref="GeneID:9950"
                     /db_xref="HGNC:HGNC:4428"
                     /db_xref="MIM:606918"
ORIGIN      
        1 mswfvdlagk aedllnrvdq gaatalsrkd nasniysknt dytelhqqnt dliyqtgpks
       61 tyissaadni rnqkatilag tanvkvgsrt pveashpven asvprpsshf vrrkksepdd
      121 ellfdflnss qkeptgrvei rkekgktpvf qssqtssvss vnpsvttikt ieensfgsqt
      181 heaasnsdss hegqeesske nvssnaacpd htptpnddgk shelsnlrle nqllrnevqs
      241 lnqemasllq rsketqeeln kararvekwn adhsksdrmt rglraqvddl teavaakdsq
      301 lavlkvrlqe adqllstrte alealqseks rimqdqsegn slqnqalqtf qerlheadat
      361 lkreqesykq mqsefaarln kvemerqnla eaitlaerky sdekkrvdel qqqvklykln
      421 lesskqelid ykqkatrilq skeklinslk egsgfeglds stassmelee lrhekemqre
      481 eiqklmgqih qlrselqdme aqqvneaesa reqlqdlhdq iagqkaskqe letelerlkq
      541 efhyieedly rtkntlqsri kdrdeeiqkl rnqltnktls nssqselenr lhqltetliq
      601 kqtmleslst eknslvfqle rleqqmnsas gsssngssin msgidngegt rlrnvpvlfn
      661 dtetnlagmy gkvrkaassi dqfsirlgif lrrypiarvf viiymallhl wvmivlltyt
      721 pemhhdqpyg k
//
LOCUS       NP_055580                145 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial import receptor subunit TOM20 homolog [Homo sapiens].
ACCESSION   NP_055580
VERSION     NP_055580.1
DBSOURCE    REFSEQ: accession NM_014765.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Raimi,O.G., Ojha,H., Ehses,K., Dederer,V., Lange,S.M., Rivera,C.P.,
            Deegan,T.D., Chen,Y., Wightman,M., Toth,R., Labib,K.P.M.,
            Mathea,S., Ranson,N., Fernandez-Busnadiego,R. and Muqit,M.M.K.
  TITLE     Mechanism of human PINK1 activation at the TOM complex in a
            reconstituted system
  JOURNAL   Sci Adv 10 (23), eadn7191 (2024)
   PUBMED   38848361
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Mi,D., Yanatori,I., Zheng,H., Kong,Y., Hirayama,T. and Toyokuni,S.
  TITLE     Association of poly(rC)-binding protein-2 with sideroflexin-3
            through TOM20 as an iron entry pathway to mitochondria
  JOURNAL   Free Radic Res 58 (4), 261-275 (2024)
   PUBMED   38599240
  REMARK    GeneRIF: Association of poly(rC)-binding protein-2 with
            sideroflexin-3 through TOM20 as an iron entry pathway to
            mitochondria.
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Yin,L., Ye,Y., Zou,L., Lin,J., Dai,Y., Fu,Y., Liu,Y., Peng,Y.,
            Gao,Y., Fu,Y., Qi,X., Deng,T., Zhang,S. and Li,X.
  TITLE     AR antagonists develop drug resistance through TOMM20 autophagic
            degradation-promoted transformation to neuroendocrine prostate
            cancer
  JOURNAL   J Exp Clin Cancer Res 42 (1), 204 (2023)
   PUBMED   37563661
  REMARK    GeneRIF: AR antagonists develop drug resistance through TOMM20
            autophagic degradation-promoted transformation to neuroendocrine
            prostate cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Wu,C., Wang,L., Chen,S., Shi,L., Liu,M., Tu,P., Sun,J., Zhao,R.,
            Zhang,Y., Wang,J., Pan,Y., Ma,Y. and Guo,Y.
  TITLE     Iron induces B cell pyroptosis through Tom20-Bax-caspase-gasdermin
            E signaling to promote inflammation post-spinal cord injury
  JOURNAL   J Neuroinflammation 20 (1), 171 (2023)
   PUBMED   37480037
  REMARK    GeneRIF: Iron induces B cell pyroptosis through
            Tom20-Bax-caspase-gasdermin E signaling to promote inflammation
            post-spinal cord injury.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Micaily,I., Lee,S., Basu Mallick,A., Zhan,T., O'Neill,R.,
            Gargano,S., Hozack,B., Thapa,S., Martinez-Outschoorn,U., Abraham,J.
            and Jiang,W.
  TITLE     TOMM20 as a Potential Prognostic Biomarker in Chordoma: Results
            From a High-Volume, Single-Center Study
  JOURNAL   Am J Clin Pathol 159 (5), 492-501 (2023)
   PUBMED   36857736
  REMARK    GeneRIF: TOMM20 as a Potential Prognostic Biomarker in Chordoma:
            Results From a High-Volume, Single-Center Study.
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Schleiff,E. and Turnbull,J.L.
  TITLE     Characterization of the N-terminal targeting signal binding domain
            of the mitochondrial outer membrane receptor, Tom20
  JOURNAL   Biochemistry 37 (38), 13052-13058 (1998)
   PUBMED   9748310
REFERENCE   7  (residues 1 to 145)
  AUTHORS   Schleiff,E., Shore,G.C. and Goping,I.S.
  TITLE     Interactions of the human mitochondrial protein import receptor,
            hTom20, with precursor proteins in vitro reveal pleiotropic
            specificities and different receptor domain requirements
  JOURNAL   J Biol Chem 272 (28), 17784-17789 (1997)
   PUBMED   9211931
REFERENCE   8  (residues 1 to 145)
  AUTHORS   Schleiff,E., Shore,G.C. and Goping,I.S.
  TITLE     Human mitochondrial import receptor, Tom20p. Use of glutathione to
            reveal specific interactions between Tom20-glutathione
            S-transferase and mitochondrial precursor proteins
  JOURNAL   FEBS Lett 404 (2-3), 314-318 (1997)
   PUBMED   9119086
REFERENCE   9  (residues 1 to 145)
  AUTHORS   Seki,N., Moczko,M., Nagase,T., Zufall,N., Ehmann,B., Dietmeier,K.,
            Schafer,E., Nomura,N. and Pfanner,N.
  TITLE     A human homolog of the mitochondrial protein import receptor Mom19
            can assemble with the yeast mitochondrial receptor complex
  JOURNAL   FEBS Lett 375 (3), 307-310 (1995)
   PUBMED   7498524
REFERENCE   10 (residues 1 to 145)
  AUTHORS   Goping,I.S., Millar,D.G. and Shore,G.C.
  TITLE     Identification of the human mitochondrial protein import receptor,
            huMas20p. Complementation of delta mas20 in yeast
  JOURNAL   FEBS Lett 373 (1), 45-50 (1995)
   PUBMED   7589431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK289810.1, BC100286.1, D13641.1 and BC009886.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D13641.1, SRR14038195.118540.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000366607.5/
                                                  ENSP00000355566.4
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.3"
     Protein         1..145
                     /product="mitochondrial import receptor subunit TOM20
                     homolog"
                     /note="translocase of outer mitochondrial membrane 20
                     homolog type II; mitochondrial 20 kDa outer membrane
                     protein; outer mitochondrial membrane receptor Tom20"
                     /calculated_mol_wt=16167
     Region          1..127
                     /region_name="MAS20"
                     /note="MAS20 protein import receptor; cl03428"
                     /db_xref="CDD:470806"
     Site            7..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15388.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15388.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q15388.1)"
     CDS             1..145
                     /gene="TOMM20"
                     /gene_synonym="MAS20; MOM19; TOM20"
                     /coded_by="NM_014765.3:123..560"
                     /db_xref="CCDS:CCDS1603.1"
                     /db_xref="GeneID:9804"
                     /db_xref="HGNC:HGNC:20947"
                     /db_xref="MIM:601848"
ORIGIN      
        1 mvgrnsaiaa gvcgalfigy ciyfdrkrrs dpnfknrlre rrkkqklake raglsklpdl
       61 kdaeavqkff leeiqlgeel laqgeyekgv dhltnaiavc gqpqqllqvl qqtlpppvfq
      121 mlltklptis qrivsaqsla eddve
//
LOCUS       NP_001356860             643 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001356860 XP_016884495
VERSION     NP_001356860.1
DBSOURCE    REFSEQ: accession NM_001369931.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            On Apr 24, 2019 this sequence version replaced XP_016884495.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.24651.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..643
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 9"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=73067
     Region          355..394
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..643
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369931.1:717..2648"
                     /note="isoform 9 is encoded by transcript variant 14"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mqkrlhrsvf ltflrmsthk eskdhfisps afgeilynnf lfdipkildl cvlfgkgnsp
       61 llqkmignif tqqpsyysdl detlptilqv fsnilqhcgl qgdganttpq kleergrltp
      121 sdmpllelkd ivlylcdtct tlwafldifp lacqtfqkhd fcyrlasfye aaipemesai
      181 kkrrledskl lgdlwqrlsh srkklmeifh iilnqicllp ilesscdniq gfieeflqif
      241 ssllqekrfl rdydalfpva edisllqqas svldetrtay ilqavesawe gvdrrkatda
      301 kdpsvieepn gepngvtvta eavsqasshp enseeeecmg aaaavgpamc gveldslisq
      361 vkdllpdlge gfilacleyy hydpeqvinn ileerlaptl sqldrnldre mkpdptpllt
      421 srhnvfqnde fdvfsrdsvd lsrvhkgkst rkeentrsll ndkravaaqr qryeqysvvv
      481 eevplqpges lpyhsvyyed eyddtydgnq vgandadsdd elisrrpfti pqvlrtkvpr
      541 egqeedddde eddadeeapk pdhfvqdpav lrekaearrm aflakkgyrh dsstavagsp
      601 rghgqsrett qerrkkeank atranhnrrt madrkrskgm ips
//
LOCUS       NP_001307452             135 aa            linear   PRI 27-APR-2025
DEFINITION  synaptogyrin-2 isoform 2 [Homo sapiens].
ACCESSION   NP_001307452 XP_005257850
VERSION     NP_001307452.1
DBSOURCE    REFSEQ: accession NM_001320523.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Liu,C., Qu,Z., Zhao,H., Wang,P., Zhan,C. and Zhang,Y.
  TITLE     Pan-cancer analysis of SYNGR2 with a focus on clinical implications
            and immune landscape in liver hepatocellular carcinoma
  JOURNAL   BMC Bioinformatics 24 (1), 192 (2023)
   PUBMED   37170221
  REMARK    GeneRIF: Pan-cancer analysis of SYNGR2 with a focus on clinical
            implications and immune landscape in liver hepatocellular
            carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Sun,Q., Qi,X., Zhang,Y., Wu,X., Liang,M., Li,C., Li,D.,
            Cardona,C.J. and Xing,Z.
  TITLE     Synaptogyrin-2 Promotes Replication of a Novel Tick-borne
            Bunyavirus through Interacting with Viral Nonstructural Protein NSs
  JOURNAL   J Biol Chem 291 (31), 16138-16149 (2016)
   PUBMED   27226560
  REMARK    GeneRIF: synaptogyrin-2 is essential to promoting the formation of
            the IBs to become virus factories for viral RNA replication through
            its interaction with NSs. These findings unveil the function of
            synaptogyrin-2 as an enhancer in viral infection.
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Kedra,D., Pan,H.Q., Seroussi,E., Fransson,I., Guilbaud,C.,
            Collins,J.E., Dunham,I., Blennow,E., Roe,B.A., Piehl,F. and
            Dumanski,J.P.
  TITLE     Characterization of the human synaptogyrin gene family
  JOURNAL   Hum Genet 103 (2), 131-141 (1998)
   PUBMED   9760194
REFERENCE   6  (residues 1 to 135)
  AUTHORS   Janz,R. and Sudhof,T.C.
  TITLE     Cellugyrin, a novel ubiquitous form of synaptogyrin that is
            phosphorylated by pp60c-src
  JOURNAL   J Biol Chem 273 (5), 2851-2857 (1998)
   PUBMED   9446595
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021593.15, CF122406.1,
            BC105992.1 and BI160076.1.
            
            On Feb 26, 2016 this sequence version replaced XP_005257850.1.
            
            Summary: This gene encodes an integral membrane protein containing
            four transmembrane regions and a C-terminal cytoplasmic tail that
            is tyrosine phosphorylated. The exact function of this protein is
            unclear, but studies of a similar rat protein suggest that it may
            play a role in regulating membrane traffic in non-neuronal cells.
            The gene belongs to the synaptogyrin gene family. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Feb 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.947580.1,
                                           SRR1163657.348151.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..135
                     /product="synaptogyrin-2 isoform 2"
                     /note="cellugyrin"
                     /calculated_mol_wt=14581
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (O43760.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43760.1)"
     Region          20..>117
                     /region_name="MARVEL"
                     /note="Membrane-associating domain; pfam01284"
                     /db_xref="CDD:366555"
     Site            26..46
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43760.1)"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43760.1)"
     CDS             1..135
                     /gene="SYNGR2"
                     /coded_by="NM_001320523.2:73..480"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:9144"
                     /db_xref="HGNC:HGNC:11499"
                     /db_xref="MIM:603926"
ORIGIN      
        1 mesgaygaak aggsfdlrrf ltqpqvvara vclvfalivf sciygegysn aheskqmycv
       61 fnrnedacry gsaigvlafl asafflvvda yfpqisnatd rkylvigdll fsgcaglpgl
      121 palqgwrgrl hpelr
//
LOCUS       NP_001287719             264 aa            linear   PRI 27-APR-2025
DEFINITION  HLA class II histocompatibility antigen, DQ beta 2 chain isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001287719
VERSION     NP_001287719.1
DBSOURCE    REFSEQ: accession NM_001300790.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wang,X., Cao,X., Zhang,W., Zhang,L., Lu,L., Li,X., El-Ashram,S.,
            Wu,J. and Chen,C.
  TITLE     Association of human leukocyte antigens-DQB2/DPA1/DPB1 polymorphism
            and pulmonary tuberculosis in the Chinese Uygur population
  JOURNAL   Mol Genet Genomic Med 7 (3), e544 (2019)
   PUBMED   30600606
  REMARK    GeneRIF: The functional HLA-DQB2 rs7453920 G>A polymorphism may
            contribute to the genetic susceptibility to pulmonary tuberculosis
            in the Chinese Uygur population.
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Pereira,V.R.Z.B., Wolf,J.M., Stumm,G.Z., Boeira,T.R., Galvan,J.,
            Simon,D. and Lunge,V.R.
  TITLE     Lack of association between human leukocyte antigen polymorphisms
            rs9277535 and rs7453920 and chronic hepatitis B in a Brazilian
            population
  JOURNAL   Genet Mol Res 16 (2) (2017)
   PUBMED   28613373
  REMARK    GeneRIF: No statistically significant association was found between
            rs7453920 SNP and chronic hepatitis B.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Liu,X., Yang,B., Li,L., Cai,B., Liao,Y., Li,L., Wu,Z. and Wang,L.
  TITLE     Association of HLA-DP/DQ and STAT4 polymorphisms with ankylosing
            spondylitis in Southwest China
  JOURNAL   Int Immunopharmacol 39, 10-15 (2016)
   PUBMED   27394003
  REMARK    GeneRIF: this study shows that HLA-DQ gene polymorphisms are
            associated with ankylosing spondylitis in Southwest China
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Chang,S.W., Fann,C.S., Su,W.H., Wang,Y.C., Weng,C.C., Yu,C.J.,
            Hsu,C.L., Hsieh,A.R., Chien,R.N., Chu,C.M. and Tai,D.I.
  TITLE     A genome-wide association study on chronic HBV infection and its
            clinical progression in male Han-Taiwanese
  JOURNAL   PLoS One 9 (6), e99724 (2014)
   PUBMED   24940741
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Hu,Z., Liu,Y., Zhai,X., Dai,J., Jin,G., Wang,L., Zhu,L., Yang,Y.,
            Liu,J., Chu,M., Wen,J., Xie,K., Du,G., Wang,Q., Zhou,Y., Cao,M.,
            Liu,L., He,Y., Wang,Y., Zhou,G., Jia,W., Lu,J., Li,S., Liu,J.,
            Yang,H., Shi,Y., Zhou,W. and Shen,H.
  TITLE     New loci associated with chronic hepatitis B virus infection in Han
            Chinese
  JOURNAL   Nat Genet 45 (12), 1499-1503 (2013)
   PUBMED   24162738
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Beck,S., Abdulla,S., Alderton,R.P., Glynne,R.J., Gut,I.G.,
            Hosking,L.K., Jackson,A., Kelly,A., Newell,W.R., Sanseau,P.,
            Radley,E., Thorpe,K.L. and Trowsdale,J.
  TITLE     Evolutionary dynamics of non-coding sequences within the class II
            region of the human MHC
  JOURNAL   J Mol Biol 255 (1), 1-13 (1996)
   PUBMED   8568858
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Wang,Y., Lu,P., Zhou,K., Clay,T., Wood,N., Bradley,B. and
            Bidwell,J.
  TITLE     Nucleotide sequencing of HLA-DQ gene second exons in Chinese
            homozygous cells
  JOURNAL   Eur J Immunogenet 19 (5), 287-293 (1992)
   PUBMED   1420115
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Berdoz,J., Tiercy,J.M., Rollini,P., Mach,B. and Gorski,J.
  TITLE     Remarkable sequence conservation of the HLA-DQB2 locus (DX beta)
            within the highly polymorphic DQ subregion of the human MHC
  JOURNAL   Immunogenetics 29 (4), 241-248 (1989)
   PUBMED   2564844
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Jonsson,A.K., Hyldig-Nielsen,J.J., Servenius,B., Larhammar,D.,
            Andersson,G., Jorgensen,F., Peterson,P.A. and Rask,L.
  TITLE     Class II genes of the human major histocompatibility complex.
            Comparisons of the DQ and DX alpha and beta genes
  JOURNAL   J Biol Chem 262 (18), 8767-8777 (1987)
   PUBMED   3036828
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Okada,K., Boss,J.M., Prentice,H., Spies,T., Mengler,R., Auffray,C.,
            Lillie,J., Grossberger,D. and Strominger,J.L.
  TITLE     Gene organization of DC and DX subregions of the human major
            histocompatibility complex
  JOURNAL   Proc Natl Acad Sci U S A 82 (10), 3410-3414 (1985)
   PUBMED   3858830
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL672104.4.
            
            Summary: HLA-DQB2 belongs to the family of HLA class II beta chain
            paralogs. Class II molecules are heterodimers consisting of an
            alpha (DQA) and a beta chain (DQB), both anchored in the membrane.
            They play a central role in the immune system by presenting
            peptides derived from extracellular proteins. Class II molecules
            are expressed in antigen presenting cells (APC: B lymphocytes,
            dendritic cells, macrophages). Polymorphisms in the alpha and beta
            chains specify the peptide binding specificity, and typing for
            these polymorphisms is routinely done for bone marrow
            transplantation. However this gene, HLA-DQB2, is not routinely
            typed, as it is not thought to have an effect on transplantation.
            There is conflicting evidence in the literature and public sequence
            databases for the protein-coding capacity of HLA-DQB2. Because
            there is evidence of transcription and an intact ORF, HLA-DQB2 is
            represented in Entrez Gene and in RefSeq as a protein-coding locus.
            [provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000437316.7/ ENSP00000396330.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..264
                     /product="HLA class II histocompatibility antigen, DQ beta
                     2 chain isoform 1 precursor"
                     /note="MHC class II antigen DQB2; HLA class II
                     histocompatibility antigen, DX beta chain; HLA class II
                     histocompatibility antigen, DQ beta 2 chain; DV19.1 (major
                     histocompatibility complex, class II, DQ beta 2
                     (HLA-DXB))"
                     /calculated_mol_wt=26997
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2876
     Region          41..111
                     /region_name="MHC_II_beta"
                     /note="Class II histocompatibility antigen, beta domain;
                     pfam00969"
                     /db_xref="CDD:425967"
     Region          121..217
                     /region_name="IgC1_MHC_II_beta_HLA-DQ_I-A"
                     /note="Class II major histocompatibility complex (MHC)
                     beta chain immunoglobulin domain of histocompatibility
                     antigen (HLA) DQ and I-A; member of the C1-set of Ig
                     superfamily (IgSF) domains; cd21001"
                     /db_xref="CDD:409592"
     Region          123..131
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409592"
     Site            order(129,147..148,150,176..183)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409592"
     Region          141..150
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409592"
     Site            order(150,178..180,182)
                     /site_type="other"
                     /note="MHC binding domain interface [polypeptide binding]"
                     /db_xref="CDD:409592"
     Region          154..160
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409592"
     Region          162..165
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409592"
     Region          169..177
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409592"
     Region          180..190
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409592"
     Region          197..204
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409592"
     Region          211..215
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409592"
     CDS             1..264
                     /gene="HLA-DQB2"
                     /gene_synonym="DQB2; HLA-DQB1; HLA-DXB"
                     /coded_by="NM_001300790.2:63..857"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS78128.1"
                     /db_xref="GeneID:3120"
                     /db_xref="HGNC:HGNC:4945"
                     /db_xref="MIM:615161"
ORIGIN      
        1 malqipggfw aaavtvmlvm lstpvaeard fpkdflvqfk gmcyftngte rvrgvaryiy
       61 nreeygrfds dvgefqavte lgrsiedwnn ykdfleqera avdkvcrhny eaelrttlqr
      121 qveptvtisp srtealnhhn llvcsvtdfy paqikvrwfr ndqeetagvv stslirngdw
      181 tfqilvmlei tpqrgdiytc qvehpslqsp itvewraqse saqskmlsgi ggfvlglifl
      241 glgliirhrg qkgprgpppa gllh
//
LOCUS       NP_689948                473 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 9 [Homo sapiens].
ACCESSION   NP_689948
VERSION     NP_689948.1
DBSOURCE    REFSEQ: accession NM_152735.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 473)
  AUTHORS   Siedlinski,M., Cho,M.H., Bakke,P., Gulsvik,A., Lomas,D.A.,
            Anderson,W., Kong,X., Rennard,S.I., Beaty,T.H., Hokanson,J.E.,
            Crapo,J.D. and Silverman,E.K.
  CONSRTM   COPDGene Investigators; ECLIPSE Investigators
  TITLE     Genome-wide association study of smoking behaviours in patients
            with COPD
  JOURNAL   Thorax 66 (10), 894-902 (2011)
   PUBMED   21685187
REFERENCE   6  (residues 1 to 473)
  AUTHORS   Ravasi,T., Suzuki,H., Cannistraci,C.V., Katayama,S., Bajic,V.B.,
            Tan,K., Akalin,A., Schmeier,S., Kanamori-Katayama,M., Bertin,N.,
            Carninci,P., Daub,C.O., Forrest,A.R., Gough,J., Grimmond,S.,
            Han,J.H., Hashimoto,T., Hide,W., Hofmann,O., Kamburov,A., Kaur,M.,
            Kawaji,H., Kubosaki,A., Lassmann,T., van Nimwegen,E.,
            MacPherson,C.R., Ogawa,C., Radovanovic,A., Schwartz,A.,
            Teasdale,R.D., Tegner,J., Lenhard,B., Teichmann,S.A., Arakawa,T.,
            Ninomiya,N., Murakami,K., Tagami,M., Fukuda,S., Imamura,K., Kai,C.,
            Ishihara,R., Kitazume,Y., Kawai,J., Hume,D.A., Ideker,T. and
            Hayashizaki,Y.
  TITLE     An atlas of combinatorial transcriptional regulation in mouse and
            man
  JOURNAL   Cell 140 (5), 744-752 (2010)
   PUBMED   20211142
  REMARK    Erratum:[Cell. 2010 Apr 16;141(2):369. Kamburov, Atanas [added];
            Kaur, Mandeep [added]; MacPherson, Cameron Ross [added];
            Radovanovic, Aleksandar [added]; Schwartz, Ariel [added]]
REFERENCE   7  (residues 1 to 473)
  AUTHORS   Barcellos,L.F., May,S.L., Ramsay,P.P., Quach,H.L., Lane,J.A.,
            Nititham,J., Noble,J.A., Taylor,K.E., Quach,D.L., Chung,S.A.,
            Kelly,J.A., Moser,K.L., Behrens,T.W., Seldin,M.F., Thomson,G.,
            Harley,J.B., Gaffney,P.M. and Criswell,L.A.
  TITLE     High-density SNP screening of the major histocompatibility complex
            in systemic lupus erythematosus demonstrates strong evidence for
            independent susceptibility regions
  JOURNAL   PLoS Genet 5 (10), e1000696 (2009)
   PUBMED   19851445
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL662799.16, AK122644.1, BX488390.1 and BC014978.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014978.1, AK122644.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395064.3/ ENSP00000378503.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..473
                     /product="zinc finger and BTB domain-containing protein 9"
                     /calculated_mol_wt=50471
     Region          30..140
                     /region_name="BTB_POZ_ZBTB9"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 9 (ZBTB9); cd18200"
                     /db_xref="CDD:349509"
     Region          177..279
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C00.1)"
     Region          293..376
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C00.1)"
     Region          388..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(390,392,394,396..397,400..401,404,418,420,424..425,
                     428..429,432,445,447,449,451..452,455..456)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          440..457
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..473
                     /gene="ZBTB9"
                     /gene_synonym="ZNF919"
                     /coded_by="NM_152735.4:272..1693"
                     /db_xref="CCDS:CCDS4780.1"
                     /db_xref="GeneID:221504"
                     /db_xref="HGNC:HGNC:28323"
ORIGIN      
        1 metptplppv pasptcnpap rtiqiefpqh ssslleslnr hrlegkfcdv sllvqgrelr
       61 ahkavlaaas pyfhdklllg daprltlpsv ieadafegll qliysgrlrl pldalpahll
      121 vasglqmwqv vdqcseilre letsgggisa rggnsyhall sttsstggwc irsspfqtpv
      181 qssastespa stespvggeg selgevlqiq veeeeeeeed dddedqgsat lsqtpqpqrv
      241 sgvfprphgp hplpmtatpr klpegesapl elpappalpp kifyikqepf epkeeisgsg
      301 tqpggakeet kvfsggdteg ngelgfllps gpgptsgggg pswkpvdlhg neilsggggp
      361 ggagqavhgp vklggtppad gkrfgclcgk rfavkpkrdr himltfslrp fgcgicnkrf
      421 klkhhltehm kthagalhac phcgrrfrvh acflrhrdlc kgqgwatahw tyk
//
LOCUS       NP_001171671             672 aa            linear   PRI 27-APR-2025
DEFINITION  transcriptional regulator Kaiso [Homo sapiens].
ACCESSION   NP_001171671
VERSION     NP_001171671.1
DBSOURCE    REFSEQ: accession NM_001184742.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Ahmed,S., Khan,S., Qureshi,M.A., Bukhari,U., Anis,M. and
            Mughal,M.N.
  TITLE     Expressional variations of Kaiso: an association with pathological
            characteristics and field cancerization of OSCC
  JOURNAL   BMC Cancer 22 (1), 990 (2022)
   PUBMED   36115941
  REMARK    GeneRIF: Expressional variations of Kaiso: an association with
            pathological characteristics and field cancerization of OSCC.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Tian,W., Yuan,H., Qin,S., Liu,W., Zhang,B., Gu,L., Zhou,J. and
            Deng,D.
  TITLE     Kaiso phosphorylation at threonine 606 leads to its accumulation in
            the cytoplasm, reducing its transcriptional repression of the
            tumour suppressor CDH1
  JOURNAL   Mol Oncol 16 (17), 3192-3209 (2022)
   PUBMED   35851744
  REMARK    GeneRIF: Kaiso phosphorylation at threonine 606 leads to its
            accumulation in the cytoplasm, reducing its transcriptional
            repression of the tumour suppressor CDH1.
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Nikolova,E.N., Stanfield,R.L., Dyson,H.J. and Wright,P.E.
  TITLE     A Conformational Switch in the Zinc Finger Protein Kaiso Mediates
            Differential Readout of Specific and Methylated DNA Sequences
  JOURNAL   Biochemistry 59 (20), 1909-1926 (2020)
   PUBMED   32352758
  REMARK    GeneRIF: A Conformational Switch in the Zinc Finger Protein Kaiso
            Mediates Differential Readout of Specific and Methylated DNA
            Sequences.
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 672)
  AUTHORS   Kondapalli,J., Flozak,A.S. and Albuquerque,M.L.
  TITLE     Laminar shear stress differentially modulates gene expression of
            p120 catenin, Kaiso transcription factor, and vascular endothelial
            cadherin in human coronary artery endothelial cells
  JOURNAL   J Biol Chem 279 (12), 11417-11424 (2004)
   PUBMED   14699141
  REMARK    GeneRIF: differential expression of p120(ctn) and Kaiso mRNA was
            observed in human coronary artery endothelial cells depending on
            how laminar shear stress was applied in relation to the wounding
            process
REFERENCE   7  (residues 1 to 672)
  AUTHORS   Yoon,H.G., Chan,D.W., Reynolds,A.B., Qin,J. and Wong,J.
  TITLE     N-CoR mediates DNA methylation-dependent repression through a
            methyl CpG binding protein Kaiso
  JOURNAL   Mol Cell 12 (3), 723-734 (2003)
   PUBMED   14527417
REFERENCE   8  (residues 1 to 672)
  AUTHORS   Prokhortchouk,A., Hendrich,B., Jorgensen,H., Ruzov,A., Wilm,M.,
            Georgiev,G., Bird,A. and Prokhortchouk,E.
  TITLE     The p120 catenin partner Kaiso is a DNA methylation-dependent
            transcriptional repressor
  JOURNAL   Genes Dev 15 (13), 1613-1618 (2001)
   PUBMED   11445535
REFERENCE   9  (residues 1 to 672)
  AUTHORS   Daniel,J.M., Ireton,R.C. and Reynolds,A.B.
  TITLE     Monoclonal antibodies to Kaiso: a novel transcription factor and
            p120ctn-binding protein
  JOURNAL   Hybridoma 20 (3), 159-166 (2001)
   PUBMED   11461664
REFERENCE   10 (residues 1 to 672)
  AUTHORS   Daniel,J.M. and Reynolds,A.B.
  TITLE     The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain
            zinc finger transcription factor
  JOURNAL   Mol Cell Biol 19 (5), 3614-3623 (1999)
   PUBMED   10207085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB468333.1, AK312321.1,
            BC042753.1 and AC002086.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a transcriptional regulator with bimodal
            DNA-binding specificity, which binds to methylated CGCG and also to
            the non-methylated consensus KAISO-binding site TCCTGCNA. The
            protein contains an N-terminal POZ/BTB domain and 3 C-terminal zinc
            finger motifs. It recruits the N-CoR repressor complex to promote
            histone deacetylation and the formation of repressive chromatin
            structures in target gene promoters. It may contribute to the
            repression of target genes of the Wnt signaling pathway, and may
            also activate transcription of a subset of target genes by the
            recruitment of catenin delta-2 (CTNND2). Its interaction with
            catenin delta-1 (CTNND1) inhibits binding to both methylated and
            non-methylated DNA. It also interacts directly with the nuclear
            import receptor Importin-alpha2 (also known as karyopherin alpha2
            or RAG cohort 1), which may mediate nuclear import of this protein.
            Alternatively spliced transcript variants encoding the same protein
            have been identified.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) is the longer transcript.
            Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.81070.1,
                                           SRR1803613.273544.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000557385.2/ ENSP00000450969.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq24"
     Protein         1..672
                     /product="transcriptional regulator Kaiso"
                     /note="kaiso transcription factor; WUGSC:H_DJ525N14.1;
                     zinc finger and BTB domain-containing protein 33"
                     /calculated_mol_wt=74354
     Region          1..136
                     /region_name="Self-association. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T24.2)"
     Region          1..103
                     /region_name="Interaction with NCOR1.
                     /evidence=ECO:0000269|PubMed:14527417"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T24.2)"
     Region          11..116
                     /region_name="BTB_POZ_ZBTB33_KAISO"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kaiso; cd18219"
                     /db_xref="CDD:349528"
     Region          209..>322
                     /region_name="PRK11901"
                     /note="hypothetical protein; Reviewed"
                     /db_xref="CDD:237015"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86T24.2)"
     Region          298..573
                     /region_name="Interaction with CBFA2T3.
                     /evidence=ECO:0000269|PubMed:23251453"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T24.2)"
     Region          325..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T24.2)"
     Region          454..672
                     /region_name="Interaction with CTNND1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T24.2)"
     Region          471..480
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T24.2)"
     Region          496..516
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(496,499,512,516)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(501,503,505,507..508,511..512,515,529,531,535..536,
                     539..540,543,557,559,561,563..564,567..568,572)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          508..531
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          514..638
                     /region_name="Required for DNA-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T24.2)"
     Region          524..544
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          539..561
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          552..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          616..635
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86T24.2)"
     CDS             1..672
                     /gene="ZBTB33"
                     /gene_synonym="ZNF-kaiso; ZNF348"
                     /coded_by="NM_001184742.2:271..2289"
                     /db_xref="CCDS:CCDS14596.1"
                     /db_xref="GeneID:10009"
                     /db_xref="HGNC:HGNC:16682"
                     /db_xref="MIM:300329"
ORIGIN      
        1 mesrklisat diqysgslln slneqrghgl fcdvtvived rkfrahknil sasstyfhql
       61 fsvagqvvel sfiraeifae ilnyiysski vrvrsdllde liksgqllgv kfiaelgvpl
      121 sqvksisgta qdgnteplpp dsgdknlviq kskdeaqdng atimpiites fslsaedyem
      181 kkiivtdsdd ddddvifcse ilptketlps nntvaqvqsn pgpvaisdva psasnnsppl
      241 tnitptqklp tpvnqatlsq tqgsekllvs sapthltpni illnqtplst ppnvssslpn
      301 hmpssinllv qnqqtpnsai ltgnkaneee eeeiiddddd tissspdsav sntslvpqad
      361 tsqntsfdgs liqkmqiptl lqeplsnslk isdiitrntn dpgvgskhlm egqkiitldt
      421 ateieglstg ckvyaniged tydivipvkd dpdegearle neipktsgse mankrmkvkh
      481 ddhyelivdg rvyyicivck rsyvcltslr rhfnihswek kypcrycekv fplaeyrtkh
      541 eihhtgerry qclacgksfi nyqfmsshik svhsqdpsgd sklyrlhpcr slqirqyayl
      601 sdrsstipam kddgigykvd tgkeppvgtt tstqnkpmtw edifiqqend sifkqnvtdg
      661 stefefiipe sy
//
LOCUS       NP_056243                871 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 473 isoform 1 [Homo sapiens].
ACCESSION   NP_056243
VERSION     NP_056243.1
DBSOURCE    REFSEQ: accession NM_015428.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 871)
  AUTHORS   de Filippo,C., Key,F.M., Ghirotto,S., Benazzo,A., Meneu,J.R.,
            Weihmann,A., Parra,G., Green,E.D. and Andres,A.M.
  CONSRTM   NISC Comparative Sequence Program
  TITLE     Recent Selection Changes in Human Genes under Long-Term Balancing
            Selection
  JOURNAL   Mol Biol Evol 33 (6), 1435-1447 (2016)
   PUBMED   26831942
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Wagner,E.J. and Marzluff,W.F.
  TITLE     ZFP100, a component of the active U7 snRNP limiting for histone
            pre-mRNA processing, is required for entry into S phase
  JOURNAL   Mol Cell Biol 26 (17), 6702-6712 (2006)
   PUBMED   16914750
  REMARK    GeneRIF: ZFP100 is the limiting factor for histone pre-mRNA
            processing in vivo.
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Wagner,E.J., Ospina,J.K., Hu,Y., Dundr,M., Matera,A.G. and
            Marzluff,W.F.
  TITLE     Conserved zinc fingers mediate multiple functions of ZFP100, a
            U7snRNP associated protein
  JOURNAL   RNA 12 (7), 1206-1218 (2006)
   PUBMED   16714279
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Pillai,R.S., Grimmler,M., Meister,G., Will,C.L., Luhrmann,R.,
            Fischer,U. and Schumperli,D.
  TITLE     Unique Sm core structure of U7 snRNPs: assembly by a specialized
            SMN complex and the role of a new component, Lsm11, in histone RNA
            processing
  JOURNAL   Genes Dev 17 (18), 2321-2333 (2003)
   PUBMED   12975319
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Dominski,Z., Erkmann,J.A., Yang,X., Sanchez,R. and Marzluff,W.F.
  TITLE     A novel zinc finger protein is associated with U7 snRNP and
            interacts with the stem-loop binding protein in the histone
            pre-mRNP to stimulate 3'-end processing
  JOURNAL   Genes Dev 16 (1), 58-71 (2002)
   PUBMED   11782445
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB032967.1, BX492803.1,
            AF454744.1 and AL080143.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the Krueppel C2H2-type
            zinc-finger family of proteins. The encoded protein, a component of
            the U7 snRNP complex, plays a role in histone 3'-end pre-mRNA
            processing and may be required for cell cycle progression to S
            phase. Expression level and methylation status of this gene may be
            correlated with bone mineral density. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Variants 1 and 2
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX648093.1, SRR1803614.36734.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270617.8/ ENSP00000270617.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..871
                     /product="zinc finger protein 473 isoform 1"
                     /note="zinc finger protein 100 homolog"
                     /calculated_mol_wt=100052
     Region          6..45
                     /region_name="KRAB_A-box"
                     /note="KRAB (Kruppel-associated box) domain -A box;
                     cd07765"
                     /db_xref="CDD:143639"
     Region          47..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WTR7.1)"
     Region          140..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WTR7.1)"
     Region          207..614
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          211..231
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(211,214,227,231)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          239..259
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          267..286
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          290..318
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WTR7.1)"
     Region          312..552
                     /region_name="Interaction with SLBP/pre-mRNA complex"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WTR7.1)"
     Region          322..342
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(322,325,338,342)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          349..369
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          377..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(377,380,393,397)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          405..425
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(405,408,421,425)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(410,412,414,416..417,420..421,424,438,440,444..445,
                     448..449,452,466,468,470,472..473,476..477,480)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          433..453
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          457..860
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          461..481
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          489..509
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          517..537
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(517,520,533,537)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          564..584
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(564,567,580,584)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          593..613
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(593,596,609,613)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          648..668
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          676..696
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(676,679,692,696)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          704..724
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(704,707,720,724)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          732..752
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(732,735,748,752)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(737,739,741,743..744,747..748,751,765,767,771..772,
                     775..776,779,793,795,797,799..800,803..804,807)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          760..780
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          788..808
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          816..836
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          844..864
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..871
                     /gene="ZNF473"
                     /gene_synonym="ZFP100; ZN473"
                     /coded_by="NM_015428.4:310..2925"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33077.1"
                     /db_xref="GeneID:25888"
                     /db_xref="HGNC:HGNC:23239"
                     /db_xref="MIM:617908"
ORIGIN      
        1 maeefvtlkd vgmdftlgdw eqlgleqgdt fwdtaldncq dlflldpprp nltshpdgse
       61 dleplaggsp eatspdvtet knsplmedff eegfsqeiie mlskdgfwns nfgeaciedt
      121 wldsllgdpe sllrsdiatn gesptecksh elkrglspvs tvstgedsmv hnvsektltp
      181 akskeyrgef fsysdhsqqd svqegekpyq csecgksfsg syrltqhwit htrekptvhq
      241 eceqgfdrna slsvypktht gykfyvcney gttfsqstyl whqkthtgek pcksqdsdhp
      301 pshdtqpgeh qkthtdsksy ncnecgkaft rifhltrhqk ihtrkryecs kcqatfnlrk
      361 hliqhqktha akttsecqec gkifrhssll iehqalhage epykcnergk sfrhnstlki
      421 hqrvhsgekp ykcsecgkaf hrhthlnehr rihtgyrphk cqecvrsfsr pshlmrhqai
      481 htaekpysca ecketfsdnn rlvqhqkmht vktpyecqec gerficgstl kchesvhare
      541 kqgffvsgki ldqnpeqkek cfkcnkcekt fscskyltqh erihtrgvkp fecdqcgkaf
      601 gqstrlihhq rihsrvrlyk wgeqgkaiss asliklqsfh tkehpfkcne cgktfshsah
      661 lskhqlihag enpfkcskcd rvftqrnylv qhertharkk plvcnecgkt frqssclskh
      721 qrihsgekpy vcdycgkafg lsaelvrhqr ihtgekpyvc qecgkaftqs sclsihrrvh
      781 tgekpyrcge cgkafaqkan ltqhqrihtg ekpyscnvcg kafvlsahln qhlrvhtqet
      841 lyqcqrcqka frchsslsrh qrvhnkqqyc l
//
LOCUS       NP_083495                731 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF19B isoform 2 [Mus musculus].
ACCESSION   NP_083495 XP_204030 XP_915468
VERSION     NP_083495.1
DBSOURCE    REFSEQ: accession NM_029219.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Lawrence,D.W., Shornick,L.P. and Kornbluth,J.
  TITLE     Mice deficient in NKLAM have attenuated inflammatory cytokine
            production in a Sendai virus pneumonia model
  JOURNAL   PLoS One 14 (9), e0222802 (2019)
   PUBMED   31539400
  REMARK    GeneRIF: Results indicate that natural killer lytic-associated
            molecule (NKLAM/RNF19b) plays a role in regulating the production
            of pro-inflammatory cytokines during viral infection.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Lawrence,D.W. and Kornbluth,J.
  TITLE     Reduced inflammation and cytokine production in NKLAM deficient
            mice during Streptococcus pneumoniae infection
  JOURNAL   PLoS One 13 (3), e0194202 (2018)
   PUBMED   29518136
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Lawrence,D.W., Gullickson,G. and Kornbluth,J.
  TITLE     E3 ubiquitin ligase NKLAM positively regulates macrophage inducible
            nitric oxide synthase expression
  JOURNAL   Immunobiology 220 (1), 83-92 (2015)
   PUBMED   25182373
  REMARK    GeneRIF: E3 ubiquitin ligase NKLAM positively regulates macrophage
            inducible nitric oxide synthase expression.
REFERENCE   6  (residues 1 to 731)
  AUTHORS   Lawrence,D.W. and Kornbluth,J.
  TITLE     E3 ubiquitin ligase NKLAM is a macrophage phagosome protein and
            plays a role in bacterial killing
  JOURNAL   Cell Immunol 279 (1), 46-52 (2012)
   PUBMED   23085241
  REMARK    GeneRIF: Data show that Natural Killer Lytic-Associated Molecule
            (NKLAM) is a component of macrophage phagosomes and is involved in
            macrophage bactericidal functions.
REFERENCE   7  (residues 1 to 731)
  AUTHORS   Hoover,R.G., Gullickson,G. and Kornbluth,J.
  TITLE     Impaired NK cytolytic activity and enhanced tumor growth in NK
            lytic-associated molecule-deficient mice
  JOURNAL   J Immunol 183 (11), 6913-6921 (2009)
   PUBMED   19915045
  REMARK    GeneRIF: support the role for NKLAM in NK function both in vitro
            and in vivo.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606977.28.
            
            On or before Jul 8, 2009 this sequence version replaced
            XP_915468.2, XP_204030.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.339223.1,
                                           SRR5286962.42080.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 62.76 cM"
     Protein         1..731
                     /product="E3 ubiquitin-protein ligase RNF19B isoform 2"
                     /EC_number="2.3.2.31"
                     /note="IBR domain containing 3; E3 ubiquitin-protein
                     ligase RNF19B; IBR domain-containing protein 3; natural
                     killer lytic-associated molecule"
                     /calculated_mol_wt=77925
     Region          1..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2A7Q9.2)"
     Region          116..176
                     /region_name="RING-HC_RBR_RNF19B"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 19B (RNF19B) and similar proteins; cd16776"
                     /db_xref="CDD:438432"
     Region          181..255
                     /region_name="BRcat-RBR_RNF19B"
                     /note="BRcat domain found in RING finger protein 19B
                     (RNF19B); cd20363"
                     /db_xref="CDD:439024"
     Region          277..345
                     /region_name="Rcat_RBR_RNF19"
                     /note="Rcat domain found in the RING finger protein 19
                     (RNF19) subfamily; cd20355"
                     /db_xref="CDD:439016"
     Site            350..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A2A7Q9.2)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A2A7Q9.2)"
     Region          597..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2A7Q9.2)"
     Region          659..731
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2A7Q9.2)"
     CDS             1..731
                     /gene="Rnf19b"
                     /gene_synonym="4930534K13Rik; 4930555L03Rik; Ibrdc3"
                     /coded_by="NM_029219.2:128..2323"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS51305.1"
                     /db_xref="GeneID:75234"
                     /db_xref="MGI:MGI:1922484"
ORIGIN      
        1 mgsekdsesp rstslhaaap dpkcrsggrr rrltfhsvfs asargrrart kpqaeppppa
       61 apppppppap apveaqappv ealpsepaae aeaeavaagp eedeaaeggg aeevecplcl
      121 vrlpperapr llscphrscr dclrhylrle isesrvpisc pecserlnph dirllladpp
      181 lmhkyeefml rrylasdpdc rwcpapdcgy aviaygcasc pkltceregc qtefcyhckq
      241 iwhpnqtcdm arqqraqtlr vrtkhtsgls ygqesgpddi kpcprcsayi ikmndgscnh
      301 mtcavcgcef cwlcmkeisd lhylspsgct fwgkkpwsrk kkilwqlgtl igapvgisli
      361 agiaipamvi gipvyvgrki hsryegrkts khkrnlaitg gvtlsviasp viaavsvgig
      421 vpimlayvyg vvpislcrgg gcgvstangk gvkiefdedd gpitvadawr alknpsiges
      481 siegltsvls tsgsptdgls vmqgpyseta sfaalsggtl sggilssgkg kysrlevqad
      541 vqkeifpkdt aslgaisdsa stramagsii ssynpqdrec nnmeiqvdie akpshyqlvs
      601 gsstedslhv haqvaekeee gngagggsgg seddppykhq sceqkdclas kawdislaqp
      661 esirsdless dtqsddvpdi tsdecgsprs haaacpstpq vhgapspsah knlaapaegq
      721 tvlkseeyev e
//
LOCUS       NP_001354252             434 aa            linear   PRI 27-APR-2025
DEFINITION  CCA tRNA nucleotidyltransferase 1, mitochondrial isoform 1 [Homo
            sapiens].
ACCESSION   NP_001354252 XP_011532078
VERSION     NP_001354252.1
DBSOURCE    REFSEQ: accession NM_001367323.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Fatica,T., Naas,T., Liwak,U., Slaa,H., Souaid,M., Frangione,B.,
            Kattini,R., Gaudreau-Lapierre,A., Trinkle-Mulcahy,L.,
            Chakraborty,P. and Holcik,M.
  TITLE     TRNT-1 Deficiency Is Associated with Loss of tRNA Integrity and
            Imbalance of Distinct Proteins
  JOURNAL   Genes (Basel) 14 (5), 1043 (2023)
   PUBMED   37239403
  REMARK    GeneRIF: TRNT-1 Deficiency Is Associated with Loss of tRNA
            Integrity and Imbalance of Distinct Proteins.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Seki,M., Komuro,A., Ishikawa,T., Takahashi,M. and Nashimoto,M.
  TITLE     Genes for tRNA recycling are upregulated in response to infection
            with Theiler's mouse encephalitis virus
  JOURNAL   Biochem Biophys Res Commun 587, 63-68 (2022)
   PUBMED   34864548
  REMARK    GeneRIF: Genes for tRNA recycling are upregulated in response to
            infection with Theiler's mouse encephalitis virus.
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Odom,J., Amin,H., Gijavanekar,C., Elsea,S.H., Kralik,S., Chinen,J.,
            Lin,Y., Yates,A.M.M., Mizerik,E., Potocki,L. and Scaglia,F.
  TITLE     A phenotypic expansion of TRNT1 associated sideroblastic anemia
            with immunodeficiency, fevers, and developmental delay
  JOURNAL   Am J Med Genet A 188 (1), 259-268 (2022)
   PUBMED   34510712
  REMARK    GeneRIF: A phenotypic expansion of TRNT1 associated sideroblastic
            anemia with immunodeficiency, fevers, and developmental delay.
            Review article
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Wang,J., Deng,Q., He,X., Chen,D., Hang,S., Gao,Y. and Chen,Y.
  TITLE     Two cases of sideroblastic anemia with B-cell immunodeficiency,
            periodic fevers, and developmental delay (SIFD) syndrome in Chinese
            Han children caused by novel compound heterozygous variants of the
            TRNT1 gene
  JOURNAL   Clin Chim Acta 521, 244-250 (2021)
   PUBMED   34310935
  REMARK    GeneRIF: Two cases of sideroblastic anemia with B-cell
            immunodeficiency, periodic fevers, and developmental delay (SIFD)
            syndrome in Chinese Han children caused by novel compound
            heterozygous variants of the TRNT1 gene.
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Augustin,M.A., Reichert,A.S., Betat,H., Huber,R., Morl,M. and
            Steegborn,C.
  TITLE     Crystal structure of the human CCA-adding enzyme: insights into
            template-independent polymerization
  JOURNAL   J Mol Biol 328 (5), 985-994 (2003)
   PUBMED   12729736
  REMARK    GeneRIF: The crystal structure reveals a four domain architecture
            with a cluster of conserved residues forming a positively charged
            cleft between the first two domains.
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Nagaike,T., Suzuki,T., Tomari,Y., Takemoto-Hori,C., Negayama,F.,
            Watanabe,K. and Ueda,T.
  TITLE     Identification and characterization of mammalian mitochondrial tRNA
            nucleotidyltransferases
  JOURNAL   J Biol Chem 276 (43), 40041-40049 (2001)
   PUBMED   11504732
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Reichert,A.S., Thurlow,D.L. and Morl,M.
  TITLE     A eubacterial origin for the human tRNA nucleotidyltransferase?
  JOURNAL   Biol Chem 382 (10), 1431-1438 (2001)
   PUBMED   11727826
  REMARK    GeneRIF: human gene transcript CGI-47 (#AF151805) was cloned and
            encodes a bona fide CCA-adding enzyme and not a poly(A) polymerase.
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024060.6.
            
            On Nov 21, 2018 this sequence version replaced XP_011532078.1.
            
            Summary: The protein encoded by this gene is a CCA-adding enzyme
            which belongs to the tRNA nucleotidyltransferase/poly(A) polymerase
            family. This essential enzyme functions by catalyzing the addition
            of the conserved nucleotide triplet CCA to the 3' terminus of tRNA
            molecules. Mutations in this gene result in sideroblastic anemia
            with B-cell immunodeficiency, periodic fevers, and developmental
            delay. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.212232.1,
                                           SRR1803614.163649.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p26.2"
     Protein         1..434
                     /product="CCA tRNA nucleotidyltransferase 1, mitochondrial
                     isoform 1"
                     /EC_number="2.7.7.72"
                     /note="mitochondrial CCA-adding
                     tRNA-nucleotidyltransferase; tRNA nucleotidyl transferase,
                     CCA-adding, 1; tRNA-nucleotidyltransferase 1,
                     mitochondrial; CCA tRNA nucleotidyltransferase 1,
                     mitochondrial; mt CCA-adding enzyme; mt tRNA
                     CCA-diphosphorylase; mt tRNA adenylyltransferase; mt tRNA
                     CCA-pyrophosphorylase; tRNA CCA nucleotidyl transferase 1;
                     ATP(CTP):tRNA nucleotidyltransferase"
                     /calculated_mol_wt=44922
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q96Q11.2)"
                     /calculated_mol_wt=5224
     mat_peptide     42..434
                     /product="CCA tRNA nucleotidyltransferase 1,
                     mitochondrial. /id=PRO_0000004782"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q11.2)"
                     /calculated_mol_wt=44922
     Region          43..428
                     /region_name="PcnB"
                     /note="tRNA nucleotidyltransferase/poly(A) polymerase
                     [Translation, ribosomal structure and biogenesis];
                     COG0617"
                     /db_xref="CDD:440382"
     Site            152
                     /site_type="other"
                     /note="May assist in discriminating ATP from CTP.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB1; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            193
                     /site_type="other"
                     /note="Involved in nucleotide selection.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            402
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     CDS             1..434
                     /gene="TRNT1"
                     /gene_synonym="CCA1; CGI-47; MtCCA; RPEM; SIFD"
                     /coded_by="NM_001367323.1:1107..2411"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS2561.2"
                     /db_xref="GeneID:51095"
                     /db_xref="HGNC:HGNC:17341"
                     /db_xref="MIM:612907"
ORIGIN      
        1 mlrclyhwhr pvlnrrwsrl clpkqylftm klqspefqsl fteglkslte lfvkenhelr
       61 iaggavrdll ngvkpqdidf attatptqmk emfqsagirm innrgekhgt itarlheenf
      121 eittlridvt tdgrhaevef ttdwqkdaer rdltinsmfl gfdgtlfdyf ngyedlknkk
      181 vrfvghakqr iqedylrilr yfrfygrivd kpgdhdpetl eaiaenakgl agisgeriwv
      241 elkkilvgnh vnhlihliyd ldvapyiglp anasleefdk vsknvdgfsp kpvtllaslf
      301 kvqddvtkld lrlkiakeek nlglfivknr kdlikatdss dplkpyqdfi idsrepdatt
      361 rvcellkyqg ehcllkemqq wsippfpvsg hdirkvgiss gkeigallqq lreqwkksgy
      421 qmekdellsy ikkt
//
LOCUS       NP_001357514             209 aa            linear   PRI 27-APR-2025
DEFINITION  tudor-interacting repair regulator protein isoform 3 [Homo
            sapiens].
ACCESSION   NP_001357514
VERSION     NP_001357514.1
DBSOURCE    REFSEQ: accession NM_001370585.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Parnandi,N., Rendo,V., Cui,G., Botuyan,M.V., Remisova,M.,
            Nguyen,H., Drane,P., Beroukhim,R., Altmeyer,M., Mer,G. and
            Chowdhury,D.
  TITLE     TIRR inhibits the 53BP1-p53 complex to alter cell-fate programs
  JOURNAL   Mol Cell 81 (12), 2583-2595 (2021)
   PUBMED   33961797
  REMARK    GeneRIF: TIRR inhibits the 53BP1-p53 complex to alter cell-fate
            programs.
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Avolio,R., Jarvelin,A.I., Mohammed,S., Agliarulo,I., Condelli,V.,
            Zoppoli,P., Calice,G., Sarnataro,D., Bechara,E., Tartaglia,G.G.,
            Landriscina,M., Castello,A., Esposito,F. and Matassa,D.S.
  TITLE     Protein Syndesmos is a novel RNA-binding protein that regulates
            primary cilia formation
  JOURNAL   Nucleic Acids Res 46 (22), 12067-12086 (2018)
   PUBMED   30260431
  REMARK    GeneRIF: Identification of a small subset of mRNAs responsible for
            the biogenesis of primary cilium that have been linked to
            developmental and degenerative diseases, known as ciliopathies, and
            cancer. SDOS binds and regulates the translation of several of
            these mRNAs, controlling cilia development.
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Zhang,A., Peng,B., Huang,P., Chen,J. and Gong,Z.
  TITLE     The p53-binding protein 1-Tudor-interacting repair regulator
            complex participates in the DNA damage response
  JOURNAL   J Biol Chem 292 (16), 6461-6467 (2017)
   PUBMED   28213517
  REMARK    GeneRIF: TIRR is a novel 53BP1-interacting protein that
            participates in the DNA damage response
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Song,M.G., Li,Y. and Kiledjian,M.
  TITLE     Multiple mRNA decapping enzymes in mammalian cells
  JOURNAL   Mol Cell 40 (3), 423-432 (2010)
   PUBMED   21070968
REFERENCE   9  (residues 1 to 209)
  AUTHORS   Taylor,M.J. and Peculis,B.A.
  TITLE     Evolutionary conservation supports ancient origin for Nudt16, a
            nuclear-localized, RNA-binding, RNA-decapping enzyme
  JOURNAL   Nucleic Acids Res 36 (18), 6021-6034 (2008)
   PUBMED   18820299
REFERENCE   10 (residues 1 to 209)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023830.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI823073.1, DRR138528.751381.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..209
                     /product="tudor-interacting repair regulator protein
                     isoform 3"
                     /note="protein syndesmos; NUDT16-like protein 1; nudix
                     (nucleoside diphosphate linked moiety X)-type motif
                     16-like 1; tudor-interacting repair regulator protein"
                     /calculated_mol_wt=22948
     Site            10
                     /site_type="other"
                     /note="Required for interaction with TP53BP1.
                     /evidence=ECO:0000269|PubMed:28241136; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ7.1)"
     Region          23..192
                     /region_name="NUDIX_U8_SnoRNA_DE_Nudt16"
                     /note="nucleoside diphosphate-linked moiety X)) motif 16;
                     cd18869"
                     /db_xref="CDD:467581"
     Region          116..203
                     /region_name="Interaction with PXN.
                     /evidence=ECO:0000250|UniProtKB:Q8VHN8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRJ7.1)"
     CDS             1..209
                     /gene="NUDT16L1"
                     /gene_synonym="SDOS; TIRR"
                     /coded_by="NM_001370585.1:10..639"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84309"
                     /db_xref="HGNC:HGNC:28154"
                     /db_xref="MIM:617338"
ORIGIN      
        1 mstaavpelk qisrveamrl gpgwshscha mlyaanpgql fgripmrfsv lmrfdgllgf
       61 pggfvdrrfw sledglnrvl glglgclrlt eadylsshlt egphrvvahl yarqltleql
      121 haveisavhs rdhglevlgl vrvplytqkd rvggfpnfls nafvstakcq llfalkvlnm
      181 mpeeklveal aaatekqkka lekllpass
//
LOCUS       NP_001353520             805 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 20 [Homo
            sapiens].
ACCESSION   NP_001353520 XP_011538785
VERSION     NP_001353520.1
DBSOURCE    REFSEQ: accession NM_001366591.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 805)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 805)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 805)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 805)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 805)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 805)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 805)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_011538785.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.78566.1,
                                           SRR1803612.204464.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..805
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 20"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=90455
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <38..126
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <507..>641
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..805
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366591.1:2055..4472"
                     /note="isoform 20 is encoded by transcript variant 31"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rtksrspspa pekkektpel pepsvkvkep
      121 svqeatstsd ilkvpkpepi pepkepspek nskkekekek trprsrsrsk srsrtrsrsp
      181 shtrprrrhr srsrsysprr rpsprrrpsp rrrtpprrmp ppprhrrsrs pvrrrrrssa
      241 slsgssssss ssrsrsppkk ppkrtssppr ktrrlspsas pprrrhrpsp patpppktrh
      301 sptpqqsnrt rksrvsvspg rtsgkvtkhk gtekrespsp apkprkvels eseedkggkm
      361 aaadsvqqrr qyrrqnqqss sdsgssssse derpkrshvk ngevgrrrrh spsrsaspsp
      421 rkrqketspr mqmgkrwqsp vtksgrrrrs psppptrrrr spspappprr rrtptppprr
      481 rtpsppprrr spsprryspp iqrryspspp pkrrtasppp ppkrraspsp ppkrrvshsp
      541 ppkqrsspvt krrspslssk hrkgsspsrs trearspqpn krhspsprpr apqtsssppp
      601 vrrgassspq rrqspspstr pirrvsrtpe pkkikkaasp spqsvrrvss srsvsgspep
      661 aakkppapps pvqsqspstn wspavpvkka ksptpspspp rnsdqegggk kkkkkkdkkh
      721 kkdkkhkkhk khkkekavaa aaaaavtpaa iaaatttlaq eepvaapepk keteseaedn
      781 lddlekhlre kalrsmrkaq vspqs
//
LOCUS       NP_001624                352 aa            linear   PRI 27-APR-2025
DEFINITION  protein AMBP preproprotein [Homo sapiens].
ACCESSION   NP_001624
VERSION     NP_001624.1
DBSOURCE    REFSEQ: accession NM_001633.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Jin,L., Niu,C. and Ni,Y.
  TITLE     Correlation between peripheral blood alpha1-MG, DNMT1 expression,
            and the severity of diabetic nephropathy renal pathological damage
  JOURNAL   Medicine (Baltimore) 102 (42), e35409 (2023)
   PUBMED   37861555
  REMARK    GeneRIF: Correlation between peripheral blood alpha1-MG, DNMT1
            expression, and the severity of diabetic nephropathy renal
            pathological damage.
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Xu,Y., Carr,P.D., Guss,J.M. and Ollis,D.L.
  TITLE     The crystal structure of bikunin from the inter-alpha-inhibitor
            complex: a serine protease inhibitor with two Kunitz domains
  JOURNAL   J Mol Biol 276 (5), 955-966 (1998)
   PUBMED   9566199
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Vetr,H. and Gebhard,W.
  TITLE     Structure of the human alpha 1-microglobulin-bikunin gene
  JOURNAL   Biol Chem Hoppe Seyler 371 (12), 1185-1196 (1990)
   PUBMED   1708673
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Diarra-Mehrpour,M., Bourguignon,J., Sesboue,R., Salier,J.P.,
            Leveillard,T. and Martin,J.P.
  TITLE     Structural analysis of the human inter-alpha-trypsin inhibitor
            light-chain gene
  JOURNAL   Eur J Biochem 191 (1), 131-139 (1990)
   PUBMED   1696200
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Schreitmuller,T., Hochstrasser,K., Reisinger,P.W., Wachter,E. and
            Gebhard,W.
  TITLE     cDNA cloning of human inter-alpha-trypsin inhibitor discloses three
            different proteins
  JOURNAL   Biol Chem Hoppe Seyler 368 (8), 963-970 (1987)
   PUBMED   3663330
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Kaumeyer,J.F., Polazzi,J.O. and Kotick,M.P.
  TITLE     The mRNA for a proteinase inhibitor related to the HI-30 domain of
            inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin
            (protein HC)
  JOURNAL   Nucleic Acids Res 14 (20), 7839-7850 (1986)
   PUBMED   2430261
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Traboni,C. and Cortese,R.
  TITLE     Sequence of a full length cDNA coding for human protein HC (alpha 1
            microglobulin)
  JOURNAL   Nucleic Acids Res 14 (15), 6340 (1986)
   PUBMED   2428011
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Lopez Otin,C., Grubb,A.O. and Mendez,E.
  TITLE     The complete amino acid sequence of human complex-forming
            glycoprotein heterogeneous in charge (protein HC) from one
            individual
  JOURNAL   Arch Biochem Biophys 228 (2), 544-554 (1984)
   PUBMED   6198962
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Takagi,T., Takagi,K. and Kawai,T.
  TITLE     Complete amino acid sequence of human alpha 1-microglobulin
  JOURNAL   Biochem Biophys Res Commun 98 (4), 997-1001 (1981)
   PUBMED   6164372
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Ekstrom,B. and Berggard,I.
  TITLE     Human alpha1-microglobulin. Purification procedure, chemical and
            physiochemical properties
  JOURNAL   J Biol Chem 252 (22), 8048-8057 (1977)
   PUBMED   72071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC041593.1.
            
            Summary: This gene encodes a complex glycoprotein secreted in
            plasma. The precursor is proteolytically processed into distinct
            functioning proteins: alpha-1-microglobulin, which belongs to the
            superfamily of lipocalin transport proteins and may play a role in
            the regulation of inflammatory processes, and bikunin, which is a
            urinary trypsin inhibitor belonging to the superfamily of
            Kunitz-type protease inhibitors and plays an important role in many
            physiological and pathological processes. This gene is located on
            chromosome 9 in a cluster of lipocalin genes. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC041593.1, SRR5189652.12257.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265132.8/ ENSP00000265132.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..352
                     /product="protein AMBP preproprotein"
                     /note="protein HC; complex-forming glycoprotein
                     heterogeneous in charge; uronic-acid-rich protein;
                     trypstatin; bikunin; inter-alpha-trypsin inhibitor light
                     chain; protein AMBP; uristatin; growth-inhibiting protein
                     19"
                     /calculated_mol_wt=37115
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1902
     mat_peptide     20..203
                     /product="Alpha-1-microglobulin. /id=PRO_0000017886"
                     /note="propagated from UniProtKB/Swiss-Prot (P02760.1)"
                     /calculated_mol_wt=20847
     Site            24
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1694784. /id=CAR_000172;
                     propagated from UniProtKB/Swiss-Prot (P02760.1)"
     Region          28..190
                     /region_name="lipocalin_A1M-like"
                     /note="lipocalin domain of alpha1-microglobulin and
                     similar proteins; cd19418"
                     /db_xref="CDD:381193"
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:1694784; propagated from
                     UniProtKB/Swiss-Prot (P02760.1)"
     Site            order(40,44,68,70,79,81,83,94,96,98,107,109,118,120,122,
                     131,133,135,147,149,151)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381193"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:1694784,
                     ECO:0000269|PubMed:22171320; propagated from
                     UniProtKB/Swiss-Prot (P02760.1)"
     Site            199
                     /site_type="cleavage"
                     /note="Cleavage, in the presence of oxyhemoglobin or MPO.
                     /evidence=ECO:0000269|PubMed:11877257; propagated from
                     UniProtKB/Swiss-Prot (P02760.1)"
     mat_peptide     206..352
                     /product="Inter-alpha-trypsin inhibitor light chain.
                     /id=PRO_0000017887"
                     /note="propagated from UniProtKB/Swiss-Prot (P02760.1)"
                     /calculated_mol_wt=15974
     Region          206..226
                     /region_name="Glycopeptide (secretory piece)"
                     /note="propagated from UniProtKB/Swiss-Prot (P02760.1)"
     Site            215
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:1898736,
                     ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:32337544,
                     ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717,
                     ECO:0000269|PubMed:6171497, ECO:0000269|PubMed:7682553;
                     propagated from UniProtKB/Swiss-Prot (P02760.1)"
     Region          229..282
                     /region_name="Kunitz_bikunin_1-like"
                     /note="first Kunitz domain of bikunin and similar
                     proteins; cd22596"
                     /db_xref="CDD:438639"
     Site            order(237..241,243..245,260,264)
                     /site_type="other"
                     /note="putative serine protease binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438639"
     Site            241..242
                     /site_type="inhibition"
                     /note="Inhibitory (P1) (chymotrypsin, elastase).
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P02760.1)"
     Site            250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:22171320,
                     ECO:0000269|PubMed:6171497; propagated from
                     UniProtKB/Swiss-Prot (P02760.1)"
     mat_peptide     284..344
                     /product="Trypstatin. /evidence=ECO:0000250.
                     /id=PRO_0000318926"
                     /note="propagated from UniProtKB/Swiss-Prot (P02760.1)"
                     /calculated_mol_wt=6620
     Region          284..338
                     /region_name="Kunitz_bikunin_2-like"
                     /note="second Kunitz domain of bikunin and similar
                     proteins; cd22597"
                     /db_xref="CDD:438640"
     Site            order(295..300,318..321)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438640"
     Site            297..298
                     /site_type="inhibition"
                     /note="Inhibitory (P1) (trypsin). /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P02760.1)"
     CDS             1..352
                     /gene="AMBP"
                     /gene_synonym="A1M; EDC1; HCP; HI30; IATIL; ITI; ITIL;
                     ITILC; UTI"
                     /coded_by="NM_001633.4:92..1150"
                     /db_xref="CCDS:CCDS6800.1"
                     /db_xref="GeneID:259"
                     /db_xref="HGNC:HGNC:453"
                     /db_xref="MIM:176870"
ORIGIN      
        1 mrslgallll lsaclavsag pvptppdniq vqenfnisri ygkwynlaig stcpwlkkim
       61 drmtvstlvl gegateaeis mtstrwrkgv ceetsgayek tdtdgkflyh kskwnitmes
      121 yvvhtnydey aifltkkfsr hhgptitakl ygrapqlret llqdfrvvaq gvgipedsif
      181 tmadrgecvp geqepepili prvrravlpq eeegsgggql vtevtkkeds cqlgysagpc
      241 mgmtsryfyn gtsmacetfq yggcmgngnn fvtekeclqt crtvaacnlp ivrgpcrafi
      301 qlwafdavkg kcvlfpyggc qgngnkfyse kecreycgvp gdgdeellrf sn
//
LOCUS       NP_733934                166 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein uL11m isoform b [Homo sapiens].
ACCESSION   NP_733934
VERSION     NP_733934.1
DBSOURCE    REFSEQ: accession NM_170738.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Jager,S., Cimermancic,P., Gulbahce,N., Johnson,J.R., McGovern,K.E.,
            Clarke,S.C., Shales,M., Mercenne,G., Pache,L., Li,K., Hernandez,H.,
            Jang,G.M., Roth,S.L., Akiva,E., Marlett,J., Stephens,M., D'Orso,I.,
            Fernandes,J., Fahey,M., Mahon,C., O'Donoghue,A.J., Todorovic,A.,
            Morris,J.H., Maltby,D.A., Alber,T., Cagney,G., Bushman,F.D.,
            Young,J.A., Chanda,S.K., Sundquist,W.I., Kortemme,T.,
            Hernandez,R.D., Craik,C.S., Burlingame,A., Sali,A., Frankel,A.D.
            and Krogan,N.J.
  TITLE     Global landscape of HIV-human protein complexes
  JOURNAL   Nature 481 (7381), 365-370 (2011)
   PUBMED   22190034
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Han,M.J., Cimen,H., Miller-Lee,J.L., Koc,H. and Koc,E.C.
  TITLE     Purification of human mitochondrial ribosomal L7/L12 stalk proteins
            and reconstitution of functional hybrid ribosomes in Escherichia
            coli
  JOURNAL   Protein Expr Purif 78 (1), 48-54 (2011)
   PUBMED   21453772
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Structural compensation for the deficit of rRNA with proteins in
            the mammalian mitochondrial ribosome. Systematic analysis of
            protein components of the large ribosomal subunit from mammalian
            mitochondria
  JOURNAL   J Biol Chem 276 (24), 21724-21736 (2001)
   PUBMED   11279069
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002748.4.
            
            Summary: This nuclear gene encodes a 39S subunit component of the
            mitochondial ribosome. Alternative splicing results in multiple
            transcript variants. Pseudogenes for this gene are found on
            chromosomes 5 and 12. [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1, which
            results in an isoform (b) that lacks an internal segment of
            sequence, compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3765690.1,
                                           SRR18074967.3585870.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..166
                     /product="large ribosomal subunit protein uL11m isoform b"
                     /note="39S ribosomal protein L11, mitochondrial;
                     mitochondrial large ribosomal subunit protein uL11m"
                     /calculated_mol_wt=18074
     Region          16..129
                     /region_name="Ribosomal_L11"
                     /note="Ribosomal protein L11. Ribosomal protein L11,
                     together with proteins L10 and L7/L12, and 23S rRNA, form
                     the L7/L12 stalk on the surface of the large subunit of
                     the ribosome. The homologous eukaryotic cytoplasmic
                     protein is also called 60S ribosomal...; cd00349"
                     /db_xref="CDD:100101"
     Site            order(43,45..48,52,54..55,99..100,107..108)
                     /site_type="other"
                     /note="L7/L12 interface [polypeptide binding]"
                     /db_xref="CDD:100101"
     Site            order(60..62,66,73,98,107..109,113,116..117,120..121,
                     123..125)
                     /site_type="other"
                     /note="23S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:100101"
     Site            order(79,82)
                     /site_type="other"
                     /note="L25 interface [polypeptide binding]"
                     /db_xref="CDD:100101"
     CDS             1..166
                     /gene="MRPL11"
                     /gene_synonym="CGI-113; L11MT; MRP-L11; uL11m"
                     /coded_by="NM_170738.4:95..595"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44655.1"
                     /db_xref="GeneID:65003"
                     /db_xref="HGNC:HGNC:14042"
                     /db_xref="MIM:611826"
ORIGIN      
        1 msklgraarg lrkpergvsi nqfckefner tkdikegipl ptkilvkpdr tfeikigqpt
       61 vsyflkaaag iekgarqtgk evaglvtlkh vyeiarikaq deafalqdvp lssvvrsiig
      121 sarslgirvv kdlsseelaa fqkeraifla aqkeadlaaq eeaakk
//
LOCUS       NP_071370                608 aa            linear   PRI 27-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 11 isoform 1 [Homo
            sapiens].
ACCESSION   NP_071370
VERSION     NP_071370.2
DBSOURCE    REFSEQ: accession NM_022087.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Gorski,M., Tin,A., Garnaas,M., McMahon,G.M., Chu,A.Y., Tayo,B.O.,
            Pattaro,C., Teumer,A., Chasman,D.I., Chalmers,J., Hamet,P.,
            Tremblay,J., Woodward,M., Aspelund,T., Eiriksdottir,G.,
            Gudnason,V., Harris,T.B., Launer,L.J., Smith,A.V., Mitchell,B.D.,
            O'Connell,J.R., Shuldiner,A.R., Coresh,J., Li,M., Freudenberger,P.,
            Hofer,E., Schmidt,H., Schmidt,R., Holliday,E.G., Mitchell,P.,
            Wang,J.J., de Boer,I.H., Li,G., Siscovick,D.S., Kutalik,Z.,
            Corre,T., Vollenweider,P., Waeber,G., Gupta,J., Kanetsky,P.A.,
            Hwang,S.J., Olden,M., Yang,Q., de Andrade,M., Atkinson,E.J.,
            Kardia,S.L., Turner,S.T., Stafford,J.M., Ding,J., Liu,Y.,
            Barlassina,C., Cusi,D., Salvi,E., Staessen,J.A., Ridker,P.M.,
            Grallert,H., Meisinger,C., Muller-Nurasyid,M., Kramer,B.K.,
            Kramer,H., Rosas,S.E., Nolte,I.M., Penninx,B.W., Snieder,H.,
            Fabiola Del Greco,M., Franke,A., Nothlings,U., Lieb,W.,
            Bakker,S.J., Gansevoort,R.T., van der Harst,P., Dehghan,A.,
            Franco,O.H., Hofman,A., Rivadeneira,F., Sedaghat,S.,
            Uitterlinden,A.G., Coassin,S., Haun,M., Kollerits,B.,
            Kronenberg,F., Paulweber,B., Aumann,N., Endlich,K., Pietzner,M.,
            Volker,U., Rettig,R., Chouraki,V., Helmer,C., Lambert,J.C.,
            Metzger,M., Stengel,B., Lehtimaki,T., Lyytikainen,L.P.,
            Raitakari,O., Johnson,A., Parsa,A., Bochud,M., Heid,I.M.,
            Goessling,W., Kottgen,A., Kao,W.H., Fox,C.S. and Boger,C.A.
  TITLE     Genome-wide association study of kidney function decline in
            individuals of European descent
  JOURNAL   Kidney Int 87 (5), 1017-1029 (2015)
   PUBMED   25493955
  REMARK    GeneRIF: possible role in the deterioration of kidney function
            [meta-analysis]
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Libisch,M.G., Casas,M., Chiribao,M., Moreno,P., Cayota,A.,
            Osinaga,E., Oppezzo,P. and Robello,C.
  TITLE     GALNT11 as a new molecular marker in chronic lymphocytic leukemia
  JOURNAL   Gene 533 (1), 270-279 (2014)
   PUBMED   24076351
  REMARK    GeneRIF: evidence suggests that CLL patient samples harbor aberrant
            O-glycosylation highlighted by Tn antigen expression and that the
            over-expression of GALNT11 constitutes a new molecular marker for
            CLL
REFERENCE   4  (residues 1 to 608)
  AUTHORS   Boskovski,M.T., Yuan,S., Pedersen,N.B., Goth,C.K., Makova,S.,
            Clausen,H., Brueckner,M. and Khokha,M.K.
  TITLE     The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia
            type and laterality
  JOURNAL   Nature 504 (7480), 456-459 (2013)
   PUBMED   24226769
REFERENCE   5  (residues 1 to 608)
  AUTHORS   Yuasa,I., Umetsu,K., Matsusue,A., Nishimukai,H., Harihara,S.,
            Fukumori,Y., Saitou,N., Jin,F., Chattopadhyay,P.K., Henke,L. and
            Henke,J.
  TITLE     A Japanese-specific allele in the GALNT11 gene
  JOURNAL   Leg Med (Tokyo) 12 (4), 208-211 (2010)
   PUBMED   20547088
  REMARK    GeneRIF: Single nucleiotide polymorphism in the GALNT11 genes were
            investigated to assess allele frequencies in different populations.
            This SNP would be useful marker for forensic individualization, in
            particular, as ancestry-informative markers.
            GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 608)
  AUTHORS   Bennett,E.P., Chen,Y.W., Schwientek,T., Mandel,U., Schjoldager,Kt.,
            Cohen,S.M. and Clausen,H.
  TITLE     Rescue of Drosophila Melanogaster l(2)35Aa lethality is only
            mediated by polypeptide GalNAc-transferase pgant35A, but not by the
            evolutionary conserved human ortholog GalNAc-transferase-T11
  JOURNAL   Glycoconj J 27 (4), 435-444 (2010)
   PUBMED   20422447
  REMARK    GeneRIF: GALNT11, the human ortholog to Drosophila melanogaster
            pgant35A, was shown not to support rescue of the l(2)35Aa lethality
            during Drosophila embryogenesis.
REFERENCE   7  (residues 1 to 608)
  AUTHORS   Schwientek,T., Bennett,E.P., Flores,C., Thacker,J., Hollmann,M.,
            Reis,C.A., Behrens,J., Mandel,U., Keck,B., Schafer,M.A.,
            Haselmann,K., Zubarev,R., Roepstorff,P., Burchell,J.M.,
            Taylor-Papadimitriou,J., Hollingsworth,M.A. and Clausen,H.
  TITLE     Functional conservation of subfamilies of putative
            UDP-N-acetylgalactosamine:polypeptide
            N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis
            elegans, and mammals. One subfamily composed of l(2)35Aa is
            essential in Drosophila
  JOURNAL   J Biol Chem 277 (25), 22623-22638 (2002)
   PUBMED   11925450
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006017.2.
            
            On Jul 25, 2007 this sequence version replaced NP_071370.1.
            
            Transcript Variant: This variant (1), as well as variants 3-8,
            encodes isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.472144.1,
                                           SRR3476690.1053710.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000430044.7/ ENSP00000395122.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..608
                     /product="polypeptide N-acetylgalactosaminyltransferase 11
                     isoform 1"
                     /EC_number="2.4.1.41"
                     /note="pp-GaNTase 11; polypeptide GalNAc transferase 11;
                     protein-UDP acetylgalactosaminyltransferase 11;
                     UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
                     11; UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 11 (GalNAc-T11)"
                     /calculated_mol_wt=68788
     Site            7..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCW6.2)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q921L8; propagated from
                     UniProtKB/Swiss-Prot (Q8NCW6.2)"
     Region          150..261
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCW6.2)"
     Region          154..452
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(158..160,162,191,222,225,229,245..247,327..328,
                     350..351,353,378,381,386)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(245,247,378)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          319..381
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCW6.2)"
     Site            428
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NCW6.2)"
     Region          478..606
                     /region_name="beta-trefoil_Ricin_GALNT11"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide N-acetylgalactosaminyltransferase 11
                     (GALNT11) and similar proteins; cd23440"
                     /db_xref="CDD:467318"
     Site            order(495..498,508,510,513,518..519)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467318"
     Site            order(538..541,549,551,554,559..560)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467318"
     Site            order(580..583,592,594,597,601..602)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467318"
     CDS             1..608
                     /gene="GALNT11"
                     /gene_synonym="GALNAC-T11; GALNACT11"
                     /coded_by="NM_022087.4:250..2076"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5930.1"
                     /db_xref="GeneID:63917"
                     /db_xref="HGNC:HGNC:19875"
                     /db_xref="MIM:615130"
ORIGIN      
        1 mgsvtvryfc ygclftsatw tvllfvyfnf sevtqplknv pvkgsgphgp spkkfyprft
       61 rgpsrvlepq fkankiddvi dsrvedpeeg hlkfsselgm ifnerdqelr dlgyqkhafn
      121 mlisdrlgyh rdvpdtrnaa ckekfyppdl paasvvicfy neafsallrt vhsvidrtpa
      181 hllheiilvd ddsdfddlkg eldeyvqkyl pgkikvirnt kreglirgrm igaahatgev
      241 lvfldshcev nvmwlqplla airedrhtvv cpvidiisad tlayssspvv rggfnwglhf
      301 kwdlvplsel graegatapi ksptmagglf amnrqyfhel gqydsgmdiw ggenleisfr
      361 iwmcggklfi ipcsrvghif rkrrpygspe gqdtmthnsl rlahvwldey keqyfslrpd
      421 lktksygnis ervelrkklg cksfkwyldn vypemqisgs hakpqqpifv nrgpkrpkvl
      481 qrgrlyhlqt nkclvaqgrp sqkgglvvlk acdysdpnqi wiyneehelv lnsllcldms
      541 etrssdpprl mkchgsggsq qwtfgknnrl yqvsvgqclr avdplgqkgs vamaicdgss
      601 sqqwhleg
//
LOCUS       NP_057313                276 aa            linear   PRI 27-APR-2025
DEFINITION  NADH-cytochrome b5 reductase 2 isoform 1 [Homo sapiens].
ACCESSION   NP_057313
VERSION     NP_057313.2
DBSOURCE    REFSEQ: accession NM_016229.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Chen,J., Sun,Y., Chen,L. and Zhou,Y.
  TITLE     NADH-Cytochrome B5 reductase 2 suppresses retinal vascular
            dysfunction through regulation of vascular endothelial growth
            factor A in diabetic retinopathy
  JOURNAL   Exp Eye Res 222, 109186 (2022)
   PUBMED   35820466
  REMARK    GeneRIF: NADH-Cytochrome B5 reductase 2 suppresses retinal vascular
            dysfunction through regulation of vascular endothelial growth
            factor A in diabetic retinopathy.
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Chen,J., Liao,L., Xu,H., Zhang,Z. and Zhang,J.
  TITLE     Long non-coding RNA MEG3 inhibits neovascularization in diabetic
            retinopathy by regulating microRNA miR-6720-5p and cytochrome B5
            reductase 2
  JOURNAL   Bioengineered 12 (2), 11872-11884 (2021)
   PUBMED   34978518
  REMARK    GeneRIF: Long non-coding RNA MEG3 inhibits neovascularization in
            diabetic retinopathy by regulating microRNA miR-6720-5p and
            cytochrome B5 reductase 2.
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Jo,Y.S., Kim,M.S., Yoo,N.J. and Lee,S.H.
  TITLE     Intratumoral Heterogeneity for Inactivating Frameshift Mutation of
            CYB5R2 Gene in Colorectal Cancers
  JOURNAL   Pathol Oncol Res 26 (1), 585-586 (2020)
   PUBMED   29532410
  REMARK    GeneRIF: Intratumoral Heterogeneity for Inactivating Frameshift
            Mutation of CYB5R2 Gene in Colorectal Cancers.
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Liu,Q., Liu,Y., Li,W., Wang,X., Sawaya,R., Lang,F.F., Yung,W.K.,
            Chen,K., Fuller,G.N. and Zhang,W.
  TITLE     Genetic, epigenetic, and molecular landscapes of multifocal and
            multicentric glioblastoma
  JOURNAL   Acta Neuropathol 130 (4), 587-597 (2015)
   PUBMED   26323991
  REMARK    GeneRIF: Study showed that multifocal or multicentric glioblastomas
            have some underlying genetic and epigenetic characteristics that
            are associated with poor prognosis and that CYB5R2 is a new
            epigenetic marker for glioblastoma prognosis
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Xiao,X., Zhao,W., Tian,F., Zhou,X., Zhang,J., Huang,T., Hou,B.,
            Du,C., Wang,S., Mo,Y., Yu,N., Zhou,S., You,J., Zhang,Z., Huang,G.
            and Zeng,X.
  TITLE     Cytochrome b5 reductase 2 is a novel candidate tumor suppressor
            gene frequently inactivated by promoter hypermethylation in human
            nasopharyngeal carcinoma
  JOURNAL   Tumour Biol 35 (4), 3755-3763 (2014)
   PUBMED   24338690
  REMARK    GeneRIF: findings suggest that CYB5R2 may be a functional tumor
            suppressor gene, frequently inactivated by hypermethylation of its
            promoter in nasopharyngeal carcinoma
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Franceschini,N., Fox,E., Zhang,Z., Edwards,T.L., Nalls,M.A.,
            Sung,Y.J., Tayo,B.O., Sun,Y.V., Gottesman,O., Adeyemo,A.,
            Johnson,A.D., Young,J.H., Rice,K., Duan,Q., Chen,F., Li,Y.,
            Tang,H., Fornage,M., Keene,K.L., Andrews,J.S., Smith,J.A.,
            Faul,J.D., Guangfa,Z., Guo,W., Liu,Y., Murray,S.S., Musani,S.K.,
            Srinivasan,S., Velez Edwards,D.R., Wang,H., Becker,L.C., Bovet,P.,
            Bochud,M., Broeckel,U., Burnier,M., Carty,C., Chasman,D.I.,
            Ehret,G., Chen,W.M., Chen,G., Chen,W., Ding,J., Dreisbach,A.W.,
            Evans,M.K., Guo,X., Garcia,M.E., Jensen,R., Keller,M.F., Lettre,G.,
            Lotay,V., Martin,L.W., Moore,J.H., Morrison,A.C., Mosley,T.H.,
            Ogunniyi,A., Palmas,W., Papanicolaou,G., Penman,A., Polak,J.F.,
            Ridker,P.M., Salako,B., Singleton,A.B., Shriner,D., Taylor,K.D.,
            Vasan,R., Wiggins,K., Williams,S.M., Yanek,L.R., Zhao,W.,
            Zonderman,A.B., Becker,D.M., Berenson,G., Boerwinkle,E.,
            Bottinger,E., Cushman,M., Eaton,C., Nyberg,F., Heiss,G.,
            Hirschhron,J.N., Howard,V.J., Karczewsk,K.J., Lanktree,M.B.,
            Liu,K., Liu,Y., Loos,R., Margolis,K., Snyder,M., Psaty,B.M.,
            Schork,N.J., Weir,D.R., Rotimi,C.N., Sale,M.M., Harris,T.,
            Kardia,S.L., Hunt,S.C., Arnett,D., Redline,S., Cooper,R.S.,
            Risch,N.J., Rao,D.C., Rotter,J.I., Chakravarti,A., Reiner,A.P.,
            Levy,D., Keating,B.J. and Zhu,X.
  CONSRTM   Asian Genetic Epidemiology Network Consortium
  TITLE     Genome-wide association analysis of blood-pressure traits in
            African-ancestry individuals reveals common associated genes in
            African and non-African populations
  JOURNAL   Am J Hum Genet 93 (3), 545-554 (2013)
   PUBMED   23972371
REFERENCE   8  (residues 1 to 276)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 276)
  AUTHORS   Baker,M.A., Krutskikh,A., Curry,B.J., Hetherington,L. and
            Aitken,R.J.
  TITLE     Identification of cytochrome-b5 reductase as the enzyme responsible
            for NADH-dependent lucigenin chemiluminescence in human spermatozoa
  JOURNAL   Biol Reprod 73 (2), 334-342 (2005)
   PUBMED   15858218
  REMARK    GeneRIF: CYB5R2 is a key enzyme involved in the mediation of
            NADH-induced redox activity in human spermatozoa.
REFERENCE   10 (residues 1 to 276)
  AUTHORS   Zhu,H., Qiu,H., Yoon,H.W., Huang,S. and Bunn,H.F.
  TITLE     Identification of a cytochrome b-type NAD(P)H oxidoreductase
            ubiquitously expressed in human cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 14742-14747 (1999)
   PUBMED   10611283
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104237.2, CB149369.1 and
            AY665398.1.
            
            On May 28, 2004 this sequence version replaced NP_057313.1.
            
            Summary: The protein encoded by this gene belongs to the
            flavoprotein pyridine nucleotide cytochrome reductase family of
            proteins. Cytochrome b-type NAD(P)H oxidoreductases are implicated
            in many processes including cholesterol biosynthesis, fatty acid
            desaturation and elongation, and respiratory burst in neutrophils
            and macrophages. Cytochrome b5 reductases have soluble and
            membrane-bound forms that are the product of alternative splicing.
            In animal cells, the membrane-bound form binds to the endoplasmic
            reticulum, where it is a member of a fatty acid desaturation
            complex. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Nov 2014].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein
            (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.53345.1,
                                           SRR5189667.1732.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299498.11/ ENSP00000299498.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..276
                     /product="NADH-cytochrome b5 reductase 2 isoform 1"
                     /EC_number="1.6.2.2"
                     /note="cytochrome b5 reductase b5R.2; NADH-cytochrome b5
                     reductase 2"
                     /calculated_mol_wt=31327
     Region          <8..276
                     /region_name="PLN02252"
                     /note="nitrate reductase [NADPH]"
                     /db_xref="CDD:215141"
     Site            17
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P00387; propagated from
                     UniProtKB/Swiss-Prot (Q6BCY4.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00387; propagated from
                     UniProtKB/Swiss-Prot (Q6BCY4.1)"
     CDS             1..276
                     /gene="CYB5R2"
                     /gene_synonym="B5R.2"
                     /coded_by="NM_016229.5:149..979"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7780.1"
                     /db_xref="GeneID:51700"
                     /db_xref="HGNC:HGNC:24376"
                     /db_xref="MIM:608342"
ORIGIN      
        1 mnsrrrepit lqdpeakypl pliekekish ntrrfrfglp spdhvlglpv gnyvqllaki
       61 dnelvvrayt pvssdddrgf vdliikiyfk nvhpqypegg kmtqylenmk igetiffrgp
      121 rgrlfyhgpg nlgirpdqts epkktladhl gmiaggtgit pmlqlirhit kdpsdrtrms
      181 lifanqteed ilvrkeleei arthpdqfnl wytldrppig wkyssgfvta dmikehlppp
      241 akstlilvcg pppliqtaah pnleklgytq dmifty
//
LOCUS       NP_066549                314 aa            linear   PRI 27-APR-2025
DEFINITION  ecto-ADP-ribosyltransferase 4 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_066549
VERSION     NP_066549.2
DBSOURCE    REFSEQ: accession NM_021071.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Wangmo,T., Intharanut,K., Leetrakool,N., Mitundee,S.,
            Bejrachandra,S. and Nathalang,O.
  TITLE     Development of DO*A and DO*B Allele Detections to Predict
            Transfusion-Induced Alloimmunization Risks in Thai Populations
  JOURNAL   Clin Lab 67 (10) (2021)
   PUBMED   34655192
  REMARK    GeneRIF: Development of DO*A and DO*B Allele Detections to Predict
            Transfusion-Induced Alloimmunization Risks in Thai Populations.
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Morin,P.A., Ethier,C., Lavoie,J., Robitaille,N. and Baillargeon,N.
  TITLE     A novel variant DO*A allele with a c.370delT mutation leading to a
            DO-null phenotype in a Syrian family
  JOURNAL   Transfusion 61 (2), E16-E17 (2021)
   PUBMED   33206405
  REMARK    GeneRIF: A novel variant DO*A allele with a c.370delT mutation
            leading to a DO-null phenotype in a Syrian family.
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Durousseau de Coulgeans,C., Chiaroni,J., Bailly,P. and
            Chapel-Fernandes,S.
  TITLE     Sequencing of the ART4 gene in sub-Saharan cohorts reveals ethnic
            differences and two new DO alleles: DO*B-Ile5Thr and DO*B-Trp266Arg
  JOURNAL   Transfusion 55 (10), 2376-2383 (2015)
   PUBMED   25988428
  REMARK    GeneRIF: Characterization of two novel DO*B alleles highlights the
            value of testing selected ethnic groups in understanding DO allele
            diversity.
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Rios,M., Hue-Roye,K., Oyen,R., Miller,J. and Reid,M.E.
  TITLE     Insights into the Holley- and Joseph- phenotypes
  JOURNAL   Transfusion 42 (1), 52-58 (2002)
   PUBMED   11896313
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Wu,G.G., Jin,S.Z., Deng,Z.H. and Zhao,T.M.
  TITLE     Polymerase chain reaction with sequence-specific primers-based
            genotyping of the human Dombrock blood group DO1 and DO2 alleles
            and the DO gene frequencies in Chinese blood donors
  JOURNAL   Vox Sang 81 (1), 49-51 (2001)
   PUBMED   11520417
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Gubin,A.N., Njoroge,J.M., Wojda,U., Pack,S.D., Rios,M., Reid,M.E.
            and Miller,J.L.
  TITLE     Identification of the dombrock blood group glycoprotein as a
            polymorphic member of the ADP-ribosyltransferase gene family
  JOURNAL   Blood 96 (7), 2621-2627 (2000)
   PUBMED   11001920
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Mauthe,J., Coghlan,G. and Zelinski,T.
  TITLE     Confirmation of the assignment of the Dombrock blood group locus
            (DO) to chromosome 12p: narrowing the boundaries to 12p12.3-p13.2
  JOURNAL   Vox Sang 79 (1), 53-56 (2000)
   PUBMED   10971215
REFERENCE   8  (residues 1 to 314)
  AUTHORS   Koch-Nolte,F., Haag,F., Braren,R., Kuhl,M., Hoovers,J.,
            Balasubramanian,S., Bazan,F. and Thiele,H.G.
  TITLE     Two novel human members of an emerging mammalian gene family
            related to mono-ADP-ribosylating bacterial toxins
  JOURNAL   Genomics 39 (3), 370-376 (1997)
   PUBMED   9119374
  REMARK    Erratum:[Genomics 1999 Jan 1;55(1):130]
REFERENCE   9  (residues 1 to 314)
  AUTHORS   Eiberg,H. and Mohr,J.
  TITLE     Dombrock blood group (DO): assignment to chromosome 12p
  JOURNAL   Hum Genet 98 (5), 518-521 (1996)
   PUBMED   8882867
REFERENCE   10 (residues 1 to 314)
  AUTHORS   Tippett,P.
  TITLE     Genetics of the Dombrock blood group system
  JOURNAL   J Med Genet 4 (1), 7-11 (1967)
   PUBMED   6034522
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007655.1, CR746266.1,
            AF290204.1 and BX096478.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 25, 2005 this sequence version replaced NP_066549.1.
            
            Summary: This gene encodes a protein that contains a
            mono-ADP-ribosylation (ART) motif. It is a member of the
            ADP-ribosyltransferase gene family but enzymatic activity has not
            been demonstrated experimentally. Antigens of the Dombrock blood
            group system are located on the gene product, which is
            glycosylphosphatidylinosotol-anchored to the erythrocyte membrane.
            Allelic variants, some of which lead to adverse transfusion
            reactions, are known. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291662.1, AY829434.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000228936.6/ ENSP00000228936.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.3"
     Protein         1..314
                     /product="ecto-ADP-ribosyltransferase 4 isoform 1
                     precursor"
                     /EC_number="2.4.2.31"
                     /note="ADP-ribosyltransferase 4 (DO blood group);
                     ecto-ADP-ribosyltransferase 4; mono-ADP-ribosyltransferase
                     4; Dombrock blood group carrier molecule;
                     NAD(P)(+)--arginine ADP-ribosyltransferase 4;
                     ADP-ribosyltransferase C2 and C3 toxin-like 4; Dombrock
                     glycoprotein; NAD(+)--protein-arginine
                     ADP-ribosyltransferase 4; Do glycoprotein;
                     ADP-ribosyltransferase 4 (Dombrock blood group)"
                     /calculated_mol_wt=30857
     sig_peptide     1..46
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q93070.3)"
                     /calculated_mol_wt=5040
     mat_peptide     47..285
                     /product="Ecto-ADP-ribosyltransferase 4.
                     /id=PRO_0000019329"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93070.3)"
                     /calculated_mol_wt=27766
     Region          56..277
                     /region_name="VIP2"
                     /note="A family of actin-ADP-ribosylating toxin. A member
                     of the Bacillus-prodiced vegetative insecticidal proteins
                     (VIPs) possesses high specificity against the major insect
                     pest, corn rootworms, and belongs to a classs of binary
                     toxins and regulators of...; cl00173"
                     /db_xref="CDD:469640"
     Site            114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q93070.3)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q93070.3)"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q93070.3)"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q93070.3)"
     Site            274
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q93070.3)"
     CDS             1..314
                     /gene="ART4"
                     /gene_synonym="ARTC4; CD297; DO; DO/ART4; DOK1"
                     /coded_by="NM_021071.4:414..1358"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8668.1"
                     /db_xref="GeneID:420"
                     /db_xref="HGNC:HGNC:726"
                     /db_xref="MIM:110600"
ORIGIN      
        1 mgplinrckk illpttvppa tmriwllggl lpfllllsgl qrptegseva ikidfdfapg
       61 sfddqyqgcs kqvmekltqg dyftkdieaq knyfrmwqka hlawlnqgkv lpqnmtttha
      121 vailfytlns nvhsdftram asvartpqqy ersfhfkylh yyltsaiqll rkdsimengt
      181 lcyevhyrtk dvhfnaytga tirfgqflst sllkeeaqef gnqtlftift clgapvqyfs
      241 lkkevlippy elfkvinmsy hprgdwlqlr stgnlstync qllkasskkc ipdpiaiasl
      301 sfltsviifs ksrv
//
LOCUS       NP_001351999             332 aa            linear   ROD 27-APR-2025
DEFINITION  alpha-centractin isoform 2 [Mus musculus].
ACCESSION   NP_001351999
VERSION     NP_001351999.1
DBSOURCE    REFSEQ: accession NM_001365070.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lee,M., Liu,Y.C., Chen,C., Lu,C.H., Lu,S.T., Huang,T.N., Hsu,M.T.,
            Hsueh,Y.P. and Cheng,P.L.
  TITLE     Ecm29-mediated proteasomal distribution modulates excitatory GABA
            responses in the developing brain
  JOURNAL   J Cell Biol 219 (2) (2020)
   PUBMED   31910261
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Clarkson,Y.L., Gillespie,T., Perkins,E.M., Lyndon,A.R. and
            Jackson,M.
  TITLE     Beta-III spectrin mutation L253P associated with spinocerebellar
            ataxia type 5 interferes with binding to Arp1 and protein
            trafficking from the Golgi
  JOURNAL   Hum Mol Genet 19 (18), 3634-3641 (2010)
   PUBMED   20603325
  REMARK    GeneRIF: Beta-III spectrin mutation L253P interferes with binding
            to Arp1 and protein trafficking from the Golgi.
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Lin,S.S., Bassik,M.C., Suh,H., Nishino,M., Arroyo,J.D., Hahn,W.C.,
            Korsmeyer,S.J. and Roberts,T.M.
  TITLE     PP2A regulates BCL-2 phosphorylation and proteasome-mediated
            degradation at the endoplasmic reticulum
  JOURNAL   J Biol Chem 281 (32), 23003-23012 (2006)
   PUBMED   16717086
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Eckley,D.M. and Schroer,T.A.
  TITLE     Interactions between the evolutionarily conserved, actin-related
            protein, Arp11, actin, and Arp1
  JOURNAL   Mol Biol Cell 14 (7), 2645-2654 (2003)
   PUBMED   12857853
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Carninci,P., Waki,K., Shiraki,T., Konno,H., Shibata,K., Itoh,M.,
            Aizawa,K., Arakawa,T., Ishii,Y., Sasaki,D., Bono,H., Kondo,S.,
            Sugahara,Y., Saito,R., Osato,N., Fukuda,S., Sato,K., Watahiki,A.,
            Hirozane-Kishikawa,T., Nakamura,M., Shibata,Y., Yasunishi,A.,
            Kikuchi,N., Yoshiki,A., Kusakabe,M., Gustincich,S., Beisel,K.,
            Pavan,W., Aidinis,V., Nakagawara,A., Held,W.A., Iwata,H., Kono,T.,
            Nakauchi,H., Lyons,P., Wells,C., Hume,D.A., Fagiolini,M.,
            Hensch,T.K., Brinkmeier,M., Camper,S., Hirota,J., Mombaerts,P.,
            Muramatsu,M., Okazaki,Y., Kawai,J. and Hayashizaki,Y.
  TITLE     Targeting a complex transcriptome: the construction of the mouse
            full-length cDNA encyclopedia
  JOURNAL   Genome Res 13 (6B), 1273-1289 (2003)
   PUBMED   12819125
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Kusano,K., Abe,H. and Obinata,T.
  TITLE     Primary structure of mouse actin-related protein 1 (Arp1) and its
            tissue expression
  JOURNAL   Zoolog Sci 14 (1), 77-82 (1997)
   PUBMED   9200982
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY794369.1, AK019518.1 and CD776146.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK019518.1, SRR7345562.4864080.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 38.84 cM"
     Protein         1..332
                     /product="alpha-centractin isoform 2"
                     /note="actin-related protein 1 alpha; alpha-centractin;
                     centrosome-associated actin homolog; ARP1 actin-related
                     protein 1 homolog A, centractin alpha"
                     /calculated_mol_wt=37538
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P61163; propagated from
                     UniProtKB/Swiss-Prot (P61164.1)"
     Region          9..308
                     /region_name="ASKHA_NBD_Arp1"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein 1 (Arp1) and similar proteins; cd10216"
                     /db_xref="CDD:466820"
     CDS             1..332
                     /gene="Actr1a"
                     /gene_synonym="actin-RPV; alpha-Arp1; Arp1"
                     /coded_by="NM_001365070.1:65..1063"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS89411.1"
                     /db_xref="GeneID:54130"
                     /db_xref="MGI:MGI:1858964"
ORIGIN      
        1 mesydvianq pvvidngsgv ikagfagdqi pkycfpnyvg rpkhvrvmag alegdifigp
       61 kaeehrglls irypmehgiv kdwndmeriw qyvyskdqlq tfseehpvll teaplnprkn
      121 reraaevffe tfnvpalfis mqavlslyat grttgvvlds gdgvthavpi yegfamphsi
      181 mridiagrdv srflrlylrk egydfhssse feivkaiker acylsinpqk detletekaq
      241 yylpdgstie igpsrfrape llfrpdlige esegihevlv faiqksdmdl rrtlfsnivl
      301 sggstlfkdi ctpgetvfhm dwrfypcfpg hl
//
LOCUS       NP_776600                514 aa            linear   MAM 27-APR-2025
DEFINITION  serine--tRNA ligase, cytoplasmic [Bos taurus].
ACCESSION   NP_776600
VERSION     NP_776600.1
DBSOURCE    REFSEQ: accession NM_174175.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Dai,W., Zhao,F., Liu,J. and Liu,H.
  TITLE     ASCT2 Is Involved in SARS-Mediated beta-Casein Synthesis of Bovine
            Mammary Epithelial Cells with Methionine Supply
  JOURNAL   J Agric Food Chem 68 (46), 13038-13045 (2020)
   PUBMED   31597423
  REMARK    GeneRIF: ASCT2 Is Involved in SARS-Mediated beta-Casein Synthesis
            of Bovine Mammary Epithelial Cells with Methionine Supply.
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Chimnaronk,S., Jeppesen,M.G., Shimada,N., Suzuki,T., Nyborg,J. and
            Watanabe,K.
  TITLE     Crystallization and preliminary X-ray diffraction study of
            mammalian mitochondrial seryl-tRNA synthetase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 7), 1319-1322 (2004)
   PUBMED   15213404
  REMARK    GeneRIF: crystal structure
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000003.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6764281.21803.1,
                                           SRR5571254.12406.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA6648754,
                                           SAMEA6648756 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="3"
                     /map="3"
                     /breed="Hereford"
     Protein         1..514
                     /product="serine--tRNA ligase, cytoplasmic"
                     /EC_number="6.1.1.11"
                     /note="seryl-tRNA synthetase, cytoplasmic; serRS;
                     seryl-tRNA(Ser/Sec) synthetase"
                     /calculated_mol_wt=58474
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P49591; propagated from
                     UniProtKB/Swiss-Prot (Q9GMB8.3)"
     Region          3..486
                     /region_name="PLN02678"
                     /note="seryl-tRNA synthetase"
                     /db_xref="CDD:215364"
     Region          9..61
                     /region_name="Interaction with tRNA.
                     /evidence=ECO:0000250|UniProtKB:P49591"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GMB8.3)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49591; propagated from
                     UniProtKB/Swiss-Prot (Q9GMB8.3)"
     Site            323
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49591; propagated from
                     UniProtKB/Swiss-Prot (Q9GMB8.3)"
     Site            429
                     /site_type="other"
                     /note="Important for serine binding.
                     /evidence=ECO:0000250|UniProtKB:P49591; propagated from
                     UniProtKB/Swiss-Prot (Q9GMB8.3)"
     Region          475..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GMB8.3)"
     Region          482..494
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:P49591"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GMB8.3)"
     CDS             1..514
                     /gene="SARS1"
                     /gene_synonym="SARS"
                     /coded_by="NM_174175.3:87..1631"
                     /db_xref="BGD:BT12720"
                     /db_xref="GeneID:281476"
                     /db_xref="VGNC:VGNC:34291"
ORIGIN      
        1 mvldldlfrv dkggdpalir esqekrfkdp glvdqlvkad sewrrcrfra dnlnklknlc
       61 sktigekmkk kepvgndesi pedvlnlddl tadtltnlkv sqikkvrllv deailkcdae
      121 rikleaerfe slreignllh psvpisdded adnkveriwg dctvrkkysh vdlvvmvdgf
      181 egekgavvag srgyflkgvl vfleqaliqf alrtlasrgy tpiytpffmr kevmqevaql
      241 sqfdeelykv igkgseksdd nsyeekylia tseqpiaalh rdewlrpedl pikyaglstc
      301 frqevgshgr dtrgifrvhq fekieqfvys sphdnkswem feemiataee fyqslgipyh
      361 ivnivsgsln haaskkldle awfpgsgafr elvscsnctd yqarrlriry gqtkkmmdkv
      421 efvhmlnatm cattrticai lenyqtekgi lvpeklkefm ppglqelipf vkaapidqep
      481 skkqkkqheg skkkgaardv alesqlqnme vtda
//
LOCUS       NP_057521                451 aa            linear   PRI 27-APR-2025
DEFINITION  tubulin gamma-2 chain isoform 2 [Homo sapiens].
ACCESSION   NP_057521
VERSION     NP_057521.1
DBSOURCE    REFSEQ: accession NM_016437.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Draberova,E., Sulimenko,V., Vinopal,S., Sulimenko,T., Sladkova,V.,
            D'Agostino,L., Sobol,M., Hozak,P., Kren,L., Katsetos,C.D. and
            Draber,P.
  TITLE     Differential expression of human gamma-tubulin isotypes during
            neuronal development and oxidative stress points to a
            gamma-tubulin-2 prosurvival function
  JOURNAL   FASEB J 31 (5), 1828-1846 (2017)
   PUBMED   28119396
  REMARK    GeneRIF: that in the face of predominant gamma-tubulin-1
            expression, the accumulation of gamma-tubulin-2 in mature neurons
            and neuroblastoma cells during oxidative stress may denote a
            prosurvival role of gamma-tubulin-2 in neurons
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Ohashi,T., Yamamoto,T., Yamanashi,Y. and Ohsugi,M.
  TITLE     Human TUBG2 gene is expressed as two splice variant mRNA and
            involved in cell growth
  JOURNAL   FEBS Lett 590 (8), 1053-1063 (2016)
   PUBMED   27015882
  REMARK    GeneRIF: expression of gamma-tubulin2 along with gamma-tubulin1 and
            a novel TUBG2 splice variant are identified.
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Maounis,N.F., Draberova,E., Mahera,E., Chorti,M., Caracciolo,V.,
            Sulimenko,T., Riga,D., Trakas,N., Emmanouilidou,A., Giordano,A.,
            Draber,P. and Katsetos,C.D.
  TITLE     Overexpression of gamma-tubulin in non-small cell lung cancer
  JOURNAL   Histol Histopathol 27 (9), 1183-1194 (2012)
   PUBMED   22806905
  REMARK    GeneRIF: Our results reveal for the first time an increased
            expression of TUBG1 and TUBG2 in lung cancer
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Vinopal,S., Cernohorska,M., Sulimenko,V., Sulimenko,T., Vosecka,V.,
            Flemr,M., Draberova,E. and Draber,P.
  TITLE     gamma-Tubulin 2 nucleates microtubules and is downregulated in
            mouse early embryogenesis
  JOURNAL   PLoS One 7 (1), e29919 (2012)
   PUBMED   22235350
  REMARK    GeneRIF: gamma-tubulin 2 is able to nucleate microtubules and
            substitute for gamma-tubulin 1
            Erratum:[PLoS One. 2012;7(6):
            doi/10.1371/annotation/5dd084b1-20e6-4e1f-88e0-dfe05289da08]
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Bharti,P., Schliebs,W., Schievelbusch,T., Neuhaus,A., David,C.,
            Kock,K., Herrmann,C., Meyer,H.E., Wiese,S., Warscheid,B., Theiss,C.
            and Erdmann,R.
  TITLE     PEX14 is required for microtubule-based peroxisome motility in
            human cells
  JOURNAL   J Cell Sci 124 (Pt 10), 1759-1768 (2011)
   PUBMED   21525035
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Niwa,J., Ishigaki,S., Doyu,M., Suzuki,T., Tanaka,K. and Sobue,G.
  TITLE     A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin
            ligase activity
  JOURNAL   Biochem Biophys Res Commun 281 (3), 706-713 (2001)
   PUBMED   11237715
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Herreros,L., Rodriguez-Fernandez,J.L., Brown,M.C.,
            Alonso-Lebrero,J.L., Cabanas,C., Sanchez-Madrid,F., Longo,N.,
            Turner,C.E. and Sanchez-Mateos,P.
  TITLE     Paxillin localizes to the lymphocyte microtubule organizing center
            and associates with the microtubule cytoskeleton
  JOURNAL   J Biol Chem 275 (34), 26436-26440 (2000)
   PUBMED   10840040
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Wise,D.O., Krahe,R. and Oakley,B.R.
  TITLE     The gamma-tubulin gene family in humans
  JOURNAL   Genomics 67 (2), 164-170 (2000)
   PUBMED   10903841
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Tassin,A.M., Celati,C., Moudjou,M. and Bornens,M.
  TITLE     Characterization of the human homologue of the yeast spc98p and its
            association with gamma-tubulin
  JOURNAL   J Cell Biol 141 (3), 689-701 (1998)
   PUBMED   9566969
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Hsu,H.L. and Yeh,N.H.
  TITLE     Dynamic changes of NuMA during the cell cycle and possible
            appearance of a truncated form of NuMA during apoptosis
  JOURNAL   J Cell Sci 109 (Pt 2), 277-288 (1996)
   PUBMED   8838651
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC353745.1 and BC108739.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. It encodes
            isoform 2 which has a shorter N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.367929.1,
                                           SRR3476690.1097203.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000251412.8/ ENSP00000251412.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..451
                     /product="tubulin gamma-2 chain isoform 2"
                     /note="gamma-2-tubulin; tubulin gamma 2 chain"
                     /calculated_mol_wt=50961
     Region          3..435
                     /region_name="gamma_tubulin"
                     /note="The gamma-tubulin family; cd02188"
                     /db_xref="CDD:276957"
     Site            order(3,47,133,252,254,258,261..262,264..265,330..331,
                     333..334,337..338,341,353..354,357..358,430,433..434)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:276957"
     Site            order(11..13,16,102,140,142..146,171,173,207,225,228..229)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:276957"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by BRSK1.
                     /evidence=ECO:0000250|UniProtKB:Q8VCK3; propagated from
                     UniProtKB/Swiss-Prot (Q9NRH3.1)"
     CDS             1..451
                     /gene="TUBG2"
                     /coded_by="NM_016437.3:221..1576"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS32658.1"
                     /db_xref="GeneID:27175"
                     /db_xref="HGNC:HGNC:12419"
                     /db_xref="MIM:605785"
ORIGIN      
        1 mpreiitlql gqcgnqigfe fwkqlcaehg ispegiveef ategtdrkdv ffyqaddehy
       61 ipravlldle prvihsilns pyaklynpen iylsehggga gnnwasgfsq gekihedifd
      121 iidreadgsd slegfvlchs iaggtgsglg syllerlndr ypkklvqtys vfpyqdemsd
      181 vvvqpynsll tlkrltqnad cvvvldntal nriatdrlhi qnpsfsqinq lvstimsast
      241 ttlrypgymn ndligliasl iptprlhflm tgytplttdq svasvrkttv ldvmrrllqp
      301 knvmvstgrd rqtnhcyiai lniiqgevdp tqvhkslqri rerklanfip wgpasiqval
      361 srkspylpsa hrvsglmman htsisslfes scqqfdklrk rdafleqfrk edmfkdnfde
      421 mdrsrevvqe lideyhaatq pdyiswgtqe q
//
LOCUS       NP_001355928             292 aa            linear   PRI 27-APR-2025
DEFINITION  aprataxin isoform g [Homo sapiens].
ACCESSION   NP_001355928 XP_024303347
VERSION     NP_001355928.1
DBSOURCE    REFSEQ: accession NM_001368999.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_024303347.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.407504.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..292
                     /product="aprataxin isoform g"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=33163
     Region          3..102
                     /region_name="FHA_APTX"
                     /note="forkhead associated (FHA) domain found in aprataxin
                     and similar proteins; cd22735"
                     /db_xref="CDD:438787"
     Site            order(29..31,34..36,38..42,63..65,91)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438787"
     Region          164..265
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(258,260,262..264)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            260
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     CDS             1..292
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001368999.1:322..1200"
                     /note="isoform g is encoded by transcript variant 20"
                     /db_xref="CCDS:CCDS6532.2"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqvqlkae cnkgyvkvkq
       61 vgvnptsids vvigkdqevk lqpgqvlhmv nelypyivef eeeaknpgle thrkrkrsgn
      121 sdsierdaaq eaeagtglep gsnsgqcsvp lkkgkdapik keslghwsqg lkismqdpkm
      181 qvykdeqvvv ikdkypkary hwlvlpwtsi sslkavareh lellkhmhtv gekvivdfag
      241 ssklrfrlgy haipsmshvh lhvisqdfds pclknkkhwn sfnteyfles qe
//
LOCUS       NP_062558                463 aa            linear   PRI 27-APR-2025
DEFINITION  interferon-inducible GTPase 5 [Homo sapiens].
ACCESSION   NP_062558
VERSION     NP_062558.1
DBSOURCE    REFSEQ: accession NM_019612.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Li,J., Xu,X., Liu,J., Zhang,S., Wang,T., Liu,Y. and Wang,Z.
  TITLE     The immunity-related GTPase IRGC mediates interaction between lipid
            droplets and mitochondria to facilitate sperm motility
  JOURNAL   FEBS Lett 597 (12), 1595-1605 (2023)
   PUBMED   37195149
  REMARK    GeneRIF: The immunity-related GTPase IRGC mediates interaction
            between lipid droplets and mitochondria to facilitate sperm
            motility.
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Bekpen,C., Xavier,R.J. and Eichler,E.E.
  TITLE     Human IRGM gene 'to be or not to be'
  JOURNAL   Semin Immunopathol 32 (4), 437-444 (2010)
   PUBMED   20737271
  REMARK    Review article
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC033853.1 and BC066939.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC066939.1, SRR5189667.230285.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000244314.6/ ENSP00000244314.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..463
                     /product="interferon-inducible GTPase 5"
                     /note="immunity-related GTPase family, cinema 1;
                     immunity-related GTPase cinema 1;
                     interferon-gamma-inducible GTPase IFGGE protein"
                     /calculated_mol_wt=50157
     Region          <12..>76
                     /region_name="RsgA_GTPase"
                     /note="RsgA GTPase; pfam03193"
                     /db_xref="CDD:427191"
     Region          54..250
                     /region_name="p47_IIGP_like"
                     /note="p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47,
                     GTPI, LRG-47, and IIGP1; cd04104"
                     /db_xref="CDD:206690"
     Site            61..68
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206690"
     Site            order(64..69,87..88,169,171..172,216..218)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206690"
     Site            89..99
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206690"
     Site            93
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206690"
     Site            111..114
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206690"
     Site            order(113..131,133..136)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206690"
     Site            order(153..154,157..158,160,163)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206690"
     Site            168..171
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206690"
     Site            216..218
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206690"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AYF9; propagated from
                     UniProtKB/Swiss-Prot (Q6NXR0.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AYF9; propagated from
                     UniProtKB/Swiss-Prot (Q6NXR0.1)"
     Region          404..437
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXR0.1)"
     CDS             1..463
                     /gene="IRGC"
                     /gene_synonym="CINEMA; IFGGE; Iigp5; IRGC1; R30953_1"
                     /coded_by="NM_019612.4:134..1525"
                     /db_xref="CCDS:CCDS12629.1"
                     /db_xref="GeneID:56269"
                     /db_xref="HGNC:HGNC:28835"
                     /db_xref="MIM:620634"
ORIGIN      
        1 matsklpvvp geeentilma kerlealrta fesgdlpqaa shlqellast esirlevgvt
       61 gesgagkssl inalrgleae dpgaaltgvm ettmqpspyp hpqfpdvtlw dlpgagspgc
      121 padkylkqvd fsrydffllv sprrcgavet rlaaeilcqg kkfyfvrtkv dedlaatrtq
      181 rpsgfreaav lqeirdhcae rlreagvadp riflvsnlsp arydfptlvs twehdlpshr
      241 rhagllslpd islealqkkk amlqeqvlkt alvlgviqal pvpglaaayd dallihslrg
      301 yhrsfglddd slaklaeqvg kqagdlrsvi rsplanevsp etvlrlysqs sdgamrvara
      361 fergipvfgt lvaggisfga vytmlqgcln emaedaqrvr ikaleddepq pevslevasd
      421 ngvekggsge gggeeaplst crklglllky ildswkkhds eek
//
LOCUS       NP_942146                269 aa            linear   PRI 27-APR-2025
DEFINITION  seven in absentia homolog 3 [Homo sapiens].
ACCESSION   NP_942146 XP_210264
VERSION     NP_942146.2
DBSOURCE    REFSEQ: accession NM_198849.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Li,X., Chu,S.G., Shen,X.N., Hou,X.H., Xu,W., Ou,Y.N., Dong,Q.,
            Tan,L. and Yu,J.T.
  TITLE     Genome-wide association study identifies SIAH3 locus influencing
            the rate of ventricular enlargement in non-demented elders
  JOURNAL   Aging (Albany NY) 11 (21), 9862-9874 (2019)
   PUBMED   31711042
  REMARK    GeneRIF: Genome-wide association study identifies SIAH3 locus
            influencing the rate of ventricular enlargement in non-demented
            elders.
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Pepper,I.J., Van Sciver,R.E. and Tang,A.H.
  TITLE     Phylogenetic analysis of the SINA/SIAH ubiquitin E3 ligase family
            in Metazoa
  JOURNAL   BMC Evol Biol 17 (1), 182 (2017)
   PUBMED   28784114
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Wang,Y. and Tatakis,D.N.
  TITLE     Human gingiva transcriptome during wound healing
  JOURNAL   J Clin Periodontol 44 (4), 394-402 (2017)
   PUBMED   28005267
  REMARK    GeneRIF: SIAH3 expression is significantly downregulated in human
            masticatory mucosa during wound healing
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL157819.15, BC041372.2 and DA804734.1.
            
            On Jul 20, 2006 this sequence version replaced NP_942146.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC041372.2, DR000833.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000400405.4/ ENSP00000383256.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.13"
     Protein         1..269
                     /product="seven in absentia homolog 3"
                     /note="siah-3"
                     /calculated_mol_wt=30529
     Region          133..259
                     /region_name="Sina"
                     /note="Seven in absentia (Sina) protein family, C-terminal
                     substrate binding domain; composed of the Drosophila Sina
                     protein, the mammalian Sina homolog (Siah), the plant
                     protein SINAT5, and similar proteins. Sina, Siah and
                     SINAT5 are RING-containing proteins...; cd03829"
                     /db_xref="CDD:239753"
     Site            order(140..142,144,146,155..156)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239753"
     Site            order(197,209..215,217,232..233,240,244)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239753"
     CDS             1..269
                     /gene="SIAH3"
                     /coded_by="NM_198849.3:125..934"
                     /db_xref="CCDS:CCDS41883.1"
                     /db_xref="GeneID:283514"
                     /db_xref="HGNC:HGNC:30553"
                     /db_xref="MIM:615609"
ORIGIN      
        1 mlfftqcfga vldlihlrfq hykakrvfsa agqlvcvvnp thnlkyvssr ravtqsapeq
       61 gsfhphhlsh hhchhrhhhh lrhhahphhl hhqeaglhan pvtpclcmcp lfscqwegrl
      121 evvvphlrqi hrvdilqgae ivflatdmhl papadwiimh sclghhfllv lrkqerhegh
      181 pqffatmmli gtptqadcft yrlelnrnhr rlkweatprs vlecvdsvit dgdclvlnts
      241 laqlfsdngs laigiaitat evlpseaem
//
LOCUS       NP_001349908             137 aa            linear   PRI 27-APR-2025
DEFINITION  golgin subfamily A member 7 isoform a [Homo sapiens].
ACCESSION   NP_001349908 XP_024302942
VERSION     NP_001349908.1
DBSOURCE    REFSEQ: accession NM_001362979.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Zeng,X.T., Yu,X.X. and Cheng,W.
  TITLE     Correction to: The interactions of ZDHHC5/GOLGA7 with SARS-CoV-2
            spike (S) protein and their effects on S protein's subcellular
            localization, palmitoylation and pseudovirus entry
  JOURNAL   Virol J 19 (1), 25 (2022)
   PUBMED   35115020
  REMARK    Correction to:[Virol J. 2021 Dec 27;18(1):257. doi:
            10.1186/s12985-021-01722-w. PMID: 34961524]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Zeng,X.T., Yu,X.X. and Cheng,W.
  TITLE     The interactions of ZDHHC5/GOLGA7 with SARS-CoV-2 spike (S) protein
            and their effects on S protein's subcellular localization,
            palmitoylation and pseudovirus entry
  JOURNAL   Virol J 18 (1), 257 (2021)
   PUBMED   34961524
  REMARK    GeneRIF: The interactions of ZDHHC5/GOLGA7 with SARS-CoV-2 spike
            (S) protein and their effects on S protein's subcellular
            localization, palmitoylation and pseudovirus entry.
            Erratum:[Virol J. 2022 Feb 3;19(1):25. doi:
            10.1186/s12985-022-01750-0. PMID: 35115020]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Wu,Z., Zhang,Z., Wang,X., Zhang,J., Ren,C., Li,Y., Gao,L.,
            Liang,X., Wang,P. and Ma,C.
  TITLE     Palmitoylation of SARS-CoV-2 S protein is essential for viral
            infectivity
  JOURNAL   Signal Transduct Target Ther 6 (1), 231 (2021)
   PUBMED   34117209
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Stukalov,A., Girault,V., Grass,V., Karayel,O., Bergant,V.,
            Urban,C., Haas,D.A., Huang,Y., Oubraham,L., Wang,A., Hamad,M.S.,
            Piras,A., Hansen,F.M., Tanzer,M.C., Paron,I., Zinzula,L.,
            Engleitner,T., Reinecke,M., Lavacca,T.M., Ehmann,R., Wolfel,R.,
            Jores,J., Kuster,B., Protzer,U., Rad,R., Ziebuhr,J., Thiel,V.,
            Scaturro,P., Mann,M. and Pichlmair,A.
  TITLE     Multilevel proteomics reveals host perturbations by SARS-CoV-2 and
            SARS-CoV
  JOURNAL   Nature 594 (7862), 246-252 (2021)
   PUBMED   33845483
REFERENCE   5  (residues 1 to 137)
  AUTHORS   Gordon,D.E., Hiatt,J., Bouhaddou,M., Rezelj,V.V., Ulferts,S.,
            Braberg,H., Jureka,A.S., Obernier,K., Guo,J.Z., Batra,J.,
            Kaake,R.M., Weckstein,A.R., Owens,T.W., Gupta,M., Pourmal,S.,
            Titus,E.W., Cakir,M., Soucheray,M., McGregor,M., Cakir,Z., Jang,G.,
            O'Meara,M.J., Tummino,T.A., Zhang,Z., Foussard,H., Rojc,A.,
            Zhou,Y., Kuchenov,D., Huttenhain,R., Xu,J., Eckhardt,M.,
            Swaney,D.L., Fabius,J.M., Ummadi,M., Tutuncuoglu,B., Rathore,U.,
            Modak,M., Haas,P., Haas,K.M., Naing,Z.Z.C., Pulido,E.H., Shi,Y.,
            Barrio-Hernandez,I., Memon,D., Petsalaki,E., Dunham,A.,
            Marrero,M.C., Burke,D., Koh,C., Vallet,T., Silvas,J.A.,
            Azumaya,C.M., Billesbolle,C., Brilot,A.F., Campbell,M.G.,
            Diallo,A., Dickinson,M.S., Diwanji,D., Herrera,N., Hoppe,N.,
            Kratochvil,H.T., Liu,Y., Merz,G.E., Moritz,M., Nguyen,H.C.,
            Nowotny,C., Puchades,C., Rizo,A.N., Schulze-Gahmen,U., Smith,A.M.,
            Sun,M., Young,I.D., Zhao,J., Asarnow,D., Biel,J., Bowen,A.,
            Braxton,J.R., Chen,J., Chio,C.M., Chio,U.S., Deshpande,I., Doan,L.,
            Faust,B., Flores,S., Jin,M., Kim,K., Lam,V.L., Li,F., Li,J.,
            Li,Y.L., Li,Y., Liu,X., Lo,M., Lopez,K.E., Melo,A.A., Moss,F.R.
            3rd, Nguyen,P., Paulino,J., Pawar,K.I., Peters,J.K., Pospiech,T.H.
            Jr., Safari,M., Sangwan,S., Schaefer,K., Thomas,P.V., Thwin,A.C.,
            Trenker,R., Tse,E., Tsui,T.K.M., Wang,F., Whitis,N., Yu,Z.,
            Zhang,K., Zhang,Y., Zhou,F., Saltzberg,D., Hodder,A.J.,
            Shun-Shion,A.S., Williams,D.M., White,K.M., Rosales,R., Kehrer,T.,
            Miorin,L., Moreno,E., Patel,A.H., Rihn,S., Khalid,M.M.,
            Vallejo-Gracia,A., Fozouni,P., Simoneau,C.R., Roth,T.L., Wu,D.,
            Karim,M.A., Ghoussaini,M., Dunham,I., Berardi,F., Weigang,S.,
            Chazal,M., Park,J., Logue,J., McGrath,M., Weston,S., Haupt,R.,
            Hastie,C.J., Elliott,M., Brown,F., Burness,K.A., Reid,E.,
            Dorward,M., Johnson,C., Wilkinson,S.G., Geyer,A., Giesel,D.M.,
            Baillie,C., Raggett,S., Leech,H., Toth,R., Goodman,N., Keough,K.C.,
            Lind,A.L., Klesh,R.J., Hemphill,K.R., Carlson-Stevermer,J., Oki,J.,
            Holden,K., Maures,T., Pollard,K.S., Sali,A., Agard,D.A., Cheng,Y.,
            Fraser,J.S., Frost,A., Jura,N., Kortemme,T., Manglik,A.,
            Southworth,D.R., Stroud,R.M., Alessi,D.R., Davies,P., Frieman,M.B.,
            Ideker,T., Abate,C., Jouvenet,N., Kochs,G., Shoichet,B., Ott,M.,
            Palmarini,M., Shokat,K.M., Garcia-Sastre,A., Rassen,J.A.,
            Grosse,R., Rosenberg,O.S., Verba,K.A., Basler,C.F., Vignuzzi,M.,
            Peden,A.A., Beltrao,P. and Krogan,N.J.
  CONSRTM   QCRG Structural Biology Consortium; Zoonomia Consortium
  TITLE     Comparative host-coronavirus protein interaction networks reveal
            pan-viral disease mechanisms
  JOURNAL   Science 370 (6521) (2020)
   PUBMED   33060197
REFERENCE   6  (residues 1 to 137)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 137)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 137)
  AUTHORS   Swarthout,J.T., Lobo,S., Farh,L., Croke,M.R., Greentree,W.K.,
            Deschenes,R.J. and Linder,M.E.
  TITLE     DHHC9 and GCP16 constitute a human protein fatty acyltransferase
            with specificity for H- and N-Ras
  JOURNAL   J Biol Chem 280 (35), 31141-31148 (2005)
   PUBMED   16000296
  REMARK    GeneRIF: Data show that H- and N-Ras are palmitoylated by a human
            protein palmitoyltransferase encoded by the ZDHHC9 and GCP16 genes.
REFERENCE   9  (residues 1 to 137)
  AUTHORS   Ohta,E., Misumi,Y., Sohda,M., Fujiwara,T., Yano,A. and Ikehara,Y.
  TITLE     Identification and characterization of GCP16, a novel acylated
            Golgi protein that interacts with GCP170
  JOURNAL   J Biol Chem 278 (51), 51957-51967 (2003)
   PUBMED   14522980
  REMARK    GeneRIF: results indicate that GCP16 is the acylated membrane
            protein, associated with GCP170, and possibly involved in vesicular
            transport from the Golgi to the cell surface
REFERENCE   10 (residues 1 to 137)
  AUTHORS   Jia,L., Young,M.F., Powell,J., Yang,L., Ho,N.C., Hotchkiss,R.,
            Robey,P.G. and Francomano,C.A.
  TITLE     Gene expression profile of human bone marrow stromal cells:
            high-throughput expressed sequence tag sequencing analysis
  JOURNAL   Genomics 79 (1), 7-17 (2002)
   PUBMED   11827452
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI546026.1, BC001227.2, AF068291.1, AV650886.1, AF125102.1 and
            BG939345.1.
            
            On May 4, 2018 this sequence version replaced XP_024302942.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.22583.1,
                                           SRR1660807.220545.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..137
                     /product="golgin subfamily A member 7 isoform a"
                     /note="Golgi complex-associated protein of 16kDa; golgi
                     autoantigen, golgin subfamily a, 7; golgin subfamily A
                     member 7; golgi complex-associated protein of 16 kDa"
                     /calculated_mol_wt=15693
     Region          11..124
                     /region_name="Erf4"
                     /note="Golgin subfamily A member 7/ERF4 family; pfam10256"
                     /db_xref="CDD:463029"
     CDS             1..137
                     /gene="GOLGA7"
                     /gene_synonym="GCP16; GOLGA3AP1; GOLGA7A; HSPC041"
                     /coded_by="NM_001362979.1:194..607"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS34887.1"
                     /db_xref="GeneID:51125"
                     /db_xref="HGNC:HGNC:24876"
                     /db_xref="MIM:609453"
ORIGIN      
        1 mrpqqapvsg kvfiqrdyss gtrcqfqtkf paelenridr qqfeetvrtl nnlyaeaekl
       61 ggqsylegcl acltaytifl cmethyekvl kkvskyiqeq nekiyapqgl lltdpiergl
      121 rvieitiyed rgmssgr
//
LOCUS       NP_056469                207 aa            linear   PRI 27-APR-2025
DEFINITION  alpha/beta-tubulin-N-acetyltransferase 9 isoform 1 [Homo sapiens].
ACCESSION   NP_056469
VERSION     NP_056469.2
DBSOURCE    REFSEQ: accession NM_015654.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deshpande,P., Chimata,A.V., Snider,E., Singh,A., Kango-Singh,M. and
            Singh,A.
  TITLE     N-Acetyltransferase 9 ameliorates Abeta42-mediated
            neurodegeneration in the Drosophila eye
  JOURNAL   Cell Death Dis 14 (7), 478 (2023)
   PUBMED   37507384
  REMARK    GeneRIF: N-Acetyltransferase 9 ameliorates Abeta42-mediated
            neurodegeneration in the Drosophila eye.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Mok,J.W. and Choi,K.W.
  TITLE     Novel function of N-acetyltransferase for microtubule stability and
            JNK signaling in Drosophila organ development
  JOURNAL   Proc Natl Acad Sci U S A 118 (4) (2021)
   PUBMED   33479178
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Jiugang,Z., Jing,L. and Yonggang,L.
  TITLE     Characterization, expression profile, polymorphism and association
            of porcine NAT9 gene
  JOURNAL   Mol Biol Rep 39 (3), 3137-3142 (2012)
   PUBMED   21688147
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Danik,J.S., Pare,G., Chasman,D.I., Zee,R.Y., Kwiatkowski,D.J.,
            Parker,A., Miletich,J.P. and Ridker,P.M.
  TITLE     Novel loci, including those related to Crohn disease, psoriasis,
            and inflammation, identified in a genome-wide association study of
            fibrinogen in 17 686 women: the Women's Genome Health Study
  JOURNAL   Circ Cardiovasc Genet 2 (2), 134-141 (2009)
   PUBMED   20031577
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   6  (residues 1 to 207)
  AUTHORS   Filer,C.E., Ho,P., Bruce,I.N., Worthington,J. and Barton,A.
  TITLE     Investigation of association of genes NAT9, SLC9A3R1 and RAPTOR on
            chromosome 17q25 with psoriatic arthritis
  JOURNAL   Ann Rheum Dis 68 (2), 292-293 (2009)
   PUBMED   19139211
  REMARK    GeneRIF: no evidence was found for association of SNPs mapping to
            the NAT9, SLC9A3R1 and RAPTOR loci with susceptibility to psoriatic
            arthritis
REFERENCE   7  (residues 1 to 207)
  AUTHORS   Helms,C., Cao,L., Krueger,J.G., Wijsman,E.M., Chamian,F.,
            Gordon,D., Heffernan,M., Daw,J.A., Robarge,J., Ott,J., Kwok,P.Y.,
            Menter,A. and Bowcock,A.M.
  TITLE     A putative RUNX1 binding site variant between SLC9A3R1 and NAT9 is
            associated with susceptibility to psoriasis
  JOURNAL   Nat Genet 35 (4), 349-356 (2003)
   PUBMED   14608357
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA259097.1, BC004195.2 and HY222854.1.
            
            On Jun 9, 2003 this sequence version replaced NP_056469.1.
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004195.2, SRR1660805.211804.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357814.8/ ENSP00000350467.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..207
                     /product="alpha/beta-tubulin-N-acetyltransferase 9 isoform
                     1"
                     /EC_number="2.3.1.308"
                     /note="embryo brain specific protein; N-acetyltransferase
                     9 (GCN5-related, putative);
                     alpha/beta-tubulin-N-acetyltransferase 9;
                     N-acetyltransferase 9 (putative)"
                     /calculated_mol_wt=23230
     Region          9..166
                     /region_name="RimL"
                     /note="Protein N-acetyltransferase, RimJ/RimL family
                     [Translation, ribosomal structure and biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG1670"
                     /db_xref="CDD:441276"
     CDS             1..207
                     /gene="NAT9"
                     /gene_synonym="EBSP; hNATL"
                     /coded_by="NM_015654.5:89..712"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11706.1"
                     /db_xref="GeneID:26151"
                     /db_xref="HGNC:HGNC:23133"
                     /db_xref="MIM:620913"
ORIGIN      
        1 mrlnqntlll gkkvvlvpyt sehvpsryhe wmkseelqrl tasepltleq eyamqcswqe
       61 dadkctfivl daekwqaqpg ateescmvgd vnlfltdled ltlgeievmi aepscrgkgl
      121 gteavlamls ygvttlgltk feakigqgne psirmfqklh feqvatssvf qevtlrltvs
      181 esehqwlleq tshveekpyr dgsaepc
//
LOCUS       NP_060342                298 aa            linear   PRI 27-APR-2025
DEFINITION  probable tRNA(His) guanylyltransferase isoform 1 [Homo sapiens].
ACCESSION   NP_060342
VERSION     NP_060342.2
DBSOURCE    REFSEQ: accession NM_017872.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Antika,T.R., Nazilah,K.R., Lee,Y.H., Lo,Y.T., Yeh,C.S., Yeh,F.L.,
            Chang,T.H., Wang,T.L. and Wang,C.C.
  TITLE     Human Thg1 displays tRNA-inducible GTPase activity
  JOURNAL   Nucleic Acids Res 50 (17), 10015-10025 (2022)
   PUBMED   36107775
  REMARK    GeneRIF: Human Thg1 displays tRNA-inducible GTPase activity.
            Erratum:[Nucleic Acids Res. 2022 Nov 11;50(20):11992. doi:
            10.1093/nar/gkac1057. PMID: 36305790]
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Nakamura,A., Wang,D. and Komatsu,Y.
  TITLE     Analysis of GTP addition in the reverse (3'-5') direction by human
            tRNAHis guanylyltransferase
  JOURNAL   RNA 27 (6), 665-675 (2021)
   PUBMED   33758037
  REMARK    GeneRIF: Analysis of GTP addition in the reverse (3'-5') direction
            by human tRNA(His) guanylyltransferase.
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Rabin,R., Hirsch,Y., Johansson,M.M., Ekstein,J., Ekstein,A. and
            Pappas,J.
  TITLE     Severe epileptic encephalopathy associated with compound
            heterozygosity of THG1L variants in the Ashkenazi Jewish population
  JOURNAL   Am J Med Genet A 185 (5), 1589-1597 (2021)
   PUBMED   33682303
  REMARK    GeneRIF: Severe epileptic encephalopathy associated with compound
            heterozygosity of THG1L variants in the Ashkenazi Jewish
            population.
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Perona,J.J. and Oza,J.P.
  TITLE     Crystal structure of a reverse polymerase
  JOURNAL   Proc Natl Acad Sci U S A 107 (47), 20149-20150 (2010)
   PUBMED   21078997
  REMARK    GeneRIF: The catalytic domain of Thg1 shares both a common
            architecture and a two-metal ion-dependent mechanism with canonical
            5'-3' DNA polymerases.
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Hyde,S.J., Eckenroth,B.E., Smith,B.A., Eberley,W.A., Heintz,N.H.,
            Jackman,J.E. and Doublie,S.
  TITLE     tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl
            transferase, shares unexpected structural homology with canonical
            5'-3' DNA polymerases
  JOURNAL   Proc Natl Acad Sci U S A 107 (47), 20305-20310 (2010)
   PUBMED   21059936
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Murphy,M., Docherty,N.G., Griffin,B., Howlin,J., McArdle,E.,
            McMahon,R., Schmid,H., Kretzler,M., Droguett,A., Mezzano,S.,
            Brady,H.R., Furlong,F., Godson,C. and Martin,F.
  TITLE     IHG-1 amplifies TGF-beta1 signaling and is increased in renal
            fibrosis
  JOURNAL   J Am Soc Nephrol 19 (9), 1672-1680 (2008)
   PUBMED   18508967
  REMARK    GeneRIF: induced in high glucose-1 (IHG-1)which increases in
            diabetic nephropathy, may enhance the actions of TGF-beta1 and
            contribute to the development of tubulointerstitial fibrosis
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Guo,D., Hu,K., Lei,Y., Wang,Y., Ma,T. and He,D.
  TITLE     Identification and characterization of a novel cytoplasm protein
            ICF45 that is involved in cell cycle regulation
  JOURNAL   J Biol Chem 279 (51), 53498-53505 (2004)
   PUBMED   15459185
  REMARK    GeneRIF: ICF45 is a highly conserved novel protein, which is
            expressed in a cell cycle-dependent manner and seemed to be
            involved in cell cycle progression and cell proliferation
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY463216.1, AC026407.4 and
            CA426270.1.
            
            On Mar 7, 2006 this sequence version replaced NP_060342.1.
            
            Summary: The protein encoded by this gene is a mitochondrial
            protein that is induced by high levels of glucose and is associated
            with diabetic nephropathy. The encoded protein appears to increase
            mitochondrial biogenesis, which could lead to renal fibrosis.
            Another function of this protein is that of a guanyltransferase,
            adding GMP to the 5' end of tRNA(His). Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.204482.1,
                                           SRR1803616.138890.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000231198.12/ ENSP00000231198.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..298
                     /product="probable tRNA(His) guanylyltransferase isoform
                     1"
                     /EC_number="2.7.7.79"
                     /note="probable tRNA(His) guanylyltransferase; interphase
                     cytoplasmic foci protein 45; induced by high glucose-1;
                     induced in high glucose-1"
                     /calculated_mol_wt=34700
     Region          35..164
                     /region_name="Thg1"
                     /note="tRNAHis guanylyltransferase; pfam04446"
                     /db_xref="CDD:461314"
     Region          167..283
                     /region_name="Thg1C"
                     /note="Thg1 C terminal domain; pfam14413"
                     /db_xref="CDD:464167"
     CDS             1..298
                     /gene="THG1L"
                     /gene_synonym="hTHG1; ICF45; IHG-1; IHG1; SCAR28; THG1"
                     /coded_by="NM_017872.5:22..918"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4341.1"
                     /db_xref="GeneID:54974"
                     /db_xref="HGNC:HGNC:26053"
                     /db_xref="MIM:618802"
ORIGIN      
        1 mwgackvkvh dslatisitl rrylrlgatm akskfeyvrd feaddtclah cwvvvrldgr
       61 nfhrfaekhn fakpndsral qlmtkcaqtv meeledivia ygqsdeysfv fkrktnwfkr
      121 raskfmthva sqfassyvfy wrdyfedqpl lyppgfdgrv vvypsnqtlk dylswrqadc
      181 hinnlyntvf waliqqsglt pvqaqgrlqg tlaadkneil fsefninynn elpmyrkgtv
      241 liwqkvdevm tkeiklptem egkkmavtrt rtkpvplhcd iigdafwkeh peildeds
//
LOCUS       NP_940918                607 aa            linear   PRI 27-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 18 isoform 1 [Homo
            sapiens].
ACCESSION   NP_940918 XP_350824
VERSION     NP_940918.2
DBSOURCE    REFSEQ: accession NM_198516.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Jia,W., Zou,X., Xu,Z., Bai,L., Shan,A., Li,Y., Shi,J., Yang,F.,
            Ding,C., Narimatsu,H. and Zhang,Y.
  TITLE     Polypeptide N-acetylgalactosaminyltransferase 18 retains in
            endoplasmic reticulum depending on its luminal regions interacting
            with ER resident UGGT1, PLOD3 and LPCAT1
  JOURNAL   Glycobiology 31 (8), 947-958 (2021)
   PUBMED   33909026
  REMARK    GeneRIF: Polypeptide N-acetylgalactosaminyltransferase 18 retains
            in endoplasmic reticulum depending on its luminal regions
            interacting with ER resident UGGT1, PLOD3 and LPCAT1.
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Wang,J., Bansal,A.T., Martin,M., Germer,S., Benayed,R., Essioux,L.,
            Lee,J.S., Begovich,A., Hemmings,A., Kenwright,A., Taylor,K.E.,
            Upmanyu,R., Cutler,P., Harari,O., Marchini,J., Criswell,L.A. and
            Platt,A.
  TITLE     Genome-wide association analysis implicates the involvement of
            eight loci with response to tocilizumab for the treatment of
            rheumatoid arthritis
  JOURNAL   Pharmacogenomics J 13 (3), 235-241 (2013)
   PUBMED   22491018
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Raman,J., Guan,Y., Perrine,C.L., Gerken,T.A. and Tabak,L.A.
  TITLE     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
            N-acetylgalactosaminyltransferases: completion of the family tree
  JOURNAL   Glycobiology 22 (6), 768-777 (2012)
   PUBMED   22186971
  REMARK    Erratum:[Glycobiology. 2015 Apr;25(4):465. doi:
            10.1093/glycob/cwv003. PMID: 25715345]
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Li,X., Wang,J., Li,W., Xu,Y., Shao,D., Xie,Y., Xie,W., Kubota,T.,
            Narimatsu,H. and Zhang,Y.
  TITLE     Characterization of ppGalNAc-T18, a member of the
            vertebrate-specific Y subfamily of
            UDP-N-acetyl-alpha-D-galactosamine:polypeptide
            N-acetylgalactosaminyltransferases
  JOURNAL   Glycobiology 22 (5), 602-615 (2012)
   PUBMED   22171061
REFERENCE   5  (residues 1 to 607)
  AUTHORS   Palmer,N.D., McDonough,C.W., Hicks,P.J., Roh,B.H., Wing,M.R.,
            An,S.S., Hester,J.M., Cooke,J.N., Bostrom,M.A., Rudock,M.E.,
            Talbert,M.E., Lewis,J.P., Ferrara,A., Lu,L., Ziegler,J.T.,
            Sale,M.M., Divers,J., Shriner,D., Adeyemo,A., Rotimi,C.N., Ng,M.C.,
            Langefeld,C.D., Freedman,B.I., Bowden,D.W., Voight,B.F.,
            Scott,L.J., Steinthorsdottir,V., Morris,A.P., Dina,C., Welch,R.P.,
            Zeggini,E., Huth,C., Aulchenko,Y.S., Thorleifsson,G.,
            McCulloch,L.J., Ferreira,T., Grallert,H., Amin,N., Wu,G.,
            Willer,C.J., Raychaudhuri,S., McCarroll,S.A., Langenberg,C.,
            Hofmann,O.M., Dupuis,J., Qi,L., Segre,A.V., van Hoek,M.,
            Navarro,P., Ardlie,K., Balkau,B., Benediktsson,R., Bennett,A.J.,
            Blagieva,R., Boerwinkle,E., Bonnycastle,L.L., Bostrom,K.B.,
            Bravenboer,B., Bumpstead,S., Burtt,N.P., Charpentier,G.,
            Chines,P.S., Cornelis,M., Couper,D.J., Crawford,G., Doney,A.S.,
            Elliott,K.S., Elliott,A.L., Erdos,M.R., Fox,C.S., Franklin,C.S.,
            Ganser,M., Gieger,C., Grarup,N., Green,T., Griffin,S., Groves,C.J.,
            Guiducci,C., Hadjadj,S., Hassanali,N., Herder,C., Isomaa,B.,
            Jackson,A.U., Johnson,P.R., Jorgensen,T., Kao,W.H., Klopp,N.,
            Kong,A., Kraft,P., Kuusisto,J., Lauritzen,T., Li,M., Lieverse,A.,
            Lindgren,C.M., Lyssenko,V., Marre,M., Meitinger,T., Midthjell,K.,
            Morken,M.A., Narisu,N., Nilsson,P., Owen,K.R., Payne,F.,
            Perry,J.R., Petersen,A.K., Platou,C., Proenca,C., Prokopenko,I.,
            Rathmann,W., Rayner,N.W., Robertson,N.R., Rocheleau,G., Roden,M.,
            Sampson,M.J., Saxena,R., Shields,B.M., Shrader,P., Sigurdsson,G.,
            Sparso,T., Strassburger,K., Stringham,H.M., Sun,Q., Swift,A.J.,
            Thorand,B., Tichet,J., Tuomi,T., van Dam,R.M., van Haeften,T.W.,
            van Herpt,T., van Vliet-Ostaptchouk,J.V., Walters,G.B.,
            Weedon,M.N., Wijmenga,C., Witteman,J., Bergman,R.N., Cauchi,S.,
            Collins,F.S., Gloyn,A.L., Gyllensten,U., Hansen,T., Hide,W.A.,
            Hitman,G.A., Hofman,A., Hunter,D.J., Hveem,K., Laakso,M.,
            Mohlke,K.L., Morris,A.D., Palmer,C.N., Pramstaller,P.P., Rudan,I.,
            Sijbrands,E., Stein,L.D., Tuomilehto,J., Uitterlinden,A.,
            Walker,M., Wareham,N.J., Watanabe,R.M., Abecasis,G.R., Boehm,B.O.,
            Campbell,H., Daly,M.J., Hattersley,A.T., Hu,F.B., Meigs,J.B.,
            Pankow,J.S., Pedersen,O., Wichmann,H.E., Barroso,I., Florez,J.C.,
            Frayling,T.M., Groop,L., Sladek,R., Thorsteinsdottir,U.,
            Wilson,J.F., Illig,T., Froguel,P., van Duijn,C.M., Stefansson,K.,
            Altshuler,D., Boehnke,M., McCarthy,M.I., Soranzo,N., Wheeler,E.,
            Glazer,N.L., Bouatia-Naji,N., Magi,R., Randall,J., Johnson,T.,
            Elliott,P., Rybin,D., Henneman,P., Dehghan,A., Hottenga,J.J.,
            Song,K., Goel,A., Egan,J.M., Lajunen,T., Doney,A., Kanoni,S.,
            Cavalcanti-Proenca,C., Kumari,M., Timpson,N.J., Zabena,C.,
            Ingelsson,E., An,P., O'Connell,J., Luan,J., Elliott,A.,
            McCarroll,S.A., Roccasecca,R.M., Pattou,F., Sethupathy,P.,
            Ariyurek,Y., Barter,P., Beilby,J.P., Ben-Shlomo,Y., Bergmann,S.,
            Bochud,M., Bonnefond,A., Borch-Johnsen,K., Bottcher,Y., Brunner,E.,
            Bumpstead,S.J., Chen,Y.D., Chines,P., Clarke,R., Coin,L.J.,
            Cooper,M.N., Crisponi,L., Day,I.N., de Geus,E.J., Delplanque,J.,
            Fedson,A.C., Fischer-Rosinsky,A., Forouhi,N.G., Frants,R.,
            Franzosi,M.G., Galan,P., Goodarzi,M.O., Graessler,J., Grundy,S.,
            Gwilliam,R., Hallmans,G., Hammond,N., Han,X., Hartikainen,A.L.,
            Hayward,C., Heath,S.C., Hercberg,S., Hicks,A.A., Hillman,D.R.,
            Hingorani,A.D., Hui,J., Hung,J., Jula,A., Kaakinen,M., Kaprio,J.,
            Kesaniemi,Y.A., Kivimaki,M., Knight,B., Koskinen,S., Kovacs,P.,
            Kyvik,K.O., Lathrop,G.M., Lawlor,D.A., Le Bacquer,O., Lecoeur,C.,
            Li,Y., Mahley,R., Mangino,M., Manning,A.K., Martinez-Larrad,M.T.,
            McAteer,J.B., McPherson,R., Meisinger,C., Melzer,D., Meyre,D.,
            Mitchell,B.D., Mukherjee,S., Naitza,S., Neville,M.J., Oostra,B.A.,
            Orru,M., Pakyz,R., Paolisso,G., Pattaro,C., Pearson,D., Peden,J.F.,
            Pedersen,N.L., Perola,M., Pfeiffer,A.F., Pichler,I., Polasek,O.,
            Posthuma,D., Potter,S.C., Pouta,A., Province,M.A., Psaty,B.M.,
            Rayner,N.W., Rice,K., Ripatti,S., Rivadeneira,F., Rolandsson,O.,
            Sandbaek,A., Sandhu,M., Sanna,S., Sayer,A.A., Scheet,P.,
            Seedorf,U., Sharp,S.J., Shields,B., Sijbrands,E.J., Silveira,A.,
            Simpson,L., Singleton,A., Smith,N.L., Sovio,U., Swift,A.,
            Syddall,H., Syvanen,A.C., Tanaka,T., Tonjes,A., Uitterlinden,A.G.,
            van Dijk,K.W., Varma,D., Visvikis-Siest,S., Vitart,V.,
            Vogelzangs,N., Waeber,G., Wagner,P.J., Walley,A., Ward,K.L.,
            Watkins,H., Wild,S.H., Willemsen,G., Witteman,J.C., Yarnell,J.W.,
            Zelenika,D., Zethelius,B., Zhai,G., Zhao,J.H., Zillikens,M.C.,
            Borecki,I.B., Loos,R.J., Meneton,P., Magnusson,P.K., Nathan,D.M.,
            Williams,G.H., Silander,K., Salomaa,V., Smith,G.D., Bornstein,S.R.,
            Schwarz,P., Spranger,J., Karpe,F., Shuldiner,A.R., Cooper,C.,
            Dedoussis,G.V., Serrano-Rios,M., Lind,L., Palmer,L.J., Franks,P.W.,
            Ebrahim,S., Marmot,M., Kao,W.H., Pramstaller,P.P., Wright,A.F.,
            Stumvoll,M., Hamsten,A., Buchanan,T.A., Valle,T.T., Rotter,J.I.,
            Siscovick,D.S., Penninx,B.W., Boomsma,D.I., Deloukas,P.,
            Spector,T.D., Ferrucci,L., Cao,A., Scuteri,A., Schlessinger,D.,
            Uda,M., Ruokonen,A., Jarvelin,M.R., Waterworth,D.M.,
            Vollenweider,P., Peltonen,L., Mooser,V. and Sladek,R.
  CONSRTM   DIAGRAM Consortium; MAGIC Investigators
  TITLE     A genome-wide association search for type 2 diabetes genes in
            African Americans
  JOURNAL   PLoS One 7 (1), e29202 (2012)
   PUBMED   22238593
REFERENCE   6  (residues 1 to 607)
  AUTHORS   Xu,J., Zheng,S.L., Isaacs,S.D., Wiley,K.E., Wiklund,F., Sun,J.,
            Kader,A.K., Li,G., Purcell,L.D., Kim,S.T., Hsu,F.C., Stattin,P.,
            Hugosson,J., Adolfsson,J., Walsh,P.C., Trent,J.M., Duggan,D.,
            Carpten,J., Gronberg,H. and Isaacs,W.B.
  TITLE     Inherited genetic variant predisposes to aggressive but not
            indolent prostate cancer
  JOURNAL   Proc Natl Acad Sci U S A 107 (5), 2136-2140 (2010)
   PUBMED   20080650
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 607)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131935.7, AB078147.1 and BC037341.2.
            
            On Feb 4, 2009 this sequence version replaced NP_940918.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060864.1, AK055111.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000227756.5/ ENSP00000227756.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..607
                     /product="polypeptide N-acetylgalactosaminyltransferase 18
                     isoform 1"
                     /EC_number="2.4.1.41"
                     /note="putative polypeptide
                     N-acetylgalactosaminyltransferase-like protein 4;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 15; GalNAc-transferase
                     18; galNAc-T-like protein 4; pp-GaNTase-like protein 4;
                     polypeptide GalNAc transferase-like protein 4; protein-UDP
                     acetylgalactosaminyltransferase-like protein 4;
                     UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase-like protein 4;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase-like 4; polypeptide
                     GalNAc transferase 18;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 18"
                     /calculated_mol_wt=69430
     Site            13..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P9A2.2)"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P9A2.2)"
     Region          153..267
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P9A2.2)"
     Region          157..458
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(161..163,165,194,228,231,235,251..253,332..333,
                     354..355,357,382,385,390)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P9A2.2)"
     Site            order(251,253,382)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Site            320
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P9A2.2)"
     Region          324..385
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P9A2.2)"
     Region          461..602
                     /region_name="beta-trefoil_Ricin_GALNT18"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide N-acetylgalactosaminyltransferase 18
                     (GALNT18) and similar proteins; cd23475"
                     /db_xref="CDD:467353"
     Site            order(484..487,494,496,499,503..504)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467353"
     Site            order(532..535,539,541,544,552..553)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467353"
     Site            order(573..576,587,589,592..594)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467353"
     CDS             1..607
                     /gene="GALNT18"
                     /gene_synonym="GalNAc-T15; GalNAc-T18; GALNACT18; GALNT15;
                     GALNTL4"
                     /coded_by="NM_198516.3:413..2236"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7807.1"
                     /db_xref="GeneID:374378"
                     /db_xref="HGNC:HGNC:30488"
                     /db_xref="MIM:615136"
ORIGIN      
        1 mvctrktktl vstcvilsgm tniicllyvg wvtnyiasvy vrgqepapdk kleedkgdtl
       61 kiierldhle nvikqhiqea pakpeeaeae pftdsslfah wgqelspegr rvalkqfqyy
      121 gynaylsdrl pldrplpdlr psgcrnlsfp dslpevsivf ifvnealsvl lrsihsamer
      181 tpphllkeii lvddnssnee lkeklteyvd kvnsqkpgfi kvvrhskqeg lirsrvsgwr
      241 aatapvvalf dahvefnvgw aepvltrike nrkriispsf dnikydnfei eeyplaaqgf
      301 dwelwcryln ppkawwklen stapirspal igcfivdrqy fqeiglldeg mevyggenve
      361 lgirvwqcgg svevlpcsri ahierahkpy tedltahvrr nalrvaevwm defkshvyma
      421 wnipqedsgi digditarka lrkqlqcktf rwylvsvype mrmysdiiay gvlqnslktd
      481 lcldqgpdte nvpimyichg mtpqnvyyts sqqihvgils ptvddddnrc lvdvnsrprl
      541 iecsyakakr mklhwqfsqg gpiqnrkskr clelqensdl efgfqlvlqk csgqhwsitn
      601 vlrslas
//
LOCUS       NP_001348966             774 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 14 [Mus musculus].
ACCESSION   NP_001348966
VERSION     NP_001348966.1
DBSOURCE    REFSEQ: accession NM_001362037.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 774)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 774)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 774)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 774)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 774)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            Transcript Variant: This variant (47), as well as variant 46,
            encodes isoform 14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AK032543.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMN00849374,
                                    SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..774
                     /product="cAMP-regulated phosphoprotein 21 isoform 14"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=84166
     Region          162..223
                     /region_name="R3H_encore_like"
                     /note="R3H domain of encore-like and DIP1-like proteins.
                     Drosophila encore is involved in the germline exit after
                     four mitotic divisions, by facilitating
                     SCF-ubiquitin-proteasome-dependent proteolysis. Maize
                     DBF1-interactor protein 1 (DIP1) containing an R3H...;
                     cd02642"
                     /db_xref="CDD:100071"
     Site            order(195,199)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100071"
     Region          520..>749
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..774
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362037.1:474..2798"
                     /note="isoform 14 is encoded by transcript variant 47"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqesih lqlssfpslq eedksrkdds erekekdknr
      121 eklserpkir mlskdcsqey tdstgidlhg flintlknns rdrmillkme qemidfiads
      181 nnhykkfpqm ssyqrmlvhr vaayfgldhn vdqtgksvii nktsstripe qrfcehlkde
      241 kseesqkrfi lkrdnssidk ednqsvcsqe slfldnsrlq edmhicnety kkrqlfrahr
      301 dssgrtsgsr qsssetelrw pdhqrawsst dsdssnrnlk ptmtktasfg gitvltrgds
      361 tsstrsagkl sktgsessss agssgslsrt hpqstaltss vaagspgcma ysengmggqv
      421 ppsstsyill plesatgipp gsillnphtg qpfvnpdgtp aiynppgsqq tlrgtvggqp
      481 qqppqqqpsp qpqqqvqasq pqmagplvtq reelaaqfsq lsmsrqssgd tpeppsgtvy
      541 pasllpqtaq pqsyvitsag qqlstggfsd sgppisqqvl qappspqgfv qqpppaqmsv
      601 yyypsgqypt stsqqyrpla svqysaqrsq qipqttqqag yqpvlsgqqg fqgmmgvqqs
      661 ahsqgvmssq qgapvhgvmv syptmssyqv pmtqgsqavp qqtyqppiml psqagqgslp
      721 atgmpvycnv tppnpqnnlr lmgphcpsst vpvmsascrt ncgnvsnagw qvkf
//
LOCUS       NP_055932                948 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger CCCH domain-containing protein 3 [Homo sapiens].
ACCESSION   NP_055932
VERSION     NP_055932.2
DBSOURCE    REFSEQ: accession NM_015117.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Silla,T., Schmid,M., Dou,Y., Garland,W., Milek,M., Imami,K.,
            Johnsen,D., Polak,P., Andersen,J.S., Selbach,M., Landthaler,M. and
            Jensen,T.H.
  TITLE     The human ZC3H3 and RBM26/27 proteins are critical for
            PAXT-mediated nuclear RNA decay
  JOURNAL   Nucleic Acids Res 48 (5), 2518-2530 (2020)
   PUBMED   31950173
  REMARK    GeneRIF: three additional proteins required for Poly(A) Tail
            eXosome Targeting (PAXT) function: ZC3H3, RBM26 and RBM27 along
            with the known PAXT-associated protein, PABPN1, were identified.
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Greliche,N., Germain,M., Lambert,J.C., Cohen,W., Bertrand,M.,
            Dupuis,A.M., Letenneur,L., Lathrop,M., Amouyel,P., Morange,P.E. and
            Tregouet,D.A.
  TITLE     A genome-wide search for common SNP x SNP interactions on the risk
            of venous thrombosis
  JOURNAL   BMC Med Genet 14, 36 (2013)
   PUBMED   23509962
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 948)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 948)
  AUTHORS   Hurt,J.A., Obar,R.A., Zhai,B., Farny,N.G., Gygi,S.P. and
            Silver,P.A.
  TITLE     A conserved CCCH-type zinc finger protein regulates mRNA nuclear
            adenylation and export
  JOURNAL   J Cell Biol 185 (2), 265-277 (2009)
   PUBMED   19364924
REFERENCE   6  (residues 1 to 948)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 948)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   8  (residues 1 to 948)
  AUTHORS   Collart,C., Remacle,J.E., Barabino,S., van Grunsven,L.A.,
            Nelles,L., Schellens,A., Van de Putte,T., Pype,S., Huylebroeck,D.
            and Verschueren,K.
  TITLE     Smicl is a novel Smad interacting protein and cleavage and
            polyadenylation specificity factor associated protein
  JOURNAL   Genes Cells 10 (9), 897-906 (2005)
   PUBMED   16115198
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM148116.1, AC067930.7, D63484.1 and AA806585.1.
            
            On Aug 14, 2007 this sequence version replaced NP_055932.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D63484.1, BC038670.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262577.6/ ENSP00000262577.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..948
                     /product="zinc finger CCCH domain-containing protein 3"
                     /note="smad-interacting CPSF-like factor; zinc finger
                     CCCH-type domain containing 3"
                     /calculated_mol_wt=101811
     Region          25..108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXZ2.3)"
     Region          121..219
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXZ2.3)"
     Region          265..296
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXZ2.3)"
     Region          336..493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXZ2.3)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IXZ2.3)"
     Region          <672..>777
                     /region_name="YTH1"
                     /note="Cleavage and polyadenylation specificity factor
                     (CPSF) Clipper subunit and related makorin family
                     Zn-finger proteins [General function prediction only];
                     COG5084"
                     /db_xref="CDD:227416"
     Region          798..891
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXZ2.3)"
     Region          913..948
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXZ2.3)"
     Site            918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IXZ2.3)"
     Site            920
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IXZ2.3)"
     CDS             1..948
                     /gene="ZC3H3"
                     /gene_synonym="SMICL; ZC3HDC3"
                     /coded_by="NM_015117.3:27..2873"
                     /db_xref="CCDS:CCDS6402.1"
                     /db_xref="GeneID:23144"
                     /db_xref="HGNC:HGNC:28972"
                     /db_xref="MIM:618640"
ORIGIN      
        1 meekeilrrq irllqglidd yktlhgnapa pgtpaasgwq pptyhsgraf saryprpsrr
       61 gysshhgpsw rkkyslvnrp pgpsdppadh avrplhgarg gqppvpqqhv lerqvqlsqg
      121 qnvvikvkpp sksgsasasg aqrgsleefe etpwsdqrpr egegepprgq lqpsrptrar
      181 gtcsvedpll vcqkepgkpr mvksvgsvgd spreprrtvs esviavkasf pssalpprtg
      241 valgrklgsh svascapqll gdrrvdaght dqpvpsgsvg gparpasgpr qareaslvvt
      301 crtnkfrknn ykwvaassks prvarralsp rvaaenvcka sagmankvek pqliadpepk
      361 prkpatsskp gsapskykwk asspsassss sfrwqseass kdhasqlspv lsrspsgdrp
      421 avghsglkpl sgetplsayk vksrtkiirr rsstslpgdk ksgtspaata kshlslrrrq
      481 alrgksspvl kktpnkglvq vtthrlcrlp psrahlptke asslhavrta ptskviktry
      541 rivkktpasp lsappfplsl pswrarrlsl srslvlnrlr pvasgggkaq pgspwwrskg
      601 yrciggvlyk vsanklskts gqpsdagsrp llrtgrldpa gscsrslasr avqrslaiir
      661 qarqrrekrk eycmyynrfg rcnrgercpy ihdpekvavc trfvrgtckk tdgtcpfshh
      721 vskekmpvcs yflkgicsns ncpyshvyvs rkaevcsdfl kgycplgakc kkkhtllcpd
      781 farrgacprg aqcqllhrtq krhsrraats papgpsdata rsrvsashgp rkpsasqrpt
      841 rqtpssaalt aaavaapphc pggsaspsss kassssssss sppasldhea pslqeaalaa
      901 acsnrlcklp sfislqssps pgaqprvrap rapltkdsgk plhikprl
//
LOCUS       NP_077343                893 aa            linear   ROD 27-APR-2025
DEFINITION  ephrin type-A receptor 5 isoform 2 [Rattus norvegicus].
ACCESSION   NP_077343
VERSION     NP_077343.1
DBSOURCE    REFSEQ: accession NM_024367.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Song,H., Zheng,Y., Cai,F., Ma,Y., Yang,J. and Wu,Y.
  TITLE     c-Fos downregulation positively regulates EphA5 expression in a
            congenital hypothyroidism rat model
  JOURNAL   J Mol Histol 49 (2), 147-155 (2018)
   PUBMED   29330744
  REMARK    GeneRIF: c-fos overexpression could upregulate EphA5 expression in
            hippocampal neurons of rats with congenital hypothyroidism.
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Liu,T.T., Xiao,B., Li,S.Y., Li,G.L., Lu,X.Q. and Liu,W.P.
  TITLE     [Changes in the expression of EphA5/ephrinA5 in the CA3 region of
            the hippocampus in rats with epilepsy and their role in the
            pathogenesis of temporal lobe epilepsy]
  JOURNAL   Zhongguo Dang Dai Er Ke Za Zhi 19 (12), 1272-1277 (2017)
   PUBMED   29237529
  REMARK    GeneRIF: Downregulation of ephrinA5 and EphA5 in the CA3 region of
            the hippocampus may participate in the mechanism of mossy fiber
            sprouting and is closely associated with the development and
            progression of epilepsy.
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Wu,Y., Song,H., Sun,B., Xu,M. and Shi,J.
  TITLE     DNA Methylation of the EphA5 Promoter Is Associated with Rat
            Congenital Hypothyroidism
  JOURNAL   J Mol Neurosci 57 (2), 203-210 (2015)
   PUBMED   26109526
  REMARK    GeneRIF: EphA5 promoter methylation in the hippocampus of rats with
            congenital hypothyroidism is associated with the levels of EphA5
            expression.
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Szepietowska,B., Horvath,T.L. and Sherwin,R.S.
  TITLE     Role of synaptic plasticity and EphA5-ephrinA5 interaction within
            the ventromedial hypothalamus in response to recurrent hypoglycemia
  JOURNAL   Diabetes 63 (3), 1140-1147 (2014)
   PUBMED   24222347
  REMARK    GeneRIF: changes in ephrinA5/EphA5 interactions and synaptic
            plasticity within the ventromedial hypothalamus may contribute to
            the impairment in glucagon secretion and counterregulatory
            responses caused by recurrent hypoglycemia.
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Buensuceso,A.V. and Deroo,B.J.
  TITLE     The ephrin signaling pathway regulates morphology and adhesion of
            mouse granulosa cells in vitro
  JOURNAL   Biol Reprod 88 (1), 25 (2013)
   PUBMED   23242526
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 893)
  AUTHORS   Bruce,V., Olivieri,G., Eickelberg,O. and Miescher,G.C.
  TITLE     Functional activation of EphA5 receptor does not promote cell
            proliferation in the aberrant EphA5 expressing human glioblastoma
            U-118 MG cell line
  JOURNAL   Brain Res 821 (1), 169-176 (1999)
   PUBMED   10064801
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Miescher,G.C., Taylor,V., Olivieri,G., Mindermann,T., Schrock,E.
            and Steck,A.J.
  TITLE     Extensive splice variation and localization of the EHK-1 receptor
            tyrosine kinase in adult human brain and glial tumors
  JOURNAL   Brain Res Mol Brain Res 46 (1-2), 17-24 (1997)
   PUBMED   9191074
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Winslow,J.W., Moran,P., Valverde,J., Shih,A., Yuan,J.Q., Wong,S.C.,
            Tsai,S.P., Goddard,A., Henzel,W.J., Hefti,F. et al.
  TITLE     Cloning of AL-1, a ligand for an Eph-related tyrosine kinase
            receptor involved in axon bundle formation
  JOURNAL   Neuron 14 (5), 973-981 (1995)
   PUBMED   7748564
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Taylor,V., Miescher,G.C., Pfarr,S., Honegger,P., Breitschopf,H.,
            Lassmann,H. and Steck,A.J.
  TITLE     Expression and developmental regulation of Ehk-1, a neuronal
            Elk-like receptor tyrosine kinase in brain
  JOURNAL   Neuroscience 63 (1), 163-178 (1994)
   PUBMED   7898646
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Maisonpierre,P.C., Barrezueta,N.X. and Yancopoulos,G.D.
  TITLE     Ehk-1 and Ehk-2: two novel members of the Eph receptor-like
            tyrosine kinase family with distinctive structures and neuronal
            expression
  JOURNAL   Oncogene 8 (12), 3277-3288 (1993)
   PUBMED   7504232
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region and uses an alternate splice
            pattern in the 3' coding region, compared to variant 1. The
            resulting isoform (2) lacks an internal segment and has a shorter
            and distinct C-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X78689.1, SRR26360176.1696901.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..893
                     /product="ephrin type-A receptor 5 isoform 2"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 5; EPH homology kinase 1;
                     tyrosine-protein kinase receptor EHK-1; eck-like sequence
                     1"
                     /calculated_mol_wt=98905
     Region          62..234
                     /region_name="EphR_LBD"
                     /note="Ligand Binding Domain of Ephrin Receptors; cl02704"
                     /db_xref="CDD:470656"
     Site            order(74,86..89,91..92,97,99,102,135,137,185,193..195,
                     222..224,226)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198439"
     Region          359..449
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(359,422,437)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(438..439,441..442)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          465..562
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          560..826
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(571,573..575,579,595,597,643..644,646,690,694..695,
                     697,708,727..731,740,774)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(571..575,579,595,597,643..646,649..650,694..695,697,
                     708)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            order(690,694,727..731,740,774)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            707..733
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Region          855..>893
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     CDS             1..893
                     /gene="Epha5"
                     /gene_synonym="EHK-1; Els1; Els1."
                     /coded_by="NM_024367.2:358..3039"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:79208"
                     /db_xref="RGD:620831"
ORIGIN      
        1 mrgsgprgag rrrtqgrggg gdtprvpasl agcysaplkg plwtclllca alrtllasps
       61 nevnlldsrt vlgdlgwiaf pkngweeige vdenyapiht yqvckvmeqn qnnwlltswi
      121 snegasrifi elkftlrdcn slpgglgtck etfnmyyfes ddengrnike nqyikidtia
      181 adesfteldl gdrvmklnte vrdvgplskk gfylafqdvg acialvsvrv yykkcpsvvr
      241 hlavfpdtit gadssqllev sgscvnhsvt ddppkmhcsa egewlvpigk cmckagyeek
      301 ngtcqvcrpg ffkasphsqt cskcpphsyt heeastscvc ekdyfrresd pptmacttps
      361 pvtnvkkgki aknsislswq epdrpngiil eyeikyfekd qetsytiiks kettitaegl
      421 kpasvyvfqi rartaagygv fsrrfefett pvfaasndqs qipiiavsvt vgvillavmi
      481 gfllsgscce cgcgrasslc avahpsliwr cgyskakqdp eeekmhfhng hiklpgvrty
      541 idphtyedpt qavhefakei eascitierv igagefgevc sgrlklpgkr elpvaiktlk
      601 vgytekqrrd flseasimgq fdhpniihle gvvtkskpvm ivteymengs ldtflkkndg
      661 qftviqlvgm lrgiaagmky lsdmgyvhrd laarnilins nlvckvsdfg lsrvleddpe
      721 aayttrggki pirwtapeai afrkftsasd vwsygivmwe vvsygerpyw emtnqdvika
      781 veegyrlpsp mdcpaalyql mldcwqkdrn srpkfddivn mldklirnps slktlvnass
      841 rvstllaehg slgsgayrsv gewleaikmg ryteifmeng yssmdavaqv tle
//
LOCUS       NP_004988                477 aa            linear   PRI 27-APR-2025
DEFINITION  myosin-binding protein H [Homo sapiens].
ACCESSION   NP_004988
VERSION     NP_004988.2
DBSOURCE    REFSEQ: accession NM_004997.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Mouton,J.M., van der Merwe,L., Goosen,A., Revera,M., Brink,P.A.,
            Moolman-Smook,J.C. and Kinnear,C.
  TITLE     MYBPH acts as modifier of cardiac hypertrophy in hypertrophic
            cardiomyopathy (HCM) patients
  JOURNAL   Hum Genet 135 (5), 477-483 (2016)
   PUBMED   26969327
  REMARK    GeneRIF: variation in MYBPH can modulate the severity of
            hypertrophy in hypertrophic cardiomyopathy patients.
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Goldstein,J.I., Jarskog,L.F., Hilliard,C., Alfirevic,A., Duncan,L.,
            Fourches,D., Huang,H., Lek,M., Neale,B.M., Ripke,S., Shianna,K.,
            Szatkiewicz,J.P., Tropsha,A., van den Oord,E.J., Cascorbi,I.,
            Dettling,M., Gazit,E., Goff,D.C., Holden,A.L., Kelly,D.L.,
            Malhotra,A.K., Nielsen,J., Pirmohamed,M., Rujescu,D., Werge,T.,
            Levy,D.L., Josiassen,R.C., Kennedy,J.L., Lieberman,J.A., Daly,M.J.
            and Sullivan,P.F.
  TITLE     Clozapine-induced agranulocytosis is associated with rare HLA-DQB1
            and HLA-B alleles
  JOURNAL   Nat Commun 5, 4757 (2014)
   PUBMED   25187353
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Conti,A., Riva,N., Pesca,M., Iannaccone,S., Cannistraci,C.V.,
            Corbo,M., Previtali,S.C., Quattrini,A. and Alessio,M.
  TITLE     Increased expression of Myosin binding protein H in the skeletal
            muscle of amyotrophic lateral sclerosis patients
  JOURNAL   Biochim Biophys Acta 1842 (1), 99-106 (2014)
   PUBMED   24184715
  REMARK    GeneRIF: MyBP-H expression signals the onset of dysregulation in
            actin-myosin interaction; this in turn might contribute to the
            pathogenesis of amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Blandin,G., Marchand,S., Charton,K., Daniele,N., Gicquel,E.,
            Boucheteil,J.B., Bentaib,A., Barrault,L., Stockholm,D., Bartoli,M.
            and Richard,I.
  TITLE     A human skeletal muscle interactome centered on proteins involved
            in muscular dystrophies: LGMD interactome
  JOURNAL   Skelet Muscle 3 (1), 3 (2013)
   PUBMED   23414517
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Hosono,Y., Usukura,J., Yamaguchi,T., Yanagisawa,K., Suzuki,M. and
            Takahashi,T.
  TITLE     MYBPH inhibits NM IIA assembly via direct interaction with NMHC IIA
            and reduces cell motility
  JOURNAL   Biochem Biophys Res Commun 428 (1), 173-178 (2012)
   PUBMED   23068101
  REMARK    GeneRIF: These results suggest that MYBPH inhibits RLC and NMHC
            IIA, independent components of NM IIA, and negatively regulates
            actomyosin organization at 2 distinct steps, resulting in firm
            inhibition of NM IIA assembly.
REFERENCE   6  (residues 1 to 477)
  AUTHORS   Hosono,Y., Yamaguchi,T., Mizutani,E., Yanagisawa,K., Arima,C.,
            Tomida,S., Shimada,Y., Hiraoka,M., Kato,S., Yokoi,K., Suzuki,M. and
            Takahashi,T.
  TITLE     MYBPH, a transcriptional target of TTF-1, inhibits ROCK1, and
            reduces cell motility and metastasis
  JOURNAL   EMBO J 31 (2), 481-493 (2012)
   PUBMED   22085929
  REMARK    GeneRIF: MYBPH inhibited assembly competence-conferring
            phosphorylation of the myosin regulatory light chain (RLC) as well
            as activating phosphorylation of LIM domain kinase, unexpectedly
            through its direct physical interaction with Rho kinase 1
REFERENCE   7  (residues 1 to 477)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 477)
  AUTHORS   Welikson,R.E. and Fischman,D.A.
  TITLE     The C-terminal IgI domains of myosin-binding proteins C and H
            (MyBP-C and MyBP-H) are both necessary and sufficient for the
            intracellular crosslinking of sarcomeric myosin in transfected
            non-muscle cells
  JOURNAL   J Cell Sci 115 (Pt 17), 3517-3526 (2002)
   PUBMED   12154082
REFERENCE   9  (residues 1 to 477)
  AUTHORS   Gruen,M. and Gautel,M.
  TITLE     Mutations in beta-myosin S2 that cause familial hypertrophic
            cardiomyopathy (FHC) abolish the interaction with the regulatory
            domain of myosin-binding protein-C
  JOURNAL   J Mol Biol 286 (3), 933-949 (1999)
   PUBMED   10024460
REFERENCE   10 (residues 1 to 477)
  AUTHORS   Vaughan,K.T., Weber,F.E., Ried,T., Ward,D.C., Reinach,F.C. and
            Fischman,D.A.
  TITLE     Human myosin-binding protein H (MyBP-H): complete primary sequence,
            genomic organization, and chromosomal localization
  JOURNAL   Genomics 16 (1), 34-40 (1993)
   PUBMED   8486381
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC105940.2, BC044226.1 and L05606.1.
            
            On Nov 22, 2004 this sequence version replaced NP_004988.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.2552.1, BC044226.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000255416.9/ ENSP00000255416.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..477
                     /product="myosin-binding protein H"
                     /note="myBP-H; H-protein"
                     /calculated_mol_wt=51919
     Region          1..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13203.4)"
     Region          <4..>69
                     /region_name="rad23"
                     /note="UV excision repair protein Rad23; TIGR00601"
                     /db_xref="CDD:273167"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88599; propagated from
                     UniProtKB/Swiss-Prot (Q13203.4)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88599; propagated from
                     UniProtKB/Swiss-Prot (Q13203.4)"
     Region          71..157
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(71,137,152)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(153..154,156..157)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          183..263
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          192..196
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409406"
     Region          205..209
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409406"
     Region          229..233
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409406"
     Region          243..248
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409406"
     Region          256..259
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409406"
     Region          267..355
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(267,332,347)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(348..349,351..352)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          382..471
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          399..403
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409543"
     Region          412..416
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409543"
     Region          437..441
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409543"
     Region          451..456
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409543"
     Region          464..467
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409543"
     CDS             1..477
                     /gene="MYBPH"
                     /coded_by="NM_004997.3:72..1505"
                     /db_xref="CCDS:CCDS30975.1"
                     /db_xref="GeneID:4608"
                     /db_xref="HGNC:HGNC:7552"
                     /db_xref="MIM:160795"
ORIGIN      
        1 mmekntsegp acspeetase sakvptaepp gevavsestr eeqvpkpqap apqaptasta
       61 tkpappsedv psapllltld dvssssvtvs wepperlgrl glqgyvlelc regasewvpv
      121 sarpmmvtqq tvrnlalgdk fllrvsavss agagppamld qpihirenie apkirvprhl
      181 rqtyirqvge tvnlqipfqg kpkpqatwth nghaldsqrv smrtgdqdsi lfirsaqrsd
      241 sgryeltvrv edleakavid ilviekpgpp ssirlldvwg cnaalqwtpp qdtgntellg
      301 ymvqkadkkt gqwftvlery hpttctisdl iignsysfrv fsenlcglst satvtkelah
      361 iqkadiaakp kgfierdfse apsftqplad htstpgystq lfcsvraspk pkiiwmknkm
      421 eiqgnpkyra lseqgvctle irkpspfdsg vytckainvl geasvdcrle vkasaah
//
LOCUS       NP_079103                347 aa            linear   PRI 27-APR-2025
DEFINITION  histone deacetylase 11 isoform 1 [Homo sapiens].
ACCESSION   NP_079103
VERSION     NP_079103.2
DBSOURCE    REFSEQ: accession NM_024827.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Shi,J.Q., Liu,X.F. and Wang,C.
  TITLE     [Progress on the involvement of HDAC11 in the regulation of
            mammalian oocyte maturation and early embryonic development]
  JOURNAL   Sheng Li Xue Bao 76 (3), 438-446 (2024)
   PUBMED   38939938
  REMARK    GeneRIF: [Progress on the involvement of HDAC11 in the regulation
            of mammalian oocyte maturation and early embryonic development].
            Review article
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Byeon,H.E., Choi,S.E., Kim,Y., Choi,S., Lee,S.J., Kim,D.H., Mo,J.S.
            and Jeon,J.Y.
  TITLE     HDAC11 Regulates Palmitate-induced NLRP3 Inflammasome Activation by
            Inducing YAP Expression in THP-1 Cells and PBMCs
  JOURNAL   Endocrinology 165 (3) (2024)
   PUBMED   38366363
  REMARK    GeneRIF: HDAC11 Regulates Palmitate-induced NLRP3 Inflammasome
            Activation by Inducing YAP Expression in THP-1 Cells and PBMCs.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Liu,Y., Tong,X., Hu,W. and Chen,D.
  TITLE     HDAC11: A novel target for improved cancer therapy
  JOURNAL   Biomed Pharmacother 166, 115418 (2023)
   PUBMED   37659201
  REMARK    GeneRIF: HDAC11: A novel target for improved cancer therapy.
            Review article
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Wu,H., Yin,X., Zhao,X., Wu,Z., Xiao,Y., Di,Q., Sun,P., Tang,H.,
            Quan,J. and Chen,W.
  TITLE     HDAC11 negatively regulates antifungal immunity by inhibiting Nos2
            expression via binding with transcriptional repressor STAT3
  JOURNAL   Redox Biol 56, 102461 (2022)
   PUBMED   36087429
  REMARK    GeneRIF: HDAC11 negatively regulates antifungal immunity by
            inhibiting Nos2 expression via binding with transcriptional
            repressor STAT3.
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Li,R., Wu,X., Zhao,P., Xue,K. and Li,J.
  TITLE     A pan-cancer analysis identifies HDAC11 as an immunological and
            prognostic biomarker
  JOURNAL   FASEB J 36 (7), e22326 (2022)
   PUBMED   35657209
  REMARK    GeneRIF: A pan-cancer analysis identifies HDAC11 as an
            immunological and prognostic biomarker.
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Feng,W., Lu,Z., Luo,R.Z., Zhang,X., Seto,E., Liao,W.S. and Yu,Y.
  TITLE     Multiple histone deacetylases repress tumor suppressor gene ARHI in
            breast cancer
  JOURNAL   Int J Cancer 120 (8), 1664-1668 (2007)
   PUBMED   17230502
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Lindberg,D., Akerstrom,G. and Westin,G.
  TITLE     Mutational analyses of WNT7A and HDAC11 as candidate tumour
            suppressor genes in sporadic malignant pancreatic endocrine tumours
  JOURNAL   Clin Endocrinol (Oxf) 66 (1), 110-114 (2007)
   PUBMED   17201809
  REMARK    GeneRIF: the absence of tumour-specific somatic events in WNT7A and
            HDAC11 suggests that these genes are unlikely to have a classical
            tumour suppressor gene role in sporadic malignant pancreatic
            endocrine tumours
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Voelter-Mahlknecht,S., Ho,A.D. and Mahlknecht,U.
  TITLE     Chromosomal organization and localization of the novel class IV
            human histone deacetylase 11 gene
  JOURNAL   Int J Mol Med 16 (4), 589-598 (2005)
   PUBMED   16142391
  REMARK    GeneRIF: Fluorescence in situ hybridization analysis localized
            HDAC11 gene to chromosome 3p25, a region characterized by frequent
            gains and losses of chromosomal material in a number of various
            types of cancer.
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Bradbury,C.A., Khanim,F.L., Hayden,R., Bunce,C.M., White,D.A.,
            Drayson,M.T., Craddock,C. and Turner,B.M.
  TITLE     Histone deacetylases in acute myeloid leukaemia show a distinctive
            pattern of expression that changes selectively in response to
            deacetylase inhibitors
  JOURNAL   Leukemia 19 (10), 1751-1759 (2005)
   PUBMED   16121216
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Gao,L., Cueto,M.A., Asselbergs,F. and Atadja,P.
  TITLE     Cloning and functional characterization of HDAC11, a novel member
            of the human histone deacetylase family
  JOURNAL   J Biol Chem 277 (28), 25748-25755 (2002)
   PUBMED   11948178
  REMARK    GeneRIF: cloning and functional characterization
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB025431.1, BC009676.1,
            AC027124.5 and AW291816.1.
            
            On Dec 11, 2008 this sequence version replaced NP_079103.1.
            
            Summary: This gene encodes a class IV histone deacetylase. The
            encoded protein is localized to the nucleus and may be involved in
            regulating the expression of interleukin 10. Alternative splicing
            results in multiple transcript variants.[provided by RefSeq, Apr
            2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.648618.1,
                                           SRR1660807.265243.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295757.8/ ENSP00000295757.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..347
                     /product="histone deacetylase 11 isoform 1"
                     /EC_number="3.5.1.98"
                     /calculated_mol_wt=39052
     Region          14..326
                     /region_name="Histone deacetylase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DB2.1)"
     Region          35..319
                     /region_name="HDAC_classIV"
                     /note="Histone deacetylase class IV also known as histone
                     deacetylase 11; cd09993"
                     /db_xref="CDD:212519"
     Site            order(41,140..143,151..153,181,183,257,261,301..302,304)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:212519"
     CDS             1..347
                     /gene="HDAC11"
                     /gene_synonym="HD11"
                     /coded_by="NM_024827.4:43..1086"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2615.1"
                     /db_xref="GeneID:79885"
                     /db_xref="HGNC:HGNC:19086"
                     /db_xref="MIM:607226"
ORIGIN      
        1 mlhttqlyqh vpetrwpivy sprynitfmg leklhpfdag kwgkvinflk eekllsdsml
       61 veareaseed llvvhtrryl nelkwsfava titeippvif lpnflvqrkv lrplrtqtgg
      121 timagklave rgwainvggg fhhcssdrgg gfcayaditl aikflferve gisratiidl
      181 dahqgngher dfmddkrvyi mdvynrhiyp gdrfakqair rkvelewgte ddeyldkver
      241 nikkslqehl pdvvvynagt dilegdrlgg lsispagivk rdelvfrmvr grrvpilmvt
      301 sggyqkrtar iiadsilnlf glgligpesp svsaqnsdtp llppavp
//
LOCUS       NP_079469                369 aa            linear   PRI 27-APR-2025
DEFINITION  3 beta-hydroxysteroid dehydrogenase type 7 isoform a [Homo
            sapiens].
ACCESSION   NP_079469
VERSION     NP_079469.2
DBSOURCE    REFSEQ: accession NM_025193.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Zhao,J., Setchell,K.D.R., Gong,Y., Sun,Y., Zhang,P., Heubi,J.E.,
            Fang,L., Lu,Y., Xie,X., Gong,J. and Wang,J.S.
  TITLE     Genetic spectrum and clinical characteristics of
            3beta-hydroxy-Delta5-C27-steroid oxidoreductase (HSD3B7) deficiency
            in China
  JOURNAL   Orphanet J Rare Dis 16 (1), 417 (2021)
   PUBMED   34627351
  REMARK    GeneRIF: Genetic spectrum and clinical characteristics of
            3beta-hydroxy-Delta(5)-C27-steroid oxidoreductase (HSD3B7)
            deficiency in China.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Lu,Z.J., Wang,L., Sun,X.Y., Li,J.Y., Cheng,L., Li,N.N. and Peng,R.
  TITLE     The association between HSD3B7 gene variant and Parkinson's disease
            in ethnic Chinese
  JOURNAL   Brain Behav 8 (4), e00913 (2018)
   PUBMED   29670816
  REMARK    GeneRIF: In the classical pathway, HSD3B7 catalyzes the second step
            of bile acid formation and its mutations may reduce the synthetic
            capability.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Huang,H.Y., Zhou,H., Wang,H., Chen,Y.X. and Fang,F.
  TITLE     Novel Mutations in the 3beta-hydroxy-5-C27-steroid Dehydrogenase
            Gene (HSD3B7) in a Patient with Neonatal Cholestasis
  JOURNAL   Chin Med J (Engl) 129 (1), 98-100 (2016)
   PUBMED   26712441
  REMARK    GeneRIF: Novel Mutations in the 3beta-hydroxy-5-C27-steroid
            Dehydrogenase Gene (HSD3B7) in a Patient with Neonatal Cholestasis.
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Plaza-Parrochia,F., Poblete,C., Gabler,F., Carvajal,R., Romero,C.,
            Valladares,L. and Vega,M.
  TITLE     Expression of steroid sulfated transporters and 3beta-HSD activity
            in endometrium of women having polycystic ovary syndrome
  JOURNAL   Steroids 104, 189-195 (2015)
   PUBMED   26450365
  REMARK    GeneRIF: Expression of steroid sulfated transporters and 3beta-HSD
            activity in endometrium of polycystic ovary syndrome
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Cheng,J.B., Jacquemin,E., Gerhardt,M., Nazer,H., Cresteil,D.,
            Heubi,J.E., Setchell,K.D. and Russell,D.W.
  TITLE     Molecular genetics of 3beta-hydroxy-Delta5-C27-steroid
            oxidoreductase deficiency in 16 patients with loss of bile acid
            synthesis and liver disease
  JOURNAL   J Clin Endocrinol Metab 88 (4), 1833-1841 (2003)
   PUBMED   12679481
REFERENCE   9  (residues 1 to 369)
  AUTHORS   Schwarz,M., Wright,A.C., Davis,D.L., Nazer,H., Bjorkhem,I. and
            Russell,D.W.
  TITLE     The bile acid synthetic gene 3beta-hydroxy-Delta(5)-C(27)-steroid
            oxidoreductase is mutated in progressive intrahepatic cholestasis
  JOURNAL   J Clin Invest 106 (9), 1175-1184 (2000)
   PUBMED   11067870
REFERENCE   10 (residues 1 to 369)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135048.2 and BC004929.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_079469.1.
            
            Summary: This gene encodes an enzyme which is involved in the
            initial stages of the synthesis of bile acids from cholesterol and
            a member of the short-chain dehydrogenase/reductase superfamily.
            The encoded protein is a membrane-associated endoplasmic reticulum
            protein which is active against 7-alpha hydrosylated sterol
            substrates. Mutations in this gene are associated with a congenital
            bile acid synthesis defect which leads to neonatal cholestasis, a
            form of progressive liver disease. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX379834.2, BC004929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297679.10/ ENSP00000297679.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..369
                     /product="3 beta-hydroxysteroid dehydrogenase type 7
                     isoform a"
                     /EC_number="1.1.1.181"
                     /note="3 beta-hydroxy-delta 5-C27-steroid oxidoreductase;
                     short chain dehydrogenase/reductase family 11E, member 3;
                     C(27)-3BETA-HSD; 3 beta-hydroxysteroid dehydrogenase type
                     VII; 3-beta-HSD VII; 3 beta-hydroxysteroid dehydrogenase
                     type 7; c(27) 3-beta-HSD; 3-beta-hydroxy-Delta(5)-C27
                     steroid oxidoreductase; cholest-5-ene-3-beta,7-alpha-diol
                     3-beta-dehydrogenase"
                     /calculated_mol_wt=40885
     Region          11..361
                     /region_name="3b-HSD_HSDB1_like_SDR_e"
                     /note="human 3beta-HSD (hydroxysteroid dehydrogenase) and
                     HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs;
                     cd09811"
                     /db_xref="CDD:187671"
     Site            order(16,18..21,43..45,86..88,104,127..129,159,163,
                     191..194)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187671"
     Site            order(105,129,159,163)
                     /site_type="active"
                     /db_xref="CDD:187671"
     Site            order(129,159,193,206,216,221)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187671"
     Site            289..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2F3.2)"
     Site            311..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2F3.2)"
     CDS             1..369
                     /gene="HSD3B7"
                     /gene_synonym="CBAS1; PFIC4; SDR11E3"
                     /coded_by="NM_025193.4:98..1207"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10698.1"
                     /db_xref="GeneID:80270"
                     /db_xref="HGNC:HGNC:18324"
                     /db_xref="MIM:607764"
ORIGIN      
        1 madsaqaqkl vylvtggcgf lgehvvrmll qreprlgelr vfdqhlgpwl eelktgpvrv
       61 taiqgdvtqa hevaaavaga hvvihtaglv dvfgraspkt ihevnvqgtr nvieacvqtg
      121 trflvytssm evvgpntkgh pfyrgnedtp yeavhrhpyp cskalaewlv leangrkvrg
      181 glplvtcalr ptgiygeghq imrdfyrqgl rlggwlfrai pasvehgrvy vgnvawmhvl
      241 aareleqrat lmggqvyfcy dgspyrsyed fnmeflgpcg lrlvgarpll pywllvflaa
      301 lnallqwllr plvlyaplln pytlavantt ftvstdkaqr hfgyeplfsw edsrtrtilw
      361 vqaatgsaq
//
LOCUS       NP_000428                392 aa            linear   PRI 27-APR-2025
DEFINITION  platelet-activating factor acetylhydrolase 2, cytoplasmic [Homo
            sapiens].
ACCESSION   NP_000428
VERSION     NP_000428.2
DBSOURCE    REFSEQ: accession NM_000437.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Moschos,M.M., Pantazis,P., Gatzioufas,Z., Panos,G.D., Gazouli,M.,
            Nitoda,E. and Brouzas,D.
  TITLE     'Association between platelet activating factor acetylhydrolase and
            diabetic retinopathy: Does inflammation affect the retinal status?'
  JOURNAL   Prostaglandins Other Lipid Mediat 122, 69-72 (2016)
   PUBMED   26791393
  REMARK    GeneRIF: Data show that the activity of plasma platelet activating
            factor acetylhydrolase (PAF-AH) increases in parallel with diabetic
            retinopathy (DR) severity.
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Monillas,E.S., Caplan,J.L., Thevenin,A.F. and Bahnson,B.J.
  TITLE     Oligomeric state regulated trafficking of human platelet-activating
            factor acetylhydrolase type-II
  JOURNAL   Biochim Biophys Acta 1854 (5), 469-475 (2015)
   PUBMED   25707358
  REMARK    GeneRIF: The oligomeric state of PAFAH-II drives functional protein
            trafficking. PAFAH-II localization to the membrane is critical for
            substrate acquisition and effective oxidative stress protection.
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Schmidt,E.B., Koenig,W., Khuseyinova,N. and Christensen,J.H.
  TITLE     Lipoprotein-associated phospholipase A2 concentrations in plasma
            are associated with the extent of coronary artery disease and
            correlate to adipose tissue levels of marine n-3 fatty acids
  JOURNAL   Atherosclerosis 196 (1), 420-424 (2008)
   PUBMED   17157859
  REMARK    GeneRIF: Lp-PLA2 was higher in those with more extensive Coronary
            artery disease
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Umemura,K., Kato,I., Hirashima,Y., Ishii,Y., Inoue,T., Aoki,J.,
            Kono,N., Oya,T., Hayashi,N., Hamada,H., Endo,S., Oda,M., Arai,H.,
            Kinouchi,H. and Hiraga,K.
  TITLE     Neuroprotective role of transgenic PAF-acetylhydrolase II in mouse
            models of focal cerebral ischemia
  JOURNAL   Stroke 38 (3), 1063-1068 (2007)
   PUBMED   17272759
  REMARK    GeneRIF: PAF-AH II exerts strong neuroprotective effects against
            ischemic injury: the neurological deficit scores, cerebral edema
            index, and relative infarction volume are all significantly lower
            in PAFAH2 transgenic mice than in wild-type mice.
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Unno,N., Sakaguchi,T., Nakamura,T., Yamamoto,N., Sugatani,J.,
            Miwa,M. and Konno,H.
  TITLE     A single nucleotide polymorphism in the plasma PAF acetylhydrolase
            gene and risk of atherosclerosis in Japanese patients with
            peripheral artery occlusive disease
  JOURNAL   J Surg Res 134 (1), 36-43 (2006)
   PUBMED   16650870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Marques,M., Pei,Y., Southall,M.D., Johnston,J.M., Arai,H., Aoki,J.,
            Inoue,T., Seltmann,H., Zouboulis,C.C. and Travers,J.B.
  TITLE     Identification of platelet-activating factor acetylhydrolase II in
            human skin
  JOURNAL   J Invest Dermatol 119 (4), 913-919 (2002)
   PUBMED   12406338
  REMARK    GeneRIF: presence of platelet-activating factor acetylhydrolase II
            in a restricted pattern in human skin; it is involved in protecting
            this organ against oxidative stress through the degradation of
            oxidatively modified bioactive phospholipids.
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Min,J.H., Wilder,C., Aoki,J., Arai,H., Inoue,K., Paul,L. and
            Gelb,M.H.
  TITLE     Platelet-activating factor acetylhydrolases: broad substrate
            specificity and lipoprotein binding does not modulate the catalytic
            properties of the plasma enzyme
  JOURNAL   Biochemistry 40 (15), 4539-4549 (2001)
   PUBMED   11294621
  REMARK    GeneRIF: examines substrate specificity for intracellular and
            plasma PAF-AHs
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Rice,S.Q., Southan,C., Boyd,H.F., Terrett,J.A., MacPhee,C.H.,
            Moores,K., Gloger,I.S. and Tew,D.G.
  TITLE     Expression, purification and characterization of a human
            serine-dependent phospholipase A2 with high specificity for
            oxidized phospholipids and platelet activating factor
  JOURNAL   Biochem J 330 (Pt 3) (Pt 3), 1309-1315 (1998)
   PUBMED   9494101
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Stafforini,D.M., McIntyre,T.M., Zimmerman,G.A. and Prescott,S.M.
  TITLE     Platelet-activating factor acetylhydrolases
  JOURNAL   J Biol Chem 272 (29), 17895-17898 (1997)
   PUBMED   9218411
  REMARK    Review article
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Hattori,K., Adachi,H., Matsuzawa,A., Yamamoto,K., Tsujimoto,M.,
            Aoki,J., Hattori,M., Arai,H. and Inoue,K.
  TITLE     cDNA cloning and expression of intracellular platelet-activating
            factor (PAF) acetylhydrolase II. Its homology with plasma PAF
            acetylhydrolase
  JOURNAL   J Biol Chem 271 (51), 33032-33038 (1996)
   PUBMED   8955149
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D87845.1, U89386.1, BC001158.1,
            BU630496.1 and AL592064.14.
            
            On May 7, 1999 this sequence version replaced NP_000428.1.
            
            Summary: This gene encodes platelet-activating factor
            acetylhydrolase isoform 2, a single-subunit intracellular enzyme
            that catalyzes the removal of the acetyl group at the SN-2 position
            of platelet-activating factor (identified as
            1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine). However, this
            lipase exhibits a broader substrate specificity than simply
            platelet activating factor. Two other isoforms of intracellular
            platelet-activating factor acetylhydrolase exist, and both are
            multi-subunit enzymes. Additionally, there is a single-subunit
            serum isoform of this enzyme. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.67248.1,
                                           SRR1163657.101110.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374282.8/ ENSP00000363400.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..392
                     /product="platelet-activating factor acetylhydrolase 2,
                     cytoplasmic"
                     /EC_number="3.1.1.47"
                     /EC_number="2.3.1.149"
                     /note="SD-PLA2; serine-dependent phospholipase A2;
                     platelet-activating factor acetylhydrolase 2, 40kDa;
                     PAF:sphingosine transacetylase; PAF:lysophospholipid
                     transacetylase; platelet-activating factor
                     acetyltransferase PAFAH2"
                     /calculated_mol_wt=43905
     Region          1..381
                     /region_name="PAF-AH_p_II"
                     /note="Platelet-activating factor acetylhydrolase, isoform
                     II; pfam03403"
                     /db_xref="CDD:397462"
     CDS             1..392
                     /gene="PAFAH2"
                     /gene_synonym="HSD-PLA2"
                     /coded_by="NM_000437.4:87..1265"
                     /db_xref="CCDS:CCDS270.1"
                     /db_xref="GeneID:5051"
                     /db_xref="HGNC:HGNC:8579"
                     /db_xref="MIM:602344"
ORIGIN      
        1 mgvnqsvgfp pvtgphlvgc gdvmegqnlq gsffrlfypc qkaeetmeqp lwipryeyct
       61 glaeylqfnk rcggllfnla vgscrlpvsw ngpfktkdsg ypliifshgl gafrtlysaf
      121 cmelasrgfv vavpehrdrs aattyfckqa peenqptnes lqeewipfrr veegekefhv
      181 rnpqvhqrvs eclrvlkilq evtagqtvfn ilpggldlmt lkgnidmsrv avmghsfgga
      241 tailalaket qfrcavalda wmfplerdfy pkargpvffi ntekfqtmes vnlmkkicaq
      301 heqsriitvl gsvhrsqtdf afvtgnligk ffstetrgsl dpyegqevmv ramlaflqkh
      361 ldlkedynqw nnliegigps ltpgaphhls sl
//
LOCUS       NP_001354467             418 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 31 [Homo sapiens].
ACCESSION   NP_001354467
VERSION     NP_001354467.1
DBSOURCE    REFSEQ: accession NM_001367538.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 418)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 418)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 418)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22 and AC022400.9.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..418
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 31"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=46399
     Region          <11..199
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          259..>314
                     /region_name="NTF2_like"
                     /note="Nuclear transport factor 2 (NTF2-like) superfamily.
                     This family includes members of the NTF2 family,
                     Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases,
                     and the beta subunit of Ring hydroxylating dioxygenases.
                     This family is a classic example of...; cl09109"
                     /db_xref="CDD:471850"
     CDS             1..418
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367538.1:286..1542"
                     /note="isoform 31 is encoded by transcript variant 31"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mstsetskhr hcihqilesv nhihqhdivh rdlkpenlll askckgaavk ladfglaiev
       61 qgeqqawfgf agtpgylspe vlrkdpygkp vdiwacgvil yillvgyppf wdedqhklyq
      121 qikagaydfp spewdtvtpe aknlinqmlt inpakritad qalkhpwvcq rstvasmmhr
      181 qetveclrkf narrklkgai lttmlvsrnf saaksllnkk sdggvkepqt tvvhnatdgi
      241 kgstescntt tededlkvrk qeiikiteql ieainngdfe aytkicdpgl tsfepealgn
      301 lvegmdfhkf yfenrewvra adillpaplp lclcllltfs sqlptfplfd lraalllcml
      361 vplcpdgcrq aplkalllss kchsfcscfv avpvttiklt yflpgavaya cnpntlgg
//
LOCUS       NP_003667                323 aa            linear   PRI 27-APR-2025
DEFINITION  sphingolipid delta(4)-desaturase DES1 isoform 1 [Homo sapiens].
ACCESSION   NP_003667
VERSION     NP_003667.1
DBSOURCE    REFSEQ: accession NM_003676.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Dei Cas,M., Montavoci,L., Pasini,C., Caretti,A., Penati,S.,
            Martinelli,C., Gianelli,U., Casati,S., Nardecchia,F., Torella,A.,
            Brunetti-Pierri,N. and Trinchera,M.
  TITLE     Loss of function and reduced levels of sphingolipid desaturase
            DEGS1 variants are both relevant in disease mechanism
  JOURNAL   J Lipid Res 65 (3), 100517 (2024)
   PUBMED   38342436
  REMARK    GeneRIF: Loss of function and reduced levels of sphingolipid
            desaturase DEGS1 variants are both relevant in disease mechanism.
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Hulsmeier,A.J., Toelle,S.P., Bellstedt,P., Wentzel,C., Bahr,A.,
            Kolokotronis,K. and Hornemann,T.
  TITLE     The atypical sphingolipid SPB 18:1(14Z);O2 is a biomarker for DEGS1
            related hypomyelinating leukodystrophy
  JOURNAL   J Lipid Res 64 (12), 100464 (2023)
   PUBMED   37890668
  REMARK    GeneRIF: The atypical sphingolipid SPB 18:1(14Z);O2 is a biomarker
            for DEGS1 related hypomyelinating leukodystrophy.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Planas-Serra,L., Launay,N., Goicoechea,L., Heron,B., Jou,C.,
            Julia-Palacios,N., Ruiz,M., Fourcade,S., Casasnovas,C., De La
            Torre,C., Gelot,A., Marsal,M., Loza-Alvarez,P., Garcia-Cazorla,A.,
            Fatemi,A., Ferrer,I., Portero-Otin,M., Area-Gomez,E. and Pujol,A.
  TITLE     Sphingolipid desaturase DEGS1 is essential for
            mitochondria-associated membrane integrity
  JOURNAL   J Clin Invest 133 (10), e162957 (2023)
   PUBMED   36951944
  REMARK    GeneRIF: Sphingolipid desaturase DEGS1 is essential for
            mitochondria-associated membrane integrity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Hayashi,Y., Matsuda,K., Tanigawa,K., Tanikawa,T., Maeda,K. and
            Tsuchiya,K.
  TITLE     Dihydroceramide Delta4-Desaturase 1 Is Not Involved in SARS-CoV-2
            Infection
  JOURNAL   Biol Pharm Bull 45 (10), 1559-1563 (2022)
   PUBMED   36184516
  REMARK    GeneRIF: Dihydroceramide Delta4-Desaturase 1 Is Not Involved in
            SARS-CoV-2 Infection.
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Spassieva,S.D., Rahmaniyan,M., Bielawski,J., Clarke,C.J.,
            Kraveka,J.M. and Obeid,L.M.
  TITLE     Cell density-dependent reduction of dihydroceramide desaturase
            activity in neuroblastoma cells
  JOURNAL   J Lipid Res 53 (5), 918-928 (2012)
   PUBMED   22377532
  REMARK    GeneRIF: a role of the sphingolipid pathway, dihydroceramides
            desaturase in particular, in confluence-induced growth arrest in
            neuroblastoma cells
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Devlin,C.M., Lahm,T., Hubbard,W.C., Van Demark,M., Wang,K.C.,
            Wu,X., Bielawska,A., Obeid,L.M., Ivan,M. and Petrache,I.
  TITLE     Dihydroceramide-based response to hypoxia
  JOURNAL   J Biol Chem 286 (44), 38069-38078 (2011)
   PUBMED   21914808
  REMARK    GeneRIF: overexpression of DEGS1 or DEGS2 attenuates the DHC
            accumulation and increased cell proliferation during hypoxia
            Erratum:[J Biol Chem. 2012 May 18;287(21):17425]
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Idkowiak-Baldys,J., Apraiz,A., Li,L., Rahmaniyan,M., Clarke,C.J.,
            Kraveka,J.M., Asumendi,A. and Hannun,Y.A.
  TITLE     Dihydroceramide desaturase activity is modulated by oxidative
            stress
  JOURNAL   Biochem J 427 (2), 265-274 (2010)
   PUBMED   20105137
  REMARK    GeneRIF: oxidative stress leads to potent inhibition of
            dihydroceramide desaturase resulting in significant elevation in
            dihydroceramide levels in vivo
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Kraveka,J.M., Li,L., Szulc,Z.M., Bielawski,J., Ogretmen,B.,
            Hannun,Y.A., Obeid,L.M. and Bielawska,A.
  TITLE     Involvement of dihydroceramide desaturase in cell cycle progression
            in human neuroblastoma cells
  JOURNAL   J Biol Chem 282 (23), 16718-16728 (2007)
   PUBMED   17283068
  REMARK    GeneRIF: partial loss of DEGS-1 inhibited cell growth, with cell
            cycle arrest at G(0)/G(1). This was accompanied by a significant
            decrease in the amount of phosphorylated retinoblastoma protein
REFERENCE   9  (residues 1 to 323)
  AUTHORS   Ternes,P., Franke,S., Zahringer,U., Sperling,P. and Heinz,E.
  TITLE     Identification and characterization of a sphingolipid delta
            4-desaturase family
  JOURNAL   J Biol Chem 277 (28), 25512-25518 (2002)
   PUBMED   11937514
  REMARK    GeneRIF: identification of sphingolipid delta 4-desaturase family
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Cadena,D.L., Kurten,R.C. and Gill,G.N.
  TITLE     The product of the MLD gene is a member of the membrane fatty acid
            desaturase family: overexpression of MLD inhibits EGF receptor
            biosynthesis
  JOURNAL   Biochemistry 36 (23), 6960-6967 (1997)
   PUBMED   9188692
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000961.2 and AY423730.1.
            
            Summary: This gene encodes a member of the membrane fatty acid
            desaturase family which is responsible for inserting double bonds
            into specific positions in fatty acids. This protein contains three
            His-containing consensus motifs that are characteristic of a group
            of membrane fatty acid desaturases. It is predicted to be a
            multiple membrane-spanning protein localized to the endoplasmic
            reticulum. Overexpression of this gene inhibited biosynthesis of
            the EGF receptor, suggesting a possible role of a fatty acid
            desaturase in regulating biosynthetic processing of the EGF
            receptor. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000961.2, SRR3476690.245725.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323699.9/ ENSP00000316476.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.11"
     Protein         1..323
                     /product="sphingolipid delta(4)-desaturase DES1 isoform 1"
                     /EC_number="1.14.19.17"
                     /note="membrane fatty acid (lipid) desaturase;
                     sphingolipid delta 4 desaturase; migration-inducing gene
                     15 protein; membrane lipid desaturase; cell
                     migration-inducing gene 15 protein; degenerative
                     spermatocyte homolog 1, lipid desaturase; sphingolipid
                     delta(4)-desaturase 1; dihydroceramide desaturase 1;
                     degenerative spermatocyte homolog, lipid desaturase;
                     retinol isomerase"
                     /calculated_mol_wt=37735
     Region          6..42
                     /region_name="Lipid_DES"
                     /note="Sphingolipid Delta4-desaturase (DES); pfam08557"
                     /db_xref="CDD:462517"
     Region          26..315
                     /region_name="Delta4-sphingolipid-FADS-like"
                     /note="The Delta4-sphingolipid Fatty Acid Desaturase
                     (Delta4-sphingolipid-FADS)-like CD includes the
                     integral-membrane enzymes, dihydroceramide Delta-4
                     desaturase, involved in the synthesis of sphingosine; and
                     the human membrane fatty acid (lipid) desaturase...;
                     cd03508"
                     /db_xref="CDD:239585"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            order(89,93,128,131..132,259,262..263)
                     /site_type="other"
                     /note="putative di-iron ligands [ion binding]"
                     /db_xref="CDD:239585"
     Region          89..93
                     /region_name="Histidine box-1. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            102..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Region          128..132
                     /region_name="Histidine box-2. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            152..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            209..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Region          259..263
                     /region_name="Histidine box-3. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15121.1)"
     CDS             1..323
                     /gene="DEGS1"
                     /gene_synonym="DEGS; DEGS-1; Des-1; DES1; FADS7; HLD18;
                     MIG15; MLD"
                     /coded_by="NM_003676.4:98..1069"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1540.1"
                     /db_xref="GeneID:8560"
                     /db_xref="HGNC:HGNC:13709"
                     /db_xref="MIM:615843"
ORIGIN      
        1 mgsrvsredf ewvytdqpha drrreilaky peikslmkpd pnliwiiimm vltqlgafyi
       61 vkdldwkwvi fgayafgsci nhsmtlaihe iahnaafgnc kamwnrwfgm fanlpigipy
      121 sisfkryhmd hhrylgadgv dvdiptdfeg wffctafrkf iwvilqplfy afrplfinpk
      181 pitylevint vaqvtfdili yyflgikslv ymlaasllgl glhpisghfi aehymflkgh
      241 etysyygpln lltfnvgyhn ehhdfpnipg kslplvrkia aeyydnlphy nswikvlydf
      301 vmddtispys rmkrhqkgem vle
//
LOCUS       NP_063937                483 aa            linear   PRI 27-APR-2025
DEFINITION  glycogen synthase kinase-3 alpha [Homo sapiens].
ACCESSION   NP_063937
VERSION     NP_063937.2
DBSOURCE    REFSEQ: accession NM_019884.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Zheng,X., Yang,L., Shen,X., Pan,J., Chen,Y., Chen,J., Wang,H.,
            Meng,J., Chen,Z., Xie,S., Li,Y., Zhu,B., Zhu,W., Qin,L. and Lu,L.
  TITLE     Targeting Gsk3a reverses immune evasion to enhance immunotherapy in
            hepatocellular carcinoma
  JOURNAL   J Immunother Cancer 12 (8), e009642 (2024)
   PUBMED   39174053
  REMARK    GeneRIF: Targeting Gsk3a reverses immune evasion to enhance
            immunotherapy in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Zhao,J., Wei,M., Guo,M., Wang,M., Niu,H., Xu,T. and Zhou,Y.
  TITLE     GSK3: A potential target and pending issues for treatment of
            Alzheimer's disease
  JOURNAL   CNS Neurosci Ther 30 (7), e14818 (2024)
   PUBMED   38946682
  REMARK    GeneRIF: GSK3: A potential target and pending issues for treatment
            of Alzheimer's disease.
            Review article
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Umbarkar,P., Ejantkar,S., Ruiz Ramirez,S.Y., Toro Cora,A.,
            Zhang,Q., Tousif,S. and Lal,H.
  TITLE     Cardiac fibroblast GSK-3alpha aggravates ischemic cardiac injury by
            promoting fibrosis, inflammation, and impairing angiogenesis
  JOURNAL   Basic Res Cardiol 118 (1), 35 (2023)
   PUBMED   37656238
  REMARK    GeneRIF: Cardiac fibroblast GSK-3alpha aggravates ischemic cardiac
            injury by promoting fibrosis, inflammation, and impairing
            angiogenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Loxha,L., Ibrahim,N.K., Stasche,A.S., Cinar,B., Dolgner,T.,
            Niessen,J., Schreek,S., Fehlhaber,B., Forster,M., Stanulla,M. and
            Hinze,L.
  TITLE     GSK3alpha Regulates Temporally Dynamic Changes in Ribosomal
            Proteins upon Amino Acid Starvation in Cancer Cells
  JOURNAL   Int J Mol Sci 24 (17), 13260 (2023)
   PUBMED   37686063
  REMARK    GeneRIF: GSK3alpha Regulates Temporally Dynamic Changes in
            Ribosomal Proteins upon Amino Acid Starvation in Cancer Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Park,D.S., Nguyen,S.C., Isenhart,R., Shah,P.P., Kim,W.,
            Barnett,R.J., Chandra,A., Luppino,J.M., Harke,J., Wai,M.,
            Walsh,P.J., Abdill,R.J., Yang,R., Lan,Y., Yoon,S., Yunker,R.,
            Kanemaki,M.T., Vahedi,G., Phillips-Cremins,J.E., Jain,R. and
            Joyce,E.F.
  TITLE     High-throughput Oligopaint screen identifies druggable 3D genome
            regulators
  JOURNAL   Nature 620 (7972), 209-217 (2023)
   PUBMED   37438531
  REMARK    GeneRIF: High-throughput Oligopaint screen identifies druggable 3D
            genome regulators.
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Hart,M.J., de los Santos,R., Albert,I.N., Rubinfeld,B. and
            Polakis,P.
  TITLE     Downregulation of beta-catenin by human Axin and its association
            with the APC tumor suppressor, beta-catenin and GSK3 beta
  JOURNAL   Curr Biol 8 (10), 573-581 (1998)
   PUBMED   9601641
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Harr,S.D., Hollister,R.D. and Hyman,B.T.
  TITLE     Glycogen synthase kinase 3 alpha and 3 beta do not colocalize with
            neurofibrillary tangles
  JOURNAL   Neurobiol Aging 17 (3), 343-348 (1996)
   PUBMED   8725894
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Cross,D.A., Alessi,D.R., Cohen,P., Andjelkovich,M. and
            Hemmings,B.A.
  TITLE     Inhibition of glycogen synthase kinase-3 by insulin mediated by
            protein kinase B
  JOURNAL   Nature 378 (6559), 785-789 (1995)
   PUBMED   8524413
REFERENCE   9  (residues 1 to 483)
  AUTHORS   He,X., Saint-Jeannet,J.P., Woodgett,J.R., Varmus,H.E. and
            Dawid,I.B.
  TITLE     Glycogen synthase kinase-3 and dorsoventral patterning in Xenopus
            embryos
  JOURNAL   Nature 374 (6523), 617-622 (1995)
   PUBMED   7715701
  REMARK    Erratum:[Nature 1995 May 18;375(6528):253]
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Yang,S.D., Yu,J.S., Shiah,S.G. and Huang,J.J.
  TITLE     Protein kinase FA/glycogen synthase kinase-3 alpha after heparin
            potentiation phosphorylates tau on sites abnormally phosphorylated
            in Alzheimer's disease brain
  JOURNAL   J Neurochem 63 (4), 1416-1425 (1994)
   PUBMED   7931292
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006486.1, BC027984.1, L40027.1 and D63424.1.
            
            On Jul 1, 2004 this sequence version replaced NP_063937.1.
            
            Summary: This gene encodes a multifunctional Ser/Thr protein kinase
            that is implicated in the control of several regulatory proteins
            including glycogen synthase, and transcription factors, such as
            JUN. It also plays a role in the WNT and PI3K signaling pathways,
            as well as regulates the production of beta-amyloid peptides
            associated with Alzheimer's disease. [provided by RefSeq, Oct
            2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC027984.1, L40027.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222330.8/ ENSP00000222330.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..483
                     /product="glycogen synthase kinase-3 alpha"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.11.26"
                     /note="GSK-3 alpha; serine/threonine-protein kinase GSK3A"
                     /calculated_mol_wt=50850
     Region          1..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49840.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P49840.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P49840.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000250|UniProtKB:Q2NL51; propagated from
                     UniProtKB/Swiss-Prot (P49840.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P49840.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P49840.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P49840.2)"
     Region          114..406
                     /region_name="STKc_GSK3"
                     /note="The catalytic domain of the Serine/Threonine
                     Kinase, Glycogen Synthase Kinase 3; cd14137"
                     /db_xref="CDD:271039"
     Site            order(125..129,133,146,148,159,173,195..198,201,203..204,
                     244,246,248..249,251,263,266,277,279..282,284,322)
                     /site_type="active"
                     /db_xref="CDD:271039"
     Site            order(125..128,133,146,148,173,195..198,201,246,248..249,
                     251,263)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271039"
     Site            order(129..130,275..283,291..292,323..327,329..330,334,
                     354..357)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271039"
     Site            order(159,203,244,246,266,277,279..282,284,322)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271039"
     Site            order(262..272,274..284)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271039"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P18265; propagated from
                     UniProtKB/Swiss-Prot (P49840.2)"
     Site            order(291,326..327,329..330,333..334,354..359)
                     /site_type="other"
                     /note="axin binding site [polypeptide binding]"
                     /db_xref="CDD:271039"
     Region          449..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49840.2)"
     CDS             1..483
                     /gene="GSK3A"
                     /coded_by="NM_019884.3:138..1589"
                     /db_xref="CCDS:CCDS12599.1"
                     /db_xref="GeneID:2931"
                     /db_xref="HGNC:HGNC:4616"
                     /db_xref="MIM:606784"
ORIGIN      
        1 msgggpsggg pggsgrarts sfaepggggg gggggpggsa sgpggtgggk asvgamgggv
       61 gasssgggpg gsggggsggp gagtsfpppg vklgrdsgkv ttvvatlgqg persqevayt
      121 dikvigngsf gvvyqarlae trelvaikkv lqdkrfknre lqimrkldhc nivrlryffy
      181 ssgekkdely lnlvleyvpe tvyrvarhft kakltipily vkvymyqlfr slayihsqgv
      241 chrdikpqnl lvdpdtavlk lcdfgsakql vrgepnvsyi csryyrapel ifgatdytss
      301 idvwsagcvl aelllgqpif pgdsgvdqlv eiikvlgtpt reqiremnpn ytefkfpqik
      361 ahpwtkvfks rtppeaialc sslleytpss rlspleacah sffdelrclg tqlpnnrplp
      421 plfnfsagel siqpslnail ipphlrspag tttltpssqa ltetptssdw qstdatptlt
      481 nss
//
LOCUS       NP_056298                623 aa            linear   PRI 27-APR-2025
DEFINITION  kelch repeat and BTB domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_056298 XP_291224 XP_374418
VERSION     NP_056298.2
DBSOURCE    REFSEQ: accession NM_015483.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Hu,Y., Zhang,Z., Mao,Q., Zhang,X., Hao,A., Xun,Y., Wang,Y., Han,L.,
            Zhan,W., Liu,Q., Yin,Y., Peng,C., Moresco,E.M.Y., Chen,Z.,
            Beutler,B. and Sun,L.
  TITLE     Dynamic molecular architecture and substrate recruitment of
            cullin3-RING E3 ligase CRL3KBTBD2
  JOURNAL   Nat Struct Mol Biol 31 (2), 336-350 (2024)
   PUBMED   38332366
  REMARK    GeneRIF: Dynamic molecular architecture and substrate recruitment
            of cullin3-RING E3 ligase CRL3[KBTBD2].
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Zhang,Z., Turer,E., Li,X., Zhan,X., Choi,M., Tang,M., Press,A.,
            Smith,S.R., Divoux,A., Moresco,E.M. and Beutler,B.
  TITLE     Insulin resistance and diabetes caused by genetic or diet-induced
            KBTBD2 deficiency in mice
  JOURNAL   Proc Natl Acad Sci U S A 113 (42), E6418-E6426 (2016)
   PUBMED   27708159
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018648.5 and BC037887.2.
            
            On Feb 12, 2009 this sequence version replaced NP_056298.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037887.2, SRR1660805.199725.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405, SAMN03267754
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304056.9/ ENSP00000302586.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..623
                     /product="kelch repeat and BTB domain-containing protein
                     2"
                     /note="BTB and kelch domain containing 1; BTB and kelch
                     domain-containing protein 1; kelch repeat and BTB (POZ)
                     domain containing 2"
                     /calculated_mol_wt=71200
     Region          5..137
                     /region_name="BTB_POZ_KBTBD2_BKLHD1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch repeat
                     and BTB domain-containing protein 2 (KBTBD2); cd18270"
                     /db_xref="CDD:349579"
     Region          23..516
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          128..223
                     /region_name="BACK_KBTBD2"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch repeat and BTB domain-containing protein 2 (KBTBD2);
                     cd18479"
                     /db_xref="CDD:350554"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8IY47.2)"
     Region          310..366
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          317..380
                     /region_name="Kelch 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY47.2)"
     Region          370..416
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          381..429
                     /region_name="Kelch 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY47.2)"
     Region          419..453
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          431..469
                     /region_name="Kelch 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY47.2)"
     Region          459..516
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          470..529
                     /region_name="Kelch 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY47.2)"
     Region          519..568
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          535..581
                     /region_name="Kelch 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY47.2)"
     CDS             1..623
                     /gene="KBTBD2"
                     /gene_synonym="BKLHD1"
                     /coded_by="NM_015483.3:564..2435"
                     /db_xref="CCDS:CCDS34614.1"
                     /db_xref="GeneID:25948"
                     /db_xref="HGNC:HGNC:21751"
                     /db_xref="MIM:619393"
ORIGIN      
        1 mstqderqin teyavslleq lklfyeqqlf tdivlivegt efpchkmvla tcssyframf
       61 msglseskqt hvhlrnvdaa tlqiiityay tgnlamndst veqlyetacf lqvedvlqrc
      121 reylikkina encvrllsfa dlfsceelkq sakrmvehkf tavyhqdafm qlshdllidi
      181 lssdnlnvek eetvreaaml wleyntesrs qylssvlsqi ridalsevtq rawfqglppn
      241 dksvvvqgly ksmpkffkpr lgmtkeemmi fieassenpc slyssvcysp qaekvyklcs
      301 ppadlhkvgt vvtpdndiyi aggqvplknt ktnhsktskl qtafrtvncf ywfdaqqntw
      361 fpktpmlfvr ikpslvcceg yiyaiggdsv ggelnrrtve rydtekdewt mvsplpcawq
      421 wsaavvvhdc iyvmtlnlmy cyfprsdswv emamrqtsrs fasaaafgdk ifyigglhia
      481 tnsgirlpsg tvdgssvtve iydvnknewk maanipakry sdpcvravvi snslcvfmre
      541 thlnerakyv tyqydleldr wslrqhiser vlwdlgrdfr ctvgklypsc leespwkppt
      601 ylfstdgtee feldgemval ppv
//
LOCUS       NP_001350894             250 aa            linear   PRI 27-APR-2025
DEFINITION  rab-like protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001350894 XP_016861716
VERSION     NP_001350894.1
DBSOURCE    REFSEQ: accession NM_001363965.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Ma,Y., Ren,Y., Wen,H. and Cui,C.
  TITLE     circCOL1A1 Promotes the Progression of Gastric Cancer Cells through
            Sponging miR-145 to Enhance RABL3 Expression
  JOURNAL   J Immunol Res 2021, 6724854 (2021)
   PUBMED   34631898
  REMARK    GeneRIF: circCOL1A1 Promotes the Progression of Gastric Cancer
            Cells through Sponging miR-145 to Enhance RABL3 Expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Roberts,N.J., Grant,R.C., Gallinger,S. and Klein,A.P.
  CONSRTM   Familial Pancreatic Cancer Genome Sequencing Project
  TITLE     Germline sequence analysis of RABL3 in a large series of pancreatic
            ductal adenocarcinoma patients reveals no evidence of deleterious
            variants
  JOURNAL   Genes Chromosomes Cancer 60 (8), 559-564 (2021)
   PUBMED   33724601
  REMARK    GeneRIF: Germline sequence analysis of RABL3 in a large series of
            pancreatic ductal adenocarcinoma patients reveals no evidence of
            deleterious variants.
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Xu,Z., Li,H., Lin,C., Zeng,B., Chen,Y. and Luo,Y.
  TITLE     Knockdown of RABL3 suppresses the proliferation and invasion of
            oral squamous cell carcinoma through inactivating the FAK/AKT
            pathway
  JOURNAL   J Bioenerg Biomembr 53 (2), 203-211 (2021)
   PUBMED   33438143
  REMARK    GeneRIF: Knockdown of RABL3 suppresses the proliferation and
            invasion of oral squamous cell carcinoma through inactivating the
            FAK/AKT pathway.
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Puzzono,M., Crippa,S., Zuppardo,R.A., Zapparoli,E., Falconi,M. and
            Cavestro,G.M.
  TITLE     Low-frequency of RABL3 pathogenetic variants in hereditary and
            familial pancreatic cancer
  JOURNAL   Dig Liver Dis 53 (4), 519-521 (2021)
   PUBMED   33353859
  REMARK    GeneRIF: Low-frequency of RABL3 pathogenetic variants in hereditary
            and familial pancreatic cancer.
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Qi,W.Y., Mao,X.B., He,Y.B. and Xiao,C.H.
  TITLE     Long non-coding RNA LINC00858 promotes cells proliferation and
            invasion through the miR-153-3p/Rabl3 axis in hepatocellular
            carcinoma
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (18), 9343-9352 (2020)
   PUBMED   33015775
  REMARK    GeneRIF: Long non-coding RNA LINC00858 promotes cells proliferation
            and invasion through the miR-153-3p/Rabl3 axis in hepatocellular
            carcinoma.
REFERENCE   6  (residues 1 to 250)
  AUTHORS   An,J., Liu,Z., Liang,Q., Pan,Y., Li,H., Wang,R. and Jin,Y.
  TITLE     Overexpression of Rabl3 and Cullin7 is associated with pathogenesis
            and poor prognosis in hepatocellular carcinoma
  JOURNAL   Hum Pathol 67, 146-151 (2017)
   PUBMED   28739496
  REMARK    GeneRIF: Hepatocellular carcinoma patients with positive expression
            for both Rabl3 and Cullin7 had a remarkably shorter survival time
            compared with patients with negative expression for both proteins.
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Pan,Y., Liu,Z., Feng,Z., Hui,D., Huang,X., Tong,D. and Jin,Y.
  TITLE     The overexpression of Rabl3 is associated with pathogenesis and
            clinicopathologic variables in hepatocellular carcinoma
  JOURNAL   Tumour Biol 39 (4), 1010428317696230 (2017)
   PUBMED   28443498
  REMARK    GeneRIF: Our studies suggest that the Rabl3 is a valuable marker of
            hepatocellular carcinoma progression and that the overexpression of
            Rabl3 plays an important role in the development and pathogenesis
            of hepatocellular carcinoma.
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Zhang,W., Sun,J. and Luo,J.
  TITLE     High Expression of Rab-like 3 (Rabl3) is Associated with Poor
            Survival of Patients with Non-Small Cell Lung Cancer via Repression
            of MAPK8/9/10-Mediated Autophagy
  JOURNAL   Med Sci Monit 22, 1582-1588 (2016)
   PUBMED   27164297
  REMARK    GeneRIF: We examine the correlation between the expression level of
            Rabl3 and survival of non-small cell lung cancer (NSCLC) patients
            in three independent cohorts containing 484 patients. We found high
            expression of Rabl3 might inhibit cell death in non-small cell lung
            cancer via repression of MAPK8/9/10-mediated autophagy
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   10 (residues 1 to 250)
  AUTHORS   Li,Q., Wang,L., Zeng,L., Zhang,Y., Li,K., Jin,P., Su,B. and Wang,L.
  TITLE     Evaluation of the novel gene Rabl3 in the regulation of
            proliferation and motility in human cancer cells
  JOURNAL   Oncol Rep 24 (2), 433-440 (2010)
   PUBMED   20596630
  REMARK    GeneRIF: Rabl3 can be considered as a novel candidate in the
            control of tumorigenesis and as a new target for anticancer
            treatment.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC117472.3 and AC133474.2.
            
            On Jun 3, 2018 this sequence version replaced XP_016861716.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.257621.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.33"
     Protein         1..250
                     /product="rab-like protein 3 isoform 1"
                     /note="rab-like protein 3"
                     /calculated_mol_wt=28018
     Region          7..210
                     /region_name="RabL3"
                     /note="Rab GTPase-like family 3 (Rab-like3); cd04102"
                     /db_xref="CDD:206689"
     Site            13..20
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206689"
     Site            order(15..21,37..38,69,147..148,150,182)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206689"
     Site            order(37..39,42..45)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206689"
     Site            38
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206689"
     Site            order(39,42..43,63,65,89)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206689"
     Site            order(39,42,65..66)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206689"
     Site            order(42..47,61)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206689"
     Site            66..69
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206689"
     Site            69
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206689"
     Site            147..150
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206689"
     Site            182..184
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206689"
     CDS             1..250
                     /gene="RABL3"
                     /gene_synonym="PNCA5"
                     /coded_by="NM_001363965.1:174..926"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:285282"
                     /db_xref="HGNC:HGNC:18072"
                     /db_xref="MIM:618542"
ORIGIN      
        1 masldrvkvl vlgdsgvgks slvhllcqnq vlgnpswtvg csvdvrvhdy kegtpeekty
       61 yielwdvggs vgsassvkst ravfynsvng iifvhdltnk kssqnlrrws lealnrdlvp
      121 tgvlvtngdy dqeqfadnqi pllvigtkld qihetkrhev ltrtaflaed fnpeeinldc
      181 tnprylaags snavklsrff dkviekryfl regnqmtlsp icwemfsiwi pgfpdrkrfg
      241 agtlkslhyd
//
LOCUS       NP_004301                191 aa            linear   PRI 27-APR-2025
DEFINITION  rho-related GTP-binding protein RhoH precursor [Homo sapiens].
ACCESSION   NP_004301
VERSION     NP_004301.1
DBSOURCE    REFSEQ: accession NM_004310.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   He,J., Tang,J., Feng,Q., Li,T., Wu,K., Yang,K., Jia,D. and Xia,Q.
  TITLE     Weighted gene co-expression network analysis identifies RHOH and
            TRAF1 as key candidate genes for psoriatic arthritis
  JOURNAL   Clin Rheumatol 40 (4), 1381-1391 (2021)
   PUBMED   32959187
  REMARK    GeneRIF: Weighted gene co-expression network analysis identifies
            RHOH and TRAF1 as key candidate genes for psoriatic arthritis.
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Ni,J., Shi,Q.Q., Wu,W., Sun,X., Fang,Y.Z. and Gu,J.
  TITLE     [Expression Difference of RhoH Gene in Leukemia and Its Clinical
            Significance]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 27 (3), 758-762 (2019)
   PUBMED   31204928
  REMARK    GeneRIF: In AML, RhoH expression negatively correlates with
            recurrence rate, which can be used as a prognostic indicator
            independently
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Tajadura-Ortega,V., Garg,R., Allen,R., Owczarek,C., Bright,M.D.,
            Kean,S., Mohd-Noor,A., Grigoriadis,A., Elston,T.C., Hahn,K.M. and
            Ridley,A.J.
  TITLE     An RNAi screen of Rho signalling networks identifies RhoH as a
            regulator of Rac1 in prostate cancer cell migration
  JOURNAL   BMC Biol 16 (1), 29 (2018)
   PUBMED   29510700
  REMARK    GeneRIF: RhoH promotes prostate cancer cell migration and RhoH
            expression levels correlate with prostate cancer progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Lahousse,S., Smorowski,A.L., Denis,C., Lantoine,D., Kerckaert,J.P.
            and Galiegue-Zouitina,S.
  TITLE     Structural features of hematopoiesis-specific RhoH/ARHH gene: high
            diversity of 5'-UTR in different hematopoietic lineages suggests a
            complex post-transcriptional regulation
  JOURNAL   Gene 343 (1), 55-68 (2004)
   PUBMED   15563831
  REMARK    GeneRIF: 5' end heterogeneity of RhoH mRNAs was observed, due to
            alternative splicing of some 5' exons and to the use of these
            different transcription start sites.
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Faure,J. and Dagher,M.C.
  TITLE     Interactions between Rho GTPases and Rho GDP dissociation inhibitor
            (Rho-GDI)
  JOURNAL   Biochimie 83 (5), 409-414 (2001)
   PUBMED   11368848
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Yousefi,S., Cooper,P.R., Mueck,B., Potter,S.L. and Jarai,G.
  TITLE     cDNA representational difference analysis of human neutrophils
            stimulated by GM-CSF
  JOURNAL   Biochem Biophys Res Commun 277 (2), 401-409 (2000)
   PUBMED   11032736
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Preudhomme,C., Roumier,C., Hildebrand,M.P., Dallery-Prudhomme,E.,
            Lantoine,D., Lai,J.L., Daudignon,A., Adenis,C., Bauters,F.,
            Fenaux,P., Kerckaert,J.P. and Galiegue-Zouitina,S.
  TITLE     Nonrandom 4p13 rearrangements of the RhoH/TTF gene, encoding a
            GTP-binding protein, in non-Hodgkin's lymphoma and multiple myeloma
  JOURNAL   Oncogene 19 (16), 2023-2032 (2000)
   PUBMED   10803463
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Dallery-Prudhomme,E., Roumier,C., Denis,C., Preudhomme,C.,
            Kerckaert,J.P. and Galiegue-Zouitina,S.
  TITLE     Genomic structure and assignment of the RhoH/TTF small GTPase gene
            (ARHH) to 4p13 by in situ hybridization
  JOURNAL   Genomics 43 (1), 89-94 (1997)
   PUBMED   9226377
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Dallery,E., Galiegue-Zouitina,S., Collyn-d'Hooghe,M., Quief,S.,
            Denis,C., Hildebrand,M.P., Lantoine,D., Deweindt,C., Tilly,H.,
            Bastard,C. et al.
  TITLE     TTF, a gene encoding a novel small G protein, fuses to the
            lymphoma-associated LAZ3 gene by t(3;4) chromosomal translocation
  JOURNAL   Oncogene 10 (11), 2171-2178 (1995)
   PUBMED   7784061
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA906265.1, BC014261.2,
            BX413967.2, AA767445.1 and AC095057.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the Ras
            superfamily of guanosine triphosphate (GTP)-metabolizing enzymes.
            The encoded protein is expressed in hematopoietic cells, where it
            functions as a negative regulator of cell growth and survival. This
            gene may be hypermutated or misexpressed in leukemias and
            lymphomas. Chromosomal translocations in non-Hodgkin's lymphoma
            occur between this locus and B-cell CLL/lymphoma 6 (BCL6) on
            chromosome 3, leading to the production of fusion transcripts.
            Alternative splicing in the 5' untranslated region results in
            multiple transcript variants that encode the same protein.
            [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (6) lacks an exon in the 5' UTR,
            compared to variant 1. Variants 1 through 12 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP271287.1, SRR1163657.341450.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381799.10/ ENSP00000371219.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..191
                     /product="rho-related GTP-binding protein RhoH precursor"
                     /note="rho-related GTP-binding protein RhoH; TTF,
                     translocation three four; GTP-binding protein TTF; ras
                     homolog gene family, member H"
                     /calculated_mol_wt=21199
     mat_peptide     1..188
                     /product="Rho-related GTP-binding protein RhoH.
                     /id=PRO_0000198867"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15669.1)"
                     /calculated_mol_wt=20942
     Region          5..169
                     /region_name="Rho"
                     /note="Ras homology family (Rho) of small guanosine
                     triphosphatases (GTPases); cd00157"
                     /db_xref="CDD:206641"
     Site            order(6,36..37,39..40,42,44,53,57..62,68,71)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206641"
     Site            11..18
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206641"
     Site            order(14..19,36,58..59,117,119,153..154)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206641"
     Region          33..41
                     /region_name="Effector region. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15669.1)"
     Site            order(35,37..38,62,68,71)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206641"
     Site            order(36..37,60,68,70..71)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206641"
     Site            36
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206641"
     Site            37..41
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206641"
     Site            order(38,68,71)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:206641"
     Site            58..61
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206641"
     Site            order(60..62,68..71,76..78)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206641"
     Region          73..86
                     /region_name="Interaction with ZAP70.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15669.1)"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206641"
     Site            152..154
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206641"
     Site            188
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q15669.1)"
     CDS             1..191
                     /gene="RHOH"
                     /gene_synonym="ARHH; IMD129; TTF"
                     /coded_by="NM_004310.5:601..1176"
                     /db_xref="CCDS:CCDS3458.1"
                     /db_xref="GeneID:399"
                     /db_xref="HGNC:HGNC:686"
                     /db_xref="MIM:602037"
ORIGIN      
        1 mlssikcvlv gdsavgktsl lvrftsetfp eaykptvyen tgvdvfmdgi qislglwdta
       61 gndafrsirp lsyqqadvvl mcysvanhns flnlknkwig eirsnlpctp vlvvatqtdq
      121 remgphrasc vnamegkkla qdvrakgyle csalsnrgvq qvfecavrta vnqarrrnrr
      181 rlfsinecki f
//
LOCUS       NP_065109                504 aa            linear   PRI 27-APR-2025
DEFINITION  patatin-like phospholipase domain-containing protein 2 [Homo
            sapiens].
ACCESSION   NP_065109 XP_003120346
VERSION     NP_065109.1
DBSOURCE    REFSEQ: accession NM_020376.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Li,W., Liu,Q., Qian,Y., Wang,C., Kong,C., Sun,L., Sun,L., Liu,H.,
            Zhang,Y., Jiang,D., Jiang,C., Wang,S. and Xia,P.
  TITLE     Adipose triglyceride lipase suppresses noncanonical inflammasome by
            hydrolyzing LPS
  JOURNAL   Nat Chem Biol 20 (11), 1434-1442 (2024)
   PUBMED   38413746
  REMARK    GeneRIF: Adipose triglyceride lipase suppresses noncanonical
            inflammasome by hydrolyzing LPS.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Kondkar,A.A., Azad,T.A., Sultan,T., Khatlani,T., Alshehri,A.A.,
            Lobo,G.P., Kalantan,H., Al-Obeidan,S.A. and Al-Muammar,A.M.
  TITLE     Association between Polymorphism rs61876744 in PNPLA2 Gene and
            Keratoconus in a Saudi Cohort
  JOURNAL   Genes (Basel) 14 (12), 2108 (2023)
   PUBMED   38136930
  REMARK    GeneRIF: Association between Polymorphism rs61876744 in PNPLA2 Gene
            and Keratoconus in a Saudi Cohort.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Su,B.C., Xiao,K.M., Wang,K.L., Yang,S.F., Huang,Z.X. and Luo,J.W.
  TITLE     ATGL promotes colorectal cancer growth by regulating autophagy
            process and SIRT1 expression
  JOURNAL   Med Oncol 40 (12), 350 (2023)
   PUBMED   37935950
  REMARK    GeneRIF: ATGL promotes colorectal cancer growth by regulating
            autophagy process and SIRT1 expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Rossi,T., Zamponi,R., Chirico,M., Pisanu,M.E., Iorio,E.,
            Torricelli,F., Gugnoni,M., Ciarrocchi,A. and Pistoni,M.
  TITLE     BETi enhance ATGL expression and its lipase activity to exert their
            antitumoral effects in triple-negative breast cancer (TNBC) cells
  JOURNAL   J Exp Clin Cancer Res 42 (1), 7 (2023)
   PUBMED   36604676
  REMARK    GeneRIF: BETi enhance ATGL expression and its lipase activity to
            exert their antitumoral effects in triple-negative breast cancer
            (TNBC) cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Patel,R., Santoro,A., Hofer,P., Tan,D., Oberer,M., Nelson,A.T.,
            Konduri,S., Siegel,D., Zechner,R., Saghatelian,A. and Kahn,B.B.
  TITLE     ATGL is a biosynthetic enzyme for fatty acid esters of hydroxy
            fatty acids
  JOURNAL   Nature 606 (7916), 968-975 (2022)
   PUBMED   35676490
  REMARK    GeneRIF: ATGL is a biosynthetic enzyme for fatty acid esters of
            hydroxy fatty acids.
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Lake,A.C., Sun,Y., Li,J.L., Kim,J.E., Johnson,J.W., Li,D.,
            Revett,T., Shih,H.H., Liu,W., Paulsen,J.E. and Gimeno,R.E.
  TITLE     Expression, regulation, and triglyceride hydrolase activity of
            Adiponutrin family members
  JOURNAL   J Lipid Res 46 (11), 2477-2487 (2005)
   PUBMED   16150821
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Zimmermann,R., Strauss,J.G., Haemmerle,G., Schoiswohl,G.,
            Birner-Gruenberger,R., Riederer,M., Lass,A., Neuberger,G.,
            Eisenhaber,F., Hermetter,A. and Zechner,R.
  TITLE     Fat mobilization in adipose tissue is promoted by adipose
            triglyceride lipase
  JOURNAL   Science 306 (5700), 1383-1386 (2004)
   PUBMED   15550674
  REMARK    GeneRIF: reported that adipose triglyceride lipase (ATGL),
            catalyzes the initial step in triglyceride hydrolysis; ATGL and
            hormone-sensitive lipase (HSL) coordinately catabolize stored
            triglycerides in adipose tissue [ATGL]
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Jenkins,C.M., Mancuso,D.J., Yan,W., Sims,H.F., Gibson,B. and
            Gross,R.W.
  TITLE     Identification, cloning, expression, and purification of three
            novel human calcium-independent phospholipase A2 family members
            possessing triacylglycerol lipase and acylglycerol transacylase
            activities
  JOURNAL   J Biol Chem 279 (47), 48968-48975 (2004)
   PUBMED   15364929
  REMARK    GeneRIF: iPLA2epsilon (adiponutrin), iPLA2zeta (TTS-2.2), and
            iPLA2eta (GS2) are three novel TAG lipases/acylglycerol
            transacylases that likely participate in TAG hydrolysis and the
            acyl-CoA independent transacylation of acylglycerols
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Villena,J.A., Roy,S., Sarkadi-Nagy,E., Kim,K.H. and Sul,H.S.
  TITLE     Desnutrin, an adipocyte gene encoding a novel patatin
            domain-containing protein, is induced by fasting and
            glucocorticoids: ectopic expression of desnutrin increases
            triglyceride hydrolysis
  JOURNAL   J Biol Chem 279 (45), 47066-47075 (2004)
   PUBMED   15337759
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Hobart,M.J., Fernie,B.A., Stanley,K.K. and Lachmann,P.J.
  TITLE     C6 epitope expression by an unrelated antisense cDNA clone: an
            inadvertent surface-simulation mimotope
  JOURNAL   Proc Biol Sci 252 (1334), 157-162 (1993)
   PUBMED   7686673
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC017280.2, AP006621.1 and
            BC011958.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 4, 2011 this sequence version replaced XP_003120346.1.
            
            Summary: This gene encodes an enzyme which catalyzes the first step
            in the hydrolysis of triglycerides in adipose tissue. Mutations in
            this gene are associated with neutral lipid storage disease with
            myopathy. [provided by RefSeq, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HQ651812.1, JF279441.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336615.9/ ENSP00000337701.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..504
                     /product="patatin-like phospholipase domain-containing
                     protein 2"
                     /EC_number="3.1.1.3"
                     /EC_number="3.1.1.4"
                     /note="pigment epithelium-derived factor;
                     transport-secretion protein 2.2; desnutrin; triglyceride
                     hydrolase; adipose triglyceride lipase; TTS2.2;
                     IPLA2-zeta; calcium-independent phospholipase A2; patatin
                     like phospholipase domain containing 2; mutant
                     patatin-like phospholipase domain containing 2;
                     calcium-independent phospholipase A2-zeta; pigment
                     epithelium-derived factor receptor"
                     /calculated_mol_wt=55185
     Region          4..252
                     /region_name="Pat_PNPLA2"
                     /note="Patatin-like phospholipase domain containing
                     protein 2; cd07220"
                     /db_xref="CDD:132859"
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AD5.1)"
     Region          14..19
                     /region_name="GXGXXG.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01161"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AD5.1)"
     Site            order(15..16,18,47,166)
                     /site_type="active"
                     /db_xref="CDD:132859"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96AD5.1)"
     Site            43..63
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AD5.1)"
     Region          45..49
                     /region_name="GXSXG.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01161"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AD5.1)"
     Site            45..49
                     /site_type="other"
                     /note="nucleophile elbow"
                     /db_xref="CDD:132859"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AD5.1)"
     Region          166..168
                     /region_name="DGA/G.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01161"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AD5.1)"
     Site            330..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AD5.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine, in vitro.
                     /evidence=ECO:0000250|UniProtKB:Q8BJ56; propagated from
                     UniProtKB/Swiss-Prot (Q96AD5.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and FAM20C.
                     /evidence=ECO:0000269|PubMed:22733971,
                     ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96AD5.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96AD5.1)"
     Region          463..492
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AD5.1)"
     CDS             1..504
                     /gene="PNPLA2"
                     /gene_synonym="1110001C14Rik; ATGL; FP17548; iPLA2zeta;
                     PEDF-R; TTS-2.2; TTS2"
                     /coded_by="NM_020376.4:191..1705"
                     /db_xref="CCDS:CCDS7718.1"
                     /db_xref="GeneID:57104"
                     /db_xref="HGNC:HGNC:30802"
                     /db_xref="MIM:609059"
ORIGIN      
        1 mfprektwni sfagcgflgv yyvgvasclr ehapflvana thiygasaga ltatalvtgv
       61 clgeagakfi evskearkrf lgplhpsfnl vkiirsfllk vlpadsheha sgrlgisltr
      121 vsdgenviis hfnskdeliq anvcsgfipv ycglippslq gvryvdggis dnlplyelkn
      181 titvspfsge sdicpqdsst nihelrvtnt siqfnlrnly rlskalfppe plvlremckq
      241 gyrdglrflq rngllnrpnp llalpparph gpedkdqave saqaedysql pgedhilehl
      301 parlnealle acveptdllt tlsnmlpvrl atammvpytl plesalsfti rllewlpdvp
      361 edirwmkeqt gsicqylvmr akrklgrhlp srlpeqvelr rvqslpsvpl scaayrealp
      421 gwmrnnlslg dalakweecq rqlllglfct nvafppealr mrapadpapa padpaspqhq
      481 lagpapllst papearpvig algl
//
LOCUS       NP_004685                523 aa            linear   PRI 27-APR-2025
DEFINITION  monocarboxylate transporter 7 [Homo sapiens].
ACCESSION   NP_004685
VERSION     NP_004685.2
DBSOURCE    REFSEQ: accession NM_004694.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Higuchi,K., Sugiyama,K., Tomabechi,R., Kishimoto,H. and Inoue,K.
  TITLE     Mammalian monocarboxylate transporter 7 (MCT7/Slc16a6) is a novel
            facilitative taurine transporter
  JOURNAL   J Biol Chem 298 (4), 101800 (2022)
   PUBMED   35257743
  REMARK    GeneRIF: Mammalian monocarboxylate transporter 7 (MCT7/Slc16a6) is
            a novel facilitative taurine transporter.
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Dai,W., Liu,H., Chen,K., Xu,X., Qian,D., Luo,S., Amos,C.I.,
            Lee,J.E., Li,X., Nan,H., Li,C. and Wei,Q.
  TITLE     Genetic variants in PDSS1 and SLC16A6 of the ketone body metabolic
            pathway predict cutaneous melanoma-specific survival
  JOURNAL   Mol Carcinog 59 (6), 640-650 (2020)
   PUBMED   32232919
  REMARK    GeneRIF: Genetic variants in PDSS1 and SLC16A6 of the ketone body
            metabolic pathway predict cutaneous melanoma-specific survival.
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Murakami,Y., Kohyama,N., Kobayashi,Y., Ohbayashi,M., Ohtani,H.,
            Sawada,Y. and Yamamoto,T.
  TITLE     Functional characterization of human monocarboxylate transporter 6
            (SLC16A5)
  JOURNAL   Drug Metab Dispos 33 (12), 1845-1851 (2005)
   PUBMED   16174808
  REMARK    GeneRIF: MCT6 is involved in the disposition of various drugs,
            including bumetanide.
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Halestrap,A.P. and Meredith,D.
  TITLE     The SLC16 gene family-from monocarboxylate transporters (MCTs) to
            aromatic amino acid transporters and beyond
  JOURNAL   Pflugers Arch 447 (5), 619-628 (2004)
   PUBMED   12739169
  REMARK    Review article
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Halestrap,A.P. and Price,N.T.
  TITLE     The proton-linked monocarboxylate transporter (MCT) family:
            structure, function and regulation
  JOURNAL   Biochem J 343 Pt 2 (Pt 2), 281-299 (1999)
   PUBMED   10510291
  REMARK    Review article
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Price,N.T., Jackson,V.N. and Halestrap,A.P.
  TITLE     Cloning and sequencing of four new mammalian monocarboxylate
            transporter (MCT) homologues confirms the existence of a
            transporter family with an ancient past
  JOURNAL   Biochem J 329 (Pt 2) (Pt 2), 321-328 (1998)
   PUBMED   9425115
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC064832.1 and AC005332.1.
            
            On Jan 11, 2004 this sequence version replaced NP_004685.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064832.1, SRR14243140.652329.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000580666.6/ ENSP00000462985.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..523
                     /product="monocarboxylate transporter 7"
                     /note="monocarboxylate transporter 6; breast cancer
                     protein BCY5; solute carrier family 16, member 6
                     (monocarboxylic acid transporter 7)"
                     /calculated_mol_wt=57263
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Region          24..472
                     /region_name="MFS_MCT7"
                     /note="Monocarboxylate transporter 7 of the Major
                     Facilitator Superfamily of transporters; cd17422"
                     /db_xref="CDD:340980"
     Site            order(35..36,39..40,43,78,129..130,132..134,137,156,
                     159..160,163,301,304..305,308..310,313,340,344,395..396,
                     400,404,422,425..426,429..430,433)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340980"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Site            92..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Site            119..139
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B1AT66; propagated from
                     UniProtKB/Swiss-Prot (O15403.2)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15403.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15403.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15403.2)"
     Site            300..320
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Site            331..351
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Site            359..379
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Site            382..402
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Site            424..444
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     Site            453..473
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15403.2)"
     CDS             1..523
                     /gene="SLC16A6"
                     /gene_synonym="MCT6; MCT7"
                     /coded_by="NM_004694.5:50..1621"
                     /db_xref="CCDS:CCDS11675.1"
                     /db_xref="GeneID:9120"
                     /db_xref="HGNC:HGNC:10927"
                     /db_xref="MIM:603880"
ORIGIN      
        1 mtqnklklcs kanvytevpd ggwgwavavs fffvevftyg iiktfgvffn dlmdsfnesn
       61 sriswiisic vfvltfsapl atvlsnrfgh rlvvmlggll vstgmvaasf sqevshmyva
      121 igiisglgyc fsflptvtil sqyfgkrrsi vtavastgec favfafapai malkerigwr
      181 ysllfvgllq lnivifgall rpifirgpas pkiviqenrk eaqymlenek trtsidsids
      241 gvelttspkn vpthtnlele pkadmqqvlv ktsprpsekk aplldfsilk eksficyalf
      301 glfatlgffa pslyiiplgi slgidqdraa fllstmaiae vfgrigagfv lnrepirkiy
      361 ielicvillt vslfaftfat efwglmscsi ffgfmvgtig gthipllaed dvvgiekmss
      421 aagvyifiqs iaglagppla gllvdqskiy srafyscaag malaavclal vrpckmglcq
      481 hhhsgetkvv shrgktlqdi pedflemdla knehrvhvqm epv
//
LOCUS       NP_000837                222 aa            linear   PRI 27-APR-2025
DEFINITION  glutathione S-transferase A2 [Homo sapiens].
ACCESSION   NP_000837
VERSION     NP_000837.3
DBSOURCE    REFSEQ: accession NM_000846.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Rohrdanz,E., Nguyen,T. and Pickett,C.B.
  TITLE     Isolation and characterization of the human glutathione
            S-transferase A2 subunit gene
  JOURNAL   Arch Biochem Biophys 298 (2), 747-752 (1992)
   PUBMED   1329668
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Bogaards,J.J., van Ommen,B. and van Bladeren,P.J.
  TITLE     Purification and characterization of eight glutathione
            S-transferase isoenzymes of hamster. Comparison of subunit
            composition of enzymes from liver, kidney, testis, pancreas and
            trachea
  JOURNAL   Biochem J 286 (Pt 2) (Pt 2), 383-388 (1992)
   PUBMED   1530570
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Klone,A., Hussnatter,R. and Sies,H.
  TITLE     Cloning, sequencing and characterization of the human alpha
            glutathione S-transferase gene corresponding to the cDNA clone
            pGTH2
  JOURNAL   Biochem J 285 (Pt 3) (Pt 3), 925-928 (1992)
   PUBMED   1497629
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Strange,R.C., Fryer,A.A., Matharoo,B., Zhao,L., Broome,J.,
            Campbell,D.A., Jones,P., Pastor,I.C. and Singh,R.V.
  TITLE     The human glutathione S-transferases: comparison of isoenzyme
            expression in normal and astrocytoma brain
  JOURNAL   Biochim Biophys Acta 1139 (3), 222-228 (1992)
   PUBMED   1627661
REFERENCE   10 (residues 1 to 222)
  AUTHORS   Hayes,J.D., Kerr,L.A. and Cronshaw,A.D.
  TITLE     Evidence that glutathione S-transferases B1B1 and B2B2 are the
            products of separate genes and that their expression in human liver
            is subject to inter-individual variation. Molecular relationships
            between the B1 and B2 subunits and other Alpha class glutathione
            S-transferases
  JOURNAL   Biochem J 264 (2), 437-445 (1989)
   PUBMED   2604726
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC002895.2, AL109918.25,
            AK292602.1 and BU685446.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 29, 2008 this sequence version replaced NP_000837.2.
            
            Summary: Cytosolic and membrane-bound forms of glutathione
            S-transferase are encoded by two distinct supergene families. These
            enzymes function in the detoxification of electrophilic compounds,
            including carcinogens, therapeutic drugs, environmental toxins and
            products of oxidative stress, by conjugation with glutathione. The
            genes encoding these enzymes are known to be highly polymorphic.
            These genetic variations can change an individual's susceptibility
            to carcinogens and toxins as well as affect the toxicity and
            efficacy of some drugs. At present, eight distinct classes of the
            soluble cytoplasmic mammalian glutathione S-transferases have been
            identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta.
            This gene encodes a glutathione S-tranferase belonging to the alpha
            class. The alpha class genes, located in a cluster mapped to
            chromosome 6, are the most abundantly expressed glutathione
            S-transferases in liver. In addition to metabolizing bilirubin and
            certain anti-cancer drugs in the liver, the alpha class of these
            enzymes exhibit glutathione peroxidase activity thereby protecting
            the cells from reactive oxygen species and the products of
            peroxidation. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005682.1, SRR5189664.131477.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000493422.3/ ENSP00000420168.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.2"
     Protein         1..222
                     /product="glutathione S-transferase A2"
                     /EC_number="2.5.1.18"
                     /note="liver GST2; glutathione S-alkyltransferase A2;
                     glutathione S-aryltransferase A2;
                     S-(hydroxyalkyl)glutathione lyase A2; glutathione
                     S-aralkyltransferase A2; GST-gamma; GST HA subunit 2; GST
                     class-alpha member 2; testis tissue sperm-binding protein
                     Li 59n"
                     /calculated_mol_wt=25533
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P30115; propagated from
                     UniProtKB/Swiss-Prot (P09210.4)"
     Region          4..82
                     /region_name="GST_N_Alpha"
                     /note="GST_N family, Class Alpha subfamily; GSTs are
                     cytosolic dimeric proteins involved in cellular
                     detoxification by catalyzing the conjugation of
                     glutathione (GSH) with a wide range of endogenous and
                     xenobiotic alkylating agents, including carcinogens;
                     cd03077"
                     /db_xref="CDD:239375"
     Site            order(11,13,15,17..18,21,24..25,32,36,69,72..73)
                     /site_type="other"
                     /note="C-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:239375"
     Site            order(45,54..55,67..68)
                     /site_type="other"
                     /note="GSH binding site (G-site) [chemical binding]"
                     /db_xref="CDD:239375"
     Site            order(52..53,61,66..67,69..70,73..74,78)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239375"
     Region          86..220
                     /region_name="GST_C_Alpha"
                     /note="C-terminal, alpha helical domain of Class Alpha
                     Glutathione S-transferases; cd03208"
                     /db_xref="CDD:198317"
     Site            order(86..87,89,93..95,97..98,101,131)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(97,104,107,110..111,131..132,135,152..155,158,
                     161..162,165..166,169,193..194,196..201)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(101,107,111,131,208,216,220)
                     /site_type="other"
                     /note="substrate binding pocket (H-site) [chemical
                     binding]"
                     /db_xref="CDD:198317"
     Region          199..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09210.4)"
     CDS             1..222
                     /gene="GSTA2"
                     /gene_synonym="GST2; GSTA2-2; GTA2; GTH2"
                     /coded_by="NM_000846.5:63..731"
                     /db_xref="CCDS:CCDS4944.1"
                     /db_xref="GeneID:2939"
                     /db_xref="HGNC:HGNC:4627"
                     /db_xref="MIM:138360"
ORIGIN      
        1 maekpklhys nirgrmesir wllaaagvef eekfiksaed ldklrndgyl mfqqvpmvei
       61 dgmklvqtra ilnyiaskyn lygkdikeka lidmyiegia dlgemilllp fsqpeeqdak
      121 laliqektkn ryfpafekvl kshgqdylvg nklsradihl vellyyveel dsslissfpl
      181 lkalktrisn lptvkkflqp gsprkppmde ksleesrkif rf
//
LOCUS       NP_001351930             667 aa            linear   PRI 27-APR-2025
DEFINITION  transcription initiation factor TFIID subunit 6 isoform delta [Homo
            sapiens].
ACCESSION   NP_001351930 XP_006716165
VERSION     NP_001351930.1
DBSOURCE    REFSEQ: accession NM_001365001.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Tuc,E., Bengur,F.B., Aykut,A., Sahin,O. and Alanay,Y.
  TITLE     The third family with TAF6-related phenotype: Alazami-Yuan syndrome
  JOURNAL   Clin Genet 97 (5), 795-796 (2020)
   PUBMED   32030742
  REMARK    GeneRIF: The third family with TAF6-related phenotype: Alazami-Yuan
            syndrome.
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Delannoy,A., Wilhelm,E., Eilebrecht,S., Alvarado-Cuevas,E.M.,
            Benecke,A.G. and Bell,B.
  TITLE     BIM and NOXA are mitochondrial effectors of TAF6delta-driven
            apoptosis
  JOURNAL   Cell Death Dis 9 (2), 70 (2018)
   PUBMED   29358700
  REMARK    GeneRIF: BIM and NOXA contribute to TAF6delta-dependent cell death.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Gupta,K., Watson,A.A., Baptista,T., Scheer,E., Chambers,A.L.,
            Koehler,C., Zou,J., Obong-Ebong,I., Kandiah,E., Temblador,A.,
            Round,A., Forest,E., Man,P., Bieniossek,C., Laue,E.D., Lemke,E.A.,
            Rappsilber,J., Robinson,C.V., Devys,D., Tora,L. and Berger,I.
  TITLE     Architecture of TAF11/TAF13/TBP complex suggests novel regulation
            properties of general transcription factor TFIID
  JOURNAL   Elife 6, e30395 (2017)
   PUBMED   29111974
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Bell,B., Scheer,E. and Tora,L.
  TITLE     Identification of hTAF(II)80 delta links apoptotic signaling
            pathways to transcription factor TFIID function
  JOURNAL   Mol Cell 8 (3), 591-600 (2001)
   PUBMED   11583621
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Hisatake,K., Ohta,T., Takada,R., Guermah,M., Horikoshi,M.,
            Nakatani,Y. and Roeder,R.G.
  TITLE     Evolutionary conservation of human
            TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and
            interactions of TAFII80 with other TAFs and with general
            transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 92 (18), 8195-8199 (1995)
   PUBMED   7667268
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Weinzierl,R.O., Ruppert,S., Dynlacht,B.D., Tanese,N. and Tjian,R.
  TITLE     Cloning and expression of Drosophila TAFII60 and human TAFII70
            reveal conserved interactions with other subunits of TFIID
  JOURNAL   EMBO J 12 (13), 5303-5309 (1993)
   PUBMED   8262073
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 667)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
REFERENCE   10 (residues 1 to 667)
  AUTHORS   Mathe,G., Schwarzenberg,L., Halle-Pannenko,O. and Simmler,M.C.
  TITLE     Discussion paper: experimental and clinical immunopharmacology data
            applicable to cancer immunotherapy
  JOURNAL   Ann N Y Acad Sci 277 (00), 467-484 (1976)
   PUBMED   826207
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073842.5.
            
            On Jul 20, 2018 this sequence version replaced XP_006716165.1.
            
            Summary: Initiation of transcription by RNA polymerase II requires
            the activities of more than 70 polypeptides. The protein that
            coordinates these activities is transcription factor IID (TFIID),
            which binds to the core promoter to position the polymerase
            properly, serves as the scaffold for assembly of the remainder of
            the transcription complex, and acts as a channel for regulatory
            signals. TFIID is composed of the TATA-binding protein (TBP) and a
            group of evolutionarily conserved proteins known as TBP-associated
            factors or TAFs. TAFs may participate in basal transcription, serve
            as coactivators, function in promoter recognition or modify general
            transcription factors (GTFs) to facilitate complex assembly and
            transcription initiation. This gene encodes one of the smaller
            subunits of TFIID that binds weakly to TBP but strongly to TAF1,
            the largest subunit of TFIID. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jun 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.63449.1,
                                           SRR1660803.175966.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..667
                     /product="transcription initiation factor TFIID subunit 6
                     isoform delta"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, E, 70/85kD; transcription initiation
                     factor TFIID subunit 6; RNA polymerase II TBP-associated
                     factor subunit E; transcription initiation factor TFIID 70
                     kDa subunit; TAF6 RNA polymerase II, TATA box binding
                     protein (TBP)-associated factor, 80kDa"
                     /calculated_mol_wt=71349
     Region          12..67
                     /region_name="HFD_TAF6"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 6 (TAF6) and similar
                     proteins; cd22931"
                     /db_xref="CDD:467055"
     Site            order(38,42,46..47,49..54,62..63,66)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467055"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          132..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Region          204..420
                     /region_name="TAF6C"
                     /note="C-terminal domain of TATA Binding Protein (TBP)
                     Associated Factor 6 (TAF6); cd08050"
                     /db_xref="CDD:381749"
     Site            order(208..210,212..213,216,227..228,231,235,238..239,245)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:381749"
     Region          208..239
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          246..281
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63801; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          291..334
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          341..373
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          375..419
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          514..564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Site            514
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Region          601..667
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49848.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62311; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49848.1)"
     CDS             1..667
                     /gene="TAF6"
                     /gene_synonym="ALYUS; MGC:8964; TAF(II)70; TAF(II)80;
                     TAF2E; TAFII-70; TAFII-80; TAFII70; TAFII80; TAFII85"
                     /coded_by="NM_001365001.1:90..2093"
                     /note="isoform delta is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS94153.1"
                     /db_xref="GeneID:6878"
                     /db_xref="HGNC:HGNC:11540"
                     /db_xref="MIM:602955"
ORIGIN      
        1 maeekklkls ntvlpsesmk vvaesmgiaq iqeetcqllt dedalkfmhm gkrqklttsd
       61 idyalklknv eplygfhaqe fipfrfasgg grelyfyeek evdlsdiint plprvpldvc
      121 lkahwlsieg cqpaipenpp papkeqqkae ateplksakp gqeedgplkg kgqgattadg
      181 kgkekkappl legaplrlkp rsihelsveq qlyykeitea cvgsceakra ealqsiatdp
      241 glyqmlprfs tfisegvrvn vvqnnlalli ylmrmvkalm dnptlyleky vhelipavmt
      301 civsrqlclr pdvdnhwalr dfaarlvaqi ckhfstttnn iqsritktft kswvdektpw
      361 ttrygsiagl aelghdvikt lilprlqqeg erirsvldgp vlsnidriga dhvqslllkh
      421 capvlaklrp ppdnqdayra efgslgpllc sqvvkaraqa alqaqqvnrt tltitqprpt
      481 ltlsqapqpg prtpgllkvp gsialpvqtl vsaraaappq psppptkfiv msssssapst
      541 qqvlslstsa pgsgstttsp vtttvpsvqp ivklvstatt appstapsgp gsvqkyivvs
      601 lpptgegkgg ptshpspvpp passpsplsg salcggkqea gdspppapgt pkangsqpns
      661 gspqpap
//
LOCUS       NP_001357260             619 aa            linear   PRI 27-APR-2025
DEFINITION  ETS-related transcription factor Elf-1 isoform a [Homo sapiens].
ACCESSION   NP_001357260 XP_005266333
VERSION     NP_001357260.1
DBSOURCE    REFSEQ: accession NM_001370331.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Zhu,P., Dou,C., Song,Z., Bi,X., Wu,X. and Miao,Y.
  TITLE     ELF1/PRR11/ARP2/3 promoted trophoblast cells proliferation and
            motility in early pregnancy
  JOURNAL   Am J Reprod Immunol 90 (3), e13758 (2023)
   PUBMED   37641376
  REMARK    GeneRIF: ELF1/PRR11/ARP2/3 promoted trophoblast cells proliferation
            and motility in early pregnancy.
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Zhao,L., Wu,X., Zhang,Z., Fang,L., Yang,B. and Li,Y.
  TITLE     ELF1 suppresses autophagy to reduce cisplatin resistance via the
            miR-152-3p/NCAM1/ERK axis in lung cancer cells
  JOURNAL   Cancer Sci 114 (6), 2650-2663 (2023)
   PUBMED   36846943
  REMARK    GeneRIF: ELF1 suppresses autophagy to reduce cisplatin resistance
            via the miR-152-3p/NCAM1/ERK axis in lung cancer cells.
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Han,D., Li,X. and Cheng,Y.
  TITLE     Transcription Factor ELF1 Modulates Cisplatin Sensitivity in
            Prostate Cancer by Targeting MEIS Homeobox 2
  JOURNAL   Chem Res Toxicol 36 (3), 360-368 (2023)
   PUBMED   36763086
  REMARK    GeneRIF: Transcription Factor ELF1 Modulates Cisplatin Sensitivity
            in Prostate Cancer by Targeting MEIS Homeobox 2.
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Hu,M., Li,H., Xie,H., Fan,M., Wang,J., Zhang,N., Ma,J. and Che,S.
  TITLE     ELF1 Transcription Factor Enhances the Progression of Glioma via
            ATF5 promoter
  JOURNAL   ACS Chem Neurosci 12 (7), 1252-1261 (2021)
   PUBMED   33720698
  REMARK    GeneRIF: ELF1 Transcription Factor Enhances the Progression of
            Glioma via ATF5 promoter.
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Oettgen,P., Akbarali,Y., Boltax,J., Best,J., Kunsch,C. and
            Libermann,T.A.
  TITLE     Characterization of NERF, a novel transcription factor related to
            the Ets factor ELF-1
  JOURNAL   Mol Cell Biol 16 (9), 5091-5106 (1996)
   PUBMED   8756667
REFERENCE   7  (residues 1 to 619)
  AUTHORS   John,S., Reeves,R.B., Lin,J.X., Child,R., Leiden,J.M.,
            Thompson,C.B. and Leonard,W.J.
  TITLE     Regulation of cell-type-specific interleukin-2 receptor alpha-chain
            gene expression: potential role of physical interactions between
            Elf-1, HMG-I(Y), and NF-kappa B family proteins
  JOURNAL   Mol Cell Biol 15 (3), 1786-1796 (1995)
   PUBMED   7862168
REFERENCE   8  (residues 1 to 619)
  AUTHORS   Wang,C.Y., Petryniak,B., Thompson,C.B., Kaelin,W.G. and Leiden,J.M.
  TITLE     Regulation of the Ets-related transcription factor Elf-1 by binding
            to the retinoblastoma protein
  JOURNAL   Science 260 (5112), 1330-1335 (1993)
   PUBMED   8493578
REFERENCE   9  (residues 1 to 619)
  AUTHORS   Leiden,J.M., Wang,C.Y., Petryniak,B., Markovitz,D.M., Nabel,G.J.
            and Thompson,C.B.
  TITLE     A novel Ets-related transcription factor, Elf-1, binds to human
            immunodeficiency virus type 2 regulatory elements that are required
            for inducible trans activation in T cells
  JOURNAL   J Virol 66 (10), 5890-5897 (1992)
   PUBMED   1527846
REFERENCE   10 (residues 1 to 619)
  AUTHORS   Thompson,C.B., Wang,C.Y., Ho,I.C., Bohjanen,P.R., Petryniak,B.,
            June,C.H., Miesfeldt,S., Zhang,L., Nabel,G.J., Karpinski,B. et al.
  TITLE     cis-acting sequences required for inducible interleukin-2 enhancer
            function bind a novel Ets-related protein, Elf-1
  JOURNAL   Mol Cell Biol 12 (3), 1043-1053 (1992)
   PUBMED   1545787
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157877.11.
            
            On May 7, 2019 this sequence version replaced XP_005266333.1.
            
            Summary: This gene encodes an E26 transformation-specific related
            transcription factor. The encoded protein is primarily expressed in
            lymphoid cells and acts as both an enhancer and a repressor to
            regulate transcription of various genes. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Feb
            2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.218358.1,
                                           SRR1660807.197569.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267775 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.11"
     Protein         1..619
                     /product="ETS-related transcription factor Elf-1 isoform
                     a"
                     /note="ets-related transcription factor Elf-1; E74-like
                     factor 1 (ets domain transcription factor)"
                     /calculated_mol_wt=67367
     Region          2..111
                     /region_name="Elf-1_N"
                     /note="Transcription factor protein N terminal; pfam12310"
                     /db_xref="CDD:463529"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P32519.2)"
     Region          158..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32519.2)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P32519.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P32519.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P32519.2)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P32519.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P32519.2)"
     Region          207..289
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     Region          300..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32519.2)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P32519.2)"
     Region          564..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32519.2)"
     CDS             1..619
                     /gene="ELF1"
                     /gene_synonym="EFTUD1; RIA1"
                     /coded_by="NM_001370331.1:271..2130"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS9374.1"
                     /db_xref="GeneID:1997"
                     /db_xref="HGNC:HGNC:3316"
                     /db_xref="MIM:189973"
ORIGIN      
        1 maavvqqndl vfefasnvme derqlgdpai fpavivehvp gadilnsyag lacveepndm
       61 itessldvae eeiidddddd itltveasch dgdetietie aaeallnmds pgpmldekri
      121 nnnifssped dmvvapvthv svtldgipev metqqvqeky adspgasspe qpkrkkgrkt
      181 kpprpdspat tpnisvkkkn kdgkgntiyl wefllallqd katcpkyikw tqrekgifkl
      241 vdskavsrlw gkhknkpdmn yetmgralry yyqrgilakv egqrlvyqfk empkdliyin
      301 dedpsssies sdpslsssat snrnqtsrsr vssspgvkgg attvlkpgns kaakpkdpve
      361 vaqpsevlrt vqptqspypt qlfrtvhvvq pvqavpegea artstmqdet lnssvqsirt
      421 iqaptqvpvv vsprnqqlht vtlqtvpltt viastdpsag tgsqkfilqa ipssqpmtvl
      481 kenvmlqsqk agsppsivlg paqvqqvlts nvqticngtv svasspsfsa tapvvtfspr
      541 ssqlvahppg tvitsviktq etktltqeve kkesedhlke ntekteqqpq pyvmvvsssn
      601 gftsqvamkq nellepnsf
//
LOCUS       NP_002472                982 aa            linear   PRI 27-APR-2025
DEFINITION  protein phosphatase 1 regulatory subunit 12B isoform a [Homo
            sapiens].
ACCESSION   NP_002472
VERSION     NP_002472.2
DBSOURCE    REFSEQ: accession NM_002481.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 982)
  AUTHORS   Jia,D., Wang,K., Huang,L., Zhou,Z., Zhang,Y., Chen,N., Yang,Q.,
            Wen,Z., Jiang,H., Yao,C. and Wu,R.
  TITLE     Revealing PPP1R12B and COL1A1 as piRNA pathway genes contributing
            to abdominal aortic aneurysm through integrated analysis and
            experimental validation
  JOURNAL   Gene 897, 148068 (2024)
   PUBMED   38070790
  REMARK    GeneRIF: Revealing PPP1R12B and COL1A1 as piRNA pathway genes
            contributing to abdominal aortic aneurysm through integrated
            analysis and experimental validation.
REFERENCE   2  (residues 1 to 982)
  AUTHORS   Song,S.E., Kim,Y., Jeong,H., Lee,B., Lee,J., Roh,J.S., So,M.W.,
            Lee,S.G. and Sohn,D.H.
  TITLE     FAT10 differentially stabilizes MYPT2 isoforms
  JOURNAL   Biochem Biophys Res Commun 676, 115-120 (2023)
   PUBMED   37506472
  REMARK    GeneRIF: FAT10 differentially stabilizes MYPT2 isoforms.
REFERENCE   3  (residues 1 to 982)
  AUTHORS   Tan,J., Lu,T., Xu,J., Hou,Y., Chen,Z., Zhou,K., Ding,Y., Jiang,B.
            and Zhu,Y.
  TITLE     MicroRNA-4463 facilitates the development of colon cancer by
            suppression of the expression of PPP1R12B
  JOURNAL   Clin Transl Oncol 24 (6), 1115-1123 (2022)
   PUBMED   35064454
  REMARK    GeneRIF: MicroRNA-4463 facilitates the development of colon cancer
            by suppression of the expression of PPP1R12B.
REFERENCE   4  (residues 1 to 982)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 982)
  AUTHORS   Bannert,N., Vollhardt,K., Asomuddinov,B., Haag,M., Konig,H.,
            Norley,S. and Kurth,R.
  TITLE     PDZ Domain-mediated interaction of interleukin-16 precursor
            proteins with myosin phosphatase targeting subunits
  JOURNAL   J Biol Chem 278 (43), 42190-42199 (2003)
   PUBMED   12923170
REFERENCE   6  (residues 1 to 982)
  AUTHORS   Arimura,T., Suematsu,N., Zhou,Y.B., Nishimura,J., Satoh,S.,
            Takeshita,A., Kanaide,H. and Kimura,A.
  TITLE     Identification, characterization, and functional analysis of
            heart-specific myosin light chain phosphatase small subunit
  JOURNAL   J Biol Chem 276 (9), 6073-6082 (2001)
   PUBMED   11067852
REFERENCE   7  (residues 1 to 982)
  AUTHORS   Somlyo,A.P.
  TITLE     Kinases, myosin phosphatase and Rho proteins: curiouser and
            curiouser
  JOURNAL   J Physiol 516 (Pt 3) (Pt 3), 630 (1999)
   PUBMED   10200412
REFERENCE   8  (residues 1 to 982)
  AUTHORS   Somlyo,A.P., Wu,X., Walker,L.A. and Somlyo,A.V.
  TITLE     Pharmacomechanical coupling: the role of calcium, G-proteins,
            kinases and phosphatases
  JOURNAL   Rev Physiol Biochem Pharmacol 134, 201-234 (1999)
   PUBMED   10087910
  REMARK    Review article
REFERENCE   9  (residues 1 to 982)
  AUTHORS   Moorhead,G., Johnson,D., Morrice,N. and Cohen,P.
  TITLE     The major myosin phosphatase in skeletal muscle is a complex
            between the beta-isoform of protein phosphatase 1 and the MYPT2
            gene product
  JOURNAL   FEBS Lett 438 (3), 141-144 (1998)
   PUBMED   9827534
REFERENCE   10 (residues 1 to 982)
  AUTHORS   Fujioka,M., Takahashi,N., Odai,H., Araki,S., Ichikawa,K., Feng,J.,
            Nakamura,M., Kaibuchi,K., Hartshorne,D.J., Nakano,T. and Ito,M.
  TITLE     A new isoform of human myosin phosphatase targeting/regulatory
            subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal
            mapping
  JOURNAL   Genomics 49 (1), 59-68 (1998)
   PUBMED   9570949
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356953.17, AK307591.1,
            BC144699.1, AF324888.1, AC099336.2 and AC118556.2.
            
            On Nov 18, 2009 this sequence version replaced NP_002472.1.
            
            Summary: Myosin phosphatase is a protein complex comprised of three
            subunits: a catalytic subunit (PP1c-delta, protein phosphatase 1,
            catalytic subunit delta), a large regulatory subunit (MYPT, myosin
            phosphatase target) and small regulatory subunit (sm-M20). Two
            isoforms of MYPT have been isolated--MYPT1 and MYPT2, the first of
            which is widely expressed, and the second of which may be specific
            to heart, skeletal muscle, and brain. Each of the MYPT isoforms
            functions to bind PP1c-delta and increase phosphatase activity.
            This locus encodes both MYTP2 and M20. Alternatively spliced
            transcript variants encoding different isoforms have been
            identified. Related pseudogenes have been defined on the Y
            chromosome. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) lacks an alternate in-frame
            exon compared to variant 8. The resulting isoform (a, also known as
            the large myosin binding subunit) has the same N- and C-termini but
            is shorter compared to isoform h.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.139958.1, AF324888.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000608999.6/ ENSP00000476755.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..982
                     /product="protein phosphatase 1 regulatory subunit 12B
                     isoform a"
                     /EC_number="3.1.3.53"
                     /note="myosin phosphatase target subunit 2; myosin
                     phosphatase-targeting subunit 2; protein phosphatase 1,
                     regulatory (inhibitor) subunit 12B"
                     /calculated_mol_wt=110273
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG95; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     Region          57..86
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          <62..308
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(67..69,71..72,76,79,88,90,92,96..97,100..102,
                     104..105,109,112,121,123,125,129..130,133..135,137..138,
                     142,145,154)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          90..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          90..119
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          123..154
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          123..152
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          156..247
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <169..>257
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Region          216..245
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          249..280
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          249..278
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          342..517
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG95; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     Region          556..579
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          606..864
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Region          608..664
                     /region_name="IPD_MYPT1"
                     /note="inhibitory phosphorylation domain of myosin
                     phosphatase targeting subunit 1(MYPT1); cd21944"
                     /db_xref="CDD:412019"
     Region          <624..>738
                     /region_name="PspC_subgroup_1"
                     /note="pneumococcal surface protein PspC, choline-binding
                     form; NF033838"
                     /db_xref="CDD:468201"
     Site            646
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG95; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     Site            839
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG95; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     Region          881..982
                     /region_name="PRKG1_interact"
                     /note="cGMP-dependent protein kinase interacting domain;
                     pfam15898"
                     /db_xref="CDD:464927"
     Region          918..948
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60237.2)"
     Site            947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG95; propagated from
                     UniProtKB/Swiss-Prot (O60237.2)"
     CDS             1..982
                     /gene="PPP1R12B"
                     /gene_synonym="MYPT2; PP1bp55"
                     /coded_by="NM_002481.4:154..3102"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1426.1"
                     /db_xref="GeneID:4660"
                     /db_xref="HGNC:HGNC:7619"
                     /db_xref="MIM:603768"
ORIGIN      
        1 maelehlggk raesarmrra eqlrrwrgsl teqepaerrg agrqpltrrg sprvrfedga
       61 vflaacssgd tdevrkllar gadintvnvd gltalhqaci denldmvkfl venranvnqq
      121 dnegwtplha aascgylnia eyfinhgasv givnsegevp sdlaeepamk dllleqvkkq
      181 gvdleqsrke eeqqmlqdar qwlnsgkied vrqarsgata lhvaaakgys evlrlliqag
      241 yelnvqdydg wtplhaaahw gvkeacsila ealcdmdirn klgqtpfdva deglvehlel
      301 lqkkqnvlrs eketrnklie sdlnskiqsg ffknkekmly eeetpksqem eeenkessss
      361 sseeeegede asesetekea dkkpeafvnh snseskssit eqipapaqnt fsassarrfs
      421 sglfnkpeep kdespsswrl glrktgshnm lsevansrep irdrgssiyr ssssprisal
      481 ldnkdkeren ksyisslapr klnstsdiee kenresavnl vrsgsytrql wrdeakgnei
      541 pqtiapstyv stylkrtphk sqadttaekt adnvssstpl cvitnrplps tangvtatpv
      601 lsitgtdssv earekrrsyl tpvrdeeaes lrkarsrqar qtrrstqgvt ltdlqeaert
      661 fsrsraerqa qeqprekptd teglegspek hepsavpate agegqqpwgr sldeepichr
      721 lrcpaqpdkp ttpaspstsr pslytsshll wtnrfsvpds essetttntt takemdknen
      781 eeadldeqss krlsirerrr pkerrrgtgi nfwtkdedet dgseevketw herlsrlesg
      841 gsnpttsdsy gdrasararr earearlatl tsrveedsnr dykklyesal tenqklktkl
      901 qeaqleladi ksklekvaqq kqektsdrss vlemekrerr alerkmseme eemkvltelk
      961 sdnqrlkden galirviskl sk
//
LOCUS       NP_001015594             282 aa            linear   MAM 27-APR-2025
DEFINITION  armadillo repeat-containing protein 1 [Bos taurus].
ACCESSION   NP_001015594 XP_591780
VERSION     NP_001015594.2
DBSOURCE    REFSEQ: accession NM_001015594.3
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Harhay,G.P., Sonstegard,T.S., Keele,J.W., Heaton,M.P.,
            Clawson,M.L., Snelling,W.M., Wiedmann,R.T., Van Tassell,C.P. and
            Smith,T.P.
  TITLE     Characterization of 954 bovine full-CDS cDNA sequences
  JOURNAL   BMC Genomics 6, 166 (2005)
   PUBMED   16305752
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Smith,T.P., Grosse,W.M., Freking,B.A., Roberts,A.J., Stone,R.T.,
            Casas,E., Wray,J.E., White,J., Cho,J., Fahrenkrug,S.C.,
            Bennett,G.L., Heaton,M.P., Laegreid,W.W., Rohrer,G.A.,
            Chitko-McKown,C.G., Pertea,G., Holt,I., Karamycheva,S., Liang,F.,
            Quackenbush,J. and Keele,J.W.
  TITLE     Sequence evaluation of four pooled-tissue normalized bovine cDNA
            libraries and construction of a gene index for cattle
  JOURNAL   Genome Res 11 (4), 626-630 (2001)
   PUBMED   11282978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EH163954.1, EV727326.1 and NKLS02000014.1.
            
            On Aug 28, 2005 this sequence version replaced NP_001015594.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5571264.15056.1,
                                           SRR5571264.15909.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA6648753,
                                           SAMEA6648754 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="14"
                     /map="14"
                     /breed="Hereford"
     Protein         1..282
                     /product="armadillo repeat-containing protein 1"
                     /note="RasGEF domain family, member 1A"
                     /calculated_mol_wt=31149
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9NVT9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBE1.1)"
     Region          27..67
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          39..81
                     /region_name="ARM"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBE1.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NVT9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBE1.1)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NVT9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBE1.1)"
     Region          239..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBE1.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D7A8; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBE1.1)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NVT9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBE1.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D7A8; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBE1.1)"
     CDS             1..282
                     /gene="ARMC1"
                     /coded_by="NM_001015594.3:229..1077"
                     /db_xref="BGD:BT25210"
                     /db_xref="GeneID:514000"
                     /db_xref="VGNC:VGNC:26155"
ORIGIN      
        1 mnsssstmne epdalsvvnq lrdlaadpln rraivqdqgc lpglilfmdh pnppvvhsal
       61 lalrylaecr anrekmkgel gmmlslqnvi qksttpgetk llaseiydil qssnmadgds
      121 fnemnsrrrk aqfflgttnk raktvvlhid glddtsrrnl ceeallkikg visftfqmav
      181 qrcvvrirsd lkaealasai astkvmkaqq vvksesgeem lvpfqdtpve veqntelpdy
      241 lpedesptke qdkavsrvgs hpeggaswls taanflsrsf yw
//
LOCUS       NP_004545                902 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear factor of activated T-cells, cytoplasmic 4 isoform 2 [Homo
            sapiens].
ACCESSION   NP_004545
VERSION     NP_004545.2
DBSOURCE    REFSEQ: accession NM_004554.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Yu,S., Sun,Z., Ju,T., Liu,Y., Mei,Z., Wang,C., Qu,Z., Li,N., Wu,F.,
            Liu,K., Lu,M., Huang,M., Pang,X., Jia,Y., Li,Y., Zhang,Y., Dou,S.,
            Jiang,J., Dong,X., Huang,C., Li,W., Zhang,Y., Yuan,Y., Yang,B. and
            Du,W.
  TITLE     The m7G Methyltransferase Mettl1 Drives Cardiac Hypertrophy by
            Regulating SRSF9-Mediated Splicing of NFATc4
  JOURNAL   Adv Sci (Weinh) 11 (29), e2308769 (2024)
   PUBMED   38810124
  REMARK    GeneRIF: The m7G Methyltransferase Mettl1 Drives Cardiac
            Hypertrophy by Regulating SRSF9-Mediated Splicing of NFATc4.
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Zhang,X., Lei,F., Wang,X.M., Deng,K.Q., Ji,Y.X., Zhang,Y., Li,H.,
            Zhang,X.D., Lu,Z. and Zhang,P.
  TITLE     NULP1 Alleviates Cardiac Hypertrophy by Suppressing NFAT3
            Transcriptional Activity
  JOURNAL   J Am Heart Assoc 9 (16), e016419 (2020)
   PUBMED   32805187
  REMARK    GeneRIF: NULP1 Alleviates Cardiac Hypertrophy by Suppressing NFAT3
            Transcriptional Activity.
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Cole,A.J., Iyengar,M., Panesso-Gomez,S., O'Hayer,P., Chan,D.,
            Delgoffe,G.M., Aird,K.M., Yoon,E., Bai,S. and Buckanovich,R.J.
  TITLE     NFATC4 promotes quiescence and chemotherapy resistance in ovarian
            cancer
  JOURNAL   JCI Insight 5 (7), 131486 (2020)
   PUBMED   32182216
  REMARK    GeneRIF: NFATC4 promotes quiescence and chemotherapy resistance in
            ovarian cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 902)
  AUTHORS   Kaminuma,O., Kitamura,N., Nishito,Y., Nemoto,S., Tatsumi,H.,
            Mori,A. and Hiroi,T.
  TITLE     Downregulation of NFAT3 Due to Lack of T-Box Transcription Factor
            TBX5 Is Crucial for Cytokine Expression in T Cells
  JOURNAL   J Immunol 200 (1), 92-100 (2018)
   PUBMED   29180489
  REMARK    GeneRIF: TBX5 deficiency-mediated downregulation of NFAT3 is
            crucial for the high cytokine-producing activity of T cells
REFERENCE   6  (residues 1 to 902)
  AUTHORS   Molkentin,J.D., Lu,J.R., Antos,C.L., Markham,B., Richardson,J.,
            Robbins,J., Grant,S.R. and Olson,E.N.
  TITLE     A calcineurin-dependent transcriptional pathway for cardiac
            hypertrophy
  JOURNAL   Cell 93 (2), 215-228 (1998)
   PUBMED   9568714
REFERENCE   7  (residues 1 to 902)
  AUTHORS   Aramburu,J., Garcia-Cozar,F., Raghavan,A., Okamura,H., Rao,A. and
            Hogan,P.G.
  TITLE     Selective inhibition of NFAT activation by a peptide spanning the
            calcineurin targeting site of NFAT
  JOURNAL   Mol Cell 1 (5), 627-637 (1998)
   PUBMED   9660947
REFERENCE   8  (residues 1 to 902)
  AUTHORS   Rao,A., Luo,C. and Hogan,P.G.
  TITLE     Transcription factors of the NFAT family: regulation and function
  JOURNAL   Annu Rev Immunol 15, 707-747 (1997)
   PUBMED   9143705
  REMARK    Review article
REFERENCE   9  (residues 1 to 902)
  AUTHORS   Hoey,T., Sun,Y.L., Williamson,K. and Xu,X.
  TITLE     Isolation of two new members of the NF-AT gene family and
            functional characterization of the NF-AT proteins
  JOURNAL   Immunity 2 (5), 461-472 (1995)
   PUBMED   7749981
REFERENCE   10 (residues 1 to 902)
  AUTHORS   Vacca,A., Farina,M., Maroder,M., Alesse,E., Screpanti,I., Frati,L.
            and Gulino,A.
  TITLE     Human immunodeficiency virus type-1 tat enhances interleukin-2
            promoter activity through synergism with phorbol ester and
            calcium-mediated activation of the NF-AT cis-regulatory motif
  JOURNAL   Biochem Biophys Res Commun 205 (1), 467-474 (1994)
   PUBMED   7999066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC318153.1, BC053855.1,
            BC008857.2 and DB372155.1.
            
            On Jan 24, 2003 this sequence version replaced NP_004545.1.
            
            Summary: This gene encodes a member of the nuclear factor of
            activated T cells (NFAT) protein family. The encoded protein is
            part of a DNA-binding transcription complex. This complex consists
            of at least two components: a preexisting cytosolic component that
            translocates to the nucleus upon T cell receptor stimulation and an
            inducible nuclear component. NFAT proteins are activated by the
            calmodulin-dependent phosphatase, calcineurin. The encoded protein
            plays a role in the inducible expression of cytokine genes in T
            cells, especially in the induction of interleukin-2 and
            interleukin-4. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053855.1, L41066.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000250373.9/ ENSP00000250373.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..902
                     /product="nuclear factor of activated T-cells, cytoplasmic
                     4 isoform 2"
                     /note="nuclear factor of activated T-cells, cytoplasmic 4;
                     T-cell transcription factor NFAT3; nuclear factor of
                     activated T-cells, cytoplasmic, calcineurin-dependent 4"
                     /calculated_mol_wt=95318
     Region          16..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14934.2)"
     Region          114..119
                     /region_name="Calcineurin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14934.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK7 and MAPK14.
                     /evidence=ECO:0000269|PubMed:11997522,
                     ECO:0000269|PubMed:18347059; propagated from
                     UniProtKB/Swiss-Prot (Q14934.2)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK7 and MAPK14.
                     /evidence=ECO:0000269|PubMed:11997522,
                     ECO:0000269|PubMed:18347059; propagated from
                     UniProtKB/Swiss-Prot (Q14934.2)"
     Region          208..369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14934.2)"
     Region          213..293
                     /region_name="2 approximate SP repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14934.2)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8 and MAPK9.
                     /evidence=ECO:0000269|PubMed:17875713; propagated from
                     UniProtKB/Swiss-Prot (Q14934.2)"
     Region          <214..413
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8 and MAPK9.
                     /evidence=ECO:0000269|PubMed:17875713; propagated from
                     UniProtKB/Swiss-Prot (Q14934.2)"
     Region          268..270
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14934.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA3.
                     /evidence=ECO:0000269|PubMed:17213202; propagated from
                     UniProtKB/Swiss-Prot (Q14934.2)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA3.
                     /evidence=ECO:0000269|PubMed:17213202; propagated from
                     UniProtKB/Swiss-Prot (Q14934.2)"
     Region          407..580
                     /region_name="RHD-n_NFAT"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor of activated T-cells (NFAT)
                     proteins; cd07881"
                     /db_xref="CDD:143641"
     Site            order(430,433,435..436,438..440,487,528,530..531,545..546,
                     548,579)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143641"
     Region          585..685
                     /region_name="IPT_NFAT"
                     /note="IPT domain of the NFAT family of transcription
                     factors. NFAT transcription complexes are a target of
                     calcineurin, a calcium dependent phosphatase, and activate
                     genes mainly involved in cell-cell-interaction; cd01178"
                     /db_xref="CDD:238583"
     Site            order(609,673)
                     /site_type="DNA binding"
                     /note="DNA binding sites [nucleotide binding]"
                     /db_xref="CDD:238583"
     Region          672..674
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14934.2)"
     Region          791..870
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14934.2)"
     CDS             1..902
                     /gene="NFATC4"
                     /gene_synonym="NF-AT3; NF-ATC4; NFAT3"
                     /coded_by="NM_004554.5:158..2866"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9629.1"
                     /db_xref="GeneID:4776"
                     /db_xref="HGNC:HGNC:7778"
                     /db_xref="MIM:602699"
ORIGIN      
        1 mgaascedee lefklvfgee keapplgagg lgeeldseda ppccrlalge pppygaapig
       61 iprpppprpg mhsppprpap spgtwesqpa rsvrlggpgg gaggagggrv lecpsirits
      121 isptpeppaa lednpdawgd gsprdypppe gfggyreagg qgggaffsps pgssslssws
      181 ffsdasdeaa lyaacdeves elneaasrfg lgsplpspra sprpwtpedp wslygpspgg
      241 rgpedswlll sapgptpasp rpaspcgkrr ysssgtpssa spalsrrgsl geegsepppp
      301 pplplardpg spgpfdyvga ppaesipqkt rrtsseqava lprseepasc ngklplgaee
      361 svappggsrk evagmdylav psplawskar igghspifrt salppldwpl psqyeqlelr
      421 ievqprahhr ahyetegsrg avkaapgghp vvkllgysek pltlqmfigt adernlrpha
      481 fyqvhritgk mvatasyeav vsgtkvlemt llpennmaan idcagilklr nsdielrkge
      541 tdigrkntrv rlvfrvhvpq gggkvvsvqa asvpiecsqr saqelpqvea yspsacsvrg
      601 geelvltgsn flpdskvvfi ergpdgklqw eeeatvnrlq snevtltltv peysnkrvsr
      661 pvqvyfyvsn grrkrsptqs frflpvicke eplpdsslrg fpsasatpfg tdmdfspprp
      721 pypsyphedp acetpylseg fgygmpplyp qtgpppsyrp glrmfpetrg ttgcaqppav
      781 sflprpfpsd pyggrgssfs lglpfsppap frppplpasp plegpfpsqs dvhplpaegy
      841 nkvgpgygpg egapeqeksr ggyssgfrds vpiqgitlee vseiigrdls gfpappgeep
      901 pa
//
LOCUS       NP_001355934             254 aa            linear   PRI 27-APR-2025
DEFINITION  aprataxin isoform j [Homo sapiens].
ACCESSION   NP_001355934 XP_006716855
VERSION     NP_001355934.1
DBSOURCE    REFSEQ: accession NM_001369005.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_006716855.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.233379.1,
                                           SRR1660805.182456.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..254
                     /product="aprataxin isoform j"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=28977
     Region          76..177
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(170,172,174..176)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            172
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          195..254
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..254
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001369005.1:432..1196"
                     /note="isoform j is encoded by transcript variant 26"
                     /db_xref="CCDS:CCDS47957.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mvnelypyiv efeeeaknpg lethrkrkrs gnsdsierda aqeaeagtgl epgsnsgqcs
       61 vplkkgkdap ikkeslghws qglkismqdp kmqvykdeqv vvikdkypka ryhwlvlpwt
      121 sisslkavar ehlellkhmh tvgekvivdf agssklrfrl gyhaipsmsh vhlhvisqdf
      181 dspclknkkh wnsfnteyfl esqaviemvq eagrvtvrdg mpellklplr checqqllps
      241 ipqlkehlrk hwtq
//
LOCUS       NP_001355555             310 aa            linear   ROD 27-APR-2025
DEFINITION  aminoacyl tRNA synthase complex-interacting multifunctional protein
            1 isoform 2 [Mus musculus].
ACCESSION   NP_001355555
VERSION     NP_001355555.1
DBSOURCE    REFSEQ: accession NM_001368626.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Ranasinghe,A.D.C.U., Lee,D.D. and Schwarz,M.A.
  TITLE     Mechanistic regulation of SPHK1 expression and translocation by
            EMAP II in pulmonary smooth muscle cells
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (12), 158789 (2020)
   PUBMED   32771459
  REMARK    GeneRIF: Mechanistic regulation of SPHK1 expression and
            translocation by EMAP II in pulmonary smooth muscle cells.
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Bertrand-Gaday,C., Letheule,M., Blanchet,E., Vernus,B.,
            Pessemesse,L., Bonnet-Garnier,A., Bonnieu,A. and Casas,F.
  TITLE     Transient Changes of Metabolism at the Pronuclear Stage in Mice
            Influences Skeletal Muscle Phenotype in Adulthood
  JOURNAL   Int J Mol Sci 21 (19), 7203 (2020)
   PUBMED   33003470
  REMARK    GeneRIF: Transient Changes of Metabolism at the Pronuclear Stage in
            Mice Influences Skeletal Muscle Phenotype in Adulthood.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Lee,D.D., Hochstetler,A., Sah,E., Xu,H., Lowe,C.W., Santiaguel,S.,
            Thornton,J.L., Pajakowski,A. and Schwarz,M.A.
  TITLE     Influence of aminoacyl-tRNA synthetase complex-interacting
            multifunctional protein 1 on epithelial differentiation and
            organization during lung development
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 319 (2), L369-L379 (2020)
   PUBMED   32579851
  REMARK    GeneRIF: Influence of aminoacyl-tRNA synthetase complex-interacting
            multifunctional protein 1 on epithelial differentiation and
            organization during lung development.
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Zou,C., Gu,C., Zhao,M., Zhu,D., Wang,N., Yu,J., Yao,Y., Chen,Y.,
            Shi,M., Gu,Q., Qian,Y., Qiu,Q. and Zheng,Z.
  TITLE     The Role of the AIMP1 Pathway in Diabetic Retinopathy:
            AIMP1-Targeted Intervention Study in Diabetic Retinopathy
  JOURNAL   Ophthalmic Res 63 (2), 122-132 (2020)
   PUBMED   31962335
  REMARK    GeneRIF: The Role of the AIMP1 Pathway in Diabetic Retinopathy:
            AIMP1-Targeted Intervention Study in Diabetic Retinopathy.
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Zhang,F. and Schwarz,M.A.
  TITLE     Temporo-spatial distribution of endothelial-monocyte activating
            polypeptide II, an anti-angiogenic protein, in the mouse embryo
  JOURNAL   Dev Dyn 218 (3), 490-498 (2000)
   PUBMED   10878614
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Knies,U.E., Kroger,S. and Clauss,M.
  TITLE     Expression of EMAP II in the developing and adult mouse
  JOURNAL   Apoptosis 5 (2), 141-151 (2000)
   PUBMED   11232242
REFERENCE   8  (residues 1 to 310)
  AUTHORS   Kao,J., Houck,K., Fan,Y., Haehnel,I., Libutti,S.K., Kayton,M.L.,
            Grikscheit,T., Chabot,J., Nowygrod,R., Greenberg,S. et al.
  TITLE     Characterization of a novel tumor-derived cytokine.
            Endothelial-monocyte activating polypeptide II
  JOURNAL   J Biol Chem 269 (40), 25106-25119 (1994)
   PUBMED   7929199
REFERENCE   9  (residues 1 to 310)
  AUTHORS   Kao,J., Fan,Y.G., Haehnel,I., Brett,J., Greenberg,S., Clauss,M.,
            Kayton,M., Houck,K., Kisiel,W., Seljelid,R. et al.
  TITLE     A peptide derived from the amino terminus of
            endothelial-monocyte-activating polypeptide II modulates
            mononuclear and polymorphonuclear leukocyte functions, defines an
            apparently novel cellular interaction site, and induces an acute
            inflammatory response
  JOURNAL   J Biol Chem 269 (13), 9774-9782 (1994)
   PUBMED   7545917
REFERENCE   10 (residues 1 to 310)
  AUTHORS   Kao,J., Ryan,J., Brett,G., Chen,J., Shen,H., Fan,Y.G., Godman,G.,
            Familletti,P.C., Wang,F., Pan,Y.C. et al.
  TITLE     Endothelial monocyte-activating polypeptide II. A novel
            tumor-derived polypeptide that activates host-response mechanisms
  JOURNAL   J Biol Chem 267 (28), 20239-20247 (1992)
   PUBMED   1400342
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC135118.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3472511.1,
                                           ERR2680379.320809.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3 61.48 cM"
     Protein         1..310
                     /product="aminoacyl tRNA synthase complex-interacting
                     multifunctional protein 1 isoform 2"
                     /note="small inducible cytokine subfamily E, member 1;
                     aminoacyl tRNA synthase complex-interacting
                     multifunctional protein 1; multisynthetase complex
                     auxiliary component p43; multisynthase complex auxiliary
                     component p43; ARS inducible multifunctional protein 1;
                     endothelial monocyte activating polypeptide 2"
                     /calculated_mol_wt=33866
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q12904; propagated from
                     UniProtKB/Swiss-Prot (P31230.2)"
     Region          5..>73
                     /region_name="PRK05431"
                     /note="seryl-tRNA synthetase; Provisional"
                     /db_xref="CDD:235461"
     Region          6..46
                     /region_name="Required for fibroblast proliferation.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P31230.2)"
     Region          54..192
                     /region_name="Interaction with HSP90B1.
                     /evidence=ECO:0000269|PubMed:17525271"
                     /note="propagated from UniProtKB/Swiss-Prot (P31230.2)"
     Region          92..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31230.2)"
     Region          101..115
                     /region_name="Required for endothelial cell death.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P31230.2)"
     Region          <106..310
                     /region_name="PLN02610"
                     /note="probable methionyl-tRNA synthetase"
                     /db_xref="CDD:215329"
     Region          115..190
                     /region_name="Required for endothelial cell migration.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P31230.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12904; propagated from
                     UniProtKB/Swiss-Prot (P31230.2)"
     CDS             1..310
                     /gene="Aimp1"
                     /gene_synonym="9830137A06Rik; AIMP1/p43; Emap2; EMAPII;
                     p43; Scye1"
                     /coded_by="NM_001368626.1:209..1141"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS89689.1"
                     /db_xref="GeneID:13722"
                     /db_xref="MGI:MGI:102774"
ORIGIN      
        1 matndavlkr leqkgaeadq iieylkqqva llkekailqa tmreekklrv enaklkkeie
       61 elkqelilae ihngveqvrv rlstplqtnc tasesvvqsp svattaspat keqikageek
      121 kvkektekkg ekkekqqsaa astdskpida srldlrigci vtakkhpdad slyveevdvg
      181 eaaprtvvsg lvnhvpleqm qnrmvvllcn lkpakmrgvl sqamvmcass pekveilapp
      241 ngsvpgdrit fdafpgepdk elnpkkkiwe qiqpdlhtna ecvatykgap fevkgkgvcr
      301 aqtmansgik
//
LOCUS       NP_079033               1298 aa            linear   PRI 27-APR-2025
DEFINITION  histone-lysine N-methyltransferase EHMT1 isoform 1 [Homo sapiens].
ACCESSION   NP_079033 XP_947661 XP_951210 XP_951212 XP_951215 XP_951217
            XP_951219 XP_951221 XP_951223 XP_951226
VERSION     NP_079033.4
DBSOURCE    REFSEQ: accession NM_024757.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1298)
  AUTHORS   Souza,B.K., Freire,N.H., Monteiro,T.S., Herlinger,A.L., Jaeger,M.,
            Dalmolin,M.G.S., de Farias,C.B., Gregianin,L., Brunetto,A.T.,
            Brunetto,A.L., Thiele,C.J. and Roesler,R.
  TITLE     Histone Methyltransferases G9a/Ehmt2 and GLP/Ehmt1 Are Associated
            with Cell Viability and Poorer Prognosis in Neuroblastoma and Ewing
            Sarcoma
  JOURNAL   Int J Mol Sci 24 (20), 15242 (2023)
   PUBMED   37894922
  REMARK    GeneRIF: Histone Methyltransferases G9a/Ehmt2 and GLP/Ehmt1 Are
            Associated with Cell Viability and Poorer Prognosis in
            Neuroblastoma and Ewing Sarcoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1298)
  AUTHORS   Besschetnova,A., Han,W., Liu,M., Gao,Y., Li,M., Wang,Z., Labaf,M.,
            Patalano,S., Venkataramani,K., Muriph,R.E., Macoska,J.A.,
            Siegfried,K.R., Evans,J., Balk,S.P., Gao,S., Han,D. and Cai,C.
  TITLE     Demethylation of EHMT1/GLP Protein Reprograms Its Transcriptional
            Activity and Promotes Prostate Cancer Progression
  JOURNAL   Cancer Res Commun 3 (8), 1716-1730 (2023)
   PUBMED   37663929
  REMARK    GeneRIF: Demethylation of EHMT1/GLP Protein Reprograms Its
            Transcriptional Activity and Promotes Prostate Cancer Progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1298)
  AUTHORS   Iglesias-Ortega,L., Megias-Fernandez,C., Dominguez-Gimenez,P.,
            Jimeno-Gonzalez,S. and Rivero,S.
  TITLE     Cell consequences of loss of function of the epigenetic factor
            EHMT1
  JOURNAL   Cell Signal 108, 110734 (2023)
   PUBMED   37257768
  REMARK    GeneRIF: Cell consequences of loss of function of the epigenetic
            factor EHMT1.
REFERENCE   4  (residues 1 to 1298)
  AUTHORS   Nachiyappan,A., Gupta,N. and Taneja,R.
  TITLE     EHMT1/EHMT2 in EMT, cancer stemness and drug resistance: emerging
            evidence and mechanisms
  JOURNAL   FEBS J 289 (5), 1329-1351 (2022)
   PUBMED   34954891
  REMARK    GeneRIF: EHMT1/EHMT2 in EMT, cancer stemness and drug resistance:
            emerging evidence and mechanisms.
            Review article
REFERENCE   5  (residues 1 to 1298)
  AUTHORS   Kleefstra,T., Brunner,H.G., Amiel,J., Oudakker,A.R., Nillesen,W.M.,
            Magee,A., Genevieve,D., Cormier-Daire,V., van Esch,H., Fryns,J.P.,
            Hamel,B.C., Sistermans,E.A., de Vries,B.B. and van Bokhoven,H.
  TITLE     Loss-of-function mutations in euchromatin histone methyl
            transferase 1 (EHMT1) cause the 9q34 subtelomeric deletion syndrome
  JOURNAL   Am J Hum Genet 79 (2), 370-377 (2006)
   PUBMED   16826528
  REMARK    GeneRIF: Haploinsufficiency of EHMT1 is causative for 9q
            subtelomeric deletion syndrome.
REFERENCE   6  (residues 1 to 1298)
  AUTHORS   Cebrian,A., Pharoah,P.D., Ahmed,S., Ropero,S., Fraga,M.F.,
            Smith,P.L., Conroy,D., Luben,R., Perkins,B., Easton,D.F.,
            Dunning,A.M., Esteller,M. and Ponder,B.A.
  TITLE     Genetic variants in epigenetic genes and breast cancer risk
  JOURNAL   Carcinogenesis 27 (8), 1661-1669 (2006)
   PUBMED   16501248
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1298)
  AUTHORS   Ueda,J., Tachibana,M., Ikura,T. and Shinkai,Y.
  TITLE     Zinc finger protein Wiz links G9a/GLP histone methyltransferases to
            the co-repressor molecule CtBP
  JOURNAL   J Biol Chem 281 (29), 20120-20128 (2006)
   PUBMED   16702210
REFERENCE   8  (residues 1 to 1298)
  AUTHORS   Kleefstra,T., Smidt,M., Banning,M.J., Oudakker,A.R., Van Esch,H.,
            de Brouwer,A.P., Nillesen,W., Sistermans,E.A., Hamel,B.C., de
            Bruijn,D., Fryns,J.P., Yntema,H.G., Brunner,H.G., de Vries,B.B. and
            van Bokhoven,H.
  TITLE     Disruption of the gene Euchromatin Histone Methyl Transferase1
            (Eu-HMTase1) is associated with the 9q34 subtelomeric deletion
            syndrome
  JOURNAL   J Med Genet 42 (4), 299-306 (2005)
   PUBMED   15805155
  REMARK    GeneRIF: This indicates that haploinsufficiency of Eu-HMTase1 is
            responsible for the 9q submicroscopic subtelomeric deletion
            syndrome
REFERENCE   9  (residues 1 to 1298)
  AUTHORS   Ogawa,H., Ishiguro,K., Gaubatz,S., Livingston,D.M. and Nakatani,Y.
  TITLE     A complex with chromatin modifiers that occupies E2F- and
            Myc-responsive genes in G0 cells
  JOURNAL   Science 296 (5570), 1132-1136 (2002)
   PUBMED   12004135
REFERENCE   10 (residues 1 to 1298)
  AUTHORS   Kleefstra,T. and de Leeuw,N.
  TITLE     Kleefstra Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20945554
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC047504.1, AB028932.1,
            BC011608.2 and CA426038.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 3, 2009 this sequence version replaced NP_079033.3.
            
            Summary: The protein encoded by this gene is a histone
            methyltransferase that methylates the lysine-9 position of histone
            H3. This action marks the genomic region packaged with these
            methylated histones for transcriptional repression. This protein
            may be involved in the silencing of MYC- and E2F-responsive genes
            and therefore could play a role in the G0/G1 cell cycle transition.
            Defects in this gene are a cause of chromosome 9q subtelomeric
            deletion syndrome (9q-syndrome, also known as Kleefstra syndrome).
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2017].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.42755.1,
                                           SRR1803613.6578.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000460843.6/ ENSP00000417980.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..1298
                     /product="histone-lysine N-methyltransferase EHMT1 isoform
                     1"
                     /EC_number="2.1.1.367"
                     /note="histone-lysine N-methyltransferase EHMT1;
                     histone-lysine N-methyltransferase, H3 lysine-9 specific
                     5; histone H3-K9 methyltransferase 5; euchromatic
                     histone-lysine N-methyltransferase 1; H3-K9-HMTase 5;
                     lysine N-methyltransferase 1D; G9a-like protein 1; EHMT1
                     intronic transcript 1"
                     /calculated_mol_wt=141336
     Region          1..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:25489052; propagated from
                     UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          144..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          211..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          339..479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          514..644
                     /region_name="EHMT_ZBD"
                     /note="Zinc-binding domain of euchromatic histone lysine
                     methyltransferases EHMT1 and EHTM2; cd20905"
                     /db_xref="CDD:411018"
     Region          644..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          720..976
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          737..766
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          742..768
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          772..801
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          774..803
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(805,807,811..812,815..817,819..820,824,827,836,838,
                     840,844..845,848..850,852..853,857,860,870,872,874,
                     878..879,882..884,886..887,891,894,903)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          805..836
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          805..834
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          838..870
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          838..868
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          872..903
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          872..901
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          905..936
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          905..934
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          905..907
                     /region_name="Histone H3K9me binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          938..969
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          938..967
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          971..1004
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Site            1004
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          1036..1266
                     /region_name="SET_EHMT1"
                     /note="SET domain (including pre-SET and post-SET domains)
                     found in euchromatic histone-lysine N-methyltransferase 1
                     (EHMT1) and similar proteins; cd10535"
                     /db_xref="CDD:380933"
     Site            1048
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Site            order(1136..1138,1155,1162,1165..1166,1168,1171..1176,
                     1179,1186,1197..1201,1209,1211,1224,1240,1242,1245..1246,
                     1249..1250,1254..1258)
                     /site_type="active"
                     /db_xref="CDD:380933"
     Site            order(1136..1138,1172..1173,1197..1201,1242,1246,
                     1254..1258)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380933"
     Site            1155
                     /site_type="other"
                     /note="Histone H3K9me binding.
                     /evidence=ECO:0000269|PubMed:18264113,
                     ECO:0000269|PubMed:20084102; propagated from
                     UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Site            order(1162,1165..1166,1168,1171,1174,1176,1186,1245..1246,
                     1249..1250)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:380933"
     Region          1162..1181
                     /region_name="Interaction with histone H3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Site            order(1203,1256,1258,1263)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380933"
     Region          1242..1245
                     /region_name="Interaction with histone H3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     Region          1274..1298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9B1.4)"
     CDS             1..1298
                     /gene="EHMT1"
                     /gene_synonym="EHMT1-IT1; Eu-HMTase1; EUHMTASE1; FP13812;
                     GLP; GLP1; KLEFS1; KMT1D"
                     /coded_by="NM_024757.5:25..3921"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7050.2"
                     /db_xref="GeneID:79813"
                     /db_xref="HGNC:HGNC:24650"
                     /db_xref="MIM:607001"
ORIGIN      
        1 maaadaeavp argepqqdcc vktellgeet pmaadegsae kqageahmaa dgetngscen
       61 sdasshanaa khtqdsarvn pqdgtntltr iaengvserd seaakqnhvt addfvqtsvi
      121 gsngyilnkp alqaqplrtt stlasslpgh aaktlpggag kgrtpsafpq tpaappatlg
      181 egsadtedrk lpapgadvkv hrarktmpks vvglhaaskd prevreardh kepkeeinkn
      241 isdfgrqqll ppfpslhqsl pqnqcymatt ksqtaclpfv laaavsrkkk rrmgtyslvp
      301 kkktkvlkqr tviemfksit hstvgskgek dlgasslhvn geslemdsde ddseeleedd
      361 ghgaeqaaaf ptedsrtske smseadraqk mdgeseeeqe svdtgeeeeg gdesdlsses
      421 sikkkflkrk gktdspwikp arkrrrrsrk kpsgalgses ykssagsaeq tapgdstgym
      481 evsldsldlr vkgilssqae glangpdvle tdglqevplc scrmetpksr eittlannqc
      541 matesvdhel grctnsvvky elmrpsnkap llvlcedhrg rmvkhqccpg cgyfctagnf
      601 mecqpessis hrfhkdcasr vnnasycphc geesskakev tiakadttst vtpvpgqekg
      661 salegradtt tgsaagppls eddklqgaas hvpegfdptg paglgrptpg lsqgpgketl
      721 esalialdse kpkklrfhpk qlyfsarqge lqkvllmlvd gidpnfkmeh qnkrsplhaa
      781 aeaghvdich mlvqaganid tcsedqrtpl meaaennhle avkylikaga lvdpkdaegs
      841 tclhlaakkg hyevvqylls ngqmdvncqd dggwtpmiwa teykhvdlvk lllskgsdin
      901 irdneenicl hwaafsgcvd iaeillaakc dlhavnihgd splhiaaren rydcvvlfls
      961 rdsdvtlknk egetplqcas lnsqvwsalq mskalqdsap drpspveriv srdiargyer
     1021 ipipcvnavd sepcpsnyky vsqncvtspm nidrnithlq ycvciddcss sncmcgqlsm
     1081 rcwydkdgrl lpefnmaepp lifecnhacs cwrncrnrvv qnglrarlql yrtrdmgwgv
     1141 rslqdippgt fvceyvgeli sdseadvree dsylfdldnk dgevycidar fygnvsrfin
     1201 hhcepnlvpv rvfmahqdlr fpriaffstr lieageqlgf dygerfwdik gklfscrcgs
     1261 pkcrhssaal aqrqasaaqe aqedglpdts saaaadpl
//
LOCUS       NP_808818                632 aa            linear   PRI 27-APR-2025
DEFINITION  armadillo repeat-containing X-linked protein 2 [Homo sapiens].
ACCESSION   NP_808818
VERSION     NP_808818.1
DBSOURCE    REFSEQ: accession NM_177949.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Wang,T., Zhong,H., Qin,Y., Wei,W., Li,Z., Huang,M. and Luo,X.
  TITLE     ARMCX Family Gene Expression Analysis and Potential Prognostic
            Biomarkers for Prediction of Clinical Outcome in Patients with
            Gastric Carcinoma
  JOURNAL   Biomed Res Int 2020, 3575038 (2020)
   PUBMED   32685472
  REMARK    GeneRIF: ARMCX Family Gene Expression Analysis and Potential
            Prognostic Biomarkers for Prediction of Clinical Outcome in
            Patients with Gastric Carcinoma.
            Erratum:[Biomed Res Int. 2021 Feb 9;2021:3179693. doi:
            10.1155/2021/3179693. PMID: 33644226]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Zeller,C., Dai,W., Steele,N.L., Siddiq,A., Walley,A.J.,
            Wilhelm-Benartzi,C.S., Rizzo,S., van der Zee,A., Plumb,J.A. and
            Brown,R.
  TITLE     Candidate DNA methylation drivers of acquired cisplatin resistance
            in ovarian cancer identified by methylome and expression profiling
  JOURNAL   Oncogene 31 (42), 4567-4576 (2012)
   PUBMED   22249249
  REMARK    GeneRIF: Data indicate that ARMCX2, COL1A1, MDK, MEST and MLH1
            genes acquired methylation in drug-resistant ovarian
            cancer-sustaining (side population) cells.
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Lopez-Domenech,G., Serrat,R., Mirra,S., D'Aniello,S., Somorjai,I.,
            Abad,A., Vitureira,N., Garcia-Arumi,E., Alonso,M.T.,
            Rodriguez-Prados,M., Burgaya,F., Andreu,A.L., Garcia-Sancho,J.,
            Trullas,R., Garcia-Fernandez,J. and Soriano,E.
  TITLE     The Eutherian Armcx genes regulate mitochondrial trafficking in
            neurons and interact with Miro and Trak2
  JOURNAL   Nat Commun 3, 814 (2012)
   PUBMED   22569362
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Winter,E.E. and Ponting,C.P.
  TITLE     Mammalian BEX, WEX and GASP genes: coding and non-coding chimaerism
            sustained by gene conversion events
  JOURNAL   BMC Evol Biol 5, 54 (2005)
   PUBMED   16221301
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 632)
  AUTHORS   Kurochkin,I.V., Yonemitsu,N., Funahashi,S.I. and Nomura,H.
  TITLE     ALEX1, a novel human armadillo repeat protein that is expressed
            differentially in normal tissues and carcinomas
  JOURNAL   Biochem Biophys Res Commun 280 (1), 340-347 (2001)
   PUBMED   11162520
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK291342.1, AC234775.5 and
            BC015926.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein containing a potential
            N-terminal transmembrane domain and multiple armadillo (arm)
            repeats. Proteins containing arm repeats are involved in
            development, maintenance of tissue integrity, and tumorigenesis.
            This gene is located in a cluster of related genes on chromosome X.
            There is a pseudogene for this gene on chromosome 7. Alternative
            splicing in the 5' UTR results in multiple transcript variants
            encoding the same protein. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, and 3 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291342.1, SRR1803611.235778.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356824.9/ ENSP00000349281.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..632
                     /product="armadillo repeat-containing X-linked protein 2"
                     /note="armadillo repeat protein ALEX2; ARM protein lost in
                     epithelial cancers on chromosome X 2"
                     /calculated_mol_wt=65553
     Region          1..6
                     /region_name="Mitochondrion outer membrane (MOM)-targeting
                     sequence. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L311.1)"
     Site            7..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L311.1)"
     Region          26..40
                     /region_name="Mitochondrion outer membrane (MOM)-targeting
                     sequence. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L311.1)"
     Region          <39..>279
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          68..124
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L311.1)"
     Region          160..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L311.1)"
     Region          335..369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L311.1)"
     Region          376..416
                     /region_name="ARM 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L311.1)"
     Region          383..601
                     /region_name="Arm_2"
                     /note="Armadillo-like; pfam04826"
                     /db_xref="CDD:461447"
     Region          391..416
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(405..406,409,412..413,416,446..447,450,453..454,457,
                     485..486,489,491..492,526..527,530,533..534)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          418..457
                     /region_name="ARM 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L311.1)"
     Region          426..458
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          467..492
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          498..537
                     /region_name="ARM 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L311.1)"
     Region          503..535
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..632
                     /gene="ARMCX2"
                     /gene_synonym="ALEX2; GASP9"
                     /coded_by="NM_177949.4:512..2410"
                     /db_xref="CCDS:CCDS14490.1"
                     /db_xref="GeneID:9823"
                     /db_xref="HGNC:HGNC:16869"
                     /db_xref="MIM:300363"
ORIGIN      
        1 msrvrdagcv aagivigaga wycvykytrg rdqtkkrmak pknravagtg araraglrag
       61 ftidlgsgfs pptpvraeae draqdeasal dtvgaeavap aassaeaqsg agsqaqeadg
      121 agvgpkaesv vgaamasaia pppgvtealg aaeapamaga pkvaeaprea etsraavppg
      181 tvvpteaaap tevtegpgva aptkvaeapg vaspteaaea pvpatptgaa aptgaaespg
      241 tsgsprtavv pgtsaakkat pgahtgaipk atsatgavpk gggkgvtrsr nggkgkgkks
      301 kvevdelgmg frpgdgaaaa aaasanggqa flaevpdsee gesgwtdtes dsdsepetqr
      361 rgrgrrpvam qkrpfpyeid eilgvrdlrk vlallqksdd pfiqqvallt lsnnanyscn
      421 qetirklggl piianminkt dphikekalm amnnlsenye nqgrlqvymn kvmddimasn
      481 lnsavqvvgl kfltnmtitn dyqhllvnsi anffrllsqg ggkikveilk ilsnfaenpd
      541 mlkkllstqv pasfsslyns yveseilina ltlfeiiydn lraevfnyre fnkgslfylc
      601 ttsgvcvkki ralanhhdll vkvkviklvn kf
//
LOCUS       NP_001353509             825 aa            linear   PRI 27-APR-2025
DEFINITION  protein O-mannosyl-transferase TMTC3 isoform 4 [Homo sapiens].
ACCESSION   NP_001353509
VERSION     NP_001353509.1
DBSOURCE    REFSEQ: accession NM_001366580.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Yuan,H., Zhao,Z., Guo,Z., Ma,L., Han,J. and Song,Y.
  TITLE     A Novel ER Stress Mediator TMTC3 Promotes Squamous Cell Carcinoma
            Progression by Activating GRP78/PERK Signaling Pathway
  JOURNAL   Int J Biol Sci 18 (13), 4853-4868 (2022)
   PUBMED   35982901
  REMARK    GeneRIF: A Novel ER Stress Mediator TMTC3 Promotes Squamous Cell
            Carcinoma Progression by Activating GRP78/PERK Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Biyik,I., Kalkan,U. and Simsek,S.
  TITLE     The deep infiltrating endometriosis tissue has lower T-cadherin,
            E-cadherin, progesterone receptor and oestrogen receptor than
            endometrioma tissue
  JOURNAL   Taiwan J Obstet Gynecol 60 (6), 1059-1065 (2021)
   PUBMED   34794738
  REMARK    GeneRIF: The deep infiltrating endometriosis tissue has lower
            T-cadherin, E-cadherin, progesterone receptor and oestrogen
            receptor than endometrioma tissue.
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Eisenhaber,B., Sinha,S., Jadalanki,C.K., Shitov,V.A., Tan,Q.W.,
            Sirota,F.L. and Eisenhaber,F.
  TITLE     Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4,
            new O-mannosyltransferases from the GT-C/PMT clan, are rationalized
            as ligand binding sites
  JOURNAL   Biol Direct 16 (1), 4 (2021)
   PUBMED   33436046
  REMARK    GeneRIF: Conserved sequence motifs in human TMTC1, TMTC2, TMTC3,
            and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are
            rationalized as ligand binding sites.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Larsen,I.S.B., Narimatsu,Y., Joshi,H.J., Siukstaite,L.,
            Harrison,O.J., Brasch,J., Goodman,K.M., Hansen,L., Shapiro,L.,
            Honig,B., Vakhrushev,S.Y., Clausen,H. and Halim,A.
  TITLE     Discovery of an O-mannosylation pathway selectively serving
            cadherins and protocadherins
  JOURNAL   Proc Natl Acad Sci U S A 114 (42), 11163-11168 (2017)
   PUBMED   28973932
  REMARK    GeneRIF: O-mannosylation pathway dedicated to cadherins/
            protocadherins orchestrated by the four TMTC1-4 genes
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Jerber,J., Zaki,M.S., Al-Aama,J.Y., Rosti,R.O., Ben-Omran,T.,
            Dikoglu,E., Silhavy,J.L., Caglar,C., Musaev,D., Albrecht,B.,
            Campbell,K.P., Willer,T., Almuriekhi,M., Caglayan,A.O., Vajsar,J.,
            Bilguvar,K., Ogur,G., Abou Jamra,R., Gunel,M. and Gleeson,J.G.
  TITLE     Biallelic Mutations in TMTC3, Encoding a Transmembrane and
            TPR-Containing Protein, Lead to Cobblestone Lissencephaly
  JOURNAL   Am J Hum Genet 99 (5), 1181-1189 (2016)
   PUBMED   27773428
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Goldstein,J.I., Jarskog,L.F., Hilliard,C., Alfirevic,A., Duncan,L.,
            Fourches,D., Huang,H., Lek,M., Neale,B.M., Ripke,S., Shianna,K.,
            Szatkiewicz,J.P., Tropsha,A., van den Oord,E.J., Cascorbi,I.,
            Dettling,M., Gazit,E., Goff,D.C., Holden,A.L., Kelly,D.L.,
            Malhotra,A.K., Nielsen,J., Pirmohamed,M., Rujescu,D., Werge,T.,
            Levy,D.L., Josiassen,R.C., Kennedy,J.L., Lieberman,J.A., Daly,M.J.
            and Sullivan,P.F.
  TITLE     Clozapine-induced agranulocytosis is associated with rare HLA-DQB1
            and HLA-B alleles
  JOURNAL   Nat Commun 5, 4757 (2014)
   PUBMED   25187353
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Yun,E.J. and Vu,T.H.
  TITLE     mSmile is necessary for bronchial smooth muscle and alveolar
            myofibroblast development
  JOURNAL   Anat Rec (Hoboken) 295 (1), 167-176 (2012)
   PUBMED   21956870
  REMARK    GeneRIF: SMILE is a novel transgene specifying both bronchial
            smooth muscle and lung alveolar myofibroblast lineages,
            contributing to the understanding of the biological control of the
            development of these cells.
REFERENCE   8  (residues 1 to 825)
  AUTHORS   Racape,M., Duong Van Huyen,J.P., Danger,R., Giral,M., Bleicher,F.,
            Foucher,Y., Pallier,A., Pilet,P., Tafelmeyer,P., Ashton-Chess,J.,
            Dugast,E., Pettre,S., Charreau,B., Soulillou,J.P. and Brouard,S.
  TITLE     The involvement of SMILE/TMTC3 in endoplasmic reticulum stress
            response
  JOURNAL   PLoS One 6 (5), e19321 (2011)
   PUBMED   21603654
  REMARK    GeneRIF: that SMILE is involved in the endoplasmic reticulum stress
            response, by modulating proteasome activity and XBP-1 transcript
            expression. This function of SMILE may influence immune cell
            behavior in the context of transplantation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091516.8, KF455688.1,
            AC087865.8 and AC127901.6.
            
            Summary: This gene encodes a protein that belongs to the
            transmembrane and tetratricopeptide repeat-containing protein
            family. [provided by RefSeq, May 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.259765.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.32"
     Protein         1..825
                     /product="protein O-mannosyl-transferase TMTC3 isoform 4"
                     /EC_number="2.4.1.109"
                     /note="transmembrane and TPR repeat-containing protein 3;
                     protein O-mannosyl-transferase TMTC3; transmembrane and
                     tetratricopeptide repeat containing 3"
                     /calculated_mol_wt=93542
     Region          169..242
                     /region_name="TMTC_DUF1736"
                     /note="Protein O-mannosyl-transferase TMTC, DUF1736;
                     pfam08409"
                     /db_xref="CDD:462468"
     Region          350..579
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          357..385
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          390..434
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          441..468
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(443..444,447,449,451,475,478..479,482..483,485..486,
                     509,512..513,516..517,520)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          455..710
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          473..503
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          508..536
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          579..607
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          612..642
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          647..676
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          682..710
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..825
                     /gene="TMTC3"
                     /gene_synonym="LIS8; SMILE"
                     /coded_by="NM_001366580.1:260..2737"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:160418"
                     /db_xref="HGNC:HGNC:26899"
                     /db_xref="MIM:617218"
ORIGIN      
        1 msyhllnmif havvsviflk vcklfldnks sviasllfav hpihteavtg vvgraellss
       61 ifflaaflsy trskgpdnsi iwtpialtvf lvavatlcke qgitvvgicc vyevfiaqgy
      121 tlpllcttag qflrgkgsip fsmlqtlvkl ivlmfstlll vvirvqviqs qlpvftrfdn
      181 paavsptptr qltfnyllpv nawlllnpse lccdwtmgti plieslldir nlatftffcf
      241 lgmlgvfsir ysgdssktvl malclmalpf ipasnlffpv gfvvaervly vpsmgfcilv
      301 ahgwqkistk svfkklswic lsmvilthsl ktfhrnwdwe seytlfmsal kvnknnaklw
      361 nnvghalene knferalkyf lqathvqpdd igahmnvgrt yknlnrtkea eesymmaksl
      421 mpqiipgkky aariapnhln vyinlanlir anesrleead qlyrqaismr pdfkqayisr
      481 gelllkmnkp lkakeaylka leldrnnadl wynlaivhie lkepnealkn fnralelnpk
      541 hklalfnsai vmqesgevkl rpearkrlls yineepldan gyfnlgmlam ddkkdneaei
      601 wmkkaiklqa dfrsalfnla llysqtakel kalpileell ryypdhikgl ilkgdilmnq
      661 kkdilgakkc ferilemdps nvqgkhnlcv vyfeekdllk aerclletla lapheeyiqr
      721 hlnivrdkis sssfiepifp tskissvegk kiptesvkei rgesrqtqiv ktsdnksqsk
      781 snkqlgkngd eetphkttkd ikeiekkrva alkrleeier ilnge
//
LOCUS       NP_001353187             110 aa            linear   PRI 27-APR-2025
DEFINITION  protein archease isoform 5 [Homo sapiens].
ACCESSION   NP_001353187 XP_024302400
VERSION     NP_001353187.1
DBSOURCE    REFSEQ: accession NM_001366258.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Mason,C.C., Khorashad,J.S., Tantravahi,S.K., Kelley,T.W.,
            Zabriskie,M.S., Yan,D., Pomicter,A.D., Reynolds,K.R., Eiring,A.M.,
            Kronenberg,Z., Sherman,R.L., Tyner,J.W., Dalley,B.K., Dao,K.H.,
            Yandell,M., Druker,B.J., Gotlib,J., O'Hare,T. and Deininger,M.W.
  TITLE     Age-related mutations and chronic myelomonocytic leukemia
  JOURNAL   Leukemia 30 (4), 906-913 (2016)
   PUBMED   26648538
  REMARK    GeneRIF: ARCH mutation is associated with chronic myelomonocytic
            leukemia.
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Jurkin,J., Henkel,T., Nielsen,A.F., Minnich,M., Popow,J.,
            Kaufmann,T., Heindl,K., Hoffmann,T., Busslinger,M. and Martinez,J.
  TITLE     The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA
            and controls antibody secretion in plasma cells
  JOURNAL   EMBO J 33 (24), 2922-2936 (2014)
   PUBMED   25378478
  REMARK    GeneRIF: RTCB, the catalytic subunit of the tRNA ligase complex,
            and its co-factor archease mediate XBP1 mRNA splicing both in vitro
            and in vivo.
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Popow,J., Jurkin,J., Schleiffer,A. and Martinez,J.
  TITLE     Analysis of orthologous groups reveals archease and DDX1 as tRNA
            splicing factors
  JOURNAL   Nature 511 (7507), 104-107 (2014)
   PUBMED   24870230
  REMARK    GeneRIF: archease (also called ZBTB8OS), a protein of unknown
            function, is required for full activity of the human tRNA ligase
            complex and, in cooperation with DDX1, facilitates the formation of
            an RTCB-guanylate intermediate central to mammalian RNA ligation
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Popow,J., Englert,M., Weitzer,S., Schleiffer,A., Mierzwa,B.,
            Mechtler,K., Trowitzsch,S., Will,C.L., Luhrmann,R., Soll,D. and
            Martinez,J.
  TITLE     HSPC117 is the essential subunit of a human tRNA splicing ligase
            complex
  JOURNAL   Science 331 (6018), 760-764 (2011)
   PUBMED   21311021
REFERENCE   7  (residues 1 to 110)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 110)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2 and AL033529.25.
            
            On Sep 27, 2018 this sequence version replaced XP_024302400.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.27452.1,
                                           ERR3218374.28357.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..110
                     /product="protein archease isoform 5"
                     /note="protein archease; archease-like protein; archease
                     (ARCH); zinc finger and BTB domain-containing opposite
                     strand protein 8"
                     /calculated_mol_wt=12646
     Region          1..110
                     /region_name="Archease"
                     /note="Archease protein family (MTH1598/TM1083);
                     pfam01951"
                     /db_xref="CDD:426527"
     CDS             1..110
                     /gene="ZBTB8OS"
                     /gene_synonym="ARCH; ARCH2"
                     /coded_by="NM_001366258.1:679..1011"
                     /note="isoform 5 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS76134.1"
                     /db_xref="GeneID:339487"
                     /db_xref="HGNC:HGNC:24094"
                     /db_xref="MIM:615891"
ORIGIN      
        1 mamfgymtdt gtveplqtve vetqgddlqs llfhfldewl ykfsadeffi prevkvlsid
       61 qrnfklrsig wgeefslskh pqgtevkait ysamqvynee npevfviidi
//
LOCUS       NP_940873                821 aa            linear   PRI 27-APR-2025
DEFINITION  KN motif and ankyrin repeat domain-containing protein 3 [Homo
            sapiens].
ACCESSION   NP_940873 XP_170882
VERSION     NP_940873.2
DBSOURCE    REFSEQ: accession NM_198471.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Dai,Z., Xie,B., Yang,B., Chen,X., Hu,C. and Chen,Q.
  TITLE     KANK3 mediates the p38 MAPK pathway to regulate the proliferation
            and invasion of lung adenocarcinoma cells
  JOURNAL   Tissue Cell 80, 101974 (2023)
   PUBMED   36463587
  REMARK    GeneRIF: KANK3 mediates the p38 MAPK pathway to regulate the
            proliferation and invasion of lung adenocarcinoma cells.
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Tadijan,A., Samarzija,I., Humphries,J.D., Humphries,M.J. and
            Ambriovic-Ristov,A.
  TITLE     KANK family proteins in cancer
  JOURNAL   Int J Biochem Cell Biol 131, 105903 (2021)
   PUBMED   33309958
  REMARK    GeneRIF: KANK family proteins in cancer.
            Review article
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Kim,I., Kang,J., Gee,H.Y. and Park,J.W.
  TITLE     A novel HIF1AN substrate KANK3 plays a tumor-suppressive role in
            hepatocellular carcinoma
  JOURNAL   Cell Biol Int 42 (3), 303-312 (2018)
   PUBMED   29047187
  REMARK    GeneRIF: Authors identified KANK3 as a new substrate for the oxygen
            sensor hypoxia-inducible factor 1-alpha inhibitor (HIF1AN), which
            hydroxylates HIF-1/2alpha and other ankyrin repeat
            domain-containing proteins at asparagine residues.
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Kakinuma,N., Zhu,Y., Wang,Y., Roy,B.C. and Kiyama,R.
  TITLE     Kank proteins: structure, functions and diseases
  JOURNAL   Cell Mol Life Sci 66 (16), 2651-2659 (2009)
   PUBMED   19554261
  REMARK    Review article
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Zhu,Y., Kakinuma,N., Wang,Y. and Kiyama,R.
  TITLE     Kank proteins: a new family of ankyrin-repeat domain-containing
            proteins
  JOURNAL   Biochim Biophys Acta 1780 (2), 128-133 (2008)
   PUBMED   17996375
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC066124.1.
            
            On Sep 25, 2007 this sequence version replaced NP_940873.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC066124.1, AB284126.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330915.7/ ENSP00000328923.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..821
                     /product="KN motif and ankyrin repeat domain-containing
                     protein 3"
                     /note="ankyrin repeat domain 47; kidney ankyrin
                     repeat-containing protein 3; ankyrin repeat
                     domain-containing protein 47"
                     /calculated_mol_wt=85762
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NY19.2)"
     Region          33..74
                     /region_name="KN_motif"
                     /note="KN motif; pfam12075"
                     /db_xref="CDD:432311"
     Region          <58..586
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          58..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NY19.2)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6NY19.2)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1P7; propagated from
                     UniProtKB/Swiss-Prot (Q6NY19.2)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1P7; propagated from
                     UniProtKB/Swiss-Prot (Q6NY19.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6NY19.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6NY19.2)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6NY19.2)"
     Region          224..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NY19.2)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6NY19.2)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1P7; propagated from
                     UniProtKB/Swiss-Prot (Q6NY19.2)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6NY19.2)"
     Region          385..547
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NY19.2)"
     Region          <597..786
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(622,624,628..629,632..634,636..637,641,644,692,695,
                     697,701..702,705..707,709..710,714,717,726,728,730,
                     734..735,738..740,742..743,747,751,760)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          622..692
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          622..652
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NY19.2)"
     Region          656..690
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NY19.2)"
     Region          695..726
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          695..724
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NY19.2)"
     Region          728..760
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          728..758
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NY19.2)"
     Region          762..785
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NY19.2)"
     Region          784..821
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NY19.2)"
     CDS             1..821
                     /gene="KANK3"
                     /gene_synonym="ANKRD47"
                     /coded_by="NM_198471.3:67..2532"
                     /db_xref="CCDS:CCDS12199.1"
                     /db_xref="GeneID:256949"
                     /db_xref="HGNC:HGNC:24796"
                     /db_xref="MIM:614611"
ORIGIN      
        1 makfalnqnl pdlggprlcp vpaaggarsp sspysvetpy gfhldldflk yieelergpa
       61 arrapgppts rrpraprpgl agarspgawt sseslasddg gapgilsqga psgllmqpls
      121 prapvrnprv ehtlretsrr lelaqthera pspgrgvprs prgsgrsspa pnlapaspgp
      181 aqlqlvreqm aaalrrlrel edqartlpel qeqvralrae karllagraq pepdgeaetr
      241 pdklaqlrrl terlatserg grarasprad spdglaagrs egalqvldge vgsldgtpqt
      301 revaaeavpe treagaqavp etreagveaa petveadawv teallglpaa aerelellra
      361 slehqrgvse llrgrlrele eareaaeeaa agaraqlrea ttqtpwscae kaaqtespae
      421 apsltqessp gsmdgdrava pagilksimk krdgtpgaqp ssgpkslqfv gvlngeyess
      481 ssedasdsdg dsenggaepp gsssgsgdds gggsdsgtpg ppsggdirdp epeaeaepqq
      541 vaqgrcelsp rlreacvalq rqlsrprgva sdggavrlva qewfrvssqr rsqaepvarm
      601 legvrrlgpe llahvvnlad gngntalhys vshgnlaias llldtgacev nrqnragysa
      661 lmlaaltsvr qeeedmavvq rlfcmgdvna kasqtgqtal mlaishgrqd mvatllacga
      721 dvnaqdadga talmcaseyg rldtvrlllt qpgcdpaild negtsalaia leaeqdevaa
      781 llhahlssgq pdtqsesppg sqtatpgege cgdngenpqv q
//
LOCUS       NP_002922                406 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RING1 [Homo sapiens].
ACCESSION   NP_002922
VERSION     NP_002922.2
DBSOURCE    REFSEQ: accession NM_002931.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Ryan,C.W., Regan,S.L., Mills,E.F., McGrath,B.T., Gong,E., Lai,Y.T.,
            Sheingold,J.B., Patel,K., Horowitz,T., Moccia,A., Tsan,Y.C.,
            Srivastava,A. and Bielas,S.L.
  TITLE     RING1 missense variants reveal sensitivity of DNA damage repair to
            H2A monoubiquitination dosage during neurogenesis
  JOURNAL   Nat Commun 15 (1), 7931 (2024)
   PUBMED   39256363
  REMARK    GeneRIF: RING1 missense variants reveal sensitivity of DNA damage
            repair to H2A monoubiquitination dosage during neurogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Szustka,A., Kozal,K. and Krzeslak,A.
  TITLE     RING1 Inhibition Has a Cell-Specific Antitumoral Role by Promoting
            Autophagy in Endometrial Cancer Cells
  JOURNAL   Cell Physiol Biochem 58 (1), 1-13 (2024)
   PUBMED   38219048
  REMARK    GeneRIF: RING1 Inhibition Has a Cell-Specific Antitumoral Role by
            Promoting Autophagy in Endometrial Cancer Cells.
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Liu,D., Guo,Y., Du,Q., Zhu,Y. and Guo,Y.
  TITLE     RING induces cell cycle arrest and apoptosis in human breast cancer
            cells by regulating the HSF1/MT2A axis
  JOURNAL   Exp Cell Res 433 (1), 113795 (2023)
   PUBMED   37797799
  REMARK    GeneRIF: RING induces cell cycle arrest and apoptosis in human
            breast cancer cells by regulating the HSF1/MT2A axis.
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Liang,Q., Wang,S., Zhou,X., Li,Y., Xing,S., Sha,Y., Yang,F.,
            Huang,W., Liu,N., Li,Z., Chen,Y., Xu,Y., Zhu,P., Lan,F. and Sun,N.
  TITLE     Essential role of MESP1-RING1A complex in cardiac differentiation
  JOURNAL   Dev Cell 57 (22), 2533-2549 (2022)
   PUBMED   36413948
  REMARK    GeneRIF: Essential role of MESP1-RING1A complex in cardiac
            differentiation.
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Satijn,D.P. and Otte,A.P.
  TITLE     RING1 interacts with multiple Polycomb-group proteins and displays
            tumorigenic activity
  JOURNAL   Mol Cell Biol 19 (1), 57-68 (1999)
   PUBMED   9858531
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Kikuti,Y.Y., Tamiya,G., Ando,A., Chen,L., Kimura,M., Ferreira,E.,
            Tsuji,K., Trowsdale,J. and Inoko,H.
  TITLE     Physical mapping 220 kb centromeric of the human MHC and DNA
            sequence analysis of the 43-kb segment including the RING1, HKE6,
            and HKE4 genes
  JOURNAL   Genomics 42 (3), 422-435 (1997)
   PUBMED   9205114
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Lovering,R., Hanson,I.M., Borden,K.L., Martin,S., O'Reilly,N.J.,
            Evan,G.I., Rahman,D., Pappin,D.J., Trowsdale,J. and Freemont,P.S.
  TITLE     Identification and preliminary characterization of a protein motif
            related to the zinc finger
  JOURNAL   Proc Natl Acad Sci U S A 90 (6), 2112-2116 (1993)
   PUBMED   7681583
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Hanson,I.M., Poustka,A. and Trowsdale,J.
  TITLE     New genes in the class II region of the human major
            histocompatibility complex
  JOURNAL   Genomics 10 (2), 417-424 (1991)
   PUBMED   1906426
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645940.4, BI259576.1 and
            BC051866.2.
            
            On Aug 20, 2004 this sequence version replaced NP_002922.1.
            
            Summary: This gene belongs to the RING finger family, members of
            which encode proteins characterized by a RING domain, a
            zinc-binding motif related to the zinc finger domain. The gene
            product can bind DNA and can act as a transcriptional repressor. It
            is associated with the multimeric polycomb group protein complex.
            The gene product interacts with the polycomb group proteins BMI1,
            EDR1, and CBX4, and colocalizes with these proteins in large
            nuclear domains. It interacts with the CBX4 protein via its
            glycine-rich C-terminal domain. The gene maps to the HLA class II
            region, where it is contiguous with the RING finger genes FABGL and
            HKE4. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.6253.1,
                                           SRR3476690.734216.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374656.5/ ENSP00000363787.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..406
                     /product="E3 ubiquitin-protein ligase RING1"
                     /EC_number="2.3.2.27"
                     /note="polycomb complex protein RING1; really interesting
                     new gene 1 protein; RING-type E3 ubiquitin transferase
                     RING1"
                     /calculated_mol_wt=42298
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Region          30..234
                     /region_name="Necessary for transcriptional repression.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06587.2)"
     Region          34..110
                     /region_name="RING-HC_RING2"
                     /note="RING finger, HC subclass, found in really
                     interesting new gene 2 protein (RING2) and similar
                     proteins; cd16740"
                     /db_xref="CDD:438398"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            order(45..46,60,62..63,65,67,74,78,82,90,92..95,98..100,
                     102..103,105..106,109..110)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:438398"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Region          148..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06587.2)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Region          201..204
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06587.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Region          230..406
                     /region_name="Necessary for interaction with CBX2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06587.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Region          261..400
                     /region_name="RAWUL_RING1"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in really interesting new gene 1
                     protein (RING1); cd17166"
                     /db_xref="CDD:340686"
     Site            order(263..265,283..286,290,293..295,297..298,301..302,
                     392..394)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:340686"
     Region          309..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06587.2)"
     CDS             1..406
                     /gene="RING1"
                     /gene_synonym="RING1A; RNF1"
                     /coded_by="NM_002931.4:204..1424"
                     /db_xref="CCDS:CCDS34424.1"
                     /db_xref="GeneID:6015"
                     /db_xref="HGNC:HGNC:10018"
                     /db_xref="MIM:602045"
ORIGIN      
        1 mttpanaqna sktwelslye lhrtpqeaim dgteiavspr slhselmcpi cldmlkntmt
       61 tkeclhrfcs dcivtalrsg nkecptcrkk lvskrslrpd pnfdaliski ypsreeyeah
      121 qdrvlirlsr lhnqqalsss ieeglrmqam hraqrvrrpi pgsdqtttms ggegepgege
      181 gdgedvssds apdsapgpap krprgggagg ssvgtggggt ggvgggagse dsgdrggtlg
      241 ggtlgppspp gapsppepgg eielvfrphp llvekgeycq tryvkttgna tvdhlskyla
      301 lrialerrqq qeagepggpg ggasdtggpd gcggegggag ggdgpeepal pslegvsekq
      361 ytiyiapggg afttlngslt lelvnekfwk vsrplelcya ptkdpk
//
LOCUS       NP_060671                400 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 13 isoform a [Homo sapiens].
ACCESSION   NP_060671
VERSION     NP_060671.3
DBSOURCE    REFSEQ: accession NM_018201.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Shin,S.Y., Fauman,E.B., Petersen,A.K., Krumsiek,J., Santos,R.,
            Huang,J., Arnold,M., Erte,I., Forgetta,V., Yang,T.P., Walter,K.,
            Menni,C., Chen,L., Vasquez,L., Valdes,A.M., Hyde,C.L., Wang,V.,
            Ziemek,D., Roberts,P., Xi,L., Grundberg,E., Waldenberger,M.,
            Richards,J.B., Mohney,R.P., Milburn,M.V., John,S.L., Trimmer,J.,
            Theis,F.J., Overington,J.P., Suhre,K., Brosnan,M.J., Gieger,C.,
            Kastenmuller,G., Spector,T.D. and Soranzo,N.
  CONSRTM   Multiple Tissue Human Expression Resource (MuTHER) Consortium
  TITLE     An atlas of genetic influences on human blood metabolites
  JOURNAL   Nat Genet 46 (6), 543-550 (2014)
   PUBMED   24816252
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Davey,J.R., Humphrey,S.J., Junutula,J.R., Mishra,A.K.,
            Lambright,D.G., James,D.E. and Stockli,J.
  TITLE     TBC1D13 is a RAB35 specific GAP that plays an important role in
            GLUT4 trafficking in adipocytes
  JOURNAL   Traffic 13 (10), 1429-1441 (2012)
   PUBMED   22762500
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL441992.17.
            
            On Jun 11, 2008 this sequence version replaced NP_060671.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.149220.1,
                                           SRR1660807.66384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372648.10/ ENSP00000361731.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..400
                     /product="TBC1 domain family member 13 isoform a"
                     /note="epididymis secretory sperm binding protein"
                     /calculated_mol_wt=46423
     Region          32..367
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..400
                     /gene="TBC1D13"
                     /coded_by="NM_018201.5:102..1304"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6911.1"
                     /db_xref="GeneID:54662"
                     /db_xref="HGNC:HGNC:25571"
                     /db_xref="MIM:616218"
ORIGIN      
        1 msslhksria dfqdvlkeps ialeklrels fsgipceggl rclcwkilln ylpleraswt
       61 silakqrely aqflremiiq pgiakanmgv sredvtfedh plnpnpdsrw ntyfkdnevl
      121 lqidkdvrrl cpdisffqra tdypcllild pqnefetlrk rveqttlksq tvarnrsgvt
      181 nmssphknsv psslneyevl pngceahwev verilfiyak lnpgiayvqg mneivgplyy
      241 tfatdpnsew kehaeadtff cftnlmaeir dnfiksldds qcgitykmek vystlkdkdv
      301 elylklqeqn ikpqffafrw ltlllsqefl lpdviriwds lfaddnrfdf lllvccamlm
      361 lireqllegd ftvnmrllqd ypitdvcqil qkakelqdsk
//
LOCUS       NP_005870                469 aa            linear   PRI 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRAIP [Homo sapiens].
ACCESSION   NP_005870
VERSION     NP_005870.2
DBSOURCE    REFSEQ: accession NM_005879.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Gu,Y. and Liang,C.
  TITLE     TRAIP suppressed apoptosis and cell cycle to promote prostate
            cancer proliferation via TRAF2-PI3K-AKT pathway activation
  JOURNAL   Int Urol Nephrol 56 (5), 1639-1648 (2024)
   PUBMED   38100027
  REMARK    GeneRIF: TRAIP suppressed apoptosis and cell cycle to promote
            prostate cancer proliferation via TRAF2-PI3K-AKT pathway
            activation.
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Scaramuzza,S., Jones,R.M., Sadurni,M.M., Reynolds-Winczura,A.,
            Poovathumkadavil,D., Farrell,A., Natsume,T., Rojas,P., Cuesta,C.F.,
            Kanemaki,M.T., Saponaro,M. and Gambus,A.
  TITLE     TRAIP resolves DNA replication-transcription conflicts during the
            S-phase of unperturbed cells
  JOURNAL   Nat Commun 14 (1), 5071 (2023)
   PUBMED   37604812
  REMARK    GeneRIF: TRAIP resolves DNA replication-transcription conflicts
            during the S-phase of unperturbed cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Chung,H.J., Lee,J.R., Kim,T.M., Kim,S., Park,K., Kim,M.J., Jung,E.,
            Kim,S., Lee,E.A., Ra,J.S., Hwang,S., Lee,J.Y., Scharer,O.D.,
            Kim,Y., Myung,K. and Kim,H.
  TITLE     ZNF212 promotes genomic integrity through direct interaction with
            TRAIP
  JOURNAL   Nucleic Acids Res 51 (2), 631-649 (2023)
   PUBMED   36594163
  REMARK    GeneRIF: ZNF212 promotes genomic integrity through direct
            interaction with TRAIP.
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Zheng,Y., Jia,H., Wang,P., Liu,L., Chen,Z., Xing,X., Wang,J.,
            Tan,X. and Wang,C.
  TITLE     Silencing TRAIP suppresses cell proliferation and
            migration/invasion of triple negative breast cancer via RB-E2F
            signaling and EMT
  JOURNAL   Cancer Gene Ther 30 (1), 74-84 (2023)
   PUBMED   36064576
  REMARK    GeneRIF: Silencing TRAIP suppresses cell proliferation and
            migration/invasion of triple negative breast cancer via RB-E2F
            signaling and EMT.
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Li,M., Wu,W., Deng,S., Shao,Z. and Jin,X.
  TITLE     TRAIP modulates the IGFBP3/AKT pathway to enhance the invasion and
            proliferation of osteosarcoma by promoting KANK1 degradation
  JOURNAL   Cell Death Dis 12 (8), 767 (2021)
   PUBMED   34349117
  REMARK    GeneRIF: TRAIP modulates the IGFBP3/AKT pathway to enhance the
            invasion and proliferation of osteosarcoma by promoting KANK1
            degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 469)
  AUTHORS   Besse,A., Campos,A.D., Webster,W.K. and Darnay,B.G.
  TITLE     TRAF-interacting protein (TRIP) is a RING-dependent ubiquitin
            ligase
  JOURNAL   Biochem Biophys Res Commun 359 (3), 660-664 (2007)
   PUBMED   17544371
REFERENCE   7  (residues 1 to 469)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   8  (residues 1 to 469)
  AUTHORS   Regamey,A., Hohl,D., Liu,J.W., Roger,T., Kogerman,P., Toftgard,R.
            and Huber,M.
  TITLE     The tumor suppressor CYLD interacts with TRIP and regulates
            negatively nuclear factor kappaB activation by tumor necrosis
            factor
  JOURNAL   J Exp Med 198 (12), 1959-1964 (2003)
   PUBMED   14676304
  REMARK    GeneRIF: CYLD interacts with TRIP and regulates negatively nuclear
            factor kappaB activation by tumor necrosis factor.
REFERENCE   9  (residues 1 to 469)
  AUTHORS   Wilson,S.A., Brown,E.C., Kingsman,A.J. and Kingsman,S.M.
  TITLE     TRIP: a novel double stranded RNA binding protein which interacts
            with the leucine rich repeat of flightless I
  JOURNAL   Nucleic Acids Res 26 (15), 3460-3467 (1998)
   PUBMED   9671805
REFERENCE   10 (residues 1 to 469)
  AUTHORS   Lee,S.Y., Lee,S.Y. and Choi,Y.
  TITLE     TRAF-interacting protein (TRIP): a novel component of the tumor
            necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes
            that inhibits TRAF2-mediated NF-kappaB activation
  JOURNAL   J Exp Med 185 (7), 1275-1285 (1997)
   PUBMED   9104814
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139451.7, BX473682.1,
            BC019283.1 and BQ446539.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 13, 2004 this sequence version replaced NP_005870.1.
            
            Summary: This gene encodes a protein that contains an N-terminal
            RING finger motif and a putative coiled-coil domain. A similar
            murine protein interacts with TNFR-associated factor 1 (TRAF1),
            TNFR-associated factor 2 (TRAF2), and cylindromatosis. The
            interaction with TRAF2 inhibits TRAF2-mediated nuclear factor
            kappa-B, subunit 1 activation that is required for cell activation
            and protection against apoptosis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.268051.1, U77845.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331456.7/ ENSP00000328203.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..469
                     /product="E3 ubiquitin-protein ligase TRAIP"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 206; RING-type E3 ubiquitin
                     transferase TRAIP"
                     /calculated_mol_wt=53163
     Region          6..50
                     /region_name="RING-H2_TRAIP"
                     /note="RING finger, H2 subclass, found in TRAF-interacting
                     protein (TRAIP) and similar proteins; cd16480"
                     /db_xref="CDD:438143"
     Region          65..>278
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          211..469
                     /region_name="Interaction with CYLD.
                     /evidence=ECO:0000269|PubMed:14676304"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BWF2.1)"
     Region          460..469
                     /region_name="PIP-box.
                     /evidence=ECO:0000269|PubMed:26711499"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BWF2.1)"
     CDS             1..469
                     /gene="TRAIP"
                     /gene_synonym="RNF206; SCKL9; TRIP"
                     /coded_by="NM_005879.3:112..1521"
                     /db_xref="CCDS:CCDS2806.1"
                     /db_xref="GeneID:10293"
                     /db_xref="HGNC:HGNC:30764"
                     /db_xref="MIM:605958"
ORIGIN      
        1 mpiralctic sdffdhsrdv aaihcghtfh lqcliqwfet apsrtcpqcr iqvgkrtiin
       61 klffdlaqee envldaeflk neldnvraql sqkdkekrds qviidtlrdt leernatvvs
      121 lqqalgkaem lcstlkkqmk yleqqqdetk qaqeearrlr skmktmeqie lllqsqrpev
      181 eemirdmgvg qsaveqlavy cvslkkeyen lkearkasge vadklrkdlf ssrsklqtvy
      241 seldqaklel ksaqkdlqsa dkeimslkkk ltmlqetlnl ppvasetvdr lvlespapve
      301 vnlklrrpsf rddidlnatf dvdtpparps ssqhgyyekl clekshspiq dvpkkickgp
      361 rkesqlslgg qscagepdee lvgafpifvr nailgqkqpk rprsesscsk dvvrtgfdgl
      421 ggrtkfiqpt dtvmirplpv kpktkvkqrv rvktvpslfq akldtflws
//
LOCUS       NP_002585                638 aa            linear   PRI 27-APR-2025
DEFINITION  neuroendocrine convertase 2 isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_002585
VERSION     NP_002585.2
DBSOURCE    REFSEQ: accession NM_002594.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Remes,S.M., Leijon,H., Vesterinen,T., Louhimo,J., Pulkkinen,V.,
            Ezer,S., Kere,J., Haglund,C. and Arola,J.
  TITLE     PCSK2 expression in neuroendocrine tumors points to a midgut,
            pulmonary, or pheochromocytoma-paraganglioma origin
  JOURNAL   APMIS 128 (11), 563-572 (2020)
   PUBMED   32794589
  REMARK    GeneRIF: PCSK2 expression in neuroendocrine tumors points to a
            midgut, pulmonary, or pheochromocytoma-paraganglioma origin.
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Fujimaki,T., Kato,K., Yokoi,K., Oguri,M., Yoshida,T., Watanabe,S.,
            Metoki,N., Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y., Kimura,G.
            and Yamada,Y.
  TITLE     Association of genetic variants in SEMA3F, CLEC16A, LAMA3, and
            PCSK2 with myocardial infarction in Japanese individuals
  JOURNAL   Atherosclerosis 210 (2), 468-473 (2010)
   PUBMED   20036365
  REMARK    GeneRIF: SEMA3F, CLEC16A, LAMA3, and PCSK2 variants have roles in
            myocardial infarction in Japanese individuals
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Leak,T.S., Keene,K.L., Langefeld,C.D., Gallagher,C.J.,
            Mychaleckyj,J.C., Freedman,B.I., Bowden,D.W., Rich,S.S. and
            Sale,M.M.
  TITLE     Association of the proprotein convertase subtilisin/kexin-type 2
            (PCSK2) gene with type 2 diabetes in an African American population
  JOURNAL   Mol Genet Metab 92 (1-2), 145-150 (2007)
   PUBMED   17618154
  REMARK    GeneRIF: Single nucleotide polymorphisms in PCSK2 is associated
            with type 2 diabetes
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Taylor,N.A., Shennan,K.I., Cutler,D.F. and Docherty,K.
  TITLE     Mutations within the propeptide, the primary cleavage site or the
            catalytic site, or deletion of C-terminal sequences, prevents
            secretion of proPC2 from transfected COS-7 cells
  JOURNAL   Biochem J 321 (Pt 2) (Pt 2), 367-373 (1997)
   PUBMED   9020868
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Bailyes,E.M., Shennan,K.I., Usac,E.F., Arden,S.D., Guest,P.C.,
            Docherty,K. and Hutton,J.C.
  TITLE     Differences between the catalytic properties of recombinant human
            PC2 and endogenous rat PC2
  JOURNAL   Biochem J 309 (Pt 2) (Pt 2), 587-594 (1995)
   PUBMED   7626024
REFERENCE   7  (residues 1 to 638)
  AUTHORS   Ohagi,S., LaMendola,J., LeBeau,M.M., Espinosa,R. 3rd, Takeda,J.,
            Smeekens,S.P., Chan,S.J. and Steiner,D.F.
  TITLE     Identification and analysis of the gene encoding human PC2, a
            prohormone convertase expressed in neuroendocrine tissues
  JOURNAL   Proc Natl Acad Sci U S A 89 (11), 4977-4981 (1992)
   PUBMED   1594602
REFERENCE   8  (residues 1 to 638)
  AUTHORS   Seidah,N.G., Mattei,M.G., Gaspar,L., Benjannet,S., Mbikay,M. and
            Chretien,M.
  TITLE     Chromosomal assignments of the genes for neuroendocrine convertase
            PC1 (NEC1) to human 5q15-21, neuroendocrine convertase PC2 (NEC2)
            to human 20p11.1-11.2, and furin (mouse 7[D1-E2] region)
  JOURNAL   Genomics 11 (1), 103-107 (1991)
   PUBMED   1765368
REFERENCE   9  (residues 1 to 638)
  AUTHORS   Smeekens,S.P. and Steiner,D.F.
  TITLE     Identification of a human insulinoma cDNA encoding a novel
            mammalian protein structurally related to the yeast dibasic
            processing protease Kex2
  JOURNAL   J Biol Chem 265 (6), 2997-3000 (1990)
   PUBMED   2154467
REFERENCE   10 (residues 1 to 638)
  AUTHORS   Sanke,T., Bell,G.I., Sample,C., Rubenstein,A.H. and Steiner,D.F.
  TITLE     An islet amyloid peptide is derived from an 89-amino acid precursor
            by proteolytic processing
  JOURNAL   J Biol Chem 263 (33), 17243-17246 (1988)
   PUBMED   3053705
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY137524.1, BC001905.1,
            BC005815.2, BC040546.1, DA148468.1, CD519990.1 and BP384064.1.
            
            On Apr 28, 2002 this sequence version replaced NP_002585.1.
            
            Summary: This gene encodes a member of the subtilisin-like
            proprotein convertase family, which includes proteases that process
            protein and peptide precursors trafficking through regulated or
            constitutive branches of the secretory pathway. The protein
            undergoes an initial autocatalytic processing event and interacts
            with a neuroendocrine secretory protein in the ER, exits the ER and
            sorts to secretory granules, where it is cleaved and catalytically
            activated during intracellular transport. The encoded protease is
            packaged into and activated in dense core secretory granules and
            expressed in the neuroendocrine system and brain. This gene encodes
            one of the seven basic amino acid-specific members which cleave
            their substrates at single or paired basic residues. It functions
            in the proteolytic activation of polypeptide hormones and
            neuropeptides precursors. Single nucleotide polymorphisms in this
            gene may increase susceptibility to myocardial infarction and type
            2 diabetes. This gene may also play a role in tumor development and
            progression. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Jan 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.72025.1,
                                           SRR1660809.4612.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262545.7/ ENSP00000262545.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.1"
     Protein         1..638
                     /product="neuroendocrine convertase 2 isoform 1
                     preproprotein"
                     /EC_number="3.4.21.94"
                     /note="prohormone convertase 2; neuroendocrine convertase
                     2; KEX2-like endoprotease 2"
                     /calculated_mol_wt=67973
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2610
     proprotein      26..638
                     /product="neuroendocrine convertase 2 isoform 1
                     proprotein"
                     /calculated_mol_wt=67973
     Region          33..109
                     /region_name="S8_pro-domain"
                     /note="Peptidase S8 pro-domain; pfam16470"
                     /db_xref="CDD:465126"
     mat_peptide     110..638
                     /product="Neuroendocrine convertase 2. /id=PRO_0000027066"
                     /note="propagated from UniProtKB/Swiss-Prot (P16519.2)"
                     /calculated_mol_wt=58062
     Region          122..418
                     /region_name="Peptidases_S8_Protein_convertases_Kexins_Fur
                     in-lik"
                     /note="Peptidase S8 family domain in Protein convertases;
                     cd04059"
                     /db_xref="CDD:173789"
     Site            order(123,176,222)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173789"
     Site            order(167..168,205,208,251,269,279,310,320,384)
                     /site_type="active"
                     /db_xref="CDD:173789"
     Site            order(167,208,384)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173789"
     Site            order(315,345)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173789"
     Site            order(323,325,328,330)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:173789"
     Site            375
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16519.2)"
     Region          504..591
                     /region_name="P_proprotein"
                     /note="Proprotein convertase P-domain; pfam01483"
                     /db_xref="CDD:460225"
     Site            514
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16519.2)"
     Site            524
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16519.2)"
     CDS             1..638
                     /gene="PCSK2"
                     /gene_synonym="NEC 2; NEC-2; NEC2; PC2; SPC2"
                     /coded_by="NM_002594.5:267..2183"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS13125.1"
                     /db_xref="GeneID:5126"
                     /db_xref="HGNC:HGNC:8744"
                     /db_xref="MIM:162151"
ORIGIN      
        1 mkggcvsqwk aaagflfcvm vfasaerpvf tnhflvelhk ggedkarqva aehgfgvrkl
       61 pfaeglyhfy hnglakakrr rslhhkqqle rdprvkmalq qegfdrkkrg yrdineidin
      121 mndplftkqw ylintgqadg tpgldlnvae awelgytgkg vtigimddgi dylhpdlasn
      181 ynaeasydfs sndpypypry tddwfnshgt rcagevsaaa nnnicgvgva ynskvagirm
      241 ldqpfmtdii eassishmpq lidiysaswg ptdngktvdg preltlqama dgvnkgrggk
      301 gsiyvwasgd ggsyddcncd gyassmwtis insaindgrt alydescsst lastfsngrk
      361 rnpeagvatt dlygnctlrh sgtsaaapea agvfalalea nlgltwrdmq hltvltskrn
      421 qlhdevhqwr rngvglefnh lfgygvldag amvkmakdwk tvperfhcvg gsvqdpekip
      481 stgklvltlt tdacegkenf vrylehvqav itvnatrrgd lninmtspmg tksillsrrp
      541 rdddskvgfd kwpfmtthtw gedargtwtl elgfvgsapq kgvlkewtlm lhgtqsapyi
      601 dqvvrdyqsk lamskkeele eeldeavers lksilnkn
//
LOCUS       NP_005667                930 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding protein 10 isoform 1 [Homo sapiens].
ACCESSION   NP_005667
VERSION     NP_005667.2
DBSOURCE    REFSEQ: accession NM_005676.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Chang,J., Zhang,Y., Zhou,T., Qiao,Q., Shan,J., Chen,Y., Jiang,W.,
            Wang,Y., Liu,S., Wang,Y., Yu,Y., Li,C. and Li,X.
  TITLE     RBM10 C761Y mutation induced oncogenic ASPM isoforms and regulated
            beta-catenin signaling in cholangiocarcinoma
  JOURNAL   J Exp Clin Cancer Res 43 (1), 104 (2024)
   PUBMED   38576051
  REMARK    GeneRIF: RBM10 C761Y mutation induced oncogenic ASPM isoforms and
            regulated beta-catenin signaling in cholangiocarcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Li,Y., Wei,D., Chen,Z., Chen,Y., Deng,Y., Li,M., Zhao,Y. and Niu,K.
  TITLE     RBM10 regulates the tumorigenic potential of human cancer cells by
            modulating PPM1B and YBX1 activities
  JOURNAL   Exp Cell Res 435 (2), 113932 (2024)
   PUBMED   38246397
  REMARK    GeneRIF: RBM10 regulates the tumorigenic potential of human cancer
            cells by modulating PPM1B and YBX1 activities.
REFERENCE   3  (residues 1 to 930)
  AUTHORS   Tripathi,S., Sengar,S., Shree,B., Mohapatra,S., Basu,A. and
            Sharma,V.
  TITLE     An RBM10 and NF-kappaB interacting host lncRNA promotes JEV
            replication and neuronal cell death
  JOURNAL   J Virol 97 (12), e0118323 (2023)
   PUBMED   37991381
  REMARK    GeneRIF: An RBM10 and NF-kappaB interacting host lncRNA promotes
            JEV replication and neuronal cell death.
REFERENCE   4  (residues 1 to 930)
  AUTHORS   Lee,H., Jung,J.H., Ko,H.M., Park,H., Segall,A.M., Sheffmaker,R.L.,
            Wang,J., Frey,W.D., Pham,N., Wang,Y., Zhang,Y., Jackson,J.G.,
            Zeng,S.X. and Lu,H.
  TITLE     RNA-binding motif protein 10 inactivates c-Myc by partnering with
            ribosomal proteins uL18 and uL5
  JOURNAL   Proc Natl Acad Sci U S A 120 (49), e2308292120 (2023)
   PUBMED   38032932
  REMARK    GeneRIF: RNA-binding motif protein 10 inactivates c-Myc by
            partnering with ribosomal proteins uL18 and uL5.
REFERENCE   5  (residues 1 to 930)
  AUTHORS   Cao,Y., Di,X., Cong,S., Tian,C., Wang,Y., Jin,X., Zhao,M., Zhou,X.,
            Li,R. and Wang,K.
  TITLE     RBM10 recruits METTL3 to induce N6-methyladenosine-MALAT1-dependent
            modification, inhibiting the invasion and migration of NSCLC
  JOURNAL   Life Sci 315, 121359 (2023)
   PUBMED   36608868
  REMARK    GeneRIF: RBM10 recruits METTL3 to induce
            N6-methyladenosine-MALAT1-dependent modification, inhibiting the
            invasion and migration of NSCLC.
REFERENCE   6  (residues 1 to 930)
  AUTHORS   Martinez-Arribas,F., Agudo,D., Pollan,M., Gomez-Esquer,F.,
            Diaz-Gil,G., Lucas,R. and Schneider,J.
  TITLE     Positive correlation between the expression of X-chromosome RBM
            genes (RBMX, RBM3, RBM10) and the proapoptotic Bax gene in human
            breast cancer
  JOURNAL   J Cell Biochem 97 (6), 1275-1282 (2006)
   PUBMED   16552754
  REMARK    GeneRIF: From these results, it seems that the X-chromosome,
            through its RBM genes, plays a formerly unknown role in the
            regulation of programmed cell death (apoptosis) in breast cancer.
REFERENCE   7  (residues 1 to 930)
  AUTHORS   Thiselton,D.L., McDowall,J., Brandau,O., Ramser,J., d'Esposito,F.,
            Bhattacharya,S.S., Ross,M.T., Hardcastle,A.J. and Meindl,A.
  TITLE     An integrated, functionally annotated gene map of the DXS8026-ELK1
            interval on human Xp11.3-Xp11.23: potential hotspot for
            neurogenetic disorders
  JOURNAL   Genomics 79 (4), 560-572 (2002)
   PUBMED   11944989
  REMARK    Erratum:[Genomics 2002 Jun;79(6):891]
REFERENCE   8  (residues 1 to 930)
  AUTHORS   Inoue,A., Takahashi,K.P., Kimura,M., Watanabe,T. and Morisawa,S.
  TITLE     Molecular cloning of a RNA binding protein, S1-1
  JOURNAL   Nucleic Acids Res 24 (15), 2990-2997 (1996)
   PUBMED   8760884
REFERENCE   9  (residues 1 to 930)
  AUTHORS   Coleman,M.P., Ambrose,H.J., Carrel,L., Nemeth,A.H., Willard,H.F.
            and Davies,K.E.
  TITLE     A novel gene, DXS8237E, lies within 20 kb upstream of UBE1 in
            Xp11.23 and has a different X inactivation status
  JOURNAL   Genomics 31 (1), 135-138 (1996)
   PUBMED   8808293
REFERENCE   10 (residues 1 to 930)
  AUTHORS   Gorlin,R.J., Cervenka,J., Anderson,R.C., Sauk,J.J. and Bevis,W.D.
  TITLE     Robin's syndrome. A probably X-linked recessive subvariety
            exhibiting persistence of left superior vena cava and atrial septal
            defect
  JOURNAL   Am J Dis Child 119 (2), 176-178 (1970)
   PUBMED   5410571
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB183041.1, BC008733.2 and
            AW248804.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 10, 2002 this sequence version replaced NP_005667.1.
            
            Summary: This gene encodes a nuclear protein that belongs to a
            family proteins that contain an RNA-binding motif. The encoded
            protein associates with hnRNP proteins and may be involved in
            regulating alternative splicing. Defects in this gene are the cause
            of the X-linked recessive disorder, TARP syndrome. Alternate
            splicing results in multiple transcript variants.[provided by
            RefSeq, Mar 2011].
            
            Transcript Variant: This variant (1) encodes isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004181.2, BC008733.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377604.8/ ENSP00000366829.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.3"
     Protein         1..930
                     /product="RNA-binding protein 10 isoform 1"
                     /note="RNA-binding protein S1-1; g patch domain-containing
                     protein 9; epididymis secretory sperm binding protein;
                     G-patch domain containing 9; zinc finger RANBP2-type
                     containing 5"
                     /calculated_mol_wt=103402
     Region          1..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P98175.3)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P98175.3)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Region          128..211
                     /region_name="RRM1_RBM10"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     RNA-binding protein 10 (RBM10); cd12753"
                     /db_xref="CDD:410147"
     Region          215..239
                     /region_name="ZnF_RBZ"
                     /note="Zinc finger domain; smart00547"
                     /db_xref="CDD:197784"
     Region          217..236
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     Region          298..384
                     /region_name="RRM2_RBM10"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     RNA-binding protein 10 (RBM10); cd12754"
                     /db_xref="CDD:410148"
     Site            383
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P98175.3)"
     Region          466..524
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Region          537..569
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Region          564..627
                     /region_name="OCRE_RBM10"
                     /note="OCRE domain found in RNA-binding protein 10 (RBM10)
                     and similar proteins; cd16167"
                     /db_xref="CDD:293886"
     Region          570..577
                     /region_name="OCRE repeat 1"
                     /note="OCRE repeat 1 [structural motif]"
                     /db_xref="CDD:293886"
     Region          578..585
                     /region_name="OCRE repeat 2"
                     /note="OCRE repeat 2 [structural motif]"
                     /db_xref="CDD:293886"
     Region          586..593
                     /region_name="OCRE repeat 3"
                     /note="OCRE repeat 3 [structural motif]"
                     /db_xref="CDD:293886"
     Region          594..601
                     /region_name="OCRE repeat 4"
                     /note="OCRE repeat 4 [structural motif]"
                     /db_xref="CDD:293886"
     Region          603..610
                     /region_name="OCRE repeat 5"
                     /note="OCRE repeat 5 [structural motif]"
                     /db_xref="CDD:293886"
     Region          620..685
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Region          700..753
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Site            723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P98175.3)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P98175.3)"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P98175.3)"
     Site            781
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P98175.3)"
     Site            797
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Region          815..861
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98175.3)"
     Site            845
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P98175.3)"
     Region          858..902
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     Site            902
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P98175.3)"
     CDS             1..930
                     /gene="RBM10"
                     /gene_synonym="DXS8237E; GPATC9; GPATCH9; MINAS-60; S1-1;
                     TARPS; ZRANB5"
                     /coded_by="NM_005676.5:391..3183"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14274.1"
                     /db_xref="GeneID:8241"
                     /db_xref="HGNC:HGNC:9896"
                     /db_xref="MIM:300080"
ORIGIN      
        1 meyerrggrg drtgrygatd rsqddggenr srdhdyrdmd yrsypreygs qegkhdydds
       61 seeqsaedsy easpgsetqr rrrrrhrhsp tgppgfprdg dyrdqdyrte qgeeeeeeed
      121 eeeeekasni vmlrmlpqaa teddirgqlq shgvqarevr lmrnkssgqs rgfafvefsh
      181 lqdatrwmea nqhslnilgq kvsmhysdpk pkinedwlcn kcgvqnfkrr ekcfkcgvpk
      241 seaeqklplg trldqqtlpl ggrelsqgll plpqpyqaqg vlasqalsqg sepssenand
      301 tiilrnlnph stmdsilgal apyavlsssn vrvikdkqtq lnrgfafiql stiveaaqll
      361 qilqalhppl tidgktinve fakgskrdma snegsrisaa svastaiaaa qwaisqasqg
      421 gegtwatsee ppvdysyyqq degygnsqgt esslyahgyl kgtkgpgitg tkgdptgagp
      481 easlepgads vsmqafsraq pgaapgiyqq saeasssqgt aansqsytim spavlkselq
      541 spthpssalp patsptaqes ysqypvpdvs tyqydetsgy yydpqtglyy dpnsqyyyna
      601 qsqqylywdg errtyvpale qsadghketg apskegkekk ekhktktaqq iakdmerwar
      661 slnkqkenfk nsfqpisslr dderresata dagyailekk galaerqhts mdlpklasdd
      721 rpspprglva aysgesdsee eqerggpere ekltdwqkla cllcrrqfps kealirhqql
      781 sglhkqnlei hrrahlsene lealekndme qmkyrdraae rrekygipep pepkrrkygg
      841 istasvdfeq ptrdglgsdn igsrmlqamg wkegsglgrk kqgivtpiea qtrvrgsglg
      901 argssygvts tesyketlhk tmvtrfneaq
//
LOCUS       NP_001307108             526 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 69 homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001307108 XP_006710670
VERSION     NP_001307108.1
DBSOURCE    REFSEQ: accession NM_001320179.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Scherneck,S., Nestler,M., Vogel,H., Bluher,M., Block,M.D., Berriel
            Diaz,M., Herzig,S., Schulz,N., Teichert,M., Tischer,S.,
            Al-Hasani,H., Kluge,R., Schurmann,A. and Joost,H.G.
  TITLE     Positional cloning of zinc finger domain transcription factor
            Zfp69, a candidate gene for obesity-associated diabetes contributed
            by mouse locus Nidd/SJL
  JOURNAL   PLoS Genet 5 (7), e1000541 (2009)
   PUBMED   19578398
  REMARK    GeneRIF: Zfp69 is the most likely candidate for the diabetogenic
            effect of Nidd/SJL locus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL603839.9, BC041873.1, AK122618.1 and BM677727.1.
            
            On Feb 13, 2016 this sequence version replaced XP_006710670.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and uses
            an alternate in-frame splice site in the 5' coding region, compared
            to variant 1. It encodes isoform 2, which is shorter than isoform 1
            by a single amino acid. Variants 2 and 3 encode the same isoform
            (2).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC041873.1, SRR1660803.62440.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372706.6/ ENSP00000361791.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..526
                     /product="zinc finger protein 69 homolog isoform 2"
                     /note="zinc finger protein 642; ZFP69 zinc finger protein
                     A; zinc finger protein ZFP69; zinc finger protein 69
                     homolog"
                     /calculated_mol_wt=61050
     Region          <3..66
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          76..136
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <232..515
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(278,280,282,284..285,288..289,292,306,308,312..313,
                     316..317,320,334,336,338,340..341,344..345,348)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          301..321
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          329..349
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          385..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..526
                     /gene="ZFP69"
                     /gene_synonym="ZFP69A; ZKSCAN23A; ZNF642; ZSCAN54A"
                     /coded_by="NM_001320179.2:932..2512"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS30686.1"
                     /db_xref="GeneID:339559"
                     /db_xref="HGNC:HGNC:24708"
                     /db_xref="MIM:617939"
ORIGIN      
        1 mpqqllitlp teastwvklq hpkkavegap lwedvtkmfe geallsqdae dvktqresle
       61 devtpglpta esqelltfkd isidftqeew gqlapahqnl yrevmlenys nlvsvgyqls
      121 kpsvisqlek geepwmaeke gpgdpssdlk skietiesta kstisqerly hgimmesfmr
      181 ddiiystlrk vstyddvler hqetcmrdvr qailthkkrv qetnkfgeni ivhsnviieq
      241 rhhkydtptk rntykldlin hptsyirtkt yecnicekif kqpihltehm rihtgekpfr
      301 ckecgrafsq saslsthqri htgekpfece ecgkafrhrs slnqhhrtht gekpyvcdkc
      361 qkafsqnisl vqhlrthsge kpftcnecgk tfrqirhlse hirihtgekp yactaccktf
      421 shraylthhq rihtgerpyk ckecgkafrq rihlsnhktv htgvkayecn rcgkayrhds
      481 sfkkhqrhht gekpyecnec gkafsynssl srhheihrrn afrnkv
//
LOCUS       NP_057030                385 aa            linear   PRI 27-APR-2025
DEFINITION  protein pelota homolog [Homo sapiens].
ACCESSION   NP_057030 NP_054819 XP_005248600
VERSION     NP_057030.3
DBSOURCE    REFSEQ: accession NM_015946.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Wu,X., Yang,Z.H., Wu,J. and Han,J.
  TITLE     Ribosome-rescuer PELO catalyzes the oligomeric assembly of NOD-like
            receptor family proteins via activating their ATPase enzymatic
            activity
  JOURNAL   Immunity 56 (5), 926-943 (2023)
   PUBMED   36948192
  REMARK    GeneRIF: Ribosome-rescuer PELO catalyzes the oligomeric assembly of
            NOD-like receptor family proteins via activating their ATPase
            enzymatic activity.
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Mills,E.W., Green,R. and Ingolia,N.T.
  TITLE     Slowed decay of mRNAs enhances platelet specific translation
  JOURNAL   Blood 129 (17), e38-e48 (2017)
   PUBMED   28213379
  REMARK    GeneRIF: The data suggest that the decay of platelet mRNAs is
            slowed by the natural loss of the mRNA surveillance and ribosome
            rescue factor Pelota.
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Davis,O.S., Butcher,L.M., Docherty,S.J., Meaburn,E.L., Curtis,C.J.,
            Simpson,M.A., Schalkwyk,L.C. and Plomin,R.
  TITLE     A three-stage genome-wide association study of general cognitive
            ability: hunting the small effects
  JOURNAL   Behav Genet 40 (6), 759-767 (2010)
   PUBMED   20306291
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 385)
  AUTHORS   Cheli,Y., Kanaji,S., Jacquelin,B., Chang,M., Nugent,D.J. and
            Kunicki,T.J.
  TITLE     Transcriptional and epigenetic regulation of the integrin collagen
            receptor locus ITGA1-PELO-ITGA2
  JOURNAL   Biochim Biophys Acta 1769 (9-10), 546-558 (2007)
   PUBMED   17669516
  REMARK    GeneRIF: thrombopoietin-induced in vitro differentiation of primary
            human cord blood mononuclear cells into megakaryocytes, we observed
            rapid, progressive CpG methylation of ITGA1, but not PELO or ITGA2.
REFERENCE   9  (residues 1 to 385)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   10 (residues 1 to 385)
  AUTHORS   Shamsadin,R., Adham,I.M., von Beust,G. and Engel,W.
  TITLE     Molecular cloning, expression and chromosome location of the human
            pelota gene PELO
  JOURNAL   Cytogenet Cell Genet 90 (1-2), 75-78 (2000)
   PUBMED   11060452
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026230.5.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_005248600.1, NP_054819.1, NP_057030.2.
            
            Summary: This gene encodes a protein which contains a conserved
            nuclear localization signal. The encoded protein may have a role in
            spermatogenesis, cell cycle control, and in meiotic cell division.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY117399.1, AK056144.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274311.3/ ENSP00000274311.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q11.2"
     Protein         1..385
                     /product="protein pelota homolog"
                     /note="pelota homolog; hPelota; protein Dom34 homolog"
                     /calculated_mol_wt=43228
     Region          1..370
                     /region_name="aRF1/eRF1"
                     /note="peptide chain release factor 1, archaeal and
                     eukaryotic forms; cl42864"
                     /db_xref="CDD:456209"
     Region          168..172
                     /region_name="nuclear localization signal"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BRX2.2)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BRX2.2)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9BRX2.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BRX2.2)"
     CDS             1..385
                     /gene="PELO"
                     /gene_synonym="CGI-17; PRO1770"
                     /coded_by="NM_015946.5:1010..2167"
                     /db_xref="CCDS:CCDS3956.1"
                     /db_xref="GeneID:53918"
                     /db_xref="HGNC:HGNC:8829"
                     /db_xref="MIM:605757"
ORIGIN      
        1 mklvrkniek dnagqvtlvp eepedmwhty nlvqvgdslr astirkvqte sstgsvgsnr
       61 vrttltlcve aidfdsqacq lrvkgtniqe neyvkmgayh tielepnrqf tlakkqwdsv
      121 vlerieqacd pawsadvaav vmqeglahic lvtpsmtltr akvevniprk rkgncsqhdr
      181 alerfyeqvv qaiqrhihfd vvkcilvasp gfvreqfcdy lfqqavktdn klllenrskf
      241 lqvhassghk yslkealcdp tvasrlsdtk aagevkaldd fykmlqhepd rafyglkqve
      301 kaneamaidt llisdelfrh qdvatrsryv rlvdsvkena gtvrifsslh vsgeqlsqlt
      361 gvaailrfpv pelsdqegds sseed
//
LOCUS       NP_001651                180 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-ribosylation factor 4 [Homo sapiens].
ACCESSION   NP_001651 XP_946648
VERSION     NP_001651.1
DBSOURCE    REFSEQ: accession NM_001660.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Zhang,L., Fang,Z., Zhu,Q., Yang,S., Fu,J., Sun,Z., Lu,G., Wei,C.,
            Zhang,Z., Lee,K., Zhong,Y., Liu,R. and He,J.C.
  TITLE     Cholesterol 25-Hydroxylase Protects Against Diabetic Kidney Disease
            by Regulating ADP Ribosylation Factor 4
  JOURNAL   Adv Sci (Weinh) 11 (29), e2309642 (2024)
   PUBMED   38816950
  REMARK    GeneRIF: Cholesterol 25-Hydroxylase Protects Against Diabetic
            Kidney Disease by Regulating ADP Ribosylation Factor 4.
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Fu,J., Lou,X., Wan,S., Zhao,X., Chen,Z., Zhu,M., Guo,L., Wu,D. and
            Wang,S.
  TITLE     microRNA-196a-3p inhibits cell proliferation and promotes cell
            apoptosis by targeting ADP ribosylation factor 4 in diffuse large
            B-cell lymphoma
  JOURNAL   Oncol Rep 45 (2), 764-775 (2021)
   PUBMED   33416178
  REMARK    GeneRIF: microRNA196a3p inhibits cell proliferation and promotes
            cell apoptosis by targeting ADP ribosylation factor 4 in diffuse
            large Bcell lymphoma.
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Zhang,Q., Wu,L., Bai,B., Li,D., Xiao,P., Li,Q., Zhang,Z., Wang,H.,
            Li,L. and Jiang,Q.
  TITLE     Quantitative Proteomics Reveals Association of Neuron Projection
            Development Genes ARF4, KIF5B, and RAB8A With Hirschsprung Disease
  JOURNAL   Mol Cell Proteomics 20, 100007 (2021)
   PUBMED   33561610
  REMARK    GeneRIF: Quantitative Proteomics Reveals Association of Neuron
            Projection Development Genes ARF4, KIF5B, and RAB8A With
            Hirschsprung Disease.
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Dejgaard,S.Y. and Presley,J.F.
  TITLE     Class II Arfs require a brefeldin-A-sensitive factor for Golgi
            association
  JOURNAL   Biochem Biophys Res Commun 530 (1), 301-306 (2020)
   PUBMED   32828303
  REMARK    GeneRIF: Class II Arfs require a brefeldin-A-sensitive factor for
            Golgi association.
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Vorobieva,N., Protopopov,A., Protopopova,M., Kashuba,V.,
            Allikmets,R.L., Modi,W., Zabarovsky,E.R., Klein,G., Kisselev,L. and
            Graphodatsky,A.
  TITLE     Localization of human ARF2 and NCK genes and 13 other NotI-linking
            clones to chromosome 3 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 91-94 (1995)
   PUBMED   7956370
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Lee,F.J., Moss,J. and Vaughan,M.
  TITLE     Human and Giardia ADP-ribosylation factors (ARFs) complement ARF
            function in Saccharomyces cerevisiae
  JOURNAL   J Biol Chem 267 (34), 24441-24445 (1992)
   PUBMED   1447192
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Kahn,R.A., Kern,F.G., Clark,J., Gelmann,E.P. and Rulka,C.
  TITLE     Human ADP-ribosylation factors. A functionally conserved family of
            GTP-binding proteins
  JOURNAL   J Biol Chem 266 (4), 2606-2614 (1991)
   PUBMED   1899243
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Monaco,L., Murtagh,J.J., Newman,K.B., Tsai,S.C., Moss,J. and
            Vaughan,M.
  TITLE     Selective amplification of an mRNA and related pseudogene for a
            human ADP-ribosylation factor, a guanine nucleotide-dependent
            protein activator of cholera toxin
  JOURNAL   Proc Natl Acad Sci U S A 87 (6), 2206-2210 (1990)
   PUBMED   2107548
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Stearns,T., Willingham,M.C., Botstein,D. and Kahn,R.A.
  TITLE     ADP-ribosylation factor is functionally and physically associated
            with the Golgi complex
  JOURNAL   Proc Natl Acad Sci U S A 87 (3), 1238-1242 (1990)
   PUBMED   2105501
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA259855.1 and BC003364.1.
            
            On Mar 4, 2006 this sequence version replaced XP_946648.1.
            
            Summary: This gene is a member of the human ARF gene family whose
            members encode small guanine nucleotide-binding proteins that
            stimulate the ADP-ribosyltransferase activity of cholera toxin and
            play a role in vesicular trafficking and as activators of
            phospholipase D. The gene products include 5 ARF proteins and 11
            ARF-like proteins and constitute one family of the RAS superfamily.
            The ARF proteins are categorized as class I, class II and class
            III; this gene is a class II member. The members of each class
            share a common gene organization. The ARF4 gene spans approximately
            12kb and contains six exons and five introns. This gene is the most
            divergent member of the human ARFs. Conflicting map positions at
            3p14 or 3p21 have been reported for this gene. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1001558.1,
                                           SRR3476690.1024844.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2154405
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303436.11/ ENSP00000306010.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     Protein         1..180
                     /product="ADP-ribosylation factor 4"
                     /note="ADP-ribosylation factor 2; ADP ribosylation factor
                     4"
                     /calculated_mol_wt=20380
     Region          1..180
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            24..31
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206717"
     Site            order(26..32,126..127,129,159..161)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206717"
     Site            order(26..27,31,35,47..54,76,81)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206717"
     Site            36..51
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206717"
     Site            order(48..52,57,67,71,73,77,79..81)
                     /site_type="other"
                     /note="GEF interaction site [polypeptide binding]"
                     /db_xref="CDD:206717"
     Site            48
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206717"
     Site            order(49..51,73,80)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:206717"
     Site            51..66
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206717"
     Site            67..70
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206717"
     Site            69..86
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206717"
     Site            126..129
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206717"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P18085.3)"
     Site            159..161
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206717"
     CDS             1..180
                     /gene="ARF4"
                     /gene_synonym="ARF2"
                     /coded_by="NM_001660.4:205..747"
                     /db_xref="CCDS:CCDS2884.1"
                     /db_xref="GeneID:378"
                     /db_xref="HGNC:HGNC:655"
                     /db_xref="MIM:601177"
ORIGIN      
        1 mgltisslfs rlfgkkqmri lmvgldaagk ttilyklklg eivttiptig fnvetveykn
       61 icftvwdvgg qdrirplwkh yfqntqglif vvdsndreri qevadelqkm llvdelrdav
      121 lllfankqdl pnamaisemt dklglqslrn rtwyvqatca tqgtglyegl dwlsnelskr
//
LOCUS       NP_001278207             305 aa            linear   PRI 27-APR-2025
DEFINITION  serpin B11 isoform b [Homo sapiens].
ACCESSION   NP_001278207 XP_006722632
VERSION     NP_001278207.1
DBSOURCE    REFSEQ: accession NM_001291278.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Heit,C., Jackson,B.C., McAndrews,M., Wright,M.W., Thompson,D.C.,
            Silverman,G.A., Nebert,D.W. and Vasiliou,V.
  TITLE     Update of the human and mouse SERPIN gene superfamily
  JOURNAL   Hum Genomics 7 (1), 22 (2013)
   PUBMED   24172014
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Lim,W., Kim,J.H., Ahn,S.E., Jeong,W., Kim,J., Bazer,F.W., Han,J.Y.
            and Song,G.
  TITLE     Avian SERPINB11 gene: a marker for ovarian endometrioid cancer in
            chickens
  JOURNAL   Exp Biol Med (Maywood) 237 (2), 150-159 (2012)
   PUBMED   22289513
  REMARK    GeneRIF: SERPINB11 has a role in ovarian endometrioid carcinoma in
            chickens and human
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Seixas,S., Ivanova,N., Ferreira,Z., Rocha,J. and Victor,B.L.
  TITLE     Loss and gain of function in SERPINB11: an example of a gene under
            selection on standing variation, with implications for
            host-pathogen interactions
  JOURNAL   PLoS One 7 (2), e32518 (2012)
   PUBMED   22393410
  REMARK    GeneRIF: SERPINB11 is a gene under selection on standing variation,
            with roles in host-pathogen interactions
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Askew,D.J., Cataltepe,S., Kumar,V., Edwards,C., Pace,S.M.,
            Howarth,R.N., Pak,S.C., Askew,Y.S., Bromme,D., Luke,C.J.,
            Whisstock,J.C. and Silverman,G.A.
  TITLE     SERPINB11 is a new noninhibitory intracellular serpin. Common
            single nucleotide polymorphisms in the scaffold impair
            conformational change
  JOURNAL   J Biol Chem 282 (34), 24948-24960 (2007)
   PUBMED   17562709
  REMARK    GeneRIF: SERPINB11 is a new noninhibitory intracellular serpin
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Denoeud,F., Kapranov,P., Ucla,C., Frankish,A., Castelo,R.,
            Drenkow,J., Lagarde,J., Alioto,T., Manzano,C., Chrast,J., Dike,S.,
            Wyss,C., Henrichsen,C.N., Holroyd,N., Dickson,M.C., Taylor,R.,
            Hance,Z., Foissac,S., Myers,R.M., Rogers,J., Hubbard,T., Harrow,J.,
            Guigo,R., Gingeras,T.R., Antonarakis,S.E. and Reymond,A.
  TITLE     Prominent use of distal 5' transcription start sites and discovery
            of a large number of additional exons in ENCODE regions
  JOURNAL   Genome Res 17 (6), 746-759 (2007)
   PUBMED   17567994
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC069356.6 and KF459701.1.
            
            On Apr 1, 2014 this sequence version replaced XP_006722632.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY792324.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968832, SAMEA2144335 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            polymorphic pseudogene    :: PMID: 22393410
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.33"
     Protein         1..305
                     /product="serpin B11 isoform b"
                     /note="serine (or cysteine) proteinase inhibitor, clade B
                     (ovalbumin), member 11; serpin B11; serpin peptidase
                     inhibitor, clade B (ovalbumin), member 11"
                     /calculated_mol_wt=33853
     Region          1..305
                     /region_name="serpin"
                     /note="SERine Proteinase INhibitors (serpin) family;
                     cl38926"
                     /db_xref="CDD:476815"
     Site            order(256..266,283)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381036"
     CDS             1..305
                     /gene="SERPINB11"
                     /gene_synonym="EPIPIN; SERPIN11"
                     /coded_by="NM_001291278.2:63..980"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77196.1"
                     /db_xref="GeneID:89778"
                     /db_xref="HGNC:HGNC:14221"
                     /db_xref="MIM:615682"
ORIGIN      
        1 mgslstanve fcldvfkeln snnigdniff sslsllyals mvllgarget eeqlekvlhf
       61 shtvdslkpg fkdspkcsqa grihsefgve fsqinqpdsn ctlsianrly gtktmafhqg
      121 knvtvemmyq igtfklafvk epqmqvlelp yvnnklsmii llpvgianlk qiekqlnsgt
      181 fhewtsssnm merevevhlp rfkletkyel nsllkslgvt dlfnqvkadl sgmsptkgly
      241 lskaihksyl dvseegteaa aatgdsiavk slpmraqfka nhpflffirh thtntilfcg
      301 klasp
//
LOCUS       NP_803876                337 aa            linear   PRI 27-APR-2025
DEFINITION  ras association domain-containing protein 6 isoform a [Homo
            sapiens].
ACCESSION   NP_803876
VERSION     NP_803876.1
DBSOURCE    REFSEQ: accession NM_177532.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Kuleape,J.A., Hossain,S., Sinclear,C.K., Shimizu,T., Iwasa,H.,
            Maruyama,J., Arimoto-Matsuzaki,K., Nishina,H. and Hata,Y.
  TITLE     DNA Damage Triggers the Nuclear Accumulation of RASSF6 Tumor
            Suppressor Protein via CDK9 and BAF53 To Regulate p53 Target Gene
            Transcription
  JOURNAL   Mol Cell Biol 42 (2), e0031021 (2022)
   PUBMED   34898277
  REMARK    GeneRIF: DNA Damage Triggers the Nuclear Accumulation of RASSF6
            Tumor Suppressor Protein via CDK9 and BAF53 To Regulate p53 Target
            Gene Transcription.
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Zhou,W., Liu,Y. and Wu,X.
  TITLE     Down-regulation of circITCH promotes osteosarcoma development and
            resistance to doxorubicin via the miR-524/RASSF6 axis
  JOURNAL   J Gene Med 23 (10), e3373 (2021)
   PUBMED   34151476
  REMARK    GeneRIF: Down-regulation of circITCH promotes osteosarcoma
            development and resistance to doxorubicin via the miR-524/RASSF6
            axis.
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Bozdogan,O., Guresci,S., Ocalan,D. and Bozdogan,N.
  TITLE     Kindlin-3 and RASSF6 are probable biomarkers for predicting
            metastasis in cutaneous melanoma
  JOURNAL   Pol J Pathol 72 (3), 237-244 (2021)
   PUBMED   35048636
  REMARK    GeneRIF: Kindlin-3 and RASSF6 are probable biomarkers for
            predicting metastasis in cutaneous melanoma.
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Hesson,L.B., Dunwell,T.L., Cooper,W.N., Catchpoole,D., Brini,A.T.,
            Chiaramonte,R., Griffiths,M., Chalmers,A.D., Maher,E.R. and
            Latif,F.
  TITLE     The novel RASSF6 and RASSF10 candidate tumour suppressor genes are
            frequently epigenetically inactivated in childhood leukaemias
  JOURNAL   Mol Cancer 8, 42 (2009)
   PUBMED   19570220
  REMARK    GeneRIF: Sequencing revealed RASSF6 and RASSF10 were the only RASSF
            members with a high frequency of leukaemia-specific methylation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Hillian,A.D., Londono,D., Dunn,J.M., Goddard,K.A., Pace,R.G.,
            Knowles,M.R. and Drumm,M.L.
  CONSRTM   CF Gene Modifier Study Group
  TITLE     Modulation of cystic fibrosis lung disease by variants in
            interleukin-8
  JOURNAL   Genes Immun 9 (6), 501-508 (2008)
   PUBMED   18563170
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Allen,N.P., Donninger,H., Vos,M.D., Eckfeld,K., Hesson,L.,
            Gordon,L., Birrer,M.J., Latif,F. and Clark,G.J.
  TITLE     RASSF6 is a novel member of the RASSF family of tumor suppressors
  JOURNAL   Oncogene 26 (42), 6203-6211 (2007)
   PUBMED   17404571
  REMARK    GeneRIF: Demonstrates properties of a Ras effector and tumor
            suppressor but exhibits biological properties that are unique and
            distinct from those of other family members.
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Ikeda,M., Hirabayashi,S., Fujiwara,N., Mori,H., Kawata,A., Iida,J.,
            Bao,Y., Sato,Y., Iida,T., Sugimura,H. and Hata,Y.
  TITLE     Ras-association domain family protein 6 induces apoptosis via both
            caspase-dependent and caspase-independent pathways
  JOURNAL   Exp Cell Res 313 (7), 1484-1495 (2007)
   PUBMED   17367779
  REMARK    GeneRIF: These findings indicate that RASSF6 is implicated in
            apoptosis in HeLa cells and that it triggers both caspase-dependent
            and caspase-independent pathways.
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Hull,J., Rowlands,K., Lockhart,E., Sharland,M., Moore,C.,
            Hanchard,N. and Kwiatkowski,D.P.
  TITLE     Haplotype mapping of the bronchiolitis susceptibility locus near
            IL8
  JOURNAL   Hum Genet 114 (3), 272-279 (2004)
   PUBMED   14605870
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074250.6.
            
            Summary: This gene encodes a member of the Ras-association domain
            family (RASSF). Members of this family form the core of a highly
            conserved tumor suppressor network, the Salvador-Warts-Hippo (SWH)
            pathway. The protein encoded by this gene is a Ras effector protein
            that induces apoptosis. A genomic region containing this gene has
            been linked to susceptibility to viral bronchiolitis. Alternative
            splicing results in multiple transcript variants and protein
            isoforms. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. It encodes isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749283.1, AY217664.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307439.10/ ENSP00000303877.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.3"
     Protein         1..337
                     /product="ras association domain-containing protein 6
                     isoform a"
                     /note="Ras association (RalGDS/AF-6) domain family 6;
                     putative RAS binding protein; ras association
                     domain-containing protein 6; Ras association (RalGDS/AF-6)
                     domain family member 6"
                     /calculated_mol_wt=39673
     Region          187..273
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          283..328
                     /region_name="SARAH_RASSF6"
                     /note="C-terminal SARAH domain found in Ras-association
                     domain-containing protein 6 (RASSF6); cd21895"
                     /db_xref="CDD:439189"
     Site            order(284..285,287,289,292,296,299..300,302..303,306..307,
                     310..311,313..314,317..318,321,324..325)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:439189"
     CDS             1..337
                     /gene="RASSF6"
                     /coded_by="NM_177532.5:184..1197"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3559.1"
                     /db_xref="GeneID:166824"
                     /db_xref="HGNC:HGNC:20796"
                     /db_xref="MIM:612620"
ORIGIN      
        1 mtmmahqyps wifinektfi treqlnsllk tynifyenqk nlhilygete dgklivegml
       61 difwgvkrpi qlkiqdekpf ssftsmkssd vfsskgmtrw gefddlyris eldrtqipms
      121 ekrnsqedyl syhsntlkph akdepdspvl yrtmseaalv rkrmkplmmd rkerqknras
      181 inghfynhet sifipafese tkvrvnsnmr teevikqllq kfkienspqd falhiifatg
      241 eqrrlkktdi pllqrllqgp seknariflm dkdaeeissd vaqyinfhfs llesilqrln
      301 eeekreiqri vtkfnkekai ilkclqnklv iktettv
//
LOCUS       NP_001347546             157 aa            linear   ROD 27-APR-2025
DEFINITION  alkaline ceramidase 3 isoform 4 [Mus musculus].
ACCESSION   NP_001347546
VERSION     NP_001347546.1
DBSOURCE    REFSEQ: accession NM_001360617.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Li,F., Xu,R., Lin,C.L., Low,B.E., Cai,L., Li,S., Ji,P., Huang,L.,
            Wiles,M.V., Hannun,Y.A., Obeid,L.M., Chen,Y. and Mao,C.
  TITLE     Maternal and fetal alkaline ceramidase 2 is required for placental
            vascular integrity in mice
  JOURNAL   FASEB J 34 (11), 15252-15268 (2020)
   PUBMED   32959379
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Wang,K., Li,C., Lin,X., Sun,H., Xu,R., Li,Q., Wei,Y., Li,Y.,
            Qian,J., Liu,C., Zhang,Q., Yu,S., Cui,Z., Huang,X., Zhu,B., Zhou,J.
            and Mao,C.
  TITLE     Targeting alkaline ceramidase 3 alleviates the severity of
            nonalcoholic steatohepatitis by reducing oxidative stress
  JOURNAL   Cell Death Dis 11 (1), 28 (2020)
   PUBMED   31949129
  REMARK    GeneRIF: Targeting alkaline ceramidase 3 alleviates the severity of
            nonalcoholic steatohepatitis by reducing oxidative stress.
            Erratum:[Cell Death Dis. 2020 Mar 17;11(3):191. doi:
            10.1038/s41419-020-2396-1. PMID: 32184395]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Li,F., Xu,R., Low,B.E., Lin,C.L., Garcia-Barros,M., Schrandt,J.,
            Mileva,I., Snider,A., Luo,C.K., Jiang,X.C., Li,M.S., Hannun,Y.A.,
            Obeid,L.M., Wiles,M.V. and Mao,C.
  TITLE     Alkaline ceramidase 2 is essential for the homeostasis of plasma
            sphingoid bases and their phosphates
  JOURNAL   FASEB J 32 (6), 3058-3069 (2018)
   PUBMED   29401619
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Wang,K., Xu,R., Snider,A.J., Schrandt,J., Li,Y., Bialkowska,A.B.,
            Li,M., Zhou,J., Hannun,Y.A., Obeid,L.M., Yang,V.W. and Mao,C.
  TITLE     Alkaline ceramidase 3 deficiency aggravates colitis and
            colitis-associated tumorigenesis in mice by hyperactivating the
            innate immune system
  JOURNAL   Cell Death Dis 7 (3), e2124 (2016)
   PUBMED   26938296
  REMARK    GeneRIF: Alkaline ceramidase 3 expression has an important role in
            the innate immune response by regulating the expression of
            pro-inflammatory cytokines in cells of the innate immune system
            through C18:1-ceramide.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 157)
  AUTHORS   Wang,K., Xu,R., Schrandt,J., Shah,P., Gong,Y.Z., Preston,C.,
            Wang,L., Yi,J.K., Lin,C.L., Sun,W., Spyropoulos,D.D., Rhee,S.,
            Li,M., Zhou,J., Ge,S., Zhang,G., Snider,A.J., Hannun,Y.A.,
            Obeid,L.M. and Mao,C.
  TITLE     Alkaline Ceramidase 3 Deficiency Results in Purkinje Cell
            Degeneration and Cerebellar Ataxia Due to Dyshomeostasis of
            Sphingolipids in the Brain
  JOURNAL   PLoS Genet 11 (10), e1005591 (2015)
   PUBMED   26474409
  REMARK    GeneRIF: Acer3 plays critically protective roles in controlling the
            homeostasis of various sphingolipids, including ceramides,
            sphingosine, S1P, and certain complex sphingolipids in the brain
            and protects Purkinje cells from premature degeneration.
            Erratum:[PLoS Genet. 2018 Jan 23;14(1):e1007190. doi:
            10.1371/journal.pgen.1007190. PMID: 29360825]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 157)
  AUTHORS   Wang,Z., Kirkwood,J.S., Taylor,A.W., Stevens,J.F., Leid,M.,
            Ganguli-Indra,G. and Indra,A.K.
  TITLE     Transcription factor Ctip2 controls epidermal lipid metabolism and
            regulates expression of genes involved in sphingolipid biosynthesis
            during skin development
  JOURNAL   J Invest Dermatol 133 (3), 668-676 (2013)
   PUBMED   23096701
REFERENCE   7  (residues 1 to 157)
  AUTHORS   Boon,A.C., deBeauchamp,J., Hollmann,A., Luke,J., Kotb,M., Rowe,S.,
            Finkelstein,D., Neale,G., Lu,L., Williams,R.W. and Webby,R.J.
  TITLE     Host genetic variation affects resistance to infection with a
            highly pathogenic H5N1 influenza A virus in mice
  JOURNAL   J Virol 83 (20), 10417-10426 (2009)
   PUBMED   19706712
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC111084.12 and AC119880.11.
            
            Transcript Variant: This variant (4) contains an alternate exon
            compared to variant 1. The resulting isoform (4) has a shorter and
            distinct N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164142,
                              SAMN01164143 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 53.65 cM"
     Protein         1..157
                     /product="alkaline ceramidase 3 isoform 4"
                     /EC_number="3.5.1.23"
                     /note="phytoceramidase, alkaline; alkCDase 3; alkaline
                     CDase 3; alkaline phytoceramidase"
                     /calculated_mol_wt=18387
     Region          <45..153
                     /region_name="Ceramidase"
                     /note="pfam05875"
                     /db_xref="CDD:461766"
     CDS             1..157
                     /gene="Acer3"
                     /gene_synonym="1110057L18Rik; 5430429L08Rik; aPHC; Phca"
                     /coded_by="NM_001360617.1:587..1060"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:66190"
                     /db_xref="MGI:MGI:1913440"
ORIGIN      
        1 mcisrvlsvl smngpcadev lalsfapcyl dnqrhsfhpt eefcfvlllr tedlpwvypw
       61 lrglgytslt vfllgfllwn idnifcdslr nfrkrvppvl gvttqfhaww hiltglgsyl
      121 hilfslytrt lylryrpkvk flfgiwpavm fepqrkh
//
LOCUS       NP_787071                739 aa            linear   PRI 27-APR-2025
DEFINITION  homeobox protein SIX5 [Homo sapiens].
ACCESSION   NP_787071
VERSION     NP_787071.3
DBSOURCE    REFSEQ: accession NM_175875.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Masuda,M., Kanno,A., Nara,K., Mutai,H., Morisada,N., Iijima,K.,
            Morimoto,N., Nakano,A., Sugiuchi,T., Okamoto,Y., Masuda,S.,
            Katsunuma,S., Ogawa,K. and Matsunaga,T.
  TITLE     Phenotype-genotype correlation in patients with typical and
            atypical branchio-oto-renal syndrome
  JOURNAL   Sci Rep 12 (1), 969 (2022)
   PUBMED   35046468
  REMARK    GeneRIF: Phenotype-genotype correlation in patients with typical
            and atypical branchio-oto-renal syndrome.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Liu,Q., Li,A., Tian,Y., Liu,Y., Li,T., Zhang,C., Wu,J.D., Han,X.
            and Wu,K.
  TITLE     The expression profile and clinic significance of the SIX family in
            non-small cell lung cancer
  JOURNAL   J Hematol Oncol 9 (1), 119 (2016)
   PUBMED   27821176
  REMARK    GeneRIF: the higher expressions of SIX1-5 were associated with the
            greater possibility of the tumorigenesis in lung neoplasms
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Morisada,N., Nozu,K. and Iijima,K.
  TITLE     Branchio-oto-renal syndrome: comprehensive review based on
            nationwide surveillance in Japan
  JOURNAL   Pediatr Int 56 (3), 309-314 (2014)
   PUBMED   24730701
  REMARK    GeneRIF: Three causative genes for BOR syndrome have been reported
            thus far: EYA1, SIX1, and SIX5, but the causative genes for
            approximately half of all BOR patients remain unknown.[review]
            Review article
REFERENCE   4  (residues 1 to 739)
  AUTHORS   Wang,S.H., Wu,C.C., Lu,Y.C., Lin,Y.H., Su,Y.N., Hwu,W.L., Yu,I.S.
            and Hsu,C.J.
  TITLE     Mutation screening of the EYA1, SIX1, and SIX5 genes in an East
            Asian cohort with branchio-oto-renal syndrome
  JOURNAL   Laryngoscope 122 (5), 1130-1136 (2012)
   PUBMED   22447252
  REMARK    GeneRIF: In East Asian populations, a SIX1 mutation has been
            reported in a Japanese family with branchio-oto (BO) syndrome,yet
            SIX5 mutations have never been reported.
REFERENCE   5  (residues 1 to 739)
  AUTHORS   Krug,P., Moriniere,V., Marlin,S., Koubi,V., Gabriel,H.D., Colin,E.,
            Bonneau,D., Salomon,R., Antignac,C. and Heidet,L.
  TITLE     Mutation screening of the EYA1, SIX1, and SIX5 genes in a large
            cohort of patients harboring branchio-oto-renal syndrome calls into
            question the pathogenic role of SIX5 mutations
  JOURNAL   Hum Mutat 32 (2), 183-190 (2011)
   PUBMED   21280147
  REMARK    GeneRIF: Study reports a screening of 140 patients from 124
            families with Branchio-oto-renal and identified 36 EYA1 mutations
            in 42 unrelated patients, 2 mutations, and 1 change of unknown
            significance in SIX1 in 3 unrelated patients, but no mutation in
            SIX5.
REFERENCE   6  (residues 1 to 739)
  AUTHORS   Winchester,C.L., Ferrier,R.K., Sermoni,A., Clark,B.J. and
            Johnson,K.J.
  TITLE     Characterization of the expression of DMPK and SIX5 in the human
            eye and implications for pathogenesis in myotonic dystrophy
  JOURNAL   Hum Mol Genet 8 (3), 481-492 (1999)
   PUBMED   9949207
REFERENCE   7  (residues 1 to 739)
  AUTHORS   Murakami,Y., Ohto,H., Ikeda,U., Shimada,K., Momoi,T. and
            Kawakami,K.
  TITLE     Promoter of mDMAHP/Six5: differential utilization of multiple
            transcription initiation sites and positive/negative regulatory
            elements
  JOURNAL   Hum Mol Genet 7 (13), 2103-2112 (1998)
   PUBMED   9817928
REFERENCE   8  (residues 1 to 739)
  AUTHORS   Klesert,T.R., Otten,A.D., Bird,T.D. and Tapscott,S.J.
  TITLE     Trinucleotide repeat expansion at the myotonic dystrophy locus
            reduces expression of DMAHP
  JOURNAL   Nat Genet 16 (4), 402-406 (1997)
   PUBMED   9241282
REFERENCE   9  (residues 1 to 739)
  AUTHORS   Boucher,C.A., King,S.K., Carey,N., Krahe,R., Winchester,C.L.,
            Rahman,S., Creavin,T., Meghji,P., Bailey,M.E., Chartier,F.L. et al.
  TITLE     A novel homeodomain-encoding gene is associated with a large CpG
            island interrupted by the myotonic dystrophy unstable (CTG)n repeat
  JOURNAL   Hum Mol Genet 4 (10), 1919-1925 (1995)
   PUBMED   8595416
REFERENCE   10 (residues 1 to 739)
  AUTHORS   Smith,R.J.H.
  TITLE     Branchiootorenal Spectrum Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301554
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074212.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_787071.2.
            
            Summary: The protein encoded by this gene is a
            homeodomain-containing transcription factor that appears to
            function in the regulation of organogenesis. This gene is located
            downstream of the dystrophia myotonica-protein kinase gene.
            Mutations in this gene are a cause of branchiootorenal syndrome
            type 2. [provided by RefSeq, Jul 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.484181.1, AK074826.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155770, SAMEA2155984
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317578.7/ ENSP00000316842.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..739
                     /product="homeobox protein SIX5"
                     /note="DM locus-associated homeodomain protein; dystrophia
                     myotonica-associated homeodomain protein; sine oculis
                     homeobox homolog 5"
                     /calculated_mol_wt=74431
     Region          1..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N196.3)"
     Region          86..195
                     /region_name="SIX1_SD"
                     /note="Transcriptional regulator, SIX1, N-terminal SD
                     domain; pfam16878"
                     /db_xref="CDD:465293"
     Region          206..257
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(207,247,250..251,254)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          251..294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N196.3)"
     Region          361..381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N196.3)"
     Region          <424..663
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          617..650
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N196.3)"
     CDS             1..739
                     /gene="SIX5"
                     /gene_synonym="BOR2; DMAHP"
                     /coded_by="NM_175875.5:409..2628"
                     /db_xref="CCDS:CCDS12673.1"
                     /db_xref="GeneID:147912"
                     /db_xref="HGNC:HGNC:10891"
                     /db_xref="MIM:600963"
ORIGIN      
        1 matlpaepsa gpaaggeava aaaateeeee earqllqtlq aaegeaaaaa gagagaaaag
       61 aegpgspgvp gsppeaasep ptglrfspeq vacvceallq aghagrlsrf lgalppaerl
      121 rgsdpvlrar alvafqrgey aelyrllesr pfpaahhafl qdlylraryh eaerargral
      181 gavdkyrlrk kfplpktiwd geetvycfke rsraalkacy rgnryptpde krrlatltgl
      241 sltqvsnwfk nrrqrdrtga gggapckses dgnpttedes srspedlerg aapvsaeaaa
      301 qgsiflagtg ppapcpasss ilvngsflaa sgspavllng gpviinglal geasslgpll
      361 ltggggappp qpspqgaset ktslvldpqt gevrleeaqs eapetkgaqv aapgpalgee
      421 vlgplaqvvp gpptaatfpl ppgpvpavaa pqvvplsppp gyptglspts pllnlpqvvp
      481 tsqvvtlpqa vgplqllaag pgspvkvaaa agpanvhlin sgvgvtalql psatapgnfl
      541 lanpvsgspi vtgvalqqgk iiltatfpts mlvsqvlppa pglalplkpe taisvpeggl
      601 pvapspalpe ahalgtlsaq qpppaaatts stslpfspds pgllpnfpap ppeglmlspa
      661 avpvwsagle lsagteglle aekglgtqap htvlrlpdpd peglllgata ggevdeglea
      721 eakvltqlqs vpveeplel
//
LOCUS       NP_002124                288 aa            linear   PRI 27-APR-2025
DEFINITION  heme oxygenase 1 [Homo sapiens].
ACCESSION   NP_002124
VERSION     NP_002124.1
DBSOURCE    REFSEQ: accession NM_002133.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Chudy,P., Kochan,J., Wawro,M., Nguyen,P., Gorczyca,M., Varanko,A.,
            Retka,A., Ghadei,S.S., Napieralska,E., Grochot-Przeczek,A.,
            Szade,K., Berendes,L.S., Park,J., Sokolowski,G., Yu,Q.,
            Jozkowicz,A., Nowak,W.N. and Krzeptowski,W.
  TITLE     Heme oxygenase-1 protects cells from replication stress
  JOURNAL   Redox Biol 75, 103247 (2024)
   PUBMED   39047636
  REMARK    GeneRIF: Heme oxygenase-1 protects cells from replication stress.
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Salloom,R.J., Ahmad,I.M., Sahtout,D.Z., Baine,M.J. and Abdalla,M.Y.
  TITLE     Heme Oxygenase-1 and Prostate Cancer: Function, Regulation, and
            Implication in Cancer Therapy
  JOURNAL   Int J Mol Sci 25 (17), 9195 (2024)
   PUBMED   39273143
  REMARK    GeneRIF: Heme Oxygenase-1 and Prostate Cancer: Function,
            Regulation, and Implication in Cancer Therapy.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Zhao,Y., Wang,L., Li,X., Jiang,J., Ma,Y., Guo,S., Zhou,J. and Li,Y.
  TITLE     Programmed Cell Death-Related Gene Signature Associated with
            Prognosis and Immune Infiltration and the Roles of HMOX1 in the
            Proliferation and Apoptosis were Investigated in Uveal Melanoma
  JOURNAL   Genes Genomics 46 (7), 785-801 (2024)
   PUBMED   38767825
  REMARK    GeneRIF: Programmed Cell Death-Related Gene Signature Associated
            with Prognosis and Immune Infiltration and the Roles of HMOX1 in
            the Proliferation and Apoptosis were Investigated in Uveal
            Melanoma.
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Chu,M., Chen,G., Chen,K., Zhu,P., Wang,Z., Qian,Z., Tao,H., Xu,Y.
            and Geng,D.
  TITLE     Heme oxygenase 1 linked to inactivation of subchondral osteoclasts
            in osteoarthritis
  JOURNAL   J Zhejiang Univ Sci B 25 (6), 513-528 (2024)
   PUBMED   38910496
  REMARK    GeneRIF: Heme oxygenase 1 linked to inactivation of subchondral
            osteoclasts in osteoarthritis.
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Chen,J., Li,J., Wang,X., Fu,X., Ke,J., Li,J., Wen,J., Cheng,K.,
            Li,S. and Shi,Z.
  TITLE     Heme Oxygenase-1 Gene (GT)n Polymorphism Linked to Deep White
            Matter Hyperintensities, Not Periventricular Hyperintensities
  JOURNAL   J Am Heart Assoc 13 (11), e033981 (2024)
   PUBMED   38818928
  REMARK    GeneRIF: Heme Oxygenase-1 Gene (GT)n Polymorphism Linked to Deep
            White Matter Hyperintensities, Not Periventricular
            Hyperintensities.
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Schipper,H.M., Cisse,S. and Stopa,E.G.
  TITLE     Expression of heme oxygenase-1 in the senescent and
            Alzheimer-diseased brain
  JOURNAL   Ann Neurol 37 (6), 758-768 (1995)
   PUBMED   7778849
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Wilks,A., Black,S.M., Miller,W.L. and Ortiz de Montellano,P.R.
  TITLE     Expression and characterization of truncated human heme oxygenase
            (hHO-1) and a fusion protein of hHO-1 with human cytochrome P450
            reductase
  JOURNAL   Biochemistry 34 (13), 4421-4427 (1995)
   PUBMED   7703255
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Shibahara,S., Sato,M., Muller,R.M. and Yoshida,T.
  TITLE     Structural organization of the human heme oxygenase gene and the
            function of its promoter
  JOURNAL   Eur J Biochem 179 (3), 557-563 (1989)
   PUBMED   2537723
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Keyse,S.M. and Tyrrell,R.M.
  TITLE     Heme oxygenase is the major 32-kDa stress protein induced in human
            skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium
            arsenite
  JOURNAL   Proc Natl Acad Sci U S A 86 (1), 99-103 (1989)
   PUBMED   2911585
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Yoshida,T., Biro,P., Cohen,T., Muller,R.M. and Shibahara,S.
  TITLE     Human heme oxygenase cDNA and induction of its mRNA by hemin
  JOURNAL   Eur J Biochem 171 (3), 457-461 (1988)
   PUBMED   3345742
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP288767.1, X06985.1 and
            CA306357.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Heme oxygenase, an essential enzyme in heme catabolism,
            cleaves heme to form biliverdin, which is subsequently converted to
            bilirubin by biliverdin reductase, and carbon monoxide, a putative
            neurotransmitter. Heme oxygenase activity is induced by its
            substrate heme and by various nonheme substances. Heme oxygenase
            occurs as 2 isozymes, an inducible heme oxygenase-1 and a
            constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme
            oxygenase family. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1099521.1, X06985.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216117.9/ ENSP00000216117.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..288
                     /product="heme oxygenase 1"
                     /EC_number="1.14.14.18"
                     /note="heat shock protein, 32-kD; heme oxygenase
                     (decycling) 1"
                     /calculated_mol_wt=32688
     Region          11..216
                     /region_name="Heme_oxygenase"
                     /note="Heme oxygenase; pfam01126"
                     /db_xref="CDD:395895"
     Site            order(18,25,28..29,57,134..136,138..139,143,147,179,183,
                     207,210,214)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:350855"
     Region          127..154
                     /region_name="kinked helix"
                     /note="kinked helix [structural motif]"
                     /db_xref="CDD:350855"
     Site            140
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000269|PubMed:11121422; propagated from
                     UniProtKB/Swiss-Prot (P09601.1)"
     Region          223..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09601.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P09601.1)"
     Site            266..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P09601.1)"
     CDS             1..288
                     /gene="HMOX1"
                     /gene_synonym="bK286B10; HMOX1D; HO-1; HSP32"
                     /coded_by="NM_002133.3:79..945"
                     /db_xref="CCDS:CCDS13914.1"
                     /db_xref="GeneID:3162"
                     /db_xref="HGNC:HGNC:5013"
                     /db_xref="MIM:141250"
ORIGIN      
        1 merpqpdsmp qdlsealkea tkevhtqaen aefmrnfqkg qvtrdgfklv maslyhiyva
       61 leeeiernke spvfapvyfp eelhrkaale qdlafwygpr wqevipytpa mqryvkrlhe
      121 vgrtepellv ahaytrylgd lsggqvlkki aqkaldlpss geglafftfp niasatkfkq
      181 lyrsrmnsle mtpavrqrvi eeaktaflln iqlfeelqel lthdtkdqsp srapglrqra
      241 snkvqdsapv etprgkppln trsqapllrw vltlsflvat vavglyam
//
LOCUS       NP_872299                819 aa            linear   PRI 27-APR-2025
DEFINITION  myosin light chain kinase 3 isoform 1 [Homo sapiens].
ACCESSION   NP_872299
VERSION     NP_872299.2
DBSOURCE    REFSEQ: accession NM_182493.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Tobita,T., Nomura,S., Morita,H., Ko,T., Fujita,T., Toko,H., Uto,K.,
            Hagiwara,N., Aburatani,H. and Komuro,I.
  TITLE     Identification of MYLK3 mutations in familial dilated
            cardiomyopathy
  JOURNAL   Sci Rep 7 (1), 17495 (2017)
   PUBMED   29235529
  REMARK    GeneRIF: Study identified MYLK3 mutations associated with familial
            dilated cardiomyopathy. In vitro experiments and
            immunohistochemistry suggested that the MYLK3 mutations identified
            in this study result in markedly reduced levels of protein
            expression and myosin light chain 2 phosphorylation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Samak,G., Gangwar,R., Crosby,L.M., Desai,L.P., Wilhelm,K.,
            Waters,C.M. and Rao,R.
  TITLE     Cyclic stretch disrupts apical junctional complexes in Caco-2 cell
            monolayers by a JNK-2-, c-Src-, and MLCK-dependent mechanism
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 306 (11), G947-G958 (2014)
   PUBMED   24722904
  REMARK    GeneRIF: This study demonstrates that cyclic stretch disrupts tight
            junctions and adherens junctions by a JNK2, c-Src, and
            MLCK-dependent mechanism.
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Kuo,C.Y., Chou,T.Y., Chen,C.M., Tsai,Y.F., Hwang,G.Y. and
            Hwang,T.L.
  TITLE     Hepatitis B virus X protein disrupts stress fiber formation and
            triggers apoptosis
  JOURNAL   Virus Res 175 (1), 20-29 (2013)
   PUBMED   23591626
  REMARK    GeneRIF: These findings suggest that hepatitis B virus X protein
            disrupts stress fiber formation and triggers apoptosis via an MLCK
            and a PTEN-dependent pathway.
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Tsukamoto,O. and Kitakaze,M.
  TITLE     Biochemical and physiological regulation of cardiac myocyte
            contraction by cardiac-specific myosin light chain kinase
  JOURNAL   Circ J 77 (9), 2218-2225 (2013)
   PUBMED   23863751
  REMARK    GeneRIF: Biochemical and physiological regulation of cardiac
            myocyte contraction by cardiac-specific myosin light chain kinase.
            Review article
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Al-Sadi,R., Ye,D., Dokladny,K. and Ma,T.Y.
  TITLE     Mechanism of IL-1beta-induced increase in intestinal epithelial
            tight junction permeability
  JOURNAL   J Immunol 180 (8), 5653-5661 (2008)
   PUBMED   18390750
  REMARK    GeneRIF: data indicate that the IL-1beta-induced increase in MLCK
            protein expression and Caco-2 TJ permeability was mediated by an
            increase in MLCK expression and activity and by an
            NF-kappaB-dependent increase in MLCK gene transcription
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Chan,J.Y., Takeda,M., Briggs,L.E., Graham,M.L., Lu,J.T.,
            Horikoshi,N., Weinberg,E.O., Aoki,H., Sato,N., Chien,K.R. and
            Kasahara,H.
  TITLE     Identification of cardiac-specific myosin light chain kinase
  JOURNAL   Circ Res 102 (5), 571-580 (2008)
   PUBMED   18202317
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Seguchi,O., Takashima,S., Yamazaki,S., Asakura,M., Asano,Y.,
            Shintani,Y., Wakeno,M., Minamino,T., Kondo,H., Furukawa,H.,
            Nakamaru,K., Naito,A., Takahashi,T., Ohtsuka,T., Kawakami,K.,
            Isomura,T., Kitamura,S., Tomoike,H., Mochizuki,N. and Kitakaze,M.
  TITLE     A cardiac myosin light chain kinase regulates sarcomere assembly in
            the vertebrate heart
  JOURNAL   J Clin Invest 117 (10), 2812-2824 (2007)
   PUBMED   17885681
  REMARK    GeneRIF: Integrated cDNA expression analysis of failing human
            myocardia uncovered a novel protein kinase, cardiac-specific myosin
            light chain kinase (cardiac-MLCK), which acts on MLC2v.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007225.2, AJ247087.1, DA561361.1, CR739116.1 and AL691746.1.
            
            On May 3, 2007 this sequence version replaced NP_872299.1.
            
            Summary: Phosphorylation of cardiac myosin heavy chains (see MYH7B,
            MIM 609928) and light chains (see MYL2, MIM 160781) by a kinase,
            such as MYLK3, potentiates the force and rate of cross-bridge
            recruitment in cardiac myocytes (Chan et al., 2008 [PubMed
            18202317]).[supplied by OMIM, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ247087.1, BC109096.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394809.9/ ENSP00000378288.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q11.2"
     Protein         1..819
                     /product="myosin light chain kinase 3 isoform 1"
                     /EC_number="2.7.11.18"
                     /note="MLC kinase; cardiac-MyBP-C associated Ca/CaM
                     kinase; putative myosin light chain kinase 3;
                     cardiac-MLCK"
                     /calculated_mol_wt=88262
     Region          146..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32MK0.3)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PT87; propagated from
                     UniProtKB/Swiss-Prot (Q32MK0.3)"
     Region          273..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32MK0.3)"
     Region          347..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32MK0.3)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PT87; propagated from
                     UniProtKB/Swiss-Prot (Q32MK0.3)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q32MK0.3)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q32MK0.3)"
     Region          510..770
                     /region_name="STKc_MLCK3"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Myosin Light Chain Kinase 3; cd14192"
                     /db_xref="CDD:271094"
     Site            order(521..525,527,529,542,544,573,589..590,592,596,598,
                     636,638,640..641,643,655..656,659,674..677)
                     /site_type="active"
                     /db_xref="CDD:271094"
     Site            order(521..525,527,529,542,544,573,589..590,592,596,
                     640..641,643,655..656)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271094"
     Site            order(525,596,598,636,638,640,659,674..677)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271094"
     Site            655..677
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271094"
     CDS             1..819
                     /gene="MYLK3"
                     /gene_synonym="caMLCK; MLCK; MLCK2"
                     /coded_by="NM_182493.3:152..2611"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10723.2"
                     /db_xref="GeneID:91807"
                     /db_xref="HGNC:HGNC:29826"
                     /db_xref="MIM:612147"
ORIGIN      
        1 msgtskeslg hgglpglgkt clttmdtkln mlnekvdqll hfqedvtekl qsmcrdmghl
       61 erglhrleas rapgpggadg vphidtqagw pevlelvram qqdaaqhgar lealfrmvaa
      121 vdraialvga tfqkskvadf lmqgrvpwrr gspgdspeen kerveeeggk pkhvlstsgv
      181 qsdarepgee sqkadvlegt aerlppiras glgadpaqav vspgqgdgvp gpaqafpghl
      241 plptkveaka petpsenlrt glelapapgr vnvvspslev apgagqgass srpdpeplee
      301 gtrltpgpgp qcpgppglpa qarathsgge tpprisihiq emdtpgemlm tgrgslgptl
      361 tteapaaaqp gkqgppgtgr clqapgtepg eqtpegarel splqessspg gvkaeeeqra
      421 gaepgtrpsl arsddndhev galglqqgks pgagnpepeq dcaarapvra eavrrmppga
      481 eagsvvldds pappapfehr vvsvketsis agyevcqhev lgggrfgqvh rctekstglp
      541 laakiikvks akdredvkne inimnqlshv nliqlydafe skhsctlvme yvdggelfdr
      601 itdekyhlte ldvvlftrqi cegvhylhqh yilhldlkpe nilcvnqtgh qikiidfgla
      661 rrykpreklk vnfgtpefla pevvnyefvs fptdmwsvgv itymllsgls pflgetdaet
      721 mnfivncswd fdadtfegls eeakdfvsrl lvkekscrms atqclkhewl nnlpakasrs
      781 ktrlksqlll qkyiaqrkwk khfyvvtaan rlrkfptsp
//
LOCUS       NP_694816                781 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial inner membrane m-AAA protease component paraplegin
            isoform 1 preproprotein [Mus musculus].
ACCESSION   NP_694816
VERSION     NP_694816.3
DBSOURCE    REFSEQ: accession NM_153176.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Montoro-Gamez,C., Nolte,H., Molinie,T., Evangelista,G.,
            Troder,S.E., Barth,E., Popovic,M., Trifunovic,A., Zevnik,B.,
            Langer,T. and Rugarli,E.I.
  TITLE     SARM1 deletion delays cerebellar but not spinal cord degeneration
            in an enhanced mouse model of SPG7 deficiency
  JOURNAL   Brain 146 (10), 4117-4131 (2023)
   PUBMED   37086482
  REMARK    GeneRIF: SARM1 deletion delays cerebellar but not spinal cord
            degeneration in an enhanced mouse model of SPG7 deficiency.
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Sambri,I., Massa,F., Gullo,F., Meneghini,S., Cassina,L.,
            Carraro,M., Dina,G., Quattrini,A., Patanella,L., Carissimo,A.,
            Iuliano,A., Santorelli,F., Codazzi,F., Grohovaz,F., Bernardi,P.,
            Becchetti,A. and Casari,G.
  TITLE     Impaired flickering of the permeability transition pore causes SPG7
            spastic paraplegia
  JOURNAL   EBioMedicine 61, 103050 (2020)
   PUBMED   33045469
  REMARK    GeneRIF: Impaired flickering of the permeability transition pore
            causes SPG7 spastic paraplegia.
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Schatton,D., Pla-Martin,D., Marx,M.C., Hansen,H., Mourier,A.,
            Nemazanyy,I., Pessia,A., Zentis,P., Corona,T., Kondylis,V.,
            Barth,E., Schauss,A.C., Velagapudi,V. and Rugarli,E.I.
  TITLE     CLUH regulates mitochondrial metabolism by controlling translation
            and decay of target mRNAs
  JOURNAL   J Cell Biol 216 (3), 675-693 (2017)
   PUBMED   28188211
REFERENCE   4  (residues 1 to 781)
  AUTHORS   Mancuso,G., Barth,E., Crivello,P. and Rugarli,E.I.
  TITLE     Alternative splicing of Spg7, a gene involved in hereditary spastic
            paraplegia, encodes a variant of paraplegin targeted to the
            endoplasmic reticulum
  JOURNAL   PLoS One 7 (5), e36337 (2012)
   PUBMED   22563492
  REMARK    GeneRIF: Studies indicate that both mouse and human SPG7 ESTs
            containing alternative first exons.
REFERENCE   5  (residues 1 to 781)
  AUTHORS   Koppen,M., Bonn,F., Ehses,S. and Langer,T.
  TITLE     Autocatalytic processing of m-AAA protease subunits in mitochondria
  JOURNAL   Mol Biol Cell 20 (19), 4216-4224 (2009)
   PUBMED   19656850
  REMARK    GeneRIF: Data show that Afg3l1 or Afg3l2 are required for
            maturation of newly imported paraplegin subunits after their
            cleavage by MPP.
REFERENCE   6  (residues 1 to 781)
  AUTHORS   Pirozzi,M., Quattrini,A., Andolfi,G., Dina,G., Malaguti,M.C.,
            Auricchio,A. and Rugarli,E.I.
  TITLE     Intramuscular viral delivery of paraplegin rescues peripheral
            axonopathy in a model of hereditary spastic paraplegia
  JOURNAL   J Clin Invest 116 (1), 202-208 (2006)
   PUBMED   16357941
  REMARK    Erratum:[J Clin Invest. 2014 Feb;124(2):871]
REFERENCE   7  (residues 1 to 781)
  AUTHORS   Nolden,M., Ehses,S., Koppen,M., Bernacchia,A., Rugarli,E.I. and
            Langer,T.
  TITLE     The m-AAA protease defective in hereditary spastic paraplegia
            controls ribosome assembly in mitochondria
  JOURNAL   Cell 123 (2), 277-289 (2005)
   PUBMED   16239145
REFERENCE   8  (residues 1 to 781)
  AUTHORS   Nishimura,M., Yokoi,N., Miki,T., Horikawa,Y., Yoshioka,H.,
            Takeda,J., Ohara,O. and Seino,S.
  TITLE     Construction of a multi-functional cDNA library specific for mouse
            pancreatic islets and its application to microarray
  JOURNAL   DNA Res 11 (5), 315-323 (2004)
   PUBMED   15747579
REFERENCE   9  (residues 1 to 781)
  AUTHORS   Ferreirinha,F., Quattrini,A., Pirozzi,M., Valsecchi,V., Dina,G.,
            Broccoli,V., Auricchio,A., Piemonte,F., Tozzi,G., Gaeta,L.,
            Casari,G., Ballabio,A. and Rugarli,E.I.
  TITLE     Axonal degeneration in paraplegin-deficient mice is associated with
            abnormal mitochondria and impairment of axonal transport
  JOURNAL   J Clin Invest 113 (2), 231-242 (2004)
   PUBMED   14722615
REFERENCE   10 (residues 1 to 781)
  AUTHORS   Molla,A., Rouard-Talbot,L. and Block,M.R.
  TITLE     Cotranscription of two RNA coding for the cell adhesion regulator
            and its variant in Reh leukemia cells
  JOURNAL   Biochim Biophys Acta 1315 (1), 6-8 (1996)
   PUBMED   8611648
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK145540.1 and BP770238.1.
            
            On Jun 3, 2007 this sequence version replaced NP_694816.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF512565.1, AF547215.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 72.04 cM"
     Protein         1..781
                     /product="mitochondrial inner membrane m-AAA protease
                     component paraplegin isoform 1 preproprotein"
                     /note="paraplegin; cell matrix adhesion regulator; spastic
                     paraplegia 7 protein; spastic paraplegia 7 homolog;
                     mitochondrial inner membrane m-AAA protease component
                     paraplegin"
                     /calculated_mol_wt=81463
     transit_peptide 1..43
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:19656850; propagated from
                     UniProtKB/Swiss-Prot (Q3ULF4.1)"
                     /calculated_mol_wt=4551
     Region          22..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ULF4.1)"
     Region          103..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ULF4.1)"
     mat_peptide     106..781
                     /product="Mitochondrial inner membrane m-AAA protease
                     component paraplegin. /id=PRO_0000442307"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ULF4.1)"
                     /calculated_mol_wt=75004
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ULF4.1)"
     Region          147..749
                     /region_name="HflB"
                     /note="ATP-dependent Zn proteases [Posttranslational
                     modification, protein turnover, chaperones]; COG0465"
                     /db_xref="CDD:440233"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ULF4.1)"
     Region          701..781
                     /region_name="Interaction with PPIF.
                     /evidence=ECO:0000250|UniProtKB:Q9UQ90"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ULF4.1)"
     CDS             1..781
                     /gene="Spg7"
                     /gene_synonym="Cmar; PGN"
                     /coded_by="NM_153176.5:20..2365"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS40508.1"
                     /db_xref="GeneID:234847"
                     /db_xref="MGI:MGI:2385906"
ORIGIN      
        1 maaallllrg lrpgpeprpr rlwgllsgrg pglssgagar rpyaargtpv gpaaagghap
       61 qslllriltp sfegisglll kqhivpnavr lwplsgstly fntsrmkqkn kdndkpkgkt
      121 peddeeekrr keredqmyre rlrtlfiial vmsllnslst sggsiswadf vnemlakgev
      181 qrvqvvpesd vvevylhpga vvfgrprlal myrmqvanid kfeeklraae delnieskdr
      241 ipvsykrtgf fgnalyalgm tavglailwy vfrlagmtgr eggfsafnql kmarftivdg
      301 ktgkgvsfqd vagmheakle vrefvdylks perflqlgak vpkgalllgp pgcgktllak
      361 avateaqvpf lamagpefve vigglgaarv rslfkearar apcivyidei davgkkrsts
      421 msgfsnteee qtlnqllvem dgmgttdhvi vlastnradv ldnalmrpgr ldrhvfidlp
      481 tlqerreife qhlkglkltq pssfysqrla eltpgfsgad ianicneaal haareghtsv
      541 htfnfeyave rviagtakks kilskeeqrv vafhesghal vgwllehtea vmkvsiaprt
      601 naalgfsqml prdqylftke qlfermcmal ggraaeaisf srvtsgaqdd lrkvtriays
      661 mvkqfgmaps igpvsfpeaq eglmgigrrp fsqglqqmmd heakllvaka yrhtekvlld
      721 nldklqalan allekeviny ediealigpp phgpkkmiap qkwidaeker qasgeeeapa
      781 p
//
LOCUS       NP_056453                797 aa            linear   PRI 27-APR-2025
DEFINITION  short transient receptor potential channel 4-associated protein
            isoform a [Homo sapiens].
ACCESSION   NP_056453
VERSION     NP_056453.1
DBSOURCE    REFSEQ: accession NM_015638.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Choukair,D., Eberle,B., Vick,P., Hermanns,P., Weiss,B.,
            Paramasivam,N., Schlesner,M., Lornsen,K., Roeth,R., Klutmann,C.,
            Kreis,J., Hoffmann,G.F., Pohlenz,J., Rappold,G.A. and Bettendorf,M.
  TITLE     Identification of Transient Receptor Potential Channel 4-Associated
            Protein as a Novel Candidate Gene Causing Congenital Primary
            Hypothyroidism
  JOURNAL   Horm Res Paediatr 93 (1), 16-29 (2020)
   PUBMED   32428920
  REMARK    GeneRIF: Identification of Transient Receptor Potential Channel
            4-Associated Protein as a Novel Candidate Gene Causing Congenital
            Primary Hypothyroidism.
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Yu,C.J., Wang,Q.S., Wu,M.M., Song,B.L., Liang,C., Lou,J.,
            Tang,L.L., Yu,X.D., Niu,N., Yang,X., Zhang,B.L., Qu,Y., Liu,Y.,
            Dong,Z.C. and Zhang,Z.R.
  TITLE     TRUSS Exacerbates NAFLD Development by Promoting IkappaBalpha
            Degradation in Mice
  JOURNAL   Hepatology 68 (5), 1769-1785 (2018)
   PUBMED   29704259
  REMARK    GeneRIF: Hepatocyte TRUSS promotes pathological stimuli-induced non
            alcoholic fatty liver disease and metabolic disorders, through
            activation of NF-kappaB by promoting ubiquitination and degradation
            of IkappaBalpha
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Koren,I., Timms,R.T., Kula,T., Xu,Q., Li,M.Z. and Elledge,S.J.
  TITLE     The Eukaryotic Proteome Is Shaped by E3 Ubiquitin Ligases Targeting
            C-Terminal Degrons
  JOURNAL   Cell 173 (7), 1622-1635 (2018)
   PUBMED   29779948
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Jamal,A., Swarnalatha,M., Sultana,S., Joshi,P., Panda,S.K. and
            Kumar,V.
  TITLE     The G1 phase E3 ubiquitin ligase TRUSS that gets deregulated in
            human cancers is a novel substrate of the S-phase E3 ubiquitin
            ligase Skp2
  JOURNAL   Cell Cycle 14 (16), 2688-2700 (2015)
   PUBMED   26038816
  REMARK    GeneRIF: TRUSS is a novel substrate of E3 ligase Skp2.
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Tang,W., Schwienbacher,C., Lopez,L.M., Ben-Shlomo,Y.,
            Oudot-Mellakh,T., Johnson,A.D., Samani,N.J., Basu,S., Gogele,M.,
            Davies,G., Lowe,G.D., Tregouet,D.A., Tan,A., Pankow,J.S.,
            Tenesa,A., Levy,D., Volpato,C.B., Rumley,A., Gow,A.J., Minelli,C.,
            Yarnell,J.W., Porteous,D.J., Starr,J.M., Gallacher,J.,
            Boerwinkle,E., Visscher,P.M., Pramstaller,P.P., Cushman,M.,
            Emilsson,V., Plump,A.S., Matijevic,N., Morange,P.E., Deary,I.J.,
            Hicks,A.A. and Folsom,A.R.
  TITLE     Genetic associations for activated partial thromboplastin time and
            prothrombin time, their gene expression profiles, and risk of
            coronary artery disease
  JOURNAL   Am J Hum Genet 91 (1), 152-162 (2012)
   PUBMED   22703881
REFERENCE   6  (residues 1 to 797)
  AUTHORS   Jikuya,H., Takano,J., Kikuno,R., Hirosawa,M., Nagase,T., Nomura,N.
            and Ohara,O.
  TITLE     Characterization of long cDNA clones from human adult spleen. II.
            The complete sequences of 81 cDNA clones
  JOURNAL   DNA Res 10 (1), 49-57 (2003)
   PUBMED   12693554
REFERENCE   7  (residues 1 to 797)
  AUTHORS   Antoniou,A.N., Ford,S., Pilley,E.S., Blake,N. and Powis,S.J.
  TITLE     Interactions formed by individually expressed TAP1 and TAP2
            polypeptide subunits
  JOURNAL   Immunology 106 (2), 182-189 (2002)
   PUBMED   12047747
REFERENCE   8  (residues 1 to 797)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   9  (residues 1 to 797)
  AUTHORS   Gaudet,R. and Wiley,D.C.
  TITLE     Structure of the ABC ATPase domain of human TAP1, the transporter
            associated with antigen processing
  JOURNAL   EMBO J 20 (17), 4964-4972 (2001)
   PUBMED   11532960
REFERENCE   10 (residues 1 to 797)
  AUTHORS   Ritz,U., Momburg,F., Pircher,H.P., Strand,D., Huber,C. and
            Seliger,B.
  TITLE     Identification of sequences in the human peptide transporter
            subunit TAP1 required for transporter associated with antigen
            processing (TAP) function
  JOURNAL   Int Immunol 13 (1), 31-41 (2001)
   PUBMED   11133832
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM149369.1, BC013144.1, BI488542.1, CF125531.1, BM723903.1 and
            BC008836.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.31176.1,
                                           SRR1660803.37423.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252015.3/ ENSP00000252015.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..797
                     /product="short transient receptor potential channel
                     4-associated protein isoform a"
                     /note="tumor necrosis factor receptor-associated
                     ubiquitous scaffolding and signaling protein;
                     TRP4-associated protein; short transient receptor
                     potential channel 4-associated protein; trpc4-associated
                     protein; TNF-receptor ubiquitous scaffolding/signaling
                     protein; protein phosphatase 1, regulatory subunit 158"
                     /calculated_mol_wt=90721
     Region          2..400
                     /region_name="Interaction with TNFRSF1A.
                     /evidence=ECO:0000250|UniProtKB:Q9JLV2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEL6.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8TEL6.2)"
     Region          407..713
                     /region_name="DUF3689"
                     /note="Protein of unknown function (DUF3689); pfam12463"
                     /db_xref="CDD:463595"
     CDS             1..797
                     /gene="TRPC4AP"
                     /gene_synonym="C20orf188; PPP1R158; TRRP4AP; TRUSS"
                     /coded_by="NM_015638.3:27..2420"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13246.1"
                     /db_xref="GeneID:26133"
                     /db_xref="HGNC:HGNC:16181"
                     /db_xref="MIM:608430"
ORIGIN      
        1 maaapvaags gagrgrrsaa tvaawggwgg rprpgnillq lrqgqltgrg lvravqftet
       61 flterdkqsk wsgipqlllk lhttshlhsd fvecqnilke ispllsmeam afvteerklt
      121 qettypntyi fdlfggvdll veilmrptis irgqklkisd emskdclsil yntcvctegv
      181 tkrlaekndf viflftlmts kktflqtatl iedilgvkke mirldevpnl sslvsnfdqq
      241 qlanfcrila vtisemdtgn ddkhtllakn aqqkkslslg psaaeinqaa llsipgfver
      301 lcklatrkvs estgtasflq eleewytwld nalvldalmr vaneesehnq asivfpppga
      361 seenglphts artqlpqsmk imheimykle vlyvlcvllm grqrnqvhrm iaefklipgl
      421 nnlfdkliwr khsasalvlh ghnqncdcsp ditlkiqflr llqsfsdhhe nkylllnnqe
      481 lnelsaislk anipeveavl ntdrslvcdg krglltrllq vmkkepaess frfwqarave
      541 sflrgttsya dqmfllkrgl lehilycivd secksrdvlq syfdllgelm kfnvdafkrf
      601 nkyintdakf qvflkqinss lvdsnmlvrc vtlsldrfen qvdmkvaevl secrllayis
      661 qvptqmsflf rliniihvqt ltqenvscln tslvilmlar rkerlplylr llqrmehskk
      721 ypgfllnnfh nllrfwqqhy lhkdkdstcl ensscisfsy wketvsilln pdrqspsalv
      781 syieepymdi drdftee
//
LOCUS       NP_115495               6306 aa            linear   PRI 27-APR-2025
DEFINITION  adhesion G-protein coupled receptor V1 precursor [Homo sapiens].
ACCESSION   NP_115495
VERSION     NP_115495.3
DBSOURCE    REFSEQ: accession NM_032119.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 6306)
  AUTHORS   Linnert,J., Guler,B.E., Krzysko,J. and Wolfrum,U.
  TITLE     The adhesion G protein-coupled receptor VLGR1/ADGRV1 controls
            autophagy
  JOURNAL   Basic Clin Pharmacol Toxicol 133 (4), 313-330 (2023)
   PUBMED   37002809
  REMARK    GeneRIF: The adhesion G protein-coupled receptor VLGR1/ADGRV1
            controls autophagy.
REFERENCE   2  (residues 1 to 6306)
  AUTHORS   Guler,B.E., Linnert,J. and Wolfrum,U.
  TITLE     Monitoring paxillin in astrocytes reveals the significance of the
            adhesion G protein coupled receptor VLGR1/ADGRV1 for focal adhesion
            assembly
  JOURNAL   Basic Clin Pharmacol Toxicol 133 (4), 301-312 (2023)
   PUBMED   36929698
  REMARK    GeneRIF: Monitoring paxillin in astrocytes reveals the significance
            of the adhesion G protein coupled receptor VLGR1/ADGRV1 for focal
            adhesion assembly.
REFERENCE   3  (residues 1 to 6306)
  AUTHORS   Leng,X., Zhang,T., Guan,Y. and Tang,M.
  TITLE     Genotype and phenotype analysis of epilepsy caused by ADGRV1
            mutations in Chinese children
  JOURNAL   Seizure 103, 108-114 (2022)
   PUBMED   36399868
  REMARK    GeneRIF: Genotype and phenotype analysis of epilepsy caused by
            ADGRV1 mutations in Chinese children.
REFERENCE   4  (residues 1 to 6306)
  AUTHORS   Knapp,B., Roedig,J., Roedig,H., Krzysko,J., Horn,N., Guler,B.E.,
            Kusuluri,D.K., Yildirim,A., Boldt,K., Ueffing,M., Liebscher,I. and
            Wolfrum,U.
  TITLE     Affinity Proteomics Identifies Interaction Partners and Defines
            Novel Insights into the Function of the Adhesion GPCR VLGR1/ADGRV1
  JOURNAL   Molecules 27 (10), 3108 (2022)
   PUBMED   35630584
  REMARK    GeneRIF: Affinity Proteomics Identifies Interaction Partners and
            Defines Novel Insights into the Function of the Adhesion GPCR
            VLGR1/ADGRV1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 6306)
  AUTHORS   Fakin,A., Bonnet,C., Kurtenbach,A., Mohand-Said,S., Zobor,D.,
            Stingl,K., Testa,F., Simonelli,F., Sahel,J.A., Audo,I., Zrenner,E.,
            Hawlina,M. and Petit,C.
  TITLE     Characteristics of Retinitis Pigmentosa Associated with ADGRV1 and
            Comparison with USH2A in Patients from a Multicentric Usher
            Syndrome Study Treatrush
  JOURNAL   Int J Mol Sci 22 (19), 10352 (2021)
   PUBMED   34638692
  REMARK    GeneRIF: Characteristics of Retinitis Pigmentosa Associated with
            ADGRV1 and Comparison with USH2A in Patients from a Multicentric
            Usher Syndrome Study Treatrush.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 6306)
  AUTHORS   Pieke-Dahl,S., Moller,C.G., Kelley,P.M., Astuto,L.M., Cremers,C.W.,
            Gorin,M.B. and Kimberling,W.J.
  TITLE     Genetic heterogeneity of Usher syndrome type II: localisation to
            chromosome 5q
  JOURNAL   J Med Genet 37 (4), 256-262 (2000)
   PUBMED   10745043
REFERENCE   7  (residues 1 to 6306)
  AUTHORS   Nakayama,J., Hamano,K., Iwasaki,N., Nakahara,S., Horigome,Y.,
            Saitoh,H., Aoki,T., Maki,T., Kikuchi,M., Migita,T., Ohto,T.,
            Yokouchi,Y., Tanaka,R., Hasegawa,M., Matsui,A., Hamaguchi,H. and
            Arinami,T.
  TITLE     Significant evidence for linkage of febrile seizures to chromosome
            5q14-q15
  JOURNAL   Hum Mol Genet 9 (1), 87-91 (2000)
   PUBMED   10587582
REFERENCE   8  (residues 1 to 6306)
  AUTHORS   Hmani,M., Ghorbel,A., Boulila-Elgaied,A., Ben Zina,Z., Kammoun,W.,
            Drira,M., Chaabouni,M., Petit,C. and Ayadi,H.
  TITLE     A novel locus for Usher syndrome type II, USH2B, maps to chromosome
            3 at p23-24.2
  JOURNAL   Eur J Hum Genet 7 (3), 363-367 (1999)
   PUBMED   10234513
REFERENCE   9  (residues 1 to 6306)
  AUTHORS   Pieke Dahl,S., Kimberling,W.J., Gorin,M.B., Weston,M.D.,
            Furman,J.M., Pikus,A. and Moller,C.
  TITLE     Genetic heterogeneity of Usher syndrome type II
  JOURNAL   J Med Genet 30 (10), 843-848 (1993)
   PUBMED   7901420
REFERENCE   10 (residues 1 to 6306)
  AUTHORS   Koenekoop,R., Arriaga,M., Trzupek,K.M. and Lentz,J.
  TITLE     Usher Syndrome Type II
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027323.5, AC093529.2,
            AC094109.2, AC099512.2, AC034215.4, AC074132.5 and AC093281.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 31, 2006 this sequence version replaced NP_115495.2.
            
            Summary: This gene encodes a member of the G-protein coupled
            receptor superfamily. The encoded protein contains a
            7-transmembrane receptor domain, binds calcium and is expressed in
            the central nervous system. Mutations in this gene are associated
            with Usher syndrome 2 and familial febrile seizures. Several
            alternatively spliced transcripts have been described. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF435925.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267750, SAMN03267768
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000405460.9/ ENSP00000384582.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..6306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.3"
     Protein         1..6306
                     /product="adhesion G-protein coupled receptor V1
                     precursor"
                     /note="G-protein coupled receptor 98; usher syndrome
                     type-2C protein; very large G-protein coupled receptor 1;
                     monogenic audiogenic seizure susceptibility protein 1
                     homolog"
                     /calculated_mol_wt=690083
     sig_peptide     1..29
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WXG9.2)"
                     /calculated_mol_wt=3008
     mat_peptide     30..6306
                     /product="Adhesion G-protein coupled receptor V1.
                     /id=PRO_0000232735"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
                     /calculated_mol_wt=690083
     mat_peptide     30..5890
                     /product="ADGRV1 subunit alpha.
                     /evidence=ECO:0000250|UniProtKB:Q8VHN7.
                     /id=PRO_0000445731"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
                     /calculated_mol_wt=644019
     Region          <53..>236
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <330..>487
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <859..>1092
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <1000..>1207
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          1346..1495
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Region          <1503..>1693
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <1626..>1808
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <1729..>1947
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <1999..>2205
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <2140..>2323
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <2495..>2675
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <2606..>2789
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          2843..2925
                     /region_name="Calx-beta"
                     /note="Calx-beta domain; cl02522"
                     /db_xref="CDD:413355"
     Region          <2962..>3174
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          3255..3296
                     /region_name="EAR 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00075"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          3297..3345
                     /region_name="EAR 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00075"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          3348..3393
                     /region_name="EAR 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00075"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          3395..3439
                     /region_name="EAR 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00075"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          3396..3437
                     /region_name="EPTP"
                     /note="EPTP domain; pfam03736"
                     /db_xref="CDD:461033"
     Region          3441..3488
                     /region_name="EAR 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00075"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          3492..3534
                     /region_name="EAR 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00075"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          <3585..>3726
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <3793..>4005
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          4032..4122
                     /region_name="Calx-beta"
                     /note="Calx-beta domain; cl02522"
                     /db_xref="CDD:413355"
     Region          <4284..>4488
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <4971..>5094
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <5040..>5336
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          <5293..>5387
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          5853..5895
                     /region_name="GPS"
                     /note="GPCR proteolysis site, GPS, motif; cl02559"
                     /db_xref="CDD:470616"
     Region          5856..5903
                     /region_name="GPS.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Site            5890..5891
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098; propagated
                     from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     mat_peptide     5891..6306
                     /product="ADGRV1 subunit beta.
                     /evidence=ECO:0000250|UniProtKB:Q8VHN7.
                     /id=PRO_0000445732"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
                     /calculated_mol_wt=46082
     Site            5909..5929
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          5919..6158
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          5938..5959
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            5940..5960
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          5971..5993
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            5980..6000
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Site            6011..6031
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          6012..6028
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          6057..6080
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            6060..6080
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          6105..6127
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            6105..6125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          6131..6156
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            6134..6154
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     Region          6216..6248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXG9.2)"
     CDS             1..6306
                     /gene="ADGRV1"
                     /gene_synonym="FEB4; GPR98; MASS1; USH2B; USH2C; VLGR1;
                     VLGR1b"
                     /coded_by="NM_032119.4:100..19020"
                     /db_xref="CCDS:CCDS47246.1"
                     /db_xref="GeneID:84059"
                     /db_xref="HGNC:HGNC:17416"
                     /db_xref="MIM:602851"
ORIGIN      
        1 msvflgpgmp sasllvnlls allilfvfge teirftgqte fvvnetsttv irliierige
       61 panvtaivsl ygedagdffd tyaaafipag etnrtvyiav cdddlpepde tfifhltlqk
      121 psanvklgwp rtvtvtilsn dnafgiisfn mlpsiavsep kgrnesmplt lirekgtygm
      181 vmvtfevegg pnppdedlsp vkgnitfppg ratviynltv lddevpende ifliqlksve
      241 ggaeintsrn sieiiikknd spvrflqsiy lvpeedhili ipvvrgkdnn gnligsdeye
      301 vsisyavttg nstahaqqnl dfidlqpntt vvfppfihes hlkfqivddt ipeiaesfhi
      361 mllkdtlqgd avlispsvvq vtikpndkpy gvlsfnsvlf ertviidedr isryeeitvv
      421 rnggthgnvs anwvltrnst dpspvtadir pssgvlhfaq gqmlatiplt vvdddlpeea
      481 eayllqilph tirggaevse paellfyiqd sddvyglitf fpmenqkies spgerylsls
      541 ftrlggtkgd vrllysvlyi pagavdplqa kegilnisrr ndlifpeqkt qvttklpirn
      601 daflqngahf lvqletvell niiplippis prfgeicnis llvtpaiang eigflsnlpi
      661 ilhepedfaa evvyiplhrd gtdgqatvyw slkpsgfnsk avtpddigpf ngsvlflsgq
      721 sdttinitik gddipemnet vtlsldrvnv enqvlksgyt srdliilend dpggvfefsp
      781 asrgpyvike gesvelhiir srgslvkqfl hyrveprdsn efygntgvle fkpgereivi
      841 tllarldgip eldehywvvl sshgereskl gsativniti lknddphgii efvsdglivm
      901 ineskgdaiy savydvvrnr gnfgdvsvsw vvspdftqdv fpvqgtvvfg dqefskniti
      961 yslpdeipee meeftvilln gtggakvgnr ttatlrirrn ddpiyfaepr vvrvqegeta
     1021 nftvlrngsv dvtcmvqyat kdgkatarer dfipvekget lifevgsrqq sisifvnedg
     1081 ipetdepfyi illnstgdtv vyqygvatvi ieanddpngi fslepidkav eegktnafwi
     1141 lrhrgyfgsv svswqlfqnd salqpgqefy etsgtvnfmd geeakpiilh afpdkipefn
     1201 efyflklvni sggspgpggq laetnlqvtv mvpfnddpfg vfildpecle revaedvlse
     1261 ddmsyitnft ilrqqgvfgd vqlgweilss efpaglppmi dfllvgifpt tvhlqqhmrr
     1321 hhsgtdalyf tglegafgtv npkyhpsrnn tianftfsaw vmpnantngf iiakddgngs
     1381 iyygvkiqtn eshvtlslhy ktlgsnatyi akttvmkyle esvwlhllii ledgiiefyl
     1441 dgnamprgik slkgeaitdg pgilrigagi ngndrftglm qdvrsyerkl tleeiyelha
     1501 mpaksdlhpi sgylefrqge tnksfiisar ddndeegeel filklvsvyg gariseentt
     1561 arltiqksdn anglfgftga cipeiaeegs tiscvvertr galdyvhvfy tisqietdgi
     1621 nylvddfana sgtitflpwq rsevlniyvl dddipelney frvtlvsaip gdgklgstpt
     1681 sgasidpeke ttditikasd hpygllqfst glppqpkdam tlpassvphi tveeedgeir
     1741 llviraqgll grvtaefrtv sltafspedy qnvagtlefq pgerykyifi nitdnsipel
     1801 eksfkvelln leggvaelfr vdgsgsgdgd mefflptihk raslgvasqi lvtiaasdha
     1861 hgvfefspes lfvsgteped gystvtlnvi rhhgtlspvt lhwnidsdpd gdlaftsgni
     1921 tfeigqtsan itveilpded peldkafsvs vlsvssgslg ahinatltvl asddpygifi
     1981 fseknrpvkv eeatqnitls iirlkglmgk vlvsyatldd mekppyfppn laratqgrdy
     2041 ipasgfalfg anqseatiai sildddeper sesvfielln stlvakvqsr sipnsprlgp
     2101 kvetiaqlii ianddafgtl qlsapivrva enhvgpiinv trtggafadv svkfkavpit
     2161 aiagedysia ssdvvllege tskavpiyvi ndiypelees flvqlmnett ggarlgalte
     2221 aviiieasdd pyglfgfqit kliveepefn svkvnlpiir nsgtlgnvtv qwvatingql
     2281 atgdlrvvsg nvtfapgeti qtlllevlad dvpeieeviq vqltdasggg tigldriani
     2341 iipanddpyg tvafaqmvyr vqeplerssc anitvrrsgg hfgrlllfys tsdidvvala
     2401 meegqdllsy yespiqgvpd plwrtwmnvs avgeplytca tlclkeqacs afsffsaseg
     2461 pqcfwmtswi spavnnsdfw tyrknmtrva slfsgqavag sdyepvtrqw aimqegdefa
     2521 nltvsilpdd fpemdesfli sllevhlmni saslknqpti gqpnistvvi alngdafgvf
     2581 viynispnts edglfvevqe qpqtlvelmi hrtggslgqv avewrvvggt ategldfiga
     2641 geiltfaege tkktviltil ddsepeddes iivslvyteg gsrilpssdt vrvnilandn
     2701 vagivsfqta srsvighege ilqfhvirtf pgrgnvtvnw kiigqnleln fanfsgqlff
     2761 pegslnttlf vhllddnipe ekevyqvily dvrtqgvppa gialldaqgy aavltveasd
     2821 ephgvlnfal ssrfvllqea nitiqlfinr efgslgainv tyttvpgmls lknqtvgnla
     2881 epevdfvpii gflileeget aaainitile ddvpeleeyf lvnltyvglt maastsfppr
     2941 ldsegltaqv iidandgarg viewqqsrfe vnethgsltl vaqrsreplg hvslfvyaqn
     3001 leaqvgldyi ftpmilhfad geryknvnim ildddipegd ekfqliltnp spglelgknt
     3061 ialiivland dgpgvlsfnn sehfflrept alyvqesvav lyivrepaqg lfgtvtvqfi
     3121 vtevnssnes kdltpskgyi vleegvrfka lqisaildte pemdeyfvct lfnptggarl
     3181 gvhvqtlitv lqnqaplglf sisavenrat sidieeanrt vylnvsrtng idlavsvqwe
     3241 tvsetafgmr gmdvvfsvfq sfldesasgw cfftlenliy gimlrkssvt vyrwqgifip
     3301 vedlnienpk tceafnigfs pyfvitheer neekpslnsv ftftsgfklf lvqtiiiles
     3361 sqvryftsds qdyliiasqr ddseltqvfr wnggsfvlhq klpvrgvltv alfnkggsvf
     3421 laisqanarl nsllfrwsgs gfinfqevpv sgtteveals sandiylifa envflgdqns
     3481 idifiwemgq ssfryfqsvd faavnrihsf tpasgiahil ligqdmsaly cwnsernqfs
     3541 fvlevpsayd vasvtvksln ssknlialvg ahshiyelay isshsdfips sgelifepge
     3601 reatiavnil ddtvpekees fkvqlknpkg gaeigindsv titilsndda ygivafaqns
     3661 lykqveemeq dslvtlnver lkgtygriti aweadgsisd ifptsgvilf tegqvlstit
     3721 ltiladnipe lsevvivtlt rittegveds ykgatidqdr sksvittlpn dspfglvgwr
     3781 aasvfirvae pkentttlql qiardkgllg diaihlraqp nfllhvdnqa tenedyvlqe
     3841 tiiimkenik eahaevsilp ddlpeleegf ivtitevnlv nsdfstgqps vrrpgmeiae
     3901 imieenddpr gifmfhvtrg agevitayev ppplnvlqvp vvrlagsfga vnvywkaspd
     3961 sagledfkps hgilefadkq vtamieitii ddaefeltet fnislisvag ggrlgddvvv
     4021 tvvipqndsp fgvfgfeekt vmideslssd dpdsyvtltv vrspggkgtv rlewtideka
     4081 khnlsplngt lhfdetesqk tivlhtlqdt vleedrrfti qlisidevei spvkgsasii
     4141 irgdkrasge vgiapssrhi ligepsakyn gtaiislvrg pgilgevtvf wrifppsvge
     4201 faetsgkltm rdeqsavivv iqalnddipe eksfyefqlt avseggvlse ssstanitvv
     4261 asdspygrfa fsheqlrvse aqrvnitiir ssgdfghvrl wyktmsgtae agldfvpaag
     4321 ellfeagemr kslhveildd dypegpeefs ltitkvelqg rgydftiqen glqidqppei
     4381 gnisivriii mkndnaegii efdpkytafe veedvglimi pvvrlhgtyg yvtadfisqs
     4441 ssaspggvdy ilhgstvtfq hgqnlsfini siiddnesef eepieilltg atggavlgrh
     4501 lvsriiiaks dspfgvirfl nqskisianp nstmilslvl ertggllgei qvnwetvgpn
     4561 sqeallpqnr diadpvsglf yfgegeggvr tiiltiyphe eieveetfii klhlvkgeak
     4621 ldsrakdvtl tiqefgdpng vvqfapetls kktyseplal egpllitffv rrvkgtfgei
     4681 mvywelssef ditedflsts gfftiadges easfdvhllp devpeieedy viqlvsvegg
     4741 aeldleksit wfsvyanddp hgvfalysdr qsiligqnli rsiqinitrl agtfgdvavg
     4801 lrissdhkeq pivtenaerq lvvkdgatyk vdvvpiknqv flslgsnftl qlvtvmlvgg
     4861 rfygmptilq eaksavlpvs ekaansqvgf estafqlmni tagtshvmis rrgtygalsv
     4921 awttgyapgl eipefivvgn mtptlgslsf shgeqrkgvf lwtfpspgwp eafvlhlsgv
     4981 qssapggaql rsgfivaeie pmgvfqfsts srniivsedt qmirlhvqrl fgfhsdlikv
     5041 syqttagsak pledfepvqn gelffqkfqt evdfeitiin dqlseieeff yinltsveir
     5101 glqkfdvnws prlnldfsva vitildnddl agmdisfpet tvavavdttl ipvetestty
     5161 lstsktttil qptnvvaivt eatgvsaipe klvtlhgtpa vsekpdvatv tanvsihgtf
     5221 slgpsivyie eemkngtfnt aevlirrtgg ftgnvsitvk tfgercaqme pnalpfrgiy
     5281 gisnltwave eedfeeqtlt lifldgerer kvsvqilddd epegqeffyv fltnpqggaq
     5341 iveekddtgf aafamviitg sdlhngiigf seesqsglel regavmrrlh livtrqpnra
     5401 fedvkvfwrv tlnktvvvlq kdgvnlveel qsvsgtttct mgqtkcfisi elkpekvpqv
     5461 evyffvelye atagaainns arfaqikile sdesqslvyf svgsrlavah kkatlislqv
     5521 ardsgtglmm svnfstqelr saetigrtii spaisgkdfv itegtlvfep gqrstvldvi
     5581 ltpetgslns fpkrfqivlf dpkggaridk vygtanitlv sdadsqaiwg ladqlhqpvn
     5641 ddilnrvlht ismkvatent deqlsammhl iekittegki qafsvasrtl fyeilcslin
     5701 pkrkdtrgfs hfaevtenfa fslltnvtcg spgeksktil dscpylsila lhwypqqing
     5761 hkfegkegdy iriperlldv qdaeimagks tcklvqftey ssqqwfisgn nlptlknkvl
     5821 slsvkgqssq lltndnevly riyaaeprii pqtslcllwn qaaaswlsds qfckvveeta
     5881 dyvecacshm svyavyartd nlssyneaff tsgficisgl clavlshifc arysmfaakl
     5941 lthmmaaslg tqilflasay aspqlaeesc samaavthyl ylcqfswmli qsvnfwyvlv
     6001 mndehterry llffllswgl pafvvilliv ilkgiyhqsm sqiyglihgd lcfipnvyaa
     6061 lftaalvplt clvvvfvvfi hayqvkpqwk ayddvfrgrt naaeiplily lfalisvtwl
     6121 wgglhmayrh fwmlvlfvif nslqglyvfm vyfilhnqmc cpmkasytve mnghpgpsta
     6181 fftpgsgmpp aggeiskstq nligameevp pdwerasfqq gsqaspdlkp spqngatfps
     6241 sggygqgsli adeesqefdd lifalktgag lsvsdnesgq gsqeggtltd sqivelrrip
     6301 iadthl
//
LOCUS       NP_001356835             214 aa            linear   PRI 27-APR-2025
DEFINITION  immunoglobulin lambda-like polypeptide 1 isoform c [Homo sapiens].
ACCESSION   NP_001356835 XP_011528471
VERSION     NP_001356835.1
DBSOURCE    REFSEQ: accession NM_001369906.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Gemayel,K.T., Litman,G.W. and Sriaroon,P.
  TITLE     Autosomal recessive agammaglobulinemia associated with an IGLL1
            gene missense mutation
  JOURNAL   Ann Allergy Asthma Immunol 117 (4), 439-441 (2016)
   PUBMED   27576013
  REMARK    GeneRIF: in autosomal recessive agammaglobulinemia a homozygous
            missense mutation at codon 142 (CCG>with CTG) resulting in a
            Pro>Leu substitution was identified in exon 3 of the IGLL1 gene; 2
            additional silent homozygous substitutions were identified at
            codons 131 (T>C) and 140 (T>C); sequencing also revealed 2
            homozygous single-nucleotide polymorphisms in the noncoding region
            of exon 3
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Chen,D., Zheng,J., Gerasimcik,N., Lagerstedt,K., Sjogren,H.,
            Abrahamsson,J., Fogelstrand,L. and Martensson,I.L.
  TITLE     The Expression Pattern of the Pre-B Cell Receptor Components
            Correlates with Cellular Stage and Clinical Outcome in Acute
            Lymphoblastic Leukemia
  JOURNAL   PLoS One 11 (9), e0162638 (2016)
   PUBMED   27611867
  REMARK    GeneRIF: Irrespective of subtype, Acute Lymphoblastic Leukemia with
            high levels of IGHM, IGLL1 and VPREB1 are arrested at the pre-B
            stage and correlate with good prognosis in high-risk pediatric
            B-cell precursor acute lymphoblastic leukemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Kullo,I.J., Shameer,K., Jouni,H., Lesnick,T.G., Pathak,J.,
            Chute,C.G. and de Andrade,M.
  TITLE     The ATXN2-SH2B3 locus is associated with peripheral arterial
            disease: an electronic medical record-based genome-wide association
            study
  JOURNAL   Front Genet 5, 166 (2014)
   PUBMED   25009551
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 214)
  AUTHORS   Elantak,L., Espeli,M., Boned,A., Bornet,O., Bonzi,J., Gauthier,L.,
            Feracci,M., Roche,P., Guerlesquin,F. and Schiff,C.
  TITLE     Structural basis for galectin-1-dependent pre-B cell receptor
            (pre-BCR) activation
  JOURNAL   J Biol Chem 287 (53), 44703-44713 (2012)
   PUBMED   23124203
  REMARK    GeneRIF: Hhydrophobic residues from the lambda5-UR is crucial for
            the interaction with GAL1 and for pre-BCR clustering.
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Bossy,D., Milili,M., Zucman,J., Thomas,G., Fougereau,M. and
            Schiff,C.
  TITLE     Organization and expression of the lambda-like genes that
            contribute to the mu-psi light chain complex in human pre-B cells
  JOURNAL   Int Immunol 3 (11), 1081-1090 (1991)
   PUBMED   1760403
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Mattei,M.G., Fumoux,F., Roeckel,N., Fougereau,M. and Schiff,C.
  TITLE     The human pre-B-specific lambda-like cluster is located in the
            22q11.2-22q12.3 region, distal to the IgC lambda locus
  JOURNAL   Genomics 9 (3), 544-546 (1991)
   PUBMED   1903358
REFERENCE   8  (residues 1 to 214)
  AUTHORS   Tsubata,T. and Reth,M.
  TITLE     The products of pre-B cell-specific genes (lambda 5 and VpreB) and
            the immunoglobulin mu chain form a complex that is transported onto
            the cell surface
  JOURNAL   J Exp Med 172 (3), 973-976 (1990)
   PUBMED   2117639
REFERENCE   9  (residues 1 to 214)
  AUTHORS   Schiff,C., Bensmana,M., Guglielmi,P., Milili,M., Lefranc,M.P. and
            Fougereau,M.
  TITLE     The immunoglobulin lambda-like gene cluster (14.1, 16.1 and F
            lambda 1) contains gene(s) selectively expressed in pre-B cells and
            is the human counterpart of the mouse lambda 5 gene
  JOURNAL   Int Immunol 2 (3), 201-207 (1990)
   PUBMED   2128466
REFERENCE   10 (residues 1 to 214)
  AUTHORS   Hollis,G.F., Evans,R.J., Stafford-Hollis,J.M., Korsmeyer,S.J. and
            McKearn,J.P.
  TITLE     Immunoglobulin lambda light-chain-related genes 14.1 and 16.1 are
            expressed in pre-B cells and may encode the human immunoglobulin
            omega light-chain protein
  JOURNAL   Proc Natl Acad Sci U S A 86 (14), 5552-5556 (1989)
   PUBMED   2501791
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000345.1.
            
            On Apr 24, 2019 this sequence version replaced XP_011528471.1.
            
            Summary: The preB cell receptor is found on the surface of proB and
            preB cells, where it is involved in transduction of signals for
            cellular proliferation, differentiation from the proB cell to the
            preB cell stage, allelic exclusion at the Ig heavy chain gene
            locus, and promotion of Ig light chain gene rearrangements. The
            preB cell receptor is composed of a membrane-bound Ig mu heavy
            chain in association with a heterodimeric surrogate light chain.
            This gene encodes one of the surrogate light chain subunits and is
            a member of the immunoglobulin gene superfamily. This gene does not
            undergo rearrangement. Mutations in this gene can result in B cell
            deficiency and agammaglobulinemia, an autosomal recessive disease
            in which few or no gamma globulins or antibodies are made. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DN998537.1, HY068682.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.23"
     Protein         1..214
                     /product="immunoglobulin lambda-like polypeptide 1 isoform
                     c"
                     /note="Pre-B lymphocyte-specific protein-2; lambda5;
                     immunoglobulin-related 14.1 protein; immunoglobulin omega
                     polypeptide chain; CD179b antigen; ig lambda-5; CD179
                     antigen-like family member B; immunoglobulin-related
                     protein 14.1"
                     /calculated_mol_wt=22919
     Region          98..109
                     /region_name="J region. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15814.1)"
     Region          110..214
                     /region_name="C region. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15814.1)"
     Region          115..210
                     /region_name="IgC1_L"
                     /note="Immunoglobulin light chain Constant domain; member
                     of the C1-set of Ig superfamily (IgSF) domains; cd07699"
                     /db_xref="CDD:409496"
     Region          115..122
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409496"
     Site            order(118..120,133,135,137,139..140,162..165,175..177,
                     206..207)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409496"
     Region          132..140
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409496"
     Site            order(142,167..168,172)
                     /site_type="other"
                     /note="intrachain IgV domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:409496"
     Region          145..152
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409496"
     Region          154..157
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409496"
     Region          161..166
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409496"
     Region          174..182
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409496"
     Region          192..199
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409496"
     Region          204..209
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409496"
     CDS             1..214
                     /gene="IGLL1"
                     /gene_synonym="14.1; AGM2; CD179b; IGL1; IGL5; IGLJ14.1;
                     IGLL; IGO; IGVPB; VPREB2"
                     /coded_by="NM_001369906.1:101..745"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:3543"
                     /db_xref="HGNC:HGNC:5870"
                     /db_xref="MIM:146770"
ORIGIN      
        1 mrpgtgqggl eapgepgpnl rqrwpllllg lavvthgllr ptaasqsral gpgapggssr
       61 sslrsrwgsr fllqrgswtg prcwprgfqs khnsvthvfg sgtqltvlsq pkatpsvtlf
      121 ppsseelqan katlvclmnd fypgiltvtw kadgtpitqg vemttpskqs nnkyaassyl
      181 sltpeqwrsr rsyscqvmhe gstvektvap aecs
//
LOCUS       NP_002597                593 aa            linear   PRI 27-APR-2025
DEFINITION  high affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
            isoform a [Homo sapiens].
ACCESSION   NP_002597
VERSION     NP_002597.1
DBSOURCE    REFSEQ: accession NM_002606.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Besler,C., Rommel,K.P., Kresoja,K.P., Morbitz,J., Kirsten,H.,
            Scholz,M., Klingel,K., Thiery,J., Burkhardt,R., Buttner,P.,
            Adams,V., Thiele,H. and Lurz,P.
  TITLE     Evaluation of phosphodiesterase 9A as a novel biomarker in heart
            failure with preserved ejection fraction
  JOURNAL   ESC Heart Fail 8 (3), 1861-1872 (2021)
   PUBMED   33787083
  REMARK    GeneRIF: Evaluation of phosphodiesterase 9A as a novel biomarker in
            heart failure with preserved ejection fraction.
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Susmi,T.F., Rahman,A., Khan,M.M.R., Yasmin,F., Islam,M.S.,
            Nasif,O., Alharbi,S.A., Batiha,G.E. and Hossain,M.U.
  TITLE     Prognostic and clinicopathological insights of phosphodiesterase 9A
            gene as novel biomarker in human colorectal cancer
  JOURNAL   BMC Cancer 21 (1), 577 (2021)
   PUBMED   34016083
  REMARK    GeneRIF: Prognostic and clinicopathological insights of
            phosphodiesterase 9A gene as novel biomarker in human colorectal
            cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 593)
  AUTHORS   Wang,P., Wu,P., Egan,R.W. and Billah,M.M.
  TITLE     Identification and characterization of a new human type 9
            cGMP-specific phosphodiesterase splice variant (PDE9A5).
            Differential tissue distribution and subcellular localization of
            PDE9A variants
  JOURNAL   Gene 314, 15-27 (2003)
   PUBMED   14527714
REFERENCE   7  (residues 1 to 593)
  AUTHORS   Rentero,C., Monfort,A. and Puigdomenech,P.
  TITLE     Identification and distribution of different mRNA variants produced
            by differential splicing in the human phosphodiesterase 9A gene
  JOURNAL   Biochem Biophys Res Commun 301 (3), 686-692 (2003)
   PUBMED   12565835
  REMARK    GeneRIF: Identification and distribution of different variants
            produced by differential splicing of phosphodiesterase 9A mRNA.
REFERENCE   8  (residues 1 to 593)
  AUTHORS   Guipponi,M., Scott,H.S., Kudoh,J., Kawasaki,K., Shibuya,K.,
            Shintani,A., Asakawa,S., Chen,H., Lalioti,M.D., Rossier,C.,
            Minoshima,S., Shimizu,N. and Antonarakis,S.E.
  TITLE     Identification and characterization of a novel cyclic nucleotide
            phosphodiesterase gene (PDE9A) that maps to 21q22.3: alternative
            splicing of mRNA transcripts, genomic structure and sequence
  JOURNAL   Hum Genet 103 (4), 386-392 (1998)
   PUBMED   9856478
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Fisher,D.A., Smith,J.F., Pillar,J.S., St Denis,S.H. and Cheng,J.B.
  TITLE     Isolation and characterization of PDE9A, a novel human
            cGMP-specific phosphodiesterase
  JOURNAL   J Biol Chem 273 (25), 15559-15564 (1998)
   PUBMED   9624146
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Loughney,K., Martins,T.J., Harris,E.A., Sadhu,K., Hicks,J.B.,
            Sonnenburg,W.K., Beavo,J.A. and Ferguson,K.
  TITLE     Isolation and characterization of cDNAs corresponding to two human
            calcium, calmodulin-regulated, 3',5'-cyclic nucleotide
            phosphodiesterases
  JOURNAL   J Biol Chem 271 (2), 796-806 (1996)
   PUBMED   8557689
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001626.1, AI492065.1,
            AF067223.1, BC009047.1 and AF048837.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene catalyzes the hydrolysis
            of cAMP and cGMP to their corresponding monophosphates. The encoded
            protein plays a role in signal transduction by regulating the
            intracellular concentration of these cyclic nucleotides. Multiple
            transcript variants encoding several different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF067223.1, AF048837.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000291539.11/ ENSP00000291539.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..593
                     /product="high affinity cGMP-specific 3',5'-cyclic
                     phosphodiesterase 9A isoform a"
                     /EC_number="3.1.4.35"
                     /note="CGMP-specific 3',5'-cyclic phosphodiesterase type
                     9; high affinity cGMP-specific 3',5'-cyclic
                     phosphodiesterase 9A; phosphodiesterase PDE9A21"
                     /calculated_mol_wt=68362
     Region          87..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O76083.1)"
     Region          311..539
                     /region_name="PDEase_I"
                     /note="3'5'-cyclic nucleotide phosphodiesterase;
                     pfam00233"
                     /db_xref="CDD:459723"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8QZV1; propagated from
                     UniProtKB/Swiss-Prot (O76083.1)"
     Region          564..593
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O76083.1)"
     CDS             1..593
                     /gene="PDE9A"
                     /gene_synonym="HSPDE9A2"
                     /coded_by="NM_002606.3:195..1976"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13690.1"
                     /db_xref="GeneID:5152"
                     /db_xref="HGNC:HGNC:8795"
                     /db_xref="MIM:602973"
ORIGIN      
        1 mgsgsssyrp kaiyldidgr iqkvifskyc nssdimdlfc iatglprntt isllttddam
       61 vsidptmpan sertpykvrp vaikqlsagv edkrttsrgq saerplrdrr vvgleqprre
      121 gafesgqvep rprepqgcyq egqrippere eliqsvlaqv aeqfsrafki nelkaevanh
      181 lavlekrvel eglkvveiek cksdikkmre elaarssrtn cpckysfldn hkkltprrdv
      241 ptypkyllsp etiealrkpt fdvwlwepne mlsclehmyh dlglvrdfsi npvtlrrwlf
      301 cvhdnyrnnp fhnfrhcfcv aqmmysmvwl cslqekfsqt dililmtaai chdldhpgyn
      361 ntyqinarte lavryndisp lenhhcavaf qilaepecni fsnippdgfk qirqgmitli
      421 latdmarhae imdsfkekme nfdysneehm tllkmilikc cdisnevrpm evaepwvdcl
      481 leeyfmqsdr ekseglpvap fmdrdkvtka taqigfikfv lipmfetvtk lfpmveeiml
      541 qplwesrdry eelkriddam kelqkktdsl tsgateksre rsrdvknseg dca
//
LOCUS       NP_034077                557 aa            linear   ROD 27-APR-2025
DEFINITION  copine-6 isoform a [Mus musculus].
ACCESSION   NP_034077
VERSION     NP_034077.1
DBSOURCE    REFSEQ: accession NM_009947.4
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Liu,P., Khvotchev,M., Li,Y.C., Chanaday,N.L. and Kavalali,E.T.
  TITLE     Copine-6 Binds to SNAREs and Selectively Suppresses Spontaneous
            Neurotransmission
  JOURNAL   J Neurosci 38 (26), 5888-5899 (2018)
   PUBMED   29802203
  REMARK    GeneRIF: we identify copine-6 as a specific regulator of
            spontaneous neurotransmission
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Larimore,J., Zlatic,S.A., Arnold,M., Singleton,K.S., Cross,R.,
            Rudolph,H., Bruegge,M.V., Sweetman,A., Garza,C., Whisnant,E. and
            Faundez,V.
  TITLE     Dysbindin Deficiency Modifies the Expression of GABA Neuron and Ion
            Permeation Transcripts in the Developing Hippocampus
  JOURNAL   Front Genet 8, 28 (2017)
   PUBMED   28344592
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Reinhard,J.R., Kriz,A., Galic,M., Angliker,N., Rajalu,M., Vogt,K.E.
            and Ruegg,M.A.
  TITLE     The calcium sensor Copine-6 regulates spine structural plasticity
            and learning and memory
  JOURNAL   Nat Commun 7, 11613 (2016)
   PUBMED   27194588
  REMARK    GeneRIF: links activity-triggered calcium signals to spine
            structural plasticity necessary for learning and memory
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Perestenko,P., Watanabe,M., Beusnard-Bee,T., Guna,P. and
            McIlhinney,J.
  TITLE     The second C2-domain of copine-2, copine-6 and copine-7 is
            responsible for their calcium-dependent membrane association
  JOURNAL   FEBS J 282 (19), 3722-3736 (2015)
   PUBMED   26175110
  REMARK    GeneRIF: The second C2-domain of copine-6 is responsible for
            calcium-dependent membrane association.
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Perestenko,P.V., Pooler,A.M., Noorbakhshnia,M., Gray,A., Bauccio,C.
            and Jeffrey McIlhinney,R.A.
  TITLE     Copines-1, -2, -3, -6 and -7 show different calcium-dependent
            intracellular membrane translocation and targeting
  JOURNAL   FEBS J 277 (24), 5174-5189 (2010)
   PUBMED   21087455
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Nakayama,T., Yaoi,T., Kuwajima,G., Yoshie,O. and Sakata,T.
  TITLE     Ca2(+)-dependent interaction of N-copine, a member of the two C2
            domain protein family, with OS-9, the product of a gene frequently
            amplified in osteosarcoma
  JOURNAL   FEBS Lett 453 (1-2), 77-80 (1999)
   PUBMED   10403379
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Nakayama,T., Yaoi,T. and Kuwajima,G.
  TITLE     Localization and subcellular distribution of N-copine in mouse
            brain
  JOURNAL   J Neurochem 72 (1), 373-379 (1999)
   PUBMED   9886090
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Nakayama,T., Yaoi,T., Yasui,M. and Kuwajima,G.
  TITLE     N-copine: a novel two C2-domain-containing protein with neuronal
            activity-regulated expression
  JOURNAL   FEBS Lett 428 (1-2), 80-84 (1998)
   PUBMED   9645480
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Creutz,C.E., Tomsig,J.L., Snyder,S.L., Gautier,M.C., Skouri,F.,
            Beisson,J. and Cohen,J.
  TITLE     The copines, a novel class of C2 domain-containing,
            calcium-dependent, phospholipid-binding proteins conserved from
            Paramecium to humans
  JOURNAL   J Biol Chem 273 (3), 1393-1402 (1998)
   PUBMED   9430674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC159002.2, CJ143652.1,
            AK144410.1, AK134548.1 and CJ286371.1.
            
            Summary: Calcium-dependent membrane-binding proteins may regulate
            molecular events at the interface of the cell membrane and
            cytoplasm. This gene is one of several genes that encodes a
            calcium-dependent protein containing two N-terminal type II C2
            domains and an integrin A domain-like sequence in the C-terminus.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jan 2018].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 4 encode the same isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB008893.1, ERR3363660.947076.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 28.19 cM"
     Protein         1..557
                     /product="copine-6 isoform a"
                     /note="copine-6; N-copine; neuronal-copine"
                     /calculated_mol_wt=61650
     Region          20..137
                     /region_name="C2A_Copine"
                     /note="C2 domain first repeat in Copine; cd04048"
                     /db_xref="CDD:176013"
     Site            order(35,41,93,95,105)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176013"
     Region          152..266
                     /region_name="C2B_Copine"
                     /note="C2 domain second repeat in Copine; cd04047"
                     /db_xref="CDD:176012"
     Site            order(167,173,229,231,237)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176012"
     Region          244..303
                     /region_name="Linker region.
                     /evidence=ECO:0000269|PubMed:21087455,
                     ECO:0000269|PubMed:26175110"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z140.1)"
     Region          325..538
                     /region_name="Copine"
                     /note="pfam07002"
                     /db_xref="CDD:462064"
     CDS             1..557
                     /gene="Cpne6"
                     /coded_by="NM_009947.4:93..1766"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS27112.1"
                     /db_xref="GeneID:12891"
                     /db_xref="MGI:MGI:1334445"
ORIGIN      
        1 msdpemgwvp eppamtlgas rvelrvschg lldrdtltkp hpcvllklys deqwvevert
       61 evlrscsspv fsrvlaieyf feekqplqfh vfdaedgats pssdtflgst ectlgqivsq
      121 tkvtkplllk ngktagksti tivaeevsgt ndyvqltfra hkldnkdlfs ksdpfmeiyk
      181 tngdqsdqlv wrtevvknnl npswepfrls lhslcscdih rplkflvydy dssgkhdfig
      241 eftstfqemq egtanpgqem qwdcinpkyr dkkknykssg tvvlaqctve kvhtfldyim
      301 ggcqisftva idftasngdp rssqslhcls prqpnhylqa lrtvggicqd ydsdkrfpaf
      361 gfgarippnf evshdfainf dpenpeceei sgviasyrrc lpqiqlygpt nvapiinrva
      421 epaqreqstg qatkysvllv ltdgvvsdma etrtaivras rlpmsiiivg vgnadfsdmr
      481 lldgddgplr cpkgvpaard ivqfvpfrdf kdaapsalak cvlaevprqv veyyasqgis
      541 pgaprpstpa mtpspsp
//
LOCUS       NP_000189                372 aa            linear   PRI 27-APR-2025
DEFINITION  3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
            [Homo sapiens].
ACCESSION   NP_000189
VERSION     NP_000189.1
DBSOURCE    REFSEQ: accession NM_000198.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Makretskaya,N., Kalinchenko,N., Tebieva,I., Ionova,S.,
            Zinchenko,R., Marakhonov,A. and Tiulpakov,A.
  TITLE     High carrier frequency of a nonsense p.Trp230* variant in HSD3B2
            gene in Ossetians
  JOURNAL   Front Endocrinol (Lausanne) 14, 1146768 (2023)
   PUBMED   37274334
  REMARK    GeneRIF: High carrier frequency of a nonsense p.Trp230* variant in
            HSD3B2 gene in Ossetians.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Mellone,S., Bertelli,E., Roviglione,B., Vurchio,D., Ronzani,S.,
            Secco,A., Felici,E., Strozzi,M.M., Schena,F. and Giordano,M.
  TITLE     Co-Occurrence of a Pathogenic HSD3B2 Variant and a Duplication on
            10q22.3-q23.2 Detected in Newborn Twins with Salt-Wasting
            Congenital Adrenal Hyperplasia
  JOURNAL   Genes (Basel) 13 (12), 2190 (2022)
   PUBMED   36553457
  REMARK    GeneRIF: Co-Occurrence of a Pathogenic HSD3B2 Variant and a
            Duplication on 10q22.3-q23.2 Detected in Newborn Twins with
            Salt-Wasting Congenital Adrenal Hyperplasia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Tetti,M., Castellano,I., Venziano,F., Magnino,C., Veglio,F.,
            Mulatero,P. and Monticone,S.
  TITLE     Role of Cryptochrome-1 and Cryptochrome-2 in Aldosterone-Producing
            Adenomas and Adrenocortical Cells
  JOURNAL   Int J Mol Sci 19 (6), 1675 (2018)
   PUBMED   29874863
  REMARK    GeneRIF: Independent silencing of CRY1 and CRY2 genes in HAC15
            cells resulted in a mild upregulation of HSD3B2 without affecting
            HSD3B1 expression. In conclusion, our results support the
            hypothesis that CRY1 and CRY2, being AngII-regulated genes, and
            showing a differential expression in APAs when compared with the
            adjacent adrenal cortex, might be involved in adrenal cell
            function, and in the regulation of aldosterone production
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Osinski,M., Wirstlein,P., Wender-Ozegowska,E., Mikolajczyk,M.,
            Jagodzinski,P.P. and Szczepanska,M.
  TITLE     HSD3B2, HSD17B1, HSD17B2, ESR1, ESR2 and AR expression in infertile
            women with endometriosis
  JOURNAL   Ginekol Pol 89 (3), 125-134 (2018)
   PUBMED   29664547
  REMARK    GeneRIF: Observed significant increase in HSD3B2 and ESR1
            transcripts in follicular eutropic endometrium from infertile women
            with endometriosis may be related to abnormal biological effect of
            E2 in endometrium, further affecting the development of human
            embryos.
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Rheaume,E., Simard,J., Morel,Y., Mebarki,F., Zachmann,M.,
            Forest,M.G., New,M.I. and Labrie,F.
  TITLE     Congenital adrenal hyperplasia due to point mutations in the type
            II 3 beta-hydroxysteroid dehydrogenase gene
  JOURNAL   Nat Genet 1 (4), 239-245 (1992)
   PUBMED   1363812
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Lachance,Y., Luu-The,V., Verreault,H., Dumont,M., Rheaume,E.,
            Leblanc,G. and Labrie,F.
  TITLE     Structure of the human type II 3 beta-hydroxysteroid
            dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD) gene: adrenal
            and gonadal specificity
  JOURNAL   DNA Cell Biol 10 (10), 701-711 (1991)
   PUBMED   1741954
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Rheaume,E., Lachance,Y., Zhao,H.F., Breton,N., Dumont,M., de
            Launoit,Y., Trudel,C., Luu-The,V., Simard,J. and Labrie,F.
  TITLE     Structure and expression of a new complementary DNA encoding the
            almost exclusive 3 beta-hydroxysteroid dehydrogenase/delta 5-delta
            4-isomerase in human adrenals and gonads
  JOURNAL   Mol Endocrinol 5 (8), 1147-1157 (1991)
   PUBMED   1944309
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Morrison,N., Nickson,D.A., McBride,M.W., Mueller,U.W., Boyd,E. and
            Sutcliffe,R.G.
  TITLE     Regional chromosomal assignment of human 3-beta-hydroxy-5-ene
            steroid dehydrogenase to 1p13.1 by non-isotopic in situ
            hybridisation
  JOURNAL   Hum Genet 87 (2), 223-225 (1991)
   PUBMED   2066113
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Zachmann,M., Forest,M.G. and De Peretti,E.
  TITLE     3 beta-hydroxysteroid dehydrogenase deficiency. Follow-up study in
            a girl with pubertal bone age
  JOURNAL   Horm Res 11 (6), 292-302 (1979)
   PUBMED   295036
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AV705363.1, BC038419.1 and
            AK222997.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a bifunctional enzyme
            that catalyzes the oxidative conversion of
            delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion
            of ketosteroids. It plays a crucial role in the biosynthesis of all
            classes of hormonal steroids. This gene is predominantly expressed
            in the adrenals and the gonads. Mutations in this gene are
            associated with 3-beta-hydroxysteroid dehydrogenase, type II,
            deficiency. Alternatively spliced transcript variants have been
            found for this gene. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313413.1, AK222997.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369416.4/ ENSP00000358424.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..372
                     /product="3 beta-hydroxysteroid dehydrogenase/Delta
                     5-->4-isomerase type 2"
                     /EC_number="1.1.1.145"
                     /EC_number="5.3.3.1"
                     /note="short chain dehydrogenase/reductase family 11E,
                     member 2; 3-beta-hydroxy-5-ene steroid dehydrogenase;
                     progesterone reductase; 3-beta-hydroxy-Delta(5)-steroid
                     dehydrogenase; 3 beta-HSD type II; delta 5-delta
                     4-isomerase type II; 3 beta-hydroxysteroid dehydrogenase
                     type II, delta 5-delta 4-isomerase type II, 3 beta-HSD
                     type II; 3-beta-HSD II; 3 beta-hydroxysteroid
                     dehydrogenase/Delta 5-->4-isomerase type II; 3-beta-HSD
                     adrenal and gonadal type"
                     /calculated_mol_wt=41921
     Region          4..356
                     /region_name="3b-HSD_HSDB1_like_SDR_e"
                     /note="human 3beta-HSD (hydroxysteroid dehydrogenase) and
                     HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs;
                     cd09811"
                     /db_xref="CDD:187671"
     Site            order(9,11..14,35..37,81..83,99,122..124,154,158,186..189)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187671"
     Site            order(100,124,154,158)
                     /site_type="active"
                     /db_xref="CDD:187671"
     Site            order(124,154,188,201,211,216)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187671"
     Site            287..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26439.2)"
     CDS             1..372
                     /gene="HSD3B2"
                     /gene_synonym="HSD3B; HSDB; SDR11E2"
                     /coded_by="NM_000198.4:143..1261"
                     /db_xref="CCDS:CCDS902.1"
                     /db_xref="GeneID:3284"
                     /db_xref="HGNC:HGNC:5218"
                     /db_xref="MIM:613890"
ORIGIN      
        1 mgwsclvtga ggllgqrivr llveekelke iraldkafrp elreefsklq nrtkltvleg
       61 dildepflkr acqdvsvvih taciidvfgv thresimnvn vkgtqlllea cvqasvpvfi
      121 ytssievagp nsykeiiqng heeeplentw ptpypyskkl aekavlaang wnlkngdtly
      181 tcalrptyiy geggpflsas inealnnngi lssvgkfstv npvyvgnvaw ahilalralr
      241 dpkkapsvrg qfyyisddtp hqsydnlnyi lskefglrld srwslpltlm ywigfllevv
      301 sfllspiysy qppfnrhtvt lsnsvftfsy kkaqrdlayk plysweeakq ktvewvgslv
      361 drhketlksk tq
//
LOCUS       NP_001351803             180 aa            linear   PRI 27-APR-2025
DEFINITION  brain and acute leukemia cytoplasmic protein isoform 3 [Homo
            sapiens].
ACCESSION   NP_001351803
VERSION     NP_001351803.1
DBSOURCE    REFSEQ: accession NM_001364874.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Verma,D., Kumar,R., Ali,M.S., Singh,J., Arora,M., Singh,I.,
            Kumari,S., Bakhshi,S., Sharma,A., Palanichamy,J.K., Tanwar,P.,
            Singh,A.R. and Chopra,A.
  TITLE     BAALC gene expression tells a serious patient outcome tale in
            NPM1-wild type/FLT3-ITD negative cytogenetically normal-acute
            myeloid leukemia in adults
  JOURNAL   Blood Cells Mol Dis 95, 102662 (2022)
   PUBMED   35429905
  REMARK    GeneRIF: BAALC gene expression tells a serious patient outcome tale
            in NPM1-wild type/FLT3-ITD negative cytogenetically normal-acute
            myeloid leukemia in adults.
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Marjanovic,I., Karan-Djurasevic,T., Kostic,T., Virijevic,M.,
            Vukovic,N.S., Pavlovic,S. and Tosic,N.
  TITLE     Prognostic significance of combined BAALC and MN1 gene expression
            level in acute myeloid leukemia with normal karyotype
  JOURNAL   Int J Lab Hematol 43 (3), 433-440 (2021)
   PUBMED   33242229
  REMARK    GeneRIF: Prognostic significance of combined BAALC and MN1 gene
            expression level in acute myeloid leukemia with normal karyotype.
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Dannenmann,B., Klimiankou,M., Oswald,B., Solovyeva,A., Mardan,J.,
            Nasri,M., Ritter,M., Zahabi,A., Arreba-Tutusaus,P., Mir,P.,
            Stein,F., Kandabarau,S., Lachmann,N., Moritz,T., Morishima,T.,
            Konantz,M., Lengerke,C., Ripperger,T., Steinemann,D., Erlacher,M.,
            Niemeyer,C.M., Zeidler,C., Welte,K. and Skokowa,J.
  TITLE     iPSC modeling of stage-specific leukemogenesis reveals BAALC as a
            key oncogene in severe congenital neutropenia
  JOURNAL   Cell Stem Cell 28 (5), 906-922 (2021)
   PUBMED   33894142
  REMARK    GeneRIF: iPSC modeling of stage-specific leukemogenesis reveals
            BAALC as a key oncogene in severe congenital neutropenia.
            Erratum:[Cell Stem Cell. 2023 Sep 7;30(9):1282. doi:
            10.1016/j.stem.2023.07.015. PMID: 37683606]
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Maki,H., Yoshimi,A., Shimada,T., Arai,S., Morita,K., Kamikubo,Y.,
            Ikegawa,M. and Kurokawa,M.
  TITLE     Physical interaction between BAALC and DBN1 induces chemoresistance
            in leukemia
  JOURNAL   Exp Hematol 94, 31-36 (2021)
   PUBMED   33453340
  REMARK    GeneRIF: Physical interaction between BAALC and DBN1 induces
            chemoresistance in leukemia.
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Jentzsch,M., Bill,M., Grimm,J., Brauer,D., Backhaus,D.,
            Goldmann,K., Schulz,J., Niederwieser,D., Platzbecker,U. and
            Schwind,S.
  TITLE     Allogeneic stem cell transplantation mitigates the adverse
            prognostic impact of high diagnostic BAALC and MN1 expression in
            AML
  JOURNAL   Ann Hematol 99 (10), 2417-2427 (2020)
   PUBMED   32862286
  REMARK    GeneRIF: Allogeneic stem cell transplantation mitigates the adverse
            prognostic impact of high diagnostic BAALC and MN1 expression in
            AML.
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Langer,C., Radmacher,M.D., Ruppert,A.S., Whitman,S.P., Paschka,P.,
            Mrozek,K., Baldus,C.D., Vukosavljevic,T., Liu,C.G., Ross,M.E.,
            Powell,B.L., de la Chapelle,A., Kolitz,J.E., Larson,R.A.,
            Marcucci,G. and Bloomfield,C.D.
  CONSRTM   Cancer and Leukemia Group B (CALGB)
  TITLE     High BAALC expression associates with other molecular prognostic
            markers, poor outcome, and a distinct gene-expression signature in
            cytogenetically normal patients younger than 60 years with acute
            myeloid leukemia: a Cancer and Leukemia Group B (CALGB) study
  JOURNAL   Blood 111 (11), 5371-5379 (2008)
   PUBMED   18378853
  REMARK    GeneRIF: high BAALC expression is an independent adverse prognostic
            factor and is associated with a specific gene-expression profile
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Baldus,C.D., Martus,P., Burmeister,T., Schwartz,S., Gokbuget,N.,
            Bloomfield,C.D., Hoelzer,D., Thiel,E. and Hofmann,W.K.
  TITLE     Low ERG and BAALC expression identifies a new subgroup of adult
            acute T-lymphoblastic leukemia with a highly favorable outcome
  JOURNAL   J Clin Oncol 25 (24), 3739-3745 (2007)
   PUBMED   17646667
  REMARK    GeneRIF: Low expression of both ERG and BAALC identifies T-ALL
            patients with a distinctly favorable long-term outcome.
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Satoskar,A.A., Tanner,S.M., Weinstein,M., Qualman,S.J. and de la
            Chapelle,A.
  TITLE     Baalc, a marker of mesoderm and muscle
  JOURNAL   Gene Expr Patterns 5 (4), 463-473 (2005)
   PUBMED   15749074
  REMARK    GeneRIF: High transcript levels occur in leukemic blasts from some
            patients with acute myeloid leukemia.
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Marcucci,G., Mrozek,K. and Bloomfield,C.D.
  TITLE     Molecular heterogeneity and prognostic biomarkers in adults with
            acute myeloid leukemia and normal cytogenetics
  JOURNAL   Curr Opin Hematol 12 (1), 68-75 (2005)
   PUBMED   15604894
  REMARK    GeneRIF: The BAALC gene, located on chromosome 8q22.3, encodes a
            protein with no homology to any known proteins or functional
            domains.
            Review article
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Tanner,S.M., Austin,J.L., Leone,G., Rush,L.J., Plass,C.,
            Heinonen,K., Mrozek,K., Sill,H., Knuutila,S., Kolitz,J.E.,
            Archer,K.J., Caligiuri,M.A., Bloomfield,C.D. and de La Chapelle,A.
  TITLE     BAALC, the human member of a novel mammalian neuroectoderm gene
            lineage, is implicated in hematopoiesis and acute leukemia
  JOURNAL   Proc Natl Acad Sci U S A 98 (24), 13901-13906 (2001)
   PUBMED   11707601
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK022077.1, BI602606.1 and
            BC035038.2.
            
            Summary: This gene was identified by gene expression studies in
            patients with acute myeloid leukemia (AML). The gene is conserved
            among mammals and is not found in lower organisms. Tissues that
            express this gene develop from the neuroectoderm. Multiple
            alternatively spliced transcript variants that encode different
            proteins have been described for this gene; however, some of the
            transcript variants are found only in AML cell lines. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.229774.1,
                                           SRR1660807.55001.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..180
                     /product="brain and acute leukemia cytoplasmic protein
                     isoform 3"
                     /note="brain and acute leukemia cytoplasmic protein; brain
                     and acute leukemia, cytoplasmic; BAALC, MEKK1 and KLF4
                     binding; BAALC, MAP3K1 and KLF4 binding"
                     /calculated_mol_wt=19093
     Region          1..50
                     /region_name="BAALC_N"
                     /note="BAALC N-terminus; pfam06989"
                     /db_xref="CDD:369161"
     CDS             1..180
                     /gene="BAALC"
                     /coded_by="NM_001364874.1:174..716"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS94326.1"
                     /db_xref="GeneID:79870"
                     /db_xref="HGNC:HGNC:14333"
                     /db_xref="MIM:606602"
ORIGIN      
        1 mgcggsrada iepryyeswt retestwlty tdsdappsaa apdsgpeagg lhsvleaeks
       61 kikaptdsvs deglfsaskm aplavfshgm ledglpsngv prstapggip npekktncet
      121 qcpnpqslss gpltqkqngl qtteakrdak rmpakevtin vtdsiqqmdr srritkncvn
//
LOCUS       NP_001019380              72 aa            linear   PRI 27-APR-2025
DEFINITION  small proline-rich protein 2E [Homo sapiens].
ACCESSION   NP_001019380
VERSION     NP_001019380.2
DBSOURCE    REFSEQ: accession NM_001024209.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Kainu,K., Kivinen,K., Zucchelli,M., Suomela,S., Kere,J., Inerot,A.,
            Baker,B.S., Powles,A.V., Fry,L., Samuelsson,L. and
            Saarialho-Kere,U.
  TITLE     Association of psoriasis to PGLYRP and SPRR genes at PSORS4 locus
            on 1q shows heterogeneity between Finnish, Swedish and Irish
            families
  JOURNAL   Exp Dermatol 18 (2), 109-115 (2009)
   PUBMED   18643845
  REMARK    GeneRIF: Association of psoriasis to PGLYRP and SPRR genes at
            PSORS4 locus on 1q shows heterogeneity between Finnish, Swedish and
            Irish families.
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Hong,S.H., Nah,H.Y., Lee,J.Y., Lee,Y.J., Lee,J.W., Gye,M.C.,
            Kim,C.H., Kang,B.M. and Kim,M.K.
  TITLE     Estrogen regulates the expression of the small proline-rich 2 gene
            family in the mouse uterus
  JOURNAL   Mol Cells 17 (3), 477-484 (2004)
   PUBMED   15232223
REFERENCE   3  (residues 1 to 72)
  AUTHORS   Cabral,A., Voskamp,P., Cleton-Jansen,A.M., South,A., Nizetic,D. and
            Backendorf,C.
  TITLE     Structural organization and regulation of the small proline-rich
            family of cornified envelope precursors suggest a role in adaptive
            barrier function
  JOURNAL   J Biol Chem 276 (22), 19231-19237 (2001)
   PUBMED   11279051
REFERENCE   4  (residues 1 to 72)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   5  (residues 1 to 72)
  AUTHORS   Song,H.J., Poy,G., Darwiche,N., Lichti,U., Kuroki,T., Steinert,P.M.
            and Kartasova,T.
  TITLE     Mouse Sprr2 genes: a clustered family of genes showing differential
            expression in epithelial tissues
  JOURNAL   Genomics 55 (1), 28-42 (1999)
   PUBMED   9888996
REFERENCE   6  (residues 1 to 72)
  AUTHORS   Tarcsa,E., Candi,E., Kartasova,T., Idler,W.W., Marekov,L.N. and
            Steinert,P.M.
  TITLE     Structural and transglutaminase substrate properties of the small
            proline-rich 2 family of cornified cell envelope proteins
  JOURNAL   J Biol Chem 273 (36), 23297-23303 (1998)
   PUBMED   9722562
REFERENCE   7  (residues 1 to 72)
  AUTHORS   Steinert,P.M. and Marekov,L.N.
  TITLE     The proteins elafin, filaggrin, keratin intermediate filaments,
            loricrin, and small proline-rich proteins 1 and 2 are isodipeptide
            cross-linked components of the human epidermal cornified cell
            envelope
  JOURNAL   J Biol Chem 270 (30), 17702-17711 (1995)
   PUBMED   7543090
REFERENCE   8  (residues 1 to 72)
  AUTHORS   Gibbs,S., Fijneman,R., Wiegant,J., van Kessel,A.G., van De Putte,P.
            and Backendorf,C.
  TITLE     Molecular characterization and evolution of the SPRR family of
            keratinocyte differentiation markers encoding small proline-rich
            proteins
  JOURNAL   Genomics 16 (3), 630-637 (1993)
   PUBMED   8325635
REFERENCE   9  (residues 1 to 72)
  AUTHORS   Kartasova,T. and van de Putte,P.
  TITLE     Isolation, characterization, and UV-stimulated expression of two
            families of genes encoding polypeptides of related structure in
            human epidermal keratinocytes
  JOURNAL   Mol Cell Biol 8 (5), 2195-2203 (1988)
   PUBMED   3133554
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BE714447.1, DA761769.1,
            DA761491.1 and BG185829.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 13, 2005 this sequence version replaced NP_001019380.1.
            
            Summary: This gene encodes a member of a family of small
            proline-rich proteins clustered in the epidermal differentiation
            complex on chromosome 1q21. The encoded protein, along with other
            family members, is a component of the cornified cell envelope that
            forms beneath the plasma membrane in terminally differentiated
            stratified squamous epithelia. This envelope serves as a barrier
            against extracellular and environmental factors. The seven SPRR2
            genes (A-G) appear to have been homogenized by gene conversion
            compared to others in the cluster that exhibit greater differences
            in protein structure. [provided by RefSeq, Feb 2014].
            
            ##Evidence-Data-START##
            Transcript exon combination :: M20030.1, DA761491.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368750.8/ ENSP00000357739.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..72
                     /product="small proline-rich protein 2E"
                     /note="SPR-2E; SPR-II; small proline-rich protein II"
                     /calculated_mol_wt=7724
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22531.2)"
     Region          21..47
                     /region_name="3 X 9 AA tandem repeats of
                     P-K-C-P-[EQ]-P-C-P-P"
                     /note="propagated from UniProtKB/Swiss-Prot (P22531.2)"
     Region          42..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22531.2)"
     CDS             1..72
                     /gene="SPRR2E"
                     /coded_by="NM_001024209.4:63..281"
                     /db_xref="CCDS:CCDS30866.1"
                     /db_xref="GeneID:6704"
                     /db_xref="HGNC:HGNC:11265"
                     /db_xref="MIM:617588"
ORIGIN      
        1 msyqqqqckq pcqpppvcpt pkcpepcppp kcpepcpppk cpqpcppqqc qqkcppvtps
       61 ppcqpkcppk sk
//
LOCUS       NP_065071               1067 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger MIZ domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_065071
VERSION     NP_065071.1
DBSOURCE    REFSEQ: accession NM_020338.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Zulfiqar,S., Fiaz,A., Khan,W.A., Hussain,M., Ali,A., Ahmed,N.,
            Ali,B. and Masood,M.A.
  TITLE     Association of LPP and ZMIZ1 Gene Polymorphism with Celiac Disease
            in Subjects from Punjab, Pakistan
  JOURNAL   Genes (Basel) 15 (7), 852 (2024)
   PUBMED   39062631
  REMARK    GeneRIF: Association of LPP and ZMIZ1 Gene Polymorphism with Celiac
            Disease in Subjects from Punjab, Pakistan.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Pang,Y., Sun,Y., Wu,Y., Li,J., Qin,P., Guo,S., Zhou,W., Chen,J. and
            Wang,J.
  TITLE     Targeting the ZMIZ1-Notch1 signaling axis for the treatment of
            tongue squamous cell carcinoma
  JOURNAL   Sci Rep 14 (1), 13577 (2024)
   PUBMED   38866828
  REMARK    GeneRIF: Targeting the ZMIZ1-Notch1 signaling axis for the
            treatment of tongue squamous cell carcinoma.
            Erratum:[Sci Rep. 2024 Jul 18;14(1):16609. doi:
            10.1038/s41598-024-67609-2. PMID: 39025882]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   K,C. R, Patel,N.R., Shenoy,A., Scallan,J.P., Chiang,M.Y.,
            Galazo,M.J. and Meadows,S.M.
  TITLE     Zmiz1 is a novel regulator of lymphatic endothelial cell gene
            expression and function
  JOURNAL   PLoS One 19 (5), e0302926 (2024)
   PUBMED   38718095
  REMARK    GeneRIF: Zmiz1 is a novel regulator of lymphatic endothelial cell
            gene expression and function.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1067)
  AUTHORS   Li,X., Wu,A., Wang,Y., Li,D. and Wu,M.
  TITLE     Knockdown of circZMIZ1 enhances the anti-tumor activity of CD8+ T
            cells to alleviate hepatocellular carcinoma
  JOURNAL   Funct Integr Genomics 24 (1), 27 (2024)
   PUBMED   38332346
  REMARK    GeneRIF: Knockdown of circZMIZ1 enhances the anti-tumor activity of
            CD8[+] T cells to alleviate hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1067)
  AUTHORS   Dubois,P.C., Trynka,G., Franke,L., Hunt,K.A., Romanos,J.,
            Curtotti,A., Zhernakova,A., Heap,G.A., Adany,R., Aromaa,A.,
            Bardella,M.T., van den Berg,L.H., Bockett,N.A., de la Concha,E.G.,
            Dema,B., Fehrmann,R.S., Fernandez-Arquero,M., Fiatal,S.,
            Grandone,E., Green,P.M., Groen,H.J., Gwilliam,R., Houwen,R.H.,
            Hunt,S.E., Kaukinen,K., Kelleher,D., Korponay-Szabo,I., Kurppa,K.,
            MacMathuna,P., Maki,M., Mazzilli,M.C., McCann,O.T., Mearin,M.L.,
            Mein,C.A., Mirza,M.M., Mistry,V., Mora,B., Morley,K.I.,
            Mulder,C.J., Murray,J.A., Nunez,C., Oosterom,E., Ophoff,R.A.,
            Polanco,I., Peltonen,L., Platteel,M., Rybak,A., Salomaa,V.,
            Schweizer,J.J., Sperandeo,M.P., Tack,G.J., Turner,G., Veldink,J.H.,
            Verbeek,W.H., Weersma,R.K., Wolters,V.M., Urcelay,E., Cukrowska,B.,
            Greco,L., Neuhausen,S.L., McManus,R., Barisani,D., Deloukas,P.,
            Barrett,J.C., Saavalainen,P., Wijmenga,C. and van Heel,D.A.
  TITLE     Multiple common variants for celiac disease influencing immune gene
            expression
  JOURNAL   Nat Genet 42 (4), 295-302 (2010)
   PUBMED   20190752
  REMARK    Erratum:[Nat Genet.2010 May;42(5):465]
REFERENCE   6  (residues 1 to 1067)
  AUTHORS   Soler,G., Radford-Weiss,I., Ben-Abdelali,R., Mahlaoui,N.,
            Ponceau,J.F., Macintyre,E.A., Vekemans,M., Bernard,O.A. and
            Romana,S.P.
  TITLE     Fusion of ZMIZ1 to ABL1 in a B-cell acute lymphoblastic leukaemia
            with a t(9;10)(q34;q22.3) translocation
  JOURNAL   Leukemia 22 (6), 1278-1280 (2008)
   PUBMED   18007576
  REMARK    GeneRIF: Fusion of ZMIZ1 to ABL1 is associated with a B-cell acute
            lymphoblastic leukemia with a t(9;10)(q34;q22.3) translocation
REFERENCE   7  (residues 1 to 1067)
  AUTHORS   Beliakoff,J., Lee,J., Ueno,H., Aiyer,A., Weissman,I.L., Barsh,G.S.,
            Cardiff,R.D. and Sun,Z.
  TITLE     The PIAS-like protein Zimp10 is essential for embryonic viability
            and proper vascular development
  JOURNAL   Mol Cell Biol 28 (1), 282-292 (2008)
   PUBMED   17967885
  REMARK    GeneRIF: provides evidence to demonstrate a crucial role for Zimp10
            in vasculogenesis
REFERENCE   8  (residues 1 to 1067)
  AUTHORS   Lee,J., Beliakoff,J. and Sun,Z.
  TITLE     The novel PIAS-like protein hZimp10 is a transcriptional
            co-activator of the p53 tumor suppressor
  JOURNAL   Nucleic Acids Res 35 (13), 4523-4534 (2007)
   PUBMED   17584785
  REMARK    GeneRIF: Expression of exogenous hZimp10 enhances the
            transcriptional activity of p53 and knockdown of endogenous hZimp10
            reduces the transcriptional activity of p53.
REFERENCE   9  (residues 1 to 1067)
  AUTHORS   Li,X., Thyssen,G., Beliakoff,J. and Sun,Z.
  TITLE     The novel PIAS-like protein hZimp10 enhances Smad transcriptional
            activity
  JOURNAL   J Biol Chem 281 (33), 23748-23756 (2006)
   PUBMED   16777850
  REMARK    GeneRIF: First line of evidence demonstrates a physiological role
            for endogenous Zimp10 in regulating Smad3/4-mediated transcription.
REFERENCE   10 (residues 1 to 1067)
  AUTHORS   Sharma,M., Li,X., Wang,Y., Zarnegar,M., Huang,C.Y., Palvimo,J.J.,
            Lim,B. and Sun,Z.
  TITLE     hZimp10 is an androgen receptor co-activator and forms a complex
            with SUMO-1 at replication foci
  JOURNAL   EMBO J 22 (22), 6101-6114 (2003)
   PUBMED   14609956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356753.16, BC007288.1,
            AL358782.9, AL391665.28, AY235683.1 and AB033050.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the PIAS (protein inhibitor
            of activated STAT) family of proteins. The encoded protein
            regulates the activity of various transcription factors, including
            the androgen receptor, Smad3/4, and p53. The encoded protein may
            also play a role in sumoylation. A translocation between this locus
            on chromosome 10 and the protein tyrosine kinase ABL1 locus on
            chromosome 9 has been associated with acute lymphoblastic leukemia.
            [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY235683.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968189, SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334512.10/ ENSP00000334474.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.3"
     Protein         1..1067
                     /product="zinc finger MIZ domain-containing protein 1"
                     /note="zinc finger-containing, Miz1, PIAS-like protein on
                     chromosome 10; retinoic acid induced 17"
                     /calculated_mol_wt=115352
     Region          1..120
                     /region_name="Sufficient for transactivation activity,
                     sufficient for interaction with NOTCH1.
                     /evidence=ECO:0000269|PubMed:26522984"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ6.3)"
     Region          8..100
                     /region_name="Zmiz1_N"
                     /note="Zmiz1 N-terminal tetratricopeptide repeat domain;
                     pfam18028"
                     /db_xref="CDD:375500"
     Region          112..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ6.3)"
     Region          <185..556
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          327..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ6.3)"
     Region          737..800
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(742,745,758,760,765,768,781,784)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438111"
     Region          837..1067
                     /region_name="Transactivation domain.
                     /evidence=ECO:0000269|PubMed:26522984"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ6.3)"
     Region          868..1067
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ6.3)"
     CDS             1..1067
                     /gene="ZMIZ1"
                     /gene_synonym="MIZ; NEDDFSA; RAI17; TRAFIP10; ZIMP10"
                     /coded_by="NM_020338.4:642..3845"
                     /db_xref="CCDS:CCDS7357.1"
                     /db_xref="GeneID:57178"
                     /db_xref="HGNC:HGNC:16493"
                     /db_xref="MIM:607159"
ORIGIN      
        1 mnsmdrhiqq tndrlqcikq hlqnpanfhn aatelldwcg dprafqrpfe qslmgcltvv
       61 srvaaqqgfd ldlgyrllav caanrdkftp ksaallsswc eelgrllllr hqksrqsdpp
      121 gklpmqppls smssmkptls hsdgsfpyds vpwqqntnqp pgslsvvttv wgvtntsqsq
      181 vlgnpmanan npmnpggnpm asgmttsnpg lnspqfagqq qqfsakagpa qpyiqqsmyg
      241 rpnypgsggf gasypggpna pagmgippht rppadftqpa aaaaaaavaa aaatatatat
      301 atvaalqetq nkdinqygpm gptqaynsqf mnqpgprgpa smggsmnpas maagmtpsgm
      361 sgppmgmnqp rppgispfgt hgqrmpqqty pgprpqslpi qnikrpypge pnygnqqygp
      421 nsqfptqpgq ypapnpprpl tspnypgqrm psqpssgqyp pptvnmgqyy kpeqfngqnn
      481 tfsgssysny sqgnvnrppr pvpvanyphs pvpgnptppm tpgssippyl spsqdvkppf
      541 ppdikpnmsa lppppanhnd elrltfpvrd gvvlepfrle hnlavsnhvf hlrptvhqtl
      601 mwrsdlelqf kcyhhedrqm ntnwpasvqv svnatpltie rgdnktshkp lhlkhvcqpg
      661 rntiqitvta cccshlfvlq lvhrpsvrsv lqgllkkrll paehcitkik rnfssvaass
      721 gnttlngedg veqtaikvsl kcpitfrriq lparghdckh vqcfdlesyl qlncergtwr
      781 cpvcnktall eglevdqymw gilnaiqhse feevtidptc swrpvpiksd lhikddpdgi
      841 pskrfktmsp sqmimpnvme miaalgpgps pyplppppgg tnsndyssqg nnyqghgnfd
      901 fphgnpggts mndfmhgppq lshppdmpnn maalekplsh pmqetmphag ssdqphpsiq
      961 qglhvphpss qsgpplhhsg apppppsqpp rqppqaapss hphsdltfnp ssalegqaga
     1021 qgasdmpeps ldllpeltnp dellsyldpp dlpsnsnddl lslfenn
//
LOCUS       NP_659496               1084 aa            linear   PRI 27-APR-2025
DEFINITION  L-fucose kinase [Homo sapiens].
ACCESSION   NP_659496
VERSION     NP_659496.2
DBSOURCE    REFSEQ: accession NM_145059.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Fazelzadeh Haghighi,M., Jafari Khamirani,H., Fallahi,J.,
            Monfared,A.A., Ashrafi Dehkordi,K. and Tabei,S.M.B.
  TITLE     Novel insight into FCSK-congenital disorder of glycosylation
            through a CRISPR-generated cell model
  JOURNAL   Mol Genet Genomic Med 12 (5), e2445 (2024)
   PUBMED   38722107
  REMARK    GeneRIF: Novel insight into FCSK-congenital disorder of
            glycosylation through a CRISPR-generated cell model.
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Ng,B.G., Rosenfeld,J.A., Emrick,L., Jain,M., Burrage,L.C., Lee,B.,
            Craigen,W.J., Bearden,D.R., Graham,B.H. and Freeze,H.H.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     Pathogenic Variants in Fucokinase Cause a Congenital Disorder of
            Glycosylation
  JOURNAL   Am J Hum Genet 103 (6), 1030-1037 (2018)
   PUBMED   30503518
REFERENCE   4  (residues 1 to 1084)
  AUTHORS   Keeley,T., Lin,S., Lester,D.K., Lau,E.K. and Yang,S.
  TITLE     The fucose salvage pathway inhibits invadopodia formation and
            extracellular matrix degradation in melanoma cells
  JOURNAL   PLoS One 13 (6), e0199128 (2018)
   PUBMED   29924834
  REMARK    GeneRIF: Ectopic expression of FUK inhibits the formation and the
            proteolytic activities of invadopodia, suggesting that the fucose
            salvage pathway might control melanoma invasion through
            invadopodium-mediated ECM remodeling. FUK depletion in WM793
            melanoma cells at least partially abrogated the L-fucose-mediated
            inhibition of invadopodium formation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1084)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 1084)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   7  (residues 1 to 1084)
  AUTHORS   Hinderlich,S., Berger,M., Blume,A., Chen,H., Ghaderi,D. and
            Bauer,C.
  TITLE     Identification of human L-fucose kinase amino acid sequence
  JOURNAL   Biochem Biophys Res Commun 294 (3), 650-654 (2002)
   PUBMED   12056818
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ441184.1, BC032542.1 and
            BC013735.1.
            
            On May 11, 2005 this sequence version replaced NP_659496.1.
            
            Summary: The protein encoded by this gene belongs to the GHMP
            (galacto-, homoserine, mevalonate and phosphomevalonate) kinase
            family and catalyzes the phosphorylation of L-fucose to form
            beta-L-fucose 1-phosphate. This enzyme catalyzes the first step in
            the utilization of free L-fucose in glycoprotein and glycolipid
            synthesis. L-fucose may be important in mediating a number of
            cell-cell interactions such as blood group antigen recognition,
            inflammation, and metastatis. While several transcript variants may
            exist for this gene, the full-length nature of only one has been
            described to date. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ441184.1, BC032542.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000288078.11/ ENSP00000288078.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..1084
                     /product="L-fucose kinase"
                     /EC_number="2.7.1.52"
                     /note="fucokinase"
                     /calculated_mol_wt=117492
     Region          45..1047
                     /region_name="fkp"
                     /note="bifunctional
                     fucokinase/L-fucose-1-P-guanylyltransferase; Provisional;
                     PRK13412"
                     /db_xref="CDD:237379"
     Region          91..496
                     /region_name="Fucokinase"
                     /note="L-fucokinase; pfam07959"
                     /db_xref="CDD:462323"
     CDS             1..1084
                     /gene="FCSK"
                     /gene_synonym="1110046B12Rik; CDGF2; FUK"
                     /coded_by="NM_145059.3:59..3313"
                     /db_xref="CCDS:CCDS10891.2"
                     /db_xref="GeneID:197258"
                     /db_xref="HGNC:HGNC:29500"
                     /db_xref="MIM:608675"
ORIGIN      
        1 meqpkgvdwt viiltcqykd svqvfqrele vrqkreqipa gtlllavedp ekrvgsggat
       61 lnallvaaeh lsaragftvv tsdvlhsawi lilhmgrdfp fddcgraftc lpvenpeapv
      121 ealvcnldcl ldimtyrlgp gsppgvwvcs tdmllsvpan pgiswdsfrg arvialpgsp
      181 ayaqnhgvyl tdpqglvldi yyqgteaeiq rcvrpdgrvp lvsgvvffsv etaerllath
      241 vsppldacty lgldsgarpv qlslffdilh cmaenvtred flvgrppelg qgdadvagyl
      301 qsaraqlwre lrdqpltmay vssgsysymt ssasefllsl tlpgapgaqi vhsqveeqql
      361 laagssvvsc llegpvqlgp gsvlqhchlq gpihigagcl vtgldtahsk alhgrelrdl
      421 vlqghhtrlh gspghaftlv grldswerqg agtylnvpws effkrtgvra wdlwdpetlp
      481 aeyclpsarl fpvlhpsrel gpqdllwmld hqedggealr awraswrlsw eqlqpcldra
      541 atlasrrdlf frqalhkarh vlearqdlsl rpliwaavre gcpgpllatl dqvaagagdp
      601 gvaaralacv advlgcmaeg rgglrsgpaa npewmrpfsy lecgdlaagv ealaqerdkw
      661 lsrpallvra arhyegagqi lirqavmsaq hfvsteqvel pgpgqwvvae cparvdfsgg
      721 wsdtpplaye lggavlglav rvdgrrpiga rarripepel wlavgprqde mtvkivcrcl
      781 adlrdycqph apgallkaaf icagivhvhs elqlseqllr tfgggfelht wselphgsgl
      841 gtssilagta laalqraagr vvgtealiha vlhleqvltt gggwqdqvgg lmpgikvgrs
      901 raqlplkvev eevtvpegfv qklndhlllv ytgktrlarn llqdvlrswy arlpavvqna
      961 hslvrqteec aegfrqgslp llgqcltsyw eqkklmapgc epltvrrmmd vlaphvhgqs
     1021 lagaggggfl ylltkepqqk ealeavlakt eglgnysihl vevdtqglsl kllgteastc
     1081 cpfp
//
LOCUS       NP_000456                777 aa            linear   PRI 27-APR-2025
DEFINITION  BRCA1-associated RING domain protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_000456
VERSION     NP_000456.2
DBSOURCE    REFSEQ: accession NM_000465.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Salunkhe,S., Daley,J.M., Kaur,H., Tomimatsu,N., Xue,C., Raina,V.B.,
            Jasper,A.M., Rogers,C.M., Li,W., Zhou,S., Mojidra,R., Kwon,Y.,
            Fang,Q., Ji,J.H., Badamchi Shabestari,A., Fitzgerald,O., Dinh,H.,
            Mukherjee,B., Habib,A.A., Hromas,R., Mazin,A.V., Wasmuth,E.V.,
            Olsen,S.K., Libich,D.S., Zhou,D., Zhao,W., Greene,E.C., Burma,S.
            and Sung,P.
  TITLE     Promotion of DNA end resection by BRCA1-BARD1 in homologous
            recombination
  JOURNAL   Nature 634 (8033), 482-491 (2024)
   PUBMED   39261729
  REMARK    GeneRIF: Promotion of DNA end resection by BRCA1-BARD1 in
            homologous recombination.
REFERENCE   2  (residues 1 to 777)
  AUTHORS   Ceppi,I., Dello Stritto,M.R., Mutze,M., Braunshier,S., Mengoli,V.,
            Reginato,G., Vo,H.M.P., Jimeno,S., Acharya,A., Roy,M., Sanchez,A.,
            Halder,S., Howard,S.M., Guerois,R., Huertas,P., Noordermeer,S.M.,
            Seidel,R. and Cejka,P.
  TITLE     Mechanism of BRCA1-BARD1 function in DNA end resection and DNA
            protection
  JOURNAL   Nature 634 (8033), 492-500 (2024)
   PUBMED   39261728
  REMARK    GeneRIF: Mechanism of BRCA1-BARD1 function in DNA end resection and
            DNA protection.
REFERENCE   3  (residues 1 to 777)
  AUTHORS   Novelli,F., Yoshikawa,Y., Vitto,V.A.M., Modesti,L., Minaai,M.,
            Pastorino,S., Emi,M., Kim,J.H., Kricek,F., Bai,F., Onuchic,J.N.,
            Bononi,A., Suarez,J.S., Tanji,M., Favaron,C., Zolondick,A.A.,
            Xu,R., Takanishi,Y., Wang,Z., Sakamoto,G., Gaudino,G., Grzymski,J.,
            Grosso,F., Schrump,D.S., Pass,H.I., Atanesyan,L., Smout,J.,
            Savola,S., Sarin,K.Y., Abolhassani,H., Hammarstrom,L.,
            Pan-Hammarstrom,Q., Giorgi,C., Pinton,P., Yang,H. and Carbone,M.
  TITLE     Germline BARD1 variants predispose to mesothelioma by impairing DNA
            repair and calcium signaling
  JOURNAL   Proc Natl Acad Sci U S A 121 (29), e2405231121 (2024)
   PUBMED   38990952
  REMARK    GeneRIF: Germline BARD1 variants predispose to mesothelioma by
            impairing DNA repair and calcium signaling.
REFERENCE   4  (residues 1 to 777)
  AUTHORS   Tsukada,K., Jones,S.E., Bannister,J., Durin,M.A., Vendrell,I.,
            Fawkes,M., Fischer,R., Kessler,B.M., Chapman,J.R. and
            Blackford,A.N.
  TITLE     BLM and BRCA1-BARD1 coordinate complementary mechanisms of joint
            DNA molecule resolution
  JOURNAL   Mol Cell 84 (4), 640-658 (2024)
   PUBMED   38266639
  REMARK    GeneRIF: BLM and BRCA1-BARD1 coordinate complementary mechanisms of
            joint DNA molecule resolution.
REFERENCE   5  (residues 1 to 777)
  AUTHORS   Burdett,H., Foglizzo,M., Musgrove,L.J., Kumar,D., Clifford,G.,
            Campbell,L.J., Heath,G.R., Zeqiraj,E. and Wilson,M.D.
  TITLE     BRCA1-BARD1 combines multiple chromatin recognition modules to
            bridge nascent nucleosomes
  JOURNAL   Nucleic Acids Res 51 (20), 11080-11103 (2023)
   PUBMED   37823591
  REMARK    GeneRIF: BRCA1-BARD1 combines multiple chromatin recognition
            modules to bridge nascent nucleosomes.
REFERENCE   6  (residues 1 to 777)
  AUTHORS   Meza,J.E., Brzovic,P.S., King,M.C. and Klevit,R.E.
  TITLE     Mapping the functional domains of BRCA1. Interaction of the ring
            finger domains of BRCA1 and BARD1
  JOURNAL   J Biol Chem 274 (9), 5659-5665 (1999)
   PUBMED   10026184
REFERENCE   7  (residues 1 to 777)
  AUTHORS   Ayi,T.C., Tsan,J.T., Hwang,L.Y., Bowcock,A.M. and Baer,R.
  TITLE     Conservation of function and primary structure in the
            BRCA1-associated RING domain (BARD1) protein
  JOURNAL   Oncogene 17 (16), 2143-2148 (1998)
   PUBMED   9798686
REFERENCE   8  (residues 1 to 777)
  AUTHORS   Thai,T.H., Du,F., Tsan,J.T., Jin,Y., Phung,A., Spillman,M.A.,
            Massa,H.F., Muller,C.Y., Ashfaq,R., Mathis,J.M., Miller,D.S.,
            Trask,B.J., Baer,R. and Bowcock,A.M.
  TITLE     Mutations in the BRCA1-associated RING domain (BARD1) gene in
            primary breast, ovarian and uterine cancers
  JOURNAL   Hum Mol Genet 7 (2), 195-202 (1998)
   PUBMED   9425226
REFERENCE   9  (residues 1 to 777)
  AUTHORS   Jin,Y., Xu,X.L., Yang,M.C., Wei,F., Ayi,T.C., Bowcock,A.M. and
            Baer,R.
  TITLE     Cell cycle-dependent colocalization of BARD1 and BRCA1 proteins in
            discrete nuclear domains
  JOURNAL   Proc Natl Acad Sci U S A 94 (22), 12075-12080 (1997)
   PUBMED   9342365
REFERENCE   10 (residues 1 to 777)
  AUTHORS   Wu,L.C., Wang,Z.W., Tsan,J.T., Spillman,M.A., Phung,A., Xu,X.L.,
            Yang,M.C., Hwang,L.Y., Bowcock,A.M. and Baer,R.
  TITLE     Identification of a RING protein that can interact in vivo with the
            BRCA1 gene product
  JOURNAL   Nat Genet 14 (4), 430-440 (1996)
   PUBMED   8944023
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB088853.1, BC126428.1,
            BC126426.1, BX098964.1, AC016708.11 and BU753556.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 14, 2007 this sequence version replaced NP_000456.1.
            
            Summary: This gene encodes a protein which interacts with the
            N-terminal region of BRCA1. In addition to its ability to bind
            BRCA1 in vivo and in vitro, it shares homology with the 2 most
            conserved regions of BRCA1: the N-terminal RING motif and the
            C-terminal BRCT domain. The RING motif is a cysteine-rich sequence
            found in a variety of proteins that regulate cell growth, including
            the products of tumor suppressor genes and dominant protooncogenes.
            This protein also contains 3 tandem ankyrin repeats. The
            BARD1/BRCA1 interaction is disrupted by tumorigenic amino acid
            substitutions in BRCA1, implying that the formation of a stable
            complex between these proteins may be an essential aspect of BRCA1
            tumor suppression. This protein may be the target of oncogenic
            mutations in breast or ovarian cancer. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2752190.1,
                                           SRR14038196.2213370.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260947.9/ ENSP00000260947.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..777
                     /product="BRCA1-associated RING domain protein 1 isoform
                     1"
                     /EC_number="2.3.2.27"
                     /note="BRCA1-associated RING domain protein 1;
                     BRCA1-associated RING domain gene 1; RING-type E3
                     ubiquitin transferase BARD1"
                     /calculated_mol_wt=86517
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99728.2)"
     Region          26..119
                     /region_name="Interaction with BRCA1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99728.2)"
     Region          33..118
                     /region_name="RING-HC_BARD1"
                     /note="RING finger, HC subclass, found in BRCA1-associated
                     RING domain protein 1 (BARD-1) and similar proteins;
                     cd16496"
                     /db_xref="CDD:438159"
     Site            order(33..34,36..37,40..41,43..44,47..48,62,64..69,91,96,
                     98,100..101,103..104,107..108,110..111,113..114,117..118)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438159"
     Region          40..>213
                     /region_name="RAD18"
                     /note="RING-finger-containing E3 ubiquitin ligase [Signal
                     transduction mechanisms]; COG5432"
                     /db_xref="CDD:227719"
     Region          167..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99728.2)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99728.2)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99728.2)"
     Region          356..404
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99728.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q99728.2)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q99728.2)"
     Region          <424..>533
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(427,429,433..434,437..439,441..442,446,449,458,460,
                     462,466..467,470..472,474..475,479,482,491,493,495,
                     499..500,503..505,507..508,512,515,524)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          427..459
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99728.2)"
     Region          427..458
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          460..492
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99728.2)"
     Region          460..491
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          493..525
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99728.2)"
     Region          493..524
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          526..546
                     /region_name="ANK 4, degenerate"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99728.2)"
     Region          554..558
                     /region_name="Flexible linker"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99728.2)"
     Region          570..646
                     /region_name="BRCT_Bard1_rpt1"
                     /note="first BRCT domain of BRCA1-associated RING domain
                     protein 1 (Bard1) and similar proteins; cd17734"
                     /db_xref="CDD:349366"
     Region          671..771
                     /region_name="BRCT_Bard1_rpt2"
                     /note="second (C-terminal) BRCT domain of BRCA1-associated
                     RING domain protein 1 (Bard1) and similar proteins;
                     cd17720"
                     /db_xref="CDD:349352"
     CDS             1..777
                     /gene="BARD1"
                     /coded_by="NM_000465.4:115..2448"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2397.1"
                     /db_xref="GeneID:580"
                     /db_xref="HGNC:HGNC:952"
                     /db_xref="MIM:601593"
ORIGIN      
        1 mpdnrqprnr qprirsgnep rsapamepdg rgawahsraa ldrlekllrc srctnilrep
       61 vclggcehif csncvsdcig tgcpvcytpa wiqdlkinrq ldsmiqlcsk lrnllhdnel
      121 sdlkedkprk slfndagnkk nsikmwfspr skkvryvvsk asvqtqpaik kdasaqqdsy
      181 efvspsppad vserakkasa rsgkkqkkkt laeinqkwnl eaekedgefd skeeskqklv
      241 sfcsqpsvis spqingeidl lasgsltese cfgsltevsl plaeqiespd tksrnevvtp
      301 ekvcknylts kkslplenng krghhnrlss piskrcrtsi lstsgdfvkq tvpseniplp
      361 ecssppsckr kvggtsgrkn snmsdefisl spgtppstls sssyrrvmss psamkllpnm
      421 avkrnhrget llhiasikgd ipsveyllqn gsdpnvkdha gwtplheacn hghlkvvell
      481 lqhkalvntt gyqndsplhd aaknghvdiv klllsygasr navnifglrp vdytddesmk
      541 sllllpekne sssashcsvm ntgqrrdgpl vligsglsse qqkmlselav ilkakkytef
      601 dstvthvvvp gdavqstlkc mlgilngcwi lkfewvkacl rrkvceqeek yeipegprrs
      661 rlnreqllpk lfdgcyfylw gtfkhhpkdn liklvtaggg qilsrkpkpd sdvtqtintv
      721 ayharpdsdq rfctqyiiye dlcnyhperv rqgkvwkaps swfidcvmsf ellplds
//
LOCUS       NP_116045               1157 aa            linear   PRI 27-APR-2025
DEFINITION  probable ATP-dependent RNA helicase DHX37 [Homo sapiens].
ACCESSION   NP_116045
VERSION     NP_116045.2
DBSOURCE    REFSEQ: accession NM_032656.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1157)
  AUTHORS   de Oliveira,F.R., Guaragna,M.S., Maciel-Guerra,A.T., Barros,B.A.,
            de Mello,M.P., Guerra-Junior,G. and Fabbri-Scallet,H.
  TITLE     DHX37 and the Implications in Disorders of Sex Development: An
            Update Review
  JOURNAL   Horm Res Paediatr 97 (5), 433-444 (2024)
   PUBMED   38142677
  REMARK    GeneRIF: DHX37 and the Implications in Disorders of Sex
            Development: An Update Review.
            Review article
REFERENCE   2  (residues 1 to 1157)
  AUTHORS   Liu,Z., Ye,Y., Liu,Y., Liu,Y., Chen,H., Shen,M., Wang,Z., Huang,S.,
            Han,L., Chen,Z. and He,X.
  TITLE     RNA Helicase DHX37 Facilitates Liver Cancer Progression by
            Cooperating with PLRG1 to Drive Superenhancer-Mediated
            Transcription of Cyclin D1
  JOURNAL   Cancer Res 82 (10), 1937-1952 (2022)
   PUBMED   35290436
  REMARK    GeneRIF: RNA Helicase DHX37 Facilitates Liver Cancer Progression by
            Cooperating with PLRG1 to Drive Superenhancer-Mediated
            Transcription of Cyclin D1.
REFERENCE   3  (residues 1 to 1157)
  AUTHORS   McElreavey,K., Pailhoux,E. and Bashamboo,A.
  TITLE     DHX37 and 46,XY DSD: A New Ribosomopathy?
  JOURNAL   Sex Dev 16 (2-3), 194-206 (2022)
   PUBMED   35835064
  REMARK    GeneRIF: DHX37 and 46,XY DSD: A New Ribosomopathy?
            Review article
REFERENCE   4  (residues 1 to 1157)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   5  (residues 1 to 1157)
  AUTHORS   Zidoune,H., Martinerie,L., Tan,D.S., Askari,M., Rezgoune,D.,
            Ladjouze,A., Boukri,A., Benelmadani,Y., Sifi,K., Abadi,N.,
            Satta,D., Rastari,M., Seresht-Ahmadi,M., Bignon-Topalovic,J.,
            Mazen,I., Leger,J., Simon,D., Brauner,R., Totonchi,M., Jauch,R.,
            Bashamboo,A. and McElreavey,K.
  TITLE     Expanding DSD Phenotypes Associated with Variants in the DEAH-Box
            RNA Helicase DHX37
  JOURNAL   Sex Dev 15 (4), 244-252 (2021)
   PUBMED   34293745
  REMARK    GeneRIF: Expanding DSD Phenotypes Associated with Variants in the
            DEAH-Box RNA Helicase DHX37.
REFERENCE   6  (residues 1 to 1157)
  AUTHORS   McElreavey,K., Jorgensen,A., Eozenou,C., Merel,T.,
            Bignon-Topalovic,J., Tan,D.S., Houzelstein,D., Buonocore,F.,
            Warr,N., Kay,R.G.G., Peycelon,M., Siffroi,J.P., Mazen,I.,
            Achermann,J.C., Shcherbak,Y., Leger,J., Sallai,A., Carel,J.C.,
            Martinerie,L., Le Ru,R., Conway,G.S., Mignot,B., Van Maldergem,L.,
            Bertalan,R., Globa,E., Brauner,R., Jauch,R., Nef,S., Greenfield,A.
            and Bashamboo,A.
  TITLE     Pathogenic variants in the DEAH-box RNA helicase DHX37 are a
            frequent cause of 46,XY gonadal dysgenesis and 46,XY testicular
            regression syndrome
  JOURNAL   Genet Med 22 (1), 150-159 (2020)
   PUBMED   31337883
  REMARK    GeneRIF: Results identified heterozygous missense pathogenic
            variants involving DHX37 gene as a new cause of an autosomal
            dominant form of 46,XY DSD, including gonadal dysgenesis and
            testicular regression syndrome (TRS), showing that these conditions
            are part of a clinical spectrum. Some of the variants are clustered
            in two highly conserved functional domains.
REFERENCE   7  (residues 1 to 1157)
  AUTHORS   da Silva,T.E., Gomes,N.L., Lerario,A.M., Keegan,C.E., Nishi,M.Y.,
            Carvalho,F.M., Vilain,E., Barseghyan,H., Martinez-Aguayo,A.,
            Forclaz,M.V., Papazian,R., Pedroso de Paula,L.C., Costa,E.C.,
            Carvalho,L.R., Jorge,A.A.L., Elias,F.M., Mitchell,R., Costa,E.M.F.,
            Mendonca,B.B. and Domenice,S.
  TITLE     Genetic Evidence of the Association of DEAH-Box Helicase 37 Defects
            With 46,XY Gonadal Dysgenesis Spectrum
  JOURNAL   J Clin Endocrinol Metab 104 (12), 5923-5934 (2019)
   PUBMED   31287541
  REMARK    GeneRIF: In 46,XY Gonadal dysgenesis, we identified four
            heterozygous missense rare variants, classified as pathogenic or
            likely pathogenic in the Asp-Glu-Ala-His-box (DHX) helicase 37
            (DHX37) gene.Two variants were recurrent: p.Arg308Gln and
            p.Arg674Trp. The variants were specifically associated with
            embryonic testicular regression syndrome. DHX37 is a player in the
            complex cascade of male gonadal differentiation and maintenance.
REFERENCE   8  (residues 1 to 1157)
  AUTHORS   Paine,I., Posey,J.E., Grochowski,C.M., Jhangiani,S.N.,
            Rosenheck,S., Kleyner,R., Marmorale,T., Yoon,M., Wang,K.,
            Robison,R., Cappuccio,G., Pinelli,M., Magli,A., Coban Akdemir,Z.,
            Hui,J., Yeung,W.L., Wong,B.K.Y., Ortega,L., Bekheirnia,M.R.,
            Bierhals,T., Hempel,M., Johannsen,J., Santer,R., Aktas,D.,
            Alikasifoglu,M., Bozdogan,S., Aydin,H., Karaca,E., Bayram,Y.,
            Ityel,H., Dorschner,M., White,J.J., Wilichowski,E., Wortmann,S.B.,
            Casella,E.B., Kitajima,J.P., Kok,F., Monteiro,F., Muzny,D.M.,
            Bamshad,M., Gibbs,R.A., Sutton,V.R., Van Esch,H.,
            Brunetti-Pierri,N., Hildebrandt,F., Brautbar,A., Van den
            Veyver,I.B., Glass,I., Lessel,D., Lyon,G.J. and Lupski,J.R.
  CONSRTM   University of Washington Center for Mendelian Genomics,
            Baylor-Hopkins Center for Mendelian Genomics, Telethon Undiagnosed
            Diseases Program
  TITLE     Paralog Studies Augment Gene Discovery: DDX and DHX Genes
  JOURNAL   Am J Hum Genet 105 (2), 302-316 (2019)
   PUBMED   31256877
REFERENCE   9  (residues 1 to 1157)
  AUTHORS   Choudhury,P., Hackert,P., Memet,I., Sloan,K.E. and Bohnsack,M.T.
  TITLE     The human RNA helicase DHX37 is required for release of the U3
            snoRNP from pre-ribosomal particles
  JOURNAL   RNA Biol 16 (1), 54-68 (2019)
   PUBMED   30582406
REFERENCE   10 (residues 1 to 1157)
  AUTHORS   Mohnach,L., Fechner,P.Y. and Keegan,C.E.
  TITLE     Nonsyndromic Disorders of Testicular Development Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301714
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093719.26, BC037964.1 and
            BU633279.1.
            
            On Mar 18, 2003 this sequence version replaced NP_116045.1.
            
            Summary: This gene encodes a DEAD box protein. DEAD box proteins,
            characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are
            putative RNA helicases. They are implicated in a number of cellular
            processes involving alteration of RNA secondary structure such as
            translation initiation, nuclear and mitochondrial splicing, and
            ribosome and spliceosome assembly. Based on their distribution
            patterns, some members of this family are believed to be involved
            in embryogenesis, spermatogenesis, and cellular growth and
            division. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037964.1, SRR11853567.8197.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308736.7/ ENSP00000311135.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1157
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..1157
                     /product="probable ATP-dependent RNA helicase DHX37"
                     /EC_number="3.6.4.13"
                     /note="DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 37;
                     DEAD/DEAH box helicase DDX37; DEAH box protein 37; DEAH
                     (Asp-Glu-Ala-His) box polypeptide 37"
                     /calculated_mol_wt=129415
     Region          1..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY37.1)"
     Region          116..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY37.1)"
     Region          252..>1043
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
     Region          372..375
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY37.1)"
     Region          494..523
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY37.1)"
     Region          542..584
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY37.1)"
     CDS             1..1157
                     /gene="DHX37"
                     /gene_synonym="DDX37; Dhr1; NEDBAVC; SRXY11"
                     /coded_by="NM_032656.4:110..3583"
                     /db_xref="CCDS:CCDS9261.1"
                     /db_xref="GeneID:57647"
                     /db_xref="HGNC:HGNC:17210"
                     /db_xref="MIM:617362"
ORIGIN      
        1 mgklrrryni kgrqqagpgp skgppepppv qleledkdtl kgvdasnalv lpgkkkkktk
       61 applskkekk pltkkekkvl qkileqkekk sqraemlqkl sevqaseaem rlfyttsklg
      121 tgnrmyhtke kadevvapgq ekisslsgah rkrrrwpsae eeeeeeeese seleeeseld
      181 edpaaepaea gvgttvaplp papapssqpv pagmtvpppp aaapplpral akpavfipvn
      241 rspemqeerl klpilseeqv imeavaehpi vivcgetgsg kttqvpqfly eagfssedsi
      301 igvteprrva avamsqrvak emnlsqrvvs yqiryegnvt eetrikfmtd gvllkeiqkd
      361 flllrykvvi ideahersvy tdiligllsr ivtlrakrnl plkllimsat lrvedftqnp
      421 rlfakpppvi kvesrqfpvt vhfnkrtple dysgecfrkv ckihrmlpag gilvfltgqa
      481 evhalcrrlr kafppsrarp qekdddqkds veemrkfkks rarakkarae vlpqinldhy
      541 svlpagegde dreaevdeee galdsdldld lgdggqdgge qpdaslplhv lplysllape
      601 kqaqvfkppp egtrlcvvat nvaetsltip gikyvvdcgk vkkryydrvt gvssfrvtwv
      661 sqasadqrag ragrtepghc yrlyssavfg dfeqfpppei trrpvedlil qmkalnvekv
      721 infpfptpps veallaaeel lialgalqpp qkaervkqlq enrlscpita lgrtmatfpv
      781 apryakmlal srqhgclpya itivasmtvr elfeeldrpa asdeeltrlk skrarvaqmk
      841 rtwagqgasl klgdlmvllg avgaceyasc tpqfceangl rykammeirr lrgqlttavn
      901 avcpeaelfv dpkmqpptes qvtylrqivt aglgdhlarr vqseemledk wrnayktpll
      961 ddpvfihpss vlfkelpefv vyqeivettk mymkgvssve vqwipallps ycqfdkplee
     1021 paptycperg rvlchrasvf yrvgwplpai evdfpegidr ykhfarflle gqvfrklasy
     1081 rscllsspgt mlktwarlqp rtesllralv aekadcheal laawkknpky llaeycewlp
     1141 qamhpdieka wppttvh
//
LOCUS       NP_055166                284 aa            linear   PRI 27-APR-2025
DEFINITION  sulfotransferase 4A1 [Homo sapiens].
ACCESSION   NP_055166
VERSION     NP_055166.1
DBSOURCE    REFSEQ: accession NM_014351.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Idris,M., Mitchell,D.J., Gordon,R., Sidharthan,N.P., Butcher,N.J.
            and Minchin,R.F.
  TITLE     Interaction of the Brain-Selective Sulfotransferase SULT4A1 with
            Other Cytosolic Sulfotransferases: Effects on Protein Expression
            and Function
  JOURNAL   Drug Metab Dispos 48 (5), 337-344 (2020)
   PUBMED   32152050
  REMARK    GeneRIF: Interaction of the Brain-Selective Sulfotransferase
            SULT4A1 with Other Cytosolic Sulfotransferases: Effects on Protein
            Expression and Function.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Hossain,M.I., Marcus,J.M., Lee,J.H., Garcia,P.L., Gagne,J.P.,
            Poirier,G.G., Falany,C.N. and Andrabi,S.A.
  TITLE     SULT4A1 Protects Against Oxidative-Stress Induced Mitochondrial
            Dysfunction in Neuronal Cells
  JOURNAL   Drug Metab Dispos 47 (9), 949-953 (2019)
   PUBMED   31266751
  REMARK    GeneRIF: Study in SULT4A1 knockout mice demonstrates that depletion
            of SULT4A1 induces oxidative stress in neurons and expression of
            SULT4A1 in human SH-SY5Y cells protects against
            oxidative-stress-induced mitochondrial dysfunction and cell death.
            Results suggest that SULT4A1 may have a crucial protective function
            against mitochondrial dysfunction and oxidative stress.
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Glatt,H.
  TITLE     Sulfotransferases in the bioactivation of xenobiotics
  JOURNAL   Chem Biol Interact 129 (1-2), 141-170 (2000)
   PUBMED   11154739
  REMARK    Review article
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Glatt,H., Engelke,C.E., Pabel,U., Teubner,W., Jones,A.L.,
            Coughtrie,M.W., Andrae,U., Falany,C.N. and Meinl,W.
  TITLE     Sulfotransferases: genetics and role in toxicology
  JOURNAL   Toxicol Lett 112-113, 341-348 (2000)
   PUBMED   10720750
  REMARK    Review article
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Falany,C.N., Xie,X., Wang,J., Ferrer,J. and Falany,J.L.
  TITLE     Molecular cloning and expression of novel sulphotransferase-like
            cDNAs from human and rat brain
  JOURNAL   Biochem J 346 Pt 3 (Pt 3), 857-864 (2000)
   PUBMED   10698717
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Weinshilboum,R.M., Otterness,D.M., Aksoy,I.A., Wood,T.C., Her,C.
            and Raftogianis,R.B.
  TITLE     Sulfation and sulfotransferases 1: Sulfotransferase molecular
            biology: cDNAs and genes
  JOURNAL   FASEB J 11 (1), 3-14 (1997)
   PUBMED   9034160
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z97055.1 and AF251263.1.
            
            Summary: This gene encodes a member of the sulfotransferase family.
            The encoded protein is a brain-specific sulfotransferase believed
            to be involved in the metabolism of neurotransmitters.
            Polymorphisms in this gene may be associated with susceptibility to
            schizophrenia. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF188698.1, SRR3476690.392545.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330884.9/ ENSP00000332565.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..284
                     /product="sulfotransferase 4A1"
                     /EC_number="2.8.2.-"
                     /note="sulfotransferase-related protein; nervous system
                     cytosolic sulfotransferase; ST4A1; hBR-STL; nervous system
                     sulfotransferase; brain sulfotransferase-like protein"
                     /calculated_mol_wt=32954
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P63047; propagated from
                     UniProtKB/Swiss-Prot (Q9BR01.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P63047; propagated from
                     UniProtKB/Swiss-Prot (Q9BR01.2)"
     Region          45..277
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; pfam00685"
                     /db_xref="CDD:425820"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9BR01.2)"
     CDS             1..284
                     /gene="SULT4A1"
                     /gene_synonym="BR-STL-1; BRSTL1; DJ388M5.3; hBR-STL-1;
                     NST; SULTX3"
                     /coded_by="NM_014351.4:132..986"
                     /db_xref="CCDS:CCDS14051.1"
                     /db_xref="GeneID:25830"
                     /db_xref="HGNC:HGNC:14903"
                     /db_xref="MIM:608359"
ORIGIN      
        1 maeseaetps tpgefeskyf efhgvrlppf crgkmeeian fpvrpsdvwi vtypksgtsl
       61 lqevvylvsq gadpdeiglm nideqlpvle ypqpgldiik eltsprliks hlpyrflpsd
      121 lhngdskviy marnpkdlvv syyqfhrslr tmsyrgtfqe fcrrfmndkl gygswfehvq
      181 efwehrmdsn vlflkyedmh rdlvtmveql arflgvscdk aqlealtehc hqlvdqccna
      241 ealpvgrgrv glwkdiftvs mnekfdlvyk qkmgkcdltf dfyl
//
LOCUS       NP_000753                494 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome P450 2A6 [Homo sapiens].
ACCESSION   NP_000753
VERSION     NP_000753.3
DBSOURCE    REFSEQ: accession NM_000762.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Langlois,A.W.R., Pouget,J.G., Knight,J., Chenoweth,M.J. and
            Tyndale,R.F.
  TITLE     Associating CYP2A6 structural variants with ovarian and lung cancer
            risk in the UK Biobank: replication and extension
  JOURNAL   Eur J Hum Genet 32 (3), 357-360 (2024)
   PUBMED   38097766
  REMARK    GeneRIF: Associating CYP2A6 structural variants with ovarian and
            lung cancer risk in the UK Biobank: replication and extension.
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Giratallah,H., Chenoweth,M.J., Pouget,J.G., El-Boraie,A.,
            Alsaafin,A., Lerman,C., Knight,J. and Tyndale,R.F.
  TITLE     CYP2A6 associates with respiratory disease risk and younger age of
            diagnosis: a phenome-wide association Mendelian Randomization study
  JOURNAL   Hum Mol Genet 33 (2), 198-210 (2024)
   PUBMED   37802914
  REMARK    GeneRIF: CYP2A6 associates with respiratory disease risk and
            younger age of diagnosis: a phenome-wide association Mendelian
            Randomization study.
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Ferrari,E., Cornali,C., Fiorindi,A., Agosti,E., Gallone,S.,
            Rubino,E., Ponzio,F., Fontanella,M.M. and De Maria,L.
  TITLE     Cigarette Smoking and Intracranial Aneurysms: A Pilot Analysis of
            SNPs in the CYP2A6 Gene in the Italian Population
  JOURNAL   World Neurosurg 179, e492-e499 (2023)
   PUBMED   37689358
  REMARK    GeneRIF: Cigarette Smoking and Intracranial Aneurysms: A Pilot
            Analysis of SNPs in the CYP2A6 Gene in the Italian Population.
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Langlois,A.W.R., El-Boraie,A., Pouget,J.G., Cox,L.S.,
            Ahluwalia,J.S., Fukunaga,K., Mushiroda,T., Knight,J.,
            Chenoweth,M.J. and Tyndale,R.F.
  TITLE     Genotyping, characterization, and imputation of known and novel
            CYP2A6 structural variants using SNP array data
  JOURNAL   J Hum Genet 68 (8), 533-541 (2023)
   PUBMED   37059825
  REMARK    GeneRIF: Genotyping, characterization, and imputation of known and
            novel CYP2A6 structural variants using SNP array data.
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Ding,X., Zhang,W., Yu,W., Li,Y., Shao,G., Zhang,L., Zhao,R.C. and
            Li,X.
  TITLE     Recurrent CYP2A6 gene mutation in biphasic hyalinizing psammomatous
            renal cell carcinoma: Additional support of three cases
  JOURNAL   Pathol Res Pract 245, 154468 (2023)
   PUBMED   37104959
  REMARK    GeneRIF: Recurrent CYP2A6 gene mutation in biphasic hyalinizing
            psammomatous renal cell carcinoma: Additional support of three
            cases.
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Yun,C.H., Shimada,T. and Guengerich,F.P.
  TITLE     Purification and characterization of human liver microsomal
            cytochrome P-450 2A6
  JOURNAL   Mol Pharmacol 40 (5), 679-685 (1991)
   PUBMED   1944238
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Maurice,M., Emiliani,S., Dalet-Beluche,I., Derancourt,J. and
            Lange,R.
  TITLE     Isolation and characterization of a cytochrome P450 of the IIA
            subfamily from human liver microsomes
  JOURNAL   Eur J Biochem 200 (2), 511-517 (1991)
   PUBMED   1889415
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Yamano,S., Tatsuno,J. and Gonzalez,F.J.
  TITLE     The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human
            liver microsomes
  JOURNAL   Biochemistry 29 (5), 1322-1329 (1990)
   PUBMED   2322567
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Miles,J.S., Bickmore,W., Brook,J.D., McLaren,A.W., Meehan,R. and
            Wolf,C.R.
  TITLE     Close linkage of the human cytochrome P450IIA and P450IIB gene
            subfamilies: implications for the assignment of substrate
            specificity
  JOURNAL   Nucleic Acids Res 17 (8), 2907-2917 (1989)
   PUBMED   2726448
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA641580.1, BC096254.1,
            BC096256.1 and X13897.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 4, 2008 this sequence version replaced NP_000753.2.
            
            Summary: This gene, CYP2A6, encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This protein localizes to the endoplasmic reticulum and its
            expression is induced by phenobarbital. The enzyme is known to
            hydroxylate coumarin, and also metabolizes nicotine, aflatoxin B1,
            nitrosamines, and some pharmaceuticals. Individuals with certain
            allelic variants are said to have a poor metabolizer phenotype,
            meaning they do not efficiently metabolize coumarin or nicotine.
            This gene is part of a large cluster of cytochrome P450 genes from
            the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q. The gene
            was formerly referred to as CYP2A3; however, it has been renamed
            CYP2A6. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK312964.1, SRR5189664.143627.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162895 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301141.10/ ENSP00000301141.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..494
                     /product="cytochrome P450 2A6"
                     /EC_number="1.14.14.1"
                     /note="xenobiotic monooxygenase; flavoprotein-linked
                     monooxygenase; coumarin 7-hydroxylase; cytochrome P450,
                     subfamily IIA (phenobarbital-inducible), polypeptide 6;
                     cytochrome P450(I); cytochrome P450 IIA3; 1,4-cineole
                     2-exo-monooxygenase; cytochrome P450, family 2, subfamily
                     A, polypeptide 6"
                     /calculated_mol_wt=56387
     Region          65..489
                     /region_name="CYP2A"
                     /note="cytochrome P450 family 2, subfamily A; cd20668"
                     /db_xref="CDD:410761"
     Site            order(101,116..117,128,298,301..302,305..306,309,360,
                     369..370,372,395,431..433,437..441,444..445)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410761"
     Site            order(107,111,117..118,209,297,300..301,305,366,370,480)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410761"
     Site            439
                     /site_type="binding"
                     /note="heme binding site"
     CDS             1..494
                     /gene="CYP2A6"
                     /gene_synonym="CPA6; CYP2A; CYP2A3; CYPIIA6; P450C2A;
                     P450PB"
                     /coded_by="NM_000762.6:22..1506"
                     /db_xref="CCDS:CCDS12568.1"
                     /db_xref="GeneID:1548"
                     /db_xref="HGNC:HGNC:2610"
                     /db_xref="MIM:122720"
ORIGIN      
        1 mlasgmllva llvcltvmvl msvwqqrksk gklppgptpl pfignylqln teqmynslmk
       61 iserygpvft ihlgprrvvv lcghdavrea lvdqaeefsg rgeqatfdwv fkgygvvfsn
      121 gerakqlrrf siatlrdfgv gkrgieeriq eeagflidal rgtgganidp tfflsrtvsn
      181 vissivfgdr fdykdkefls llrmmlgifq ftststgqly emfssvmkhl pgpqqqafql
      241 lqgledfiak kvehnqrtld pnsprdfids flirmqeeek npntefylkn lvmttlnlfi
      301 ggtetvsttl rygflllmkh peveakvhee idrvigknrq pkfedrakmp ymeaviheiq
      361 rfgdvipmsl arrvkkdtkf rdfflpkgte vypmlgsvlr dpsffsnpqd fnpqhflnek
      421 gqfkksdafv pfsigkrncf geglarmelf lffttvmqnf rlkssqspkd idvspkhvgf
      481 atiprnytms flpr
//
LOCUS       NP_081655                515 aa            linear   ROD 27-APR-2025
DEFINITION  fatty acyl-CoA reductase 1 isoform 1 [Mus musculus].
ACCESSION   NP_081655
VERSION     NP_081655.2
DBSOURCE    REFSEQ: accession NM_027379.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Pan,B., Yuan,S., Mayernik,L., Yap,Y.T., Moin,K., Chung,C.S.,
            Maddipati,K., Krawetz,S.A., Zhang,Z., Hess,R.A. and Chen,X.
  TITLE     Disrupted intercellular bridges and spermatogenesis in fatty
            acyl-CoA reductase 1 knockout mice: A new model of ether lipid
            deficiency
  JOURNAL   FASEB J 37 (5), e22908 (2023)
   PUBMED   37039784
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Tang,T., Li,L., Tang,J., Li,Y., Lin,W.Y., Martin,F., Grant,D.,
            Solloway,M., Parker,L., Ye,W., Forrest,W., Ghilardi,N., Oravecz,T.,
            Platt,K.A., Rice,D.S., Hansen,G.M., Abuin,A., Eberhart,D.E.,
            Godowski,P., Holt,K.H., Peterson,A., Zambrowicz,B.P. and de
            Sauvage,F.J.
  TITLE     A mouse knockout library for secreted and transmembrane proteins
  JOURNAL   Nat Biotechnol 28 (7), 749-755 (2010)
   PUBMED   20562862
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Cheng,J.B. and Russell,D.W.
  TITLE     Mammalian wax biosynthesis. II. Expression cloning of wax synthase
            cDNAs encoding a member of the acyltransferase enzyme family
  JOURNAL   J Biol Chem 279 (36), 37798-37807 (2004)
   PUBMED   15220349
  REMARK    GeneRIF: wax monoester synthesis in mammals involves a two step
            biosynthetic pathway catalyzed by fatty acyl-CoA reductase and wax
            synthase enzymes
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Cheng,J.B. and Russell,D.W.
  TITLE     Mammalian wax biosynthesis. I. Identification of two fatty
            acyl-Coenzyme A reductases with different substrate specificities
            and tissue distributions
  JOURNAL   J Biol Chem 279 (36), 37789-37797 (2004)
   PUBMED   15220348
  REMARK    GeneRIF: fatty alcohol synthesis in mammals is accomplished by two
            fatty acyl-CoA reductase isozymes that are expressed at high levels
            in tissues known to synthesize wax monoesters and ether lipids
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC156987.7, AK014486.1 and AC102841.7.
            
            On Jul 1, 2005 this sequence version replaced NP_081655.1.
            
            Transcript Variant: This variant (1) represents the predominant
            transcript. Variants 1, 3, and 4 all encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK030067.1, AK014405.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 59.21 cM"
     Protein         1..515
                     /product="fatty acyl-CoA reductase 1 isoform 1"
                     /EC_number="1.2.1.84"
                     /note="male sterility domain containing 2"
                     /calculated_mol_wt=59304
     Region          11..330
                     /region_name="FAR-N_SDR_e"
                     /note="fatty acyl CoA reductases (FARs), extended (e)
                     SDRs; cd05236"
                     /db_xref="CDD:187547"
     Site            order(17,19..22,44..46,111..113,130,151..153,204,208,
                     229..232)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187547"
     Site            order(131,153,204,208)
                     /site_type="active"
                     /db_xref="CDD:187547"
     Site            order(153,204,231,243,259,265)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187547"
     Region          357..447
                     /region_name="Sterile"
                     /note="Male sterility protein; pfam03015"
                     /db_xref="CDD:460779"
     Region          451..507
                     /region_name="Necessary and sufficient for PEX19-mediated
                     localization into peroxisome membrane.
                     /evidence=ECO:0000250|UniProtKB:Q8WVX9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q922J9.1)"
     Site            466..483
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q922J9.1)"
     CDS             1..515
                     /gene="Far1"
                     /gene_synonym="2600011M19Rik; 2900034E22Rik;
                     3732409C05Rik; Mlstd2"
                     /coded_by="NM_027379.4:161..1708"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS40093.1"
                     /db_xref="GeneID:67420"
                     /db_xref="MGI:MGI:1914670"
ORIGIN      
        1 mvsipeyyeg knilltgatg flgkvllekl lrscprvnsv yvlvrqkagq tpqerveeil
       61 ssklfdrlrd enpdfrekii ainseltqpk lalseedkei iidstnvifh caatvrfnen
      121 lrdavqlnvi atrqlillaq qmknlevfmh vstayaycnr khidevvypp pvdpkklids
      181 lewmddglvn ditpkligdr pntyiytkal aeyvvqqega klnvaivrps ivgaswkepf
      241 pgwidnfngp sglfiaagkg ilrtmrasnn aladlvpvdv vvntslaaaw ysgvnrprni
      301 mvyncttgst npfhwgevey hvistfkrnp leqafrrpnv nltsnhllyh ywiavshkap
      361 aflydiylrm tgrsprmmkt itrlhkamvf leyftsnswv wntdnvnmlm nqlnpedkkt
      421 fnidvrqlhw aeyienycmg tkkyvlneem sglpaarkhl nklrnirygf ntilviliwr
      481 ifiarsqmar niwyfvvslc ykflsyfras stmry
//
LOCUS       NP_689607                663 aa            linear   PRI 27-APR-2025
DEFINITION  glutamate-rich protein 6 isoform 1 [Homo sapiens].
ACCESSION   NP_689607
VERSION     NP_689607.2
DBSOURCE    REFSEQ: accession NM_152394.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Pineau,C., Hikmet,F., Zhang,C., Oksvold,P., Chen,S., Fagerberg,L.,
            Uhlen,M. and Lindskog,C.
  TITLE     Cell Type-Specific Expression of Testis Elevated Genes Based on
            Transcriptomics and Antibody-Based Proteomics
  JOURNAL   J Proteome Res 18 (12), 4215-4230 (2019)
   PUBMED   31429579
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC036239.1, DB058602.1 and BC029577.1.
            
            On Feb 15, 2006 this sequence version replaced NP_689607.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036239.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295910.11/ ENSP00000295910.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.1"
     Protein         1..663
                     /product="glutamate-rich protein 6 isoform 1"
                     /note="protein FAM194A; family with sequence similarity
                     194, member A; glutamate-rich 6A; glutamate-rich protein
                     6"
                     /calculated_mol_wt=75124
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L0X2.1)"
     Region          106..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L0X2.1)"
     Region          422..625
                     /region_name="FAM194"
                     /note="FAM194 protein; pfam14977"
                     /db_xref="CDD:464417"
     CDS             1..663
                     /gene="ERICH6"
                     /gene_synonym="C3orf44; ERICH6A; FAM194A"
                     /coded_by="NM_152394.5:23..2014"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3151.2"
                     /db_xref="GeneID:131831"
                     /db_xref="HGNC:HGNC:28602"
ORIGIN      
        1 mahlrspsgf gdpgkkdqke seeeleeeee eeeveeeeee veeeeeevee eeeevveeel
       61 vgeeqeleap etfseeylwk vtdigdyddd fpdvrprlas ivspsltstf vpsqsatste
      121 tpsasppsst sshksfpkif qtfrkdmsem sidrnihrnl spgipvsvqt eeswlqdlsd
      181 kvqsrkkask ekaepeclas klrekwvinp eesklnilye lefkedfitl fepslrtlps
      241 igppsilayk eessnlginf kdeeeetspk cefcgsdlra ffsnvdvsse pkghasccia
      301 fqnlidyiye eqiktkppka eliaidphaa hgsevdrlka kekalqrkqe qrmarhfaii
      361 sreqthfsed dskrlktisy qlsvdipekq iiddivfdfq lrnsnmsiic cdsriacgkv
      421 vrnellekhy khgskfltsf pdgttqifyp sgnlaiirvp nkvngftciv qedmptnpai
      481 lavldssgrs scyhpngnvw vyinilggqy sdqagnrira wnwsnsitss pfvsfkpvfl
      541 alnryigvri leqdkisitf lamgqqaris vgtkvklpnp eeipilryvs gddllllasl
      601 ikirrlfhkl egcvnfpssq vweklkqpsy lsslslklia lchssgikqd imktirniin
      661 eei
//
LOCUS       NP_071330                631 aa            linear   PRI 27-APR-2025
DEFINITION  differentially expressed in FDCP 6 homolog [Homo sapiens].
ACCESSION   NP_071330
VERSION     NP_071330.3
DBSOURCE    REFSEQ: accession NM_022047.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Fournier,B., Tusseau,M., Villard,M., Malcus,C., Chopin,E.,
            Martin,E., Jorge Cordeiro,D., Fabien,N., Fusaro,M., Gauthier,A.,
            Garnier,N., Goncalves,D., Lounis,S., Lenoir,C., Mathieu,A.L.,
            Moreews,M., Perret,M., Picard,C., Picard,C., Poitevin,F., Viel,S.,
            Bertrand,Y., Walzer,T., Belot,A. and Latour,S.
  TITLE     DEF6 deficiency, a mendelian susceptibility to EBV infection,
            lymphoma, and autoimmunity
  JOURNAL   J Allergy Clin Immunol 147 (2), 740-743 (2021)
   PUBMED   32562707
  REMARK    GeneRIF: DEF6 deficiency, a mendelian susceptibility to EBV
            infection, lymphoma, and autoimmunity.
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Zhu,Z.P., Lin,L.R., Lv,T.D., Xu,C.R., Cai,T.Y. and Lin,J.
  TITLE     High expression levels of DEF6 predicts a poor prognosis for
            patients with clear cell renal cell carcinoma
  JOURNAL   Oncol Rep 44 (5), 2056-2066 (2020)
   PUBMED   33000227
  REMARK    GeneRIF: High expression levels of DEF6 predicts a poor prognosis
            for patients with clear cell renal cell carcinoma.
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Serwas,N.K., Hoeger,B., Ardy,R.C., Stulz,S.V., Sui,Z., Memaran,N.,
            Meeths,M., Krolo,A., Yuce Petronczki,O., Pfajfer,L., Hou,T.Z.,
            Halliday,N., Santos-Valente,E., Kalinichenko,A., Kennedy,A.,
            Mace,E.M., Mukherjee,M., Tesi,B., Schrempf,A., Pickl,W.F.,
            Loizou,J.I., Kain,R., Bidmon-Fliegenschnee,B., Schickel,J.N.,
            Glauzy,S., Huemer,J., Garncarz,W., Salzer,E., Pierides,I.,
            Bilic,I., Thiel,J., Priftakis,P., Banerjee,P.P., Forster-Waldl,E.,
            Medgyesi,D., Huber,W.D., Orange,J.S., Meffre,E., Sansom,D.M.,
            Bryceson,Y.T., Altman,A. and Boztug,K.
  TITLE     Human DEF6 deficiency underlies an immunodeficiency syndrome with
            systemic autoimmunity and aberrant CTLA-4 homeostasis
  JOURNAL   Nat Commun 10 (1), 3106 (2019)
   PUBMED   31308374
  REMARK    Erratum:[Nat Commun. 2019 Oct 2;10(1):4555. doi:
            10.1038/s41467-019-12454-5. PMID: 31578334]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Oka,T., Ihara,S. and Fukui,Y.
  TITLE     Cooperation of DEF6 with activated Rac in regulating cell
            morphology
  JOURNAL   J Biol Chem 282 (3), 2011-2018 (2007)
   PUBMED   17121847
  REMARK    GeneRIF: DEF6 not only activates Rho-family GTPases but also
            cooperates with activated Rac1 to exert its cellular function
REFERENCE   7  (residues 1 to 631)
  AUTHORS   Mavrakis,K.J., McKinlay,K.J., Jones,P. and Sablitzky,F.
  TITLE     DEF6, a novel PH-DH-like domain protein, is an upstream activator
            of the Rho GTPases Rac1, Cdc42, and RhoA
  JOURNAL   Exp Cell Res 294 (2), 335-344 (2004)
   PUBMED   15023524
  REMARK    GeneRIF: DEF6, a novel PH-DH-like domain protein, is an upstream
            activator of the Rho GTPases Rac1, Cdc42, and RhoA.
REFERENCE   8  (residues 1 to 631)
  AUTHORS   Gupta,S., Fanzo,J.C., Hu,C., Cox,D., Jang,S.Y., Lee,A.E.,
            Greenberg,S. and Pernis,A.B.
  TITLE     T cell receptor engagement leads to the recruitment of IBP, a novel
            guanine nucleotide exchange factor, to the immunological synapse
  JOURNAL   J Biol Chem 278 (44), 43541-43549 (2003)
   PUBMED   12923183
  REMARK    GeneRIF: IBP is a novel guanine nucleotide exchange factor and is
            recruited to the immunological synapse by T cell receptor
            engagement
REFERENCE   9  (residues 1 to 631)
  AUTHORS   Gupta,S., Lee,A., Hu,C., Fanzo,J., Goldberg,I., Cattoretti,G. and
            Pernis,A.B.
  TITLE     Molecular cloning of IBP, a SWAP-70 homologous GEF, which is highly
            expressed in the immune system
  JOURNAL   Hum Immunol 64 (4), 389-401 (2003)
   PUBMED   12651066
  REMARK    GeneRIF: Molecular cloning of IBP, a guanine nucleotide exchange
            factor, which is highly expressed in the immune system.
REFERENCE   10 (residues 1 to 631)
  AUTHORS   Tanaka,Y., Bi,K., Kitamura,R., Hong,S., Altman,Y., Matsumoto,A.,
            Tabata,H., Lebedeva,S., Bushway,P.J. and Altman,A.
  TITLE     SWAP-70-like adapter of T cells, an adapter protein that regulates
            early TCR-initiated signaling in Th2 lineage cells
  JOURNAL   Immunity 18 (3), 403-414 (2003)
   PUBMED   12648457
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY241694.1, AJ276095.1 and Z97832.11.
            
            On Apr 18, 2007 this sequence version replaced NP_071330.2.
            
            Summary: DEF6, or IBP, is a guanine nucleotide exchange factor
            (GEF) for RAC (MIM 602048) and CDC42 (MIM 116952) that is highly
            expressed in B and T cells (Gupta et al., 2003 [PubMed
            12923183]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY241694.1, SRR1163658.502397.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316637.7/ ENSP00000319831.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..631
                     /product="differentially expressed in FDCP 6 homolog"
                     /note="SWAP-70-like adaptor protein of T cells;
                     IRF4-binding protein; DEF-6"
                     /calculated_mol_wt=73780
     Region          210..319
                     /region_name="PH_SWAP-70"
                     /note="Switch-associated protein-70 Pleckstrin homology
                     (PH) domain; cd13273"
                     /db_xref="CDD:270092"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:12923183; propagated from
                     UniProtKB/Swiss-Prot (Q9H4E7.1)"
     Site            225
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H4E7.1)"
     Region          <296..>536
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          318..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4E7.1)"
     Region          397..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4E7.1)"
     Region          494..631
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4E7.1)"
     Site            590
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H4E7.1)"
     CDS             1..631
                     /gene="DEF6"
                     /gene_synonym="IBP; IMD87; SLAT; SWAP70L"
                     /coded_by="NM_022047.4:40..1935"
                     /db_xref="CCDS:CCDS4802.1"
                     /db_xref="GeneID:50619"
                     /db_xref="HGNC:HGNC:2760"
                     /db_xref="MIM:610094"
ORIGIN      
        1 malrkellks iwyaftaldv eksgkvsksq lkvlshnlyt vlhiphdpva leehfrdddd
       61 gpvssqgymp ylnkyildkv eegafvkehf delcwtltak knyradsngn smlsnqdafr
      121 lwclfnflse dkyplimvpd eveyllkkvl ssmslevslg eleellaqea qvaqttggls
      181 vwqflelfns grclrgvgrd tlsmaihevy qeliqdvlkq gylwkrghlr rnwaerwfql
      241 qpsclcyfgs eeckekrgii pldahccvev lpdrdgkrcm fcvktanrty emsasdtrqr
      301 qewtaaiqma irlqaegkts lhkdlkqkrr eqreqrerrr aakeeellrl qqlqeekerk
      361 lqelellqea qrqaerllqe eeerrrsqhr elqqalegql reaeqarasm qaemelkeee
      421 aarqrqrike leemqqrlqe alqlevkarr deesvriaqt rlleeeeekl kqlmqlkeeq
      481 eryieraqqe keelqqemaq qsrslqqaqq qleevrqnrq radedveaaq rklrqastnv
      541 khwnvqmnrl mhpiepgdkr pvtsssfsgf qppllahrds slkrltrwgs qgnrtpspns
      601 neqqkslngg deapapastp qedkldpape n
//
LOCUS       NP_631917                286 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 [Homo
            sapiens].
ACCESSION   NP_631917
VERSION     NP_631917.1
DBSOURCE    REFSEQ: accession NM_139178.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chang,Y., Jin,H., Cui,Y., Yang,F., Chen,K., Kuang,W., Huo,C.,
            Xu,Z., Li,Y., Lin,A., Yang,B., Liu,W., Xie,S. and Zhou,T.
  TITLE     PUS7-dependent pseudouridylation of ALKBH3 mRNA inhibits gastric
            cancer progression
  JOURNAL   Clin Transl Med 14 (8), e1811 (2024)
   PUBMED   39175405
  REMARK    GeneRIF: PUS7-dependent pseudouridylation of ALKBH3 mRNA inhibits
            gastric cancer progression.
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Gu,X., Zhuang,A., Yu,J., Yang,L., Ge,S., Ruan,J., Jia,R., Fan,X.
            and Chai,P.
  TITLE     Histone lactylation-boosted ALKBH3 potentiates tumor progression
            and diminished promyelocytic leukemia protein nuclear condensates
            by m1A demethylation of SP100A
  JOURNAL   Nucleic Acids Res 52 (5), 2273-2289 (2024)
   PUBMED   38118002
  REMARK    GeneRIF: Histone lactylation-boosted ALKBH3 potentiates tumor
            progression and diminished promyelocytic leukemia protein nuclear
            condensates by m1A demethylation of SP100A.
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Zhang,L., Duan,H.C., Paduch,M., Hu,J., Zhang,C., Mu,Y., Lin,H.,
            He,C., Kossiakoff,A.A., Jia,G. and Zhang,L.
  TITLE     The Molecular Basis of Human ALKBH3 Mediated RNA N1
            -methyladenosine (m1 A) Demethylation
  JOURNAL   Angew Chem Int Ed Engl 63 (7), e202313900 (2024)
   PUBMED   38158383
  REMARK    GeneRIF: The Molecular Basis of Human ALKBH3 Mediated RNA N[1]
            -methyladenosine (m[1] A) Demethylation.
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Kanazhevskaya,L.Y., Gorbunov,A.A., Lukina,M.V., Smyshliaev,D.A.,
            Zhdanova,P.V., Lomzov,A.A. and Koval,V.V.
  TITLE     The Role of Key Amino Acids of the Human Fe(II)/2OG-Dependent
            Dioxygenase ALKBH3 in Structural Dynamics and Repair Activity
            toward Methylated DNA
  JOURNAL   Int J Mol Sci 25 (2), 1145 (2024)
   PUBMED   38256217
  REMARK    GeneRIF: The Role of Key Amino Acids of the Human
            Fe(II)/2OG-Dependent Dioxygenase ALKBH3 in Structural Dynamics and
            Repair Activity toward Methylated DNA.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Lu,Q., Wang,H., Lei,X., Ma,Q., Zhao,J., Sun,W., Guo,C., Huang,D.
            and Xu,Q.
  TITLE     LncRNA ALKBH3-AS1 enhances ALKBH3 mRNA stability to promote
            hepatocellular carcinoma cell proliferation and invasion
  JOURNAL   J Cell Mol Med 26 (20), 5292-5302 (2022)
   PUBMED   36098205
  REMARK    GeneRIF: LncRNA ALKBH3-AS1 enhances ALKBH3 mRNA stability to
            promote hepatocellular carcinoma cell proliferation and invasion.
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Liu,B.Q., Wu,Y.D., Li,P.H., Wei,J.X., Zhang,T. and Liu,R.L.
  TITLE     Prostate cancer antigen-1 as a potential novel marker for prostate
            cancer
  JOURNAL   Asian J Androl 9 (6), 821-826 (2007)
   PUBMED   17968469
  REMARK    GeneRIF: PCA-1 might be a novel diagnostic marker for prostate
            cancer, and increased PCA-1 expression might denote more aggressive
            variants of prostate cancer [PCA-1].
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Sundheim,O., Vagbo,C.B., Bjoras,M., Sousa,M.M., Talstad,V.,
            Aas,P.A., Drablos,F., Krokan,H.E., Tainer,J.A. and Slupphaug,G.
  TITLE     Human ABH3 structure and key residues for oxidative demethylation
            to reverse DNA/RNA damage
  JOURNAL   EMBO J 25 (14), 3389-3397 (2006)
   PUBMED   16858410
  REMARK    GeneRIF: Crystallographic study reveals beta-strand jelly-roll fold
            of hABH3 that coordinates a catalytically active iron center by a
            conserved His1-X-Asp/Glu-X(n)-His2 motif [ABH3]
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Lee,D.H., Jin,S.G., Cai,S., Chen,Y., Pfeifer,G.P. and O'Connor,T.R.
  TITLE     Repair of methylation damage in DNA and RNA by mammalian AlkB
            homologues
  JOURNAL   J Biol Chem 280 (47), 39448-39459 (2005)
   PUBMED   16174769
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Aas,P.A., Otterlei,M., Falnes,P.O., Vagbo,C.B., Skorpen,F.,
            Akbari,M., Sundheim,O., Bjoras,M., Slupphaug,G., Seeberg,E. and
            Krokan,H.E.
  TITLE     Human and bacterial oxidative demethylases repair alkylation damage
            in both RNA and DNA
  JOURNAL   Nature 421 (6925), 859-863 (2003)
   PUBMED   12594517
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Duncan,T., Trewick,S.C., Koivisto,P., Bates,P.A., Lindahl,T. and
            Sedgwick,B.
  TITLE     Reversal of DNA alkylation damage by two human dioxygenases
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16660-16665 (2002)
   PUBMED   12486230
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087521.10.
            
            Summary: The Escherichia coli AlkB protein protects against the
            cytotoxicity of methylating agents by repair of the specific DNA
            lesions generated in single-stranded DNA. ALKBH2 (MIM 610602) and
            ALKBH3 are E. coli AlkB homologs that catalyze the removal of
            1-methyladenine and 3-methylcytosine (Duncan et al., 2002 [PubMed
            12486230]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.511497.1,
                                           SRR1660803.22762.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302708.9/ ENSP00000302232.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..286
                     /product="alpha-ketoglutarate-dependent dioxygenase alkB
                     homolog 3"
                     /EC_number="1.14.11.33"
                     /EC_number="1.14.11.54"
                     /note="prostate cancer antigen-1; alkylated DNA repair
                     protein alkB homolog 3; alkB, alkylation repair homolog 3;
                     alkB homolog 3, alpha-ketoglutaratedependent dioxygenase"
                     /calculated_mol_wt=33244
     Region          21..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q83.1)"
     Region          90..279
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
     Site            177
                     /site_type="hydroxylation"
                     /note="(4R)-5-hydroxyleucine, alternate.
                     /evidence=ECO:0000269|PubMed:16858410; propagated from
                     UniProtKB/Swiss-Prot (Q96Q83.1)"
     CDS             1..286
                     /gene="ALKBH3"
                     /gene_synonym="ABH3; DEPC-1; DEPC1; hABH3; PCA1"
                     /coded_by="NM_139178.4:420..1280"
                     /db_xref="CCDS:CCDS7906.1"
                     /db_xref="GeneID:221120"
                     /db_xref="HGNC:HGNC:30141"
                     /db_xref="MIM:610603"
ORIGIN      
        1 meekrrrarv qgawaapvks qaiaqpatta kshlhqkpgq twknkehhls drefvfkepq
       61 qvvrrapepr vidregvyei slsptgvsrv clypgfvdvk eadwileqlc qdvpwkqrtg
      121 iredityqqp rltawygelp ytysritmep nphwhpvlrt lknrieentg htfnsllcnl
      181 yrnekdsvdw hsddepslgr cpiiaslsfg atrtfemrkk pppeengdyt yvervkipld
      241 hgtllimega tqadwqhrvp keyhsreprv nltfrtvypd prgapw
//
LOCUS       NP_079119                286 aa            linear   PRI 27-APR-2025
DEFINITION  plasma membrane ascorbate-dependent reductase CYBRD1 isoform 1
            [Homo sapiens].
ACCESSION   NP_079119
VERSION     NP_079119.3
DBSOURCE    REFSEQ: accession NM_024843.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Wang,X., Men,C., Shan,S., Yang,J., Zhang,S., Ji,X., Li,C. and
            Wang,Y.
  TITLE     EGFR upregulates miRNA subset to inhibit CYBRD1 and cause DDP
            resistance in gastric cancer
  JOURNAL   Gene 933, 149005 (2025)
   PUBMED   39419238
  REMARK    GeneRIF: EGFR upregulates miRNA subset to inhibit CYBRD1 and cause
            DDP resistance in gastric cancer.
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Zhao,G., Wang,Q., Zhang,Y., Gu,R., Liu,M., Li,Q., Zhang,J.,
            Yuan,H., Feng,T., Ou,D., Li,S., Li,S., Li,K., Mo,C. and Lin,P.
  TITLE     DDX17 induces epithelial-mesenchymal transition and metastasis
            through the miR-149-3p/CYBRD1 pathway in colorectal cancer
  JOURNAL   Cell Death Dis 14 (1), 1 (2023)
   PUBMED   36593242
  REMARK    GeneRIF: DDX17 induces epithelial-mesenchymal transition and
            metastasis through the miR-149-3p/CYBRD1 pathway in colorectal
            cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Ma,J., Huang,W., Zhu,C., Sun,X., Zhang,Q., Zhang,L., Qi,Q., Bai,X.,
            Feng,Y. and Wang,C.
  TITLE     miR-423-3p activates FAK signaling pathway to drive EMT process and
            tumor growth in lung adenocarcinoma through targeting CYBRD1
  JOURNAL   J Clin Lab Anal 35 (12), e24044 (2021)
   PUBMED   34714955
  REMARK    GeneRIF: miR-423-3p activates FAK signaling pathway to drive EMT
            process and tumor growth in lung adenocarcinoma through targeting
            CYBRD1.
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Su,D., May,J.M., Koury,M.J. and Asard,H.
  TITLE     Human erythrocyte membranes contain a cytochrome b561 that may be
            involved in extracellular ascorbate recycling
  JOURNAL   J Biol Chem 281 (52), 39852-39859 (2006)
   PUBMED   17068337
  REMARK    GeneRIF: Duodenal cytochrome b present in human erythrocytes may
            contribute to their ability to reduce extracellular
            monodehydroascorbate.
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Zaahl,M.G., Merryweather-Clarke,A.T., Kotze,M.J., van der Merwe,S.,
            Warnich,L. and Robson,K.J.
  TITLE     Analysis of genes implicated in iron regulation in individuals
            presenting with primary iron overload
  JOURNAL   Hum Genet 115 (5), 409-417 (2004)
   PUBMED   15338274
  REMARK    GeneRIF: In Africans with iron overload not related to the HFE
            gene, the possible involvement of the SLC40A1 and CYBRD1 genes was
            demonstrated for the first time.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Vargas,J.D., Herpers,B., McKie,A.T., Gledhill,S., McDonnell,J., van
            den Heuvel,M., Davies,K.E. and Ponting,C.P.
  TITLE     Stromal cell-derived receptor 2 and cytochrome b561 are functional
            ferric reductases
  JOURNAL   Biochim Biophys Acta 1651 (1-2), 116-123 (2003)
   PUBMED   14499595
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Zoller,H., Theurl,I., Koch,R.O., McKie,A.T., Vogel,W. and Weiss,G.
  TITLE     Duodenal cytochrome b and hephaestin expression in patients with
            iron deficiency and hemochromatosis
  JOURNAL   Gastroenterology 125 (3), 746-754 (2003)
   PUBMED   12949720
REFERENCE   10 (residues 1 to 286)
  AUTHORS   McKie,A.T., Barrow,D., Latunde-Dada,G.O., Rolfs,A., Sager,G.,
            Mudaly,E., Mudaly,M., Richardson,C., Barlow,D., Bomford,A.,
            Peters,T.J., Raja,K.B., Shirali,S., Hediger,M.A., Farzaneh,F. and
            Simpson,R.J.
  TITLE     An iron-regulated ferric reductase associated with the absorption
            of dietary iron
  JOURNAL   Science 291 (5509), 1755-1759 (2001)
   PUBMED   11230685
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136693.1, CX866825.1, AK027115.1, CB266845.1, DB000953.1,
            AL834483.1 and AC007969.3.
            
            On May 20, 2008 this sequence version replaced NP_079119.2.
            
            Summary: This gene is a member of the cytochrome b(561) family that
            encodes an iron-regulated protein. It highly expressed in the
            duodenal brush border membrane. It has ferric reductase activity
            and is believed to play a physiological role in dietary iron
            absorption. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136693.1, SRR1660809.135756.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321348.9/ ENSP00000319141.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..286
                     /product="plasma membrane ascorbate-dependent reductase
                     CYBRD1 isoform 1"
                     /EC_number="7.2.1.3"
                     /note="duodenal cytochrome b; ferric-chelate reductase 3;
                     cytochrome b561 family, member A2; plasma membrane
                     ascorbate-dependent reductase CYBRD1"
                     /calculated_mol_wt=31510
     Site            8..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TN4.1)"
     Region          36..188
                     /region_name="Cyt_b561_CYBRD1"
                     /note="Vertebrate cytochrome b(561), CYBRD1 gene product;
                     cd08765"
                     /db_xref="CDD:176495"
     Site            48..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TN4.1)"
     Site            order(50,86,120,159)
                     /site_type="other"
                     /note="putative heme binding sites [chemical binding]"
                     /db_xref="CDD:176495"
     Site            79..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TN4.1)"
     Site            119..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TN4.1)"
     Site            152..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TN4.1)"
     Site            198..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TN4.1)"
     Region          229..268
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53TN4.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53TN4.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53TN4.1)"
     CDS             1..286
                     /gene="CYBRD1"
                     /gene_synonym="CYB561A2; DCYTB; FRRS3"
                     /coded_by="NM_024843.4:73..933"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2244.1"
                     /db_xref="GeneID:79901"
                     /db_xref="HGNC:HGNC:20797"
                     /db_xref="MIM:605745"
ORIGIN      
        1 mamegywrfl allgsallvg flsvifalvw vlhyreglgw dgsalefnwh pvlmvtgfvf
       61 iqgiaiivyr lpwtwkcskl lmksihagln avaailaiis vvavfenhnv nnianmyslh
      121 swvgliavic yllqllsgfs vfllpwapls lraflmpihv ysgivifgtv iatalmglte
      181 klifslrdpa ystfppegvf vntlgllilv fgalifwivt rpqwkrpkep nstilhpngg
      241 teqgargsmp aysgnnmdks dselnsevaa rkrnlaldea gqrstm
//
LOCUS       NP_033225                523 aa            linear   ROD 27-APR-2025
DEFINITION  excitatory amino acid transporter 3 [Mus musculus].
ACCESSION   NP_033225 XP_001002136 XP_001002144 XP_001002151 XP_001002163
            XP_001002173 XP_001002184 XP_001002198 XP_001002207
VERSION     NP_033225.1
DBSOURCE    REFSEQ: accession NM_009199.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Zhang,Y., Ya,D., Yang,J., Jiang,Y., Li,X., Wang,J., Tian,N.,
            Deng,J., Yang,B., Li,Q. and Liao,R.
  TITLE     EAAT3 impedes oligodendrocyte remyelination in chronic cerebral
            hypoperfusion-induced white matter injury
  JOURNAL   CNS Neurosci Ther 30 (1), e14487 (2024)
   PUBMED   37803915
  REMARK    GeneRIF: EAAT3 impedes oligodendrocyte remyelination in chronic
            cerebral hypoperfusion-induced white matter injury.
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Yang,Z., Su,W., Wei,X., Qu,S., Zhao,D., Zhou,J., Wang,Y., Guan,Q.,
            Qin,C., Xiang,J., Zen,K. and Yao,B.
  TITLE     HIF-1alpha drives resistance to ferroptosis in solid tumors by
            promoting lactate production and activating SLC1A1
  JOURNAL   Cell Rep 42 (8), 112945 (2023)
   PUBMED   37542723
  REMARK    GeneRIF: HIF-1alpha drives resistance to ferroptosis in solid
            tumors by promoting lactate production and activating SLC1A1.
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Petroccione,M.A., D'Brant,L.Y., Affinnih,N., Wehrle,P.H.,
            Todd,G.C., Zahid,S., Chesbro,H.E., Tschang,I.L. and Scimemi,A.
  TITLE     Neuronal glutamate transporters control reciprocal inhibition and
            gain modulation in D1 medium spiny neurons
  JOURNAL   Elife 12, e81830 (2023)
   PUBMED   37435808
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Wang,X., Chen,Z., Xu,J., Tang,S., An,N., Jiang,L., Zhang,Y.,
            Zhang,S., Zhang,Q., Shen,Y., Chen,S., Lan,X., Wang,T., Zhai,L.,
            Cao,S., Guo,S., Liu,Y., Bi,A., Chen,Y., Gai,X., Duan,Y., Zheng,Y.,
            Fu,Y., Li,Y., Yuan,L., Tong,L., Mo,K., Wang,M., Lin,S.H., Tan,M.,
            Luo,C., Chen,Y., Liu,J., Zhang,Q., Li,L. and Huang,M.
  TITLE     SLC1A1-mediated cellular and mitochondrial influx of
            R-2-hydroxyglutarate in vascular endothelial cells promotes tumor
            angiogenesis in IDH1-mutant solid tumors
  JOURNAL   Cell Res 32 (7), 638-658 (2022)
   PUBMED   35459936
  REMARK    GeneRIF: SLC1A1-mediated cellular and mitochondrial influx of
            R-2-hydroxyglutarate in vascular endothelial cells promotes tumor
            angiogenesis in IDH1-mutant solid tumors.
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Shibata,T., Watanabe,M., Tanaka,K., Wada,K. and Inoue,Y.
  TITLE     Dynamic changes in expression of glutamate transporter mRNAs in
            developing brain
  JOURNAL   Neuroreport 7 (3), 705-709 (1996)
   PUBMED   8733726
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Mukainaka,Y., Tanaka,K., Hagiwara,T. and Wada,K.
  TITLE     Molecular cloning of two glutamate transporter subtypes from mouse
            brain
  JOURNAL   Biochim Biophys Acta 1244 (1), 233-237 (1995)
   PUBMED   7766664
REFERENCE   8  (residues 1 to 523)
  AUTHORS   Tanaka,K.
  TITLE     Cloning and expression of a glutamate transporter from mouse brain
  JOURNAL   Neurosci Lett 159 (1-2), 183-186 (1993)
   PUBMED   7903437
REFERENCE   9  (residues 1 to 523)
  AUTHORS   Rothstein,J.D., Martin,L.J. and Kuncl,R.W.
  TITLE     Decreased glutamate transport by the brain and spinal cord in
            amyotrophic lateral sclerosis
  JOURNAL   N Engl J Med 326 (22), 1464-1468 (1992)
   PUBMED   1349424
REFERENCE   10 (residues 1 to 523)
  AUTHORS   Swarna,M., Rao,D.N. and Reddy,P.P.
  TITLE     Dicarboxylic aminoaciduria associated with mental retardation
  JOURNAL   Hum Genet 82 (3), 299-300 (1989)
   PUBMED   2567279
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC163993.3 and AC113961.14.
            
            On or before May 4, 2006 this sequence version replaced
            XP_001002207.1, XP_001002184.1, XP_001002173.1, XP_001002163.1,
            XP_001002198.1, XP_001002144.1, XP_001002151.1, XP_001002136.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065099.1, AK018188.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 23.5 cM"
     Protein         1..523
                     /product="excitatory amino acid transporter 3"
                     /note="glutamate transporter mEAAC2; excitatory amino acid
                     carrier 2; excitatory amino-acid carrier 1;
                     sodium-dependent glutamate/aspartate transporter 3"
                     /calculated_mol_wt=56563
     Site            19..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51906.2)"
     Region          51..467
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51906.2)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51906.2)"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51906.2)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51906.2)"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51906.2)"
     Site            205..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51906.2)"
     Site            238..265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51906.2)"
     Site            286..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51906.2)"
     Site            353..379
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51906.2)"
     Site            440..461
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51906.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P51906.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P51906.2)"
     CDS             1..523
                     /gene="Slc1a1"
                     /gene_synonym="D130048G10Rik; EAAC1; EAAC2; EAAT3; MEAAC1"
                     /coded_by="NM_009199.3:108..1679"
                     /db_xref="CCDS:CCDS29727.1"
                     /db_xref="GeneID:20510"
                     /db_xref="MGI:MGI:105083"
ORIGIN      
        1 mgkptssgcd wrrflrnhwl llstvaavvl givlgvvvrg hselsnldkf yfafpgeilm
       61 rmlklvilpl ivssmitgva aldsnvsgki glravvyyfs ttviavilgi vlvvsikpgv
      121 tqkvndinrt gktpevstmd amldlirnmf penlvqacfq qyktkreevk pvgdpggnat
      181 evsvttamtt msenktkeyk ivglysdgin vlgliifclv fglvigkmge kgqilvdffn
      241 alsdatmkiv qiimcympig ilfliagkii evedweifrk lglymatvls glaihslivl
      301 pllyfivvrk npfrfalgma qalltalmis sssatlpvtf rcaeeknqvd kritrfvlpv
      361 gatinmdgta lyeavaavfi aqlngldlsi gqivtisita taasigaagv pqaglvtmvi
      421 vlsavglpae dvtliiavdw lldrfrtmvn vlgdafgtgi veklskkele qmdvssevni
      481 vnpfaleptt ldnedsdtkk syvnggfavd ksdtisftqt sqf
//
LOCUS       NP_112567               1623 aa            linear   PRI 27-APR-2025
DEFINITION  RING finger protein 17 isoform 1 [Homo sapiens].
ACCESSION   NP_112567 NP_061911
VERSION     NP_112567.2
DBSOURCE    REFSEQ: accession NM_031277.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1623)
  AUTHORS   Guo,Y., An,L., Ng,H.M., Sy,S.M. and Huen,M.S.
  TITLE     An E2-guided E3 Screen Identifies the RNF17-UBE2U Pair as Regulator
            of the Radiosensitivity, Immunodeficiency, Dysmorphic Features, and
            Learning Difficulties (RIDDLE) Syndrome Protein RNF168
  JOURNAL   J Biol Chem 292 (3), 967-978 (2017)
   PUBMED   27903633
  REMARK    GeneRIF: Further mining of the UBE2U interactome uncovered its
            cognate E3 RNF17 as a novel factor that, via the radiosensitivity,
            immunodeficiency, dysmorphic features, and learning difficulties
            (RIDDLE) syndrome protein RNF168, enforces DNA damage responses.
REFERENCE   2  (residues 1 to 1623)
  AUTHORS   Seifi-Alan,M., Shamsi,R., Ghafouri-Fard,S., Mirfakhraie,R.,
            Zare-Abdollahi,D., Movafagh,A., Modarressi,M.H., Kazemi,G.,
            Geranpayeh,L. and Najafi-Ashtiani,M.
  TITLE     Expression analysis of two cancer-testis genes, FBXO39 and TDRD4,
            in breast cancer tissues and cell lines
  JOURNAL   Asian Pac J Cancer Prev 14 (11), 6625-6629 (2014)
   PUBMED   24377578
  REMARK    GeneRIF: TDRD4 showed significant up-regulation in invasive ductal
            breast carcinoma.
REFERENCE   3  (residues 1 to 1623)
  AUTHORS   Yoon,H., Lee,H., Kim,H.J., You,K.T., Park,Y.N., Kim,H. and Kim,H.
  TITLE     Tudor domain-containing protein 4 as a potential cancer/testis
            antigen in liver cancer
  JOURNAL   Tohoku J Exp Med 224 (1), 41-46 (2011)
   PUBMED   21515969
  REMARK    GeneRIF: TDRD4 mRNA is expressed in a subset of liver cancers, and
            TDRD4 is a candidate CT antigen for liver cancer.
REFERENCE   4  (residues 1 to 1623)
  AUTHORS   Wang,P.J., McCarrey,J.R., Yang,F. and Page,D.C.
  TITLE     An abundance of X-linked genes expressed in spermatogonia
  JOURNAL   Nat Genet 27 (4), 422-426 (2001)
   PUBMED   11279525
REFERENCE   5  (residues 1 to 1623)
  AUTHORS   Janne,O.A., Moilanen,A.M., Poukka,H., Rouleau,N., Karvonen,U.,
            Kotaja,N., Hakli,M. and Palvimo,J.J.
  TITLE     Androgen-receptor-interacting nuclear proteins
  JOURNAL   Biochem Soc Trans 28 (4), 401-405 (2000)
   PUBMED   10961928
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC037275.1, CD358307.1,
            AK001907.1 and DB517763.1.
            
            On or before Apr 28, 2006 this sequence version replaced
            NP_061911.2, NP_112567.1.
            
            Summary: This gene is similar to a mouse gene that encodes a
            testis-specific protein containing a RING finger domain.
            Alternatively spliced transcript variants encoding different
            isoforms have been found. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037275.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000255324.10/ ENSP00000255324.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1623
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.12"
     Protein         1..1623
                     /product="RING finger protein 17 isoform 1"
                     /note="spermatogenesis associated 23; tudor domain
                     containing 4; tudor domain-containing protein 4"
                     /calculated_mol_wt=184513
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXT8.3)"
     Region          <47..74
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            234
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MV7; propagated from
                     UniProtKB/Swiss-Prot (Q9BXT8.3)"
     Region          465..541
                     /region_name="Tudor_TDRD4_rpt1"
                     /note="first Tudor domain found in Tudor domain-containing
                     protein 4 (TDRD4) and similar proteins; cd20414"
                     /db_xref="CDD:410485"
     Site            order(474,481,517,520,522)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410485"
     Region          703..798
                     /region_name="Tudor_TDRD4_rpt2"
                     /note="second Tudor domain found in Tudor
                     domain-containing protein 4 (TDRD4) and similar proteins;
                     cd20415"
                     /db_xref="CDD:410486"
     Site            order(737,743,760,763,765)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410486"
     Region          945..1026
                     /region_name="Tudor_TDRD4_rpt3"
                     /note="third Tudor domain found in Tudor domain-containing
                     protein 4 (TDRD4) and similar proteins; cd20416"
                     /db_xref="CDD:410487"
     Site            order(973,980,997,1000,1002)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410487"
     Region          1229..1296
                     /region_name="Tudor_TDRD4_rpt4"
                     /note="fourth Tudor domain found in Tudor
                     domain-containing protein 4 (TDRD4) and similar proteins;
                     cd20417"
                     /db_xref="CDD:410488"
     Site            order(1239,1245,1261,1264,1266)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410488"
     Region          1438..1462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXT8.3)"
     Region          1477..1581
                     /region_name="Tudor_TDRD4_rpt5"
                     /note="fifth Tudor domain found in Tudor domain-containing
                     protein 4 (TDRD4) and similar proteins; cd20418"
                     /db_xref="CDD:410489"
     Site            order(1490,1496,1515,1518,1520)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410489"
     CDS             1..1623
                     /gene="RNF17"
                     /gene_synonym="Mmip-2; SPATA23; TDRD4"
                     /coded_by="NM_031277.3:36..4907"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9308.2"
                     /db_xref="GeneID:56163"
                     /db_xref="HGNC:HGNC:10060"
                     /db_xref="MIM:605793"
ORIGIN      
        1 maaeasktgp srssyqrmgr ksqpwgaaei qctrcgrrvs rssghhcelq cghafcelcl
       61 lmteecttii cpdcevatav ntrqryypma gyikedsime klqpktiknc sqdfkktadq
      121 lttglersas tdktllnssa vmldtntaee idealntahh sfeqlsiagk alehmqkqti
      181 eerervievv ekqfdqllaf fdsrkknlce efarttddyl snlikaksyi eekknnlnaa
      241 mniaralqls pslrtycdln qiirtlqlts dselaqvssp qlrnpprlsv ncseiicmfn
      301 nmgkiefrds tkcypqenei rqnvqkkynn kkelscydty pplekkkvdm svltseappp
      361 plqpetndvh leaknfqpqk dvataspkti avlpqmgssp dviieeiied nvessaelvf
      421 vshvidpchf yirkysqikd akvlekkvne fcnrsshldp sdilelgari fvssikngmw
      481 crgtitelip iegrntrkpc sptrlfvhev aliqifmvdf gnsevlivtg vvdthvrpeh
      541 sakqhialnd lclvlrksep ytegllkdiq plaqpcslkd ivpqnsnegw eeeakveflk
      601 mvnnkavsmk vfreedgvli vdlqkpppnk issdmpvslr dalvfmelak fksqslrshf
      661 eknttlhyhp pilpkemtdv svtvchinsp gdfylqlieg ldilfllkti eefyksedge
      721 nleilcpvqd qacvakfedg iwyrakvigl pghqevevky vdfgntakit ikdvrkikde
      781 flnapekaik cklayiepyk rtmqwskeak ekfeekaqdk fmtcsvikil ednvllvelf
      841 dslgapemtt tsindqlvke glasyeigyi lkdnsqkhie vwdpspeeii snevhnlnpv
      901 sakslpnenf qslynkelpv hicnvispek iyvqwllten llnsleekmi aayenskwep
      961 vkwendmhca vkiqdknqwr rgqiirmvtd tlvevllydv gvelvvnvdc lrkleenlkt
     1021 mgrlslecsl vdirpaggsd kwtatacdcl slyltgavat iilqvdseen nttwplpvki
     1081 fcrdekgerv dvskylikkg lalrerrinn ldnshslsek slevpleqed svvtnciktn
     1141 fdpdkktadi iseqkvsefq ekileprttr gykppaipnm nvfeatvscv gddgtifvvp
     1201 klsefelikm tneiqsnlkc lgllepyfwk kgeacavrgs dtlwyrgkvm evvggavrvq
     1261 yldhgfteki pqchlypill ypdipqfcip cqlhnttpvg nvwqpdaiev lqqllskrqv
     1321 dihimelpkn pweklsihly fdgmslsyfm ayykyctseh teemlkekpr sdhdkkyeee
     1381 qweirfeell saetdtpllp pylssslpsp gelyavqvkh vvspnevyic ldsietsnqs
     1441 nqhsdtddsg vsgesesesl dealqrvnkk vealppltdf rtempclaey ddglwyraki
     1501 vaikefnpls ilvqfvdygs takltlnrlc qipshlmryp araikvllag fkpplrdlge
     1561 tripycpkws mealwamidc lqgkqlyavs mapapeqivt lyddeqhpvh mplvemglad
     1621 kde
//
LOCUS       NP_035065                371 aa            linear   ROD 27-APR-2025
DEFINITION  neuropeptide Y receptor type 6 [Mus musculus].
ACCESSION   NP_035065
VERSION     NP_035065.1
DBSOURCE    REFSEQ: accession NM_010935.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Khor,E.C., Yulyaningsih,E., Driessler,F., Kovacic,N., Wee,N.K.Y.,
            Kulkarni,R.N., Lee,N.J., Enriquez,R.F., Xu,J., Zhang,L., Herzog,H.
            and Baldock,P.A.
  TITLE     The y6 receptor suppresses bone resorption and stimulates bone
            formation in mice via a suprachiasmatic nucleus relay
  JOURNAL   Bone 84, 139-147 (2016)
   PUBMED   26721736
  REMARK    GeneRIF: y6R signalling is required for maintenance of bone mass,
            with loss of y6R uncoupling bone remodelling and resulting in a
            negative bone balance.
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Yulyaningsih,E., Loh,K., Lin,S., Lau,J., Zhang,L., Shi,Y.,
            Berning,B.A., Enriquez,R., Driessler,F., Macia,L., Khor,E.C.,
            Qi,Y., Baldock,P., Sainsbury,A. and Herzog,H.
  TITLE     Pancreatic polypeptide controls energy homeostasis via Npy6r
            signaling in the suprachiasmatic nucleus in mice
  JOURNAL   Cell Metab 19 (1), 58-72 (2014)
   PUBMED   24411939
  REMARK    GeneRIF: PP-initiated signaling through Npy6r in vasoactive
            intestinal peptide neurons regulates the growth hormone axis and
            body composition.
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Starback,P., Wraith,A., Eriksson,H. and Larhammar,D.
  TITLE     Neuropeptide Y receptor gene y6: multiple deaths or resurrections?
  JOURNAL   Biochem Biophys Res Commun 277 (1), 264-269 (2000)
   PUBMED   11027673
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Wraith,A., Tornsten,A., Chardon,P., Harbitz,I., Chowdhary,B.P.,
            Andersson,L., Lundin,L.G. and Larhammar,D.
  TITLE     Evolution of the neuropeptide Y receptor family: gene and
            chromosome duplications deduced from the cloning and mapping of the
            five receptor subtype genes in pig
  JOURNAL   Genome Res 10 (3), 302-310 (2000)
   PUBMED   10720571
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Kanatani,A., Mashiko,S., Murai,N., Sugimoto,N., Ito,J.,
            Fukuroda,T., Fukami,T., Morin,N., MacNeil,D.J., Van der Ploeg,L.H.,
            Saga,Y., Nishimura,S. and Ihara,M.
  TITLE     Role of the Y1 receptor in the regulation of neuropeptide
            Y-mediated feeding: comparison of wild-type, Y1 receptor-deficient,
            and Y5 receptor-deficient mice
  JOURNAL   Endocrinology 141 (3), 1011-1016 (2000)
   PUBMED   10698177
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Naveilhan,P., Neveu,I., Arenas,E. and Ernfors,P.
  TITLE     Complementary and overlapping expression of Y1, Y2 and Y5 receptors
            in the developing and adult mouse nervous system
  JOURNAL   Neuroscience 87 (1), 289-302 (1998)
   PUBMED   9722158
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Lutz,C.M., Richards,J.E., Scott,K.L., Sinha,S., Yang-Feng,T.L.,
            Frankel,W.N. and Thompson,D.A.
  TITLE     Neuropeptide Y receptor genes mapped in human and mouse: receptors
            with high affinity for pancreatic polypeptide are not clustered
            with receptors specific for neuropeptide Y and peptide YY
  JOURNAL   Genomics 46 (2), 287-290 (1997)
   PUBMED   9417917
REFERENCE   8  (residues 1 to 371)
  AUTHORS   Nakamura,M., Yokoyama,M., Watanabe,H. and Matsumoto,T.
  TITLE     Molecular cloning, organization and localization of the gene for
            the mouse neuropeptide Y-Y5 receptor
  JOURNAL   Biochim Biophys Acta 1328 (2), 83-89 (1997)
   PUBMED   9315606
REFERENCE   9  (residues 1 to 371)
  AUTHORS   Gregor,P., Feng,Y., DeCarr,L.B., Cornfield,L.J. and McCaleb,M.L.
  TITLE     Molecular characterization of a second mouse pancreatic polypeptide
            receptor and its inactivated human homologue
  JOURNAL   J Biol Chem 271 (44), 27776-27781 (1996)
   PUBMED   8910373
REFERENCE   10 (residues 1 to 371)
  AUTHORS   Weinberg,D.H., Sirinathsinghji,D.J., Tan,C.P., Shiao,L.L.,
            Morin,N., Rigby,M.R., Heavens,R.H., Rapoport,D.R., Bayne,M.L.,
            Cascieri,M.A., Strader,C.D., Linemeyer,D.L. and MacNeil,D.J.
  TITLE     Cloning and expression of a novel neuropeptide Y receptor
  JOURNAL   J Biol Chem 271 (28), 16435-16438 (1996)
   PUBMED   8663568
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132130.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK030279.1, BC103667.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 23.74 cM"
     Protein         1..371
                     /product="neuropeptide Y receptor type 6"
                     /note="PP2; NPY6-R; pancreatic polypeptide receptor 2"
                     /calculated_mol_wt=42583
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q61212.1)"
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q61212.1)"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61212.1)"
     Region          42..329
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          42..63
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320518"
     Region          72..94
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320518"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61212.1)"
     Region          110..132
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320518"
     Site            112..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61212.1)"
     Site            151..171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61212.1)"
     Region          153..169
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320518"
     Site            182
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q61212.1)"
     Region          207..230
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320518"
     Site            207..227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61212.1)"
     Region          260..282
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320518"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61212.1)"
     Region          297..322
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320518"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q61212.1)"
     CDS             1..371
                     /gene="Npy6r"
                     /coded_by="NM_010935.4:400..1515"
                     /db_xref="CCDS:CCDS29227.1"
                     /db_xref="GeneID:18169"
                     /db_xref="MGI:MGI:1098590"
ORIGIN      
        1 mevltnqptp nktsgksnns affyfescqp pflailllli aytvilimgi fgnlsliiii
       61 fkkqreaqnv tnilianlsl sdilvcvmci pftviytlmd hwvfgntmck ltsyvqsvsv
      121 svsifslvli aieryqlivn prgwkprvah aywgiiliwl isltlsiplf lsyhltnepf
      181 hnlslptdiy thqvacveiw psklnqllfs tslfmlqyfv plgfilicyl kivlclrkrt
      241 rqvdrrkenk srlnenkrvn vmlisivvtf gacwlplnif nvifdwyhem lmschhdlvf
      301 vvchliamvs tcinplfygf lnknfqkdlm mlihhcwcge pqesyeniam stmhtdeskg
      361 slklahiptg i
//
LOCUS       NP_055550                823 aa            linear   PRI 27-APR-2025
DEFINITION  protein Jade-3 [Homo sapiens].
ACCESSION   NP_055550
VERSION     NP_055550.1
DBSOURCE    REFSEQ: accession NM_014735.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Munir,M., Embry,A., Doench,J.G., Heaton,N.S., Wilen,C.B. and
            Orchard,R.C.
  TITLE     Genome-wide CRISPR activation screen identifies JADE3 as an
            antiviral activator of NF-kB-dependent IFITM3 expression
  JOURNAL   J Biol Chem 300 (4), 107153 (2024)
   PUBMED   38462163
  REMARK    GeneRIF: Genome-wide CRISPR activation screen identifies JADE3 as
            an antiviral activator of NF-kB-dependent IFITM3 expression.
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 823)
  AUTHORS   Jian,Y., Wang,M., Zhang,Y., Ou,R., Zhu,Z., Ou,Y., Chen,X.,
            Liang,X., Ding,Y., Song,L., Xu,X. and Liao,W.
  TITLE     Jade family PHD finger 3 (JADE3) increases cancer stem cell-like
            properties and tumorigenicity in colon cancer
  JOURNAL   Cancer Lett 428, 1-11 (2018)
   PUBMED   29660380
  REMARK    GeneRIF: JADE3 was markedly upregulated in colon cancer tissues and
            correlated with cancer progression and predicted shorter patient
            survival. JADE3 interacted with the promoters of LGR5 and activated
            its transcription, by increasing the occupancy of p300
            acetyltransferase and histone acetylation on the promoters. These
            findings suggest an oncogenic role of JADE3 by regulating cancer
            stem cell-like traits in the colon cancer.
REFERENCE   5  (residues 1 to 823)
  AUTHORS   Liu,Y.X., Zhang,S.F., Ji,Y.H., Guo,S.J., Wang,G.F. and Zhang,G.W.
  TITLE     Whole-exome sequencing identifies mutated PCK2 and HUWE1 associated
            with carcinoma cell proliferation in a hepatocellular carcinoma
            patient
  JOURNAL   Oncol Lett 4 (4), 847-851 (2012)
   PUBMED   23205112
REFERENCE   6  (residues 1 to 823)
  AUTHORS   Doyon,Y., Cayrou,C., Ullah,M., Landry,A.J., Cote,V., Selleck,W.,
            Lane,W.S., Tan,S., Yang,X.J. and Cote,J.
  TITLE     ING tumor suppressor proteins are critical regulators of chromatin
            acetylation required for genome expression and perpetuation
  JOURNAL   Mol Cell 21 (1), 51-64 (2006)
   PUBMED   16387653
REFERENCE   7  (residues 1 to 823)
  AUTHORS   Tzouanacou,E., Tweedie,S. and Wilson,V.
  TITLE     Identification of Jade1, a gene encoding a PHD zinc finger protein,
            in a gene trap mutagenesis screen for genes involved in
            anteroposterior axis development
  JOURNAL   Mol Cell Biol 23 (23), 8553-8552 (2003)
   PUBMED   14612400
REFERENCE   8  (residues 1 to 823)
  AUTHORS   Thiselton,D.L., McDowall,J., Brandau,O., Ramser,J., d'Esposito,F.,
            Bhattacharya,S.S., Ross,M.T., Hardcastle,A.J. and Meindl,A.
  TITLE     An integrated, functionally annotated gene map of the DXS8026-ELK1
            interval on human Xp11.3-Xp11.23: potential hotspot for
            neurogenetic disorders
  JOURNAL   Genomics 79 (4), 560-572 (2002)
   PUBMED   11944989
  REMARK    Erratum:[Genomics 2002 Jun;79(6):891]
REFERENCE   9  (residues 1 to 823)
  AUTHORS   Szelei,J., Soto,A.M., Geck,P., Desronvil,M., Prechtl,N.V.,
            Weill,B.C. and Sonnenschein,C.
  TITLE     Identification of human estrogen-inducible transcripts that
            potentially mediate the apoptotic response in breast cancer
  JOURNAL   J Steroid Biochem Mol Biol 72 (3-4), 89-102 (2000)
   PUBMED   10775800
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627143.15, BN000289.1,
            AF127774.1 and AW071647.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of a family of large proteins
            containing PHD (plant homeo domain)-type zinc fingers. The encoded
            protein may be associated in a nuclear complex that functions in
            histone H4 acetylation. Alternative splicing results in multiple
            transcript variants encoding the same protein. [provided by RefSeq,
            Aug 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BN000289.1, D86969.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000614628.5/ ENSP00000481850.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.3"
     Protein         1..823
                     /product="protein Jade-3"
                     /note="PHD finger protein 16; jade family PHD finger
                     protein 3"
                     /calculated_mol_wt=93677
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92613.1)"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92613.1)"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92613.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92613.1)"
     Region          138..533
                     /region_name="COG5141"
                     /note="PHD zinc finger-containing protein [General
                     function prediction only]"
                     /db_xref="CDD:227470"
     Region          255..365
                     /region_name="ePHD_JADE3"
                     /note="Extended PHD finger found in protein Jade-3 and
                     similar proteins; cd15706"
                     /db_xref="CDD:277176"
     Site            order(311,321..325,331,360)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277176"
     Region          372..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92613.1)"
     Region          542..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92613.1)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92613.1)"
     Site            601
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6IE82; propagated from
                     UniProtKB/Swiss-Prot (Q92613.1)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92613.1)"
     Region          609..630
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92613.1)"
     Site            638
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92613.1)"
     Region          650..684
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92613.1)"
     Site            735
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6IE82; propagated from
                     UniProtKB/Swiss-Prot (Q92613.1)"
     Region          758..823
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92613.1)"
     Site            774
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92613.1)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92613.1)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92613.1)"
     CDS             1..823
                     /gene="JADE3"
                     /gene_synonym="JADE-3; PHF16"
                     /coded_by="NM_014735.5:311..2782"
                     /db_xref="CCDS:CCDS14271.1"
                     /db_xref="GeneID:9767"
                     /db_xref="HGNC:HGNC:22982"
                     /db_xref="MIM:300618"
ORIGIN      
        1 mkrhrpvsss dssdespsts ftsgsmyrik skipnehkkp aevfrkdlis amklpdshhi
       61 npdsyylfad twkeewekgv qvpaspdtvp qpslriiaek vkdvlfirpr kyihcsspdt
      121 tepgyinime laasvcrydl ddmdifwlqe lnedlaemgc gpvdenlmek tvevlerhch
      181 enmnhaiete eglgieyded vicdvcrspd seegndmvfc dkcnvcvhqa cygilkvpeg
      241 swlcrscvlg iypqcvlcpk kggalkttkt gtkwahvsca lwipevsiac permepitki
      301 shippsrwal vcnlcklktg aciqcsiksc itafhvtcaf ehglemktil degdevkfks
      361 yclkhsqnrq klgeaeyphh rakeqsqaks ektslraqkl releeefysl vrvedvaael
      421 gmptlavdfi ynywklkrks nfnkplfppk edeenglvqp keesihtrmr mfmhlrqdle
      481 rvrnlcymis rreklklshn kiqeqifglq vqllnqeida glpltnalen slfyppprit
      541 lklkmpkstp edhrnsstet dqqphspdss ssvhsirnmq vpqeslemrt ksypryples
      601 knnrllasls hsrseakess pawrtpssec yhgqslgkpl vlqaalhgqs signgksqpn
      661 skfaksngle gswsgnvtqk dsssemfcdq epvfsphlvs qgsfrkstve hfsrsfkett
      721 nrwvkntedl qcyvkptknm spkeqfwgrq vlrrsagrap yqendgycpd lelsdseaes
      781 dgnkekvrvr kdssdrenpp hdsrrdchgk skthplshss mqr
//
LOCUS       NP_001355787             359 aa            linear   ROD 27-APR-2025
DEFINITION  growth hormone-regulated TBC protein 1 isoform 2 [Mus musculus].
ACCESSION   NP_001355787
VERSION     NP_001355787.1
DBSOURCE    REFSEQ: accession NM_001368858.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Shalom-Barak,T., Zhang,X., Chu,T., Timothy Schaiff,W., Reddy,J.K.,
            Xu,J., Sadovsky,Y. and Barak,Y.
  TITLE     Placental PPARgamma regulates spatiotemporally diverse genes and a
            unique metabolic network
  JOURNAL   Dev Biol 372 (1), 143-155 (2012)
   PUBMED   22967998
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Lu,C., Kasik,J., Stephan,D.A., Yang,S., Sperling,M.A. and
            Menon,R.K.
  TITLE     Grtp1, a novel gene regulated by growth hormone
  JOURNAL   Endocrinology 142 (10), 4568-4571 (2001)
   PUBMED   11564724
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK007905.1, AK017251.1 and AK149322.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK017251.1, SRR17784646.452781.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 5.73 cM"
     Protein         1..359
                     /product="growth hormone-regulated TBC protein 1 isoform
                     2"
                     /note="growth hormone-regulated TBC protein 1; TBC1 domain
                     family member 6"
                     /calculated_mol_wt=40497
     Region          71..301
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..359
                     /gene="Grtp1"
                     /gene_synonym="5430401C05Rik; Tbc1d6"
                     /coded_by="NM_001368858.1:98..1177"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS90375.1"
                     /db_xref="GeneID:66790"
                     /db_xref="MGI:MGI:1914040"
ORIGIN      
        1 mdpaeraqaa rarvpridpy gferpedfdy aayeeffsty lviltkraik wskllkgngg
       61 vrksvtvkry vrkgiplehr arvwmavsga qarmdqspgy yhrllegess ssldeairtd
      121 lnrtfpdnvm frktadpclq ktlynvllay glhnpdvgyc qccaqkpgss aglrssltgm
      181 nfiagylili tkneeesfwl ldalvgrilp dyyspamlgl ktdqevlael vrmklpavaa
      241 lmdghgvlwt llvsrwficl fvdilpvetv lriwdclfne gskiifrval tlikqhqefi
      301 leassipdic dkfkqitkgd fvtechafmq kifsepgsls mttitrlrks craalqaqs
//
LOCUS       NP_114156                223 aa            linear   PRI 27-APR-2025
DEFINITION  fibroblast growth factor-binding protein 2 precursor [Homo
            sapiens].
ACCESSION   NP_114156
VERSION     NP_114156.1
DBSOURCE    REFSEQ: accession NM_031950.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Liu,Z., Ma,C., Gu,J. and Yu,M.
  TITLE     Potential biomarkers of acute myocardial infarction based on
            weighted gene co-expression network analysis
  JOURNAL   Biomed Eng Online 18 (1), 9 (2019)
   PUBMED   30683112
  REMARK    GeneRIF: three overlapping genes (FGFBP2, GFOD1 and MLC1) between
            two modules could potentially have a role in acute myocardial
            infarction and have diagnostic potential
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Salemi,M., Barone,C., Morale,M.C., Caniglia,S., Romano,C.,
            Salluzzo,M.G., Rando,R.G., Ragalmuto,A., Bosco,P. and Romano,C.
  TITLE     Killer-specific secretory (Ksp37) gene expression in subjects with
            Down's syndrome
  JOURNAL   Neurol Sci 37 (5), 793-795 (2016)
   PUBMED   27032399
  REMARK    GeneRIF: results of this study suggest that the expression of Ksp37
            gene might be associated with increased susceptibility of
            individuals with Down syndrome to EBV infections and autoimmune
            problems.
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Jeff,J.M., Ritchie,M.D., Denny,J.C., Kho,A.N., Ramirez,A.H.,
            Crosslin,D., Armstrong,L., Basford,M.A., Wolf,W.A., Pacheco,J.A.,
            Chisholm,R.L., Roden,D.M., Hayes,M.G. and Crawford,D.C.
  TITLE     Generalization of variants identified by genome-wide association
            studies for electrocardiographic traits in African Americans
  JOURNAL   Ann Hum Genet 77 (4), 321-332 (2013)
   PUBMED   23534349
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Elgaaen,B.V., Haug,K.B., Wang,J., Olstad,O.K., Fortunati,D.,
            Onsrud,M., Staff,A.C., Sauer,T. and Gautvik,K.M.
  TITLE     POLD2 and KSP37 (FGFBP2) correlate strongly with histology, stage
            and outcome in ovarian carcinomas
  JOURNAL   PLoS One 5 (11), e13837 (2010)
   PUBMED   21079801
  REMARK    GeneRIF: Results suggest that POLD2 and KSP37 might be potential
            prognostic biomarkers.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Yamanaka,R., Arao,T., Yajima,N., Tsuchiya,N., Homma,J., Tanaka,R.,
            Sano,M., Oide,A., Sekijima,M. and Nishio,K.
  TITLE     Identification of expressed genes characterizing long-term survival
            in malignant glioma patients
  JOURNAL   Oncogene 25 (44), 5994-6002 (2006)
   PUBMED   16652150
REFERENCE   7  (residues 1 to 223)
  AUTHORS   Kuepper,M., Bratke,K., Julius,P., Ogawa,K., Nagata,K., Luttmann,W.
            and Virchow,J.C. Jr.
  TITLE     Increase in killer-specific secretory protein of 37 kDa in
            bronchoalveolar lavage fluid of allergen-challenged patients with
            atopic asthma
  JOURNAL   Clin Exp Allergy 35 (5), 643-649 (2005)
   PUBMED   15898988
REFERENCE   8  (residues 1 to 223)
  AUTHORS   Hayano,C., Koi,H., Ogawa,K., Nagata,K., Matsumoto,Y., Nakamura,M.
            and Aso,T.
  TITLE     Accumulation of CD16+ cells with secretion of Ksp37 in decidua at
            the end of pregnancy
  JOURNAL   Am J Reprod Immunol 48 (1), 57-62 (2002)
   PUBMED   12322897
  REMARK    GeneRIF: Secreted from NK cells in decidua, elevated at late
            gestational period.
REFERENCE   9  (residues 1 to 223)
  AUTHORS   Ogawa,K., Tanaka,K., Ishii,A., Nakamura,Y., Kondo,S., Sugamura,K.,
            Takano,S., Nakamura,M. and Nagata,K.
  TITLE     A novel serum protein that is selectively produced by cytotoxic
            lymphocytes
  JOURNAL   J Immunol 166 (10), 6404-6412 (2001)
   PUBMED   11342666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY358978.1, AC005598.6 and
            CN480296.1.
            
            Summary: This gene encodes a member of the fibroblast growth factor
            binding protein family. The encoded protein is a serum protein that
            is selectively secreted by cytotoxic lymphocytes and may be
            involved in cytotoxic lymphocyte-mediated immunity. An increase in
            the amount of gene product may be associated with atopic asthma and
            mild extrinsic asthma.[provided by RefSeq, Jan 2025].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358978.1, BC025720.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259989.7/ ENSP00000259989.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.32"
     Protein         1..223
                     /product="fibroblast growth factor-binding protein 2
                     precursor"
                     /note="killer-specific secretory protein of 37 kDa;
                     FGF-binding protein 2; HBp17-related protein; FGF-BP2;
                     FGFBP-2; HBp17-RP; 37 kDa killer-specific secretory
                     protein"
                     /calculated_mol_wt=22591
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2009
     Region          5..223
                     /region_name="FGF-BP1"
                     /note="FGF binding protein 1 (FGF-BP1); pfam06473"
                     /db_xref="CDD:461927"
     mat_peptide     20..223
                     /product="fibroblast growth factor-binding protein 2"
                     /calculated_mol_wt=22591
     Region          23..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYJ0.1)"
     Region          120..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYJ0.1)"
     CDS             1..223
                     /gene="FGFBP2"
                     /gene_synonym="HBP17RP; KSP37"
                     /coded_by="NM_031950.4:47..718"
                     /db_xref="CCDS:CCDS3419.1"
                     /db_xref="GeneID:83888"
                     /db_xref="HGNC:HGNC:29451"
                     /db_xref="MIM:607713"
ORIGIN      
        1 mkfvpclllv tlsclgtlgq aprqkqgstg eefhfqtggr dsctmrpssl gqgagevwlr
       61 vdcrntdqty wceyrgqpsm cqafaadpkp ywnqalqelr rlhhacqgap vlrpsvcrea
      121 gpqahmqqvt sslkgspepn qqpeagtpsl rpkatvklte atqlgkdsme elgkakpttr
      181 ptakptqpgp rpggneeakk kawehcwkpf qalcaflisf frg
//
LOCUS       NP_059116                781 aa            linear   PRI 27-APR-2025
DEFINITION  homeobox protein SIX4 [Homo sapiens].
ACCESSION   NP_059116
VERSION     NP_059116.3
DBSOURCE    REFSEQ: accession NM_017420.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Heiat,M., Rezaei,E., Gharechahi,J., Abbasi,M., Behroozi,J.,
            Abyazi,M.A. and Baradaran,B.
  TITLE     Knockdown of SIX4 inhibits pancreatic cancer cells via apoptosis
            induction
  JOURNAL   Med Oncol 40 (10), 287 (2023)
   PUBMED   37656231
  REMARK    GeneRIF: Knockdown of SIX4 inhibits pancreatic cancer cells via
            apoptosis induction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Li,B., Dang,X., Duan,J., Zhang,G., Zhang,J. and Song,Q.
  TITLE     SIX4 upregulates IDH1 and metabolic reprogramming to promote
            osteosarcoma progression
  JOURNAL   J Cell Mol Med 27 (2), 259-265 (2023)
   PUBMED   36601689
  REMARK    GeneRIF: SIX4 upregulates IDH1 and metabolic reprogramming to
            promote osteosarcoma progression.
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Han,J. and Hu,X.
  TITLE     IGF2BP3-stabilized SIX4 promotes the proliferation, migration,
            invasion and tube formation of ovarian cancer cells
  JOURNAL   Mol Med Rep 26 (1) (2022)
   PUBMED   35616130
  REMARK    GeneRIF: IGF2BP3stabilized SIX4 promotes the proliferation,
            migration, invasion and tube formation of ovarian cancer cells.
REFERENCE   4  (residues 1 to 781)
  AUTHORS   Li,Y., Jiang,X., Yan,X. and Wang,Y.
  TITLE     Upregulation of SIX4 indicates poor clinical outcome and promotes
            tumor growth and cell metastasis in esophageal squamous cell
            carcinoma
  JOURNAL   Thorac Cancer 12 (6), 752-759 (2021)
   PUBMED   33481352
  REMARK    GeneRIF: Upregulation of SIX4 indicates poor clinical outcome and
            promotes tumor growth and cell metastasis in esophageal squamous
            cell carcinoma.
REFERENCE   5  (residues 1 to 781)
  AUTHORS   He,Q., Lin,Z., Wang,Z., Huang,W., Tian,D., Liu,M. and Xia,L.
  TITLE     SIX4 promotes hepatocellular carcinoma metastasis through
            upregulating YAP1 and c-MET
  JOURNAL   Oncogene 39 (50), 7279-7295 (2020)
   PUBMED   33046796
  REMARK    GeneRIF: SIX4 promotes hepatocellular carcinoma metastasis through
            upregulating YAP1 and c-MET.
REFERENCE   6  (residues 1 to 781)
  AUTHORS   Liu,Q., Li,A., Tian,Y., Liu,Y., Li,T., Zhang,C., Wu,J.D., Han,X.
            and Wu,K.
  TITLE     The expression profile and clinic significance of the SIX family in
            non-small cell lung cancer
  JOURNAL   J Hematol Oncol 9 (1), 119 (2016)
   PUBMED   27821176
  REMARK    GeneRIF: SIX4 and SIX6 were linked to the lymph node metastasis in
            NSCLC.
            Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 781)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   8  (residues 1 to 781)
  AUTHORS   Gallardo,M.E., Lopez-Rios,J., Fernaud-Espinosa,I., Granadino,B.,
            Sanz,R., Ramos,C., Ayuso,C., Seller,M.J., Brunner,H.G.,
            Bovolenta,P. and Rodriguez de Cordoba,S.
  TITLE     Genomic cloning and characterization of the human homeobox gene
            SIX6 reveals a cluster of SIX genes in chromosome 14 and associates
            SIX6 hemizygosity with bilateral anophthalmia and pituitary
            anomalies
  JOURNAL   Genomics 61 (1), 82-91 (1999)
   PUBMED   10512683
REFERENCE   9  (residues 1 to 781)
  AUTHORS   Ozaki,H., Yamada,K., Kobayashi,M., Asakawa,S., Minoshima,S.,
            Shimizu,N., Kajitani,M. and Kawakami,K.
  TITLE     Structure and chromosome mapping of the human SIX4 and murine Six4
            genes
  JOURNAL   Cytogenet Cell Genet 87 (1-2), 108-112 (1999)
   PUBMED   10640827
REFERENCE   10 (residues 1 to 781)
  AUTHORS   Kawakami,K., Ohto,H., Ikeda,K. and Roeder,R.G.
  TITLE     Structure, function and expression of a murine homeobox protein
            AREC3, a homologue of Drosophila sine oculis gene product, and
            implication in development
  JOURNAL   Nucleic Acids Res 24 (2), 303-310 (1996)
   PUBMED   8628654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL132777.4, BC099722.1 and
            AA424469.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 6, 2007 this sequence version replaced NP_059116.2.
            
            Summary: This gene encodes a member of the homeobox family,
            subfamily SIX. The drosophila homolog is a nuclear homeoprotein
            required for eye development. Studies in mouse show that this gene
            product functions as a transcription factor, and may have a role in
            the differentiation or maturation of neuronal cells. [provided by
            RefSeq, May 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.140483.1, BC098135.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216513.5/ ENSP00000216513.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.1"
     Protein         1..781
                     /product="homeobox protein SIX4"
                     /note="sine oculis homeobox homolog 4"
                     /calculated_mol_wt=82803
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIU6.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UIU6.2)"
     Region          108..217
                     /region_name="SIX1_SD"
                     /note="Transcriptional regulator, SIX1, N-terminal SD
                     domain; pfam16878"
                     /db_xref="CDD:465293"
     Region          228..282
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(229,269,272..273,276)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          270..321
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIU6.2)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q9UIU6.2)"
     CDS             1..781
                     /gene="SIX4"
                     /gene_synonym="AREC3"
                     /coded_by="NM_017420.5:278..2623"
                     /db_xref="CCDS:CCDS9749.2"
                     /db_xref="GeneID:51804"
                     /db_xref="HGNC:HGNC:10890"
                     /db_xref="MIM:606342"
ORIGIN      
        1 mssssptgqi asaadikqen gmesasegqe ahrevaggaa vglsppapap fplepgdaat
       61 aaarvsgeeg avaaaaagaa adqvqlhsel lgrhhhaaaa aaqtplafsp dhvacvceal
      121 qqggnldrla rflwslpqsd llrgnesllk aralvafhqg iypelysile shsfesanhp
      181 llqqlwykar yteaerargr plgavdkyrl rrkfplprti wdgeetvycf keksrnalke
      241 lykqnrypsp aekrhlakit glsltqvsnw fknrrqrdrn psetqskses dgnpstedes
      301 skghedlsph plssssdgit nlslsshmep vymqqignak islsssgvll ngslvpasts
      361 pvflngnsfi qgpsgvilng lnvgntqava lnppkmssni vsngismtdi lgstsqdvke
      421 fkvlqssans atttsyspsv pvsfpglips tevkregiqt vasqdggsvv tfttpvqinq
      481 ygivqipnsg ansqflngsi gfsplqlppv svaasqgnis vssstsdgst ftsesttvqq
      541 gkvflsslap savvytvpnt gqtigsvkqe glerslvfsq lmpvnqnaqv nanlssenis
      601 gsglhplass lvnvspthnf slspstllnp telnrdiads qpmsapvask stvtsvsntn
      661 yatlqncsli tgqdllsvpm tqaalgeivp taedqvghps pavhqdfvqe hrlvlqsvan
      721 mkenflsnse skatsslmml dskskyvldg mvdtvcedle tdkkelaklq tvqldedmqd
      781 l
//
LOCUS       NP_000670                520 aa            linear   PRI 27-APR-2025
DEFINITION  alpha-1B adrenergic receptor [Homo sapiens].
ACCESSION   NP_000670
VERSION     NP_000670.1
DBSOURCE    REFSEQ: accession NM_000679.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Masukawa,D., Takahagi,R., Nakao,Y. and Goshima,Y.
  TITLE     L-DOPA Receptor GPR143 Functionally Couples with Adrenergic alpha1B
            Receptor at the Second Transmembrane Interface
  JOURNAL   Biol Pharm Bull 46 (7), 869-873 (2023)
   PUBMED   37394637
  REMARK    GeneRIF: L-DOPA Receptor GPR143 Functionally Couples with
            Adrenergic alpha1B Receptor at the Second Transmembrane Interface.
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Renkhold,L., Kollmann,R., Inderwiedenstrasse,L. and Kienitz,M.C.
  TITLE     PKC-isoform specific regulation of receptor desensitization and
            KCNQ1/KCNE1 K+ channel activity by mutant alpha1B-adrenergic
            receptors
  JOURNAL   Cell Signal 91, 110228 (2022)
   PUBMED   34958868
  REMARK    GeneRIF: PKC-isoform specific regulation of receptor
            desensitization and KCNQ1/KCNE1 K(+) channel activity by mutant
            alpha1B-adrenergic receptors.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Gao,X., Enten,G.A., DeSantis,A.J., Volkman,B.F., Gaponenko,V. and
            Majetschak,M.
  TITLE     Characterization of heteromeric complexes between chemokine (C-X-C
            motif) receptor 4 and alpha1-adrenergic receptors utilizing
            intermolecular bioluminescence resonance energy transfer assays
  JOURNAL   Biochem Biophys Res Commun 528 (2), 368-375 (2020)
   PUBMED   32085899
  REMARK    GeneRIF: Characterization of heteromeric complexes between
            chemokine (C-X-C motif) receptor 4 and alpha1-adrenergic receptors
            utilizing intermolecular bioluminescence resonance energy transfer
            assays.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Hernandez-Espinosa,D.A., Reyes-Cruz,G. and Garcia-Sainz,J.A.
  TITLE     Roles of the G protein-coupled receptor kinase 2 and Rab5 in
            alpha1B-adrenergic receptor function and internalization
  JOURNAL   Eur J Pharmacol 867, 172846 (2020)
   PUBMED   31811856
  REMARK    GeneRIF: Study data indicate that GRK2 and RAB5 play key roles in
            alpha1B-adrenergic receptor phosphorylation, internalization, and
            desensitization. The possibility that RAB5 might form part of a
            signaling complex is suggested, as well as that GDP-Rab5 might
            interfere with the ability of GRK2 to catalyze alpha1B-adrenergic
            receptor phosphorylation.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Wijaya,L.K., Stumbles,P.A. and Drummond,P.D.
  TITLE     Tumor necrosis factor alpha induces alpha1B-adrenergic receptor
            expression in keratinocytes
  JOURNAL   Cytokine 125, 154851 (2020)
   PUBMED   31520851
  REMARK    GeneRIF: Tumor necrosis factor alpha induces alpha1B-adrenergic
            receptor expression in keratinocytes.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Warrington,J.A. and Bengtsson,U.
  TITLE     High-resolution physical mapping of human 5q31-q33 using three
            methods: radiation hybrid mapping, interphase fluorescence in situ
            hybridization, and pulsed-field gel electrophoresis
  JOURNAL   Genomics 24 (2), 395-398 (1994)
   PUBMED   7698768
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Ramarao,C.S., Denker,J.M., Perez,D.M., Gaivin,R.J., Riek,R.P. and
            Graham,R.M.
  TITLE     Genomic organization and expression of the human alpha
            1B-adrenergic receptor
  JOURNAL   J Biol Chem 267 (30), 21936-21945 (1992)
   PUBMED   1328250
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Allen,L.F., Lefkowitz,R.J., Caron,M.G. and Cotecchia,S.
  TITLE     G-protein-coupled receptor genes as protooncogenes: constitutively
            activating mutation of the alpha 1B-adrenergic receptor enhances
            mitogenesis and tumorigenicity
  JOURNAL   Proc Natl Acad Sci U S A 88 (24), 11354-11358 (1991)
   PUBMED   1662393
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Lomasney,J.W., Cotecchia,S., Lorenz,W., Leung,W.Y., Schwinn,D.A.,
            Yang-Feng,T.L., Brownstein,M., Lefkowitz,R.J. and Caron,M.G.
  TITLE     Molecular cloning and expression of the cDNA for the alpha
            1A-adrenergic receptor. The gene for which is located on human
            chromosome 5
  JOURNAL   J Biol Chem 266 (10), 6365-6369 (1991)
   PUBMED   1706716
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Yang-Feng,T.L., Xue,F.Y., Zhong,W.W., Cotecchia,S., Frielle,T.,
            Caron,M.G., Lefkowitz,R.J. and Francke,U.
  TITLE     Chromosomal organization of adrenergic receptor genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (4), 1516-1520 (1990)
   PUBMED   2154750
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011343.3, U03865.1,
            BQ576306.1 and AC068657.6.
            
            Summary: Alpha-1-adrenergic receptors (alpha-1-ARs) are members of
            the G protein-coupled receptor superfamily. They activate mitogenic
            responses and regulate growth and proliferation of many cells.
            There are 3 alpha-1-AR subtypes: alpha-1A, -1B and -1D, all of
            which signal through the Gq/11 family of G-proteins and different
            subtypes show different patterns of activation. This gene encodes
            alpha-1B-adrenergic receptor, which induces neoplastic
            transformation when transfected into NIH 3T3 fibroblasts and other
            cell lines. Thus, this normal cellular gene is identified as a
            protooncogene. This gene comprises 2 exons and a single large
            intron of at least 20 kb that interrupts the coding region.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U03865.1, BC136568.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306675.5/ ENSP00000306662.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..520
                     /product="alpha-1B adrenergic receptor"
                     /note="alpha-1B adrenoceptor; alpha-1B adrenoreceptor;
                     adrenergic, alpha-1B-, receptor"
                     /calculated_mol_wt=56705
     Site            10
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35368.3)"
     Site            24
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35368.3)"
     Site            29
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35368.3)"
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35368.3)"
     Region          46..359
                     /region_name="7tmA_alpha1B_AR"
                     /note="alpha-1 adrenergic receptors subtype B, member of
                     the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15326"
                     /db_xref="CDD:320449"
     Site            46..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          47..73
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320449"
     Region          80..106
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320449"
     Site            84..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Site            116..141
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          118..148
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320449"
     Site            order(121,125..126,129..130,197,204,207..208,211,307,
                     310..311,314,330,334,338)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320449"
     Region          160..183
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320449"
     Site            162..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          200..229
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320449"
     Site            202..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P97717; propagated from
                     UniProtKB/Swiss-Prot (P35368.3)"
     Region          287..317
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320449"
     Site            296..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          327..352
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320449"
     Site            327..351
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          368..380
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          394..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          479..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     CDS             1..520
                     /gene="ADRA1B"
                     /gene_synonym="ADRA1; ALPHA1BAR"
                     /coded_by="NM_000679.4:425..1987"
                     /db_xref="CCDS:CCDS4347.1"
                     /db_xref="GeneID:147"
                     /db_xref="HGNC:HGNC:278"
                     /db_xref="MIM:104220"
ORIGIN      
        1 mnpdldtghn tsapahwgel knanftgpnq tssnstlpql ditraisvgl vlgafilfai
       61 vgnilvilsv acnrhlrtpt nyfivnlama dlllsftvlp fsaalevlgy wvlgrifcdi
      121 waavdvlcct asilslcais idryigvrys lqyptlvtrr kailallsvw vlstvisigp
      181 llgwkepapn ddkecgvtee pfyalfsslg sfyiplavil vmycrvyiva krttknleag
      241 vmkemsnske ltlrihsknf hedtlsstka kghnprssia vklfkfsrek kaaktlgivv
      301 gmfilcwlpf fialplgslf stlkppdavf kvvfwlgyfn sclnpiiypc sskefkrafv
      361 rilgcqcrgr grrrrrrrrr lggcaytyrp wtrggslers qsrkdsldds gsclsgsqrt
      421 lpsaspspgy lgrgapppve lcafpewkap gallslpape ppgrrgrhds gplftfkllt
      481 epespgtdgg asnggceaaa dvangqpgfk snmplapgqf
//
LOCUS       NP_001123484             337 aa            linear   PRI 27-APR-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF2 isoform a [Homo
            sapiens].
ACCESSION   NP_001123484
VERSION     NP_001123484.1
DBSOURCE    REFSEQ: accession NM_001130012.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Zizak,M., Lamprecht,G., Steplock,D., Tariq,N., Shenolikar,S.,
            Donowitz,M., Yun,C.H. and Weinman,E.J.
  TITLE     cAMP-induced phosphorylation and inhibition of Na(+)/H(+) exchanger
            3 (NHE3) are dependent on the presence but not the phosphorylation
            of NHE regulatory factor
  JOURNAL   J Biol Chem 274 (35), 24753-24758 (1999)
   PUBMED   10455146
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Imai,K., Sarker,A.H., Akiyama,K., Ikeda,S., Yao,M., Tsutsui,K.,
            Shohmori,T. and Seki,S.
  TITLE     Genomic structure and sequence of a human homologue (NTHL1/NTH1) of
            Escherichia coli endonuclease III with those of the adjacent parts
            of TSC2 and SLC9A3R2 genes
  JOURNAL   Gene 222 (2), 287-295 (1998)
   PUBMED   9831664
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Yun,C.H., Lamprecht,G., Forster,D.V. and Sidor,A.
  TITLE     NHE3 kinase A regulatory protein E3KARP binds the epithelial brush
            border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin
  JOURNAL   J Biol Chem 273 (40), 25856-25863 (1998)
   PUBMED   9748260
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Hall,R.A., Ostedgaard,L.S., Premont,R.T., Blitzer,J.T., Rahman,N.,
            Welsh,M.J. and Lefkowitz,R.J.
  TITLE     A C-terminal motif found in the beta2-adrenergic receptor, P2Y1
            receptor and cystic fibrosis transmembrane conductance regulator
            determines binding to the Na+/H+ exchanger regulatory factor family
            of PDZ proteins
  JOURNAL   Proc Natl Acad Sci U S A 95 (15), 8496-8501 (1998)
   PUBMED   9671706
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Yun,C.H., Oh,S., Zizak,M., Steplock,D., Tsao,S., Tse,C.M.,
            Weinman,E.J. and Donowitz,M.
  TITLE     cAMP-mediated inhibition of the epithelial brush border Na+/H+
            exchanger, NHE3, requires an associated regulatory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (7), 3010-3015 (1997)
   PUBMED   9096337
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1997 Sep 2;94(18):10006]
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Poulat,F., de Santa Barbara,P., Desclozeaux,M., Soullier,S.,
            Moniot,B., Bonneaud,N., Boizet,B. and Berta,P.
  TITLE     The human testis determining factor SRY binds a nuclear factor
            containing PDZ protein interaction domains
  JOURNAL   J Biol Chem 272 (11), 7167-7172 (1997)
   PUBMED   9054412
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC014513.1 and AC093513.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the NHERF family of PDZ
            scaffolding proteins. These proteins mediate many cellular
            processes by binding to and regulating the membrane expression and
            protein-protein interactions of membrane receptors and transport
            proteins. The encoded protein plays a role in intestinal sodium
            absorption by regulating the activity of the sodium/hydrogen
            exchanger 3, and may also regulate the cystic fibrosis
            transmembrane regulator (CFTR) ion channel. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Nov 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014513.1, AF004900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000424542.7/ ENSP00000408005.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..337
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF2
                     isoform a"
                     /note="solute carrier family 9, subfamily A (NHE3, cation
                     proton antiporter 3), member 3 regulator 2; Na(+)/H(+)
                     exchange regulatory cofactor NHE-RF2; SRY-interacting
                     protein 1; tyrosine kinase activator protein 1; NHE3
                     kinase A regulatory protein E3KARP; NHE3 regulatory factor
                     2; SLC9A3 regulator 2; sodium/hydrogen exchanger 3 kinase
                     A regulatory protein; solute carrier family 9
                     (sodium/hydrogen exchanger), member 3 regulator 2;
                     Na(+)/H(+) exchange regulatory cofactor 2"
                     /calculated_mol_wt=37283
     Region          10..89
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(20..26,37,40,69,73,76..77)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          107..144
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15599.2)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHL1; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     Region          150..229
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(160..166,177,180,209,213,216..217)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     Region          232..337
                     /region_name="EBP50_C"
                     /note="EBP50, C-terminal; pfam09007"
                     /db_xref="CDD:462654"
     Region          240..337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15599.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHL1; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     CDS             1..337
                     /gene="NHERF2"
                     /gene_synonym="E3KARP; NHE3RF2; NHERF-2; OCTS2; SIP-1;
                     SIP1; SLC9A3R2; TKA-1"
                     /coded_by="NM_001130012.3:105..1118"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45382.1"
                     /db_xref="GeneID:9351"
                     /db_xref="HGNC:HGNC:11076"
                     /db_xref="MIM:606553"
ORIGIN      
        1 maapeplrpr lcrlvrgeqg ygfhlhgekg rrgqfirrve pgspaeaaal ragdrlvevn
       61 gvnvegethh qvvqrikave gqtrllvvdq etdeelrrrq ltcteemaqr glppahdpwe
      121 pkpdwahtgs hsseagkkdv sgplrelrpr lchlrkgpqg ygfnlhsdks rpgqyirsvd
      181 pgspaarsgl raqdrlievn gqnveglrha evvasikare dearllvvdp etdehfkrlr
      241 vtpteehveg plpspvtngt spaqlnggsa cssrsdlpgs dkdtedgsaw kqdpfqesgl
      301 hlsptaaeak ekaramrvnk rapqmdwnrk reifsnf
//
LOCUS       NP_056234               2828 aa            linear   PRI 27-APR-2025
DEFINITION  matrix-remodeling-associated protein 5 precursor [Homo sapiens].
ACCESSION   NP_056234
VERSION     NP_056234.2
DBSOURCE    REFSEQ: accession NM_015419.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2828)
  AUTHORS   Nie,L., Huang,L., Zhu,Q., Yao,Q., Wu,Y., Zhao,L., Yu,L. and Fu,F.
  TITLE     HIF-1alpha Activates Hypoxia-Induced MXRA5 Expression in the
            Progression of Ovarian Cancer
  JOURNAL   J Environ Pathol Toxicol Oncol 44 (1), 47-55 (2025)
   PUBMED   39462449
  REMARK    GeneRIF: HIF-1alpha Activates Hypoxia-Induced MXRA5 Expression in
            the Progression of Ovarian Cancer.
REFERENCE   2  (residues 1 to 2828)
  AUTHORS   Sun,Y., Yang,H., Guo,J., Du,J., Han,S. and Yang,X.
  TITLE     Identification of HTRA1, DPT and MXRA5 as potential biomarkers
            associated with osteoarthritis progression and immune infiltration
  JOURNAL   BMC Musculoskelet Disord 25 (1), 647 (2024)
   PUBMED   39148085
  REMARK    GeneRIF: Identification of HTRA1, DPT and MXRA5 as potential
            biomarkers associated with osteoarthritis progression and immune
            infiltration.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2828)
  AUTHORS   Yoshida,K., Suzuki,S., Yuan,H., Sato,A., Hirata-Tsuchiya,S.,
            Saito,M., Yamada,S. and Shiba,H.
  TITLE     Public RNA-seq data-based identification and functional analyses
            reveal that MXRA5 retains proliferative and migratory abilities of
            dental pulp stem cells
  JOURNAL   Sci Rep 13 (1), 15574 (2023)
   PUBMED   37730838
  REMARK    GeneRIF: Public RNA-seq data-based identification and functional
            analyses reveal that MXRA5 retains proliferative and migratory
            abilities of dental pulp stem cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2828)
  AUTHORS   Sun,J.Z., Zhang,J.H., Li,J.B., Yuan,F., Tong,L.Q., Wang,X.Y.,
            Chen,L.L., Fan,X.G., Zhang,Y.M., Ren,X., Zhang,C., Yu,S.P. and
            Yang,X.J.
  TITLE     MXRA5 Is a Novel Immune-Related Biomarker That Predicts Poor
            Prognosis in Glioma
  JOURNAL   Dis Markers 2021, 6680883 (2021)
   PUBMED   34211612
  REMARK    GeneRIF: MXRA5 Is a Novel Immune-Related Biomarker That Predicts
            Poor Prognosis in Glioma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2828)
  AUTHORS   Xiao,H., Jiang,Y., He,W., Xu,D., Chen,P., Liu,D., Liu,J., Wang,X.,
            DiSanto,M.E. and Zhang,X.
  TITLE     Identification and functional activity of matrix-remodeling
            associated 5 (MXRA5) in benign hyperplastic prostate
  JOURNAL   Aging (Albany NY) 12 (9), 8605-8621 (2020)
   PUBMED   32392178
  REMARK    GeneRIF: Identification and functional activity of
            matrix-remodeling associated 5 (MXRA5) in benign hyperplastic
            prostate.
REFERENCE   6  (residues 1 to 2828)
  AUTHORS   He,Y., Chen,X., Liu,H., Xiao,H., Kwapong,W.R. and Mei,J.
  TITLE     Matrix-remodeling associated 5 as a novel tissue biomarker predicts
            poor prognosis in non-small cell lung cancers
  JOURNAL   Cancer Biomark 15 (5), 645-651 (2015)
   PUBMED   26406953
  REMARK    GeneRIF: These results indicated the potential value of MXRA5 as a
            novel therapeutic target for the treatment of non-small cell lung
            cancer.
REFERENCE   7  (residues 1 to 2828)
  AUTHORS   Xiong,D., Li,G., Li,K., Xu,Q., Pan,Z., Ding,F., Vedell,P., Liu,P.,
            Cui,P., Hua,X., Jiang,H., Yin,Y., Zhu,Z., Li,X., Zhang,B., Ma,D.,
            Wang,Y. and You,M.
  TITLE     Exome sequencing identifies MXRA5 as a novel cancer gene frequently
            mutated in non-small cell lung carcinoma from Chinese patients
  JOURNAL   Carcinogenesis 33 (9), 1797-1805 (2012)
   PUBMED   22696596
  REMARK    GeneRIF: screened one most frequently mutated novel gene,
            matrix-remodeling associated 5 (MXRA5), in an additional larger
            Chinese sample set of 52 patients with NSCLC and confirmed its high
            somatic mutation frequency
REFERENCE   8  (residues 1 to 2828)
  AUTHORS   Lyons,P.A., Rayner,T.F., Trivedi,S., Holle,J.U., Watts,R.A.,
            Jayne,D.R., Baslund,B., Brenchley,P., Bruchfeld,A., Chaudhry,A.N.,
            Cohen Tervaert,J.W., Deloukas,P., Feighery,C., Gross,W.L.,
            Guillevin,L., Gunnarsson,I., Harper,L., Hruskova,Z., Little,M.A.,
            Martorana,D., Neumann,T., Ohlsson,S., Padmanabhan,S., Pusey,C.D.,
            Salama,A.D., Sanders,J.S., Savage,C.O., Segelmark,M.,
            Stegeman,C.A., Tesar,V., Vaglio,A., Wieczorek,S., Wilde,B.,
            Zwerina,J., Rees,A.J., Clayton,D.G. and Smith,K.G.
  TITLE     Genetically distinct subsets within ANCA-associated vasculitis
  JOURNAL   N Engl J Med 367 (3), 214-223 (2012)
   PUBMED   22808956
REFERENCE   9  (residues 1 to 2828)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   10 (residues 1 to 2828)
  AUTHORS   Chondrogianni,N., de C M Simoes,D., Franceschi,C. and Gonos,E.S.
  TITLE     Cloning of differentially expressed genes in skin fibroblasts from
            centenarians
  JOURNAL   Biogerontology 5 (6), 401-409 (2004)
   PUBMED   15609104
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004616.1, CD626974.1,
            BC064986.1 and AF245505.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2007 this sequence version replaced NP_056234.1.
            
            Summary: This gene encodes one of the matrix-remodelling associated
            proteins. This protein contains 7 leucine-rich repeats and 12
            immunoglobulin-like C2-type domains related to perlecan. This gene
            has a pseudogene on chromosome Y. [provided by RefSeq, Mar 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by transcript alignments. An in-frame AUG is located 25
            codons upstream of the annotated translation start site but is not
            being annotated as a start site since it is poorly conserved, is in
            a weak Kozak sequence context, and is predicted to disrupt an
            N-terminal signal peptide sequence.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF245505.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            MANE Ensembl match               :: ENST00000217939.7/
                                                ENSP00000217939.5
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2828
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.33"
     Protein         1..2828
                     /product="matrix-remodeling-associated protein 5
                     precursor"
                     /note="adlican; adhesion protein with leucine-rich repeats
                     and Immunoglobulin domains related to perlecan;
                     matrix-remodelling associated 5"
                     /calculated_mol_wt=309277
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2893
     mat_peptide     27..2828
                     /product="matrix-remodeling-associated protein 5"
                     /calculated_mol_wt=309277
     Region          38..55
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <46..>218
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          56..77
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          57..80
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          80..101
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          81..104
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          104..125
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          105..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          128..149
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          129..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          152..173
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          153..184
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          184..205
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          185..208
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          217..>263
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Site            287
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NR99.3)"
     Site            321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          486..572
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          497..501
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          510..515
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          538..542
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          552..557
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          590..668
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          595..599
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          608..612
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            633
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          634..638
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          648..653
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          671..715
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Site            702
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:25326458,
                     ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313;
                     propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          933..962
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          1068..1190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          1181..>1561
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     Region          1204..1275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          1367..1389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Site            1403
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          1410..1434
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          <1465..1799
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1479..1499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          1536..1566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          1579..1603
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          1669..1689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          1700..1719
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR99.3)"
     Site            1735
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          1852..1932
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          1958..2042
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1968..1972
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1981..1985
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            2007
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          2008..2012
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2022..2027
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2035..2038
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            2056
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          2065..2137
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          2065..2069
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2078..2082
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2105..2109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2119..2124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2133..2136
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          2147..2225
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          2258..2341
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          2274..2278
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2307..2311
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2321..2326
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2356..2431
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          2364..2368
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2377..2381
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2401..2405
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2415..2420
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2428..2431
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          2457..2535
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          2462..2466
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2475..2480
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2501..2505
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2515..2520
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2528..2531
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          2549..2633
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          2560..2564
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409568"
     Region          2573..2577
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409568"
     Region          2599..2603
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409568"
     Region          2613..2618
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409568"
     Region          2626..2629
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409568"
     Region          2652..2728
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          2655..2659
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2668..2672
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            2693
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NR99.3)"
     Region          2694..2698
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2708..2713
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2732..2814
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     CDS             1..2828
                     /gene="MXRA5"
                     /coded_by="NM_015419.4:167..8653"
                     /db_xref="CCDS:CCDS14124.1"
                     /db_xref="GeneID:25878"
                     /db_xref="HGNC:HGNC:7539"
                     /db_xref="MIM:300938"
ORIGIN      
        1 mpkrahwgal svvlillwgh prvalacphp cacyvpsevh ctfrslasvp agiakhveri
       61 nlgfnsiqal setsfagltk lellmihgne ipsipdgalr dlsslqvfkf synklrvitg
      121 qtlqglsnlm rlhidhnkie fihpqafngl tslrllhleg nllhqlhpst fstftfldyf
      181 rlstirhlyl aenmvrtlpa smlrnmplle nlylqgnpwt cdcemrwfle wdaksrgilk
      241 ckkdkayegg qlcamcfspk klykheihkl kdmtclkpsi esplrqnrsr sieeeqeqee
      301 dggsqlilek fqlpqwsisl nmtdehgnmv nlvcdikkpm dvykihlnqt dppdidinat
      361 valdfecpmt renyeklwkl iayysevpvk lhrelmlskd prvsyqyrqd adeealyytg
      421 vraqilaepe wvmqpsidiq lnrrqstakk vllsyytqys qtistkdtrq argrswvmie
      481 psgavqrdqt vleggpcqls cnvkasesps ifwvlpdgsi lkapmddpds kfsilssgwl
      541 riksmepsds glyqciaqvr demdrmvyrv lvqspstqpa ekdtvtigkn pgesvtlpcn
      601 alaipeahls wilpnrriin dlantshvym lpngtlsipk vqvsdsgyyr cvavnqqgad
      661 hftvgitvtk kgsglpskrg rrpgakalsr vredivedeg gsgmgdeent srrllhpkdq
      721 evflktkdda ingdkkakkg rrklklwkhs ekepetnvae grrvfesrrr inmankqinp
      781 erwadilakv rgknlpkgte vpplikttsp pslslevtpp fpaisppsas pvqtvtsaee
      841 ssadvpllge eehvlgtiss asmglehnhn gvilvepevt stpleevvdd lsekteeits
      901 tegdlkgtaa ptlisepyep sptlhtldtv yekptheeta tegwsaadvg sspeptssey
      961 eppldavsla esepmqyfdp dletksqpde dkmkedtfah ltptptiwvn dsstsqlfed
     1021 stigepgvpg qshlqgltdn ihlvksslst qdtllikkgm kemsqtlqgg nmlegdpths
     1081 rssesegqes ksitlpdstl gimssmspvk kpaettvgtl ldkdtttatt tprqkvapss
     1141 tmsthpsrrr pngrrrlrpn kfrhrhkqtp pttfapsetf stqptqapdi kissqvessl
     1201 vptawvdntv ntpkqlemek naeptskgtp rrkhgkrpnk hrytpstvss rasgskpsps
     1261 penkhrnivt pssetillpr tvslktegpy dsldymtttr kiyssypkvq etlpvtykpt
     1321 sdgkeikddv atnvdkhksd ilvtgesitn aiptsrslvs tmgefkeess pvgfpgtptw
     1381 npsrtaqpgr lqtgipvtts genltdppll keledvdfts eflssltvst pfhqeeagss
     1441 ttlssikvev assqaetttl dqdhlettva illsetrpqn htptaarmke passspstil
     1501 mslgqttttk palpsprisq asrdskenvf lnyvgnpete atpvnnegtq hmsgpnelst
     1561 pssdqdafnl stklelekqv fgsrslprgp dsqrqdgrvh ashqltrvpa kpilptatvr
     1621 lpemstqsas ryfvtsqspr hwtnkpeitt ypsgalpenk qfttprlsst tiplplhmsk
     1681 psipskftdr rtdqfngysk vfgnnnipea rnpvgkppsp riphysngrl pfftnktlsf
     1741 pqlgvtrrpq iptspapvmr erkvipgsyn rihshstfhl dfgppappll htpqttgsps
     1801 tnlqnipmvs stqssisfit ssvqssgsfh qssskffagg ppaskfwslg ekpqiltksp
     1861 qtvsvtaetd tvfpceatgk pkpfvtwtkv stgalmtpnt riqrfevlkn gtlvirkvqv
     1921 qdrgqymcta snlhgldrmv vllsvtvqqp qilashyqdv tvylgdtiam eclakgtpap
     1981 qiswifpdrr vwqtvspveg ritlhenrtl sikeasfsdr gvykcvasna agadslairl
     2041 hvaalppvih qeklenislp pglsihihct akaaplpsvr wvlgdgtqir psqflhgnlf
     2101 vfpngtlyir nlapkdsgry ecvaanlvgs arrtvqlnvq raaanaritg tsprrtdvry
     2161 ggtlkldcsa sgdpwprilw rlpskrmida lfsfdsrikv fangtlvvks vtdkdagdyl
     2221 cvarnkvgdd yvvlkvdvvm kpakiehkee ndhkvfyggd lkvdcvatgl pnpeiswslp
     2281 dgslvnsfmq sddsggrtkr yvvfnngtly fnevgmreeg dytcfaenqv gkdemrvrvk
     2341 vvtapatirn ktylavqvpy gdvvtvacea kgepmpkvtw lsptnkvipt ssekyqiyqd
     2401 gtlliqkaqr sdsgnytclv rnsagedrkt vwihvnvqpp kingnpnpit tvreiaaggs
     2461 rklidckaeg iptprvlwaf pegvvlpapy ygnritvhgn gsldirslrk sdsvqlvcma
     2521 rneggearli lqltvlepme kpifhdpise kitamaghti slncsaagtp tpslvwvlpn
     2581 gtdlqsgqql qrfyhkadgm lhisglssvd agayrcvarn aaghterlvs lkvglkpean
     2641 kqyhnlvsii ngetlklpct ppgagqgrfs wtlpngmhle gpqtlgrvsl ldngtltvre
     2701 asvfdrgtyv crmeteygps vtsipvivia yppritsept pviytrpgnt vklncmamgi
     2761 pkaditwelp dkshlkagvq arlygnrflh pqgsltiqha tqrdagfykc maknilgsds
     2821 kttyihvf
//
LOCUS       NP_066956                741 aa            linear   PRI 27-APR-2025
DEFINITION  2-5A-dependent ribonuclease [Homo sapiens].
ACCESSION   NP_066956
VERSION     NP_066956.1
DBSOURCE    REFSEQ: accession NM_021133.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Kadanga,E., Zoure,A.A., Zohoncon,T.M., Traore,L., Ky,B.D.,
            Yonli,A.T., Traore,D.D.A., Bazie,B.V.J.T.E., Sombie,H.K.,
            Sorgho,P.A., Tovo,S.F.A., Traore,K., Ouedraogo,T.C., Djigma,F.W.
            and Simpore,J.
  TITLE     Carriage of mutations R462Q (rs 486907) and D541E (rs 627928) of
            the RNASEL gene and risk factors in patients with prostate cancer
            in Burkina Faso
  JOURNAL   BMC Med Genomics 15 (1), 123 (2022)
   PUBMED   35655265
  REMARK    GeneRIF: Carriage of mutations R462Q (rs 486907) and D541E (rs
            627928) of the RNASEL gene and risk factors in patients with
            prostate cancer in Burkina Faso.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Boehmer,D.F.R., Formisano,S., de Oliveira Mann,C.C., Mueller,S.A.,
            Kluge,M., Metzger,P., Rohlfs,M., Horth,C., Kocheise,L.,
            Lichtenthaler,S.F., Hopfner,K.P., Endres,S., Rothenfusser,S.,
            Friedel,C.C., Duewell,P., Schnurr,M. and Koenig,L.M.
  TITLE     OAS1/RNase L executes RIG-I ligand-dependent tumor cell apoptosis
  JOURNAL   Sci Immunol 6 (61) (2021)
   PUBMED   34272227
  REMARK    GeneRIF: OAS1/RNase L executes RIG-I ligand-dependent tumor cell
            apoptosis.
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Whelan,J.N., Parenti,N.A., Hatterschide,J., Renner,D.M., Li,Y.,
            Reyes,H.M., Dong,B., Perez,E.R., Silverman,R.H. and Weiss,S.R.
  TITLE     Zika virus employs the host antiviral RNase L protein to support
            replication factory assembly
  JOURNAL   Proc Natl Acad Sci U S A 118 (22) (2021)
   PUBMED   34031250
  REMARK    GeneRIF: Zika virus employs the host antiviral RNase L protein to
            support replication factory assembly.
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Li,Y., Renner,D.M., Comar,C.E., Whelan,J.N., Reyes,H.M.,
            Cardenas-Diaz,F.L., Truitt,R., Tan,L.H., Dong,B.,
            Alysandratos,K.D., Huang,J., Palmer,J.N., Adappa,N.D.,
            Kohanski,M.A., Kotton,D.N., Silverman,R.H., Yang,W., Morrisey,E.E.,
            Cohen,N.A. and Weiss,S.R.
  TITLE     SARS-CoV-2 induces double-stranded RNA-mediated innate immune
            responses in respiratory epithelial-derived cells and
            cardiomyocytes
  JOURNAL   Proc Natl Acad Sci U S A 118 (16) (2021)
   PUBMED   33811184
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2023 Jul 18;120(29):e2310153120.
            doi: 10.1073/pnas.2310153120. PMID: 37428938]
REFERENCE   5  (residues 1 to 741)
  AUTHORS   Ramnani,B., Manivannan,P., Jaggernauth,S. and Malathi,K.
  TITLE     ABCE1 Regulates RNase L-Induced Autophagy during Viral Infections
  JOURNAL   Viruses 13 (2), 315 (2021)
   PUBMED   33670646
  REMARK    GeneRIF: ABCE1 Regulates RNase L-Induced Autophagy during Viral
            Infections.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 741)
  AUTHORS   Bisbal,C., Martinand,C., Silhol,M., Lebleu,B. and Salehzada,T.
  TITLE     Cloning and characterization of a RNAse L inhibitor. A new
            component of the interferon-regulated 2-5A pathway
  JOURNAL   J Biol Chem 270 (22), 13308-13317 (1995)
   PUBMED   7539425
REFERENCE   7  (residues 1 to 741)
  AUTHORS   Dong,B., Xu,L., Zhou,A., Hassel,B.A., Lee,X., Torrence,P.F. and
            Silverman,R.H.
  TITLE     Intrinsic molecular activities of the interferon-induced
            2-5A-dependent RNase
  JOURNAL   J Biol Chem 269 (19), 14153-14158 (1994)
   PUBMED   7514601
REFERENCE   8  (residues 1 to 741)
  AUTHORS   Squire,J., Zhou,A., Hassel,B.A., Nie,H. and Silverman,R.H.
  TITLE     Localization of the interferon-induced, 2-5A-dependent RNase gene
            (RNS4) to human chromosome 1q25
  JOURNAL   Genomics 19 (1), 174-175 (1994)
   PUBMED   7514564
REFERENCE   9  (residues 1 to 741)
  AUTHORS   Zhou,A., Hassel,B.A. and Silverman,R.H.
  TITLE     Expression cloning of 2-5A-dependent RNAase: a uniquely regulated
            mediator of interferon action
  JOURNAL   Cell 72 (5), 753-765 (1993)
   PUBMED   7680958
REFERENCE   10 (residues 1 to 741)
  AUTHORS   Carter,B.S., Beaty,T.H., Steinberg,G.D., Childs,B. and Walsh,P.C.
  TITLE     Mendelian inheritance of familial prostate cancer
  JOURNAL   Proc Natl Acad Sci U S A 89 (8), 3367-3371 (1992)
   PUBMED   1565627
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138776.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a component of the interferon-regulated
            2-5A system that functions in the antiviral and antiproliferative
            roles of interferons. The protein is involved in innate immunity
            and is active against multiple RNA viruses, including the influenza
            and SARS-CoV-2 viruses. Mutations in this gene have been associated
            with predisposition to prostate cancer and this gene is a candidate
            for the hereditary prostate cancer 1 (HPC1) allele. [provided by
            RefSeq, Nov 2021].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.2432.1,
                                           SRR11853565.2404.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000367559.7/ ENSP00000356530.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.3"
     Protein         1..741
                     /product="2-5A-dependent ribonuclease"
                     /EC_number="3.1.26.-"
                     /EC_number="3.1.27.-"
                     /note="interferon-induced 2-5A-dependent RNase;
                     2',5'-oligoisoadenylate synthetase-dependent; ribonuclease
                     4; RNase L"
                     /calculated_mol_wt=83402
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          24..56
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          24..53
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          25..297
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          58..87
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          59..89
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(60,64..65,68..70,72..73,77,80,89,91,93,97..98,
                     101..103,105..106,110,113,122,124,126,130..131,134..136,
                     138..139,143,146)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          91..122
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          91..120
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          124..154
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          124..153
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          167..199
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          167..197
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          201..236
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          201..234
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          229..242
                     /region_name="2-5A binding (P-loop) 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          238..268
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          253..275
                     /region_name="2-5A binding (P-loop) 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          272..326
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          272..301
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          303..329
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     Region          375..587
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          590..708
                     /region_name="RNase_RNase-L"
                     /note="RNase domain (also known as the kinase extension
                     nuclease domain) of RNase L; cd10423"
                     /db_xref="CDD:199218"
     Site            order(590..591,594,598,670)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:199218"
     Site            order(592,693,697,700..701,705)
                     /site_type="other"
                     /note="putative kinase interface [polypeptide binding]"
                     /db_xref="CDD:199218"
     Site            order(594,598,601..602,667,670..671)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:199218"
     Site            684
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q05823.2)"
     Region          715..741
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05823.2)"
     CDS             1..741
                     /gene="RNASEL"
                     /gene_synonym="PRCA1; RNS4"
                     /coded_by="NM_021133.4:255..2480"
                     /db_xref="CCDS:CCDS1347.1"
                     /db_xref="GeneID:6041"
                     /db_xref="HGNC:HGNC:10050"
                     /db_xref="MIM:180435"
ORIGIN      
        1 mesrdhnnpq egptsssgrr aavednhlli kavqnedvdl vqqlleggan vnfqeeeggw
       61 tplhnavqms redivelllr hgadpvlrkk ngatpfilaa iagsvkllkl flskgadvne
      121 cdfygftafm eaavygkvka lkflykrgan vnlrrktked qerlrkggat almdaaekgh
      181 vevlkillde mgadvnacdn mgrnalihal lssddsdvea ithllldhga dvnvrgergk
      241 tplilavekk hlglvqrlle qehieindtd sdgktallla velklkkiae llckrgastd
      301 cgdlvmtarr nydhslvkvl lshgakedfh ppaedwkpqs shwgaalkdl hriyrpmigk
      361 lkffidekyk iadtseggiy lgfyekqeva vktfcegspr aqrevsclqs srenshlvtf
      421 ygseshrghl fvcvtlceqt leacldvhrg edveneedef arnvlssifk avqelhlscg
      481 ythqdlqpqn ilidskkaah ladfdksikw agdpqevkrd ledlgrlvly vvkkgsisfe
      541 dlkaqsneev vqlspdeetk dlihrlfhpg ehvrdclsdl lghpffwtwe sryrtlrnvg
      601 nesdiktrks eseilrllqp gpsehsksfd kwttkinecv mkkmnkfyek rgnfyqntvg
      661 dllkfirnlg ehideekhkk mklkigdpsl yfqktfpdlv iyvytklqnt eyrkhfpqth
      721 spnkpqcdga ggasglaspg c
//
LOCUS       NP_064584                265 aa            linear   PRI 27-APR-2025
DEFINITION  keratinocyte-associated transmembrane protein 2 precursor [Homo
            sapiens].
ACCESSION   NP_064584
VERSION     NP_064584.1
DBSOURCE    REFSEQ: accession NM_020199.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Ding,Y., Chu,L., Cao,Q., Lei,H., Li,X. and Zhuang,Q.
  TITLE     A meta-validated immune infiltration-related gene model predicts
            prognosis and immunotherapy sensitivity in HNSCC
  JOURNAL   BMC Cancer 23 (1), 45 (2023)
   PUBMED   36639648
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Xie,T., Deng,L., Mei,P., Zhou,Y., Wang,B., Zhang,J., Lin,J.,
            Wei,Y., Zhang,X. and Xu,R.
  TITLE     Genome-wide association study combining pathway analysis for
            typical sporadic amyotrophic lateral sclerosis in Chinese Han
            populations
  JOURNAL   Neurobiol Aging 35 (7), 1778 (2014)
   PUBMED   24529757
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Anney,R.J., Lasky-Su,J., O'Dushlaine,C., Kenny,E., Neale,B.M.,
            Mulligan,A., Franke,B., Zhou,K., Chen,W., Christiansen,H.,
            Arias-Vasquez,A., Banaschewski,T., Buitelaar,J., Ebstein,R.,
            Miranda,A., Mulas,F., Oades,R.D., Roeyers,H., Rothenberger,A.,
            Sergeant,J., Sonuga-Barke,E., Steinhausen,H., Asherson,P.,
            Faraone,S.V. and Gill,M.
  TITLE     Conduct disorder and ADHD: evaluation of conduct problems as a
            categorical and quantitative trait in the international multicentre
            ADHD genetics study
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 147B (8), 1369-1378 (2008)
   PUBMED   18951430
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Bonkobara,M., Das,A., Takao,J., Cruz,P.D. and Ariizumi,K.
  TITLE     Identification of novel genes for secreted and membrane-anchored
            proteins in human keratinocytes
  JOURNAL   Br J Dermatol 148 (4), 654-664 (2003)
   PUBMED   12752121
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP245947.1, BC020875.1 and BM681428.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF226055.1, BC020875.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1970526,
                                           SAMEA2149876 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000231512.5/ ENSP00000231512.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..265
                     /product="keratinocyte-associated transmembrane protein 2
                     precursor"
                     /note="keratinocytes associated transmembrane protein 2;
                     keratinocyte-associated transmembrane protein 2"
                     /calculated_mol_wt=24375
     sig_peptide     1..49
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NC54.2)"
                     /calculated_mol_wt=4878
     mat_peptide     50..265
                     /product="Keratinocyte-associated transmembrane protein 2.
                     /id=PRO_0000019579"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC54.2)"
                     /calculated_mol_wt=24375
     Region          73..123
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC54.2)"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NC54.2)"
     Region          79..265
                     /region_name="KCT2"
                     /note="Keratinocyte-associated gene product; pfam17818"
                     /db_xref="CDD:407686"
     Region          135..168
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC54.2)"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC54.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NC54.2)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NC54.2)"
     CDS             1..265
                     /gene="C5orf15"
                     /gene_synonym="HTGN29; KCT2"
                     /coded_by="NM_020199.3:42..839"
                     /db_xref="CCDS:CCDS4167.1"
                     /db_xref="GeneID:56951"
                     /db_xref="HGNC:HGNC:20656"
ORIGIN      
        1 maaavpkrmr gpaqakllpg saiqalvgla rplvlalllv saalssvvsr tdspsptvln
       61 shistpnvna lthenqtkps isqisttlpp ttstkksgga svvphpsptp lsqeeadnne
      121 dpsieeedll mlnsspstak dtldngdyge pdydwttgpr dddesddtle enrgymeieq
      181 svksfkmpss nieeedshff fhliifafci avvyityhnk rkifllvqsr kwrdglcskt
      241 veyhrldqnv neampslkit ndyif
//
LOCUS       NP_787033                555 aa            linear   PRI 27-APR-2025
DEFINITION  spermine oxidase isoform 1 [Homo sapiens].
ACCESSION   NP_787033
VERSION     NP_787033.1
DBSOURCE    REFSEQ: accession NM_175839.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Gobert,A.P., Latour,Y.L., Asim,M., Barry,D.P., Allaman,M.M.,
            Finley,J.L., Smith,T.M., McNamara,K.M., Singh,K., Sierra,J.C.,
            Delgado,A.G., Luis,P.B., Schneider,C., Washington,M.K.,
            Piazuelo,M.B., Zhao,S., Coburn,L.A. and Wilson,K.T.
  TITLE     Protective Role of Spermidine in Colitis and Colon Carcinogenesis
  JOURNAL   Gastroenterology 162 (3), 813-827 (2022)
   PUBMED   34767785
  REMARK    GeneRIF: Protective Role of Spermidine in Colitis and Colon
            Carcinogenesis.
            Erratum:[Gastroenterology. 2022 Jun;162(7):2138-2143. doi:
            10.1053/j.gastro.2022.04.006. PMID: 35461802]
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Fadista,J., Yakimov,V., Vosa,U., Hansen,C.S., Kasela,S., Skotte,L.,
            Geller,F., Courraud,J., Esko,T., Kukuskina,V., Buil,A., Melbye,M.,
            Werge,T.M., Hougaard,D.M., Milani,L., Bybjerg-Grauholm,J.,
            Cohen,A.S. and Feenstra,B.
  TITLE     Genetic regulation of spermine oxidase activity and cancer risk: a
            Mendelian randomization study
  JOURNAL   Sci Rep 11 (1), 17463 (2021)
   PUBMED   34465810
  REMARK    GeneRIF: Genetic regulation of spermine oxidase activity and cancer
            risk: a Mendelian randomization study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Leonetti,A., Cervoni,L., Polticelli,F., Kanamori,Y.,
            Yurtsever,Z.N., Agostinelli,E., Mariottini,P., Stano,P. and
            Cervelli,M.
  TITLE     Spectroscopic and calorimetric characterization of spermine oxidase
            and its association forms
  JOURNAL   Biochem J 474 (24), 4253-4268 (2017)
   PUBMED   29138259
  REMARK    GeneRIF: Data suggest that intermolecular disulfide bond links
            spermine oxidase (SMOX) molecules to form the homodimer and plays a
            critical role in the stabilization of the overall three-dimensional
            SMOX structure.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Uemura,T., Takasaka,T., Igarashi,K. and Ikegaya,H.
  TITLE     Spermine oxidase promotes bile canalicular lumen formation through
            acrolein production
  JOURNAL   Sci Rep 7 (1), 14841 (2017)
   PUBMED   29093526
  REMARK    GeneRIF: SMOX plays a central role in the formation of bile
            canalicular lumen in liver cells by activating Akt pathway through
            acrolein production.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Murray-Stewart,T., Sierra,J.C., Piazuelo,M.B., Mera,R.M.,
            Chaturvedi,R., Bravo,L.E., Correa,P., Schneider,B.G., Wilson,K.T.
            and Casero,R.A.
  TITLE     Epigenetic silencing of miR-124 prevents spermine oxidase
            regulation: implications for Helicobacter pylori-induced gastric
            cancer
  JOURNAL   Oncogene 35 (42), 5480-5488 (2016)
   PUBMED   27041578
  REMARK    GeneRIF: These results indicate a protective role for miR-124
            through the inhibition of SMOX-mediated DNA damage in the etiology
            of H. pylori-associated gastric cancer.
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Murray-Stewart,T., Wang,Y., Devereux,W. and Casero,R.A. Jr.
  TITLE     Cloning and characterization of multiple human polyamine oxidase
            splice variants that code for isoenzymes with different biochemical
            characteristics
  JOURNAL   Biochem J 368 (Pt 3), 673-677 (2002)
   PUBMED   12398765
  REMARK    GeneRIF: There are at least four isoenzymes of human PAO, each with
            different biochemical characteristics and roles in polyamine
            catabolism
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Vujcic,S., Diegelman,P., Bacchi,C.J., Kramer,D.L. and Porter,C.W.
  TITLE     Identification and characterization of a novel flavin-containing
            spermine oxidase of mammalian cell origin
  JOURNAL   Biochem J 367 (Pt 3), 665-675 (2002)
   PUBMED   12141946
REFERENCE   8  (residues 1 to 555)
  AUTHORS   Wang,Y., Devereux,W., Woster,P.M., Stewart,T.M., Hacker,A. and
            Casero,R.A. Jr.
  TITLE     Cloning and characterization of a human polyamine oxidase that is
            inducible by polyamine analogue exposure
  JOURNAL   Cancer Res 61 (14), 5370-5373 (2001)
   PUBMED   11454677
REFERENCE   9  (residues 1 to 555)
  AUTHORS   Tsukada,T., Furusako,S., Maekawa,S., Hibasami,H. and Nakashima,K.
  TITLE     Purification by affinity chromatography and characterization of
            porcine liver cytoplasmic polyamine oxidase
  JOURNAL   Int J Biochem 20 (7), 695-702 (1988)
   PUBMED   3181599
REFERENCE   10 (residues 1 to 555)
  AUTHORS   Holtta,E.
  TITLE     Oxidation of spermidine and spermine in rat liver: purification and
            properties of polyamine oxidase
  JOURNAL   Biochemistry 16 (1), 91-100 (1977)
   PUBMED   12798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG679874.1, EF032141.1,
            AY358104.1 and AW136764.1.
            
            Summary: Polyamines are ubiquitous polycationic alkylamines which
            include spermine, spermidine, putrescine, and agmatine. These
            molecules participate in a broad range of cellular functions which
            include cell cycle modulation, scavenging reactive oxygen species,
            and the control of gene expression. These molecules also play
            important roles in neurotransmission through their regulation of
            cell-surface receptor activity, involvement in intracellular
            signalling pathways, and their putative roles as neurotransmitters.
            This gene encodes an FAD-containing enzyme that catalyzes the
            oxidation of spermine to spermadine and secondarily produces
            hydrogen peroxide. Multiple transcript variants encoding different
            isoenzymes have been identified for this gene, some of which have
            failed to demonstrate significant oxidase activity on natural
            polyamine substrates. The characterized isoenzymes have distinctive
            biochemical characteristics and substrate specificities, suggesting
            the existence of additional levels of complexity in polyamine
            catabolism. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the most abundant
            transcript and encodes isoform (1), also known as PAOh1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.684032.1,
                                           SRR3476690.325510.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305958.9/ ENSP00000307252.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..555
                     /product="spermine oxidase isoform 1"
                     /EC_number="1.5.3.16"
                     /note="flavin-containing spermine oxidase; putative cyclin
                     G1 interacting protein; flavin containing amine oxidase;
                     polyamine oxidase 1"
                     /calculated_mol_wt=61688
     Region          50..548
                     /region_name="PLN02568"
                     /note="polyamine oxidase"
                     /db_xref="CDD:215308"
     Region          271..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWM0.1)"
     CDS             1..555
                     /gene="SMOX"
                     /gene_synonym="C20orf16; PAO; PAO-1; PAO1; PAOH; PAOH1;
                     SMO"
                     /coded_by="NM_175839.3:177..1844"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13075.1"
                     /db_xref="GeneID:54498"
                     /db_xref="HGNC:HGNC:15862"
                     /db_xref="MIM:615854"
ORIGIN      
        1 mqscessgds addplsrglr rrgqprvvvi gaglaglaaa kalleqgftd vtvleasshi
       61 ggrvqsvklg hatfelgatw ihgshgnpiy hlaeanglle ettdgersvg rislyskngv
      121 acyltnhgrr ipkdvveefs dlynevynlt qeffrhdkpv naesqnsvgv ftreevrnri
      181 rndpddpeat krlklamiqq ylkvescess shsmdevsls afgewteipg ahhiipsgfm
      241 rvvellaegi pahviqlgkp vrcihwdqas arprgpeiep rgegdhnhdt geggqggeep
      301 rggrwdedeq wsvvvecedc elipadhviv tvslgvlkrq ytsffrpglp tekvaaihrl
      361 gigttdkifl efeepfwgpe cnslqfvwed eaeshtltyp pelwyrkicg fdvlyppery
      421 ghvlsgwicg eealvmekcd deavaeicte mlrqftgnpn ipkprrilrs awgsnpyfrg
      481 sysytqvgss gadveklakp lpytesskta pmqvlfsgea thrkyystth gallsgqrea
      541 arliemyrdl fqqgt
//
LOCUS       NP_001660                593 aa            linear   PRI 27-APR-2025
DEFINITION  arylsulfatase D isoform alpha precursor [Homo sapiens].
ACCESSION   NP_001660
VERSION     NP_001660.2
DBSOURCE    REFSEQ: accession NM_001669.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Lin,Y., Li,C., Xiong,W., Fan,L., Pan,H. and Li,Y.
  TITLE     ARSD, a novel ERalpha downstream target gene, inhibits
            proliferation and migration of breast cancer cells via activating
            Hippo/YAP pathway
  JOURNAL   Cell Death Dis 12 (11), 1042 (2021)
   PUBMED   34725332
  REMARK    GeneRIF: ARSD, a novel ERalpha downstream target gene, inhibits
            proliferation and migration of breast cancer cells via activating
            Hippo/YAP pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Bahramian,S., T Shamsabadi,F., Fazel,A., Delshad,E., Amini,A.,
            Memari,F. and Shafiee,M.
  TITLE     Evaluation of Arylsulfatase D (ARSD) and long noncoding RNA
            ARSD-AS1 gene expression in breast cancer patients and their
            association with oncogenic transcription factors
  JOURNAL   J BUON 25 (4), 1805-1813 (2020)
   PUBMED   33099917
  REMARK    GeneRIF: Evaluation of Arylsulfatase D (ARSD) and long noncoding
            RNA ARSD-AS1 gene expression in breast cancer patients and their
            association with oncogenic transcription factors.
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Trojani,A., Di Camillo,B., Tedeschi,A., Lodola,M., Montesano,S.,
            Ricci,F., Vismara,E., Greco,A., Veronese,S., Orlacchio,A.,
            Martino,S., Colombo,C., Mura,M., Nichelatti,M., Colosimo,A.,
            Scarpati,B., Montillo,M. and Morra,E.
  TITLE     Gene expression profiling identifies ARSD as a new marker of
            disease progression and the sphingolipid metabolism as a potential
            novel metabolism in chronic lymphocytic leukemia
  JOURNAL   Cancer Biomark 11 (1), 15-28 (2011)
   PUBMED   22820137
  REMARK    GeneRIF: ARSD protein level and IGVH were independently associated
            with the need for therapy of chronic lymphocytic leukemia patients.
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Savarirayan,R., Boyle,R.J., Masel,J., Rogers,J.G. and
            Sheffield,L.J.
  TITLE     Longterm follow-up in chondrodysplasia punctata, tibia-metacarpal
            type, demonstrating natural history
  JOURNAL   Am J Med Genet A 124A (2), 148-157 (2004)
   PUBMED   14699613
  REMARK    Review article
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Urbitsch,P., Salzer,M.J., Hirschmann,P. and Vogt,P.H.
  TITLE     Arylsulfatase D gene in Xp22.3 encodes two protein isoforms
  JOURNAL   DNA Cell Biol 19 (12), 765-773 (2000)
   PUBMED   11177574
REFERENCE   6  (residues 1 to 593)
  AUTHORS   Dooley,T.P., Haldeman-Cahill,R., Joiner,J. and Wilborn,T.W.
  TITLE     Expression profiling of human sulfotransferase and sulfatase gene
            superfamilies in epithelial tissues and cultured cells
  JOURNAL   Biochem Biophys Res Commun 277 (1), 236-245 (2000)
   PUBMED   11027669
REFERENCE   7  (residues 1 to 593)
  AUTHORS   Puca,A.A., Zollo,M., Repetto,M., Andolfi,G., Guffanti,A., Simon,G.,
            Ballabio,A. and Franco,B.
  TITLE     Identification by shotgun sequencing, genomic organization, and
            functional analysis of a fourth arylsulfatase gene (ARSF) from the
            Xp22.3 region
  JOURNAL   Genomics 42 (2), 192-199 (1997)
   PUBMED   9192838
REFERENCE   8  (residues 1 to 593)
  AUTHORS   Glaser,B., Grutzner,F., Taylor,K., Schiebel,K., Meroni,G.,
            Tsioupra,K., Pasantes,J., Rietschel,W., Toder,R., Willmann,U.,
            Zeitler,S., Yen,P., Ballabio,A., Rappold,G. and Schempp,W.
  TITLE     Comparative mapping of Xp22 genes in hominoids--evolutionary linear
            instability of their Y homologues
  JOURNAL   Chromosome Res 5 (3), 167-176 (1997)
   PUBMED   9246409
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Meroni,G., Franco,B., Archidiacono,N., Messali,S., Andolfi,G.,
            Rocchi,M. and Ballabio,A.
  TITLE     Characterization of a cluster of sulfatase genes on Xp22.3 suggests
            gene duplications in an ancestral pseudoautosomal region
  JOURNAL   Hum Mol Genet 5 (4), 423-431 (1996)
   PUBMED   8845834
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Franco,B., Meroni,G., Parenti,G., Levilliers,J., Bernard,L.,
            Gebbia,M., Cox,L., Maroteaux,P., Sheffield,L., Rappold,G.A.,
            Andria,G., Petit,C. and Ballabio,A.
  TITLE     A cluster of sulfatase genes on Xp22.3: mutations in
            chondrodysplasia punctata (CDPX) and implications for warfarin
            embryopathy
  JOURNAL   Cell 81 (1), 15-25 (1995)
   PUBMED   7720070
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA869167.1, BC020229.1,
            AK314479.1, AC005295.1 and AI289224.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 5, 2005 this sequence version replaced NP_001660.1.
            
            Summary: The protein encoded by this gene is a member of the
            sulfatase family. Sulfatases are essential for the correct
            composition of bone and cartilage matrix. The encoded protein is
            postranslationally glycosylated and localized to the lysosome. This
            gene is located within a cluster of similar arylsulfatase genes on
            chromosome X. A related pseudogene has been identified in the
            pseudoautosomal region of chromosome Y. [provided by RefSeq, Jul
            2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (alpha).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314479.1, HM005546.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381154.6/ ENSP00000370546.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.33"
     Protein         1..593
                     /product="arylsulfatase D isoform alpha precursor"
                     /EC_number="3.1.6.1"
                     /note="testis tissue sperm-binding protein Li 39a"
                     /calculated_mol_wt=61281
     sig_peptide     1..33
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51689.2)"
                     /calculated_mol_wt=3597
     mat_peptide     34..593
                     /product="Arylsulfatase D. /id=PRO_0000033424"
                     /note="propagated from UniProtKB/Swiss-Prot (P51689.2)"
                     /calculated_mol_wt=61281
     Region          40..563
                     /region_name="ALP_like"
                     /note="alkaline phosphatases and sulfatases; cl23718"
                     /db_xref="CDD:474031"
     Site            order(49,89,304,356..357)
                     /site_type="active"
                     /db_xref="CDD:293732"
     Site            order(49,89,304,357)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293732"
     Site            61
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51689.2)"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51689.2)"
     Site            347
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P51689.2)"
     CDS             1..593
                     /gene="ARSD"
                     /gene_synonym="ASD"
                     /coded_by="NM_001669.4:65..1846"
                     /note="isoform alpha precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS35196.1"
                     /db_xref="GeneID:414"
                     /db_xref="HGNC:HGNC:717"
                     /db_xref="MIM:300002"
ORIGIN      
        1 mrsaarrgra apaardslpv llflclllkt cepktanafk pnillimadd lgtgdlgcyg
       61 nntlrtpnid qlaeegvrlt qhlaaaplct psraafltgr hsfrsgmdas ngyralqwna
      121 gsgglpenet tfarilqqhg yatgligkwh qgvncasrgd hchhplnhgf dyfygmpftl
      181 tndcdpgrpp evdaalraql wgytqflalg iltlaagqtc gffsvsarav tgmagvgclf
      241 fiswyssfgf vrrwncilmr nhdvteqpmv lektaslmlk eavsyierhk hgpfllflsl
      301 lhvhiplvtt saflgksqhg lygdnveemd wligkvlnai ednglknstf tyftsdhggh
      361 leardghsql ggwngiykgg kgmggweggi rvpgifhwpg vlpagrvige ptslmdvfpt
      421 vvqlvggevp qdrvidghsl vpllqgaear saheflfhyc gqhlhaarwh qkdsgsvwkv
      481 hyttpqfhpe gagacygrgv cpcsgegvth hrppllfdls rdpsearplt pdseplyhav
      541 iarvgaavse hrqtlspvpq qfsmsnilwk pwlqpccghf pfcschedgd gtp
//
LOCUS       NP_056449                621 aa            linear   PRI 27-APR-2025
DEFINITION  KIF-binding protein [Homo sapiens].
ACCESSION   NP_056449
VERSION     NP_056449.1
DBSOURCE    REFSEQ: accession NM_015634.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Ooi,J.C.E., Azman,A., Chan,M.Y., Toh,E.S.Y., Seo,G.H., Kim,J.H.,
            Yakob,Y. and Chia,Y.K.
  TITLE     Progressive ataxia, ophthalmoparesis, and hypogonadotropic
            hypogonadism in a family with a novel variant in the KIFBP gene
  JOURNAL   Clin Genet 105 (2), 228-230 (2024)
   PUBMED   37903629
  REMARK    GeneRIF: Progressive ataxia, ophthalmoparesis, and hypogonadotropic
            hypogonadism in a family with a novel variant in the KIFBP gene.
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Atherton,J., Hummel,J.J., Olieric,N., Locke,J., Pena,A.,
            Rosenfeld,S.S., Steinmetz,M.O., Hoogenraad,C.C. and Moores,C.A.
  TITLE     The mechanism of kinesin inhibition by kinesin-binding protein
  JOURNAL   Elife 9, e61481 (2020)
   PUBMED   33252036
  REMARK    GeneRIF: The mechanism of kinesin inhibition by kinesin-binding
            protein.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 621)
  AUTHORS   MacKenzie,K.C., de Graaf,B.M., Syrimis,A., Zhao,Y., Brosens,E.,
            Mancini,G.M.S., Schot,R., Halley,D., Wilke,M., Vollo,A.,
            Flinter,F., Green,A., Mansour,S., Pilch,J., Stark,Z.,
            Zamba-Papanicolaou,E., Christophidou-Anastasiadou,V.,
            Hofstra,R.M.W., Jongbloed,J.D.H., Nicolaou,N., Tanteles,G.A.,
            Brooks,A.S. and Alves,M.M.
  TITLE     Goldberg-Shprintzen syndrome is determined by the absence, or
            reduced expression levels, of KIFBP
  JOURNAL   Hum Mutat 41 (11), 1906-1917 (2020)
   PUBMED   32939943
  REMARK    GeneRIF: Goldberg-Shprintzen syndrome is determined by the absence,
            or reduced expression levels, of KIFBP.
REFERENCE   5  (residues 1 to 621)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 621)
  AUTHORS   Drevillon,L., Megarbane,A., Demeer,B., Matar,C., Benit,P.,
            Briand-Suleau,A., Bodereau,V., Ghoumid,J., Nasser,M., Decrouy,X.,
            Doco-Fenzy,M., Rustin,P., Gaillard,D., Goossens,M. and Giurgea,I.
  TITLE     KBP-cytoskeleton interactions underlie developmental anomalies in
            Goldberg-Shprintzen syndrome
  JOURNAL   Hum Mol Genet 22 (12), 2387-2399 (2013)
   PUBMED   23427148
  REMARK    GeneRIF: KBP-cytoskeleton interactions is involved in neuronal
            development in Goldberg-Shprintzen syndrome.
REFERENCE   7  (residues 1 to 621)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 621)
  AUTHORS   Wozniak,M.J., Melzer,M., Dorner,C., Haring,H.U. and Lammers,R.
  TITLE     The novel protein KBP regulates mitochondria localization by
            interaction with a kinesin-like protein
  JOURNAL   BMC Cell Biol 6, 35 (2005)
   PUBMED   16225668
  REMARK    GeneRIF: KBP is a new binding partner for KIF1Balpha that is a
            regulator of its transport function and thus represents a new type
            of kinesin interacting protein.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 621)
  AUTHORS   Brooks,A.S., Bertoli-Avella,A.M., Burzynski,G.M., Breedveld,G.J.,
            Osinga,J., Boven,L.G., Hurst,J.A., Mancini,G.M., Lequin,M.H., de
            Coo,R.F., Matera,I., de Graaff,E., Meijers,C., Willems,P.J.,
            Tibboel,D., Oostra,B.A. and Hofstra,R.M.
  TITLE     Homozygous nonsense mutations in KIAA1279 are associated with
            malformations of the central and enteric nervous systems
  JOURNAL   Am J Hum Genet 77 (1), 120-126 (2005)
   PUBMED   15883926
REFERENCE   10 (residues 1 to 621)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA292451.1, BC006427.1 and
            AL050190.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a kinesin family member 1 binding
            protein that is characterized by two tetratrico peptide repeats.
            The encoded protein localizes to the mitochondria and may be
            involved in regulating transport of the mitochondria. Mutations in
            this gene are associated with Goldberg-Shprintzen megacolon
            syndrome. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.677431.1,
                                           SRR3476690.378913.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000361983.7/
                                                  ENSP00000354848.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..621
                     /product="KIF-binding protein"
                     /note="kinesin binding protein; mutant KIF1 binding
                     protein"
                     /calculated_mol_wt=71683
     Region          51..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EK5.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96EK5.1)"
     Region          247..614
                     /region_name="KBP_C"
                     /note="KIF-1 binding protein C terminal; pfam12309"
                     /db_xref="CDD:463528"
     CDS             1..621
                     /gene="KIFBP"
                     /gene_synonym="KBP; KIAA1279; KIF1BP; TTC20"
                     /coded_by="NM_015634.4:31..1896"
                     /db_xref="CCDS:CCDS7284.1"
                     /db_xref="GeneID:26128"
                     /db_xref="HGNC:HGNC:23419"
                     /db_xref="MIM:609367"
ORIGIN      
        1 manvpwaevc ekfqaalals rvelhknpek epykskysar alleevkall gpapededer
       61 peaedgpgag dhalglpaev vepegpvaqr avrlaviefh lgvnhidtee lsageehlvk
      121 clrllrryrl shdcislciq aqnnlgilws ereeietaqa ylessealyn qymkevgspp
      181 ldpterflpe eeklteqers krfekvythn lyylaqvyqh lemfekaahy chstlkrqle
      241 hnayhpiewa inaatlsqfy inklcfmear hclsaanvif gqtgkisate dtpeaegevp
      301 elyhqrkgei arcwikyclt lmqnaqlsmq dnigeldldk qselralrkk eldeeesirk
      361 kavqfgtgel cdaisaveek vsylrpldfe earelfllgq hyvfeakeff qidgyvtdhi
      421 evvqdhsalf kvlaffetdm errckmhkrr iamlepltvd lnpqyyllvn rqiqfeiaha
      481 yydmmdlkva iadrlrdpds hivkkinnln ksalkyyqlf ldslrdpnkv fpehigedvl
      541 rpamlakfrv arlygkiita dpkkelenla tslehykfiv dycekhpeaa qeievelels
      601 kemvsllptk merfrtkmal t
//
LOCUS       NP_872434                611 aa            linear   PRI 27-APR-2025
DEFINITION  cilia- and flagella-associated protein 100 [Homo sapiens].
ACCESSION   NP_872434
VERSION     NP_872434.2
DBSOURCE    REFSEQ: accession NM_182628.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Sigg,M.A., Menchen,T., Lee,C., Johnson,J., Jungnickel,M.K.,
            Choksi,S.P., Garcia,G. 3rd, Busengdal,H., Dougherty,G.W.,
            Pennekamp,P., Werner,C., Rentzsch,F., Florman,H.M., Krogan,N.,
            Wallingford,J.B., Omran,H. and Reiter,J.F.
  TITLE     Evolutionary Proteomics Uncovers Ancient Associations of Cilia with
            Signaling Pathways
  JOURNAL   Dev Cell 43 (6), 744-762 (2017)
   PUBMED   29257953
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Yamamoto,R., Song,K., Yanagisawa,H.A., Fox,L., Yagi,T.,
            Wirschell,M., Hirono,M., Kamiya,R., Nicastro,D. and Sale,W.S.
  TITLE     The MIA complex is a conserved and novel dynein regulator essential
            for normal ciliary motility
  JOURNAL   J Cell Biol 201 (2), 263-278 (2013)
   PUBMED   23569216
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Kwon,Y.J., Lee,S.J., Koh,J.S., Kim,S.H., Lee,H.W., Kang,M.C.,
            Bae,J.B., Kim,Y.J. and Park,J.H.
  TITLE     Genome-wide analysis of DNA methylation and the gene expression
            change in lung cancer
  JOURNAL   J Thorac Oncol 7 (1), 20-33 (2012)
   PUBMED   22011669
  REMARK    GeneRIF: We confirmed that the expression of CCDC37 in squamous
            cell carcinoma is regulated by DNA methylation of its specific
            promoter region.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC063919.15, AK097402.1, BC101367.2 and AC073439.26.
            
            On Dec 11, 2008 this sequence version replaced NP_872434.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK097402.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000352312.6/ ENSP00000344749.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.3"
     Protein         1..611
                     /product="cilia- and flagella-associated protein 100"
                     /note="coiled-coil domain-containing protein 37;
                     coiled-coil domain containing 37"
                     /calculated_mol_wt=70986
     Region          1..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q494V2.1)"
     Region          151..269
                     /region_name="DUF4200"
                     /note="Domain of unknown function (DUF4200); pfam13863"
                     /db_xref="CDD:464003"
     Region          287..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q494V2.1)"
     Region          338..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q494V2.1)"
     CDS             1..611
                     /gene="CFAP100"
                     /gene_synonym="CCDC37; MIA1"
                     /coded_by="NM_182628.3:130..1965"
                     /db_xref="CCDS:CCDS3037.1"
                     /db_xref="GeneID:348807"
                     /db_xref="HGNC:HGNC:26842"
ORIGIN      
        1 mseipstivs knmtndknsl esmnisssss teenpkkqar kneehgpdps anpfhlsgdv
       61 dffllrdqer nkalserqqq ktmrvhqkmt ysskvsakht slrrqlqled kqedlearae
      121 aehqrafrdy ttwkltltke knvepenmsg yikqkrqmfl lqyaldvkrr eiqrletlat
      181 keearlerae kslekdaalf defvrendcs svqamraaek etkakiekil eirdlttqiv
      241 nikseisrfe dtlkhykvyk dflyklspke wleeqekkhs flkkakevse askessvnst
      301 pgdkgpgikg kassmwakeg qgtkkpwrfl qtmrlgrsps ylsspqqgsq psessggdsr
      361 gsnspipptq edtdsdgeep qlyftepqql ldvfreleeq nlsliqnsqe tektleelsh
      421 tlkhtqirmd revnqlkqwv ttmmmsitke edtaaelelk arvfhfgeyk gdqqdklles
      481 lnckvldvyr hctgtqqean lgtvqmltii ehqldellen lehvpqvkie qaerakeker
      541 rirlreeklq mqkilqeehl qrararaqae ikkkrgrtlv crsrppahri kqqsehtlmd
      601 keeeellfff t
//
LOCUS       NP_001091058             169 aa            linear   PRI 27-APR-2025
DEFINITION  small proline-rich protein 3 [Homo sapiens].
ACCESSION   NP_001091058
VERSION     NP_001091058.1
DBSOURCE    REFSEQ: accession NM_001097589.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Liao,S., Zhao,W., Yin,S., Xu,J., Yang,L., Yang,Y., Yan,H., Ou,T.
            and Zeng,X.
  TITLE     Predictive role and molecular biological function of proline-rich
            small repeat protein SPRR3 in the diagnosis of lung adenocarcinoma
  JOURNAL   Int J Biol Macromol 278 (Pt 1), 134674 (2024)
   PUBMED   39134193
  REMARK    GeneRIF: Predictive role and molecular biological function of
            proline-rich small repeat protein SPRR3 in the diagnosis of lung
            adenocarcinoma.
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Xie,Y., Li,H., Zhong,B., Zhu,X., Ye,R., Xie,B. and Zhang,J.
  TITLE     SPRR3 Contributes to Aggressiveness of Pancreatic Cancer Cells via
            NF-kappaB Signaling Pathway
  JOURNAL   Biomed Res Int 2023, 7518744 (2023)
   PUBMED   36685674
  REMARK    GeneRIF: SPRR3 Contributes to Aggressiveness of Pancreatic Cancer
            Cells via NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Zhu,G., Cai,H., Ye,L., Mo,Y., Zhu,M., Zeng,Y., Song,X., Yang,C.,
            Gao,X., Wang,J. and Jin,M.
  TITLE     Small Proline-Rich Protein 3 Regulates IL-33/ILC2 Axis to Promote
            Allergic Airway Inflammation
  JOURNAL   Front Immunol 12, 758829 (2022)
   PUBMED   35126350
  REMARK    GeneRIF: Small Proline-Rich Protein 3 Regulates IL-33/ILC2 Axis to
            Promote Allergic Airway Inflammation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Bae,J.E., Choi,H., Shin,D.W., Na,H.W., Park,N.Y., Kim,J.B.,
            Jo,D.S., Cho,M.J., Lyu,J.H., Chang,J.H., Lee,E.H., Lee,T.R.,
            Kim,H.J. and Cho,D.H.
  TITLE     Fine particulate matter (PM2.5) inhibits ciliogenesis by increasing
            SPRR3 expression via c-Jun activation in RPE cells and skin
            keratinocytes
  JOURNAL   Sci Rep 9 (1), 3994 (2019)
   PUBMED   30850686
  REMARK    GeneRIF: Fine particulate matter (PM2.5) inhibits ciliogenesis by
            increasing SPRR3 expression via c-Jun activation in RPE cells and
            skin keratinocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 169)
  AUTHORS   Steinert,P.M. and Marekov,L.N.
  TITLE     Direct evidence that involucrin is a major early isopeptide
            cross-linked component of the keratinocyte cornified cell envelope
  JOURNAL   J Biol Chem 272 (3), 2021-2030 (1997)
   PUBMED   8999895
REFERENCE   7  (residues 1 to 169)
  AUTHORS   Abraham,J.M., Wang,S., Suzuki,H., Jiang,H.Y., Rosenblum-Vos,L.S.,
            Yin,J. and Meltzer,S.J.
  TITLE     Esophagin cDNA cloning and characterization: a tissue-specific
            member of the small proline-rich protein family that is not
            expressed in esophageal tumors
  JOURNAL   Cell Growth Differ 7 (7), 855-860 (1996)
   PUBMED   8809402
REFERENCE   8  (residues 1 to 169)
  AUTHORS   Greco,M.A., Lorand,L., Lane,W.S., Baden,H.P., Parameswaran,K.N. and
            Kvedar,J.C.
  TITLE     The pancornulins: a group of small proline rich-related cornified
            envelope precursors with bifunctional capabilities in isopeptide
            bond formation
  JOURNAL   J Invest Dermatol 104 (2), 204-210 (1995)
   PUBMED   7829876
REFERENCE   9  (residues 1 to 169)
  AUTHORS   Robinson,P.A., Marley,J.J., High,A.S. and Hume,W.J.
  TITLE     Differential expression of protease inhibitor and small
            proline-rich protein genes between normal human oral tissue and
            odontogenic keratocysts
  JOURNAL   Arch Oral Biol 39 (3), 251-259 (1994)
   PUBMED   8018055
REFERENCE   10 (residues 1 to 169)
  AUTHORS   Gibbs,S., Fijneman,R., Wiegant,J., van Kessel,A.G., van De Putte,P.
            and Backendorf,C.
  TITLE     Molecular characterization and evolution of the SPRR family of
            keratinocyte differentiation markers encoding small proline-rich
            proteins
  JOURNAL   Genomics 16 (3), 630-637 (1993)
   PUBMED   8325635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA763011.1, AL356867.23 and BM955458.1.
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' UTR, compared to variant 1. Both variants 1 and 2 encode the
            same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017802.1, AY118269.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295367.5/ ENSP00000295367.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..169
                     /product="small proline-rich protein 3"
                     /note="esophagin; cornifin beta; 22 kDa pancornulin"
                     /calculated_mol_wt=18023
     Region          1..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBC9.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:20599699; propagated from
                     UniProtKB/Swiss-Prot (Q9UBC9.2)"
     Region          38..167
                     /region_name="Cornifin"
                     /note="Cornifin (SPRR) family; pfam02389"
                     /db_xref="CDD:280537"
     Region          43..154
                     /region_name="14 X 8 AA approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBC9.2)"
     Region          150..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBC9.2)"
     CDS             1..169
                     /gene="SPRR3"
                     /coded_by="NM_001097589.2:65..574"
                     /db_xref="CCDS:CCDS1033.1"
                     /db_xref="GeneID:6707"
                     /db_xref="HGNC:HGNC:11268"
                     /db_xref="MIM:182271"
ORIGIN      
        1 mssyqqkqtf tpppqlqqqq vkqpsqpppq eifvpttkep chskvpqpgn tkipepgctk
       61 vpepgctkvp epgctkvpep gctkvpepgc tkvpepgctk vpepgytkvp epgsikvpdq
      121 gfikfpepga ikvpeqgytk vpvpgytklp epcpstvtpg paqqktkqk
//
LOCUS       NP_003136                183 aa            linear   PRI 27-APR-2025
DEFINITION  translocon-associated protein subunit beta precursor [Homo
            sapiens].
ACCESSION   NP_003136 XP_946862 XP_950520 XP_950521 XP_950523
VERSION     NP_003136.1
DBSOURCE    REFSEQ: accession NM_003145.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Kriegler,T., Kiburg,G. and Hessa,T.
  TITLE     Translocon-Associated Protein Complex (TRAP) is Crucial for
            Co-Translational Translocation of Pre-Proinsulin
  JOURNAL   J Mol Biol 432 (24), 166694 (2020)
   PUBMED   33137310
  REMARK    GeneRIF: Translocon-Associated Protein Complex (TRAP) is Crucial
            for Co-Translational Translocation of Pre-Proinsulin.
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Garg,B., Pathria,G., Wagner,C., Maurer,M. and Wagner,S.N.
  TITLE     Signal Sequence Receptor 2 is required for survival of human
            melanoma cells as part of an unfolded protein response to
            endoplasmic reticulum stress
  JOURNAL   Mutagenesis 31 (5), 573-582 (2016)
   PUBMED   27180333
  REMARK    GeneRIF: The Unfolded Protein Response (UPR) to ER stress was shown
            as an inducer of SSR2 via transcriptional regulation through X-Box
            Binding Protein 1s (XBP1s).
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Ishikawa,H. and Barber,G.N.
  TITLE     STING is an endoplasmic reticulum adaptor that facilitates innate
            immune signalling
  JOURNAL   Nature 455 (7213), 674-678 (2008)
   PUBMED   18724357
  REMARK    Erratum:[Nature. 2008 Nov 13;456(7219):274]
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Sikorska,M., Sandhu,J.K., Deb-Rinker,P., Jezierski,A., Leblanc,J.,
            Charlebois,C., Ribecco-Lutkiewicz,M., Bani-Yaghoub,M. and
            Walker,P.R.
  TITLE     Epigenetic modifications of SOX2 enhancers, SRR1 and SRR2,
            correlate with in vitro neural differentiation
  JOURNAL   J Neurosci Res 86 (8), 1680-1693 (2008)
   PUBMED   18293417
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Zhang,H., Li,X.J., Martin,D.B. and Aebersold,R.
  TITLE     Identification and quantification of N-linked glycoproteins using
            hydrazide chemistry, stable isotope labeling and mass spectrometry
  JOURNAL   Nat Biotechnol 21 (6), 660-666 (2003)
   PUBMED   12754519
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Dodson,G. and Steiner,D.
  TITLE     The role of assembly in insulin's biosynthesis
  JOURNAL   Curr Opin Struct Biol 8 (2), 189-194 (1998)
   PUBMED   9631292
  REMARK    Review article
REFERENCE   7  (residues 1 to 183)
  AUTHORS   Chinen,K., Sudo,K., Takahashi,E. and Nakamura,Y.
  TITLE     Isolation and mapping of the human beta-signal sequence receptor
            gene (SSR2)
  JOURNAL   Cytogenet Cell Genet 70 (3-4), 215-217 (1995)
   PUBMED   7789174
REFERENCE   8  (residues 1 to 183)
  AUTHORS   Bodescot,M. and Brison,O.
  TITLE     Cloning and sequence analysis of the beta subunit of the human
            translocon-associated protein
  JOURNAL   Biochim Biophys Acta 1217 (1), 101-102 (1994)
   PUBMED   8286409
REFERENCE   9  (residues 1 to 183)
  AUTHORS   Hartmann,E., Gorlich,D., Kostka,S., Otto,A., Kraft,R., Knespel,S.,
            Burger,E., Rapoport,T.A. and Prehn,S.
  TITLE     A tetrameric complex of membrane proteins in the endoplasmic
            reticulum
  JOURNAL   Eur J Biochem 214 (2), 375-381 (1993)
   PUBMED   7916687
REFERENCE   10 (residues 1 to 183)
  AUTHORS   Tajima,S., Lauffer,L., Rath,V.L. and Walter,P.
  TITLE     The signal recognition particle receptor is a complex that contains
            two distinct polypeptide chains
  JOURNAL   J Cell Biol 103 (4), 1167-1178 (1986)
   PUBMED   3021779
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP196192.1, X74104.1 and
            AK222600.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_950520.1, XP_950521.1, XP_950523.1, XP_946862.1.
            
            Summary: The signal sequence receptor (SSR) is a glycosylated
            endoplasmic reticulum (ER) membrane receptor associated with
            protein translocation across the ER membrane. The SSR consists of 2
            subunits, a 34-kD glycoprotein (alpha-SSR or SSR1) and a 22-kD
            glycoprotein (beta-SSR or SSR2). The human beta-signal sequence
            receptor gene (SSR2) maps to chromosome bands 1q21-q23. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.19014.1,
                                           SRR5189667.257487.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            MANE Ensembl match               :: ENST00000295702.9/
                                                ENSP00000295702.4
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..183
                     /product="translocon-associated protein subunit beta
                     precursor"
                     /note="translocon-associated protein beta;
                     translocon-associated protein subunit beta; SSR-beta;
                     signal sequence receptor subunit beta; signal sequence
                     receptor, beta (translocon-associated protein beta)"
                     /calculated_mol_wt=18274
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1879
     Region          4..179
                     /region_name="TRAP_beta"
                     /note="Translocon-associated protein beta (TRAPB);
                     pfam05753"
                     /db_xref="CDD:399046"
     mat_peptide     18..183
                     /product="Translocon-associated protein subunit beta.
                     /id=PRO_0000033290"
                     /note="propagated from UniProtKB/Swiss-Prot (P43308.1)"
                     /calculated_mol_wt=18274
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P43308.1)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P43308.1)"
     Site            150..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43308.1)"
     CDS             1..183
                     /gene="SSR2"
                     /gene_synonym="HSD25; TLAP; TRAP-BETA; TRAPB"
                     /coded_by="NM_003145.4:65..616"
                     /db_xref="CCDS:CCDS1126.1"
                     /db_xref="GeneID:6746"
                     /db_xref="HGNC:HGNC:11324"
                     /db_xref="MIM:600867"
ORIGIN      
        1 mrllsfvvla lfavtqaeeg arllasksll nryavegrdl tlqyniynvg ssaaldvels
       61 ddsfppedfg ivsgmlnvkw driapasnvs htvvlrplka gyfnftsati tylaqedgpv
      121 vigstsapgq ggilaqrefd rrfsphfldw aafgvmtlps igiplllwys skrkydtpkt
      181 kkn
//
LOCUS       NP_001356306             375 aa            linear   PRI 27-APR-2025
DEFINITION  nucleosome assembly protein 1-like 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001356306
VERSION     NP_001356306.1
DBSOURCE    REFSEQ: accession NM_001369377.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Tan,L., Cheng,W., Liu,F., Wang,D.O., Wu,L., Cao,N. and Wang,J.
  TITLE     Positive natural selection of N6-methyladenosine on the RNAs of
            processed pseudogenes
  JOURNAL   Genome Biol 22 (1), 180 (2021)
   PUBMED   34120636
  REMARK    GeneRIF: Positive natural selection of N6-methyladenosine on the
            RNAs of processed pseudogenes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Mizuhashi,S., Fukushima,S., Ishibashi,T., Kuriyama,H., Kimura,T.,
            Kanemaru,H., Kajihara,I., Makino,K., Miyashita,A., Aoi,J., Kita,K.
            and Ihn,H.
  TITLE     Nucleosome assembly protein 1-like 4, a new therapeutic target for
            proliferation and invasion of melanoma cells
  JOURNAL   J Dermatol Sci 102 (1), 16-24 (2021)
   PUBMED   33583643
  REMARK    GeneRIF: Nucleosome assembly protein 1-like 4, a new therapeutic
            target for proliferation and invasion of melanoma cells.
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Tanaka,T., Hozumi,Y., Martelli,A.M., Iino,M. and Goto,K.
  TITLE     Nucleosome assembly proteins NAP1L1 and NAP1L4 modulate p53
            acetylation to regulate cell fate
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1866 (12), 118560 (2019)
   PUBMED   31634504
  REMARK    GeneRIF: The NAP1L4 regulates cell fate by controlling the
            expression of p53-responsive proarrest and proapoptotic genes
            through selective modulation of p53 acetylation at specific sites
            during normal homeostasis and in stress-induced responses.
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Tanaka,T., Hozumi,Y., Iino,M. and Goto,K.
  TITLE     NAP1L1 regulates NF-kappaB signaling pathway acting on
            anti-apoptotic Mcl-1 gene expression
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1864 (10), 1759-1768 (2017)
   PUBMED   28687276
  REMARK    GeneRIF: knockdown of NAP1L1 suppresses IkappaBalpha degradation
            and nuclear transport of p65 subunit after treatment with TNF-a
            stimulation, leading to attenuation of the NF-kappaB
            transcriptional activity, whereas NAP1L4 knockdown remains
            silent.results of this study suggest that NAP1L1 downregulation
            renders the cell vulnerable to apoptotic cell death through
            attenuation of NF-kappaB transcriptional activity on the
            anti-apop...
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Rodriguez,P., Ruiz,M.T., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2 is part of multi-protein complexes in HeLa cells
  JOURNAL   J Cell Biochem 93 (2), 398-408 (2004)
   PUBMED   15368365
  REMARK    GeneRIF: NAP-2 is in complex(es) with other proteins, which are
            distinct from histones
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Shikama,N., Chan,H.M., Krstic-Demonacos,M., Smith,L., Lee,C.W.,
            Cairns,W. and La Thangue,N.B.
  TITLE     Functional interaction between nucleosome assembly proteins and
            p300/CREB-binding protein family coactivators
  JOURNAL   Mol Cell Biol 20 (23), 8933-8943 (2000)
   PUBMED   11073993
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Rodriguez,P., Pelletier,J., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2: histone chaperone function and phosphorylation state through
            the cell cycle
  JOURNAL   J Mol Biol 298 (2), 225-238 (2000)
   PUBMED   10764593
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Rodriguez,P., Munroe,D., Prawitt,D., Chu,L.L., Bric,E., Kim,J.,
            Reid,L.H., Davies,C., Nakagama,H., Loebbert,R., Winterpacht,A.,
            Petruzzi,M.J., Higgins,M.J., Nowak,N., Evans,G., Shows,T.,
            Weissman,B.E., Zabel,B., Housman,D.E. and Pelletier,J.
  TITLE     Functional characterization of human nucleosome assembly protein-2
            (NAP1L4) suggests a role as a histone chaperone
  JOURNAL   Genomics 44 (3), 253-265 (1997)
   PUBMED   9325046
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Hu,R.J., Lee,M.P., Johnson,L.A. and Feinberg,A.P.
  TITLE     A novel human homologue of yeast nucleosome assembly protein, 65 kb
            centromeric to the p57KIP2 gene, is biallelically expressed in
            fetal and adult tissues
  JOURNAL   Hum Mol Genet 5 (11), 1743-1748 (1996)
   PUBMED   8923002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC131971.9.
            
            Summary: This gene encodes a member of the nucleosome assembly
            protein (NAP) family which can interact with both core and linker
            histones. It can shuttle between the cytoplasm and nucleus,
            suggesting a role as a histone chaperone. This gene is one of
            several located near the imprinted gene domain of 11p15.5, an
            important tumor-suppressor gene region. Alterations in this region
            have been associated with the Beckwith-Wiedemann syndrome, Wilms
            tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung,
            ovarian, and breast cancer. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: DRR138524.664427.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..375
                     /product="nucleosome assembly protein 1-like 4 isoform 1"
                     /note="nucleosome assembly protein 2; nucleosome assembly
                     protein 1-like 4b; NAP-2"
                     /calculated_mol_wt=42692
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          65..338
                     /region_name="NAP"
                     /note="Nucleosome assembly protein (NAP); pfam00956"
                     /db_xref="CDD:460010"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P28656; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          116..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          265..271
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          339..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     CDS             1..375
                     /gene="NAP1L4"
                     /gene_synonym="hNAP2; NAP1L4b; NAP2; NAP2L"
                     /coded_by="NM_001369377.1:213..1340"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS41599.1"
                     /db_xref="GeneID:4676"
                     /db_xref="HGNC:HGNC:7640"
                     /db_xref="MIM:601651"
ORIGIN      
        1 madhsfsdgv psdsveaakn asntekltdq vmqnprvlaa lqerldnvph tpssyietlp
       61 kavkrrinal kqlqvrcahi eakfyeevhd lerkyaalyq plfdkrrefi tgdveptdae
      121 sewhseneee eklagdmksk vvvtekaaat aeepdpkgip efwftifrnv dmlselvqey
      181 depilkhlqd ikvkfsdpgq pmsfvlefhf epndyftnsv ltktykmkse pdkadpfsfe
      241 gpeivdcdgc tidwkkgknv tvktikkkqk hkgrgtvrti tkqvpnesff nffnplkasg
      301 dgesldedse ftlasdfeig hffrerivpr avlyftgeai edddnfeege egeeeelegd
      361 eegededdae inpkv
//
LOCUS       NP_001356027             347 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001356027
VERSION     NP_001356027.1
DBSOURCE    REFSEQ: accession NM_001369098.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.19368.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..347
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 7"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=40001
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..319
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..347
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369098.1:214..1257"
                     /note="isoform 7 is encoded by transcript variant 19"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilkv slmhilrayq enpriekglg hrelvvv
//
LOCUS       NP_001092284             473 aa            linear   PRI 27-APR-2025
DEFINITION  sarcalumenin isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001092284 XP_064152 XP_947147
VERSION     NP_001092284.1
DBSOURCE    REFSEQ: accession NM_001098814.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Conte,E., Dinoi,G., Imbrici,P., De Luca,A. and Liantonio,A.
  TITLE     Sarcoplasmic Reticulum Ca2+ Buffer Proteins: A Focus on the
            Yet-To-Be-Explored Role of Sarcalumenin in Skeletal Muscle Health
            and Disease
  JOURNAL   Cells 12 (5), 715 (2023)
   PUBMED   36899851
  REMARK    GeneRIF: Sarcoplasmic Reticulum Ca[2+] Buffer Proteins: A Focus on
            the Yet-To-Be-Explored Role of Sarcalumenin in Skeletal Muscle
            Health and Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Arking,D.E., Pulit,S.L., Crotti,L., van der Harst,P., Munroe,P.B.,
            Koopmann,T.T., Sotoodehnia,N., Rossin,E.J., Morley,M., Wang,X.,
            Johnson,A.D., Lundby,A., Gudbjartsson,D.F., Noseworthy,P.A.,
            Eijgelsheim,M., Bradford,Y., Tarasov,K.V., Dorr,M.,
            Muller-Nurasyid,M., Lahtinen,A.M., Nolte,I.M., Smith,A.V.,
            Bis,J.C., Isaacs,A., Newhouse,S.J., Evans,D.S., Post,W.S.,
            Waggott,D., Lyytikainen,L.P., Hicks,A.A., Eisele,L., Ellinghaus,D.,
            Hayward,C., Navarro,P., Ulivi,S., Tanaka,T., Tester,D.J.,
            Chatel,S., Gustafsson,S., Kumari,M., Morris,R.W., Naluai,A.T.,
            Padmanabhan,S., Kluttig,A., Strohmer,B., Panayiotou,A.G.,
            Torres,M., Knoflach,M., Hubacek,J.A., Slowikowski,K.,
            Raychaudhuri,S., Kumar,R.D., Harris,T.B., Launer,L.J.,
            Shuldiner,A.R., Alonso,A., Bader,J.S., Ehret,G., Huang,H.,
            Kao,W.H., Strait,J.B., Macfarlane,P.W., Brown,M., Caulfield,M.J.,
            Samani,N.J., Kronenberg,F., Willeit,J., Smith,J.G., Greiser,K.H.,
            Meyer Zu Schwabedissen,H., Werdan,K., Carella,M., Zelante,L.,
            Heckbert,S.R., Psaty,B.M., Rotter,J.I., Kolcic,I., Polasek,O.,
            Wright,A.F., Griffin,M., Daly,M.J., Arnar,D.O., Holm,H.,
            Thorsteinsdottir,U., Denny,J.C., Roden,D.M., Zuvich,R.L.,
            Emilsson,V., Plump,A.S., Larson,M.G., O'Donnell,C.J., Yin,X.,
            Bobbo,M., D'Adamo,A.P., Iorio,A., Sinagra,G., Carracedo,A.,
            Cummings,S.R., Nalls,M.A., Jula,A., Kontula,K.K., Marjamaa,A.,
            Oikarinen,L., Perola,M., Porthan,K., Erbel,R., Hoffmann,P.,
            Jockel,K.H., Kalsch,H., Nothen,M.M., den Hoed,M., Loos,R.J.,
            Thelle,D.S., Gieger,C., Meitinger,T., Perz,S., Peters,A.,
            Prucha,H., Sinner,M.F., Waldenberger,M., de Boer,R.A., Franke,L.,
            van der Vleuten,P.A., Beckmann,B.M., Martens,E., Bardai,A.,
            Hofman,N., Wilde,A.A., Behr,E.R., Dalageorgou,C., Giudicessi,J.R.,
            Medeiros-Domingo,A., Barc,J., Kyndt,F., Probst,V., Ghidoni,A.,
            Insolia,R., Hamilton,R.M., Scherer,S.W., Brandimarto,J.,
            Margulies,K., Moravec,C.E., del Greco,M. F, Fuchsberger,C.,
            O'Connell,J.R., Lee,W.K., Watt,G.C., Campbell,H., Wild,S.H., El
            Mokhtari,N.E., Frey,N., Asselbergs,F.W., Mateo Leach,I., Navis,G.,
            van den Berg,M.P., van Veldhuisen,D.J., Kellis,M., Krijthe,B.P.,
            Franco,O.H., Hofman,A., Kors,J.A., Uitterlinden,A.G.,
            Witteman,J.C., Kedenko,L., Lamina,C., Oostra,B.A., Abecasis,G.R.,
            Lakatta,E.G., Mulas,A., Orru,M., Schlessinger,D., Uda,M.,
            Markus,M.R., Volker,U., Snieder,H., Spector,T.D., Arnlov,J.,
            Lind,L., Sundstrom,J., Syvanen,A.C., Kivimaki,M., Kahonen,M.,
            Mononen,N., Raitakari,O.T., Viikari,J.S., Adamkova,V., Kiechl,S.,
            Brion,M., Nicolaides,A.N., Paulweber,B., Haerting,J.,
            Dominiczak,A.F., Nyberg,F., Whincup,P.H., Hingorani,A.D.,
            Schott,J.J., Bezzina,C.R., Ingelsson,E., Ferrucci,L., Gasparini,P.,
            Wilson,J.F., Rudan,I., Franke,A., Muhleisen,T.W., Pramstaller,P.P.,
            Lehtimaki,T.J., Paterson,A.D., Parsa,A., Liu,Y., van Duijn,C.M.,
            Siscovick,D.S., Gudnason,V., Jamshidi,Y., Salomaa,V., Felix,S.B.,
            Sanna,S., Ritchie,M.D., Stricker,B.H., Stefansson,K., Boyer,L.A.,
            Cappola,T.P., Olsen,J.V., Lage,K., Schwartz,P.J., Kaab,S.,
            Chakravarti,A., Ackerman,M.J., Pfeufer,A., de Bakker,P.I. and
            Newton-Cheh,C.
  CONSRTM   CARe Consortium; COGENT Consortium; DCCT/EDIC; eMERGE Consortium;
            HRGEN Consortium
  TITLE     Genetic association study of QT interval highlights role for
            calcium signaling pathways in myocardial repolarization
  JOURNAL   Nat Genet 46 (8), 826-836 (2014)
   PUBMED   24952745
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   5  (residues 1 to 473)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
REFERENCE   6  (residues 1 to 473)
  AUTHORS   Leberer,E., Charuk,J.H., Green,N.M. and MacLennan,D.H.
  TITLE     Molecular cloning and expression of cDNA encoding a lumenal calcium
            binding glycoprotein from sarcoplasmic reticulum
  JOURNAL   Proc Natl Acad Sci U S A 86 (16), 6047-6051 (1989)
   PUBMED   2762314
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB149163.1, AL831973.2, AK056588.1, AL832361.1, DA563862.1 and
            F26773.1.
            
            On or before Jun 26, 2007 this sequence version replaced
            XP_064152.8, XP_947147.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056588.1, SRR1803614.58257.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399609.7/ ENSP00000382518.3
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..473
                     /product="sarcalumenin isoform 1 precursor"
                     /calculated_mol_wt=52372
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2077
     mat_peptide     21..473
                     /product="Sarcalumenin. /id=PRO_0000045426"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TD4.3)"
                     /calculated_mol_wt=52372
     Region          59..91
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Region          95..336
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Region          100..107
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TD4.3)"
     Site            100..107
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(105..108,190,256,258,292..294)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Region          128..129
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TD4.3)"
     Site            131
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            135..137
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Region          190..193
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TD4.3)"
     Site            190..193
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(192..193,219..220)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Region          255..258
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TD4.3)"
     Site            255..258
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Region          278
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TD4.3)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86TD4.3)"
     Site            292..294
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     Site            389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86TD4.3)"
     CDS             1..473
                     /gene="SRL"
                     /gene_synonym="SAR"
                     /coded_by="NM_001098814.2:14..1435"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS42113.1"
                     /db_xref="GeneID:6345"
                     /db_xref="HGNC:HGNC:11295"
                     /db_xref="MIM:604992"
ORIGIN      
        1 mralvllgcl lasllfsgqa eetedaneea plrdrshiek tlmlnedkps ddysavlqrl
       61 rkiyhssikp leqsykynel rqheitdgei tskpmvlflg pwsvgkstmi nyllglentr
      121 yqlytgaept tseftvlmhg pklktiegiv maadsarsfs plekfgqnfl ekligievph
      181 kllervtfvd tpgiienrkq qergypfndv cqwfidradl ifvvfdptkl dvglelemlf
      241 rqlkgresqi riilnkadnl atqmlmrvyg alfwslapli nvtepprvyv ssfwpqeykp
      301 dthqelflqe eislledlnq vienrlenki afirqhairv rihallvdry lqtykdkmtf
      361 fsdgelvfkd ivedpdkfyi fktilaktnv skfdlpnrea ykdffginpi ssfkllsqqc
      421 symggcflek ieraitqelp gllgslglgk npgalncdkt gcsetpknry rkh
//
LOCUS       NP_000137                175 aa            linear   PRI 27-APR-2025
DEFINITION  ferritin light chain [Homo sapiens].
ACCESSION   NP_000137
VERSION     NP_000137.2
DBSOURCE    REFSEQ: accession NM_000146.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Swanson,M.E.V., Mrkela,M., Murray,H.C., Cao,M.C., Turner,C.,
            Curtis,M.A., Faull,R.L.M., Walker,A.K. and Scotter,E.L.
  TITLE     Microglial CD68 and L-ferritin upregulation in response to
            phosphorylated-TDP-43 pathology in the amyotrophic lateral
            sclerosis brain
  JOURNAL   Acta Neuropathol Commun 11 (1), 69 (2023)
   PUBMED   37118836
  REMARK    GeneRIF: Microglial CD68 and L-ferritin upregulation in response to
            phosphorylated-TDP-43 pathology in the amyotrophic lateral
            sclerosis brain.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Yang,X., Ding,Y., Sun,L., Shi,M., Zhang,P., Huang,Z., Wang,J.,
            He,A., Wang,J., Wei,J., Liu,M., Liu,J., Wang,G., Yang,X. and Li,R.
  TITLE     Ferritin light chain deficiency-induced ferroptosis is involved in
            preeclampsia pathophysiology by disturbing uterine spiral artery
            remodelling
  JOURNAL   Redox Biol 58, 102555 (2022)
   PUBMED   36446230
  REMARK    GeneRIF: Ferritin light chain deficiency-induced ferroptosis is
            involved in preeclampsia pathophysiology by disturbing uterine
            spiral artery remodelling.
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Yang,Y., Lin,T., Kuang,P. and Chen,X.
  TITLE     Ferritin L-subunit gene mutation and hereditary hyperferritinaemia
            cataract syndrome (HHCS): a case report and literature review
  JOURNAL   Hematology 26 (1), 896-903 (2021)
   PUBMED   34789084
  REMARK    GeneRIF: Ferritin L-subunit gene mutation and hereditary
            hyperferritinaemia cataract syndrome (HHCS): a case report and
            literature review.
            Review article
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Otsu,W., Ishida,K., Chinen,N., Nakamura,S., Shimazawa,M.,
            Tsusaki,H. and Hara,H.
  TITLE     Cigarette smoke extract and heated tobacco products promote
            ferritin cleavage and iron accumulation in human corneal epithelial
            cells
  JOURNAL   Sci Rep 11 (1), 18555 (2021)
   PUBMED   34535730
  REMARK    GeneRIF: Cigarette smoke extract and heated tobacco products
            promote ferritin cleavage and iron accumulation in human corneal
            epithelial cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Gregory,A., A Kurian,M., Wilson,J. and Hayflick,S.
  TITLE     Neurodegeneration with Brain Iron Accumulation Disorders Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23447832
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Chinnery,P.F.
  TITLE     Neuroferritinopathy
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301320
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Gatti,R.A., Shaked,R., Mohandas,T.K. and Salser,W.
  TITLE     Human ferritin genes: chromosomal assignments and polymorphisms
  JOURNAL   Am J Hum Genet 41 (4), 654-667 (1987)
   PUBMED   2821803
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Lebo,R.V., Kan,Y.W., Cheung,M.C., Jain,S.K. and Drysdale,J.
  TITLE     Human ferritin light chain gene sequences mapped to several sorted
            chromosomes
  JOURNAL   Hum Genet 71 (4), 325-328 (1985)
   PUBMED   3000916
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Arosio,P., Adelman,T.G. and Drysdale,J.W.
  TITLE     On ferritin heterogeneity. Further evidence for heteropolymers
  JOURNAL   J Biol Chem 253 (12), 4451-4458 (1978)
   PUBMED   659425
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK130191.1 and BC004245.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 15, 2002 this sequence version replaced NP_000137.1.
            
            Summary: This gene encodes the light subunit of the ferritin
            protein. Ferritin is the major intracellular iron storage protein
            in prokaryotes and eukaryotes. It is composed of 24 subunits of the
            heavy and light ferritin chains. Variation in ferritin subunit
            composition may affect the rates of iron uptake and release in
            different tissues. A major function of ferritin is the storage of
            iron in a soluble and nontoxic state. Defects in this light chain
            ferritin gene are associated with several neurodegenerative
            diseases and hyperferritinemia-cataract syndrome. This gene has
            multiple pseudogenes. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.170280.1,
                                           SRR3476690.1169062.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331825.11/ ENSP00000366525.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..175
                     /product="ferritin light chain"
                     /note="ferritin light polypeptide-like 3; ferritin L
                     subunit; ferritin L-chain; ferritin, light polypeptide;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=19889
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:6653779; propagated from
                     UniProtKB/Swiss-Prot (P02792.2)"
     Region          10..169
                     /region_name="Ferritin"
                     /note="Ferritin iron storage proteins; cd00904"
                     /db_xref="CDD:153098"
     Site            order(24,58..59,62,104,137,140..141)
                     /site_type="other"
                     /note="ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153098"
     Region          54..61
                     /region_name="Catalytic site for iron oxidation"
                     /note="propagated from UniProtKB/Swiss-Prot (P02792.2)"
     CDS             1..175
                     /gene="FTL"
                     /gene_synonym="FTL1; LFTD; NBIA3"
                     /coded_by="NM_000146.4:200..727"
                     /db_xref="CCDS:CCDS33070.1"
                     /db_xref="GeneID:2512"
                     /db_xref="HGNC:HGNC:3999"
                     /db_xref="MIM:134790"
ORIGIN      
        1 mssqirqnys tdveaavnsl vnlylqasyt ylslgfyfdr ddvalegvsh ffrelaeekr
       61 egyerllkmq nqrggralfq dikkpaedew gktpdamkaa malekklnqa lldlhalgsa
      121 rtdphlcdfl ethfldeevk likkmgdhlt nlhrlggpea glgeylferl tlkhd
//
LOCUS       NP_000685                468 aa            linear   PRI 27-APR-2025
DEFINITION  aldehyde dehydrogenase family 3 member B1 isoform a [Homo sapiens].
ACCESSION   NP_000685
VERSION     NP_000685.1
DBSOURCE    REFSEQ: accession NM_000694.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Tang,C., Xu,J., Zheng,M., Qian,D., Gao,Z., Li,X. and Zhang,W.
  TITLE     Potential clinical significance of ALDH3B1 in auxiliary diagnosis
            of gastric cancer
  JOURNAL   Biomark Med 18 (1), 15-23 (2024)
   PUBMED   38334412
  REMARK    GeneRIF: Potential clinical significance of ALDH3B1 in auxiliary
            diagnosis of gastric cancer.
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Li,Q., Qiu,Q., Zhang,L., Zhang,X., Wang,Y., Geng,Z., Ge,S., Zuo,L.,
            Song,X., Li,J. and Hu,J.
  TITLE     [ALDH3B1 expression is correlated with histopathology and long-term
            prognosis of gastric cancer]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 42 (5), 633-640 (2022)
   PUBMED   35673905
  REMARK    GeneRIF: [ALDH3B1 expression is correlated with histopathology and
            long-term prognosis of gastric cancer].
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Sun,H., Zhang,M., Li,L. and Huang,Z.
  TITLE     ALDH3B1 Is an Independent Prognostic Biomarker of Lung
            Adenocarcinoma
  JOURNAL   Technol Cancer Res Treat 19, 1533033820946018 (2020)
   PUBMED   32744175
  REMARK    GeneRIF: ALDH3B1 Is an Independent Prognostic Biomarker of Lung
            Adenocarcinoma.
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Kitamura,T., Naganuma,T., Abe,K., Nakahara,K., Ohno,Y. and
            Kihara,A.
  TITLE     Substrate specificity, plasma membrane localization, and lipid
            modification of the aldehyde dehydrogenase ALDH3B1
  JOURNAL   Biochim Biophys Acta 1831 (8), 1395-1401 (2013)
   PUBMED   23721920
  REMARK    GeneRIF: the likely physiological function of ALDH3B1 is to oxidize
            lipid-derived aldehydes generated in the plasma membrane and not to
            be involved in the sphingolipid metabolism in the endoplasmic
            reticulum.
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Jin,P., Fu,G.K., Wilson,A.D., Yang,J., Chien,D., Hawkins,P.R.,
            Au-Young,J. and Stuve,L.L.
  TITLE     PCR isolation and cloning of novel splice variant mRNAs from known
            drug target genes
  JOURNAL   Genomics 83 (4), 566-571 (2004)
   PUBMED   15028279
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Yoshida,A., Rzhetsky,A., Hsu,L.C. and Chang,C.
  TITLE     Human aldehyde dehydrogenase gene family
  JOURNAL   Eur J Biochem 251 (3), 549-557 (1998)
   PUBMED   9490025
  REMARK    Review article
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Hsu,L.C., Chang,W.C. and Yoshida,A.
  TITLE     Human aldehyde dehydrogenase genes, ALDH7 and ALDH8: genomic
            organization and gene structure comparison
  JOURNAL   Gene 189 (1), 89-94 (1997)
   PUBMED   9161417
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Hsu,L.C., Chang,W.C. and Yoshida,A.
  TITLE     Cloning of a cDNA encoding human ALDH7, a new member of the
            aldehyde dehydrogenase family
  JOURNAL   Gene 151 (1-2), 285-289 (1994)
   PUBMED   7828891
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA624671.1 and BC013584.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the aldehyde dehydrogenase
            protein family. Aldehyde dehydrogenases are a family of isozymes
            that may play a major role in the detoxification of aldehydes
            generated by alcohol metabolism and lipid peroxidation. The encoded
            protein is able to oxidize long-chain fatty aldehydes in vitro, and
            may play a role in protection from oxidative stress. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Feb 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1 and 3 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013584.2, SRR3476690.601337.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342456.11/ ENSP00000473990.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..468
                     /product="aldehyde dehydrogenase family 3 member B1
                     isoform a"
                     /EC_number="1.2.1.5"
                     /EC_number="1.2.1.28"
                     /EC_number="1.2.1.7"
                     /EC_number="1.2.1.48"
                     /note="aldehyde dehydrogenase 3B1; aldehyde dehydrogenase
                     7; long-chain fatty aldehyde dehydrogenase; medium-chain
                     fatty aldehyde dehydrogenase"
                     /calculated_mol_wt=51709
     mat_peptide     1..465
                     /product="Aldehyde dehydrogenase family 3 member B1.
                     /id=PRO_0000056481"
                     /note="propagated from UniProtKB/Swiss-Prot (P43353.1)"
                     /calculated_mol_wt=51513
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P43353.1)"
     Region          6..447
                     /region_name="ALDH_F3AB"
                     /note="Aldehyde dehydrogenase family 3 members A1, A2, and
                     B1 and related proteins; cd07132"
                     /db_xref="CDD:143450"
     Site            order(57,87..88,92,99,103,105,180,182,190,194,197,204,224,
                     227,230..231,234,271,281,359..360,364,369,375,378,
                     381..390,396,401,404..405,407,410,424,426..427,429..433,
                     437,439..440,442..446)
                     /site_type="other"
                     /note="homodimeric interface [polypeptide binding]"
                     /db_xref="CDD:143450"
     Site            order(113..115,141,170,188,287,289..290,293,334,336)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143450"
     Site            order(115,210,241,244)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143450"
     Site            465
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P43353.1)"
     CDS             1..468
                     /gene="ALDH3B1"
                     /gene_synonym="ALDH4; ALDH7"
                     /coded_by="NM_000694.4:68..1474"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS73335.1"
                     /db_xref="GeneID:221"
                     /db_xref="HGNC:HGNC:410"
                     /db_xref="MIM:600466"
ORIGIN      
        1 mdplgdtlrr lreafhagrt rpaefraaql qglgrflqen kqllhdalaq dlhksafese
       61 vsevaisqge vtlalrnlra wmkdervpkn latqldsafi rkepfglvli iapwnyplnl
      121 tlvplvgala agncvvlkps eisknvekil aevlpqyvdq scfavvlggp qetgqllehr
      181 fdyifftgsp rvgkivmtaa akhltpvtle lggknpcyvd dncdpqtvan rvawfryfna
      241 gqtcvapdyv lcspemqerl lpalqstitr fygddpqssp nlgriinqkq fqrlrallgc
      301 grvaiggqsd esdryiaptv lvdvqemepv mqeeifgpil pivnvqslde aiefinrrek
      361 plalyafsns sqvvkrvltq tssggfcgnd gfmhmtlasl pfggvgasgm gryhgkfsfd
      421 tfshhracll rspgmeklna lryppqsprr lrmllvamea qgcsctll
//
LOCUS       NP_071762                761 aa            linear   PRI 27-APR-2025
DEFINITION  semaphorin-4A isoform 1 precursor [Homo sapiens].
ACCESSION   NP_071762
VERSION     NP_071762.2
DBSOURCE    REFSEQ: accession NM_022367.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Hou,T., Zhang,P., Tian,H., Luo,Y., Li,J., Zhang,K. and Li,Y.
  TITLE     Semaphorin 4A Maintains Trophoblastic Function via Activating the
            STAT3 Pathway
  JOURNAL   Biomolecules 14 (7), 826 (2024)
   PUBMED   39062540
  REMARK    GeneRIF: Semaphorin 4A Maintains Trophoblastic Function via
            Activating the STAT3 Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Naito,Y., Koyama,S., Masuhiro,K., Hirai,T., Uenami,T., Inoue,T.,
            Osa,A., Machiyama,H., Watanabe,G., Sax,N., Villa,J.,
            Kinugasa-Katayama,Y., Nojima,S., Yaga,M., Hosono,Y., Okuzaki,D.,
            Satoh,S., Tsuda,T., Nakanishi,Y., Suga,Y., Morita,T., Fukushima,K.,
            Nishide,M., Shiroyama,T., Miyake,K., Iwahori,K., Hirata,H.,
            Nagatomo,I., Yano,Y., Tamiya,M., Kumagai,T., Takemoto,N.,
            Inohara,H., Yamasaki,S., Yamashita,K., Aoshi,T., Akbay,E.A.,
            Hosen,N., Shintani,Y., Takamatsu,H., Mori,M., Takeda,Y. and
            Kumanogoh,A.
  TITLE     Tumor-derived semaphorin 4A improves PD-1-blocking antibody
            efficacy by enhancing CD8+ T cell cytotoxicity and proliferation
  JOURNAL   Sci Adv 9 (20), eade0718 (2023)
   PUBMED   37205755
  REMARK    GeneRIF: Tumor-derived semaphorin 4A improves PD-1-blocking
            antibody efficacy by enhancing CD8[+] T cell cytotoxicity and
            proliferation.
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Eiza,N., Garty,M., Staun-Ram,E., Miller,A. and Vadasz,Z.
  TITLE     The possible involvement of sema3A and sema4A in the pathogenesis
            of multiple sclerosis
  JOURNAL   Clin Immunol 238, 109017 (2022)
   PUBMED   35460904
  REMARK    GeneRIF: The possible involvement of sema3A and sema4A in the
            pathogenesis of multiple sclerosis.
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Chapoval,S.P., Lee,M., Lemmer,A., Ajayi,O., Qi,X., Neuwald,A.F. and
            Keegan,A.D.
  TITLE     Identifying Function Determining Residues in Neuroimmune Semaphorin
            4A
  JOURNAL   Int J Mol Sci 23 (6), 3024 (2022)
   PUBMED   35328445
  REMARK    GeneRIF: Identifying Function Determining Residues in Neuroimmune
            Semaphorin 4A.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Kumanogoh,A. and Kikutani,H.
  TITLE     Immune semaphorins: a new area of semaphorin research
  JOURNAL   J Cell Sci 116 (Pt 17), 3463-3470 (2003)
   PUBMED   12893810
  REMARK    Review article
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Kikutani,H. and Kumanogoh,A.
  TITLE     Semaphorins in interactions between T cells and antigen-presenting
            cells
  JOURNAL   Nat Rev Immunol 3 (2), 159-167 (2003)
   PUBMED   12563299
  REMARK    Review article
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Kumanogoh,A., Marukawa,S., Suzuki,K., Takegahara,N., Watanabe,C.,
            Ch'ng,E., Ishida,I., Fujimura,H., Sakoda,S., Yoshida,K. and
            Kikutani,H.
  TITLE     Class IV semaphorin Sema4A enhances T-cell activation and interacts
            with Tim-2
  JOURNAL   Nature 419 (6907), 629-633 (2002)
   PUBMED   12374982
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Puschel,A.W., Adams,R.H. and Betz,H.
  TITLE     Murine semaphorin D/collapsin is a member of a diverse gene family
            and creates domains inhibitory for axonal extension
  JOURNAL   Neuron 14 (5), 941-948 (1995)
   PUBMED   7748561
REFERENCE   10 (residues 1 to 761)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA409501.1, BC020974.1 and
            AY358531.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_071762.1.
            
            Summary: This gene encodes a member of the semaphorin family of
            soluble and transmembrane proteins. Semaphorins are involved in
            numerous functions, including axon guidance, morphogenesis,
            carcinogenesis, and immunomodulation. The encoded protein is a
            single-pass type I membrane protein containing an
            immunoglobulin-like C2-type domain, a PSI domain and a sema domain.
            It inhibits axonal extension by providing local signals to specify
            territories inaccessible for growing axons. It is an activator of
            T-cell-mediated immunity and suppresses vascular endothelial growth
            factor (VEGF)-mediated endothelial cell migration and proliferation
            in vitro and angiogenesis in vivo. Mutations in this gene are
            associated with retinal degenerative diseases including retinitis
            pigmentosa type 35 (RP35) and cone-rod dystrophy type 10 (CORD10).
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been identified.[provided by RefSeq, Sep
            2010].
            
            Transcript Variant: This variant (1) is the longest transcript.
            Variants 1-3 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020974.1, SRR1660803.161175.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368285.8/ ENSP00000357268.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..761
                     /product="semaphorin-4A isoform 1 precursor"
                     /note="sema B; semaphorin-B; sema domain, immunoglobulin
                     domain (Ig), transmembrane domain (TM) and short
                     cytoplasmic domain, (semaphorin) 4A"
                     /calculated_mol_wt=80167
     sig_peptide     1..32
                     /calculated_mol_wt=3425
     mat_peptide     33..761
                     /product="semaphorin-4A isoform 1"
                     /calculated_mol_wt=80167
     Region          55..495
                     /region_name="Sema_4A"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4A (Sema4A); cd11256"
                     /db_xref="CDD:200517"
     Site            order(115..117,178,199,201..202,204,219,222,224,229,252,
                     276..280,282,361..362,386,390,393)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200517"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Site            order(253..254,256,259..261,295,297..299,301,303,326..328,
                     334..335,399,411)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200517"
     Region          496..540
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Site            496
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          566..638
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          576..580
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409456"
     Region          588..592
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409456"
     Region          607..611
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409456"
     Site            607
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          621..626
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409456"
     Site            684..704
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          722..749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S1.2)"
     CDS             1..761
                     /gene="SEMA4A"
                     /gene_synonym="CORD10; RP35; SEMAB; SEMB"
                     /coded_by="NM_022367.4:210..2495"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1132.1"
                     /db_xref="GeneID:64218"
                     /db_xref="HGNC:HGNC:10729"
                     /db_xref="MIM:607292"
ORIGIN      
        1 malpalgldp wsllglflfq llqlllpttt aggggqgpmp rvryyagder ralsffhqkg
       61 lqdfdtllls gdgntlyvga reailaldiq dpgvprlknm ipwpasdrkk secafkkksn
      121 etqcfnfirv lvsynvthly tcgtfafspa ctfielqdsy llpisedkvm egkgqspfdp
      181 ahkhtavlvd gmlysgtmnn flgsepilmr tlgsqpvlkt dnflrwlhhd asfvaaipst
      241 qvvyfffeet asefdfferl htsrvarvck ndvggekllq kkwttflkaq llctqpgqlp
      301 fnvirhavll padsptaphi yavftsqwqv ggtrssavca fslldiervf kgkykelnke
      361 tsrwttyrgp etnprpgscs vgpssdkalt fmkdhflmde qvvgtpllvk sgveytrlav
      421 etaqgldghs hlvmylgttt gslhkavvsg dssahlveei qlfpdpepvr nlqlaptqga
      481 vfvgfsggvw rvprancsvy escvdcvlar dphcawdpes rtccllsapn lnswkqdmer
      541 gnpewacasg pmsrslrpqs rpqiikevla vpnsilelpc phlsalasyy wshgpaavpe
      601 asstvyngsl llivqdgvgg lyqcwateng fsypvisywv dsqdqtlald pelagipreh
      661 vkvpltrvsg gaalaaqqsy wphfvtvtvl falvlsgali ilvasplral rargkvqgce
      721 tlrpgekapl sreqhlqspk ecrtsasdvd adnnclgtev a
//
LOCUS       NP_060718                605 aa            linear   PRI 27-APR-2025
DEFINITION  endonuclease 8-like 3 [Homo sapiens].
ACCESSION   NP_060718
VERSION     NP_060718.3
DBSOURCE    REFSEQ: accession NM_018248.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Zhang,M., Jiang,Y., Wang,J., Yue,Y., Liu,W., Wang,L., Li,Y.,
            Wang,W., Cai,H., Yang,Z., Ma,M., Lu,S. and Fan,J.
  TITLE     NEIL3 promotes cell proliferation of ccRCC via the cyclin
            D1-Rb-E2F1 feedback loop regulation
  JOURNAL   DNA Repair (Amst) 133, 103604 (2024)
   PUBMED   37992567
  REMARK    GeneRIF: NEIL3 promotes cell proliferation of ccRCC via the cyclin
            D1-Rb-E2F1 feedback loop regulation.
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Wang,G.N., Zhang,Y.P., Wang,M.C., Han,W. and Zhang,Y.C.
  TITLE     [Overexpression of Nei endonuclease VIII-like protein 3 in
            hepatocellular carcinoma indicates increased levels of immune
            infiltration and an unfavorable prognosis]
  JOURNAL   Zhonghua Gan Zang Bing Za Zhi 31 (9), 986-995 (2023)
   PUBMED   37872095
  REMARK    GeneRIF: [Overexpression of Nei endonuclease VIII-like protein 3 in
            hepatocellular carcinoma indicates increased levels of immune
            infiltration and an unfavorable prognosis].
REFERENCE   3  (residues 1 to 605)
  AUTHORS   Pan,Z., Zhao,R., Li,B., Qi,Y., Qiu,W., Guo,Q., Zhang,S., Zhao,S.,
            Xu,H., Li,M., Gao,Z., Fan,Y., Xu,J., Wang,H., Wang,S., Qiu,J.,
            Wang,Q., Guo,X., Deng,L., Zhang,P., Xue,H. and Li,G.
  TITLE     EWSR1-induced circNEIL3 promotes glioma progression and
            exosome-mediated macrophage immunosuppressive polarization via
            stabilizing IGF2BP3
  JOURNAL   Mol Cancer 21 (1), 16 (2022)
   PUBMED   35031058
  REMARK    GeneRIF: EWSR1-induced circNEIL3 promotes glioma progression and
            exosome-mediated macrophage immunosuppressive polarization via
            stabilizing IGF2BP3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 605)
  AUTHORS   Wang,Y., Xu,L., Shi,S., Wu,S., Meng,R., Chen,H. and Jiang,Z.
  TITLE     Deficiency of NEIL3 Enhances the Chemotherapy Resistance of
            Prostate Cancer
  JOURNAL   Int J Mol Sci 22 (8), 4098 (2021)
   PUBMED   33921035
  REMARK    GeneRIF: Deficiency of NEIL3 Enhances the Chemotherapy Resistance
            of Prostate Cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 605)
  AUTHORS   Shen,P., Yang,T., Chen,Q., Yuan,H., Wu,P., Cai,B., Meng,L.,
            Huang,X., Liu,J., Zhang,Y., Hu,W., Miao,Y., Lu,Z. and Jiang,K.
  TITLE     CircNEIL3 regulatory loop promotes pancreatic ductal adenocarcinoma
            progression via miRNA sponging and A-to-I RNA-editing
  JOURNAL   Mol Cancer 20 (1), 51 (2021)
   PUBMED   33750389
  REMARK    GeneRIF: CircNEIL3 regulatory loop promotes pancreatic ductal
            adenocarcinoma progression via miRNA sponging and A-to-I
            RNA-editing.
            Erratum:[Mol Cancer. 2022 Aug 19;21(1):165. doi:
            10.1186/s12943-022-01636-3. PMID: 35986360]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 605)
  AUTHORS   Newton-Cheh,C., Guo,C.Y., Wang,T.J., O'donnell,C.J., Levy,D. and
            Larson,M.G.
  TITLE     Genome-wide association study of electrocardiographic and heart
            rate variability traits: the Framingham Heart Study
  JOURNAL   BMC Med Genet 8 Suppl 1 (Suppl 1), S7 (2007)
   PUBMED   17903306
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 605)
  AUTHORS   Rosenquist,T.A., Zaika,E., Fernandes,A.S., Zharkov,D.O., Miller,H.
            and Grollman,A.P.
  TITLE     The novel DNA glycosylase, NEIL1, protects mammalian cells from
            radiation-mediated cell death
  JOURNAL   DNA Repair (Amst) 2 (5), 581-591 (2003)
   PUBMED   12713815
REFERENCE   8  (residues 1 to 605)
  AUTHORS   Morland,I., Rolseth,V., Luna,L., Rognes,T., Bjoras,M. and
            Seeberg,E.
  TITLE     Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an
            alternative pathway for the repair of 8-oxoguanine and other
            oxidation products in DNA
  JOURNAL   Nucleic Acids Res 30 (22), 4926-4936 (2002)
   PUBMED   12433996
  REMARK    GeneRIF: hFPG1 and hFPG2 repair 8-oxoguanine and other DNA
            oxidation products. (hFPG1 and hFPG2)
REFERENCE   9  (residues 1 to 605)
  AUTHORS   Takao,M., Kanno,S., Kobayashi,K., Zhang,Q.M., Yonei,S., van der
            Horst,G.T. and Yasui,A.
  TITLE     A back-up glycosylase in Nth1 knock-out mice is a functional Nei
            (endonuclease VIII) homologue
  JOURNAL   J Biol Chem 277 (44), 42205-42213 (2002)
   PUBMED   12200441
REFERENCE   10 (residues 1 to 605)
  AUTHORS   Bandaru,V., Sunkara,S., Wallace,S.S. and Bond,J.P.
  TITLE     A novel human DNA glycosylase that removes oxidative DNA damage and
            is homologous to Escherichia coli endonuclease VIII
  JOURNAL   DNA Repair (Amst) 1 (7), 517-529 (2002)
   PUBMED   12509226
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027627.6.
            
            On Nov 23, 2018 this sequence version replaced NP_060718.2.
            
            Summary: NEIL3 belongs to a class of DNA glycosylases homologous to
            the bacterial Fpg/Nei family. These glycosylases initiate the first
            step in base excision repair by cleaving bases damaged by reactive
            oxygen species and introducing a DNA strand break via the
            associated lyase reaction (Bandaru et al., 2002 [PubMed
            12509226]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001720.1, SRR1803615.54197.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264596.4/ ENSP00000264596.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q34.3"
     Protein         1..605
                     /product="endonuclease 8-like 3"
                     /EC_number="4.2.99.18"
                     /note="DNA glycosylase hFPG2; endonuclease VIII-like 3;
                     nei-like protein 3; DNA glycosylase FPG2; zinc finger,
                     GRF-type containing 3; nei endonuclease VIII-like 3; DNA
                     glycosylase/AP lyase Neil3"
                     /calculated_mol_wt=67638
     Region          1..151
                     /region_name="MeNeil3_N"
                     /note="N-terminal domain of metazoan Nei-like glycosylase
                     3 (NEIL3); cd08969"
                     /db_xref="CDD:176803"
     Site            order(2..3,81,95,97..99,115..116)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176803"
     Site            2
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:176803"
     Site            2
                     /site_type="other"
                     /note="Important for monofunctional glycosylase activity;
                     propagated from UniProtKB/Swiss-Prot (Q8TAT5.3)"
     Site            order(3..6,8..9,12,78..82)
                     /site_type="other"
                     /note="putative H2TH interface [polypeptide binding]"
                     /db_xref="CDD:176803"
     Site            order(3,81)
                     /site_type="active"
                     /note="putative catalytic residues [active]"
                     /db_xref="CDD:176803"
     Site            81
                     /site_type="other"
                     /note="Required for glycosylase and lyase activities;
                     propagated from UniProtKB/Swiss-Prot (Q8TAT5.3)"
     Region          <180..281
                     /region_name="PRK01103"
                     /note="bifunctional DNA-formamidopyrimidine
                     glycosylase/DNA-(apurinic or apyrimidinic site) lyase"
                     /db_xref="CDD:234899"
     Region          317..345
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          321..340
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TAT5.3)"
     Region          456..477
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAT5.3)"
     Region          505..550
                     /region_name="zf-GRF"
                     /note="GRF zinc finger; pfam06839"
                     /db_xref="CDD:462017"
     Region          552..596
                     /region_name="zf-GRF"
                     /note="GRF zinc finger; pfam06839"
                     /db_xref="CDD:462017"
     CDS             1..605
                     /gene="NEIL3"
                     /gene_synonym="FGP2; FPG2; hFPG2; hNEI3; NEI3; ZGRF3"
                     /coded_by="NM_018248.3:81..1898"
                     /db_xref="CCDS:CCDS3828.1"
                     /db_xref="GeneID:55247"
                     /db_xref="HGNC:HGNC:24573"
                     /db_xref="MIM:608934"
ORIGIN      
        1 mvegpgctln gekirarvlp gqavtgvrgs alrslqgral rlaastvvvs pqaaalnnds
       61 sqnvlslfng yvysgvetlg kelfmyfgpk alrihfgmkg fiminpleyk ykngaspvle
      121 vqltkdlicf fdssvelrns mesqqrirmm keldvcspef sflraesevk kqkgrmlgdv
      181 lmdqnvlpgv gniiknealf dsglhpavkv cqltdeqihh lmkmirdfsi lfyrcrkagl
      241 alskhykvyk rpncgqchcr itvcrfgdnn rmtyfcphcq kenpqhvdic klptrntiis
      301 wtssrvdhvm dsvarkseeh wtcvvctlin kpsskacdac ltsrpidsvl kseenstvfs
      361 hlmkypcntf gkphtevkin rktafgtttl vltdfsnkss tlerktkqnq ildeefqnsp
      421 pasvclndiq hpskkttndi tqpsskvnis ptissesklf spahkkpkta qysspelksc
      481 npgysnselq inmtdgprtl npdsprcskh nrlcilrvvg kdgenkgrqf yacplpreaq
      541 cgffewadls fpfcnhgkrs tmktvlkigp nngknffvcp lgkekqcnff qwaengpgik
      601 iipgc
//
LOCUS       NP_001350514             370 aa            linear   PRI 27-APR-2025
DEFINITION  polyadenylate-binding protein 4-like [Homo sapiens].
ACCESSION   NP_001350514 XP_016863216
VERSION     NP_001350514.1
DBSOURCE    REFSEQ: accession NM_001363585.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Aslam,M., Ullah,A., Paramasivam,N., Kandasamy,N., Naureen,S.,
            Badshah,M., Khan,K., Wajid,M., Abbasi,R., Eils,R., Brockmann,M.A.,
            Schlesner,M., Ahmad,N. and von Engelhardt,J.
  TITLE     Segregation and potential functional impact of a rare stop-gain
            PABPC4L variant in familial atypical Parkinsonism
  JOURNAL   Sci Rep 9 (1), 13576 (2019)
   PUBMED   31537871
  REMARK    GeneRIF: Segregation and potential functional impact of a rare
            stop-gain PABPC4L variant in familial atypical Parkinsonism.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Randall,J.C., Winkler,T.W., Kutalik,Z., Berndt,S.I., Jackson,A.U.,
            Monda,K.L., Kilpelainen,T.O., Esko,T., Magi,R., Li,S.,
            Workalemahu,T., Feitosa,M.F., Croteau-Chonka,D.C., Day,F.R.,
            Fall,T., Ferreira,T., Gustafsson,S., Locke,A.E., Mathieson,I.,
            Scherag,A., Vedantam,S., Wood,A.R., Liang,L., Steinthorsdottir,V.,
            Thorleifsson,G., Dermitzakis,E.T., Dimas,A.S., Karpe,F., Min,J.L.,
            Nicholson,G., Clegg,D.J., Person,T., Krohn,J.P., Bauer,S.,
            Buechler,C., Eisinger,K., Bonnefond,A., Froguel,P., Hottenga,J.J.,
            Prokopenko,I., Waite,L.L., Harris,T.B., Smith,A.V., Shuldiner,A.R.,
            McArdle,W.L., Caulfield,M.J., Munroe,P.B., Gronberg,H., Chen,Y.D.,
            Li,G., Beckmann,J.S., Johnson,T., Thorsteinsdottir,U.,
            Teder-Laving,M., Khaw,K.T., Wareham,N.J., Zhao,J.H., Amin,N.,
            Oostra,B.A., Kraja,A.T., Province,M.A., Cupples,L.A.,
            Heard-Costa,N.L., Kaprio,J., Ripatti,S., Surakka,I., Collins,F.S.,
            Saramies,J., Tuomilehto,J., Jula,A., Salomaa,V., Erdmann,J.,
            Hengstenberg,C., Loley,C., Schunkert,H., Lamina,C., Wichmann,H.E.,
            Albrecht,E., Gieger,C., Hicks,A.A., Johansson,A., Pramstaller,P.P.,
            Kathiresan,S., Speliotes,E.K., Penninx,B., Hartikainen,A.L.,
            Jarvelin,M.R., Gyllensten,U., Boomsma,D.I., Campbell,H.,
            Wilson,J.F., Chanock,S.J., Farrall,M., Goel,A., Medina-Gomez,C.,
            Rivadeneira,F., Estrada,K., Uitterlinden,A.G., Hofman,A.,
            Zillikens,M.C., den Heijer,M., Kiemeney,L.A., Maschio,A., Hall,P.,
            Tyrer,J., Teumer,A., Volzke,H., Kovacs,P., Tonjes,A., Mangino,M.,
            Spector,T.D., Hayward,C., Rudan,I., Hall,A.S., Samani,N.J.,
            Attwood,A.P., Sambrook,J.G., Hung,J., Palmer,L.J., Lokki,M.L.,
            Sinisalo,J., Boucher,G., Huikuri,H., Lorentzon,M., Ohlsson,C.,
            Eklund,N., Eriksson,J.G., Barlassina,C., Rivolta,C., Nolte,I.M.,
            Snieder,H., Van der Klauw,M.M., Van Vliet-Ostaptchouk,J.V.,
            Gejman,P.V., Shi,J., Jacobs,K.B., Wang,Z., Bakker,S.J., Mateo
            Leach,I., Navis,G., van der Harst,P., Martin,N.G., Medland,S.E.,
            Montgomery,G.W., Yang,J., Chasman,D.I., Ridker,P.M., Rose,L.M.,
            Lehtimaki,T., Raitakari,O., Absher,D., Iribarren,C., Basart,H.,
            Hovingh,K.G., Hypponen,E., Power,C., Anderson,D., Beilby,J.P.,
            Hui,J., Jolley,J., Sager,H., Bornstein,S.R., Schwarz,P.E.,
            Kristiansson,K., Perola,M., Lindstrom,J., Swift,A.J., Uusitupa,M.,
            Atalay,M., Lakka,T.A., Rauramaa,R., Bolton,J.L., Fowkes,G.,
            Fraser,R.M., Price,J.F., Fischer,K., Krjuta Kov,K., Metspalu,A.,
            Mihailov,E., Langenberg,C., Luan,J., Ong,K.K., Chines,P.S.,
            Keinanen-Kiukaanniemi,S.M., Saaristo,T.E., Edkins,S., Franks,P.W.,
            Hallmans,G., Shungin,D., Morris,A.D., Palmer,C.N., Erbel,R.,
            Moebus,S., Nothen,M.M., Pechlivanis,S., Hveem,K., Narisu,N.,
            Hamsten,A., Humphries,S.E., Strawbridge,R.J., Tremoli,E.,
            Grallert,H., Thorand,B., Illig,T., Koenig,W., Muller-Nurasyid,M.,
            Peters,A., Boehm,B.O., Kleber,M.E., Marz,W., Winkelmann,B.R.,
            Kuusisto,J., Laakso,M., Arveiler,D., Cesana,G., Kuulasmaa,K.,
            Virtamo,J., Yarnell,J.W., Kuh,D., Wong,A., Lind,L., de Faire,U.,
            Gigante,B., Magnusson,P.K., Pedersen,N.L., Dedoussis,G.,
            Dimitriou,M., Kolovou,G., Kanoni,S., Stirrups,K., Bonnycastle,L.L.,
            Njolstad,I., Wilsgaard,T., Ganna,A., Rehnberg,E., Hingorani,A.,
            Kivimaki,M., Kumari,M., Assimes,T.L., Barroso,I., Boehnke,M.,
            Borecki,I.B., Deloukas,P., Fox,C.S., Frayling,T., Groop,L.C.,
            Haritunians,T., Hunter,D., Ingelsson,E., Kaplan,R., Mohlke,K.L.,
            O'Connell,J.R., Schlessinger,D., Strachan,D.P., Stefansson,K., van
            Duijn,C.M., Abecasis,G.R., McCarthy,M.I., Hirschhorn,J.N., Qi,L.,
            Loos,R.J., Lindgren,C.M., North,K.E. and Heid,I.M.
  CONSRTM   DIAGRAM Consortium; MAGIC Investigators
  TITLE     Sex-stratified genome-wide association studies including 270,000
            individuals show sexual dimorphism in genetic loci for
            anthropometric traits
  JOURNAL   PLoS Genet 9 (6), e1003500 (2013)
   PUBMED   23754948
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC015631.10.
            
            On May 24, 2018 this sequence version replaced XP_016863216.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.120294.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.3"
     Protein         1..370
                     /product="polyadenylate-binding protein 4-like"
                     /note="PABP-4-like"
                     /calculated_mol_wt=41723
     Region          10..>369
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..370
                     /gene="PABPC4L"
                     /coded_by="NM_001363585.1:354..1466"
                     /db_xref="CCDS:CCDS47135.1"
                     /db_xref="GeneID:132430"
                     /db_xref="HGNC:HGNC:31955"
ORIGIN      
        1 mnvaakyrma slyvgdlhad vtedllfrkf stvgpvlsir icrdqvtrrs lgyayvnflq
       61 ladaqkaldt mnfdiikgks irlmwsqrda ylrrsgignv fiknldksid nktlyehfsa
      121 fgkilsskvm sddqgskgya fvhfqnqsaa draieemngk llkgckvfvg rfknrkdrea
      181 elrskaseft nvyiknfggd mdderlkdvf skygktlsvk vmtdssgksk gfgfvsfdsh
      241 eaakkaveem ngrdingqli fvgraqkkve rqaelkqmfe qlkrerirgc qgvklyiknl
      301 ddtiddeklr nefssfgsis rvkvmqeegq skgfglicfs spedatkamt emngrilgsk
      361 plsialaqrh
//
LOCUS       NP_001287944             683 aa            linear   PRI 27-APR-2025
DEFINITION  actin-binding LIM protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001287944 XP_006714826
VERSION     NP_001287944.1
DBSOURCE    REFSEQ: accession NM_001301015.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Cao,J., Shen,Y., Zhu,L., Xu,Y., Zhou,Y., Wu,Z., Li,Y., Yan,X. and
            Zhu,X.
  TITLE     miR-129-3p controls cilia assembly by regulating CP110 and actin
            dynamics
  JOURNAL   Nat Cell Biol 14 (7), 697-706 (2012)
   PUBMED   22684256
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Ruau,D., Dudley,J.T., Chen,R., Phillips,N.G., Swan,G.E.,
            Lazzeroni,L.C., Clark,J.D., Butte,A.J. and Angst,M.S.
  TITLE     Integrative approach to pain genetics identifies pain sensitivity
            loci across diseases
  JOURNAL   PLoS Comput Biol 8 (6), e1002538 (2012)
   PUBMED   22685391
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Matsuda,M., Yamashita,J.K., Tsukita,S. and Furuse,M.
  TITLE     abLIM3 is a novel component of adherens junctions with
            actin-binding activity
  JOURNAL   Eur J Cell Biol 89 (11), 807-816 (2010)
   PUBMED   20709423
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Barrientos,T., Frank,D., Kuwahara,K., Bezprozvannaya,S.,
            Pipes,G.C., Bassel-Duby,R., Richardson,J.A., Katus,H.A., Olson,E.N.
            and Frey,N.
  TITLE     Two novel members of the ABLIM protein family, ABLIM-2 and -3,
            associate with STARS and directly bind F-actin
  JOURNAL   J Biol Chem 282 (11), 8393-8403 (2007)
   PUBMED   17194709
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Krupp,M., Weinmann,A., Galle,P.R. and Teufel,A.
  TITLE     Actin binding LIM protein 3 (abLIM3)
  JOURNAL   Int J Mol Med 17 (1), 129-133 (2006)
   PUBMED   16328021
  REMARK    GeneRIF: Results characterize a third member of the actin binding
            LIM protein subgroup, actin binding LIM protein 3.
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Zheng,B., Wen,J.K., Han,M. and Zhou,A.R.
  TITLE     hhLIM protein is involved in cardiac hypertrophy
  JOURNAL   Biochim Biophys Acta 1690 (1), 1-10 (2004)
   PUBMED   15337165
REFERENCE   10 (residues 1 to 683)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091940.3 and AC012613.7.
            
            On Jul 18, 2014 this sequence version replaced XP_006714826.1.
            
            Summary: This gene encodes a member of the actin-binding LIM
            (abLIM) family of proteins. These proteins are characterized by an
            N-terminal LIM domain and a C-terminal dematin-like domain. The
            encoded protein interacts with actin filaments and may be a
            component of adherens junctions in several cell types. A variant of
            this gene may be associated with pain sensitivity in male human
            patients. [provided by RefSeq, Sep 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225769.1, SRR1803615.147779.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..683
                     /product="actin-binding LIM protein 3 isoform 1"
                     /note="abLIM-3"
                     /calculated_mol_wt=77671
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Region          23..74
                     /region_name="LIM1_abLIM"
                     /note="The first LIM domain of actin binding LIM (abLIM)
                     proteins; cd09327"
                     /db_xref="CDD:188713"
     Site            order(23,26,43,46,49,52,70,73)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188713"
     Region          79..134
                     /region_name="LIM2_abLIM"
                     /note="The second LIM domain on actin binding LIM (abLIM)
                     proteins; cd09328"
                     /db_xref="CDD:188714"
     Site            order(82,85,102,105,108,111,130,133)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188714"
     Region          151..202
                     /region_name="LIM3_abLIM"
                     /note="The third LIM domain of actin binding LIM (abLIM)
                     proteins; cd09329"
                     /db_xref="CDD:188715"
     Site            order(151,154,172,175,178,181,198,201)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188715"
     Region          210..265
                     /region_name="LIM4_abLIM"
                     /note="The fourth LIM domain of actin binding LIM (abLIM)
                     proteins; cd09330"
                     /db_xref="CDD:188716"
     Site            order(210,213,230,233,236,239,258,261)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188716"
     Region          273..633
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZX8; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZX8; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZX8; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZX8; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Region          372..472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94929.3)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZX8; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94929.3)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94929.3)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZX8; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            607
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZX8; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Site            631
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZX8; propagated from
                     UniProtKB/Swiss-Prot (O94929.3)"
     Region          648..683
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..683
                     /gene="ABLIM3"
                     /gene_synonym="HMFN1661"
                     /coded_by="NM_001301015.3:366..2417"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4294.1"
                     /db_xref="GeneID:22885"
                     /db_xref="HGNC:HGNC:29132"
                     /db_xref="MIM:611305"
ORIGIN      
        1 mntsipyqqn pynprgssnv iqcyrcgdtc kgevvrvhnn hfhircftcq vcgcglaqsg
       61 fffknqeyic tqdyqqlygt rcdscrdfit gevisalgrt yhpkcfvcsl crkpfpigdk
      121 vtfsgkecvc qtcsqsmass kpikirgpsh cagckeeikh gqsllaldkq whvscfkcqt
      181 csviltgeyi skdgvpyces dyhaqfgikc etcdryisgr vleaggkhyh ptcarcvrch
      241 qmftegeemy ltgsevwhpi ckqaaraekk lkhrrtsets isppgssigs pnrvicakvd
      301 neilnykdla alpkvksiye vqrpdlisye phsrymsdem lercgygesl gtlspysqdi
      361 yenldlrqrr asspgyidsp tysrqgmspt fsrsphhyyr sgpesgrssp yhsqldvrss
      421 tptsyqapkh fhipagdsni yrkppiykrh gdlstatksk tsedisqtsk yspiyspdpy
      481 yaseseywty hgspkvprar rfssggeedd fdrsmhklqs gigrlilkee mkarsssyad
      541 pwtpprssts srealhtagy emslngsprs hyladsdpli sksaslpayr rnglhrtpsa
      601 dlfhydsmna vnwgmreyki ypyelllvtt rgrnrlpkdv drtrlerhls qeefyqvfgm
      661 tisefdrlal wkrnelkkqa rlf
//
LOCUS       NP_115580                757 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_115580
VERSION     NP_115580.2
DBSOURCE    REFSEQ: accession NM_032204.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 757)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 757)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 757)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 757)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 757)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 757)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 757)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP201867.1 and BC025368.2.
            
            On Apr 23, 2002 this sequence version replaced NP_115580.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025368.2, SRR1803613.190231.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307790.8/ ENSP00000305502.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..757
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 1"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=86230
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H1I8.3)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H1I8.3)"
     Region          469..508
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     Region          617..687
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1I8.3)"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H1I8.3)"
     Region          699..757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H1I8.3)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H1I8.3)"
     CDS             1..757
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_032204.5:115..2388"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13869.1"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mpalpldqlq ithkdpktgk lrtspalhpe qkadryfvly kpppkdnipa lveeylerat
       61 fvandldwll alphdkfwcq vifdetlqkc ldsylryvpr kfdegvasap evvdmqkrlh
      121 rsvfltflrm sthkeskdhf ispsafgeil ynnflfdipk ildlcvlfgk gnspllqkmi
      181 gniftqqpsy ysdldetlpt ilqvfsnilq hcglqgdgan ttpqkleerg rltpsdmpll
      241 elkdivlylc dtcttlwafl difplacqtf qkhdfcyrla sfyeaaipem esaikkrrle
      301 dskllgdlwq rlshsrkklm eifhiilnqi cllpilessc dniqgfieef lqifssllqe
      361 krflrdydal fpvaedisll qqassvldet rtayilqave sawegvdrrk atdakdpsvi
      421 eepngepngv tvtaeavsqa sshpenseee ecmgaaaavg pamcgvelds lisqvkdllp
      481 dlgegfilac leyyhydpeq vinnileerl aptlsqldrn ldremkpdpt plltsrhnvf
      541 qndefdvfsr dsvdlsrvhk gkstrkeent rsllndkrav aaqrqryeqy svvveevplq
      601 pgeslpyhsv yyedeyddty dgnqvganda dsddelisrr pftipqvlrt kvpregqeed
      661 dddeeddade eapkpdhfvq dpavlrekae arrmaflakk gyrhdsstav agsprghgqs
      721 rettqerrkk eankatranh nrrtmadrkr skgmips
//
LOCUS       NP_001354456             554 aa            linear   PRI 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 20 [Homo sapiens].
ACCESSION   NP_001354456 XP_005270256
VERSION     NP_001354456.1
DBSOURCE    REFSEQ: accession NM_001367527.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Miyauchi,M., Sasaki,K., Kagoya,Y., Taoka,K., Masamoto,Y.,
            Yamazaki,S., Arai,S., Mizuno,H. and Kurokawa,M.
  TITLE     CAMK2G is identified as a novel therapeutic target for
            myelofibrosis
  JOURNAL   Blood Adv 6 (5), 1585-1597 (2022)
   PUBMED   34521112
  REMARK    GeneRIF: CAMK2G is identified as a novel therapeutic target for
            myelofibrosis.
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_005270256.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.275052.1,
                                           SRR3476690.683250.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..554
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 20"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=61465
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          422..549
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..554
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367527.1:95..1759"
                     /note="isoform 20 is encoded by transcript variant 20"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kepqttvvhn
      361 atdgikgste scnttteded lkaaplrtgn gssvpegrss rdrtapsagm qpqpslcssa
      421 mrkqeiikit eqlieainng dfeaytkicd pgltsfepea lgnlvegmdf hkfyfenlls
      481 knskpihtti lnphvhvige daaciayirl tqyidgqgrp rtsqseetrv whrrdgkwln
      541 vhyhcsgapa aplq
//
LOCUS       NP_065939               1094 aa            linear   PRI 27-APR-2025
DEFINITION  NHS-like protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_065939 XP_036299
VERSION     NP_065939.2
DBSOURCE    REFSEQ: accession NM_020888.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Guo,Y., Tian,S., Li,H., Zuo,S., Yu,C. and Sun,C.
  TITLE     Transcription factor KLF9 inhibits the proliferation, invasion, and
            migration of pancreatic cancer cells by repressing KIAA1522
  JOURNAL   Asia Pac J Clin Oncol 20 (3), 423-432 (2024)
   PUBMED   38520660
  REMARK    GeneRIF: Transcription factor KLF9 inhibits the proliferation,
            invasion, and migration of pancreatic cancer cells by repressing
            KIAA1522.
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Palukuri,M.V., Patil,R.S. and Marcotte,E.M.
  TITLE     Molecular complex detection in protein interaction networks through
            reinforcement learning
  JOURNAL   BMC Bioinformatics 24 (1), 306 (2023)
   PUBMED   37532987
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Ou,M., Chu,Y., Zhang,Q., Zhao,H. and Song,Q.
  TITLE     HOXA cluster antisense RNA 2 elevates KIAA1522 expression through
            microRNA-520d-3p and insulin like growth factor 2 mRNA binding
            protein 3 to promote the growth of vascular smooth muscle cells in
            thoracic aortic aneurysm
  JOURNAL   ESC Heart Fail 9 (5), 2955-2966 (2022)
   PUBMED   35730141
  REMARK    GeneRIF: HOXA cluster antisense RNA 2 elevates KIAA1522 expression
            through microRNA-520d-3p and insulin like growth factor 2 mRNA
            binding protein 3 to promote the growth of vascular smooth muscle
            cells in thoracic aortic aneurysm.
REFERENCE   4  (residues 1 to 1094)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1094)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1094)
  AUTHORS   Wang,B., Jing,T., Jin,W., Chen,J., Wu,C., Wang,M. and Liu,Y.
  TITLE     KIAA1522 potentiates TNFalpha-NFkappaB signaling to antagonize
            platinum-based chemotherapy in lung adenocarcinoma
  JOURNAL   J Exp Clin Cancer Res 39 (1), 170 (2020)
   PUBMED   32854746
  REMARK    GeneRIF: KIAA1522 potentiates TNFalpha-NFkappaB signaling to
            antagonize platinum-based chemotherapy in lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1094)
  AUTHORS   Li,Y., Wang,Y., Fan,H., Zhang,Z. and Li,N.
  TITLE     miR-125b-5p inhibits breast cancer cell proliferation, migration
            and invasion by targeting KIAA1522
  JOURNAL   Biochem Biophys Res Commun 504 (1), 277-282 (2018)
   PUBMED   30177391
  REMARK    GeneRIF: miR-125b-5p functions as a tumor suppressor and regulates
            breast cancer cell progression through targeting KIAA1522
REFERENCE   8  (residues 1 to 1094)
  AUTHORS   Liu,Y.Z., Yang,H., Cao,J., Jiang,Y.Y., Hao,J.J., Xu,X., Cai,Y. and
            Wang,M.R.
  TITLE     KIAA1522 is a novel prognostic biomarker in patients with non-small
            cell lung cancer
  JOURNAL   Sci Rep 6, 24786 (2016)
   PUBMED   27098511
  REMARK    GeneRIF: high expression of KIAA1522 can be used as an independent
            biomarker for predication of poor survival and platinum-resistance
            of NSCLC patients, and aberrant KIAA1522 might be a new target for
            the therapy of the disease.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1094)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2, AI587184.1, AB040955.1 and AL713671.1.
            
            On Aug 18, 2006 this sequence version replaced NP_065939.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1966682,
                              SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000401073.7/ ENSP00000383851.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..1094
                     /product="NHS-like protein 3 isoform 1"
                     /note="NHS-like protein 3"
                     /calculated_mol_wt=112931
     Region          <783..1059
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1094
                     /gene="NHSL3"
                     /gene_synonym="KIAA1522"
                     /coded_by="NM_020888.3:126..3410"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41298.1"
                     /db_xref="GeneID:57648"
                     /db_xref="HGNC:HGNC:29301"
ORIGIN      
        1 maarappaap aaeepgnpgg pprrkksrsg asglrrafsw lrgkrrkkka agaegaepaa
       61 prakkaedka krakgkgrgs akaendkhls vgpgqgpgsa vdehqdnvff psgrpphlee
      121 lhtqaqeglr slqhqekqkl nkggwdhgdt qsiqssrtgp dednisfcsq ttsyvaesst
      181 aedalsirse miqrkgstfr phdsfpksgk sgrrrrerrs tvlglpqhvq kelglrnere
      241 apgtprapga rdavriptvd grprgtsgmg arvslqalea eaeagaetea mlqrhidrvy
      301 rddtfvgrst gtrappltrp mslavpgltg gagpaeplsp amsispqaty lskliphavl
      361 pptvdvvalg rcslrtlsrc slhsaspasv rslgrfssvs spqprsrhps sssdtwshsq
      421 ssdtivsdgs tlsskggseg qpesstasns vvpppqggsg rgspsggsta easdtlsirs
      481 sgqlsgrsvs lrklkrpppp prrthslhqr glavpdgplg lppkperkqq pqlprppttg
      541 gsegagaapc ppnpanswvp glspggsrrp prspertlsp ssgyssqsgt ptlppkglag
      601 ppaspgkaqp pkpervtslr spgasvsssl tslcssssdp apsdrsgpqi ltplgdrfvi
      661 pphpkvpapf spppskprsp npaapalaap avvpgpvstt daspqspptp qttltplqes
      721 pviskdqspp pspppsyhpp ppptkkpevv veapsaseta eeplqdpnwp pppppapeeq
      781 dlsmadfppp eeaffsvasp epagpsgspe lvsspaasss satalqiqpp gspdpppapp
      841 apapassapg hvaklpqkep vgcskgggpp redvgaplvt psllqmvrlr svgapggapt
      901 palgpsapqk plrralsgra spvpapssgl haavrlkacs laaseglssa qpngppeaep
      961 rppqspasta sfifskgsrk lqlerpvspe tqadlqrnlv aelrsiseqr ppqapkkspk
     1021 apppvarkps vgvpppasps ypraepltap ptnglphtqd rtkrelaeng gvlqlvgpee
     1081 kmglpgsdsq kela
//
LOCUS       NP_081667                285 aa            linear   ROD 27-APR-2025
DEFINITION  iodotyrosine deiodinase 1 [Mus musculus].
ACCESSION   NP_081667
VERSION     NP_081667.1
DBSOURCE    REFSEQ: accession NM_027391.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Phatarphekar,A., Buss,J.M. and Rokita,S.E.
  TITLE     Iodotyrosine deiodinase: a unique flavoprotein present in organisms
            of diverse phyla
  JOURNAL   Mol Biosyst 10 (1), 86-92 (2014)
   PUBMED   24153409
  REMARK    GeneRIF: At least for Metazoa, IYD should provide a new marker for
            tracing the evolutionary development of iodinated amino acids as
            regulatory signals through the tree of life.
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Afink,G.B., Veenboer,G., de Randamie,J., Keijser,R., Meischl,C.,
            Niessen,H. and Ris-Stalpers,C.
  TITLE     Initial characterization of C16orf89, a novel thyroid-specific gene
  JOURNAL   Thyroid 20 (7), 811-821 (2010)
   PUBMED   20578903
REFERENCE   4  (residues 1 to 285)
  AUTHORS   McTamney,P.M. and Rokita,S.E.
  TITLE     A mammalian reductive deiodinase has broad power to dehalogenate
            chlorinated and brominated substrates
  JOURNAL   J Am Chem Soc 131 (40), 14212-14213 (2009)
   PUBMED   19777994
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Thomas,S.R., McTamney,P.M., Adler,J.M., Laronde-Leblanc,N. and
            Rokita,S.E.
  TITLE     Crystal structure of iodotyrosine deiodinase, a novel flavoprotein
            responsible for iodide salvage in thyroid glands
  JOURNAL   J Biol Chem 284 (29), 19659-19667 (2009)
   PUBMED   19436071
  REMARK    GeneRIF: Data show that the structures provide a molecular basis
            for understanding thyroid disease based on mutations of IYD.
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Friedman,J.E., Watson,J.A. Jr., Lam,D.W. and Rokita,S.E.
  TITLE     Iodotyrosine deiodinase is the first mammalian member of the NADH
            oxidase/flavin reductase superfamily
  JOURNAL   J Biol Chem 281 (5), 2812-2819 (2006)
   PUBMED   16316988
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC155833.10 and AC153571.14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC023358.1, AK002363.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849376, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 2.06 cM"
     Protein         1..285
                     /product="iodotyrosine deiodinase 1"
                     /EC_number="1.21.1.1"
                     /note="iodotyrosine dehalogenase 1 protein"
                     /calculated_mol_wt=32683
     Site            1..21
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DCX8.1)"
     Region          89..281
                     /region_name="iodotyrosine_dehalogenase"
                     /note="iodotyrosine dehalogenase; cd02144"
                     /db_xref="CDD:380320"
     Site            order(89..90,93..99,108..111,113..118,122..123,127..138,
                     141,193,208,210..211,214..215,217..219,221..223,225..230,
                     233,235..236,247..249,256..257,263..264,272..278,280..281)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380320"
     Site            order(96..98,100,123..127,208,211..212,215,232..235,257,
                     273,275)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380320"
     CDS             1..285
                     /gene="Iyd"
                     /gene_synonym="0610009A07Rik; Dehal1; IYD-1"
                     /coded_by="NM_027391.4:23..880"
                     /db_xref="CCDS:CCDS56670.1"
                     /db_xref="GeneID:70337"
                     /db_xref="MGI:MGI:1917587"
ORIGIN      
        1 mflltpvlva vvcilvvwvf knadrnlekk keeaqvqpwv dedlkdsted lqveedaeew
       61 qeaeesvehi pfshtrypeq emrmrsqefy ellnkrrsvr fissehvpme vienvikaag
      121 tapsgahtep wtfvvvkdpd mkhkireiie eeeeinymkr mgkrwvtdlk klrtnwikey
      181 ldtapvlili fkqvhgfaan gkkkvhyyne isvsiacgll laalqnaglv tvtttplncg
      241 prlrvllgrp shekllvllp vgypsrdatv pdlkrkaldq imvtv
//
LOCUS       NP_694574                896 aa            linear   PRI 27-APR-2025
DEFINITION  NEDD4-binding protein 1 [Homo sapiens].
ACCESSION   NP_694574
VERSION     NP_694574.3
DBSOURCE    REFSEQ: accession NM_153029.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 896)
  AUTHORS   Wu,C., Guo,X., Zheng,W., Sun,R., Chen,L., Shen,Y., Chen,M.,
            Song,Y., Mao,R., Chen,X. and Fan,Y.
  TITLE     N4BP1 regulates keratinocytes development and plays protective role
            in burn- and adhesive-related skin injury via MMP9
  JOURNAL   Cell Signal 110, 110850 (2023)
   PUBMED   37579928
  REMARK    GeneRIF: N4BP1 regulates keratinocytes development and plays
            protective role in burn- and adhesive-related skin injury via MMP9.
REFERENCE   2  (residues 1 to 896)
  AUTHORS   Zhao,D., Wang,C., Liu,X., Liu,N., Zhuang,S., Zhang,Q., Bao,X.,
            Xu,S., Zhou,X., Meng,Q., Li,S. and Tang,L.
  TITLE     CircN4bp1 Facilitates Sepsis-Induced Acute Respiratory Distress
            Syndrome through Mediating Macrophage Polarization via the
            miR-138-5p/EZH2 Axis
  JOURNAL   Mediators Inflamm 2021, 7858746 (2021)
   PUBMED   35002536
  REMARK    GeneRIF: CircN4bp1 Facilitates Sepsis-Induced Acute Respiratory
            Distress Syndrome through Mediating Macrophage Polarization via the
            miR-138-5p/EZH2 Axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 896)
  AUTHORS   Gitlin,A.D., Heger,K., Schubert,A.F., Reja,R., Yan,D., Pham,V.C.,
            Suto,E., Zhang,J., Kwon,Y.C., Freund,E.C., Kang,J., Pham,A.,
            Caothien,R., Bacarro,N., Hinkle,T., Xu,M., McKenzie,B.S., Haley,B.,
            Lee,W.P., Lill,J.R., Roose-Girma,M., Dohse,M., Webster,J.D.,
            Newton,K. and Dixit,V.M.
  TITLE     Integration of innate immune signalling by caspase-8 cleavage of
            N4BP1
  JOURNAL   Nature 587 (7833), 275-280 (2020)
   PUBMED   32971525
  REMARK    GeneRIF: Integration of innate immune signalling by caspase-8
            cleavage of N4BP1.
REFERENCE   4  (residues 1 to 896)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 896)
  AUTHORS   Nepravishta,R., Ferrentino,F., Mandaliti,W., Mattioni,A., Weber,J.,
            Polo,S., Castagnoli,L., Cesareni,G., Paci,M. and Santonico,E.
  TITLE     CoCUN, a Novel Ubiquitin Binding Domain Identified in N4BP1
  JOURNAL   Biomolecules 9 (7), 284 (2019)
   PUBMED   31319543
  REMARK    Erratum:[Biomolecules. 2019 Nov 28;9(12):E803. doi:
            10.3390/biom9120803. PMID: 31795258]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 896)
  AUTHORS   Li,S., Wang,L., Berman,M., Kong,Y.Y. and Dorf,M.E.
  TITLE     Mapping a dynamic innate immunity protein interaction network
            regulating type I interferon production
  JOURNAL   Immunity 35 (3), 426-440 (2011)
   PUBMED   21903422
  REMARK    Erratum:[Immunity. 2011 Oct 28;35(4):647-8]
REFERENCE   7  (residues 1 to 896)
  AUTHORS   Enjuanes,A., Benavente,Y., Bosch,F., Martin-Guerrero,I.,
            Colomer,D., Perez-Alvarez,S., Reina,O., Ardanaz,M.T., Jares,P.,
            Garcia-Orad,A., Pujana,M.A., Montserrat,E., de Sanjose,S. and
            Campo,E.
  TITLE     Genetic variants in apoptosis and immunoregulation-related genes
            are associated with risk of chronic lymphocytic leukemia
  JOURNAL   Cancer Res 68 (24), 10178-10186 (2008)
   PUBMED   19074885
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 896)
  AUTHORS   Oberst,A., Malatesta,M., Aqeilan,R.I., Rossi,M., Salomoni,P.,
            Murillas,R., Sharma,P., Kuehn,M.R., Oren,M., Croce,C.M.,
            Bernassola,F. and Melino,G.
  TITLE     The Nedd4-binding partner 1 (N4BP1) protein is an inhibitor of the
            E3 ligase Itch
  JOURNAL   Proc Natl Acad Sci U S A 104 (27), 11280-11285 (2007)
   PUBMED   17592138
REFERENCE   9  (residues 1 to 896)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
REFERENCE   10 (residues 1 to 896)
  AUTHORS   Murillas,R., Simms,K.S., Hatakeyama,S., Weissman,A.M. and
            Kuehn,M.R.
  TITLE     Identification of developmentally expressed proteins that
            functionally interact with Nedd4 ubiquitin ligase
  JOURNAL   J Biol Chem 277 (4), 2897-2907 (2002)
   PUBMED   11717310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB014515.1, BC051897.1, AK026937.1, AK124782.1, AK056383.1 and
            AL831882.1.
            
            On Jun 18, 2004 this sequence version replaced NP_694574.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.845067.1, BC152472.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262384.4/ ENSP00000262384.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..896
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.1"
     Protein         1..896
                     /product="NEDD4-binding protein 1"
                     /calculated_mol_wt=100248
     Region          8..73
                     /region_name="KH-I_N4BP1_like_rpt1"
                     /note="first type I K homology (KH) RNA-binding domain
                     found in the family of NEDD4-binding protein 1 (N4BP1);
                     cd09032"
                     /db_xref="CDD:411808"
     Region          75..142
                     /region_name="KH-I_N4BP1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     NEDD4-binding protein 1 (N4BP1) and similar proteins;
                     cd22476"
                     /db_xref="CDD:411904"
     Site            order(86,88..90,92..96,99..100,103..104,109..112)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411904"
     Site            200..201
                     /site_type="cleavage"
                     /note="Cleavage, by CASP8.
                     /evidence=ECO:0000250|UniProtKB:Q6A037; propagated from
                     UniProtKB/Swiss-Prot (O75113.4)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75113.4)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75113.4)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O75113.4)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75113.4)"
     Site            326..327
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250|UniProtKB:Q6A037;
                     propagated from UniProtKB/Swiss-Prot (O75113.4)"
     Region          403..430
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75113.4)"
     Region          488..507
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75113.4)"
     Site            490..491
                     /site_type="cleavage"
                     /note="Cleavage, by CASP8.
                     /evidence=ECO:0000250|UniProtKB:Q6A037; propagated from
                     UniProtKB/Swiss-Prot (O75113.4)"
     Site            509..510
                     /site_type="cleavage"
                     /note="Cleavage, by MALT1.
                     /evidence=ECO:0000269|PubMed:31133753; propagated from
                     UniProtKB/Swiss-Prot (O75113.4)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6A037; propagated from
                     UniProtKB/Swiss-Prot (O75113.4)"
     Region          620..746
                     /region_name="PIN_N4BP1-like"
                     /note="PRORP-like PIN domain of NEDD4 binding protein 1
                     and related proteins; cd18728"
                     /db_xref="CDD:350295"
     Region          801..821
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75113.4)"
     Region          849..896
                     /region_name="CoCUN.
                     /evidence=ECO:0000305|PubMed:31319543"
                     /note="propagated from UniProtKB/Swiss-Prot (O75113.4)"
     CDS             1..896
                     /gene="N4BP1"
                     /coded_by="NM_153029.4:209..2899"
                     /db_xref="CCDS:CCDS45479.1"
                     /db_xref="GeneID:9683"
                     /db_xref="HGNC:HGNC:29850"
                     /db_xref="MIM:619138"
ORIGIN      
        1 maaravldef tapaekaell eqsrgriegl fgvslavlga lgaeeplpar iwlqlcgaqe
       61 avhsakeyik gicepeleer ecypkdmhci fvgaeslflk sliqdtcadl cildigllgi
      121 rgsaeavvma rshiqqfvkl fenkenlpss qkesevkref kqfveahadn ytmdllilpt
      181 slkkelltlt qgeenlfetg ddeviemrds qqteftqnaa tglnisrdet vlqeearnka
      241 gtpvseltkq mdtvlssspd vlfdpinglt pdeealsner icqkrrfsds eerhtkkqfs
      301 lenvqegeil hdaktlagnv iadlsdssad senlspdike tteemeynil vnffktmgys
      361 qeivekvikv ygpsteplll leeiekenkr fqedrefsag tvypetnktk nkgvysstne
      421 lttdstpkkt qahtqqnmve kfsqlpfkve akpctsncri ntfrtvpieq khevwgsnqn
      481 yicntdpetd glspsvasps pkevnfvsrg asshqprvpl fpenglhqqp epllpnnmks
      541 acekrlgccs sphskpncst lsppmplpql lpsvtdarsa gpsdhidssv tgvqrfrdtl
      601 kipyklelkn epgrtdlkhi vidgsnvait hglkkffscr giaiaveyfw klgnrnitvf
      661 vpqwrtrrdp nvteqhfltq lqelgilslt parmvfgeri ashddrfllh ladktggiiv
      721 tndnfrefvn esvswreiit krllqytfvg difmvpddpl grsgprleef lqkevclrdm
      781 qpllsalpnv gmfdpsfrvp gtqaastshq pptriqgaps shwlpqqphf pllpalpslq
      841 qnlpmpaqrs saetnelrea llkifpdseq rlkidqilva hpymkdlnal samvld
//
LOCUS       NP_001082709             216 aa            linear   VRT 27-APR-2025
DEFINITION  UMP-CMP kinase [Xenopus laevis].
ACCESSION   NP_001082709 NP_001082710
VERSION     NP_001082709.2
DBSOURCE    REFSEQ: accession NM_001089240.2
KEYWORDS    RefSeq.
SOURCE      Xenopus laevis (African clawed frog)
  ORGANISM  Xenopus laevis
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae;
            Xenopus; Xenopus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Klein,S.L., Strausberg,R.L., Wagner,L., Pontius,J., Clifton,S.W.
            and Richardson,P.
  TITLE     Genetic and genomic tools for Xenopus research: The NIH Xenopus
            initiative
  JOURNAL   Dev Dyn 225 (4), 384-391 (2002)
   PUBMED   12454917
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF615537.1 and BC045275.1.
            
            On Jan 10, 2019 this sequence version replaced NP_001082709.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00012418,
                              SAMD00012419 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Xenopus laevis"
                     /db_xref="taxon:8355"
                     /chromosome="4S"
                     /map="4S"
     Protein         1..216
                     /product="UMP-CMP kinase"
                     /EC_number="2.7.4.6"
                     /EC_number="2.7.4.14"
                     /note="UMP-CMP kinase 1; cytidylate kinase; uridine
                     monophosphate kinase; cytidine monophosphate (UMP-CMP)
                     kinase 1, cytosolic L homeolog; cytidine monophosphate
                     kinase"
                     /calculated_mol_wt=24669
     Region          28..216
                     /region_name="UMP_CMP_kin_fam"
                     /note="UMP-CMP kinase family; TIGR01359"
                     /db_xref="CDD:273576"
     CDS             1..216
                     /gene="cmpk1.S"
                     /gene_synonym="CK; cmpk; cmpk1; cmpk1.L"
                     /coded_by="NM_001089240.2:83..733"
                     /db_xref="GeneID:398670"
                     /db_xref="Xenbase:XB-GENE-980044"
ORIGIN      
        1 mlyrllktlp rvsaasfhcv rhimkplvvf vlggpgagkg tqcerivqky gythlsagdl
       61 lrderkkpds qygeliesyi rdgkivpvei tisllqrame rtmafdankh kflidgfprn
      121 ednlqgwert mngkadvsfv lffdcdnetc ierclergks sgrsddnres lekriqtylq
      181 strpiidlye krgkvrkvda sksvdevftk vqnifd
//
LOCUS       NP_848659                501 aa            linear   PRI 27-APR-2025
DEFINITION  nuclear receptor-binding protein 2 [Homo sapiens].
ACCESSION   NP_848659
VERSION     NP_848659.2
DBSOURCE    REFSEQ: accession NM_178564.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Chi,F., Jin,X., Chen,L., He,G. and Han,S.
  TITLE     TRG16, targeted by miR-765, inhibits breast cancer stem cell-like
            properties via regulating the NF-kappaB pathway
  JOURNAL   Mol Cell Biochem 477 (12), 2801-2816 (2022)
   PUBMED   35648115
  REMARK    GeneRIF: TRG16, targeted by miR-765, inhibits breast cancer stem
            cell-like properties via regulating the NF-kappaB pathway.
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Gil-Cayuela,C., Lopez,A., Martinez-Dolz,L., Gonzalez-Juanatey,J.R.,
            Lago,F., Rosello-Lleti,E., Rivera,M. and Portoles,M.
  TITLE     The altered expression of autophagy-related genes participates in
            heart failure: NRBP2 and CALCOCO2 are associated with left
            ventricular dysfunction parameters in human dilated cardiomyopathy
  JOURNAL   PLoS One 14 (4), e0215818 (2019)
   PUBMED   31009519
  REMARK    GeneRIF: The altered expression of NRBP2 and CALCOCO2 is associated
            with left ventricular dysfunction parameters in human dilated
            cardiomyopathy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 501)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Larsson,J., Forsberg,M., Brannvall,K., Zhang,X.Q., Enarsson,M.,
            Hedborg,F. and Forsberg-Nilsson,K.
  TITLE     Nuclear receptor binding protein 2 is induced during neural
            progenitor differentiation and affects cell survival
  JOURNAL   Mol Cell Neurosci 39 (1), 32-39 (2008)
   PUBMED   18619852
  REMARK    GeneRIF: Data show that NRBP2 protein levels increase as neural
            progenitor cells differentiate, and its down regulation renders
            neural progenitor cells more vulnerable to apoptosis, which suggest
            a role in stem cell survival.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK293943.1, BC071605.1, AI094905.1 and AC234917.3.
            
            On May 18, 2010 this sequence version replaced NP_848659.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.222364.1,
                                           SRR3476690.1010888.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000442628.7/ ENSP00000414055.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..501
                     /product="nuclear receptor-binding protein 2"
                     /note="transformation-related protein 16"
                     /calculated_mol_wt=57672
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSY0.2)"
     Region          46..307
                     /region_name="PK_MADML"
                     /note="Pseudokinase domain of MLF1-ADaptor Molecule-Like;
                     cd14035"
                     /db_xref="CDD:270937"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q91V36; propagated from
                     UniProtKB/Swiss-Prot (Q9NSY0.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NSY0.2)"
     CDS             1..501
                     /gene="NRBP2"
                     /gene_synonym="pp9320; TRG16"
                     /coded_by="NM_178564.4:140..1645"
                     /db_xref="CCDS:CCDS34959.2"
                     /db_xref="GeneID:340371"
                     /db_xref="HGNC:HGNC:19339"
                     /db_xref="MIM:615563"
ORIGIN      
        1 maapepaprr arererered esedesdile espcgrwqkr reqvnqgnmp glqstflamd
       61 teegvevvwn elhfgdrkaf aaheekiqtv feqlvlvdhp nivklhkywl dtseacarvi
      121 fiteyvssgs lkqflkktkk nhkamnaraw krwctqilsa lsflhacspp iihgnltsdt
      181 ifiqhnglik igsvwhrifs nalpddlrsp iraereelrn lhffppeyge vadgtavdif
      241 sfgmcalema vleiqtngdt rvteeaiara rhslsdpnmr efilcclard parrpsahsl
      301 lfhrvlfevh slkllaahcf iqhqylmpen vveektkamd lhavlaelpr prrpplqwry
      361 sevsfmeldk fledvrngiy plmnfaatrp lglprvlapp peevqkaktp tpepfdsetr
      421 kviqmqcnle rsedkarwhl tlllvledrl hrqltydllp tdsaqdlase lvhygflhed
      481 drmklaafle stflkyrgtq a
//
LOCUS       NP_056508                942 aa            linear   PRI 27-APR-2025
DEFINITION  protein inturned [Homo sapiens].
ACCESSION   NP_056508 XP_371707
VERSION     NP_056508.2
DBSOURCE    REFSEQ: accession NM_015693.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Wang,S., Liu,A., Su,Y. and Dong,Z.
  TITLE     Deficiency of the Planar Cell Polarity Protein Intu Delays Kidney
            Repair and Suppresses Renal Fibrosis after Acute Kidney Injury
  JOURNAL   Am J Pathol 193 (3), 275-285 (2023)
   PUBMED   36586478
  REMARK    GeneRIF: Deficiency of the Planar Cell Polarity Protein Intu Delays
            Kidney Repair and Suppresses Renal Fibrosis after Acute Kidney
            Injury.
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Chan,H.Y.E. and Chen,Z.S.
  TITLE     Multifaceted investigation underlies diverse mechanisms
            contributing to the downregulation of Hedgehog pathway-associated
            genes INTU and IFT88 in lung adenocarcinoma and uterine corpus
            endometrial carcinoma
  JOURNAL   Aging (Albany NY) 14 (19), 7794-7823 (2022)
   PUBMED   36084949
  REMARK    GeneRIF: Multifaceted investigation underlies diverse mechanisms
            contributing to the downregulation of Hedgehog pathway-associated
            genes INTU and IFT88 in lung adenocarcinoma and uterine corpus
            endometrial carcinoma.
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 942)
  AUTHORS   Chou,Y.C., Chen,M.J., Chen,P.H., Chang,C.W., Yu,M.H., Chen,Y.J.,
            Tsai,E.M., Tsai,S.F., Kuo,W.S. and Tzeng,C.R.
  TITLE     Integration of genome-wide association study and expression
            quantitative trait locus mapping for identification of
            endometriosis-associated genes
  JOURNAL   Sci Rep 11 (1), 478 (2021)
   PUBMED   33436679
  REMARK    GeneRIF: Integration of genome-wide association study and
            expression quantitative trait locus mapping for identification of
            endometriosis-associated genes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 942)
  AUTHORS   Toriyama,M., Lee,C., Taylor,S.P., Duran,I., Cohn,D.H., Bruel,A.L.,
            Tabler,J.M., Drew,K., Kelly,M.R., Kim,S., Park,T.J., Braun,D.A.,
            Pierquin,G., Biver,A., Wagner,K., Malfroot,A., Panigrahi,I.,
            Franco,B., Al-Lami,H.A., Yeung,Y., Choi,Y.J., Duffourd,Y.,
            Faivre,L., Riviere,J.B., Chen,J., Liu,K.J., Marcotte,E.M.,
            Hildebrandt,F., Thauvin-Robinet,C., Krakow,D., Jackson,P.K. and
            Wallingford,J.B.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     The ciliopathy-associated CPLANE proteins direct basal body
            recruitment of intraflagellar transport machinery
  JOURNAL   Nat Genet 48 (6), 648-656 (2016)
   PUBMED   27158779
  REMARK    Erratum:[Nat Genet. 2016 Jul 27;48(8):970. doi:
            10.1038/ng0816-970b. PMID: 27463398]
REFERENCE   6  (residues 1 to 942)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 942)
  AUTHORS   Yasunaga,T., Hoff,S., Schell,C., Helmstadter,M., Kretz,O.,
            Kuechlin,S., Yakulov,T.A., Engel,C., Muller,B., Bensch,R.,
            Ronneberger,O., Huber,T.B., Lienkamp,S.S. and Walz,G.
  TITLE     The polarity protein Inturned links NPHP4 to Daam1 to control the
            subapical actin network in multiciliated cells
  JOURNAL   J Cell Biol 211 (5), 963-973 (2015)
   PUBMED   26644512
REFERENCE   8  (residues 1 to 942)
  AUTHORS   Al-Balool,H.H., Weber,D., Liu,Y., Wade,M., Guleria,K., Nam,P.L.,
            Clayton,J., Rowe,W., Coxhead,J., Irving,J., Elliott,D.J.,
            Hall,A.G., Santibanez-Koref,M. and Jackson,M.S.
  TITLE     Post-transcriptional exon shuffling events in humans can be
            evolutionarily conserved and abundant
  JOURNAL   Genome Res 21 (11), 1788-1799 (2011)
   PUBMED   21948523
REFERENCE   9  (residues 1 to 942)
  AUTHORS   Heydeck,W. and Liu,A.
  TITLE     PCP effector proteins inturned and fuzzy play nonredundant roles in
            the patterning but not convergent extension of mammalian neural
            tube
  JOURNAL   Dev Dyn 240 (8), 1938-1948 (2011)
   PUBMED   21761479
REFERENCE   10 (residues 1 to 942)
  AUTHORS   Park,T.J., Haigo,S.L. and Wallingford,J.B.
  TITLE     Ciliogenesis defects in embryos lacking inturned or fuzzy function
            are associated with failure of planar cell polarity and Hedgehog
            signaling
  JOURNAL   Nat Genet 38 (3), 303-311 (2006)
   PUBMED   16493421
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB195553.1, BC130611.1, DB302901.1 and AC093591.3.
            
            On or before Mar 22, 2004 this sequence version replaced
            XP_371707.1, NP_056508.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.73433.1, AB033110.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335251.11/ ENSP00000334003.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.1"
     Protein         1..942
                     /product="protein inturned"
                     /note="PDZ domain containing 6; PDZ domain-containing
                     protein 6; inturned planar cell polarity effector homolog;
                     ciliogenesis and planar polarity effector 4; ciliogenesis
                     and planar polarity effector complex subunit 4"
                     /calculated_mol_wt=105518
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULD6.2)"
     Region          202..271
                     /region_name="cpPDZ_Deg_HtrA-like"
                     /note="permuted PDZ domain of Deg/high-temperature
                     requirement factor A (HtrA) family of housekeeping serine
                     proteases and related domains; cl49614"
                     /db_xref="CDD:483954"
     Region          306..416
                     /region_name="Intu_longin_1"
                     /note="First Longin domain of INTU, CCZ1 and HPS4;
                     pfam19031"
                     /db_xref="CDD:436911"
     Region          514..633
                     /region_name="Intu_longin_2"
                     /note="Intu longin-like domain 2; pfam19032"
                     /db_xref="CDD:465951"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D4ACE5; propagated from
                     UniProtKB/Swiss-Prot (Q9ULD6.2)"
     Site            674
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULD6.2)"
     Region          704..754
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULD6.2)"
     Region          796..936
                     /region_name="Intu_longin_3"
                     /note="Intu longin-like domain 3; pfam19033"
                     /db_xref="CDD:436913"
     CDS             1..942
                     /gene="INTU"
                     /gene_synonym="CPLANE4; INT; OFD17; PDZD6; PDZK6; SRTD20"
                     /coded_by="NM_015693.4:79..2907"
                     /db_xref="CCDS:CCDS34061.1"
                     /db_xref="GeneID:27152"
                     /db_xref="HGNC:HGNC:29239"
                     /db_xref="MIM:610621"
ORIGIN      
        1 masvascdsr pssdelpgdp ssqeededyd fedrvsdsgs yssassdydd lepewldsvq
       61 kngelfylel sedeeesllp etptvnhvrf seneiiiedd ykerkkyepk lkqftkilrr
      121 krllpkrcnk knsndngpvs ilkhqsnqkt gvivqqrykd vnvyvnpkkl tvikakeqlk
      181 llevlvgiih qtkwswrrtg kqgdgerlvv hgllpggsam ksgqvligdv lvavndvdvt
      241 teniervlsc ipgpmqvklt fenaydvkre tshprqkktq sntsdlvkll wgeevegiqq
      301 sglntphiim yltlqldset skeeqeilyh ypmseasqkl ksvrgifltl cdmlenvtgt
      361 qvtsssllln gkqihvaywk esdkllligl paeevplprl rnmienviqt lkfmygslds
      421 afcqienvpr ldhffnlffq ralqpaklhs saspsaqqyd assavlldnl pgvrwltlpl
      481 eikmeldmal sdleaadfae lsedyydmrr lytilgsslf ykgylicshl pkddlidiav
      541 ycrhycllpl aakqrigqli iwrevfpqhh lrpladsste vfpepegryf llvvglkhym
      601 lcvlleaggc askaigspgp dcvyvdqvkt tlhqldgvds riderlassp vpclscadwf
      661 ltgsrektds lttspilsrl qgtskvatsp tcrrtlfgdy slktrkpsps cssggsdngc
      721 eggeddgfsp httpdavrkq resqgsdgle esgtllkvtk kkstlpnpfh lgnlkkdlpe
      781 keleiyntvk ltsgpentlf hyvaletvqg ifitptleev aqlsgsihpq liknfhqccl
      841 siravfqqtl veekkkglns gdhsdsaksv sslnpvkehg vlfecspgnw tdqkkappvm
      901 aywvvgrlfl hpkpqelyvc fhdsvteiai eiafklffgl tl
//
LOCUS       NP_543023                664 aa            linear   PRI 27-APR-2025
DEFINITION  RBBP8 N-terminal-like protein [Homo sapiens].
ACCESSION   NP_543023
VERSION     NP_543023.2
DBSOURCE    REFSEQ: accession NM_080833.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA871775.1, AK074919.1, AL121832.56 and BC033142.1.
            
            On Feb 5, 2010 this sequence version replaced NP_543023.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK074919.1, AK290299.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252998.2/ ENSP00000252998.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..664
                     /product="RBBP8 N-terminal-like protein"
                     /calculated_mol_wt=71301
     Region          4..123
                     /region_name="CtIP_N"
                     /note="Tumour-suppressor protein CtIP N-terminal domain;
                     pfam10482"
                     /db_xref="CDD:463107"
     Region          125..284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC74.3)"
     Region          <129..519
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          369..664
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC74.3)"
     CDS             1..664
                     /gene="RBBP8NL"
                     /gene_synonym="C20orf151"
                     /coded_by="NM_080833.3:164..2158"
                     /db_xref="CCDS:CCDS13498.1"
                     /db_xref="GeneID:140893"
                     /db_xref="HGNC:HGNC:16144"
ORIGIN      
        1 mesfmeslnr lkeihekevl glqnklleln sercrdaqri eelfsknhql reqqktlken
       61 lrvlenrlra glcdrcmvtq elarkrqqef esshlqnlqr ifiltnemng lkeenetlke
      121 evkrlrglgd rpkprakegt sdppsplllp spggwkaite kppggheeae edhqgvglrg
      181 eekpaghrts pvakispgat lpesrapdms pqrisnqlhg tiavvrpgsq acpadrgpan
      241 gtppplpars sppspayerg lsldsflras rpsamtheap klspkvdrlc llnrplslhl
      301 qsphssplap aaapsdprlq dlkareaeaw eeptellglp salagmqdlr legalhllla
      361 qqqlrarara gsvrprgqpt pgemlpslpv gsdsegpene gtraalaaag lsggrhtqpa
      421 gpgraqrtea aatqdcaldk pldlsewgra rgqdtpkpag qhgslspaaa htaspepptq
      481 sgpltrspqa lsngtkgtrv peqeeastpm dpsrplpgsq lslsspgste dedtgrplpp
      541 phpqppphpq ppdldghpep skaevlrpes deldetdtpg sevglssqae attsttgegp
      601 ecictqehgq gpprkrkras epgdkaskkp srgrrkltat egpgsprdae dhspspnssp
      661 weet
//
LOCUS       NP_666945                314 aa            linear   ROD 27-APR-2025
DEFINITION  olfactory receptor 5P6 [Mus musculus].
ACCESSION   NP_666945 XP_006507934
VERSION     NP_666945.1
DBSOURCE    REFSEQ: accession NM_146734.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Olender,T., Jones,T.E.M., Bruford,E. and Lancet,D.
  TITLE     A unified nomenclature for vertebrate olfactory receptors
  JOURNAL   BMC Evol Biol 20 (1), 42 (2020)
   PUBMED   32295537
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Young,J.M., Shykind,B.M., Lane,R.P., Tonnes-Priddy,L., Ross,J.A.,
            Walker,M., Williams,E.M. and Trask,B.J.
  TITLE     Odorant receptor expressed sequence tags demonstrate olfactory
            expression of over 400 genes, extensive alternate splicing and
            unequal expression levels
  JOURNAL   Genome Biol 4 (11), R71 (2003)
   PUBMED   14611657
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Young,J.M., Friedman,C., Williams,E.M., Ross,J.A., Tonnes-Priddy,L.
            and Trask,B.J.
  TITLE     Different evolutionary processes shaped the mouse and human
            olfactory receptor gene families
  JOURNAL   Hum Mol Genet 11 (5), 535-546 (2002)
   PUBMED   11875048
  REMARK    Erratum:[Hum Mol Genet. 2002 Jul 1;11(14):1683.]
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Zhang,X. and Firestein,S.
  TITLE     The olfactory receptor gene superfamily of the mouse
  JOURNAL   Nat Neurosci 5 (2), 124-133 (2002)
   PUBMED   11802173
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099573.15.
            
            On Apr 6, 2018 this sequence version replaced XP_006507934.1.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DR065530.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 57.21 cM"
     Protein         1..314
                     /product="olfactory receptor 5P6"
                     /note="olfactory receptor MOR204-13; olfactory receptor
                     204-13; olfactory receptor 478"
                     /calculated_mol_wt=34809
     Site            8
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VG04.1)"
     Region          28..306
                     /region_name="7tmA_OR5P-like"
                     /note="olfactory receptor subfamily 5P and related
                     proteins, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15416"
                     /db_xref="CDD:320538"
     Region          29..55
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320538"
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VG04.1)"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VG04.1)"
     Region          62..88
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320538"
     Site            order(84,87..88,100..105,107..108,111,156,158..162,198,
                     201..203,205..207,209..210,255,258..259,261..262,265,
                     271..272,274..276,279,282..283)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320538"
     Region          100..130
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320538"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VG04.1)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VG04.1)"
     Region          143..164
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320538"
     Region          198..228
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320538"
     Site            200..220
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VG04.1)"
     Region          235..265
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320538"
     Site            241..261
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VG04.1)"
     Region          272..297
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320538"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VG04.1)"
     CDS             1..314
                     /gene="Or5p6"
                     /gene_synonym="GA_x6K02T2PBJ9-10361879-10360935;
                     MOR204-13; Olfr478"
                     /coded_by="NM_146734.2:79..1023"
                     /db_xref="CCDS:CCDS21700.1"
                     /db_xref="GeneID:258729"
                     /db_xref="MGI:MGI:3030312"
ORIGIN      
        1 mafqedgnht avtefvlfgl tddpvlrvil fiiflciylv tvsgnlstil lirvssqlhh
       61 pmyfflshla fadigysssv tpnmlvnflv erhtisyigc aiqlgsvvff gssecfilaa
      121 maydrfmaic npllystkms tqvcvqllli ayiggflntw sfticfyslv fcgpngvnhf
      181 fcdfapliel scsdvsvpat vpsftagsii vvtviviais yiyilitilk mhstegrqka
      241 fstctshlta vtlfygtitf iyvmpkssfs tdqnkvvsvf ymvvipmlnp liyslrnnei
      301 kgalkrqigr kifs
//
LOCUS       NP_001049                407 aa            linear   PRI 27-APR-2025
DEFINITION  substance-P receptor isoform long [Homo sapiens].
ACCESSION   NP_001049
VERSION     NP_001049.1
DBSOURCE    REFSEQ: accession NM_001058.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Lambert,J., Petrovitch,D., Himes,K.P., Freiermuth,C.E., Braun,R.S.,
            Brown,J.L., Bischof,J.J., Lyons,M.S., Punches,B.E.,
            Littlefield,A.K., Kisor,D.F. and Sprague,J.E.
  TITLE     Association of genetic variants in CYP3A5, DRD2 and NK1R with
            opioid overdose
  JOURNAL   Chem Biol Interact 403, 111242 (2024)
   PUBMED   39265714
  REMARK    GeneRIF: Association of genetic variants in CYP3A5, DRD2 and NK1R
            with opioid overdose.
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Al-Keilani,M.S., Almomani,B.A., Jaradat,S.A., Al-Sawalha,N.A. and
            Qawasmeh,M.A.
  TITLE     Alpha Calcitonin Gene-related Peptide, Neuropeptide Y, and
            Substance P as Biomarkers for Diagnosis and Disease Activity and
            Severity in Multiple Sclerosis
  JOURNAL   CNS Neurol Disord Drug Targets 23 (4), 512-524 (2024)
   PUBMED   37013432
  REMARK    GeneRIF: Alpha Calcitonin Gene-related Peptide, Neuropeptide Y, and
            Substance P as Biomarkers for Diagnosis and Disease Activity and
            Severity in Multiple Sclerosis.
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Gao,X. and Bayraktutan,U.
  TITLE     TNF-alpha evokes blood-brain barrier dysfunction through activation
            of Rho-kinase and neurokinin 1 receptor
  JOURNAL   Immunobiology 228 (5), 152706 (2023)
   PUBMED   37454559
  REMARK    GeneRIF: TNF-alpha evokes blood-brain barrier dysfunction through
            activation of Rho-kinase and neurokinin 1 receptor.
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Rosso,P., Fico,E., Colafrancesco,S., Bellizzi,M.G., Priori,R.,
            Cerbelli,B., Leopizzi,M., Giordano,C., Greco,A., Tirassa,P.,
            Severini,C. and Fusconi,M.
  TITLE     Involvement of Substance P (SP) and Its Related NK1 Receptor in
            Primary Sjogren's Syndrome (pSS) Pathogenesis
  JOURNAL   Cells 12 (10), 1347 (2023)
   PUBMED   37408182
  REMARK    GeneRIF: Involvement of Substance P (SP) and Its Related NK1
            Receptor in Primary Sjogren's Syndrome (pSS) Pathogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Kokabi,F., Ebrahimi,S., Mirzavi,F., Ghiasi Nooghabi,N.,
            Hashemi,S.F. and Hashemy,S.I.
  TITLE     The neuropeptide substance P/neurokinin-1 receptor system and
            diabetes: From mechanism to therapy
  JOURNAL   Biofactors 49 (3), 534-559 (2023)
   PUBMED   36651605
  REMARK    GeneRIF: The neuropeptide substance P/neurokinin-1 receptor system
            and diabetes: From mechanism to therapy.
            Review article
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Fong,T.M., Huang,R.R. and Strader,C.D.
  TITLE     Localization of agonist and antagonist binding domains of the human
            neurokinin-1 receptor
  JOURNAL   J Biol Chem 267 (36), 25664-25667 (1992)
   PUBMED   1281469
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Fong,T.M., Yu,H., Huang,R.R. and Strader,C.D.
  TITLE     The extracellular domain of the neurokinin-1 receptor is required
            for high-affinity binding of peptides
  JOURNAL   Biochemistry 31 (47), 11806-11811 (1992)
   PUBMED   1280161
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Takahashi,K., Tanaka,A., Hara,M. and Nakanishi,S.
  TITLE     The primary structure and gene organization of human substance P
            and neuromedin K receptors
  JOURNAL   Eur J Biochem 204 (3), 1025-1033 (1992)
   PUBMED   1312928
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Walsh,D.A., Mapp,P.I., Wharton,J., Rutherford,R.A., Kidd,B.L.,
            Revell,P.A., Blake,D.R. and Polak,J.M.
  TITLE     Localisation and characterisation of substance P binding to human
            synovial tissue in rheumatoid arthritis
  JOURNAL   Ann Rheum Dis 51 (3), 313-317 (1992)
   PUBMED   1374227
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Fong,T.M., Anderson,S.A., Yu,H., Huang,R.R. and Strader,C.D.
  TITLE     Differential activation of intracellular effector by two isoforms
            of human neurokinin-1 receptor
  JOURNAL   Mol Pharmacol 41 (1), 24-30 (1992)
   PUBMED   1310144
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007681.3, DB203452.1,
            M74290.1, AC007400.4 and AW206679.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to a gene family of tachykinin
            receptors. These tachykinin receptors are characterized by
            interactions with G proteins and contain seven hydrophobic
            transmembrane regions. This gene encodes the receptor for the
            tachykinin substance P, also referred to as neurokinin 1. The
            encoded protein is also involved in the mediation of
            phosphatidylinositol metabolism of substance P. [provided by
            RefSeq, Sep 2008].
            
            Transcript Variant: This variant (long) represents the longer and
            predominant transcript and it encodes the longer protein (isoform
            long).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.36400.1, AK289765.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305249.10/ ENSP00000303522.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p12"
     Protein         1..407
                     /product="substance-P receptor isoform long"
                     /note="tachykinin receptor 1 (substance P receptor;
                     neurokinin-1 receptor); NK-1 receptor; NK-1R; neurokinin
                     receptor 1"
                     /calculated_mol_wt=46120
     Site            14
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25103.1)"
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25103.1)"
     Site            32..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          33..316
                     /region_name="7tmA_NK1R"
                     /note="neurokinin 1 receptor, member of the class A family
                     of seven-transmembrane G protein-coupled receptors;
                     cd16002"
                     /db_xref="CDD:320668"
     Region          34..60
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320668"
     Site            65..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          67..93
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320668"
     Site            order(89,92..93,105..110,112..113,116,159,161..165,193,
                     196..198,200..202,204..205,261,264..265,267..268,271,
                     283..284,286..288,291,294..295)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320668"
     Region          105..135
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320668"
     Site            107..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          146..167
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320668"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          193..222
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320668"
     Site            195..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          241..271
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320668"
     Site            249..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          284..309
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320668"
     Site            284..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          364..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     CDS             1..407
                     /gene="TACR1"
                     /gene_synonym="NK1R; NKIR; SPR; TAC1R"
                     /coded_by="NM_001058.4:587..1810"
                     /note="isoform long is encoded by transcript variant long"
                     /db_xref="CCDS:CCDS1958.1"
                     /db_xref="GeneID:6869"
                     /db_xref="HGNC:HGNC:11526"
                     /db_xref="MIM:162323"
ORIGIN      
        1 mdnvlpvdsd lspnistnts epnqfvqpaw qivlwaaayt vivvtsvvgn vvvmwiilah
       61 krmrtvtnyf lvnlafaeas maafntvvnf tyavhnewyy glfyckfhnf fpiaavfasi
      121 ysmtavafdr ymaiihplqp rlsatatkvv icviwvlall lafpqgyyst tetmpsrvvc
      181 miewpehpnk iyekvyhicv tvliyflpll vigyaytvvg itlwaseipg dssdryheqv
      241 sakrkvvkmm ivvvctfaic wlpfhiffll pyinpdlylk kfiqqvylai mwlamsstmy
      301 npiiycclnd rfrlgfkhaf rccpfisagd yeglemkstr ylqtqgsvyk vsrlettist
      361 vvgaheeepe dgpkatpssl dltsncssrs dsktmtesfs fssnvls
//
LOCUS       NP_945173                396 aa            linear   PRI 27-APR-2025
DEFINITION  calcium-responsive transactivator isoform 1 [Homo sapiens].
ACCESSION   NP_945173
VERSION     NP_945173.1
DBSOURCE    REFSEQ: accession NM_198935.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chen,C., Wang,J., Kang,M., Wu,P., Zhu,L., Fang,Y. and Xue,Y.
  TITLE     Identification of a novel MEF2C::SS18L1 fusion in childhood acute
            B-lymphoblastic leukemia
  JOURNAL   J Cancer Res Clin Oncol 150 (6), 314 (2024)
   PUBMED   38907739
  REMARK    GeneRIF: Identification of a novel MEF2C::SS18L1 fusion in
            childhood acute B-lymphoblastic leukemia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Min,S. and Park,M.S.
  TITLE     The SS18L1 gene rs2295207 polymorphisms in association with
            hepatocellular carcinoma
  JOURNAL   Asian J Surg 45 (10), 2125-2126 (2022)
   PUBMED   35584997
  REMARK    GeneRIF: The SS18L1 gene rs2295207 polymorphisms in association
            with hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Du,A., Li,L., Jiao,Z., Zhu,G., Peng,T. and Li,H.
  TITLE     Protein expression pattern of calcium-responsive transactivator in
            early postnatal and adult testes
  JOURNAL   Histochem Cell Biol 155 (4), 491-502 (2021)
   PUBMED   33398438
  REMARK    GeneRIF: Protein expression pattern of calcium-responsive
            transactivator in early postnatal and adult testes.
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Teyssou,E., Vandenberghe,N., Moigneu,C., Boillee,S., Couratier,P.,
            Meininger,V., Pradat,P.F., Salachas,F., Leguern,E. and
            Millecamps,S.
  TITLE     Genetic analysis of SS18L1 in French amyotrophic lateral sclerosis
  JOURNAL   Neurobiol Aging 35 (5), 1213 (2014)
   PUBMED   24360741
  REMARK    GeneRIF: Its mutation causes amyotrophic lateral sclerosis.
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Pradhan,A. and Liu,Y.
  TITLE     A multifunctional domain of the calcium-responsive transactivator
            (CREST) that inhibits dendritic growth in cultured neurons
  JOURNAL   J Biol Chem 280 (26), 24738-24743 (2005)
   PUBMED   15866867
  REMARK    GeneRIF: analysis of the CREST domain that inhibits dendritic
            growth in cultured neurons
REFERENCE   8  (residues 1 to 396)
  AUTHORS   Aizawa,H., Hu,S.C., Bobb,K., Balakrishnan,K., Ince,G., Gurevich,I.,
            Cowan,M. and Ghosh,A.
  TITLE     Dendrite development regulated by CREST, a calcium-regulated
            transcriptional activator
  JOURNAL   Science 303 (5655), 197-202 (2004)
   PUBMED   14716005
REFERENCE   9  (residues 1 to 396)
  AUTHORS   Storlazzi,C.T., Mertens,F., Mandahl,N., Gisselsson,D., Isaksson,M.,
            Gustafson,P., Domanski,H.A. and Panagopoulos,I.
  TITLE     A novel fusion gene, SS18L1/SSX1, in synovial sarcoma
  JOURNAL   Genes Chromosomes Cancer 37 (2), 195-200 (2003)
   PUBMED   12696068
  REMARK    GeneRIF: A synovial sarcoma of classic morphology contained a novel
            t(20;X) SS18L1(strong homology to SS18 on Ch20)/SSX1 fusion
            transcript in which nucleotide 1216 (exon 10) of SS18L1 was fused
            in-frame with nucleotide 422 (exon 6) of SSX1.
REFERENCE   10 (residues 1 to 396)
  AUTHORS   de Bruijn,D.R., Kater-Baats,E., Eleveld,M., Merkx,G. and Geurts Van
            Kessel,A.
  TITLE     Mapping and characterization of the mouse and human SS18 genes, two
            human SS18-like genes and a mouse Ss18 pseudogene
  JOURNAL   Cytogenet Cell Genet 92 (3-4), 310-319 (2001)
   PUBMED   11435705
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC375156.1, AB014593.1,
            BX640848.1 and AL078633.32.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a calcium-responsive transactivator
            which is an essential subunit of a neuron-specific
            chromatin-remodeling complex. The structure of this gene is similar
            to that of the SS18 gene. Mutations in this gene are involved in
            amyotrophic lateral sclerosis (ALS). Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Sep 2014].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.90635.1, AB014593.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331758.8/ ENSP00000333012.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..396
                     /product="calcium-responsive transactivator isoform 1"
                     /note="calcium-responsive transactivator; SS18-like
                     protein 1; SYT homolog 1; SS18L1, nBAF chromatin
                     remodeling complex subunit; synovial sarcoma translocation
                     gene on chromosome 18-like 1"
                     /calculated_mol_wt=42859
     Region          1..148
                     /region_name="N-terminal auto-inhibitory domain, necessary
                     for interaction with SMARCA4/BRG1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          14..73
                     /region_name="SSXT"
                     /note="SSXT protein (N-terminal region); pfam05030"
                     /db_xref="CDD:428268"
     Region          50..53
                     /region_name="SH2-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          72..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          149..232
                     /region_name="Methionine-rich intra-molecular domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          192..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          246..317
                     /region_name="MFD domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          311..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          334..396
                     /region_name="Necessary for nuclear localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          353..356
                     /region_name="SH2-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          371..379
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          387..396
                     /region_name="Necessary for interaction with CREBBP and
                     for the recruitment of CREBBP to the nuclear bodies.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     Region          391..394
                     /region_name="SH2-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75177.2)"
     CDS             1..396
                     /gene="SS18L1"
                     /gene_synonym="CREST; LP2261; SMARCL2"
                     /coded_by="NM_198935.3:53..1243"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13491.1"
                     /db_xref="GeneID:26039"
                     /db_xref="HGNC:HGNC:15592"
                     /db_xref="MIM:606472"
ORIGIN      
        1 msvafasarp rgkgevtqqt iqkmldenhh liqcileyqs kgktaectqy qqilhrnlvy
       61 latiadsnqn mqsllpappt qnmnlgpgal tqsgssqglh sqgslsdais tglppssllq
      121 gqigngpshv smqqtapntl pttsmsisgp gyshagpasq gvpmqgqgti gnyvsrtnin
      181 mqsnpvsmmq qqaatshyss aqggsqhyqg qssiammgqg sqgssmmgqr pmapyrpsqq
      241 gssqqylgqe eyygeqyshs qgaaepmgqq yypdghgdya yqqssyteqs ydrsfeestq
      301 hyyeggnsqy sqqqagyqqg aaqqqtysqq qypsqqsypg qqqgygsaqg apsqypgyqq
      361 gqgqqygsyr apqtapsaqq qrpygyeqgq ygnyqq
//
LOCUS       NP_001357384             111 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 577 isoform c [Homo sapiens].
ACCESSION   NP_001357384
VERSION     NP_001357384.1
DBSOURCE    REFSEQ: accession NM_001370455.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Lorenzo,P.M., Izquierdo,A.G., Diaz-Lagares,A., Carreira,M.C.,
            Macias-Gonzalez,M., Sandoval,J., Cueva,J., Lopez-Lopez,R.,
            Casanueva,F.F. and Crujeiras,A.B.
  TITLE     ZNF577 Methylation Levels in Leukocytes From Women With Breast
            Cancer Is Modulated by Adiposity, Menopausal State, and the
            Mediterranean Diet
  JOURNAL   Front Endocrinol (Lausanne) 11, 245 (2020)
   PUBMED   32390948
  REMARK    GeneRIF: ZNF577 Methylation Levels in Leukocytes From Women With
            Breast Cancer Is Modulated by Adiposity, Menopausal State, and the
            Mediterranean Diet.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011460.3, AC074141.3 and AC006272.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.58490.1,
                                           SRR1803613.220997.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267750 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..111
                     /product="zinc finger protein 577 isoform c"
                     /calculated_mol_wt=12340
     Region          25..83
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     CDS             1..111
                     /gene="ZNF577"
                     /coded_by="NM_001370455.1:1350..1685"
                     /note="isoform c is encoded by transcript variant 8"
                     /db_xref="GeneID:84765"
                     /db_xref="HGNC:HGNC:28673"
ORIGIN      
        1 mknativmsv rreqgsssge gslsfedvav gftreewqfl dqsqkvlyke vmlenyinlv
       61 sigyrgtkpd slfkleqgep pgiaegaahs qicpgysfrr rtlqmegmqe s
//
LOCUS       NP_065975                441 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 26 [Homo sapiens].
ACCESSION   NP_065975
VERSION     NP_065975.1
DBSOURCE    REFSEQ: accession NM_020924.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Vick,P., Eberle,B., Choukair,D., Weiss,B., Roeth,R., Schneider,I.,
            Paramasivam,N., Bettendorf,M. and Rappold,G.A.
  TITLE     Identification of ZBTB26 as a Novel Risk Factor for Congenital
            Hypothyroidism
  JOURNAL   Genes (Basel) 12 (12), 1862 (2021)
   PUBMED   34946811
  REMARK    GeneRIF: Identification of ZBTB26 as a Novel Risk Factor for
            Congenital Hypothyroidism.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY066289.1, BC018748.1, AK058083.1, BM682342.1 and AC007066.4.
            
            Transcript Variant: This variant (1) and variants 2 and 3 encode
            the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018748.1, SRR1660803.136412.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373656.4/ ENSP00000362760.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.2"
     Protein         1..441
                     /product="zinc finger and BTB domain-containing protein
                     26"
                     /note="zinc finger protein 483; zinc finger protein 481;
                     zinc finger protein Bioref"
                     /calculated_mol_wt=49822
     Region          8..129
                     /region_name="BTB_POZ_ZBTB26_Bioref"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 26 (ZBTB26); cd18214"
                     /db_xref="CDD:349523"
     Region          134..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK0.2)"
     Region          194..216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK0.2)"
     Region          <269..>381
                     /region_name="COG5236"
                     /note="Uncharacterized conserved protein, contains RING
                     Zn-finger [General function prediction only]"
                     /db_xref="CDD:227561"
     Region          275..295
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..320
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(305,307,309,311..312,315..316,319,333,335,339..340,
                     343..344,347,361,363,365,367..368,371..372)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          312..337
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          356..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..441
                     /gene="ZBTB26"
                     /gene_synonym="bioref; ZNF481"
                     /coded_by="NM_020924.4:87..1412"
                     /db_xref="CCDS:CCDS6847.1"
                     /db_xref="GeneID:57684"
                     /db_xref="HGNC:HGNC:23383"
                     /db_xref="MIM:620164"
ORIGIN      
        1 msersdllhf kfenygdsml qkmnklreen kfcdvtvlid dievqghkiv faagspflrd
       61 qfllndsrev kisilqssev grqlllscys gvlefpemel vnyltaasfl qmshiverct
      121 qalwkfikpk qpmdskegce pqsaspqske qqgdargspk qdspcihpse dsmdmedsdi
      181 qivkvesigd vsevrskkdq nqfissepta lhssepqhsl instvenrvs eieqnhlhny
      241 alsytgsdni imaskdvfgp nirgvdkglq whhqcpkctr vfrhlenyan hlkmhklfmc
      301 llcgktftqk gnlhrhmrvh agikpfqcki cgktfsqkcs lqdhlnlhsg dkphkcnycd
      361 mvfahkpvlr khlkqlhgkn sfdnanernv qdltvdfdsf acttvtdskg cqpqpdatqv
      421 ldagklaqav lnlrndstcv n
//
LOCUS       NP_056994                746 aa            linear   PRI 27-APR-2025
DEFINITION  WD repeat-containing and planar cell polarity effector protein
            fritz homolog isoform 2 [Homo sapiens].
ACCESSION   NP_056994
VERSION     NP_056994.3
DBSOURCE    REFSEQ: accession NM_015910.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   O'Farrell,F., Aleyakpo,B., Mustafa,R., Jiang,X., Pinto,R.C.,
            Elliott,P., Tzoulaki,I., Dehghan,A., Loh,S.H.Y., Barclay,J.W.,
            Martins,L.M. and Pazoki,R.
  TITLE     Evidence for involvement of the alcohol consumption WDPCP gene in
            lipid metabolism, and liver cirrhosis
  JOURNAL   Sci Rep 13 (1), 20616 (2023)
   PUBMED   37996473
  REMARK    GeneRIF: Evidence for involvement of the alcohol consumption WDPCP
            gene in lipid metabolism, and liver cirrhosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Bruel,A.L., Franco,B., Duffourd,Y., Thevenon,J., Jego,L., Lopez,E.,
            Deleuze,J.F., Doummar,D., Giles,R.H., Johnson,C.A., Huynen,M.A.,
            Chevrier,V., Burglen,L., Morleo,M., Desguerres,I., Pierquin,G.,
            Doray,B., Gilbert-Dussardier,B., Reversade,B.,
            Steichen-Gersdorf,E., Baumann,C., Panigrahi,I.,
            Fargeot-Espaliat,A., Dieux,A., David,A., Goldenberg,A., Bongers,E.,
            Gaillard,D., Argente,J., Aral,B., Gigot,N., St-Onge,J.,
            Birnbaum,D., Phadke,S.R., Cormier-Daire,V., Eguether,T.,
            Pazour,G.J., Herranz-Perez,V., Goldstein,J.S., Pasquier,L.,
            Loget,P., Saunier,S., Megarbane,A., Rosnet,O., Leroux,M.R.,
            Wallingford,J.B., Blacque,O.E., Nachury,M.V., Attie-Bitach,T.,
            Riviere,J.B., Faivre,L. and Thauvin-Robinet,C.
  TITLE     Fifteen years of research on oral-facial-digital syndromes: from 1
            to 16 causal genes
  JOURNAL   J Med Genet 54 (6), 371-380 (2017)
   PUBMED   28289185
  REMARK    Review article
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Ma,Y., Sun,Y., Jiang,L., Zuo,K., Chen,H., Guo,J., Chen,F., Lai,Y.
            and Shi,J.
  TITLE     WDPCP regulates the ciliogenesis of human sinonasal epithelial
            cells in chronic rhinosinusitis
  JOURNAL   Cytoskeleton (Hoboken) 74 (2), 82-90 (2017)
   PUBMED   28001338
  REMARK    GeneRIF: Inflammatory cytokines cause reduced WDPCP expression,
            which contributes to impaired ciliogenesis in human rhinosinusitis.
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Toriyama,M., Lee,C., Taylor,S.P., Duran,I., Cohn,D.H., Bruel,A.L.,
            Tabler,J.M., Drew,K., Kelly,M.R., Kim,S., Park,T.J., Braun,D.A.,
            Pierquin,G., Biver,A., Wagner,K., Malfroot,A., Panigrahi,I.,
            Franco,B., Al-Lami,H.A., Yeung,Y., Choi,Y.J., Duffourd,Y.,
            Faivre,L., Riviere,J.B., Chen,J., Liu,K.J., Marcotte,E.M.,
            Hildebrandt,F., Thauvin-Robinet,C., Krakow,D., Jackson,P.K. and
            Wallingford,J.B.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     The ciliopathy-associated CPLANE proteins direct basal body
            recruitment of intraflagellar transport machinery
  JOURNAL   Nat Genet 48 (6), 648-656 (2016)
   PUBMED   27158779
  REMARK    Erratum:[Nat Genet. 2016 Jul 27;48(8):970. doi:
            10.1038/ng0816-970b. PMID: 27463398]
REFERENCE   5  (residues 1 to 746)
  AUTHORS   Aliferis,K., Helle,S., Gyapay,G., Duchatelet,S., Stoetzel,C.,
            Mandel,J.L. and Dollfus,H.
  TITLE     Differentiating Alstrom from Bardet-Biedl syndrome (BBS) using
            systematic ciliopathy genes sequencing
  JOURNAL   Ophthalmic Genet 33 (1), 18-22 (2012)
   PUBMED   22004009
REFERENCE   6  (residues 1 to 746)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 746)
  AUTHORS   Chen,J., Smaoui,N., Hammer,M.B., Jiao,X., Riazuddin,S.A.,
            Harper,S., Katsanis,N., Riazuddin,S., Chaabouni,H., Berson,E.L. and
            Hejtmancik,J.F.
  TITLE     Molecular analysis of Bardet-Biedl syndrome families: report of 21
            novel mutations in 10 genes
  JOURNAL   Invest Ophthalmol Vis Sci 52 (8), 5317-5324 (2011)
   PUBMED   21642631
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 746)
  AUTHORS   Kim,S.K., Shindo,A., Park,T.J., Oh,E.C., Ghosh,S., Gray,R.S.,
            Lewis,R.A., Johnson,C.A., Attie-Bittach,T., Katsanis,N. and
            Wallingford,J.B.
  TITLE     Planar cell polarity acts through septins to control collective
            cell movement and ciliogenesis
  JOURNAL   Science 329 (5997), 1337-1340 (2010)
   PUBMED   20671153
  REMARK    GeneRIF: study linked mutations in Fritz to Bardet-Biedl and
            Meckel-Gruber syndromes, a notable link given that other genes
            mutated in these syndromes also influence collective cell movement
            and ciliogenesis
REFERENCE   9  (residues 1 to 746)
  AUTHORS   Collier,S., Lee,H., Burgess,R. and Adler,P.
  TITLE     The WD40 repeat protein fritz links cytoskeletal planar polarity to
            frizzled subcellular localization in the Drosophila epidermis
  JOURNAL   Genetics 169 (4), 2035-2045 (2005)
   PUBMED   15654087
REFERENCE   10 (residues 1 to 746)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016734.7, AL833623.1,
            AC079353.5, AC009501.4 and BM991121.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 9, 2006 this sequence version replaced NP_056994.2.
            
            Summary: This gene encodes a cytoplasmic WD40 repeat protein. A
            similar gene in frogs encodes a planar cell polarity protein that
            plays a critical role in collective cell movement and ciliogenesis
            by mediating septin localization. Mutations in this gene are
            associated with Bardet-Biedl syndrome 15 and may also play a role
            in Meckel-Gruber syndrome. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jun 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.43457.1, AL833623.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000272321.12/ ENSP00000272321.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p15"
     Protein         1..746
                     /product="WD repeat-containing and planar cell polarity
                     effector protein fritz homolog isoform 2"
                     /note="WD repeat-containing protein C2orf86; WD
                     repeat-containing and planar cell polarity effector
                     protein fritz homolog; Bardet-Biedl syndrome 15 protein;
                     ciliogenesis and planar polarity effector 5; ciliogenesis
                     and planar polarity effector complex subunit 5"
                     /calculated_mol_wt=84953
     Region          79..622
                     /region_name="Frtz"
                     /note="WD repeat-containing and planar cell polarity
                     effector protein Fritz; pfam11768"
                     /db_xref="CDD:432059"
     Region          326..374
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O95876.2)"
     Region          375..414
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O95876.2)"
     CDS             1..746
                     /gene="WDPCP"
                     /gene_synonym="BBS15; C2orf86; CHDTHP; CPLANE5; FRITZ;
                     FRTZ"
                     /coded_by="NM_015910.7:207..2447"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42688.1"
                     /db_xref="GeneID:51057"
                     /db_xref="HGNC:HGNC:28027"
                     /db_xref="MIM:613580"
ORIGIN      
        1 mrrefcwday skaagsrass plprqdrdsf chqmsfclte lhlwslkntl hiadrdigiy
       61 qyydkkdppa tehgnlekkq klaesrdypw tlknrrpekl rdslkeleel mqnsrcvlsk
      121 wknkyvcqll fgsgvlvsls lsgpqlekvv idrslvgkli sdtisdallt dsfiilsfla
      181 qnklcfiqft kkmessdvnk rleklsaldy kifyyeipgp inktterhla incvhdrvvc
      241 wwplvnddaw pwapissekd ranllllgya qgrlevlssv rtewdpldvr fgtkqpyqvf
      301 tvehsvsvdk epmadsciye cirnkiqcvs vtriplkska isccrnvted klilgcedss
      361 lilyethrrv tllaqtellp slischpsga illvgsnqge lqifdmalsp iniqllaedr
      421 lpretlqfsk lfdassslvq mqwiapqvvs qkgegsdiyd llflrfergp lgvllfklgv
      481 ftrgqlglid iifqyihcde iyeainilss mnwdtlghqc fismsaivnh llrqkltper
      541 eaqletslgt fyaptrplld stileyrdqi skyarrffhh llryqrfeka fllavdvgar
      601 dlfmdihyla ldkgelalae varkrasdid aesitsgvel lgpldrgdml neafiglsla
      661 pqgedsfpdn lppscpthrh ilqqrilngs snrqiidrrn elekdicsgf lmtntcnaed
      721 gelredgreq eirdggslkm ihfglv
//
LOCUS       NP_849195                802 aa            linear   PRI 27-APR-2025
DEFINITION  neuronal PAS domain-containing protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_849195
VERSION     NP_849195.2
DBSOURCE    REFSEQ: accession NM_178864.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Selcuk,B., Aksu,T., Dereli,O. and Adebali,O.
  TITLE     Downregulated NPAS4 in multiple brain regions is associated with
            major depressive disorder
  JOURNAL   Sci Rep 13 (1), 21596 (2023)
   PUBMED   38062059
  REMARK    GeneRIF: Downregulated NPAS4 in multiple brain regions is
            associated with major depressive disorder.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Sun,X., Jing,L., Li,F., Zhang,M., Diao,X., Zhuang,J., Rastinejad,F.
            and Wu,D.
  TITLE     Structures of NPAS4-ARNT and NPAS4-ARNT2 heterodimers reveal new
            dimerization modalities in the bHLH-PAS transcription factor family
  JOURNAL   Proc Natl Acad Sci U S A 119 (46), e2208804119 (2022)
   PUBMED   36343253
  REMARK    GeneRIF: Structures of NPAS4-ARNT and NPAS4-ARNT2 heterodimers
            reveal new dimerization modalities in the bHLH-PAS transcription
            factor family.
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Xiong,H., Wang,H. and Yu,Q.
  TITLE     Circular RNA circ_0003420 mediates inflammation in sepsis-induced
            liver damage by downregulating neuronal PAS domain protein 4
  JOURNAL   Immunopharmacol Immunotoxicol 43 (3), 271-282 (2021)
   PUBMED   33719821
  REMARK    GeneRIF: Circular RNA circ_0003420 mediates inflammation in
            sepsis-induced liver damage by downregulating neuronal PAS domain
            protein 4.
            Erratum:[Immunopharmacol Immunotoxicol. 2021 Oct;43(5):I. doi:
            10.1080/08923973.2021.1975024. PMID: 34468267]
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Rossi,J.J., Rosenfeld,J.A., Chan,K.M., Streff,H., Nankivell,V.,
            Peet,D.J., Whitelaw,M.L. and Bersten,D.C.
  TITLE     Molecular characterisation of rare loss-of-function NPAS3 and NPAS4
            variants identified in individuals with neurodevelopmental
            disorders
  JOURNAL   Sci Rep 11 (1), 6602 (2021)
   PUBMED   33758288
  REMARK    GeneRIF: Molecular characterisation of rare loss-of-function NPAS3
            and NPAS4 variants identified in individuals with
            neurodevelopmental disorders.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 802)
  AUTHORS   Esser,J.S., Charlet,A., Schmidt,M., Heck,S., Allen,A., Lother,A.,
            Epting,D., Patterson,C., Bode,C. and Moser,M.
  TITLE     The neuronal transcription factor NPAS4 is a strong inducer of
            sprouting angiogenesis and tip cell formation
  JOURNAL   Cardiovasc Res 113 (2), 222-223 (2017)
   PUBMED   28082451
  REMARK    GeneRIF: NPAS4 is expressed in endothelial cells, regulates
            VE-cadherin expression and regulates sprouting angiogenesis.
REFERENCE   6  (residues 1 to 802)
  AUTHORS   Choy,F.C., Klaric,T.S., Koblar,S.A. and Lewis,M.D.
  TITLE     The Role of the Neuroprotective Factor Npas4 in Cerebral Ischemia
  JOURNAL   Int J Mol Sci 16 (12), 29011-29028 (2015)
   PUBMED   26690124
  REMARK    GeneRIF: This review summarizes the current knowledge of the roles
            that Npas4 may play in neuroinflammation and ischemia.  [review]
            Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 802)
  AUTHORS   Klaric,T.S., Thomas,P.Q., Dottori,M., Leong,W.K., Koblar,S.A. and
            Lewis,M.D.
  TITLE     A reduction in Npas4 expression results in delayed neural
            differentiation of mouse embryonic stem cells
  JOURNAL   Stem Cell Res Ther 5 (3), 64 (2014)
   PUBMED   24887558
  REMARK    GeneRIF: we provide the first evidence that Npas4 is expressed
            during embryonic development and that it may have a developmental
            role that is unrelated to its function in the adult brain
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 802)
  AUTHORS   Bersten,D.C., Bruning,J.B., Peet,D.J. and Whitelaw,M.L.
  TITLE     Human variants in the neuronal basic helix-loop-helix/Per-Arnt-Sim
            (bHLH/PAS) transcription factor complex NPAS4/ARNT2 disrupt
            function
  JOURNAL   PLoS One 9 (1), e85768 (2014)
   PUBMED   24465693
  REMARK    GeneRIF: These results provide insight into the mechanisms of
            NPAS4/ARNT dimerisation and transcriptional activation.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 802)
  CONSRTM   Psychiatric GWAS Consortium Bipolar Disorder Working Group
  TITLE     Large-scale genome-wide association analysis of bipolar disorder
            identifies a new susceptibility locus near ODZ4
  JOURNAL   Nat Genet 43 (10), 977-983 (2011)
   PUBMED   21926972
  REMARK    Erratum:[Nat Genet. 2012 Sep;44(9):1072. Fullerton, Janice M
            [added]; Hyoun, Phil L [corrected to Lee, Phil H]; Meng, Fan Guo
            [corrected to Meng, Fan]]
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 802)
  AUTHORS   Ooe,N., Saito,K., Mikami,N., Nakatuka,I. and Kaneko,H.
  TITLE     Identification of a novel basic helix-loop-helix-PAS factor, NXF,
            reveals a Sim2 competitive, positive regulatory role in
            dendritic-cytoskeleton modulator drebrin gene expression
  JOURNAL   Mol Cell Biol 24 (2), 608-616 (2004)
   PUBMED   14701734
  REMARK    GeneRIF: a novel NXF signaling system on neural gene promoter may
            be a molecular target of the adverse effects of Sim2 in the mental
            retardation of Down's syndrome
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK096253.1, AB049469.1 and AP001107.5.
            
            On Jul 11, 2008 this sequence version replaced NP_849195.1.
            
            Summary: NXF is a member of the basic helix-loop-helix-PER (MIM
            602260)-ARNT (MIM 126110)-SIM (see SIM2; MIM 600892) (bHLH-PAS)
            class of transcriptional regulators, which are involved in a wide
            range of physiologic and developmental events (Ooe et al., 2004
            [PubMed 14701734]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB049469.1, AK096253.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2156670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311034.7/ ENSP00000311196.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..802
                     /product="neuronal PAS domain-containing protein 4 isoform
                     1"
                     /note="neuronal PAS domain-containing protein 4; HLH-PAS
                     transcription factor NXF; neuronal PAS4; PAS
                     domain-containing protein 10; class E basic
                     helix-loop-helix protein 79"
                     /calculated_mol_wt=86986
     Region          1..13
                     /region_name="Basic motif, degenerate.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00981"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUM7.1)"
     Region          2..57
                     /region_name="bHLH-PAS_NPAS4_PASD10"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in neuronal PAS domain-containing protein 4
                     (NPAS4) and similar proteins; cd19697"
                     /db_xref="CDD:381540"
     Site            order(4..6,10,12..13,17,38..39)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381540"
     Region          14..53
                     /region_name="Helix-loop-helix motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00981"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUM7.1)"
     Site            order(15..16,19..20,22..23,40,43,47,49..50,54,56)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381540"
     Region          72..135
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          217..319
                     /region_name="PAS_11"
                     /note="PAS domain; pfam14598"
                     /db_xref="CDD:464214"
     Region          466..485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUM7.1)"
     Region          506..555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUM7.1)"
     Region          717..749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUM7.1)"
     CDS             1..802
                     /gene="NPAS4"
                     /gene_synonym="bHLHe79; Le-PAS; NXF; PASD10"
                     /coded_by="NM_178864.4:146..2554"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8138.1"
                     /db_xref="GeneID:266743"
                     /db_xref="HGNC:HGNC:18983"
                     /db_xref="MIM:608554"
ORIGIN      
        1 myrstkgask arrdqinaei rnlkellpla eadkvrlsyl himslaciyt rkgvffaggt
       61 plagptglls aqeledivaa lpgfllvfta egkllylses vsehlghsmv dlvaqgdsiy
      121 diidpadhlt vrqqltlpsa ldtdrlfrcr fntskslrrq sagnklvlir grfhahppga
      181 ywagnpvfta fcapleprpr pgpgpgpgpa slflamfqsr hakdlalldi sesvliylgf
      241 ersellcksw ygllhpedla hasaqhyrll aesgdiqaem vvrlqaktgg wawiycllys
      301 egpegpitan nypisdmeaw slrqqlnsed tqaayvlgtp tmlpsfpeni lsqeecsstn
      361 plftaalgap rstsfpsape lsvvsaseel prpskeldfs yltfpsgpep slqaelskdl
      421 vctppytphq pggcaflfsl hepfqthlpt psstlqeqlt pstatfsdql tpssatfpdp
      481 ltsplqgqlt etsvrsyedq ltpctstfpd qllpstatfp eplgspaheq ltppstafqa
      541 hldspsqtfp eqlspnptkt yfaqegcsfl yeklppspss pgngdctlla laqlrgplsv
      601 dvplvpegll tpeaspvkqs ffhysekeqn eidrliqqis qlaqgmdrpf saeagtggle
      661 plggleplds nlslsgagpp vlsldlkpwk cqeldfladp dnmfleetpv edifmdlstp
      721 dpseewgsgd peaegpggap spcnnlsped hsfledlaty etafetgvsa fpydgftdel
      781 hqlqsqvqds fhedgsggep tf
//
LOCUS       NP_001128165              37 aa            linear   PRI 27-APR-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit 4 [Homo sapiens].
ACCESSION   NP_001128165 XP_001717715 XP_001717773 XP_001720087
VERSION     NP_001128165.1
DBSOURCE    REFSEQ: accession NM_001134693.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 37)
  AUTHORS   Lampson,B.L., Ramiotarez,A.S., Baro,M., He,L., Hegde,M., Koduri,V.,
            Pfaff,J.L., Hanna,R.E., Kowal,J., Shirole,N.H., He,Y., Doench,J.G.,
            Contessa,J.N., Locher,K.P. and Kaelin,W.G. Jr.
  TITLE     Positive selection CRISPR screens reveal a druggable pocket in an
            oligosaccharyltransferase required for inflammatory signaling to
            NF-kappaB
  JOURNAL   Cell 187 (9), 2209-2223 (2024)
   PUBMED   38670073
REFERENCE   2  (residues 1 to 37)
  AUTHORS   Gemmer,M., Chaillet,M.L., van Loenhout,J., Cuevas Arenas,R.,
            Vismpas,D., Grollers-Mulderij,M., Koh,F.A., Albanese,P.,
            Scheltema,R.A., Howes,S.C., Kotecha,A., Fedry,J. and Forster,F.
  TITLE     Visualization of translation and protein biogenesis at the ER
            membrane
  JOURNAL   Nature 614 (7946), 160-167 (2023)
   PUBMED   36697828
REFERENCE   3  (residues 1 to 37)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 37)
  AUTHORS   Ramirez,A.S., Kowal,J. and Locher,K.P.
  TITLE     Cryo-electron microscopy structures of human
            oligosaccharyltransferase complexes OST-A and OST-B
  JOURNAL   Science 366 (6471), 1372-1375 (2019)
   PUBMED   31831667
REFERENCE   5  (residues 1 to 37)
  AUTHORS   Dumax-Vorzet,A., Roboti,P. and High,S.
  TITLE     OST4 is a subunit of the mammalian oligosaccharyltransferase
            required for efficient N-glycosylation
  JOURNAL   J Cell Sci 126 (Pt 12), 2595-2606 (2013)
   PUBMED   23606741
REFERENCE   6  (residues 1 to 37)
  AUTHORS   Gayen,S. and Kang,C.
  TITLE     Solution structure of a human minimembrane protein Ost4, a subunit
            of the oligosaccharyltransferase complex
  JOURNAL   Biochem Biophys Res Commun 409 (3), 572-576 (2011)
   PUBMED   21609714
  REMARK    GeneRIF: This study determined the solution structure of human Ost4
            in solvent system using NMR spectroscopy.
REFERENCE   7  (residues 1 to 37)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 37)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 37)
  AUTHORS   Kelleher,D.J. and Gilmore,R.
  TITLE     An evolving view of the eukaryotic oligosaccharyltransferase
  JOURNAL   Glycobiology 16 (4), 47R-62R (2006)
   PUBMED   16317064
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF697310.1, BC105283.1 and AA772256.1.
            
            On or before Sep 5, 2008 this sequence version replaced
            XP_001717773.1, XP_001720087.1, XP_001717715.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CN484950.1, BG705396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000456793.2/ ENSP00000457935.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..37
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..37
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit 4"
                     /note="oligosaccharyltransferase 4 homolog"
                     /calculated_mol_wt=4062
     Region          1..34
                     /region_name="Ost4"
                     /note="Oligosaccaryltransferase; pfam10215"
                     /db_xref="CDD:431142"
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6T2.1)"
     CDS             1..37
                     /gene="OST4"
                     /coded_by="NM_001134693.2:56..169"
                     /db_xref="CCDS:CCDS58703.1"
                     /db_xref="GeneID:100128731"
                     /db_xref="HGNC:HGNC:32483"
                     /db_xref="MIM:618932"
ORIGIN      
        1 mitdvqlaif anmlgvslfl lvvlyhyvav nnpkkqe
//
LOCUS       NP_001060                445 aa            linear   PRI 27-APR-2025
DEFINITION  tubulin beta-2A chain isoform 1 [Homo sapiens].
ACCESSION   NP_001060
VERSION     NP_001060.1
DBSOURCE    REFSEQ: accession NM_001069.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Schroter,J., Syring,H., Gohring,G., Kolker,S., Opladen,T.,
            Hoffmann,G.F., Syrbe,S. and Jung-Klawitter,S.
  TITLE     Generation of an induced pluripotent stem cell line (DHMCi009-A)
            from an individual with TUBB2A tubulinopathy
  JOURNAL   Stem Cell Res 64, 102879 (2022)
   PUBMED   35930870
  REMARK    GeneRIF: Generation of an induced pluripotent stem cell line
            (DHMCi009-A) from an individual with TUBB2A tubulinopathy.
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Ragoussis,V., Pagnamenta,A.T., Haines,R.L., Giacopuzzi,E.,
            McClatchey,M.A., Sampson,J.R., Suri,M., Gardham,A., Cobben,J.M.,
            Osio,D., Fry,A.E. and Taylor,J.C.
  CONSRTM   Genomics England Research Consortium
  TITLE     Using data from the 100,000 Genomes Project to resolve conflicting
            interpretations of a recurrent TUBB2A mutation
  JOURNAL   J Med Genet 59 (4), 366-369 (2022)
   PUBMED   33547136
  REMARK    GeneRIF: Using data from the 100,000 Genomes Project to resolve
            conflicting interpretations of a recurrent TUBB2A mutation.
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Jin,Y., Zhang,S. and Liu,L.
  TITLE     Circular RNA circ_C16orf62 Suppresses Cell Growth in Gastric Cancer
            by miR-421/Tubulin beta-2A Chain (TUBB2A) Axis
  JOURNAL   Med Sci Monit 26, e924343 (2020)
   PUBMED   33006960
  REMARK    GeneRIF: Circular RNA circ_C16orf62 Suppresses Cell Growth in
            Gastric Cancer by miR-421/Tubulin beta-2A Chain (TUBB2A) Axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Takahashi,M., Tomizawa,K., Sato,K., Ohtake,A. and Omori,A.
  TITLE     A novel tau-tubulin kinase from bovine brain
  JOURNAL   FEBS Lett 372 (1), 59-64 (1995)
   PUBMED   7556643
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Bahi-Buisson,N. and Maillard,C.
  TITLE     Tubulinopathies Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27010057
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Horisberger,M.A.
  TITLE     Interferon-induced human protein MxA is a GTPase which binds
            transiently to cellular proteins
  JOURNAL   J Virol 66 (8), 4705-4709 (1992)
   PUBMED   1629950
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Wang,D., Villasante,A., Lewis,S.A. and Cowan,N.J.
  TITLE     The mammalian beta-tubulin repertoire: hematopoietic expression of
            a novel, heterologous beta-tubulin isotype
  JOURNAL   J Cell Biol 103 (5), 1903-1910 (1986)
   PUBMED   3782288
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Lee,M.G., Lewis,S.A., Wilde,C.D. and Cowan,N.J.
  TITLE     Evolutionary history of a multigene family: an expressed human
            beta-tubulin gene and three processed pseudogenes
  JOURNAL   Cell 33 (2), 477-487 (1983)
   PUBMED   6688039
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031963.40, X79535.1 and
            AL038778.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Microtubules, key participants in processes such as
            mitosis and intracellular transport, are composed of heterodimers
            of alpha- and beta-tubulins. The protein encoded by this gene is a
            beta-tubulin. Defects in this gene are associated with complex
            cortical dysplasia with other brain malformations-5. Two transcript
            variants encoding distinct isoforms have been found for this gene.
            [provided by RefSeq, Jul 2015].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.53490.1,
                                           SRR3476690.1019106.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000333628.4/ ENSP00000369703.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p25.2"
     Protein         1..445
                     /product="tubulin beta-2A chain isoform 1"
                     /note="tubulin, beta polypeptide 2; class IIa
                     beta-tubulin; tubulin beta-2A chain; tubulin, beta 2A"
                     /calculated_mol_wt=49776
     Region          1..430
                     /region_name="PLN00220"
                     /note="tubulin beta chain; Provisional"
                     /db_xref="CDD:215107"
     Region          1..4
                     /region_name="MREI motif.
                     /evidence=ECO:0000250|UniProtKB:P07437"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13885.1)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P99024; propagated from
                     UniProtKB/Swiss-Prot (Q13885.1)"
     Site            58
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P07437; propagated from
                     UniProtKB/Swiss-Prot (Q13885.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:16371510; propagated from
                     UniProtKB/Swiss-Prot (Q13885.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07437; propagated from
                     UniProtKB/Swiss-Prot (Q13885.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07437; propagated from
                     UniProtKB/Swiss-Prot (Q13885.1)"
     Site            318
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P07437; propagated from
                     UniProtKB/Swiss-Prot (Q13885.1)"
     Region          422..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13885.1)"
     CDS             1..445
                     /gene="TUBB2A"
                     /gene_synonym="CDCBM5; TUBB; TUBB2"
                     /coded_by="NM_001069.3:82..1419"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4484.1"
                     /db_xref="GeneID:7280"
                     /db_xref="HGNC:HGNC:12412"
                     /db_xref="MIM:615101"
ORIGIN      
        1 mreivhiqag qcgnqigakf wevisdehgi dptgsyhgds dlqlerinvy yneaagnkyv
       61 prailvdlep gtmdsvrsgp fgqifrpdnf vfgqsgagnn wakghytega elvdsvldvv
      121 rkesescdcl qgfqlthslg ggtgsgmgtl liskireeyp drimntfsvm pspkvsdtvv
      181 epynatlsvh qlventdety sidnealydi cfrtlklttp tygdlnhlvs atmsgvttcl
      241 rfpgqlnadl rklavnmvpf prlhffmpgf apltsrgsqq yraltvpelt qqmfdsknmm
      301 aacdprhgry ltvaaifrgr msmkevdeqm lnvqnknssy fvewipnnvk tavcdipprg
      361 lkmsatfign staiqelfkr iseqftamfr rkaflhwytg egmdemefte aesnmndlvs
      421 eyqqyqdata deqgefeeee gedea
//
LOCUS       NP_001356687             139 aa            linear   PRI 27-APR-2025
DEFINITION  ATP synthase F(0) complex subunit C2, mitochondrial isoform f
            precursor [Homo sapiens].
ACCESSION   NP_001356687
VERSION     NP_001356687.1
DBSOURCE    REFSEQ: accession NM_001369758.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Tebbenkamp,A.T.N., Varela,L., Choi,J., Paredes,M.I., Giani,A.M.,
            Song,J.E., Sestan-Pesa,M., Franjic,D., Sousa,A.M.M., Liu,Z.W.,
            Li,M., Bichsel,C., Koch,M., Szigeti-Buck,K., Liu,F., Li,Z.,
            Kawasawa,Y.I., Paspalas,C.D., Mineur,Y.S., Prontera,P., Merla,G.,
            Picciotto,M.R., Arnsten,A.F.T., Horvath,T.L. and Sestan,N.
  TITLE     The 7q11.23 Protein DNAJC30 Interacts with ATP Synthase and Links
            Mitochondria to Brain Development
  JOURNAL   Cell 175 (4), 1088-1104 (2018)
   PUBMED   30318146
REFERENCE   3  (residues 1 to 139)
  AUTHORS   He,J., Ford,H.C., Carroll,J., Ding,S., Fearnley,I.M. and
            Walker,J.E.
  TITLE     Persistence of the mitochondrial permeability transition in the
            absence of subunit c of human ATP synthase
  JOURNAL   Proc Natl Acad Sci U S A 114 (13), 3409-3414 (2017)
   PUBMED   28289229
  REMARK    GeneRIF: ATP5G1, ATP5G2, and ATP5G3 of the ATP synthase are not
            involved in forming the permeability transition pore.
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Fujikawa,M., Sugawara,K., Tanabe,T. and Yoshida,M.
  TITLE     Assembly of human mitochondrial ATP synthase through two separate
            intermediates, F1-c-ring and b-e-g complex
  JOURNAL   FEBS Lett 589 (19 Pt B), 2707-2712 (2015)
   PUBMED   26297831
REFERENCE   5  (residues 1 to 139)
  AUTHORS   He,M., Xu,M., Zhang,B., Liang,J., Chen,P., Lee,J.Y., Johnson,T.A.,
            Li,H., Yang,X., Dai,J., Liang,L., Gui,L., Qi,Q., Huang,J., Li,Y.,
            Adair,L.S., Aung,T., Cai,Q., Cheng,C.Y., Cho,M.C., Cho,Y.S.,
            Chu,M., Cui,B., Gao,Y.T., Go,M.J., Gu,D., Gu,W., Guo,H., Hao,Y.,
            Hong,J., Hu,Z., Hu,Y., Huang,J., Hwang,J.Y., Ikram,M.K., Jin,G.,
            Kang,D.H., Khor,C.C., Kim,B.J., Kim,H.T., Kubo,M., Lee,J., Lee,J.,
            Lee,N.R., Li,R., Li,J., Liu,J., Longe,J., Lu,W., Lu,X., Miao,X.,
            Okada,Y., Ong,R.T., Qiu,G., Seielstad,M., Sim,X., Song,H.,
            Takeuchi,F., Tanaka,T., Taylor,P.R., Wang,L., Wang,W., Wang,Y.,
            Wu,C., Wu,Y., Xiang,Y.B., Yamamoto,K., Yang,H., Liao,M., Yokota,M.,
            Young,T., Zhang,X., Kato,N., Wang,Q.K., Zheng,W., Hu,F.B., Lin,D.,
            Shen,H., Teo,Y.Y., Mo,Z., Wong,T.Y., Lin,X., Mohlke,K.L., Ning,G.,
            Tsunoda,T., Han,B.G., Shu,X.O., Tai,E.S., Wu,T. and Qi,L.
  TITLE     Meta-analysis of genome-wide association studies of adult height in
            East Asians identifies 17 novel loci
  JOURNAL   Hum Mol Genet 24 (6), 1791-1800 (2015)
   PUBMED   25429064
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Houstek,J., Andersson,U., Tvrdik,P., Nedergaard,J. and Cannon,B.
  TITLE     The expression of subunit c correlates with and thus may limit the
            biosynthesis of the mitochondrial F0F1-ATPase in brown adipose
            tissue
  JOURNAL   J Biol Chem 270 (13), 7689-7694 (1995)
   PUBMED   7706317
REFERENCE   7  (residues 1 to 139)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   8  (residues 1 to 139)
  AUTHORS   Yan,W.L., Lerner,T.J., Haines,J.L. and Gusella,J.F.
  TITLE     Sequence analysis and mapping of a novel human mitochondrial ATP
            synthase subunit 9 cDNA (ATP5G3)
  JOURNAL   Genomics 24 (2), 375-377 (1994)
   PUBMED   7698763
REFERENCE   9  (residues 1 to 139)
  AUTHORS   Dyer,M.R. and Walker,J.E.
  TITLE     Sequences of members of the human gene family for the c subunit of
            mitochondrial ATP synthase
  JOURNAL   Biochem J 293 (Pt 1) (Pt 1), 51-64 (1993)
   PUBMED   8328972
REFERENCE   10 (residues 1 to 139)
  AUTHORS   Farrell,L.B. and Nagley,P.
  TITLE     Human liver cDNA clones encoding proteolipid subunit 9 of the
            mitochondrial ATPase complex
  JOURNAL   Biochem Biophys Res Commun 144 (3), 1257-1264 (1987)
   PUBMED   2883974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073594.31.
            
            Summary: This gene encodes a subunit of mitochondrial ATP synthase.
            Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an
            electrochemical gradient of protons across the inner membrane
            during oxidative phosphorylation. ATP synthase is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, comprising the proton channel.
            The catalytic portion of mitochondrial ATP synthase consists of 5
            different subunits (alpha, beta, gamma, delta, and epsilon)
            assembled with a stoichiometry of 3 alpha, 3 beta, and single
            representatives of the gamma, delta, and epsilon subunits. The
            proton channel likely has nine subunits (a, b, c, d, e, f, g, F6
            and 8). There are three separate genes which encode subunit c of
            the proton channel and they specify precursors with different
            import sequences but identical mature proteins. The protein encoded
            by this gene is one of three precursors of subunit c. This gene has
            multiple pseudogenes. [provided by RefSeq, Jan 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1847001.1,
                                           SRR14243140.6448411.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..139
                     /product="ATP synthase F(0) complex subunit C2,
                     mitochondrial isoform f precursor"
                     /note="ATP synthase, H+ transporting, mitochondrial F0
                     complex, subunit C2 (subunit 9); ATP synthase
                     lipid-binding protein, mitochondrial; ATP synthase
                     proteolipid P2; ATPase protein 9; ATPase subunit C; ATP
                     synthase c subunit; ATP synthase proton-transporting
                     mitochondrial F(0) complex subunit C2; ATP synthase, H+
                     transporting, mitochondrial Fo complex subunit C2 (subunit
                     9); ATP synthase F(0) complex subunit C2, mitochondrial;
                     dicyclohexylcarbodiimide (DCCD)-reactive proteolipid
                     subunit"
                     /calculated_mol_wt=14279
     mat_peptide     65..139
                     /product="ATP synthase F(0) complex subunit C2,
                     mitochondrial. /id=PRO_0000002562"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
                     /calculated_mol_wt=7608
     Region          65..139
                     /region_name="ATP9"
                     /note="ATP synthase F0 subunit 9; Provisional; MTH00222"
                     /db_xref="CDD:164765"
     Site            80..100
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
     Site            107
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000269|PubMed:30530489; propagated from
                     UniProtKB/Swiss-Prot (Q06055.1)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
     Site            122
                     /site_type="other"
                     /note="Reversibly protonated during proton transport.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q06055.1)"
     CDS             1..139
                     /gene="ATP5MC2"
                     /gene_synonym="ATP5A; ATP5G2"
                     /coded_by="NM_001369758.1:63..482"
                     /note="isoform f precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:517"
                     /db_xref="HGNC:HGNC:842"
                     /db_xref="MIM:603193"
ORIGIN      
        1 mfacskfvst pslstsqlls rplsavvlkr peiltdesls slavscplts lvssrsfqts
       61 aisrdidtaa kfigagaatv gvagsgagig tvfgsliigy arnpslkqql fsyailgfal
      121 seamglfclm vaflilfam
//
LOCUS       NP_081209                 76 aa            linear   ROD 27-APR-2025
DEFINITION  TP53-regulated inhibitor of apoptosis 1 [Mus musculus].
ACCESSION   NP_081209
VERSION     NP_081209.1
DBSOURCE    REFSEQ: accession NM_026933.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Ma,J., Wang,P.Y., Zhuang,J., Son,A.Y., Karius,A.K., Syed,A.M.,
            Nishi,M., Wu,Z., Mori,M.P., Kim,Y.C. and Hwang,P.M.
  TITLE     CHCHD4-TRIAP1 regulation of innate immune signaling mediates
            skeletal muscle adaptation to exercise
  JOURNAL   Cell Rep 43 (1), 113626 (2024)
   PUBMED   38157298
  REMARK    GeneRIF: CHCHD4-TRIAP1 regulation of innate immune signaling
            mediates skeletal muscle adaptation to exercise.
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Nakano,Y., Jahan,I., Bonde,G., Sun,X., Hildebrand,M.S.,
            Engelhardt,J.F., Smith,R.J., Cornell,R.A., Fritzsch,B. and Banfi,B.
  TITLE     A mutation in the Srrm4 gene causes alternative splicing defects
            and deafness in the Bronx waltzer mouse
  JOURNAL   PLoS Genet 8 (10), e1002966 (2012)
   PUBMED   23055939
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC117735.8.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030325.1, AK007514.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 56.06 cM"
     Protein         1..76
                     /product="TP53-regulated inhibitor of apoptosis 1"
                     /note="protein 15E1.1; p53-inducible cell-survival factor"
                     /calculated_mol_wt=8625
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O43715; propagated from
                     UniProtKB/Swiss-Prot (Q9D8Z2.1)"
     Region          2..68
                     /region_name="UPF0203"
                     /note="Uncharacterized protein family (UPF0203);
                     pfam05254"
                     /db_xref="CDD:461604"
     Region          8..18
                     /region_name="Cx9C motif 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D8Z2.1)"
     Site            27
                     /site_type="other"
                     /note="Important for interaction with PRELID3A.
                     /evidence=ECO:0000250|UniProtKB:O43715; propagated from
                     UniProtKB/Swiss-Prot (Q9D8Z2.1)"
     Region          37..47
                     /region_name="Cx9C motif 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D8Z2.1)"
     Site            41
                     /site_type="other"
                     /note="Important for interaction with PRELID3A.
                     /evidence=ECO:0000250|UniProtKB:O43715; propagated from
                     UniProtKB/Swiss-Prot (Q9D8Z2.1)"
     CDS             1..76
                     /gene="Triap1"
                     /gene_synonym="1810015M01Rik; P53csv; Wf-1"
                     /coded_by="NM_026933.3:41..271"
                     /db_xref="CCDS:CCDS39228.1"
                     /db_xref="GeneID:69076"
                     /db_xref="MGI:MGI:1916326"
ORIGIN      
        1 mnsvgeactd mkreydqcfn rwfaekflkg dgsgdpctdl fkryqqcvqk aikekeipie
       61 glefmghgke kpenss
//
LOCUS       NP_001081416             340 aa            linear   VRT 27-APR-2025
DEFINITION  homeobox protein GBX-2 [Xenopus laevis].
ACCESSION   NP_001081416 NP_001081417
VERSION     NP_001081416.2
DBSOURCE    REFSEQ: accession NM_001087947.2
KEYWORDS    RefSeq.
SOURCE      Xenopus laevis (African clawed frog)
  ORGANISM  Xenopus laevis
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae;
            Xenopus; Xenopus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Klein,S.L., Strausberg,R.L., Wagner,L., Pontius,J., Clifton,S.W.
            and Richardson,P.
  TITLE     Genetic and genomic tools for Xenopus research: The NIH Xenopus
            initiative
  JOURNAL   Dev Dyn 225 (4), 384-391 (2002)
   PUBMED   12454917
REFERENCE   2  (residues 1 to 340)
  AUTHORS   von Bubnoff,A., Schmidt,J.E. and Kimelman,D.
  TITLE     The Xenopus laevis homeobox gene Xgbx-2 is an early marker of
            anteroposterior patterning in the ectoderm
  JOURNAL   Mech Dev 54 (2), 149-160 (1996)
   PUBMED   8652408
REFERENCE   3  (residues 1 to 340)
  AUTHORS   King,M.W. and Moore,M.J.
  TITLE     Novel HOX, POU and FKH genes expressed during bFGF-induced
            mesodermal differentiation in Xenopus
  JOURNAL   Nucleic Acids Res 22 (19), 3990-3996 (1994)
   PUBMED   7937122
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAGEVR010000044.1.
            
            On Sep 1, 2018 this sequence version replaced NP_001081416.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U04867.1, BC169847.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00012418, SAMD00012419
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Xenopus laevis"
                     /db_xref="taxon:8355"
                     /chromosome="9_10L"
                     /map="9_10L"
     Protein         1..340
                     /product="homeobox protein GBX-2"
                     /note="homeobox protein Xgbx-2; XGBX-2; gastrulation and
                     brain-specific homeobox protein 2"
                     /calculated_mol_wt=37038
     Region          58..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91907.1)"
     Region          154..196
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91907.1)"
     Region          211..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91907.1)"
     Region          240..296
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..340
                     /gene="gbx2.2.L"
                     /gene_synonym="gbx2; gbx2.2"
                     /coded_by="NM_001087947.2:638..1660"
                     /db_xref="GeneID:397824"
                     /db_xref="Xenbase:XB-GENE-866652"
ORIGIN      
        1 msaafqpplm mmqrplgsst afsidslign ppqpspghfv ytgypmfmpy rpvvlppppp
       61 pppslsqatl qstlssahhh hpipslpggf csslaqgmal tstlmatlpg gfsastqhqe
      121 aarkfgaqsl hgafeksdgs qsdgeegnkt hitkegtllp fsaseaslgp vrgqgkeesg
      181 keaegkgked sylmdsdldy ssddniscqt ahkeedtpee spqnsnpsnn sntsstgknr
      241 rrrtaftseq llelekefhc kkylslters qiahvlklse vqvkiwfqnr rakwkrvkag
      301 ntnsktgeps rnpkivvpip vhvnrfairs qhqqleqarp
//
LOCUS       NP_001356439             248 aa            linear   PRI 27-APR-2025
DEFINITION  protein maestro isoform a [Homo sapiens].
ACCESSION   NP_001356439 XP_005258422
VERSION     NP_001356439.1
DBSOURCE    REFSEQ: accession NM_001369510.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Kenigsberg,S., Lima,P.D., Maghen,L., Wyse,B.A., Lackan,C.,
            Cheung,A.N., Tsang,B.K. and Librach,C.L.
  TITLE     The elusive MAESTRO gene: Its human reproductive tissue-specific
            expression pattern
  JOURNAL   PLoS One 12 (4), e0174873 (2017)
   PUBMED   28406912
  REMARK    GeneRIF: study also shows a punctate nuclear expression pattern and
            disperse cytoplasmic expression pattern of the MRO protein in human
            granulosa-cumulus cells and in testicular germ cells, which was
            later validated by western blotting
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
  REMARK    GeneRIF: The sequence and function of the related mouse gene are
            described.
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Yanaihara,N., Kohno,T., Takakura,S., Takei,K., Otsuka,A.,
            Sunaga,N., Takahashi,M., Yamazaki,M., Tashiro,H., Fukuzumi,Y.,
            Fujimori,Y., Hagiwara,K., Tanaka,T. and Yokota,J.
  TITLE     Physical and transcriptional map of a 311-kb segment of chromosome
            18q21, a candidate lung tumor suppressor locus
  JOURNAL   Genomics 72 (2), 169-179 (2001)
   PUBMED   11401430
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015864.5.
            
            On Apr 10, 2019 this sequence version replaced XP_005258422.1.
            
            Summary: This gene is specifically transcribed in males before and
            after differentiation of testis, and the encoded protein may play
            an important role in a mammalian sex determination. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.339829.1,
                                           SRR5189667.341793.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..248
                     /product="protein maestro isoform a"
                     /note="beside the Ma29 deletion; protein maestro;
                     male-specific transcription in the developing reproductive
                     organs"
                     /calculated_mol_wt=28923
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYG7.2)"
     Region          128..163
                     /region_name="HEAT"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYG7.2)"
     CDS             1..248
                     /gene="MRO"
                     /gene_synonym="B29; C18orf3"
                     /coded_by="NM_001369510.2:77..823"
                     /note="isoform a is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS11947.1"
                     /db_xref="GeneID:83876"
                     /db_xref="HGNC:HGNC:24121"
                     /db_xref="MIM:608080"
ORIGIN      
        1 mdqrqrrilg qplsiptsqp kqkrtsmisf fskvswklrf qkreplknvf filaerardp
       61 sakkrhmamr nlgtmayeap dkvrkykkiv ldllvyglyd pvnlevihes mktltvvlgk
      121 iqgkglgsff iditlqtrtl lddendslry safvlfgqla afagrkwkkf ftsqvkqtrd
      181 sllihlqdrn pqvakacktt fqacspylkl keeysfqsee dqrntklyqq lshyhpeilq
      241 ffyankil
//
LOCUS       NP_848796                795 aa            linear   ROD 27-APR-2025
DEFINITION  diacylglycerol kinase beta isoform 2 [Mus musculus].
ACCESSION   NP_848796
VERSION     NP_848796.2
DBSOURCE    REFSEQ: accession NM_178681.5
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Cesari,E., Farini,D., Medici,V., Ehrmann,I., Guerra,M., Testa,E.,
            Naro,C., Geloso,M.C., Pagliarini,V., La Barbera,L., D'Amelio,M.,
            Orsini,T., Vecchioli,S.F., Tamagnone,L., Fort,P., Viscomi,M.T.,
            Elliott,D.J. and Sette,C.
  TITLE     Differential expression of paralog RNA binding proteins establishes
            a dynamic splicing program required for normal cerebral cortex
            development
  JOURNAL   Nucleic Acids Res 52 (8), 4167-4184 (2024)
   PUBMED   38324473
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Veerakumar,A., Yung,A.R., Liu,Y. and Krasnow,M.A.
  TITLE     Molecularly defined circuits for cardiovascular and cardiopulmonary
            control
  JOURNAL   Nature 606 (7915), 739-746 (2022)
   PUBMED   35650438
REFERENCE   4  (residues 1 to 795)
  AUTHORS   Kakefuda,K., Ishisaka,M., Tsuruma,K., Shimazawa,M. and Hara,H.
  TITLE     Memantine, an NMDA receptor antagonist, improves working memory
            deficits in DGKbeta knockout mice
  JOURNAL   Neurosci Lett 630, 228-232 (2016)
   PUBMED   27495014
  REMARK    GeneRIF: Memantine, an NMDA receptor antagonist, improves working
            memory deficits in Diacylglycerol kinase (DGK) beta knockout mice.
            These findings may support the hypothesis that DGKbeta has a
            pivotal role in cognitive function.
REFERENCE   5  (residues 1 to 795)
  AUTHORS   Hozumi,Y., Kakefuda,K., Yamasaki,M., Watanabe,M., Hara,H. and
            Goto,K.
  TITLE     Involvement of diacylglycerol kinase beta in the spine formation at
            distal dendrites of striatal medium spiny neurons
  JOURNAL   Brain Res 1594, 36-45 (2015)
   PUBMED   25446448
  REMARK    GeneRIF: These findings suggest that DGKbeta regulates the spine
            formation at distal dendrites in medium spiny neurons
REFERENCE   6  (residues 1 to 795)
  AUTHORS   Shirai,Y., Kouzuki,T., Kakefuda,K., Moriguchi,S., Oyagi,A.,
            Horie,K., Morita,S.Y., Shimazawa,M., Fukunaga,K., Takeda,J.,
            Saito,N. and Hara,H.
  TITLE     Essential role of neuron-enriched diacylglycerol kinase (DGK),
            DGKbeta in neurite spine formation, contributing to cognitive
            function
  JOURNAL   PLoS One 5 (7), e11602 (2010)
   PUBMED   20657643
  REMARK    GeneRIF: Results demonstrate that membrane-localized DGKbeta
            regulates spine formation by regulation of lipids, contributing to
            the maintenance of neural networks in synaptic transmission of
            cognitive processes including memory.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 795)
  AUTHORS   Crotty,T., Cai,J., Sakane,F., Taketomi,A., Prescott,S.M. and
            Topham,M.K.
  TITLE     Diacylglycerol kinase delta regulates protein kinase C and
            epidermal growth factor receptor signaling
  JOURNAL   Proc Natl Acad Sci U S A 103 (42), 15485-15490 (2006)
   PUBMED   17021016
REFERENCE   8  (residues 1 to 795)
  AUTHORS   Keng,V.W., Yae,K., Hayakawa,T., Mizuno,S., Uno,Y., Yusa,K.,
            Kokubu,C., Kinoshita,T., Akagi,K., Jenkins,N.A., Copeland,N.G.,
            Horie,K. and Takeda,J.
  TITLE     Region-specific saturation germline mutagenesis in mice using the
            Sleeping Beauty transposon system
  JOURNAL   Nat Methods 2 (10), 763-769 (2005)
   PUBMED   16179923
REFERENCE   9  (residues 1 to 795)
  AUTHORS   Horie,K., Yusa,K., Yae,K., Odajima,J., Fischer,S.E., Keng,V.W.,
            Hayakawa,T., Mizuno,S., Kondoh,G., Ijiri,T., Matsuda,Y.,
            Plasterk,R.H. and Takeda,J.
  TITLE     Characterization of Sleeping Beauty transposition and its
            application to genetic screening in mice
  JOURNAL   Mol Cell Biol 23 (24), 9189-9207 (2003)
   PUBMED   14645530
REFERENCE   10 (residues 1 to 795)
  AUTHORS   Cipres,A., Carrasco,S., Merino,E., Diaz,E., Krishna,U.M.,
            Falck,J.R., Martinez-A,C. and Merida,I.
  TITLE     Regulation of diacylglycerol kinase alpha by phosphoinositide
            3-kinase lipid products
  JOURNAL   J Biol Chem 278 (37), 35629-35635 (2003)
   PUBMED   12832407
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CJ128305.1, AK139408.1, BG088459.2 and AW493391.1.
            
            On Dec 22, 2005 this sequence version replaced NP_848796.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.179046.1,
                                           SRR1660813.17848.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 17.11 cM"
     Protein         1..795
                     /product="diacylglycerol kinase beta isoform 2"
                     /EC_number="2.7.1.107"
                     /note="DAG kinase beta; diglyceride kinase beta"
                     /calculated_mol_wt=89301
     Region          6..141
                     /region_name="DAG_kinase_N"
                     /note="Diacylglycerol kinase N-terminus; pfam14513"
                     /db_xref="CDD:464196"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NS52.2)"
     Region          145..214
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cd00051"
                     /db_xref="CDD:238008"
     Site            order(154,156,158,165,199,201,203,210)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238008"
     Region          230..295
                     /region_name="C1_DGKbeta_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase beta (DAG kinase
                     beta) and similar proteins; cd20845"
                     /db_xref="CDD:410395"
     Site            order(242..248,256..260,263)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410395"
     Region          300..358
                     /region_name="C1_DGKbeta_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase beta (DAG kinase
                     beta) and similar proteins; cd20891"
                     /db_xref="CDD:410441"
     Site            order(307..311,319..323,327)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410441"
     Region          377..409
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NS52.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NS52.2)"
     Region          431..552
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          573..753
                     /region_name="DAGKa"
                     /note="Diacylglycerol kinase accessory domain (presumed);
                     smart00045"
                     /db_xref="CDD:214486"
     Region          664..689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NS52.2)"
     Region          764..795
                     /region_name="Required for association with membranes and
                     function in neurite spine formation.
                     /evidence=ECO:0000269|PubMed:20657643"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NS52.2)"
     Site            784
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NS52.2)"
     CDS             1..795
                     /gene="Dgkb"
                     /gene_synonym="6430574F24; 90kda; C630029D13Rik; DAGK2;
                     DGK; DGK-beta; mKIAA0718"
                     /coded_by="NM_178681.5:625..3012"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS25889.1"
                     /db_xref="GeneID:217480"
                     /db_xref="MGI:MGI:2442474"
ORIGIN      
        1 mtnqekwahl spsefsqlqk yaeystkklk dvleefhgng vlakynpegt idfegfklfm
       61 ktfleaelpd dftahlfmsf snkfphsspn vkskpallsg glrmnkgait pprsspantc
      121 spevihlkdi vcylsllerg rpedklefmf rlydtdgngf ldsselenii gqmmhvaeyl
      181 ewdvtelnpi lhemmeeidy drdgtvslee wiqggmttip llvllglenn vkddgqhvwr
      241 lkhfnkpayc nlclnmligv gkqglccsfc kytvhercva rappscikty vkskkntdvm
      301 hhywvegncp tkcdkchktv kcyqgltglh cvwcqttlhn kcashlkpec dcgplkdhil
      361 pptticpvvl tmpsagasvp eerqstakke ksssqqpnka tdknkmqran svtmdgqglq
      421 itpvpgthpl lvfvnpksgg kqgeriyrkf qyllnprqvy slsgngpmpg lhffrdvpdf
      481 rvlacggdgt vgwildciek anvvkhppva ilplgtgndl arclrwgggy egenlmkilk
      541 diessteiml drwkfevtpn dkdekgdpvp ysiinnyfsi gvdasiahrf himrekhpek
      601 fnsrmknkfw yfefgtsetf satckklhes veiecdgvqi dlinislegi ailnipsmhg
      661 gsnlwgeskk krshrriekk gsdkrptltd akelkfasqd lsdqllevvg legamemgqi
      721 ytglksagrr laqcssvvir tskslpmqid gepwmqtpct ikithknqap mlmgpppktg
      781 lfcslikrtr nrske
//
LOCUS       NP_659061               1810 aa            linear   ROD 27-APR-2025
DEFINITION  trinucleotide repeat-containing gene 6B protein isoform 1 [Mus
            musculus].
ACCESSION   NP_659061
VERSION     NP_659061.2
DBSOURCE    REFSEQ: accession NM_144812.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1810)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1810)
  AUTHORS   Parras,A., Anta,H., Santos-Galindo,M., Swarup,V., Elorza,A.,
            Nieto-Gonzalez,J.L., Pico,S., Hernandez,I.H., Diaz-Hernandez,J.I.,
            Belloc,E., Rodolosse,A., Parikshak,N.N., Penagarikano,O.,
            Fernandez-Chacon,R., Irimia,M., Navarro,P., Geschwind,D.H.,
            Mendez,R. and Lucas,J.J.
  TITLE     Autism-like phenotype and risk gene mRNA deadenylation by CPEB4
            mis-splicing
  JOURNAL   Nature 560 (7719), 441-446 (2018)
   PUBMED   30111840
REFERENCE   3  (residues 1 to 1810)
  AUTHORS   Guo,H., Kazadaeva,Y., Ortega,F.E., Manjunath,N. and Desai,T.J.
  TITLE     Trinucleotide repeat containing 6c (TNRC6c) is essential for
            microvascular maturation during distal airspace sacculation in the
            developing lung
  JOURNAL   Dev Biol 430 (1), 214-223 (2017)
   PUBMED   28811219
REFERENCE   4  (residues 1 to 1810)
  AUTHORS   Nakahara,M., Tateyama,H., Araki,M., Nakagata,N., Yamamura,K. and
            Araki,K.
  TITLE     Gene-trap mutagenesis using Mol/MSM-1 embryonic stem cells from
            MSM/Ms mice
  JOURNAL   Mamm Genome 24 (5-6), 228-239 (2013)
   PUBMED   23604909
REFERENCE   5  (residues 1 to 1810)
  AUTHORS   Jiang,Z., Yu,N., Kuang,P., Chen,M., Shao,F., Martin,G., Chui,D.H.,
            Cardoso,W.V., Ai,X. and Lu,J.
  TITLE     Trinucleotide repeat containing 6a (Tnrc6a)-mediated microRNA
            function is required for development of yolk sac endoderm
  JOURNAL   J Biol Chem 287 (8), 5979-5987 (2012)
   PUBMED   22187428
REFERENCE   6  (residues 1 to 1810)
  AUTHORS   Taniwaki,T., Haruna,K., Nakamura,H., Sekimoto,T., Oike,Y.,
            Imaizumi,T., Saito,F., Muta,M., Soejima,Y., Utoh,A., Nakagata,N.,
            Araki,M., Yamamura,K. and Araki,K.
  TITLE     Characterization of an exchangeable gene trap using pU-17 carrying
            a stop codon-beta geo cassette
  JOURNAL   Dev Growth Differ 47 (3), 163-172 (2005)
   PUBMED   15840001
REFERENCE   7  (residues 1 to 1810)
  AUTHORS   Sharov,A.A., Piao,Y., Matoba,R., Dudekula,D.B., Qian,Y.,
            VanBuren,V., Falco,G., Martin,P.R., Stagg,C.A., Bassey,U.C.,
            Wang,Y., Carter,M.G., Hamatani,T., Aiba,K., Akutsu,H., Sharova,L.,
            Tanaka,T.S., Kimber,W.L., Yoshikawa,T., Jaradat,S.A., Pantano,S.,
            Nagaraja,R., Boheler,K.R., Taub,D., Hodes,R.J., Longo,D.L.,
            Schlessinger,D., Keller,J., Klotz,E., Kelsoe,G., Umezawa,A.,
            Vescovi,A.L., Rossant,J., Kunath,T., Hogan,B.L., Curci,A.,
            D'Urso,M., Kelso,J., Hide,W. and Ko,M.S.
  TITLE     Transcriptome analysis of mouse stem cells and early embryos
  JOURNAL   PLoS Biol 1 (3), E74 (2003)
   PUBMED   14691545
REFERENCE   8  (residues 1 to 1810)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Aizawa,H., Yuasa,S.,
            Nakajima,D., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: II. The complete nucleotide sequences of 400 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (1), 35-48 (2003)
   PUBMED   12693553
REFERENCE   9  (residues 1 to 1810)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 1810)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC126682.3 and AC125540.4.
            
            On Jun 15, 2005 this sequence version replaced NP_659061.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and it encodes the longer protein (isoform 1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR10223970.17742.1,
                                           SRR10223971.15424.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1810
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 37.91 cM"
     Protein         1..1810
                     /product="trinucleotide repeat-containing gene 6B protein
                     isoform 1"
                     /note="trinucleotide repeat-containing gene 6B protein"
                     /calculated_mol_wt=191833
     Region          1..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          37..1028
                     /region_name="Interaction with argonaute proteins.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          235..1080
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          <371..>627
                     /region_name="ser_rich_anae_1"
                     /note="serine-rich protein; NF033849"
                     /db_xref="CDD:468206"
     Site            913
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPQ9; propagated from
                     UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          979..1094
                     /region_name="Ago_hook"
                     /note="Argonaute hook; pfam10427"
                     /db_xref="CDD:463088"
     Region          1141..1196
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          1191..1700
                     /region_name="Silencing domain, interaction with CNOT1 and
                     PAN3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          1293..1329
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          1344..1622
                     /region_name="TNRC6-PABC_bdg"
                     /note="TNRC6-PABC binding domain; pfam16608"
                     /db_xref="CDD:465195"
     Site            1409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Site            1426
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Site            1438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Site            1441
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          1449..1467
                     /region_name="PABPC1-interacting motif-2 (PAM2).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          1568..1619
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          1624..1706
                     /region_name="RRM_TNRC6B"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     trinucleotide repeat-containing gene 6B protein (TNRC6B);
                     cd12712"
                     /db_xref="CDD:410111"
     Region          1706..1740
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Region          1786..1810
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Site            1793
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPQ9; propagated from
                     UniProtKB/Swiss-Prot (Q8BKI2.2)"
     Site            1809
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPQ9; propagated from
                     UniProtKB/Swiss-Prot (Q8BKI2.2)"
     CDS             1..1810
                     /gene="Tnrc6b"
                     /gene_synonym="2700090M07Rik; A730065C02Rik;
                     D230019K20Rik"
                     /coded_by="NM_144812.3:291..5723"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS37146.1"
                     /db_xref="GeneID:213988"
                     /db_xref="MGI:MGI:2443730"
ORIGIN      
        1 mqtnegevee esssqveqed fvmeghgktp ppgeeskqek eqereeqlme dkkrkkedkk
       61 kkeatqkvte qktkvpevtk pslsqptaas pigsspsppv nggnnakrva vpngqppsaa
      121 rymprevppr frcqqdhkvl lkrgqpppps cmllgggagp ppctapganp nnnaqvtgal
      181 lqsesgtape stlggaaasn yanstwgpga ssnsgaspnp ihiwdkvivd gsdmeewpci
      241 askdtessse nttdnnsasn pgseksslpg sttsnkgkgs qcqaassgne cnlgvwksdp
      301 kaksvqppns tsdsnnglgn wrstsgqdri gpgsgfsnfn pnsnpsawpa lvqegtsrkg
      361 aletesssss aqvstvgqas reqqskmena gvnfvvsgre qaqihntdgp kngntnslnl
      421 sspnpmenkg mpfgmglgnt srstdapsqs tgdrktgsvg swgaargpsg tdtvsgqsns
      481 gnngnngkdr edswkgasvp kptgsksdsw dnnnrstggs wnfgpqdnnd nkwgegnkmt
      541 sgvsqgewkq ptgsdelkig ewsgpnqpns stgawdnqkg hplpenqgna qapcwgrsss
      601 sagsevggqs tgsnhkagss dshnsgrrsy rpthpdcqav lqtllsrtdl dprvlsntgw
      661 gqtqikqdtv wdieevprpe gksdkgtegw esaatqtkns ggwgdapsqs nqmksgwgel
      721 sastewkdpk stggwndykn nnssnwgggr adektpsswn essckdqgwg ggrqpnqgwt
      781 sgkngwgeev dqvknnnwes sankpvsgwg eggqneigtw gnggntnlas kggwedckrs
      841 pawnetgrqp nswnkqhqqq qqppppqpea sgswggpppp pqgnvrpsns nwssgpqptt
      901 pkddepsgwe epspqsisrk mdiddgtsaw gdpnsynykn vnlwdknsqg gpaprepnlp
      961 tpmtgksasv wskstppapd ngtsawgepn esspgwgemd dagasttgwg ntpanapnam
     1021 kpnsksmqdg wgesdgpvtg arhpsweeed dggvwntags qgstsshnsa swgqggkkqm
     1081 kcslkggnnd swmnplakqf snmgllsqte dnpsskmdls vdkkfdvdkr tmnlgdfndi
     1141 mrkdrpgfrp pnskdlgttd sgpyfekggs hglfgnstaq srglhtpvqp lssspglraq
     1201 vppqfispqv sasmlkqfpn sglnpglfnv gpqlspqqia mlsqlpqipq fqlacqlllq
     1261 qqqqqqqllq nqrkisqavr qqqeqqlarm vsalqqqqqq qqqqqrqpsm khspshpvgp
     1321 kphldnmvpn alnvglpdlp tkgpipgygs gfssggmdyg mvggkeagte srfkqwtsmm
     1381 eglpsvatqe atmhkngaiv apgktrggsp ynqfdiipgd tlgghtgpag dswlpakspp
     1441 tnkigskssn aswppefqpg vpwkgiqnid pesdpyvtpg svlggtttsp ivdtdhqllr
     1501 dnttgsnssl ntslpspgaw pysasdnsft nvhstsakfp dykstwspdp ighnpthlsn
     1561 kmwknhissr nttpltrppp gltnpkpasp wsstaprsvr gwgtqdsria sastwsdggs
     1621 vrpsywlvlh nltpqidgst lrticmqhgp lltfhlnltq gtalirystk qeaakaqtal
     1681 hmcvlgntti laefatedev srflaqaqpp tpaatpsapa tgwqsletsq nqadpvgpal
     1741 nlfggstglg qwsssaggss gadlagtslw gppnyssslw gvptvedphr mgspapllpg
     1801 dllgggsdsi
//
LOCUS       NP_004835                455 aa            linear   PRI 27-APR-2025
DEFINITION  SH3 domain-binding protein 5 isoform a [Homo sapiens].
ACCESSION   NP_004835
VERSION     NP_004835.2
DBSOURCE    REFSEQ: accession NM_004844.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Zhang,B., Qian,R. and Li,X.
  TITLE     METTL3 suppresses invasion of lung cancer via SH3BP5 m6A
            modification
  JOURNAL   Arch Biochem Biophys 752, 109876 (2024)
   PUBMED   38141906
  REMARK    GeneRIF: METTL3 suppresses invasion of lung cancer via SH3BP5 m6A
            modification.
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Qiao,R., Zhong,R., Liu,C., Di,F., Zhang,Z., Wang,L., Xu,T.,
            Wang,Y., Dai,L., Gu,W., Han,B. and Yang,R.
  TITLE     Novel blood-based hypomethylation of SH3BP5 is associated with very
            early-stage lung adenocarcinoma
  JOURNAL   Genes Genomics 44 (4), 445-453 (2022)
   PUBMED   34783986
  REMARK    GeneRIF: Novel blood-based hypomethylation of SH3BP5 is associated
            with very early-stage lung adenocarcinoma.
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Chandrakumar,A.A., Coyaud,E., Marshall,C.B., Ikura,M., Raught,B.
            and Rottapel,R.
  TITLE     Tankyrase regulates epithelial lumen formation via suppression of
            Rab11 GEFs
  JOURNAL   J Cell Biol 220 (7) (2021)
   PUBMED   34128958
  REMARK    GeneRIF: Tankyrase regulates epithelial lumen formation via
            suppression of Rab11 GEFs.
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Hirata,Y., Inoue,A., Suzuki,S., Takahashi,M., Matsui,R., Kono,N.,
            Noguchi,T. and Matsuzawa,A.
  TITLE     trans-Fatty acids facilitate DNA damage-induced apoptosis through
            the mitochondrial JNK-Sab-ROS positive feedback loop
  JOURNAL   Sci Rep 10 (1), 2743 (2020)
   PUBMED   32066809
  REMARK    GeneRIF: trans-Fatty acids facilitate DNA damage-induced apoptosis
            through the mitochondrial JNK-Sab-ROS positive feedback loop.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Court,N.W., Kuo,I., Quigley,O. and Bogoyevitch,M.A.
  TITLE     Phosphorylation of the mitochondrial protein Sab by
            stress-activated protein kinase 3
  JOURNAL   Biochem Biophys Res Commun 319 (1), 130-137 (2004)
   PUBMED   15158451
  REMARK    GeneRIF: mitochondrial protein Sab is phosphorylated by
            stress-activated protein kinase 3
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Wiltshire,C., Matsushita,M., Tsukada,S., Gillespie,D.A. and
            May,G.H.
  TITLE     A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab
            (SH3BP5), associates with mitochondria
  JOURNAL   Biochem J 367 (Pt 3), 577-585 (2002)
   PUBMED   12167088
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Yamadori,T., Baba,Y., Matsushita,M., Hashimoto,S., Kurosaki,M.,
            Kurosaki,T., Kishimoto,T. and Tsukada,S.
  TITLE     Bruton's tyrosine kinase activity is negatively regulated by Sab,
            the Btk-SH3 domain-binding protein
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6341-6346 (1999)
   PUBMED   10339589
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Baba,Y., Matsushita,M., Matsuda,Y., Inazawa,J., Yamadori,T.,
            Hashimoto,S., Kishimoto,T. and Tsukada,S.
  TITLE     Assignment of SH3BP5/Sh3bp5 encoding sab, an SH3 domain-binding
            protein which preferentially associates with Bruton's tyrosine
            kinase, to human chromosome 1q43 and mouse chromosome 14B by in
            situ hybridization
  JOURNAL   Cytogenet Cell Genet 87 (3-4), 221-222 (1999)
   PUBMED   10702676
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Matsushita,M., Yamadori,T., Kato,S., Takemoto,Y., Inazawa,J.,
            Baba,Y., Hashimoto,S., Sekine,S., Arai,S., Kunikata,T.,
            Kurimoto,M., Kishimoto,T. and Tsukada,S.
  TITLE     Identification and characterization of a novel SH3-domain binding
            protein, Sab, which preferentially associates with Bruton's
            tyrosine kinase (BtK)
  JOURNAL   Biochem Biophys Res Commun 245 (2), 337-343 (1998)
   PUBMED   9571151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP308415.1, AB005047.1 and CA429664.1.
            
            On Jun 15, 2006 this sequence version replaced NP_004835.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313167.1, SRR1803611.15222.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000383791.8/ ENSP00000373301.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..455
                     /product="SH3 domain-binding protein 5 isoform a"
                     /note="SH3 domain-binding protein that preferentially
                     associates with BTK; SH3-domain binding protein 5
                     (BTK-associated)"
                     /calculated_mol_wt=50294
     Region          1..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60239.2)"
     Region          31..265
                     /region_name="Sufficient for interaction with RAB11A and
                     for guanine nucleotide exchange activity.
                     /evidence=ECO:0000269|PubMed:30217979"
                     /note="propagated from UniProtKB/Swiss-Prot (O60239.2)"
     Region          41..269
                     /region_name="SH3BP5"
                     /note="SH3 domain-binding protein 5 (SH3BP5); pfam05276"
                     /db_xref="CDD:461608"
     Region          259..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60239.2)"
     Region          306..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60239.2)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK12 and MAPK9.
                     /evidence=ECO:0000250|UniProtKB:Q91Y80; propagated from
                     UniProtKB/Swiss-Prot (O60239.2)"
     Region          369..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60239.2)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z131; propagated from
                     UniProtKB/Swiss-Prot (O60239.2)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z131; propagated from
                     UniProtKB/Swiss-Prot (O60239.2)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91Y80; propagated from
                     UniProtKB/Swiss-Prot (O60239.2)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60239.2)"
     CDS             1..455
                     /gene="SH3BP5"
                     /gene_synonym="SAB; SH3BP-5"
                     /coded_by="NM_004844.5:179..1546"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2625.2"
                     /db_xref="GeneID:9467"
                     /db_xref="HGNC:HGNC:10827"
                     /db_xref="MIM:605612"
ORIGIN      
        1 mdaalkrsrs eepaeilppa rdeeeeeeeg meqgleeeee vdpriqgele klnqstddin
       61 rreteledar qkfrsvlvea tvkldelvkk igkavedskp ywearrvarq aqleaqkatq
      121 dfqratevlr aaketislae qrlleddkrq fdsawqemln hatqrvmeae qtktrselvh
      181 ketaarynaa mgrmrqlekk lkrainkskp yfelkakyyv qleqlkktvd dlqakltlak
      241 geykmalknl emisdeiher rrssamgprg cgvgaegsst svedlpgskp epdaisvase
      301 afeddscsnf vseddsetqs vssfssgpts psempdqfpa vvrpgsldlp spvslsefgm
      361 mfpvlgprse csgasspece vergdraega enktsdkann nrglssssgs ggssksqsst
      421 spegqalenr mkqlslqcsk grdgiiadik mvqig
//
LOCUS       NP_780315                311 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 177 [Mus musculus].
ACCESSION   NP_780315
VERSION     NP_780315.1
DBSOURCE    REFSEQ: accession NM_175106.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BB578893.1 and BC094344.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094344.1, SRR7974084.8821.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849390 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 52.53 cM"
     Protein         1..311
                     /product="transmembrane protein 177"
                     /calculated_mol_wt=33936
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BPE4.1)"
     Site            165..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BPE4.1)"
     Site            191..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BPE4.1)"
     CDS             1..311
                     /gene="Tmem177"
                     /gene_synonym="2300008B03Rik"
                     /coded_by="NM_175106.4:259..1194"
                     /db_xref="CCDS:CCDS15228.1"
                     /db_xref="GeneID:66343"
                     /db_xref="MGI:MGI:1913593"
ORIGIN      
        1 magplwraaa fiqrhrtsll vgscaglfgv qisfhlfpdp ivqwlyqywp qgqpaplsph
       61 lwslfqevlk digvpsghcy kpftaftfqp vsagfprlpa gavvgipaif lggpvtnieh
      121 sviihgqrvd wqspagtrlr daltmshnaq kfalakevvy lesgvaalqt lpapaclagt
      181 waisvgakha lglyggpmsl rtafnlvaiv vgyvaytfsk dsltlalegw ldrrtaslsa
      241 ayvqggvefy ekilsgnlal rsllgrqgek lytpsgnivp rhwfrinhlp yttrrdslqq
      301 mwratvspgr f
//
LOCUS       NP_001074690            1481 aa            linear   ROD 27-APR-2025
DEFINITION  DNA excision repair protein ERCC-6 [Mus musculus].
ACCESSION   NP_001074690 NP_796017 XP_484360
VERSION     NP_001074690.1
DBSOURCE    REFSEQ: accession NM_001081221.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1481)
  AUTHORS   Mulderrig,L., Garaycoechea,J.I., Tuong,Z.K., Millington,C.L.,
            Dingler,F.A., Ferdinand,J.R., Gaul,L., Tadross,J.A., Arends,M.J.,
            O'Rahilly,S., Crossan,G.P., Clatworthy,M.R. and Patel,K.J.
  TITLE     Aldehyde-driven transcriptional stress triggers an anorexic DNA
            damage response
  JOURNAL   Nature 600 (7887), 158-163 (2021)
   PUBMED   34819667
REFERENCE   2  (residues 1 to 1481)
  AUTHORS   Okur,M.N., Fang,E.F., Fivenson,E.M., Tiwari,V., Croteau,D.L. and
            Bohr,V.A.
  TITLE     Cockayne syndrome proteins CSA and CSB maintain mitochondrial
            homeostasis through NAD+ signaling
  JOURNAL   Aging Cell 19 (12), e13268 (2020)
   PUBMED   33166073
REFERENCE   3  (residues 1 to 1481)
  AUTHORS   Collin,G.B., Gogna,N., Chang,B., Damkham,N., Pinkney,J., Hyde,L.F.,
            Stone,L., Naggert,J.K., Nishina,P.M. and Krebs,M.P.
  TITLE     Mouse Models of Inherited Retinal Degeneration with Photoreceptor
            Cell Loss
  JOURNAL   Cells 9 (4), 931 (2020)
   PUBMED   32290105
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1481)
  AUTHORS   Mulderrig,L. and Garaycoechea,J.I.
  TITLE     XPF-ERCC1 protects liver, kidney and blood homeostasis outside the
            canonical excision repair pathways
  JOURNAL   PLoS Genet 16 (4), e1008555 (2020)
   PUBMED   32271760
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1481)
  AUTHORS   Hill,R.J. and Crossan,G.P.
  TITLE     DNA cross-link repair safeguards genomic stability during
            premeiotic germ cell development
  JOURNAL   Nat Genet 51 (8), 1283-1294 (2019)
   PUBMED   31367016
REFERENCE   6  (residues 1 to 1481)
  AUTHORS   Okada,K., Fujita,T., Minamoto,K., Liao,H., Naka,Y. and Pinsky,D.J.
  TITLE     Potentiation of endogenous fibrinolysis and rescue from lung
            ischemia/reperfusion injury in interleukin (IL)-10-reconstituted
            IL-10 null mice
  JOURNAL   J Biol Chem 275 (28), 21468-21476 (2000)
   PUBMED   10806208
REFERENCE   7  (residues 1 to 1481)
  AUTHORS   Garssen,J., van Steeg,H., de Gruijl,F., de Boer,J., van der
            Horst,G.T., van Kranen,H., van Loveren,H., van Dijk,M.,
            Fluitman,A., Weeda,G. and Hoeijmakers,J.H.
  TITLE     Transcription-coupled and global genome repair differentially
            influence UV-B-induced acute skin effects and systemic
            immunosuppression
  JOURNAL   J Immunol 164 (12), 6199-6205 (2000)
   PUBMED   10843671
REFERENCE   8  (residues 1 to 1481)
  AUTHORS   de Boer,J., van Steeg,H., Berg,R.J., Garssen,J., de Wit,J., van
            Oostrum,C.T., Beems,R.B., van der Horst,G.T., van Kreijl,C.F., de
            Gruijl,F.R., Bootsma,D., Hoeijmakers,J.H. and Weeda,G.
  TITLE     Mouse model for the DNA repair/basal transcription disorder
            trichothiodystrophy reveals cancer predisposition
  JOURNAL   Cancer Res 59 (14), 3489-3494 (1999)
   PUBMED   10416615
REFERENCE   9  (residues 1 to 1481)
  AUTHORS   Jacobs,H., Fukita,Y., van der Horst,G.T., de Boer,J., Weeda,G.,
            Essers,J., de Wind,N., Engelward,B.P., Samson,L., Verbeek,S., de
            Murcia,J.M., de Murcia,G., te Riele,H. and Rajewsky,K.
  TITLE     Hypermutation of immunoglobulin genes in memory B cells of DNA
            repair-deficient mice
  JOURNAL   J Exp Med 187 (11), 1735-1743 (1998)
   PUBMED   9607915
REFERENCE   10 (residues 1 to 1481)
  AUTHORS   van der Horst,G.T., van Steeg,H., Berg,R.J., van Gool,A.J., de
            Wit,J., Weeda,G., Morreau,H., Beems,R.B., van Kreijl,C.F., de
            Gruijl,F.R., Bootsma,D. and Hoeijmakers,J.H.
  TITLE     Defective transcription-coupled repair in Cockayne syndrome B mice
            is associated with skin cancer predisposition
  JOURNAL   Cell 89 (3), 425-435 (1997)
   PUBMED   9150142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC154412.3.
            
            On or before Apr 17, 2018 this sequence version replaced
            NP_796017.1, XP_484360.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR10223971.14107.1,
                                           SRR13948564.893393.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1481
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 19.4 cM"
     Protein         1..1481
                     /product="DNA excision repair protein ERCC-6"
                     /note="CS group B correcting; ATP-dependent helicase
                     ERCC6; cockayne syndrome protein CSB"
                     /calculated_mol_wt=165828
     Region          1..506
                     /region_name="N-terminal domain, essential for its
                     chromatin remodeling activity.
                     /evidence=ECO:0000250|UniProtKB:Q03468"
                     /note="propagated from UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          83..159
                     /region_name="cc_ERCC-6_N"
                     /note="coiled-coil domain located near the N-terminus of
                     human Excision Repair Cross Complementing 6 (ERCC-6) and
                     related proteins; cd21397"
                     /db_xref="CDD:411064"
     Site            order(114,118)
                     /site_type="other"
                     /note="Mg binding site [ion binding]"
                     /db_xref="CDD:411064"
     Region          <122..>199
                     /region_name="46"
                     /note="endonuclease subunit; Provisional; PHA02562"
                     /db_xref="CDD:222878"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000250|UniProtKB:Q03468; propagated from
                     UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Site            170
                     /site_type="methylation"
                     /note="N6-methylated lysine, by EHMT2.
                     /evidence=ECO:0000250|UniProtKB:Q03468; propagated from
                     UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          280..983
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Site            298
                     /site_type="methylation"
                     /note="N6-methylated lysine, by EHMT2.
                     /evidence=ECO:0000250|UniProtKB:Q03468; propagated from
                     UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          309..452
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03468; propagated from
                     UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03468; propagated from
                     UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Site            444
                     /site_type="methylation"
                     /note="N6-methylated lysine, by EHMT2.
                     /evidence=ECO:0000250|UniProtKB:Q03468; propagated from
                     UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03468; propagated from
                     UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03468; propagated from
                     UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          642..645
                     /region_name="DEAH box.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00541"
                     /note="propagated from UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          1040..1096
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Site            1047
                     /site_type="methylation"
                     /note="N6-methylated lysine, by EHMT2.
                     /evidence=ECO:0000250|UniProtKB:Q03468; propagated from
                     UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          1114..1238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          1307..1372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          1373..1385
                     /region_name="CSA-interacting motif (CIM).
                     /evidence=ECO:0000250|UniProtKB:Q03468"
                     /note="propagated from UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          1387..1416
                     /region_name="Ubiquitin-binding domain (UBD).
                     /evidence=ECO:0000250|UniProtKB:Q03468"
                     /note="propagated from UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          1410..1480
                     /region_name="CSB_WHD"
                     /note="winged-helix domain (WHD) found in cockayne
                     syndrome group B (CSB) and similar proteins; cd22254"
                     /db_xref="CDD:439329"
     Site            order(1410,1413..1414,1416..1417,1420,1424..1425,
                     1430..1431,1460,1478..1480)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:439329"
     Region          1417..1481
                     /region_name="Winged-helix domain (WHD).
                     /evidence=ECO:0000250|UniProtKB:Q03468"
                     /note="propagated from UniProtKB/Swiss-Prot (F8VPZ5.1)"
     Region          1434..1481
                     /region_name="Essential for its interaction with RNA
                     polymerase II, transcription-coupled nucleotide excision
                     repair activity, association with chromatin after UV
                     irradiation and for mediating the UV-induced translocation
                     of ERRC8 to the nuclear matrix.
                     /evidence=ECO:0000250|UniProtKB:Q03468"
                     /note="propagated from UniProtKB/Swiss-Prot (F8VPZ5.1)"
     CDS             1..1481
                     /gene="Ercc6"
                     /gene_synonym="4732403I04; C130058G22Rik; CSB"
                     /coded_by="NM_001081221.2:90..4535"
                     /db_xref="CCDS:CCDS36868.1"
                     /db_xref="GeneID:319955"
                     /db_xref="MGI:MGI:1100494"
ORIGIN      
        1 mfheevpnst hpqeqdclps qhanaykdmp vgqenggvse ageclsstsc eygpstsaea
       61 cvlaatrrgp tllhidrhqi pavepsaqal elqglgvdvy dqavleqgvl qqvdsamhea
      121 scvaqladae keyqsvlddl mscttslrqi nkiieqlspq aasnrdinrk ldsvkrqkyn
      181 keqqlkkita kqkrlqailg gagvqveldh asleeddaep gpsclgsmlm paqetaweel
      241 irtgqmtpfg tpapqkqekk prkimlneas gfekylaeqa qlsferkkqa atkrtakkai
      301 visessraai etkadqrsqv lsqtdkrlkk hsrklqrral qfqgkvglps gkkplepevr
      361 peaegdtege esgssptdge eeeeqeeeeg vaslssddvs yelkplrkrq kyqkkvpvqe
      421 idddffpsse eedeamegrg ggrkvarrqd dgdedyykqr lrrwnrlrlq dkekrlkled
      481 dseesdaefd egfkvpgflf kklfkyqqtg vrwlwelhcq qaggilgdem glgktiqiia
      541 flaglsyski rtrgsnyrfe glgptiivcp ttvmhqwvke fhtwwppfrv avlhetgsyt
      601 hkkerlirdi vychgvlits ysyirlmqdd isrhdwhyvi ldeghkirnp naavtlackq
      661 frtphriils gspmqnnlre lwslfdfifp gklgtlpvfm eqfsvpitmg gysnaspvqv
      721 ktaykcacvl rdtinpyllr rmksdvkmsl slpdkneqvl fcrltdeqhk vyqnfidska
      781 vyrilngenq ifsglvalrk icnhpdlfsg gpknasgppe deleeeqfgh wrrsgkmivv
      841 esllkiwhrq gqrvllfsqs rqmlhilevf lrahkysylk mdgtttiasr qplitkyned
      901 tsifvflltt rvgglgvnlt ganrviiydp dwnpstdtqa rerawrigqk kqvtvyrllt
      961 agtieekiyh rqifkqfltn rvlkdpkqrr ffksndlyel ftltspdasq gtetsaifag
     1021 tgssiqtpkc qlkkrtstvl gtdpkckkpp vsdtpanaat ligekpkaag atgrsvtsge
     1081 sgpfkgdhdt ngnrassvaf geetdagstl ehlsvmsgdg khsdsptvdh tsrppveast
     1141 sekqgssyag arcqaqtepv pmseqmegqf skykskrkhd aseeettekr pqpkqkakns
     1201 khcrdakfeg trvphlvkkr ryrqqtseqe ggakdrssdd yvleklfkks vgvhsvvrhd
     1261 aiidgsspdy vlveaeanrv aqdalkalrl srqqclgaas gvptwtghrg isgaptgvkn
     1321 rfgqkrdssl pvqhpsslte ktqnnmkkeg kahtpehfsg kedgasvsga pssssllarm
     1381 rarnhmilpe rlesdsehla eaaavppcgt ehddllvdmr nfiafqaqvd gqastqeilq
     1441 efesklsvaq scvfrellrn lcnfhrtpgg egiwklkpey c
//
LOCUS       NP_055619                967 aa            linear   PRI 27-APR-2025
DEFINITION  protein moonraker isoform 1 [Homo sapiens].
ACCESSION   NP_055619 XP_375397
VERSION     NP_055619.2
DBSOURCE    REFSEQ: accession NM_014804.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 967)
  AUTHORS   Inskeep,K.A., Zarate,Y.A., Monteil,D., Spranger,J., Doherty,D.,
            Stottmann,R.W. and Weaver,K.N.
  TITLE     Genetic and phenotypic heterogeneity in KIAA0753-related
            ciliopathies
  JOURNAL   Am J Med Genet A 188 (1), 104-115 (2022)
   PUBMED   34523780
  REMARK    GeneRIF: Genetic and phenotypic heterogeneity in KIAA0753-related
            ciliopathies.
REFERENCE   2  (residues 1 to 967)
  AUTHORS   Chang,C.H., Chen,T.Y., Lu,I.L., Li,R.B., Tsai,J.J., Lin,P.Y. and
            Tang,T.K.
  TITLE     CEP120-mediated KIAA0753 recruitment onto centrioles is required
            for timely neuronal differentiation and germinal zone exit in the
            developing cerebellum
  JOURNAL   Genes Dev 35 (21-22), 1445-1460 (2021)
   PUBMED   34711653
  REMARK    GeneRIF: CEP120-mediated KIAA0753 recruitment onto centrioles is
            required for timely neuronal differentiation and germinal zone exit
            in the developing cerebellum.
REFERENCE   3  (residues 1 to 967)
  AUTHORS   Kumar,D., Rains,A., Herranz-Perez,V., Lu,Q., Shi,X., Swaney,D.L.,
            Stevenson,E., Krogan,N.J., Huang,B., Westlake,C.,
            Garcia-Verdugo,J.M., Yoder,B.K. and Reiter,J.F.
  TITLE     A ciliopathy complex builds distal appendages to initiate
            ciliogenesis
  JOURNAL   J Cell Biol 220 (9) (2021)
   PUBMED   34241634
  REMARK    GeneRIF: A ciliopathy complex builds distal appendages to initiate
            ciliogenesis.
REFERENCE   4  (residues 1 to 967)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 967)
  AUTHORS   Hammarsjo,A., Wang,Z., Vaz,R., Taylan,F., Sedghi,M., Girisha,K.M.,
            Chitayat,D., Neethukrishna,K., Shannon,P., Godoy,R.,
            Gowrishankar,K., Lindstrand,A., Nasiri,J., Baktashian,M.,
            Newton,P.T., Guo,L., Hofmeister,W., Pettersson,M., Chagin,A.S.,
            Nishimura,G., Yan,L., Matsumoto,N., Nordgren,A., Miyake,N.,
            Grigelioniene,G. and Ikegawa,S.
  TITLE     Novel KIAA0753 mutations extend the phenotype of skeletal
            ciliopathies
  JOURNAL   Sci Rep 7 (1), 15585 (2017)
   PUBMED   29138412
  REMARK    GeneRIF: We demonstrate that KIAA0753 is expressed in normal fetal
            human growth plate and show that the affected fetus, with a
            compound heterozygous frameshift and a nonsense mutation in
            KIAA0753, has an abnormal proliferative zone and a broad
            hypertrophic zone.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 967)
  AUTHORS   Chevrier,V., Bruel,A.L., Van Dam,T.J., Franco,B., Lo Scalzo,M.,
            Lembo,F., Audebert,S., Baudelet,E., Isnardon,D., Bole,A.,
            Borg,J.P., Kuentz,P., Thevenon,J., Burglen,L., Faivre,L.,
            Riviere,J.B., Huynen,M.A., Birnbaum,D., Rosnet,O. and
            Thauvin-Robinet,C.
  TITLE     OFIP/KIAA0753 forms a complex with OFD1 and FOR20 at pericentriolar
            satellites and centrosomes and is mutated in one individual with
            oral-facial-digital syndrome
  JOURNAL   Hum Mol Genet 25 (3), 497-513 (2016)
   PUBMED   26643951
REFERENCE   7  (residues 1 to 967)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   8  (residues 1 to 967)
  AUTHORS   Kodani,A., Yu,T.W., Johnson,J.R., Jayaraman,D., Johnson,T.L.,
            Al-Gazali,L., Sztriha,L., Partlow,J.N., Kim,H., Krup,A.L.,
            Dammermann,A., Krogan,N.J., Walsh,C.A. and Reiter,J.F.
  TITLE     Centriolar satellites assemble centrosomal microcephaly proteins to
            recruit CDK2 and promote centriole duplication
  JOURNAL   Elife 4, e07519 (2015)
   PUBMED   26297806
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 967)
  AUTHORS   Firat-Karalar,E.N., Rauniyar,N., Yates,J.R. 3rd and Stearns,T.
  TITLE     Proximity interactions among centrosome components identify
            regulators of centriole duplication
  JOURNAL   Curr Biol 24 (6), 664-670 (2014)
   PUBMED   24613305
REFERENCE   10 (residues 1 to 967)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB075150.1, BC113016.1,
            AB018296.1, AL080108.1 and AC015916.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 3, 2007 this sequence version replaced NP_055619.1.
            
            Summary: This gene encodes a subunit of a protein complex that
            regulates ciliogenesis and cilia maintenance. The encoded protein
            has also been shown to regulate centriolar duplication. Mutations
            in this gene cause an orofaciodigital syndrome and a form of
            Joubert syndrome in human patients. [provided by RefSeq, May 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB018296.1, AK292876.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361413.8/ ENSP00000355250.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..967
                     /product="protein moonraker isoform 1"
                     /note="protein moonraker; OFD1 and FOPNL interacting
                     protein; OFD1 and FOR20 interacting protein"
                     /calculated_mol_wt=109276
     Region          1..962
                     /region_name="MNR"
                     /note="Protein moonraker; pfam15718"
                     /db_xref="CDD:464822"
     Region          178..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHM9.3)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHM9.3)"
     Region          401..431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHM9.3)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHM9.3)"
     Region          490..601
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHM9.3)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHM9.3)"
     Site            826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHM9.3)"
     Region          849..872
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHM9.3)"
     Region          885..967
                     /region_name="Necessary and sufficient for CEP20-binding.
                     /evidence=ECO:0000269|PubMed:26643951"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHM9.3)"
     CDS             1..967
                     /gene="KIAA0753"
                     /gene_synonym="JBTS38; MNR; OFIP; SRTD21"
                     /coded_by="NM_014804.3:144..3047"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42247.1"
                     /db_xref="GeneID:9851"
                     /db_xref="HGNC:HGNC:29110"
                     /db_xref="MIM:617112"
ORIGIN      
        1 mgpgqpastc vhlaprtqld grsdpkvlqt qnqlqfnrnv pthssnlair yscphairie
       61 klkhsynesy hckdadcrvg pdlgssvsfs visqerlsya vhlarrdvkr rqfekhikeh
      121 hlrsqpqssq kcghtkykip dhrverkesk sqaacqcshq pskveisssg akvylysshp
      181 gqsdltvpns ppthdpglqp hprigdhkni seqksllevq rlqkelssci hkieevtkkd
      241 rleealdpde erririrrqe qaarsarmly vlqqqvkeiq eeldklsphk ikhtkkswam
      301 sklaaahrga iralqmfvtq ftdrgehplp arckelgsli rqlslcsvkl dadpsvpdvv
      361 idilqqieal esllekklsp kkvkkcfsei rsrfpigsqk alerwpstsp kgerrpltak
      421 dtfpqetsrp svakqlladk yqpdtelpet qrlqseldvl dadivleegp fildqsasfk
      481 devlavaktk agkkkpvten vpfrkkdtla parqqglrka ergrqsqphs ksrvqqttvs
      541 srlkmnrqpv kdrkapwipp nptsppaspk caawlkvkts prdatkeplq qedpqeeshl
      601 tgaveheaar lawldaetsk rlkeleelka keidsmqkqr ldwldaetsr rtkelnelka
      661 eemyrlqqls vsathladkv eeavldrlkp llvkaqrvns tteanihlkd gssvntakaq
      721 paqevaavdf esnnirqldd fledcaselw avthakilgs etlatvedsk dspdleimmr
      781 rmeemekyqe svrqrynkia yadprlwmqe enndqkisai sekplsphpi ritktvdrkd
      841 pavnimlerp cngnsldesv gteegsekre apllslaeds qqkegraplf vppgmqhsig
      901 dycsrfeqyl riisheavgs fnpwliaesf seelvdealg avaaelqdmc edyaeavfts
      961 efleaat
//
LOCUS       NP_062636                307 aa            linear   ROD 27-APR-2025
DEFINITION  GTP-binding protein RAD [Mus musculus].
ACCESSION   NP_062636
VERSION     NP_062636.2
DBSOURCE    REFSEQ: accession NM_019662.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Elmore,G., Ahern,B.M., McVay,N.M., Barker,K.W., Lohano,S.S.,
            Ali,N., Sebastian,A., Andres,D.A., Satin,J. and Levitan,B.M.
  TITLE     The C-terminus of Rad is required for membrane localization and
            L-type calcium channel regulation
  JOURNAL   J Gen Physiol 156 (9) (2024)
   PUBMED   38990175
  REMARK    GeneRIF: The C-terminus of Rad is required for membrane
            localization and L-type calcium channel regulation.
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Ahern,B.M., Sebastian,A., Levitan,B.M., Goh,J., Andres,D.A. and
            Satin,J.
  TITLE     L-type channel inactivation balances the increased peak calcium
            current due to absence of Rad in cardiomyocytes
  JOURNAL   J Gen Physiol 153 (9) (2021)
   PUBMED   34269819
  REMARK    GeneRIF: L-type channel inactivation balances the increased peak
            calcium current due to absence of Rad in cardiomyocytes.
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Ahern,B.M., Levitan,B.M., Veeranki,S., Shah,M., Ali,N.,
            Sebastian,A., Su,W., Gong,M.C., Li,J., Stelzer,J.E., Andres,D.A.
            and Satin,J.
  TITLE     Myocardial-restricted ablation of the GTPase RAD results in a
            pro-adaptive heart response in mice
  JOURNAL   J Biol Chem 294 (28), 10913-10927 (2019)
   PUBMED   31147441
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Zhang,P., Bai,H., Li,J., Liu,J., Ma,W., Xu,B., Xia,Q., Wang,J.,
            Fan,Yi. and Du,Q.
  TITLE     Knockdown of slincRAD leads to defective adipose development in
            vivo
  JOURNAL   Biochem Biophys Res Commun 513 (4), 983-989 (2019)
   PUBMED   31005260
  REMARK    GeneRIF: Compared to normal adipocytes, slincRAD knockdown cells
            had defective differentiation features, such as smaller sizes and
            decreased lipid production. For elder mice, slincRAD knockdown led
            to abnormal glucose and lipid metabolism.
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Yada,H., Murata,M., Shimoda,K., Yuasa,S., Kawaguchi,H., Ieda,M.,
            Adachi,T., Murata,M., Ogawa,S. and Fukuda,K.
  TITLE     Dominant negative suppression of Rad leads to QT prolongation and
            causes ventricular arrhythmias via modulation of L-type Ca2+
            channels in the heart
  JOURNAL   Circ Res 101 (1), 69-77 (2007)
   PUBMED   17525370
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Ilany,J., Bilan,P.J., Kapur,S., Caldwell,J.S., Patti,M.E.,
            Marette,A. and Kahn,C.R.
  TITLE     Overexpression of Rad in muscle worsens diet-induced insulin
            resistance and glucose intolerance and lowers plasma triglyceride
            level
  JOURNAL   Proc Natl Acad Sci U S A 103 (12), 4481-4486 (2006)
   PUBMED   16537411
  REMARK    GeneRIF: These results demonstrate a potential synergistic
            interaction between increased expression of Rad and high-fat diet
            in creation of insulin resistance and altered lipid metabolism
            present in type 2 diabetes.
REFERENCE   8  (residues 1 to 307)
  AUTHORS   Hawke,T.J., Kanatous,S.B., Martin,C.M., Goetsch,S.C. and Garry,D.J.
  TITLE     Rad is temporally regulated within myogenic progenitor cells during
            skeletal muscle regeneration
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C379-C387 (2006)
   PUBMED   16221735
REFERENCE   9  (residues 1 to 307)
  AUTHORS   Finlin,B.S., Crump,S.M., Satin,J. and Andres,D.A.
  TITLE     Regulation of voltage-gated calcium channel activity by the Rem and
            Rad GTPases
  JOURNAL   Proc Natl Acad Sci U S A 100 (24), 14469-14474 (2003)
   PUBMED   14623965
  REMARK    GeneRIF: both Rem and Rad bind directly to Ca2+ channel
            beta-subunits (CaV beta) in vivo
REFERENCE   10 (residues 1 to 307)
  AUTHORS   Shimizu-Nishikawa,K., Tsuji,S. and Yoshizato,K.
  TITLE     Identification and characterization of newt rad (ras associated
            with diabetes), a gene specifically expressed in regenerating limb
            muscle
  JOURNAL   Dev Dyn 220 (1), 74-86 (2001)
   PUBMED   11146509
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK087473.1, AK159550.1 and AI894172.1.
            
            On Sep 7, 2006 this sequence version replaced NP_062636.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057138.1, SRR7345562.1088878.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849389, SAMN01164137
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 53.04 cM"
     Protein         1..307
                     /product="GTP-binding protein RAD"
                     /EC_number="3.6.5.2"
                     /note="Ras-like GTP-binding protein rad"
                     /calculated_mol_wt=33090
     Site            23
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O88667.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O88667.1)"
     Region          91..307
                     /region_name="RGK"
                     /note="Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras
                     GTPases; cd04148"
                     /db_xref="CDD:206715"
     Site            97..104
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206715"
     Site            order(98..99,145..146)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(99..105,143,146,202..203,205,232..233)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206715"
     Site            order(104..105,117,119,126..127,140..141,143,145..146,234)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(118..119,124..127)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206715"
     Site            order(118..123,124..126)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206715"
     Site            120
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206715"
     Site            143..146
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206715"
     Site            order(145..146,154..157,160..163)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206715"
     Site            202..205
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206715"
     Site            232..234
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206715"
     Region          277..296
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O88667.1)"
     Site            301..304
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:206715"
     CDS             1..307
                     /gene="Rrad"
                     /gene_synonym="Rad; REM3"
                     /coded_by="NM_019662.3:235..1158"
                     /db_xref="CCDS:CCDS22584.1"
                     /db_xref="GeneID:56437"
                     /db_xref="MGI:MGI:1930943"
ORIGIN      
        1 mtlnggsgas gsrgagrerd rrrgstpwgp applhrrsmp vderdlqaal apgslattaa
       61 gtrtqgqrld wpegssdsls sggsgseegv ykvlllgapg vgksalarif ggiedgpeae
      121 aaghtydrsi tvdgeeasll vydiweqdgg cwlpghcmam gdayvivysi tdkgsfekas
      181 elrvqlrrar qtddvpiilv gnksdlvrsr evsvdegrac avvfdckfie tsaalhhnvq
      241 alfegvvrqi rlrrdskedn arrqagtrrr eslgkkakrf lgrivarnsr kmafraksks
      301 chdlsvl
//
LOCUS       NP_659400                838 aa            linear   PRI 27-APR-2025
DEFINITION  protein FAM91A1 isoform 1 [Homo sapiens].
ACCESSION   NP_659400
VERSION     NP_659400.3
DBSOURCE    REFSEQ: accession NM_144963.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Zhao,L., Deng,H., Yang,Q., Tang,Y., Zhao,J., Li,P., Zhang,S.,
            Yong,X., Li,T., Billadeau,D.D. and Jia,D.
  TITLE     FAM91A1-TBC1D23 complex structure reveals human genetic variations
            susceptible for PCH
  JOURNAL   Proc Natl Acad Sci U S A 120 (45), e2309910120 (2023)
   PUBMED   37903274
  REMARK    GeneRIF: FAM91A1-TBC1D23 complex structure reveals human genetic
            variations susceptible for PCH.
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Navarro Negredo,P., Edgar,J.R., Manna,P.T., Antrobus,R. and
            Robinson,M.S.
  TITLE     The WDR11 complex facilitates the tethering of AP-1-derived
            vesicles
  JOURNAL   Nat Commun 9 (1), 596 (2018)
   PUBMED   29426865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Shin,J.J.H., Gillingham,A.K., Begum,F., Chadwick,J. and Munro,S.
  TITLE     TBC1D23 is a bridging factor for endosomal vesicle capture by
            golgins at the trans-Golgi
  JOURNAL   Nat Cell Biol 19 (12), 1424-1432 (2017)
   PUBMED   29084197
  REMARK    Erratum:[Nat Cell Biol. 2018 Feb;20(2):222. doi:
            10.1038/s41556-017-0026-7. PMID: 29311657]
REFERENCE   4  (residues 1 to 838)
  AUTHORS   Han,M.H., Hu,Z., Chen,C.Y., Chen,Y., Gucek,M., Li,Z. and
            Markey,S.P.
  TITLE     Dysbindin-associated proteome in the p2 synaptosome fraction of
            mouse brain
  JOURNAL   J Proteome Res 13 (11), 4567-4580 (2014)
   PUBMED   25198678
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Low,S.K., Kuchiba,A., Zembutsu,H., Saito,A., Takahashi,A., Kubo,M.,
            Daigo,Y., Kamatani,N., Chiku,S., Totsuka,H., Ohnami,S., Hirose,H.,
            Shimada,K., Okusaka,T., Yoshida,T., Nakamura,Y. and Sakamoto,H.
  TITLE     Genome-wide association study of pancreatic cancer in Japanese
            population
  JOURNAL   PLoS One 5 (7), e11824 (2010)
   PUBMED   20686608
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Need,A.C., Attix,D.K., McEvoy,J.M., Cirulli,E.T., Linney,K.L.,
            Hunt,P., Ge,D., Heinzen,E.L., Maia,J.M., Shianna,K.V., Weale,M.E.,
            Cherkas,L.F., Clement,G., Spector,T.D., Gibson,G. and
            Goldstein,D.B.
  TITLE     A genome-wide study of common SNPs and CNVs in cognitive
            performance in the CANTAB
  JOURNAL   Hum Mol Genet 18 (23), 4650-4661 (2009)
   PUBMED   19734545
REFERENCE   7  (residues 1 to 838)
  AUTHORS   Nusbaum,C., Mikkelsen,T.S., Zody,M.C., Asakawa,S., Taudien,S.,
            Garber,M., Kodira,C.D., Schueler,M.G., Shimizu,A., Whittaker,C.A.,
            Chang,J.L., Cuomo,C.A., Dewar,K., FitzGerald,M.G., Yang,X.,
            Allen,N.R., Anderson,S., Asakawa,T., Blechschmidt,K., Bloom,T.,
            Borowsky,M.L., Butler,J., Cook,A., Corum,B., DeArellano,K.,
            DeCaprio,D., Dooley,K.T., Dorris,L. 3rd, Engels,R., Glockner,G.,
            Hafez,N., Hagopian,D.S., Hall,J.L., Ishikawa,S.K., Jaffe,D.B.,
            Kamat,A., Kudoh,J., Lehmann,R., Lokitsang,T., Macdonald,P.,
            Major,J.E., Matthews,C.D., Mauceli,E., Menzel,U., Mihalev,A.H.,
            Minoshima,S., Murayama,Y., Naylor,J.W., Nicol,R., Nguyen,C.,
            O'Leary,S.B., O'Neill,K., Parker,S.C., Polley,A., Raymond,C.K.,
            Reichwald,K., Rodriguez,J., Sasaki,T., Schilhabel,M., Siddiqui,R.,
            Smith,C.L., Sneddon,T.P., Talamas,J.A., Tenzin,P., Topham,K.,
            Venkataraman,V., Wen,G., Yamazaki,S., Young,S.K., Zeng,Q.,
            Zimmer,A.R., Rosenthal,A., Birren,B.W., Platzer,M., Shimizu,N. and
            Lander,E.S.
  TITLE     DNA sequence and analysis of human chromosome 8
  JOURNAL   Nature 439 (7074), 331-335 (2006)
   PUBMED   16421571
REFERENCE   8  (residues 1 to 838)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011134.15.
            
            On Nov 23, 2018 this sequence version replaced NP_659400.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.38700.1,
                                           SRR1660803.259490.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334705.12/ ENSP00000335082.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..838
                     /product="protein FAM91A1 isoform 1"
                     /note="skeletal muscle cells re-entry induced; protein
                     FAM91A1"
                     /calculated_mol_wt=93778
     Region          8..312
                     /region_name="FAM91_N"
                     /note="FAM91 N-terminus; pfam14647"
                     /db_xref="CDD:434094"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q658Y4.3)"
     Region          334..367
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q658Y4.3)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q658Y4.3)"
     Region          374..821
                     /region_name="FAM91_C"
                     /note="FAM91 C-terminus; pfam14648"
                     /db_xref="CDD:464235"
     Region          670..690
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q658Y4.3)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q658Y4.3)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q658Y4.3)"
     CDS             1..838
                     /gene="FAM91A1"
                     /coded_by="NM_144963.4:265..2781"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6346.2"
                     /db_xref="GeneID:157769"
                     /db_xref="HGNC:HGNC:26306"
ORIGIN      
        1 mnidvefhir hnypwnklpa nvrqslgnsq reyekqvvly sirnqlryrn nlvkhvkkde
       61 rryyeellky srdhlmlypy hlsdimvkgl ritpfsyytg imedimnsek sydslpnfta
      121 adclrllgig rnqyidlmnq crsskkffrr ktardllpik pveiaieaww vvqagyited
      181 dikictlpek cavdkiidsg pqlsgsldyn vvhslynkgf iyldvpisdd sciavppleg
      241 fvmnrvqgdy fetllykifv sidehtnvae lanvleidls lvknavsmyc rlgfahkkgq
      301 vinldqlhss wknvpsvnrl kstldpqkml lswdggesrs pvqeassatd tdtnsqedpa
      361 dtasvsslsl stghtkriaf lfdstltafl mmgnlspnlk shavtmfevg klsdesldsf
      421 lielekvqst gegeaqryfd haltlrntil flrhnkdlva qtaqpdqpny gfpldllrce
      481 sllgldpatc srvlnknytl lvsmapltne irpvssctpq higpaipevs svwfklyiyh
      541 vtgqgppsll lskgtrlrkl pdifqsydrl litswghdpg vvptsnvltm lndalthsav
      601 liqghglhgi getvhvpfpf detelqgeft rvnmgvhkal qilrnrvdlq hlcgyvtmln
      661 assqladrkl sdasdergep dlasgsdvng stesfemvie eatidsatkq tsgatteadw
      721 vplelcfgip lfsselnrkv crkiaahglc rkeslqnllh ssrklslqvl nfvhsfqega
      781 sildihteps fssllsqssc admgvplpak nlifkdgvls ewsgrspssl lianlhlq
//
LOCUS       NP_780683                266 aa            linear   ROD 27-APR-2025
DEFINITION  sesquipedalian-1 [Mus musculus].
ACCESSION   NP_780683
VERSION     NP_780683.1
DBSOURCE    REFSEQ: accession NM_175474.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Swan,L.E., Tomasini,L., Pirruccello,M., Lunardi,J. and De
            Camilli,P.
  TITLE     Two closely related endocytic proteins that share a common
            OCRL-binding motif with APPL1
  JOURNAL   Proc Natl Acad Sci U S A 107 (8), 3511-3516 (2010)
   PUBMED   20133602
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY347960.1, AK039192.1 and BE993987.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All three variants encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK033618.1, CK128893.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 62.01 cM"
     Protein         1..266
                     /product="sesquipedalian-1"
                     /note="27 kDa inositol polyphosphate phosphatase
                     interacting protein A; family with sequence similarity
                     109, member A"
                     /calculated_mol_wt=29087
     Region          11..130
                     /region_name="PH_Ses"
                     /note="Sesquipedalian family Pleckstrin homology (PH)
                     domain; cd13288"
                     /db_xref="CDD:270105"
     Region          165..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH49.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N4B1; propagated from
                     UniProtKB/Swiss-Prot (Q8BH49.1)"
     Region          191..203
                     /region_name="F&H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH49.1)"
     CDS             1..266
                     /gene="Pheta1"
                     /gene_synonym="A230106M15Rik; Fam109a; IPIP27A; Ses1"
                     /coded_by="NM_175474.4:344..1144"
                     /db_xref="CCDS:CCDS19642.1"
                     /db_xref="GeneID:231717"
                     /db_xref="MGI:MGI:2442708"
ORIGIN      
        1 mklnerslaf yatcdapvdn agflykrggr gtgshrrwfv lrgnilfyfe aegsreplgv
       61 illegctvel vdareefafa vrfaggrsrp yvlaadsqaa legwvkalsr asfhylrlvv
      121 releqqlaam regspanalp anpspvltqr pkengwvvws tlpeqpsvap qrppplpprr
      181 rasaangpla sfaqlharyg levqalrdqw rggqaglasl evpwhpgsae tqtqdqpalr
      241 ghsgckvlhv frsvewpvcn pgsqgt
//
LOCUS       NP_001347797             649 aa            linear   ROD 27-APR-2025
DEFINITION  actin-binding LIM protein 3 isoform 2 [Mus musculus].
ACCESSION   NP_001347797 XP_017173414
VERSION     NP_001347797.1
DBSOURCE    REFSEQ: accession NM_001360868.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Liu,C.F., Angelozzi,M., Haseeb,A. and Lefebvre,V.
  TITLE     SOX9 is dispensable for the initiation of epigenetic remodeling and
            the activation of marker genes at the onset of chondrogenesis
  JOURNAL   Development 145 (14) (2018)
   PUBMED   30021842
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Gineste,C., De Winter,J.M., Kohl,C., Witt,C.C., Giannesini,B.,
            Brohm,K., Le Fur,Y., Gretz,N., Vilmen,C., Pecchi,E., Jubeau,M.,
            Cozzone,P.J., Stienen,G.J., Granzier,H., Labeit,S.,
            Ottenheijm,C.A., Bendahan,D. and Gondin,J.
  TITLE     In vivo and in vitro investigations of heterozygous nebulin
            knock-out mice disclose a mild skeletal muscle phenotype
  JOURNAL   Neuromuscul Disord 23 (4), 357-369 (2013)
   PUBMED   23375831
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Cao,J., Shen,Y., Zhu,L., Xu,Y., Zhou,Y., Wu,Z., Li,Y., Yan,X. and
            Zhu,X.
  TITLE     miR-129-3p controls cilia assembly by regulating CP110 and actin
            dynamics
  JOURNAL   Nat Cell Biol 14 (7), 697-706 (2012)
   PUBMED   22684256
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 649)
  AUTHORS   Matsuda,M., Yamashita,J.K., Tsukita,S. and Furuse,M.
  TITLE     abLIM3 is a novel component of adherens junctions with
            actin-binding activity
  JOURNAL   Eur J Cell Biol 89 (11), 807-816 (2010)
   PUBMED   20709423
REFERENCE   6  (residues 1 to 649)
  AUTHORS   Barrientos,T., Frank,D., Kuwahara,K., Bezprozvannaya,S.,
            Pipes,G.C., Bassel-Duby,R., Richardson,J.A., Katus,H.A., Olson,E.N.
            and Frey,N.
  TITLE     Two novel members of the ABLIM protein family, ABLIM-2 and -3,
            associate with STARS and directly bind F-actin
  JOURNAL   J Biol Chem 282 (11), 8393-8403 (2007)
   PUBMED   17194709
  REMARK    GeneRIF: ABLIM-2 and -3 associate with STARS and directly bind
            F-actin
REFERENCE   7  (residues 1 to 649)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   8  (residues 1 to 649)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   9  (residues 1 to 649)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091677.12 and AC125157.4.
            
            On Feb 16, 2018 this sequence version replaced XP_017173414.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 34.77 cM"
     Protein         1..649
                     /product="actin-binding LIM protein 3 isoform 2"
                     /note="actin-binding LIM protein 3; abLIM-3"
                     /calculated_mol_wt=73866
     Region          23..74
                     /region_name="LIM1_abLIM"
                     /note="The first LIM domain of actin binding LIM (abLIM)
                     proteins; cd09327"
                     /db_xref="CDD:188713"
     Site            order(23,26,43,46,49,52,70,73)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188713"
     Region          79..134
                     /region_name="LIM2_abLIM"
                     /note="The second LIM domain on actin binding LIM (abLIM)
                     proteins; cd09328"
                     /db_xref="CDD:188714"
     Site            order(82,85,102,105,108,111,130,133)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188714"
     Region          151..202
                     /region_name="LIM3_abLIM"
                     /note="The third LIM domain of actin binding LIM (abLIM)
                     proteins; cd09329"
                     /db_xref="CDD:188715"
     Site            order(151,154,172,175,178,181,198,201)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188715"
     Region          210..265
                     /region_name="LIM4_abLIM"
                     /note="The fourth LIM domain of actin binding LIM (abLIM)
                     proteins; cd09330"
                     /db_xref="CDD:188716"
     Site            order(210,213,230,233,236,239,258,261)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188716"
     Region          273..599
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          614..649
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..649
                     /gene="Ablim3"
                     /gene_synonym="D930036B08Rik"
                     /coded_by="NM_001360868.1:265..2214"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:319713"
                     /db_xref="MGI:MGI:2442582"
ORIGIN      
        1 mntsipyqqs pysprggsnv iqcyrcgdtc kgevvrvhnn hfhircftcq vcgcglaqsg
       61 fffknqeyic tqdyqqlygt rcdscrdfit gevisalgrt yhpkcfvcsl crkpfpigdk
      121 vtfsgkecvc qtcsqsmtss kpikirgpsh cagckeeikh gqsllaldkq whvscfkcqt
      181 csviltgeyi skdgvpyces dyhsqfgikc etcdryisgr vleaggkhyh ptcarcvrch
      241 qmftegeemy ltgsevwhpi ckqaaraekk lkhrrtsets isppgssigs pnrvicakvd
      301 neilnykdla alpkvksiye vqrpdlisye phsrytsdem lercgygesl gtlspysqdi
      361 yenldlrqrr asspgyidsp tysrqgmspt fsrsphyyrs agesniyrkp piykrhgdls
      421 tatksktsed isqaskyspa yspdpyyase seywtyhgsp kvprarrfss ggeeedfdrs
      481 mhklqsgigr lilkeemkar sssyadpwtp prsstssrea lhttgyemsf ngsprshyla
      541 dsdplisksa slpayrrngl hrtpsadlfh ydsmnavnwg mreykiypye lllvttrgrn
      601 rlpkdvdrtr lerhlsqeef yqvfgmtise ferlalwkrn elkkqarlf
//
LOCUS       NP_112190                546 aa            linear   PRI 27-APR-2025
DEFINITION  DNA replication factor Cdt1 [Homo sapiens].
ACCESSION   NP_112190
VERSION     NP_112190.2
DBSOURCE    REFSEQ: accession NM_030928.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Mi,Y., Li,X., Wang,C., Lin,C., Zhao,Z., Yan,X., Shi,P. and Wang,L.
  TITLE     [miR-2110 Affects the Biological Behaviors of Lung Adenocarcinoma
            by Regulating CDT1]
  JOURNAL   Sichuan Da Xue Xue Bao Yi Xue Ban 55 (5), 1202-1209 (2024)
   PUBMED   39507968
  REMARK    GeneRIF: [miR-2110 Affects the Biological Behaviors of Lung
            Adenocarcinoma by Regulating CDT1].
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Moriyama,M., Kanda,T., Midorikawa,Y., Matsumura,H., Masuzaki,R.,
            Nakamura,H., Ogawa,M., Matsuoka,S., Shibata,T., Yamazaki,M.,
            Kuroda,K., Nakayama,H., Higaki,T., Kanemaru,K., Miki,T.,
            Sugitani,M. and Takayama,T.
  TITLE     The proliferation of atypical hepatocytes and CDT1 expression in
            noncancerous tissue are associated with the postoperative
            recurrence of hepatocellular carcinoma
  JOURNAL   Sci Rep 12 (1), 20508 (2022)
   PUBMED   36443564
  REMARK    GeneRIF: The proliferation of atypical hepatocytes and CDT1
            expression in noncancerous tissue are associated with the
            postoperative recurrence of hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Fu,Q., Wang,F., Yang,J., Sun,W., Hu,Z., Xu,L., Chu,H., Wang,X. and
            Zhang,W.
  TITLE     Long non-coding RNA-PCGEM1 contributes to prostate cancer
            progression by sponging microRNA miR-129-5p to enhance chromatin
            licensing and DNA replication factor 1 expression
  JOURNAL   Bioengineered 13 (4), 9411-9424 (2022)
   PUBMED   35412947
  REMARK    GeneRIF: Long non-coding RNA-PCGEM1 contributes to prostate cancer
            progression by sponging microRNA miR-129-5p to enhance chromatin
            licensing and DNA replication factor 1 expression.
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Shi,H.X., Huang,S.W., Luo,W.J., Pan,F., Jin,H.J. and Wei,W.
  TITLE     Elevated expression of CDT1 in childhood acute lymphoblastic
            leukemia promotes cell proliferation, invasion and migration
            through activation of EMT
  JOURNAL   J Biol Regul Homeost Agents 35 (Special Issue on Internal Medicine
            n.1) (2021)
   PUBMED   34348833
  REMARK    GeneRIF: Elevated expression of CDT1 in childhood acute
            lymphoblastic leukemia promotes cell proliferation, invasion and
            migration through activation of EMT.
REFERENCE   5  (residues 1 to 546)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 546)
  AUTHORS   Wohlschlegel,J.A., Dwyer,B.T., Dhar,S.K., Cvetic,C., Walter,J.C.
            and Dutta,A.
  TITLE     Inhibition of eukaryotic DNA replication by geminin binding to Cdt1
  JOURNAL   Science 290 (5500), 2309-2312 (2000)
   PUBMED   11125146
REFERENCE   7  (residues 1 to 546)
  AUTHORS   Izumi,M., Yanagi,K., Mizuno,T., Yokoi,M., Kawasaki,Y., Moon,K.Y.,
            Hurwitz,J., Yatagai,F. and Hanaoka,F.
  TITLE     The human homolog of Saccharomyces cerevisiae Mcm10 interacts with
            replication factors and dissociates from nuclease-resistant nuclear
            structures in G(2) phase
  JOURNAL   Nucleic Acids Res 28 (23), 4769-4777 (2000)
   PUBMED   11095689
REFERENCE   8  (residues 1 to 546)
  AUTHORS   Whittaker,A.J., Royzman,I. and Orr-Weaver,T.L.
  TITLE     Drosophila double parked: a conserved, essential replication
            protein that colocalizes with the origin recognition complex and
            links DNA replication with mitosis and the down-regulation of S
            phase transcripts
  JOURNAL   Genes Dev 14 (14), 1765-1776 (2000)
   PUBMED   10898791
REFERENCE   9  (residues 1 to 546)
  AUTHORS   Nishitani,H., Lygerou,Z., Nishimoto,T. and Nurse,P.
  TITLE     The Cdt1 protein is required to license DNA for replication in
            fission yeast
  JOURNAL   Nature 404 (6778), 625-628 (2000)
   PUBMED   10766248
REFERENCE   10 (residues 1 to 546)
  AUTHORS   Herbig,U., Marlar,C.A. and Fanning,E.
  TITLE     The Cdc6 nucleotide-binding site regulates its activity in DNA
            replication in human cells
  JOURNAL   Mol Biol Cell 10 (8), 2631-2645 (1999)
   PUBMED   10436018
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB053172.1, AC092384.5 and
            BC000137.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 16, 2008 this sequence version replaced NP_112190.1.
            
            Summary: The protein encoded by this gene is involved in the
            formation of the pre-replication complex that is necessary for DNA
            replication. The encoded protein can bind geminin, which prevents
            replication and may function to prevent this protein from
            initiating replication at inappropriate origins. Phosphorylation of
            this protein by cyclin A-dependent kinases results in degradation
            of the protein. [provided by RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB053172.1, SRR1163655.442740.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301019.9/ ENSP00000301019.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..546
                     /product="DNA replication factor Cdt1"
                     /note="Double parked, Drosophila, homolog of"
                     /calculated_mol_wt=60259
     Region          1..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H211.3)"
     Region          1..23
                     /region_name="PIP-box K+4 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H211.3)"
     Region          <18..>169
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK8.
                     /evidence=ECO:0000269|PubMed:21856198; propagated from
                     UniProtKB/Swiss-Prot (Q9H211.3)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H211.3)"
     Region          68..70
                     /region_name="Cyclin-binding motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H211.3)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8.
                     /evidence=ECO:0000269|PubMed:21856198; propagated from
                     UniProtKB/Swiss-Prot (Q9H211.3)"
     Region          143..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H211.3)"
     Region          150..190
                     /region_name="Interaction with GMNN"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H211.3)"
     Region          168..352
                     /region_name="Cdt1_m"
                     /note="The middle winged helix fold of replication
                     licensing factor Cdt1 binds geminin to inhibit binding of
                     the MCM complex to origins of replication and DNA;
                     cd08674"
                     /db_xref="CDD:176571"
     Site            order(168..170,172..173,176..179,182,198,228,287..289,292,
                     295,314,323,327..334)
                     /site_type="active"
                     /note="Cdt1-Geminin inhibitory interaction site [active]"
                     /db_xref="CDD:176571"
     Site            order(169..170,172..173,176..179,181,323,327..334,336)
                     /site_type="active"
                     /note="Cdt1-Geminin permissive interaction site [active]"
                     /db_xref="CDD:176571"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8.
                     /evidence=ECO:0000269|PubMed:21856198,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H211.3)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H211.3)"
     Region          383..415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H211.3)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H211.3)"
     Region          415..537
                     /region_name="Cdt1_c"
                     /note="The C-terminal fold of replication licensing factor
                     Cdt1 is essential for Cdt1 activity and directly interacts
                     with MCM2-7 helicase; cd08767"
                     /db_xref="CDD:176572"
     Site            order(429,433,469..470,474,496,500,504,511,513,516,534,
                     537)
                     /site_type="active"
                     /note="putative Cdt1-MCM complex binding site [active]"
                     /db_xref="CDD:176572"
     Region          451..546
                     /region_name="Interaction with LRWD1.
                     /evidence=ECO:0000269|PubMed:22645314"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H211.3)"
     CDS             1..546
                     /gene="CDT1"
                     /gene_synonym="DUP; RIS2"
                     /coded_by="NM_030928.4:44..1684"
                     /db_xref="CCDS:CCDS32510.1"
                     /db_xref="GeneID:81620"
                     /db_xref="HGNC:HGNC:24576"
                     /db_xref="MIM:605525"
ORIGIN      
        1 meqrrvtdff arrrpgppri appklacrtp sparpalrap asatsgsrkr arppaapgrd
       61 qarpparrrl rlsvdevssp stpeapdipa cpspgqkikk stpaagqpph ltsaqdqdti
      121 selasclqra relgarvral kasaqdages ctpeaegrpe epcgekapay qrfhalaqpg
      181 lpglvlpyky qvlaemfrsm dtivgmlhnr setptfakvq rgvqdmmrrr feecnvgqik
      241 tvypasyrfr qersvptfkd gtrrsdyqlt ieplleqead gaapqltasr llqrrqifsq
      301 klvehvkehh kaflaslspa mvvpedqltr whprfnvdev pdiepaalpq ppatekltta
      361 qevlararnl isprmekals qlalrsaaps spgsprpalp atppatppaa spsalkgvsq
      421 dllerirake aqkqlaqmtr cpeqeqrlqr lerlpelarv lrsvfvserk palsmevaca
      481 rmvgscctim spgemekhll llsellpdwl slhrirtdty vkldkaadla hitarlahqt
      541 raeegl
//
LOCUS       NP_001269154             511 aa            linear   PRI 27-APR-2025
DEFINITION  adenosine deaminase 2 isoform a precursor [Homo sapiens].
ACCESSION   NP_001269154 XP_005261302
VERSION     NP_001269154.1
DBSOURCE    REFSEQ: accession NM_001282225.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Dong,L., Luo,W., Maksym,S., Robson,S.C. and Zavialov,A.V.
  TITLE     Adenosine deaminase 2 regulates the activation of the toll-like
            receptor 9 in response to nucleic acids
  JOURNAL   Front Med 18 (5), 814-830 (2024)
   PUBMED   39078537
  REMARK    GeneRIF: Adenosine deaminase 2 regulates the activation of the
            toll-like receptor 9 in response to nucleic acids.
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Verschoof,M.A., van Meenen,L.C.C., Andriessen,M.V.E.,
            Brinkman,D.M.C., Kamphuis,S., Kuijpers,T.W., Leavis,H.L.,
            Legger,G.E., Mulders-Manders,C.M., de Pagter,A.P.J., Rutgers,A.,
            van Well,G.T.J., Coutinho,J.M., Hak,A.E., van Montfrans,J.M. and
            Klouwer,F.C.C.
  TITLE     Neurological phenotype of adenosine deaminase 2 deficient patients:
            a cohort study
  JOURNAL   Eur J Neurol 31 (1), e16043 (2024)
   PUBMED   37584090
  REMARK    GeneRIF: Neurological phenotype of adenosine deaminase 2 deficient
            patients: a cohort study.
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Jedrzejewska,A., Kawecka,A., Braczko,A., Romanowska-Kocejko,M.,
            Stawarska,K., Deptula,M., Zawrzykraj,M., Franczak,M., Krol,O.,
            Harasim,G., Walczak,I., Pikula,M., Hellmann,M. and Kutryb-Zajac,B.
  TITLE     Changes in Adenosine Deaminase Activity and Endothelial Dysfunction
            after Mild Coronavirus Disease-2019
  JOURNAL   Int J Mol Sci 24 (17), 13140 (2023)
   PUBMED   37685949
  REMARK    GeneRIF: Changes in Adenosine Deaminase Activity and Endothelial
            Dysfunction after Mild Coronavirus Disease-2019.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Asna Ashari,K., Aslani,N., Parvaneh,N., Assari,R., Heidari,M.,
            Fathi,M., Tahghighi Sharabian,F., Ronagh,A., Shahrooei,M.,
            Moafi,A., Rezaei,N. and Ziaee,V.
  TITLE     A case series of ten plus one deficiency of adenosine deaminase 2
            (DADA2) patients in Iran
  JOURNAL   Pediatr Rheumatol Online J 21 (1), 55 (2023)
   PUBMED   37312195
  REMARK    GeneRIF: A case series of ten plus one deficiency of adenosine
            deaminase 2 (DADA2) patients in Iran.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Sharma,V., Deo,P. and Sharma,A.
  TITLE     Deficiency of adenosine deaminase 2 (DADA2): Review
  JOURNAL   Best Pract Res Clin Rheumatol 37 (1), 101844 (2023)
   PUBMED   37328410
  REMARK    GeneRIF: Deficiency of adenosine deaminase 2 (DADA2): Review.
            Review article
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Zavialov,A.V. and Engstrom,A.
  TITLE     Human ADA2 belongs to a new family of growth factors with adenosine
            deaminase activity
  JOURNAL   Biochem J 391 (Pt 1), 51-57 (2005)
   PUBMED   15926889
  REMARK    GeneRIF: findings show ADA2 is encoded by the CECR1 gene & belongs
            to novel family of ADA-related growth factors;ADA2 may be active in
            sites of inflammation during hypoxia & in areas of tumour growth
            where adenosine is elevated & extracellular pH is acidic
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Footz,T.K., Brinkman-Mills,P., Banting,G.S., Maier,S.A.,
            Riazi,M.A., Bridgland,L., Hu,S., Birren,B., Minoshima,S.,
            Shimizu,N., Pan,H., Nguyen,T., Fang,F., Fu,Y., Ray,L., Wu,H.,
            Shaull,S., Phan,S., Yao,Z., Chen,F., Huan,A., Hu,P., Wang,Q.,
            Loh,P., Qi,S., Roe,B.A. and McDermid,H.E.
  TITLE     Analysis of the cat eye syndrome critical region in humans and the
            region of conserved synteny in mice: a search for candidate genes
            at or near the human chromosome 22 pericentromere
  JOURNAL   Genome Res 11 (6), 1053-1070 (2001)
   PUBMED   11381032
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Charlab,R., Valenzuela,J.G., Andersen,J. and Ribeiro,J.M.
  TITLE     The invertebrate growth factor/CECR1 subfamily of adenosine
            deaminase proteins
  JOURNAL   Gene 267 (1), 13-22 (2001)
   PUBMED   11311551
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Riazi,M.A., Brinkman-Mills,P., Nguyen,T., Pan,H., Phan,S., Ying,F.,
            Roe,B.A., Tochigi,J., Shimizu,Y., Minoshima,S., Shimizu,N.,
            Buchwald,M. and McDermid,H.E.
  TITLE     The human homolog of insect-derived growth factor, CECR1, is a
            candidate gene for features of cat eye syndrome
  JOURNAL   Genomics 64 (3), 277-285 (2000)
   PUBMED   10756095
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Aksentijevich,I., Sampaio Moura,N. and Barron,K.
  TITLE     Adenosine Deaminase 2 Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31393689
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC391616.1, CR456417.1,
            AK074702.1, CD369524.1 and AI523928.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 24, 2013 this sequence version replaced XP_005261302.1.
            
            Summary: This gene encodes a member of a subfamily of the adenosine
            deaminase protein family. The encoded protein is one of two
            adenosine deaminases found in humans, which regulate levels of the
            signaling molecule, adenosine. The encoded protein is secreted from
            monocytes undergoing differentiation and may regulate cell
            proliferation and differentiation. This gene may be responsible for
            some of the phenotypic features associated with cat eye syndrome.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (a). Both variants 3 and
            4 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.6826.1,
                                           SRR1803611.71334.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399837.8/ ENSP00000382731.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.1"
     Protein         1..511
                     /product="adenosine deaminase 2 isoform a precursor"
                     /EC_number="3.5.4.4"
                     /note="adenosine deaminase CECR1; cat eye syndrome
                     critical region protein 1; cat eye syndrome chromosome
                     region, candidate 1"
                     /calculated_mol_wt=55908
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3044
     mat_peptide     30..511
                     /product="Adenosine deaminase 2. /id=PRO_0000006725"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZK5.2)"
                     /calculated_mol_wt=55908
     Region          30..509
                     /region_name="adm_rel"
                     /note="adenosine deaminase-related growth factor;
                     TIGR01431"
                     /db_xref="CDD:273620"
     Region          30..100
                     /region_name="Dimerization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZK5.2)"
     Region          127..185
                     /region_name="PRB domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZK5.2)"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20147294; propagated from
                     UniProtKB/Swiss-Prot (Q9NZK5.2)"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9NZK5.2)"
     Site            185
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20147294; propagated from
                     UniProtKB/Swiss-Prot (Q9NZK5.2)"
     Site            378
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:20147294; propagated from
                     UniProtKB/Swiss-Prot (Q9NZK5.2)"
     CDS             1..511
                     /gene="ADA2"
                     /gene_synonym="ADGF; CECR1; IDGFL; PAN; SNEDS; VAIHS"
                     /coded_by="NM_001282225.2:127..1662"
                     /note="isoform a precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS13742.1"
                     /db_xref="GeneID:51816"
                     /db_xref="HGNC:HGNC:1839"
                     /db_xref="MIM:607575"
ORIGIN      
        1 mlvdgpserp alcflllava msffgsalsi detrahlllk ekmmrlggrl vlntkeelan
       61 erlmtlkiae mkeamrtlif ppsmhffqak hliersqvfn ilrmmpkgaa lhlhdigivt
      121 mdwlvrnvty rphchicftp rgimqfrfah ptprpsekcs kwilledyrk rvqnvtefdd
      181 sllrnftlvt qhpeviytnq nvvwskfeti fftisglihy apvfrdyvfr smqefyednv
      241 lymeirarll pvyelsgehh deewsvktyq evaqkfveth pefigikiiy sdhrskdvav
      301 iaesirmamg lrikfptvva gfdlvghedt ghslhdykea lmipakdgvk lpyffhaget
      361 dwqgtsidrn ildalmlntt righgfalsk hpavrtyswk kdipievcpi snqvlklvsd
      421 lrnhpvatlm atghpmviss ddpamfgakg lsydfyevfm giggmkadlr tlkqlamnsi
      481 kystllesek ntfmeiwkkr wdkfiadvat k
//
LOCUS       NP_001352172             566 aa            linear   PRI 27-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 6
            [Homo sapiens].
ACCESSION   NP_001352172
VERSION     NP_001352172.1
DBSOURCE    REFSEQ: accession NM_001365243.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Zhang,S., Huang,J., Lan,Z., Xiao,Y., Liao,Y., Basnet,S., Huang,P.,
            Li,Y., Yan,J., Sheng,Y., Zhou,W., Liu,Q., Tan,H., Tan,Y., Yuan,L.,
            Wang,L., Dai,L., Zhang,W. and Du,C.
  TITLE     CPEB1 Controls NRF2 Proteostasis and Ferroptosis Susceptibility in
            Pancreatic Cancer
  JOURNAL   Int J Biol Sci 20 (8), 3156-3172 (2024)
   PUBMED   38904009
  REMARK    GeneRIF: CPEB1 Controls NRF2 Proteostasis and Ferroptosis
            Susceptibility in Pancreatic Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Pico,S., Parras,A., Santos-Galindo,M., Pose-Utrilla,J., Castro,M.,
            Fraga,E., Hernandez,I.H., Elorza,A., Anta,H., Wang,N.,
            Marti-Sanchez,L., Belloc,E., Garcia-Esparcia,P., Garrido,J.J.,
            Ferrer,I., Macias-Garcia,D., Mir,P., Artuch,R., Perez,B.,
            Hernandez,F., Navarro,P., Lopez-Sendon,J.L., Iglesias,T.,
            Yang,X.W., Mendez,R. and Lucas,J.J.
  TITLE     CPEB alteration and aberrant transcriptome-polyadenylation lead to
            a treatable SLC19A3 deficiency in Huntington's disease
  JOURNAL   Sci Transl Med 13 (613), eabe7104 (2021)
   PUBMED   34586830
  REMARK    GeneRIF: CPEB alteration and aberrant transcriptome-polyadenylation
            lead to a treatable SLC19A3 deficiency in Huntington's disease.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Shao,K., Pu,W., Zhang,J., Guo,S., Qian,F., Glurich,I., Jin,Q.,
            Ma,Y., Ju,S., Zhang,Z. and Ding,W.
  TITLE     DNA hypermethylation contributes to colorectal cancer metastasis by
            regulating the binding of CEBPB and TFCP2 to the CPEB1 promoter
  JOURNAL   Clin Epigenetics 13 (1), 89 (2021)
   PUBMED   33892791
  REMARK    GeneRIF: DNA hypermethylation contributes to colorectal cancer
            metastasis by regulating the binding of CEBPB and TFCP2 to the
            CPEB1 promoter.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Sovijit,W., Sovijit,W., Ishii,Y., Kambe,J., Fujita,T., Watanabe,G.,
            Yamaguchi,H. and Nagaoka,K.
  TITLE     Estrogen promotes increased breast cancer cell proliferation and
            migration through downregulation of CPEB1 expression
  JOURNAL   Biochem Biophys Res Commun 534, 871-876 (2021)
   PUBMED   33162033
  REMARK    GeneRIF: Estrogen promotes increased breast cancer cell
            proliferation and migration through downregulation of CPEB1
            expression.
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Jiao,W., Zhao,S., Liu,R., Guo,T. and Qin,Y.
  TITLE     CPEB1 deletion is not a common explanation for premature ovarian
            insufficiency in a Chinese cohort
  JOURNAL   J Ovarian Res 13 (1), 49 (2020)
   PUBMED   32354341
  REMARK    GeneRIF: CPEB1 deletion is not a common explanation for premature
            ovarian insufficiency in a Chinese cohort.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Hagele,S., Kuhn,U., Boning,M. and Katschinski,D.M.
  TITLE     Cytoplasmic polyadenylation-element-binding protein (CPEB)1 and 2
            bind to the HIF-1alpha mRNA 3'-UTR and modulate HIF-1alpha protein
            expression
  JOURNAL   Biochem J 417 (1), 235-246 (2009)
   PUBMED   18752464
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Sasayama,T., Marumoto,T., Kunitoku,N., Zhang,D., Tamaki,N.,
            Kohmura,E., Saya,H. and Hirota,T.
  TITLE     Over-expression of Aurora-A targets cytoplasmic polyadenylation
            element binding protein and promotes mRNA polyadenylation of Cdk1
            and cyclin B1
  JOURNAL   Genes Cells 10 (7), 627-638 (2005)
   PUBMED   15966895
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Wilczynska,A., Aigueperse,C., Kress,M., Dautry,F. and Weil,D.
  TITLE     The translational regulator CPEB1 provides a link between dcp1
            bodies and stress granules
  JOURNAL   J Cell Sci 118 (Pt 5), 981-992 (2005)
   PUBMED   15731006
  REMARK    GeneRIF: CPEB1 has a role in compartmentalization of mRNA
            metabolism in the cytoplasm, between dcp1 bodies and stress
            granules
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Mendez,R. and Richter,J.D.
  TITLE     Translational control by CPEB: a means to the end
  JOURNAL   Nat Rev Mol Cell Biol 2 (7), 521-529 (2001)
   PUBMED   11433366
  REMARK    Review article
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Welk,J.F., Charlesworth,A., Smith,G.D. and MacNicol,A.M.
  TITLE     Identification and characterization of the gene encoding human
            cytoplasmic polyadenylation element binding protein
  JOURNAL   Gene 263 (1-2), 113-120 (2001)
   PUBMED   11223249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105339.9, AC110291.7 and
            AC245033.2.
            
            Summary: This gene encodes a member of the cytoplasmic
            polyadenylation element binding protein family. This highly
            conserved protein binds to a specific RNA sequence, called the
            cytoplasmic polyadenylation element, found in the 3' untranslated
            region of some mRNAs. The encoded protein functions in both the
            cytoplasm and the nucleus. It is involved in the regulation of mRNA
            translation, as well as processing of the 3' untranslated region,
            and may play a role in cell proliferation and tumorigenesis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.155568.1,
                                           SRR1803614.179236.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..566
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 6"
                     /note="CPE-binding protein 1"
                     /calculated_mol_wt=62508
     Region          1..307
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9BZB8.1)"
     Region          162..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZB8.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKA and CAMK2A.
                     /evidence=ECO:0000250|UniProtKB:P70166; propagated from
                     UniProtKB/Swiss-Prot (Q9BZB8.1)"
     Region          309..416
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          330..566
                     /region_name="Necessary for stress granule assembly and
                     correct localization in dcp1 bodies"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZB8.1)"
     Site            411
                     /site_type="other"
                     /note="Important for the positionning of RRM1 relative to
                     RRM2. /evidence=ECO:0000269|PubMed:24990967; propagated
                     from UniProtKB/Swiss-Prot (Q9BZB8.1)"
     Region          427..510
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          504..559
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..566
                     /gene="CPEB1"
                     /gene_synonym="CPE-BP1; CPEB; CPEB-1; h-CPEB; hCPEB-1"
                     /coded_by="NM_001365243.1:181..1881"
                     /note="isoform 6 is encoded by transcript variant 10"
                     /db_xref="GeneID:64506"
                     /db_xref="HGNC:HGNC:21744"
                     /db_xref="MIM:607342"
ORIGIN      
        1 mafpleeeag rikdcwdnqe apalstcsna nifrrinail dnsldfsrvc ttpinrgihd
       61 hlpdfqdsee tvtsrmlfpt saqessrglp dandlclglq slsltgwdrp wstqdsdssa
      121 qssthsvlsm lhnplgnvlg kpplsflpld plgsdlvdkf papsvrgsrl dtrpildsrs
      181 sspsdsdtsg fssgsdhlsd lisslrispp lpflslsggg prdplkmgvg srmdqeqaal
      241 aavtpsptsa skrwpgasvw pswdlleapk dpfsierear lhrqaaavne atctwsgqlp
      301 prnyknpiys ckvflggvpw diteaglvnt frvfgslsve wpgkdgkhpr cppkgnmpkg
      361 yvylvfelek svrsllqacs hdplspdgls eyyfkmssrr mrckevqvip wvladsnfvr
      421 spsqrldpsr tvfvgalhgm lnaealaail ndlfggvvya gidtdkhkyp igsgrvtfnn
      481 qrsylkavsa afveikttkf tkkvqidpyl edslchicss qpgpffcrdq vcfkyfcrsc
      541 whwrhsmegl rhhsplmrnq knrdss
//
LOCUS       NP_061910                245 aa            linear   PRI 27-APR-2025
DEFINITION  exosome complex component RRP41 [Homo sapiens].
ACCESSION   NP_061910
VERSION     NP_061910.1
DBSOURCE    REFSEQ: accession NM_019037.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wang,N., Miao,X., Lu,W., Ji,Y., Zheng,Y., Meng,D., Liu,H. and
            Xiang,C.
  TITLE     RUNX3 exerts tumor-suppressive role through inhibiting EXOSC4
            expression
  JOURNAL   Funct Integr Genomics 24 (3), 103 (2024)
   PUBMED   38913281
  REMARK    GeneRIF: RUNX3 exerts tumor-suppressive role through inhibiting
            EXOSC4 expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Taniue,K., Tanu,T., Shimoura,Y., Mitsutomi,S., Han,H., Kakisaka,R.,
            Ono,Y., Tamamura,N., Takahashi,K., Wada,Y., Mizukami,Y. and
            Akimitsu,N.
  TITLE     RNA Exosome Component EXOSC4 Amplified in Multiple Cancer Types Is
            Required for the Cancer Cell Survival
  JOURNAL   Int J Mol Sci 23 (1), 496 (2022)
   PUBMED   35008922
  REMARK    GeneRIF: RNA Exosome Component EXOSC4 Amplified in Multiple Cancer
            Types Is Required for the Cancer Cell Survival.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Pan,Y., Tong,J.H.M., Kang,W., Lung,R.W.M., Chak,W.P., Chung,L.Y.,
            Wu,F., Li,H., Yu,J., Chan,A.W.H. and To,K.F.
  TITLE     EXOSC4 functions as a potential oncogene in development and
            progression of colorectal cancer
  JOURNAL   Mol Carcinog 57 (12), 1780-1791 (2018)
   PUBMED   30155936
  REMARK    GeneRIF: Findings show that EXOSC4 is highly expressed in
            colorectal cancer (CRC) tumors and cell lines and demonstrate its
            oncogenic role in development and progression of CRC.
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Raijmakers,R., Noordman,Y.E., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Protein-protein interactions of hCsl4p with other human exosome
            subunits
  JOURNAL   J Mol Biol 315 (4), 809-818 (2002)
   PUBMED   11812149
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Allmang,C., Petfalski,E., Podtelejnikov,A., Mann,M., Tollervey,D.
            and Mitchell,P.
  TITLE     The yeast exosome and human PM-Scl are related complexes of 3' -->
            5' exonucleases
  JOURNAL   Genes Dev 13 (16), 2148-2158 (1999)
   PUBMED   10465791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM839994.1, BC002777.2 and AK000598.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.324876.1,
                                           SRR1660803.24566.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316052.6/ ENSP00000315476.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..245
                     /product="exosome complex component RRP41"
                     /note="exosome complex exonuclease RRP41; exosome
                     component Rrp41; ribosomal RNA-processing protein 41"
                     /calculated_mol_wt=26252
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NPD3.3)"
     Region          11..237
                     /region_name="RNase_PH_RRP41"
                     /note="RRP41 subunit of eukaryotic exosome; cd11370"
                     /db_xref="CDD:206775"
     Site            order(34,36,51,53..55,73,75,80,98,101,105,119,124,129,
                     147..149,156,196..207,210,214)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:206775"
     Site            order(36,54..57,59,112,116,119,147..150,152..154,156,229,
                     232..233,236..237)
                     /site_type="other"
                     /note="Rrp4 interface [polypeptide binding]"
                     /db_xref="CDD:206775"
     CDS             1..245
                     /gene="EXOSC4"
                     /gene_synonym="hRrp41p; p12A; RRP41; RRP41A; Rrp41p; SKI6;
                     Ski6p"
                     /coded_by="NM_019037.3:58..795"
                     /db_xref="CCDS:CCDS6414.1"
                     /db_xref="GeneID:54512"
                     /db_xref="HGNC:HGNC:18189"
                     /db_xref="MIM:606491"
ORIGIN      
        1 maglellsdq gyrvdgrrag elrkiqarmg vfaqadgsay ieqgntkala vvygpheirg
       61 sraralpdra lvncqyssat fstgerkrrp hgdrkscemg lqlrqtfeaa iltqlhprsq
      121 idiyvqvlqa dggtyaacvn aatlavldag ipmrdfvcac sagfvdgtal adlshveeaa
      181 ggpqlalall pasgqialle mdarlhedhl ervleaaaqa ardvhtlldr vvrqhvreas
      241 illgd
//
LOCUS       NP_082927                741 aa            linear   ROD 27-APR-2025
DEFINITION  protein O-mannosyl-transferase TMTC4 [Mus musculus].
ACCESSION   NP_082927 XP_127899
VERSION     NP_082927.1
DBSOURCE    REFSEQ: accession NM_028651.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Li,J., Choi,B.Y., Eltawil,Y., Ismail Mohamad,N., Park,Y.,
            Matthews,I.R., Han,J.H., Kim,B.J., Sherr,E.H. and Chan,D.K.
  TITLE     TMTC4 is a hair cell-specific human deafness gene
  JOURNAL   JCI Insight 8 (24), e172665 (2023)
   PUBMED   37943620
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Li,J., Akil,O., Rouse,S.L., McLaughlin,C.W., Matthews,I.R.,
            Lustig,L.R., Chan,D.K. and Sherr,E.H.
  TITLE     Deletion of Tmtc4 activates the unfolded protein response and
            causes postnatal hearing loss
  JOURNAL   J Clin Invest 128 (11), 5150-5162 (2018)
   PUBMED   30188326
  REMARK    GeneRIF: mice with homozygous inactivation of both Tmtc4 and Chop
            had less hearing loss than knockout of Tmtc4 alone. This study
            implicated a novel mechanism for hearing impairment, highlighting a
            potential treatment approach for a broad range of human hearing
            loss disorders.
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   5  (residues 1 to 741)
  AUTHORS   Coulpier,F., Le Crom,S., Maro,G.S., Manent,J., Giovannini,M.,
            Maciorowski,Z., Fischer,A., Gessler,M., Charnay,P. and Topilko,P.
  TITLE     Novel features of boundary cap cells revealed by the analysis of
            newly identified molecular markers
  JOURNAL   Glia 57 (13), 1450-1457 (2009)
   PUBMED   19243017
REFERENCE   6  (residues 1 to 741)
  AUTHORS   Pang,A.L., Taylor,H.C., Johnson,W., Alexander,S., Chen,Y., Su,Y.A.,
            Li,X., Ravindranath,N., Dym,M., Rennert,O.M. and Chan,W.Y.
  TITLE     Identification of differentially expressed genes in mouse
            spermatogenesis
  JOURNAL   J Androl 24 (6), 899-911 (2003)
   PUBMED   14581517
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY125796.1, AK033947.1 and BX512100.1.
            
            On Jan 24, 2005 this sequence version replaced XP_127899.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK033947.1, AK045271.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 66.04 cM"
     Protein         1..741
                     /product="protein O-mannosyl-transferase TMTC4"
                     /EC_number="2.4.1.109"
                     /note="transmembrane and TPR repeat-containing protein 4;
                     transmembrane O-mannosyltransferase targeting cadherins 4"
                     /calculated_mol_wt=82832
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            111..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            147..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            167..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            199..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            266..286
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          292..366
                     /region_name="TMTC_DUF1736"
                     /note="Protein O-mannosyl-transferase TMTC, DUF1736;
                     pfam08409"
                     /db_xref="CDD:462468"
     Site            355..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            413..433
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Site            442..462
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          475..681
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          482..515
                     /region_name="TPR 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          482..510
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(483,486..487,490..491,493,517,520..521,524..525,
                     527..528,551,554..555,558..559,562)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          515..545
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          516..549
                     /region_name="TPR 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          550..583
                     /region_name="TPR 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          550..578
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          584..617
                     /region_name="TPR 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          584..610
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            609
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          618..651
                     /region_name="TPR 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          618..646
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          645..>738
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          651..681
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          652..685
                     /region_name="TPR 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          686..719
                     /region_name="TPR 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG19.1)"
     Region          686..714
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            725
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8BG19.1)"
     CDS             1..741
                     /gene="Tmtc4"
                     /gene_synonym="4930403J22Rik; 5730419O14Rik"
                     /coded_by="NM_028651.3:167..2392"
                     /db_xref="CCDS:CCDS27352.1"
                     /db_xref="GeneID:70551"
                     /db_xref="MGI:MGI:1921050"
ORIGIN      
        1 mveldadldh ivpsvlppfw aklvvgfvsl lcfarsydgd fvfddseaiv nnkdlqsdtp
       61 lgdlwhhdfw gsklssntsh ksyrpltvlt frinyylsgg fhpvgfhvvn illhgsisil
      121 mldvfsvlfg glqytgkgqr vhlaprasll atllfavhpv htecvagvvg radllcalff
      181 llsflgycqa fketgnkegt hsstfwvlls iflgavamlc keqgitvlgl navfdilvig
      241 kldilaavrk vlhkdksqen agmfknggll frialltigg tsmlyirwki mgtgppafte
      301 vdnpasfads mlvrainyny yyslnawlll cpwwlcfdws mgcipliksv gdwrvialaa
      361 lwlcliglif qalcsedsck rriltlglgf lvipflpasn lffrvgfvva ervlylpsag
      421 ycvlltfgfg alsrhtkkkk pvaaiilgil linalrcvir sgewrseeql frsalsvcpl
      481 nakvhynigk nladqgnqta aikyyreavr lnpkyvhamn nlgnilkern elqeaeells
      541 lavqiqpdfa aawmnlgivq nslkrfeeae qsyrtaikhr rkypdcyynl grlyadlnrh
      601 vdalnawrna tvlkpehsla wnnmiilldn tgnlaqaeav grealqlipn dhslmfslan
      661 vlgksqkyke sealflkaik anpnvasyhg nlavlyhrwg hldsakkhye islqldpvav
      721 gtkenysllr rkleqtqkkd v
//
LOCUS       NP_008961                219 aa            linear   PRI 27-APR-2025
DEFINITION  tubulin polymerization-promoting protein [Homo sapiens].
ACCESSION   NP_008961
VERSION     NP_008961.1
DBSOURCE    REFSEQ: accession NM_007030.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Pehlivanoglu,B., Araya,J.C., Lawrence,S., Roa,J.C., Balci,S.,
            Andersen,J.B., Rashid,A., Hsing,A.W., Zhu,B., Gao,Y.T., Koshiol,J.
            and Adsay,V.
  TITLE     TPPP-BRD9 fusion-related gallbladder carcinomas are frequently
            associated with intracholecystic neoplasia, neuroendocrine
            carcinoma, and a distinctive small tubular-type adenocarcinoma
            commonly accompanied with a syringomatous pattern
  JOURNAL   Hum Pathol 150, 67-73 (2024)
   PUBMED   38972607
  REMARK    GeneRIF: TPPP-BRD9 fusion-related gallbladder carcinomas are
            frequently associated with intracholecystic neoplasia,
            neuroendocrine carcinoma, and a distinctive small tubular-type
            adenocarcinoma commonly accompanied with a syringomatous pattern.
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Olah,J., Norris,V., Lehotzky,A. and Ovadi,J.
  TITLE     Perspective Strategies for Interventions in Parkinsonism: Remedying
            the Neglected Role of TPPP
  JOURNAL   Cells 13 (4), 338 (2024)
   PUBMED   38391951
  REMARK    GeneRIF: Perspective Strategies for Interventions in Parkinsonism:
            Remedying the Neglected Role of TPPP.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Yan,Q., Wu,X., Zhou,P., Zhou,Y., Li,X., Liu,Z., Tan,H., Yao,W.,
            Xia,Y. and Zhu,F.
  TITLE     HERV-W Envelope Triggers Abnormal Dopaminergic Neuron Process
            through DRD2/PP2A/AKT1/GSK3 for Schizophrenia Risk
  JOURNAL   Viruses 14 (1), 145 (2022)
   PUBMED   35062349
  REMARK    GeneRIF: HERV-W Envelope Triggers Abnormal Dopaminergic Neuron
            Process through DRD2/PP2A/AKT1/GSK3 for Schizophrenia Risk.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Olah,J., Lehotzky,A., Szenasi,T. and Ovadi,J.
  TITLE     Anti-Aggregative Effect of the Antioxidant DJ-1 on the
            TPPP/p25-Derived Pathological Associations of Alpha-Synuclein
  JOURNAL   Cells 10 (11), 2909 (2021)
   PUBMED   34831132
  REMARK    GeneRIF: Anti-Aggregative Effect of the Antioxidant DJ-1 on the
            TPPP/p25-Derived Pathological Associations of Alpha-Synuclein.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Lehotzky,A., Tirian,L., Tokesi,N., Lenart,P., Szabo,B., Kovacs,J.
            and Ovadi,J.
  TITLE     Dynamic targeting of microtubules by TPPP/p25 affects cell survival
  JOURNAL   J Cell Sci 117 (Pt 25), 6249-6259 (2004)
   PUBMED   15564385
  REMARK    GeneRIF: TPPP/p25 has a role in stabilization of physiological
            microtubular ultrastructures and cell survival
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Tirian,L., Hlavanda,E., Olah,J., Horvath,I., Orosz,F., Szabo,B.,
            Kovacs,J., Szabad,J. and Ovadi,J.
  TITLE     TPPP/p25 promotes tubulin assemblies and blocks mitotic spindle
            formation
  JOURNAL   Proc Natl Acad Sci U S A 100 (24), 13976-13981 (2003)
   PUBMED   14623963
REFERENCE   8  (residues 1 to 219)
  AUTHORS   Hlavanda,E., Kovacs,J., Olah,J., Orosz,F., Medzihradszky,K.F. and
            Ovadi,J.
  TITLE     Brain-specific p25 protein binds to tubulin and microtubules and
            induces aberrant microtubule assemblies at substoichiometric
            concentrations
  JOURNAL   Biochemistry 41 (27), 8657-8664 (2002)
   PUBMED   12093283
REFERENCE   9  (residues 1 to 219)
  AUTHORS   Martin,C.P., Vazquez,J., Avila,J. and Moreno,F.J.
  TITLE     P24, a glycogen synthase kinase 3 (GSK 3) inhibitor
  JOURNAL   Biochim Biophys Acta 1586 (1), 113-122 (2002)
   PUBMED   11781156
REFERENCE   10 (residues 1 to 219)
  AUTHORS   Seki,N., Hattori,A., Sugano,S., Suzuki,Y., Nakagawara,A.,
            Muramatsu,M., Hori,T. and Saito,T.
  TITLE     A novel human gene whose product shares significant homology with
            the bovine brain-specific protein p25 on chromosome 5p15.3
  JOURNAL   J Hum Genet 44 (2), 121-122 (1999)
   PUBMED   10083737
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB478250.2, AB017016.1, BQ066916.1, AW955330.1, AI796918.1,
            DB546894.2 and BU726600.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA294431.1, AB017016.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2145743,
                                           SAMEA2150585 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360578.7/ ENSP00000353785.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.33"
     Protein         1..219
                     /product="tubulin polymerization-promoting protein"
                     /note="glycogen synthase kinase 3 (GSK3) inhibitor p24;
                     brain specific protein p25 alpha; p25-alpha; 25 kDa
                     brain-specific protein"
                     /calculated_mol_wt=23563
     Region          1..116
                     /region_name="Mediates interaction with LIMK1.
                     /evidence=ECO:0000269|PubMed:18028908"
                     /note="propagated from UniProtKB/Swiss-Prot (O94811.1)"
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94811.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1 and CDK5.
                     /evidence=ECO:0000269|PubMed:17693641,
                     ECO:0000269|PubMed:23355470, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94811.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1, CDK5 and MAPK1.
                     /evidence=ECO:0000269|PubMed:17693641,
                     ECO:0000269|PubMed:23355470, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (O94811.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ROCK1.
                     /evidence=ECO:0000269|PubMed:17693641,
                     ECO:0000269|PubMed:23093407, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (O94811.1)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O94811.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:23355470,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O94811.1)"
     Region          52..207
                     /region_name="p25-alpha"
                     /note="pfam05517"
                     /db_xref="CDD:461670"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA, in vitro.
                     /evidence=ECO:0000269|PubMed:17693641; propagated from
                     UniProtKB/Swiss-Prot (O94811.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ROCK1.
                     /evidence=ECO:0000269|PubMed:23093407; propagated from
                     UniProtKB/Swiss-Prot (O94811.1)"
     Site            152
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQD2; propagated from
                     UniProtKB/Swiss-Prot (O94811.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ROCK1.
                     /evidence=ECO:0000269|PubMed:17693641,
                     ECO:0000269|PubMed:23093407, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94811.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1, CDK5 and MAPK1.
                     /evidence=ECO:0000269|PubMed:17693641,
                     ECO:0000269|PubMed:23355470; propagated from
                     UniProtKB/Swiss-Prot (O94811.1)"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94811.1)"
     CDS             1..219
                     /gene="TPPP"
                     /gene_synonym="p24; p25; p25alpha; TPPP/p25; TPPP1"
                     /coded_by="NM_007030.3:80..739"
                     /db_xref="CCDS:CCDS3856.1"
                     /db_xref="GeneID:11076"
                     /db_xref="HGNC:HGNC:24164"
                     /db_xref="MIM:608773"
ORIGIN      
        1 madkakpaka anrtppkspg dpskdraakr lslesegage gaaaspelsa leeafrrfav
       61 hgdaratgre mhgknwsklc kdcqvidgrn vtvtdvdivf skikgkscrt itfeqfqeal
      121 eelakkrfkd ksseeavrev hrliegkapi isgvtkaiss ptvsrltdtt kftgshkerf
      181 dpsgkgkgka grvdlvdesg yvsgykhagt ydqkvqggk
//
LOCUS       NP_000971                176 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein eL20 [Homo sapiens].
ACCESSION   NP_000971
VERSION     NP_000971.1
DBSOURCE    REFSEQ: accession NM_000980.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Dhar,D., Mapa,K., Pudi,R., Srinivasan,P., Bodhinathan,K. and Das,S.
  TITLE     Human ribosomal protein L18a interacts with hepatitis C virus
            internal ribosome entry site
  JOURNAL   Arch Virol 151 (3), 509-524 (2006)
   PUBMED   16195786
  REMARK    GeneRIF: L18a might influence the HCV IRES mediated translation.
REFERENCE   6  (residues 1 to 176)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   7  (residues 1 to 176)
  AUTHORS   Jakel,S., Mingot,J.M., Schwarzmaier,P., Hartmann,E. and Gorlich,D.
  TITLE     Importins fulfil a dual function as nuclear import receptors and
            cytoplasmic chaperones for exposed basic domains
  JOURNAL   EMBO J 21 (3), 377-386 (2002)
   PUBMED   11823430
REFERENCE   8  (residues 1 to 176)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 176)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 176)
  AUTHORS   Gramatikoff,K., Schaffner,W. and Georgiev,O.
  TITLE     The leucine zipper of c-Jun binds to ribosomal protein L18a: a role
            in Jun protein regulation?
  JOURNAL   Biol Chem Hoppe Seyler 376 (5), 321-325 (1995)
   PUBMED   7662174
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from HY050156.1, BC007512.2 and BI753938.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a member of the
            L18AE family of ribosomal proteins that is a component of the 60S
            subunit. The encoded protein may play a role in viral replication
            by interacting with the hepatitis C virus internal ribosome entry
            site (IRES). This gene is co-transcribed with the U68 snoRNA,
            located within the third intron. As is typical for genes encoding
            ribosomal proteins, there are multiple processed pseudogenes of
            this gene dispersed throughout the genome. [provided by RefSeq, Jul
            2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD174123.1, CD173034.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222247.10/ ENSP00000222247.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..176
                     /product="large ribosomal subunit protein eL20"
                     /note="60S ribosomal protein L18a; ribosomal protein
                     L18a-like protein"
                     /calculated_mol_wt=20631
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q02543.2)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q02543.2)"
     Region          83..130
                     /region_name="Ribosomal_L18A"
                     /note="Ribosomal proteins 50S-L18Ae/60S-L20/60S-L18A;
                     pfam01775"
                     /db_xref="CDD:396369"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62717; propagated from
                     UniProtKB/Swiss-Prot (Q02543.2)"
     CDS             1..176
                     /gene="RPL18A"
                     /gene_synonym="eL20; L18A"
                     /coded_by="NM_000980.4:48..578"
                     /db_xref="CCDS:CCDS12367.1"
                     /db_xref="GeneID:6142"
                     /db_xref="HGNC:HGNC:10311"
                     /db_xref="MIM:604178"
ORIGIN      
        1 mkasgtlrey kvvgrclptp kchtpplyrm rifapnhvva ksrfwyfvsq lkkmkkssge
       61 ivycgqvfek splrvknfgi wlrydsrsgt hnmyreyrdl ttagavtqcy rdmgarhrar
      121 ahsiqimkve eiaaskcrrp avkqfhdski kfplphrvlr rqhkprfttk rpntff
//
LOCUS       NP_059103               1165 aa            linear   ROD 27-APR-2025
DEFINITION  sperm-associated antigen 5 [Mus musculus].
ACCESSION   NP_059103
VERSION     NP_059103.1
DBSOURCE    REFSEQ: accession NM_017407.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1165)
  AUTHORS   Guo,L., Yuan,H., Zhu,H., Zhou,J., Wan,Z. and Zhou,Y.
  TITLE     SPAG5 deficiency activates autophagy to reduce atherosclerotic
            plaque formation in ApoE-/- mice
  JOURNAL   BMC Cardiovasc Disord 24 (1), 275 (2024)
   PUBMED   38807081
  REMARK    GeneRIF: SPAG5 deficiency activates autophagy to reduce
            atherosclerotic plaque formation in ApoE[-/-] mice.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1165)
  AUTHORS   Mora-Bermudez,F., Kanis,P., Macak,D., Peters,J., Naumann,R.,
            Xing,L., Sarov,M., Winkler,S., Oegema,C.E., Haffner,C.,
            Wimberger,P., Riesenberg,S., Maricic,T., Huttner,W.B. and Paabo,S.
  TITLE     Longer metaphase and fewer chromosome segregation errors in modern
            human than Neanderthal brain development
  JOURNAL   Sci Adv 8 (30), eabn7702 (2022)
   PUBMED   35905187
REFERENCE   3  (residues 1 to 1165)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1165)
  AUTHORS   Lau,E.O., Damiani,D., Chehade,G., Ruiz-Reig,N., Saade,R.,
            Jossin,Y., Aittaleb,M., Schakman,O., Tajeddine,N., Gailly,P. and
            Tissir,F.
  TITLE     DIAPH3 deficiency links microtubules to mitotic errors, defective
            neurogenesis, and brain dysfunction
  JOURNAL   Elife 10, e61974 (2021)
   PUBMED   33899739
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1165)
  AUTHORS   Ulmke,P.A., Sakib,M.S., Ditte,P., Sokpor,G., Kerimoglu,C., Pham,L.,
            Xie,Y., Mao,X., Rosenbusch,J., Teichmann,U., Nguyen,H.P.,
            Fischer,A., Eichele,G., Staiger,J.F. and Tuoc,T.
  TITLE     Molecular Profiling Reveals Involvement of ESCO2 in Intermediate
            Progenitor Cell Maintenance in the Developing Mouse Cortex
  JOURNAL   Stem Cell Reports 16 (4), 968-984 (2021)
   PUBMED   33798452
REFERENCE   6  (residues 1 to 1165)
  AUTHORS   Xue,J., Tarnasky,H.A., Rancourt,D.E. and van Der Hoorn,F.A.
  TITLE     Targeted disruption of the testicular SPAG5/deepest protein does
            not affect spermatogenesis or fertility
  JOURNAL   Mol Cell Biol 22 (7), 1993-1997 (2002)
   PUBMED   11884588
REFERENCE   7  (residues 1 to 1165)
  AUTHORS   Mack,G.J. and Compton,D.A.
  TITLE     Analysis of mitotic microtubule-associated proteins using mass
            spectrometry identifies astrin, a spindle-associated protein
  JOURNAL   Proc Natl Acad Sci U S A 98 (25), 14434-14439 (2001)
   PUBMED   11724960
REFERENCE   8  (residues 1 to 1165)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
REFERENCE   9  (residues 1 to 1165)
  AUTHORS   Shao,X., Xue,J. and van der Hoorn,F.A.
  TITLE     Testicular protein Spag5 has similarity to mitotic spindle protein
            Deepest and binds outer dense fiber protein Odf1
  JOURNAL   Mol Reprod Dev 59 (4), 410-416 (2001)
   PUBMED   11468777
REFERENCE   10 (residues 1 to 1165)
  AUTHORS   Nehls,M., Luno,K., Schorpp,M., Pfeifer,D., Krause,S.,
            Matysiak-Scholze,U., Dierbach,H. and Boehm,T.
  TITLE     YAC/P1 contigs defining the location of 56 microsatellite markers
            and several genes across a 3.4-cM interval on mouse chromosome 11
  JOURNAL   Mamm Genome 6 (5), 321-331 (1995)
   PUBMED   7626882
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591070.19.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052672.1, AK076619.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849380, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1165
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 46.74 cM"
     Protein         1..1165
                     /product="sperm-associated antigen 5"
                     /note="astrin; microtubule-associated protein; mitotic
                     spindle-associated protein p126"
                     /calculated_mol_wt=129862
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TME2.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q7TME2.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q7TME2.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96R06; propagated from
                     UniProtKB/Swiss-Prot (Q7TME2.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96R06; propagated from
                     UniProtKB/Swiss-Prot (Q7TME2.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96R06; propagated from
                     UniProtKB/Swiss-Prot (Q7TME2.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96R06; propagated from
                     UniProtKB/Swiss-Prot (Q7TME2.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96R06; propagated from
                     UniProtKB/Swiss-Prot (Q7TME2.1)"
     Region          431..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TME2.1)"
     Region          453..821
                     /region_name="Interaction with KNSTRN.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TME2.1)"
     Region          <521..>1070
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          875..907
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TME2.1)"
     Site            946
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:Q96R06; propagated from
                     UniProtKB/Swiss-Prot (Q7TME2.1)"
     CDS             1..1165
                     /gene="Spag5"
                     /gene_synonym="D11Bhm180e; Deepest; MAP126; Mastrin; S17"
                     /coded_by="NM_017407.3:70..3567"
                     /db_xref="CCDS:CCDS25098.1"
                     /db_xref="GeneID:54141"
                     /db_xref="MGI:MGI:1927470"
ORIGIN      
        1 mwrvktlnlg lspspqkgkp amstplrelk lqpealadsg kgpsmisalt pylcrlelke
       61 rcnnsspvdf intennflse qfshpsthie acqresdptp esnslfhtle eaietvddfv
      121 vdprddsive smvllpfslg qqqdlmlqah ldttaertks slneslgled lvgkevapcv
      181 edslteivai rpeqptfqdp plgpsdteda pvdlvpsenv lnfslarlsp savlaqdfsv
      241 dhvdpgeetv enrvlqemet sfptfpeeae lgdqapaana eavsplylts slvemgprea
      301 pgptvedasr ipglesetwm splawlekgv ntsvmlqnlr qslsfssvlq daavgntpla
      361 tcsvgtsftp paplevgtkd stseterlll gcrppdlatl srhdleenll nslvllevls
      421 hqlqawksql tvphreards stqtdsspcg vtktpkhlqd skeirqallq arnvmqswgl
      481 vsgdllsllh lslthvqegr vtvsqesqrs ktlvsscsrv lkklkaklqs lkteceearh
      541 skemalkgka aaeavleafr ahasqrisql eqgltsmqef rgllqeaqtq liglhteqke
      601 laqqtvslss alqqdwtsvq lnygiwaall swsreltkkl taksrqalqe rdaaieekkq
      661 vvkeveqvsa hledckgqie qlklensrlt adlsaqlqil tstesqlkev rsqhsrcvqd
      721 lavkdellcq ltqsnkeqat qwqkeemelk hiqaellqqq avlakevqdl retvefidee
      781 sqvahrelgq iesqlkvtle llrerslqce tlrdtvdslr aelasteakh ekqalekthq
      841 hsqelrllae qlqsltlflq aklkenkaes eiilpstgsa paqehplsnd ssiseqtpta
      901 avdevpepap vpllgsvksa ftrvasmasf qptetpdlek slaemstvlq elkslcsllq
      961 eskeeatgvl qreicelhsr lqaqeeehqe alkakeadme klnqalcllr knekellevi
     1021 qkqnekilgq idksgqlinl reevtqltqs lrraetetkv lqealegqld pscqlmatnw
     1081 iqekvflsqe vsklrvmfle mktekeqlmd kylshrhile enlrrsdtel kklddtiqhv
     1141 yetllsipet mksckelqgl lefls
//
LOCUS       NP_057307                424 aa            linear   PRI 27-APR-2025
DEFINITION  protein kinase C and casein kinase substrate in neurons protein 3
            [Homo sapiens].
ACCESSION   NP_057307 XP_005252937
VERSION     NP_057307.2
DBSOURCE    REFSEQ: accession NM_016223.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Tanaka,M., Nanba,D., Mori,S., Shiba,F., Ishiguro,H., Yoshino,K.,
            Matsuura,N. and Higashiyama,S.
  TITLE     ADAM binding protein Eve-1 is required for ectodomain shedding of
            epidermal growth factor receptor ligands
  JOURNAL   J Biol Chem 279 (40), 41950-41959 (2004)
   PUBMED   15280379
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Kessels,M.M. and Qualmann,B.
  TITLE     The syndapin protein family: linking membrane trafficking with the
            cytoskeleton
  JOURNAL   J Cell Sci 117 (Pt 15), 3077-3086 (2004)
   PUBMED   15226389
  REMARK    Review article
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Mori,S., Tanaka,M., Nanba,D., Nishiwaki,E., Ishiguro,H.,
            Higashiyama,S. and Matsuura,N.
  TITLE     PACSIN3 binds ADAM12/meltrin alpha and up-regulates ectodomain
            shedding of heparin-binding epidermal growth factor-like growth
            factor
  JOURNAL   J Biol Chem 278 (46), 46029-46034 (2003)
   PUBMED   12952982
  REMARK    GeneRIF: PACSIN3 has a novel function as an up-regulator in the
            signaling of proHB-EGF shedding induced by TPA and angiotensin II
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Sumoy,L., Pluvinet,R., Andreu,N., Estivill,X. and Escarceller,M.
  TITLE     PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the
            pacsin-syndapin-FAP52 gene family
  JOURNAL   Gene 262 (1-2), 199-205 (2001)
   PUBMED   11179684
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Modregger,J., Ritter,B., Witter,B., Paulsson,M. and Plomann,M.
  TITLE     All three PACSIN isoforms bind to endocytic proteins and inhibit
            endocytosis
  JOURNAL   J Cell Sci 113 Pt 24, 4511-4521 (2000)
   PUBMED   11082044
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Howard,L., Nelson,K.K., Maciewicz,R.A. and Blobel,C.P.
  TITLE     Interaction of the metalloprotease disintegrins MDC9 and MDC15 with
            two SH3 domain-containing proteins, endophilin I and SH3PX1
  JOURNAL   J Biol Chem 274 (44), 31693-31699 (1999)
   PUBMED   10531379
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI601317.1, BC011889.2 and
            BC007914.2.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_005252937.1, NP_057307.1.
            
            Summary: This gene is a member of the protein kinase C and casein
            kinase substrate in neurons family. The encoded protein is involved
            in linking the actin cytoskeleton with vesicle formation.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF242530.1, BC007914.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298838.11/ ENSP00000298838.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..424
                     /product="protein kinase C and casein kinase substrate in
                     neurons protein 3"
                     /note="syndapin III; SH3 domain-containing protein 6511"
                     /calculated_mol_wt=48356
     Region          16..273
                     /region_name="BAR"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain, a
                     dimerization module that binds membranes and detects
                     membrane curvature; cl12013"
                     /db_xref="CDD:472257"
     Site            order(25,28..29,33,35..36,39..40,42..43,53..54,56..57,
                     60..61,63..64,67,87,90..91,232,235..236,238,240,243..244,
                     246..247,250..251,254..255,257..258,261..262,264..265)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153365"
     Region          155..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JB8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Region          311..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Region          365..420
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(372,374,377,381,400..401,415,417..418)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212930"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     CDS             1..424
                     /gene="PACSIN3"
                     /gene_synonym="SDPIII"
                     /coded_by="NM_016223.5:190..1464"
                     /db_xref="CCDS:CCDS31481.1"
                     /db_xref="GeneID:29763"
                     /db_xref="HGNC:HGNC:8572"
                     /db_xref="MIM:606513"
ORIGIN      
        1 mapeedagge alggsfweag nyrrtvqrve dghrlcgdlv scfqerarie kayaqqladw
       61 arkwrgtvek gpqygtleka whafftaaer lsalhlevre klqgqdserv rawqrgafhr
      121 pvlggfresr aaedgfrkaq kpwlkrlkev easkksyhaa rkdektaqtr eshakadsav
      181 sqeqlrklqe rvercakeae ktkaqyeqtl aelhrytpry medmeqafet cqaaerqrll
      241 ffkdmlltlh qhldlsssek fhelhrdlhq gieaasdeed lrwwrsthgp gmamnwpqfe
      301 ewsldtqrti srkekggrsp devtltsivp trdgtapppq spgspgtgqd eewsdeespr
      361 kaatgvrvra lydyagqead elsfrageel lkmseedeqg wcqgqlqsgr iglypanyve
      421 cvga
//
LOCUS       NP_001034568             823 aa            linear   PRI 27-APR-2025
DEFINITION  apoptosis-resistant E3 ubiquitin protein ligase 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001034568
VERSION     NP_001034568.1
DBSOURCE    REFSEQ: accession NM_001039479.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Li,Y., Song,Y. and Liang,Y.
  TITLE     AREL1 resists the apoptosis induced by TGF-beta by inhibiting SMAC
            in vascular endothelial cells
  JOURNAL   J Biochem Mol Toxicol 37 (10), e23439 (2023)
   PUBMED   37522329
  REMARK    GeneRIF: AREL1 resists the apoptosis induced by TGF-beta by
            inhibiting SMAC in vascular endothelial cells.
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Rydbirk,R., Folke,J., Busato,F., Roche,E., Chauhan,A.S.,
            Lokkegaard,A., Hejl,A.M., Bode,M., Blaabjerg,M., Moller,M.,
            Danielsen,E.H., Brudek,T., Pakkenberg,B., Tost,J. and Aznar,S.
  TITLE     Epigenetic modulation of AREL1 and increased HLA expression in
            brains of multiple system atrophy patients
  JOURNAL   Acta Neuropathol Commun 8 (1), 29 (2020)
   PUBMED   32151281
  REMARK    GeneRIF: Epigenetic modulation of AREL1 and increased HLA
            expression in brains of multiple system atrophy patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Singh,S., Ng,J., Nayak,D. and Sivaraman,J.
  TITLE     Structural insights into a HECT-type E3 ligase AREL1 and its
            ubiquitination activities in vitro
  JOURNAL   J Biol Chem 294 (52), 19934-19949 (2019)
   PUBMED   31732561
  REMARK    GeneRIF: The AREL1 HECT domain assembled Lys(33)-, Lys(48)-, and
            Lys(63)-linked polyubiquitin chains. E701A substitution in the
            AREL1 HECT domain substantially increased its
            autopolyubiquitination and SMAC ubiquitination activity, whereas
            deletion of the last three amino acids at the C terminus completely
            abrogated AREL1 autoubiquitination and reduced SMAC ubiquitination.
REFERENCE   4  (residues 1 to 823)
  AUTHORS   Lear,T.B., McKelvey,A.C., Evankovich,J.W., Rajbhandari,S.,
            Coon,T.A., Dunn,S.R., Londino,J.D., McVerry,B.J., Zhang,Y.,
            Valenzi,E., Burton,C.L., Gordon,R., Gingras,S., Lockwood,K.C.,
            Jurczak,M.J., Lafyatis,R., Shlomchik,M.J., Liu,Y. and Chen,B.B.
  TITLE     KIAA0317 regulates pulmonary inflammation through SOCS2 degradation
  JOURNAL   JCI Insight 4 (19), 129110 (2019)
   PUBMED   31578312
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 823)
  AUTHORS   Lear,T., McKelvey,A.C., Rajbhandari,S., Dunn,S.R., Coon,T.A.,
            Connelly,W., Zhao,J.Y., Kass,D.J., Zhang,Y., Liu,Y. and Chen,B.B.
  TITLE     Ubiquitin E3 ligase FIEL1 regulates fibrotic lung injury through
            SUMO-E3 ligase PIAS4
  JOURNAL   J Exp Med 213 (6), 1029-1046 (2016)
   PUBMED   27162139
  REMARK    GeneRIF: new protein isoform encoded by KIAA0317, termed
            fibrosis-inducing E3 ligase 1 (FIEL1), which potently stimulates
            the TGFbeta signaling pathway through the site-specific
            ubiquitination of PIAS4.
REFERENCE   6  (residues 1 to 823)
  AUTHORS   Michel,M.A., Elliott,P.R., Swatek,K.N., Simicek,M., Pruneda,J.N.,
            Wagstaff,J.L., Freund,S.M. and Komander,D.
  TITLE     Assembly and specific recognition of k29- and k33-linked
            polyubiquitin
  JOURNAL   Mol Cell 58 (1), 95-109 (2015)
   PUBMED   25752577
REFERENCE   7  (residues 1 to 823)
  AUTHORS   Kim,J.B., Kim,S.Y., Kim,B.M., Lee,H., Kim,I., Yun,J., Jo,Y., Oh,T.,
            Jo,Y., Chae,H.D. and Shin,D.Y.
  TITLE     Identification of a novel anti-apoptotic E3 ubiquitin ligase that
            ubiquitinates antagonists of inhibitor of apoptosis proteins SMAC,
            HtrA2, and ARTS
  JOURNAL   J Biol Chem 288 (17), 12014-12021 (2013)
   PUBMED   23479728
REFERENCE   8  (residues 1 to 823)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI459956.1, BC032944.2, AB002315.1 and AC007956.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304217.1, SRR1803617.12469.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356357.9/ ENSP00000348714.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..823
                     /product="apoptosis-resistant E3 ubiquitin protein ligase
                     1 isoform 1"
                     /EC_number="2.3.2.26"
                     /note="fibrosis-inducing E3 ligase 1; apoptosis-resistant
                     HECT-type E3 ubiquitin transferase 1"
                     /calculated_mol_wt=94092
     Region          52..158
                     /region_name="Filamin"
                     /note="propagated from UniProtKB/Swiss-Prot (O15033.3)"
     Region          56..154
                     /region_name="Filamin"
                     /note="Filamin/ABP280 repeat; pfam00630"
                     /db_xref="CDD:395505"
     Region          315..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15033.3)"
     Site            order(468,498,509,577,754,784..785,788..792,812,820)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          483..789
                     /region_name="Interaction with SOCS2.
                     /evidence=ECO:0000269|PubMed:31578312"
                     /note="propagated from UniProtKB/Swiss-Prot (O15033.3)"
     Region          486..820
                     /region_name="HECTc"
                     /note="Domain Homologous to E6-AP Carboxyl Terminus with;
                     smart00119"
                     /db_xref="CDD:214523"
     Site            order(605,608..609,611..612,615,621,623,627..628,630,636,
                     642,659,663)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..823
                     /gene="AREL1"
                     /gene_synonym="FIEL1; KIAA0317"
                     /coded_by="NM_001039479.2:482..2953"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41971.1"
                     /db_xref="GeneID:9870"
                     /db_xref="HGNC:HGNC:20363"
                     /db_xref="MIM:615380"
ORIGIN      
        1 mfyviggitv svvaffftik flfelaarvv sflqnedrer rgdrtiydyv rgnyldprsc
       61 kvswdwkdpy evghsmafrv hlfykngqpf pahrpvglrv hishvelave ipvtqevlqe
      121 pnsnvvkvaf tvrkagryei tvklgglnva yspyykifqp gmvvpsktki vchfstlvlt
      181 cgqphtlqiv prdeydnptn nsmslrdehn ytlsihelgp qeeestgvsf eksvtsnrqt
      241 fqvflrltlh srgcfhacis yqnqpinnge fdiivlsede knivernvst sgvsiyfeay
      301 lynatncsst pwhlppmhmt ssqrrpstav deededspse chtpekvkkp kkvycyvspk
      361 qfsvkefylk iipwrlytfr vcpgtkfsyl gpdpvhkllt lvvddgiqpp velsckerni
      421 laatfirslh kniggsetfq dkvnffqrel rqvhmkrphs kvtlkvsrha llesslkatr
      481 nfsisdwskn fevvfqdeea ldwggprrew felickalfd ttnqlftrfs dnnqalvhpn
      541 pnrpahlrlk myefagrlvg kclyesslgg aykqlvrarf trsflaqiig lrmhykyfet
      601 ddpefykskv cfilnndmse melvfaeeky nksgqldkvv elmtggaqtp vtnankifyl
      661 nllaqyrlas qvkeevehfl kglnelvpen llaifdenel ellmcgtgdi svsdfkahav
      721 vvggswhfre kvmrwfwtvv ssltqeelar llqfttgssq lppggfaalc psfqiiaapt
      781 hstlptahtc fnqlclptyd syeevhrmlq laisegcegf gml
//
LOCUS       NP_032674                178 aa            linear   ROD 27-APR-2025
DEFINITION  major urinary protein 4 precursor [Mus musculus].
ACCESSION   NP_032674
VERSION     NP_032674.1
DBSOURCE    REFSEQ: accession NM_008648.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Charkoftaki,G., Wang,Y., McAndrews,M., Bruford,E.A., Thompson,D.C.,
            Vasiliou,V. and Nebert,D.W.
  TITLE     Update on the human and mouse lipocalin (LCN) gene family,
            including evidence the mouse Mup cluster is result of an
            'evolutionary bloom'
  JOURNAL   Hum Genomics 13 (1), 11 (2019)
   PUBMED   30782214
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Perez-Miller,S., Zou,Q., Novotny,M.V. and Hurley,T.D.
  TITLE     High resolution X-ray structures of mouse major urinary protein
            nasal isoform in complex with pheromones
  JOURNAL   Protein Sci 19 (8), 1469-1479 (2010)
   PUBMED   20509168
  REMARK    GeneRIF: Data determine the X-ray crystal structure of major
            urinary protein-IV bound to three mouse pheromones: SBT,
            2,5-dimethylpyrazine, and 2-heptanone, and report the structure of
            MUP-IV with 2-ethylhexanol bound in the cavity.
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Logan,D.W., Marton,T.F. and Stowers,L.
  TITLE     Species specificity in major urinary proteins by parallel evolution
  JOURNAL   PLoS One 3 (9), e3280 (2008)
   PUBMED   18815613
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Ohashi,Y., Tsuzaka,K., Takeuchi,T., Sasaki,Y. and Tsubota,K.
  TITLE     Altered distribution of aquaporin 5 and its C-terminal binding
            protein in the lacrimal glands of a mouse model for Sjogren's
            syndrome
  JOURNAL   Curr Eye Res 33 (8), 621-629 (2008)
   PUBMED   18696337
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Chamero,P., Marton,T.F., Logan,D.W., Flanagan,K., Cruz,J.R.,
            Saghatelian,A., Cravatt,B.F. and Stowers,L.
  TITLE     Identification of protein pheromones that promote aggressive
            behaviour
  JOURNAL   Nature 450 (7171), 899-902 (2007)
   PUBMED   18064011
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Sharrow,S.D., Vaughn,J.L., Zidek,L., Novotny,M.V. and Stone,M.J.
  TITLE     Pheromone binding by polymorphic mouse major urinary proteins
  JOURNAL   Protein Sci 11 (9), 2247-2256 (2002)
   PUBMED   12192080
  REMARK    Erratum:[Protein Sci. 2004 Jan;13(1):306]
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Held,W.A., Gallagher,J.F., Hohman,C.M., Kuhn,N.J., Sampsell,B.M.
            and Hughes,R.G. Jr.
  TITLE     Identification and characterization of functional genes encoding
            the mouse major urinary proteins
  JOURNAL   Mol Cell Biol 7 (10), 3705-3712 (1987)
   PUBMED   2824995
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Shahan,K., Denaro,M., Gilmartin,M., Shi,Y. and Derman,E.
  TITLE     Expression of six mouse major urinary protein genes in the mammary,
            parotid, sublingual, submaxillary, and lachrymal glands and in the
            liver
  JOURNAL   Mol Cell Biol 7 (5), 1947-1954 (1987)
   PUBMED   3600653
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Shahan,K., Gilmartin,M. and Derman,E.
  TITLE     Nucleotide sequences of liver, lachrymal, and submaxillary gland
            mouse major urinary protein mRNAs: mosaic structure and
            construction of panels of gene-specific synthetic oligonucleotide
            probes
  JOURNAL   Mol Cell Biol 7 (5), 1938-1946 (1987)
   PUBMED   3600652
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL831738.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012227.1, BF535758.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN00849381,
                                           SAMN00849386 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 32.82 cM"
     Protein         1..178
                     /product="major urinary protein 4 precursor"
                     /note="major urinary protein 1; MUP 4"
                     /calculated_mol_wt=18819
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1741
     mat_peptide     17..178
                     /product="Major urinary protein 4. /id=PRO_0000017930"
                     /note="propagated from UniProtKB/Swiss-Prot (P11590.1)"
                     /calculated_mol_wt=18819
     Region          21..178
                     /region_name="lipocalin_MUP-like"
                     /note="major urinary proteins (MUPs) and similar proteins;
                     cd19428"
                     /db_xref="CDD:381203"
     Site            order(31,35,40,54,56,58..59,61,68,70,72,83,85,87,96,98,
                     104,106,108,117,119,121,132,134,136)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381203"
     CDS             1..178
                     /gene="Mup4"
                     /gene_synonym="Mup-4; Mup1"
                     /coded_by="NM_008648.2:69..605"
                     /db_xref="CCDS:CCDS18228.1"
                     /db_xref="GeneID:17843"
                     /db_xref="MGI:MGI:97236"
ORIGIN      
        1 mklllclglt lvcihaeeat skgqnlnvek ingewfsill asdkrekiee hgsmrvfveh
       61 ihvlenslaf kfhtvidgec seiflvadkt ekageysvmy dgfntftilk tdydnyimfh
      121 linekdgktf qlmelygrka dlnsdikekf vklceehgii keniidltkt nrclkare
//
LOCUS       NP_001348846             326 aa            linear   ROD 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 9 [Mus musculus].
ACCESSION   NP_001348846
VERSION     NP_001348846.1
DBSOURCE    REFSEQ: accession NM_001361917.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC153152.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CK793660.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849379, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="12"
                     /map="12 60.9 cM"
     Protein         1..326
                     /product="ankyrin repeat domain-containing protein 9"
                     /calculated_mol_wt=35382
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH83.1)"
     Region          70..99
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH83.1)"
     Region          <74..227
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          108..109
                     /region_name="Important role in both nutrient sensing and
                     binding/regulation of IMPDH2.
                     /evidence=ECO:0000250|UniProtKB:Q96BM1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH83.1)"
     Region          111..140
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH83.1)"
     Region          157..188
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          157..186
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BH83.1)"
     CDS             1..326
                     /gene="Ankrd9"
                     /gene_synonym="2500003O20Rik"
                     /coded_by="NM_001361917.1:379..1359"
                     /db_xref="CCDS:CCDS26174.1"
                     /db_xref="GeneID:74251"
                     /db_xref="MGI:MGI:1921501"
ORIGIN      
        1 mpwdtrpgrs anggpegpga arlrvqkqcr kssfafylav rdqlpvwlle diraseafhc
       61 dergraaays pseallyalv hdhqayahyl latfprcala ppsagfrcct apgphvalav
      121 rynrvgilrr ilrtvqdfpv eervrlldrr gcsrvegggt slhvacelar peclflllgh
      181 gaspglrdgs gftplelllr qlnqdassap tkaeaasatv naatanttss eevcqrrlll
      241 ldllvlytpg gvvgparcel lgdqlrwqrl lgedkfqwla glappslfvr amqvlvttis
      301 pgrfpealde lplpsflqpl dltgkg
//
LOCUS       NP_006178               1087 aa            linear   PRI 27-APR-2025
DEFINITION  2'-5'-oligoadenylate synthase 3 isoform 1 [Homo sapiens].
ACCESSION   NP_006178
VERSION     NP_006178.2
DBSOURCE    REFSEQ: accession NM_006187.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Benmansour,R., Tagajdid,M.R., El Hamzaoui,H., Fjouji,S., Doghmi,N.,
            Houba,A., Belbacha,I., Elkochri,S., Aabi,R., Elannaz,H.,
            Laraqui,A., El Mchichi,B., Chmitah,T., Touil,N., Ennibi,K.,
            Eljaoudi,R., Elmir,E., Amine Lahlou,I. and Oumzil,H.
  TITLE     TYK2, IFITM3, IFNAR2 and OAS3 single-nucleotide polymorphisms among
            severe COVID-19 ICU patients in Morocco
  JOURNAL   Int J Immunopathol Pharmacol 38, 3946320241257241 (2024)
   PUBMED   38760017
  REMARK    GeneRIF: TYK2, IFITM3, IFNAR2 and OAS3 single-nucleotide
            polymorphisms among severe COVID-19 ICU patients in Morocco.
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Gupta,S., Singh,P., Tasneem,A., Almatroudi,A., Rahmani,A.H.,
            Dohare,R. and Parveen,S.
  TITLE     Integrative Multiomics and Regulatory Network Analyses Uncovers the
            Role of OAS3, TRAFD1, miR-222-3p, and miR-125b-5p in Hepatitis E
            Virus Infection
  JOURNAL   Genes (Basel) 14 (1), 42 (2022)
   PUBMED   36672782
  REMARK    GeneRIF: Integrative Multiomics and Regulatory Network Analyses
            Uncovers the Role of OAS3, TRAFD1, miR-222-3p, and miR-125b-5p in
            Hepatitis E Virus Infection.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Zheng,B., Zhou,X., Tian,L., Wang,J. and Zhang,W.
  TITLE     IFN-beta1b induces OAS3 to inhibit EV71 via IFN-beta1b/JAK/STAT1
            pathway
  JOURNAL   Virol Sin 37 (5), 676-684 (2022)
   PUBMED   35934228
  REMARK    GeneRIF: IFN-beta1b induces OAS3 to inhibit EV71 via
            IFN-beta1b/JAK/STAT1 pathway.
REFERENCE   4  (residues 1 to 1087)
  AUTHORS   Huang,Y.Z., Zheng,Y.X., Zhou,Y., Xu,F., Cui,Y.Z., Chen,X.Y.,
            Wang,Z.Y., Yan,B.X., Zheng,M. and Man,X.Y.
  TITLE     OAS1, OAS2, and OAS3 Contribute to Epidermal Keratinocyte
            Proliferation by Regulating Cell Cycle and Augmenting IFN-1-Induced
            Jak1-Signal Transducer and Activator of Transcription 1
            Phosphorylation in Psoriasis
  JOURNAL   J Invest Dermatol 142 (10), 2635-2645 (2022)
   PUBMED   35305973
  REMARK    GeneRIF: OAS1, OAS2, and OAS3 Contribute to Epidermal Keratinocyte
            Proliferation by Regulating Cell Cycle and Augmenting IFN-1Induced
            Jak1Signal Transducer and Activator of Transcription 1
            Phosphorylation in Psoriasis.
REFERENCE   5  (residues 1 to 1087)
  AUTHORS   Whelan,J.N., Parenti,N.A., Hatterschide,J., Renner,D.M., Li,Y.,
            Reyes,H.M., Dong,B., Perez,E.R., Silverman,R.H. and Weiss,S.R.
  TITLE     Zika virus employs the host antiviral RNase L protein to support
            replication factory assembly
  JOURNAL   Proc Natl Acad Sci U S A 118 (22) (2021)
   PUBMED   34031250
  REMARK    GeneRIF: Zika virus employs the host antiviral RNase L protein to
            support replication factory assembly.
REFERENCE   6  (residues 1 to 1087)
  AUTHORS   Rebouillat,D., Hovnanian,A., Marie,I. and Hovanessian,A.G.
  TITLE     The 100-kDa 2',5'-oligoadenylate synthetase catalyzing
            preferentially the synthesis of dimeric pppA2'p5'A molecules is
            composed of three homologous domains
  JOURNAL   J Biol Chem 274 (3), 1557-1565 (1999)
   PUBMED   9880533
REFERENCE   7  (residues 1 to 1087)
  AUTHORS   Hovnanian,A., Rebouillat,D., Mattei,M.G., Levy,E.R., Marie,I.,
            Monaco,A.P. and Hovanessian,A.G.
  TITLE     The human 2',5'-oligoadenylate synthetase locus is composed of
            three distinct genes clustered on chromosome 12q24.2 encoding the
            100-, 69-, and 40-kDa forms
  JOURNAL   Genomics 52 (3), 267-277 (1998)
   PUBMED   9790745
REFERENCE   8  (residues 1 to 1087)
  AUTHORS   Marie,I., Blanco,J., Rebouillat,D. and Hovanessian,A.G.
  TITLE     69-kDa and 100-kDa isoforms of interferon-induced
            (2'-5')oligoadenylate synthetase exhibit differential catalytic
            parameters
  JOURNAL   Eur J Biochem 248 (2), 558-566 (1997)
   PUBMED   9346316
REFERENCE   9  (residues 1 to 1087)
  AUTHORS   Silverman,R.H. and Sengupta,D.N.
  TITLE     Translational regulation by HIV leader RNA, TAT, and
            interferon-inducible enzymes
  JOURNAL   J Exp Pathol 5 (2), 69-77 (1990)
   PUBMED   1708818
REFERENCE   10 (residues 1 to 1087)
  AUTHORS   Hovanessian,A.G., Laurent,A.G., Chebath,J., Galabru,J., Robert,N.
            and Svab,J.
  TITLE     Identification of 69-kd and 100-kd forms of 2-5A synthetase in
            interferon-treated human cells by specific monoclonal antibodies
  JOURNAL   EMBO J 6 (5), 1273-1280 (1987)
   PUBMED   2440675
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC113746.1, AB044545.1,
            AC004551.1 and AF063613.1.
            
            On Mar 4, 2004 this sequence version replaced NP_006178.1.
            
            Summary: This gene encodes an enzyme included in the 2', 5'
            oligoadenylate synthase family.  This enzyme is induced by
            interferons and catalyzes the 2', 5' oligomers of adenosine in
            order to bind and activate RNase L.  This enzyme family plays a
            significant role in the inhibition of cellular protein synthesis
            and viral infection resistance. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB044545.1, AF063613.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000228928.12/ ENSP00000228928.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.13"
     Protein         1..1087
                     /product="2'-5'-oligoadenylate synthase 3 isoform 1"
                     /EC_number="2.7.7.84"
                     /note="2'-5'oligoadenylate synthetase p100;
                     2'-5'-oligoadenylate synthase 3; p100 OAS; 2-5A synthetase
                     3; (2-5')oligo(A) synthetase 3; 2-5A synthase 3;
                     (2-5')oligo(A) synthase 3; 2'-5'-oligoadenylate synthetase
                     3, 100kDa"
                     /calculated_mol_wt=121040
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6K5.3)"
     Region          6..343
                     /region_name="OAS domain 1. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6K5.3)"
     Region          12..57
                     /region_name="Interaction with dsRNA.
                     /evidence=ECO:0000269|PubMed:25775560"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6K5.3)"
     Region          46..172
                     /region_name="NT_2-5OAS_ClassI-CCAase"
                     /note="Nucleotidyltransferase (NT) domain of
                     2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I
                     CCA-adding enzyme; cd05400"
                     /db_xref="CDD:143390"
     Site            order(60..62,65,67..69,74,76,123..124,127,145,159,163,166)
                     /site_type="active"
                     /db_xref="CDD:143390"
     Site            order(61..62,74,76,124,159,163,166)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143390"
     Site            order(74,76,145)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143390"
     Site            155
                     /site_type="other"
                     /note="Interaction with dsRNA.
                     /evidence=ECO:0000269|PubMed:25775560; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6K5.3)"
     Region          161..343
                     /region_name="OAS1_C"
                     /note="2'-5'-oligoadenylate synthetase 1, domain 2,
                     C-terminus; pfam10421"
                     /db_xref="CDD:463087"
     Region          186..200
                     /region_name="Interaction with dsRNA.
                     /evidence=ECO:0000269|PubMed:25775560"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6K5.3)"
     Site            244
                     /site_type="other"
                     /note="Interaction with dsRNA.
                     /evidence=ECO:0000269|PubMed:25775560; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6K5.3)"
     Region          344..410
                     /region_name="Linker. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6K5.3)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6K5.3)"
     Region          411..742
                     /region_name="OAS domain 2. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6K5.3)"
     Region          430..571
                     /region_name="NT_2-5OAS_ClassI-CCAase"
                     /note="Nucleotidyltransferase (NT) domain of
                     2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I
                     CCA-adding enzyme; cd05400"
                     /db_xref="CDD:143390"
     Site            order(459..461,464,466..468,473,475,511,514,544,562,565)
                     /site_type="active"
                     /db_xref="CDD:143390"
     Site            order(460..461,473,475,511,562,565)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143390"
     Site            order(473,475,544)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143390"
     Region          559..745
                     /region_name="OAS1_C"
                     /note="2'-5'-oligoadenylate synthetase 1, domain 2,
                     C-terminus; pfam10421"
                     /db_xref="CDD:463087"
     Region          750..1084
                     /region_name="OAS domain 3. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6K5.3)"
     Region          769..948
                     /region_name="NT_2-5OAS_ClassI-CCAase"
                     /note="Nucleotidyltransferase (NT) domain of
                     2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I
                     CCA-adding enzyme; cd05400"
                     /db_xref="CDD:143390"
     Site            order(802..804,807,809..811,816,818,859,866,869,888,934,
                     938,941)
                     /site_type="active"
                     /db_xref="CDD:143390"
     Site            order(803..804,816,818,866,934,938,941)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143390"
     Site            order(816,818,888)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143390"
     Region          903..1086
                     /region_name="OAS1_C"
                     /note="2'-5'-oligoadenylate synthetase 1, domain 2,
                     C-terminus; pfam10421"
                     /db_xref="CDD:463087"
     CDS             1..1087
                     /gene="OAS3"
                     /gene_synonym="p100; p100OAS"
                     /coded_by="NM_006187.4:58..3321"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44981.1"
                     /db_xref="GeneID:4940"
                     /db_xref="HGNC:HGNC:8088"
                     /db_xref="MIM:603351"
ORIGIN      
        1 mdlystpaaa ldrfvarrlq prkefvekar ralgalaaal rerggrlgaa aprvlktvkg
       61 gssgrgtalk ggcdselvif ldcfksyvdq rarraeilse mrasleswwq npvpglrltf
      121 peqsvpgalq frltsvdled wmdvslvpaf nvlgqagsgv kpkpqvystl lnsgcqggeh
      181 aacftelrrn fvnirpaklk nlillvkhwy hqvclqglwk etlppvyale lltifaweqg
      241 ckkdafslae glrtvlgliq qhqhlcvfwt vnygfedpav gqflqrqlkr prpvildpad
      301 ptwdlgngaa whwdllaqea ascydhpcfl rgmgdpvqsw kgpglpragc sglghpiqld
      361 pnqktpensk slnavyprag skppscpapg ptgaasivps vpgmaldlsq iptkeldrfi
      421 qdhlkpspqf qeqvkkaidi ilrclhencv hkasrvskgg sfgrgtdlrd gcdveliifl
      481 ncftdykdqg prraeildem raqleswwqd qvpslslqfp eqnvpealqf qlvstalksw
      541 tdvsllpafd avgqlssgtk pnpqvysrll tsgcqegehk acfaelrrnf mnirpvklkn
      601 lillvkhwyr qvaaqnkgkg papaslppay alelltifaw eqgcrqdcfn maqgfrtvlg
      661 lvqqhqqlcv ywtvnysted pamrmhllgq lrkprplvld padptwnvgh gswellaqea
      721 aalgmqacfl srdgtsvqpw dvmpallyqt pagdldkfis eflqpnrqfl aqvnkavdti
      781 csflkencfr nspikvikvv kggssakgta lrgrsdadlv vflscfsqft eqgnkraeii
      841 seiraqleac qqerqfevkf evskwenprv lsfsltsqtm ldqsvdfdvl pafdalgqlv
      901 sgsrpssqvy vdlihsysna geystcftel qrdfiisrpt klkslirlvk hwyqqctkis
      961 kgrgslppqh glelltvyaw eqggkdsqfn maegfrtvle lvtqyrqlci ywtinynakd
     1021 ktvgdflkqq lqkprpiild padptgnlgh narwdllake aaactsalcc mgrngipiqp
     1081 wpvkaav
//
LOCUS       NP_001560                712 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-1 receptor-associated kinase 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001560
VERSION     NP_001560.2
DBSOURCE    REFSEQ: accession NM_001569.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Rao,Z., Ao,G., Zhang,Y., Jiang,Z., Li,L. and Hua,Z.
  TITLE     HNRNP I promotes IRAK1 degradation to reduce podocyte apoptosis and
            inflammatory response alleviating renal injury in diabetic
            nephropathy
  JOURNAL   Immunobiology 229 (5), 152835 (2024)
   PUBMED   38986278
  REMARK    GeneRIF: HNRNP I promotes IRAK1 degradation to reduce podocyte
            apoptosis and inflammatory response alleviating renal injury in
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Chen,J.J., Lu,T.Z., Wang,T., Yan,W.H., Zhong,F.Y., Qu,X.H.,
            Gong,X.C., Li,J.G., Tou,F.F., Jiang,L.P. and Han,X.J.
  TITLE     The m6A reader HNRNPC promotes glioma progression by enhancing the
            stability of IRAK1 mRNA through the MAPK pathway
  JOURNAL   Cell Death Dis 15 (6), 390 (2024)
   PUBMED   38830885
  REMARK    GeneRIF: The m6A reader HNRNPC promotes glioma progression by
            enhancing the stability of IRAK1 mRNA through the MAPK pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Zhu,D., Nie,Y., Zhao,Y., Chen,X., Yang,Z. and Yang,Y.
  TITLE     RNF152 Suppresses Fatty Acid Oxidation and Metastasis of Lung
            Adenocarcinoma by Inhibiting IRAK1-Mediated AKR1B10 Expression
  JOURNAL   Am J Pathol 193 (10), 1603-1617 (2023)
   PUBMED   37717980
  REMARK    GeneRIF: RNF152 Suppresses Fatty Acid Oxidation and Metastasis of
            Lung Adenocarcinoma by Inhibiting IRAK1-Mediated AKR1B10
            Expression.
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Zaghloul,H.M., Abdelshafy,S.S., Abdelaleem,E.A., Ali,H.M. and
            Khattab,R.A.M.
  TITLE     Transmembrane Protein 187 (TMEM187) and Interleukin 1 Receptor
            Associated Kinase (IRAK1) gene polymorphism association with
            rheumatoid arthritis susceptibility in Egyptian patients
  JOURNAL   Egypt J Immunol 30 (3), 171-179 (2023)
   PUBMED   37440666
  REMARK    GeneRIF: Transmembrane Protein 187 (TMEM187) and Interleukin 1
            Receptor Associated Kinase (IRAK1) gene polymorphism association
            with rheumatoid arthritis susceptibility in Egyptian patients.
REFERENCE   5  (residues 1 to 712)
  AUTHORS   Zhou,M., Liu,Y., Xu,H., Chen,X., Zheng,N., Duan,Z., Ge,Y., Li,D.,
            Lin,T., Zeng,R., Chen,Q. and Li,M.
  TITLE     YTHDC1-Modified m6A Methylation of Hsa_circ_0102678 Promotes
            Keratinocyte Inflammation Induced by Cutibacterium acnes Biofilm
            through Regulating miR-146a/TRAF6 and IRAK1 Axis
  JOURNAL   J Innate Immun 15 (1), 822-835 (2023)
   PUBMED   37903473
  REMARK    GeneRIF: YTHDC1-Modified m6A Methylation of Hsa_circ_0102678
            Promotes Keratinocyte Inflammation Induced by Cutibacterium acnes
            Biofilm through Regulating miR-146a/TRAF6 and IRAK1 Axis.
REFERENCE   6  (residues 1 to 712)
  AUTHORS   Muzio,M., Ni,J., Feng,P. and Dixit,V.M.
  TITLE     IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators
            of IL-1 signaling
  JOURNAL   Science 278 (5343), 1612-1615 (1997)
   PUBMED   9374458
REFERENCE   7  (residues 1 to 712)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   8  (residues 1 to 712)
  AUTHORS   DiDonato,J.A., Hayakawa,M., Rothwarf,D.M., Zandi,E. and Karin,M.
  TITLE     A cytokine-responsive IkappaB kinase that activates the
            transcription factor NF-kappaB
  JOURNAL   Nature 388 (6642), 548-554 (1997)
   PUBMED   9252186
REFERENCE   9  (residues 1 to 712)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   10 (residues 1 to 712)
  AUTHORS   Cao,Z., Henzel,W.J. and Gao,X.
  TITLE     IRAK: a kinase associated with the interleukin-1 receptor
  JOURNAL   Science 271 (5252), 1128-1131 (1996)
   PUBMED   8599092
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52112.2, L76191.1, BC054000.1,
            BE276817.1 and BC014963.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 5, 2005 this sequence version replaced NP_001560.1.
            
            Summary: This gene encodes the interleukin-1 receptor-associated
            kinase 1, one of two putative serine/threonine kinases that become
            associated with the interleukin-1 receptor (IL1R) upon stimulation.
            This gene is partially responsible for IL1-induced upregulation of
            the transcription factor NF-kappa B. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L76191.1, SRR14038194.2450777.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369980.8/ ENSP00000358997.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..712
                     /product="interleukin-1 receptor-associated kinase 1
                     isoform 1"
                     /EC_number="2.7.11.1"
                     /note="Pelle homolog"
                     /calculated_mol_wt=76406
     Region          17..100
                     /region_name="Death_IRAK1"
                     /note="Death domain of Interleukin 1 Receptor Associated
                     Kinase-1; cd08794"
                     /db_xref="CDD:260061"
     Site            order(19..20,22..25,58,67..68,71..77,82)
                     /site_type="other"
                     /note="putative IRAK1-IRAK4 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:260061"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC/PRKCI.
                     /evidence=ECO:0000269|PubMed:14684752; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Region          105..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51617.2)"
     Region          110..211
                     /region_name="ProST region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51617.2)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by IRAK4.
                     /evidence=ECO:0000305|PubMed:14625308; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Region          218..521
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(218..221,224,226,237,239,272,288..291,340,344..345,
                     347,357..358)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271061"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14625308; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Region          <509..>597
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          532..591
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51617.2)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Region          613..660
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51617.2)"
     Region          690..712
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51617.2)"
     CDS             1..712
                     /gene="IRAK1"
                     /gene_synonym="IRAK; pelle"
                     /coded_by="NM_001569.4:91..2229"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14740.1"
                     /db_xref="GeneID:3654"
                     /db_xref="HGNC:HGNC:6112"
                     /db_xref="MIM:300283"
ORIGIN      
        1 maggpgpgep aapgaqhfly evppwvmcrf ykvmdalepa dwcqfaaliv rdqtelrlce
       61 rsgqrtasvl wpwinrnarv adlvhilthl qllrardiit awhppaplps pgttaprpss
      121 ipapaeaeaw sprklpssas tflspafpgs qthsgpelgl vpspaslwpp ppspapsstk
      181 pgpessvsll qgarpfpfcw plceisrgth nfseelkige ggfgcvyrav mrntvyavkr
      241 lkenadlewt avkqsfltev eqlsrfrhpn ivdfagycaq ngfyclvygf lpngsledrl
      301 hcqtqacppl swpqrldill gtaraiqflh qdspslihgd ikssnvllde rltpklgdfg
      361 larfsrfags spsqssmvar tqtvrgtlay lpeeyiktgr lavdtdtfsf gvvvletlag
      421 qravkthgar tkylkdlvee eaeeagvalr stqstlqagl aadawaapia mqiykkhldp
      481 rpgpcppelg lglgqlaccc lhrrakrrpp mtqvyerlek lqavvagvpg hseaascipp
      541 spqensyvss tgrahsgaap wqplaapsga saqaaeqlqr gpnqpvesde slgglsaalr
      601 swhltpscpl dpaplreagc pqgdtagess wgsgpgsrpt aveglalgss asssseppqi
      661 iinparqkmv qklalyedga ldslqllsss slpglgleqd rqgpeesdef qs
//
LOCUS       NP_005164                999 aa            linear   PRI 27-APR-2025
DEFINITION  sarcoplasmic/endoplasmic reticulum calcium ATPase 3 isoform a [Homo
            sapiens].
ACCESSION   NP_005164
VERSION     NP_005164.2
DBSOURCE    REFSEQ: accession NM_005173.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Adle-Biassette,H., Ricci,R., Martin,A., Martini,M., Ravegnini,G.,
            Kaci,R., Gelebart,P., Poirot,B., Sandor,Z., Lehman-Che,J., Toth,E.
            and Papp,B.
  TITLE     Sarco/endoplasmic reticulum calcium ATPase 3 (SERCA3) expression in
            gastrointestinal stromal tumours
  JOURNAL   Pathology 56 (3), 343-356 (2024)
   PUBMED   38184384
  REMARK    GeneRIF: Sarco/endoplasmic reticulum calcium ATPase 3 (SERCA3)
            expression in gastrointestinal stromal tumours.
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Li,M., Shao,F., Qian,Q., Yu,W., Zhang,Z., Chen,B., Su,D., Guo,Y.,
            Phan,A.V., Song,L.S., Stephens,S.B., Sebag,J., Imai,Y., Yang,L. and
            Cao,H.
  TITLE     A putative long noncoding RNA-encoded micropeptide maintains
            cellular homeostasis in pancreatic beta cells
  JOURNAL   Mol Ther Nucleic Acids 26, 307-320 (2021)
   PUBMED   34513312
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 999)
  AUTHORS   Meneses-Morales,I., Izquierdo-Torres,E., Flores-Peredo,L.,
            Rodriguez,G., Hernandez-Oliveras,A. and Zarain-Herzberg,A.
  TITLE     Epigenetic regulation of the human ATP2A3 gene promoter in gastric
            and colon cancer cell lines
  JOURNAL   Mol Carcinog 58 (6), 887-897 (2019)
   PUBMED   30657210
  REMARK    GeneRIF: Data show that the nucleotide sequence from -280 to -135
            position is an ATP2A3 epigenetic regulatory CpG region. SERCA3 mRNA
            expression is decreased during gastric and colorectal carcinoma
            development and tumors with high SERCA3 expression are associated
            with increased overall survival. These results suggest an essential
            role for SERCA3 in the regulation of cellular identity and growth,
            through cellular Ca2+ management.
REFERENCE   5  (residues 1 to 999)
  AUTHORS   Zhang,Y., Li,F., Liu,L., Jiang,H., Hu,H., Du,X., Ge,X., Cao,J. and
            Wang,Y.
  TITLE     Salinomycin triggers endoplasmic reticulum stress through ATP2A3
            upregulation in PC-3 cells
  JOURNAL   BMC Cancer 19 (1), 381 (2019)
   PUBMED   31023247
  REMARK    GeneRIF: This study demonstrates that ATP2A3 might be one of the
            potential targets for salinomycin, which can inhibit Ca(2+) release
            and trigger ER stress to exert anti-cancer effects.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 999)
  AUTHORS   Martin,V., Bredoux,R., Corvazier,E., Van Gorp,R., Kovacs,T.,
            Gelebart,P. and Enouf,J.
  TITLE     Three novel sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) 3
            isoforms. Expression, regulation, and function of the membranes of
            the SERCA3 family
  JOURNAL   J Biol Chem 277 (27), 24442-24452 (2002)
   PUBMED   11956212
  REMARK    GeneRIF: novel sarco/endoplasmic isoforms; data suggest that the
            SERCA3 gene products have a more widespread role in cellular Ca2+
            signaling than previously appreciated
REFERENCE   7  (residues 1 to 999)
  AUTHORS   Poch,E., Leach,S., Snape,S., Cacic,T., MacLennan,D.H. and Lytton,J.
  TITLE     Functional characterization of alternatively spliced human SERCA3
            transcripts
  JOURNAL   Am J Physiol 275 (6), C1449-C1458 (1998)
   PUBMED   9843705
REFERENCE   8  (residues 1 to 999)
  AUTHORS   Dode,L., De Greef,C., Mountian,I., Attard,M., Town,M.M.,
            Casteels,R. and Wuytack,F.
  TITLE     Structure of the human sarco/endoplasmic reticulum Ca2+-ATPase 3
            gene. Promoter analysis and alternative splicing of the SERCA3
            pre-mRNA
  JOURNAL   J Biol Chem 273 (22), 13982-13994 (1998)
   PUBMED   9593748
REFERENCE   9  (residues 1 to 999)
  AUTHORS   Dode,L., Wuytack,F., Kools,P.F., Baba-Aissa,F., Raeymaekers,L.,
            Brike,F., van de Ven,W.J. and Casteels,R.
  TITLE     cDNA cloning, expression and chromosomal localization of the human
            sarco/endoplasmic reticulum Ca(2+)-ATPase 3 gene
  JOURNAL   Biochem J 318 (Pt 2) (Pt 2), 689-699 (1996)
   PUBMED   8809064
  REMARK    Erratum:[Biochem J 1996 Nov 1;319(Pt 3):1008. Brik F [corrected to
            Brike F]]
REFERENCE   10 (residues 1 to 999)
  AUTHORS   Wuytack,F., Papp,B., Verboomen,H., Raeymaekers,L., Dode,L.,
            Bobe,R., Enouf,J., Bokkala,S., Authi,K.S. and Casteels,R.
  TITLE     A sarco/endoplasmic reticulum Ca(2+)-ATPase 3-type Ca2+ pump is
            expressed in platelets, in lymphoid cells, and in mast cells
  JOURNAL   J Biol Chem 269 (2), 1410-1416 (1994)
   PUBMED   8288608
  REMARK    Erratum:[J Biol Chem 1994 Apr 29;269(17):13056]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292716.1, BC035729.1,
            AC005940.3, Z69881.1 and AA643105.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 13, 2003 this sequence version replaced NP_005164.1.
            
            Summary: This gene encodes one of the SERCA Ca(2+)-ATPases, which
            are intracellular pumps located in the sarcoplasmic or endoplasmic
            reticula of muscle cells. This enzyme catalyzes the hydrolysis of
            ATP coupled with the translocation of calcium from the cytosol to
            the sarcoplasmic reticulum lumen, and is involved in calcium
            sequestration associated with muscular excitation and contraction.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z69881.1, BC035729.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397041.8/ ENSP00000380234.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..999
                     /product="sarcoplasmic/endoplasmic reticulum calcium
                     ATPase 3 isoform a"
                     /EC_number="7.2.2.10"
                     /note="ATPase, Ca(2+)-transporting, ubiquitous;
                     sarcoplasmic/endoplasmic reticulum calcium ATPase 3; SR
                     Ca(2+)-ATPase 3; calcium pump 3; adenosine triphosphatase,
                     calcium; ATPase, Ca++ transporting, ubiquitous;
                     sarco/endoplasmic reticulum Ca2+ -ATPase;
                     calcium-translocating P-type ATPase"
                     /calculated_mol_wt=109126
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:12665801, ECO:0000269|Ref.9;
                     propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Region          5..989
                     /region_name="P-type_ATPase_SERCA"
                     /note="sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA),
                     similar to mammalian ATP2A1-3/SERCA1-3; cd02083"
                     /db_xref="CDD:319778"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64518; propagated from
                     UniProtKB/Swiss-Prot (Q93084.3)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q64518; propagated from
                     UniProtKB/Swiss-Prot (Q93084.3)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64518; propagated from
                     UniProtKB/Swiss-Prot (Q93084.3)"
     Site            49..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            254..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            296..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            order(309,796,800)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:319778"
     Site            order(351..353,442,487,489,492,494,515..517,560,562,
                     625..627,678,684,703,706)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:319778"
     Region          370..400
                     /region_name="Interaction with phospholamban 1.
                     /evidence=ECO:0000250|UniProtKB:P04191"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q64518; propagated from
                     UniProtKB/Swiss-Prot (Q93084.3)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q93084.3)"
     Site            758..777
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            order(768,771,799..800,908)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:319778"
     Region          788..808
                     /region_name="Interaction with phospholamban 2.
                     /evidence=ECO:0000250|UniProtKB:P04191"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            788..808
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            829..851
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            898..917
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            931..949
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     Site            965..985
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93084.3)"
     CDS             1..999
                     /gene="ATP2A3"
                     /gene_synonym="SERCA3"
                     /coded_by="NM_005173.4:147..3146"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45579.1"
                     /db_xref="GeneID:489"
                     /db_xref="HGNC:HGNC:813"
                     /db_xref="MIM:601929"
ORIGIN      
        1 meaahllpaa dvlrhfsvta egglspaqvt garerygpne lpseegkslw elvleqfedl
       61 lvrilllaal vsfvlawfee geetttafve plvimlilva naivgvwqer naesaiealk
      121 eyepemgkvi rsdrkgvqri rardivpgdi vevavgdkvp adlrlieiks ttlrvdqsil
      181 tgesvsvtkh teaipdprav nqdkknmlfs gtnitsgkav gvavatglht elgkirsqma
      241 avepertplq rkldefgrql shaisvicva vwvinighfa dpahggswlr gavyyfkiav
      301 alavaaipeg lpavittcla lgtrrmarkn aivrslpsve tlgctsvics dktgtlttnq
      361 msvcrmfvva eadagscllh eftisgttyt pegevrqgdq pvrcgqfdgl velaticalc
      421 ndsaldynea kgvyekvgea tetaltclve kmnvfdtdlq alsrveraga cntvikqlmr
      481 keftlefsrd rksmsvyctp trphptgqgs kmfvkgapes viercssvrv gsrtapltpt
      541 sreqilakir dwgsgsdtlr clalatrdap prkedmeldd cskfvqyetd ltfvgcvgml
      601 dpprpevaac itrcyqagir vvmitgdnkg tavaicrrlg ifgdtedvag kaytgrefdd
      661 lspeqqrqac rtarcfarve pahksriven lqsfneitam tgdgvndapa lkkaeigiam
      721 gsgtavaksa aemvlsddnf asivaaveeg raiysnmkqf irylissnvg evvcifltai
      781 lglpealipv qllwvnlvtd glpatalgfn ppdldimekl prsprealis gwlffrylai
      841 gvyvglatva aatwwfvyda egphinfyql rnflkcsedn plfagidcev fesrfpttma
      901 lsvlvtiemc nalnsvsenq sllrmppwmn pwllvavams malhflillv pplplifqvt
      961 plsgrqwvvv lqislpvill dealkylsrn hmheemsqk
//
LOCUS       NP_001356684             141 aa            linear   PRI 27-APR-2025
DEFINITION  ATP synthase F(0) complex subunit C2, mitochondrial isoform c
            precursor [Homo sapiens].
ACCESSION   NP_001356684
VERSION     NP_001356684.1
DBSOURCE    REFSEQ: accession NM_001369755.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Tebbenkamp,A.T.N., Varela,L., Choi,J., Paredes,M.I., Giani,A.M.,
            Song,J.E., Sestan-Pesa,M., Franjic,D., Sousa,A.M.M., Liu,Z.W.,
            Li,M., Bichsel,C., Koch,M., Szigeti-Buck,K., Liu,F., Li,Z.,
            Kawasawa,Y.I., Paspalas,C.D., Mineur,Y.S., Prontera,P., Merla,G.,
            Picciotto,M.R., Arnsten,A.F.T., Horvath,T.L. and Sestan,N.
  TITLE     The 7q11.23 Protein DNAJC30 Interacts with ATP Synthase and Links
            Mitochondria to Brain Development
  JOURNAL   Cell 175 (4), 1088-1104 (2018)
   PUBMED   30318146
REFERENCE   3  (residues 1 to 141)
  AUTHORS   He,J., Ford,H.C., Carroll,J., Ding,S., Fearnley,I.M. and
            Walker,J.E.
  TITLE     Persistence of the mitochondrial permeability transition in the
            absence of subunit c of human ATP synthase
  JOURNAL   Proc Natl Acad Sci U S A 114 (13), 3409-3414 (2017)
   PUBMED   28289229
  REMARK    GeneRIF: ATP5G1, ATP5G2, and ATP5G3 of the ATP synthase are not
            involved in forming the permeability transition pore.
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Fujikawa,M., Sugawara,K., Tanabe,T. and Yoshida,M.
  TITLE     Assembly of human mitochondrial ATP synthase through two separate
            intermediates, F1-c-ring and b-e-g complex
  JOURNAL   FEBS Lett 589 (19 Pt B), 2707-2712 (2015)
   PUBMED   26297831
REFERENCE   5  (residues 1 to 141)
  AUTHORS   He,M., Xu,M., Zhang,B., Liang,J., Chen,P., Lee,J.Y., Johnson,T.A.,
            Li,H., Yang,X., Dai,J., Liang,L., Gui,L., Qi,Q., Huang,J., Li,Y.,
            Adair,L.S., Aung,T., Cai,Q., Cheng,C.Y., Cho,M.C., Cho,Y.S.,
            Chu,M., Cui,B., Gao,Y.T., Go,M.J., Gu,D., Gu,W., Guo,H., Hao,Y.,
            Hong,J., Hu,Z., Hu,Y., Huang,J., Hwang,J.Y., Ikram,M.K., Jin,G.,
            Kang,D.H., Khor,C.C., Kim,B.J., Kim,H.T., Kubo,M., Lee,J., Lee,J.,
            Lee,N.R., Li,R., Li,J., Liu,J., Longe,J., Lu,W., Lu,X., Miao,X.,
            Okada,Y., Ong,R.T., Qiu,G., Seielstad,M., Sim,X., Song,H.,
            Takeuchi,F., Tanaka,T., Taylor,P.R., Wang,L., Wang,W., Wang,Y.,
            Wu,C., Wu,Y., Xiang,Y.B., Yamamoto,K., Yang,H., Liao,M., Yokota,M.,
            Young,T., Zhang,X., Kato,N., Wang,Q.K., Zheng,W., Hu,F.B., Lin,D.,
            Shen,H., Teo,Y.Y., Mo,Z., Wong,T.Y., Lin,X., Mohlke,K.L., Ning,G.,
            Tsunoda,T., Han,B.G., Shu,X.O., Tai,E.S., Wu,T. and Qi,L.
  TITLE     Meta-analysis of genome-wide association studies of adult height in
            East Asians identifies 17 novel loci
  JOURNAL   Hum Mol Genet 24 (6), 1791-1800 (2015)
   PUBMED   25429064
REFERENCE   6  (residues 1 to 141)
  AUTHORS   Houstek,J., Andersson,U., Tvrdik,P., Nedergaard,J. and Cannon,B.
  TITLE     The expression of subunit c correlates with and thus may limit the
            biosynthesis of the mitochondrial F0F1-ATPase in brown adipose
            tissue
  JOURNAL   J Biol Chem 270 (13), 7689-7694 (1995)
   PUBMED   7706317
REFERENCE   7  (residues 1 to 141)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   8  (residues 1 to 141)
  AUTHORS   Yan,W.L., Lerner,T.J., Haines,J.L. and Gusella,J.F.
  TITLE     Sequence analysis and mapping of a novel human mitochondrial ATP
            synthase subunit 9 cDNA (ATP5G3)
  JOURNAL   Genomics 24 (2), 375-377 (1994)
   PUBMED   7698763
REFERENCE   9  (residues 1 to 141)
  AUTHORS   Dyer,M.R. and Walker,J.E.
  TITLE     Sequences of members of the human gene family for the c subunit of
            mitochondrial ATP synthase
  JOURNAL   Biochem J 293 (Pt 1) (Pt 1), 51-64 (1993)
   PUBMED   8328972
REFERENCE   10 (residues 1 to 141)
  AUTHORS   Farrell,L.B. and Nagley,P.
  TITLE     Human liver cDNA clones encoding proteolipid subunit 9 of the
            mitochondrial ATPase complex
  JOURNAL   Biochem Biophys Res Commun 144 (3), 1257-1264 (1987)
   PUBMED   2883974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073594.31.
            
            Summary: This gene encodes a subunit of mitochondrial ATP synthase.
            Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an
            electrochemical gradient of protons across the inner membrane
            during oxidative phosphorylation. ATP synthase is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, comprising the proton channel.
            The catalytic portion of mitochondrial ATP synthase consists of 5
            different subunits (alpha, beta, gamma, delta, and epsilon)
            assembled with a stoichiometry of 3 alpha, 3 beta, and single
            representatives of the gamma, delta, and epsilon subunits. The
            proton channel likely has nine subunits (a, b, c, d, e, f, g, F6
            and 8). There are three separate genes which encode subunit c of
            the proton channel and they specify precursors with different
            import sequences but identical mature proteins. The protein encoded
            by this gene is one of three precursors of subunit c. This gene has
            multiple pseudogenes. [provided by RefSeq, Jan 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG217012.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..141
                     /product="ATP synthase F(0) complex subunit C2,
                     mitochondrial isoform c precursor"
                     /note="ATP synthase, H+ transporting, mitochondrial F0
                     complex, subunit C2 (subunit 9); ATP synthase
                     lipid-binding protein, mitochondrial; ATP synthase
                     proteolipid P2; ATPase protein 9; ATPase subunit C; ATP
                     synthase c subunit; ATP synthase proton-transporting
                     mitochondrial F(0) complex subunit C2; ATP synthase, H+
                     transporting, mitochondrial Fo complex subunit C2 (subunit
                     9); ATP synthase F(0) complex subunit C2, mitochondrial;
                     dicyclohexylcarbodiimide (DCCD)-reactive proteolipid
                     subunit"
                     /calculated_mol_wt=7608
     transit_peptide 1..66
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q06055.1)"
                     /calculated_mol_wt=7047
     mat_peptide     67..141
                     /product="ATP synthase F(0) complex subunit C2,
                     mitochondrial. /id=PRO_0000002562"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
                     /calculated_mol_wt=7608
     Region          67..141
                     /region_name="ATP9"
                     /note="ATP synthase F0 subunit 9; Provisional; MTH00222"
                     /db_xref="CDD:164765"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
     Site            109
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000269|PubMed:30530489; propagated from
                     UniProtKB/Swiss-Prot (Q06055.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06055.1)"
     Site            124
                     /site_type="other"
                     /note="Reversibly protonated during proton transport.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q06055.1)"
     CDS             1..141
                     /gene="ATP5MC2"
                     /gene_synonym="ATP5A; ATP5G2"
                     /coded_by="NM_001369755.1:121..546"
                     /note="isoform c precursor is encoded by transcript
                     variant 6"
                     /db_xref="CCDS:CCDS81694.1"
                     /db_xref="GeneID:517"
                     /db_xref="HGNC:HGNC:842"
                     /db_xref="MIM:603193"
ORIGIN      
        1 mfacskfvst pslvkstsql lsrplsavvl krpeiltdes lsslavscpl tslvssrsfq
       61 tsaisrdidt aakfigagaa tvgvagsgag igtvfgslii gyarnpslkq qlfsyailgf
      121 alseamglfc lmvaflilfa m
//
LOCUS       NP_073739               1430 aa            linear   PRI 27-APR-2025
DEFINITION  3'-5' RNA helicase YTHDC2 isoform 1 [Homo sapiens].
ACCESSION   NP_073739
VERSION     NP_073739.3
DBSOURCE    REFSEQ: accession NM_022828.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1430)
  AUTHORS   Tian,S., Faheem,M., Satti,H.S., Xiao,J., Zhang,F., Khan,T.N. and
            Liu,C.
  TITLE     A homozygous missense variant in YTHDC2 induces azoospermia in two
            siblings
  JOURNAL   Mol Genet Genomics 299 (1), 84 (2024)
   PUBMED   39223386
  REMARK    GeneRIF: A homozygous missense variant in YTHDC2 induces
            azoospermia in two siblings.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1430)
  AUTHORS   Yang,Z., Verghese,M., Yang,S., Shah,P. and He,Y.Y.
  TITLE     The m6A reader YTHDC2 regulates UVB-induced DNA damage repair and
            histone modification
  JOURNAL   Photochem Photobiol 100 (4), 1031-1040 (2024)
   PUBMED   38190286
  REMARK    GeneRIF: The m[6]A reader YTHDC2 regulates UVB-induced DNA damage
            repair and histone modification.
REFERENCE   3  (residues 1 to 1430)
  AUTHORS   Sun,Y., Liu,Y., Wang,P., Chang,L. and Huang,J.
  TITLE     The m6A Reader YTHDC2 Suppresses Lung Adenocarcinoma Tumorigenesis
            by Destabilizing MRPL12
  JOURNAL   Mol Biotechnol 66 (5), 1051-1061 (2024)
   PUBMED   38129673
  REMARK    GeneRIF: The m6A Reader YTHDC2 Suppresses Lung Adenocarcinoma
            Tumorigenesis by Destabilizing MRPL12.
REFERENCE   4  (residues 1 to 1430)
  AUTHORS   Zhou,G. and Wang,S.
  TITLE     YTHDC2 Retards Cell Proliferation and Triggers Apoptosis in
            Papillary Thyroid Cancer by Regulating CYLD-Mediated Inactivation
            of Akt Signaling
  JOURNAL   Appl Biochem Biotechnol 196 (1), 588-603 (2024)
   PUBMED   37162682
  REMARK    GeneRIF: YTHDC2 Retards Cell Proliferation and Triggers Apoptosis
            in Papillary Thyroid Cancer by Regulating CYLD-Mediated
            Inactivation of Akt Signaling.
REFERENCE   5  (residues 1 to 1430)
  AUTHORS   Sun,T., Xu,Y., Xiang,Y., Ou,J., Soderblom,E.J. and Diao,Y.
  TITLE     Crosstalk between RNA m6A and DNA methylation regulates
            transposable element chromatin activation and cell fate in human
            pluripotent stem cells
  JOURNAL   Nat Genet 55 (8), 1324-1335 (2023)
   PUBMED   37474847
  REMARK    GeneRIF: Crosstalk between RNA m[6]A and DNA methylation regulates
            transposable element chromatin activation and cell fate in human
            pluripotent stem cells.
REFERENCE   6  (residues 1 to 1430)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 1430)
  AUTHORS   Li,S., Wang,L., Berman,M., Kong,Y.Y. and Dorf,M.E.
  TITLE     Mapping a dynamic innate immunity protein interaction network
            regulating type I interferon production
  JOURNAL   Immunity 35 (3), 426-440 (2011)
   PUBMED   21903422
  REMARK    Erratum:[Immunity. 2011 Oct 28;35(4):647-8]
REFERENCE   8  (residues 1 to 1430)
  AUTHORS   Morohashi,K., Sahara,H., Watashi,K., Iwabata,K., Sunoki,T.,
            Kuramochi,K., Takakusagi,K., Miyashita,H., Sato,N., Tanabe,A.,
            Shimotohno,K., Kobayashi,S., Sakaguchi,K. and Sugawara,F.
  TITLE     Cyclosporin A associated helicase-like protein facilitates the
            association of hepatitis C virus RNA polymerase with its cellular
            cyclophilin B
  JOURNAL   PLoS One 6 (4), e18285 (2011)
   PUBMED   21559518
  REMARK    GeneRIF: CAHL is a CsA associated helicase-like protein, which
            would form trimer complex with cyclophilin B and NS5B of HCV.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1430)
  AUTHORS   Bhatnagar,P., Purvis,S., Barron-Casella,E., DeBaun,M.R.,
            Casella,J.F., Arking,D.E. and Keefer,J.R.
  TITLE     Genome-wide association study identifies genetic variants
            influencing F-cell levels in sickle-cell patients
  JOURNAL   J Hum Genet 56 (4), 316-323 (2011)
   PUBMED   21326311
REFERENCE   10 (residues 1 to 1430)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK096486.1, BC137285.1 and
            AC010389.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 24, 2009 this sequence version replaced NP_073739.2.
            
            Summary: This gene encodes a member of the DEAH (Asp-Glu-Ala-His)
            subfamily of proteins, part of the DEAD (Asp-Glu-Ala-Asp) box
            family of RNA helicases. The encoded protein binds to
            N6-methyladenosine, a common modified RNA nucleotide that is
            enriched in the stop codons and 3' UTRs of eukaryotic messenger
            RNAs. Binding of proteins to this modified nucleotide may regulate
            mRNA translation and stability. This gene may be associated with
            susceptibility to pancreatic cancer in human patients, and
            knockdown of this gene resulted in reduced proliferation in a human
            liver cancer cell line. [provided by RefSeq, Sep 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.118755.1,
                                           SRR1660807.231200.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000161863.9/ ENSP00000161863.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1430
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..1430
                     /product="3'-5' RNA helicase YTHDC2 isoform 1"
                     /EC_number="3.6.4.13"
                     /note="probable ATP-dependent RNA helicase YTHDC2;
                     CsA-associated helicase-like protein; 3'-5' RNA helicase
                     YTHDC2; YTH domain containing 2"
                     /calculated_mol_wt=160118
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Region          46..104
                     /region_name="R3H_DEXH_helicase"
                     /note="R3H domain of a group of proteins which also
                     contain a DEXH-box helicase domain, and may function as
                     ATP-dependent DNA or RNA helicases. The name of the R3H
                     domain comes from the characteristic spacing of the most
                     conserved arginine and histidine...; cd06007"
                     /db_xref="CDD:100077"
     Site            order(75,79)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100077"
     Region          188..>948
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
     Region          193..368
                     /region_name="DEXHc_YTHDC2"
                     /note="DEXH-box helicase domain of YTH domain containing
                     2; cd17987"
                     /db_xref="CDD:350745"
     Site            order(193,218..224,259,316..317)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350745"
     Region          316..319
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Region          505..537
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          506..538
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Region          539..571
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Region          539..564
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          971..1066
                     /region_name="OB_NTP_bind"
                     /note="Oligonucleotide/oligosaccharide-binding (OB)-fold;
                     pfam07717"
                     /db_xref="CDD:400182"
     Site            1089
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Site            1090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B2RR83; propagated from
                     UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Site            1092
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Region          1164..1288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Site            1202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Site            1263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B2RR83; propagated from
                     UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Site            1267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B2RR83; propagated from
                     UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Site            1281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H6S0.2)"
     Region          1289..1418
                     /region_name="YTH"
                     /note="YTH (YT521-B homology) domains are RNA-binding
                     domains that belong to the PUA superfamily; cd21134"
                     /db_xref="CDD:410979"
     CDS             1..1430
                     /gene="YTHDC2"
                     /gene_synonym="CAHL; hYTHDC2"
                     /coded_by="NM_022828.5:203..4495"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4113.1"
                     /db_xref="GeneID:64848"
                     /db_xref="HGNC:HGNC:24721"
                     /db_xref="MIM:616530"
ORIGIN      
        1 msrpssvspr qpapgggggg gpspcgpggg grakglkdir ideevkiavn ialerfrygd
       61 qremefpssl tsterafihr lsqslglvsk skgkganryl tvkkkdgset ahammtcnlt
      121 hntkhavrsl iqrfpvtnke rtellpkter gnvfaveaen remsktsgrl nngipqipvk
      181 rgesefdsfr qslpvfekqe eivkiikenk vvlivgetgs gkttqipqfl lddcfkngip
      241 crifctqprr laaiavaerv aaerrerigq tigyqirles rvspktlltf ctngvllrtl
      301 magdstlstv thvivdevhe rdrfsdfllt klrdllqkhp tlklilssaa ldvnlfiryf
      361 gscpviyiqg rpfevkemfl edilrttgyt nkemlkykke kqqeekqqtt ltewysaqen
      421 sfkpesqrqr tvlnvtdeyd llddggdavf sqltekdvnc lepwlikemd aclsdiwlhk
      481 didafaqvfh liltenvsvd yrhsetsata lmvaagrgfa sqveqlismg anvhskasng
      541 wmaldwakhf gqteivdlle sysatlefgn ldesslvqtn gsdlsaedre llkayhhsfd
      601 dekvdldlim hllynichsc dagavliflp gydeivglrd rilfddkrfa dsthryqvfm
      661 lhsnmqtsdq kkvlknppag vrkiilstni aetsitvndv vfvidsgkvk eksfdalnfv
      721 tmlkmvwisk asaiqrkgra grcrpgicfr lfsrlrfqnm lefqtpellr mplqelclht
      781 kllapvncpi adflmkapep ppalivrnav qmlktidamd twedltelgy hladlpveph
      841 lgkmvlcavv lkcldpilti actlayrdpf vlptqasqkr aamlcrkrft agafsdhmal
      901 lrafqawqka rsdgwerafc eknflsqatm eiiigmrtql lgqlrasgfv rargggdird
      961 vntnsenwav vkaalvagmy pnlvhvdren lvltgpkekk vrfhpasvls qpqykkippa
     1021 ngqaaaikal ptdwliydem trahrianir ccsavtpvti lvfcgparla snalqepssf
     1081 rvdgipndss dsemedktta nlaalkldew lhftlepeaa slllqlrqkw hslflrrmra
     1141 pskpwsqvde atiraiiavl steeqsaglq qpsgigqrpr pmsseelpla sswrsnnsrk
     1201 ssadtefsde cttaervlmk spspalhppq kykdrgilhp krgtedrsdq sslkstdsss
     1261 ypspcaspsp pssgkgsksp sprpnmpvry fimkssnlrn leisqqkgiw sttpsnerkl
     1321 nrafwessiv ylvfsvqgsg hfqgfsrmss eigreksqdw gsaglggvfk vewirkeslp
     1381 fqfahhllnp wndnkkvqis rdgqeleplv geqllqlwer lplgeknttd
//
LOCUS       NP_001357329             549 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 266 isoform 1 [Homo sapiens].
ACCESSION   NP_001357329
VERSION     NP_001357329.1
DBSOURCE    REFSEQ: accession NM_001370400.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Abrink,M., Aveskogh,M. and Hellman,L.
  TITLE     Isolation of cDNA clones for 42 different Kruppel-related zinc
            finger proteins expressed in the human monoblast cell line U-937
  JOURNAL   DNA Cell Biol 14 (2), 125-136 (1995)
   PUBMED   7865130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011451.6.
            
            Summary: This gene encodes a protein containing many tandem
            zinc-finger motifs. Zinc fingers are protein or nucleic
            acid-binding domains, and may be involved in a variety of
            functions, including regulation of transcription. This gene is
            located in a cluster of similar genes encoding zinc finger proteins
            on chromosome 19. Alternative splicing results in multiple
            transcript variants for this gene. [provided by RefSeq, Sep 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: ERR3218373.30269.1, SRR7346977.1828825.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..549
                     /product="zinc finger protein 266 isoform 1"
                     /note="zinc finger protein 1; zinc finger protein HZF1"
                     /calculated_mol_wt=61985
     Region          <1..28
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          132..150
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          158..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..549
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,303,305,307,309..310,313..314,317)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(387,389,391,393..394,397..398,401,415,417,421..422,
                     425..426,429,443,445,447,449..450,453..454,457)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(471,473,475,477..478,481..482,485,499,501,505..506,
                     509..510,513,527,529,531,533..534,537..538,541)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          522..542
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14584.2)"
     CDS             1..549
                     /gene="ZNF266"
                     /gene_synonym="HZF1"
                     /coded_by="NM_001370400.1:1497..3146"
                     /note="isoform 1 is encoded by transcript variant 29"
                     /db_xref="CCDS:CCDS12213.1"
                     /db_xref="GeneID:10781"
                     /db_xref="HGNC:HGNC:13059"
                     /db_xref="MIM:604751"
ORIGIN      
        1 mlenyknlat vgyqlfkpsl iswleqeesr tvqrgdfqas ewkvqlktke lalqqdvlge
       61 ptssgiqmig shnggevsdv kqcgdvsseh sclkthvrtq nsentfecyl ygvdfltlhk
      121 ktstgeqrsv fsqcgkafsl npdvvcqrtc tgekafdcsd sgksfinhsh lqghlrthng
      181 eslhewkecg rgfihstdla vriqthrsek pykckecgkg frysaylnih mgthtgdnpy
      241 eckecgkaft rscqltqhrk thtgekpykc kdcgraftvs sclsqhmkih vgekpyecke
      301 cgiaftrssq ltehlkthta kdpfeckicg ksfrnsscls dhfrihtgik pykckdcgka
      361 ftqnsdltkh arthsgerpy eckecgkafa rssrlsehtr thtgekpfec vkcgkafais
      421 snlsghlrih tgekpfecle cgkafthsss lnnhmrthsa kkpftcmecg kafkfptcvn
      481 lhmrihtgek pykckqcgks fsysnsfqlh erthtgekpy eckecgkafs ssssfrnher
      541 rhaderlsa
//
LOCUS       NP_001546               1336 aa            linear   PRI 27-APR-2025
DEFINITION  immunoglobulin superfamily member 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001546
VERSION     NP_001546.2
DBSOURCE    REFSEQ: accession NM_001555.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1336)
  AUTHORS   Zhang,C., Chen,L., Chen,X., Xie,R., Wang,F., Chen,T., Wang,X.,
            Sun,H., Zhang,D. and Wu,H.
  TITLE     [Clinical characteristics and genetic analysis of four patients
            with central hypothyroidism due to IGSF1 gene variants]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 40 (3), 322-327 (2023)
   PUBMED   36854408
  REMARK    GeneRIF: [Clinical characteristics and genetic analysis of four
            patients with central hypothyroidism due to IGSF1 gene variants].
REFERENCE   2  (residues 1 to 1336)
  AUTHORS   Costas Eimil,J. and Sanchez-Sobrino,P.
  TITLE     IGSF1 mutation as a cause of isolated central hypothyroidism
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 69 (10), 913-914 (2022)
   PUBMED   36464600
  REMARK    GeneRIF: IGSF1 mutation as a cause of isolated central
            hypothyroidism.
REFERENCE   3  (residues 1 to 1336)
  AUTHORS   Fourneaux,R., Reynaud,R., Mougel,G., Castets,S., Bretones,P.,
            Dauriat,B., Edouard,T., Raverot,G., Barlier,A., Brue,T.,
            Castinetti,F. and Saveanu,A.
  TITLE     IGSF1 mutations are the most frequent genetic aetiology of
            thyrotropin deficiency
  JOURNAL   Eur J Endocrinol 187 (6), 787-795 (2022)
   PUBMED   36201163
  REMARK    GeneRIF: IGSF1 mutations are the most frequent genetic aetiology of
            thyrotropin deficiency.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1336)
  AUTHORS   Elizabeth,M.S.M., Hokken-Koelega,A., Visser,J.A., Joustra,S.D. and
            de Graaff,L.C.G.
  TITLE     Case Report: A Detailed Phenotypic Description of Patients and
            Relatives with Combined Central Hypothyroidism and Growth Hormone
            Deficiency Carrying IGSF1 Mutations
  JOURNAL   Genes (Basel) 13 (4), 623 (2022)
   PUBMED   35456429
  REMARK    GeneRIF: Case Report: A Detailed Phenotypic Description of Patients
            and Relatives with Combined Central Hypothyroidism and Growth
            Hormone Deficiency Carrying IGSF1 Mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1336)
  AUTHORS   Fourneaux,R., Castets,S., Godefroy,A., Grelet,M., Abeillon-du
            Payrat,J., Saveanu,A., Castinetti,F. and Reynaud,R.
  TITLE     Congenital Central Hypothyroidism Caused by a Novel IGSF1 Variant
            Identified in a French Family
  JOURNAL   Horm Res Paediatr 95 (3), 296-303 (2022)
   PUBMED   35350016
  REMARK    GeneRIF: Congenital Central Hypothyroidism Caused by a Novel IGSF1
            Variant Identified in a French Family.
REFERENCE   6  (residues 1 to 1336)
  AUTHORS   Tanaka,S., Tatsumi,K., Okubo,K., Itoh,K., Kawamoto,S., Matsubara,K.
            and Amino,N.
  TITLE     Expression profile of active genes in the human pituitary gland
  JOURNAL   J Mol Endocrinol 28 (1), 33-44 (2002)
   PUBMED   11854097
REFERENCE   7  (residues 1 to 1336)
  AUTHORS   Gui,Y. and Murphy,L.J.
  TITLE     Insulin-like growth factor (IGF)-binding protein-3 (IGFBP-3) binds
            to fibronectin (FN): demonstration of IGF-I/IGFBP-3/fn ternary
            complexes in human plasma
  JOURNAL   J Clin Endocrinol Metab 86 (5), 2104-2110 (2001)
   PUBMED   11344214
REFERENCE   8  (residues 1 to 1336)
  AUTHORS   Chapman,S.C. and Woodruff,T.K.
  TITLE     Modulation of activin signal transduction by inhibin B and
            inhibin-binding protein (INhBP)
  JOURNAL   Mol Endocrinol 15 (4), 668-679 (2001)
   PUBMED   11266516
REFERENCE   9  (residues 1 to 1336)
  AUTHORS   Frattini,A., Faranda,S., Redolfi,E., Allavena,P. and Vezzoni,P.
  TITLE     Identification and genomic organization of a gene coding for a new
            member of the cell adhesion molecule family mapping to Xq25
  JOURNAL   Gene 214 (1-2), 1-6 (1998)
   PUBMED   9729118
REFERENCE   10 (residues 1 to 1336)
  AUTHORS   Mazzarella,R., Pengue,G., Jones,J., Jones,C. and Schlessinger,D.
  TITLE     Cloning and expression of an immunoglobulin superfamily gene
            (IGSF1) in Xq25
  JOURNAL   Genomics 48 (2), 157-162 (1998)
   PUBMED   9521868
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590806.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 17, 2004 this sequence version replaced NP_001546.1.
            
            Summary: This gene encodes a member of the immunoglobulin-like
            domain-containing superfamily. Proteins in this superfamily contain
            varying numbers of immunoglobulin-like domains and are thought to
            participate in the regulation of interactions between cells.
            Multiple transcript variants encoding different isoforms have been
            found for this gene.[provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (1) uses an alternate in-frame
            splice site in a 3' exon compared to variant 3. The resulting
            protein (isoform 1) is shorter compared to isoform 3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063884.1, SRR1803615.4201.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361420.8/ ENSP00000355010.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1336
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..1336
                     /product="immunoglobulin superfamily member 1 isoform 1
                     precursor"
                     /note="inhibin-binding protein; pituitary gland-specific
                     factor 2; immunoglobulin-like domain-containing protein 1"
                     /calculated_mol_wt=145852
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3103
     mat_peptide     29..1336
                     /product="Immunoglobulin superfamily member 1.
                     /id=PRO_0000318512"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6C5.3)"
                     /calculated_mol_wt=145852
     Region          37..123
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          54..58
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          67..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          89..93
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          103..108
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          118..121
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          131..221
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          148..152
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          160..164
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          182..186
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          196..201
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          214..217
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          227..316
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          244..248
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          256..260
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..283
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          293..298
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          309..312
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          325..414
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            338
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          339..343
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          351..355
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            374
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          375..379
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          389..394
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          407..410
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          420..504
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          437..441
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          449..453
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          467..471
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          481..486
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          499..502
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            519..539
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Site            560..580
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          591..679
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            607
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          608..612
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          621..625
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          643..647
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          657..662
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          672..675
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          685..772
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          699..703
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          711..715
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          733..737
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          747..752
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            747
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          765..768
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          778..868
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          795..799
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            798
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          807..811
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          832..836
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          846..851
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            846
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          861..864
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          874..960
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          891..895
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          903..907
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          925..929
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          939..944
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            939
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          957..960
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          970..1060
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            986
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          987..991
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          999..1003
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1021..1025
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            1027
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          1035..1040
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1053..1056
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1066..1156
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            1082
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          1083..1087
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1095..1099
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1117..1121
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1131..1136
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            1147
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          1149..1152
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1162..1248
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1179..1183
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1191..1195
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1209..1213
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1223..1228
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            1223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N6C5.3)"
     Region          1241..1244
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1308..1336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6C5.3)"
     CDS             1..1336
                     /gene="IGSF1"
                     /gene_synonym="CHTE; IGCD1; IGDC1; INHBP; p120; PGSF2"
                     /coded_by="NM_001555.5:161..4171"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS14629.1"
                     /db_xref="GeneID:3547"
                     /db_xref="HGNC:HGNC:5948"
                     /db_xref="MIM:300137"
ORIGIN      
        1 mtldrpgega tmlktftvll fcirmslgmt sivmdpqpel wiesnypqap wenitlwcrs
       61 psrisskfll lkdktqmtwi rpshktfqvs fligaltesn aglyrccywk etgwskpskv
      121 leleapgqlp kpifwiqaet palpgcnvni lchgwlqdlv fmlfkegyae pvdyqvptgt
      181 maifsidnlt pedegvyicr thiqmlptlw sepsnplklv vaglypkptl tahpgpimap
      241 geslnlrcqg piygmtfalm rvedleksfy hkktiknean fffqslkiqd tghylcfyyd
      301 asyrgsllsd vlkiwvtdtf pktwllarps avvqmgqnvs lrcrgpvdgv glalykkged
      361 kplqfldats iddntsffln nvtysdtgiy schylltwkt sirmpshntv elmvvdkppk
      421 pslsawpstv fklgkaitlq crvshpvlef sleweeretf qkfsvngdfi isnvdgkgtg
      481 tyscsyrvet hpniwshrse plklmgpagy ltwnyvlnea irlslimqlv alllvvlwir
      541 wkcrrlrire awllgtaqgv tmlfivtall ccglcngvli eeteivmptp kpelwaetnf
      601 plapwknltl wcrspsgstk efvllkdgtg wiatrpaseq vraafplgal tqshtgsyhc
      661 hsweemavse psealelvgt dilpkpvisa sptirgqelq lrckgwlagm gfalykegeq
      721 epvqqlgavg reafftiqrm edkdegnysc rthtekrpfk wsepseplel vikemypkpf
      781 fktwaspvvt pgarvtfncs tphqhmsfil ykdgseiass drswaspgas aahfliisvg
      841 igdggnyscr yydfsiwsep sdpvelvvte fypkptllaq pgpvvfpgks vilrcqgtfq
      901 gmrfallqeg ahvplqfrsv sgnsadfllh tvgaedsgny sciyyettms nrgsylsmpl
      961 miwvtdtfpk pwlfaepssv vpmgqnvtlw crgpvhgvgy ilhkegeats mqlwgstsnd
     1021 gafpitnisg tsmgrysccy hpdwtssiki qpsntlellv tgllpkpsll aqpgpmvapg
     1081 enmtlqcqge lpdstfvllk egaqepleqq rpsgyradfw mpavrgedsg iyscvyylds
     1141 tpfaasnhsd sleiwvtdkp pkpslsawps tmfklgkdit lqcrgplpgv efvlehdgee
     1201 apqqfsedgd fvinnvegkg ignyscsyrl qaypdiwsep sdplelvgaa gpvaqectvg
     1261 nivrsslivv vvvalgvvla iewkkwprlr trgsetdgrd qtialeecnq egepgtpans
     1321 psstsqrisv elpvpi
//
LOCUS       NP_001094896             451 aa            linear   PRI 27-APR-2025
DEFINITION  D-ribitol-5-phosphate cytidylyltransferase isoform a [Homo
            sapiens].
ACCESSION   NP_001094896 XP_001126777 XP_001131763 XP_001132057
VERSION     NP_001094896.1
DBSOURCE    REFSEQ: accession NM_001101426.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Hu,Q., Gu,Y., Chen,S., Tian,Y. and Yang,S.
  TITLE     Hsa_circ_0079480 promotes tumor progression in acute myeloid
            leukemia via miR-654-3p/HDGF axis
  JOURNAL   Aging (Albany NY) 13 (1), 1120-1131 (2020)
   PUBMED   33290265
  REMARK    GeneRIF: Hsa_circ_0079480 promotes tumor progression in acute
            myeloid leukemia via miR-654-3p/HDGF axis.
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Song,D., Fu,X., Ge,L., Chang,X., Wei,C., Liu,J., Yang,H., Qu,S.,
            Bao,X., Toda,T., Wu,X. and Xiong,H.
  TITLE     A splice site mutation c.1251G>A of ISPD gene is a common cause of
            congenital muscular dystrophy in Chinese patients
  JOURNAL   Clin Genet 97 (5), 789-790 (2020)
   PUBMED   31909476
  REMARK    GeneRIF: A splice site mutation c.1251G>A of ISPD gene is a common
            cause of congenital muscular dystrophy in Chinese patients.
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Sheikh,M.O., Halmo,S.M. and Wells,L.
  TITLE     Recent advancements in understanding mammalian O-mannosylation
  JOURNAL   Glycobiology 27 (9), 806-819 (2017)
   PUBMED   28810660
  REMARK    Review article
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Gerin,I., Ury,B., Breloy,I., Bouchet-Seraphin,C., Bolsee,J.,
            Halbout,M., Graff,J., Vertommen,D., Muccioli,G.G., Seta,N.,
            Cuisset,J.M., Dabaj,I., Quijano-Roy,S., Grahn,A., Van
            Schaftingen,E. and Bommer,G.T.
  TITLE     ISPD produces CDP-ribitol used by FKTN and FKRP to transfer ribitol
            phosphate onto alpha-dystroglycan
  JOURNAL   Nat Commun 7, 11534 (2016)
   PUBMED   27194101
  REMARK    GeneRIF: ISPD and FKTN are essential for the incorporation of
            ribitol into alpha-dystroglycan.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Takata,R., Matsuda,K., Sugimura,J., Obara,W., Fujioka,T.,
            Okihara,K., Takaha,N., Miki,T., Ashida,S., Inoue,K., Tanikawa,C.,
            Shuin,T., Sasaki,S., Kojima,Y., Kohri,K., Kubo,M., Yamaguchi,M.,
            Ohnishi,Y. and Nakamura,Y.
  TITLE     Impact of four loci on serum tamsulosin hydrochloride concentration
  JOURNAL   J Hum Genet 58 (1), 21-26 (2013)
   PUBMED   23151678
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Vuillaumier-Barrot,S., Bouchet-Seraphin,C., Chelbi,M., Devisme,L.,
            Quentin,S., Gazal,S., Laquerriere,A., Fallet-Bianco,C., Loget,P.,
            Odent,S., Carles,D., Bazin,A., Aziza,J., Clemenson,A., Guimiot,F.,
            Bonniere,M., Monnot,S., Bole-Feysot,C., Bernard,J.P., Loeuillet,L.,
            Gonzales,M., Socha,K., Grandchamp,B., Attie-Bitach,T.,
            Encha-Razavi,F. and Seta,N.
  TITLE     Identification of mutations in TMEM5 and ISPD as a cause of severe
            cobblestone lissencephaly
  JOURNAL   Am J Hum Genet 91 (6), 1135-1143 (2012)
   PUBMED   23217329
  REMARK    GeneRIF: TMEM5 mutations were frequently associated with gonadal
            dysgenesis and neural tube defects, and ISPD mutations were
            frequently associated with brain vascular anomalies.
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Roscioli,T., Kamsteeg,E.J., Buysse,K., Maystadt,I., van
            Reeuwijk,J., van den Elzen,C., van Beusekom,E., Riemersma,M.,
            Pfundt,R., Vissers,L.E., Schraders,M., Altunoglu,U., Buckley,M.F.,
            Brunner,H.G., Grisart,B., Zhou,H., Veltman,J.A., Gilissen,C.,
            Mancini,G.M., Delree,P., Willemsen,M.A., Ramadza,D.P., Chitayat,D.,
            Bennett,C., Sheridan,E., Peeters,E.A., Tan-Sindhunata,G.M., de
            Die-Smulders,C.E., Devriendt,K., Kayserili,H., El-Hashash,O.A.,
            Stemple,D.L., Lefeber,D.J., Lin,Y.Y. and van Bokhoven,H.
  TITLE     Mutations in ISPD cause Walker-Warburg syndrome and defective
            glycosylation of alpha-dystroglycan
  JOURNAL   Nat Genet 44 (5), 581-585 (2012)
   PUBMED   22522421
  REMARK    GeneRIF: Mutations in ISPD cause Walker-Warburg syndrome and
            defective glycosylation of alpha-dystroglycan.
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Willer,T., Lee,H., Lommel,M., Yoshida-Moriguchi,T., de
            Bernabe,D.B., Venzke,D., Cirak,S., Schachter,H., Vajsar,J.,
            Voit,T., Muntoni,F., Loder,A.S., Dobyns,W.B., Winder,T.L.,
            Strahl,S., Mathews,K.D., Nelson,S.F., Moore,S.A. and Campbell,K.P.
  TITLE     ISPD loss-of-function mutations disrupt dystroglycan
            O-mannosylation and cause Walker-Warburg syndrome
  JOURNAL   Nat Genet 44 (5), 575-580 (2012)
   PUBMED   22522420
  REMARK    GeneRIF: ISPD loss-of-function mutations disrupt dystroglycan
            O-mannosylation and cause Walker-Warburg syndrome.
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Wylam,M.E., Samsel,R.W., Umans,J.G., Mitchell,R.W., Leff,A.R. and
            Schumacker,P.T.
  TITLE     Endotoxin in vivo impairs endothelium-dependent relaxation of
            canine arteries in vitro
  JOURNAL   Am Rev Respir Dis 142 (6 Pt 1), 1263-1267 (1990)
   PUBMED   2252242
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079155.7, AC004741.2,
            AC073629.6 and AC006035.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Sep 22, 2007 this sequence version replaced
            XP_001131763.1, XP_001126777.1, XP_001132057.1.
            
            Summary: This gene encodes a 2-C-methyl-D-erythritol 4-phosphate
            cytidylyltransferase-like protein. Mutations in this gene are the
            cause of Walker-Warburg syndrome. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longest isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments. The full extent of this transcript
            is supported by and orthologous data in mouse (NM_178629.5).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.77161.1,
                                           SRR1660807.174457.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000407010.7/ ENSP00000385478.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.2"
     Protein         1..451
                     /product="D-ribitol-5-phosphate cytidylyltransferase
                     isoform a"
                     /EC_number="2.7.7.40"
                     /note="4-diphosphocytidyl-2C-methyl-D-erythritol synthase
                     homolog; notch1-induced protein; 2-C-methyl-D-erythritol
                     4-phosphate cytidylyltransferase-like protein; testicular
                     tissue protein Li 97; D-ribitol-5-phosphate
                     cytidylyltransferase; isoprenoid synthase domain
                     containing"
                     /calculated_mol_wt=49742
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4D126.2)"
     Region          47..273
                     /region_name="CDP-ME_synthetase"
                     /note="CDP-ME synthetase is involved in
                     mevalonate-independent isoprenoid production; cd02516"
                     /db_xref="CDD:133009"
     Site            order(52,54..59,66,123..126,129,156..158,263)
                     /site_type="active"
                     /note="substrate binding site [active]"
                     /db_xref="CDD:133009"
     Site            59
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:Q46893; propagated from
                     UniProtKB/Swiss-Prot (A4D126.2)"
     Site            66
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:Q46893; propagated from
                     UniProtKB/Swiss-Prot (A4D126.2)"
     Site            order(159,178,186,188,206..211,238..239,241..242,245,
                     251..254,258..259)
                     /site_type="active"
                     /note="dimer interface [active]"
                     /db_xref="CDD:133009"
     Site            205
                     /site_type="other"
                     /note="Positions substrate for the nucleophilic attack.
                     /evidence=ECO:0000250|UniProtKB:Q46893; propagated from
                     UniProtKB/Swiss-Prot (A4D126.2)"
     Site            263
                     /site_type="other"
                     /note="Positions substrate for the nucleophilic attack.
                     /evidence=ECO:0000250|UniProtKB:Q46893; propagated from
                     UniProtKB/Swiss-Prot (A4D126.2)"
     Region          283..451
                     /region_name="ISPD_C"
                     /note="D-ribitol-5-phosphate cytidylyltransferase
                     C-terminal domain; pfam18706"
                     /db_xref="CDD:465843"
     CDS             1..451
                     /gene="CRPPA"
                     /gene_synonym="hISPD; ISPD; LGMDR20; MDDGA7; MDDGC7; Nip"
                     /coded_by="NM_001101426.4:217..1572"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:729920"
                     /db_xref="HGNC:HGNC:37276"
                     /db_xref="MIM:614631"
ORIGIN      
        1 meagppgsar paepgpclsg qrgadhtasa slqsvagtep grhpqavaav lpaggcgerm
       61 gvptpkqfcp ilerplisyt lqalervcwi kdivvavtge nmevmksiiq kyqhkrislv
      121 eagvtrhrsi fnglkalaed qinsklskpe vviihdavrp fveegvllkv vtaakehgaa
      181 gairplvstv vspsadgcld yslerarhra sempqaflfd viyeayqqcs dydlefgtec
      241 lqlalkycct kaklvegspd lwkvtykrdl yaaesiiker isqeicvvmd teednkhvgh
      301 lleevlksel nhvkvtseal ghagrhlqqi ildqcynfvc vnvttsdfqe tqkllsmlee
      361 sslcilypvv vvsvhfldfk lvppsqkmen lmqirefake vkernillyg llisypqddq
      421 klqeslrqga iiiasliker nsgligqlli a
//
LOCUS       NP_001357271             422 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 42 [Homo sapiens].
ACCESSION   NP_001357271 XP_016876400
VERSION     NP_001357271.1
DBSOURCE    REFSEQ: accession NM_001370342.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Patel,N., Smith,L.L., Faqeih,E., Mohamed,J., Gupta,V.A. and
            Alkuraya,F.S.
  TITLE     ZBTB42 mutation defines a novel lethal congenital contracture
            syndrome (LCCS6)
  JOURNAL   Hum Mol Genet 23 (24), 6584-6593 (2014)
   PUBMED   25055871
  REMARK    GeneRIF: ZBTB42 mutation defines a novel lethal congenital
            contracture syndrome.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Devaney,S.A., Mate,S.E., Devaney,J.M. and Hoffman,E.P.
  TITLE     Characterization of the ZBTB42 gene in humans and mice
  JOURNAL   Hum Genet 129 (4), 433-441 (2011)
   PUBMED   21193930
  REMARK    GeneRIF: Data show that ZBTB42 protein is expressed in human
            skeletal muscle and a murine cell line C2C12 myotubes.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590327.3.
            
            On May 7, 2019 this sequence version replaced XP_016876400.1.
            
            Summary: The protein encoded by this gene is a member of the C2H2
            zinc finger protein family. This protein is predicted to have a pox
            virus and zinc finger (POZ) domain at the N-terminus and four zinc
            finger domains at the C-terminus. In human and mouse, the protein
            localizes to the nuclei of skeletal muscle cells. Knockdown of this
            gene in zebrafish results in abnormal skeletal muscle development
            and myofibrillar disorganization. A novel homozygous variant of the
            human gene has been associated with lethal congenital contracture
            syndrome, an autosomal recessive disorder that results in muscle
            wasting. [provided by RefSeq, Mar 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..422
                     /product="zinc finger and BTB domain-containing protein
                     42"
                     /calculated_mol_wt=46360
     Region          1..129
                     /region_name="BTB_POZ_ZBTB42"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 42 (ZBTB42); cd18956"
                     /db_xref="CDD:349737"
     Region          121..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RXF5.2)"
     Region          166..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RXF5.2)"
     Region          207..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RXF5.2)"
     Region          <292..>405
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          296..316
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(296,299,312,316)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          336..356
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(336,339,352,356)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(341,343,345,347..348,351..352,355,369,371,375..376,
                     379..380,383,397,399,401,403..404,407..408)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          349..371
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          364..384
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          392..410
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..422
                     /gene="ZBTB42"
                     /gene_synonym="LCCS6; ZNF925"
                     /coded_by="NM_001370342.1:165..1433"
                     /db_xref="CCDS:CCDS45174.1"
                     /db_xref="GeneID:100128927"
                     /db_xref="HGNC:HGNC:32550"
                     /db_xref="MIM:613915"
ORIGIN      
        1 mefpehggrl lgrlrqqrel gflcdctvlv gdarfpahra vlaacsvyfh lfyrdrpags
       61 rdtvrlngdi vtapafgrll dfmyegrldl rslpvedvla aasylhmydi vkvckgrlqe
      121 kdrsldpgnp apgaepaqpp cpwpvwtadl cpaarkaklp pfgvkaalpp rasgpppcqv
      181 peesdqaldl slksgprqer vhppcvlqtp lcsqrqpgaq plvkderdsl seqeessssr
      241 sphsppkppp vpaakglvvg lqplplsgeg srelelgagr lasedelgpg gplcicplcs
      301 klfpsshvlq lhlsahfrer dstrarlspd gvaptcplcg ktfsctytlk rherthsgek
      361 pytcvqcgks fqyshnlsrh tvvhtrekph acrwcerrft qsgdlyrhvr kfhcglvksl
      421 lv
//
LOCUS       NP_002955                 93 aa            linear   PRI 27-APR-2025
DEFINITION  protein S100-A8 isoform d [Homo sapiens].
ACCESSION   NP_002955
VERSION     NP_002955.2
DBSOURCE    REFSEQ: accession NM_002964.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Zhang,Y., Zhao,Y., Zhang,J., Gao,Y., Gao,X., Li,S., Chang,C. and
            Yang,G.
  TITLE     Proteomics of plasma-derived extracellular vesicles reveals S100A8
            as a novel biomarker for Alzheimer's disease: A preliminary study
  JOURNAL   J Proteomics 308, 105279 (2024)
   PUBMED   39159863
  REMARK    GeneRIF: Proteomics of plasma-derived extracellular vesicles
            reveals S100A8 as a novel biomarker for Alzheimer's disease: A
            preliminary study.
REFERENCE   2  (residues 1 to 93)
  AUTHORS   De Luca,G., Goette,N.P., Lev,P.R., Baroni Pietto,M.C., Marin
            Oyarzun,C.P., Castro Rios,M.A., Moiraghi,B., Sackmann,F.,
            Kamiya,L.J., Verri,V., Caula,V., Fernandez,V., Vicente,A., Pose
            Cabarcos,J., Caruso,V., Camacho,M.F., Larripa,I.B., Khoury,M.,
            Marta,R.F., Glembotsky,A.C. and Heller,P.G.
  TITLE     Elevated levels of damage-associated molecular patterns HMGB1 and
            S100A8/A9 coupled with toll-like receptor-triggered monocyte
            activation are associated with inflammation in patients with
            myelofibrosis
  JOURNAL   Front Immunol 15, 1365015 (2024)
   PUBMED   39391311
  REMARK    GeneRIF: Elevated levels of damage-associated molecular patterns
            HMGB1 and S100A8/A9 coupled with toll-like receptor-triggered
            monocyte activation are associated with inflammation in patients
            with myelofibrosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Ding,L., Lu,L., Zheng,S., Zhang,Z., Huang,X., Ma,R., Zhang,M.,
            Xu,Z., Chen,M., Guo,Z., Zhu,S., Gong,J., Mao,H., Zhang,W. and Xu,P.
  TITLE     Usp14 deficiency removes alpha-synuclein by regulating S100A8/A9 in
            Parkinson's disease
  JOURNAL   Cell Mol Life Sci 81 (1), 232 (2024)
   PUBMED   38780644
  REMARK    GeneRIF: Usp14 deficiency removes alpha-synuclein by regulating
            S100A8/A9 in Parkinson's disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Munoz-Grajales,C., Barraclough,M.L., Diaz-Martinez,J.P., Su,J.,
            Bingham,K., Kakvan,M., Kretzmann,R.P., Tartaglia,M.C., Ruttan,L.,
            Choi,M.Y., Appenzeller,S., Marzouk,S., Bonilla,D., Katz,P.,
            Beaton,D., Green,R., Gladman,D.D., Wither,J. and Touma,Z.
  TITLE     Serum S100A8/A9 and MMP-9 levels are elevated in systemic lupus
            erythematosus patients with cognitive impairment
  JOURNAL   Front Immunol 14, 1326751 (2024)
   PUBMED   38332909
  REMARK    GeneRIF: Serum S100A8/A9 and MMP-9 levels are elevated in systemic
            lupus erythematosus patients with cognitive impairment.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 93)
  AUTHORS   Cho,S.B., Kim,I.K., Yeo,C.D. and Lee,S.H.
  TITLE     Association Between Clinicopathological Parameters and S100A8/A9
            Expression According to Smoking History in Patients With Non-small
            Cell Lung Cancer
  JOURNAL   In Vivo 38 (1), 474-481 (2024)
   PUBMED   38148054
  REMARK    GeneRIF: Association Between Clinicopathological Parameters and
            S100A8/A9 Expression According to Smoking History in Patients With
            Non-small Cell Lung Cancer.
REFERENCE   6  (residues 1 to 93)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   7  (residues 1 to 93)
  AUTHORS   Lemarchand,P., Vaglio,M., Mauel,J. and Markert,M.
  TITLE     Translocation of a small cytosolic calcium-binding protein (MRP-8)
            to plasma membrane correlates with human neutrophil activation
  JOURNAL   J Biol Chem 267 (27), 19379-19382 (1992)
   PUBMED   1326551
REFERENCE   8  (residues 1 to 93)
  AUTHORS   Schafer,T., Sachse,G.E. and Gassen,H.G.
  TITLE     The calcium-binding protein MRP-8 is produced by human pulmonary
            tumor cells
  JOURNAL   Biol Chem Hoppe Seyler 372 (1), 1-4 (1991)
   PUBMED   2039599
REFERENCE   9  (residues 1 to 93)
  AUTHORS   Dorin,J.R., Emslie,E. and van Heyningen,V.
  TITLE     Related calcium-binding proteins map to the same subregion of
            chromosome 1q and to an extended region of synteny on mouse
            chromosome 3
  JOURNAL   Genomics 8 (3), 420-426 (1990)
   PUBMED   2149559
REFERENCE   10 (residues 1 to 93)
  AUTHORS   Wilkinson,M.M., Busuttil,A., Hayward,C., Brock,D.J., Dorin,J.R. and
            Van Heyningen,V.
  TITLE     Expression pattern of two related cystic fibrosis-associated
            calcium-binding proteins in normal and abnormal tissues
  JOURNAL   J Cell Sci 91 (Pt 2), 221-230 (1988)
   PUBMED   3267695
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK291328.1 and X06234.1.
            
            On Jun 26, 2002 this sequence version replaced NP_002955.1.
            
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21. This protein may function
            in the inhibition of casein kinase and as a cytokine. Altered
            expression of this protein is associated with the disease cystic
            fibrosis. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (4) uses an alternate splice
            junction compared to variant 1. The resulting isoform (d) is
            shorter at the N-terminus compared to isoform a. Variants 4 and 5
            both encode the same isoform (d).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X06234.1, BP225716.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368733.4/ ENSP00000357722.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..93
                     /product="protein S100-A8 isoform d"
                     /note="protein S100-A8; calgranulin A; cystic fibrosis
                     antigen; calprotectin L1L subunit; urinary stone protein
                     band A; leukocyte L1 complex light chain; migration
                     inhibitory factor-related protein 8"
                     /calculated_mol_wt=10703
     Region          3..86
                     /region_name="calgranulins"
                     /note="Calgranulins: S-100 domain found in proteins
                     belonging to the Calgranulin subgroup of the S100 family
                     of EF-hand calcium-modulated proteins, including S100A8,
                     S100A9, and S100A12 . Note that the S-100 hierarchy, to
                     which this Calgranulin group belongs; cd05030"
                     /db_xref="CDD:240156"
     Site            order(3,9,11,17,41,43,68,76,78)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240156"
     Site            order(20,25,28,33,59,61,63,65,70)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:240156"
     CDS             1..93
                     /gene="S100A8"
                     /gene_synonym="60B8AG; CAGA; CFAG; CGLA; CP-10; L1Ag;
                     MA387; MIF; MRP8; NIF; P8; S100-A8"
                     /coded_by="NM_002964.5:56..337"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS1038.1"
                     /db_xref="GeneID:6279"
                     /db_xref="HGNC:HGNC:10498"
                     /db_xref="MIM:123885"
ORIGIN      
        1 mltelekaln siidvyhkys likgnfhavy rddlkkllet ecpqyirkkg advwfkeldi
       61 ntdgavnfqe flilvikmgv aahkkshees hke
//
LOCUS       NP_110385                916 aa            linear   PRI 27-APR-2025
DEFINITION  oxysterol-binding protein 2 isoform a [Homo sapiens].
ACCESSION   NP_110385
VERSION     NP_110385.1
DBSOURCE    REFSEQ: accession NM_030758.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 916)
  AUTHORS   Wu,Q., Li,X., Long,M., Xie,X. and Liu,Q.
  TITLE     Integrated analysis of histone lysine lactylation (Kla)-specific
            genes suggests that NR6A1, OSBP2 and UNC119B are novel therapeutic
            targets for hepatocellular carcinoma
  JOURNAL   Sci Rep 13 (1), 18642 (2023)
   PUBMED   37903971
  REMARK    GeneRIF: Integrated analysis of histone lysine lactylation
            (Kla)-specific genes suggests that NR6A1, OSBP2 and UNC119B are
            novel therapeutic targets for hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 916)
  AUTHORS   Zhong,W., Cao,X., Pan,G., Niu,Q., Feng,X., Xu,M., Li,M., Huang,Y.,
            Yi,Q. and Yan,D.
  TITLE     ORP4L is a prerequisite for the induction of T-cell leukemogenesis
            associated with human T-cell leukemia virus 1
  JOURNAL   Blood 139 (7), 1052-1065 (2022)
   PUBMED   34797912
  REMARK    GeneRIF: ORP4L is a prerequisite for the induction of T-cell
            leukemogenesis associated with human T-cell leukemia virus 1.
REFERENCE   3  (residues 1 to 916)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 916)
  AUTHORS   Cao,X., Chen,J., Li,D., Xie,P., Xu,M., Lin,W., Li,S., Pan,G.,
            Tang,Y., Xu,J., Olkkonen,V.M., Yan,D. and Zhong,W.
  TITLE     ORP4L couples IP3 to ITPR1 in control of endoplasmic reticulum
            calcium release
  JOURNAL   FASEB J 33 (12), 13852-13865 (2019)
   PUBMED   31648575
  REMARK    GeneRIF: ORP4L is a cofactor of ITPR1.
REFERENCE   5  (residues 1 to 916)
  AUTHORS   Wang,C., JeBailey,L. and Ridgway,N.D.
  TITLE     Oxysterol-binding-protein (OSBP)-related protein 4 binds
            25-hydroxycholesterol and interacts with vimentin intermediate
            filaments
  JOURNAL   Biochem J 361 (Pt 3), 461-472 (2002)
   PUBMED   11802775
REFERENCE   6  (residues 1 to 916)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   7  (residues 1 to 916)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
REFERENCE   8  (residues 1 to 916)
  AUTHORS   Moreira,E.F., Jaworski,C., Li,A. and Rodriguez,I.R.
  TITLE     Molecular and biochemical characterization of a novel
            oxysterol-binding protein (OSBP2) highly expressed in retina
  JOURNAL   J Biol Chem 276 (21), 18570-18578 (2001)
   PUBMED   11278871
REFERENCE   9  (residues 1 to 916)
  AUTHORS   Silva,N.H., Pimenta,G., Pulcheri,W.A., Fournier,M.V., Spector,N.
            and da Costa Carvalho,M.G.
  TITLE     Detection of messenger RNA in leukocytes or plasma of patients with
            chronic myeloid leukemia
  JOURNAL   Oncol Rep 8 (3), 693-696 (2001)
   PUBMED   11295104
REFERENCE   10 (residues 1 to 916)
  AUTHORS   Fournier,M.V., Guimaraes da Costa,F., Paschoal,M.E., Ronco,L.V.,
            Carvalho,M.G. and Pardee,A.B.
  TITLE     Identification of a gene encoding a human oxysterol-binding
            protein-homologue: a potential general molecular marker for blood
            dissemination of solid tumors
  JOURNAL   Cancer Res 59 (15), 3748-3753 (1999)
   PUBMED   10446991
  REMARK    Erratum:[Cancer Res 2001 Jan 15;61(2):792. Guimaraes, FC [corrected
            to Guimaraes da Costa, F]]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF323731.1 and AB051451.2.
            
            Summary: The protein encoded by this gene contains a pleckstrin
            homology (PH) domain and an oxysterol-binding region. It binds
            oxysterols such as 7-ketocholesterol and may inhibit their
            cytotoxicity. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB051451.2, AF288741.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000332585.11/ ENSP00000332576.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..916
                     /product="oxysterol-binding protein 2 isoform a"
                     /note="oxysterol binding protein-like 1; OSBP-related
                     protein 4; oxysterol-binding protein-related protein 4"
                     /calculated_mol_wt=101135
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969R2.2)"
     Region          34..121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969R2.2)"
     Region          139..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969R2.2)"
     Region          185..280
                     /region_name="PH_OSBP_ORP4"
                     /note="Human Oxysterol binding protein and OSBP-related
                     protein 4 Pleckstrin homology (PH) domain; cd13284"
                     /db_xref="CDD:270101"
     Region          282..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969R2.2)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5QNQ6; propagated from
                     UniProtKB/Swiss-Prot (Q969R2.2)"
     Region          417..448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969R2.2)"
     Region          522..905
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     Site            763
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q969R2.2)"
     Region          813..842
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969R2.2)"
     CDS             1..916
                     /gene="OSBP2"
                     /gene_synonym="HLM; ORP-4; ORP4; OSBPL1; OSBPL4"
                     /coded_by="NM_030758.4:37..2787"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43002.1"
                     /db_xref="GeneID:23762"
                     /db_xref="HGNC:HGNC:8504"
                     /db_xref="MIM:606729"
ORIGIN      
        1 mgkaaapsrg ggcggrsrgl sslftvvpcl schtaapgms astsgsgpep kpqpqpvpep
       61 ergplseqvs eavseavprs epvsettsep epgagqpsel lqgsrpgses ssgvgagpft
      121 kaaseplsra vgsatflrpe sgslpalkpl pllrpgqakt plgvpmsgtg ttssaplall
      181 pldsfegwll kwtnylkgyq rrwfvlgngl lsyyrnqgem ahtcrgtinl stahidteds
      241 cgilltsgar syhlkassev drqqwitale lakakavrvm nthsddsgdd deattpadks
      301 elhhtlknls lklddlstcn dliakhgaal qrslteldgl kipsesgekl kvvneratlf
      361 ritsnamina crdflelaei hsrkwqralq yeqeqrvhle etieqlakqh nslerafhsa
      421 pgrpanpsks fiegslltpk gedseededt eyfdamedst sfitviteak edsrkaegst
      481 gtssvdwssa dnvldgaslv pkgsskvkrr vripnkpnys lnlwsimknc igrelsripm
      541 pvnfneplsm lqrltedley hhlldkavhc tssveqmclv aafsvssyst tvhriakpfn
      601 pmlgetfeld rlddmglrsl ceqvshhpps aahyvfskhg wslwqeitis skfrgkyisi
      661 mplgaihlef qasgnhyvwr kststvhnii vgklwidqsg dieivnhktn drcqlkflpy
      721 syfskeaark vtgvvsdsqg kahyvlsgsw deqmecskvm hsspsspssd gkqktvyqtl
      781 sakllwkkyp lpenaenmyy fselaltlne heegvaptds rlrpdqrlme kgrwdeante
      841 kqrleekqrl srrrrleacg pgsscsseee keadaytplw fekrldpltg emacvykggy
      901 weakekqdwh mcpnif
//
LOCUS       NP_660279                401 aa            linear   PRI 27-APR-2025
DEFINITION  UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7 [Homo
            sapiens].
ACCESSION   NP_660279
VERSION     NP_660279.1
DBSOURCE    REFSEQ: accession NM_145236.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Wang,X., Wang,Y., Chen,X., He,Y., Zhou,X., Jiao,S., Zhu,Z., Wu,C.
            and Bao,J.
  TITLE     Identification of glycogene-based prognostic signature and
            validation of B3GNT7 as a potential biomarker and therapeutic
            target in breast cancer
  JOURNAL   J Cancer Res Clin Oncol 149 (19), 16957-16969 (2023)
   PUBMED   37740763
  REMARK    GeneRIF: Identification of glycogene-based prognostic signature and
            validation of B3GNT7 as a potential biomarker and therapeutic
            target in breast cancer.
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Carroll,D.J., Burns,M.W.N., Mottram,L., Propheter,D.C., Boucher,A.,
            Lessen,G.M., Kumar,A., Malaker,S.A., Xing,C., Hooper,L.V., Yrlid,U.
            and Kohler,J.J.
  TITLE     Interleukin-22 regulates B3GNT7 expression to induce fucosylation
            of glycoproteins in intestinal epithelial cells
  JOURNAL   J Biol Chem 298 (2), 101463 (2022)
   PUBMED   34864058
  REMARK    GeneRIF: Interleukin-22 regulates B3GNT7 expression to induce
            fucosylation of glycoproteins in intestinal epithelial cells.
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Lu,C.H., Wu,W.Y., Lai,Y.J., Yang,C.M. and Yu,L.C.
  TITLE     Suppression of B3GNT7 gene expression in colon adenocarcinoma and
            its potential effect in the metastasis of colon cancer cells
  JOURNAL   Glycobiology 24 (4), 359-367 (2014)
   PUBMED   24418929
  REMARK    GeneRIF: The nude mice xenograft model demonstrated that ectopic
            expression of the B3GNT7 gene in colon cancer cells diminished the
            migration capability and the liver-metastasis potential,
            respectively, of colon cancer cells.
REFERENCE   5  (residues 1 to 401)
  AUTHORS   den Hoed,M., Eijgelsheim,M., Esko,T., Brundel,B.J., Peal,D.S.,
            Evans,D.M., Nolte,I.M., Segre,A.V., Holm,H., Handsaker,R.E.,
            Westra,H.J., Johnson,T., Isaacs,A., Yang,J., Lundby,A., Zhao,J.H.,
            Kim,Y.J., Go,M.J., Almgren,P., Bochud,M., Boucher,G.,
            Cornelis,M.C., Gudbjartsson,D., Hadley,D., van der Harst,P.,
            Hayward,C., den Heijer,M., Igl,W., Jackson,A.U., Kutalik,Z.,
            Luan,J., Kemp,J.P., Kristiansson,K., Ladenvall,C., Lorentzon,M.,
            Montasser,M.E., Njajou,O.T., O'Reilly,P.F., Padmanabhan,S., St
            Pourcain,B., Rankinen,T., Salo,P., Tanaka,T., Timpson,N.J.,
            Vitart,V., Waite,L., Wheeler,W., Zhang,W., Draisma,H.H.,
            Feitosa,M.F., Kerr,K.F., Lind,P.A., Mihailov,E., Onland-Moret,N.C.,
            Song,C., Weedon,M.N., Xie,W., Yengo,L., Absher,D., Albert,C.M.,
            Alonso,A., Arking,D.E., de Bakker,P.I., Balkau,B., Barlassina,C.,
            Benaglio,P., Bis,J.C., Bouatia-Naji,N., Brage,S., Chanock,S.J.,
            Chines,P.S., Chung,M., Darbar,D., Dina,C., Dorr,M., Elliott,P.,
            Felix,S.B., Fischer,K., Fuchsberger,C., de Geus,E.J., Goyette,P.,
            Gudnason,V., Harris,T.B., Hartikainen,A.L., Havulinna,A.S.,
            Heckbert,S.R., Hicks,A.A., Hofman,A., Holewijn,S.,
            Hoogstra-Berends,F., Hottenga,J.J., Jensen,M.K., Johansson,A.,
            Junttila,J., Kaab,S., Kanon,B., Ketkar,S., Khaw,K.T., Knowles,J.W.,
            Kooner,A.S., Kors,J.A., Kumari,M., Milani,L., Laiho,P.,
            Lakatta,E.G., Langenberg,C., Leusink,M., Liu,Y., Luben,R.N.,
            Lunetta,K.L., Lynch,S.N., Markus,M.R., Marques-Vidal,P., Mateo
            Leach,I., McArdle,W.L., McCarroll,S.A., Medland,S.E., Miller,K.A.,
            Montgomery,G.W., Morrison,A.C., Muller-Nurasyid,M., Navarro,P.,
            Nelis,M., O'Connell,J.R., O'Donnell,C.J., Ong,K.K., Newman,A.B.,
            Peters,A., Polasek,O., Pouta,A., Pramstaller,P.P., Psaty,B.M.,
            Rao,D.C., Ring,S.M., Rossin,E.J., Rudan,D., Sanna,S., Scott,R.A.,
            Sehmi,J.S., Sharp,S., Shin,J.T., Singleton,A.B., Smith,A.V.,
            Soranzo,N., Spector,T.D., Stewart,C., Stringham,H.M., Tarasov,K.V.,
            Uitterlinden,A.G., Vandenput,L., Hwang,S.J., Whitfield,J.B.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilson,J.F., Witteman,J.C.,
            Wong,A., Wong,Q., Jamshidi,Y., Zitting,P., Boer,J.M., Boomsma,D.I.,
            Borecki,I.B., van Duijn,C.M., Ekelund,U., Forouhi,N.G., Froguel,P.,
            Hingorani,A., Ingelsson,E., Kivimaki,M., Kronmal,R.A., Kuh,D.,
            Lind,L., Martin,N.G., Oostra,B.A., Pedersen,N.L., Quertermous,T.,
            Rotter,J.I., van der Schouw,Y.T., Verschuren,W.M., Walker,M.,
            Albanes,D., Arnar,D.O., Assimes,T.L., Bandinelli,S., Boehnke,M., de
            Boer,R.A., Bouchard,C., Caulfield,W.L., Chambers,J.C., Curhan,G.,
            Cusi,D., Eriksson,J., Ferrucci,L., van Gilst,W.H., Glorioso,N., de
            Graaf,J., Groop,L., Gyllensten,U., Hsueh,W.C., Hu,F.B.,
            Huikuri,H.V., Hunter,D.J., Iribarren,C., Isomaa,B., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kiemeney,L.A., van der Klauw,M.M.,
            Kooner,J.S., Kraft,P., Iacoviello,L., Lehtimaki,T., Lokki,M.L.,
            Mitchell,B.D., Navis,G., Nieminen,M.S., Ohlsson,C., Poulter,N.R.,
            Qi,L., Raitakari,O.T., Rimm,E.B., Rioux,J.D., Rizzi,F., Rudan,I.,
            Salomaa,V., Sever,P.S., Shields,D.C., Shuldiner,A.R., Sinisalo,J.,
            Stanton,A.V., Stolk,R.P., Strachan,D.P., Tardif,J.C.,
            Thorsteinsdottir,U., Tuomilehto,J., van Veldhuisen,D.J.,
            Virtamo,J., Viikari,J., Vollenweider,P., Waeber,G., Widen,E.,
            Cho,Y.S., Olsen,J.V., Visscher,P.M., Willer,C., Franke,L.,
            Erdmann,J., Thompson,J.R., Pfeufer,A., Sotoodehnia,N.,
            Newton-Cheh,C., Ellinor,P.T., Stricker,B.H., Metspalu,A.,
            Perola,M., Beckmann,J.S., Smith,G.D., Stefansson,K., Wareham,N.J.,
            Munroe,P.B., Sibon,O.C., Milan,D.J., Snieder,H., Samani,N.J. and
            Loos,R.J.
  CONSRTM   Global BPgen Consortium; CARDIoGRAM Consortium; PR GWAS Consortium;
            QRS GWAS Consortium; QT-IGC Consortium; CHARGE-AF Consortium
  TITLE     Identification of heart rate-associated loci and their effects on
            cardiac conduction and rhythm disorders
  JOURNAL   Nat Genet 45 (6), 621-631 (2013)
   PUBMED   23583979
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Kitayama,K., Hayashida,Y., Nishida,K. and Akama,T.O.
  TITLE     Enzymes responsible for synthesis of corneal keratan sulfate
            glycosaminoglycans
  JOURNAL   J Biol Chem 282 (41), 30085-30096 (2007)
   PUBMED   17690104
  REMARK    GeneRIF: sulfated keratan sulfate is produced by beta3GNT7,
            beta4GalT4, CGn6ST, and KSG6ST
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Seko,A. and Yamashita,K.
  TITLE     beta1,3-N-Acetylglucosaminyltransferase-7 (beta3Gn-T7) acts
            efficiently on keratan sulfate-related glycans
  JOURNAL   FEBS Lett 556 (1-3), 216-220 (2004)
   PUBMED   14706853
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Kataoka,K. and Huh,N.H.
  TITLE     A novel beta1,3-N-acetylglucosaminyltransferase involved in
            invasion of cancer cells as assayed in vitro
  JOURNAL   Biochem Biophys Res Commun 294 (4), 843-848 (2002)
   PUBMED   12061784
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF502430.1, AK126207.1, AC017104.8 and AK000770.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB224859.1, AK126207.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287590.6/ ENSP00000287590.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..401
                     /product="UDP-GlcNAc:betaGal
                     beta-1,3-N-acetylglucosaminyltransferase 7"
                     /note="beta 1,3-N-acetylglucosaminyltransferase 7; BGnT-7;
                     beta3Gn-T7; beta-1,3-Gn-T7"
                     /calculated_mol_wt=45856
     Site            7..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFL0.1)"
     Region          35..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFL0.1)"
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFL0.1)"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFL0.1)"
     Region          148..342
                     /region_name="Galactosyl_T"
                     /note="Galactosyltransferase; cl21608"
                     /db_xref="CDD:473923"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFL0.1)"
     Site            391
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFL0.1)"
     CDS             1..401
                     /gene="B3GNT7"
                     /gene_synonym="beta3GnT7"
                     /coded_by="NM_145236.3:95..1300"
                     /db_xref="CCDS:CCDS46540.1"
                     /db_xref="GeneID:93010"
                     /db_xref="HGNC:HGNC:18811"
                     /db_xref="MIM:615313"
ORIGIN      
        1 mslwkktvyr slclalallv avtvfqrslt pgqflqeppp ptlepqkaqk pngqlvnpnn
       61 fwknpkdvaa ptpmasqgpq awdvtttncs aninlthqpw fqvlepqfrq flfyrhcryf
      121 pmllnhpekc rgdvyllvvv ksvitqhdrr eairqtwgre rqsagggrga vrtlfllgta
      181 skqeerthyq qllayedrly gdilqwgfld tffnltlkei hflkwldiyc phvpfifkgd
      241 ddvfvnptnl lefladrqpq enlfvgdvlq harpirrkdn kyyipgalyg kasyppyagg
      301 ggflmagsla rrlhhacdtl elypiddvfl gmclevlgvq ptahegfktf gisrnrnsrm
      361 nkepcffram lvvhkllppe llamwglvhs nltcsrklqv l
//
LOCUS       NP_001355550            1770 aa            linear   ROD 27-APR-2025
DEFINITION  ADAMTS-like protein 1 isoform 3 precursor [Mus musculus].
ACCESSION   NP_001355550
VERSION     NP_001355550.1
DBSOURCE    REFSEQ: accession NM_001368621.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1770)
  AUTHORS   Naba,A., Clauser,K.R., Mani,D.R., Carr,S.A. and Hynes,R.O.
  TITLE     Quantitative proteomic profiling of the extracellular matrix of
            pancreatic islets during the angiogenic switch and insulinoma
            progression
  JOURNAL   Sci Rep 7, 40495 (2017)
   PUBMED   28071719
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1770)
  AUTHORS   Naba,A., Clauser,K.R., Hoersch,S., Liu,H., Carr,S.A. and Hynes,R.O.
  TITLE     The matrisome: in silico definition and in vivo characterization by
            proteomics of normal and tumor extracellular matrices
  JOURNAL   Mol Cell Proteomics 11 (4), M111.014647 (2012)
   PUBMED   22159717
REFERENCE   3  (residues 1 to 1770)
  AUTHORS   Du,J., Takeuchi,H., Leonhard-Melief,C., Shroyer,K.R., Dlugosz,M.,
            Haltiwanger,R.S. and Holdener,B.C.
  TITLE     O-fucosylation of thrombospondin type 1 repeats restricts
            epithelial to mesenchymal transition (EMT) and maintains epiblast
            pluripotency during mouse gastrulation
  JOURNAL   Dev Biol 346 (1), 25-38 (2010)
   PUBMED   20637190
REFERENCE   4  (residues 1 to 1770)
  AUTHORS   Tang,T., Li,L., Tang,J., Li,Y., Lin,W.Y., Martin,F., Grant,D.,
            Solloway,M., Parker,L., Ye,W., Forrest,W., Ghilardi,N., Oravecz,T.,
            Platt,K.A., Rice,D.S., Hansen,G.M., Abuin,A., Eberhart,D.E.,
            Godowski,P., Holt,K.H., Peterson,A., Zambrowicz,B.P. and de
            Sauvage,F.J.
  TITLE     A mouse knockout library for secreted and transmembrane proteins
  JOURNAL   Nat Biotechnol 28 (7), 749-755 (2010)
   PUBMED   20562862
REFERENCE   5  (residues 1 to 1770)
  AUTHORS   Hall,N.G., Klenotic,P., Anand-Apte,B. and Apte,S.S.
  TITLE     ADAMTSL-3/punctin-2, a novel glycoprotein in extracellular matrix
            related to the ADAMTS family of metalloproteases
  JOURNAL   Matrix Biol 22 (6), 501-510 (2003)
   PUBMED   14667842
REFERENCE   6  (residues 1 to 1770)
  AUTHORS   Hirohata,S., Wang,L.W., Miyagi,M., Yan,L., Seldin,M.F., Keene,D.R.,
            Crabb,J.W. and Apte,S.S.
  TITLE     Punctin, a novel ADAMTS-like molecule, ADAMTSL-1, in extracellular
            matrix
  JOURNAL   J Biol Chem 277 (14), 12182-12189 (2002)
   PUBMED   11805097
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL772130.15, AL807242.7 and AL824705.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849374,
                              SAMN00849375 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1770
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 40.32 cM"
     Protein         1..1770
                     /product="ADAMTS-like protein 1 isoform 3 precursor"
                     /note="ADAMTS-like protein 1; punctin-1"
                     /calculated_mol_wt=191770
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3034
     Region          36..82
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          87..185
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Region          204..296
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8BLI0.2)"
     Region          301..359
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            310
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q8BLI0.2)"
     Region          380..437
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            391
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q8BLI0.2)"
     Region          440..492
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            451
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q8BLI0.2)"
     Region          531..583
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          611..666
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          670..728
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          732..788
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          792..849
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          895..949
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          895..899
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          908..912
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          930..934
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          944..949
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          991..1016
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BLI0.2)"
     Region          1139..1162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BLI0.2)"
     Region          <1197..1257
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1198..1202
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1211..1215
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1233..1237
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1247..1252
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1285..1365
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          1403..1494
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1422..1426
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1435..1439
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1457..1464
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1474..1479
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1487..1490
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1557..1615
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1618..1674
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1678..1733
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1738..1767
                     /region_name="PLAC"
                     /note="PLAC (protease and lacunin) domain; pfam08686"
                     /db_xref="CDD:462560"
     CDS             1..1770
                     /gene="Adamtsl1"
                     /gene_synonym="5930437A14Rik; 6720426B09Rik; ADAMTSL-1"
                     /coded_by="NM_001368621.1:84..5396"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:77739"
                     /db_xref="MGI:MGI:1924989"
ORIGIN      
        1 meccrraapg tpllvlafll lssrtarsee dreglwdawg pwsecsrtcg ggasyslrrc
       61 lsskscegrn iryrtcsnvd cppeagdfra qqcsahndvk yhgqlyewlp vsndpdnpcs
      121 lkcqakgtsl vvelapkvld gtrcytesld mcisglcqiv gcdhqlgstv kedncgvcng
      181 dgstcrlvrg qyksqlsask sddtvvaipy gsrhirlvlk gpdhlyletk tlqgtkgens
      241 lsstgiflvd nstvdfqklp dkeilrmtgp ltadfiikih dlgpadstvq fifyqpiihr
      301 wretdffpcs atcgggyqlt saecydlrsn rvvadqychy ypenvkpkpk lqecnldpcp
      361 asdgykqimp ydlyhplprw eatpwtacss scgggiqsra vscveediqg hvtsveewkc
      421 mytpkmpvvq pcnifdcpkw laqewspctv tcgqglryrv vlcidhrgmh tggcsaktkp
      481 hikeeciipt pcykpreklp ieaklpwfkq aqeleegaav seepsfipea wsactvtcgv
      541 gtqvriircq vllpfsqsva dlpadecegp kpasqracya gpcngetpef npdngdgllg
      601 glqdldelyd weyegftkcs escgggvqea vvsclnkqtr eladenlcvt srrppqllks
      661 cnldpcparw eigkwspcsl tcgvglqtrd vvcshllsre mnevvvlade lchhpkpstv
      721 qacnrfncpp awypaqwqlc srtcgggiqk rdvlckqrma dgsflelpet fcsaskptsh
      781 qgckkddcps ewllsewsec svscgegtqt rsaicqrvlk tgvstvvnst lcpplpfsss
      841 irpcmlatca rpgrpstkhs phiaaarniy iqtrrqrklh fvvggfayll pkttvvlrcp
      901 trrfrkplit wekdgqhsis sahvtvapfg ylkihrlkps dagiytcsag pareqfvikl
      961 iggnrklvar plslwseeee alqvrktnpk ealqthkhqn gifsngskae krgltadpgn
     1021 ryddivsrll eqggwpgell aswevqdsae rnasseedpn aeqallhlpf tmvaeqkrld
     1081 dilrnlsqqp eelrdlyskh lvaqlaqdif rshlenqdll pkpseqrfpp mavpahkhvs
     1141 gfssslrsss geagggsrrp hrkpailrki saaqqlsase vvthlgqtva lasgtlsvll
     1201 hceavgnprp tihwtrngea vqfsdrillq pddslqilap veadvgfytc natnalgyds
     1261 vsiavtlagk plvktsrmtv lntekptvtv diggtvrtvr gvnvtincqv agvpeaevtw
     1321 frnksklgss hhlhegsshh lhegsllltd vsfsdqglys craanlhgeq testqllild
     1381 ppqvptqled iralllatgp nlpsvlmspl gtqlvldpgn sallgcpikg hptpnitwfq
     1441 ngqpiatapg lthhiwgagq ilrvanlsgg pqgefsclaq neagtllqka slviqdywws
     1501 vdrlatcsas cgnrgihqpr lrcllnttev dpehctgkpr pavqpvacnr rdcpsrwmvt
     1561 swsactrscg ggvqtrrvtc qklkasgist pvsndmcsql akrpvdtqac nqqlcvewaf
     1621 sswgqcngpc igprlavqhr qvfcqtrdgi tlpseqcsal prpvstqncw seacsvhwrv
     1681 slwtlctatc gnygfqsrrv ecvhvrtnka vpehlcswgp rpanwqrcnv tpcentecrd
     1741 ttrycekvrq lklcqlgqfr srccgtcgka
//
LOCUS       NP_001355965             495 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 9 isoform 4 [Homo sapiens].
ACCESSION   NP_001355965 XP_016884857
VERSION     NP_001355965.1
DBSOURCE    REFSEQ: accession NM_001369036.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Ma,X., Yan,W., Xu,P., Ma,L., Zan,Y., Huang,L., Wang,G., Liu,L. and
            Hui,W.
  TITLE     LncRNA-p21 suppresses cell proliferation and induces apoptosis in
            gastric cancer by sponging miR-514b-3p and up-regulating ARHGEF9
            expression
  JOURNAL   Biol Chem 403 (10), 945-958 (2022)
   PUBMED   35947460
  REMARK    GeneRIF: LncRNA-p21 suppresses cell proliferation and induces
            apoptosis in gastric cancer by sponging miR-514b-3p and
            up-regulating ARHGEF9 expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Yang,H., Liao,H., Gan,S., Xiao,T. and Wu,L.
  TITLE     ARHGEF9 gene variant leads to developmental and epileptic
            encephalopathy: Genotypic phenotype analysis and treatment
            exploration
  JOURNAL   Mol Genet Genomic Med 10 (7), e1967 (2022)
   PUBMED   35638461
  REMARK    GeneRIF: ARHGEF9 gene variant leads to developmental and epileptic
            encephalopathy: Genotypic phenotype analysis and treatment
            exploration.
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Hines,D.J., Contreras,A., Garcia,B., Barker,J.S., Boren,A.J.,
            Moufawad El Achkar,C., Moss,S.J. and Hines,R.M.
  TITLE     Human ARHGEF9 intellectual disability syndrome is phenocopied by a
            mutation that disrupts collybistin binding to the GABAA receptor
            alpha2 subunit
  JOURNAL   Mol Psychiatry 27 (3), 1729-1741 (2022)
   PUBMED   35169261
  REMARK    GeneRIF: Human ARHGEF9 intellectual disability syndrome is
            phenocopied by a mutation that disrupts collybistin binding to the
            GABAA receptor alpha2 subunit.
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Ghesh,L., Besnard,T., Nizon,M., Trochu,E., Landeau-Trottier,G.,
            Breheret,F., Thauvin-Robinet,C., Bruel,A.L., Kuentz,P., Coubes,C.,
            Cuisset,L., Mignot,C., Keren,B., Bezieau,S. and Cogne,B.
  TITLE     Loss-of-function variants in ARHGEF9 are associated with an
            X-linked intellectual disability dominant disorder
  JOURNAL   Hum Mutat 42 (5), 498-505 (2021)
   PUBMED   33600053
  REMARK    GeneRIF: Loss-of-function variants in ARHGEF9 are associated with
            an X-linked intellectual disability dominant disorder.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Scala,M., Zonneveld-Huijssoon,E., Brienza,M., Mecarelli,O., van der
            Hout,A.H., Zambrelli,E., Turner,K., Zara,F., Peron,A., Vignoli,A.
            and Striano,P.
  TITLE     De novo ARHGEF9 missense variants associated with
            neurodevelopmental disorder in females: expanding the genotypic and
            phenotypic spectrum of ARHGEF9 disease in females
  JOURNAL   Neurogenetics 22 (1), 87-94 (2021)
   PUBMED   32939676
  REMARK    GeneRIF: De novo ARHGEF9 missense variants associated with
            neurodevelopmental disorder in females: expanding the genotypic and
            phenotypic spectrum of ARHGEF9 disease in females.
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Harrington,A.W., Kim,J.Y. and Yoon,S.O.
  TITLE     Activation of Rac GTPase by p75 is necessary for c-jun N-terminal
            kinase-mediated apoptosis
  JOURNAL   J Neurosci 22 (1), 156-166 (2002)
   PUBMED   11756498
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Grosskreutz,Y., Hermann,A., Kins,S., Fuhrmann,J.C., Betz,H. and
            Kneussel,M.
  TITLE     Identification of a gephyrin-binding motif in the GDP/GTP exchange
            factor collybistin
  JOURNAL   Biol Chem 382 (10), 1455-1462 (2001)
   PUBMED   11727829
  REMARK    GeneRIF: Here we identified residues critical for interaction with
            gephyrin in the linker region between the SH3 and the DH domains of
            collybistin.
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Kins,S., Betz,H. and Kirsch,J.
  TITLE     Collybistin, a newly identified brain-specific GEF, induces
            submembrane clustering of gephyrin
  JOURNAL   Nat Neurosci 3 (1), 22-29 (2000)
   PUBMED   10607391
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Reid,T., Bathoorn,A., Ahmadian,M.R. and Collard,J.G.
  TITLE     Identification and characterization of hPEM-2, a guanine nucleotide
            exchange factor specific for Cdc42
  JOURNAL   J Biol Chem 274 (47), 33587-33593 (1999)
   PUBMED   10559246
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Balint,B. and Thomas,R.
  TITLE     Hereditary Hyperekplexia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL451106.9, AL355142.11 and
            AL391277.16.
            
            On Mar 14, 2019 this sequence version replaced XP_016884857.1.
            
            Summary: The protein encoded by this gene is a Rho-like GTPase that
            switches between the active (GTP-bound) state and inactive
            (GDP-bound) state to regulate CDC42 and other genes. This
            brain-specific protein also acts as an adaptor protein for the
            recruitment of gephyrin and together these proteins facilitate
            receceptor recruitement in GABAnergic and glycinergic synapses.
            Defects in this gene are the cause of startle disease with epilepsy
            (STHEE), also known as hyperekplexia with epilepsy, as well as
            several other types of cognitive disability. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.148880.1,
                                           SRR1803611.61716.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq11.1"
     Protein         1..495
                     /product="rho guanine nucleotide exchange factor 9 isoform
                     4"
                     /note="hPEM-2 collybistin; rho guanine nucleotide exchange
                     factor 9; PEM-2 homolog; rac/Cdc42 guanine nucleotide
                     exchange factor 9; Cdc42 guanine nucleotide exchange
                     factor (GEF) 9"
                     /calculated_mol_wt=58611
     Region          <1..47
                     /region_name="SH3_ARHGEF9"
                     /note="Src homology 3 domain of the Rho guanine nucleotide
                     exchange factor ARHGEF9; cd11975"
                     /db_xref="CDD:212908"
     Region          86..265
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; smart00325"
                     /db_xref="CDD:214619"
     Site            order(89,93,188,215..216,219..220,222..223,226..227,
                     230..231,234,260,264)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          270..409
                     /region_name="PH_Collybistin_ASEF"
                     /note="Collybistin/APC-stimulated guanine nucleotide
                     exchange factor pleckstrin homology (PH) domain; cd01224"
                     /db_xref="CDD:269931"
     CDS             1..495
                     /gene="ARHGEF9"
                     /gene_synonym="COLLYBISTIN; DEE8; EIEE8; HPEM-2; PEM-2;
                     PEM2"
                     /coded_by="NM_001369036.1:942..2429"
                     /note="isoform 4 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS83477.1"
                     /db_xref="GeneID:23229"
                     /db_xref="HGNC:HGNC:14561"
                     /db_xref="MIM:300429"
ORIGIN      
        1 manrelafka gdvikvldas nkdwwwgqid deegwfpasf vrlwvnqede veegpsdvqn
       61 ghldpnsdcl clgrplqnrd qmranvinei msterhyikh lkdicegylk qcrkrrdmfs
      121 deqlkvifgn iediyrfqmg fvrdlekqyn nddphlseig pcflehqdgf wiyseycnnh
      181 ldacmelskl mkdsryqhff eacrllqqmi diaidgfllt pvqkickypl qlaellkyta
      241 qdhsdyryva aalavmrnvt qqinerkrrl enidkiaqwq asvldweged ildrsseliy
      301 tgemawiyqp ygrnqqrvff lfdhqmvlck kdlirrdily ykgridmdky evvdiedgrd
      361 ddfnvsmkna fklhnketee ihlffakkle ekirwlrafr eerkmvqede kigfeisenq
      421 krqaamtvrk vpkqkgvnsa rsvppsyppp qdplnhgqyl vpdgiaqsqv feftepkrsq
      481 spfwqnfsrl tpfkk
//
LOCUS       NP_001156783             339 aa            linear   ROD 27-APR-2025
DEFINITION  serine racemase isoform 1 [Mus musculus].
ACCESSION   NP_001156783
VERSION     NP_001156783.1
DBSOURCE    REFSEQ: accession NM_001163311.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wang,Y., Xu,D., Zhao,Y., Zhu,H., Xiu,X., Jiang,H., Liu,Y., Shan,G.
            and Wu,S.
  TITLE     Age- and Sex-Specific Regulation of Serine Racemase in the Retina
            of an Alzheimer's Disease Mouse
  JOURNAL   Invest Ophthalmol Vis Sci 66 (1), 36 (2025)
   PUBMED   39813057
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Barragan,E.V., Anisimova,M., Vijayakumar,V., Coblentz,A.,
            Park,D.K., Salaka,R.J., Nisan,A.F.K., Petshow,S., Dore,K., Zito,K.
            and Gray,J.A.
  TITLE     d-Serine Inhibits Non-ionotropic NMDA Receptor Signaling
  JOURNAL   J Neurosci 44 (32), e0140242024 (2024)
   PUBMED   38942470
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Radzishevsky,I., Odeh,M., Bodner,O., Zubedat,S., Shaulov,L.,
            Litvak,M., Esaki,K., Yoshikawa,T., Agranovich,B., Li,W.H.,
            Radzishevsky,A., Gottlieb,E., Avital,A. and Wolosker,H.
  TITLE     Impairment of serine transport across the blood-brain barrier by
            deletion of Slc38a5 causes developmental delay and motor
            dysfunction
  JOURNAL   Proc Natl Acad Sci U S A 120 (42), e2302780120 (2023)
   PUBMED   37812701
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Ni,X., Inoue,R., Wu,Y., Yoshida,T., Yaku,K., Nakagawa,T., Saito,T.,
            Saido,T.C., Takao,K. and Mori,H.
  TITLE     Regional contributions of D-serine to Alzheimer's disease pathology
            in male AppNL-G-F/NL-G-F mice
  JOURNAL   Front Aging Neurosci 15, 1211067 (2023)
   PUBMED   37455930
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Cook,S.P., Galve-Roperh,I., Martinez del Pozo,A. and
            Rodriguez-Crespo,I.
  TITLE     Direct calcium binding results in activation of brain serine
            racemase
  JOURNAL   J Biol Chem 277 (31), 27782-27792 (2002)
   PUBMED   12021263
  REMARK    GeneRIF: Direct calcium binding results in activation in brain
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Panizzutti,R., De Miranda,J., Ribeiro,C.S., Engelender,S. and
            Wolosker,H.
  TITLE     A new strategy to decrease N-methyl-D-aspartate (NMDA) receptor
            coactivation: inhibition of D-serine synthesis by converting serine
            racemase into an eliminase
  JOURNAL   Proc Natl Acad Sci U S A 98 (9), 5294-5299 (2001)
   PUBMED   11309496
REFERENCE   8  (residues 1 to 339)
  AUTHORS   De Miranda,J., Santoro,A., Engelender,S. and Wolosker,H.
  TITLE     Human serine racemase: moleular cloning, genomic organization and
            functional analysis
  JOURNAL   Gene 256 (1-2), 183-188 (2000)
   PUBMED   11054547
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Wolosker,H., Blackshaw,S. and Snyder,S.H.
  TITLE     Serine racemase: a glial enzyme synthesizing D-serine to regulate
            glutamate-N-methyl-D-aspartate neurotransmission
  JOURNAL   Proc Natl Acad Sci U S A 96 (23), 13409-13414 (1999)
   PUBMED   10557334
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL604066.9, AB232342.1, AK043738.1, AK079343.1 and BY475189.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK157122.1, SRR9219380.14313.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 45.76 cM"
     Protein         1..339
                     /product="serine racemase isoform 1"
                     /EC_number="4.3.1.17"
                     /EC_number="5.1.1.18"
                     /EC_number="4.3.1.18"
                     /note="D-serine dehydratase; L-serine dehydratase;
                     D-serine ammonia-lyase; L-serine ammonia-lyase"
                     /calculated_mol_wt=36228
     Region          5..322
                     /region_name="Trp-synth-beta_II"
                     /note="Tryptophan synthase beta superfamily (fold type
                     II); this family of pyridoxal phosphate (PLP)-dependent
                     enzymes catalyzes beta-replacement and beta-elimination
                     reactions. This CD corresponds to
                     aminocyclopropane-1-carboxylate deaminase (ACCD),
                     tryptophan...; cl00342"
                     /db_xref="CDD:444852"
     Site            order(9..10,13,16..17,48..49,198..199,268,271..272,275,
                     279..281,315..318)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:107205"
     Site            order(56,86,185..189,313)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107205"
     Site            56
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107205"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QZX7.1)"
     CDS             1..339
                     /gene="Srr"
                     /gene_synonym="M100034; Rgsc34; Srs"
                     /coded_by="NM_001163311.2:335..1354"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS25038.1"
                     /db_xref="GeneID:27364"
                     /db_xref="MGI:MGI:1351636"
ORIGIN      
        1 mcaqycisfa dvekahiniq dsihltpvlt ssilnqiagr nlffkcelfq ktgsfkirga
       61 lnairglipd tpeekpkavv thssgnhgqa ltyaaklegi payivvpqta pnckklaiqa
      121 ygasivycdp sdesrekvtq rimqetegil vhpnqepavi agqgtialev lnqvplvdal
      181 vvpvggggmv agiaitikal kpsvkvyaae psnaddcyqs klkgeltpnl hppetiadgv
      241 kssiglntwp iirdlvddvf tvtedeikya tqlvwgrmkl lieptagval aavlsqhfqt
      301 vspevknvci vlsggnvdlt slnwvgqaer papyqtvsv
//
LOCUS       NP_008880                593 aa            linear   PRI 27-APR-2025
DEFINITION  syntaxin-binding protein 2 isoform a [Homo sapiens].
ACCESSION   NP_008880
VERSION     NP_008880.2
DBSOURCE    REFSEQ: accession NM_006949.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Xinh,P.T., Chuong,H.Q., Diem,T.P.H., Nguyen,T.M., Van,N.D., Mai
            Anh,N.H., Nghia,H. and Vu,H.A.
  TITLE     Spectrum mutations of PRF1, UNC13D, STX11, and STXBP2 genes in
            Vietnamese patients with hemophagocytic lymphohistiocytosis
  JOURNAL   Int J Lab Hematol 43 (6), 1524-1530 (2021)
   PUBMED   34339548
  REMARK    GeneRIF: Spectrum mutations of PRF1, UNC13D, STX11, and STXBP2
            genes in Vietnamese patients with hemophagocytic
            lymphohistiocytosis.
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Benavides,N., Spessott,W.A., Sanmillan,M.L., Vargas,M.,
            Livingston,M.S., Erickson,N., Pozos,T.C., McCormick,M.E.,
            Scharrig,E., Messinger,Y.H. and Giraudo,C.G.
  TITLE     STXBP2-R190C Variant in a Patient With Neonatal Hemophagocytic
            Lymphohistiocytosis (HLH) and G6PD Deficiency Reveals a Critical
            Role of STXBP2 Domain 2 on Granule Exocytosis
  JOURNAL   Front Immunol 11, 545414 (2020)
   PUBMED   33162974
  REMARK    GeneRIF: STXBP2-R190C Variant in a Patient With Neonatal
            Hemophagocytic Lymphohistiocytosis (HLH) and G6PD Deficiency
            Reveals a Critical Role of STXBP2 Domain 2 on Granule Exocytosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Akyol,S., Ozcan,A., Sekine,T., Chiang,S.C.C., Yilmaz,E.,
            Karakurkcu,M., Patiroglu,T., Bryceson,Y. and Unal,E.
  TITLE     Different Clinical Presentation of 3 Children With Familial
            Hemophagocytic Lymphohistiocytosis With 2 Novel Mutations
  JOURNAL   J Pediatr Hematol Oncol 42 (7), e627-e629 (2020)
   PUBMED   31651726
  REMARK    GeneRIF: Different Clinical Presentation of 3 Children With
            Familial Hemophagocytic Lymphohistiocytosis With 2 Novel Mutations.
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Mosa,M.H., Nicolle,O., Maschalidi,S., Sepulveda,F.E.,
            Bidaud-Meynard,A., Menche,C., Michels,B.E., Michaux,G., de Saint
            Basile,G. and Farin,H.F.
  TITLE     Dynamic Formation of Microvillus Inclusions During Enterocyte
            Differentiation in Munc18-2-Deficient Intestinal Organoids
  JOURNAL   Cell Mol Gastroenterol Hepatol 6 (4), 477-493.e1 (2018)
   PUBMED   30364784
  REMARK    GeneRIF: Loss of Munc18-2/Stxbp2 recapitulated the pathologic
            features observed in patients with MUNC18-2 deficiency.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 593)
  AUTHORS   Tellam,J.T., Macaulay,S.L., McIntosh,S., Hewish,D.R., Ward,C.W. and
            James,D.E.
  TITLE     Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes.
            Putative role in insulin-dependent movement of GLUT-4
  JOURNAL   J Biol Chem 272 (10), 6179-6186 (1997)
   PUBMED   9045631
REFERENCE   7  (residues 1 to 593)
  AUTHORS   Ziegler,S.F., Mortrud,M.T., Swartz,A.R., Baker,E., Sutherland,G.R.,
            Burmeister,M. and Mulligan,J.T.
  TITLE     Molecular characterization of a nonneuronal human UNC18 homolog
  JOURNAL   Genomics 37 (1), 19-23 (1996)
   PUBMED   8921365
REFERENCE   8  (residues 1 to 593)
  AUTHORS   Ibaraki,K., Horikawa,H.P., Morita,T., Mori,H., Sakimura,K.,
            Mishina,M., Saisu,H. and Abe,T.
  TITLE     Identification of four different forms of syntaxin 3
  JOURNAL   Biochem Biophys Res Commun 211 (3), 997-1005 (1995)
   PUBMED   7598732
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Zhang,K., Astigarraga,I., Bryceson,Y., Lehmberg,K., Machowicz,R.,
            Marsh,R., Sieni,E., Wang,Z. and Nichols,K.E.
  TITLE     Familial Hemophagocytic Lymphohistiocytosis
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA431480.1, AK222967.1 and
            BC002869.2.
            
            On May 17, 2008 this sequence version replaced NP_008880.1.
            
            Summary: This gene encodes a member of the STXBP/unc-18/SEC1
            family. The encoded protein is involved in intracellular
            trafficking, control of SNARE (soluble NSF attachment protein
            receptor) complex assembly, and the release of cytotoxic granules
            by natural killer cells. Mutations in this gene are associated with
            familial hemophagocytic lymphohistiocytosis. Alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene. [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (1) uses an alternate in-frame
            splice site in the coding region, compared to variant 3. The
            encoded isoform (a) is shorter than isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.145586.1,
                                           SRR3476690.85116.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221283.10/ ENSP00000221283.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..593
                     /product="syntaxin-binding protein 2 isoform a"
                     /note="protein unc-18 homolog B"
                     /calculated_mol_wt=66322
     Region          29..579
                     /region_name="Sec1"
                     /note="Sec1 family; pfam00995"
                     /db_xref="CDD:460020"
     Region          444..466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15833.2)"
     CDS             1..593
                     /gene="STXBP2"
                     /gene_synonym="FHL5; Hunc18b; MUNC18-2; pp10122; unc-18B;
                     UNC18-2; UNC18B"
                     /coded_by="NM_006949.4:41..1822"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12181.1"
                     /db_xref="GeneID:6813"
                     /db_xref="HGNC:HGNC:11445"
                     /db_xref="MIM:601717"
ORIGIN      
        1 mapsglkavv gekilsgvir svkkdgewkv limdhpsmri lsscckmsdi laegitived
       61 inkrrepips leaiyllspt eksvqalikd fqgtptftyk aahifftdtc peplfselgr
      121 srlakvvktl keihlaflpy eaqvfsldap hstynlycpf raeertrqle vlaqqiatlc
      181 atlqeypair yrkgpedtaq lahavlakln afkadtpslg egpektrsql limdraadpv
      241 spllheltfq amaydlldie qdtyryettg lsearekavl ldedddlwve lrhmhiadvs
      301 kkvtellrtf ceskrlttdk anikdlsqil kkmpqyqkel nkysthlhla ddcmkhfkgs
      361 veklcsveqd lamgsdaege kikdsmkliv pvlldaavpa ydkirvllly illrngvsee
      421 nlakliqhan vqahsslirn leqlggtvtn pggsgtssrl eprermepty qlsrwtpvik
      481 dvmedavedr ldrnlwpfvs dpaptassqa avsarfghwh knkagieara gprlivyvmg
      541 gvamsemraa yevtrategk wevligsshi ltptrflddl kaldkkledi alp
//
LOCUS       NP_001397                340 aa            linear   PRI 27-APR-2025
DEFINITION  ephrin-B3 precursor [Homo sapiens].
ACCESSION   NP_001397
VERSION     NP_001397.1
DBSOURCE    REFSEQ: accession NM_001406.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Qiao,Z., Liao,M., Xiao,M., Luo,S., Wang,K., Niu,M., Jiang,H.,
            Sun,S., Xu,G., Xu,N., Xu,Q. and Liu,Y.
  TITLE     Ephrin B3 exacerbates colitis and colitis-associated colorectal
            cancer
  JOURNAL   Biochem Pharmacol 220, 116004 (2024)
   PUBMED   38142837
  REMARK    GeneRIF: Ephrin B3 exacerbates colitis and colitis-associated
            colorectal cancer.
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Garcia-Diaz,B., Bachelin,C., Coulpier,F., Gerschenfeld,G.,
            Deboux,C., Zujovic,V., Charnay,P., Topilko,P. and Baron-Van
            Evercooren,A.
  TITLE     Blood vessels guide Schwann cell migration in the adult
            demyelinated CNS through Eph/ephrin signaling
  JOURNAL   Acta Neuropathol 138 (3), 457-476 (2019)
   PUBMED   31011859
  REMARK    GeneRIF: Blood vessels guide Schwann cell migration in the adult
            demyelinated CNS through Eph/ephrin signaling.
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Wu,T., Zhang,B.Q., Raelson,J., Yao,Y.M., Wu,H.D., Xu,Z.X.,
            Marois-Blanchet,F.C., Tahir,M.R., Wang,Y., Bradley,W.E., Luo,H.,
            Wu,J., Sheng,J.Z. and Hu,S.J.
  TITLE     Analysis of the association of EPHB6, EFNB1 and EFNB3 variants with
            hypertension risks in males with hypogonadism
  JOURNAL   Sci Rep 8 (1), 14497 (2018)
   PUBMED   30262919
  REMARK    GeneRIF: Analysis of the association of EPHB6, EFNB1 and EFNB3
            variants with hypertension risks in males with hypogonadism.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Prydz,K., Halstensen,T.S., Holen,H.L. and Aasheim,H.C.
  TITLE     Ephrin-B3 binds both cell-associated and secreted proteoglycans
  JOURNAL   Biochem Biophys Res Commun 503 (4), 2212-2217 (2018)
   PUBMED   29953858
  REMARK    GeneRIF: identified secretory and cell associated proteoglycans
            with high ability to bind ephrin-B3 and suggest that ephrin-B3 can
            bind to a protein complex organized by a membrane associated PG.
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Zhou,R.
  TITLE     The Eph family receptors and ligands
  JOURNAL   Pharmacol Ther 77 (3), 151-181 (1998)
   PUBMED   9576626
  REMARK    Review article
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Bergemann,A.D., Zhang,L., Chiang,M.K., Brambilla,R., Klein,R. and
            Flanagan,J.G.
  TITLE     Ephrin-B3, a ligand for the receptor EphB3, expressed at the
            midline of the developing neural tube
  JOURNAL   Oncogene 16 (4), 471-480 (1998)
   PUBMED   9484836
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Flanagan,J.G. and Vanderhaeghen,P.
  TITLE     The ephrins and Eph receptors in neural development
  JOURNAL   Annu Rev Neurosci 21, 309-345 (1998)
   PUBMED   9530499
  REMARK    Review article
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Tang,X.X., Pleasure,D.E. and Ikegaki,N.
  TITLE     cDNA cloning, chromosomal localization, and expression pattern of
            EPLG8, a new member of the EPLG gene family encoding ligands of
            EPH-related protein-tyrosine kinase receptors
  JOURNAL   Genomics 41 (1), 17-24 (1997)
   PUBMED   9126477
REFERENCE   10 (residues 1 to 340)
  AUTHORS   Gale,N.W., Flenniken,A., Compton,D.C., Jenkins,N., Copeland,N.G.,
            Gilbert,D.J., Davis,S., Wilkinson,D.G. and Yancopoulos,G.D.
  TITLE     Elk-L3, a novel transmembrane ligand for the Eph family of receptor
            tyrosine kinases, expressed in embryonic floor plate, roof plate
            and hindbrain segments
  JOURNAL   Oncogene 13 (6), 1343-1352 (1996)
   PUBMED   8808709
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ892951.1, U57001.1, U66406.1
            and BC022499.1.
            
            Summary:  EFNB3, a member of the ephrin gene family, is important
            in brain development as well as in its maintenance. Moreover, since
            levels of EFNB3 expression were particularly high in several
            forebrain subregions compared to other brain subregions, it may
            play a pivotal role in forebrain function.  The EPH and EPH-related
            receptors comprise the largest subfamily of receptor
            protein-tyrosine kinases and have been implicated in mediating
            developmental events, particularly in the nervous system. EPH
            Receptors typically have a single kinase domain and an
            extracellular region containing a Cys-rich domain and 2 fibronectin
            type III repeats. The ephrin ligands and receptors have been named
            by the Eph Nomenclature Committee (1997). Based on their structures
            and sequence relationships, ephrins are divided into the ephrin-A
            (EFNA) class, which are anchored to the membrane by a
            glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB)
            class, which are transmembrane proteins. The Eph family of
            receptors are similarly divided into 2 groups based on the
            similarity of their extracellular domain sequences and their
            affinities for binding ephrin-A and ephrin-B ligands. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042944.2, U66406.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000226091.3/ ENSP00000226091.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..340
                     /product="ephrin-B3 precursor"
                     /note="eph-related receptor tyrosine kinase ligand 8;
                     EPH-related receptor transmembrane ligand ELK-L3"
                     /calculated_mol_wt=33342
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2511
     mat_peptide     28..340
                     /product="ephrin-B3"
                     /calculated_mol_wt=33342
     Region          31..168
                     /region_name="Cupredoxin"
                     /note="Cupredoxin superfamily; cl19115"
                     /db_xref="CDD:473140"
     Region          168..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15768.1)"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15768.1)"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15768.1)"
     Region          254..298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15768.1)"
     Site            271
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O35393; propagated from
                     UniProtKB/Swiss-Prot (Q15768.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15768.1)"
     Region          338..340
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15768.1)"
     CDS             1..340
                     /gene="EFNB3"
                     /gene_synonym="EFL6; EPLG8; LERK8"
                     /coded_by="NM_001406.4:398..1420"
                     /db_xref="CCDS:CCDS11120.1"
                     /db_xref="GeneID:1949"
                     /db_xref="HGNC:HGNC:3228"
                     /db_xref="MIM:602297"
ORIGIN      
        1 mgpphsgpgg vrvgallllg vlglvsglsl epvywnsank rfqaeggyvl ypqigdrldl
       61 lcprarppgp hsspnyefyk lylvggaqgr rceappapnl lltcdrpdld lrftikfqey
      121 spnlwghefr shhdyyiiat sdgtregles lqggvcltrg mkvllrvgqs prggavprkp
      181 vsempmerdr gaahslepgk enlpgdptsn atsrgaegpl pppsmpavag aagglallll
      241 gvagaggamc wrrrrakpse srhpgpgsfg rggslglggg ggmgpreaep gelgialrgg
      301 gaadppfcph yekvsgdygh pvyivqdgpp qsppniyykv
//
LOCUS       NP_078779               2406 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor HIVEP3 isoform a [Homo sapiens].
ACCESSION   NP_078779
VERSION     NP_078779.2
DBSOURCE    REFSEQ: accession NM_024503.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2406)
  AUTHORS   Tang,Y., Xu,G., Hu,B. and Zhu,Y.
  TITLE     HIVEP3 as a potential prognostic factor promotes the development of
            acute myeloid leukemia
  JOURNAL   Growth Factors 41 (1), 43-56 (2023)
   PUBMED   36571205
  REMARK    GeneRIF: HIVEP3 as a potential prognostic factor promotes the
            development of acute myeloid leukemia.
REFERENCE   2  (residues 1 to 2406)
  AUTHORS   Zhang,X., Zhang,X., Liu,K., Li,W., Wang,J., Liu,P. and Ma,W.
  TITLE     HIVEP3 cooperates with ferroptosis gene signatures to confer
            adverse prognosis in acute myeloid leukemia
  JOURNAL   Cancer Med 11 (24), 5050-5065 (2022)
   PUBMED   35535739
  REMARK    GeneRIF: HIVEP3 cooperates with ferroptosis gene signatures to
            confer adverse prognosis in acute myeloid leukemia.
REFERENCE   3  (residues 1 to 2406)
  AUTHORS   Soini,L., Leysen,S., Crabbe,T., Davis,J. and Ottmann,C.
  TITLE     The identification and structural analysis of potential 14-3-3
            interaction sites on the bone regulator protein Schnurri-3
  JOURNAL   Acta Crystallogr F Struct Biol Commun 77 (Pt 8), 254-261 (2021)
   PUBMED   34341191
  REMARK    GeneRIF: The identification and structural analysis of potential
            14-3-3 interaction sites on the bone regulator protein Schnurri-3.
REFERENCE   4  (residues 1 to 2406)
  AUTHORS   Lavocat,F., Osta,B. and Miossec,P.
  TITLE     Increased sensitivity of rheumatoid synoviocytes to Schnurri-3
            expression in TNF-alpha and IL-17A induced osteoblastic
            differentiation
  JOURNAL   Bone 87, 89-96 (2016)
   PUBMED   27072520
  REMARK    GeneRIF: rheumatoid arthritis-fibroblast-like synoviocytes were
            more sensitive to the synergistic increase of Schnurri-3
            expression.
REFERENCE   5  (residues 1 to 2406)
  AUTHORS   Chung,S.A., Brown,E.E., Williams,A.H., Ramos,P.S., Berthier,C.C.,
            Bhangale,T., Alarcon-Riquelme,M.E., Behrens,T.W., Criswell,L.A.,
            Graham,D.C., Demirci,F.Y., Edberg,J.C., Gaffney,P.M., Harley,J.B.,
            Jacob,C.O., Kamboh,M.I., Kelly,J.A., Manzi,S., Moser-Sivils,K.L.,
            Russell,L.P., Petri,M., Tsao,B.P., Vyse,T.J., Zidovetzki,R.,
            Kretzler,M., Kimberly,R.P., Freedman,B.I., Graham,R.R. and
            Langefeld,C.D.
  CONSRTM   International Consortium for Systemic Lupus Erythematosus Genetics
  TITLE     Lupus nephritis susceptibility loci in women with systemic lupus
            erythematosus
  JOURNAL   J Am Soc Nephrol 25 (12), 2859-2870 (2014)
   PUBMED   24925725
REFERENCE   6  (residues 1 to 2406)
  AUTHORS   Qin,H., Wang,J., Liang,Y., Taniguchi,Y., Tanigaki,K. and Han,H.
  TITLE     RING1 inhibits transactivation of RBP-J by Notch through
            interaction with LIM protein KyoT2
  JOURNAL   Nucleic Acids Res 32 (4), 1492-1501 (2004)
   PUBMED   14999091
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 2406)
  AUTHORS   Oukka,M., Wein,M.N. and Glimcher,L.H.
  TITLE     Schnurri-3 (KRC) interacts with c-Jun to regulate the IL-2 gene in
            T cells
  JOURNAL   J Exp Med 199 (1), 15-24 (2004)
   PUBMED   14707112
  REMARK    GeneRIF: Overexpression of KRC in transformed and primary T cells
            leads to increased IL-2 production.
REFERENCE   8  (residues 1 to 2406)
  AUTHORS   Oukka,M., Kim,S.T., Lugo,G., Sun,J., Wu,L.C. and Glimcher,L.H.
  TITLE     A mammalian homolog of Drosophila schnurri, KRC, regulates TNF
            receptor-driven responses and interacts with TRAF2
  JOURNAL   Mol Cell 9 (1), 121-131 (2002)
   PUBMED   11804591
REFERENCE   9  (residues 1 to 2406)
  AUTHORS   Hicar,M.D., Liu,Y., Allen,C.E. and Wu,L.C.
  TITLE     Structure of the human zinc finger protein HIVEP3: molecular
            cloning, expression, exon-intron structure, and comparison with
            paralogous genes HIVEP1 and HIVEP2
  JOURNAL   Genomics 71 (1), 89-100 (2001)
   PUBMED   11161801
REFERENCE   10 (residues 1 to 2406)
  AUTHORS   Rustgi,A.K., Van 't Veer,L.J. and Bernards,R.
  TITLE     Two genes encode factors with NF-kappa B- and H2TF1-like
            DNA-binding properties
  JOURNAL   Proc Natl Acad Sci U S A 87 (22), 8707-8710 (1990)
   PUBMED   2247438
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105268.2, BC152563.1,
            AF278765.1, AL445933.32 and AI082114.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 13, 2006 this sequence version replaced NP_078779.1.
            
            Summary: This gene encodes a member of the human immunodeficiency
            virus type 1 enhancer-binding protein family. Members of this
            protein family contain multiple zinc finger and acid-rich (ZAS)
            domains and serine-threonine rich regions. This protein acts as a
            transcription factor and is able to regulate nuclear factor
            kappaB-mediated transcription by binding the kappaB motif in target
            genes. This protein also binds the recombination signal sequence
            that flanks the V, D, and J regions of immunoglobulin and T-cell
            receptors. Alternate splicing results in both coding and non-coding
            transcript variants. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF278765.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529, SAMEA2159931
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372583.6/ ENSP00000361664.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..2406
                     /product="transcription factor HIVEP3 isoform a"
                     /note="transcription factor HIVEP3; kappa-binding protein
                     1; zinc finger protein ZAS3; kappa-B and V(D)J
                     recombination signal sequences-binding protein; ZAS
                     family, member 3; human immunodeficiency virus type I
                     enhancer binding protein 3"
                     /calculated_mol_wt=259335
     Region          1..112
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          192..242
                     /region_name="ZAS1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          194..214
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          207..231
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          211..1074
                     /region_name="No DNA binding activity or transactivation
                     activity, but complete prevention of TRAF-dependent
                     NF-Kappa-B activation, associates with TRAF2 and JUN.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          222..242
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          264..287
                     /region_name="Acidic 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          272..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          377..409
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          481..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          597..633
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          677..696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          706..1115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          862..883
                     /region_name="Acidic 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          903..909
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          1268..1303
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          1406..1459
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          1472..1594
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          1692..1727
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          1754..1806
                     /region_name="ZAS2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          1754..1776
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          1756..1776
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(1761,1763,1765,1767..1768,1771..1772,1775,1789,
                     1791..1793,1795..1796,1800)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          1768..1793
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1779..1812
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          1784..1802
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          1817..1872
                     /region_name="Acidic 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          1818..2033
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          <1877..2395
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          2052..2113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          2053..2148
                     /region_name="6 X 4 AA tandem repeats of S-P-X-[RK]"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          2125..2151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     Region          2224..2406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1R4.1)"
     CDS             1..2406
                     /gene="HIVEP3"
                     /gene_synonym="KBP-1; KBP1; KRC; Schnurri-3; SHN3; ZAS3;
                     ZNF40C"
                     /coded_by="NM_024503.5:1311..8531"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS463.1"
                     /db_xref="GeneID:59269"
                     /db_xref="HGNC:HGNC:13561"
                     /db_xref="MIM:606649"
ORIGIN      
        1 mdpeqsvkgt kkaegsprkr ltkgeaiqts vsssvpypgs gtaatqespa qellapqpfp
       61 gpssvlregs qektgqqqkp pkrppieasv hisqlpqhpl tpafmspgkp ehllegstwq
      121 lvdpmrpgps gsfvapglhp qsqllpshas iippedlpgv pkvfvprpsq vslkpteeah
      181 kkerkpqkpg kyicqycsrp cakpsvlqkh irshtgerpy pcgpcgfsfk tksnlykhrk
      241 shahrikagl asgmggemyp hglemeripg eefeeptege stdseeetsa tsghpaelsp
      301 rpkqpllssg lyssgshsss hercslsqss taqsledppp fvepssehpl shkpedthti
      361 kqklalrlse rkkvideqaf lspgskgste sgyfsrsesa eqqvsppntn aksyaeiifg
      421 kcgrigqrta mltatstqpl lplstedkps lvplsvprtq viehitklit ineavvdtse
      481 idsvkprrss lsrrssmesp ksslyrepls shsektkpeq sllslqhpps tappvpllrs
      541 hsmpsaacti stphhpfrgs ysfddhitds ealshsshvf tshprmlkrq paielplgge
      601 ysseepgpss kdtaskpsde vepkeseltk ktkkglktkg viyecnicga rykkrdnyea
      661 hkkyycselq iakpisagth tspeaeksqi ehepwsqmmh yklgttlelt plrkrrkeks
      721 lgdeeeppaf estksqfgsp gpsdaarnlp lestkspaep sksvpslegp tgfqprtpkp
      781 gsgsesgker rttskeisvi qhtssfeksd sleqpsgleg edkplaqfps pppaphgrsa
      841 hslqpklvrq pniqvpeilv teepdrpdte pepppkepek teefqwpqrs qtlaqlpaek
      901 lppkkkrlrl aemaqssges sfessvplsr spsqesnvsl sgssrsasfe rddhgkaeap
      961 spssdmrpkp lgthmltvps hhpharemrr saseqspnvs hsahmtetrs ksfdygslsl
     1021 tgpsapapva pparvapper rkcflvrqas lsrppesele vapkgrqese epqpssskps
     1081 aksslsqiss aatshggppg gkgpgqdrpp lgptvpytea lqvfhhpvaq tplhekpylp
     1141 ppvslfsfqh lvqhepgqsp effstqamss llsspysmpp lppslfqapp lplqptvlhp
     1201 gqlhlpqlmp hpanipfrqp psflpmpypt ssalssgffl plqsqfalql pgdveshlpq
     1261 iktslaplat gsaglspste yssdirlppv appasssapt sapplalpac pdtmvslvvp
     1321 vrvqtnmpsy gsamyttlsq ilvtqsqgss atvalpkfee ppskgttvcg advhevgpgp
     1381 sglseeqsra fptpylrvpv tlperkgtsl ssesilsleg ssstaggskr vlspagslel
     1441 tmetqqqkrv keeeaskade klelvkpcsv vltstedgkr pekshlgnqg qgrrelemls
     1501 slssdpsdtk eipplphpal shgtapgsea lkeypqpsgk phrrgltpls vkkedskeqp
     1561 dlpslappss lplsetssrp aksqegtdsk kvlqfpslht ttnvswcyln yikpnhiqha
     1621 drrssvyagw cislynpnlp gvstkaalsl lrskqkvske tytmataphp eagrlvpsss
     1681 rkprmtevhl pslvspegqk dlarvekeee rrgepeedap asqrgepari kifeggyksn
     1741 eeyvyvrgrg rgkyvceecg irckkpsmlk khirthtdvr pyvckhchfa fktkgnltkh
     1801 mkskahskkc qetgvleele aeegtsddlf qdsegregse aveehqfsdl edsdsdsdld
     1861 edededeees qdelsrpsse apppgpphal radsspilgp qppdapasgt eatrgssvse
     1921 aerltasscs mssqsmpglp wlgpaplgsv ekdtgsalsy kpvsprrpws pskeagsrpp
     1981 larkhsltkn dsspqrcspa repqasapsp pglhvdpgrg mgalpcgspr lqlspltlcp
     2041 lgrelaprah vlsklegttd pglprysptr rwspgqaesp prsappgkwa lagpgspsag
     2101 ehgpglgldp rvlfppaplp hkllsrspet caspwqkaes rspscspgpa hplssrpfsa
     2161 lhdfhghila rteenifshl plhsqhltra pcplipiggi qmvqarpgah ptllpgptaa
     2221 wvsgfsgggs dltgareaqe rgrwsptess sasvspvakv skftlssele ggdypkerer
     2281 tgggpgrppd wtphgtgapa eptpthspct ppdtlprppq grraaqswsp rlespraptn
     2341 pepsatppld rsssvgclae asarfpartr nlsgeprtrq dspkpsgsge prahphqped
     2401 rvppna
//
LOCUS       NP_059965                239 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding protein 38 isoform a [Homo sapiens].
ACCESSION   NP_059965
VERSION     NP_059965.2
DBSOURCE    REFSEQ: accession NM_017495.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Zhong,T., Zhang,J., Liu,X. and Li,H.
  TITLE     TRIM17-mediated ubiquitination and degradation of RBM38 promotes
            cisplatin resistance in non-small cell lung cancer
  JOURNAL   Cell Oncol (Dordr) 46 (5), 1493-1507 (2023)
   PUBMED   37219768
  REMARK    GeneRIF: TRIM17-mediated ubiquitination and degradation of RBM38
            promotes cisplatin resistance in non-small cell lung cancer.
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Zhang,X., Zhang,X., Jia,Q., Li,H., Ma,R., Yang,G., Yin,F., Jiang,N.
            and Yin,D.
  TITLE     LncRNA CALML3-AS1 suppresses papillary thyroid cancer progression
            via sponging miR-20a-5p/RBM38 axis
  JOURNAL   BMC Cancer 22 (1), 344 (2022)
   PUBMED   35351042
  REMARK    GeneRIF: LncRNA CALML3-AS1 suppresses papillary thyroid cancer
            progression via sponging miR-20a-5p/RBM38 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Zhang,Y.P., Gao,D. and Wu,P.
  TITLE     [RBM38 Mediates the Proliferation of Acute Myeloid Leukemia Cells
            HL-60 by Regulating FZD1 mRNA Stability]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 29 (6), 1775-1779 (2021)
   PUBMED   34893109
  REMARK    GeneRIF: [RBM38 Mediates the Proliferation of Acute Myeloid
            Leukemia Cells HL-60 by Regulating FZD1 mRNA Stability].
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Li,Y., Shi,Y., He,Y., Li,X. and Yang,J.
  TITLE     RNA binding Motif protein-38 regulates myocardial hypertrophy in
            LXR-alpha-dependent lipogenesis pathway
  JOURNAL   Bioengineered 12 (2), 9655-9667 (2021)
   PUBMED   34854353
  REMARK    GeneRIF: RNA binding Motif protein-38 regulates myocardial
            hypertrophy in LXR-alpha-dependent lipogenesis pathway.
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Guan,B., Li,G., Wan,B., Guo,X., Huang,D., Ma,J., Gong,P., Guo,J.
            and Bu,Y.
  TITLE     RNA-binding protein RBM38 inhibits colorectal cancer progression by
            partly and competitively binding to PTEN 3'UTR with miR-92a-3p
  JOURNAL   Environ Toxicol 36 (12), 2436-2447 (2021)
   PUBMED   34453780
  REMARK    GeneRIF: RNA-binding protein RBM38 inhibits colorectal cancer
            progression by partly and competitively binding to PTEN 3'UTR with
            miR-92a-3p.
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Kamatani,Y., Matsuda,K., Okada,Y., Kubo,M., Hosono,N., Daigo,Y.,
            Nakamura,Y. and Kamatani,N.
  TITLE     Genome-wide association study of hematological and biochemical
            traits in a Japanese population
  JOURNAL   Nat Genet 42 (3), 210-215 (2010)
   PUBMED   20139978
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Miyamoto,S., Hidaka,K., Jin,D. and Morisaki,T.
  TITLE     RNA-binding proteins Rbm38 and Rbm24 regulate myogenic
            differentiation via p21-dependent and -independent regulatory
            pathways
  JOURNAL   Genes Cells 14 (11), 1241-1252 (2009)
   PUBMED   19817877
  REMARK    GeneRIF: it was found that this protein Rbm38 regulates myogenic
            differentiation via the p21 signal pathway.
REFERENCE   8  (residues 1 to 239)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
REFERENCE   9  (residues 1 to 239)
  AUTHORS   Shu,L., Yan,W. and Chen,X.
  TITLE     RNPC1, an RNA-binding protein and a target of the p53 family, is
            required for maintaining the stability of the basal and
            stress-induced p21 transcript
  JOURNAL   Genes Dev 20 (21), 2961-2972 (2006)
   PUBMED   17050675
  REMARK    GeneRIF: RNPC1a is required to maintain the stability of p21
            transcript induced by p53.
REFERENCE   10 (residues 1 to 239)
  AUTHORS   Krackhardt,A.M., Witzens,M., Harig,S., Hodi,F.S., Zauls,A.J.,
            Chessia,M., Barrett,P. and Gribben,J.G.
  TITLE     Identification of tumor-associated antigens in chronic lymphocytic
            leukemia by SEREX
  JOURNAL   Blood 100 (6), 2123-2131 (2002)
   PUBMED   12200376
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL109955.38.
            
            On Sep 11, 2003 this sequence version replaced NP_059965.1.
            
            Transcript Variant: This variant (1) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 3, resulting in
            an isoform (a) that is shorter than isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.364281.1, AF432218.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356208.10/ ENSP00000348538.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.31"
     Protein         1..239
                     /product="RNA-binding protein 38 isoform a"
                     /note="RNA-binding region (RNP1, RRM) containing 1;
                     CLL-associated antigen KW-5; RNA-binding protein 38;
                     ssDNA-binding protein SEB4; RNA-binding region-containing
                     protein 1"
                     /calculated_mol_wt=25367
     Region          34..109
                     /region_name="RRM_RBM24_RBM38_like"
                     /note="RNA recognition motif (RRM) found in eukaryotic
                     RNA-binding protein RBM24, RBM38 and similar proteins;
                     cd12384"
                     /db_xref="CDD:409818"
     Region          <46..237
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..239
                     /gene="RBM38"
                     /gene_synonym="dJ800J21.2; HSRNASEB; RNPC1; SEB4B; SEB4D"
                     /coded_by="NM_017495.6:187..906"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46617.1"
                     /db_xref="GeneID:55544"
                     /db_xref="HGNC:HGNC:15818"
                     /db_xref="MIM:612428"
ORIGIN      
        1 mllqpapcap sagfprplaa pgamhgsqkd ttftkifvgg lpyhttdasl rkyfegfgdi
       61 eeavvitdrq tgksrgygfv tmadraaaer ackdpnpiid grkanvnlay lgakprslqt
      121 gfaigvqqlh ptliqrtygl tphyiyppai vqpsvvipaa pvpslsspyi eytpaspaya
      181 qyppatydqy pyaaspataa sfvgysypaa vpqalsaaap agttfvqyqa pqlqpdrmq
//
LOCUS       NP_079131                607 aa            linear   PRI 27-APR-2025
DEFINITION  actin-related protein 5 [Homo sapiens].
ACCESSION   NP_079131
VERSION     NP_079131.3
DBSOURCE    REFSEQ: accession NM_024855.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Ayala,R., Willhoft,O., Aramayo,R.J., Wilkinson,M., McCormack,E.A.,
            Ocloo,L., Wigley,D.B. and Zhang,X.
  TITLE     Structure and regulation of the human INO80-nucleosome complex
  JOURNAL   Nature 556 (7701), 391-395 (2018)
   PUBMED   29643506
REFERENCE   5  (residues 1 to 607)
  AUTHORS   Zhang,S., Zhou,B., Wang,L., Li,P., Bennett,B.D., Snyder,R.,
            Garantziotis,S., Fargo,D.C., Cox,A.D., Chen,L. and Hu,G.
  TITLE     INO80 is required for oncogenic transcription and tumor growth in
            non-small cell lung cancer
  JOURNAL   Oncogene 36 (10), 1430-1439 (2017)
   PUBMED   27641337
REFERENCE   6  (residues 1 to 607)
  AUTHORS   Aoyama,N., Oka,A., Kitayama,K., Kurumizaka,H. and Harata,M.
  TITLE     The actin-related protein hArp8 accumulates on the mitotic
            chromosomes and functions in chromosome alignment
  JOURNAL   Exp Cell Res 314 (4), 859-868 (2008)
   PUBMED   18163988
REFERENCE   7  (residues 1 to 607)
  AUTHORS   Wu,S., Shi,Y., Mulligan,P., Gay,F., Landry,J., Liu,H., Lu,J.,
            Qi,H.H., Wang,W., Nickoloff,J.A., Wu,C. and Shi,Y.
  TITLE     A YY1-INO80 complex regulates genomic stability through homologous
            recombination-based repair
  JOURNAL   Nat Struct Mol Biol 14 (12), 1165-1172 (2007)
   PUBMED   18026119
REFERENCE   8  (residues 1 to 607)
  AUTHORS   Jin,J., Cai,Y., Yao,T., Gottschalk,A.J., Florens,L., Swanson,S.K.,
            Gutierrez,J.L., Coleman,M.K., Workman,J.L., Mushegian,A.,
            Washburn,M.P., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian chromatin remodeling complex with similarities to the
            yeast INO80 complex
  JOURNAL   J Biol Chem 280 (50), 41207-41212 (2005)
   PUBMED   16230350
REFERENCE   9  (residues 1 to 607)
  AUTHORS   Lee,S.Y., Obata,Y., Yoshida,M., Stockert,E., Williamson,B.,
            Jungbluth,A.A., Chen,Y.T., Old,L.J. and Scanlan,M.J.
  TITLE     Immunomic analysis of human sarcoma
  JOURNAL   Proc Natl Acad Sci U S A 100 (5), 2651-2656 (2003)
   PUBMED   12601173
REFERENCE   10 (residues 1 to 607)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC038402.1, AK022847.1, BF529768.1 and AL133519.28.
            
            On Jul 6, 2007 this sequence version replaced NP_079131.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.112801.1,
                                           SRR1803611.171891.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000243903.6/ ENSP00000243903.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.23"
     Protein         1..607
                     /product="actin-related protein 5"
                     /note="INO80 complex subunit M; ARP5 actin related protein
                     5 homolog; sarcoma antigen NY-SAR-16; hARP5"
                     /calculated_mol_wt=68167
     Region          32..568
                     /region_name="ASKHA_NBD_Arp5"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein5 (Arp5) and similar proteins; cd10211"
                     /db_xref="CDD:466817"
     Region          <339..558
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
     Region          584..607
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9F9.2)"
     CDS             1..607
                     /gene="ACTR5"
                     /gene_synonym="Arp5; INO80M"
                     /coded_by="NM_024855.4:20..1843"
                     /db_xref="CCDS:CCDS13308.1"
                     /db_xref="GeneID:79913"
                     /db_xref="HGNC:HGNC:14671"
                     /db_xref="MIM:619730"
ORIGIN      
        1 maanvfpfrd araapdpvle agpvahgplp vplvldngsf qvragwacpg qdpgpeprlq
       61 fravcargrg gargasgpqv gnalgslepl rwmlrspfdr nvpvnlelqe llldysfqhl
      121 gvssqgcvdh pivlteavcn plysrqmmse llfecygipk vaygidslfs fyhnkpknsm
      181 csgliissgy qcthvlpile grldaknckr inlggsqaag ylqrllqlky pghlaaitls
      241 rmeeilhehs yiaedyveel hkwrcpdyye nnvhkmqlpf sskllgstlt seekqerrqq
      301 qlrrlqelna rrreeklqld qerldrllyv qelledgqmd qfhkalieln mdspeelqsy
      361 iqklsiaveq akqkilqaev nlevdvvdsk petpdleqle psledvesmn dfdplfseet
      421 pgvekpvttv qpvfnlaayh qlfvgterir apeiifqpsl igeeqagiae tlqyildryp
      481 kdiqemlvqn vfltggntmy pgmkarmeke llemrpfrss fqvqlasnpv ldawygardw
      541 alnhlddnev witrkeyeek ggeylkehca sniyvpirlp kqasrssdaq asskgsaagg
      601 ggageqa
//
LOCUS       NP_034134                491 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome P450 2C40 precursor [Mus musculus].
ACCESSION   NP_034134 NP_598904 XP_922590 XP_930072 XP_930073 XP_930075
            XP_930076
VERSION     NP_034134.3
DBSOURCE    REFSEQ: accession NM_010004.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Creasy,K.T., Jiang,J., Ren,H., Peterson,M.L. and Spear,B.T.
  TITLE     Zinc Fingers and Homeoboxes 2 (Zhx2) Regulates Sexually Dimorphic
            Cyp Gene Expression in the Adult Mouse Liver
  JOURNAL   Gene Expr 17 (1), 7-17 (2016)
   PUBMED   27197076
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Kasai,F., Yoshihara,M., Matsukuma,S., O'Brien,P. and
            Ferguson-Smith,M.A.
  TITLE     Emergence of complex rearrangements at translocation breakpoints in
            a transgenic mouse; implications for mechanisms involved in the
            formation of chromosome rearrangements
  JOURNAL   Cytogenet Genome Res 119 (1-2), 83-90 (2007)
   PUBMED   18160786
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Ghazalpour,A., Doss,S., Zhang,B., Wang,S., Plaisier,C.,
            Castellanos,R., Brozell,A., Schadt,E.E., Drake,T.A., Lusis,A.J. and
            Horvath,S.
  TITLE     Integrating genetic and network analysis to characterize genes
            related to mouse weight
  JOURNAL   PLoS Genet 2 (8), e130 (2006)
   PUBMED   16934000
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Wang,S., Yehya,N., Schadt,E.E., Wang,H., Drake,T.A. and Lusis,A.J.
  TITLE     Genetic and genomic analysis of a fat mass trait with complex
            inheritance reveals marked sex specificity
  JOURNAL   PLoS Genet 2 (2), e15 (2006)
   PUBMED   16462940
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Choudhary,D., Jansson,I., Schenkman,J.B., Sarfarazi,M. and
            Stoilov,I.
  TITLE     Comparative expression profiling of 40 mouse cytochrome P450 genes
            in embryonic and adult tissues
  JOURNAL   Arch Biochem Biophys 414 (1), 91-100 (2003)
   PUBMED   12745259
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Tsao,C.C., Foley,J., Coulter,S.J., Maronpot,R., Zeldin,D.C. and
            Goldstein,J.A.
  TITLE     CYP2C40, a unique arachidonic acid 16-hydroxylase, is the major
            CYP2C in murine intestinal tract
  JOURNAL   Mol Pharmacol 58 (2), 279-287 (2000)
   PUBMED   10908295
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Luo,G., Zeldin,D.C., Blaisdell,J.A., Hodgson,E. and Goldstein,J.A.
  TITLE     Cloning and expression of murine CYP2Cs and their ability to
            metabolize arachidonic acid
  JOURNAL   Arch Biochem Biophys 357 (1), 45-57 (1998)
   PUBMED   9721182
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC121935.3.
            
            On Mar 8, 2019 this sequence version replaced NP_034134.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF047727.1, BC139471.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 34.24 cM"
     Protein         1..491
                     /product="cytochrome P450 2C40 precursor"
                     /EC_number="1.14.14.1"
                     /note="cytochrome P450 2C40; CYPIIC40; cytochrome P450,
                     2c40"
                     /calculated_mol_wt=52875
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P56657.2)"
                     /calculated_mol_wt=2907
     mat_peptide     26..491
                     /product="Cytochrome P450 2C40. /evidence=ECO:0000255.
                     /id=PRO_0000051723"
                     /note="propagated from UniProtKB/Swiss-Prot (P56657.2)"
                     /calculated_mol_wt=52875
     Region          61..485
                     /region_name="CYP2C-like"
                     /note="cytochrome P450 family 2, subfamily C, and similar
                     cytochrome P450s; cd20665"
                     /db_xref="CDD:410758"
     Site            order(97,112..113,120,124,294,297..298,301..302,305,356,
                     361..362,365..366,368,427..429,433,435..437,441,444)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410758"
     Site            order(108,113..114,204..205,208,214,233,237,240,292..293,
                     296..297,300..301,362,366,476..477)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410758"
     CDS             1..491
                     /gene="Cyp2c40"
                     /coded_by="NM_010004.3:93..1568"
                     /db_xref="CCDS:CCDS29798.3"
                     /db_xref="GeneID:13099"
                     /db_xref="MGI:MGI:1306815"
ORIGIN      
        1 mdpfvvlvlc lsfllvlslw rqrsargnlp pgptplpiig nyhlidmkdi gqcltnfskt
       61 ygpvftlyfg sqpivvlhgy eaikealidh geefsgrgri pvfdkvstgk gigfshgnvw
      121 katrvftvnt lrnlgmgkrt ienkvqeeaq wlmkelkktn gspcdpqfii gcapcnvics
      181 ivfqnrfdyk dkdflsligk vnecteilss pgcqifnavp ilidycpgsh nklfknhtwi
      241 ksyllgkike heesldvtnp rdfidyfliq rrqkngiehm dytiehlatl vtdlvfggte
      301 tlsstmrfal lllmkhthit akvqeeidnv igrhrspcmq drnhmpytna mvhevqryid
      361 lgpngvvhev tcdtkfrnyf ipkgtqvmts ltsvlhdste fpnpevfdpg hflddngnfk
      421 ksdyfvpfsa gkricvgesl armelflflt tilqnfklkp lvdpkdidmt pkhsgfskip
      481 pnfqmcfipv e
//
LOCUS       NP_000478                509 aa            linear   PRI 27-APR-2025
DEFINITION  arylsulfatase A isoform a precursor [Homo sapiens].
ACCESSION   NP_000478
VERSION     NP_000478.3
DBSOURCE    REFSEQ: accession NM_000487.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Li,T., Huang,Y., Tao,C., Yin,X., Su,X., Shao,Y., Liang,C.,
            Jiang,M., Cai,Y., Lin,Y., Zeng,C., Zhao,X., Liu,L. and Zhang,W.
  TITLE     Biochemical and molecular analysis of pediatric patients with
            metachromatic leukodystrophy in South China: functional
            characterization of five novel ARSA variants
  JOURNAL   Metab Brain Dis 39 (5), 753-762 (2024)
   PUBMED   38775997
  REMARK    GeneRIF: Biochemical and molecular analysis of pediatric patients
            with metachromatic leukodystrophy in South China: functional
            characterization of five novel ARSA variants.
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Mir,Y.R., Agrahari,A.K., Hassan,A., Choudhary,A., Asthana,S.,
            Taneja,A.K., Nawaz,S., Ilyas,M., Scotti,C. and Kuchay,R.A.H.
  TITLE     Identification and structural characterization of a pathogenic ARSA
            missense variant in two consanguineous families from Jammu and
            Kashmir (India) with late infantile metachromatic leukodystrophy
  JOURNAL   Mol Biol Rep 51 (1), 30 (2023)
   PUBMED   38153581
  REMARK    GeneRIF: Identification and structural characterization of a
            pathogenic ARSA missense variant in two consanguineous families
            from Jammu and Kashmir (India) with late infantile metachromatic
            leukodystrophy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Senkevich,K., Beletskaia,M., Dworkind,A., Yu,E., Ahmad,J.,
            Ruskey,J.A., Asayesh,F., Spiegelman,D., Fahn,S., Waters,C.,
            Monchi,O., Dauvilliers,Y., Dupre,N., Greenbaum,L., Hassin-Baer,S.,
            Nagornov,I., Tyurin,A., Miliukhina,I., Timofeeva,A., Emelyanov,A.,
            Trempe,J.F., Zakharova,E., Alcalay,R.N., Pchelina,S. and Gan-Or,Z.
  TITLE     Association of Rare Variants in ARSA with Parkinson's Disease
  JOURNAL   Mov Disord 38 (10), 1806-1812 (2023)
   PUBMED   37381728
  REMARK    GeneRIF: Association of Rare Variants in ARSA with Parkinson's
            Disease.
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Abtahi,R., Karimzadeh,P., Rezayi,A., Salehpour,S., Akbarzadeh,D.,
            Tonekaboni,S.H., Emameh,R.Z. and Houshmand,M.
  TITLE     Analysis of the HEXA, HEXB, ARSA, and SMPD1 Genes in 68 Iranian
            Patients
  JOURNAL   J Mol Neurosci 72 (3), 555-564 (2022)
   PUBMED   34554397
  REMARK    GeneRIF: Analysis of the HEXA, HEXB, ARSA, and SMPD1 Genes in 68
            Iranian Patients.
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Gomez-Ospina,N.
  TITLE     Arylsulfatase A Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301309
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Fujii,T., Kobayashi,T., Honke,K., Gasa,S., Ishikawa,M., Shimizu,T.
            and Makita,A.
  TITLE     Proteolytic processing of human lysosomal arylsulfatase A
  JOURNAL   Biochim Biophys Acta 1122 (1), 93-98 (1992)
   PUBMED   1352993
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Narahara,K., Takahashi,Y., Murakami,M., Tsuji,K., Yokoyama,Y.,
            Murakami,R., Ninomiya,S. and Seino,Y.
  TITLE     Terminal 22q deletion associated with a partial deficiency of
            arylsulphatase A
  JOURNAL   J Med Genet 29 (6), 432-433 (1992)
   PUBMED   1352356
  REMARK    Review article
REFERENCE   10 (residues 1 to 509)
  AUTHORS   DeLuca,C., Brown,J.A. and Shows,T.B.
  TITLE     Lysosomal arylsulfatase deficiencies in humans: chromosome
            assignments for arylsulfatase A and B
  JOURNAL   Proc Natl Acad Sci U S A 76 (4), 1957-1961 (1979)
   PUBMED   36611
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301098.1, AB448736.1,
            U62317.2 and BQ184813.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 4, 2010 this sequence version replaced NP_000478.2.
            
            Summary: The protein encoded by this gene hydrolyzes cerebroside
            sulfate to cerebroside and sulfate. Defects in this gene lead to
            metachromatic leucodystrophy (MLD), a progressive demyelination
            disease which results in a variety of neurological symptoms and
            ultimately death. Alternatively spliced transcript variants have
            been described for this gene. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and it encodes the longer protein (isoform a). Variants
            1, 2, 3, and 4 encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.21861.1, AB448736.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216124.10/ ENSP00000216124.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..509
                     /product="arylsulfatase A isoform a precursor"
                     /EC_number="3.1.6.8"
                     /note="cerebroside-sulfatase; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=51911
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1913
     mat_peptide     21..509
                     /product="arylsulfatase A isoform a"
                     /calculated_mol_wt=51911
     Region          22..505
                     /region_name="ARSA"
                     /note="Arylsulfatase A or cerebroside-sulfatase; cd16158"
                     /db_xref="CDD:293777"
     Site            order(31..32,71,125,127,152,231,283..284,304..305)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293777"
     Site            order(71,125,127,152,231,304..305)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293777"
     CDS             1..509
                     /gene="ARSA"
                     /gene_synonym="ASA; MLD"
                     /coded_by="NM_000487.6:374..1903"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS14100.2"
                     /db_xref="GeneID:410"
                     /db_xref="HGNC:HGNC:713"
                     /db_xref="MIM:607574"
ORIGIN      
        1 msmgaprsll lalaaglava rppnivlifa ddlgygdlgc yghpssttpn ldqlaagglr
       61 ftdfyvpvsl ctpsraallt grlpvrmgmy pgvlvpssrg glpleevtva evlaargylt
      121 gmagkwhlgv gpegaflpph qgfhrflgip yshdqgpcqn ltcfppatpc dggcdqglvp
      181 ipllanlsve aqppwlpgle arymafahdl madaqrqdrp fflyyashht hypqfsgqsf
      241 aersgrgpfg dslmeldaav gtlmtaigdl glleetlvif tadngpetmr msrggcsgll
      301 rcgkgttyeg gvrepalafw pghiapgvth elassldllp tlaalagapl pnvtldgfdl
      361 splllgtgks prqslffyps ypdevrgvfa vrtgkykahf ftqgsahsdt tadpachass
      421 sltaheppll ydlskdpgen ynllggvaga tpevlqalkq lqllkaqlda avtfgpsqva
      481 rgedpalqic chpgctprpa cchcpdpha
//
LOCUS       NP_078863                277 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 53 isoform 1 [Homo sapiens].
ACCESSION   NP_078863
VERSION     NP_078863.2
DBSOURCE    REFSEQ: accession NM_024587.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Guo,L., Iida,A., Bhavani,G.S., Gowrishankar,K., Wang,Z., Xue,J.Y.,
            Wang,J., Miyake,N., Matsumoto,N., Hasegawa,T., Iizuka,Y.,
            Matsuda,M., Nakashima,T., Takechi,M., Iseki,S., Yambe,S.,
            Nishimura,G., Koseki,H., Shukunami,C., Girisha,K.M. and Ikegawa,S.
  TITLE     Deficiency of TMEM53 causes a previously unknown sclerosing bone
            disorder by dysregulation of BMP-SMAD signaling
  JOURNAL   Nat Commun 12 (1), 2046 (2021)
   PUBMED   33824347
  REMARK    GeneRIF: Deficiency of TMEM53 causes a previously unknown
            sclerosing bone disorder by dysregulation of BMP-SMAD signaling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY108001.1, BC064520.1 and BM675039.1.
            
            On Feb 22, 2004 this sequence version replaced NP_078863.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.147921.1,
                                           SRR1660809.150841.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153307, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372237.8/ ENSP00000361311.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..277
                     /product="transmembrane protein 53 isoform 1"
                     /note="novel DUF829 domain-containing protein; nuclear
                     envelope transmembrane protein 4"
                     /calculated_mol_wt=31499
     Region          36..271
                     /region_name="DUF829"
                     /note="Eukaryotic protein of unknown function (DUF829);
                     pfam05705"
                     /db_xref="CDD:461719"
     Site            171..191
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2H8.1)"
     CDS             1..277
                     /gene="TMEM53"
                     /gene_synonym="CTDI; NET4"
                     /coded_by="NM_024587.4:91..924"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS511.1"
                     /db_xref="GeneID:79639"
                     /db_xref="HGNC:HGNC:26186"
                     /db_xref="MIM:619722"
ORIGIN      
        1 masaeldyti eipdqpcwsq knspspggke aetrqpvvil lgwggckdkn lakysaiyhk
       61 rgciviryta pwhmvffses lgipslrvla qkllellfdy eiekepllfh vfsnggvmly
      121 ryvlellqtr rfcrlrvvgt ifdsapgdsn lvgalralaa ilerraamlr llllvafalv
      181 vvlfhvllap italfhthfy drlqdagsrw pelylysrad evvlardier mvearlarrv
      241 larsvdfvss ahvshlrdyp tyytslcvdf mrncvrc
//
LOCUS       NP_001341859             671 aa            linear   PRI 27-APR-2025
DEFINITION  receptor-interacting serine/threonine-protein kinase 1 isoform 1
            [Homo sapiens].
ACCESSION   NP_001341859 XP_005249514
VERSION     NP_001341859.1
DBSOURCE    REFSEQ: accession NM_001354930.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Mannion,J., Gifford,V., Bellenie,B., Fernando,W., Ramos Garcia,L.,
            Wilson,R., John,S.W., Udainiya,S., Patin,E.C., Tiu,C., Smith,A.,
            Goicoechea,M., Craxton,A., Moraes de Vasconcelos,N., Guppy,N.,
            Cheung,K.J., Cundy,N.J., Pierrat,O., Brennan,A., Roumeliotis,T.I.,
            Benstead-Hume,G., Alexander,J., Muirhead,G., Layzell,S., Lyu,W.,
            Roulstone,V., Allen,M., Baldock,H., Legrand,A., Gabel,F.,
            Serrano-Aparicio,N., Starling,C., Guo,H., Upton,J., Gyrd-Hansen,M.,
            MacFarlane,M., Seddon,B., Raynaud,F., Roxanis,I., Harrington,K.,
            Haider,S., Choudhary,J.S., Hoelder,S., Tenev,T. and Meier,P.
  TITLE     A RIPK1-specific PROTAC degrader achieves potent antitumor activity
            by enhancing immunogenic cell death
  JOURNAL   Immunity 57 (7), 1514-1532 (2024)
   PUBMED   38788712
  REMARK    GeneRIF: A RIPK1-specific PROTAC degrader achieves potent antitumor
            activity by enhancing immunogenic cell death.
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Jin,X., Zhang,Y., Zhou,Y., Luo,Y., Han,X., Gao,Y., Yu,H., Duan,Y.,
            Shi,L., Wu,Y. and Li,Y.
  TITLE     Sirt1 Deficiency Promotes Age-Related AF Through Enhancing Atrial
            Necroptosis by Activation of RIPK1 Acetylation
  JOURNAL   Circ Arrhythm Electrophysiol 17 (7), e012452 (2024)
   PUBMED   39012929
  REMARK    GeneRIF: Sirt1 Deficiency Promotes Age-Related AF Through Enhancing
            Atrial Necroptosis by Activation of RIPK1 Acetylation.
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Yang,M., Wei,Y., He,X. and Xia,C.
  TITLE     The deubiquitinating protein OTUD6B promotes lung adenocarcinoma
            progression by stabilizing RIPK1
  JOURNAL   Biol Direct 19 (1), 46 (2024)
   PUBMED   38880876
  REMARK    GeneRIF: The deubiquitinating protein OTUD6B promotes lung
            adenocarcinoma progression by stabilizing RIPK1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Damhofer,H., Tatar,T., Southgate,B., Scarneo,S., Agger,K.,
            Shlyueva,D., Uhrbom,L., Morrison,G.M., Hughes,P.F., Haystead,T.,
            Pollard,S.M. and Helin,K.
  TITLE     TAK1 inhibition leads to RIPK1-dependent apoptosis in
            immune-activated cancers
  JOURNAL   Cell Death Dis 15 (4), 273 (2024)
   PUBMED   38632238
  REMARK    GeneRIF: TAK1 inhibition leads to RIPK1-dependent apoptosis in
            immune-activated cancers.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Lee,Y.M. and Vucic,D.
  TITLE     The role of autophagy in RIP1 mediated cell death and intestinal
            inflammation
  JOURNAL   Adv Immunol 163, 1-20 (2024)
   PUBMED   39271257
  REMARK    GeneRIF: The role of autophagy in RIP1 mediated cell death and
            intestinal inflammation.
            Review article
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Silke,J., Rickard,J.A. and Gerlic,M.
  TITLE     The diverse role of RIP kinases in necroptosis and inflammation
  JOURNAL   Nat Immunol 16 (7), 689-697 (2015)
   PUBMED   26086143
  REMARK    GeneRIF: Studies indicate that RIP kinases RIPK1 and RIPK3 directly
            regulate inflammatory signaling.
            Review article
            Erratum:[Nat Immunol. 2015 Aug;16(8):889. doi: 10.1038/ni0815-889b.
            PMID: 26194288]
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Takeuchi,M., Rothe,M. and Goeddel,D.V.
  TITLE     Anatomy of TRAF2. Distinct domains for nuclear factor-kappaB
            activation and association with tumor necrosis factor signaling
            proteins
  JOURNAL   J Biol Chem 271 (33), 19935-19942 (1996)
   PUBMED   8702708
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Hsu,H., Huang,J., Shu,H.B., Baichwal,V. and Goeddel,D.V.
  TITLE     TNF-dependent recruitment of the protein kinase RIP to the TNF
            receptor-1 signaling complex
  JOURNAL   Immunity 4 (4), 387-396 (1996)
   PUBMED   8612133
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Hsu,H., Xiong,J. and Goeddel,D.V.
  TITLE     The TNF receptor 1-associated protein TRADD signals cell death and
            NF-kappa B activation
  JOURNAL   Cell 81 (4), 495-504 (1995)
   PUBMED   7758105
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Stanger,B.Z., Leder,P., Lee,T.H., Kim,E. and Seed,B.
  TITLE     RIP: a novel protein containing a death domain that interacts with
            Fas/APO-1 (CD95) in yeast and causes cell death
  JOURNAL   Cell 81 (4), 513-523 (1995)
   PUBMED   7538908
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031963.40.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 30, 2017 this sequence version replaced XP_005249514.2.
            
            Summary: This gene encodes a member of the receptor-interacting
            protein (RIP) family of serine/threonine protein kinases. The
            encoded protein plays a role in inflammation and cell death in
            response to tissue damage, pathogen recognition, and as part of
            developmental regulation. RIPK1/RIPK3 kinase-mediated necrosis is
            referred to as necroptosis. Genetic disruption of this gene in mice
            results in death shortly after birth. [provided by RefSeq, Aug
            2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.265177.1,
                                           SRR1660803.229431.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259808.9/ ENSP00000259808.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p25.2"
     Protein         1..671
                     /product="receptor-interacting serine/threonine-protein
                     kinase 1 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="receptor-interacting serine/threonine-protein
                     kinase 1; serine/threonine-protein kinase RIP; cell death
                     protein RIP; receptor-interacting protein 1; receptor
                     (TNFRSF)-interacting serine-threonine kinase 1;
                     receptor-interacting protein kinase 1"
                     /calculated_mol_wt=75800
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA and IKKB.
                     /evidence=ECO:0000269|PubMed:18408713; propagated from
                     UniProtKB/Swiss-Prot (Q13546.3)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13546.3)"
     Region          23..290
                     /region_name="STKc_RIP1"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Receptor Interacting Protein 1; cd14027"
                     /db_xref="CDD:270929"
     Site            order(23..27,31,43,45,76,92..95,99,101,138,140,142..143,
                     145,156,159,188..191)
                     /site_type="active"
                     /db_xref="CDD:270929"
     Site            order(23..27,31,43,45,76,92..95,99,138,140,142..143,145,
                     156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270929"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA and IKKB.
                     /evidence=ECO:0000269|PubMed:18408713,
                     ECO:0000269|PubMed:30988283; propagated from
                     UniProtKB/Swiss-Prot (Q13546.3)"
     Site            order(27,99,101,138,140,142,159,188..191)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270929"
     Site            order(45,64,67..68,70,75..76,78,90,92,129,134,136,
                     154..157,159,161..162,165)
                     /site_type="other"
                     /note="Necrostatin binding site [chemical binding]"
                     /db_xref="CDD:270929"
     Site            155..191
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270929"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RIPK3 and autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13546.3)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:29440439,
                     ECO:0000269|PubMed:31827280; propagated from
                     UniProtKB/Swiss-Prot (Q13546.3)"
     Region          290..582
                     /region_name="Interaction with SQSTM1.
                     /evidence=ECO:0000269|PubMed:10356400"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13546.3)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18408713; propagated from
                     UniProtKB/Swiss-Prot (Q13546.3)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K7.
                     /evidence=ECO:0000269|PubMed:18408713,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13546.3)"
     Site            324..325
                     /site_type="cleavage"
                     /note="Cleavage, by CASP8.
                     /evidence=ECO:0000269|PubMed:10521396,
                     ECO:0000269|PubMed:31827280, ECO:0000269|PubMed:31827281;
                     propagated from UniProtKB/Swiss-Prot (Q13546.3)"
     Region          331..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13546.3)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K7.
                     /evidence=ECO:0000250|UniProtKB:Q60855; propagated from
                     UniProtKB/Swiss-Prot (Q13546.3)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K7.
                     /evidence=ECO:0000269|PubMed:18408713; propagated from
                     UniProtKB/Swiss-Prot (Q13546.3)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (Q13546.3)"
     Region          389..455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13546.3)"
     Region          531..547
                     /region_name="RIP homotypic interaction motif (RHIM).
                     /evidence=ECO:0000269|PubMed:11734559,
                     ECO:0000269|PubMed:29681455"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13546.3)"
     Region          583..668
                     /region_name="Death_RIP1"
                     /note="Death Domain of Receptor-Interacting Protein 1;
                     cd08777"
                     /db_xref="CDD:260048"
     Site            603
                     /site_type="glycosylation"
                     /note="(Microbial infection) N-beta-linked (GlcNAc)
                     arginine. /evidence=ECO:0000269|PubMed:30979585,
                     ECO:0000305|PubMed:23955153, ECO:0007744|PDB:6AC5;
                     propagated from UniProtKB/Swiss-Prot (Q13546.3)"
     CDS             1..671
                     /gene="RIPK1"
                     /gene_synonym="AIEFL; IMD57; RIP; RIP-1; RIP1"
                     /coded_by="NM_001354930.2:229..2244"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS4482.1"
                     /db_xref="GeneID:8737"
                     /db_xref="HGNC:HGNC:10019"
                     /db_xref="MIM:603453"
ORIGIN      
        1 mqpdmslnvi kmkssdfles aeldsggfgk vslcfhrtqg lmimktvykg pnciehneal
       61 leeakmmnrl rhsrvvkllg viieegkysl vmeymekgnl mhvlkaemst plsvkgriil
      121 eiiegmcylh gkgvihkdlk penilvdndf hikiadlgla sfkmwsklnn eehnelrevd
      181 gtakknggtl yymapehlnd vnakpteksd vysfavvlwa ifankepyen aiceqqlimc
      241 iksgnrpdvd diteycprei islmklcwea npearptfpg ieekfrpfyl sqleesveed
      301 vkslkkeysn enavvkrmqs lqldcvavps srsnsateqp gslhssqglg mgpveeswfa
      361 pslehpqeen epslqsklqd eanyhlygsr mdrqtkqqpr qnvaynreee rrrrvshdpf
      421 aqqrpyenfq ntegkgtays saashgnavh qpsgltsqpq vlyqnnglys shgfgtrpld
      481 pgtagprvwy rpipshmpsl hnipvpetny lgntptmpfs slpptdesik ytiynstgiq
      541 igaynymeig gtssslldst ntnfkeepaa kyqaifdntt sltdkhldpi renlgkhwkn
      601 carklgftqs qideidhdye rdglkekvyq mlqkwvmreg ikgatvgkla qalhqcsrid
      661 llssliyvsq n
//
LOCUS       NP_001019764             460 aa            linear   PRI 27-APR-2025
DEFINITION  putative protein MSS51 homolog, mitochondrial [Homo sapiens].
ACCESSION   NP_001019764
VERSION     NP_001019764.1
DBSOURCE    REFSEQ: accession NM_001024593.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Jiao,Y.Y., Song,N., Fang,X.Y., Lu,X.T., Sun,N., Jin,H.X., Chen,L.,
            Huang,X.J., Wen,S., Wu,Z.T., Wang,X.P., Cheng,T.T., Yao,G.D. and
            Song,W.Y.
  TITLE     YTHDF2 regulates MSS51 expression contributing to mitochondria
            dysfunction of granulosa cells in polycystic ovarian syndrome
            patients
  JOURNAL   Mol Cell Endocrinol 592, 112292 (2024)
   PUBMED   38830447
  REMARK    GeneRIF: YTHDF2 regulates MSS51 expression contributing to
            mitochondria dysfunction of granulosa cells in polycystic ovarian
            syndrome patients.
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Baleva,M.V., Piunova,U.E., Chicherin,I.V., Krasavina,D.G.,
            Levitskii,S.A. and Kamenski,P.A.
  TITLE     Yeast Translational Activator Mss51p and Human ZMYND17 - Two
            Proteins with a Common Origin, but Different Functions
  JOURNAL   Biochemistry (Mosc) 86 (9), 1151-1161 (2021)
   PUBMED   34565318
  REMARK    GeneRIF: Yeast Translational Activator Mss51p and Human ZMYND17 -
            Two Proteins with a Common Origin, but Different Functions.
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Liu,C.M., Fann,C.S., Chen,C.Y., Liu,Y.L., Oyang,Y.J., Yang,W.C.,
            Chang,C.C., Wen,C.C., Chen,W.J., Hwang,T.J., Hsieh,M.H., Liu,C.C.,
            Faraone,S.V., Tsuang,M.T. and Hwu,H.G.
  TITLE     ANXA7, PPP3CB, DNAJC9, and ZMYND17 genes at chromosome 10q22
            associated with the subgroup of schizophrenia with deficits in
            attention and executive function
  JOURNAL   Biol Psychiatry 70 (1), 51-58 (2011)
   PUBMED   21531385
  REMARK    GeneRIF: ANXA7, PPP3CB, DNAJC9, and ZMYND17 genes are potential
            candidate genes for schizophrenia, especially in patients with
            deficits in sustained attention and executive function.
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Perez-Martinez,X., Butler,C.A., Shingu-Vazquez,M. and Fox,T.D.
  TITLE     Dual functions of Mss51 couple synthesis of Cox1 to assembly of
            cytochrome c oxidase in Saccharomyces cerevisiae mitochondria
  JOURNAL   Mol Biol Cell 20 (20), 4371-4380 (2009)
   PUBMED   19710419
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX500736.1, BC094693.1 and CN395159.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094693.1, SRR1803615.197425.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000299432.7/
                                                  ENSP00000299432.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..460
                     /product="putative protein MSS51 homolog, mitochondrial"
                     /note="zinc finger, MYND domain containing 17; zinc finger
                     MYND domain-containing protein 17; zinc finger, MYND-type
                     containing 17; MSS51 mitochondrial translational activator
                     homolog"
                     /calculated_mol_wt=51158
     Region          105..149
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          243..423
                     /region_name="MSS51_C"
                     /note="MSS51 C-terminal domain; pfam20179"
                     /db_xref="CDD:466330"
     CDS             1..460
                     /gene="MSS51"
                     /gene_synonym="ZMYND17"
                     /coded_by="NM_001024593.2:67..1449"
                     /db_xref="CCDS:CCDS31221.1"
                     /db_xref="GeneID:118490"
                     /db_xref="HGNC:HGNC:21000"
                     /db_xref="MIM:614773"
ORIGIN      
        1 maprsrrrrh kkppssvapi imapttivtp vpltpskpgp sidtlgffsl ddnvpglsql
       61 ilqklnmksy eeyklvvdgg tpvsgfgfrc pqemfqrmed tfrfcahcra lpsglsdskv
      121 lrhckrcrnv yycgpecqks dwpahrrvcq elrlvavdrl mewllvtgdf vlpsgpwpwp
      181 peavqdwdsw fsmkglhlda tldavlvsha vttlwasvgr prpdpdvlqg slkrlltdvl
      241 srpltlglgl ralgidvrrt ggstvhvvga shvetfltrp gdydelgymf pghlglrvvm
      301 vgvdvatgfs qststsplep gtiqlsahrg lyhdfweeqv etgqthhpdl vaafhpgfhs
      361 spdlmeawlp tllllrdyki ptlitvyshq elvsslqilv eldthitafg snpfmslkpe
      421 qvysspnkqp vycsayyimf lgsscqldnr qleekvdggi
//
LOCUS       NP_848930                179 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-ribosylation factor-like protein 5B [Homo sapiens].
ACCESSION   NP_848930
VERSION     NP_848930.1
DBSOURCE    REFSEQ: accession NM_178815.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Houghton,F.J., Makhoul,C., Cho,E.H., Williamson,N.A. and
            Gleeson,P.A.
  TITLE     Interacting partners of Golgi-localized small G protein Arl5b
            identified by a combination of in vivo proximity labelling and
            GFP-Trap pull down
  JOURNAL   FEBS Lett 596 (18), 2382-2399 (2022)
   PUBMED   35789482
  REMARK    GeneRIF: Interacting partners of Golgi-localized small G protein
            Arl5b identified by a combination of in vivo proximity labelling
            and GFP-Trap pull down.
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Zhang,L., Hu,X., Wu,H., Tian,H., Zeng,J., Song,D., Yang,K.,
            Chen,J., Xu,J. and Dong,F.
  TITLE     Knockdown of ARL5B Induces Mitochondrial-mediated Apoptosis and
            Inhibits Glycolysis in Breast Cancer Cells by Activating MDA5
            Signaling
  JOURNAL   Curr Cancer Drug Targets 22 (10), 843-853 (2022)
   PUBMED   35546774
  REMARK    GeneRIF: Knockdown of ARL5B Induces Mitochondrial-mediated
            Apoptosis and Inhibits Glycolysis in Breast Cancer Cells by
            Activating MDA5 Signaling.
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Jaimon,E., Tripathi,A., Khurana,A., Ghosh,D., Sugatha,J. and
            Datta,S.
  TITLE     Binding with heat shock cognate protein HSC70 fine-tunes the Golgi
            association of the small GTPase ARL5B
  JOURNAL   J Biol Chem 297 (6), 101422 (2021)
   PUBMED   34798070
  REMARK    GeneRIF: Binding with heat shock cognate protein HSC70 fine-tunes
            the Golgi association of the small GTPase ARL5B.
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Zhao,S., Zhang,Y., Pei,M., Wu,L. and Li,J.
  TITLE     miR-145 inhibits mitochondrial function of ovarian cancer by
            targeting ARL5B
  JOURNAL   J Ovarian Res 14 (1), 8 (2021)
   PUBMED   33419459
  REMARK    GeneRIF: miR-145 inhibits mitochondrial function of ovarian cancer
            by targeting ARL5B.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Aouizerat,B.E., Vittinghoff,E., Musone,S.L., Pawlikowska,L.,
            Kwok,P.Y., Olgin,J.E. and Tseng,Z.H.
  TITLE     GWAS for discovery and replication of genetic loci associated with
            sudden cardiac arrest in patients with coronary artery disease
  JOURNAL   BMC Cardiovasc Disord 11, 29 (2011)
   PUBMED   21658281
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Han,M.R., Schellenberg,G.D. and Wang,L.S.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     Genome-wide association reveals genetic effects on human Abeta42
            and tau protein levels in cerebrospinal fluids: a case control
            study
  JOURNAL   BMC Neurol 10, 90 (2010)
   PUBMED   20932310
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Sebald,E., Krueger,R., King,L.M., Cohn,D.H. and Krakow,D.
  TITLE     Isolation of a new member of the ADP-ribosylation like factor gene
            family, ARL8, from a cartilage cDNA library
  JOURNAL   Gene 311, 147-151 (2003)
   PUBMED   12853149
  REMARK    GeneRIF: ARL8 contains six exons and five introns, and encodes a
            179 amino acid protein that shares homology to the other ARL
            proteins.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL512641.9 and AL133611.1.
            
            Summary: ARL5B (ARL8) belongs to a family of proteins that are
            structurally similar to ADP-ribosylation factors (ARFs; see MIM
            103180). ARLs and ARFs are part of the RAS superfamily of
            regulatory GTPases.[supplied by OMIM, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027275.1, SRR1660803.160272.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377275.4/ ENSP00000366487.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.31"
     Protein         1..179
                     /product="ADP-ribosylation factor-like protein 5B"
                     /note="ADP-ribosylation factor-like 8;
                     ADP-ribosylation-like factor 8; ADP-ribosylation
                     factor-like 5B; ADP-ribosylation factor-like protein 8;
                     ADP ribosylation factor like GTPase 5B"
                     /calculated_mol_wt=20244
     Region          3..175
                     /region_name="Arl5_Arl8"
                     /note="Arf-like 5 (Arl5) and 8 (Arl8) GTPases; cd04153"
                     /db_xref="CDD:133353"
     Site            23..30
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133353"
     Site            order(25..31,125..126,128,158..159)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133353"
     Site            order(25..26,30,34,46..53,75,80)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133353"
     Site            35..50
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133353"
     Site            order(47..51,56,66,70,76,78..80)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133353"
     Site            47
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133353"
     Site            order(48..55,65,76,79..80)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133353"
     Site            order(51..57,60..65)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:133353"
     Site            66..83
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133353"
     Site            66..69
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133353"
     Site            125..128
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133353"
     Site            158..160
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133353"
     CDS             1..179
                     /gene="ARL5B"
                     /gene_synonym="ARL8"
                     /coded_by="NM_178815.5:208..747"
                     /db_xref="CCDS:CCDS7131.1"
                     /db_xref="GeneID:221079"
                     /db_xref="HGNC:HGNC:23052"
                     /db_xref="MIM:608909"
ORIGIN      
        1 mglifaklws lfcnqehkvi ivgldnagkt tilyqflmne vvhtsptigs nveeivvknt
       61 hflmwdiggq eslrsswnty ysntefiilv vdsidrerla itkeelyrml ahedlrkaav
      121 lifankqdmk gcmtaaeisk yltlssikdh pwhiqsccal tgeglcqgle wmtsrigvr
//
LOCUS       NP_001348931              88 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 1 [Mus musculus].
ACCESSION   NP_001348931
VERSION     NP_001348931.1
DBSOURCE    REFSEQ: accession NM_001362002.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 88)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 88)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 88)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 88)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7.
            
            Transcript Variant: This variant (12), as well as variants 1, 8-11,
            and 13-19, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.107398.1,
                                           SRR1660813.114148.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..88
                     /product="cAMP-regulated phosphoprotein 21 isoform 1"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=9408
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q7M2N1; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10854908,
                     ECO:0000269|PubMed:15499021; propagated from
                     UniProtKB/Swiss-Prot (Q9DCB4.2)"
     CDS             1..88
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362002.1:474..740"
                     /note="isoform 1 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS40786.1"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqtl
//
LOCUS       NP_001972                896 aa            linear   PRI 27-APR-2025
DEFINITION  epidermal growth factor receptor substrate 15 isoform A [Homo
            sapiens].
ACCESSION   NP_001972
VERSION     NP_001972.1
DBSOURCE    REFSEQ: accession NM_001981.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 896)
  AUTHORS   Wang,Q., Hou,K., Yang,J., Li,H., Li,C., Zhang,Y., Tian,J., Li,C.,
            Guo,B., Jia,S. and Luo,Y.
  TITLE     Modified iPOND revealed the role of mutant p53 in promoting
            helicase function and telomere maintenance
  JOURNAL   Aging (Albany NY) 15 (19), 10767-10784 (2023)
   PUBMED   37827695
  REMARK    GeneRIF: Modified iPOND revealed the role of mutant p53 in
            promoting helicase function and telomere maintenance.
REFERENCE   2  (residues 1 to 896)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   3  (residues 1 to 896)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 896)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 896)
  AUTHORS   Yang,S., Li,L., Chen,D., Xiao,M. and Xian,L.
  TITLE     EPS15-NTRK1: a novel NTRK1 oncogenic fusion in patient with lung
            adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 146 (12), 3389-3392 (2020)
   PUBMED   33037466
  REMARK    GeneRIF: EPS15-NTRK1: a novel NTRK1 oncogenic fusion in patient
            with lung adenocarcinoma.
REFERENCE   6  (residues 1 to 896)
  AUTHORS   Matsuda,M., Ota,S., Tanimura,R., Nakamura,H., Matuoka,K.,
            Takenawa,T., Nagashima,K. and Kurata,T.
  TITLE     Interaction between the amino-terminal SH3 domain of CRK and its
            natural target proteins
  JOURNAL   J Biol Chem 271 (24), 14468-14472 (1996)
   PUBMED   8662907
REFERENCE   7  (residues 1 to 896)
  AUTHORS   Benmerah,A., Begue,B., Dautry-Varsat,A. and Cerf-Bensussan,N.
  TITLE     The ear of alpha-adaptin interacts with the COOH-terminal domain of
            the Eps 15 protein
  JOURNAL   J Biol Chem 271 (20), 12111-12116 (1996)
   PUBMED   8662627
REFERENCE   8  (residues 1 to 896)
  AUTHORS   Schumacher,C., Knudsen,B.S., Ohuchi,T., Di Fiore,P.P.,
            Glassman,R.H. and Hanafusa,H.
  TITLE     The SH3 domain of Crk binds specifically to a conserved
            proline-rich motif in Eps15 and Eps15R
  JOURNAL   J Biol Chem 270 (25), 15341-15347 (1995)
   PUBMED   7797522
REFERENCE   9  (residues 1 to 896)
  AUTHORS   Wong,W.T., Kraus,M.H., Carlomagno,F., Zelano,A., Druck,T.,
            Croce,C.M., Huebner,K. and Di Fiore,P.P.
  TITLE     The human eps15 gene, encoding a tyrosine kinase substrate, is
            conserved in evolution and maps to 1p31-p32
  JOURNAL   Oncogene 9 (6), 1591-1597 (1994)
   PUBMED   8183552
REFERENCE   10 (residues 1 to 896)
  AUTHORS   Bernard,O.A., Mauchauffe,M., Mecucci,C., Van den Berghe,H. and
            Berger,R.
  TITLE     A novel gene, AF-1p, fused to HRX in t(1;11)(p32;q23), is not
            related to AF-4, AF-9 nor ENL
  JOURNAL   Oncogene 9 (4), 1039-1045 (1994)
   PUBMED   8134107
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z29064.1, CD657119.1 and
            AL671986.7.
            
            Summary: This gene encodes a protein that is part of the EGFR
            pathway. The protein is present at clatherin-coated pits and is
            involved in receptor-mediated endocytosis of EGF. Notably, this
            gene is rearranged with the HRX/ALL/MLL gene in acute myelogeneous
            leukemias. Alternative splicing results in multiple transcript
            variants encoding distinct isoforms. [provided by RefSeq, May
            2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (A). Isoform A mainly
            localizes to clathrin-coated pits at the plasma membrane.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.30770.1,
                                           SRR1803617.23096.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371733.8/ ENSP00000360798.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..896
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..896
                     /product="epidermal growth factor receptor substrate 15
                     isoform A"
                     /note="ALL1 fused gene from chromosome 1; epidermal growth
                     factor receptor substrate 15; protein AF-1p"
                     /calculated_mol_wt=98525
     Region          2..330
                     /region_name="Interaction with DAB2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Region          13..103
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P42566.2)"
     Region          121..215
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P42566.2)"
     Region          218..313
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Region          330..>493
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P42566.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P42566.2)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Region          542..606
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42567; propagated from
                     UniProtKB/Swiss-Prot (P42566.2)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42567; propagated from
                     UniProtKB/Swiss-Prot (P42566.2)"
     Region          599..827
                     /region_name="15 X 3 AA repeats of D-P-F"
                     /note="propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42566.2)"
     Region          760..848
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Region          768..774
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Site            777
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P42566.2)"
     Site            779
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P42567; propagated from
                     UniProtKB/Swiss-Prot (P42566.2)"
     Site            790
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Site            796
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P42566.2)"
     Site            849
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by EGFR.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P42566.2)"
     CDS             1..896
                     /gene="EPS15"
                     /gene_synonym="AF-1P; AF1P; MLLT5"
                     /coded_by="NM_001981.3:36..2726"
                     /note="isoform A is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS557.1"
                     /db_xref="GeneID:2060"
                     /db_xref="HGNC:HGNC:3419"
                     /db_xref="MIM:600051"
ORIGIN      
        1 maaaaqlslt qlssgnpvye kyyrqvdtgn tgrvlasdaa aflkksglpd lilgkiwdla
       61 dtdgkgilnk qeffvalrlv acaqnglevs lsslnlavpp prfhdtsspl lisgtsaael
      121 pwavkpedka kydaifdsls pvngflsgdk vkpvllnskl pvdilgrvwe lsdidhdgml
      181 drdefavamf lvycalekep vpmslppalv ppskrktwvv spaekakyde iflktdkdmd
      241 gfvsglevre iflktglpst llahiwslcd tkdcgklskd qfalafhlis qklikgidpp
      301 hvltpemipp sdraslqkni igsspvadfs aikeldtlnn eivdlqrekn nveqdlkeke
      361 dtikqrtsev qdlqdevqre ntnlqklqaq kqqvqellde ldeqkaqlee qlkevrkkca
      421 eeaqlisslk aeltsqesqi styeeelaka reelsrlqqe taeleesves gkaqleplqq
      481 hlqdsqqeis smqmklmemk dlenhnsqln wcssphsilv ngatdycsls tsssetanln
      541 ehvegqsnle sepihqespa rsspellpsg vtdenevtta vtekvcseld nnrhskeedp
      601 fnvdsssltg pvadtnldff qsdpfvgsdp fkddpfgkid pfggdpfkgs dpfasdcffr
      661 qstdpfatss tdpfsaanns sitsvetlkh ndpfapggtv vaasdsatdp fasvfgnesf
      721 gggfadfstl skvnnedpfr satsssvsnv vitknvfeet svksedeppa lppkigtptr
      781 pcplppgkrs inkldspdpf klndpfqpfp gndspkekdp eifcdpftsa ttttnkeadp
      841 snfanfsayp seedmiewak resereeeqr larlnqqeqe dlelaialsk seisea
//
LOCUS       NP_000681                517 aa            linear   PRI 27-APR-2025
DEFINITION  aldehyde dehydrogenase, mitochondrial isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_000681
VERSION     NP_000681.2
DBSOURCE    REFSEQ: accession NM_000690.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Yokoyama,A., Yokoyama,T., Yumoto,Y., Takimura,T., Toyama,T.,
            Yoneda,J., Nishimura,K., Minobe,R., Matsuzaki,T., Kimura,M. and
            Matsushita,S.
  TITLE     Associations of ADH1B and ALDH2 genotypes and alcohol flushing with
            drinking history, withdrawal symptoms, and ICD-10 criteria in
            Japanese alcohol-dependent men
  JOURNAL   Pharmacogenet Genomics 34 (5), 139-148 (2024)
   PUBMED   38465575
  REMARK    GeneRIF: Associations of ADH1B and ALDH2 genotypes and alcohol
            flushing with drinking history, withdrawal symptoms, and ICD-10
            criteria in Japanese alcohol-dependent men.
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Liu,Z.Y., Lin,X.H., Guo,H.Y., Shi,X., Zhang,D.Y., Sun,J.L.,
            Zhang,G.C., Xu,R.C., Wang,F., Yu,X.N., Wang,D., Weng,S.Q.,
            Shen,X.Z., Liu,T.T., Dong,L. and Zhu,J.M.
  TITLE     Multi-Omics profiling identifies aldehyde dehydrogenase 2 as a
            critical mediator in the crosstalk between Treg-mediated
            immunosuppression microenvironment and hepatocellular carcinoma
  JOURNAL   Int J Biol Sci 20 (7), 2763-2778 (2024)
   PUBMED   38725845
  REMARK    GeneRIF: Multi-Omics profiling identifies aldehyde dehydrogenase 2
            as a critical mediator in the crosstalk between Treg-mediated
            immunosuppression microenvironment and hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Wang,X., Wang,J., Chen,Y., Qian,X., Luo,S., Wang,X., Ma,C. and
            Ge,W.
  TITLE     The aldehyde dehydrogenase 2 rs671 variant enhances amyloid beta
            pathology
  JOURNAL   Nat Commun 15 (1), 2594 (2024)
   PUBMED   38519490
  REMARK    GeneRIF: The aldehyde dehydrogenase 2 rs671 variant enhances
            amyloid beta pathology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Liu,R., Peng,M., Zhang,J., Qiu,K., Zeng,T. and Chen,L.
  TITLE     The ALDH2 gene rs671 polymorphism is associated with
            cardiometabolic risk factors in East Asian population: an updated
            meta-analysis
  JOURNAL   Front Endocrinol (Lausanne) 15, 1333595 (2024)
   PUBMED   38567307
  REMARK    GeneRIF: The ALDH2 gene rs671 polymorphism is associated with
            cardiometabolic risk factors in East Asian population: an updated
            meta-analysis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Tokiya,M., Hashimoto,M., Fukuda,K., Kawamoto,K., Akao,C., Tsuji,M.,
            Yakushiji,Y., Koike,H. and Matsumoto,A.
  TITLE     Asian flush gene variant increases mild cognitive impairment risk:
            a cross-sectional study of the Yoshinogari Brain MRI Checkup Cohort
  JOURNAL   Environ Health Prev Med 29, 55 (2024)
   PUBMED   39401906
  REMARK    GeneRIF: Asian flush gene variant increases mild cognitive
            impairment risk: a cross-sectional study of the Yoshinogari Brain
            MRI Checkup Cohort.
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Yoshida,A.
  TITLE     Molecular genetics of human aldehyde dehydrogenase
  JOURNAL   Pharmacogenetics 2 (4), 139-147 (1992)
   PUBMED   1306115
  REMARK    Review article
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Crabb,D.W., Edenberg,H.J., Bosron,W.F. and Li,T.K.
  TITLE     Genotypes for aldehyde dehydrogenase deficiency and alcohol
            sensitivity. The inactive ALDH2(2) allele is dominant
  JOURNAL   J Clin Invest 83 (1), 314-316 (1989)
   PUBMED   2562960
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Hsu,L.C., Bendel,R.E. and Yoshida,A.
  TITLE     Genomic structure of the human mitochondrial aldehyde dehydrogenase
            gene
  JOURNAL   Genomics 2 (1), 57-65 (1988)
   PUBMED   2838413
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Hsu,L.C., Tani,K., Fujiyoshi,T., Kurachi,K. and Yoshida,A.
  TITLE     Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2
  JOURNAL   Proc Natl Acad Sci U S A 82 (11), 3771-3775 (1985)
   PUBMED   2987944
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Greenfield,N.J. and Pietruszko,R.
  TITLE     Two aldehyde dehydrogenases from human liver. Isolation via
            affinity chromatography and characterization of the isozymes
  JOURNAL   Biochim Biophys Acta 483 (1), 35-45 (1977)
   PUBMED   18196
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC353712.1, BC002967.1,
            CB851683.1 and AC003029.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 27, 2002 this sequence version replaced NP_000681.1.
            
            Summary: This protein belongs to the aldehyde dehydrogenase family
            of proteins. Aldehyde dehydrogenase is the second enzyme of the
            major oxidative pathway of alcohol metabolism. Two major liver
            isoforms of aldehyde dehydrogenase, cytosolic and mitochondrial,
            can be distinguished by their electrophoretic mobilities, kinetic
            properties, and subcellular localizations. Most Caucasians have two
            major isozymes, while approximately 50% of East Asians have the
            cytosolic isozyme but not the mitochondrial isozyme. A remarkably
            higher frequency of acute alcohol intoxication among East Asians
            than among Caucasians could be related to the absence of a
            catalytically active form of the mitochondrial isozyme. The
            increased exposure to acetaldehyde in individuals with the
            catalytically inactive form may also confer greater susceptibility
            to many types of cancer. This gene encodes a mitochondrial isoform,
            which has a low Km for acetaldehydes, and is localized in
            mitochondrial matrix. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms.[provided by RefSeq,
            Nov 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.169202.1,
                                           SRR1803612.222503.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000261733.7/
                                                  ENSP00000261733.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.12"
     Protein         1..517
                     /product="aldehyde dehydrogenase, mitochondrial isoform 1
                     precursor"
                     /EC_number="1.2.1.3"
                     /note="acetaldehyde dehydrogenase 2; nucleus-encoded
                     mitochondrial aldehyde dehydrogenase 2; liver
                     mitochondrial ALDH; ALDH class 2; aldehyde dehydrogenase 2
                     family (mitochondrial); epididymis secretory sperm binding
                     protein"
                     /calculated_mol_wt=54445
     transit_peptide 1..17
                     /calculated_mol_wt=1954
     Region          9..24
                     /region_name="SIFI-degron.
                     /evidence=ECO:0000269|PubMed:38297121"
                     /note="propagated from UniProtKB/Swiss-Prot (P05091.2)"
     mat_peptide     18..517
                     /product="aldehyde dehydrogenase, mitochondrial isoform 1"
                     /calculated_mol_wt=54445
     Region          31..511
                     /region_name="ALDH_F1AB_F2_RALDH1"
                     /note="NAD+-dependent retinal dehydrogenase 1, ALDH
                     families 1A, 1B, and 2-like; cd07141"
                     /db_xref="CDD:143459"
     Site            52
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47738; propagated from
                     UniProtKB/Swiss-Prot (P05091.2)"
     Site            73
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47738; propagated from
                     UniProtKB/Swiss-Prot (P05091.2)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47738; propagated from
                     UniProtKB/Swiss-Prot (P05091.2)"
     Site            order(89..90,94,97,99,103,144,147..148,152,154..155,
                     158..162,164..165,168..175,268,271,274..275,278..279,281,
                     286,451,453,460,463,465..472,479..481,484..487,489,492,
                     497,504..509,511)
                     /site_type="other"
                     /note="homotetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143459"
     Site            159
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47738; propagated from
                     UniProtKB/Swiss-Prot (P05091.2)"
     Site            order(182..185,209,212,242,246..247,260,263,266,286..287,
                     319,366,369,416)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143459"
     Site            order(186,285,316,319)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143459"
     Site            186
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P20000; propagated from
                     UniProtKB/Swiss-Prot (P05091.2)"
     Site            368
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47738; propagated from
                     UniProtKB/Swiss-Prot (P05091.2)"
     Site            383
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47738; propagated from
                     UniProtKB/Swiss-Prot (P05091.2)"
     Site            426
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47738; propagated from
                     UniProtKB/Swiss-Prot (P05091.2)"
     Site            428
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47738; propagated from
                     UniProtKB/Swiss-Prot (P05091.2)"
     Site            451
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47738; propagated from
                     UniProtKB/Swiss-Prot (P05091.2)"
     CDS             1..517
                     /gene="ALDH2"
                     /gene_synonym="ALDH-E2; ALDHI; ALDM"
                     /coded_by="NM_000690.4:51..1604"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9155.1"
                     /db_xref="GeneID:217"
                     /db_xref="HGNC:HGNC:404"
                     /db_xref="MIM:100650"
ORIGIN      
        1 mlraaarfgp rlgrrllsaa atqavpapnq qpevfcnqif innewhdavs rktfptvnps
       61 tgevicqvae gdkedvdkav kaaraafqlg spwrrmdash rgrllnrlad lierdrtyla
      121 aletldngkp yvisylvdld mvlkclryya gwadkyhgkt ipidgdffsy trhepvgvcg
      181 qiipwnfpll mqawklgpal atgnvvvmkv aeqtpltaly vanlikeagf ppgvvnivpg
      241 fgptagaaia shedvdkvaf tgsteigrvi qvaagssnlk rvtlelggks pniimsdadm
      301 dwaveqahfa lffnqgqccc agsrtfvqed iydefversv araksrvvgn pfdskteqgp
      361 qvdetqfkki lgyintgkqe gakllcgggi aadrgyfiqp tvfgdvqdgm tiakeeifgp
      421 vmqilkfkti eevvgranns tyglaaavft kdldkanyls qalqagtvwv ncydvfgaqs
      481 pfggykmsgs grelgeyglq aytevktvtv kvpqkns
//
LOCUS       NP_054886                241 aa            linear   PRI 27-APR-2025
DEFINITION  thyroid transcription factor 1-associated protein 26 [Homo
            sapiens].
ACCESSION   NP_054886
VERSION     NP_054886.2
DBSOURCE    REFSEQ: accession NM_014167.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Geller,F., Feenstra,B., Carstensen,L., Pers,T.H., van Rooij,I.A.,
            Korberg,I.B., Choudhry,S., Karjalainen,J.M., Schnack,T.H.,
            Hollegaard,M.V., Feitz,W.F., Roeleveld,N., Hougaard,D.M.,
            Hirschhorn,J.N., Franke,L., Baskin,L.S., Nordenskjold,A., van der
            Zanden,L.F. and Melbye,M.
  TITLE     Genome-wide association analyses identify variants in developmental
            genes associated with hypospadias
  JOURNAL   Nat Genet 46 (9), 957-963 (2014)
   PUBMED   25108383
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Yang,M.C., Guo,Y., Liu,C.C., Weissler,J.C. and Yang,Y.S.
  TITLE     The TTF-1/TAP26 complex differentially modulates surfactant
            protein-B (SP-B) and -C (SP-C) promoters in lung cells
  JOURNAL   Biochem Biophys Res Commun 344 (2), 484-490 (2006)
   PUBMED   16630564
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Yang,M.C., Wang,B., Weissler,J.C., Margraf,L.R. and Yang,Y.S.
  TITLE     BR22, a 26 kDa thyroid transcription factor-1 associated protein
            (TAP26), is expressed in human lung cells
  JOURNAL   Eur Respir J 22 (1), 28-34 (2003)
   PUBMED   12882447
  REMARK    Erratum:[Eur Respir J. 2025 Apr 24;65(4):0251177. doi:
            10.1183/09031936.03.50117702. PMID: 40274302]
REFERENCE   7  (residues 1 to 241)
  AUTHORS   Yang,Y.S., Yang,M.C., Wang,B. and Weissler,J.C.
  TITLE     BR22, a novel protein, interacts with thyroid transcription
            factor-1 and activates the human surfactant protein B promoter
  JOURNAL   Am J Respir Cell Mol Biol 24 (1), 30-37 (2001)
   PUBMED   11152647
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG538660.1, BC020647.1 and AC083811.22.
            
            On Aug 21, 2007 this sequence version replaced NP_054886.1.
            
            Transcript Variant: This variant (1) encodes the functional
            protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF213377.1, SRR1660805.127505.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256151.8/ ENSP00000256151.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.31"
     Protein         1..241
                     /product="thyroid transcription factor 1-associated
                     protein 26"
                     /note="TTF-1-associated protein 26; TTF-1-associated
                     protein BR2; coiled-coil domain-containing protein 59"
                     /calculated_mol_wt=28539
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P031.2)"
     Region          <160..238
                     /region_name="rRNA_processing"
                     /note="rRNA processing; pfam08524"
                     /db_xref="CDD:400708"
     Region          182..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P031.2)"
     CDS             1..241
                     /gene="CCDC59"
                     /gene_synonym="BR22; HSPC128; TAP26"
                     /coded_by="NM_014167.5:12..737"
                     /db_xref="CCDS:CCDS9023.1"
                     /db_xref="GeneID:29080"
                     /db_xref="HGNC:HGNC:25005"
                     /db_xref="MIM:619280"
ORIGIN      
        1 mapvrrsakw rpggiearge gvstvgyrnk nvrqktwrpn hpqafvgsvr egqgfafrrk
       61 lkiqqsykkl lrkekkaqts lesqftdryp dnlkhlylae eerhrkqark vdhplseqvh
      121 qplleeqcsi deplfedqcs fdqpqpeeqc iktvnsftip kknkkktsnq kaqeeyeqiq
      181 akraakkqef errkqereea qrqykkkkme vfkilnkktk kgqpnlnvqm eyllqkiqek
      241 c
//
LOCUS       NP_001012660             354 aa            linear   PRI 27-APR-2025
DEFINITION  GRAM domain-containing protein 2A [Homo sapiens].
ACCESSION   NP_001012660 XP_113796
VERSION     NP_001012660.1
DBSOURCE    REFSEQ: accession NM_001012642.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Besprozvannaya,M., Dickson,E., Li,H., Ginburg,K.S., Bers,D.M.,
            Auwerx,J. and Nunnari,J.
  TITLE     GRAM domain proteins specialize functionally distinct ER-PM contact
            sites in human cells
  JOURNAL   Elife 7, e31019 (2018)
   PUBMED   29469807
  REMARK    GeneRIF: GRAMD2a, but not GRAMD1a, co-localizes with the E-Syt2/3
            tethers at endoplasmic reticulum-plasma membrane contact sites in a
            phosphatidylinositol phosphate lipid-dependent manner. Data from an
            analysis of cells lacking GRAMD2a suggest that it is an organizer
            of the membrane contact sites with pleiotropic functions including
            calcium homeostasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Luykx,J.J., Bakker,S.C., Lentjes,E., Neeleman,M., Strengman,E.,
            Mentink,L., DeYoung,J., de Jong,S., Sul,J.H., Eskin,E., van
            Eijk,K., van Setten,J., Buizer-Voskamp,J.E., Cantor,R.M., Lu,A.,
            van Amerongen,M., van Dongen,E.P., Keijzers,P., Kappen,T.,
            Borgdorff,P., Bruins,P., Derks,E.M., Kahn,R.S. and Ophoff,R.A.
  TITLE     Genome-wide association study of monoamine metabolite levels in
            human cerebrospinal fluid
  JOURNAL   Mol Psychiatry 19 (2), 228-234 (2014)
   PUBMED   23319000
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA854662.1, BC038451.1 and BM663624.1.
            
            On Mar 10, 2005 this sequence version replaced XP_113796.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038451.1, AK095072.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309731.12/ ENSP00000311657.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q23"
     Protein         1..354
                     /product="GRAM domain-containing protein 2A"
                     /note="GRAM domain-containing protein 2; GRAM domain
                     containing 2"
                     /calculated_mol_wt=40118
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUY3.2)"
     Region          84..177
                     /region_name="PH-GRAM_GRAMDC"
                     /note="GRAM domain-containing protein (GRAMDC) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13220"
                     /db_xref="CDD:275406"
     Site            312..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUY3.2)"
     CDS             1..354
                     /gene="GRAMD2A"
                     /gene_synonym="GRAMD2"
                     /coded_by="NM_001012642.3:17..1081"
                     /db_xref="CCDS:CCDS32283.1"
                     /db_xref="GeneID:196996"
                     /db_xref="HGNC:HGNC:27287"
                     /db_xref="MIM:620181"
ORIGIN      
        1 mtalsrseat eeggnqqmhr ktaslnspvs ckekpdrvee ppdyslhwpe glkgeeikkc
       61 gregitlnky nqqyhklfkd vpleevvlkv cscalqrdfl lqgrlyispn wlcfhaslfg
      121 kdikvvipvv svqmikkhkm arllpnglai ttntsqkyif vsllsrdsvy dllrrvcthl
      181 qpsskkslsv refsgepesl evlipemkwr kvcpssrsls lpdnipcipp ssvdstdsff
      241 psrkppmsek sraqvaseng grwawpmpgw gpacpkkmpn csptaknavy eedeleeepr
      301 stgelrlwdy rllkvffvli cflvmsssyl afrisrleqq lcslswddpv pghr
//
LOCUS       NP_001354795             139 aa            linear   PRI 27-APR-2025
DEFINITION  sialidase-3 isoform e [Homo sapiens].
ACCESSION   NP_001354795
VERSION     NP_001354795.1
DBSOURCE    REFSEQ: accession NM_001367866.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Wu,G., Cao,B., Zhai,H., Liu,B., Huang,Y., Chen,X., Ling,H.,
            Ling,S., Jin,S., Yang,X. and Wang,J.
  TITLE     EPO promotes the progression of rheumatoid arthritis by inducing
            desialylation via increasing the expression of neuraminidase 3
  JOURNAL   Ann Rheum Dis 83 (5), 564-575 (2024)
   PUBMED   38272667
  REMARK    GeneRIF: EPO promotes the progression of rheumatoid arthritis by
            inducing desialylation via increasing the expression of
            neuraminidase 3.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Kirolos,S.A., Pilling,D. and Gomer,R.H.
  TITLE     The extracellular sialidase NEU3 primes neutrophils
  JOURNAL   J Leukoc Biol 112 (6), 1399-1411 (2022)
   PUBMED   35899930
  REMARK    GeneRIF: The extracellular sialidase NEU3 primes neutrophils.
            Erratum:[J Leukoc Biol. 2024 Feb 23;115(3):583. doi:
            10.1093/jleuko/qiad154. PMID: 38206829]
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Miyagi,T. and Yamamoto,K.
  TITLE     Sialidase NEU3 and its pathological significance
  JOURNAL   Glycoconj J 39 (5), 677-683 (2022)
   PUBMED   35675020
  REMARK    GeneRIF: Sialidase NEU3 and its pathological significance.
            Review article
            Erratum:[Glycoconj J. 2022 Aug;39(4):543. doi:
            10.1007/s10719-022-10075-7. PMID: 35834088]
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Bovio,F., Epistolio,S., Mozzi,A., Monti,E., Fusi,P., Forcella,M.
            and Frattini,M.
  TITLE     Role of NEU3 Overexpression in the Prediction of Efficacy of
            EGFR-Targeted Therapies in Colon Cancer Cell Lines
  JOURNAL   Int J Mol Sci 21 (22), 8805 (2020)
   PUBMED   33233823
  REMARK    GeneRIF: Role of NEU3 Overexpression in the Prediction of Efficacy
            of EGFR-Targeted Therapies in Colon Cancer Cell Lines.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Ghiroldi,A., Piccoli,M., Creo,P., Cirillo,F., Rota,P.,
            D'Imperio,S., Ciconte,G., Monasky,M.M., Micaglio,E., Garatti,A.,
            Aureli,M., Carsana,E.V., Menicanti,L., Pappone,C. and Anastasia,L.
  TITLE     Role of sialidase Neu3 and ganglioside GM3 in cardiac fibroblasts
            activation
  JOURNAL   Biochem J 477 (17), 3401-3415 (2020)
   PUBMED   32869836
  REMARK    GeneRIF: Role of sialidase Neu3 and ganglioside GM3 in cardiac
            fibroblasts activation.
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Kakugawa,Y., Wada,T., Yamaguchi,K., Yamanami,H., Ouchi,K., Sato,I.
            and Miyagi,T.
  TITLE     Up-regulation of plasma membrane-associated ganglioside sialidase
            (Neu3) in human colon cancer and its involvement in apoptosis
            suppression
  JOURNAL   Proc Natl Acad Sci U S A 99 (16), 10718-10723 (2002)
   PUBMED   12149448
  REMARK    GeneRIF: up-regulation of plasma membrane-associated ganglioside
            sialidase (Neu3) in human colon cancer and its involvement in
            apoptosis suppression
REFERENCE   7  (residues 1 to 139)
  AUTHORS   Wang,Y., Yamaguchi,K., Wada,T., Hata,K., Zhao,X., Fujimoto,T. and
            Miyagi,T.
  TITLE     A close association of the ganglioside-specific sialidase Neu3 with
            caveolin in membrane microdomains
  JOURNAL   J Biol Chem 277 (29), 26252-26259 (2002)
   PUBMED   12011038
  REMARK    GeneRIF: Neu3 functions as a caveolin-related signaling molecule
            within caveolin-rich microdomains
REFERENCE   8  (residues 1 to 139)
  AUTHORS   Wang,Y., Yamaguchi,K., Shimada,Y., Zhao,X. and Miyagi,T.
  TITLE     Site-directed mutagenesis of human membrane-associated ganglioside
            sialidase: identification of amino-acid residues contributing to
            substrate specificity
  JOURNAL   Eur J Biochem 268 (8), 2201-2208 (2001)
   PUBMED   11298736
REFERENCE   9  (residues 1 to 139)
  AUTHORS   Monti,E., Bassi,M.T., Papini,N., Riboni,M., Manzoni,M.,
            Venerando,B., Croci,G., Preti,A., Ballabio,A., Tettamanti,G. and
            Borsani,G.
  TITLE     Identification and expression of NEU3, a novel human sialidase
            associated to the plasma membrane
  JOURNAL   Biochem J 349 (Pt 1), 343-351 (2000)
   PUBMED   10861246
REFERENCE   10 (residues 1 to 139)
  AUTHORS   Wada,T., Yoshikawa,Y., Tokuyama,S., Kuwabara,M., Akita,H. and
            Miyagi,T.
  TITLE     Cloning, expression, and chromosomal mapping of a human ganglioside
            sialidase
  JOURNAL   Biochem Biophys Res Commun 261 (1), 21-27 (1999)
   PUBMED   10405317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001992.4 and BP352846.1.
            
            Summary: This gene product belongs to a family of glycohydrolytic
            enzymes which remove sialic acid residues from glycoproteins and
            glycolipids. It is localized in the plasma membrane, and its
            activity is specific for gangliosides. It may play a role in
            modulating the ganglioside content of the lipid bilayer. [provided
            by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2624319.1, BP352846.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155371 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..139
                     /product="sialidase-3 isoform e"
                     /EC_number="3.2.1.18"
                     /note="ganglioside sialidase; N-acetyl-alpha-neuraminidase
                     3; sialidase-3; membrane sialidase; sialidase 3 (membrane
                     sialidase); ganglioside sialidasedis"
                     /calculated_mol_wt=15635
     Region          46..>93
                     /region_name="NanH"
                     /note="Neuraminidase (sialidase) NanH, contains C-terminal
                     autotransporter domain [Carbohydrate transport and
                     metabolism, Cell wall/membrane/envelope biogenesis];
                     COG4409"
                     /db_xref="CDD:443531"
     CDS             1..139
                     /gene="NEU3"
                     /gene_synonym="SIAL3"
                     /coded_by="NM_001367866.1:129..548"
                     /note="isoform e is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS91537.1"
                     /db_xref="GeneID:10825"
                     /db_xref="HGNC:HGNC:7760"
                     /db_xref="MIM:604617"
ORIGIN      
        1 mrpadlpprp meespasssa pteteepgss aevmeevttc sfnsplfrqe ddrgityrip
       61 allyipptht flafaekrst rrdedalhlv lrrglrigql vqrwgfamlp rlvsnswtqa
      121 ilkcwdysms hcawpfggp
//
LOCUS       NP_001008710             196 aa            linear   PRI 27-APR-2025
DEFINITION  RNA-binding protein with multiple splicing isoform A [Homo
            sapiens].
ACCESSION   NP_001008710
VERSION     NP_001008710.1
DBSOURCE    REFSEQ: accession NM_001008710.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Gan,P., Wang,Z., Bezprozvannaya,S., McAnally,J.R., Tan,W., Li,H.,
            Bassel-Duby,R., Liu,N. and Olson,E.N.
  TITLE     RBPMS regulates cardiomyocyte contraction and cardiac function
            through RNA alternative splicing
  JOURNAL   Cardiovasc Res 120 (1), 56-68 (2024)
   PUBMED   37890031
  REMARK    GeneRIF: RBPMS regulates cardiomyocyte contraction and cardiac
            function through RNA alternative splicing.
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Gong,T.T., Liu,F.H., Xiao,Q., Li,Y.Z., Wei,Y.F., Xu,H.L., Cao,F.,
            Sun,M.L., Jiang,F.L., Tao,T., Ma,Q.P., Qin,X., Song,Y., Gao,S.,
            Wu,L., Zhao,Y.H., Huang,D.H. and Wu,Q.J.
  TITLE     SH3RF2 contributes to cisplatin resistance in ovarian cancer cells
            by promoting RBPMS degradation
  JOURNAL   Commun Biol 7 (1), 67 (2024)
   PUBMED   38195842
  REMARK    GeneRIF: SH3RF2 contributes to cisplatin resistance in ovarian
            cancer cells by promoting RBPMS degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Yang,Y., Lee,G.C., Nakagaki-Silva,E., Huang,Y., Peacey,M.,
            Partridge,R., Gooding,C. and Smith,C.W.J.
  TITLE     Cell-type specific regulator RBPMS switches alternative splicing
            via higher-order oligomerization and heterotypic interactions with
            other splicing regulators
  JOURNAL   Nucleic Acids Res 51 (18), 9961-9982 (2023)
   PUBMED   37548402
  REMARK    GeneRIF: Cell-type specific regulator RBPMS switches alternative
            splicing via higher-order oligomerization and heterotypic
            interactions with other splicing regulators.
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Bartsch,D., Kalamkar,K., Ahuja,G., Lackmann,J.W., Hescheler,J.,
            Weber,T., Bazzi,H., Clamer,M., Mendjan,S., Papantonis,A. and
            Kurian,L.
  TITLE     mRNA translational specialization by RBPMS presets the competence
            for cardiac commitment in hESCs
  JOURNAL   Sci Adv 9 (13), eade1792 (2023)
   PUBMED   36989351
  REMARK    GeneRIF: mRNA translational specialization by RBPMS presets the
            competence for cardiac commitment in hESCs.
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Rabelo-Fernandez,R.J., Noriega Rivera,R.A., Rivera,Y.S.,
            Tous-Beveraggi,J., Valiyeva,F. and Vivas-Mejia,P.E.
  TITLE     Increased Expression of the RBPMS Splice Variants Inhibits Cell
            Proliferation in Ovarian Cancer Cells
  JOURNAL   Int J Mol Sci 23 (23), 14742 (2022)
   PUBMED   36499073
  REMARK    GeneRIF: Increased Expression of the RBPMS Splice Variants Inhibits
            Cell Proliferation in Ovarian Cancer Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Sun,Y., Ding,L., Zhang,H., Han,J., Yang,X., Yan,J., Zhu,Y., Li,J.,
            Song,H. and Ye,Q.
  TITLE     Potentiation of Smad-mediated transcriptional activation by the
            RNA-binding protein RBPMS
  JOURNAL   Nucleic Acids Res 34 (21), 6314-6326 (2006)
   PUBMED   17099224
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Shimamoto,A., Kitao,S., Ichikawa,K., Suzuki,N., Yamabe,Y.,
            Imamura,O., Tokutake,Y., Satoh,M., Matsumoto,T., Kuromitsu,J.,
            Kataoka,H., Sugawara,K., Sugawara,M., Sugimoto,M., Goto,M. and
            Furuichi,Y.
  TITLE     A unique human gene that spans over 230 kb in the human chromosome
            8p11-12 and codes multiple family proteins sharing RNA-binding
            motifs
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10913-10917 (1996)
   PUBMED   8855282
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CX165198.1, BC003608.2,
            D84107.1, CX781149.1, CN360712.1 and BX097929.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the RNA recognition motif
            family of RNA-binding proteins. The RNA recognition motif is
            between 80-100 amino acids in length and family members contain one
            to four copies of the motif. The RNA recognition motif consists of
            two short stretches of conserved sequence, as well as a few highly
            conserved hydrophobic residues. The encoded protein has a single,
            putative RNA recognition motif in its N-terminus. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (1) encodes isoform A. Variants 1
            and 4 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.54264.1,
                                           SRR1660809.128176.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397323.9/ ENSP00000380486.4
            NMD candidate          :: translation inferred from conservation
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..196
                     /product="RNA-binding protein with multiple splicing
                     isoform A"
                     /note="heart and RRM expressed sequence; RNA binding
                     protein with multiple splicing"
                     /calculated_mol_wt=21671
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVB0; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Region          23..98
                     /region_name="RRM_RBPMS"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     RNA-binding protein with multiple splicing (RBP-MS);
                     cd12682"
                     /db_xref="CDD:410083"
     Site            27
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:26347403; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Site            61
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:26347403; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Region          <64..>165
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Region          98..105
                     /region_name="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:26347403"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93062.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     CDS             1..196
                     /gene="RBPMS"
                     /gene_synonym="HERMES"
                     /coded_by="NM_001008710.3:553..1143"
                     /note="isoform A is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6077.1"
                     /db_xref="GeneID:11030"
                     /db_xref="HGNC:HGNC:19097"
                     /db_xref="MIM:601558"
ORIGIN      
        1 mnnggkaeke ntpseanlqe eevrtlfvsg lpldikprel yllfrpfkgy egslikltsk
       61 qpvgfvsfds rseaeaakna lngirfdpei pqtlrlefak antkmaknkl vgtpnpstpl
      121 pntvpqfiar epyeltvpal ypsspevwap yplypaelap alpppaftyp aslhaqmrwl
      181 ppseatsqgw ksrqfc
//
LOCUS       NP_001124295            1632 aa            linear   PRI 27-APR-2025
DEFINITION  DNA (cytosine-5)-methyltransferase 1 isoform a [Homo sapiens].
ACCESSION   NP_001124295
VERSION     NP_001124295.1
DBSOURCE    REFSEQ: accession NM_001130823.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1632)
  AUTHORS   De,I., Weidenhausen,J., Concha,N. and Muller,C.W.
  TITLE     Structural insight into the DNMT1 reaction cycle by cryo-electron
            microscopy
  JOURNAL   PLoS One 19 (9), e0307850 (2024)
   PUBMED   39226277
  REMARK    GeneRIF: Structural insight into the DNMT1 reaction cycle by
            cryo-electron microscopy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1632)
  AUTHORS   Wang,R., Yu,X., Ye,H., Ao,M., Xi,M. and Hou,M.
  TITLE     LncRNA FAM83H-AS1 inhibits ferroptosis of endometrial cancer by
            promoting DNMT1-mediated CDO1 promoter hypermethylation
  JOURNAL   J Biol Chem 300 (9), 107680 (2024)
   PUBMED   39159808
  REMARK    GeneRIF: LncRNA FAM83H-AS1 inhibits ferroptosis of endometrial
            cancer by promoting DNMT1-mediated CDO1 promoter hypermethylation.
REFERENCE   3  (residues 1 to 1632)
  AUTHORS   Bonfils,C., Beaulieu,N., Chan,E., Cotton-Montpetit,J. and
            MacLeod,A.R.
  TITLE     Characterization of the human DNA methyltransferase splice variant
            Dnmt1b
  JOURNAL   J Biol Chem 275 (15), 10754-10760 (2000)
   PUBMED   10753866
REFERENCE   4  (residues 1 to 1632)
  AUTHORS   Bigey,P., Ramchandani,S., Theberge,J., Araujo,F.D. and Szyf,M.
  TITLE     Transcriptional regulation of the human DNA Methyltransferase
            (dnmt1) gene
  JOURNAL   Gene 242 (1-2), 407-418 (2000)
   PUBMED   10721735
REFERENCE   5  (residues 1 to 1632)
  AUTHORS   Hsu,D.W., Lin,M.J., Lee,T.L., Wen,S.C., Chen,X. and Shen,C.K.
  TITLE     Two major forms of DNA (cytosine-5) methyltransferase in human
            somatic tissues
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9751-9756 (1999)
   PUBMED   10449766
REFERENCE   6  (residues 1 to 1632)
  AUTHORS   Yoder,J.A., Yen,R.W., Vertino,P.M., Bestor,T.H. and Baylin,S.B.
  TITLE     New 5' regions of the murine and human genes for DNA
            (cytosine-5)-methyltransferase
  JOURNAL   J Biol Chem 271 (49), 31092-31097 (1996)
   PUBMED   8940105
REFERENCE   7  (residues 1 to 1632)
  AUTHORS   Klein,C.J.
  TITLE     DNMT1-Related Disorder
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22338191
REFERENCE   8  (residues 1 to 1632)
  AUTHORS   Yen,R.W., Vertino,P.M., Nelkin,B.D., Yu,J.J., el-Deiry,W.,
            Cumaraswamy,A., Lennon,G.G., Trask,B.J., Celano,P. and Baylin,S.B.
  TITLE     Isolation and characterization of the cDNA encoding human DNA
            methyltransferase
  JOURNAL   Nucleic Acids Res 20 (9), 2287-2291 (1992)
   PUBMED   1594447
REFERENCE   9  (residues 1 to 1632)
  AUTHORS   el-Deiry,W.S., Nelkin,B.D., Celano,P., Yen,R.W., Falco,J.P.,
            Hamilton,S.R. and Baylin,S.B.
  TITLE     High expression of the DNA methyltransferase gene characterizes
            human neoplastic cells and progression stages of colon cancer
  JOURNAL   Proc Natl Acad Sci U S A 88 (8), 3470-3474 (1991)
   PUBMED   2014266
REFERENCE   10 (residues 1 to 1632)
  AUTHORS   Bestor,T.H.
  TITLE     DNA methylation: evolution of a bacterial immune function into a
            regulator of gene expression and genome structure in higher
            eukaryotes
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1235), 179-187 (1990)
   PUBMED   1968655
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC126227.1, BC092517.1,
            DA653750.1 and X63692.1.
            
            Summary: This gene encodes an enzyme that transfers methyl groups
            to cytosine nucleotides of genomic DNA. This protein is the major
            enzyme responsible for maintaining methylation patterns following
            DNA replication and shows a preference for hemi-methylated DNA.
            Methylation of DNA is an important component of mammalian
            epigenetic gene regulation. Aberrant methylation patterns are found
            in human tumors and associated with developmental abnormalities.
            Variation in this gene has been associated with cerebellar ataxia,
            deafness, and narcolepsy, and neuropathy, hereditary sensory, type
            IE. Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1, also known as Dnmt1b in PMIDs
            10449766 and 10753866) represents the longest transcript and
            encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144093.1, SRR11853567.15044.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359526.9/ ENSP00000352516.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1632
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1632
                     /product="DNA (cytosine-5)-methyltransferase 1 isoform a"
                     /EC_number="2.1.1.37"
                     /note="DNA MTase HsaI; DNA methyltransferase HsaI;
                     CXXC-type zinc finger protein 9; DNA
                     (cytosine-5-)-methyltransferase 1"
                     /calculated_mol_wt=184689
     Region          1..148
                     /region_name="Interaction with DNMT3A.
                     /evidence=ECO:0000269|PubMed:12145218"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Region          1..120
                     /region_name="Interaction with DMAP1.
                     /evidence=ECO:0000269|PubMed:10888872"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Region          16..105
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Site            70
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0000269|PubMed:18438403; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          <112..434
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13864; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            142
                     /site_type="methylation"
                     /note="N6-methyllysine, by SETD7.
                     /evidence=ECO:0000269|PubMed:21151116; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:21151116,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Region          165..233
                     /region_name="Interaction with DNMT3B.
                     /evidence=ECO:0000269|PubMed:12145218"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21565170,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            176
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          179..190
                     /region_name="Interaction with PCNA.
                     /evidence=ECO:0000269|PubMed:9302295"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            189
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          193..221
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            204
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          324..622
                     /region_name="Interaction with the PRC2/EED-EZH2 complex.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Region          326..518
                     /region_name="Homodimerization"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          347..566
                     /region_name="DNA replication foci-targeting sequence.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            382
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          415..550
                     /region_name="DNMT1-RFD"
                     /note="Cytosine specific DNA methyltransferase replication
                     foci domain; pfam12047"
                     /db_xref="CDD:463444"
     Site            525
                     /site_type="other"
                     /note="Important for activity. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13864; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          661..707
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          667..713
                     /region_name="Required for activity"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Region          709..770
                     /region_name="Autoinhibitory linker"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Region          715..745
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            748
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            765
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          770..893
                     /region_name="BAH_Dnmt1_I"
                     /note="BAH, or Bromo Adjacent Homology domain, first copy
                     present in DNA (Cytosine-5)-methyltransferases from
                     Bilateria, Dnmt1 and similar proteins. DNA methylation, or
                     the covalent addition of a methyl group to cytosine within
                     the context of the CpG...; cd04760"
                     /db_xref="CDD:240107"
     Site            894
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            907
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            973
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            977
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          981..1117
                     /region_name="BAH_Dnmt1_II"
                     /note="BAH, or Bromo Adjacent Homology domain, second copy
                     present in DNA (Cytosine-5)-methyltransferases from
                     Bilateria, Dnmt1 and similar proteins. DNA methylation, or
                     the covalent addition of a methyl group to cytosine within
                     the context of the CpG...; cd04711"
                     /db_xref="CDD:240062"
     Site            991
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            1070
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          1111..1146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Region          1125..1136
                     /region_name="6 X 2 AA tandem repeats of K-G"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            1127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            1129
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            1131
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            1133
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EHMT2.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            1135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P13864; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          1137..1632
                     /region_name="Interaction with the PRC2/EED-EZH2 complex.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            1137
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P13864; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Region          1153..1609
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
     Region          1155..1632
                     /region_name="Catalytic"
                     /note="propagated from UniProtKB/Swiss-Prot (P26358.2)"
     Site            1365
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     Site            1431
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:21947282; propagated from
                     UniProtKB/Swiss-Prot (P26358.2)"
     CDS             1..1632
                     /gene="DNMT1"
                     /gene_synonym="ADCADN; AIM; CXXC9; DNMT; HSN1E; m.HsaI;
                     MCMT"
                     /coded_by="NM_001130823.3:55..4953"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45958.1"
                     /db_xref="GeneID:1786"
                     /db_xref="HGNC:HGNC:2976"
                     /db_xref="MIM:126375"
ORIGIN      
        1 mpartaparv ptlavpaisl pddvrrrlkd lerdslteke cvkeklnllh eflqteiknq
       61 lcdletklrk eelseegyla kvksllnkdl slengahayn revngrleng nqarsearrv
      121 gmadansppk plskprtprr sksdgeakrs rdppasasqv tgiraepsps pritrkstrq
      181 ttitshfakg pakrkpqees eraksdesik eedkdqdekr rrvtsrerva rplpaeeper
      241 aksgtrteke eerdekeekr lrsqtkeptp kqklkeepdr earagvqade dedgdekdek
      301 khrsqpkdla akrrpeekep ekvnpqisde kdedekeekr rkttpkepte kkmaraktvm
      361 nskthppkci qcgqylddpd lkygqhppda vdepqmltne klsifdanes gfesyealpq
      421 hkltcfsvyc khghlcpidt glieknielf fsgsakpiyd ddpsleggvn gknlgpinew
      481 witgfdggek aligfstsfa eyilmdpspe yapifglmqe kiyiskivve flqsnsdsty
      541 edlinkiett vppsglnlnr ftedsllrha qfvveqvesy deagdsdeqp ifltpcmrdl
      601 iklagvtlgq rraqarrqti rhstrekdrg ptkatttklv yqifdtffae qiekddredk
      661 enafkrrrcg vcevcqqpec gkckackdmv kfggsgrskq acqerrcpnm amkeadddee
      721 vddnipemps pkkmhqgkkk kqnknriswv geavktdgkk syykkvcida etlevgdcvs
      781 vipddsskpl ylarvtalwe dssngqmfha hwfcagtdtv lgatsdplel flvdecedmq
      841 lsyihskvkv iykapsenwa meggmdpesl legddgktyf yqlwydqdya rfesppktqp
      901 tednkfkfcv scarlaemrq keiprvleql edldsrvlyy satkngilyr vgdgvylppe
      961 aftfniklss pvkrprkepv dedlypehyr kysdyikgsn ldapepyrig rikeifcpkk
     1021 sngrpnetdi kirvnkfyrp enthkstpas yhadinllyw sdeeavvdfk avqgrctvey
     1081 gedlpecvqv ysmggpnrfy fleaynaksk sfedppnhar spgnkgkgkg kgkgkpksqa
     1141 cepsepeiei klpklrtldv fsgcgglseg fhqagisdtl waiemwdpaa qafrlnnpgs
     1201 tvftedcnil lklvmagett nsrgqrlpqk gdvemlcggp pcqgfsgmnr fnsrtyskfk
     1261 nslvvsflsy cdyyrprffl lenvrnfvsf krsmvlkltl rclvrmgyqc tfgvlqagqy
     1321 gvaqtrrrai ilaaapgekl plfpeplhvf apracqlsvv vddkkfvsni trlssgpfrt
     1381 itvrdtmsdl pevrngasal eisyngepqs wfqrqlrgaq yqpilrdhic kdmsalvaar
     1441 mrhiplapgs dwrdlpniev rlsdgtmark lrythhdrkn grsssgalrg vcscveagka
     1501 cdpaarqfnt lipwclphtg nrhnhwagly grlewdgffs ttvtnpepmg kqgrvlhpeq
     1561 hrvvsvreca rsqgfpdtyr lfgnildkhr qvgnavpppl akaigleikl cmlakaresa
     1621 sakikeeeaa kd
//
LOCUS       NP_004023                282 aa            linear   PRI 27-APR-2025
DEFINITION  D-aspartate oxidase isoform b [Homo sapiens].
ACCESSION   NP_004023
VERSION     NP_004023.3
DBSOURCE    REFSEQ: accession NM_004032.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Rabattoni,V., Motta,Z., Miceli,M., Molla,G., Fissore,A.,
            Adinolfi,S., Pollegioni,L. and Sacchi,S.
  TITLE     On the regulation of human D-aspartate oxidase
  JOURNAL   Protein Sci 32 (11), e4802 (2023)
   PUBMED   37805834
  REMARK    GeneRIF: On the regulation of human D-aspartate oxidase.
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Lombardo,B., Pagani,M., De Rosa,A., Nunziato,M., Migliarini,S.,
            Garofalo,M., Terrile,M., D'Argenio,V., Galbusera,A., Nuzzo,T.,
            Ranieri,A., Vitale,A., Leggiero,E., Di Maio,A., Barsotti,N.,
            Borello,U., Napolitano,F., Mandarino,A., Carotenuto,M.,
            Heresco-Levy,U., Pasqualetti,M., Malatesta,P., Gozzi,A., Errico,F.,
            Salvatore,F., Pastore,L. and Usiello,A.
  TITLE     D-aspartate oxidase gene duplication induces social recognition
            memory deficit in mice and intellectual disabilities in humans
  JOURNAL   Transl Psychiatry 12 (1), 305 (2022)
   PUBMED   35915065
  REMARK    GeneRIF: D-aspartate oxidase gene duplication induces social
            recognition memory deficit in mice and intellectual disabilities in
            humans.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Chen,A.S., Liu,H., Wu,Y., Luo,S., Patz,E.F. Jr., Glass,C., Su,L.,
            Du,M., Christiani,D.C. and Wei,Q.
  TITLE     Genetic variants in DDO and PEX5L in peroxisome-related pathways
            predict non-small cell lung cancer survival
  JOURNAL   Mol Carcinog 61 (7), 619-628 (2022)
   PUBMED   35502931
  REMARK    GeneRIF: Genetic variants in DDO and PEX5L in peroxisome-related
            pathways predict non-small cell lung cancer survival.
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Rabattoni,V., Pollegioni,L., Tedeschi,G., Maffioli,E. and Sacchi,S.
  TITLE     Cellular studies of the two main isoforms of human d-aspartate
            oxidase
  JOURNAL   FEBS J 288 (16), 4939-4954 (2021)
   PUBMED   33650155
  REMARK    GeneRIF: Cellular studies of the two main isoforms of human
            d-aspartate oxidase.
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Molla,G., Chaves-Sanjuan,A., Savinelli,A., Nardini,M. and
            Pollegioni,L.
  TITLE     Structure and kinetic properties of human d-aspartate oxidase, the
            enzyme-controlling d-aspartate levels in brain
  JOURNAL   FASEB J 34 (1), 1182-1197 (2020)
   PUBMED   31914658
  REMARK    GeneRIF: three-dimensional structural analysis contributes insights
            into the structure-function relationships of human DASPO
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Setoyama,C. and Miura,R.
  TITLE     Structural and functional characterization of the human brain
            D-aspartate oxidase
  JOURNAL   J Biochem 121 (4), 798-803 (1997)
   PUBMED   9163533
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Simonic,T., Duga,S., Negri,A., Tedeschi,G., Malcovati,M.,
            Tenchini,M.L. and Ronchi,S.
  TITLE     cDNA cloning and expression of the flavoprotein D-aspartate oxidase
            from bovine kidney cortex
  JOURNAL   Biochem J 322 (Pt 3) (Pt 3), 729-735 (1997)
   PUBMED   9148742
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Nagasaki,H.
  TITLE     Gender-related differences of mouse liver D-aspartate oxidase in
            the activity and response to administration of D-aspartate and
            peroxisome proliferators
  JOURNAL   Int J Biochem 26 (3), 415-423 (1994)
   PUBMED   8187937
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Van Veldhoven,P.P., Brees,C. and Mannaerts,G.P.
  TITLE     D-aspartate oxidase, a peroxisomal enzyme in liver of rat and man
  JOURNAL   Biochim Biophys Acta 1073 (1), 203-208 (1991)
   PUBMED   1991137
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Barker,R.F. and Hopkinson,D.A.
  TITLE     The genetic and biochemical properties of the D-amino acid oxidases
            in human tissues
  JOURNAL   Ann Hum Genet 41 (1), 27-42 (1977)
   PUBMED   21608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL050350.14.
            
            On Jan 19, 2019 this sequence version replaced NP_004023.2.
            
            Summary: The protein encoded by this gene is a peroxisomal
            flavoprotein that catalyzes the oxidative deamination of
            D-aspartate and N-methyl D-aspartate. Flavin adenine dinucleotide
            or 6-hydroxyflavin adenine dinucleotide can serve as the cofactor
            in this reaction. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jan
            2019].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (b) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.219486.1,
                                           SRR1803613.245384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..282
                     /product="D-aspartate oxidase isoform b"
                     /EC_number="1.4.3.1"
                     /note="aspartic oxidase; D-aspartate oxidase, DDO"
                     /calculated_mol_wt=30391
     Region          5..265
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
     CDS             1..282
                     /gene="DDO"
                     /gene_synonym="DASOX; DASPO; DDO-1; DDO-2"
                     /coded_by="NM_004032.3:114..962"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5083.2"
                     /db_xref="GeneID:8528"
                     /db_xref="HGNC:HGNC:2727"
                     /db_xref="MIM:124450"
ORIGIN      
        1 mdtariavvg agvvglstav cisklvprcs vtiisdkftp dttsdvaagm liphtypdtp
       61 ihtqkqwfre tfnhlfaian saeagdagvh lvsgikgsgg wtltrriedl welhpsfdiv
      121 vncsglgsrq lagdskifpv rgqvlqvqap wvehfirdgs gltyiypgts hvtlggtrqk
      181 gdwnlspdae nsreilsrcc alepslhgac nirekvglrp yrpgvrlqte llardgqrlp
      241 vvhhyghgsg gisvhwgtal eaarlvsecv halrtpipks nl
//
LOCUS       NP_037064                572 aa            linear   ROD 27-APR-2025
DEFINITION  dihydropyrimidinase-related protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_037064
VERSION     NP_037064.1
DBSOURCE    REFSEQ: accession NM_012932.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Zhang,J., Li,X., Zhang,Z., Zhang,J., Ma,L., Wang,S., Guo,X., Li,H.,
            Pan,B. and Niu,Q.
  TITLE     Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced PC12 cells
            necroptosis
  JOURNAL   Ecotoxicol Environ Saf 270, 115860 (2024)
   PUBMED   38142589
  REMARK    GeneRIF: Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced
            PC12 cells necroptosis.
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Liu,Y. and Xu,Y.J.
  TITLE     LKB1 and CRMP1 cooperatively promote the repair of the sciatic
            nerve injury
  JOURNAL   Dev Neurobiol 84 (1), 18-31 (2024)
   PUBMED   38105470
  REMARK    GeneRIF: LKB1 and CRMP1 cooperatively promote the repair of the
            sciatic nerve injury.
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Cruz Hernandez,J.H., Rosado Loman,W.N., Gomez-Crisostomo,N.P., De
            la Cruz-Hernandez,E.N., Guzman Garcia,L.M., Gomez Gomez,M.,
            Hernandez Del Angel,N.A., Aguilar Gamas,C.F., Cruz Hernandez,V.S.
            and Martinez-Abundis,E.
  TITLE     High sugar but not high fat diet consumption induces hepatic
            metabolic disruption and up-regulation of mitochondrial
            fission-associated protein Drp1 in a model of moderate obesity
  JOURNAL   Arch Physiol Biochem 129 (1), 233-240 (2023)
   PUBMED   32880477
  REMARK    GeneRIF: High sugar but not high fat diet consumption induces
            hepatic metabolic disruption and up-regulation of mitochondrial
            fission-associated protein Drp1 in a model of moderate obesity.
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Chua,J.Y., Ng,S.J., Yagensky,O., Wanker,E.E. and Chua,J.J.E.
  TITLE     FEZ1 Forms Complexes with CRMP1 and DCC to Regulate Axon and
            Dendrite Development
  JOURNAL   eNeuro 8 (2) (2021)
   PUBMED   33771901
  REMARK    GeneRIF: FEZ1 Forms Complexes with CRMP1 and DCC to Regulate Axon
            and Dendrite Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Nakamura,F., Kumeta,K., Hida,T., Isono,T., Nakayama,Y.,
            Kuramata-Matsuoka,E., Yamashita,N., Uchida,Y., Ogura,K.,
            Gengyo-Ando,K., Mitani,S., Ogino,T. and Goshima,Y.
  TITLE     Amino- and carboxyl-terminal domains of Filamin-A interact with
            CRMP1 to mediate Sema3A signalling
  JOURNAL   Nat Commun 5, 5325 (2014)
   PUBMED   25358863
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Chen,T.C., Lee,S.A., Hong,T.M., Shih,J.Y., Lai,J.M., Chiou,H.Y.,
            Yang,S.C., Chan,C.H., Kao,C.Y., Yang,P.C. and Huang,C.Y.
  TITLE     From midbody protein-protein interaction network construction to
            novel regulators in cytokinesis
  JOURNAL   J Proteome Res 8 (11), 4943-4953 (2009)
   PUBMED   19799413
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Bevers,M.B., Lawrence,E., Maronski,M., Starr,N., Amesquita,M. and
            Neumar,R.W.
  TITLE     Knockdown of m-calpain increases survival of primary hippocampal
            neurons following NMDA excitotoxicity
  JOURNAL   J Neurochem 108 (5), 1237-1250 (2009)
   PUBMED   19141074
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Bretin,S., Reibel,S., Charrier,E., Maus-Moatti,M., Auvergnon,N.,
            Thevenoux,A., Glowinski,J., Rogemond,V., Premont,J., Honnorat,J.
            and Gauchy,C.
  TITLE     Differential expression of CRMP1, CRMP2A, CRMP2B, and CRMP5 in
            axons or dendrites of distinct neurons in the mouse brain
  JOURNAL   J Comp Neurol 486 (1), 1-17 (2005)
   PUBMED   15834957
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Fukada,M., Watakabe,I., Yuasa-Kawada,J., Kawachi,H., Kuroiwa,A.,
            Matsuda,Y. and Noda,M.
  TITLE     Molecular characterization of CRMP5, a novel member of the
            collapsin response mediator protein family
  JOURNAL   J Biol Chem 275 (48), 37957-37965 (2000)
   PUBMED   10956643
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Wang,L.H. and Strittmatter,S.M.
  TITLE     A family of rat CRMP genes is differentially expressed in the
            nervous system
  JOURNAL   J Neurosci 16 (19), 6197-6207 (1996)
   PUBMED   8815901
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            Transcript Variant: This variant (2) contains an alternate 5'
            terminal exon and initiates translation at an alternate start codon
            compared to variant 1. The encoded isoform (2) is shorter with a
            distinct N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U52102.2, SRR26643289.35085.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..572
                     /product="dihydropyrimidinase-related protein 1 isoform 2"
                     /note="dihydropyrimidinase-related protein 1; DRP-1;
                     CRMP-1; inactive dihydropyrimidinase"
                     /calculated_mol_wt=62065
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Region          17..466
                     /region_name="D-HYD"
                     /note="D-hydantoinases (D-HYD) also called
                     dihydropyrimidases (DHPase) and related proteins; DHPases
                     are a family of enzymes that catalyze the reversible
                     hydrolytic ring opening of the amide bond in five- or
                     six-membered cyclic diamides, like dihydropyrimidine...;
                     cd01314"
                     /db_xref="CDD:238639"
     Site            order(28..29,31,44..45,180,201,204,207,230,234,238,241,
                     268..269,271..272,390,395,400)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238639"
     Site            order(73,75,165,198,254,332)
                     /site_type="active"
                     /db_xref="CDD:238639"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14194; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14194; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Region          246..247
                     /region_name="Required for interaction with FLNA.
                     /evidence=ECO:0000250|UniProtKB:Q14194"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62950.1)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P97427; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Region          509..572
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62950.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P97427; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97427; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97427; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97427; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     CDS             1..572
                     /gene="Crmp1"
                     /coded_by="NM_012932.3:212..1930"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25415"
                     /db_xref="RGD:2407"
ORIGIN      
        1 mshqgkksip hitsdrllir ggriinddqs fyadvyledg likqigenli vpggvktiea
       61 ngrmvipggi dvntylqkps qgmtsaddff qgtraalagg ttmiidhvvp epgsslltsf
      121 ekwheaadtk sccdyslhvd itswydgvre elevlvqdkg vnsfqvymay kdlyqmsdsq
      181 lyeaftflkg lgavilvhae ngdliaqeqk rilemgitgp eghalsrpee leaeavfrai
      241 aiagrincpv yitkvmsksa adiialarkk gplvfgepia aslgtdgthy wsknwakaaa
      301 fvtspplspd pttpdyltsl lacgdlqvtg sghcpystaq kavgkdnftl ipegvngiee
      361 rmtvvwdkav atgkmdenqf vavtstnaak ifnlyprkgr iavgsdadvv iwdpdkmktl
      421 takshkstve ynifegmech gsplvvisqg kivfedgnis vskgmgrfip rkpfpehlyq
      481 rvrirskvfg lhsvsrgmyd gpvyevpatp khaapapsak sspskhqppp irnlhqsnfs
      541 lsgaqiddnn prrtghriva ppggrsnits lg
//
LOCUS       NP_078813                564 aa            linear   PRI 27-APR-2025
DEFINITION  probable cysteine--tRNA ligase, mitochondrial isoform 1 [Homo
            sapiens].
ACCESSION   NP_078813
VERSION     NP_078813.1
DBSOURCE    REFSEQ: accession NM_024537.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Akaike,T., Ida,T., Wei,F.Y., Nishida,M., Kumagai,Y., Alam,M.M.,
            Ihara,H., Sawa,T., Matsunaga,T., Kasamatsu,S., Nishimura,A.,
            Morita,M., Tomizawa,K., Nishimura,A., Watanabe,S., Inaba,K.,
            Shima,H., Tanuma,N., Jung,M., Fujii,S., Watanabe,Y., Ohmuraya,M.,
            Nagy,P., Feelisch,M., Fukuto,J.M. and Motohashi,H.
  TITLE     Cysteinyl-tRNA synthetase governs cysteine polysulfidation and
            mitochondrial bioenergetics
  JOURNAL   Nat Commun 8 (1), 1177 (2017)
   PUBMED   29079736
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Coughlin,C.R. 2nd, Scharer,G.H., Friederich,M.W., Yu,H.C.,
            Geiger,E.A., Creadon-Swindell,G., Collins,A.E., Vanlander,A.V.,
            Coster,R.V., Powell,C.A., Swanson,M.A., Minczuk,M., Van Hove,J.L.
            and Shaikh,T.H.
  TITLE     Mutations in the mitochondrial cysteinyl-tRNA synthase gene, CARS2,
            lead to a severe epileptic encephalopathy and complex movement
            disorder
  JOURNAL   J Med Genet 52 (8), 532-540 (2015)
   PUBMED   25787132
  REMARK    GeneRIF: Mutations in CARS2 result in a mitochondrial translational
            defect as seen in individuals with mitochondrial epileptic
            encephalopathy.
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Hallmann,K., Zsurka,G., Moskau-Hartmann,S., Kirschner,J.,
            Korinthenberg,R., Ruppert,A.K., Ozdemir,O., Weber,Y., Becker,F.,
            Lerche,H., Elger,C.E., Thiele,H., Nurnberg,P., Sander,T. and
            Kunz,W.S.
  TITLE     A homozygous splice-site mutation in CARS2 is associated with
            progressive myoclonic epilepsy
  JOURNAL   Neurology 83 (23), 2183-2187 (2014)
   PUBMED   25361775
  REMARK    GeneRIF: CARS2 is a novel disease gene associated with a severe
            progressive myoclonic epilepsy most resembling MERRF syndrome
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Bonnefond,L., Fender,A., Rudinger-Thirion,J., Giege,R., Florentz,C.
            and Sissler,M.
  TITLE     Toward the full set of human mitochondrial aminoacyl-tRNA
            synthetases: characterization of AspRS and TyrRS
  JOURNAL   Biochemistry 44 (12), 4805-4816 (2005)
   PUBMED   15779907
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY150557.1, BC007220.1,
            AK301907.1 and CB047094.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a putative member of the class I family
            of aminoacyl-tRNA synthetases. These enzymes play a critical role
            in protein biosynthesis by charging tRNAs with their cognate amino
            acids. This protein is encoded by the nuclear genome but is likely
            to be imported to the mitochondrion where it is thought to catalyze
            the ligation of cysteine to tRNA molecules. A splice-site mutation
            in this gene has been associated with a novel progressive myoclonic
            epilepsy disease with similar symptoms to MERRF syndrome.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jun 2017].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022180.1, SRR1163658.42357.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000257347.9/
                                                  ENSP00000257347.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..564
                     /product="probable cysteine--tRNA ligase, mitochondrial
                     isoform 1"
                     /EC_number="6.1.1.16"
                     /note="cysteine tRNA ligase 2, mitochondrial (putative);
                     probable cysteine--tRNA ligase, mitochondrial;
                     cysteinyl-tRNA synthetase 2, mitochondrial (putative)"
                     /calculated_mol_wt=62093
     Region          35..563
                     /region_name="PTZ00399"
                     /note="cysteinyl-tRNA-synthetase; Provisional"
                     /db_xref="CDD:240402"
     Region          80..90
                     /region_name="'HIGH' region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HA77.1)"
     Region          124..127
                     /region_name="'KIIK' region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HA77.1)"
     Region          317..321
                     /region_name="'KMSKS' region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HA77.1)"
     CDS             1..564
                     /gene="CARS2"
                     /gene_synonym="COXPD27; cysRS"
                     /coded_by="NM_024537.4:24..1718"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9514.1"
                     /db_xref="GeneID:79587"
                     /db_xref="HGNC:HGNC:25695"
                     /db_xref="MIM:612800"
ORIGIN      
        1 mlrttrgpgl gppllqaalg lgragwhwpa graasggrgr awlqptgret gvqvynsltg
       61 rkeplivaha eaaswyscgp tvydhahlgh acsyvrfdii rriltkvfgc sivmvmgitd
      121 vddkiikran emnispasla slyeedfkqd maalkvlppt vylrvtenip qiisfiegii
      181 argnaystak gnvyfdlksr gdkygklvgv vpgpvgepad sdkrhasdfa lwkaakpqev
      241 fwaspwgpgr pgwhiecsai asmvfgsqld ihsggidlaf phheneiaqc evfhqceqwg
      301 nyflhsghlh akgkeekmsk slknyitikd flktfspdvf rffclrssyr saidysdsam
      361 lqaqqlllgl gsfledaray mkgqlacgsv reamlwerls stkravkaal addfdtprvv
      421 dailglahhg ngqlraslke pegprspavf gaiisyfeqf fetvgislan qqyvsgdgse
      481 atlhgvvdel vrfrqkvrqf alampeatgd arrqqllerq plleacdtlr rgltahgini
      541 kdrssttstw elldqrtkdq ksag
//
LOCUS       NP_056322                553 aa            linear   PRI 27-APR-2025
DEFINITION  epidermal growth factor-like protein 6 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_056322
VERSION     NP_056322.2
DBSOURCE    REFSEQ: accession NM_015507.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Hamze Sinno,S., Imperatore,J.A., Bai,S., Gomes-Jourdan,N.,
            Mafarachisi,N., Coronnello,C., Zhang,L., Jasarevic,E.,
            Osmanbeyoglu,H.U., Buckanovich,R.J. and Cascio,S.
  TITLE     Egfl6 promotes ovarian cancer progression by enhancing the
            immunosuppressive functions of tumor-associated myeloid cells
  JOURNAL   J Clin Invest 134 (21), e175147 (2024)
   PUBMED   39312740
  REMARK    GeneRIF: Egfl6 promotes ovarian cancer progression by enhancing the
            immunosuppressive functions of tumor-associated myeloid cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Hsu,H.T., Lin,Y.M., Hsing,M.T., Yeh,K.T., Lu,J.W. and Yang,S.F.
  TITLE     Cytoplasmic Expression of the EGFL6 Protein Is an Independent
            Prognostic Factor for Shortened Patient Survival in Human
            Hepatocellular Carcinoma
  JOURNAL   In Vivo 38 (5), 2455-2463 (2024)
   PUBMED   39187367
  REMARK    GeneRIF: Cytoplasmic Expression of the EGFL6 Protein Is an
            Independent Prognostic Factor for Shortened Patient Survival in
            Human Hepatocellular Carcinoma.
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Garrett,A.A., Bai,S., Cascio,S., Gupta,N., Yang,D. and
            Buckanovich,R.J.
  TITLE     EGFL6 promotes endometrial cancer cell migration and proliferation
  JOURNAL   Gynecol Oncol 185, 75-82 (2024)
   PUBMED   38368816
  REMARK    GeneRIF: EGFL6 promotes endometrial cancer cell migration and
            proliferation.
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Landgraf,K., Kuhnapfel,A., Schlanstein,M., Biemann,R., Isermann,B.,
            Kempf,E., Kirsten,H., Scholz,M. and Korner,A.
  TITLE     Transcriptome Analyses of Adipose Tissue Samples Identify EGFL6 as
            a Candidate Gene Involved in Obesity-Related Adipose Tissue
            Dysfunction in Children
  JOURNAL   Int J Mol Sci 23 (8), 4349 (2022)
   PUBMED   35457174
  REMARK    GeneRIF: Transcriptome Analyses of Adipose Tissue Samples Identify
            EGFL6 as a Candidate Gene Involved in Obesity-Related Adipose
            Tissue Dysfunction in Children.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Liu,H. and Wang,X.
  TITLE     Epidermal growth factor-like domain protein 6 recombinant protein
            facilitates osteogenic differentiation in adipose stem cells via
            bone morphogenetic protein 2/recombinant mothers against
            decapentaplegic homolog 4 signaling pathway
  JOURNAL   Bioengineered 13 (3), 6558-6566 (2022)
   PUBMED   35220882
  REMARK    GeneRIF: Epidermal growth factor-like domain protein 6 recombinant
            protein facilitates osteogenic differentiation in adipose stem
            cells via bone morphogenetic protein 2/recombinant mothers against
            decapentaplegic homolog 4 signaling pathway.
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Wang,X., Gong,Y., Wang,D., Xie,Q., Zheng,M., Zhou,Y., Li,Q.,
            Yang,Z., Tang,H., Li,Y., Hu,R., Chen,X. and Mao,Y.
  TITLE     Analysis of gene expression profiling in meningioma: deregulated
            signaling pathways associated with meningioma and EGFL6
            overexpression in benign meningioma tissue and serum
  JOURNAL   PLoS One 7 (12), e52707 (2012)
   PUBMED   23285163
  REMARK    GeneRIF: EGFL6 was overexpressed in benign meningioma tissues and
            serum.
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Oberauer,R., Rist,W., Lenter,M.C., Hamilton,B.S. and Neubauer,H.
  TITLE     EGFL6 is increasingly expressed in human obesity and promotes
            proliferation of adipose tissue-derived stromal vascular cells
  JOURNAL   Mol Cell Biochem 343 (1-2), 257-269 (2010)
   PUBMED   20574786
  REMARK    GeneRIF: results indicate that human EGFL6 is a paracrine/autocrine
            growth factor of adipose tissue up-regulated in obesity and
            potentially involved in the process of adipose tissue expansion and
            the development of obesity
REFERENCE   8  (residues 1 to 553)
  AUTHORS   Lee,S.H., Jeong,E.G., Soung,Y.H., Lee,J.W., Yoo,N.J. and Lee,S.H.
  TITLE     Absence of GNAS and EGFL6 mutations in common human cancers
  JOURNAL   Pathology 40 (1), 95-97 (2008)
   PUBMED   18038328
  REMARK    GeneRIF: There is an absence of GNAS and EGFL6 mutations in common
            human cancers.
REFERENCE   9  (residues 1 to 553)
  AUTHORS   Buchner,G., Orfanelli,U., Quaderi,N., Bassi,M.T., Andolfi,G.,
            Ballabio,A. and Franco,B.
  TITLE     Identification of a new EGF-repeat-containing gene from human Xp22:
            a candidate for developmental disorders
  JOURNAL   Genomics 65 (1), 16-23 (2000)
   PUBMED   10777661
REFERENCE   10 (residues 1 to 553)
  AUTHORS   Yeung,G., Mulero,J.J., Berntsen,R.P., Loeb,D.B., Drmanac,R. and
            Ford,J.E.
  TITLE     Cloning of a novel epidermal growth factor repeat containing gene
            EGFL6: expressed in tumor and fetal tissues
  JOURNAL   Genomics 62 (2), 304-307 (1999)
   PUBMED   10610727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC380958.1, DA534733.1 and
            BC038587.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 26, 2001 this sequence version replaced NP_056322.1.
            
            Summary: This gene encodes a member of the epidermal growth factor
            (EGF) repeat superfamily. Members of this superfamily are
            characterized by the presence of EGF-like repeats and are often
            involved in the regulation of cell cycle, proliferation, and
            developmental processes. The gene product contains a signal
            peptide, suggesting that it is secreted; an EGF repeat region
            consisting of 4 complete EGF-like repeats and 1 partial EGF-like
            repeat, 3 of which have a calcium-binding consensus sequence; an
            arg-gly-asp integrin association motif; and a MAM domain, which is
            believed to have an adhesive function. This gene is expressed early
            during development, and its expression has been detected in lung
            and meningioma tumors. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the shorter isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF186084.1, AK075214.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361306.6/ ENSP00000355126.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..553
                     /product="epidermal growth factor-like protein 6 isoform 1
                     precursor"
                     /note="MAM and EGF domain containing; EGF
                     repeat-containing protein 6; epidermal growth factor-like
                     protein 6; EGF-like protein 6; MAM and EGF
                     domains-containing gene protein"
                     /calculated_mol_wt=59110
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2226
     mat_peptide     19..553
                     /product="epidermal growth factor-like protein 6 isoform
                     1"
                     /calculated_mol_wt=59371
     Region          94..125
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(94,97,111)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          174..202
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF domain; pfam07645"
                     /db_xref="CDD:429571"
     Site            order(174,177,193)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          223..258
                     /region_name="EGF_3"
                     /note="EGF domain; pfam12947"
                     /db_xref="CDD:463759"
     Region          291..350
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX8.1)"
     Site            397
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IUX8.1)"
     Region          402..544
                     /region_name="MAM"
                     /note="Meprin, A5 protein, and protein tyrosine
                     phosphatase Mu (MAM) domain. MAM is an extracellular
                     domain which mediates protein-protein interactions and is
                     found in a diverse set of proteins, many of which are
                     known to function in cell adhesion. Members...; cd06263"
                     /db_xref="CDD:99706"
     CDS             1..553
                     /gene="EGFL6"
                     /gene_synonym="MAEG; W80"
                     /coded_by="NM_015507.4:262..1923"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS14155.1"
                     /db_xref="GeneID:25975"
                     /db_xref="HGNC:HGNC:3235"
                     /db_xref="MIM:300239"
ORIGIN      
        1 mplpwslalp lllswvaggf gnaasarhhg llasarqpgv chygtklacc ygwrrnskgv
       61 ceatcepgck fgecvgpnkc rcfpgytgkt csqdvnecgm kprpcqhrcv nthgsykcfc
      121 lsghmlmpda tcvnsrtcam incqyscedt eegpqclcps sglrlapngr dcldidecas
      181 gkvicpynrr cvntfgsyyc kchigfelqy isgrydcidi nectmdshtc shhancfntq
      241 gsfkckckqg ykgnglrcsa ipensvkevl rapgtikdri kkllahknsm kkkakiknvt
      301 peptrtptpk vnlqpfnyee ivsrggnshg gkkgneekmk egledekree kalkndieer
      361 slrgdvffpk vneagefgli lvqrkaltsk lehkdlnisv dcsfnhgicd wkqdreddfd
      421 wnpadrdnai gfymavpala ghkkdigrlk lllpdlqpqs nfcllfdyrl agdkvgklrv
      481 fvknsnnala wekttsedek wktgkiqlyq gtdatksiif eaergkgktg eiavdgvllv
      541 sglcpdslls vdd
//
LOCUS       NP_001347672             156 aa            linear   ROD 27-APR-2025
DEFINITION  acyl carrier protein, mitochondrial precursor [Mus musculus].
ACCESSION   NP_001347672
VERSION     NP_001347672.1
DBSOURCE    REFSEQ: accession NM_001360743.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Vercellino,I. and Sazanov,L.A.
  TITLE     SCAF1 drives the compositional diversity of mammalian respirasomes
  JOURNAL   Nat Struct Mol Biol 31 (7), 1061-1071 (2024)
   PUBMED   38575788
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Zhang,R., Hou,T., Cheng,H. and Wang,X.
  TITLE     NDUFAB1 protects against obesity and insulin resistance by
            enhancing mitochondrial metabolism
  JOURNAL   FASEB J 33 (12), 13310-13322 (2019)
   PUBMED   31530015
  REMARK    GeneRIF: Skeletal muscle-specific ablation of NDUFAB1 disrupts
            glucose homeostasis and results in obesity and insulin resistance.
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Boniecki,M.T., Freibert,S.A., Muhlenhoff,U., Lill,R. and Cygler,M.
  TITLE     Structure and functional dynamics of the mitochondrial Fe/S cluster
            synthesis complex
  JOURNAL   Nat Commun 8 (1), 1287 (2017)
   PUBMED   29097656
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Gakh,O., Ranatunga,W., Smith,D.Y. 4th, Ahlgren,E.C.,
            Al-Karadaghi,S., Thompson,J.R. and Isaya,G.
  TITLE     Architecture of the Human Mitochondrial Iron-Sulfur Cluster
            Assembly Machinery
  JOURNAL   J Biol Chem 291 (40), 21296-21321 (2016)
   PUBMED   27519411
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Wirtz,S. and Schuelke,M.
  TITLE     Region-specific expression of mitochondrial complex I genes during
            murine brain development
  JOURNAL   PLoS One 6 (4), e18897 (2011)
   PUBMED   21556144
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Wertz,K. and Herrmann,B.G.
  TITLE     Large-scale screen for genes involved in gonad development
  JOURNAL   Mech Dev 98 (1-2), 51-70 (2000)
   PUBMED   11044607
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC124379.3 and BF019966.1.
            
            Transcript Variant: This variant (2) differs in the 3' UTR compared
            to variant 1. Variants 1, 2, and 3 all encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BF019966.1, SRR7652917.1043976.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164137, SAMN01164143
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 65.38 cM"
     Protein         1..156
                     /product="acyl carrier protein, mitochondrial precursor"
                     /note="acyl carrier protein, mitochondrial;
                     NADH-ubiquinone oxidoreductase 9.6 kDa subunit; NADH
                     dehydrogenase (ubiquinone) 1, alpha/beta subcomplex, 1"
                     /calculated_mol_wt=10096
     transit_peptide 1..68
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9CR21.1)"
                     /calculated_mol_wt=7293
     Region          <66..152
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; cl09936"
                     /db_xref="CDD:447865"
     mat_peptide     69..156
                     /product="Acyl carrier protein, mitochondrial.
                     /id=PRO_0000000562"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CR21.1)"
                     /calculated_mol_wt=10096
     Site            88
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CR21.1)"
     CDS             1..156
                     /gene="Ndufab1"
                     /gene_synonym="2210401F17Rik; 2310039H15Rik;
                     2610003B19Rik; 8kDa; 9130423F15Rik; ACP; CI-SDAP; SDAP"
                     /coded_by="NM_001360743.1:27..497"
                     /db_xref="CCDS:CCDS21809.1"
                     /db_xref="GeneID:70316"
                     /db_xref="MGI:MGI:1917566"
ORIGIN      
        1 masrvlcacv rrlpaafapl prlptlalar plsttlcpeg irrrpgalqs alalaqvpgt
       61 vthlcrqysd appltldgik drvlyvlkly dkidpeklsv nshfmkdlgl dsldqveiim
      121 amedefgfei pdidaeklmc pqeivdyiad kkdvye
//
LOCUS       NP_001180481            1090 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 850 isoform 1 [Homo sapiens].
ACCESSION   NP_001180481
VERSION     NP_001180481.1
DBSOURCE    REFSEQ: accession NM_001193552.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC052603.1, AC020928.7 and AC074138.5.
            
            Transcript Variant: This variant (1) is the longer transcript and
            encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC136266.1, SRR1163658.407666.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267752 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000591344.2/ ENSP00000464976.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..1090
                     /product="zinc finger protein 850 isoform 1"
                     /note="putative zinc finger protein ENSP00000330994"
                     /calculated_mol_wt=125301
     Region          7..67
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          199..219
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          227..244
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          243..659
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          255..275
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          283..303
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          311..331
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(316,318,320,322..323,326..327,330,344,346,350..351,
                     354..355,358,372,374,376,378..379,382..383,386)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          339..359
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          367..387
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          395..415
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          423..443
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(428,430,432,434..435,438..439,442,456,458,462..463,
                     466..467,470,484,486,488,490..491,494..495,498)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          451..471
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          479..499
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          507..527
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          531..947
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          535..555
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(540,542,544,546..547,550..551,554,568,570,574..575,
                     578..579,582,596,598,600,602..603,606..607,610)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          563..583
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          591..611
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          619..639
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(624,626,628,630..631,634..635,638,652,654,658..659,
                     662..663,666,680,682,684,686..687,690..691,694)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          647..667
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          675..695
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          703..723
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          732..751
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          759..779
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          787..807
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          815..835
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          843..863
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          871..891
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          899..919
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(904,906,908,910..911,914..915,918,932,934,938..939,
                     942..943,946,960,962,964,966..967,970..971,974)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          927..947
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          955..975
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          967..992
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          983..1003
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <1005..1083
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          1011..1031
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1039..1059
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1067..1087
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1090
                     /gene="ZNF850"
                     /gene_synonym="ZNF850P"
                     /coded_by="NM_001193552.2:153..3425"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS59379.1"
                     /db_xref="GeneID:342892"
                     /db_xref="HGNC:HGNC:27994"
ORIGIN      
        1 mnmeglvmfq dlsidfsqee wecldaaqkd lyrdvmmeny sslvslglsi pkpdvislle
       61 qgkepwmvsr dvlggwcrds efrcktkdsc lpkeiyevts sqwvrmekch slvgssvrdd
      121 weckgqfqhq dinqerylek aimtyettpt fclqtsltlh hrihpgekly kstecmafky
      181 gseltqqqet htgeklykck ecgkafhhfs ylvkhqriht gekpcackey gkafisgshl
      241 iqhqkmytde rphecqesvk afrpsahliq hwrihtgdkp yeckecgksf tsgstlnqhq
      301 qihtgekpyh ckqcgksftv gstlirhqqi htgekpydck ecgksfasgs alirhqriht
      361 gekpydckec gksftfhsal irhqrihtge kpydckecgk sftfrsglig hqaihtgekp
      421 ydckecgksf tagstliqhq rihtgekpyd ckecgksfas gsallqhqri htgekpycck
      481 ecgksftfrs trnrhqriht gekpynckec gksfasgsal lqhqrihtge kpyhckecgk
      541 sftfrsglig hqavhtgekp ydckecgksf tsrsaliqhq rihtgekpyh ckecgksftv
      601 gstllqhqqi htgekpydck ecgkafrlrl rltqhqqiht gekpyqcqec gkafvsvsgl
      661 tqhhrihtge kpyecpdcgk afrqrtylnq hrrihtgekp yeckecgksf tfcsgliqhq
      721 qnhtdekpyd gkecgksfts hstliqhqqi htgekpydck ecgksftshs tliqhqqiht
      781 geklydckec gksftshstl iqhqplhtge kpyhckecgk sftlrsaliq hrpvhtgekr
      841 ysckecgksf tsrstliehq rihtgekpyh ckecgksfaf rsaiiqhrri htgekpydck
      901 ecgkafrrrs kltqhqriht gekpyrchec gkafvrfsgl tkhhsihtge kpyecktcgk
      961 sfrqrthltl hqrihtgdrp yeckecgksf tcgselirhq rthtgekpyd ckecgkafrc
     1021 psqlsqhkri htgektyqcp ecgkaffyas glsrhqsvht gekpyecktc gkafkqltql
     1081 trhqrihdlt
//
LOCUS       NP_055187                154 aa            linear   PRI 27-APR-2025
DEFINITION  RING finger protein 11 [Homo sapiens].
ACCESSION   NP_055187
VERSION     NP_055187.1
DBSOURCE    REFSEQ: accession NM_014372.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Mihalic,F., Simonetti,L., Giudice,G., Sander,M.R., Lindqvist,R.,
            Peters,M.B.A., Benz,C., Kassa,E., Badgujar,D., Inturi,R., Ali,M.,
            Krystkowiak,I., Sayadi,A., Andersson,E., Aronsson,H., Soderberg,O.,
            Dobritzsch,D., Petsalaki,E., Overby,A.K., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Large-scale phage-based screening reveals extensive pan-viral
            mimicry of host short linear motifs
  JOURNAL   Nat Commun 14 (1), 2409 (2023)
   PUBMED   37100772
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Chen,S., Xu,K., Kong,D., Wu,L., Chen,Q., Ma,X., Ma,S., Li,T.,
            Xie,Q., Liu,H. and Luo,L.
  TITLE     Ubiquitin ligase OsRINGzf1 regulates drought resistance by
            controlling the turnover of OsPIP2;1
  JOURNAL   Plant Biotechnol J 20 (9), 1743-1755 (2022)
   PUBMED   35587579
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Deng,W., Long,T. and Du,Y.
  TITLE     [Mechanism of ring finger protein 11 regulating Akt signaling
            pathway to promote osteogenic differentiation of bone marrow
            mesenchymal stem cells]
  JOURNAL   Zhongguo Xiu Fu Chong Jian Wai Ke Za Zhi 36 (1), 102-110 (2022)
   PUBMED   35038807
  REMARK    GeneRIF: [Mechanism of ring finger protein 11 regulating Akt
            signaling pathway to promote osteogenic differentiation of bone
            marrow mesenchymal stem cells].
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Subramaniam,V., Li,H., Wong,M., Kitching,R., Attisano,L., Wrana,J.,
            Zubovits,J., Burger,A.M. and Seth,A.
  TITLE     The RING-H2 protein RNF11 is overexpressed in breast cancer and is
            a target of Smurf2 E3 ligase
  JOURNAL   Br J Cancer 89 (8), 1538-1544 (2003)
   PUBMED   14562029
  REMARK    GeneRIF: overexpression of RNF11, through its interaction with
            Smurf2, can restore TGFbeta responsiveness in transfected tumor
            cells
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Kitching,R., Wong,M.J., Koehler,D., Burger,A.M., Landberg,G.,
            Gish,G. and Seth,A.
  TITLE     The RING-H2 protein RNF11 is differentially expressed in breast
            tumours and interacts with HECT-type E3 ligases
  JOURNAL   Biochim Biophys Acta 1639 (2), 104-112 (2003)
   PUBMED   14559117
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Watanabe,T., Ichihara,M., Hashimoto,M., Shimono,K., Shimoyama,Y.,
            Nagasaka,T., Murakumo,Y., Murakami,H., Sugiura,H., Iwata,H.,
            Ishiguro,N. and Takahashi,M.
  TITLE     Characterization of gene expression induced by RET with MEN2A or
            MEN2B mutation
  JOURNAL   Am J Pathol 161 (1), 249-256 (2002)
   PUBMED   12107109
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Jolliffe,C.N., Harvey,K.F., Haines,B.P., Parasivam,G. and Kumar,S.
  TITLE     Identification of multiple proteins expressed in murine embryos as
            binding partners for the WW domains of the ubiquitin-protein ligase
            Nedd4
  JOURNAL   Biochem J 351 Pt 3 (Pt 3), 557-565 (2000)
   PUBMED   11042109
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Seki,N., Hattori,A., Hayashi,A., Kozuma,S., Sasaki,M., Suzuki,Y.,
            Sugano,S., Muramatsu,M.A. and Saito,T.
  TITLE     Cloning and expression profile of mouse and human genes,
            Rnf11/RNF11, encoding a novel RING-H2 finger protein
  JOURNAL   Biochim Biophys Acta 1489 (2-3), 421-427 (1999)
   PUBMED   10673045
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB265274.1, BC047654.1,
            BC036670.1, BC020964.2, DB564333.1 and AA224090.1.
            
            Summary: The protein encoded by this gene contains a RING-H2 finger
            motif, which is known to be important for protein-protein
            interactions. The expression of this gene has been shown to be
            induced by mutant RET proteins (MEN2A/MEN2B). The germline
            mutations in RET gene are known to be responsible for the
            development of multiple endocrine neoplasia (MEN). [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.213058.1,
                                           SRR1660803.151881.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242719.4/ ENSP00000242719.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..154
                     /product="RING finger protein 11"
                     /calculated_mol_wt=17313
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3C5.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3C5.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYK7; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3C5.1)"
     Region          37..40
                     /region_name="PPxY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3C5.1)"
     Region          98..140
                     /region_name="RING-H2_RNF11"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 11 (RNF11) and similar proteins; cd16468"
                     /db_xref="CDD:438131"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:16123141; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3C5.1)"
     CDS             1..154
                     /gene="RNF11"
                     /gene_synonym="CGI-123; SID1669"
                     /coded_by="NM_014372.5:485..949"
                     /db_xref="CCDS:CCDS556.1"
                     /db_xref="GeneID:26994"
                     /db_xref="HGNC:HGNC:10056"
                     /db_xref="MIM:612598"
ORIGIN      
        1 mgnclkspts ddisllhesq sdrasfgegt epdqeppppy qeqvpvpvyh ptpsqtrlat
       61 qlteeeqiri aqrigliqhl pkgvydpgrd gsekkirecv icmmdfvygd pirflpcmhi
      121 yhldciddwl mrsftcpscm epvdaallss yetn
//
LOCUS       NP_001129734              97 aa            linear   PRI 27-APR-2025
DEFINITION  ataxin-7-like protein 3B [Homo sapiens].
ACCESSION   NP_001129734
VERSION     NP_001129734.1
DBSOURCE    REFSEQ: accession NM_001136262.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Chen,B., Cha,J.H., Yan,M., Cao,N., Ye,P., Yan,X. and Yang,W.H.
  TITLE     ATXN7L3B promotes hepatocellular carcinoma stemness and is
            downregulated by metformin
  JOURNAL   Biochem Biophys Res Commun 573, 1-8 (2021)
   PUBMED   34375763
  REMARK    GeneRIF: ATXN7L3B promotes hepatocellular carcinoma stemness and is
            downregulated by metformin.
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Woldegebriel,R., Kvist,J., Andersson,N., Ounap,K., Reinson,K.,
            Wojcik,M.H., Bijlsma,E.K., Hoffer,M.J.V., Ryan,M.M., Stark,Z.,
            Walsh,M., Cuppen,I., van den Boogaard,M.H., Bharucha-Goebel,D.,
            Donkervoort,S., Winchester,S., Zori,R., Bonnemann,C.G.,
            Maroofian,R., O'Connor,E., Houlden,H., Zhao,F., Carpen,O.,
            White,M., Sreedharan,J., Stewart,M., Ylikallio,E. and Tyynismaa,H.
  TITLE     Distinct effects on mRNA export factor GANP underlie neurological
            disease phenotypes and alter gene expression depending on intron
            content
  JOURNAL   Hum Mol Genet 29 (9), 1426-1439 (2020)
   PUBMED   32202298
  REMARK    GeneRIF: Distinct effects on mRNA export factor GANP underlie
            neurological disease phenotypes and alter gene expression depending
            on intron content.
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Leberfarb,E.Y., Degtyareva,A.O., Brusentsov,I.I., Maximov,V.N.,
            Voevoda,M.I., Autenshlus,A.I., Morozov,D.V., Sokolov,A.V. and
            Merkulova,T.I.
  TITLE     Potential regulatory SNPs in the ATXN7L3B and KRT15 genes are
            associated with gender-specific colorectal cancer risk
  JOURNAL   Per Med 17 (1), 43-54 (2020)
   PUBMED   31797724
  REMARK    GeneRIF: Potential regulatory SNPs in the ATXN7L3B and KRT15 genes
            are associated with gender-specific colorectal cancer risk.
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Li,W., Atanassov,B.S., Lan,X., Mohan,R.D., Swanson,S.K.,
            Farria,A.T., Florens,L., Washburn,M.P., Workman,J.L. and
            Dent,S.Y.R.
  TITLE     Cytoplasmic ATXN7L3B Interferes with Nuclear Functions of the SAGA
            Deubiquitinase Module
  JOURNAL   Mol Cell Biol 36 (22), 2855-2866 (2016)
   PUBMED   27601583
  REMARK    GeneRIF: Study reports that ATXN7L3B interacts with ENY2 but not
            other SAGA components. Even though ATXN7L3B localizes in the
            cytoplasm, ATXN7L3B overexpression increases H2Bub1 levels, while
            overexpression of ATXN7L3 decreases H2Bub1 levels.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Tan,J.Y., Vance,K.W., Varela,M.A., Sirey,T., Watson,L.M.,
            Curtis,H.J., Marinello,M., Alves,S., Steinkraus,B., Cooper,S.,
            Nesterova,T., Brockdorff,N., Fulga,T., Brice,A., Sittler,A.,
            Oliver,P.L., Wood,M.J., Ponting,C.P. and Marques,A.C.
  TITLE     Cross-talking noncoding RNAs contribute to cell-specific
            neurodegeneration in SCA7
  JOURNAL   Nat Struct Mol Biol 21 (11), 955-961 (2014)
   PUBMED   25306109
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Mar;22(3):272. doi:
            10.1038/nsmb0315-272b. PMID: 25736092]
REFERENCE   6  (residues 1 to 97)
  AUTHORS   Rajakulendran,S., Roberts,J., Koltzenburg,M., Hanna,M.G. and
            Stewart,H.
  TITLE     Deletion of chromosome 12q21 affecting KCNC2 and ATXN7L3B in a
            family with neurodevelopmental delay and ataxia
  JOURNAL   J Neurol Neurosurg Psychiatry 84 (11), 1255-1257 (2013)
   PUBMED   23475819
  REMARK    GeneRIF: This family's complex phenotype is associated with a new
            chromosomal deletion, which suggests potential roles for the two
            genes, KCNC2 and ATXN7L3B, in human neurological disease.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025257.22.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR1803614.17557.1, SRR1803616.148482.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000519948.4/ ENSP00000430000.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.1"
     Protein         1..97
                     /product="ataxin-7-like protein 3B"
                     /note="putative ataxin-7-like protein 3B"
                     /calculated_mol_wt=10640
     Region          77..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GX2.2)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UD01; propagated from
                     UniProtKB/Swiss-Prot (Q96GX2.2)"
     CDS             1..97
                     /gene="ATXN7L3B"
                     /gene_synonym="lnc-SCA7"
                     /coded_by="NM_001136262.2:279..572"
                     /db_xref="CCDS:CCDS53815.1"
                     /db_xref="GeneID:552889"
                     /db_xref="HGNC:HGNC:37931"
                     /db_xref="MIM:615579"
ORIGIN      
        1 meeislanld tnkleaiaqe iyvdliedsc lgfcfevhra vkcgyfylef aetgsvkdfg
       61 iqpvedkgac rlplcslpge pgngpdqqlq rsppefq
//
LOCUS       NP_653171                190 aa            linear   PRI 27-APR-2025
DEFINITION  jupiter microtubule associated homolog 2 isoform 4 [Homo sapiens].
ACCESSION   NP_653171
VERSION     NP_653171.1
DBSOURCE    REFSEQ: accession NM_144570.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Chen,X., Song,Q.L., Ji,R., Wang,J.Y., Cao,M.L., Guo,D.Y., Zhang,Y.
            and Yang,J.
  TITLE     JPT2 Affects Trophoblast Functions and Macrophage Polarization and
            Metabolism, and Acts as a Potential Therapeutic Target for
            Recurrent Spontaneous Abortion
  JOURNAL   Adv Sci (Weinh) 11 (16), e2306359 (2024)
   PUBMED   38417123
  REMARK    GeneRIF: JPT2 Affects Trophoblast Functions and Macrophage
            Polarization and Metabolism, and Acts as a Potential Therapeutic
            Target for Recurrent Spontaneous Abortion.
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Gunaratne,G.S., Brailoiu,E., Kumar,S., Yuan,Y., Slama,J.T.,
            Walseth,T.F., Patel,S. and Marchant,J.S.
  TITLE     Convergent activation of two-pore channels mediated by the
            NAADP-binding proteins JPT2 and LSM12
  JOURNAL   Sci Signal 16 (799), eadg0485 (2023)
   PUBMED   37607218
  REMARK    GeneRIF: Convergent activation of two-pore channels mediated by the
            NAADP-binding proteins JPT2 and LSM12.
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Zeng,T.T., Deng,T.H., Liu,Z., Zhan,J.R., Ma,Y.Z., Yan,Y.Y., Sun,X.,
            Zhu,Y.H., Li,Y., Guan,X.Y. and Li,L.
  TITLE     HN1L/AP-2gamma/PLK1 signaling drives tumor progression and
            chemotherapy resistance in esophageal squamous cell carcinoma
  JOURNAL   Cell Death Dis 13 (12), 1026 (2022)
   PUBMED   36476988
  REMARK    GeneRIF: HN1L/AP-2gamma/PLK1 signaling drives tumor progression and
            chemotherapy resistance in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Nong,S., Wang,Z., Wei,Z., Ma,L., Guan,Y. and Ni,J.
  TITLE     HN1L promotes stem cell-like properties by regulating TGF-beta
            signaling pathway through targeting FOXP2 in prostate cancer
  JOURNAL   Cell Biol Int 46 (1), 83-95 (2022)
   PUBMED   34519127
  REMARK    GeneRIF: HN1L promotes stem cell-like properties by regulating
            TGF-beta signaling pathway through targeting FOXP2 in prostate
            cancer.
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Roggenkamp,H.G., Khansahib,I., Hernandez,C. LC, Zhang,Y.,
            Lodygin,D., Kruger,A., Gu,F., Mockl,F., Lohndorf,A., Wolters,V.,
            Woike,D., Rosche,A., Bauche,A., Schetelig,D., Werner,R.,
            Schluter,H., Failla,A.V., Meier,C., Fliegert,R., Walseth,T.F.,
            Flugel,A., Diercks,B.P. and Guse,A.H.
  TITLE     HN1L/JPT2: A signaling protein that connects NAADP generation to
            Ca2+ microdomain formation
  JOURNAL   Sci Signal 14 (675) (2021)
   PUBMED   33758062
  REMARK    GeneRIF: HN1L/JPT2: A signaling protein that connects NAADP
            generation to Ca(2+) microdomain formation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 190)
  AUTHORS   Karpova,N., Bobinnec,Y., Fouix,S., Huitorel,P. and Debec,A.
  TITLE     Jupiter, a new Drosophila protein associated with microtubules
  JOURNAL   Cell Motil Cytoskeleton 63 (5), 301-312 (2006)
   PUBMED   16518797
REFERENCE   7  (residues 1 to 190)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 190)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
REFERENCE   9  (residues 1 to 190)
  AUTHORS   Zhou,G., Wang,J., Zhang,Y., Zhong,C., Ni,J., Wang,L., Guo,J.,
            Zhang,K., Yu,L. and Zhao,S.
  TITLE     Cloning, expression and subcellular localization of HN1 and HN1L
            genes, as well as characterization of their orthologs, defining an
            evolutionarily conserved gene family
  JOURNAL   Gene 331, 115-123 (2004)
   PUBMED   15094197
REFERENCE   10 (residues 1 to 190)
  AUTHORS   Daniels,R.J., Peden,J.F., Lloyd,C., Horsley,S.W., Clark,K.,
            Tufarelli,C., Kearney,L., Buckle,V.J., Doggett,N.A., Flint,J. and
            Higgs,D.R.
  TITLE     Sequence, structure and pathology of the fully annotated terminal 2
            Mb of the short arm of human chromosome 16
  JOURNAL   Hum Mol Genet 10 (4), 339-352 (2001)
   PUBMED   11157797
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM837125.1, AK023154.1, BC060853.1, BM474060.1 and AL031710.11.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023154.1, BC060853.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248098.8/ ENSP00000248098.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..190
                     /product="jupiter microtubule associated homolog 2 isoform
                     4"
                     /note="hematological and neurological expressed 1-like
                     protein; HN1 like; CRAMP_1 like; HN1-like protein;
                     hematological and neurological expressed 1 like"
                     /calculated_mol_wt=19932
     Region          1..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H910.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H910.1)"
     Region          10..>48
                     /region_name="JUPITER"
                     /note="Microtubule-Associated protein Jupiter; pfam17054"
                     /db_xref="CDD:293659"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H910.1)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H910.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H910.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H910.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H910.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H910.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H910.1)"
     CDS             1..190
                     /gene="JPT2"
                     /gene_synonym="C16orf34; HN1L; L11"
                     /coded_by="NM_144570.3:35..607"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS10441.1"
                     /db_xref="GeneID:90861"
                     /db_xref="HGNC:HGNC:14137"
                     /db_xref="MIM:619241"
ORIGIN      
        1 mfqvpdsegg ragsramkpp ggessnlfgs peeatpssrp nrmasnifgp teepqnipkr
       61 tnppggkgsg ifdestpvqt rqhlnppggk tsdifgspvt atsrlahpnk pkdhvflceg
      121 eepksdlkaa rsipagaepg ekgsarkagp akeqepmptv dsheprlgpr prshnkvlnp
      181 pggkssisfy
//
LOCUS       NP_003146                247 aa            linear   PRI 27-APR-2025
DEFINITION  stanniocalcin-1 precursor [Homo sapiens].
ACCESSION   NP_003146
VERSION     NP_003146.1
DBSOURCE    REFSEQ: accession NM_003155.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Kim,J.H., Kim,K., Kim,I., Seong,S., Koh,J.T. and Kim,N.
  TITLE     Stanniocalcin 1 and 1,25-dihydroxyvitamin D3 cooperatively regulate
            bone mineralization by osteoblasts
  JOURNAL   Exp Mol Med 56 (9), 1991-2001 (2024)
   PUBMED   39218976
  REMARK    GeneRIF: Stanniocalcin 1 and 1,25-dihydroxyvitamin D3 cooperatively
            regulate bone mineralization by osteoblasts.
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Duan,C., He,B., Wang,Y., Liu,W., Bao,W., Yu,L., Xin,J., Gui,H.,
            Lei,J., Yang,Z., Liu,J., Tao,W., Qin,J., Luo,J. and Dong,Z.
  TITLE     Stanniocalcin-1 promotes temozolomide resistance of glioblastoma
            through regulation of MGMT
  JOURNAL   Sci Rep 14 (1), 20199 (2024)
   PUBMED   39215105
  REMARK    GeneRIF: Stanniocalcin-1 promotes temozolomide resistance of
            glioblastoma through regulation of MGMT.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Ren,Z., Xu,Z., Chang,X., Liu,J. and Xiao,W.
  TITLE     STC1 competitively binding betaPIX enhances melanoma progression
            via YAP nuclear translocation and M2 macrophage recruitment through
            the YAP/CCL2/VEGFA/AKT feedback loop
  JOURNAL   Pharmacol Res 204, 107218 (2024)
   PUBMED   38768671
  REMARK    GeneRIF: STC1 competitively binding betaPIX enhances melanoma
            progression via YAP nuclear translocation and M2 macrophage
            recruitment through the YAP/CCL2/VEGFA/AKT feedback loop.
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Choi,S., An,H.J., Yeo,H.J., Sung,M.J., Oh,J., Lee,K., Lee,S.A.,
            Kim,S.K., Kim,J., Kim,I. and Lee,S.
  TITLE     MicroRNA-606 inhibits the growth and metastasis of triple-negative
            breast cancer by targeting Stanniocalcin 1
  JOURNAL   Oncol Rep 51 (1) (2024)
   PUBMED   37975233
  REMARK    GeneRIF: MicroRNA-606 inhibits the growth and metastasis of
            triple-negative breast cancer by targeting Stanniocalcin 1.
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Luo,M., Wang,X., Wu,S., Yang,C., Su,Q., Huang,L., Fu,K., An,S.,
            Xie,F., To,K.K.W., Wang,F. and Fu,L.
  TITLE     A20 promotes colorectal cancer immune evasion by upregulating STC1
            expression to block 'eat-me' signal
  JOURNAL   Signal Transduct Target Ther 8 (1), 312 (2023)
   PUBMED   37607946
  REMARK    GeneRIF: A20 promotes colorectal cancer immune evasion by
            upregulating STC1 expression to block 'eat-me' signal.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Chang,A.C., Jeffrey,K.J., Tokutake,Y., Shimamoto,A., Neumann,A.A.,
            Dunham,M.A., Cha,J., Sugawara,M., Furuichi,Y. and Reddel,R.R.
  TITLE     Human stanniocalcin (STC): genomic structure, chromosomal
            localization, and the presence of CAG trinucleotide repeats
  JOURNAL   Genomics 47 (3), 393-398 (1998)
   PUBMED   9480753
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Olsen,H.S., Cepeda,M.A., Zhang,Q.Q., Rosen,C.A., Vozzolo,B.L. and
            Wagner,G.F.
  TITLE     Human stanniocalcin: a possible hormonal regulator of mineral
            metabolism
  JOURNAL   Proc Natl Acad Sci U S A 93 (5), 1792-1796 (1996)
   PUBMED   8700837
REFERENCE   8  (residues 1 to 247)
  AUTHORS   Chang,A.C., Janosi,J., Hulsbeek,M., de Jong,D., Jeffrey,K.J.,
            Noble,J.R. and Reddel,R.R.
  TITLE     A novel human cDNA highly homologous to the fish hormone
            stanniocalcin
  JOURNAL   Mol Cell Endocrinol 112 (2), 241-247 (1995)
   PUBMED   7489828
REFERENCE   9  (residues 1 to 247)
  AUTHORS   Wagner,G.F., Guiraudon,C.C., Milliken,C. and Copp,D.H.
  TITLE     Immunological and biological evidence for a stanniocalcin-like
            hormone in human kidney
  JOURNAL   Proc Natl Acad Sci U S A 92 (6), 1871-1875 (1995)
   PUBMED   7892193
REFERENCE   10 (residues 1 to 247)
  AUTHORS   Liang,P., Averboukh,L., Keyomarsi,K., Sager,R. and Pardee,A.B.
  TITLE     Differential display and cloning of messenger RNAs from human
            breast cancer versus mammary epithelial cells
  JOURNAL   Cancer Res 52 (24), 6966-6968 (1992)
   PUBMED   1458489
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U25997.1, BC029044.1 and
            AC012119.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a secreted, homodimeric glycoprotein
            that is expressed in a wide variety of tissues and may have
            autocrine or paracrine functions. The gene contains a 5' UTR rich
            in CAG trinucleotide repeats. The encoded protein contains 11
            conserved cysteine residues and is phosphorylated by protein kinase
            C exclusively on its serine residues. The protein may play a role
            in the regulation of renal and intestinal calcium and phosphate
            transport, cell metabolism, or cellular calcium/phosphate
            homeostasis. Overexpression of human stanniocalcin 1 in mice
            produces high serum phosphate levels, dwarfism, and increased
            metabolic rate. This gene has altered expression in hepatocellular,
            ovarian, and breast cancers. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.180030.1, U25997.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465411 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000290271.7/ ENSP00000290271.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..247
                     /product="stanniocalcin-1 precursor"
                     /calculated_mol_wt=25910
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1729
     Region          6..206
                     /region_name="Stanniocalcin"
                     /note="Stanniocalcin family; pfam03298"
                     /db_xref="CDD:397405"
     mat_peptide     18..247
                     /product="stanniocalcin-1"
                     /calculated_mol_wt=25910
     Site            62
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P52823.1)"
     CDS             1..247
                     /gene="STC1"
                     /gene_synonym="STC"
                     /coded_by="NM_003155.3:284..1027"
                     /db_xref="CCDS:CCDS6043.1"
                     /db_xref="GeneID:6781"
                     /db_xref="HGNC:HGNC:11373"
                     /db_xref="MIM:601185"
ORIGIN      
        1 mlqnsavllv lvisasathe aeqndsvspr ksrvaaqnsa evvrclnsal qvgcgafacl
       61 enstcdtdgm ydicksflys aakfdtqgka fvkeslkcia ngvtskvfla irrcstfqrm
      121 iaevqeecys klnvcsiakr npeaitevvq lpnhfsnryy nrlvrsllec dedtvstird
      181 slmekigpnm aslfhilqtd hcaqthprad fnrrrtnepq klkvllrnlr geedspshik
      241 rtshesa
//
LOCUS       NP_001347605             377 aa            linear   ROD 27-APR-2025
DEFINITION  palmitoyltransferase ZDHHC16 isoform 1 [Mus musculus].
ACCESSION   NP_001347605 XP_006527466
VERSION     NP_001347605.1
DBSOURCE    REFSEQ: accession NM_001360676.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Cao,N., Li,J.K., Rao,Y.Q., Liu,H., Wu,J., Li,B., Zhao,P., Zeng,L.
            and Li,J.
  TITLE     A potential role for protein palmitoylation and zDHHC16 in DNA
            damage response
  JOURNAL   BMC Mol Biol 17 (1), 12 (2016)
   PUBMED   27159997
  REMARK    GeneRIF: Knockout of zDHHC16, a palmitoyltransferase gene is
            identified as an interacting protein for c-Abl, a non-receptor
            tyrosine kinase involved in DNA damage response, reproduced most of
            the defects in DNA damage responses produced by the inhibition of
            protein palmitoylation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Fukata,Y., Murakami,T., Yokoi,N. and Fukata,M.
  TITLE     Local Palmitoylation Cycles and Specialized Membrane Domain
            Organization
  JOURNAL   Curr Top Membr 77, 97-141 (2016)
   PUBMED   26781831
  REMARK    Review article
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Zhou,T., Li,J., Zhao,P., Liu,H., Jia,D., Jia,H., He,L., Cang,Y.,
            Boast,S., Chen,Y.H., Thibault,H., Scherrer-Crosbie,M., Goff,S.P.
            and Li,B.
  TITLE     Palmitoyl acyltransferase Aph2 in cardiac function and the
            development of cardiomyopathy
  JOURNAL   Proc Natl Acad Sci U S A 112 (51), 15666-15671 (2015)
   PUBMED   26644582
  REMARK    GeneRIF: Aph2 as a critical in vivo regulator of cardiac function
            and reveal roles for protein palmitoylation in the development of
            other organs including eyes.
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Blaskovic,S., Adibekian,A., Blanc,M. and van der Goot,G.F.
  TITLE     Mechanistic effects of protein palmitoylation and the cellular
            consequences thereof
  JOURNAL   Chem Phys Lipids 180, 44-52 (2014)
   PUBMED   24534427
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Chamberlain,L.H., Lemonidis,K., Sanchez-Perez,M., Werno,M.W.,
            Gorleku,O.A. and Greaves,J.
  TITLE     Palmitoylation and the trafficking of peripheral membrane proteins
  JOURNAL   Biochem Soc Trans 41 (1), 62-66 (2013)
   PUBMED   23356259
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Conibear,E. and Davis,N.G.
  TITLE     Palmitoylation and depalmitoylation dynamics at a glance
  JOURNAL   J Cell Sci 123 (Pt 23), 4007-4010 (2010)
   PUBMED   21084560
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Guo,G., Huss,M., Tong,G.Q., Wang,C., Li Sun,L., Clarke,N.D. and
            Robson,P.
  TITLE     Resolution of cell fate decisions revealed by single-cell gene
            expression analysis from zygote to blastocyst
  JOURNAL   Dev Cell 18 (4), 675-685 (2010)
   PUBMED   20412781
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Evsikov,A.V., Graber,J.H., Brockman,J.M., Hampl,A., Holbrook,A.E.,
            Singh,P., Eppig,J.J., Solter,D. and Knowles,B.B.
  TITLE     Cracking the egg: molecular dynamics and evolutionary aspects of
            the transition from the fully grown oocyte to embryo
  JOURNAL   Genes Dev 20 (19), 2713-2727 (2006)
   PUBMED   17015433
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Li,B., Cong,F., Tan,C.P., Wang,S.X. and Goff,S.P.
  TITLE     Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has
            pro-apoptotic activity
  JOURNAL   J Biol Chem 277 (32), 28870-28876 (2002)
   PUBMED   12021275
  REMARK    GeneRIF: Aph2 may be involved in ER stress-induced apoptosis in
            which c-Abl plays an important role
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC140193.3.
            
            On Feb 9, 2018 this sequence version replaced XP_006527466.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7652917.609976.1,
                                           SRR7345562.2108518.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 35.48 cM"
     Protein         1..377
                     /product="palmitoyltransferase ZDHHC16 isoform 1"
                     /EC_number="2.3.1.225"
                     /note="probable palmitoyltransferase ZDHHC16; ablphilin-2;
                     zinc finger DHHC domain-containing protein 16; Abl-philin
                     2"
                     /calculated_mol_wt=43516
     Region          156..305
                     /region_name="DHHC"
                     /note="DHHC palmitoyltransferase; pfam01529"
                     /db_xref="CDD:396215"
     CDS             1..377
                     /gene="Zdhhc16"
                     /gene_synonym="1500015N03Rik; Aph2"
                     /coded_by="NM_001360676.1:373..1506"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:74168"
                     /db_xref="MGI:MGI:1921418"
ORIGIN      
        1 mrgqrslllg parlclrlll llgyrrrcpp llrglvqrwr ygkvclrsll ynsfggsdta
       61 vdaafepvyw lvdnvirwfg vvfvvlvivl tgsivaiayl cvlplilrty svprlcwhff
      121 yshwnliliv fhyyqaittp pgyppqgrnd iatvsickkc iypkparthh csicnrcvlk
      181 mdhhcpwlnn cvghynhryf fsfcffmtlg cvycsygswd lfreayaaie kmkqldknkl
      241 qaianqtyhq tppptfsfre rithkslvyl wflcssvala lgaltmwhav lisrgetsie
      301 rhinkkerrr lqakgrvfrn pynygcldnw kvflgvdtgr hwltrvllps shlphgngms
      361 wdpppwvtah sasvmav
//
LOCUS       NP_055312               1978 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 638 isoform 1 [Homo sapiens].
ACCESSION   NP_055312
VERSION     NP_055312.2
DBSOURCE    REFSEQ: accession NM_014497.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1978)
  AUTHORS   Das,A., Vijayan,M., Walton,E.M., Stafford,V.G., Fiflis,D.N. and
            Asokan,A.
  TITLE     Epigenetic Silencing of Recombinant Adeno-associated Virus Genomes
            by NP220 and the HUSH Complex
  JOURNAL   J Virol 96 (4), e0203921 (2022)
   PUBMED   34878926
  REMARK    GeneRIF: Epigenetic Silencing of Recombinant Adeno-associated Virus
            Genomes by NP220 and the HUSH Complex.
REFERENCE   2  (residues 1 to 1978)
  AUTHORS   Ni,W., Lin,S., Bian,S., Zheng,W., Qu,L., Fan,Y., Lu,C., Xiao,M. and
            Zhou,P.
  TITLE     USP7 mediates pathological hepatic de novo lipogenesis through
            promoting stabilization and transcription of ZNF638
  JOURNAL   Cell Death Dis 11 (10), 843 (2020)
   PUBMED   33040080
  REMARK    GeneRIF: USP7 mediates pathological hepatic de novo lipogenesis
            through promoting stabilization and transcription of ZNF638.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1978)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 1978)
  AUTHORS   Zhu,Y., Wang,G.Z., Cingoz,O. and Goff,S.P.
  TITLE     NP220 mediates silencing of unintegrated retroviral DNA
  JOURNAL   Nature 564 (7735), 278-282 (2018)
   PUBMED   30487602
  REMARK    GeneRIF: NP220 is the key protein that recruits the HUSH complex,
            SETDB1 and the histone deacetylases HDAC1 and HDAC4 to silence the
            unintegrated retroviral DNA; knockout of NP220 accelerates the
            replication of retroviruses; these experiments identify the
            molecular machinery that silences extrachromosomal retroviral DNA
REFERENCE   5  (residues 1 to 1978)
  AUTHORS   He,M., Xu,M., Zhang,B., Liang,J., Chen,P., Lee,J.Y., Johnson,T.A.,
            Li,H., Yang,X., Dai,J., Liang,L., Gui,L., Qi,Q., Huang,J., Li,Y.,
            Adair,L.S., Aung,T., Cai,Q., Cheng,C.Y., Cho,M.C., Cho,Y.S.,
            Chu,M., Cui,B., Gao,Y.T., Go,M.J., Gu,D., Gu,W., Guo,H., Hao,Y.,
            Hong,J., Hu,Z., Hu,Y., Huang,J., Hwang,J.Y., Ikram,M.K., Jin,G.,
            Kang,D.H., Khor,C.C., Kim,B.J., Kim,H.T., Kubo,M., Lee,J., Lee,J.,
            Lee,N.R., Li,R., Li,J., Liu,J., Longe,J., Lu,W., Lu,X., Miao,X.,
            Okada,Y., Ong,R.T., Qiu,G., Seielstad,M., Sim,X., Song,H.,
            Takeuchi,F., Tanaka,T., Taylor,P.R., Wang,L., Wang,W., Wang,Y.,
            Wu,C., Wu,Y., Xiang,Y.B., Yamamoto,K., Yang,H., Liao,M., Yokota,M.,
            Young,T., Zhang,X., Kato,N., Wang,Q.K., Zheng,W., Hu,F.B., Lin,D.,
            Shen,H., Teo,Y.Y., Mo,Z., Wong,T.Y., Lin,X., Mohlke,K.L., Ning,G.,
            Tsunoda,T., Han,B.G., Shu,X.O., Tai,E.S., Wu,T. and Qi,L.
  TITLE     Meta-analysis of genome-wide association studies of adult height in
            East Asians identifies 17 novel loci
  JOURNAL   Hum Mol Genet 24 (6), 1791-1800 (2015)
   PUBMED   25429064
REFERENCE   6  (residues 1 to 1978)
  AUTHORS   Meruvu,S., Hugendubler,L. and Mueller,E.
  TITLE     Regulation of adipocyte differentiation by the zinc finger protein
            ZNF638
  JOURNAL   J Biol Chem 286 (30), 26516-26523 (2011)
   PUBMED   21602272
  REMARK    GeneRIF: ZNF638 is a novel and early regulator of adipogenesis that
            works as a transcription cofactor of C/EBPs.
REFERENCE   7  (residues 1 to 1978)
  AUTHORS   Ng,E.K., Chan,K.K., Wong,C.H., Tsui,S.K., Ngai,S.M., Lee,S.M.,
            Kotaka,M., Lee,C.Y., Waye,M.M. and Fung,K.P.
  TITLE     Interaction of the heart-specific LIM domain protein, FHL2, with
            DNA-binding nuclear protein, hNP220
  JOURNAL   J Cell Biochem 84 (3), 556-566 (2002)
   PUBMED   11813260
REFERENCE   8  (residues 1 to 1978)
  AUTHORS   Eichmuller,S., Usener,D., Dummer,R., Stein,A., Thiel,D. and
            Schadendorf,D.
  TITLE     Serological detection of cutaneous T-cell lymphoma-associated
            antigens
  JOURNAL   Proc Natl Acad Sci U S A 98 (2), 629-634 (2001)
   PUBMED   11149944
REFERENCE   9  (residues 1 to 1978)
  AUTHORS   Okumara,K., Nogami,M., Matsushima,Y., Matsumura,K., Nakamura,K.,
            Taguchi,H. and Kitagawa,Y.
  TITLE     Mapping of human DNA-binding nuclear protein (NP220) to chromosome
            band 2p13.1-p13.2 and its relation to matrin 3
  JOURNAL   Biosci Biotechnol Biochem 62 (8), 1640-1642 (1998)
   PUBMED   9757574
REFERENCE   10 (residues 1 to 1978)
  AUTHORS   Inagaki,H., Matsushima,Y., Nakamura,K., Ohshima,M., Kadowaki,T. and
            Kitagawa,Y.
  TITLE     A large DNA-binding nuclear protein with RNA recognition motif and
            serine/arginine-rich domain
  JOURNAL   J Biol Chem 271 (21), 12525-12531 (1996)
   PUBMED   8647861
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP348645.1, D83032.1,
            BC143728.1, DB130984.1 and AI357871.1.
            
            On Jun 28, 2002 this sequence version replaced NP_055312.1.
            
            Summary: The protein encoded by this gene is a nucleoplasmic
            protein. It binds cytidine-rich sequences in double-stranded DNA.
            This protein has three types of domains: MH1, MH2 (repeated three
            times) and MH3. It is associated with packaging, transferring, or
            processing transcripts. Multiple alternatively spliced transcript
            variants have been found for this gene, but the biological validity
            of some variants has not been determined. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) encodes isoform 1. Variants 1,
            2 and 3 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D83032.1, SRR1803615.35787.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264447.9/ ENSP00000264447.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1978
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.2"
     Protein         1..1978
                     /product="zinc finger protein 638 isoform 1"
                     /note="NP220 nuclear protein; CTCL tumor antigen se33-1;
                     nuclear protein 220; CTCL-associated antigen se33-1; zinc
                     finger matrin-like protein; cutaneous T-cell
                     lymphoma-associated antigen se33-1"
                     /calculated_mol_wt=220495
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Site            47
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Site            49
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Site            54
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Region          465..638
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Region          472..571
                     /region_name="Involved in localization to nuclear
                     speckles. /evidence=ECO:0000250|UniProtKB:Q61464"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Region          676..751
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          <749..873
                     /region_name="PRK13808"
                     /note="adenylate kinase; Provisional"
                     /db_xref="CDD:172341"
     Region          835..861
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Region          905..979
                     /region_name="RRM1_2_NP220"
                     /note="RNA recognition motif 1 (RRM1) and 2 (RRM2) found
                     in vertebrate nuclear protein 220 (NP220); cd12716"
                     /db_xref="CDD:410115"
     Region          1009..1082
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          1094..1148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Region          <1293..1907
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          1294..1340
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Region          1354..1532
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Site            1401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Site            1641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61464; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Site            1667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Region          1793..1823
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Region          1867..1916
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     Site            1882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14966.2)"
     Region          1927..1959
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          1946..1978
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14966.2)"
     CDS             1..1978
                     /gene="ZNF638"
                     /gene_synonym="NP220; ZFML; Zfp638"
                     /coded_by="NM_014497.5:297..6233"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1917.1"
                     /db_xref="GeneID:27332"
                     /db_xref="HGNC:HGNC:17894"
                     /db_xref="MIM:614349"
ORIGIN      
        1 msrprfnprg dfplqrprap npsgmrppgp fmrpgsmglp rfypagrarg iphrfaghes
       61 yqnmgpqrmn vqvtqhrtdp rltkekldfh eaqqkkgkph gsrwddephi sasvavkqss
      121 vtqvteqspk vqsrytkesa ssilasfgls nedleelsry pdeqltpenm plilrdirmr
      181 kmgrrlpnlp sqsrnketlg seavssnvid yghaskygyt edplevriyd peiptdeven
      241 efqsqqnisa svpnpnvicn smfpvedvfr qmdfpgessn nrsffsvesg tkmsglhisg
      301 gqsvlepiks vnqsinqtvs qtmsqslipp smnqqpfsse lissvsqqer iphepvinss
      361 nvhvgsrgsk knyqsqadip irspfgivka swlpkfshad aqkmkrlptp smmndyyaas
      421 prifphlcsl cnvecshlkd wiqhqntsth iescrqlrqq ypdwnpeilp srrnegnrke
      481 netprrrshs psprrsrrss sshrfrrsrs pmhymyrprs rsprichrfi sryrsrsrsr
      541 spyrirnpfr gspkcfrsvs permsrrsvr ssdrkkaled vvqrsghgte fnkqkhleaa
      601 dkghspaqkp ktssgtkpsv kptsatksds nlgghsirck sknleddtls eckqvsdkav
      661 slqrklrkeq slhygsvlli telpedgcte edvrklfqpf gkvndvlivp yrkeayleme
      721 fkeaitaimk yiettpltik gksvkicvpg kkkaqnkevk kktleskkvs astlkrdada
      781 skaveivtst saaktgqaka svakvnkstg ksassvksvv tvavkgnkas iktaksggkk
      841 sleakktgnv knkdsnkpvt ipenseikts ievkatenca keaisdaale ateneplnke
      901 teemcvmlvs nlpnkgysve evydlakpfg glkdililss hkkayieinr kaaesmvkfy
      961 tcfpvlmdgn qlsismapen mnikdeeaif itlvkendpe anidtiydrf vhldnlpedg
     1021 lqcvlcvglq fgkvdhhvfi snrnkailql dspesaqsmy sflkqnpqni gdhmltcsls
     1081 pkidlpevqi ehdpelekes pglknspide sevqtatdsp svkpneleee stpsiqtetl
     1141 vqqeepceee aekatcdsdf avetleletq geevkeeipl vasasvsieq ftenaeecal
     1201 nqqmfnsdle kkgaeiinpk tallpsdsvf aeernlkgil eespseaedf isgitqtmve
     1261 avaeveknet vseilpstci vtlvpgiptg dektvdkkni sekkgnmdek eekefntket
     1321 rmdlqigtek aeknegrmda ekvekmaamk ekpaentlfk aypnkgvgqa nkpdetskts
     1381 ilavsdvsss kpsikavivs spkakatvsk tenqksfpks vprdqinaek klsakefgll
     1441 kptsarsgla essskfkptq ssltrggsgr isalqgklsk ldyrditkqs qetearpsim
     1501 krddsnnktl aeqntknpks ttgrsskske eplfpfnlde fvtvdeviee vnpsqakqnp
     1561 lkgkrketlk nvpfselnlk kkkgktstpr gvegelsfvt ldeigeeeda aahlaqalvt
     1621 vdevideeel nmeemvknsn slftldelid qddcishsep kdvtvlsvae eqdllkqerl
     1681 vtvdeigeve elplnesadi tfatlntkgn egdtvrdsig fissqvpedp stlvtvdeiq
     1741 ddssdlhlvt ldevteeded sladfnnlke elnfvtvdev geeedgdndl kvelaqsknd
     1801 hptdkkgnrk kravdtkktk leslsqvgpv nenvmeedlk tmierhltak tptkrvrigk
     1861 tlpsekavvt epakgeeafq msevdeesgl kdseperkrk ktedsssgks vasdvpeeld
     1921 flvpkagffc picslfysge kamtnhckst rhkqntekfm akqrkekeqn eaeerssr
//
LOCUS       NP_078861                198 aa            linear   PRI 27-APR-2025
DEFINITION  armadillo repeat-containing protein 7 isoform 1 [Homo sapiens].
ACCESSION   NP_078861
VERSION     NP_078861.1
DBSOURCE    REFSEQ: accession NM_024585.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK300997.1, BC011728.1 and AC022211.5.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.965129.1, BC011728.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000245543.6/ ENSP00000245543.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..198
                     /product="armadillo repeat-containing protein 7 isoform 1"
                     /note="armadillo repeat-containing protein 7"
                     /calculated_mol_wt=21793
     Region          50..86
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          57..99
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6L4.1)"
     Region          87..126
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          91..122
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          100..140
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6L4.1)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H6L4.1)"
     CDS             1..198
                     /gene="ARMC7"
                     /coded_by="NM_024585.4:321..917"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11714.1"
                     /db_xref="GeneID:79637"
                     /db_xref="HGNC:HGNC:26168"
ORIGIN      
        1 maqkpkvdph vgrlgylqal vtefqetqsq dakeqvlanl anfaydpsny eylrqlqvld
       61 lfldslseen etlvefaigg lcnlcpdran kehilhaggv pliinclssp neetvlsait
      121 tlmhlsppgr sflpeltatp vvqcmlrfsl sasarlrnla qifledfcsp rqvaearsrq
      181 ahsalgiplp rsvaprqr
//
LOCUS       NP_001156863             611 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger and SCAN domain-containing protein 12 [Homo sapiens].
ACCESSION   NP_001156863
VERSION     NP_001156863.1
DBSOURCE    REFSEQ: accession NM_001163391.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Wen,X., Jin,H.Y., Li,M., Kim,Y., Cho,N.Y., Kwak,Y., Bae,J.M.,
            Lee,H.S. and Kang,G.H.
  TITLE     Methylation statuses of NCOR2, PARK2, and ZSCAN12 signify densities
            of tumor-infiltrating lymphocytes in gastric carcinoma
  JOURNAL   Sci Rep 12 (1), 862 (2022)
   PUBMED   35039565
  REMARK    GeneRIF: Methylation statuses of NCOR2, PARK2, and ZSCAN12 signify
            densities of tumor-infiltrating lymphocytes in gastric carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Lee,P.L., Gelbart,T., West,C., Adams,M., Blackstone,R. and
            Beutler,E.
  TITLE     Three genes encoding zinc finger proteins on human chromosome
            6p21.3: members of a new subclass of the Kruppel gene family
            containing the conserved SCAN box domain
  JOURNAL   Genomics 43 (2), 191-201 (1997)
   PUBMED   9244436
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z98745.1.
            
            Transcript Variant: This variant (1), as well as variant 10,
            encodes the functional protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.168581.1,
                                           SRR7346977.3043798.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267776 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000684592.1/ ENSP00000507347.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..611
                     /product="zinc finger and SCAN domain-containing protein
                     12"
                     /note="zinc finger protein 305; zinc finger protein 96"
                     /calculated_mol_wt=70829
     Region          42..152
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          154..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43309.2)"
     Region          198..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43309.2)"
     Region          248..268
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          276..296
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          276..296
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Site            order(281,283,285,287..288,291..292,295,309,311,315..316,
                     319..320,323,337,339,341,343..344,347..348,351)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          299..579
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          304..324
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          332..352
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          360..380
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          388..408
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          416..436
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          444..463
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          471..491
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          499..519
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(504,506,508,510..511,514..515,518,532,534,538..539,
                     542..543,546,560,562,564,566..567,570..571,574)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          527..547
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          555..575
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          581..603
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          583..603
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..611
                     /gene="ZSCAN12"
                     /gene_synonym="dJ29K1.2; ZFP96; ZNF29K1; ZNF305; ZNF96"
                     /coded_by="NM_001163391.2:160..1995"
                     /db_xref="CCDS:CCDS93876.1"
                     /db_xref="GeneID:9753"
                     /db_xref="HGNC:HGNC:13172"
                     /db_xref="MIM:603978"
ORIGIN      
        1 mastwaiqah mdqdeplevk ieeekyttrq dwdlrknnth srevfrqyfr qfcyqetsgp
       61 realsrlrel chqwlrpeth tkeqilellv leqfltilpe elqawvqeqh pesgeevvtv
      121 ledlerelde pgeqvsvhtg eqemflqetv rlrkegepsm slqsmkaqpk yespelesqq
      181 eqvldvetgn eygnlkqevs eemephgkts skfendmsks arcgetrepe eiteepsacs
      241 redkqptcde ngvsltensd htehqricpg eesygcddcg kafsqhshli ehqrihtgdr
      301 pykceecgka frgrtvlirh kiihtgekpy kcnecgkafg rwsalnqhqr lhtgekhyhc
      361 ndcgkafsqk aglfhhikih trdkpyqctq cnksfsrrsi ltqhqgvhtg akpyecnecg
      421 kafvynsslv shqeihhkek cyqckecgks fsqsgliqhq rihtgekpyk cdvcekafiq
      481 rtsltehqri htgerpykcd kcgkaftqrs vltehqriht gerpykcdec gnafrgitsl
      541 iqhqrihtge kpyqcdecgk afrqrsdlsk hqrihnrrgt yvckecgksf rqnsaltqhq
      601 tihkgeksvs v
//
LOCUS       NP_598003                376 aa            linear   PRI 27-APR-2025
DEFINITION  zinc transporter 7 [Homo sapiens].
ACCESSION   NP_598003
VERSION     NP_598003.2
DBSOURCE    REFSEQ: accession NM_133496.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Yu,W., Gui,S., Xie,J., Peng,L., Xiao,J., Luo,H., Tao,Z. and
            Cheng,Z.
  TITLE     Investigation of cuproptosis regulator-mediated modification
            patterns and SLC30A7 function in GBM
  JOURNAL   Aging (Albany NY) 16 (4), 3554-3582 (2024)
   PUBMED   38393693
  REMARK    GeneRIF: Investigation of cuproptosis regulator-mediated
            modification patterns and SLC30A7 function in GBM.
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Huang,L., Yang,Z., Kirschke,C.P., Prouteau,C., Copin,M.C.,
            Bonneau,D., Pellier,I., Coutant,R., Miot,C. and Ziegler,A.
  TITLE     Identification of novel compound heterozygous variants in the
            SLC30A7 (ZNT7) gene in two French brothers with stunted growth,
            testicular hypoplasia and bone marrow failure
  JOURNAL   Hum Mol Genet 32 (12), 2016-2031 (2023)
   PUBMED   36821639
  REMARK    GeneRIF: Identification of novel compound heterozygous variants in
            the SLC30A7 (ZNT7) gene in two French brothers with stunted growth,
            testicular hypoplasia and bone marrow failure.
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Penon-Portmann,M., Eldomery,M.K., Potocki,L., Marafi,D.,
            Posey,J.E., Coban-Akdemir,Z., Harel,T., Grochowski,C.M., Loucks,H.,
            Devine,W.P., Van Ziffle,J., Doherty,D., Lupski,J.R. and Shieh,J.T.
  TITLE     De novo heterozygous variants in SLC30A7 are a candidate cause for
            Joubert syndrome
  JOURNAL   Am J Med Genet A 188 (8), 2360-2366 (2022)
   PUBMED   35751429
  REMARK    GeneRIF: De novo heterozygous variants in SLC30A7 are a candidate
            cause for Joubert syndrome.
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Li,W., Yang,S., Chen,G. and He,S.
  TITLE     MiR-200c-3p regulates pyroptosis by targeting SLC30A7 in diabetic
            retinopathy
  JOURNAL   Hum Exp Toxicol 41, 9603271221099589 (2022)
   PUBMED   35607288
  REMARK    GeneRIF: MiR-200c-3p regulates pyroptosis by targeting SLC30A7 in
            diabetic retinopathy.
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Wei,T., Ji,X., Gao,Y., Zhu,X. and Xiao,G.
  TITLE     ZnT7 RNAi favors RafGOFscrib-/--induced tumor growth and invasion
            in Drosophila through JNK signaling pathway
  JOURNAL   Oncogene 40 (12), 2217-2229 (2021)
   PUBMED   33649534
  REMARK    GeneRIF: ZnT7 RNAi favors Raf(GOF)scrib(-/-)-induced tumor growth
            and invasion in Drosophila through JNK signaling pathway.
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Matsuura,W., Kohda,A.,
            Okumura,K., Nagao,M., Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Zinc transporters, ZnT5 and ZnT7, are required for the activation
            of alkaline phosphatases, zinc-requiring enzymes that are
            glycosylphosphatidylinositol-anchored to the cytoplasmic membrane
  JOURNAL   J Biol Chem 280 (1), 637-643 (2005)
   PUBMED   15525635
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Devergnas,S., Chimienti,F., Naud,N., Pennequin,A., Coquerel,Y.,
            Chantegrel,J., Favier,A. and Seve,M.
  TITLE     Differential regulation of zinc efflux transporters ZnT-1, ZnT-5
            and ZnT-7 gene expression by zinc levels: a real-time RT-PCR study
  JOURNAL   Biochem Pharmacol 68 (4), 699-709 (2004)
   PUBMED   15276077
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Seve,M., Chimienti,F., Devergnas,S. and Favier,A.
  TITLE     In silico identification and expression of SLC30 family genes: an
            expressed sequence tag data mining strategy for the
            characterization of zinc transporters' tissue expression
  JOURNAL   BMC Genomics 5 (1), 32 (2004)
   PUBMED   15154973
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Kirschke,C.P. and Huang,L.
  TITLE     ZnT7, a novel mammalian zinc transporter, accumulates zinc in the
            Golgi apparatus
  JOURNAL   J Biol Chem 278 (6), 4096-4102 (2003)
   PUBMED   12446736
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA997188.1, BC064692.1, AL732465.6 and BX648884.1.
            
            On Dec 20, 2003 this sequence version replaced NP_598003.1.
            
            Summary: Zinc functions as a cofactor for numerous enzymes, nuclear
            factors, and hormones and as an intra- and intercellular signal
            ion. Members of the zinc transporter (ZNT)/SLC30 subfamily of the
            cation diffusion facilitator family, such as SLC30A7, permit
            cellular efflux of zinc (Seve et al., 2004 [PubMed
            15154973]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) is the longer transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.17968.1, BC064692.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357650.9/ ENSP00000350278.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.2"
     Protein         1..376
                     /product="zinc transporter 7"
                     /note="zinc transporter like 2; zinc transporter ZnT-7;
                     znt-like transporter 2; solute carrier family 30 (zinc
                     transporter), member 7"
                     /calculated_mol_wt=41495
     Region          31..354
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Region          161..218
                     /region_name="His-rich loop"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Region          <182..219
                     /region_name="ureE"
                     /note="urease accessory protein UreE; Provisional;
                     PRK13263"
                     /db_xref="CDD:237323"
     Region          194..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            237..257
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            263..283
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     CDS             1..376
                     /gene="SLC30A7"
                     /gene_synonym="ZHS; ZnT-7; ZNT7; ZnTL2"
                     /coded_by="NM_133496.5:174..1304"
                     /db_xref="CCDS:CCDS776.1"
                     /db_xref="GeneID:148867"
                     /db_xref="HGNC:HGNC:19306"
                     /db_xref="MIM:611149"
ORIGIN      
        1 mlplsikdde ykppkfnlfg kisgwfrsil sdktsrnlff flclnlsfaf vellygiwsn
       61 clglisdsfh mffdstaila glaasviskw rdndafsygy vraevlagfv nglfliftaf
      121 fifsegvera lappdvhher lllvsilgfv vnligifvfk hgghghshgs ghghshslfn
      181 galdqahghv dhchshevkh gaahshdhah ghghfhshdg pslkettgps rqilqgvflh
      241 iladtlgsig viasaimmqn fglmiadpic siliailivv svipllresv gilmqrtppl
      301 lenslpqcyq rvqqlqgvys lqeqhfwtlc sdvyvgtlkl ivapdadarw ilsqthnift
      361 qagvrqlyvq idfaam
//
LOCUS       NP_115982                163 aa            linear   PRI 27-APR-2025
DEFINITION  adenosine 5'-monophosphoramidase HINT2 precursor [Homo sapiens].
ACCESSION   NP_115982
VERSION     NP_115982.1
DBSOURCE    REFSEQ: accession NM_032593.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Yao,J., Miao,Y., Zhu,L., Wan,M., Lu,Y. and Tang,W.
  TITLE     Histidine triad nucleotide-binding protein 2: From basic science to
            clinical implications
  JOURNAL   Biochem Pharmacol 212, 115527 (2023)
   PUBMED   37004779
  REMARK    GeneRIF: Histidine triad nucleotide-binding protein 2: From basic
            science to clinical implications.
            Review article
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Dolot,R., Krakowiak,A., Kaczmarek,R., Wlodarczyk,A., Pichlak,M. and
            Nawrot,B.
  TITLE     Biochemical, crystallographic and biophysical characterization of
            histidine triad nucleotide-binding protein 2 with different ligands
            including a non-hydrolyzable analog of Ap4A
  JOURNAL   Biochim Biophys Acta Gen Subj 1865 (11), 129968 (2021)
   PUBMED   34329705
  REMARK    GeneRIF: Biochemical, crystallographic and biophysical
            characterization of histidine triad nucleotide-binding protein 2
            with different ligands including a non-hydrolyzable analog of Ap4A.
            Erratum:[Biochim Biophys Acta Gen Subj. 2022 Feb;1866(2):130035.
            doi: 10.1016/j.bbagen.2021.130035. PMID: 34687819]
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Strom,A., Tong,C.L. and Wagner,C.R.
  TITLE     Histidine triad nucleotide-binding proteins HINT1 and HINT2 share
            similar substrate specificities and little affinity for the
            signaling dinucleotide Ap4A
  JOURNAL   FEBS Lett 594 (10), 1497-1505 (2020)
   PUBMED   31990367
  REMARK    GeneRIF: Histidine triad nucleotide-binding proteins HINT1 and
            HINT2 share similar substrate specificities and little affinity for
            the signaling dinucleotide Ap4A.
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Lenglet,S., Antigny,F., Vetterli,L., Dufour,J.F. and Rossier,M.F.
  TITLE     Hint2 is expressed in the mitochondria of H295R cells and is
            involved in steroidogenesis
  JOURNAL   Endocrinology 149 (11), 5461-5469 (2008)
   PUBMED   18653718
  REMARK    GeneRIF: Hint2 is required for an optimal steroidogenic response,
            possibly because of a particular signalling function exerted within
            the mitochondria.
REFERENCE   8  (residues 1 to 163)
  AUTHORS   Martin,J., Magnino,F., Schmidt,K., Piguet,A.C., Lee,J.S.,
            Semela,D., St-Pierre,M.V., Ziemiecki,A., Cassio,D., Brenner,C.,
            Thorgeirsson,S.S. and Dufour,J.F.
  TITLE     Hint2, a mitochondrial apoptotic sensitizer down-regulated in
            hepatocellular carcinoma
  JOURNAL   Gastroenterology 130 (7), 2179-2188 (2006)
   PUBMED   16762638
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 163)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI759951.1, BM764627.1 and BC047737.2.
            
            Summary: Histidine triad proteins, such as HINT2, are nucleotide
            hydrolases and transferases that act on the alpha-phosphate of
            ribonucleotides (Brenner, 2002 [PubMed 12119013]).[supplied by
            OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.327484.1, DN994618.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000259667.6/
                                                  ENSP00000259667.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..163
                     /product="adenosine 5'-monophosphoramidase HINT2
                     precursor"
                     /note="PKCI-1-related HIT protein; histidine triad
                     nucleotide-binding protein 2, mitochondrial; protein
                     kinase C inhibitor-2; HINT-2; HINT-3; HIT-17kDa; adenosine
                     5'-monophosphoramidase HINT2"
                     /calculated_mol_wt=15512
     transit_peptide 1..17
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9BX68.1)"
                     /calculated_mol_wt=1668
     mat_peptide     18..163
                     /product="Adenosine 5'-monophosphoramidase HINT2.
                     /id=PRO_0000109786"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX68.1)"
                     /calculated_mol_wt=15512
     Region          53..155
                     /region_name="PKCI_related"
                     /note="Protein Kinase C Interacting protein related
                     (PKCI): PKCI and related proteins belong to the ubiquitous
                     HIT family of hydrolases that act on alpha-phosphates of
                     ribonucleotides. The members of this subgroup have a
                     conserved HxHxHxx motif (x is a...; cd01276"
                     /db_xref="CDD:238607"
     Site            order(78,80..81,88,90,136,143,145,149,151)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238607"
     Site            119
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0S9; propagated from
                     UniProtKB/Swiss-Prot (Q9BX68.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0S9; propagated from
                     UniProtKB/Swiss-Prot (Q9BX68.1)"
     Site            order(147,149,151..153)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238607"
     Region          147..151
                     /region_name="Histidine triad motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX68.1)"
     Site            149
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238607"
     CDS             1..163
                     /gene="HINT2"
                     /gene_synonym="HIT-17"
                     /coded_by="NM_032593.3:64..555"
                     /db_xref="CCDS:CCDS6594.1"
                     /db_xref="GeneID:84681"
                     /db_xref="HGNC:HGNC:18344"
                     /db_xref="MIM:609997"
ORIGIN      
        1 maaavvlaag lraarravaa tgvrggqvrg aagvtdgnev akaqqatpgg aaptifsril
       61 dkslpadily edqqclvfrd vapqapvhfl vipkkpipri sqaeeedqql lghlllvakq
      121 takaeglgdg yrlvindgkl gaqsvyhlhi hvlggrqlqw ppg
//
LOCUS       NP_001357084             177 aa            linear   PRI 27-APR-2025
DEFINITION  DPY30 domain-containing protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001357084 XP_024303595
VERSION     NP_001357084.1
DBSOURCE    REFSEQ: accession NM_001370155.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Li,S., Qiao,Y., Di,Q., Le,X., Zhang,L., Zhang,X., Zhang,C.,
            Cheng,J., Zong,S., Koide,S.S., Miao,S. and Wang,L.
  TITLE     Interaction of SH3P13 and DYDC1 protein: a germ cell component that
            regulates acrosome biogenesis during spermiogenesis
  JOURNAL   Eur J Cell Biol 88 (9), 509-520 (2009)
   PUBMED   19545932
  REMARK    Erratum:[Eur J Cell Biol. 2019 Jan;98(1):51-52. doi:
            10.1016/j.ejcb.2018.11.002. PMID: 30497823]
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Kuhl,A., Melberg,A., Meinl,E., Nurnberg,G., Nurnberg,P.,
            Kehrer-Sawatzki,H. and Jenne,D.E.
  TITLE     Myofibrillar myopathy with arrhythmogenic right ventricular
            cardiomyopathy 7: corroboration and narrowing of the critical
            region on 10q22.3
  JOURNAL   Eur J Hum Genet 16 (3), 367-373 (2008)
   PUBMED   18197198
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359195.24.
            
            On May 2, 2019 this sequence version replaced XP_024303595.1.
            
            Summary: This gene encodes a member of a family of proteins that
            contains a DPY30 domain. The encoded protein is involved in
            acrosome formation during spermatid development. This gene locus
            overlaps with a closely related gene on the opposite strand.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longer isoform (a). Variants 1-4 all
            encode the longer isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.163222.1,
                                           SRR5189667.317847.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..177
                     /product="DPY30 domain-containing protein 1 isoform a"
                     /note="DPY30 domain-containing protein 1"
                     /calculated_mol_wt=20762
     Region          2..43
                     /region_name="DD_DYDC-like"
                     /note="dimerization/docking (D/D) domain found in the
                     DPY30 domain-containing protein (DYDC)-like family;
                     cd22966"
                     /db_xref="CDD:438535"
     CDS             1..177
                     /gene="DYDC1"
                     /gene_synonym="DPY30D1"
                     /coded_by="NM_001370155.1:413..946"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS7366.1"
                     /db_xref="GeneID:143241"
                     /db_xref="HGNC:HGNC:23460"
                     /db_xref="MIM:615154"
ORIGIN      
        1 mesiylqkhl gacltqglae varvrpvdpi eylalwiyky kenvtmeqlr qkemaklere
       61 relalmeqem merlkaeell lqqqqlalql elemqekerq riqelqraqe qlgkemrmnm
      121 enlvrnedil hseeatldsg ktlaeisdry gapnlsrvee ldepmfsdia lnidqdl
//
LOCUS       NP_006707                674 aa            linear   PRI 27-APR-2025
DEFINITION  protein DBF4 homolog A isoform 1 [Homo sapiens].
ACCESSION   NP_006707
VERSION     NP_006707.1
DBSOURCE    REFSEQ: accession NM_006716.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Goder,A., Maric,C.A., Rainey,M.D., O'Connor,A., Cazzaniga,C.,
            Shamavu,D., Cadoret,J.C. and Santocanale,C.
  TITLE     DBF4, not DRF1, is the crucial regulator of CDC7 kinase at
            replication forks
  JOURNAL   J Cell Biol 223 (8) (2024)
   PUBMED   38865090
  REMARK    GeneRIF: DBF4, not DRF1, is the crucial regulator of CDC7 kinase at
            replication forks.
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Wu,Z., Zhang,L., Li,X., Liu,L., Kuang,T., Qiu,Z., Deng,W. and
            Wang,W.
  TITLE     The prognostic significance and potential mechanism of DBF4 zinc
            finger in hepatocellular carcinoma
  JOURNAL   Sci Rep 14 (1), 10662 (2024)
   PUBMED   38724606
  REMARK    GeneRIF: The prognostic significance and potential mechanism of
            DBF4 zinc finger in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 674)
  AUTHORS   Zhang,L., Hong,J., Chen,W., Zhang,W., Liu,X., Lu,J., Tang,H.,
            Yang,Z., Zhou,K., Xie,H., Jia,C., Jiang,D. and Zheng,S.
  TITLE     DBF4 Dependent Kinase Inhibition Suppresses Hepatocellular
            Carcinoma Progression and Potentiates Anti-Programmed Cell Death-1
            Therapy
  JOURNAL   Int J Biol Sci 19 (11), 3412-3427 (2023)
   PUBMED   37497004
  REMARK    GeneRIF: DBF4 Dependent Kinase Inhibition Suppresses Hepatocellular
            Carcinoma Progression and Potentiates Anti-Programmed Cell Death-1
            Therapy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 674)
  AUTHORS   Tang,Y., Xu,L., Ren,Y., Li,Y., Yuan,F., Cao,M., Zhang,Y., Deng,M.
            and Yao,Z.
  TITLE     Identification and Validation of a Prognostic Model Based on Three
            MVI-Related Genes in Hepatocellular Carcinoma
  JOURNAL   Int J Biol Sci 18 (1), 261-275 (2022)
   PUBMED   34975331
  REMARK    GeneRIF: Identification and Validation of a Prognostic Model Based
            on Three MVI-Related Genes in Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 674)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 674)
  AUTHORS   Yamada,M., Sato,N., Taniyama,C., Ohtani,K., Arai,K. and Masai,H.
  TITLE     A 63-base pair DNA segment containing an Sp1 site but not a
            canonical E2F site can confer growth-dependent and E2F-mediated
            transcriptional stimulation of the human ASK gene encoding the
            regulatory subunit for human Cdc7-related kinase
  JOURNAL   J Biol Chem 277 (31), 27668-27681 (2002)
   PUBMED   12015319
  REMARK    GeneRIF: results suggest that E2F regulates the ASK promoter
            through an atypical mode of recognition of the target site
REFERENCE   7  (residues 1 to 674)
  AUTHORS   Masai,H., Matsui,E., You,Z., Ishimi,Y., Tamai,K. and Arai,K.
  TITLE     Human Cdc7-related kinase complex. In vitro phosphorylation of MCM
            by concerted actions of Cdks and Cdc7 and that of a criticial
            threonine residue of Cdc7 bY Cdks
  JOURNAL   J Biol Chem 275 (37), 29042-29052 (2000)
   PUBMED   10846177
REFERENCE   8  (residues 1 to 674)
  AUTHORS   Jiang,W., McDonald,D., Hope,T.J. and Hunter,T.
  TITLE     Mammalian Cdc7-Dbf4 protein kinase complex is essential for
            initiation of DNA replication
  JOURNAL   EMBO J 18 (20), 5703-5713 (1999)
   PUBMED   10523313
REFERENCE   9  (residues 1 to 674)
  AUTHORS   Lepke,M., Putter,V., Staib,C., Kneissl,M., Berger,C., Hoehn,K.,
            Nanda,I., Schmid,M. and Grummt,F.
  TITLE     Identification, characterization and chromosomal localization of
            the cognate human and murine DBF4 genes
  JOURNAL   Mol Gen Genet 262 (2), 220-229 (1999)
   PUBMED   10517317
REFERENCE   10 (residues 1 to 674)
  AUTHORS   Kumagai,H., Sato,N., Yamada,M., Mahony,D., Seghezzi,W., Lees,E.,
            Arai,K. and Masai,H.
  TITLE     A novel growth- and cell cycle-regulated protein, ASK, activates
            human Cdc7-related kinase and is essential for G1/S transition in
            mammalian cells
  JOURNAL   Mol Cell Biol 19 (7), 5083-5095 (1999)
   PUBMED   10373557
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB028069.1, BC036045.1 and AC005164.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036045.1, SRR1803614.91073.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265728.6/ ENSP00000265728.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.12"
     Protein         1..674
                     /product="protein DBF4 homolog A isoform 1"
                     /note="activator of S phase kinase; zinc finger, DBF-type
                     containing 1; DBF4 homolog; DBF4 zinc finger A; protein
                     DBF4 homolog A; chiffon homolog A; DBF4-type zinc
                     finger-containing protein 1; regulatory subunit of DDK"
                     /calculated_mol_wt=76727
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Region          100..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Region          294..336
                     /region_name="ZnF_DBF"
                     /note="Zinc finger in DBF-like proteins; smart00586"
                     /db_xref="CDD:128854"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Region          614..638
                     /region_name="Integrase domain-binding motif 1 (IBM1).
                     /evidence=ECO:0000269|PubMed:29997176"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            625
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29997176; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Region          655..674
                     /region_name="Integrase domain-binding motif 2 (IBM2).
                     /evidence=ECO:0000269|PubMed:29997176"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29997176; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29997176; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU7.1)"
     CDS             1..674
                     /gene="DBF4"
                     /gene_synonym="ASK; CHIF; DBF4A; ZDBF1"
                     /coded_by="NM_006716.4:241..2265"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5611.1"
                     /db_xref="GeneID:10926"
                     /db_xref="HGNC:HGNC:17364"
                     /db_xref="MIM:604281"
ORIGIN      
        1 mnsgamrihs kghfqggiqv kneknrpslk slktdnrpek skckplwgkv fyldlpsvti
       61 seklqkdikd lggrveefls kdisylisnk keakfaqtlg rispvpspes aytaettsph
      121 pshdgssfks pdtvclsrgk llvekaikdh dfipsnsils nalswgvkil hiddiryyie
      181 qkkkelyllk ksstsvrdgg krvgsgaqkt rtgrlkkpfv kvedmsqlyr pfylqltnmp
      241 finysiqkpc spfdvdkpss mqkqtqvklr iqtdgdkygg tsiqlqlkek kkkgyceccl
      301 qkyedlethl lseqhrnfaq snqyqvvddi vsklvfdfve yekdtpkkkr ikysvgslsp
      361 vsasvlkkte qkekvelqhi sqkdcqeddt tvkeqnflyk etqetekkll fisepiphps
      421 nelrglnekm snkcsmlsta eddirqnftq lplhknkqec ildisehtls endleelrvd
      481 hykcniqasv hvsdfstdns gsqpkqksdt vlfpakdlke kdlhsifthd sglitinssq
      541 ehltvqakap fhtppeepne cdfknmdslp sgkihrkvki ilgrnrkenl epnaefdkrt
      601 efitqeenri csspvqslld lfqtseekse flgftsytek sgicnvldiw eeensdnllt
      661 affsspstst ftgf
//
LOCUS       NP_057512                366 aa            linear   PRI 27-APR-2025
DEFINITION  ABI gene family member 3 isoform 1 [Homo sapiens].
ACCESSION   NP_057512
VERSION     NP_057512.2
DBSOURCE    REFSEQ: accession NM_016428.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Turner,A.K., Shaw,B.C., Simpson,J.F. and Estus,S.
  TITLE     Identification and Quantitation of Novel ABI3 Isoforms Relative to
            Alzheimer's Disease Genetics and Neuropathology
  JOURNAL   Genes (Basel) 13 (9), 1607 (2022)
   PUBMED   36140776
  REMARK    GeneRIF: Identification and Quantitation of Novel ABI3 Isoforms
            Relative to Alzheimer's Disease Genetics and Neuropathology.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Cao,M., Liu,J., Zhang,X., Yang,T., Wang,Y., Hou,Y., Song,Q.,
            Cui,Y., Wang,Y. and Wang,P.
  TITLE     ABI3 Is a Novel Early Biomarker of Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 87 (1), 335-344 (2022)
   PUBMED   35275543
  REMARK    GeneRIF: ABI3 Is a Novel Early Biomarker of Alzheimer's Disease.
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Strickland,S.L., Morel,H., Prusinski,C., Allen,M., Patel,T.A.,
            Carrasquillo,M.M., Conway,O.J., Lincoln,S.J., Reddy,J.S.,
            Nguyen,T., Malphrus,K.G., Soto,A.I., Walton,R.L., Crook,J.E.,
            Murray,M.E., Boeve,B.F., Petersen,R.C., Lucas,J.A., Ferman,T.J.,
            Uitti,R.J., Wszolek,Z.K., Ross,O.A., Graff-Radford,N.R.,
            Dickson,D.W. and Ertekin-Taner,N.
  TITLE     Association of ABI3 and PLCG2 missense variants with disease risk
            and neuropathology in Lewy body disease and progressive
            supranuclear palsy
  JOURNAL   Acta Neuropathol Commun 8 (1), 172 (2020)
   PUBMED   33092647
  REMARK    GeneRIF: Association of ABI3 and PLCG2 missense variants with
            disease risk and neuropathology in Lewy body disease and
            progressive supranuclear palsy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Olive,C., Ibanez,L., Farias,F.H.G., Wang,F., Budde,J.P.,
            Norton,J.B., Gentsch,J., Morris,J.C., Li,Z., Dube,U.,
            Del-Aguila,J., Bergmann,K., Bradley,J., Benitez,B.A., Harari,O.,
            Fagan,A., Ances,B., Cruchaga,C. and Fernandez,M.V.
  TITLE     Examination of the Effect of Rare Variants in TREM2, ABI3, and
            PLCG2 in LOAD Through Multiple Phenotypes
  JOURNAL   J Alzheimers Dis 77 (4), 1469-1482 (2020)
   PUBMED   32894242
  REMARK    GeneRIF: Examination of the Effect of Rare Variants in TREM2, ABI3,
            and PLCG2 in LOAD Through Multiple Phenotypes.
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Hirao,N., Sato,S., Gotoh,T., Maruoka,M., Suzuki,J., Matsuda,S.,
            Shishido,T. and Tani,K.
  TITLE     NESH (Abi-3) is present in the Abi/WAVE complex but does not
            promote c-Abl-mediated phosphorylation
  JOURNAL   FEBS Lett 580 (27), 6464-6470 (2006)
   PUBMED   17101133
  REMARK    GeneRIF: NESH (Abi-3), like Abi-1 and Abi-2, is a component of the
            Abi/WAVE complex, but likely plays a different role in the
            regulation of c-Abl.
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Ichigotani,Y., Fujii,K., Hamaguchi,M. and Matsuda,S.
  TITLE     In search of a function for the E3B1/Abi2/Argbp1/NESH family
            (Review)
  JOURNAL   Int J Mol Med 9 (6), 591-595 (2002)
   PUBMED   12011975
  REMARK    Review article
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Ichigotani,Y., Yokozaki,S., Fukuda,Y., Hamaguchi,M. and Matsuda,S.
  TITLE     Forced expression of NESH suppresses motility and metastatic
            dissemination of malignant cells
  JOURNAL   Cancer Res 62 (8), 2215-2219 (2002)
   PUBMED   11956071
  REMARK    GeneRIF: Forced expression of NESH suppresses motility and
            metastatic dissemination of malignant cells.
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Matsuda,S., Iriyama,C., Yokozaki,S., Ichigotani,Y., Shirafuji,N.,
            Yamaki,K., Hayakawa,T. and Hamaguchi,M.
  TITLE     Cloning and sequencing of a novel human gene that encodes a
            putative target protein of Nesh-SH3
  JOURNAL   J Hum Genet 46 (8), 483-486 (2001)
   PUBMED   11501947
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Miyazaki,K., Matsuda,S., Ichigotani,Y., Takenouchi,Y., Hayashi,K.,
            Fukuda,Y., Nimura,Y. and Hamaguchi,M.
  TITLE     Isolation and characterization of a novel human gene (NESH) which
            encodes a putative signaling molecule similar to e3B1 protein
  JOURNAL   Biochim Biophys Acta 1493 (1-2), 237-241 (2000)
   PUBMED   10978530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC069454.22 and AC004797.1.
            
            On Nov 23, 2018 this sequence version replaced NP_057512.1.
            
            Summary: This gene encodes a member of an adaptor protein family.
            Members of this family encode proteins containing a homeobox
            homology domain, proline rich region and Src-homology 3 (SH3)
            domain, and are components of the Abi/WAVE complex which regulates
            actin polymerization. The encoded protein inhibits ectopic
            metastasis of tumor cells as well as cell migration. This may be
            accomplished through interaction with p21-activated kinase.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.250957.1, AB037886.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000225941.6/ ENSP00000225941.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..366
                     /product="ABI gene family member 3 isoform 1"
                     /note="new molecule including SH3; ABI gene family member
                     3"
                     /calculated_mol_wt=38904
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          161..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2A4.2)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P2A4.2)"
     Region          215..302
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2A4.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P2A4.2)"
     Region          312..363
                     /region_name="SH3_Abi"
                     /note="Src homology 3 domain of Abl Interactor proteins;
                     cd11826"
                     /db_xref="CDD:212760"
     Site            order(317,319,322,326,344..345,358,360..361)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212760"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P2A4.2)"
     CDS             1..366
                     /gene="ABI3"
                     /gene_synonym="NESH; SSH3BP3"
                     /coded_by="NM_016428.3:19..1119"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11546.1"
                     /db_xref="GeneID:51225"
                     /db_xref="HGNC:HGNC:29859"
                     /db_xref="MIM:606363"
ORIGIN      
        1 maelqqlqef eiptgrealr gnhsallrva dycednyvqa tdkrkaleet mafttqalas
       61 vayqvgnlag htlrmldlqg aalrqvearv stlgqmvnmh mekvarreig tlatvqrlpp
      121 gqkviapenl ppltpycrrp lnfgclddig hgikdlstql srtgtlsrks ikapatpasa
      181 tlgrppripe pvhlpvvpdg rlsaassafs lasagsaegv ggaptpkgqa appapplpss
      241 ldpppppaav evfqrpptle elsppppdee lplpldlppp ppldgdelgl pppppgfgpd
      301 epswvpasyl ekvvtlypyt sqkdnelsfs egtvicvtrr ysdgwcegvs segtgffpgn
      361 yvepsc
//
LOCUS       NP_056222                271 aa            linear   PRI 27-APR-2025
DEFINITION  protein ABHD14A [Homo sapiens].
ACCESSION   NP_056222
VERSION     NP_056222.2
DBSOURCE    REFSEQ: accession NM_015407.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Hoshino,J., Aruga,J., Ishiguro,A. and Mikoshiba,K.
  TITLE     Dorz1, a novel gene expressed in differentiating cerebellar granule
            neurons, is down-regulated in Zic1-deficient mouse
  JOURNAL   Brain Res Mol Brain Res 120 (1), 57-64 (2003)
   PUBMED   14667578
  REMARK    GeneRIF: Identification and characterization of Mouse Dorz1, along
            with sequence comparison to a similar protein in human.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN256406.1, BC002571.2 and AY358201.1.
            
            On Apr 8, 2009 this sequence version replaced NP_056222.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC002571.2, SRR1660803.63732.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000273596.8/ ENSP00000273596.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..271
                     /product="protein ABHD14A"
                     /note="abhydrolase domain-containing protein 14A;
                     alpha/beta hydrolase domain-containing protein 14A"
                     /calculated_mol_wt=29634
     Site            35..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUJ0.2)"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BUJ0.2)"
     Region          97..270
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Site            201
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BUJ0.2)"
     CDS             1..271
                     /gene="ABHD14A"
                     /gene_synonym="DORZ1"
                     /coded_by="NM_015407.5:73..888"
                     /db_xref="CCDS:CCDS2843.1"
                     /db_xref="GeneID:25864"
                     /db_xref="HGNC:HGNC:24538"
                     /db_xref="MIM:618771"
ORIGIN      
        1 mvgalcgcwf rlggarplip lgptvvqtsm srsqvallgl slllmlllyv glpgppeqts
       61 clwgdpnvtv lagltpgnsp ifyrevlpln qahrvevvll hgkafnshtw eqlgtlqlls
      121 qrgyravald lpgfgnsaps keasteagra alleralrdl evqnavlvsp slsghyalpf
      181 lmrghhqlhg fvpiaptstq nytqeqfwav ktptlilyge ldhilaresl rqlrhlpnhs
      241 vvklrnagha cylhkpqdfh lvllafldhl p
//
LOCUS       NP_002061                355 aa            linear   PRI 27-APR-2025
DEFINITION  guanine nucleotide-binding protein G(i) subunit alpha-2 isoform 1
            [Homo sapiens].
ACCESSION   NP_002061
VERSION     NP_002061.1
DBSOURCE    REFSEQ: accession NM_002070.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Deng,X., Zeng,Y. and Ding,D.
  TITLE     MiR-30c-5p-Targeted Regulation of GNAI2 Improves Neural Function
            Injury and Inflammation in Cerebral Ischemia-Reperfusion Injury
  JOURNAL   Appl Biochem Biotechnol 196 (8), 5235-5248 (2024)
   PUBMED   38153649
  REMARK    GeneRIF: MiR-30c-5p-Targeted Regulation of GNAI2 Improves Neural
            Function Injury and Inflammation in Cerebral Ischemia-Reperfusion
            Injury.
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Miete,C., Solis,G.P., Koval,A., Bruckner,M., Katanaev,V.L.,
            Behrens,J. and Bernkopf,D.B.
  TITLE     Galphai2-induced conductin/axin2 condensates inhibit
            Wnt/beta-catenin signaling and suppress cancer growth
  JOURNAL   Nat Commun 13 (1), 674 (2022)
   PUBMED   35115535
  REMARK    GeneRIF: Galphai2-induced conductin/axin2 condensates inhibit
            Wnt/beta-catenin signaling and suppress cancer growth.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Zhang,Z., Ji,Z., He,J., Lu,Y., Tian,W., Zheng,C., Chen,H.,
            Zhang,Q., Yang,F., Zhang,M., Yin,Y., Jiang,R., Chu,W.M., Zhang,W.
            and Sun,B.
  TITLE     Guanine Nucleotide-Binding Protein G(i) Subunit Alpha 2 Exacerbates
            NASH Progression by Regulating Peroxiredoxin 1-Related Inflammation
            and Lipophagy
  JOURNAL   Hepatology 74 (6), 3110-3126 (2021)
   PUBMED   34322898
  REMARK    GeneRIF: Guanine Nucleotide-Binding Protein G(i) Subunit Alpha 2
            Exacerbates NASH Progression by Regulating Peroxiredoxin 1-Related
            Inflammation and Lipophagy.
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Ha,J.H., Jayaraman,M., Yan,M., Dhanasekaran,P., Isidoro,C.,
            Song,Y.S. and Dhanasekaran,D.N.
  TITLE     GNAi2/gip2-Regulated Transcriptome and Its Therapeutic Significance
            in Ovarian Cancer
  JOURNAL   Biomolecules 11 (8), 1211 (2021)
   PUBMED   34439877
  REMARK    GeneRIF: GNAi2/gip2-Regulated Transcriptome and Its Therapeutic
            Significance in Ovarian Cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Magovcevic,I., Ang,S.L., Seidman,J.G., Tolman,C.J., Neer,E.J. and
            Morton,C.C.
  TITLE     Regional localization of the human G protein alpha i2 (GNAI2) gene:
            assignment to 3p21 and a related sequence (GNAI2L) to 12p12-p13
  JOURNAL   Genomics 12 (1), 125-129 (1992)
   PUBMED   1733849
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Cormont,M., Le Marchand-Brustel,Y., Van Obberghen,E., Spiegel,A.M.
            and Sharp,G.W.
  TITLE     Identification of G protein alpha-subunits in RINm5F cells and
            their selective interaction with galanin receptor
  JOURNAL   Diabetes 40 (9), 1170-1176 (1991)
   PUBMED   1718802
REFERENCE   8  (residues 1 to 355)
  AUTHORS   Offermanns,S., Schultz,G. and Rosenthal,W.
  TITLE     Evidence for opioid receptor-mediated activation of the G-proteins,
            Go and Gi2, in membranes of neuroblastoma x glioma (NG108-15)
            hybrid cells
  JOURNAL   J Biol Chem 266 (6), 3365-3368 (1991)
   PUBMED   1671672
REFERENCE   9  (residues 1 to 355)
  AUTHORS   Lyons,J., Landis,C.A., Harsh,G., Vallar,L., Grunewald,K.,
            Feichtinger,H., Duh,Q.Y., Clark,O.H., Kawasaki,E., Bourne,H.R. et
            al.
  TITLE     Two G protein oncogenes in human endocrine tumors
  JOURNAL   Science 249 (4969), 655-659 (1990)
   PUBMED   2116665
REFERENCE   10 (residues 1 to 355)
  AUTHORS   Bushfield,M., Murphy,G.J., Lavan,B.E., Parker,P.J., Hruby,V.J.,
            Milligan,G. and Houslay,M.D.
  TITLE     Hormonal regulation of Gi2 alpha-subunit phosphorylation in intact
            hepatocytes
  JOURNAL   Biochem J 268 (2), 449-457 (1990)
   PUBMED   2114093
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012138.1, AK055574.1 and
            U73166.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is an alpha subunit of
            guanine nucleotide binding proteins (G proteins). The encoded
            protein contains the guanine nucleotide binding site and is
            involved in the hormonal regulation of adenylate cyclase. Several
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.70720.1,
                                           SRR3476690.992179.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313601.11/ ENSP00000312999.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..355
                     /product="guanine nucleotide-binding protein G(i) subunit
                     alpha-2 isoform 1"
                     /note="guanine nucleotide-binding protein G(i) subunit
                     alpha-2; guanine nucleotide-binding protein G(i), alpha-2
                     subunit; adenylate cyclase-inhibiting G alpha protein;
                     GTP-binding regulatory protein Gi alpha-2 chain; guanine
                     nucleotide binding protein (G protein), alpha inhibiting
                     activity polypeptide 2; heterotrimeric guanine
                     nucleotide-binding protein 1C"
                     /calculated_mol_wt=40320
     Region          34..349
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Region          35..48
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P04899.3)"
     Site            order(40,45..47,182,201,204,270..271,273,326..327)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            40..47
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(41..43,71,75,79,82,85..86,104,107,150,179,204,212,
                     216)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Region          174..182
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P04899.3)"
     Site            177..185
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            182
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(183,185,187,198,200,204..206,208,211..212,214..217)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(185,210,213..214,217)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Region          197..206
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P04899.3)"
     Site            201..204
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            202..218
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Region          266..273
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P04899.3)"
     Site            270..273
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(318..329,331..334)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Region          325..330
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P04899.3)"
     Site            326..328
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..355
                     /gene="GNAI2"
                     /gene_synonym="GIP; GNAI2B; HG1C; H_LUCA15.1; H_LUCA16.1"
                     /coded_by="NM_002070.4:133..1200"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2813.1"
                     /db_xref="GeneID:2771"
                     /db_xref="HGNC:HGNC:4385"
                     /db_xref="MIM:139360"
ORIGIN      
        1 mgctvsaedk aaaerskmid knlredgeka arevkllllg agesgkstiv kqmkiihedg
       61 yseeecrqyr avvysntiqs imaivkamgn lqidfadpsr addarqlfal sctaeeqgvl
      121 pddlsgvirr lwadhgvqac fgrsreyqln dsaayylndl eriaqsdyip tqqdvlrtrv
      181 kttgivethf tfkdlhfkmf dvggqrserk kwihcfegvt aiifcvalsa ydlvlaedee
      241 mnrmhesmkl fdsicnnkwf tdtsiilfln kkdlfeekit hsplticfpe ytgankydea
      301 asyiqskfed lnkrkdtkei ythftcatdt knvqfvfdav tdviiknnlk dcglf
//
LOCUS       NP_057267                239 aa            linear   PRI 27-APR-2025
DEFINITION  mRNA turnover protein 4 homolog [Homo sapiens].
ACCESSION   NP_057267
VERSION     NP_057267.2
DBSOURCE    REFSEQ: accession NM_016183.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Zheng,Y., Huang,Y., Li,W. and Cheng,H.
  TITLE     MRTO4 Enhances Glycolysis to Facilitate HCC Progression by
            Inhibiting ALDOB
  JOURNAL   Med Sci Monit 30, e944685 (2024)
   PUBMED   38778508
  REMARK    GeneRIF: MRTO4 Enhances Glycolysis to Facilitate HCC Progression by
            Inhibiting ALDOB.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Cao,X., Khitun,A., Harold,C.M., Bryant,C.J., Zheng,S.J.,
            Baserga,S.J. and Slavoff,S.A.
  TITLE     Nascent alt-protein chemoproteomics reveals a pre-60S assembly
            checkpoint inhibitor
  JOURNAL   Nat Chem Biol 18 (6), 643-651 (2022)
   PUBMED   35393574
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Michalec-Wawiorka,B., Wawiorka,L., Derylo,K., Krokowski,D.,
            Boguszewska,A., Molestak,E., Szajwaj,M. and Tchorzewski,M.
  TITLE     Molecular behavior of human Mrt4 protein, MRTO4, in stress
            conditions is regulated by its C-terminal region
  JOURNAL   Int J Biochem Cell Biol 69, 233-240 (2015)
   PUBMED   26494001
  REMARK    GeneRIF: Human Mrt4 undergoes phosphorylation in vivo and serines
            S229, S233, and S235 are phosphorylated by CK2 kinase in vitro.
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Michalec,B., Krokowski,D., Grela,P., Wawiorka,L., Sawa-Makarska,J.,
            Grankowski,N. and Tchorzewski,M.
  TITLE     Subcellular localization of ribosomal P0-like protein MRT4 is
            determined by its N-terminal domain
  JOURNAL   Int J Biochem Cell Biol 42 (5), 736-748 (2010)
   PUBMED   20083226
  REMARK    GeneRIF: characterization of Mrt4; findings show Mrt4 is a
            trans-acting factor involved in ribosome maturation, with
            nucleus-cytoplasm shuttling capacity
REFERENCE   8  (residues 1 to 239)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 239)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ670859.1, AY303790.1 and
            AL035413.19.
            
            On Feb 4, 2002 this sequence version replaced NP_057267.1.
            
            Summary: This gene encodes a protein sharing a low level of
            sequence similarity with ribosomal protein P0. While the precise
            function of the encoded protein is currently unknown, it appears to
            be involved in mRNA turnover and ribosome assembly. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.735471.1,
                                           SRR1803613.8636.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330263.5/ ENSP00000364320.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..239
                     /product="mRNA turnover protein 4 homolog"
                     /note="60S acidic ribosomal protein PO; MRT4, mRNA
                     turnover 4, homolog; ribosome assembly factor MRTO4; mRNA
                     turnover 4 homolog; MRTO4 ribosome maturation factor"
                     /calculated_mol_wt=27429
     Region          21..183
                     /region_name="Ribosomal_P0_like"
                     /note="Ribosomal protein L10 family, P0-like protein
                     subfamily; composed of uncharacterized eukaryotic proteins
                     with similarity to the 60S ribosomal protein P0, including
                     the Saccharomyces cerevisiae protein called mRNA turnover
                     protein 4 (MRT4). MRT4 may be...; cd05796"
                     /db_xref="CDD:240222"
     Site            order(23..24,27,69..72,75)
                     /site_type="other"
                     /note="23S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:240222"
     Site            order(110,130,134,152,155..156,159..160,162..165,168..170,
                     173..174,176..177,179)
                     /site_type="other"
                     /note="putative Interface with L7/L12 ribosomal proteins
                     [polypeptide binding]"
                     /db_xref="CDD:240222"
     Region          215..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKD2.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0I8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKD2.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0I8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKD2.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0I8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKD2.2)"
     CDS             1..239
                     /gene="MRTO4"
                     /gene_synonym="C1orf33; dJ657E11.4; MRT4"
                     /coded_by="NM_016183.4:32..751"
                     /db_xref="CCDS:CCDS191.1"
                     /db_xref="GeneID:51154"
                     /db_xref="HGNC:HGNC:18477"
                     /db_xref="MIM:620476"
ORIGIN      
        1 mpkskrdkkv sltktakkgl elkqnlieel rkcvdtykyl fifsvanmrn sklkdirnaw
       61 khsrmffgkn kvmmvalgrs psdeykdnlh qvskrlrgev gllftnrtke evnewftkyt
      121 emdyaragnk aaftvsldpg pleqfphsme pqlrqlglpt alkrgvvtll sdyevckegd
      181 vltpeqarvl klfgyemaef kvtikymwds qsgrfqqmgd dlpesasest eesdseddd
//
LOCUS       NP_001357559             433 aa            linear   ROD 27-APR-2025
DEFINITION  ectonucleoside triphosphate diphosphohydrolase 6 isoform 2 [Mus
            musculus].
ACCESSION   NP_001357559
VERSION     NP_001357559.1
DBSOURCE    REFSEQ: accession NM_001370630.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Chadwick,B.P. and Frischauf,A.M.
  TITLE     The CD39-like gene family: identification of three new human
            members (CD39L2, CD39L3, and CD39L4), their murine homologues, and
            a member of the gene family from Drosophila melanogaster
  JOURNAL   Genomics 50 (3), 357-367 (1998)
   PUBMED   9676430
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Chadwick,B.P., Williamson,J., Sheer,D. and Frischauf,A.M.
  TITLE     cDNA cloning and chromosomal mapping of a mouse gene with homology
            to NTPases
  JOURNAL   Mamm Genome 9 (2), 162-164 (1998)
   PUBMED   9457681
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL845174.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.4035803.1,
                                           ERR3363658.402890.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 74.74 cM"
     Protein         1..433
                     /product="ectonucleoside triphosphate diphosphohydrolase 6
                     isoform 2"
                     /EC_number="3.6.1.6"
                     /note="CD39 antigen-like 2; NTPDase 6"
                     /calculated_mol_wt=46971
     Site            13..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U0P5.1)"
     Region          72..424
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
     CDS             1..433
                     /gene="Entpd6"
                     /gene_synonym="2700026H11Rik; Cd39l2; NTPDase-6"
                     /coded_by="NM_001370630.1:184..1485"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:12497"
                     /db_xref="MGI:MGI:1202295"
ORIGIN      
        1 mrkipnhgtl rmtkvayplg lcvglfiyva yikwhrasaa qafftiagaa sgarwtqqaf
       61 sspgsaargh evfygimfda gstgtrihvf qfarppgetp tlthetfkal kpglsayadd
      121 veksaqgiqe llnvakqhip ydfwkatplv lkataglrll pgekaqkllq kvkevfkasp
      181 flvgddcvsi mngtdegvsa witvnfltgs lktpgsssvg mldlgggstq itflprvegt
      241 lqasppghlt alqmfnrtyk lysysylglg lmsarlailg gvegkpaend kelvspclsp
      301 rfrgewehae vtyrisgqka vglyelcasr vsevlrnkvh rteeaqhvdf yafsyyydla
      361 asfglidaek ggslvvgdfe iaakyvcrtl etqppsspfa cmdltyisll lhefgfpgdk
      421 vlkippglcs sal
//
LOCUS       NP_982279                367 aa            linear   PRI 27-APR-2025
DEFINITION  putative C->U-editing enzyme APOBEC-4 [Homo sapiens].
ACCESSION   NP_982279
VERSION     NP_982279.1
DBSOURCE    REFSEQ: accession NM_203454.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Marino,D., Perkovic,M., Hain,A., Jaguva Vasudevan,A.A., Hofmann,H.,
            Hanschmann,K.M., Muhlebach,M.D., Schumann,G.G., Konig,R.,
            Cichutek,K., Haussinger,D. and Munk,C.
  TITLE     APOBEC4 Enhances the Replication of HIV-1
  JOURNAL   PLoS One 11 (6), e0155422 (2016)
   PUBMED   27249646
  REMARK    GeneRIF: APOBEC4 was capable of similarly enhancing transcription
            from a broad spectrum of promoters, regardless of whether they were
            viral or mammalian
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Yang,W., Tang,H., Zhang,Y., Tang,X., Zhang,J., Sun,L., Yang,J.,
            Cui,Y., Zhang,L., Hirankarn,N., Cheng,H., Pan,H.F., Gao,J.,
            Lee,T.L., Sheng,Y., Lau,C.S., Li,Y., Chan,T.M., Yin,X., Ying,D.,
            Lu,Q., Leung,A.M., Zuo,X., Chen,X., Tong,K.L., Zhou,F., Diao,Q.,
            Tse,N.K., Xie,H., Mok,C.C., Hao,F., Wong,S.N., Shi,B., Lee,K.W.,
            Hui,Y., Ho,M.H., Liang,B., Lee,P.P., Cui,H., Guo,Q., Chung,B.H.,
            Pu,X., Liu,Q., Zhang,X., Zhang,C., Chong,C.Y., Fang,H., Wong,R.W.,
            Sun,Y., Mok,M.Y., Li,X.P., Avihingsanon,Y., Zhai,Z.,
            Rianthavorn,P., Deekajorndej,T., Suphapeetiporn,K., Gao,F.,
            Shotelersuk,V., Kang,X., Ying,S.K., Zhang,L., Wong,W.H., Zhu,D.,
            Fung,S.K., Zeng,F., Lai,W.M., Wong,C.M., Ng,I.O.,
            Garcia-Barcelo,M.M., Cherny,S.S., Shen,N., Tam,P.K., Sham,P.C.,
            Ye,D.Q., Yang,S., Zhang,X. and Lau,Y.L.
  TITLE     Meta-analysis followed by replication identifies loci in or near
            CDKN1B, TET3, CD80, DRAM1, and ARID5B as associated with systemic
            lupus erythematosus in Asians
  JOURNAL   Am J Hum Genet 92 (1), 41-51 (2013)
   PUBMED   23273568
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Prochnow,C., Bransteitter,R. and Chen,X.S.
  TITLE     APOBEC deaminases-mutases with defensive roles for immunity
  JOURNAL   Sci China C Life Sci 52 (10), 893-902 (2009)
   PUBMED   19911124
  REMARK    GeneRIF: Studies indicate the APOBEC family consists of 11 members:
            APOBEC-1 (Apo1), APOBEC-2 (Apo2), activation induced cytidine
            deaminase (AID), APOBEC- 3A, -3B, -3C, -3DE, -3F, -3H (Apo3A-H) and
            APOBEC- 4 (Apo4).
            Review article
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Rogozin,I.B., Basu,M.K., Jordan,I.K., Pavlov,Y.I. and Koonin,E.V.
  TITLE     APOBEC4, a new member of the AID/APOBEC family of polynucleotide
            (deoxy)cytidine deaminases predicted by computational analysis
  JOURNAL   Cell Cycle 4 (9), 1281-1285 (2005)
   PUBMED   16082223
  REMARK    GeneRIF: APOBEC4 is expressed primarily in testis which suggests
            the possibility that it is an editing enzyme for mRNAs involved in
            spermatogenesis
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL137800.12, BC021711.2 and
            AI961390.1.
            
            Summary: This gene encodes a member of the AID/APOBEC family of
            polynucleotide (deoxy)cytidine deaminases, which convert cytidine
            to uridine. Other AID/APOBEC family members are involved in mRNA
            editing, somatic hypermutation and recombination of immunoglobulin
            genes, and innate immunity to retroviral infection. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021711.2, SRR5189667.353799.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308641.6/ ENSP00000310622.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.3"
     Protein         1..367
                     /product="putative C->U-editing enzyme APOBEC-4"
                     /note="apolipoprotein B mRNA editing enzyme, catalytic
                     polypeptide-like 4 (putative)"
                     /calculated_mol_wt=41450
     Region          47..202
                     /region_name="APOBEC_N"
                     /note="APOBEC-like N-terminal domain; pfam08210"
                     /db_xref="CDD:462396"
     CDS             1..367
                     /gene="APOBEC4"
                     /gene_synonym="C1orf169"
                     /coded_by="NM_203454.3:276..1379"
                     /db_xref="CCDS:CCDS1358.1"
                     /db_xref="GeneID:403314"
                     /db_xref="HGNC:HGNC:32152"
                     /db_xref="MIM:609908"
ORIGIN      
        1 mepiyeeyla nhgtivkpyy wlsfsldcsn cpyhirtgee arvsltefcq ifgfpygttf
       61 pqtkhltfye lktssgslvq kghassctgn yihpesmlfe mngyldsaiy nndsirhiil
      121 ysnnspcnea nhcciskmyn flitypgitl siyfsqlyht emdfpasawn realrslasl
      181 wprvvlspis ggiwhsvlhs fisgvsgshv fqpiltgral adrhnayein aitgvkpyft
      241 dvllqtkrnp ntkaqeales yplnnafpgq ffqmpsgqlq pnlppdlrap vvfvlvplrd
      301 lppmhmgqnp nkprnivrhl nmpqmsfqet kdlgrlptgr sveiveiteq fasskeadek
      361 kkkkgkk
//
LOCUS       NP_055830               1096 aa            linear   PRI 27-APR-2025
DEFINITION  lysine-specific demethylase 4B isoform 1 [Homo sapiens].
ACCESSION   NP_055830 XP_290852
VERSION     NP_055830.1
DBSOURCE    REFSEQ: accession NM_015015.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Li,Y.Q., Shao,Y.L., Li,M.Y., Wang,L.L. and Gao,X.N.
  TITLE     [The Regulatory Effect of RNA m6 A Methylation Modification on
            KDM4B Gene Expression in t (8;21) AML Cells by MeRIP-qPCR]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 32 (2), 382-388 (2024)
   PUBMED   38660840
  REMARK    GeneRIF: [The Regulatory Effect of RNA m[6] A Methylation
            Modification on KDM4B Gene Expression in t (8;21) AML Cells by
            MeRIP-qPCR].
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Wang,X.Y., Li,H.M., Xia,R., Li,X., Zhang,X., Jin,T.Z. and
            Zhang,H.S.
  TITLE     KDM4B down-regulation facilitated breast cancer cell stemness via
            PHGDH upregulation in H3K36me3-dependent manner
  JOURNAL   Mol Cell Biochem 479 (4), 915-928 (2024)
   PUBMED   37249813
  REMARK    GeneRIF: KDM4B down-regulation facilitated breast cancer cell
            stemness via PHGDH upregulation in H3K36me3-dependent manner.
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Wang,Z., Cai,H., Li,Z., Sun,W., Zhao,E. and Cui,H.
  TITLE     Histone demethylase KDM4B accelerates the progression of
            glioblastoma via the epigenetic regulation of MYC stability
  JOURNAL   Clin Epigenetics 15 (1), 192 (2023)
   PUBMED   38093312
  REMARK    GeneRIF: Histone demethylase KDM4B accelerates the progression of
            glioblastoma via the epigenetic regulation of MYC stability.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1096)
  AUTHORS   Tang,H., Guan,Y., Yuan,Z., Guo,T., Tan,X., Fan,Y., Zhang,E. and
            Wang,X.
  TITLE     Histone demethylase KDM4B contributes to advanced clear cell renal
            carcinoma and association with copy number variations and cell
            cycle progression
  JOURNAL   Epigenetics 18 (1), 2192319 (2023)
   PUBMED   36952476
  REMARK    GeneRIF: Histone demethylase KDM4B contributes to advanced clear
            cell renal carcinoma and association with copy number variations
            and cell cycle progression.
REFERENCE   5  (residues 1 to 1096)
  AUTHORS   Shao,Y.L., Li,Y.Q., Li,M.Y., Wang,L.L., Zhou,H.S., Liu,D.H., Yu,L.,
            Lin,J. and Gao,X.N.
  TITLE     HIF1alpha-mediated transactivation of WTAP promotes AML cell
            proliferation via m6A-dependent stabilization of KDM4B mRNA
  JOURNAL   Leukemia 37 (6), 1254-1267 (2023)
   PUBMED   37087529
  REMARK    GeneRIF: HIF1alpha-mediated transactivation of WTAP promotes AML
            cell proliferation via m[6]A-dependent stabilization of KDM4B mRNA.
REFERENCE   6  (residues 1 to 1096)
  AUTHORS   Whetstine,J.R., Nottke,A., Lan,F., Huarte,M., Smolikov,S., Chen,Z.,
            Spooner,E., Li,E., Zhang,G., Colaiacovo,M. and Shi,Y.
  TITLE     Reversal of histone lysine trimethylation by the JMJD2 family of
            histone demethylases
  JOURNAL   Cell 125 (3), 467-481 (2006)
   PUBMED   16603238
REFERENCE   7  (residues 1 to 1096)
  AUTHORS   Gray,S.G., Iglesias,A.H., Lizcano,F., Villanueva,R., Camelo,S.,
            Jingu,H., Teh,B.T., Koibuchi,N., Chin,W.W., Kokkotou,E. and
            Dangond,F.
  TITLE     Functional characterization of JMJD2A, a histone deacetylase- and
            retinoblastoma-binding protein
  JOURNAL   J Biol Chem 280 (31), 28507-28518 (2005)
   PUBMED   15927959
REFERENCE   8  (residues 1 to 1096)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 1096)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of JMJD2 family genes in silico
  JOURNAL   Int J Oncol 24 (6), 1623-1628 (2004)
   PUBMED   15138608
REFERENCE   10 (residues 1 to 1096)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB636535.1, AB020683.2, BF917212.1, DA379611.1, AF052144.1 and
            BC015378.1.
            
            On Mar 22, 2004 this sequence version replaced XP_290852.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB020683.2, DRR138518.343131.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000159111.9/ ENSP00000159111.3
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1096
                     /product="lysine-specific demethylase 4B isoform 1"
                     /EC_number="1.14.11.66"
                     /note="jumonji domain containing 2B; lysine-specific
                     demethylase 4B; lysine (K)-specific demethylase 4B;
                     jumonji domain-containing protein 2B; jmjC
                     domain-containing histone demethylation protein 3B; tudor
                     domain containing 14B; [histone H3]-trimethyl-L-lysine(9)
                     demethylase 4B"
                     /calculated_mol_wt=121767
     Region          15..56
                     /region_name="JmjN"
                     /note="Small domain found in the jumonji family of
                     transcription factors; smart00545"
                     /db_xref="CDD:128818"
     Region          176..292
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     Region          369..478
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94953.4)"
     Region          557..649
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94953.4)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94953.4)"
     Site            602
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O94953.4)"
     Region          683..788
                     /region_name="PHD_JMJD2B"
                     /note="PHD finger found in Jumonji domain-containing
                     protein 2B (JMJD2B); cd15576"
                     /db_xref="CDD:277051"
     Site            order(683,756..760,764,783)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277051"
     Region          797..906
                     /region_name="ePHD_JMJD2B"
                     /note="Extended PHD finger found in Jumonji
                     domain-containing protein 2B (JMJD2B); cd15714"
                     /db_xref="CDD:277184"
     Site            order(851,865..869,875,901)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277184"
     Region          919..972
                     /region_name="Tudor_JMJD2B_rpt1"
                     /note="first Tudor domain found in Jumonji
                     domain-containing protein 2B (JMJD2B) and similar
                     proteins; cd20464"
                     /db_xref="CDD:410535"
     Site            order(920..921,940..944)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:410535"
     Site            order(951..952,954..957,959)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410535"
     Region          976..1031
                     /region_name="Tudor_JMJD2B_rpt2"
                     /note="second Tudor domain found in Jumonji
                     domain-containing protein 2B (JMJD2B) and similar
                     proteins; cd20467"
                     /db_xref="CDD:410538"
     Site            order(987..989,993)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410538"
     Site            order(1004,1006,1012..1013)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:410538"
     Region          1037..1073
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94953.4)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94953.4)"
     CDS             1..1096
                     /gene="KDM4B"
                     /gene_synonym="JMJD2B; MRD65; TDRD14B"
                     /coded_by="NM_015015.3:227..3517"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12138.1"
                     /db_xref="GeneID:23030"
                     /db_xref="HGNC:HGNC:29136"
                     /db_xref="MIM:609765"
ORIGIN      
        1 mgsedhgaqn psckimtfrp tmeefkdfnk yvayiesqga hraglakiip pkewkprqty
       61 ddiddvvipa piqqvvtgqs glftqyniqk kamtvgeyrr lansekyctp rhqdfddler
      121 kywknltfvs piygadisgs lydddvaqwn igslrtildm verecgtiie gvntpylyfg
      181 mwkttfawht edmdlysiny lhfgepkswy aippehgkrl erlaigffpg ssqgcdaflr
      241 hkmtlispii lkkygipfsr itqeagefmi tfpygyhagf nhgfncaest nfatlrwidy
      301 gkvatqctcr kdmvkismdv fvrilqpery elwkqgkdlt vldhtrptal tspelsswsa
      361 sraslkakll rrshrkrsqp kkpkpedpkf pgegtagaal leeaggsvke eagpevdpee
      421 eeeepqplph greaegaeed grgklrptka kserkkksfg llppqlpppp ahfpseealw
      481 lpspleppvl gpgpaamees plpaplnvvp pevpseelea kprpiipmly vvprpgkaaf
      541 nqehvscqqa fehfaqkgpt wkepvspmel tgpedgaass gagrmetkar agegqapstf
      601 sklkmeikks rrhplgrppt rsplsvvkqe assdeeaspf sgeedvsdpd alrpllslqw
      661 knraasfqae rkfnaaaart epycaictlf ypycqalqte keapiaslge gcpatlpsks
      721 rqktrplipe mcftsggent eplpansyig ddgtspliac gkcclqvhas cygirpelvn
      781 egwtcsrcaa hawtaecclc nlrggalqmt tdrrwihvic aiavpearfl nvierhpvdi
      841 saipeqrwkl kcvycrkrmk kvsgaciqcs yehcstsfhv tcahaagvlm epddwpyvvs
      901 itclkhksgg havqllravs lgqvvitknr nglyyrcrvi gaasqtcyev nfddgsysdn
      961 lypesitsrd cvqlgppseg elvelrwtdg nlykakfiss vtshiyqvef edgsqltvkr
     1021 gdiftleeel pkrvrsrlsl stgapqepaf sgeeakaakr prvgtplate dsgrsqdyva
     1081 fvesllqvqg rpgapf
//
LOCUS       NP_998786                510 aa            linear   PRI 27-APR-2025
DEFINITION  5-hydroxytryptamine receptor 3A isoform a precursor [Homo sapiens].
ACCESSION   NP_998786
VERSION     NP_998786.3
DBSOURCE    REFSEQ: accession NM_213621.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Nikolic,J., Vukojevic,K., Soljic,V., Miskovic,J., Orlovic Vlaho,M.,
            Saraga-Babic,M. and Filipovic,N.
  TITLE     Expression Patterns of Serotonin Receptors 5-HT1A, 5-HT2A, and
            5-HT3A during Human Fetal Lung Development
  JOURNAL   Int J Mol Sci 24 (3), 2965 (2023)
   PUBMED   36769290
  REMARK    GeneRIF: Expression Patterns of Serotonin Receptors 5-HT1A, 5-HT2A,
            and 5-HT3A during Human Fetal Lung Development.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Berens,S., Dong,Y., Fritz,N., Walstab,J., D'Amato,M., Zheng,T.,
            Wahl,V., Boekstegers,F., Bermejo,J.L., Martinez,C.,
            Schmitteckert,S., Clevers,E., Engel,F., Gauss,A., Herzog,W.,
            Spiller,R., Goebel-Stengel,M., Monnikes,H., Andresen,V., Thomas,F.,
            Keller,J., Pehl,C., Stein-Thoringer,C., Clarke,G., Dinan,T.G.,
            Quigley,E.M., Sayuk,G., Simren,M., Tesarz,J., Rappold,G., van
            Oudenhove,L., Schaefert,R. and Niesler,B.
  TITLE     Serotonin type 3 receptor subunit gene polymorphisms associated
            with psychosomatic symptoms in irritable bowel syndrome: A
            multicenter retrospective study
  JOURNAL   World J Gastroenterol 28 (21), 2334-2349 (2022)
   PUBMED   35800179
  REMARK    GeneRIF: Serotonin type 3 receptor subunit gene polymorphisms
            associated with psychosomatic symptoms in irritable bowel syndrome:
            A multicenter retrospective study.
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Olatunji,B.O., Cox,R.C. and Blackford,J.U.
  TITLE     Fear reacquisition and symptoms of combat-related PTSD: Specificity
            and preliminary examination of the influence of the 5-HT3A receptor
            gene
  JOURNAL   Behav Res Ther 153, 104085 (2022)
   PUBMED   35413654
  REMARK    GeneRIF: Fear reacquisition and symptoms of combat-related PTSD:
            Specificity and preliminary examination of the influence of the
            5-HT3A receptor gene.
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Ritter,K.E., Buehler,D.P., Asher,S.B., Deal,K.K., Zhao,S., Guo,Y.
            and Southard-Smith,E.M.
  TITLE     5-HT3 Signaling Alters Development of Sacral Neural Crest
            Derivatives That Innervate the Lower Urinary Tract
  JOURNAL   Int J Mol Sci 22 (13), 6838 (2021)
   PUBMED   34202161
  REMARK    GeneRIF: 5-HT3 Signaling Alters Development of Sacral Neural Crest
            Derivatives That Innervate the Lower Urinary Tract.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Basak,S., Kumar,A., Ramsey,S., Gibbs,E., Kapoor,A., Filizola,M. and
            Chakrapani,S.
  TITLE     High-resolution structures of multiple 5-HT3AR-setron complexes
            reveal a novel mechanism of competitive inhibition
  JOURNAL   Elife 9, e57870 (2020)
   PUBMED   33063666
  REMARK    GeneRIF: High-resolution structures of multiple 5-HT3AR-setron
            complexes reveal a novel mechanism of competitive inhibition.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Niesler,B., Flohr,T., Nothen,M.M., Fischer,C., Rietschel,M.,
            Franzek,E., Albus,M., Propping,P. and Rappold,G.A.
  TITLE     Association between the 5' UTR variant C178T of the serotonin
            receptor gene HTR3A and bipolar affective disorder
  JOURNAL   Pharmacogenetics 11 (6), 471-475 (2001)
   PUBMED   11505217
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Belelli,D., Balcarek,J.M., Hope,A.G., Peters,J.A., Lambert,J.J. and
            Blackburn,T.P.
  TITLE     Cloning and functional expression of a human 5-hydroxytryptamine
            type 3AS receptor subunit
  JOURNAL   Mol Pharmacol 48 (6), 1054-1062 (1995)
   PUBMED   8848005
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Weiss,B., Mertz,A., Schrock,E., Koenen,M. and Rappold,G.
  TITLE     Assignment of a human homolog of the mouse Htr3 receptor gene to
            chromosome 11q23.1-q23.2
  JOURNAL   Genomics 29 (1), 304-305 (1995)
   PUBMED   8530095
REFERENCE   9  (residues 1 to 510)
  AUTHORS   Miyake,A., Mochizuki,S., Takemoto,Y. and Akuzawa,S.
  TITLE     Molecular cloning of human 5-hydroxytryptamine3 receptor:
            heterogeneity in distribution and function among species
  JOURNAL   Mol Pharmacol 48 (3), 407-416 (1995)
   PUBMED   7565620
REFERENCE   10 (residues 1 to 510)
  AUTHORS   Uetz,P., Abdelatty,F., Villarroel,A., Rappold,G., Weiss,B. and
            Koenen,M.
  TITLE     Organisation of the murine 5-HT3 receptor gene and assignment to
            human chromosome 11
  JOURNAL   FEBS Lett 339 (3), 302-306 (1994)
   PUBMED   8112471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK304630.1, AJ003078.1,
            AP000908.4 and CD014118.1.
            
            On Jul 27, 2018 this sequence version replaced NP_998786.2.
            
            Summary: The product of this gene belongs to the ligand-gated ion
            channel receptor superfamily. This gene encodes subunit A of the
            type 3 receptor for 5-hydroxytryptamine (serotonin), a biogenic
            hormone that functions as a neurotransmitter, a hormone, and a
            mitogen. This receptor causes fast, depolarizing responses in
            neurons after activation. It appears that the heteromeric
            combination of A and B subunits is necessary to provide the full
            functional features of this receptor, since either subunit alone
            results in receptors with very low conductance and response
            amplitude. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1), also known as h5-HT3RL,
            represents the longest transcript, and encodes the longest isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD014118.1, AJ003078.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            regulatory uORF                  :: PMID: 11505217
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.2"
     Protein         1..510
                     /product="5-hydroxytryptamine receptor 3A isoform a
                     precursor"
                     /note="serotonin-gated ion channel receptor; 5HT3
                     serotonin receptor; serotonin receptor 3A;
                     5-hydroxytryptamine receptor 3; 5-hydroxytryptamine
                     (serotonin) receptor 3A, ionotropic"
                     /calculated_mol_wt=56286
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2121
     Region          23..504
                     /region_name="LIC"
                     /note="Cation transporter family protein; TIGR00860"
                     /db_xref="CDD:273305"
     CDS             1..510
                     /gene="HTR3A"
                     /gene_synonym="5-HT-3; 5-HT3A; 5-HT3R; 5HT3R; HTR3"
                     /coded_by="NM_213621.4:219..1751"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8366.3"
                     /db_xref="GeneID:3359"
                     /db_xref="HGNC:HGNC:5297"
                     /db_xref="MIM:182139"
ORIGIN      
        1 mllwvqqall alllptllaq gearrsrntt rpallrlsdy lltnyrkgvr pvrdwrkptt
       61 vsidvivyai lnvdeknqvl ttyiwyrqyw tdeflqwnpe dfdnitklsi ptdsiwvpdi
      121 linefvdvgk spnipyvyir hqgevqnykp lqvvtacsld iynfpfdvqn csltftswlh
      181 tiqdinislw rlpekvksdr svfmnqgewe llgvlpyfre fsmessnyya emkfyvvirr
      241 rplfyvvsll lpsiflmvmd ivgfylppns gervsfkitl llgysvflii vsdtlpatai
      301 gtpligkapp gsraqsgekp apshllhvsl asalgctgvy fvvcmallvi slaetifivr
      361 lvhkqdlqqp vpawlrhlvl eriawllclr eqstsqrppa tsqatktddc samgnhcshm
      421 ggpqdfeksp rdrcsppppp reaslavcgl lqelssirqf lekrdeirev ardwlrvgsv
      481 ldkllfhiyl lavlaysitl vmlwsiwqya
//
LOCUS       NP_001123947             395 aa            linear   PRI 27-APR-2025
DEFINITION  THAP domain-containing protein 5 isoform 1 [Homo sapiens].
ACCESSION   NP_001123947
VERSION     NP_001123947.1
DBSOURCE    REFSEQ: accession NM_001130475.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Yoon,D., Kim,Y.J., Cui,W.Y., Van der Vaart,A., Cho,Y.S., Lee,J.Y.,
            Ma,J.Z., Payne,T.J., Li,M.D. and Park,T.
  TITLE     Large-scale genome-wide association study of Asian population
            reveals genetic factors in FRMD4A and other loci influencing
            smoking initiation and nicotine dependence
  JOURNAL   Hum Genet 131 (6), 1009-1021 (2012)
   PUBMED   22006218
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Cilenti,L., Balakrishnan,M.P., Wang,X.L., Ambivero,C.,
            Sterlicchi,M., del Monte,F., Ma,X.L. and Zervos,A.S.
  TITLE     Regulation of Abro1/KIAA0157 during myocardial infarction and cell
            death reveals a novel cardioprotective mechanism for Lys63-specific
            deubiquitination
  JOURNAL   J Mol Cell Cardiol 50 (4), 652-661 (2011)
   PUBMED   21195082
  REMARK    GeneRIF: Study identified Abro1 as a specific interactor of THAP5,
            a zinc finger transcription factor that is involved in G2/M control
            and apoptosis.
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Balakrishnan,M.P., Cilenti,L., Ambivero,C., Goto,Y., Takata,M.,
            Turkson,J., Li,X.S. and Zervos,A.S.
  TITLE     THAP5 is a DNA-binding transcriptional repressor that is regulated
            in melanoma cells during DNA damage-induced cell death
  JOURNAL   Biochem Biophys Res Commun 404 (1), 195-200 (2011)
   PUBMED   21110952
  REMARK    GeneRIF: this work suggests that THAP5 is a DNA-binding protein and
            a transcriptional repressor. THAP5 has a pro-apoptotic function and
            it was induced in melanoma cells under conditions that promoted
            cell death.
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Docherty,S.J., Kovas,Y., Petrill,S.A. and Plomin,R.
  TITLE     Generalist genes analysis of DNA markers associated with
            mathematical ability and disability reveals shared influence across
            ages and abilities
  JOURNAL   BMC Genet 11, 61 (2010)
   PUBMED   20602751
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Balakrishnan,M.P., Cilenti,L., Mashak,Z., Popat,P., Alnemri,E.S.
            and Zervos,A.S.
  TITLE     THAP5 is a human cardiac-specific inhibitor of cell cycle that is
            cleaved by the proapoptotic Omi/HtrA2 protease during cell death
  JOURNAL   Am J Physiol Heart Circ Physiol 297 (2), H643-H653 (2009)
   PUBMED   19502560
  REMARK    GeneRIF: THAP5 and its regulation by Omi/HtrA2 provide a new link
            between cell cycle control and apoptosis in cardiomyocytes
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Roussigne,M., Kossida,S., Lavigne,A.C., Clouaire,T., Ecochard,V.,
            Glories,A., Amalric,F. and Girard,J.P.
  TITLE     The THAP domain: a novel protein motif with similarity to the
            DNA-binding domain of P element transposase
  JOURNAL   Trends Biochem Sci 28 (2), 66-69 (2003)
   PUBMED   12575992
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL833137.1 and AC005058.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.171430.1,
                                           SRR1803616.65885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147920, SAMEA2155371
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000415914.4/ ENSP00000400500.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..395
                     /product="THAP domain-containing protein 5 isoform 1"
                     /note="THAP domain-containing protein 5"
                     /calculated_mol_wt=45285
     Region          4..85
                     /region_name="THAP"
                     /note="The THAP domain is a putative DNA-binding domain
                     (DBD) and probably also binds a zinc ion; smart00980"
                     /db_xref="CDD:214951"
     Region          85..112
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6K1.2)"
     Region          321..324
                     /region_name="HCFC1-binding motif (HBM).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6K1.2)"
     CDS             1..395
                     /gene="THAP5"
                     /coded_by="NM_001130475.3:138..1325"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47687.1"
                     /db_xref="GeneID:168451"
                     /db_xref="HGNC:HGNC:23188"
                     /db_xref="MIM:612534"
ORIGIN      
        1 mprycaaicc knrrgrnnkd rklsfypfpl hdkerlekwl knmkrdswvp skyqflcsdh
       61 ftpdsldirw girylkqtav ptifslpedn qgkdpskkks qkknledeke vcpkaksees
      121 fvlnetkkni vntdvphqhp ellhssslvk ppapktgsiq nnmltlnlvk qhtgkpestl
      181 etsvnqdtgr ggfhtcfenl nsttitltts nsesihqsle tqevlevtts hlanpnftsn
      241 smeiksaqen pflfstinqt veelntnkes viaifvpaen skpsvnsfis aqkettemed
      301 tdiedslykd vdygtevlqi ehsycrqdin kehlwqkvsk lhskitllel keqqtlgrlk
      361 slealirqlk qenwlseenv kiienhftty evtmi
//
LOCUS       NP_996879               2223 aa            linear   PRI 27-APR-2025
DEFINITION  sperm-associated antigen 17 [Homo sapiens].
ACCESSION   NP_996879
VERSION     NP_996879.1
DBSOURCE    REFSEQ: accession NM_206996.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2223)
  AUTHORS   Sapao,P., Roberson,E.D.O., Shi,B., Assassi,S., Skaug,B., Lee,F.,
            Naba,A., Perez White,B.E., Cordova-Fletes,C., Tsou,P.S.,
            Sawalha,A.H., Gudjonsson,J.E., Ma,F., Verma,P., Bhattacharyya,D.,
            Carns,M., Strauss,J.F. 3rd, Sicard,D., Tschumperlin,D.J.,
            Champer,M.I., Campagnola,P.J., Teves,M.E. and Varga,J.
  TITLE     Reduced SPAG17 Expression in Systemic Sclerosis Triggers
            Myofibroblast Transition and Drives Fibrosis
  JOURNAL   J Invest Dermatol 143 (2), 284-293 (2023)
   PUBMED   36116512
  REMARK    GeneRIF: Reduced SPAG17 Expression in Systemic Sclerosis Triggers
            Myofibroblast Transition and Drives Fibrosis.
REFERENCE   2  (residues 1 to 2223)
  AUTHORS   Roberson,E.D.O., Carns,M., Cao,L., Aren,K., Goldberg,I.A.,
            Morales-Heil,D.J., Korman,B.D., Atkinson,J.P. and Varga,J.
  TITLE     Alterations of the Primary Cilia Gene SPAG17 and SOX9 Locus
            Noncoding RNAs Identified by RNA-Sequencing Analysis in Patients
            With Systemic Sclerosis
  JOURNAL   Arthritis Rheumatol 75 (1), 108-119 (2023)
   PUBMED   35762854
  REMARK    GeneRIF: Alterations of the Primary Cilia Gene SPAG17 and SOX9
            Locus Noncoding RNAs Identified by RNA-Sequencing Analysis in
            Patients With Systemic Sclerosis.
REFERENCE   3  (residues 1 to 2223)
  AUTHORS   Cordova-Fletes,C., Becerra-Solano,L.E., Rangel-Sosa,M.M.,
            Rivas-Estilla,A.M., Alberto Galan-Huerta,K., Ortiz-Lopez,R.,
            Rojas-Martinez,A., Juarez-Vazquez,C.I. and Garcia-Ortiz,J.E.
  TITLE     Uncommon runs of homozygosity disclose homozygous missense
            mutations in two ciliopathy-related genes (SPAG17 and WDR35) in a
            patient with multiple brain and skeletal anomalies
  JOURNAL   Eur J Med Genet 61 (3), 161-167 (2018)
   PUBMED   29174089
  REMARK    GeneRIF: Homozygous missense mutation in SPAG17 gene is associated
            with multiple congenital anomalies, including brain malformations
            and skeletal dysplasia suggestive of cranioectodermal dysplasia
            ciliopathy.
REFERENCE   4  (residues 1 to 2223)
  AUTHORS   Xu,X., Sha,Y.W., Mei,L.B., Ji,Z.Y., Qiu,P.P., Ji,H., Li,P., Wang,T.
            and Li,L.
  TITLE     A familial study of twins with severe asthenozoospermia identified
            a homozygous SPAG17 mutation by whole-exome sequencing
  JOURNAL   Clin Genet 93 (2), 345-349 (2018)
   PUBMED   28548327
  REMARK    GeneRIF: In silico analysis revealed that R1448Q is a potential
            pathogenic mutation. Immunostaining and western blot assays showed
            that the R1448Q mutation may exert a negative effect on the
            steady-state of the SPAG17 protein. Therefore, SPAG17 may be a new
            pathogenic gene causing Asthenozoospermia (AZS) .
REFERENCE   5  (residues 1 to 2223)
  AUTHORS   Teves,M.E., Nagarkatti-Gude,D.R., Zhang,Z. and Strauss,J.F. 3rd.
  TITLE     Mammalian axoneme central pair complex proteins: Broader roles
            revealed by gene knockout phenotypes
  JOURNAL   Cytoskeleton (Hoboken) 73 (1), 3-22 (2016)
   PUBMED   26785425
  REMARK    Review article
REFERENCE   6  (residues 1 to 2223)
  AUTHORS   Teves,M.E., Sundaresan,G., Cohen,D.J., Hyzy,S.L., Kajan,I.,
            Maczis,M., Zhang,Z., Costanzo,R.M., Zweit,J., Schwartz,Z.,
            Boyan,B.D. and Strauss,J.F. 3rd.
  TITLE     Spag17 deficiency results in skeletal malformations and bone
            abnormalities
  JOURNAL   PLoS One 10 (5), e0125936 (2015)
   PUBMED   26017218
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 2223)
  AUTHORS   Silina,K., Zayakin,P., Kalnina,Z., Ivanova,L., Meistere,I.,
            Endzelins,E., Abols,A., Stengrevics,A., Leja,M., Ducena,K.,
            Kozirovskis,V. and Line,A.
  TITLE     Sperm-associated antigens as targets for cancer immunotherapy:
            expression pattern and humoral immune response in cancer patients
  JOURNAL   J Immunother 34 (1), 28-44 (2011)
   PUBMED   21150711
REFERENCE   8  (residues 1 to 2223)
  AUTHORS   Zhao,J., Li,M., Bradfield,J.P., Zhang,H., Mentch,F.D., Wang,K.,
            Sleiman,P.M., Kim,C.E., Glessner,J.T., Hou,C., Keating,B.J.,
            Thomas,K.A., Garris,M.L., Deliard,S., Frackelton,E.C., Otieno,F.G.,
            Chiavacci,R.M., Berkowitz,R.I., Hakonarson,H. and Grant,S.F.
  TITLE     The role of height-associated loci identified in genome wide
            association studies in the determination of pediatric stature
  JOURNAL   BMC Med Genet 11, 96 (2010)
   PUBMED   20546612
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2223)
  AUTHORS   Kim,J.J., Lee,H.I., Park,T., Kim,K., Lee,J.E., Cho,N.H., Shin,C.,
            Cho,Y.S., Lee,J.Y., Han,B.G., Yoo,H.W. and Lee,J.K.
  TITLE     Identification of 15 loci influencing height in a Korean population
  JOURNAL   J Hum Genet 55 (1), 27-31 (2010)
   PUBMED   19893584
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   10 (residues 1 to 2223)
  AUTHORS   Zhang,Z., Jones,B.H., Tang,W., Moss,S.B., Wei,Z., Ho,C.,
            Pollack,M., Horowitz,E., Bennett,J., Baker,M.E. and Strauss,J.F.
            3rd.
  TITLE     Dissecting the axoneme interactome: the mammalian orthologue of
            Chlamydomonas PF6 interacts with sperm-associated antigen 6, the
            mammalian orthologue of Chlamydomonas PF16
  JOURNAL   Mol Cell Proteomics 4 (7), 914-923 (2005)
   PUBMED   15827353
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513191.4, DB060943.1,
            AY555274.1, DB340825.1 and AL121993.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a central pair protein present in the
            axonemes of cells with a '9 + 2' organization of microtubules. The
            encoded protein is required for the proper function of the axoneme.
            Mutations in the orthologous gene in mice lead to primary ciliary
            dyskinesia characterized by immotile nasal and tracheal cilia,
            reduced clearance of nasal mucus, profound respiratory distress,
            hydrocephalus, and neonatal lethality within twelve hours of birth
            due to impaired airway mucociliary clearance. Single-nucleotide
            polymorphisms in this gene are associated with human height and
            targeted mutations lead to skeletal malformations affecting the
            limbs in mice, suggesting a role for this gene in skeletal
            development. [provided by RefSeq, Feb 2017].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY555274.1, BX648110.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336338.10/ ENSP00000337804.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..2223
                     /product="sperm-associated antigen 17"
                     /note="projection protein PF6 homolog"
                     /calculated_mol_wt=251612
     Region          144..214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q759.1)"
     Region          248..>346
                     /region_name="Leo1"
                     /note="Leo1-like protein; pfam04004"
                     /db_xref="CDD:461126"
     Region          387..416
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q759.1)"
     Region          680..710
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q759.1)"
     Region          731..762
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q759.1)"
     Region          950..1015
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q759.1)"
     Region          1179..1212
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q759.1)"
     Region          1345..1378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q759.1)"
     Region          1938..1957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q759.1)"
     Region          1962..2008
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q759.1)"
     Region          2076..2180
                     /region_name="PapD-like"
                     /note="Flagellar-associated PapD-like; pfam14874"
                     /db_xref="CDD:373355"
     CDS             1..2223
                     /gene="SPAG17"
                     /gene_synonym="CT143; PF6; SPGF55"
                     /coded_by="NM_206996.4:72..6743"
                     /db_xref="CCDS:CCDS899.1"
                     /db_xref="GeneID:200162"
                     /db_xref="HGNC:HGNC:26620"
                     /db_xref="MIM:616554"
ORIGIN      
        1 mapkkekggt vntsskiwep sliaaqfnqn dwqasiafvv gnqieddlli qaltvavqvp
       61 qrklfsmvsw qdilqqinei ntlvgsassk kakkpvggna plyyevltaa kaimdsgekl
      121 tlpligkllk fqllqikfkd qqrrenekkv iedkpklekd kgkakspkek kapsakpakg
      181 kgkdqpeana pvkkttqlkr rgeddhtnry iddepddgaq hyiivvgfnn pqllaimael
      241 gipitsviki ssenyeplqt hlaavnqqqe vllqsedlea eklkkenaik elktfwkyle
      301 pvlnnekpet nlfdvarley mvkaadfpsd wsdgemmlkl gtdifeniac lmydildwkr
      361 qhqhylesmq linvpqvvne kpvleampts eapqpavpap gkkkaqyeep qapppvtsvi
      421 ttevdmryyn yllnpireef isvplilhcm leqvvateed lvppslreps pradgldhri
      481 aahivsllps lclserekkn lhdiflseee neskavpkgp lllnyhdaha hkkyalqdqk
      541 nfdpvqieqe mqsklplwef lqfplpppwn ntkrlatihe lmhfctsdvl swneverafk
      601 vftfeslkls evdekgklkp sgmmcgsdse mfnipwdnpa rfakqirqqy vmkmntqeak
      661 qkadikikdr tlfvdqnlsm svqdnesnre psdpsqcdan nmkhsdlnnl klsvpdnrql
      721 leqesimkaq pqhesleqtt nneikddavt kadshekkpk kmmveadled ikktqqrslm
      781 dwsftehfkp kvllqvlqea hkqyrcvdsy yhtqdnslll vfhnpmnrqr lhceywnial
      841 hsnvgfrnyl elvaksiqdw itkeeaiyqe skmnekiirt raelelkssa nakltsaski
      901 fsikesksnk giskteisdq ekekekekip filegslkaw keeqhrlaee erlreekkae
      961 kkgkeagkkk gkdnaekeds rslkkkspyk ekskeeqvki qevteesphq pepkitypfh
     1021 gynmgniptq isgsnyylyp sdggqievek tmfekgptfi kvrvvkdnhn fmihlndpke
     1081 ivkkeekgdy yleeeeegde eqsletevsd aknkafskfg sfsatlengi clsisyygsn
     1141 gmapedkdpd letilnipsa ltptvvpviv tvpqskakgk ikgkekpkes lkeeehpkee
     1201 ekkeeevepe pvlqetldvp tfqslnvscp sgllltfigq estgqyvide eptwdimvrq
     1261 sypqrvkhye fyktvmppae qeasrvitsq gtvvkymldg stqilfadga vsrspnsgli
     1321 cppsempatp hsgdlmdsis qqksetipse itntkkgksh ksqssmahkg eihdpppeav
     1381 qtvtpvevhi gtwftttpeg nrigtkgler iadltpllsf qatdpvngtv mttredkvvi
     1441 verkdgtriv dhadgtritt fyqvyedqii lpddqetteg prtvtrqvkc mrvessryat
     1501 viancedssc catfgdgtti iakpqgtyqv lppntgslyi dkdcsavych esssniyypf
     1561 qkreqlragr yimrhtsevi cevldpegnt fqvmadgsis tilpekkled dlnektegyd
     1621 slssmhlekn hqqiygehvp rffvmyadgs gmellrdsdi eeylslayke sntvvlqepv
     1681 qeqpgtltit vlrpfheasp wqvkkedtiv ppnlrsrswe tfpsvekktp gppfgtqiwk
     1741 glcieskqlv sapgailksp svlqmrqfiq heviknevkl rlqvslkdyi nyilkkedel
     1801 qemmvkdsrt eeergnaadl lklvmsfpkm eettkshvte vaahltdlfk qslatppkcp
     1861 pdtfgkdffe ktwrhtassk rwkekidktr keiettqnyl mdiknriipp ffkselnqly
     1921 qsqynhldsl skklpsftkk nedanetavq dtsdlnldfk phkvseqkss svpslpkpei
     1981 sadkkdftaq nqtenltksp eeaesyepvk iptqsllqdv agqtrkekvk lphyllsskp
     2041 ksqplakvqd svggkvntss vasaainnak sslfgfhllp ssvkfgvlke ghtyatvvkl
     2101 knvgvdfcrf kvkqpppstg lkvtykpgpv aagmqtelni elfatavged gakgsahish
     2161 nieimtehev lflpveatvl tssnydkrpk dfpqgkenpm vqrtstiyss tlgvfmsrkv
     2221 sph
//
LOCUS       NP_000487                205 aa            linear   PRI 27-APR-2025
DEFINITION  beta-crystallin B2 [Homo sapiens].
ACCESSION   NP_000487
VERSION     NP_000487.1
DBSOURCE    REFSEQ: accession NM_000496.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Sun,J., Morishima,K., Inoue,R., Sugiyama,M. and Takata,T.
  TITLE     Characterization of betaB2-crystallin tryptophan mutants reveals
            two different folding states in solution
  JOURNAL   Protein Sci 33 (7), e5092 (2024)
   PUBMED   38924206
  REMARK    GeneRIF: Characterization of betaB2-crystallin tryptophan mutants
            reveals two different folding states in solution.
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Tovar-Ramirez,M.E., Schuth,N., Rodriguez-Meza,O., Kroll,T.,
            Saab-Rincon,G., Costas,M., Lampi,K. and Quintanar,L.
  TITLE     ATCUN-like Copper Site in betaB2-Crystallin Plays a Protective Role
            in Cataract-Associated Aggregation
  JOURNAL   Inorg Chem 62 (27), 10592-10604 (2023)
   PUBMED   37379524
  REMARK    GeneRIF: ATCUN-like Copper Site in betaB2-Crystallin Plays a
            Protective Role in Cataract-Associated Aggregation.
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Wu,J., Chen,S., Xu,J., Xu,W., Zheng,S., Tian,Q., Luo,C., Chen,X.
            and Shentu,X.
  TITLE     Insight into Pathogenic Mechanism Underlying the Hereditary
            Cataract Caused by betaB2-G149V Mutation
  JOURNAL   Biomolecules 13 (5), 864 (2023)
   PUBMED   37238733
  REMARK    GeneRIF: Insight into Pathogenic Mechanism Underlying the
            Hereditary Cataract Caused by betaB2-G149V Mutation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Velasco-Bolom,J.L. and Dominguez,L.
  TITLE     Conformational stability of the deamidated and mutated human
            betaB2-crystallin
  JOURNAL   Biophys Chem 296, 106986 (2023)
   PUBMED   36905841
  REMARK    GeneRIF: Conformational stability of the deamidated and mutated
            human betaB2-crystallin.
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Yan,Y., Narayan,A., Cho,S., Cheng,Z., Liu,J.O., Zhu,H., Wang,G.,
            Wharram,B., Lisok,A., Brummet,M., Saeki,H., Huang,T.,
            Gabrielson,K., Gabrielson,E., Cope,L., Kanaan,Y.M., Afsari,A.,
            Naab,T., Yfantis,H.G., Ambs,S., Pomper,M.G., Sukumar,S. and
            Merino,V.F.
  TITLE     CRYbetaB2 enhances tumorigenesis through upregulation of nucleolin
            in triple negative breast cancer
  JOURNAL   Oncogene 40 (38), 5752-5763 (2021)
   PUBMED   34341513
  REMARK    GeneRIF: CRYbetaB2 enhances tumorigenesis through upregulation of
            nucleolin in triple negative breast cancer.
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Miesbauer,L.R., Zhou,X., Yang,Z., Yang,Z., Sun,Y., Smith,D.L. and
            Smith,J.B.
  TITLE     Post-translational modifications of water-soluble human lens
            crystallins from young adults
  JOURNAL   J Biol Chem 269 (17), 12494-12502 (1994)
   PUBMED   8175657
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Chambers,C. and Russell,P.
  TITLE     Sequence of the human lens beta B2-crystallin-encoding cDNA
  JOURNAL   Gene 133 (2), 295-299 (1993)
   PUBMED   8224918
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Datiles,M.B., Schumer,D.J., Zigler,J.S. Jr., Russell,P.,
            Anderson,L. and Garland,D.
  TITLE     Two-dimensional gel electrophoretic analysis of human lens proteins
  JOURNAL   Curr Eye Res 11 (7), 669-677 (1992)
   PUBMED   1521468
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Hulsebos,T.J., Bijlsma,E.K., Geurts van Kessel,A.H.,
            Brakenhoff,R.H. and Westerveld,A.
  TITLE     Direct assignment of the human beta B2 and beta B3 crystallin genes
            to 22q11.2----q12: markers for neurofibromatosis 2
  JOURNAL   Cytogenet Cell Genet 56 (3-4), 171-175 (1991)
   PUBMED   2055112
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Aarts,H.J., Den Dunnen,J.T., Lubsen,N.H. and Schoenmakers,J.G.
  TITLE     Linkage between the beta B2 and beta B3 crystallin genes in man and
            rat: a remnant of an ancient beta-crystallin gene cluster
  JOURNAL   Gene 59 (1), 127-135 (1987)
   PUBMED   3436525
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z99916.1, BF847403.1,
            BC069535.1 and BM667912.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Crystallins are separated into two classes:
            taxon-specific, or enzyme, and ubiquitous. The latter class
            constitutes the major proteins of vertebrate eye lens and maintains
            the transparency and refractive index of the lens. Since lens
            central fiber cells lose their nuclei during development, these
            crystallins are made and then retained throughout life, making them
            extremely stable proteins. Mammalian lens crystallins are divided
            into alpha, beta, and gamma families; beta and gamma crystallins
            are also considered as a superfamily. Alpha and beta families are
            further divided into acidic and basic groups. Seven protein regions
            exist in crystallins: four homologous motifs, a connecting peptide,
            and N- and C-terminal extensions. Beta-crystallins, the most
            heterogeneous, differ by the presence of the C-terminal extension
            (present in the basic group, none in the acidic group).
            Beta-crystallins form aggregates of different sizes and are able to
            self-associate to form dimers or to form heterodimers with other
            beta-crystallins. This gene, a beta basic group member, is part of
            a gene cluster with beta-A4, beta-B1, and beta-B3. A
            chain-terminating mutation was found to cause type 2 cerulean
            cataracts. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY794982.2, KR052784.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398215.3/ ENSP00000381273.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.23"
     Protein         1..205
                     /product="beta-crystallin B2"
                     /note="eye lens structural protein; beta-B2 crystallin;
                     beta-crystallin Bp; CTA-221G9.7"
                     /calculated_mol_wt=23249
     Region          2..16
                     /region_name="N-terminal arm"
                     /note="propagated from UniProtKB/Swiss-Prot (P43320.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:8443605; propagated from
                     UniProtKB/Swiss-Prot (P43320.2)"
     Region          18..100
                     /region_name="XTALbg"
                     /note="Beta/gamma crystallins; smart00247"
                     /db_xref="CDD:214583"
     Region          102..106
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P43320.2)"
     Region          108..190
                     /region_name="Crystall"
                     /note="Beta/Gamma crystallin; pfam00030"
                     /db_xref="CDD:459639"
     Region          193..205
                     /region_name="C-terminal arm"
                     /note="propagated from UniProtKB/Swiss-Prot (P43320.2)"
     CDS             1..205
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /coded_by="NM_000496.3:55..672"
                     /db_xref="CCDS:CCDS13831.1"
                     /db_xref="GeneID:1415"
                     /db_xref="HGNC:HGNC:2398"
                     /db_xref="MIM:123620"
ORIGIN      
        1 masdhqtqag kpqslnpkii ifeqenfqgh shelngpcpn lketgvekag svlvqagpwv
       61 gyeqanckge qfvfekgeyp rwdswtssrr tdslsslrpi kvdsqehkii lyenpnftgk
      121 kmeiidddvp sfhahgyqek vssvrvqsgt wvgyqypgyr glqyllekgd ykdssdfgap
      181 hpqvqsvrri rdmqwhqrga fhpsn
//
LOCUS       NP_004297                316 aa            linear   PRI 27-APR-2025
DEFINITION  annexin A13 isoform a [Homo sapiens].
ACCESSION   NP_004297
VERSION     NP_004297.2
DBSOURCE    REFSEQ: accession NM_004306.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maltseva,D.V., Raigorodskaya,M.P., Zgoda,V.G., Tonevitsky,E.A. and
            Knyazev,E.N.
  TITLE     Intracellular Transport of Ribosome-Inactivating Proteins Depends
            on Annexin 13
  JOURNAL   Dokl Biochem Biophys 494 (1), 219-221 (2020)
   PUBMED   33119820
  REMARK    GeneRIF: Intracellular Transport of Ribosome-Inactivating Proteins
            Depends on Annexin 13.
REFERENCE   2  (residues 1 to 316)
  AUTHORS   McCulloch,K.M., Yamakawa,I., Shifrin,D.A. Jr., McConnell,R.E.,
            Foegeding,N.J., Singh,P.K., Mao,S., Tyska,M.J. and Iverson,T.M.
  TITLE     An alternative N-terminal fold of the intestine-specific annexin
            A13a induces dimerization and regulates membrane-binding
  JOURNAL   J Biol Chem 294 (10), 3454-3463 (2019)
   PUBMED   30610115
  REMARK    GeneRIF: a mechanism for how the association of the ANX A13a
            isoform with the membrane is regulated
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Jiang,G., Wang,P., Wang,W., Li,W., Dai,L. and Chen,K.
  TITLE     Annexin A13 promotes tumor cell invasion in vitro and is associated
            with metastasis in human colorectal cancer
  JOURNAL   Oncotarget 8 (13), 21663-21673 (2017)
   PUBMED   28423508
  REMARK    GeneRIF: ANXA13 is associated with colorectal cancer cell invasion
            in vitro, and with lymph node metastasis and poor survival in
            colorectal cancer patients
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Fernandez-Lizarbe,S., Lecona,E., Santiago-Gomez,A., Olmo,N.,
            Lizarbe,M.A. and Turnay,J.
  TITLE     Structural and lipid-binding characterization of human annexin A13a
            reveals strong differences with its long A13b isoform
  JOURNAL   Biol Chem 398 (3), 359-371 (2017)
   PUBMED   27676605
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Benjachat,T., Tongyoo,P., Tantivitayakul,P., Somparn,P.,
            Hirankarn,N., Prom-On,S., Pisitkun,P., Leelahavanichkul,A.,
            Avihingsanon,Y. and Townamchai,N.
  TITLE     Biomarkers for Refractory Lupus Nephritis: A Microarray Study of
            Kidney Tissue
  JOURNAL   Int J Mol Sci 16 (6), 14276-14290 (2015)
   PUBMED   26110394
  REMARK    GeneRIF: High ANXA13 expression is associated with Refractory Lupus
            Nephritis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Iglesias,J.M., Morgan,R.O., Jenkins,N.A., Copeland,N.G.,
            Gilbert,D.J. and Fernandez,M.P.
  TITLE     Comparative genetics and evolution of annexin A13 as the founder
            gene of vertebrate annexins
  JOURNAL   Mol Biol Evol 19 (5), 608-618 (2002)
   PUBMED   11961095
  REMARK    GeneRIF: The unique, conserved aspects of annexin A13 primary
            structure, gene organization, and genetic maps identify it as the
            probable common ancestor of all vertebrate annexins.
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Noda,Y., Okada,Y., Saito,N., Setou,M., Xu,Y., Zhang,Z. and
            Hirokawa,N.
  TITLE     KIFC3, a microtubule minus end-directed motor for the apical
            transport of annexin XIIIb-associated Triton-insoluble membranes
  JOURNAL   J Cell Biol 155 (1), 77-88 (2001)
   PUBMED   11581287
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Plant,P.J., Lafont,F., Lecat,S., Verkade,P., Simons,K. and Rotin,D.
  TITLE     Apical membrane targeting of Nedd4 is mediated by an association of
            its C2 domain with annexin XIIIb
  JOURNAL   J Cell Biol 149 (7), 1473-1484 (2000)
   PUBMED   10871286
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Morgan,R.O., Bell,D.W., Testa,J.R. and Fernandez,M.P.
  TITLE     Genomic locations of ANX11 and ANX13 and the evolutionary genetics
            of human annexins
  JOURNAL   Genomics 48 (1), 100-110 (1998)
   PUBMED   9503022
REFERENCE   10 (residues 1 to 316)
  AUTHORS   Wice,B.M. and Gordon,J.I.
  TITLE     A strategy for isolation of cDNAs encoding proteins affecting human
            intestinal epithelial cell growth and differentiation:
            characterization of a novel gut-specific N-myristoylated annexin
  JOURNAL   J Cell Biol 116 (2), 405-422 (1992)
   PUBMED   1530946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011134.15 and AC135166.8.
            
            On Sep 7, 2004 this sequence version replaced NP_004297.1.
            
            Summary: This gene encodes a member of the annexin family. Members
            of this calcium-dependent phospholipid-binding protein family play
            a role in the regulation of cellular growth and in signal
            transduction pathways. The specific function of this gene has not
            yet been determined; however, it is associated with the plasma
            membrane of undifferentiated, proliferating endothelial cells and
            differentiated villus enterocytes. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript, and encodes the shorter isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z11502.1, SRR5189661.65698.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144835, SAMEA2152474
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000419625.6/ ENSP00000390809.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..316
                     /product="annexin A13 isoform a"
                     /note="annexin, intestine-specific; annexin XIII;
                     intestine-specific annexin; annexin-13"
                     /calculated_mol_wt=35284
     Region          14..85
                     /region_name="Annexin 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P27216.3)"
     Region          18..83
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          86..157
                     /region_name="Annexin 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P27216.3)"
     Region          90..155
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          169..241
                     /region_name="Annexin 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P27216.3)"
     Region          173..239
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          245..316
                     /region_name="Annexin 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P27216.3)"
     Region          249..314
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     CDS             1..316
                     /gene="ANXA13"
                     /gene_synonym="ANX13; ISA"
                     /coded_by="NM_004306.4:60..1010"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47917.1"
                     /db_xref="GeneID:312"
                     /db_xref="HGNC:HGNC:536"
                     /db_xref="MIM:602573"
ORIGIN      
        1 mgnrhakass pqgfdvdrda kklnkackgm gtneaaiiei lsgrtsderq qikqkykaty
       61 gkeleevlks elsgnfekta lalldrpsey aarqlqkamk glgtdesvli evlctrtnke
      121 iiaikeayqr lfdrslesdv kgdtsgnlkk ilvsllqanr negddvdkdl agqdakdlyd
      181 agegrwgtde lafnevlakr sykqlratfq ayqiligkdi eeaieeetsg dlqkayltlv
      241 rcaqdcedyf aerlyksmkg agtdeetlir ivvtraevdl qgikakfqek yqkslsdmvr
      301 sdtsgdfrkl lvallh
//
LOCUS       NP_055416                543 aa            linear   PRI 27-APR-2025
DEFINITION  EH domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_055416
VERSION     NP_055416.2
DBSOURCE    REFSEQ: accession NM_014601.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Li,W., Li,G. and Cao,L.
  TITLE     Circular RNA Eps15-homology domain-containing protein 2 induce
            resistance of renal cell carcinoma to sunitinib via
            microRNA-4731-5p/ABCF2 axis
  JOURNAL   Bioengineered 13 (4), 9729-9740 (2022)
   PUBMED   35412955
  REMARK    GeneRIF: Circular RNA Eps15-homology domain-containing protein 2
            induce resistance of renal cell carcinoma to sunitinib via
            microRNA-4731-5p/ABCF2 axis.
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Zhang,M.S., Cui,J.D., Lee,D., Yuen,V.W., Chiu,D.K., Goh,C.C.,
            Cheu,J.W., Tse,A.P., Bao,M.H., Wong,B.P.Y., Chen,C.Y., Wong,C.M.,
            Ng,I.O. and Wong,C.C.
  TITLE     Hypoxia-induced macropinocytosis represents a metabolic route for
            liver cancer
  JOURNAL   Nat Commun 13 (1), 954 (2022)
   PUBMED   35177645
  REMARK    GeneRIF: Hypoxia-induced macropinocytosis represents a metabolic
            route for liver cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Guan,C., Lu,C., Xiao,M. and Chen,W.
  TITLE     EHD2 Overexpression Suppresses the Proliferation, Migration, and
            Invasion in Human Colon Cancer
  JOURNAL   Cancer Invest 39 (4), 297-309 (2021)
   PUBMED   33356637
  REMARK    GeneRIF: EHD2 Overexpression Suppresses the Proliferation,
            Migration, and Invasion in Human Colon Cancer.
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Fan,H., Liu,T., Tian,H. and Zhang,S.
  TITLE     TUSC8 inhibits the development of osteosarcoma by sponging
            miR-197-3p and targeting EHD2
  JOURNAL   Int J Mol Med 46 (4), 1311-1320 (2020)
   PUBMED   32945345
  REMARK    GeneRIF: TUSC8 inhibits the development of osteosarcoma by sponging
            miR1973p and targeting EHD2.
            Erratum:[Int J Mol Med. 2021 Apr;47(4):58. doi:
            10.3892/ijmm.2021.4891. PMID: 33655323]
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Matthaeus,C., Lahmann,I., Kunz,S., Jonas,W., Melo,A.A., Lehmann,M.,
            Larsson,E., Lundmark,R., Kern,M., Bluher,M., Olschowski,H.,
            Kompa,J., Brugger,B., Muller,D.N., Haucke,V., Schurmann,A.,
            Birchmeier,C. and Daumke,O.
  TITLE     EHD2-mediated restriction of caveolar dynamics regulates cellular
            fatty acid uptake
  JOURNAL   Proc Natl Acad Sci U S A 117 (13), 7471-7481 (2020)
   PUBMED   32170013
  REMARK    GeneRIF: EHD2-mediated restriction of caveolar dynamics regulates
            cellular fatty acid uptake.
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Aboulaich,N., Vainonen,J.P., Stralfors,P. and Vener,A.V.
  TITLE     Vectorial proteomics reveal targeting, phosphorylation and specific
            fragmentation of polymerase I and transcript release factor (PTRF)
            at the surface of caveolae in human adipocytes
  JOURNAL   Biochem J 383 (Pt 2), 237-248 (2004)
   PUBMED   15242332
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Park,S.Y., Ha,B.G., Choi,G.H., Ryu,J., Kim,B., Jung,C.Y. and Lee,W.
  TITLE     EHD2 interacts with the insulin-responsive glucose transporter
            (GLUT4) in rat adipocytes and may participate in insulin-induced
            GLUT4 recruitment
  JOURNAL   Biochemistry 43 (23), 7552-7562 (2004)
   PUBMED   15182197
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Naslavsky,N., Boehm,M., Backlund,P.S. Jr. and Caplan,S.
  TITLE     Rabenosyn-5 and EHD1 interact and sequentially regulate protein
            recycling to the plasma membrane
  JOURNAL   Mol Biol Cell 15 (5), 2410-2422 (2004)
   PUBMED   15020713
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Guilherme,A., Soriano,N.A., Bose,S., Holik,J., Bose,A.,
            Pomerleau,D.P., Furcinitti,P., Leszyk,J., Corvera,S. and Czech,M.P.
  TITLE     EHD2 and the novel EH domain binding protein EHBP1 couple
            endocytosis to the actin cytoskeleton
  JOURNAL   J Biol Chem 279 (11), 10593-10605 (2004)
   PUBMED   14676205
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Pohl,U., Smith,J.S., Tachibana,I., Ueki,K., Lee,H.K., Ramaswamy,S.,
            Wu,Q., Mohrenweiser,H.W., Jenkins,R.B. and Louis,D.N.
  TITLE     EHD2, EHD3, and EHD4 encode novel members of a highly conserved
            family of EH domain-containing proteins
  JOURNAL   Genomics 63 (2), 255-262 (2000)
   PUBMED   10673336
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK315548.1, DB260808.1,
            BC014445.1 and BG677716.1.
            
            On Jun 10, 2002 this sequence version replaced NP_055416.1.
            
            Summary: This gene encodes a member of the EH domain-containing
            protein family. These proteins are characterized by a C-terminal
            EF-hand domain, a nucleotide-binding consensus site at the N
            terminus and a bipartite nuclear localization signal. The encoded
            protein interacts with the actin cytoskeleton through an N-terminal
            domain and also binds to an EH domain-binding protein through the
            C-terminal EH domain. This interaction appears to connect
            clathrin-dependent endocytosis to actin, suggesting that this gene
            product participates in the endocytic pathway. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014445.1, SRR1660809.52005.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263277.8/ ENSP00000263277.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..543
                     /product="EH domain-containing protein 2"
                     /note="PAST homolog 2"
                     /calculated_mol_wt=61031
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4V8H8; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Region          24..56
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Region          60..300
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Region          65..72
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Site            65..72
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(70..73,153,220,222,256..258)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Region          91..92
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Site            94
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            98..100
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Region          120..122
                     /region_name="KPF loop, caveolar targeting.
                     /evidence=ECO:0000269|PubMed:22323287"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Region          153..156
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Site            153..156
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(155..156,183..184)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Region          219..222
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Site            219..222
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Region          243
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Site            256..258
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     Region          288..394
                     /region_name="DUF5600"
                     /note="Domain of unknown function (DUF5600); pfam18150"
                     /db_xref="CDD:465667"
     Region          320..340
                     /region_name="Mediates membrane-binding.
                     /evidence=ECO:0000250|UniProtKB:Q8BH64"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Region          443..536
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4V8H8; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN4.2)"
     Region          523..543
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN4.2)"
     CDS             1..543
                     /gene="EHD2"
                     /gene_synonym="PAST2"
                     /coded_by="NM_014601.4:173..1804"
                     /db_xref="CCDS:CCDS12704.1"
                     /db_xref="GeneID:30846"
                     /db_xref="HGNC:HGNC:3243"
                     /db_xref="MIM:605890"
ORIGIN      
        1 mfswlkrgga rgqqpeairt vtsalkelyr tkllpleehy rfgafhspal edadfdgkpm
       61 vlvagqystg ktsfiqylle qevpgsrvgp epttdcfvav mhgdtegtvp gnalvvdpdk
      121 pfrklnpfgn tflnrfmcaq lpnqvlesis iidtpgilsg akqrvsrgyd fpavlrwfae
      181 rvdliillfd ahkleisdef seaigalrgh edkirvvlnk admvetqqlm rvygalmwal
      241 gkvvgtpevl rvyigsfwsq pllvpdnrrl feleeqdlfr diqglprhaa lrklndlvkr
      301 arlvrvhayi isylkkemps vfgkenkkkq lilklpvifa kiqlehhisp gdfpdcqkmq
      361 ellmahdftk fhslkpklle aldemlthdi aklmpllrqe elestevgvq ggafegthmg
      421 pfvergpdea medgeegsdd eaewvvtkdk skydeifynl apadgklsgs kaktwmvgtk
      481 lpnsvlgriw klsdvdrdgm lddeefalas hlieaklegh glpanlprrl vppskrrhkg
      541 sae
//
LOCUS       NP_060259                833 aa            linear   PRI 27-APR-2025
DEFINITION  semaphorin-4C precursor [Homo sapiens].
ACCESSION   NP_060259
VERSION     NP_060259.4
DBSOURCE    REFSEQ: accession NM_017789.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Liu,H., Ye,H. and Li,X.
  TITLE     Effect of microrna-138 on epithelial-Mesenchymal transition and
            invasion of breast cancer cells by targeting semaphorin 4C
  JOURNAL   Bioengineered 12 (2), 10117-10125 (2021)
   PUBMED   34747314
  REMARK    GeneRIF: Effect of microrna-138 on epithelial-Mesenchymal
            transition and invasion of breast cancer cells by targeting
            semaphorin 4C.
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Wang,Y., Liu,J., Li,J., Li,H., Li,X., Qiao,L., Yang,J., Fang,T.,
            Chen,S., Ma,J., Wan,J., Li,X., Zhang,L., Xia,Y., Wu,Y., Xu,T.,
            Shao,J., Feng,Y., Kamel,I.R., Yang,Q., Li,Z. and Gao,Q.
  TITLE     Serum semaphorin4C as an auxiliary diagnostic biomarker for breast
            cancer
  JOURNAL   Clin Transl Med 11 (8), e480 (2021)
   PUBMED   34459126
  REMARK    GeneRIF: Serum semaphorin4C as an auxiliary diagnostic biomarker
            for breast cancer.
REFERENCE   4  (residues 1 to 833)
  AUTHORS   Hou,Y., Wang,W., Zeng,Z., Gan,W., Lv,S., Li,T., Yan,Z., Zhang,R.
            and Yang,M.
  TITLE     High SEMA4C expression promotes the epithelial-mesenchymal
            transition and predicts poor prognosis in colorectal carcinoma
  JOURNAL   Aging (Albany NY) 12 (21), 21992-22018 (2020)
   PUBMED   33177246
  REMARK    GeneRIF: High SEMA4C expression promotes the epithelial-mesenchymal
            transition and predicts poor prognosis in colorectal carcinoma.
REFERENCE   5  (residues 1 to 833)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 833)
  AUTHORS   Inagaki,S., Ohoka,Y., Sugimoto,H., Fujioka,S., Amazaki,M.,
            Kurinami,H., Miyazaki,N., Tohyama,M. and Furuyama,T.
  TITLE     Sema4c, a transmembrane semaphorin, interacts with a post-synaptic
            density protein, PSD-95
  JOURNAL   J Biol Chem 276 (12), 9174-9181 (2001)
   PUBMED   11134026
REFERENCE   7  (residues 1 to 833)
  AUTHORS   Ohoka,Y., Hirotani,M., Sugimoto,H., Fujioka,S., Furuyama,T. and
            Inagaki,S.
  TITLE     Semaphorin 4C, a transmembrane semaphorin, [corrected] associates
            with a neurite-outgrowth-related protein, SFAP75
  JOURNAL   Biochem Biophys Res Commun 280 (1), 237-243 (2001)
   PUBMED   11162505
  REMARK    Erratum:[Biochem Biophys Res Commun 2001 Feb 16;281(1):266]
REFERENCE   8  (residues 1 to 833)
  AUTHORS   Wang,L.H., Kalb,R.G. and Strittmatter,S.M.
  TITLE     A PDZ protein regulates the distribution of the transmembrane
            semaphorin, M-SemF
  JOURNAL   J Biol Chem 274 (20), 14137-14146 (1999)
   PUBMED   10318831
REFERENCE   9  (residues 1 to 833)
  AUTHORS   Simmons,A.D., Puschel,A.W., McPherson,J.D., Overhauser,J. and
            Lovett,M.
  TITLE     Molecular cloning and mapping of human semaphorin F from the
            Cri-du-chat candidate interval
  JOURNAL   Biochem Biophys Res Commun 242 (3), 685-691 (1998)
   PUBMED   9464278
REFERENCE   10 (residues 1 to 833)
  AUTHORS   Inagaki,S., Furuyama,T. and Iwahashi,Y.
  TITLE     Identification of a member of mouse semaphorin family
  JOURNAL   FEBS Lett 370 (3), 269-272 (1995)
   PUBMED   7656991
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092636.3, BI518922.1, BC109104.1 and BC017476.1.
            
            On Sep 20, 2007 this sequence version replaced NP_060259.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358842.1, BC109103.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305476.10/ ENSP00000306844.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..833
                     /product="semaphorin-4C precursor"
                     /note="M-Sema F; sema domain, immunoglobulin domain (Ig),
                     transmembrane domain (TM) and short cytoplasmic domain,
                     (semaphorin) 4C"
                     /calculated_mol_wt=90423
     sig_peptide     1..20
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C4.2)"
                     /calculated_mol_wt=2219
     mat_peptide     21..833
                     /product="Semaphorin-4C. /id=PRO_0000032325"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C4.2)"
                     /calculated_mol_wt=90423
     Region          42..498
                     /region_name="Sema_4C"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4C (Sema4C); cd11258"
                     /db_xref="CDD:200519"
     Region          46..489
                     /region_name="Dominant negative effect on myogenic
                     differentiation. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Site            order(101..103,161,182,184..185,187,202,205,207,212,244,
                     268..272,274,352..353,388,392,395)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200519"
     Site            106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Site            order(245..246,248,251..253,287,290..292,294,296,319..321,
                     325..326,401,416)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200519"
     Site            310
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Site            419
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Region          499..>528
                     /region_name="PSI"
                     /note="domain found in Plexins, Semaphorins and Integrins;
                     smart00423"
                     /db_xref="CDD:214655"
     Site            522
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Region          563..647
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            564
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Region          573..577
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409456"
     Region          585..589
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409456"
     Region          610..614
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409456"
     Region          624..629
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409456"
     Region          641..644
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409456"
     Site            664..684
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Region          748..807
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Region          814..833
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C4.2)"
     Region          830..833
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C4.2)"
     CDS             1..833
                     /gene="SEMA4C"
                     /gene_synonym="M-SEMA-F; SEMACL1; SEMAF; SEMAI"
                     /coded_by="NM_017789.5:243..2744"
                     /db_xref="CCDS:CCDS2029.1"
                     /db_xref="GeneID:54910"
                     /db_xref="HGNC:HGNC:10731"
                     /db_xref="MIM:604462"
ORIGIN      
        1 maphwavwll aarlwglgig aevwwnlvpr ktvssgelat vvrrfsqtgi qdfltltlte
       61 ptgllyvgar ealfafsmea lelqgaiswe apvekkteci qkgknnqtec fnfirflqpy
      121 nashlyvcgt yafqpkctyv nmltftlehg efedgkgkcp ydpakghagl lvdgelysat
      181 lnnflgtepi ilrnmgphhs mkteylafwl nephfvgsay vpesvgsftg dddkvyfffr
      241 eravesdcya eqvvarvarv ckgdmggart lqrkwttflk arlacsapnw qlyfnqlqam
      301 htlqdtswhn ttffgvfqaq wgdmylsaic eyqleeiqrv fegpykeyhe eaqkwdrytd
      361 pvpsprpgsc innwhrrhgy tsslelpdni lnfvkkhplm eeqvgprwsr pllvkkgtnf
      421 thlvadrvtg ldgatytvlf igtgdgwllk avslgpwvhl ieelqlfdqe pmrslvlsqs
      481 kkllfagsrs qlvqlpvadc mkyrscadcv lardpycaws vntsrcvavg ghsgslliqh
      541 vmtsdtsgic nlrgskkvrp tpknitvvag tdlvlpchls snlaharwtf ggrdlpaeqp
      601 gsflydarlq alvvmaaqpr hagayhcfse eqgarlaaeg ylvavvagps vtlearaple
      661 nlglvwlavv algavclvll llvlslrrrl reelekgaka tertlvyple lpkeptsppf
      721 rpcpepdekl wdpvgyyysd gslkivpgha rcqpgggpps pppgipgqpl psptrlhlgg
      781 grnsnangyv rlqlggedrg glghplpela delrrklqqr qplpdsnpee ssv
//
LOCUS       NP_055029                288 aa            linear   PRI 27-APR-2025
DEFINITION  inositol monophosphatase 2 [Homo sapiens].
ACCESSION   NP_055029
VERSION     NP_055029.1
DBSOURCE    REFSEQ: accession NM_014214.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Lei,X., Liao,R., Chen,X., Wang,Z., Cao,Q., Bai,L., Ma,C., Deng,X.,
            Ma,Y., Wu,X., Li,J., Dai,Z. and Dong,C.
  TITLE     IMPA2 promotes basal-like breast cancer aggressiveness by a
            MYC-mediated positive feedback loop
  JOURNAL   Cancer Lett 582, 216527 (2024)
   PUBMED   38048842
  REMARK    GeneRIF: IMPA2 promotes basal-like breast cancer aggressiveness by
            a MYC-mediated positive feedback loop.
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Zhang,K., Liu,L., Wang,M., Yang,M., Li,X., Xia,X., Tian,J., Tan,S.
            and Luo,L.
  TITLE     A novel function of IMPA2, plays a tumor-promoting role in cervical
            cancer
  JOURNAL   Cell Death Dis 11 (5), 371 (2020)
   PUBMED   32409648
  REMARK    GeneRIF: A novel function of IMPA2, plays a tumor-promoting role in
            cervical cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Lin,Y.F., Chou,J.L., Chang,J.S., Chiu,I.J., Chiu,H.W. and Lin,Y.F.
  TITLE     Dysregulation of the miR-25-IMPA2 axis promotes metastatic
            progression in clear cell renal cell carcinoma
  JOURNAL   EBioMedicine 45, 220-230 (2019)
   PUBMED   31202813
  REMARK    GeneRIF: We conclude that miR-25-mediated IMPA2 downregulation
            constitutes a novel signature for cancer metastasis and poor
            outcomes in clear cell renal cell carcinoma (ccRCC). We further
            postulate that the therapeutic targeting of miR-25 can be useful
            for preventing the metastatic progression of ccRCC associated with
            IMPA2 downregulation.
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Arai,R., Ito,K., Ohnishi,T., Ohba,H., Akasaka,R., Bessho,Y.,
            Hanawa-Suetsugu,K., Yoshikawa,T., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of human myo-inositol monophosphatase 2, the
            product of the putative susceptibility gene for bipolar disorder,
            schizophrenia, and febrile seizures
  JOURNAL   Proteins 67 (3), 732-742 (2007)
   PUBMED   17340635
  REMARK    GeneRIF: The crystal structures of human IMPA2 are useful for
            understanding the effect of nonsynonymous polymorphism reported in
            IMPA2, and will contribute to further functional analyses of IMPA2.
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Yoshikawa,T., Kikuchi,M., Saito,K., Watanabe,A., Yamada,K.,
            Shibuya,H., Nankai,M., Kurumaji,A., Hattori,E., Ishiguro,H.,
            Shimizu,H., Okubo,Y., Toru,M. and Detera-Wadleigh,S.D.
  TITLE     Evidence for association of the myo-inositol monophosphatase 2
            (IMPA2) gene with schizophrenia in Japanese samples
  JOURNAL   Mol Psychiatry 6 (2), 202-210 (2001)
   PUBMED   11317223
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Sjoholt,G., Gulbrandsen,A.K., Lovlie,R., Berle,J.O., Molven,A. and
            Steen,V.M.
  TITLE     A human myo-inositol monophosphatase gene (IMPA2) localized in a
            putative susceptibility region for bipolar disorder on chromosome
            18p11.2: genomic structure and polymorphism screening in
            manic-depressive patients
  JOURNAL   Mol Psychiatry 5 (2), 172-180 (2000)
   PUBMED   10822345
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Yoshikawa,T., Padigaru,M., Karkera,J.D., Sharma,M.,
            Berrettini,W.H., Esterling,L.E. and Detera-Wadleigh,S.D.
  TITLE     Genomic structure and novel variants of myo-inositol
            monophosphatase 2 (IMPA2)
  JOURNAL   Mol Psychiatry 5 (2), 165-171 (2000)
   PUBMED   10822344
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Yoshikawa,T., Turner,G., Esterling,L.E., Sanders,A.R. and
            Detera-Wadleigh,S.D.
  TITLE     A novel human myo-inositol monophosphatase gene, IMP.18p, maps to a
            susceptibility region for bipolar disorder
  JOURNAL   Mol Psychiatry 2 (5), 393-397 (1997)
   PUBMED   9322233
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001269.4 and BC017176.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This locus encodes an inositol monophosphatase. The
            encoded protein catalyzes the dephosphoylration of inositol
            monophosphate and plays an important role in phosphatidylinositol
            signaling. This locus may be associated with susceptibility to
            bipolar disorder. [provided by RefSeq, Jan 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.98649.1, AF014398.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269159.8/ ENSP00000269159.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..288
                     /product="inositol monophosphatase 2"
                     /EC_number="3.1.3.25"
                     /note="inosine monophosphatase 2; IMP 2; IMPase 2;
                     myo-inositol monophosphatase A2; inositol(myo)-1(or
                     4)-monophosphatase 2; myo-inositol monophosphatase 2"
                     /calculated_mol_wt=31190
     Region          19..265
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(47,52,58,81..82,101..106,230..231)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(51,53,107..108,110..115,167..169,171,173..174,
                     183..184,187,190..191,194,199..205,213,217..220)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
     CDS             1..288
                     /gene="IMPA2"
                     /coded_by="NM_014214.3:164..1030"
                     /db_xref="CCDS:CCDS11855.1"
                     /db_xref="GeneID:3613"
                     /db_xref="HGNC:HGNC:6051"
                     /db_xref="MIM:605922"
ORIGIN      
        1 mkpsgedqaa laagpweecf qaavqlalra gqiirkalte ekrvstktsa adlvtetdhl
       61 vedliiselr erfpshrfia eeaaasgakc vlthsptwii dpidgtcnfv hrfptvavsi
      121 gfavrqelef gviyhcteer lytgrrgrga fcngqrlrvs getdlskalv lteigpkrdp
      181 atlklflsnm erllhakahg vrvigsstla lchlasgaad ayyqfglhcw dlaaatviir
      241 eaggividts ggpldlmacr vvaastrema mliaqalqti nygrddek
//
LOCUS       NP_001353335              96 aa            linear   PRI 27-APR-2025
DEFINITION  protein S100-A2 isoform 2 [Homo sapiens].
ACCESSION   NP_001353335
VERSION     NP_001353335.1
DBSOURCE    REFSEQ: accession NM_001366406.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Zeng,T., Ren,W., Zeng,H., Wang,D., Wu,X. and Xu,G.
  TITLE     TFAP2A Activates S100A2 to Mediate Glutamine Metabolism and Promote
            Lung Adenocarcinoma Metastasis
  JOURNAL   Clin Respir J 18 (8), e13825 (2024)
   PUBMED   39187936
  REMARK    GeneRIF: TFAP2A Activates S100A2 to Mediate Glutamine Metabolism
            and Promote Lung Adenocarcinoma Metastasis.
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Yang,J., Wan,S., Zhao,M., Cai,H., Gao,Y. and Wang,H.
  TITLE     Multi-omics Analysis Identifies Hypoxia Subtypes and S100A2 as an
            Immunosuppressive Factor in Cervical Cancer
  JOURNAL   Reprod Sci 31 (1), 107-121 (2024)
   PUBMED   37648942
  REMARK    GeneRIF: Multi-omics Analysis Identifies Hypoxia Subtypes and
            S100A2 as an Immunosuppressive Factor in Cervical Cancer.
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Zhang,J., Wang,Z., Liang,Z., Jin,C., Shi,Y., Fan,M., Hu,X. and
            Wan,Y.
  TITLE     NFIC1 inhibits the migration and invasion of MDA-MB-231 cells
            through S100A2-mediated inactivation of MEK/ERK pathway
  JOURNAL   Arch Biochem Biophys 734, 109497 (2023)
   PUBMED   36574914
  REMARK    GeneRIF: NFIC1 inhibits the migration and invasion of MDA-MB-231
            cells through S100A2-mediated inactivation of MEK/ERK pathway.
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Yan,J., Huang,Y.J., Huang,Q.Y., Liu,P.X. and Wang,C.S.
  TITLE     Transcriptional activation of S100A2 expression by HIF-1alpha via
            binding to the hypomethylated hypoxia response elements in HCC
            cells
  JOURNAL   Mol Carcinog 61 (5), 494-507 (2022)
   PUBMED   35107180
  REMARK    GeneRIF: Transcriptional activation of S100A2 expression by
            HIF-1alpha via binding to the hypomethylated hypoxia response
            elements in HCC cells.
REFERENCE   5  (residues 1 to 96)
  AUTHORS   Zhang,Q., Xia,T., Qi,C., Du,J. and Ye,C.
  TITLE     High expression of S100A2 predicts poor prognosis in patients with
            endometrial carcinoma
  JOURNAL   BMC Cancer 22 (1), 77 (2022)
   PUBMED   35042454
  REMARK    GeneRIF: High expression of S100A2 predicts poor prognosis in
            patients with endometrial carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 96)
  AUTHORS   Schafer,B.W. and Heizmann,C.W.
  TITLE     The S100 family of EF-hand calcium-binding proteins: functions and
            pathology
  JOURNAL   Trends Biochem Sci 21 (4), 134-140 (1996)
   PUBMED   8701470
  REMARK    Review article
REFERENCE   7  (residues 1 to 96)
  AUTHORS   Schafer,B.W., Wicki,R., Engelkamp,D., Mattei,M.G. and Heizmann,C.W.
  TITLE     Isolation of a YAC clone covering a cluster of nine S100 genes on
            human chromosome 1q21: rationale for a new nomenclature of the S100
            calcium-binding protein family
  JOURNAL   Genomics 25 (3), 638-643 (1995)
   PUBMED   7759097
REFERENCE   8  (residues 1 to 96)
  AUTHORS   Engelkamp,D., Schafer,B.W., Mattei,M.G., Erne,P. and Heizmann,C.W.
  TITLE     Six S100 genes are clustered on human chromosome 1q21:
            identification of two genes coding for the two previously
            unreported calcium-binding proteins S100D and S100E
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6547-6551 (1993)
   PUBMED   8341667
REFERENCE   9  (residues 1 to 96)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 96)
  AUTHORS   Lee,S.W., Tomasetto,C., Swisshelm,K., Keyomarsi,K. and Sager,R.
  TITLE     Down-regulation of a member of the S100 gene family in mammary
            carcinoma cells and reexpression by azadeoxycytidine treatment
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2504-2508 (1992)
   PUBMED   1372446
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX470102.12.
            
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21. This protein may have a
            tumor suppressor function. Chromosomal rearrangements and altered
            expression of this gene have been implicated in breast cancer.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.229836.1,
                                           DRR138524.576228.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..96
                     /product="protein S100-A2 isoform 2"
                     /note="protein S100-A2"
                     /calculated_mol_wt=10970
     Region          4..>56
                     /region_name="S-100"
                     /note="S-100 domain, which represents the largest family
                     within the superfamily of proteins carrying the Ca-binding
                     EF-hand motif. Note that this S-100 hierarchy contains
                     only S-100 EF-hand domains, other EF-hands have been
                     modeled separately. S100 proteins are...; cd00213"
                     /db_xref="CDD:238131"
     CDS             1..96
                     /gene="S100A2"
                     /gene_synonym="CAN19; S100L"
                     /coded_by="NM_001366406.1:11..301"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS91059.1"
                     /db_xref="GeneID:6273"
                     /db_xref="HGNC:HGNC:10492"
                     /db_xref="MIM:176993"
ORIGIN      
        1 mmcssleqal avlvttfhky scqegdkfkl skgemkellh kelpsfvghs repcavrafr
       61 vhlfnpvigd lrnqspegks dcpkitqhwr kwmrrg
//
LOCUS       NP_848600                368 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 26 [Homo sapiens].
ACCESSION   NP_848600
VERSION     NP_848600.2
DBSOURCE    REFSEQ: accession NM_178505.8
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Han,G., Zhou,S., Shen,J., Yang,Y., Bian,X., Li,Y., Ling,R.,
            Liang,R. and Tao,M.
  TITLE     The role of TMEM26 in disrupting tight junctions and activating
            NF-kappaB signaling to promote epithelial-mesenchymal transition in
            esophageal squamous cell carcinoma
  JOURNAL   Clinics (Sao Paulo) 78, 100276 (2023)
   PUBMED   37611445
  REMARK    GeneRIF: The role of TMEM26 in disrupting tight junctions and
            activating NF-kappaB signaling to promote epithelial-mesenchymal
            transition in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Finlin,B.S., Memetimin,H., Confides,A.L., Kasza,I., Zhu,B.,
            Vekaria,H.J., Harfmann,B., Jones,K.A., Johnson,Z.R., Westgate,P.M.,
            Alexander,C.M., Sullivan,P.G., Dupont-Versteegden,E.E. and
            Kern,P.A.
  TITLE     Human adipose beiging in response to cold and mirabegron
  JOURNAL   JCI Insight 3 (15), 121510 (2018)
   PUBMED   30089732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Nass,N., Dittmer,A., Hellwig,V., Lange,T., Beyer,J.M., Leyh,B.,
            Ignatov,A., Weibetaenborn,C., Kirkegaard,T., Lykkesfeldt,A.E.,
            Kalinski,T. and Dittmer,J.
  TITLE     Expression of transmembrane protein 26 (TMEM26) in breast cancer
            and its association with drug response
  JOURNAL   Oncotarget 7 (25), 38408-38426 (2016)
   PUBMED   27224909
  REMARK    GeneRIF: High TMEM26 expression was found to be associated with a
            higher risk of recurrence.
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Hankir,M.K., Bronisch,F., Hintschich,C., Krugel,U., Seyfried,F. and
            Fenske,W.K.
  TITLE     Differential effects of Roux-en-Y gastric bypass surgery on brown
            and beige adipose tissue thermogenesis
  JOURNAL   Metabolism 64 (10), 1240-1249 (2015)
   PUBMED   26211711
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Rockstroh,D., Landgraf,K., Wagner,I.V., Gesing,J., Tauscher,R.,
            Lakowa,N., Kiess,W., Buhligen,U., Wojan,M., Till,H., Bluher,M. and
            Korner,A.
  TITLE     Direct evidence of brown adipocytes in different fat depots in
            children
  JOURNAL   PLoS One 10 (2), e0117841 (2015)
   PUBMED   25706927
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Okla,M., Ha,J.H., Temel,R.E. and Chung,S.
  TITLE     BMP7 drives human adipogenic stem cells into metabolically active
            beige adipocytes
  JOURNAL   Lipids 50 (2), 111-120 (2015)
   PUBMED   25534037
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Jespersen,N.Z., Larsen,T.J., Peijs,L., Daugaard,S., Homoe,P.,
            Loft,A., de Jong,J., Mathur,N., Cannon,B., Nedergaard,J.,
            Pedersen,B.K., Moller,K. and Scheele,C.
  TITLE     A classical brown adipose tissue mRNA signature partly overlaps
            with brite in the supraclavicular region of adult humans
  JOURNAL   Cell Metab 17 (5), 798-805 (2013)
   PUBMED   23663743
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Hansel,N.N., Ruczinski,I., Rafaels,N., Sin,D.D., Daley,D.,
            Malinina,A., Huang,L., Sandford,A., Murray,T., Kim,Y., Vergara,C.,
            Heckbert,S.R., Psaty,B.M., Li,G., Elliott,W.M., Aminuddin,F.,
            Dupuis,J., O'Connor,G.T., Doheny,K., Scott,A.F., Boezen,H.M.,
            Postma,D.S., Smolonska,J., Zanen,P., Mohamed Hoesein,F.A., de
            Koning,H.J., Crystal,R.G., Tanaka,T., Ferrucci,L., Silverman,E.,
            Wan,E., Vestbo,J., Lomas,D.A., Connett,J., Wise,R.A., Neptune,E.R.,
            Mathias,R.A., Pare,P.D., Beaty,T.H. and Barnes,K.C.
  TITLE     Genome-wide study identifies two loci associated with lung function
            decline in mild to moderate COPD
  JOURNAL   Hum Genet 132 (1), 79-90 (2013)
   PUBMED   22986903
  REMARK    GeneRIF: show novel expression of genes near regions of
            significantly associated SNPS, including TMEM26 and FOXA1 in airway
            epithelium and lung parenchyma, and ANK3 in alveolar macrophages in
            COPD
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Zhao,Y., Guo,S., Sun,J., Huang,Z., Zhu,T., Zhang,H., Gu,J., He,Y.,
            Wang,W., Ma,K., Wang,J. and Yu,J.
  TITLE     Methylcap-seq reveals novel DNA methylation markers for the
            diagnosis and recurrence prediction of bladder cancer in a Chinese
            population
  JOURNAL   PLoS One 7 (4), e35175 (2012)
   PUBMED   22529986
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Town,L., McGlinn,E., Davidson,T.L., Browne,C.M.,
            Chawengsaksophak,K., Koopman,P., Richman,J.M. and Wicking,C.
  TITLE     Tmem26 is dynamically expressed during palate and limb development
            but is not required for embryonic survival
  JOURNAL   PLoS One 6 (9), e25228 (2011)
   PUBMED   21980401
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CR749606.1, AC068892.7 and
            AW510476.1.
            
            On Jul 11, 2004 this sequence version replaced NP_848600.1.
            
            Summary: This gene encodes a protein containing multiple
            transmembrane helices. It is a selective surface protein marker of
            brite/beige adipocytes, which may coexist with classical brown
            adipocytes in brown adipose tissue. Alternative splicing of this
            gene results in multiple transcript variants. [provided by RefSeq,
            Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the supported protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749606.1, SRR1803612.110231.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399298.8/ ENSP00000382237.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.2"
     Protein         1..368
                     /product="transmembrane protein 26"
                     /calculated_mol_wt=41541
     Region          3..303
                     /region_name="Tmem26"
                     /note="Transmembrane protein 26; pfam09772"
                     /db_xref="CDD:430813"
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZUK4.1)"
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZUK4.1)"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZUK4.1)"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q6ZUK4.1)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZUK4.1)"
     Site            177..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZUK4.1)"
     Site            208..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZUK4.1)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZUK4.1)"
     Site            281..301
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZUK4.1)"
     Region          324..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZUK4.1)"
     CDS             1..368
                     /gene="TMEM26"
                     /coded_by="NM_178505.8:301..1407"
                     /db_xref="CCDS:CCDS41530.1"
                     /db_xref="GeneID:219623"
                     /db_xref="HGNC:HGNC:28550"
                     /db_xref="MIM:617803"
ORIGIN      
        1 meglvflnal atrllfllhs lvgvwrvtev kkeprywlla llnlllflet altlkfkrgr
       61 gykwfspaif lylisivpsl wllelhhetq ycsiqaegts qntsrkedfn qtltsneqts
      121 raddlietak vfvnnlstvc ekvwtlglhq tfllmliigr wllpigggit rdqlsqlllm
      181 fvgtaadile ftsetleeqn vrnspalvya ilviwtwsml qfpldlavqn vvcpvsvter
      241 gfpslffcqy sadlwnigis vfiqdgpflv vrlilmtyfk vinqmlvffa aknflvvvlq
      301 lyrlvvlala vraslrsqse glkgehgcra qtsesgpsqr dwqneskegl aiplrgspvt
      361 sddshhtp
//
LOCUS       NP_082377                269 aa            linear   ROD 27-APR-2025
DEFINITION  jmjC domain-containing protein 8 precursor [Mus musculus].
ACCESSION   NP_082377
VERSION     NP_082377.3
DBSOURCE    REFSEQ: accession NM_028101.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Li,Y., Zhang,Y., Zhou,Z., Yi,L., Ji,F., Zhang,K., Zhang,Y. and
            Xu,H.
  TITLE     JMJD8 regulates neuropathic pain by affecting spinal cord astrocyte
            differentiation
  JOURNAL   Neurosci Lett 809, 137307 (2023)
   PUBMED   37211325
  REMARK    GeneRIF: JMJD8 regulates neuropathic pain by affecting spinal cord
            astrocyte differentiation.
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Yi,J., Wang,L., Du,J., Wang,M., Shen,H., Liu,Z., Qin,Y., Liu,J.,
            Hu,G., Xiao,R., Ding,J., Chen,X., Wang,H., Huang,H., Ouyang,G. and
            Liu,W.
  TITLE     ER-localized JmjC domain-containing protein JMJD8 targets STING to
            promote immune evasion and tumor growth in breast cancer
  JOURNAL   Dev Cell 58 (9), 760-778 (2023)
   PUBMED   37054705
  REMARK    GeneRIF: ER-localized JmjC domain-containing protein JMJD8 targets
            STING to promote immune evasion and tumor growth in breast cancer.
REFERENCE   4  (residues 1 to 269)
  AUTHORS   You,D., Chul Jung,B., Villivalam,S.D., Lim,H.W. and Kang,S.
  TITLE     JMJD8 is a Novel Molecular Nexus Between Adipocyte-Intrinsic
            Inflammation and Insulin Resistance
  JOURNAL   Diabetes (2021) In press
   PUBMED   34957483
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Zhang,F., Zhao,X., Jiang,R., Wang,Y., Wang,X., Gu,Y., Xu,L., Ye,J.,
            Chen,C.D., Guo,S., Zhang,D. and Zhao,D.
  TITLE     Identification of Jmjd3 as an Essential Epigenetic Regulator of Hox
            Gene Temporal Collinear Activation for Body Axial Patterning in
            Mice
  JOURNAL   Front Cell Dev Biol 9, 642931 (2021)
   PUBMED   34368113
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Sundberg,J.P., Dadras,S.S., Silva,K.A., Kennedy,V.E., Garland,G.,
            Murray,S.A., Sundberg,B.A., Schofield,P.N. and Pratt,C.H.
  TITLE     Systematic screening for skin, hair, and nail abnormalities in a
            large-scale knockout mouse program
  JOURNAL   PLoS One 12 (7), e0180682 (2017)
   PUBMED   28700664
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Boeckel,J.N., Derlet,A., Glaser,S.F., Luczak,A., Lucas,T.,
            Heumuller,A.W., Kruger,M., Zehendner,C.M., Kaluza,D.,
            Doddaballapur,A., Ohtani,K., Treguer,K. and Dimmeler,S.
  TITLE     JMJD8 Regulates Angiogenic Sprouting and Cellular Metabolism by
            Interacting With Pyruvate Kinase M2 in Endothelial Cells
  JOURNAL   Arterioscler Thromb Vasc Biol 36 (7), 1425-1433 (2016)
   PUBMED   27199445
  REMARK    GeneRIF: Jmjd8 is upregulated during endothelial differentiation
            and regulates endothelial sprouting and metabolism by interacting
            with pyruvate kinase M2.
REFERENCE   8  (residues 1 to 269)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK155810.1 and BE982271.1.
            
            On Sep 12, 2018 this sequence version replaced NP_082377.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK155810.1, SRR7345562.4877875.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 12.92 cM"
     Protein         1..269
                     /product="jmjC domain-containing protein 8 precursor"
                     /note="jmjC domain-containing protein 8; jumonji
                     domain-containing protein 8"
                     /calculated_mol_wt=27733
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3TA59.4)"
                     /calculated_mol_wt=2672
     mat_peptide     25..269
                     /product="JmjC domain-containing protein 8.
                     /evidence=ECO:0000255. /id=PRO_0000344532"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3TA59.4)"
                     /calculated_mol_wt=27733
     Region          59..253
                     /region_name="Cupin_8"
                     /note="Cupin-like domain; pfam13621"
                     /db_xref="CDD:463936"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q3TA59.4)"
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q3TA59.4)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q3TA59.4)"
     CDS             1..269
                     /gene="Jmjd8"
                     /gene_synonym="2610003J06Rik"
                     /coded_by="NM_028101.5:30..839"
                     /db_xref="CCDS:CCDS28532.2"
                     /db_xref="GeneID:72106"
                     /db_xref="MGI:MGI:1919356"
ORIGIN      
        1 maaagrrgll llfvlwmmvt vilpasgegg wkqnglgiaa avmeeerctv errahityse
       61 fmqhyaflkp vilqgltdns kfralcsren llasfgdniv rlstantysy qkvdlpfqey
      121 veqllqpqdp aslgndtlyf fgdnnftewa slfqhysppp frllgttpay sfgiagagsg
      181 vpfhwhgpgf seviygrkrw flyppektpe fhpnkttlaw lleiypslal sarplectiq
      241 agevlyfpdr wwhatlnldt svfistflg
//
LOCUS       NP_996892                357 aa            linear   PRI 27-APR-2025
DEFINITION  DENN domain-containing protein 10 isoform 1 [Homo sapiens].
ACCESSION   NP_996892
VERSION     NP_996892.1
DBSOURCE    REFSEQ: accession NM_207009.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Zhang,J., Zhang,K., Qi,L., Hu,Q., Shen,Z., Liu,B., Deng,J.,
            Zhang,C. and Zhang,Y.
  TITLE     DENN domain-containing protein FAM45A regulates the homeostasis of
            late/multivesicular endosomes
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1866 (5), 916-929 (2019)
   PUBMED   30771381
  REMARK    GeneRIF: FAM45A defines a novel regulatory step in the homeostasis
            of late endocytic pathway, including endosomal positioning,
            maturation and secretion, possibly through activating Rab proteins
            such as Rab27a/b.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA531569.1, BC022271.1 and AL355598.26.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.212539.1,
                                           SRR1803614.88193.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361432.3/ ENSP00000354688.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.11"
     Protein         1..357
                     /product="DENN domain-containing protein 10 isoform 1"
                     /note="protein FAM45A; family with sequence similarity 45
                     member A; DENN domain-containing protein 10"
                     /calculated_mol_wt=40382
     Region          158..264
                     /region_name="SPA"
                     /note="Stabilization of polarity axis; cl40631"
                     /db_xref="CDD:454797"
     CDS             1..357
                     /gene="DENND10"
                     /gene_synonym="FAM45A"
                     /coded_by="NM_207009.4:31..1104"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7609.1"
                     /db_xref="GeneID:404636"
                     /db_xref="HGNC:HGNC:31793"
ORIGIN      
        1 maaaevadtq lmlgvgliek dtngevlwvw cypsttatlr nlllrkcclt denkllhpfv
       61 fgqyrrtwfy ittievpdss ilkkvthfsi vltakdfnpe kyaaftrilc rmylkhgspv
      121 kmmesyiavl tkgicqseen gsflskdfda rkaylagsik divsqfgmet vilhtalmlk
      181 krivvyhpki eavqeftrtl palvwhrqdw tilhsyvhln adelealqmc tgyvagfvdl
      241 evsnrpdlyd vfvnlaesei tiaplakeam amgklhkemg qlivqsaedp ekseshviqd
      301 ialktreift nlapfsevsa dgekrvlnle alkqkrfppa tenflyhlaa aeqmlki
//
LOCUS       NP_001507                308 aa            linear   PRI 27-APR-2025
DEFINITION  general transcription factor IIH subunit 3 isoform a [Homo
            sapiens].
ACCESSION   NP_001507
VERSION     NP_001507.2
DBSOURCE    REFSEQ: accession NM_001516.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Radu,L., Schoenwetter,E., Braun,C., Marcoux,J., Koelmel,W.,
            Schmitt,D.R., Kuper,J., Cianferani,S., Egly,J.M., Poterszman,A. and
            Kisker,C.
  TITLE     The intricate network between the p34 and p44 subunits is central
            to the activity of the transcription/DNA repair factor TFIIH
  JOURNAL   Nucleic Acids Res 45 (18), 10872-10883 (2017)
   PUBMED   28977422
  REMARK    GeneRIF: interface variants between the p34 and p44 subunits only
            mildly affected the association between the full length proteins
            and did not impinge on TFIIH activities due to the presence of an
            additional interface involving the C4 domain of p34.
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 308)
  AUTHORS   He,Y., Yan,C., Fang,J., Inouye,C., Tjian,R., Ivanov,I. and
            Nogales,E.
  TITLE     Near-atomic resolution visualization of human transcription
            promoter opening
  JOURNAL   Nature 533 (7603), 359-365 (2016)
   PUBMED   27193682
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Marcon,E., Ni,Z., Pu,S., Turinsky,A.L., Trimble,S.S., Olsen,J.B.,
            Silverman-Gavrila,R., Silverman-Gavrila,L., Phanse,S., Guo,H.,
            Zhong,G., Guo,X., Young,P., Bailey,S., Roudeva,D., Zhao,D.,
            Hewel,J., Li,J., Graslund,S., Paduch,M., Kossiakoff,A.A.,
            Lupien,M., Emili,A., Wodak,S.J. and Greenblatt,J.
  TITLE     Human-chromatin-related protein interactions identify a demethylase
            complex required for chromosome segregation
  JOURNAL   Cell Rep 8 (1), 297-310 (2014)
   PUBMED   24981860
REFERENCE   6  (residues 1 to 308)
  AUTHORS   Blau,J., Xiao,H., McCracken,S., O'Hare,P., Greenblatt,J. and
            Bentley,D.
  TITLE     Three functional classes of transcriptional activation domain
  JOURNAL   Mol Cell Biol 16 (5), 2044-2055 (1996)
   PUBMED   8628270
REFERENCE   7  (residues 1 to 308)
  AUTHORS   Tong,X., Drapkin,R., Reinberg,D. and Kieff,E.
  TITLE     The 62- and 80-kDa subunits of transcription factor IIH mediate the
            interaction with Epstein-Barr virus nuclear protein 2
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3259-3263 (1995)
   PUBMED   7724549
REFERENCE   8  (residues 1 to 308)
  AUTHORS   Humbert,S., van Vuuren,H., Lutz,Y., Hoeijmakers,J.H., Egly,J.M. and
            Moncollin,V.
  TITLE     p44 and p34 subunits of the BTF2/TFIIH transcription factor have
            homologies with SSL1, a yeast protein involved in DNA repair
  JOURNAL   EMBO J 13 (10), 2393-2398 (1994)
   PUBMED   8194529
REFERENCE   9  (residues 1 to 308)
  AUTHORS   Schaeffer,L., Roy,R., Humbert,S., Moncollin,V., Vermeulen,W.,
            Hoeijmakers,J.H., Chambon,P. and Egly,J.M.
  TITLE     DNA repair helicase: a component of BTF2 (TFIIH) basic
            transcription factor
  JOURNAL   Science 260 (5104), 58-63 (1993)
   PUBMED   8465201
REFERENCE   10 (residues 1 to 308)
  AUTHORS   Gerard,M., Fischer,L., Moncollin,V., Chipoulet,J.M., Chambon,P. and
            Egly,J.M.
  TITLE     Purification and interaction properties of the human RNA polymerase
            B(II) general transcription factor BTF2
  JOURNAL   J Biol Chem 266 (31), 20940-20945 (1991)
   PUBMED   1939143
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313200.1, BC039726.2,
            AC117503.8, CB955773.1, BM013501.1 and CA306634.1.
            
            On Apr 4, 2002 this sequence version replaced NP_001507.1.
            
            Summary: This gene encodes a member of the TFB4 family. The encoded
            protein is a subunit of the core-TFIIH basal transcription factor
            and localizes to the nucleus. The encoded protein is involved in
            RNA transcription by RNA polymerase II and nucleotide excision
            repair and associates with the Cdk-activating kinase complex.
            Alternative splicing results in multiple transcript variants. A
            related pseudogene has been identified on chromosome 14. [provided
            by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313200.1, SRR1660807.112180.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000543341.7/ ENSP00000445162.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..308
                     /product="general transcription factor IIH subunit 3
                     isoform a"
                     /note="basic transcription factor 2 34 kDa subunit; TFIIH
                     basal transcription factor complex p34 subunit; general
                     transcription factor IIH, polypeptide 3, 34kDa"
                     /calculated_mol_wt=34247
     Region          7..289
                     /region_name="tfb4"
                     /note="transcription factor tfb4; TIGR00627"
                     /db_xref="CDD:273181"
     CDS             1..308
                     /gene="GTF2H3"
                     /gene_synonym="BTF2; P34; TFB4; TFIIH"
                     /coded_by="NM_001516.5:32..958"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9252.1"
                     /db_xref="GeneID:2967"
                     /db_xref="HGNC:HGNC:4657"
                     /db_xref="MIM:601750"
ORIGIN      
        1 mvsdedelnl lvivvdanpi wwgkqalkes qftlskcida vmvlgnshlf mnrsnklavi
       61 ashiqesrfl ypgkngrlgd ffgdpgnppe fnpsgskdgk yelltsanev iveeikdlmt
      121 ksdikgqhte tllagslaka lcyihrmnke vkdnqemksr ilvikaaeds alqymnfmnv
      181 ifaaqkqnil idacvldsds gllqqacdit gglylkvpqm psllqyllwv flpdqdqrsq
      241 lilpppvhvd yraacfchrn lieigyvcsv clsifcnfsp icttcetafk islppvlkak
      301 kkklkvsa
//
LOCUS       NP_055399                468 aa            linear   PRI 27-APR-2025
DEFINITION  ERO1-like protein alpha isoform 2 precursor [Homo sapiens].
ACCESSION   NP_055399
VERSION     NP_055399.1
DBSOURCE    REFSEQ: accession NM_014584.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Germani,S., Van Ho,A.T., Cherubini,A., Varone,E., Chernorudskiy,A.,
            Renna,G.M., Fumagalli,S., Gobbi,M., Lucchetti,J., Bolis,M.,
            Guarrera,L., Craparotta,I., Rastelli,G., Piccoli,G., de Napoli,C.,
            Nogara,L., Poggio,E., Brini,M., Cattaneo,A., Bachi,A., Simmen,T.,
            Cali,T., Quijano-Roy,S., Boncompagni,S., Blaauw,B., Ferreiro,A. and
            Zito,E.
  TITLE     SEPN1-related myopathy depends on the oxidoreductase ERO1A and is
            druggable with the chemical chaperone TUDCA
  JOURNAL   Cell Rep Med 5 (3), 101439 (2024)
   PUBMED   38402623
  REMARK    GeneRIF: SEPN1-related myopathy depends on the oxidoreductase ERO1A
            and is druggable with the chemical chaperone TUDCA.
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Chen,P., Sharma,A., Weiher,H. and Schmidt-Wolf,I.G.H.
  TITLE     Biological mechanisms and clinical significance of endoplasmic
            reticulum oxidoreductase 1 alpha (ERO1alpha) in human cancer
  JOURNAL   J Exp Clin Cancer Res 43 (1), 71 (2024)
   PUBMED   38454454
  REMARK    GeneRIF: Biological mechanisms and clinical significance of
            endoplasmic reticulum oxidoreductase 1 alpha (ERO1alpha) in human
            cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Wu,M., Li,R., Qin,J., Wang,Z., Guo,J., Lv,F., Wang,G. and Huang,Y.
  TITLE     ERO1alpha promotes the proliferation and inhibits apoptosis of
            colorectal cancer cells by regulating the PI3K/AKT pathway
  JOURNAL   J Mol Histol 54 (6), 621-631 (2023)
   PUBMED   37776473
  REMARK    GeneRIF: ERO1alpha promotes the proliferation and inhibits
            apoptosis of colorectal cancer cells by regulating the PI3K/AKT
            pathway.
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Liu,L., Li,S., Qu,Y., Bai,H., Pan,X., Wang,J., Wang,Z., Duan,J.,
            Zhong,J., Wan,R., Fei,K., Xu,J., Yuan,L., Wang,C., Xue,P.,
            Zhang,X., Ma,Z. and Wang,J.
  TITLE     Ablation of ERO1A induces lethal endoplasmic reticulum stress
            responses and immunogenic cell death to activate anti-tumor
            immunity
  JOURNAL   Cell Rep Med 4 (10), 101206 (2023)
   PUBMED   37769655
  REMARK    GeneRIF: Ablation of ERO1A induces lethal endoplasmic reticulum
            stress responses and immunogenic cell death to activate anti-tumor
            immunity.
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Shergalis,A.G., Hu,S., Bankhead,A. 3rd and Neamati,N.
  TITLE     Role of the ERO1-PDI interaction in oxidative protein folding and
            disease
  JOURNAL   Pharmacol Ther 210, 107525 (2020)
   PUBMED   32201313
  REMARK    Review article
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Fan,Y. and Simmen,T.
  TITLE     Mechanistic Connections between Endoplasmic Reticulum (ER) Redox
            Control and Mitochondrial Metabolism
  JOURNAL   Cells 8 (9), 1071 (2019)
   PUBMED   31547228
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Pagani,M., Pilati,S., Bertoli,G., Valsasina,B. and Sitia,R.
  TITLE     The C-terminal domain of yeast Ero1p mediates membrane localization
            and is essential for function
  JOURNAL   FEBS Lett 508 (1), 117-120 (2001)
   PUBMED   11707280
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Benham,A.M., Cabibbo,A., Fassio,A., Bulleid,N., Sitia,R. and
            Braakman,I.
  TITLE     The CXXCXXC motif determines the folding, structure and stability
            of human Ero1-Lalpha
  JOURNAL   EMBO J 19 (17), 4493-4502 (2000)
   PUBMED   10970843
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Pagani,M., Fabbri,M., Benedetti,C., Fassio,A., Pilati,S.,
            Bulleid,N.J., Cabibbo,A. and Sitia,R.
  TITLE     Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human
            gene induced in the course of the unfolded protein response
  JOURNAL   J Biol Chem 275 (31), 23685-23692 (2000)
   PUBMED   10818100
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Cabibbo,A., Pagani,M., Fabbri,M., Rocchi,M., Farmery,M.R.,
            Bulleid,N.J. and Sitia,R.
  TITLE     ERO1-L, a human protein that favors disulfide bond formation in the
            endoplasmic reticulum
  JOURNAL   J Biol Chem 275 (7), 4827-4833 (2000)
   PUBMED   10671517
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC012941.1 and AL133453.3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF081886.1, AK292839.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395686.8/ ENSP00000379042.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.1"
     Protein         1..468
                     /product="ERO1-like protein alpha isoform 2 precursor"
                     /note="ERO1-like protein alpha; oxidoreductin-1-L-alpha;
                     endoplasmic oxidoreductin-1-like protein; endoplasmic
                     reticulum oxidoreductase alpha"
                     /calculated_mol_wt=51992
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2419
     mat_peptide     24..468
                     /product="ERO1-like protein alpha. /id=PRO_0000008415"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HE7.2)"
                     /calculated_mol_wt=51992
     Region          60..457
                     /region_name="ERO1"
                     /note="Endoplasmic Reticulum Oxidoreductin 1 (ERO1);
                     pfam04137"
                     /db_xref="CDD:461191"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96HE7.2)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96HE7.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:29858230; propagated from
                     UniProtKB/Swiss-Prot (Q96HE7.2)"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q96HE7.2)"
     Site            384
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96HE7.2)"
     CDS             1..468
                     /gene="ERO1A"
                     /gene_synonym="ERO1-alpha; ERO1-L; ERO1-L-alpha;
                     Ero1alpha; ERO1L; ERO1LA"
                     /coded_by="NM_014584.3:78..1484"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS9709.1"
                     /db_xref="GeneID:30001"
                     /db_xref="HGNC:HGNC:13280"
                     /db_xref="MIM:615435"
ORIGIN      
        1 mgrgwgflfg llgavwllss ghgeeqppet aaqrcfcqvs gylddctcdv etidrfnnyr
       61 lfprlqklle sdyfryykvn lkrpcpfwnd isqcgrrdca vkpcqsdevp dgiksasyky
      121 seeannliee ceqaerlgav deslseetqk avlqwtkhdd ssdnfceadd iqspeaeyvd
      181 lllnperytg ykgpdawkiw nviyeencfk pqtikrplnp lasgqgtsee ntfyswlegl
      241 cvekrafyrl isglhasinv hlsaryllqe twlekkwghn itefqqrfdg iltegegprr
      301 lknlyflyli elralskvlp fferpdfqlf tgnkiqdeen kmllleilhe iksfplhfde
      361 nsffagdkke ahklkedfrl hfrnisrimd cvgcfkcrlw gklqtqglgt alkilfsekl
      421 ianmpesgps yefhltrqei vslfnafgri stsvkelenf rnllqnih
//
LOCUS       NP_004818                655 aa            linear   PRI 27-APR-2025
DEFINITION  broad substrate specificity ATP-binding cassette transporter ABCG2
            isoform 1 [Homo sapiens].
ACCESSION   NP_004818
VERSION     NP_004818.2
DBSOURCE    REFSEQ: accession NM_004827.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Wu,C.P., Hung,C.Y., Murakami,M., Wu,Y.S., Chu,Y.H., Huang,Y.H.,
            Yu,J.S. and Ambudkar,S.V.
  TITLE     ABCG2 Mediates Resistance to the Dual EGFR and PI3K Inhibitor
            MTX-211 in Cancer Cells
  JOURNAL   Int J Mol Sci 25 (10), 5160 (2024)
   PUBMED   38791198
  REMARK    GeneRIF: ABCG2 Mediates Resistance to the Dual EGFR and PI3K
            Inhibitor MTX-211 in Cancer Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Chen,S., Liu,Z., Wu,H., Wang,B., Ouyang,Y., Liu,J., Zheng,X.,
            Zhang,H., Li,X., Feng,X., Li,Y., Shen,Y., Zhang,H., Xiao,B., Yu,C.
            and Deng,W.
  TITLE     Adipocyte-rich microenvironment promotes chemoresistance via
            upregulation of peroxisome proliferator-activated receptor
            gamma/ABCG2 in epithelial ovarian cancer
  JOURNAL   Int J Mol Med 53 (4) (2024)
   PUBMED   38426604
  REMARK    GeneRIF: Adipocyte-rich microenvironment promotes chemoresistance
            via upregulation of peroxisome proliferator-activated receptor
            gamma/ABCG2 in epithelial ovarian cancer.
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Raguz,M., Tarle,M., Muller,D., Tomasovic-Loncaric,C., Chudy,H.,
            Marinovic,T. and Chudy,D.
  TITLE     ABCG2 Expression as a Potential Survival Predictor in Human Gliomas
  JOURNAL   Int J Mol Sci 25 (6), 3116 (2024)
   PUBMED   38542090
  REMARK    GeneRIF: ABCG2 Expression as a Potential Survival Predictor in
            Human Gliomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Ajenu,E.O., Seideneck,A.M., Pandellapalli,E., Shinsky,E.M.,
            Humphries,C.L., Aparicio,N.L., Sharma,M., Marden,J.H. and
            Krasilnikova,M.M.
  TITLE     ABCG2 transporter reduces protein aggregation in cigarette smoke
            condensate-exposed A549 lung cancer cells
  JOURNAL   PLoS One 19 (3), e0297661 (2024)
   PUBMED   38442133
  REMARK    GeneRIF: ABCG2 transporter reduces protein aggregation in cigarette
            smoke condensate-exposed A549 lung cancer cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Singh,H., Dhotre,K., Shyamveer, Choudhari,R., Verma,A.,
            Mahajan,S.D. and Ali,N.
  TITLE     ABCG2 polymorphisms and susceptibility to ARV-associated
            hepatotoxicity
  JOURNAL   Mol Genet Genomic Med 12 (3), e2362 (2024)
   PUBMED   38451012
  REMARK    GeneRIF: ABCG2 polymorphisms and susceptibility to ARV-associated
            hepatotoxicity.
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Ross,D.D., Yang,W., Abruzzo,L.V., Dalton,W.S., Schneider,E.,
            Lage,H., Dietel,M., Greenberger,L., Cole,S.P. and Doyle,L.A.
  TITLE     Atypical multidrug resistance: breast cancer resistance protein
            messenger RNA expression in mitoxantrone-selected cell lines
  JOURNAL   J Natl Cancer Inst 91 (5), 429-433 (1999)
   PUBMED   10070941
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Miyake,K., Mickley,L., Litman,T., Zhan,Z., Robey,R., Cristensen,B.,
            Brangi,M., Greenberger,L., Dean,M., Fojo,T. and Bates,S.E.
  TITLE     Molecular cloning of cDNAs which are highly overexpressed in
            mitoxantrone-resistant cells: demonstration of homology to ABC
            transport genes
  JOURNAL   Cancer Res 59 (1), 8-13 (1999)
   PUBMED   9892175
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Doyle,L.A., Yang,W., Abruzzo,L.V., Krogmann,T., Gao,Y., Rishi,A.K.
            and Ross,D.D.
  TITLE     A multidrug resistance transporter from human MCF-7 breast cancer
            cells
  JOURNAL   Proc Natl Acad Sci U S A 95 (26), 15665-15670 (1998)
   PUBMED   9861027
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1999 Mar 2;96(5):2569]
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Allikmets,R., Schriml,L.M., Hutchinson,A., Romano-Spica,V. and
            Dean,M.
  TITLE     A human placenta-specific ATP-binding cassette gene (ABCP) on
            chromosome 4q22 that is involved in multidrug resistance
  JOURNAL   Cancer Res 58 (23), 5337-5339 (1998)
   PUBMED   9850061
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI598784.1, BC021281.2 and
            BC092408.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 12, 2005 this sequence version replaced NP_004818.1.
            
            Summary: The membrane-associated protein encoded by this gene is
            included in the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intra-cellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White). This protein is a member of the White subfamily.
            Alternatively referred to as a breast cancer resistance protein,
            this protein functions as a xenobiotic transporter which may play a
            major role in multi-drug resistance. It likely serves as a cellular
            defense mechanism in response to mitoxantrone and anthracycline
            exposure. Significant expression of this protein has been observed
            in the placenta, which may suggest a potential role for this
            molecule in placenta tissue. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Apr 2012].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.118989.1,
                                           SRR14038191.4108211.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000237612.8/ ENSP00000237612.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.1"
     Protein         1..655
                     /product="broad substrate specificity ATP-binding cassette
                     transporter ABCG2 isoform 1"
                     /EC_number="7.6.2.2"
                     /note="breast cancer resistance protein; placenta specific
                     MDR protein; ABC transporter; ATP-binding cassette
                     transporter G2; mitoxantrone resistance-associated
                     protein; placenta-specific ATP-binding cassette
                     transporter; ATPbinding cassette transporter ABCG2; ATP
                     binding cassette subfamily G member 2 (Junior blood
                     group); multi drug resistance efflux transport ATP-binding
                     cassette sub-family G (WHITE) member 2; broad substrate
                     specificity ATP-binding cassette transporter ABCG2 isoform
                     1 (Junior blood group); urate exporter; ATP-binding
                     cassette, sub-family G (WHITE), member 2 (Junior blood
                     group)"
                     /calculated_mol_wt=72183
     Region          55..649
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PIM1.
                     /evidence=ECO:0000269|PubMed:18056989; propagated from
                     UniProtKB/Swiss-Prot (Q9UNQ0.3)"
     Site            396..416
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNQ0.3)"
     Site            418
                     /site_type="other"
                     /note="Not glycosylated.
                     /evidence=ECO:0000269|PubMed:15807535; propagated from
                     UniProtKB/Swiss-Prot (Q9UNQ0.3)"
     Site            429..449
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNQ0.3)"
     Site            478..498
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNQ0.3)"
     Site            507..527
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNQ0.3)"
     Site            536..556
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNQ0.3)"
     Site            557
                     /site_type="other"
                     /note="Not glycosylated.
                     /evidence=ECO:0000269|PubMed:15807535; propagated from
                     UniProtKB/Swiss-Prot (Q9UNQ0.3)"
     Site            596
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15807535,
                     ECO:0000269|PubMed:28554189, ECO:0007744|PDB:5NJ3,
                     ECO:0007744|PDB:5NJG; propagated from UniProtKB/Swiss-Prot
                     (Q9UNQ0.3)"
     Site            631..651
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNQ0.3)"
     CDS             1..655
                     /gene="ABCG2"
                     /gene_synonym="ABC15; ABCP; BCRP; BCRP1; BMDP; CD338;
                     CDw338; CDw388; EST157481; GOUT1; MRX; MXR; MXR-1; MXR1;
                     UAQTL1"
                     /coded_by="NM_004827.3:274..2241"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3628.1"
                     /db_xref="GeneID:9429"
                     /db_xref="HGNC:HGNC:74"
                     /db_xref="MIM:603756"
ORIGIN      
        1 msssnvevfi pvsqgntngf patasndlka ftegavlsfh nicyrvklks gflpcrkpve
       61 keilsningi mkpglnailg ptgggkssll dvlaarkdps glsgdvling aprpanfkcn
      121 sgyvvqddvv mgtltvrenl qfsaalrlat tmtnhekner inrviqelgl dkvadskvgt
      181 qfirgvsgge rkrtsigmel itdpsilfld epttgldsst anavllllkr mskqgrtiif
      241 sihqprysif klfdsltlla sgrlmfhgpa qealgyfesa gyhceaynnp adffldiing
      301 dstavalnre edfkateiie pskqdkplie klaeiyvnss fyketkaelh qlsggekkkk
      361 itvfkeisyt tsfchqlrwv skrsfknllg npqasiaqii vtvvlglvig aiyfglknds
      421 tgiqnragvl fflttnqcfs svsavelfvv ekklfiheyi sgyyrvssyf lgkllsdllp
      481 mrmlpsiift civyfmlglk pkadaffvmm ftlmmvaysa ssmalaiaag qsvvsvatll
      541 mticfvfmmi fsgllvnltt iaswlswlqy fsiprygfta lqhneflgqn fcpglnatgn
      601 npcnyatctg eeylvkqgid lspwglwknh valacmivif ltiaylkllf lkkys
//
LOCUS       NP_878901                508 aa            linear   PRI 27-APR-2025
DEFINITION  cyclic AMP-responsive element-binding protein 5 isoform alpha [Homo
            sapiens].
ACCESSION   NP_878901
VERSION     NP_878901.2
DBSOURCE    REFSEQ: accession NM_182898.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Yamada,C., Okada,K., Odaira,K., Tokoro,M., Iwamoto,E., Sanada,M.,
            Noura,M., Okamoto,S., Yasuda,T., Tsuzuki,S., Kiyoi,H. and
            Hayakawa,F.
  TITLE     RGS1 and CREB5 are direct and common transcriptional targets of
            ZNF384-fusion proteins
  JOURNAL   Cancer Med 13 (14), e7471 (2024)
   PUBMED   39015025
  REMARK    GeneRIF: RGS1 and CREB5 are direct and common transcriptional
            targets of ZNF384-fusion proteins.
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Li,Z., Dai,F., Zhu,R., Zhang,Y., Chen,J., Chen,L., Liu,H. and
            Cheng,Y.
  TITLE     Dysregulation of CREB5 Impairs Decidualization and Maternal-Fetal
            Interactions by Inhibiting Autophagy in Recurrent Spontaneous
            Abortion
  JOURNAL   Reprod Sci 31 (7), 1983-2000 (2024)
   PUBMED   38424407
  REMARK    GeneRIF: Dysregulation of CREB5 Impairs Decidualization and
            Maternal-Fetal Interactions by Inhibiting Autophagy in Recurrent
            Spontaneous Abortion.
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Wu,Z., Wang,X., Wu,H., Du,S., Wang,Z., Xie,S., Zhang,R., Chen,G.
            and Chen,H.
  TITLE     Identification of CREB5 as a prognostic and immunotherapeutic
            biomarker in glioma through multi-omics pan-cancer analysis
  JOURNAL   Comput Biol Med 173, 108307 (2024)
   PUBMED   38547657
  REMARK    GeneRIF: Identification of CREB5 as a prognostic and
            immunotherapeutic biomarker in glioma through multi-omics
            pan-cancer analysis.
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Zhou,R., Zhao,L., Wang,Q., Cheng,Y., Song,M. and Huang,C.
  TITLE     Plasma microRNA-320c as a Potential Biomarker for the Severity of
            Knee Osteoarthritis and Regulates cAMP Responsive Element Binding
            Protein 5 (CREB5) in Chondrocytes
  JOURNAL   Dis Markers 2024, 9936295 (2024)
   PUBMED   38549717
  REMARK    GeneRIF: Plasma microRNA-320c as a Potential Biomarker for the
            Severity of Knee Osteoarthritis and Regulates cAMP Responsive
            Element Binding Protein 5 (CREB5) in Chondrocytes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Gong,D.A., Zhou,P., Chang,W.Y., Yang,J.Y., Zhang,Y.L., Huang,A.L.,
            Tang,N. and Wang,K.
  TITLE     SPOP promotes CREB5 ubiquitination to inhibit MET signaling in
            liver cancer
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (2), 119642 (2024)
   PUBMED   37996058
  REMARK    GeneRIF: SPOP promotes CREB5 ubiquitination to inhibit MET
            signaling in liver cancer.
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Qi,L. and Ding,Y.
  TITLE     Involvement of the CREB5 regulatory network in colorectal cancer
            metastasis
  JOURNAL   Yi Chuan 36 (7), 679-684 (2014)
   PUBMED   25076032
  REMARK    GeneRIF: CREB5 accelerate the metastasis of colorectal cancer by
            regulating these five key genes.
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Zu,Y.L., Maekawa,T., Nomura,N., Nakata,T. and Ishii,S.
  TITLE     Regulation of trans-activating capacity of CRE-BPa by phorbol ester
            tumor promoter TPA
  JOURNAL   Oncogene 8 (10), 2749-2758 (1993)
   PUBMED   8378084
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Nomura,N., Zu,Y.L., Maekawa,T., Tabata,S., Akiyama,T. and Ishii,S.
  TITLE     Isolation and characterization of a novel member of the gene family
            encoding the cAMP response element-binding protein CRE-BP1
  JOURNAL   J Biol Chem 268 (6), 4259-4266 (1993)
   PUBMED   8440710
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006367.3, L05515.1,
            AB451409.1, AC005013.3 and BQ130001.1.
            
            On Feb 18, 2005 this sequence version replaced NP_878901.1.
            
            Summary: The product of this gene belongs to the CRE (cAMP response
            element)-binding protein family. Members of this family contain
            zinc-finger and bZIP DNA-binding domains. The encoded protein
            specifically binds to CRE as a homodimer or a heterodimer with
            c-Jun or CRE-BP1, and functions as a CRE-dependent trans-activator.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript, and encodes the longest isoform (alpha).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L05515.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467150, SAMN03267757
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357727.7/ ENSP00000350359.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.1-p14.3"
     Protein         1..508
                     /product="cyclic AMP-responsive element-binding protein 5
                     isoform alpha"
                     /note="cAMP response element-binding protein CRE-BPa;
                     cyclic AMP-responsive element-binding protein 5;
                     cAMP-response element-binding protein A"
                     /calculated_mol_wt=56787
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q02930.3)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q02930.3)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q02930.3)"
     Region          265..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02930.3)"
     Region          377..436
                     /region_name="bZIP_ATF2"
                     /note="Basic leucine zipper (bZIP) domain of Activating
                     Transcription Factor-2 (ATF-2) and similar proteins: a
                     DNA-binding and dimerization domain; cd14687"
                     /db_xref="CDD:269835"
     Region          377..436
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269835"
     Region          377..397
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02930.3)"
     Site            order(378,382,384..386,389,391..393,395..397)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269835"
     Site            order(396,403..404,406..407,410..411,414,417..418,421,
                     424..425,427..428,431..432,435..436)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269835"
     Region          403..431
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02930.3)"
     Region          449..468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02930.3)"
     CDS             1..508
                     /gene="CREB5"
                     /gene_synonym="CRE-BPA; CREB-5; CREBPA"
                     /coded_by="NM_182898.4:398..1924"
                     /note="isoform alpha is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5417.1"
                     /db_xref="GeneID:9586"
                     /db_xref="HGNC:HGNC:16844"
                     /db_xref="MIM:618262"
ORIGIN      
        1 miyeeskmnl eqerpfvcsa pgcsqrfpte dhlmihrhkh emtlkfpsik tdnmlsdqtp
       61 tptrflknce evglfseldc slehefrkaq eeesskrnis mhnavggamt gpgthqlssa
      121 rlpnhdtnvv iqqampspqs ssvitqapst nrqigpvpgs lssllhlhnr qrqpmpasmp
      181 gtlpnptmpg ssavlmpmer qmsvnssimg mqgpnlsnpc aspqvqpmhs eakmrlkaal
      241 thhpaamsng nmntmghmme mmgsrqdqtp hhhmhshphq hqtlpphhpy phqhqhpahh
      301 phpqphhqqn hphhhshshl hahpahhqts phpplhtgnq aqvspatqqm qptqtiqppq
      361 ptggrrrrvv dedpderrrk flernraaat rcrqkrkvwv mslekkaeel tqtnmqlqne
      421 vsmlknevaq lkqlllthkd cpitamqkes qgylspessp paspvpacsq qqviqhntit
      481 tsssvsevvg sstlsqltth rtdlnpil
//
LOCUS       NP_003065               1105 aa            linear   PRI 27-APR-2025
DEFINITION  SWI/SNF complex subunit SMARCC1 [Homo sapiens].
ACCESSION   NP_003065
VERSION     NP_003065.3
DBSOURCE    REFSEQ: accession NM_003074.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Singh,A.K., Allington,G., Viviano,S., McGee,S., Kiziltug,E., Ma,S.,
            Zhao,S., Mekbib,K.Y., Shohfi,J.P., Duy,P.Q., DeSpenza,T. Jr.,
            Furey,C.G., Reeves,B.C., Smith,H., Sousa,A.M.M., Cherskov,A.,
            Allocco,A., Nelson-Williams,C., Haider,S., Rizvi,S.R.A.,
            Alper,S.L., Sestan,N., Shimelis,H., Walsh,L.K., Lifton,R.P.,
            Moreno-De-Luca,A., Jin,S.C., Kruszka,P., Deniz,E. and Kahle,K.T.
  TITLE     A novel SMARCC1 BAFopathy implicates neural progenitor epigenetic
            dysregulation in human hydrocephalus
  JOURNAL   Brain 147 (4), 1553-1570 (2024)
   PUBMED   38128548
  REMARK    GeneRIF: A novel SMARCC1 BAFopathy implicates neural progenitor
            epigenetic dysregulation in human hydrocephalus.
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Hourvitz,N., Kurolap,A., Mory,A., Haratz,K.K., Kidron,D.,
            Malinger,G., Baris Feldman,H. and Yaron,Y.
  TITLE     SMARCC1 is a susceptibility gene for congenital hydrocephalus with
            an autosomal dominant inheritance mode and incomplete penetrance
  JOURNAL   Prenat Diagn 43 (10), 1374-1377 (2023)
   PUBMED   37639281
  REMARK    GeneRIF: SMARCC1 is a susceptibility gene for congenital
            hydrocephalus with an autosomal dominant inheritance mode and
            incomplete penetrance.
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Rive Le Gouard,N., Nicolle,R., Lefebvre,M., Gelot,A., Heide,S.,
            Gerasimenko,A., Grigorescu,R., Derive,N., Jouannic,J.M., Garel,C.,
            Valence,S., Quenum-Miraillet,G., Chantot-Bastaraud,S., Keren,B.,
            Heron,D. and Attie-Bitach,T.
  TITLE     First reports of fetal SMARCC1 related hydrocephalus
  JOURNAL   Eur J Med Genet 66 (8), 104797 (2023)
   PUBMED   37285932
  REMARK    GeneRIF: First reports of fetal SMARCC1 related hydrocephalus.
            Review article
REFERENCE   4  (residues 1 to 1105)
  AUTHORS   Paun,O., Tan,Y.X., Patel,H., Strohbuecker,S., Ghanate,A.,
            Cobolli-Gigli,C., Llorian Sopena,M., Gerontogianni,L.,
            Goldstone,R., Ang,S.L., Guillemot,F. and Dias,C.
  TITLE     Pioneer factor ASCL1 cooperates with the mSWI/SNF complex at distal
            regulatory elements to regulate human neural differentiation
  JOURNAL   Genes Dev 37 (5-6), 218-242 (2023)
   PUBMED   36931659
REFERENCE   5  (residues 1 to 1105)
  AUTHORS   Liu,W., Wang,Z., Liu,S., Zhang,X., Cao,X. and Jiang,M.
  TITLE     RNF138 inhibits late inflammatory gene transcription through
            degradation of SMARCC1 of the SWI/SNF complex
  JOURNAL   Cell Rep 42 (2), 112097 (2023)
   PUBMED   36800290
  REMARK    GeneRIF: RNF138 inhibits late inflammatory gene transcription
            through degradation of SMARCC1 of the SWI/SNF complex.
REFERENCE   6  (residues 1 to 1105)
  AUTHORS   Ring,H.Z., Vameghi-Meyers,V., Wang,W., Crabtree,G.R. and Francke,U.
  TITLE     Five SWI/SNF-related, matrix-associated, actin-dependent regulator
            of chromatin (SMARC) genes are dispersed in the human genome
  JOURNAL   Genomics 51 (1), 140-143 (1998)
   PUBMED   9693044
REFERENCE   7  (residues 1 to 1105)
  AUTHORS   Fryer,C.J. and Archer,T.K.
  TITLE     Chromatin remodelling by the glucocorticoid receptor requires the
            BRG1 complex
  JOURNAL   Nature 393 (6680), 88-91 (1998)
   PUBMED   9590696
REFERENCE   8  (residues 1 to 1105)
  AUTHORS   Reyes,J.C., Muchardt,C. and Yaniv,M.
  TITLE     Components of the human SWI/SNF complex are enriched in active
            chromatin and are associated with the nuclear matrix
  JOURNAL   J Cell Biol 137 (2), 263-274 (1997)
   PUBMED   9128241
REFERENCE   9  (residues 1 to 1105)
  AUTHORS   Wang,W., Cote,J., Xue,Y., Zhou,S., Khavari,P.A., Biggar,S.R.,
            Muchardt,C., Kalpana,G.V., Goff,S.P., Yaniv,M., Workman,J.L. and
            Crabtree,G.R.
  TITLE     Purification and biochemical heterogeneity of the mammalian SWI-SNF
            complex
  JOURNAL   EMBO J 15 (19), 5370-5382 (1996)
   PUBMED   8895581
REFERENCE   10 (residues 1 to 1105)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC012101.1, BC050564.1, BC040242.1 and AC112512.6.
            
            On May 20, 2008 this sequence version replaced NP_003065.2.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins, whose members display helicase and
            ATPase activities and which are thought to regulate transcription
            of certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI and contains a predicted
            leucine zipper motif typical of many transcription factors.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U66615.1, BC050564.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254480.10/ ENSP00000254480.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1105
                     /product="SWI/SNF complex subunit SMARCC1"
                     /note="chromatin remodeling complex BAF155 subunit;
                     SWI/SNF complex 155 kDa subunit; mammalian chromatin
                     remodeling complex BRG1-associated factor 155;
                     SWI/SNF-related matrix-associated actin-dependent
                     regulator of chromatin subfamily C member 1; SWI/SNF
                     related, matrix associated, actin dependent regulator of
                     chromatin subfamily c member 1"
                     /calculated_mol_wt=122736
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.3,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Region          28..302
                     /region_name="MarR-like, BRCT and chromo domains module.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01376"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92922.3)"
     Region          32..445
                     /region_name="SWIRM-assoc_2"
                     /note="SWIRM-associated domain at the N-terminal;
                     pfam16496"
                     /db_xref="CDD:465143"
     Region          296..439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92922.3)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92922.3)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Site            345
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Site            346
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Site            354
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Site            359
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Region          444..>710
                     /region_name="RSC8"
                     /note="RSC chromatin remodeling complex subunit RSC8
                     [Chromatin structure and dynamics / Transcription];
                     COG5259"
                     /db_xref="CDD:227584"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Region          706..772
                     /region_name="SWIRM-assoc_3"
                     /note="SWIRM-associated domain at the C-terminal;
                     pfam16498"
                     /db_xref="CDD:465145"
     Region          745..860
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92922.3)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Region          883..954
                     /region_name="SWIRM-assoc_1"
                     /note="SWIRM-associated region 1; pfam16495"
                     /db_xref="CDD:465142"
     Site            948
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     Region          956..1028
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92922.3)"
     Region          1041..1105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92922.3)"
     Site            1064
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P97496; propagated from
                     UniProtKB/Swiss-Prot (Q92922.3)"
     CDS             1..1105
                     /gene="SMARCC1"
                     /gene_synonym="BAF155; CRACC1; HYC5; Rsc8; SRG3; SWI3"
                     /coded_by="NM_003074.4:97..3414"
                     /db_xref="CCDS:CCDS2758.1"
                     /db_xref="GeneID:6599"
                     /db_xref="HGNC:HGNC:11104"
                     /db_xref="MIM:601732"
ORIGIN      
        1 maaaaggggp gtavgatgsg iaaaaaglav yrrkdggpat kfwespetvs qldsvrvwlg
       61 khykkyvhad aptnktlagl vvqllqfqed afgkhvtnpa ftklpakcfm dfkaggalch
      121 ilgaaykykn eqgwrrfdlq npsrmdrnve mfmniektlv qnncltrpni ylipdidlkl
      181 anklkdiikr hqgtftdeks kashhiypys ssqddeewlr pvmrkekqvl vhwgfypdsy
      241 dtwvhsndvd aeiedppipe kpwkvhvkwi ldtdifnewm needyevden rkpvsfrqri
      301 stkneepvrs perrdrkasa narkrkhsps pppptptesr kksgkkgqas lygkrrsqke
      361 edeqedltkd medptpvpni eevvlpknvn lkkdsentpv kggtvadlde qdeetvtagg
      421 kededpakgd qsrsvdlged nvteqtnhii ipsyaswfdy ncihvierra lpeffngknk
      481 sktpeiylay rnfmidtyrl npqeyltsta crrnltgdvc avmrvhafle qwglvnyqvd
      541 pesrpmamgp pptphfnvla dtpsglvplh lrspqvpaaq qmlnfpeknk ekpvdlqnfg
      601 lrtdiyskkt lakskgasag rewteqetll llealemykd dwnkvsehvg srtqdecilh
      661 flrlpiedpy lensdaslgp layqpvpfsq sgnpvmstva flasvvdprv asaaakaale
      721 efsrvreevp lelveahvkk vqeaarasgk vdptygless ciagtgpdep eklegaeeek
      781 meadpdgqqp ekaenkvene tdegdkaqdg eneknsekeq dsevsedtks eeketeenke
      841 ltdtckeres dtgkkkvehe isegnvataa aaalasaatk akhlaaveer kikslvallv
      901 etqmkkleik lrhfeeleti mdrekealeq qrqqllterq nfhmeqlkya elrarqqmeq
      961 qqhgqnpqqa hqhsggpgla plgaaghpgm mphqqpppyp lmhhqmppph ppqpgqipgp
     1021 gsmmpgqhmp grmiptvaan ihpsgsgptp pgmppmpgni lgprvpltap ngmyppppqq
     1081 qppppppadg vppppapgpp asaap
//
LOCUS       NP_005864                217 aa            linear   PRI 27-APR-2025
DEFINITION  regulator of G-protein signaling 19 [Homo sapiens].
ACCESSION   NP_005864
VERSION     NP_005864.1
DBSOURCE    REFSEQ: accession NM_005873.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Ke,S., Lu,S., Xu,Y., Bai,M., Yu,H., Yin,B., Wang,C., Feng,Z.,
            Li,Z., Huang,J., Li,X., Qian,B., Hua,Y., Fu,Y., Sun,B., Wu,Y. and
            Ma,Y.
  TITLE     RGS19 activates the MYH9/beta-catenin/c-Myc positive feedback loop
            in hepatocellular carcinoma
  JOURNAL   Exp Mol Med 56 (6), 1412-1425 (2024)
   PUBMED   38825640
  REMARK    GeneRIF: RGS19 activates the MYH9/beta-catenin/c-Myc positive
            feedback loop in hepatocellular carcinoma.
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Liu,Y., Lou,W., Chen,G., Ding,B., Kuang,J., Zhang,Y., Wang,C.,
            Duan,S., Deng,Y. and Lu,X.
  TITLE     Genome-wide screening for the G-protein-coupled receptor (GPCR)
            pathway-related therapeutic gene RGS19 (regulator of G protein
            signaling 19) in bladder cancer
  JOURNAL   Bioengineered 12 (1), 5892-5903 (2021)
   PUBMED   34482807
  REMARK    GeneRIF: Genome-wide screening for the G-protein-coupled receptor
            (GPCR) pathway-related therapeutic gene RGS19 (regulator of G
            protein signaling 19) in bladder cancer.
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Solis,G.P., Kozhanova,T.V., Koval,A., Zhilina,S.S.,
            Mescheryakova,T.I., Abramov,A.A., Ishmuratov,E.V., Bolshakova,E.S.,
            Osipova,K.V., Ayvazyan,S.O., Lebon,S., Kanivets,I.V., Pyankov,D.V.,
            Troccaz,S., Silachev,D.N., Zavadenko,N.N., Prityko,A.G. and
            Katanaev,V.L.
  TITLE     Pediatric Encephalopathy: Clinical, Biochemical and Cellular
            Insights into the Role of Gln52 of GNAO1 and GNAI1 for the Dominant
            Disease
  JOURNAL   Cells 10 (10), 2749 (2021)
   PUBMED   34685729
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Hwang,J., Kim,H.S., Kang,B.S., Kim,D.H., Ryoo,Z.Y., Choi,S.U. and
            Lee,S.
  TITLE     RGS19 converts iron deprivation stress into a growth-inhibitory
            signal
  JOURNAL   Biochem Biophys Res Commun 464 (1), 168-175 (2015)
   PUBMED   26116529
  REMARK    GeneRIF: RGS19 senses cellular iron availability and is stabilized
            under iron-depleted conditions, resulting in the induction of a
            growth-inhibitory signal.
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Wang,J., Ducret,A., Tu,Y., Kozasa,T., Aebersold,R. and Ross,E.M.
  TITLE     RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane
            association, regulation by Galphaz phosphorylation, and
            relationship to a Gz gtpase-activating protein subfamily
  JOURNAL   J Biol Chem 273 (40), 26014-26025 (1998)
   PUBMED   9748280
REFERENCE   7  (residues 1 to 217)
  AUTHORS   De Vries,L., Elenko,E., McCaffery,J.M., Fischer,T., Hubler,L.,
            McQuistan,T., Watson,N. and Farquhar,M.G.
  TITLE     RGS-GAIP, a GTPase-activating protein for Galphai heterotrimeric G
            proteins, is located on clathrin-coated vesicles
  JOURNAL   Mol Biol Cell 9 (5), 1123-1134 (1998)
   PUBMED   9571244
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Ogier-Denis,E., Petiot,A., Bauvy,C. and Codogno,P.
  TITLE     Control of the expression and activity of the Galpha-interacting
            protein (GAIP) in human intestinal cells
  JOURNAL   J Biol Chem 272 (39), 24599-24603 (1997)
   PUBMED   9305927
REFERENCE   9  (residues 1 to 217)
  AUTHORS   De Vries,L., Elenko,E., Hubler,L., Jones,T.L. and Farquhar,M.G.
  TITLE     GAIP is membrane-anchored by palmitoylation and interacts with the
            activated (GTP-bound) form of G alpha i subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (26), 15203-15208 (1996)
   PUBMED   8986788
REFERENCE   10 (residues 1 to 217)
  AUTHORS   De Vries,L., Mousli,M., Wurmser,A. and Farquhar,M.G.
  TITLE     GAIP, a protein that specifically interacts with the trimeric G
            protein G alpha i3, is a member of a protein family with a highly
            conserved core domain
  JOURNAL   Proc Natl Acad Sci U S A 92 (25), 11916-11920 (1995)
   PUBMED   8524874
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590548.22, AF285097.1 and
            BC063010.1.
            
            Summary: G proteins mediate a number of cellular processes. The
            protein encoded by this gene belongs to the RGS (regulators of
            G-protein signaling) family and specifically interacts with G
            protein, GAI3. This protein is a guanosine
            triphosphatase-activating protein that functions to down-regulate
            Galpha i/Galpha q-linked signaling. Alternatively spliced
            transcript variants encoding the same protein isoform have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the longer transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.83188.1,
                                           SRR3476690.598730.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395042.2/ ENSP00000378483.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..217
                     /product="regulator of G-protein signaling 19"
                     /note="G alpha interacting protein; regulator of G-protein
                     signalling 19; G protein signalling regulator 19; guanine
                     nucleotide binding protein alpha inhibiting activity
                     polypeptide 3 interacting protein"
                     /calculated_mol_wt=24505
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49795.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70521; propagated from
                     UniProtKB/Swiss-Prot (P49795.1)"
     Region          87..204
                     /region_name="RGS_RGS19"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS19 protein; cd08745"
                     /db_xref="CDD:188699"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P49795.1)"
     Site            order(112,116,119,155..156,184,187)
                     /site_type="other"
                     /note="putative G-alpha interaction site"
                     /db_xref="CDD:188699"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1 and MAPK3.
                     /evidence=ECO:0000269|PubMed:10993892; propagated from
                     UniProtKB/Swiss-Prot (P49795.1)"
     Region          207..217
                     /region_name="Interaction with GIPC"
                     /note="propagated from UniProtKB/Swiss-Prot (P49795.1)"
     CDS             1..217
                     /gene="RGS19"
                     /gene_synonym="GAIP; RGSGAIP"
                     /coded_by="NM_005873.3:294..947"
                     /db_xref="CCDS:CCDS13555.1"
                     /db_xref="GeneID:10287"
                     /db_xref="HGNC:HGNC:13735"
                     /db_xref="MIM:605071"
ORIGIN      
        1 mptpheaekq itgpeeadrp psmsshdtas paapsrnpcc lcwccccscs wnqerrrawq
       61 asresklqpl pscevcatps peevqswaqs fdklmhspag rsvfraflrt eyseenmlfw
      121 laceelkaea nqhvvdekar liyedyvsil spkevsldsr vreginkkmq epsahtfdda
      181 qlqiytlmhr dsyprflssp tyralllqgp sqsssea
//
LOCUS       NP_620775                409 aa            linear   PRI 27-APR-2025
DEFINITION  BRCA1-A complex subunit Abraxas 1 isoform 1 [Homo sapiens].
ACCESSION   NP_620775
VERSION     NP_620775.2
DBSOURCE    REFSEQ: accession NM_139076.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Sachsenweger,J., Jansche,R., Merk,T., Heitmeir,B., Deniz,M.,
            Faust,U., Roggia,C., Tzschach,A., Schroeder,C., Riess,A.,
            Pospiech,H., Peltoketo,H., Pylkas,K., Winqvist,R. and Wiesmuller,L.
  TITLE     ABRAXAS1 orchestrates BRCA1 activities to counter genome
            destabilizing repair pathways-lessons from breast cancer patients
  JOURNAL   Cell Death Dis 14 (5), 328 (2023)
   PUBMED   37198153
  REMARK    GeneRIF: ABRAXAS1 orchestrates BRCA1 activities to counter genome
            destabilizing repair pathways-lessons from breast cancer patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Wu,Q., Paul,A., Su,D., Mehmood,S., Foo,T.K., Ochi,T., Bunting,E.L.,
            Xia,B., Robinson,C.V., Wang,B. and Blundell,T.L.
  TITLE     Structure of BRCA1-BRCT/Abraxas Complex Reveals
            Phosphorylation-Dependent BRCT Dimerization at DNA Damage Sites
  JOURNAL   Mol Cell 61 (3), 434-448 (2016)
   PUBMED   26778126
  REMARK    GeneRIF: Demonstrate a mechanism involving IR-induced
            phosphorylation and dimerization of the BRCT/Abraxas complex for
            regulating Abraxas-mediated recruitment of BRCA1 in response to IR.
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Osorio,A., Barroso,A., Garcia,M.J., Martinez-Delgado,B., Urioste,M.
            and Benitez,J.
  TITLE     Evaluation of the BRCA1 interacting genes RAP80 and CCDC98 in
            familial breast cancer susceptibility
  JOURNAL   Breast Cancer Res Treat 113 (2), 371-376 (2009)
   PUBMED   18270812
  REMARK    GeneRIF: Mutational analysis in 168 multiple-case breast/ovarian
            cancer families, negative for mutations in BRCA1 or BRCA2, suggests
            that CCDC98 does not play an important role as a high penetrance
            breast cancer susceptibility gene.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 409)
  AUTHORS   Wang,B. and Elledge,S.J.
  TITLE     Ubc13/Rnf8 ubiquitin ligases control foci formation of the
            Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage
  JOURNAL   Proc Natl Acad Sci U S A 104 (52), 20759-20763 (2007)
   PUBMED   18077395
  REMARK    GeneRIF: the human Ubc13/Rnf8 ubiquitin ligases control foci
            formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to
            DNA damage
REFERENCE   8  (residues 1 to 409)
  AUTHORS   Kim,H., Huang,J. and Chen,J.
  TITLE     CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA
            damage response
  JOURNAL   Nat Struct Mol Biol 14 (8), 710-715 (2007)
   PUBMED   17643122
  REMARK    GeneRIF: CCDC98 is a mediator of BRCA1 function involved in the
            mammalian DNA damage response.
REFERENCE   9  (residues 1 to 409)
  AUTHORS   Liu,Z., Wu,J. and Yu,X.
  TITLE     CCDC98 targets BRCA1 to DNA damage sites
  JOURNAL   Nat Struct Mol Biol 14 (8), 716-720 (2007)
   PUBMED   17643121
  REMARK    GeneRIF: CCDC98 is a BRCA1 binding partner that mediates BRCA1
            function in response to DNA damage.
REFERENCE   10 (residues 1 to 409)
  AUTHORS   Wang,B., Matsuoka,S., Ballif,B.A., Zhang,D., Smogorzewska,A.,
            Gygi,S.P. and Elledge,S.J.
  TITLE     Abraxas and RAP80 form a BRCA1 protein complex required for the DNA
            damage response
  JOURNAL   Science 316 (5828), 1194-1198 (2007)
   PUBMED   17525340
  REMARK    GeneRIF: Abraxas and RAP80 were required for DNA damage resistance,
            G(2)-M checkpoint control, and DNA repair.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096768.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 15, 2006 this sequence version replaced NP_620775.1.
            
            Summary: This gene encodes a protein that binds to the C-terminal
            repeats of breast cancer 1 (BRCA1) through a phospho-SXXF motif.
            The encoded protein recruits ubiquitin interaction motif containing
            1 protein to BRCA1 protein and is required for DNA damage
            resistance, DNA repair, and cell cycle checkpoint control.
            Pseudogenes of this gene are found on chromosomes 3 and 8.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022704.1, BC039573.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321945.12/ ENSP00000369857.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.23"
     Protein         1..409
                     /product="BRCA1-A complex subunit Abraxas 1 isoform 1"
                     /note="coiled-coil domain containing 98; abraxas protein;
                     family with sequence similarity 175 member A; BRCA1-A
                     complex subunit Abraxas 1"
                     /calculated_mol_wt=46532
     Region          2..380
                     /region_name="Abraxas_1"
                     /note="BRCA1-A complex subunit Abraxas 1; cd23523"
                     /db_xref="CDD:467803"
     Site            order(11..13,15..17,19..20,23..28,45..47,49,62..66,68..71,
                     76,87,91,101,103..109,111..114,116,139..140,144..152,
                     163..165,168..177,179..184,186,188..191,195,199,202..203,
                     207..209,211..213,215..216,218..219,222..223,225..227,
                     229..230,233..234,236..241,243..244,246..247,250..251,
                     253..254,257,275..277,279..280,283..284,287..288,294,
                     297..307,321..325,327..329)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467803"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPZ8; propagated from
                     UniProtKB/Swiss-Prot (Q6UWZ7.2)"
     Site            170
                     /site_type="active"
                     /note="BRCC36 activation site [active]"
                     /db_xref="CDD:467803"
     Region          362..409
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWZ7.2)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q6UWZ7.2)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q6UWZ7.2)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6UWZ7.2)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26778126; propagated from
                     UniProtKB/Swiss-Prot (Q6UWZ7.2)"
     Region          406..409
                     /region_name="pSXXF motif. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWZ7.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17525340,
                     ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122,
                     ECO:0000269|PubMed:26778126, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UWZ7.2)"
     CDS             1..409
                     /gene="ABRAXAS1"
                     /gene_synonym="ABRA1; CCDC98; FAM175A"
                     /coded_by="NM_139076.3:29..1258"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3605.2"
                     /db_xref="GeneID:84142"
                     /db_xref="HGNC:HGNC:25829"
                     /db_xref="MIM:611143"
ORIGIN      
        1 megestsavl sgfvlgalaf qhlntdsdte gfllgevkge aknsitdsqm ddvevvytid
       61 iqkyipcyql fsfynssgev neqalkkils nvkknvvgwy kfrrhsdqim tfrerllhkn
      121 lqehfsnqdl vfllltpsii tescsthrle hslykpqkgl fhrvplvvan lgmseqlgyk
      181 tvsgscmstg fsravqthss kffeedgslk evhkinemya slqeelksic kkvedseqav
      241 dklvkdvnrl kreiekrrga qiqaarekni qkdpqenifl cqalrtffpn seflhscvms
      301 lknrhvskss cnynhhldvv dnltlmveht dipeaspast pqiikhkald lddrwqfkrs
      361 rlldtqdkrs kadtgssnqd kaskmsspet deeiekmkgf geysrsptf
//
LOCUS       NP_001335195             315 aa            linear   PRI 27-APR-2025
DEFINITION  olfactory receptor 4K3 [Homo sapiens].
ACCESSION   NP_001335195
VERSION     NP_001335195.2
DBSOURCE    REFSEQ: accession NM_001348266.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Malnic,B., Godfrey,P.A. and Buck,L.B.
  TITLE     The human olfactory receptor gene family
  JOURNAL   Proc Natl Acad Sci U S A 101 (8), 2584-2589 (2004)
   PUBMED   14983052
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 May 4;101(18):7205]
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Menashe,I., Man,O., Lancet,D. and Gilad,Y.
  TITLE     Different noses for different people
  JOURNAL   Nat Genet 34 (2), 143-144 (2003)
   PUBMED   12730696
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Fuchs,T., Malecova,B., Linhart,C., Sharan,R., Khen,M., Herwig,R.,
            Shmulevich,D., Elkon,R., Steinfath,M., O'Brien,J.K., Radelof,U.,
            Lehrach,H., Lancet,D. and Shamir,R.
  TITLE     DEFOG: a practical scheme for deciphering families of genes
  JOURNAL   Genomics 80 (3), 295-302 (2002)
   PUBMED   12213199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AMYH02028810.1.
            
            On Nov 10, 2018 this sequence version replaced NP_001335195.1.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. This olfactory receptor gene is a
            segregating pseudogene, where some individuals have an allele that
            encodes a functional olfactory receptor, while other individuals
            have an allele encoding a protein that is predicted to be
            non-functional. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (1) represents the functional
            allele encoding the full-length protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: lack of evidence for use of
                                                upstream AUG
            polymorphic pseudogene           :: based on alignments, homology
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..315
                     /product="olfactory receptor 4K3"
                     /note="olfactory receptor, family 4, subfamily K, member 3
                     pseudogene; olfactory receptor OR14-14"
                     /calculated_mol_wt=35277
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96R72.3)"
     Region          25..291
                     /region_name="7tmA_OR4-like"
                     /note="olfactory receptor family 4 and related proteins,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15226"
                     /db_xref="CDD:320354"
     Region          26..52
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320354"
     Site            26..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R72.3)"
     Site            58..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R72.3)"
     Region          59..85
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320354"
     Site            order(81,84..85,97..102,104..105,108,153,155..159,195,
                     198..200,202..204,206..207,251,254..255,257..258,261,
                     265..266,268..270,273,276..277)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320354"
     Region          97..127
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320354"
     Site            101..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R72.3)"
     Region          140..161
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320354"
     Site            140..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R72.3)"
     Region          195..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320354"
     Site            196..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R72.3)"
     Region          231..261
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320354"
     Site            236..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R72.3)"
     Region          266..291
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320354"
     Site            270..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R72.3)"
     CDS             1..315
                     /gene="OR4K3"
                     /gene_synonym="OR14-10; OR4K3P"
                     /coded_by="NM_001348266.2:31..978"
                     /db_xref="GeneID:283617"
                     /db_xref="HGNC:HGNC:14731"
ORIGIN      
        1 mawsnqsavt efilrglsss lelqifyflf fsivyaatvl gnllivvtia sephlhspmy
       61 fllgnlsfid mslasfatpk miadflrehk aisfegcmtq mfflhllgga eivllismsf
      121 dryvaickpl hyltimsrrm cvglvilswi vgifhalsql aftvnlpfcg pnevdsffcd
      181 lplviklacv dtyilgvfmi stsgmialvc fillvisyti ilvtvrqrss ggsskalstc
      241 sahftvvtlf fgpctfiyvw pftnfpidkv lsvfytiytp llnpviytvr nkdvkysmrk
      301 lsshifksrk tdhtp
//
LOCUS       NP_000169                474 aa            linear   PRI 27-APR-2025
DEFINITION  glutathione synthetase [Homo sapiens].
ACCESSION   NP_000169
VERSION     NP_000169.1
DBSOURCE    REFSEQ: accession NM_000178.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Angelova,S., Salim,A., Kiselova-Kaneva,Y., Ivanova,D. and Peev,S.
  TITLE     Association of mRNA Levels of IL6, MMP-8, GSS in Saliva and
            Pyelonephritis in Children
  JOURNAL   Molecules 25 (1), 85 (2019)
   PUBMED   31881666
  REMARK    GeneRIF: Salivary IL-6, MMP-8 and GSS mRNA levels in combination
            with urine test analysis could be useful diagnostic tool for the
            very distributed disorder of pyelonephritis in childhood.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Strohkamp,S., Gemoll,T., Humborg,S., Hartwig,S., Lehr,S.,
            Freitag-Wolf,S., Becker,S., Franzen,B., Pries,R., Wollenberg,B.,
            Roblick,U.J., Bruch,H.P., Keck,T., Auer,G. and Habermann,J.K.
  TITLE     Protein levels of clusterin and glutathione synthetase in platelets
            allow for early detection of colorectal cancer
  JOURNAL   Cell Mol Life Sci 75 (2), 323-334 (2018)
   PUBMED   28849249
  REMARK    GeneRIF: Data suggest that the potential of clusterin and
            glutathione synthetase (GSH-S) as platelet biomarkers for early
            detection of colorectal cancer (CRC) could improve existing
            screening modalities in clinical application.
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Gunduz,M., Unal,O., Kavurt,S., Turk,E. and Mungan,N.O.
  TITLE     Clinical findings and effect of sodium hydrogen carbonate in
            patients with glutathione synthetase deficiency
  JOURNAL   J Pediatr Endocrinol Metab 29 (4), 481-485 (2016)
   PUBMED   26669244
  REMARK    GeneRIF: Mutation in Glutathione Synthase gene is associated with
            chronic metabolic acidosis in glutathione synthetase deficiency.
REFERENCE   5  (residues 1 to 474)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 474)
  AUTHORS   Gali,R.R. and Board,P.G.
  TITLE     Sequencing and expression of a cDNA for human glutathione
            synthetase
  JOURNAL   Biochem J 310 (Pt 1) (Pt 1), 353-358 (1995)
   PUBMED   7646467
REFERENCE   7  (residues 1 to 474)
  AUTHORS   Uhlig,S. and Wendel,A.
  TITLE     The physiological consequences of glutathione variations
  JOURNAL   Life Sci 51 (14), 1083-1094 (1992)
   PUBMED   1518371
  REMARK    Review article
REFERENCE   8  (residues 1 to 474)
  AUTHORS   Meister,A. and Anderson,M.E.
  TITLE     Glutathione
  JOURNAL   Annu Rev Biochem 52, 711-760 (1983)
   PUBMED   6137189
  REMARK    Review article
REFERENCE   9  (residues 1 to 474)
  AUTHORS   Rollins,D., Larsson,A., Steen,B., Krishnaswamy,K., Hagenfeldt,L.,
            Moldeus,P. and Rane,A.
  TITLE     Glutathione and gamma-glutamyl cycle enzymes in human fetal liver
  JOURNAL   J Pharmacol Exp Ther 217 (3), 697-700 (1981)
   PUBMED   6112263
REFERENCE   10 (residues 1 to 474)
  AUTHORS   Spielberg,S.P., Boxer,L.A., Oliver,J.M., Allen,J.M. and
            Schulman,J.D.
  TITLE     Oxidative damage to neutrophils in glutathione synthetase
            deficiency
  JOURNAL   Br J Haematol 42 (2), 215-223 (1979)
   PUBMED   465367
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU076581.1, BC007927.1 and
            AL133324.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Glutathione is important for a variety of biological
            functions, including protection of cells from oxidative damage by
            free radicals, detoxification of xenobiotics, and membrane
            transport. The protein encoded by this gene functions as a
            homodimer to catalyze the second step of glutathione biosynthesis,
            which is the ATP-dependent conversion of
            gamma-L-glutamyl-L-cysteine to glutathione. Defects in this gene
            are a cause of glutathione synthetase deficiency. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.73296.1,
                                           SRR3476690.360308.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000651619.1/ ENSP00000498303.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..474
                     /product="glutathione synthetase"
                     /EC_number="6.3.2.3"
                     /note="GSH synthetase; glutathione synthase; GSH-S"
                     /calculated_mol_wt=52254
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P48637.1)"
     Region          6..474
                     /region_name="eu-GS"
                     /note="Eukaryotic Glutathione Synthetase (eu-GS);
                     catalyses the production of glutathione from
                     gamma-glutamylcysteine and glycine in an ATP-dependent
                     manner. Belongs to the ATP-grasp superfamily; cd00228"
                     /db_xref="CDD:238140"
     Site            order(6..10,12..25,31..34,43..47)
                     /site_type="active"
                     /note="dimerization unit [active]"
                     /db_xref="CDD:238140"
     Site            order(125,149,151,214,216,220,267,270,450,461..462)
                     /site_type="other"
                     /note="glutathione (GSH) binding pocket [chemical
                     binding]"
                     /db_xref="CDD:238140"
     Site            order(125,151,369,450)
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:238140"
     Site            order(129,143,305,362,364,370,373,375,398..401,425,452)
                     /site_type="other"
                     /note="ATP binding pocket [chemical binding]"
                     /db_xref="CDD:238140"
     Site            order(144,146,368)
                     /site_type="other"
                     /note="magnesium binding site [ion binding]"
                     /db_xref="CDD:238140"
     Site            366..376
                     /site_type="active"
                     /note="glycine rich loop [active]"
                     /db_xref="CDD:238140"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P48637.1)"
     Site            454..466
                     /site_type="other"
                     /note="alanine rich loop"
                     /db_xref="CDD:238140"
     CDS             1..474
                     /gene="GSS"
                     /gene_synonym="CNSHA6; GSHS; HEL-S-64p; HEL-S-88n"
                     /coded_by="NM_000178.4:89..1513"
                     /db_xref="CCDS:CCDS13245.1"
                     /db_xref="GeneID:2937"
                     /db_xref="HGNC:HGNC:4624"
                     /db_xref="MIM:601002"
ORIGIN      
        1 matnwgsllq dkqqleelar qavdralaeg vllrtsqept ssevvsyapf tlfpslvpsa
       61 lleqayavqm dfnllvdavs qnaafleqtl sstikqddft arlfdihkqv lkegiaqtvf
      121 lglnrsdymf qrsadgspal kqieintisa sfgglasrtp avhrhvlsvl sktkeagkil
      181 snnpskglal giakawelyg spnalvllia qekernifdq raienellar nihvirrtfe
      241 disekgsldq drrlfvdgqe iavvyfrdgy mprqyslqnw earlllersh aakcpdiatq
      301 lagtkkvqqe lsrpgmleml lpgqpeavar lratfaglys ldvgeegdqa iaealaapsr
      361 fvlkpqregg gnnlygeemv qalkqlkdse erasyilmek iepepfencl lrpgsparvv
      421 qciselgifg vyvrqektlv mnkhvghllr tkaiehadgg vaagvavldn pypv
//
LOCUS       NP_620410                241 aa            linear   PRI 27-APR-2025
DEFINITION  homeobox protein TGIF2LX [Homo sapiens].
ACCESSION   NP_620410
VERSION     NP_620410.3
DBSOURCE    REFSEQ: accession NM_138960.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Tabarestani,F.O., Akbari,A., Karizi,S.Z. and
            Sotoodehnejadnematalahi,F.
  TITLE     Regulation of long non-coding RNAs XIST and ROR induced by
            homeodomain protein TGIF2LX in colorectal cancer
  JOURNAL   J Cancer Res Ther 18 (Supplement), S359-S366 (2022)
   PUBMED   36510989
  REMARK    GeneRIF: Regulation of long non-coding RNAs XIST and ROR induced by
            homeodomain protein TGIF2LX in colorectal cancer.
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Mobini,G.R., Ghafari,A., Amanpour,S., Fateh,R., Ghahremani,M.H.,
            Muhammadnejad,S., Dehpour,A.R., Akbari,A., Hoseiniharouni,S.M.,
            Kazemirad,E., Bolhassani,M. and Heidari,M.
  TITLE     In vivo identification of novel TGIF2LX target genes in colorectal
            adenocarcinoma using the cDNA-AFLP method
  JOURNAL   Arab J Gastroenterol 19 (2), 65-70 (2018)
   PUBMED   29960902
  REMARK    GeneRIF: To the best of our knowledge, this is the first report
            that proposes Nir1, Nir2, and Fhit genes might be regulated by
            homeodomain protein TGIF2LX in colorectal adenocarcinoma cells.
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Lyons,P.A., Rayner,T.F., Trivedi,S., Holle,J.U., Watts,R.A.,
            Jayne,D.R., Baslund,B., Brenchley,P., Bruchfeld,A., Chaudhry,A.N.,
            Cohen Tervaert,J.W., Deloukas,P., Feighery,C., Gross,W.L.,
            Guillevin,L., Gunnarsson,I., Harper,L., Hruskova,Z., Little,M.A.,
            Martorana,D., Neumann,T., Ohlsson,S., Padmanabhan,S., Pusey,C.D.,
            Salama,A.D., Sanders,J.S., Savage,C.O., Segelmark,M.,
            Stegeman,C.A., Tesar,V., Vaglio,A., Wieczorek,S., Wilde,B.,
            Zwerina,J., Rees,A.J., Clayton,D.G. and Smith,K.G.
  TITLE     Genetically distinct subsets within ANCA-associated vasculitis
  JOURNAL   N Engl J Med 367 (3), 214-223 (2012)
   PUBMED   22808956
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Ousati Ashtiani,Z., Ayati,M., Modarresi,M.H., Raoofian,R., Sabah
            Goulian,B., Greene,W.K. and Heidari,M.
  TITLE     Association of TGIFLX/Y mRNA expression with prostate cancer
  JOURNAL   Med Oncol 26 (1), 73-77 (2009)
   PUBMED   18663611
  REMARK    GeneRIF: most prostate tumors (73.5%) express at least one of these
            genes (TGIFLX and TGIFLY), although different patterns of mRNA
            expression were observed. These results suggest an association of
            TGIFLX/Y expression with the progression of prostate cancer.
REFERENCE   7  (residues 1 to 241)
  AUTHORS   Aarabi,M., Ousati-Ashtiani,Z., Nazarian,A., Modarressi,M.H. and
            Heidari,M.
  TITLE     Association of TGIFLX/Y mRNA expression with azoospermia in
            infertile men
  JOURNAL   Mol Reprod Dev 75 (12), 1761-1766 (2008)
   PUBMED   18384077
  REMARK    GeneRIF: Association of TGIFLX/Y mRNA expression with azoospermia
            in infertile men.(
REFERENCE   8  (residues 1 to 241)
  AUTHORS   Ross,M.T., Grafham,D.V., Coffey,A.J., Scherer,S., McLay,K.,
            Muzny,D., Platzer,M., Howell,G.R., Burrows,C., Bird,C.P.,
            Frankish,A., Lovell,F.L., Howe,K.L., Ashurst,J.L., Fulton,R.S.,
            Sudbrak,R., Wen,G., Jones,M.C., Hurles,M.E., Andrews,T.D.,
            Scott,C.E., Searle,S., Ramser,J., Whittaker,A., Deadman,R.,
            Carter,N.P., Hunt,S.E., Chen,R., Cree,A., Gunaratne,P., Havlak,P.,
            Hodgson,A., Metzker,M.L., Richards,S., Scott,G., Steffen,D.,
            Sodergren,E., Wheeler,D.A., Worley,K.C., Ainscough,R.,
            Ambrose,K.D., Ansari-Lari,M.A., Aradhya,S., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Ballabio,A., Banerjee,R., Barker,G.E.,
            Barlow,K.F., Barrett,I.P., Bates,K.N., Beare,D.M., Beasley,H.,
            Beasley,O., Beck,A., Bethel,G., Blechschmidt,K., Brady,N.,
            Bray-Allen,S., Bridgeman,A.M., Brown,A.J., Brown,M.J., Bonnin,D.,
            Bruford,E.A., Buhay,C., Burch,P., Burford,D., Burgess,J.,
            Burrill,W., Burton,J., Bye,J.M., Carder,C., Carrel,L., Chako,J.,
            Chapman,J.C., Chavez,D., Chen,E., Chen,G., Chen,Y., Chen,Z.,
            Chinault,C., Ciccodicola,A., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S., Clerc-Blankenburg,K., Clifford,K., Cobley,V., Cole,C.G.,
            Conquer,J.S., Corby,N., Connor,R.E., David,R., Davies,J., Davis,C.,
            Davis,J., Delgado,O., Deshazo,D., Dhami,P., Ding,Y., Dinh,H.,
            Dodsworth,S., Draper,H., Dugan-Rocha,S., Dunham,A., Dunn,M.,
            Durbin,K.J., Dutta,I., Eades,T., Ellwood,M., Emery-Cohen,A.,
            Errington,H., Evans,K.L., Faulkner,L., Francis,F., Frankland,J.,
            Fraser,A.E., Galgoczy,P., Gilbert,J., Gill,R., Glockner,G.,
            Gregory,S.G., Gribble,S., Griffiths,C., Grocock,R., Gu,Y.,
            Gwilliam,R., Hamilton,C., Hart,E.A., Hawes,A., Heath,P.D.,
            Heitmann,K., Hennig,S., Hernandez,J., Hinzmann,B., Ho,S., Hoffs,M.,
            Howden,P.J., Huckle,E.J., Hume,J., Hunt,P.J., Hunt,A.R.,
            Isherwood,J., Jacob,L., Johnson,D., Jones,S., de Jong,P.J.,
            Joseph,S.S., Keenan,S., Kelly,S., Kershaw,J.K., Khan,Z.,
            Kioschis,P., Klages,S., Knights,A.J., Kosiura,A., Kovar-Smith,C.,
            Laird,G.K., Langford,C., Lawlor,S., Leversha,M., Lewis,L., Liu,W.,
            Lloyd,C., Lloyd,D.M., Loulseged,H., Loveland,J.E., Lovell,J.D.,
            Lozado,R., Lu,J., Lyne,R., Ma,J., Maheshwari,M., Matthews,L.H.,
            McDowall,J., McLaren,S., McMurray,A., Meidl,P., Meitinger,T.,
            Milne,S., Miner,G., Mistry,S.L., Morgan,M., Morris,S., Muller,I.,
            Mullikin,J.C., Nguyen,N., Nordsiek,G., Nyakatura,G., O'Dell,C.N.,
            Okwuonu,G., Palmer,S., Pandian,R., Parker,D., Parrish,J.,
            Pasternak,S., Patel,D., Pearce,A.V., Pearson,D.M., Pelan,S.E.,
            Perez,L., Porter,K.M., Ramsey,Y., Reichwald,K., Rhodes,S.,
            Ridler,K.A., Schlessinger,D., Schueler,M.G., Sehra,H.K.,
            Shaw-Smith,C., Shen,H., Sheridan,E.M., Shownkeen,R., Skuce,C.D.,
            Smith,M.L., Sotheran,E.C., Steingruber,H.E., Steward,C.A.,
            Storey,R., Swann,R.M., Swarbreck,D., Tabor,P.E., Taudien,S.,
            Taylor,T., Teague,B., Thomas,K., Thorpe,A., Timms,K., Tracey,A.,
            Trevanion,S., Tromans,A.C., d'Urso,M., Verduzco,D., Villasana,D.,
            Waldron,L., Wall,M., Wang,Q., Warren,J., Warry,G.L., Wei,X.,
            West,A., Whitehead,S.L., Whiteley,M.N., Wilkinson,J.E.,
            Willey,D.L., Williams,G., Williams,L., Williamson,A.,
            Williamson,H., Wilming,L., Woodmansey,R.L., Wray,P.W., Yen,J.,
            Zhang,J., Zhou,J., Zoghbi,H., Zorilla,S., Buck,D., Reinhardt,R.,
            Poustka,A., Rosenthal,A., Lehrach,H., Meindl,A., Minx,P.J.,
            Hillier,L.W., Willard,H.F., Wilson,R.K., Waterston,R.H., Rice,C.M.,
            Vaudin,M., Coulson,A., Nelson,D.L., Weinstock,G., Sulston,J.E.,
            Durbin,R., Hubbard,T., Gibbs,R.A., Beck,S., Rogers,J. and
            Bentley,D.R.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
REFERENCE   9  (residues 1 to 241)
  AUTHORS   Skaletsky,H., Kuroda-Kawaguchi,T., Minx,P.J., Cordum,H.S.,
            Hillier,L., Brown,L.G., Repping,S., Pyntikova,T., Ali,J., Bieri,T.,
            Chinwalla,A., Delehaunty,A., Delehaunty,K., Du,H., Fewell,G.,
            Fulton,L., Fulton,R., Graves,T., Hou,S.F., Latrielle,P.,
            Leonard,S., Mardis,E., Maupin,R., McPherson,J., Miner,T., Nash,W.,
            Nguyen,C., Ozersky,P., Pepin,K., Rock,S., Rohlfing,T., Scott,K.,
            Schultz,B., Strong,C., Tin-Wollam,A., Yang,S.P., Waterston,R.H.,
            Wilson,R.K., Rozen,S. and Page,D.C.
  TITLE     The male-specific region of the human Y chromosome is a mosaic of
            discrete sequence classes
  JOURNAL   Nature 423 (6942), 825-837 (2003)
   PUBMED   12815422
REFERENCE   10 (residues 1 to 241)
  AUTHORS   Blanco-Arias,P., Sargent,C.A. and Affara,N.A.
  TITLE     The human-specific Yp11.2/Xq21.3 homology block encodes a
            potentially functional testis-specific TGIF-like retroposon
  JOURNAL   Mamm Genome 13 (8), 463-468 (2002)
   PUBMED   12226713
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590041.9.
            
            On Aug 28, 2003 this sequence version replaced NP_620410.2.
            
            Summary: This gene encodes a member of the TALE/TGIF homeobox
            family of transcription factors. Testis-specific expression
            suggests that this gene may play a role in spermatogenesis. A
            homolog of this gene lies within the male specific region of
            chromosome Y, in a block of sequence that is thought to be the
            result of a large X-to-Y transposition. [provided by RefSeq, Jul
            2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.12168.1,
                                           SRR5189667.50511.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283891.6/ ENSP00000355119.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq21.31"
     Protein         1..241
                     /product="homeobox protein TGIF2LX"
                     /note="TGFB-induced factor 2-like, X-linked; TGIF-like on
                     the X; TGFB-induced factor 2-like protein, X-linked;
                     TGF-beta-induced transcription factor 2-like protein"
                     /calculated_mol_wt=26544
     Region          1..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUE1.1)"
     Site            order(51..55,57,77,83,96,98..99,102..103,105..107)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(53,56,99,102..103,106)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          69..107
                     /region_name="Homeobox_KN"
                     /note="Homeobox KN domain; pfam05920"
                     /db_xref="CDD:428673"
     Region          126..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUE1.1)"
     CDS             1..241
                     /gene="TGIF2LX"
                     /gene_synonym="TGIFLX"
                     /coded_by="NM_138960.4:83..808"
                     /db_xref="CCDS:CCDS14459.1"
                     /db_xref="GeneID:90316"
                     /db_xref="HGNC:HGNC:18570"
                     /db_xref="MIM:300411"
ORIGIN      
        1 meaaadgpae tqspvekdsp aktqspaqdt simsrnnadt grvlalpehk kkrkgnlpae
       61 svkilrdwmy khrfkaypse eekqmlsekt nlsllqisnw finarrrilp dmlqqrrndp
      121 iighktgkda hathlqstea svpaksgpsg pdnvqslplw plpkgqmsre kqpdpesaps
      181 qkltgiaqpk kkvkvsvtsp sspelvspee hadfssflll vdaavqraae lelekkqepn
      241 p
//
LOCUS       NP_035033                660 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear factor erythroid 2-related factor 3 [Mus musculus].
ACCESSION   NP_035033
VERSION     NP_035033.1
DBSOURCE    REFSEQ: accession NM_010903.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Nedomova,M., Haberecht-Muller,S., Moller,S., Venz,S.,
            Prochazkova,M., Prochazka,J., Sedlak,F., Chawengsaksophak,K.,
            Hammer,E., Kasparek,P., Adamek,M., Sedlacek,R., Konvalinka,J.,
            Kruger,E. and Grantz Saskova,K.
  TITLE     DDI2 protease controls embryonic development and inflammation via
            TCF11/NRF1
  JOURNAL   iScience 27 (10), 110893 (2024)
   PUBMED   39328932
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Munz,M., Bharioke,A., Kosche,G., Moreno-Juan,V., Brignall,A.,
            Rodrigues,T.M., Graff-Meyer,A., Ulmer,T., Haeuselmann,S.,
            Pavlinic,D., Ledergerber,N., Gross-Scherf,B., Rozsa,B., Krol,J.,
            Picelli,S., Cowan,C.S. and Roska,B.
  TITLE     Pyramidal neurons form active, transient, multilayered circuits
            perturbed by autism-associated mutations at the inception of
            neocortex
  JOURNAL   Cell 186 (9), 1930-1949 (2023)
   PUBMED   37071993
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Waku,T., Iwami,T., Masuda,H., Hirose,S., Aketa,I. and Kobayashi,A.
  TITLE     Nrf3 Functions Reversely as a Tumorigenic to an Antitumorigenic
            Transcription Factor in Obese Mice
  JOURNAL   Tohoku J Exp Med 259 (1), 1-8 (2022)
   PUBMED   36328531
  REMARK    GeneRIF: Nrf3 Functions Reversely as a Tumorigenic to an
            Antitumorigenic Transcription Factor in Obese Mice.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Du,H., Wang,Z., Guo,R., Yang,L., Liu,G., Zhang,Z., Xu,Z., Tian,Y.,
            Yang,Z., Li,X. and Chen,B.
  TITLE     Transcription factors Bcl11a and Bcl11b are required for the
            production and differentiation of cortical projection neurons
  JOURNAL   Cereb Cortex 32 (17), 3611-3632 (2022)
   PUBMED   34963132
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Saliba,J., Coutaud,B., Makhani,K., Epstein Roth,N., Jackson,J.,
            Park,J.Y., Gagnon,N., Costa,P., Jeyakumar,T., Bury,M.,
            Beauchemin,N., Mann,K.K. and Blank,V.
  TITLE     Loss of NFE2L3 protects against inflammation-induced colorectal
            cancer through modulation of the tumor microenvironment
  JOURNAL   Oncogene 41 (11), 1563-1575 (2022)
   PUBMED   35091681
  REMARK    GeneRIF: Loss of NFE2L3 protects against inflammation-induced
            colorectal cancer through modulation of the tumor microenvironment.
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Zhang,Y., Kobayashi,A., Yamamoto,M. and Hayes,J.D.
  TITLE     The Nrf3 transcription factor is a membrane-bound glycoprotein
            targeted to the endoplasmic reticulum through its N-terminal
            homology box 1 sequence
  JOURNAL   J Biol Chem 284 (5), 3195-3210 (2009)
   PUBMED   19047052
  REMARK    GeneRIF: data are presented suggesting that the NHB2 sequence in
            mouse Nrf3 may regulate the topology of the transcription factor
            within the ER membrane
REFERENCE   7  (residues 1 to 660)
  AUTHORS   Sankaranarayanan,K. and Jaiswal,A.K.
  TITLE     Nrf3 negatively regulates antioxidant-response element-mediated
            expression and antioxidant induction of NAD(P)H:quinone
            oxidoreductase1 gene
  JOURNAL   J Biol Chem 279 (49), 50810-50817 (2004)
   PUBMED   15385560
REFERENCE   8  (residues 1 to 660)
  AUTHORS   Funatsu,N., Inoue,T. and Nakamura,S.
  TITLE     Gene expression analysis of the late embryonic mouse cerebral
            cortex using DNA microarray: identification of several region- and
            layer-specific genes
  JOURNAL   Cereb Cortex 14 (9), 1031-1044 (2004)
   PUBMED   15142957
REFERENCE   9  (residues 1 to 660)
  AUTHORS   Derjuga,A., Gourley,T.S., Holm,T.M., Heng,H.H., Shivdasani,R.A.,
            Ahmed,R., Andrews,N.C. and Blank,V.
  TITLE     Complexity of CNC transcription factors as revealed by gene
            targeting of the Nrf3 locus
  JOURNAL   Mol Cell Biol 24 (8), 3286-3294 (2004)
   PUBMED   15060151
  REMARK    GeneRIF: Data show that Nrf3 null mice develop normally with no
            obvious phenotypic differences compared to wild-type animals, that
            they are fertile, and that gross anatomy as well as behavior appear
            normal.
REFERENCE   10 (residues 1 to 660)
  AUTHORS   Kobayashi,A., Ito,E., Toki,T., Kogame,K., Takahashi,S.,
            Igarashi,K., Hayashi,N. and Yamamoto,M.
  TITLE     Molecular cloning and functional characterization of a new Cap'n'
            collar family transcription factor Nrf3
  JOURNAL   J Biol Chem 274 (10), 6443-6452 (1999)
   PUBMED   10037736
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CJ045939.1, AK133935.1, AC154011.3 and AV237858.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC005416.1, AB013852.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849376
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 24.84 cM"
     Protein         1..660
                     /product="nuclear factor erythroid 2-related factor 3"
                     /note="nuclear factor erythroid 2-like 3; NFE2-related
                     factor 3; NF-E2-related factor 3"
                     /calculated_mol_wt=72576
     Region          120..214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTM4.1)"
     Region          538..605
                     /region_name="bZIP_NFE2-like"
                     /note="Basic leucine zipper (bZIP) domain of Nuclear
                     Factor, Erythroid-derived 2 (NFE2) and similar proteins: a
                     DNA-binding and dimerization domain; cd14720"
                     /db_xref="CDD:269868"
     Region          539..601
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269868"
     Region          543..562
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTM4.1)"
     Site            order(547..548,550..552,554..559,561..563)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269868"
     Site            order(562,565..566,569..570,572..573,576..577,579..580,
                     583..584,586..587,590..591,593..594)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269868"
     Region          566..573
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTM4.1)"
     CDS             1..660
                     /gene="Nfe2l3"
                     /gene_synonym="Nrf3"
                     /coded_by="NM_010903.2:239..2221"
                     /db_xref="CCDS:CCDS20134.1"
                     /db_xref="GeneID:18025"
                     /db_xref="MGI:MGI:1339958"
ORIGIN      
        1 mklpkpwwag ggllqltill slvglrvdld lflpppaaal weellplcpt rpasasnpfs
       61 asegwertpl lpakgrllhe vralgvpfip rtrvdawlvh svatgnadga hgllgtaass
      121 avgdggqsas agggdpraah ssplaaeeee ekaaeptaqv pdaggcgsqe ngmlreksea
      181 vdhssqqeen eegvsaqaks rqqskteehk macasareae kitearnesh lhwsdtsfsl
      241 edlfqllssq pehslegisv edippflssv cesvnssaqn inlsqaishd vnlheamlly
      301 pnntfrrdps arssqaqepf lqlnphtnpe qatpamslpp fdnqmrnlts qdllydldsn
      361 ifdginlmsl atgfsplevs qlfeepdsgl slnssynsts ltnsyriydg tvgynsdlqs
      421 lchdlgavgg cypephkhch mdhrtiagfh vslecqqvfh dhtyhlqsga septsesfaw
      481 seksqktsgc ldnpdrnlsr deqrakalhi pfsvdeivrm pvdsfnsmls ryyltdlqvs
      541 lirdirrrgk nkvaaqncrk rkldiilnle ddicnlqakk ealkneqtqc skaidimrqk
      601 lhglhqdvfn rlrddqgrpv npsqyalqys hdgtvlivpk elissghkke apkgkrerrn
//
LOCUS       NP_002895                380 aa            linear   PRI 27-APR-2025
DEFINITION  negative elongation factor E [Homo sapiens].
ACCESSION   NP_002895
VERSION     NP_002895.3
DBSOURCE    REFSEQ: accession NM_002904.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Zhang,J., Hu,Z., Chung,H.H., Tian,Y., Lau,K.W., Ser,Z., Lim,Y.T.,
            Sobota,R.M., Leong,H.F., Chen,B.J., Yeo,C.J., Tan,S.Y.X., Kang,J.,
            Tan,D.E.K., Sou,I.F., McClurg,U.L., Lakshmanan,M., Vaiyapuri,T.S.,
            Raju,A., Wong,E.S.M., Tergaonkar,V., Rajarethinam,R., Pathak,E.,
            Tam,W.L., Tan,E.Y. and Tee,W.W.
  TITLE     Dependency of NELF-E-SLUG-KAT2B epigenetic axis in breast cancer
            carcinogenesis
  JOURNAL   Nat Commun 14 (1), 2439 (2023)
   PUBMED   37117180
  REMARK    GeneRIF: Dependency of NELF-E-SLUG-KAT2B epigenetic axis in breast
            cancer carcinogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Chignon,A., Argaud,D., Boulanger,M.C., Mkannez,G., Bon-Baret,V.,
            Li,Z., Theriault,S., Bosse,Y. and Mathieu,P.
  TITLE     Genome-wide chromatin contacts of super-enhancer-associated lncRNA
            identify LINC01013 as a regulator of fibrosis in the aortic valve
  JOURNAL   PLoS Genet 18 (1), e1010010 (2022)
   PUBMED   35041643
  REMARK    GeneRIF: Genome-wide chromatin contacts of
            super-enhancer-associated lncRNA identify LINC01013 as a regulator
            of fibrosis in the aortic valve.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Yu,S., Li,L., Cai,H., He,B., Gao,Y. and Li,Y.
  TITLE     Overexpression of NELFE contributes to gastric cancer progression
            via Wnt/beta-catenin signaling-mediated activation of CSNK2B
            expression
  JOURNAL   J Exp Clin Cancer Res 40 (1), 54 (2021)
   PUBMED   33526068
  REMARK    GeneRIF: Overexpression of NELFE contributes to gastric cancer
            progression via Wnt/beta-catenin signaling-mediated activation of
            CSNK2B expression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Bishara,L.A., Machour,F.E., Awwad,S.W. and Ayoub,N.
  TITLE     NELF complex fosters BRCA1 and RAD51 recruitment to DNA damage
            sites and modulates sensitivity to PARP inhibition
  JOURNAL   DNA Repair (Amst) 97, 103025 (2021)
   PUBMED   33248388
  REMARK    GeneRIF: NELF complex fosters BRCA1 and RAD51 recruitment to DNA
            damage sites and modulates sensitivity to PARP inhibition.
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Lee,S.G. and Song,K.
  TITLE     Genomic organization of the human DDX13 gene located between RD and
            RP1 in the class III MHC complex
  JOURNAL   Mol Cells 7 (3), 414-418 (1997)
   PUBMED   9264031
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Cheng,J., Macon,K.J. and Volanakis,J.E.
  TITLE     cDNA cloning and characterization of the protein encoded by RD, a
            gene located in the class III region of the human major
            histocompatibility complex
  JOURNAL   Biochem J 294 (Pt 2) (Pt 2), 589-593 (1993)
   PUBMED   8373374
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Surowy,C.S., Hoganson,G., Gosink,J., Strunk,K. and Spritz,R.A.
  TITLE     The human RD protein is closely related to nuclear RNA-binding
            proteins and has been highly conserved
  JOURNAL   Gene 90 (2), 299-302 (1990)
   PUBMED   2119325
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Speiser,P.W. and White,P.C.
  TITLE     Structure of the human RD gene: a highly conserved gene in the
            class III region of the major histocompatibility complex
  JOURNAL   DNA 8 (10), 745-751 (1989)
   PUBMED   2612324
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Levi-Strauss,M., Carroll,M.C., Steinmetz,M. and Meo,T.
  TITLE     A previously undetected MHC gene with an unusual periodic structure
  JOURNAL   Science 240 (4849), 201-204 (1988)
   PUBMED   3353717
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD579634.2, BC050617.2 and
            BU935034.1.
            
            On Jul 11, 2001 this sequence version replaced NP_002895.2.
            
            Summary: The protein encoded by this gene is part of a complex
            termed negative elongation factor (NELF) which represses RNA
            polymerase II transcript elongation. This protein bears similarity
            to nuclear RNA-binding proteins; however, it has not been
            demonstrated that this protein binds RNA. The protein contains a
            tract of alternating basic and acidic residues, largely arginine
            (R) and aspartic acid (D). The gene localizes to the major
            histocompatibility complex (MHC) class III region on chromosome 6.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.67520.1,
                                           SRR1163658.484386.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375429.8/ ENSP00000364578.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..380
                     /product="negative elongation factor E"
                     /note="RD RNA-binding protein; major histocompatibility
                     complex gene RD; negative elongation factor polypeptide E;
                     nuclear protein; RNA-binding protein RD"
                     /calculated_mol_wt=43109
     Region          30..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18615.3)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Region          79..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18615.3)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK9.
                     /evidence=ECO:0000305|PubMed:14701750,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Region          184..243
                     /region_name="30 X 2 AA approximate tandem repeats of
                     R-[DSNE]"
                     /note="propagated from UniProtKB/Swiss-Prot (P18615.3)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK9.
                     /evidence=ECO:0000305|PubMed:14701750,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK9.
                     /evidence=ECO:0000305|PubMed:14701750; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK9.
                     /evidence=ECO:0000305|PubMed:14701750; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P18615.3)"
     Region          258..332
                     /region_name="RRM_NELFE"
                     /note="RNA recognition motif in negative elongation factor
                     E (NELF-E) and similar proteins; cd12305"
                     /db_xref="CDD:409746"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P18615.3)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P18615.3)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P18615.3)"
     CDS             1..380
                     /gene="NELFE"
                     /gene_synonym="D6S45; NELF-E; RD; RDBP; RDP"
                     /coded_by="NM_002904.6:89..1231"
                     /db_xref="CCDS:CCDS4730.1"
                     /db_xref="GeneID:7936"
                     /db_xref="HGNC:HGNC:13974"
                     /db_xref="MIM:154040"
ORIGIN      
        1 mlvippglse eeealqkkfn klkkkkkall alkkqsssst tsqggvkrsl seqpvmdtat
       61 ateqakqlvk sgaisaikae tknsgfkrsr tlegklkdpe kgpvptfqpf qrsisadddl
      121 qessrrpqrk slyesfvsss drlrelgpdg eeaegpgagd gpprsfdwgy eersgahssa
      181 spprsrsrdr shernrdrdr drerdrdrdr drdrerdrdr drdrdrdrer drdrerdrdr
      241 dregpfrrsd sfperraprk gntlyvyged mtptllrgaf spfgniidls mdpprncafv
      301 tyekmesadq avaelngtqv esvqlkvnia rkqpmldaat gksvwgslav qnspkgchrd
      361 krtqivysdd vykenlvdgf
//
LOCUS       NP_055223                180 aa            linear   PRI 27-APR-2025
DEFINITION  trafficking protein particle complex subunit 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_055223
VERSION     NP_055223.1
DBSOURCE    REFSEQ: accession NM_014408.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Wang,Y., Anderson,E.P. and Tatakis,D.N.
  TITLE     Whole transcriptome analysis of smoker palatal mucosa identifies
            multiple downregulated innate immunity genes
  JOURNAL   J Periodontol 91 (6), 756-766 (2020)
   PUBMED   31682009
  REMARK    GeneRIF: TRAPPC3 expression in healthy human palatal mucosa is
            strongly negatively correlated with serum cotinine levels.
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Kummel,D., Muller,J.J., Roske,Y., Henke,N. and Heinemann,U.
  TITLE     Structure of the Bet3-Tpc6B core of TRAPP: two Tpc6 paralogs form
            trimeric complexes with Bet3 and Mum2
  JOURNAL   J Mol Biol 361 (1), 22-32 (2006)
   PUBMED   16828797
  REMARK    GeneRIF: The crystal structure of human Bet3-Tpc6B heterodimer
            presented here represents a core sub-complex in the assembly of
            TRAPP.
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Kim,M.S., Yi,M.J., Lee,K.H., Wagner,J., Munger,C., Kim,Y.G.,
            Whiteway,M., Cygler,M., Oh,B.H. and Sacher,M.
  TITLE     Biochemical and crystallographic studies reveal a specific
            interaction between TRAPP subunits Trs33p and Bet3p
  JOURNAL   Traffic 6 (12), 1183-1195 (2005)
   PUBMED   16262728
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Loh,E., Peter,F., Subramaniam,V.N. and Hong,W.
  TITLE     Mammalian Bet3 functions as a cytosolic factor participating in
            transport from the ER to the Golgi apparatus
  JOURNAL   J Cell Sci 118 (Pt 6), 1209-1222 (2005)
   PUBMED   15728249
  REMARK    GeneRIF: Bet3 functions as a cytosolic factor participating in
            transport from the ER to the Golgi apparatus
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Turnbull,A.P., Kummel,D., Prinz,B., Holz,C., Schultchen,J.,
            Lang,C., Niesen,F.H., Hofmann,K.P., Delbruck,H., Behlke,J.,
            Muller,E.C., Jarosch,E., Sommer,T. and Heinemann,U.
  TITLE     Structure of palmitoylated BET3: insights into TRAPP complex
            assembly and membrane localization
  JOURNAL   EMBO J 24 (5), 875-884 (2005)
   PUBMED   15692564
  REMARK    GeneRIF: crystal structure
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Kim,Y.G., Sohn,E.J., Seo,J., Lee,K.J., Lee,H.S., Hwang,I.,
            Whiteway,M., Sacher,M. and Oh,B.H.
  TITLE     Crystal structure of bet3 reveals a novel mechanism for Golgi
            localization of tethering factor TRAPP
  JOURNAL   Nat Struct Mol Biol 12 (1), 38-45 (2005)
   PUBMED   15608655
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Sacher,M., Jiang,Y., Barrowman,J., Scarpa,A., Burston,J., Zhang,L.,
            Schieltz,D., Yates,J.R. 3rd, Abeliovich,H. and Ferro-Novick,S.
  TITLE     TRAPP, a highly conserved novel complex on the cis-Golgi that
            mediates vesicle docking and fusion
  JOURNAL   EMBO J 17 (9), 2494-2503 (1998)
   PUBMED   9564032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG704657.1 and BC007662.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a component of the trafficking protein
            particle complex, which tethers transport vesicles to the cis-Golgi
            membrane. The encoded protein participates in the regulation of
            transport from the endoplasmic reticulum to the Golgi apparatus.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (1) encodes isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.30649.1,
                                           SRR5189655.48863.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373166.8/ ENSP00000362261.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..180
                     /product="trafficking protein particle complex subunit 3
                     isoform 1"
                     /note="trafficking protein particle complex 3"
                     /calculated_mol_wt=20143
     Region          15..169
                     /region_name="TRAPPC3_bet3"
                     /note="Bet3-TRAPPC3 subunit of the TRAPP complex; cd14942"
                     /db_xref="CDD:271345"
     Site            order(15..19,21..23,25..26,29,43,47,50..51,54..55,58,
                     85..86,88,109,130)
                     /site_type="other"
                     /note="TRS31 interface [polypeptide binding]"
                     /db_xref="CDD:271345"
     Site            order(19,55..56,59,65..69,73..74,77..78,82..83,86..87,
                     130..131,134..135,138..139,144)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:271345"
     Site            order(53..54,57..58,60..63,65,67,141)
                     /site_type="other"
                     /note="TRS23 interface [polypeptide binding]"
                     /db_xref="CDD:271345"
     CDS             1..180
                     /gene="TRAPPC3"
                     /gene_synonym="BET3"
                     /coded_by="NM_014408.5:109..651"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS404.1"
                     /db_xref="GeneID:27095"
                     /db_xref="HGNC:HGNC:19942"
                     /db_xref="MIM:610955"
ORIGIN      
        1 msrqanrgte skkmsselft ltygalvtql ckdyendedv nkqldkmgfn igvrliedfl
       61 arsnvgrchd fretadviak vafkmylgit psitnwspag defslilenn plvdfvelpd
      121 nhssliysnl lcgvlrgale mvqmaveakf vqdtlkgdgv teirmrfirr iednlpagee
//
LOCUS       NP_653322                222 aa            linear   PRI 27-APR-2025
DEFINITION  THAP domain-containing protein 6 isoform 1 [Homo sapiens].
ACCESSION   NP_653322
VERSION     NP_653322.1
DBSOURCE    REFSEQ: accession NM_144721.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Roussigne,M., Kossida,S., Lavigne,A.C., Clouaire,T., Ecochard,V.,
            Glories,A., Amalric,F. and Girard,J.P.
  TITLE     The THAP domain: a novel protein motif with similarity to the
            DNA-binding domain of P element transposase
  JOURNAL   Trends Biochem Sci 28 (2), 66-69 (2003)
   PUBMED   12575992
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC308535.1, AL833350.1, AC096759.3 and AI743405.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL833350.1, SRR1803613.90867.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311638.7/ ENSP00000309007.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.1"
     Protein         1..222
                     /product="THAP domain-containing protein 6 isoform 1"
                     /note="THAP domain-containing protein 6"
                     /calculated_mol_wt=25560
     Region          4..90
                     /region_name="THAP"
                     /note="The THAP domain is a putative DNA-binding domain
                     (DBD) and probably also binds a zinc ion; smart00980"
                     /db_xref="CDD:214951"
     Region          139..142
                     /region_name="HCFC1-binding motif (HBM).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBB0.1)"
     CDS             1..222
                     /gene="THAP6"
                     /coded_by="NM_144721.6:69..737"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3568.1"
                     /db_xref="GeneID:152815"
                     /db_xref="HGNC:HGNC:23189"
                     /db_xref="MIM:612535"
ORIGIN      
        1 mvkccsaigc asrclpnskl kgltfhvfpt denikrkwvl amkrldvnaa giwepkkgdv
       61 lcsrhfkktd fdrsapnikl kpgvipsifd spyhlqgkre klhcrknftl ktvpatnynh
      121 hlvgasscie efqsqfifeh sysvmdspkk lkhkldhvig eledtkeslr nvldrekrfq
      181 kslrktirel kdeclisqet anrldtfcwd ccqesieqdy is
//
LOCUS       NP_001073861             455 aa            linear   PRI 27-APR-2025
DEFINITION  DENN domain-containing protein 11 [Homo sapiens].
ACCESSION   NP_001073861 XP_001126074
VERSION     NP_001073861.1
DBSOURCE    REFSEQ: accession NM_001080392.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004918.1.
            
            On Jan 18, 2007 this sequence version replaced XP_001126074.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB032973.2, SRR12921934.1162421.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000536163.6/ ENSP00000445768.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..455
                     /product="DENN domain-containing protein 11"
                     /note="protein LCHN; predicted protein of HQ2561"
                     /calculated_mol_wt=51315
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4D1U4.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylvaline.
                     /evidence=ECO:0000269|PubMed:25489052; propagated from
                     UniProtKB/Swiss-Prot (A4D1U4.1)"
     Site            41
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (A4D1U4.1)"
     Region          80..347
                     /region_name="DENND11"
                     /note="DENN domain-containing protein 11; pfam09804"
                     /db_xref="CDD:430838"
     CDS             1..455
                     /gene="DENND11"
                     /gene_synonym="KIAA1147; LCHN; PRO2561"
                     /coded_by="NM_001080392.2:14..1381"
                     /db_xref="CCDS:CCDS47726.1"
                     /db_xref="GeneID:57189"
                     /db_xref="HGNC:HGNC:29472"
                     /db_xref="MIM:620122"
ORIGIN      
        1 mveqgdaapl lrwaegpavs lpqapqpqag gwgrggggga rpaaepprrr epeepaapev
       61 llqpgrlelg dveedqvvav fvvtfdprsg nmvewclpqd idlegvefks masgshkiqs
      121 dfiyfrkgpf fglacfanmp veselergar mksvgilsps ytllyrymhf lenqvrhqle
      181 mpghyshlaa fyedkkgvlh agpgrgsslp pvywlpsihr ymypemkith pagcmsqfik
      241 ffgeqililw kfallrkril ifspppvgvv cyrvyccccl anvslpgigg tipeskpffy
      301 vnvadiesle vevsyvactt ekifeekrel ydvyvdnqnv kthhdhlqpl lkinsadrek
      361 yrrlneqrqm llysqeveed ynpceedlfv lffleqnnri fqtllevsas qdktltaeha
      421 rgmgldpqgd rsflldllea ygidvmlvid npccp
//
LOCUS       NP_001129611             651 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor E2-alpha isoform E47 [Homo sapiens].
ACCESSION   NP_001129611 XP_016882671
VERSION     NP_001129611.1
DBSOURCE    REFSEQ: accession NM_001136139.4
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Collinson,R.J., Wilson,L., Boey,D., Ng,Z.Y., Mirzai,B., Chuah,H.S.,
            Howman,R., Grove,C.S., Malherbe,J.A.J., Leahy,M.F., Linden,M.D.,
            Fuller,K.A., Erber,W.N. and Guo,B.B.
  TITLE     Transcription factor 3 is dysregulated in megakaryocytes in
            myelofibrosis
  JOURNAL   Platelets 35 (1), 2304173 (2024)
   PUBMED   38303515
  REMARK    GeneRIF: Transcription factor 3 is dysregulated in megakaryocytes
            in myelofibrosis.
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Xie,W., Liu,W., Wang,L., Li,S., Liao,Z., Xu,H., Li,Y., Jiang,X. and
            Ren,C.
  TITLE     Embryonic stem cell related gene regulates alternative splicing of
            transcription factor 3 to maintain human embryonic stem cells'
            self-renewal and pluripotency
  JOURNAL   Stem Cells 42 (6), 540-553 (2024)
   PUBMED   38393342
  REMARK    GeneRIF: Embryonic stem cell related gene regulates alternative
            splicing of transcription factor 3 to maintain human embryonic stem
            cells' self-renewal and pluripotency.
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Li,Y., Li,R., Li,Y., Li,G., Zhao,Y., Mou,H., Chen,Y., Xiao,L. and
            Gong,K.
  TITLE     Transcription Factor TCF3 Promotes Macrophage-Mediated Inflammation
            and MMP Secretion in Abdominal Aortic Aneurysm by Regulating
            miR-143-5p /CCL20
  JOURNAL   J Cardiovasc Pharmacol 82 (6), 458-469 (2023)
   PUBMED   37721971
  REMARK    GeneRIF: Transcription Factor TCF3 Promotes Macrophage-Mediated
            Inflammation and MMP Secretion in Abdominal Aortic Aneurysm by
            Regulating miR-143-5p /CCL20.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Zhang,W., Nowotny,H., Theodoropoulou,M., Simon,J., Hemmer,C.M.,
            Bidlingmaier,M., Auer,M.K., Reincke,M., Uhlenhaut,H. and Reisch,N.
  TITLE     E47 as a novel glucocorticoid-dependent gene mediating lipid
            metabolism in patients with endogenous glucocorticoid excess
  JOURNAL   Front Endocrinol (Lausanne) 14, 1249863 (2023)
   PUBMED   38047107
  REMARK    GeneRIF: E47 as a novel glucocorticoid-dependent gene mediating
            lipid metabolism in patients with endogenous glucocorticoid excess.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Burmeister,T., Groger,D., Gokbuget,N., Spriewald,B., Starck,M.,
            Elmaagacli,A., Hoelzer,D., Keller,U. and Schwartz,S.
  TITLE     Molecular characterization of TCF3::PBX1 chromosomal breakpoints in
            acute lymphoblastic leukemia and their use for measurable residual
            disease assessment
  JOURNAL   Sci Rep 13 (1), 15167 (2023)
   PUBMED   37704696
  REMARK    GeneRIF: Molecular characterization of TCF3::PBX1 chromosomal
            breakpoints in acute lymphoblastic leukemia and their use for
            measurable residual disease assessment.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Chakraborty,T., Martin,J.F. and Olson,E.N.
  TITLE     Analysis of the oligomerization of myogenin and E2A products in
            vivo using a two-hybrid assay system
  JOURNAL   J Biol Chem 267 (25), 17498-17501 (1992)
   PUBMED   1325437
REFERENCE   7  (residues 1 to 651)
  AUTHORS   Inaba,T., Roberts,W.M., Shapiro,L.H., Jolly,K.W., Raimondi,S.C.,
            Smith,S.D. and Look,A.T.
  TITLE     Fusion of the leucine zipper gene HLF to the E2A gene in human
            acute B-lineage leukemia
  JOURNAL   Science 257 (5069), 531-534 (1992)
   PUBMED   1386162
REFERENCE   8  (residues 1 to 651)
  AUTHORS   Sommer,L., Hagenbuchle,O., Wellauer,P.K. and Strubin,M.
  TITLE     Nuclear targeting of the transcription factor PTF1 is mediated by a
            protein subunit that does not bind to the PTF1 cognate sequence
  JOURNAL   Cell 67 (5), 987-994 (1991)
   PUBMED   1720355
REFERENCE   9  (residues 1 to 651)
  AUTHORS   Lassar,A.B., Davis,R.L., Wright,W.E., Kadesch,T., Murre,C.,
            Voronova,A., Baltimore,D. and Weintraub,H.
  TITLE     Functional activity of myogenic HLH proteins requires
            hetero-oligomerization with E12/E47-like proteins in vivo
  JOURNAL   Cell 66 (2), 305-315 (1991)
   PUBMED   1649701
REFERENCE   10 (residues 1 to 651)
  AUTHORS   Hunger,S.P., Galili,N., Carroll,A.J., Crist,W.M., Link,M.P. and
            Cleary,M.L.
  TITLE     The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1
            coding sequences in acute lymphoblastic leukemias
  JOURNAL   Blood 77 (4), 687-693 (1991)
   PUBMED   1671560
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006274.1, CD674814.1,
            CD516687.1, BU528547.1, BG284440.1, M24404.1, AW028755.1,
            AC005321.1 and KC877695.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced XP_016882671.1.
            
            Summary: This gene encodes a member of the E protein (class I)
            family of helix-loop-helix transcription factors. E proteins
            activate transcription by binding to regulatory E-box sequences on
            target genes as heterodimers or homodimers, and are inhibited by
            heterodimerization with inhibitor of DNA-binding (class IV)
            helix-loop-helix proteins. E proteins play a critical role in
            lymphopoiesis, and the encoded protein is required for B and T
            lymphocyte development. Deletion of this gene or diminished
            activity of the encoded protein may play a role in lymphoid
            malignancies. This gene is also involved in several chromosomal
            translocations that are associated with lymphoid malignancies
            including pre-B-cell acute lymphoblastic leukemia (t(1;19), with
            PBX1), childhood leukemia (t(19;19), with TFPT) and acute leukemia
            (t(12;19), with ZNF384). Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene, and a
            pseudogene of this gene is located on the short arm of chromosome
            9. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (2) differs in the 3' UTR, lacks
            an exon and includes an alternate exon in the 3' coding region, but
            maintains the reading frame, compared to variant 1. The encoded
            isoform (E47, also known as Pan-1) is shorter than isoform E12.
            Variants 2 and 4 encode the same isoform (E47).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352441.308179.1,
                                           SRR14038191.1229519.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match :: ENST00000588136.7/ ENSP00000468487.1
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..651
                     /product="transcription factor E2-alpha isoform E47"
                     /note="VDR interacting repressor; transcription factor
                     E2-alpha; immunoglobulin transcription factor 1;
                     kappa-E2-binding factor; transcription factor ITF-1;
                     E2A-HLF fusion transcript protein; class B basic
                     helix-loop-helix protein 21; vitamin D
                     receptor-interacting repressor; negative vitamin D
                     response element-binding protein; helix-loop-helix protein
                     HE47; transcription factor 3 (E2A immunoglobulin enhancer
                     binding factors E12/E47); NOL1-TCF3 fusion"
                     /calculated_mol_wt=67134
     Region          538..611
                     /region_name="bHLH_E-protein_E47-like"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor E47 and similar proteins; cd18943"
                     /db_xref="CDD:381513"
     Site            order(548,552,554..556,558,563,584..585)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381513"
     Site            order(561..562,565..566,568..569,572,576,586,589,593,
                     595..597,599..600,602..604,606)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:381513"
     Site            order(561..562,565..566,568..569,572,576,586,589,593,596,
                     599..604)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381513"
     CDS             1..651
                     /gene="TCF3"
                     /gene_synonym="AGM8; AGM8A; AGM8B; bHLHb21; E2A; E47;
                     ITF1; p75; TCF-3; VDIR"
                     /coded_by="NM_001136139.4:356..2311"
                     /note="isoform E47 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45899.1"
                     /db_xref="GeneID:6929"
                     /db_xref="HGNC:HGNC:11633"
                     /db_xref="MIM:147141"
ORIGIN      
        1 mnqpqrmapv gtdkelsdll dfsmmfplpv tngkgrpasl agaqfggsgl edrpssgswg
       61 sgdqssssfd psrtfsegth fteshsslss stflgpglgg ksgergayas fgrdagvggl
      121 tqagflsgel alnspgplsp sgmkgtsqyy psysgssrrr aadgsldtqp kkvrkvppgl
      181 pssvyppssg edygrdatay psaktpssty papfyvadgs lhpsaelwsp pgqagfgpml
      241 gggssplplp pgsgpvgssg ssstfgglhq hermgyqlhg aevngglpsa ssfssapgat
      301 yggvsshtpp vsgadsllgs rgttagssgd algkalasiy spdhssnnfs sspstpvgsp
      361 qglagtsqwp ragapgalsp sydgglhglq skiedhldea ihvlrshavg tagdmhtllp
      421 ghgalasgft gpmslggrha glvggshped glagstslmh nhaalpsqpg tlpdlsrppd
      481 sysglgraga taaaseikre ekedeentsa adhseeekke lkaprartss tdevlsleek
      541 dlrdrerrma nnarervrvr dineafrelg rmcqmhlksd kaqtkllilq qavqvilgle
      601 qqvrernlnp kaaclkrree ekvsgvvgdp qmvlsaphpg lseahnpagh m
//
LOCUS       NP_001350072             352 aa            linear   ROD 27-APR-2025
DEFINITION  RING finger protein 215 isoform 2 precursor [Mus musculus].
ACCESSION   NP_001350072 XP_006514869
VERSION     NP_001350072.1
DBSOURCE    REFSEQ: accession NM_001363143.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL807825.5.
            
            On May 9, 2018 this sequence version replaced XP_006514869.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK154140.1, SRR7345562.2291286.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849378
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 2.89 cM"
     Protein         1..352
                     /product="RING finger protein 215 isoform 2 precursor"
                     /calculated_mol_wt=34524
     sig_peptide     1..45
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4534
     Region          298..347
                     /region_name="RING-H2_RNF215"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 215 (RNF215) and similar proteins; cd16670"
                     /db_xref="CDD:438332"
     CDS             1..352
                     /gene="Rnf215"
                     /gene_synonym="0610009J22Rik"
                     /coded_by="NM_001363143.1:114..1172"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:71673"
                     /db_xref="MGI:MGI:1918923"
ORIGIN      
        1 mgsadrpalr spslppppps ppsplllllp llplwlglmg pgaaadgsep atgegrggar
       61 svrvdvklpr qdalvlegvr igpedgpepl lggrlllmdv vdaeqeipvd gwiavayvgk
      121 eqvaqfhqen qgssqkaypk alvqqmrral flgasallll ilnhsvvrel dvsqlllrpv
      181 ivlhyssnvt klleallqsp cssygtpscl wpcscvqdlw frpngrrqdr tsrslearwe
      241 pdggsphtrs pwacktvaif fpqedlfkrr vvrrlaslkt rrcrlsraah slpepgtetc
      301 avcldyfcnk qwlrvlpckh efhrdcvdpw lmlqqtcplc kfnvlgnhys dd
//
LOCUS       NP_612380                432 aa            linear   PRI 27-APR-2025
DEFINITION  PC-esterase domain-containing protein 1B [Homo sapiens].
ACCESSION   NP_612380 XP_005269282
VERSION     NP_612380.1
DBSOURCE    REFSEQ: accession NM_138371.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Novel eukaryotic enzymes modifying cell-surface biopolymers
  JOURNAL   Biol Direct 5, 1 (2010)
   PUBMED   20056006
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC072670.1 and CR985281.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005269282.1.
            
            Summary: This gene encodes a protein that belongs to the
            GDSL/SGNH-like acyl-esterase family. Members of this family are
            hydrolases thought to function in modification of biopolymers on
            the cell surface. Alternate splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Jul
            2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072670.1, BM543579.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152719, SAMEA2161920
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000546455.6/ ENSP00000446688.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..432
                     /product="PC-esterase domain-containing protein 1B"
                     /note="family with sequence similarity 113, member B"
                     /calculated_mol_wt=49596
     Region          17..249
                     /region_name="SGNH_hydrolase"
                     /note="or GDSL_hydrolase, is a diverse family of lipases
                     and esterases. The tertiary fold of the enzyme is
                     substantially different from that of the alpha/beta
                     hydrolase family and unique among all known hydrolases;
                     its active site closely resembles the typical...; cl01053"
                     /db_xref="CDD:470049"
     Site            order(24,64,126,228,231)
                     /site_type="active"
                     /db_xref="CDD:238141"
     Site            order(24,228,231)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238141"
     Site            order(24,64,126)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238141"
     Region          264..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HM7.1)"
     Region          398..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HM7.1)"
     CDS             1..432
                     /gene="PCED1B"
                     /gene_synonym="FAM113B"
                     /coded_by="NM_138371.3:714..2012"
                     /db_xref="CCDS:CCDS8752.1"
                     /db_xref="GeneID:91523"
                     /db_xref="HGNC:HGNC:28255"
ORIGIN      
        1 millrasevr qllhnkfvvi lgdsvhravy kdlvlllqkd rlltpgqlra rgelnfeqde
       61 lvdggqrghm hnglnyrevr efrsdhhlvr fyfltrvysd ylqtilkelq sgehapdlvi
      121 mnsclwdisr ygpnswrsyl enlenlfqcl gqvlpescll vwntampvge evtggflppk
      181 lrrqkatflk nevvkanfhs atearkhnfd vldlhfhfrh arenlhwdgv hwngrvhrcl
      241 sqlllahvad awgvelphrh pvgewikkkk pgprvegppq anrnhpalpl spplpsptyr
      301 pllgfppqrl pllpllspqp pppilhhqgm prfpqgppda cfssdhtfqs dqfychsdvp
      361 ssahagffve dnfmvgpqlp mpffptpryq rpapvvhrgf gryrprgpyt pwgqrprpsk
      421 rrapanpepr pq
//
LOCUS       NP_001061                451 aa            linear   PRI 27-APR-2025
DEFINITION  tubulin gamma-1 chain [Homo sapiens].
ACCESSION   NP_001061 XP_945344 XP_949600 XP_949603
VERSION     NP_001061.2
DBSOURCE    REFSEQ: accession NM_001070.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Zhang,Y., Wang,Z.Z., Han,A.Q., Yang,M.Y., Zhu,L.X., Pan,F.M. and
            Wang,Y.
  TITLE     TuBG1 promotes hepatocellular carcinoma via ATR/P53-apoptosis and
            cycling pathways
  JOURNAL   Hepatobiliary Pancreat Dis Int 23 (2), 195-209 (2024)
   PUBMED   37806848
  REMARK    GeneRIF: TuBG1 promotes hepatocellular carcinoma via
            ATR/P53-apoptosis and cycling pathways.
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Malycheva,D. and Alvarado-Kristensson,M.
  TITLE     Centrosome Movements Are TUBG1-Dependent
  JOURNAL   Int J Mol Sci 24 (17), 13154 (2023)
   PUBMED   37685969
  REMARK    GeneRIF: Centrosome Movements Are TUBG1-Dependent.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Wang,Z.J., Dai,Z.Z., Hu,M.Z., Liu,J.N., Liang,H., Shen,M.M.,
            Zhu,S.J., Sheng,H.J., Gao,J., Huang,A.L. and Tang,K.F.
  TITLE     Upregulation of TUBG1 expression promotes hepatocellular carcinoma
            development
  JOURNAL   Med Oncol 40 (3), 96 (2023)
   PUBMED   36792863
  REMARK    GeneRIF: Upregulation of TUBG1 expression promotes hepatocellular
            carcinoma development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Batman,U., Deretic,J. and Firat-Karalar,E.N.
  TITLE     The ciliopathy protein CCDC66 controls mitotic progression and
            cytokinesis by promoting microtubule nucleation and organization
  JOURNAL   PLoS Biol 20 (7), e3001708 (2022)
   PUBMED   35849559
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Kapeller,R., Toker,A., Cantley,L.C. and Carpenter,C.L.
  TITLE     Phosphoinositide 3-kinase binds constitutively to
            alpha/beta-tubulin and binds to gamma-tubulin in response to
            insulin
  JOURNAL   J Biol Chem 270 (43), 25985-25991 (1995)
   PUBMED   7592789
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Rommens,J.M., Durocher,F., McArthur,J., Tonin,P., LeBlanc,J.F.,
            Allen,T., Samson,C., Ferri,L., Narod,S., Morgan,K. et al.
  TITLE     Generation of a transcription map at the HSD17B locus centromeric
            to BRCA1 at 17q21
  JOURNAL   Genomics 28 (3), 530-542 (1995)
   PUBMED   7490091
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Bahi-Buisson,N. and Maillard,C.
  TITLE     Tubulinopathies Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27010057
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Zheng,Y., Jung,M.K. and Oakley,B.R.
  TITLE     Gamma-tubulin is present in Drosophila melanogaster and Homo
            sapiens and is associated with the centrosome
  JOURNAL   Cell 65 (5), 817-823 (1991)
   PUBMED   1904010
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC000619.2 and BG167819.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_949600.1, XP_949603.1, XP_945344.1, NP_001061.1.
            
            Summary: This gene encodes a member of the tubulin superfamily. The
            encoded protein localizes to the centrosome where it binds to
            microtubules as part of a complex referred to as the gamma-tubulin
            ring complex. The protein mediates microtubule nucleation and is
            required for microtubule formation and progression of the cell
            cycle. A pseudogene of this gene is found on chromosome 7.
            [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.319742.1,
                                           SRR3476690.775721.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000251413.8/ ENSP00000251413.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..451
                     /product="tubulin gamma-1 chain"
                     /note="tubulin, gamma polypeptide; gamma-tubulin complex
                     component 1"
                     /calculated_mol_wt=51039
     Region          3..435
                     /region_name="gamma_tubulin"
                     /note="The gamma-tubulin family; cd02188"
                     /db_xref="CDD:276957"
     Site            order(3,47,133,252,254,258,261..262,264..265,330..331,
                     333..334,337..338,341,353..354,357..358,430,433..434)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:276957"
     Site            order(11..13,16,102,140,142..146,171,173,207,225,228..229)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:276957"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by BRSK1.
                     /evidence=ECO:0000250|UniProtKB:P83887; propagated from
                     UniProtKB/Swiss-Prot (P23258.2)"
     CDS             1..451
                     /gene="TUBG1"
                     /gene_synonym="CDCBM4; GCP-1; TUBG; TUBGCP1"
                     /coded_by="NM_001070.5:56..1411"
                     /db_xref="CCDS:CCDS11433.1"
                     /db_xref="GeneID:7283"
                     /db_xref="HGNC:HGNC:12417"
                     /db_xref="MIM:191135"
ORIGIN      
        1 mpreiitlql gqcgnqigfe fwkqlcaehg ispegiveef ategtdrkdv ffyqaddehy
       61 ipravlldle prvihsilns pyaklynpen iylsehggga gnnwasgfsq gekihedifd
      121 iidreadgsd slegfvlchs iaggtgsglg syllerlndr ypkklvqtys vfpnqdemsd
      181 vvvqpynsll tlkrltqnad cvvvldntal nriatdrlhi qnpsfsqinq lvstimsast
      241 ttlrypgymn ndligliasl iptprlhflm tgytplttdq svasvrkttv ldvmrrllqp
      301 knvmvstgrd rqtnhcyiai lniiqgevdp tqvhkslqri rerklanfip wgpasiqval
      361 srkspylpsa hrvsglmman htsisslfer tcrqydklrk reafleqfrk edmfkdnfde
      421 mdtsreivqq lideyhaatr pdyiswgtqe q
//
LOCUS       NP_001348946             789 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-regulated phosphoprotein 21 isoform 4 [Mus musculus].
ACCESSION   NP_001348946 XP_017169149
VERSION     NP_001348946.1
DBSOURCE    REFSEQ: accession NM_001362017.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Xu,M., Ito-Kureha,T., Kang,H.S., Chernev,A., Raj,T., Hoefig,K.P.,
            Hohn,C., Giesert,F., Wang,Y., Pan,W., Zietara,N., Straub,T.,
            Feederle,R., Daniel,C., Adler,B., Konig,J., Feske,S., Tsokos,G.C.,
            Wurst,W., Urlaub,H., Sattler,M., Kisielow,J., Wulczyn,F.G.,
            Lyszkiewicz,M. and Heissmeyer,V.
  TITLE     The thymocyte-specific RNA-binding protein Arpp21 provides TCR
            repertoire diversity by binding to the 3'-UTR and promoting Rag1
            mRNA expression
  JOURNAL   Nat Commun 15 (1), 2194 (2024)
   PUBMED   38467629
  REMARK    GeneRIF: The thymocyte-specific RNA-binding protein Arpp21 provides
            TCR repertoire diversity by binding to the 3'-UTR and promoting
            Rag1 mRNA expression.
            Erratum:[Nat Commun. 2024 Aug 5;15(1):6632. doi:
            10.1038/s41467-024-50610-8. PMID: 39103338]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   3  (residues 1 to 789)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 789)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 789)
  AUTHORS   Tan,Y.Y., Zhang,Y., Li,B., Ou,Y.W., Xie,S.J., Chen,P.P., Mei,S.Q.,
            Huang,Q.J., Zheng,L.L. and Qu,L.H.
  TITLE     PERK Signaling Controls Myoblast Differentiation by Regulating
            MicroRNA Networks
  JOURNAL   Front Cell Dev Biol 9, 670435 (2021)
   PUBMED   34124052
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 789)
  AUTHORS   Rakhilin,S.V., Olson,P.A., Nishi,A., Starkova,N.N., Fienberg,A.A.,
            Nairn,A.C., Surmeier,D.J. and Greengard,P.
  TITLE     A network of control mediated by regulator of
            calcium/calmodulin-dependent signaling
  JOURNAL   Science 306 (5696), 698-701 (2004)
   PUBMED   15499021
  REMARK    GeneRIF: Through a molecular mechanism that amplifies GPCR- &
            PKA-mediated signaling & attenuates GPCR- & PP2B-mediated
            signaling, RCS (ARPP-21) synergistically increases phosphorylation
            of key proteins whose phosphorylation is regulated by PKA and PP2B
            [RCS]
REFERENCE   7  (residues 1 to 789)
  AUTHORS   Kim,J., Lee,J., Yadav,N., Wu,Q., Carter,C., Richard,S., Richie,E.
            and Bedford,M.T.
  TITLE     Loss of CARM1 results in hypomethylation of thymocyte cyclic
            AMP-regulated phosphoprotein and deregulated early T cell
            development
  JOURNAL   J Biol Chem 279 (24), 25339-25344 (2004)
   PUBMED   15096520
  REMARK    GeneRIF: CARM1 plays a significant role in promoting the
            differentiation of early thymocyte progenitors, possibly through
            its direct action on TARPP.
REFERENCE   8  (residues 1 to 789)
  AUTHORS   Kisielow,J., Nairn,A.C. and Karjalainen,K.
  TITLE     TARPP, a novel protein that accompanies TCR gene rearrangement and
            thymocyte education
  JOURNAL   Eur J Immunol 31 (4), 1141-1149 (2001)
   PUBMED   11298339
REFERENCE   9  (residues 1 to 789)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
REFERENCE   10 (residues 1 to 789)
  AUTHORS   Ivkovic,S., Blau,S., Polanskaya,O. and Ehrlich,M.E.
  TITLE     ARPP-21: murine gene structure and promoter identification of a
            neuronal phosphoprotein enriched in the limbic striatum
  JOURNAL   Brain Res 709 (1), 10-16 (1996)
   PUBMED   8869551
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100550.7 and AC130551.4.
            
            On Mar 31, 2018 this sequence version replaced XP_017169149.1.
            
            Transcript Variant: This variant (27), as well as variants 4, 26,
            and 28, encodes isoform 4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164131
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 62.46 cM"
     Protein         1..789
                     /product="cAMP-regulated phosphoprotein 21 isoform 4"
                     /note="cAMP-regulated phosphoprotein 21; thymocyte ARPP;
                     protein phosphatase 1, regulatory (inhibitory) subunit 1C;
                     regulator of calmodulin signaling; thymocyte
                     cAMP-regulated phosphoprotein"
                     /calculated_mol_wt=85487
     Region          162..223
                     /region_name="R3H_encore_like"
                     /note="R3H domain of encore-like and DIP1-like proteins.
                     Drosophila encore is involved in the germline exit after
                     four mitotic divisions, by facilitating
                     SCF-ubiquitin-proteasome-dependent proteolysis. Maize
                     DBF1-interactor protein 1 (DIP1) containing an R3H...;
                     cd02642"
                     /db_xref="CDD:100071"
     Site            order(195,199)
                     /site_type="other"
                     /note="RxxxH motif"
                     /db_xref="CDD:100071"
     Region          535..>764
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..789
                     /gene="Arpp21"
                     /gene_synonym="0710001E13Rik; ARPP-21; D9Bwg1012e; R3hdm3;
                     Tarpp"
                     /coded_by="NM_001362017.1:434..2803"
                     /note="isoform 4 is encoded by transcript variant 27"
                     /db_xref="CCDS:CCDS52944.1"
                     /db_xref="GeneID:74100"
                     /db_xref="MGI:MGI:107562"
ORIGIN      
        1 mseqggltpt ileegqtepe sapengilks esldeeekle lqrrlaaqnq errksksgag
       61 kgkltrslav ceessarsgg eshqdqesih lqlssfpslq eedksrkdds erekekdknr
      121 eklserpkir mlskdcsqey tdstgidlhg flintlknns rdrmillkme qemidfiads
      181 nnhykkfpqm ssyqrmlvhr vaayfgldhn vdqtgksvii nktsstripe qrfcehlkde
      241 kseesqkrfi lkrdnssidk ednqsvcsqe slfldnrahr dssgrtsgsr qsssetelrw
      301 pdhqrawsst dsdssnrnlk ptmtktasfg gitvltrgds tsstrsagkl sktgsessss
      361 agssgslsrt hpqstaltss vaagspgcma ysengmggqv ppsstsyill plesatgipp
      421 gsillnphtg qpfvnpdgtp aiynppgsqq tlrgtvggqp qqppqqqpsp qpqqqvqasq
      481 pqmagplvtq svqslqpssq svqypavsfp pqhllpmspt qhfplreela aqfsqlsmsr
      541 qssgdtpepp sgtvypasll pqtaqpqsyv itsagqqlst ggfsdsgppi sqqvlqapps
      601 pqgfvqqppp aqmsvyyyps gqyptstsqq yrplasvqys aqrsqqipqt tqqagyqpvl
      661 sgqqgfqgmm gvqqsahsqg vmssqqgapv hgvmvsyptm ssyqvpmtqg sqavpqqtyq
      721 ppimlpsqag qgslpatgmp vycnvtppnp qnnlrlmgph cpsstvpvms ascrtncgnv
      781 snagwqvkf
//
LOCUS       NP_001164047             136 aa            linear   ROD 27-APR-2025
DEFINITION  SNARE-associated protein Snapin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001164047
VERSION     NP_001164047.1
DBSOURCE    REFSEQ: accession NM_001170576.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Somanath,S., Partridge,C.J., Marshall,C., Rowe,T. and Turner,M.D.
  TITLE     Snapin mediates insulin secretory granule docking, but not
            trans-SNARE complex formation
  JOURNAL   Biochem Biophys Res Commun 473 (2), 403-407 (2016)
   PUBMED   26946359
  REMARK    GeneRIF: In pancreatic beta-cells the SNAP-25 accessory protein,
            snapin, C-terminal H2 domain binds SNAP-25 through its N-terminal
            Sn-1 domain.
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Pu,J., Schindler,C., Jia,R., Jarnik,M., Backlund,P. and
            Bonifacino,J.S.
  TITLE     BORC, a multisubunit complex that regulates lysosome positioning
  JOURNAL   Dev Cell 33 (2), 176-188 (2015)
   PUBMED   25898167
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Yun,H.J., Park,J., Ho,D.H., Kim,H., Kim,C.H., Oh,H., Ga,I., Seo,H.,
            Chang,S., Son,I. and Seol,W.
  TITLE     LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with
            SNAP-25
  JOURNAL   Exp Mol Med 45 (8), e36 (2013)
   PUBMED   23949442
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Kim,H.J., Zhong,Q., Sheng,Z.H., Yoshimori,T., Liang,C. and
            Jung,J.U.
  TITLE     Beclin-1-interacting autophagy protein Atg14L targets the
            SNARE-associated protein Snapin to coordinate endocytic trafficking
  JOURNAL   J Cell Sci 125 (Pt 20), 4740-4750 (2012)
   PUBMED   22797916
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Lee,H.H., Nemecek,D., Schindler,C., Smith,W.J., Ghirlando,R.,
            Steven,A.C., Bonifacino,J.S. and Hurley,J.H.
  TITLE     Assembly and architecture of biogenesis of lysosome-related
            organelles complex-1 (BLOC-1)
  JOURNAL   J Biol Chem 287 (8), 5882-5890 (2012)
   PUBMED   22203680
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Starcevic,M. and Dell'Angelica,E.C.
  TITLE     Identification of snapin and three novel proteins (BLOS1, BLOS2,
            and BLOS3/reduced pigmentation) as subunits of biogenesis of
            lysosome-related organelles complex-1 (BLOC-1)
  JOURNAL   J Biol Chem 279 (27), 28393-28401 (2004)
   PUBMED   15102850
REFERENCE   7  (residues 1 to 136)
  AUTHORS   Vites,O., Rhee,J.S., Schwarz,M., Rosenmund,C. and Jahn,R.
  TITLE     Reinvestigation of the role of snapin in neurotransmitter release
  JOURNAL   J Biol Chem 279 (25), 26251-26256 (2004)
   PUBMED   15084593
  REMARK    GeneRIF: snapin may not have a role as a SNARE regulator in
            neurotransmitter release, as had been previously thought [SNAPIN]
REFERENCE   8  (residues 1 to 136)
  AUTHORS   Buxton,P., Zhang,X.M., Walsh,B., Sriratana,A., Schenberg,I.,
            Manickam,E. and Rowe,T.
  TITLE     Identification and characterization of Snapin as a ubiquitously
            expressed SNARE-binding protein that interacts with SNAP23 in
            non-neuronal cells
  JOURNAL   Biochem J 375 (Pt 2), 433-440 (2003)
   PUBMED   12877659
REFERENCE   9  (residues 1 to 136)
  AUTHORS   Chheda,M.G., Ashery,U., Thakur,P., Rettig,J. and Sheng,Z.H.
  TITLE     Phosphorylation of Snapin by PKA modulates its interaction with the
            SNARE complex
  JOURNAL   Nat Cell Biol 3 (4), 331-338 (2001)
   PUBMED   11283605
REFERENCE   10 (residues 1 to 136)
  AUTHORS   Ilardi,J.M., Mochida,S. and Sheng,Z.H.
  TITLE     Snapin: a SNARE-associated protein implicated in synaptic
            transmission
  JOURNAL   Nat Neurosci 2 (2), 119-124 (1999)
   PUBMED   10195194
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY315040.1 and BC098864.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DY315040.1, CO401616.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..136
                     /product="SNARE-associated protein Snapin isoform 1"
                     /note="SNARE associated protein snapin;
                     synaptosomal-associated protein 25-binding protein; BLOC-1
                     subunit 7; biogenesis of lysosome-related organelles
                     complex 1 subunit 7"
                     /calculated_mol_wt=14773
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Region          23..110
                     /region_name="Snapin_Pallidin"
                     /note="Snapin/Pallidin; pfam14712"
                     /db_xref="CDD:464275"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:Q9Z266; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Region          83..136
                     /region_name="Interaction with TOR1A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P60192.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     CDS             1..136
                     /gene="Snapin"
                     /gene_synonym="Snapap"
                     /coded_by="NM_001170576.2:32..442"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:295217"
                     /db_xref="RGD:1560377"
ORIGIN      
        1 maaagsaavs gagtpvagpt grdlfaegll eflrpavqql dshvhavres qvelreqidn
       61 latelcrine dqkvaldldp yvkkllnarr rvvlvnnilq naqerlrrln hsvaketarr
      121 ramldsgvyp pgspsk
//
LOCUS       NP_001028313             230 aa            linear   ROD 27-APR-2025
DEFINITION  endothelial cell-specific chemotaxis regulator isoform 3 [Mus
            musculus].
ACCESSION   NP_001028313 XP_358515
VERSION     NP_001028313.1
DBSOURCE    REFSEQ: accession NM_001033141.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Zhu,Z., Zou,Q., Wang,C., Li,D., Yang,Y., Xiao,Y., Jin,Y., Yan,J.,
            Luo,L., Sun,Y. and Liang,X.
  TITLE     Isl Identifies the Extraembryonic Mesodermal/Allantois Progenitors
            and is Required for Placenta Morphogenesis and Vasculature
            Formation
  JOURNAL   Adv Sci (Weinh) 11 (32), e2400238 (2024)
   PUBMED   38923264
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Ahuja,N., Hiltabidle,M.S., Rajasekhar,H., Voss,S., Lu,S.Z.,
            Barlow,H.R., Cowdin,M.A., Daniel,E., Vaddaraju,V., Anandakumar,T.,
            Black,E., Cleaver,O. and Maynard,C.
  TITLE     Endothelial Cyp26b1 restrains murine heart valve growth during
            development
  JOURNAL   Dev Biol 486, 81-95 (2022)
   PUBMED   35364055
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Chen,X., Wang,L., Huang,R., Qiu,H., Wang,P., Wu,D., Zhu,Y.,
            Ming,J., Wang,Y., Wang,J. and Na,J.
  TITLE     Dgcr8 deletion in the primitive heart uncovered novel microRNA
            regulating the balance of cardiac-vascular gene program
  JOURNAL   Protein Cell 10 (5), 327-346 (2019)
   PUBMED   30128894
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Wu,W., Shi,C., Ma,F., Balducci,J., Huang,H., Ji,H.L., Chang,Y. and
            Huang,Y.
  TITLE     Structural and functional characterization of two alternative
            splicing variants of mouse Endothelial Cell-Specific Chemotaxis
            Regulator (ECSCR)
  JOURNAL   Int J Mol Sci 13 (4), 4920-4936 (2012)
   PUBMED   22606020
  REMARK    GeneRIF: two mouse ECSCR splicing variants/isoform precursors exist
            and are differentially expressed in a variety of tissue types and
            likely involved in modulation of vascular Endothelial cell
            migration.
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Koide,M., Ikeda,K., Akakabe,Y., Kitamura,Y., Ueyama,T., Matoba,S.,
            Yamada,H., Okigaki,M. and Matsubara,H.
  TITLE     Apoptosis regulator through modulating IAP expression (ARIA)
            controls the PI3K/Akt pathway in endothelial and endothelial
            progenitor cells
  JOURNAL   Proc Natl Acad Sci U S A 108 (23), 9472-9477 (2011)
   PUBMED   21593423
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2015 May 5;112(18):E2411. doi:
            10.1073/pnas.1506580112. PMID: 25883266]
REFERENCE   8  (residues 1 to 230)
  AUTHORS   Verissimo,A.R., Herbert,J.M., Heath,V.L., Legg,J.A., Sheldon,H.,
            Andre,M., Swain,R.K. and Bicknell,R.
  TITLE     Functionally defining the endothelial transcriptome, from Robo4 to
            ECSCR
  JOURNAL   Biochem Soc Trans 37 (Pt 6), 1214-1217 (2009)
   PUBMED   19909249
REFERENCE   9  (residues 1 to 230)
  AUTHORS   Ikeda,K., Nakano,R., Uraoka,M., Nakagawa,Y., Koide,M., Katsume,A.,
            Minamino,K., Yamada,E., Yamada,H., Quertermous,T. and Matsubara,H.
  TITLE     Identification of ARIA regulating endothelial apoptosis and
            angiogenesis by modulating proteasomal degradation of cIAP-1 and
            cIAP-2
  JOURNAL   Proc Natl Acad Sci U S A 106 (20), 8227-8232 (2009)
   PUBMED   19416853
  REMARK    GeneRIF: ARIA was expressed in blood vessels during mouse
            embryogenesis, as well as in endothelial cells both in vitro and in
            vivo.
REFERENCE   10 (residues 1 to 230)
  AUTHORS   Ma,F., Zhang,D., Yang,H., Sun,H., Wu,W., Gan,Y., Balducci,J.,
            Wei,Y.Q., Zhao,X. and Huang,Y.
  TITLE     Endothelial cell-specific molecule 2 (ECSM2) modulates actin
            remodeling and epidermal growth factor receptor signaling
  JOURNAL   Genes Cells 14 (3), 281-293 (2009)
   PUBMED   19267780
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132837.11.
            
            On Sep 16, 2005 this sequence version replaced XP_358515.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK157485.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 19.22 cM"
     Protein         1..230
                     /product="endothelial cell-specific chemotaxis regulator
                     isoform 3"
                     /note="endothelial cell-specific molecule 2; endothelial
                     cell-specific chemotaxis regulator; apoptosis regulator
                     through modulating IAP expression"
                     /calculated_mol_wt=24341
     Region          134..228
                     /region_name="ECSCR"
                     /note="Endothelial cell-specific chemotaxis regulator;
                     pfam15820"
                     /db_xref="CDD:292448"
     CDS             1..230
                     /gene="Ecscr"
                     /gene_synonym="1110006O17Rik; ARIA"
                     /coded_by="NM_001033141.2:82..774"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS37763.1"
                     /db_xref="GeneID:68545"
                     /db_xref="MGI:MGI:1915795"
ORIGIN      
        1 mlrdisleah glgstltpll ahqlpqgrvr gyssqptttq tsqeilqkss qvslvsnqpv
       61 tprsstmdkq slslpdlmsf qpqkhtlgpg tgtperssss ssssssrrge asldatpspe
      121 ttslqtkkmt illtilptpt sesvltvaaf gvisfivilv vvviilvsvv slrfkcrknk
      181 esedpqkpgs sglsescsta ngekdsitli smrninvnns kgsmsaekil
//
LOCUS       NP_001334349             209 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein bL21m isoform 2 [Mus musculus].
ACCESSION   NP_001334349 XP_006531840
VERSION     NP_001334349.1
DBSOURCE    REFSEQ: accession NM_001347420.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Cheong,A., Lingutla,R. and Mager,J.
  TITLE     Expression analysis of mammalian mitochondrial ribosomal protein
            genes
  JOURNAL   Gene Expr Patterns 38, 119147 (2020)
   PUBMED   32987154
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Easterday,M.C., Dougherty,J.D., Jackson,R.L., Ou,J., Nakano,I.,
            Paucar,A.A., Roobini,B., Dianati,M., Irvin,D.K., Weissman,I.L.,
            Terskikh,A.V., Geschwind,D.H. and Kornblum,H.I.
  TITLE     Neural progenitor genes. Germinal zone expression and analysis of
            genetic overlap in stem cell populations
  JOURNAL   Dev Biol 264 (2), 309-322 (2003)
   PUBMED   14651920
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL626765.22, BC028768.1 and AW050299.1.
            
            On Nov 26, 2016 this sequence version replaced XP_006531840.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB195624.1, BC028768.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 3.05 cM"
     Protein         1..209
                     /product="large ribosomal subunit protein bL21m isoform 2"
                     /note="39S ribosomal protein L21, mitochondrial; large
                     ribosomal subunit protein bL21m"
                     /calculated_mol_wt=19114
     transit_peptide 1..43
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9D1N9.1)"
                     /calculated_mol_wt=4270
     mat_peptide     44..209
                     /product="Large ribosomal subunit protein bL21m.
                     /id=PRO_0000252443"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D1N9.1)"
                     /calculated_mol_wt=19114
     Region          100..202
                     /region_name="Ribosomal_L21p"
                     /note="Ribosomal prokaryotic L21 protein; pfam00829"
                     /db_xref="CDD:459952"
     CDS             1..209
                     /gene="Mrpl21"
                     /gene_synonym="L21mt; MRP-L21"
                     /coded_by="NM_001347420.2:31..660"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS84406.1"
                     /db_xref="GeneID:353242"
                     /db_xref="MGI:MGI:2660674"
ORIGIN      
        1 maaaiaasal pgafgrlvsv csrsilasqg sgsaslwsas rrfnsqsasy pqgyvpktsl
       61 ssppwqevvl pdpveetrhh aevvkrvnel iatgqygrlf avvhfashqw kvtaedlili
      121 eneldikcge rirlekvllv gadnftllgk pllrkelvrv eatviektes wpkinmkfrk
      181 rknfrkkkii vnpqtilrin tieiaprll
//
LOCUS       NP_054768                621 aa            linear   PRI 27-APR-2025
DEFINITION  complex I assembly factor ACAD9, mitochondrial isoform 1 [Homo
            sapiens].
ACCESSION   NP_054768
VERSION     NP_054768.2
DBSOURCE    REFSEQ: accession NM_014049.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Brauer,N., Maruta,Y., Lisci,M., Strege,K., Oschlies,I.,
            Nakamura,H., Bohm,S., Lehmberg,K., Brandhoff,L., Ehl,S.,
            Parvaneh,N., Klapper,W., Fukuda,M., Griffiths,G.M., Hennies,H.C.,
            Niehues,T. and Ammann,S.
  TITLE     Immunodeficiency with susceptibility to lymphoma with complex
            genotype affecting energy metabolism (FBP1, ACAD9) and vesicle
            trafficking (RAB27A)
  JOURNAL   Front Immunol 14, 1151166 (2023)
   PUBMED   37388727
  REMARK    GeneRIF: Immunodeficiency with susceptibility to lymphoma with
            complex genotype affecting energy metabolism (FBP1, ACAD9) and
            vesicle trafficking (RAB27A).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Carroll,J., He,J., Ding,S., Fearnley,I.M. and Walker,J.E.
  TITLE     TMEM70 and TMEM242 help to assemble the rotor ring of human ATP
            synthase and interact with assembly factors for complex I
  JOURNAL   Proc Natl Acad Sci U S A 118 (13) (2021)
   PUBMED   33753518
REFERENCE   4  (residues 1 to 621)
  AUTHORS   Formosa,L.E., Muellner-Wong,L., Reljic,B., Sharpe,A.J.,
            Jackson,T.D., Beilharz,T.H., Stojanovski,D., Lazarou,M.,
            Stroud,D.A. and Ryan,M.T.
  TITLE     Dissecting the Roles of Mitochondrial Complex I Intermediate
            Assembly Complex Factors in the Biogenesis of Complex I
  JOURNAL   Cell Rep 31 (3), 107541 (2020)
   PUBMED   32320651
REFERENCE   5  (residues 1 to 621)
  AUTHORS   Leipnitz,G., Mohsen,A.W., Karunanidhi,A., Seminotti,B.,
            Roginskaya,V.Y., Markantone,D.M., Grings,M., Mihalik,S.J., Wipf,P.,
            Van Houten,B. and Vockley,J.
  TITLE     Evaluation of mitochondrial bioenergetics, dynamics, endoplasmic
            reticulum-mitochondria crosstalk, and reactive oxygen species in
            fibroblasts from patients with complex I deficiency
  JOURNAL   Sci Rep 8 (1), 1165 (2018)
   PUBMED   29348607
  REMARK    GeneRIF: Mutations in the ND6, NDUFV1 or ACAD9 genes are
            responsible for the mitochondrial complex I deficiency.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 621)
  AUTHORS   He,M., Rutledge,S.L., Kelly,D.R., Palmer,C.A., Murdoch,G.,
            Majumder,N., Nicholls,R.D., Pei,Z., Watkins,P.A. and Vockley,J.
  TITLE     A new genetic disorder in mitochondrial fatty acid beta-oxidation:
            ACAD9 deficiency
  JOURNAL   Am J Hum Genet 81 (1), 87-103 (2007)
   PUBMED   17564966
  REMARK    GeneRIF: We now report three cases of ACAD9 deficiency.
REFERENCE   7  (residues 1 to 621)
  AUTHORS   Oey,N.A., Ruiter,J.P., Ijlst,L., Attie-Bitach,T., Vekemans,M.,
            Wanders,R.J. and Wijburg,F.A.
  TITLE     Acyl-CoA dehydrogenase 9 (ACAD 9) is the long-chain acyl-CoA
            dehydrogenase in human embryonic and fetal brain
  JOURNAL   Biochem Biophys Res Commun 346 (1), 33-37 (2006)
   PUBMED   16750164
  REMARK    GeneRIF: acyl-CoA dehydrogenase 9 (ACAD 9)was identified as the
            long-chain ACAD in human embryonic and fetal brain and central
            nervous tissue, using in situ hybridization as well as enzymatic
            studies
REFERENCE   8  (residues 1 to 621)
  AUTHORS   Ensenauer,R., He,M., Willard,J.M., Goetzman,E.S., Corydon,T.J.,
            Vandahl,B.B., Mohsen,A.W., Isaya,G. and Vockley,J.
  TITLE     Human acyl-CoA dehydrogenase-9 plays a novel role in the
            mitochondrial beta-oxidation of unsaturated fatty acids
  JOURNAL   J Biol Chem 280 (37), 32309-32316 (2005)
   PUBMED   16020546
  REMARK    GeneRIF: ACAD9 may play a role in the turnover of lipid membrane
            unsaturated fatty acids that are essential for membrane integrity
            and structure
REFERENCE   9  (residues 1 to 621)
  AUTHORS   Oey,N.A., den Boer,M.E., Ruiter,J.P., Wanders,R.J., Duran,M.,
            Waterham,H.R., Boer,K., van der Post,J.A. and Wijburg,F.A.
  TITLE     High activity of fatty acid oxidation enzymes in human placenta:
            implications for fetal-maternal disease
  JOURNAL   J Inherit Metab Dis 26 (4), 385-392 (2003)
   PUBMED   12971426
  REMARK    GeneRIF: Very high activity of CPT2 and VCLAD, involved in the
            metabolism of long-chain fatty acids. Fatty acid oxidation may play
            role in energy generation in placenta, and deficiency in may result
            in placental dysfunction and gestational complications.
REFERENCE   10 (residues 1 to 621)
  AUTHORS   Zhang,J., Zhang,W., Zou,D., Chen,G., Wan,T., Zhang,M. and Cao,X.
  TITLE     Cloning and functional characterization of ACAD-9, a novel member
            of human acyl-CoA dehydrogenase family
  JOURNAL   Biochem Biophys Res Commun 297 (4), 1033-1042 (2002)
   PUBMED   12359260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA630022.1, BC013354.2 and
            BC007970.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_054768.1.
            
            Summary: This gene encodes a member of the acyl-CoA dehydrogenase
            family. Members of this family of proteins localize to the
            mitochondria and catalyze the rate-limiting step in the
            beta-oxidation of fatty acyl-CoA. The encoded protein is
            specifically active toward palmitoyl-CoA and long-chain unsaturated
            substrates. Mutations in this gene cause acyl-CoA dehydrogenase
            family member type 9 deficiency. Alternate splicing results in
            multiple transcript variants.[provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (1) encodes the functional
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007970.2, SRR1803614.183932.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000308982.12/
                                                  ENSP00000312618.7
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.3"
     Protein         1..621
                     /product="complex I assembly factor ACAD9, mitochondrial
                     isoform 1"
                     /EC_number="1.3.8.-"
                     /note="acyl-Coenzyme A dehydrogenase family, member 9;
                     very-long-chain acyl-CoA dehydrogenase VLCAD; complex I
                     assembly factor ACAD9, mitochondrial"
                     /calculated_mol_wt=64819
     transit_peptide 1..37
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:16020546; propagated from
                     UniProtKB/Swiss-Prot (Q9H845.1)"
                     /calculated_mol_wt=3960
     mat_peptide     38..621
                     /product="Complex I assembly factor ACAD9, mitochondrial.
                     /id=PRO_0000000524"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H845.1)"
                     /calculated_mol_wt=64819
     Region          38..445
                     /region_name="VLCAD"
                     /note="Very long chain acyl-CoA dehydrogenase; cd01161"
                     /db_xref="CDD:173850"
     Site            41
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H845.1)"
     Site            order(178,180..181,186..187,213,215,421,428,430)
                     /site_type="other"
                     /note="FAD binding site [chemical binding]"
                     /db_xref="CDD:173850"
     Site            order(187,293,300..301,304,425..426)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:173850"
     Site            426
                     /site_type="active"
                     /note="catalytic base [active]"
                     /db_xref="CDD:173850"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZN5; propagated from
                     UniProtKB/Swiss-Prot (Q9H845.1)"
     Site            521
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8JZN5; propagated from
                     UniProtKB/Swiss-Prot (Q9H845.1)"
     CDS             1..621
                     /gene="ACAD9"
                     /gene_synonym="MC1DN20; NPD002"
                     /coded_by="NM_014049.5:73..1938"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3053.1"
                     /db_xref="GeneID:28976"
                     /db_xref="HGNC:HGNC:21497"
                     /db_xref="MIM:611103"
ORIGIN      
        1 msgcglflrt taaaracrgl vvstanrrll rtsppvrafa kelflgkikk kevfpfpevs
       61 qdelneinqf lgpvekffte evdsrkidqe gkipdetlek lkslglfglq vpeeygglgf
      121 sntmysrlge iismdgsitv tlaahqaigl kgiilagtee qkakylpkla sgehiaafcl
      181 tepasgsdaa sirsratlse dkkhyilngs kvwitnggla niftvfakte vvdsdgsvkd
      241 kitafiverd fggvtngkpe dklgirgsnt cevhfentki pvenilgevg dgfkvamnil
      301 nsgrfsmgsv vagllkrlie mtaeyactrk qfnkrlsefg liqekfalma qkayvmesmt
      361 yltagmldqp gfpdcsieaa mvkvfsseaa wqcvsealqi lgglgytrdy pyerilrdtr
      421 illifegtne ilrmyialtg lqhagriltt rihelkqakv stvmdtvgrr lrdslgrtvd
      481 lgltgnhgvv hpsladsank feentycfgr tvetlllrfg ktimeeqlvl krvanilinl
      541 ygmtavlsra srsiriglrn hdhevllant fcveaylqnl fslsqldkya penldeqikk
      601 vsqqilekra yicahpldrt c
//
LOCUS       NP_001355075            2613 aa            linear   PRI 27-APR-2025
DEFINITION  teneurin-2 isoform 4 [Homo sapiens].
ACCESSION   NP_001355075 XP_016865156
VERSION     NP_001355075.1
DBSOURCE    REFSEQ: accession NM_001368146.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2613)
  AUTHORS   Vysokov,N.V., Silva,J.P., Lelianova,V.G., Suckling,J., Cassidy,J.,
            Blackburn,J.K., Yankova,N., Djamgoz,M.B., Kozlov,S.V.,
            Tonevitsky,A.G. and Ushkaryov,Y.A.
  TITLE     Proteolytically released Lasso/teneurin-2 induces axonal attraction
            by interacting with latrophilin-1 on axonal growth cones
  JOURNAL   Elife 7, e37935 (2018)
   PUBMED   30457553
  REMARK    GeneRIF: These findings reveal a novel mechanism of axonal
            pathfinding, whereby latrophilin-1 and Lasso mediate both
            short-range interaction that supports synaptogenesis, and
            long-range signaling that induces axonal attraction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2613)
  AUTHORS   Tews,D., Fromme,T., Keuper,M., Hofmann,S.M., Debatin,K.M.,
            Klingenspor,M., Wabitsch,M. and Fischer-Posovszky,P.
  TITLE     Teneurin-2 (TENM2) deficiency induces UCP1 expression in
            differentiating human fat cells
  JOURNAL   Mol Cell Endocrinol 443, 106-113 (2017)
   PUBMED   28088466
  REMARK    GeneRIF: TENM2 knockdown induces both UCP1 mRNA and protein
            expression upon adipogenic differentiation without affecting
            mitochondrial mass.
REFERENCE   3  (residues 1 to 2613)
  AUTHORS   Perry,J.R., Day,F., Elks,C.E., Sulem,P., Thompson,D.J.,
            Ferreira,T., He,C., Chasman,D.I., Esko,T., Thorleifsson,G.,
            Albrecht,E., Ang,W.Q., Corre,T., Cousminer,D.L., Feenstra,B.,
            Franceschini,N., Ganna,A., Johnson,A.D., Kjellqvist,S.,
            Lunetta,K.L., McMahon,G., Nolte,I.M., Paternoster,L., Porcu,E.,
            Smith,A.V., Stolk,L., Teumer,A., Tsernikova,N., Tikkanen,E.,
            Ulivi,S., Wagner,E.K., Amin,N., Bierut,L.J., Byrne,E.M.,
            Hottenga,J.J., Koller,D.L., Mangino,M., Pers,T.H.,
            Yerges-Armstrong,L.M., Zhao,J.H., Andrulis,I.L., Anton-Culver,H.,
            Atsma,F., Bandinelli,S., Beckmann,M.W., Benitez,J., Blomqvist,C.,
            Bojesen,S.E., Bolla,M.K., Bonanni,B., Brauch,H., Brenner,H.,
            Buring,J.E., Chang-Claude,J., Chanock,S., Chen,J.,
            Chenevix-Trench,G., Collee,J.M., Couch,F.J., Couper,D.,
            Coveillo,A.D., Cox,A., Czene,K., D'adamo,A.P., Smith,G.D., De
            Vivo,I., Demerath,E.W., Dennis,J., Devilee,P., Dieffenbach,A.K.,
            Dunning,A.M., Eiriksdottir,G., Eriksson,J.G., Fasching,P.A.,
            Ferrucci,L., Flesch-Janys,D., Flyger,H., Foroud,T., Franke,L.,
            Garcia,M.E., Garcia-Closas,M., Geller,F., de Geus,E.E., Giles,G.G.,
            Gudbjartsson,D.F., Gudnason,V., Guenel,P., Guo,S., Hall,P.,
            Hamann,U., Haring,R., Hartman,C.A., Heath,A.C., Hofman,A.,
            Hooning,M.J., Hopper,J.L., Hu,F.B., Hunter,D.J., Karasik,D.,
            Kiel,D.P., Knight,J.A., Kosma,V.M., Kutalik,Z., Lai,S.,
            Lambrechts,D., Lindblom,A., Magi,R., Magnusson,P.K., Mannermaa,A.,
            Martin,N.G., Masson,G., McArdle,P.F., McArdle,W.L., Melbye,M.,
            Michailidou,K., Mihailov,E., Milani,L., Milne,R.L., Nevanlinna,H.,
            Neven,P., Nohr,E.A., Oldehinkel,A.J., Oostra,B.A., Palotie,A.,
            Peacock,M., Pedersen,N.L., Peterlongo,P., Peto,J., Pharoah,P.D.,
            Postma,D.S., Pouta,A., Pylkas,K., Radice,P., Ring,S.,
            Rivadeneira,F., Robino,A., Rose,L.M., Rudolph,A., Salomaa,V.,
            Sanna,S., Schlessinger,D., Schmidt,M.K., Southey,M.C., Sovio,U.,
            Stampfer,M.J., Stockl,D., Storniolo,A.M., Timpson,N.J., Tyrer,J.,
            Visser,J.A., Vollenweider,P., Volzke,H., Waeber,G.,
            Waldenberger,M., Wallaschofski,H., Wang,Q., Willemsen,G.,
            Winqvist,R., Wolffenbuttel,B.H., Wright,M.J., Boomsma,D.I.,
            Econs,M.J., Khaw,K.T., Loos,R.J., McCarthy,M.I., Montgomery,G.W.,
            Rice,J.P., Streeten,E.A., Thorsteinsdottir,U., van Duijn,C.M.,
            Alizadeh,B.Z., Bergmann,S., Boerwinkle,E., Boyd,H.A., Crisponi,L.,
            Gasparini,P., Gieger,C., Harris,T.B., Ingelsson,E., Jarvelin,M.R.,
            Kraft,P., Lawlor,D., Metspalu,A., Pennell,C.E., Ridker,P.M.,
            Snieder,H., Sorensen,T.I., Spector,T.D., Strachan,D.P.,
            Uitterlinden,A.G., Wareham,N.J., Widen,E., Zygmunt,M., Murray,A.,
            Easton,D.F., Stefansson,K., Murabito,J.M. and Ong,K.K.
  CONSRTM   Australian Ovarian Cancer Study; GENICA Network; kConFab; LifeLines
            Cohort Study; InterAct Consortium; Early Growth Genetics (EGG)
            Consortium
  TITLE     Parent-of-origin-specific allelic associations among 106 genomic
            loci for age at menarche
  JOURNAL   Nature 514 (7520), 92-97 (2014)
   PUBMED   25231870
REFERENCE   4  (residues 1 to 2613)
  AUTHORS   Scannell Bryan,M., Argos,M., Pierce,B., Tong,L., Rakibuz-Zaman,M.,
            Ahmed,A., Rahman,M., Islam,T., Yunus,M., Parvez,F., Roy,S.,
            Jasmine,F., Baron,J.A., Kibriya,M.G. and Ahsan,H.
  TITLE     Genome-wide association studies and heritability estimates of body
            mass index related phenotypes in Bangladeshi adults
  JOURNAL   PLoS One 9 (8), e105062 (2014)
   PUBMED   25133637
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2613)
  AUTHORS   Tanaka,T., Ngwa,J.S., van Rooij,F.J., Zillikens,M.C.,
            Wojczynski,M.K., Frazier-Wood,A.C., Houston,D.K., Kanoni,S.,
            Lemaitre,R.N., Luan,J., Mikkila,V., Renstrom,F., Sonestedt,E.,
            Zhao,J.H., Chu,A.Y., Qi,L., Chasman,D.I., de Oliveira Otto,M.C.,
            Dhurandhar,E.J., Feitosa,M.F., Johansson,I., Khaw,K.T.,
            Lohman,K.K., Manichaikul,A., McKeown,N.M., Mozaffarian,D.,
            Singleton,A., Stirrups,K., Viikari,J., Ye,Z., Bandinelli,S.,
            Barroso,I., Deloukas,P., Forouhi,N.G., Hofman,A., Liu,Y.,
            Lyytikainen,L.P., North,K.E., Dimitriou,M., Hallmans,G.,
            Kahonen,M., Langenberg,C., Ordovas,J.M., Uitterlinden,A.G.,
            Hu,F.B., Kalafati,I.P., Raitakari,O., Franco,O.H., Johnson,A.,
            Emilsson,V., Schrack,J.A., Semba,R.D., Siscovick,D.S., Arnett,D.K.,
            Borecki,I.B., Franks,P.W., Kritchevsky,S.B., Lehtimaki,T.,
            Loos,R.J., Orho-Melander,M., Rotter,J.I., Wareham,N.J.,
            Witteman,J.C., Ferrucci,L., Dedoussis,G., Cupples,L.A. and
            Nettleton,J.A.
  TITLE     Genome-wide meta-analysis of observational studies shows common
            genetic variants associated with macronutrient intake
  JOURNAL   Am J Clin Nutr 97 (6), 1395-1402 (2013)
   PUBMED   23636237
REFERENCE   6  (residues 1 to 2613)
  AUTHORS   Vinatzer,U., Gollinger,M., Mullauer,L., Raderer,M., Chott,A. and
            Streubel,B.
  TITLE     Mucosa-associated lymphoid tissue lymphoma: novel translocations
            including rearrangements of ODZ2, JMJD2C, and CNN3
  JOURNAL   Clin Cancer Res 14 (20), 6426-6431 (2008)
   PUBMED   18927281
  REMARK    GeneRIF: Gene rearrangements of ODZ2 is associated with
            mucosa-associated lymphoid tissue lymphoma.
REFERENCE   7  (residues 1 to 2613)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   8  (residues 1 to 2613)
  AUTHORS   Bagutti,C., Forro,G., Ferralli,J., Rubin,B. and
            Chiquet-Ehrismann,R.
  TITLE     The intracellular domain of teneurin-2 has a nuclear function and
            represses zic-1-mediated transcription
  JOURNAL   J Cell Sci 116 (Pt 14), 2957-2966 (2003)
   PUBMED   12783990
  REMARK    GeneRIF: intracellular domain of teneurin-2 has a nuclear function
            and role in repressing zic-1-mediated transcription
REFERENCE   9  (residues 1 to 2613)
  AUTHORS   Ben-Zur,T., Feige,E., Motro,B. and Wides,R.
  TITLE     The mammalian Odz gene family: homologs of a Drosophila pair-rule
            gene with expression implying distinct yet overlapping
            developmental roles
  JOURNAL   Dev Biol 217 (1), 107-120 (2000)
   PUBMED   10625539
REFERENCE   10 (residues 1 to 2613)
  AUTHORS   Oohashi,T., Zhou,X.H., Feng,K., Richter,B., Morgelin,M.,
            Perez,M.T., Su,W.D., Chiquet-Ehrismann,R., Rauch,U. and Fassler,R.
  TITLE     Mouse ten-m/Odz is a new family of dimeric type II transmembrane
            proteins expressed in many tissues
  JOURNAL   J Cell Biol 145 (3), 563-577 (1999)
   PUBMED   10225957
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008634.5, AC093304.4, AC008464.7, AC008705.6, AC011369.4,
            AC008637.7 and AC026689.6.
            
            On Jan 17, 2019 this sequence version replaced XP_016865156.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145743,
                              SAMN03465403 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2613
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..2613
                     /product="teneurin-2 isoform 4"
                     /note="odd Oz/ten-m homolog 2; teneurin-2; neurestin
                     alpha; odz, odd Oz/ten-m homolog 2; tenascin-M2; protein
                     Odd Oz/ten-m homolog 2"
                     /calculated_mol_wt=289651
     Region          <10..222
                     /region_name="Ten_N"
                     /note="Teneurin Intracellular Region; pfam06484"
                     /db_xref="CDD:461932"
     Region          423..582
                     /region_name="DUF5885"
                     /note="Family of unknown function (DUF5885); pfam19232"
                     /db_xref="CDD:437064"
     Region          515..679
                     /region_name="Keratin_B2"
                     /note="Keratin, high sulfur B2 protein; pfam01500"
                     /db_xref="CDD:366678"
     Region          682..712
                     /region_name="acid_disulf_rpt"
                     /note="acidic double-disulfide repeat; NF033662"
                     /db_xref="CDD:411265"
     Region          1079..1409
                     /region_name="NHL"
                     /note="NHL repeat unit of beta-propeller proteins;
                     cl18310"
                     /db_xref="CDD:302697"
     Region          1079..1118
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1130..1173
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1197..1235
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1251..1292
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1315..1348
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1370..2306
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          1383..1409
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          2529..2606
                     /region_name="Tox-GHH"
                     /note="GHH signature containing HNH/Endo VII superfamily
                     nuclease toxin; pfam15636"
                     /db_xref="CDD:464783"
     CDS             1..2613
                     /gene="TENM2"
                     /gene_synonym="ODZ2; ten-2; TEN-M2; TEN2; TNM2"
                     /coded_by="NM_001368146.1:323..8164"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS93819.1"
                     /db_xref="GeneID:57451"
                     /db_xref="HGNC:HGNC:29943"
                     /db_xref="MIM:610119"
ORIGIN      
        1 mlhaankgrk psaeagrpip ptsspsllps aqlpsshnpp pvscqmplld sntshqimdt
       61 npdeefspns yllracsgpq qasssgppnh hsqstlrppl ppphnhtlsh hhssanslnr
      121 nsltnrrsqi hapapapndl attpesvqlq dswvlnsnvp letrhflfkt ssgstplfss
      181 sspgypltsg tvytppprll prntfsrkaf klkkpskycs wkcaalsaia aalllailla
      241 yfiamhllgl nwqlqpadgh tfnngirtgl pgnddvatmp sggkvpwslk nssidsgeae
      301 vgrrvtqevp pgvfwrsqih isqpqflkfn islgkdalfg vyirrglpps haqydfmerl
      361 dgkekwsvve sprerrsiqt lvqneavfvq yldvglwhla fyndgkdkem vsfntvvlds
      421 vqdcprnchg ngecvsgvch cfpgflgadc akaacpvlcs gngqyskgtc qcysgwkgae
      481 cdvpmnqcid pscgghgsci dgncvcsagy kgehceevdc ldptcsshgv cvngeclcsp
      541 gwgglncela rvqcpdqcsg hgtylpdtgl cscdpnwmgp dcsvevcsvd cgthgvcigg
      601 acrceegwtg aacdqrvchp rciehgtckd gkcecregwn gehctidgcp dlcngngrct
      661 lgqnswqcvc qtgwrgpgcn vametscadn kdnegdglvd cldpdcclqs acqnsllcrg
      721 srdpldiiqq gqtdwpavks fydrikllag kdsthiipge npfnsslvsl irgqvvttdg
      781 tplvgvnvsf vkypkygyti trqdgtfdli anggasltlh ferapfmsqe rtvwlpwnsf
      841 yamdtlvmkt eensipscdl sgfvrpdpii issplstffs aapgqnpivp etqvlheeie
      901 lpgsnvklry lssrtagyks llkitmtqst vplnlirvhl mvaveghlfq ksfqaspnla
      961 ytfiwdktda ygqrvyglsd avvsvgfeye tcpslilwek rtallqgfel dpsnlggwsl
     1021 dkhhilnvks gilhkgtgen qfltqqpaii tsimgngrrr siscpscngl aegnkllapv
     1081 alavgidgsl yvgdfnyirr ifpsrnvtsi lelrnkefkh snnpahkyyl avdpvsgsly
     1141 vsdtnsrriy rvkslsgtkd lagnsevvag tgeqclpfde arcgdggkai datlmsprgi
     1201 avdknglmyf vdatmirkvd qngiistllg sndltavrpl scdssmdvaq vrlewptdla
     1261 vnpmdnslyv lennvilrit enhqvsiiag rpmhcqvpgi dyslsklaih salesasaia
     1321 ishtgvlyit etdekkinrl rqvttngeic llagaasdcd ckndvncncy sgddayatda
     1381 ilnspsslav apdgtiyiad lgniriravs knkpvlnafn qyeaaspgeq elyvfnadgi
     1441 hqytvslvtg eylynftyst dndvtelidn ngnslkirrd ssgmprhllm pdnqiitltv
     1501 gtngglkvvs tqnlelglmt ydgntgllat ksdetgwttf ydydhegrlt nvtrptgvvt
     1561 slhremeksi tidiensnrd ddvtvitnls sveasytvvq dqvrnsyqlc nngtlrvmya
     1621 ngmgisfhse phvlagtitp tigrcnislp menglnsiew rlrkeqikgk vtifgrklrv
     1681 hgrnllsidy drnirtekiy ddhrkftlri iydqvgrpfl wlpssglaav nvsyffngrl
     1741 aglqrgamse rtdidkqgri vsrmfadgkv wsysyldksm vlllqsqrqy ifeydssdrl
     1801 lavtmpsvar hsmsthtsig yirniynppe snasvifdys ddgrilktsf lgtgrqvfyk
     1861 ygklsklsei vydstavtfg ydettgvlkm vnlqsggfsc tiryrkigpl vdkqiyrfse
     1921 egmvnarfdy tyhdnsfria sikpvisetp lpvdlyryde isgkvehfgk fgviyydinq
     1981 iittavmtls khfdthgrik evqyemfrsl mywmtvqyds mgrvikrelk lgpyanttky
     2041 tydydgdgql qsvavndrpt wrysydlngn lhllnpgnsv rlmplrydlr dritrlgdvq
     2101 ykidddgylc qrgsdifeyn skglltrayn kasgwsvqyr ydgvgrrasy ktnlghhlqy
     2161 fysdlhnptr ithvynhsns eitslyydlq ghlfamesss geeyyvasdn tgtplavfsi
     2221 nglmikqlqy taygeiyyds npdfqmvigf hgglydpltk lvhftqrdyd vlagrwtspd
     2281 ytmwknvgke papfnlymfk snnplsseld lknyvtdvks wlvmfgfqls niipgfprak
     2341 myfvpppyel sesqasengq litgvqqtte rhnqafmale gqvitkklha sirekaghwf
     2401 atttpiigkg imfaikegrv ttgvssiase dsrkvasvln nayyldkmhy siegkdthyf
     2461 vkigsadgdl vtlgttigrk vlesgvnvtv sqptllvngr trrftniefq ystlllsiry
     2521 gltpdtldee karvldqarq ralgtawake qqkardgreg srlwtegekq qllstgrvqg
     2581 yegyyvlpve qypeladsss niqflrqnem gkr
//
LOCUS       NP_003282               1249 aa            linear   PRI 27-APR-2025
DEFINITION  tripeptidyl-peptidase 2 isoform 1 [Homo sapiens].
ACCESSION   NP_003282
VERSION     NP_003282.2
DBSOURCE    REFSEQ: accession NM_003291.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1249)
  AUTHORS   Liao,C.L., Hu,R.C., Liao,M.S., Chen,Y.J., Chen,Y.P., Hsieh,H.H.,
            Tai,C.H., Chou,T.C., Chu,C.Y., Chen,Y.J., Lo,L.C. and Lin,J.J.
  TITLE     Unveiling a novel serpinB2-tripeptidyl peptidase II signaling axis
            during senescence
  JOURNAL   J Cell Sci 135 (10) (2022)
   PUBMED   35466366
  REMARK    GeneRIF: Unveiling a novel serpinB2-tripeptidyl peptidase II
            signaling axis during senescence.
REFERENCE   2  (residues 1 to 1249)
  AUTHORS   Atallah,I., Quinodoz,M., Campos-Xavier,B., Peter,V.G., Fouriki,A.,
            Bonvin,C., Bottani,A., Kumps,C., Angelini,F., Bellutti Enders,F.,
            Christen-Zaech,S., Rizzi,M., Renella,R., Beck-Popovic,M.,
            Poloni,C., Frossard,V., Blouin,J.L., Rivolta,C., Riccio,O.,
            Candotti,F., Hofer,M., Unger,S. and Superti-Furga,A.
  TITLE     Immune deficiency, autoimmune disease and intellectual disability:
            A pleiotropic disorder caused by biallelic variants in the TPP2
            gene
  JOURNAL   Clin Genet 99 (6), 780-788 (2021)
   PUBMED   33586135
  REMARK    GeneRIF: Immune deficiency, autoimmune disease and intellectual
            disability: A pleiotropic disorder caused by biallelic variants in
            the TPP2 gene.
REFERENCE   3  (residues 1 to 1249)
  AUTHORS   Lindas,A.C. and Tomkinson,B.
  TITLE     Characterization of the promoter of the gene encoding human
            tripeptidyl-peptidase II and identification of upstream silencer
            elements
  JOURNAL   Gene 393 (1-2), 62-69 (2007)
   PUBMED   17343995
  REMARK    GeneRIF: This investigation reveals that TPP II expression could be
            regulated through both positive and negative regulatory elements.
REFERENCE   4  (residues 1 to 1249)
  AUTHORS   York,I.A., Bhutani,N., Zendzian,S., Goldberg,A.L. and Rock,K.L.
  TITLE     Tripeptidyl peptidase II is the major peptidase needed to trim long
            antigenic precursors, but is not required for most MHC class I
            antigen presentation
  JOURNAL   J Immunol 177 (3), 1434-1443 (2006)
   PUBMED   16849449
  REMARK    GeneRIF: TPP2 plays a specialized role in antigen processing and
            one that is not essential for the generation of most presented
            peptides.
REFERENCE   5  (residues 1 to 1249)
  AUTHORS   Lindas,A.C. and Tomkinson,B.
  TITLE     Identification and characterization of the promoter for the gene
            encoding human tripeptidyl-peptidase II
  JOURNAL   Gene 345 (2), 249-257 (2005)
   PUBMED   15716107
  REMARK    GeneRIF: the promoter could be localized to a 215 bp fragment
            upstream of the initiation codon.
REFERENCE   6  (residues 1 to 1249)
  AUTHORS   Geier,E., Pfeifer,G., Wilm,M., Lucchiari-Hartz,M., Baumeister,W.,
            Eichmann,K. and Niedermann,G.
  TITLE     A giant protease with potential to substitute for some functions of
            the proteasome
  JOURNAL   Science 283 (5404), 978-981 (1999)
   PUBMED   9974389
REFERENCE   7  (residues 1 to 1249)
  AUTHORS   Tomkinson,B. and Jonsson,A.K.
  TITLE     Characterization of cDNA for human tripeptidyl peptidase II: the
            N-terminal part of the enzyme is similar to subtilisin
  JOURNAL   Biochemistry 30 (1), 168-174 (1991)
   PUBMED   1670990
REFERENCE   8  (residues 1 to 1249)
  AUTHORS   Tomkinson,B.
  TITLE     Nucleotide sequence of cDNA covering the N-terminus of human
            tripeptidyl peptidase II
  JOURNAL   Biomed Biochim Acta 50 (4-6), 727-729 (1991)
   PUBMED   1840501
REFERENCE   9  (residues 1 to 1249)
  AUTHORS   Tomkinson,B. and Zetterqvist,O.
  TITLE     Immunological cross-reactivity between human tripeptidyl peptidase
            II and fibronectin
  JOURNAL   Biochem J 267 (1), 149-154 (1990)
   PUBMED   1691635
REFERENCE   10 (residues 1 to 1249)
  AUTHORS   Tomkinson,B., Wernstedt,C., Hellman,U. and Zetterqvist,O.
  TITLE     Active site of tripeptidyl peptidase II from human erythrocytes is
            of the subtilisin type
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7508-7512 (1987)
   PUBMED   3313395
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU132468.1, BC039905.1,
            M73047.1, BF514671.1, N27441.1, DB303355.1 and BM684792.1.
            
            On Apr 30, 2008 this sequence version replaced NP_003282.1.
            
            Summary: This gene encodes a mammalian peptidase that, at neutral
            pH, removes tripeptides from the N terminus of longer peptides. The
            protein has a specialized function that is essential for some MHC
            class I antigen presentation. The protein is a high molecular mass
            serine exopeptidase; the amino acid sequence surrounding the serine
            residue at the active site is similar to the peptidases of the
            subtilisin class rather than the trypsin class. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shortest
            transcript and encodes the shortest, but most predominant, isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.207306.1,
                                           SRR1803611.74573.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1249
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q33.1"
     Protein         1..1249
                     /product="tripeptidyl-peptidase 2 isoform 1"
                     /EC_number="3.4.14.10"
                     /note="tripeptidyl-peptidase II; tripeptidyl
                     aminopeptidase"
                     /calculated_mol_wt=138219
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6;
                     propagated from UniProtKB/Swiss-Prot (P29144.4)"
     Region          14..489
                     /region_name="Peptidases_S8_Tripeptidyl_Aminopeptidase_II"
                     /note="Peptidase S8 family domain in Tripeptidyl
                     aminopeptidases_II; cd04857"
                     /db_xref="CDD:173796"
     Site            order(44,264,449)
                     /site_type="active"
                     /note="putative catalytic triad [active]"
                     /db_xref="CDD:173796"
     Site            order(190,264,328..330,362,449)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:173796"
     Site            401
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q64514; propagated from
                     UniProtKB/Swiss-Prot (P29144.4)"
     Region          777..963
                     /region_name="TPPII"
                     /note="Tripeptidyl peptidase II; pfam12580"
                     /db_xref="CDD:463636"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P29144.4)"
     Region          998..1018
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29144.4)"
     CDS             1..1249
                     /gene="TPP2"
                     /gene_synonym="IMD78; TPP-2; TPP-II; TPPII"
                     /coded_by="NM_003291.4:54..3803"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9502.1"
                     /db_xref="GeneID:7174"
                     /db_xref="HGNC:HGNC:12016"
                     /db_xref="MIM:190470"
ORIGIN      
        1 mataateepf pfhgllpkke tgaasflcry peydgrgvli avldtgvdpg apgmqvttdg
       61 kpkivdiidt tgsgdvntat evepkdgeiv glsgrvlkip aswtnpsgky higikngydf
      121 ypkalkeriq kerkekiwdp vhrvalaeac rkqeefdvan ngssqankli keelqsqvel
      181 lnsfekkysd pgpvydclvw hdgevwraci dsnedgdlsk stvlrnykea qeygsfgtae
      241 mlnysvniyd dgnllsivts ggahgthvas iaaghfpeep erngvapgaq ilsikigdtr
      301 lstmetgtgl iramievinh kcdlvnysyg eathwpnsgr icevineavw khniiyvssa
      361 gnngpclstv gcpggttssv igvgayvspd mmvaeyslre klpanqytws srgpsadgal
      421 gvsisapgga iasvpnwtlr gtqlmngtsm sspnacggia lilsglkann idytvhsvrr
      481 alentavkad nievfaqghg iiqvdkaydy lvqntsfank lgftvtvgnn rgiylrdpvq
      541 vaapsdhgvg iepvfpente nsekislqlh laltsnsswv qcpshlelmn qcrhinirvd
      601 prglreglhy tevcgydias pnagplfrvp itaviaakvn esshydlaft dvhfkpgqir
      661 rhfievpega twaevtvcsc ssevsakfvl havqlvkqra yrshefykfc slpekgtlte
      721 afpvlggkai efciarwwas lsdvnidyti sfhgivctap qlnihasegi nrfdvqsslk
      781 yedlapcitl knwvqtlrpv saktkplgsr dvlpnnrqly emvltynfhq pksgevtpsc
      841 pllcellyes efdsqlwiif dqnkrqmgsg dayphqyslk lekgdytirl qirheqisdl
      901 erlkdlpfiv shrlsntlsl dihenhsfal lgkkkssnlt lppkynqpff vtslpddkip
      961 kgagpgcyla gsltlsktel gkkadvipvh yylippptkt kngskdkekd sekekdlkee
     1021 ftealrdlki qwmtkldssd iynelketyp nylplyvarl hqldaekerm krlneivdaa
     1081 navishidqt alavyiamkt dprpdaatik ndmdkqkstl vdalcrkgca ladhllhtqa
     1141 qdgaistdae gkeeegespl dslaetfwet tkwtdlfdnk vltfaykhal vnkmygrglk
     1201 fatklveekp tkenwknciq lmkllgwthc asftenwlpi myppdycvf
//
LOCUS       NP_110382                280 aa            linear   PRI 27-APR-2025
DEFINITION  thioredoxin-related transmembrane protein 1 precursor [Homo
            sapiens].
ACCESSION   NP_110382
VERSION     NP_110382.3
DBSOURCE    REFSEQ: accession NM_030755.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Luo,N., Mei,Z., Zhang,Q., Tang,H., Wan,R., Deng,A., Zou,X. and
            Lv,C.
  TITLE     TMX family genes and their association with prognosis, immune
            infiltration, and chemotherapy in human pan-cancer
  JOURNAL   Aging (Albany NY) 15 (24), 15064-15083 (2023)
   PUBMED   38147024
  REMARK    GeneRIF: TMX family genes and their association with prognosis,
            immune infiltration, and chemotherapy in human pan-cancer.
            Erratum:[Aging (Albany NY). 2024 Jun 30;16(12):10666-10667. doi:
            10.18632/aging.205990. PMID: 38967984]
REFERENCE   2  (residues 1 to 280)
  AUTHORS   McLelland,G.L., Lopez-Osias,M., Verzijl,C.R.C., Ellenbroek,B.D.,
            Oliveira,R.A., Boon,N.J., Dekker,M., van den Hengel,L.G., Ali,R.,
            Janssen,H., Song,J.Y., Krimpenfort,P., van Zutphen,T., Jonker,J.W.
            and Brummelkamp,T.R.
  TITLE     Identification of an alternative triglyceride biosynthesis pathway
  JOURNAL   Nature 621 (7977), 171-178 (2023)
   PUBMED   37648867
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Gaspar,R.S. and Gibbins,J.M.
  TITLE     Thiol Isomerases Orchestrate Thrombosis and Hemostasis
  JOURNAL   Antioxid Redox Signal 35 (13), 1116-1133 (2021)
   PUBMED   33940944
  REMARK    GeneRIF: Thiol Isomerases Orchestrate Thrombosis and Hemostasis.
            Review article
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Lynes,E.M., Bui,M., Yap,M.C., Benson,M.D., Schneider,B.,
            Ellgaard,L., Berthiaume,L.G. and Simmen,T.
  TITLE     Palmitoylated TMX and calnexin target to the
            mitochondria-associated membrane
  JOURNAL   EMBO J 31 (2), 457-470 (2012)
   PUBMED   22045338
  REMARK    GeneRIF: TMX1 is enriched on the mitochondria-associated membrane.
            Targeting TMX to the MAM requires palmitoylation of two
            membrane-proximal cytosolic cysteines.
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Matsuo,Y., Masutani,H., Son,A., Kizaka-Kondoh,S. and Yodoi,J.
  TITLE     Physical and functional interaction of transmembrane
            thioredoxin-related protein with major histocompatibility complex
            class I heavy chain: redox-based protein quality control and its
            potential relevance to immune responses
  JOURNAL   Mol Biol Cell 20 (21), 4552-4562 (2009)
   PUBMED   19741092
  REMARK    GeneRIF: These results suggest a specific role for transmembrane
            thioredoxin-related protein TMX and its mechanism of action in
            redox-based ER quality control.
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Matsuo,Y., Akiyama,N., Nakamura,H., Yodoi,J., Noda,M. and
            Kizaka-Kondoh,S.
  TITLE     Identification of a novel thioredoxin-related transmembrane protein
  JOURNAL   J Biol Chem 276 (13), 10032-10038 (2001)
   PUBMED   11152479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB048246.1, BC056874.1, AL591807.1 and BU754378.1.
            
            On Jul 5, 2007 this sequence version replaced NP_110382.2.
            
            Summary: This gene encodes a member of the disulfide isomerase
            (PDI) family of endoplasmic reticulum (ER) proteins that catalyze
            protein folding and thiol-disulfide interchange reactions. The
            encoded protein has an N-terminal ER-signal sequence, a
            catalytically active thioredoxin domain, and one transmembrane
            domain. Unlike most members of this gene family, it lacks a
            C-terminal ER-retention sequence. The mature membrane-bound protein
            can both oxidize and reduce disulfide bonds and acts selectively on
            membrane-associated polypeptides. [provided by RefSeq, Jan 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.138510.1,
                                           SRR1660805.46843.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000457354.7/ ENSP00000393316.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.1"
     Protein         1..280
                     /product="thioredoxin-related transmembrane protein 1
                     precursor"
                     /EC_number="5.3.4.1"
                     /note="thioredoxin domain containing 1; protein disulfide
                     isomerase family A, member 11; protein disulfide-isomerase
                     TMX1; transmembrane Trx-related protein; thioredoxin
                     domain-containing protein 1"
                     /calculated_mol_wt=29152
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2657
     mat_peptide     27..280
                     /product="Thioredoxin-related transmembrane protein 1.
                     /id=PRO_0000034153"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3N1.1)"
                     /calculated_mol_wt=29152
     Region          29..129
                     /region_name="PDI_a_TMX"
                     /note="PDIa family, TMX subfamily; composed of proteins
                     similar to the TRX-related human transmembrane protein,
                     TMX. TMX is a type I integral membrane protein; the
                     N-terminal redox active TRX domain is present in the
                     endoplasmic reticulum (ER) lumen while the...; cd02994"
                     /db_xref="CDD:239292"
     Site            order(56,59)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239292"
     Site            181..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3N1.1)"
     Region          218..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3N1.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H3N1.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H3N1.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H3N1.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H3N1.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H3N1.1)"
     CDS             1..280
                     /gene="TMX1"
                     /gene_synonym="PDIA11; TMX; TXNDC; TXNDC1"
                     /coded_by="NM_030755.5:47..889"
                     /db_xref="CCDS:CCDS41953.1"
                     /db_xref="GeneID:81542"
                     /db_xref="HGNC:HGNC:15487"
                     /db_xref="MIM:610527"
ORIGIN      
        1 mapsgslavp lavlvlllwg apwthgrrsn vrvitdenwr ellegdwmie fyapwcpacq
       61 nlqpewesfa ewgedlevni akvdvteqpg lsgrfiital ptiyhckdge frryqgprtk
      121 kdfinfisdk ewksiepvss wfgpgsvlms smsalfqlsm wirtchnyfi edlglpvwgs
      181 ytvfalatlf sglllglcmi fvadclcpsk rrrpqpypyp skkllsesaq plkkveeeqe
      241 adeedvseee aeskegtnkd fpqnairqrs lgpslatdks
//
LOCUS       NP_035239                144 aa            linear   ROD 27-APR-2025
DEFINITION  group IID secretory phospholipase A2 isoform 1 precursor [Mus
            musculus].
ACCESSION   NP_035239
VERSION     NP_035239.1
DBSOURCE    REFSEQ: accession NM_011109.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Taketomi,Y., Higashi,T., Kano,K., Miki,Y., Mochizuki,C.,
            Toyoshima,S., Okayama,Y., Nishito,Y., Nakae,S., Tanaka,S.,
            Tokuoka,S.M., Oda,Y., Shichino,S., Ueha,S., Matsushima,K.,
            Akahoshi,N., Ishii,S., Chun,J., Aoki,J. and Murakami,M.
  TITLE     Lipid-orchestrated paracrine circuit coordinates mast cell
            maturation and anaphylaxis through functional interaction with
            fibroblasts
  JOURNAL   Immunity 57 (8), 1828-1847 (2024)
   PUBMED   39002541
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Zheng,J., Meyerholz,D., Wong,L.R., Gelb,M., Murakami,M. and
            Perlman,S.
  TITLE     Coronavirus-specific antibody production in middle-aged mice
            requires phospholipase A2G2D
  JOURNAL   J Clin Invest 131 (11) (2021)
   PUBMED   34060490
  REMARK    GeneRIF: Coronavirus-specific antibody production in middle-aged
            mice requires phospholipase A2G2D.
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Watanabe,K., Taketomi,Y., Miki,Y., Kugiyama,K. and Murakami,M.
  TITLE     Group V secreted phospholipase A2 plays a protective role against
            aortic dissection
  JOURNAL   J Biol Chem 295 (30), 10092-10111 (2020)
   PUBMED   32482892
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Sato,H., Taketomi,Y., Miki,Y., Murase,R., Yamamoto,K. and
            Murakami,M.
  TITLE     Secreted Phospholipase PLA2G2D Contributes to Metabolic Health by
            Mobilizing omega3 Polyunsaturated Fatty Acids in WAT
  JOURNAL   Cell Rep 31 (5), 107579 (2020)
   PUBMED   32375030
  REMARK    GeneRIF: Secreted Phospholipase PLA2G2D Contributes to Metabolic
            Health by Mobilizing omega3 Polyunsaturated Fatty Acids in WAT.
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Cormier,R.T., Bilger,A., Lillich,A.J., Halberg,R.B., Hong,K.H.,
            Gould,K.A., Borenstein,N., Lander,E.S. and Dove,W.F.
  TITLE     The Mom1AKR intestinal tumor resistance region consists of Pla2g2a
            and a locus distal to D4Mit64
  JOURNAL   Oncogene 19 (28), 3182-3192 (2000)
   PUBMED   10918573
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Shakhov,A.N., Rubtsov,A.V., Lyakhov,I.G., Tumanov,A.V. and
            Nedospasov,S.A.
  TITLE     SPLASH (PLA2IID), a novel member of phospholipase A2 family, is
            associated with lymphotoxin deficiency
  JOURNAL   Genes Immun 1 (3), 191-199 (2000)
   PUBMED   11196711
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Valentin,E., Ghomashchi,F., Gelb,M.H., Lazdunski,M. and Lambeau,G.
  TITLE     On the diversity of secreted phospholipases A(2). Cloning, tissue
            distribution, and functional expression of two novel mouse group II
            enzymes
  JOURNAL   J Biol Chem 274 (44), 31195-31202 (1999)
   PUBMED   10531313
  REMARK    Erratum:[J Biol Chem 2000 Jan 21;275(3):2246]
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Ishizaki,J., Suzuki,N., Higashino,K., Yokota,Y., Ono,T.,
            Kawamoto,K., Fujii,N., Arita,H. and Hanasaki,K.
  TITLE     Cloning and characterization of novel mouse and human secretory
            phospholipase A(2)s
  JOURNAL   J Biol Chem 274 (35), 24973-24979 (1999)
   PUBMED   10455175
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Valentin,E., Koduri,R.S., Scimeca,J.C., Carle,G., Gelb,M.H.,
            Lazdunski,M. and Lambeau,G.
  TITLE     Cloning and recombinant expression of a novel mouse-secreted
            phospholipase A2
  JOURNAL   J Biol Chem 274 (27), 19152-19160 (1999)
   PUBMED   10383420
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL844178.7.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF169408.1, AF169407.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 70.57 cM"
     Protein         1..144
                     /product="group IID secretory phospholipase A2 isoform 1
                     precursor"
                     /EC_number="3.1.1.4"
                     /note="group IID secretory phospholipase A2;
                     phosphatidylcholine 2-acylhydrolase 2D; secretory-type
                     PLA, stroma-associated homolog"
                     /calculated_mol_wt=14267
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1915
     mat_peptide     20..144
                     /product="Group IID secretory phospholipase A2.
                     /id=PRO_0000022756"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVF6.1)"
                     /calculated_mol_wt=14267
     Region          20..137
                     /region_name="PLA2c"
                     /note="Phospholipase A2, a family of secretory and
                     cytosolic enzymes; the latter are either Ca dependent or
                     Ca independent. PLA2 cleaves the sn-2 position of the
                     glycerol backbone of phospholipids (PC or
                     phosphatidylethanolamine), usually in a
                     metal-dependent...; cd00125"
                     /db_xref="CDD:153091"
     Site            order(21,24,28,37,49,81)
                     /site_type="active"
                     /note="putative hydrophobic channel [active]"
                     /db_xref="CDD:153091"
     Site            order(46,48,50,67)
                     /site_type="other"
                     /note="primary metal binding site"
                     /db_xref="CDD:153091"
     Site            order(48,66..67,70,85,111)
                     /site_type="active"
                     /note="catalytic network [active]"
                     /db_xref="CDD:153091"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WVF6.1)"
     CDS             1..144
                     /gene="Pla2g2d"
                     /gene_synonym="GIID; GIID sPLA2; mGIID; PLA2IID;
                     sPLA2-IID; Splash"
                     /coded_by="NM_011109.3:80..514"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS18833.1"
                     /db_xref="GeneID:18782"
                     /db_xref="MGI:MGI:1341796"
ORIGIN      
        1 mrlallcgll lagitatqgg llnlnkmvth mtgkkaffsy wpygchcglg gkgqpkdatd
       61 wccqkhdccy ahlkidgcks ltdnykysis qgtiqcsdng swcerqlcac dkevalclkq
      121 nldsynkrlr yywrprckgk tpac
//
LOCUS       NP_001355309             462 aa            linear   ROD 27-APR-2025
DEFINITION  DNA polymerase delta subunit 3 isoform 2 [Mus musculus].
ACCESSION   NP_001355309 XP_006508212
VERSION     NP_001355309.1
DBSOURCE    REFSEQ: accession NM_001368380.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Zhou,Z., Wang,L., Ge,F., Gong,P., Wang,H., Wang,F., Chen,L. and
            Liu,L.
  TITLE     Pold3 is required for genomic stability and telomere integrity in
            embryonic stem cells and meiosis
  JOURNAL   Nucleic Acids Res 46 (7), 3468-3486 (2018)
   PUBMED   29447390
  REMARK    GeneRIF: These data suggest that Pold3 maintains telomere integrity
            and genomic stability of both Embryonic stem cells and meiosis by
            suppressing replicative stress.
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Ducoux,M., Urbach,S., Baldacci,G., Hubscher,U., Koundrioukoff,S.,
            Christensen,J. and Hughes,P.
  TITLE     Mediation of proliferating cell nuclear antigen (PCNA)-dependent
            DNA replication through a conserved p21(Cip1)-like PCNA-binding
            motif present in the third subunit of human DNA polymerase delta
  JOURNAL   J Biol Chem 276 (52), 49258-49266 (2001)
   PUBMED   11595739
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Hughes,P., Tratner,I., Ducoux,M., Piard,K. and Baldacci,G.
  TITLE     Isolation and identification of the third subunit of mammalian DNA
            polymerase delta by PCNA-affinity chromatography of mouse FM3A cell
            extracts
  JOURNAL   Nucleic Acids Res 27 (10), 2108-2114 (1999)
   PUBMED   10219083
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Mizuno,T., Ito,N., Yokoi,M., Kobayashi,A., Tamai,K., Miyazawa,H.
            and Hanaoka,F.
  TITLE     The second-largest subunit of the mouse DNA polymerase
            alpha-primase complex facilitates both production and nuclear
            translocation of the catalytic subunit of DNA polymerase alpha
  JOURNAL   Mol Cell Biol 18 (6), 3552-3562 (1998)
   PUBMED   9584195
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Longley,M.J., Pierce,A.J. and Modrich,P.
  TITLE     DNA polymerase delta is required for human mismatch repair in vitro
  JOURNAL   J Biol Chem 272 (16), 10917-10921 (1997)
   PUBMED   9099749
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Zeng,X.R., Jiang,Y., Zhang,S.J., Hao,H. and Lee,M.Y.
  TITLE     DNA polymerase delta is involved in the cellular response to UV
            damage in human cells
  JOURNAL   J Biol Chem 269 (19), 13748-13751 (1994)
   PUBMED   7910606
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC161205.3.
            
            On Feb 9, 2019 this sequence version replaced XP_006508212.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF294329.1, SRR17784645.1342666.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 54.32 cM"
     Protein         1..462
                     /product="DNA polymerase delta subunit 3 isoform 2"
                     /note="polymerase (DNA directed), delta 3; DNA polymerase
                     delta subunit 3; DNA polymerase delta subunit p66; GC12"
                     /calculated_mol_wt=50705
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q15054; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Region          19..462
                     /region_name="CDC27"
                     /note="DNA polymerase subunit Cdc27; pfam09507"
                     /db_xref="CDD:462819"
     Region          144..186
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Region          200..230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Region          254..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Region          403..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15054; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15054; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15054; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15054; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Region          452..459
                     /region_name="PIP-box.
                     /evidence=ECO:0000250|UniProtKB:Q15054"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQ28.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15054; propagated from
                     UniProtKB/Swiss-Prot (Q9EQ28.2)"
     CDS             1..462
                     /gene="Pold3"
                     /gene_synonym="2410142G14Rik; P66; P68"
                     /coded_by="NM_001368380.1:80..1468"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:67967"
                     /db_xref="MGI:MGI:1915217"
ORIGIN      
        1 maeqlyleni defvtdqnki vtykwlsytl gvhvnqakqm lyeyverkrk ensgaqlhvt
       61 ylvsgsliqn ghschkvavv redkleavks klavtasihv ysiqkamlkd sgplfntdyd
      121 ilksnlqncs kfsaiqcaaa vprapaesps srkyeqsnlq aaseaqasel ttnghgppas
      181 kqasqqpkgi mgmliskaat ktqdtnketk pearevtsas saggkapgkg svmsnffgka
      241 amnklkvnld seqavkeekt veqppvsvte pklaappaqk kssrksepgk vqqkekssrg
      301 krvdlsdeea ketehlkkkr rriklpqsds sedevfedsp emyeadspsp ppvspppdpm
      361 pktepppvkr ssgetkrrrk rvlksktfvd eegcivtekv yesesctdse eelkmkpasa
      421 hkppaaavkr epreerkgpk kgaaalgkan rqvsitgffq kk
//
LOCUS       NP_061893                767 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 16 isoform a [Homo sapiens].
ACCESSION   NP_061893
VERSION     NP_061893.2
DBSOURCE    REFSEQ: accession NM_019020.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Yan,J., Zheng,Y., Yuan,P., Wang,S., Han,S., Yin,J., Peng,B., Li,Z.,
            Sun,Y., He,X. and Liu,W.
  TITLE     Novel Host Protein TBC1D16, a GTPase Activating Protein of Rab5C,
            Inhibits Prototype Foamy Virus Replication
  JOURNAL   Front Immunol 12, 658660 (2021)
   PUBMED   34367131
  REMARK    GeneRIF: Novel Host Protein TBC1D16, a GTPase Activating Protein of
            Rab5C, Inhibits Prototype Foamy Virus Replication.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Liu,H., Chen,P., Yang,Y.L., Zhu,K.W., Wang,T., Tang,L., Liu,Y.L.,
            Cao,S., Zhou,G., Zeng,H., Zhao,X.L., Zhang,W. and Chen,X.P.
  TITLE     TBC1D16 predicts chemosensitivity and prognosis in adult acute
            myeloid leukemia (AML) patients
  JOURNAL   Eur J Pharmacol 895, 173894 (2021)
   PUBMED   33476656
  REMARK    GeneRIF: TBC1D16 predicts chemosensitivity and prognosis in adult
            acute myeloid leukemia (AML) patients.
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Rodger,E.J., Chatterjee,A., Stockwell,P.A. and Eccles,M.R.
  TITLE     Characterisation of DNA methylation changes in EBF3 and TBC1D16
            associated with tumour progression and metastasis in multiple
            cancer types
  JOURNAL   Clin Epigenetics 11 (1), 114 (2019)
   PUBMED   31383000
  REMARK    GeneRIF: Findings suggest characteristic DNA methylation changes in
            TBC1D16 is relatively common tumor-associated epigenetic events in
            multiple tumor types, which is consistent with a potential role as
            more general drivers of tumor progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 767)
  AUTHORS   Yang,Z., Shen,H., He,W., Ouyang,L., Guo,Y., Qian,F., Xu,B., Xie,D.
            and Yang,G.
  TITLE     Expression of TBC1D16 Is Associated with Favorable Prognosis of
            Epithelial Ovarian Cancer
  JOURNAL   Tohoku J Exp Med 245 (3), 141-148 (2018)
   PUBMED   29962380
  REMARK    GeneRIF: TBC1D16 is a predictive marker for favorable prognosis of
            Epithelial ovarian cancer.
REFERENCE   5  (residues 1 to 767)
  AUTHORS   Jeremian,R., Chen,Y.A., De Luca,V., Vincent,J.B., Kennedy,J.L.,
            Zai,C.C. and Strauss,J.
  TITLE     Investigation of correlations between DNA methylation, suicidal
            behavior and aging
  JOURNAL   Bipolar Disord 19 (1), 32-40 (2017)
   PUBMED   28276657
  REMARK    GeneRIF: Bipolar disorder participants with a history of Suicidal
            behavior showed less overall methylation in the intron 3 of
            TRE2/BUB2/CDC16 domain family member 16 (TBC1D16).
REFERENCE   6  (residues 1 to 767)
  AUTHORS   Vizoso,M., Ferreira,H.J., Lopez-Serra,P., Carmona,F.J.,
            Martinez-Cardus,A., Girotti,M.R., Villanueva,A., Guil,S.,
            Moutinho,C., Liz,J., Portela,A., Heyn,H., Moran,S., Vidal,A.,
            Martinez-Iniesta,M., Manzano,J.L., Fernandez-Figueras,M.T.,
            Elez,E., Munoz-Couselo,E., Botella-Estrada,R., Berrocal,A.,
            Ponten,F., Oord,Jv., Gallagher,W.M., Frederick,D.T., Flaherty,K.T.,
            McDermott,U., Lorigan,P., Marais,R. and Esteller,M.
  TITLE     Epigenetic activation of a cryptic TBC1D16 transcript enhances
            melanoma progression by targeting EGFR
  JOURNAL   Nat Med 21 (7), 741-750 (2015)
   PUBMED   26030178
  REMARK    GeneRIF: RAB5C is identified as a new TBC1D16 target and showed
            that it regulates EGFR in melanoma cells.
REFERENCE   7  (residues 1 to 767)
  AUTHORS   Goueli,B.S., Powell,M.B., Finger,E.C. and Pfeffer,S.R.
  TITLE     TBC1D16 is a Rab4A GTPase activating protein that regulates
            receptor recycling and EGF receptor signaling
  JOURNAL   Proc Natl Acad Sci U S A 109 (39), 15787-15792 (2012)
   PUBMED   23019362
  REMARK    GeneRIF: TBC1D16 is a GTPase activating protein for Rab4A that
            regulates transferrin receptor recycling and EGFR trafficking and
            signaling.
REFERENCE   8  (residues 1 to 767)
  AUTHORS   Popovic,D., Akutsu,M., Novak,I., Harper,J.W., Behrends,C. and
            Dikic,I.
  TITLE     Rab GTPase-activating proteins in autophagy: regulation of
            endocytic and autophagy pathways by direct binding to human ATG8
            modifiers
  JOURNAL   Mol Cell Biol 32 (9), 1733-1744 (2012)
   PUBMED   22354992
REFERENCE   9  (residues 1 to 767)
  AUTHORS   Akavia,U.D., Litvin,O., Kim,J., Sanchez-Garcia,F., Kotliar,D.,
            Causton,H.C., Pochanard,P., Mozes,E., Garraway,L.A. and Pe'er,D.
  TITLE     An integrated approach to uncover drivers of cancer
  JOURNAL   Cell 143 (6), 1005-1017 (2010)
   PUBMED   21129771
  REMARK    GeneRIF: TBC1D16 and RAB27A, were identified known drivers of
            melanoma both are involved in the regulation of vesicular
            trafficking, which highlights this process as important for
            proliferation in melanoma.
REFERENCE   10 (residues 1 to 767)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116025.21, CN361974.1, BC028290.1, AC100791.15 and BC062601.1.
            
            On Aug 9, 2003 this sequence version replaced NP_061893.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028290.1, SRR3476690.49392.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310924.7/ ENSP00000309794.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..767
                     /product="TBC1 domain family member 16 isoform a"
                     /note="CTD-2529O21.1"
                     /calculated_mol_wt=86241
     Region          93..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBP0.1)"
     Region          169..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBP0.1)"
     Region          424..652
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Region          729..767
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBP0.1)"
     CDS             1..767
                     /gene="TBC1D16"
                     /coded_by="NM_019020.4:141..2444"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11766.1"
                     /db_xref="GeneID:125058"
                     /db_xref="HGNC:HGNC:28356"
                     /db_xref="MIM:616637"
ORIGIN      
        1 mslgrllrra sskasdlltl tpggsgsgsp svldgeiiys knnvcvhppe glqglgehhp
       61 gylclymekd emlgatlila wvpnsriqrq deealryitp esspvrkapr prgrrtrssg
      121 ashqpsptel rptltpkded ilvvaqsvpd rmlaspaped eeklaqglgv dgaqpasqpa
      181 cspsgilstv spqdvteegr eprpeageed gslelsaegv srdssfdsds dtfsspfcls
      241 pisaalaesr gsvflesdss ppsssdaglr fpdsngllqt prwdepqrvc aleqicgvfr
      301 vdlghmrslr lffsdeacts gqlvvasres qykvfhfhhg gldklsdvfq qwkyctemql
      361 kdqqvapdkt cmqfsirrpk lpssethpee smykrlgvsa wlnhlnelgq veeeyklrka
      421 iffggidvsi rgevwpfllr yyshestsee realrlqkrk eyseiqqkrl smtpeehraf
      481 wrnvqftvdk dvvrtdrnnq ffrgednpnv esmrrillny avynpavgys qgmsdlvapi
      541 laevldesdt fwcfvglmqn tifvssprde dmekqllylr ellrlthvrf yqhlvslged
      601 glqmlfchrw lllcfkrefp eaealriwea cwahyqtdyf hlficvaiva iygddvieqq
      661 latdqmllhf gnlamhmnge lvlrkarsll yqfrllprip cslhdlcklc gsgmwdsgsm
      721 pavectghhp gsescpyggt vempspkslr egkkgpktpq dgfgfrr
//
LOCUS       NP_001120               1158 aa            linear   PRI 27-APR-2025
DEFINITION  adipocyte enhancer-binding protein 1 precursor [Homo sapiens].
ACCESSION   NP_001120
VERSION     NP_001120.3
DBSOURCE    REFSEQ: accession NM_001129.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Liu,S., Gu,Y., Shi,Y., Yu,S., Li,W. and Lv,W.
  TITLE     AEBP1 upregulation contributes to cervical cancer progression by
            facilitating cell proliferation, migration, and invasion
  JOURNAL   J Obstet Gynaecol Res 50 (7), 1166-1174 (2024)
   PUBMED   38684171
  REMARK    GeneRIF: AEBP1 upregulation contributes to cervical cancer
            progression by facilitating cell proliferation, migration, and
            invasion.
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Asadie,M., Miri,A., Badri,T., Hosseini Nejad,J. and Gharechahi,J.
  TITLE     Dysregulated AEBP1 and COLEC12 Genes in Late-Onset Alzheimer's
            Disease: Insights from Brain Cortex and Peripheral Blood Analysis
  JOURNAL   J Mol Neurosci 74 (2), 37 (2024)
   PUBMED   38568322
  REMARK    GeneRIF: Dysregulated AEBP1 and COLEC12 Genes in Late-Onset
            Alzheimer's Disease: Insights from Brain Cortex and Peripheral
            Blood Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Ju,G., Xing,T., Xu,M., Zhang,X., Sun,Y., Mu,Z., Sun,D., Miao,S.,
            Li,L., Liang,J. and Lin,Y.
  TITLE     AEBP1 promotes papillary thyroid cancer progression by activating
            BMP4 signaling
  JOURNAL   Neoplasia 49, 100972 (2024)
   PUBMED   38237535
  REMARK    GeneRIF: AEBP1 promotes papillary thyroid cancer progression by
            activating BMP4 signaling.
REFERENCE   4  (residues 1 to 1158)
  AUTHORS   Corano Scheri,K., Lavine,J.A., Tedeschi,T., Thomson,B.R. and
            Fawzi,A.A.
  TITLE     Single-cell transcriptomics analysis of proliferative diabetic
            retinopathy fibrovascular membranes reveals AEBP1 as fibrogenesis
            modulator
  JOURNAL   JCI Insight 8 (23), e172062 (2023)
   PUBMED   37917183
  REMARK    GeneRIF: Single-cell transcriptomics analysis of proliferative
            diabetic retinopathy fibrovascular membranes reveals AEBP1 as
            fibrogenesis modulator.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1158)
  AUTHORS   Li,Y.X., Zhu,X.X., Wu,X., Li,J.H., Ni,X.H., Li,S.J., Zhao,W. and
            Yin,X.Y.
  TITLE     ACLP promotes activation of cancer-associated fibroblasts and tumor
            metastasis via ACLP-PPARgamma-ACLP feedback loop in pancreatic
            cancer
  JOURNAL   Cancer Lett 544, 215802 (2022)
   PUBMED   35732215
  REMARK    GeneRIF: ACLP promotes activation of cancer-associated fibroblasts
            and tumor metastasis via ACLP-PPARgamma-ACLP feedback loop in
            pancreatic cancer.
REFERENCE   6  (residues 1 to 1158)
  AUTHORS   Layne,M.D., Yet,S.F., Maemura,K., Hsieh,C.M., Bernfield,M.,
            Perrella,M.A. and Lee,M.E.
  TITLE     Impaired abdominal wall development and deficient wound healing in
            mice lacking aortic carboxypeptidase-like protein
  JOURNAL   Mol Cell Biol 21 (15), 5256-5261 (2001)
   PUBMED   11438679
  REMARK    GeneRIF: Most ACLP knockout mice die perinatally due to abdominal
            issues.
REFERENCE   7  (residues 1 to 1158)
  AUTHORS   Muise,A.M. and Ro,H.S.
  TITLE     Enzymic characterization of a novel member of the regulatory B-like
            carboxypeptidase with transcriptional repression function:
            stimulation of enzymic activity by its target DNA
  JOURNAL   Biochem J 343 Pt 2 (Pt 2), 341-345 (1999)
   PUBMED   10510298
REFERENCE   8  (residues 1 to 1158)
  AUTHORS   Layne,M.D., Endege,W.O., Jain,M.K., Yet,S.F., Hsieh,C.M.,
            Chin,M.T., Perrella,M.A., Blanar,M.A., Haber,E. and Lee,M.E.
  TITLE     Aortic carboxypeptidase-like protein, a novel protein with
            discoidin and carboxypeptidase-like domains, is up-regulated during
            vascular smooth muscle cell differentiation
  JOURNAL   J Biol Chem 273 (25), 15654-15660 (1998)
   PUBMED   9624159
REFERENCE   9  (residues 1 to 1158)
  AUTHORS   Song,L. and Fricker,L.D.
  TITLE     Cloning and expression of human carboxypeptidase Z, a novel
            metallocarboxypeptidase
  JOURNAL   J Biol Chem 272 (16), 10543-10550 (1997)
   PUBMED   9099699
REFERENCE   10 (residues 1 to 1158)
  AUTHORS   Ohno,I., Hashimoto,J., Shimizu,K., Takaoka,K., Ochi,T.,
            Matsubara,K. and Okubo,K.
  TITLE     A cDNA cloning of human AEBP1 from primary cultured osteoblasts and
            its expression in a differentiating osteoblastic cell line
  JOURNAL   Biochem Biophys Res Commun 228 (2), 411-414 (1996)
   PUBMED   8920928
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006454.4, BC038588.1 and
            DB213495.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 1, 2004 this sequence version replaced NP_001120.2.
            
            Summary: This gene encodes a member of carboxypeptidase A protein
            family. The encoded protein may function as a transcriptional
            repressor and play a role in adipogenesis and smooth muscle cell
            differentiation. Studies in mice suggest that this gene functions
            in wound healing and abdominal wall development. Overexpression of
            this gene is associated with glioblastoma. [provided by RefSeq, May
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038588.1, AB209744.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000223357.8/ ENSP00000223357.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..1158
                     /product="adipocyte enhancer-binding protein 1 precursor"
                     /note="aortic carboxypeptidase-like protein; adipocyte
                     enhancer-binding protein 1"
                     /calculated_mol_wt=128483
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2464
     mat_peptide     26..1158
                     /product="Adipocyte enhancer-binding protein 1.
                     /id=PRO_0000333189"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
                     /calculated_mol_wt=128483
     Region          41..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          386..539
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Region          390..555
                     /region_name="Required for DNA-binding and interaction
                     with NFKBIA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          421..624
                     /region_name="Interaction with MAPK1 and MAPK3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Site            order(434,462,469)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            528
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          555..985
                     /region_name="Interaction with PTEN.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          564..903
                     /region_name="Peptidase_M14_like"
                     /note="M14 family of metallocarboxypeptidases and related
                     proteins; cl11393"
                     /db_xref="CDD:472171"
     Site            order(625,628,690,699..700,763..764,770,874)
                     /site_type="active"
                     /db_xref="CDD:349441"
     Region          907..982
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cd11308"
                     /db_xref="CDD:200604"
     Site            922
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          941..1158
                     /region_name="Required for transcriptional repression.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          1006..1158
                     /region_name="Interaction with MAPK1 and MAPK3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     Region          1108..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUX7.1)"
     CDS             1..1158
                     /gene="AEBP1"
                     /gene_synonym="ACLP"
                     /coded_by="NM_001129.5:322..3798"
                     /db_xref="CCDS:CCDS5476.1"
                     /db_xref="GeneID:165"
                     /db_xref="HGNC:HGNC:303"
                     /db_xref="MIM:602981"
ORIGIN      
        1 maavrgapll scllallalc pggrpqtvlt ddeieefleg flselepepr eddveapppp
       61 eptprvrkaq aggkpgkrpg taaevppekt kdkgkkgkkd kgpkvpkesl egsprppkkg
      121 kekppkatkk pkekppkatk kpkekppkat kkpkekppka tkkppsgkrp pilapsetle
      181 wplppppspg peelpqegga plsnnwqnpg eethveareh qpepeeeteq ptldyndqie
      241 redyedfeyi rrqkqprppp srrrrpervw peppeekapa papeeriepp vkpllpplpp
      301 dygdgyvipn yddmdyyfgp pppqkpdaer qtdeekeelk kpkkedsspk eetdkwavek
      361 gkdhkeprkg eeleeewtpt ekvkcppigm eshriednqi rassmlrhgl gaqrgrlnmq
      421 tgateddyyd gawcaeddar tqwievdtrr ttrftgvitq grdssihddf vttffvgfsn
      481 dsqtwvmytn gyeemtfhgn vdkdtpvlse lpepvvarfi riypltwngs lcmrlevlgc
      541 svapvysyya qnevvatddl dfrhhsykdm rqlmkvvnee cptitrtysl gkssrglkiy
      601 ameisdnpge helgepefry tagihgnevl grelllllmq ylcreyrdgn prvrslvqdt
      661 rihlvpslnp dgyevaaqmg sefgnwalgl wteegfdife dfpdlnsvlw gaeerkwvpy
      721 rvpnnnlpip erylspdatv stevraiiaw meknpfvlga nlnggerlvs ypydmartpt
      781 qeqllaaama aargededev seaqetpdha ifrwlaisfa sahltltepy rggcqaqdyt
      841 ggmgivngak wnprtgtind fsylhtncle lsfylgcdkf pheselprew ennkealltf
      901 meqvhrgikg vvtdeqgipi anatisvsgi nhgvktasgg dywrilnpge yrvtahaegy
      961 tpsaktcnvd ydigatqcnf ilarsnwkri reimamngnr piphidpsrp mtpqqrrlqq
     1021 rrlqhrlrlr aqmrlrrlna tttlgphtvp ptlppapatt lsttiepwgl ippttagwee
     1081 setetytevv tefgtevepe fgtkvepefe tqlepefetq lepefeeeee eekeeeiatg
     1141 qafpfttvet ytvnfgdf
//
LOCUS       NP_001346745            1075 aa            linear   ROD 27-APR-2025
DEFINITION  atos homolog protein A isoform 1 [Mus musculus].
ACCESSION   NP_001346745 XP_006511190
VERSION     NP_001346745.1
DBSOURCE    REFSEQ: accession NM_001359816.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Soulez,M., Saba-El-Leil,M.K., Turgeon,B., Mathien,S., Coulombe,P.,
            Klinger,S., Rousseau,J., Levesque,K. and Meloche,S.
  TITLE     Reevaluation of the Role of Extracellular Signal-Regulated Kinase 3
            in Perinatal Survival and Postnatal Growth Using New Genetically
            Engineered Mouse Models
  JOURNAL   Mol Cell Biol 39 (6), e00527-18 (2019)
   PUBMED   30642949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CT025657.12 and CT033761.14.
            
            On Jan 18, 2018 this sequence version replaced XP_006511190.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660821.194256.1,
                                           SRR7652917.823744.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 42.12 cM"
     Protein         1..1075
                     /product="atos homolog protein A isoform 1"
                     /note="protein FAM214A; family with sequence similarity
                     214, member A; atos homolog protein A"
                     /calculated_mol_wt=119141
     Region          24..32
                     /region_name="Transactivation domain 1 (TAD1).
                     /evidence=ECO:0000269|PubMed:35319107"
                     /note="propagated from UniProtKB/Swiss-Prot (Q69ZK7.3)"
     Region          430..469
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q69ZK7.3)"
     Region          570..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q69ZK7.3)"
     Region          703..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q69ZK7.3)"
     Region          878..935
                     /region_name="DUF4210"
                     /note="Domain of unknown function (DUF4210); pfam13915"
                     /db_xref="CDD:404751"
     Region          878..935
                     /region_name="Required for macropage invasion.
                     /evidence=ECO:0000269|PubMed:35319107"
                     /note="propagated from UniProtKB/Swiss-Prot (Q69ZK7.3)"
     Region          962..970
                     /region_name="Transactivation domain 2 (TAD2).
                     /evidence=ECO:0000269|PubMed:35319107"
                     /note="propagated from UniProtKB/Swiss-Prot (Q69ZK7.3)"
     Region          1017..1074
                     /region_name="Chromosome_seg"
                     /note="Chromosome segregation during meiosis; pfam13889"
                     /db_xref="CDD:464021"
     CDS             1..1075
                     /gene="Atosa"
                     /gene_synonym="6330415I01Rik; C130047D21Rik; Fam214a;
                     Kiaa1370; mKIAA1370"
                     /coded_by="NM_001359816.1:231..3458"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS52857.1"
                     /db_xref="GeneID:235493"
                     /db_xref="MGI:MGI:2387648"
ORIGIN      
        1 mkpdrdalde yfeydaeefl vslalliteg rtpecsvkgr aesfhcppaq srfpgtarhe
       61 csdklaqcrq arrtrsevtl lwknnlpimv evmllpdccy sdegpstega dlndpaikqd
      121 alllerwile pvprqngdrf ieekalllav rsfvffsqls awlsvshgai prnilyrisa
      181 advdlqwsfs qtptehvfpv pnvshnvalk vsvqslprqa hypvltcsih tniglyekri
      241 qeqelracqh hgpgeveyrc psssqslcsk htwtmapvsa lhvrsgmppe ytaairnvrl
      301 cpgtgsksdq gapqasvlgf sgtggevrsq easvrtfksl pvvdssvssc qssrqpvgep
      361 nplmdsliqd rqeviariaq hlihcdpsss rmselpfntq estslspklh pvsqesgcvr
      421 rykeafsvsf gspefgspgd sregkvreks etrpgetcts hslyprqpag eanpligsll
      481 qerqdviari aqhlehidpa ahiprpafsk hdsnsipskv frssfddktl lkkgrenvsv
      541 svshtevsll gdrgdgeslk pskclrsfky spqekplkpe vrtqhqnhpd sitptarqel
      601 lnkaagllts sntalckess lglvsrlest scklqlkeqe mshetekqcl hcnsidkqic
      661 tntctekind ehspgslrhl qcddskgids klkvtllemp dslnknktnc sskdskrskt
      721 ceqsirvgte ndlseenegp gstvsdrlkt eqeakrdsga gkphsvkhcl sagerlhsad
      781 mlrttlkhss vwrkhnfhsl dgtstrafhp qtglpllssp vpqrktqsgc fdldasllhl
      841 rslsskssrp clnidedpdv hekpflsssa ppitslsllg nfeesvlnyr ldplgivdgf
      901 taevgasgtf cpthltlpve vsfysvsddn apspymgvit leslgkrgyr vppsgtiqvt
      961 lfnpnktvvk mfvvvydlrg mpanhqtflr qrtfsvpvkq emkrsinken vqhtaqllry
     1021 lihlrfqssk sgkiylhrdv rllfsrksme vdsgaayelk sytesptnpq fsprc
//
LOCUS       NP_079031               1034 aa            linear   PRI 27-APR-2025
DEFINITION  SAFB-like transcription modulator isoform a [Homo sapiens].
ACCESSION   NP_079031
VERSION     NP_079031.2
DBSOURCE    REFSEQ: accession NM_024755.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Chen,R., Tong,Y., Hu,X., Wang,W. and Liao,F.
  TITLE     circSLTM knockdown attenuates chondrocyte inflammation, apoptosis
            and ECM degradation in osteoarthritis by regulating the
            miR-515-5p/VAPB axis
  JOURNAL   Int Immunopharmacol 138, 112435 (2024)
   PUBMED   38981227
  REMARK    GeneRIF: circSLTM knockdown attenuates chondrocyte inflammation,
            apoptosis and ECM degradation in osteoarthritis by regulating the
            miR-515-5p/VAPB axis.
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Feng,X., He,S., Chen,Y. and Zhang,L.
  TITLE     Deubiquitinase BRCC3 promotes the migration, invasion and EMT
            progression of colon adenocarcinoma by stabilizing MET expression
  JOURNAL   Genes Genomics 46 (5), 637-646 (2024)
   PUBMED   38470543
  REMARK    GeneRIF: Deubiquitinase BRCC3 promotes the migration, invasion and
            EMT progression of colon adenocarcinoma by stabilizing MET
            expression.
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Liang,Q., Hu,Y., Yuan,Q., Yu,M., Wang,H. and Zhao,B.
  TITLE     MET exon 14 skipping mutation drives cancer progression and
            recurrence via activation of SMAD2 signalling
  JOURNAL   Br J Cancer 130 (3), 380-393 (2024)
   PUBMED   38110666
  REMARK    GeneRIF: MET exon 14 skipping mutation drives cancer progression
            and recurrence via activation of SMAD2 signalling.
REFERENCE   4  (residues 1 to 1034)
  AUTHORS   Gong,D.A., Zhou,P., Chang,W.Y., Yang,J.Y., Zhang,Y.L., Huang,A.L.,
            Tang,N. and Wang,K.
  TITLE     SPOP promotes CREB5 ubiquitination to inhibit MET signaling in
            liver cancer
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (2), 119642 (2024)
   PUBMED   37996058
  REMARK    GeneRIF: SPOP promotes CREB5 ubiquitination to inhibit MET
            signaling in liver cancer.
REFERENCE   5  (residues 1 to 1034)
  AUTHORS   Tsujio,G., Yashiro,M., Sakuma,T., Aoyama,R., Maruo,K., Yamamoto,Y.
            and Maeda,K.
  TITLE     Impact of SMAD2 and MET Expression on Lymph Node Metastasis of
            HER2-positive Gastric Cancer Cells
  JOURNAL   Anticancer Res 43 (10), 4359-4364 (2023)
   PUBMED   37772583
  REMARK    GeneRIF: Impact of SMAD2 and MET Expression on Lymph Node
            Metastasis of HER2-positive Gastric Cancer Cells.
REFERENCE   6  (residues 1 to 1034)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 1034)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 1034)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 1034)
  AUTHORS   Salyakina,D., Ma,D.Q., Jaworski,J.M., Konidari,I., Whitehead,P.L.,
            Henson,R., Martinez,D., Robinson,J.L., Sacharow,S., Wright,H.H.,
            Abramson,R.K., Gilbert,J.R., Cuccaro,M.L. and Pericak-Vance,M.A.
  TITLE     Variants in several genomic regions associated with asperger
            disorder
  JOURNAL   Autism Res 3 (6), 303-310 (2010)
   PUBMED   21182207
REFERENCE   10 (residues 1 to 1034)
  AUTHORS   Gratacos,M., Costas,J., de Cid,R., Bayes,M., Gonzalez,J.R.,
            Baca-Garcia,E., de Diego,Y., Fernandez-Aranda,F.,
            Fernandez-Piqueras,J., Guitart,M., Martin-Santos,R., Martorell,L.,
            Menchon,J.M., Roca,M., Saiz-Ruiz,J., Sanjuan,J., Torrens,M.,
            Urretavizcaya,M., Valero,J., Vilella,E., Estivill,X. and
            Carracedo,A.
  CONSRTM   Psychiatric Genetics Network Group
  TITLE     Identification of new putative susceptibility genes for several
            psychiatric disorders by association analysis of regulatory and
            non-synonymous SNPs of 306 genes involved in neurotransmission and
            neurodevelopment
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 150B (6), 808-816 (2009)
   PUBMED   19086053
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025918.7, DA215437.1, BC140851.1 and BC046119.1.
            
            On May 11, 2005 this sequence version replaced NP_079031.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and it encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.51521.1,
                                           SRR1660807.146606.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380516.7/ ENSP00000369887.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.1"
     Protein         1..1034
                     /product="SAFB-like transcription modulator isoform a"
                     /note="modulator of estrogen-induced transcription"
                     /calculated_mol_wt=117018
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.4,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Region          22..56
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Region          <34..723
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          55..242
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CH25; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Region          268..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Region          385..458
                     /region_name="RRM_SLTM"
                     /note="RNA recognition motif (RRM) found in Scaffold
                     attachment factor (SAF)-like transcription modulator
                     (SLTM) and similar proteins; cd12678"
                     /db_xref="CDD:410079"
     Site            401
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Region          456..599
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            550
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Region          713..1034
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            748
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Region          798..>1033
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            800
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            815
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            909
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            923
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            929
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            944
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            998
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            1002
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            1014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            1017
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            1019
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            1021
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     Site            1024
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NWH9.2)"
     CDS             1..1034
                     /gene="SLTM"
                     /gene_synonym="Met"
                     /coded_by="NM_024755.4:115..3219"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10168.2"
                     /db_xref="GeneID:79811"
                     /db_xref="HGNC:HGNC:20709"
                     /db_xref="MIM:620992"
ORIGIN      
        1 maaatgavaa saasgqaegk kitdlrvidl kselkrrnld itgvktvlis rlkqaieeeg
       61 gdpdnieltv stdtpnkkpt kgkgkkhead elsgdasved dafikdcele nqeaheqdgn
      121 delkdseefg eneeenvhsk ellsaeenkr ahelieaegi ediekedies qeieaqeged
      181 dtfltaqdge eeenekdiag sgdgtqevsk plpsegslae adhtaheeme ahttvkeaed
      241 dnisvtiqae daitldfdgd dlletgknvk itdseaskpk dgqdaiaqsp ekeskdyemn
      301 anhkdgkked cvkgdpveke aresskkaes gdkekdtlkk gpsstgasgq akssskeskd
      361 sktsskddkg stsstsgssg sstkniwvsg lssntkaadl knlfgkygkv lsakvvtnar
      421 spgakcygiv tmssstevsr ciahlhrtel hgqlisvekv kgdpskkemk kendeksssr
      481 ssgdkkntsd rssktqasvk keekrsseks ekkeskdtkk iegkdekndn gasgqtsesi
      541 kkseekkris skspghmvil dqtkgdhcrp srrgryekih grskekeras ldkkrdkdyr
      601 rkeilpfekm keqrlrehlv rferlrrame lrrrreiaer errereriri irereererl
      661 qrererleie rqklererme rerlererir ieqerrkeae riarereelr rqqqqlryeq
      721 ekrnslkrpr dvdhrrddpy wsenkklsld tdarfghgsd ysrqqnrfnd fdhrergrfp
      781 essavqsssf errdrfvgqs egkkarptar redpsferyp knfsdsrrne pppprnelre
      841 sdrrevrger derrtviihd rpdithprhp reagpnpsrp tswksegsms tdkretrver
      901 persgrevsg hsvrgappgn rssasgygsr egdrgvitdr gggsqhypee rhvverhgrd
      961 tsgprkewhg ppsqgpsyhd trrmgdgrag agmitqhssn aspinrivqi sgnsmprgsg
     1021 sgfkpfkggp prrf
//
LOCUS       NP_036590                 95 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim13 [Homo
            sapiens].
ACCESSION   NP_036590
VERSION     NP_036590.1
DBSOURCE    REFSEQ: accession NM_012458.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Wang,Z., Fan,M., Candas,D., Zhang,T.Q., Qin,L., Eldridge,A.,
            Wachsmann-Hogiu,S., Ahmed,K.M., Chromy,B.A., Nantajit,D., Duru,N.,
            He,F., Chen,M., Finkel,T., Weinstein,L.S. and Li,J.J.
  TITLE     Cyclin B1/Cdk1 coordinates mitochondrial respiration for cell-cycle
            G2/M progression
  JOURNAL   Dev Cell 29 (2), 217-232 (2014)
   PUBMED   24746669
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Gentle,I.E., Perry,A.J., Alcock,F.H., Likic,V.A., Dolezal,P.,
            Ng,E.T., Purcell,A.W., McConnville,M., Naderer,T., Chanez,A.L.,
            Charriere,F., Aschinger,C., Schneider,A., Tokatlidis,K. and
            Lithgow,T.
  TITLE     Conserved motifs reveal details of ancestry and structure in the
            small TIM chaperones of the mitochondrial intermembrane space
  JOURNAL   Mol Biol Evol 24 (5), 1149-1160 (2007)
   PUBMED   17329230
REFERENCE   6  (residues 1 to 95)
  AUTHORS   Rothbauer,U., Hofmann,S., Muhlenbein,N., Paschen,S.A.,
            Gerbitz,K.D., Neupert,W., Brunner,M. and Bauer,M.F.
  TITLE     Role of the deafness dystonia peptide 1 (DDP1) in import of human
            Tim23 into the inner membrane of mitochondria
  JOURNAL   J Biol Chem 276 (40), 37327-37334 (2001)
   PUBMED   11489896
REFERENCE   7  (residues 1 to 95)
  AUTHORS   Rehling,P., Wiedemann,N., Pfanner,N. and Truscott,K.N.
  TITLE     The mitochondrial import machinery for preproteins
  JOURNAL   Crit Rev Biochem Mol Biol 36 (3), 291-336 (2001)
   PUBMED   11450972
  REMARK    Review article
REFERENCE   8  (residues 1 to 95)
  AUTHORS   Paschen,S.A., Rothbauer,U., Kaldi,K., Bauer,M.F., Neupert,W. and
            Brunner,M.
  TITLE     The role of the TIM8-13 complex in the import of Tim23 into
            mitochondria
  JOURNAL   EMBO J 19 (23), 6392-6400 (2000)
   PUBMED   11101512
REFERENCE   9  (residues 1 to 95)
  AUTHORS   Bauer,M.F., Rothbauer,U., Muhlenbein,N., Smith,R.J., Gerbitz,K.,
            Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     The mitochondrial TIM22 preprotein translocase is highly conserved
            throughout the eukaryotic kingdom
  JOURNAL   FEBS Lett 464 (1-2), 41-47 (1999)
   PUBMED   10611480
REFERENCE   10 (residues 1 to 95)
  AUTHORS   Jin,H., Kendall,E., Freeman,T.C., Roberts,R.G. and Vetrie,D.L.
  TITLE     The human family of Deafness/Dystonia peptide (DDP) related
            mitochondrial import proteins
  JOURNAL   Genomics 61 (3), 259-267 (1999)
   PUBMED   10552927
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY098076.1, AK024764.1 and
            AC011522.8.
            
            Summary: This gene encodes a member of the evolutionarily conserved
            TIMM (translocase of inner mitochondrial membrane) family of
            proteins that function as chaperones in the import of proteins from
            the cytoplasm into the mitochondrial inner membrane. Proteins of
            this family play a role in collecting substrate proteins from the
            translocase of the outer mitochondrial membrane (TOM) complex and
            delivering them to either the sorting and assembly machinery in the
            outer mitochondrial membrane (SAM) complex or the TIMM22 complex in
            the inner mitochondrial membrane. The encoded protein and the
            translocase of mitochondrial inner membrane 8a protein form a 70
            kDa complex in the intermembrane space. [provided by RefSeq, Jul
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.773314.1,
                                           SRR3476690.880947.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2163105
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000215570.8/
                                                  ENSP00000215570.2
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..95
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim13"
                     /note="mitochondrial import inner membrane translocase
                     subunit Tim13B; translocase of inner mitochondrial
                     membrane 13 homolog"
                     /calculated_mol_wt=10369
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5L4.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5L4.1)"
     Region          24..86
                     /region_name="zf-Tim10_DDP"
                     /note="Tim10/DDP family zinc finger; pfam02953"
                     /db_xref="CDD:460764"
     Region          46..69
                     /region_name="Twin CX3C motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5L4.1)"
     CDS             1..95
                     /gene="TIMM13"
                     /gene_synonym="ppv1; TIM13; TIM13B; TIMM13A; TIMM13B"
                     /coded_by="NM_012458.4:54..341"
                     /db_xref="CCDS:CCDS12089.1"
                     /db_xref="GeneID:26517"
                     /db_xref="HGNC:HGNC:11816"
                     /db_xref="MIM:607383"
ORIGIN      
        1 meggfgsdfg gsgsgkldpg limeqvkvqi avanaqellq rmtdkcfrkc igkpggsldn
       61 seqkciamcm drymdawntv sraynsrlqr eranm
//
LOCUS       NP_034989                204 aa            linear   ROD 27-APR-2025
DEFINITION  myosin light chain 3 [Mus musculus].
ACCESSION   NP_034989 XP_984544
VERSION     NP_034989.1
DBSOURCE    REFSEQ: accession NM_010859.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Cao,H., Yang,P., Liu,J., Shao,Y., Li,H., Lai,P., Wang,H., Liu,A.,
            Guo,B., Tang,Y., Bai,X. and Li,K.
  TITLE     MYL3 protects chondrocytes from senescence by inhibiting
            clathrin-mediated endocytosis and activating of Notch signaling
  JOURNAL   Nat Commun 14 (1), 6190 (2023)
   PUBMED   37794006
  REMARK    GeneRIF: MYL3 protects chondrocytes from senescence by inhibiting
            clathrin-mediated endocytosis and activating of Notch signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Gerber,S.D., Beauchamp,P., Zhuang,L., Villiger,P.M. and Trueb,B.
  TITLE     Functional domains of the FgfrL1 receptor
  JOURNAL   Dev Biol 461 (1), 43-54 (2020)
   PUBMED   31923383
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Agarwal,M., Sharma,A., Kumar,P., Kumar,A., Bharadwaj,A., Saini,M.,
            Kardon,G. and Mathew,S.J.
  TITLE     Myosin heavy chain-embryonic regulates skeletal muscle
            differentiation during mammalian development
  JOURNAL   Development 147 (7) (2020)
   PUBMED   32094117
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Gao,R., Liang,X., Cheedipudi,S., Cordero,J., Jiang,X., Zhang,Q.,
            Caputo,L., Gunther,S., Kuenne,C., Ren,Y., Bhattacharya,S., Yuan,X.,
            Barreto,G., Chen,Y., Braun,T., Evans,S.M., Sun,Y. and Dobreva,G.
  TITLE     Pioneering function of Isl1 in the epigenetic control of
            cardiomyocyte cell fate
  JOURNAL   Cell Res 29 (6), 486-501 (2019)
   PUBMED   31024170
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Houzelstein,D., Lyons,G.E., Chamberlain,J. and Buckingham,M.E.
  TITLE     Localization of dystrophin gene transcripts during mouse
            embryogenesis
  JOURNAL   J Cell Biol 119 (4), 811-821 (1992)
   PUBMED   1429837
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Keller,A., Ott,M.O., Lamande,N., Lucas,M., Gros,F., Buckingham,M.
            and Lazar,M.
  TITLE     Activation of the gene encoding the glycolytic enzyme beta-enolase
            during early myogenesis precedes an increased expression during
            fetal muscle development
  JOURNAL   Mech Dev 38 (1), 41-54 (1992)
   PUBMED   1525038
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Lyons,G.E., Buckingham,M.E., Tweedie,S. and Edwards,Y.H.
  TITLE     Carbonic anhydrase III, an early mesodermal marker, is expressed in
            embryonic mouse skeletal muscle and notochord
  JOURNAL   Development 111 (1), 233-244 (1991)
   PUBMED   1901785
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Lyons,G.E., Schiaffino,S., Sassoon,D., Barton,P. and Buckingham,M.
  TITLE     Developmental regulation of myosin gene expression in mouse cardiac
            muscle
  JOURNAL   J Cell Biol 111 (6 Pt 1), 2427-2436 (1990)
   PUBMED   2277065
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Lyons,G.E., Ontell,M., Cox,R., Sassoon,D. and Buckingham,M.
  TITLE     The expression of myosin genes in developing skeletal muscle in the
            mouse embryo
  JOURNAL   J Cell Biol 111 (4), 1465-1476 (1990)
   PUBMED   2211821
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK146943.1, AK002312.1 and AV015350.1.
            
            On May 4, 2006 this sequence version replaced XP_984544.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061222.1, AK146943.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849376
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 60.69 cM"
     Protein         1..204
                     /product="myosin light chain 3"
                     /note="myosin, light polypeptide 3, alkali; ventricular,
                     skeletal, slow; myosin light chain, alkali, cardiac
                     ventricles"
                     /calculated_mol_wt=22290
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09542.4)"
     Site            2
                     /site_type="methylation"
                     /note="N,N,N-trimethylalanine, by NTM1.
                     /evidence=ECO:0000269|PubMed:20668449; propagated from
                     UniProtKB/Swiss-Prot (P09542.4)"
     Region          53..203
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P16409; propagated from
                     UniProtKB/Swiss-Prot (P09542.4)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P09542.4)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P16409; propagated from
                     UniProtKB/Swiss-Prot (P09542.4)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P16409; propagated from
                     UniProtKB/Swiss-Prot (P09542.4)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P09542.4)"
     CDS             1..204
                     /gene="Myl3"
                     /gene_synonym="MLC1s; MLC1SB; MLC1v; Mylc; VLC1"
                     /coded_by="NM_010859.3:68..682"
                     /db_xref="CCDS:CCDS23571.1"
                     /db_xref="GeneID:17897"
                     /db_xref="MGI:MGI:97268"
ORIGIN      
        1 mapkkpepkk ddakaaapka apapaaapaa apaaapeper pkeaefdask ikieftpeqi
       61 eefkeafllf drtpkgemki tygqcgdvlr algqnptqae vlrvlgkpkq eelnskmmdf
      121 etflpmlqhi sknkdtgtye dfveglrvfd kegngtvmga elrhvlatlg erltedevek
      181 lmagqedsng cinyeafvkh imas
//
LOCUS       NP_057726               3674 aa            linear   PRI 27-APR-2025
DEFINITION  spectrin beta chain, non-erythrocytic 5 [Homo sapiens].
ACCESSION   NP_057726
VERSION     NP_057726.4
DBSOURCE    REFSEQ: accession NM_016642.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3674)
  AUTHORS   Cortese,M., Papal,S., Pisciottano,F., Elgoyhen,A.B., Hardelin,J.P.,
            Petit,C., Franchini,L.F. and El-Amraoui,A.
  TITLE     Spectrin betaV adaptive mutations and changes in subcellular
            location correlate with emergence of hair cell electromotility in
            mammalians
  JOURNAL   Proc Natl Acad Sci U S A 114 (8), 2054-2059 (2017)
   PUBMED   28179572
  REMARK    GeneRIF: Adaptive mutations of spectrin-betaV occurred in the
            mammalian lineage and were accompanied with substantial changes in
            the protein distribution within inner ear hair cells.
REFERENCE   2  (residues 1 to 3674)
  AUTHORS   Papal,S., Cortese,M., Legendre,K., Sorusch,N., Dragavon,J.,
            Sahly,I., Shorte,S., Wolfrum,U., Petit,C. and El-Amraoui,A.
  TITLE     The giant spectrin betaV couples the molecular motors to
            phototransduction and Usher syndrome type I proteins along their
            trafficking route
  JOURNAL   Hum Mol Genet 22 (18), 3773-3788 (2013)
   PUBMED   23704327
  REMARK    GeneRIF: study identified spectrin betaV as a myosin VIIa- and
            rhodopsin-interacting partner in photoreceptor cells; suggest that
            spectrin betaV homomers couple some USH1 proteins, opsin and other
            phototransduction proteins to both actin- and microtubule-based
            motors, thereby contributing to their transport towards the
            photoreceptor outer disks
REFERENCE   3  (residues 1 to 3674)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 3674)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with ischemic stroke in Japanese
            individuals with or without metabolic syndrome
  JOURNAL   Int J Mol Med 25 (2), 281-286 (2010)
   PUBMED   20043139
  REMARK    GeneRIF: The initial chi-square test revealed that the Cright
            curved arrow T polymorphism of CLEC16A and the Aright curved arrow
            G polymorphism of SPTBN5 were significantly ssociated with ischemic
            stroke among individuals with metabolic syndrome.
REFERENCE   5  (residues 1 to 3674)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 3674)
  AUTHORS   Odell,A.F., Van Helden,D.F. and Scott,J.L.
  TITLE     The spectrin cytoskeleton influences the surface expression and
            activation of human transient receptor potential channel 4 channels
  JOURNAL   J Biol Chem 283 (7), 4395-4407 (2008)
   PUBMED   18048348
  REMARK    GeneRIF: interaction of hTRPC4 with alphaII-spectrin and
            betaV-spectrin was confirmed by glutathione S-transferase pulldown
            and co-immunoprecipitation experiments
REFERENCE   7  (residues 1 to 3674)
  AUTHORS   Stabach,P.R. and Morrow,J.S.
  TITLE     Identification and characterization of beta V spectrin, a mammalian
            ortholog of Drosophila beta H spectrin
  JOURNAL   J Biol Chem 275 (28), 21385-21395 (2000)
   PUBMED   10764729
REFERENCE   8  (residues 1 to 3674)
  AUTHORS   Chardin,P., Camonis,J.H., Gale,N.W., van Aelst,L., Schlessinger,J.,
            Wigler,M.H. and Bar-Sagi,D.
  TITLE     Human Sos1: a guanine nucleotide exchange factor for Ras that binds
            to GRB2
  JOURNAL   Science 260 (5112), 1338-1343 (1993)
   PUBMED   8493579
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF233523.1, AC020659.5 and AA599654.1.
            
            On May 3, 2013 this sequence version replaced NP_057726.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF233523.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000320955.8/ ENSP00000317790.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3674
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1"
     Protein         1..3674
                     /product="spectrin beta chain, non-erythrocytic 5"
                     /note="beta V spectrin; spectrin beta chain, brain 4;
                     spectrin, non-erythroid beta chain 4"
                     /calculated_mol_wt=416621
     Region          1..279
                     /region_name="Actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          36..160
                     /region_name="CH_SPTBN5_rpt1"
                     /note="first calponin homology (CH) domain found in
                     spectrin beta chain, non-erythrocytic 5 (SPTBN5) and
                     similar proteins; cd21247"
                     /db_xref="CDD:409096"
     Site            order(37..38,41,44..45,48..49,52..53,56,112,115..116,119,
                     126,130..138,145..146,148..149,152..153,156..157)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409096"
     Region          175..283
                     /region_name="CH_SPTBN5_rpt2"
                     /note="second calponin homology (CH) domain found in
                     spectrin beta chain, non-erythrocytic 5 (SPTBN5) and
                     similar proteins; cd21249"
                     /db_xref="CDD:409098"
     Site            order(179,183,233,235..236,239,246,251..259,268..269,
                     271..272,275..276,279)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409098"
     Region          307..416
                     /region_name="Spectrin 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          311..532
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Site            order(417..421,430)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          427..639
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          428..529
                     /region_name="Spectrin 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Site            532..537
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          642..742
                     /region_name="Spectrin 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          643..>810
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            744..749
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          747..810
                     /region_name="Spectrin 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          749..999
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            895..900
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          900..996
                     /region_name="Spectrin 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          1005..1206
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            1101..1106
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1103..1206
                     /region_name="Spectrin 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          1209..1418
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          1209..1311
                     /region_name="Spectrin 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Site            1313..1318
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1315..1417
                     /region_name="Spectrin 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          1430..1517
                     /region_name="SPEC"
                     /note="Spectrin repeats; smart00150"
                     /db_xref="CDD:197544"
     Region          1441..1469
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          1521..1727
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          1521..1624
                     /region_name="Spectrin 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Site            1625..1630
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1628..1835
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          1628..1727
                     /region_name="Spectrin 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Site            1729..1734
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1731..1835
                     /region_name="Spectrin 11. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          1841..2048
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          1842..1940
                     /region_name="Spectrin 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Site            1942..1947
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1944..2046
                     /region_name="Spectrin 13. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          2050..2253
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          2052..2146
                     /region_name="Spectrin 14. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Site            2148..2153
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2150..2253
                     /region_name="Spectrin 15. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          2256..2361
                     /region_name="Spectrin 16. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          2257..2470
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            2363..2368
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2366..2467
                     /region_name="Spectrin 17. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          2471..2680
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          2471..2574
                     /region_name="Spectrin 18. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Site            2575..2580
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2577..2680
                     /region_name="Spectrin 19. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          2585..2786
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            2681..2686
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2683..2784
                     /region_name="Spectrin 20. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          2788..2992
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          2791..2890
                     /region_name="Spectrin 21. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Site            2892..2897
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2894..3099
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          2894..2997
                     /region_name="Spectrin 22. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Site            2998..3003
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          3000..3103
                     /region_name="Spectrin 23. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          3007..3212
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            3104..3109
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          3106..3209
                     /region_name="Spectrin 24. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          3213..3415
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          3213..3311
                     /region_name="Spectrin 25. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Site            3313..3318
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          3318..3415
                     /region_name="Spectrin 26. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          3422..3488
                     /region_name="Spectrin 27. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRC6.2)"
     Region          3423..>3482
                     /region_name="SPEC"
                     /note="Spectrin repeats; smart00150"
                     /db_xref="CDD:197544"
     Region          3536..3636
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     CDS             1..3674
                     /gene="SPTBN5"
                     /gene_synonym="BSPECV; HUBSPECV; HUSPECV"
                     /coded_by="NM_016642.4:205..11229"
                     /db_xref="CCDS:CCDS61599.1"
                     /db_xref="GeneID:51332"
                     /db_xref="HGNC:HGNC:15680"
                     /db_xref="MIM:605916"
ORIGIN      
        1 magqphspre llgaaghrsr rpstelrvpp spsltmdsqy etghirklqa rhmqmqektf
       61 tkwinnvfqc gqagikirnl yteladgihl lrllelisge alpppsrgrl rvhflenssr
      121 alaflrakvp vpligpeniv dgdqtlilgl iwviilrfqi shisldkeef gasaallstk
      181 eallvwcqrk tasytnvnit dfsrswsdgl gfnalihahr pdlldygslr pdrplhnlaf
      241 aflvaeqelg iaqlldpedv aaaqpdersi mtyvslyyhy csrlhqgqtv qrrltkillq
      301 lqetellqtq yeqlvadllr wiaekqmqle ardfpdslpa mrqllaafti frtqekpprl
      361 qqrgaaeall frlqtalqaq nrrpflpheg lglaelsqcw aglewaeaar sqalqqrllq
      421 lqrletlarr fqhkaalres flkdaeqvld qarappasla tveaavqrlg mleagilpqe
      481 grfqalaeia dilrqeqyhs wadvarrqee vtvrwqrllq hlqgqrkqva dmqavlsllq
      541 eveaashqle elqeparsta cgqqlaevve llqrhdllea qvsahgahvs hlaqqtaeld
      601 sslgtsvevl qakartlaql qqslvalvra rralleqtlq raeflrncee eeawlkecgq
      661 rvgnaalgrd lsqiagalqk hkaleaevhr hqavcvdlvr rgrdlsarrp ptqpdpgera
      721 eavqggwqll qtrvvgrgar lqtallvlqy fadaaeaasw lrerrssler ascgqdqaaa
      781 etllrrhvrl ervlrafaae lrrleeqgra asaraslftv nsalsppges lrnpgpwsea
      841 schpgpgdaw kmalpaepdp dfdpntilqt qdhlsqdyes lralaqlrra rleeamalfg
      901 fcsscgelql wlekqtvllq rvqpqadtle vmqlkyenfl talavgkglw aevsssaeql
      961 rqrypgnstq iqrqqeelsq rwgqlealkr ekavqlahsv evcsflqecg ptqvqlrdvl
     1021 lqlealqpgs sedtchalql aqkktlvler rvhflqsvvv kveepgyaes qplqgqvetl
     1081 qgllkqvqeq vaqrarrqae tqarqsflqe sqqlllwaes vqaqlrskev svdvasaqrl
     1141 lrehqdllee ihlwqerlqq ldaqsqpmaa ldcpdsqevp ntlrvlgqqg qelkvlweqr
     1201 qqwlqeglel qkfgrevdgf tatcanhqaw lhldnlgedv realsllqqh refgrllstl
     1261 gpraealrah geklvqsqhp aahtvreqlq siqaqwtrlq grseqrrrql laslqlqewk
     1321 qdvaelmqwm eekglmaahe psgarrnilq tlkrheaaes ellatrrhve alqqvgrell
     1381 srrpcgqedi qtrlqglrsk wealnrkmte rgdelqqagq qeqllrqlqd akeqleqleg
     1441 alqssetgqd lrssqrlqkr hqqlesesrt laakmaalas mahgmaaspa ileetqkhlr
     1501 rlellqghla irglqlqasv elhqfchlsn melswvaehm phgsptsyte clngaqslhr
     1561 khkelqvevk ahqgqvqrvl ssgrslaasg hpqaqhiveq cqeleghwae leracearaq
     1621 clqqavtfqq yfldvseleg wveekrplvs srdygrdeaa tlrlinkhqa lqeelaiyws
     1681 smeeldqtaq tltgpevpeq qrvvqerlre qlralqelaa trdrelegtl rlheflreae
     1741 dlqgwlasqk qaakggeslg edpehalhlc tkfakfqhqv emgsqrvaac rllaesller
     1801 ghsagpmvrq rqqdlqtaws elweltqarg halrdtettl rvhrdllevl tqvqekatsl
     1861 pnnvardlcg leaqlrshqg lerelvgter qlqelletag rvqklcpgpq ahavqqrqqa
     1921 vtqawavlqr rmeqrraqle rarllarfrt avrdyaswaa rvrqdlqvee ssqepssgpl
     1981 klsahqwlra eleareklwq qatqlgqqal laagtptkev qeelralqdq rdqvyqtwar
     2041 kqerlqaeqq eqlflrecgr leeilaaqev slktsalgss veeveqlirk hevflkvlta
     2101 qdkkeaalre rlktlrrprv rdrlpillqr rmrvkelaes rghalhasll masftqaatq
     2161 aedwiqawaq qlkepvppgd lrdklkpllk hqafeaevqa heevmtsvak kgeallaqsh
     2221 pragevsqrl qglrkhwedl rqamalrgqe ledrrnflef lqrvdlaeaw iqekevkmnv
     2281 gdlgqdlehc lqlrrrlref rgnsagdtvg dacirsisdl slqlknrdpe evkiicqrrs
     2341 qlnnrwasfh gnllryqqql egaleihvls reldnvtkri qekealiqal dcgkdlesvq
     2401 rllrkheele revhpiqaqv eslerevgrl cqrspeaahg lrhrqqevae swwqlrsraq
     2461 krrealdalh qaqklqamlq ellvsaqrlr aqmdtspapr spvearrmle ehqeckaeld
     2521 swtdsislar stgqqlltag hpfssdirqv lagleqelss legawqehql qlqqalelql
     2581 flssvekmer wlcskedsla seglwdplap mepllwkhkm lewdlevqag kisaleatar
     2641 glhqgghpea qsalgrcqam llrkealfrq agtrrhrlee lrqlqaflqd sqevaawlre
     2701 knlvaleegl ldtamlpaql qkqqnfqael dasmhqqqel qregqrllqg ghpaseaiqe
     2761 rleelgalwg elqdnsqkkv aklqkaceal rlrrsmeele nwlepievel raptvgqalp
     2821 gvgellgtqr eleaavdkka rqaeallgqa qafvreghcl aqdveeqarr llqrfkslre
     2881 plqerrtale arslllkffr dadeemawvq eklplaaaqd ygqslsavrh lqeqhqnles
     2941 emsshealtr vvlgtgyklv qaghfaahev aarvqqleka mahlraeaar rrlllqqaqe
     3001 aqqfltelle agswlaergh vldsedmghs aeatqallrr leatkrdlea fsprierlqq
     3061 taallesrkn pespkvlaql qavreahael lrraearghg lqeqlqlhql eretllldaw
     3121 lttkaataes qdygqdlegv kvleekfdaf rkevqslgqa kvyalrklag tlergaprry
     3181 phiqaqrsri eaawerldqa ikartenlaa ahevhsfqqa aaelqgrmqe ktalmkgedg
     3241 ghslssvrtl qqqhrrlere leamekevar lqteacrlgq lhpaapggla kvqeawatlq
     3301 akaqergqwl aqaaqghafl grcqellawa qerqelasse elaedvagae qllgqheelg
     3361 qeirecrlqa qdlrqegqql vdnshfmsae vteclqeleg rlqeleeawa lrwqrcaesw
     3421 glqklrqrle qaeawlacwe glllkpdygh svsdvelllh rhqdleklla aqeekfaqmq
     3481 ktemeqelll qpqelkpgra gssltsfqwr psghqglgaq laetrdpqda kgtptmegsl
     3541 efkqhllpgg rqpsssswds crgnlqgssl slfldermaa ekvasialld ltgarcerlr
     3601 grhgrkhtfs lrltsgaeil faapseeqae swwralgsta aqslspklka kpvsslnect
     3661 tkdarpgcll rsdp
//
LOCUS       NP_001635                236 aa            linear   PRI 27-APR-2025
DEFINITION  C->U-editing enzyme APOBEC-1 isoform a [Homo sapiens].
ACCESSION   NP_001635
VERSION     NP_001635.2
DBSOURCE    REFSEQ: accession NM_001644.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wang,S., Kim,K., Gelvez,N., Chung,C., Gout,J.F., Fixman,B.,
            Vermulst,M. and Chen,X.S.
  TITLE     Identification of RBM46 as a novel APOBEC1 cofactor for C-to-U
            RNA-editing activity
  JOURNAL   J Mol Biol 435 (24), 168333 (2023)
   PUBMED   38708190
  REMARK    GeneRIF: Identification of RBM46 as a novel APOBEC1 cofactor for
            C-to-U RNA-editing activity.
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Wang,Y., Robinson,P.S., Coorens,T.H.H., Moore,L., Lee-Six,H.,
            Noorani,A., Sanders,M.A., Jung,H., Katainen,R., Heuschkel,R.,
            Brunton-Sim,R., Weston,R., Read,D., Nobbs,B., Fitzgerald,R.C.,
            Saeb-Parsy,K., Martincorena,I., Campbell,P.J., Rushbrook,S.,
            Zilbauer,M., Buczacki,S.J.A. and Stratton,M.R.
  TITLE     APOBEC mutagenesis is a common process in normal human small
            intestine
  JOURNAL   Nat Genet 55 (2), 246-254 (2023)
   PUBMED   36702998
  REMARK    GeneRIF: APOBEC mutagenesis is a common process in normal human
            small intestine.
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Kim,K., Calabrese,P., Wang,S., Qin,C., Rao,Y., Feng,P. and
            Chen,X.S.
  TITLE     The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations,
            replication and fitness
  JOURNAL   Sci Rep 12 (1), 14972 (2022)
   PUBMED   36100631
  REMARK    GeneRIF: The roles of APOBEC-mediated RNA editing in SARS-CoV-2
            mutations, replication and fitness.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Yu,W., Li,J., Huang,S., Li,X., Li,P., Li,G., Liang,A., Chi,T. and
            Huang,X.
  TITLE     Harnessing A3G for efficient and selective C-to-T conversion at
            C-rich sequences
  JOURNAL   BMC Biol 19 (1), 34 (2021)
   PUBMED   33602235
  REMARK    GeneRIF: Harnessing A3G for efficient and selective C-to-T
            conversion at C-rich sequences.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Wong,L., Vizeacoumar,F.S., Vizeacoumar,F.J. and Chelico,L.
  TITLE     APOBEC1 cytosine deaminase activity on single-stranded DNA is
            suppressed by replication protein A
  JOURNAL   Nucleic Acids Res 49 (1), 322-339 (2021)
   PUBMED   33330905
  REMARK    GeneRIF: APOBEC1 cytosine deaminase activity on single-stranded DNA
            is suppressed by replication protein A.
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Anant,S., MacGinnitie,A.J. and Davidson,N.O.
  TITLE     apobec-1, the catalytic subunit of the mammalian apolipoprotein B
            mRNA editing enzyme, is a novel RNA-binding protein
  JOURNAL   J Biol Chem 270 (24), 14762-14767 (1995)
   PUBMED   7782342
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Navaratnam,N., Bhattacharya,S., Fujino,T., Patel,D., Jarmuz,A.L.
            and Scott,J.
  TITLE     Evolutionary origins of apoB mRNA editing: catalysis by a cytidine
            deaminase that has acquired a novel RNA-binding motif at its active
            site
  JOURNAL   Cell 81 (2), 187-195 (1995)
   PUBMED   7736571
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Davidson,N.O., Innerarity,T.L., Scott,J., Smith,H., Driscoll,D.M.,
            Teng,B. and Chan,L.
  TITLE     Proposed nomenclature for the catalytic subunit of the mammalian
            apolipoprotein B mRNA editing enzyme: APOBEC-1
  JOURNAL   RNA 1 (1), 3 (1995)
   PUBMED   7489485
REFERENCE   9  (residues 1 to 236)
  AUTHORS   Espinosa,R. 3rd, Funahashi,T., Hadjiagapiou,C., Le Beau,M.M. and
            Davidson,N.O.
  TITLE     Assignment of the gene encoding the human apolipoprotein B mRNA
            editing enzyme (APOBEC1) to chromosome 12p13.1
  JOURNAL   Genomics 24 (2), 414-415 (1994)
   PUBMED   7698776
REFERENCE   10 (residues 1 to 236)
  AUTHORS   Lau,P.P., Zhu,H.J., Baldini,A., Charnsangavej,C. and Chan,L.
  TITLE     Dimeric structure of a human apolipoprotein B mRNA editing protein
            and cloning and chromosomal localization of its gene
  JOURNAL   Proc Natl Acad Sci U S A 91 (18), 8522-8526 (1994)
   PUBMED   8078915
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006927.27, BC144708.1,
            U72891.1 and AI380263.1.
            
            On Mar 24, 2005 this sequence version replaced NP_001635.1.
            
            Summary: This gene encodes a member of the cytidine deaminase
            enzyme family. The encoded protein forms a multiple-protein editing
            holoenzyme with APOBEC1 complementation factor (ACF) and APOBEC1
            stimulating protein (ASP). This holoenzyme is involved in the
            editing of C-to-U nucleotide bases in apolipoprotein B and
            neurofibromatosis-1 mRNAs. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1 and 2
            both encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U72891.1, L25877.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA2142586 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000229304.5/
                                                ENSP00000229304.4
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..236
                     /product="C->U-editing enzyme APOBEC-1 isoform a"
                     /EC_number="3.5.4.36"
                     /note="C->U-editing enzyme APOBEC-1; apolipoprotein B mRNA
                     editing enzyme complex-1; apolipoprotein B mRNA-editing
                     enzyme 1; mRNA(cytosine(6666)) deaminase 1; apolipoprotein
                     B mRNA editing enzyme, catalytic polypeptide 1"
                     /calculated_mol_wt=28061
     Region          16..186
                     /region_name="NAD1"
                     /note="Novel AID APOBEC clade 1; pfam18778"
                     /db_xref="CDD:465865"
     CDS             1..236
                     /gene="APOBEC1"
                     /gene_synonym="APO1; APOBEC-1; BEDP; CDAR1; HEPR"
                     /coded_by="NM_001644.5:37..747"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8579.1"
                     /db_xref="GeneID:339"
                     /db_xref="HGNC:HGNC:604"
                     /db_xref="MIM:600130"
ORIGIN      
        1 mtsekgpstg dptlrrriep wefdvfydpr elrkeaclly eikwgmsrki wrssgknttn
       61 hvevnfikkf tserdfhpsm scsitwflsw spcwecsqai reflsrhpgv tlviyvarlf
      121 whmdqqnrqg lrdlvnsgvt iqimraseyy hcwrnfvnyp pgdeahwpqy pplwmmlyal
      181 elhciilslp pclkisrrwq nhltffrlhl qnchyqtipp hillatglih psvawr
//
LOCUS       NP_034647                254 aa            linear   ROD 27-APR-2025
DEFINITION  insulin-like growth factor-binding protein 4 precursor [Mus
            musculus].
ACCESSION   NP_034647 XP_984960
VERSION     NP_034647.1
DBSOURCE    REFSEQ: accession NM_010517.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Basu,S., Mautner,L., Whiting,K., Hasenpusch-Theil,K., Borkowska,M.
            and Theil,T.
  TITLE     Identification of Pappa and Sall3 as Gli3 direct target genes
            acting downstream of cilia signaling in corticogenesis
  JOURNAL   Cereb Cortex 34 (12) (2024)
   PUBMED   39716738
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Tao,L., Wang,Y., Shen,Z., Cai,J., Zheng,J., Xia,S., Lin,Z., Wan,Z.,
            Qi,H., Jin,R., Wang,L., Xu,J. and Liang,X.
  TITLE     Activation of IGFBP4 via unconventional mechanism of miRNA
            attenuates metastasis of intrahepatic cholangiocarcinoma
  JOURNAL   Hepatol Int 18 (1), 91-107 (2024)
   PUBMED   37349627
  REMARK    GeneRIF: Activation of IGFBP4 via unconventional mechanism of miRNA
            attenuates metastasis of intrahepatic cholangiocarcinoma.
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Chen,W., Hu,L., Lu,X., Wang,X., Zhao,C., Guo,C., Li,X., Ding,Y.,
            Zhao,H., Tong,D., Wang,L. and Huang,C.
  TITLE     The RNA binding protein MEX3A promotes tumor progression of breast
            cancer by post-transcriptional regulation of IGFBP4
  JOURNAL   Breast Cancer Res Treat 201 (3), 353-366 (2023)
   PUBMED   37433992
  REMARK    GeneRIF: The RNA binding protein MEX3A promotes tumor progression
            of breast cancer by post-transcriptional regulation of IGFBP4.
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Jepsen,M.R., Ostergaard,J.A., Conover,C.A., Wogensen,L., Birn,H.,
            Krag,S.P., Fenton,R.A. and Oxvig,C.
  TITLE     Increased activity of the metalloproteinase PAPP-A promotes
            diabetes-induced glomerular hypertrophy
  JOURNAL   Metabolism 132, 155218 (2022)
   PUBMED   35588861
  REMARK    GeneRIF: Increased activity of the metalloproteinase PAPP-A
            promotes diabetes-induced glomerular hypertrophy.
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Kheirollahi,V., Khadim,A., Kiliaris,G., Korfei,M., Barroso,M.M.,
            Alexopoulos,I., Vazquez-Armendariz,A.I., Wygrecka,M., Ruppert,C.,
            Guenther,A., Seeger,W., Herold,S. and El Agha,E.
  TITLE     Transcriptional Profiling of Insulin-like Growth Factor Signaling
            Components in Embryonic Lung Development and Idiopathic Pulmonary
            Fibrosis
  JOURNAL   Cells 11 (12), 1973 (2022)
   PUBMED   35741102
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Boney,C.M., Moats-Staats,B.M., Stiles,A.D. and D'Ercole,A.J.
  TITLE     Expression of insulin-like growth factor-I (IGF-I) and IGF-binding
            proteins during adipogenesis
  JOURNAL   Endocrinology 135 (5), 1863-1868 (1994)
   PUBMED   7525256
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Scharla,S.H., Strong,D.D., Mohan,S., Chevalley,T. and Linkhart,T.A.
  TITLE     Effect of tumor necrosis factor-alpha on the expression of
            insulin-like growth factor I and insulin-like growth factor binding
            protein 4 in mouse osteoblasts
  JOURNAL   Eur J Endocrinol 131 (3), 293-301 (1994)
   PUBMED   7522842
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Hahnel,A. and Schultz,G.A.
  TITLE     Insulin-like growth factor binding proteins are transcribed by
            preimplantation mouse embryos
  JOURNAL   Endocrinology 134 (4), 1956-1959 (1994)
   PUBMED   7511095
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Donahue,L.R., Watson,G. and Beamer,W.G.
  TITLE     Regulation of metabolic water and protein compartments by
            insulin-like growth factor-I and testosterone in growth
            hormone-deficient lit/lit mice
  JOURNAL   J Endocrinol 139 (3), 431-439 (1993)
   PUBMED   7510770
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Cerro,J.A., Grewal,A., Wood,T.L. and Pintar,J.E.
  TITLE     Tissue-specific expression of the insulin-like growth factor
            binding protein (IGFBP) mRNAs in mouse and rat development
  JOURNAL   Regul Pept 48 (1-2), 189-198 (1993)
   PUBMED   7505465
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591067.35 and AI838737.1.
            
            On May 4, 2006 this sequence version replaced XP_984960.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK031212.1, BC019836.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 62.92 cM"
     Protein         1..254
                     /product="insulin-like growth factor-binding protein 4
                     precursor"
                     /note="IGF-binding protein 4; differentially expressed in
                     B16F10 2; Band 3A"
                     /calculated_mol_wt=25761
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2065
     mat_peptide     22..254
                     /product="Insulin-like growth factor-binding protein 4.
                     /id=PRO_0000014383"
                     /note="propagated from UniProtKB/Swiss-Prot (P47879.2)"
                     /calculated_mol_wt=25761
     Region          25..101
                     /region_name="IB"
                     /note="Insulin growth factor-binding protein homologues;
                     smart00121"
                     /db_xref="CDD:197525"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47879.2)"
     Region          170..245
                     /region_name="Thyroglobulin_1"
                     /note="Thyroglobulin type-1 repeat; pfam00086"
                     /db_xref="CDD:459665"
     Site            order(174,195,213,221)
                     /site_type="active"
                     /note="protease interaction site [active]"
                     /db_xref="CDD:238114"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P22692; propagated from
                     UniProtKB/Swiss-Prot (P47879.2)"
     CDS             1..254
                     /gene="Igfbp4"
                     /gene_synonym="Deb2; IBP-4; IGFBP-4"
                     /coded_by="NM_010517.4:254..1018"
                     /db_xref="CCDS:CCDS25371.1"
                     /db_xref="GeneID:16010"
                     /db_xref="MGI:MGI:96439"
ORIGIN      
        1 mlpfglvaal llaagprpsl gdeaihcppc seeklarcrp pvgceelvre pgcgccatca
       61 lglgmpcgvy tprcgsgmrc ypprgvekpl rtlmhgqgvc telseieaiq eslqtsdkde
      121 sehpnnsfnp csahdhrclq khmakirdrs kmkivgtpre eprpvpqgsc qselhraler
      181 laasqsrthe dlfiipipnc drngnfhpkq chpaldgqrg kcwcvdrktg vklpgglepk
      241 geldchqlad sfqe
//
LOCUS       NP_001347673             156 aa            linear   ROD 27-APR-2025
DEFINITION  acyl carrier protein, mitochondrial precursor [Mus musculus].
ACCESSION   NP_001347673 XP_006508263
VERSION     NP_001347673.1
DBSOURCE    REFSEQ: accession NM_001360744.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Vercellino,I. and Sazanov,L.A.
  TITLE     SCAF1 drives the compositional diversity of mammalian respirasomes
  JOURNAL   Nat Struct Mol Biol 31 (7), 1061-1071 (2024)
   PUBMED   38575788
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Zhang,R., Hou,T., Cheng,H. and Wang,X.
  TITLE     NDUFAB1 protects against obesity and insulin resistance by
            enhancing mitochondrial metabolism
  JOURNAL   FASEB J 33 (12), 13310-13322 (2019)
   PUBMED   31530015
  REMARK    GeneRIF: Skeletal muscle-specific ablation of NDUFAB1 disrupts
            glucose homeostasis and results in obesity and insulin resistance.
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Boniecki,M.T., Freibert,S.A., Muhlenhoff,U., Lill,R. and Cygler,M.
  TITLE     Structure and functional dynamics of the mitochondrial Fe/S cluster
            synthesis complex
  JOURNAL   Nat Commun 8 (1), 1287 (2017)
   PUBMED   29097656
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Gakh,O., Ranatunga,W., Smith,D.Y. 4th, Ahlgren,E.C.,
            Al-Karadaghi,S., Thompson,J.R. and Isaya,G.
  TITLE     Architecture of the Human Mitochondrial Iron-Sulfur Cluster
            Assembly Machinery
  JOURNAL   J Biol Chem 291 (40), 21296-21321 (2016)
   PUBMED   27519411
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Wirtz,S. and Schuelke,M.
  TITLE     Region-specific expression of mitochondrial complex I genes during
            murine brain development
  JOURNAL   PLoS One 6 (4), e18897 (2011)
   PUBMED   21556144
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Wertz,K. and Herrmann,B.G.
  TITLE     Large-scale screen for genes involved in gonad development
  JOURNAL   Mech Dev 98 (1-2), 51-70 (2000)
   PUBMED   11044607
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK010307.1 and AC124379.3.
            
            On Feb 10, 2018 this sequence version replaced XP_006508263.1.
            
            Transcript Variant: This variant (3) differs in the 3' UTR compared
            to variant 1. Variants 1, 2, and 3 all encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK152995.1, AK151719.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164134, SAMN01164136
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 65.38 cM"
     Protein         1..156
                     /product="acyl carrier protein, mitochondrial precursor"
                     /note="acyl carrier protein, mitochondrial;
                     NADH-ubiquinone oxidoreductase 9.6 kDa subunit; NADH
                     dehydrogenase (ubiquinone) 1, alpha/beta subcomplex, 1"
                     /calculated_mol_wt=10096
     transit_peptide 1..68
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9CR21.1)"
                     /calculated_mol_wt=7293
     Region          <66..152
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; cl09936"
                     /db_xref="CDD:447865"
     mat_peptide     69..156
                     /product="Acyl carrier protein, mitochondrial.
                     /id=PRO_0000000562"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CR21.1)"
                     /calculated_mol_wt=10096
     Site            88
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CR21.1)"
     CDS             1..156
                     /gene="Ndufab1"
                     /gene_synonym="2210401F17Rik; 2310039H15Rik;
                     2610003B19Rik; 8kDa; 9130423F15Rik; ACP; CI-SDAP; SDAP"
                     /coded_by="NM_001360744.1:27..497"
                     /db_xref="CCDS:CCDS21809.1"
                     /db_xref="GeneID:70316"
                     /db_xref="MGI:MGI:1917566"
ORIGIN      
        1 masrvlcacv rrlpaafapl prlptlalar plsttlcpeg irrrpgalqs alalaqvpgt
       61 vthlcrqysd appltldgik drvlyvlkly dkidpeklsv nshfmkdlgl dsldqveiim
      121 amedefgfei pdidaeklmc pqeivdyiad kkdvye
//
LOCUS       NP_001353498             917 aa            linear   PRI 27-APR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001353498 XP_005245775
VERSION     NP_001353498.1
DBSOURCE    REFSEQ: accession NM_001366569.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 917)
  AUTHORS   Chwalenia,K., Qin,F., Singh,S. and Li,H.
  TITLE     A cell-based splicing reporter system to identify regulators of
            cis-splicing between adjacent genes
  JOURNAL   Nucleic Acids Res 47 (4), e24 (2019)
   PUBMED   30590765
  REMARK    GeneRIF: We discovered that two factors, SRRM1 and SF3B1, affect
            not only cis-SAGe chimeras, but also other types of chimeric RNAs
            in a genome-wide fashion.
REFERENCE   5  (residues 1 to 917)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   6  (residues 1 to 917)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 917)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 917)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 917)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 917)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_005245775.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.229491.1,
                                           SRR1660805.118199.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..917
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 7"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=103721
     Region          1..156
                     /region_name="Necessary for mRNA 3'-end cleavage and
                     cytoplasmic accumulation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          1..151
                     /region_name="Necessary for DNA and RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          <414..743
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            587
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          <619..>753
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            651
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            707
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            731
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            753
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            765
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            769
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            782
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            790
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            804
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            806
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            815
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            885
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     CDS             1..917
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366569.1:26..2779"
                     /note="isoform 7 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS90885.1"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkekt pelpepsvkv kepsvqeats
      241 tsdilkvpkp epipepkeps peknskkeke kektrprsrs rsksrsrtrs rspshtrprr
      301 rhrsrsrsys prrrpsprrr psprrrtppr rmpppprhrr srspvrrrrr ssaslsgsss
      361 sssssrsrsp pkkppkrtss pprktrrlsp saspprrrhr psppatpppk trhsptpqqs
      421 nrtrksrvsv spgrtsgkvt khkgtekres pspapkprkv elsesedkgg kmaaadsvqq
      481 rrqyrrqnqq sssdsgssss sederpkrsh vkngevgrrr rhspsrsasp sprkrqkets
      541 prmqmgkrwq spvtksgrrr rspsppptrr rrspspappp rrrrtptppp rrrtpspppr
      601 rrspsprrys ppiqrrysps pppkrrtasp ppppkrrasp spppkrrvsh spppkqrssp
      661 vtkrrspsls skhrkgssps rstrearspq pnkrhspspr prapqtsssp ppvrrgasss
      721 pqrrqspsps trpirrvsrt pepkkikkaa spspqsvrrv sssrsvsgsp epaakkppap
      781 pspvqsqsps tnwspavpvk kaksptpsps pprnsdqegg gkkkkkkkdk khkkdkkhkk
      841 hkkhkkekav aaaaaaavtp aaiaaatttl aqeepvaape pkketeseae dnlddlekhl
      901 rekalrsmrk aqvspqs
//
LOCUS       NP_001356348             273 aa            linear   PRI 27-APR-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 3 [Homo sapiens].
ACCESSION   NP_001356348
VERSION     NP_001356348.1
DBSOURCE    REFSEQ: accession NM_001369419.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
            Review article
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Du,P., Li,G., Wu,L. and Huang,M.
  TITLE     Perspectives of ERCC1 in early-stage and advanced cervical cancer:
            From experiments to clinical applications
  JOURNAL   Front Immunol 13, 1065379 (2023)
   PUBMED   36713431
  REMARK    GeneRIF: Perspectives of ERCC1 in early-stage and advanced cervical
            cancer: From experiments to clinical applications.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 273)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 273)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139353.3 and AC092309.3.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2492152.1,
                                           SRR14038197.1285588.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..273
                     /product="DNA excision repair protein ERCC-1 isoform 3"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=29862
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          235..264
                     /region_name="HHH"
                     /note="Helix-hairpin-helix motif; pfam00633"
                     /db_xref="CDD:425789"
     CDS             1..273
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369419.1:155..976"
                     /note="isoform 3 is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS54279.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrsleqli
      241 aasredlalc pglgpqkarr lfdvlhepfl kvp
//
LOCUS       NP_001350383             191 aa            linear   ROD 27-APR-2025
DEFINITION  rho-related GTP-binding protein RhoH [Mus musculus].
ACCESSION   NP_001350383
VERSION     NP_001350383.1
DBSOURCE    REFSEQ: accession NM_001363454.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Peng,S., Stojkov,D., Gao,J., Oberson,K., Latzin,P., Casaulta,C.,
            Yousefi,S. and Simon,H.U.
  TITLE     Nascent RHOH acts as a molecular brake on actomyosin-mediated
            effector functions of inflammatory neutrophils
  JOURNAL   PLoS Biol 20 (9), e3001794 (2022)
   PUBMED   36108062
  REMARK    GeneRIF: Nascent RHOH acts as a molecular brake on
            actomyosin-mediated effector functions of inflammatory neutrophils.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Horiguchi,H., Xu,H., Duvert,B., Ciuculescu,F., Yao,Q., Sinha,A.,
            McGuinness,M., Harris,C., Brendel,C., Troeger,A., Chiarle,R. and
            Williams,D.A.
  TITLE     Deletion of murine Rhoh leads to de-repression of Bcl-6 via
            decreased KAISO levels and accelerates a malignancy phenotype in a
            murine model of lymphoma
  JOURNAL   Small GTPases 13 (1), 267-281 (2022)
   PUBMED   34983288
  REMARK    GeneRIF: Deletion of murine Rhoh leads to de-repression of Bcl-6
            via decreased KAISO levels and accelerates a malignancy phenotype
            in a murine model of lymphoma.
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Tamehiro,N., Nishida,K., Sugita,Y., Hayakawa,K., Oda,H., Nitta,T.,
            Nakano,M., Nishioka,A., Yanobu-Takanashi,R., Goto,M., Okamura,T.,
            Adachi,R., Kondo,K., Morita,A. and Suzuki,H.
  TITLE     Ras homolog gene family H (RhoH) deficiency induces psoriasis-like
            chronic dermatitis by promoting TH17 cell polarization
  JOURNAL   J Allergy Clin Immunol 143 (5), 1878-1891 (2019)
   PUBMED   30339851
  REMARK    GeneRIF: RhoH deficiency in mice induced TH17 polarization during
            effector T-cell differentiation, thereby inducing psoriasis-like
            chronic dermatitis
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Muro,R., Nitta,T., Nakano,K., Okamura,T., Takayanagi,H. and
            Suzuki,H.
  TITLE     gammadeltaTCR recruits the Syk/PI3K axis to drive proinflammatory
            differentiation program
  JOURNAL   J Clin Invest 128 (1), 415-426 (2018)
   PUBMED   29202478
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Fredenburgh,L.E., Liang,O.D., Macias,A.A., Polte,T.R., Liu,X.,
            Riascos,D.F., Chung,S.W., Schissel,S.L., Ingber,D.E.,
            Mitsialis,S.A., Kourembanas,S. and Perrella,M.A.
  TITLE     Absence of cyclooxygenase-2 exacerbates hypoxia-induced pulmonary
            hypertension and enhances contractility of vascular smooth muscle
            cells
  JOURNAL   Circulation 117 (16), 2114-2122 (2008)
   PUBMED   18391113
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Chae,H.D., Lee,K.E., Williams,D.A. and Gu,Y.
  TITLE     Cross-talk between RhoH and Rac1 in regulation of actin
            cytoskeleton and chemotaxis of hematopoietic progenitor cells
  JOURNAL   Blood 111 (5), 2597-2605 (2008)
   PUBMED   18089848
  REMARK    GeneRIF: An antagonistic role of RhoH in regulation of cortical
            F-actin assembly and chemotaxis via suppressing Rac1 membrane
            targeting and activation in primary hematopoietic progenitor cells,
            is identified.
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Dorn,T., Kuhn,U., Bungartz,G., Stiller,S., Bauer,M., Ellwart,J.,
            Peters,T., Scharffetter-Kochanek,K., Semmrich,M., Laschinger,M.,
            Holzmann,B., Klinkert,W.E., Straten,P.T., Kollgaard,T., Sixt,M. and
            Brakebusch,C.
  TITLE     RhoH is important for positive thymocyte selection and T-cell
            receptor signaling
  JOURNAL   Blood 109 (6), 2346-2355 (2007)
   PUBMED   17119112
  REMARK    GeneRIF: RhoH is important for pre-T-cell receptor and T-cell
            receptor signaling
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Gu,Y., Chae,H.D., Siefring,J.E., Jasti,A.C., Hildeman,D.A. and
            Williams,D.A.
  TITLE     RhoH GTPase recruits and activates Zap70 required for T cell
            receptor signaling and thymocyte development
  JOURNAL   Nat Immunol 7 (11), 1182-1190 (2006)
   PUBMED   17028588
  REMARK    GeneRIF: RhoH is a critical regulator of thymocyte development and
            TCR signaling by mediating recruitment and activation of Zap70.
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Gu,Y., Jasti,A.C., Jansen,M. and Siefring,J.E.
  TITLE     RhoH, a hematopoietic-specific Rho GTPase, regulates proliferation,
            survival, migration, and engraftment of hematopoietic progenitor
            cells
  JOURNAL   Blood 105 (4), 1467-1475 (2005)
   PUBMED   15494435
  REMARK    GeneRIF: RhoH serves as a negative regulator of both growth and
            actin-based function of hematopoietic progenitor cells possibly via
            suppression of Rac-mediated signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK138090.1, AC156029.2, AK137909.1 and AI448508.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK138090.1, ERR2680377.824708.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN01164135
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 33.8 cM"
     Protein         1..191
                     /product="rho-related GTP-binding protein RhoH"
                     /note="ras homolog gene family, member H"
                     /calculated_mol_wt=21193
     mat_peptide     1..188
                     /product="Rho-related GTP-binding protein RhoH.
                     /id=PRO_0000198868"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D3G9.1)"
                     /calculated_mol_wt=20936
     Region          5..169
                     /region_name="Rho"
                     /note="Ras homology family (Rho) of small guanosine
                     triphosphatases (GTPases); cd00157"
                     /db_xref="CDD:206641"
     Site            order(6,36..37,39..40,42,44,53,57..62,68,71)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206641"
     Site            11..18
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206641"
     Site            order(14..19,36,58..59,117,119,153..154)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206641"
     Region          33..41
                     /region_name="Effector region. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D3G9.1)"
     Site            order(35,37..38,62,68,71)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206641"
     Site            order(36..37,60,68,70..71)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206641"
     Site            36
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206641"
     Site            37..41
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206641"
     Site            order(38,68,71)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:206641"
     Site            58..61
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206641"
     Site            order(60..62,68..71,76..78)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206641"
     Region          73..86
                     /region_name="Interaction with ZAP70.
                     /evidence=ECO:0000269|PubMed:17028588"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9D3G9.1)"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206641"
     Site            152..154
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206641"
     Site            188
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9D3G9.1)"
     CDS             1..191
                     /gene="Rhoh"
                     /gene_synonym="5830400A04Rik; Arhh"
                     /coded_by="NM_001363454.1:775..1350"
                     /db_xref="CCDS:CCDS39100.1"
                     /db_xref="GeneID:74734"
                     /db_xref="MGI:MGI:1921984"
ORIGIN      
        1 mlssikcvlv gdsavgktsl lvrftsetfp eaykptvyen tgvdvfmdgi qislglwdta
       61 gndafrsirp lsyqqadvvl mcysvanhns flnlknkwis eirsnlpctp vlvvatqtdq
      121 revgphrasc inaiegkrla qdvrakgyle csalsnrgvq qvfecavrta vnqarrrnrr
      181 klfsinecki f
//
LOCUS       NP_001152765             536 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 737 [Homo sapiens].
ACCESSION   NP_001152765 NP_660332
VERSION     NP_001152765.1
DBSOURCE    REFSEQ: accession NM_001159293.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Bellefroid,E.J., Marine,J.C., Ried,T., Lecocq,P.J., Riviere,M.,
            Amemiya,C., Poncelet,D.A., Coulie,P.G., de Jong,P., Szpirer,C. et
            al.
  TITLE     Clustered organization of homologous KRAB zinc-finger genes with
            enhanced expression in human T lymphoid cells
  JOURNAL   EMBO J 12 (4), 1363-1374 (1993)
   PUBMED   8467795
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA043454.1, BC015765.1, AC008554.8 and AI857360.1.
            
            On Jul 31, 2014 this sequence version replaced NP_660332.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA147904.1, SRR1660809.25124.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148, SAMN03267759
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000427401.9/ ENSP00000395733.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p12"
     Protein         1..536
                     /product="zinc finger protein 737"
                     /note="zinc finger protein 102 (Y3)"
                     /calculated_mol_wt=61800
     Region          4..62
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          170..503
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          175..195
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(180,182,184,186..187,190..191,194,208,210,214..215,
                     218..219,222,236,238,240,242..243,246..247,250)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          203..223
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          231..251
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          259..279
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          287..307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          315..335
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(320,322,324,326..327,330..331,334,348,350,354..355,
                     358..359,362,376,378,380,382..383,386..387,390)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          343..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          371..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          399..419
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          427..447
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(432,434,436,438..439,442..443,446,460,462,466..467,
                     470..471,474,488,490,492,494..495,498..499,502)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          455..475
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          483..503
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          496..520
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          511..531
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..536
                     /gene="ZNF737"
                     /gene_synonym="ZNF102"
                     /coded_by="NM_001159293.2:142..1752"
                     /db_xref="CCDS:CCDS54238.1"
                     /db_xref="GeneID:100129842"
                     /db_xref="HGNC:HGNC:32468"
                     /db_xref="MIM:603984"
ORIGIN      
        1 mgplqfrdva iefsleewhc ldtaqrnlyr nvmlenyrnl vflgivvskp dlitcleqgk
       61 kpltmkkhem vanpsvtcsh fardlwpeqs ikdsfqkvtl rryenyghdn lqfkkgcesv
      121 deckvhkrgy nglnqylttt qskifqcdky vkvihkfsns nrhkirhtgk kpfkciecgk
      181 afnqsstltt hkkihtgekp fkceecgkaf nwsshltthk rihtgekryk cedcgkafsr
      241 fsyltahkii hsgekpykce ecgkafkrss nltthkiiht gekpykceec gkafkrssil
      301 tahkiihsge kpykceecgk afkhpsvltt hkrihtgekp ykceecgraf kyfssltthk
      361 iihsgekpyk ceecgkafnw sshltthkri htgekpykce ecgeafkyss sltthkiiht
      421 gqqpfkceec gkafkcfsil tthkrihtge kpykceecgk afnssshlta hkrihtgekp
      481 ykcercgkaf krsfiltrhk rihtgekpyk ceecgkgfkc pstltthkvi htgekl
//
LOCUS       NP_001353923             122 aa            linear   PRI 27-APR-2025
DEFINITION  interferon alpha-inducible protein 27, mitochondrial isoform 1
            [Homo sapiens].
ACCESSION   NP_001353923
VERSION     NP_001353923.1
DBSOURCE    REFSEQ: accession NM_001366994.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Oguz,A.K., Oygur,C.S., Tasir,S., Ozdag,H. and Akar,M.N.
  TITLE     Behcet syndrome: The disturbed balance between anti- (CLEC12A, CLC)
            and proinflammatory (IFI27) gene expressions
  JOURNAL   Immun Inflamm Dis 11 (4), e836 (2023)
   PUBMED   37102643
  REMARK    GeneRIF: Behcet syndrome: The disturbed balance between anti-
            (CLEC12A, CLC) and proinflammatory (IFI27) gene expressions.
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Jiang,C., He,C., Kan,J., Guan,H., Zhou,T. and Yang,Y.
  TITLE     Integrative bulk and single-cell transcriptome profiling analysis
            reveals IFI27 as a novel interferon-stimulated gene in dengue
  JOURNAL   J Med Virol 95 (4), e28706 (2023)
   PUBMED   36971141
  REMARK    GeneRIF: Integrative bulk and single-cell transcriptome profiling
            analysis reveals IFI27 as a novel interferon-stimulated gene in
            dengue.
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Shojaei,M., Shamshirian,A., Monkman,J., Grice,L., Tran,M.,
            Tan,C.W., Teo,S.M., Rodrigues Rossi,G., McCulloch,T.R., Nalos,M.,
            Raei,M., Razavi,A., Ghasemian,R., Gheibi,M., Roozbeh,F., Sly,P.D.,
            Spann,K.M., Chew,K.Y., Zhu,Y., Xia,Y., Wells,T.J., Senegaglia,A.C.,
            Kuniyoshi,C.L., Franck,C.L., Dos Santos,A.F.R., de Noronha,L.,
            Motamen,S., Valadan,R., Amjadi,O., Gogna,R., Madan,E.,
            Alizadeh-Navaei,R., Lamperti,L., Zuniga,F., Nova-Lamperti,E.,
            Labarca,G., Knippenberg,B., Herwanto,V., Wang,Y., Phu,A., Chew,T.,
            Kwan,T., Kim,K., Teoh,S., Pelaia,T.M., Kuan,W.S., Jee,Y.,
            Iredell,J., O'Byrne,K., Fraser,J.F., Davis,M.J., Belz,G.T.,
            Warkiani,M.E., Gallo,C.S., Souza-Fonseca-Guimaraes,F., Nguyen,Q.,
            Mclean,A., Kulasinghe,A., Short,K.R. and Tang,B.
  TITLE     IFI27 transcription is an early predictor for COVID-19 outcomes, a
            multi-cohort observational study
  JOURNAL   Front Immunol 13, 1060438 (2023)
   PUBMED   36685600
  REMARK    GeneRIF: IFI27 transcription is an early predictor for COVID-19
            outcomes, a multi-cohort observational study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Saini,J., Thapa,U., Bandyopadhyay,B., Vrati,S. and Banerjee,A.
  TITLE     Knockdown of NEAT1 restricts dengue virus replication by augmenting
            interferon alpha-inducible protein 27 via the RIG-I pathway
  JOURNAL   J Gen Virol 104 (1) (2023)
   PUBMED   36748518
  REMARK    GeneRIF: Knockdown of NEAT1 restricts dengue virus replication by
            augmenting interferon alpha-inducible protein 27 via the RIG-I
            pathway.
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Guo,M., Cao,W., Chen,S., Tian,R., Xue,B., Wang,L., Liu,Q., Deng,R.,
            Wang,X., Wang,Z., Zhang,Y., Yang,D., Zuo,C., Li,G., Tang,S. and
            Zhu,H.
  TITLE     TRIM21 Regulates Virus-Induced Cell Pyroptosis through
            Polyubiquitination of ISG12a
  JOURNAL   J Immunol 209 (10), 1987-1998 (2022)
   PUBMED   36426955
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Izmailova,E., Bertley,F.M., Huang,Q., Makori,N., Miller,C.J.,
            Young,R.A. and Aldovini,A.
  TITLE     HIV-1 Tat reprograms immature dendritic cells to express
            chemoattractants for activated T cells and macrophages
  JOURNAL   Nat Med 9 (2), 191-197 (2003)
   PUBMED   12539042
REFERENCE   7  (residues 1 to 122)
  AUTHORS   Martensen,P.M., Sogaard,T.M., Gjermandsen,I.M., Buttenschon,H.N.,
            Rossing,A.B., Bonnevie-Nielsen,V., Rosada,C., Simonsen,J.L. and
            Justesen,J.
  TITLE     The interferon alpha induced protein ISG12 is localized to the
            nuclear membrane
  JOURNAL   Eur J Biochem 268 (22), 5947-5954 (2001)
   PUBMED   11722583
REFERENCE   8  (residues 1 to 122)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 122)
  AUTHORS   Taules,M., Rius,E., Talaya,D., Lopez-Girona,A., Bachs,O. and
            Agell,N.
  TITLE     Calmodulin is essential for cyclin-dependent kinase 4 (Cdk4)
            activity and nuclear accumulation of cyclin D1-Cdk4 during G1
  JOURNAL   J Biol Chem 273 (50), 33279-33286 (1998)
   PUBMED   9837900
REFERENCE   10 (residues 1 to 122)
  AUTHORS   Rasmussen,U.B., Wolf,C., Mattei,M.G., Chenard,M.P., Bellocq,J.P.,
            Chambon,P., Rio,M.C. and Basset,P.
  TITLE     Identification of a new interferon-alpha-inducible gene (p27) on
            human chromosome 14q32 and its expression in breast carcinoma
  JOURNAL   Cancer Res 53 (17), 4096-4101 (1993)
   PUBMED   8358738
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL079302.7, AL121838.4 and KF573698.1.
            
            Transcript Variant: This variant (12) differs in the 5' UTR
            compared to variant 1. This variant represents an allele commonly
            found in the human population and corresponds to the allele present
            in the GRC reference assembly. Variants 1, 3, 5, 11 and 12 encode
            the same isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: ERR279855.1987.1, BM919299.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2142363 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..122
                     /product="interferon alpha-inducible protein 27,
                     mitochondrial isoform 1"
                     /note="2310061N23Rik; interferon alpha-inducible protein
                     27, mitochondrial; ISG12(a); interferon-stimulated gene
                     12a protein; interferon alpha-induced 11.5 kDa protein"
                     /calculated_mol_wt=8318
     transit_peptide 1..33
                     /note="Mitochondrion.
                     /evidence=ECO:0000305|PubMed:18330707; propagated from
                     UniProtKB/Swiss-Prot (P40305.4)"
                     /calculated_mol_wt=3242
     mat_peptide     34..122
                     /product="Interferon alpha-inducible protein 27,
                     mitochondrial. /id=PRO_0000147372"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
                     /calculated_mol_wt=8318
     Site            34..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
     Region          37..115
                     /region_name="Ifi-6-16"
                     /note="Interferon-induced 6-16 family; pfam06140"
                     /db_xref="CDD:461837"
     Site            71..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
     Region          76..122
                     /region_name="Mediates interaction with SKP2 and hepatitis
                     C virus non-structural protein NS5A.
                     /evidence=ECO:0000269|PubMed:27194766"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
     Region          103..112
                     /region_name="Required for hepatitis C virus
                     non-structural protein NS5A degradation.
                     /evidence=ECO:0000269|PubMed:27194766"
                     /note="propagated from UniProtKB/Swiss-Prot (P40305.4)"
     CDS             1..122
                     /gene="IFI27"
                     /gene_synonym="FAM14D; ISG12; ISG12A; P27"
                     /coded_by="NM_001366994.1:51..419"
                     /note="isoform 1 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS32148.1"
                     /db_xref="GeneID:3429"
                     /db_xref="HGNC:HGNC:5397"
                     /db_xref="MIM:600009"
ORIGIN      
        1 measaltssa vtsvakvvrv asgsavvlpl ariatvvigg vvamaavpmv lsamgftaag
       61 iasssiaakm msaaaiangg gvasgslvat lqslgatgls gltkfilgsi gsaiaaviar
      121 fy
//
LOCUS       NP_001353555             178 aa            linear   PRI 27-APR-2025
DEFINITION  transmembrane protein 196 isoform 4 [Homo sapiens].
ACCESSION   NP_001353555 XP_011513552
VERSION     NP_001353555.1
DBSOURCE    REFSEQ: accession NM_001366626.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Chen,J., Wang,D., Chen,H., Gu,J., Jiang,X., Han,F., Cao,J., Liu,W.
            and Liu,J.
  TITLE     TMEM196 inhibits lung cancer metastasis by regulating the
            Wnt/beta-catenin signaling pathway
  JOURNAL   J Cancer Res Clin Oncol 149 (2), 653-667 (2023)
   PUBMED   36355209
  REMARK    GeneRIF: TMEM196 inhibits lung cancer metastasis by regulating the
            Wnt/beta-catenin signaling pathway.
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Lee,J.U., Chang,H.S., Baek,D.G., Shin,H.D., Park,C.S. and Park,J.S.
  TITLE     Associations between TMEM196 polymorphisms and NSAID-exacerbated
            respiratory disease in asthma
  JOURNAL   Pharmacogenet Genomics 29 (4), 69-75 (2019)
   PUBMED   30694883
  REMARK    GeneRIF: The minor alleles of the four SNPs in TMEM196 may exert a
            protective effect against the development of NSAID-exacerbated
            respiratory disease(NERD) and may be useful genetic markers to
            predict the risk of NERD.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Liu,W.B., Han,F., Huang,Y.S., Chen,H.Q., Chen,J.P., Wang,D.D.,
            Jiang,X., Yin,L., Cao,J. and Liu,J.Y.
  TITLE     TMEM196 hypermethylation as a novel diagnostic and prognostic
            biomarker for lung cancer
  JOURNAL   Mol Carcinog 58 (4), 474-487 (2019)
   PUBMED   30536447
  REMARK    GeneRIF: Low TMEM196 expression is associated with lung cancer.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Liu,W.B., Han,F., Jiang,X., Chen,H.Q., Zhao,H., Liu,Y., Li,Y.H.,
            Huang,C., Cao,J. and Liu,J.Y.
  TITLE     TMEM196 acts as a novel functional tumour suppressor inactivated by
            DNA methylation and is a potential prognostic biomarker in lung
            cancer
  JOURNAL   Oncotarget 6 (25), 21225-21239 (2015)
   PUBMED   26056045
  REMARK    GeneRIF: TMEM196 acts as a novel functional tumour suppressor
            inactivated by DNA methylation and is an independent prognostic
            factor of lung cancer
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Foroud,T., Lai,D., Koller,D., Van't Hof,F., Kurki,M.I.,
            Anderson,C.S., Brown,R.D. Jr., Connolly,E.S., Eriksson,J.G.,
            Flaherty,M., Fornage,M., von Und Zu Fraunberg,M., Gaal,E.I.,
            Laakso,A., Hernesniemi,J., Huston,J., Jaaskelainen,J.E.,
            Kiemeney,L.A., Kivisaari,R., Kleindorfer,D., Ko,N., Lehto,H.,
            Mackey,J., Meissner,I., Moomaw,C.J., Mosley,T.H., Moskala,M.,
            Niemela,M., Palotie,A., Pera,J., Rinkel,G., Ripke,S., Rouleau,G.,
            Ruigrok,Y., Sauerbeck,L., Slowik,A., Vermeulen,S.H., Woo,D.,
            Worrall,B.B. and Broderick,J.
  CONSRTM   Familial Intracranial Aneurysm Study Investigators
  TITLE     Genome-wide association study of intracranial aneurysm identifies a
            new association on chromosome 7
  JOURNAL   Stroke 45 (11), 3194-3199 (2014)
   PUBMED   25256182
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Hwang,S.J., Yang,Q., Meigs,J.B., Pearce,E.N. and Fox,C.S.
  TITLE     A genome-wide association for kidney function and endocrine-related
            traits in the NHLBI's Framingham Heart Study
  JOURNAL   BMC Med Genet 8 Suppl 1 (Suppl 1), S10 (2007)
   PUBMED   17903292
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004543.2 and CK823401.1.
            
            On Oct 13, 2018 this sequence version replaced XP_011513552.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.187064.1,
                                           SRR1660805.187599.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.1"
     Protein         1..178
                     /product="transmembrane protein 196 isoform 4"
                     /calculated_mol_wt=18894
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYL7.2)"
     Site            47..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYL7.2)"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYL7.2)"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYL7.2)"
     CDS             1..178
                     /gene="TMEM196"
                     /coded_by="NM_001366626.1:922..1458"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:256130"
                     /db_xref="HGNC:HGNC:22431"
ORIGIN      
        1 mctsgqiigs llvlsvleig lgvssvavga vsfslalreh kpqlgdsspv wsgvcfllcg
       61 icgilcakkk sglvmilfsa ccicgliggi lnfqflravt kktsslyplh lasmslacig
      121 iggctlsswl tcrlasyeqr rmfserehsl hhshemaeke itdnmsnggp qlifngrv
//
LOCUS       NP_001357346             650 aa            linear   PRI 27-APR-2025
DEFINITION  actin-binding LIM protein 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001357346 XP_024301771
VERSION     NP_001357346.1
DBSOURCE    REFSEQ: accession NM_001370417.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 650)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   4  (residues 1 to 650)
  AUTHORS   Cao,J., Shen,Y., Zhu,L., Xu,Y., Zhou,Y., Wu,Z., Li,Y., Yan,X. and
            Zhu,X.
  TITLE     miR-129-3p controls cilia assembly by regulating CP110 and actin
            dynamics
  JOURNAL   Nat Cell Biol 14 (7), 697-706 (2012)
   PUBMED   22684256
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 650)
  AUTHORS   Ruau,D., Dudley,J.T., Chen,R., Phillips,N.G., Swan,G.E.,
            Lazzeroni,L.C., Clark,J.D., Butte,A.J. and Angst,M.S.
  TITLE     Integrative approach to pain genetics identifies pain sensitivity
            loci across diseases
  JOURNAL   PLoS Comput Biol 8 (6), e1002538 (2012)
   PUBMED   22685391
REFERENCE   6  (residues 1 to 650)
  AUTHORS   Matsuda,M., Yamashita,J.K., Tsukita,S. and Furuse,M.
  TITLE     abLIM3 is a novel component of adherens junctions with
            actin-binding activity
  JOURNAL   Eur J Cell Biol 89 (11), 807-816 (2010)
   PUBMED   20709423
REFERENCE   7  (residues 1 to 650)
  AUTHORS   Barrientos,T., Frank,D., Kuwahara,K., Bezprozvannaya,S.,
            Pipes,G.C., Bassel-Duby,R., Richardson,J.A., Katus,H.A., Olson,E.N.
            and Frey,N.
  TITLE     Two novel members of the ABLIM protein family, ABLIM-2 and -3,
            associate with STARS and directly bind F-actin
  JOURNAL   J Biol Chem 282 (11), 8393-8403 (2007)
   PUBMED   17194709
REFERENCE   8  (residues 1 to 650)
  AUTHORS   Krupp,M., Weinmann,A., Galle,P.R. and Teufel,A.
  TITLE     Actin binding LIM protein 3 (abLIM3)
  JOURNAL   Int J Mol Med 17 (1), 129-133 (2006)
   PUBMED   16328021
  REMARK    GeneRIF: Results characterize a third member of the actin binding
            LIM protein subgroup, actin binding LIM protein 3.
REFERENCE   9  (residues 1 to 650)
  AUTHORS   Zheng,B., Wen,J.K., Han,M. and Zhou,A.R.
  TITLE     hhLIM protein is involved in cardiac hypertrophy
  JOURNAL   Biochim Biophys Acta 1690 (1), 1-10 (2004)
   PUBMED   15337165
REFERENCE   10 (residues 1 to 650)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091940.3 and AC012613.7.
            
            On May 7, 2019 this sequence version replaced XP_024301771.1.
            
            Summary: This gene encodes a member of the actin-binding LIM
            (abLIM) family of proteins. These proteins are characterized by an
            N-terminal LIM domain and a C-terminal dematin-like domain. The
            encoded protein interacts with actin filaments and may be a
            component of adherens junctions in several cell types. A variant of
            this gene may be associated with pain sensitivity in male human
            patients. [provided by RefSeq, Sep 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.231578.1,
                                           SRR1803612.55183.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..650
                     /product="actin-binding LIM protein 3 isoform 2"
                     /note="abLIM-3"
                     /calculated_mol_wt=74037
     Region          23..74
                     /region_name="LIM1_abLIM"
                     /note="The first LIM domain of actin binding LIM (abLIM)
                     proteins; cd09327"
                     /db_xref="CDD:188713"
     Site            order(23,26,43,46,49,52,70,73)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188713"
     Region          79..134
                     /region_name="LIM2_abLIM"
                     /note="The second LIM domain on actin binding LIM (abLIM)
                     proteins; cd09328"
                     /db_xref="CDD:188714"
     Site            order(82,85,102,105,108,111,130,133)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188714"
     Region          151..202
                     /region_name="LIM3_abLIM"
                     /note="The third LIM domain of actin binding LIM (abLIM)
                     proteins; cd09329"
                     /db_xref="CDD:188715"
     Site            order(151,154,172,175,178,181,198,201)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188715"
     Region          210..265
                     /region_name="LIM4_abLIM"
                     /note="The fourth LIM domain of actin binding LIM (abLIM)
                     proteins; cd09330"
                     /db_xref="CDD:188716"
     Site            order(210,213,230,233,236,239,258,261)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188716"
     Region          273..600
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          615..650
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..650
                     /gene="ABLIM3"
                     /gene_synonym="HMFN1661"
                     /coded_by="NM_001370417.1:366..2318"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS78069.1"
                     /db_xref="GeneID:22885"
                     /db_xref="HGNC:HGNC:29132"
                     /db_xref="MIM:611305"
ORIGIN      
        1 mntsipyqqn pynprgssnv iqcyrcgdtc kgevvrvhnn hfhircftcq vcgcglaqsg
       61 fffknqeyic tqdyqqlygt rcdscrdfit gevisalgrt yhpkcfvcsl crkpfpigdk
      121 vtfsgkecvc qtcsqsmass kpikirgpsh cagckeeikh gqsllaldkq whvscfkcqt
      181 csviltgeyi skdgvpyces dyhaqfgikc etcdryisgr vleaggkhyh ptcarcvrch
      241 qmftegeemy ltgsevwhpi ckqaaraekk lkhrrtsets isppgssigs pnrvicakvd
      301 neilnykdla alpkvksiye vqrpdlisye phsrymsdem lercgygesl gtlspysqdi
      361 yenldlrqrr asspgyidsp tysrqgmspt fsrsphhyyr sagdsniyrk ppiykrhgdl
      421 statksktse disqtskysp iyspdpyyas eseywtyhgs pkvprarrfs sggeeddfdr
      481 smhklqsgig rlilkeemka rsssyadpwt pprsstssre alhtagyems lngsprshyl
      541 adsdplisks aslpayrrng lhrtpsadlf hydsmnavnw gmreykiypy elllvttrgr
      601 nrlpkdvdrt rlerhlsqee fyqvfgmtis efdrlalwkr nelkkqarlf
//
LOCUS       NP_001357003             479 aa            linear   PRI 27-APR-2025
DEFINITION  RAC-gamma serine/threonine-protein kinase isoform 1 [Homo sapiens].
ACCESSION   NP_001357003
VERSION     NP_001357003.1
DBSOURCE    REFSEQ: accession NM_001370074.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Xu,Y., Lu,R., Li,H., Feng,W. and Zhao,R.
  TITLE     A spectrum of AKT3 activating mutations cause focal malformations
            of cortical development (FMCDs) in cortical organoids
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (6), 167232 (2024)
   PUBMED   38759814
  REMARK    GeneRIF: A spectrum of AKT3 activating mutations cause focal
            malformations of cortical development (FMCDs) in cortical
            organoids.
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Corre,E., Soum,C., Pfeifer,R., Bessiere,C., Dailhau,S.,
            Marboeuf,C., Meggetto,F., Touriol,C., Recher,C., Bousquet,M. and
            Pyronnet,S.
  TITLE     Differential prognostic values of the three AKT isoforms in acute
            myeloid leukemia
  JOURNAL   Sci Rep 14 (1), 7070 (2024)
   PUBMED   38528080
  REMARK    GeneRIF: Differential prognostic values of the three AKT isoforms
            in acute myeloid leukemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Jougasaki,M., Takenoshita,Y., Umebashi,K., Yamamoto,M., Sudou,K.,
            Nakashima,H., Sonoda,M. and Kinjo,T.
  TITLE     Autocrine Regulation of Interleukin-6 via the Activation of STAT3
            and Akt in Cardiac Myxoma Cells
  JOURNAL   Int J Mol Sci 25 (4), 2232 (2024)
   PUBMED   38396907
  REMARK    GeneRIF: Autocrine Regulation of Interleukin-6 via the Activation
            of STAT3 and Akt in Cardiac Myxoma Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Murthy,S.S., Tosolini,A., Taguchi,T. and Testa,J.R.
  TITLE     Mapping of AKT3, encoding a member of the Akt/protein kinase B
            family, to human and rodent chromosomes by fluorescence in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 88 (1-2), 38-40 (2000)
   PUBMED   10773662
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Masure,S., Haefner,B., Wesselink,J.J., Hoefnagel,E., Mortier,E.,
            Verhasselt,P., Tuytelaars,A., Gordon,R. and Richardson,A.
  TITLE     Molecular cloning, expression and characterization of the human
            serine/threonine kinase Akt-3
  JOURNAL   Eur J Biochem 265 (1), 353-360 (1999)
   PUBMED   10491192
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Nakatani,K., Sakaue,H., Thompson,D.A., Weigel,R.J. and Roth,R.A.
  TITLE     Identification of a human Akt3 (protein kinase B gamma) which
            contains the regulatory serine phosphorylation site
  JOURNAL   Biochem Biophys Res Commun 257 (3), 906-910 (1999)
   PUBMED   10208883
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Brodbeck,D., Cron,P. and Hemmings,B.A.
  TITLE     A human protein kinase Bgamma with regulatory phosphorylation sites
            in the activation loop and in the C-terminal hydrophobic domain
  JOURNAL   J Biol Chem 274 (14), 9133-9136 (1999)
   PUBMED   10092583
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Walker,K.S., Deak,M., Paterson,A., Hudson,K., Cohen,P. and
            Alessi,D.R.
  TITLE     Activation of protein kinase B beta and gamma isoforms by insulin
            in vivo and by 3-phosphoinositide-dependent protein kinase-1 in
            vitro: comparison with protein kinase B alpha
  JOURNAL   Biochem J 331 (Pt 1) (Pt 1), 299-308 (1998)
   PUBMED   9512493
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Borgatti,P., Zauli,G., Colamussi,M.L., Gibellini,D., Previati,M.,
            Cantley,L.L. and Capitani,S.
  TITLE     Extracellular HIV-1 Tat protein activates phosphatidylinositol 3-
            and Akt/PKB kinases in CD4+ T lymphoblastoid Jurkat cells
  JOURNAL   Eur J Immunol 27 (11), 2805-2811 (1997)
   PUBMED   9394803
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Mirzaa,G.
  TITLE     MPPH Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27854409
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL592151.13, AL662889.5,
            AL591721.7 and AC096539.2.
            
            Summary: The protein encoded by this gene is a member of the AKT,
            also called PKB,  serine/threonine protein kinase family. AKT
            kinases are known to be regulators of cell signaling in response to
            insulin and growth factors. They are involved in a wide variety of
            biological processes including cell proliferation, differentiation,
            apoptosis, tumorigenesis, as well as glycogen synthesis and glucose
            uptake. This kinase has been shown to be stimulated by
            platelet-derived growth factor (PDGF), insulin, and insulin-like
            growth factor 1 (IGF1). Alternatively splice transcript variants
            encoding distinct isoforms have been described. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.130086.1,
                                           SRR14038196.2724549.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q43-q44"
     Protein         1..479
                     /product="RAC-gamma serine/threonine-protein kinase
                     isoform 1"
                     /EC_number="2.7.11.1"
                     /note="RAC-gamma serine/threonine protein kinase; PKB
                     gamma; v-akt murine thymoma viral oncogene homolog 3
                     (protein kinase B, gamma)"
                     /calculated_mol_wt=55644
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9Y243.1)"
     Region          4..110
                     /region_name="PH_PKB"
                     /note="Protein Kinase B-like pleckstrin homology (PH)
                     domain; cd01241"
                     /db_xref="CDD:269947"
     Site            order(14,16..19,23,25,51..52,54,85)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269947"
     Region          132..479
                     /region_name="STKc_PKB_gamma"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Protein Kinase B gamma (also called Akt3); cd05593"
                     /db_xref="CDD:270745"
     Site            order(154..155,157..158,162,175,177,189,192,209,225..228,
                     232,234,238,271,273,275..276,278,288..289,292,306..313,
                     338,344,347,435,439)
                     /site_type="active"
                     /db_xref="CDD:270745"
     Site            order(154..155,157,162,175,177,209,225..228,232,271,273,
                     275..276,278,288..289,435)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270745"
     Site            order(158,189,192,232,234,238,271,273,275,292,306..313,
                     338,344,347,439)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270745"
     Site            288..311
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270745"
     Site            302
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (Q9Y243.1)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PDPK1.
                     /evidence=ECO:0000269|PubMed:9512493; propagated from
                     UniProtKB/Swiss-Prot (Q9Y243.1)"
     Site            309
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (Q9Y243.1)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y243.1)"
     Site            447
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270745"
     Region          458..479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y243.1)"
     Site            468..473
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270745"
     Site            472
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P31750; propagated from
                     UniProtKB/Swiss-Prot (Q9Y243.1)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCZ.
                     /evidence=ECO:0000269|PubMed:12162751; propagated from
                     UniProtKB/Swiss-Prot (Q9Y243.1)"
     CDS             1..479
                     /gene="AKT3"
                     /gene_synonym="MPPH; MPPH2; PKB-GAMMA; PKBG; PRKBG;
                     RAC-gamma; RAC-PK-gamma; STK-2"
                     /coded_by="NM_001370074.1:144..1583"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS31077.1"
                     /db_xref="GeneID:10000"
                     /db_xref="HGNC:HGNC:393"
                     /db_xref="MIM:611223"
ORIGIN      
        1 msdvtivkeg wvqkrgeyik nwrpryfllk tdgsfigyke kpqdvdlpyp lnnfsvakcq
       61 lmkterpkpn tfiirclqwt tviertfhvd tpeereewte aiqavadrlq rqeeermncs
      121 ptsqidnige eemdastthh krktmndfdy lkllgkgtfg kvilvrekas gkyyamkilk
      181 keviiakdev ahtltesrvl kntrhpflts lkysfqtkdr lcfvmeyvng gelffhlsre
      241 rvfsedrtrf ygaeivsald ylhsgkivyr dlklenlmld kdghikitdf glckegitda
      301 atmktfcgtp eylapevled ndygravdww glgvvmyemm cgrlpfynqd heklfelilm
      361 edikfprtls sdaksllsgl likdpnkrlg ggpddakeim rhsffsgvnw qdvydkklvp
      421 pfkpqvtset dtryfdeeft aqtititppe kydedgmdcm dnerrphfpq fsysasgre
//
LOCUS       NP_663696                615 aa            linear   PRI 27-APR-2025
DEFINITION  protein DBF4 homolog B isoform 1 [Homo sapiens].
ACCESSION   NP_663696
VERSION     NP_663696.1
DBSOURCE    REFSEQ: accession NM_145663.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Goder,A., Maric,C.A., Rainey,M.D., O'Connor,A., Cazzaniga,C.,
            Shamavu,D., Cadoret,J.C. and Santocanale,C.
  TITLE     DBF4, not DRF1, is the crucial regulator of CDC7 kinase at
            replication forks
  JOURNAL   J Cell Biol 223 (8) (2024)
   PUBMED   38865090
  REMARK    GeneRIF: DBF4, not DRF1, is the crucial regulator of CDC7 kinase at
            replication forks.
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Chen,L., Luo,C., Shen,L., Liu,Y., Wang,Q., Zhang,C., Guo,R.,
            Zhang,Y., Xie,Z., Wei,N., Wu,W., Han,J. and Feng,Y.
  TITLE     SRSF1 Prevents DNA Damage and Promotes Tumorigenesis through
            Regulation of DBF4B Pre-mRNA Splicing
  JOURNAL   Cell Rep 21 (12), 3406-3413 (2017)
   PUBMED   29262322
  REMARK    GeneRIF: Knockdown of the exon6-containing isoform (DBF4B-FL)
            significantly inhibits the tumorigenic potential of colon cancer.
            Overexpression of DBF4B-FL protects against DNA damage induced by
            SRSF1 knockdown.
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Tsuji,T., Lau,E., Chiang,G.G. and Jiang,W.
  TITLE     The role of Dbf4/Drf1-dependent kinase Cdc7 in DNA-damage
            checkpoint control
  JOURNAL   Mol Cell 32 (6), 862-869 (2008)
   PUBMED   19111665
  REMARK    GeneRIF: These results indicate that Ddk functions as an upstream
            regulator to monitor S-phase checkpoint signaling.
REFERENCE   6  (residues 1 to 615)
  AUTHORS   Yoshizawa-Sugata,N., Ishii,A., Taniyama,C., Matsui,E., Arai,K. and
            Masai,H.
  TITLE     A second human Dbf4/ASK-related protein, Drf1/ASKL1, is required
            for efficient progression of S and M phases
  JOURNAL   J Biol Chem 280 (13), 13062-13070 (2005)
   PUBMED   15668232
  REMARK    GeneRIF: ASKL1 in a complex with Cdc7 may play a role in normal
            progression of both S and M phases
REFERENCE   7  (residues 1 to 615)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 615)
  AUTHORS   Montagnoli,A., Bosotti,R., Villa,F., Rialland,M., Brotherton,D.,
            Mercurio,C., Berthelsen,J. and Santocanale,C.
  TITLE     Drf1, a novel regulatory subunit for human Cdc7 kinase
  JOURNAL   EMBO J 21 (12), 3171-3181 (2002)
   PUBMED   12065429
  REMARK    GeneRIF: Results describe a novel human protein, Drf1, related to
            both human and yeast Dbf4. Drf1 is a nuclear cell cycle-regulated
            protein which binds to Cdc7 and activates the kinase.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC016158.1, AF448801.1 and
            AW290902.1.
            
            Summary: This gene encodes a regulator of the cell division cycle 7
            homolog (S. cerevisiae) protein, a serine-threonine kinase which
            links cell cycle regulation to genome duplication. This protein
            localizes to the nucleus and, in complex with the cell division
            cycle 7 homolog (S. cerevisiae) protein, may facilitate M phase
            progression. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Sep 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF448801.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315005.8/ ENSP00000323663.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..615
                     /product="protein DBF4 homolog B isoform 1"
                     /note="Dbf4-related factor 1; activator of S-phase
                     kinase-like protein 1; chiffon homolog B; zinc finger,
                     DBF-type containing 1B; ASK-like protein 1; DBF4 homolog
                     B; DBF4 zinc finger B"
                     /calculated_mol_wt=67112
     Region          18..340
                     /region_name="DBF4"
                     /note="Protein kinase essential for the initiation of DNA
                     replication [DNA replication, recombination, and repair /
                     Cell division and chromosome partitioning]; COG5067"
                     /db_xref="CDD:227399"
     Region          93..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFT6.1)"
     Region          264..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFT6.1)"
     Region          299..340
                     /region_name="zf-DBF"
                     /note="DBF zinc finger; pfam07535"
                     /db_xref="CDD:462197"
     Region          371..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFT6.1)"
     CDS             1..615
                     /gene="DBF4B"
                     /gene_synonym="ASKL1; CHIFB; DRF1; ZDBF1B"
                     /coded_by="NM_145663.3:157..2004"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11485.1"
                     /db_xref="GeneID:80174"
                     /db_xref="HGNC:HGNC:17883"
                     /db_xref="MIM:611661"
ORIGIN      
        1 msepgkgddc lelessmaes rlrapdlgvs rclgkcqkns pgarkhpfsg ksfyldlpag
       61 knlqfltgai qqlggviegf lskevsyivs srrevkaess gkshrgcpsp spsevrvets
      121 amvdpkgshp rpsrkpvdsv plsrgkellq kairnqgsis gggsggsssl ltnarswgvr
      181 ilhvdemmmh vqqlslaslc vkkqqpkkpe gtcpaaesrt rkvarlkapf lkiedesrkf
      241 rpfhhqfksf peisflgpkd aspfeapttl gsmhhtresk dgepsprsaa htmprrkkgy
      301 ceccqeafee lhvhlqsaqh rsfaleahly aevdriiaql shsfadipfq aglprwsgsp
      361 asdcdplcpe tlhphqpshp raasprirke dscqasvtqg raagqqrwte sldgvmgppa
      421 shtcvsattl lpalpkgsre qgclcpcpas ftqshlvtsl allpgewspa edmplhpsqe
      481 nsfapadipv kgpllfpear pwlmsarcwv rpfpfvtwgc liphdttplh eevspcpclr
      541 lgylyllltq slwcrvrvps lstagpiprt shpctlafps ylndhdlghl cqakpqgwnt
      601 pqpflhcgfl avdsg
//
LOCUS       NP_110395                392 aa            linear   PRI 27-APR-2025
DEFINITION  integrin-linked kinase-associated serine/threonine phosphatase 2C
            [Homo sapiens].
ACCESSION   NP_110395
VERSION     NP_110395.1
DBSOURCE    REFSEQ: accession NM_030768.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Zhang,R., Yuan,J., Liu,S., Torraca,V., Liao,Z., Wu,Y., Tan,H.,
            Yao,X., Hou,X., Lyu,H., Xiao,S., Guo,D., Ali,D.W., Michalak,M.,
            Chen,X.Z., Zhou,C. and Tang,J.
  TITLE     ILKAP Promotes the Metastasis of Hepatocellular Carcinoma Cells by
            Inhibiting beta-Catenin Degradation and Enhancing the WNT Signaling
            Pathway
  JOURNAL   Adv Biol (Weinh) 8 (5), e2300117 (2024)
   PUBMED   38379270
  REMARK    GeneRIF: ILKAP Promotes the Metastasis of Hepatocellular Carcinoma
            Cells by Inhibiting beta-Catenin Degradation and Enhancing the WNT
            Signaling Pathway.
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Liu,T., Liu,Y., Cao,J., Gao,X., Wang,J., Chen,G., Wang,Y., Liu,G.,
            Bai,G., Hu,Y., Yang,J., Dong,L., Quan,X. and Zou,W.
  TITLE     ILKAP Binding to and Dephosphorylating HIF-1alpha is Essential for
            Apoptosis Induced by Severe Hypoxia
  JOURNAL   Cell Physiol Biochem 46 (6), 2500-2507 (2018)
   PUBMED   29742494
  REMARK    GeneRIF: ILKAP physically interacted with HIF-1A and induced its
            dephosphorylation. Both the HIF-1A-p53 interaction and apoptosis
            relied on ILKAP.
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Hausmann,C., Temme,A., Cordes,N. and Eke,I.
  TITLE     ILKAP, ILK and PINCH1 control cell survival of p53-wildtype
            glioblastoma cells after irradiation
  JOURNAL   Oncotarget 6 (33), 34592-34605 (2015)
   PUBMED   26460618
  REMARK    GeneRIF: our data suggest an essential role of PINCH1, ILK and
            ILKAP for the radioresistance of p53-wildtype glioblastoma
            multiforme cells
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Shao,G., Zheng,Q., Xu,X., Zhao,J. and Liu,P.
  TITLE     Endometrial ILKAP expression among patients with endometriosis and
            its association with clinical characteristics
  JOURNAL   Int J Gynaecol Obstet 130 (1), 23-26 (2015)
   PUBMED   25872452
  REMARK    GeneRIF: The expression of ILKAP was considerably lower in eutopic
            and ectopic endometrial samples from women with endometriosis than
            in control endometrium. Expression varied depending on the phase of
            the menstrual cycle.
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Zhou,W., Cui,S., Han,S., Cheng,B., Zheng,Y. and Zhang,Y.
  TITLE     Palladin is a novel binding partner of ILKAP in eukaryotic cells
  JOURNAL   Biochem Biophys Res Commun 411 (4), 768-773 (2011)
   PUBMED   21782789
  REMARK    GeneRIF: these results suggested that palladin played a specific
            role in modulating the subcellular localization of the cytoplasmic
            ILKAP and promoting the ILKAP-induced apoptosis.
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Nakrieko,K.A., Vespa,A., Mason,D., Irvine,T.S., D'Souza,S.J. and
            Dagnino,L.
  TITLE     Modulation of integrin-linked kinase nucleo-cytoplasmic shuttling
            by ILKAP and CRM1
  JOURNAL   Cell Cycle 7 (14), 2157-2166 (2008)
   PUBMED   18635968
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Kumar,A.S., Naruszewicz,I., Wang,P., Leung-Hagesteijn,C. and
            Hannigan,G.E.
  TITLE     ILKAP regulates ILK signaling and inhibits anchorage-independent
            growth
  JOURNAL   Oncogene 23 (19), 3454-3461 (2004)
   PUBMED   14990992
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Leung-Hagesteijn,C., Mahendra,A., Naruszewicz,I. and Hannigan,G.E.
  TITLE     Modulation of integrin signal transduction by ILKAP, a protein
            phosphatase 2C associating with the integrin-linked kinase, ILK1
  JOURNAL   EMBO J 20 (9), 2160-2170 (2001)
   PUBMED   11331582
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Tong,Y., Quirion,R. and Shen,S.H.
  TITLE     Cloning and characterization of a novel mammalian PP2C isozyme
  JOURNAL   J Biol Chem 273 (52), 35282-35290 (1998)
   PUBMED   9857069
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016757.10.
            
            Summary: The protein encoded by this gene is a protein
            serine/threonine phosphatase of the PP2C family. This protein can
            interact with integrin-linked kinase (ILK/ILK1), a regulator of
            integrin mediated signaling, and regulate the kinase activity of
            ILK. Through the interaction with ILK, this protein may selectively
            affect the signaling process of ILK-mediated glycogen synthase
            kinase 3 beta (GSK3beta), and thus participate in Wnt signaling
            pathway. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001043.1, BC006576.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254654.8/ ENSP00000254654.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..392
                     /product="integrin-linked kinase-associated
                     serine/threonine phosphatase 2C"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2c, delta isozyme;
                     integrin-linked kinase associated phosphatase; protein
                     phosphatase, Mg2+/Mn2+ dependent 1O"
                     /calculated_mol_wt=42776
     Region          1..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0C8.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H0C8.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H0C8.1)"
     Region          108..390
                     /region_name="PP2Cc"
                     /note="Serine/threonine phosphatases, family 2C, catalytic
                     domain; The protein architecture and deduced catalytic
                     mechanism of PP2C phosphatases are similar to the PP1,
                     PP2A, PP2B family of protein Ser/Thr phosphatases, with
                     which PP2C shares no sequence...; cd00143"
                     /db_xref="CDD:238083"
     Site            order(118,122..123,152..154,326,381)
                     /site_type="active"
                     /db_xref="CDD:238083"
     Site            210
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H0C8.1)"
     CDS             1..392
                     /gene="ILKAP"
                     /gene_synonym="ILKAP2; ILKAP3; PP2C-DELTA; PP2CD; PPM1O"
                     /coded_by="NM_030768.3:143..1321"
                     /db_xref="CCDS:CCDS2526.1"
                     /db_xref="GeneID:80895"
                     /db_xref="HGNC:HGNC:15566"
                     /db_xref="MIM:618909"
ORIGIN      
        1 mdlfgdlpep ersprpaagk eaqkgpllfd dlppasstds gsggpllfdd lppassgdsg
       61 slatsisqmv ktegkgakrk tseeekngse elvekkvcka ssvifglkgy vaerkgeree
      121 mqdahvilnd iteecrppss litrvsyfav fdghggiras kfaaqnlhqn lirkfpkgdv
      181 isvektvkrc lldtfkhtde eflkqassqk pawkdgstat cvlavdnily ianlgdsrai
      241 lcryneesqk haalslskeh nptqyeermr iqkaggnvrd grvlgvlevs rsigdgqykr
      301 cgvtsvpdir rcqltpndrf illacdglfk vftpeeavnf ilscledeki qtregksaad
      361 aryeaacnrl ankavqrgsa dnvtvmvvri gh
//
LOCUS       NP_002200               1170 aa            linear   PRI 27-APR-2025
DEFINITION  integrin alpha-L isoform a precursor [Homo sapiens].
ACCESSION   NP_002200
VERSION     NP_002200.2
DBSOURCE    REFSEQ: accession NM_002209.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1170)
  AUTHORS   Zhang,R., Zhu,G., Li,Z., Meng,Z., Huang,H., Ding,C., Wang,Y.,
            Chen,C., Li,Y., Liu,H. and Chen,J.
  TITLE     ITGAL expression in non-small-cell lung cancer tissue and its
            association with immune infiltrates
  JOURNAL   Front Immunol 15, 1382231 (2024)
   PUBMED   38646528
  REMARK    GeneRIF: ITGAL expression in non-small-cell lung cancer tissue and
            its association with immune infiltrates.
            Erratum:[Front Immunol. 2024 Apr 26;15:1415814. doi:
            10.3389/fimmu.2024.1415814. PMID: 38736883]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1170)
  AUTHORS   Lacouture,C., Chaves,B., Guipouy,D., Houmadi,R., Duplan-Eche,V.,
            Allart,S., Destainville,N. and Dupre,L.
  TITLE     LFA-1 nanoclusters integrate TCR stimulation strength to tune
            T-cell cytotoxic activity
  JOURNAL   Nat Commun 15 (1), 407 (2024)
   PUBMED   38195629
  REMARK    GeneRIF: LFA-1 nanoclusters integrate TCR stimulation strength to
            tune T-cell cytotoxic activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1170)
  AUTHORS   Wang,Q., Xiao,G., Li,N., Jiang,X. and Li,C.
  TITLE     lncRNA PCBP1-AS1 mediated downregulation of ITGAL as a prognostic
            biomarker in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 15 (10), 4510-4523 (2023)
   PUBMED   37256932
  REMARK    GeneRIF: lncRNA PCBP1-AS1 mediated downregulation of ITGAL as a
            prognostic biomarker in lung adenocarcinoma.
REFERENCE   4  (residues 1 to 1170)
  AUTHORS   Hickman,A., Koetsier,J., Kurtanich,T., Nielsen,M.C., Winn,G.,
            Wang,Y., Bentebibel,S.E., Shi,L., Punt,S., Williams,L.,
            Haymaker,C., Chesson,C.B., Fa'ak,F., Dominguez,A.L., Jones,R.,
            Kuiatse,I., Caivano,A.R., Khounlo,S., Warier,N.D., Marathi,U.,
            Market,R.V., Biediger,R.J., Craft,J.W. Jr., Hwu,P., Davies,M.A.,
            Woodside,D.G., Vanderslice,P., Diab,A., Overwijk,W.W. and
            Hailemichael,Y.
  TITLE     LFA-1 activation enriches tumor-specific T cells in a cold tumor
            model and synergizes with CTLA-4 blockade
  JOURNAL   J Clin Invest 132 (13) (2022)
   PUBMED   35552271
  REMARK    GeneRIF: LFA-1 activation enriches tumor-specific T cells in a cold
            tumor model and synergizes with CTLA-4 blockade.
REFERENCE   5  (residues 1 to 1170)
  AUTHORS   Garcia-Salido,A., Cuenca-Carcelen,S. and Castillo-Robleda,A.
  TITLE     CD64, CD11a and CD18 leukocytes expression in children with
            SARS-CoV-2 multisystem inflammatory syndrome versus children with
            Kawasaki disease: Similar but not the same
  JOURNAL   Med Clin (Barc) 156 (2), 89-91 (2021)
   PUBMED   33160625
  REMARK    GeneRIF: CD64, CD11a and CD18 leukocytes expression in children
            with SARS-CoV-2 multisystem inflammatory syndrome versus children
            with Kawasaki disease: Similar but not the same.
REFERENCE   6  (residues 1 to 1170)
  AUTHORS   Fawcett,J., Holness,C.L., Needham,L.A., Turley,H., Gatter,K.C.,
            Mason,D.Y. and Simmons,D.L.
  TITLE     Molecular cloning of ICAM-3, a third ligand for LFA-1,
            constitutively expressed on resting leukocytes
  JOURNAL   Nature 360 (6403), 481-484 (1992)
   PUBMED   1448173
REFERENCE   7  (residues 1 to 1170)
  AUTHORS   Alvarez,V., Pulido,R., Campanero,M.R., Paraiso,V., de
            Landazuri,M.O. and Sanchez-Madrid,F.
  TITLE     Differentially regulated cell surface expression of leukocyte
            adhesion receptors on neutrophils
  JOURNAL   Kidney Int 40 (5), 899-905 (1991)
   PUBMED   1762294
REFERENCE   8  (residues 1 to 1170)
  AUTHORS   Maurer,D., Holter,W., Majdic,O., Fischer,G.F. and Knapp,W.
  TITLE     CD27 expression by a distinct subpopulation of human B lymphocytes
  JOURNAL   Eur J Immunol 20 (12), 2679-2684 (1990)
   PUBMED   1702722
REFERENCE   9  (residues 1 to 1170)
  AUTHORS   Dustin,M.L. and Springer,T.A.
  TITLE     T-cell receptor cross-linking transiently stimulates adhesiveness
            through LFA-1
  JOURNAL   Nature 341 (6243), 619-624 (1989)
   PUBMED   2477710
REFERENCE   10 (residues 1 to 1170)
  AUTHORS   Larson,R.S., Corbi,A.L., Berman,L. and Springer,T.
  TITLE     Primary structure of the leukocyte function-associated molecule-1
            alpha subunit: an integrin with an embedded domain defining a
            protein superfamily
  JOURNAL   J Cell Biol 108 (2), 703-712 (1989)
   PUBMED   2537322
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314246.1, BC008777.2 and
            CA430398.1.
            
            On Feb 8, 2008 this sequence version replaced NP_002200.1.
            
            Summary: ITGAL encodes the integrin alpha L chain. Integrins are
            heterodimeric integral membrane proteins composed of an alpha chain
            and a beta chain. This I-domain containing alpha integrin combines
            with the beta 2 chain (ITGB2) to form the integrin lymphocyte
            function-associated antigen-1 (LFA-1), which is expressed on all
            leukocytes. LFA-1 plays a central role in leukocyte intercellular
            adhesion through interactions with its ligands, ICAMs 1-3
            (intercellular adhesion molecules 1 through 3), and also functions
            in lymphocyte costimulatory signaling. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y00796.1, AK314246.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356798.11/ ENSP00000349252.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..1170
                     /product="integrin alpha-L isoform a precursor"
                     /note="antigen CD11A (p180), lymphocyte
                     function-associated antigen 1, alpha polypeptide; integrin
                     alpha-L; LFA-1 alpha; integrin gene promoter; LFA-1A; CD11
                     antigen-like family member A; leukocyte adhesion
                     glycoprotein LFA-1 alpha chain; leukocyte
                     function-associated molecule 1 alpha chain; integrin,
                     alpha L (antigen CD11A (p180), lymphocyte
                     function-associated antigen 1; alpha polypeptide)"
                     /calculated_mol_wt=126115
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2673
     mat_peptide     26..1170
                     /product="integrin alpha-L isoform a"
                     /calculated_mol_wt=126115
     Region          31..82
                     /region_name="FG-GAP 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P20701.3)"
     Site            65
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Region          83..141
                     /region_name="FG-GAP 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P20701.3)"
     Site            89
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Region          155..323
                     /region_name="vWA_integrins_alpha_subunit"
                     /note="Integrins are a class of adhesion receptors that
                     link the extracellular matrix to the cytoskeleton and
                     cooperate with growth factor receptors to promote celll
                     survival, cell cycle progression and cell migration.
                     Integrins consist of an alpha and a beta...; cd01469"
                     /db_xref="CDD:238746"
     Site            order(155,157,178,258,260,282,312)
                     /site_type="active"
                     /note="integrin inhibitor binding pocket [active]"
                     /db_xref="CDD:238746"
     Site            order(162,164,166,231,264)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238746"
     Site            order(164..166,168,231)
                     /site_type="active"
                     /note="integrin-collagen binding site [active]"
                     /db_xref="CDD:238746"
     Region          170..349
                     /region_name="I-domain (insertion domain)"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Region          390..445
                     /region_name="FG-GAP 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P20701.3)"
     Region          446..506
                     /region_name="FG-GAP 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P20701.3)"
     Region          456..503
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          507..563
                     /region_name="FG-GAP 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P20701.3)"
     Region          517..569
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          567..627
                     /region_name="FG-GAP 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P20701.3)"
     Region          579..>603
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          613..999
                     /region_name="Integrin_alpha2"
                     /note="Integrin alpha; pfam08441"
                     /db_xref="CDD:462478"
     Site            649
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Site            670
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Site            726
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Site            730
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Site            862
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Site            885
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Site            897
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Site            1060
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Site            1071
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     Site            1089..1112
                     /site_type="transmembrane region"
     Region          1113..1127
                     /region_name="Integrin_alpha"
                     /note="Integrin alpha cytoplasmic region; pfam00357"
                     /db_xref="CDD:459778"
     Region          1115..1119
                     /region_name="GFFKR motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P20701.3)"
     Region          1128..1170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20701.3)"
     Site            1165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16301335; propagated from
                     UniProtKB/Swiss-Prot (P20701.3)"
     CDS             1..1170
                     /gene="ITGAL"
                     /gene_synonym="CD11A; LFA-1; LFA1A"
                     /coded_by="NM_002209.3:97..3609"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS32433.1"
                     /db_xref="GeneID:3683"
                     /db_xref="HGNC:HGNC:6148"
                     /db_xref="MIM:153370"
ORIGIN      
        1 mkdscitvma mallsgffff apassynldv rgarsfsppr agrhfgyrvl qvgngvivga
       61 pgegnstgsl yqcqsgtghc lpvtlrgsny tskylgmtla tdptdgsila cdpglsrtcd
      121 qntylsglcy lfrqnlqgpm lqgrpgfqec ikgnvdlvfl fdgsmslqpd efqkildfmk
      181 dvmkklsnts yqfaavqfst syktefdfsd yvkrkdpdal lkhvkhmlll tntfgainyv
      241 atevfreelg arpdatkvli iitdgeatds gnidaakdii ryiigigkhf qtkesqetlh
      301 kfaskpasef vkildtfekl kdlftelqkk iyviegtskq dltsfnmels ssgisadlsr
      361 ghavvgavga kdwaggfldl kadlqddtfi gnepltpevr agylgytvtw lpsrqktsll
      421 asgapryqhm grvllfqepq ggghwsqvqt ihgtqigsyf ggelcgvdvd qdgetellli
      481 gaplfygeqr ggrvfiyqrr qlgfeevsel qgdpgyplgr fgeaitaltd ingdglvdva
      541 vgapleeqga vyifngrhgg lspqpsqrie gtqvlsgiqw fgrsihgvkd legdgladva
      601 vgaesqmivl ssrpvvdmvt lmsfspaeip vhevecsyst snkmkegvni ticfqiksli
      661 pqfqgrlvan ltytlqldgh rtrrrglfpg grhelrrnia vttsmsctdf sfhfpvcvqd
      721 lispinvsln fslweeegtp rdqraqgkdi ppilrpslhs etweipfekn cgedkkcean
      781 lrvsfspars ralrltafas lsvelslsnl eedaywvqld lhfppglsfr kvemlkphsq
      841 ipvsceelpe esrllsrals cnvsspifka ghsvalqmmf ntlvnsswgd svelhanvtc
      901 nnedsdlled nsattiipil ypiniliqdq edstlyvsft pkgpkihqvk hmyqvriqps
      961 ihdhniptle avvgvpqpps egpithqwsv qmeppvpchy edlerlpdaa epclpgalfr
     1021 cpvvfrqeil vqvigtlelv geieassmfs lcsslsisfn sskhfhlygs naslaqvvmk
     1081 vdvvyekqml ylyvlsgigg llllllifiv lykvgffkrn lkekmeagrg vpngipaeds
     1141 eqlasgqeag dpgclkplhe kdsesgggkd
//
LOCUS       NP_060417                888 aa            linear   PRI 27-APR-2025
DEFINITION  molybdenum cofactor sulfurase [Homo sapiens].
ACCESSION   NP_060417
VERSION     NP_060417.4
DBSOURCE    REFSEQ: accession NM_017947.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Rontani,P., Perche,O., Greetham,L., Jullien,N., Gepner,B.,
            Feron,F., Nivet,E. and Erard-Garcia,M.
  TITLE     Impaired expression of the COSMOC/MOCOS gene unit in ASD patient
            stem cells
  JOURNAL   Mol Psychiatry 26 (5), 1606-1618 (2021)
   PUBMED   32327736
  REMARK    GeneRIF: Impaired expression of the COSMOC/MOCOS gene unit in ASD
            patient stem cells.
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Taheri,M., Noroozi,R., Aghaei,K., Omrani,M.D. and Ghafouri-Fard,S.
  TITLE     The rs594445 in MOCOS gene is associated with risk of autism
            spectrum disorder
  JOURNAL   Metab Brain Dis 35 (3), 497-501 (2020)
   PUBMED   31900757
  REMARK    GeneRIF: The rs594445 in MOCOS gene is associated with risk of
            autism spectrum disorder.
REFERENCE   5  (residues 1 to 888)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 888)
  AUTHORS   Peretz,H., Naamati,M.S., Levartovsky,D., Lagziel,A., Shani,E.,
            Horn,I., Shalev,H. and Landau,D.
  TITLE     Identification and characterization of the first mutation
            (Arg776Cys) in the C-terminal domain of the Human Molybdenum
            Cofactor Sulfurase (HMCS) associated with type II classical
            xanthinuria
  JOURNAL   Mol Genet Metab 91 (1), 23-29 (2007)
   PUBMED   17368066
  REMARK    GeneRIF: Two mutations, both in the N-terminal domain of the Human
            Molybdenum Cofactor Sulfurase (HMCS), were reported in patients
            with type II xanthinuria.
REFERENCE   7  (residues 1 to 888)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 888)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 888)
  AUTHORS   Yamamoto,T., Moriwaki,Y., Takahashi,S., Tsutsumi,Z., Tuneyoshi,K.,
            Matsui,K., Cheng,J. and Hada,T.
  TITLE     Identification of a new point mutation in the human molybdenum
            cofactor sulferase gene that is responsible for xanthinuria type II
  JOURNAL   Metabolism 52 (11), 1501-1504 (2003)
   PUBMED   14624414
REFERENCE   10 (residues 1 to 888)
  AUTHORS   Ichida,K., Matsumura,T., Sakuma,R., Hosoya,T. and Nishino,T.
  TITLE     Mutation of human molybdenum cofactor sulfurase gene is responsible
            for classical xanthinuria type II
  JOURNAL   Biochem Biophys Res Commun 282 (5), 1194-1200 (2001)
   PUBMED   11302742
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC023043.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_060417.3.
            
            Summary: This gene encodes an enzyme that sulfurates the molybdenum
            cofactor which is required for activation of the xanthine
            dehydrogenase (XDH) and aldehyde oxidase (AO) enzymes. XDH
            catalyzes the conversion of hypoxanthine to uric acid via xanthine,
            as well as the conversion of allopurinol to oxypurinol, and
            pyrazinamide to 5-hydroxy pyrazinamide. Mutations in this gene
            cause the metabolic disorder classical xanthinuria type II which is
            characterized by the loss of XDH/XO and AO enzyme activity,
            decreased levels of uric acid in the urine, increased levels of
            xanthine and hypoxanthine in the serum and urine, formation of
            xanthine stones in the urinary tract, and myositis due to tissue
            deposition of xanthine. [provided by RefSeq, Apr 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000740.1, AK222886.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261326.6/ ENSP00000261326.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..888
                     /product="molybdenum cofactor sulfurase"
                     /EC_number="2.8.1.9"
                     /note="human molybdenum cofactor sulfurase"
                     /calculated_mol_wt=97989
     Region          28..866
                     /region_name="PLN02724"
                     /note="Molybdenum cofactor sulfurase"
                     /db_xref="CDD:215384"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96EN8.2)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96EN8.2)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96EN8.2)"
     CDS             1..888
                     /gene="MOCOS"
                     /gene_synonym="HMCS; MCS; MOS"
                     /coded_by="NM_017947.4:44..2710"
                     /db_xref="CCDS:CCDS11919.1"
                     /db_xref="GeneID:55034"
                     /db_xref="HGNC:HGNC:18234"
                     /db_xref="MIM:613274"
ORIGIN      
        1 magaaaesgr elwtfagsrd psaprlaygy gpgslrelra refsrlagtv yldhagatlf
       61 sqsqlesfts dlmentygnp hsqnissklt hdtveqvryr ilahfhttae dytviftags
      121 taalklvaea fpwvsqgpes sgsrfcyltd shtsvvgmrn vtmainvist pvrpedlwsa
      181 eersasasnp dcqlphlfcy paqsnfsgvr yplswieevk sgrlhpvstp gkwfvlldaa
      241 syvstspldl sahqadfvpi sfykifgfpt glgallvhnr aapllrktyf gggtasayla
      301 gedfyiprqs vaqrfedgti sfldvialkh gfdtlerltg gmenikqhtf tlaqytyval
      361 sslqypngap vvriysdsef sspevqgpii nfnvlddkgn iigysqvdkm aslynihlrt
      421 gcfcntgacq rhlgisnemv rkhfqaghvc gdnmdlidgq ptgsvrisfg ymstlddvqa
      481 flrfiidtrl hssgdwpvpq ahadtgetga psadsqadvi pavmgrrsls pqedaltgsr
      541 vwnnsstvna vpvappvcdv artqptpsek aagvlegalg phvvtnlyly pikscaafev
      601 trwpvgnqgl lydrswmvvn hngvclsqkq eprlcliqpf idlrqrimvi kakgmepiev
      661 pleensertq irqsrvcadr vstydcgeki sswlstffgr pchlikqssn sqrnakkkhg
      721 kdqlpgtmat lslvneaqyl lintssilel hrqlntsden gkeelfslkd lslrfranii
      781 ingkrafeee kwdeisigsl rfqvlgpchr cqmicidqqt gqrnqhvfqk lsesretkvn
      841 fgmylmhasl dlsspcflsv gsqvlpvlke nveghdlpas ekhqdvts
//
LOCUS       NP_001020017             907 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 62 isoform 2 [Mus musculus].
ACCESSION   NP_001020017
VERSION     NP_001020017.1
DBSOURCE    REFSEQ: accession NM_001024846.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Choi,M.Y., Romer,A.I., Hu,M., Lepourcelet,M., Mechoor,A.,
            Yesilaltay,A., Krieger,M., Gray,P.A. and Shivdasani,R.A.
  TITLE     A dynamic expression survey identifies transcription factors
            relevant in mouse digestive tract development
  JOURNAL   Development 133 (20), 4119-4129 (2006)
   PUBMED   16971476
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Hunt,C.R., Parsian,A.J. and Kozak,C.A.
  TITLE     Genetic mapping of mouse heat shock protein genes Hsc4a to
            chromosome 11 and Hsc74 to chromosome 18 and two Hsc74 pseudogenes
            to chromosomes X and 8
  JOURNAL   Genomics 56 (3), 358-360 (1999)
   PUBMED   10087208
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Agata,Y., Matsuda,E. and Shimizu,A.
  TITLE     Rapid and efficient cloning of cDNAs encoding Kruppel-like zinc
            finger proteins by degenerate PCR
  JOURNAL   Gene 213 (1-2), 55-64 (1998)
   PUBMED   9630514
REFERENCE   5  (residues 1 to 907)
  AUTHORS   Polimeni,M., Giorgi,S., De Gregorio,L., Dragani,T.A., Molinaro,M.,
            Cossu,G. and Bouche,M.
  TITLE     Differentiation dependent expression in muscle cells of ZT3, a
            novel zinc finger factor differentially expressed in embryonic and
            adult tissues
  JOURNAL   Mech Dev 54 (1), 107-117 (1996)
   PUBMED   8808410
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Danciger,M., Brady,J., Adamson,M.C., Farber,D.B., Piatigorsky,J.
            and Kozak,C.A.
  TITLE     Chromosomal localization of the genes for five zinc finger proteins
            expressed in mouse lens
  JOURNAL   Genomics 28 (1), 39-43 (1995)
   PUBMED   7590745
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606829.13, AK048619.1, AK028351.1, BC065692.1 and BE635021.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK028351.1, SRR9219380.68379.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849390, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 29.23 cM"
     Protein         1..907
                     /product="zinc finger protein 62 isoform 2"
                     /note="ZT3"
                     /calculated_mol_wt=103856
     Region          120..535
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          126..146
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          154..174
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          182..202
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          210..230
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(215,217,219,221..222,225..226,229,243,245,249..250,
                     253..254,257,271,273,275,277..278,281..282,285)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          238..258
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          266..286
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          294..314
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          322..342
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(327,329,331,333..334,337..338,341,355,357,361..362,
                     365..366,369,383,385,387,389..390,393..394,397)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          350..370
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <372..451
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          378..398
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          406..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          430..843
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          434..454
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(439,441,443,445..446,449..450,453,467,469,473..474,
                     477..478,481,495,497,499,501..502,505..506,509)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          462..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          490..510
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          602..622
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(607,609,611,613..614,617..618,621,635,637,641..642,
                     645..646,649,663,665,667,669..670,673..674,677)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          630..650
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          658..678
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          686..706
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(691,693,695,697..698,701..702,705,719,721,725..726,
                     729..730,733,747,749,751,753..754,757..758,761)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          714..734
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          742..762
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          770..790
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          798..817
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          825..845
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..907
                     /gene="Zfp62"
                     /coded_by="NM_001024846.2:503..3226"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS24601.1"
                     /db_xref="GeneID:22720"
                     /db_xref="MGI:MGI:99662"
ORIGIN      
        1 medeesskkn endsnadsqc psvgffhkdh mqksktgdtc dlfpkwkilk egkssiremi
       61 dthtnaanik leqddetsek sfypstntmh qtiptepnct kqgehtenin gnvhpahiad
      121 kklhkcdecg ksfkynsrlv qhkimhtgek ryecddcrgt frsssslrvh krihtgekpy
      181 kcdecgkaym sysslinhks thsgeknckc decgksfnys svldqhkrih tgekpyecge
      241 cgkafrnssg lrvhkrihtg ekpyecdtcg ktfsnssglr vhkrihtgek pyecdecgka
      301 fitcrtllnh ksihfgdkpy kcdeceksfn ysslliqhkv ihtgekpyec decgkafrns
      361 sglivhkrih tgekpykcdi cgkafsyssg lavhksihpg kkaheckdcg ksfsynslll
      421 qhktihtger pyvcdvcgkt frnnsglkvh rrlhtgekpy kcdvcgkayi srsslknhkg
      481 ihmgekpykc syceksfnys saleqhkrih trekpfgcde cgkafrnnsg lkvhkrihtg
      541 erpykceecg kayislssli nhksvhpgek pfkcdeceka fityrtllnh kkihlgekpy
      601 kcdvceksfn ytsllsqhkr vhtrekpfec drcekvfrnn sslkvhkrih tgekpyecdi
      661 cgkayishss linhksthpg ktsytcdecg kaffssrtli shkrvhlgek pfkcvecgks
      721 fsyssllsqh krihtgekpy vcdwcgkafr nssgltvhkr ihtgekpygc decekayish
      781 sslinhksvh rgkqpyncec gksfnyrsvl dqhkrihtgk kpyrcndcgk afnirsnltk
      841 hkrihtgees lnmanmeshs gtfqkmiyye ggnsldgtrm qmpvweaeha ksqrnqieek
      901 lyeynnf
//
LOCUS       NP_055210                280 aa            linear   PRI 27-APR-2025
DEFINITION  dual adapter for phosphotyrosine and 3-phosphotyrosine and
            3-phosphoinositide isoform 1 [Homo sapiens].
ACCESSION   NP_055210
VERSION     NP_055210.2
DBSOURCE    REFSEQ: accession NM_014395.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Ortner,D., Grabher,D., Hermann,M., Kremmer,E., Hofer,S. and
            Heufler,C.
  TITLE     The adaptor protein Bam32 in human dendritic cells participates in
            the regulation of MHC class I-induced CD8+ T cell activation
  JOURNAL   J Immunol 187 (8), 3972-3978 (2011)
   PUBMED   21930970
  REMARK    GeneRIF: we propose a role for Bam32 in the signaling of MHC class
            I molecules in professional Ag-presenting DC for the regulation of
            CD8(+) T cell activation.
            Erratum:[J Immunol. 2011 Dec 15;187(12):6584]
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Manna,D., Albanese,A., Park,W.S. and Cho,W.
  TITLE     Mechanistic basis of differential cellular responses of
            phosphatidylinositol 3,4-bisphosphate- and phosphatidylinositol
            3,4,5-trisphosphate-binding pleckstrin homology domains
  JOURNAL   J Biol Chem 282 (44), 32093-32105 (2007)
   PUBMED   17823121
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Dowler,S., Currie,R.A., Campbell,D.G., Deak,M., Kular,G.,
            Downes,C.P. and Alessi,D.R.
  TITLE     Identification of pleckstrin-homology-domain-containing proteins
            with novel phosphoinositide-binding specificities
  JOURNAL   Biochem J 351 (Pt 1), 19-31 (2000)
   PUBMED   11001876
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Ferguson,K.M., Kavran,J.M., Sankaran,V.G., Fournier,E.,
            Isakoff,S.J., Skolnik,E.Y. and Lemmon,M.A.
  TITLE     Structural basis for discrimination of 3-phosphoinositides by
            pleckstrin homology domains
  JOURNAL   Mol Cell 6 (2), 373-384 (2000)
   PUBMED   10983984
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Dowler,S., Montalvo,L., Cantrell,D., Morrice,N. and Alessi,D.R.
  TITLE     Phosphoinositide 3-kinase-dependent phosphorylation of the dual
            adaptor for phosphotyrosine and 3-phosphoinositides by the Src
            family of tyrosine kinase
  JOURNAL   Biochem J 349 (Pt 2), 605-610 (2000)
   PUBMED   10880360
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Marshall,A.J., Niiro,H., Lerner,C.G., Yun,T.J., Thomas,S.,
            Disteche,C.M. and Clark,E.A.
  TITLE     A novel B lymphocyte-associated adaptor protein, Bam32, regulates
            antigen receptor signaling downstream of phosphatidylinositol
            3-kinase
  JOURNAL   J Exp Med 191 (8), 1319-1332 (2000)
   PUBMED   10770799
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Dowler,S., Currie,R.A., Downes,C.P. and Alessi,D.R.
  TITLE     DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides
  JOURNAL   Biochem J 342 (Pt 1) (Pt 1), 7-12 (1999)
   PUBMED   10432293
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN995752.1, AF163254.1, BC012924.1, BM968883.1 and CA428013.1.
            
            On Oct 24, 2007 this sequence version replaced NP_055210.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.261143.1,
                                           SRR1660803.51428.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000512369.2/ ENSP00000423602.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..280
                     /product="dual adapter for phosphotyrosine and
                     3-phosphotyrosine and 3-phosphoinositide isoform 1"
                     /note="dual adapter for phosphotyrosine and
                     3-phosphotyrosine and 3-phosphoinositide; hDAPP1; B-cell
                     adapter molecule of 32 kDa; b lymphocyte adapter protein
                     Bam32"
                     /calculated_mol_wt=32063
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UN19.1)"
     Region          28..119
                     /region_name="SH2_DAPP1_BAM32_like"
                     /note="Src homology 2 domain found in dual adaptor for
                     phosphotyrosine and 3-phosphoinositides (DAPP1)/B
                     lymphocyte adaptor molecule of 32 kDa (Bam32)-like
                     proteins; cd10355"
                     /db_xref="CDD:198218"
     Site            order(42,61,82,84)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198218"
     Site            order(83,109)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198218"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXT1; propagated from
                     UniProtKB/Swiss-Prot (Q9UN19.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXT1; propagated from
                     UniProtKB/Swiss-Prot (Q9UN19.1)"
     Region          163..258
                     /region_name="PH_DAPP1"
                     /note="Dual Adaptor for Phosphotyrosine and
                     3-Phosphoinositides Pleckstrin homology (PH) domain;
                     cd10573"
                     /db_xref="CDD:269977"
     Site            order(173,180,182,184,195,197,235)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269977"
     CDS             1..280
                     /gene="DAPP1"
                     /gene_synonym="BAM32"
                     /coded_by="NM_014395.3:88..930"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47112.1"
                     /db_xref="GeneID:27071"
                     /db_xref="HGNC:HGNC:16500"
                     /db_xref="MIM:605768"
ORIGIN      
        1 mgraellegk mstqdpsdlw srsdgeaell qdlgwyhgnl trhaaealll sngcdgsyll
       61 rdsnettgly slsvrakdsv khfhveytgy sfkfgfnefs slkdfvkhfa nqpligsetg
      121 tlmvlkhpyp rkveepsiye svrvhtamqt grteddlvpt apslgtkegy ltkqgglvkt
      181 wktrwftlhr nelkyfkdqm spepirildl tecsavqfdy sqervncfcl vfpfrtfylc
      241 aktgveadew ikilrwklsq irkqlnqgeg tirsrsfifk
//
LOCUS       NP_001054                698 aa            linear   PRI 27-APR-2025
DEFINITION  serotransferrin isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001054 NP_054830
VERSION     NP_001054.2
DBSOURCE    REFSEQ: accession NM_001063.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Wang,M., Zhang,D., Jiang,L., Ye,M., Nie,J. and Yin,J.
  TITLE     Association between serum transferrin saturation levels and heart
            failure in adults aged >/=40 years: a cross-sectional study based
            on NHANES (2017-2020.03)
  JOURNAL   Front Endocrinol (Lausanne) 15, 1419064 (2024)
   PUBMED   39280001
  REMARK    GeneRIF: Association between serum transferrin saturation levels
            and heart failure in adults aged >/=40 years: a cross-sectional
            study based on NHANES (2017-2020.03).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Floegel,A., Intemann,T., Siani,A., Moreno,L.A., Molnar,D.,
            Veidebaum,T., Hadjigeorgiou,C., De Henauw,S., Hunsberger,M.,
            Eiben,G., Ahrens,W. and Wolters,M.
  CONSRTM   IDEFICS/I.Family consortia
  TITLE     Cohort-Based Reference Values for Serum Ferritin and Transferrin
            and Longitudinal Determinants of Iron Status in European Children
            Aged 3-15 Years
  JOURNAL   J Nutr 154 (2), 658-669 (2024)
   PUBMED   38048991
  REMARK    GeneRIF: Cohort-Based Reference Values for Serum Ferritin and
            Transferrin and Longitudinal Determinants of Iron Status in
            European Children Aged 3-15 Years.
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Tavakoli,F., Ghavimi,M.A., Fakhrzadeh,V., Abdolzadeh,D., Afshari,A.
            and Eslami,H.
  TITLE     Evaluation of salivary transferrin in patients with oral squamous
            cell carcinoma
  JOURNAL   Clin Exp Dent Res 10 (1), e809 (2024)
   PUBMED   37964689
  REMARK    GeneRIF: Evaluation of salivary transferrin in patients with oral
            squamous cell carcinoma.
REFERENCE   4  (residues 1 to 698)
  AUTHORS   Barton,J.C., Barton,J.C. and Acton,R.T.
  TITLE     Height of non-Hispanic white adults with homeostatic iron regulator
            HFE genotypes p.C282Y/p.C282Y and wt/wt
  JOURNAL   Mol Genet Genomic Med 12 (1), e2321 (2024)
   PUBMED   37930135
  REMARK    GeneRIF: Height of non-Hispanic white adults with homeostatic iron
            regulator HFE genotypes p.C282Y/p.C282Y and wt/wt.
REFERENCE   5  (residues 1 to 698)
  AUTHORS   Skarzynska,E., Mularczyk,K., Issat,T., Jakimiuk,A. and
            Lisowska-Myjak,B.
  TITLE     Meconium Transferrin and Ferritin as Markers of Homeostasis in the
            Developing Fetus
  JOURNAL   Int J Mol Sci 24 (21), 15937 (2023)
   PUBMED   37958917
  REMARK    GeneRIF: Meconium Transferrin and Ferritin as Markers of
            Homeostasis in the Developing Fetus.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 698)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 698)
  AUTHORS   Hershberger,C.L., Larson,J.L., Arnold,B., Rosteck,P.R. Jr.,
            Williams,P., DeHoff,B., Dunn,P., O'Neal,K.L., Riemen,M.W.,
            Tice,P.A. et al.
  TITLE     A cloned gene for human transferrin
  JOURNAL   Ann N Y Acad Sci 646, 140-154 (1991)
   PUBMED   1809186
  REMARK    Review article
REFERENCE   8  (residues 1 to 698)
  AUTHORS   Woodworth,R.C., Mason,A.B., Funk,W.D. and MacGillivray,R.T.
  TITLE     Expression and initial characterization of five site-directed
            mutants of the N-terminal half-molecule of human transferrin
  JOURNAL   Biochemistry 30 (45), 10824-10829 (1991)
   PUBMED   1932003
REFERENCE   9  (residues 1 to 698)
  AUTHORS   Guillou,F., Zakin,M.M., Part,D., Boissier,F. and Schaeffer,E.
  TITLE     Sertoli cell-specific expression of the human transferrin gene.
            Comparison with the liver-specific expression
  JOURNAL   J Biol Chem 266 (15), 9876-9884 (1991)
   PUBMED   1851757
REFERENCE   10 (residues 1 to 698)
  AUTHORS   Dautry-Varsat,A.
  TITLE     Receptor-mediated endocytosis: the intracellular journey of
            transferrin and its receptor
  JOURNAL   Biochimie 68 (3), 375-381 (1986)
   PUBMED   2874839
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC083905.20 and AC080128.21.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_001054.1.
            
            Summary: This gene encodes a glycoprotein with an approximate
            molecular weight of 76.5 kDa. It is thought to have been created as
            a result of an ancient gene duplication event that led to
            generation of homologous C and N-terminal domains each of which
            binds one ion of ferric iron. The function of this protein is to
            transport iron from the intestine, reticuloendothelial system, and
            liver parenchymal cells to all proliferating cells in the body.
            This protein may also have a physiologic role as
            granulocyte/pollen-binding protein (GPBP) involved in the removal
            of certain organic matter and allergens from serum. [provided by
            RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.111522.1,
                                           SRR1660809.219437.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000402696.9/ ENSP00000385834.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.1"
     Protein         1..698
                     /product="serotransferrin isoform 1 precursor"
                     /note="serotransferrin; siderophilin; beta-1 metal-binding
                     globulin; epididymis secretory sperm binding protein Li
                     71p"
                     /calculated_mol_wt=75196
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1886
     mat_peptide     20..698
                     /product="serotransferrin isoform 1"
                     /calculated_mol_wt=75196
     Region          24..346
                     /region_name="PBP2_transferrin_N"
                     /note="The N-lobe of transferrin, a member of the type 2
                     periplasmic binding protein fold superfamily; cd13618"
                     /db_xref="CDD:270336"
     Site            42
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:P12346; propagated from
                     UniProtKB/Swiss-Prot (P02787.5)"
     Site            51
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /id=CAR_000073;
                     propagated from UniProtKB/Swiss-Prot (P02787.5)"
     Site            order(82,114,139,143..146,207,268)
                     /site_type="active"
                     /db_xref="CDD:270336"
     Region          358..682
                     /region_name="PBP2_transferrin_C"
                     /note="The C-lobe of transferrin, a member of the type 2
                     periplasmic binding protein fold superfamily; cd13617"
                     /db_xref="CDD:270335"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P02787.5)"
     Site            order(411,445,471,475..478,536,604)
                     /site_type="active"
                     /db_xref="CDD:270335"
     Site            432
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295,
                     ECO:0000269|PubMed:31636418, ECO:0007744|PDB:6SOY,
                     ECO:0007744|PDB:6SOZ. /id=CAR_000074; propagated from
                     UniProtKB/Swiss-Prot (P02787.5)"
     Site            491
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, atypical, partial.
                     /evidence=ECO:0000269|PubMed:15536627; propagated from
                     UniProtKB/Swiss-Prot (P02787.5)"
     Site            630
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15536627,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22327295.
                     /id=CAR_000075; propagated from UniProtKB/Swiss-Prot
                     (P02787.5)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P02787.5)"
     CDS             1..698
                     /gene="TF"
                     /gene_synonym="HEL-S-71p; PRO1557; PRO2086; TFQTL1"
                     /coded_by="NM_001063.4:49..2145"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3080.1"
                     /db_xref="GeneID:7018"
                     /db_xref="HGNC:HGNC:11740"
                     /db_xref="MIM:190000"
ORIGIN      
        1 mrlavgallv cavlglclav pdktvrwcav seheatkcqs frdhmksvip sdgpsvacvk
       61 kasyldcira iaaneadavt ldaglvyday lapnnlkpvv aefygskedp qtfyyavavv
      121 kkdsgfqmnq lrgkkschtg lgrsagwnip igllycdlpe prkplekava nffsgscapc
      181 adgtdfpqlc qlcpgcgcst lnqyfgysga fkclkdgagd vafvkhstif enlankadrd
      241 qyellcldnt rkpvdeykdc hlaqvpshtv varsmggked liwellnqaq ehfgkdkske
      301 fqlfssphgk dllfkdsahg flkvpprmda kmylgyeyvt airnlregtc peaptdeckp
      361 vkwcalshhe rlkcdewsvn svgkiecvsa ettedciaki mngeadamsl dggfvyiagk
      421 cglvpvlaen ynksdncedt peagyfaiav vkksasdltw dnlkgkksch tavgrtagwn
      481 ipmgllynki nhcrfdeffs egcapgskkd sslcklcmgs glnlcepnnk egyygytgaf
      541 rclvekgdva fvkhqtvpqn tggknpdpwa knlnekdyel lcldgtrkpv eeyanchlar
      601 apnhavvtrk dkeacvhkil rqqqhlfgsn vtdcsgnfcl frsetkdllf rddtvclakl
      661 hdrntyekyl geeyvkavgn lrkcstssll eactfrrp
//
LOCUS       NP_004369                137 aa            linear   PRI 27-APR-2025
DEFINITION  cellular retinoic acid-binding protein 1 [Homo sapiens].
ACCESSION   NP_004369
VERSION     NP_004369.1
DBSOURCE    REFSEQ: accession NM_004378.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Sakata,K., Kanda,M., Shimizu,D., Nakamura,S., Inokawa,Y.,
            Hattori,N., Hayashi,M., Tanaka,C., Nakayama,G. and Kodera,Y.
  TITLE     Expression of cellular retinoic acid binding protein 1 predicts
            peritoneal recurrence of gastric cancer
  JOURNAL   Int J Oncol 60 (6) (2022)
   PUBMED   35417033
  REMARK    GeneRIF: Expression of cellular retinoic acid binding protein 1
            predicts peritoneal recurrence of gastric cancer.
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Enikeev,A.D., Komelkov,A.V., Axelrod,M.E., Galetsky,S.A.,
            Kuzmichev,S.A. and Tchevkina,E.M.
  TITLE     CRABP1 and CRABP2 Protein Levels Correlate with Each Other but Do
            Not Correlate with Sensitivity of Breast Cancer Cells to Retinoic
            Acid
  JOURNAL   Biochemistry (Mosc) 86 (2), 217-229 (2021)
   PUBMED   33832420
  REMARK    GeneRIF: CRABP1 and CRABP2 Protein Levels Correlate with Each Other
            but Do Not Correlate with Sensitivity of Breast Cancer Cells to
            Retinoic Acid.
REFERENCE   5  (residues 1 to 137)
  AUTHORS   Lin,Y.L., Lin,Y.W., Nhieu,J., Zhang,X. and Wei,L.N.
  TITLE     Sonic Hedgehog-Gli1 Signaling and Cellular Retinoic Acid Binding
            Protein 1 Gene Regulation in Motor Neuron Differentiation and
            Diseases
  JOURNAL   Int J Mol Sci 21 (11), 4125 (2020)
   PUBMED   32527063
  REMARK    GeneRIF: Sonic Hedgehog-Gli1 Signaling and Cellular Retinoic Acid
            Binding Protein 1 Gene Regulation in Motor Neuron Differentiation
            and Diseases.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 137)
  AUTHORS   Flagiello,D., Apiou,F., Gibaud,A., Poupon,M.F., Dutrillaux,B. and
            Malfoy,B.
  TITLE     Assignment of the genes for cellular retinoic acid binding protein
            1 (CRABP1) and 2 (CRABP2) to human chromosome band 15q24 and
            1q21.3, respectively, by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 76 (1-2), 17-18 (1997)
   PUBMED   9154115
REFERENCE   7  (residues 1 to 137)
  AUTHORS   Liu,W., Hellman,P., Li,Q., Yu,W.R., Juhlin,C., Nordlinder,H.,
            Rollman,O., Akerstrom,G., Torma,H. and Melhus,H.
  TITLE     Biosynthesis and function of all-trans- and 9-cis-retinoic acid in
            parathyroid cells
  JOURNAL   Biochem Biophys Res Commun 229 (3), 922-929 (1996)
   PUBMED   9005841
REFERENCE   8  (residues 1 to 137)
  AUTHORS   Eller,M.S., Oleksiak,M.F., McQuaid,T.J., McAfee,S.G. and
            Gilchrest,B.A.
  TITLE     The molecular cloning and expression of two CRABP cDNAs from human
            skin
  JOURNAL   Exp Cell Res 198 (2), 328-336 (1992)
   PUBMED   1309505
REFERENCE   9  (residues 1 to 137)
  AUTHORS   Astrom,A., Tavakkol,A., Pettersson,U., Cromie,M., Elder,J.T. and
            Voorhees,J.J.
  TITLE     Molecular cloning of two human cellular retinoic acid-binding
            proteins (CRABP). Retinoic acid-induced expression of CRABP-II but
            not CRABP-I in adult human skin in vivo and in skin fibroblasts in
            vitro
  JOURNAL   J Biol Chem 266 (26), 17662-17666 (1991)
   PUBMED   1654334
REFERENCE   10 (residues 1 to 137)
  AUTHORS   Ong,D.E.
  TITLE     Cellular retinoid-binding proteins
  JOURNAL   Arch Dermatol 123 (12), 1693-1695a (1987)
   PUBMED   2825608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU132726.1, BC022069.1 and
            AI863257.1.
            
            Summary: This gene encodes a specific binding protein for a vitamin
            A family member and is thought to play an important role in
            retinoic acid-mediated differentiation and proliferation processes.
            It is structurally similar to the cellular retinol-binding
            proteins, but binds only retinoic acid at specific sites within the
            nucleus, which may contribute to vitamin A-directed differentiation
            in epithelial tissue. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.48515.1, BC022069.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299529.7/ ENSP00000299529.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..137
                     /product="cellular retinoic acid-binding protein 1"
                     /note="cellular retinoic acid-binding protein I"
                     /calculated_mol_wt=15434
     Region          2..137
                     /region_name="CRABP1"
                     /note="cellular retinoic acid-binding protein 1; cd19460"
                     /db_xref="CDD:381235"
     Site            order(4,16,19..20,23,25,29..30,32..33,40,42,44,51,53,55,
                     57,59..60,62,64,66,74,76..79,94,96,110,112,119,121,123,
                     132,134)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381235"
     Site            order(16,25,29,32,40,55,57,59..60,77..79,121,132,134)
                     /site_type="other"
                     /note="retinoid binding site [chemical binding]"
                     /db_xref="CDD:381235"
     Region          21..31
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P29762.2)"
     CDS             1..137
                     /gene="CRABP1"
                     /gene_synonym="CRABP; CRABP-I; CRABPI; RBP5"
                     /coded_by="NM_004378.3:77..490"
                     /db_xref="CCDS:CCDS10301.1"
                     /db_xref="GeneID:1381"
                     /db_xref="HGNC:HGNC:2338"
                     /db_xref="MIM:180230"
ORIGIN      
        1 mpnfagtwkm rssenfdell kalgvnamlr kvavaaaskp hveirqdgdq fyiktsttvr
       61 tteinfkvge gfeeetvdgr kcrslatwen enkihctqtl legdgpktyw trelandeli
      121 ltfgaddvvc triyvre
//
LOCUS       NP_001236                453 aa            linear   PRI 27-APR-2025
DEFINITION  sialic acid-binding Ig-like lectin 6 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001236
VERSION     NP_001236.4
DBSOURCE    REFSEQ: accession NM_001245.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Schmidt,E.N., Lamprinaki,D., McCord,K.A., Joe,M., Sojitra,M.,
            Waldow,A., Nguyen,J., Monyror,J., Kitova,E.N., Mozaneh,F.,
            Guo,X.Y., Jung,J., Enterina,J.R., Daskhan,G.C., Han,L.,
            Krysler,A.R., Cromwell,C.R., Hubbard,B.P., West,L.J., Kulka,M.,
            Sipione,S., Klassen,J.S., Derda,R., Lowary,T.L., Mahal,L.K.,
            Riddell,M.R. and Macauley,M.S.
  TITLE     Siglec-6 mediates the uptake of extracellular vesicles through a
            noncanonical glycolipid binding pocket
  JOURNAL   Nat Commun 14 (1), 2327 (2023)
   PUBMED   37087495
  REMARK    GeneRIF: Siglec-6 mediates the uptake of extracellular vesicles
            through a noncanonical glycolipid binding pocket.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Smiljkovic,D., Herrmann,H., Sadovnik,I., Gamperl,S., Berger,D.,
            Stefanzl,G., Eisenwort,G., Hoermann,G., Kopanja,S., Dorofeeva,Y.,
            Focke-Tejkl,M., Jaksch,P., Hoetzenecker,K., Szepfalusi,Z.,
            Valenta,R., Arock,M. and Valent,P.
  TITLE     Expression and regulation of Siglec-6 (CD327) on human mast cells
            and basophils
  JOURNAL   J Allergy Clin Immunol 151 (1), 202-211 (2023)
   PUBMED   35953001
  REMARK    GeneRIF: Expression and regulation of Siglec-6 (CD327) on human
            mast cells and basophils.
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Guan,X., Yu,M., Wu,L., Chen,J., Tong,J., Wu,X., Yin,A., Xiao,T.,
            Wang,B., Zhang,J.V. and Niu,J.
  TITLE     Elevated trophoblastic Siglec6 contributes to the impairment of
            vascular endothelial cell functions by downregulating
            Wnt6/beta-catenin signaling in preeclampsia
  JOURNAL   Arch Biochem Biophys 730, 109396 (2022)
   PUBMED   36113626
  REMARK    GeneRIF: Elevated trophoblastic Siglec6 contributes to the
            impairment of vascular endothelial cell functions by downregulating
            Wnt6/beta-catenin signaling in preeclampsia.
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Stefanski,A.L., Renecle,M.D., Kramer,A., Sehgal,S., Narasimhan,P.,
            Rumer,K.K. and Winn,V.D.
  TITLE     Siglec-6 Signaling Uses Src Kinase Tyrosine Phosphorylation and
            SHP-2 Recruitment
  JOURNAL   Cells 11 (21), 3427 (2022)
   PUBMED   36359823
  REMARK    GeneRIF: Siglec-6 Signaling Uses Src Kinase Tyrosine
            Phosphorylation and SHP-2 Recruitment.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Robida,P.A., Rische,C.H., Morgenstern,N.B., Janarthanam,R., Cao,Y.,
            Krier-Burris,R.A., Korver,W., Xu,A., Luu,T., Schanin,J., Leung,J.,
            Rothenberg,M.E., Wechsler,J.B., Youngblood,B.A., Bochner,B.S. and
            O'Sullivan,J.A.
  TITLE     Functional and Phenotypic Characterization of Siglec-6 on Human
            Mast Cells
  JOURNAL   Cells 11 (7), 1138 (2022)
   PUBMED   35406705
  REMARK    GeneRIF: Functional and Phenotypic Characterization of Siglec-6 on
            Human Mast Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 453)
  AUTHORS   Winn,V.D., Gormley,M., Paquet,A.C., Kjaer-Sorensen,K., Kramer,A.,
            Rumer,K.K., Haimov-Kochman,R., Yeh,R.F., Overgaard,M.T., Varki,A.,
            Oxvig,C. and Fisher,S.J.
  TITLE     Severe preeclampsia-related changes in gene expression at the
            maternal-fetal interface include sialic acid-binding
            immunoglobulin-like lectin-6 and pappalysin-2
  JOURNAL   Endocrinology 150 (1), 452-462 (2009)
   PUBMED   18818296
  REMARK    GeneRIF: Preeclampsia involves changes in the gene expression of
            SIGLEC6 in placental cytotrophoblasts.
            Review article
REFERENCE   8  (residues 1 to 453)
  AUTHORS   Brinkman-Van der Linden,E.C., Hurtado-Ziola,N., Hayakawa,T.,
            Wiggleton,L., Benirschke,K., Varki,A. and Varki,N.
  TITLE     Human-specific expression of Siglec-6 in the placenta
  JOURNAL   Glycobiology 17 (9), 922-931 (2007)
   PUBMED   17580316
  REMARK    GeneRIF: the negative signaling potential of Siglec-6 may have a
            role in human-specific placental expression, to slow the tempo of
            the human birth process
REFERENCE   9  (residues 1 to 453)
  AUTHORS   Patel,N., Brinkman-Van der Linden,E.C., Altmann,S.W., Gish,K.,
            Balasubramanian,S., Timans,J.C., Peterson,D., Bell,M.P.,
            Bazan,J.F., Varki,A. and Kastelein,R.A.
  TITLE     OB-BP1/Siglec-6. a leptin- and sialic acid-binding protein of the
            immunoglobulin superfamily
  JOURNAL   J Biol Chem 274 (32), 22729-22738 (1999)
   PUBMED   10428856
  REMARK    Erratum:[J Biol Chem 1999 Sep 24;274(39):28058]
REFERENCE   10 (residues 1 to 453)
  AUTHORS   Takei,Y., Sasaki,S., Fujiwara,T., Takahashi,E., Muto,T. and
            Nakamura,Y.
  TITLE     Molecular cloning of a novel gene similar to myeloid antigen CD33
            and its specific expression in placenta
  JOURNAL   Cytogenet Cell Genet 78 (3-4), 295-300 (1997)
   PUBMED   9465907
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020914.9 and BC035359.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 3, 2008 this sequence version replaced NP_001236.3.
            
            Summary: This gene encodes a member of the SIGLEC (sialic acid
            binding immunoglobulin-like lectin) family of proteins. The encoded
            transmembrane receptor binds sialyl-TN glycans and leptin.
            Placental expression of the encoded protein is upregulated in
            preeclampsia. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U71382.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000425629.8/ ENSP00000401502.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..453
                     /product="sialic acid-binding Ig-like lectin 6 isoform 1
                     precursor"
                     /note="CD33 antigen-like 1; obesity-binding protein 1"
                     /calculated_mol_wt=47249
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2682
     mat_peptide     27..453
                     /product="Sialic acid-binding Ig-like lectin 6.
                     /id=PRO_0000014946"
                     /note="propagated from UniProtKB/Swiss-Prot (O43699.2)"
                     /calculated_mol_wt=47249
     Region          31..141
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          47..51
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43699.2)"
     Region          104..108
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          118..123
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          131..137
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          148..233
                     /region_name="IgC2_CD33_d2_like"
                     /note="Second immunoglobulin domain of Cluster of
                     Differentiation (CD) 33 and related Siglecs; member of the
                     C2-set of IgSF domains; cd20987"
                     /db_xref="CDD:409579"
     Region          148..152
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409579"
     Site            149
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43699.2)"
     Region          161..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409579"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43699.2)"
     Region          179..184
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409579"
     Region          198..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409579"
     Region          211..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409579"
     Region          225..233
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409579"
     Site            233
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43699.2)"
     Region          259..336
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          270..274
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          283..287
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          305..309
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          316..321
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..334
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            348..368
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43699.2)"
     Region          424..429
                     /region_name="ITIM motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O43699.2)"
     Region          444..449
                     /region_name="SLAM-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O43699.2)"
     CDS             1..453
                     /gene="SIGLEC6"
                     /gene_synonym="CD327; CD33L; CD33L1; CD33L2; CDW327;
                     OBBP1"
                     /coded_by="NM_001245.7:23..1384"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12834.3"
                     /db_xref="GeneID:946"
                     /db_xref="HGNC:HGNC:10875"
                     /db_xref="MIM:604405"
ORIGIN      
        1 mqgaqeasas emlplllpll wagalaqerr fqlegpeslt vqeglcvlvp crlpttlpas
       61 yygygywfle gadvpvatnd pdeevqeetr grfhllwdpr rkncslsird arrrdnaayf
      121 frlkskwmky gytssklsvr vmalthrpni sipgtlesgh psnltcsvpw vceqgtppif
      181 swmsaaptsl gprttqssvl titprpqdhs tnltcqvtfp gagvtmerti qlnvsyapqk
      241 vaisifqgns aafkilqnts slpvlegqal rllcdadgnp pahlswfqgf palnatpisn
      301 tgvlelpqvg saeegdftcr aqhplgslqi slslfvhwkp egraggvlga vwgasittlv
      361 flcvcfifrv ktrrkkaaqp vqntddvnpv mvsgsrghqh qfqtgivsdh paeagpised
      421 eqelhyavlh fhkvqpqepk vtdteyseik ihk
//
LOCUS       NP_001346232             401 aa            linear   ROD 27-APR-2025
DEFINITION  2-hydroxyacyl-CoA lyase 2 isoform 3 [Mus musculus].
ACCESSION   NP_001346232 XP_011241703
VERSION     NP_001346232.1
DBSOURCE    REFSEQ: accession NM_001359303.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Rhein,S., Costalunga,R., Inderhees,J., Gurtzgen,T., Faupel,T.C.,
            Shaheryar,Z., Arrulo Pereira,A., Othman,A., Begemann,K., Binder,S.,
            Stolting,I., Dorta,V., Nawroth,P.P., Fleming,T., Oexle,K.,
            Prevot,V., Nogueiras,R., Meyhofer,S., Meyhofer,S.M. and
            Schwaninger,M.
  TITLE     The reactive pyruvate metabolite dimethylglyoxal mediates
            neurological consequences of diabetes
  JOURNAL   Nat Commun 15 (1), 5745 (2024)
   PUBMED   38987239
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Mori,K., Naganuma,T. and Kihara,A.
  TITLE     Role of 2-hydroxy acyl-CoA lyase HACL2 in odd-chain fatty acid
            production via alpha-oxidation in vivo
  JOURNAL   Mol Biol Cell 34 (9), ar85 (2023)
   PUBMED   37285239
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Liu,S., Lu,S., Xu,R., Atzberger,A., Gunther,S., Wettschureck,N. and
            Offermanns,S.
  TITLE     Members of Bitter Taste Receptor Cluster Tas2r143/Tas2r135/Tas2r126
            Are Expressed in the Epithelium of Murine Airways and Other
            Non-gustatory Tissues
  JOURNAL   Front Physiol 8, 849 (2017)
   PUBMED   29163195
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Wiltshire,T., Pletcher,M., Cole,S.E., Villanueva,M., Birren,B.,
            Lehoczky,J., Dewar,K. and Reeves,R.H.
  TITLE     Perfect conserved linkage across the entire mouse chromosome 10
            region homologous to human chromosome 21
  JOURNAL   Genome Res 9 (12), 1214-1222 (1999)
   PUBMED   10613844
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK133553.1 and AK143918.1.
            
            On Jan 3, 2018 this sequence version replaced XP_011241703.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK143918.1, SRR7345562.4528274.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 39.72 cM"
     Protein         1..401
                     /product="2-hydroxyacyl-CoA lyase 2 isoform 3"
                     /EC_number="2.2.1.-"
                     /note="acetolactate synthase-like protein; ilvB-like
                     protein; 2-hydroxyacyl-CoA lyase 2"
                     /calculated_mol_wt=42681
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BU33.1)"
     Region          53..>361
                     /region_name="PRK05858"
                     /note="acetolactate synthase"
                     /db_xref="CDD:235629"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BU33.1)"
     CDS             1..401
                     /gene="Ilvbl"
                     /gene_synonym="5830463I21"
                     /coded_by="NM_001359303.1:107..1312"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS88046.1"
                     /db_xref="GeneID:216136"
                     /db_xref="MGI:MGI:1351911"
ORIGIN      
        1 metsaaaasa ggffpsflll afgtlvaavl gvahrlglfy qlmhkvdkts irhggesvaa
       61 vlrahgvrfv ftlvgghisp llvaceklgi rvvdtrhevt avfaadavar ltgtvgvaav
      121 tagpgltntv tavknaqvaq spvlllggaa stllqkrgal qaidqmslfr plckfcasvr
      181 rvrdivptlr taiaaaqsgt pgpvfvelpl dvlypyfmve kemiptklpn slmgrvvvwy
      241 lqnclanlfv gaweprpegp lpldipqasp qqvqrcveil srakrpllvl gsqallpptp
      301 anklraavet lgvpcflggm srgllgrnhp lhirqnrsaa lkkadvvvla gavcdfrlsy
      361 grvlnrkssi iivnrnrddl llnsdifwkp qeavqagpas p
//
LOCUS       NP_001159441             314 aa            linear   PRI 27-APR-2025
DEFINITION  STE20-related kinase adapter protein alpha isoform 5 [Homo
            sapiens].
ACCESSION   NP_001159441
VERSION     NP_001159441.1
DBSOURCE    REFSEQ: accession NM_001165969.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Smith,R.H.B., Khan,Z.M., Ung,P.M., Scopton,A.P., Silber,L.,
            Mack,S.M., Real,A.M., Schlessinger,A. and Dar,A.C.
  TITLE     Type II Binders Targeting the 'GLR-Out' Conformation of the
            Pseudokinase STRADalpha
  JOURNAL   Biochemistry 60 (4), 289-302 (2021)
   PUBMED   33440120
  REMARK    GeneRIF: Type II Binders Targeting the ''GLR-Out'' Conformation of
            the Pseudokinase STRADalpha.
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Alsaif,H.S., Khashab,H.Y.E.L. and Alkuraya,F.S.
  TITLE     Two further cases of polyhydramnios, megalencephaly, and
            symptomatic epilepsy syndrome, caused by a truncating variant in
            STRADA
  JOURNAL   Am J Med Genet A 185 (2), 604-607 (2021)
   PUBMED   33247513
  REMARK    GeneRIF: Two further cases of polyhydramnios, megalencephaly, and
            symptomatic epilepsy syndrome, caused by a truncating variant in
            STRADA.
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Milburn,C.C., Boudeau,J., Deak,M., Alessi,D.R. and van Aalten,D.M.
  TITLE     Crystal structure of MO25 alpha in complex with the C terminus of
            the pseudo kinase STE20-related adaptor
  JOURNAL   Nat Struct Mol Biol 11 (2), 193-200 (2004)
   PUBMED   14730349
REFERENCE   8  (residues 1 to 314)
  AUTHORS   Boudeau,J., Baas,A.F., Deak,M., Morrice,N.A., Kieloch,A.,
            Schutkowski,M., Prescott,A.R., Clevers,H.C. and Alessi,D.R.
  TITLE     MO25alpha/beta interact with STRADalpha/beta enhancing their
            ability to bind, activate and localize LKB1 in the cytoplasm
  JOURNAL   EMBO J 22 (19), 5102-5114 (2003)
   PUBMED   14517248
REFERENCE   9  (residues 1 to 314)
  AUTHORS   Baas,A.F., Boudeau,J., Sapkota,G.P., Smit,L., Medema,R.,
            Morrice,N.A., Alessi,D.R. and Clevers,H.C.
  TITLE     Activation of the tumour suppressor kinase LKB1 by the STE20-like
            pseudokinase STRAD
  JOURNAL   EMBO J 22 (12), 3062-3072 (2003)
   PUBMED   12805220
  REMARK    GeneRIF: Identification and characterization of an LKB1-specific
            adaptor protein and substrate, STRAD. Results imply that STRAD
            plays a key role in regulating the tumor suppressor activities of
            LKB1.
REFERENCE   10 (residues 1 to 314)
  AUTHORS   Scanlan,M.J., Gout,I., Gordon,C.M., Williamson,B., Stockert,E.,
            Gure,A.O., Jager,D., Chen,Y.T., Mackay,A., O'Hare,M.J. and Old,L.J.
  TITLE     Humoral immunity to human breast cancer: antigen definition and
            quantitative analysis of mRNA expression
  JOURNAL   Cancer Immun 1, 4 (2001)
   PUBMED   12747765
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA049174.1, AY290821.2,
            AK301331.1, AL832407.1 and BQ682133.1.
            
            Summary: The protein encoded by this gene contains a STE20-like
            kinase domain, but lacks several residues that are critical for
            catalytic activity, so it is termed a 'pseudokinase'. The protein
            forms a heterotrimeric complex with serine/threonine kinase 11
            (STK11, also known as LKB1) and the scaffolding protein calcium
            binding protein 39 (CAB39, also known as MO25). The protein
            activates STK11 leading to the phosphorylation of both proteins and
            excluding STK11 from the nucleus. The protein is necessary for
            STK11-induced G1 cell cycle arrest. A mutation in this gene has
            been shown to result in polyhydramnios, megalencephaly, and
            symptomatic epilepsy (PMSE) syndrome. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            Additional transcript variants have been described but their
            full-length nature is not known. [provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.478748.1, AK301331.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..314
                     /product="STE20-related kinase adapter protein alpha
                     isoform 5"
                     /note="STE20-like pseudokinase; STE20-related kinase
                     adapter protein alpha; protein kinase LYK5; serologically
                     defined breast cancer antigen NY-BR-96; STE20-related
                     kinase adaptor alpha"
                     /calculated_mol_wt=34494
     Region          41..312
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(46..49,54,56,69,71,102,118..121,166,170..171,173,
                     183..184)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..314
                     /gene="STRADA"
                     /gene_synonym="LYK5; NY-BR-96; PMSE; Stlk; STRAD; STRAD
                     alpha"
                     /coded_by="NM_001165969.2:291..1235"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS58585.1"
                     /db_xref="GeneID:92335"
                     /db_xref="HGNC:HGNC:30172"
                     /db_xref="MIM:608626"
ORIGIN      
        1 msflvskper irtndasses iasfskqevm ssflpeggcy elltvigkgf edlmtvnlar
       61 ykptgeyvtv rrinleacsn emvtflqgel hvsklfnhpn ivpyratfia dnelwvvtsf
      121 maygsakdli cthfmdgmne laiayilqgv lkaldyihhm gyvhrsvkas hilisvdgkv
      181 ylsglrsnls mishgqrqrv vhdfpkysvk vlpwlspevl qqnlqgydak sdiysvgita
      241 celanghvpf kdmpatqmll eklngtvpcl ldtstipaee ltmspsrsva nsglsdsltt
      301 stprpsngpv paps
//
LOCUS       NP_002398                 95 aa            linear   PRI 27-APR-2025
DEFINITION  mammaglobin-B precursor [Homo sapiens].
ACCESSION   NP_002398
VERSION     NP_002398.1
DBSOURCE    REFSEQ: accession NM_002407.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Soleimani,S., Alizadeh Shargh,S., Keramatinia,A., Mehrvar,N.,
            Mansouri,N., Doosti,A., Mortazavi-Tabatabaei,S.A., Hashemi,M. and
            Movafagh,A.
  TITLE     Detection of gene expression in sentinel lymph node of primary
            breast cancer patients
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 64 (5), 118-121 (2018)
   PUBMED   29729704
  REMARK    GeneRIF: The expression of HOXB13, IL17BR, and mammaglobin 1 in
            sentinel lymph nodes predict the outcome of primary breast cancer
            patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Sangoi,A.R., Shrestha,B., Yang,G., Mego,O. and Beck,A.H.
  TITLE     The Novel Marker GATA3 is Significantly More Sensitive Than
            Traditional Markers Mammaglobin and GCDFP15 for Identifying Breast
            Cancer in Surgical and Cytology Specimens of Metastatic and Matched
            Primary Tumors
  JOURNAL   Appl Immunohistochem Mol Morphol 24 (4), 229-237 (2016)
   PUBMED   25906123
  REMARK    GeneRIF: novel marker GATA3 stains a significantly higher
            proportion of both primary and metastatic breast carcinomas than
            GCDFP15 or mammaglobin with stronger and more diffuse staining,
            helpful in cases with small tissue samples
            Review article
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Ni,Y.B., Tsang,J.Y., Chan,S.K. and Tse,G.M.
  TITLE     GATA-binding protein 3, gross cystic disease fluid protein-15 and
            mammaglobin have distinct prognostic implications in different
            invasive breast carcinoma subgroups
  JOURNAL   Histopathology 67 (1), 96-105 (2015)
   PUBMED   25425335
  REMARK    GeneRIF: The commonly used breast carcinoma biomarkers vary in
            their prognostic implications. GCDFP-15 independently indicated a
            favourable prognosis. GATA-3 and MGB were not associated with
            outcome.
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Cheng,M., Chen,Y., Zou,D., Shen,G., Bian,G., Shen,G. and Hu,S.
  TITLE     The clinical utility of circulating tumor cells in breast cancer
            patients: detection by a quantitative assay of h-MAM gene
            expression
  JOURNAL   Int J Biol Markers 29 (3), e268-e278 (2014)
   PUBMED   24706379
  REMARK    GeneRIF: Results indicate that the quantitative analysis of h-MAM
            mRNA is a useful tool for detecting CTCs in breast cancer patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Guan,W., Steffen,B.T., Lemaitre,R.N., Wu,J.H.Y., Tanaka,T.,
            Manichaikul,A., Foy,M., Rich,S.S., Wang,L., Nettleton,J.A.,
            Tang,W., Gu,X., Bandinelli,S., King,I.B., McKnight,B., Psaty,B.M.,
            Siscovick,D., Djousse,L., Chen,Y.I., Ferrucci,L., Fornage,M.,
            Mozafarrian,D., Tsai,M.Y. and Steffen,L.M.
  TITLE     Genome-wide association study of plasma N6 polyunsaturated fatty
            acids within the cohorts for heart and aging research in genomic
            epidemiology consortium
  JOURNAL   Circ Cardiovasc Genet 7 (3), 321-331 (2014)
   PUBMED   24823311
REFERENCE   6  (residues 1 to 95)
  AUTHORS   Evans,V., Vockler,C., Friedlander,M., Walsh,B. and Willcox,M.D.
  TITLE     Lacryglobin in human tears, a potential marker for cancer
  JOURNAL   Clin Exp Ophthalmol 29 (3), 161-163 (2001)
   PUBMED   11446459
REFERENCE   7  (residues 1 to 95)
  AUTHORS   Zhao,C., Nguyen,T., Yusifov,T., Glasgow,B.J. and Lehrer,R.I.
  TITLE     Lipophilins: human peptides homologous to rat prostatein
  JOURNAL   Biochem Biophys Res Commun 256 (1), 147-155 (1999)
   PUBMED   10066439
REFERENCE   8  (residues 1 to 95)
  AUTHORS   Becker,R.M., Darrow,C., Zimonjic,D.B., Popescu,N.C., Watson,M.A.
            and Fleming,T.P.
  TITLE     Identification of mammaglobin B, a novel member of the uteroglobin
            gene family
  JOURNAL   Genomics 54 (1), 70-78 (1998)
   PUBMED   9806831
REFERENCE   9  (residues 1 to 95)
  AUTHORS   Lehrer,R.I., Xu,G., Abduragimov,A., Dinh,N.N., Qu,X.D., Martin,D.
            and Glasgow,B.J.
  TITLE     Lipophilin, a novel heterodimeric protein of human tears
  JOURNAL   FEBS Lett 432 (3), 163-167 (1998)
   PUBMED   9720917
REFERENCE   10 (residues 1 to 95)
  AUTHORS   Molloy,M.P., Bolis,S., Herbert,B.R., Ou,K., Tyler,M.I., van
            Dyk,D.D., Willcox,M.D., Gooley,A.A., Williams,K.L., Morris,C.A. and
            Walsh,B.J.
  TITLE     Establishment of the human reflex tear two-dimensional
            polyacrylamide gel electrophoresis reference map: new proteins of
            potential diagnostic value
  JOURNAL   Electrophoresis 18 (15), 2811-2815 (1997)
   PUBMED   9504814
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF071219.1, BC062218.1, AJ224173.1 and AP003306.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD723581.1, BC062218.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000244930.6/ ENSP00000244930.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..95
                     /product="mammaglobin-B precursor"
                     /note="lipophilin C; mammaglobin-B; lacryglobin;
                     mammaglobin-2"
                     /calculated_mol_wt=8854
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2048
     Region          15..90
                     /region_name="Uteroglobin"
                     /note="Uteroglobin family; pfam01099"
                     /db_xref="CDD:460063"
     mat_peptide     19..95
                     /product="Mammaglobin-B. /id=PRO_0000036373"
                     /note="propagated from UniProtKB/Swiss-Prot (O75556.1)"
                     /calculated_mol_wt=8854
     Site            order(24..25,28,42,46,49,54..59,61..62,65,73,75..77,
                     79..80,83)
                     /site_type="other"
                     /note="Dimer interface [polypeptide binding]"
                     /db_xref="CDD:238346"
     Site            order(25,32,42,59,62,77,80..81)
                     /site_type="other"
                     /note="Hydrophobic pocket - steroid binding site [chemical
                     binding]"
                     /db_xref="CDD:238346"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75556.1)"
     CDS             1..95
                     /gene="SCGB2A1"
                     /gene_synonym="LPHC; LPNC; MGB2; UGB3"
                     /coded_by="NM_002407.3:60..347"
                     /db_xref="CCDS:CCDS8016.1"
                     /db_xref="GeneID:4246"
                     /db_xref="HGNC:HGNC:7051"
                     /db_xref="MIM:604398"
ORIGIN      
        1 mkllmvlmla alllhcyads gcklledmve ktinsdisip eykellqefi dsdaaaeamg
       61 kfkqcflnqs hrtlknfglm mhtvydsiwc nmksn
//
LOCUS       NP_080704                244 aa            linear   ROD 27-APR-2025
DEFINITION  L-xylulose reductase isoform 1 [Mus musculus].
ACCESSION   NP_080704
VERSION     NP_080704.2
DBSOURCE    REFSEQ: accession NM_026428.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Sapir,T., Kshirsagar,A., Gorelik,A., Olender,T., Porat,Z.,
            Scheffer,I.E., Goldstein,D.B., Devinsky,O. and Reiner,O.
  TITLE     Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the
            developing mouse cortex
  JOURNAL   Nat Commun 13 (1), 4209 (2022)
   PUBMED   35864088
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Hubbs,A.F., Fluharty,K.L., Edwards,R.J., Barnabei,J.L.,
            Grantham,J.T., Palmer,S.M., Kelly,F., Sargent,L.M., Reynolds,S.H.,
            Mercer,R.R., Goravanahally,M.P., Kashon,M.L., Honaker,J.C.,
            Jackson,M.C., Cumpston,A.M., Goldsmith,W.T., McKinney,W.,
            Fedan,J.S., Battelli,L.A., Munro,T., Bucklew-Moyers,W.,
            McKinstry,K., Schwegler-Berry,D., Friend,S., Knepp,A.K., Smith,S.L.
            and Sriram,K.
  TITLE     Accumulation of Ubiquitin and Sequestosome-1 Implicate Protein
            Damage in Diacetyl-Induced Cytotoxicity
  JOURNAL   Am J Pathol 186 (11), 2887-2908 (2016)
   PUBMED   27643531
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Abdallah,B.M., Ditzel,N., Mahmood,A., Isa,A., Traustadottir,G.A.,
            Schilling,A.F., Ruiz-Hidalgo,M.J., Laborda,J., Amling,M. and
            Kassem,M.
  TITLE     DLK1 is a novel regulator of bone mass that mediates estrogen
            deficiency-induced bone loss in mice
  JOURNAL   J Bone Miner Res 26 (7), 1457-1471 (2011)
   PUBMED   21308776
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Sudo,T., Ishii,A., Asami,J., Uematsu,Y., Saitoh,M., Nakamura,A.,
            Tada,N., Ohnuki,T., Komurasaki,T. and Nakagawa,J.
  TITLE     Transgenic mice over-expressing dicarbonyl/L-xylulose reductase
            gene crossed with KK-Ay diabetic model mice: an animal model for
            the metabolism of renal carbonyl compounds
  JOURNAL   Exp Anim 54 (5), 385-394 (2005)
   PUBMED   16365515
  REMARK    GeneRIF: DCXR might function in the metabolism of glucose or
            carbonyl compounds, and play a protective role in a kidney which is
            under hyperglycemic pressure.
REFERENCE   8  (residues 1 to 244)
  AUTHORS   Cheung,C.C., Martin,I.C., Zenger,K.R., Donald,J.A., Thomson,P.C.,
            Moran,C. and Buckley,M.F.
  TITLE     Quantitative trait loci for steady-state platelet count in mice
  JOURNAL   Mamm Genome 15 (10), 784-797 (2004)
   PUBMED   15520881
REFERENCE   9  (residues 1 to 244)
  AUTHORS   Nakagawa,J., Ishikura,S., Asami,J., Isaji,T., Usami,N., Hara,A.,
            Sakurai,T., Tsuritani,K., Oda,K., Takahashi,M., Yoshimoto,M.,
            Otsuka,N. and Kitamura,K.
  TITLE     Molecular characterization of mammalian dicarbonyl/L-xylulose
            reductase and its localization in kidney
  JOURNAL   J Biol Chem 277 (20), 17883-17891 (2002)
   PUBMED   11882650
  REMARK    GeneRIF: highly expressed in kidney and liver
REFERENCE   10 (residues 1 to 244)
  AUTHORS   Tulsiani,D.R. and Touster,O.
  TITLE     Studies on dehydrogenases of the glucuronate-xylulose cycle in the
            livers of diabetic mice and rats
  JOURNAL   Diabetes 28 (9), 793-798 (1979)
   PUBMED   38160
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL663030.12, AK007627.1, AK153521.1 and BY500715.1.
            
            On Apr 28, 2007 this sequence version replaced NP_080704.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI219348.1, AK004023.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 84.47 cM"
     Protein         1..244
                     /product="L-xylulose reductase isoform 1"
                     /EC_number="1.1.1.10"
                     /note="diacetyl/L-xylulose reductase"
                     /calculated_mol_wt=25615
     Region          1..243
                     /region_name="XR_like_SDR_c"
                     /note="xylulose reductase-like, classical (c) SDRs;
                     cd05351"
                     /db_xref="CDD:187609"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4W1; propagated from
                     UniProtKB/Swiss-Prot (Q91X52.2)"
     Site            order(14,16..19,38..40,43,59..62,83..86,102,106,134..136,
                     149,153,179..182,184..187)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187609"
     Site            21
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4W1; propagated from
                     UniProtKB/Swiss-Prot (Q91X52.2)"
     Site            order(64,91..93,95,97,100..101,104,108..109,112,115..116,
                     120,123,138..142,147..148,150..151,154..155,158..159,
                     161..166,168..169,203,205..208,210,213..214,217..218,221,
                     226,228..231,236..240,242..243)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187609"
     Site            order(64,91..93,95,97,100..101,104,108..109,112,115..116,
                     120,123,138..142,147..148,150..151,154..155,158..159,
                     161..163,165..166)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187609"
     Site            order(107,136,149,153)
                     /site_type="active"
                     /db_xref="CDD:187609"
     CDS             1..244
                     /gene="Dcxr"
                     /gene_synonym="0610038K04Rik; 1810027P18Rik; XR"
                     /coded_by="NM_026428.3:56..790"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS25755.1"
                     /db_xref="GeneID:67880"
                     /db_xref="MGI:MGI:1915130"
ORIGIN      
        1 mdlglagrra lvtgagkgig rstvlalkaa gaqvvavsrt redlddlvre cpgvepvcvd
       61 ladweateqa lsnvgpvdll vnnaavallq pflevtkeac dtsfnvnlra viqvsqivak
      121 gmiargvpga ivnvssqasq raltnhtvyc stkgaldmlt kmmalelgph kirvnavnpt
      181 vvmtpmgrtn wsdphkakam ldriplgkfa evenvvdtil fllsnrsgmt tgstlpvdgg
      241 flat
//
LOCUS       NP_001355756             976 aa            linear   ROD 27-APR-2025
DEFINITION  protein phosphatase 1 regulatory subunit 12B isoform 2 [Mus
            musculus].
ACCESSION   NP_001355756 XP_006529773
VERSION     NP_001355756.1
DBSOURCE    REFSEQ: accession NM_001368827.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Ye,Z., Okamoto,R., Ito,H., Ito,R., Moriwaki,K., Ichikawa,M.,
            Kimena,L., Ali,Y., Ito,M., Gomez-Sanchez,C.E. and Dohi,K.
  TITLE     Myosin Light Chain Phosphatase Plays an Important Role in Cardiac
            Fibrosis in a Model of Mineralocorticoid Receptor-Associated
            Hypertension
  JOURNAL   J Am Heart Assoc 13 (5), e032828 (2024)
   PUBMED   38420846
  REMARK    GeneRIF: Myosin Light Chain Phosphatase Plays an Important Role in
            Cardiac Fibrosis in a Model of Mineralocorticoid
            Receptor-Associated Hypertension.
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Lee,E., May,H., Kazmierczak,K., Liang,J., Nguyen,N., Hill,J.A.,
            Gillette,T.G., Szczesna-Cordary,D. and Chang,A.N.
  TITLE     The MYPT2-regulated striated muscle-specific myosin light chain
            phosphatase limits cardiac myosin phosphorylation in vivo
  JOURNAL   J Biol Chem 300 (2), 105652 (2024)
   PUBMED   38224947
  REMARK    GeneRIF: The MYPT2-regulated striated muscle-specific myosin light
            chain phosphatase limits cardiac myosin phosphorylation in vivo.
REFERENCE   4  (residues 1 to 976)
  AUTHORS   Hu,T., Kalyanaraman,H., Pilz,R.B. and Casteel,D.E.
  TITLE     Phosphatase regulatory subunit MYPT2 knockout partially compensates
            for the cardiac dysfunction in mice caused by lack of myosin light
            chain kinase 3
  JOURNAL   J Biol Chem 299 (4), 104584 (2023)
   PUBMED   36889588
  REMARK    GeneRIF: Phosphatase regulatory subunit MYPT2 knockout partially
            compensates for the cardiac dysfunction in mice caused by lack of
            myosin light chain kinase 3.
REFERENCE   5  (residues 1 to 976)
  AUTHORS   Liu,K., Zhao,J., Chen,C., Xu,J., Bell,R.L., Hall,F.S., Koob,G.F.,
            Volkow,N.D., Qing,H. and Lin,Z.
  TITLE     Epistatic evidence for gender-dependant slow neurotransmission
            signalling in substance use disorders: PPP1R12B versus PPP1R1B
  JOURNAL   EBioMedicine 61, 103066 (2020)
   PUBMED   33096475
  REMARK    GeneRIF: Epistatic evidence for gender-dependant slow
            neurotransmission signalling in substance use disorders: PPP1R12B
            versus PPP1R1B.
REFERENCE   6  (residues 1 to 976)
  AUTHORS   Hughes,J.J., Alkhunaizi,E., Kruszka,P., Pyle,L.C., Grange,D.K.,
            Berger,S.I., Payne,K.K., Masser-Frye,D., Hu,T., Christie,M.R.,
            Clegg,N.J., Everson,J.L., Martinez,A.F., Walsh,L.E., Bedoukian,E.,
            Jones,M.C., Harris,C.J., Riedhammer,K.M., Choukair,D.,
            Fechner,P.Y., Rutter,M.M., Hufnagel,S.B., Roifman,M., Kletter,G.B.,
            Delot,E., Vilain,E., Lipinski,R.J., Vezina,C.M., Muenke,M. and
            Chitayat,D.
  TITLE     Loss-of-Function Variants in PPP1R12A: From Isolated Sex Reversal
            to Holoprosencephaly Spectrum and Urogenital Malformations
  JOURNAL   Am J Hum Genet 106 (1), 121-128 (2020)
   PUBMED   31883643
REFERENCE   7  (residues 1 to 976)
  AUTHORS   Mizutani,H., Okamoto,R., Moriki,N., Konishi,K., Taniguchi,M.,
            Fujita,S., Dohi,K., Onishi,K., Suzuki,N., Satoh,S., Makino,N.,
            Itoh,T., Hartshorne,D.J. and Ito,M.
  TITLE     Overexpression of myosin phosphatase reduces Ca(2+) sensitivity of
            contraction and impairs cardiac function
  JOURNAL   Circ J 74 (1), 120-128 (2010)
   PUBMED   19966500
  REMARK    GeneRIF: MYPT2 is truly the regulatory subunit of cardiac myosin
            phosphatase in-vivo and plays a significant role in modulating
            cardiac function.
REFERENCE   8  (residues 1 to 976)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   9  (residues 1 to 976)
  AUTHORS   Arimura,T., Suematsu,N., Zhou,Y.B., Nishimura,J., Satoh,S.,
            Takeshita,A., Kanaide,H. and Kimura,A.
  TITLE     Identification, characterization, and functional analysis of
            heart-specific myosin light chain phosphatase small subunit
  JOURNAL   J Biol Chem 276 (9), 6073-6082 (2001)
   PUBMED   11067852
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC117827.6 and AC131591.13.
            
            On Mar 1, 2019 this sequence version replaced XP_006529773.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164139
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 58.24 cM"
     Protein         1..976
                     /product="protein phosphatase 1 regulatory subunit 12B
                     isoform 2"
                     /EC_number="3.1.3.53"
                     /note="myosin phosphatase target subunit 2; myosin
                     phosphatase-targeting subunit 2; protein phosphatase 1,
                     regulatory (inhibitor) subunit 12B"
                     /calculated_mol_wt=108919
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG95.2)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BG95.2)"
     Region          57..86
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG95.2)"
     Region          <62..290
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(67..69,71..72,76,79,88,90,92,96..97,100..102,
                     104..105,109,112,121,123,125,129..130,133..135,137..138,
                     142,145,154)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          90..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          90..119
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG95.2)"
     Region          123..154
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          123..152
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG95.2)"
     Region          156..247
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <169..>257
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Region          216..245
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG95.2)"
     Region          249..280
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          249..278
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG95.2)"
     Region          342..489
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG95.2)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BG95.2)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BG95.2)"
     Region          503..873
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BG95.2)"
     Region          608..663
                     /region_name="IPD_MYPT1"
                     /note="inhibitory phosphorylation domain of myosin
                     phosphatase targeting subunit 1(MYPT1); cd21944"
                     /db_xref="CDD:412019"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60237; propagated from
                     UniProtKB/Swiss-Prot (Q8BG95.2)"
     Site            802
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BG95.2)"
     Site            833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BG95.2)"
     Region          875..976
                     /region_name="PRKG1_interact"
                     /note="cGMP-dependent protein kinase interacting domain;
                     pfam15898"
                     /db_xref="CDD:464927"
     Site            941
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BG95.2)"
     CDS             1..976
                     /gene="Ppp1r12b"
                     /gene_synonym="1810037O03Rik; 9530009M10Rik; Mypt2"
                     /coded_by="NM_001368827.1:159..3089"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS87881.1"
                     /db_xref="GeneID:329251"
                     /db_xref="MGI:MGI:1916417"
ORIGIN      
        1 maelehlggk raesararra eqlrrwrgsl teqepaerqg agrqlqtrrg sprvrfedga
       61 vflaacssgd tdevkkllar gadintvnvd gltalhqaci denldmvkfl venranvnqq
      121 dnegwtplha aascgylnia eyfishgasv givnsegevp sdlaeepamk dllleqvkkq
      181 gvdleqsrke eeqqmlqdar qwlnsgried vrqarsgata lhvaaakgys evlrlliqag
      241 yelnvqdhdg wtplhaaahw gvkeacsila ealcdmdirn klgqtpfdva deglvehlem
      301 lqkkqdvlrs eketrnklie sdlnskfqsg lfknkekmly eeeipksqdt eeenkessss
      361 sseeeegede vsesetekea dkkpeatvnh snseiksrim eqipapaqnt fsassarrls
      421 slfnkaeepk despsswrlg lrktgshnml sevansreal rdrgssiyrs sssprisall
      481 ddkdkerenk syfsmlvprr lsstsdieek enresavnlv rsgshtrqlw rdeakgsetp
      541 qtiapstyts tylkrtpyks qadstaekta dsvssstplc vitnrpapst angvpaatvf
      601 ssagtdpsve arekrrsylt pvrdeeaesl rkarsrqarq trrstqgvtl tdlqeaektf
      661 srsraerqaq eqpgekledp gglegstkkq epsaaptkga gegrsleeep iyhrlryptq
      721 pdkpttpvsp sasrpslytg shllrtsras gpdsensets thataakemd tsekgeadld
      781 dqssnrlsvr errrakdrrr gtginfwtnd edetdvseev kealherlsr lesggtnpts
      841 sdsysdrasa rarrearear lasltsrvee dsnrdykkly esaltenqkl ktklqeaqle
      901 ladikaklek maqqkqekts drssvlevek rerralerkm semeeemkvl telksdnqrl
      961 kdengalirv isklsk
//
LOCUS       NP_003816                211 aa            linear   PRI 27-APR-2025
DEFINITION  synaptosomal-associated protein 23 isoform SNAP23A [Homo sapiens].
ACCESSION   NP_003816
VERSION     NP_003816.2
DBSOURCE    REFSEQ: accession NM_003825.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Gigon,L., Fettrelet,T., Miholic,M., McLeish,K.R., Yousefi,S.,
            Stojkov,D. and Simon,H.U.
  TITLE     Syntaxin-4 and SNAP23 are involved in neutrophil degranulation, but
            not in the release of mitochondrial DNA during NET formation
  JOURNAL   Front Immunol 14, 1272699 (2023)
   PUBMED   37885878
  REMARK    GeneRIF: Syntaxin-4 and SNAP23 are involved in neutrophil
            degranulation, but not in the release of mitochondrial DNA during
            NET formation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Xie,B.W., Guan,B., Chen,W., Zhou,M., Gu,Q., Liu,Y. and Yan,D.
  TITLE     Tumor-derived extracellular vesicles delivering TNF-alpha promotes
            colorectal cancer metastasis via the NF-kB/LAMB3/AKT axis by
            targeting SNAP23
  JOURNAL   Arch Biochem Biophys 741, 109605 (2023)
   PUBMED   37086961
  REMARK    GeneRIF: Tumor-derived extracellular vesicles delivering TNF-alpha
            promotes colorectal cancer metastasis via the NF-kB/LAMB3/AKT axis
            by targeting SNAP23.
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Miller,K., Wagner,M.A., Jassey,A. and Jackson,W.T.
  TITLE     SNAP23 is essential for germination of EV-D68 replication
            organelles
  JOURNAL   Virology 578, 117-127 (2023)
   PUBMED   36527930
  REMARK    GeneRIF: SNAP23 is essential for germination of EV-D68 replication
            organelles.
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Mitani,F., Hayasaka,R., Hirayama,A. and Oneyama,C.
  TITLE     SNAP23-Mediated Perturbation of Cholesterol-Enriched Membrane
            Microdomain Promotes Extracellular Vesicle Production in
            Src-Activated Cancer Cells
  JOURNAL   Biol Pharm Bull 45 (10), 1572-1580 (2022)
   PUBMED   36184518
  REMARK    GeneRIF: SNAP23-Mediated Perturbation of Cholesterol-Enriched
            Membrane Microdomain Promotes Extracellular Vesicle Production in
            Src-Activated Cancer Cells.
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Tang,B.L., Tan,A.E., Lim,L.K., Lee,S.S., Low,D.Y. and Hong,W.
  TITLE     Syntaxin 12, a member of the syntaxin family localized to the
            endosome
  JOURNAL   J Biol Chem 273 (12), 6944-6950 (1998)
   PUBMED   9507000
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Araki,S., Tamori,Y., Kawanishi,M., Shinoda,H., Masugi,J., Mori,H.,
            Niki,T., Okazawa,H., Kubota,T. and Kasuga,M.
  TITLE     Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c
  JOURNAL   Biochem Biophys Res Commun 234 (1), 257-262 (1997)
   PUBMED   9168999
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Mollinedo,F. and Lazo,P.A.
  TITLE     Identification of two isoforms of the vesicle-membrane fusion
            protein SNAP-23 in human neutrophils and HL-60 cells
  JOURNAL   Biochem Biophys Res Commun 231 (3), 808-812 (1997)
   PUBMED   9070898
REFERENCE   10 (residues 1 to 211)
  AUTHORS   Ravichandran,V., Chawla,A. and Roche,P.A.
  TITLE     Identification of a novel syntaxin- and synaptobrevin/VAMP-binding
            protein, SNAP-23, expressed in non-neuronal tissues
  JOURNAL   J Biol Chem 271 (23), 13300-13303 (1996)
   PUBMED   8663154
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290152.1, BC022890.1 and
            BM782600.1.
            
            On Feb 19, 2002 this sequence version replaced NP_003816.1.
            
            Summary: Specificity of vesicular transport is regulated, in part,
            by the interaction of a vesicle-associated membrane protein termed
            synaptobrevin/VAMP with a target compartment membrane protein
            termed syntaxin. These proteins, together with SNAP25
            (synaptosome-associated protein of 25 kDa), form a complex which
            serves as a binding site for the general membrane fusion machinery.
            Synaptobrevin/VAMP and syntaxin are believed to be involved in
            vesicular transport in most, if not all cells, while SNAP25 is
            present almost exclusively in the brain, suggesting that a
            ubiquitously expressed homolog of SNAP25 exists to facilitate
            transport vesicle/target membrane fusion in other tissues. The
            protein encoded by this gene is structurally and functionally
            similar to SNAP25 and binds tightly to multiple syntaxins and
            synaptobrevins/VAMPs. It is an essential component of the high
            affinity receptor for the general membrane fusion machinery and is
            an important regulator of transport vesicle docking and fusion. Two
            alternative transcript variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the longer transcript,
            containing eight exons and encoding the full-length isoform
            (SNAP23A).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.112212.1,
                                           SRR1660809.125591.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000249647.8/ ENSP00000249647.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1-q15.2"
     Protein         1..211
                     /product="synaptosomal-associated protein 23 isoform
                     SNAP23A"
                     /note="synaptosomal-associated protein 23;
                     synaptosomal-associated protein, 23kDa; vesicle-membrane
                     fusion protein SNAP-23; synaptosome associated protein
                     23kDa"
                     /calculated_mol_wt=23223
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (O00161.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Region          9..75
                     /region_name="SNARE_SNAP23N"
                     /note="N-terminal SNARE motif of SNAP23; cd15895"
                     /db_xref="CDD:277248"
     Site            order(13,16..21,23..28,30..31,34..35,37..42,44..45,47..49,
                     51..56,58..59,61..63,65..66,68..70,72..73,75)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277248"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O09044; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Site            48
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277248"
     Region          86..148
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00161.1)"
     Region          149..207
                     /region_name="SNARE_SNAP23C"
                     /note="C-terminal SNARE motif of SNAP23; cd15884"
                     /db_xref="CDD:277237"
     Site            order(149,151..152,155..160,162..163,166..167,169..171,
                     173..174,177..178,180..181,183..188,190..191,194,197,201,
                     204,207)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277237"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Site            180
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277237"
     CDS             1..211
                     /gene="SNAP23"
                     /gene_synonym="HsT17016; SNAP-23; SNAP23A; SNAP23B"
                     /coded_by="NM_003825.4:95..730"
                     /note="isoform SNAP23A is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10087.1"
                     /db_xref="GeneID:8773"
                     /db_xref="HGNC:HGNC:11131"
                     /db_xref="MIM:602534"
ORIGIN      
        1 mdnlsseeiq qrahqitdes lestrrilgl aiesqdagik titmldeqke qlnrieegld
       61 qinkdmrete ktltelnkcc glcvcpcnrt knfesgkayk ttwgdggens pcnvvskqpg
      121 pvtngqlqqp ttgaasggyi kritndared emeenltqvg silgnlkdma lnigneidaq
      181 npqikritdk adtnrdridi anarakklid s
//
LOCUS       NP_036230                493 aa            linear   PRI 27-APR-2025
DEFINITION  angiopoietin-related protein 2 precursor [Homo sapiens].
ACCESSION   NP_036230
VERSION     NP_036230.1
DBSOURCE    REFSEQ: accession NM_012098.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Liu,P.I., Jiang,Y.J., Chang,A.C., Huang,C.L., Fong,Y.C., Guo,J.H.,
            Liu,C.L., Wang,S.W., Liu,J.F., Chang,S.L. and Tang,C.H.
  TITLE     ANGPTL2 promotes VEGF-A synthesis in human lung cancer and
            facilitates lymphangiogenesis
  JOURNAL   Aging (Albany NY) 15 (5), 1652-1667 (2023)
   PUBMED   36917086
  REMARK    GeneRIF: ANGPTL2 promotes VEGF-A synthesis in human lung cancer and
            facilitates lymphangiogenesis.
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Jiang,C., Yao,S., Guo,Y., Ma,L., Wang,X., Chen,Y., Zhang,H. and
            Cao,Z.
  TITLE     Angiopoietin-like protein 2 deficiency promotes periodontal
            inflammation and alveolar bone loss
  JOURNAL   J Periodontol 93 (10), 1525-1539 (2022)
   PUBMED   34709660
  REMARK    GeneRIF: Angiopoietin-like protein 2 deficiency promotes
            periodontal inflammation and alveolar bone loss.
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Thorin-Trescases,N., Labbe,P., Mury,P., Lambert,M. and Thorin,E.
  TITLE     Angptl2 is a Marker of Cellular Senescence: The Physiological and
            Pathophysiological Impact of Angptl2-Related Senescence
  JOURNAL   Int J Mol Sci 22 (22), 12232 (2021)
   PUBMED   34830112
  REMARK    GeneRIF: Angptl2 is a Marker of Cellular Senescence: The
            Physiological and Pathophysiological Impact of Angptl2-Related
            Senescence.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Takeshita,Y., Motohara,T., Kadomatsu,T., Doi,T., Obayashi,K.,
            Oike,Y., Katabuchi,H. and Endo,M.
  TITLE     Angiopoietin-like protein 2 decreases peritoneal metastasis of
            ovarian cancer cells by suppressing anoikis resistance
  JOURNAL   Biochem Biophys Res Commun 561, 26-32 (2021)
   PUBMED   34000514
  REMARK    GeneRIF: Angiopoietin-like protein 2 decreases peritoneal
            metastasis of ovarian cancer cells by suppressing anoikis
            resistance.
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Xie,P., Wang,H., Fang,J., Du,D., Tian,Z., Zhen,J., Liu,Y., Ding,Y.,
            Fu,B., Liu,F., Huang,D. and Yu,J.
  TITLE     CSN5 Promotes Carcinogenesis of Thyroid Carcinoma Cells Through
            ANGPTL2
  JOURNAL   Endocrinology 162 (3) (2021)
   PUBMED   33508120
  REMARK    GeneRIF: CSN5 Promotes Carcinogenesis of Thyroid Carcinoma Cells
            Through ANGPTL2.
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Sun,H., Zheng,J.M., Chen,S., Zeng,C.H., Liu,Z.H. and Li,L.S.
  TITLE     Enhanced expression of ANGPTL2 in the microvascular lesions of
            diabetic glomerulopathy
  JOURNAL   Nephron Exp Nephrol 105 (4), e117-e123 (2007)
   PUBMED   17347581
  REMARK    GeneRIF: The upregulation of ANGPTL2 in diabetic glomerulopathy
            shows a close relationship to abnormal microvasculature and
            endothelial inflammation.
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Zeng,L., Dai,J., Ying,K., Zhao,E., Jin,W., Ye,Y., Dai,J., Xu,J.,
            Xie,Y. and Mao,Y.
  TITLE     Identification of a novel human angiopoietin-like gene expressed
            mainly in heart
  JOURNAL   J Hum Genet 48 (3), 159-162 (2003)
   PUBMED   12624729
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Kim,I., Moon,S.O., Koh,K.N., Kim,H., Uhm,C.S., Kwak,H.J., Kim,N.G.
            and Koh,G.Y.
  TITLE     Molecular cloning, expression, and characterization of
            angiopoietin-related protein. angiopoietin-related protein induces
            endothelial cell sprouting
  JOURNAL   J Biol Chem 274 (37), 26523-26528 (1999)
   PUBMED   10473614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL598400.1, BC012368.1,
            AK074726.1 and AL356862.10.
            
            Summary: Angiopoietins are members of the vascular endothelial
            growth factor family and the only known growth factors largely
            specific for vascular endothelium. Angiopoietin-1, angiopoietin-2,
            and angiopoietin-4 participate in the formation of blood vessels.
            ANGPTL2 protein is a secreted glycoprotein with homology to the
            angiopoietins and may exert a function on endothelial cells through
            autocrine or paracrine action. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.944677.1,
                                           SRR3476690.517902.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373425.8/ ENSP00000362524.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..493
                     /product="angiopoietin-related protein 2 precursor"
                     /note="angiopoietin-related protein 2; angiopoietin-like
                     protein 2"
                     /calculated_mol_wt=54803
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2320
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UKU9.1)"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UKU9.1)"
     Region          273..487
                     /region_name="FReD"
                     /note="Fibrinogen-related domains (FReDs); C terminal
                     globular domain of fibrinogen. Fibrinogen is involved in
                     blood clotting, being activated by thrombin to assemble
                     into fibrin clots. The N-termini of 2 times 3 chains come
                     together to form a globular...; cd00087"
                     /db_xref="CDD:238040"
     Site            394
                     /site_type="other"
                     /note="gamma-gamma dimer interface [polypeptide binding]"
                     /db_xref="CDD:238040"
     Site            order(422,424,426)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238040"
     Site            order(430,433..434,443..444)
                     /site_type="active"
                     /note="polymerization pocket [active]"
                     /db_xref="CDD:238040"
     CDS             1..493
                     /gene="ANGPTL2"
                     /gene_synonym="ARP2; HARP"
                     /coded_by="NM_012098.3:371..1852"
                     /db_xref="CCDS:CCDS6868.1"
                     /db_xref="GeneID:23452"
                     /db_xref="HGNC:HGNC:490"
                     /db_xref="MIM:605001"
ORIGIN      
        1 mrplcvtcww lgllaamgav agqedgfegt eegsprefiy lnrykrages qdkctytfiv
       61 pqqrvtgaic vnskepevll enrvhkqele llnnellkqk rqietlqqlv evdggivsev
      121 kllrkesrnm nsrvtqlymq llheiirkrd nalelsqlen rilnqtadml qlaskykdle
      181 hkyqhlatla hnqseiiaql eehcqrvpsa rpvpqpppaa pprvyqppty nriinqistn
      241 eiqsdqnlkv lppplptmpt ltslpsstdk psgpwrdclq aledghdtss iylvkpentn
      301 rlmqvwcdqr hdpggwtviq rrldgsvnff rnwetykqgf gnidgeywlg leniywltnq
      361 gnykllvtme dwsgrkvfae yasfrlepes eyyklrlgry hgnagdsftw hngkqfttld
      421 rdhdvytgnc ahyqkggwwy nacahsnlng vwyrgghyrs ryqdgvywae frggsyslkk
      481 vvmmirpnpn tfh
//
LOCUS       NP_005788                215 aa            linear   PRI 27-APR-2025
DEFINITION  myelin protein zero-like protein 2 precursor [Homo sapiens].
ACCESSION   NP_005788
VERSION     NP_005788.1
DBSOURCE    REFSEQ: accession NM_005797.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Lo,E., Blair,J., Yamamoto,N., Diaz-Miranda,M.A., Bedoukian,E.,
            Gray,C., Lawrence,A., Dedhia,K., Elden,L.M., Germiller,J.A.,
            Kazahaya,K., Sobol,S.E., Luo,M., Krantz,I.D. and Hartman,T.R.
  TITLE     Recurrent missense variant identified in two unrelated families
            with MPZL2-related hearing loss, expanding the variant spectrum
            associated with DFNB111
  JOURNAL   Am J Med Genet A 194 (5), e63530 (2024)
   PUBMED   38197511
  REMARK    GeneRIF: Recurrent missense variant identified in two unrelated
            families with MPZL2-related hearing loss, expanding the variant
            spectrum associated with DFNB111.
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Zhang,L., Yang,J.Y., Wang,Q.Q., Gao,X., Wang,G.J., Han,M.Y.,
            Kang,D.Y., Han,D.Y., Huang,S.S. and Yuan,Y.Y.
  TITLE     MPZL2-a common autosomal recessive deafness gene related to
            moderate sensorineural hearing loss in the Chinese population
  JOURNAL   BMC Med Genomics 17 (1), 32 (2024)
   PUBMED   38254107
  REMARK    GeneRIF: MPZL2-a common autosomal recessive deafness gene related
            to moderate sensorineural hearing loss in the Chinese population.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Li,W., Guo,L., Chen,B., Shu,Y. and Li,H.
  TITLE     MPZL2 variant analysis with whole exome sequencing in a cohort of
            Chinese hearing loss patients
  JOURNAL   Int J Pediatr Otorhinolaryngol 171, 111635 (2023)
   PUBMED   37390746
  REMARK    GeneRIF: MPZL2 variant analysis with whole exome sequencing in a
            cohort of Chinese hearing loss patients.
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Eshibona,N., Giwa,A., Rossouw,S.C., Gamieldien,J., Christoffels,A.
            and Bendou,H.
  TITLE     Upregulation of FHL1, SPNS3, and MPZL2 predicts poor prognosis in
            pediatric acute myeloid leukemia patients with FLT3-ITD mutation
  JOURNAL   Leuk Lymphoma 63 (8), 1897-1906 (2022)
   PUBMED   35249471
  REMARK    GeneRIF: Upregulation of FHL1, SPNS3, and MPZL2 predicts poor
            prognosis in pediatric acute myeloid leukemia patients with
            FLT3-ITD mutation.
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Amalou,G., Bonnet,C., Riahi,Z., Bouzidi,A., Elrharchi,S.,
            Bousfiha,A., Charif,M., Kandil,M., Lenaers,G., Petit,C. and
            Barakat,A.
  TITLE     A homozygous MPZL2 deletion is associated with non syndromic
            hearing loss in a moroccan family
  JOURNAL   Int J Pediatr Otorhinolaryngol 140, 110481 (2021)
   PUBMED   33234333
  REMARK    GeneRIF: A homozygous MPZL2 deletion is associated with non
            syndromic hearing loss in a moroccan family.
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Ohtsu,N., Nakatani,Y., Yamashita,D., Ohue,S., Ohnishi,T. and
            Kondo,T.
  TITLE     Eva1 Maintains the Stem-like Character of Glioblastoma-Initiating
            Cells by Activating the Noncanonical NF-kappaB Signaling Pathway
  JOURNAL   Cancer Res 76 (1), 171-181 (2016)
   PUBMED   26677976
  REMARK    GeneRIF: Findings highlight Eva1 as a novel regulator of GIC
            function and also provide new mechanistic insight into the role of
            noncanonical NF-kappaB activation in GIC.
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Ramani,S.R., Tom,I., Lewin-Koh,N., Wranik,B., Depalatis,L.,
            Zhang,J., Eaton,D. and Gonzalez,L.C.
  TITLE     A secreted protein microarray platform for extracellular protein
            interaction discovery
  JOURNAL   Anal Biochem 420 (2), 127-138 (2012)
   PUBMED   21982860
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Wojcik,E., Carrithers,L.M. and Carrithers,M.D.
  TITLE     Characterization of epithelial V-like antigen in human choroid
            plexus epithelial cells: potential role in CNS immune surveillance
  JOURNAL   Neurosci Lett 495 (2), 115-120 (2011)
   PUBMED   21440040
  REMARK    GeneRIF: EVA is expressed in human choroid plexus epithelial cells
            and CD4 T lymphocytes and regulates CD4+ T lymphocyte adhesion to
            human choroid plexus epithelial cells in vitro. These data suggest
            a novel mechanism to regulate CNS immune surveillance.
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Guttinger,M., Sutti,F., Panigada,M., Porcellini,S., Merati,B.,
            Mariani,M., Teesalu,T., Consalez,G.G. and Grassi,F.
  TITLE     Epithelial V-like antigen (EVA), a novel member of the
            immunoglobulin superfamily, expressed in embryonic epithelia with a
            potential role as homotypic adhesion molecule in thymus
            histogenesis
  JOURNAL   J Cell Biol 141 (4), 1061-1071 (1998)
   PUBMED   9585423
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA163069.1, AF275945.1 and
            AW073724.1.
            
            Summary: Thymus development depends on a complex series of
            interactions between thymocytes and the stromal component of the
            organ. Epithelial V-like antigen (EVA) is expressed in thymus
            epithelium and strongly downregulated by thymocyte developmental
            progression. This gene is expressed in the thymus and in several
            epithelial structures early in embryogenesis. It is highly
            homologous to the myelin protein zero and, in thymus-derived
            epithelial cell lines, is poorly soluble in nonionic detergents,
            strongly suggesting an association to the cytoskeleton. Its
            capacity to mediate cell adhesion through a homophilic interaction
            and its selective regulation by T cell maturation might imply the
            participation of EVA in the earliest phases of thymus
            organogenesis. The protein bears a characteristic V-type domain and
            two potential N-glycosylation sites in the extracellular domain; a
            putative serine phosphorylation site for casein kinase 2 is also
            present in the cytoplasmic tail. Two transcript variants encoding
            the same protein have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.142024.1,
                                           SRR1660805.227446.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278937.7/ ENSP00000278937.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..215
                     /product="myelin protein zero-like protein 2 precursor"
                     /note="epithelial V-like antigen 1; myelin protein
                     zero-like protein 2"
                     /calculated_mol_wt=21715
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2787
     mat_peptide     27..215
                     /product="myelin protein zero-like protein 2"
                     /calculated_mol_wt=21715
     Region          27..142
                     /region_name="IgV_EVA1"
                     /note="Immunoglobulin (Ig)-like domain of epithelial
                     V-like antigen (EVA) 1; cd05880"
                     /db_xref="CDD:409464"
     Region          27..50
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409464"
     Region          27..31
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409464"
     Region          33..39
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409464"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O60487.1)"
     Region          41..51
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409464"
     Region          51..59
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409464"
     Region          59..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409464"
     Region          60..72
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409464"
     Region          73..86
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409464"
     Region          74..80
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409464"
     Region          81..86
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409464"
     Region          91..125
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409464"
     Region          94..100
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409464"
     Region          104..112
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409464"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60487.1)"
     Region          119..126
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409464"
     Region          127..133
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409464"
     Region          134..142
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409464"
     Region          134..142
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409464"
     Site            155..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60487.1)"
     CDS             1..215
                     /gene="MPZL2"
                     /gene_synonym="DFNB111; EVA; EVA1"
                     /coded_by="NM_005797.4:145..792"
                     /db_xref="CCDS:CCDS8393.1"
                     /db_xref="GeneID:10205"
                     /db_xref="HGNC:HGNC:3496"
                     /db_xref="MIM:604873"
ORIGIN      
        1 mygksstrav llllgiqlta lwpiaaveiy tsrvleavng tdarlkctfs sfapvgdalt
       61 vtwnfrpldg gpeqfvfyyh idpfqpmsgr fkdrvswdgn perydasill wklqfddngt
      121 ytcqvknppd vdgvigeirl svvhtvrfse ihflalaigs acalmiiivi vvvlfqhyrk
      181 krwaerahkv veikskeeer lnqekkvsvy ledtd
//
LOCUS       NP_000176                499 aa            linear   PRI 27-APR-2025
DEFINITION  heparin cofactor 2 precursor [Homo sapiens].
ACCESSION   NP_000176
VERSION     NP_000176.2
DBSOURCE    REFSEQ: accession NM_000185.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Hara,T., Uemoto,R., Sekine,A., Mitsui,Y., Masuda,S., Yamagami,H.,
            Kurahashi,K., Yoshida,S., Otoda,T., Yuasa,T., Kuroda,A., Ikeda,Y.,
            Endo,I., Honda,S., Yoshimoto,K., Kondo,A., Tamaki,T., Matsumoto,T.,
            Matsuhisa,M., Abe,M. and Aihara,K.I.
  TITLE     Plasma Heparin Cofactor II Activity Is Inversely Associated with
            Hepatic Fibrosis of Non-Alcoholic Fatty Liver Disease in Patients
            with Type 2 Diabetes Mellitus
  JOURNAL   J Atheroscler Thromb 30 (8), 871-883 (2023)
   PUBMED   36244745
  REMARK    GeneRIF: Plasma Heparin Cofactor II Activity Is Inversely
            Associated with Hepatic Fibrosis of Non-Alcoholic Fatty Liver
            Disease in Patients with Type 2 Diabetes Mellitus.
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Bano,S., Fatima,S., Ahamad,S., Ansari,S., Gupta,D., Tabish,M.,
            Rehman,S.U. and Jairajpuri,M.A.
  TITLE     Identification and characterization of a novel isoform of heparin
            cofactor II in human liver
  JOURNAL   IUBMB Life 72 (10), 2180-2193 (2020)
   PUBMED   32827448
  REMARK    GeneRIF: Identification and characterization of a novel isoform of
            heparin cofactor II in human liver.
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Van Deerlin,V.M. and Tollefsen,D.M.
  TITLE     The N-terminal acidic domain of heparin cofactor II mediates the
            inhibition of alpha-thrombin in the presence of glycosaminoglycans
  JOURNAL   J Biol Chem 266 (30), 20223-20231 (1991)
   PUBMED   1939083
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Herzog,R., Lutz,S., Blin,N., Marasa,J.C., Blinder,M.A. and
            Tollefsen,D.M.
  TITLE     Complete nucleotide sequence of the gene for human heparin cofactor
            II and mapping to chromosomal band 22q11
  JOURNAL   Biochemistry 30 (5), 1350-1357 (1991)
   PUBMED   1671335
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Church,F.C., Pratt,C.W. and Hoffman,M.
  TITLE     Leukocyte chemoattractant peptides from the serpin heparin cofactor
            II
  JOURNAL   J Biol Chem 266 (2), 704-709 (1991)
   PUBMED   1985958
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Uszynski,M.
  TITLE     Tissue anticoagulants in the human placenta: preliminary study with
            a heparin-like anticoagulant and review of the literature
  JOURNAL   Gynecol Obstet Invest 32 (3), 129-133 (1991)
   PUBMED   1836773
  REMARK    Review article
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Blinder,M.A. and Tollefsen,D.M.
  TITLE     Site-directed mutagenesis of arginine 103 and lysine 185 in the
            proposed glycosaminoglycan-binding site of heparin cofactor II
  JOURNAL   J Biol Chem 265 (1), 286-291 (1990)
   PUBMED   2104620
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Blinder,M.A., Marasa,J.C., Reynolds,C.H., Deaven,L.L. and
            Tollefsen,D.M.
  TITLE     Heparin cofactor II: cDNA sequence, chromosome localization,
            restriction fragment length polymorphism, and expression in
            Escherichia coli
  JOURNAL   Biochemistry 27 (2), 752-759 (1988)
   PUBMED   2894851
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007308.13 and BC035028.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 29, 2005 this sequence version replaced NP_000176.1.
            
            Summary: This gene belongs to the serpin gene superfamily. Serpins
            play roles in many processes including inflammation, blood
            clotting, and cancer metastasis. Members of this family have highly
            conserved secondary structures with a reactive center loop that
            interacts with the protease active site to inhibit protease
            activity. This gene encodes a plasma serine protease that functions
            as a thrombin and chymotrypsin inhibitor. The protein is activated
            by heparin, dermatan sulfate, and glycosaminoglycans. Allelic
            variations in this gene are associated with heparin cofactor II
            deficiency. [provided by RefSeq, Jul 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035028.2, SRR1803613.60943.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215727.10/ ENSP00000215727.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..499
                     /product="heparin cofactor 2 precursor"
                     /note="serine (or cysteine) proteinase inhibitor, clade D
                     (heparin cofactor), member 1; leuserpin 2; heparin
                     cofactor 2; serpin D1; protease inhibitor leuserpin-2;
                     serpin peptidase inhibitor, clade D (heparin cofactor),
                     member 1"
                     /calculated_mol_wt=54960
     sig_peptide     1..19
                     /note="/evidence=ECO:0000269|PubMed:3907702; propagated
                     from UniProtKB/Swiss-Prot (P05546.3)"
                     /calculated_mol_wt=2129
     mat_peptide     20..499
                     /product="heparin cofactor 2"
                     /calculated_mol_wt=54960
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P05546.3)"
     Site            49
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (P05546.3)"
     Region          51..499
                     /region_name="serpinD1_HCF2"
                     /note="serpin family D member 1, Heparin cofactor II;
                     cd02047"
                     /db_xref="CDD:381004"
     Region          68..79
                     /region_name="Chemotactic activity"
                     /note="propagated from UniProtKB/Swiss-Prot (P05546.3)"
     Region          73..97
                     /region_name="2 X 11 AA approximate repeats, Asp/Glu-rich
                     (acidic) (hirudin-like)"
                     /note="propagated from UniProtKB/Swiss-Prot (P05546.3)"
     Site            order(75..80,82,85..86,89,305..309,327,361..362,388,
                     458..466,468,473)
                     /site_type="other"
                     /note="thrombin binding site [polypeptide binding]"
                     /db_xref="CDD:381004"
     Site            79
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000269|PubMed:12169660; propagated from
                     UniProtKB/Swiss-Prot (P05546.3)"
     Site            92
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000269|PubMed:12169660; propagated from
                     UniProtKB/Swiss-Prot (P05546.3)"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12169660,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (P05546.3)"
     Region          192..212
                     /region_name="Glycosaminoglycan-binding site"
                     /note="propagated from UniProtKB/Swiss-Prot (P05546.3)"
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12169660; propagated from
                     UniProtKB/Swiss-Prot (P05546.3)"
     Site            449..474
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381004"
     Site            463..464
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P05546.3)"
     CDS             1..499
                     /gene="SERPIND1"
                     /gene_synonym="D22S673; HC2; HCF2; HCII; HLS2; LS2;
                     THPH10"
                     /coded_by="NM_000185.4:50..1549"
                     /db_xref="CCDS:CCDS13783.1"
                     /db_xref="GeneID:3053"
                     /db_xref="HGNC:HGNC:4838"
                     /db_xref="MIM:142360"
ORIGIN      
        1 mkhslnalli fliitsawgg skgpldqlek ggetaqsadp qweqlnnknl smpllpadfh
       61 kentvtndwi pegeedddyl dlekifsedd dyidivdsls vsptdsdvsa gnilqlfhgk
      121 sriqrlniln akfafnlyrv lkdqvntfdn ifiapvgist amgmislglk getheqvhsi
      181 lhfkdfvnas skyeittihn lfrklthrlf rrnfgytlrs vndlyiqkqf pilldfktkv
      241 reyyfaeaqi adfsdpafis ktnnhimklt kglikdalen idpatqmmil nciyfkgswv
      301 nkfpvemthn hnfrlnerev vkvsmmqtkg nflaandqel dcdilqleyv ggismlivvp
      361 hkmsgmktle aqltprvver wqksmtnrtr evllpkfkle knynlveslk lmgirmlfdk
      421 ngnmagisdq riaidlfkhq gtitvneegt qattvttvgf mplstqvrft vdrpflfliy
      481 ehrtscllfm grvanpsrs
//
LOCUS       NP_001349979             661 aa            linear   PRI 27-APR-2025
DEFINITION  junctophilin-1 [Homo sapiens].
ACCESSION   NP_001349979 XP_005251331
VERSION     NP_001349979.1
DBSOURCE    REFSEQ: accession NM_001363050.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Tammineni,E.R., Figueroa,L., Manno,C., Varma,D., Kraeva,N.,
            Ibarra,C.A., Klip,A., Riazi,S. and Rios,E.
  TITLE     Muscle calcium stress cleaves junctophilin1, unleashing a gene
            regulatory program predicted to correct glucose dysregulation
  JOURNAL   Elife 12, e78874 (2023)
   PUBMED   36724092
  REMARK    GeneRIF: Muscle calcium stress cleaves junctophilin1, unleashing a
            gene regulatory program predicted to correct glucose dysregulation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Perni,S. and Beam,K.
  TITLE     Junctophilins 1, 2, and 3 all support voltage-induced Ca2+ release
            despite considerable divergence
  JOURNAL   J Gen Physiol 154 (9) (2022)
   PUBMED   35089322
  REMARK    GeneRIF: Junctophilins 1, 2, and 3 all support voltage-induced Ca2+
            release despite considerable divergence.
REFERENCE   3  (residues 1 to 661)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 661)
  AUTHORS   Kanwal,S. and Perveen,S.
  TITLE     Association of SNP in JPH1 gene with severity of disease in Charcot
            Marie Tooth 2K patients
  JOURNAL   J Pak Med Assoc 69 (2), 241-243 (2019)
   PUBMED   30804591
  REMARK    GeneRIF: Charcot Marie Tooth 2K patients with early and late onset
            were analyzed for association of rs139723190 SNP in JPH1 gene
            responsible for CMT type severe and mild phenotypes.
REFERENCE   5  (residues 1 to 661)
  AUTHORS   Pla-Martin,D., Calpena,E., Lupo,V., Marquez,C., Rivas,E.,
            Sivera,R., Sevilla,T., Palau,F. and Espinos,C.
  TITLE     Junctophilin-1 is a modifier gene of GDAP1-related
            Charcot-Marie-Tooth disease
  JOURNAL   Hum Mol Genet 24 (1), 213-229 (2015)
   PUBMED   25168384
  REMARK    GeneRIF: Results show that JPH1 and GDAP1 share a common pathway
            and depend on each other; therefore, JPH1 can contribute to the
            phenotypical consequences of GDAP1 mutations.
REFERENCE   6  (residues 1 to 661)
  AUTHORS   Nusbaum,C., Mikkelsen,T.S., Zody,M.C., Asakawa,S., Taudien,S.,
            Garber,M., Kodira,C.D., Schueler,M.G., Shimizu,A., Whittaker,C.A.,
            Chang,J.L., Cuomo,C.A., Dewar,K., FitzGerald,M.G., Yang,X.,
            Allen,N.R., Anderson,S., Asakawa,T., Blechschmidt,K., Bloom,T.,
            Borowsky,M.L., Butler,J., Cook,A., Corum,B., DeArellano,K.,
            DeCaprio,D., Dooley,K.T., Dorris,L. 3rd, Engels,R., Glockner,G.,
            Hafez,N., Hagopian,D.S., Hall,J.L., Ishikawa,S.K., Jaffe,D.B.,
            Kamat,A., Kudoh,J., Lehmann,R., Lokitsang,T., Macdonald,P.,
            Major,J.E., Matthews,C.D., Mauceli,E., Menzel,U., Mihalev,A.H.,
            Minoshima,S., Murayama,Y., Naylor,J.W., Nicol,R., Nguyen,C.,
            O'Leary,S.B., O'Neill,K., Parker,S.C., Polley,A., Raymond,C.K.,
            Reichwald,K., Rodriguez,J., Sasaki,T., Schilhabel,M., Siddiqui,R.,
            Smith,C.L., Sneddon,T.P., Talamas,J.A., Tenzin,P., Topham,K.,
            Venkataraman,V., Wen,G., Yamazaki,S., Young,S.K., Zeng,Q.,
            Zimmer,A.R., Rosenthal,A., Birren,B.W., Platzer,M., Shimizu,N. and
            Lander,E.S.
  TITLE     DNA sequence and analysis of human chromosome 8
  JOURNAL   Nature 439 (7074), 331-335 (2006)
   PUBMED   16421571
REFERENCE   7  (residues 1 to 661)
  AUTHORS   Takeshima,H.
  TITLE     [Ryanodine receptor and junctional membrane structure]
  JOURNAL   Nihon Yakurigaku Zasshi 121 (4), 203-210 (2003)
   PUBMED   12777839
  REMARK    Review article
REFERENCE   8  (residues 1 to 661)
  AUTHORS   Komazaki,S., Ito,K., Takeshima,H. and Nakamura,H.
  TITLE     Deficiency of triad formation in developing skeletal muscle cells
            lacking junctophilin type 1
  JOURNAL   FEBS Lett 524 (1-3), 225-229 (2002)
   PUBMED   12135771
REFERENCE   9  (residues 1 to 661)
  AUTHORS   Nishi,M., Mizushima,A., Nakagawara,Ki. and Takeshima,H.
  TITLE     Characterization of human junctophilin subtype genes
  JOURNAL   Biochem Biophys Res Commun 273 (3), 920-927 (2000)
   PUBMED   10891348
REFERENCE   10 (residues 1 to 661)
  AUTHORS   Takeshima,H., Komazaki,S., Nishi,M., Iino,M. and Kangawa,K.
  TITLE     Junctophilins: a novel family of junctional membrane complex
            proteins
  JOURNAL   Mol Cell 6 (1), 11-22 (2000)
   PUBMED   10949023
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC140875.1, BX537756.1,
            BC049372.1, AC087792.7 and BU687964.1.
            
            On Jun 20, 2018 this sequence version replaced XP_005251331.1.
            
            Summary: Junctional complexes between the plasma membrane and
            endoplasmic/sarcoplasmic reticulum are a common feature of all
            excitable cell types and mediate cross talk between cell surface
            and intracellular ion channels. The protein encoded by this gene is
            a component of junctional complexes and is composed of a C-terminal
            hydrophobic segment spanning the endoplasmic/sarcoplasmic reticulum
            membrane and a remaining cytoplasmic domain that shows specific
            affinity for the plasma membrane. This gene is a member of the
            junctophilin gene family. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.101502.1,
                                           SRR1660809.144892.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..661
                     /product="junctophilin-1"
                     /note="junctophilin type 1"
                     /calculated_mol_wt=71555
     Region          <3..333
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          14..36
                     /region_name="MORN 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Region          38..59
                     /region_name="MORN 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Region          60..82
                     /region_name="MORN 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Region          106..128
                     /region_name="MORN 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Region          129..151
                     /region_name="MORN 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Region          228..247
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Region          281..303
                     /region_name="MORN 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Region          304..326
                     /region_name="MORN 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Region          <405..571
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          433..631
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9HDC5.2)"
     Site            640..660
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HDC5.2)"
     CDS             1..661
                     /gene="JPH1"
                     /gene_synonym="CMT2K; CMYO25; JP-1; JP1"
                     /coded_by="NM_001363050.1:75..2060"
                     /db_xref="CCDS:CCDS6217.1"
                     /db_xref="GeneID:56704"
                     /db_xref="HGNC:HGNC:14201"
                     /db_xref="MIM:605266"
ORIGIN      
        1 mtggrfdfdd ggtycggwee gkahghgict gpkgqgeysg swshgfevvg gytwpsgnty
       61 qgywaqgkrh glgvetkgkw myrgewshgf kgrygvrqsl ctparyegtw snglqdgygv
      121 etygdggtyq gqwaggmrhg ygvrqsvpyg matvirsplr tslaslrseq sngsvlhdaa
      181 aaadspagtr ggfvlnfhad aelagkkkgg lfrrgsllgs mklrksesks sisskrssvr
      241 sdaamsriss sdanstisfg dvdcdfcpve dhvdatttet ymgewkndkr ngfgvsersn
      301 gmkyegewan nkrhgygctv fpdgskeegk yknnilvrgi rkqlipirht ktrekvdrai
      361 egaqraaama rtkveiansr taharakada adqaalaarq ecdiaravar elspdfyqpg
      421 pdyvkqrfqe gvdakenpee kvpekpptpk esphfyrkgt tpprspeasp khshspassp
      481 kplkkqnpss garlnqdkrs vadeqvtaiv nkplmskapt keagavvpqs kysgrhhipn
      541 psngelhsqy hgyyvklnap qhppvdvedg dgssqsssal vhkpsankws psksvtkpva
      601 keskaepkak kselaipknp asndscpale keansgpnsi mivlvmllni glailfvhfl
      661 t
//
LOCUS       NP_079276                520 aa            linear   PRI 27-APR-2025
DEFINITION  DDB1- and CUL4-associated factor 17 isoform 1 [Homo sapiens].
ACCESSION   NP_079276
VERSION     NP_079276.2
DBSOURCE    REFSEQ: accession NM_025000.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Fozia,F., Shah,K., Nazli,R., Khan,S.A., Ahmad,I., Mohammad,N.,
            Khan,S. and Alotaibi,A.
  TITLE     Novel splicing-site mutation in DCAF17 gene causing
            Woodhouse-Sakati syndrome in a large consanguineous family
  JOURNAL   J Clin Lab Anal 36 (1), e24127 (2022)
   PUBMED   34877714
  REMARK    GeneRIF: Novel splicing-site mutation in DCAF17 gene causing
            Woodhouse-Sakati syndrome in a large consanguineous family.
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Alharbi,M.S.
  TITLE     Woodhouse-Sakati syndrome (WSS): A case report of 3 Saudi sisters
            with urogenital anomalies
  JOURNAL   Saudi Med J 42 (11), 1237-1242 (2021)
   PUBMED   34732557
  REMARK    GeneRIF: Woodhouse-Sakati syndrome (WSS): A case report of 3 Saudi
            sisters with urogenital anomalies.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Shah,K., Jan,A., Ahmad,F., Basit,S., Ramzan,K. and Ahmad,W.
  TITLE     Woodhouse-Sakati syndrome in a family is associated with a
            homozygous start loss mutation in the DCAF17 gene
  JOURNAL   Clin Exp Dermatol 45 (2), 159-164 (2020)
   PUBMED   31323129
  REMARK    GeneRIF: Analysis of the exome data revealed a start loss sequence
            variant (c.1A>G, p.M1?) in DCAF17 in a Pakastani family with
            Woodhouse-Sakati syndrome. This variant is predicted to abolish
            translation of the DCAF17 polypeptide. To our knowledge, this is
            the first start loss variant identified in the DCAF17.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Almeqdadi,M., Kemppainen,J.L., Pichurin,P.N. and Gavrilova,R.H.
  TITLE     Phenotypic Variability of c.436delC DCAF17 Gene Mutation in
            Woodhouse-Sakati Syndrome
  JOURNAL   Am J Case Rep 19, 347-353 (2018)
   PUBMED   29574468
  REMARK    GeneRIF: The phenotypic variability of Woodhouse-Sakati syndrome
            due to c.436delC founder DCAF17 mutation may have a wider range
            than previously recognized.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Alazami,A.M., Al-Saif,A., Al-Semari,A., Bohlega,S., Zlitni,S.,
            Alzahrani,F., Bavi,P., Kaya,N., Colak,D., Khalak,H., Baltus,A.,
            Peterlin,B., Danda,S., Bhatia,K.P., Schneider,S.A., Sakati,N.,
            Walsh,C.A., Al-Mohanna,F., Meyer,B. and Alkuraya,F.S.
  TITLE     Mutations in C2orf37, encoding a nucleolar protein, cause
            hypogonadism, alopecia, diabetes mellitus, mental retardation, and
            extrapyramidal syndrome
  JOURNAL   Am J Hum Genet 83 (6), 684-691 (2008)
   PUBMED   19026396
  REMARK    GeneRIF: Mutations in C2orf37, encoding a nucleolar protein, cause
            hypogonadism, alopecia, diabetes mellitus, mental retardation, and
            extrapyramidal syndrome.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Lee,J. and Zhou,P.
  TITLE     DCAFs, the missing link of the CUL4-DDB1 ubiquitin ligase
  JOURNAL   Mol Cell 26 (6), 775-780 (2007)
   PUBMED   17588513
  REMARK    Review article
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Bohlega,S.A. and Abusrair,A.
  TITLE     Woodhouse-Sakati Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27489925
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Gregory,A., A Kurian,M., Wilson,J. and Hayflick,S.
  TITLE     Neurodegeneration with Brain Iron Accumulation Disorders Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23447832
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007969.3, AK307877.1,
            BC140843.1 and BM676973.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 24, 2006 this sequence version replaced NP_079276.1.
            
            Summary: This gene encodes a nuclear transmembrane protein that
            associates with cullin 4A/damaged DNA binding protein 1 ubiquitin
            ligase complex. Mutations in this gene are associated with
            Woodhouse-Sakati syndrome. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR933646.1, SRR1660809.254534.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375255.8/ ENSP00000364404.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..520
                     /product="DDB1- and CUL4-associated factor 17 isoform 1"
                     /calculated_mol_wt=58647
     Region          31..505
                     /region_name="DCAF17"
                     /note="DDB1- and CUL4-associated factor 17; pfam15802"
                     /db_xref="CDD:464881"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9S7.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9S7.1)"
     CDS             1..520
                     /gene="DCAF17"
                     /gene_synonym="C20orf37; C2orf37"
                     /coded_by="NM_025000.4:353..1915"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2243.2"
                     /db_xref="GeneID:80067"
                     /db_xref="HGNC:HGNC:25784"
                     /db_xref="MIM:612515"
ORIGIN      
        1 mgptrkpnvc srlsrralgc fsrdagvvqr tnlgilralv cqestkfknv wtthsrspia
       61 yergriyfdn yrrcvssvas eprklyempk csksekieda llwecpvgdi lpnssdykss
      121 lialtahnwl lrisattgki lekiylapyc kfrylswdtp qeviavksaq nrgsavarqa
      181 giqqhvllyl avfrvlpfsl vgileinkki fgnvtdatls hgilivmyss glvrlysfqt
      241 iaeqfmqqkl dlgcacrwgg ttgtvgeapf gipcnikitd mppllfevss lenafqiggh
      301 pwhyivtpnk kkqkgvfhic alkdnslakn giqemdccsl esdwiyfhpd asgriihvgp
      361 nqvkvlklte iennssqhqi sedfvilanr enhknenvlt vtasgrvvkk sfnlldddpe
      421 qetfkivdye deldllsvva vtqidaegka hldfhcneyg tllksiplve swdvtyshev
      481 yfdrdlvlhi eqkpnrvfsc yvyqmicdtg eeeetinrsc
//
LOCUS       NP_001290355             485 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 639 [Homo sapiens].
ACCESSION   NP_001290355
VERSION     NP_001290355.1
DBSOURCE    REFSEQ: accession NM_001303426.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Bruce,J.W., Reddington,R., Mathieu,E., Bracken,M., Young,J.A. and
            Ahlquist,P.
  TITLE     ZASC1 stimulates HIV-1 transcription elongation by recruiting
            P-TEFb and TAT to the LTR promoter
  JOURNAL   PLoS Pathog 9 (10), e1003712 (2013)
   PUBMED   24204263
  REMARK    GeneRIF: ZASC1 as novel regulator of HIV-1 gene expression that
            functions through the DNA-dependent, RNA-independent recruitment of
            TAT/P-TEFb to the HIV-1 promoter.
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Chiang,W.F., Hung,P.S., Liu,S.Y., Yuan,T.C., Chang,K.W., Chen,Y.P.,
            Liu,Y.C. and Lin,S.C.
  TITLE     Increase of ZASC1 gene copy number in recurrent oral carcinoma
  JOURNAL   Oral Dis 17 (1), 53-59 (2011)
   PUBMED   20646234
  REMARK    GeneRIF: ZASC1 copy number that increased from primary to recurrent
            tumor suggested the importance of ZASC1 in tumor progression. The
            increase of ZASC1 gene copy number in recurrent tumors was
            associated with the consumption of betel quid in patients.
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Bruce,J.W., Hierl,M., Young,J.A. and Ahlquist,P.
  TITLE     Cellular transcription factor ZASC1 regulates murine leukemia virus
            transcription
  JOURNAL   J Virol 84 (15), 7473-7483 (2010)
   PUBMED   20484494
REFERENCE   7  (residues 1 to 485)
  AUTHORS   Bogaerts,S., Vanlandschoot,A., van Hengel,J. and van Roy,F.
  TITLE     Nuclear translocation of alphaN-catenin by the novel zinc finger
            transcriptional repressor ZASC1
  JOURNAL   Exp Cell Res 311 (1), 1-13 (2005)
   PUBMED   16182284
REFERENCE   8  (residues 1 to 485)
  AUTHORS   Imoto,I., Yuki,Y., Sonoda,I., Ito,T., Shimada,Y., Imamura,M. and
            Inazawa,J.
  TITLE     Identification of ZASC1 encoding a Kruppel-like zinc finger protein
            as a novel target for 3q26 amplification in esophageal squamous
            cell carcinomas
  JOURNAL   Cancer Res 63 (18), 5691-5696 (2003)
   PUBMED   14522885
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB457196.1, BC026181.1,
            AB097862.1, BP260931.1 and AC007823.38.
            
            Summary: This gene encodes a member of the Kruppel-like zinc finger
            family of proteins. Amplification and overexpression of this gene
            have been observed in esophageal squamous cell carcinoma. The
            encoded protein has been shown to bind DNA in a sequence-specific
            manner and may regulate HIV-1 gene expression. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Dec
            2014].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026181.1, ERR279857.594.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000496856.6/ ENSP00000417740.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.33"
     Protein         1..485
                     /product="zinc finger protein 639"
                     /note="zinc finger amplified in esophageal squamous cell
                     carcinomas 1"
                     /calculated_mol_wt=55924
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UID6.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UID6.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UID6.1)"
     Region          235..255
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(240,242,244,246..247,250..251,254,268,272,273..274,
                     277..278,282,296,298,300,302..303,306..307)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          262..283
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          291..307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          371..455
                     /region_name="Interaction with CTNNA2.
                     /evidence=ECO:0000269|PubMed:16182284"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UID6.1)"
     Region          376..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          405..425
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(410,412,414,416..417,420..421,424,438,440,444..445,
                     448..449,453,467,469,471,473..474,477..478,481)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          433..454
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          462..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..485
                     /gene="ZNF639"
                     /gene_synonym="ANC-2H01; ANC_2H01; ZASC1"
                     /coded_by="NM_001303426.2:344..1801"
                     /db_xref="CCDS:CCDS3227.1"
                     /db_xref="GeneID:51193"
                     /db_xref="HGNC:HGNC:30950"
                     /db_xref="MIM:619214"
ORIGIN      
        1 mneypkkrkr ktlhpsrysd ssgisriadg fngifsdhcy svcsmrqpdl kyfdnkddds
       61 dtetsndlpk fadgikarnr nqnylvpspv lrildhtafs teksadivic deecdspesv
      121 nqqtqeespi evhtaedvpi avevhaised ydietennss eslqdqtdee ppaklckild
      181 ksqalnvtaq qkwpllrans sglykcelce fnskyfsdlk qhmilkhkrt dsnvcrvcke
      241 sfstnmllie haklheedpy ickycdyktv ifenlsqhia dthfsdhlyw ceqcdvqfss
      301 sselylhfqe hscdeqylcq fcehetndpe dlhshvvneh acklielsdk ynngehgqys
      361 llskitfdkc knffvcqvcg frsrlhtnvn rhvaiehtki fphvcddcgk gfssmleyck
      421 hlnshlsegi ylcqyceyst gqiedlkihl dfkhsadlph kcsdclmrfg nerelishlp
      481 vhett
//
LOCUS       NP_001258803             384 aa            linear   PRI 27-APR-2025
DEFINITION  protein AAR2 homolog [Homo sapiens].
ACCESSION   NP_001258803
VERSION     NP_001258803.1
DBSOURCE    REFSEQ: accession NM_001271874.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Preussner,M., Santos,K.F., Alles,J., Heroven,C., Heyd,F., Wahl,M.C.
            and Weber,G.
  TITLE     Structural and functional investigation of the human snRNP assembly
            factor AAR2 in complex with the RNase H-like domain of PRPF8
  JOURNAL   Acta Crystallogr D Struct Biol 78 (Pt 11), 1373-1383 (2022)
   PUBMED   36322420
  REMARK    GeneRIF: Structural and functional investigation of the human snRNP
            assembly factor AAR2 in complex with the RNase H-like domain of
            PRPF8.
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Fan,L., Gao,B., Xu,Y., Flynn,N., Le,B., You,C., Li,S., Achkar,N.,
            Manavella,P.A., Yang,Z. and Chen,X.
  TITLE     Arabidopsis AAR2, a conserved splicing factor in eukaryotes, acts
            in microRNA biogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (41), e2208415119 (2022)
   PUBMED   36191209
  REMARK    GeneRIF: Arabidopsis AAR2, a conserved splicing factor in
            eukaryotes, acts in microRNA biogenesis.
            Erratum:[Proc Natl Acad Sci U S A. 2022 Dec 27;119(52):e2219264119.
            doi: 10.1073/pnas.2219264119. PMID: 36534814]
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Klimesova,K., Vojackova,J., Radivojevic,N., Vandermoere,F.,
            Bertrand,E., Verheggen,C. and Stanek,D.
  TITLE     TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation
  JOURNAL   Nat Commun 12 (1), 3646 (2021)
   PUBMED   34131137
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Santos,K., Preussner,M., Heroven,A.C. and Weber,G.
  TITLE     Crystallization and biochemical characterization of the human
            spliceosomal Aar2-Prp8(RNaseH) complex
  JOURNAL   Acta Crystallogr F Struct Biol Commun 71 (Pt 11), 1421-1428 (2015)
   PUBMED   26527271
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Gottschalk,A., Kastner,B., Luhrmann,R. and Fabrizio,P.
  TITLE     The yeast U5 snRNP coisolated with the U1 snRNP has an unexpected
            protein composition and includes the splicing factor Aar2p
  JOURNAL   RNA 7 (11), 1554-1565 (2001)
   PUBMED   11720285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY019727.1 and BC001751.1.
            
            Summary: This gene encodes the homolog of the yeast A1-alpha2
            repressin protein that is involved in mRNA splicing. Alternately
            spliced transcript variants have been found for this gene.
            [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.369361.1,
                                           SRR1660805.154005.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000320849.9/ ENSP00000313674.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.23"
     Protein         1..384
                     /product="protein AAR2 homolog"
                     /note="AAR2 splicing factor homolog"
                     /calculated_mol_wt=43341
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9Y312.2)"
     Region          17..363
                     /region_name="AAR2"
                     /note="AAR2 protein; pfam05282"
                     /db_xref="CDD:461609"
     CDS             1..384
                     /gene="AAR2"
                     /gene_synonym="C20orf4; CGI-23"
                     /coded_by="NM_001271874.2:75..1229"
                     /db_xref="CCDS:CCDS13273.1"
                     /db_xref="GeneID:25980"
                     /db_xref="HGNC:HGNC:15886"
                     /db_xref="MIM:617365"
ORIGIN      
        1 maavqmdpel akrlffegat vvilnmpkgt efgidynswe vgpkfrgvkm ippgihflhy
       61 ssvdkanpke vgprmgffls lhqrgltvlr wstlreevdl spapesevea mranlqeldq
      121 flgpypyatl kkwisltnfi seatveklqp enrqicafsd vlpvlsmkht kdrvgqnlpr
      181 cgiecksyqe glarlpemkp ragteirfse lptqmfpega tpaeitkhsm dlsyaletvl
      241 nkqfpsspqd vlgelqfafv cfllgnvyea fehwkrllnl lcrseaammk hhtlyinlis
      301 ilyhqlgeip adffvdivsq dnfltstlqv ffssacsiav datlrkkaek fqahltkkfr
      361 wdfaaepedc apvvvelpeg iemg
//
LOCUS       NP_001347598             515 aa            linear   ROD 27-APR-2025
DEFINITION  fatty acyl-CoA reductase 1 isoform 1 [Mus musculus].
ACCESSION   NP_001347598 XP_006508190
VERSION     NP_001347598.1
DBSOURCE    REFSEQ: accession NM_001360669.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Pan,B., Yuan,S., Mayernik,L., Yap,Y.T., Moin,K., Chung,C.S.,
            Maddipati,K., Krawetz,S.A., Zhang,Z., Hess,R.A. and Chen,X.
  TITLE     Disrupted intercellular bridges and spermatogenesis in fatty
            acyl-CoA reductase 1 knockout mice: A new model of ether lipid
            deficiency
  JOURNAL   FASEB J 37 (5), e22908 (2023)
   PUBMED   37039784
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Tang,T., Li,L., Tang,J., Li,Y., Lin,W.Y., Martin,F., Grant,D.,
            Solloway,M., Parker,L., Ye,W., Forrest,W., Ghilardi,N., Oravecz,T.,
            Platt,K.A., Rice,D.S., Hansen,G.M., Abuin,A., Eberhart,D.E.,
            Godowski,P., Holt,K.H., Peterson,A., Zambrowicz,B.P. and de
            Sauvage,F.J.
  TITLE     A mouse knockout library for secreted and transmembrane proteins
  JOURNAL   Nat Biotechnol 28 (7), 749-755 (2010)
   PUBMED   20562862
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Cheng,J.B. and Russell,D.W.
  TITLE     Mammalian wax biosynthesis. II. Expression cloning of wax synthase
            cDNAs encoding a member of the acyltransferase enzyme family
  JOURNAL   J Biol Chem 279 (36), 37798-37807 (2004)
   PUBMED   15220349
  REMARK    GeneRIF: wax monoester synthesis in mammals involves a two step
            biosynthetic pathway catalyzed by fatty acyl-CoA reductase and wax
            synthase enzymes
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Cheng,J.B. and Russell,D.W.
  TITLE     Mammalian wax biosynthesis. I. Identification of two fatty
            acyl-Coenzyme A reductases with different substrate specificities
            and tissue distributions
  JOURNAL   J Biol Chem 279 (36), 37789-37797 (2004)
   PUBMED   15220348
  REMARK    GeneRIF: fatty alcohol synthesis in mammals is accomplished by two
            fatty acyl-CoA reductase isozymes that are expressed at high levels
            in tissues known to synthesize wax monoesters and ether lipids
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC156987.7 and AC102841.7.
            
            On Feb 9, 2018 this sequence version replaced XP_006508190.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1, 3, and 4 all encode the same isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660811.170626.1,
                                           SRR1660815.155044.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 59.21 cM"
     Protein         1..515
                     /product="fatty acyl-CoA reductase 1 isoform 1"
                     /EC_number="1.2.1.84"
                     /note="male sterility domain containing 2"
                     /calculated_mol_wt=59304
     Region          11..330
                     /region_name="FAR-N_SDR_e"
                     /note="fatty acyl CoA reductases (FARs), extended (e)
                     SDRs; cd05236"
                     /db_xref="CDD:187547"
     Site            order(17,19..22,44..46,111..113,130,151..153,204,208,
                     229..232)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187547"
     Site            order(131,153,204,208)
                     /site_type="active"
                     /db_xref="CDD:187547"
     Site            order(153,204,231,243,259,265)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187547"
     Region          357..447
                     /region_name="Sterile"
                     /note="Male sterility protein; pfam03015"
                     /db_xref="CDD:460779"
     Region          451..507
                     /region_name="Necessary and sufficient for PEX19-mediated
                     localization into peroxisome membrane.
                     /evidence=ECO:0000250|UniProtKB:Q8WVX9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q922J9.1)"
     Site            466..483
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q922J9.1)"
     CDS             1..515
                     /gene="Far1"
                     /gene_synonym="2600011M19Rik; 2900034E22Rik;
                     3732409C05Rik; Mlstd2"
                     /coded_by="NM_001360669.1:157..1704"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS40093.1"
                     /db_xref="GeneID:67420"
                     /db_xref="MGI:MGI:1914670"
ORIGIN      
        1 mvsipeyyeg knilltgatg flgkvllekl lrscprvnsv yvlvrqkagq tpqerveeil
       61 ssklfdrlrd enpdfrekii ainseltqpk lalseedkei iidstnvifh caatvrfnen
      121 lrdavqlnvi atrqlillaq qmknlevfmh vstayaycnr khidevvypp pvdpkklids
      181 lewmddglvn ditpkligdr pntyiytkal aeyvvqqega klnvaivrps ivgaswkepf
      241 pgwidnfngp sglfiaagkg ilrtmrasnn aladlvpvdv vvntslaaaw ysgvnrprni
      301 mvyncttgst npfhwgevey hvistfkrnp leqafrrpnv nltsnhllyh ywiavshkap
      361 aflydiylrm tgrsprmmkt itrlhkamvf leyftsnswv wntdnvnmlm nqlnpedkkt
      421 fnidvrqlhw aeyienycmg tkkyvlneem sglpaarkhl nklrnirygf ntilviliwr
      481 ifiarsqmar niwyfvvslc ykflsyfras stmry
//
LOCUS       NP_060291                303 aa            linear   PRI 27-APR-2025
DEFINITION  rhomboid-related protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_060291
VERSION     NP_060291.2
DBSOURCE    REFSEQ: accession NM_017821.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Che,Z., Jin,W., Wu,Y., Li,H. and Liang,P.
  TITLE     Rhomboid-like 2 correlated with TME infiltration inhibits
            cuproptosis-related genes and drives malignant phenotype in clear
            cell renal cell carcinoma
  JOURNAL   Sci Rep 14 (1), 27053 (2024)
   PUBMED   39511359
  REMARK    GeneRIF: Rhomboid-like 2 correlated with TME infiltration inhibits
            cuproptosis-related genes and drives malignant phenotype in clear
            cell renal cell carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Koch,L., Kespohl,B., Agthe,M., Schumertl,T., Dusterhoft,S.,
            Lemberg,M.K., Lokau,J. and Garbers,C.
  TITLE     Interleukin-11 (IL-11) receptor cleavage by the rhomboid protease
            RHBDL2 induces IL-11 trans-signaling
  JOURNAL   FASEB J 35 (3), e21380 (2021)
   PUBMED   33566379
  REMARK    GeneRIF: Interleukin-11 (IL-11) receptor cleavage by the rhomboid
            protease RHBDL2 induces IL-11 trans-signaling.
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Freeman,M.
  TITLE     The rhomboid-like superfamily: molecular mechanisms and biological
            roles
  JOURNAL   Annu Rev Cell Dev Biol 30, 235-254 (2014)
   PUBMED   25062361
  REMARK    Review article
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Bergbold,N. and Lemberg,M.K.
  TITLE     Emerging role of rhomboid family proteins in mammalian biology and
            disease
  JOURNAL   Biochim Biophys Acta 1828 (12), 2840-2848 (2013)
   PUBMED   23562403
  REMARK    Review article
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Lemberg,M.K.
  TITLE     Sampling the membrane: function of rhomboid-family proteins
  JOURNAL   Trends Cell Biol 23 (5), 210-217 (2013)
   PUBMED   23369641
  REMARK    Review article
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Pascall,J.C. and Brown,K.D.
  TITLE     Intramembrane cleavage of ephrinB3 by the human rhomboid family
            protease, RHBDL2
  JOURNAL   Biochem Biophys Res Commun 317 (1), 244-252 (2004)
   PUBMED   15047175
  REMARK    GeneRIF: The encoded protein is thought to release soluble growth
            factors by proteolytic cleavage of certain membrane-bound
            substrates, including ephrin B2 and ephrin B3.
REFERENCE   9  (residues 1 to 303)
  AUTHORS   Urban,S. and Freeman,M.
  TITLE     Substrate specificity of rhomboid intramembrane proteases is
            governed by helix-breaking residues in the substrate transmembrane
            domain
  JOURNAL   Mol Cell 11 (6), 1425-1434 (2003)
   PUBMED   12820957
  REMARK    GeneRIF: Substrate specificity of RHBDL2 intramembrane protease is
            governed by helix-breaking residues in the transmembrane domain.
REFERENCE   10 (residues 1 to 303)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB036310.1, AK294115.1 and
            AL139260.19.
            
            On Oct 15, 2004 this sequence version replaced NP_060291.1.
            
            Summary: The protein encoded by this gene is a member of the
            rhomboid family of integral membrane proteins. This family contains
            proteins that are related to Drosophila rhomboid protein. Members
            of this family are found in both prokaryotes and eukaryotes and are
            thought to function as intramembrane serine proteases. The encoded
            protein is thought to release soluble growth factors by proteolytic
            cleavage of certain membrane-bound substrates, including ephrin B2
            and ephrin B3. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Feb 2015].
            
            Transcript Variant: This variant (2) uses an alternate first exon
            in place of that of variant 1, which results in variant 2 using a
            downstream translation start site compared to variant 1. The
            resulting isoform (2) is shorter at the N-terminus compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.212005.1,
                                           SRR1660803.137482.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372990.6/ ENSP00000362081.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..303
                     /product="rhomboid-related protein 2 isoform 2"
                     /EC_number="3.4.21.105"
                     /note="rhomboid (veinlet, Drosophila)-like 2; rhomboid
                     protease 2; rhomboid-related protein 2; rhomboid-like
                     protein 2; rhomboid, veinlet-like 2"
                     /calculated_mol_wt=33890
     Region          20..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX52.2)"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX52.2)"
     Region          114..266
                     /region_name="Rhomboid"
                     /note="Rhomboid family; pfam01694"
                     /db_xref="CDD:426384"
     Site            128..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX52.2)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX52.2)"
     Site            183..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX52.2)"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX52.2)"
     Site            245..265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX52.2)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX52.2)"
     CDS             1..303
                     /gene="RHBDL2"
                     /gene_synonym="RRP2"
                     /coded_by="NM_017821.5:275..1186"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS30680.1"
                     /db_xref="GeneID:54933"
                     /db_xref="HGNC:HGNC:16083"
                     /db_xref="MIM:608962"
ORIGIN      
        1 maavhdleme smnlnmgrem keeleeeekm redgggkdra kskkvhrivs kwmlpeksrg
       61 tylerancfp ppvfiisisl aelavfiyya vwkpqkqwit ldtgilespf iyspekreea
      121 wrfisymlvh agvqhilgnl cmqlvlgipl emvhkglrvg lvylagviag slassifdpl
      181 rylvgasggv yalmggyfmn vlvnfqemip afgifrllii iliivldmgf alyrrffvpe
      241 dgspvsfaah iaggfagmsi gytvfscfdk allkdprfwi aiaaylacvl favffnifls
      301 pan
//
LOCUS       NP_071764                667 aa            linear   PRI 27-APR-2025
DEFINITION  receptor for retinol uptake STRA6 isoform a [Homo sapiens].
ACCESSION   NP_071764
VERSION     NP_071764.3
DBSOURCE    REFSEQ: accession NM_022369.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Zhou,C., Haneke,T., Rohner,E., Sohlmer,J., Kameneva,P., Artemov,A.,
            Adameyko,I. and Sahara,M.
  TITLE     STRA6 is essential for induction of vascular smooth muscle lineages
            in human embryonic cardiac outflow tract development
  JOURNAL   Cardiovasc Res 119 (5), 1202-1217 (2023)
   PUBMED   36635482
  REMARK    GeneRIF: STRA6 is essential for induction of vascular smooth muscle
            lineages in human embryonic cardiac outflow tract development.
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Yang,F., Xu,P., Yao,S., Li,M., Bian,Z. and Huang,Z.
  TITLE     Up-regulation of STRA6 predicts poor prognosis and contributes to
            oxaliplatin resistance in colorectal cancer
  JOURNAL   Pathol Res Pract 243, 154352 (2023)
   PUBMED   36758416
  REMARK    GeneRIF: Up-regulation of STRA6 predicts poor prognosis and
            contributes to oxaliplatin resistance in colorectal cancer.
REFERENCE   3  (residues 1 to 667)
  AUTHORS   He,W., Sun,Y., Ge,J., Wang,X., Lin,B., Yu,S., Li,Y., Hong,S. and
            Xiao,H.
  TITLE     STRA6 regulates tumor immune microenvironment and is a prognostic
            marker in BRAF-mutant papillary thyroid carcinoma
  JOURNAL   Front Endocrinol (Lausanne) 14, 1076640 (2023)
   PUBMED   36843593
  REMARK    GeneRIF: STRA6 regulates tumor immune microenvironment and is a
            prognostic marker in BRAF-mutant papillary thyroid carcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Nakamura,S., Kanda,M., Shimizu,D., Sawaki,K., Tanaka,C.,
            Hattori,N., Hayashi,M., Yamada,S., Nakayama,G., Omae,K., Koike,M.
            and Kodera,Y.
  TITLE     STRA6 Expression Serves as a Prognostic Biomarker of Gastric Cancer
  JOURNAL   Cancer Genomics Proteomics 17 (5), 509-516 (2020)
   PUBMED   32859629
  REMARK    GeneRIF: STRA6 Expression Serves as a Prognostic Biomarker of
            Gastric Cancer.
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Szeto,W., Jiang,W., Tice,D.A., Rubinfeld,B., Hollingshead,P.G.,
            Fong,S.E., Dugger,D.L., Pham,T., Yansura,D.G., Wong,T.A.,
            Grimaldi,J.C., Corpuz,R.T., Singh,J.S., Frantz,G.D., Devaux,B.,
            Crowley,C.W., Schwall,R.H., Eberhard,D.A., Rastelli,L., Polakis,P.
            and Pennica,D.
  TITLE     Overexpression of the retinoic acid-responsive gene Stra6 in human
            cancers and its synergistic induction by Wnt-1 and retinoic acid
  JOURNAL   Cancer Res 61 (10), 4197-4205 (2001)
   PUBMED   11358845
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Bouillet,P., Sapin,V., Chazaud,C., Messaddeq,N., Decimo,D.,
            Dolle,P. and Chambon,P.
  TITLE     Developmental expression pattern of Stra6, a retinoic
            acid-responsive gene encoding a new type of membrane protein
  JOURNAL   Mech Dev 63 (2), 173-186 (1997)
   PUBMED   9203140
REFERENCE   9  (residues 1 to 667)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
REFERENCE   10 (residues 1 to 667)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC025256.1, AF352729.1 and
            AK056125.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 12, 2008 this sequence version replaced NP_071764.2.
            
            Summary: The protein encoded by this gene is a membrane protein
            involved in the metabolism of retinol. The encoded protein acts as
            a receptor for retinol/retinol binding protein complexes. This
            protein removes the retinol from the complex and transports it
            across the cell membrane. Defects in this gene are a cause of
            syndromic microphthalmia type 9 (MCOPS9). Several transcript
            variants encoding a few different isoforms have been found for this
            gene. [provided by RefSeq, Dec 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 8. The resulting isoform (a) is
            shorter at the N-terminus compared to isoform f. Variants 1, 2, and
            3 all encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025256.1, AF370419.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395105.9/ ENSP00000378537.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..667
                     /product="receptor for retinol uptake STRA6 isoform a"
                     /note="stimulated by retinoic acid gene 6 protein homolog;
                     stimulated by retinoic acid gene 6 homolog; stimulated by
                     retinoic acid 6 homolog; retinol binding protein 4
                     receptor; retinol-binding protein receptor STRA6; receptor
                     for retinol uptake STRA6; RBP receptor"
                     /calculated_mol_wt=73372
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Site            8
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BX79.1)"
     Region          41..657
                     /region_name="RBP_receptor"
                     /note="Retinol binding protein receptor; pfam14752"
                     /db_xref="CDD:464298"
     Site            51..71
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Site            169..189
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Site            206..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Region          235..293
                     /region_name="Interaction with RBP1.
                     /evidence=ECO:0000269|PubMed:22665496"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Site            296..316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Site            368..388
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Site            423..443
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Site            474..494
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX79.1)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21368206; propagated from
                     UniProtKB/Swiss-Prot (Q9BX79.1)"
     CDS             1..667
                     /gene="STRA6"
                     /gene_synonym="MCOPCB8; MCOPS9; PP14296; SLC69A1"
                     /coded_by="NM_022369.4:91..2094"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10261.1"
                     /db_xref="GeneID:64220"
                     /db_xref="HGNC:HGNC:30650"
                     /db_xref="MIM:610745"
ORIGIN      
        1 mssqpagnqt spgatedysy gswyidepqg geelqpegev pschtsippg lyhaclasls
       61 ilvllllaml vrrrqlwpdc vrgrpglpsp vdflagdrpr avpaavfmvl lsslclllpd
      121 edalpfltla sapsqdgkte aprgawkilg lfyyaalyyp laacataght aahllgstls
      181 wahlgvqvwq raecpqvpki ykyysllasl plllglgfls lwypvqlvrs fsrrtgagsk
      241 glqssyseey lrnllcrkkl gssyhtskhg flswarvclr hciytpqpgf hlplklvlsa
      301 tltgtaiyqv allllvgvvp tiqkvragvt tdvsyllagf givlsedkqe vvelvkhhlw
      361 alevcyisal vlsclltflv lmrslvthrt nlralhrgaa ldlsplhrsp hpsrqaifcw
      421 msfsayqtaf iclgllvqqi ifflgttala flvlmpvlhg rnlllfrsle sswpfwltla
      481 lavilqnmaa hwvflethdg hpqltnrrvl yaatfllfpl nvlvgamvat wrvllsalyn
      541 aihlgqmdls llppraatld pgyytyrnfl kievsqshpa mtafcslllq aqsllprtma
      601 apqdslrpge edegmqllqt kdsmakgarp gasrgrarwg laytllhnpt lqvfrktall
      661 gangaqp
//
LOCUS       NP_861527                242 aa            linear   MAM 27-APR-2025
DEFINITION  myogenic factor 6 [Bos taurus].
ACCESSION   NP_861527
VERSION     NP_861527.1
DBSOURCE    REFSEQ: accession NM_181811.2
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wang,S., Cai,X., Xue,K. and Chen,H.
  TITLE     Polymorphisms of MRF4 and H-FABP genes association with growth
            traits in Qinchuan cattle and related hybrids
  JOURNAL   Mol Biol Rep 38 (2), 1013-1020 (2011)
   PUBMED   20582633
  REMARK    GeneRIF: MRF4 and H-FABP genes are associated with growth traits in
            Qinchuan cattle and related hybrids [MRF4]
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Shibata,M., Matsumoto,K., Aikawa,K., Muramoto,T., Fujimura,S. and
            Kadowaki,M.
  TITLE     Gene expression of myostatin during development and regeneration of
            skeletal muscle in Japanese Black Cattle
  JOURNAL   J Anim Sci 84 (11), 2983-2989 (2006)
   PUBMED   17032792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000005.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC142159.1, SRR5571255.1549.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03145412, SAMN03145418
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="5"
                     /map="5"
                     /breed="Hereford"
     Protein         1..242
                     /product="myogenic factor 6"
                     /note="myogenic factor 6, transcription activator; myf-6;
                     muscle-specific regulatory factor 4; myogenic factor 6
                     (herculin)"
                     /calculated_mol_wt=26845
     Region          3..98
                     /region_name="Basic"
                     /note="Myogenic Basic domain; cl11603"
                     /db_xref="CDD:472231"
     Region          31..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7YS80.1)"
     Region          93..156
                     /region_name="bHLH_TS_MRF4_Myf6"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     muscle-specific regulatory factor 4 (MRF4) and similar
                     proteins; cd18934"
                     /db_xref="CDD:381504"
     Site            order(94..95,99,101..103,105,110,127..130)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381504"
     Site            order(108..109,112..113,115..116,131,134,138,140..141,145,
                     147..148)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381504"
     CDS             1..242
                     /gene="MYF6"
                     /gene_synonym="MRF4"
                     /coded_by="NM_181811.2:80..808"
                     /db_xref="BGD:BT23555"
                     /db_xref="GeneID:281336"
                     /db_xref="VGNC:VGNC:31793"
ORIGIN      
        1 mmmdlfetgs yffyldgenv tlqplevaeg splypgsdgt lspcqdqmpp eagsdssgee
       61 hvlappglqp phcpgqcliw acktckrksa ptdrrkaatl rerrrlkkin eafealkrrt
      121 vanpnqrlpk veilrsainy ierlqdllhr ldqqdkmqel gvdpfsyrpk qenlegadfl
      181 rtcssqwpsv sdhsrglvit akeggtsids sassslrcls sivdsissee hklpcveevv
      241 ek
//
LOCUS       NP_001355632             425 aa            linear   ROD 27-APR-2025
DEFINITION  palmitoyltransferase ZDHHC23 [Mus musculus].
ACCESSION   NP_001355632 XP_006522373
VERSION     NP_001355632.1
DBSOURCE    REFSEQ: accession NM_001368703.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Duncan,P.J., Bi,D., McClafferty,H., Chen,L., Tian,L. and
            Shipston,M.J.
  TITLE     S-Acylation controls functional coupling of BK channel pore-forming
            alpha-subunits and beta1-subunits
  JOURNAL   J Biol Chem 294 (32), 12066-12076 (2019)
   PUBMED   31213527
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Jones,M.R., Dilai,S., Lingampally,A., Chao,C.M., Danopoulos,S.,
            Carraro,G., Mukhametshina,R., Wilhelm,J., Baumgart-Vogt,E., Al
            Alam,D., Chen,C., Minoo,P., Zhang,J.S. and Bellusci,S.
  TITLE     A Comprehensive Analysis of Fibroblast Growth Factor Receptor 2b
            Signaling on Epithelial Tip Progenitor Cells During Early Mouse
            Lung Branching Morphogenesis
  JOURNAL   Front Genet 9, 746 (2019)
   PUBMED   30728831
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Koscielny,G., Yaikhom,G., Iyer,V., Meehan,T.F., Morgan,H.,
            Atienza-Herrero,J., Blake,A., Chen,C.K., Easty,R., Di Fenza,A.,
            Fiegel,T., Grifiths,M., Horne,A., Karp,N.A., Kurbatova,N.,
            Mason,J.C., Matthews,P., Oakley,D.J., Qazi,A., Regnart,J.,
            Retha,A., Santos,L.A., Sneddon,D.J., Warren,J., Westerberg,H.,
            Wilson,R.J., Melvin,D.G., Smedley,D., Brown,S.D., Flicek,P.,
            Skarnes,W.C., Mallon,A.M. and Parkinson,H.
  TITLE     The International Mouse Phenotyping Consortium Web Portal, a
            unified point of access for knockout mice and related phenotyping
            data
  JOURNAL   Nucleic Acids Res 42 (Database issue), D802-D809 (2014)
   PUBMED   24194600
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Tian,L., McClafferty,H., Knaus,H.G., Ruth,P. and Shipston,M.J.
  TITLE     Distinct acyl protein transferases and thioesterases control
            surface expression of calcium-activated potassium channels
  JOURNAL   J Biol Chem 287 (18), 14718-14725 (2012)
   PUBMED   22399288
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Lau,N.C., Seto,A.G., Kim,J., Kuramochi-Miyagawa,S., Nakano,T.,
            Bartel,D.P. and Kingston,R.E.
  TITLE     Characterization of the piRNA complex from rat testes
  JOURNAL   Science 313 (5785), 363-367 (2006)
   PUBMED   16778019
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Fukata,M., Fukata,Y., Adesnik,H., Nicoll,R.A. and Bredt,D.S.
  TITLE     Identification of PSD-95 palmitoylating enzymes
  JOURNAL   Neuron 44 (6), 987-996 (2004)
   PUBMED   15603741
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC129306.5, AK147553.1 and CT025520.10.
            
            On Feb 16, 2019 this sequence version replaced XP_006522373.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK147553.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="16"
                     /map="16 28.44 cM"
     Protein         1..425
                     /product="palmitoyltransferase ZDHHC23"
                     /EC_number="2.3.1.225"
                     /note="probable palmitoyltransferase ZDHHC23; zinc finger
                     DHHC domain-containing protein 23; DHHC-containing protein
                     11; nNOS-intereacting DHHC-containing Dem protein-L"
                     /calculated_mol_wt=48019
     Site            82..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5Y5T3.1)"
     Site            103..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5Y5T3.1)"
     Site            131..151
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5Y5T3.1)"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5Y5T3.1)"
     Region          248..374
                     /region_name="DHHC"
                     /note="DHHC palmitoyltransferase; pfam01529"
                     /db_xref="CDD:396215"
     Site            293..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5Y5T3.1)"
     Site            344..364
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5Y5T3.1)"
     Region          422..425
                     /region_name="Interaction with NOS1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5Y5T3.1)"
     CDS             1..425
                     /gene="Zdhhc23"
                     /gene_synonym="DHHC-23; Gm1751; Gm779; nidd"
                     /coded_by="NM_001368703.1:379..1656"
                     /db_xref="CCDS:CCDS28180.1"
                     /db_xref="GeneID:332175"
                     /db_xref="MGI:MGI:2685625"
ORIGIN      
        1 mkpvkkkkte epeleplccc eyidrngekn hvaaclcdcq dldegcdrwl tcqslrpetc
       61 eritdtisdr lripwlrgak kvnisivppl vllpvflhva swhfllgvvv ltslpmlalw
      121 yyylthrrke qtlfflslgl fslgymyyvf lrevvpqgrv gptqlalltc glllillaly
      181 rakknpgyls ndkspsnsqi ecpvkkgqek tkgfpgtdas gslnnrtlkd dvrgssrvgl
      241 dspakvkedw cakcqlvrpa rawhcricgi cvrrmdhhcv winscvgesn hqafilalsi
      301 flltsvygis ltlnticrdr slftalfycp gvyanyssal sftcvwysvi itagmayifl
      361 iqlinisynv terevqqalr qktgrrllcg livdtgqynr gflrnwlqfs tlgthtvhtp
      421 aediv
//
LOCUS       NP_001409                907 aa            linear   PRI 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001409
VERSION     NP_001409.3
DBSOURCE    REFSEQ: accession NM_001418.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Shen,Y., Zhang,Y., Wang,Q., Jiang,B., Jiang,X. and Luo,B.
  TITLE     MicroRNA-877-5p promotes osteoblast differentiation by targeting
            EIF4G2 expression
  JOURNAL   J Orthop Surg Res 19 (1), 134 (2024)
   PUBMED   38342889
  REMARK    GeneRIF: MicroRNA-877-5p promotes osteoblast differentiation by
            targeting EIF4G2 expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Meril,S., Bahlsen,M., Eisenstein,M., Savidor,A., Levin,Y.,
            Bialik,S., Pietrokovski,S. and Kimchi,A.
  TITLE     Loss-of-function cancer-linked mutations in the EIF4G2
            non-canonical translation initiation factor
  JOURNAL   Life Sci Alliance 7 (3), e202302338 (2023)
   PUBMED   38129098
  REMARK    GeneRIF: Loss-of-function cancer-linked mutations in the EIF4G2
            non-canonical translation initiation factor.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Jia,Z., Wang,Y., Gao,J., Zheng,M., Wang,P. and Zu,G.
  TITLE     miR-379-5P INHIBITION ENHANCES INTESTINAL EPITHELIAL PROLIFERATION
            AND BARRIER FUNCTION RECOVERY AFTER ISCHEMIA/REPERFUSION BY
            TARGETING EIF4G2
  JOURNAL   Shock 60 (4), 594-602 (2023)
   PUBMED   37646610
  REMARK    GeneRIF: miR-379-5P INHIBITION ENHANCES INTESTINAL EPITHELIAL
            PROLIFERATION AND BARRIER FUNCTION RECOVERY AFTER
            ISCHEMIA/REPERFUSION BY TARGETING EIF4G2.
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Alard,A., Katsara,O., Rios-Fuller,T., Parra,C., Ozerdem,U.,
            Ernlund,A. and Schneider,R.J.
  TITLE     Breast cancer cell mesenchymal transition and metastasis directed
            by DAP5/eIF3d-mediated selective mRNA translation
  JOURNAL   Cell Rep 42 (6), 112646 (2023)
   PUBMED   37314929
  REMARK    GeneRIF: Breast cancer cell mesenchymal transition and metastasis
            directed by DAP5/eIF3d-mediated selective mRNA translation.
REFERENCE   5  (residues 1 to 907)
  AUTHORS   Takahashi,K., Maruyama,M., Tokuzawa,Y., Murakami,M., Oda,Y.,
            Yoshikane,N., Makabe,K.W., Ichisaka,T. and Yamanaka,S.
  TITLE     Evolutionarily conserved non-AUG translation initiation in
            NAT1/p97/DAP5 (EIF4G2)
  JOURNAL   Genomics 85 (3), 360-371 (2005)
   PUBMED   15718103
  REMARK    GeneRIF: Exclusive use of a GUG translation initiation codon is
            conserved in human, chicken, Xenopus, and zebrafish.
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   7  (residues 1 to 907)
  AUTHORS   Imataka,H. and Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) possesses
            two separate and independent binding sites for eIF4A
  JOURNAL   Mol Cell Biol 17 (12), 6940-6947 (1997)
   PUBMED   9372926
REFERENCE   8  (residues 1 to 907)
  AUTHORS   Levy-Strumpf,N., Deiss,L.P., Berissi,H. and Kimchi,A.
  TITLE     DAP-5, a novel homolog of eukaryotic translation initiation factor
            4G isolated as a putative modulator of gamma interferon-induced
            programmed cell death
  JOURNAL   Mol Cell Biol 17 (3), 1615-1625 (1997)
   PUBMED   9032289
REFERENCE   9  (residues 1 to 907)
  AUTHORS   Imataka,H., Olsen,H.S. and Sonenberg,N.
  TITLE     A new translational regulator with homology to eukaryotic
            translation initiation factor 4G
  JOURNAL   EMBO J 16 (4), 817-825 (1997)
   PUBMED   9049310
  REMARK    GeneRIF: translation starts exclusively at a non-AUG translation
            initiation codon (GUG).
REFERENCE   10 (residues 1 to 907)
  AUTHORS   Shaughnessy,J.D. Jr., Jenkins,N.A. and Copeland,N.G.
  TITLE     cDNA cloning, expression analysis, and chromosomal localization of
            a gene with high homology to wheat eIF-(iso)4F and mammalian eIF-4G
  JOURNAL   Genomics 39 (2), 192-197 (1997)
   PUBMED   9027506
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK223548.1 and DB272352.1.
            
            On Feb 25, 2010 this sequence version replaced NP_001409.2.
            
            Summary: Translation initiation is mediated by specific recognition
            of the cap structure by eukaryotic translation initiation factor 4F
            (eIF4F), which is a cap binding protein complex that consists of
            three subunits: eIF4A, eIF4E and eIF4G. The protein encoded by this
            gene shares similarity with the C-terminal region of eIF4G that
            contains the binding sites for eIF4A and eIF3; eIF4G, in addition,
            contains a binding site for eIF4E at the N-terminus. Unlike eIF4G,
            which supports cap-dependent and independent translation, this gene
            product functions as a general repressor of translation by forming
            translationally inactive complexes. In vitro and in vivo studies
            indicate that translation of this mRNA initiates exclusively at a
            non-AUG (GUG) codon. Alternatively spliced transcript variants
            encoding different isoforms of this gene have been described.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1). Both variants 1 and 3 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.280558.1, BC043149.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2467144
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match       :: ENST00000339995.11/ ENSP00000340281.6
            non-AUG initiation codon :: PMID: 9049310, 15718103
            RefSeq Select criteria   :: based on conservation, expression,
                                        longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..907
                     /product="eukaryotic translation initiation factor 4 gamma
                     2 isoform 1"
                     /note="eIF-4-gamma 2; eukaryotic translation initiation
                     factor 4G-like 1; death-associated protein 5;
                     aging-associated protein 1; DAP-5; eIF4G 2; eIF-4G 2"
                     /calculated_mol_wt=102231
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78344.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P78344.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P78344.1)"
     Region          78..308
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P78344.1)"
     Site            360
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P78344.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P78344.1)"
     Site            431
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P78344.1)"
     Region          <436..>543
                     /region_name="PRK12757"
                     /note="cell division protein FtsN; Provisional"
                     /db_xref="CDD:237191"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P78344.1)"
     Region          498..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78344.1)"
     Site            505
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P78344.1)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P78344.1)"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P78344.1)"
     Region          544..657
                     /region_name="MA3"
                     /note="Domain in DAP-5, eIF4G, MA-3 and other proteins;
                     smart00544"
                     /db_xref="CDD:214714"
     Region          740..876
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P78344.1)"
     CDS             1..907
                     /gene="EIF4G2"
                     /gene_synonym="AAG1; DAP5; NAT1; P97"
                     /coded_by="NM_001418.4:309..3032"
                     /note="isoform 1 is encoded by transcript variant 1;
                     non-AUG (GUG) translation initiation codon"
                     /db_xref="CCDS:CCDS31428.1"
                     /db_xref="GeneID:1982"
                     /db_xref="HGNC:HGNC:3297"
                     /db_xref="MIM:602325"
ORIGIN      
        1 mesaiaegga srfsassggg gsrgapqhyp ktagnseflg ktpgqnaqkw iparstrrdd
       61 nsaannsane kerhdaifrk vrgilnkltp ekfdklclel lnvgveskli lkgvillivd
      121 kaleepkyss lyaqlclrla edapnfdgpa aegqpgqkqs ttfrrllisk lqdefenrtr
      181 nvdvydkren pllpeeeeqr aiakikmlgn ikfigelgkl dlihesilhk ciktllekkk
      241 rvqlkdmged leclcqimrt vgprldhera kslmdqyfar mcslmlskel parirfllqd
      301 tvelrehhwv prkafldngp ktinqirqda vkdlgvfipa pmaqgmrsdf flegpfmppr
      361 mkmdrdplgg ladmfgqmpg sgigtgpgvi qdrfsptmgr hrsnqlfngh gghimpptqs
      421 qfgemggkfm ksqglsqlyh nqsqgllsql qgqskdmppr fskkgqlnad eislrpaqsf
      481 lmnknqvpkl qpqitmipps aqpprtqtpp lgqtpqlglk tnppliqekp aktskkppps
      541 keellkltet vvteylnsgn aneavngvre mrapkhflpe mlskviilsl drsdedkeka
      601 sslisllkqe giatsdnfmq aflnvldqcp klevdiplvk sylaqfaara iiselvsise
      661 laqplesgth fplfllclqq laklqdrewl telfqqskvn mqkmlpeidq nkdrmleile
      721 gkglsflfpl lklekellkq ikldpspqti ykwikdnisp klhvdkgfvn ilmtsflqyi
      781 ssevnppsde tdsssapske qleqekqlll sfkpvmqkfl hdhvdlqvsa lyalqvhcyn
      841 snfpkgmllr ffvhfydmei ieeeaflawk editqefpgk gkalfqvnqw ltwletaeee
      901 eseeead
//
LOCUS       NP_071746                351 aa            linear   PRI 27-APR-2025
DEFINITION  N-terminal EF-hand calcium-binding protein 1 [Homo sapiens].
ACCESSION   NP_071746
VERSION     NP_071746.1
DBSOURCE    REFSEQ: accession NM_022351.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Zhang,M.D., Barde,S., Szodorai,E., Josephson,A., Mitsios,N.,
            Watanabe,M., Attems,J., Lubec,G., Kovacs,G.G., Uhlen,M., Mulder,J.,
            Harkany,T. and Hokfelt,T.
  TITLE     Comparative anatomical distribution of neuronal calcium-binding
            protein (NECAB) 1 and -2 in rodent and human spinal cord
  JOURNAL   Brain Struct Funct 221 (7), 3803-3823 (2016)
   PUBMED   26843217
  REMARK    GeneRIF: Study suggests that the phenotypic segregation of Neuronal
            calcium-binding protein 1 and -2 (NECAB1 and -2) to respective
            excitatory and inhibitory spinal systems can underpin functional
            modalities in determining the fidelity of synaptic
            neurotransmission and neuronal responsiveness, and might bear
            translational relevance to humans.
            Erratum:[Brain Struct Funct. 2016 Sep;221(7):3843. doi:
            10.1007/s00429-016-1236-7. PMID: 27206425]
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Wu,H., Li,D., Shan,Y., Wan,B., Hexige,S., Guo,J., Wu,C. and Yu,L.
  TITLE     EFCBP1/NECAB1, a brain-specifically expressed gene with highest
            abundance in temporal lobe, encodes a protein containing EF-hand
            and antibiotic biosynthesis monooxygenase domains
  JOURNAL   DNA Seq 18 (1), 73-79 (2007)
   PUBMED   17364817
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Sugita,S., Ho,A. and Sudhof,T.C.
  TITLE     NECABs: a family of neuronal Ca(2+)-binding proteins with an
            unusual domain structure and a restricted expression pattern
  JOURNAL   Neuroscience 112 (1), 51-63 (2002)
   PUBMED   12044471
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF414126.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.195227.1,
                                           SRR1660809.70887.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000417640.7/ ENSP00000387380.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.3"
     Protein         1..351
                     /product="N-terminal EF-hand calcium-binding protein 1"
                     /note="synaptotagmin interacting protein 1; neuronal
                     calcium binding protein; EF-hand calcium-binding protein
                     1; neuronal calcium-binding protein 1"
                     /calculated_mol_wt=40440
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESB5; propagated from
                     UniProtKB/Swiss-Prot (Q8N987.1)"
     Region          <33..92
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          180..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N987.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG18; propagated from
                     UniProtKB/Swiss-Prot (Q8N987.1)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG18; propagated from
                     UniProtKB/Swiss-Prot (Q8N987.1)"
     Region          254..324
                     /region_name="ABM"
                     /note="Antibiotic biosynthesis monooxygenase; pfam03992"
                     /db_xref="CDD:427635"
     CDS             1..351
                     /gene="NECAB1"
                     /gene_synonym="EFCBP1; STIP-1"
                     /coded_by="NM_022351.5:113..1168"
                     /db_xref="CCDS:CCDS47889.1"
                     /db_xref="GeneID:64168"
                     /db_xref="HGNC:HGNC:20983"
ORIGIN      
        1 medsqetsps snnsseelss alhlskgmsi fldilrradk nddgklsfee fkayfadgvl
       61 sgeelhelfh tidthntnnl dteelceyfs qhlgeyenvl aaledlnlsi lkamgktkkd
      121 yqeasnleqf vtrfllketl nqlqslqnsl ecametteeq trqerqgpak pevlsiqwpg
      181 krssrrvqrh nsfspnspqf nvsgpgllee dnqwmtqinr lqklidrlek kdlkleppee
      241 eiiegntksh imlvqrqmsv ieedleefql alkhyvesas sqsgclrisi qklsnesrym
      301 iyefwenssv wnshlqtnys ktfqrsnvdf letpeltstm lvpaswwiln n
//
LOCUS       NP_037424                169 aa            linear   PRI 27-APR-2025
DEFINITION  myosin regulatory light chain 11 [Homo sapiens].
ACCESSION   NP_037424
VERSION     NP_037424.2
DBSOURCE    REFSEQ: accession NM_013292.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Chong,J.X., Talbot,J.C., Teets,E.M., Previs,S., Martin,B.L.,
            Shively,K.M., Marvin,C.T., Aylsworth,A.S., Saadeh-Haddad,R.,
            Schatz,U.A., Inzana,F., Ben-Omran,T., Almusafri,F., Al-Mulla,M.,
            Buckingham,K.J., Harel,T., Mor-Shaked,H., Radhakrishnan,P.,
            Girisha,K.M., Nayak,S.S., Shukla,A., Dieterich,K., Faure,J.,
            Rendu,J., Capri,Y., Latypova,X., Nickerson,D.A., Warshaw,D.M.,
            Janssen,P.M.L., Amacher,S.L. and Bamshad,M.J.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Mutations in MYLPF Cause a Novel Segmental Amyoplasia that
            Manifests as Distal Arthrogryposis
  JOURNAL   Am J Hum Genet 107 (2), 293-310 (2020)
   PUBMED   32707087
  REMARK    GeneRIF: Mutations in MYLPF Cause a Novel Segmental Amyoplasia that
            Manifests as Distal Arthrogryposis.
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Kondo,T., Okada,M., Kunihiro,K., Takahashi,M., Yaoita,Y., Hosoya,H.
            and Hamao,K.
  TITLE     Characterization of myosin II regulatory light chain isoforms in
            HeLa cells
  JOURNAL   Cytoskeleton (Hoboken) 72 (12), 609-620 (2015)
   PUBMED   26663899
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Sachdev,S., Raychowdhury,M.K. and Sarkar,S.
  TITLE     Human fast skeletal myosin light chain 2 cDNA: isolation, tissue
            specific expression of the single copy gene, comparative sequence
            analysis of isoforms and evolutionary relationships
  JOURNAL   DNA Seq 14 (5), 339-350 (2003)
   PUBMED   14756420
  REMARK    GeneRIF: A cDNA clone encoding human fast skeletal myosin
            regulatory light chain (HSRLC) has been isolated and characterized
            from a fetal muscle cDNA library.
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Nudel,U., Calvo,J.M., Shani,M. and Levy,Z.
  TITLE     The nucleotide sequence of a rat myosin light chain 2 gene
  JOURNAL   Nucleic Acids Res 12 (18), 7175-7186 (1984)
   PUBMED   6091059
REFERENCE   6  (residues 1 to 169)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK314082.1 and AA662706.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 13, 2003 this sequence version replaced NP_037424.1.
            
            Transcript Variant: This variant (1) is the predominant variant.
            Variants 1, 2, and 3 all encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138525.680494.1, BF693409.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322861.12/ ENSP00000325239.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..169
                     /product="myosin regulatory light chain 11"
                     /note="myosin, light chain 11, regulatory; fast skeletal
                     myosin light chain 2; myosin light chain,
                     phosphorylatable, fast skeletal muscle"
                     /calculated_mol_wt=18883
     Site            2
                     /site_type="methylation"
                     /note="N,N,N-trimethylalanine.
                     /evidence=ECO:0000250|UniProtKB:P02608; propagated from
                     UniProtKB/Swiss-Prot (Q96A32.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97457; propagated from
                     UniProtKB/Swiss-Prot (Q96A32.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97457; propagated from
                     UniProtKB/Swiss-Prot (Q96A32.1)"
     Region          21..157
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04466; propagated from
                     UniProtKB/Swiss-Prot (Q96A32.1)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04466; propagated from
                     UniProtKB/Swiss-Prot (Q96A32.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04466; propagated from
                     UniProtKB/Swiss-Prot (Q96A32.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04466; propagated from
                     UniProtKB/Swiss-Prot (Q96A32.1)"
     CDS             1..169
                     /gene="MYL11"
                     /gene_synonym="DA1C; HUMMLC2B; MLC2B; MRLC2; MYLPF"
                     /coded_by="NM_013292.5:57..566"
                     /db_xref="CCDS:CCDS10677.1"
                     /db_xref="GeneID:29895"
                     /db_xref="HGNC:HGNC:29824"
                     /db_xref="MIM:617378"
ORIGIN      
        1 mapkrakrrt veggsssvfs mfdqtqiqef keaftvidqn rdgiidkedl rdtfaamgrl
       61 nvkneeldam mkeasgpinf tvfltmfgek lkgadpedvi tgafkvldpe gkgtikkkfl
      121 eellttqcdr fsqeeiknmw aafppdvggn vdyknicyvi thgdakdqe
//
LOCUS       NP_037381                606 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 214 isoform 2 [Homo sapiens].
ACCESSION   NP_037381 XP_495864
VERSION     NP_037381.2
DBSOURCE    REFSEQ: accession NM_013249.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Lovering,R.C., Gaudet,P., Acencio,M.L., Ignatchenko,A., Jolma,A.,
            Fornes,O., Kuiper,M., Kulakovskiy,I.V., Laegreid,A., Martin,M.J.
            and Logie,C.
  TITLE     A GO catalogue of human DNA-binding transcription factors
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1864 (11-12), 194765 (2021)
   PUBMED   34673265
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Sofos,E., Pescosolido,M.F., Quintos,J.B., Abuelo,D., Gunn,S.,
            Hovanes,K., Morrow,E.M. and Shur,N.
  TITLE     A novel familial 11p15.4 microduplication associated with
            intellectual disability, dysmorphic features, and obesity with
            involvement of the ZNF214 gene
  JOURNAL   Am J Med Genet A 158A (1), 50-58 (2012)
   PUBMED   22052655
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Nord,A.S., Roeb,W., Dickel,D.E., Walsh,T., Kusenda,M.,
            O'Connor,K.L., Malhotra,D., McCarthy,S.E., Stray,S.M., Taylor,S.M.,
            Sebat,J., King,B., King,M.C. and McClellan,J.M.
  CONSRTM   STAART Psychopharmacology Network
  TITLE     Reduced transcript expression of genes affected by inherited and de
            novo CNVs in autism
  JOURNAL   Eur J Hum Genet 19 (6), 727-731 (2011)
   PUBMED   21448237
  REMARK    GeneRIF: For a number of genes affected by de novo copy number
            variants CNVs in autism (CNTNAP2, ZNF214, ARID1B, Proline
            Dehydrogenase), reduced transcript expression may be a mechanism of
            pathogenesis during neurodevelopment.
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Massart,F. and Saggese,G.
  TITLE     Morphogenetic targets and genetics of undescended testis
  JOURNAL   Sex Dev 4 (6), 326-335 (2010)
   PUBMED   20980787
  REMARK    Review article
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Gianotten,J., van der Veen,F., Alders,M., Leschot,N.J., Tanck,M.W.,
            Land,J.A., Kremer,J.A., Hoefsloot,L.H., Mannens,M.M., Lombardi,M.P.
            and Hoffer,M.J.
  TITLE     Chromosomal region 11p15 is associated with male factor
            subfertility
  JOURNAL   Mol Hum Reprod 9 (10), 587-592 (2003)
   PUBMED   12970396
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Alders,M., Ryan,A., Hodges,M., Bliek,J., Feinberg,A.P.,
            Privitera,O., Westerveld,A., Little,P.F. and Mannens,M.
  TITLE     Disruption of a novel imprinted zinc-finger gene, ZNF215, in
            Beckwith-Wiedemann syndrome
  JOURNAL   Am J Hum Genet 66 (5), 1473-1484 (2000)
   PUBMED   10762538
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Redeker,E., Hoovers,J.M., Alders,M., van Moorsel,C.J., Ivens,A.C.,
            Gregory,S., Kalikin,L., Bliek,J., de Galan,L., van den Bogaard,R.
            et al.
  TITLE     An integrated physical map of 210 markers assigned to the short arm
            of human chromosome 11
  JOURNAL   Genomics 21 (3), 538-550 (1994)
   PUBMED   7959730
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB262997.1, AF056617.1,
            AC100875.3, AA678604.1 and CA313222.1.
            
            On Aug 28, 2007 this sequence version replaced NP_037381.1.
            
            Summary: This gene is expressed predominantly in the testis and
            encodes a zinc finger protein that contains an N-terminal
            kruppel-associated box A (KRABA) domain and twelve zinc finger
            domains. This gene is located within one of three regions on
            chromosome 11p15 associated with Beckwith-Wiedemann syndrome,
            called Beckwith-Wiedemann syndrome chromosome region-2 (BWSCR2),
            and is thought to play a role in the etiology of this disease.
            [provided by RefSeq, Aug 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.237865.1,
                                           SRR1803614.185476.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267765 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278314.5/ ENSP00000278314.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..606
                     /product="zinc finger protein 214 isoform 2"
                     /note="BWSCR2-associated zinc finger protein 1"
                     /calculated_mol_wt=70861
     Region          3..42
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          235..576
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          249..269
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          277..297
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          305..325
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          334..352
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          360..380
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          388..408
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          416..436
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          444..464
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          472..492
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(477,479,481,483..484,487..488,491,505,507,511..512,
                     515..516,519,533,535,537,539..540,543..544,547)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          500..520
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          528..548
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          556..576
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          584..603
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..606
                     /gene="ZNF214"
                     /gene_synonym="BAZ-1; BAZ1"
                     /coded_by="NM_013249.4:295..2115"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS31418.1"
                     /db_xref="GeneID:7761"
                     /db_xref="HGNC:HGNC:13006"
                     /db_xref="MIM:605015"
ORIGIN      
        1 mavtfedvti iftweewkfl dssqkrlyre vmwenytnvm svenwnesyk sqeekfryle
       61 yenfsywqgw wnagaqmyen qnygetvqgt dskdltqqdr sqcqewlils tqvpgygnye
      121 ltfeskslrn lkyknfmpwq sletkttqdy greiymsgsh gfqggryrlg isrknlsmek
      181 eqklivqhsy ipveealpqy vgvicqedll rdsmeekycg cnkckgiyyw nsrcvfhkrn
      241 qpgenlcqcs ickacfsqrs dlyrhprnhi gkklygcdev dgnfhqssgv hfhqrvhige
      301 vpyscnacgk sfsqisslhn hqrvhteekf ykiecdkdls rnsllhihqr lhigekpfkc
      361 nqcgksfnrs svlhvhqrvh tgekpykcde cgkgfsqssn lrihqlvhtg eksykcedcg
      421 kgftqrsnlq ihqrvhtgek pykcddcgkd fshssdlrih qrvhtgekpy tcpecgkgfs
      481 kssklhthqr vhtgekpykc eecgkgfsqr shllihqrvh tgekpykchd cgkgfshssn
      541 lhihqrvhtg ekpyqcakcg kgfshssalr ihqrvhagek pykcreyykg fdhnshlhnn
      601 hrrgnl
//
LOCUS       NP_080341                142 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein mL42 isoform 1 precursor [Mus
            musculus].
ACCESSION   NP_080341
VERSION     NP_080341.1
DBSOURCE    REFSEQ: accession NM_026065.4
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Wang,Y., Yasmin,L., Li,L., Gao,P., Xu,X., Sun,X. and Godbout,R.
  TITLE     DDX1 vesicles control calcium-dependent mitochondrial activity in
            mouse embryos
  JOURNAL   Nat Commun 13 (1), 3794 (2022)
   PUBMED   35778392
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Chern,T., Achilleos,A., Tong,X., Hill,M.C., Saltzman,A.B.,
            Reineke,L.C., Chaudhury,A., Dasgupta,S.K., Redhead,Y., Watkins,D.,
            Neilson,J.R., Thiagarajan,P., Green,J.B.A., Malovannaya,A.,
            Martin,J.F., Rosenblatt,D.S. and Poche,R.A.
  TITLE     Mutations in Hcfc1 and Ronin result in an inborn error of cobalamin
            metabolism and ribosomopathy
  JOURNAL   Nat Commun 13 (1), 134 (2022)
   PUBMED   35013307
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Cheong,A., Lingutla,R. and Mager,J.
  TITLE     Expression analysis of mammalian mitochondrial ribosomal protein
            genes
  JOURNAL   Gene Expr Patterns 38, 119147 (2020)
   PUBMED   32987154
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Nelson,P.S., Pritchard,C., Abbott,D. and Clegg,N.
  TITLE     The human (PEDB) and mouse (mPEDB) Prostate Expression Databases
  JOURNAL   Nucleic Acids Res 30 (1), 218-220 (2002)
   PUBMED   11752298
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Schriml,L.M., Peterson,R.J., Gerrard,B. and Dean,M.
  TITLE     Use of denaturing HPLC to map human and murine genes and to
            validate single-nucleotide polymorphisms
  JOURNAL   Biotechniques 28 (4), 740-745 (2000)
   PUBMED   10769753
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Goldschmidt-Reisin,S., Kitakawa,M., Herfurth,E.,
            Wittmann-Liebold,B., Grohmann,L. and Graack,H.R.
  TITLE     Mammalian mitochondrial ribosomal proteins. N-terminal amino acid
            sequencing, characterization, and identification of corresponding
            gene sequences
  JOURNAL   J Biol Chem 273 (52), 34828-34836 (1998)
   PUBMED   9857009
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DV060222.1, DV050100.1, AK003427.2 and AI839395.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY703684.1, AK003427.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164143 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 49.39 cM"
     Protein         1..142
                     /product="large ribosomal subunit protein mL42 isoform 1
                     precursor"
                     /note="mitochndrial ribosomal protein L42; 28S ribosomal
                     protein L42, mitochondrial; 39S ribosomal protein L42,
                     mitochondrial; 28S ribosomal protein S32, mitochondrial;
                     39S ribosomal protein L31, mitochondrial; large ribosomal
                     subunit protein mL42"
                     /calculated_mol_wt=13122
     transit_peptide 1..31
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9CPV3.1)"
                     /calculated_mol_wt=3389
     mat_peptide     32..142
                     /product="Large ribosomal subunit protein mL42.
                     /id=PRO_0000087725"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CPV3.1)"
                     /calculated_mol_wt=13122
     Region          46..142
                     /region_name="MRP-S32"
                     /note="Mitochondrial 28S ribosomal protein S32; pfam10210"
                     /db_xref="CDD:462999"
     CDS             1..142
                     /gene="Mrpl42"
                     /gene_synonym="2700009F22Rik; 2900055D03Rik; D10Ertd322e;
                     HSPC204; L31mt; L42mt; MRP-L31; MRP-L42; MRP-S32; PTD007;
                     Rpml31; S32mt"
                     /coded_by="NM_026065.4:134..562"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS24137.1"
                     /db_xref="GeneID:67270"
                     /db_xref="MGI:MGI:1333774"
ORIGIN      
        1 maaavkwais nrtiwkhllp iqngalssac hkstysslpd dyncqvdlal tadgrtivcy
       61 hpsvdipyeh tkpipqpdll hnneetheqi lkaklevrks kqleqgpmie qlskvfyttk
      121 hrwyphgqyh nrrkklnppr dr
//
LOCUS       NP_659445                127 aa            linear   PRI 27-APR-2025
DEFINITION  protein yippee-like 4 [Homo sapiens].
ACCESSION   NP_659445
VERSION     NP_659445.1
DBSOURCE    REFSEQ: accession NM_145008.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Oki,K., Plonczynski,M.W., Gomez-Sanchez,E.P. and Gomez-Sanchez,C.E.
  TITLE     YPEL4 modulates HAC15 adrenal cell proliferation and is associated
            with tumor diameter
  JOURNAL   Mol Cell Endocrinol 434, 93-98 (2016)
   PUBMED   27333825
  REMARK    GeneRIF: Results demonstrated that YPEL4 stimulates human adrenal
            cortical cell proliferation, increasing aldosterone production.
            Also, YPEL4 expression levels are higher in human aldosterone
            producing adenoma.
REFERENCE   2  (residues 1 to 127)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Liang,P., Wan,Y., Yan,Y., Wang,Y., Luo,N., Deng,Y., Fan,X.,
            Zhou,J., Li,Y., Wang,Z., Yuan,W., Tang,M., Mo,X. and Wu,X.
  TITLE     MVP interacts with YPEL4 and inhibits YPEL4-mediated activities of
            the ERK signal pathway
  JOURNAL   Biochem Cell Biol 88 (3), 445-450 (2010)
   PUBMED   20555386
  REMARK    GeneRIF: Data show that major vault protein (MVP), a lung
            resistance associated protein, is a binding partner of YPEL4.
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Hosono,K., Sasaki,T., Minoshima,S. and Shimizu,N.
  TITLE     Identification and characterization of a novel gene family YPEL in
            a wide spectrum of eukaryotic species
  JOURNAL   Gene 340 (1), 31-43 (2004)
   PUBMED   15556292
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB098738.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB098738.1, SRR3476690.433653.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300022.8/ ENSP00000300022.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..127
                     /product="protein yippee-like 4"
                     /calculated_mol_wt=14170
     Region          28..118
                     /region_name="RLR_C_like"
                     /note="C-terminal domain of Retinoic acid-inducible gene
                     (RIG)-I-like Receptors, Cereblon (CRBN), and similar
                     protein domains; cl13152"
                     /db_xref="CDD:472430"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5XID5; propagated from
                     UniProtKB/Swiss-Prot (Q96NS1.1)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5XID5; propagated from
                     UniProtKB/Swiss-Prot (Q96NS1.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q5XID5; propagated from
                     UniProtKB/Swiss-Prot (Q96NS1.1)"
     CDS             1..127
                     /gene="YPEL4"
                     /coded_by="NM_145008.3:413..796"
                     /db_xref="CCDS:CCDS7963.1"
                     /db_xref="GeneID:219539"
                     /db_xref="HGNC:HGNC:18328"
                     /db_xref="MIM:609725"
ORIGIN      
        1 mpscdpgpgp aclptktfrs ylprchrtys cvhcrahlak hdelisksfq gshgraylfn
       61 svvnvgcgpa eqrllltglh svadifcesc kttlgwkyeq afetsqkyke gkyiiemshm
      121 vkdngwd
//
LOCUS       NP_859066                693 aa            linear   PRI 27-APR-2025
DEFINITION  CREB-regulated transcription coactivator 2 [Homo sapiens].
ACCESSION   NP_859066
VERSION     NP_859066.1
DBSOURCE    REFSEQ: accession NM_181715.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Carper,M.B., Goel,S., Zhang,A.M., Damrauer,J.S., Cohen,S.,
            Zimmerman,M.P., Gentile,G.M., Parag-Sharma,K., Murphy,R.M.,
            Sato,K., Nickel,K.P., Kimple,R.J., Yarbrough,W.G. and Amelio,A.L.
  TITLE     Activation of the CREB Coactivator CRTC2 by Aberrant Mitogen
            Signaling promotes oncogenic functions in HPV16 positive head and
            neck cancer
  JOURNAL   Neoplasia 29, 100799 (2022)
   PUBMED   35504112
  REMARK    GeneRIF: Activation of the CREB Coactivator CRTC2 by Aberrant
            Mitogen Signaling promotes oncogenic functions in HPV16 positive
            head and neck cancer.
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Mi,Z., Song,Y., Wang,J., Liu,Z., Cao,X., Dang,L., Lu,Y., Sun,Y.,
            Xiong,H., Zhang,L. and Chen,Y.
  TITLE     cAMP-Induced Nuclear Condensation of CRTC2 Promotes Transcription
            Elongation and Cystogenesis in Autosomal Dominant Polycystic Kidney
            Disease
  JOURNAL   Adv Sci (Weinh) 9 (10), e2104578 (2022)
   PUBMED   35037420
  REMARK    GeneRIF: cAMP-Induced Nuclear Condensation of CRTC2 Promotes
            Transcription Elongation and Cystogenesis in Autosomal Dominant
            Polycystic Kidney Disease.
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Wu,Z., Huang,X., Feng,Y., Handschin,C., Feng,Y., Gullicksen,P.S.,
            Bare,O., Labow,M., Spiegelman,B. and Stevenson,S.C.
  TITLE     Transducer of regulated CREB-binding proteins (TORCs) induce
            PGC-1alpha transcription and mitochondrial biogenesis in muscle
            cells
  JOURNAL   Proc Natl Acad Sci U S A 103 (39), 14379-14384 (2006)
   PUBMED   16980408
  REMARK    GeneRIF: These results strongly suggest that TORCs play a key role
            in linking these external signals to the transcriptional program of
            adaptive mitochondrial biogenesis by activating PGC-1alpha gene
            transcription.
REFERENCE   6  (residues 1 to 693)
  AUTHORS   Siu,Y.T., Chin,K.T., Siu,K.L., Yee Wai Choy,E., Jeang,K.T. and
            Jin,D.Y.
  TITLE     TORC1 and TORC2 coactivators are required for tax activation of the
            human T-cell leukemia virus type 1 long terminal repeats
  JOURNAL   J Virol 80 (14), 7052-7059 (2006)
   PUBMED   16809310
  REMARK    GeneRIF: Thus, both TORC1/2 and p300 families of coactivators are
            essential for optimal activation of HTLV-1 transcription by Tax.
REFERENCE   7  (residues 1 to 693)
  AUTHORS   Al-Hakim,A.K., Goransson,O., Deak,M., Toth,R., Campbell,D.G.,
            Morrice,N.A., Prescott,A.R. and Alessi,D.R.
  TITLE     14-3-3 cooperates with LKB1 to regulate the activity and
            localization of QSK and SIK
  JOURNAL   J Cell Sci 118 (Pt 23), 5661-5673 (2005)
   PUBMED   16306228
REFERENCE   8  (residues 1 to 693)
  AUTHORS   Screaton,R.A., Conkright,M.D., Katoh,Y., Best,J.L., Canettieri,G.,
            Jeffries,S., Guzman,E., Niessen,S., Yates,J.R. 3rd, Takemori,H.,
            Okamoto,M. and Montminy,M.
  TITLE     The CREB coactivator TORC2 functions as a calcium- and
            cAMP-sensitive coincidence detector
  JOURNAL   Cell 119 (1), 61-74 (2004)
   PUBMED   15454081
REFERENCE   9  (residues 1 to 693)
  AUTHORS   Iourgenko,V., Zhang,W., Mickanin,C., Daly,I., Jiang,C.,
            Hexham,J.M., Orth,A.P., Miraglia,L., Meltzer,J., Garza,D.,
            Chirn,G.W., McWhinnie,E., Cohen,D., Skelton,J., Terry,R., Yu,Y.,
            Bodian,D., Buxton,F.P., Zhu,J., Song,C. and Labow,M.A.
  TITLE     Identification of a family of cAMP response element-binding protein
            coactivators by genome-scale functional analysis in mammalian cells
  JOURNAL   Proc Natl Acad Sci U S A 100 (21), 12147-12152 (2003)
   PUBMED   14506290
REFERENCE   10 (residues 1 to 693)
  AUTHORS   Conkright,M.D., Canettieri,G., Screaton,R., Guzman,E., Miraglia,L.,
            Hogenesch,J.B. and Montminy,M.
  TITLE     TORCs: transducers of regulated CREB activity
  JOURNAL   Mol Cell 12 (2), 413-423 (2003)
   PUBMED   14536081
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY360172.1, BC053562.1,
            AY726597.1 and BM987537.1.
            
            Summary: This gene encodes a member of the transducers of regulated
            cAMP response element-binding protein activity family of
            transcription coactivators. These proteins promote the
            transcription of genes targeted by the cAMP response
            element-binding protein, and therefore play an important role in
            many cellular processes. Under basal conditions the encoded protein
            is phosphorylated by AMP-activated protein kinase or the
            salt-inducible kinases and is sequestered in the cytoplasm. Upon
            activation by elevated cAMP or calcium, the encoded protein
            translocates to the nucleus and increases target gene expression.
            Single nucleotide polymorphisms in this gene may increase the risk
            of type 2 diabetes. A pseudogene of this gene is located on the
            long arm of chromosome 5. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053562.1, SRR1803611.28709.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368633.2/ ENSP00000357622.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..693
                     /product="CREB-regulated transcription coactivator 2"
                     /note="transducer of regulated cAMP response
                     element-binding protein (CREB) 2"
                     /calculated_mol_wt=73171
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          18..72
                     /region_name="TORC_N"
                     /note="Transducer of regulated CREB activity, N terminus;
                     pfam12884"
                     /db_xref="CDD:463738"
     Site            51
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            99
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            120
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            123
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            161
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          168..320
                     /region_name="TORC_M"
                     /note="Transducer of regulated CREB activity middle
                     domain; pfam12885"
                     /db_xref="CDD:463739"
     Site            168
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK, MARK2, SIK1 and SIK2.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:17210223,
                     ECO:0000269|PubMed:18626018; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          271..287
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MARK2.
                     /evidence=ECO:0000269|PubMed:18626018; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          282..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          328..554
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          615..692
                     /region_name="TORC_C"
                     /note="Transducer of regulated CREB activity, C terminus;
                     pfam12886"
                     /db_xref="CDD:463740"
     Site            623
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            629
                     /site_type="other"
                     /note="Required for ubiquitination and degradation.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     CDS             1..693
                     /gene="CRTC2"
                     /gene_synonym="TORC-2; TORC2"
                     /coded_by="NM_181715.3:116..2197"
                     /db_xref="CCDS:CCDS30875.1"
                     /db_xref="GeneID:200186"
                     /db_xref="HGNC:HGNC:27301"
                     /db_xref="MIM:608972"
ORIGIN      
        1 matsgangpg satasasnpr kfsekialqk qrqaeetaaf eevmmdigst rlqaqklrla
       61 ytrsshyggs lpnvnqigsg laefqsplhs pldssrstrh hglvervqrd prrmvsplrr
      121 ytrhidsspy spaylspppe sswrrtmawg nfpaekgqlf rlpsalnrts sdsalhtsvm
      181 npspqdtypg ptppsilpsr rggildgemd pkvpaieenl lddkhllkpw dakklsssss
      241 rprscevpgi nifpspdqpa nvpvlppamn tggslpdltn lhfppplptp ldpeetayps
      301 lsggnstsnl thtmthlgis rgmglgpgyd apglhsplsh pslqsslsnp nlqaslsspq
      361 pqlqgshshp slpasslarh vlpttslghp slsapalsss ssssstsspv lgapsypast
      421 pgasphhrrv plsplsllag padarrsqqq lpkqfsptms ptlssitqgv pldtsklstd
      481 qrlppypyss pslvlptqph tpkslqqpgl psqscsvqss ggqppgrqsh ygtpyppgps
      541 ghgqqsyhrp msdfnlgnle qfsmespsas lvldppgfse gpgflggegp mggpqdphtf
      601 nhqnlthcsr hgsgpniilt gdsspgfske iaaalagvpg fevsaaglel glgledelrm
      661 eplgleglnm lsdpcallpd paveesfrsd rlq
//
LOCUS       NP_036139                132 aa            linear   ROD 27-APR-2025
DEFINITION  SH2 domain-containing protein 1B [Mus musculus].
ACCESSION   NP_036139 XP_997428
VERSION     NP_036139.3
DBSOURCE    REFSEQ: accession NM_012009.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Chen,J., Zhong,M.C., Guo,H., Davidson,D., Mishel,S., Lu,Y.,
            Rhee,I., Perez-Quintero,L.A., Zhang,S., Cruz-Munoz,M.E., Wu,N.,
            Vinh,D.C., Sinha,M., Calderon,V., Lowell,C.A., Danska,J.S. and
            Veillette,A.
  TITLE     SLAMF7 is critical for phagocytosis of haematopoietic tumour cells
            via Mac-1 integrin
  JOURNAL   Nature 544 (7651), 493-497 (2017)
   PUBMED   28424516
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Guo,H., Cranert,S.A., Lu,Y., Zhong,M.C., Zhang,S., Chen,J., Li,R.,
            Mahl,S.E., Wu,N., Davidson,D., Waggoner,S.N. and Veillette,A.
  TITLE     Deletion of Slam locus in mice reveals inhibitory role of SLAM
            family in NK cell responses regulated by cytokines and LFA-1
  JOURNAL   J Exp Med 213 (10), 2187-2207 (2016)
   PUBMED   27573813
  REMARK    Erratum:[J Exp Med. 2016 Sep 19;213(10):2227. doi:
            10.1084/jem.2016055209072016c. PMID: 27621421]
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Wu,N., Zhong,M.C., Roncagalli,R., Perez-Quintero,L.A., Guo,H.,
            Zhang,Z., Lenoir,C., Dong,Z., Latour,S. and Veillette,A.
  TITLE     A hematopoietic cell-driven mechanism involving SLAMF6 receptor,
            SAP adaptors and SHP-1 phosphatase regulates NK cell education
  JOURNAL   Nat Immunol 17 (4), 387-396 (2016)
   PUBMED   26878112
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Talaei,N., Yu,T., Manion,K., Bremner,R. and Wither,J.E.
  TITLE     Identification of the SLAM Adapter Molecule EAT-2 as a
            Lupus-Susceptibility Gene That Acts through Impaired Negative
            Regulation of Dendritic Cell Signaling
  JOURNAL   J Immunol 195 (10), 4623-4631 (2015)
   PUBMED   26432891
  REMARK    GeneRIF: EAT-2 negatively regulates cytokine production in
            dendritic cells downstream of SLAM engagement and a genetic
            polymorphism that disturbs this process promotes the development of
            lupus.
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Guo,H., Cruz-Munoz,M.E., Wu,N., Robbins,M. and Veillette,A.
  TITLE     Immune cell inhibition by SLAMF7 is mediated by a mechanism
            requiring src kinases, CD45, and SHIP-1 that is defective in
            multiple myeloma cells
  JOURNAL   Mol Cell Biol 35 (1), 41-51 (2015)
   PUBMED   25312647
REFERENCE   6  (residues 1 to 132)
  AUTHORS   Calpe,S., Erdos,E., Liao,G., Wang,N., Rietdijk,S., Simarro,M.,
            Scholtz,B., Mooney,J., Lee,C.H., Shin,M.S., Rajnavolgyi,E.,
            Schatzle,J., Morse,H.C. 3rd, Terhorst,C. and Lanyi,A.
  TITLE     Identification and characterization of two related murine genes,
            Eat2a and Eat2b, encoding single SH2-domain adapters
  JOURNAL   Immunogenetics 58 (1), 15-25 (2006)
   PUBMED   16425036
  REMARK    GeneRIF: Taken together, the data suggest that both EAT-2A and
            EAT-2B are adapters that recruit Src kinases to SLAM family
            receptors using a mechanism that is distinct from that of SAP.
REFERENCE   7  (residues 1 to 132)
  AUTHORS   Roncagalli,R., Taylor,J.E., Zhang,S., Shi,X., Chen,R.,
            Cruz-Munoz,M.E., Yin,L., Latour,S. and Veillette,A.
  TITLE     Negative regulation of natural killer cell function by EAT-2, a
            SAP-related adaptor
  JOURNAL   Nat Immunol 6 (10), 1002-1010 (2005)
   PUBMED   16127454
REFERENCE   8  (residues 1 to 132)
  AUTHORS   Tangye,S.G., van de Weerdt,B.C., Avery,D.T. and Hodgkin,P.D.
  TITLE     CD84 is up-regulated on a major population of human memory B cells
            and recruits the SH2 domain containing proteins SAP and EAT-2
  JOURNAL   Eur J Immunol 32 (6), 1640-1649 (2002)
   PUBMED   12115647
REFERENCE   9  (residues 1 to 132)
  AUTHORS   Morra,M., Lu,J., Poy,F., Martin,M., Sayos,J., Calpe,S., Gullo,C.,
            Howie,D., Rietdijk,S., Thompson,A., Coyle,A.J., Denny,C.,
            Yaffe,M.B., Engel,P., Eck,M.J. and Terhorst,C.
  TITLE     Structural basis for the interaction of the free SH2 domain EAT-2
            with SLAM receptors in hematopoietic cells
  JOURNAL   EMBO J 20 (21), 5840-5852 (2001)
   PUBMED   11689425
REFERENCE   10 (residues 1 to 132)
  AUTHORS   Thompson,A.D., Braun,B.S., Arvand,A., Stewart,S.D., May,W.A.,
            Chen,E., Korenberg,J. and Denny,C.
  TITLE     EAT-2 is a novel SH2 domain containing protein that is up regulated
            by Ewing's sarcoma EWS/FLI1 fusion gene
  JOURNAL   Oncogene 13 (12), 2649-2658 (1996)
   PUBMED   9000139
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC123650.7 and BC116698.1.
            
            On Jun 10, 2007 this sequence version replaced NP_036139.2.
            
            Transcript Variant: This variant (1) represents the longer,
            protein-coding transcript.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK089191.1, BC117508.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849377
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 76.84 cM"
     Protein         1..132
                     /product="SH2 domain-containing protein 1B"
                     /note="EWS/FLI1 activated transcript 2; SH2 domain protein
                     1B1"
                     /calculated_mol_wt=15126
     Region          1..103
                     /region_name="SH2_SAP1"
                     /note="Src homology 2 (SH2) domain found in
                     SLAM-associated protein (SAP)1; cd10342"
                     /db_xref="CDD:198205"
     Site            order(12,31,54)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198205"
     Site            order(52..53,65..66,71,90..92)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198205"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:24687958; propagated from
                     UniProtKB/Swiss-Prot (O35324.1)"
     CDS             1..132
                     /gene="Sh2d1b1"
                     /gene_synonym="EAT-2; EAT-2A; Eat2; Eat2a; Sh2d1b"
                     /coded_by="NM_012009.5:59..457"
                     /db_xref="CCDS:CCDS35767.1"
                     /db_xref="GeneID:26904"
                     /db_xref="MGI:MGI:1349420"
ORIGIN      
        1 mdlpyyhgcl tkrecealll kggvdgnfli rdsesvpgal clcvsfkklv ysyrifrekh
       61 gyyrietnah tprtifpnlq elvskygkpg qglvvhlsnp imrnnlcqrg rrmelelnvy
      121 entdkeyvdv lp
//
LOCUS       NP_001106963             586 aa            linear   PRI 27-APR-2025
DEFINITION  septin-9 isoform a [Homo sapiens].
ACCESSION   NP_001106963
VERSION     NP_001106963.1
DBSOURCE    REFSEQ: accession NM_001113491.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Wang,W., Zhang,X., Gui,P., Zou,Q., Nie,Y., Ma,S. and Zhang,S.
  TITLE     SEPT9: From pan-cancer to lung squamous cell carcinoma
  JOURNAL   BMC Cancer 24 (1), 1105 (2024)
   PUBMED   39237897
  REMARK    GeneRIF: SEPT9: From pan-cancer to lung squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Yan,Z., Liu,H. and Wang,K.
  TITLE     Diagnostic efficacy of SEPT9 and PAX5 gene methylation in
            gastrointestinal cancer and precancerous lesions
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (7), 128-133 (2024)
   PUBMED   39097885
  REMARK    GeneRIF: Diagnostic efficacy of SEPT9 and PAX5 gene methylation in
            gastrointestinal cancer and precancerous lesions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Hecht,M., Alber,N., Marhoffer,P., Johnsson,N. and Gronemeyer,T.
  TITLE     The concerted action of SEPT9 and EPLIN modulates the adhesion and
            migration of human fibroblasts
  JOURNAL   Life Sci Alliance 7 (7), e202201686 (2024)
   PUBMED   38719752
  REMARK    GeneRIF: The concerted action of SEPT9 and EPLIN modulates the
            adhesion and migration of human fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 586)
  AUTHORS   McDade,S.S., Hall,P.A. and Russell,S.E.
  TITLE     Translational control of SEPT9 isoforms is perturbed in disease
  JOURNAL   Hum Mol Genet 16 (7), 742-752 (2007)
   PUBMED   17468182
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Burrows,J.F., Chanduloy,S., McIlhatton,M.A., Nagar,H., Yeates,K.,
            Donaghy,P., Price,J., Godwin,A.K., Johnston,P.G. and Russell,S.E.
  TITLE     Altered expression of the septin gene, SEPT9, in ovarian neoplasia
  JOURNAL   J Pathol 201 (4), 581-588 (2003)
   PUBMED   14648661
REFERENCE   6  (residues 1 to 586)
  AUTHORS   McIlhatton,M.A., Burrows,J.F., Donaghy,P.G., Chanduloy,S.,
            Johnston,P.G. and Russell,S.E.
  TITLE     Genomic organization, complex splicing pattern and expression of a
            human septin gene on chromosome 17q25.3
  JOURNAL   Oncogene 20 (41), 5930-5939 (2001)
   PUBMED   11593400
  REMARK    GeneRIF: Describes alternative splicing of this gene.
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Taki,T., Ohnishi,H., Shinohara,K., Sako,M., Bessho,F.,
            Yanagisawa,M. and Hayashi,Y.
  TITLE     AF17q25, a putative septin family gene, fuses the MLL gene in acute
            myeloid leukemia with t(11;17)(q23;q25)
  JOURNAL   Cancer Res 59 (17), 4261-4265 (1999)
   PUBMED   10485469
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Osaka,M., Rowley,J.D. and Zeleznik-Le,N.J.
  TITLE     MSF (MLL septin-like fusion), a fusion partner gene of MLL, in a
            therapy-related acute myeloid leukemia with a t(11;17)(q23;q25)
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6428-6433 (1999)
   PUBMED   10339604
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Pellegrino,J.E., George,R.A., Biegel,J., Farlow,M.R., Gardner,K.,
            Caress,J., Brown,M.J., Rebbeck,T.R., Bird,T.D. and Chance,P.F.
  TITLE     Hereditary neuralgic amyotrophy: evidence for genetic homogeneity
            and mapping to chromosome 17q25
  JOURNAL   Hum Genet 101 (3), 277-283 (1997)
   PUBMED   9439655
REFERENCE   10 (residues 1 to 586)
  AUTHORS   van Alfen,N., Hannibal,M.C., Chance,P.F. and van Engelen,B.G.M.
  TITLE     Hereditary Neuralgic Amyotrophy - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301569
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068594.15, AC111182.21 and
            AC111170.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the septin family involved in
            cytokinesis and cell cycle control. This gene is a candidate for
            the ovarian tumor suppressor gene. Mutations in this gene cause
            hereditary neuralgic amyotrophy, also known as neuritis with
            brachial predilection. A chromosomal translocation involving this
            gene on chromosome 17 and the MLL gene on chromosome 11 results in
            acute myelomonocytic leukemia. Multiple alternatively spliced
            transcript variants encoding different isoforms have been
            described.[provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1, also known as epsilon) encodes
            the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF189713.3, SRR14038197.1467570.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000427177.6/ ENSP00000391249.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..586
                     /product="septin-9 isoform a"
                     /note="septin D1; ovarian/breast septin; Ov/Br septin; MLL
                     septin-like fusion protein MSF-A; peanut-like 4"
                     /calculated_mol_wt=65271
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Region          <39..247
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Region          62..108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            62
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q80UG5; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Region          134..268
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Region          150..>278
                     /region_name="PHA03269"
                     /note="envelope glycoprotein C; Provisional"
                     /db_xref="CDD:165527"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Region          295..569
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Region          305..312
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            305..312
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(307..313,362,365,444..445,447,501..502)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            337..345
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            339
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Region          362..365
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            362..365
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            364..410
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Region          444..447
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHD8.2)"
     Site            444..447
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            501..503
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     CDS             1..586
                     /gene="SEPTIN9"
                     /gene_synonym="AF17q25; MSF; MSF1; NAPB; PNUTL4; SEPT9;
                     SeptD1; SINT1"
                     /coded_by="NM_001113491.2:38..1798"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45790.1"
                     /db_xref="GeneID:10801"
                     /db_xref="HGNC:HGNC:7323"
                     /db_xref="MIM:604061"
ORIGIN      
        1 mkksysggtr tssgrlrrlg dssgpalkrs feveevetpn stpprrvqtp llratvasst
       61 qkfqdlgvkn sepsarhvds lsqrspkasl rrvelsgpka aepvsrrtel sidisskqve
      121 nagaigpsrf glkraevlgh ktpepaprrt eitivkpqes ahrrmeppas kvpevptapa
      181 tdaapkrvei qmpkpaeapt apspaqtlen sepapvsqlq srlepkpqpp vaeatprsqe
      241 ateaapscvg dmadtprdag lkqapasrne kapvdfgyvg idsileqmrr kamkqgfefn
      301 imvvgqsglg kstlintlfk skisrksvqp tseeripkti eiksithdie ekgvrmkltv
      361 idtpgfgdhi nnencwqpim kfindqyeky lqeevninrk kripdtrvhc clyfipatgh
      421 slrpldiefm krlskvvniv pviakadtlt leervhfkqr itadllsngi dvypqkefde
      481 dsedrlvnek fremipfavv gsdheyqvng krilgrktkw gtieventth cefaylrdll
      541 irthmqnikd itssihfeay rvkrlnegss amangmeeke peapem
//
LOCUS       NP_149053                371 aa            linear   PRI 27-APR-2025
DEFINITION  caytaxin [Homo sapiens].
ACCESSION   NP_149053
VERSION     NP_149053.1
DBSOURCE    REFSEQ: accession NM_033064.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Manzoor,H., Bruggemann,N., Hussain,H.M.J., Baumer,T., Hinrichs,F.,
            Wajid,M., Munchau,A., Naz,S. and Lohmann,K.
  TITLE     Novel homozygous variants in ATCAY, MCOLN1, and SACS in complex
            neurological disorders
  JOURNAL   Parkinsonism Relat Disord 51, 91-95 (2018)
   PUBMED   29449188
  REMARK    GeneRIF: Novel homozygous variants in ATCAY, MCOLN1, and SACS in a
            complex movement disorder in five consanguineous Pakistani
            families.
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Sikora,K.M., Nosavanh,L.M., Kantheti,P., Burmeister,M. and
            Hortsch,M.
  TITLE     Expression of Caytaxin protein in Cayman Ataxia mouse models
            correlates with phenotype severity
  JOURNAL   PLoS One 7 (11), e50570 (2012)
   PUBMED   23226316
  REMARK    GeneRIF: Caytaxin's role in maintaining normal neuronal function
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Walter,S., Atzmon,G., Demerath,E.W., Garcia,M.E., Kaplan,R.C.,
            Kumari,M., Lunetta,K.L., Milaneschi,Y., Tanaka,T., Tranah,G.J.,
            Volker,U., Yu,L., Arnold,A., Benjamin,E.J., Biffar,R.,
            Buchman,A.S., Boerwinkle,E., Couper,D., De Jager,P.L., Evans,D.A.,
            Harris,T.B., Hoffmann,W., Hofman,A., Karasik,D., Kiel,D.P.,
            Kocher,T., Kuningas,M., Launer,L.J., Lohman,K.K., Lutsey,P.L.,
            Mackenbach,J., Marciante,K., Psaty,B.M., Reiman,E.M., Rotter,J.I.,
            Seshadri,S., Shardell,M.D., Smith,A.V., van Duijn,C., Walston,J.,
            Zillikens,M.C., Bandinelli,S., Baumeister,S.E., Bennett,D.A.,
            Ferrucci,L., Gudnason,V., Kivimaki,M., Liu,Y., Murabito,J.M.,
            Newman,A.B., Tiemeier,H. and Franceschini,N.
  TITLE     A genome-wide association study of aging
  JOURNAL   Neurobiol Aging 32 (11), 2109 (2011)
   PUBMED   21782286
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Buschdorf,J.P., Chew,L.L., Soh,U.J., Liou,Y.C. and Low,B.C.
  TITLE     Nerve growth factor stimulates interaction of Cayman ataxia protein
            BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in
            differentiating neurons
  JOURNAL   PLoS One 3 (7), e2686 (2008)
   PUBMED   18628984
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Buschdorf,J.P., Li Chew,L., Zhang,B., Cao,Q., Liang,F.Y.,
            Liou,Y.C., Zhou,Y.T. and Low,B.C.
  TITLE     Brain-specific BNIP-2-homology protein Caytaxin relocalises
            glutaminase to neurite terminals and reduces glutamate levels
  JOURNAL   J Cell Sci 119 (Pt 16), 3337-3350 (2006)
   PUBMED   16899818
REFERENCE   8  (residues 1 to 371)
  AUTHORS   Grelle,G., Kostka,S., Otto,A., Kersten,B., Genser,K.F.,
            Muller,E.C., Walter,S., Boddrich,A., Stelzl,U., Hanig,C.,
            Volkmer-Engert,R., Landgraf,C., Alberti,S., Hohfeld,J.,
            Strodicke,M. and Wanker,E.E.
  TITLE     Identification of VCP/p97, carboxyl terminus of Hsp70-interacting
            protein (CHIP), and amphiphysin II interaction partners using
            membrane-based human proteome arrays
  JOURNAL   Mol Cell Proteomics 5 (2), 234-244 (2006)
   PUBMED   16275660
REFERENCE   9  (residues 1 to 371)
  AUTHORS   Bomar,J.M., Benke,P.J., Slattery,E.L., Puttagunta,R., Taylor,L.P.,
            Seong,E., Nystuen,A., Chen,W., Albin,R.L., Patel,P.D.,
            Kittles,R.A., Sheffield,V.C. and Burmeister,M.
  TITLE     Mutations in a novel gene encoding a CRAL-TRIO domain cause human
            Cayman ataxia and ataxia/dystonia in the jittery mouse
  JOURNAL   Nat Genet 35 (3), 264-269 (2003)
   PUBMED   14556008
  REMARK    Erratum:[Nat Genet. 2005 May;37(5):555]
REFERENCE   10 (residues 1 to 371)
  AUTHORS   Nystuen,A., Benke,P.J., Merren,J., Stone,E.M. and Sheffield,V.C.
  TITLE     A cerebellar ataxia locus identified by DNA pooling to search for
            linkage disequilibrium in an isolated population from the Cayman
            Islands
  JOURNAL   Hum Mol Genet 5 (4), 525-531 (1996)
   PUBMED   8845847
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011488.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a neuron-restricted protein that
            contains a CRAL-TRIO motif common to proteins that bind small
            lipophilic molecules. Mutations in this gene are associated with
            cerebellar ataxia, Cayman type. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027889.1, AB058775.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000450849.7/ ENSP00000390941.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..371
                     /product="caytaxin"
                     /note="Cayman ataxia; ATCAY, caytaxin; ataxia cayman type
                     protein; BNIP-2-homolgy; BNIP-2-homology; ataxia
                     cerebellar Cayman type"
                     /calculated_mol_wt=41990
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86WG3.2)"
     Region          59..187
                     /region_name="BNIP2"
                     /note="Bcl2-/adenovirus E1B nineteen kDa-interacting
                     protein 2; pfam12496"
                     /db_xref="CDD:463609"
     Site            105..106
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000269|PubMed:21369758; propagated from
                     UniProtKB/Swiss-Prot (Q86WG3.2)"
     Region          115..120
                     /region_name="Required for interaction with KLC1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86WG3.2)"
     Region          189..326
                     /region_name="CRAL_TRIO_2"
                     /note="Divergent CRAL/TRIO domain; pfam13716"
                     /db_xref="CDD:463965"
     Region          190..371
                     /region_name="Mediates interaction with GLS.
                     /evidence=ECO:0000269|PubMed:16899818"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86WG3.2)"
     Region          331..371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86WG3.2)"
     CDS             1..371
                     /gene="ATCAY"
                     /gene_synonym="BNIP-H; CLAC"
                     /coded_by="NM_033064.5:366..1481"
                     /db_xref="CCDS:CCDS45923.1"
                     /db_xref="GeneID:85300"
                     /db_xref="HGNC:HGNC:779"
                     /db_xref="MIM:608179"
ORIGIN      
        1 mgtteatlrm envdvkeewq dedlprplpe etgvellgsp vedtssppnt lnfngahrkr
       61 ktlvapeini sldqsegsll sddfldtpdd ldinvddiet pdetdslefl gngnelewed
      121 dtpvataknm pgdsadlfgd gttedgsaan grlwrtviig eqehridlhm irpymkvvth
      181 ggyygeglna iivfaacflp dsslpdyhyi menlflyvis slellvaedy mivylngatp
      241 rrrmpgigwl kkcyqmidrr lrknlkslii vhpswfirtv laisrpfisv kfinkiqyvh
      301 sledleqlip mehvqipdcv lqyeeerlka rresarpqpe fvlprseekp evapvenrsa
      361 lvsedqetsm s
//
LOCUS       NP_001349796             315 aa            linear   ROD 27-APR-2025
DEFINITION  SERTA domain-containing protein 2 isoform 2 [Mus musculus].
ACCESSION   NP_001349796 XP_006514828
VERSION     NP_001349796.1
DBSOURCE    REFSEQ: accession NM_001362867.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Chen,C., Deng,Y., Hu,X., Ren,H., Zhu,J., Fu,S., Xie,J. and Peng,Y.
  TITLE     miR-128-3p regulates 3T3-L1 adipogenesis and lipolysis by targeting
            Pparg and Sertad2
  JOURNAL   J Physiol Biochem 74 (3), 381-393 (2018)
   PUBMED   29654510
  REMARK    GeneRIF: Data suggest that expression of microRNA-128-3p is
            down-regulated during adipogenesis; an abundance of microRNA-128-3p
            appears to down-regulate adipogenesis and up-regulate lipolysis in
            adipocytes by targeting expression of Pparg (peroxisome
            proliferator-activated receptor gamma) and Sertad2 (SERTA
            domain-containing protein-2).
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Qiang,G., Whang Kong,H., Gil,V. and Liew,C.W.
  TITLE     Transcription regulator TRIP-Br2 mediates ER stress-induced brown
            adipocytes dysfunction
  JOURNAL   Sci Rep 7, 40215 (2017)
   PUBMED   28067333
  REMARK    GeneRIF: Study demonstrates a role for TRIP-Br2 in endoplasmic
            reticulum stress-induced brown adipose tissue (BAT) dysfunction,
            and inhibiting TRIP-Br2 could be a potential approach for
            counteracting obesity-induced BAT dysfunction.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Qiang,G., Kong,H.W., Fang,D., McCann,M., Yang,X., Du,G., Bluher,M.,
            Zhu,J. and Liew,C.W.
  TITLE     The obesity-induced transcriptional regulator TRIP-Br2 mediates
            visceral fat endoplasmic reticulum stress-induced inflammation
  JOURNAL   Nat Commun 7, 11378 (2016)
   PUBMED   27109496
  REMARK    GeneRIF: Transcription factor GATA3 is responsible for the ER
            stress-induced TRIP-Br2 expression in visceral fat.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Thompson,C.L., Ng,L., Menon,V., Martinez,S., Lee,C.K.,
            Glattfelder,K., Sunkin,S.M., Henry,A., Lau,C., Dang,C.,
            Garcia-Lopez,R., Martinez-Ferre,A., Pombero,A., Rubenstein,J.L.R.,
            Wakeman,W.B., Hohmann,J., Dee,N., Sodt,A.J., Young,R., Smith,K.,
            Nguyen,T.N., Kidney,J., Kuan,L., Jeromin,A., Kaykas,A., Miller,J.,
            Page,D., Orta,G., Bernard,A., Riley,Z., Smith,S., Wohnoutka,P.,
            Hawrylycz,M.J., Puelles,L. and Jones,A.R.
  TITLE     A high-resolution spatiotemporal atlas of gene expression of the
            developing mouse brain
  JOURNAL   Neuron 83 (2), 309-323 (2014)
   PUBMED   24952961
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Peng,Y., Zhao,S., Song,L., Wang,M. and Jiao,K.
  TITLE     Sertad1 encodes a novel transcriptional co-activator of SMAD1 in
            mouse embryonic hearts
  JOURNAL   Biochem Biophys Res Commun 441 (4), 751-756 (2013)
   PUBMED   24211589
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Sim,K.G., Cheong,J.K. and Hsu,S.I.
  TITLE     The TRIP-Br family of transcriptional regulators is essential for
            the execution of cyclin E-mediated cell cycle progression
  JOURNAL   Cell Cycle 5 (10), 1111-1115 (2006)
   PUBMED   16721052
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Watanabe-Fukunaga,R., Iida,S., Shimizu,Y., Nagata,S. and
            Fukunaga,R.
  TITLE     SEI family of nuclear factors regulates p53-dependent
            transcriptional activation
  JOURNAL   Genes Cells 10 (8), 851-860 (2005)
   PUBMED   16098148
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Fuchs,S., Resch,K., Thiel,C., Ulbrich,M., Platzer,M., Jockusch,H.
            and Schmitt-John,T.
  TITLE     Comparative transcription map of the wobbler critical region on
            mouse chromosome 11 and the homologous region on human chromosome
            2p13-14
  JOURNAL   BMC Genet 3, 14 (2002)
   PUBMED   12174196
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Hsu,S.I., Yang,C.M., Sim,K.G., Hentschel,D.M., O'Leary,E. and
            Bonventre,J.V.
  TITLE     TRIP-Br: a novel family of PHD zinc finger- and
            bromodomain-interacting proteins that regulate the transcriptional
            activity of E2F-1/DP-1
  JOURNAL   EMBO J 20 (9), 2273-2285 (2001)
   PUBMED   11331592
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK147674.1 and AL663115.11.
            
            On May 2, 2018 this sequence version replaced XP_006514828.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK147674.1, SRR7345562.4394592.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 13.03 cM"
     Protein         1..315
                     /product="SERTA domain-containing protein 2 isoform 2"
                     /note="SERTA domain-containing protein 2; PHD zinc finger-
                     and bromodomain-interacting protein 2; transcriptional
                     regulator interacting with the PHD-bromodomain 2"
                     /calculated_mol_wt=34073
     Region          46..81
                     /region_name="SERTA"
                     /note="SERTA motif; pfam06031"
                     /db_xref="CDD:461806"
     CDS             1..315
                     /gene="Sertad2"
                     /gene_synonym="Kiaa0127; mKIAA0127; MNCb-1504; SEI-2;
                     Sei2; TRIP-Br2"
                     /coded_by="NM_001362867.1:667..1614"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:58172"
                     /db_xref="MGI:MGI:1931026"
ORIGIN      
        1 mrvwrymlgk ggkrkfdehe dglegkivsp sdgpsrvsyt lqrqtifnis lmklynhrpl
       61 tepslqktvl innmlrriqe elkqegslrp aftpssqpsn slsdsyqeap ppaphpcdlg
      121 sttpleaclt paslleddnd dtfctlqavh paaptrlssa alpaekdsfs saldeieelc
      181 ptststeaah taapegpkgt ssessvqkpe gpeegrtdds rfmdslpgnf eittstgflt
      241 dltlddilfa didtsmydfd pctsasgtas kmapvsaddl lktlapysnq pvapsqpfkm
      301 dlteldhime vlvgs
//
LOCUS       NP_001346533              59 aa            linear   ROD 27-APR-2025
DEFINITION  single-pass membrane and coiled-coil domain-containing protein 4
            [Mus musculus].
ACCESSION   NP_001346533 XP_011240710
VERSION     NP_001346533.1
DBSOURCE    REFSEQ: accession NM_001359604.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 59)
  AUTHORS   Taher,L., Collette,N.M., Murugesh,D., Maxwell,E., Ovcharenko,I. and
            Loots,G.G.
  TITLE     Global gene expression analysis of murine limb development
  JOURNAL   PLoS One 6 (12), e28358 (2011)
   PUBMED   22174793
REFERENCE   2  (residues 1 to 59)
  AUTHORS   Kehrer-Sawatzki,H., Moschgath,E., Maier,C., Legius,E., Elgar,G. and
            Krone,W.
  TITLE     Characterization of the Fugu rubripes NLK and FN5 genes flanking
            the NF1 (Neurofibromatosis type 1) gene in the 5' direction and
            mapping of the human counterparts
  JOURNAL   Gene 251 (1), 63-71 (2000)
   PUBMED   10863097
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC155259.1 and AC155249.2.
            
            On Jan 13, 2018 this sequence version replaced XP_011240710.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK146267.1, SRR7652917.963675.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 4.95 cM"
     Protein         1..59
                     /product="single-pass membrane and coiled-coil
                     domain-containing protein 4"
                     /note="UPF0443 protein C11orf75 homolog"
                     /calculated_mol_wt=6563
     Region          1..55
                     /region_name="DUF4519"
                     /note="Domain of unknown function (DUF4519); pfam15012"
                     /db_xref="CDD:464444"
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIS3.2)"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIS3.2)"
     CDS             1..59
                     /gene="Smco4"
                     /gene_synonym="Fn5"
                     /coded_by="NM_001359604.1:357..536"
                     /db_xref="CCDS:CCDS22838.1"
                     /db_xref="GeneID:170748"
                     /db_xref="MGI:MGI:3039636"
ORIGIN      
        1 mrqlkgkpkk etskdkkerk qamqearqqi ttvvlptlav vvllivvfvy vatrpavte
//
LOCUS       NP_001308                217 aa            linear   PRI 27-APR-2025
DEFINITION  chorionic somatomammotropin hormone 1 precursor [Homo sapiens].
ACCESSION   NP_001308
VERSION     NP_001308.1
DBSOURCE    REFSEQ: accession NM_001317.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Friedrich,C., Neugebauer,L., Zamora,M., Robles,J.P., Martinez de la
            Escalera,G., Clapp,C., Bertsch,T. and Triebel,J.
  TITLE     Plasmin generates vasoinhibin-like peptides by cleaving prolactin
            and placental lactogen
  JOURNAL   Mol Cell Endocrinol 538, 111471 (2021)
   PUBMED   34601001
  REMARK    GeneRIF: Plasmin generates vasoinhibin-like peptides by cleaving
            prolactin and placental lactogen.
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Cattini,P.A., Jin,Y., Jarmasz,J.S., Noorjahan,N. and Bock,M.E.
  TITLE     Obesity and regulation of human placental lactogen production in
            pregnancy
  JOURNAL   J Neuroendocrinol 32 (11), e12859 (2020)
   PUBMED   32500948
  REMARK    GeneRIF: Obesity and regulation of human placental lactogen
            production in pregnancy.
            Review article
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Prager,S., Wollmann,H.A., Mergenthaler,S., Mavany,M., Eggermann,K.,
            Ranke,M.B. and Eggermann,T.
  TITLE     Characterization of genomic variants in CSH1 and GH2, two candidate
            genes for Silver-Russell syndrome in 17q24-q25
  JOURNAL   Genet Test 7 (3), 259-263 (2003)
   PUBMED   14642004
  REMARK    GeneRIF: a role for CSH1 haploinsufficiency in the etiology of
            growth retardation
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Selby,M.J., Barta,A., Baxter,J.D., Bell,G.I. and Eberhardt,N.L.
  TITLE     Analysis of a major human chorionic somatomammotropin gene.
            Evidence for two functional promoter elements
  JOURNAL   J Biol Chem 259 (21), 13131-13138 (1984)
   PUBMED   6208192
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Roskam,W.G. and Rougeon,F.
  TITLE     Molecular cloning and nucleotide sequence of the human growth
            hormone structural gene
  JOURNAL   Nucleic Acids Res 7 (2), 305-320 (1979)
   PUBMED   386281
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Martial,J.A., Hallewell,R.A., Baxter,J.D. and Goodman,H.M.
  TITLE     Human growth hormone: complementary DNA cloning and expression in
            bacteria
  JOURNAL   Science 205 (4406), 602-607 (1979)
   PUBMED   377496
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Seeburg,P.H., Shine,J., Martial,J.A., Ullrich,A., Baxter,J.D. and
            Goodman,H.M.
  TITLE     Nucleotide sequence of part of the gene for human chorionic
            somatomammotropin: purification of DNA complementary to predominant
            mRNA species
  JOURNAL   Cell 12 (1), 157-165 (1977)
   PUBMED   71212
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Li,C.H., Dixon,J.S. and Chung,D.
  TITLE     Amino acid sequence of human chorionic somatomammotropin
  JOURNAL   Arch Biochem Biophys 155 (1), 95-110 (1973)
   PUBMED   4712450
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Sherwood,L.M., Handwerger,S., McLaurin,W.D. and Lanner,M.
  TITLE     Amino-acid sequence of human placental lactogen
  JOURNAL   Nat New Biol 233 (36), 59-61 (1971)
   PUBMED   5286363
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU134786.2, BG436049.1 and
            BC020756.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            somatotropin/prolactin family of hormones and plays an important
            role in growth control. The gene is located at the growth hormone
            locus on chromosome 17 along with four other related genes in the
            same transcriptional orientation; an arrangement which is thought
            to have evolved by a series of gene duplications. Although the five
            genes share a remarkably high degree of sequence identity, they are
            expressed selectively in different tissues. Alternative splicing
            generates additional isoforms of each of the five growth hormones,
            leading to further diversity and potential for specialization. This
            particular family member is expressed mainly in the placenta and
            utilizes multiple transcription initiation sites. Expression of the
            identical mature proteins for chorionic somatomammotropin hormones
            1 and 2 is upregulated during development, although the ratio of 1
            to 2 increases by term. Mutations in this gene result in placental
            lactogen deficiency and Silver-Russell syndrome. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX395942.2, AL547300.3 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2149398
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316193.13/ ENSP00000316416.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..217
                     /product="chorionic somatomammotropin hormone 1 precursor"
                     /note="chorionic somatomammotropin A; choriomammotropin;
                     placental lactogen; growth hormone B3; Chorionic
                     somatomammotropin hormone 2; chorionic
                     somatomammotropin-1"
                     /calculated_mol_wt=22308
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2730
     mat_peptide     27..217
                     /product="Chorionic somatomammotropin hormone 1.
                     /id=PRO_0000032958"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DML2.1)"
                     /calculated_mol_wt=22308
     Region          35..215
                     /region_name="somatotropin_like"
                     /note="Somatotropin or growth hormone (GH), placental
                     lactogen, and related pituitary gland hormones; cd10285"
                     /db_xref="CDD:198435"
     Site            order(35,38,41..42,44,47..48,51,67..68,71..72,75,87..90,
                     93..94,142,145..146,149,190,193..194,197..198,200..201,
                     204..205,208,215)
                     /site_type="other"
                     /note="receptor binding interface [polypeptide binding]"
                     /db_xref="CDD:198435"
     CDS             1..217
                     /gene="CSH1"
                     /gene_synonym="CS-1; CSA; CSMT; GHB3; hCS-1; hCS-A; PL"
                     /coded_by="NM_001317.6:64..717"
                     /db_xref="CCDS:CCDS11649.1"
                     /db_xref="GeneID:1442"
                     /db_xref="HGNC:HGNC:2440"
                     /db_xref="MIM:150200"
ORIGIN      
        1 mapgsrtsll lafallclpw lqeagavqtv plsrlfdham lqahrahqla idtyqefeet
       61 yipkdqkysf lhdsqtsfcf sdsiptpsnm eetqqksnle llrislllie swlepvrflr
      121 smfannlvyd tsdsddyhll kdleegiqtl mgrledgsrr tgqilkqtys kfdtnshnhd
      181 allknyglly cfrkdmdkve tflrmvqcrs vegscgf
//
LOCUS       NP_077134                357 aa            linear   ROD 27-APR-2025
DEFINITION  hsp70-binding protein 1 [Mus musculus].
ACCESSION   NP_077134
VERSION     NP_077134.1
DBSOURCE    REFSEQ: accession NM_024172.4
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Zhao,T., Hong,Y., Yin,P., Li,S. and Li,X.J.
  TITLE     Differential HspBP1 expression accounts for the greater
            vulnerability of neurons than astrocytes to misfolded proteins
  JOURNAL   Proc Natl Acad Sci U S A 114 (37), E7803-E7811 (2017)
   PUBMED   28847953
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Rogon,C., Ulbricht,A., Hesse,M., Alberti,S., Vijayaraj,P., Best,D.,
            Adams,I.R., Magin,T.M., Fleischmann,B.K. and Hohfeld,J.
  TITLE     HSP70-binding protein HSPBP1 regulates chaperone expression at a
            posttranslational level and is essential for spermatogenesis
  JOURNAL   Mol Biol Cell 25 (15), 2260-2271 (2014)
   PUBMED   24899640
  REMARK    GeneRIF: Male HSPBP1knockout mice are sterile because of impaired
            meiosis and massive apoptosis of spermatocytes.
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Miller,J.A., Nathanson,J., Franjic,D., Shim,S., Dalley,R.A.,
            Shapouri,S., Smith,K.A., Sunkin,S.M., Bernard,A., Bennett,J.L.,
            Lee,C.K., Hawrylycz,M.J., Jones,A.R., Amaral,D.G., Sestan,N.,
            Gage,F.H. and Lein,E.S.
  TITLE     Conserved molecular signatures of neurogenesis in the hippocampal
            subgranular zone of rodents and primates
  JOURNAL   Development 140 (22), 4633-4644 (2013)
   PUBMED   24154525
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Kettern,N., Rogon,C., Limmer,A., Schild,H. and Hohfeld,J.
  TITLE     The Hsc/Hsp70 co-chaperone network controls antigen aggregation and
            presentation during maturation of professional antigen presenting
            cells
  JOURNAL   PLoS One 6 (1), e16398 (2011)
   PUBMED   21283720
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Zhang,C., Xu,Z., He,X.R., Michael,L.H. and Patterson,C.
  TITLE     CHIP, a cochaperone/ubiquitin ligase that regulates protein quality
            control, is required for maximal cardioprotection after myocardial
            infarction in mice
  JOURNAL   Am J Physiol Heart Circ Physiol 288 (6), H2836-H2842 (2005)
   PUBMED   15665051
  REMARK    GeneRIF: Provides a critical cardioprotective effect in the setting
            of ischemia-reperfusion injury due in part to increased apoptosis
            in cardiac cells.
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC161197.9.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK160128.1, BC014758.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 2.69 cM"
     Protein         1..357
                     /product="hsp70-binding protein 1"
                     /note="hsp70-interacting protein 1; heat shock
                     protein-binding protein 1; SPA) binding protein,
                     cytoplasmic cochaperone 1"
                     /calculated_mol_wt=39036
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P31.1)"
     Region          43..137
                     /region_name="Fes1"
                     /note="Nucleotide exchange factor Fes1; pfam08609"
                     /db_xref="CDD:462534"
     Site            order(119,123,127,161,165,169,203,208,212)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          130..172
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P31.1)"
     Region          135..172
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          175..215
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P31.1)"
     Region          178..213
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          218..257
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P31.1)"
     Region          231..255
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          260..299
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P31.1)"
     Region          263..299
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99P31.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NZL4; propagated from
                     UniProtKB/Swiss-Prot (Q99P31.1)"
     CDS             1..357
                     /gene="Hspbp1"
                     /gene_synonym="1500019G21Rik"
                     /coded_by="NM_024172.4:183..1256"
                     /db_xref="CCDS:CCDS20740.1"
                     /db_xref="GeneID:66245"
                     /db_xref="MGI:MGI:1913495"
ORIGIN      
        1 madkgsggsr lplalppasq gcssggsgss aggsgnprpp rnlqgllqma itagsqepdp
       61 ppepmseerr qwlqeamsaa frgqreeveq mknclrvlsq atpamageae latdqqereg
      121 alelladlce nmdnaadfcq lsgmhllvgr yleagaaglr wraaqligtc sqnvaaiqeq
      181 vlglgalrkl lrlldrdscd tvrvkalfai sclvreqeag llqflrldgf svlmramqqq
      241 vqklkvksaf llqnllvghp ehkgtlcsmg mvqqlvalvr tehspfhehv lgalcslvtd
      301 fpqgvrecre pelgleellr hrcqllqqre eyqeelefce kllqtcfssp tddsmdr
//
LOCUS       NP_002510               1427 aa            linear   PRI 27-APR-2025
DEFINITION  protein NPAT isoform 2 [Homo sapiens].
ACCESSION   NP_002510
VERSION     NP_002510.2
DBSOURCE    REFSEQ: accession NM_002519.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1427)
  AUTHORS   Terradas,M., Schubert,S.A., Viana-Errasti,J., Ruano,D., Aiza,G.,
            Nielsen,M., Marciel,P., Tops,C.M., Parra,G., Morreau,H.,
            Torrents,D., van Leerdam,M.E., Capella,G., de Miranda,N.F.C.C.,
            Valle,L. and van Wezel,T.
  TITLE     Germline NPAT inactivating variants as cause of hereditary
            colorectal cancer
  JOURNAL   Eur J Hum Genet 32 (7), 871-875 (2024)
   PUBMED   38778081
  REMARK    GeneRIF: Germline NPAT inactivating variants as cause of hereditary
            colorectal cancer.
REFERENCE   2  (residues 1 to 1427)
  AUTHORS   Chen,C., Gallagher,J.R., Tarlton,J., van Aalten,L., Bray,S.E.,
            Ashford,M.L.J., McCrimmon,R.J., Pearson,E.R., McNeilly,A.D. and
            Sutherland,C.
  TITLE     The genetic association of the transcription factor NPAT with
            glycemic response to metformin involves regulation of fuel
            selection
  JOURNAL   PLoS One 16 (7), e0253533 (2021)
   PUBMED   34197485
  REMARK    GeneRIF: The genetic association of the transcription factor NPAT
            with glycemic response to metformin involves regulation of fuel
            selection.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1427)
  AUTHORS   Bucholc,K., Skrajna,A., Adamska,K., Yang,X.C., Krajewski,K.,
            Poznanski,J., Dadlez,M., Dominski,Z. and Zhukov,I.
  TITLE     Structural Analysis of the SANT/Myb Domain of FLASH and YARP
            Proteins and Their Complex with the C-Terminal Fragment of NPAT by
            NMR Spectroscopy and Computer Simulations
  JOURNAL   Int J Mol Sci 21 (15), 5268 (2020)
   PUBMED   32722282
  REMARK    GeneRIF: Structural Analysis of the SANT/Myb Domain of FLASH and
            YARP Proteins and Their Complex with the C-Terminal Fragment of
            NPAT by NMR Spectroscopy and Computer Simulations.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1427)
  AUTHORS   Ling Zheng,L., Wang,F.Y., Cong,X.X., Shen,Y., Rao,X.S., Huang,D.S.,
            Fan,W., Yi,P., Wang,X.B., Zheng,L., Zhou,Y.T. and Luo,Y.
  TITLE     Interaction of Heat Shock Protein Cpn10 with the Cyclin E/Cdk2
            Substrate Nuclear Protein Ataxia-Telangiectasia (NPAT) Is Involved
            in Regulating Histone Transcription
  JOURNAL   J Biol Chem 290 (49), 29290-29300 (2015)
   PUBMED   26429916
  REMARK    GeneRIF: Cpn10 has a role in the spatial regulation of NPAT
            signaling
REFERENCE   5  (residues 1 to 1427)
  AUTHORS   Yang,X.C., Sabath,I., Kunduru,L., van Wijnen,A.J., Marzluff,W.F.
            and Dominski,Z.
  TITLE     A conserved interaction that is essential for the biogenesis of
            histone locus bodies
  JOURNAL   J Biol Chem 289 (49), 33767-33782 (2014)
   PUBMED   25339177
  REMARK    GeneRIF: The conserved C-terminal domain shared by FLASH, YARP, and
            Mute recognizes the C-terminal sequence of NPAT orthologues, thus
            acting as a signal targeting proteins to histone locus bodies.
REFERENCE   6  (residues 1 to 1427)
  AUTHORS   Imai,T., Sugawara,T., Nishiyama,A., Shimada,R., Ohki,R., Seki,N.,
            Sagara,M., Ito,H., Yamauchi,M. and Hori,T.
  TITLE     The structure and organization of the human NPAT gene
  JOURNAL   Genomics 42 (3), 388-392 (1997)
   PUBMED   9205109
REFERENCE   7  (residues 1 to 1427)
  AUTHORS   Platzer,M., Rotman,G., Bauer,D., Uziel,T., Savitsky,K.,
            Bar-Shira,A., Gilad,S., Shiloh,Y. and Rosenthal,A.
  TITLE     Ataxia-telangiectasia locus: sequence analysis of 184 kb of human
            genomic DNA containing the entire ATM gene
  JOURNAL   Genome Res 7 (6), 592-605 (1997)
   PUBMED   9199932
REFERENCE   8  (residues 1 to 1427)
  AUTHORS   Byrd,P.J., Cooper,P.R., Stankovic,T., Kullar,H.S., Watts,G.D.,
            Robinson,P.J. and Taylor,M.R.
  TITLE     A gene transcribed from the bidirectional ATM promoter coding for a
            serine rich protein: amino acid sequence, structure and expression
            studies
  JOURNAL   Hum Mol Genet 5 (11), 1785-1791 (1996)
   PUBMED   8923007
REFERENCE   9  (residues 1 to 1427)
  AUTHORS   Imai,T., Yamauchi,M., Seki,N., Sugawara,T., Saito,T., Matsuda,Y.,
            Ito,H., Nagase,T., Nomura,N. and Hori,T.
  TITLE     Identification and characterization of a new gene physically linked
            to the ATM gene
  JOURNAL   Genome Res 6 (5), 439-447 (1996)
   PUBMED   8743993
REFERENCE   10 (residues 1 to 1427)
  AUTHORS   Byrd,P.J., McConville,C.M., Cooper,P., Parkhill,J., Stankovic,T.,
            McGuire,G.M., Thick,J.A. and Taylor,A.M.
  TITLE     Mutations revealed by sequencing the 5' half of the gene for ataxia
            telangiectasia
  JOURNAL   Hum Mol Genet 5 (1), 145-149 (1996)
   PUBMED   8789452
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA338219.1, BC050561.2, BC094769.1, X97186.1 and AP002433.5.
            
            On Aug 15, 2007 this sequence version replaced NP_002510.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290020.1, SRR1660803.14079.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278612.9/ ENSP00000278612.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..1427
                     /product="protein NPAT isoform 2"
                     /note="protein NPAT; nuclear protein of the ATM locus;
                     nuclear protein of the ataxia telangiectasia mutated
                     locus; nuclear protein, ataxia-telangiectasia locus;
                     nuclear protein, co-activator of histone transcription"
                     /calculated_mol_wt=154160
     Region          1..318
                     /region_name="Interaction with MIZF.
                     /evidence=ECO:0000269|PubMed:15988025"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          5..25
                     /region_name="Required for activation of histone gene
                     transcription and interaction with MIZF.
                     /evidence=ECO:0000269|PubMed:15988025"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          121..145
                     /region_name="Required for activation of histone gene
                     transcription and interaction with MIZF.
                     /evidence=ECO:0000269|PubMed:15988025"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          199..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          262..338
                     /region_name="Mediates transcriptional activation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BMA5; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          628..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          629..653
                     /region_name="Required for acceleration of G1 phase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          683..732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          758..1427
                     /region_name="NPAT_C"
                     /note="NPAT C terminus; pfam15712"
                     /db_xref="CDD:434876"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10995387; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Site            779
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10995387; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          828..853
                     /region_name="Required for acceleration of G1 phase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1039..1054
                     /region_name="Required for acceleration of G1 phase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1095..1121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10995387; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1133..1152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1228..1252
                     /region_name="Required for acceleration of G1 phase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1228
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1253..1327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BMA5; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1270
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10995387; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1325..1349
                     /region_name="Required for acceleration of G1 phase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1348..1413
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1350
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10995387,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     CDS             1..1427
                     /gene="NPAT"
                     /gene_synonym="E14; E14/NPAT; p220"
                     /coded_by="NM_002519.3:103..4386"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41710.1"
                     /db_xref="GeneID:4863"
                     /db_xref="HGNC:HGNC:7896"
                     /db_xref="MIM:601448"
ORIGIN      
        1 mllpsdvarl vlgylqqenl istcqtfile ssdlkeyaeh ctdegfipac llslfgknlt
       61 tilneyvamk tketsnnvpa imsslwkkld htlsqirsmq ssprfagsqr artrtgiaei
      121 krqrklasqt apasaelltl pylsgqfttp pstgtqvtrp sgqisdpsrs yfvvvnhsqs
      181 qdtvttgeal nvipgaqekk ahaslmspgr rksesqrkst tlsgphstir nfqdpnafav
      241 ekqmvienar ekilsnkslq eklaeninkf ltsdnniaqv pkqtdnnpte petsideflg
      301 lpseihmsee aiqdileqte sdpafqalfd lfdygktknn knisqsissq pmesnpsivl
      361 adetnlavkg sfeteesdgq sgqpafctsy qnddplnalk nsnnhdvlrq edqenfsqis
      421 tsiqkkafkt avpteqkcdi ditfesvpnl ndfnqrgnsn aecnphcael ytnqmstete
      481 maigieknsl ssnvpsesql qpdqpdipit sfvslgcean nenlilsgks sqllsqdtsl
      541 tgkpskksqf censndtvkl kinfhgskss dssevhkski einvlepvms qlsncqdnsc
      601 lqseilpvsv esshlnvsgq veihlgdsls stkqpsndsa svelnhtene aqasksensq
      661 epsssvkeen tiflslggna ncekvaltpp egtpvenshs lppesvcssv gdshpesqnt
      721 ddkpssnnsa eidasnivsl kviisddpfv ssdteltsav ssingenlpt iilssptksp
      781 tknaelvkcl sseetvgavv yaevgdsasm eqslltfkse dsavnntqne dgiafsanvt
      841 pcvskdggyi qlmpatstaf gnsnniliat cvtdptalgt svsqsnvvvl pgnsapmtaq
      901 plppqlqtpp rsnsvfavnq avspnfsqgs aiiiaspvqp vlqgmvgmip vsvvgqngnn
      961 fstpprqvlh mpltapvcnr sipqfpvppk sqkaqglrnk pcigkqvnnl vdssghsvgc
     1021 haqktevsdk siatdlgkks eettvpfpee sivpaakpch rrvlcfdstt apvantqgpn
     1081 hkmvsqnker navsfpnlds pnvsstlkpp snnaikreke kpplpkilsk sesaisrhtt
     1141 iretqsekkv spteivlesf hkatankene lcsdverqkn pensklsigq qngglrseks
     1201 iaslqemtkk qgtssnnknv lsvgtavkdl kqeqtksass littemlqdi qrhssvsrla
     1261 dssdlpvprt pgsgagekhk eepidiikap ssrrfsedss tskvmvppvt pdlpacspas
     1321 etgsensvnm aahtlmilsr aaisrttsat plkdntqqfr assrsttkkr kieelderer
     1381 nsrpssknlt nssipmkkkk ikkkklpssf pagmdvdkfl lslhyde
//
LOCUS       NP_055751                453 aa            linear   PRI 27-APR-2025
DEFINITION  bis(5'-adenosyl)-triphosphatase ENPP4 precursor [Homo sapiens].
ACCESSION   NP_055751 XP_376503
VERSION     NP_055751.1
DBSOURCE    REFSEQ: accession NM_014936.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Albright,R.A., Ornstein,D.L., Cao,W., Chang,W.C., Robert,D.,
            Tehan,M., Hoyer,D., Liu,L., Stabach,P., Yang,G., De La Cruz,E.M.
            and Braddock,D.T.
  TITLE     Molecular basis of purinergic signal metabolism by ectonucleotide
            pyrophosphatase/phosphodiesterases 4 and 1 and implications in
            stroke
  JOURNAL   J Biol Chem 289 (6), 3294-3306 (2014)
   PUBMED   24338010
  REMARK    GeneRIF: The combined studies expand our understanding of NPP1 and
            NPP4 substrate specificity and range and provide a rational
            mechanism by which polymorphisms in NPP1 confer stroke resistance.
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Albright,R.A., Chang,W.C., Robert,D., Ornstein,D.L., Cao,W.,
            Liu,L., Redick,M.E., Young,J.I., De La Cruz,E.M. and Braddock,D.T.
  TITLE     NPP4 is a procoagulant enzyme on the surface of vascular
            endothelium
  JOURNAL   Blood 120 (22), 4432-4440 (2012)
   PUBMED   22995898
  REMARK    GeneRIF: NPP4 promotes hemostasis in vivo by augmenting
            ADP-mediated platelet aggregation at the site of vascular injury.
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA261977.1, AB020686.1 and CA433087.1.
            
            On Oct 14, 2004 this sequence version replaced XP_376503.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.285982.1,
                                           SRR1660807.93025.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321037.5/ ENSP00000318066.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..453
                     /product="bis(5'-adenosyl)-triphosphatase ENPP4 precursor"
                     /EC_number="3.6.1.29"
                     /note="ectonucleotide pyrophosphatase/phosphodiesterase 4
                     (putative function); ectonucleotide
                     pyrophosphatase/phosphodiesterase family member 4; NPP-4;
                     E-NPP 4; AP3Aase; AP3A hydrolase;
                     bis(5'-adenosyl)-triphosphatase ENPP4; ectonucleotide
                     pyrophosphatase/phosphodiesterase 4 (putative)"
                     /calculated_mol_wt=50041
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1618
     mat_peptide     16..453
                     /product="Bis(5'-adenosyl)-triphosphatase ENPP4.
                     /id=PRO_0000324795"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6X5.3)"
                     /calculated_mol_wt=50041
     Region          26..379
                     /region_name="Enpp"
                     /note="Ectonucleotide pyrophosphatase/phosphodiesterase,
                     also called autotaxin; cd16018"
                     /db_xref="CDD:293742"
     Site            order(34,69..70,91,189,193,237..238,336)
                     /site_type="active"
                     /db_xref="CDD:293742"
     Site            order(34,69..70,91,189,193,238,336)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293742"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:24338010; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6X5.3)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:24338010; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6X5.3)"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6X5.3)"
     Site            361..363
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293742"
     Site            386
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:24338010; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6X5.3)"
     Site            408..428
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6X5.3)"
     CDS             1..453
                     /gene="ENPP4"
                     /gene_synonym="NPP4"
                     /coded_by="NM_014936.5:235..1596"
                     /db_xref="CCDS:CCDS34468.1"
                     /db_xref="GeneID:22875"
                     /db_xref="HGNC:HGNC:3359"
                     /db_xref="MIM:617000"
ORIGIN      
        1 mkllvillfs glitgfrsds ssslppklll vsfdgfrady lknyefphlq nfikegvlve
       61 hvknvfitkt fpnhysivtg lyeeshgiva nsmydavtkk hfsdsndkdp fwwneavpiw
      121 vtnqlqenrs saaamwpgtd vpihdtissy fmnynssvsf eerlnnitmw lnnsnppvtf
      181 atlyweepda sghkygpedk enmsrvlkki ddligdlvqr lkmlglwenl nviitsdhgm
      241 tqcsqdrlin ldscidhsyy tlidlspvaa ilpkinrtev ynklkncsph mnvylkedip
      301 nrfyyqhndr iqpiilvade gwtivlness qklgdhgydn slpsmhpfla ahgpafhkgy
      361 khstinivdi ypmmchilgl kphpnngtfg htkcllvdqw cinlpeaiai vigsllvltm
      421 ltcliiimqn rlsvprpfsr lqlqeddddp lig
//
LOCUS       NP_001349838             127 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein mL55 isoform 2 precursor [Mus
            musculus].
ACCESSION   NP_001349838 XP_006534041
VERSION     NP_001349838.1
DBSOURCE    REFSEQ: accession NM_001362909.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Cheong,A., Lingutla,R. and Mager,J.
  TITLE     Expression analysis of mammalian mitochondrial ribosomal protein
            genes
  JOURNAL   Gene Expr Patterns 38, 119147 (2020)
   PUBMED   32987154
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Distler,U., Schmeisser,M.J., Pelosi,A., Reim,D., Kuharev,J.,
            Weiczner,R., Baumgart,J., Boeckers,T.M., Nitsch,R., Vogt,J. and
            Tenzer,S.
  TITLE     In-depth protein profiling of the postsynaptic density from mouse
            hippocampus using data-independent acquisition proteomics
  JOURNAL   Proteomics 14 (21-22), 2607-2613 (2014)
   PUBMED   25211037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL645854.10.
            
            On May 4, 2018 this sequence version replaced XP_006534041.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3193680.1,
                                           SRR11927937.3156764.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 37.05 cM"
     Protein         1..127
                     /product="large ribosomal subunit protein mL55 isoform 2
                     precursor"
                     /note="39S ribosomal protein L55, mitochondrial; large
                     ribosomal subunit protein mL55"
                     /calculated_mol_wt=11554
     transit_peptide 1..32
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9CZ83.1)"
                     /calculated_mol_wt=3585
     Region          10..124
                     /region_name="Mitoc_L55"
                     /note="Mitochondrial ribosomal protein L55; pfam09776"
                     /db_xref="CDD:462893"
     mat_peptide     33..127
                     /product="Large ribosomal subunit protein mL55.
                     /id=PRO_0000273100"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZ83.1)"
                     /calculated_mol_wt=11554
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CZ83.1)"
     CDS             1..127
                     /gene="Mrpl55"
                     /gene_synonym="2810038N09Rik; L55mt; MRP-L55"
                     /coded_by="NM_001362909.1:296..679"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 7"
                     /db_xref="CCDS:CCDS24763.1"
                     /db_xref="GeneID:67212"
                     /db_xref="MGI:MGI:1914462"
ORIGIN      
        1 mplaillsll rhcgvraalp tprhlhtspw radcsraslt rlrrqayarl ypvllvkqdg
       61 stihiryrep rrmlampldl dalspeerra rfrkreaqlq qkreeepevv dsfdterykq
      121 fwtktkk
//
LOCUS       NP_542177                147 aa            linear   PRI 27-APR-2025
DEFINITION  cystatin-9-like precursor [Homo sapiens].
ACCESSION   NP_542177
VERSION     NP_542177.1
DBSOURCE    REFSEQ: accession NM_080610.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Frygelius,J., Arvestad,L., Wedell,A. and Tohonen,V.
  TITLE     Evolution and human tissue expression of the Cres/Testatin subgroup
            genes, a reproductive tissue specific subgroup of the type 2
            cystatins
  JOURNAL   Evol Dev 12 (3), 329-342 (2010)
   PUBMED   20565543
  REMARK    GeneRIF: We show with phylogenetic relations that the CTES genes
            are clustered into three original groups, a testatin, a Cres, and a
            CstL1 group
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Hwang,S.J., Yang,Q., Meigs,J.B., Pearce,E.N. and Fox,C.S.
  TITLE     A genome-wide association for kidney function and endocrine-related
            traits in the NHLBI's Framingham Heart Study
  JOURNAL   BMC Med Genet 8 Suppl 1 (Suppl 1), S10 (2007)
   PUBMED   17903292
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Cornwall,G.A. and Hsia,N.
  TITLE     A new subgroup of the family 2 cystatins
  JOURNAL   Mol Cell Endocrinol 200 (1-2), 1-8 (2003)
   PUBMED   12644294
  REMARK    Review article
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Eriksson,A., Tohonen,V., Wedell,A. and Nordqvist,K.
  TITLE     Isolation of the human testatin gene and analysis in patients with
            abnormal gonadal development
  JOURNAL   Mol Hum Reprod 8 (1), 8-15 (2002)
   PUBMED   11756564
  REMARK    GeneRIF: Results describe the sequence, genomic structure,
            chromosomal location, and expression pattern of the human testatin
            gene.
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Brown,W.M. and Dziegielewska,K.M.
  TITLE     Friends and relations of the cystatin superfamily--new members and
            their evolution
  JOURNAL   Protein Sci 6 (1), 5-12 (1997)
   PUBMED   9007972
  REMARK    Review article
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Dickinson,D.P., Zhao,Y., Thiesse,M. and Siciliano,M.J.
  TITLE     Direct mapping of seven genes encoding human type 2 cystatins to a
            single site located at 20p11.2
  JOURNAL   Genomics 24 (1), 172-175 (1994)
   PUBMED   7896273
REFERENCE   8  (residues 1 to 147)
  AUTHORS   Thiesse,M., Millar,S.J. and Dickinson,D.P.
  TITLE     The human type 2 cystatin gene family consists of eight to nine
            members, with at least seven genes clustered at a single locus on
            human chromosome 20
  JOURNAL   DNA Cell Biol 13 (2), 97-116 (1994)
   PUBMED   8179826
REFERENCE   9  (residues 1 to 147)
  AUTHORS   Dickinson,D.P., Thiesse,M., Dempsey,L.D. and Millar,S.J.
  TITLE     Genomic cloning, physical mapping, and expression of human type 2
            cystatin genes
  JOURNAL   Crit Rev Oral Biol Med 4 (3-4), 573-580 (1993)
   PUBMED   7690606
REFERENCE   10 (residues 1 to 147)
  AUTHORS   Saitoh,E., Isemura,S., Sanada,K., Kim,H.S., Smithies,O. and
            Maeda,N.
  TITLE     Cystatin superfamily. Evidence that family II cystatin genes are
            evolutionarily related to family III cystatin genes
  JOURNAL   Biol Chem Hoppe Seyler 369 Suppl, 191-197 (1988)
   PUBMED   3202964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC029656.1.
            
            Summary: The cystatin superfamily encompasses proteins that contain
            multiple cystatin-like sequences. Some of the members are active
            cysteine protease inhibitors, while others have lost or perhaps
            never acquired this inhibitory activity. There are three inhibitory
            families in the superfamily, including the type 1 cystatins
            (stefins), type 2 cystatins and the kininogens. The type 2 cystatin
            proteins are a class of cysteine proteinase inhibitors found in a
            variety of human fluids and secretions. The cystatin locus on
            chromosome 20 contains the majority of the type 2 cystatin genes
            and pseudogenes. This gene is located in the cystatin locus and
            encodes a protein similar to mouse cystatin 9. Based on its
            testis-specific expression, it is likely to have a role in tissue
            reorganization during early testis development. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029656.1, AY358615.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188, SAMEA2161674
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376979.4/ ENSP00000366178.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.21"
     Protein         1..147
                     /product="cystatin-9-like precursor"
                     /note="testatin; testicular tissue protein Li 45"
                     /calculated_mol_wt=17145
     mat_peptide     29..147
                     /product="cystatin-9-like"
                     /calculated_mol_wt=14240
     Region          51..143
                     /region_name="CY"
                     /note="Cystatin-like domain; smart00043"
                     /db_xref="CDD:214484"
     Site            order(80..82,84)
                     /site_type="active"
                     /note="putative proteinase inhibition site [active]"
                     /db_xref="CDD:238002"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H4G1.1)"
     Site            139
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H4G1.1)"
     CDS             1..147
                     /gene="CST9L"
                     /gene_synonym="bA218C14.1; CTES7B"
                     /coded_by="NM_080610.3:35..478"
                     /db_xref="CCDS:CCDS13157.1"
                     /db_xref="GeneID:128821"
                     /db_xref="HGNC:HGNC:16233"
                     /db_xref="MIM:616536"
ORIGIN      
        1 mlglpwkggl swallllllg sqilliyawh fheqrdcdeh nvmarylpat vefavhtfnq
       61 qskdyyayrl ghilnswkeq vesktvfsme lllgrtrcgk feddidnchf qestelnntf
      121 tcfftistrp wmtqfsllnk tclegfh
//
LOCUS       NP_001127838             585 aa            linear   PRI 27-APR-2025
DEFINITION  glutamate decarboxylase 2 [Homo sapiens].
ACCESSION   NP_001127838
VERSION     NP_001127838.1
DBSOURCE    REFSEQ: accession NM_001134366.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Wang,J., Owji,A.P., Kittredge,A., Clark,Z., Zhang,Y. and Yang,T.
  TITLE     GAD65 tunes the functions of Best1 as a GABA receptor and a
            neurotransmitter conducting channel
  JOURNAL   Nat Commun 15 (1), 8051 (2024)
   PUBMED   39277606
  REMARK    GeneRIF: GAD65 tunes the functions of Best1 as a GABA receptor and
            a neurotransmitter conducting channel.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Su,Z., Ma,C., Zhao,R., Jiang,Y., Cai,Y., Yong,G., Yang,T. and Xu,X.
  TITLE     Heterogeneity of circulating CXCR5-PD-1hiTph cells in patients of
            type 2 and type 1 diabetes in Chinese population
  JOURNAL   Acta Diabetol 60 (6), 767-776 (2023)
   PUBMED   36879107
  REMARK    GeneRIF: Heterogeneity of circulating CXCR5-PD-1[hi]Tph cells in
            patients of type 2 and type 1 diabetes in Chinese population.
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Cai,R., Zhao,F., Zhou,H., Wang,Z., Lin,D., Huang,L., Xie,W.,
            Chen,J., Zhou,L., Zhang,N. and Huang,C.
  TITLE     A tumor-associated autoantibody panel for the detection of
            non-small cell lung cancer
  JOURNAL   Front Oncol 12, 1056572 (2022)
   PUBMED   36531074
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Bedi,S., Richardson,T.M., Jia,B., Saab,H., Brinkman,F.S.L. and
            Westley,M.
  TITLE     Similarities between bacterial GAD and human GAD65: Implications in
            gut mediated autoimmune type 1 diabetes
  JOURNAL   PLoS One 17 (2), e0261103 (2022)
   PUBMED   35196314
  REMARK    GeneRIF: Similarities between bacterial GAD and human GAD65:
            Implications in gut mediated autoimmune type 1 diabetes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Vazifekhah,S., Barfi,S., Soleimany,F., Aliakbar,A., Zavvari,F. and
            Karimzadeh,F.
  TITLE     The plasma level of glutamic acid decarboxylase 65 (GAD65)
            increased in severely autistic Iranian children
  JOURNAL   Bratisl Lek Listy 123 (5), 347-351 (2022)
   PUBMED   35420879
  REMARK    GeneRIF: The plasma level of glutamic acid decarboxylase 65 (GAD65)
            increased in severely autistic Iranian children.
REFERENCE   6  (residues 1 to 585)
  AUTHORS   Dirkx,R. Jr., Thomas,A., Li,L., Lernmark,A., Sherwin,R.S., De
            Camilli,P. and Solimena,M.
  TITLE     Targeting of the 67-kDa isoform of glutamic acid decarboxylase to
            intracellular organelles is mediated by its interaction with the
            NH2-terminal region of the 65-kDa isoform of glutamic acid
            decarboxylase
  JOURNAL   J Biol Chem 270 (5), 2241-2246 (1995)
   PUBMED   7836456
REFERENCE   7  (residues 1 to 585)
  AUTHORS   Mauch,L., Abney,C.C., Berg,H., Scherbaum,W.A., Liedvogel,B. and
            Northemann,W.
  TITLE     Characterization of a linear epitope within the human pancreatic
            64-kDa glutamic acid decarboxylase and its autoimmune recognition
            by sera from insulin-dependent diabetes mellitus patients
  JOURNAL   Eur J Biochem 212 (2), 597-603 (1993)
   PUBMED   7680313
REFERENCE   8  (residues 1 to 585)
  AUTHORS   Bu,D.F., Erlander,M.G., Hitz,B.C., Tillakaratne,N.J., Kaufman,D.L.,
            Wagner-McPherson,C.B., Evans,G.A. and Tobin,A.J.
  TITLE     Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are
            each encoded by a single gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2115-2119 (1992)
   PUBMED   1549570
REFERENCE   9  (residues 1 to 585)
  AUTHORS   Karlsen,A.E., Hagopian,W.A., Grubin,C.E., Dube,S., Disteche,C.M.,
            Adler,D.A., Barmeier,H., Mathewes,S., Grant,F.J., Foster,D. and
            Lernmark,A.
  TITLE     Cloning and primary structure of a human islet isoform of glutamic
            acid decarboxylase from chromosome 10
  JOURNAL   Proc Natl Acad Sci U S A 88 (19), 8337-8341 (1991)
   PUBMED   1924293
REFERENCE   10 (residues 1 to 585)
  AUTHORS   Cram,D.S., Barnett,L.D., Joseph,J.L. and Harrison,L.C.
  TITLE     Cloning and partial nucleotide sequence of human glutamic acid
            decarboxylase cDNA from brain and pancreatic islets
  JOURNAL   Biochem Biophys Res Commun 176 (3), 1239-1244 (1991)
   PUBMED   2039509
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M81882.1 and AL162503.12.
            
            Summary: This gene encodes one of several forms of glutamic acid
            decarboxylase, identified as a major autoantigen in
            insulin-dependent diabetes. The enzyme encoded is responsible for
            catalyzing the production of gamma-aminobutyric acid from
            L-glutamic acid. A pathogenic role for this enzyme has been
            identified in the human pancreas since it has been identified as an
            autoantibody and an autoreactive T cell target in insulin-dependent
            diabetes. This gene may also play a role in the stiff man syndrome.
            Alternative splicing results in multiple transcript variants that
            encode the same protein. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (2) differs in the 3' UTR,
            compared to variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M81882.1, SRR1803614.163972.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376261.8/ ENSP00000365437.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..585
                     /product="glutamate decarboxylase 2"
                     /EC_number="4.1.1.15"
                     /note="Glutamate decarboxylase-2 (pancreas); GAD-65; 65
                     kDa glutamic acid decarboxylase; glutamate decarboxylase 2
                     (pancreatic islets and brain, 65kDa)"
                     /calculated_mol_wt=65280
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05329.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8999827; propagated from
                     UniProtKB/Swiss-Prot (Q05329.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8999827; propagated from
                     UniProtKB/Swiss-Prot (Q05329.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8999827; propagated from
                     UniProtKB/Swiss-Prot (Q05329.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8999827; propagated from
                     UniProtKB/Swiss-Prot (Q05329.1)"
     Region          138..509
                     /region_name="Pyridoxal_deC"
                     /note="Pyridoxal-dependent decarboxylase conserved domain;
                     pfam00282"
                     /db_xref="CDD:395219"
     Site            order(243..244,247,335,364,367,393,396)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99743"
     Site            396
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99743"
     CDS             1..585
                     /gene="GAD2"
                     /gene_synonym="GAD65"
                     /coded_by="NM_001134366.2:37..1794"
                     /db_xref="CCDS:CCDS7149.1"
                     /db_xref="GeneID:2572"
                     /db_xref="HGNC:HGNC:4093"
                     /db_xref="MIM:138275"
ORIGIN      
        1 maspgsgfws fgsedgsgds enpgtarawc qvaqkftggi gnklcallyg daekpaesgg
       61 sqppraaark aacacdqkpc scskvdvnya flhatdllpa cdgerptlaf lqdvmnillq
      121 yvvksfdrst kvidfhypne llqeynwela dqpqnleeil mhcqttlkya iktghpryfn
      181 qlstgldmvg laadwltsta ntnmftyeia pvfvlleyvt lkkmreiigw pggsgdgifs
      241 pggaisnmya mmiarfkmfp evkekgmaal prliaftseh shfslkkgaa algigtdsvi
      301 likcdergkm ipsdlerril eakqkgfvpf lvsatagttv ygafdpllav adickkykiw
      361 mhvdaawggg llmsrkhkwk lsgveransv twnphkmmgv plqcsallvr eeglmqncnq
      421 mhasylfqqd khydlsydtg dkalqcgrhv dvfklwlmwr akgttgfeah vdkclelaey
      481 lyniiknreg yemvfdgkpq htnvcfwyip pslrtledne ermsrlskva pvikarmmey
      541 gttmvsyqpl gdkvnffrmv isnpaathqd idflieeier lgqdl
//
LOCUS       NP_598463                723 aa            linear   ROD 27-APR-2025
DEFINITION  nucleolar protein 11 isoform 1 [Mus musculus].
ACCESSION   NP_598463
VERSION     NP_598463.2
DBSOURCE    REFSEQ: accession NM_133702.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK076704.1, AK078524.1 and AL596116.14.
            
            On May 28, 2009 this sequence version replaced NP_598463.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK078524.1, BC024874.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 70.19 cM"
     Protein         1..723
                     /product="nucleolar protein 11 isoform 1"
                     /calculated_mol_wt=80687
     Region          200..243
                     /region_name="NUC205"
                     /note="NUC205 domain; pfam08168"
                     /db_xref="CDD:429856"
     Site            346
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8H0; propagated from
                     UniProtKB/Swiss-Prot (Q8BJW5.1)"
     Region          549..572
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BJW5.1)"
     CDS             1..723
                     /gene="Nol11"
                     /gene_synonym="1500002M01Rik"
                     /coded_by="NM_133702.3:125..2296"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS25566.1"
                     /db_xref="GeneID:68979"
                     /db_xref="MGI:MGI:1916229"
ORIGIN      
        1 matleeeftl stgvlgagpe gflgveqtdk adqflvtdsg rtvvlykvsd qkplgswsvk
       61 qgqsitcpav cnfqtgeyim vhdhkvlriw nnddvnvdkv fkatlsaevh rihsvqrtep
      121 lvlfrggaar gleallvepq qniesvipde evivwsevfm lfkqpvlifi tenhghyyay
      181 vrlckshsls kytlllekee ksvkpnftar vdgkfislvs lssdgciyet lipiyssdte
      241 qnqrlvralm lksvvsggvr ngvaltildq dhiavlgppl saskeclsiw nikfqtlqts
      301 kelpqgtsgq lwyhgevlfm lhgksltvip ykceesslag algklkhtqe sgthsvphfv
      361 nwetcsgyel gssgaeqsrt lrrkkvetnl qpevpgfkql lsiikkdsek hievelrkfl
      421 akstpafhti igdlvaglvg rckaepsfyp rncltqliqt hvlsyslcpd lmeialehtd
      481 vqmlqlclqq fpdipesttc aclklflsvg ddclrdsnin mesvfdysds tqdekkemee
      541 qieivqngfg pedgncseds qqlndkpadt ahepgsfpvt scpvapkraa llnavlhsay
      601 sepfllphlk dipakhvtlf lqylyflylk ctgsatmtlp gvnpptvsqi mdwiclllda
      661 nftvllmipe akrlllilyn fvksqisiys elnkiavsfr elqrlnreks srglysievl
      721 elf
//
LOCUS       NP_001533               1214 aa            linear   PRI 27-APR-2025
DEFINITION  immunoglobulin superfamily member 3 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001533 XP_005270850
VERSION     NP_001533.2
DBSOURCE    REFSEQ: accession NM_001542.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1214)
  AUTHORS   Schweitzer,K.S., Jinawath,N., Yonescu,R., Ni,K., Rush,N.,
            Charoensawan,V., Bronova,I., Berdyshev,E., Leach,S.M.,
            Gillenwater,L.A., Bowler,R.P., Pearse,D.B., Griffin,C.A. and
            Petrache,I.
  TITLE     IGSF3 mutation identified in patient with severe COPD alters cell
            function and motility
  JOURNAL   JCI Insight 5 (14), 138101 (2020)
   PUBMED   32573489
  REMARK    GeneRIF: IGSF3 mutation identified in patient with severe COPD
            alters cell function and motility.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1214)
  AUTHORS   Yuan,Y., Yang,L., Liu,T., Zhang,H. and Lu,Q.
  TITLE     Osteoclastogenesis inhibition by mutated IGSF23 results in human
            osteopetrosis
  JOURNAL   Cell Prolif 52 (6), e12693 (2019)
   PUBMED   31560140
  REMARK    GeneRIF: the IGSF23 mutation led to decreased c-Fos and NFATC1
            expression levels by inhibiting the mitogen-activated protein
            kinase signalling pathways
REFERENCE   3  (residues 1 to 1214)
  AUTHORS   Foster,J. 2nd, Kapoor,S., Diaz-Horta,O., Singh,A., Abad,C.,
            Rastogi,A., Moharana,R., Tekeli,O., Walz,K. and Tekin,M.
  TITLE     Identification of an IGSF3 mutation in a family with congenital
            nasolacrimal duct obstruction
  JOURNAL   Clin Genet 86 (6), 589-591 (2014)
   PUBMED   24372406
  REMARK    GeneRIF: Based on IGSF3 mutation in a family with congenital
            nasolacrimal duct obstruction we conclude that the disruption of
            IGSF3 is the very likely cause of autosomal recessive nasolacrimal
            duct obstruction.
REFERENCE   4  (residues 1 to 1214)
  AUTHORS   Saupe,S., Roizes,G., Peter,M., Boyle,S., Gardiner,K. and De
            Sario,A.
  TITLE     Molecular cloning of a human cDNA IGSF3 encoding an
            immunoglobulin-like membrane protein: expression and mapping to
            chromosome band 1p13
  JOURNAL   Genomics 52 (3), 305-311 (1998)
   PUBMED   9790749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC110651.1, AF031174.1,
            AB007935.2 and AI968231.1.
            
            On or before Sep 13, 2018 this sequence version replaced
            XP_005270850.1, NP_001533.1.
            
            Summary: The protein encoded by this gene is an immunoglobulin-like
            membrane protein containing several V-type Ig-like domains. A
            mutation in this gene has been associated with bilateral
            nasolacrimal duct obstruction (LCDD). [provided by RefSeq, Jun
            2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            CDS exon combination :: AF031174.1 [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.1"
     Protein         1..1214
                     /product="immunoglobulin superfamily member 3 isoform 1
                     precursor"
                     /note="glu-Trp-Ile EWI motif-containing protein 3;
                     immunoglobin superfamily, member 3"
                     /calculated_mol_wt=135550
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1985
     Region          32..132
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          38..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75054.3)"
     Region          103..107
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          152..251
                     /region_name="IgV"
                     /note="Immunoglobulin variable domain (IgV); cd00099"
                     /db_xref="CDD:409355"
     Region          155..157
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409355"
     Region          161..169
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409355"
     Region          169..179
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409355"
     Site            order(179..180,182,249)
                     /site_type="other"
                     /note="antigen binding site [polypeptide binding]"
                     /db_xref="CDD:409355"
     Region          180..194
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409355"
     Region          180..186
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409355"
     Region          192..195
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409355"
     Region          195..219
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409355"
     Region          219..224
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409355"
     Region          220..248
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409355"
     Region          228..234
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409355"
     Region          242..249
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409355"
     Region          250..252
                     /region_name="EWI motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O75054.3)"
     Region          293..389
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          298..306
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          315..319
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          356..363
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          373..378
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            438
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75054.3)"
     Region          441..534
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Site            675
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75054.3)"
     Region          707..804
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     Region          841..940
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     Site            862
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75054.3)"
     Region          1017..1053
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75054.3)"
     Site            1097
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75054.3)"
     Site            1145..1165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75054.3)"
     CDS             1..1214
                     /gene="IGSF3"
                     /gene_synonym="EWI-3; LCDD; V8"
                     /coded_by="NM_001542.4:769..4413"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS30814.1"
                     /db_xref="GeneID:3321"
                     /db_xref="HGNC:HGNC:5950"
                     /db_xref="MIM:603491"
ORIGIN      
        1 mkcffpvlsc lavlgvvsaq rqvtvqegpl yrtegshiti wcnvsgyqgp seqnfqwsiy
       61 lpssperevq ivstmdssfp yaiytqrvrg gkifiervqg nstllhitdl qardageyec
      121 htpstdkqyf gsysakmnlv vipdslqtta mpqtlhrveq dpleltceva setiqhshls
      181 vawlrqkvge kpvevislsr dfmlhsssey aqrqslgevr ldklgrttfr ltifhlqpsd
      241 qgefyceaae wiqdpdgswy amtrkrsega vvnvqptdke ftvrletekr lhtvgepvef
      301 rcileaqnvp dryfavswaf nssliatmgp navpvlnsef ahreargqlk vakesdsvfv
      361 lkiyhlrqed sgkyncrvte rektvtgefi dkeskrpkni piivlpltdn wvvkvpqhhq
      421 llsqghless isvevasnas vilegedlrf scsvrtagrp qgrfsviwql vdrqnrrsni
      481 mwldrdgtvq pgssywerss fggvqmeqvq pnsfslgifn srkedegqye chvtewvrav
      541 dgewqivger rastpisita lemgfavtai srtpgvtysd sfdlqciikp hypawvpvsv
      601 twrfqpvgtv efhdlvtftr dggvqwgdrs ssfrtrtaie kaessnnvrl sisrasdtea
      661 gkyqcvaelw rknynntwtr laertsnlle irvlqpvtkl qvskskrtlt lvenkpiqln
      721 csvksqtsqn shfavlwyvh kpsdadgkli lktthnsafe ygtyaeeegl rarlqferhv
      781 sgglfsltvq raevsdsgsy ychveewlls pnyawyklae evsgrtevtv kqpdsrlrls
      841 qaqgnlsvle trqvqlecvv lnrtsitsql mvewfvwkpn hperetvarl srdatfhyge
      901 qaaknnlkgr lhlespspgv yrlfiqnvav qdsgtyschv eewlpspsgm wykraedtag
      961 qtaltvmrpd aslqvdtvvp natvsekaaf qldcsivsrs sqdsrfavaw yslrtkaggk
     1021 rsspgleeqe eereeeeeed ddddddpter tallsvgpda vfgpegspwe grlrfqrlsp
     1081 vlyrltvlqa spqdtgnysc hveewlpspq kewyrlteee sapigirvld tsptlqsiic
     1141 sndalfyfvf fypfpifgil iitillvrfk srnssknsdg kngvpllwik ephlnysptc
     1201 leppvlsihp gaid
//
LOCUS       NP_060290                876 aa            linear   PRI 27-APR-2025
DEFINITION  exonuclease mut-7 homolog isoform a [Homo sapiens].
ACCESSION   NP_060290
VERSION     NP_060290.3
DBSOURCE    REFSEQ: accession NM_017820.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 876)
  AUTHORS   Sun,D., Liu,M., Huang,F. and Huang,F.
  TITLE     [Bioinformatics analysis of expression and function of EXD3 gene in
            gastric cancer]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 39 (2), 215-221 (2019)
   PUBMED   30890511
  REMARK    GeneRIF: EXD3 may be a potential oncogene in gastric cancer
            possibly in relation to DNA damage repair. The up-regulation of
            EXD3 plays an important role in the development and prognosis of
            gastric cancer, and may serve as an important indicator for
            prognostic evaluation of the patients.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK094438.1, HM005438.1, AL536907.3, BX322799.22, BC131749.1 and
            AI682614.1.
            
            On Apr 14, 2007 this sequence version replaced NP_060290.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005438.1, AK094438.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340951.9/ ENSP00000340474.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..876
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..876
                     /product="exonuclease mut-7 homolog isoform a"
                     /note="exonuclease 3'-5' domain-containing protein 3;
                     exonuclease mut-7 homolog; testicular tissue protein Li
                     125; nibbler homolog"
                     /calculated_mol_wt=96467
     Region          373..568
                     /region_name="mut-7_like_exo"
                     /note="DEDDy 3'-5' exonuclease domain of Caenorhabditis
                     elegans mut-7 and similar proteins; cd06146"
                     /db_xref="CDD:176655"
     Site            order(399..402,463..464,466..468,517..518,551,555)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176655"
     Site            order(399,401,468,551,555)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176655"
     Site            order(400..402,463..464,466..467,517..518,551,555)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176655"
     Region          578..607
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9H8.3)"
     Region          631..864
                     /region_name="Mut7-C"
                     /note="Mut7-C RNAse domain; cl19501"
                     /db_xref="CDD:473177"
     Region          751..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9H8.3)"
     CDS             1..876
                     /gene="EXD3"
                     /gene_synonym="mut-7; Nbr"
                     /coded_by="NM_017820.5:97..2727"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS48066.1"
                     /db_xref="GeneID:54932"
                     /db_xref="HGNC:HGNC:26023"
                     /db_xref="MIM:620859"
ORIGIN      
        1 mdpgdpagdp aagerhrmgr dpllllqalq tlwstrerkq lreeawrgfa alddplagll
       61 dmlescrgqr gegpslaawi shqlqcwlqa qpcpslaqhs lrlkqlqara vkvltespps
      121 laaplasifq lqdadrscll ahvhrlhheg rfreaatlga tlklqselgv ekmsiplllq
      181 dkvalveryv agfpdlqrrl lvlmdswcqp gfdikdvarr ypevtslsle klspkalsrq
      241 vlrlqerygv apalcpnaai qqrlaalrhl chkrfveksl sqenwtdhvq glvgqspwlq
      301 eqlsqllvsh sdpvtaaqca melllpeerl paavavelrr frlqgratea dsrlevkdmk
      361 dryyqlpipr envhllaswe dltrhegall qchqvvgvdv ewtpvfvagg rprpsllqva
      421 veghvflldv lalsqpptgq gaqafsrlva qllsdpsitk lgygmvgdlq klgtscpala
      481 hvekqilggm dlllvhrqmr vasvpapavd rarelrglsl lvqqvlgtal dktqqlsnwd
      541 rrplceeqvi yaaadaycll evhqalcrep arfhlsedla gsrrprhrer pgarkppglq
      601 kasapaaprq vpvavavseg aapqiparaf rvvcdnmlqg larslrclgv darmlgnged
      661 hrraaevarq egriiltsgq pfhklraqvg agrclsvdcs lkaqqqakav lkhfnvrvth
      721 adifsrcqac ncdqylkvsr dmmkqlmwls shqegprssg deatqsqavq epgpapdaap
      781 egctydrpcr wlqmadlrae tpdmladgtr lqlagvpvgv lrtpglrcfy cctgcgkvfw
      841 dgshlgrvat hfrdmlesap spcepspaps passpf
//
LOCUS       NP_006769                481 aa            linear   PRI 27-APR-2025
DEFINITION  tripartite motif-containing protein 10 isoform 1 [Homo sapiens].
ACCESSION   NP_006769
VERSION     NP_006769.2
DBSOURCE    REFSEQ: accession NM_006778.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Guo,M., Cao,W., Chen,S., Tian,R., Wang,L., Liu,Q., Zhang,L.,
            Wang,Z., Zhao,M., Lu,Q. and Zhu,H.
  TITLE     TRIM10 binds to IFN-alpha/beta receptor 1 to negatively regulate
            type I IFN signal transduction
  JOURNAL   Eur J Immunol 51 (7), 1762-1773 (2021)
   PUBMED   33811647
  REMARK    GeneRIF: TRIM10 binds to IFN-alpha/beta receptor 1 to negatively
            regulate type I IFN signal transduction.
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Xi,X., Bao,Y., Zhou,Y., Chen,Y., Zhong,X., Liao,J., Zhou,J., Xu,S.,
            Cao,Z., Hu,K., Hu,Y., He,X., Zhou,L., Lin,H. and Wu,Q.
  TITLE     Oncogenic gene TRIM10 confers resistance to cisplatin in
            osteosarcoma cells and activates the NF-kappaB signaling pathway
  JOURNAL   Cell Biol Int 45 (1), 74-82 (2021)
   PUBMED   32997424
  REMARK    GeneRIF: Oncogenic gene TRIM10 confers resistance to cisplatin in
            osteosarcoma cells and activates the NF-kappaB signaling pathway.
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Orimo,A., Yamagishi,T., Tominaga,N., Yamauchi,Y., Hishinuma,T.,
            Okada,K., Suzuki,M., Sato,M., Nogi,Y., Suzuki,H., Inoue,S.,
            Yoshimura,K., Shimizu,Y. and Muramatsu,M.
  TITLE     Molecular cloning of testis-abundant finger Protein/Ring finger
            protein 23 (RNF23), a novel RING-B box-coiled coil-B30.2 protein on
            the class I region of the human MHC
  JOURNAL   Biochem Biophys Res Commun 276 (1), 45-51 (2000)
   PUBMED   11006080
REFERENCE   8  (residues 1 to 481)
  AUTHORS   Harada,H., Harada,Y., O'Brien,D.P., Rice,D.S., Naeve,C.W. and
            Downing,J.R.
  TITLE     HERF1, a novel hematopoiesis-specific RING finger protein, is
            required for terminal differentiation of erythroid cells
  JOURNAL   Mol Cell Biol 19 (5), 3808-3815 (1999)
   PUBMED   10207104
REFERENCE   9  (residues 1 to 481)
  AUTHORS   Henry,J., Ribouchon,M., Depetris,D., Mattei,M., Offer,C.,
            Tazi-Ahnini,R. and Pontarotti,P.
  TITLE     Cloning, structural analysis, and mapping of the B30 and B7
            multigenic families to the major histocompatibility complex (MHC)
            and other chromosomal regions
  JOURNAL   Immunogenetics 46 (5), 383-395 (1997)
   PUBMED   9271628
REFERENCE   10 (residues 1 to 481)
  AUTHORS   Goei,V.L., Parimoo,S., Capossela,A., Chu,T.W. and Gruen,J.R.
  TITLE     Isolation of novel non-HLA gene fragments from the hemochromatosis
            region (6p21.3) by cDNA hybridization selection
  JOURNAL   Am J Hum Genet 54 (2), 244-251 (1994)
   PUBMED   8304341
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL669914.2, BC093926.1 and AL360163.1.
            
            On Sep 22, 2007 this sequence version replaced NP_006769.1.
            
            Summary: The protein encoded by this gene is a member of the
            tripartite motif (TRIM) family. The TRIM motif includes three
            zinc-binding domains, a RING, a B-box type 1 and a B-box type 2,
            and a coiled-coil region. This protein localizes to cytoplasmic
            bodies. Studies in mice suggest that this protein plays a role in
            terminal differentiation of erythroid cells. Alternate splicing of
            this gene generates two transcript variants encoding different
            isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform 1, which has a
            distinct C-terminus and is 86 aa longer than isoform 2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence consistent with
            the reference genome assembly was not available for all regions of
            the RefSeq transcript. The extent of this transcript is supported
            by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF220122.1, BX405576.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000449742.7/ ENSP00000397073.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..481
                     /product="tripartite motif-containing protein 10 isoform
                     1"
                     /note="hematopoietic RING finger 1; ring finger protein 9;
                     tripartite motif protein 10; tripartite motif-containing
                     protein 10; Zn-finger protein; B30-RING finger protein"
                     /calculated_mol_wt=54906
     Region          9..69
                     /region_name="RING-HC_TRIM10_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 10 (TRIM10) and similar proteins;
                     cd16593"
                     /db_xref="CDD:438255"
     Region          97..135
                     /region_name="Bbox_SF"
                     /note="B-box-type zinc finger superfamily; cl00034"
                     /db_xref="CDD:469587"
     Region          143..>217
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          309..480
                     /region_name="SPRY_PRY_TRIM10"
                     /note="PRY/SPRY domain of tripartite motif-binding protein
                     10 (TRIM10) also known as hematopoietic RING finger 1
                     (HERF1); cd15827"
                     /db_xref="CDD:293999"
     CDS             1..481
                     /gene="TRIM10"
                     /gene_synonym="HERF1; RFB30; RNF9"
                     /coded_by="NM_006778.4:354..1799"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34375.1"
                     /db_xref="GeneID:10107"
                     /db_xref="HGNC:HGNC:10072"
                     /db_xref="MIM:605701"
ORIGIN      
        1 masaasvtsl adevncpicq gtlrepvtid cghnfcracl tryceipgpd leesptcplc
       61 kepfrpgsfr pnwqlanvve nierlqlvst lglgeedvcq ehgekiyffc eddemqlcvv
      121 creagehath tmrfledaaa pyreqihkcl kclrkereei qeiqsrenkr mqvlltqvst
      181 krqqvisefa hlrkfleeqq sillaqlesq dgdilrqrde fdllvageic rfsalieele
      241 eknerparel ltdirstlir cetrkcrkpv avspelgqri rdfpqqalpl qremkmflek
      301 lcfeldyepa hisldpqtsh pklllsedhq raqfsykwqn spdnpqrfdr atcvlahtgi
      361 tggrhtwvvs idlahggsct vgvvsedvqr kgelrlrpee gvwavrlawg fvsalgsfpt
      421 rltlkeqprq vrvsldyevg wvtftnavtr epiytftasf trkvipffgl wgrgssfsls
      481 s
//
LOCUS       NP_060943                140 aa            linear   PRI 27-APR-2025
DEFINITION  acyl-coenzyme A thioesterase 13 isoform 1 [Homo sapiens].
ACCESSION   NP_060943
VERSION     NP_060943.1
DBSOURCE    REFSEQ: accession NM_018473.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Wang,B., Yang,Q., Che,L., Sun,L. and Du,N.
  TITLE     Acyl-CoA thioesterase 13 (ACOT13) attenuates the progression of
            autosomal dominant polycystic kidney disease in vitro via
            triggering mitochondrial-related cell apoptosis
  JOURNAL   Aging (Albany NY) 16 (16), 11877-11892 (2024)
   PUBMED   39172111
  REMARK    GeneRIF: Acyl-CoA thioesterase 13 (ACOT13) attenuates the
            progression of autosomal dominant polycystic kidney disease in
            vitro via triggering mitochondrial-related cell apoptosis.
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Du,N., Dong,D., Sun,L., Che,L., Li,X., Liu,Y. and Wang,B.
  TITLE     Identification of ACOT13 and PTGER2 as novel candidate genes of
            autosomal dominant polycystic kidney disease through whole exome
            sequencing
  JOURNAL   Eur J Med Res 26 (1), 142 (2021)
   PUBMED   34886911
  REMARK    GeneRIF: Identification of ACOT13 and PTGER2 as novel candidate
            genes of autosomal dominant polycystic kidney disease through whole
            exome sequencing.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Kanno,K., Wu,M.K., Agate,D.S., Fanelli,B.J., Wagle,N., Scapa,E.F.,
            Ukomadu,C. and Cohen,D.E.
  TITLE     Interacting proteins dictate function of the minimal START domain
            phosphatidylcholine transfer protein/StarD2
  JOURNAL   J Biol Chem 282 (42), 30728-30736 (2007)
   PUBMED   17704541
  REMARK    GeneRIF: Yeast two-hybrid screening using libraries prepared from
            mouse liver and embryo identified Them2 (thioesterase superfamily
            member 2) and the homeodomain transcription factor Pax3 (paired box
            gene 3), respectively, as PC-TP-interacting proteins.
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Cheng,Z., Bao,S., Shan,X., Xu,H. and Gong,W.
  TITLE     Human thioesterase superfamily member 2 (hTHEM2) is co-localized
            with beta-tubulin onto the microtubule
  JOURNAL   Biochem Biophys Res Commun 350 (4), 850-853 (2006)
   PUBMED   17045243
  REMARK    GeneRIF: Small interference RNA silencing in cell line HCT116 shows
            that the hthem2 gene is essential for the cell sustained
            proliferation.
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Cheng,Z., Song,F., Shan,X., Wei,Z., Wang,Y., Dunaway-Mariano,D. and
            Gong,W.
  TITLE     Crystal structure of human thioesterase superfamily member 2
  JOURNAL   Biochem Biophys Res Commun 349 (1), 172-177 (2006)
   PUBMED   16934754
  REMARK    GeneRIF: analysis of human thioesterase superfamily member 2
            crystal structure
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB214267.1, BC000894.1,
            AL031775.1 and CB852340.1.
            
            Summary: This gene encodes a member of the thioesterase
            superfamily. In humans, the protein co-localizes with microtubules
            and is essential for sustained cell proliferation. The orthologous
            mouse protein forms a homotetramer and is associated with
            mitochondria. The mouse protein functions as a medium- and
            long-chain acyl-CoA thioesterase. Multiple transcript variants
            encoding different isoforms have been found for this gene.[provided
            by RefSeq, May 2009].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript but encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA893550.1, SRR1803614.16882.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000230048.5/ ENSP00000230048.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.3"
     Protein         1..140
                     /product="acyl-coenzyme A thioesterase 13 isoform 1"
                     /EC_number="3.1.2.2"
                     /note="thioesterase superfamily member 2; hypothalamus
                     protein HT012; acyl-coenzyme A thioesterase 13;
                     palmitoyl-CoA hydrolase; hotdog-fold thioesterase
                     superfamily member 2"
                     /calculated_mol_wt=14829
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (Q9NPJ3.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in Acyl-coenzyme A thioesterase
                     13, N-terminally processed.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9NPJ3.1)"
     Region          25..138
                     /region_name="PaaI_thioesterase"
                     /note="PaaI_thioesterase is a tetrameric acyl-CoA
                     thioesterase with a hot dog fold and one of several
                     proteins responsible for phenylacetic acid (PA)
                     degradation in bacteria. Although orthologs of PaaI exist
                     in archaea and eukaryotes, their function has not...;
                     cd03443"
                     /db_xref="CDD:239527"
     Site            27
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQR4; propagated from
                     UniProtKB/Swiss-Prot (Q9NPJ3.1)"
     Site            37
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQR4; propagated from
                     UniProtKB/Swiss-Prot (Q9NPJ3.1)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQR4; propagated from
                     UniProtKB/Swiss-Prot (Q9NPJ3.1)"
     Site            order(55,83,90..93)
                     /site_type="other"
                     /note="CoenzymeA binding site [chemical binding]"
                     /db_xref="CDD:239527"
     Site            order(56,58,61,84..88,90)
                     /site_type="other"
                     /note="subunit interaction site [polypeptide binding]"
                     /db_xref="CDD:239527"
     Site            order(57,65..66,69..70,83)
                     /site_type="active"
                     /note="PHB binding site [active]"
                     /db_xref="CDD:239527"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQR4; propagated from
                     UniProtKB/Swiss-Prot (Q9NPJ3.1)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQR4; propagated from
                     UniProtKB/Swiss-Prot (Q9NPJ3.1)"
     CDS             1..140
                     /gene="ACOT13"
                     /gene_synonym="HT012; PNAS-27; THEM2"
                     /coded_by="NM_018473.4:188..610"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4558.1"
                     /db_xref="GeneID:55856"
                     /db_xref="HGNC:HGNC:20999"
                     /db_xref="MIM:615652"
ORIGIN      
        1 mtsmtqslre vikamtkarn fervlgkitl vsaapgkvic emkveeehtn aigtlhgglt
       61 atlvdnistm allctergap gvsvdmnity mspaklgedi vitahvlkqg ktlaftsvdl
      121 tnkatgklia qgrhtkhlgn
//
LOCUS       NP_057077                182 aa            linear   PRI 27-APR-2025
DEFINITION  plasmolipin [Homo sapiens].
ACCESSION   NP_057077
VERSION     NP_057077.1
DBSOURCE    REFSEQ: accession NM_015993.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Azzaz,F., Mazzarino,M., Chahinian,H., Yahi,N., Scala,C.D. and
            Fantini,J.
  TITLE     Structure of the Myelin Sheath Proteolipid Plasmolipin (PLLP) in a
            Ganglioside-Containing Lipid Raft
  JOURNAL   Front Biosci (Landmark Ed) 28 (8), 157 (2023)
   PUBMED   37664934
  REMARK    GeneRIF: Structure of the Myelin Sheath Proteolipid Plasmolipin
            (PLLP) in a Ganglioside-Containing Lipid Raft.
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Zheng,P., Sun,S., Wang,J., Cheng,Z.J., Lei,K.C., Xue,M., Zhang,T.,
            Huang,H., Zhang,X.D. and Sun,B.
  TITLE     Integrative omics analysis identifies biomarkers of idiopathic
            pulmonary fibrosis
  JOURNAL   Cell Mol Life Sci 79 (1), 66 (2022)
   PUBMED   35015148
  REMARK    GeneRIF: Integrative omics analysis identifies biomarkers of
            idiopathic pulmonary fibrosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Cacho-Navas,C., Reglero-Real,N., Colas-Algora,N., Barroso,S., de
            Rivas,G., Stamatakis,K., Feito,J., Andres,G., Fresno,M., Kremer,L.,
            Correas,I., Alonso,M.A. and Millan,J.
  TITLE     Plasmolipin regulates basolateral-to-apical transcytosis of ICAM-1
            and leukocyte adhesion in polarized hepatic epithelial cells
  JOURNAL   Cell Mol Life Sci 79 (1), 61 (2022)
   PUBMED   34999972
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Yaffe,Y., Hugger,I., Yassaf,I.N., Shepshelovitch,J., Sklan,E.H.,
            Elkabetz,Y., Yeheskel,A., Pasmanik-Chor,M., Benzing,C.,
            Macmillan,A., Gaus,K., Eshed-Eisenbach,Y., Peles,E. and
            Hirschberg,K.
  TITLE     The myelin proteolipid plasmolipin forms oligomers and induces
            liquid-ordered membranes in the Golgi complex
  JOURNAL   J Cell Sci 128 (13), 2293-2302 (2015)
   PUBMED   26002055
  REMARK    GeneRIF: These data support a model in which PLLP functions in
            myelin biogenesis through organization of myelin liquid-ordered
            membranes in the Golgi complex.
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Byrne,E.M., Gehrman,P.R., Medland,S.E., Nyholt,D.R., Heath,A.C.,
            Madden,P.A., Hickie,I.B., Van Duijn,C.M., Henders,A.K.,
            Montgomery,G.W., Martin,N.G. and Wray,N.R.
  CONSRTM   Chronogen Consortium
  TITLE     A genome-wide association study of sleep habits and insomnia
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 162B (5), 439-451 (2013)
   PUBMED   23728906
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Hamacher,M., Pippirs,U., Kohler,A., Muller,H.W. and Bosse,F.
  TITLE     Plasmolipin: genomic structure, chromosomal localization, protein
            expression pattern, and putative association with Bardet-Biedl
            syndrome
  JOURNAL   Mamm Genome 12 (12), 933-937 (2001)
   PUBMED   11707781
REFERENCE   8  (residues 1 to 182)
  AUTHORS   Fischer,I. and Sapirstein,V.S.
  TITLE     Molecular cloning of plasmolipin. Characterization of a novel
            proteolipid restricted to brain and kidney
  JOURNAL   J Biol Chem 269 (40), 24912-24919 (1994)
   PUBMED   7929173
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA366260.1 and BC002760.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1100809.1,
                                           SRR3476690.131888.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153733 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219207.10/ ENSP00000219207.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..182
                     /product="plasmolipin"
                     /note="transmembrane 4 superfamily member 11
                     (plasmolipin); plasma membrane proteolipid (plasmolipin)"
                     /calculated_mol_wt=19856
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y342.1)"
     Region          32..160
                     /region_name="MARVEL"
                     /note="Membrane-associating domain; pfam01284"
                     /db_xref="CDD:366555"
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y342.1)"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y342.1)"
     Site            100..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y342.1)"
     Site            142..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y342.1)"
     CDS             1..182
                     /gene="PLLP"
                     /gene_synonym="PMLP; TM4SF11"
                     /coded_by="NM_015993.3:133..681"
                     /db_xref="CCDS:CCDS10777.1"
                     /db_xref="GeneID:51090"
                     /db_xref="HGNC:HGNC:18553"
                     /db_xref="MIM:600340"
ORIGIN      
        1 maefpskvst rtsspaqgae asvsalrpdl gfvrsrlgal mllqlvlgll vwaliadtpy
       61 hlypaygwvm fvavflwlvt ivlfnlylfq lhmklymvpw plvlmifnis atvlyitafi
      121 acsaavdlts lrgtrpynqr aaasffaclv miaygvsaff syqawrgvgs naatsqmagg
      181 ya
//
LOCUS       NP_079533                710 aa            linear   PRI 27-APR-2025
DEFINITION  choline transporter-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_079533 NP_116183
VERSION     NP_079533.2
DBSOURCE    REFSEQ: accession NM_025257.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Sabui,S., Anthonymuthu,S., Ramamoorthy,K., Skupsky,J.,
            Jennings,T.S.K., Rahmatpanah,F., Fleckenstein,J.M. and Said,H.M.
  TITLE     Effect of knocking out mouse Slc44a4 on colonic uptake of the
            microbiota-generated thiamine pyrophosphate and colon physiology
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 327 (1), G36-G46 (2024)
   PUBMED   38713615
  REMARK    GeneRIF: Effect of knocking out mouse Slc44a4 on colonic uptake of
            the microbiota-generated thiamine pyrophosphate and colon
            physiology.
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Wu,J., Cheng,Y., Zhang,R., Shen,H., Ma,L., Yang,J., Zhang,Y. and
            Zhang,J.
  TITLE     Evaluating the Association of Common Variants of the SLC44A4 Gene
            with Ulcerative Colitis Susceptibility in the Han Chinese
            Population
  JOURNAL   Genet Test Mol Biomarkers 21 (9), 555-559 (2017)
   PUBMED   28753073
  REMARK    GeneRIF: We found that rs2736428 was significantly associated with
            UC risk (allelic p = 0.0004), and the CT and TT genotypes of
            rs2736428 had a higher distribution compared with the CC genotypes
            (genotypic p = 0.001), suggesting that the T allele was a risk
            allele (odds ratio = 1.45, 95% confidence interval = 1.18-1.78).
            Moreover, one haplotype block that included rs2736428 was found to
            be strongly associated with UC risk as well
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Ma,Z., Xia,W., Liu,F., Ma,J., Sun,S., Zhang,J., Jiang,N., Wang,X.,
            Hu,J. and Ma,D.
  TITLE     SLC44A4 mutation causes autosomal dominant hereditary postlingual
            non-syndromic mid-frequency hearing loss
  JOURNAL   Hum Mol Genet 26 (2), 383-394 (2017)
   PUBMED   28013291
  REMARK    GeneRIF: Whole-exome sequencing revealed SLC44A4, which encodes the
            choline transport protein, as the pathogenic gene in this family.
            In the zebrafish model, downregulation of slc44a4 using morpholinos
            led to significant abnormalities in the zebrafish inner ear and
            lateral line neuromasts and contributed, to some extent, to
            disabilities in hearing and balance.
            Erratum:[Hum Mol Genet. 2017 Aug 15;26(16):3234. doi:
            10.1093/hmg/ddx232. PMID: 28859437]
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Nabokina,S.M., Ramos,M.B. and Said,H.M.
  TITLE     Mechanism(S) Involved in the Colon-Specific Expression of the
            Thiamine Pyrophosphate (Tpp) Transporter
  JOURNAL   PLoS One 11 (2), e0149255 (2016)
   PUBMED   26901654
  REMARK    GeneRIF: epigenetic mechanisms (histone modifications) play a role
            in determining the tissue-specific pattern of expression of the
            TPPT along the GI tract.
            Erratum:[PLoS One. 2017 Oct 11;12(10):e0186550. doi:
            10.1371/journal.pone.0186550. PMID: 29020075]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Gupta,A., Juyal,G., Sood,A., Midha,V., Yamazaki,K., Vich Vila,A.,
            Esaki,M., Matsui,T., Takahashi,A., Kubo,M., Weersma,R.K. and
            Thelma,B.K.
  TITLE     A cross-ethnic survey of CFB and SLC44A4, Indian ulcerative colitis
            GWAS hits, underscores their potential role in disease
            susceptibility
  JOURNAL   Eur J Hum Genet 25 (1), 111-122 (2016)
   PUBMED   27759029
  REMARK    GeneRIF: These results suggest (i) apparent allelic heterogeneity
            in CFB and genetic heterogeneity in SLC44A4 across different ethnic
            groups; (ii) shared ulcerative colitis genetic etiological factors
            among Asians
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Xie,T., Rowen,L., Aguado,B., Ahearn,M.E., Madan,A., Qin,S.,
            Campbell,R.D. and Hood,L.
  TITLE     Analysis of the gene-dense major histocompatibility complex class
            III region and its comparison to mouse
  JOURNAL   Genome Res 13 (12), 2621-2636 (2003)
   PUBMED   14656967
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   8  (residues 1 to 710)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 710)
  AUTHORS   Uhl,J., Penzel,R., Sergi,C., Kopitz,J., Otto,H.F. and Cantz,M.
  TITLE     Identification of a CTL4/Neu1 fusion transcript in a sialidosis
            patient
  JOURNAL   FEBS Lett 521 (1-3), 19-23 (2002)
   PUBMED   12067718
REFERENCE   10 (residues 1 to 710)
  AUTHORS   O'Regan,S., Traiffort,E., Ruat,M., Cha,N., Compaore,D. and
            Meunier,F.M.
  TITLE     An electric lobe suppressor for a yeast choline transport mutation
            belongs to a new family of transporter-like proteins
  JOURNAL   Proc Natl Acad Sci U S A 97 (4), 1835-1840 (2000)
   PUBMED   10677542
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC300771.1, BC014659.1,
            AK222998.1, DA924720.1 and AI560195.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jun 6, 2007 this sequence version replaced
            NP_116183.1, NP_079533.1.
            
            Summary: The protein encoded by this gene may be a sodium-dependent
            transmembrane transport protein involved in the uptake of choline
            by cholinergic neurons. Defects in this gene can cause sialidosis,
            a lysosomal storage disease. Three transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, May 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027397.1, BC014659.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000229729.11/ ENSP00000229729.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..710
                     /product="choline transporter-like protein 4 isoform 1"
                     /note="choline transporter-like protein 4; testicular
                     tissue protein Li 48; thiamine pyrophosphate transporter
                     1"
                     /calculated_mol_wt=79123
     Site            35..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            69
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26828122; propagated from
                     UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26828122; propagated from
                     UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26828122; propagated from
                     UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            230..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            253..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            308
                     /site_type="other"
                     /note="Breakpoint for translocation with NEU1; propagated
                     from UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            310..330
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GD3.2)"
     Region          314..675
                     /region_name="Choline_transpo"
                     /note="Plasma-membrane choline transporter; pfam04515"
                     /db_xref="CDD:461337"
     Site            359..379
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26828122; propagated from
                     UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            405
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            416
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26828122; propagated from
                     UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            456..476
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            502..522
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            561..581
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            598..618
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GD3.2)"
     Site            639..659
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GD3.2)"
     CDS             1..710
                     /gene="SLC44A4"
                     /gene_synonym="C6orf29; CTL4; DFNA72; hTPPT1; NG22; TPPT"
                     /coded_by="NM_025257.3:18..2150"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4724.2"
                     /db_xref="GeneID:80736"
                     /db_xref="HGNC:HGNC:13941"
                     /db_xref="MIM:606107"
ORIGIN      
        1 mggkqrdedd eaygkpvkyd psfrgpiknr sctdviccvl fllfilgyiv vgivawlygd
       61 prqvlyprns tgaycgmgen kdkpyllyfn ifscilssni isvaenglqc ptpqvcvssc
      121 pedpwtvgkn efsqtvgevf ytknrnfclp gvpwnmtvit slqqelcpsf llpsapalgr
      181 cfpwtnvtpp alpgitndtt iqqgisglid slnardisvk ifedfaqswy wilvalgval
      241 vlsllfilll rlvagplvlv lilgvlgvla ygiyycweey rvlrdkgasi sqlgfttnls
      301 ayqsvqetwl aalivlavle ailllmlifl rqririaial lkeaskavgq mmstmfyplv
      361 tfvlllicia ywamtalyla tsgqpqyvlw asnisspgce kvpintscnp tahlvnsscp
      421 glmcvfqgys skgliqrsvf nlqiygvlgl fwtlnwvlal gqcvlagafa sfywafhkpq
      481 diptfplisa firtlryhtg slafgalilt lvqiarvile yidhklrgvq npvarcimcc
      541 fkcclwclek fikflnrnay imiaiygknf cvsaknafml lmrnivrvvv ldkvtdlllf
      601 fgkllvvggv gvlsffffsg ripglgkdfk sphlnyywlp imtsilgayv iasgffsvfg
      661 mcvdtlflcf ledlernngs ldrpyymsks llkilgkkne appdnkkrkk
//
LOCUS       NP_057062                835 aa            linear   PRI 27-APR-2025
DEFINITION  serine/threonine-protein kinase TNNI3K [Homo sapiens].
ACCESSION   NP_057062
VERSION     NP_057062.1
DBSOURCE    REFSEQ: accession NM_015978.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Pham,C., Koopmann,T.T., Vinocur,J.M., Blom,N.A., Nogueira
            Silbiger,V., Mittal,K., Bootsma,M., Palm,K.C.A., Clur,S.B.,
            Barge-Schaapveld,D.Q.C.M., Hamilton,R.M. and Lodder,E.M.
  TITLE     Reduced kinase function in two ultra-rare TNNI3K variants in
            families with congenital junctional ectopic tachycardia
  JOURNAL   Clin Genet 106 (1), 37-46 (2024)
   PUBMED   38424693
  REMARK    GeneRIF: Reduced kinase function in two ultra-rare TNNI3K variants
            in families with congenital junctional ectopic tachycardia.
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Ramzan,S., Tennstedt,S., Tariq,M., Khan,S., Noor Ul Ayan,H.,
            Ali,A., Munz,M., Thiele,H., Korejo,A.A., Mughal,A.R., Jamal,S.Z.,
            Nurnberg,P., Baig,S.M., Erdmann,J. and Ahmad,I.
  TITLE     A Novel Missense Mutation in TNNI3K Causes Recessively Inherited
            Cardiac Conduction Disease in a Consanguineous Pakistani Family
  JOURNAL   Genes (Basel) 12 (8), 1282 (2021)
   PUBMED   34440456
  REMARK    GeneRIF: A Novel Missense Mutation in TNNI3K Causes Recessively
            Inherited Cardiac Conduction Disease in a Consanguineous Pakistani
            Family.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Touat-Hamici,Z., Blancard,M., Ma,R., Lin,L., Iddir,Y., Denjoy,I.,
            Leenhardt,A., Yuchi,Z. and Guicheney,P.
  TITLE     A SPRY1 domain cardiac ryanodine receptor variant associated with
            short-coupled torsade de pointes
  JOURNAL   Sci Rep 11 (1), 5243 (2021)
   PUBMED   33664309
  REMARK    GeneRIF: A SPRY1 domain cardiac ryanodine receptor variant
            associated with short-coupled torsade de pointes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Liu,J., Liu,D., Li,M., Wu,K., Liu,N., Zhao,C., Shi,X. and Liu,Q.
  TITLE     Identification of a nonsense mutation in TNNI3K associated with
            cardiac conduction disease
  JOURNAL   J Clin Lab Anal 34 (9), e23418 (2020)
   PUBMED   32529721
  REMARK    GeneRIF: Identification of a nonsense mutation in TNNI3K associated
            with cardiac conduction disease.
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Lai,Z.F., Chen,Y.Z., Feng,L.P., Meng,X.M., Ding,J.F., Wang,L.Y.,
            Ye,J., Li,P., Cheng,X.S., Kitamoto,Y., Monzen,K., Komuro,I.,
            Sakaguchi,N. and Kim-Mitsuyama,S.
  TITLE     Overexpression of TNNI3K, a cardiac-specific MAP kinase, promotes
            P19CL6-derived cardiac myogenesis and prevents myocardial
            infarction-induced injury
  JOURNAL   Am J Physiol Heart Circ Physiol 295 (2), H708-H716 (2008)
   PUBMED   18552163
  REMARK    GeneRIF: TNNI3K promotes cardiomyogenesis, enhances cardiac
            performance, and protects the myocardium from ischemic injury by
            suppressing p38/JNK-mediated apoptosis.
            Erratum:[Am J Physiol Heart Circ Physiol. 2008 Oct;295(4):H815]
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Feng,Y., Liu,D.Q., Wang,Z., Liu,Z., Cao,H.Q., Wang,L.Y., Shi,N. and
            Meng,X.M.
  TITLE     AOP-1 interacts with cardiac-specific protein kinase TNNI3K and
            down-regulates its kinase activity
  JOURNAL   Biochemistry (Mosc) 72 (11), 1199-1204 (2007)
   PUBMED   18205602
  REMARK    GeneRIF: coexpression of AOP-1 inhibited TNNI3K kinase activity
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Feng,Y., Cao,H.Q., Liu,Z., Ding,J.F. and Meng,X.M.
  TITLE     Identification of the dual specificity and the functional domains
            of the cardiac-specific protein kinase TNNI3K
  JOURNAL   Gen Physiol Biophys 26 (2), 104-109 (2007)
   PUBMED   17660584
  REMARK    GeneRIF: TNNI3K exhibits dual-specific kinase activity and forms
            dimers or oligomers that may be necessary for its activation
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Zhao,Y., Meng,X.M., Wei,Y.J., Zhao,X.W., Liu,D.Q., Cao,H.Q.,
            Liew,C.C. and Ding,J.F.
  TITLE     Cloning and characterization of a novel cardiac-specific kinase
            that interacts specifically with cardiac troponin I
  JOURNAL   J Mol Med (Berl) 81 (5), 297-304 (2003)
   PUBMED   12721663
  REMARK    GeneRIF: cloning of TNNI3K which interacts specifically with
            cardiac troponin I; data suggest that TNNI3K is a cardiac-specific
            kinase and plays important roles in the cardiac system
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX502807.1, BC113539.1 and
            AA758546.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that belongs to the MAP kinase
            kinase kinase (MAPKKK) family of protein kinases. The protein
            contains ankyrin repeat, protein kinase and serine-rich domains and
            is thought to play a role in cardiac physiology. [provided by
            RefSeq, Sep 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF116826.1, AY303691.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151741, SAMEA2154361
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326637.8/ ENSP00000322251.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..835
                     /product="serine/threonine-protein kinase TNNI3K"
                     /EC_number="2.7.11.1"
                     /note="cardiac ankyrin repeat kinase; cardiac troponin
                     I-interacting kinase"
                     /calculated_mol_wt=92720
     Region          54..290
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          66..98
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          66..96
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     Region          100..131
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          100..129
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     Region          133..162
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     Region          134..164
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(135,139..140,143..145,147..148,152,155,164,166,168,
                     172..173,176..178,180..181,185,188,197,199,201,205..206,
                     209..211,213..214,218,221,232)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          166..197
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          166..195
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     Region          199..232
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          199..228
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     Region          234..263
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     Region          234..262
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(269,271,275..276,279..281,283..284,288,291,302,304,
                     306,310..311,314..316,319..320,324,328,337,339,341,
                     345..346,349..351,353..354,358,361)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          269..302
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          269..298
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     Region          304..337
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          304..335
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     Region          309..401
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          339..369
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          339..368
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     Region          381..410
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     Region          469..722
                     /region_name="PKc_TNNI3K"
                     /note="Catalytic domain of the Dual-specificity protein
                     kinase, TNNI3-interacting kinase; cd14064"
                     /db_xref="CDD:270966"
     Site            order(469..473,477,488,490,522,539..542,546,548,588,590,
                     592..593,595,606,609,626..629)
                     /site_type="active"
                     /db_xref="CDD:270966"
     Site            order(469..473,477,488,490,522,539..542,546,588,590,
                     592..593,595,606)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270966"
     Site            order(473,546,548,588,590,592,609,626..629)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270966"
     Site            605..629
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270966"
     Region          732..751
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q59H18.3)"
     CDS             1..835
                     /gene="TNNI3K"
                     /gene_synonym="CARK; CCDD"
                     /coded_by="NM_015978.3:66..2573"
                     /db_xref="CCDS:CCDS664.1"
                     /db_xref="GeneID:51086"
                     /db_xref="HGNC:HGNC:19661"
                     /db_xref="MIM:613932"
ORIGIN      
        1 mgnyksrptq tctdewkkkv sesyvitier leddlqikek eltelrnifg sdeafskvnl
       61 nyrtenglsl lhlccicggk kshirtlmlk glrpsrltrn gftalhlavy kdnaelitsl
      121 lhsgadiqqv gyggltalhi atiaghleaa dvllqhganv niqdavfftp lhiaayyghe
      181 qvtrlllkfg advnvsgevg drplhlasak gflniakllm eegskadvna qdnedhvplh
      241 fcsrfghhdi vkyllqsdle vqphvvniyg dtplhlacyn gkfevakeii qisgtesltk
      301 enifsetafh sactygksid lvkflldqnv ininhqgrdg htglhsacyh ghirlvqfll
      361 dngadmnlva cdpsrssgek deqtclmway ekghdaivtl lkhykrpqde lpcneysqpg
      421 gdgsyvsvps plgkiksmtk ekadilllra glpshfhlql seiefheiig sgsfgkvykg
      481 rcrnkivaik ryrantycsk sdvdmfcrev silcqlnhpc viqfvgacln dpsqfaivtq
      541 yisggslfsl lheqkrildl qskliiavdv akgmeylhnl tqpiihrdln shnillyedg
      601 havvadfges rflqsldedn mtkqpgnlrw mapevftqct rytikadvfs yalclweilt
      661 geipfahlkp aaaaadmayh hirppigysi pkpissllir gwnacpegrp efsevvmkle
      721 eclcnielms passnssgsl spssssdclv nrggpgrshv aalrsrfele yalnarsyaa
      781 lsqsagqyss qglsleemkr slqytpidky gyvsdpmssm hfhscrnsss fedss
//
LOCUS       NP_001346956             383 aa            linear   ROD 27-APR-2025
DEFINITION  dematin isoform 2 [Mus musculus].
ACCESSION   NP_001346956 XP_017171328
VERSION     NP_001346956.1
DBSOURCE    REFSEQ: accession NM_001360027.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Huang,S., Reed,C., Ilsley,M., Magor,G., Tallack,M., Landsberg,M.,
            Mitchell,H., Gillinder,K. and Perkins,A.
  TITLE     Mutations in linker-2 of KLF1 impair expression of membrane
            transporters and cytoskeletal proteins causing hemolysis
  JOURNAL   Nat Commun 15 (1), 7019 (2024)
   PUBMED   39147774
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Fritz,D.I., Ding,Y., Merrill-Skoloff,G., Flaumenhaft,R., Hanada,T.
            and Chishti,A.H.
  TITLE     Dematin Regulates Calcium Mobilization, Thrombosis, and Early Akt
            Activation in Platelets
  JOURNAL   Mol Cell Biol 43 (6), 283-299 (2023)
   PUBMED   37216480
  REMARK    GeneRIF: Dematin Regulates Calcium Mobilization, Thrombosis, and
            Early Akt Activation in Platelets.
REFERENCE   3  (residues 1 to 383)
  AUTHORS   O'Neil,S.D., Racz,B., Brown,W.E., Gao,Y., Soderblom,E.J., Yasuda,R.
            and Soderling,S.H.
  TITLE     Action potential-coupled Rho GTPase signaling drives presynaptic
            plasticity
  JOURNAL   Elife 10, e63756 (2021)
   PUBMED   34269176
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Huang,Y.S., Delgadillo,L.F., Cyr,K.H., Kingsley,P.D., An,X.,
            McGrath,K.E., Mohandas,N., Conboy,J.G., Waugh,R.E., Wan,J. and
            Palis,J.
  TITLE     Circulating primitive erythroblasts establish a functional, protein
            4.1R-dependent cytoskeletal network prior to enucleating
  JOURNAL   Sci Rep 7 (1), 5164 (2017)
   PUBMED   28701737
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Lu,Y., Hanada,T., Fujiwara,Y., Nwankwo,J.O., Wieschhaus,A.J.,
            Hartwig,J., Huang,S., Han,J. and Chishti,A.H.
  TITLE     Gene disruption of dematin causes precipitous loss of erythrocyte
            membrane stability and severe hemolytic anemia
  JOURNAL   Blood 128 (1), 93-103 (2016)
   PUBMED   27073223
  REMARK    GeneRIF: results demonstrate that dematin plays a critical role in
            maintaining the fundamental properties of the membrane cytoskeleton
            complex.
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Strehl,S., Glatt,K., Liu,Q.M., Glatt,H. and Lalande,M.
  TITLE     Characterization of two novel protocadherins (PCDH8 and PCDH9)
            localized on human chromosome 13 and mouse chromosome 14
  JOURNAL   Genomics 53 (1), 81-89 (1998)
   PUBMED   9787079
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Cornwall,G.A. and Hsia,N.
  TITLE     ADAM7, a member of the ADAM (a disintegrin and metalloprotease)
            gene family is specifically expressed in the mouse anterior
            pituitary and epididymis
  JOURNAL   Endocrinology 138 (10), 4262-4272 (1997)
   PUBMED   9322939
REFERENCE   8  (residues 1 to 383)
  AUTHORS   Malgaretti,N., Pozzoli,O., Bosetti,A., Corradi,A., Ciarmatori,S.,
            Panigada,M., Bianchi,M.E., Martinez,S. and Consalez,G.G.
  TITLE     Mmot1, a new helix-loop-helix transcription factor gene displaying
            a sharp expression boundary in the embryonic mouse brain
  JOURNAL   J Biol Chem 272 (28), 17632-17639 (1997)
   PUBMED   9211912
REFERENCE   9  (residues 1 to 383)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
REFERENCE   10 (residues 1 to 383)
  AUTHORS   Peters,L.L., Eicher,E.M., Azim,A.C. and Chishti,A.H.
  TITLE     The gene encoding the erythrocyte membrane skeleton protein dematin
            (Epb4.9) maps to mouse chromosome 14
  JOURNAL   Genomics 26 (3), 634-635 (1995)
   PUBMED   7607697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY270342.1, CJ070069.1, AA510592.1, CB527108.1, AK162866.1,
            AK165204.1, BY601680.1 and AI413696.1.
            
            On Jan 25, 2018 this sequence version replaced XP_017171328.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.11278.1,
                                           SRR1660817.133681.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="14"
                     /map="14 36.32 cM"
     Protein         1..383
                     /product="dematin isoform 2"
                     /note="erythrocyte membrane protein band 4.9; erythrocyte
                     protein band 4.9"
                     /calculated_mol_wt=42911
     Region          8..333
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          348..383
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..383
                     /gene="Dmtn"
                     /gene_synonym="dematin; Epb4.9; Epb49"
                     /coded_by="NM_001360027.1:281..1432"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS27259.1"
                     /db_xref="GeneID:13829"
                     /db_xref="MGI:MGI:99670"
ORIGIN      
        1 merlqkqplt spgsvsssrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srecslspks tspppspevw aesrtlgiis qastprttgt
      121 prtslphfhh pettrpdsni ykkppiykqr esvggspqsk hliedliies skfpaaqppd
      181 pnqpakietd ywpcppslav vetewrkrka srkgaeeeee eedddseeei kairerqkee
      241 lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl hsgtsksssl psygrttlsr
      301 lqstefspsg seagspglqi ypyemlvvtn kgrtklppgv drmrlerhls aedfsrvfam
      361 speefgklal wkrnelkkka slf
//
LOCUS       NP_003281                248 aa            linear   PRI 27-APR-2025
DEFINITION  tropomyosin alpha-4 chain isoform Tpm4.2cy [Homo sapiens].
ACCESSION   NP_003281
VERSION     NP_003281.1
DBSOURCE    REFSEQ: accession NM_003290.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Yan,J., Xie,B., Tian,Y., An,W., Peng,Z., Liu,Z., Li,J. and Li,L.
  TITLE     MicroRNA-5195-3p mediated malignant biological behaviour of
            insulin-resistant liver cancer cells via SOX9 and TPM4
  JOURNAL   BMC Cancer 23 (1), 557 (2023)
   PUBMED   37328795
  REMARK    GeneRIF: MicroRNA-5195-3p mediated malignant biological behaviour
            of insulin-resistant liver cancer cells via SOX9 and TPM4.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Guo,Q., Zhao,L., Yan,N., Li,Y., Guo,C., Dang,S., Shen,X., Han,J.
            and Luo,Y.
  TITLE     Integrated pan-cancer analysis and experimental verification of the
            roles of tropomyosin 4 in gastric cancer
  JOURNAL   Front Immunol 14, 1148056 (2023)
   PUBMED   36993958
  REMARK    GeneRIF: Integrated pan-cancer analysis and experimental
            verification of the roles of tropomyosin 4 in gastric cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Luo,A., Lan,X., Qiu,Q., Zhou,Q., Li,J., Wu,M., Liu,P., Zhang,H.,
            Lu,B., Lu,Y. and Lu,W.
  TITLE     LncRNA SFTA1P promotes cervical cancer progression by interaction
            with PTBP1 to facilitate TPM4 mRNA degradation
  JOURNAL   Cell Death Dis 13 (11), 936 (2022)
   PUBMED   36344495
  REMARK    GeneRIF: LncRNA SFTA1P promotes cervical cancer progression by
            interaction with PTBP1 to facilitate TPM4 mRNA degradation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Marin-Quilez,A., Vuelta,E., Diaz-Ajenjo,L., Fernandez-Infante,C.,
            Garcia-Tunon,I., Benito,R., Palma-Barqueros,V.,
            Hernandez-Rivas,J.M., Gonzalez-Porras,J.R., Rivera,J. and
            Bastida,J.M.
  TITLE     A novel nonsense variant in TPM4 caused dominant
            macrothrombocytopenia, mild bleeding tendency and disrupted
            cytoskeleton remodeling
  JOURNAL   J Thromb Haemost 20 (5), 1248-1255 (2022)
   PUBMED   35170221
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Stapley,R.J., Poulter,N.S., Khan,A.O., Smith,C.W., Bignell,P.,
            Fratter,C., Lester,W., Lowe,G. and Morgan,N.V.
  CONSRTM   UK GAPP Study Group
  TITLE     Rare missense variants in Tropomyosin-4 (TPM4) are associated with
            platelet dysfunction, cytoskeletal defects, and excessive bleeding
  JOURNAL   J Thromb Haemost 20 (2), 478-485 (2022)
   PUBMED   34758189
  REMARK    GeneRIF: Rare missense variants in Tropomyosin-4 (TPM4) are
            associated with platelet dysfunction, cytoskeletal defects, and
            excessive bleeding.
            Erratum:[J Thromb Haemost. 2022 Jun;20(6):1511. doi:
            10.1111/jth.15719. PMID: 35596517]
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Crabos,M., Yamakado,T., Heizmann,C.W., Cerletti,N., Buhler,F.R. and
            Erne,P.
  TITLE     The calcium binding protein tropomyosin in human platelets and
            cardiac tissue: elevation in hypertensive cardiac hypertrophy
  JOURNAL   Eur J Clin Invest 21 (5), 472-478 (1991)
   PUBMED   1836432
REFERENCE   9  (residues 1 to 248)
  AUTHORS   MacLeod,A.R., Talbot,K., Smillie,L.B. and Houlker,C.
  TITLE     Characterization of a cDNA defining a gene family encoding TM30p1,
            a human fibroblast tropomyosin
  JOURNAL   J Mol Biol 194 (1), 1-10 (1987)
   PUBMED   3612796
REFERENCE   10 (residues 1 to 248)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC037576.1 and AC008894.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins involved in the contractile system of
            striated and smooth muscles and the cytoskeleton of non-muscle
            cells. Tropomyosins are dimers of coiled-coil proteins that
            polymerize end-to-end along the major groove in most actin
            filaments. They provide stability to the filaments and regulate
            access of other actin-binding proteins. In muscle cells, they
            regulate muscle contraction by controlling the binding of myosin
            heads to the actin filament. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2009].
            
            Transcript Variant: This variant (Tpm4.2, also known as variant 2)
            differs in the 5' UTR and coding sequence compared to variant
            Tpm4.1. The resulting isoform (Tpm4.2cy, also known as isoform 2)
            has a shorter and distinct N-terminus compared to isoform Tpm4.1cy.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.108830.1,
                                           SRR3476690.1123291.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000643579.2/ ENSP00000495347.1
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12-p13.11"
     Protein         1..248
                     /product="tropomyosin alpha-4 chain isoform Tpm4.2cy"
                     /note="tropomyosin alpha-4 chain; TM30p1; epididymis
                     secretory protein Li 108"
                     /calculated_mol_wt=28391
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P67936.3)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09495; propagated from
                     UniProtKB/Swiss-Prot (P67936.3)"
     Region          12..246
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     Region          15..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P67936.3)"
     Site            177
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P67936.3)"
     Site            215
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P67936.3)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P67936.3)"
     CDS             1..248
                     /gene="TPM4"
                     /gene_synonym="BDPLT25; HEL-S-108"
                     /coded_by="NM_003290.3:72..818"
                     /note="isoform Tpm4.2cy is encoded by transcript variant
                     1"
                     /db_xref="CCDS:CCDS12338.1"
                     /db_xref="GeneID:7171"
                     /db_xref="HGNC:HGNC:12013"
                     /db_xref="MIM:600317"
ORIGIN      
        1 maglnsleav krkiqalqqq adeaedraqg lqreldgere rrekaegdva alnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkvienramk deekmeiqem qlkeakhiae
      121 eadrkyeeva rklvilegel eraeeraevs elkcgdleee lknvtnnlks leaasekyse
      181 kedkyeeeik llsdklkeae traefaertv aklektiddl eeklaqakee nvglhqtldq
      241 tlnelnci
//
LOCUS       NP_001074007             344 aa            linear   PRI 27-APR-2025
DEFINITION  aldo-keto reductase family 1 member B15 isoform a [Homo sapiens].
ACCESSION   NP_001074007 XP_935641
VERSION     NP_001074007.2
DBSOURCE    REFSEQ: accession NM_001080538.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Gimenez-Dejoz,J., Kolar,M.H., Ruiz,F.X., Crespo,I.,
            Cousido-Siah,A., Podjarny,A., Barski,O.A., Fanfrlik,J., Pares,X.,
            Farres,J. and Porte,S.
  TITLE     Substrate Specificity, Inhibitor Selectivity and Structure-Function
            Relationships of Aldo-Keto Reductase 1B15: A Novel Human
            Retinaldehyde Reductase
  JOURNAL   PLoS One 10 (7), e0134506 (2015)
   PUBMED   26222439
  REMARK    GeneRIF: Amino acid substitutions clustered in loops A and C result
            in a smaller more hydrophobic and more rigid active site in AKR1B15
            compared with the AKR1B10 pocket, consistent with distinct
            substrate specificity and narrower inhibitor selectivity for
            AKR1B15.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Weber,S., Salabei,J.K., Moller,G., Kremmer,E., Bhatnagar,A.,
            Adamski,J. and Barski,O.A.
  TITLE     Aldo-keto Reductase 1B15 (AKR1B15): a mitochondrial human aldo-keto
            reductase with activity toward steroids and 3-keto-acyl-CoA
            conjugates
  JOURNAL   J Biol Chem 290 (10), 6531-6545 (2015)
   PUBMED   25577493
  REMARK    GeneRIF: AKR1B15.2 localizes to the cytosol and displays no
            enzymatic activity with the substrates tested.
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Jagoe,W.N., Howe,K., O'Brien,S.C. and Carroll,J.
  TITLE     Identification of a role for a mouse sperm surface aldo-keto
            reductase (AKR1B7) and its human analogue in the detoxification of
            the reactive aldehyde, acrolein
  JOURNAL   Andrologia 45 (5), 326-331 (2013)
   PUBMED   22970857
  REMARK    GeneRIF: human sperm possess an aldo-keto reductase on their
            membrane surface and are thus enzymatically protected against
            reactive aldehyde species both in the male and female reproductive
            tract
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Calvo,S.E., Compton,A.G., Hershman,S.G., Lim,S.C., Lieber,D.S.,
            Tucker,E.J., Laskowski,A., Garone,C., Liu,S., Jaffe,D.B.,
            Christodoulou,J., Fletcher,J.M., Bruno,D.L., Goldblatt,J.,
            Dimauro,S., Thorburn,D.R. and Mootha,V.K.
  TITLE     Molecular diagnosis of infantile mitochondrial disease with
            targeted next-generation sequencing
  JOURNAL   Sci Transl Med 4 (118), 118ra10 (2012)
   PUBMED   22277967
  REMARK    GeneRIF: Strong candidate gene for mitochondrial disease, based on
            recessive mutations detected in infantile patients
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Salabei,J.K., Li,X.P., Petrash,J.M., Bhatnagar,A. and Barski,O.A.
  TITLE     Functional expression of novel human and murine AKR1B genes
  JOURNAL   Chem Biol Interact 191 (1-3), 177-184 (2011)
   PUBMED   21276782
  REMARK    GeneRIF: AKR1B15 and Akr1b16 genes are expressed as functional
            proteins in human and murine tissues
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX335355.2 and AC078847.2.
            
            On Mar 20, 2010 this sequence version replaced NP_001074007.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1 and 2 both encode the same isoform (a).
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000457545.7/ ENSP00000389289.1
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..344
                     /product="aldo-keto reductase family 1 member B15 isoform
                     a"
                     /EC_number="1.1.1.64"
                     /EC_number="1.1.1.300"
                     /EC_number="1.1.1.216"
                     /EC_number="1.1.1.54"
                     /note="putative aldo-keto reductase family 1 member B15;
                     estradiol 17-beta-dehydrogenase AKR1B15; farnesol
                     dehydrogenase; testosterone 17beta-dehydrogenase"
                     /calculated_mol_wt=39329
     Region          51..344
                     /region_name="AKR_AKR1B1-19"
                     /note="AKR1B family of aldo-keto reductase (AKR); cd19107"
                     /db_xref="CDD:381333"
     Site            order(72,76..77,106,108,139..140,142,144,151,188..189,212,
                     238..245,248,257,274,289..294,297,300..301,327..329,332,
                     338..339)
                     /site_type="active"
                     /db_xref="CDD:381333"
     Site            order(72,77,106,139)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381333"
     CDS             1..344
                     /gene="AKR1B15"
                     /gene_synonym="AK1R1B7; AKR1B10L; AKR1R1B7"
                     /coded_by="NM_001080538.3:287..1321"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47715.2"
                     /db_xref="GeneID:441282"
                     /db_xref="HGNC:HGNC:37281"
                     /db_xref="MIM:616336"
ORIGIN      
        1 mvlqmepqvn stnnfhqgpl dqpvgpltgl kssllkdtts agpllrpypa sllgkvkeav
       61 kvaidaeyrh idcayfyenq hevgeaiqek iqekavmred lfivskvwpt fferplvrka
      121 fektlkdlkl syldvylihw pqgfktgddf fpkddkgnmi sgkgtfldaw eameelvdeg
      181 lvkalgvsnf nhfqierlln kpglkykpvt nqvechpylt qekliqychs kgitvtaysp
      241 lgspdrpwak pedpslledp kikeiaakhk kttaqvlirf hiqrnvtvip ksmtpahive
      301 niqvfdfkls deematilsf nrnwrafdfk efshledfpf daey
//
LOCUS       NP_057291                684 aa            linear   PRI 27-APR-2025
DEFINITION  cleavage and polyadenylation specificity factor subunit 3 isoform a
            [Homo sapiens].
ACCESSION   NP_057291
VERSION     NP_057291.1
DBSOURCE    REFSEQ: accession NM_016207.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Zhang,Y., Liu,D., Guo,D., Lin,W., Lu,W., Hu,L., Chen,S. and Chen,C.
  TITLE     CPSF3 regulates alternative polyadenylation of CNIH2 to promote
            esophageal squamous cell carcinoma progression
  JOURNAL   Cancer Lett 593, 216925 (2024)
   PUBMED   38718887
  REMARK    GeneRIF: CPSF3 regulates alternative polyadenylation of CNIH2 to
            promote esophageal squamous cell carcinoma progression.
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Alahmari,A.A., Chaubey,A.H., Jonnakuti,V.S., Tisdale,A.A.,
            Schwarz,C.D., Cornwell,A.C., Maraszek,K.E., Paterson,E.J., Kim,M.,
            Venkat,S., Gomez,E.C., Wang,J., Gurova,K.V., Yalamanchili,H.K. and
            Feigin,M.E.
  TITLE     CPSF3 inhibition blocks pancreatic cancer cell proliferation
            through disruption of core histone mRNA processing
  JOURNAL   RNA 30 (3), 281-297 (2024)
   PUBMED   38191171
  REMARK    GeneRIF: CPSF3 inhibition blocks pancreatic cancer cell
            proliferation through disruption of core histone mRNA processing.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Shen,P., Ye,K., Xiang,H., Zhang,Z., He,Q., Zhang,X., Cai,M.C.,
            Chen,J., Sun,Y., Lin,L., Qi,C., Zhang,M., Cheung,L.W.T., Shi,T.,
            Yin,X., Li,Y., Di,W., Zang,R., Tan,L. and Zhuang,G.
  TITLE     Therapeutic targeting of CPSF3-dependent transcriptional
            termination in ovarian cancer
  JOURNAL   Sci Adv 9 (47), eadj0123 (2023)
   PUBMED   37992178
  REMARK    GeneRIF: Therapeutic targeting of CPSF3-dependent transcriptional
            termination in ovarian cancer.
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Huang,J., Liu,X., Sun,Y., Li,Z., Lin,M.H., Hamilton,K.,
            Mandel,C.R., Sandmeir,F., Conti,E., Oyala,P.H. and Tong,L.
  TITLE     An examination of the metal ion content in the active sites of
            human endonucleases CPSF73 and INTS11
  JOURNAL   J Biol Chem 299 (4), 103047 (2023)
   PUBMED   36822327
  REMARK    GeneRIF: An examination of the metal ion content in the active
            sites of human endonucleases CPSF73 and INTS11.
REFERENCE   5  (residues 1 to 684)
  AUTHORS   Arnadottir,G.A., Oddsson,A., Jensson,B.O., Gisladottir,S.,
            Simon,M.T., Arnthorsson,A.O., Katrinardottir,H., Fridriksdottir,R.,
            Ivarsdottir,E.V., Jonasdottir,A., Jonasdottir,A., Barrick,R.,
            Saemundsdottir,J., le Roux,L., Oskarsson,G.R., Asmundsson,J.,
            Steffensen,T., Gudmundsson,K.R., Ludvigsson,P., Jonsson,J.J.,
            Masson,G., Jonsdottir,I., Holm,H., Jonasson,J.G., Magnusson,O.T.,
            Thorarensen,O., Abdenur,J., Norddahl,G.L., Gudbjartsson,D.F.,
            Bjornsson,H.T., Thorsteinsdottir,U., Sulem,P. and Stefansson,K.
  TITLE     Population-level deficit of homozygosity unveils CPSF3 as an
            intellectual disability syndrome gene
  JOURNAL   Nat Commun 13 (1), 705 (2022)
   PUBMED   35121750
  REMARK    GeneRIF: Population-level deficit of homozygosity unveils CPSF3 as
            an intellectual disability syndrome gene.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 684)
  AUTHORS   McCracken,S., Fong,N., Yankulov,K., Ballantyne,S., Pan,G.,
            Greenblatt,J., Patterson,S.D., Wickens,M. and Bentley,D.L.
  TITLE     The C-terminal domain of RNA polymerase II couples mRNA processing
            to transcription
  JOURNAL   Nature 385 (6614), 357-361 (1997)
   PUBMED   9002523
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Jenny,A., Minvielle-Sebastia,L., Preker,P.J. and Keller,W.
  TITLE     Sequence similarity between the 73-kilodalton protein of mammalian
            CPSF and a subunit of yeast polyadenylation factor I
  JOURNAL   Science 274 (5292), 1514-1517 (1996)
   PUBMED   8929409
REFERENCE   8  (residues 1 to 684)
  AUTHORS   Murthy,K.G. and Manley,J.L.
  TITLE     The 160-kD subunit of human cleavage-polyadenylation specificity
            factor coordinates pre-mRNA 3'-end formation
  JOURNAL   Genes Dev 9 (21), 2672-2683 (1995)
   PUBMED   7590244
REFERENCE   9  (residues 1 to 684)
  AUTHORS   Jenny,A., Hauri,H.P. and Keller,W.
  TITLE     Characterization of cleavage and polyadenylation specificity factor
            and cloning of its 100-kilodalton subunit
  JOURNAL   Mol Cell Biol 14 (12), 8183-8190 (1994)
   PUBMED   7969155
REFERENCE   10 (residues 1 to 684)
  AUTHORS   Thuresson,A.C., Astrom,J., Astrom,A., Gronvik,K.O. and Virtanen,A.
  TITLE     Multiple forms of poly(A) polymerases in human cells
  JOURNAL   Proc Natl Acad Sci U S A 91 (3), 979-983 (1994)
   PUBMED   8302877
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC420903.1, BC020211.1 and
            AA635764.1.
            
            Summary: This gene encodes a member of the metallo-beta-lactamase
            family. The encoded protein is a 73kDa subunit of the cleavage and
            polyadenylation specificity factor and functions as an endonuclease
            that recognizes the pre-mRNA 3'-cleavage site AAUAAA prior to
            polyadenylation. It also cleaves after the pre-mRNA sequence ACCCA
            during histone 3'-end pre-mRNA processing. [provided by RefSeq, Oct
            2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.92137.1,
                                           SRR1803615.243113.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000238112.8/ ENSP00000238112.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..684
                     /product="cleavage and polyadenylation specificity factor
                     subunit 3 isoform a"
                     /note="cleavage and polyadenylation specificity factor
                     subunit 3; mRNA 3'-end-processing endonuclease CPSF-73;
                     cleavage and polyadenylation specific factor 3, 73kDa"
                     /calculated_mol_wt=77355
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9UKF6.1)"
     Region          12..205
                     /region_name="CPSF3-like_MBL-fold"
                     /note="cleavage and polyadenylation specificity factor
                     (CPSF) subunit 3 and related proteins; MBL-fold
                     metallo-hydrolase domain; cd16292"
                     /db_xref="CDD:293850"
     Region          14..421
                     /region_name="YSH1"
                     /note="RNA processing exonuclease, beta-lactamase fold,
                     Cft2 family [Translation, ribosomal structure and
                     biogenesis]; COG1236"
                     /db_xref="CDD:440849"
     Site            order(71,73,75..76,158,179)
                     /site_type="active"
                     /db_xref="CDD:293850"
     Region          479..682
                     /region_name="CPSF73-100_C"
                     /note="Pre-mRNA 3'-end-processing endonuclease
                     polyadenylation factor C-term; pfam11718"
                     /db_xref="CDD:463330"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXK7; propagated from
                     UniProtKB/Swiss-Prot (Q9UKF6.1)"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKF6.1)"
     CDS             1..684
                     /gene="CPSF3"
                     /gene_synonym="CPSF-73; CPSF73; NEDMHS; NEDMHSN"
                     /coded_by="NM_016207.4:121..2175"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1664.1"
                     /db_xref="GeneID:51692"
                     /db_xref="HGNC:HGNC:2326"
                     /db_xref="MIM:606029"
ORIGIN      
        1 msaipaeesd qllirplgag qevgrsciil efkgrkimld cgihpglegm dalpyidlid
       61 paeidlllis hfhldhcgal pwflqktsfk grtfmthatk aiyrwllsdy vkvsnisadd
      121 mlytetdlee smdkietinf hevkevagik fwcyhaghvl gaamfmieia gvkllytgdf
      181 srqedrhlma aeipnikpdi liiestygth ihekreerea rfcntvhdiv nrggrglipv
      241 falgraqell lildeywqnh pelhdipiyy asslakkcma vyqtyvnamn dkirkqinin
      301 npfvfkhisn lksmdhfddi gpsvvmaspg mmqsglsrel feswctdkrn gviiagycve
      361 gtlakhimse peeittmsgq klplkmsvdy isfsahtdyq qtsefiralk pphvilvhge
      421 qnemarlkaa lireyednde vhievhnprn teavtlnfrg eklakvmgfl adkkpeqgqr
      481 vsgilvkrnf nyhilspcdl snytdlamst vkqtqaipyt gpfnllcyql qkltgdveel
      541 eiqekpalkv fknitviqep gmvvlewlan psndmyadtv ttvilevqsn pkirkgavqk
      601 vskklemhvy skrleimlqd ifgedcvsvk ddsilsvtvd gktanlnlet rtveceegse
      661 ddeslremve laaqrlyeal tpvh
//
LOCUS       NP_002198               1035 aa            linear   PRI 27-APR-2025
DEFINITION  integrin alpha-9 precursor [Homo sapiens].
ACCESSION   NP_002198
VERSION     NP_002198.2
DBSOURCE    REFSEQ: accession NM_002207.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Niibori-Nambu,A., Wang,C.Q., Chin,D.W.L., Chooi,J.Y., Hosoi,H.,
            Sonoki,T., Tham,C.Y., Nah,G.S.S., Cirovic,B., Tan,D.Q.,
            Takizawa,H., Sashida,G., Goh,Y., Tng,J., Fam,W.N., Fullwood,M.J.,
            Suda,T., Yang,H., Tergaonkar,V., Taniuchi,I., Li,S., Chng,W.J. and
            Osato,M.
  TITLE     Integrin-alpha9 overexpression underlies the niche-independent
            maintenance of leukemia stem cells in acute myeloid leukemia
  JOURNAL   Gene 928, 148761 (2024)
   PUBMED   39002785
  REMARK    GeneRIF: Integrin-alpha9 overexpression underlies the
            niche-independent maintenance of leukemia stem cells in acute
            myeloid leukemia.
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Ellergezen,P., Coskun,B.N., Bozkurt,Z.Y., Cecen,G.S., Agca,H.,
            Pehlivan,Y., Dalkilic,H.E., Cavun,S. and Yanar,Y.B.
  TITLE     alpha9beta1 integrin & its ligands as new potential biomarkers in
            FMF
  JOURNAL   Indian J Med Res 160 (1), 102-108 (2024)
   PUBMED   39382510
  REMARK    GeneRIF: alpha9beta1 integrin & its ligands as new potential
            biomarkers in FMF.
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Liu,W., Fang,S., Yang,Z., Ma,J., Tan,Y., Chen,Y., Zhang,K., Liu,K.
            and Gu,W.
  TITLE     ITGA9-AS1 up-regulates ITGA9 by targeting miR-4765 and recruiting
            HNRNPU to affect the proliferation and apoptosis of non-small cell
            lung cancer cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (14), 22-28 (2023)
   PUBMED   38279497
  REMARK    GeneRIF: ITGA9-AS1 up-regulates ITGA9 by targeting miR-4765 and
            recruiting HNRNPU to affect the proliferation and apoptosis of
            non-small cell lung cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1035)
  AUTHORS   Morris,G.E., Denniff,M.J., Karamanavi,E., Andrews,S.A.,
            Kostogrys,R.B., Bountziouka,V., Ghaderi-Najafabadi,M., Shamkhi,N.,
            McConnell,G., Kaiser,M.A., Carleton,L., Schofield,C., Kessler,T.,
            Rainbow,R.D., Samani,N.J. and Webb,T.R.
  TITLE     The integrin ligand SVEP1 regulates GPCR-mediated vasoconstriction
            via integrins alpha9beta1 and alpha4beta1
  JOURNAL   Br J Pharmacol 179 (21), 4958-4973 (2022)
   PUBMED   35802072
REFERENCE   5  (residues 1 to 1035)
  AUTHORS   Navarro,N., Molist,C., Sansa-Girona,J., Zarzosa,P., Gallo-Oller,G.,
            Pons,G., Magdaleno,A., Guillen,G., Hladun,R., Garrido,M.,
            Segura,M.F., Hontecillas-Prieto,L., de Alava,E., Ponsati,B.,
            Fernandez-Carneado,J., Almazan-Moga,A., Valles-Miret,M.,
            Farrera-Sinfreu,J., de Toledo,J.S., Moreno,L., Gallego,S. and
            Roma,J.
  TITLE     Integrin alpha9 emerges as a key therapeutic target to reduce
            metastasis in rhabdomyosarcoma and neuroblastoma
  JOURNAL   Cell Mol Life Sci 79 (11), 546 (2022)
   PUBMED   36221013
  REMARK    GeneRIF: Integrin alpha9 emerges as a key therapeutic target to
            reduce metastasis in rhabdomyosarcoma and neuroblastoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1035)
  AUTHORS   Taooka,Y., Chen,J., Yednock,T. and Sheppard,D.
  TITLE     The integrin alpha9beta1 mediates adhesion to activated endothelial
            cells and transendothelial neutrophil migration through interaction
            with vascular cell adhesion molecule-1
  JOURNAL   J Cell Biol 145 (2), 413-420 (1999)
   PUBMED   10209034
REFERENCE   7  (residues 1 to 1035)
  AUTHORS   Yokosaki,Y., Matsuura,N., Higashiyama,S., Murakami,I., Obara,M.,
            Yamakido,M., Shigeto,N., Chen,J. and Sheppard,D.
  TITLE     Identification of the ligand binding site for the integrin alpha9
            beta1 in the third fibronectin type III repeat of tenascin-C
  JOURNAL   J Biol Chem 273 (19), 11423-11428 (1998)
   PUBMED   9565552
REFERENCE   8  (residues 1 to 1035)
  AUTHORS   Hibi,K., Yamakawa,K., Ueda,R., Horio,Y., Murata,Y., Tamari,M.,
            Uchida,K., Takahashi,T., Nakamura,Y. and Takahashi,T.
  TITLE     Aberrant upregulation of a novel integrin alpha subunit gene at
            3p21.3 in small cell lung cancer
  JOURNAL   Oncogene 9 (2), 611-619 (1994)
   PUBMED   8290272
REFERENCE   9  (residues 1 to 1035)
  AUTHORS   Palmer,E.L., Ruegg,C., Ferrando,R., Pytela,R. and Sheppard,D.
  TITLE     Sequence and tissue distribution of the integrin alpha 9 subunit, a
            novel partner of beta 1 that is widely distributed in epithelia and
            muscle
  JOURNAL   J Cell Biol 123 (5), 1289-1297 (1993)
   PUBMED   8245132
  REMARK    Erratum:[J Cell Biol 1994 Feb;124(3):395]
REFERENCE   10 (residues 1 to 1035)
  AUTHORS   Yamakawa,K., Takahashi,T., Horio,Y., Murata,Y., Takahashi,E.,
            Hibi,K., Yokoyama,S., Ueda,R., Takahashi,T. and Nakamura,Y.
  TITLE     Frequent homozygous deletions in lung cancer cell lines detected by
            a DNA marker located at 3p21.3-p22
  JOURNAL   Oncogene 8 (2), 327-330 (1993)
   PUBMED   8381220
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092055.2, BC030198.1,
            D25303.1, L24158.1, BX647350.1 and AC093415.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 22, 2004 this sequence version replaced NP_002198.1.
            
            Summary: This gene encodes an alpha integrin. Integrins are
            heterodimeric integral membrane glycoproteins composed of an alpha
            chain and a beta chain that mediate cell-cell and cell-matrix
            adhesion. The protein encoded by this gene, when bound to the beta
            1 chain, forms an integrin that is a receptor for VCAM1, cytotactin
            and osteopontin. Expression of this gene has been found to be
            upregulated in small cell lung cancers. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D25303.1, L24158.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147920, SAMEA2154405
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264741.10/ ENSP00000264741.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..1035
                     /product="integrin alpha-9 precursor"
                     /note="integrin alpha-RLC; integrin alpha-9"
                     /calculated_mol_wt=111810
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2697
     mat_peptide     30..1035
                     /product="integrin alpha-9"
                     /calculated_mol_wt=111810
     Region          35..96
                     /region_name="FG-GAP 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13797.2)"
     Region          44..101
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          111..174
                     /region_name="FG-GAP 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13797.2)"
     Region          182..232
                     /region_name="FG-GAP 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13797.2)"
     Site            225
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Region          233..289
                     /region_name="FG-GAP 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13797.2)"
     Region          244..294
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          290..349
                     /region_name="FG-GAP 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13797.2)"
     Region          300..347
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          351..408
                     /region_name="FG-GAP 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13797.2)"
     Region          361..414
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          411..474
                     /region_name="FG-GAP 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13797.2)"
     Region          425..>466
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          460..903
                     /region_name="Integrin_alpha2"
                     /note="Integrin alpha; pfam08441"
                     /db_xref="CDD:462478"
     Site            476
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            493
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            565..566
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            612
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            654
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            658
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            672
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            676
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            807
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            854
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            904
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13797.2)"
     Site            982..1002
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13797.2)"
     Region          1005..1009
                     /region_name="GFFKR motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13797.2)"
     CDS             1..1035
                     /gene="ITGA9"
                     /gene_synonym="ALPHA-RLC; ITGA4L; RLC"
                     /coded_by="NM_002207.3:235..3342"
                     /db_xref="CCDS:CCDS2669.1"
                     /db_xref="GeneID:3680"
                     /db_xref="HGNC:HGNC:6145"
                     /db_xref="MIM:603963"
ORIGIN      
        1 mggpaaprga grlralllal vvagipagay nldpqrpvhf qgpadsffgy avlehfhdnt
       61 rwvlvgapka dskyspsvks pgavfkcrvh tnpdrrctel dmargknrgt scgktcredr
      121 ddewmgvsla rqpkadgrvl acahrwkniy yeadhilphg fcyiipsnlq akgrtlipcy
      181 eeykkkygee hgscqagiag ffteelvvmg apgsfywagt ikvlnltdnt ylklndevim
      241 nrrytylgya vtaghfshps tidvvggapq dkgigkvyif radrrsgtli kifqasgkkm
      301 gsyfgsslca vdlngdglsd llvgapmfse irdegqvtvy inrgngalee qlaltgdgay
      361 nahfgesias lddldndgfp dvaigapked dfagavyiyh gdaggivpqy smklsgqkin
      421 pvlrmfgqsi sggidmdgng ypdvtvgafm sdsvvllrar pvitvdvsif lpgsinitap
      481 qchdgqqpvn clnvttcfsf hgkhvpgeig lnyvlmadva kkekgqmprv yfvllgetmg
      541 qvteklqlty meetcrhyva hvkrrvqdvi spivfeaays lsehvtgeee relppltpvl
      601 rwkkgqkiaq knqtvfernc rsedcaadlq lqgklllssm dektlylalg avknislnis
      661 isnlgddayd anvsfnvsre lffinmwqke emgiscelle sdflkcsvgf pfmrskskye
      721 fsvifdtshl sgeeevlsfi vtaqsgnter seslhdntlv lmvplmhevd tsitgimspt
      781 sfvygesvda anfiqlddle chfqpinitl qvyntgpstl pgssvsisfp nrlssggaem
      841 fhvqemvvgq ekgncsfqkn ptpciipqeq enifhtifaf ftksgrkvld cekpgisclt
      901 ahcnfsalak eesrtidiym llnteilkkd sssviqfmsr akvkvdpalr vveiahgnpe
      961 evtvvfealh nleprgyvvg wiiaisllvg iliflllavl lwkmgffrrr ykeiieaekn
     1021 rkenedswdw vqknq
//
LOCUS       NP_076952                350 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-ribose pyrophosphatase, mitochondrial isoform a precursor [Homo
            sapiens].
ACCESSION   NP_076952 NP_932156
VERSION     NP_076952.1
DBSOURCE    REFSEQ: accession NM_024047.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Debar,L., Ishak,L., Moretton,A., Anoosheh,S., Morel,F.,
            Jenninger,L., Garreau-Balandier,I., Vernet,P., Hofer,A., van den
            Wildenberg,S. and Farge,G.
  TITLE     NUDT6 and NUDT9, two mitochondrial members of the NUDIX family,
            have distinct hydrolysis activities
  JOURNAL   Mitochondrion 71, 93-103 (2023)
   PUBMED   37343711
  REMARK    GeneRIF: NUDT6 and NUDT9, two mitochondrial members of the NUDIX
            family, have distinct hydrolysis activities.
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Gattkowski,E., Rutherford,T.J., Mockl,F., Bauche,A., Sander,S.,
            Fliegert,R. and Tidow,H.
  TITLE     Analysis of ligand binding and resulting conformational changes in
            pyrophosphatase NUDT9
  JOURNAL   FEBS J 288 (23), 6769-6782 (2021)
   PUBMED   34189846
  REMARK    GeneRIF: Analysis of ligand binding and resulting conformational
            changes in pyrophosphatase NUDT9.
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Yoon,B., Yang,E.G. and Kim,S.Y.
  TITLE     The ADP-ribose reactive NUDIX hydrolase isoforms can modulate
            HIF-1alpha in cancer cells
  JOURNAL   Biochem Biophys Res Commun 504 (1), 321-327 (2018)
   PUBMED   30190133
  REMARK    GeneRIF: ADP-ribose reactive NUDT9 NUDIX hydrolase isoforms
            modulate HIF-1alpha in cancer cells
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Shen,B.W., Perraud,A.L., Scharenberg,A. and Stoddard,B.L.
  TITLE     The crystal structure and mutational analysis of human NUDT9
  JOURNAL   J Mol Biol 332 (2), 385-398 (2003)
   PUBMED   12948489
  REMARK    GeneRIF: Data report the crystal structures of NUDT9 in the
            presence and in the absence of the reaction product ribose
            5'-phosphate.
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Zhang,H.T., Yan,Z.Q., Hu,X.B., Yang,S.L. and Gong,Y.
  TITLE     Interaction of C17orf25 with ADP-ribose pyrophosphatase NUDT9
            detected via yeast two-hybrid method
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 35 (8),
            747-751 (2003)
   PUBMED   12897971
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Perraud,A.L., Shen,B., Dunn,C.A., Rippe,K., Smith,M.K.,
            Bessman,M.J., Stoddard,B.L. and Scharenberg,A.M.
  TITLE     NUDT9, a member of the Nudix hydrolase family, is an evolutionarily
            conserved mitochondrial ADP-ribose pyrophosphatase
  JOURNAL   J Biol Chem 278 (3), 1794-1801 (2003)
   PUBMED   12427752
  REMARK    GeneRIF: analysis of the human NUDT9 gene and its potential
            alternative transcripts along with detailed studies of the
            enzymatic properties and cell biological behavior of human NUDT9
            protein
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Lin,S., Gasmi,L., Xie,Y., Ying,K., Gu,S., Wang,Z., Jin,H., Chao,Y.,
            Wu,C., Zhou,Z., Tang,R., Mao,Y. and McLennan,A.G.
  TITLE     Cloning, expression and characterisation of a human Nudix hydrolase
            specific for adenosine 5'-diphosphoribose (ADP-ribose)
  JOURNAL   Biochim Biophys Acta 1594 (1), 127-135 (2002)
   PUBMED   11825615
  REMARK    GeneRIF: Hydrolyses ADP-ribose to AMP and ribose-5-phosphate
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Perraud,A.L., Fleig,A., Dunn,C.A., Bagley,L.A., Launay,P.,
            Schmitz,C., Stokes,A.J., Zhu,Q., Bessman,M.J., Penner,R.,
            Kinet,J.P. and Scharenberg,A.M.
  TITLE     ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed
            by Nudix motif homology
  JOURNAL   Nature 411 (6837), 595-599 (2001)
   PUBMED   11385575
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112250.4, BP277630.1,
            AK027295.1 and AK074845.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 22, 2006 this sequence version replaced NP_932156.1.
            
            Summary: The protein encoded by this gene belongs to the Nudix
            hydrolase family. Nudix boxes are found in a family of diverse
            enzymes that catalyze the hydrolysis of nucleoside diphosphate
            derivatives. This enzyme is an ADP-ribose pyrophosphatase that
            catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. It
            requires divalent metal ions and an intact Nudix motif for
            enzymatic activity. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1, also known as NUDT9 alpha)
            represents the predominant transcript, and encodes the longest
            isoform (a). This isoform is localized in the mitochondria
            (PMID:12427752).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.261349.1,
                                           SRR1660803.62581.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 12427752
            MANE Ensembl match                 :: ENST00000302174.9/
                                                  ENSP00000303575.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.1"
     Protein         1..350
                     /product="ADP-ribose pyrophosphatase, mitochondrial
                     isoform a precursor"
                     /EC_number="3.6.1.13"
                     /note="nucleoside diphosphate linked moiety X-type motif
                     9; ADP-ribose diphosphatase; adenosine diphosphoribose
                     pyrophosphatase; ADP-ribose phosphohydrolase; ADP-ribose
                     pyrosphosphatase NUDT9; ADP-ribose pyrophosphatase,
                     mitochondrial; ADPR-PPase; nudix (nucleoside diphosphate
                     linked moiety X)-type motif 9"
                     /calculated_mol_wt=34204
     transit_peptide 1..46
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9BW91.1)"
                     /calculated_mol_wt=4939
     mat_peptide     21..350
                     /product="ADP-ribose pyrophosphatase, mitochondrial
                     isoform a"
                     /calculated_mol_wt=37217
     mat_peptide     47..350
                     /product="ADP-ribose pyrophosphatase, mitochondrial.
                     /id=PRO_0000019950"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BW91.1)"
                     /calculated_mol_wt=34204
     Region          53..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BW91.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BW91.1)"
     Region          149..335
                     /region_name="NUDIX_ADPRase_Nudt9"
                     /note="ADP-ribose pyrophosphatase; cd03670"
                     /db_xref="CDD:467538"
     Region          215..237
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BW91.1)"
     CDS             1..350
                     /gene="NUDT9"
                     /gene_synonym="NUDT10"
                     /coded_by="NM_024047.5:334..1386"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3620.1"
                     /db_xref="GeneID:53343"
                     /db_xref="HGNC:HGNC:8056"
                     /db_xref="MIM:606022"
ORIGIN      
        1 magrllgkal aavslslala svtirssrcr giqafrnsfs sswfhlntnv msgsngsken
       61 shnkartspy pgskversqv pnekvgwlve wqdykpveyt avsvlagprw adpqisesnf
      121 spkfnekdgh verkskngly eiengrprnp agrtglvgrg llgrwgpnha adpiitrwkr
      181 dssgnkimhp vsgkhilqfv aikrkdcgew aipggmvdpg ekisatlkre fgeealnslq
      241 ktsaekreie eklhklfsqd hlviykgyvd dprntdnawm eteavnyhde tgeimdnlml
      301 eagddagkvk wvdindklkl yashsqfikl vaekrdahws edseadchal
//
LOCUS       NP_001008273             199 aa            linear   PRI 27-APR-2025
DEFINITION  transgelin-3 [Homo sapiens].
ACCESSION   NP_001008273
VERSION     NP_001008273.1
DBSOURCE    REFSEQ: accession NM_001008272.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Ito,M., Depaz,I., Wilce,P., Suzuki,T., Niwa,S. and Matsumoto,I.
  TITLE     Expression of human neuronal protein 22, a novel
            cytoskeleton-associated protein, was decreased in the anterior
            cingulate cortex of schizophrenia
  JOURNAL   Neurosci Lett 378 (3), 125-130 (2005)
   PUBMED   15781144
  REMARK    GeneRIF: Altered expression of hNP22 may be associated with
            modifications in neuronal cytoarchitecture leading to dysregulation
            of neural signal transduction in the anterior cingulate cortex of
            the schizophrenia brain.
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Depaz,I., Ito,M., Matsumoto,I., Niwa,S., Kroon,P. and Wilce,P.A.
  TITLE     Expression of hNP22 is altered in the frontal cortex and
            hippocampus of the alcoholic human brain
  JOURNAL   Alcohol Clin Exp Res 27 (9), 1481-1488 (2003)
   PUBMED   14506410
  REMARK    GeneRIF: Western blots revealed a significant increase in hNP22
            protein levels in the frontal cortex but not the motor cortex of
            alcoholic cases.
            Erratum:[Alcohol Clin Exp Res. 2004 Sep;28(9):1431]
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 199)
  AUTHORS   Fan,L., Jaquet,V., Dodd,P.R., Chen,W. and Wilce,P.A.
  TITLE     Molecular cloning and characterization of hNP22: a gene
            up-regulated in human alcoholic brain
  JOURNAL   J Neurochem 76 (5), 1275-1281 (2001)
   PUBMED   11238712
REFERENCE   7  (residues 1 to 199)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   8  (residues 1 to 199)
  AUTHORS   Ren,W.Z., Ng,G.Y., Wang,R.X., Wu,P.H., O'Dowd,B.F., Osmond,D.H.,
            George,S.R. and Liew,C.C.
  TITLE     The identification of NP25: a novel protein that is differentially
            expressed by neuronal subpopulations
  JOURNAL   Brain Res Mol Brain Res 22 (1-4), 173-185 (1994)
   PUBMED   8015377
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI752099.1, BC015329.1 and BM894229.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF087855.1, SRR5189652.253305.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000478951.6/ ENSP00000419105.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.2"
     Protein         1..199
                     /product="transgelin-3"
                     /note="neuronal protein 22; neuronal protein NP25"
                     /calculated_mol_wt=22342
     Region          23..141
                     /region_name="CH_TAGLN3"
                     /note="calponin homology (CH) domain found in
                     transgelin-3; cd21281"
                     /db_xref="CDD:409130"
     Site            order(26,30,88,90..91,94..95,97,107..115,121,123..124,
                     126..127,130..131,134)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409130"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P37805; propagated from
                     UniProtKB/Swiss-Prot (Q9UI15.2)"
     Region          174..199
                     /region_name="Calponin-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UI15.2)"
     Region          174..198
                     /region_name="Calponin"
                     /note="Calponin family repeat; pfam00402"
                     /db_xref="CDD:459803"
     Region          176..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UI15.2)"
     CDS             1..199
                     /gene="TAGLN3"
                     /gene_synonym="NP22; NP24; NP25"
                     /coded_by="NM_001008272.2:196..795"
                     /db_xref="CCDS:CCDS33816.1"
                     /db_xref="GeneID:29114"
                     /db_xref="HGNC:HGNC:29868"
                     /db_xref="MIM:607953"
ORIGIN      
        1 manrgpsygl srevqekieq kydadlenkl vdwiilqcae diehpppgra hfqkwlmdgt
       61 vlcklinsly ppgqepipki seskmafkqm eqisqflkaa etygvrttdi fqtvdlwegk
      121 dmaavqrtlm algsvavtkd dgcyrgepsw fhrkaqqnrr gfseeqlrqg qnviglqmgs
      181 nkgasqagmt gygmprqim
//
LOCUS       NP_059132                353 aa            linear   PRI 27-APR-2025
DEFINITION  lactosylceramide 4-alpha-galactosyltransferase [Homo sapiens].
ACCESSION   NP_059132
VERSION     NP_059132.1
DBSOURCE    REFSEQ: accession NM_017436.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Mo,C., Jia,S., Luo,G. and Ji,Y.
  TITLE     Identification of a novel A4GALT*299A allele associated with the
            rare p phenotype in one Chinese family
  JOURNAL   Transfusion 64 (4), E13-E15 (2024)
   PUBMED   38501748
  REMARK    GeneRIF: Identification of a novel A4GALT*299A allele associated
            with the rare p phenotype in one Chinese family.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Jia,S., Li,S., Liao,Z., Mo,C., Fang,Q., Luo,G. and Ji,Y.
  TITLE     Identification of a novel P1PK allele (A4GALT*c.1-504_1044del1548)
            in two Chinese sisters with a history of recurrent spontaneous
            abortion
  JOURNAL   Transfusion 62 (9), E52-E54 (2022)
   PUBMED   35929100
  REMARK    GeneRIF: Identification of a novel P1PK allele
            (A4GALT*c.1-504_1044del1548) in two Chinese sisters with a history
            of recurrent spontaneous abortion.
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Mikolajczyk,K., Bereznicka,A., Szymczak-Kulus,K.,
            Haczkiewicz-Lesniak,K., Szulc,B., Olczak,M., Rossowska,J.,
            Majorczyk,E., Kapczynska,K., Bovin,N., Lisowska,M., Kaczmarek,R.,
            Miazek,A. and Czerwinski,M.
  TITLE     Missing the sweet spot: one of the two N-glycans on human Gb3/CD77
            synthase is expendable
  JOURNAL   Glycobiology 31 (9), 1145-1162 (2021)
   PUBMED   33978735
  REMARK    GeneRIF: Missing the sweet spot: one of the two N-glycans on human
            Gb3/CD77 synthase is expendable.
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Szymczak-Kulus,K., Weidler,S., Bereznicka,A., Mikolajczyk,K.,
            Kaczmarek,R., Bednarz,B., Zhang,T., Urbaniak,A., Olczak,M.,
            Park,E.Y., Majorczyk,E., Kapczynska,K., Lukasiewicz,J., Wuhrer,M.,
            Unverzagt,C. and Czerwinski,M.
  TITLE     Human Gb3/CD77 synthase produces P1 glycotope-capped N-glycans,
            which mediate Shiga toxin 1 but not Shiga toxin 2 cell entry
  JOURNAL   J Biol Chem 296, 100299 (2021)
   PUBMED   33460651
  REMARK    GeneRIF: Human Gb3/CD77 synthase produces P1 glycotope-capped
            N-glycans, which mediate Shiga toxin 1 but not Shiga toxin 2 cell
            entry.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Hellberg,A., Chester,M.A. and Olsson,M.L.
  TITLE     Two previously proposed P1/P2-differentiating and nine novel
            polymorphisms at the A4GALT (Pk) locus do not correlate with the
            presence of the P1 blood group antigen
  JOURNAL   BMC Genet 6, 49 (2005)
   PUBMED   16212661
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Iwamura,K., Furukawa,K., Uchikawa,M., Sojka,B.N., Kojima,Y.,
            Wiels,J., Shiku,H., Urano,T. and Furukawa,K.
  TITLE     The blood group P1 synthase gene is identical to the Gb3/CD77
            synthase gene. A clue to the solution of the P1/P2/p puzzle
  JOURNAL   J Biol Chem 278 (45), 44429-44438 (2003)
   PUBMED   12888565
  REMARK    GeneRIF: results strongly suggested that P1 synthase is identical
            to Gb3/CD77 synthase
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Keusch,J.J., Manzella,S.M., Nyame,K.A., Cummings,R.D. and
            Baenziger,J.U.
  TITLE     Cloning of Gb3 synthase, the key enzyme in globo-series
            glycosphingolipid synthesis, predicts a family of alpha 1,
            4-glycosyltransferases conserved in plants, insects, and mammals
  JOURNAL   J Biol Chem 275 (33), 25315-25321 (2000)
   PUBMED   10854428
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Steffensen,R., Carlier,K., Wiels,J., Levery,S.B., Stroud,M.,
            Cedergren,B., Nilsson Sojka,B., Bennett,E.P., Jersild,C. and
            Clausen,H.
  TITLE     Cloning and expression of the histo-blood group Pk UDP-galactose:
            Ga1beta-4G1cbeta1-cer alpha1, 4-galactosyltransferase. Molecular
            genetic basis of the p phenotype
  JOURNAL   J Biol Chem 275 (22), 16723-16729 (2000)
   PUBMED   10747952
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Kojima,Y., Fukumoto,S., Furukawa,K., Okajima,T., Wiels,J.,
            Yokoyama,K., Suzuki,Y., Urano,T., Ohta,M. and Furukawa,K.
  TITLE     Molecular cloning of globotriaosylceramide/CD77 synthase, a
            glycosyltransferase that initiates the synthesis of globo series
            glycosphingolipids
  JOURNAL   J Biol Chem 275 (20), 15152-15156 (2000)
   PUBMED   10748143
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY140390.1, BC017068.2 and
            AB037883.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene catalyzes the transfer of
            galactose to lactosylceramide to form globotriaosylceramide, which
            has been identified as the P(k) antigen of the P blood group
            system. This protein, a type II membrane protein found in the
            Golgi, is also required for the synthesis of the bacterial
            verotoxins receptor. Alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) encodes the supported protein.
            Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017068.2, SRR1163657.514031.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2162568
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000642412.2/ ENSP00000494127.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..353
                     /product="lactosylceramide 4-alpha-galactosyltransferase"
                     /EC_number="2.4.1.228"
                     /note="P blood group (P one antigen); GB3 synthase; P one
                     antigen (P blood group); alpha-1,4-galactosyltransferase;
                     globotriaosylceramide synthase; CD77 synthase; P(k)
                     antigen synthase; P1/Pk synthase;
                     alpha-1,4-N-acetylglucosaminyltransferase; alpha4Gal-T1;
                     UDP-galactose:beta-D-galactosyl-beta1-R
                     4-alpha-D-galactosyltransferase; alpha
                     1,4-galactosyltransferase (P blood group); alpha
                     14-galactosyltransferase"
                     /calculated_mol_wt=40368
     Site            23..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPC4.1)"
     Region          94..214
                     /region_name="Gly_transf_sug"
                     /note="Glycosyltransferase sugar-binding region containing
                     DXD motif; cl19952"
                     /db_xref="CDD:418730"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPC4.1)"
     Region          192..194
                     /region_name="DXD motif. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPC4.1)"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPC4.1)"
     Region          222..349
                     /region_name="Gb3_synth"
                     /note="Alpha 1,4-glycosyltransferase conserved region;
                     pfam04572"
                     /db_xref="CDD:428017"
     CDS             1..353
                     /gene="A4GALT"
                     /gene_synonym="A14GALT; A4GALT1; Gb3S; P(k); P1; P1PK; PK"
                     /coded_by="NM_017436.7:262..1323"
                     /db_xref="CCDS:CCDS14041.1"
                     /db_xref="GeneID:53947"
                     /db_xref="HGNC:HGNC:18149"
                     /db_xref="MIM:607922"
ORIGIN      
        1 mskppdlllr llrgaprqrv ctlfiigfkf tffvsimiyw hvvgepkekg qlynlpaeip
       61 cptltpptpp shgptpgnif fletsdrtnp nflfmcsves aarthpeshv lvlmkglpgg
      121 naslprhlgi sllscfpnvq mlpldlrelf rdtpladwya avqgrwepyl lpvlsdasri
      181 almwkfggiy ldtdfivlkn lrnltnvlgt qsryvlngaf laferrhefm alcmrdfvdh
      241 yngwiwghqg pqlltrvfkk wcsirslaes racrgvttlp peafypipwq dwkkyfedin
      301 peelprllsa tyavhvwnkk sqgtrfeats rallaqlhar ycpttheamk myl
//
LOCUS       NP_001005404             119 aa            linear   PRI 27-APR-2025
DEFINITION  protein yippee-like 2 [Homo sapiens].
ACCESSION   NP_001005404 XP_371070
VERSION     NP_001005404.1
DBSOURCE    REFSEQ: accession NM_001005404.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Xu,J.X., Tang,M.L., Lu,Z.F., Song,Y., Zhang,K.L., He,R.C.,
            Guo,X.N., Yuan,Y.Q., Dai,X. and Ma,X.
  TITLE     A novel role for YPEL2 in mediating endothelial cellular senescence
            via the p53/p21 pathway
  JOURNAL   Mech Ageing Dev 211, 111803 (2023)
   PUBMED   36963468
  REMARK    GeneRIF: A novel role for YPEL2 in mediating endothelial cellular
            senescence via the p53/p21 pathway.
REFERENCE   2  (residues 1 to 119)
  AUTHORS   de Bruijn,S.E., Fiorentino,A., Ottaviani,D., Fanucchi,S.,
            Melo,U.S., Corral-Serrano,J.C., Mulders,T., Georgiou,M.,
            Rivolta,C., Pontikos,N., Arno,G., Roberts,L., Greenberg,J.,
            Albert,S., Gilissen,C., Aben,M., Rebello,G., Mead,S., Raymond,F.L.,
            Corominas,J., Smith,C.E.L., Kremer,H., Downes,S., Black,G.C.,
            Webster,A.R., Inglehearn,C.F., van den Born,L.I., Koenekoop,R.K.,
            Michaelides,M., Ramesar,R.S., Hoyng,C.B., Mundlos,S., Mhlanga,M.M.,
            Cremers,F.P.M., Cheetham,M.E., Roosing,S. and Hardcastle,A.J.
  TITLE     Structural Variants Create New Topological-Associated Domains and
            Ectopic Retinal Enhancer-Gene Contact in Dominant Retinitis
            Pigmentosa
  JOURNAL   Am J Hum Genet 107 (5), 802-814 (2020)
   PUBMED   33022222
  REMARK    GeneRIF: Structural Variants Create New Topological-Associated
            Domains and Ectopic Retinal Enhancer-Gene Contact in Dominant
            Retinitis Pigmentosa.
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Arking,D.E., Pulit,S.L., Crotti,L., van der Harst,P., Munroe,P.B.,
            Koopmann,T.T., Sotoodehnia,N., Rossin,E.J., Morley,M., Wang,X.,
            Johnson,A.D., Lundby,A., Gudbjartsson,D.F., Noseworthy,P.A.,
            Eijgelsheim,M., Bradford,Y., Tarasov,K.V., Dorr,M.,
            Muller-Nurasyid,M., Lahtinen,A.M., Nolte,I.M., Smith,A.V.,
            Bis,J.C., Isaacs,A., Newhouse,S.J., Evans,D.S., Post,W.S.,
            Waggott,D., Lyytikainen,L.P., Hicks,A.A., Eisele,L., Ellinghaus,D.,
            Hayward,C., Navarro,P., Ulivi,S., Tanaka,T., Tester,D.J.,
            Chatel,S., Gustafsson,S., Kumari,M., Morris,R.W., Naluai,A.T.,
            Padmanabhan,S., Kluttig,A., Strohmer,B., Panayiotou,A.G.,
            Torres,M., Knoflach,M., Hubacek,J.A., Slowikowski,K.,
            Raychaudhuri,S., Kumar,R.D., Harris,T.B., Launer,L.J.,
            Shuldiner,A.R., Alonso,A., Bader,J.S., Ehret,G., Huang,H.,
            Kao,W.H., Strait,J.B., Macfarlane,P.W., Brown,M., Caulfield,M.J.,
            Samani,N.J., Kronenberg,F., Willeit,J., Smith,J.G., Greiser,K.H.,
            Meyer Zu Schwabedissen,H., Werdan,K., Carella,M., Zelante,L.,
            Heckbert,S.R., Psaty,B.M., Rotter,J.I., Kolcic,I., Polasek,O.,
            Wright,A.F., Griffin,M., Daly,M.J., Arnar,D.O., Holm,H.,
            Thorsteinsdottir,U., Denny,J.C., Roden,D.M., Zuvich,R.L.,
            Emilsson,V., Plump,A.S., Larson,M.G., O'Donnell,C.J., Yin,X.,
            Bobbo,M., D'Adamo,A.P., Iorio,A., Sinagra,G., Carracedo,A.,
            Cummings,S.R., Nalls,M.A., Jula,A., Kontula,K.K., Marjamaa,A.,
            Oikarinen,L., Perola,M., Porthan,K., Erbel,R., Hoffmann,P.,
            Jockel,K.H., Kalsch,H., Nothen,M.M., den Hoed,M., Loos,R.J.,
            Thelle,D.S., Gieger,C., Meitinger,T., Perz,S., Peters,A.,
            Prucha,H., Sinner,M.F., Waldenberger,M., de Boer,R.A., Franke,L.,
            van der Vleuten,P.A., Beckmann,B.M., Martens,E., Bardai,A.,
            Hofman,N., Wilde,A.A., Behr,E.R., Dalageorgou,C., Giudicessi,J.R.,
            Medeiros-Domingo,A., Barc,J., Kyndt,F., Probst,V., Ghidoni,A.,
            Insolia,R., Hamilton,R.M., Scherer,S.W., Brandimarto,J.,
            Margulies,K., Moravec,C.E., del Greco,M. F, Fuchsberger,C.,
            O'Connell,J.R., Lee,W.K., Watt,G.C., Campbell,H., Wild,S.H., El
            Mokhtari,N.E., Frey,N., Asselbergs,F.W., Mateo Leach,I., Navis,G.,
            van den Berg,M.P., van Veldhuisen,D.J., Kellis,M., Krijthe,B.P.,
            Franco,O.H., Hofman,A., Kors,J.A., Uitterlinden,A.G.,
            Witteman,J.C., Kedenko,L., Lamina,C., Oostra,B.A., Abecasis,G.R.,
            Lakatta,E.G., Mulas,A., Orru,M., Schlessinger,D., Uda,M.,
            Markus,M.R., Volker,U., Snieder,H., Spector,T.D., Arnlov,J.,
            Lind,L., Sundstrom,J., Syvanen,A.C., Kivimaki,M., Kahonen,M.,
            Mononen,N., Raitakari,O.T., Viikari,J.S., Adamkova,V., Kiechl,S.,
            Brion,M., Nicolaides,A.N., Paulweber,B., Haerting,J.,
            Dominiczak,A.F., Nyberg,F., Whincup,P.H., Hingorani,A.D.,
            Schott,J.J., Bezzina,C.R., Ingelsson,E., Ferrucci,L., Gasparini,P.,
            Wilson,J.F., Rudan,I., Franke,A., Muhleisen,T.W., Pramstaller,P.P.,
            Lehtimaki,T.J., Paterson,A.D., Parsa,A., Liu,Y., van Duijn,C.M.,
            Siscovick,D.S., Gudnason,V., Jamshidi,Y., Salomaa,V., Felix,S.B.,
            Sanna,S., Ritchie,M.D., Stricker,B.H., Stefansson,K., Boyer,L.A.,
            Cappola,T.P., Olsen,J.V., Lage,K., Schwartz,P.J., Kaab,S.,
            Chakravarti,A., Ackerman,M.J., Pfeufer,A., de Bakker,P.I. and
            Newton-Cheh,C.
  CONSRTM   CARe Consortium; COGENT Consortium; DCCT/EDIC; eMERGE Consortium;
            HRGEN Consortium
  TITLE     Genetic association study of QT interval highlights role for
            calcium signaling pathways in myocardial repolarization
  JOURNAL   Nat Genet 46 (8), 826-836 (2014)
   PUBMED   24952745
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Couch,F.J., Wang,X., Bamlet,W.R., de Andrade,M., Petersen,G.M. and
            McWilliams,R.R.
  TITLE     Association of mitotic regulation pathway polymorphisms with
            pancreatic cancer risk and outcome
  JOURNAL   Cancer Epidemiol Biomarkers Prev 19 (1), 251-257 (2010)
   PUBMED   20056645
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 119)
  AUTHORS   Dalmasso,C., Carpentier,W., Meyer,L., Rouzioux,C., Goujard,C.,
            Chaix,M.L., Lambotte,O., Avettand-Fenoel,V., Le Clerc,S., de
            Senneville,L.D., Deveau,C., Boufassa,F., Debre,P., Delfraissy,J.F.,
            Broet,P. and Theodorou,I.
  CONSRTM   ANRS Genome Wide Association 01
  TITLE     Distinct genetic loci control plasma HIV-RNA and cellular HIV-DNA
            levels in HIV-1 infection: the ANRS Genome Wide Association 01
            study
  JOURNAL   PLoS One 3 (12), e3907 (2008)
   PUBMED   19107206
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 119)
  AUTHORS   Hosono,K., Sasaki,T., Minoshima,S. and Shimizu,N.
  TITLE     Identification and characterization of a novel gene family YPEL in
            a wide spectrum of eukaryotic species
  JOURNAL   Gene 340 (1), 31-43 (2004)
   PUBMED   15556292
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091059.12, AI540782.1 and AB098736.1.
            
            On Oct 2, 2004 this sequence version replaced XP_371070.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.235628.1,
                                           SRR1660805.80393.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312655.9/ ENSP00000312272.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q22"
     Protein         1..119
                     /product="protein yippee-like 2"
                     /note="DiGeorge syndrome-related protein"
                     /calculated_mol_wt=13446
     Region          20..110
                     /region_name="RLR_C_like"
                     /note="C-terminal domain of Retinoic acid-inducible gene
                     (RIG)-I-like Receptors, Cereblon (CRBN), and similar
                     protein domains; cl13152"
                     /db_xref="CDD:472430"
     CDS             1..119
                     /gene="YPEL2"
                     /gene_synonym="FKSG4"
                     /coded_by="NM_001005404.4:366..725"
                     /db_xref="CCDS:CCDS32695.1"
                     /db_xref="GeneID:388403"
                     /db_xref="HGNC:HGNC:18326"
                     /db_xref="MIM:609723"
ORIGIN      
        1 mvkmtrsktf qaylpschrt yscihcrahl anhdelisks fqgsqgrayl fnsvvnvgcg
       61 paeervlltg lhavadiyce nckttlgwky ehafessqky kegkyiiela hmikdngwd
//
LOCUS       NP_112601                476 aa            linear   PRI 27-APR-2025
DEFINITION  probable serine carboxypeptidase CPVL isoform b precursor [Homo
            sapiens].
ACCESSION   NP_112601
VERSION     NP_112601.3
DBSOURCE    REFSEQ: accession NM_031311.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Wang,X., Chen,L., Huang,K., Lin,Y., Hong,Y. and Lin,Z.
  TITLE     CPVL suppresses metastasis of nasopharyngeal carcinoma through
            inhibiting epithelial-mesenchymal transition
  JOURNAL   J Cancer Res Clin Oncol 149 (18), 16473-16488 (2023)
   PUBMED   37712963
  REMARK    GeneRIF: CPVL suppresses metastasis of nasopharyngeal carcinoma
            through inhibiting epithelial-mesenchymal transition.
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Kanazawa,T., Ikeda,M., Glatt,S.J., Tsutsumi,A., Kikuyama,H.,
            Kawamura,Y., Nishida,N., Miyagawa,T., Hashimoto,R., Takeda,M.,
            Sasaki,T., Tokunaga,K., Koh,J., Iwata,N. and Yoneda,H.
  TITLE     Genome-wide association study of atypical psychosis
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 162B (7), 679-686 (2013)
   PUBMED   24132900
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Hu,C., Zhang,R., Yu,W., Wang,J., Wang,C., Pang,C., Ma,X., Bao,Y.,
            Xiang,K. and Jia,W.
  TITLE     CPVL/CHN2 genetic variant is associated with diabetic retinopathy
            in Chinese type 2 diabetic patients
  JOURNAL   Diabetes 60 (11), 3085-3089 (2011)
   PUBMED   21911749
  REMARK    GeneRIF: genetic association studies in a Chinese population with
            type 2 diabetes: An SNP in CPVL (rs39059) is associated with
            diabetic retinopathy in a Chinese population of type 2 diabetic
            patients.
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Maeda,S., Araki,S., Babazono,T., Toyoda,M., Umezono,T., Kawai,K.,
            Imanishi,M., Uzu,T., Watada,H., Suzuki,D., Kashiwagi,A.,
            Iwamoto,Y., Kaku,K., Kawamori,R. and Nakamura,Y.
  TITLE     Replication study for the association between four Loci identified
            by a genome-wide association study on European American subjects
            with type 1 diabetes and susceptibility to diabetic nephropathy in
            Japanese subjects with type 2 diabetes
  JOURNAL   Diabetes 59 (8), 2075-2079 (2010)
   PUBMED   20460425
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Meigs,J.B., Manning,A.K., Fox,C.S., Florez,J.C., Liu,C.,
            Cupples,L.A. and Dupuis,J.
  TITLE     Genome-wide association with diabetes-related traits in the
            Framingham Heart Study
  JOURNAL   BMC Med Genet 8 Suppl 1 (Suppl 1), S16 (2007)
   PUBMED   17903298
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Mahoney,J.A., Ntolosi,B., DaSilva,R.P., Gordon,S. and McKnight,A.J.
  TITLE     Cloning and characterization of CPVL, a novel serine
            carboxypeptidase, from human macrophages
  JOURNAL   Genomics 72 (3), 243-251 (2001)
   PUBMED   11401439
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Ignatovich,O., Tomlinson,I.M., Popov,A.V., Bruggemann,M. and
            Winter,G.
  TITLE     Dominance of intrinsic genetic factors in shaping the human
            immunoglobulin Vlambda repertoire
  JOURNAL   J Mol Biol 294 (2), 457-465 (1999)
   PUBMED   10610771
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Wang,X. and Stollar,B.D.
  TITLE     Immunoglobulin VH gene expression in human aging
  JOURNAL   Clin Immunol 93 (2), 132-142 (1999)
   PUBMED   10527689
  REMARK    Erratum:[Clin Immunol 2000 Mar;94(3):219]
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Striebich,C.C., Falta,M.T., Wang,Y., Bill,J. and Kotzin,B.L.
  TITLE     Selective accumulation of related CD4+ T cell clones in the
            synovial fluid of patients with rheumatoid arthritis
  JOURNAL   J Immunol 161 (8), 4428-4436 (1998)
   PUBMED   9780222
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK075433.1 and AC005162.1.
            
            On Dec 14, 2005 this sequence version replaced NP_112601.2.
            
            Summary: The protein encoded by this gene is a carboxypeptidase and
            bears strong sequence similarity to serine carboxypeptidases.
            Carboxypeptidases are a large class of proteases that act to cleave
            a single amino acid from the carboxy termini of proteins or
            peptides. The exact function of this protein, however, has not been
            determined. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 5. Variants 1-12 all encode the same isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.21304.1, AY358549.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265394.10/ ENSP00000265394.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..476
                     /product="probable serine carboxypeptidase CPVL isoform b
                     precursor"
                     /note="vitellogenic carboxypeptidase-like protein;
                     VCP-like protein; probable serine carboxypeptidase CPVL;
                     carboxypeptidase WUG; CP-Mac carboxypeptidase"
                     /calculated_mol_wt=51865
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2317
     Region          69..468
                     /region_name="Peptidase_S10"
                     /note="Serine carboxypeptidase; pfam00450"
                     /db_xref="CDD:459815"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9H3G5.2)"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9H3G5.2)"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3G5.2)"
     Site            346
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9H3G5.2)"
     CDS             1..476
                     /gene="CPVL"
                     /gene_synonym="HVLP"
                     /coded_by="NM_031311.5:120..1550"
                     /note="isoform b precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS5419.1"
                     /db_xref="GeneID:54504"
                     /db_xref="HGNC:HGNC:14399"
                     /db_xref="MIM:609780"
ORIGIN      
        1 mvgamwkviv slvllmpgpc dglfrslyrs vsmppkgdsg qplfltpyie agkiqkgrel
       61 slvgpfpgln mksyagfltv nktynsnlff wffpaqiqpe dapvvlwlqg gpggssmfgl
      121 fvehgpyvvt snmtlrdrdf pwtttlsmly idnpvgtgfs ftddthgyav neddvardly
      181 saliqffqif peyknndfyv tgesyagkyv paiahlihsl npvrevkinl ngiaigdgys
      241 dpesiiggya eflyqiglld ekqkkyfqkq checiehirk qnwfeafeil dklldgdlts
      301 dpsyfqnvtg csnyynflrc tepedqlyyv kflslpevrq aihvgnqtfn dgtivekylr
      361 edtvqsvkpw lteimnnykv liyngqldii vaaaltersl mgmdwkgsqe ykkaekkvwk
      421 ifksdsevag yirqagdfhq viirggghil pydqplrafd minrfiygkg wdpyvg
//
LOCUS       NP_001108206             370 aa            linear   PRI 27-APR-2025
DEFINITION  polyadenylate-binding protein 4-like [Homo sapiens].
ACCESSION   NP_001108206
VERSION     NP_001108206.3
DBSOURCE    REFSEQ: accession NM_001114734.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Aslam,M., Ullah,A., Paramasivam,N., Kandasamy,N., Naureen,S.,
            Badshah,M., Khan,K., Wajid,M., Abbasi,R., Eils,R., Brockmann,M.A.,
            Schlesner,M., Ahmad,N. and von Engelhardt,J.
  TITLE     Segregation and potential functional impact of a rare stop-gain
            PABPC4L variant in familial atypical Parkinsonism
  JOURNAL   Sci Rep 9 (1), 13576 (2019)
   PUBMED   31537871
  REMARK    GeneRIF: Segregation and potential functional impact of a rare
            stop-gain PABPC4L variant in familial atypical Parkinsonism.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Randall,J.C., Winkler,T.W., Kutalik,Z., Berndt,S.I., Jackson,A.U.,
            Monda,K.L., Kilpelainen,T.O., Esko,T., Magi,R., Li,S.,
            Workalemahu,T., Feitosa,M.F., Croteau-Chonka,D.C., Day,F.R.,
            Fall,T., Ferreira,T., Gustafsson,S., Locke,A.E., Mathieson,I.,
            Scherag,A., Vedantam,S., Wood,A.R., Liang,L., Steinthorsdottir,V.,
            Thorleifsson,G., Dermitzakis,E.T., Dimas,A.S., Karpe,F., Min,J.L.,
            Nicholson,G., Clegg,D.J., Person,T., Krohn,J.P., Bauer,S.,
            Buechler,C., Eisinger,K., Bonnefond,A., Froguel,P., Hottenga,J.J.,
            Prokopenko,I., Waite,L.L., Harris,T.B., Smith,A.V., Shuldiner,A.R.,
            McArdle,W.L., Caulfield,M.J., Munroe,P.B., Gronberg,H., Chen,Y.D.,
            Li,G., Beckmann,J.S., Johnson,T., Thorsteinsdottir,U.,
            Teder-Laving,M., Khaw,K.T., Wareham,N.J., Zhao,J.H., Amin,N.,
            Oostra,B.A., Kraja,A.T., Province,M.A., Cupples,L.A.,
            Heard-Costa,N.L., Kaprio,J., Ripatti,S., Surakka,I., Collins,F.S.,
            Saramies,J., Tuomilehto,J., Jula,A., Salomaa,V., Erdmann,J.,
            Hengstenberg,C., Loley,C., Schunkert,H., Lamina,C., Wichmann,H.E.,
            Albrecht,E., Gieger,C., Hicks,A.A., Johansson,A., Pramstaller,P.P.,
            Kathiresan,S., Speliotes,E.K., Penninx,B., Hartikainen,A.L.,
            Jarvelin,M.R., Gyllensten,U., Boomsma,D.I., Campbell,H.,
            Wilson,J.F., Chanock,S.J., Farrall,M., Goel,A., Medina-Gomez,C.,
            Rivadeneira,F., Estrada,K., Uitterlinden,A.G., Hofman,A.,
            Zillikens,M.C., den Heijer,M., Kiemeney,L.A., Maschio,A., Hall,P.,
            Tyrer,J., Teumer,A., Volzke,H., Kovacs,P., Tonjes,A., Mangino,M.,
            Spector,T.D., Hayward,C., Rudan,I., Hall,A.S., Samani,N.J.,
            Attwood,A.P., Sambrook,J.G., Hung,J., Palmer,L.J., Lokki,M.L.,
            Sinisalo,J., Boucher,G., Huikuri,H., Lorentzon,M., Ohlsson,C.,
            Eklund,N., Eriksson,J.G., Barlassina,C., Rivolta,C., Nolte,I.M.,
            Snieder,H., Van der Klauw,M.M., Van Vliet-Ostaptchouk,J.V.,
            Gejman,P.V., Shi,J., Jacobs,K.B., Wang,Z., Bakker,S.J., Mateo
            Leach,I., Navis,G., van der Harst,P., Martin,N.G., Medland,S.E.,
            Montgomery,G.W., Yang,J., Chasman,D.I., Ridker,P.M., Rose,L.M.,
            Lehtimaki,T., Raitakari,O., Absher,D., Iribarren,C., Basart,H.,
            Hovingh,K.G., Hypponen,E., Power,C., Anderson,D., Beilby,J.P.,
            Hui,J., Jolley,J., Sager,H., Bornstein,S.R., Schwarz,P.E.,
            Kristiansson,K., Perola,M., Lindstrom,J., Swift,A.J., Uusitupa,M.,
            Atalay,M., Lakka,T.A., Rauramaa,R., Bolton,J.L., Fowkes,G.,
            Fraser,R.M., Price,J.F., Fischer,K., Krjuta Kov,K., Metspalu,A.,
            Mihailov,E., Langenberg,C., Luan,J., Ong,K.K., Chines,P.S.,
            Keinanen-Kiukaanniemi,S.M., Saaristo,T.E., Edkins,S., Franks,P.W.,
            Hallmans,G., Shungin,D., Morris,A.D., Palmer,C.N., Erbel,R.,
            Moebus,S., Nothen,M.M., Pechlivanis,S., Hveem,K., Narisu,N.,
            Hamsten,A., Humphries,S.E., Strawbridge,R.J., Tremoli,E.,
            Grallert,H., Thorand,B., Illig,T., Koenig,W., Muller-Nurasyid,M.,
            Peters,A., Boehm,B.O., Kleber,M.E., Marz,W., Winkelmann,B.R.,
            Kuusisto,J., Laakso,M., Arveiler,D., Cesana,G., Kuulasmaa,K.,
            Virtamo,J., Yarnell,J.W., Kuh,D., Wong,A., Lind,L., de Faire,U.,
            Gigante,B., Magnusson,P.K., Pedersen,N.L., Dedoussis,G.,
            Dimitriou,M., Kolovou,G., Kanoni,S., Stirrups,K., Bonnycastle,L.L.,
            Njolstad,I., Wilsgaard,T., Ganna,A., Rehnberg,E., Hingorani,A.,
            Kivimaki,M., Kumari,M., Assimes,T.L., Barroso,I., Boehnke,M.,
            Borecki,I.B., Deloukas,P., Fox,C.S., Frayling,T., Groop,L.C.,
            Haritunians,T., Hunter,D., Ingelsson,E., Kaplan,R., Mohlke,K.L.,
            O'Connell,J.R., Schlessinger,D., Strachan,D.P., Stefansson,K., van
            Duijn,C.M., Abecasis,G.R., McCarthy,M.I., Hirschhorn,J.N., Qi,L.,
            Loos,R.J., Lindgren,C.M., North,K.E. and Heid,I.M.
  CONSRTM   DIAGRAM Consortium; MAGIC Investigators
  TITLE     Sex-stratified genome-wide association studies including 270,000
            individuals show sexual dimorphism in genetic loci for
            anthropometric traits
  JOURNAL   PLoS Genet 9 (6), e1003500 (2013)
   PUBMED   23754948
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC015631.10, DR005318.1 and BX648831.1.
            
            On May 24, 2018 this sequence version replaced NP_001108206.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1839220.1,
                                           SRR18074967.536178.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000421491.4/
                                                ENSP00000463233.1
            RefSeq Select criteria           :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.3"
     Protein         1..370
                     /product="polyadenylate-binding protein 4-like"
                     /note="PABP-4-like"
                     /calculated_mol_wt=41723
     Region          10..>369
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..370
                     /gene="PABPC4L"
                     /coded_by="NM_001114734.2:299..1411"
                     /db_xref="CCDS:CCDS47135.1"
                     /db_xref="GeneID:132430"
                     /db_xref="HGNC:HGNC:31955"
ORIGIN      
        1 mnvaakyrma slyvgdlhad vtedllfrkf stvgpvlsir icrdqvtrrs lgyayvnflq
       61 ladaqkaldt mnfdiikgks irlmwsqrda ylrrsgignv fiknldksid nktlyehfsa
      121 fgkilsskvm sddqgskgya fvhfqnqsaa draieemngk llkgckvfvg rfknrkdrea
      181 elrskaseft nvyiknfggd mdderlkdvf skygktlsvk vmtdssgksk gfgfvsfdsh
      241 eaakkaveem ngrdingqli fvgraqkkve rqaelkqmfe qlkrerirgc qgvklyiknl
      301 ddtiddeklr nefssfgsis rvkvmqeegq skgfglicfs spedatkamt emngrilgsk
      361 plsialaqrh
//
LOCUS       NP_644670                541 aa            linear   PRI 27-APR-2025
DEFINITION  EH domain-containing protein 4 [Homo sapiens].
ACCESSION   NP_644670
VERSION     NP_644670.1
DBSOURCE    REFSEQ: accession NM_139265.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Malinova,T.S., Angulo-Urarte,A., Nuchel,J., Tauber,M., van der
            Stoel,M.M., Janssen,V., de Haan,A., Groenen,A.G., Tebbens,M.,
            Graupera,M., Plomann,M. and Huveneers,S.
  TITLE     A junctional PACSIN2/EHD4/MICAL-L1 complex coordinates VE-cadherin
            trafficking for endothelial migration and angiogenesis
  JOURNAL   Nat Commun 12 (1), 2610 (2021)
   PUBMED   33972531
  REMARK    GeneRIF: A junctional PACSIN2/EHD4/MICAL-L1 complex coordinates
            VE-cadherin trafficking for endothelial migration and angiogenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Lin,Y.S., Huang,K.Y., Yu,H.C., Lu,M.C., Fan,C.J., Huang Tseng,H.Y.,
            Jhuang,B.Y., Liu,S.Q., Lai,N.S., Lin,T.H. and Huang,H.B.
  TITLE     Identification of phostensin in association with Eps 15 homology
            domain-containing protein 1 (EHD1) and EHD4
  JOURNAL   Biochem Biophys Res Commun 531 (2), 236-241 (2020)
   PUBMED   32800345
  REMARK    GeneRIF: Identification of phostensin in association with Eps 15
            homology domain-containing protein 1 (EHD1) and EHD4.
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Jones,T., Naslavsky,N. and Caplan,S.
  TITLE     Eps15 Homology Domain Protein 4 (EHD4) is required for Eps15
            Homology Domain Protein 1 (EHD1)-mediated endosomal recruitment and
            fission
  JOURNAL   PLoS One 15 (9), e0239657 (2020)
   PUBMED   32966336
  REMARK    GeneRIF: Eps15 Homology Domain Protein 4 (EHD4) is required for
            Eps15 Homology Domain Protein 1 (EHD1)-mediated endosomal
            recruitment and fission.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Sharma,M., Naslavsky,N. and Caplan,S.
  TITLE     A role for EHD4 in the regulation of early endosomal transport
  JOURNAL   Traffic 9 (6), 995-1018 (2008)
   PUBMED   18331452
  REMARK    GeneRIF: EHD4 is involved in the control of trafficking at the
            early endosome and regulates exit of cargo toward both the
            recycling compartment and the late endocytic pathway.
REFERENCE   8  (residues 1 to 541)
  AUTHORS   George,M., Ying,G., Rainey,M.A., Solomon,A., Parikh,P.T., Gao,Q.,
            Band,V. and Band,H.
  TITLE     Shared as well as distinct roles of EHD proteins revealed by
            biochemical and functional comparisons in mammalian cells and C.
            elegans
  JOURNAL   BMC Cell Biol 8, 3 (2007)
   PUBMED   17233914
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Kuo,H.J., Tran,N.T., Clary,S.A., Morris,N.P. and Glanville,R.W.
  TITLE     Characterization of EHD4, an EH domain-containing protein expressed
            in the extracellular matrix
  JOURNAL   J Biol Chem 276 (46), 43103-43110 (2001)
   PUBMED   11533061
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Pohl,U., Smith,J.S., Tachibana,I., Ueki,K., Lee,H.K., Ramaswamy,S.,
            Wu,Q., Mohrenweiser,H.W., Jenkins,R.B. and Louis,D.N.
  TITLE     EHD2, EHD3, and EHD4 encode novel members of a highly conserved
            family of EH domain-containing proteins
  JOURNAL   Genomics 63 (2), 255-262 (2000)
   PUBMED   10673336
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP314075.1, BC051823.1, AK292634.1, CF541306.1, AC039056.7 and
            AC020659.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.18768.1,
                                           SRR1660807.224957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2155974
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000220325.9/ ENSP00000220325.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1"
     Protein         1..541
                     /product="EH domain-containing protein 4"
                     /note="ortholog of rat pincher; hepatocellular
                     carcinoma-associated protein HCA11; PAST homolog 4;
                     hepatocellular carcinoma-associated protein 10/11"
                     /calculated_mol_wt=61044
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4M9; propagated from
                     UniProtKB/Swiss-Prot (Q9H223.1)"
     Region          27..59
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Region          63..303
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Region          68..75
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H223.1)"
     Site            68..75
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(73..76,156,223,225,259..261)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Region          94..95
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H223.1)"
     Site            97
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            101..103
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Region          156..159
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H223.1)"
     Site            156..159
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(158..159,186..187)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H223.1)"
     Region          222..225
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H223.1)"
     Site            222..225
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Region          246
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H223.1)"
     Site            259..261
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     Region          292..397
                     /region_name="DUF5600"
                     /note="Domain of unknown function (DUF5600); pfam18150"
                     /db_xref="CDD:465667"
     Region          441..534
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q9H223.1)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H223.1)"
     CDS             1..541
                     /gene="EHD4"
                     /gene_synonym="PAST4"
                     /coded_by="NM_139265.4:64..1689"
                     /db_xref="CCDS:CCDS10081.1"
                     /db_xref="GeneID:30844"
                     /db_xref="HGNC:HGNC:3245"
                     /db_xref="MIM:605892"
ORIGIN      
        1 mfswmgrqag greraggada vqtvtgglrs lylrkvlple eayrfhefhs paledadfen
       61 kpmillvgqy stgkttfiry lleqdfpgmr igpepttdsf iavmygeteg stpgnalvvd
      121 pkkpfrklsr fgnaflnrfm csqlpnqvlk sisvidspgi lsgekqrisr gydfcqvlqw
      181 faervdriil lfdahkldis defseaikaf rgqddkirvv lnkadqvdtq qlmrvygalm
      241 wslgkvintp evlrvyigsf waqplqntdn rrlfeaeaqd lfrdiqslpq kaavrklndl
      301 ikrarlakvh ayiisylkke mpsvfgkenk krelisrlpe iyiqlqreyq isagdfpevk
      361 amqeqlenyd ftkfhslkpk lieavdnmls nkisplmnli sqeetstptq lvqggafdgt
      421 tegpfnqgyg egakegadee ewvvakdkpv ydelfytlsp ingkisgvna kkemvtsklp
      481 nsvlgkiwkl adcdcdgmld eeefalakhl ikikldgyel psslpphlvp pshrkslpka
      541 d
//
LOCUS       NP_001354984             220 aa            linear   PRI 27-APR-2025
DEFINITION  cell cycle checkpoint control protein RAD9B isoform h [Homo
            sapiens].
ACCESSION   NP_001354984
VERSION     NP_001354984.1
DBSOURCE    REFSEQ: accession NM_001368055.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Barroso-Chinea,P., Salas-Hernandez,J., Cruz-Muros,I.,
            Lopez-Fernandez,J., Freire,R. and Afonso-Oramas,D.
  TITLE     Expression of RAD9B in the mesostriatal system of rats and humans:
            Overexpression in a 6-OHDA rat model of Parkinson's disease
  JOURNAL   Ann Anat 250, 152135 (2023)
   PUBMED   37460044
  REMARK    GeneRIF: Expression of RAD9B in the mesostriatal system of rats and
            humans: Overexpression in a 6-OHDA rat model of Parkinson's
            disease.
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Cao,X., Tian,T., Steele,J.W., Cabrera,R.M., Aguiar-Pulido,V.,
            Wadhwa,S., Bhavani,N., Bi,P., Gargurevich,N.H., Hoffman,E.N.,
            Cai,C.Q., Marini,N.J., Yang,W., Shaw,G.M., Ross,M.E., Finnell,R.H.
            and Lei,Y.
  TITLE     Loss of RAD9B impairs early neural development and contributes to
            the risk for human spina bifida
  JOURNAL   Hum Mutat 41 (4), 786-799 (2020)
   PUBMED   31898828
  REMARK    GeneRIF: Loss of RAD9B impairs early neural development and
            contributes to the risk for human spina bifida.
            Erratum:[Hum Mutat. 2021 Apr;42(4):487. doi: 10.1002/humu.24175.
            PMID: 33856736]
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Lyndaker,A.M., Vasileva,A., Wolgemuth,D.J., Weiss,R.S. and
            Lieberman,H.B.
  TITLE     Clamping down on mammalian meiosis
  JOURNAL   Cell Cycle 12 (19), 3135-3145 (2013)
   PUBMED   24013428
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Perez-Castro,A.J. and Freire,R.
  TITLE     Rad9B responds to nucleolar stress through ATR and JNK signalling,
            and delays the G1-S transition
  JOURNAL   J Cell Sci 125 (Pt 5), 1152-1164 (2012)
   PUBMED   22399810
  REMARK    GeneRIF: Rad9B responds to nucleolar stress after the activation of
            JNK-dependent stress signalling and ATR-dependent DNA damage
            response pathways, and actively accumulates within nucleoli, where
            it does not cause a transcription block.
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Lieberman,H.B.
  TITLE     Rad9, an evolutionarily conserved gene with multiple functions for
            preserving genomic integrity
  JOURNAL   J Cell Biochem 97 (4), 690-697 (2006)
   PUBMED   16365875
  REMARK    GeneRIF: The encoded mammalian proteins participate in promoting
            resistance to DNA damage, cell cycle checkpoint control, DNA
            repair, and apoptosis.
            Review article
REFERENCE   6  (residues 1 to 220)
  AUTHORS   Dufault,V.M., Oestreich,A.J., Vroman,B.T. and Karnitz,L.M.
  TITLE     Identification and characterization of RAD9B, a paralog of the RAD9
            checkpoint gene
  JOURNAL   Genomics 82 (6), 644-651 (2003)
   PUBMED   14611806
REFERENCE   7  (residues 1 to 220)
  AUTHORS   Hopkins,K.M., Wang,X., Berlin,A., Hang,H., Thaker,H.M. and
            Lieberman,H.B.
  TITLE     Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint
            control genes in normal and cancerous testicular tissue
  JOURNAL   Cancer Res 63 (17), 5291-5298 (2003)
   PUBMED   14500360
REFERENCE   8  (residues 1 to 220)
  AUTHORS   Zou,L. and Elledge,S.J.
  TITLE     Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
  JOURNAL   Science 300 (5625), 1542-1548 (2003)
   PUBMED   12791985
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002350.1.
            
            Transcript Variant: This variant (12), as well as variant 11,
            encodes isoform h.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.261751.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..220
                     /product="cell cycle checkpoint control protein RAD9B
                     isoform h"
                     /EC_number="3.1.11.2"
                     /note="DNA repair exonuclease rad9 homolog B; cell cycle
                     checkpoint control protein RAD9B; RAD9 homolog B"
                     /calculated_mol_wt=24109
     Region          <1..79
                     /region_name="Rad9"
                     /note="pfam04139"
                     /db_xref="CDD:427739"
     CDS             1..220
                     /gene="RAD9B"
                     /coded_by="NM_001368055.1:470..1132"
                     /note="isoform h is encoded by transcript variant 12"
                     /db_xref="GeneID:144715"
                     /db_xref="HGNC:HGNC:21700"
                     /db_xref="MIM:608368"
ORIGIN      
        1 mdlsnavhse mfvgsdefdf fqigmdteit fcfkelkgil tfseathapi siyfdfpgkp
       61 lalsiddmlv eanfilatla deqsrasspq slclsqkrkr sdliekkagk nvtgqaleci
      121 skkaaprrly pketltnisa lencgspamk rvdgdvsevs essvsnteev pgslclrkfs
      181 cmffgavssd qqehfnhpfd slarasdsee dmnngsfsif
//
LOCUS       NP_001001995             328 aa            linear   PRI 27-APR-2025
DEFINITION  neuronal membrane glycoprotein M6-b isoform 1 [Homo sapiens].
ACCESSION   NP_001001995
VERSION     NP_001001995.1
DBSOURCE    REFSEQ: accession NM_001001995.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   He,S., Huang,Z., Li,X., Ding,Y., Sheng,H., Liu,B. and Jia,Z.
  TITLE     GPM6B Inhibit PCa Proliferation by Blocking Prostate Cancer Cell
            Serotonin Absorptive Capacity
  JOURNAL   Dis Markers 2020, 8810756 (2020)
   PUBMED   33294057
  REMARK    GeneRIF: GPM6B Inhibit PCa Proliferation by Blocking Prostate
            Cancer Cell Serotonin Absorptive Capacity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Zhang,X., Xie,H., Chang,P., Zhao,H., Xia,Y., Zhang,L., Guo,X.,
            Huang,C., Yan,F., Hu,L., Lin,C., Li,Y., Xiong,Z., Wang,X., Li,G.,
            Deng,L., Wang,S. and Tao,L.
  TITLE     Glycoprotein M6B Interacts with TbetaRI to Activate
            TGF-beta-Smad2/3 Signaling and Promote Smooth Muscle Cell
            Differentiation
  JOURNAL   Stem Cells 37 (2), 190-201 (2019)
   PUBMED   30372567
  REMARK    GeneRIF: Findings demonstrate that GPM6B plays a crucial role in
            SMC differentiation and regulates SMC differentiation through the
            activation of TGF-beta-Smad2/3 signaling via direct interactions
            with TbetaRI.
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Urban,P., Rabajdova,M.B., Varga,J., Kruzliak,P., Fialkovicova,V.,
            Durovcova,E. and Marekova,M.
  TITLE     Vascular marker expression during the development of various types
            of gynaecological malignancy
  JOURNAL   Tumour Biol 35 (11), 11229-11235 (2014)
   PUBMED   25113253
  REMARK    GeneRIF: Increase in the expression levels of mRNA and protein for
            the Gpm6B is associated with various types of gynaecological
            malignancy.
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Henneke,M., Wehner,L.E., Hennies,H.C., Preuss,N. and Gartner,J.
  TITLE     Mutation analysis of the M6b gene in patients with
            Pelizaeus-Merzbacher-like syndrome
  JOURNAL   Am J Med Genet A 128A (2), 156-158 (2004)
   PUBMED   15214007
  REMARK    GeneRIF: it is unlikely that mutations in M6B have a role in
            Pelizaeus-Merzbacher-like syndrome, as examined in eight patients
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Werner,H., Dimou,L., Klugmann,M., Pfeiffer,S. and Nave,K.A.
  TITLE     Multiple splice isoforms of proteolipid M6B in neurons and
            oligodendrocytes
  JOURNAL   Mol Cell Neurosci 18 (6), 593-605 (2001)
   PUBMED   11749036
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Yoshida,M., Shan,W.S. and Colman,D.R.
  TITLE     Conserved and divergent expression patterns of the proteolipid
            protein gene family in the amphibian central nervous system
  JOURNAL   J Neurosci Res 57 (1), 13-22 (1999)
   PUBMED   10397631
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Narayanan,V., Olinsky,S., Dahle,E., Naidu,S. and Zoghbi,H.Y.
  TITLE     Mutation analysis of the M6b gene in patients with Rett syndrome
  JOURNAL   Am J Med Genet 78 (2), 165-168 (1998)
   PUBMED   9674909
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Olinsky,S., Loop,B.T., DeKosky,A., Ripepi,B., Weng,W., Cummins,J.,
            Wenger,S.L., Yan,Y., Lagenaur,C. and Narayanan,V.
  TITLE     Chromosomal mapping of the human M6 genes
  JOURNAL   Genomics 33 (3), 532-536 (1996)
   PUBMED   8661015
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Yan,Y., Lagenaur,C. and Narayanan,V.
  TITLE     Molecular cloning of M6: identification of a PLP/DM20 gene family
  JOURNAL   Neuron 11 (3), 423-431 (1993)
   PUBMED   8398137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA191910.1, BC047295.1,
            BG532134.1, AK095657.1, AL119977.1, AA991690.1, BI669888.1 and
            AC003037.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a membrane glycoprotein that belongs to
            the proteolipid protein family. Proteolipid protein family members
            are expressed in most brain regions and are thought to be involved
            in cellular housekeeping functions such as membrane trafficking and
            cell-to-cell communication. This protein may also be involved in
            osteoblast differentiation. Alternate splicing results in multiple
            transcript variants. Pseudogenes of this gene are located on
            chromosomes Y and 22. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longest protein
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.34840.1,
                                           SRR1660807.75799.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316715.9/ ENSP00000316861.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..328
                     /product="neuronal membrane glycoprotein M6-b isoform 1"
                     /note="protolipid M6B; neuronal membrane glycoprotein
                     M6-b"
                     /calculated_mol_wt=36089
     Region          63..298
                     /region_name="Myelin_PLP"
                     /note="Myelin proteolipid protein (PLP or lipophilin);
                     pfam01275"
                     /db_xref="CDD:460144"
     CDS             1..328
                     /gene="GPM6B"
                     /gene_synonym="M6B"
                     /coded_by="NM_001001995.3:190..1176"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35206.1"
                     /db_xref="GeneID:2824"
                     /db_xref="HGNC:HGNC:4461"
                     /db_xref="MIM:300051"
ORIGIN      
        1 mkpametaae enteqsqerk vnsraemeig ryhwmypgsk nhqyhpvptl gdrasplssp
       61 gcfeccikcl ggvpyaslva tilcfsgval fcgcghvala gtvaileqhf stnasdhall
      121 seviqlmqyv iygiasfffl ygiillaegf yttsavkelh gefkttacgr cisgmfvflt
      181 yvlgvawlgv fgfsavpvfm fyniwstcev ikspqtngtt gveqicvdir qygiipwnaf
      241 pgkicgsale nicntnefym syhlfivaca gagatviali hflmilssnw aylkdaskmq
      301 ayqdikakee qelqdiqsrs keqlnsyt
//
LOCUS       NP_694945                802 aa            linear   PRI 27-APR-2025
DEFINITION  rho guanine nucleotide exchange factor 19 [Homo sapiens].
ACCESSION   NP_694945
VERSION     NP_694945.2
DBSOURCE    REFSEQ: accession NM_153213.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Omble,A., Mahajan,S., Bhoite,A. and Kulkarni,K.
  TITLE     Dishevelled2 activates WGEF via its interaction with a unique
            internal peptide motif of the GEF
  JOURNAL   Commun Biol 7 (1), 543 (2024)
   PUBMED   38714795
  REMARK    GeneRIF: Dishevelled2 activates WGEF via its interaction with a
            unique internal peptide motif of the GEF.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Wang,Z., Kan,G., Sheng,C., Yao,C., Mao,Y. and Chen,S.
  TITLE     ARHGEF19 regulates MAPK/ERK signaling and promotes the progression
            of small cell lung cancer
  JOURNAL   Biochem Biophys Res Commun 533 (4), 792-799 (2020)
   PUBMED   32993957
  REMARK    GeneRIF: ARHGEF19 regulates MAPK/ERK signaling and promotes the
            progression of small cell lung cancer.
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Li,Y., Ye,Z., Chen,S., Pan,Z., Zhou,Q., Li,Y.Z., Shuai,W.D.,
            Kuang,C.M., Peng,Q.H., Shi,W., Mao,X., Liu,R.Y. and Huang,W.
  TITLE     ARHGEF19 interacts with BRAF to activate MAPK signaling during the
            tumorigenesis of non-small cell lung cancer
  JOURNAL   Int J Cancer 142 (7), 1379-1391 (2018)
   PUBMED   29164615
  REMARK    GeneRIF: These findings suggest that ARHGEF19 upregulation, due to
            the low expression of miR-29 in non-small cell lung cancer tissues,
            may play a crucial role in non-small cell lung cancer tumorigenesis
            by activating MAPK signaling
REFERENCE   5  (residues 1 to 802)
  AUTHORS   Zhou,J., Tao,Y., Peng,C., Gu,P. and Wang,W.
  TITLE     miR-503 regulates metastatic function through Rho guanine
            nucleotide exchanger factor 19 in hepatocellular carcinoma
  JOURNAL   J Surg Res 188 (1), 129-136 (2014)
   PUBMED   24405610
  REMARK    GeneRIF: overcomes the suppressive influence of miR-503 in
            hepatocellular carcinoma cells
REFERENCE   6  (residues 1 to 802)
  AUTHORS   Caddy,J., Wilanowski,T., Darido,C., Dworkin,S., Ting,S.B., Zhao,Q.,
            Rank,G., Auden,A., Srivastava,S., Papenfuss,T.A., Murdoch,J.N.,
            Humbert,P.O., Parekh,V., Boulos,N., Weber,T., Zuo,J.,
            Cunningham,J.M. and Jane,S.M.
  TITLE     Epidermal wound repair is regulated by the planar cell polarity
            signaling pathway
  JOURNAL   Dev Cell 19 (1), 138-147 (2010)
   PUBMED   20643356
  REMARK    Erratum:[Dev Cell. 2010 Aug 17;19(2):353. Parekh, Vishwas [added]]
REFERENCE   7  (residues 1 to 802)
  AUTHORS   Horii,T., Morita,S., Kimura,M. and Hatada,I.
  TITLE     Epigenetic regulation of adipocyte differentiation by a Rho guanine
            nucleotide exchange factor, WGEF
  JOURNAL   PLoS One 4 (6), e5809 (2009)
   PUBMED   19503838
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 802)
  AUTHORS   Tanegashima,K., Zhao,H. and Dawid,I.B.
  TITLE     WGEF activates Rho in the Wnt-PCP pathway and controls convergent
            extension in Xenopus gastrulation
  JOURNAL   EMBO J 27 (4), 606-617 (2008)
   PUBMED   18256687
REFERENCE   9  (residues 1 to 802)
  AUTHORS   Wang,Y., Suzuki,H., Yokoo,T., Tada-Iida,K., Kihara,R., Miura,M.,
            Watanabe,K., Sone,H., Shimano,H., Toyoshima,H. and Yamada,N.
  TITLE     WGEF is a novel RhoGEF expressed in intestine, liver, heart, and
            kidney
  JOURNAL   Biochem Biophys Res Commun 324 (3), 1053-1058 (2004)
   PUBMED   15485661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK297707.1, BC040640.1 and AL137736.1.
            
            On Dec 20, 2003 this sequence version replaced NP_694945.1.
            
            Summary: Guanine nucleotide exchange factors (GEFs) such as
            ARHGEF19 accelerate the GTPase activity of Rho GTPases (see RHOA,
            MIM 165390).[supplied by OMIM, Dec 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040640.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270747.8/ ENSP00000270747.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..802
                     /product="rho guanine nucleotide exchange factor 19"
                     /note="weakly similar to Rho GEF; ephexin-2; Rho guanine
                     nucleotide exchange factor (GEF) 19; ephexin2"
                     /calculated_mol_wt=89067
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW93.1)"
     Region          10..>353
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          84..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW93.1)"
     Region          171..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW93.1)"
     Region          222..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW93.1)"
     Region          306..342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW93.1)"
     Region          382..558
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          580..706
                     /region_name="PH_ephexin"
                     /note="Ephexin Pleckstrin homology (PH) domain; cd01221"
                     /db_xref="CDD:269929"
     Region          719..773
                     /region_name="SH3_ARHGEF5_19"
                     /note="Src homology 3 domain of the Rho guanine nucleotide
                     exchange factors ARHGEF5 and ARHGEF19; cd11940"
                     /db_xref="CDD:212873"
     Site            order(724,726,729,733,751..752,767,769..770)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212873"
     CDS             1..802
                     /gene="ARHGEF19"
                     /gene_synonym="WGEF"
                     /coded_by="NM_153213.5:181..2589"
                     /db_xref="CCDS:CCDS170.1"
                     /db_xref="GeneID:128272"
                     /db_xref="HGNC:HGNC:26604"
                     /db_xref="MIM:612496"
ORIGIN      
        1 mdcgppatlq phltgppgta hhpvavcqqe slsfaelpal kppspvcldl fpvapeelra
       61 pgsrwslgtp aplqgllwpl spggsdteit sggmrpsrag swphcpgaqp palegpwspr
      121 htqpqrrash gsekksawrk mrvyqreevp gcpeahavfl epgqvvqeqa lsteeprvel
      181 sgstrvsleg perrrfsase lmtrlhsslr lgrnsaaral isgsgtgaar egkasgmear
      241 svemsgdrvs rpapgdsreg dwseprldtq eepplgsrst nerrqsrfll nsvlyqeysd
      301 vasarelrrq qreeegpgde aegaeegpgp pranlspsss fraqrsargs tfslwqdipd
      361 vrgsgvlatl slrdcklqea kfelitseas yihslsvavg hflgsaelse clgaqdkqwl
      421 fsklpevkst serflqdleq rleadvlrfs vcdvvldhcp afrrvylpyv tnqayqerty
      481 qrlllenprf pgilarlees pvcqrlplts flilpfqrit rlkmlvenil krtaqgsede
      541 dmatkafnal kelvqecnas vqsmkrteel ihlskkihfe gkifplisqa rwlvrhgelv
      601 elaplpaapp aklklsskav ylhlfndcll lsrrkelgkf avfvhakmae lqvrdlslkl
      661 qgipghvfll qllhgqhmkh qfllrartes ekqrwisalc psspqedkev isegedcpqv
      721 qcvrtykalh pdeltlektd ilsvrtwtsd gwlegvrlad gekgwvpqay veeisslsar
      781 lrnlrenkrv tsatsklgea pv
//
LOCUS       NP_653182                354 aa            linear   PRI 27-APR-2025
DEFINITION  trans-3-hydroxy-L-proline dehydratase isoform a [Homo sapiens].
ACCESSION   NP_653182
VERSION     NP_653182.1
DBSOURCE    REFSEQ: accession NM_144581.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Visser,W.F., Verhoeven-Duif,N.M. and de Koning,T.J.
  TITLE     Identification of a human trans-3-hydroxy-L-proline dehydratase,
            the first characterized member of a novel family of proline
            racemase-like enzymes
  JOURNAL   J Biol Chem 287 (26), 21654-21662 (2012)
   PUBMED   22528483
  REMARK    GeneRIF: human trans-3-hydroxy-L-proline dehydratase is the first
            characterized member of a novel family of proline racemase-like
            enzymes
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL159140.4 and AK058165.1.
            
            Summary: The protein encoded by this gene is a dehydratase that
            converts trans-3-hydroxy-L-proline to
            delta(1)-pyrroline-2-carboxylate. This enzyme may function to
            degrade dietary proteins that contain trans-3-hydroxy-L-proline as
            well as other proteins such as collagen IV. The encoded protein can
            be converted to an epimerase by changing a threonine to a cysteine
            at a catalytic site. [provided by RefSeq, Sep 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1041615.1,
                                           SRR1660807.155725.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467147 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247194.9/ ENSP00000247194.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.1"
     Protein         1..354
                     /product="trans-3-hydroxy-L-proline dehydratase isoform a"
                     /EC_number="4.2.1.77"
                     /note="trans-3-hydroxyl-L-proline dehydratase;
                     trans-3-hydroxy-l-proline dehydratase; L-3-hydroxyproline
                     dehydratase (trans-)"
                     /calculated_mol_wt=38007
     Region          22..352
                     /region_name="Pro_racemase"
                     /note="Proline racemase; pfam05544"
                     /db_xref="CDD:398923"
     CDS             1..354
                     /gene="L3HYPDH"
                     /gene_synonym="C14orf149"
                     /coded_by="NM_144581.2:93..1157"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9739.1"
                     /db_xref="GeneID:112849"
                     /db_xref="HGNC:HGNC:20488"
                     /db_xref="MIM:614811"
ORIGIN      
        1 mesalavprl pphdpgtpvl svvdmhtgge plrivlagcp evsgptllak rrymrqhldh
       61 vrrrlmfepr ghrdmygavl vpselpdahl gvlflhnegy ssmcghavla lgrfaldfgl
      121 vpappagtre arvnihcpcg lvtafvaced grshgpvrfh svpafvlatd lmvdvpghgk
      181 vmvdiaygga fyafvtaekl gldicsaktr dlvdaasavt eavkaqfkin hpdsedlafl
      241 ygtiltdgkd aytkepttni cvfadeqvdr sptgsgvtar ialqyhkgll elnqmrafks
      301 satgsvftgk avreakcgdf kavivevsgq ahytgtasfi iedddplrdg fllk
//
LOCUS       NP_001357460             226 aa            linear   PRI 27-APR-2025
DEFINITION  doublesex- and mab-3-related transcription factor 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001357460
VERSION     NP_001357460.1
DBSOURCE    REFSEQ: accession NM_001370531.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Sui,J.D., Tang,Z., Chen,B.P.C., Huang,P., Yang,M.Q., Wang,N.H.,
            Yang,H.N., Tu,H.L., Jiang,Q.M., Zhang,J., Wang,Y. and Wu,Y.Z.
  TITLE     Protein Phosphatase 2A-Dependent Mitotic hnRNPA1 Dephosphorylation
            and TERRA Formation Facilitate Telomere Capping
  JOURNAL   Mol Cancer Res 20 (4), 583-595 (2022)
   PUBMED   34933911
  REMARK    GeneRIF: Protein Phosphatase 2A-Dependent Mitotic hnRNPA1
            Dephosphorylation and TERRA Formation Facilitate Telomere Capping.
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Nie,X., Xiao,D., Ge,Y., Xie,Y., Zhou,H., Zheng,T., Li,X., Liu,H.,
            Huang,H. and Zhao,Y.
  TITLE     TRF2 recruits nucleolar protein TCOF1 to coordinate telomere
            transcription and replication
  JOURNAL   Cell Death Differ 28 (3), 1062-1075 (2021)
   PUBMED   33082515
  REMARK    GeneRIF: TRF2 recruits nucleolar protein TCOF1 to coordinate
            telomere transcription and replication.
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Aschacher,T., Wolf,B., Aschacher,O., Enzmann,F., Laszlo,V.,
            Messner,B., Turkcan,A., Weis,S., Spiegl-Kreinecker,S., Holzmann,K.,
            Laufer,G., Ehrlich,M. and Bergmann,M.
  TITLE     Long interspersed element-1 ribonucleoprotein particles protect
            telomeric ends in alternative lengthening of telomeres dependent
            cells
  JOURNAL   Neoplasia 22 (2), 61-75 (2020)
   PUBMED   31846834
  REMARK    GeneRIF: Long interspersed element-1 ribonucleoprotein particles
            protect telomeric ends in alternative lengthening of telomeres
            dependent cells.
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Feretzaki,M., Renck Nunes,P. and Lingner,J.
  TITLE     Expression and differential regulation of human TERRA at several
            chromosome ends
  JOURNAL   RNA 25 (11), 1470-1480 (2019)
   PUBMED   31350341
  REMARK    GeneRIF: study confirms that TERRA corresponds to a large gene
            family transcribed from multiple chromosome ends where we
            identified two types of TERRA promoters, only one of which is
            regulated by DNA methylation
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Lasky-Su,J., Neale,B.M., Franke,B., Anney,R.J., Zhou,K.,
            Maller,J.B., Vasquez,A.A., Chen,W., Asherson,P., Buitelaar,J.,
            Banaschewski,T., Ebstein,R., Gill,M., Miranda,A., Mulas,F.,
            Oades,R.D., Roeyers,H., Rothenberger,A., Sergeant,J.,
            Sonuga-Barke,E., Steinhausen,H.C., Taylor,E., Daly,M., Laird,N.,
            Lange,C. and Faraone,S.V.
  TITLE     Genome-wide association scan of quantitative traits for attention
            deficit hyperactivity disorder identifies novel associations and
            confirms candidate gene associations
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 147B (8), 1345-1354 (2008)
   PUBMED   18821565
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Calvari,V., Bertini,V., De Grandi,A., Peverali,G., Zuffardi,O.,
            Ferguson-Smith,M., Knudtzon,J., Camerino,G., Borsani,G. and
            Guioli,S.
  TITLE     A new submicroscopic deletion that refines the 9p region for sex
            reversal
  JOURNAL   Genomics 65 (3), 203-212 (2000)
   PUBMED   10857744
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Ottolenghi,C., Veitia,R., Barbieri,M., Fellous,M. and McElreavey,K.
  TITLE     The human doublesex-related gene, DMRT2, is homologous to a gene
            involved in somitogenesis and encodes a potential bicistronic
            transcript
  JOURNAL   Genomics 64 (2), 179-186 (2000)
   PUBMED   10729224
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Raymond,C.S., Parker,E.D., Kettlewell,J.R., Brown,L.G., Page,D.C.,
            Kusz,K., Jaruzelska,J., Reinberg,Y., Flejter,W.L., Bardwell,V.J.,
            Hirsch,B. and Zarkower,D.
  TITLE     A region of human chromosome 9p required for testis development
            contains two genes related to known sexual regulators
  JOURNAL   Hum Mol Genet 8 (6), 989-996 (1999)
   PUBMED   10332030
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL358976.11.
            
            Summary: The protein encoded by this gene belongs to the DMRT gene
            family, sharing a DM DNA-binding domain with Drosophila 'doublesex'
            (dsx) and C. elegans mab3, genes involved in sex determination in
            these organisms. Also, this gene is located in a region of the
            human genome (chromosome 9p24.3) associated with gonadal dysgenesis
            and XY sex reversal. Hence this gene is one of the candidates for
            sex-determining gene(s) on chr 9. [provided by RefSeq, Apr 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138525.551434.1,
                                           DRR138524.174359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.3"
     Protein         1..226
                     /product="doublesex- and mab-3-related transcription
                     factor 2 isoform 1"
                     /note="terra-like protein; doublesex-like 2 protein"
                     /calculated_mol_wt=24338
     Region          1..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5R5.2)"
     Region          119..165
                     /region_name="DM"
                     /note="DM DNA binding domain; pfam00751"
                     /db_xref="CDD:459924"
     CDS             1..226
                     /gene="DMRT2"
                     /gene_synonym="DSXL-2"
                     /coded_by="NM_001370531.1:171..851"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS6445.1"
                     /db_xref="GeneID:10655"
                     /db_xref="HGNC:HGNC:2935"
                     /db_xref="MIM:604935"
ORIGIN      
        1 madpqagsaa gdweidvesl eleedvcgap rstppgpspp padgdcedde dddgvdedae
       61 eegdgeeaga spgmpgqpeq rggpqprppl apqaspagtg prerctpagg gaeprklsrt
      121 pkcarcrnhg vvsclkghkr fcrwrdcqca ncllvverqr vmaaqvalrr qqatedkkgl
      181 sgkqnnferk avyqrqvrap sllaksilev llglfysyyv yimnhl
//
LOCUS       NP_919225                353 aa            linear   PRI 27-APR-2025
DEFINITION  dead end protein homolog 1 [Homo sapiens].
ACCESSION   NP_919225
VERSION     NP_919225.1
DBSOURCE    REFSEQ: accession NM_194249.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Zhang,W., Xu,Q., Shi,C., Chen,X., Shen,C., Zhang,Y., Zheng,B. and
            Zhu,H.
  TITLE     RNA-binding protein DND1 participates in migration, invasion, and
            EMT of prostate cancer cells by degrading CLIC4
  JOURNAL   Histol Histopathol 39 (10), 1343-1358 (2024)
   PUBMED   38390782
  REMARK    GeneRIF: RNA-binding protein DND1 participates in migration,
            invasion, and EMT of prostate cancer cells by degrading CLIC4.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Yang,Y., Li,J., Wei,C., Wang,L., Gao,Z., Shen,K., Li,Y., Ren,M.,
            Zhu,Y., Ding,Y., Wei,C., Zhang,T., Zheng,S., Lu,N. and Gu,J.
  TITLE     Circular RNA circFCHO2(hsa_circ_0002490) promotes the proliferation
            of melanoma by directly binding to DND1
  JOURNAL   Cell Biol Toxicol 40 (1), 9 (2024)
   PUBMED   38311675
  REMARK    GeneRIF: Circular RNA circFCHO2(hsa_circ_0002490) promotes the
            proliferation of melanoma by directly binding to DND1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Hirano,T., Wright,D., Suzuki,A. and Saga,Y.
  TITLE     A cooperative mechanism of target RNA selection via
            germ-cell-specific RNA-binding proteins NANOS2 and DND1
  JOURNAL   Cell Rep 39 (11), 110894 (2022)
   PUBMED   35705038
  REMARK    GeneRIF: A cooperative mechanism of target RNA selection via
            germ-cell-specific RNA-binding proteins NANOS2 and DND1.
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Xu,G., Yang,X., Li,C., Wang,F., Cui,J., Li,B., Xiao,H., Tang,K. and
            Cui,Z.
  TITLE     High DND1 Level Indicates a Poor Prognostic Factor in Prostate
            Cancer
  JOURNAL   Dis Markers 2021, 9948241 (2021)
   PUBMED   34721738
  REMARK    GeneRIF: High DND1 Level Indicates a Poor Prognostic Factor in
            Prostate Cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Kumari,P. and Bhavesh,N.S.
  TITLE     Human DND1-RRM2 forms a non-canonical domain swapped dimer
  JOURNAL   Protein Sci 30 (6), 1184-1195 (2021)
   PUBMED   33860980
  REMARK    GeneRIF: Human DND1-RRM2 forms a non-canonical domain swapped
            dimer.
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Linger,R., Dudakia,D., Huddart,R., Tucker,K., Friedlander,M.,
            Phillips,K.A., Hogg,D., Jewett,M.A., Lohynska,R., Daugaard,G.,
            Richard,S., Chompret,A., Stoppa-Lyonnet,D., Bonaiti-Pellie,C.,
            Heidenreich,A., Albers,P., Olah,E., Geczi,L., Bodrogi,I.,
            Daly,P.A., Guilford,P., Fossa,S.D., Heimdal,K., Tjulandin,S.A.,
            Liubchenko,L., Stoll,H., Weber,W., Einhorn,L., McMaster,M.,
            Korde,L., Greene,M.H., Nathanson,K.L., Cortessis,V., Easton,D.F.,
            Bishop,D.T., Stratton,M.R. and Rapley,E.A.
  TITLE     Analysis of the DND1 gene in men with sporadic and familial
            testicular germ cell tumors
  JOURNAL   Genes Chromosomes Cancer 47 (3), 247-252 (2008)
   PUBMED   18069663
  REMARK    GeneRIF: The variant, p. Glu86Ala, found in only one case of
            testiciular germ cell tumor, is within a known functional domain of
            DND1 and is highly conserved through evolution; mutations in DND1
            make, at most, a very small contribution to TGCT susceptibility
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Kedde,M., Strasser,M.J., Boldajipour,B., Oude Vrielink,J.A.,
            Slanchev,K., le Sage,C., Nagel,R., Voorhoeve,P.M., van Duijse,J.,
            Orom,U.A., Lund,A.H., Perrakis,A., Raz,E. and Agami,R.
  TITLE     RNA-binding protein Dnd1 inhibits microRNA access to target mRNA
  JOURNAL   Cell 131 (7), 1273-1286 (2007)
   PUBMED   18155131
  REMARK    GeneRIF: Unravels a novel role of Dnd1 in protecting certain mRNAs
            from miRNA-mediated repression.
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Matin,A.
  TITLE     What leads from dead-end?
  JOURNAL   Cell Mol Life Sci 64 (11), 1317-1322 (2007)
   PUBMED   17464447
  REMARK    Review article
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Youngren,K.K., Coveney,D., Peng,X., Bhattacharya,C., Schmidt,L.S.,
            Nickerson,M.L., Lamb,B.T., Deng,J.M., Behringer,R.R., Capel,B.,
            Rubin,E.M., Nadeau,J.H. and Matin,A.
  TITLE     The Ter mutation in the dead end gene causes germ cell loss and
            testicular germ cell tumours
  JOURNAL   Nature 435 (7040), 360-364 (2005)
   PUBMED   15902260
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Weidinger,G., Stebler,J., Slanchev,K., Dumstrei,K., Wise,C.,
            Lovell-Badge,R., Thisse,C., Thisse,B. and Raz,E.
  TITLE     dead end, a novel vertebrate germ plasm component, is required for
            zebrafish primordial germ cell migration and survival
  JOURNAL   Curr Biol 13 (16), 1429-1434 (2003)
   PUBMED   12932328
  REMARK    GeneRIF: Cloning of zebrafish dnd1 and identification of human DND1
            by database analysis.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC033496.1 and AC116353.2.
            
            Summary: This gene encodes a protein that binds to
            microRNA-targeting sequences of mRNAs, inhibiting microRNA-mediated
            repression. Reduced expression of this gene has been implicated in
            tongue squamous cell carcinoma. Two pseudogenes of this gene are
            located on the long arm of chromosome 17. [provided by RefSeq, Dec
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033496.1, AY321065.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000542735.2/ ENSP00000445366.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..353
                     /product="dead end protein homolog 1"
                     /note="dead end homolog 1; RNA-binding motif,
                     single-stranded-interacting protein 4"
                     /calculated_mol_wt=38556
     Region          18..>219
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Region          254..333
                     /region_name="DSRM_DND1"
                     /note="double-stranded RNA binding motif of dead end
                     protein homolog 1 (DND1) and similar proteins; cd20313"
                     /db_xref="CDD:380745"
     Site            order(254,256..257,260..261,264..265,270..271,286,288,
                     316..318,321..322)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380745"
     CDS             1..353
                     /gene="DND1"
                     /gene_synonym="RBMS4"
                     /coded_by="NM_194249.3:35..1096"
                     /db_xref="CCDS:CCDS4236.1"
                     /db_xref="GeneID:373863"
                     /db_xref="HGNC:HGNC:23799"
                     /db_xref="MIM:609385"
ORIGIN      
        1 mqskrdcelw cervnpenka aleawvretg irlvqvngqr kyggpppgwv gspppagsev
       61 figrlpqdvy ehqliplfqr vgrlyefrlm mtfsglnrgf ayaryssrrg aqaaiatlhn
      121 hplrpscpll vcrstekcel svdglppnlt rsalllalqp lgpglqearl lpspgpapgq
      181 iallkfsshr aaamakkalv egqshlcgeq vavewlkpdl kqrlrqqlvg pflrspqpeg
      241 sqlalardkl gfqgaratlq llcqrmklgs pvfltkclgi gpagwhrfwy qvvipghpvp
      301 fsgliwvvlt ldgrdgheva kdavsvrllq alsesganll wsagaeagtm vkq
//
LOCUS       NP_001073977             607 aa            linear   PRI 27-APR-2025
DEFINITION  T-box transcription factor TBX18 [Homo sapiens].
ACCESSION   NP_001073977 XP_496819
VERSION     NP_001073977.1
DBSOURCE    REFSEQ: accession NM_001080508.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Zhou,J., Wu,J., Wu,G., Huang,J., Zhang,Y., Che,J., Zhu,K., Geng,J.
            and Fan,Q.
  TITLE     TBX18 knockdown sensitizes esophageal squamous cell carcinoma to
            radiotherapy by blocking the CHN1/RhoA axis
  JOURNAL   Radiother Oncol 186, 109788 (2023)
   PUBMED   37399907
  REMARK    GeneRIF: TBX18 knockdown sensitizes esophageal squamous cell
            carcinoma to radiotherapy by blocking the CHN1/RhoA axis.
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Engwerda,A., Abbott,K.M., Hitzert,M.M., van Ravenswaaij-Arts,C.M.A.
            and Kerstjens-Frederikse,W.S.
  TITLE     The role of TBX18 in congenital heart defects in humans not
            confirmed
  JOURNAL   Eur J Hum Genet 31 (2), 138-141 (2023)
   PUBMED   36418409
  REMARK    GeneRIF: The role of TBX18 in congenital heart defects in humans
            not confirmed.
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Sanchez,L., Mesquita,T., Zhang,R., Liao,K., Rogers,R., Lin,Y.N.,
            Miguel-Dos-Santos,R., Akhmerov,A., Li,L., Nawaz,A., Holm,K.,
            Marban,E. and Cingolani,E.
  TITLE     MicroRNA-dependent suppression of biological pacemaker activity
            induced by TBX18
  JOURNAL   Cell Rep Med 3 (12), 100871 (2022)
   PUBMED   36543116
  REMARK    GeneRIF: MicroRNA-dependent suppression of biological pacemaker
            activity induced by TBX18.
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Zhang,W., Zhao,H., Quan,D., Tang,Y., Wang,X. and Huang,C.
  TITLE     Tbx18 promoted the conversion of human-induced pluripotent stem
            cell-derived cardiomyocytes into sinoatrial node-like pacemaker
            cells
  JOURNAL   Cell Biol Int 46 (3), 403-414 (2022)
   PUBMED   34882885
  REMARK    GeneRIF: Tbx18 promoted the conversion of human-induced pluripotent
            stem cell-derived cardiomyocytes into sinoatrial node-like
            pacemaker cells.
REFERENCE   5  (residues 1 to 607)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 607)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 607)
  AUTHORS   McNally,E.M. and Svensson,E.C.
  TITLE     Setting the pace: Tbx3 and Tbx18 in cardiac conduction system
            development
  JOURNAL   Circ Res 104 (3), 285-287 (2009)
   PUBMED   19213963
REFERENCE   8  (residues 1 to 607)
  AUTHORS   Farin,H.F., Bussen,M., Schmidt,M.K., Singh,M.K.,
            Schuster-Gossler,K. and Kispert,A.
  TITLE     Transcriptional repression by the T-box proteins Tbx18 and Tbx15
            depends on Groucho corepressors
  JOURNAL   J Biol Chem 282 (35), 25748-25759 (2007)
   PUBMED   17584735
  REMARK    GeneRIF: Tbx18 interacts with Gata4 and Nkx2-5 and competes
            Tbx5-mediated activation of the cardiac Natriuretic peptide
            precursor type a-promoter. Tbx18 down-regulates Tbx6-activated
            Delta-like 1 expression in the somitic mesoderm in vivo
REFERENCE   9  (residues 1 to 607)
  AUTHORS   King,M., Arnold,J.S., Shanske,A. and Morrow,B.E.
  TITLE     T-genes and limb bud development
  JOURNAL   Am J Med Genet A 140 (13), 1407-1413 (2006)
   PUBMED   16688725
  REMARK    Review article
REFERENCE   10 (residues 1 to 607)
  AUTHORS   Yi,C.H., Terrett,J.A., Li,Q.Y., Ellington,K., Packham,E.A.,
            Armstrong-Buisseret,L., McClure,P., Slingsby,T. and Brook,J.D.
  TITLE     Identification, mapping, and phylogenomic analysis of four new
            human members of the T-box gene family: EOMES, TBX6, TBX18, and
            TBX19
  JOURNAL   Genomics 55 (1), 10-20 (1999)
   PUBMED   9888994
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL035694.8, BC132715.1 and
            BC157841.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 18, 2007 this sequence version replaced XP_496819.2.
            
            Summary: This genes codes for a member of an evolutionarily
            conserved family of transcription factors that plays a crucial role
            in embryonic development. The family is characterized by the
            presence of the DNA-binding T-box domain and is divided into five
            sub-families based on sequence conservation in this domain. The
            encoded protein belongs to the vertebrate specific Tbx1 sub-family.
            The protein acts as a transcriptional repressor by antagonizing
            transcriptional activators in the T-box family. The protein forms
            homo- or heterodimers with other transcription factors of the T-box
            family or other transcription factors. [provided by RefSeq, Nov
            2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC157841.1, SRR7346977.2169646.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369663.10/ ENSP00000358677.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..607
                     /product="T-box transcription factor TBX18"
                     /note="T-box protein 18; T-box 18"
                     /calculated_mol_wt=64622
     Region          18..28
                     /region_name="Engrailed homology 1 repressor.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O95935.3)"
     Region          30..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95935.3)"
     Region          <32..>139
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          36..40
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O95935.3)"
     Region          137..330
                     /region_name="T-box_TBX15_18_22-like"
                     /note="DNA-binding domain of T-box transcription factor
                     15, 18 and 22, and related T-box proteins; cd20191"
                     /db_xref="CDD:410317"
     Site            order(166..167,200,246,249,262..263,307..310,315,318..319,
                     322..328)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410317"
     CDS             1..607
                     /gene="TBX18"
                     /gene_synonym="CAKUT2; PUJO"
                     /coded_by="NM_001080508.3:418..2241"
                     /db_xref="CCDS:CCDS34495.1"
                     /db_xref="GeneID:9096"
                     /db_xref="HGNC:HGNC:11595"
                     /db_xref="MIM:604613"
ORIGIN      
        1 maekrrgspc smlslkahaf svealigaek qqqlqkkrrk lgaeeaagav ddggcsrggg
       61 agekgssegd egaalpppag atsgparsga dlergaaggc edgfqqgasp laspggspkg
      121 sparslarpg tplpspqapr vdlqgaelwk rfheigtemi itkagrrmfp amrvkisgld
      181 phqqyyiamd ivpvdnkryr yvyhsskwmv agnadspvpp rvyihpdspa sgetwmrqvi
      241 sfdklkltnn elddqghiil hsmhkyqprv hvirkdcgdd lspikpvpsg egvkafsfpe
      301 tvfttvtayq nqqitrlkid rnpfakgfrd sgrnrmglea lvesyafwrp slrtltfedi
      361 pgipkqgnas sstllqgtgn gvpathphll sgsscsspaf hlgpntsqlc slapadysac
      421 arsgltlnry stslaetynr ltnqagetfa pprtpsyvgv ssstsvnmsm ggtdgdtfsc
      481 pqtslsmqis gmspqlqyim pspssnafat nqthqgsynt frlhspcaly gynfstspkl
      541 aaspekivss qgsflgssps gtmtdrqmlp pvegvhllss ggqqsffdsr tlgsltlsss
      601 qvsahmv
//
LOCUS       NP_006504                514 aa            linear   PRI 27-APR-2025
DEFINITION  serine--tRNA ligase, cytoplasmic isoform a [Homo sapiens].
ACCESSION   NP_006504
VERSION     NP_006504.2
DBSOURCE    REFSEQ: accession NM_006513.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Liu,Z., Wang,J., Shi,Y., Yee,B.A., Terrey,M., Zhang,Q., Lee,J.C.,
            Lin,K.I., Wang,A.H., Ackerman,S.L., Yeo,G.W., Cui,H. and Yang,X.L.
  TITLE     Seryl-tRNA synthetase promotes translational readthrough by mRNA
            binding and involvement of the selenocysteine incorporation
            machinery
  JOURNAL   Nucleic Acids Res 51 (19), 10768-10781 (2023)
   PUBMED   37739431
  REMARK    GeneRIF: Seryl-tRNA synthetase promotes translational readthrough
            by mRNA binding and involvement of the selenocysteine incorporation
            machinery.
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Verdura,E., Senger,B., Raspall-Chaure,M., Schluter,A., Launay,N.,
            Ruiz,M., Casasnovas,C., Rodriguez-Palmero,A., Macaya,A.,
            Becker,H.D. and Pujol,A.
  TITLE     Loss of seryl-tRNA synthetase (SARS1) causes complex spastic
            paraplegia and cellular senescence
  JOURNAL   J Med Genet 59 (12), 1227-1233 (2022)
   PUBMED   36041817
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Bogershausen,N., Krawczyk,H.E., Jamra,R.A., Lin,S.J., Yigit,G.,
            Huning,I., Polo,A.M., Vona,B., Huang,K., Schmidt,J., Altmuller,J.,
            Luppe,J., Platzer,K., Dorgeloh,B.B., Busche,A., Biskup,S.,
            Mendes,M.I., Smith,D.E.C., Salomons,G.S., Zibat,A., Bultmann,E.,
            Nurnberg,P., Spielmann,M., Lemke,J.R., Li,Y., Zenker,M.,
            Varshney,G.K., Hillen,H.S., Kratz,C.P. and Wollnik,B.
  TITLE     WARS1 and SARS1: Two tRNA synthetases implicated in autosomal
            recessive microcephaly
  JOURNAL   Hum Mutat 43 (10), 1454-1471 (2022)
   PUBMED   35790048
  REMARK    GeneRIF: WARS1 and SARS1: Two tRNA synthetases implicated in
            autosomal recessive microcephaly.
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Ravel,J.M., Dreumont,N., Mosca,P., Smith,D.E.C., Mendes,M.I.,
            Wiedemann,A., Coelho,D., Schmitt,E., Riviere,J.B., Tran
            Mau-Them,F., Thevenon,J., Kuentz,P., Polivka,M., Fuchs,S.A.,
            Kok,G., Thauvin-Robinet,C., Gueant,J.L., Salomons,G.S., Faivre,L.
            and Feillet,F.
  TITLE     A bi-allelic loss-of-function SARS1 variant in children with
            neurodevelopmental delay, deafness, cardiomyopathy, and
            decompensation during fever
  JOURNAL   Hum Mutat 42 (12), 1576-1583 (2021)
   PUBMED   34570399
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Zhao,J., Bai,H., Li,X., Yan,J., Zou,G., Wang,L., Li,X., Liu,Z.,
            Xiang,R., Yang,X.L. and Shi,Y.
  TITLE     Glucose-sensitive acetylation of Seryl tRNA synthetase regulates
            lipid synthesis in breast cancer
  JOURNAL   Signal Transduct Target Ther 6 (1), 303 (2021)
   PUBMED   34400610
  REMARK    GeneRIF: Glucose-sensitive acetylation of Seryl tRNA synthetase
            regulates lipid synthesis in breast cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Shimada,N., Suzuki,T. and Watanabe,K.
  TITLE     Dual mode recognition of two isoacceptor tRNAs by mammalian
            mitochondrial seryl-tRNA synthetase
  JOURNAL   J Biol Chem 276 (50), 46770-46778 (2001)
   PUBMED   11577083
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Shah,Z.H., Toompuu,M., Hakkinen,T., Rovio,A.T., van Ravenswaay,C.,
            De Leenheer,E.M., Smith,R.J., Cremers,F.P., Cremers,C.W. and
            Jacobs,H.T.
  TITLE     Novel coding-region polymorphisms in mitochondrial seryl-tRNA
            synthetase (SARSM) and mitoribosomal protein S12 (RPMS12) genes in
            DFNA4 autosomal dominant deafness families
  JOURNAL   Hum Mutat 17 (5), 433-434 (2001)
   PUBMED   11317363
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Heckl,M., Busch,K. and Gross,H.J.
  TITLE     Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA
            synthetase: contribution of tRNA domains to serylation and tertiary
            structure
  JOURNAL   FEBS Lett 427 (3), 315-319 (1998)
   PUBMED   9637248
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Vincent,C., Tarbouriech,N. and Hartlein,M.
  TITLE     Genomic organization, cDNA sequence, bacterial expression, and
            purification of human seryl-tRNA synthase
  JOURNAL   Eur J Biochem 250 (1), 77-84 (1997)
   PUBMED   9431993
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Hartlein,M. and Cusack,S.
  TITLE     Structure, function and evolution of seryl-tRNA synthetases:
            implications for the evolution of aminoacyl-tRNA synthetases and
            the genetic code
  JOURNAL   J Mol Evol 40 (5), 519-530 (1995)
   PUBMED   7540217
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC111398.1, BC009390.2 and
            BM666450.1.
            
            On Oct 22, 2001 this sequence version replaced NP_006504.1.
            
            Summary: This gene belongs to the class II amino-acyl tRNA family.
            The encoded enzyme catalyzes the transfer of L-serine to tRNA (Ser)
            and is related to bacterial and yeast counterparts. Multiple
            alternatively spliced transcript variants have been described but
            the biological validity of all variants is unknown. [provided by
            RefSeq, Jul 2010].
            
            Transcript Variant: This variant (1) lacks an alternate in-frame
            exon compared to variant 3. The resulting isoform (a) has the same
            N- and C-termini but is shorter compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.274910.1,
                                           SRR5189658.83431.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000234677.7/ ENSP00000234677.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..514
                     /product="serine--tRNA ligase, cytoplasmic isoform a"
                     /EC_number="6.1.1.11"
                     /note="serine tRNA ligase 1, cytoplasmic; seryl-tRNA
                     synthetase, cytoplasmic; seryl-tRNA(Ser/Sec) synthetase;
                     serine--tRNA ligase, cytoplasmic"
                     /calculated_mol_wt=58646
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P49591.3)"
     Region          3..486
                     /region_name="PLN02678"
                     /note="seryl-tRNA synthetase"
                     /db_xref="CDD:215364"
     Region          9..61
                     /region_name="Interaction with tRNA.
                     /evidence=ECO:0000269|PubMed:26433229"
                     /note="propagated from UniProtKB/Swiss-Prot (P49591.3)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (P49591.3)"
     Site            323
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49591.3)"
     Site            429
                     /site_type="other"
                     /note="Important for serine binding.
                     /evidence=ECO:0000269|PubMed:28236339; propagated from
                     UniProtKB/Swiss-Prot (P49591.3)"
     Region          473..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49591.3)"
     Region          482..494
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:22353712"
                     /note="propagated from UniProtKB/Swiss-Prot (P49591.3)"
     CDS             1..514
                     /gene="SARS1"
                     /gene_synonym="NEDMAS; SARS; SERRS; SERS"
                     /coded_by="NM_006513.4:76..1620"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS795.1"
                     /db_xref="GeneID:6301"
                     /db_xref="HGNC:HGNC:10537"
                     /db_xref="MIM:607529"
ORIGIN      
        1 mvldldlfrv dkggdpalir etqekrfkdp glvdqlvkad sewrrcrfra dnlnklknlc
       61 sktigekmkk kepvgddesv penvlsfddl tadalanlkv sqikkvrlli deailkcdae
      121 rikleaerfe nlreignllh psvpisnded vdnkveriwg dctvrkkysh vdlvvmvdgf
      181 egekgavvag srgyflkgvl vfleqaliqy alrtlgsrgy ipiytpffmr kevmqevaql
      241 sqfdeelykv igkgseksdd nsydekylia tseqpiaalh rdewlrpedl pikyaglstc
      301 frqevgshgr dtrgifrvhq fekieqfvys sphdnkswem feemittaee fyqslgipyh
      361 ivnivsgsln haaskkldle awfpgsgafr elvscsnctd yqarrlriry gqtkkmmdkv
      421 efvhmlnatm cattrticai lenyqtekgi tvpeklkefm ppglqelipf vkpapieqep
      481 skkqkkqheg skkkaaardv tlenrlqnme vtda
//
LOCUS       NP_002940                198 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein bL12m [Homo sapiens].
ACCESSION   NP_002940
VERSION     NP_002940.2
DBSOURCE    REFSEQ: accession NM_002949.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Rai,A.K., Sanghvi,S., Muthukumaran,N.S., Chandrasekera,D.,
            Kadam,A., Kishore,J., Kyriazis,I.D., Tomar,D., Ponnalagu,D.,
            Shettigar,V., Khan,M., Singh,H., Goukassian,D., Katare,R. and
            Garikipati,V.N.S.
  TITLE     Role of mitochondrial ribosomal protein L7/L12 (MRPL12) in diabetic
            ischemic heart disease
  JOURNAL   Free Radic Biol Med 222, 531-538 (2024)
   PUBMED   38977138
  REMARK    GeneRIF: Role of mitochondrial ribosomal protein L7/L12 (MRPL12) in
            diabetic ischemic heart disease.
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Paluch,K.V., Platz,K.R., Rudisel,E.J., Erdmann,R.R., Laurin,T.R.
            and Dittenhafer-Reed,K.E.
  TITLE     The role of lysine acetylation in the function of mitochondrial
            ribosomal protein L12
  JOURNAL   Proteins 92 (5), 583-592 (2024)
   PUBMED   38146092
  REMARK    GeneRIF: The role of lysine acetylation in the function of
            mitochondrial ribosomal protein L12.
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Sun,Y., Liu,Y., Wang,P., Chang,L. and Huang,J.
  TITLE     The m6A Reader YTHDC2 Suppresses Lung Adenocarcinoma Tumorigenesis
            by Destabilizing MRPL12
  JOURNAL   Mol Biotechnol 66 (5), 1051-1061 (2024)
   PUBMED   38129673
  REMARK    GeneRIF: The m6A Reader YTHDC2 Suppresses Lung Adenocarcinoma
            Tumorigenesis by Destabilizing MRPL12.
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Ji,X., Yang,Z., Li,C., Zhu,S., Zhang,Y., Xue,F., Sun,S., Fu,T.,
            Ding,C., Liu,Y. and Wan,Q.
  TITLE     Mitochondrial ribosomal protein L12 potentiates hepatocellular
            carcinoma by regulating mitochondrial biogenesis and metabolic
            reprogramming
  JOURNAL   Metabolism 152, 155761 (2024)
   PUBMED   38104924
  REMARK    GeneRIF: Mitochondrial ribosomal protein L12 potentiates
            hepatocellular carcinoma by regulating mitochondrial biogenesis and
            metabolic reprogramming.
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Ji,X., Yang,X., Gu,X., Chu,L., Sun,S., Sun,J., Song,P., Mu,Q.,
            Wang,Y., Sun,X., Su,D., Su,T., Hou,S., Lu,Y., Ma,C., Liu,M.,
            Zhang,T., Zhang,W., Liu,Y. and Wan,Q.
  TITLE     CUL3 induces mitochondrial dysfunction via MRPL12 ubiquitination in
            renal tubular epithelial cells
  JOURNAL   FEBS J 290 (22), 5340-5352 (2023)
   PUBMED   37526061
  REMARK    GeneRIF: CUL3 induces mitochondrial dysfunction via MRPL12
            ubiquitination in renal tubular epithelial cells.
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Koc,E.C., Burkhart,W., Blackburn,K., Moyer,M.B., Schlatzer,D.M.,
            Moseley,A. and Spremulli,L.L.
  TITLE     The large subunit of the mammalian mitochondrial ribosome. Analysis
            of the complement of ribosomal proteins present
  JOURNAL   J Biol Chem 276 (47), 43958-43969 (2001)
   PUBMED   11551941
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Graack,H.R., Bryant,M.L. and O'Brien,T.W.
  TITLE     Identification of mammalian mitochondrial ribosomal proteins (MRPs)
            by N-terminal sequencing of purified bovine MRPs and comparison to
            data bank sequences: the large subribosomal particle
  JOURNAL   Biochemistry 38 (50), 16569-16577 (1999)
   PUBMED   10600119
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Marty,L., Taviaux,S. and Fort,P.
  TITLE     Expression and human chromosomal localization to 17q25 of the
            growth-regulated gene encoding the mitochondrial ribosomal protein
            MRPL12
  JOURNAL   Genomics 41 (3), 453-457 (1997)
   PUBMED   9169145
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Marty,L. and Fort,P.
  TITLE     A delayed-early response nuclear gene encoding MRPL12, the
            mitochondrial homologue to the bacterial translational regulator
            L7/L12 protein
  JOURNAL   J Biol Chem 271 (19), 11468-11476 (1996)
   PUBMED   8626705
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139530.3, DA648796.1,
            BC002344.2 and AF105278.1.
            
            On Dec 31, 2002 this sequence version replaced NP_002940.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein which forms
            homodimers. In prokaryotic ribosomes, two L7/L12 dimers and one L10
            protein form the L8 protein complex. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.348680.1,
                                           SRR1803613.225094.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000333676.8/
                                                  ENSP00000333837.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..198
                     /product="large ribosomal subunit protein bL12m"
                     /note="39S ribosomal protein L12, mitochondrial; MRP-L12;
                     mitochondrial large ribosomal subunit protein bL12m"
                     /calculated_mol_wt=21217
     Region          63..198
                     /region_name="RplL"
                     /note="Ribosomal protein L7/L12 [Translation, ribosomal
                     structure and biogenesis]; COG0222"
                     /db_xref="CDD:439992"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            138
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DB15; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            142
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            150
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            163
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            178
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            185
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     CDS             1..198
                     /gene="MRPL12"
                     /gene_synonym="5c5-2; bL12m; L12mt; MRP-L31/34; MRPL7;
                     MRPL7/L12; RPML12"
                     /coded_by="NM_002949.4:136..732"
                     /db_xref="CCDS:CCDS11785.1"
                     /db_xref="GeneID:6182"
                     /db_xref="HGNC:HGNC:10378"
                     /db_xref="MIM:602375"
ORIGIN      
        1 mlpaaarplw gpclglraaa frlarrqvpc vcavrhmrss ghqrcealag apldnapkey
       61 ppkiqqlvqd iasltlleis dlnellkktl kiqdvglvpm ggvmsgavpa aaaqeaveed
      121 ipiakerthf tvrlteakpv dkvklikeik nyiqginlvq akklveslpq eikanvakae
      181 aekikaalea vggtvvle
//
LOCUS       NP_001007468            1242 aa            linear   PRI 27-APR-2025
DEFINITION  protein SFI1 homolog isoform a [Homo sapiens].
ACCESSION   NP_001007468
VERSION     NP_001007468.1
DBSOURCE    REFSEQ: accession NM_001007467.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1242)
  AUTHORS   Arslanhan,M.D., Cengiz-Emek,S., Odabasi,E., Steib,E., Hamel,V.,
            Guichard,P. and Firat-Karalar,E.N.
  TITLE     CCDC15 localizes to the centriole inner scaffold and controls
            centriole length and integrity
  JOURNAL   J Cell Biol 222 (12) (2023)
   PUBMED   37934472
REFERENCE   2  (residues 1 to 1242)
  AUTHORS   Laporte,M.H., Bouhlel,I.B., Bertiaux,E., Morrison,C.G., Giroud,A.,
            Borgers,S., Azimzadeh,J., Bornens,M., Guichard,P., Paoletti,A. and
            Hamel,V.
  TITLE     Human SFI1 and Centrin form a complex critical for centriole
            architecture and ciliogenesis
  JOURNAL   EMBO J 41 (21), e112107 (2022)
   PUBMED   36125182
  REMARK    GeneRIF: Human SFI1 and Centrin form a complex critical for
            centriole architecture and ciliogenesis.
REFERENCE   3  (residues 1 to 1242)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1242)
  AUTHORS   Karlsson,L., Barbaro,M., Ewing,E., Gomez-Cabrero,D. and Lajic,S.
  TITLE     Genome-wide investigation of DNA methylation in congenital adrenal
            hyperplasia
  JOURNAL   J Steroid Biochem Mol Biol 201, 105699 (2020)
   PUBMED   32428554
  REMARK    GeneRIF: Genome-wide investigation of DNA methylation in congenital
            adrenal hyperplasia.
REFERENCE   5  (residues 1 to 1242)
  AUTHORS   Kodani,A., Moyer,T., Chen,A., Holland,A., Walsh,C.A. and
            Reiter,J.F.
  TITLE     SFI1 promotes centriole duplication by recruiting USP9X to
            stabilize the microcephaly protein STIL
  JOURNAL   J Cell Biol 218 (7), 2185-2197 (2019)
   PUBMED   31197030
  REMARK    GeneRIF: these results demonstrate that SFI1 is a centrosomal
            protein that localizes USP9X to the centrosome to stabilize STIL
            and promote centriole duplication. We propose that the USP9X
            protection of STIL to facilitate centriole duplication underlies
            roles of both proteins in human neurodevelopment.
REFERENCE   6  (residues 1 to 1242)
  AUTHORS   Kilmartin,J.V.
  TITLE     Sfi1p has conserved centrin-binding sites and an essential function
            in budding yeast spindle pole body duplication
  JOURNAL   J Cell Biol 162 (7), 1211-1221 (2003)
   PUBMED   14504268
REFERENCE   7  (residues 1 to 1242)
  AUTHORS   Casenghi,M., Meraldi,P., Weinhart,U., Duncan,P.I., Korner,R. and
            Nigg,E.A.
  TITLE     Polo-like kinase 1 regulates Nlp, a centrosome protein involved in
            microtubule nucleation
  JOURNAL   Dev Cell 5 (1), 113-125 (2003)
   PUBMED   12852856
REFERENCE   8  (residues 1 to 1242)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   9  (residues 1 to 1242)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   10 (residues 1 to 1242)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC369842.1, AK292408.1, AL708501.1, BC021576.1, AI141022.1 and
            AL096768.7.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292408.1, SRR7346977.1509962.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000400288.7/ ENSP00000383145.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..1242
                     /product="protein SFI1 homolog isoform a"
                     /note="homolog of yeast Sfi1; protein SFI1 homolog;
                     protein phosphatase 1, regulatory subunit 139; Sfi1
                     homolog, spindle assembly associated"
                     /calculated_mol_wt=147533
     Region          111..130
                     /region_name="Interaction with CETN2.
                     /evidence=ECO:0000269|PubMed:16956364"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          138..170
                     /region_name="HAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          172..201
                     /region_name="HAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          270..302
                     /region_name="HAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          334..368
                     /region_name="HAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          399..431
                     /region_name="HAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          417..841
                     /region_name="Sfi1"
                     /note="Sfi1 spindle body protein; pfam08457"
                     /db_xref="CDD:430007"
     Region          475..494
                     /region_name="Interaction with CETN2.
                     /evidence=ECO:0000269|PubMed:16956364"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          641..660
                     /region_name="Interaction with CETN2.
                     /evidence=ECO:0000269|PubMed:16956364"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          <936..1129
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1017..1038
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          1053..1081
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          1101..1122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     Region          1148..1180
                     /region_name="HAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (A8K8P3.2)"
     CDS             1..1242
                     /gene="SFI1"
                     /gene_synonym="hSfi1p; PISD; PPP1R139"
                     /coded_by="NM_001007467.3:133..3861"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43004.1"
                     /db_xref="GeneID:9814"
                     /db_xref="HGNC:HGNC:29064"
                     /db_xref="MIM:612765"
ORIGIN      
        1 mknlltekci sshnfhqkvi kqrmekkvds ryfkdgavkk pysaktlsnk kssasfgirr
       61 elpstshlvq yrgthtctrq grlrelrirc varkflylwi rmtfgrvfps karfyyeqrl
      121 lrkvfeewke ewwvfqhewk lcvradchyr yylynlmfqt wktyvrqqqe mrnkyiraev
      181 hdakqkmrqa wkswliyvvv rrtklqmqtt alefrqriil rvwwstwrqr lgqvrvsral
      241 hasalkhral slqvqawsqw reqllyvqke kqkvvsavkh hqhwqkrrfl kawleylqvr
      301 rvkrqqnema erfhhvtvlq iyfcdwqqaw erreslyahh aqveklarkm alrrafthwk
      361 hymllcaeea aqfemaeehh rhsqlyfcfr alkdnvthah lqqirrnlah qqhgvtllhr
      421 fwnlwrsqie qkkerellpl lhaawdhyri allckcielw lqytqkrryk qllqaradgh
      481 fqqralpaaf htwnrlwrwr hqenvlsara trfhretlek qvfslwrqkm fqhrenrlae
      541 rmailhaerq llyrswfmwh qqaaarhqeq ewqtvacahh rhgrlkkafc lwresaqglr
      601 tertgrvraa efhmaqllrw awsqwrecla lrgaerqklm radlhhqhsv lhralqawvt
      661 yqgrvrsilr evaaresqhn rqllrgalrr wkentmarvd eakktfqast hyrrticskv
      721 lvqwreavsv qmyyrqqedc aiweaqkvld rgclrtwfqr wwdcsrrsaq qrlqleravq
      781 hhhrqllleg larwkthhlq cvrkrllhrq stqllaqrls rtcfrqwrqq laarrqeqra
      841 tvralwfwaf slqakvwatw lafvlerrrk karlqwalqa yqgqllqega trllrfaasm
      901 kasrqqlqaq qqvqaahslh ravrrcatlw kqkvlgrggk pqplaaiaps rkvtfegpll
      961 nriaagagdg tletkrpqas rplgalgrla aeephaleln tahsarkqpr rphfllepaq
     1021 sqrpqkpqeh glgmaqpaap sltrpflaea ptalvphspl pgalssapgp kqpptastgp
     1081 ellllplssf mpcgaaapar vsaqratprd kppvpsslas vpdphlllpg dfsatragpg
     1141 lstagsldle aeleeiqqql lhyqttkqnl wscrrqassl rrwlelnree pgpedqeveq
     1201 qvqkeleqve mqiqllaeel qaqrqpigac variqalrqa lc
//
LOCUS       NP_004076                 97 aa            linear   PRI 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim8 A
            isoform 1 [Homo sapiens].
ACCESSION   NP_004076
VERSION     NP_004076.1
DBSOURCE    REFSEQ: accession NM_004085.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Chi,Y., Hirachan,S., Zhou,Y. and Bhandari,A.
  TITLE     Exploring the Oncogenic Potential of TIMM8A: A Crucial Factor in
            Breast Cancer Tumorigenesis
  JOURNAL   Clin Breast Cancer 24 (5), e333-e349.e1 (2024)
   PUBMED   38548519
  REMARK    GeneRIF: Exploring the Oncogenic Potential of TIMM8A: A Crucial
            Factor in Breast Cancer Tumorigenesis.
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Song,P., Guan,Y., Chen,X., Wu,C., Qiao,A., Jiang,H., Li,Q.,
            Huang,Y., Huang,W., Xu,M., Niemtiah,O., Yuan,C., Li,W., Zhou,L.,
            Xiao,Z., Pan,S. and Hu,Y.
  TITLE     Frameshift mutation of Timm8a1 gene in mouse leads to an abnormal
            mitochondrial structure in the brain, correlating with hearing and
            memory impairment
  JOURNAL   J Med Genet 58 (9), 619-627 (2021)
   PUBMED   32820032
  REMARK    GeneRIF: Frameshift mutation of Timm8a1 gene in mouse leads to an
            abnormal mitochondrial structure in the brain, correlating with
            hearing and memory impairment.
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Wallace,D.C. and Murdock,D.G.
  TITLE     Mitochondria and dystonia: the movement disorder connection?
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 1817-1819 (1999)
   PUBMED   10051550
REFERENCE   6  (residues 1 to 97)
  AUTHORS   Jin,H., May,M., Tranebjaerg,L., Kendall,E., Fontan,G., Jackson,J.,
            Subramony,S.H., Arena,F., Lubs,H., Smith,S., Stevenson,R.,
            Schwartz,C. and Vetrie,D.
  TITLE     A novel X-linked gene, DDP, shows mutations in families with
            deafness (DFN-1), dystonia, mental deficiency and blindness
  JOURNAL   Nat Genet 14 (2), 177-180 (1996)
   PUBMED   8841189
REFERENCE   7  (residues 1 to 97)
  AUTHORS   Tranebjaerg,L., Schwartz,C., Eriksen,H., Andreasson,S.,
            Ponjavic,V., Dahl,A., Stevenson,R.E., May,M., Arena,F., Barker,D.
            et al.
  TITLE     A new X linked recessive deafness syndrome with blindness,
            dystonia, fractures, and mental deficiency is linked to Xq22
  JOURNAL   J Med Genet 32 (4), 257-263 (1995)
   PUBMED   7643352
REFERENCE   8  (residues 1 to 97)
  AUTHORS   Vorechovsky,I., Vetrie,D., Holland,J., Bentley,D.R., Thomas,K.,
            Zhou,J.N., Notarangelo,L.D., Plebani,A., Fontan,G., Ochs,H.D. et
            al.
  TITLE     Isolation of cosmid and cDNA clones in the region surrounding the
            BTK gene at Xq21.3-q22
  JOURNAL   Genomics 21 (3), 517-524 (1994)
   PUBMED   7959728
REFERENCE   9  (residues 1 to 97)
  AUTHORS   Tranebjaerg,L.
  TITLE     Deafness-Dystonia-Optic Neuronopathy Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301395
REFERENCE   10 (residues 1 to 97)
  AUTHORS   Klein,C., Lohmann,K., Marras,C. and Munchau,A.
  TITLE     Hereditary Dystonia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN410182.1, BC006994.1 and
            AW204693.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This translocase is involved in the import and insertion
            of hydrophobic membrane proteins from the cytoplasm into the
            mitochondrial inner membrane. The gene is mutated in
            Mohr-Tranebjaerg syndrome/Deafness Dystonia Syndrome (MTS/DDS) and
            it is postulated that MTS/DDS is a mitochondrial disease caused by
            a defective mitochondrial protein import system. Defects in this
            gene also cause Jensen syndrome; an X-linked disease with
            opticoacoustic nerve atrophy and muscle weakness. This protein,
            along with TIMM13, forms a 70 kDa heterohexamer. Alternative
            splicing results in multiple transcript variants encoding distinct
            isoforms.[provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.114906.1,
                                           SRR1803613.248108.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000372902.4/
                                                  ENSP00000361993.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..97
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim8 A isoform 1"
                     /note="deafness/dystonia peptide; mitochondrial import
                     inner membrane translocase subunit Tim8 A; deafness
                     dystonia protein 1; translocase of inner mitochondrial
                     membrane 8 homolog A; X-linked deafness dystonia protein"
                     /calculated_mol_wt=10867
     Region          21..83
                     /region_name="zf-Tim10_DDP"
                     /note="Tim10/DDP family zinc finger; pfam02953"
                     /db_xref="CDD:460764"
     Region          43..66
                     /region_name="Twin CX3C motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O60220.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVA2; propagated from
                     UniProtKB/Swiss-Prot (O60220.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVA2; propagated from
                     UniProtKB/Swiss-Prot (O60220.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O60220.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60220.1)"
     CDS             1..97
                     /gene="TIMM8A"
                     /gene_synonym="DDP; DDP1; DFN1; MTS; TIM8"
                     /coded_by="NM_004085.4:79..372"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14481.1"
                     /db_xref="GeneID:1678"
                     /db_xref="HGNC:HGNC:11817"
                     /db_xref="MIM:300356"
ORIGIN      
        1 mdssssssaa glgavdpqlq hfievetqkq rfqqlvhqmt elcwekcmdk pgpkldsrae
       61 acfvncverf idtsqfilnr leqtqkskpv fseslsd
//
LOCUS       NP_001350312             413 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 821 isoform a [Mus musculus].
ACCESSION   NP_001350312 XP_011246835
VERSION     NP_001350312.1
DBSOURCE    REFSEQ: accession NM_001363383.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Sharov,A.A., Piao,Y., Matoba,R., Dudekula,D.B., Qian,Y.,
            VanBuren,V., Falco,G., Martin,P.R., Stagg,C.A., Bassey,U.C.,
            Wang,Y., Carter,M.G., Hamatani,T., Aiba,K., Akutsu,H., Sharova,L.,
            Tanaka,T.S., Kimber,W.L., Yoshikawa,T., Jaradat,S.A., Pantano,S.,
            Nagaraja,R., Boheler,K.R., Taub,D., Hodes,R.J., Longo,D.L.,
            Schlessinger,D., Keller,J., Klotz,E., Kelsoe,G., Umezawa,A.,
            Vescovi,A.L., Rossant,J., Kunath,T., Hogan,B.L., Curci,A.,
            D'Urso,M., Kelso,J., Hide,W. and Ko,M.S.
  TITLE     Transcriptome analysis of mouse stem cells and early embryos
  JOURNAL   PLoS Biol 1 (3), E74 (2003)
   PUBMED   14691545
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132138.2.
            
            On May 17, 2018 this sequence version replaced XP_011246835.1.
            
            Transcript Variant: This variant (8), as well as variants 1, 2, 5,
            6, and 7, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.4189443.1,
                                           SRR7652917.1081949.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 57.21 cM"
     Protein         1..413
                     /product="zinc finger protein 821 isoform a"
                     /calculated_mol_wt=46697
     Region          26..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PD05.2)"
     Region          121..141
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(126,128,130,132..133,136..137,140,158,160,164..165,
                     168..169,172,186,188,190,192..193)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          151..173
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          153..173
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <261..>335
                     /region_name="COG2433"
                     /note="Possible nuclease of RNase H fold, RuvC/YqgF family
                     [General function prediction only]"
                     /db_xref="CDD:441980"
     Region          279..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PD05.2)"
     CDS             1..413
                     /gene="Zfp821"
                     /gene_synonym="4930566A11Rik; Znf821"
                     /coded_by="NM_001363383.1:459..1700"
                     /note="isoform a is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS40473.1"
                     /db_xref="GeneID:75871"
                     /db_xref="MGI:MGI:1923121"
ORIGIN      
        1 msrrkqtnpn kvhwdqvfag leeqarqamm ktdfpgdlgs qrqaiqqlrd qdssssdseg
       61 deeettqdev sshtseedgg vvkvekelet aeapvssgda laerevtenl nsdpllqlcq
      121 cplcqldcgs reqliahvyq htaavvsaks ymcpvcgral sspgslgrhl lihsedqrsn
      181 cavcgarfts hatfnseklp qvlnmesvpq vhsegpssae gkdiacsppv ypagillvcn
      241 ncaayrklle tqtpsvrkwa lrrqneplev rlqrlerert akksrrdnet peerevrrmr
      301 dreakrlqrm qetdeqrarr lqrdreamrl kranetpekr qarlirerea krlkrrlekm
      361 dmmlraqfgq dpsamaalaa emnffqlpvs gveldsqllg kmafeeqnns slh
//
LOCUS       NP_005937                 61 aa            linear   PRI 27-APR-2025
DEFINITION  metallothionein-1A [Homo sapiens].
ACCESSION   NP_005937
VERSION     NP_005937.2
DBSOURCE    REFSEQ: accession NM_005946.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Korkola,N.C. and Stillman,M.J.
  TITLE     Human apo-metallothionein 1a is not a random coil: Evidence from
            guanidinium chloride, high temperature, and acidic pH unfolding
            studies
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1872 (4), 141010 (2024)
   PUBMED   38490456
  REMARK    GeneRIF: Human apo-metallothionein 1a is not a random coil:
            Evidence from guanidinium chloride, high temperature, and acidic pH
            unfolding studies.
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Michalczyk,K., Kapczuk,P., Witczak,G., Tousty,P., Bosiacki,M.,
            Kurzawski,M., Chlubek,D. and Cymbaluk-Ploska,A.
  TITLE     An Assessment of MT1A (rs11076161), MT2A (rs28366003) and MT1L
            (rs10636) Gene Polymorphisms and MT2 Concentration in Women with
            Endometrial Pathologies
  JOURNAL   Genes (Basel) 14 (3), 773 (2023)
   PUBMED   36981043
  REMARK    GeneRIF: An Assessment of MT1A (rs11076161), MT2A (rs28366003) and
            MT1L (rs10636) Gene Polymorphisms and MT2 Concentration in Women
            with Endometrial Pathologies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 61)
  AUTHORS   Melenbacher,A., Korkola,N.C. and Stillman,M.J.
  TITLE     The pathways and domain specificity of Cu(I) binding to human
            metallothionein 1A
  JOURNAL   Metallomics 12 (12), 1951-1964 (2020)
   PUBMED   33225329
  REMARK    GeneRIF: The pathways and domain specificity of Cu(I) binding to
            human metallothionein 1A.
REFERENCE   4  (residues 1 to 61)
  AUTHORS   Thirumoorthy,N., Manisenthil Kumar,K.T., Shyam Sundar,A.,
            Panayappan,L. and Chatterjee,M.
  TITLE     Metallothionein: an overview
  JOURNAL   World J Gastroenterol 13 (7), 993-996 (2007)
   PUBMED   17373731
  REMARK    GeneRIF: One biomarker which has recently shown to be expressed in
            various human tumors but still less reported in carcinoma is
            metallothionein.
            Review article
REFERENCE   5  (residues 1 to 61)
  AUTHORS   Levadoux-Martin,M., Hesketh,J.E., Beattie,J.H. and Wallace,H.M.
  TITLE     Influence of metallothionein-1 localization on its function
  JOURNAL   Biochem J 355 (Pt 2), 473-479 (2001)
   PUBMED   11284736
REFERENCE   6  (residues 1 to 61)
  AUTHORS   Masters,B.A., Kelly,E.J., Quaife,C.J., Brinster,R.L. and
            Palmiter,R.D.
  TITLE     Targeted disruption of metallothionein I and II genes increases
            sensitivity to cadmium
  JOURNAL   Proc Natl Acad Sci U S A 91 (2), 584-588 (1994)
   PUBMED   8290567
  REMARK    GeneRIF: Disruption of metallothionein I and II genes in mouse
            produced viable mice with increased susceptibility to cadmium
            poisoning.
REFERENCE   7  (residues 1 to 61)
  AUTHORS   Grider,A., Bailey,L.B. and Cousins,R.J.
  TITLE     Erythrocyte metallothionein as an index of zinc status in humans
  JOURNAL   Proc Natl Acad Sci U S A 87 (4), 1259-1262 (1990)
   PUBMED   2304897
REFERENCE   8  (residues 1 to 61)
  AUTHORS   Sutherland,G.R., Baker,E., Callen,D.F., Garson,O.M. and West,A.K.
  TITLE     The human metallothionein gene cluster is not disrupted in
            myelomonocytic leukemia
  JOURNAL   Genomics 6 (1), 144-148 (1990)
   PUBMED   2303255
REFERENCE   9  (residues 1 to 61)
  AUTHORS   Le Beau,M.M., Diaz,M.O., Karin,M. and Rowley,J.D.
  TITLE     Metallothionein gene cluster is split by chromosome 16
            rearrangements in myelomonocytic leukaemia
  JOURNAL   Nature 313 (6004), 709-711 (1985)
   PUBMED   3856101
REFERENCE   10 (residues 1 to 61)
  AUTHORS   Karin,M., Eddy,R.L., Henry,W.M., Haley,L.L., Byers,M.G. and
            Shows,T.B.
  TITLE     Human metallothionein genes are clustered on chromosome 16
  JOURNAL   Proc Natl Acad Sci U S A 81 (17), 5494-5498 (1984)
   PUBMED   6089206
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY028617.1 and BC029475.1.
            
            On Jul 27, 2005 this sequence version replaced NP_005937.1.
            
            Summary: This gene is a member of the metallothionein family of
            genes. Proteins encoded by this gene family are low in molecular
            weight, are cysteine-rich, lack aromatic residues, and bind
            divalent heavy metal ions. The conserved cysteine residues
            co-ordinate metal ions using mercaptide linkages. These proteins
            act as anti-oxidants, protect against hydroxyl free radicals, are
            important in homeostatic control of metal in the cell, and play a
            role in detoxification of heavy metals. Disruption of two
            metallothionein genes in mouse resulted in defects in protection
            against heavy metals, oxidative stress, immune reactions,
            carcinogens, and displayed obesity. [provided by RefSeq, Sep 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY028617.1, BJ995397.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000290705.12/ ENSP00000290705.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..61
                     /product="metallothionein-1A"
                     /note="metallothionein 1A (functional); metallothionein
                     1S; metallothionein-IA"
                     /calculated_mol_wt=5989
     Region          1..29
                     /region_name="Beta"
                     /note="propagated from UniProtKB/Swiss-Prot (P04731.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P11957; propagated from
                     UniProtKB/Swiss-Prot (P04731.2)"
     Region          4..61
                     /region_name="Metallothio"
                     /note="Metallothionein; pfam00131"
                     /db_xref="CDD:395080"
     Region          30..61
                     /region_name="Alpha"
                     /note="propagated from UniProtKB/Swiss-Prot (P04731.2)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02795; propagated from
                     UniProtKB/Swiss-Prot (P04731.2)"
     CDS             1..61
                     /gene="MT1A"
                     /gene_synonym="MT-1A; MT-IA; MT1; MT1S; MTC"
                     /coded_by="NM_005946.3:74..259"
                     /db_xref="CCDS:CCDS32454.1"
                     /db_xref="GeneID:4489"
                     /db_xref="HGNC:HGNC:7393"
                     /db_xref="MIM:156350"
ORIGIN      
        1 mdpncscatg gsctctgsck ckeckctsck ksccsccpms cakcaqgcic kgasekcscc
       61 a
//
LOCUS       NP_001355187             101 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 234 isoform 5 [Mus musculus].
ACCESSION   NP_001355187 XP_006503542
VERSION     NP_001355187.1
DBSOURCE    REFSEQ: accession NM_001368258.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Tang,T., Li,L., Tang,J., Li,Y., Lin,W.Y., Martin,F., Grant,D.,
            Solloway,M., Parker,L., Ye,W., Forrest,W., Ghilardi,N., Oravecz,T.,
            Platt,K.A., Rice,D.S., Hansen,G.M., Abuin,A., Eberhart,D.E.,
            Godowski,P., Holt,K.H., Peterson,A., Zambrowicz,B.P. and de
            Sauvage,F.J.
  TITLE     A mouse knockout library for secreted and transmembrane proteins
  JOURNAL   Nat Biotechnol 28 (7), 749-755 (2010)
   PUBMED   20562862
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL671759.10.
            
            On Feb 1, 2019 this sequence version replaced XP_006503542.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR9219381.46556.1, CX230503.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 63.26 cM"
     Protein         1..101
                     /product="transmembrane protein 234 isoform 5"
                     /calculated_mol_wt=10497
     Region          <14..87
                     /region_name="TMEM234"
                     /note="Putative transmembrane family 234; cl46810"
                     /db_xref="CDD:481150"
     CDS             1..101
                     /gene="Tmem234"
                     /gene_synonym="1500002D11Rik; 2510006D16Rik;
                     4933407D05Rik"
                     /coded_by="NM_001368258.1:355..660"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:76799"
                     /db_xref="MGI:MGI:1924049"
ORIGIN      
        1 mptpvgrckp eqglsnwylm pfllnqsgsl lyyltlastd ltlavpicns laivftlivg
       61 kvlgediggk eavagmvlti tgitvcitss vsktqgqpsh s
//
LOCUS       NP_570116                382 aa            linear   PRI 27-APR-2025
DEFINITION  mucosal addressin cell adhesion molecule 1 isoform a precursor
            [Homo sapiens].
ACCESSION   NP_570116 NP_009095 NP_570117
VERSION     NP_570116.2
DBSOURCE    REFSEQ: accession NM_130760.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Jagtap,D., Bhor,V.M., Bhowmick,S., Kasarpalkar,N., Sagvekar,P.,
            Kulkarni,B., Pathak,M., Chatterjee,N., Dolas,P., Palav,H.,
            Kaginkar,S., Bhagat,S., Munshi,I., Parikh,S., Agrawal,S., Pawar,C.,
            Kaneria,M., Mahale,S.D., Shastri,J. and Patel,V.
  TITLE     sMAdCAM: IL-6 Ratio Influences Disease Progression and Anti-Viral
            Responses in SARS-CoV-2 Infection
  JOURNAL   Front Immunol 12, 619906 (2021)
   PUBMED   34194420
  REMARK    GeneRIF: sMAdCAM: IL-6 Ratio Influences Disease Progression and
            Anti-Viral Responses in SARS-CoV-2 Infection.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Kasarpalkar,N.J., Bhowmick,S., Patel,V., Savardekar,L., Agrawal,S.,
            Shastri,J. and Bhor,V.M.
  TITLE     Frequency of Effector Memory Cells Expressing Integrin alpha4beta7
            Is Associated With TGF-beta1 Levels in Therapy Naive HIV Infected
            Women With Low CD4+ T Cell Count
  JOURNAL   Front Immunol 12, 651122 (2021)
   PUBMED   33828560
  REMARK    GeneRIF: Frequency of Effector Memory Cells Expressing Integrin
            alpha4beta7 Is Associated With TGF-beta1 Levels in Therapy Naive
            HIV Infected Women With Low CD4(+) T Cell Count.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Allner,C., Melde,M., Becker,E., Fuchs,F., Muhl,L., Klenske,E.,
            Muller,L., Morgenstern,N., Fietkau,K., Hirschmann,S., Atreya,R.,
            Atreya,I., Neurath,M.F. and Zundler,S.
  TITLE     Baseline levels of dynamic CD4+ T cell adhesion to MAdCAM-1
            correlate with clinical response to vedolizumab treatment in
            ulcerative colitis: a cohort study
  JOURNAL   BMC Gastroenterol 20 (1), 103 (2020)
   PUBMED   32293299
  REMARK    GeneRIF: Baseline levels of dynamic CD4(+) T cell adhesion to
            MAdCAM-1 correlate with clinical response to vedolizumab treatment
            in ulcerative colitis: a cohort study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Satoh,T., Oikawa,H., Yashima-Abo,A., Nishiya,M. and Masuda,T.
  TITLE     Expression of mucosal addressin cell adhesion molecule-1 on the
            reticular framework between white pulp and the marginal zone in the
            human spleen
  JOURNAL   J Clin Exp Hematop 59 (4), 187-195 (2019)
   PUBMED   31866620
  REMARK    GeneRIF: n the present study, mucosal addressin cell adhesion
            molecule-1 was selectively expressed on alpha-smooth muscle
            actin-positive reticular framework. The reticular framework may
            function in lymphocyte homing and segregation into the
            periarteriolar lymphoid sheath, lymph follicle and marginal zone.
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Wang,J., Ma,L., Tang,X., Zhang,X., Qiao,Y., Shi,Y., Xu,Y., Wang,Z.,
            Yu,Y. and Sun,F.
  TITLE     Doxorubicin induces apoptosis by targeting Madcam1 and AKT and
            inhibiting protein translation initiation in hepatocellular
            carcinoma cells
  JOURNAL   Oncotarget 6 (27), 24075-24091 (2015)
   PUBMED   26124182
  REMARK    GeneRIF: Doxo-induced apoptosis has a role in inhibiting
            hepatocellular carcinoma by targeting Madcam1 and AKT and blocking
            protein translation initiation
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Leung,E., Berg,R.W., Langley,R., Greene,J., Raymond,L.A.,
            Augustus,M., Ni,J., Carter,K.C., Spurr,N., Choo,K.H. and
            Krissansen,G.W.
  TITLE     Genomic organization, chromosomal mapping, and analysis of the 5'
            promoter region of the human MAdCAM-1 gene
  JOURNAL   Immunogenetics 46 (2), 111-119 (1997)
   PUBMED   9162097
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Leung,E., Greene,J., Ni,J., Raymond,L.G., Lehnert,K., Langley,R.
            and Krissansen,G.W.
  TITLE     Cloning of the mucosal addressin MAdCAM-1 from human brain:
            identification of novel alternatively spliced transcripts
  JOURNAL   Immunol Cell Biol 74 (6), 490-496 (1996)
   PUBMED   8989586
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Shyjan,A.M., Bertagnolli,M., Kenney,C.J. and Briskin,M.J.
  TITLE     Human mucosal addressin cell adhesion molecule-1 (MAdCAM-1)
            demonstrates structural and functional similarities to the alpha 4
            beta 7-integrin binding domains of murine MAdCAM-1, but extreme
            divergence of mucin-like sequences
  JOURNAL   J Immunol 156 (8), 2851-2857 (1996)
   PUBMED   8609404
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Briskin,M.J., McEvoy,L.M. and Butcher,E.C.
  TITLE     MAdCAM-1 has homology to immunoglobulin and mucin-like adhesion
            receptors and to IgA1
  JOURNAL   Nature 363 (6428), 461-464 (1993)
   PUBMED   8502297
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Picker,L.J., Nakache,M. and Butcher,E.C.
  TITLE     Monoclonal antibodies to human lymphocyte homing receptors define a
            novel class of adhesion molecules on diverse cell types
  JOURNAL   J Cell Biol 109 (2), 927-937 (1989)
   PUBMED   2474557
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005775.1, U82483.1, U43628.1
            and DB323303.1.
            
            On or before Jun 23, 2006 this sequence version replaced
            NP_570117.1, NP_570116.1.
            
            Summary: The protein encoded by this gene is an endothelial cell
            adhesion molecule that interacts preferentially with the leukocyte
            beta7 integrin LPAM-1 (alpha4beta7), L-selectin, and VLA-4
            (alpha4beta1) on myeloid cells to direct leukocytes into mucosal
            and inflamed tissues. It is a member of the immunoglobulin family
            and is similar to ICAM1 and VCAM1. At least seven alternatively
            spliced transcripts encoding different protein isoforms have been
            found for this gene, but the full-length nature of some variants
            has not been determined. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the longer, predominant
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U82483.1, AY819760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215637.8/ ENSP00000215637.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..382
                     /product="mucosal addressin cell adhesion molecule 1
                     isoform a precursor"
                     /note="mucosal addressin cell adhesion molecule 1;
                     MAdCAM-1; hMAdCAM-1"
                     /calculated_mol_wt=38373
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1800
     mat_peptide     19..382
                     /product="mucosal addressin cell adhesion molecule 1
                     isoform a"
                     /calculated_mol_wt=38373
     Region          25..112
                     /region_name="IgI_MAdCAM-1"
                     /note="Immunoglobulin-like domain of Mucosal addressin
                     cell-adhesion molecule (MAdCAM-1); member of the I-set of
                     IgSF domains; cd20942"
                     /db_xref="CDD:409535"
     Region          25..30
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409535"
     Region          33..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409535"
     Region          41..49
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409535"
     Region          56..61
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409535"
     Region          63..65
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409535"
     Region          68..72
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409535"
     Region          76..81
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409535"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:23297416;
                     propagated from UniProtKB/Swiss-Prot (Q13477.2)"
     Region          90..98
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409535"
     Region          101..112
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409535"
     Region          113..224
                     /region_name="Adhes-Ig_like"
                     /note="Adhesion molecule, immunoglobulin-like; pfam09085"
                     /db_xref="CDD:430399"
     Region          <228..290
                     /region_name="MSA-2c"
                     /note="Merozoite surface antigen 2c; pfam12238"
                     /db_xref="CDD:289042"
     Region          232..271
                     /region_name="repeat expansion"
                     /note="length polymorphism due to repeat motif in
                     mucin-like region"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13477.2)"
     CDS             1..382
                     /gene="MADCAM1"
                     /gene_synonym="MACAM1"
                     /coded_by="NM_130760.3:15..1163"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12028.1"
                     /db_xref="GeneID:8174"
                     /db_xref="HGNC:HGNC:6765"
                     /db_xref="MIM:102670"
ORIGIN      
        1 mdfglallla gllglllgqs lqvkplqvep pepvvavalg asrqltcrla cadrgasvqw
       61 rgldtslgav qsdtgrsvlt vrnaslsaag trvcvgscgg rtfqhtvqll vyafpdqltv
      121 spaalvpgdp evactahkvt pvdpnalsfs llvggqeleg aqalgpevqe eeeepqgded
      181 vlfrvterwr lpplgtpvpp alycqatmrl pglelshrqa ipvlhsptsp eppdttspes
      241 pdttspespd ttsqeppdtt speppdktsp epapqqgsth tprspgstrt rrpeisqagp
      301 tqgeviptgs skpagdqlpa alwtssavlg llllalptyh lwkrcrhlae ddthppaslr
      361 llpqvsawag lrgtgqvgis ps
//
LOCUS       NP_001356638             559 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger Y-chromosomal protein isoform 6 [Homo sapiens].
ACCESSION   NP_001356638
VERSION     NP_001356638.1
DBSOURCE    REFSEQ: accession NM_001369709.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Ni,W., Perez,A.A., Schreiner,S., Nicolet,C.M. and Farnham,P.J.
  TITLE     Characterization of the ZFX family of transcription factors that
            bind downstream of the start site of CpG island promoters
  JOURNAL   Nucleic Acids Res 48 (11), 5986-6000 (2020)
   PUBMED   32406922
  REMARK    GeneRIF: Characterization of the ZFX family of transcription
            factors that bind downstream of the start site of CpG island
            promoters.
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Decarpentrie,F., Vernet,N., Mahadevaiah,S.K., Longepied,G.,
            Streichemberger,E., Aknin-Seifer,I., Ojarikre,O.A., Burgoyne,P.S.,
            Metzler-Guillemain,C. and Mitchell,M.J.
  TITLE     Human and mouse ZFY genes produce a conserved testis-specific
            transcript encoding a zinc finger protein with a short acidic
            domain and modified transactivation potential
  JOURNAL   Hum Mol Genet 21 (12), 2631-2645 (2012)
   PUBMED   22407129
  REMARK    GeneRIF: Studies identified a major testis-specific ZFY transcript
            that encodes a protein with the same short acidic domain.
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Tricoli,J.V. and Bracken,R.B.
  TITLE     ZFY gene expression and retention in human prostate adenocarcinoma
  JOURNAL   Genes Chromosomes Cancer 6 (2), 65-72 (1993)
   PUBMED   7680890
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Kochoyan,M., Keutmann,H.T. and Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            refinement of the NMR structure of an even finger by selective
            deuterium labeling and implications for DNA recognition
  JOURNAL   Biochemistry 30 (29), 7063-7072 (1991)
   PUBMED   1854720
REFERENCE   8  (residues 1 to 559)
  AUTHORS   North,M., Sargent,C., O'Brien,J., Taylor,K., Wolfe,J., Affara,N.A.
            and Ferguson-Smith,M.A.
  TITLE     Comparison of ZFY and ZFX gene structure and analysis of
            alternative 3' untranslated regions of ZFY
  JOURNAL   Nucleic Acids Res 19 (10), 2579-2586 (1991)
   PUBMED   2041734
REFERENCE   9  (residues 1 to 559)
  AUTHORS   Kochoyan,M., Havel,T.F., Nguyen,D.T., Dahl,C.E., Keutmann,H.T. and
            Weiss,M.A.
  TITLE     Alternating zinc fingers in the human male associated protein ZFY:
            2D NMR structure of an even finger and implications for
            'jumping-linker' DNA recognition
  JOURNAL   Biochemistry 30 (14), 3371-3386 (1991)
   PUBMED   1849423
REFERENCE   10 (residues 1 to 559)
  AUTHORS   Palmer,M.S., Berta,P., Sinclair,A.H., Pym,B. and Goodfellow,P.N.
  TITLE     Comparison of human ZFY and ZFX transcripts
  JOURNAL   Proc Natl Acad Sci U S A 87 (5), 1681-1685 (1990)
   PUBMED   2308929
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006157.2.
            
            Summary: This gene encodes a zinc finger-containing protein that
            may function as a transcription factor. This gene was once a
            candidate gene for the testis-determining factor (TDF) and was
            erroneously referred to as TDF. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.225725.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2467143
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yp11.2"
     Protein         1..559
                     /product="zinc finger Y-chromosomal protein isoform 6"
                     /note="zinc finger Y-chromosomal protein"
                     /calculated_mol_wt=64359
     Region          <22..164
                     /region_name="Zfx_Zfy_act"
                     /note="Zfx / Zfy transcription activation region;
                     pfam04704"
                     /db_xref="CDD:461400"
     Region          <181..>203
                     /region_name="ROS_MUCR"
                     /note="ROS/MUCR transcriptional regulator protein;
                     cl19880"
                     /db_xref="CDD:473244"
     Region          181..201
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          212..236
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          244..264
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(249,251,253,255..256,259..260,263,309,311,315..316,
                     319..320,323,337,339,341,343..344,347..348,351)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          297..>434
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          304..324
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          316..340
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          332..351
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          361..410
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          418..438
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          475..495
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(480,482,484,486..487,490..491,494,508,510,514..515,
                     518..519,523,537,539,541,543..544,547..548,551)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          487..511
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          503..524
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          532..552
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..559
                     /gene="ZFY"
                     /gene_synonym="ZNF911"
                     /coded_by="NM_001369709.1:95..1774"
                     /note="isoform 6 is encoded by transcript variant 11"
                     /db_xref="GeneID:7544"
                     /db_xref="HGNC:HGNC:12870"
                     /db_xref="MIM:490000"
ORIGIN      
        1 mdedefelqp qepnsffdgi vddagkiehd gstgvtidae semdpckvds tcpevikvyi
       61 fkadpgeddl ggtvdivese pendhgvell dqnssirvpr ekmvymtvnd sqqededlsn
      121 nsdgienrng tasallhide saglgrlakq kpkkkrrpds rqyqtaiiig pdghpltvyp
      181 cmicgkkfks rgflkrhmkn hpehlakkky hctdcdyttn kkislhnhle shkltskaek
      241 aiecdecgkh fshagalfth kmvhkekgan kmhkckfcey etaeqgllnr hllavhsknf
      301 phicvecgkg frhpselrkh mrihtgekpy qcqyceyrsa dssnlkthik tkhskempfk
      361 cdiclltfsd tkevqqhtlv hqeskthqcl hcdhkssnss dlkrhvisvh tkdyphkcem
      421 cekgfhrpse lkkhvavhkg kkmhqcrhcd fkiadpfvls rhilsvhtkd lpfrckrcrk
      481 gfrqqnelkk hmkthsgrkv yqceyceyst tdasgfkrhv isihtkdyph rceyckkgfr
      541 rpseknqhim rhhkevglp
//
LOCUS       NP_689526                504 aa            linear   PRI 27-APR-2025
DEFINITION  neutral amino acid uniporter 4 isoform 1 [Homo sapiens].
ACCESSION   NP_689526
VERSION     NP_689526.2
DBSOURCE    REFSEQ: accession NM_152313.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Fan,S.J., Snell,C., Turley,H., Li,J.L., McCormick,R., Perera,S.M.,
            Heublein,S., Kazi,S., Azad,A., Wilson,C., Harris,A.L. and
            Goberdhan,D.C.
  TITLE     PAT4 levels control amino-acid sensitivity of rapamycin-resistant
            mTORC1 from the Golgi and affect clinical outcome in colorectal
            cancer
  JOURNAL   Oncogene 35 (23), 3004-3015 (2016)
   PUBMED   26434594
  REMARK    GeneRIF: Data predict that colorectal cancer cells with high PAT4
            expression will be more resistant to depletion of serine and
            glutamine, allowing them to survive and outgrow neighbouring normal
            and tumorigenic cells.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Kerns,S.L., Stock,R.G., Stone,N.N., Blacksburg,S.R., Rath,L.,
            Vega,A., Fachal,L., Gomez-Caamano,A., De Ruysscher,D.,
            Lammering,G., Parliament,M., Blackshaw,M., Sia,M., Cesaretti,J.,
            Terk,M., Hixson,R., Rosenstein,B.S. and Ostrer,H.
  TITLE     Genome-wide association study identifies a region on chromosome
            11q14.3 associated with late rectal bleeding following radiation
            therapy for prostate cancer
  JOURNAL   Radiother Oncol 107 (3), 372-376 (2013)
   PUBMED   23719583
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Schioth,H.B., Roshanbin,S., Hagglund,M.G. and Fredriksson,R.
  TITLE     Evolutionary origin of amino acid transporter families SLC32, SLC36
            and SLC38 and physiological, pathological and therapeutic aspects
  JOURNAL   Mol Aspects Med 34 (2-3), 571-585 (2013)
   PUBMED   23506890
  REMARK    Review article
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Pillai,S.M. and Meredith,D.
  TITLE     SLC36A4 (hPAT4) is a high affinity amino acid transporter when
            expressed in Xenopus laevis oocytes
  JOURNAL   J Biol Chem 286 (4), 2455-2460 (2011)
   PUBMED   21097500
  REMARK    GeneRIF: SLC36A4 (hPAT4) is a high affinity amino acid transporter
            when expressed in Xenopus laevis oocytes.
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Heublein,S., Kazi,S., Ogmundsdottir,M.H., Attwood,E.V., Kala,S.,
            Boyd,C.A., Wilson,C. and Goberdhan,D.C.
  TITLE     Proton-assisted amino-acid transporters are conserved regulators of
            proliferation and amino-acid-dependent mTORC1 activation
  JOURNAL   Oncogene 29 (28), 4068-4079 (2010)
   PUBMED   20498635
  REMARK    GeneRIF: SLC36A4 has a similar in vivo growth regulatory activity
            to fly SLC36 family members when expressed in Drosophila and is
            also required for amino acid-dependent mTORC1 activation, and
            mTORC1-regulated proliferation in human cells.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003072.2, HY170772.1 and AY162216.1.
            
            On Jan 13, 2004 this sequence version replaced NP_689526.1.
            
            Summary: SLC36A4 belongs to the SLC36 family of amino acid
            transporters based on sequence similarity with other family members
            (e.g., SLC36A1; MIM 606561). SLC36 proteins contain about 500 amino
            acids and have 9 to 11 transmembrane domains. Unlike other SLC36
            family members, which are proton-coupled amino acid transporters,
            SLC36A4 is a high-affinity/low-capacity non-proton-coupled amino
            acid transporter (Pillai and Meredith, 2011 [PubMed
            21097500]).[supplied by OMIM, Feb 2011].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.230169.1,
                                           SRR1660803.15402.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159080 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326402.9/ ENSP00000317382.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..504
                     /product="neutral amino acid uniporter 4 isoform 1"
                     /note="proton-coupled amino acid transporter 4; solute
                     carrier family 36 (proton/amino acid symporter), member 4;
                     neutral amino acid uniporter 4"
                     /calculated_mol_wt=56026
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Region          58..476
                     /region_name="SLC5-6-like_sbd"
                     /note="Solute carrier families 5 and 6-like; solute
                     binding domain; cl00456"
                     /db_xref="CDD:444915"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Site            154..174
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Site            206..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Site            231..251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Site            273..293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Site            309..329
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Site            358..378
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Site            389..409
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Site            414..434
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Site            456..476
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YBV0.1)"
     Site            495
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6YBV0.1)"
     CDS             1..504
                     /gene="SLC36A4"
                     /gene_synonym="PAT4"
                     /coded_by="NM_152313.4:160..1674"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8291.1"
                     /db_xref="GeneID:120103"
                     /db_xref="HGNC:HGNC:19660"
                     /db_xref="MIM:613760"
ORIGIN      
        1 meaaatpaaa gaarreeldm dvmrplineq nfdgtsdeeh eqellpvqkh yqlddqegis
       61 fvqtlmhllk gnigtgllgl plaiknagiv lgpislvfig iisvhcmhil vrcshflclr
      121 fkkstlgysd tvsfamevsp wsclqkqaaw grsvvdfflv itqlgfcsvy ivflaenvkq
      181 vhegfleskv fisnstnssn pcerrsvdlr iymlcflpfi illvfirelk nlfvlsflan
      241 vsmavslvii yqyvvrnmpd phnlpivagw kkyplffgta vfafegigvv lplenqmkes
      301 krfpqalnig mgivttlyvt latlgymcfh deikgsitln lpqdvwlyqs vkilysfgif
      361 vtysiqfyvp aeiiipgits kfhtkwkqic efgirsflvs itcagailip rldivisfvg
      421 avssstlali lpplveiltf skehyniwmv lknisiaftg vvgfllgtyi tveeiiyptp
      481 kvvagtpqsp flnlnstclt sglk
//
LOCUS       NP_005984               1192 aa            linear   PRI 27-APR-2025
DEFINITION  tubulin-specific chaperone D isoform 1 [Homo sapiens].
ACCESSION   NP_005984
VERSION     NP_005984.3
DBSOURCE    REFSEQ: accession NM_005993.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1192)
  AUTHORS   Grinshpun-Cohen,J., Marans,R.S. and Singer,A.
  TITLE     [MOH SCREENING FOR TBCD IN COCHIN JEWS: COLLABORATION BETWEEN
            MEDICAL, RESEARCH AND COMMUNITY MEMBERS IN ACHIEVING PUBLIC HEALTH
            GOALS]
  JOURNAL   Harefuah 162 (6), 359-361 (2023)
   PUBMED   37394437
  REMARK    GeneRIF: [MOH SCREENING FOR TBCD IN COCHIN JEWS: COLLABORATION
            BETWEEN MEDICAL, RESEARCH AND COMMUNITY MEMBERS IN ACHIEVING PUBLIC
            HEALTH GOALS].
REFERENCE   2  (residues 1 to 1192)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1192)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1192)
  AUTHORS   Gronborg,S., Risom,L., Ek,J., Larsen,K.B., Scheie,D., Petkov,Y.,
            Larsen,V.A., Duno,M., Joensen,F. and Ostergaard,E.
  TITLE     A Faroese founder variant in TBCD causes early onset, progressive
            encephalopathy with a homogenous clinical course
  JOURNAL   Eur J Hum Genet 26 (10), 1512-1520 (2018)
   PUBMED   29921875
  REMARK    GeneRIF: We present a detailed description of the neuropathology
            and MR imaging characteristics of a subset of these patients,
            adding insight into the phenotype of TBCD-related encephalopathy.
            The finding of a Faroese founder variant will allow targeted
            genetic diagnostics in patients of Faroese descent as well as
            improved genetic counseling and testing of at-risk couples.
REFERENCE   5  (residues 1 to 1192)
  AUTHORS   Stephen,J., Nampoothiri,S., Vinayan,K.P., Yesodharan,D., Remesh,P.,
            Gahl,W.A. and Malicdan,M.C.V.
  TITLE     Cortical atrophy and hypofibrinogenemia due to FGG and TBCD
            mutations in a single family: a case report
  JOURNAL   BMC Med Genet 19 (1), 80 (2018)
   PUBMED   29769041
  REMARK    GeneRIF: Study identified a homozygous novel pathogenic missense
            mutation (c.1423G > A;p.Ala475Thr) in TBCD gene to be associated
            with concurrent hypofibrinogenemia and cortical atrophy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1192)
  AUTHORS   Bhamidipati,A., Lewis,S.A. and Cowan,N.J.
  TITLE     ADP ribosylation factor-like protein 2 (Arl2) regulates the
            interaction of tubulin-folding cofactor D with native tubulin
  JOURNAL   J Cell Biol 149 (5), 1087-1096 (2000)
   PUBMED   10831612
REFERENCE   7  (residues 1 to 1192)
  AUTHORS   Martin,L., Fanarraga,M.L., Aloria,K. and Zabala,J.C.
  TITLE     Tubulin folding cofactor D is a microtubule destabilizing protein
  JOURNAL   FEBS Lett 470 (1), 93-95 (2000)
   PUBMED   10722852
REFERENCE   8  (residues 1 to 1192)
  AUTHORS   Tian,G., Lewis,S.A., Feierbach,B., Stearns,T., Rommelaere,H.,
            Ampe,C. and Cowan,N.J.
  TITLE     Tubulin subunits exist in an activated conformational state
            generated and maintained by protein cofactors
  JOURNAL   J Cell Biol 138 (4), 821-832 (1997)
   PUBMED   9265649
REFERENCE   9  (residues 1 to 1192)
  AUTHORS   Tian,G., Huang,Y., Rommelaere,H., Vandekerckhove,J., Ampe,C. and
            Cowan,N.J.
  TITLE     Pathway leading to correctly folded beta-tubulin
  JOURNAL   Cell 86 (2), 287-296 (1996)
   PUBMED   8706133
REFERENCE   10 (residues 1 to 1192)
  AUTHORS   Lewis,S.A., Tian,G., Vainberg,I.E. and Cowan,N.J.
  TITLE     Chaperonin-mediated folding of actin and tubulin
  JOURNAL   J Cell Biol 132 (1-2), 1-4 (1996)
   PUBMED   8567715
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC003094.1, BI464569.1,
            BC012824.2 and AC130371.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 27, 2004 this sequence version replaced NP_005984.2.
            
            Summary: Cofactor D is one of four proteins (cofactors A, D, E, and
            C) involved in the pathway leading to correctly folded beta-tubulin
            from folding intermediates. Cofactors A and D are believed to play
            a role in capturing and stabilizing beta-tubulin intermediates in a
            quasi-native confirmation. Cofactor E binds to the cofactor
            D/beta-tubulin complex; interaction with cofactor C then causes the
            release of beta-tubulin polypeptides that are committed to the
            native state. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC003094.1, AB023205.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355528.9/ ENSP00000347719.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..1192
                     /product="tubulin-specific chaperone D isoform 1"
                     /note="tubulin-specific chaperone d; beta-tubulin cofactor
                     D"
                     /calculated_mol_wt=132469
     Region          63..>914
                     /region_name="TFCD_C"
                     /note="Tubulin folding cofactor D C terminal; cl19887"
                     /db_xref="CDD:473247"
     Region          361..399
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTW9.2)"
     Region          557..594
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTW9.2)"
     Region          596..632
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTW9.2)"
     Region          901..1087
                     /region_name="TFCD_C"
                     /note="Tubulin folding cofactor D C terminal; pfam12612"
                     /db_xref="CDD:463643"
     CDS             1..1192
                     /gene="TBCD"
                     /gene_synonym="PEBAT; SSD-1; tfcD"
                     /coded_by="NM_005993.5:130..3708"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45818.1"
                     /db_xref="GeneID:6904"
                     /db_xref="HGNC:HGNC:11581"
                     /db_xref="MIM:604649"
ORIGIN      
        1 malsdepaag gpeeeaedet lafgaaleaf gesaetrall grlrevhggg aerevalerf
       61 rvimdkyqeq phlldphlew mmnllldivq dqtspaslvh lafkflyiit kvrgyktflr
      121 lfphevadve pvldlvtiqn pkdheawetr ymlllwlsvt clipfdfsrl dgnlltqpgq
      181 armsimdril qiaesylivs dkardaaavl vsrfitrpdv kqskmaefld wslcnlarss
      241 fqtmqgvitm dgtlqalaqi fkhgkredcl pyaatvlrcl dgcrlpesnq tllrklgvkl
      301 vqrlgltflk pkvaawryqr gcrslaanlq lltqgqseqk plilteddde dddvpegver
      361 vieqllvglk dkdtvvrwsa akgigrmagr lpraladdvv gsvldcfsfq etdkawhggc
      421 lalaelgrrg lllpsrlvdv vavilkalty dekrgacsvg tnvrdaacyv cwafarayep
      481 qelkpfvtai ssalviaavf drdincrraa saafqenvgr qgtfphgidi lttadyfavg
      541 nrsncflvis vfiagfpeyt qpmidhlvtm kishwdgvir elaaralhnl aqqapefsat
      601 qvfprllsmt lspdlhmrhg silacaevay alyklaaqen rpvtdhldeq avqglkqihq
      661 qlydrqlyrg lggqlmrqav cvlieklsls kmpfrgdtvi dgwqwlindt lrhlhlissh
      721 srqqmkdaav salaalcsey ymkepgeadp aiqeelitqy laelrnpeem trcgfslalg
      781 alpgfllkgr lqqvltglra vthtspedvs faesrrdglk aiaricqtvg vkagapdeav
      841 cgenvsqiyc allgcmddyt tdsrgdvgtw vrkaamtslm dltlllarsq pelieahtce
      901 rimccvaqqa sekidrfrah aasvfltllh fdsppiphvp hrgeleklfp rsdvasvnws
      961 apsqafprit qllglptyry hvllglvvsl ggltestirh stqslfeymk giqsdpqalg
     1021 sfsgtllqif ednllnervs vpllktldhv lthgcfdift teedhpfavk llalckkeik
     1081 nskdiqklls giavfcemvq fpgdvrrqal lqlclllchr fplirkttas qvyetlltys
     1141 dvvgadvlde vvtvlsdtaw daelavvreq rnrlcdllgv prpqlvpqpg ac
//
LOCUS       NP_689408                430 aa            linear   PRI 27-APR-2025
DEFINITION  tumor necrosis factor receptor superfamily member 19L isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_689408
VERSION     NP_689408.1
DBSOURCE    REFSEQ: accession NM_152222.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Yao,W., Chen,Q., Li,S., Jia,X., Xu,L. and Wei,L.
  TITLE     RELT promotes the growth of esophageal squamous cell carcinoma by
            activating the NF-kappaB pathway
  JOURNAL   Cell Cycle 20 (13), 1231-1241 (2021)
   PUBMED   34121605
  REMARK    GeneRIF: RELT promotes the growth of esophageal squamous cell
            carcinoma by activating the NF-kappaB pathway.
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Nikolopoulos,G., Smith,C.E.L., Brookes,S.J., El-Asrag,M.E.,
            Brown,C.J., Patel,A., Murillo,G., O'Connell,M.J., Inglehearn,C.F.
            and Mighell,A.J.
  TITLE     New missense variants in RELT causing hypomineralised amelogenesis
            imperfecta
  JOURNAL   Clin Genet 97 (5), 688-695 (2020)
   PUBMED   32052416
  REMARK    GeneRIF: New missense variants in RELT causing hypomineralised
            amelogenesis imperfecta.
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Kim,J.W., Zhang,H., Seymen,F., Koruyucu,M., Hu,Y., Kang,J.,
            Kim,Y.J., Ikeda,A., Kasimoglu,Y., Bayram,M., Zhang,C., Kawasaki,K.,
            Bartlett,J.D., Saunders,T.L., Simmer,J.P. and Hu,J.C.
  TITLE     Mutations in RELT cause autosomal recessive amelogenesis imperfecta
  JOURNAL   Clin Genet 95 (3), 375-383 (2019)
   PUBMED   30506946
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Moua,P., Checketts,M., Xu,L.G., Shu,H.B., Reyland,M.E. and
            Cusick,J.K.
  TITLE     RELT family members activate p38 and induce apoptosis by a
            mechanism distinct from TNFR1
  JOURNAL   Biochem Biophys Res Commun 491 (1), 25-32 (2017)
   PUBMED   28688764
  REMARK    GeneRIF: Collectively, this study provides more insights into RELT
            expression, RELT family member function, and the mechanism of
            RELT-induced death.
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Cusick,J.K., Mustian,A., Jacobs,A.T. and Reyland,M.E.
  TITLE     Identification of PLSCR1 as a protein that interacts with RELT
            family members
  JOURNAL   Mol Cell Biochem 362 (1-2), 55-63 (2012)
   PUBMED   22052202
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Bossen,C., Ingold,K., Tardivel,A., Bodmer,J.L., Gaide,O.,
            Hertig,S., Ambrose,C., Tschopp,J. and Schneider,P.
  TITLE     Interactions of tumor necrosis factor (TNF) and TNF receptor family
            members in the mouse and human
  JOURNAL   J Biol Chem 281 (20), 13964-13971 (2006)
   PUBMED   16547002
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Polek,T.C., Talpaz,M. and Spivak-Kroizman,T.
  TITLE     The TNF receptor, RELT, binds SPAK and uses it to mediate p38 and
            JNK activation
  JOURNAL   Biochem Biophys Res Commun 343 (1), 125-134 (2006)
   PUBMED   16530727
REFERENCE   8  (residues 1 to 430)
  AUTHORS   Cusick,J.K., Xu,L.G., Bin,L.H., Han,K.J. and Shu,H.B.
  TITLE     Identification of RELT homologues that associate with RELT and are
            phosphorylated by OSR1
  JOURNAL   Biochem Biophys Res Commun 340 (2), 535-543 (2006)
   PUBMED   16389068
  REMARK    GeneRIF: Receptor expressed in lymphoid tissue (RELT) and its novel
            homologues RELL1 and RELL2 co-localize with one another at the
            plasma membrane.
REFERENCE   9  (residues 1 to 430)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   10 (residues 1 to 430)
  AUTHORS   Sica,G.L., Zhu,G., Tamada,K., Liu,D., Ni,J. and Chen,L.
  TITLE     RELT, a new member of the tumor necrosis factor receptor
            superfamily, is selectively expressed in hematopoietic tissues and
            activates transcription factor NF-kappaB
  JOURNAL   Blood 97 (9), 2702-2707 (2001)
   PUBMED   11313261
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000562.5 and AP000763.5.
            
            Summary: The protein encoded by this gene is a member of the
            TNF-receptor superfamily. This receptor is especially abundant in
            hematologic tissues. It has been shown to activate the NF-kappaB
            pathway and selectively bind TNF receptor-associated factor 1
            (TRAF1). This receptor is capable of stimulating T-cell
            proliferation in the presence of CD3 signaling, which suggests its
            regulatory role in immune response. Two alternatively spliced
            transcript variants of this gene encoding the same protein have
            been reported. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.628144.1, BC051810.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000064780.7/ ENSP00000064780.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..430
                     /product="tumor necrosis factor receptor superfamily
                     member 19L isoform 1 precursor"
                     /note="receptor expressed in lymphoid tissues; RELT tumor
                     necrosis factor receptor"
                     /calculated_mol_wt=43265
     sig_peptide     1..25
                     /note="/evidence=ECO:0000269|PubMed:11313261,
                     ECO:0000269|PubMed:15340161; propagated from
                     UniProtKB/Swiss-Prot (Q969Z4.1)"
                     /calculated_mol_wt=2846
     mat_peptide     26..430
                     /product="Tumor necrosis factor receptor superfamily
                     member 19L. /id=PRO_0000034599"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969Z4.1)"
                     /calculated_mol_wt=43265
     Region          27..112
                     /region_name="TNFRSF19L"
                     /note="tumor necrosis factor receptor superfamily member
                     19-like (TNFRSF19L), also known as receptor expressed in
                     lymphoid tissues (RELT); cd13419"
                     /db_xref="CDD:276924"
     Region          27..48
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276924"
     Region          50..90
                     /region_name="TNFR-Cys"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969Z4.1)"
     Region          51..90
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276924"
     Region          134..156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969Z4.1)"
     Site            149
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q969Z4.1)"
     Region          163..198
                     /region_name="RELT"
                     /note="Tumour necrosis factor receptor superfamily member
                     19; pfam12606"
                     /db_xref="CDD:403713"
     Site            163..183
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969Z4.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q969Z4.1)"
     Region          349..352
                     /region_name="RFRV motif, mediates interaction with STK39.
                     /evidence=ECO:0000269|PubMed:16530727"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969Z4.1)"
     Region          373..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969Z4.1)"
     CDS             1..430
                     /gene="RELT"
                     /gene_synonym="AI3C; TNFRSF19L; TRLT"
                     /coded_by="NM_152222.2:127..1419"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS8222.1"
                     /db_xref="GeneID:84957"
                     /db_xref="HGNC:HGNC:13764"
                     /db_xref="MIM:611211"
ORIGIN      
        1 mkpsllcrpl scflmllpwp latltsttlw qcppgeepdl dpgqgtlcrp cppgtfsaaw
       61 gsspcqphar cslwrrleaq vgmatrdtlc gdcwpgwfgp wgvprvpcqp cswaplgthg
      121 cdewgrrarr gvevaagass ggetrqpgng traggpeeta aqyaviaivp vfclmgllgi
      181 lvcnllkrkg yhctahkevg pgpggggsgi npayrtedan edtigvlvrl itekkenaaa
      241 leellkeyhs kqlvqtshrp vsklppappn vphicphrhh lhtvqglasl sgpccsrcsq
      301 kkwpevllsp eavaattpvp sllpnptrvp kagakagrqg eitilsvgrf rvaripeqrt
      361 ssmvsevkti teagpswgdl pdspqpglpp eqqallgsgg srtkwlkppa enkaeenryv
      421 vrlsesnlvi
//
LOCUS       NP_004288                355 aa            linear   PRI 27-APR-2025
DEFINITION  guanine nucleotide-binding protein subunit alpha-14 [Homo sapiens].
ACCESSION   NP_004288
VERSION     NP_004288.1
DBSOURCE    REFSEQ: accession NM_004297.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Ren,J., Cui,Z., Jiang,C., Wang,L., Guan,Y., Ren,Y., Zhang,S.,
            Tu,T., Yu,J., Li,Y., Duan,W., Guan,J., Wang,K., Zhang,H., Xing,D.,
            Kahn,M.L., Zhang,H. and Hong,T.
  TITLE     GNA14 and GNAQ somatic mutations cause spinal and intracranial
            extra-axial cavernous hemangiomas
  JOURNAL   Am J Hum Genet 111 (7), 1370-1382 (2024)
   PUBMED   38917801
  REMARK    GeneRIF: GNA14 and GNAQ somatic mutations cause spinal and
            intracranial extra-axial cavernous hemangiomas.
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Xu,C., Li,Y.M., Sun,B., Zhong,F.J. and Yang,L.Y.
  TITLE     GNA14's interaction with RACK1 inhibits hepatocellular carcinoma
            progression through reducing MAPK/JNK and PI3K/AKT signaling
            pathway
  JOURNAL   Carcinogenesis 42 (11), 1357-1369 (2021)
   PUBMED   34657150
  REMARK    GeneRIF: GNA14's interaction with RACK1 inhibits hepatocellular
            carcinoma progression through reducing MAPK/JNK and PI3K/AKT
            signaling pathway.
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Wang,J., Teng,F., Chai,H., Zhang,C., Liang,X. and Yang,Y.
  TITLE     GNA14 stimulation of KLF7 promotes malignant growth of endometrial
            cancer through upregulation of HAS2
  JOURNAL   BMC Cancer 21 (1), 456 (2021)
   PUBMED   33892667
  REMARK    GeneRIF: GNA14 stimulation of KLF7 promotes malignant growth of
            endometrial cancer through upregulation of HAS2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Song,G., Zhu,X., Xuan,Z., Zhao,L., Dong,H., Chen,J., Li,Z.,
            Song,W., Jin,C., Zhou,M., Xie,H., Zheng,S. and Song,P.
  TITLE     Hypermethylation of GNA14 and its tumor-suppressive role in
            hepatitis B virus-related hepatocellular carcinoma
  JOURNAL   Theranostics 11 (5), 2318-2333 (2021)
   PUBMED   33500727
  REMARK    GeneRIF: Hypermethylation of GNA14 and its tumor-suppressive role
            in hepatitis B virus-related hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Rubio,J.P., Levy,E.R., Dobson-Stone,C. and Monaco,A.P.
  TITLE     Genomic organization of the human galpha14 and Galphaq genes and
            mutation analysis in chorea-acanthocytosis (CHAC)
  JOURNAL   Genomics 57 (1), 84-93 (1999)
   PUBMED   10191087
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Kuang,Y., Wu,Y., Jiang,H. and Wu,D.
  TITLE     Selective G protein coupling by C-C chemokine receptors
  JOURNAL   J Biol Chem 271 (8), 3975-3978 (1996)
   PUBMED   8626727
REFERENCE   8  (residues 1 to 355)
  AUTHORS   Kleuss,C., Raw,A.S., Lee,E., Sprang,S.R. and Gilman,A.G.
  TITLE     Mechanism of GTP hydrolysis by G-protein alpha subunits
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9828-9831 (1994)
   PUBMED   7937899
REFERENCE   9  (residues 1 to 355)
  AUTHORS   Wu,D., LaRosa,G.J. and Simon,M.I.
  TITLE     G protein-coupled signal transduction pathways for interleukin-8
  JOURNAL   Science 261 (5117), 101-103 (1993)
   PUBMED   8316840
REFERENCE   10 (residues 1 to 355)
  AUTHORS   Berstein,G., Blank,J.L., Jhon,D.Y., Exton,J.H., Rhee,S.G. and
            Ross,E.M.
  TITLE     Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11,
            its physiologic regulator
  JOURNAL   Cell 70 (3), 411-418 (1992)
   PUBMED   1322796
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355535.14, AK312460.1,
            BC027886.1, AI629022.1, AL158159.14 and AI263118.1.
            
            Summary: This gene encodes a member of the guanine
            nucleotide-binding, or G protein family. G proteins are
            heterotrimers consisting of alpha, beta and gamma subunits. The
            encoded protein is a member of the alpha family of G proteins, more
            specifically the alpha q subfamily of G proteins. The encoded
            protein may play a role in pertussis-toxin resistant activation of
            phospholipase C-beta and its downstream effectors.[provided by
            RefSeq, Feb 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.91110.1,
                                           SRR1660807.57257.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341700.7/ ENSP00000365807.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.2"
     Protein         1..355
                     /product="guanine nucleotide-binding protein subunit
                     alpha-14"
                     /note="guanine nucleotide-binding protein 14; guanine
                     nucleotide binding protein (G protein), alpha 14; g
                     alpha-14; heterotrimeric guanine nucleotide-binding
                     protein 1I"
                     /calculated_mol_wt=41440
     Region          36..349
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Region          37..50
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (O95837.1)"
     Site            order(42,47..49,182,201,204,270..271,273,326..327)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            42..49
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(43..45,73,77,81,84,87..88,106,109,150,179,204,212,
                     216)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Region          174..182
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (O95837.1)"
     Site            177..185
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            182
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(183,185,187,198,200,204..206,208,211..212,214..217)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(185,210,213..214,217)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Region          197..206
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (O95837.1)"
     Site            201..204
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            202..218
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Region          266..273
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (O95837.1)"
     Site            270..273
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(318..329,331..334)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Region          325..330
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (O95837.1)"
     Site            326..328
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..355
                     /gene="GNA14"
                     /gene_synonym="HG1I"
                     /coded_by="NM_004297.4:530..1597"
                     /db_xref="CCDS:CCDS6657.1"
                     /db_xref="GeneID:9630"
                     /db_xref="HGNC:HGNC:4382"
                     /db_xref="MIM:604397"
ORIGIN      
        1 magccclsae ekesqrisae ierqlrrdkk darrelklll lgtgesgkst fikqmriihg
       61 sgysdedrkg ftklvyqnif tamqamiram dtlriqyvce qnkenaqiir evevdkvsml
      121 sreqveaikq lwqdpgiqec ydrrreyqls dsakyyltdi driatpsfvp tqqdvlrvrv
      181 pttgiieypf dleniifrmv dvggqrserr kwihcfesvt siiflvalse ydqvlaecdn
      241 enrmeeskal fktiitypwf lnssvilfln kkdlleekim yshlisyfpe ytgpkqdvra
      301 ardfilklyq dqnpdkekvi yshftcatdt dnirfvfaav kdtilqlnlr efnlv
//
LOCUS       NP_001356444             196 aa            linear   PRI 27-APR-2025
DEFINITION  protein maestro isoform b [Homo sapiens].
ACCESSION   NP_001356444 XP_016881525
VERSION     NP_001356444.1
DBSOURCE    REFSEQ: accession NM_001369515.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Kenigsberg,S., Lima,P.D., Maghen,L., Wyse,B.A., Lackan,C.,
            Cheung,A.N., Tsang,B.K. and Librach,C.L.
  TITLE     The elusive MAESTRO gene: Its human reproductive tissue-specific
            expression pattern
  JOURNAL   PLoS One 12 (4), e0174873 (2017)
   PUBMED   28406912
  REMARK    GeneRIF: study also shows a punctate nuclear expression pattern and
            disperse cytoplasmic expression pattern of the MRO protein in human
            granulosa-cumulus cells and in testicular germ cells, which was
            later validated by western blotting
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
  REMARK    GeneRIF: The sequence and function of the related mouse gene are
            described.
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Yanaihara,N., Kohno,T., Takakura,S., Takei,K., Otsuka,A.,
            Sunaga,N., Takahashi,M., Yamazaki,M., Tashiro,H., Fukuzumi,Y.,
            Fujimori,Y., Hagiwara,K., Tanaka,T. and Yokota,J.
  TITLE     Physical and transcriptional map of a 311-kb segment of chromosome
            18q21, a candidate lung tumor suppressor locus
  JOURNAL   Genomics 72 (2), 169-179 (2001)
   PUBMED   11401430
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015864.5.
            
            On Apr 10, 2019 this sequence version replaced XP_016881525.1.
            
            Summary: This gene is specifically transcribed in males before and
            after differentiation of testis, and the encoded protein may play
            an important role in a mammalian sex determination. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.5235.1,
                                           SRR1803616.215434.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..196
                     /product="protein maestro isoform b"
                     /note="beside the Ma29 deletion; protein maestro;
                     male-specific transcription in the developing reproductive
                     organs"
                     /calculated_mol_wt=22885
     CDS             1..196
                     /gene="MRO"
                     /gene_synonym="B29; C18orf3"
                     /coded_by="NM_001369515.2:247..837"
                     /note="isoform b is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS45869.1"
                     /db_xref="GeneID:83876"
                     /db_xref="HGNC:HGNC:24121"
                     /db_xref="MIM:608080"
ORIGIN      
        1 mdqrqrrilg qplsiptsqp kqkrtsmisf fskvswklrf qkreplknvf filaerardp
       61 sakkrhmamr nlgtmayeap dkvrkykkiv ldllvyglyd pvnlevihes mktltvvlgk
      121 iqgkglgsff iditlqtrtl lddackttfq acspylklke eysfqseedq rntklyqqls
      181 hyhpeilqff yankil
//
LOCUS       NP_001035373             367 aa            linear   PRI 27-APR-2025
DEFINITION  doublesex- and mab-3-related transcription factor C2 [Homo
            sapiens].
ACCESSION   NP_001035373
VERSION     NP_001035373.1
DBSOURCE    REFSEQ: accession NM_001040283.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Ottolenghi,C., Fellous,M., Barbieri,M. and McElreavey,K.
  TITLE     Novel paralogy relations among human chromosomes support a link
            between the phylogeny of doublesex-related genes and the evolution
            of sex determination
  JOURNAL   Genomics 79 (3), 333-343 (2002)
   PUBMED   11863363
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB026313.1, AJ291669.1, AC243967.3 and AC010616.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029202.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269945.8/ ENSP00000269945.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..367
                     /product="doublesex- and mab-3-related transcription
                     factor C2"
                     /calculated_mol_wt=38993
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXT2.2)"
     Region          38..84
                     /region_name="DM"
                     /note="DM DNA binding domain; pfam00751"
                     /db_xref="CDD:459924"
     Region          103..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXT2.2)"
     Region          239..366
                     /region_name="DMRT-like"
                     /note="Doublesex-and mab-3-related transcription factor C1
                     and C2; pfam15791"
                     /db_xref="CDD:464871"
     CDS             1..367
                     /gene="DMRTC2"
                     /coded_by="NM_001040283.3:65..1168"
                     /db_xref="CCDS:CCDS33034.1"
                     /db_xref="GeneID:63946"
                     /db_xref="HGNC:HGNC:13911"
                     /db_xref="MIM:614806"
ORIGIN      
        1 mepsdmpagy hcpldsapwd etrdpqstel iprraisrsp tcarcrnhgv tahlkghkrl
       61 clfqacechk cvlilerrrv maaqvalrrq qeaqlkkhlm rrgeaspkap nhfrkgttqp
      121 qvpsgkenia pqpqtphgav llaptppgkn scgplllshp peasplswtp vppgpwvpgh
      181 wlppgfsmpp pvvcrllyqe pavslppfpg fdpgtslqlp thgpfttcpg shpvltapls
      241 gepqgppsqp rthstlilqp cgtpdplqlq pqasgascla rtsgpsewql qqeaaealvg
      301 lkdssqaprv tpsvppnpaw isllhpcgpp apaggrgfqp vgpclrpspa psvalhigrl
      361 gsislls
//
LOCUS       NP_005951               3323 aa            linear   PRI 27-APR-2025
DEFINITION  mucin-3A precursor [Homo sapiens].
ACCESSION   NP_005951
VERSION     NP_005951.1
DBSOURCE    REFSEQ: accession NM_005960.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3323)
  AUTHORS   Sotoudeh,M., Mansouri,V., Shakeri,R., Sharififard,B., Sajadi,N.,
            Haghpanah,V. and Naderi,M.
  TITLE     Decoding the expression pattern of MUC3A in gastric adenocarcinoma:
            unveiling the key to successful immunotherapy
  JOURNAL   Expert Opin Ther Targets 27 (12), 1299-1305 (2023)
   PUBMED   38069509
  REMARK    GeneRIF: Decoding the expression pattern of MUC3A in gastric
            adenocarcinoma: unveiling the key to successful immunotherapy.
REFERENCE   2  (residues 1 to 3323)
  AUTHORS   Su,W., Feng,B., Hu,L., Guo,X. and Yu,M.
  TITLE     MUC3A promotes the progression of colorectal cancer through the
            PI3K/Akt/mTOR pathway
  JOURNAL   BMC Cancer 22 (1), 602 (2022)
   PUBMED   35655161
  REMARK    GeneRIF: MUC3A promotes the progression of colorectal cancer
            through the PI3K/Akt/mTOR pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 3323)
  AUTHORS   Sun,Y., Sun,X., You,C., Ma,S., Luo,Y., Peng,S., Tang,F., Tian,X.,
            Wang,F., Huang,Z., Yu,H., Xiao,Y., Wang,X., Zhang,J., Gong,Y. and
            Xie,C.
  TITLE     MUC3A promotes non-small cell lung cancer progression via
            activating the NFkappaB pathway and attenuates radiosensitivity
  JOURNAL   Int J Biol Sci 17 (10), 2523-2536 (2021)
   PUBMED   34326691
  REMARK    GeneRIF: MUC3A promotes non-small cell lung cancer progression via
            activating the NFkappaB pathway and attenuates radiosensitivity.
            Erratum:[Int J Biol Sci. 2022 Nov 3;18(16):6226. doi:
            10.7150/ijbs.79140. PMID: 36439877]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3323)
  AUTHORS   Gum,J.R. Jr., Hicks,J.W., Crawley,S.C., Dahl,C.M., Yang,S.C.,
            Roberton,A.M. and Kim,Y.S.
  TITLE     Initiation of transcription of the MUC3A human intestinal mucin
            from a TATA-less promoter and comparison with the MUC3B amino
            terminus
  JOURNAL   J Biol Chem 278 (49), 49600-49609 (2003)
   PUBMED   12958310
  REMARK    GeneRIF: has highly conserved amino and carboxyl termini,
            suggesting a recent duplication of the entire ancestral gene
REFERENCE   5  (residues 1 to 3323)
  AUTHORS   Pratt,W.S., Crawley,S., Hicks,J., Ho,J., Nash,M., Kim,Y.S.,
            Gum,J.R. and Swallow,D.M.
  TITLE     Multiple transcripts of MUC3: evidence for two genes, MUC3A and
            MUC3B
  JOURNAL   Biochem Biophys Res Commun 275 (3), 916-923 (2000)
   PUBMED   10973822
REFERENCE   6  (residues 1 to 3323)
  AUTHORS   Crawley,S.C., Gum,J.R. Jr., Hicks,J.W., Pratt,W.S., Aubert,J.P.,
            Swallow,D.M. and Kim,Y.S.
  TITLE     Genomic organization and structure of the 3' region of human MUC3:
            alternative splicing predicts membrane-bound and soluble forms of
            the mucin
  JOURNAL   Biochem Biophys Res Commun 263 (3), 728-736 (1999)
   PUBMED   10512748
REFERENCE   7  (residues 1 to 3323)
  AUTHORS   Gum,J.R. Jr., Ho,J.J., Pratt,W.S., Hicks,J.W., Hill,A.S.,
            Vinall,L.E., Roberton,A.M., Swallow,D.M. and Kim,Y.S.
  TITLE     MUC3 human intestinal mucin. Analysis of gene structure, the
            carboxyl terminus, and a novel upstream repetitive region
  JOURNAL   J Biol Chem 272 (42), 26678-26686 (1997)
   PUBMED   9334251
REFERENCE   8  (residues 1 to 3323)
  AUTHORS   Gendler,S.J. and Spicer,A.P.
  TITLE     Epithelial mucin genes
  JOURNAL   Annu Rev Physiol 57, 607-634 (1995)
   PUBMED   7778880
  REMARK    Review article
REFERENCE   9  (residues 1 to 3323)
  AUTHORS   Fox,M.F., Lahbib,F., Pratt,W., Attwood,J., Gum,J., Kim,Y. and
            Swallow,D.M.
  TITLE     Regional localization of the intestinal mucin gene MUC3 to
            chromosome 7q22
  JOURNAL   Ann Hum Genet 56 (4), 281-287 (1992)
   PUBMED   1362870
REFERENCE   10 (residues 1 to 3323)
  AUTHORS   Gum,J.R., Hicks,J.W., Swallow,D.M., Lagace,R.L., Byrd,J.C.,
            Lamport,D.T., Siddiki,B. and Kim,Y.S.
  TITLE     Molecular cloning of cDNAs derived from a novel human intestinal
            mucin gene
  JOURNAL   Biochem Biophys Res Commun 171 (1), 407-415 (1990)
   PUBMED   2393399
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC254629.1, BI005786.1 and AB038784.1.
            
            Summary: The mucin genes encode epithelial glycoproteins, some of
            which are secreted and some membrane bound. Each of the genes
            contains at least one large domain of tandemly repeated sequence
            that encodes the peptide sequence rich in serine and/or threonine
            residues, which carries most of the O-linked glycosylation (Gendler
            and Spicer, 1995 [PubMed 7778880]).[supplied by OMIM, Aug 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The genomic coordinates used for
            the transcript record were based on transcript alignments and on
            publication data (PMIDs: 9334251, 10512748, 10973822, 12958310).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000379458.9/ ENSP00000368771.5
            RefSeq Select criteria    :: based on single protein-coding
                                         transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..3323
                     /product="mucin-3A precursor"
                     /note="mucin 3, intestinal; mucin-3A; intestinal mucin"
                     /calculated_mol_wt=343446
     sig_peptide     1..15
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02505.3)"
                     /calculated_mol_wt=1700
     mat_peptide     16..3323
                     /product="Mucin-3A. /id=PRO_0000158955"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
                     /calculated_mol_wt=343446
     Region          114..>284
                     /region_name="Chi1"
                     /note="Chitinase [Carbohydrate transport and metabolism];
                     COG3469"
                     /db_xref="CDD:442692"
     Region          218..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          251..1871
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          270..289
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          325..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          359..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          539..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          700..722
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          734..756
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          909..991
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          1170..1201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          1318..1356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          1380..1442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          1484..1509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          1714..1746
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          1793..1844
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          1893..2446
                     /region_name="32 X approximate tandem repeats,
                     Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          1900..2056
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          2100..2447
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          2464..2508
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          2578..2608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          2631..2656
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          2834..2858
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          2897..2937
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     Region          2958..2998
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Region          3033..3117
                     /region_name="SEA"
                     /note="SEA domain; pfam01390"
                     /db_xref="CDD:460188"
     Site            3227..3247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02505.3)"
     CDS             1..3323
                     /gene="MUC3A"
                     /gene_synonym="MUC-3A; MUC3"
                     /coded_by="NM_005960.2:92..10063"
                     /db_xref="CCDS:CCDS78262.1"
                     /db_xref="GeneID:4584"
                     /db_xref="HGNC:HGNC:7513"
                     /db_xref="MIM:158371"
ORIGIN      
        1 mqllgllgll wmlkaspwat gtlstatsis qvpfpraeaa savlsnsphs rdlagwplgv
       61 pqlaspapgh renapmtltt sphdtliset llnspvssnt sttptskfaf kvettpptvl
      121 vysattecvy ptsfiitish ptsicvtttq vaftssytst pvtqkpvttv tstysmttte
      181 kgtsamtssp stttaretpi vtvtpssvsa tdttfhttis sttrttertp lptgsihttt
      241 sptpvfttlk tavtstspit ssitstntvt smtttasqpt atntlssptr tilsstpvls
      301 tetitsgitn ttplstlvtt lpttisrstp tsettyttsp tstvtdsttk iaystsmtgt
      361 lstetslppt ssslptteta ttpmtnlvtt tteisshstp sfssstiyst vststtaiss
      421 lpptsgtmvt sttmtpssls tdipfttptt ithhsvgstg flttatdlts tftvssssam
      481 stsvipssps iqntetsslv smtsattpnv rptfvstlst ptssllttfp atysfsssms
      541 assagtthte sissppasts tlhttaestl apttttsftt sttmeppstt aattgtgqtt
      601 ftsstatfpe tttptpttdm steslttamt sppitssvts tntvtsmttt tspptttnsf
      661 tsltsmplss tpvpstevvt sgtintipps ilvttlptpn assmttsett ypnsptgpgt
      721 nstteitypt tmtetsstat slpptsplvs taktaktptt nlvttttktt shsttsftss
      781 tvystastyt taitsvpttl gtmvtstsmi sstvstgipt sqpttitpss vgisgslpmm
      841 tdltsvytvs nmsarpttvi pssptvqnte isisvsmtsa ttpsggptft stentptrsl
      901 ltsfpmthsf sssmsessag tthtesissp rgttstlhtt vestpspttt tsfttstmme
      961 ppsstvsttg rgqttfpsst atfpetttlt pttdistvsl ttamtspppv sssitptntm
     1021 tsmrtttywp tatntlsplt ssilsstpvp stemitshtt nttplstlvt tllttitrst
     1081 ptsettypts ptsivsdstt eitystsitg tlstattlpp tssslpttet atmtptttli
     1141 tttpnttsls tpsftsstiy stvststtai ssasptsgtm vtsttmtpss lstdtpsttp
     1201 ttitypsvgs tgflttatdl tstftvssss amstsvipss psiqntetss lvsmtsattp
     1261 slrptitstd stltsslltt fpstysfsss msassagtth tetisslpas tntihttaes
     1321 alapttttsf ttsptmepps ttvattgtgq ttfpsstatf letttltptt dfstesltta
     1381 mtstppitss itptdtmtsm rtttswptat ntlspltssi lsstpvpste vttshttntn
     1441 pvstlvttlp ititrstlts etaypsspts tvtestteit ypttmtetss tatslpptss
     1501 lvstaetakt pttnlvtttt kttshsttsf tsstiystas tpttaitsvp ttlgtmvtst
     1561 smipstvstg iptsqpttit pssvgisgsl pmmtdltsvy tvssmsarpt svipssptvq
     1621 ntetsifvsm msattpsggp tftstentpt rslltsfpvt hsfsssmsas svgtthtqsi
     1681 ssppaitstl httaestpsp tttmsfttft kmetpsstva ttgtgqttft sstatspktt
     1741 tltptsdist gsfktavsst ppitssitst ytvtsmtttt plgptatntl psftssvsss
     1801 tpvpsteait sgttnttpls tlvttfsnsd tsstptsett yptsltsalt dsttrttyst
     1861 nmtgtlstvt slrptsssll ttvtatvptt nlvttttkit shstpsftss iattetpshs
     1921 tprftssitt tetpshstpr ftssitntkt tshsspsfts sitttettsh ntpsltssit
     1981 ttkttshstp sytslitttt ttshstpsft ssitttetts hntpsltssi tttettshst
     2041 psftssitte ttshstpsft slititeits hstlsyttsi tttetpshst lsftssittt
     2101 ettshstpsf tssittsemp shstpsftss itttenaths tpnftssitt tettshstps
     2161 ftslitttet tshrwgttet tsystpsfts sntitettsh stpsyitsit ttetpssstp
     2221 sfsssittte ttshstpgft ssitttetts hstpsftssi tttettshdt psftssitts
     2281 etpshstpss tslitttktt shstpsftss itttettshs ahsftssitt tettshntrs
     2341 ftssitttet nshsttsfts sitttettsh stpsfsssit ttetplhstp gltswvtttk
     2401 ttshitpglt ssitttetts hstpgftssi tttettsest pslssstiys tvststtait
     2461 shfttsetav tptpvtpssl stdipttslr tltpssvgts tslttttdfp siptdistlp
     2521 trthiisssp siqstetssl vgttsptmst vrmtlriten tpissfstsi vvipetptqt
     2581 ppvltsatgt qtspapttvt fgstdsstst lhtltpstal stivstsqvp ipsthsstlq
     2641 ttpstpslqt sltstseftt esftrgstst nailtsfsti iwsstptiim ssspssasit
     2701 pvfsttihsv psspyifste nvgsasitgf pslsssatts tsstsssltt alteitpfsy
     2761 islpsttpcp gtititivpa sptdpcvemd psteatsppt tpltvfpftt emvtcptsis
     2821 iqttlttymd tssmmpeses sispnassst gtgtvptntv ftstrlptse twlsnssvip
     2881 lplpgvstip ltmkpssslp tilrtsskst hpsppttrts etpvattqtp ttltsrrttr
     2941 itsqmttqst ltttagtcdn ggtweqgqca clpgfsgdrc qlqtrcqngg qwdglkcqcp
     3001 stfygsscef aveqvdldvv etevgmevsv dqqfspdlnd ntsqayrdfn ktfwnqmqki
     3061 fadmqgftfk gveilslrng sivvdylvll empfspqles eyeqvkttlk eglqnasqdv
     3121 nscqdsqtlc fkpdsikvnn nskteltpaa icrraaptgy eefyfplvea trlrcvtkct
     3181 sgvdnaidch qgqcvletsg ptcrcystdt hwfsgprcev avhwralvgg ltagaallvl
     3241 lllalgvrav rsgwwggqrr grswdqdrkw fetwdeevvg tfsnwgfedd gtdkdtnfyv
     3301 alenvdttmk vhikrpemts ssv
//
LOCUS       NP_001380               2012 aa            linear   PRI 27-APR-2025
DEFINITION  cell adhesion molecule DSCAM isoform CHD2-42 precursor [Homo
            sapiens].
ACCESSION   NP_001380
VERSION     NP_001380.2
DBSOURCE    REFSEQ: accession NM_001389.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2012)
  AUTHORS   McKean,D.M., Zhang,Q., Narayan,P., Morton,S.U., Strohmenger,V.,
            Tang,V.T., McAllister,S., Sharma,A., Quiat,D., Reichart,D.,
            DeLaughter,D.M., Wakimoto,H., Gorham,J.M., Brown,K., McDonough,B.,
            Willcox,J.A., Jang,M.Y., DePalma,S.R., Ward,T., Kim,R.,
            Cleveland,J.D., Seidman,J.G. and Seidman,C.E.
  CONSRTM   Pediatric Cardiac Genomics Consortium Investigators
  TITLE     Increased endothelial sclerostin caused by elevated DSCAM mediates
            multiple trisomy 21 phenotypes
  JOURNAL   J Clin Invest 134 (11), e167811 (2024)
   PUBMED   38828726
  REMARK    GeneRIF: Increased endothelial sclerostin caused by elevated DSCAM
            mediates multiple trisomy 21 phenotypes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2012)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2012)
  AUTHORS   Wang,N., Yang,Y., Jia,G.Z., Wang,K., Zhou,S., Zhang,B., Zhang,Z.S.,
            Qiao,Q. and He,X.L.
  TITLE     Long non-coding RNA Down syndrome cell adhesion molecule-anti-sense
            1 promotes gastric carcinoma cell proliferation and migration by
            regulating the miR-204/TPT1 axis
  JOURNAL   Hum Exp Toxicol 40 (12_suppl), S187-S195 (2021)
   PUBMED   34372727
  REMARK    GeneRIF: Long non-coding RNA Down syndrome cell adhesion
            molecule-anti-sense 1 promotes gastric carcinoma cell proliferation
            and migration by regulating the miR-204/TPT1 axis.
REFERENCE   4  (residues 1 to 2012)
  AUTHORS   Lim,C.S., Kim,M.J., Choi,J.E., Islam,M.A., Lee,Y.K., Xiong,Y.,
            Shim,K.W., Yang,J.E., Lee,R.U., Lee,J., Park,P., Kwak,J.H., Seo,H.,
            Kim,C.H., Lee,J.H., Lee,Y.S., Hwang,S.K., Lee,K., Lee,J.A. and
            Kaang,B.K.
  TITLE     Dysfunction of NMDA receptors in neuronal models of an autism
            spectrum disorder patient with a DSCAM mutation and in
            Dscam-knockout mice
  JOURNAL   Mol Psychiatry 26 (12), 7538-7549 (2021)
   PUBMED   34253863
  REMARK    GeneRIF: Dysfunction of NMDA receptors in neuronal models of an
            autism spectrum disorder patient with a DSCAM mutation and in
            Dscam-knockout mice.
REFERENCE   5  (residues 1 to 2012)
  AUTHORS   Lemieux,M., Thiry,L., Laflamme,O.D. and Bretzner,F.
  TITLE     Role of DSCAM in the Development of Neural Control of Movement and
            Locomotion
  JOURNAL   Int J Mol Sci 22 (16), 8511 (2021)
   PUBMED   34445216
  REMARK    GeneRIF: Role of DSCAM in the Development of Neural Control of
            Movement and Locomotion.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2012)
  AUTHORS   Meijers,R., Puettmann-Holgado,R., Skiniotis,G., Liu,J.H., Walz,T.,
            Wang,J.H. and Schmucker,D.
  TITLE     Structural basis of Dscam isoform specificity
  JOURNAL   Nature 449 (7161), 487-491 (2007)
   PUBMED   17721508
  REMARK    GeneRIF: The specificity of Drosophila Dscam is due to
            complementarity of variable residues in epitope I.
REFERENCE   7  (residues 1 to 2012)
  AUTHORS   Barlow,G.M., Lyons,G.E., Richardson,J.A., Sarnat,H.B. and
            Korenberg,J.R.
  TITLE     DSCAM: an endogenous promoter drives expression in the developing
            CNS and neural crest
  JOURNAL   Biochem Biophys Res Commun 299 (1), 1-6 (2002)
   PUBMED   12435380
  REMARK    GeneRIF: A specific promoter region directs expression of DSCAM in
            the developing choroid plexus and roof of the fourth ventricle, the
            floor plate of the fourth ventricle, pons and medulla oblongata,
            and the eye, limb buds, and dorsal root ganglion
REFERENCE   8  (residues 1 to 2012)
  AUTHORS   Barlow,G.M., Micales,B., Chen,X.N., Lyons,G.E. and Korenberg,J.R.
  TITLE     Mammalian DSCAMs: roles in the development of the spinal cord,
            cortex, and cerebellum?
  JOURNAL   Biochem Biophys Res Commun 293 (3), 881-891 (2002)
   PUBMED   12051741
REFERENCE   9  (residues 1 to 2012)
  AUTHORS   Agarwala,K.L., Nakamura,S., Tsutsumi,Y. and Yamakawa,K.
  TITLE     Down syndrome cell adhesion molecule DSCAM mediates homophilic
            intercellular adhesion
  JOURNAL   Brain Res Mol Brain Res 79 (1-2), 118-126 (2000)
   PUBMED   10925149
REFERENCE   10 (residues 1 to 2012)
  AUTHORS   Yamakawa,K., Huot,Y.K., Haendelt,M.A., Hubert,R., Chen,X.N.,
            Lyons,G.E. and Korenberg,J.R.
  TITLE     DSCAM: a novel member of the immunoglobulin superfamily maps in a
            Down syndrome region and is involved in the development of the
            nervous system
  JOURNAL   Hum Mol Genet 7 (2), 227-237 (1998)
   PUBMED   9426258
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF043945.2, AF217525.1,
            BE503065.1, AF064862.2 and BM684380.1.
            
            On Apr 10, 2002 this sequence version replaced NP_001380.1.
            
            Summary: This gene is a member of the immunoglobulin superfamily of
            cell adhesion molecules (Ig-CAMs), and is involved in human central
            and peripheral nervous system development. This gene is a candidate
            for Down syndrome and congenital heart disease (DSCHD). A gene
            encoding a similar Ig-CAM protein is located on chromosome 11.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Oct
            2012].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (CHD2-42).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF217525.1, AB209136.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000400454.6/ ENSP00000383303.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2012
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.2"
     Protein         1..2012
                     /product="cell adhesion molecule DSCAM isoform CHD2-42
                     precursor"
                     /note="Down syndrome cell adhesion molecule; cell adhesion
                     molecule DSCAM"
                     /calculated_mol_wt=220304
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1974
     mat_peptide     18..2012
                     /product="Cell adhesion molecule DSCAM.
                     /id=PRO_0000014747"
                     /note="propagated from UniProtKB/Swiss-Prot (O60469.2)"
                     /calculated_mol_wt=220304
     Region          26..121
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            28
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          42..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          55..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            78
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          79..83
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          99..104
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          112..116
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          125..210
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          141..145
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          157..161
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          179..183
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          192..199
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          235..310
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          242..246
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          255..259
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          290..295
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          313..395
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          331..335
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          344..348
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          368..372
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          382..387
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          406..501
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          424..428
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          437..441
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          467..471
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            470
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          481..486
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            487
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          494..497
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          504..593
                     /region_name="IgI_5_Dscam"
                     /note="Fifth immunoglobulin domain of the Drosophila
                     melanogaster Dscam protein, and similar domains; a member
                     of the I-set of IgSF domains; cd20958"
                     /db_xref="CDD:409550"
     Region          505..507
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409550"
     Region          512..516
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409550"
     Site            512
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          519..526
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409550"
     Region          533..539
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409550"
     Region          540..542
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409550"
     Region          549..553
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409550"
     Site            556
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          557..563
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409550"
     Region          571..579
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409550"
     Region          583..593
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409550"
     Region          596..686
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          613..617
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          627..631
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          652..656
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            658
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          666..671
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            666
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          679..682
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          689..784
                     /region_name="Ig_DSCAM"
                     /note="Immunoglobulin (Ig)-like domain of Down Syndrome
                     Cell Adhesion molecule (DSCAM); cd05734"
                     /db_xref="CDD:409397"
     Region          689..693
                     /region_name="putative Ig strand A"
                     /note="putative Ig strand A [structural motif]"
                     /db_xref="CDD:409397"
     Region          698..702
                     /region_name="putative Ig strand A'"
                     /note="putative Ig strand A' [structural motif]"
                     /db_xref="CDD:409397"
     Region          704..714
                     /region_name="putative Ig strand B"
                     /note="putative Ig strand B [structural motif]"
                     /db_xref="CDD:409397"
     Site            710
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          720..726
                     /region_name="putative Ig strand C"
                     /note="putative Ig strand C [structural motif]"
                     /db_xref="CDD:409397"
     Region          733..736
                     /region_name="putative Ig strand C'"
                     /note="putative Ig strand C' [structural motif]"
                     /db_xref="CDD:409397"
     Region          744..747
                     /region_name="putative Ig strand D"
                     /note="putative Ig strand D [structural motif]"
                     /db_xref="CDD:409397"
     Site            748
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          749..755
                     /region_name="putative Ig strand E"
                     /note="putative Ig strand E [structural motif]"
                     /db_xref="CDD:409397"
     Region          762..770
                     /region_name="putative Ig strand F"
                     /note="putative Ig strand F [structural motif]"
                     /db_xref="CDD:409397"
     Region          775..784
                     /region_name="putative Ig strand G"
                     /note="putative Ig strand G [structural motif]"
                     /db_xref="CDD:409397"
     Region          785..884
                     /region_name="Ig_DSCAM"
                     /note="Immunoglobulin (Ig) domain of Down Syndrome Cell
                     Adhesion molecule (DSCAM); cd05735"
                     /db_xref="CDD:409398"
     Region          785..788
                     /region_name="putative Ig strand A"
                     /note="putative Ig strand A [structural motif]"
                     /db_xref="CDD:409398"
     Site            795
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          796..800
                     /region_name="putative Ig strand A'"
                     /note="putative Ig strand A' [structural motif]"
                     /db_xref="CDD:409398"
     Region          803..810
                     /region_name="putative Ig strand B"
                     /note="putative Ig strand B [structural motif]"
                     /db_xref="CDD:409398"
     Region          818..824
                     /region_name="putative Ig strand C"
                     /note="putative Ig strand C [structural motif]"
                     /db_xref="CDD:409398"
     Region          833..836
                     /region_name="putative Ig strand C'"
                     /note="putative Ig strand C' [structural motif]"
                     /db_xref="CDD:409398"
     Region          842..846
                     /region_name="putative Ig strand D"
                     /note="putative Ig strand D [structural motif]"
                     /db_xref="CDD:409398"
     Region          848..854
                     /region_name="putative Ig strand E"
                     /note="putative Ig strand E [structural motif]"
                     /db_xref="CDD:409398"
     Region          861..869
                     /region_name="putative Ig strand F"
                     /note="putative Ig strand F [structural motif]"
                     /db_xref="CDD:409398"
     Region          872..882
                     /region_name="putative Ig strand G"
                     /note="putative Ig strand G [structural motif]"
                     /db_xref="CDD:409398"
     Region          885..978
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(885,952,967)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            924
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          <937..1300
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            order(968..969,971..972)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            1142
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Site            1160
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Site            1250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Site            1271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          1287..1363
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            1341
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Region          1380..1470
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(1380,1443,1458)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(1459..1460,1462..1463)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1486..1555
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            1488
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60469.2)"
     Site            1596..1616
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60469.2)"
     Region          1617..2012
                     /region_name="Required for netrin-mediated axon repulsion
                     of neuronal growth cones.
                     /evidence=ECO:0000250|UniProtKB:Q9ERC8"
                     /note="propagated from UniProtKB/Swiss-Prot (O60469.2)"
     Region          1718..1810
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60469.2)"
     Region          1855..1883
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60469.2)"
     Region          1971..2012
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60469.2)"
     CDS             1..2012
                     /gene="DSCAM"
                     /gene_synonym="CHD2; CHD2-42; CHD2-52"
                     /coded_by="NM_001389.5:498..6536"
                     /note="isoform CHD2-42 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS42929.1"
                     /db_xref="GeneID:1826"
                     /db_xref="HGNC:HGNC:3039"
                     /db_xref="MIM:602523"
ORIGIN      
        1 mwilalslfq sfanvfsedl hsslyfvnas lqevvfastt gtlvpcpaag ippvtlrwyl
       61 atgeeiydvp girhvhpngt lqifpfppss fstlihdnty yctaenpsgk irsqdvhika
      121 vlrepytvrv edqktmrgnv avfkciipss veayitvvsw ekdtvslvsg srflitstga
      181 lyikdvqned glynyrcitr hrytgetrqs nsarlfvsdp ansapsildg fdhrkamagq
      241 rvelpckalg hpepdyrwlk dnmplelsgr fqktvtglli enirpsdsgs yvcevsnryg
      301 takvigrlyv kqplkatisp rkvkssvgsq vslscsvtgt edqelswyrn geilnpgknv
      361 ritginhenl imdhmvksdg gayqcfvrkd klsaqdyvqv vledgtpkii safsekvvsp
      421 aepvslmcnv kgtplptitw tldddpilkg gshrisqmit segnvvsyln isssqvrdgg
      481 vyrctannsa gvvlyqarin vrgpasirpm knitaiagrd tyihcrvigy pyysikwykn
      541 snllpfnhrq vafenngtlk lsdvqkevde geytcnvlvq pqlstsqsvh vtvkvppfiq
      601 pfefprfsig qrvfipcvvv sgdlpititw qkdgrpipgs lgvtidnidf tsslrisnls
      661 lmhngnytci arneaaaveh qsqlivrvpp kfvvqprdqd giygkaviln csaegypvpt
      721 ivwkfskgag vpqfqpialn griqvlsngs llikhvveed sgyylckvsn dvgadvsksm
      781 yltvkipami tsypnttlat qgqkkemsct ahgekpiivr wekedriinp emarylvstk
      841 evgeevistl qilptvreds gffschains ygedrgiiql tvqeppdppe ieikdvkart
      901 itlrwtmgfd gnspitgydi ecknksdswd saqrtkdvsp qlnsatiidi hpsstysirm
      961 yaknrigkse psneltitad eaapdgppqe vhlepissqs irvtwkapkk hlqngiirgy
     1021 qigyreystg gnfqfniisv dtsgdsevyt ldnlnkftqy glvvqacnra gtgpssqeii
     1081 tttledvpsy ppenvqaiat spesisisws tlskealngi lqgfrviywa nlmdgelgei
     1141 knitttqpsl eldglekytn ysiqvlaftr agdgvrseqi ftrtkedvpg ppagvkaaaa
     1201 sasmvfvswl pplklngiir kytvfcshpy ptvisefeas pdsfsyripn lsrnrqysvw
     1261 vvavtsagrg nsseiitvep lakaparilt fsgtvttpwm kdivlpckav gdpspavkwm
     1321 kdsngtpslv tidgrrsifs ngsfiirtvk aedsgyysci annnwgsdei ilnlqvqvpp
     1381 dqprltvskt tsssitlswl pgdnggssir gyilqysedn seqwgsfpis psersyrlen
     1441 lkcgtwykft ltaqngvgpg riseiieakt lgkepqfske qelfasintt rvrlnligwn
     1501 dggcpitsft leyrpfgttv wttaqrtsls ksyilydlqe atwyelqmrv cnsagcaekq
     1561 anfatlnydg stippliksv vqneeglttn eglkmlvtis cilvgvlllf vlllvvrrrr
     1621 reqrlkrlrd akslaemlms kntrtsdtls kqqqtlrmhi dipraqllie erdtmetidd
     1681 rstvlltdad fgeaakqksl tvthtvhyqs vsqatgplvd vsdarpgtnp ttrrnakagp
     1741 tarnryasqw tlnrphptis ahtlttdwrl ptpraagsvd kesdsysvsp sqdtdrarss
     1801 mvstesasst yeelarayeh akmeeqlrha kftitecfis dtsseqltag tneytdslts
     1861 stpsesgicr ftasppkpqd ggrvmnmavp kahrpgdlih lppylrmdfl lnrggpgtsr
     1921 dlslgqacle pqksrtlkrp tvlepipmea assasstreg qswqpgavat lpqregaelg
     1981 qaakmsssqe slldsrghlk gnnpyaksyt lv
//
LOCUS       NP_057602                390 aa            linear   PRI 27-APR-2025
DEFINITION  peroxisomal sarcosine oxidase [Homo sapiens].
ACCESSION   NP_057602
VERSION     NP_057602.2
DBSOURCE    REFSEQ: accession NM_016518.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Jugessur,A., Shi,M., Gjessing,H.K., Lie,R.T., Wilcox,A.J.,
            Weinberg,C.R., Christensen,K., Boyles,A.L., Daack-Hirsch,S.,
            Nguyen,T.T., Christiansen,L., Lidral,A.C. and Murray,J.C.
  TITLE     Maternal genes and facial clefts in offspring: a comprehensive
            search for genetic associations in two population-based cleft
            studies from Scandinavia
  JOURNAL   PLoS One 5 (7), e11493 (2010)
   PUBMED   20634891
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   5  (residues 1 to 390)
  AUTHORS   IJlst,L., de Kromme,I., Oostheim,W. and Wanders,R.J.
  TITLE     Molecular cloning and expression of human L-pipecolate oxidase
  JOURNAL   Biochem Biophys Res Commun 270 (3), 1101-1105 (2000)
   PUBMED   10772957
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Dodt,G., Kim,D.G., Reimann,S.A., Reuber,B.E., McCabe,K., Gould,S.J.
            and Mihalik,S.J.
  TITLE     L-Pipecolic acid oxidase, a human enzyme essential for the
            degradation of L-pipecolic acid, is most similar to the monomeric
            sarcosine oxidases
  JOURNAL   Biochem J 345 Pt 3 (Pt 3), 487-494 (2000)
   PUBMED   10642506
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Dodt,G., Kim,D., Reimann,S., McCabe,K., Gould,S.J. and Mihalik,S.J.
  TITLE     The human L-pipecolic acid oxidase is similar to bacterial
            monomeric sarcosine oxidases rather than D-amino acid oxidases
  JOURNAL   Cell Biochem Biophys 32 Spring, 313-316 (2000)
   PUBMED   11330064
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC008960.2 and AF134593.1.
            
            On Mar 4, 2005 this sequence version replaced NP_057602.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.681203.1,
                                           SRR1660805.63733.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323372.9/ ENSP00000317721.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..390
                     /product="peroxisomal sarcosine oxidase"
                     /EC_number="1.5.3.1"
                     /EC_number="1.5.3.7"
                     /note="L-pipecolic acid oxidase; PSO; L-pipecolate
                     oxidase"
                     /calculated_mol_wt=43935
     Region          8..388
                     /region_name="soxA_mon"
                     /note="sarcosine oxidase, monomeric form; TIGR01377"
                     /db_xref="CDD:130444"
     Site            126
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D826; propagated from
                     UniProtKB/Swiss-Prot (Q9P0Z9.2)"
     Region          388..390
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0Z9.2)"
     CDS             1..390
                     /gene="PIPOX"
                     /gene_synonym="LPIPOX"
                     /coded_by="NM_016518.3:86..1258"
                     /db_xref="CCDS:CCDS11248.1"
                     /db_xref="GeneID:51268"
                     /db_xref="HGNC:HGNC:17804"
                     /db_xref="MIM:616713"
ORIGIN      
        1 maaqkdlwda ivigagiqgc ftayhlakhr krillleqff lphsrgsshg qsriirkayl
       61 edfytrmmhe cyqiwaqleh eagtqlhrqt gllllgmken qelktiqanl srqrvehqcl
      121 sseelkqrfp nirlprgevg lldnsggviy aykalralqd airqlggivr dgekvveinp
      181 gllvtvktts rsyqakslvi tagpwtnqll rplgiemplq tlrinvcywr emvpgsygvs
      241 qafpcflwlg lcphhiyglp tgeypglmkv syhhgnhadp eerdcptart digdvqilss
      301 fvrdhlpdlk pepaviescm ytntpdeqfi ldrhpkydni vigagfsghg fklapvvgki
      361 lyelsmkltp sydlapfris rfpslgkahl
//
LOCUS       NP_055786                817 aa            linear   PRI 27-APR-2025
DEFINITION  protein EFR3 homolog B isoform 1 [Homo sapiens].
ACCESSION   NP_055786 XP_001717639 XP_039733 XP_945557
VERSION     NP_055786.1
DBSOURCE    REFSEQ: accession NM_014971.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Baskin,J.M., Wu,X., Christiano,R., Oh,M.S., Schauder,C.M.,
            Gazzerro,E., Messa,M., Baldassari,S., Assereto,S., Biancheri,R.,
            Zara,F., Minetti,C., Raimondi,A., Simons,M., Walther,T.C.,
            Reinisch,K.M. and De Camilli,P.
  TITLE     The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P
            synthesis at the plasma membrane
  JOURNAL   Nat Cell Biol 18 (1), 132-138 (2016)
   PUBMED   26571211
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Bojjireddy,N., Guzman-Hernandez,M.L., Reinhard,N.R., Jovic,M. and
            Balla,T.
  TITLE     EFR3s are palmitoylated plasma membrane proteins that control
            responsiveness to G-protein-coupled receptors
  JOURNAL   J Cell Sci 128 (1), 118-128 (2015)
   PUBMED   25380825
  REMARK    GeneRIF: These data suggest that mammalian Efr3s contribute to the
            control of the phosphorylation state and, hence, desensitization of
            AT1a receptors, and could affect responsiveness of
            G-protein-coupled receptors in higher eukaryotes.
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Graff,M., Ngwa,J.S., Workalemahu,T., Homuth,G., Schipf,S.,
            Teumer,A., Volzke,H., Wallaschofski,H., Abecasis,G.R., Edward,L.,
            Francesco,C., Sanna,S., Scheet,P., Schlessinger,D., Sidore,C.,
            Xiao,X., Wang,Z., Chanock,S.J., Jacobs,K.B., Hayes,R.B., Hu,F., Van
            Dam,R.M., Crout,R.J., Marazita,M.L., Shaffer,J.R., Atwood,L.D.,
            Fox,C.S., Heard-Costa,N.L., White,C., Choh,A.C., Czerwinski,S.A.,
            Demerath,E.W., Dyer,T.D., Towne,B., Amin,N., Oostra,B.A., Van
            Duijn,C.M., Zillikens,M.C., Esko,T., Nelis,M., Nikopensius,T.,
            Metspalu,A., Strachan,D.P., Monda,K., Qi,L., North,K.E.,
            Cupples,L.A., Gordon-Larsen,P. and Berndt,S.I.
  CONSRTM   GIANT Consortium
  TITLE     Genome-wide analysis of BMI in adolescents and young adults reveals
            additional insight into the effects of genetic loci over the life
            course
  JOURNAL   Hum Mol Genet 22 (17), 3597-3607 (2013)
   PUBMED   23669352
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Berndt,S.I., Gustafsson,S., Magi,R., Ganna,A., Wheeler,E.,
            Feitosa,M.F., Justice,A.E., Monda,K.L., Croteau-Chonka,D.C.,
            Day,F.R., Esko,T., Fall,T., Ferreira,T., Gentilini,D.,
            Jackson,A.U., Luan,J., Randall,J.C., Vedantam,S., Willer,C.J.,
            Winkler,T.W., Wood,A.R., Workalemahu,T., Hu,Y.J., Lee,S.H.,
            Liang,L., Lin,D.Y., Min,J.L., Neale,B.M., Thorleifsson,G., Yang,J.,
            Albrecht,E., Amin,N., Bragg-Gresham,J.L., Cadby,G., den Heijer,M.,
            Eklund,N., Fischer,K., Goel,A., Hottenga,J.J., Huffman,J.E.,
            Jarick,I., Johansson,A., Johnson,T., Kanoni,S., Kleber,M.E.,
            Konig,I.R., Kristiansson,K., Kutalik,Z., Lamina,C., Lecoeur,C.,
            Li,G., Mangino,M., McArdle,W.L., Medina-Gomez,C.,
            Muller-Nurasyid,M., Ngwa,J.S., Nolte,I.M., Paternoster,L.,
            Pechlivanis,S., Perola,M., Peters,M.J., Preuss,M., Rose,L.M.,
            Shi,J., Shungin,D., Smith,A.V., Strawbridge,R.J., Surakka,I.,
            Teumer,A., Trip,M.D., Tyrer,J., Van Vliet-Ostaptchouk,J.V.,
            Vandenput,L., Waite,L.L., Zhao,J.H., Absher,D., Asselbergs,F.W.,
            Atalay,M., Attwood,A.P., Balmforth,A.J., Basart,H., Beilby,J.,
            Bonnycastle,L.L., Brambilla,P., Bruinenberg,M., Campbell,H.,
            Chasman,D.I., Chines,P.S., Collins,F.S., Connell,J.M.,
            Cookson,W.O., de Faire,U., de Vegt,F., Dei,M., Dimitriou,M.,
            Edkins,S., Estrada,K., Evans,D.M., Farrall,M., Ferrario,M.M.,
            Ferrieres,J., Franke,L., Frau,F., Gejman,P.V., Grallert,H.,
            Gronberg,H., Gudnason,V., Hall,A.S., Hall,P., Hartikainen,A.L.,
            Hayward,C., Heard-Costa,N.L., Heath,A.C., Hebebrand,J., Homuth,G.,
            Hu,F.B., Hunt,S.E., Hypponen,E., Iribarren,C., Jacobs,K.B.,
            Jansson,J.O., Jula,A., Kahonen,M., Kathiresan,S., Kee,F.,
            Khaw,K.T., Kivimaki,M., Koenig,W., Kraja,A.T., Kumari,M.,
            Kuulasmaa,K., Kuusisto,J., Laitinen,J.H., Lakka,T.A.,
            Langenberg,C., Launer,L.J., Lind,L., Lindstrom,J., Liu,J.,
            Liuzzi,A., Lokki,M.L., Lorentzon,M., Madden,P.A., Magnusson,P.K.,
            Manunta,P., Marek,D., Marz,W., Mateo Leach,I., McKnight,B.,
            Medland,S.E., Mihailov,E., Milani,L., Montgomery,G.W., Mooser,V.,
            Muhleisen,T.W., Munroe,P.B., Musk,A.W., Narisu,N., Navis,G.,
            Nicholson,G., Nohr,E.A., Ong,K.K., Oostra,B.A., Palmer,C.N.,
            Palotie,A., Peden,J.F., Pedersen,N., Peters,A., Polasek,O.,
            Pouta,A., Pramstaller,P.P., Prokopenko,I., Putter,C.,
            Radhakrishnan,A., Raitakari,O., Rendon,A., Rivadeneira,F.,
            Rudan,I., Saaristo,T.E., Sambrook,J.G., Sanders,A.R., Sanna,S.,
            Saramies,J., Schipf,S., Schreiber,S., Schunkert,H., Shin,S.Y.,
            Signorini,S., Sinisalo,J., Skrobek,B., Soranzo,N., Stancakova,A.,
            Stark,K., Stephens,J.C., Stirrups,K., Stolk,R.P., Stumvoll,M.,
            Swift,A.J., Theodoraki,E.V., Thorand,B., Tregouet,D.A., Tremoli,E.,
            Van der Klauw,M.M., van Meurs,J.B., Vermeulen,S.H., Viikari,J.,
            Virtamo,J., Vitart,V., Waeber,G., Wang,Z., Widen,E., Wild,S.H.,
            Willemsen,G., Winkelmann,B.R., Witteman,J.C., Wolffenbuttel,B.H.,
            Wong,A., Wright,A.F., Zillikens,M.C., Amouyel,P., Boehm,B.O.,
            Boerwinkle,E., Boomsma,D.I., Caulfield,M.J., Chanock,S.J.,
            Cupples,L.A., Cusi,D., Dedoussis,G.V., Erdmann,J., Eriksson,J.G.,
            Franks,P.W., Froguel,P., Gieger,C., Gyllensten,U., Hamsten,A.,
            Harris,T.B., Hengstenberg,C., Hicks,A.A., Hingorani,A., Hinney,A.,
            Hofman,A., Hovingh,K.G., Hveem,K., Illig,T., Jarvelin,M.R.,
            Jockel,K.H., Keinanen-Kiukaanniemi,S.M., Kiemeney,L.A., Kuh,D.,
            Laakso,M., Lehtimaki,T., Levinson,D.F., Martin,N.G., Metspalu,A.,
            Morris,A.D., Nieminen,M.S., Njolstad,I., Ohlsson,C.,
            Oldehinkel,A.J., Ouwehand,W.H., Palmer,L.J., Penninx,B., Power,C.,
            Province,M.A., Psaty,B.M., Qi,L., Rauramaa,R., Ridker,P.M.,
            Ripatti,S., Salomaa,V., Samani,N.J., Snieder,H., Sorensen,T.I.,
            Spector,T.D., Stefansson,K., Tonjes,A., Tuomilehto,J.,
            Uitterlinden,A.G., Uusitupa,M., van der Harst,P., Vollenweider,P.,
            Wallaschofski,H., Wareham,N.J., Watkins,H., Wichmann,H.E.,
            Wilson,J.F., Abecasis,G.R., Assimes,T.L., Barroso,I., Boehnke,M.,
            Borecki,I.B., Deloukas,P., Fox,C.S., Frayling,T., Groop,L.C.,
            Haritunian,T., Heid,I.M., Hunter,D., Kaplan,R.C., Karpe,F.,
            Moffatt,M.F., Mohlke,K.L., O'Connell,J.R., Pawitan,Y., Schadt,E.E.,
            Schlessinger,D., Steinthorsdottir,V., Strachan,D.P.,
            Thorsteinsdottir,U., van Duijn,C.M., Visscher,P.M., Di Blasio,A.M.,
            Hirschhorn,J.N., Lindgren,C.M., Morris,A.P., Meyre,D., Scherag,A.,
            McCarthy,M.I., Speliotes,E.K., North,K.E., Loos,R.J. and
            Ingelsson,E.
  TITLE     Genome-wide meta-analysis identifies 11 new loci for anthropometric
            traits and provides insights into genetic architecture
  JOURNAL   Nat Genet 45 (5), 501-512 (2013)
   PUBMED   23563607
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Melen,E., Granell,R., Kogevinas,M., Strachan,D., Gonzalez,J.R.,
            Wjst,M., Jarvis,D., Ege,M., Braun-Fahrlander,C., Genuneit,J.,
            Horak,E., Bouzigon,E., Demenais,F., Kauffmann,F., Siroux,V.,
            Michel,S., von Berg,A., Heinzmann,A., Kabesch,M.,
            Probst-Hensch,N.M., Curjuric,I., Imboden,M., Rochat,T.,
            Henderson,J., Sterne,J.A., McArdle,W.L., Hui,J., James,A.L.,
            William Musk,A., Palmer,L.J., Becker,A., Kozyrskyj,A.L.,
            Chan-Young,M., Park,J.E., Leung,A., Daley,D., Freidin,M.B.,
            Deev,I.A., Ogorodova,L.M., Puzyrev,V.P., Celedon,J.C., Brehm,J.M.,
            Cloutier,M.M., Canino,G., Acosta-Perez,E., Soto-Quiros,M.,
            Avila,L., Bergstrom,A., Magnusson,J., Soderhall,C., Kull,I.,
            Scholtens,S., Marike Boezen,H., Koppelman,G.H., Wijga,A.H.,
            Marenholz,I., Esparza-Gordillo,J., Lau,S., Lee,Y.A., Standl,M.,
            Tiesler,C.M., Flexeder,C., Heinrich,J., Myers,R.A., Ober,C.,
            Nicolae,D.L., Farrall,M., Kumar,A., Moffatt,M.F., Cookson,W.O. and
            Lasky-Su,J.
  TITLE     Genome-wide association study of body mass index in 23 000
            individuals with and without asthma
  JOURNAL   Clin Exp Allergy 43 (4), 463-474 (2013)
   PUBMED   23517042
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Nakatsu,F., Baskin,J.M., Chung,J., Tanner,L.B., Shui,G., Lee,S.Y.,
            Pirruccello,M., Hao,M., Ingolia,N.T., Wenk,M.R. and De Camilli,P.
  TITLE     PtdIns4P synthesis by PI4KIIIalpha at the plasma membrane and its
            impact on plasma membrane identity
  JOURNAL   J Cell Biol 199 (6), 1003-1016 (2012)
   PUBMED   23229899
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Bradfield,J.P., Qu,H.Q., Wang,K., Zhang,H., Sleiman,P.M., Kim,C.E.,
            Mentch,F.D., Qiu,H., Glessner,J.T., Thomas,K.A., Frackelton,E.C.,
            Chiavacci,R.M., Imielinski,M., Monos,D.S., Pandey,R., Bakay,M.,
            Grant,S.F., Polychronakos,C. and Hakonarson,H.
  TITLE     A genome-wide meta-analysis of six type 1 diabetes cohorts
            identifies multiple associated loci
  JOURNAL   PLoS Genet 7 (9), e1002293 (2011)
   PUBMED   21980299
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Gudbjartsson,D.F., Walters,G.B., Thorleifsson,G., Stefansson,H.,
            Halldorsson,B.V., Zusmanovich,P., Sulem,P., Thorlacius,S.,
            Gylfason,A., Steinberg,S., Helgadottir,A., Ingason,A.,
            Steinthorsdottir,V., Olafsdottir,E.J., Olafsdottir,G.H.,
            Jonsson,T., Borch-Johnsen,K., Hansen,T., Andersen,G., Jorgensen,T.,
            Pedersen,O., Aben,K.K., Witjes,J.A., Swinkels,D.W., den Heijer,M.,
            Franke,B., Verbeek,A.L., Becker,D.M., Yanek,L.R., Becker,L.C.,
            Tryggvadottir,L., Rafnar,T., Gulcher,J., Kiemeney,L.A., Kong,A.,
            Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Many sequence variants affecting diversity of adult human height
  JOURNAL   Nat Genet 40 (5), 609-615 (2008)
   PUBMED   18391951
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC013267.11, DA241650.1, AK095190.1, BC049384.1, AC012457.7 and
            AF131834.1.
            
            On or before Jun 20, 2008 this sequence version replaced
            XP_039733.7, XP_001717639.1, XP_945557.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2765685.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000403714.8/ ENSP00000384081.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..817
                     /product="protein EFR3 homolog B isoform 1"
                     /note="protein EFR3 homolog B"
                     /calculated_mol_wt=92356
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZQ18; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2G0.2)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZQ18; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2G0.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZQ18; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2G0.2)"
     CDS             1..817
                     /gene="EFR3B"
                     /gene_synonym="KIAA0953"
                     /coded_by="NM_014971.2:238..2691"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46231.1"
                     /db_xref="GeneID:22979"
                     /db_xref="HGNC:HGNC:29155"
                     /db_xref="MIM:616797"
ORIGIN      
        1 mygvcgccga lrprykrlvd nifpedpedg lvktnmeklt fyalsapekl drigaylser
       61 lirdvgrhry gyvciameal dqllmachcq sinlfvesfl kmvakllese kpnlqilgtn
      121 sfvkfaniee dtpsyhrsyd ffvsrfsemc hsshddleik tkirmsgikg lqgvvrktvn
      181 delqaniwdp qhmdkivpsl lfnlqhveea esrspsplqa pekekespae laerclrell
      241 graafgnikn aikpvlihld nhslwepkvf aircfkiimy siqpqhshlv iqqllghlda
      301 nsrsaatvra givevlseaa viaatgsvgp tvlemfntll rqlrlsidya ltgsydgavs
      361 lgtkiikehe ermfqeavik tvgsfastlp tyqrsevilf imskvprpsl hqavdtgrtg
      421 enrnrltqim llksllqvst gfqcnnmmsa lpsnfldrll stalmedaei rlfvleilis
      481 fidrhgnrhk fstistlsdi svlklkvdkc srqdtvfmkk hsqqlyrhiy lsckeetnvq
      541 khyealygll alisielane evvvdlirlv lavqdvaqvn eenlpvynrc alyalgaayl
      601 nlisqlttvp afcqhihevi etrkkeapym lpedvfverp rlsqnldgvv iellfrqski
      661 sevlggsgyn sdrlclpyip qltdedrlsk rrsigetisl qvevesrnsp ekeervpaee
      721 ityetlkkai vdsvaveeqe rerrrqvvek fqkapfeeia ahcgarasll qsklnqifei
      781 tirpppspsg titaaygqpq nhsipvyemk fpdlcvy
//
LOCUS       NP_996917                238 aa            linear   PRI 27-APR-2025
DEFINITION  endothelin-3 isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_996917
VERSION     NP_996917.1
DBSOURCE    REFSEQ: accession NM_207034.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wang,C.H., Tsuji,T., Wu,L.H., Yang,C.Y., Huang,T.L., Sato,M.,
            Shamsi,F. and Tseng,Y.H.
  TITLE     Endothelin 3/EDNRB signaling induces thermogenic differentiation of
            white adipose tissue
  JOURNAL   Nat Commun 15 (1), 7215 (2024)
   PUBMED   39174539
  REMARK    GeneRIF: Endothelin 3/EDNRB signaling induces thermogenic
            differentiation of white adipose tissue.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Zmarzly,N., Januszyk,S., Mieszczanski,P., Morawiec,E., Buda,P.,
            Dziobek,K., Oplawski,M. and Boron,D.
  TITLE     Endothelin-3 is epigenetically silenced in endometrioid endometrial
            cancer
  JOURNAL   J Cancer Res Clin Oncol 149 (9), 5687-5696 (2023)
   PUBMED   36542159
  REMARK    GeneRIF: Endothelin-3 is epigenetically silenced in endometrioid
            endometrial cancer.
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Chen,H., Cai,B., Liu,K. and Hua,Q.
  TITLE     miR-27a-3p regulates the inhibitory influence of endothelin 3 on
            the tumorigenesis of papillary thyroid cancer cells
  JOURNAL   Mol Med Rep 23 (4) (2021)
   PUBMED   33537832
  REMARK    GeneRIF: miR27a3p regulates the inhibitory influence of endothelin
            3 on the tumorigenesis of papillary thyroid cancer cells.
            Erratum:[Mol Med Rep. 2021 Jun;23(6):466. doi:
            10.3892/mmr.2021.12105. PMID: 33880586]
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Monti,L., Arrigucci,U. and Rossi,A.
  TITLE     Insights into Endothelin-3 and Multiple Sclerosis
  JOURNAL   Biomol Concepts 11 (1), 137-141 (2020)
   PUBMED   32589590
  REMARK    GeneRIF: Insights into Endothelin-3 and Multiple Sclerosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Lee,S., Lin,M., Mele,A., Cao,Y., Farmar,J., Russo,D. and Redman,C.
  TITLE     Proteolytic processing of big endothelin-3 by the kell blood group
            protein
  JOURNAL   Blood 94 (4), 1440-1450 (1999)
   PUBMED   10438732
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   7  (residues 1 to 238)
  AUTHORS   O'Reilly,G., Charnock-Jones,D.S., Davenport,A.P., Cameron,I.T. and
            Smith,S.K.
  TITLE     Presence of messenger ribonucleic acid for endothelin-1,
            endothelin-2, and endothelin-3 in human endometrium and a change in
            the ratio of ETA and ETB receptor subtype across the menstrual
            cycle
  JOURNAL   J Clin Endocrinol Metab 75 (6), 1545-1549 (1992)
   PUBMED   1464662
REFERENCE   8  (residues 1 to 238)
  AUTHORS   Mills,R.G., O'Donoghue,S.I., Smith,R. and King,G.F.
  TITLE     Solution structure of endothelin-3 determined using NMR
            spectroscopy
  JOURNAL   Biochemistry 31 (24), 5640-5645 (1992)
   PUBMED   1610811
REFERENCE   9  (residues 1 to 238)
  AUTHORS   Sakamoto,A., Yanagisawa,M., Sakurai,T., Takuwa,Y., Yanagisawa,H.
            and Masaki,T.
  TITLE     Cloning and functional expression of human cDNA for the ETB
            endothelin receptor
  JOURNAL   Biochem Biophys Res Commun 178 (2), 656-663 (1991)
   PUBMED   1713452
REFERENCE   10 (residues 1 to 238)
  AUTHORS   Bloch,K.D., Eddy,R.L., Shows,T.B. and Quertermous,T.
  TITLE     cDNA cloning and chromosomal assignment of the gene encoding
            endothelin 3
  JOURNAL   J Biol Chem 264 (30), 18156-18161 (1989)
   PUBMED   2509452
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC008876.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            endothelin family. Endothelins are endothelium-derived vasoactive
            peptides involved in a variety of biological functions. The active
            form of this protein is a 21 amino acid peptide processed from the
            precursor protein. The active peptide is a ligand for endothelin
            receptor type B (EDNRB). The interaction of this endothelin with
            EDNRB is essential for development of neural crest-derived cell
            lineages, such as melanocytes and enteric neurons. Mutations in
            this gene and EDNRB have been associated with Hirschsprung disease
            (HSCR) and Waardenburg syndrome (WS), which are congenital
            disorders involving neural crest-derived cells. Altered expression
            of this gene is implicated in tumorigenesis. Alternative splicing
            results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Oct 2014].
            
            Transcript Variant: This variant (4) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008876.2, SRR1803617.253442.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337938.7/ ENSP00000337128.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..238
                     /product="endothelin-3 isoform 1 preproprotein"
                     /note="preproendothelin-3"
                     /calculated_mol_wt=23738
     sig_peptide     1..16
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14138.1)"
                     /calculated_mol_wt=1735
     Region          24..89
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14138.1)"
     Region          <24..>87
                     /region_name="PHA03418"
                     /note="hypothetical E4 protein; Provisional"
                     /db_xref="CDD:177646"
     Region          93..121
                     /region_name="Endothelin"
                     /note="Endothelin family; cl27714"
                     /db_xref="CDD:452774"
     mat_peptide     97..117
                     /product="Endothelin-3. /id=PRO_0000008112"
                     /note="propagated from UniProtKB/Swiss-Prot (P14138.1)"
                     /calculated_mol_wt=2647
     Site            117..118
                     /site_type="cleavage"
                     /note="Cleavage, by KEL; propagated from
                     UniProtKB/Swiss-Prot (P14138.1)"
     Region          158..179
                     /region_name="END"
                     /note="Endothelin; smart00272"
                     /db_xref="CDD:197618"
     Region          159..173
                     /region_name="Endothelin-like"
                     /note="propagated from UniProtKB/Swiss-Prot (P14138.1)"
     Region          183..219
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14138.1)"
     CDS             1..238
                     /gene="EDN3"
                     /gene_synonym="ET-3; ET3; HSCR4; PPET3; WS4B"
                     /coded_by="NM_207034.3:203..919"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS13477.1"
                     /db_xref="GeneID:1908"
                     /db_xref="HGNC:HGNC:3178"
                     /db_xref="MIM:131242"
ORIGIN      
        1 mepglwllfg ltvtsaagfv pcsqsgdagr rgvsqaptaa rsegdceetv agpgeetvag
       61 pgegtvapta lqgpspgspg qeqaaegape hhrsrrctcf tykdkecvyy chldiiwint
      121 peqtvpygls nyrgsfrgkr sagplpgnlq lshrphlrca cvgrydkacl hfctqtldvs
      181 snsrtaektd keeegkvevk dqqskqaldl hhpklmpgsg lalapstcpr clfqegap
//
LOCUS       NP_003769                344 aa            linear   PRI 27-APR-2025
DEFINITION  beta-1,4-galactosyltransferase 4 [Homo sapiens].
ACCESSION   NP_003769
VERSION     NP_003769.1
DBSOURCE    REFSEQ: accession NM_003778.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Dai,Z., Wang,K. and Gao,Y.
  TITLE     The critical role of B4GALT4 in promoting microtubule spindle
            assembly in HCC through the regulation of PLK1 and RHAMM expression
  JOURNAL   J Cell Physiol 237 (1), 617-636 (2022)
   PUBMED   34270095
  REMARK    GeneRIF: The critical role of B4GALT4 in promoting microtubule
            spindle assembly in HCC through the regulation of PLK1 and RHAMM
            expression.
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Shauchuk,A., Szulc,B., Maszczak-Seneczko,D., Wiertelak,W.,
            Skurska,E. and Olczak,M.
  TITLE     N-glycosylation of the human beta1,4-galactosyltransferase 4 is
            crucial for its activity and Golgi localization
  JOURNAL   Glycoconj J 37 (5), 577-588 (2020)
   PUBMED   32827291
  REMARK    GeneRIF: N-glycosylation of the human beta1,4-galactosyltransferase
            4 is crucial for its activity and Golgi localization.
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Sugiyama,A., Fukushima,N. and Sato,T.
  TITLE     Transcriptional Mechanism of the beta4-Galactosyltransferase 4 Gene
            in SW480 Human Colon Cancer Cell Line
  JOURNAL   Biol Pharm Bull 40 (5), 733-737 (2017)
   PUBMED   28228616
  REMARK    GeneRIF: expression of the beta4GalT4 gene is controlled by Sp1,
            and Sp1 plays a key role in the activation of the beta4GalT4 gene
            in colon cancer cells.
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Kitayama,K., Hayashida,Y., Nishida,K. and Akama,T.O.
  TITLE     Enzymes responsible for synthesis of corneal keratan sulfate
            glycosaminoglycans
  JOURNAL   J Biol Chem 282 (41), 30085-30096 (2007)
   PUBMED   17690104
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Guo,S., Sato,T., Shirane,K. and Furukawa,K.
  TITLE     Galactosylation of N-linked oligosaccharides by human
            beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed
            in Sf-9 cells
  JOURNAL   Glycobiology 11 (10), 813-820 (2001)
   PUBMED   11588157
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Suzuki,Y., Tsunoda,T., Sese,J., Taira,H., Mizushima-Sugano,J.,
            Hata,H., Ota,T., Isogai,T., Tanaka,T., Nakamura,Y., Suyama,A.,
            Sakaki,Y., Morishita,S., Okubo,K. and Sugano,S.
  TITLE     Identification and characterization of the potential promoter
            regions of 1031 kinds of human genes
  JOURNAL   Genome Res 11 (5), 677-684 (2001)
   PUBMED   11337467
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Amado,M., Almeida,R., Schwientek,T. and Clausen,H.
  TITLE     Identification and characterization of large galactosyltransferase
            gene families: galactosyltransferases for all functions
  JOURNAL   Biochim Biophys Acta 1473 (1), 35-53 (1999)
   PUBMED   10580128
  REMARK    Review article
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Fan,Y., Yu,L., Zhang,Q., Jiang,Y., Dai,F., Chen,C., Tu,Q., Bi,A.,
            Xu,Y. and Zhao,S.
  TITLE     Cloning and characterization of a novel member of human
            beta-1,4-galactosyltransferase gene family
  JOURNAL   Sci China C Life Sci 42 (4), 337-345 (1999)
   PUBMED   18763123
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Schwientek,T., Almeida,R., Levery,S.B., Holmes,E.H., Bennett,E. and
            Clausen,H.
  TITLE     Cloning of a novel member of the
            UDP-galactose:beta-N-acetylglucosamine
            beta1,4-galactosyltransferase family, beta4Gal-T4, involved in
            glycosphingolipid biosynthesis
  JOURNAL   J Biol Chem 273 (45), 29331-29340 (1998)
   PUBMED   9792633
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Lo,N.W., Shaper,J.H., Pevsner,J. and Shaper,N.L.
  TITLE     The expanding beta 4-galactosyltransferase gene family: messages
            from the databanks
  JOURNAL   Glycobiology 8 (5), 517-526 (1998)
   PUBMED   9597550
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX647468.1, AF038662.1,
            AK123182.1 and AK001006.1.
            
            Summary: This gene is one of seven beta-1,4-galactosyltransferase
            (beta4GalT) genes. They encode type II membrane-bound glycoproteins
            that appear to have exclusive specificity for the donor substrate
            UDP-galactose; all transfer galactose in a beta1,4 linkage to
            similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a
            distinct function in the biosynthesis of different glycoconjugates
            and saccharide structures. As type II membrane proteins, they have
            an N-terminal hydrophobic signal sequence that directs the protein
            to the Golgi apparatus and which then remains uncleaved to function
            as a transmembrane anchor. By sequence similarity, the beta4GalTs
            form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and
            beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. The enzyme
            encoded by this gene appears to mainly play a role in glycolipid
            biosynthesis. Two alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an exon in the 5' UTR,
            as compared to variant 1. Both variants 1 and 2 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749555.1, SRR5189661.185202.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393765.7/ ENSP00000377360.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.32"
     Protein         1..344
                     /product="beta-1,4-galactosyltransferase 4"
                     /EC_number="2.4.1.90"
                     /EC_number="2.4.1.275"
                     /note="beta-N-acetylglucosaminyl-glycolipid
                     beta-1,4-galactosyltransferase 4; UDP-Gal:betaGlcNAc beta
                     1,4- galactosyltransferase 4; beta-1,4-GalTase 4;
                     UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 4;
                     UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 4; nal synthase;
                     UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,
                     polypeptide 4; N-acetyllactosamine synthase;
                     lactotriaosylceramide beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=39910
     Site            13..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60513.1)"
     Region          122..339
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(129,131,133,168,194..196)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            order(194,196,289)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:32827291; propagated from
                     UniProtKB/Swiss-Prot (O60513.1)"
     Site            335
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:32827291; propagated from
                     UniProtKB/Swiss-Prot (O60513.1)"
     CDS             1..344
                     /gene="B4GALT4"
                     /gene_synonym="B4Gal-T4; beta4Gal-T4"
                     /coded_by="NM_003778.4:393..1427"
                     /db_xref="CCDS:CCDS2986.1"
                     /db_xref="GeneID:8702"
                     /db_xref="HGNC:HGNC:927"
                     /db_xref="MIM:604015"
ORIGIN      
        1 mgfnltfhls ykfrlllllt lcltvvgwat snyfvgaiqe ipkakefman fhktlilgkg
       61 ktltneastk kveldncpsv spylrgqskl ifkpdltlee vqaenpkvsr gryrpqecka
      121 lqrvailvph rnrekhlmyl lehlhpflqr qqldygiyvi hqaegkkfnr akllnvgyle
      181 alkeenwdcf ifhdvdlvpe ndfnlykcee hpkhlvvgrn stgyrlrysg yfggvtalsr
      241 eqffkvngfs nnywgwgged ddlrlrvelq rmkisrplpe vgkytmvfht rdkgnevnae
      301 rmkllhqvsr vwrtdglssc syklvsvehn plyinitvdf wfga
//
LOCUS       NP_001351634             225 aa            linear   ROD 27-APR-2025
DEFINITION  storkhead-box protein 1 isoform 2 [Mus musculus].
ACCESSION   NP_001351634
VERSION     NP_001351634.1
DBSOURCE    REFSEQ: accession NM_001364705.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Parchem,J.G., Kanasaki,K., Lee,S.B., Kanasaki,M., Yang,J.L., Xu,Y.,
            Earl,K.M., Keuls,R.A., Gattone,V.H. 2nd and Kalluri,R.
  TITLE     STOX1 deficiency is associated with renin-mediated gestational
            hypertension and placental defects
  JOURNAL   JCI Insight 6 (2), 141588 (2021)
   PUBMED   33301424
  REMARK    GeneRIF: STOX1 deficiency is associated with renin-mediated
            gestational hypertension and placental defects.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Miralles,F., Collinot,H., Boumerdassi,Y., Ducat,A., Duche,A.,
            Renault,G., Marchiol,C., Lagoutte,I., Bertholle,C., Andrieu,M.,
            Jacques,S., Mehats,C. and Vaiman,D.
  TITLE     Long-term cardiovascular disorders in the STOX1 mouse model of
            preeclampsia
  JOURNAL   Sci Rep 9 (1), 11918 (2019)
   PUBMED   31417152
  REMARK    GeneRIF: Long-term cardiovascular disorders in the STOX1 mouse
            model of preeclampsia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Erlandsson,L., Ducat,A., Castille,J., Zia,I., Kalapotharakos,G.,
            Hedstrom,E., Vilotte,J.L., Vaiman,D. and Hansson,S.R.
  TITLE     Alpha-1 microglobulin as a potential therapeutic candidate for
            treatment of hypertension and oxidative stress in the STOX1
            preeclampsia mouse model
  JOURNAL   Sci Rep 9 (1), 8561 (2019)
   PUBMED   31189914
  REMARK    GeneRIF: Alpha-1 microglobulin as a potential therapeutic candidate
            for treatment of hypertension and oxidative stress in the STOX1
            preeclampsia mouse model.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Collinot,H., Marchiol,C., Lagoutte,I., Lager,F., Siauve,N.,
            Autret,G., Balvay,D., Renault,G., Salomon,L.J. and Vaiman,D.
  TITLE     Preeclampsia induced by STOX1 overexpression in mice induces
            intrauterine growth restriction, abnormal ultrasonography and BOLD
            MRI signatures
  JOURNAL   J Hypertens 36 (6), 1399-1406 (2018)
   PUBMED   29465714
  REMARK    GeneRIF: Studied association of overexpression of storkhead box 1
            (STOX1) protein, preeclampsia, intrauterine growth restriction and
            fetal imaging pathology in mice.
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Zhang,C., Ji,Z., Wang,M., Zhang,W., Yang,R., An,H., Yang,R., van
            Abel,D., van Dijk,M., Yang,X., Ou,G., Zhu,H.H. and Gao,W.Q.
  TITLE     Stox1 as a novel transcriptional suppressor of Math1 during
            cerebellar granule neurogenesis and medulloblastoma formation
  JOURNAL   Cell Death Differ 23 (12), 2042-2053 (2016)
   PUBMED   27564589
  REMARK    GeneRIF: This study illustrates a SHH-Stox1-Math1 regulatory axis
            in normal cerebellar development and medulloblastoma formation.
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Nie,X., Zhang,K., Wang,L., Ou,G., Zhu,H. and Gao,W.Q.
  TITLE     Transcription factor STOX1 regulates proliferation of inner ear
            epithelial cells via the AKT pathway
  JOURNAL   Cell Prolif 48 (2), 209-220 (2015)
   PUBMED   25677106
  REMARK    GeneRIF: STOX1 is a novel stimulatory factor for inner ear
            epithelial cell proliferation and might be an important target to
            be considered in regeneration or repair of inner ear epithelium.
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Lui,J.H., Nowakowski,T.J., Pollen,A.A., Javaherian,A.,
            Kriegstein,A.R. and Oldham,M.C.
  TITLE     Radial glia require PDGFD-PDGFRbeta signalling in human but not
            mouse neocortex
  JOURNAL   Nature 515 (7526), 264-268 (2014)
   PUBMED   25391964
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Doridot,L., Chatre,L., Ducat,A., Vilotte,J.L., Lombes,A.,
            Mehats,C., Barbaux,S., Calicchio,R., Ricchetti,M. and Vaiman,D.
  TITLE     Nitroso-redox balance and mitochondrial homeostasis are regulated
            by STOX1, a pre-eclampsia-associated gene
  JOURNAL   Antioxid Redox Signal 21 (6), 819-834 (2014)
   PUBMED   24738702
  REMARK    GeneRIF: Our data posit STOX1 as a genetic switch in the ROS/RNS
            balance and suggest an explanation for elevated blood pressure in
            pre-eclampsia.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC137978.1, BE988760.1, AK133671.1 and AI842662.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7345562.3218950.1, BE988760.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 32.45 cM"
     Protein         1..225
                     /product="storkhead-box protein 1 isoform 2"
                     /note="storkhead-box protein 1"
                     /calculated_mol_wt=24462
     Region          108..186
                     /region_name="Stork_head"
                     /note="Winged helix Storkhead-box1 domain; pfam10264"
                     /db_xref="CDD:431182"
     CDS             1..225
                     /gene="Stox1"
                     /gene_synonym="4732470K04Rik; Gm63"
                     /coded_by="NM_001364705.1:27..704"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:216021"
                     /db_xref="MGI:MGI:2684909"
ORIGIN      
        1 marpvqlapg slalvlspre agqaagepgg ralfrafrra narcfwnarl araasrlafl
       61 gwlrrgvllv rapqpcvqvl rdawrrralr pprgfritav gdvfpvqmsp iaqcrfvpla
      121 evlccaiadm naaqvmvtqq sllehlikhy pgiavpspdi lystlgaliq erkiyhtgeg
      181 yfivtpstyf itntpmqgnk sallsnegcs gptsgtylda epgiy
//
LOCUS       NP_000772                521 aa            linear   PRI 27-APR-2025
DEFINITION  cholesterol side-chain cleavage enzyme, mitochondrial isoform a
            precursor [Homo sapiens].
ACCESSION   NP_000772
VERSION     NP_000772.2
DBSOURCE    REFSEQ: accession NM_000781.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Zhang,Z., Huang,H., Chen,Z., Yan,M., Lu,C., Xu,Z. and Li,Z.
  TITLE     Helicobacter pylori promotes gastric cancer through CagA-mediated
            mitochondrial cholesterol accumulation by targeting CYP11A1
            redistribution
  JOURNAL   Int J Biol Sci 20 (10), 4007-4028 (2024)
   PUBMED   39113698
  REMARK    GeneRIF: Helicobacter pylori promotes gastric cancer through
            CagA-mediated mitochondrial cholesterol accumulation by targeting
            CYP11A1 redistribution.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   McCarty,K.D., Liu,L., Tateishi,Y., Wapshott-Stehli,H.L. and
            Guengerich,F.P.
  TITLE     The multistep oxidation of cholesterol to pregnenolone by human
            cytochrome P450 11A1 is highly processive
  JOURNAL   J Biol Chem 300 (1), 105495 (2024)
   PUBMED   38006947
  REMARK    GeneRIF: The multistep oxidation of cholesterol to pregnenolone by
            human cytochrome P450 11A1 is highly processive.
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Zhu,Y.N., Pan,F., Gan,X.W., Liu,Y., Wang,W.S. and Sun,K.
  TITLE     The Role of DNMT1 and C/EBPalpha in the Regulation of CYP11A1
            Expression During Syncytialization of Human Placental Trophoblasts
  JOURNAL   Endocrinology 165 (2) (2023)
   PUBMED   38146648
  REMARK    GeneRIF: The Role of DNMT1 and C/EBPalpha in the Regulation of
            CYP11A1 Expression During Syncytialization of Human Placental
            Trophoblasts.
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Shi,D., Zhou,X., Cai,L., Wei,X., Zhang,L., Sun,Q., Zhou,F. and
            Sun,L.
  TITLE     Placental DNA methylation analysis of selective fetal growth
            restriction in monochorionic twins reveals aberrant methylated
            CYP11A1 gene for fetal growth restriction
  JOURNAL   FASEB J 37 (10), e23207 (2023)
   PUBMED   37732623
  REMARK    GeneRIF: Placental DNA methylation analysis of selective fetal
            growth restriction in monochorionic twins reveals aberrant
            methylated CYP11A1 gene for fetal growth restriction.
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Redouane,S., Harmak,H., Elkarhat,Z., Charoute,H., Malki,A.,
            Barakat,A. and Rouba,H.
  TITLE     Exploring the impact of CYP11A1's missense SNPs on the interaction
            between CYP11A1 and cholesterol: A comprehensive structural
            analysis and MD simulation study
  JOURNAL   Comput Biol Chem 106, 107937 (2023)
   PUBMED   37552904
  REMARK    GeneRIF: Exploring the impact of CYP11A1's missense SNPs on the
            interaction between CYP11A1 and cholesterol: A comprehensive
            structural analysis and MD simulation study.
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Wada,A. and Waterman,M.R.
  TITLE     Identification by site-directed mutagenesis of two lysine residues
            in cholesterol side chain cleavage cytochrome P450 that are
            essential for adrenodoxin binding
  JOURNAL   J Biol Chem 267 (32), 22877-22882 (1992)
   PUBMED   1429635
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Coghlan,V.M. and Vickery,L.E.
  TITLE     Site-specific mutations in human ferredoxin that affect binding to
            ferredoxin reductase and cytochrome P450scc
  JOURNAL   J Biol Chem 266 (28), 18606-18612 (1991)
   PUBMED   1917982
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Sparkes,R.S., Klisak,I. and Miller,W.L.
  TITLE     Regional mapping of genes encoding human steroidogenic enzymes:
            P450scc to 15q23-q24, adrenodoxin to 11q22; adrenodoxin reductase
            to 17q24-q25; and P450c17 to 10q24-q25
  JOURNAL   DNA Cell Biol 10 (5), 359-365 (1991)
   PUBMED   1863359
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Hu,M.C., Guo,I.C., Lin,J.H. and Chung,B.C.
  TITLE     Regulated expression of cytochrome P-450scc (cholesterol-side-chain
            cleavage enzyme) in cultured cell lines detected by antibody
            against bacterially expressed human protein
  JOURNAL   Biochem J 274 (Pt 3) (Pt 3), 813-817 (1991)
   PUBMED   1849407
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX398579.2, BC032329.1 and
            AI149078.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 24, 2007 this sequence version replaced NP_000772.1.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This protein localizes to the mitochondrial inner membrane and
            catalyzes the conversion of cholesterol to pregnenolone, the first
            and rate-limiting step in the synthesis of the steroid hormones.
            Two transcript variants encoding different isoforms have been found
            for this gene. The cellular location of the smaller isoform is
            unclear since it lacks the mitochondrial-targeting transit peptide.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292300.1, SRR5189667.171723.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162841, SAMN03267755
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000268053.11/
                                                  ENSP00000268053.6
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..521
                     /product="cholesterol side-chain cleavage enzyme,
                     mitochondrial isoform a precursor"
                     /EC_number="1.14.15.6"
                     /note="cholesterol 20-22 desmolase; cholesterol
                     monooxygenase (side-chain cleaving); steroid 20-22-lyase;
                     cytochrome P450, subfamily XIA (cholesterol side chain
                     cleavage); cholesterol side-chain cleavage enzyme,
                     mitochondrial; cytochrome P450 11A1; cytochrome P450(scc);
                     cytochrome P450 family 11 subfamily A polypeptide 1"
                     /calculated_mol_wt=56100
     transit_peptide 1..39
                     /calculated_mol_wt=4021
     mat_peptide     40..521
                     /product="cholesterol side-chain cleavage enzyme,
                     mitochondrial isoform a"
                     /calculated_mol_wt=56100
     Region          82..508
                     /region_name="CYP11A1"
                     /note="cytochrome P450 family 11, subfamily A, polypeptide
                     1, also called cholesterol side-chain cleavage enzyme;
                     cd20643"
                     /db_xref="CDD:410736"
     Site            order(120..121,123,140,240..241,322,325..326,330,390..393,
                     395,497,499..500)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410736"
     Site            order(120,139..140,147,151,323,326..327,330,334,385,
                     390..391,394,396,454..457,460..464,468,472)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410736"
     Site            462
                     /site_type="binding"
                     /note="heme binding site"
     CDS             1..521
                     /gene="CYP11A1"
                     /gene_synonym="CYP11A; CYPXIA1; P450SCC"
                     /coded_by="NM_000781.3:62..1627"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS32291.1"
                     /db_xref="GeneID:1583"
                     /db_xref="HGNC:HGNC:2590"
                     /db_xref="MIM:118485"
ORIGIN      
        1 mlakglpprs vlvkgcqtfl sapreglgrl rvptgegagi strsprpfne ipspgdngwl
       61 nlyhfwretg thkvhlhhvq nfqkygpiyr eklgnvesvy vidpedvall fksegpnper
      121 flippwvayh qyyqrpigvl lkksaawkkd rvalnqevma peatknflpl ldavsrdfvs
      181 vlhrrikkag sgnysgdisd dlfrfafesi tnvifgerqg mleevvnpea qrfidaiyqm
      241 fhtsvpmlnl ppdlfrlfrt ktwkdhvaaw dvifskadiy tqnfywelrq kgsvhhdyrg
      301 ilyrllgdsk msfedikanv temlaggvdt tsmtlqwhly emarnlkvqd mlraevlaar
      361 hqaqgdmatm lqlvpllkas iketlrlhpi svtlqrylvn dlvlrdymip aktlvqvaiy
      421 algreptfff dpenfdptrw lskdknityf rnlgfgwgvr qclgrriael emtiflinml
      481 enfrveiqhl sdvgttfnli lmpekpisft fwpfnqeatq q
//
LOCUS       NP_001352155             375 aa            linear   PRI 27-APR-2025
DEFINITION  ADP-dependent glucokinase isoform 5 [Homo sapiens].
ACCESSION   NP_001352155 XP_006720776
VERSION     NP_001352155.1
DBSOURCE    REFSEQ: accession NM_001365226.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Herrera-Morande,A., Vallejos-Baccelliere,G., Cea,P.A., Zamora,R.A.,
            Cid,D., Maturana,P., Gonzalez-Ordenes,F., Castro-Fernandez,V. and
            Guixe,V.
  TITLE     Kinetic characterization and phylogenetic analysis of human
            ADP-dependent glucokinase reveal new insights into its regulatory
            properties
  JOURNAL   Arch Biochem Biophys 741, 109602 (2023)
   PUBMED   37084804
  REMARK    GeneRIF: Kinetic characterization and phylogenetic analysis of
            human ADP-dependent glucokinase reveal new insights into its
            regulatory properties.
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tandon,A., Birkenhagen,J., Nagalla,D., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase as a novel onco-target for haematological
            malignancies
  JOURNAL   Sci Rep 10 (1), 13584 (2020)
   PUBMED   32788680
  REMARK    GeneRIF: ADP-dependent glucokinase as a novel onco-target for
            haematological malignancies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Jiang,H.Y. and Wang,Z.J.
  TITLE     ADPGK-AS1 promotes the progression of colorectal cancer via
            sponging miR-525 to upregulate FUT1
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2380-2386 (2020)
   PUBMED   32196589
  REMARK    GeneRIF: ADPGK-AS1 promotes the progression of colorectal cancer
            via sponging miR-525 to upregulate FUT1.
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Imle,R., Wang,B.T., Stutzenberger,N., Birkenhagen,J., Tandon,A.,
            Carl,M., Himmelreich,N., Thiel,C., Grone,H.J., Poschet,G.,
            Volkers,M., Gulow,K., Schroder,A., Carillo,S., Mittermayr,S.,
            Bones,J., Kaminski,M.M., Kolker,S. and Sauer,S.W.
  TITLE     ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing
  JOURNAL   Sci Rep 9 (1), 14248 (2019)
   PUBMED   31582762
  REMARK    GeneRIF: ADP-dependent glucokinase regulates energy metabolism via
            ER-localized glucose sensing.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Richter,J.P., Goroncy,A.K., Ronimus,R.S. and Sutherland-Smith,A.J.
  TITLE     The Structural and Functional Characterization of Mammalian
            ADP-dependent Glucokinase
  JOURNAL   J Biol Chem 291 (8), 3694-3704 (2016)
   PUBMED   26555263
  REMARK    GeneRIF: ADPGK is substrate inhibited by high glucose concentration
            and shows high specificity for glucose, with no activity for other
            sugars, as determined by NMR spectroscopy, including 2-deoxyglucose
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Cuesta-Munoz,A.L., Tuomi,T., Cobo-Vuilleumier,N., Koskela,H.,
            Odili,S., Stride,A., Buettger,C., Otonkoski,T., Froguel,P.,
            Grimsby,J., Garcia-Gimeno,M. and Matschinsky,F.M.
  TITLE     Clinical heterogeneity in monogenic diabetes caused by mutations in
            the glucokinase gene (GCK-MODY)
  JOURNAL   Diabetes Care 33 (2), 290-292 (2010)
   PUBMED   19903754
  REMARK    GeneRIF: Glucose and insulin response to oral glucose is higher in
            GCK(261) carriers, indicating clinical heterogeneity in GCK
            maturity diabetes carriers.
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Codner,E., Rocha,A., Deng,L., Martinez-Aguayo,A., Godoy,C.,
            Mericq,V. and Chung,W.K.
  TITLE     Mild fasting hyperglycemia in children: high rate of glucokinase
            mutations and some risk of developing type 1 diabetes mellitus
  JOURNAL   Pediatr Diabetes 10 (6), 382-388 (2009)
   PUBMED   19309449
  REMARK    GeneRIF: The presence of mild persistent hyperglycemia in any
            patient without autoantibodies should lead to genetic analysis of
            glucokinase, particularly if there is a positive family history.
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Ronimus,R.S. and Morgan,H.W.
  TITLE     Cloning and biochemical characterization of a novel mouse
            ADP-dependent glucokinase
  JOURNAL   Biochem Biophys Res Commun 315 (3), 652-658 (2004)
   PUBMED   14975750
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009712.22.
            
            On Aug 9, 2018 this sequence version replaced XP_006720776.1.
            
            Summary: ADPGK (EC 2.7.1.147) catalyzes the ADP-dependent
            phosphorylation of glucose to glucose-6-phosphate and may play a
            role in glycolysis, possibly during ischemic conditions (Ronimus
            and Morgan, 2004 [PubMed 14975750]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.52303.1,
                                           SRR1803611.245272.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..375
                     /product="ADP-dependent glucokinase isoform 5"
                     /EC_number="2.7.1.147"
                     /note="ATP-dependent glucokinase; rbBP-35"
                     /calculated_mol_wt=41028
     Region          1..370
                     /region_name="ADPGK_ADPPFK"
                     /note="ADP-dependent glucokinase (ADPGK) and
                     phosphofructokinase (ADPPFK). ADPGK and ADPPFK are
                     proteins that rely on ADP rather than ATP to donate a
                     phosphoryl group. They are found in certain
                     hyperthermophilic archaea and in higher eukaryotes. A
                     functional...; cd01938"
                     /db_xref="CDD:238913"
     Site            order(37,175,203,206,359)
                     /site_type="other"
                     /note="Mg2+ binding site [ion binding]"
                     /db_xref="CDD:238913"
     Site            order(203,260..261,346,348,351,357..358,361)
                     /site_type="other"
                     /note="ADP binding site [chemical binding]"
                     /db_xref="CDD:238913"
     CDS             1..375
                     /gene="ADPGK"
                     /gene_synonym="2610017G09Rik; ADP-GK"
                     /coded_by="NM_001365226.1:647..1774"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:83440"
                     /db_xref="HGNC:HGNC:25250"
                     /db_xref="MIM:611861"
ORIGIN      
        1 mgkgaaaerf fsdketfhdi aqvasefpga qhyvggnaal igqkfaansd lkvllcgpvg
       61 pklhellddn vfvppeslqe vdefhliley qageewgqlk aphanrfifs hdlsngamnm
      121 levfvsslee fqpdlvvlsg lhmmegqske lqrkrllevv tsisdiptgi pvhlelasmt
      181 nrelmssivh qqvfpavtsl glneqellfl tqsasgphss lsswngvpdv gmvsdilfwi
      241 lkehgrsksr asdltrihfh tlvyhilatv dghwanqlaa vaagarvagt qacatetidt
      301 srvslrapqe fmtshseags rivlnpnkpv vewhregisf hftpvlvckd pirtvglgda
      361 isaeglfyse vhphy
//
LOCUS       NP_919447                859 aa            linear   MAM 27-APR-2025
DEFINITION  inositol 1,4,5-triphosphate receptor associated 1 isoform b [Bos
            taurus].
ACCESSION   NP_919447 XP_613836
VERSION     NP_919447.2
DBSOURCE    REFSEQ: accession NM_194465.4
KEYWORDS    RefSeq.
SOURCE      Bos taurus (domestic cattle)
  ORGANISM  Bos taurus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia;
            Pecora; Bovidae; Bovinae; Bos.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Desch,M., Sigl,K., Hieke,B., Salb,K., Kees,F., Bernhard,D.,
            Jochim,A., Spiessberger,B., Hocherl,K., Feil,R., Feil,S.,
            Lukowski,R., Wegener,J.W., Hofmann,F. and Schlossmann,J.
  TITLE     IRAG determines nitric oxide- and atrial natriuretic
            peptide-mediated smooth muscle relaxation
  JOURNAL   Cardiovasc Res 86 (3), 496-505 (2010)
   PUBMED   20080989
  REMARK    GeneRIF: cGKIbeta signaling via IRAG is essential for regulation of
            smooth muscle tone and of intracellular calcium by NO and by atrial
            natriuretic peptide.
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Zimin,A.V., Delcher,A.L., Florea,L., Kelley,D.R., Schatz,M.C.,
            Puiu,D., Hanrahan,F., Pertea,G., Van Tassell,C.P., Sonstegard,T.S.,
            Marcais,G., Roberts,M., Subramanian,P., Yorke,J.A. and
            Salzberg,S.L.
  TITLE     A whole-genome assembly of the domestic cow, Bos taurus
  JOURNAL   Genome Biol 10 (4), R42 (2009)
   PUBMED   19393038
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Casteel,D.E., Boss,G.R. and Pilz,R.B.
  TITLE     Identification of the interface between cGMP-dependent protein
            kinase Ibeta and its interaction partners TFII-I and IRAG reveals a
            common interaction motif
  JOURNAL   J Biol Chem 280 (46), 38211-38218 (2005)
   PUBMED   16166082
  REMARK    GeneRIF: cGMP-dependent protein kinase Ibeta binds to TFII-I and
            IRAG through a common interaction motif
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Schlossmann,J., Ammendola,A., Ashman,K., Zong,X., Huber,A.,
            Neubauer,G., Wang,G.X., Allescher,H.D., Korth,M., Wilm,M.,
            Hofmann,F. and Ruth,P.
  TITLE     Regulation of intracellular calcium by a signalling complex of
            IRAG, IP3 receptor and cGMP kinase Ibeta
  JOURNAL   Nature 404 (6774), 197-201 (2000)
   PUBMED   10724174
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            NKLS02000015.1.
            
            On Aug 8, 2007 this sequence version replaced NP_919447.1.
            
            Transcript Variant: This variant (2) uses an alternate 5' end exon
            compared to transcript variant 1, resulting in translation
            initiation from an in-frame, downstream AUG, and an isoform (b)
            with a shorter N-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF195527.1, SRR5765710.1592.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA6648759, SAMN03145415
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Bos taurus"
                     /db_xref="taxon:9913"
                     /chromosome="15"
                     /map="15"
                     /breed="Hereford"
     Protein         1..859
                     /product="inositol 1,4,5-triphosphate receptor associated
                     1 isoform b"
                     /note="IP3 receptor associated cGMP kinase substrate;
                     JAW1-related protein MRVI1; inositol 1,4,5-triphosphate
                     receptor-associated cGMP kinase substrate; murine
                     retrovirus integration site 1 homolog; inositol
                     1,4,5-trisphosphate receptor-associated cGMP kinase
                     substrate"
                     /calculated_mol_wt=92987
     Region          273..859
                     /region_name="MRVI1"
                     /note="MRVI1 protein; pfam05781"
                     /db_xref="CDD:461738"
     CDS             1..859
                     /gene="IRAG1"
                     /gene_synonym="IRAG; MRVI1"
                     /coded_by="NM_194465.4:156..2735"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="BGD:BT14004"
                     /db_xref="GeneID:281918"
ORIGIN      
        1 mphipedeep pgepqaaqsp agqdpattgi scspptiilt gdasspeget dknpvnrahs
       61 phrrlshrhl kvstasltsv dpaghvidlv ndqlpdisis eedkkknlal leeaklvser
      121 fltrrgrksr sspgesspav spnlspgasp assqsnsltv ptppgldvcs gppsplpgap
      181 pqkgdeaevp sphlgesnvl kgladrkqnd qrtlsqgrlt arsptveksk eitiehkenf
      241 dplqrpeaip kgpasgpgsg gkmalnspqp gpveselgkp laktakegnp lprgptqgsg
      301 gvapqasqgk stvgepagsk vgskaelwpp tsrppllrgv swdsgpeepg prlqkvlakl
      361 plaeeekrft gkagsklaka pglkdfqiqv qpvrmqkltk lreehillrn qnlvglklpe
      421 lseaaeqekg hpselssaie eeeskggldv mpnisdvllr klrvhkslpg sappltekev
      481 envfvqlsla frndsytles rinqaerern lteentekel enfkasitss aslwhhcehr
      541 etyqklledi avlhrlaarl ssraemvgav rqekrmskat evmmqyvenl krtyekdhae
      601 lmefkklanq nssrscgpse dgvprtarsm slslgknmpr rrvsvavvpk fnilnlpgqs
      661 pssspipslp alsessngkg nppvssalpa llengktngd pdceasasvp tpsclegisq
      721 eakarmeeea ynkgyqeglk ktkelqglre eeeeqksesp eepeeaaete eeekeqrssk
      781 leelvhflqv mypklcqhwq viwmmaaaml vltvvlglyg shnscveqad gslgkstcsa
      841 aqrdswwssg lqheqpteq
//
LOCUS       NP_001356314             386 aa            linear   PRI 27-APR-2025
DEFINITION  nucleosome assembly protein 1-like 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001356314
VERSION     NP_001356314.1
DBSOURCE    REFSEQ: accession NM_001369385.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Tan,L., Cheng,W., Liu,F., Wang,D.O., Wu,L., Cao,N. and Wang,J.
  TITLE     Positive natural selection of N6-methyladenosine on the RNAs of
            processed pseudogenes
  JOURNAL   Genome Biol 22 (1), 180 (2021)
   PUBMED   34120636
  REMARK    GeneRIF: Positive natural selection of N6-methyladenosine on the
            RNAs of processed pseudogenes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Mizuhashi,S., Fukushima,S., Ishibashi,T., Kuriyama,H., Kimura,T.,
            Kanemaru,H., Kajihara,I., Makino,K., Miyashita,A., Aoi,J., Kita,K.
            and Ihn,H.
  TITLE     Nucleosome assembly protein 1-like 4, a new therapeutic target for
            proliferation and invasion of melanoma cells
  JOURNAL   J Dermatol Sci 102 (1), 16-24 (2021)
   PUBMED   33583643
  REMARK    GeneRIF: Nucleosome assembly protein 1-like 4, a new therapeutic
            target for proliferation and invasion of melanoma cells.
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Tanaka,T., Hozumi,Y., Martelli,A.M., Iino,M. and Goto,K.
  TITLE     Nucleosome assembly proteins NAP1L1 and NAP1L4 modulate p53
            acetylation to regulate cell fate
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1866 (12), 118560 (2019)
   PUBMED   31634504
  REMARK    GeneRIF: The NAP1L4 regulates cell fate by controlling the
            expression of p53-responsive proarrest and proapoptotic genes
            through selective modulation of p53 acetylation at specific sites
            during normal homeostasis and in stress-induced responses.
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Tanaka,T., Hozumi,Y., Iino,M. and Goto,K.
  TITLE     NAP1L1 regulates NF-kappaB signaling pathway acting on
            anti-apoptotic Mcl-1 gene expression
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1864 (10), 1759-1768 (2017)
   PUBMED   28687276
  REMARK    GeneRIF: knockdown of NAP1L1 suppresses IkappaBalpha degradation
            and nuclear transport of p65 subunit after treatment with TNF-a
            stimulation, leading to attenuation of the NF-kappaB
            transcriptional activity, whereas NAP1L4 knockdown remains
            silent.results of this study suggest that NAP1L1 downregulation
            renders the cell vulnerable to apoptotic cell death through
            attenuation of NF-kappaB transcriptional activity on the
            anti-apop...
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Ruiz,M.T., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2 is part of multi-protein complexes in HeLa cells
  JOURNAL   J Cell Biochem 93 (2), 398-408 (2004)
   PUBMED   15368365
  REMARK    GeneRIF: NAP-2 is in complex(es) with other proteins, which are
            distinct from histones
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Shikama,N., Chan,H.M., Krstic-Demonacos,M., Smith,L., Lee,C.W.,
            Cairns,W. and La Thangue,N.B.
  TITLE     Functional interaction between nucleosome assembly proteins and
            p300/CREB-binding protein family coactivators
  JOURNAL   Mol Cell Biol 20 (23), 8933-8943 (2000)
   PUBMED   11073993
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Pelletier,J., Price,G.B. and Zannis-Hadjopoulos,M.
  TITLE     NAP-2: histone chaperone function and phosphorylation state through
            the cell cycle
  JOURNAL   J Mol Biol 298 (2), 225-238 (2000)
   PUBMED   10764593
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Rodriguez,P., Munroe,D., Prawitt,D., Chu,L.L., Bric,E., Kim,J.,
            Reid,L.H., Davies,C., Nakagama,H., Loebbert,R., Winterpacht,A.,
            Petruzzi,M.J., Higgins,M.J., Nowak,N., Evans,G., Shows,T.,
            Weissman,B.E., Zabel,B., Housman,D.E. and Pelletier,J.
  TITLE     Functional characterization of human nucleosome assembly protein-2
            (NAP1L4) suggests a role as a histone chaperone
  JOURNAL   Genomics 44 (3), 253-265 (1997)
   PUBMED   9325046
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Hu,R.J., Lee,M.P., Johnson,L.A. and Feinberg,A.P.
  TITLE     A novel human homologue of yeast nucleosome assembly protein, 65 kb
            centromeric to the p57KIP2 gene, is biallelically expressed in
            fetal and adult tissues
  JOURNAL   Hum Mol Genet 5 (11), 1743-1748 (1996)
   PUBMED   8923002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC131971.9.
            
            Summary: This gene encodes a member of the nucleosome assembly
            protein (NAP) family which can interact with both core and linker
            histones. It can shuttle between the cytoplasm and nucleus,
            suggesting a role as a histone chaperone. This gene is one of
            several located near the imprinted gene domain of 11p15.5, an
            important tumor-suppressor gene region. Alterations in this region
            have been associated with the Beckwith-Wiedemann syndrome, Wilms
            tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung,
            ovarian, and breast cancer. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: DRR138506.60402.1, SRR1163658.520072.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..386
                     /product="nucleosome assembly protein 1-like 4 isoform 2"
                     /note="nucleosome assembly protein 2; nucleosome assembly
                     protein 1-like 4b; NAP-2"
                     /calculated_mol_wt=43948
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          65..338
                     /region_name="NAP"
                     /note="Nucleosome assembly protein (NAP); pfam00956"
                     /db_xref="CDD:460010"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P28656; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          116..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q78ZA7; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     Region          265..271
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99733.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99733.1)"
     CDS             1..386
                     /gene="NAP1L4"
                     /gene_synonym="hNAP2; NAP1L4b; NAP2; NAP2L"
                     /coded_by="NM_001369385.1:441..1601"
                     /note="isoform 2 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS91410.1"
                     /db_xref="GeneID:4676"
                     /db_xref="HGNC:HGNC:7640"
                     /db_xref="MIM:601651"
ORIGIN      
        1 madhsfsdgv psdsveaakn asntekltdq vmqnprvlaa lqerldnvph tpssyietlp
       61 kavkrrinal kqlqvrcahi eakfyeevhd lerkyaalyq plfdkrrefi tgdveptdae
      121 sewhseneee eklagdmksk vvvtekaaat aeepdpkgip efwftifrnv dmlselvqey
      181 depilkhlqd ikvkfsdpgq pmsfvlefhf epndyftnsv ltktykmkse pdkadpfsfe
      241 gpeivdcdgc tidwkkgknv tvktikkkqk hkgrgtvrti tkqvpnesff nffnplkasg
      301 dgesldedse ftlasdfeig hffrerivpr avlyftgeai edddnfeege egeeeelegd
      361 eegededdae inpkkepsqp aeckqq
//
LOCUS       NP_001356412             264 aa            linear   PRI 27-APR-2025
DEFINITION  COP9 signalosome complex subunit 7b isoform b [Homo sapiens].
ACCESSION   NP_001356412 XP_016860205
VERSION     NP_001356412.1
DBSOURCE    REFSEQ: accession NM_001369483.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Tang,J., Wang,S., Weng,M., Guo,Q., Ren,L., He,Y., Cui,Z., Cong,M.,
            Qin,M., Yu,J., Su,R. and Li,X.
  TITLE     The IGF2BP3-COPS7B Axis Facilitates mRNA Translation to Drive
            Colorectal Cancer Progression
  JOURNAL   Cancer Res 83 (21), 3593-3610 (2023)
   PUBMED   37560971
  REMARK    GeneRIF: The IGF2BP3-COPS7B Axis Facilitates mRNA Translation to
            Drive Colorectal Cancer Progression.
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wang,J., Dubiel,D., Wu,Y., Cheng,Y., Wolf,D.A. and Dubiel,W.
  TITLE     CSN7B defines a variant COP9 signalosome complex with distinct
            function in DNA damage response
  JOURNAL   Cell Rep 34 (4), 108662 (2021)
   PUBMED   33503427
  REMARK    GeneRIF: CSN7B defines a variant COP9 signalosome complex with
            distinct function in DNA damage response.
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Fuzesi-Levi,M.G., Ben-Nissan,G., Bianchi,E., Zhou,H., Deery,M.J.,
            Lilley,K.S., Levin,Y. and Sharon,M.
  TITLE     Dynamic regulation of the COP9 signalosome in response to DNA
            damage
  JOURNAL   Mol Cell Biol 34 (6), 1066-1076 (2014)
   PUBMED   24421388
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Hoareau Alves,K., Bochard,V., Rety,S. and Jalinot,P.
  TITLE     Association of the mammalian proto-oncoprotein Int-6 with the three
            protein complexes eIF3, COP9 signalosome and 26S proteasome
  JOURNAL   FEBS Lett 527 (1-3), 15-21 (2002)
   PUBMED   12220626
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Wang,Y., Devereux,W., Stewart,T.M. and Casero,R.A. Jr.
  TITLE     Polyamine-modulated factor 1 binds to the human homologue of the 7a
            subunit of the Arabidopsis COP9 signalosome: implications in gene
            expression
  JOURNAL   Biochem J 366 (Pt 1), 79-86 (2002)
   PUBMED   12020345
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Lyapina,S., Cope,G., Shevchenko,A., Serino,G., Tsuge,T., Zhou,C.,
            Wolf,D.A., Wei,N., Shevchenko,A. and Deshaies,R.J.
  TITLE     Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome
  JOURNAL   Science 292 (5520), 1382-1385 (2001)
   PUBMED   11337588
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Bech-Otschir,D., Kraft,R., Huang,X., Henklein,P., Kapelari,B.,
            Pollmann,C. and Dubiel,W.
  TITLE     COP9 signalosome-specific phosphorylation targets p53 to
            degradation by the ubiquitin system
  JOURNAL   EMBO J 20 (7), 1630-1639 (2001)
   PUBMED   11285227
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073476.6.
            
            On Apr 10, 2019 this sequence version replaced XP_016860205.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.163426.1,
                                           SRR1803614.100923.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..264
                     /product="COP9 signalosome complex subunit 7b isoform b"
                     /note="COP9 signalosome complex subunit 7b; signalosome
                     subunit 7b; JAB1-containing signalosome subunit 7b; COP9
                     constitutive photomorphogenic homolog subunit 7B"
                     /calculated_mol_wt=29491
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:18850735,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9H9Q2.1)"
     Region          88..177
                     /region_name="PINT"
                     /note="motif in proteasome subunits, Int-6, Nip-1 and
                     TRIP-15; smart00088"
                     /db_xref="CDD:214509"
     Region          166..215
                     /region_name="CSN7a_helixI"
                     /note="COP9 signalosome complex subunit 7a helix I domain;
                     pfam18392"
                     /db_xref="CDD:465740"
     Region          223..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9Q2.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H9Q2.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H9Q2.1)"
     CDS             1..264
                     /gene="COPS7B"
                     /gene_synonym="CSN7B; SGN7b"
                     /coded_by="NM_001369483.1:230..1024"
                     /note="isoform b is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS2488.1"
                     /db_xref="GeneID:64708"
                     /db_xref="HGNC:HGNC:16760"
                     /db_xref="MIM:616010"
ORIGIN      
        1 mageqkpssn lleqfillak gtsgsaltal isqvleapgv yvfgellela nvqelaegan
       61 aaylqllnlf aygtypdyia nkeslpelst aqqnklkhlt ivslasrmkc ipysvllkdl
      121 emrnlreled liieavytdi iqgkldqrnq llevdfcigr dirkkdinni vktlhewcdg
      181 ceavllgieq qvlranqyke nhnrtqqqve aevtnikktl katasssaqe meqqlaerec
      241 pphaeqrqpt kkmskvkglv ssrh
//
LOCUS       NP_036233                588 aa            linear   PRI 27-APR-2025
DEFINITION  tripartite motif-containing protein 29 isoform 1 [Homo sapiens].
ACCESSION   NP_036233
VERSION     NP_036233.2
DBSOURCE    REFSEQ: accession NM_012101.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Sun,Z., Li,X., Shi,Y. and Yao,Y.
  TITLE     LncRNA PVT1 facilitates the growth and metastasis of colorectal
            cancer by sponging with miR-3619-5p to regulate TRIM29 expression
  JOURNAL   Cancer Rep (Hoboken) 7 (6), e2085 (2024)
   PUBMED   38837682
  REMARK    GeneRIF: LncRNA PVT1 facilitates the growth and metastasis of
            colorectal cancer by sponging with miR-3619-5p to regulate TRIM29
            expression.
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Zhao,F.Y., Chen,X., Wang,J.M., Yuan,Y., Li,C., Sun,J. and Wang,H.Q.
  TITLE     O-GlcNAcylation of TRIM29 and OGT translation forms a feedback loop
            to promote adaptive response of PDAC cells to glucose deficiency
  JOURNAL   Cell Oncol (Dordr) 47 (3), 1025-1041 (2024)
   PUBMED   38345749
  REMARK    GeneRIF: O-GlcNAcylation of TRIM29 and OGT translation forms a
            feedback loop to promote adaptive response of PDAC cells to glucose
            deficiency.
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Huang,W., Hu,X., He,X., Pan,D., Huang,Z., Gu,Z., Huang,G., Wang,P.,
            Cui,C. and Fan,Y.
  TITLE     TRIM29 facilitates gemcitabine resistance via MEK/ERK pathway and
            is modulated by circRPS29/miR-770-5p axis in PDAC
  JOURNAL   Drug Resist Updat 74, 101079 (2024)
   PUBMED   38518727
  REMARK    GeneRIF: TRIM29 facilitates gemcitabine resistance via MEK/ERK
            pathway and is modulated by circRPS29/miR-770-5p axis in PDAC.
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Yin,Y.T., Shi,L., Wu,C., Zhang,M.Y., Li,J.X., Zhou,Y.F., Wang,S.C.,
            Wang,H.Y. and Mai,S.J.
  TITLE     TRIM29 modulates proteins involved in PTEN/AKT/mTOR and JAK2/STAT3
            signaling pathway and suppresses the progression of hepatocellular
            carcinoma
  JOURNAL   Med Oncol 41 (3), 79 (2024)
   PUBMED   38393440
  REMARK    GeneRIF: TRIM29 modulates proteins involved in PTEN/AKT/mTOR and
            JAK2/STAT3 signaling pathway and suppresses the progression of
            hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 588)
  AUTHORS   Jiang,T., Xia,Y., Li,Y., Lu,C., Lin,J., Shen,Y., Lv,J., Xie,L.,
            Gu,C., Xu,Z. and Wang,L.
  TITLE     TRIM29 promotes antitumor immunity through enhancing IGF2BP1
            ubiquitination and subsequent PD-L1 downregulation in gastric
            cancer
  JOURNAL   Cancer Lett 581, 216510 (2024)
   PUBMED   38029830
  REMARK    GeneRIF: TRIM29 promotes antitumor immunity through enhancing
            IGF2BP1 ubiquitination and subsequent PD-L1 downregulation in
            gastric cancer.
REFERENCE   6  (residues 1 to 588)
  AUTHORS   Brzoska,P.M., Chen,H., Zhu,Y., Levin,N.A., Disatnik,M.H.,
            Mochly-Rosen,D., Murnane,J.P. and Christman,M.F.
  TITLE     The product of the ataxia-telangiectasia group D complementing
            gene, ATDC, interacts with a protein kinase C substrate and
            inhibitor
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7824-7828 (1995)
   PUBMED   7644499
REFERENCE   7  (residues 1 to 588)
  AUTHORS   Murnane,J.P., Zhu,Y., Young,B.R. and Christman,M.F.
  TITLE     Expression of the candidate A-T gene ATDC is not detectable in a
            human cell line with a normal response to ionizing radiation
  JOURNAL   Int J Radiat Biol 66 (6 Suppl), S77-S84 (1994)
   PUBMED   7836856
REFERENCE   8  (residues 1 to 588)
  AUTHORS   Hosoi,Y. and Kapp,L.N.
  TITLE     Expression of a candidate ataxia-telangiectasia group D gene in
            cultured fibroblast cell lines and human tissues
  JOURNAL   Int J Radiat Biol 66 (6 Suppl), S71-S76 (1994)
   PUBMED   7530755
REFERENCE   9  (residues 1 to 588)
  AUTHORS   Leonhardt,E.A., Kapp,L.N., Young,B.R. and Murnane,J.P.
  TITLE     Nucleotide sequence analysis of a candidate gene for
            ataxia-telangiectasia group D (ATDC)
  JOURNAL   Genomics 19 (1), 130-136 (1994)
   PUBMED   8188213
REFERENCE   10 (residues 1 to 588)
  AUTHORS   Kapp,L.N., Painter,R.B., Yu,L.C., van Loon,N., Richard,C.W. 3rd,
            James,M.R., Cox,D.R. and Murnane,J.P.
  TITLE     Cloning of a candidate gene for ataxia-telangiectasia group D
  JOURNAL   Am J Hum Genet 51 (1), 45-54 (1992)
   PUBMED   1609804
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000679.7 and BC017352.2.
            
            On Dec 7, 2001 this sequence version replaced NP_036233.1.
            
            Summary: The protein encoded by this gene belongs to the TRIM
            protein family. It has multiple zinc finger motifs and a leucine
            zipper motif. It has been proposed to form homo- or heterodimers
            which are involved in nucleic acid binding. Thus, it may act as a
            transcriptional regulatory factor involved in carcinogenesis and/or
            differentiation. It may also function in the suppression of
            radiosensitivity since it is associated with ataxia telangiectasia
            phenotype. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017352.2, AK223090.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341846.10/ ENSP00000343129.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..588
                     /product="tripartite motif-containing protein 29 isoform
                     1"
                     /note="tripartite motif protein TRIM29;
                     ataxia-telangiectasia group D-associated protein;
                     tripartite motif-containing protein 29"
                     /calculated_mol_wt=65704
     Region          1..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14134.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14134.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14134.2)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14134.2)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14134.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14134.2)"
     Region          171..217
                     /region_name="Bbox1_TRIM29"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 29 (TRIM29) and similar proteins;
                     cd19840"
                     /db_xref="CDD:380898"
     Region          223..260
                     /region_name="Bbox2_TRIM16-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins, TRIM16, TRIM29, TRIM47 and
                     similar proteins; cd19769"
                     /db_xref="CDD:380827"
     Region          <275..>355
                     /region_name="HlpA"
                     /note="Periplasmic chaperone for outer membrane proteins,
                     Skp family [Cell wall/membrane/envelope biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG2825"
                     /db_xref="CDD:442073"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14134.2)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14134.2)"
     CDS             1..588
                     /gene="TRIM29"
                     /gene_synonym="ATDC"
                     /coded_by="NM_012101.4:83..1849"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8428.1"
                     /db_xref="GeneID:23650"
                     /db_xref="HGNC:HGNC:17274"
                     /db_xref="MIM:610658"
ORIGIN      
        1 meaadasrsn gsspeardar spsgpsgsle ngtkadgkda kttnghggea aegkslgsal
       61 kpgegrsalf agnewrrpii qfvesgddkn snyfsmdsme gkrspyaglq lgaakkppvt
      121 faekgelrks ifsesrkptv simepgetrr nsypradtgl fsrsksgsee vlcdscignk
      181 qkavksclvc qasfcelhlk phlegaafrd hqllepirdf earkcpvhgk tmelfcqtdq
      241 tcicylcmfq ehknhstvtv eeakaekete lslqkeqlql kiieiedeae kwqkekdrik
      301 sfttnekail eqnfrdlvrd lekqkeevra aleqreqdav dqvkvimdal derakvlhed
      361 kqtreqlhsi sdsvlflqef galmsnyslp pplptyhvll egeglgqslg nfkddllnvc
      421 mrhvekmcka dlsrnfiern hmenggdhry vnnytnsfgg ewsapdtmkr ysmyltpkgg
      481 vrtsyqpssp grftkettqk nfnnlygtkg nytsrvweys ssiqnsdndl pvvqgsssfs
      541 lkgypslmrs qspkaqpqtw ksgkqtmlsh yrpfyvnkgn gigsneap
//
LOCUS       NP_036413                630 aa            linear   PRI 27-APR-2025
DEFINITION  A-type voltage-gated potassium channel KCND2 [Homo sapiens].
ACCESSION   NP_036413
VERSION     NP_036413.1
DBSOURCE    REFSEQ: accession NM_012281.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Ye,W., Zhao,H., Dai,Y., Wang,Y., Lo,Y.H., Jan,L.Y. and Lee,C.H.
  TITLE     Activation and closed-state inactivation mechanisms of the human
            voltage-gated KV4 channel complexes
  JOURNAL   Mol Cell 82 (13), 2427-2442 (2022)
   PUBMED   35597238
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Zhang,Y., Tachtsidis,G., Schob,C., Koko,M., Hedrich,U.B.S.,
            Lerche,H., Lemke,J.R., van Haeringen,A., Ruivenkamp,C.,
            Prescott,T., Tveten,K., Gerstner,T., Pruniski,B., DiTroia,S.,
            VanNoy,G.E., Rehm,H.L., McLaughlin,H., Bolz,H.J., Zechner,U.,
            Bryant,E., McDonough,T., Kindler,S. and Bahring,R.
  TITLE     KCND2 variants associated with global developmental delay
            differentially impair Kv4.2 channel gating
  JOURNAL   Hum Mol Genet 30 (23), 2300-2314 (2021)
   PUBMED   34245260
  REMARK    GeneRIF: KCND2 variants associated with global developmental delay
            differentially impair Kv4.2 channel gating.
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Kise,Y., Kasuya,G., Okamoto,H.H., Yamanouchi,D., Kobayashi,K.,
            Kusakizako,T., Nishizawa,T., Nakajo,K. and Nureki,O.
  TITLE     Structural basis of gating modulation of Kv4 channel complexes
  JOURNAL   Nature 599 (7883), 158-164 (2021)
   PUBMED   34552243
  REMARK    GeneRIF: Structural basis of gating modulation of Kv4 channel
            complexes.
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Lu,X., Li,K. and Yang,J.
  TITLE     Potassium voltage-gated channel subfamily D member 2 induces an
            aggressive phenotype in lung adenocarcinoma
  JOURNAL   Neoplasma 68 (1), 135-143 (2021)
   PUBMED   32977724
  REMARK    GeneRIF: Potassium voltage-gated channel subfamily D member 2
            induces an aggressive phenotype in lung adenocarcinoma.
REFERENCE   5  (residues 1 to 630)
  AUTHORS   Seifert,C., Storch,S. and Bahring,R.
  TITLE     Modulation of Kv4.2/KChIP3 interaction by the ceroid lipofuscinosis
            neuronal 3 protein CLN3
  JOURNAL   J Biol Chem 295 (34), 12099-12110 (2020)
   PUBMED   32641494
  REMARK    GeneRIF: Modulation of Kv4.2/KChIP3 interaction by the ceroid
            lipofuscinosis neuronal 3 protein CLN3.
REFERENCE   6  (residues 1 to 630)
  AUTHORS   An,W.F., Bowlby,M.R., Betty,M., Cao,J., Ling,H.P., Mendoza,G.,
            Hinson,J.W., Mattsson,K.I., Strassle,B.W., Trimmer,J.S. and
            Rhodes,K.J.
  TITLE     Modulation of A-type potassium channels by a family of calcium
            sensors
  JOURNAL   Nature 403 (6769), 553-556 (2000)
   PUBMED   10676964
REFERENCE   7  (residues 1 to 630)
  AUTHORS   Kurschner,C. and Yuzaki,M.
  TITLE     Neuronal interleukin-16 (NIL-16): a dual function PDZ domain
            protein
  JOURNAL   J Neurosci 19 (18), 7770-7780 (1999)
   PUBMED   10479680
REFERENCE   8  (residues 1 to 630)
  AUTHORS   Zhu,X.R., Wulf,A., Schwarz,M., Isbrandt,D. and Pongs,O.
  TITLE     Characterization of human Kv4.2 mediating a rapidly-inactivating
            transient voltage-sensitive K+ current
  JOURNAL   Recept Channels 6 (5), 387-400 (1999)
   PUBMED   10551270
REFERENCE   9  (residues 1 to 630)
  AUTHORS   Kong,W., Po,S., Yamagishi,T., Ashen,M.D., Stetten,G. and
            Tomaselli,G.F.
  TITLE     Isolation and characterization of the human gene encoding Ito:
            further diversity by alternative mRNA splicing
  JOURNAL   Am J Physiol 275 (6), H1963-H1970 (1998)
   PUBMED   9843794
REFERENCE   10 (residues 1 to 630)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004946.1, AC092020.3,
            BC110449.1 and AC004888.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Voltage-gated potassium (Kv) channels represent the most
            complex class of voltage-gated ion channels from both functional
            and structural standpoints. Their diverse functions include
            regulating neurotransmitter release, heart rate, insulin secretion,
            neuronal excitability, epithelial electrolyte transport, smooth
            muscle contraction, and cell volume. Four sequence-related
            potassium channel genes - shaker, shaw, shab, and shal - have been
            identified in Drosophila, and each has been shown to have human
            homolog(s). This gene encodes a member of the potassium channel,
            voltage-gated, shal-related subfamily, members of which form
            voltage-activated A-type potassium ion channels and are prominent
            in the repolarization phase of the action potential. This member
            mediates a rapidly inactivating, A-type outward potassium current
            which is not under the control of the N terminus as it is in Shaker
            channels. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.107642.1,
                                           SRR1660809.83254.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331113.9/ ENSP00000333496.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.31"
     Protein         1..630
                     /product="A-type voltage-gated potassium channel KCND2"
                     /note="voltage-sensitive potassium channel; voltage-gated
                     potassium channel subunit Kv4.2; potassium channel,
                     voltage gated Shal related subfamily D, member 2"
                     /calculated_mol_wt=70406
     Region          2..20
                     /region_name="Interaction with KCNIP1, KCNIP2, and other
                     family members. /evidence=ECO:0000250|UniProtKB:Q63881"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Region          6..144
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63881; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Region          71..90
                     /region_name="Interaction with KCNIP1.
                     /evidence=ECO:0000250|UniProtKB:Q63881"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Region          184..415
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            185..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            227..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            257..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            288..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Region          308..321
                     /region_name="S4-S5 linker.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            322..345
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Region          370..375
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            381..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63881; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Region          470..546
                     /region_name="DUF3399"
                     /note="Domain of unknown function (DUF3399); pfam11879"
                     /db_xref="CDD:463381"
     Region          474..630
                     /region_name="Important for normal channel activation and
                     inactivation, for interaction with KCNIP2, and probably
                     other family members as well.
                     /evidence=ECO:0000250|UniProtKB:Q63881,
                     ECO:0000305|PubMed:16934482"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Region          474..489
                     /region_name="Required for dendritic targeting.
                     /evidence=ECO:0000250|UniProtKB:Q63881"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63881; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0V2; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0V2; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0V2; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Region          600..630
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63881; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            607
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63881; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0V2; propagated from
                     UniProtKB/Swiss-Prot (Q9NZV8.2)"
     Region          627..630
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000250|UniProtKB:Q63881"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZV8.2)"
     CDS             1..630
                     /gene="KCND2"
                     /gene_synonym="KV4.2; RK5"
                     /coded_by="NM_012281.3:1459..3351"
                     /db_xref="CCDS:CCDS5776.1"
                     /db_xref="GeneID:3751"
                     /db_xref="HGNC:HGNC:6238"
                     /db_xref="MIM:605410"
ORIGIN      
        1 maagvaawlp faraaaigwm pvasgpmpap prqerkrtqd alivlnvsgt rfqtwqdtle
       61 rypdtllgss erdffyhpet qqyffdrdpd ifrhilnfyr tgklhyprhe cisaydeela
      121 ffglipeiig dccyeeykdr rrenaerlqd dadtdtages alptmtarqr vwrafenpht
      181 stmalvfyyv tgffiavsvi anvvetvpcg sspghikelp cgeryavaff cldtacvmif
      241 tveyllrlaa apsryrfvrs vmsiidvvai lpyyiglvmt dnedvsgafv tlrvfrvfri
      301 fkfsrhsqgl rilgytlksc aselgfllfs ltmaiiifat vmfyaekgss askftsipaa
      361 fwytivtmtt lgygdmvpkt iagkifgsic slsgvlvial pvpvivsnfs riyhqnqrad
      421 krraqkkarl ariraaksgs anaymqskrn gllsnqlqss edeqafvsks gssfetqhhh
      481 llhclekttn hefvdeqvfe escmevatvn rpsshspsls sqqgvtstcc srrhkktfri
      541 pnanvsgshq gsiqelstiq ircvertpls nsrsslnakm eecvklnceq pyvttaiisi
      601 ptppvttpeg ddrpespeys ggnivrvsal
//
LOCUS       NP_443117                648 aa            linear   PRI 27-APR-2025
DEFINITION  proton myo-inositol cotransporter [Homo sapiens].
ACCESSION   NP_443117
VERSION     NP_443117.3
DBSOURCE    REFSEQ: accession NM_052885.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Lai,B., Lai,Y., Zhang,Y., Zhou,M., Sheng,L. and OuYang,G.
  TITLE     The Solute Carrier Family 2 Genes Are Potential Prognostic
            Biomarkers in Acute Myeloid Leukemia
  JOURNAL   Technol Cancer Res Treat 19, 1533033819894308 (2020)
   PUBMED   31918632
  REMARK    GeneRIF: The Solute Carrier Family 2 Genes Are Potential Prognostic
            Biomarkers in Acute Myeloid Leukemia.
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Lyu,M., Zhou,J., Chen,H., Bai,H., Song,J., Liu,T., Cheng,Y. and
            Ying,B.
  TITLE     The genetic variants in calcium signaling related genes influence
            anti-tuberculosis drug induced liver injury: A prospective study
  JOURNAL   Medicine (Baltimore) 98 (44), e17821 (2019)
   PUBMED   31689868
  REMARK    GeneRIF: Our study revealed that both BDKRB2 and TENM2 genetic
            polymorphisms were interrogated in relation to anti-tuberculosis
            drug induced liver injury (ATDILI) susceptibility and some
            laboratory indicators in the Western Chinese Han population,
            shedding a new light on exploring novel biomarkers and targets for
            ATDILI.
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Sweeney,M.D., Zhao,Z., Montagne,A., Nelson,A.R. and Zlokovic,B.V.
  TITLE     Blood-Brain Barrier: From Physiology to Disease and Back
  JOURNAL   Physiol Rev 99 (1), 21-78 (2019)
   PUBMED   30280653
  REMARK    Review article
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Bankovic,J., Stojsic,J., Jovanovic,D., Andjelkovic,T.,
            Milinkovic,V., Ruzdijic,S. and Tanic,N.
  TITLE     Identification of genes associated with non-small-cell lung cancer
            promotion and progression
  JOURNAL   Lung Cancer 67 (2), 151-159 (2010)
   PUBMED   19473719
  REMARK    GeneRIF: genetic alterations of TSPAN14, SLC2A13 and PHF20 could
            play a role in non-small-cell lung cancer promotion
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Satake,W., Nakabayashi,Y., Mizuta,I., Hirota,Y., Ito,C., Kubo,M.,
            Kawaguchi,T., Tsunoda,T., Watanabe,M., Takeda,A., Tomiyama,H.,
            Nakashima,K., Hasegawa,K., Obata,F., Yoshikawa,T., Kawakami,H.,
            Sakoda,S., Yamamoto,M., Hattori,N., Murata,M., Nakamura,Y. and
            Toda,T.
  TITLE     Genome-wide association study identifies common variants at four
            loci as genetic risk factors for Parkinson's disease
  JOURNAL   Nat Genet 41 (12), 1303-1307 (2009)
   PUBMED   19915576
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Di Daniel,E., Mok,M.H., Mead,E., Mutinelli,C., Zambello,E.,
            Caberlotto,L.L., Pell,T.J., Langmead,C.J., Shah,A.J., Duddy,G.,
            Kew,J.N. and Maycox,P.R.
  TITLE     Evaluation of expression and function of the H+/myo-inositol
            transporter HMIT
  JOURNAL   BMC Cell Biol 10, 54 (2009)
   PUBMED   19607714
  REMARK    GeneRIF: HMIT is primarily a neuronal transporter widely expressed
            in the rat and human brain, with particularly high levels in the
            hippocampus and cortex, as shown by immunohistochemistry.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Fu,G.K., Wang,J.T., Yang,J., Au-Young,J. and Stuve,L.L.
  TITLE     Circular rapid amplification of cDNA ends for high-throughput
            extension cloning of partial genes
  JOURNAL   Genomics 84 (1), 205-210 (2004)
   PUBMED   15203218
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Uldry,M., Ibberson,M., Horisberger,J.D., Chatton,J.Y.,
            Riederer,B.M. and Thorens,B.
  TITLE     Identification of a mammalian H(+)-myo-inositol symporter expressed
            predominantly in the brain
  JOURNAL   EMBO J 20 (16), 4467-4477 (2001)
   PUBMED   11500374
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079630.18, AJ315644.1, BC117119.1, AC121335.5 and AK026495.1.
            
            On Sep 17, 2008 this sequence version replaced NP_443117.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.160490.1, AJ315644.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280871.9/ ENSP00000280871.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..648
                     /product="proton myo-inositol cotransporter"
                     /note="proton (H+) myo-inositol symporter;
                     H(+)-myo-inositol symporter; h(+)-myo-inositol
                     cotransporter; solute carrier family 2 (facilitated
                     glucose transporter), member 13"
                     /calculated_mol_wt=70240
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHK1; propagated from
                     UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHK1; propagated from
                     UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHK1; propagated from
                     UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Region          87..596
                     /region_name="MFS_HMIT_like"
                     /note="H(+)-myo-inositol cotransporter and similar
                     transporters of the Major Facilitator Superfamily;
                     cd17360"
                     /db_xref="CDD:340918"
     Site            order(95,99,213,216..217,220,336..337,341..342,345..346,
                     374,520..521,524..525,529,552..553,556)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340918"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            240..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            325..345
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            364..384
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            394..414
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            458
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            485
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            509..529
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            550..570
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            574..594
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96QE2.3)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96QE2.3)"
     CDS             1..648
                     /gene="SLC2A13"
                     /gene_synonym="HMIT"
                     /coded_by="NM_052885.4:274..2220"
                     /db_xref="CCDS:CCDS8736.2"
                     /db_xref="GeneID:114134"
                     /db_xref="HGNC:HGNC:15956"
                     /db_xref="MIM:611036"
ORIGIN      
        1 msrkasenve ytlrslsslm gerrrkqpep daasaagecs llaaaessts lqsagagggg
       61 vgdleraarr qfqqdetpaf vyvvavfsal ggflfgydtg vvsgamlllk rqlsldalwq
      121 ellvsstvga aavsalagga lngvfgrraa illasalfta gsavlaaann ketllagrlv
      181 vglgigiasm tvpvyiaevs ppnlrgrlvt intlfitggq ffasvvdgaf sylqkdgwry
      241 mlglaavpav iqffgflflp esprwliqkg qtqkarrils qmrgnqtide eydsiknnie
      301 eeekevgsag pvicrmlsyp ptrralivgc glqmfqqlsg intimyysat ilqmsgvedd
      361 rlaiwlasvt aftnfiftlv gvwlvekvgr rkltfgslag ttvaliilal gfvlsaqvsp
      421 ritfkpiaps gqnatctrys ycnecmldpd cgfcykmnks tvidsscvpv nkastneaaw
      481 grcenetkfk tedifwaynf cptpyswtal lglilylvff apgmgpmpwt vnseiyplwa
      541 rstgnacssg inwifnvlvs ltflhtaeyl tyygafflya gfaavgllfi ygclpetkgk
      601 kleeieslfd nrlctcgtsd sdegryieyi rvkgsnyhls dndasdve
//
LOCUS       NP_065726                224 aa            linear   PRI 27-APR-2025
DEFINITION  kinetochore protein Spc25 [Homo sapiens].
ACCESSION   NP_065726
VERSION     NP_065726.1
DBSOURCE    REFSEQ: accession NM_020675.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Zhang,W., Yu,L., Xu,C., Tang,T., Cao,J., Chen,L., Pang,X. and
            Ren,W.
  TITLE     PLEK2 activates the PI3K/AKT signaling pathway to drive lung
            adenocarcinoma progression by upregulating SPC25
  JOURNAL   Cell Biol Int 48 (9), 1285-1300 (2024)
   PUBMED   38894536
  REMARK    GeneRIF: PLEK2 activates the PI3K/AKT signaling pathway to drive
            lung adenocarcinoma progression by upregulating SPC25.
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Liao,L.X., Zhang,M., Xu,X., Zhang,S. and Guo,Y.Z.
  TITLE     SPC25 Functions as a Prognostic-Related Biomarker, and Its High
            Expression Correlates with Tumor Immune Infiltration and UCEC
            Progression
  JOURNAL   Front Biosci (Landmark Ed) 29 (2), 69 (2024)
   PUBMED   38420826
  REMARK    GeneRIF: SPC25 Functions as a Prognostic-Related Biomarker, and Its
            High Expression Correlates with Tumor Immune Infiltration and UCEC
            Progression.
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Liu,X.S., Zhang,Y., Ming,X., Hu,J., Chen,X.L., Wang,Y.L.,
            Zhang,Y.H., Gao,Y. and Pei,Z.J.
  TITLE     SPC25 as a novel therapeutic and prognostic biomarker and its
            association with glycolysis, ferroptosis and ceRNA in lung
            adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 779-798 (2024)
   PUBMED   38217547
  REMARK    GeneRIF: SPC25 as a novel therapeutic and prognostic biomarker and
            its association with glycolysis, ferroptosis and ceRNA in lung
            adenocarcinoma.
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Yang,J., Huang,Y., Song,M., Pan,Q., Zhao,J., He,J., Ouyang,D.,
            Yang,C., Han,Y., Tang,Y., Wang,Q., He,J., Li,Y., Chen,H., Weng,D.,
            Xiang,T. and Xia,J.
  TITLE     SPC25 promotes proliferation and stemness of hepatocellular
            carcinoma cells via the DNA-PK/AKT/Notch1 signaling pathway
  JOURNAL   Int J Biol Sci 18 (14), 5241-5259 (2022)
   PUBMED   36147467
  REMARK    GeneRIF: SPC25 promotes proliferation and stemness of
            hepatocellular carcinoma cells via the DNA-PK/AKT/Notch1 signaling
            pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Cui,F., Xu,Z., Hu,J. and Lv,Y.
  TITLE     Spindle pole body component 25 and platelet-derived growth factor
            mediate crosstalk between tumor-associated macrophages and prostate
            cancer cells
  JOURNAL   Front Immunol 13, 907636 (2022)
   PUBMED   35967419
  REMARK    GeneRIF: Spindle pole body component 25 and platelet-derived growth
            factor mediate crosstalk between tumor-associated macrophages and
            prostate cancer cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Ciferri,C., Pasqualato,S., Screpanti,E., Varetti,G., Santaguida,S.,
            Dos Reis,G., Maiolica,A., Polka,J., De Luca,J.G., De Wulf,P.,
            Salek,M., Rappsilber,J., Moores,C.A., Salmon,E.D. and Musacchio,A.
  TITLE     Implications for kinetochore-microtubule attachment from the
            structure of an engineered Ndc80 complex
  JOURNAL   Cell 133 (3), 427-439 (2008)
   PUBMED   18455984
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Ciferri,C., De Luca,J., Monzani,S., Ferrari,K.J., Ristic,D.,
            Wyman,C., Stark,H., Kilmartin,J., Salmon,E.D. and Musacchio,A.
  TITLE     Architecture of the human ndc80-hec1 complex, a critical
            constituent of the outer kinetochore
  JOURNAL   J Biol Chem 280 (32), 29088-29095 (2005)
   PUBMED   15961401
  REMARK    GeneRIF: the Spc24, Spc25, Nuf2, and Ndc80/Hec1 complex is a
            faithful copy of the endogenous Ndc80 complex
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Bharadwaj,R., Qi,W. and Yu,H.
  TITLE     Identification of two novel components of the human NDC80
            kinetochore complex
  JOURNAL   J Biol Chem 279 (13), 13076-13085 (2004)
   PUBMED   14699129
  REMARK    GeneRIF: hSPC25 is an essential kinetochore component that plays a
            significant role in proper execution of mitotic events
REFERENCE   9  (residues 1 to 224)
  AUTHORS   McCleland,M.L., Kallio,M.J., Barrett-Wilt,G.A., Kestner,C.A.,
            Shabanowitz,J., Hunt,D.F., Gorbsky,G.J. and Stukenberg,P.T.
  TITLE     The vertebrate Ndc80 complex contains Spc24 and Spc25 homologs,
            which are required to establish and maintain
            kinetochore-microtubule attachment
  JOURNAL   Curr Biol 14 (2), 131-137 (2004)
   PUBMED   14738735
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Kalies,K.U., Rapoport,T.A. and Hartmann,E.
  TITLE     The beta subunit of the Sec61 complex facilitates cotranslational
            protein transport and interacts with the signal peptidase during
            translocation
  JOURNAL   J Cell Biol 141 (4), 887-894 (1998)
   PUBMED   9585408
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC069137.6.
            
            Summary: This gene encodes a protein that may be involved in
            kinetochore-microtubule interaction and spindle checkpoint
            activity. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022255.1, SRR18074967.118523.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282074.7/ ENSP00000282074.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.3"
     Protein         1..224
                     /product="kinetochore protein Spc25"
                     /note="2600017H08Rik; spindle pole body component 25
                     homolog; SPC25, NDC80 kinetochore complex component,
                     homolog"
                     /calculated_mol_wt=26022
     Region          1..144
                     /region_name="Interaction with the N-terminus of SPBC24"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBM1.1)"
     Region          1..56
                     /region_name="Interaction with the NDC80-NUF2 subcomplex"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBM1.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HBM1.1)"
     Region          67..>142
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          128..215
                     /region_name="RWD_Spc25"
                     /note="RWD domain of kinetochore protein Spc25 and related
                     proteins; cd23784"
                     /db_xref="CDD:467646"
     Site            order(130..131,133..135,138..139,141,143,145..146,148,154,
                     160,197,200..201,206..213,215)
                     /site_type="other"
                     /note="Spc24 interface [polypeptide binding]"
                     /db_xref="CDD:467646"
     Region          145..224
                     /region_name="Interaction with the C-terminus of SPBC24"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBM1.1)"
     Site            order(147..149,152,154..155,157,159,169,171,176,182,188,
                     207)
                     /site_type="other"
                     /note="CENP-T binding site [polypeptide binding]"
                     /db_xref="CDD:467646"
     CDS             1..224
                     /gene="SPC25"
                     /gene_synonym="AD024; hSpc25; SPBC25"
                     /coded_by="NM_020675.4:128..802"
                     /db_xref="CCDS:CCDS2229.1"
                     /db_xref="GeneID:57405"
                     /db_xref="HGNC:HGNC:24031"
                     /db_xref="MIM:609395"
ORIGIN      
        1 mvedelalfd ksinefwnkf kstdtscqma glrdtykdsi kafaeklsvk lkeeermvem
       61 fleyqnqisr qnkliqekkd nllkliaevk gkkqelevlt aniqdlkeey srkketista
      121 nkanaerlkr lqksadlykd rlgleirkiy geklqfiftn idpknpespf mfslhlnear
      181 dyevsdsaph leglaefqen vrktnnfsaf lanvrkafta tvyn
//
LOCUS       NP_001354548             638 aa            linear   PRI 27-APR-2025
DEFINITION  double zinc ribbon and ankyrin repeat-containing protein 1 isoform
            8 [Homo sapiens].
ACCESSION   NP_001354548
VERSION     NP_001354548.1
DBSOURCE    REFSEQ: accession NM_001367619.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Dona,M., Bachmann-Gagescu,R., Texier,Y., Toedt,G., Hetterschijt,L.,
            Tonnaer,E.L., Peters,T.A., van Beersum,S.E., Bergboer,J.G.,
            Horn,N., de Vrieze,E., Slijkerman,R.W., van Reeuwijk,J., Flik,G.,
            Keunen,J.E., Ueffing,M., Gibson,T.J., Roepman,R., Boldt,K.,
            Kremer,H. and van Wijk,E.
  TITLE     NINL and DZANK1 Co-function in Vesicle Transport and Are Essential
            for Photoreceptor Development in Zebrafish
  JOURNAL   PLoS Genet 11 (10), e1005574 (2015)
   PUBMED   26485514
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Sedgwick,S.G. and Smerdon,S.J.
  TITLE     The ankyrin repeat: a diversity of interactions on a common
            structural framework
  JOURNAL   Trends Biochem Sci 24 (8), 311-316 (1999)
   PUBMED   10431175
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121893.21 and AL049646.19.
            
            Summary: This gene contains two ankyrin repeat-encoding regions.
            Ankyrin repeats are tandemly repeated modules of about 33 amino
            acids described as L-shaped structures consisting of a beta-hairpin
            and two alpha-helices. Ankyrin repeats occur in a large number of
            functionally diverse proteins, mainly from eukaryotes, and are
            known to function as protein-protein interaction domains. [provided
            by RefSeq, Dec 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749327.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..638
                     /product="double zinc ribbon and ankyrin repeat-containing
                     protein 1 isoform 8"
                     /note="ankyrin repeat-containing protein C20orf12; ankyrin
                     repeat domain 64; double zinc ribbon and ankyrin
                     repeat-containing protein 1"
                     /calculated_mol_wt=69941
     Region          97..156
                     /region_name="DZR"
                     /note="Double zinc ribbon; pfam12773"
                     /db_xref="CDD:432773"
     Region          225..273
                     /region_name="DZR"
                     /note="Double zinc ribbon; pfam12773"
                     /db_xref="CDD:432773"
     Region          <504..>618
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(505,507..508,512,515,524,526,528,532..533,536..538,
                     540..541,545,548,558,560,562,566..567,570..571,575,
                     577..578,584,593)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          526..558
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          560..593
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..638
                     /gene="DZANK1"
                     /gene_synonym="ANKRD64; C20orf12; C20orf84"
                     /coded_by="NM_001367619.1:640..2556"
                     /note="isoform 8 is encoded by transcript variant 13"
                     /db_xref="GeneID:55184"
                     /db_xref="HGNC:HGNC:15858"
                     /db_xref="MIM:620905"
ORIGIN      
        1 mltlesfqrv hwksqlmved qvldhppasp rqdtvpftfk sflfghsmei rpwkrkgrtl
       61 frrllfqspg fahvsgqkcl tsteimriqr etdflkcahc laprpsdpfa rfcqecgspv
      121 ppifgcrlpp pegaqmglca ecrslvpmnt picvvceapl alqlqpqasl hlkekvicra
      181 cgtgnpahlr ycvtcegalp ssqesmcsgd kapppptqkg gtiscyrcgr wnlweasfcg
      241 wcgamlgipa gcsvcpkcga snhlsarfcg scgicvkslv klsldrslal aaeeprpfse
      301 slniplprsd vgtkrdigtq tvglfypsgk llakkeqela sqkqrqekms dhkplltais
      361 pgrgywrrql dhisahlrcy aqnnpefral iaeprmgkli satvhedgce vsirlnysqv
      421 snknlylnka vnfsdhllss aaegdgglcg srsswvsdys qstsdtieki kriknfktkt
      481 fqekkeqlip enrlllkevg ptgegrvsvi eqlldegadp nccdednrpv itvavmnkhh
      541 eaipvlvqrg adidqqwgpl rntalheatl lglagresta tllgcnasiq kknaggqtay
      601 dlalntgddl vtslfaakfg qgledqlaqt rslslddc
//
LOCUS       NP_733749                673 aa            linear   PRI 27-APR-2025
DEFINITION  RAS guanyl-releasing protein 4 isoform a [Homo sapiens].
ACCESSION   NP_733749
VERSION     NP_733749.1
DBSOURCE    REFSEQ: accession NM_170604.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Zhu,L., Xia,C., Wu,L., Zhang,Y., Liu,J., Chen,Y., Liu,J., Xiao,Y.,
            Nie,K., Huang,L., Qu,N. and Yu,H.
  TITLE     The critical role of RasGRP4 in the growth of diffuse large B cell
            lymphoma
  JOURNAL   Cell Commun Signal 17 (1), 92 (2019)
   PUBMED   31409422
  REMARK    GeneRIF: The findings indicate the oncogenic role of RasGRP4 in
            diffuse large B cell lymphoma (DLBCL), suggesting it as a
            prognostic biomarker and potential therapeutic target in DLBCL.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Kono,M., Yasuda,S., Stevens,R.L., Koide,H., Kurita,T., Shimizu,Y.,
            Kanetsuka,Y., Oku,K., Bohgaki,T., Amengual,O., Horita,T.,
            Shimizu,T., Majima,T., Koike,T. and Atsumi,T.
  TITLE     Ras guanine nucleotide-releasing protein 4 is aberrantly expressed
            in the fibroblast-like synoviocytes of patients with rheumatoid
            arthritis and controls their proliferation
  JOURNAL   Arthritis Rheumatol 67 (2), 396-407 (2015)
   PUBMED   25330932
  REMARK    GeneRIF: Ras guanine nucleotide-releasing protein 4 is aberrantly
            expressed in the fibroblast-like synoviocytes of patients with
            rheumatoid arthritis and controls their proliferation.
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Suire,S., Lecureuil,C., Anderson,K.E., Damoulakis,G., Niewczas,I.,
            Davidson,K., Guillou,H., Pan,D., Jonathan,Clark., Phillip,T.
            Hawkins and Stephens,L.
  TITLE     GPCR activation of Ras and PI3Kc in neutrophils depends on PLCb2/b3
            and the RasGEF RasGRP4
  JOURNAL   EMBO J 31 (14), 3118-3129 (2012)
   PUBMED   22728827
  REMARK    GeneRIF: GPCR activation of Ras and PI3Kc in neutrophils depends on
            PLCb2/b3 and the RasGEF RasGRP4.
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Hashimoto,T., Yasuda,S., Koide,H., Kataoka,H., Horita,T., Atsumi,T.
            and Koike,T.
  TITLE     Aberrant splicing of the hRasGRP4 transcript and decreased levels
            of this signaling protein in the peripheral blood mononuclear cells
            in a subset of patients with rheumatoid arthritis
  JOURNAL   Arthritis Res Ther 13 (5), R154 (2011)
   PUBMED   21933395
  REMARK    GeneRIF: Identification of defective isoforms of hRasGRP4
            transcripts in rheumatoid arthritis(RA) patients raises the
            possibility that dysregulated expression of hRasGRP4 in developing
            monocytes plays a pathogenic role in this subset of RA patients.
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Watanabe-Okochi,N., Oki,T., Komeno,Y., Kato,N., Yuji,K., Ono,R.,
            Harada,Y., Harada,H., Hayashi,Y., Nakajima,H., Nosaka,T.,
            Kitaura,J. and Kitamura,T.
  TITLE     Possible involvement of RasGRP4 in leukemogenesis
  JOURNAL   Int J Hematol 89 (4), 470-481 (2009)
   PUBMED   19350351
  REMARK    GeneRIF: RasGRP4 cooperates with AML1 mutations in T cell
            leukemogenesis as a class I mutation
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Katsoulotos,G.P., Qi,M., Qi,J.C., Tanaka,K., Hughes,W.E.,
            Molloy,T.J., Adachi,R., Stevens,R.L. and Krilis,S.A.
  TITLE     The Diacylglycerol-dependent translocation of ras guanine
            nucleotide-releasing protein 4 inside a human mast cell line
            results in substantial phenotypic changes, including expression of
            interleukin 13 receptor alpha2
  JOURNAL   J Biol Chem 283 (3), 1610-1621 (2008)
   PUBMED   18024961
  REMARK    GeneRIF: RasGRP4 translocates to varied intracellular compartments
            via its DAG/PMA-binding domain to regulate signaling pathways that
            control gene and protein expression in MCs, including the cell's
            ability to respond to IL-13.
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Li,L., Yang,Y. and Stevens,R.L.
  TITLE     RasGRP4 regulates the expression of prostaglandin D2 in human and
            rat mast cell lines
  JOURNAL   J Biol Chem 278 (7), 4725-4729 (2003)
   PUBMED   12493770
  REMARK    GeneRIF: RasGRP4 regulates the expression of prostaglandin D2 in
            mast cells
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Reuther,G.W., Lambert,Q.T., Rebhun,J.F., Caligiuri,M.A.,
            Quilliam,L.A. and Der,C.J.
  TITLE     RasGRP4 is a novel Ras activator isolated from acute myeloid
            leukemia
  JOURNAL   J Biol Chem 277 (34), 30508-30514 (2002)
   PUBMED   11880369
  REMARK    GeneRIF: RasGRP4 plays a role in myeloid cell signaling growth
            regulation pathways that are responsive to diacylglycerol levels
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Yang,Y., Li,L., Wong,G.W., Krilis,S.A., Madhusudhan,M.S., Sali,A.
            and Stevens,R.L.
  TITLE     RasGRP4, a new mast cell-restricted Ras guanine
            nucleotide-releasing protein with calcium- and
            diacylglycerol-binding motifs. Identification of defective variants
            of this signaling protein in asthma, mastocytosis, and mast cell
            leukemia patients and demonstration of the importance of RasGRP4 in
            mast cell development and function
  JOURNAL   J Biol Chem 277 (28), 25756-25774 (2002)
   PUBMED   11956218
  REMARK    GeneRIF: identification of defective variants of this signaling
            protein in asthma, mastocytosis, and mast cell leukemia patients
            and demonstration of the importance of RasGRP4 in mast cell
            development and function
            GeneRIF: RasGRP4 is a cation-dependent, guanine nucleotide exchange
            factor and diacylglycerol/phorbol ester receptor that is
            selectively expressed in mast cells and their progenitors.  RasGRP4
            regulates the final stages of mast cell development.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY048119.1, AF448437.1,
            AC011469.6, AC005789.1 and BQ028385.1.
            
            Summary: The protein encoded by this gene is a member of the Ras
            guanyl nucleotide-releasing protein (RasGRP) family of Ras guanine
            nucleotide exchange factors. It contains a Ras exchange motif, a
            diacylglycerol-binding domain, and two calcium-binding EF hands.
            This protein was shown to activate H-Ras in a cation-dependent
            manner in vitro. Expression of this protein in myeloid cell lines
            was found to be correlated with elevated level of activated RAS
            protein, and the RAS activation can be greatly enhanced by phorbol
            ester treatment, which suggested a role of this protein in
            diacylglycerol regulated cell signaling pathways. Studies of a mast
            cell leukemia cell line expressing substantial amounts of abnormal
            transcripts of this gene indicated that this gene may play an
            important role in the final stages of mast cell development.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Apr 2009].
            
            Transcript Variant: This variant (a) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF448437.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000615439.5/ ENSP00000479844.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..673
                     /product="RAS guanyl-releasing protein 4 isoform a"
                     /note="guanyl nucleotide releasing protein 4"
                     /calculated_mol_wt=74752
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDF6.2)"
     Region          57..164
                     /region_name="REM"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     GTPases; N-terminal domain (RasGef_N), also called REM
                     domain (Ras exchanger motif). This domain is common in
                     nucleotide exchange factors for Ras-like small GTPases and
                     is typically found immediately...; cd06224"
                     /db_xref="CDD:100121"
     Site            order(68,115,119..120,123,126..127,162..163)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:100121"
     Region          160..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDF6.2)"
     Region          197..432
                     /region_name="RasGEF"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     small GTPases; smart00147"
                     /db_xref="CDD:214539"
     Site            order(230..232,240..241,243..245,247..248,251..252,255,
                     288,291..292,294..296,298..301,303..304,324,327,332..334,
                     337,350..352,355..357,359..361,363..366,381,385,420,
                     423..424)
                     /site_type="other"
                     /note="Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:238087"
     Region          538..594
                     /region_name="C1_RASGRP4"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in RAS guanyl-releasing protein 4 (RASGRP4) and
                     similar proteins; cd20863"
                     /db_xref="CDD:410413"
     Site            order(546..552,560..564,567)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410413"
     Region          593..621
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDF6.2)"
     Region          639..673
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDF6.2)"
     CDS             1..673
                     /gene="RASGRP4"
                     /coded_by="NM_170604.3:129..2150"
                     /note="isoform a is encoded by transcript variant a"
                     /db_xref="CCDS:CCDS46068.1"
                     /db_xref="GeneID:115727"
                     /db_xref="HGNC:HGNC:18958"
                     /db_xref="MIM:607320"
ORIGIN      
        1 mnrkdskrks hqectgkigg rgrprqvrrh ktcpspreis kvmasmnlgl lseggcsede
       61 llekciqsfd sagslchedh mlnmvlamhs wvlpsadlaa rlltsyqkat gdtqelrrlq
      121 ichlvrywlm rhpevmhqdp qleevigrfw atvaregnsa qrrlgdssdl lspggpgppl
      181 pmsspglgkk rkvsllfdhl etgelaqhlt ylefrsfqai tpqdlrsyvl qgsvrgcpal
      241 egsvglsnsv srwvqvmvls rpgplqraqv ldkfihvaqr lhqlqnfntl mavtgglchs
      301 aisrlkdsha hlspdstkal leltellash nnyaryrrtw agcagfrlpv lgvhlkdlvs
      361 lheaqpdrlp dgrlhlpkln nlylrlqelv alqgqhppcs anedllhllt lsldlfyted
      421 eiyelsyare prcpkslpps pfnaplvvew apgvtpkpdr vtlgrhveql vesvfknydp
      481 egrgtisqed ferlsgnfpf achglhpppr qgrgsfsree ltgyllrasa icsklglafl
      541 htfhevtfrk ptfcdscsgf lwgvtkqgyr crecglcchk hcrdqvkvec kkrpgakgda
      601 gppgapvpst paphascgse enhsytlsle petgcqlrha wtqtesphps wetdtvpcpv
      661 mdppstassk lds
//
LOCUS       NP_056414                542 aa            linear   PRI 27-APR-2025
DEFINITION  phosphoacetylglucosamine mutase isoform 2 [Homo sapiens].
ACCESSION   NP_056414
VERSION     NP_056414.1
DBSOURCE    REFSEQ: accession NM_015599.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Jacob,M., Masood,A. and Abdel Rahman,A.M.
  TITLE     Multi-Omics Profiling in PGM3 and STAT3 Deficiencies: A Tale of Two
            Patients
  JOURNAL   Int J Mol Sci 24 (3), 2406 (2023)
   PUBMED   36768728
  REMARK    GeneRIF: Multi-Omics Profiling in PGM3 and STAT3 Deficiencies: A
            Tale of Two Patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Zhang,N., Liu,S., Xu,J., Ning,T., Xie,S., Min,L., Zhu,S., Zhang,S.
            and Zhu,S.
  TITLE     PGM3 regulates beta-catenin activity to promote colorectal cancer
            cell progression
  JOURNAL   Exp Biol Med (Maywood) 247 (17), 1518-1528 (2022)
   PUBMED   35723049
  REMARK    GeneRIF: PGM3 regulates beta-catenin activity to promote colorectal
            cancer cell progression.
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Lee,H., Cai,F., Kelekar,N., Velupally,N.K. and Kim,J.
  TITLE     Targeting PGM3 as a Novel Therapeutic Strategy in KRAS/LKB1
            Co-Mutant Lung Cancer
  JOURNAL   Cells 11 (1), 176 (2022)
   PUBMED   35011738
  REMARK    GeneRIF: Targeting PGM3 as a Novel Therapeutic Strategy in
            KRAS/LKB1 Co-Mutant Lung Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Pang,H., Amano,S., Inagaki,Y., Okamoto,T., Yamada,K., Kimura,H.,
            Koda,Y. and Yamagishi,S.I.
  TITLE     N-acetylglucosamine-phosphate mutase genotype and diabetic
            microvascular complications
  JOURNAL   Diabet Med 20 (5), 419-420 (2003)
   PUBMED   12752494
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Pang,H., Koda,Y., Soejima,M. and Kimura,H.
  TITLE     Identification of human phosphoglucomutase 3 (PGM3) as
            N-acetylglucosamine-phosphate mutase (AGM1)
  JOURNAL   Ann Hum Genet 66 (Pt 2), 139-144 (2002)
   PUBMED   12174217
  REMARK    GeneRIF: PGM(3) is identical to AGM(1).
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Mio,T., Yamada-Okabe,T., Arisawa,M. and Yamada-Okabe,H.
  TITLE     Functional cloning and mutational analysis of the human cDNA for
            phosphoacetylglucosamine mutase: identification of the amino acid
            residues essential for the catalysis
  JOURNAL   Biochim Biophys Acta 1492 (2-3), 369-376 (2000)
   PUBMED   11004509
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Li,C., Rodriguez,M. and Banerjee,D.
  TITLE     Cloning and characterization of complementary DNA encoding human
            N-acetylglucosamine-phosphate mutase protein
  JOURNAL   Gene 242 (1-2), 97-103 (2000)
   PUBMED   10721701
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Yoshida,H., Abe,T. and Nakamura,F.
  TITLE     Studies on the frequencies of PGM1, PGM3 and Es-D types from hair
            roots in Japanese subjects and the determination of these types
            from old hair roots
  JOURNAL   Forensic Sci Int 14 (1), 1-7 (1979)
   PUBMED   468082
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Chen,S.H., Anderson,J.E., Giblett,E.R. and Stamatoyannopoulos,G.
  TITLE     Isozyme patterns in erythrocytes from human fetuses
  JOURNAL   Am J Hematol 3, 23-28 (1977)
   PUBMED   203189
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB004046.1, AF180371.1 and
            AL121716.16.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the phosphohexose mutase
            family. The encoded protein mediates both glycogen formation and
            utilization by catalyzing the interconversion of
            glucose-1-phosphate and glucose-6-phosphate. A non-synonymous
            single nucleotide polymorphism in this gene may play a role in
            resistance to diabetic nephropathy and neuropathy. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) has a distinct N-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.156420.1,
                                           SRR1803614.231276.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000513973.6/ ENSP00000424874.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..542
                     /product="phosphoacetylglucosamine mutase isoform 2"
                     /EC_number="5.4.2.3"
                     /note="acetylglucosamine phosphomutase;
                     phosphoacetylglucosamine mutase;
                     N-acetylglucosamine-phosphate mutase 1"
                     /calculated_mol_wt=59721
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (O95394.1)"
     Region          22..527
                     /region_name="PGM3"
                     /note="PGM3 (phosphoglucomutase 3), also known as PAGM
                     (phosphoacetylglucosamine mutase) and AGM1
                     (N-acetylglucosamine-phosphate mutase), is an essential
                     enzyme found in eukaryotes that reversibly catalyzes the
                     conversion of GlcNAc-6-phosphate into...; cd03086"
                     /db_xref="CDD:100088"
     Site            order(29,64..65,276,278,280..281,351..353,370,372,374,496,
                     498..500,505)
                     /site_type="active"
                     /db_xref="CDD:100088"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95394.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O95394.1)"
     Site            order(276,278,280)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100088"
     Site            order(351..353,370,372,374,496,498..500,505)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100088"
     CDS             1..542
                     /gene="PGM3"
                     /gene_synonym="AGM1; IMD23; PAGM; PGM 3"
                     /coded_by="NM_015599.3:90..1718"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4997.1"
                     /db_xref="GeneID:5238"
                     /db_xref="HGNC:HGNC:8907"
                     /db_xref="MIM:172100"
ORIGIN      
        1 mdlgaitkys alhakpngli lqygtagfrt kaehldhvmf rmgllavlrs kqtkstigvm
       61 vtashnpeed ngvklvdplg emlapsweeh atclanaeeq dmqrvlidis ekeavnlqqd
      121 afvvigrdtr psseklsqsv idgvtvlggq fhdygllttp qlhymvycrn tggrygkati
      181 egyyqklska fveltkqasc sgdeyrslkv dcangigalk lremehyfsq glsvqlfndg
      241 skgklnhlcg adfvkshqkp pqgmeiksne rccsfdgdad rivyyyhdad ghfhlidgdk
      301 iatlissflk ellveigesl nigvvqtaya ngsstrylee vmkvpvyctk tgvkhlhhka
      361 qefdigvyfe anghgtalfs tavemkikqs aeqledkkrk aakmleniid lfnqaagdai
      421 sdmlvieail alkgltvqqw dalytdlpnr qlkvqvadrr visttdaerq avtppglqea
      481 indlvkkykl srafvrpsgt edvvrvyaea dsqesadhla hevslavfql aggigerpqp
      541 gf
//
LOCUS       NP_775751                555 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 57 isoform 1 [Homo sapiens].
ACCESSION   NP_775751
VERSION     NP_775751.1
DBSOURCE    REFSEQ: accession NM_173480.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Wang,H., Sica,R.A., Kaur,G., Galbo,P.M. Jr., Jing,Z.,
            Nishimura,C.D., Ren,X., Tanwar,A., Etemad-Gilbertson,B., Will,B.,
            Zheng,D., Fooksman,D. and Zang,X.
  TITLE     TMIGD2 is an orchestrator and therapeutic target on human acute
            myeloid leukemia stem cells
  JOURNAL   Nat Commun 15 (1), 11 (2024)
   PUBMED   38167704
  REMARK    GeneRIF: TMIGD2 is an orchestrator and therapeutic target on human
            acute myeloid leukemia stem cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Liu,W., Yuan,W., Li,X., Zhuang,J., Mo,X., Dai,G., Wang,Y., Chen,J.,
            Wan,Y., Li,Y., Zhu,X., Chen,Y., Luo,S., Jiang,Z., Shi,Y., Chen,F.,
            Cao,L., Ye,X., Fan,X., Zhu,P., Zhang,K. and Wu,X.
  TITLE     ZNF424 Induces Apoptosis and Inhibits Proliferation in Lung
            Carcinoma Cells
  JOURNAL   Curr Mol Med 18 (2), 109-115 (2018)
   PUBMED   29974829
  REMARK    GeneRIF: These are the first data to associate ZNF424 with
            tumorigenesis and demonstrate an inhibitory role in lung cancer,
            indicating the potential of ZNF424 expression as a diagnostic
            marker of lung tumorigenesis.
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Wang,Y., Zhou,J., Ye,X., Wan,Y., Li,Y., Mo,X., Yuan,W., Yan,Y.,
            Luo,N., Wang,Z., Fan,X., Deng,Y. and Wu,X.
  TITLE     ZNF424, a novel human KRAB/C2H2 zinc finger protein, suppresses
            NFAT and p21 pathway
  JOURNAL   BMB Rep 43 (3), 212-218 (2010)
   PUBMED   20356463
  REMARK    GeneRIF: ZNF424 protein may act as a transcriptional repressor that
            suppresses NFAT and p21 pathway to mediate cellular functions.
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Lichter,P., Bray,P., Ried,T., Dawid,I.B. and Ward,D.C.
  TITLE     Clustering of C2-H2 zinc finger motif sequences within telomeric
            and fragile site regions of human chromosomes
  JOURNAL   Genomics 13 (4), 999-1007 (1992)
   PUBMED   1505991
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Bray,P., Lichter,P., Thiesen,H.J., Ward,D.C. and Dawid,I.B.
  TITLE     Characterization and mapping of human genes encoding zinc finger
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 88 (21), 9563-9567 (1991)
   PUBMED   1946370
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EF534355.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF534355.1, SRR3476690.631813.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306908.10/ ENSP00000303696.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..555
                     /product="zinc finger protein 57 isoform 1"
                     /note="zinc finger protein 424"
                     /calculated_mol_wt=64297
     Region          3..44
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          118..134
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          171..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <180..469
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(259,261,263,265..266,269..270,273,287,289,293..294,
                     297..298,301,315,317,319,321..322,325..326,329)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          422..442
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          450..470
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(455,457,459,461..462,465..466,469,483,485,489..490,
                     493..494,497,511,513,515,517..518,521..522,525)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          478..498
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          494..514
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          506..526
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..555
                     /gene="ZNF57"
                     /gene_synonym="ZNF424"
                     /coded_by="NM_173480.3:119..1786"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12098.1"
                     /db_xref="GeneID:126295"
                     /db_xref="HGNC:HGNC:13125"
ORIGIN      
        1 mdsvvfedva vdftleewal ldsaqrdlyr dvmletfrnl asvddgtqfk angsvslqdm
       61 ygqekskeqt ipnftgnnsc aytleknceg ygtedhhknl rnhmvdrfct hnegnqygea
      121 ihqmpdltlh kkvsagekpy ectkcrtvft hlsslkrhvk shcgrkappg eeckqacicp
      181 shlhshgrtd teekpykcqa cgqtfqhpry lshhvkthta ektykceqcr mafngfasft
      241 rhvrthtkdr pykcqecgra fiypstfqrh mtthtgekpy kcqhcgkaft ypqafqrhek
      301 thtgekpyec kqcgktfsws etlrvhmrih tgdklykceh cgkaftssrs fqghlrthtg
      361 ekpyeckqcg kaftwsstfr ehvrihtqeq lykceqcgka ftssrsfrgh lrthtgekpy
      421 eckqcgktft wsstfrehvr ihtqeqlhkc ehcgkaftss rafqghlrmh tgekpyeckq
      481 cgktftwsst lhnhvrmhtg ekphkckqcg msfkwhssfr nhlrmhtgqk shecqsyska
      541 fscqvilskt sesth
//
LOCUS       NP_001020273             276 aa            linear   ROD 27-APR-2025
DEFINITION  ARL14 effector protein [Mus musculus].
ACCESSION   NP_001020273
VERSION     NP_001020273.1
DBSOURCE    REFSEQ: accession NM_001025102.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Sansom,S.N., Griffiths,D.S., Faedo,A., Kleinjan,D.J., Ruan,Y.,
            Smith,J., van Heyningen,V., Rubenstein,J.L. and Livesey,F.J.
  TITLE     The level of the transcription factor Pax6 is essential for
            controlling the balance between neural stem cell self-renewal and
            neurogenesis
  JOURNAL   PLoS Genet 5 (6), e1000511 (2009)
   PUBMED   19521500
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX649348.8 and BX890640.4.
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 3. All four variants encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC054106.2, AK134965.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164135 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 55.97 cM"
     Protein         1..276
                     /product="ARL14 effector protein"
                     /note="ARF7 effector protein"
                     /calculated_mol_wt=30880
     Region          145..248
                     /region_name="ARF7EP_C"
                     /note="ARF7 effector protein C-terminus; pfam14949"
                     /db_xref="CDD:464395"
     Region          158..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BIX3.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N8R7; propagated from
                     UniProtKB/Swiss-Prot (Q8BIX3.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355; propagated from
                     UniProtKB/Swiss-Prot (Q8BIX3.1)"
     CDS             1..276
                     /gene="Arl14ep"
                     /gene_synonym="2700007P21Rik; 4930448O08Rik; ARF7EP"
                     /coded_by="NM_001025102.2:191..1021"
                     /db_xref="CCDS:CCDS16503.1"
                     /db_xref="GeneID:212772"
                     /db_xref="MGI:MGI:1926020"
ORIGIN      
        1 mdpcsvgvql rtthdchktf ytrhtgfktl kelssndmll lqlrtgmtls gnnticlhhv
       61 kiyidrfedl qksccdpfni hkklakknlh vidlddatfl sakfgrqlvp gwklcpkctq
      121 iingsvdvds ddrqrrkpds dgrtakalrs lqftnpgkqt efapeggkre krkltkatsa
      181 asdrqiipak skvydsqgll ifsgmdlcdc ldedclgcfy acptcgstkc gaecrcdrkw
      241 lyeqieiegg eiihnkhagk aygllspchp ydilqk
//
LOCUS       NP_001348196             485 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF14 isoform a [Mus musculus].
ACCESSION   NP_001348196 XP_006526187
VERSION     NP_001348196.1
DBSOURCE    REFSEQ: accession NM_001361267.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Ingham,A.B., Osborne,S.A., Menzies,M., Briscoe,S., Chen,W.,
            Kongsuwan,K., Reverter,A., Jeanes,A., Dalrymple,B.P., Wijffels,G.,
            Seymour,R. and Hudson,N.J.
  TITLE     RNF14 is a regulator of mitochondrial and immune function in muscle
  JOURNAL   BMC Syst Biol 8, 10 (2014)
   PUBMED   24472305
  REMARK    GeneRIF: RNF14 influences the expression of both mitochondrial and
            immune related genes
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Grimont,A., Bloch-Faure,M., El Abida,B. and Crambert,G.
  TITLE     Mapping of sex hormone receptors and their modulators along the
            nephron of male and female mice
  JOURNAL   FEBS Lett 583 (10), 1644-1648 (2009)
   PUBMED   19401201
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   7  (residues 1 to 485)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
REFERENCE   8  (residues 1 to 485)
  AUTHORS   van der Reijden,B.A., Erpelinck-Verschueren,C.A., Lowenberg,B. and
            Jansen,J.H.
  TITLE     TRIADs: a new class of proteins with a novel cysteine-rich
            signature
  JOURNAL   Protein Sci 8 (7), 1557-1561 (1999)
   PUBMED   10422847
REFERENCE   9  (residues 1 to 485)
  AUTHORS   Kang,H.Y., Yeh,S., Fujimoto,N. and Chang,C.
  TITLE     Cloning and characterization of human prostate coactivator ARA54, a
            novel protein that associates with the androgen receptor
  JOURNAL   J Biol Chem 274 (13), 8570-8576 (1999)
   PUBMED   10085091
REFERENCE   10 (residues 1 to 485)
  AUTHORS   Brady,K.P., Rowe,L.B., Her,H., Stevens,T.J., Eppig,J.,
            Sussman,D.J., Sikela,J. and Beier,D.R.
  TITLE     Genetic mapping of 262 loci derived from expressed sequences in a
            murine interspecific cross using single-strand conformational
            polymorphism analysis
  JOURNAL   Genome Res 7 (11), 1085-1093 (1997)
   PUBMED   9371744
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC152450.4.
            
            On Mar 13, 2018 this sequence version replaced XP_006526187.1.
            
            Transcript Variant: This variant (7) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 4 through 9 encode the same
            isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK011316.2, SRR1660819.13220.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 20.2 cM"
     Protein         1..485
                     /product="E3 ubiquitin-protein ligase RNF14 isoform a"
                     /EC_number="2.3.2.31"
                     /note="TRIAD2 type I; E3 ubiquitin-protein ligase RNF14;
                     protein Triad2; androgen receptor-associated protein 54"
                     /calculated_mol_wt=54795
     Region          9..135
                     /region_name="RWD_RNF14"
                     /note="RWD domain of RING finger protein 14 (RNF14) and
                     related proteins; cd23820"
                     /db_xref="CDD:467656"
     Region          37..45
                     /region_name="D-box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JI90.2)"
     Region          214..272
                     /region_name="RING-HC_RBR_RNF14"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 14 (RNF14) and similar proteins; cd16628"
                     /db_xref="CDD:438290"
     Region          217..458
                     /region_name="TRIAD supradomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JI90.2)"
     Region          301..357
                     /region_name="BRcat_RBR_RNF14"
                     /note="BRcat domain found in RING finger protein 14
                     (RNF14); cd20341"
                     /db_xref="CDD:439002"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBS8; propagated from
                     UniProtKB/Swiss-Prot (Q9JI90.2)"
     Region          390..457
                     /region_name="Rcat_RBR_RNF14"
                     /note="Rcat domain found in RING finger protein 14
                     (RNF14); cd20354"
                     /db_xref="CDD:439015"
     CDS             1..485
                     /gene="Rnf14"
                     /gene_synonym="2310075C09Rik; 2610005D23Rik; D18Ertd188e;
                     D7Bwg0165e; Triad2"
                     /coded_by="NM_001361267.1:422..1879"
                     /note="isoform a is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS29200.1"
                     /db_xref="GeneID:56736"
                     /db_xref="MGI:MGI:1929668"
ORIGIN      
        1 msaedleaqe dellalasiy dadefrkaes vqggetriyl dlpqnfkifv sgnsneslqn
       61 sgfeyticfl pplvlnfelp pdypssspps ftlsgkwlsp tqlsalckhl dnlweehrgr
      121 vvlfawmqfl keetltylni vspfelkmgs qkkvqrrata qassstelgv ggaaaadvdq
      181 eetvderavq dveslssliq eildfnqarq tkcfnsklfl csicfceklg sdcmyfleck
      241 hvyckaclkd yfeiqikdgq vkclncpepq cpsvatpgqv kelveadlfa rydrlllqst
      301 ldlmadvvyc prpccqlpvm qepggtmaic sscnfafctl crltyhglsp ckvtaeklid
      361 lrneylqade atkrfleqry gkrviqkale emeskdwlek nskscpccgt piqkldgcnk
      421 mtctgcmqyf cwicmgslsr anpyrhftds espcfnrlfh avdingdmwe deieedddde
      481 ddddd
//
LOCUS       NP_776245                170 aa            linear   PRI 27-APR-2025
DEFINITION  tubulin polymerization-promoting protein family member 2 [Homo
            sapiens].
ACCESSION   NP_776245
VERSION     NP_776245.2
DBSOURCE    REFSEQ: accession NM_173846.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Zhu,F., Yan,P., Zhang,J., Cui,Y., Zheng,M., Cheng,Y., Guo,Y.,
            Yang,X., Guo,X. and Zhu,H.
  TITLE     Deficiency of TPPP2, a factor linked to oligoasthenozoospermia,
            causes subfertility in male mice
  JOURNAL   J Cell Mol Med 23 (4), 2583-2594 (2019)
   PUBMED   30680919
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Vincze,O., Tokesi,N., Olah,J., Hlavanda,E., Zotter,A., Horvath,I.,
            Lehotzky,A., Tirian,L., Medzihradszky,K.F., Kovacs,J., Orosz,F. and
            Ovadi,J.
  TITLE     Tubulin polymerization promoting proteins (TPPPs): members of a new
            family with distinct structures and functions
  JOURNAL   Biochemistry 45 (46), 13818-13826 (2006)
   PUBMED   17105200
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Lindersson,E., Lundvig,D., Petersen,C., Madsen,P., Nyengaard,J.R.,
            Hojrup,P., Moos,T., Otzen,D., Gai,W.P., Blumbergs,P.C. and
            Jensen,P.H.
  TITLE     p25alpha Stimulates alpha-synuclein aggregation and is co-localized
            with aggregated alpha-synuclein in alpha-synucleinopathies
  JOURNAL   J Biol Chem 280 (7), 5703-5715 (2005)
   PUBMED   15590652
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB458250.1, BC038970.2, AW135537.1 and AL161668.6.
            
            On Apr 10, 2009 this sequence version replaced NP_776245.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.146997.1,
                                           SRR5189667.197413.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321760.11/ ENSP00000317595.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..170
                     /product="tubulin polymerization-promoting protein family
                     member 2"
                     /note="TPPP/p18; protein p25-beta"
                     /calculated_mol_wt=18372
     Region          6..161
                     /region_name="p25-alpha"
                     /note="pfam05517"
                     /db_xref="CDD:461670"
     Region          127..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59282.2)"
     CDS             1..170
                     /gene="TPPP2"
                     /gene_synonym="C14orf8; CT152; P18; p25beta"
                     /coded_by="NM_173846.5:158..670"
                     /db_xref="CCDS:CCDS9566.1"
                     /db_xref="GeneID:122664"
                     /db_xref="HGNC:HGNC:19293"
                     /db_xref="MIM:616956"
ORIGIN      
        1 maseaektfh rfaafgesss sgtemnnknf sklckdcgim dgktvtstdv divfskvkak
       61 nartitfqqf keavkelgqk rfkgkspdev leniyglmeg kdpattgatk attvgavdrl
      121 tdtskytgth kerfdesgkg kgiagreemt dntgyvsgyk gsgtydkktk
//
LOCUS       NP_690004                628 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 555 isoform 1 [Homo sapiens].
ACCESSION   NP_690004
VERSION     NP_690004.4
DBSOURCE    REFSEQ: accession NM_152791.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Kim,E., Rich,J., Karoutas,A., Tarlykov,P., Cochet,E., Malysheva,D.,
            Mamchaoui,K., Ogryzko,V. and Pirozhkova,I.
  TITLE     ZNF555 protein binds to transcriptional activator site of 4qA
            allele and ANT1: potential implication in Facioscapulohumeral
            dystrophy
  JOURNAL   Nucleic Acids Res 43 (17), 8227-8242 (2015)
   PUBMED   26184877
  REMARK    GeneRIF: Identification of ZNF555 as a putative transcriptional
            factor highly expressed in human primary myoblasts that interacts
            with the beta-satellite repeats enhancer site and impacts the ANT1
            promoter activity in facioscapulohumeral dystrophy myoblasts.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006130.2.
            
            On Feb 27, 2010 this sequence version replaced NP_690004.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.237165.1, AL832140.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334241.9/ ENSP00000334853.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..628
                     /product="zinc finger protein 555 isoform 1"
                     /calculated_mol_wt=72954
     Region          3..44
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          149..166
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          174..194
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..595
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          202..222
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          230..250
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          258..278
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(263,265,267,269..270,273..274,277,291,293,297..298,
                     301..302,305,319,321,323,325..326,329..330,333)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          286..306
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          314..334
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          342..362
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          370..390
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(375,377,379,381..382,385..386,389,403,405,409..410,
                     413..414,417,431,433,435,437..438,441..442,445)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          398..418
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          426..446
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          454..474
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          482..502
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          510..530
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(515,517,519,521..522,525..526,529,543,545,549..550,
                     553..554,557,571,573,575,577..578,581..582,585)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          538..558
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          566..586
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..628
                     /gene="ZNF555"
                     /coded_by="NM_152791.5:99..1985"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12096.1"
                     /db_xref="GeneID:148254"
                     /db_xref="HGNC:HGNC:28382"
ORIGIN      
        1 mdsvvfedva vdftleewal ldsaqrdlyr dvmletfqnl asvddetqfk asgsvsqqdi
       61 ygekipkesk iatftrnvsw asvlgkiwds lsiedqttnq grnlsrnhgl erlcesndqc
      121 gealsqiphl nlykkippgv kqyeyntygk vfmhrrtslk spitvhtghk pyqcqecgqa
      181 yscrshlrmh vrthngerpy vcklcgktfp rtsslnrhvr ihtaektyec kqcgkafidf
      241 ssltshlrsh tgekpykcke cgkafsysst frrhtithtg ekpykckeca eafsysstfr
      301 rhmishtgek phkckecgea fsyssafrrh mithtgekpy eckqcgktfi ylqsfrrher
      361 ihtgekpyec kqcgktfiyp qsfrrherth ggekpyecnq cgkafshpss frghmrvhtg
      421 ekpyeckqcg ktfnwpislr khmrthtrek pyeckqcgka fslsacfreh vrmhpedksy
      481 ecklcgkafy chislqkhmr rhtaeklykc kqcgkafswp ellqqhvrth tvekpyecke
      541 cgkvfkwpss lpihmrlhtg ekpyqckhcg kafncssslr rhvrihttek qykcnvghpp
      601 anefmcsase kshqerdlik vvnmvlpl
//
LOCUS       NP_005697                329 aa            linear   PRI 27-APR-2025
DEFINITION  U5 small nuclear ribonucleoprotein TSSC4 isoform a [Homo sapiens].
ACCESSION   NP_005697 XP_005252779
VERSION     NP_005697.2
DBSOURCE    REFSEQ: accession NM_005706.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Bergfort,A., Hilal,T., Kuropka,B., Ilik,I.A., Weber,G., Aktas,T.,
            Freund,C. and Wahl,M.C.
  TITLE     The intrinsically disordered TSSC4 protein acts as a helicase
            inhibitor, placeholder and multi-interaction coordinator during
            snRNP assembly and recycling
  JOURNAL   Nucleic Acids Res 50 (5), 2938-2958 (2022)
   PUBMED   35188580
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Klimesova,K., Vojackova,J., Radivojevic,N., Vandermoere,F.,
            Bertrand,E., Verheggen,C. and Stanek,D.
  TITLE     TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation
  JOURNAL   Nat Commun 12 (1), 3646 (2021)
   PUBMED   34131137
  REMARK    GeneRIF: TSSC4 is a component of U5 snRNP that promotes tri-snRNP
            formation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Paulsen,M., El-Maarri,O., Engemann,S., Strodicke,M., Franck,O.,
            Davies,K., Reinhardt,R., Reik,W. and Walter,J.
  TITLE     Sequence conservation and variability of imprinting in the
            Beckwith-Wiedemann syndrome gene cluster in human and mouse
  JOURNAL   Hum Mol Genet 9 (12), 1829-1841 (2000)
   PUBMED   10915772
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Lee,M.P., Brandenburg,S., Landes,G.M., Adams,M., Miller,G. and
            Feinberg,A.P.
  TITLE     Two novel genes in the center of the 11p15 imprinted domain escape
            genomic imprinting
  JOURNAL   Hum Mol Genet 8 (4), 683-690 (1999)
   PUBMED   10072438
  REMARK    GeneRIF: TSSC4 gene, located in the center of the 11p15 imprinted
            region, escapes genomic imprinting.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC050616.1, BC006091.1,
            AC124057.12 and AF125568.1.
            
            On or before Jul 10, 2014 this sequence version replaced
            XP_005252779.1, NP_005697.1.
            
            Summary: This gene is one of several tumor-suppressing
            subtransferable fragments located in the imprinted gene domain of
            11p15.5, an important tumor-suppressor gene region. Alterations in
            this region have been associated with the Beckwith-Wiedemann
            syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma,
            and lung, ovarian, and breast cancer. This gene is located among
            several imprinted genes; however, this gene, as well as the
            pan-hematopoietic expression gene (PHEMX), escapes imprinting. This
            gene may play a role in malignancies and disease that involve this
            region. Several transcript variants encoding two different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, and 4 all encode the same isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.286738.1,
                                           SRR3476690.966954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000333256.11/ ENSP00000331087.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..329
                     /product="U5 small nuclear ribonucleoprotein TSSC4 isoform
                     a"
                     /note="protein TSSC4; tumor-suppressing STF cDNA 4
                     protein; tumor-suppressing subchromosomal transferable
                     fragment candidate gene 4 protein; U5 small nuclear
                     ribonucleoprotein TSSC4"
                     /calculated_mol_wt=34194
     Region          1..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHE7; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHE7; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Region          77..104
                     /region_name="Hom2, mediates interaction with the U5 snRNP
                     complexes and required for spliceosomal tri-snRNP complex
                     assembly. /evidence=ECO:0000269|PubMed:34131137"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Region          94..210
                     /region_name="TSSC4"
                     /note="Tumour suppressing sub-chromosomal transferable
                     candidate 4; pfam15264"
                     /db_xref="CDD:434584"
     Region          104..156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Region          149..316
                     /region_name="Interaction with SNRNP200.
                     /evidence=ECO:0000269|PubMed:35188580"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Region          150..186
                     /region_name="Hom3, mediates interaction with the U5 snRNP
                     complexes. /evidence=ECO:0000269|PubMed:34131137"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Region          201..250
                     /region_name="Hom4, necessary for interaction with the
                     PRPF19 complex and required for spliceosomal tri-snRNP
                     complex assembly. /evidence=ECO:0000269|PubMed:34131137"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Site            217
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Region          221..329
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5U2.3)"
     CDS             1..329
                     /gene="TSSC4"
                     /coded_by="NM_005706.4:230..1219"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS7735.1"
                     /db_xref="GeneID:10078"
                     /db_xref="HGNC:HGNC:12386"
                     /db_xref="MIM:603852"
ORIGIN      
        1 maeagtgeps psvegehgte ydtlpsdtvs lsdsdsdlsl pggaeveals pmglpgeeds
       61 gpdeppspps gllpatvqpf hlrgmsstfs qrsrdifdcl egaarrapss vahtsmsdng
      121 gfkrplapsg rspveglgra hrspasprvp pvpdyvahpe rwtkysledv tevseqsnqa
      181 talaflgsqs laaptdcvss fnqdpsscge grviftkpvr gvearherkr vlgkvgepgr
      241 gglgnpatdr gegpvelahl agpgspeaee wgshhgglqe vealsgsvhs gsvpglppve
      301 tvgfhgsrkr srdhfrnkss spedpgaev
//
LOCUS       NP_002052                274 aa            linear   PRI 27-APR-2025
DEFINITION  glutamate--cysteine ligase regulatory subunit isoform 1 [Homo
            sapiens].
ACCESSION   NP_002052
VERSION     NP_002052.1
DBSOURCE    REFSEQ: accession NM_002061.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Da,D., Pan,Z., Zeng,L., Dang,Y., Dang,C., Huang,Y., Shi,D. and
            Li,H.
  TITLE     Glutamate-cysteine ligase catalytic and its modifier function as
            novel immunotargets in gastric adenocarcinoma
  JOURNAL   Asian J Surg 46 (1), 143-149 (2023)
   PUBMED   35241341
  REMARK    GeneRIF: Glutamate-cysteine ligase catalytic and its modifier
            function as novel immunotargets in gastric adenocarcinoma.
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Yang,C., Xi,M., Liu,H., Bai,H., Jiang,C., Liu,Q. and Fan,P.
  TITLE     Association of Polymorphisms of Glutamate Cysteine Ligase Genes
            GCLC C-129 T and GCLM C-588 T with Risk of Polycystic Ovary
            Syndrome in Chinese Women
  JOURNAL   Reprod Sci 29 (6), 1790-1800 (2022)
   PUBMED   34642912
  REMARK    GeneRIF: Association of Polymorphisms of Glutamate Cysteine Ligase
            Genes GCLC C-129 T and GCLM C-588 T with Risk of Polycystic Ovary
            Syndrome in Chinese Women.
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Mazloomi,S., Khodadadi,I., Alizadeh,N. and Shafiee,G.
  TITLE     Association of glutamate cystein ligase (GCL) activity
            Peroxiredoxin 4 (prxR4) and apelin levels in women with
            preeclampsia
  JOURNAL   Pregnancy Hypertens 23, 163-168 (2021)
   PUBMED   33421846
  REMARK    GeneRIF: Association of glutamate cystein ligase (GCL) activity
            Peroxiredoxin 4 (prxR4) and apelin levels in women with
            preeclampsia.
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Azarova,I., Klyosova,E., Lazarenko,V., Konoplya,A. and Polonikov,A.
  TITLE     Genetic variants in glutamate cysteine ligase confer protection
            against type 2 diabetes
  JOURNAL   Mol Biol Rep 47 (8), 5793-5805 (2020)
   PUBMED   32715377
  REMARK    GeneRIF: Genetic variants in glutamate cysteine ligase confer
            protection against type 2 diabetes.
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Misra,I. and Griffith,O.W.
  TITLE     Expression and purification of human gamma-glutamylcysteine
            synthetase
  JOURNAL   Protein Expr Purif 13 (2), 268-276 (1998)
   PUBMED   9675072
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Sierra-Rivera,E., Dasouki,M., Summar,M.L., Krishnamani,M.R.,
            Meredith,M., Rao,P.N., Phillips,J.A. 3rd and Freeman,M.L.
  TITLE     Assignment of the human gene (GLCLR) that encodes the regulatory
            subunit of gamma-glutamylcysteine synthetase to chromosome 1p21
  JOURNAL   Cytogenet Cell Genet 72 (2-3), 252-254 (1996)
   PUBMED   8978789
REFERENCE   8  (residues 1 to 274)
  AUTHORS   Tsuchiya,K., Mulcahy,R.T., Reid,L.L., Disteche,C.M. and
            Kavanagh,T.J.
  TITLE     Mapping of the glutamate-cysteine ligase catalytic subunit gene
            (GLCLC) to human chromosome 6p12 and mouse chromosome 9D-E and of
            the regulatory subunit gene (GLCLR) to human chromosome 1p21-p22
            and mouse chromosome 3H1-3
  JOURNAL   Genomics 30 (3), 630-632 (1995)
   PUBMED   8825659
REFERENCE   9  (residues 1 to 274)
  AUTHORS   Gipp,J.J., Bailey,H.H. and Mulcahy,R.T.
  TITLE     Cloning and sequencing of the cDNA for the light subunit of human
            liver gamma-glutamylcysteine synthetase and relative mRNA levels
            for heavy and light subunits in human normal tissues
  JOURNAL   Biochem Biophys Res Commun 206 (2), 584-589 (1995)
   PUBMED   7826375
REFERENCE   10 (residues 1 to 274)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290449.1, BC041809.1,
            CB123306.1, CN272168.1, BQ049850.1, N53134.1, CN422503.1,
            BF513627.1, BM982562.1 and BU754400.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Glutamate-cysteine ligase, also known as
            gamma-glutamylcysteine synthetase, is the first rate limiting
            enzyme of glutathione synthesis. The enzyme consists of two
            subunits, a heavy catalytic subunit and a light regulatory subunit.
            Gamma glutamylcysteine synthetase deficiency has been implicated in
            some forms of hemolytic anemia. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1898476.1,
                                           SRR14038193.3111008.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370238.8/ ENSP00000359258.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..274
                     /product="glutamate--cysteine ligase regulatory subunit
                     isoform 1"
                     /EC_number="6.3.2.2"
                     /note="GSC light chain; glutamate-cysteine ligase
                     (gamma-glutamylcysteine synthetase), regulatory (30.8kD);
                     glutamate-cysteine ligase regulatory protein; GCS light
                     chain; glutamate-cysteine ligase modifier subunit delta2
                     alternative splicing; gamma-ECS regulatory subunit;
                     gamma-glutamylcysteine synthetase regulatory subunit"
                     /calculated_mol_wt=30596
     Region          <86..>211
                     /region_name="AKR_SF"
                     /note="Aldo-keto reductase (AKR) superfamily; cl00470"
                     /db_xref="CDD:444925"
     Site            263
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P48507.1)"
     CDS             1..274
                     /gene="GCLM"
                     /gene_synonym="GLCLR"
                     /coded_by="NM_002061.4:268..1092"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS746.1"
                     /db_xref="GeneID:2730"
                     /db_xref="HGNC:HGNC:4312"
                     /db_xref="MIM:601176"
ORIGIN      
        1 mgtdsraaka llarartlhl qtgnllnwgr lrkkcpsths eelhdciqkt lnewssqinp
       61 dlvrefpdvl ectvshavek inpdereemk vsaklfives nsssstrsav dmacsvlgva
      121 qldsviiasp piedgvnlsl ehlqpyweel enlvqskkiv aigtsdldkt qleqlyqwaq
      181 vkpnsnqvnl asccvmppdl tafakqfdiq llthndpkel lseasfqeal qesipdiqah
      241 ewvplwllry svivksrgii kskgyilqak rrgs
//
LOCUS       NP_002183                426 aa            linear   PRI 27-APR-2025
DEFINITION  inhibin beta A chain preproprotein [Homo sapiens].
ACCESSION   NP_002183
VERSION     NP_002183.1
DBSOURCE    REFSEQ: accession NM_002192.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Abutalebi,M., Li,D., Ahmad,W., Mokhtari,K., Entezari,M.,
            Hashemi,M., Fu,J. and Maghsoudloo,M.
  TITLE     Discovery of PELATON links to the INHBA gene in the TGF-beta
            pathway in colorectal cancer using a combination of bioinformatics
            and experimental investigations
  JOURNAL   Int J Biol Macromol 270 (Pt 1), 132239 (2024)
   PUBMED   38735606
  REMARK    GeneRIF: Discovery of PELATON links to the INHBA gene in the
            TGF-beta pathway in colorectal cancer using a combination of
            bioinformatics and experimental investigations.
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Chen,X. and Fan,R.
  TITLE     Inhibin A contributes to the tumorigenesis of oral squamous cell
            carcinoma by KIAA1429-mediated m6A modification
  JOURNAL   J Oral Pathol Med 53 (4), 266-274 (2024)
   PUBMED   38531807
  REMARK    GeneRIF: Inhibin A contributes to the tumorigenesis of oral
            squamous cell carcinoma by KIAA1429-mediated m6A modification.
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Abou Kors,T., Hofmann,L., Betzler,A., Payer,K., Bens,M., Truong,J.,
            von Witzleben,A., Thomas,J., Kraus,J.M., Kalaajieh,R., Huber,D.,
            Ezic,J., Benckendorff,J., Greve,J., Schuler,P.J., Ottensmeier,C.H.,
            Kestler,H.A., Hoffmann,T.K., Theodoraki,M.N., Brunner,C. and
            Laban,S.
  TITLE     INHBA is Enriched in HPV-negative Oropharyngeal Squamous Cell
            Carcinoma and Promotes Cancer Progression
  JOURNAL   Cancer Res Commun 4 (2), 571-587 (2024)
   PUBMED   38329386
  REMARK    GeneRIF: INHBA is Enriched in HPV-negative Oropharyngeal Squamous
            Cell Carcinoma and Promotes Cancer Progression.
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Hu,C., Ye,M., Bai,J., Liu,P., Lu,F., Chen,J., Xu,Y., Yan,L., Yu,P.,
            Xiao,Z., Gu,D., Xu,L., Tian,Y. and Tang,Q.
  TITLE     FOXA2-initiated transcriptional activation of INHBA induced by
            methylmalonic acid promotes pancreatic neuroendocrine neoplasm
            progression
  JOURNAL   Cell Mol Life Sci 81 (1), 50 (2024)
   PUBMED   38252148
  REMARK    GeneRIF: FOXA2-initiated transcriptional activation of INHBA
            induced by methylmalonic acid promotes pancreatic neuroendocrine
            neoplasm progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Wu,Z., Chen,J., Yang,L., Sun,K., Jiang,Q., Dong,F., Lu,W., Chen,R.
            and Chen,Y.
  TITLE     Elevated INHBA Promotes Tumor Progression of Cervical Cancer
  JOURNAL   Technol Cancer Res Treat 23, 15330338241234798 (2024)
   PUBMED   38419562
  REMARK    GeneRIF: Elevated INHBA Promotes Tumor Progression of Cervical
            Cancer.
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Shao,L., Frigon,N.L. Jr., Young,A.L., Yu,A.L., Mathews,L.S.,
            Vaughan,J., Vale,W. and Yu,J.
  TITLE     Effect of activin A on globin gene expression in purified human
            erythroid progenitors
  JOURNAL   Blood 79 (3), 773-781 (1992)
   PUBMED   1310063
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Mathews,L.S. and Vale,W.W.
  TITLE     Expression cloning of an activin receptor, a predicted
            transmembrane serine kinase
  JOURNAL   Cell 65 (6), 973-982 (1991)
   PUBMED   1646080
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Tanimoto,K., Handa,S., Ueno,N., Murakami,K. and Fukamizu,A.
  TITLE     Structure and sequence analysis of the human activin beta A subunit
            gene
  JOURNAL   DNA Seq 2 (2), 103-110 (1991)
   PUBMED   1777673
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Mason,A.J., Berkemeier,L.M., Schmelzer,C.H. and Schwall,R.H.
  TITLE     Activin B: precursor sequences, genomic structure and in vitro
            activities
  JOURNAL   Mol Endocrinol 3 (9), 1352-1358 (1989)
   PUBMED   2575216
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Barton,D.E., Yang-Feng,T.L., Mason,A.J., Seeburg,P.H. and
            Francke,U.
  TITLE     Mapping of genes for inhibin subunits alpha, beta A, and beta B on
            human and mouse chromosomes and studies of jsd mice
  JOURNAL   Genomics 5 (1), 91-99 (1989)
   PUBMED   2767687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU137531.1, BC007858.2,
            AC005027.3, AK001903.1 and AA491465.1.
            
            Summary: This gene encodes a member of the TGF-beta (transforming
            growth factor-beta) superfamily of proteins. The encoded
            preproprotein is proteolytically processed to generate a subunit of
            the dimeric activin and inhibin protein complexes. These complexes
            activate and inhibit, respectively, follicle stimulating hormone
            secretion from the pituitary gland. The encoded protein also plays
            a role in eye, tooth and testis development. Elevated expression of
            this gene may be associated with cancer cachexia in human patients.
            [provided by RefSeq, Aug 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.577620.1, BC007858.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2149398
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242208.5/ ENSP00000242208.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.1"
     Protein         1..426
                     /product="inhibin beta A chain preproprotein"
                     /note="Inhibin, beta-1; inhibin, beta A (activin A,
                     activin AB alpha polypeptide); inhibin beta A chain;
                     follicle-stimulating hormone-releasing protein;
                     FSH-releasing protein; erythroid differentiation factor;
                     activin beta-A chain; erythroid differentiation protein;
                     inhibin beta A subunit"
                     /calculated_mol_wt=45086
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2375
     Region          56..254
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; cl46657"
                     /db_xref="CDD:480997"
     Site            165
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08476.2)"
     Region          259..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08476.2)"
     mat_peptide     311..426
                     /product="Inhibin beta A chain. /id=PRO_0000033709"
                     /note="propagated from UniProtKB/Swiss-Prot (P08476.2)"
                     /calculated_mol_wt=12976
     Region          319..426
                     /region_name="TGF_beta_INHBA"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in inhibin beta A chain (INHBA) and similar
                     proteins; cd19404"
                     /db_xref="CDD:381674"
     Site            order(327,340,342,346,397,400..402,404,410,412,414,421)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381674"
     Site            order(389..390,392,413,416..417,426)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381674"
     CDS             1..426
                     /gene="INHBA"
                     /gene_synonym="EDF; FRP"
                     /coded_by="NM_002192.4:230..1510"
                     /db_xref="CCDS:CCDS5464.1"
                     /db_xref="GeneID:3624"
                     /db_xref="HGNC:HGNC:6066"
                     /db_xref="MIM:147290"
ORIGIN      
        1 mpllwlrgfl lascwiivrs sptpgseghs aapdcpscal aalpkdvpns qpemveavkk
       61 hilnmlhlkk rpdvtqpvpk aallnairkl hvgkvgengy veieddigrr aemnelmeqt
      121 seiitfaesg tarktlhfei skegsdlsvv eraevwlflk vpkanrtrtk vtirlfqqqk
      181 hpqgsldtge eaeevglkge rselllsekv vdarkstwhv fpvsssiqrl ldqgkssldv
      241 riaceqcqes gaslvllgkk kkkeeegegk kkgggeggag adeekeqshr pflmlqarqs
      301 edhphrrrrr glecdgkvni cckkqffvsf kdigwndwii apsgyhanyc egecpshiag
      361 tsgsslsfhs tvinhyrmrg hspfanlksc cvptklrpms mlyyddgqni ikkdiqnmiv
      421 eecgcs
//
LOCUS       NP_004431                998 aa            linear   PRI 27-APR-2025
DEFINITION  ephrin type-A receptor 7 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_004431
VERSION     NP_004431.1
DBSOURCE    REFSEQ: accession NM_004440.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Wang,L., Zhao,Q.F., Yang,B.B., Liang,H.J., Zhang,X.E., Zhang,X.Y.,
            Yang,W.J., Guo,Z.Y., Xu,X., Tian,F. and Wu,Q.H.
  TITLE     STAT3-EphA7 axis contributes to the progression of esophageal
            squamous cell carcinoma
  JOURNAL   Acta Oncol 62 (12), 1757-1766 (2023)
   PUBMED   37738252
  REMARK    GeneRIF: STAT3-EphA7 axis contributes to the progression of
            esophageal squamous cell carcinoma.
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Zhang,W., Cao,H., Yang,J., Zhao,J., Liang,Z., Kang,X. and Wang,R.
  TITLE     The identification and validation of EphA7 hypermethylation, a
            novel biomarker, in cervical cancer
  JOURNAL   BMC Cancer 22 (1), 636 (2022)
   PUBMED   35681118
  REMARK    GeneRIF: The identification and validation of EphA7
            hypermethylation, a novel biomarker, in cervical cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   4  (residues 1 to 998)
  AUTHORS   Levy,J., Schell,B., Nasser,H., Rachid,M., Ruaud,L., Couque,N.,
            Callier,P., Faivre,L., Marle,N., Engwerda,A., van
            Ravenswaaij-Arts,C.M.A., Plutino,M., Karmous-Benailly,H.,
            Benech,C., Redon,S., Boute,O., Boudry Labis,E., Rama,M., Kuentz,P.,
            Assoumani,J., Maldergem,L.V., Dupont,C., Verloes,A. and Tabet,A.C.
  TITLE     EPHA7 haploinsufficiency is associated with a neurodevelopmental
            disorder
  JOURNAL   Clin Genet 100 (4), 396-404 (2021)
   PUBMED   34176129
  REMARK    GeneRIF: EPHA7 haploinsufficiency is associated with a
            neurodevelopmental disorder.
REFERENCE   5  (residues 1 to 998)
  AUTHORS   Chakraborty,S. and Varma,A.K.
  TITLE     Crystal structure of clinically reported mutations Gly656Arg,
            Gly656Glu and Asp751His identified in the kinase domain of EphA7
  JOURNAL   Biochem Biophys Res Commun 568, 62-67 (2021)
   PUBMED   34186436
  REMARK    GeneRIF: Crystal structure of clinically reported mutations
            Gly656Arg, Gly656Glu and Asp751His identified in the kinase domain
            of EphA7.
REFERENCE   6  (residues 1 to 998)
  AUTHORS   Zhou,R.
  TITLE     The Eph family receptors and ligands
  JOURNAL   Pharmacol Ther 77 (3), 151-181 (1998)
   PUBMED   9576626
  REMARK    Review article
REFERENCE   7  (residues 1 to 998)
  AUTHORS   Flanagan,J.G. and Vanderhaeghen,P.
  TITLE     The ephrins and Eph receptors in neural development
  JOURNAL   Annu Rev Neurosci 21, 309-345 (1998)
   PUBMED   9530499
  REMARK    Review article
REFERENCE   8  (residues 1 to 998)
  AUTHORS   Ciossek,T. and Ullrich,A.
  TITLE     Identification of Elf-1 and B61 as high affinity ligands for the
            receptor tyrosine kinase MDK1
  JOURNAL   Oncogene 14 (1), 35-43 (1997)
   PUBMED   9010230
REFERENCE   9  (residues 1 to 998)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   10 (residues 1 to 998)
  AUTHORS   Fox,G.M., Holst,P.L., Chute,H.T., Lindberg,R.A., Janssen,A.M.,
            Basu,R. and Welcher,A.A.
  TITLE     cDNA cloning and tissue distribution of five human EPH-like
            receptor protein-tyrosine kinases
  JOURNAL   Oncogene 10 (5), 897-905 (1995)
   PUBMED   7898931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA503795.1, AB209269.1,
            AL591036.8, L36642.1, BC126125.1 and AL354857.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to the ephrin receptor subfamily of the
            protein-tyrosine kinase family. EPH and EPH-related receptors have
            been implicated in mediating developmental events, particularly in
            the nervous system. Receptors in the EPH subfamily typically have a
            single kinase domain and an extracellular region containing a
            Cys-rich domain and 2 fibronectin type III repeats. The ephrin
            receptors are divided into 2 groups based on the similarity of
            their extracellular domain sequences and their affinities for
            binding ephrin-A and ephrin-B ligands. Increased expression of this
            gene is associated with multiple forms of carcinoma. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Dec 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.203281.1,
                                           SRR1660803.257326.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369303.9/ ENSP00000358309.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.1"
     Protein         1..998
                     /product="ephrin type-A receptor 7 isoform 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 7; tyrosine-protein kinase
                     receptor EHK-3; Eph homology kinase-3; receptor
                     protein-tyrosine kinase HEK11; EPH-like kinase 11; EPH
                     homology kinase 3"
                     /calculated_mol_wt=108799
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3316
     mat_peptide     28..998
                     /product="Ephrin type-A receptor 7. /id=PRO_0000016818"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15375.3)"
                     /calculated_mol_wt=108799
     Region          30..206
                     /region_name="EphR_LBD_A7"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 7;
                     cd10485"
                     /db_xref="CDD:198453"
     Site            order(56,58..62,69..70,72,74,105,107,112..113,155,
                     159..160,163..165,192..194,196)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198453"
     Region          <314..>539
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            343
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15375.3)"
     Site            410
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15375.3)"
     Region          443..534
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(443,507,522)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(523..524,526..527)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            556..576
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15375.3)"
     Region          565..630
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15375.3)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15375.3)"
     Region          628..894
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(639,641..643,647,663,665,711..712,714,758,762..763,
                     765,776,795..799,808,842)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(639..643,647,663,665,711..714,717..718,762..763,765,
                     776)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            order(758,762,795..799,808,842)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            775..801
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15375.3)"
     Region          919..988
                     /region_name="SAM_EPH-A7"
                     /note="SAM domain of EPH-A7 subfamily of tyrosine kinase
                     receptors; cd09548"
                     /db_xref="CDD:188947"
     Site            order(940,973)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188947"
     Site            940
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15375.3)"
     Region          996..998
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15375.3)"
     CDS             1..998
                     /gene="EPHA7"
                     /gene_synonym="EHK-3; EHK3; EK11; HEK11"
                     /coded_by="NM_004440.4:219..3215"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS5031.1"
                     /db_xref="GeneID:2045"
                     /db_xref="HGNC:HGNC:3390"
                     /db_xref="MIM:602190"
ORIGIN      
        1 mvfqtrypsw iilcyiwllr fahtgeaqaa kevllldska qqtelewiss ppngweeisg
       61 ldenytpirt yqvcqvmepn qnnwlrtnwi skgnaqrifv elkftlrdcn slpgvlgtck
      121 etfnlyyyet dydtgrnire nlyvkidtia adesftqgdl gerkmklnte vreigplskk
      181 gfylafqdvg acialvsvkv yykkcwsiie nlaifpdtvt gsefsslvev rgtcvssaee
      241 eaenaprmhc saegewlvpi gkcickagyq qkgdtcepcg rgfyksssqd lqcsrcpths
      301 fsdkegssrc ecedgyyrap sdppyvactr ppsapqnlif ninqttvsle wsppadnggr
      361 ndvtyrilck rcsweqgecv pcgsnigymp qqtglednyv tvmdllahan ytfeveavng
      421 vsdlsrsqrl faavsittgq aapsqvsgvm kervlqrsve lswqepehpn gviteyeiky
      481 yekdqrerty stvktkstsa sinnlkpgtv yvfqirafta agygnysprl dvatleeatg
      541 kmfeatavss eqnpviiiav vavagtiilv fmvfgfiigr rhcgyskadq egdeelyfhf
      601 kfpgtktyid petyedpnra vhqfakelda scikiervig agefgevcsg rlklpgkrdv
      661 avaiktlkvg ytekqrrdfl ceasimgqfd hpnvvhlegv vtrgkpvmiv iefmengald
      721 aflrkhdgqf tviqlvgmlr giaagmryla dmgyvhrdla arnilvnsnl vckvsdfgls
      781 rvieddpeav ytttggkipv rwtapeaiqy rkftsasdvw sygivmwevm sygerpywdm
      841 snqdvikaie egyrlpapmd cpaglhqlml dcwqkeraer pkfeqivgil dkmirnpnsl
      901 ktplgtcsrp isplldqntp dfttfcsvge wlqaikmery kdnftaagyn slesvarmti
      961 edvmslgitl vghqkkimss iqtmraqmlh lhgtgiqv
//
LOCUS       NP_777581                 99 aa            linear   PRI 27-APR-2025
DEFINITION  small integral membrane protein 14 [Homo sapiens].
ACCESSION   NP_777581
VERSION     NP_777581.1
DBSOURCE    REFSEQ: accession NM_174921.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Jun,M.H., Jun,Y.W., Kim,K.H., Lee,J.A. and Jang,D.J.
  TITLE     Characterization of the cellular localization of C4orf34 as a novel
            endoplasmic reticulum resident protein
  JOURNAL   BMB Rep 47 (10), 563-568 (2014)
   PUBMED   24499674
  REMARK    GeneRIF: hC4orf34 is an endoplasmic reticulum-resident type I
            transmembrane protein.
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Nain,A.S. and Cimini,D.
  TITLE     MISP: The missing link between extracellular matrix and astral
            microtubules
  JOURNAL   Cell Cycle 12 (12), 1821-1822 (2013)
   PUBMED   23759569
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY155982.1, BC008502.1, BE615527.1, AC021148.8 and AA480975.1.
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' UTR compared to variant 1. Variants 1, 2, and 3 encode the same
            protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3642976.1,
                                           SRR18074968.2046017.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295958.10/ ENSP00000295958.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..99
                     /product="small integral membrane protein 14"
                     /calculated_mol_wt=10579
     Region          3..97
                     /region_name="DUF2615"
                     /note="Protein of unknown function (DUF2615); pfam11027"
                     /db_xref="CDD:402563"
     Site            50..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QK8.1)"
     Region          78..99
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QK8.1)"
     CDS             1..99
                     /gene="SMIM14"
                     /gene_synonym="C4orf34"
                     /coded_by="NM_174921.3:163..462"
                     /db_xref="CCDS:CCDS3456.1"
                     /db_xref="GeneID:201895"
                     /db_xref="HGNC:HGNC:27321"
ORIGIN      
        1 maeggfdpce cvcshehamr rlinllrqsq syctdteclq elpgpsgdng isvtmilvaw
       61 mvialilfll rppnlrgssl pgkptsphng qdppappvd
//
LOCUS       NP_000758                491 aa            linear   PRI 27-APR-2025
DEFINITION  cytochrome P450 2B6 [Homo sapiens].
ACCESSION   NP_000758
VERSION     NP_000758.1
DBSOURCE    REFSEQ: accession NM_000767.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Yamazaki,S., Hishinuma,E., Suzuki,Y., Ueda,A., Kijogi,C.,
            Nakayoshi,T., Oda,A., Saito,S., Tadaka,S., Kinoshita,K.,
            Maekawa,M., Sato,Y., Kumondai,M., Mano,N., Hirasawa,N. and
            Hiratsuka,M.
  TITLE     Functional significance of CYP2B6 gene rare allelic variants
            identified in Japanese individuals
  JOURNAL   Biochem Pharmacol 229, 116515 (2024)
   PUBMED   39218044
  REMARK    GeneRIF: Functional significance of CYP2B6 gene rare allelic
            variants identified in Japanese individuals.
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Eniayewu,O., Akinloye,A., Shenkoya,B., Azuka,U., Bolaji,O.,
            Adejuyigbe,E., Owen,A. and Olagunju,A.
  TITLE     Prenatal efavirenz exposure is independently associated with
            maternal, but not fetal CYP2B6 genotype
  JOURNAL   Pharmacogenet Genomics 34 (8), 253-260 (2024)
   PUBMED   38934229
  REMARK    GeneRIF: Prenatal efavirenz exposure is independently associated
            with maternal, but not fetal CYP2B6 genotype.
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Al-Adl,M., Youssef,M.M., El-Sebaie,A., Refaat,S. and El-Said,A.
  TITLE     The role of polymorphic cytochrome P450 gene (CYP2B6) in B-chronic
            lymphocytic leukemia (B-CLL) incidence and outcome among Egyptian
            patients
  JOURNAL   Oncol Res 32 (4), 785-797 (2024)
   PUBMED   38560574
  REMARK    GeneRIF: The role of polymorphic cytochrome P450 gene (CYP2B6) in
            B-chronic lymphocytic leukemia (B-CLL) incidence and outcome among
            Egyptian patients.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Zhou,Y., Dong,H., Fan,J., Zhu,M., Liu,L., Wang,Y., Tang,P. and
            Chen,X.
  TITLE     Cytochrome P450 2B6 and UDP-Glucuronosyltransferase Enzyme-Mediated
            Clearance of Ciprofol (HSK3486) in Humans: The Role of Hepatic and
            Extrahepatic Metabolism
  JOURNAL   Drug Metab Dispos 52 (2), 106-117 (2024)
   PUBMED   38071562
  REMARK    GeneRIF: Cytochrome P450 2B6 and UDP-Glucuronosyltransferase
            Enzyme-Mediated Clearance of Ciprofol (HSK3486) in Humans: The Role
            of Hepatic and Extrahepatic Metabolism.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Ma,X., Zang,X., Yang,L., Zhou,W., Li,Y., Wei,J., Guo,J., Han,J.,
            Liang,J. and Jin,T.
  TITLE     Genetic polymorphisms in CYP2B6 may be associated with lung cancer
            risk in the Chinese Han population
  JOURNAL   Expert Rev Respir Med 17 (12), 1297-1305 (2023)
   PUBMED   38166557
  REMARK    GeneRIF: Genetic polymorphisms in CYP2B6 may be associated with
            lung cancer risk in the Chinese Han population.
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Fernandez-Salguero,P., Hoffman,S.M., Cholerton,S., Mohrenweiser,H.,
            Raunio,H., Rautio,A., Pelkonen,O., Huang,J.D., Evans,W.E.,
            Idle,J.R. et al.
  TITLE     A genetic polymorphism in coumarin 7-hydroxylation: sequence of the
            human CYP2A genes and identification of variant CYP2A6 alleles
  JOURNAL   Am J Hum Genet 57 (3), 651-660 (1995)
   PUBMED   7668294
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Miles,J.S., McLaren,A.W., Gonzalez,F.J. and Wolf,C.R.
  TITLE     Alternative splicing in the human cytochrome P450IIB6 gene: use of
            a cryptic exon within intron 3 and splice acceptor site within exon
            4
  JOURNAL   Nucleic Acids Res 18 (1), 189 (1990)
   PUBMED   2308828
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Miles,J.S., McLaren,A.W. and Wolf,C.R.
  TITLE     Alternative splicing in the human cytochrome P450IIB6 gene
            generates a high level of aberrant messages
  JOURNAL   Nucleic Acids Res 17 (20), 8241-8255 (1989)
   PUBMED   2813061
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Yamano,S., Nhamburo,P.T., Aoyama,T., Meyer,U.A., Inaba,T.,
            Kalow,W., Gelboin,H.V., McBride,O.W. and Gonzalez,F.J.
  TITLE     cDNA cloning and sequence and cDNA-directed expression of human
            P450 IIB1: identification of a normal and two variant cDNAs derived
            from the CYP2B locus on chromosome 19 and differential expression
            of the IIB mRNAs in human liver
  JOURNAL   Biochemistry 28 (18), 7340-7348 (1989)
   PUBMED   2573390
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Miles,J.S., Spurr,N.K., Gough,A.C., Jowett,T., McLaren,A.W.,
            Brook,J.D. and Wolf,C.R.
  TITLE     A novel human cytochrome P450 gene (P450IIB): chromosomal
            localization and evidence for alternative splicing
  JOURNAL   Nucleic Acids Res 16 (13), 5783-5795 (1988)
   PUBMED   2899870
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011541.7, BC067431.1 and
            AC023172.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene, CYP2B6, encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This protein localizes to the endoplasmic reticulum and its
            expression is induced by phenobarbital. The enzyme is known to
            metabolize some xenobiotics, such as the anti-cancer drugs
            cyclophosphamide and ifosphamide. Transcript variants for this gene
            have been described; however, it has not been resolved whether
            these transcripts are in fact produced by this gene or by a closely
            related pseudogene, CYP2B7. Both the gene and the pseudogene are
            located in the middle of a CYP2A pseudogene found in a large
            cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F
            subfamilies on chromosome 19q. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M29874.1, BC067431.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2145122
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324071.10/ ENSP00000324648.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..491
                     /product="cytochrome P450 2B6"
                     /EC_number="1.14.14.1"
                     /note="cytochrome P450, subfamily IIB
                     (phenobarbital-inducible), polypeptide 6; cytochrome P450
                     IIB1; 1,4-cineole 2-exo-monooxygenase; cytochrome P450,
                     family 2, subfamily B, polypeptide 6"
                     /calculated_mol_wt=56147
     Region          62..486
                     /region_name="CYP2B"
                     /note="cytochrome P450 family 2, subfamily B; cd20672"
                     /db_xref="CDD:410765"
     Site            order(73,98,101,104,114..115,206,209,294,297..298,
                     301..302,362..363,365..368,389,436,476..478)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410765"
     Site            order(98,113..114,121,125,179,298..299,302..303,306,357,
                     363,367,369,392,428..430,434,436..438,441..442)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410765"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P20813.1)"
     CDS             1..491
                     /gene="CYP2B6"
                     /gene_synonym="CPB6; CYP2B; CYP2B7; CYP2B7P; CYPIIB6;
                     EFVM; IIB1; P450"
                     /coded_by="NM_000767.5:25..1500"
                     /db_xref="CCDS:CCDS12570.1"
                     /db_xref="GeneID:1555"
                     /db_xref="HGNC:HGNC:2615"
                     /db_xref="MIM:123930"
ORIGIN      
        1 melsvllfla lltglllllv qrhpnthdrl ppgprplpll gnllqmdrrg llksflrfre
       61 kygdvftvhl gprpvvmlcg veairealvd kaeafsgrgk iamvdpffrg ygvifangnr
      121 wkvlrrfsvt tmrdfgmgkr sveeriqeea qclieelrks kgalmdptfl fqsitaniic
      181 sivfgkrfhy qdqeflkmln lfyqtfslis svfgqlfelf sgflkyfpga hrqvyknlqe
      241 inayighsve khretldpsa pkdlidtyll hmekeksnah sefshqnlnl ntlslffagt
      301 ettsttlryg fllmlkyphv aervyreieq vigphrppel hdrakmpyte aviyeiqrfs
      361 dllpmgvphi vtqhtsfrgy iipkdtevfl ilstalhdph yfekpdafnp dhfldangal
      421 kkteafipfs lgkriclgeg iaraelflff ttilqnfsma spvapedidl tpqecgvgki
      481 pptyqirflp r
//
LOCUS       NP_001349638             356 aa            linear   ROD 27-APR-2025
DEFINITION  selenide, water dikinase 1 isoform b [Mus musculus].
ACCESSION   NP_001349638
VERSION     NP_001349638.1
DBSOURCE    REFSEQ: accession NM_001362709.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Bang,J., Kang,D., Jung,J., Yoo,T.J., Shim,M.S., Gladyshev,V.N.,
            Tsuji,P.A., Hatfield,D.L., Kim,J.H. and Lee,B.J.
  TITLE     SEPHS1: Its evolution, function and roles in development and
            diseases
  JOURNAL   Arch Biochem Biophys 730, 109426 (2022)
   PUBMED   36202216
  REMARK    GeneRIF: SEPHS1: Its evolution, function and roles in development
            and diseases.
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Kang,D., Lee,J., Jung,J., Carlson,B.A., Chang,M.J., Chang,C.B.,
            Kang,S.B., Lee,B.C., Gladyshev,V.N., Hatfield,D.L., Lee,B.J. and
            Kim,J.H.
  TITLE     Selenophosphate synthetase 1 deficiency exacerbates osteoarthritis
            by dysregulating redox homeostasis
  JOURNAL   Nat Commun 13 (1), 779 (2022)
   PUBMED   35140209
  REMARK    GeneRIF: Selenophosphate synthetase 1 deficiency exacerbates
            osteoarthritis by dysregulating redox homeostasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Qiao,L., Dho,S.H., Kim,J.Y. and Kim,L.K.
  TITLE     SEPHS1 is dispensable for pluripotency maintenance but
            indispensable for cardiac differentiation in mouse embryonic stem
            cells
  JOURNAL   Biochem Biophys Res Commun 590, 125-131 (2022)
   PUBMED   34974300
  REMARK    GeneRIF: SEPHS1 is dispensable for pluripotency maintenance but
            indispensable for cardiac differentiation in mouse embryonic stem
            cells.
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Bang,J., Han,M., Yoo,T.J., Qiao,L., Jung,J., Na,J., Carlson,B.A.,
            Gladyshev,V.N., Hatfield,D.L., Kim,J.H., Kim,L.K. and Lee,B.J.
  TITLE     Identification of Signaling Pathways for Early Embryonic Lethality
            and Developmental Retardation in Sephs1-/- Mice
  JOURNAL   Int J Mol Sci 22 (21), 11647 (2021)
   PUBMED   34769078
  REMARK    GeneRIF: Identification of Signaling Pathways for Early Embryonic
            Lethality and Developmental Retardation in Sephs1(-/-) Mice.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Jung,J., Kim,Y., Na,J., Qiao,L., Bang,J., Kwon,D., Yoo,T.J.,
            Kang,D., Kim,L.K., Carlson,B.A., Hatfield,D.L., Kim,J.H. and
            Lee,B.J.
  TITLE     Constitutive Oxidative Stress by SEPHS1 Deficiency Induces
            Endothelial Cell Dysfunction
  JOURNAL   Int J Mol Sci 22 (21), 11646 (2021)
   PUBMED   34769076
  REMARK    GeneRIF: Constitutive Oxidative Stress by SEPHS1 Deficiency Induces
            Endothelial Cell Dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Tobe,R., Carlson,B.A., Huh,J.H., Castro,N.P., Xu,X.M., Tsuji,P.A.,
            Lee,S.G., Bang,J., Na,J.W., Kong,Y.Y., Beaglehole,D., Southon,E.,
            Seifried,H., Tessarollo,L., Salomon,D.S., Schweizer,U.,
            Gladyshev,V.N., Hatfield,D.L. and Lee,B.J.
  TITLE     Selenophosphate synthetase 1 is an essential protein with roles in
            regulation of redox homoeostasis in mammals
  JOURNAL   Biochem J 473 (14), 2141-2154 (2016)
   PUBMED   27208177
  REMARK    GeneRIF: Data found that several malignant characteristics of
            SPS1-deficient F9 cells were reversed, suggesting that SPS1 played
            a role in supporting and/or sustaining cancer. Selenophosphate
            synthetase 1 is an essential protein with roles in regulation of
            redox homoeostasis in mammals.
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Saiki,R., Nagata,A., Kainou,T., Matsuda,H. and Kawamukai,M.
  TITLE     Characterization of solanesyl and decaprenyl diphosphate synthases
            in mice and humans
  JOURNAL   FEBS J 272 (21), 5606-5622 (2005)
   PUBMED   16262699
  REMARK    GeneRIF: murine and human solanesyl and decaprenyl diphosphate
            synthases are heterotetramers composed of newly characterized hDPS1
            (mSPS1) and hDLP1 (mDLP1)
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL807778.10.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            lacks an alternate in-frame exon compared to variant 1. The
            resulting isoform (b) has the same N- and C-termini but is shorter
            compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660819.62970.1,
                                           SRR1660811.254069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849383, SAMN00849387
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 3.02 cM"
     Protein         1..356
                     /product="selenide, water dikinase 1 isoform b"
                     /EC_number="2.7.9.3"
                     /note="selenide, water dikinase 1; selenium donor protein
                     1; selenophosphate synthase 1"
                     /calculated_mol_wt=38887
     Region          19..297
                     /region_name="selD"
                     /note="selenium donor protein; TIGR00476"
                     /db_xref="CDD:273100"
     CDS             1..356
                     /gene="Sephs1"
                     /gene_synonym="1110046B24Rik; SELD; SPS; SPS1"
                     /coded_by="NM_001362709.1:379..1449"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:109079"
                     /db_xref="MGI:MGI:1923580"
ORIGIN      
        1 mstresfnpe tyeldksfrl trftelkgtg ckvpqdvlqk lleslqenhf qedeqflgav
       61 mprlgigmdt cviplrhggl slvqttdyiy pivddpymme rdkvipliiq gfkdaaeeag
      121 tsvtggqtvl npwivlggva ttvcqpnefi mpdnavpgdv lvltkplgtq vavavhqwld
      181 ipekwnkikl vvtqedvela yqeammnmar lnrtaaglmh tfnahaatdi tgfgilghaq
      241 nlakqqrnev sfvihnlpvl akmaavskac gnmfglmhgt cpetsgglli clpreqaarf
      301 caeikspkyg eghqawiigi vekgnrtari idkpriieva pqvatqnvnp tpgats
//
LOCUS       NP_000631                380 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-13 receptor subunit alpha-2 precursor [Homo sapiens].
ACCESSION   NP_000631
VERSION     NP_000631.1
DBSOURCE    REFSEQ: accession NM_000640.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Chao,H., Zheng,L., Hsu,P., He,J., Wu,R., Xu,S., Zeng,R., Zhou,Y.,
            Ma,H., Liu,H. and Tang,Q.
  TITLE     IL-13RA2 downregulation in fibroblasts promotes keloid fibrosis via
            JAK/STAT6 activation
  JOURNAL   JCI Insight 8 (6), e157091 (2023)
   PUBMED   36757802
  REMARK    GeneRIF: IL-13RA2 downregulation in fibroblasts promotes keloid
            fibrosis via JAK/STAT6 activation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Nagai,T., Terada,N., Fujii,M., Nagata,Y., Nakahara,K., Mukai,S.,
            Okasho,K., Kamiyama,Y., Akamatsu,S., Kobayashi,T., Iida,K.,
            Denawa,M., Hagiwara,M., Inoue,T., Ogawa,O. and Kamoto,T.
  TITLE     Identification of the alpha2 chain of interleukin-13 receptor as a
            potential biomarker for predicting castration resistance of
            prostate cancer using patient-derived xenograft models
  JOURNAL   Cancer Rep (Hoboken) 6 (2), e1701 (2023)
   PUBMED   36806727
  REMARK    GeneRIF: Identification of the alpha2 chain of interleukin-13
            receptor as a potential biomarker for predicting castration
            resistance of prostate cancer using patient-derived xenograft
            models.
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Marquez-Ortiz,R.A., Contreras-Zarate,M.J., Tesic,V.,
            Alvarez-Eraso,K.L.F., Kwak,G., Littrell,Z., Costello,J.C.,
            Sreekanth,V., Ormond,D.R., Karam,S.D., Kabos,P. and Cittelly,D.M.
  TITLE     IL13Ralpha2 Promotes Proliferation and Outgrowth of Breast Cancer
            Brain Metastases
  JOURNAL   Clin Cancer Res 27 (22), 6209-6221 (2021)
   PUBMED   34544797
  REMARK    GeneRIF: IL13Ralpha2 Promotes Proliferation and Outgrowth of Breast
            Cancer Brain Metastases.
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Karakas,N., Stuckey,D., Revai-Lechtich,E. and Shah,K.
  TITLE     IL13Ralpha2- and EGFR-targeted pseudomonas exotoxin potentiates the
            TRAIL-mediated death of GBM cells
  JOURNAL   Int J Mol Med 48 (1) (2021)
   PUBMED   34080646
  REMARK    GeneRIF: IL13Ralpha2 and EGFRtargeted pseudomonas exotoxin
            potentiates the TRAILmediated death of GBM cells.
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Li,L., Wei,K., Ding,Y., Ahati,P., Xu,H., Fang,H. and Wang,H.
  TITLE     M2a Macrophage-Secreted CHI3L1 Promotes Extracellular Matrix
            Metabolic Imbalances via Activation of IL-13Ralpha2/MAPK Pathway in
            Rat Intervertebral Disc Degeneration
  JOURNAL   Front Immunol 12, 666361 (2021)
   PUBMED   34168643
  REMARK    GeneRIF: M2a Macrophage-Secreted CHI3L1 Promotes Extracellular
            Matrix Metabolic Imbalances via Activation of IL-13Ralpha2/MAPK
            Pathway in Rat Intervertebral Disc Degeneration.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Donaldson,D.D., Whitters,M.J., Fitz,L.J., Neben,T.Y., Finnerty,H.,
            Henderson,S.L., O'Hara,R.M. Jr., Beier,D.R., Turner,K.J., Wood,C.R.
            and Collins,M.
  TITLE     The murine IL-13 receptor alpha 2: molecular cloning,
            characterization, and comparison with murine IL-13 receptor alpha 1
  JOURNAL   J Immunol 161 (5), 2317-2324 (1998)
   PUBMED   9725226
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Guo,J., Apiou,F., Mellerin,M.P., Lebeau,B., Jacques,Y. and
            Minvielle,S.
  TITLE     Chromosome mapping and expression of the human interleukin-13
            receptor
  JOURNAL   Genomics 42 (1), 141-145 (1997)
   PUBMED   9177784
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Zhang,J.G., Hilton,D.J., Willson,T.A., McFarlane,C., Roberts,B.A.,
            Moritz,R.L., Simpson,R.J., Alexander,W.S., Metcalf,D. and
            Nicola,N.A.
  TITLE     Identification, purification, and characterization of a soluble
            interleukin (IL)-13-binding protein. Evidence that it is distinct
            from the cloned Il-13 receptor and Il-4 receptor alpha-chains
  JOURNAL   J Biol Chem 272 (14), 9474-9480 (1997)
   PUBMED   9083087
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Gauchat,J.F., Schlagenhauf,E., Feng,N.P., Moser,R., Yamage,M.,
            Jeannin,P., Alouani,S., Elson,G., Notarangelo,L.D., Wells,T.,
            Eugster,H.P. and Bonnefoy,J.Y.
  TITLE     A novel 4-kb interleukin-13 receptor alpha mRNA expressed in human
            B, T, and endothelial cells encoding an alternate type-II
            interleukin-4/interleukin-13 receptor
  JOURNAL   Eur J Immunol 27 (4), 971-978 (1997)
   PUBMED   9130652
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Caput,D., Laurent,P., Kaghad,M., Lelias,J.M., Lefort,S., Vita,N.
            and Ferrara,P.
  TITLE     Cloning and characterization of a specific interleukin (IL)-13
            binding protein structurally related to the IL-5 receptor alpha
            chain
  JOURNAL   J Biol Chem 271 (28), 16921-16926 (1996)
   PUBMED   8663118
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y08768.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is closely related to
            Il13RA1, a subuint of the interleukin 13 receptor complex. This
            protein binds IL13 with high affinity, but lacks cytoplasmic
            domain, and does not appear to function as a signal mediator. It is
            reported to play a role in the internalization of IL13. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291957.1, Y08768.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000243213.2/ ENSP00000243213.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq23"
     Protein         1..380
                     /product="interleukin-13 receptor subunit alpha-2
                     precursor"
                     /note="cancer/testis antigen 19; interleukin 13 binding
                     protein; interleukin 13 receptor alpha 2 chain; IL-13RA2;
                     IL-13R-alpha-2; IL-13R subunit alpha-2; IL-13 receptor
                     subunit alpha-2; interleukin 13 receptor, alpha 2"
                     /calculated_mol_wt=41457
     sig_peptide     1..26
                     /calculated_mol_wt=2737
     mat_peptide     27..380
                     /product="interleukin-13 receptor subunit alpha-2"
                     /calculated_mol_wt=41457
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14627.1)"
     Region          142..235
                     /region_name="IL6Ra-bind"
                     /note="Interleukin-6 receptor alpha chain, binding;
                     pfam09240"
                     /db_xref="CDD:401252"
     Site            215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20223216; propagated from
                     UniProtKB/Swiss-Prot (Q14627.1)"
     Site            290
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14627.1)"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14627.1)"
     Region          322..326
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14627.1)"
     Site            344..363
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14627.1)"
     CDS             1..380
                     /gene="IL13RA2"
                     /gene_synonym="CD213A2; CT19; IL-13R; IL13BP"
                     /coded_by="NM_000640.3:98..1240"
                     /db_xref="CCDS:CCDS14565.1"
                     /db_xref="GeneID:3598"
                     /db_xref="HGNC:HGNC:5975"
                     /db_xref="MIM:300130"
ORIGIN      
        1 mafvclaigc lytflisttf gctsssdtei kvnppqdfei vdpgylgyly lqwqpplsld
       61 hfkectveye lkyrnigset wktiitknlh ykdgfdlnkg ieakihtllp wqctngsevq
      121 sswaettywi spqgipetkv qdmdcvyynw qyllcswkpg igvlldtnyn lfywyegldh
      181 alqcvdyika dgqnigcrfp yleasdykdf yicvngssen kpirssyftf qlqnivkplp
      241 pvyltftres sceiklkwsi plgpiparcf dyeieiredd ttlvtatven etytlkttne
      301 trqlcfvvrs kvniycsddg iwsewsdkqc wegedlskkt llrfwlpfgf ililvifvtg
      361 lllrkpntyp kmipeffcdt
//
LOCUS       NP_001356697              74 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 28 isoform 9 [Homo sapiens].
ACCESSION   NP_001356697
VERSION     NP_001356697.1
DBSOURCE    REFSEQ: accession NM_001369768.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Rousseau-Merck,M.F., Hillion,J., Jonveaux,P., Couillin,P.,
            Seite,P., Thiesen,H.J. and Berger,R.
  TITLE     Chromosomal localization of 9 KOX zinc finger genes: physical
            linkages suggest clustering of KOX genes on chromosomes 12, 16, and
            19
  JOURNAL   Hum Genet 92 (6), 583-587 (1993)
   PUBMED   8262519
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC070146.1 and AC008813.6.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070146.1, BU537030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..74
                     /product="zinc finger protein 28 isoform 9"
                     /note="zinc finger protein KOX24"
                     /calculated_mol_wt=8345
     Region          8..>48
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     CDS             1..74
                     /gene="ZNF28"
                     /gene_synonym="KOX24"
                     /coded_by="NM_001369768.1:122..346"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:7576"
                     /db_xref="HGNC:HGNC:13073"
                     /db_xref="MIM:620466"
ORIGIN      
        1 malpqglltf rdvaiefsqe ewkcldpaqr tlyrdvmlen yrnlvslged nllgmcpcvs
       61 lyflllplgs hilt
//
LOCUS       NP_004286                470 aa            linear   PRI 27-APR-2025
DEFINITION  TNF receptor-associated factor 4 [Homo sapiens].
ACCESSION   NP_004286
VERSION     NP_004286.2
DBSOURCE    REFSEQ: accession NM_004295.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Nie,X.M., Dong,D.F., Lin,J.F., Wu,B.Y. and Cai,G.
  TITLE     [TRAF4 promotes lung cancer development by activating tyrosine
            kinase of EGFR]
  JOURNAL   Zhonghua Zhong Liu Za Zhi 46 (10), 968-978 (2024)
   PUBMED   39414598
  REMARK    GeneRIF: [TRAF4 promotes lung cancer development by activating
            tyrosine kinase of EGFR].
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Liao,J., Qing,X., Li,X., Gan,Y., Wang,R., Han,S., Li,W. and Song,W.
  TITLE     TRAF4 regulates ubiquitination-modulated survivin turnover and
            confers radioresistance
  JOURNAL   Int J Biol Sci 20 (1), 182-199 (2024)
   PUBMED   38164179
  REMARK    GeneRIF: TRAF4 regulates ubiquitination-modulated survivin turnover
            and confers radioresistance.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Gu,Y., Zhong,K., Peng,L., Ding,W. and Zeng,X.
  TITLE     TRAF4 Silencing Induces Cell Apoptosis and Improves Retinoic Acid
            Sensitivity in Human Neuroblastoma
  JOURNAL   Neurochem Res 48 (7), 2116-2128 (2023)
   PUBMED   36795185
  REMARK    GeneRIF: TRAF4 Silencing Induces Cell Apoptosis and Improves
            Retinoic Acid Sensitivity in Human Neuroblastoma.
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Dong,X., Li,X., Gan,Y., Ding,J., Wei,B., Zhou,L., Cui,W. and Li,W.
  TITLE     TRAF4-mediated ubiquitination-dependent activation of JNK/Bcl-xL
            drives radioresistance
  JOURNAL   Cell Death Dis 14 (2), 102 (2023)
   PUBMED   36765039
  REMARK    GeneRIF: TRAF4-mediated ubiquitination-dependent activation of
            JNK/Bcl-xL drives radioresistance.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Wang,Y., Luo,X., Wu,N., Liao,Q. and Wang,J.
  TITLE     USP7 mediates TRAF4 deubiquitination to facilitate the malignant
            phenotype of ovarian cancer via the RSK4/PI3K/AKT axis
  JOURNAL   J Cancer Res Ther 19 (1), 97-107 (2023)
   PUBMED   37006049
  REMARK    GeneRIF: USP7 mediates TRAF4 deubiquitination to facilitate the
            malignant phenotype of ovarian cancer via the RSK4/PI3K/AKT axis.
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Ye,X., Mehlen,P., Rabizadeh,S., VanArsdale,T., Zhang,H., Shin,H.,
            Wang,J.J., Leo,E., Zapata,J., Hauser,C.A., Reed,J.C. and
            Bredesen,D.E.
  TITLE     TRAF family proteins interact with the common neurotrophin receptor
            and modulate apoptosis induction
  JOURNAL   J Biol Chem 274 (42), 30202-30208 (1999)
   PUBMED   10514511
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Krajewska,M., Krajewski,S., Zapata,J.M., Van Arsdale,T.,
            Gascoyne,R.D., Berern,K., McFadden,D., Shabaik,A., Hugh,J.,
            Reynolds,A., Clevenger,C.V. and Reed,J.C.
  TITLE     TRAF-4 expression in epithelial progenitor cells. Analysis in
            normal adult, fetal, and tumor tissues
  JOURNAL   Am J Pathol 152 (6), 1549-1561 (1998)
   PUBMED   9626059
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Masson,R., Regnier,C.H., Chenard,M.P., Wendling,C., Mattei,M.G.,
            Tomasetto,C. and Rio,M.C.
  TITLE     Tumor necrosis factor receptor associated factor 4 (TRAF4)
            expression pattern during mouse development
  JOURNAL   Mech Dev 71 (1-2), 187-191 (1998)
   PUBMED   9507120
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Regnier,C.H., Tomasetto,C., Moog-Lutz,C., Chenard,M.P.,
            Wendling,C., Basset,P. and Rio,M.C.
  TITLE     Presence of a new conserved domain in CART1, a novel member of the
            tumor necrosis factor receptor-associated protein family, which is
            expressed in breast carcinoma
  JOURNAL   J Biol Chem 270 (43), 25715-25721 (1995)
   PUBMED   7592751
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Tomasetto,C., Regnier,C., Moog-Lutz,C., Mattei,M.G., Chenard,M.P.,
            Lidereau,R., Basset,P. and Rio,M.C.
  TITLE     Identification of four novel human genes amplified and
            overexpressed in breast carcinoma and localized to the q11-q21.3
            region of chromosome 17
  JOURNAL   Genomics 28 (3), 367-376 (1995)
   PUBMED   7490069
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CR990949.1, BC001769.1 and
            AC010761.10.
            
            On Jul 31, 2002 this sequence version replaced NP_004286.1.
            
            Summary: This gene encodes a member of the TNF receptor associated
            factor (TRAF) family. TRAF proteins are associated with, and
            mediate signal transduction from members of the TNF receptor
            superfamily. The encoded protein has been shown to interact with
            neurotrophin receptor, p75 (NTR/NTSR1), and negatively regulate NTR
            induced cell death and NF-kappa B activation. This protein has been
            found to bind to p47phox, a cytosolic regulatory factor included in
            a multi-protein complex known as NAD(P)H oxidase. This protein
            thus, is thought to be involved in the oxidative activation of
            MAPK8/JNK. Alternatively spliced transcript variants have been
            observed but the full-length nature of only one has been
            determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.752357.1, BC001769.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262395.10/ ENSP00000262395.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..470
                     /product="TNF receptor-associated factor 4"
                     /EC_number="2.3.2.27"
                     /note="tumor necrosis receptor-associated factor 4A;
                     malignant 62; cysteine-rich domain associated with ring
                     and TRAF domain; MLN 62; RING finger protein 83;
                     metastatic lymph node gene 62 protein; cysteine-rich
                     domain associated with RING and Traf domains protein 1"
                     /calculated_mol_wt=53412
     Region          15..59
                     /region_name="mRING-HC-C3HC3D_TRAF4"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in tumor necrosis factor (TNF) receptor-associated
                     factor 4 (TRAF4) and similar proteins; cd16641"
                     /db_xref="CDD:438303"
     Region          102..156
                     /region_name="zf-TRAF"
                     /note="TRAF-type zinc finger; pfam02176"
                     /db_xref="CDD:280357"
     Region          <113..211
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          210..269
                     /region_name="zf-TRAF"
                     /note="TRAF-type zinc finger; pfam02176"
                     /db_xref="CDD:280357"
     Region          308..463
                     /region_name="MATH_TRAF4"
                     /note="Tumor Necrosis Factor Receptor (TNFR)-Associated
                     Factor (TRAF) family, TRAF4 subfamily, TRAF domain,
                     C-terminal MATH subdomain; composed of proteins with
                     similarity to human TRAF4, including the Drosophila
                     protein DTRAF1. TRAF molecules serve as adapter...;
                     cd03781"
                     /db_xref="CDD:239750"
     Site            order(311,313,341..342,373,376,393)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:239750"
     Site            order(349,351,366,409,432..435)
                     /site_type="active"
                     /note="TNFR binding site [active]"
                     /db_xref="CDD:239750"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BUZ4.1)"
     CDS             1..470
                     /gene="TRAF4"
                     /gene_synonym="CART1; MLN62; RNF83"
                     /coded_by="NM_004295.4:103..1515"
                     /db_xref="CCDS:CCDS11243.1"
                     /db_xref="GeneID:9618"
                     /db_xref="HGNC:HGNC:12034"
                     /db_xref="MIM:602464"
ORIGIN      
        1 mpgfdykfle kpkrrllcpl cgkpmrepvq vstcghrfcd tclqeflseg vfkcpedqlp
       61 ldyakiypdp elevqvlglp ircihseegc rwsgplrhlq ghlntcsfnv ipcpnrcpmk
      121 lsrrdlpahl qhdcpkrrlk cefcgcdfsg eayeshegmc pqesvycenk cgarmmrrll
      181 aqhatsecpk rtqpctyctk efvfdtiqsh qyqcprlpva cpnqcgvgtv aredlpghlk
      241 dscntalvlc pfkdsgckhr cpklamarhv eesvkphlam mcalvsrqrq elqelrrele
      301 elsvgsdgvl iwkigsygrr lqeakakpnl ecfspafyth kygyklqvsa flngngsgeg
      361 thlslyirvl pgafdnllew pfarrvtfsl ldqsdpglak pqhvtetfhp dpnwknfqkp
      421 gtwrgsldes slgfgypkfi shqdirkrny vrddavfira avelprkils
//
LOCUS       NP_808878                421 aa            linear   PRI 27-APR-2025
DEFINITION  synaptotagmin-12 isoform a [Homo sapiens].
ACCESSION   NP_808878
VERSION     NP_808878.1
DBSOURCE    REFSEQ: accession NM_177963.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Liu,K., Luo,J., Shao,C., Ren,Z., Sun,S., Zhu,Y., Zhou,H., Jiang,Z.,
            Li,X., Gu,W., Xu,Y., Qiang,Y., Ren,B., Xu,L., Wu,H. and Shen,Y.
  TITLE     Synaptotagmin 12 (SYT12) Gene Expression Promotes Cell
            Proliferation and Progression of Lung Adenocarcinoma and Involves
            the Phosphoinositide 3-Kinase (PI3K)/AKT/Mammalian Target of
            Rapamycin (mTOR) Pathway
  JOURNAL   Med Sci Monit 26, e920351 (2020)
   PUBMED   32108133
  REMARK    GeneRIF: Synaptotagmin 12 (SYT12) Gene Expression Promotes Cell
            Proliferation and Progression of Lung Adenocarcinoma and Involves
            the Phosphoinositide 3-Kinase (PI3K)/AKT/Mammalian Target of
            Rapamycin (mTOR) Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  CONSRTM   Psychiatric GWAS Consortium Bipolar Disorder Working Group
  TITLE     Large-scale genome-wide association analysis of bipolar disorder
            identifies a new susceptibility locus near ODZ4
  JOURNAL   Nat Genet 43 (10), 977-983 (2011)
   PUBMED   21926972
  REMARK    Erratum:[Nat Genet. 2012 Sep;44(9):1072. Fullerton, Janice M
            [added]; Hyoun, Phil L [corrected to Lee, Phil H]; Meng, Fan Guo
            [corrected to Meng, Fan]]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Maximov,A., Shin,O.H., Liu,X. and Sudhof,T.C.
  TITLE     Synaptotagmin-12, a synaptic vesicle phosphoprotein that modulates
            spontaneous neurotransmitter release
  JOURNAL   J Cell Biol 176 (1), 113-124 (2007)
   PUBMED   17190793
  REMARK    GeneRIF: Studies of the orthologous gene in rat have shown that
            spontaneous synaptic-vesicle exocytosis is selectively modulated by
            synaptotagmin 12.
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Craxton,M.
  TITLE     Genomic analysis of synaptotagmin genes
  JOURNAL   Genomics 77 (1-2), 43-49 (2001)
   PUBMED   11543631
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003176.2, DA239473.1,
            BC037406.1 and AL833834.1.
            
            Summary: This gene is a member of the synaptotagmin gene family and
            encodes a protein similar to other family members that mediate
            calcium-dependent regulation of membrane trafficking in synaptic
            transmission. Studies of the orthologous gene in rat have shown
            that the encoded protein selectively modulates spontaneous
            synaptic-vesicle exocytosis and may also be involved in regulating
            calcium independent secretion in nonneuronal cells. Alternative
            splicing results in multiple transcript variants. The gene has
            previously been referred to as synaptotagmin XI but has been
            renamed synaptotagmin XII to be standard with mouse and rat
            official nomenclature.[provided by RefSeq, Apr 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.22200.1, BC037406.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2149398
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000527043.6/ ENSP00000435316.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..421
                     /product="synaptotagmin-12 isoform a"
                     /note="synaptotagmin-XII"
                     /calculated_mol_wt=46406
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IV01.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97610; propagated from
                     UniProtKB/Swiss-Prot (Q8IV01.1)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97610; propagated from
                     UniProtKB/Swiss-Prot (Q8IV01.1)"
     Region          152..263
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q920N7; propagated from
                     UniProtKB/Swiss-Prot (Q8IV01.1)"
     Region          284..419
                     /region_name="C2B_Synaptotagmin-12"
                     /note="C2 domain second repeat present in Synaptotagmin
                     12; cd08406"
                     /db_xref="CDD:176051"
     CDS             1..421
                     /gene="SYT12"
                     /gene_synonym="SYT11; sytXII"
                     /coded_by="NM_177963.4:351..1616"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8154.1"
                     /db_xref="GeneID:91683"
                     /db_xref="HGNC:HGNC:18381"
                     /db_xref="MIM:606436"
ORIGIN      
        1 mavdvaeyhl sviksppgwe vgvyaagala llgiaavslw klwtsgsfps pspfpnydyr
       61 ylqqkygesc aearekrvpa wnaqrastrg ppsrkgslsi edtfesisel gplelmgrel
      121 dlapygtlrk sqsadslnsi ssvsntfgqd ftlgqvevsm eydtashtln vavmqgkdll
      181 ereeasfesc fmrvsllpde qivgisriqr naysiffdek fsipldptal eekslrfsvf
      241 gidedernvs tgvvelklsv ldlplqpfsg wlylqdqnka adavgeills lsylptaerl
      301 tvvvvkaknl iwtndkttad pfvkvyllqd grkmskkkta vkrddpnpvf neamifsvpa
      361 ivlqdlslrv tvaesssdgr gdnvghviig psasgmgtth wnqmlatlrr pvsmwhavrr
      421 n
//
LOCUS       NP_001349814            3025 aa            linear   ROD 27-APR-2025
DEFINITION  adhesion G-protein coupled receptor G4 [Mus musculus].
ACCESSION   NP_001349814 XP_003085307
VERSION     NP_001349814.1
DBSOURCE    REFSEQ: accession NM_001362885.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 3025)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 3025)
  AUTHORS   Hamann,J., Aust,G., Arac,D., Engel,F.B., Formstone,C.,
            Fredriksson,R., Hall,R.A., Harty,B.L., Kirchhoff,C., Knapp,B.,
            Krishnan,A., Liebscher,I., Lin,H.H., Martinelli,D.C., Monk,K.R.,
            Peeters,M.C., Piao,X., Promel,S., Schoneberg,T., Schwartz,T.W.,
            Singer,K., Stacey,M., Ushkaryov,Y.A., Vallon,M., Wolfrum,U.,
            Wright,M.W., Xu,L., Langenhan,T. and Schioth,H.B.
  TITLE     International Union of Basic and Clinical Pharmacology. XCIV.
            Adhesion G protein-coupled receptors
  JOURNAL   Pharmacol Rev 67 (2), 338-367 (2015)
   PUBMED   25713288
  REMARK    Review article
REFERENCE   3  (residues 1 to 3025)
  AUTHORS   Bjarnadottir,T.K., Fredriksson,R., Hoglund,P.J., Gloriam,D.E.,
            Lagerstrom,M.C. and Schioth,H.B.
  TITLE     The human and mouse repertoire of the adhesion family of
            G-protein-coupled receptors
  JOURNAL   Genomics 84 (1), 23-33 (2004)
   PUBMED   15203201
REFERENCE   4  (residues 1 to 3025)
  AUTHORS   Vassilatis,D.K., Hohmann,J.G., Zeng,H., Li,F., Ranchalis,J.E.,
            Mortrud,M.T., Brown,A., Rodriguez,S.S., Weller,J.R., Wright,A.C.,
            Bergmann,J.E. and Gaitanaris,G.A.
  TITLE     The G protein-coupled receptor repertoires of human and mouse
  JOURNAL   Proc Natl Acad Sci U S A 100 (8), 4903-4908 (2003)
   PUBMED   12679517
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL671998.10 and AL672263.13.
            
            On May 2, 2018 this sequence version replaced XP_003085307.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on single protein-coding
                                         transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3025
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="X"
                     /map="X 30.34 cM"
     Protein         1..3025
                     /product="adhesion G-protein coupled receptor G4"
                     /note="probable G-protein coupled receptor 112; G protein
                     coupled receptor Gpr112"
                     /calculated_mol_wt=328579
     Region          <54..162
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cl22861"
                     /db_xref="CDD:473984"
     Region          201..581
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     Region          2587..2629
                     /region_name="GPS"
                     /note="GPCR proteolysis site, GPS, motif; pfam01825"
                     /db_xref="CDD:460350"
     Region          2642..2903
                     /region_name="7tmB2_GPR112"
                     /note="Probable G protein-coupled receptor 112, member of
                     the class B2 family of seven-transmembrane G
                     protein-coupled receptors; cd15997"
                     /db_xref="CDD:320663"
     Region          2644..2669
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320663"
     Site            order(2649,2653,2696,2699..2700,2703,2712,2719,2796..2797,
                     2799,2801,2855,2858,2870,2874)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320663"
     Region          2679..2701
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320663"
     Region          2712..2739
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320663"
     Region          2754..2770
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320663"
     Region          2793..2816
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320663"
     Region          2838..2863
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320663"
     Region          2867..2892
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320663"
     CDS             1..3025
                     /gene="Adgrg4"
                     /gene_synonym="Gm367; Gpr112; PGR17"
                     /coded_by="NM_001362885.1:94..9171"
                     /db_xref="GeneID:236798"
                     /db_xref="MGI:MGI:2685213"
ORIGIN      
        1 mpelsrltac idlismtnss hywmafiyit nntllgredv dlglagdhqq lilysfgktf
       61 yvsyhlipfh whtlclvwdg vkgrlelfrn kerilaimdq phrlspngtl vlghfprnge
      121 gqiktviprf tsslyyfqlw drileneefm tcfygnvvsw eddvwlihki sptvdrrlrc
      181 fvsenmtiqe tstnvsqqid lttssqttgl nphktshsst llpegmadst instaisyan
      241 tvpsplatvs aakdlktstt etatfltdtl ftstatplpt qtvtehsylg ktrtskrvea
      301 mateifhsat atdlidtsvf tknytvsets ttksksavgk ttlflnests iaptpcpkhk
      361 stdvailhts ksgqeflvss aartvswstl eetspittdv givstfppes lltstaspvs
      421 stfpeiqlas tlsttdsema stvhsvlpmq tiptprtvkp esgstnfqdv fspsmedals
      481 vsmpkettfm afssitsspi trtqdeqiai daesthltii pgtkfvptla easlfptieg
      541 qaytqdtptt depmltltst kspstynase svltsitiks dyqfftnett wtsksgqnll
      601 tsmntttipt ftsnktltlp fqgnatnrdh ssmttnvspi easteskvtt ssdattasyt
      661 talfkptsqw lshftsvsgi tsiasqpesk lttlllksns mptvatnefp sipsepvaps
      721 vntstltdik pnfsteksis etiqietngv ssfgdtlapl pmsattqrvy ttvtkettsr
      781 hpkvkstist vaeaspfstm levtdeseqm vtasvtispf tdieklttal sketataevg
      841 vswlstklke smpesshngt tesfnsthty tvdwtseksk gnsasspnsa stqalpelps
      901 sstmktmgvt fstnssqrta aslsagilsp qtasthalvt pqllthtfsl pvnisavtsp
      961 kttmvffdet kvtlsqpstl ardfttsmps vgstlptvtm ttelvppvsp tastisdsmf
     1021 thrdllhtts evttisstta hmaisslret lvsslrpptp vitkaistip sissdsvsps
     1081 ihtlvcsrps pnnvtivsst yvssttstsv atpseshfsf pyafssggdv tmasgptgts
     1141 aggeamppnt fvnkfitsvd hesttyfvnt pvstqsvfat smvssdkeqt nismektlrt
     1201 tgvaeispsk nsfildsqst fpwemtdtel setteisshq thlpseilpg ysdsgnlttf
     1261 stsgstqsaq tlssstiigv rvsegstsle ktalpsqvqt vtkslthdke rtsalseypp
     1321 rtvekimsss pvthqatghl atsivdasrt trishpvlin ttlsyllslk tkpeatqias
     1381 stsgstenfp nsfspfttgl lstnftmitp ngsttvlsip neptnlpkkt smeastpisq
     1441 mdllalnvta ftskkvsdth tmlmtkssrt ihigtlksvs igtfglksek sempvnnsdf
     1501 sttvlysdts trlgefftss sslppkatkt tqastlnttp vahagptsqr tvfsstfsns
     1561 svvevplnyt tahfssptqr gflsmktipt tsmagistsv igatssslss skntepissi
     1621 pktmfsllls ttqqpsqeng aptldilpgi tvssggatdl inansratip anelsttpsd
     1681 nfytflntqd sptltnskvt prptesvkst pthlsfdtrk mnilteltks gpcvttpvly
     1741 plwtqtstap pltshlysph stkakfplas qmaeypawat gitpsitqal lttsrntqrv
     1801 edspfpvftt kvmtpnrmev etlhspsgtl atsttsqigl vsrdvtvmpl istseslpsl
     1861 gisestslsi sstfppttla ailptfekta mpvtpgitls snpsvnsrat sptwsssslp
     1921 sdsrasiftp srlltsssge msestfpasd iiatysnftv aplsdgsati atqatstttl
     1981 diitanslts ppipskdkdg slhtstfles slrttgadss tdmsermsfg rtsispsltr
     2041 hdlsigsltv ssptntspws kvpvtsesht lfpskstlds vmstatttst aigtsfplms
     2101 temahpstat gfslvsssfe ttwmdsifss lftqpstspt akestvsfyn ikmsfsvfde
     2161 eprvlvttvi hdltkdwlnf mfqnsefsla nlaiqiksrk tskeetamyr yileqkkgqg
     2221 mdaifhvpys cacwviikak sslesvelis sirtkihgnl thgnftqdql tllvksdhvv
     2281 veklepgkce adetpskykg tykwpltdpt etaqercikn enrnatrics isiqtgkcqw
     2341 ekprlkqckl lqglpdkivd lanitisden addvaehiln lvnespplde eetkiivskv
     2401 adisncdeis inltqiilqi lntvtekqsd sasnlppvsn eilriiervg hkmefagrta
     2461 nltvaklala vlrvdhkfeg mafsiqssee viapqiflgd iplrkalasi ylpkslrekv
     2521 pldglqtilf nffgqtslfk aktitselmt yvvsasisnt siqnladpvi iilkhiqgdw
     2581 nydqvycafw dfdtnnglgg wnpsgcklke sninyticqc nhlthfgvlm dlsrstvdav
     2641 nerilviity tgcgissifl giamvtyiaf hklrkdypsk ilinlctall mlnlaflvns
     2701 wltsfqkvgl citaavalhy fllvsltwmg leavhmyfal vkvfntyipn yilkfclagw
     2761 gipaitvaii lsvrkdlygt lspttpfcwi kddhifyisv vayfcliflm nlsmfctvlv
     2821 qltsvksqsq ktrkkmilnd lkgtisltfl lgltwgfaff awgpvriffl ylfaicntlq
     2881 gflifvfycv mkesvreqwh mplhcrwlrl enfagwinvr hkqkrlkknn esklltpslm
     2941 stttfksigs vpsipseinf sngdfddspd tfsflsckaa ptfirralpa eiqtnstqkq
     3001 rsfpinvsrd thltpssglg emfnl
//
LOCUS       NP_001355811             728 aa            linear   PRI 27-APR-2025
DEFINITION  collagen alpha-1(XIII) chain isoform 23 [Homo sapiens].
ACCESSION   NP_001355811 XP_011537594
VERSION     NP_001355811.1
DBSOURCE    REFSEQ: accession NM_001368882.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Kim,H., Choi,N., Kim,D.Y., Kim,S.Y., Song,S.Y. and Sung,J.H.
  TITLE     TGF-beta2 and collagen play pivotal roles in the spheroid formation
            and anti-aging of human dermal papilla cells
  JOURNAL   Aging (Albany NY) 13 (16), 19978-19995 (2021)
   PUBMED   34404755
  REMARK    GeneRIF: TGF-beta2 and collagen play pivotal roles in the spheroid
            formation and anti-aging of human dermal papilla cells.
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Koivunen,J., Kemppainen,A.V., Finnila,M.A., Keski-Filppula,R.,
            Haronen,H., Tu,H., Pellikka,H., Heikkinen,A., Kylmaoja,E.,
            Sormunen,R., Miinalainen,I., Saarakkala,S., Izzi,V. and
            Pihlajaniemi,T.
  TITLE     Collagen XIII-derived ectodomain regulates bone angiogenesis and
            intracortical remodeling
  JOURNAL   Matrix Biol 83, 6-25 (2019)
   PUBMED   31220558
  REMARK    GeneRIF: Data suggest that ColXIII has a role in age-dependent
            cortical bone deterioration with possible implications for
            osteoporosis and fracture risk.
REFERENCE   3  (residues 1 to 728)
  AUTHORS   Rodriguez Cruz,P.M., Cossins,J., Estephan,E.P., Munell,F.,
            Selby,K., Hirano,M., Maroofin,R., Mehrjardi,M.Y.V., Chow,G.,
            Carr,A., Manzur,A., Robb,S., Munot,P., Wei Liu,W., Banka,S.,
            Fraser,H., De Goede,C., Zanoteli,E., Conti Reed,U., Sage,A.,
            Gratacos,M., Macaya,A., Dusl,M., Senderek,J., Topf,A., Hofer,M.,
            Knight,R., Ramdas,S., Jayawant,S., Lochmuller,H., Palace,J. and
            Beeson,D.
  TITLE     The clinical spectrum of the congenital myasthenic syndrome
            resulting from COL13A1 mutations
  JOURNAL   Brain 142 (6), 1547-1560 (2019)
   PUBMED   31081514
  REMARK    GeneRIF: patients with COL13A1 mutations present mostly with severe
            early-onset myasthenic syndrome with feeding and breathing
            difficulties
REFERENCE   4  (residues 1 to 728)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
REFERENCE   5  (residues 1 to 728)
  AUTHORS   Juvonen,M., Sandberg,M. and Pihlajaniemi,T.
  TITLE     Patterns of expression of the six alternatively spliced exons
            affecting the structures of the COL1 and NC2 domains of the alpha
            1(XIII) collagen chain in human tissues and cell lines
  JOURNAL   J Biol Chem 267 (34), 24700-24707 (1992)
   PUBMED   1447210
REFERENCE   6  (residues 1 to 728)
  AUTHORS   Juvonen,M. and Pihlajaniemi,T.
  TITLE     Characterization of the spectrum of alternative splicing of alpha 1
            (XIII) collagen transcripts in HT-1080 cells and calvarial tissue
            resulted in identification of two previously unidentified
            alternatively spliced sequences, one previously unidentified exon,
            and nine new mRNA variants
  JOURNAL   J Biol Chem 267 (34), 24693-24699 (1992)
   PUBMED   1447209
REFERENCE   7  (residues 1 to 728)
  AUTHORS   Tikka,L., Elomaa,O., Pihlajaniemi,T. and Tryggvason,K.
  TITLE     Human alpha 1 (XIII) collagen gene. Multiple forms of the gene
            transcripts are generated through complex alternative splicing of
            several short exons
  JOURNAL   J Biol Chem 266 (26), 17713-17719 (1991)
   PUBMED   1894651
REFERENCE   8  (residues 1 to 728)
  AUTHORS   Pihlajaniemi,T. and Tamminen,M.
  TITLE     The alpha 1 chain of type XIII collagen consists of three
            collagenous and four noncollagenous domains, and its primary
            transcript undergoes complex alternative splicing
  JOURNAL   J Biol Chem 265 (28), 16922-16928 (1990)
   PUBMED   1698771
REFERENCE   9  (residues 1 to 728)
  AUTHORS   Shows,T.B., Tikka,L., Byers,M.G., Eddy,R.L., Haley,L.L.,
            Henry,W.M., Prockop,D.J. and Tryggvason,K.
  TITLE     Assignment of the human collagen alpha 1 (XIII) chain gene
            (COL13A1) to the q22 region of chromosome 10
  JOURNAL   Genomics 5 (1), 128-133 (1989)
   PUBMED   2767682
REFERENCE   10 (residues 1 to 728)
  AUTHORS   Tikka,L., Pihlajaniemi,T., Henttu,P., Prockop,D.J. and
            Tryggvason,K.
  TITLE     Gene structure for the alpha 1 chain of a human short-chain
            collagen (type XIII) with alternatively spliced transcripts and
            translation termination codon at the 5' end of the last exon
  JOURNAL   Proc Natl Acad Sci U S A 85 (20), 7491-7495 (1988)
   PUBMED   2459707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC025426.11, AL138925.17 and
            AC024601.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 7, 2019 this sequence version replaced XP_011537594.1.
            
            Summary: This gene encodes the alpha chain of one of the
            nonfibrillar collagens. The function of this gene product is not
            known, however, it has been detected at low levels in all
            connective tissue-producing cells so it may serve a general
            function in connective tissues. Unlike most of the collagens, which
            are secreted into the extracellular matrix, collagen XIII contains
            a transmembrane domain and the protein has been localized to the
            plasma membrane. The transcripts for this gene undergo complex and
            extensive splicing involving at least eight exons. Like other
            collagens, collagen XIII is a trimer; it is not known whether this
            trimer is composed of one or more than one alpha chain isomer. A
            number of alternatively spliced transcript variants have been
            described, but the full length nature of some of them has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.73679.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000645393.2/ ENSP00000496051.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..728
                     /product="collagen alpha-1(XIII) chain isoform 23"
                     /note="collagen alpha-1(XIII) chain; collagen, type XIII,
                     alpha 1"
                     /calculated_mol_wt=70726
     Region          <188..>451
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <340..>573
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <463..>712
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     CDS             1..728
                     /gene="COL13A1"
                     /gene_synonym="CMS19; COLXIIIA1"
                     /coded_by="NM_001368882.1:519..2705"
                     /note="isoform 23 is encoded by transcript variant 23"
                     /db_xref="CCDS:CCDS91251.1"
                     /db_xref="GeneID:1305"
                     /db_xref="HGNC:HGNC:2190"
                     /db_xref="MIM:120350"
ORIGIN      
        1 mvaerthkaa atgargpgel gapgtvalva araergarlp spgscglltl alcslalsll
       61 ahfrtaelqa rvlrleaerg eqqmetailg rvnqlldekw klhsrrrrea pktspgcncp
      121 pgppgptgrp glpgdkgaig mpgrvgvkgq pgekgspgda glsiigprgp pgqpgtrgfp
      181 gfpgpigldg kpghpgpkgd mgltgppgqp gpqgqkgekg qcgeyphrll pllnsvrlap
      241 ppvikrrtfq geqsqasiqg ppgppgppgp sgplghpglp gpmgppglpg ppgpkgdpgi
      301 qgyhgrkger gmpgmpgkhg akgapgiava gmkgepgipg tkgdpgaegk pgppgllgkr
      361 gqrgekgaeg spglpgllgq kgekgdagns igggrgepgp pglpgppgpk geagvdgqvg
      421 ppgqpgdkge rgaageqgpd gpkgskgepg kgemvdyngn inealqeirt lalmgppglp
      481 gqigppgapg ipgqkgeigl pgppghdgek gprgkpgdmg ppgpqgppgk dgppgvkgen
      541 ghpgspgekg ekgetgqags pgekgeagek gnpgaevpgl pgpegppgpp glqgvpgpkg
      601 eagldgakge kgfqgekgdr gplglpgasg ldgrpgppgt pgpigvpgpa gpkgergskg
      661 dpgmtgptga aglpglhgpp gdkgnrgerg kkgsrgpkgd kgdqgapgld apcplgedgl
      721 pvqgcwnk
//
LOCUS       NP_001349853            1132 aa            linear   PRI 27-APR-2025
DEFINITION  arf-GAP with SH3 domain, ANK repeat and PH domain-containing
            protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001349853 XP_005250982
VERSION     NP_001349853.1
DBSOURCE    REFSEQ: accession NM_001362924.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Zhang,Y., Bai,H., Zhang,W., Gao,J., Gao,C., Deng,T., Liu,X.,
            Sun,X., Liu,Y., Wang,N. and Wu,Y.
  TITLE     miR-212/132 attenuates OVA-induced airway inflammation by
            inhibiting mast cells activation through MRGPRX2 and ASAP1
  JOURNAL   Exp Cell Res 433 (2), 113828 (2023)
   PUBMED   37875175
  REMARK    GeneRIF: miR-212/132 attenuates OVA-induced airway inflammation by
            inhibiting mast cells activation through MRGPRX2 and ASAP1.
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Park,H., Son,H., Cha,H., Song,K., Bang,S., Jee,S., Kim,H.,
            Myung,J., Shin,S.J., Cha,C., Chung,M.S. and Paik,S.
  TITLE     ASAP1 Expression in Invasive Breast Cancer and Its Prognostic Role
  JOURNAL   Int J Mol Sci 24 (18), 14355 (2023)
   PUBMED   37762658
  REMARK    GeneRIF: ASAP1 Expression in Invasive Breast Cancer and Its
            Prognostic Role.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Barbagallo,C., Stella,M., Di Mauro,S., Scamporrino,A.,
            Filippello,A., Scionti,F., Di Martino,M.T., Purrello,M., Ragusa,M.,
            Purrello,F. and Piro,S.
  TITLE     An Uncharacterised lncRNA Coded by the ASAP1 Locus Is Downregulated
            in Serum of Type 2 Diabetes Mellitus Patients
  JOURNAL   Int J Mol Sci 24 (17), 13485 (2023)
   PUBMED   37686290
  REMARK    GeneRIF: An Uncharacterised lncRNA Coded by the ASAP1 Locus Is
            Downregulated in Serum of Type 2 Diabetes Mellitus Patients.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1132)
  AUTHORS   Xie,W., Han,Z., Zuo,Z., Xin,D., Chen,H., Huang,J., Zhu,S., Lou,H.,
            Yu,Z., Chen,C., Chen,S., Hu,Y., Huang,J., Zhang,F., Ni,Z., Shen,X.,
            Xue,X. and Lin,K.
  TITLE     ASAP1 activates the IQGAP1/CDC42 pathway to promote tumor
            progression and chemotherapy resistance in gastric cancer
  JOURNAL   Cell Death Dis 14 (2), 124 (2023)
   PUBMED   36792578
  REMARK    GeneRIF: ASAP1 activates the IQGAP1/CDC42 pathway to promote tumor
            progression and chemotherapy resistance in gastric cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1132)
  AUTHORS   Cui,X., Yuan,T., Ning,P., Han,J., Liu,Y., Feng,J., Lian,F., Hao,M.,
            Dong,L., Hao,J., Xing,L. and Wu,C.
  TITLE     Polymorphisms in the ASAP1 and SP110 Genes and Its Association with
            the Susceptibility to Pulmonary Tuberculosis in a Mongolian
            Population
  JOURNAL   J Immunol Res 2022, 2713869 (2022)
   PUBMED   36249417
  REMARK    GeneRIF: Polymorphisms in the ASAP1 and SP110 Genes and Its
            Association with the Susceptibility to Pulmonary Tuberculosis in a
            Mongolian Population.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1132)
  AUTHORS   Oshiro,T., Koyama,S., Sugiyama,S., Kondo,A., Onodera,Y.,
            Asahara,T., Sabe,H. and Kikuchi,A.
  TITLE     Interaction of POB1, a downstream molecule of small G protein Ral,
            with PAG2, a paxillin-binding protein, is involved in cell
            migration
  JOURNAL   J Biol Chem 277 (41), 38618-38626 (2002)
   PUBMED   12149250
  REMARK    GeneRIF: These results suggest that POB1 interacts with PAG2
            through its proline-rich motif, thereby regulating cell migration
            (PAG2).
REFERENCE   7  (residues 1 to 1132)
  AUTHORS   Scott,M.P., Zappacosta,F., Kim,E.Y., Annan,R.S. and Miller,W.T.
  TITLE     Identification of novel SH3 domain ligands for the Src family
            kinase Hck. Wiskott-Aldrich syndrome protein (WASP),
            WASP-interacting protein (WIP), and ELMO1
  JOURNAL   J Biol Chem 277 (31), 28238-28246 (2002)
   PUBMED   12029088
REFERENCE   8  (residues 1 to 1132)
  AUTHORS   Liu,Y., Loijens,J.C., Martin,K.H., Karginov,A.V. and Parsons,J.T.
  TITLE     The association of ASAP1, an ADP ribosylation factor-GTPase
            activating protein, with focal adhesion kinase contributes to the
            process of focal adhesion assembly
  JOURNAL   Mol Biol Cell 13 (6), 2147-2156 (2002)
   PUBMED   12058076
REFERENCE   9  (residues 1 to 1132)
  AUTHORS   Furman,C., Short,S.M., Subramanian,R.R., Zetter,B.R. and
            Roberts,T.M.
  TITLE     DEF-1/ASAP1 is a GTPase-activating protein (GAP) for ARF1 that
            enhances cell motility through a GAP-dependent mechanism
  JOURNAL   J Biol Chem 277 (10), 7962-7969 (2002)
   PUBMED   11773070
  REMARK    GeneRIF: DEF-1 alters cell motility through the deactivation of
            ARF1. In contrast, the inhibition of cell spreading by DEF-1 was
            not dependent on GAP activity, indicating that spreading and
            motility are altered by DEF-1 through different pathways.
REFERENCE   10 (residues 1 to 1132)
  AUTHORS   Brown,M.T., Andrade,J., Radhakrishna,H., Donaldson,J.G.,
            Cooper,J.A. and Randazzo,P.A.
  TITLE     ASAP1, a phospholipid-dependent arf GTPase-activating protein that
            associates with and is phosphorylated by Src
  JOURNAL   Mol Cell Biol 18 (12), 7038-7051 (1998)
   PUBMED   9819391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA319233.1, BC144493.1,
            DA416332.1, DA315979.1, BQ645913.1, AB033075.1 and AI494058.1.
            
            On Jun 20, 2018 this sequence version replaced XP_005250982.1.
            
            Summary: This gene encodes an ADP-ribosylation factor (ARF)
            GTPase-activating protein. The GTPase-activating activity is
            stimulated by phosphatidylinositol 4,5-biphosphate (PIP2), and is
            greater towards ARF1 and ARF5, and lesser for ARF6. This gene maybe
            involved in regulation of membrane trafficking and cytoskeleton
            remodeling. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21-q24.22"
     Protein         1..1132
                     /product="arf-GAP with SH3 domain, ANK repeat and PH
                     domain-containing protein 1 isoform 3"
                     /note="centaurin, beta 4; arf-GAP with SH3 domain, ANK
                     repeat and PH domain-containing protein 1; DEF-1;
                     PIP2-dependent ARF1 GAP; ARF GTPase-activating protein 1;
                     development and differentiation-enhancing factor 1;
                     ADP-ribosylation factor-directed GTPase-activating protein
                     1; 130 kDa phosphatidylinositol 4,5-biphosphate-dependent
                     ARF1 GTPase-activating protein; 130 kDa
                     phosphatidylinositol 4,5-bisphosphate-dependent ARF1
                     GTPase-activating protein"
                     /calculated_mol_wt=125767
     Region          54..268
                     /region_name="BAR_ASAP1"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with
                     SH3 domain, ANK repeat and PH domain containing protein 1;
                     cd07641"
                     /db_xref="CDD:153325"
     Site            order(63,66..67,71,73..74,77..78,80..81,91..92,94..95,
                     98..99,101..102,105,121,124..125,226,229..230,232,234,
                     237..238,240..241,247..248,251..252,254..255,258..259,
                     261..262)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153325"
     Region          319..425
                     /region_name="PH_ASAP"
                     /note="ArfGAP with SH3 domain, ankyrin repeat and PH
                     domain Pleckstrin homology (PH) domain; cd13251"
                     /db_xref="CDD:270071"
     Region          440..561
                     /region_name="ArfGap_ASAP1"
                     /note="ArfGAP domain of ASAP1 (ArfGAP with SH3 domain, ANK
                     repeat and PH domain-containing protein 1); cd08848"
                     /db_xref="CDD:350073"
     Site            order(443..444,447,470..472,493,501..505,507..509,
                     511..513,517..518,521..522,553,556..557)
                     /site_type="other"
                     /note="putative ANK repeat binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350073"
     Site            order(457,460,477,480,542)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350073"
     Site            order(457,460,477,480,485)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350073"
     Site            order(482,485..486)
                     /site_type="other"
                     /note="putative GTP binding site [chemical binding]"
                     /db_xref="CDD:350073"
     Region          <585..696
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          603..635
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Region          604..637
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(605,609..610,613..615,620..621,625,628,637,639,641,
                     645..646,649..651,653..654,658,661,670,672,674,678..679,
                     682..684,686..687,691)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          639..670
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          639..668
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Region          716..763
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Region          <727..1063
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q1AAU6; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Region          779..1065
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            842
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            1011
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            1030
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            1044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Site            1051
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWY8; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     Region          1074..1130
                     /region_name="SH3_ASAP1"
                     /note="Src homology 3 domain of ArfGAP with SH3 domain,
                     ankyrin repeat and PH domain containing protein 1;
                     cd11965"
                     /db_xref="CDD:212898"
     Site            order(1079,1081,1084,1088,1106..1107,1123,1125..1126)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212898"
     Site            1131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWY8; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH1.4)"
     CDS             1..1132
                     /gene="ASAP1"
                     /gene_synonym="AMAP1; CENTB4; DDEF1; PAG2; PAP; ZG14P"
                     /coded_by="NM_001362924.1:229..3627"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:50807"
                     /db_xref="HGNC:HGNC:2720"
                     /db_xref="MIM:605953"
ORIGIN      
        1 mrssasrlss fssrdslwnr mpdqisvsef iaettedyns pttssfttrl hncrntvtll
       61 eealdqdrta lqkvkksvka iynsgqdhvq neenyaqvld kfgsnflsrd npdlgtafvk
      121 fstltkelst llknllqgls hnviftldsl lkgdlkgvkg dlkkpfdkaw kdyetkftki
      181 ekekrehakq hgmirteitg aeiaeemeke rrlfqlqmce ylikvneikt kkgvdllqnl
      241 ikyyhaqcnf fqdglktadk lkqyieklaa dlynikqtqd eekkqltalr dliksslqld
      301 qkesrrdsqs rqggysmhql qgnkeygsek kgyllkksdg irkvwqrrkc svkngiltis
      361 hatsnrqpak lnlltcqvkp naedkksfdl ishnrtyhfq aedeqdyvaw isvltnskee
      421 altmafrgeq sagensledl tkaiiedvqr lpgndiccdc gsseptwlst nlgiltciec
      481 sgihremgvh isriqsleld klgtsellla knvgnnsfnd imeanlpsps pkptpssdmt
      541 vrkeyitaky vdhrfsrktc stssaklnel leaiksrdll aliqvyaegv elmepllepg
      601 qelgetalhl avrtadqtsl hlvdflvqnc gnldkqtalg ntvlhycsmy skpeclklll
      661 rskptvdivn qagetaldia krlkatqced llsqaksgkf nphvhveyew nlrqeeides
      721 dddlddkpsp ikkersprpq sfchsssisp qdklalpgfs tprdkqrlsy gaftnqifvs
      781 tstdsptspt teapplpprn agkgptgpps tlplstqtss gsstlskkrp pppppghkrt
      841 lsdppsplph gppnkgavpw gndggpssss kttnkfegls qqsstssakt algprvlpkl
      901 pqkvalrktd hlsldkatip peifqkssql aelpqkpppg dlppkptela pkpqigdlpp
      961 kpgelppkpq lgdlppkpql sdlppkpqmk dlppkpqlgd llaksqtgdv spkaqqpsev
     1021 tlkshpldls pnvqsrdaiq kqasedsndl tptlpetpvp lprkintgkn kvrrvktiyd
     1081 cqadnddelt fiegeviivt geedqewwig hiegqperkg vfpvsfvhil sd
//
LOCUS       NP_001034585             200 aa            linear   PRI 27-APR-2025
DEFINITION  cation channel sperm-associated auxiliary subunit zeta [Homo
            sapiens].
ACCESSION   NP_001034585
VERSION     NP_001034585.1
DBSOURCE    REFSEQ: accession NM_001039496.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Sinha,A., Singh,V., Singh,S. and Yadav,S.
  TITLE     Proteomic analyses reveal lower expression of TEX40 and ATP6V0A2
            proteins related to calcium ion entry and acrosomal acidification
            in asthenozoospermic males
  JOURNAL   Life Sci 218, 81-88 (2019)
   PUBMED   30550884
  REMARK    GeneRIF: Low TEX40 expression is associated with asthenozoospermia.
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Chung,J.J., Miki,K., Kim,D., Shim,S.H., Shi,H.F., Hwang,J.Y.,
            Cai,X., Iseri,Y., Zhuang,X. and Clapham,D.E.
  TITLE     CatSperzeta regulates the structural continuity of sperm Ca2+
            signaling domains and is required for normal fertility
  JOURNAL   Elife 6, e23082 (2017)
   PUBMED   28226241
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Micci,F., Panagopoulos,I., Thorsen,J., Davidson,B., Trope,C.G. and
            Heim,S.
  TITLE     Low frequency of ESRRA-C11orf20 fusion gene in ovarian carcinomas
  JOURNAL   PLoS Biol 12 (2), e1001784 (2014)
   PUBMED   24504521
  REMARK    GeneRIF: The frequency of the ESRRA/C11orf20 gene fusion in serous
            ovarian carcinomas of stages III and IV must be very low.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Salzman,J., Marinelli,R.J., Wang,P.L., Green,A.E., Nielsen,J.S.,
            Nelson,B.H., Drescher,C.W. and Brown,P.O.
  TITLE     ESRRA-C11orf20 is a recurrent gene fusion in serous ovarian
            carcinoma
  JOURNAL   PLoS Biol 9 (9), e1001156 (2011)
   PUBMED   21949640
  REMARK    GeneRIF: ESRRA-C11orf20, a gene fusion between ESRRA and C11orf20
            (TEX40) is recurrent serous ovarian carcinoma.
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001453.6 and AL117564.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.170070.1,
                                           SRR5189667.254049.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000328404.8/ ENSP00000491717.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..200
                     /product="cation channel sperm-associated auxiliary
                     subunit zeta"
                     /note="testis-expressed sequence 40 protein;
                     testis-expressed protein 40; testis expressed 40;
                     catSperzeta; catSper-zeta; cation channel sperm-associated
                     protein subunit zeta"
                     /calculated_mol_wt=22707
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTU4.1)"
     Region          58..78
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTU4.1)"
     CDS             1..200
                     /gene="CATSPERZ"
                     /gene_synonym="C11orf20; TEX40"
                     /coded_by="NM_001039496.2:54..656"
                     /db_xref="GeneID:25858"
                     /db_xref="HGNC:HGNC:19231"
                     /db_xref="MIM:617511"
ORIGIN      
        1 meekpskvsl kssdrqgsde esvhsdtrdl wttttlsqaq lnmplsevce gfdeegrnis
       61 ktrgwhspgr gsldegykas hkpeeldeha lvelelhrgs smeinlgekd tasqieaeks
      121 ssmsslniak hmphraywae qqsrlplplm elmenealei ltkalrsyql gigrdhfltk
      181 elqryieglk krrskrlyvn
//
LOCUS       NP_001353151             821 aa            linear   PRI 27-APR-2025
DEFINITION  disks large homolog 1 isoform 15 [Homo sapiens].
ACCESSION   NP_001353151 XP_016861311
VERSION     NP_001353151.1
DBSOURCE    REFSEQ: accession NM_001366222.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Veljacic Viskovic,D., Lozic,M., Vukoja,M., Soljic,V., Vukojevic,K.,
            Glavina Durdov,M., Filipovic,N. and Lozic,B.
  TITLE     Spatio-Temporal Expression Pattern of CAKUT Candidate Genes DLG1
            and KIF12 during Human Kidney Development
  JOURNAL   Biomolecules 13 (2), 340 (2023)
   PUBMED   36830709
  REMARK    GeneRIF: Spatio-Temporal Expression Pattern of CAKUT Candidate
            Genes DLG1 and KIF12 during Human Kidney Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 821)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 821)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 821)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 821)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 821)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861311.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.579.1,
                                           SRR1803617.185655.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..821
                     /product="disks large homolog 1 isoform 15"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=90496
     Region          <105..140
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          139..227
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(150..156,173,176,206,210,213..214)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          236..320
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(245..251,268,271,301,305,308..309)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          321..382
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          380..470
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(392..398,409,412,442,446,449..450)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          499..565
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(504,526..527,548)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(507,509,512,521,539..540,559,561..562)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          630..808
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..821
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366222.1:65..2530"
                     /note="isoform 15 is encoded by transcript variant 31"
                     /db_xref="CCDS:CCDS93447.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mnyifgnntl lysrgsrggn tssshgsagp kqkhwakkgs sdelqaepep srwqqivaff
       61 trrhsfidci svatsstqpt eavlpspptv pvipvlpvpa entvilptip qanpppvlvn
      121 tdsletptyv ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga
      181 aaqdgrlrvn dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli
      241 kgpkglgfsi aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt
      301 heeavtalkn tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas
      361 paryspvska vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls
      421 gelrkgdrii svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq
      481 mmnssissgs gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew
      541 wqarqvtpdg esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt
      601 snasdsessy rgqeeyvlsy epvnqqevny trpviilgpm kdrinddlis efpdkfgscv
      661 phttrpkrdy evdgrdyhfv tsreqmekdi qehkfieagq ynnhlygtsv qsvrevaekg
      721 khcildvsgn aikrlqiaql ypisifikpk smenimemnk rlteeqarkt feramkleqe
      781 ftehftaivq gdtlediynq vkqiieeqsg syiwvpakek l
//
LOCUS       NP_001125798             172 aa            linear   PRI 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 [Pongo
            abelii].
ACCESSION   NP_001125798
VERSION     NP_001125798.1
DBSOURCE    REFSEQ: accession NM_001132326.2
KEYWORDS    RefSeq.
SOURCE      Pongo abelii (Sumatran orangutan)
  ORGANISM  Pongo abelii
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Pongo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Mishmar,D., Ruiz-Pesini,E., Mondragon-Palomino,M., Procaccio,V.,
            Gaut,B. and Wallace,D.C.
  TITLE     Adaptive selection of mitochondrial complex I subunits during
            primate radiation
  JOURNAL   Gene 378, 11-18 (2006)
   PUBMED   16828987
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CR859165.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR859165.1, SRR6713218.5034.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2058385, SAMN10521808
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Pongo abelii"
                     /db_xref="taxon:9601"
                     /chromosome="13"
                     /map="13"
     Protein         1..172
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 8"
                     /note="CI-19kD; complex I-19kD; NADH-ubiquinone
                     oxidoreductase 19 kDa subunit; NADH dehydrogenase
                     (ubiquinone) 1 alpha subcomplex, 8, 19kDa"
                     /calculated_mol_wt=20004
     Region          36..46
                     /region_name="Cx9C motif 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (P0CB91.1)"
     Region          56..66
                     /region_name="Cx9C motif 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (P0CB91.1)"
     Region          78..111
                     /region_name="CHCH"
                     /note="CHCH domain; pfam06747"
                     /db_xref="CDD:429096"
     Region          78..88
                     /region_name="Cx9C motif 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (P0CB91.1)"
     Region          100..110
                     /region_name="Cx9C motif 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (P0CB91.1)"
     Region          133..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0CB91.1)"
     CDS             1..172
                     /gene="NDUFA8"
                     /coded_by="NM_001132326.2:76..594"
                     /db_xref="GeneID:100172726"
ORIGIN      
        1 mpgivelptl eelkvdevki ssavlkaaah hygaqcdkpn kefmlcrwee kdprrcleeg
       61 klvnkcaldf frqikrhcae pfteywtcid ytgqqlfrhc rkqqakfdec vldkmgwvrp
      121 dlgelskvtk vktdrplpen pyhsrprpdp speiegdlkp aihgsrfyfw tk
//
LOCUS       NP_006435               1197 aa            linear   PRI 27-APR-2025
DEFINITION  structural maintenance of chromosomes protein 2 [Homo sapiens].
ACCESSION   NP_006435
VERSION     NP_006435.2
DBSOURCE    REFSEQ: accession NM_006444.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   He,Y., Wang,Y., Luo,Z., Zhang,X., Bai,H. and Wang,J.
  TITLE     SMC2 knockdown inhibits malignant progression of lung
            adenocarcinoma by upregulating BTG2 expression
  JOURNAL   Cell Signal 120, 111216 (2024)
   PUBMED   38729325
  REMARK    GeneRIF: SMC2 knockdown inhibits malignant progression of lung
            adenocarcinoma by upregulating BTG2 expression.
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1197)
  AUTHORS   Han,Y.H., Wan,Y., Xiong,H. and Sun,G.L.
  TITLE     Structural maintenance of chromosomes 2 is identified as an
            oncogene in bladder cancer in vitro and in vivo
  JOURNAL   Neoplasma 67 (2), 364-370 (2020)
   PUBMED   31986889
  REMARK    GeneRIF: Structural maintenance of chromosomes 2 is identified as
            an oncogene in bladder cancer in vitro and in vivo.
REFERENCE   5  (residues 1 to 1197)
  AUTHORS   Feng,Y., Liu,H., Duan,B., Liu,Z., Abbruzzese,J., Walsh,K.M.,
            Zhang,X. and Wei,Q.
  TITLE     Potential functional variants in SMC2 and TP53 in the AURORA
            pathway genes and risk of pancreatic cancer
  JOURNAL   Carcinogenesis 40 (4), 521-528 (2019)
   PUBMED   30794721
  REMARK    GeneRIF: Rs3818626 and rs9895829 were significantly associated with
            SMC2 and TP53 messenger RNA expression.
REFERENCE   6  (residues 1 to 1197)
  AUTHORS   Kueng,S., Hegemann,B., Peters,B.H., Lipp,J.J., Schleiffer,A.,
            Mechtler,K. and Peters,J.M.
  TITLE     Wapl controls the dynamic association of cohesin with chromatin
  JOURNAL   Cell 127 (5), 955-967 (2006)
   PUBMED   17113138
REFERENCE   7  (residues 1 to 1197)
  AUTHORS   Cobbe,N. and Heck,M.M.
  TITLE     The evolution of SMC proteins: phylogenetic analysis and structural
            implications
  JOURNAL   Mol Biol Evol 21 (2), 332-347 (2004)
   PUBMED   14660695
REFERENCE   8  (residues 1 to 1197)
  AUTHORS   Przewloka,M.R., Pardington,P.E., Yannone,S.M., Chen,D.J. and
            Cary,R.B.
  TITLE     In vitro and in vivo interactions of DNA ligase IV with a subunit
            of the condensin complex
  JOURNAL   Mol Biol Cell 14 (2), 685-697 (2003)
   PUBMED   12589063
REFERENCE   9  (residues 1 to 1197)
  AUTHORS   Schmiesing,J.A., Gregson,H.C., Zhou,S. and Yokomori,K.
  TITLE     A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a
            homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone
            H3 during the early stage of mitotic chromosome condensation
  JOURNAL   Mol Cell Biol 20 (18), 6996-7006 (2000)
   PUBMED   10958694
REFERENCE   10 (residues 1 to 1197)
  AUTHORS   Schmiesing,J.A., Ball,A.R. Jr., Gregson,H.C., Alderton,J.M.,
            Zhou,S. and Yokomori,K.
  TITLE     Identification of two distinct human SMC protein complexes involved
            in mitotic chromosome dynamics
  JOURNAL   Proc Natl Acad Sci U S A 95 (22), 12906-12911 (1998)
   PUBMED   9789013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL833191.1, BC055081.1, AF092563.1, BC017845.1, BC032705.1,
            AL354938.12, AK124957.1 and BF969462.1.
            
            On Jul 14, 2006 this sequence version replaced NP_006435.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. All variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.176322.1,
                                           SRR1803616.146152.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374793.8/ ENSP00000363925.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.1"
     Protein         1..1197
                     /product="structural maintenance of chromosomes protein 2"
                     /note="structural maintenance of chromosomes (SMC) family
                     member, chromosome-associated protein E; SMC2 (structural
                     maintenance of chromosomes 2, yeast)-like 1; SMC protein
                     2; XCAP-E homolog"
                     /calculated_mol_wt=135526
     Region          2..1167
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; pfam02463"
                     /db_xref="CDD:426784"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95347.2)"
     Site            222
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95347.2)"
     Site            677
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95347.2)"
     Site            1158
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95347.2)"
     Site            1160
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95347.2)"
     CDS             1..1197
                     /gene="SMC2"
                     /gene_synonym="CAP-E; CAPE; SMC-2; SMC2L1"
                     /coded_by="NM_006444.3:231..3824"
                     /db_xref="CCDS:CCDS35086.1"
                     /db_xref="GeneID:10592"
                     /db_xref="HGNC:HGNC:14011"
                     /db_xref="MIM:605576"
ORIGIN      
        1 mhiksiileg fksyaqrtev ngfdplfnai tglngsgksn ildsicfllg isnlsqvras
       61 nlqdlvykng qagitkasvs itfdnsdkkq splgfevhde itvtrqvvig grnkylingv
      121 nanntrvqdl fcsvglnvnn phflimqgri tkvlnmkppe ilsmieeaag trmyeykkia
      181 aqktiekkea klkeiktile eeitptiqkl keerssyley qkvmreiehl srlyiayqfl
      241 laedtkvrsa eelkemqdkv iklqeelsen dkkikalnhe ieelekrkdk etggilrsle
      301 dalaeaqrvn tksqsafdlk kknlaceesk rkeleknmve dsktlaakek evkkitdglh
      361 alqeasnkda ealaaaqqhf navsaglssn edgaeatlag qmmackndis kaqteakqaq
      421 mklkhaqqel knkqaevkkm dsgyrkdqea leavkrlkek leaemkklny eenkeeslle
      481 krrqlsrdig rlketyeall arfpnlrfay kdpeknwnrn cvkglvasli svkdtsatta
      541 lelvagerly nvvvdtevtg kkllergelk rrytiiplnk isarciapet lrvaqnlvgp
      601 dnvhvalslv eykpelqkam efvfgttfvc dnmdnakkva fdkrimtrtv tlggdvfdph
      661 gtlsggarsq aasiltkfqe lkdvqdelri kenelralee elaglkntae kyrqlkqqwe
      721 mkteeadllq tklqqssyhk qqeeldalkk tieeseetlk ntkeiqrkae ekyevlenkm
      781 knaeaerere lkdaqkkldc aktkadassk kmkekqqeve aitleleelk rehtsykqql
      841 eavneaiksy esqievmaae vaknkesvnk aqeevtkqke vitaqdtvik akyaevakhk
      901 eqnndsqlki keldhniskh kreaedgaak vskmlkdydw inaerhlfgq pnsaydfktn
      961 npkeagqrlq klqemkeklg rnvnmramnv lteaeerynd lmkkkriven dkskilttie
     1021 dldqkknqal niawqkvnkd fgsifstllp ganamlappe gqtvldglef kvalgntwke
     1081 nltelsggqr slvalslils mllfkpapiy ildevdaald lshtqnigqm lrthfthsqf
     1141 ivvslkegmf nnanvlfktk fvdgvstvar ftqcqngkis keakskakpp kgahvev
//
LOCUS       NP_079388                858 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein ZXDC isoform 1 [Homo sapiens].
ACCESSION   NP_079388 XP_371661
VERSION     NP_079388.3
DBSOURCE    REFSEQ: accession NM_025112.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Liu,Y., Huang,Y., Zhang,X., Ma,X., He,X., Gan,C., Zou,X., Wang,S.,
            Shu,K., Lei,T. and Zhang,H.
  TITLE     CircZXDC Promotes Vascular Smooth Muscle Cell Transdifferentiation
            via Regulating miRNA-125a-3p/ABCC6 in Moyamoya Disease
  JOURNAL   Cells 11 (23), 3792 (2022)
   PUBMED   36497052
  REMARK    GeneRIF: CircZXDC Promotes Vascular Smooth Muscle Cell
            Transdifferentiation via Regulating miRNA-125a-3p/ABCC6 in Moyamoya
            Disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 858)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 858)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 858)
  AUTHORS   Suter,B., Fontaine,J.F., Yildirimman,R., Rasko,T., Schaefer,M.H.,
            Rasche,A., Porras,P., Vazquez-Alvarez,B.M., Russ,J., Rau,K.,
            Foulle,R., Zenkner,M., Saar,K., Herwig,R., Andrade-Navarro,M.A. and
            Wanker,E.E.
  TITLE     Development and application of a DNA microarray-based yeast
            two-hybrid system
  JOURNAL   Nucleic Acids Res 41 (3), 1496-1507 (2013)
   PUBMED   23275563
REFERENCE   7  (residues 1 to 858)
  AUTHORS   Aleksandrova,A., Galkin,O., Koneni,R. and Fontes,J.D.
  TITLE     An N- and C-terminal truncated isoform of zinc finger X-linked
            duplicated C protein represses MHC class II transcription
  JOURNAL   Mol Cell Biochem 337 (1-2), 1-7 (2010)
   PUBMED   19777325
  REMARK    GeneRIF: Role of ZXD proteins in regulating MHC II transcription.
REFERENCE   8  (residues 1 to 858)
  AUTHORS   Jambunathan,S. and Fontes,J.D.
  TITLE     Sumoylation of the zinc finger protein ZXDC enhances the function
            of its transcriptional activation domain
  JOURNAL   Biol Chem 388 (9), 965-972 (2007)
   PUBMED   17696781
  REMARK    GeneRIF: study found sumoylation does not appear to disrupt or
            modulate interaction of ZXDC with binding partners; sumoylation of
            ZXDC is required for full activity of transcriptional activation
            domain; study suggests sumoylation is an important regulator of
            ZXDC
REFERENCE   9  (residues 1 to 858)
  AUTHORS   Al-Kandari,W., Koneni,R., Navalgund,V., Aleksandrova,A.,
            Jambunathan,S. and Fontes,J.D.
  TITLE     The zinc finger proteins ZXDA and ZXDC form a complex that binds
            CIITA and regulates MHC II gene transcription
  JOURNAL   J Mol Biol 369 (5), 1175-1187 (2007)
   PUBMED   17493635
  REMARK    GeneRIF: ZXDA and ZXDC form an important regulatory complex for MHC
            II gene transcription.
REFERENCE   10 (residues 1 to 858)
  AUTHORS   Al-Kandari,W., Jambunathan,S., Navalgund,V., Koneni,R., Freer,M.,
            Parimi,N., Mudhasani,R. and Fontes,J.D.
  TITLE     ZXDC, a novel zinc finger protein that binds CIITA and activates
            MHC gene transcription
  JOURNAL   Mol Immunol 44 (4), 311-321 (2007)
   PUBMED   16600381
  REMARK    GeneRIF: ZXDC is an important regulator of both MHC class I and
            class II transcription
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC024558.21 and DQ079590.1.
            
            On May 18, 2006 this sequence version replaced NP_079388.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ079590.1, AY936556.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389709.8/ ENSP00000374359.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.3"
     Protein         1..858
                     /product="zinc finger protein ZXDC isoform 1"
                     /note="zinc finger protein ZXDC; SERH2790; ZXD-like zinc
                     finger protein"
                     /calculated_mol_wt=89858
     Region          1..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2QGD7.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2QGD7.2)"
     Region          151..174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2QGD7.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2QGD7.2)"
     Region          177..199
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(184,186,188,190..191,194..195,198,217,219,223..224,
                     227..228,231,247,249,251,253..254,257..258,261)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <204..260
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          210..232
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          240..317
                     /region_name="zf-C2H2_8"
                     /note="C2H2-type zinc ribbon; pfam15909"
                     /db_xref="CDD:464935"
     Region          240..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <284..443
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          299..321
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          333..352
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(337,339,341,343..344,347..348,351,367,369,373..374,
                     377..378,381,397,399,401,403..404,407..408,411)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          360..382
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          390..412
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          391..>584
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          420..442
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          579..688
                     /region_name="Required for transcriptional activation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2QGD7.2)"
     Region          660..696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2QGD7.2)"
     Site            665
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q2QGD7.2)"
     Region          726..756
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2QGD7.2)"
     Region          781..858
                     /region_name="Interaction with CIITA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2QGD7.2)"
     Region          837..858
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2QGD7.2)"
     CDS             1..858
                     /gene="ZXDC"
                     /gene_synonym="ZXDL"
                     /coded_by="NM_025112.5:27..2603"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43145.1"
                     /db_xref="GeneID:79364"
                     /db_xref="HGNC:HGNC:28160"
                     /db_xref="MIM:615746"
ORIGIN      
        1 mdlpallpap targgqhggg pgplrrapap lgasparrrl llvrgpedgg pgarpgeasg
       61 pspppaedds dgdsflvlle vphggaaaea agsqeaepgs rvnlasrpeq gpsgpaappg
      121 pgvapagavt issqdllvrl drgvlalsap pgpatagaaa prrapqasgp stpgyrcpep
      181 qcalafakkh qlkvhllthg ggqgrrpfkc plegcgwaft tsyklkrhlq shdklrpfgc
      241 pvggcgkkft tvynlkahmk gheqeslfkc evcaerfpth aklsshqrsh feperpykcd
      301 fpgcektfit vsalfshnra hfreqelfsc sfpgcskqyd kacrlkihlr shtgerpfic
      361 dsdscgwtft smskllrhrr khdddrrftc pvegcgksft raehlkghsi thlgtkpfec
      421 pvegccarfs arsslyihsk khvqdvgapk srcpvstcnr lftskhsmka hmvrqhsrrq
      481 dllpqleaps sltpsselss pgqseltnmd laalfsdtpa nasgsaggsd ealnsgilti
      541 dvtsvssslg gnlpannssl gpmeplvlva hsdippslds plvlgtaatv lqqgsfsvdd
      601 vqtvsagalg clvalpmknl sddplaltsn snlaahittp tssstprena svpellapik
      661 vepdspsrpg avgqqegshg lpqstlpspa eqhgaqdtel sagtgnfyle sggsartdyr
      721 aiqlakekkq rgagsnagas qstqrkikeg kmspphfhas qnswlcgslv vpsggrpgpa
      781 paagvqcgaq gvqvqlvqdd psgegvlpsa rgpatflpfl tvdlpvyvlq evlpssggpa
      841 gpeatqfpgs tinlqdlq
//
LOCUS       NP_001356858             700 aa            linear   PRI 27-APR-2025
DEFINITION  activating signal cointegrator 1 complex subunit 2 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001356858
VERSION     NP_001356858.1
DBSOURCE    REFSEQ: accession NM_001369929.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Narita,M., Denk,T., Matsuo,Y., Sugiyama,T., Kikuguchi,C., Ito,S.,
            Sato,N., Suzuki,T., Hashimoto,S., Machova,I., Tesina,P.,
            Beckmann,R. and Inada,T.
  TITLE     A distinct mammalian disome collision interface harbors K63-linked
            polyubiquitination of uS10 to trigger hRQT-mediated subunit
            dissociation
  JOURNAL   Nat Commun 13 (1), 6411 (2022)
   PUBMED   36302773
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 700)
  AUTHORS   Yang,Y. and Xu,X.
  TITLE     Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration
  JOURNAL   Aging (Albany NY) 13 (6), 8306-8319 (2021)
   PUBMED   33686958
  REMARK    GeneRIF: Identification of key genes in coronary artery disease: an
            integrative approach based on weighted gene co-expression network
            analysis and their correlation with immune infiltration.
REFERENCE   4  (residues 1 to 700)
  AUTHORS   Jia,J., Absmeier,E., Holton,N., Pietrzyk-Brzezinska,A.J.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T. and Wahl,M.C.
  TITLE     The interaction of DNA repair factors ASCC2 and ASCC3 is affected
            by somatic cancer mutations
  JOURNAL   Nat Commun 11 (1), 5535 (2020)
   PUBMED   33139697
  REMARK    GeneRIF: The interaction of DNA repair factors ASCC2 and ASCC3 is
            affected by somatic cancer mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 700)
  AUTHORS   Juszkiewicz,S., Speldewinde,S.H., Wan,L., Svejstrup,J.Q. and
            Hegde,R.S.
  TITLE     The ASC-1 Complex Disassembles Collided Ribosomes
  JOURNAL   Mol Cell 79 (4), 603-614 (2020)
   PUBMED   32579943
REFERENCE   6  (residues 1 to 700)
  AUTHORS   Soll,J.M., Brickner,J.R., Mudge,M.C. and Mosammaparast,N.
  TITLE     RNA ligase-like domain in activating signal cointegrator 1 complex
            subunit 1 (ASCC1) regulates ASCC complex function during alkylation
            damage
  JOURNAL   J Biol Chem 293 (35), 13524-13533 (2018)
   PUBMED   29997253
REFERENCE   7  (residues 1 to 700)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 700)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   9  (residues 1 to 700)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 700)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82171.2 and AC004882.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.81774.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..700
                     /product="activating signal cointegrator 1 complex subunit
                     2 isoform 7"
                     /note="ASC-1 complex subunit P100; trip4 complex subunit
                     p100"
                     /calculated_mol_wt=79468
     Region          416..455
                     /region_name="CUE_ASCC2"
                     /note="CUE domain found in activating signal cointegrator
                     1 complex subunit 2 (ASCC2) and similar proteins; cd14364"
                     /db_xref="CDD:270547"
     CDS             1..700
                     /gene="ASCC2"
                     /gene_synonym="ASC1p100; p100"
                     /coded_by="NM_001369929.1:115..2217"
                     /note="isoform 7 is encoded by transcript variant 12"
                     /db_xref="GeneID:84164"
                     /db_xref="HGNC:HGNC:24103"
                     /db_xref="MIM:614216"
ORIGIN      
        1 mpalpldqlq ithkdpktgk lrtspalvif detlqkclds ylryvprkfd egvasapevv
       61 dmqkrlhrsv fltflrmsth keskdhfisp safgeilynn flfdipkild lcvlfgkgns
      121 pllqkmigni ftqqpsyysd ldetlptilq vfsnilqhcg lqgdganttp qkleergrlt
      181 psdmpllelk divlylcdtc ttlwafldif placqtfqkh dfcyrlasfy eaaipemesa
      241 ikkrrledsk llgdlwqrls hsrkklmeif hiilnqicll pilesscdni qgfieeflqi
      301 fssllqekrf lrdydalfpv aedisllqqa ssvldetrta yilqavesaw egvdrrkatd
      361 akdpsvieep ngepngvtvt aeavsqassh penseeeecm gaaaavgpam cgveldslis
      421 qvkdllpdlg egfilacley yhydpeqvin nileerlapt lsqldrnldr emkpdptpll
      481 tsrhnvfqnd efdvfsrdsv dlsrvhkgks trkeentrsl lndkravaaq rqryeqysvv
      541 veepgeslpy hsvyyedeyd dtydgnqvga ndadsddeli srrpftipqv lrtkvpregq
      601 eeddddeedd adeeapkpdh fvqdpavlre kaearrmafl akkgyrhdss tavagsprgh
      661 gqsrettqer rkkeankatr anhnrrtmad rkrskgmips
//
LOCUS       NP_004719                783 aa            linear   PRI 27-APR-2025
DEFINITION  nucleolar RNA helicase 2 isoform 1 [Homo sapiens].
ACCESSION   NP_004719
VERSION     NP_004719.2
DBSOURCE    REFSEQ: accession NM_004728.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Tang,W., Yang,Y., Fu,Z., Xu,W., Ou,W., Liu,F., Du,P. and Liu,C.Y.
  TITLE     The RNA helicase DDX21 activates YAP to promote tumorigenesis and
            is transcriptionally upregulated by beta-catenin in colorectal
            cancer
  JOURNAL   Oncogene 43 (44), 3227-3239 (2024)
   PUBMED   39285230
  REMARK    GeneRIF: The RNA helicase DDX21 activates YAP to promote
            tumorigenesis and is transcriptionally upregulated by beta-catenin
            in colorectal cancer.
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 783)
  AUTHORS   Zhang,G., Yang,R., Wang,B., Yan,Q., Zhao,P., Zhang,J., Su,W.,
            Yang,L. and Cui,H.
  TITLE     TRIP13 regulates progression of gastric cancer through stabilising
            the expression of DDX21
  JOURNAL   Cell Death Dis 15 (8), 622 (2024)
   PUBMED   39187490
  REMARK    GeneRIF: TRIP13 regulates progression of gastric cancer through
            stabilising the expression of DDX21.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 783)
  AUTHORS   Jiang,Y., Sun,S., Liu,X., Su,K., Zhang,C., Zhang,P., Zhao,Z.,
            Su,Y., Wang,C. and Du,X.
  TITLE     U3 snoRNA inter-regulates with DDX21 in the perichromosomal region
            to control mitosis
  JOURNAL   Cell Death Dis 15 (5), 342 (2024)
   PUBMED   38760378
  REMARK    GeneRIF: U3 snoRNA inter-regulates with DDX21 in the
            perichromosomal region to control mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 783)
  AUTHORS   Valdez,B.C., Yang,H., Hong,E. and Sequitin,A.M.
  TITLE     Genomic structure of newly identified paralogue of RNA helicase
            II/Gu: detection of pseudogenes and multiple alternatively spliced
            mRNAs
  JOURNAL   Gene 284 (1-2), 53-61 (2002)
   PUBMED   11891046
REFERENCE   6  (residues 1 to 783)
  AUTHORS   Zhu,K., Henning,D., Valdez,B. and Busch,H.
  TITLE     Human RNA helicase II/Gu gene: genomic organization and promoter
            analysis
  JOURNAL   Biochem Biophys Res Commun 281 (4), 1006-1011 (2001)
   PUBMED   11237763
REFERENCE   7  (residues 1 to 783)
  AUTHORS   Valdez,B.C. and Wang,W.
  TITLE     Mouse RNA helicase II/Gu: cDNA and genomic sequences, chromosomal
            localization, and regulation of expression
  JOURNAL   Genomics 66 (2), 184-194 (2000)
   PUBMED   10860663
REFERENCE   8  (residues 1 to 783)
  AUTHORS   Valdez,B.C., Henning,D., Perumal,K. and Busch,H.
  TITLE     RNA-unwinding and RNA-folding activities of RNA helicase II/Gu--two
            activities in separate domains of the same protein
  JOURNAL   Eur J Biochem 250 (3), 800-807 (1997)
   PUBMED   9461305
REFERENCE   9  (residues 1 to 783)
  AUTHORS   Valdez,B.C., Henning,D., Perlaky,L., Busch,R.K. and Busch,H.
  TITLE     Cloning and characterization of Gu/RH-II binding protein
  JOURNAL   Biochem Biophys Res Commun 234 (2), 335-340 (1997)
   PUBMED   9177271
REFERENCE   10 (residues 1 to 783)
  AUTHORS   Valdez,B.C., Henning,D., Busch,R.K., Woods,K., Flores-Rozas,H.,
            Hurwitz,J., Perlaky,L. and Busch,H.
  TITLE     A nucleolar RNA helicase recognized by autoimmune antibodies from a
            patient with watermelon stomach disease
  JOURNAL   Nucleic Acids Res 24 (7), 1220-1224 (1996)
   PUBMED   8614622
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DW408689.1, BC008071.2,
            AL359844.15 and AA446317.1.
            
            On Jul 27, 2004 this sequence version replaced NP_004719.1.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. This gene encodes a DEAD box protein,
            which is an antigen recognized by autoimmune antibodies from a
            patient with watermelon stomach disease. This protein unwinds
            double-stranded RNA, folds single-stranded RNA, and may play
            important roles in ribosomal RNA biogenesis, RNA editing, RNA
            transport, and general transcription. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009432.1, SRR1660803.2314.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354185.9/ ENSP00000346120.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..783
                     /product="nucleolar RNA helicase 2 isoform 1"
                     /EC_number="3.6.4.13"
                     /note="Gu protein; RNA helicase II/Gu alpha; DEAD/H
                     (Asp-Glu-Ala-Asp/His) box polypeptide 21; nucleolar RNA
                     helicase 2; DEAD box protein 21; nucleolar RNA helicase
                     Gu; DEAD (Asp-Glu-Ala-Asp) box helicase 21; nucleolar RNA
                     helicase II; DEAD-box helicase 21"
                     /calculated_mol_wt=87214
     Region          1..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            18
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:28790157; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:28790157; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Region          186..214
                     /region_name="Q motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00552"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR30.5)"
     Region          188..574
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Region          339..342
                     /region_name="DEAD box.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            600
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:28790157; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     Region          617..709
                     /region_name="GUCT_RHII_Gualpha_beta"
                     /note="RNA-binding GUCT domain found in vertebrate RNA
                     helicase II/Gualpha (RH-II/Gualpha), RNA helicase
                     II/Gubeta (RH-II/Gubeta) and similar proteins; cd12936"
                     /db_xref="CDD:240593"
     Region          708..783
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR30.5)"
     Region          718..>771
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
     Region          724..748
                     /region_name="3 X 5 AA repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR30.5)"
     Site            779
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NR30.5)"
     CDS             1..783
                     /gene="DDX21"
                     /gene_synonym="gu-alpha; GUA; GURDB; II/Gu; RH; RH II/Gu;
                     RH-II/GU; RH-II/GuA"
                     /coded_by="NM_004728.4:57..2408"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31211.1"
                     /db_xref="GeneID:9188"
                     /db_xref="HGNC:HGNC:2744"
                     /db_xref="MIM:606357"
ORIGIN      
        1 mpgklrsdag lesdtamkkg etlrkqteek ekkekpksdk teeiaeeeet vfpkakqvkk
       61 kaepsevdmn spkskkakkk eepsqndisp ktkslrkkke piekkvvssk tkkvtkneep
      121 seeeidapkp kkmkkekemn getrekspkl kngfphpepd cnpseaasee snseieqeip
      181 veqkegafsn fpiseetikl lkgrgvtflf piqaktfhhv ysgkdliaqa rtgtgktfsf
      241 aiplieklhg elqdrkrgra pqvlvlaptr elanqvskdf sditkklsva cfyggtpygg
      301 qfermrngid ilvgtpgrik dhiqngkldl tklkhvvlde vdqmldmgfa dqveeilsva
      361 ykkdsednpq tllfsatcph wvfnvakkym kstyeqvdli gkktqktait vehlaikchw
      421 tqraavigdv irvysghqgr tiifcetkke aqelsqnsai kqdaqslhgd ipqkqreitl
      481 kgfrngsfgv lvatnvaarg ldipevdlvi qssppkdves yihrsgrtgr agrtgvcicf
      541 yqhkeeyqlv qveqkagikf krigvpsate iikasskdai rlldsvppta ishfkqsaek
      601 lieekgavea laaalahisg atsvdqrsli nsnvgfvtmi lqcsiempni syawkelkeq
      661 lgeeidskvk gmvflkgklg vcfdvptasv teiqekwhds rrwqlsvate qpelegpreg
      721 yggfrgqreg srgfrgqrdg nrrfrgqreg srgprgqrsg ggnksnrsqn kgqkrsfska
      781 fgq
//
LOCUS       NP_002552                422 aa            linear   PRI 27-APR-2025
DEFINITION  P2X purinoceptor 5 isoform A [Homo sapiens].
ACCESSION   NP_002552
VERSION     NP_002552.2
DBSOURCE    REFSEQ: accession NM_002561.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Abramowski,P., Ogrodowczyk,C., Martin,R. and Pongs,O.
  TITLE     A truncation variant of the cation channel P2RX5 is upregulated
            during T cell activation
  JOURNAL   PLoS One 9 (9), e104692 (2014)
   PUBMED   25181038
  REMARK    GeneRIF: These data indicate a functional role of the human P2RX5
            splice variant in T cell activation and immunoregulation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Ussar,S., Lee,K.Y., Dankel,S.N., Boucher,J., Haering,M.F.,
            Kleinridders,A., Thomou,T., Xue,R., Macotela,Y., Cypess,A.M.,
            Tseng,Y.H., Mellgren,G. and Kahn,C.R.
  TITLE     ASC-1, PAT2, and P2RX5 are cell surface markers for white, beige,
            and brown adipocytes
  JOURNAL   Sci Transl Med 6 (247), 247ra103 (2014)
   PUBMED   25080478
  REMARK    GeneRIF: The amino acid transporter PAT2 and the purinergic
            receptor P2RX5 are cell surface markers expressed in classical
            brown and beige adipocytes.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Sterle,I., Zupancic,D. and Romih,R.
  TITLE     Correlation between urothelial differentiation and sensory proteins
            P2X3, P2X5, TRPV1, and TRPV4 in normal urothelium and papillary
            carcinoma of human bladder
  JOURNAL   Biomed Res Int 2014, 805236 (2014)
   PUBMED   24868547
  REMARK    GeneRIF: sensory proteins P2X3 and TRPV1 are in correlation with
            urothelial differentiation, while P2X5 and TRPV4 have unique
            expression patterns
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Duckwitz,W., Hausmann,R., Aschrafi,A. and Schmalzing,G.
  TITLE     P2X5 subunit assembly requires scaffolding by the second
            transmembrane domain and a conserved aspartate
  JOURNAL   J Biol Chem 281 (51), 39561-39572 (2006)
   PUBMED   17001079
  REMARK    GeneRIF: analysis of topology, helix-helix interactions, and
            oligomerization of P2X5 subunits
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Greig,A.V., Linge,C., Terenghi,G., McGrouther,D.A. and Burnstock,G.
  TITLE     Purinergic receptors are part of a functional signaling system for
            proliferation and differentiation of human epidermal keratinocytes
  JOURNAL   J Invest Dermatol 120 (6), 1007-1015 (2003)
   PUBMED   12787128
  REMARK    GeneRIF: Different purinergic receptors have different functional
            roles in human epidermis with P2Y1 and P2Y2 receptors controlling
            proliferation, while P2X5 and P2X7 receptors control early
            differentiation, terminal differentiation and death of
            keratinocytes.
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Bo,X., Jiang,L.H., Wilson,H.L., Kim,M., Burnstock,G., Surprenant,A.
            and North,R.A.
  TITLE     Pharmacological and biophysical properties of the human P2X5
            receptor
  JOURNAL   Mol Pharmacol 63 (6), 1407-1416 (2003)
   PUBMED   12761352
REFERENCE   8  (residues 1 to 422)
  AUTHORS   North,R.A.
  TITLE     Molecular physiology of P2X receptors
  JOURNAL   Physiol Rev 82 (4), 1013-1067 (2002)
   PUBMED   12270951
  REMARK    Review article
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Touchman,J.W., Anikster,Y., Dietrich,N.L., Maduro,V.V.,
            McDowell,G., Shotelersuk,V., Bouffard,G.G.,
            Beckstrom-Sternberg,S.M., Gahl,W.A. and Green,E.D.
  TITLE     The genomic region encompassing the nephropathic cystinosis gene
            (CTNS): complete sequencing of a 200-kb segment and discovery of a
            novel gene within the common cystinosis-causing deletion
  JOURNAL   Genome Res 10 (2), 165-173 (2000)
   PUBMED   10673275
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Le,K.T., Paquet,M., Nouel,D., Babinski,K. and Seguela,P.
  TITLE     Primary structure and expression of a naturally truncated human P2X
            ATP receptor subunit from brain and immune system
  JOURNAL   FEBS Lett 418 (1-2), 195-199 (1997)
   PUBMED   9414125
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290889.1 and AA805176.1.
            
            On Feb 19, 2003 this sequence version replaced NP_002552.1.
            
            Summary: The product of this gene belongs to the family of
            purinoceptors for ATP. This receptor functions as a ligand-gated
            ion channel. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream gene, TAX1BP3 (Tax1 binding protein
            3). [provided by RefSeq, Mar 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (A).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC016917.1, SRR1163655.362604.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000225328.10/ ENSP00000225328.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..422
                     /product="P2X purinoceptor 5 isoform A"
                     /note="P2X purinoceptor 5; ionotropic ATP receptor P2X5;
                     ATP receptor subunit; lymphoid-restricted
                     histocompatibility antigen-1; purinergic receptor P2X,
                     ligand gated ion channel, 5"
                     /calculated_mol_wt=47074
     Region          1..351
                     /region_name="P2X"
                     /note="cation transporter protein; TIGR00863"
                     /db_xref="CDD:273307"
     CDS             1..422
                     /gene="P2RX5"
                     /gene_synonym="LRH-1; P2X5; P2X5R"
                     /coded_by="NM_002561.4:151..1419"
                     /note="isoform A is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11034.1"
                     /db_xref="GeneID:5026"
                     /db_xref="HGNC:HGNC:8536"
                     /db_xref="MIM:602836"
ORIGIN      
        1 mgqagckglc lslfdyktek yviaknkkvg llyrllqasi laylvvwvfl ikkgyqdvdt
       61 slqsavitkv kgvaftntsd lgqriwdvad yvipaqgenv ffvvtnlivt pnqrqnvcae
      121 negipdgacs kdsdchagea vtagngvktg rclrrenlar gtceifawcp letssrpeep
      181 flkeaedfti fiknhirfpk fnfsksnvmd vkdrsflksc hfgpknhycp ifrlgsvirw
      241 agsdfqdial eggviginie wncdldkaas echphysfsr ldnklsksvs sgynfrfary
      301 yrdaagvefr tlmkaygirf dvmvngkgaf fcdlvliyli kkrefyrdkk yeevrgleds
      361 sqeaedeasg lglseqltsg pgllgmpeqq elqeppeakr gsssqkgngs vcpqllephr
      421 st
//
LOCUS       NP_060358                579 aa            linear   PRI 27-APR-2025
DEFINITION  acyl-coenzyme A synthetase ACSM5, mitochondrial isoform 1 [Homo
            sapiens].
ACCESSION   NP_060358 XP_942394 XP_948339
VERSION     NP_060358.2
DBSOURCE    REFSEQ: accession NM_017888.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Yang,L., Pham,K., Xi,Y., Jiang,S., Robertson,K.D. and Liu,C.
  TITLE     Acyl-CoA Synthetase Medium-Chain Family Member 5-Mediated Fatty
            Acid Metabolism Dysregulation Promotes the Progression of
            Hepatocellular Carcinoma
  JOURNAL   Am J Pathol 194 (10), 1951-1966 (2024)
   PUBMED   39069168
  REMARK    GeneRIF: Acyl-CoA Synthetase Medium-Chain Family Member 5-Mediated
            Fatty Acid Metabolism Dysregulation Promotes the Progression of
            Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Cao,Y., Zhan,Y., Qiu,S., Chen,Z., Gong,K., Ni,S. and Duan,Y.
  TITLE     Integrative analysis of genome-wide DNA methylation and
            single-nucleotide polymorphism identified ACSM5 as a suppressor of
            lumbar ligamentum flavum hypertrophy
  JOURNAL   Arthritis Res Ther 23 (1), 251 (2021)
   PUBMED   34593020
  REMARK    GeneRIF: Integrative analysis of genome-wide DNA methylation and
            single-nucleotide polymorphism identified ACSM5 as a suppressor of
            lumbar ligamentum flavum hypertrophy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Shin,S.Y., Fauman,E.B., Petersen,A.K., Krumsiek,J., Santos,R.,
            Huang,J., Arnold,M., Erte,I., Forgetta,V., Yang,T.P., Walter,K.,
            Menni,C., Chen,L., Vasquez,L., Valdes,A.M., Hyde,C.L., Wang,V.,
            Ziemek,D., Roberts,P., Xi,L., Grundberg,E., Waldenberger,M.,
            Richards,J.B., Mohney,R.P., Milburn,M.V., John,S.L., Trimmer,J.,
            Theis,F.J., Overington,J.P., Suhre,K., Brosnan,M.J., Gieger,C.,
            Kastenmuller,G., Spector,T.D. and Soranzo,N.
  CONSRTM   Multiple Tissue Human Expression Resource (MuTHER) Consortium
  TITLE     An atlas of genetic influences on human blood metabolites
  JOURNAL   Nat Genet 46 (6), 543-550 (2014)
   PUBMED   24816252
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Kottgen,A., Pattaro,C., Boger,C.A., Fuchsberger,C., Olden,M.,
            Glazer,N.L., Parsa,A., Gao,X., Yang,Q., Smith,A.V., O'Connell,J.R.,
            Li,M., Schmidt,H., Tanaka,T., Isaacs,A., Ketkar,S., Hwang,S.J.,
            Johnson,A.D., Dehghan,A., Teumer,A., Pare,G., Atkinson,E.J.,
            Zeller,T., Lohman,K., Cornelis,M.C., Probst-Hensch,N.M.,
            Kronenberg,F., Tonjes,A., Hayward,C., Aspelund,T., Eiriksdottir,G.,
            Launer,L.J., Harris,T.B., Rampersaud,E., Mitchell,B.D.,
            Arking,D.E., Boerwinkle,E., Struchalin,M., Cavalieri,M.,
            Singleton,A., Giallauria,F., Metter,J., de Boer,I.H.,
            Haritunians,T., Lumley,T., Siscovick,D., Psaty,B.M.,
            Zillikens,M.C., Oostra,B.A., Feitosa,M., Province,M., de
            Andrade,M., Turner,S.T., Schillert,A., Ziegler,A., Wild,P.S.,
            Schnabel,R.B., Wilde,S., Munzel,T.F., Leak,T.S., Illig,T.,
            Klopp,N., Meisinger,C., Wichmann,H.E., Koenig,W., Zgaga,L.,
            Zemunik,T., Kolcic,I., Minelli,C., Hu,F.B., Johansson,A., Igl,W.,
            Zaboli,G., Wild,S.H., Wright,A.F., Campbell,H., Ellinghaus,D.,
            Schreiber,S., Aulchenko,Y.S., Felix,J.F., Rivadeneira,F.,
            Uitterlinden,A.G., Hofman,A., Imboden,M., Nitsch,D.,
            Brandstatter,A., Kollerits,B., Kedenko,L., Magi,R., Stumvoll,M.,
            Kovacs,P., Boban,M., Campbell,S., Endlich,K., Volzke,H.,
            Kroemer,H.K., Nauck,M., Volker,U., Polasek,O., Vitart,V.,
            Badola,S., Parker,A.N., Ridker,P.M., Kardia,S.L., Blankenberg,S.,
            Liu,Y., Curhan,G.C., Franke,A., Rochat,T., Paulweber,B.,
            Prokopenko,I., Wang,W., Gudnason,V., Shuldiner,A.R., Coresh,J.,
            Schmidt,R., Ferrucci,L., Shlipak,M.G., van Duijn,C.M., Borecki,I.,
            Kramer,B.K., Rudan,I., Gyllensten,U., Wilson,J.F., Witteman,J.C.,
            Pramstaller,P.P., Rettig,R., Hastie,N., Chasman,D.I., Kao,W.H.,
            Heid,I.M. and Fox,C.S.
  TITLE     New loci associated with kidney function and chronic kidney disease
  JOURNAL   Nat Genet 42 (5), 376-384 (2010)
   PUBMED   20383146
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Watkins,P.A., Maiguel,D., Jia,Z. and Pevsner,J.
  TITLE     Evidence for 26 distinct acyl-coenzyme A synthetase genes in the
            human genome
  JOURNAL   J Lipid Res 48 (12), 2736-2750 (2007)
   PUBMED   17762044
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC016703.1, AK000588.1, BX505437.1, AV648626.1, AV696798.1,
            AV653851.1 and AC137056.3.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_942394.1, XP_948339.1, NP_060358.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068516.1, SRR1660803.108749.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000331849.8/
                                                  ENSP00000327916.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..579
                     /product="acyl-coenzyme A synthetase ACSM5, mitochondrial
                     isoform 1"
                     /EC_number="6.2.1.2"
                     /note="acyl-coenzyme A synthetase ACSM5, mitochondrial"
                     /calculated_mol_wt=61747
     transit_peptide 1..26
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q6NUN0.2)"
                     /calculated_mol_wt=3032
     mat_peptide     27..579
                     /product="Acyl-coenzyme A synthetase ACSM5, mitochondrial.
                     /id=PRO_0000306101"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NUN0.2)"
                     /calculated_mol_wt=61747
     Region          49..577
                     /region_name="MACS_euk"
                     /note="Eukaryotic Medium-chain acyl-CoA synthetase (MACS
                     or ACSM); cd05928"
                     /db_xref="CDD:341251"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BGA8; propagated from
                     UniProtKB/Swiss-Prot (Q6NUN0.2)"
     Site            order(148,275..277,300,320,322,326,346..349,368..373,
                     376..377,392,455,467,470,476,478..481,510,541,546..547,
                     549,551)
                     /site_type="active"
                     /db_xref="CDD:341251"
     Site            152
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BGA8; propagated from
                     UniProtKB/Swiss-Prot (Q6NUN0.2)"
     Site            order(227,230..235,237..238)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341251"
     Site            order(271,322..323,326,346,478..480,541,547)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341251"
     Site            303
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BGA8; propagated from
                     UniProtKB/Swiss-Prot (Q6NUN0.2)"
     Site            order(346..349,368..373,392,455,467,470,476,481)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341251"
     CDS             1..579
                     /gene="ACSM5"
                     /coded_by="NM_017888.3:148..1887"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10585.1"
                     /db_xref="GeneID:54988"
                     /db_xref="HGNC:HGNC:26060"
                     /db_xref="MIM:614361"
ORIGIN      
        1 mrpwlrhlvl qalrnsrafc gshgkpaplp vpqkivatwe aislgrqlvp eyfnfahdvl
       61 dvwsrleeag hrppnpafww vngtgaeikw sfeelgkqsr kaanvlggac glqpgdrmml
      121 vlprlpewwl vsvacmrtgt vmipgvtqlt ekdlkyrlqa sraksiitsd slaprvdais
      181 aecpslqtkl lvsdssrpgw lnfrellrea stehncmrtk srdplaiyft sgttgapkmv
      241 ehsqssyglg fvasgrrwva ltesdifwnt tdtgwvkaaw tlfsawpngs cifvhelprv
      301 dakvilntls kfpittlccv ptifrllvqe dltryqfqsl rhcltggeal npdvrekwkh
      361 qtgvelyegy gqsetvvica npkgmkiksg smgkasppyd vqivddegnv lppgeegnva
      421 vrirptrpfc ffncyldnpe ktaaseqgdf yitgdrarmd kdgyfwfmgr nddvinsssy
      481 rigpvevesa laehpavles avvsspdpir gevvkafivl tpaysshdpe altrelqehv
      541 krvtapykyp rkvafvselp ktvsgkiqrs klrsqewgk
//
LOCUS       NP_001888               2322 aa            linear   PRI 27-APR-2025
DEFINITION  chondroitin sulfate proteoglycan 4 precursor [Homo sapiens].
ACCESSION   NP_001888
VERSION     NP_001888.2
DBSOURCE    REFSEQ: accession NM_001897.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2322)
  AUTHORS   Uno,K., Koya,Y., Yoshihara,M., Iyoshi,S., Kitami,K., Sugiyama,M.,
            Miyamoto,E., Mogi,K., Fujimoto,H., Yamakita,Y., Wang,X., Nawa,A.
            and Kajiyama,H.
  TITLE     Chondroitin Sulfate Proteoglycan 4 Provides New Treatment Approach
            to Preventing Peritoneal Dissemination in Ovarian Cancer
  JOURNAL   Int J Mol Sci 25 (3), 1626 (2024)
   PUBMED   38338902
  REMARK    GeneRIF: Chondroitin Sulfate Proteoglycan 4 Provides New Treatment
            Approach to Preventing Peritoneal Dissemination in Ovarian Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2322)
  AUTHORS   Bagheri Varzaneh,M., Zhao,Y., Rozynek,J., Han,M. and Reed,D.A.
  TITLE     Disrupting mechanical homeostasis promotes matrix
            metalloproteinase-13 mediated processing of neuron glial antigen 2
            in mandibular condylar cartilage
  JOURNAL   Eur Cell Mater 45, 113-130 (2023)
   PUBMED   37154195
  REMARK    GeneRIF: Disrupting mechanical homeostasis promotes matrix
            metalloproteinase-13 mediated processing of neuron glial antigen 2
            in mandibular condylar cartilage.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2322)
  AUTHORS   Larabee,J.L., Doyle,D.A., Ahmed,U.K.B., Shadid,T.M., Sharp,R.R.,
            Jones,K.L., Kim,Y.M., Li,S. and Ballard,J.D.
  TITLE     Discovery of Hippo signaling as a regulator of CSPG4 expression and
            as a therapeutic target for Clostridioides difficile disease
  JOURNAL   PLoS Pathog 19 (3), e1011272 (2023)
   PUBMED   36972308
  REMARK    GeneRIF: Discovery of Hippo signaling as a regulator of CSPG4
            expression and as a therapeutic target for Clostridioides difficile
            disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2322)
  AUTHORS   Xu,J., Yuan,A., Su,R., Yang,Q., Fan,X. and Zhang,J.
  TITLE     Trophoblast-specific knockdown of CSPG4 expression causes pregnancy
            complications with poor placentation in mice
  JOURNAL   Reprod Biol 23 (1), 100731 (2023)
   PUBMED   36634519
  REMARK    GeneRIF: Trophoblast-specific knockdown of CSPG4 expression causes
            pregnancy complications with poor placentation in mice.
REFERENCE   5  (residues 1 to 2322)
  AUTHORS   Yang,L., Zhang,H., Dong,C., Yue,W., Xue,R., Liu,F., Yang,L. and
            Li,L.
  TITLE     Neuron-Glial Antigen 2 Participates in Liver Fibrosis via
            Regulating the Differentiation of Bone Marrow Mesenchymal Stem Cell
            to Myofibroblast
  JOURNAL   Int J Mol Sci 24 (2), 1177 (2023)
   PUBMED   36674693
  REMARK    GeneRIF: Neuron-Glial Antigen 2 Participates in Liver Fibrosis via
            Regulating the Differentiation of Bone Marrow Mesenchymal Stem Cell
            to Myofibroblast.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2322)
  AUTHORS   Barritt,D.S., Pearn,M.T., Zisch,A.H., Lee,S.S., Javier,R.T.,
            Pasquale,E.B. and Stallcup,W.B.
  TITLE     The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the
            membrane-spanning proteoglycan NG2
  JOURNAL   J Cell Biochem 79 (2), 213-224 (2000)
   PUBMED   10967549
REFERENCE   7  (residues 1 to 2322)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
REFERENCE   8  (residues 1 to 2322)
  AUTHORS   Iida,J., Meijne,A.M., Oegema,T.R. Jr., Yednock,T.A., Kovach,N.L.,
            Furcht,L.T. and McCarthy,J.B.
  TITLE     A role of chondroitin sulfate glycosaminoglycan binding site in
            alpha4beta1 integrin-mediated melanoma cell adhesion
  JOURNAL   J Biol Chem 273 (10), 5955-5962 (1998)
   PUBMED   9488735
REFERENCE   9  (residues 1 to 2322)
  AUTHORS   Kirschfink,M., Blase,L., Engelmann,S. and Schwartz-Albiez,R.
  TITLE     Secreted chondroitin sulfate proteoglycan of human B cell lines
            binds to the complement protein C1q and inhibits complex formation
            of C1
  JOURNAL   J Immunol 158 (3), 1324-1331 (1997)
   PUBMED   9013976
REFERENCE   10 (residues 1 to 2322)
  AUTHORS   Pluschke,G., Vanek,M., Evans,A., Dittmar,T., Schmid,P., Itin,P.,
            Filardo,E.J. and Reisfeld,R.A.
  TITLE     Molecular cloning of a human melanoma-associated chondroitin
            sulfate proteoglycan
  JOURNAL   Proc Natl Acad Sci U S A 93 (18), 9710-9715 (1996)
   PUBMED   8790396
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP363063.1, AY359468.1,
            X96753.1, BQ679485.1, CA428796.1 and CA438367.1.
            
            On May 17, 2004 this sequence version replaced NP_001888.1.
            
            Summary: A human melanoma-associated chondroitin sulfate
            proteoglycan plays a role in stabilizing cell-substratum
            interactions during early events of melanoma cell spreading on
            endothelial basement membranes. CSPG4 represents an integral
            membrane chondroitin sulfate proteoglycan expressed by human
            malignant melanoma cells. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X96753.1, AY359468.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162568 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308508.5/ ENSP00000312506.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2322
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..2322
                     /product="chondroitin sulfate proteoglycan 4 precursor"
                     /note="chondroitin sulfate proteoglycan 4
                     (melanoma-associated); melanoma-associated chondroitin
                     sulfate proteoglycan; chondroitin sulfate proteoglycan
                     NG2; melanoma chondroitin sulfate proteoglycan"
                     /calculated_mol_wt=247640
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2916
     Region          29..176
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          30..639
                     /region_name="Globular or compact configuration stabilized
                     by disulfide bonds"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          30..639
                     /region_name="Neurite growth inhibition.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          203..361
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            427
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          <436..523
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          536..645
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          553..645
                     /region_name="CSPG 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201,
                     ECO:0000269|PubMed:12220645"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          574..1040
                     /region_name="Interaction with COL6A2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          631..1446
                     /region_name="Interaction with COL5A1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            685
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            772
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          <790..878
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          884..989
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Site            995
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:32337544,
                     ECO:0000269|PubMed:36213313; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          1003..1110
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1128..1215
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Site            1131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            1202
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          1225..1336
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1356..1449
                     /region_name="CSPG 9.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201,
                     ECO:0000269|PubMed:12220645"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            1364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          <1365..1446
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Site            1449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          1456..1563
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1473..1563
                     /region_name="CSPG 10.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201,
                     ECO:0000269|PubMed:12220645"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          1581..1679
                     /region_name="CSPG 11.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201,
                     ECO:0000269|PubMed:12220645"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          1586..2221
                     /region_name="Neurite growth inhibition.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          1587..2221
                     /region_name="Cysteine-containing"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            1645
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          <1710..1802
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1815..1924
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Site            1909
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            2016
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            2034
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            2040
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          2041..2123
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Site            2075
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          2182..2206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            2225..2245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Site            2252
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC/PRKCA.
                     /evidence=ECO:0000250|UniProtKB:Q00657; propagated from
                     UniProtKB/Swiss-Prot (Q6UVK1.2)"
     Region          2320..2322
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UVK1.2)"
     CDS             1..2322
                     /gene="CSPG4"
                     /gene_synonym="CSPG4A; HMW-MAA; MCSP; MCSPG; MEL-CSPG;
                     MSK16; NG2"
                     /coded_by="NM_001897.5:94..7062"
                     /db_xref="CCDS:CCDS10284.1"
                     /db_xref="GeneID:1464"
                     /db_xref="HGNC:HGNC:2466"
                     /db_xref="MIM:601172"
ORIGIN      
        1 mqsgprpplp apglalaltl tmlarlasaa sffgenhlev pvataltdid lqlqfstsqp
       61 eallllaagp adhlllqlys grlqvrlvlg qeelrlqtpa etllsdsiph tvvltvvegw
      121 atlsvdgfln assavpgapl evpyglfvgg tgtlglpylr gtsrplrgcl haatlngrsl
      181 lrpltpdvhe gcaeefsasd dvalgfsgph slaafpawgt qdegtleftl ttqsrqapla
      241 fqaggrrgdf iyvdifeghl ravvekgqgt vllhnsvpva dgqphevsvh inahrleisv
      301 dqypthtsnr gvlsyleprg slllggldae asrhlqehrl gltpeatnas llgcmedlsv
      361 ngqrrglrea lltrnmaagc rleeeeyedd ayghyeafst lapeawpame lpepcvpepg
      421 lppvfanftq lltisplvva eggtawlewr hvqptldlme aelrksqvlf svtrgarhge
      481 leldipgaqa rkmftlldvv nrkarfihdg sedtsdqlvl evsvtarvpm psclrrgqty
      541 llpiqvnpvn dpphiifphg slmvilehtq kplgpevfqa ydpdsacegl tfqvlgtssg
      601 lpverrdqpg epatefscre leagslvyvh rggpaqdltf rvsdglqasp patlkvvair
      661 paiqihrstg lrlaqgsamp ilpanlsvet navgqdvsvl frvtgalqfg elqkqgaggv
      721 egaewwatqa fhqrdveqgr vrylstdpqh haydtvenla levqvgqeil snlsfpvtiq
      781 ratvwmlrle plhtqntqqe tlttahleat leeagpsppt fhyevvqapr kgnlqlqgtr
      841 lsdgqgftqd diqagrvtyg ataraseave dtfrfrvtap pyfsplytfp ihiggdpdap
      901 vltnvllvvp eggegvlsad hlfvkslnsa sylyevmerp rhgrlawrgt qdkttmvtsf
      961 tnedllrgrl vyqhddsett eddipfvatr qgessgdmaw eevrgvfrva iqpvndhapv
     1021 qtisrifhva rggrrllttd dvafsdadsg fadaqlvltr kdllfgsiva vdeptrpiyr
     1081 ftqedlrkrr vlfvhsgadr gwiqlqvsdg qhqatallev qasepylrva ngsslvvpqg
     1141 gqgtidtavl hldtnldirs gdevhyhvta gprwgqlvra gqpatafsqq dlldgavlys
     1201 hngslsprdt mafsveagpv htdatlqvti alegplaplk lvrhkkiyvf qgeaaeirrd
     1261 qleaaqeavp padivfsvks ppsagylvmv srgaladepp sldpvqsfsq eavdtgrvly
     1321 lhsrpeawsd afsldvasgl gaplegvlve levlpaaipl eaqnfsvpeg gsltlappll
     1381 rvsgpyfptl lglslqvlep pqhgalqked gpqartlsaf swrmveeqli ryvhdgsetl
     1441 tdsfvlmana semdrqshpv aftvtvlpvn dqppilttnt glqmwegata pipaealrst
     1501 dgdsgsedlv ytieqpsngr vvlrgapgte vrsftqaqld gglvlfshrg tldggfrfrl
     1561 sdgehtspgh ffrvtaqkqv llslkgsqtl tvcpgsvqpl ssqtlrasss agtdpqllly
     1621 rvvrgpqlgr lfhaqqdstg ealvnftqae vyagnilyeh emppepfwea hdtlelqlss
     1681 ppardvaatl avavsfeaac pqrpshlwkn kglwvpegqr aritvaalda snllasvpsp
     1741 qrsehdvlfq vtqfpsrgql lvseeplhag qphflqsqla agqlvyahgg ggtqqdgfhf
     1801 rahlqgpaga svagpqtsea faitvrdvne rppqpqasvp lrltrgsrap israqlsvvd
     1861 pdsapgeiey evqraphngf lslvggglgp vtrftqadvd sgrlafvang ssvagifqls
     1921 msdgaspplp mslavdilps aievqlrapl evpqalgrss lsqqqlrvvs dreepeaayr
     1981 liqgpqyghl lvggrptsaf sqfqidqgev vfaftnfsss hdhfrvlala rgvnasavvn
     2041 vtvrallhvw aggpwpqgat lrldptvlda gelanrtgsv prfrllegpr hgrvvrvpra
     2101 rtepggsqlv eqftqqdled grlglevgrp egrapgpagd sltlelwaqg vppavasldf
     2161 atepynaarp ysvallsvpe aarteagkpe sstptgepgp masspepava kggflsflea
     2221 nmfsviipmc lvllllalil pllfylrkrn ktgkhdvqvl takprnglag dtetfrkvep
     2281 gqaipltavp gqgpppggqp dpellqfcrt pnpalkngqy wv
//
LOCUS       NP_071413                298 aa            linear   PRI 27-APR-2025
DEFINITION  Golgi phosphoprotein 3 [Homo sapiens].
ACCESSION   NP_071413
VERSION     NP_071413.1
DBSOURCE    REFSEQ: accession NM_022130.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Yin,Z., Liu,Q., Gao,Y., Wang,R., Qi,Y., Wang,D., Chen,L., Yin,X.,
            He,M. and Li,W.
  TITLE     GOLPH3 promotes tumor malignancy via inhibition of ferroptosis by
            upregulating SLC7A11 in cholangiocarcinoma
  JOURNAL   Mol Carcinog 63 (5), 912-925 (2024)
   PUBMED   38390729
  REMARK    GeneRIF: GOLPH3 promotes tumor malignancy via inhibition of
            ferroptosis by upregulating SLC7A11 in cholangiocarcinoma.
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Polanco,C.M., Cavieres,V.A., Galarza,A.J., Jara,C., Torres,A.K.,
            Cancino,J., Varas-Godoy,M., Burgos,P.V., Tapia-Rojas,C. and
            Mardones,G.A.
  TITLE     GOLPH3 Participates in Mitochondrial Fission and Is Necessary to
            Sustain Bioenergetic Function in MDA-MB-231 Breast Cancer Cells
  JOURNAL   Cells 13 (4), 316 (2024)
   PUBMED   38391929
  REMARK    GeneRIF: GOLPH3 Participates in Mitochondrial Fission and Is
            Necessary to Sustain Bioenergetic Function in MDA-MB-231 Breast
            Cancer Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Yang,H., Ma,X., Song,B., Wang,D. and Chai,Z.
  TITLE     Golgi Phosphoprotein 3 Promotes Cervical Cancer Progression via
            Wnt/beta-catenin Mediated Epithelial-Mesenchymal Transition
  JOURNAL   Ann Clin Lab Sci 53 (5), 738-748 (2023)
   PUBMED   37945014
  REMARK    GeneRIF: Golgi Phosphoprotein 3 Promotes Cervical Cancer
            Progression via Wnt/beta-catenin Mediated Epithelial-Mesenchymal
            Transition.
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Bucurica,S., Gaman,L., Jinga,M., Popa,A.A. and Ionita-Radu,F.
  TITLE     Golgi Apparatus Target Proteins in Gastroenterological Cancers: A
            Comprehensive Review of GOLPH3 and GOLGA Proteins
  JOURNAL   Cells 12 (14), 1823 (2023)
   PUBMED   37508488
  REMARK    GeneRIF: Golgi Apparatus Target Proteins in Gastroenterological
            Cancers: A Comprehensive Review of GOLPH3 and GOLGA Proteins.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Zhu,S., Lin,D., Ye,Z., Chen,X., Jiang,W., Xu,H., Quan,S. and
            Zheng,B.
  TITLE     GOLPH3 modulates expression and alternative splicing of
            transcription factors associated with endometrial decidualization
            in human endometrial stromal cells
  JOURNAL   PeerJ 11, e15048 (2023)
   PUBMED   36967990
  REMARK    GeneRIF: GOLPH3 modulates expression and alternative splicing of
            transcription factors associated with endometrial decidualization
            in human endometrial stromal cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Abraham,R.T.
  TITLE     GOLPH3 links the Golgi network to mTOR signaling and human cancer
  JOURNAL   Pigment Cell Melanoma Res 22 (4), 378-379 (2009)
   PUBMED   19624311
  REMARK    GeneRIF: GOLPH3 links the Golgi network to mTOR signaling and human
            cancer
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Scott,K.L., Kabbarah,O., Liang,M.C., Ivanova,E., Anagnostou,V.,
            Wu,J., Dhakal,S., Wu,M., Chen,S., Feinberg,T., Huang,J., Saci,A.,
            Widlund,H.R., Fisher,D.E., Xiao,Y., Rimm,D.L., Protopopov,A.,
            Wong,K.K. and Chin,L.
  TITLE     GOLPH3 modulates mTOR signalling and rapamycin sensitivity in
            cancer
  JOURNAL   Nature 459 (7250), 1085-1090 (2009)
   PUBMED   19553991
  REMARK    GeneRIF: Gain- and loss-of-function studies in vitro and in vivo
            validated GOLPH3 as a potent oncogene
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Schmitz,K.R., Liu,J., Li,S., Setty,T.G., Wood,C.S., Burd,C.G. and
            Ferguson,K.M.
  TITLE     Golgi localization of glycosyltransferases requires a Vps74p
            oligomer
  JOURNAL   Dev Cell 14 (4), 523-534 (2008)
   PUBMED   18410729
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Nakashima-Kamimura,N., Asoh,S., Ishibashi,Y., Mukai,Y., Shidara,Y.,
            Oda,H., Munakata,K., Goto,Y. and Ohta,S.
  TITLE     MIDAS/GPP34, a nuclear gene product, regulates total mitochondrial
            mass in response to mitochondrial dysfunction
  JOURNAL   J Cell Sci 118 (Pt 22), 5357-5367 (2005)
   PUBMED   16263763
  REMARK    GeneRIF: MIDAS/GPP34 is involved in the regulation of mitochondrial
            lipids, leading to increases of total mitochondrial mass in
            response to mitochondrial dysfunction.
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC025181.8 and AC025178.8.
            
            Summary: The Golgi complex plays a key role in the sorting and
            modification of proteins exported from the endoplasmic reticulum.
            The protein encoded by this gene is a peripheral membrane protein
            of the Golgi stack and may have a regulatory role in Golgi
            trafficking. Several alternatively spliced transcript variants of
            this gene have been described, but the full-length nature of these
            variants has not been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK075156.1, BC063586.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265070.7/ ENSP00000265070.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.3"
     Protein         1..298
                     /product="Golgi phosphoprotein 3"
                     /note="golgi peripheral membrane protein 1, 34 kDa;
                     coat-protein; golgi-associated protein; golgi protein;
                     coat protein GPP34; mitochondrial DNA absence factor"
                     /calculated_mol_wt=33680
     Region          1..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A6.1)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A6.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A6.1)"
     Region          62..273
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
     Region          190..201
                     /region_name="Beta-hairpin required for oligomerization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A6.1)"
     CDS             1..298
                     /gene="GOLPH3"
                     /gene_synonym="GOPP1; GPP34; MIDAS; Vps74"
                     /coded_by="NM_022130.4:286..1182"
                     /db_xref="CCDS:CCDS3896.1"
                     /db_xref="GeneID:64083"
                     /db_xref="HGNC:HGNC:15452"
                     /db_xref="MIM:612207"
ORIGIN      
        1 mtsltqrssg lvqrrteasr naadkeraag ggagssedda qsrrdeqddd dkgdsketrl
       61 tlmeevlllg lkdregytsf wndcissglr gcmlielalr grlqleacgm rrkslltrkv
      121 icksdaptgd vlldealkhv ketqppetvq nwiellsget wnplklhyql rnvrerlakn
      181 lvekgvltte kqnfllfdmt thpltnnnik qrlikkvqea vldkwvndph rmdrrllali
      241 ylahasdvle nafaplldeq ydlatkrvrq lldldpevec lkantnevlw avvaaftk
//
LOCUS       NP_001028432             990 aa            linear   ROD 27-APR-2025
DEFINITION  storkhead-box protein 1 isoform 1 [Mus musculus].
ACCESSION   NP_001028432 XP_125685 XP_910687
VERSION     NP_001028432.1
DBSOURCE    REFSEQ: accession NM_001033260.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Parchem,J.G., Kanasaki,K., Lee,S.B., Kanasaki,M., Yang,J.L., Xu,Y.,
            Earl,K.M., Keuls,R.A., Gattone,V.H. 2nd and Kalluri,R.
  TITLE     STOX1 deficiency is associated with renin-mediated gestational
            hypertension and placental defects
  JOURNAL   JCI Insight 6 (2), 141588 (2021)
   PUBMED   33301424
  REMARK    GeneRIF: STOX1 deficiency is associated with renin-mediated
            gestational hypertension and placental defects.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Miralles,F., Collinot,H., Boumerdassi,Y., Ducat,A., Duche,A.,
            Renault,G., Marchiol,C., Lagoutte,I., Bertholle,C., Andrieu,M.,
            Jacques,S., Mehats,C. and Vaiman,D.
  TITLE     Long-term cardiovascular disorders in the STOX1 mouse model of
            preeclampsia
  JOURNAL   Sci Rep 9 (1), 11918 (2019)
   PUBMED   31417152
  REMARK    GeneRIF: Long-term cardiovascular disorders in the STOX1 mouse
            model of preeclampsia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Erlandsson,L., Ducat,A., Castille,J., Zia,I., Kalapotharakos,G.,
            Hedstrom,E., Vilotte,J.L., Vaiman,D. and Hansson,S.R.
  TITLE     Alpha-1 microglobulin as a potential therapeutic candidate for
            treatment of hypertension and oxidative stress in the STOX1
            preeclampsia mouse model
  JOURNAL   Sci Rep 9 (1), 8561 (2019)
   PUBMED   31189914
  REMARK    GeneRIF: Alpha-1 microglobulin as a potential therapeutic candidate
            for treatment of hypertension and oxidative stress in the STOX1
            preeclampsia mouse model.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 990)
  AUTHORS   Collinot,H., Marchiol,C., Lagoutte,I., Lager,F., Siauve,N.,
            Autret,G., Balvay,D., Renault,G., Salomon,L.J. and Vaiman,D.
  TITLE     Preeclampsia induced by STOX1 overexpression in mice induces
            intrauterine growth restriction, abnormal ultrasonography and BOLD
            MRI signatures
  JOURNAL   J Hypertens 36 (6), 1399-1406 (2018)
   PUBMED   29465714
  REMARK    GeneRIF: Studied association of overexpression of storkhead box 1
            (STOX1) protein, preeclampsia, intrauterine growth restriction and
            fetal imaging pathology in mice.
REFERENCE   5  (residues 1 to 990)
  AUTHORS   Zhang,C., Ji,Z., Wang,M., Zhang,W., Yang,R., An,H., Yang,R., van
            Abel,D., van Dijk,M., Yang,X., Ou,G., Zhu,H.H. and Gao,W.Q.
  TITLE     Stox1 as a novel transcriptional suppressor of Math1 during
            cerebellar granule neurogenesis and medulloblastoma formation
  JOURNAL   Cell Death Differ 23 (12), 2042-2053 (2016)
   PUBMED   27564589
  REMARK    GeneRIF: This study illustrates a SHH-Stox1-Math1 regulatory axis
            in normal cerebellar development and medulloblastoma formation.
REFERENCE   6  (residues 1 to 990)
  AUTHORS   Nie,X., Zhang,K., Wang,L., Ou,G., Zhu,H. and Gao,W.Q.
  TITLE     Transcription factor STOX1 regulates proliferation of inner ear
            epithelial cells via the AKT pathway
  JOURNAL   Cell Prolif 48 (2), 209-220 (2015)
   PUBMED   25677106
  REMARK    GeneRIF: STOX1 is a novel stimulatory factor for inner ear
            epithelial cell proliferation and might be an important target to
            be considered in regeneration or repair of inner ear epithelium.
REFERENCE   7  (residues 1 to 990)
  AUTHORS   Lui,J.H., Nowakowski,T.J., Pollen,A.A., Javaherian,A.,
            Kriegstein,A.R. and Oldham,M.C.
  TITLE     Radial glia require PDGFD-PDGFRbeta signalling in human but not
            mouse neocortex
  JOURNAL   Nature 515 (7526), 264-268 (2014)
   PUBMED   25391964
REFERENCE   8  (residues 1 to 990)
  AUTHORS   Doridot,L., Chatre,L., Ducat,A., Vilotte,J.L., Lombes,A.,
            Mehats,C., Barbaux,S., Calicchio,R., Ricchetti,M. and Vaiman,D.
  TITLE     Nitroso-redox balance and mitochondrial homeostasis are regulated
            by STOX1, a pre-eclampsia-associated gene
  JOURNAL   Antioxid Redox Signal 21 (6), 819-834 (2014)
   PUBMED   24738702
  REMARK    GeneRIF: Our data posit STOX1 as a genetic switch in the ROS/RNS
            balance and suggest an explanation for elevated blood pressure in
            pre-eclampsia.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC137978.1, AK133671.1 and AI842662.1.
            
            On or before Sep 7, 2008 this sequence version replaced
            XP_910687.1, XP_125685.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK028920.1, BC137978.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 32.45 cM"
     Protein         1..990
                     /product="storkhead-box protein 1 isoform 1"
                     /note="storkhead-box protein 1"
                     /calculated_mol_wt=108772
     Region          108..186
                     /region_name="Stork_head"
                     /note="Winged helix Storkhead-box1 domain; pfam10264"
                     /db_xref="CDD:431182"
     Region          396..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RQL2.1)"
     Region          562..586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RQL2.1)"
     Region          712..736
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RQL2.1)"
     Region          809..832
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RQL2.1)"
     CDS             1..990
                     /gene="Stox1"
                     /gene_synonym="4732470K04Rik; Gm63"
                     /coded_by="NM_001033260.2:27..2999"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS48580.1"
                     /db_xref="GeneID:216021"
                     /db_xref="MGI:MGI:2684909"
ORIGIN      
        1 marpvqlapg slalvlspre agqaagepgg ralfrafrra narcfwnarl araasrlafl
       61 gwlrrgvllv rapqpcvqvl rdawrrralr pprgfritav gdvfpvqmsp iaqcrfvpla
      121 evlccaiadm naaqvmvtqq sllehlikhy pgiavpspdi lystlgaliq erkiyhtgeg
      181 yfivtpstyf itntpmqgnk sallsnegcs gptsgtylvs vdccaeptqe nealfshcps
      241 cqcypdtsmc dskdlltaae vtrksqegle ettaltenqv vsasedthic vnpkplpytk
      301 dkgkrfgfgf lwrslsrkek pkaeyhsfsa qfppeewpvr dedsstkipr dvehalikri
      361 npvltvdnlt khtalmqkye eqkkynsqgt smdilttrhk dsskevigkr qgqfaksrrr
      421 gsshkgrhka rsqgselepg npgqekekqp kvpaaqpapr tkspseqvhh lqgrnpavlg
      481 shliykkqin npfqgmhlrk hsvskghavq kthglkptcv gpeekpfwsa gssdpsgvfd
      541 geaqppypeq crdkleagst qvakapvhpv sddfrggpgn ypprrvlpgp srccsfresm
      601 lrpgvyheen kdlpevlrks wstcdmflgt kekkqalpaq rcsldpdsss vhaedktvdk
      661 ilhqfqnlgl ldcpaganrl rtherqdgns eelsrkalqi peaeivnmen eglsdseqdq
      721 valshsdpga gddggcsslc ledddfsetd dfcpslpght qhsfagggtw nhlgtpamtg
      781 ksltdcnska hrlellaier npwykatglf snagespnpd lsdnpgqnsr ipwgfnyege
      841 ptvahvqtpa aaagrsllac stvrttsfpv eilqespgdr gkspivwrqs lpsqemkehf
      901 tdklqlvkts hgpvsaqepq gehlegteny smtgdsgids prtqslvstn saildgfkrr
      961 qhflpnregv qksqnlasns lfqltpainv
//
LOCUS       NP_116321                637 aa            linear   PRI 27-APR-2025
DEFINITION  rab11 family-interacting protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_116321
VERSION     NP_116321.2
DBSOURCE    REFSEQ: accession NM_032932.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Wang,J.Z., Yang,S.X., Ye,F., Xia,X.P., Shao,X.X., Xia,S.L.,
            Zheng,B. and Xu,C.L.
  TITLE     Hypoxia-induced Rab11-family interacting protein 4 expression
            promotes migration and invasion of colon cancer and correlates with
            poor prognosis
  JOURNAL   Mol Med Rep 17 (3), 3797-3806 (2018)
   PUBMED   29257314
  REMARK    GeneRIF: Rab11-FIP4 expression promotes migration and invasion of
            colon cancer cells and correlates with poor prognosis.
REFERENCE   3  (residues 1 to 637)
  AUTHORS   He,Y., Ye,M., Zhou,L., Shan,Y., Lu,G., Zhou,Y., Zhong,J., Zheng,J.,
            Xue,Z. and Cai,Z.
  TITLE     High Rab11-FIP4 expression predicts poor prognosis and exhibits
            tumor promotion in pancreatic cancer
  JOURNAL   Int J Oncol 50 (2), 396-404 (2017)
   PUBMED   28035375
  REMARK    GeneRIF: Our findings suggest that overexpression of Rab11-FIP4
            predicts poor clinical outcomes for pancreatic cancer and
            contributes to pancreatic tumor progression.
REFERENCE   4  (residues 1 to 637)
  AUTHORS   Hu,F., Deng,X., Yang,X., Jin,H., Gu,D., Lv,X., Wang,C., Zhang,Y.,
            Huo,X., Shen,Q., Luo,Q., Zhao,F., Ge,T., Zhao,F., Chu,W., Shu,H.,
            Yao,M., Fan,J. and Qin,W.
  TITLE     Hypoxia upregulates Rab11-family interacting protein 4 through
            HIF-1alpha to promote the metastasis of hepatocellular carcinoma
  JOURNAL   Oncogene 34 (49), 6007-6017 (2015)
   PUBMED   25745995
  REMARK    GeneRIF: Results show the expression of Rab11-FIP4 upregulated in
            hepatocellular carcinoma (HCC) and correlated with poor prognosis.
            Rab11-FIP4 dramatically contributed to HCC metastasis via
            phosphorylation of PRAS40.
REFERENCE   5  (residues 1 to 637)
  AUTHORS   Makyio,H., Ohgi,M., Takei,T., Takahashi,S., Takatsu,H., Katoh,Y.,
            Hanai,A., Ueda,T., Kanaho,Y., Xie,Y., Shin,H.W., Kamikubo,H.,
            Kataoka,M., Kawasaki,M., Kato,R., Wakatsuki,S. and Nakayama,K.
  TITLE     Structural basis for Arf6-MKLP1 complex formation on the Flemming
            body responsible for cytokinesis
  JOURNAL   EMBO J 31 (11), 2590-2603 (2012)
   PUBMED   22522702
REFERENCE   6  (residues 1 to 637)
  AUTHORS   Jenne,D.E., Tinschert,S., Dorschner,M.O., Hameister,H., Stephens,K.
            and Kehrer-Sawatzki,H.
  TITLE     Complete physical map and gene content of the human NF1 tumor
            suppressor region in human and mouse
  JOURNAL   Genes Chromosomes Cancer 37 (2), 111-120 (2003)
   PUBMED   12696059
REFERENCE   7  (residues 1 to 637)
  AUTHORS   Wallace,D.M., Lindsay,A.J., Hendrick,A.G. and McCaffrey,M.W.
  TITLE     Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its
            overexpression condenses the Rab11 positive compartment in HeLa
            cells
  JOURNAL   Biochem Biophys Res Commun 299 (5), 770-779 (2002)
   PUBMED   12470645
  REMARK    GeneRIF: Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner
            and its overexpression condenses the Rab11 positive compartment in
            HeLa cells.
REFERENCE   8  (residues 1 to 637)
  AUTHORS   Hales,C.M., Griner,R., Hobdy-Henderson,K.C., Dorn,M.C., Hardy,D.,
            Kumar,R., Navarre,J., Chan,E.K., Lapierre,L.A. and Goldenring,J.R.
  TITLE     Identification and characterization of a family of
            Rab11-interacting proteins
  JOURNAL   J Biol Chem 276 (42), 39067-39075 (2001)
   PUBMED   11495908
REFERENCE   9  (residues 1 to 637)
  AUTHORS   Jenne,D.E., Tinschert,S., Reimann,H., Lasinger,W., Thiel,G.,
            Hameister,H. and Kehrer-Sawatzki,H.
  TITLE     Molecular characterization and gene content of breakpoint
            boundaries in patients with neurofibromatosis type 1 with 17q11.2
            microdeletions
  JOURNAL   Am J Hum Genet 69 (3), 516-527 (2001)
   PUBMED   11468690
REFERENCE   10 (residues 1 to 637)
  AUTHORS   Jenne,D.E., Tinschert,S., Stegmann,E., Reimann,H., Nurnberg,P.,
            Horn,D., Naumann,I., Buske,A. and Thiel,G.
  TITLE     A common set of at least 11 functional genes is lost in the
            majority of NF1 patients with gross deletions
  JOURNAL   Genomics 66 (1), 93-97 (2000)
   PUBMED   10843809
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY169244.1, BC093914.1,
            AJ314646.2 and BC047674.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 2, 2003 this sequence version replaced NP_116321.1.
            
            Summary: The protein encoded by this gene interacts with RAB11 and
            is thought to be involved in bringing recycling endosome membranes
            to the cleavage furrow in late cytokinesis. Hypoxic conditions can
            lead to an upregulation of the encoded protein and enhance the
            metastatic potential of hepatocellular carcinoma. [provided by
            RefSeq, Oct 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ314646.2, AY169244.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000621161.5/ ENSP00000482620.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..637
                     /product="rab11 family-interacting protein 4 isoform 1"
                     /note="rab11 family-interacting protein 4; arfophilin-2;
                     RAB11 family interacting protein 4 (class II)"
                     /calculated_mol_wt=71797
     Region          20..78
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Region          82..637
                     /region_name="Necessary for interaction with RAB11A,
                     subcellular location, homo-or heterooligomerization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YS3.1)"
     Region          138..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YS3.1)"
     Region          219..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YS3.1)"
     Region          <338..621
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          596..636
                     /region_name="RBD-FIP"
                     /note="FIP domain; pfam09457"
                     /db_xref="CDD:462805"
     CDS             1..637
                     /gene="RAB11FIP4"
                     /gene_synonym="FIP4-Rab11; RAB11-FIP4"
                     /coded_by="NM_032932.6:179..2092"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11267.1"
                     /db_xref="GeneID:84440"
                     /db_xref="HGNC:HGNC:30267"
                     /db_xref="MIM:611999"
ORIGIN      
        1 maggagwsga paallrsvrr lrevfevcgr dpdgflrver vaalglrfgq geeveklvky
       61 ldpndlgrin fkdfcrgvfa mkgceellkd vlsvesagtl pcapeipdcv eqgsevtgpt
      121 fadgelipre pgffpedeee amtlappegp qelytdspme stqslegsvg spaekdgglg
      181 glflpedksl vhtpsmttsd lsthsttsli sneeqfedyg egddvdcaps spcpddetrt
      241 nvysdlgssv sssagqtprk mrhvynsell dvycsqcckk inllndlear lknlkanspn
      301 rkisstafgr qlmhssnfss sngstedlfr dsidscdndi tekvsflekk vtelendslt
      361 ngdlksklkq entqlvhrvh eleemvkdqe ttaeqaleee arrhreaygk lerekateve
      421 llnarvqqle eentelrttv trlksqtekl deerqrmsdr ledtslrlkd emdlykrmmd
      481 klrqnrlefq kereatqeli edlrkelehl qmykldcerp grgrsassgl gefnararev
      541 elehevkrlk qenyklrdqn ddlngqilsl slyeaknlfa aqtkaqslaa eidtasrdel
      601 mealkeqeei nfrlrqymdk iilaildhnp sileikh
//
LOCUS       NP_872303                431 aa            linear   PRI 27-APR-2025
DEFINITION  keratin, type I cytoskeletal 40 [Homo sapiens].
ACCESSION   NP_872303 XP_496218
VERSION     NP_872303.2
DBSOURCE    REFSEQ: accession NM_182497.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Langbein,L., Rogers,M.A., Praetzel-Wunder,S., Bockler,D.,
            Schirmacher,P. and Schweizer,J.
  TITLE     Novel type I hair keratins K39 and K40 are the last to be expressed
            in differentiation of the hair: completion of the human hair
            keratin catalog
  JOURNAL   J Invest Dermatol 127 (6), 1532-1535 (2007)
   PUBMED   17301834
  REMARK    GeneRIF: KRT39 and KRT40 expression patterns complete sequential
            expression of the 16 hair keratins in the human hair follicle
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Schweizer,J., Bowden,P.E., Coulombe,P.A., Langbein,L., Lane,E.B.,
            Magin,T.M., Maltais,L., Omary,M.B., Parry,D.A., Rogers,M.A. and
            Wright,M.W.
  TITLE     New consensus nomenclature for mammalian keratins
  JOURNAL   J Cell Biol 174 (2), 169-174 (2006)
   PUBMED   16831889
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Rogers,M.A., Winter,H., Langbein,L., Bleiler,R. and Schweizer,J.
  TITLE     The human type I keratin gene family: characterization of new hair
            follicle specific members and evaluation of the chromosome 17q21.2
            gene domain
  JOURNAL   Differentiation 72 (9-10), 527-540 (2004)
   PUBMED   15617563
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Hesse,M., Zimek,A., Weber,K. and Magin,T.M.
  TITLE     Comprehensive analysis of keratin gene clusters in humans and
            rodents
  JOURNAL   Eur J Cell Biol 83 (1), 19-26 (2004)
   PUBMED   15085952
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007455.7.
            
            On Feb 9, 2007 this sequence version replaced NP_872303.1.
            
            Summary: This gene encodes a member of the type I (acidic) keratin
            family, which belongs to the superfamily of intermediate filament
            (IF) proteins. Keratins are heteropolymeric structural proteins
            which form the intermediate filament. These filaments, along with
            actin microfilaments and microtubules, compose the cytoskeleton of
            epithelial cells. The type I keratin genes are clustered in a
            region of chromosome 17q12-q21. [provided by RefSeq, Jul 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150191.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..431
                     /product="keratin, type I cytoskeletal 40"
                     /note="type I hair keratin KA36; cytokeratin-40; keratin
                     40, type I"
                     /calculated_mol_wt=48008
     Region          1..89
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6A162.2)"
     Region          88..399
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          90..124
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6A162.2)"
     Region          125..135
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6A162.2)"
     Region          136..236
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6A162.2)"
     Region          237..252
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6A162.2)"
     Region          253..396
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6A162.2)"
     Site            338
                     /site_type="other"
                     /note="Stutter; propagated from UniProtKB/Swiss-Prot
                     (Q6A162.2)"
     Region          397..431
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6A162.2)"
     CDS             1..431
                     /gene="KRT40"
                     /gene_synonym="CK-40; K40; KA36"
                     /coded_by="NM_182497.4:162..1457"
                     /db_xref="CCDS:CCDS42320.1"
                     /db_xref="GeneID:125115"
                     /db_xref="HGNC:HGNC:26707"
                     /db_xref="MIM:616679"
ORIGIN      
        1 mtsdcssthc spescgtasg capasscsve taclpgtcat srcqtpsfls rsrgltgcll
       61 pcyftgscns pclvgncawc edgvftsnek etmqflndrl asylekvrsl eetnaelesr
      121 iqeqceqdip mvcpdyqryf ntiedlqqki lctkaensrl avqldnckla tddfkskyes
      181 elslrqllea disslhgile eltlcksdle ahveslkedl lclkknheee vnllreqlgd
      241 rlsveldtap tldlnrvlde mrcqcetvla nnrreaeewl avqteelnqq qlssaeqlqg
      301 cqmeilelkr tasaleielq aqqsltesle ctvaeteaqy ssqlaqiqcl idnlenqlae
      361 ircdlerqnq eyqvlldvka rlegeintyw glldsedsrl scspcsttct ssntcepcsa
      421 yvictvencc l
//
LOCUS       NP_598758                315 aa            linear   ROD 27-APR-2025
DEFINITION  apolipoprotein F precursor [Mus musculus].
ACCESSION   NP_598758
VERSION     NP_598758.2
DBSOURCE    REFSEQ: accession NM_133997.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Shigesawa,I., Nakamura,A., Yamauchi,Y., Kawata,S., Miyazaki,A.,
            Nomoto,H., Kameda,H., Terauchi,Y. and Atsumi,T.
  TITLE     Effects of glucokinase haploinsufficiency on the pancreatic
            beta-cell mass and function of long-term high-fat, high-sucrose
            diet-fed mice
  JOURNAL   J Diabetes Investig 15 (12), 1732-1742 (2024)
   PUBMED   39305123
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Shen,X., Chen,M., Zhang,J., Lin,Y., Gao,X., Tu,J., Chen,K., Zhu,A.
            and Xu,S.
  TITLE     Unveiling the Impact of ApoF Deficiency on Liver and Lipid
            Metabolism: Insights from Transcriptome-Wide m6A Methylome Analysis
            in Mice
  JOURNAL   Genes (Basel) 15 (3), 347 (2024)
   PUBMED   38540406
  REMARK    GeneRIF: Unveiling the Impact of ApoF Deficiency on Liver and Lipid
            Metabolism: Insights from Transcriptome-Wide m6A Methylome Analysis
            in Mice.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   5  (residues 1 to 315)
  AUTHORS   West,D.B., Engelhard,E.K., Adkisson,M., Nava,A.J., Kirov,J.V.,
            Cipollone,A., Willis,B., Rapp,J., de Jong,P.J. and Lloyd,K.C.
  TITLE     Transcriptome Analysis of Targeted Mouse Mutations Reveals the
            Topography of Local Changes in Gene Expression
  JOURNAL   PLoS Genet 12 (2), e1005691 (2016)
   PUBMED   26839965
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Korstanje,R., Li,R., Howard,T., Kelmenson,P., Marshall,J.,
            Paigen,B. and Churchill,G.
  TITLE     Influence of sex and diet on quantitative trait loci for HDL
            cholesterol levels in an SM/J by NZB/BlNJ intercross population
  JOURNAL   J Lipid Res 45 (5), 881-888 (2004)
   PUBMED   14993241
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Korstanje,R., Albers,J.J., Wolfbauer,G., Li,R., Tu,A.Y.,
            Churchill,G.A. and Paigen,B.J.
  TITLE     Quantitative trait locus mapping of genes that regulate
            phospholipid transfer activity in SM/J and NZB/BlNJ inbred mice
  JOURNAL   Arterioscler Thromb Vasc Biol 24 (1), 155-160 (2004)
   PUBMED   14592843
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Wu,T., Lee,C.G., Buckler-White,A. and Kozak,C.A.
  TITLE     Genetic control of a mouse serum lipoprotein factor that
            inactivates murine leukemia viruses: evaluation of apolipoprotein F
            as a candidate
  JOURNAL   J Virol 76 (5), 2279-2286 (2002)
   PUBMED   11836406
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Yotsumoto,S., Shimada,T., Cui,C.Y., Nakashima,H., Fujiwara,H. and
            Ko,M.S.
  TITLE     Expression of adrenomedullin, a hypotensive peptide, in the
            trophoblast giant cells at the embryo implantation site in mouse
  JOURNAL   Dev Biol 203 (2), 264-275 (1998)
   PUBMED   9808778
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Gwynn,B., Eicher,E.M. and Peters,L.L.
  TITLE     Genetic localization of Cd63, a member of the transmembrane 4
            superfamily, reveals two distinct loci in the mouse genome
  JOURNAL   Genomics 35 (2), 389-391 (1996)
   PUBMED   8661157
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC135859.4.
            
            On Feb 22, 2019 this sequence version replaced NP_598758.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022795.1, AI528157.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 76.5 cM"
     Protein         1..315
                     /product="apolipoprotein F precursor"
                     /note="leukemia virus-inactivating factor"
                     /calculated_mol_wt=31618
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2760
     Region          52..250
                     /region_name="Apolipo_F"
                     /note="Apolipoprotein F; pfam15148"
                     /db_xref="CDD:464532"
     mat_peptide     155..315
                     /product="Apolipoprotein F. /id=PRO_0000002054"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91V80.2)"
                     /calculated_mol_wt=17516
     CDS             1..315
                     /gene="Apof"
                     /gene_synonym="LVIF"
                     /coded_by="NM_133997.3:89..1036"
                     /db_xref="CCDS:CCDS24268.2"
                     /db_xref="GeneID:103161"
                     /db_xref="MGI:MGI:104539"
ORIGIN      
        1 mhslrlilms iqllcylllc pvdatshgea tsvstvlpps klgyqmqtsd kplscqmllp
       61 kslpgftymp pvskflvgla lrnaleaagc qaevwalqlq lyrlggveat qalihhlqel
      121 qksghtdrev svdalssalq llaweqpgpk rakrsisntd cdndqeqsvh nvvdllpavg
      181 tyynlgtaly yaikncsdka kergrdgaid lgydllmamv gasggpagav itaalkpamk
      241 agvqrliqyy ydekevttpq pevtthqpet gkdattdigv veeiamsnfv sevesttsnw
      301 ewpllknygv laykr
//
LOCUS       NP_001357429             169 aa            linear   PRI 27-APR-2025
DEFINITION  olfactomedin-like protein 1 isoform c precursor [Homo sapiens].
ACCESSION   NP_001357429
VERSION     NP_001357429.1
DBSOURCE    REFSEQ: accession NM_001370500.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Murakami,K., Kikugawa,S., Kobayashi,Y., Uehara,S., Suzuki,T.,
            Kato,H., Udagawa,N. and Nakamura,Y.
  TITLE     Olfactomedin-like protein OLFML1 inhibits Hippo signaling and
            mineralization in osteoblasts
  JOURNAL   Biochem Biophys Res Commun 505 (2), 419-425 (2018)
   PUBMED   30266405
  REMARK    GeneRIF: mutation of OLFML1 leads to impaired osteoblast
            differentiation and abnormal development of bone tissue
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Wan,B., Zhou,Y.B., Zhang,X., Zhu,H., Huo,K. and Han,Z.G.
  TITLE     hOLFML1, a novel secreted glycoprotein, enhances the proliferation
            of human cancer cell lines in vitro
  JOURNAL   FEBS Lett 582 (21-22), 3185-3192 (2008)
   PUBMED   18708057
  REMARK    GeneRIF: These findings suggest that hOLFML1 may play a significant
            role in the regulation of cell proliferation in vitro.
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC107884.15.
            
            Transcript Variant: This variant (4), as well as variant 5, encodes
            isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138523.340443.1,
                                           DRR138520.509651.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..169
                     /product="olfactomedin-like protein 1 isoform c precursor"
                     /note="olfactomedin-like protein 1"
                     /calculated_mol_wt=16749
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2630
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWY5.2)"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWY5.2)"
     CDS             1..169
                     /gene="OLFML1"
                     /gene_synonym="MVAL564; ONT2; UNQ564"
                     /coded_by="NM_001370500.1:133..642"
                     /note="isoform c precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:283298"
                     /db_xref="HGNC:HGNC:24473"
ORIGIN      
        1 mmvalrgasa llvlflaafl pppqctqdpa mvhyiyqrfr vleqglekct qatrayiqef
       61 qefsknisvm lgrcqtytse yksavgnlal rveraqreid yiqylreade ciesedktla
      121 emllqeaeee kkirtllnas kktasfpsps rdyyaqkhtd seqsgsiie
//
LOCUS       NP_004891                382 aa            linear   PRI 27-APR-2025
DEFINITION  DNA dC->dU-editing enzyme APOBEC-3B isoform a [Homo sapiens].
ACCESSION   NP_004891
VERSION     NP_004891.5
DBSOURCE    REFSEQ: accession NM_004900.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Balasubramanian,V., Saravanan,R., Balamurugan,S.S.S., Rajendran,S.,
            Joseph,L.D., Dev,B., Srinivasan,B., Balunathan,N.,
            Shanmugasundaram,G., Gopisetty,G., Ganesan,K., Rayala,S.K. and
            Venkatraman,G.
  TITLE     Genetic alteration of mRNA editing enzyme APOBEC3B in the
            pathogenesis of ovarian endometriosis
  JOURNAL   Reprod Biomed Online 49 (5), 104111 (2024)
   PUBMED   39197402
  REMARK    GeneRIF: Genetic alteration of mRNA editing enzyme APOBEC3B in the
            pathogenesis of ovarian endometriosis.
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Kim,H., Cho,U., Hong,S.H., Park,H.S., Kim,I.H., An,H.J., Shim,B.Y.
            and Kang,J.H.
  TITLE     New insights into ATR inhibition in muscle invasive bladder cancer:
            The role of apolipoprotein B mRNA editing catalytic subunit 3B
  JOURNAL   Oncol Res 32 (6), 1021-1030 (2024)
   PUBMED   38827321
  REMARK    GeneRIF: New insights into ATR inhibition in muscle invasive
            bladder cancer: The role of apolipoprotein B mRNA editing catalytic
            subunit 3B.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Butt,Y., Sakhtemani,R., Mohamad-Ramshan,R., Lawrence,M.S. and
            Bhagwat,A.S.
  TITLE     Distinguishing preferences of human APOBEC3A and APOBEC3B for
            cytosines in hairpin loops, and reflection of these preferences in
            APOBEC-signature cancer genome mutations
  JOURNAL   Nat Commun 15 (1), 2369 (2024)
   PUBMED   38499553
  REMARK    GeneRIF: Distinguishing preferences of human APOBEC3A and APOBEC3B
            for cytosines in hairpin loops, and reflection of these preferences
            in APOBEC-signature cancer genome mutations.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Caswell,D.R., Gui,P., Mayekar,M.K., Law,E.K., Pich,O., Bailey,C.,
            Boumelha,J., Kerr,D.L., Blakely,C.M., Manabe,T., Martinez-Ruiz,C.,
            Bakker,B., De Dios Palomino Villcas,J., I Vokes,N., Dietzen,M.,
            Angelova,M., Gini,B., Tamaki,W., Allegakoen,P., Wu,W.,
            Humpton,T.J., Hill,W., Tomaschko,M., Lu,W.T., Haderk,F., Al
            Bakir,M., Nagano,A., Gimeno-Valiente,F., de Carne Trecesson,S.,
            Vendramin,R., Barbe,V., Mugabo,M., Weeden,C.E., Rowan,A.,
            McCoach,C.E., Almeida,B., Green,M., Gomez,C., Nanjo,S., Barbosa,D.,
            Moore,C., Przewrocka,J., Black,J.R.M., Gronroos,E.,
            Suarez-Bonnet,A., Priestnall,S.L., Zverev,C., Lighterness,S.,
            Cormack,J., Olivas,V., Cech,L., Andrews,T., Rule,B., Jiao,Y.,
            Zhang,X., Ashford,P., Durfee,C., Venkatesan,S., Temiz,N.A., Tan,L.,
            Larson,L.K., Argyris,P.P., Brown,W.L., Yu,E.A., Rotow,J.K.,
            Guha,U., Roper,N., Yu,J., Vogel,R.I., Thomas,N.J., Marra,A.,
            Selenica,P., Yu,H., Bakhoum,S.F., Chew,S.K., Reis-Filho,J.S.,
            Jamal-Hanjani,M., Vousden,K.H., McGranahan,N., Van Allen,E.M.,
            Kanu,N., Harris,R.S., Downward,J., Bivona,T.G. and Swanton,C.
  TITLE     The role of APOBEC3B in lung tumor evolution and targeted cancer
            therapy resistance
  JOURNAL   Nat Genet 56 (1), 60-73 (2024)
   PUBMED   38049664
  REMARK    GeneRIF: The role of APOBEC3B in lung tumor evolution and targeted
            cancer therapy resistance.
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Zhang,K., Chen,F., Shen,H.Y., Zhang,P.P., Gao,H., Peng,H., Luo,Y.S.
            and Cheng,Z.S.
  TITLE     Regulatory variants of APOBEC3 genes potentially associate with
            COVID-19 severity in populations with African ancestry
  JOURNAL   Sci Rep 13 (1), 22435 (2023)
   PUBMED   38105291
  REMARK    GeneRIF: Regulatory variants of APOBEC3 genes potentially associate
            with COVID-19 severity in populations with African ancestry.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Kidd,J.M., Newman,T.L., Tuzun,E., Kaul,R. and Eichler,E.E.
  TITLE     Population stratification of a common APOBEC gene deletion
            polymorphism
  JOURNAL   PLoS Genet 3 (4), e63 (2007)
   PUBMED   17447845
  REMARK    GeneRIF: detailed sequence and population genetic analysis of a
            29.5-kb common human deletion polymorphism that removes the
            APOBEC3B gene.
            GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Jarmuz,A., Chester,A., Bayliss,J., Gisbourne,J., Dunham,I.,
            Scott,J. and Navaratnam,N.
  TITLE     An anthropoid-specific locus of orphan C to U RNA-editing enzymes
            on chromosome 22
  JOURNAL   Genomics 79 (3), 285-296 (2002)
   PUBMED   11863358
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Suzuki,Y., Tsunoda,T., Sese,J., Taira,H., Mizushima-Sugano,J.,
            Hata,H., Ota,T., Isogai,T., Tanaka,T., Nakamura,Y., Suyama,A.,
            Sakaki,Y., Morishita,S., Okubo,K. and Sugano,S.
  TITLE     Identification and characterization of the potential promoter
            regions of 1031 kinds of human genes
  JOURNAL   Genome Res 11 (5), 677-684 (2001)
   PUBMED   11337467
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Madsen,P., Anant,S., Rasmussen,H.H., Gromov,P., Vorum,H.,
            Dumanski,J.P., Tommerup,N., Collins,J.E., Wright,C.L., Dunham,I.,
            MacGinnitie,A.J., Davidson,N.O. and Celis,J.E.
  TITLE     Psoriasis upregulated phorbolin-1 shares structural but not
            functional similarity to the mRNA-editing protein apobec-1
  JOURNAL   J Invest Dermatol 113 (2), 162-169 (1999)
   PUBMED   10469298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL022318.2.
            
            On Nov 23, 2018 this sequence version replaced NP_004891.4.
            
            Summary: This gene is a member of the cytidine deaminase gene
            family. It is one of seven related genes or pseudogenes found in a
            cluster, thought to result from gene duplication, on chromosome 22.
            Members of the cluster encode proteins that are structurally and
            functionally related to the C to U RNA-editing cytidine deaminase
            APOBEC1. It is thought that the proteins may be RNA editing enzymes
            and have roles in growth or cell cycle control. A hybrid gene
            results from the deletion of approximately 29.5 kb of sequence
            between this gene, APOBEC3B, and the adjacent gene APOBEC3A. The
            breakpoints of the deletion are within the two genes, so the
            deletion allele is predicted to have the promoter and coding region
            of APOBEC3A, but the 3' UTR of APOBEC3B. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.299085.1,
                                           SRR5189658.146530.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000333467.4/ ENSP00000327459.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..382
                     /product="DNA dC->dU-editing enzyme APOBEC-3B isoform a"
                     /EC_number="3.5.4.38"
                     /note="phorbolin 3; phorbolin 2; probable DNA
                     dC->dU-editing enzyme APOBEC-3B; cytidine deaminase;
                     phorbolin-2/3; phorbolin-1-related protein; apolipoprotein
                     B mRNA editing enzyme, catalytic polypeptide-like 3B"
                     /calculated_mol_wt=45793
     Region          10..189
                     /region_name="NAD2"
                     /note="Novel AID APOBEC clade 2; pfam18782"
                     /db_xref="CDD:436733"
     Region          191..377
                     /region_name="NAD2"
                     /note="Novel AID APOBEC clade 2; pfam18782"
                     /db_xref="CDD:436733"
     CDS             1..382
                     /gene="APOBEC3B"
                     /gene_synonym="A3B; APOBEC1L; ARCD3; ARP4; bK150C2.2;
                     DJ742C19.2; PHRBNL"
                     /coded_by="NM_004900.5:108..1256"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13982.1"
                     /db_xref="GeneID:9582"
                     /db_xref="HGNC:HGNC:17352"
                     /db_xref="MIM:607110"
ORIGIN      
        1 mnpqirnpme rmyrdtfydn fenepilygr sytwlcyevk ikrgrsnllw dtgvfrgqvy
       61 fkpqyhaemc flswfcgnql paykcfqitw fvswtpcpdc vaklaeflse hpnvtltisa
      121 arlyyywerd yrralcrlsq agarvtimdy eefaycwenf vynegqqfmp wykfdenyaf
      181 lhrtlkeilr ylmdpdtftf nfnndplvlr rrqtylcyev erldngtwvl mdqhmgflcn
      241 eaknllcgfy grhaelrfld lvpslqldpa qiyrvtwfis wspcfswgca gevraflqen
      301 thvrlrifaa riydydplyk ealqmlrdag aqvsimtyde feycwdtfvy rqgcpfqpwd
      361 gleehsqals grlrailqnq gn
//
LOCUS       NP_060565                534 aa            linear   PRI 27-APR-2025
DEFINITION  kelch repeat and BTB domain-containing protein 4 isoform a [Homo
            sapiens].
ACCESSION   NP_060565
VERSION     NP_060565.4
DBSOURCE    REFSEQ: accession NM_018095.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Chen,Z., Ioris,R.M., Richardson,S., Van Ess,A.N., Vendrell,I.,
            Kessler,B.M., Buffa,F.M., Busino,L., Clifford,S.C., Bullock,A.N.
            and D'Angiolella,V.
  TITLE     Disease-associated KBTBD4 mutations in medulloblastoma elicit
            neomorphic ubiquitylation activity to promote CoREST degradation
  JOURNAL   Cell Death Differ 29 (10), 1955-1969 (2022)
   PUBMED   35379950
  REMARK    GeneRIF: Disease-associated KBTBD4 mutations in medulloblastoma
            elicit neomorphic ubiquitylation activity to promote CoREST
            degradation.
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Uchida,E., Sasaki,A., Shirahata,M., Suzuki,T., Adachi,J.I.,
            Mishima,K., Yasuda,M., Fujimaki,T., Ichimura,K. and Nishikawa,R.
  TITLE     Role of proliferative marker index and KBTBD4 mutation in the
            pathological diagnosis of pineal parenchymal tumors
  JOURNAL   Brain Tumor Pathol 39 (3), 130-138 (2022)
   PUBMED   35000018
  REMARK    GeneRIF: Role of proliferative marker index and KBTBD4 mutation in
            the pathological diagnosis of pineal parenchymal tumors.
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Leal,L.F., Cavagna,R.O., Campanella,N.C., Mancano,B., Almeida,G.C.,
            Matsushita,M., Almeida Junior,C.R., Saggioro,F., Stavale,J.N.,
            Malheiros,S.M.F., Lima,M., Hajj,G.N.M., Neder,L. and Reis,R.M.
  TITLE     Lack of KBTBD4 Mutations in Molecularly Classified Brazilian
            Medulloblastomas
  JOURNAL   J Neuropathol Exp Neurol 78 (9), 788-790 (2019)
   PUBMED   31403685
  REMARK    GeneRIF: Our findings suggest that KBTBD4 mutations are uncommon in
            Brazilian MBGRP3 and MBGRP4 medulloblastomas subgroups.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104942.5 and KF459542.1.
            
            On Oct 17, 2008 this sequence version replaced NP_060565.3.
            
            Transcript Variant: This variant (1) differs in the 5' UTR and
            coding sequence compared to variant 4. The resulting isoform (a)
            has a shorter and distinct N-terminus compared to isoform c.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.944498.1,
                                           SRR1803612.174017.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000430070.7/ ENSP00000415106.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..534
                     /product="kelch repeat and BTB domain-containing protein 4
                     isoform a"
                     /note="BTB and kelch domain containing 4; kelch repeat and
                     BTB domain-containing protein 4; BTB and kelch
                     domain-containing protein 4; kelch repeat and BTB (POZ)
                     domain containing 4"
                     /calculated_mol_wt=59773
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     Region          29..168
                     /region_name="BTB_POZ_KBTBD4"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch repeat
                     and BTB domain-containing protein 4 (KBTBD4); cd18272"
                     /db_xref="CDD:349581"
     Region          63..495
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          158..245
                     /region_name="BACK_KBTBD4"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch repeat and BTB domain-containing protein 4 (KBTBD4);
                     cd18481"
                     /db_xref="CDD:350556"
     Region          255..301
                     /region_name="Kelch 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     Region          295..330
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          302..344
                     /region_name="Kelch 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     Region          334..381
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          347..394
                     /region_name="Kelch 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     Region          384..430
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          396..446
                     /region_name="Kelch 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     Region          438..483
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          448..497
                     /region_name="Kelch 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     CDS             1..534
                     /gene="KBTBD4"
                     /gene_synonym="BKLHD4; HSPC252"
                     /coded_by="NM_018095.6:20..1624"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44594.1"
                     /db_xref="GeneID:55709"
                     /db_xref="HGNC:HGNC:23761"
                     /db_xref="MIM:617645"
ORIGIN      
        1 mkggnadswq reklasmesp eepgasmden yfvnytfkdr shsgrvaqgi mklcleeelf
       61 advtisvegr efqlhrlvls aqscffrsmf tsnlkeahnr vivlqdvses vfqllvdyiy
      121 hgtvklraee lqeiyevsdm yqltslfeec srflartvqv gnclqvmwla drhsdpelyt
      181 aakhcakthl aqlqnteefl hlphrlltdi isdgvpcsqn pteaieawin fnkeereafa
      241 eslrtslkei genvhiylig kessrthsla vslhcaedds isvsgqnslc hqitaackhg
      301 gdlyvvggsi prrmwkcnna tvdwewcapl prdrlqhtlv svpgkdaiys lggktlqdtl
      361 snaviyyrvg dnvwtettql evavsgaaga nlngiiyllg geendldfft kpsrliqcfd
      421 tetdkchvkp yvlpfagrmh aavhkdlvfi vaegdslvcy nplldsftrl clpeawssap
      481 slwkiascng siyvfrdryk kgdantykld patsavtvtr gikvlltnlq fvla
//
LOCUS       NP_005602               1139 aa            linear   PRI 27-APR-2025
DEFINITION  retinoblastoma-like protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_005602
VERSION     NP_005602.3
DBSOURCE    REFSEQ: accession NM_005611.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Militi,S., Nibhani,R., Jalali,M. and Pauklin,S.
  TITLE     RBL2-E2F-GCN5 guide cell fate decisions during tissue specification
            by regulating cell-cycle-dependent fluctuations of
            non-cell-autonomous signaling
  JOURNAL   Cell Rep 42 (9), 113146 (2023)
   PUBMED   37725511
  REMARK    GeneRIF: RBL2-E2F-GCN5 guide cell fate decisions during tissue
            specification by regulating cell-cycle-dependent fluctuations of
            non-cell-autonomous signaling.
REFERENCE   2  (residues 1 to 1139)
  AUTHORS   Nakanoh,S., Kadiwala,J., Pinte,L., Morell,C.M., Lenaerts,A.S. and
            Vallier,L.
  TITLE     Simultaneous depletion of RB, RBL1 and RBL2 affects endoderm
            differentiation of human embryonic stem cells
  JOURNAL   PLoS One 17 (11), e0269122 (2022)
   PUBMED   36413521
  REMARK    GeneRIF: Simultaneous depletion of RB, RBL1 and RBL2 affects
            endoderm differentiation of human embryonic stem cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1139)
  AUTHORS   Ullah,F., Khurshid,N., Fatimi,Q., Loidl,P. and Saeed,M.
  TITLE     Mutations in the acetylation hotspots of Rbl2 are associated with
            increased risk of breast cancer
  JOURNAL   PLoS One 17 (4), e0266196 (2022)
   PUBMED   35385527
  REMARK    GeneRIF: Mutations in the acetylation hotspots of Rbl2 are
            associated with increased risk of breast cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1139)
  AUTHORS   Samra,N., Toubiana,S., Yttervik,H., Tzur-Gilat,A., Morani,I.,
            Itzkovich,C., Giladi,L., Abu Jabal,K., Cao,J.Z., Godley,L.A.,
            Mory,A., Baris Feldman,H., Tveten,K., Selig,S. and Weiss,K.
  TITLE     RBL2 bi-allelic truncating variants cause severe motor and
            cognitive impairment without evidence for abnormalities in DNA
            methylation or telomeric function
  JOURNAL   J Hum Genet 66 (11), 1101-1112 (2021)
   PUBMED   33980986
  REMARK    GeneRIF: RBL2 bi-allelic truncating variants cause severe motor and
            cognitive impairment without evidence for abnormalities in DNA
            methylation or telomeric function.
REFERENCE   5  (residues 1 to 1139)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1139)
  AUTHORS   Hijmans,E.M., Voorhoeve,P.M., Beijersbergen,R.L., van 't Veer,L.J.
            and Bernards,R.
  TITLE     E2F-5, a new E2F family member that interacts with p130 in vivo
  JOURNAL   Mol Cell Biol 15 (6), 3082-3089 (1995)
   PUBMED   7760804
REFERENCE   7  (residues 1 to 1139)
  AUTHORS   Hannon,G.J., Demetrick,D. and Beach,D.
  TITLE     Isolation of the Rb-related p130 through its interaction with CDK2
            and cyclins
  JOURNAL   Genes Dev 7 (12A), 2378-2391 (1993)
   PUBMED   8253384
REFERENCE   8  (residues 1 to 1139)
  AUTHORS   Li,Y., Graham,C., Lacy,S., Duncan,A.M. and Whyte,P.
  TITLE     The adenovirus E1A-associated 130-kD protein is encoded by a member
            of the retinoblastoma gene family and physically interacts with
            cyclins A and E
  JOURNAL   Genes Dev 7 (12A), 2366-2377 (1993)
   PUBMED   8253383
REFERENCE   9  (residues 1 to 1139)
  AUTHORS   Yeung,R.S., Bell,D.W., Testa,J.R., Mayol,X., Baldi,A., Grana,X.,
            Klinga-Levan,K., Knudson,A.G. and Giordano,A.
  TITLE     The retinoblastoma-related gene, RB2, maps to human chromosome
            16q12 and rat chromosome 19
  JOURNAL   Oncogene 8 (12), 3465-3468 (1993)
   PUBMED   8247552
REFERENCE   10 (residues 1 to 1139)
  AUTHORS   Dyson,N., Guida,P., Munger,K. and Harlow,E.
  TITLE     Homologous sequences in adenovirus E1A and human papillomavirus E7
            proteins mediate interaction with the same set of cellular proteins
  JOURNAL   J Virol 66 (12), 6893-6902 (1992)
   PUBMED   1331501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC034490.1 and X76061.1.
            
            On Apr 4, 2008 this sequence version replaced NP_005602.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034490.1, SRR1660807.171304.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262133.11/ ENSP00000262133.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..1139
                     /product="retinoblastoma-like protein 2 isoform 1"
                     /note="retinoblastoma-like protein 2; PRB2; RBR-2;
                     retinoblastoma-like 2; 130 kDa retinoblastoma-associated
                     protein; retinoblastoma-related protein 2"
                     /calculated_mol_wt=128236
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08999.3)"
     Region          44..134
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cd00043"
                     /db_xref="CDD:410207"
     Region          104..239
                     /region_name="DUF3452"
                     /note="Domain of unknown function (DUF3452); pfam11934"
                     /db_xref="CDD:463402"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Region          417..1024
                     /region_name="Pocket, binds E1A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08999.3)"
     Region          417..616
                     /region_name="Domain A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08999.3)"
     Region          417..609
                     /region_name="RB_A"
                     /note="Retinoblastoma-associated protein A domain;
                     pfam01858"
                     /db_xref="CDD:460364"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q64700; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            420
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:26237509; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Region          617..827
                     /region_name="Spacer"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08999.3)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11042701; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q64700; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Region          654..678
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08999.3)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Region          670..>810
                     /region_name="SP1-4_N"
                     /note="N-terminal domain of transcription factor
                     Specificity Proteins (SP) 1-4; cl41773"
                     /db_xref="CDD:425404"
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12435635,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Region          810..831
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08999.3)"
     Region          828..1024
                     /region_name="Domain B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08999.3)"
     Region          835..1024
                     /region_name="CYCLIN_RBL2"
                     /note="cyclin box found in retinoblastoma-like protein 2
                     (RBL2) and similar proteins; cd20606"
                     /db_xref="CDD:410309"
     Site            order(897,901..902,908..910,1004,1006,1009..1010,1022)
                     /site_type="other"
                     /note="LxCxE peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410309"
     Region          933..999
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08999.3)"
     Site            948
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64700; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            952
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11042701; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            966
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11042701; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            971
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:11042701; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            972
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:11042701; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            973
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:11042701; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            974
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:11042701; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:11042701; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            982
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11042701; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            986
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11042701; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            1068
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            1080
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08999.3)"
     CDS             1..1139
                     /gene="RBL2"
                     /gene_synonym="BRUWAG; P130; Rb2"
                     /coded_by="NM_005611.4:87..3506"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10748.1"
                     /db_xref="GeneID:5934"
                     /db_xref="HGNC:HGNC:9894"
                     /db_xref="MIM:180203"
ORIGIN      
        1 mpsggdqspp ppppppaaaa sdeeeeddge aedaappaes ptpqiqqrfd elcsrlnmde
       61 aaraeawdsy rsmsesytle gndlhwlaca lyvacrksvp tvskgtvegn yvsltrilkc
      121 seqslieffn kmkkwedman lpphfrerte rlernftvsa vifkkyepif qdifkypqee
      181 qprqqrgrkq rrqpctvsei fhfcwvlfiy akgnfpmisd dlvnsyhlll caldlvygna
      241 lqcsnrkelv npnfkglsed fhakdskpss dppciieklc slhdglvlea kgikehfwkp
      301 yirklyekkl lkgkeenltg flepgnfges fkainkayee yvlsvgnlde riflgedaee
      361 eigtlsrcln agsgtetaer vqmknilqqh fdkskalris tpltgvryik enspcvtpvs
      421 tathslsrlh tmltglrnap sekleqilrt csrdptqaia nrlkemfeiy sqhfqpdedf
      481 sncakeiask hfrfaemlyy kvlesvieqe qkrlgdmdls gileqdafhr sllacclevv
      541 tfsykppgnf pfiteifdvp lyhfykviev firaedglcr evvkhlnqie eqildhlawk
      601 pesplwekir dnenrvptce evmppqnler adeiciagsp ltprrvtevr adtgglgrsi
      661 tspttlydry ssppasttrr rlfvendsps dggtpgrmpp qplvnavpvq nvsgetvsvt
      721 pvpgqtlvtm atatvtanng qtvtipvqgi anenggitff pvqvnvggqa qavtgsiqpl
      781 saqalagsls sqqvtgttlq vpgqvaiqqi spggqqqkqg qsvtsssnrp rktsslslff
      841 rkvyhlaavr lrdlcakldi sdelrkkiwt cfefsiiqcp elmmdrhldq llmcaiyvma
      901 kvtkedksfq nimrcyrtqp qarsqvyrsv likgkrkrrn sgssdsrshq nsptelnkdr
      961 tsrdsspvmr ssstlpvpqp ssapptptrl tgansdmeee ergdliqfyn niyikqiktf
     1021 amkysqanmd applspypfv rtgsprriql sqnhpvyisp hknetmlspr ekifyyfsns
     1081 pskrlreins mirtgetptk krgilledgs espakricpe nhsallrrlq dvandrgsh
//
LOCUS       NP_001028222             385 aa            linear   PRI 27-APR-2025
DEFINITION  transcription termination factor 2, mitochondrial precursor [Homo
            sapiens].
ACCESSION   NP_001028222
VERSION     NP_001028222.1
DBSOURCE    REFSEQ: accession NM_001033050.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Han,Y., Gao,P., Qiu,S., Zhang,L., Yang,L., Zuo,J., Zhong,C., Zhu,S.
            and Liu,W.
  TITLE     MTERF2 contributes to MPP(+)-induced mitochondrial dysfunction and
            cell damage
  JOURNAL   Biochem Biophys Res Commun 471 (1), 177-183 (2016)
   PUBMED   26826381
  REMARK    GeneRIF: These findings demonstrate that MTERF2 contributes to
            MPP(+)-induced mitochondrial disruption and cell damage.
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Hyvarinen,A.K., Pohjoismaki,J.L., Holt,I.J. and Jacobs,H.T.
  TITLE     Overexpression of MTERFD1 or MTERFD3 impairs the completion of
            mitochondrial DNA replication
  JOURNAL   Mol Biol Rep 38 (2), 1321-1328 (2011)
   PUBMED   20577816
  REMARK    GeneRIF: MTERFD1 and MTERFD3 have a role in impairing the
            completion of mitochondrial DNA replication
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Spahr,H., Samuelsson,T., Hallberg,B.M. and Gustafsson,C.M.
  TITLE     Structure of mitochondrial transcription termination factor 3
            reveals a novel nucleic acid-binding domain
  JOURNAL   Biochem Biophys Res Commun 397 (3), 386-390 (2010)
   PUBMED   20430012
  REMARK    GeneRIF: MTERF-domain of human MTERF3 forms a half-doughnut-shaped
            right-handed superhelix.
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Pellegrini,M., Asin-Cayuela,J., Erdjument-Bromage,H., Tempst,P.,
            Larsson,N.G. and Gustafsson,C.M.
  TITLE     MTERF2 is a nucleoid component in mammalian mitochondria
  JOURNAL   Biochim Biophys Acta 1787 (5), 296-302 (2009)
   PUBMED   19366608
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Chen,Y., Zhou,G., Yu,M., He,Y., Tang,W., Lai,J., He,J., Liu,W. and
            Tan,D.
  TITLE     Cloning and functional analysis of human mTERFL encoding a novel
            mitochondrial transcription termination factor-like protein
  JOURNAL   Biochem Biophys Res Commun 337 (4), 1112-1118 (2005)
   PUBMED   16226716
  REMARK    GeneRIF: mTERFL is a novel mTERF family member and a
            serum-inhibitory factor probably participating in the regulation of
            cell growth
REFERENCE   8  (residues 1 to 385)
  AUTHORS   Linder,T., Park,C.B., Asin-Cayuela,J., Pellegrini,M., Larsson,N.G.,
            Falkenberg,M., Samuelsson,T. and Gustafsson,C.M.
  TITLE     A family of putative transcription termination factors shared
            amongst metazoans and plants
  JOURNAL   Curr Genet 48 (4), 265-269 (2005)
   PUBMED   16193327
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK024124.1, BC025984.1 and AC007541.9.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.362250.1,
                                           SRR1803616.175706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000240050.9/
                                                  ENSP00000240050.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..385
                     /product="transcription termination factor 2,
                     mitochondrial precursor"
                     /note="mTERF domain-containing protein 3, mitochondrial;
                     mitochondrial transcription termination factor-like
                     protein; MTERF domain containing 3; transcription
                     termination factor 2, mitochondrial; mTERF-like"
                     /calculated_mol_wt=40104
     transit_peptide 1..35
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:19366608; propagated from
                     UniProtKB/Swiss-Prot (Q49AM1.2)"
                     /calculated_mol_wt=4328
     mat_peptide     36..385
                     /product="Transcription termination factor 2,
                     mitochondrial. /id=PRO_0000255464"
                     /note="propagated from UniProtKB/Swiss-Prot (Q49AM1.2)"
                     /calculated_mol_wt=40104
     Region          58..360
                     /region_name="mTERF"
                     /note="pfam02536"
                     /db_xref="CDD:460581"
     CDS             1..385
                     /gene="MTERF2"
                     /gene_synonym="MTERFD3; mTERFL"
                     /coded_by="NM_001033050.3:347..1504"
                     /db_xref="CCDS:CCDS9111.1"
                     /db_xref="GeneID:80298"
                     /db_xref="HGNC:HGNC:30779"
                     /db_xref="MIM:616929"
ORIGIN      
        1 mlwklllrsq scrlcsfrkm rsppkyrpfl acftyttdkq sskentrtve klykcsvdir
       61 kirrlkgwvl ledetyveei anilqelgad etavasiler cpeaivcspt avntqrklwq
      121 lvckneeeli klieqfpesf ftikdqenqk lnvqffqelg lknvvisrll taapnvfhnp
      181 veknkqmvri lqesyldvgg seanmkvwll kllsqnpfil lnsptaiket leflqeqgft
      241 sfeilqllsk lkgflfqlcp rsiqnsisfs knafkctdhd lkqlvlkcpa llyysvpvle
      301 ermqgllreg isiaqiretp mvleltpqiv qyrirklnss gyrikdghla nlngskkefe
      361 anfgkiqakk vrplfnpvap lnvee
//
LOCUS       NP_002196               1049 aa            linear   PRI 27-APR-2025
DEFINITION  integrin alpha-5 precursor [Homo sapiens].
ACCESSION   NP_002196
VERSION     NP_002196.4
DBSOURCE    REFSEQ: accession NM_002205.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Messe,M., Bernhard,C., Foppolo,S., Thomas,L., Marchand,P.,
            Herold-Mende,C., Idbaih,A., Kessler,H., Etienne-Selloum,N.,
            Ochoa,C., Tambar,U.K., Elati,M., Laquerriere,P., Entz-Werle,N.,
            Martin,S., Reita,D. and Dontenwill,M.
  TITLE     Hypoxia-driven heterogeneous expression of alpha5 integrin in
            glioblastoma stem cells is linked to HIF-2alpha
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (8), 167471 (2024)
   PUBMED   39154793
  REMARK    GeneRIF: Hypoxia-driven heterogeneous expression of alpha5 integrin
            in glioblastoma stem cells is linked to HIF-2alpha.
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Ezzo,M., Spindler,K., Wang,J.B., Lee,D., Pecoraro,G., Cowen,J.,
            Pakshir,P. and Hinz,B.
  TITLE     Acute contact with profibrotic macrophages mechanically activates
            fibroblasts via alphavbeta3 integrin-mediated engagement of Piezo1
  JOURNAL   Sci Adv 10 (43), eadp4726 (2024)
   PUBMED   39441936
  REMARK    GeneRIF: Acute contact with profibrotic macrophages mechanically
            activates fibroblasts via alphavbeta3 integrin-mediated engagement
            of Piezo1.
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Fu,Y., Sun,X., He,Q., Gu,Z., Jia,X. and Zhuang,Z.
  TITLE     Connexin 43 controls metastatic behavior in triple negative breast
            cancer through TGFbeta1-Smad3-intergin alphaV signaling axis Based
            on optical image diagnosis
  JOURNAL   SLAS Technol 29 (5), 100190 (2024)
   PUBMED   39299505
  REMARK    GeneRIF: Connexin 43 controls metastatic behavior in triple
            negative breast cancer through TGFbeta1-Smad3-intergin alphaV
            signaling axis Based on optical image diagnosis.
REFERENCE   4  (residues 1 to 1049)
  AUTHORS   Lu,H., Ai,J., Zheng,Y., Zhou,W., Zhang,L., Zhu,J., Zhang,H. and
            Wang,S.
  TITLE     IGFBP2/ITGA5 promotes gefitinib resistance via activating
            STAT3/CXCL1 axis in non-small cell lung cancer
  JOURNAL   Cell Death Dis 15 (6), 447 (2024)
   PUBMED   38918360
  REMARK    GeneRIF: IGFBP2/ITGA5 promotes gefitinib resistance via activating
            STAT3/CXCL1 axis in non-small cell lung cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1049)
  AUTHORS   Wu,Z., Jiao,M., Shu,C., Zhang,S., Wang,J., Pu,J., Zhu,J., Zeng,Y.,
            Zhu,Y. and Liu,Z.
  TITLE     Integrin alphaVbeta1-activated PYK2 promotes the progression of
            non-small-cell lung cancer via the STAT3-VGF axis
  JOURNAL   Cell Commun Signal 22 (1), 313 (2024)
   PUBMED   38844957
  REMARK    GeneRIF: Integrin alphaVbeta1-activated PYK2 promotes the
            progression of non-small-cell lung cancer via the STAT3-VGF axis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1049)
  AUTHORS   Birkenmeier,T.M., McQuillan,J.J., Boedeker,E.D., Argraves,W.S.,
            Ruoslahti,E. and Dean,D.C.
  TITLE     The alpha 5 beta 1 fibronectin receptor. Characterization of the
            alpha 5 gene promoter
  JOURNAL   J Biol Chem 266 (30), 20544-20549 (1991)
   PUBMED   1834647
REFERENCE   7  (residues 1 to 1049)
  AUTHORS   Brake,D.A., Debouck,C. and Biesecker,G.
  TITLE     Identification of an Arg-Gly-Asp (RGD) cell adhesion site in human
            immunodeficiency virus type 1 transactivation protein, tat
  JOURNAL   J Cell Biol 111 (3), 1275-1281 (1990)
   PUBMED   2202737
REFERENCE   8  (residues 1 to 1049)
  AUTHORS   Smith,J.W., Vestal,D.J., Irwin,S.V., Burke,T.A. and Cheresh,D.A.
  TITLE     Purification and functional characterization of integrin alpha v
            beta 5. An adhesion receptor for vitronectin
  JOURNAL   J Biol Chem 265 (19), 11008-11013 (1990)
   PUBMED   1694173
REFERENCE   9  (residues 1 to 1049)
  AUTHORS   Dedhar,S. and Gray,V.
  TITLE     Isolation of a novel integrin receptor mediating
            Arg-Gly-Asp-directed cell adhesion to fibronectin and type I
            collagen from human neuroblastoma cells. Association of a novel
            beta 1-related subunit with alpha v
  JOURNAL   J Cell Biol 110 (6), 2185-2193 (1990)
   PUBMED   1693626
REFERENCE   10 (residues 1 to 1049)
  AUTHORS   Argraves,W.S., Pytela,R., Suzuki,S., Millan,J.L.,
            Pierschbacher,M.D. and Ruoslahti,E.
  TITLE     cDNA sequences from the alpha subunit of the fibronectin receptor
            predict a transmembrane domain and a short cytoplasmic peptide
  JOURNAL   J Biol Chem 261 (28), 12922-12924 (1986)
   PUBMED   2944883
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK312414.1, BC008786.2 and
            BX647780.1.
            
            On Apr 13, 2016 this sequence version replaced NP_002196.3.
            
            Summary: The product of this gene belongs to the integrin alpha
            chain family. Integrins are heterodimeric integral membrane
            proteins composed of an alpha subunit and a beta subunit that
            function in cell surface adhesion and signaling. The encoded
            preproprotein is proteolytically processed to generate light and
            heavy chains that comprise the alpha 5 subunit. This subunit
            associates with the beta 1 subunit to form a fibronectin receptor.
            This integrin may promote tumor invasion, and higher expression of
            this gene may be correlated with shorter survival time in lung
            cancer patients. Note that the integrin alpha 5 and integrin alpha
            V subunits are encoded by distinct genes. [provided by RefSeq, Oct
            2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X06256.1, AK312414.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000293379.9/ ENSP00000293379.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..1049
                     /product="integrin alpha-5 precursor"
                     /note="very late activation protein 5, alpha subunit;
                     fibronectin receptor, alpha subunit; integrin, alpha 5
                     (fibronectin receptor, alpha polypeptide); integrin
                     alpha-5; integrin alpha-F; CD49 antigen-like family member
                     E; fibronectin receptor subunit alpha; ITGA5/SLC9B1
                     fusion"
                     /calculated_mol_wt=110013
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4543
     mat_peptide     42..1049
                     /product="Integrin alpha-5. /id=PRO_0000016249"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
                     /calculated_mol_wt=110013
     mat_peptide     42..894
                     /product="Integrin alpha-5 heavy chain.
                     /id=PRO_0000016250"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
                     /calculated_mol_wt=92402
     Region          43..108
                     /region_name="FG-GAP 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     Region          56..114
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22451694,
                     ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
                     ECO:0007744|PDB:7NXD; propagated from UniProtKB/Swiss-Prot
                     (P08648.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P08648.2)"
     Region          128..188
                     /region_name="FG-GAP 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     Site            182
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22451694,
                     ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
                     ECO:0007744|PDB:7NXD; propagated from UniProtKB/Swiss-Prot
                     (P08648.2)"
     Region          192..245
                     /region_name="FG-GAP 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     Region          259..311
                     /region_name="FG-GAP 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     Region          268..>310
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Site            297
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:22451694,
                     ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
                     ECO:0007744|PDB:7NXD; propagated from UniProtKB/Swiss-Prot
                     (P08648.2)"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:22451694,
                     ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
                     ECO:0007744|PDB:7NXD; propagated from UniProtKB/Swiss-Prot
                     (P08648.2)"
     Region          312..377
                     /region_name="FG-GAP 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     Site            316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22451694,
                     ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
                     ECO:0007744|PDB:7NXD; propagated from UniProtKB/Swiss-Prot
                     (P08648.2)"
     Region          322..379
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          378..437
                     /region_name="FG-GAP 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     Region          389..443
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          441..504
                     /region_name="FG-GAP 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00803"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     Region          455..498
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          490..921
                     /region_name="Integrin_alpha2"
                     /note="Integrin alpha; pfam08441"
                     /db_xref="CDD:462478"
     Site            524
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33962943,
                     ECO:0007744|PDB:7NXD; propagated from UniProtKB/Swiss-Prot
                     (P08648.2)"
     Site            530
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08648.2)"
     Site            593
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08648.2)"
     Site            609
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22451694,
                     ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
                     ECO:0007744|PDB:7NXD; propagated from UniProtKB/Swiss-Prot
                     (P08648.2)"
     Site            675
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P08648.2)"
     Site            712
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08648.2)"
     Site            724
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08648.2)"
     Site            773
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P08648.2)"
     Site            868
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08648.2)"
     Region          877..907
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     mat_peptide     895..1049
                     /product="Integrin alpha-5 light chain.
                     /id=PRO_0000016251"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
                     /calculated_mol_wt=17629
     Site            996..1021
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     Region          1021..1028
                     /region_name="Interaction with HPS5.
                     /evidence=ECO:0000269|PubMed:10094488"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     Region          1024..1028
                     /region_name="GFFKR motif. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P08648.2)"
     CDS             1..1049
                     /gene="ITGA5"
                     /gene_synonym="CD49e; FNRA; VLA-5; VLA5A"
                     /coded_by="NM_002205.5:69..3218"
                     /db_xref="CCDS:CCDS8880.1"
                     /db_xref="GeneID:3678"
                     /db_xref="HGNC:HGNC:6141"
                     /db_xref="MIM:135620"
ORIGIN      
        1 mgsrtpespl havqlrwgpr rrppllplll lllpppprvg gfnldaeapa vlsgppgsff
       61 gfsvefyrpg tdgvsvlvga pkantsqpgv lqggavylcp wgasptqctp iefdskgsrl
      121 lesslssseg eepveykslq wfgatvrahg ssilacaply swrtekepls dpvgtcylst
      181 dnftrileya pcrsdfswaa gqgycqggfs aeftktgrvv lggpgsyfwq gqilsatqeq
      241 iaesyypeyl inlvqgqlqt rqassiydds ylgysvavge fsgddtedfv agvpkgnlty
      301 gyvtilngsd irslynfsge qmasyfgyav aatdvngdgl ddllvgapll mdrtpdgrpq
      361 evgrvyvylq hpagieptpt ltltghdefg rfgssltplg dldqdgyndv aigapfgget
      421 qqgvvfvfpg gpgglgskps qvlqplwaas htpdffgsal rggrdldgng ypdlivgsfg
      481 vdkavvyrgr pivsasaslt ifpamfnpee rscslegnpv acinlsfcln asgkhvadsi
      541 gftvelqldw qkqkggvrra lflasrqatl tqtlliqnga redcremkiy lrnesefrdk
      601 lspihialnf sldpqapvds hglrpalhyq sksriedkaq illdcgedni cvpdlqlevf
      661 geqnhvylgd knalnltfha qnvgeggaye aelrvtappe aeysglvrhp gnfsslscdy
      721 favnqsrllv cdlgnpmkag aslwgglrft vphlrdtkkt iqfdfqilsk nlnnsqsdvv
      781 sfrlsveaqa qvtlngvskp eavlfpvsdw hprdqpqkee dlgpavhhvy elinqgpssi
      841 sqgvlelscp qalegqqlly vtrvtglnct tnhpinpkgl eldpegslhh qqkreapsrs
      901 sassgpqilk cpeaecfrlr celgplhqqe sqslqlhfrv waktflqreh qpfslqceav
      961 ykalkmpyri lprqlpqker qvatavqwtk aegsygvplw iiilailfgl lllglliyil
     1021 yklgffkrsl pygtamekaq lkppatsda
//
LOCUS       NP_005140                448 aa            linear   PRI 27-APR-2025
DEFINITION  T-box transcription factor TBX19 [Homo sapiens].
ACCESSION   NP_005140
VERSION     NP_005140.1
DBSOURCE    REFSEQ: accession NM_005149.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Uccella,S., Leoni,E., Kaiser,S., Maragliano,R., Valerio,A.,
            Libera,L., Tanda,M.L., Volante,M., Diviani,D. and La Rosa,S.
  TITLE     Heterogeneity of TPIT expression in ACTH-secreting extra-pituitary
            neuroendocrine tumors (NETs) supports the existence of different
            cellular programs in pancreatic and pulmonary NETs
  JOURNAL   Virchows Arch 483 (5), 635-643 (2023)
   PUBMED   37726450
  REMARK    GeneRIF: Heterogeneity of TPIT expression in ACTH-secreting
            extra-pituitary neuroendocrine tumors (NETs) supports the existence
            of different cellular programs in pancreatic and pulmonary NETs.
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Charnay,T., Mougel,G., Amouroux,C., Gueorguieva,I., Joubert,F.,
            Pertuit,M., Reynaud,R., Barlier,A., Brue,T. and Saveanu,A.
  TITLE     A novel TBX19 gene mutation in patients with isolated ACTH
            deficiency from distinct families with a common geographical origin
  JOURNAL   Front Endocrinol (Lausanne) 13, 1080649 (2023)
   PUBMED   36890856
  REMARK    GeneRIF: A novel TBX19 gene mutation in patients with isolated ACTH
            deficiency from distinct families with a common geographical
            origin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yao,H., Xie,W., Dai,Y., Liu,Y., Gu,W., Li,J., Wu,L., Xie,J.,
            Rui,W., Ren,B., Xue,L., Cheng,Y., Lin,S., Li,C., Tang,H., Wang,Y.,
            Lou,M., Zhang,X., Hu,R., Shang,H., Huang,J. and Wu,Z.B.
  TITLE     TRIM65 determines the fate of a novel subtype of pituitary
            neuroendocrine tumors via ubiquitination and degradation of TPIT
  JOURNAL   Neuro Oncol 24 (8), 1286-1297 (2022)
   PUBMED   35218667
  REMARK    GeneRIF: TRIM65 determines the fate of a novel subtype of pituitary
            neuroendocrine tumors via ubiquitination and degradation of TPIT.
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Ji,X., Chen,X., Zhang,B., Xie,M., Zhang,T., Luo,X., Liu,D.,
            Feng,Y., Wang,Y., Sun,M., Li,C., Huang,W. and Xia,L.
  TITLE     T-box transcription factor 19 promotes hepatocellular carcinoma
            metastasis through upregulating EGFR and RAC1
  JOURNAL   Oncogene 41 (15), 2225-2238 (2022)
   PUBMED   35217793
  REMARK    GeneRIF: T-box transcription factor 19 promotes hepatocellular
            carcinoma metastasis through upregulating EGFR and RAC1.
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Wu,S., Chen,Q., Shen,L., Wei,H. and Chen,Y.
  TITLE     [Analysis of TBX19 gene variant in a child with congenital isolated
            adrenocorticotropic hormone deficiency]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 38 (1), 59-62 (2021)
   PUBMED   33423260
  REMARK    GeneRIF: [Analysis of TBX19 gene variant in a child with congenital
            isolated adrenocorticotropic hormone deficiency].
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Pulichino,A.M., Vallette-Kasic,S., Tsai,J.P., Couture,C.,
            Gauthier,Y. and Drouin,J.
  TITLE     Tpit determines alternate fates during pituitary cell
            differentiation
  JOURNAL   Genes Dev 17 (6), 738-747 (2003)
   PUBMED   12651892
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Pulichino,A.M., Vallette-Kasic,S., Couture,C., Gauthier,Y.,
            Brue,T., David,M., Malpuech,G., Deal,C., Van Vliet,G., De
            Vroede,M., Riepe,F.G., Partsch,C.J., Sippell,W.G., Berberoglu,M.,
            Atasay,B. and Drouin,J.
  TITLE     Human and mouse TPIT gene mutations cause early onset pituitary
            ACTH deficiency
  JOURNAL   Genes Dev 17 (6), 711-716 (2003)
   PUBMED   12651888
  REMARK    GeneRIF: TPIT has a role in expression of the pro-opiomelanocortin
            gene and terminal differentiation of the pituitary corticotroph
            lineage, and its mutation causes early onset pituitary ACTH
            deficiency
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Asteria,C.
  TITLE     T-box and isolated ACTH deficiency
  JOURNAL   Eur J Endocrinol 146 (4), 463-465 (2002)
   PUBMED   11916612
  REMARK    GeneRIF: Review.  Association of 2 mutations with an ACTH
            deficiency is consistent with the role of tbx19 in differentiation
            of POMC cells.
            Review article
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Lamolet,B., Pulichino,A.M., Lamonerie,T., Gauthier,Y., Brue,T.,
            Enjalbert,A. and Drouin,J.
  TITLE     A pituitary cell-restricted T box factor, Tpit, activates POMC
            transcription in cooperation with Pitx homeoproteins
  JOURNAL   Cell 104 (6), 849-859 (2001)
   PUBMED   11290323
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Yi,C.H., Terrett,J.A., Li,Q.Y., Ellington,K., Packham,E.A.,
            Armstrong-Buisseret,L., McClure,P., Slingsby,T. and Brook,J.D.
  TITLE     Identification, mapping, and phylogenomic analysis of four new
            human members of the T-box gene family: EOMES, TBX6, TBX18, and
            TBX19
  JOURNAL   Genomics 55 (1), 10-20 (1999)
   PUBMED   9888994
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL009051.1, AJ010277.1 and
            AK091404.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of a phylogenetically conserved
            family of genes that share a common DNA-binding domain, the T-box.
            T-box genes encode transcription factors involved in the regulation
            of developmental processes. Mutations in this gene were found in
            patients with isolated deficiency of pituitary POMC-derived ACTH,
            suggesting an essential role for this gene in differentiation of
            the pituitary POMC lineage. ACTH deficiency is characterized by
            adrenal insufficiency symptoms such as weight loss, lack of
            appetite (anorexia), weakness, nausea, vomiting, and low blood
            pressure. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ010277.1, BC093664.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367821.8/ ENSP00000356795.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..448
                     /product="T-box transcription factor TBX19"
                     /note="TBS 19; T-box protein 19; T-box factor, pituitary;
                     T-box 19"
                     /calculated_mol_wt=48107
     Region          36..218
                     /region_name="T-box_TBX19-like"
                     /note="DNA-binding domain of T-box transcription factor 19
                     and related T-box proteins; cd20201"
                     /db_xref="CDD:410327"
     Site            order(65,68..69,100,102,146,149..150,161..162,195..197,
                     203,206..207,210..212,214..216)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410327"
     Site            order(86,128..131)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:410327"
     CDS             1..448
                     /gene="TBX19"
                     /gene_synonym="dJ747L4.1; TBS19; TPIT"
                     /coded_by="NM_005149.3:215..1561"
                     /db_xref="CCDS:CCDS1272.1"
                     /db_xref="GeneID:9095"
                     /db_xref="HGNC:HGNC:11596"
                     /db_xref="MIM:604614"
ORIGIN      
        1 mamselgtrk psdgtvshll nvveselqag rekgdptekq lqiiledapl wqrfkevtne
       61 mivtkngrrm fpvlkisvtg ldpnamysll ldfvptdshr wkyvngewvp agkpevsshs
      121 cvyihpdspn fgahwmkapi sfskvkltnk lngggqimln slhkyepqvh ivrvgsahrm
      181 vtncsfpetq fiavtayqne eitalkikyn pfakafldak ernhlrdvpe aisesqhvty
      241 shlggwifsn pdgvctagns nyqyaaplpl paphthhgce hysglrghrq apypsaymhr
      301 nhspsvnlie sssnnlqvfs gpdswtslss tphasilsvp htngpinpgp spypclwtis
      361 ngaggpsgpg pevhastpga fllgnpavts ppsvlstqap tsagvevlge psltsiavst
      421 wtavashpfa gwggpgaggh hspssldg
//
LOCUS       NP_001347389             364 aa            linear   ROD 27-APR-2025
DEFINITION  START domain-containing protein 10 isoform 1 [Mus musculus].
ACCESSION   NP_001347389 XP_011240167
VERSION     NP_001347389.1
DBSOURCE    REFSEQ: accession NM_001360460.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Carrat,G.R., Haythorne,E., Tomas,A., Haataja,L., Muller,A.,
            Arvan,P., Piunti,A., Cheng,K., Huang,M., Pullen,T.J.,
            Georgiadou,E., Stylianides,T., Amirruddin,N.S., Salem,V.,
            Distaso,W., Cakebread,A., Heesom,K.J., Lewis,P.A., Hodson,D.J.,
            Briant,L.J., Fung,A.C.H., Sessions,R.B., Alpy,F., Kong,A.P.S.,
            Benke,P.I., Torta,F., Teo,A.K.K., Leclerc,I., Solimena,M.,
            Wigley,D.B. and Rutter,G.A.
  TITLE     The type 2 diabetes gene product STARD10 is a
            phosphoinositide-binding protein that controls insulin secretory
            granule biogenesis
  JOURNAL   Mol Metab 40, 101015 (2020)
   PUBMED   32416313
  REMARK    GeneRIF: The type 2 diabetes gene product STARD10 is a
            phosphoinositide-binding protein that controls insulin secretory
            granule biogenesis.
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Floris,A., Luo,J., Frank,J., Zhou,J., Orru,S., Biancolella,M.,
            Pucci,S., Orlandi,A., Campagna,P., Balzano,A., Ramani,K. and
            Tomasi,M.L.
  TITLE     Star-related lipid transfer protein 10 (STARD10): a novel key
            player in alcohol-induced breast cancer progression
  JOURNAL   J Exp Clin Cancer Res 38 (1), 4 (2019)
   PUBMED   30611309
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Carrat,G.R., Hu,M., Nguyen-Tu,M.S., Chabosseau,P., Gaulton,K.J.,
            van de Bunt,M., Siddiq,A., Falchi,M., Thurner,M., Canouil,M.,
            Pattou,F., Leclerc,I., Pullen,T.J., Cane,M.C., Prabhala,P.,
            Greenwald,W., Schulte,A., Marchetti,P., Ibberson,M.,
            MacDonald,P.E., Manning Fox,J.E., Gloyn,A.L., Froguel,P.,
            Solimena,M., McCarthy,M.I. and Rutter,G.A.
  TITLE     Decreased STARD10 Expression Is Associated with Defective Insulin
            Secretion in Humans and Mice
  JOURNAL   Am J Hum Genet 100 (2), 238-256 (2017)
   PUBMED   28132686
  REMARK    GeneRIF: StarD10 is required for normal insulin secretion, though
            its deletion enhances proinsulin processing.
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Dickinson,M.E., Flenniken,A.M., Ji,X., Teboul,L., Wong,M.D.,
            White,J.K., Meehan,T.F., Weninger,W.J., Westerberg,H., Adissu,H.,
            Baker,C.N., Bower,L., Brown,J.M., Caddle,L.B., Chiani,F., Clary,D.,
            Cleak,J., Daly,M.J., Denegre,J.M., Doe,B., Dolan,M.E., Edie,S.M.,
            Fuchs,H., Gailus-Durner,V., Galli,A., Gambadoro,A., Gallegos,J.,
            Guo,S., Horner,N.R., Hsu,C.W., Johnson,S.J., Kalaga,S., Keith,L.C.,
            Lanoue,L., Lawson,T.N., Lek,M., Mark,M., Marschall,S., Mason,J.,
            McElwee,M.L., Newbigging,S., Nutter,L.M., Peterson,K.A.,
            Ramirez-Solis,R., Rowland,D.J., Ryder,E., Samocha,K.E.,
            Seavitt,J.R., Selloum,M., Szoke-Kovacs,Z., Tamura,M., Trainor,A.G.,
            Tudose,I., Wakana,S., Warren,J., Wendling,O., West,D.B., Wong,L.,
            Yoshiki,A., MacArthur,D.G., Tocchini-Valentini,G.P., Gao,X.,
            Flicek,P., Bradley,A., Skarnes,W.C., Justice,M.J., Parkinson,H.E.,
            Moore,M., Wells,S., Braun,R.E., Svenson,K.L., de Angelis,M.H.,
            Herault,Y., Mohun,T., Mallon,A.M., Henkelman,R.M., Brown,S.D.,
            Adams,D.J., Lloyd,K.C., McKerlie,C., Beaudet,A.L., Bucan,M. and
            Murray,S.A.
  CONSRTM   International Mouse Phenotyping Consortium; Jackson Laboratory;
            Infrastructure Nationale PHENOMIN, Institut Clinique de la Souris
            (ICS); Charles River Laboratories; MRC Harwell; Toronto Centre for
            Phenogenomics; Wellcome Trust Sanger Institute; RIKEN BioResource
            Center
  TITLE     High-throughput discovery of novel developmental phenotypes
  JOURNAL   Nature 537 (7621), 508-514 (2016)
   PUBMED   27626380
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24643. PMID: 29144450]
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Ito,M., Yamanashi,Y., Toyoda,Y., Izumi-Nakaseko,H., Oda,S.,
            Sugiyama,A., Kuroda,M., Suzuki,H., Takada,T. and Adachi-Akahane,S.
  TITLE     Disruption of Stard10 gene alters the PPARalpha-mediated bile acid
            homeostasis
  JOURNAL   Biochim Biophys Acta 1831 (2), 459-468 (2013)
   PUBMED   23200860
  REMARK    GeneRIF: results indicate that STARD10 is involved in regulating
            bile acid metabolism through the modulation of PPARalpha-mediated
            mechanism.
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Aksu,S., Koczan,D., Renne,U., Thiesen,H.J. and Brockmann,G.A.
  TITLE     Differentially expressed genes in adipose tissues of high body
            weight-selected (obese) and unselected (lean) mouse lines
  JOURNAL   J Appl Genet 48 (2), 133-143 (2007)
   PUBMED   17495347
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Tabibiazar,R., Wagner,R.A., Liao,A. and Quertermous,T.
  TITLE     Transcriptional profiling of the heart reveals chamber-specific
            gene expression patterns
  JOURNAL   Circ Res 93 (12), 1193-1201 (2003)
   PUBMED   14576202
  REMARK    GeneRIF: Stard10 (Sdccag28) is much more highly transcribed in
            cardiac atria than in cardiac ventricles.
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Yamanaka,M., Koga,M., Tanaka,H., Nakamura,Y., Ohta,H., Yomogida,K.,
            Tsuchida,J., Iguchi,N., Nojima,H., Nozaki,M., Matsumiya,K.,
            Okuyama,A., Toshimori,K. and Nishimune,Y.
  TITLE     Molecular cloning and characterization of phosphatidylcholine
            transfer protein-like protein gene expressed in murine haploid germ
            cells
  JOURNAL   Biol Reprod 62 (6), 1694-1701 (2000)
   PUBMED   10819773
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC107638.18 and AC129079.5.
            
            On Feb 3, 2018 this sequence version replaced XP_011240167.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB031550.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849384
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 54.55 cM"
     Protein         1..364
                     /product="START domain-containing protein 10 isoform 1"
                     /note="PCTP-like protein; PCTP-L; START domain-containing
                     protein 10; stAR-related lipid transfer protein 10; START
                     domain containing 10; serologically defined colon cancer
                     antigen 28 homolog; serologically defined colon cancer
                     antigen 10"
                     /calculated_mol_wt=39985
     Region          92..314
                     /region_name="START_STARD10-like"
                     /note="Lipid-binding START domain of mammalian STARD10 and
                     related proteins; cd08871"
                     /db_xref="CDD:176880"
     Site            order(119..120,127,141,143,155,159,165,168..169,171..172,
                     191,193..196,198,201,203,205,220,237,239..242,244,256,258,
                     260,262,264,266,273,275..277,279..281,284..285,288)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:176880"
     CDS             1..364
                     /gene="Stard10"
                     /gene_synonym="CGI-52; NY-C0-28; PC-TP2; PCTP2; Pctpl;
                     Sdccag28; SdccagG28; TISP-81"
                     /coded_by="NM_001360460.1:140..1234"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS90281.1"
                     /db_xref="GeneID:56018"
                     /db_xref="MGI:MGI:1860093"
ORIGIN      
        1 mgpraapgrp gsggsggggr artpapagpg reartgprkv asasaaastl sepprrtqes
       61 rtrtrapglp tlpmekpaas tepqgsrpal gresvqvpdd qdfrsfrsec eaevgwnlty
      121 skagvsvwvq avemdrtlhk ikcrmeccdv paetlydvlh dieyrkkwds nvietfdiar
      181 ltvnadvgyy swrcpkplkn rdvitlrswl pmgadyiimn ysvkhpkypp rkdlvravsi
      241 qtgyliqstg pkscvityla qvdpkgslpk wvvnkssqfl apkamkkmyk acikypewkq
      301 khqphfkpwl hpeqsplpsl alselsvqha dslenidesa vtesreerag gaggegsddd
      361 tslt
//
LOCUS       NP_000632                199 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-11 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_000632
VERSION     NP_000632.1
DBSOURCE    REFSEQ: accession NM_000641.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Ng,B., Huang,K.Y., Pua,C.J., Viswanathan,S., Lim,W.W.,
            Kuthubudeen,F.F., Liu,Y.N., Hii,A.A., George,B.L., Widjaja,A.A.,
            Petretto,E. and Cook,S.A.
  TITLE     Interleukin-11 causes alveolar type 2 cell dysfunction and prevents
            alveolar regeneration
  JOURNAL   Nat Commun 15 (1), 8530 (2024)
   PUBMED   39358385
  REMARK    GeneRIF: Interleukin-11 causes alveolar type 2 cell dysfunction and
            prevents alveolar regeneration.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Liang,P., Ness,J., Rapp,J., Boneva,S., Schwammle,M., Jung,M.,
            Schlunck,G., Agostini,H. and Bucher,F.
  TITLE     Characterization of the angiomodulatory effects of Interleukin 11
            cis- and trans-signaling in the retina
  JOURNAL   J Neuroinflammation 21 (1), 230 (2024)
   PUBMED   39294742
  REMARK    GeneRIF: Characterization of the angiomodulatory effects of
            Interleukin 11 cis- and trans-signaling in the retina.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Widjaja,A.A., Lim,W.W., Viswanathan,S., Chothani,S., Corden,B.,
            Dasan,C.M., Goh,J.W.T., Lim,R., Singh,B.K., Tan,J., Pua,C.J.,
            Lim,S.Y., Adami,E., Schafer,S., George,B.L., Sweeney,M., Xie,C.,
            Tripathi,M., Sims,N.A., Hubner,N., Petretto,E., Withers,D.J.,
            Ho,L., Gil,J., Carling,D. and Cook,S.A.
  TITLE     Inhibition of IL-11 signalling extends mammalian healthspan and
            lifespan
  JOURNAL   Nature 632 (8023), 157-165 (2024)
   PUBMED   39020175
  REMARK    GeneRIF: Inhibition of IL-11 signalling extends mammalian
            healthspan and lifespan.
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Milara,J., Roger,I., Montero,P., Artigues,E., Escriva,J., Del
            Rio,R. and Cortijo,J.
  TITLE     Targeting IL-11 to reduce fibrocyte circulation and lung
            accumulation in animal models of pulmonary hypertension-associated
            lung fibrosis
  JOURNAL   Br J Pharmacol 181 (16), 2991-3009 (2024)
   PUBMED   38679415
  REMARK    GeneRIF: Targeting IL-11 to reduce fibrocyte circulation and lung
            accumulation in animal models of pulmonary hypertension-associated
            lung fibrosis.
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Guo,X., Zhu,X., Zhou,S. and Dong,X.
  TITLE     Serum levels of IL-9 and IL-11 serve as predictors for the
            occurrence of early neurologic deterioration in patients with
            cerebral infarction
  JOURNAL   Clin Chim Acta 558, 119683 (2024)
   PUBMED   38643817
  REMARK    GeneRIF: Serum levels of IL-9 and IL-11 serve as predictors for the
            occurrence of early neurologic deterioration in patients with
            cerebral infarction.
REFERENCE   6  (residues 1 to 199)
  AUTHORS   Wang,X.Y., Fuhrer,D.K., Marshall,M.S. and Yang,Y.C.
  TITLE     Interleukin-11 induces complex formation of Grb2, Fyn, and JAK2 in
            3T3L1 cells
  JOURNAL   J Biol Chem 270 (47), 27999-28002 (1995)
   PUBMED   7499280
REFERENCE   7  (residues 1 to 199)
  AUTHORS   Yang,Y.C. and Yin,T.
  TITLE     Interleukin-11 and its receptor
  JOURNAL   Biofactors 4 (1), 15-21 (1992)
   PUBMED   1292471
  REMARK    Review article
REFERENCE   8  (residues 1 to 199)
  AUTHORS   McKinley,D., Wu,Q., Yang-Feng,T. and Yang,Y.C.
  TITLE     Genomic sequence and chromosomal location of human interleukin-11
            gene (IL11)
  JOURNAL   Genomics 13 (3), 814-819 (1992)
   PUBMED   1386338
REFERENCE   9  (residues 1 to 199)
  AUTHORS   Kawashima,I., Ohsumi,J., Mita-Honjo,K., Shimoda-Takano,K.,
            Ishikawa,H., Sakakibara,S., Miyadai,K. and Takiguchi,Y.
  TITLE     Molecular cloning of cDNA encoding adipogenesis inhibitory factor
            and identity with interleukin-11
  JOURNAL   FEBS Lett 283 (2), 199-202 (1991)
   PUBMED   1828438
REFERENCE   10 (residues 1 to 199)
  AUTHORS   Paul,S.R., Bennett,F., Calvetti,J.A., Kelleher,K., Wood,C.R.,
            O'Hara,R.M. Jr., Leary,A.C., Sibley,B., Clark,S.C., Williams,D.A.
            et al.
  TITLE     Molecular cloning of a cDNA encoding interleukin 11, a stromal
            cell-derived lymphopoietic and hematopoietic cytokine
  JOURNAL   Proc Natl Acad Sci U S A 87 (19), 7512-7516 (1990)
   PUBMED   2145578
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK315294.1, AC020922.9 and
            BF055151.1.
            
            Summary: The protein encoded by this gene is a member of the gp130
            family of cytokines. These cytokines drive the assembly of
            multisubunit receptor complexes, all of which contain at least one
            molecule of the transmembrane signaling receptor IL6ST (gp130).
            This cytokine is shown to stimulate the T-cell-dependent
            development of immunoglobulin-producing B cells. It is also found
            to support the proliferation of hematopoietic stem cells and
            megakaryocyte progenitor cells. Alternatively spliced transcript
            variants encoding distinct isoforms have been found for this gene.
            [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (1) is the longer transcript and
            encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290572.1, X58377.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264563.7/ ENSP00000264563.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..199
                     /product="interleukin-11 isoform 1 precursor"
                     /note="adipogenesis inhibitory factor; oprelvekin"
                     /calculated_mol_wt=19144
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2303
     mat_peptide     22..199
                     /product="Interleukin-11. /id=PRO_0000015618"
                     /note="propagated from UniProtKB/Swiss-Prot (P20809.1)"
                     /calculated_mol_wt=19144
     Region          32..199
                     /region_name="IL11"
                     /note="Interleukin 11; pfam07400"
                     /db_xref="CDD:462155"
     Site            168
                     /site_type="other"
                     /note="Important for interaction with IL6ST and for the
                     stimulation of cell proliferation.
                     /evidence=ECO:0000250|UniProtKB:P47873; propagated from
                     UniProtKB/Swiss-Prot (P20809.1)"
     Region          182..190
                     /region_name="Important for interaction with IL11RA and
                     for the stimulation of cell proliferation.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P20809.1)"
     CDS             1..199
                     /gene="IL11"
                     /gene_synonym="AGIF; IL-11"
                     /coded_by="NM_000641.4:154..753"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12923.1"
                     /db_xref="GeneID:3589"
                     /db_xref="HGNC:HGNC:5966"
                     /db_xref="MIM:147681"
ORIGIN      
        1 mncvcrlvlv vlslwpdtav apgpppgppr vspdpraeld stvlltrsll adtrqlaaql
       61 rdkfpadgdh nldslptlam sagalgalql pgvltrlrad llsylrhvqw lrraggsslk
      121 tlepelgtlq arldrllrrl qllmsrlalp qpppdppapp lappssawgg iraahailgg
      181 lhltldwavr gllllktrl
//
LOCUS       NP_001357498             592 aa            linear   PRI 27-APR-2025
DEFINITION  semaphorin-4A isoform 4 [Homo sapiens].
ACCESSION   NP_001357498 XP_011508181
VERSION     NP_001357498.1
DBSOURCE    REFSEQ: accession NM_001370569.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Hou,T., Zhang,P., Tian,H., Luo,Y., Li,J., Zhang,K. and Li,Y.
  TITLE     Semaphorin 4A Maintains Trophoblastic Function via Activating the
            STAT3 Pathway
  JOURNAL   Biomolecules 14 (7), 826 (2024)
   PUBMED   39062540
  REMARK    GeneRIF: Semaphorin 4A Maintains Trophoblastic Function via
            Activating the STAT3 Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Naito,Y., Koyama,S., Masuhiro,K., Hirai,T., Uenami,T., Inoue,T.,
            Osa,A., Machiyama,H., Watanabe,G., Sax,N., Villa,J.,
            Kinugasa-Katayama,Y., Nojima,S., Yaga,M., Hosono,Y., Okuzaki,D.,
            Satoh,S., Tsuda,T., Nakanishi,Y., Suga,Y., Morita,T., Fukushima,K.,
            Nishide,M., Shiroyama,T., Miyake,K., Iwahori,K., Hirata,H.,
            Nagatomo,I., Yano,Y., Tamiya,M., Kumagai,T., Takemoto,N.,
            Inohara,H., Yamasaki,S., Yamashita,K., Aoshi,T., Akbay,E.A.,
            Hosen,N., Shintani,Y., Takamatsu,H., Mori,M., Takeda,Y. and
            Kumanogoh,A.
  TITLE     Tumor-derived semaphorin 4A improves PD-1-blocking antibody
            efficacy by enhancing CD8+ T cell cytotoxicity and proliferation
  JOURNAL   Sci Adv 9 (20), eade0718 (2023)
   PUBMED   37205755
  REMARK    GeneRIF: Tumor-derived semaphorin 4A improves PD-1-blocking
            antibody efficacy by enhancing CD8[+] T cell cytotoxicity and
            proliferation.
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Eiza,N., Garty,M., Staun-Ram,E., Miller,A. and Vadasz,Z.
  TITLE     The possible involvement of sema3A and sema4A in the pathogenesis
            of multiple sclerosis
  JOURNAL   Clin Immunol 238, 109017 (2022)
   PUBMED   35460904
  REMARK    GeneRIF: The possible involvement of sema3A and sema4A in the
            pathogenesis of multiple sclerosis.
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Chapoval,S.P., Lee,M., Lemmer,A., Ajayi,O., Qi,X., Neuwald,A.F. and
            Keegan,A.D.
  TITLE     Identifying Function Determining Residues in Neuroimmune Semaphorin
            4A
  JOURNAL   Int J Mol Sci 23 (6), 3024 (2022)
   PUBMED   35328445
  REMARK    GeneRIF: Identifying Function Determining Residues in Neuroimmune
            Semaphorin 4A.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Kumanogoh,A. and Kikutani,H.
  TITLE     Immune semaphorins: a new area of semaphorin research
  JOURNAL   J Cell Sci 116 (Pt 17), 3463-3470 (2003)
   PUBMED   12893810
  REMARK    Review article
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Kikutani,H. and Kumanogoh,A.
  TITLE     Semaphorins in interactions between T cells and antigen-presenting
            cells
  JOURNAL   Nat Rev Immunol 3 (2), 159-167 (2003)
   PUBMED   12563299
  REMARK    Review article
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Kumanogoh,A., Marukawa,S., Suzuki,K., Takegahara,N., Watanabe,C.,
            Ch'ng,E., Ishida,I., Fujimura,H., Sakoda,S., Yoshida,K. and
            Kikutani,H.
  TITLE     Class IV semaphorin Sema4A enhances T-cell activation and interacts
            with Tim-2
  JOURNAL   Nature 419 (6907), 629-633 (2002)
   PUBMED   12374982
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Puschel,A.W., Adams,R.H. and Betz,H.
  TITLE     Murine semaphorin D/collapsin is a member of a diverse gene family
            and creates domains inhibitory for axonal extension
  JOURNAL   Neuron 14 (5), 941-948 (1995)
   PUBMED   7748561
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            On May 10, 2019 this sequence version replaced XP_011508181.1.
            
            Summary: This gene encodes a member of the semaphorin family of
            soluble and transmembrane proteins. Semaphorins are involved in
            numerous functions, including axon guidance, morphogenesis,
            carcinogenesis, and immunomodulation. The encoded protein is a
            single-pass type I membrane protein containing an
            immunoglobulin-like C2-type domain, a PSI domain and a sema domain.
            It inhibits axonal extension by providing local signals to specify
            territories inaccessible for growing axons. It is an activator of
            T-cell-mediated immunity and suppresses vascular endothelial growth
            factor (VEGF)-mediated endothelial cell migration and proliferation
            in vitro and angiogenesis in vivo. Mutations in this gene are
            associated with retinal degenerative diseases including retinitis
            pigmentosa type 35 (RP35) and cone-rod dystrophy type 10 (CORD10).
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been identified.[provided by RefSeq, Sep
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.200780.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..592
                     /product="semaphorin-4A isoform 4"
                     /note="sema B; semaphorin-B; sema domain, immunoglobulin
                     domain (Ig), transmembrane domain (TM) and short
                     cytoplasmic domain, (semaphorin) 4A"
                     /calculated_mol_wt=64679
     Region          <1..326
                     /region_name="Sema"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorins and plexins; cl15693"
                     /db_xref="CDD:472829"
     Region          327..371
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          397..469
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          407..411
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          419..423
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          438..442
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          452..457
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..592
                     /gene="SEMA4A"
                     /gene_synonym="CORD10; RP35; SEMAB; SEMB"
                     /coded_by="NM_001370569.1:536..2314"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:64218"
                     /db_xref="HGNC:HGNC:10729"
                     /db_xref="MIM:607292"
ORIGIN      
        1 megkgqspfd pahkhtavlv dgmlysgtmn nflgsepilm rtlgsqpvlk tdnflrwlhh
       61 dasfvaaips tqvvyfffee tasefdffer lhtsrvarvc kndvggekll qkkwttflka
      121 qllctqpgql pfnvirhavl lpadsptaph iyavftsqwq vggtrssavc afslldierv
      181 fkgkykelnk etsrwttyrg petnprpgsc svgpssdkal tfmkdhflmd eqvvgtpllv
      241 ksgveytrla vetaqgldgh shlvmylgtt tgslhkavvs gdssahlvee iqlfpdpepv
      301 rnlqlaptqg avfvgfsggv wrvprancsv yescvdcvla rdphcawdpe srtccllsap
      361 nlnswkqdme rgnpewacas gpmsrslrpq srpqiikevl avpnsilelp cphlsalasy
      421 ywshgpaavp easstvyngs lllivqdgvg glyqcwaten gfsypvisyw vdsqdqtlal
      481 dpelagipre hvkvpltrvs ggaalaaqqs ywphfvtvtv lfalvlsgal iilvasplra
      541 lrargkvqgc etlrpgekap lsreqhlqsp kecrtsasdv dadnnclgte va
//
LOCUS       NP_001153655             126 aa            linear   PRI 27-APR-2025
DEFINITION  zinc finger protein 138 isoform 2 [Homo sapiens].
ACCESSION   NP_001153655
VERSION     NP_001153655.1
DBSOURCE    REFSEQ: accession NM_001160183.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073349.11.
            
            Transcript Variant: This variant (2) includes two alternate exons
            in the 3' coding region, which results in a frameshift, compared to
            variant 1. The resulting isoform (2) has a distinct and shorter
            C-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.227087.1,
                                           SRR1660805.170870.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..126
                     /product="zinc finger protein 138 isoform 2"
                     /note="zinc finger protein 138 (clone pHZ-32)"
                     /calculated_mol_wt=14450
     Region          4..57
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     CDS             1..126
                     /gene="ZNF138"
                     /gene_synonym="pHZ-32"
                     /coded_by="NM_001160183.3:142..522"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55115.1"
                     /db_xref="GeneID:7697"
                     /db_xref="HGNC:HGNC:12922"
                     /db_xref="MIM:604080"
ORIGIN      
        1 mgpltfmdva iefsleewqc ldtaqrnvyr hvmlenyrnl vfldlitcle qgkepwnmkr
       61 hemvvakhsa vaftfdlsgl nilsfqsilp fvsalyvmgn rnqclqkhle arnkdlcvlv
      121 lpktfg
//
LOCUS       NP_079510                305 aa            linear   PRI 27-APR-2025
DEFINITION  superkiller complex protein 8 isoform a [Homo sapiens].
ACCESSION   NP_079510
VERSION     NP_079510.1
DBSOURCE    REFSEQ: accession NM_025234.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Kogel,A., Keidel,A., Bonneau,F., Schafer,I.B. and Conti,E.
  TITLE     The human SKI complex regulates channeling of ribosome-bound RNA to
            the exosome via an intrinsic gatekeeping mechanism
  JOURNAL   Mol Cell 82 (4), 756-769 (2022)
   PUBMED   35120588
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Zinoviev,A., Ayupov,R.K., Abaeva,I.S., Hellen,C.U.T. and
            Pestova,T.V.
  TITLE     Extraction of mRNA from Stalled Ribosomes by the Ski Complex
  JOURNAL   Mol Cell 77 (6), 1340-1349 (2020)
   PUBMED   32006463
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Muntean,A.G., Tan,J., Sitwala,K., Huang,Y., Bronstein,J.,
            Connelly,J.A., Basrur,V., Elenitoba-Johnson,K.S. and Hess,J.L.
  TITLE     The PAF complex synergizes with MLL fusion proteins at HOX loci to
            promote leukemogenesis
  JOURNAL   Cancer Cell 17 (6), 609-621 (2010)
   PUBMED   20541477
REFERENCE   7  (residues 1 to 305)
  AUTHORS   Kim,J., Guermah,M. and Roeder,R.G.
  TITLE     The human PAF1 complex acts in chromatin transcription elongation
            both independently and cooperatively with SII/TFIIS
  JOURNAL   Cell 140 (4), 491-503 (2010)
   PUBMED   20178742
REFERENCE   8  (residues 1 to 305)
  AUTHORS   Tegha-Dunghu,J., Neumann,B., Reber,S., Krause,R., Erfle,H.,
            Walter,T., Held,M., Rogers,P., Hupfeld,K., Ruppert,T., Ellenberg,J.
            and Gruss,O.J.
  TITLE     EML3 is a nuclear microtubule-binding protein required for the
            correct alignment of chromosomes in metaphase
  JOURNAL   J Cell Sci 121 (Pt 10), 1718-1726 (2008)
   PUBMED   18445686
REFERENCE   9  (residues 1 to 305)
  AUTHORS   Zhu,B., Mandal,S.S., Pham,A.D., Zheng,Y., Erdjument-Bromage,H.,
            Batra,S.K., Tempst,P. and Reinberg,D.
  TITLE     The human PAF complex coordinates transcription with events
            downstream of RNA synthesis
  JOURNAL   Genes Dev 19 (14), 1668-1673 (2005)
   PUBMED   16024656
REFERENCE   10 (residues 1 to 305)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI916225.1 and AK024754.1.
            
            Summary: WDR61 is a subunit of the human PAF and SKI complexes,
            which function in transcriptional regulation and are involved in
            events downstream of RNA synthesis, such as RNA surveillance (Zhu
            et al., 2005 [PubMed 16024656]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.418005.1,
                                           SRR3476690.953537.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267973.7/ ENSP00000267973.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..305
                     /product="superkiller complex protein 8 isoform a"
                     /note="recombination protein REC14; WD repeat-containing
                     protein 61; meiotic recombination REC14 protein homolog;
                     SKI8 homolog; SKI complex component SKI8; Ski complex
                     subunit Rec14; WD repeat domain 61; SKI8 subunit of
                     superkiller complex protein; superkiller complex protein
                     8"
                     /calculated_mol_wt=33450
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9GZS3.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in WD repeat-containing protein
                     61, N-terminally processed.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9GZS3.1)"
     Region          <6..302
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          14..57
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZS3.1)"
     Region          19..62
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          62..101
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZS3.1)"
     Region          68..105
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          104..143
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZS3.1)"
     Region          110..146
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          146..187
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZS3.1)"
     Region          152..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          188..227
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZS3.1)"
     Region          193..229
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          230..269
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZS3.1)"
     Region          236..271
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          272..305
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZS3.1)"
     CDS             1..305
                     /gene="SKIC8"
                     /gene_synonym="REC14; SKI8; WDR61"
                     /coded_by="NM_025234.3:88..1005"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10300.1"
                     /db_xref="GeneID:80349"
                     /db_xref="HGNC:HGNC:30300"
                     /db_xref="MIM:609540"
ORIGIN      
        1 mtnqygilfk qeqahddaiw svawgtnkke nsetvvtgsl ddlvkvwkwr derldlqwsl
       61 eghqlgvvsv dishtlpiaa sssldahirl wdlengkqik sidagpvdaw tlafspdsqy
      121 latgthvgkv nifgvesgkk eysldtrgkf ilsiayspdg kylasgaidg iinifdiatg
      181 kllhtlegha mpirsltfsp dsqllvtasd dgyikiydvq hanlagtlsg haswvlnvaf
      241 cpddthfvss ssdksvkvwd vgtrtcvhtf fdhqdqvwgv kyngngskiv svgddqeihi
      301 ydcpi
//
LOCUS       NP_848912                502 aa            linear   ROD 27-APR-2025
DEFINITION  fatty acyl-CoA reductase 2 isoform 2 [Mus musculus].
ACCESSION   NP_848912
VERSION     NP_848912.1
DBSOURCE    REFSEQ: accession NM_178797.4
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Schwartz,B., Levi,H., Menon,G., Maria,R., Upcher,A., Kotlovski,Y.,
            Oss-Ronen,L. and Cohen,I.
  TITLE     ZNF750 Regulates Skin Barrier Function by Driving Cornified
            Envelope and Lipid Processing Pathways
  JOURNAL   J Invest Dermatol 144 (2), 296-306 (2024)
   PUBMED   37660780
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Roy,T.A., Bubier,J.A., Dickson,P.E., Wilcox,T.D., Ndukum,J.,
            Clark,J.W., Sukoff Rizzo,S.J., Crabbe,J.C., Denegre,J.M.,
            Svenson,K.L., Braun,R.E., Kumar,V., Murray,S.A., White,J.K.,
            Philip,V.M. and Chesler,E.J.
  TITLE     Discovery and validation of genes driving drug-intake and related
            behavioral traits in mice
  JOURNAL   Genes Brain Behav 23 (1), e12875 (2024)
   PUBMED   38164795
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Otsuka,K., Sawai-Ogawa,M. and Kihara,A.
  TITLE     Formation of fatty alcohols-components of meibum lipids-by the
            fatty acyl-CoA reductase FAR2 is essential for dry eye prevention
  JOURNAL   FASEB J 36 (4), e22216 (2022)
   PUBMED   35238077
  REMARK    GeneRIF: Formation of fatty alcohols-components of meibum lipids-by
            the fatty acyl-CoA reductase FAR2 is essential for dry eye
            prevention.
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Sheehan,S., Mawe,S., Cianciolo,R.E., Korstanje,R. and Mahoney,J.M.
  TITLE     Detection and Classification of Novel Renal Histologic Phenotypes
            Using Deep Neural Networks
  JOURNAL   Am J Pathol 189 (9), 1786-1796 (2019)
   PUBMED   31220455
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Thompson,C.L., Ng,L., Menon,V., Martinez,S., Lee,C.K.,
            Glattfelder,K., Sunkin,S.M., Henry,A., Lau,C., Dang,C.,
            Garcia-Lopez,R., Martinez-Ferre,A., Pombero,A., Rubenstein,J.L.R.,
            Wakeman,W.B., Hohmann,J., Dee,N., Sodt,A.J., Young,R., Smith,K.,
            Nguyen,T.N., Kidney,J., Kuan,L., Jeromin,A., Kaykas,A., Miller,J.,
            Page,D., Orta,G., Bernard,A., Riley,Z., Smith,S., Wohnoutka,P.,
            Hawrylycz,M.J., Puelles,L. and Jones,A.R.
  TITLE     A high-resolution spatiotemporal atlas of gene expression of the
            developing mouse brain
  JOURNAL   Neuron 83 (2), 309-323 (2014)
   PUBMED   24952961
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Noordmans,G.A., Caputo,C.R., Huang,Y., Sheehan,S.M., Bulthuis,M.,
            Heeringa,P., Hillebrands,J.L., van Goor,H. and Korstanje,R.
  TITLE     Genetic analysis of mesangial matrix expansion in aging mice and
            identification of Far2 as a candidate gene
  JOURNAL   J Am Soc Nephrol 24 (12), 1995-2001 (2013)
   PUBMED   24009241
  REMARK    GeneRIF: Mouse strains with mesangial matrix expansion contain a
            9-bp sequence in the 5' untranslated region of Far2 that is absent
            in most of the strains without it.
REFERENCE   8  (residues 1 to 502)
  AUTHORS   Patel,S., Xi,Z.F., Seo,E.Y., McGaughey,D. and Segre,J.A.
  TITLE     Klf4 and corticosteroids activate an overlapping set of
            transcriptional targets to accelerate in utero epidermal barrier
            acquisition
  JOURNAL   Proc Natl Acad Sci U S A 103 (49), 18668-18673 (2006)
   PUBMED   17130451
REFERENCE   9  (residues 1 to 502)
  AUTHORS   Cheng,J.B. and Russell,D.W.
  TITLE     Mammalian wax biosynthesis. II. Expression cloning of wax synthase
            cDNAs encoding a member of the acyltransferase enzyme family
  JOURNAL   J Biol Chem 279 (36), 37798-37807 (2004)
   PUBMED   15220349
  REMARK    GeneRIF: wax monoester synthesis in mammals involves a two step
            biosynthetic pathway catalyzed by fatty acyl-CoA reductase and wax
            synthase enzymes
REFERENCE   10 (residues 1 to 502)
  AUTHORS   Cheng,J.B. and Russell,D.W.
  TITLE     Mammalian wax biosynthesis. I. Identification of two fatty
            acyl-Coenzyme A reductases with different substrate specificities
            and tissue distributions
  JOURNAL   J Biol Chem 279 (36), 37789-37797 (2004)
   PUBMED   15220348
  REMARK    GeneRIF: fatty alcohol synthesis in mammals is accomplished by two
            fatty acyl-CoA reductase isozymes that are expressed at high levels
            in tissues known to synthesize wax monoesters and ether lipids
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK043388.1 and AK043589.1.
            
            Transcript Variant: This variant (2) differs in the 3' coding
            region and 3' UTR, compared to variant 1. These differences cause a
            translation frameshift and result in an isoform (2) with a shorter
            and distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK043589.1, AK038584.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849378, SAMN01164131
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 78.49 cM"
     Protein         1..502
                     /product="fatty acyl-CoA reductase 2 isoform 2"
                     /EC_number="1.2.1.84"
                     /note="male sterility domain-containing protein 1"
                     /calculated_mol_wt=57509
     Region          11..315
                     /region_name="FAR-N_SDR_e"
                     /note="fatty acyl CoA reductases (FARs), extended (e)
                     SDRs; cd05236"
                     /db_xref="CDD:187547"
     Site            order(17,19..22,44..46,111..113,130,151..153,204,208,
                     229..232)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187547"
     Site            order(131,153,204,208)
                     /site_type="active"
                     /db_xref="CDD:187547"
     Site            order(153,204,231,243,259,265)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187547"
     Region          357..447
                     /region_name="Sterile"
                     /note="Male sterility protein; pfam03015"
                     /db_xref="CDD:460779"
     Site            465..484
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNT2.1)"
     CDS             1..502
                     /gene="Far2"
                     /gene_synonym="A230046P18; Mlstd1"
                     /coded_by="NM_178797.4:135..1643"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS39718.1"
                     /db_xref="GeneID:330450"
                     /db_xref="MGI:MGI:2687035"
ORIGIN      
        1 msmiaafysn ksilitgatg flgkvlmekl frtsphlkvi yilvrpksgq tlqervfqil
       61 nsklfekvke vcpnvhekir pisadlnqrd faiskedvqe llsctniifh caatvrfdah
      121 lreavqlnvt atqqlllmas qmpkleafih istafsncnl shideviypc pveprkiids
      181 mewlddsiie eitpkligdr pntytytkal geivvqqesg nlnvaivrps ivgatwqepf
      241 pgwvdnlngp sgliiatgkg flrsikatpm avadvipvdt vvnltiavgw ytavhrpkst
      301 liyhstsgnl npcnwykmgl qvlatiekip fesafrrpna dfttsnftth ywntvshrvp
      361 aiiydfylrl tgrkprmlkl mnrllktism leyfinhswe wstnntemll selspedqrv
      421 fnfdvrqlnw leyienyvlg vkkyllkedl agipkakqhl rrlrnihylf ntalfliiwr
      481 lliarsqmar nvwfficplf kl
//
LOCUS       NP_006691                582 aa            linear   PRI 27-APR-2025
DEFINITION  TRAF-type zinc finger domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_006691
VERSION     NP_006691.1
DBSOURCE    REFSEQ: accession NM_006700.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Gupta,S., Singh,P., Tasneem,A., Almatroudi,A., Rahmani,A.H.,
            Dohare,R. and Parveen,S.
  TITLE     Integrative Multiomics and Regulatory Network Analyses Uncovers the
            Role of OAS3, TRAFD1, miR-222-3p, and miR-125b-5p in Hepatitis E
            Virus Infection
  JOURNAL   Genes (Basel) 14 (1), 42 (2022)
   PUBMED   36672782
  REMARK    GeneRIF: Integrative Multiomics and Regulatory Network Analyses
            Uncovers the Role of OAS3, TRAFD1, miR-222-3p, and miR-125b-5p in
            Hepatitis E Virus Infection.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Kaltenbach,L.S., Romero,E., Becklin,R.R., Chettier,R., Bell,R.,
            Phansalkar,A., Strand,A., Torcassi,C., Savage,J., Hurlburt,A.,
            Cha,G.H., Ukani,L., Chepanoske,C.L., Zhen,Y., Sahasrabudhe,S.,
            Olson,J., Kurschner,C., Ellerby,L.M., Peltier,J.M., Botas,J. and
            Hughes,R.E.
  TITLE     Huntingtin interacting proteins are genetic modifiers of
            neurodegeneration
  JOURNAL   PLoS Genet 3 (5), e82 (2007)
   PUBMED   17500595
REFERENCE   7  (residues 1 to 582)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 582)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   9  (residues 1 to 582)
  AUTHORS   Mashima,R., Saeki,K., Aki,D., Minoda,Y., Takaki,H., Sanada,T.,
            Kobayashi,T., Aburatani,H., Yamanashi,Y. and Yoshimura,A.
  TITLE     FLN29, a novel interferon- and LPS-inducible gene acting as a
            negative regulator of toll-like receptor signaling
  JOURNAL   J Biol Chem 280 (50), 41289-41297 (2005)
   PUBMED   16221674
  REMARK    GeneRIF: FLN29 is a new negative feedback regulator of TLR
            signaling
REFERENCE   10 (residues 1 to 582)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK312601.1, BC003553.2 and CA314188.1.
            
            Summary: The innate immune system confers host defense against
            viral and microbial infection, and TRAFD1 is a negative feedback
            regulator that controls excessive immune responses (Sanada et al.,
            2008 [PubMed 18849341]).[supplied by OMIM, Dec 2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.46222.1,
                                           SRR3476690.536433.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000412615.7/ ENSP00000396526.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.13"
     Protein         1..582
                     /product="TRAF-type zinc finger domain-containing protein
                     1"
                     /note="FLN29 gene product"
                     /calculated_mol_wt=64710
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O14545.1)"
     Region          <7..131
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14545.1)"
     Region          217..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14545.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14545.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O14545.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O14545.1)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O14545.1)"
     Region          401..582
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14545.1)"
     Region          <406..543
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O14545.1)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O14545.1)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14545.1)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O14545.1)"
     CDS             1..582
                     /gene="TRAFD1"
                     /gene_synonym="FLN29"
                     /coded_by="NM_006700.3:72..1820"
                     /db_xref="CCDS:CCDS9160.1"
                     /db_xref="GeneID:10906"
                     /db_xref="HGNC:HGNC:24808"
                     /db_xref="MIM:613197"
ORIGIN      
        1 maeflddqet rlcdnckkei pvfnftihei hcqrnigmcp tckepfpksd methmaaehc
       61 qvtckcnkkl ekrllkkhee tecplrlavc qhcdlelsil klkehedycg artelcgncg
      121 rnvlvkdlkt hpevcgrege ekrnevaipp naydeswgqd giwiasqllr qiealdppmr
      181 lprrplrafe sdvfhnrttn qrnitaqvsi qnnlfeeqer qernrgqqpp keggeesanl
      241 dfmlalslqn egqassvaeq dfwravcead qshggprsls dikgaadeim lpcefceely
      301 peellidhqt scnpsralps lntgsssprg veepdvifqn flqqaasnql dslmglsnsh
      361 pveesiiipc efcgvqleee vlfhhqdqcd qrpatatnhv tegiprldsq pqetspelpr
      421 rrvrhqgdls sgylddtkqe tangptsclp psrpinnmta tynqlsrsts gprpgcqpss
      481 pcvpklsnsd sqdiqgrnrd sqngaiapgh vsvirppqnl ypenivpsfs pgpsgrygas
      541 grseggrnsr vtpaaanyrs rtakakpskq qgagdaeeee ee
//
LOCUS       NP_060405                785 aa            linear   PRI 27-APR-2025
DEFINITION  B-cell scaffold protein with ankyrin repeats isoform 1 [Homo
            sapiens].
ACCESSION   NP_060405
VERSION     NP_060405.5
DBSOURCE    REFSEQ: accession NM_017935.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Shu,Y., Ma,X., Chen,C., Wang,Y., Sun,X., Zhang,L., Lu,Z.,
            Petersen,F., Qiu,W. and Yu,X.
  TITLE     Myelin oligodendrocyte glycoprotein-associated disease is
            associated with BANK1, RNASET2 and TNIP1 polymorphisms
  JOURNAL   J Neuroimmunol 372, 577937 (2022)
   PUBMED   36054934
  REMARK    GeneRIF: Myelin oligodendrocyte glycoprotein-associated disease is
            associated with BANK1, RNASET2 and TNIP1 polymorphisms.
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Zhang,P., Zhai,J., Wang,K. and Wu,Y.
  TITLE     IKBKE and BANK1 Polymorphisms and Clinical Characteristics in
            Chinese Women with Systemic Lupus Erythematosus
  JOURNAL   Immunol Invest 51 (7), 2097-2107 (2022)
   PUBMED   35930382
  REMARK    GeneRIF: IKBKE and BANK1 Polymorphisms and Clinical Characteristics
            in Chinese Women with Systemic Lupus Erythematosus.
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Bolin,K., Imgenberg-Kreuz,J., Leonard,D., Sandling,J.K.,
            Alexsson,A., Pucholt,P., Haarhaus,M.L., Almlof,J.C., Nititham,J.,
            Jonsen,A., Sjowall,C., Bengtsson,A.A., Rantapaa-Dahlqvist,S.,
            Svenungsson,E., Gunnarsson,I., Syvanen,A.C., Lerang,K.,
            Troldborg,A., Voss,A., Molberg,O., Jacobsen,S., Criswell,L.,
            Ronnblom,L. and Nordmark,G.
  TITLE     Variants in BANK1 are associated with lupus nephritis of European
            ancestry
  JOURNAL   Genes Immun 22 (3), 194-202 (2021)
   PUBMED   34127828
  REMARK    GeneRIF: Variants in BANK1 are associated with lupus nephritis of
            European ancestry.
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Gomez Hernandez,G., Morell,M. and Alarcon-Riquelme,M.E.
  TITLE     The Role of BANK1 in B Cell Signaling and Disease
  JOURNAL   Cells 10 (5), 1184 (2021)
   PUBMED   34066164
  REMARK    GeneRIF: The Role of BANK1 in B Cell Signaling and Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 785)
  AUTHORS   Le Berre,L., Chesneau,M., Danger,R., Dubois,F., Chaussabel,D.,
            Garand,M. and Brouard,S.
  TITLE     Connection of BANK1, Tolerance, Regulatory B cells, and Apoptosis:
            Perspectives of a Reductionist Investigation
  JOURNAL   Front Immunol 12, 589786 (2021)
   PUBMED   33815360
  REMARK    GeneRIF: Connection of BANK1, Tolerance, Regulatory B cells, and
            Apoptosis: Perspectives of a Reductionist Investigation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 785)
  AUTHORS   Fung,E.Y., Smyth,D.J., Howson,J.M., Cooper,J.D., Walker,N.M.,
            Stevens,H., Wicker,L.S. and Todd,J.A.
  TITLE     Analysis of 17 autoimmune disease-associated variants in type 1
            diabetes identifies 6q23/TNFAIP3 as a susceptibility locus
  JOURNAL   Genes Immun 10 (2), 188-191 (2009)
   PUBMED   19110536
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 785)
  AUTHORS   Orozco,G., Abelson,A.K., Gonzalez-Gay,M.A., Balsa,A.,
            Pascual-Salcedo,D., Garcia,A., Fernandez-Gutierrez,B.,
            Petersson,I., Pons-Estel,B., Eimon,A., Paira,S., Scherbarth,H.R.,
            Alarcon-Riquelme,M. and Martin,J.
  TITLE     Study of functional variants of the BANK1 gene in rheumatoid
            arthritis
  JOURNAL   Arthritis Rheum 60 (2), 372-379 (2009)
   PUBMED   19180476
  REMARK    GeneRIF: These results suggest that BANK1 SNPs and haplotypes may
            contribute to rheumatoid arthritis susceptibility with a low risk.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 785)
  AUTHORS   Kozyrev,S.V., Abelson,A.K., Wojcik,J., Zaghlool,A., Linga
            Reddy,M.V., Sanchez,E., Gunnarsson,I., Svenungsson,E., Sturfelt,G.,
            Jonsen,A., Truedsson,L., Pons-Estel,B.A., Witte,T., D'Alfonso,S.,
            Barizzone,N., Danieli,M.G., Gutierrez,C., Suarez,A., Junker,P.,
            Laustrup,H., Gonzalez-Escribano,M.F., Martin,J., Abderrahim,H. and
            Alarcon-Riquelme,M.E.
  TITLE     Functional variants in the B-cell gene BANK1 are associated with
            systemic lupus erythematosus
  JOURNAL   Nat Genet 40 (2), 211-216 (2008)
   PUBMED   18204447
  REMARK    GeneRIF: Functional variants in the B-cell gene BANK1 are
            assoicated with systemic lupus erythematosus.
            GeneRIF: Genome-wide association study of gene-disease association.
            (HuGE Navigator)
            Erratum:[Nat Genet. 2008 Apr;40(4):484. Barrizzone, Nadia
            [corrected to Barizzone, Nadia]]
REFERENCE   9  (residues 1 to 785)
  AUTHORS   Yokoyama,K., Su Ih,I.H., Tezuka,T., Yasuda,T., Mikoshiba,K.,
            Tarakhovsky,A. and Yamamoto,T.
  TITLE     BANK regulates BCR-induced calcium mobilization by promoting
            tyrosine phosphorylation of IP(3) receptor
  JOURNAL   EMBO J 21 (1-2), 83-92 (2002)
   PUBMED   11782428
REFERENCE   10 (residues 1 to 785)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC109928.4, AP002075.3 and
            AC095062.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_060405.4.
            
            Summary: The protein encoded by this gene is a B-cell-specific
            scaffold protein that functions in B-cell receptor-induced calcium
            mobilization from intracellular stores. This protein can also
            promote Lyn-mediated tyrosine phosphorylation of inositol
            1,4,5-trisphosphate receptors. Polymorphisms in this gene are
            associated with susceptibility to systemic lupus erythematosus.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032241.1, SRR1660805.240231.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322953.9/ ENSP00000320509.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..785
                     /product="B-cell scaffold protein with ankyrin repeats
                     isoform 1"
                     /note="B-cell scaffold protein with ankyrin repeats"
                     /calculated_mol_wt=89151
     Region          1..154
                     /region_name="Interaction with ITPR2.
                     /evidence=ECO:0000269|PubMed:11782428"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDB2.3)"
     Region          28..154
                     /region_name="TIR_3"
                     /note="Toll/interleukin-1 receptor domain; pfam18567"
                     /db_xref="CDD:436583"
     Region          199..328
                     /region_name="DBB"
                     /note="Dof, BCAP, and BANK (DBB) motif; pfam14545"
                     /db_xref="CDD:464205"
     Region          342..371
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDB2.3)"
     Region          378..408
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDB2.3)"
     Region          433..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDB2.3)"
     Region          493..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDB2.3)"
     Region          538..578
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDB2.3)"
     Region          606..625
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDB2.3)"
     CDS             1..785
                     /gene="BANK1"
                     /gene_synonym="BANK"
                     /coded_by="NM_017935.5:152..2509"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34038.1"
                     /db_xref="GeneID:55024"
                     /db_xref="HGNC:HGNC:18233"
                     /db_xref="MIM:610292"
ORIGIN      
        1 mlpaapgkgl gspdpapcgp appgntkdii miyeedaeew alyltevflh vvkreailly
       61 rlenfsfrhl ellnltsykc kllilsnsll rdltpkkcqf lekilhspks vvtllcgvks
      121 sdqlyellni sqsrweiste qepedyisvi qsiifkdsed yfevniptdl rakhsgeise
      181 rkeieelsea srntiplavv lpteipcenp geifiilrde vigdtvevef tssnkrirtr
      241 palwnkkvwc mkalefpags vhvnvycdgi vkattkikyy ptakakeclf rmadsgeslc
      301 qnsieeldgv ltsifkheip yyefqslqte icsqnkythf kelptllhca akfglknlai
      361 hllqcsgatw askmknmegs dpahiaerhg hkelkkifed fsiqeidinn eqendyeedi
      421 asfstyipst qnpafhhesr ktygqsadga eanemegegk qngsgmetkh splevgsess
      481 edqyddlyvf ipgadpenns qeplmssrpp lppprpvana fqlerphftl pgtmvegqme
      541 rsqnwghpgv rqetgdepkg ekekkeeeke qeeeedpytf aeiddseydm ilanlsikkk
      601 tgsrsfiinr ppaptprpts ippkeettpy iaqvfqqkta rrqsdddkfc glpkkqdrar
      661 iespafstlr gcltdgqeel illqekvkng kmsmdealek fkhwqmgksg lemiqqeklr
      721 qlrdciigkr peeenvynkl tivhhpggke tahnenkfyn vhfsnklpar pqvekefgfc
      781 ckkdh
//
LOCUS       NP_006336                568 aa            linear   PRI 27-APR-2025
DEFINITION  proton-coupled zinc antiporter SLC30A9, mitochondrial [Homo
            sapiens].
ACCESSION   NP_006336
VERSION     NP_006336.3
DBSOURCE    REFSEQ: accession NM_006345.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Ge,J., Li,H., Liang,X. and Zhou,B.
  TITLE     SLC30A9: an evolutionarily conserved mitochondrial zinc transporter
            essential for mammalian early embryonic development
  JOURNAL   Cell Mol Life Sci 81 (1), 357 (2024)
   PUBMED   39158587
  REMARK    GeneRIF: SLC30A9: an evolutionarily conserved mitochondrial zinc
            transporter essential for mammalian early embryonic development.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Ding,M., Yu,Z., Lu,T., Hu,S., Zhou,X. and Wang,X.
  TITLE     N-acetyltransferase 10 facilitates tumorigenesis of diffuse large
            B-cell lymphoma by regulating AMPK/mTOR signalling through
            N4-acetylcytidine modification of SLC30A9
  JOURNAL   Clin Transl Med 14 (7), e1747 (2024)
   PUBMED   38961519
  REMARK    GeneRIF: N-acetyltransferase 10 facilitates tumorigenesis of
            diffuse large B-cell lymphoma by regulating AMPK/mTOR signalling
            through N4-acetylcytidine modification of SLC30A9.
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Steel,D.B.D., Danti,F.R., Abunada,M., Kamien,B., Malhotra,S.,
            Topf,M., Kaliakatsos,M., Valentine,J., Nemeth,A.H., Jayawant,S.,
            Reid,K.M., Mankad,K., Sudhakar,S., Ben-Pazi,H., Barwick,K. and
            Kurian,M.A.
  TITLE     Clinical Phenotype in Individuals With Birk-Landau-Perez Syndrome
            Associated With Biallelic SLC30A9 Pathogenic Variants
  JOURNAL   Neurology 100 (21), e2214-e2223 (2023)
   PUBMED   37041080
  REMARK    GeneRIF: Clinical Phenotype in Individuals With Birk-Landau-Perez
            Syndrome Associated With Biallelic SLC30A9 Pathogenic Variants.
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Kleyner,R., Arif,M., Marchi,E., Horowitz,N., Haworth,A., King,B.,
            Gavin,M., Amble,K., Velinov,M. and Lyon,G.J.
  TITLE     Autosomal recessive SLC30A9 variants in a proband with a
            cerebrorenal syndrome and no parental consanguinity
  JOURNAL   Cold Spring Harb Mol Case Stud 8 (2), a006137 (2022)
   PUBMED   34716203
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Wang,L., McDonnell,S.K., Hebbring,S.J., Cunningham,J.M., St
            Sauver,J., Cerhan,J.R., Isaya,G., Schaid,D.J. and Thibodeau,S.N.
  TITLE     Polymorphisms in mitochondrial genes and prostate cancer risk
  JOURNAL   Cancer Epidemiol Biomarkers Prev 17 (12), 3558-3566 (2008)
   PUBMED   19064571
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 568)
  AUTHORS   Overbeck,S., Uciechowski,P., Ackland,M.L., Ford,D. and Rink,L.
  TITLE     Intracellular zinc homeostasis in leukocyte subsets is regulated by
            different expression of zinc exporters ZnT-1 to ZnT-9
  JOURNAL   J Leukoc Biol 83 (2), 368-380 (2008)
   PUBMED   17971500
  REMARK    GeneRIF: hZnT-9 was expressed at low levels in leukocytes.
REFERENCE   8  (residues 1 to 568)
  AUTHORS   Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect
            of adaptor protein 3-depleted fibroblasts by promoting zinc
            accumulation in lysosomes
  JOURNAL   Exp Cell Res 313 (7), 1473-1483 (2007)
   PUBMED   17349999
REFERENCE   9  (residues 1 to 568)
  AUTHORS   Sim,D.L., Yeo,W.M. and Chow,V.T.
  TITLE     The novel human HUEL (C4orf1) protein shares homology with the
            DNA-binding domain of the XPA DNA repair protein and displays
            nuclear translocation in a cell cycle-dependent manner
  JOURNAL   Int J Biochem Cell Biol 34 (5), 487-504 (2002)
   PUBMED   11906820
  REMARK    GeneRIF: Results indicate that HUEL, which shares significant
            homology with the DNA-binding domain of XPA, is likely to be a
            conserved, housekeeping gene that is intimately linked with
            cellular replication, DNA synthesis and/or transcriptional
            regulation.
REFERENCE   10 (residues 1 to 568)
  AUTHORS   Sim,D.L. and Chow,V.T.
  TITLE     The novel human HUEL (C4orf1) gene maps to chromosome 4p12-p13 and
            encodes a nuclear protein containing the nuclear receptor
            interaction motif
  JOURNAL   Genomics 59 (2), 224-233 (1999)
   PUBMED   10409434
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG323207.1, BC007732.2, AY594282.1, BC022981.1, AA427879.1 and
            AC113151.5.
            
            On Jan 6, 2005 this sequence version replaced NP_006336.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.55113.1,
                                           SRR1803616.45714.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264451.12/ ENSP00000264451.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p13"
     Protein         1..568
                     /product="proton-coupled zinc antiporter SLC30A9,
                     mitochondrial"
                     /note="expressed in human embryonic lung; GRIP1-dependent
                     nuclear receptor coactivator; zinc transporter 9; znT-9;
                     human embryonic lung protein; solute carrier family 30
                     (zinc transporter), member 9"
                     /calculated_mol_wt=56091
     transit_peptide 1..67
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q6PML9.1)"
                     /calculated_mol_wt=7443
     mat_peptide     68..568
                     /product="Proton-coupled zinc antiporter SLC30A9,
                     mitochondrial. /id=PRO_0000295805"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PML9.1)"
                     /calculated_mol_wt=56091
     Region          127..215
                     /region_name="NTD_ZNT9"
                     /note="N-terminal domain found in zinc transporter 9
                     (ZNT9) and similar proteins; cd21078"
                     /db_xref="CDD:410964"
     Region          238..563
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PML9.1)"
     Site            314..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PML9.1)"
     Site            342..362
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PML9.1)"
     Site            392..412
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PML9.1)"
     Site            424..444
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PML9.1)"
     Region          462..466
                     /region_name="LXXLL motif.
                     /evidence=ECO:0000269|PubMed:10409434"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PML9.1)"
     CDS             1..568
                     /gene="SLC30A9"
                     /gene_synonym="BILAPES; C4orf1; GAC63; HUEL; ZNT9"
                     /coded_by="NM_006345.4:123..1829"
                     /db_xref="CCDS:CCDS3465.1"
                     /db_xref="GeneID:10463"
                     /db_xref="HGNC:HGNC:1329"
                     /db_xref="MIM:604604"
ORIGIN      
        1 mlpglaaaaa hrcswsslcr lrlrcraaac npsdrqewqn lvtfgsfsnm vpcshpyigt
       61 lsqvklystn vqkegqgsqt lrvekvpsfe taegigtelk aplkqeplqv rvkavlkkre
      121 ygskytqnnf itgvrainef clkssdleql rkirrrsphe dtesftvylr sdveakslev
      181 wgspealare kklrkeaeie yrerlfrnqk ilreyrdflg ntkprsrtas vffkgpgkvv
      241 mvaicingln cffkflawiy tgsasmfsea ihslsdtcnq gllalgisks vqtpdpshpy
      301 gfsnmryiss lisgvgifmm gaglswyhgv mgllhpqpie sllwaycila gslvsegatl
      361 lvavnelrrn arakgmsfyk yvmesrdpst nvilledtaa vlgviiaatc mgltsitgnp
      421 lydslgslgv gtllgmvsaf liytnteall grsiqpeqvq rltellendp svraihdvka
      481 tdlglgkvrf kaevdfdgrv vtrsylekqd fdqmlqeiqe vktpeeletf mlkhgeniid
      541 tlgaevdrle kelkkrnpev rhvdleil
//
LOCUS       NP_001037506            1217 aa            linear   INV 27-APR-2025
DEFINITION  sericin 1 precursor [Bombyx mori].
ACCESSION   NP_001037506 NP_001037507 XP_004922239
VERSION     NP_001037506.2
DBSOURCE    REFSEQ: accession NM_001044041.2
KEYWORDS    RefSeq.
SOURCE      Bombyx mori (domestic silkworm)
  ORGANISM  Bombyx mori
            Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
            Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata;
            Ditrysia; Bombycoidea; Bombycidae; Bombycinae; Bombyx.
REFERENCE   1  (residues 1 to 1217)
  AUTHORS   Cheng,T., Zhang,X., Peng,Z., Fan,Y., Zhang,L. and Liu,C.
  TITLE     Effects of Osiris9a on Silk Properties in Bombyx mori Determined by
            Transgenic Overexpression
  JOURNAL   Int J Mol Sci 21 (5), 1888 (2020)
   PUBMED   32164252
  REMARK    GeneRIF: Effects of Osiris9a on Silk Properties in Bombyx mori
            Determined by Transgenic Overexpression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1217)
  AUTHORS   Liu,R., Qu,D., Ma,J., Luo,Q., Ou,Y., Tan,T., Zeng,W. and Xu,H.
  TITLE     Insights into regulatory characteristics of the promoters of
            Sericin 1 and Sericin 3 in transgenic silkworms
  JOURNAL   Biochem Biophys Res Commun 522 (2), 492-498 (2020)
   PUBMED   31780262
  REMARK    GeneRIF: Insights into regulatory characteristics of the promoters
            of Sericin 1 and Sericin 3 in transgenic silkworms.
REFERENCE   3  (residues 1 to 1217)
  AUTHORS   Qian,P., Wang,X., Li,J., Jiang,T., Tang,X., Huixiang,G. and Shen,X.
  TITLE     Bmo-miR-2780a regulates the expression of the sericin-1 gene of
            Bombyx mori
  JOURNAL   Arch Insect Biochem Physiol 103 (2), e21627 (2020)
   PUBMED   31701579
  REMARK    GeneRIF: The target gene (Ser-1) was significantly decreased by
            miR-2780a compared with the control group (p < .05), thus
            indicating that bmo-miR-2780a might negatively regulate the
            expression of Ser-1.
REFERENCE   4  (residues 1 to 1217)
  AUTHORS   Huang,K., Li,C.F., Wu,J., Wei,J.H., Zou,Y., Han,M.J. and Zhou,Z.Y.
  TITLE     Enhancer activity of Helitron in sericin-1 gene promoter from
            Bombyx mori
  JOURNAL   Insect Sci 23 (3), 396-405 (2016)
   PUBMED   27067405
  REMARK    GeneRIF: Bmhel-8 in the sericin-1 promoter exhibits enhancer
            activity. Bmhel-8 displays enhancer activity in a sericin-1
            promoter-driven gene expression system but does not regulate the
            tissue-specific expression of sericin-1.
REFERENCE   5  (residues 1 to 1217)
  AUTHORS   Tsubota,T., Tomita,S., Uchino,K., Kimoto,M., Takiya,S.,
            Kajiwara,H., Yamazaki,T. and Sezutsu,H.
  TITLE     A Hox Gene, Antennapedia, Regulates Expression of Multiple Major
            Silk Protein Genes in the Silkworm Bombyx mori
  JOURNAL   J Biol Chem 291 (13), 7087-7096 (2016)
   PUBMED   26814126
  REMARK    GeneRIF: Antennapedia regulates expression of sericin-1, a major
            silk protein gene, in the silk gland.
REFERENCE   6  (residues 1 to 1217)
  AUTHORS   Takahashi,M., Tsujimoto,K., Yamada,H., Takagi,H. and Nakamori,S.
  TITLE     The silk protein, sericin, protects against cell death caused by
            acute serum deprivation in insect cell culture
  JOURNAL   Biotechnol Lett 25 (21), 1805-1809 (2003)
   PUBMED   14677702
REFERENCE   7  (residues 1 to 1217)
  AUTHORS   Zhang,Y.Q.
  TITLE     Applications of natural silk protein sericin in biomaterials
  JOURNAL   Biotechnol Adv 20 (2), 91-100 (2002)
   PUBMED   14538058
REFERENCE   8  (residues 1 to 1217)
  AUTHORS   Garel,A., Deleage,G. and Prudhomme,J.C.
  TITLE     Structure and organization of the Bombyx mori sericin 1 gene and of
            the sericins 1 deduced from the sequence of the Ser 1B cDNA
  JOURNAL   Insect Biochem Mol Biol 27 (5), 469-477 (1997)
   PUBMED   9219370
REFERENCE   9  (residues 1 to 1217)
  AUTHORS   Michaille,J.J., Couble,P., Prudhomme,J.C. and Garel,A.
  TITLE     A single gene produces multiple sericin messenger RNAs in the silk
            gland of Bombyx mori
  JOURNAL   Biochimie 68 (10-11), 1165-1173 (1986)
   PUBMED   3024742
REFERENCE   10 (residues 1 to 1217)
  AUTHORS   Okamoto,H., Ishikawa,E. and Suzuki,Y.
  TITLE     Structural analysis of sericin genes. Homologies with fibroin gene
            in the 5' flanking nucleotide sequences
  JOURNAL   J Biol Chem 257 (24), 15192-15199 (1982)
   PUBMED   6294094
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP028181.1.
            
            On or before Feb 22, 2019 this sequence version replaced
            XP_004922239.1, NP_001037506.1.
            
            Sequence Note: The genomic coordinates were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMD00506767, SAMD00506768
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1217
                     /organism="Bombyx mori"
                     /db_xref="taxon:7091"
                     /chromosome="11"
                     /map="11"
     Protein         1..1217
                     /product="sericin 1 precursor"
                     /note="sericin 1A; sericin 1A'; sericin 1B; silk gum
                     protein"
                     /calculated_mol_wt=121204
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2024
     Region          <127..452
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     CDS             1..1217
                     /gene="LOC101740082"
                     /gene_synonym="ser1; sericin1B"
                     /coded_by="NM_001044041.2:55..3708"
                     /db_xref="GeneID:101740082"
ORIGIN      
        1 mrfvlcctli alaalsvkaf ghhpgnrdtv evknrkynaa ssessylnkd ndsisagahr
       61 aksveqsqdk skytsgpegv sysgrsqnyk dskqayadyh sdpnggsasa gqsrdsslre
      121 rnvhyvsdge avaassdard enrsaqqnaq anwnadgsyg vsadrsgsas srrrqanyys
      181 dkditaaskd dsradssrrs nayynrdsdg sesaglsdrr assskndnvf vyrtkdsigg
      241 qakssrsshs qesdayynss pdgsynagtr dssisnkkka sstiyadkdq iraandryss
      301 kqlkqssaqi ssgpegtsvs skdrqysndk rsksdayvgr dgtvaysnkd sektsrqsnt
      361 nyadqnsvrs dsaasdqtsn sydkgysdkn tvahssgsrg sqnqksssyr adkdgfssst
      421 nteksrfsss nsvvetsdgt sasressaed tkssnsnvqs detgeeeelf dvvsyqkied
      481 gkpviimkvi pveksasqss ssrssqesas yssssssstl sedssevdid lgnlgwwwns
      541 dnkaqraagg atkseassst qattvsgadd sadsytwwwn prrsssssss asssssgsnv
      601 ggssqssgss tsgsnarghl gtvsstgsts ntdsssksag srtsggssty gyssshrggs
      661 vsstgsssnt dsstknagss tsggsstygy ssshrggsvs stgsssntds stknagssts
      721 ggsstygyss shrggsvsst gsssntdsst ksagsstsgg sstygyssrh rggrvsstgs
      781 ssttdassns vgsstsggss tygyssnsrd gsvsstgsss ntdsnsnsag sstsggssty
      841 gyssnsrdgs vsstgsssnt dsnsnsagss tsggsstygy ssnsrdgsvs stgsssntda
      901 stdltgssts ggsstygyss dsrdgsvsst gsssntdast dlagsstsgg sstygyssdc
      961 gdgsvsstgs ssntdastdl agsstsggss tygyssnsrd gsvsstgsss ntdastdltg
     1021 sstsggssty gysssnrdgs vlatgsssnt dastteestt sagsstegys ssshdgsvts
     1081 tdgsstsgga ssssastaks daassedgfw wwnrrksgsg hksatvqsst tdktstdsas
     1141 stdstsstsg astttsgsss tsggsstsda sstsssvsrs hrsgvnrllh kpgqgkiclc
     1201 fenifdipyh lrknigv
//
LOCUS       NP_001162094             127 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase ZNRF1 isoform c [Mus musculus].
ACCESSION   NP_001162094
VERSION     NP_001162094.1
DBSOURCE    REFSEQ: accession NM_001168623.2
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Lin,Y.S., Chang,Y.C., Chao,T.L., Tsai,Y.M., Jhuang,S.J., Ho,Y.H.,
            Lai,T.Y., Liu,Y.L., Chen,C.Y., Tsai,C.Y., Hsueh,Y.P., Chang,S.Y.,
            Chuang,T.H., Lee,C.Y. and Hsu,L.C.
  TITLE     The Src-ZNRF1 axis controls TLR3 trafficking and interferon
            responses to limit lung barrier damage
  JOURNAL   J Exp Med 220 (8) (2023)
   PUBMED   37158982
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Lee,C.Y., Lai,T.Y., Tsai,M.K., Chang,Y.C., Ho,Y.H., Yu,I.S.,
            Yeh,T.W., Chou,C.C., Lin,Y.S., Lawrence,T. and Hsu,L.C.
  TITLE     The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and
            degradation to modulate inflammation
  JOURNAL   Nat Commun 8, 15502 (2017)
   PUBMED   28593998
  REMARK    GeneRIF: This study defines ZNRF1 as a regulator of TLR4-induced
            inflammatory responses and reveals another mechanism for the
            regulation of TLR4 signalling through CAV1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Ye,A., He,H. and Kim,J.
  TITLE     PEG3 binds to H19-ICR as a transcriptional repressor
  JOURNAL   Epigenetics 11 (12), 889-900 (2016)
   PUBMED   27824289
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Wakatsuki,S., Furuno,A., Ohshima,M. and Araki,T.
  TITLE     Oxidative stress-dependent phosphorylation activates ZNRF1 to
            induce neuronal/axonal degeneration
  JOURNAL   J Cell Biol 211 (4), 881-896 (2015)
   PUBMED   26572622
  REMARK    GeneRIF: up-regulation of ZNRF1 activity by oxidative stress leads
            to neuronal apoptosis and Wallerian degeneration.
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Wiese,C.B., Ireland,S., Fleming,N.L., Yu,J., Valerius,M.T.,
            Georgas,K., Chiu,H.S., Brennan,J., Armstrong,J., Little,M.H.,
            McMahon,A.P. and Southard-Smith,E.M.
  TITLE     A genome-wide screen to identify transcription factors expressed in
            pelvic Ganglia of the lower urinary tract
  JOURNAL   Front Neurosci 6, 130 (2012)
   PUBMED   22988430
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Wakatsuki,S., Saitoh,F. and Araki,T.
  TITLE     ZNRF1 promotes Wallerian degeneration by degrading AKT to induce
            GSK3B-dependent CRMP2 phosphorylation
  JOURNAL   Nat Cell Biol 13 (12), 1415-1423 (2011)
   PUBMED   22057101
  REMARK    GeneRIF: The ZNRF1-AKT-GSK3B-CRMP2 pathway plays an important role
            in controlling Wallerian degeneration.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Araki,T. and Milbrandt,J.
  TITLE     ZNRF proteins constitute a family of presynaptic E3 ubiquitin
            ligases
  JOURNAL   J Neurosci 23 (28), 9385-9394 (2003)
   PUBMED   14561866
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Araki,T., Nagarajan,R. and Milbrandt,J.
  TITLE     Identification of genes induced in peripheral nerve after injury.
            Expression profiling and novel gene discovery
  JOURNAL   J Biol Chem 276 (36), 34131-34141 (2001)
   PUBMED   11427537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC127356.4 and AC122364.4.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (c)
            has a shorter and distinct N-terminus compared to isoform a.
            Variants 4 and 6 both encode the same isoform (c).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849383,
                              SAMN00849384 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 57.98 cM"
     Protein         1..127
                     /product="E3 ubiquitin-protein ligase ZNRF1 isoform c"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 42; zinc ring finger protein 1;
                     E3 ubiquitin-protein ligase ZNRF1; peripheral nerve injury
                     protein nin283; zinc/RING finger protein 1; nerve
                     injury-induced gene 283 protein; RING-type E3 ubiquitin
                     transferase ZNRF1"
                     /calculated_mol_wt=14181
     Region          72..127
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(84,87,102,104,107,110,121,124)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438356"
     CDS             1..127
                     /gene="Znrf1"
                     /gene_synonym="B830022L21Rik; nin283; Rnf42; Zrfp1"
                     /coded_by="NM_001168623.2:1..384"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS52674.1"
                     /db_xref="GeneID:170737"
                     /db_xref="MGI:MGI:2177308"
ORIGIN      
        1 memnsfcall vtgqekaggg fprpwlvvgq qrpgrdfyrk tgfkcpicsk svasdememh
       61 fimclskprl synddvltkd agecviclee llqgdtiarl pclciyhksc idswfevnrs
      121 cpehpad
//
LOCUS       NP_003103                784 aa            linear   PRI 27-APR-2025
DEFINITION  transcription factor Sp4 isoform 1 [Homo sapiens].
ACCESSION   NP_003103
VERSION     NP_003103.2
DBSOURCE    REFSEQ: accession NM_003112.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Wei,L., Deng,C., Zhang,B., Wang,G., Meng,Y. and Qin,H.
  TITLE     SP4 Facilitates Esophageal Squamous Cell Carcinoma Progression by
            Activating PHF14 Transcription and Wnt/Beta-Catenin Signaling
  JOURNAL   Mol Cancer Res 22 (1), 55-69 (2024)
   PUBMED   37768180
  REMARK    GeneRIF: SP4 Facilitates Esophageal Squamous Cell Carcinoma
            Progression by Activating PHF14 Transcription and Wnt/Beta-Catenin
            Signaling.
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Dai,X., Luo,S., Guo,S., Zhou,W. and Song,W.
  TITLE     Sp4 Regulates PTTG1IP Gene Transcription and Expression
  JOURNAL   DNA Cell Biol 41 (12), 1053-1062 (2022)
   PUBMED   36383136
  REMARK    GeneRIF: Sp4 Regulates PTTG1IP Gene Transcription and Expression.
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Zhang,Q., Huo,J.H., Guo,L., Wang,L., Wang,C. and Li,M.
  TITLE     Common and rare variants within SP4 exert distinct molecular
            mechanisms contributing to the risk of schizophrenia
  JOURNAL   Psychiatry Res 318, 114948 (2022)
   PUBMED   36372009
  REMARK    GeneRIF: Common and rare variants within SP4 exert distinct
            molecular mechanisms contributing to the risk of schizophrenia.
REFERENCE   4  (residues 1 to 784)
  AUTHORS   Cui,Y., Wang,W., Luo,P., Feng,Y., Mi,C. and Jia,A.
  TITLE     The genetic polymorphisms in the SP4 gene and the risk of gastric
            cancer
  JOURNAL   Future Oncol 18 (36), 3993-4004 (2022)
   PUBMED   36346067
  REMARK    GeneRIF: The genetic polymorphisms in the SP4 gene and the risk of
            gastric cancer.
REFERENCE   5  (residues 1 to 784)
  AUTHORS   Gu,T., Pan,H., Zhang,F., Wang,L. and Cheng,Z.
  TITLE     The FOXP4-AS1/miR-3130-3p/SP4 feedback loop is associated with
            prostate cancer
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 68 (10), 161-166 (2022)
   PUBMED   37114256
  REMARK    GeneRIF: The FOXP4-AS1/miR-3130-3p/SP4 feedback loop is associated
            with prostate cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 784)
  AUTHORS   Suske,G.
  TITLE     The Sp-family of transcription factors
  JOURNAL   Gene 238 (2), 291-300 (1999)
   PUBMED   10570957
  REMARK    Review article
REFERENCE   7  (residues 1 to 784)
  AUTHORS   Hagen,G., Dennig,J., Preiss,A., Beato,M. and Suske,G.
  TITLE     Functional analyses of the transcription factor Sp4 reveal
            properties distinct from Sp1 and Sp3
  JOURNAL   J Biol Chem 270 (42), 24989-24994 (1995)
   PUBMED   7559627
REFERENCE   8  (residues 1 to 784)
  AUTHORS   Kalff-Suske,M., Kunz,J., Grzeschik,K.H. and Suske,G.
  TITLE     Human Sp4 transcription factor gene (SP4) maps to chromosome 7p15
  JOURNAL   Genomics 26 (3), 631-633 (1995)
   PUBMED   7607696
REFERENCE   9  (residues 1 to 784)
  AUTHORS   Majello,B., De Luca,P., Hagen,G., Suske,G. and Lania,L.
  TITLE     Different members of the Sp1 multigene family exert opposite
            transcriptional regulation of the long terminal repeat of HIV-1
  JOURNAL   Nucleic Acids Res 22 (23), 4914-4921 (1994)
   PUBMED   7800480
REFERENCE   10 (residues 1 to 784)
  AUTHORS   Hagen,G., Muller,S., Beato,M. and Suske,G.
  TITLE     Cloning by recognition site screening of two novel GT box binding
            proteins: a family of Sp1 related genes
  JOURNAL   Nucleic Acids Res 20 (21), 5519-5525 (1992)
   PUBMED   1454515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK289728.1, AC004595.1 and
            BF438799.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 8, 2005 this sequence version replaced NP_003103.1.
            
            Summary: The protein encoded by this gene is a transcription factor
            that can bind to the GC promoter region of a variety of genes,
            including those of the photoreceptor signal transduction system.
            The encoded protein binds to the same sites in promoter CpG islands
            as does the transcription factor SP1, although its expression is
            much more restricted compared to that of SP1. This gene may be
            involved in bipolar disorder and schizophrenia. [provided by
            RefSeq, May 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.151414.1,
                                           SRR1660803.26530.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222584.8/ ENSP00000222584.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.3"
     Protein         1..784
                     /product="transcription factor Sp4 isoform 1"
                     /calculated_mol_wt=81854
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02446.2)"
     Region          32..648
                     /region_name="SP4_N"
                     /note="N-terminal domain of transcription factor
                     Specificity Protein (SP) 4; cd22536"
                     /db_xref="CDD:411773"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q02446.2)"
     Region          109..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02446.2)"
     Region          281..390
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02446.2)"
     Region          467..475
                     /region_name="9aaTAD, inactive.
                     /evidence=ECO:0000269|PubMed:31375868"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02446.2)"
     Region          647..671
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          649..671
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(656,658,660,662..663,666..667,670,686,688,692..693,
                     696..697,700,714,716,718,720..721,724..725,728)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          677..701
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          679..701
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          693..716
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          707..729
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          709..729
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..784
                     /gene="SP4"
                     /gene_synonym="HF1B; SPR-1"
                     /coded_by="NM_003112.5:170..2524"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5373.1"
                     /db_xref="GeneID:6671"
                     /db_xref="HGNC:HGNC:11209"
                     /db_xref="MIM:600540"
ORIGIN      
        1 msdqkkeeee eaaaaaamat eggktsepen nnkkpktsgs qdsqpsplal laatcskigt
       61 pgenqatgqq qiiidpsqgl vqlqnqpqql elvttqlagn awqlvastpp askennvsqp
      121 asssssssss nngsasptkt ksgnsstpgq fqviqvqnps gsvqyqvipq lqtvegqqiq
      181 inptsssslq dlqgqiqlis agnnqailta anrtasgnil aqnlanqtvp vqirpgvsip
      241 lqlqtlpgtq aqvvttlpin iggvtlalpv innvaagggt gqvgqpaata dsgtsngnql
      301 vstptnttts astmpespss sttctttast sltssdtlvs sadtgqyast sasssertie
      361 esqtpaates eaqsssqlqp ngmqnaqdqs nslqqvqivg qpilqqiqiq qpqqqiiqai
      421 ppqsfqlqsg qtiqtiqqqp lqnvqlqavn ptqvlirapt ltpsgqiswq tvqvqniqsl
      481 snlqvqnagl sqqltitpvs ssggttlaqi apvavagapi tlntaqlasv pnlqtvsvan
      541 lgaagvqvqg vpvtitsvag qqqgqdgvkv qqatiapvtv avggianati gavspdqltq
      601 vhlqqgqqts dqevqpgkrl rrvacscpnc regegrgsne pgkkkqhich iegcgkvygk
      661 tshlrahlrw htgerpficn wmfcgkrftr sdelqrhrrt htgekrfecp ecskrfmrsd
      721 hlskhvkthq nkkgggtala ivtsgeldss vtevlgspri vtvaaisqds npatpnvstn
      781 meef
//
LOCUS       NP_002527                688 aa            linear   PRI 27-APR-2025
DEFINITION  TBC1 domain family member 25 isoform c [Homo sapiens].
ACCESSION   NP_002527
VERSION     NP_002527.1
DBSOURCE    REFSEQ: accession NM_002536.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Roy,M., Stephens,E., Bouhour,S. and Roux,S.
  TITLE     RabGAP TBC1D25 is involved in human osteoclast activity
  JOURNAL   Eur J Cell Biol 100 (3), 151145 (2021)
   PUBMED   33353759
  REMARK    GeneRIF: RabGAP TBC1D25 is involved in human osteoclast activity.
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Panarella,A., Bexiga,M.G., Galea,G., O' Neill,E.D., Salvati,A.,
            Dawson,K.A. and Simpson,J.C.
  TITLE     A systematic High-Content Screening microscopy approach reveals key
            roles for Rab33b, OATL1 and Myo6 in nanoparticle trafficking in
            HeLa cells
  JOURNAL   Sci Rep 6, 28865 (2016)
   PUBMED   27374232
  REMARK    GeneRIF: Rab33b, OATL1 and Myo6 have roles in nanoparticle
            trafficking in HeLa cells
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Tian,H., Liu,X., Zhang,B., Sun,Q. and Sun,D.
  TITLE     Adenovirus-mediated expression of both antisense ornithine
            decarboxylase and S-adenosylmethionine decarboxylase inhibits lung
            cancer cell growth
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 39 (6), 423-430 (2007)
   PUBMED   17558447
  REMARK    GeneRIF: Our study showed that adenovirus-mediated antisense ODC
            and expression inhibits tumor cell growth through blocking the
            polyamine synthesis pathway.
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Bernards,A.
  TITLE     GAPs galore! A survey of putative Ras superfamily GTPase activating
            proteins in man and Drosophila
  JOURNAL   Biochim Biophys Acta 1603 (2), 47-82 (2003)
   PUBMED   12618308
  REMARK    Review article
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Chang,L.S., Lin,S.Y., Lieu,A.S. and Wu,T.L.
  TITLE     Differential expression of human 5S snoRNA genes
  JOURNAL   Biochem Biophys Res Commun 299 (2), 196-200 (2002)
   PUBMED   12437969
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Geraghty,M.T., Brody,L.C., Martin,L.S., Marble,M., Kearns,W.,
            Pearson,P., Monaco,A.P., Lehrach,H. and Valle,D.
  TITLE     The isolation of cDNAs from OATL1 at Xp 11.2 using a 480-kb YAC
  JOURNAL   Genomics 16 (2), 440-446 (1993)
   PUBMED   8314581
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY154299.1, BC101817.1,
            AF196969.3, AC115618.3 and BU630180.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein with a TBC domain and
            functions as a Rab GTPase activating protein. The encoded protein
            is involved in the fusion of autophagosomes with endosomes and
            lysosomes. This gene was previously known as ornithine
            aminotransferase-like 1, but has no similarity to ornithine
            aminotransferase. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice junction compared to variant 1. The resulting isoform (c)
            has the same N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.156985.1,
                                           SRR1803615.174231.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376771.9/ ENSP00000365962.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..688
                     /product="TBC1 domain family member 25 isoform c"
                     /note="ornithine aminotransferase-like 1; 5SN3 snoRNA"
                     /calculated_mol_wt=76196
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MII6.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A1A5B6; propagated from
                     UniProtKB/Swiss-Prot (Q3MII6.2)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:A1A5B6; propagated from
                     UniProtKB/Swiss-Prot (Q3MII6.2)"
     Region          225..454
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            506
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q3MII6.2)"
     Region          544..606
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MII6.2)"
     CDS             1..688
                     /gene="TBC1D25"
                     /gene_synonym="MG81; OATL1"
                     /coded_by="NM_002536.4:85..2151"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS35242.1"
                     /db_xref="GeneID:4943"
                     /db_xref="HGNC:HGNC:8092"
                     /db_xref="MIM:311240"
ORIGIN      
        1 matasgasdl sgsgapppgv gaqaaaaaee eerevvrvrv kkcesflppe frsfavdpqi
       61 tsldvlqhil irafdlsgkk nfgisylgrd rlgqevylsl lsdwdlstaf ataskpylql
      121 rvdirpseds plledwdiis pkdvigsdvl laekrssltt aalpftqsil tqvgrtlskv
      181 qqvlswsyge dvkpfkppls daefhtylnh egqlsrpeel rlriyhggve pslrkvvwry
      241 llnvypdglt grermdymkr ksreyeqlks ewaqranped lefirstvlk dvlrtdrahp
      301 yyagpedgph lralhdlltt yavthpqvsy cqgmsdlasp ilavmdhegh afvcfcgimk
      361 rlaanfhpdg ramatkfahl klllrhadpd fyqylqeaga ddlffcyrwl llelkrefaf
      421 ddalrmlevt wsslppdppe hevelvgpps qvadagfggh rgwpvrqrhm lrpaggggst
      481 fedavdhlat asqgpggggr llrqasldgl qqlrdnmgsr rdplvqlphp aalissksls
      541 epllnspdpl lssfshpdsp ssssppstqe asptgdmavg splmqevgsp kdpgkslppv
      601 ppmglpppqe fgrgnpfmlf lclaillehr dhimrngldy nelamhfdrl vrkhhlgrvl
      661 rraralfady lqsevwdsee gaeataas
//
LOCUS       NP_005643                542 aa            linear   PRI 27-APR-2025
DEFINITION  telomeric repeat-binding factor 2 [Homo sapiens].
ACCESSION   NP_005643
VERSION     NP_005643.2
DBSOURCE    REFSEQ: accession NM_005652.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Liang,F., Rai,R., Sodeinde,T. and Chang,S.
  TITLE     TRF2-RAP1 represses RAD51-dependent homology-directed telomere
            repair by promoting BLM-mediated D-loop unwinding and inhibiting
            BLM-DNA2-dependent 5'-end resection
  JOURNAL   Nucleic Acids Res 52 (16), 9695-9709 (2024)
   PUBMED   39082275
  REMARK    GeneRIF: TRF2-RAP1 represses RAD51-dependent homology-directed
            telomere repair by promoting BLM-mediated D-loop unwinding and
            inhibiting BLM-DNA2-dependent 5'-end resection.
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Khayat,F., Alshmery,M., Pal,M., Oliver,A.W. and Bianchi,A.
  TITLE     Binding of the TRF2 iDDR motif to RAD50 highlights a convergent
            evolutionary strategy to inactivate MRN at telomeres
  JOURNAL   Nucleic Acids Res 52 (13), 7704-7719 (2024)
   PUBMED   38884214
  REMARK    GeneRIF: Binding of the TRF2 iDDR motif to RAD50 highlights a
            convergent evolutionary strategy to inactivate MRN at telomeres.
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Jiang,Y., Xu,J., Zeng,H., Lin,Z., Yi,Q., Guo,J. and Xiao,F.
  TITLE     miR-29b-1-5p exacerbates myocardial injury induced by sepsis in a
            mouse model by targeting TERF2
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 56 (4), 607-620 (2024)
   PUBMED   38414350
  REMARK    GeneRIF: miR-29b-1-5p exacerbates myocardial injury induced by
            sepsis in a mouse model by targeting TERF2.
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Xu,G.F., Zeng,Z., Zhang,Z.B., Zhang,X.M., Wang,M., Xiao,Q., Li,J.,
            Xie,X.Q., He,S., Fu,H.H., Liu,Y., Yang,Z.L., Chen,Y., Shi,J.,
            Wang,B., Qiu,H.Y., Zhou,Q., Liu,Y. and Chen,S.N.
  TITLE     The novel TERF2::PDGFRB fusion gene enhances tumorigenesis via
            PDGFRB/STAT5 signalling pathways and sensitivity to TKI in ph-like
            ALL
  JOURNAL   J Cell Mol Med 28 (3), e18114 (2024)
   PUBMED   38323741
  REMARK    GeneRIF: The novel TERF2::PDGFRB fusion gene enhances tumorigenesis
            via PDGFRB/STAT5 signalling pathways and sensitivity to TKI in
            ph-like ALL.
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Wong,S.Y., Soman,A., Korolev,N., Surya,W., Chen,Q., Shum,W., van
            Noort,J. and Nordenskiold,L.
  TITLE     The shelterin component TRF2 mediates columnar stacking of human
            telomeric chromatin
  JOURNAL   EMBO J 43 (1), 87-111 (2024)
   PUBMED   38177309
  REMARK    GeneRIF: The shelterin component TRF2 mediates columnar stacking of
            human telomeric chromatin.
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Sakaguchi,A.Y., Padalecki,S.S., Mattern,V., Rodriguez,A.,
            Leach,R.J., McGill,J.R., Chavez,M. and Giambernardi,T.A.
  TITLE     Chromosomal sublocalization of the transcribed human telomere
            repeat binding factor 2 gene and comparative mapping in the mouse
  JOURNAL   Somat Cell Mol Genet 24 (3), 157-163 (1998)
   PUBMED   10226653
REFERENCE   7  (residues 1 to 542)
  AUTHORS   van Steensel,B., Smogorzewska,A. and de Lange,T.
  TITLE     TRF2 protects human telomeres from end-to-end fusions
  JOURNAL   Cell 92 (3), 401-413 (1998)
   PUBMED   9476899
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Bilaud,T., Brun,C., Ancelin,K., Koering,C.E., Laroche,T. and
            Gilson,E.
  TITLE     Telomeric localization of TRF2, a novel human telobox protein
  JOURNAL   Nat Genet 17 (2), 236-239 (1997)
   PUBMED   9326951
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Broccoli,D., Smogorzewska,A., Chong,L. and de Lange,T.
  TITLE     Human telomeres contain two distinct Myb-related proteins, TRF1 and
            TRF2
  JOURNAL   Nat Genet 17 (2), 231-235 (1997)
   PUBMED   9326950
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026464.7, HY046320.1,
            AF002999.1, CB216181.1 and BX090758.1.
            
            On Dec 13, 2012 this sequence version replaced NP_005643.1.
            
            Summary: This gene encodes a telomere specific protein, TERF2,
            which is a component of the telomere nucleoprotein complex. This
            protein is present at telomeres in metaphase of the cell cycle, is
            a second negative regulator of telomere length and plays a key role
            in the protective activity of telomeres. While having similar
            telomere binding activity and domain organization, TERF2 differs
            from TERF1 in that its N terminus is basic rather than acidic.
            [provided by RefSeq, Jul 2008].
            
            CCDS Note: The coding region has been updated to extend the
            N-terminus to one that is more supported by the available
            transcript and conservation data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF002999.1, SRR1803611.49458.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254942.8/ ENSP00000254942.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..542
                     /product="telomeric repeat-binding factor 2"
                     /note="telomeric repeat binding protein 2; telomeric
                     DNA-binding protein; TTAGGG repeat-binding factor 2"
                     /calculated_mol_wt=59463
     Region          1..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15554.3)"
     Site            59
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:19596784; propagated from
                     UniProtKB/Swiss-Prot (Q15554.3)"
     Site            60
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000269|PubMed:19596784; propagated from
                     UniProtKB/Swiss-Prot (Q15554.3)"
     Region          84..287
                     /region_name="TRFH dimerization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15554.3)"
     Region          87..286
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cd00280"
                     /db_xref="CDD:238174"
     Site            order(126,129,143,147,151,161..165,173,176..177,180)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ATM.
                     /evidence=ECO:0000269|PubMed:16223874; propagated from
                     UniProtKB/Swiss-Prot (Q15554.3)"
     Region          288..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15554.3)"
     Region          317..358
                     /region_name="TRF2_RBM"
                     /note="RAP1 binding motif of telomere repeat binding
                     factor; cd11654"
                     /db_xref="CDD:212553"
     Site            order(324..330,332..334,336..338,347,350..355)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:212553"
     Region          358..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15554.3)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15554.3)"
     Region          371..375
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15554.3)"
     Region          490..538
                     /region_name="SANT_TRF"
                     /note="Telomere repeat binding factor-like DNA-binding
                     domains of the SANT/myb-like family; cd11660"
                     /db_xref="CDD:212558"
     Site            order(490..492,510,512..513,524,526..528,530..532,
                     534..535)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212558"
     CDS             1..542
                     /gene="TERF2"
                     /gene_synonym="TRBF2; TRF2"
                     /coded_by="NM_005652.5:37..1665"
                     /db_xref="CCDS:CCDS10879.2"
                     /db_xref="GeneID:7014"
                     /db_xref="HGNC:HGNC:11729"
                     /db_xref="MIM:602027"
ORIGIN      
        1 maagagtagp asgpgvvrdp aasqprkrpg reggegarrs dtmaggggss dgsgraagrr
       61 asrssgrarr grhepglggp aergagearl eeavnrwvlk fyfhealraf rgsrygdfrq
      121 irdimqallv rplgkehtvs rllrvmqcls rieegenldc sfdmeaeltp lesainvlem
      181 ikteftltea vvessrklvk eaaviicikn kefekaskil kkhmskdptt qklrndllni
      241 ireknlahpv iqnfsyetfq qkmlrflesh lddaepyllt makkalkses aasstgkedk
      301 qpapgpvekp preparqlrn ppttigmmtl kaafktlsga qdseaafakl dqkdlvlptq
      361 alpaspalkn krprkdenes sapadgeggs elqpknkrmt isrlvleeds qstepsagln
      421 ssqeaasapp skptvlnqpl pgeknpkvpk gkwnssngve eketwveede lfqvqaapde
      481 dsttnitkkq kwtveesewv kagvqkygeg nwaaisknyp fvnrtavmik drwrtmkrlg
      541 mn
//
LOCUS       NP_080907                153 aa            linear   ROD 27-APR-2025
DEFINITION  H/ACA ribonucleoprotein complex subunit 2 isoform 1 [Mus musculus].
ACCESSION   NP_080907
VERSION     NP_080907.1
DBSOURCE    REFSEQ: accession NM_026631.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Ingham,N.J., Pearson,S.A., Vancollie,V.E., Rook,V., Lewis,M.A.,
            Chen,J., Buniello,A., Martelletti,E., Preite,L., Lam,C.C.,
            Weiss,F.D., Powis,Z., Suwannarat,P., Lelliott,C.J., Dawson,S.J.,
            White,J.K. and Steel,K.P.
  TITLE     Mouse screen reveals multiple new genes underlying mouse and human
            hearing loss
  JOURNAL   PLoS Biol 17 (4), e3000194 (2019)
   PUBMED   30973865
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Kappei,D., Butter,F., Benda,C., Scheibe,M., Draskovic,I.,
            Stevense,M., Novo,C.L., Basquin,C., Araki,M., Araki,K.,
            Krastev,D.B., Kittler,R., Jessberger,R., Londono-Vallejo,J.A.,
            Mann,M. and Buchholz,F.
  TITLE     HOT1 is a mammalian direct telomere repeat-binding protein
            contributing to telomerase recruitment
  JOURNAL   EMBO J 32 (12), 1681-1701 (2013)
   PUBMED   23685356
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Egan,E.D. and Collins,K.
  TITLE     Specificity and stoichiometry of subunit interactions in the human
            telomerase holoenzyme assembled in vivo
  JOURNAL   Mol Cell Biol 30 (11), 2775-2786 (2010)
   PUBMED   20351177
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL645602.14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK019134.1, BY710231.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 31.14 cM"
     Protein         1..153
                     /product="H/ACA ribonucleoprotein complex subunit 2
                     isoform 1"
                     /note="nucleolar protein family A, member 2; h/ACA
                     ribonucleoprotein complex subunit 2; snoRNP protein NHP2;
                     H/ACA small nucleolar RNPs; NHP2 ribonucleoprotein
                     homolog"
                     /calculated_mol_wt=17116
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NX24; propagated from
                     UniProtKB/Swiss-Prot (Q9CRB2.1)"
     Region          32..130
                     /region_name="SNU13"
                     /note="U4/U6.U5 small nuclear ribonucleoprotein SNU13;
                     cl42391"
                     /db_xref="CDD:455736"
     Site            order(61..66,69,73,85..86,90,111,120..123)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:411046"
     Site            order(65,68..69,72,87,89..90,92..93,96)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:411046"
     CDS             1..153
                     /gene="Nhp2"
                     /gene_synonym="2410130M07Rik; D11Ertd175e; Nola2"
                     /coded_by="NM_026631.4:46..507"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS24655.1"
                     /db_xref="GeneID:52530"
                     /db_xref="MGI:MGI:1098547"
ORIGIN      
        1 mtkvkaapee seaqaegcse ertykellvn lnpiaqplas rrltrklykc ikkavkqkqi
       61 rrgvkevqkf vnkgekgimv lagdtlpiev ychlpvlced qnlpyvyips ktdlgaatgs
      121 krptcvimvk pheeyqetyd kcleevqalp tpl
//
LOCUS       NP_082295                417 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF135 [Mus musculus].
ACCESSION   NP_082295
VERSION     NP_082295.1
DBSOURCE    REFSEQ: accession NM_028019.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Iwamoto,A., Tsukamoto,H., Nakayama,H. and Oshiumi,H.
  TITLE     E3 Ubiquitin Ligase Riplet Is Expressed in T Cells and Suppresses T
            Cell-Mediated Antitumor Immune Responses
  JOURNAL   J Immunol 208 (8), 2067-2076 (2022)
   PUBMED   35365564
  REMARK    GeneRIF: E3 Ubiquitin Ligase Riplet Is Expressed in T Cells and
            Suppresses T Cell-Mediated Antitumor Immune Responses.
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Hayman,T.J., Hsu,A.C., Kolesnik,T.B., Dagley,L.F., Willemsen,J.,
            Tate,M.D., Baker,P.J., Kershaw,N.J., Kedzierski,L., Webb,A.I.,
            Wark,P.A., Kedzierska,K., Masters,S.L., Belz,G.T., Binder,M.,
            Hansbro,P.M., Nicola,N.A. and Nicholson,S.E.
  TITLE     RIPLET, and not TRIM25, is required for endogenous RIG-I-dependent
            antiviral responses
  JOURNAL   Immunol Cell Biol 97 (9), 840-852 (2019)
   PUBMED   31335993
  REMARK    GeneRIF: Riplet, and not TRIM25, is required endogenously for the
            ubiquitination of RIG-I.
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Cadena,C., Ahmad,S., Xavier,A., Willemsen,J., Park,S., Park,J.W.,
            Oh,S.W., Fujita,T., Hou,F., Binder,M. and Hur,S.
  TITLE     Ubiquitin-Dependent and -Independent Roles of E3 Ligase RIPLET in
            Innate Immunity
  JOURNAL   Cell 177 (5), 1187-1200 (2019)
   PUBMED   31006531
  REMARK    GeneRIF: Ubiquitin-Dependent and -Independent Roles of E3 Ligase
            RIPLET in Innate Immunity.
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Shi,Y., Yuan,B., Zhu,W., Zhang,R., Li,L., Hao,X., Chen,S. and
            Hou,F.
  TITLE     Ube2D3 and Ube2N are essential for RIG-I-mediated MAVS aggregation
            in antiviral innate immunity
  JOURNAL   Nat Commun 8, 15138 (2017)
   PUBMED   28469175
  REMARK    GeneRIF: Together with Riplet, Ube2D3 promotes covalent conjugation
            of polyubiquitin chains to RIG-I, while Ube2N preferentially
            facilitates production of unanchored chains. In the presence of
            these chains, RIG-I induces MAVS aggregation directly on the
            mitochondria. Data thus reveal two essential mechanisms underlying
            the activation of RIG-I and MAVS for triggering innate immune
            signaling in response to viral infection in cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Oshiumi,H., Miyashita,M., Matsumoto,M. and Seya,T.
  TITLE     A distinct role of Riplet-mediated K63-Linked polyubiquitination of
            the RIG-I repressor domain in human antiviral innate immune
            responses
  JOURNAL   PLoS Pathog 9 (8), e1003533 (2013)
   PUBMED   23950712
  REMARK    GeneRIF: Riplet-mediated K63-linked polyubiquitination released
            RIG-I RD autorepression, which allowed the access of positive
            factors to the RIG-I protein.
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Oshiumi,H., Miyashita,M., Inoue,N., Okabe,M., Matsumoto,M. and
            Seya,T.
  TITLE     The ubiquitin ligase Riplet is essential for RIG-I-dependent innate
            immune responses to RNA virus infection
  JOURNAL   Cell Host Microbe 8 (6), 496-509 (2010)
   PUBMED   21147464
  REMARK    GeneRIF: Riplet is essential for regulating RIG-I-mediated innate
            immune response against RNA virus infection in vivo.
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Venturin,M., Bentivegna,A., Moroni,R., Larizza,L. and Riva,P.
  TITLE     Evidence by expression analysis of candidate genes for congenital
            heart defects in the NF1 microdeletion interval
  JOURNAL   Ann Hum Genet 69 (Pt 5), 508-516 (2005)
   PUBMED   16138909
REFERENCE   9  (residues 1 to 417)
  AUTHORS   Jenne,D.E., Tinschert,S., Dorschner,M.O., Hameister,H., Stephens,K.
            and Kehrer-Sawatzki,H.
  TITLE     Complete physical map and gene content of the human NF1 tumor
            suppressor region in human and mouse
  JOURNAL   Genes Chromosomes Cancer 37 (2), 111-120 (2003)
   PUBMED   12696059
REFERENCE   10 (residues 1 to 417)
  AUTHORS   Min,S.H., Simmen,R.C., Alhonen,L., Halmekyto,M., Porter,C.W.,
            Janne,J. and Simmen,F.A.
  TITLE     Altered levels of growth-related and novel gene transcripts in
            reproductive and other tissues of female mice overexpressing
            spermidine/spermine N1-acetyltransferase (SSAT)
  JOURNAL   J Biol Chem 277 (5), 3647-3657 (2002)
   PUBMED   11709547
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591426.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK010429.1, AK152096.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 47.59 cM"
     Protein         1..417
                     /product="E3 ubiquitin-protein ligase RNF135"
                     /EC_number="2.3.2.27"
                     /note="RING-type E3 ubiquitin transferase RNF135"
                     /calculated_mol_wt=46331
     Region          16..88
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(21,24,36,38,41,44,63,66)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438111"
     Region          95..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CWS1.1)"
     Region          143..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CWS1.1)"
     Region          245..413
                     /region_name="SPRY_PRY_RNF135"
                     /note="PRY/SPRY domain in RING finger protein RNF135;
                     cd12902"
                     /db_xref="CDD:293959"
     CDS             1..417
                     /gene="Rnf135"
                     /gene_synonym="0610037N03Rik; 2410006N06Rik; Riplet; U
                     2-3-0"
                     /coded_by="NM_028019.4:49..1302"
                     /db_xref="CCDS:CCDS25129.1"
                     /db_xref="GeneID:71956"
                     /db_xref="MGI:MGI:1919206"
ORIGIN      
        1 maavcsgnav pvwlseddls ciicqglldq pttlpcghsf clrclhdlwv skrgavdgcp
       61 wacpicrkgp ltkpklhknp llqdlvdkyl qaareveags epepapaprs apqvtvqkst
      121 tnviqeltdm vrqlvddvks lqtqrpnlgs gqdnaqgtpp tdsssegehs ldspklvtfs
      181 isqkkiqeil hnleeiqekl qgsvpgrapp rervqemtss lcllpdqrrp aprkashlsl
      241 waisptfdlr tlsynlevsn nsrrvtvsrg dlhtyhwspq rfsisqvfcs qalssgqkyw
      301 evdtrncshw aigvaswgmk rdgmlgrtmd swciewrgpg qfsawakmkk tdlqsdlpev
      361 vgvwldlesg elafyavadh erllyecevs sssplhpafw lyglspgnyl eikqlnt
//
LOCUS       NP_001353277             244 aa            linear   PRI 27-APR-2025
DEFINITION  androgen-induced gene 1 protein isoform j [Homo sapiens].
ACCESSION   NP_001353277
VERSION     NP_001353277.1
DBSOURCE    REFSEQ: accession NM_001366348.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Nakada-Tsukui,K., Sekizuka,T., Sato-Ebine,E., Escueta-de Cadiz,A.,
            Ji,D.D., Tomii,K., Kuroda,M. and Nozaki,T.
  TITLE     AIG1 affects in vitro and in vivo virulence in clinical isolates of
            Entamoeba histolytica
  JOURNAL   PLoS Pathog 14 (3), e1006882 (2018)
   PUBMED   29554130
  REMARK    GeneRIF: High AIG1 expression is associated with virulence in
            clinical isolates of Entamoeba histolytica.
            Erratum:[PLoS Pathog. 2018 May 31;14(5):e1007091. doi:
            10.1371/journal.ppat.1007091. PMID: 29851996]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Parsons,W.H., Kolar,M.J., Kamat,S.S., Cognetta,A.B. 3rd,
            Hulce,J.J., Saez,E., Kahn,B.B., Saghatelian,A. and Cravatt,B.F.
  TITLE     AIG1 and ADTRP are atypical integral membrane hydrolases that
            degrade bioactive FAHFAs
  JOURNAL   Nat Chem Biol 12 (5), 367-372 (2016)
   PUBMED   27018888
  REMARK    GeneRIF: These results indicate that AIG1 and ADTRP are founding
            members of an evolutionarily conserved class of transmembrane
            threonine hydrolases involved in bioactive lipid metabolism.
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Wu,G., Sun,M., Zhang,W. and Huo,K.
  TITLE     AIG1 is a novel Pirh2-interacting protein that activates the NFAT
            signaling pathway
  JOURNAL   Front Biosci (Elite Ed) 3 (3), 834-842 (2011)
   PUBMED   21622095
  REMARK    GeneRIF: identified a novel Pirh2-interacting protein, AIG1, by
            yeast two-hybrid screening and confirmed its interaction with p53
            both in vitro and in vivo
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   8  (residues 1 to 244)
  AUTHORS   Seo,J., Kim,J. and Kim,M.
  TITLE     Cloning of androgen-inducible gene 1 (AIG1) from human dermal
            papilla cells
  JOURNAL   Mol Cells 11 (1), 35-40 (2001)
   PUBMED   11266118
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL023581.1, AL391726.8 and AL136116.11.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.745645.1,
                                           SRR9304716.202557.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.2"
     Protein         1..244
                     /product="androgen-induced gene 1 protein isoform j"
                     /note="androgen-induced gene 1 protein; FAHFA hydrolase
                     AIG1; fatty acid esters of hydroxy fatty acids hydrolase
                     AIG1"
                     /calculated_mol_wt=28021
     Region          12..219
                     /region_name="Far-17a_AIG1"
                     /note="FAR-17a/AIG1-like protein; pfam04750"
                     /db_xref="CDD:428104"
     CDS             1..244
                     /gene="AIG1"
                     /gene_synonym="AIG-1; dJ95L4.1"
                     /coded_by="NM_001366348.1:38..772"
                     /note="isoform j is encoded by transcript variant 10"
                     /db_xref="GeneID:51390"
                     /db_xref="HGNC:HGNC:21607"
                     /db_xref="MIM:608514"
ORIGIN      
        1 malvpcqvlr maillsycsi lcnykaiemp shqtyggswk fltfidlviq avffgicvlt
       61 dlsslltrgs gnqeqerqlk klislrdwml avlafpvgvf vvavfwiiya ydremiypkl
      121 ldnfipgwln hgmhttvlpf iliemrtshh qypsrssglt aictfsvgyi lwvcwvhhvt
      181 gmwvypfleh igpgariiff gsttilmnfl yllgevlnny iwdtqkkpps wqgmeeekek
      241 pkle
//
LOCUS       NP_006308                227 aa            linear   PRI 27-APR-2025
DEFINITION  brain acid soluble protein 1 [Homo sapiens].
ACCESSION   NP_006308
VERSION     NP_006308.3
DBSOURCE    REFSEQ: accession NM_006317.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Meng,Z., Zhou,L., Hong,S., Qiu,X., Chen,Z., Liu,T., Inoki,K. and
            Lin,J.D.
  TITLE     Myeloid-specific ablation of Basp1 ameliorates diet-induced NASH in
            mice by attenuating pro-inflammatory signaling
  JOURNAL   Hepatology 79 (2), 409-424 (2024)
   PUBMED   37505219
  REMARK    GeneRIF: Myeloid-specific ablation of Basp1 ameliorates
            diet-induced NASH in mice by attenuating pro-inflammatory
            signaling.
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Zhang,L., Zhao,Z., Quan,X., Xie,Z. and Zhao,J.
  TITLE     Circ_0008285 silencing suppresses angiotensin II-induced vascular
            smooth muscle cell apoptosis in thoracic aortic aneurysm via
            miR-150-5p/BASP1 axis
  JOURNAL   Thorac Cancer 14 (22), 2158-2167 (2023)
   PUBMED   37337843
  REMARK    GeneRIF: Circ_0008285 silencing suppresses angiotensin II-induced
            vascular smooth muscle cell apoptosis in thoracic aortic aneurysm
            via miR-150-5p/BASP1 axis.
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Wang,T., Liu,X., Wang,T., Zhan,L. and Zhang,M.
  TITLE     BASP1 expression is associated with poor prognosis and is
            correlated with immune infiltration in gastric cancer
  JOURNAL   FEBS Open Bio 13 (8), 1507-1521 (2023)
   PUBMED   37243901
  REMARK    GeneRIF: BASP1 expression is associated with poor prognosis and is
            correlated with immune infiltration in gastric cancer.
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Liao,X., Li,Z., Zheng,H., Qian,W., Zhang,S., Chen,S., Li,X.,
            Tang,M., Xu,Y., Yu,R., Li,M., Song,L. and Li,J.
  TITLE     Downregulation of BASP1 Promotes Temozolomide Resistance in Gliomas
            via Epigenetic Activation of the FBXO32/NF-kappaB/MGMT Axis
  JOURNAL   Mol Cancer Res 21 (7), 648-663 (2023)
   PUBMED   36961398
  REMARK    GeneRIF: Downregulation of BASP1 Promotes Temozolomide Resistance
            in Gliomas via Epigenetic Activation of the FBXO32/NF-kappaB/MGMT
            Axis.
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Sun,F., Liu,J., Wang,Y., Yang,H., Song,D., Fu,H. and Feng,X.
  TITLE     BASP1 promotes high glucose-induced endothelial apoptosis in
            diabetes via activation of EGFR signaling
  JOURNAL   J Diabetes Investig 14 (4), 535-547 (2023)
   PUBMED   36756695
  REMARK    GeneRIF: BASP1 promotes high glucose-induced endothelial apoptosis
            in diabetes via activation of EGFR signaling.
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Behan,A.T., Byrne,C., Dunn,M.J., Cagney,G. and Cotter,D.R.
  TITLE     Proteomic analysis of membrane microdomain-associated proteins in
            the dorsolateral prefrontal cortex in schizophrenia and bipolar
            disorder reveals alterations in LAMP, STXBP1 and BASP1 protein
            expression
  JOURNAL   Mol Psychiatry 14 (6), 601-613 (2009)
   PUBMED   18268500
  REMARK    GeneRIF: proteomic assessments of membrane microdomains in
            prefrontal cortex and validation in two brain series, strongly
            implicates LAMP, STXBP1 and BASP1 in schizophrenia and supports the
            view of a neuritic and synaptic dysfunction in the neuropathology
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Carpenter,B., Hill,K.J., Charalambous,M., Wagner,K.J., Lahiri,D.,
            James,D.I., Andersen,J.S., Schumacher,V., Royer-Pokora,B., Mann,M.,
            Ward,A. and Roberts,S.G.
  TITLE     BASP1 is a transcriptional cosuppressor for the Wilms' tumor
            suppressor protein WT1
  JOURNAL   Mol Cell Biol 24 (2), 537-549 (2004)
   PUBMED   14701728
  REMARK    GeneRIF: BASP1 can confer WT1 cosuppressor activity in transfection
            assays, and elimination of endogenous BASP1 expression augments
            transcriptional activation by WT1.
REFERENCE   8  (residues 1 to 227)
  AUTHORS   Fitzgibbon,J., Neat,M.J., Foot,N., Hill,A.S., Lister,T.A. and
            Gupta,R.K.
  TITLE     Assignment of brain acid-soluble protein 1 (BASP1) to human
            chromosome 5p15.1-->p14, differential expression in human cancer
            cell lines as a result of alterations in gene dosage
  JOURNAL   Cytogenet Cell Genet 89 (3-4), 147-149 (2000)
   PUBMED   10965107
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Park,S., Kim,Y.I., Kim,B., Seong,C., Oh,Y., Baek,K. and Yoon,J.
  TITLE     Characterization of bovine and human cDNAs encoding NAP-22 (22 kDa
            neuronal tissue-enriched acidic protein) homologs
  JOURNAL   Mol Cells 8 (4), 471-477 (1998)
   PUBMED   9749536
REFERENCE   10 (residues 1 to 227)
  AUTHORS   Mosevitsky,M.I., Capony,J.P., Skladchikova,G.Yu., Novitskaya,V.A.,
            Plekhanov,A.Yu. and Zakharov,V.V.
  TITLE     The BASP1 family of myristoylated proteins abundant in axonal
            termini. Primary structure analysis and physico-chemical properties
  JOURNAL   Biochimie 79 (6), 373-384 (1997)
   PUBMED   9310187
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN355202.1, BC000518.2,
            BU181147.1, BM973114.1 and HY258599.1.
            
            On May 16, 2003 this sequence version replaced NP_006308.2.
            
            Summary: This gene encodes a membrane bound protein with several
            transient phosphorylation sites and PEST motifs. Conservation of
            proteins with PEST sequences among different species supports their
            functional significance. PEST sequences typically occur in proteins
            with high turnover rates. Immunological characteristics of this
            protein are species specific. This protein also undergoes
            N-terminal myristoylation. Alternative splicing results in multiple
            transcript variants that encode the same protein. [provided by
            RefSeq, Oct 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.174187.1,
                                           SRR1163658.149186.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322611.4/ ENSP00000319281.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.1"
     Protein         1..227
                     /product="brain acid soluble protein 1"
                     /note="brain acid-soluble protein 1; neuronal axonal
                     membrane protein NAP-22; neuronal tissue-enriched acidic
                     protein; 22 kDa neuronal tissue-enriched acidic protein"
                     /calculated_mol_wt=22562
     Region          1..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P80723.2)"
     Region          12..227
                     /region_name="BASP1"
                     /note="Brain acid soluble protein 1 (BASP1 protein);
                     pfam05466"
                     /db_xref="CDD:461658"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P80723.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P80723.2)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91XV3; propagated from
                     UniProtKB/Swiss-Prot (P80723.2)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P80723.2)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P80723.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P80723.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P80723.2)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91XV3; propagated from
                     UniProtKB/Swiss-Prot (P80723.2)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P80723.2)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P80723.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P80723.2)"
     CDS             1..227
                     /gene="BASP1"
                     /gene_synonym="CAP-23; CAP23; NAP-22; NAP22"
                     /coded_by="NM_006317.5:190..873"
                     /db_xref="CCDS:CCDS3888.1"
                     /db_xref="GeneID:10409"
                     /db_xref="HGNC:HGNC:957"
                     /db_xref="MIM:605940"
ORIGIN      
        1 mggklskkkk gynvndekak ekdkkaegaa teeegtpkes epqaaaepae akegkekpdq
       61 daegkaeeke gekdaaaake eapkaepekt egaaeakaep pkapeqeqaa pgpaaggeap
      121 kaaeaaaapa esaapaagee pskeegepkk teapaapaaq etksdgapas dskpgsseaa
      181 pssketpaat eapsstpkaq gpaasaeepk pveapaansd qtvtvke
//
LOCUS       NP_004589                439 aa            linear   PRI 27-APR-2025
DEFINITION  testican-1 precursor [Homo sapiens].
ACCESSION   NP_004589
VERSION     NP_004589.1
DBSOURCE    REFSEQ: accession NM_004598.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Xiao,M., Xue,J. and Jin,E.
  TITLE     SPOCK: Master regulator of malignant tumors (Review)
  JOURNAL   Mol Med Rep 30 (6) (2024)
   PUBMED   39392048
  REMARK    GeneRIF: SPOCK: Master regulator of malignant tumors (Review).
            Review article
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Liu,Y., Han,T., Wu,J., Zhou,J., Guo,J., Miao,R., Xu,Z., Xing,Y.,
            Bai,Y. and Hu,D.
  TITLE     SPOCK1, as a potential prognostic and therapeutic biomarker for
            lung adenocarcinoma, is associated with epithelial-mesenchymal
            transition and immune evasion
  JOURNAL   J Transl Med 21 (1), 909 (2023)
   PUBMED   38087364
  REMARK    GeneRIF: SPOCK1, as a potential prognostic and therapeutic
            biomarker for lung adenocarcinoma, is associated with
            epithelial-mesenchymal transition and immune evasion.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Lin,Y.W., Wen,Y.C., Hsiao,C.H., Lai,F.R., Yang,S.F., Yang,Y.C.,
            Ho,K.H., Hsieh,F.K., Hsiao,M., Lee,W.J. and Chien,M.H.
  TITLE     Proteoglycan SPOCK1 as a Poor Prognostic Marker Promotes Malignant
            Progression of Clear Cell Renal Cell Carcinoma via Triggering the
            Snail/Slug-MMP-2 Axis-Mediated Epithelial-to-Mesenchymal Transition
  JOURNAL   Cells 12 (3), 352 (2023)
   PUBMED   36766694
  REMARK    GeneRIF: Proteoglycan SPOCK1 as a Poor Prognostic Marker Promotes
            Malignant Progression of Clear Cell Renal Cell Carcinoma via
            Triggering the Snail/Slug-MMP-2 Axis-Mediated
            Epithelial-to-Mesenchymal Transition.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Gan,C., Li,M., Lu,Y., Peng,G., Li,W., Wang,H., Peng,Y., Hu,Q.,
            Wei,W., Wang,F., Liu,L. and Zhao,Q.
  TITLE     SPOCK1 and POSTN are valuable prognostic biomarkers and correlate
            with tumor immune infiltrates in colorectal cancer
  JOURNAL   BMC Gastroenterol 23 (1), 4 (2023)
   PUBMED   36611136
  REMARK    GeneRIF: SPOCK1 and POSTN are valuable prognostic biomarkers and
            correlate with tumor immune infiltrates in colorectal cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Qu,Y.L., Liu,X.L., Zhao,S.Y. and Zhai,X.F.
  TITLE     SPOCK1 silencing decreases 5-FU resistance through PRRX1 in
            colorectal cancer
  JOURNAL   Pathol Res Pract 234, 153895 (2022)
   PUBMED   35462225
  REMARK    GeneRIF: SPOCK1 silencing decreases 5-FU resistance through PRRX1
            in colorectal cancer.
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Marr,H.S., Basalamah,M.A. and Edgell,C.J.
  TITLE     Endothelial cell expression of testican mRNA
  JOURNAL   Endothelium 5 (3), 209-219 (1997)
   PUBMED   9272383
REFERENCE   7  (residues 1 to 439)
  AUTHORS   Charbonnier,F., Perin,J.P., Roussel,G., Nussbaum,J.L. and
            Alliel,P.M.
  TITLE     [Cloning of testican/SPOCK in man and mouse. Neuromuscular
            expression perspectives in pathology]
  JOURNAL   C R Seances Soc Biol Fil 191 (1), 127-133 (1997)
   PUBMED   9181134
  REMARK    Review article
REFERENCE   8  (residues 1 to 439)
  AUTHORS   Bonnet,F., Perin,J.P., Charbonnier,F., Camuzat,A., Roussel,G.,
            Nussbaum,J.L. and Alliel,P.M.
  TITLE     Structure and cellular distribution of mouse brain testican.
            Association with the postsynaptic area of hippocampus pyramidal
            cells
  JOURNAL   J Biol Chem 271 (8), 4373-4380 (1996)
   PUBMED   8626787
REFERENCE   9  (residues 1 to 439)
  AUTHORS   Perin,J.P., Alliel,P.M., Jolles,P. and Bonnet,F.
  TITLE     Proteoglycans in male reproductive tract
  JOURNAL   EXS 70, 191-197 (1994)
   PUBMED   7507743
  REMARK    Review article
REFERENCE   10 (residues 1 to 439)
  AUTHORS   Alliel,P.M., Perin,J.P., Jolles,P. and Bonnet,F.J.
  TITLE     Testican, a multidomain testicular proteoglycan resembling
            modulators of cell social behaviour
  JOURNAL   Eur J Biochem 214 (1), 347-350 (1993)
   PUBMED   8389704
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI550122.1, AF231124.1,
            AC005213.1 and BC030691.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the protein core of a seminal plasma
            proteoglycan containing chondroitin- and heparan-sulfate chains.
            The protein's function is unknown, although similarity to
            thyropin-type cysteine protease-inhibitors suggests its function
            may be related to protease inhibition. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030691.2, AF231124.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394945.6/ ENSP00000378401.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.2"
     Protein         1..439
                     /product="testican-1 precursor"
                     /note="sparc/osteonectin, cwcv and kazal-like domains
                     proteoglycan (testican) 1; SPARC/osteonectin, cwcv and
                     kazal like domains proteoglycan 1"
                     /calculated_mol_wt=48993
     mat_peptide     22..439
                     /product="testican-1"
                     /calculated_mol_wt=47009
     Region          136..174
                     /region_name="Kazal_2"
                     /note="Kazal-type serine protease inhibitor domain;
                     pfam07648"
                     /db_xref="CDD:400135"
     Region          198..309
                     /region_name="EFh_SPARC_TICN1"
                     /note="EF-hand, extracellular calcium-binding (EC) motif,
                     found in testican-1 (TICN1); cd16237"
                     /db_xref="CDD:320016"
     Site            228
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:23234360; propagated from
                     UniProtKB/Swiss-Prot (Q08629.1)"
     Region          245..276
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320016"
     Site            order(257,261,268)
                     /site_type="other"
                     /note="putative Ca binding site [ion binding]"
                     /db_xref="CDD:320016"
     Region          277..309
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320016"
     Region          312..372
                     /region_name="TY"
                     /note="Thyroglobulin type I repeats.; The N-terminal
                     region of human thyroglobulin contains 11 type-1 repeats
                     TY repeats are proposed to be inhibitors of cysteine
                     proteases; cd00191"
                     /db_xref="CDD:238114"
     Site            order(317,332,350,354)
                     /site_type="active"
                     /note="protease interaction site [active]"
                     /db_xref="CDD:238114"
     Site            383
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q08629.1)"
     Site            388
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q08629.1)"
     Region          415..439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08629.1)"
     CDS             1..439
                     /gene="SPOCK1"
                     /gene_synonym="SPOCK; TESTICAN; TIC1"
                     /coded_by="NM_004598.4:149..1468"
                     /db_xref="CCDS:CCDS4191.1"
                     /db_xref="GeneID:6695"
                     /db_xref="HGNC:HGNC:11251"
                     /db_xref="MIM:602264"
ORIGIN      
        1 mpaiavlaaa aaawcflqve srhldalagg agpnhgnfld ndqwlstvsq ydrdkywnrf
       61 rdddyfrnwn pnkpfdqald pskdpclkvk csphkvcvtq dyqtalcvsr khllprqkkg
      121 nvaqkhwvgp snlvkckpcp vaqsamvcgs dghsytskck lefhacstgk slatlcdgpc
      181 pclpepeppk hkaersactd kelrnlasrl kdwfgalhed anrvikptss ntaqgrfdts
      241 ilpickdslg wmfnkldmny dllldpsein aiyldkyepc ikplfnscds fkdgklsnne
      301 wcycfqkpgg lpcqnemnri qklskgksll gafiprcnee gyykatqchg stgqcwcvdk
      361 ygnelagsrk qgavsceeeq etsgdfgsgg svvllddley erelgpkdke gklrvhtrav
      421 teddededdd kedevgyiw
//
LOCUS       NP_001351049             138 aa            linear   PRI 27-APR-2025
DEFINITION  AP-3 complex subunit sigma-1 isoform 8 [Homo sapiens].
ACCESSION   NP_001351049
VERSION     NP_001351049.1
DBSOURCE    REFSEQ: accession NM_001364120.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Bultema,J.J. and Di Pietro,S.M.
  TITLE     Cell type-specific Rab32 and Rab38 cooperate with the ubiquitous
            lysosome biogenesis machinery to synthesize specialized
            lysosome-related organelles
  JOURNAL   Small GTPases 4 (1), 16-21 (2013)
   PUBMED   23247405
  REMARK    Review article
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Zhou,J.B., Yang,J.K., Zhao,L. and Xin,Z.
  TITLE     Variants in KCNQ1, AP3S1, MAN2A1, and ALDH7A1 and the risk of type
            2 diabetes in the Chinese Northern Han population: a case-control
            study and meta-analysis
  JOURNAL   Med Sci Monit 16 (6), BR179-BR183 (2010)
   PUBMED   20512086
  REMARK    GeneRIF: KCNQ and AP3S1, but not MAN2A1 or ALDH7A1 have a role in
            risk of type 2 diabetes in the Chinese Northern Han population
            GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Petrenko,A.A., Pavlova,L.S., Karseladze,A.I., Kisseljov,F.L. and
            Kisseljova,N.P.
  TITLE     Downregulation of genes encoding for subunits of adaptor complex-3
            in cervical carcinomas
  JOURNAL   Biochemistry (Mosc) 71 (10), 1153-1160 (2006)
   PUBMED   17125464
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Theos,A.C., Tenza,D., Martina,J.A., Hurbain,I., Peden,A.A.,
            Sviderskaya,E.V., Stewart,A., Robinson,M.S., Bennett,D.C.,
            Cutler,D.F., Bonifacino,J.S., Marks,M.S. and Raposo,G.
  TITLE     Functions of adaptor protein (AP)-3 and AP-1 in tyrosinase sorting
            from endosomes to melanosomes
  JOURNAL   Mol Biol Cell 16 (11), 5356-5372 (2005)
   PUBMED   16162817
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Seong,E., Wainer,B.H., Hughes,E.D., Saunders,T.L., Burmeister,M.
            and Faundez,V.
  TITLE     Genetic analysis of the neuronal and ubiquitous AP-3 adaptor
            complexes reveals divergent functions in brain
  JOURNAL   Mol Biol Cell 16 (1), 128-140 (2005)
   PUBMED   15537701
REFERENCE   6  (residues 1 to 138)
  AUTHORS   VanRenterghem,B., Morin,M., Czech,M.P. and Heller-Harrison,R.A.
  TITLE     Interaction of insulin receptor substrate-1 with the sigma3A
            subunit of the adaptor protein complex-3 in cultured adipocytes
  JOURNAL   J Biol Chem 273 (45), 29942-29949 (1998)
   PUBMED   9792713
REFERENCE   7  (residues 1 to 138)
  AUTHORS   Dell'Angelica,E.C., Klumperman,J., Stoorvogel,W. and
            Bonifacino,J.S.
  TITLE     Association of the AP-3 adaptor complex with clathrin
  JOURNAL   Science 280 (5362), 431-434 (1998)
   PUBMED   9545220
REFERENCE   8  (residues 1 to 138)
  AUTHORS   Simpson,F., Peden,A.A., Christopoulou,L. and Robinson,M.S.
  TITLE     Characterization of the adaptor-related protein complex, AP-3
  JOURNAL   J Cell Biol 137 (4), 835-845 (1997)
   PUBMED   9151686
REFERENCE   9  (residues 1 to 138)
  AUTHORS   Dell'Angelica,E.C., Ohno,H., Ooi,C.E., Rabinovich,E., Roche,K.W.
            and Bonifacino,J.S.
  TITLE     AP-3: an adaptor-like protein complex with ubiquitous expression
  JOURNAL   EMBO J 16 (5), 917-928 (1997)
   PUBMED   9118953
REFERENCE   10 (residues 1 to 138)
  AUTHORS   Watanabe,T.K., Shimizu,F., Nagata,M., Takaichi,A., Fujiwara,T.,
            Nakamura,Y., Takahashi,E. and Hirai,Y.
  TITLE     Cloning, expression pattern and mapping to 12p 13.2 --> p13.1 of
            CLAPS3, a gene encoding a novel clathrin-adaptor small chain
  JOURNAL   Cytogenet Cell Genet 73 (3), 214-217 (1996)
   PUBMED   8697810
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026449.6 and AC010282.6.
            
            Summary: This gene encodes a subunit of the AP3 adaptor complex.
            This complex functions in the formation of subcellular vesicles
            budded from the Golgi body. Several related pseudogenes of this
            gene have been found. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Dec 2015].
            
            Transcript Variant: This variant (8) contains an alternate exon and
            lacks two other alternate exons compared to variant 7. The
            resulting isoform (8) has a shorter and distinct C-terminus
            compared to isoform 7.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.17886.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.3-q23.1"
     Protein         1..138
                     /product="AP-3 complex subunit sigma-1 isoform 8"
                     /note="clathrin-associated/assembly/adaptor protein, small
                     3 (22kD); AP-3 complex subunit sigma-1; sigma-adaptin 3a;
                     adapter-related protein complex 3 subunit sigma-1;
                     clathrin-associated/assembly/adapter protein, small 3;
                     clathrin adaptor complex AP3, sigma-3A subunit; adaptor
                     related protein complex 3 sigma 1 subunit"
                     /calculated_mol_wt=15802
     Region          1..122
                     /region_name="AP3_sigma"
                     /note="AP-3 complex subunit sigma; cd14834"
                     /db_xref="CDD:341438"
     Site            order(14..17,19..20,45..49,80..85,87..89,92,93..94,97..98,
                     101..112)
                     /site_type="other"
                     /note="putative AP-3 delta interface [polypeptide
                     binding]"
                     /db_xref="CDD:341438"
     Site            order(26,30,34,37,51..53,60)
                     /site_type="other"
                     /note="putative AP-3 mu interface [polypeptide binding]"
                     /db_xref="CDD:341438"
     CDS             1..138
                     /gene="AP3S1"
                     /gene_synonym="CLAPS3; Sigma3A"
                     /coded_by="NM_001364120.1:93..509"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:1176"
                     /db_xref="HGNC:HGNC:2013"
                     /db_xref="MIM:601507"
ORIGIN      
        1 mikailifnn hgkprlskfy qpysedtqqq iiretfhlvs krdenvcnfl egglliggsd
       61 nkliyrhyat lyfvfcvdss eselgildli qvhnilaemv mggmvletnm neivtqidaq
      121 nkleksetfi fqsprqdr
//
LOCUS       NP_065852                414 aa            linear   PRI 27-APR-2025
DEFINITION  arrestin domain-containing protein 3 isoform a [Homo sapiens].
ACCESSION   NP_065852
VERSION     NP_065852.1
DBSOURCE    REFSEQ: accession NM_020801.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Chen,M., Yin,B., Liu,Y., Li,M., Shen,S., Wu,J., Li,W. and Fan,J.
  TITLE     ARRDC3 regulates the targeted therapy sensitivity of clear cell
            renal cell carcinoma by promoting AXL degradation
  JOURNAL   Cell Cycle 23 (1), 56-69 (2024)
   PUBMED   38389126
  REMARK    GeneRIF: ARRDC3 regulates the targeted therapy sensitivity of clear
            cell renal cell carcinoma by promoting AXL degradation.
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Long,M. and Wang,S.
  TITLE     Hsa_circ_0001740 mediates trophoblast cell function via regulating
            miR-188-3p/ARRDC3
  JOURNAL   Mol Reprod Dev 90 (6), 406-416 (2023)
   PUBMED   37436094
  REMARK    GeneRIF: Hsa_circ_0001740 mediates trophoblast cell function via
            regulating miR-188-3p/ARRDC3.
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Huang,C.N., Huang,S.P., Pao,J.B., Chang,T.Y., Lan,Y.H., Lu,T.L.,
            Lee,H.Z., Juang,S.H., Wu,P.P., Pu,Y.S., Hsieh,C.J. and Bao,B.Y.
  TITLE     Genetic polymorphisms in androgen receptor-binding sites predict
            survival in prostate cancer patients receiving androgen-deprivation
            therapy
  JOURNAL   Ann Oncol 23 (3), 707-713 (2012)
   PUBMED   21652578
  REMARK    GeneRIF: single-nucleotide polymorphisms in ARRDC3, FLT1, and SKAP1
            were significant predictors for survival androgen-deprivation
            therapy in prostate cancer patients.
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Davis,O.S., Butcher,L.M., Docherty,S.J., Meaburn,E.L., Curtis,C.J.,
            Simpson,M.A., Schalkwyk,L.C. and Plomin,R.
  TITLE     A three-stage genome-wide association study of general cognitive
            ability: hunting the small effects
  JOURNAL   Behav Genet 40 (6), 759-767 (2010)
   PUBMED   20306291
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Draheim,K.M., Chen,H.B., Tao,Q., Moore,N., Roche,M. and Lyle,S.
  TITLE     ARRDC3 suppresses breast cancer progression by negatively
            regulating integrin beta4
  JOURNAL   Oncogene 29 (36), 5032-5047 (2010)
   PUBMED   20603614
  REMARK    GeneRIF: ARRDC3 directly binds to a phosphorylated form of ITGbeta4
            leading to its internalization, ubiquitination and ultimate
            degradation, and suppress breast cancer progression.
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Nabhan,J.F., Pan,H. and Lu,Q.
  TITLE     Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase
            to mediate ubiquitination of the beta2-adrenergic receptor
  JOURNAL   EMBO Rep 11 (8), 605-611 (2010)
   PUBMED   20559325
  REMARK    GeneRIF: Data show that ARRDC3 interacts with NEDD4 through two
            conserved PPXY motifs and recruits NEDD4 to the activated
            beta2-adrenergic receptor.
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Patwari,P., Chutkow,W.A., Cummings,K., Verstraeten,V.L.,
            Lammerding,J., Schreiter,E.R. and Lee,R.T.
  TITLE     Thioredoxin-independent regulation of metabolism by the
            alpha-arrestin proteins
  JOURNAL   J Biol Chem 284 (37), 24996-25003 (2009)
   PUBMED   19605364
  REMARK    GeneRIF: Txnip regulates cellular metabolism independent of its
            binding to thioredoxin and the arrestin domains are crucial
            structural elements in metabolic functions of alpha-arrestin
            proteins
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Oka,S., Masutani,H., Liu,W., Horita,H., Wang,D., Kizaka-Kondoh,S.
            and Yodoi,J.
  TITLE     Thioredoxin-binding protein-2-like inducible membrane protein is a
            novel vitamin D3 and peroxisome proliferator-activated receptor
            (PPAR)gamma ligand target protein that regulates PPARgamma
            signaling
  JOURNAL   Endocrinology 147 (2), 733-743 (2006)
   PUBMED   16269462
  REMARK    GeneRIF: [Thioredoxin-binding protein-2-like inducible membrane
            protein, TLIMP] TLIMP, a novel VD3- or PPARgamma ligand-inducible
            membrane-associated protein, plays a regulatory role in cell
            proliferation and PPARgamma activation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX642781.1, AB037797.1,
            HY355442.1 and AC008799.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the arrestin family of
            proteins, which regulate G protein-mediated signaling. The encoded
            protein is thought to act as a regulator of breast cancer growth
            and progression by binding to a phosphorylated form of integrin
            beta4, a tumor-related antigen, targeting the integrin for
            internalization and degradation. [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB037797.1, SRR18074969.2823903.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265138.4/ ENSP00000265138.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.3"
     Protein         1..414
                     /product="arrestin domain-containing protein 3 isoform a"
                     /note="TBP-2-like inducible membrane protein;
                     alpha-arrestin 3"
                     /calculated_mol_wt=46264
     Region          22..165
                     /region_name="Arrestin_N"
                     /note="Arrestin (or S-antigen), N-terminal domain;
                     pfam00339"
                     /db_xref="CDD:425619"
     Region          187..314
                     /region_name="Arrestin_C"
                     /note="Arrestin (or S-antigen), C-terminal domain;
                     smart01017"
                     /db_xref="CDD:214976"
     Region          346..349
                     /region_name="PPxY motif 1. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B67.1)"
     Region          391..394
                     /region_name="PPxY motif 2. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B67.1)"
     Region          393..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B67.1)"
     CDS             1..414
                     /gene="ARRDC3"
                     /gene_synonym="TLIMP"
                     /coded_by="NM_020801.4:226..1470"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34202.1"
                     /db_xref="GeneID:57561"
                     /db_xref="HGNC:HGNC:29263"
                     /db_xref="MIM:612464"
ORIGIN      
        1 mvlgkvkslt isfdclndsn vpvyssgdtv sgrvnlevtg eirvkslkih arghakvrwt
       61 esrnagsnta ytqnyteeve yfnhkdilig herdddnsee gfhtihsgrh eyafsfelpq
      121 tplatsfegr hgsvrywvka elhrpwllpv klkkeftvfe hidintpsll spqagtkekt
      181 lccwfctsgp islsakierk gytpgesiqi faeiencssr mvvpkaaiyq tqafyakgkm
      241 kevkqlvanl rgeslssgkt etwngkllki ppvspsildc siirveyslm vyvdipgamd
      301 lflnlplvig tiplhpfgsr tssvssqcsm nmnwlslslp erpeappsya evvteeqrrn
      361 nlapvsacdd feralqgplf ayiqefrflp pplyseidpn pdqsaddrps cpsr
//
LOCUS       NP_473435                573 aa            linear   ROD 27-APR-2025
DEFINITION  acyl-coenzyme A synthetase ACSM1, mitochondrial isoform 1 [Mus
            musculus].
ACCESSION   NP_473435 XP_986046
VERSION     NP_473435.1
DBSOURCE    REFSEQ: accession NM_054094.6
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Labialle,S., Marty,V., Bortolin-Cavaille,M.L., Hoareau-Osman,M.,
            Pradere,J.P., Valet,P., Martin,P.G. and Cavaille,J.
  TITLE     The miR-379/miR-410 cluster at the imprinted Dlk1-Dio3 domain
            controls neonatal metabolic adaptation
  JOURNAL   EMBO J 33 (19), 2216-2230 (2014)
   PUBMED   25124681
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Thiagarajan,R.D., Georgas,K.M., Rumballe,B.A., Lesieur,E.,
            Chiu,H.S., Taylor,D., Tang,D.T., Grimmond,S.M. and Little,M.H.
  TITLE     Identification of anchor genes during kidney development defines
            ontological relationships, molecular subcompartments and regulatory
            pathways
  JOURNAL   PLoS One 6 (2), e17286 (2011)
   PUBMED   21386911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 573)
  AUTHORS   Oka,Y., Kobayakawa,K., Nishizumi,H., Miyamichi,K., Hirose,S.,
            Tsuboi,A. and Sakano,H.
  TITLE     O-MACS, a novel member of the medium-chain acyl-CoA synthetase
            family, specifically expressed in the olfactory epithelium in a
            zone-specific manner
  JOURNAL   Eur J Biochem 270 (9), 1995-2004 (2003)
   PUBMED   12709059
REFERENCE   6  (residues 1 to 573)
  AUTHORS   Fujino,T., Takei,Y.A., Sone,H., Ioka,R.X., Kamataki,A., Magoori,K.,
            Takahashi,S., Sakai,J. and Yamamoto,T.T.
  TITLE     Molecular identification and characterization of two medium-chain
            acyl-CoA synthetases, MACS1 and the Sa gene product
  JOURNAL   J Biol Chem 276 (38), 35961-35966 (2001)
   PUBMED   11470804
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC134587.3.
            
            On May 4, 2006 this sequence version replaced XP_986046.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022149.1, AB059428.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849385, SAMN00849386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 64.02 cM"
     Protein         1..573
                     /product="acyl-coenzyme A synthetase ACSM1, mitochondrial
                     isoform 1"
                     /EC_number="6.2.1.2"
                     /EC_number="6.2.1.25"
                     /note="butyryl Coenzyme A synthetase 1; acyl-coenzyme A
                     synthetase ACSM1, mitochondrial; butyrate--CoA ligase 1;
                     lipoate-activating enzyme; middle-chain acyl-CoA
                     synthetase 1; butyryl-coenzyme A synthetase 1;
                     acetyl-Coenzyme A synthetase 3; benzoate--CoA ligase"
                     /calculated_mol_wt=60662
     transit_peptide 1..35
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q91VA0.1)"
                     /calculated_mol_wt=4117
     mat_peptide     36..573
                     /product="Acyl-coenzyme A synthetase ACSM1, mitochondrial.
                     /id=PRO_0000306092"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91VA0.1)"
                     /calculated_mol_wt=60662
     Region          42..569
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            142
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q91VA0.1)"
     Site            200
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q91VA0.1)"
     Site            210
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q91VA0.1)"
     Site            order(219,222..227,229..230)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(222,339..340,361..366,448,460,463,474,559)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(222,263..264,313,315..316,319,339..340,361..366,448,
                     460,463,471..474,540)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(263,315..316,319,339,471..473,534,540)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            352
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q91VA0.1)"
     Site            387
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q91VA0.1)"
     Site            527
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q91VA0.1)"
     Site            534
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q91VA0.1)"
     Site            545
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q91VA0.1)"
     CDS             1..573
                     /gene="Acsm1"
                     /gene_synonym="Acas3; Bucs1; Macs"
                     /coded_by="NM_054094.6:99..1820"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS21783.1"
                     /db_xref="GeneID:117147"
                     /db_xref="MGI:MGI:2152200"
ORIGIN      
        1 mqwlksfqic kvlqgfslsp tqlhrrlfsr vgaprwndhd speefnfasd vldywaqmee
       61 egkrgpspaf wwvngqgdei kwsfrklrdl tcrtanvfeq icglqqgdhl alilprvpew
      121 wlvtvgcmrt giifmpgttq lkakdilyri qisrakaivt taslvpeves vasecpdlkt
      181 klvvsdhshe gwldfcslik saspdhtcik skmkdpmaif ftsgttgypk makhnqglaf
      241 rsyipscrkl lklktsdilw cmsdpgwila tvgcliepwt sgctvfihhl pqfdpkvive
      301 vlfkypitqc laapgvyrmv lqqktsnlrf ptlehcttgg esllpeeyeq wkqrtglsih
      361 evygqsetgi ssatlremki krgsigkail pfdlqiidek gnilppnteg yigirikptr
      421 plglfmeyen spestsevec gdfynsgdra tideegyiwf lgrgddvina sgyrigpvev
      481 enalaehpav aesavvsspd kdrgevvkaf ivlnpeflsh dqeqlikelq hhvksvtapy
      541 kyprkvefvs elpktvtgki krkelrnkef gql
//
LOCUS       NP_000958                403 aa            linear   PRI 27-APR-2025
DEFINITION  large ribosomal subunit protein uL3 isoform a [Homo sapiens].
ACCESSION   NP_000958
VERSION     NP_000958.1
DBSOURCE    REFSEQ: accession NM_000967.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Deng,N., Zhang,X. and Zhang,Y.
  TITLE     BAIAP2L1 accelerates breast cancer progression and chemoresistance
            by activating AKT signaling through binding with ribosomal protein
            L3
  JOURNAL   Cancer Sci 114 (3), 764-780 (2023)
   PUBMED   36308067
  REMARK    GeneRIF: BAIAP2L1 accelerates breast cancer progression and
            chemoresistance by activating AKT signaling through binding with
            ribosomal protein L3.
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Du,C., Wang,T., Jia,J., Li,J., Xiao,Y., Wang,J., Mao,P., Wang,N.,
            Shi,L. and Wang,M.
  TITLE     Suppression of RPL34 Inhibits Tumor Cell Proliferation and Promotes
            Apoptosis in Glioblastoma
  JOURNAL   Appl Biochem Biotechnol 194 (8), 3494-3506 (2022)
   PUBMED   35377127
  REMARK    GeneRIF: Suppression of RPL34 Inhibits Tumor Cell Proliferation and
            Promotes Apoptosis in Glioblastoma.
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Matsuura-Suzuki,E., Shimazu,T., Takahashi,M., Kotoshiba,K.,
            Suzuki,T., Kashiwagi,K., Sohtome,Y., Akakabe,M., Sodeoka,M.,
            Dohmae,N., Ito,T., Shinkai,Y. and Iwasaki,S.
  TITLE     METTL18-mediated histidine methylation of RPL3 modulates
            translation elongation for proteostasis maintenance
  JOURNAL   Elife 11, e72780 (2022)
   PUBMED   35674491
  REMARK    GeneRIF: METTL18-mediated histidine methylation of RPL3 modulates
            translation elongation for proteostasis maintenance.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Malecki,J.M., Odonohue,M.F., Kim,Y., Jakobsson,M.E., Gessa,L.,
            Pinto,R., Wu,J., Davydova,E., Moen,A., Olsen,J.V., Thiede,B.,
            Gleizes,P.E., Leidel,S.A. and Falnes,P.O.
  TITLE     Human METTL18 is a histidine-specific methyltransferase that
            targets RPL3 and affects ribosome biogenesis and function
  JOURNAL   Nucleic Acids Res 49 (6), 3185-3203 (2021)
   PUBMED   33693809
  REMARK    GeneRIF: Human METTL18 is a histidine-specific methyltransferase
            that targets RPL3 and affects ribosome biogenesis and function.
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Mosca,L., Pagano,M., Pecoraro,A., Borzacchiello,L., Mele,L.,
            Cacciapuoti,G., Porcelli,M., Russo,G. and Russo,A.
  TITLE     S-Adenosyl-l-Methionine Overcomes uL3-Mediated Drug Resistance in
            p53 Deleted Colon Cancer Cells
  JOURNAL   Int J Mol Sci 22 (1), 103 (2020)
   PUBMED   33374288
  REMARK    GeneRIF: S-Adenosyl-l-Methionine Overcomes uL3-Mediated Drug
            Resistance in p53 Deleted Colon Cancer Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Van Raay,T.J., Connors,T.D., Klinger,K.W., Landes,G.M. and
            Burn,T.C.
  TITLE     A novel ribosomal protein L3-like gene (RPL3L) maps to the
            autosomal dominant polycystic kidney disease gene region
  JOURNAL   Genomics 37 (2), 172-176 (1996)
   PUBMED   8921388
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Reddy,T.R., Suhasini,M., Rappaport,J., Looney,D.J., Kraus,G. and
            Wong-Staal,F.
  TITLE     Molecular cloning and characterization of a TAR-binding nuclear
            factor from T cells
  JOURNAL   AIDS Res Hum Retroviruses 11 (6), 663-669 (1995)
   PUBMED   7576925
REFERENCE   10 (residues 1 to 403)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AK130450.1, BC012146.1 and BC071666.1.
            
            Summary: Ribosomes, the complexes that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L3P family of ribosomal proteins and it is located in the
            cytoplasm. The protein can bind to the HIV-1 TAR mRNA, and it has
            been suggested that the protein contributes to tat-mediated
            transactivation. This gene is co-transcribed with several small
            nucleolar RNA genes, which are located in several of this gene's
            introns. Alternate transcriptional splice variants, encoding
            different isoforms, have been characterized. As is typical for
            genes encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.788490.1,
                                           SRR5189652.122410.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216146.9/ ENSP00000346001.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..403
                     /product="large ribosomal subunit protein uL3 isoform a"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L3; HIV-1 TAR RNA-binding
                     protein B; large ribosomal subunit protein uL3"
                     /calculated_mol_wt=45978
     Region          1..400
                     /region_name="PTZ00103"
                     /note="60S ribosomal protein L3; Provisional"
                     /db_xref="CDD:240267"
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P39023.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P39023.2)"
     Site            136
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P27659; propagated from
                     UniProtKB/Swiss-Prot (P39023.2)"
     Site            245
                     /site_type="methylation"
                     /note="Tele-methylhistidine.
                     /evidence=ECO:0000269|PubMed:33693809,
                     ECO:0000269|PubMed:35674491; propagated from
                     UniProtKB/Swiss-Prot (P39023.2)"
     Site            286
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P27659; propagated from
                     UniProtKB/Swiss-Prot (P39023.2)"
     Site            294
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P39023.2)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P39023.2)"
     Site            366
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P39023.2)"
     Site            373
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P27659; propagated from
                     UniProtKB/Swiss-Prot (P39023.2)"
     CDS             1..403
                     /gene="RPL3"
                     /gene_synonym="ASC-1; L3; TARBP-B; uL3"
                     /coded_by="NM_000967.4:27..1238"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13988.1"
                     /db_xref="GeneID:6122"
                     /db_xref="HGNC:HGNC:10332"
                     /db_xref="MIM:604163"
ORIGIN      
        1 mshrkfsapr hgslgflprk rssrhrgkvk sfpkddpskp vhltaflgyk agmthivrev
       61 drpgskvnkk evveavtive tppmvvvgiv gyvetprglr tfktvfaehi sdeckrrfyk
      121 nwhkskkkaf tkyckkwqde dgkkqlekdf ssmkkycqvi rviahtqmrl lplrqkkahl
      181 meiqvnggtv aekldwarer leqqvpvnqv fgqdemidvi gvtkgkgykg vtsrwhtkkl
      241 prkthrglrk vacigawhpa rvafsvarag qkgyhhrtei nkkiykigqg ylikdgklik
      301 nnastdydls dksinplggf vhygevtndf vmlkgcvvgt kkrvltlrks llvqtkrral
      361 ekidlkfidt tskfghgrfq tmeekkafmg plkkdriake ega
//
LOCUS       NP_006708                262 aa            linear   PRI 27-APR-2025
DEFINITION  spindlin-1 [Homo sapiens].
ACCESSION   NP_006708
VERSION     NP_006708.2
DBSOURCE    REFSEQ: accession NM_006717.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wang,Y., Li,M., Chen,Y., Jiang,Y., Zhang,Z., Yan,Z., Liu,X. and
            Wu,C.
  TITLE     SPIN1 facilitates chemoresistance and HR repair by promoting Tip60
            binding to H3K9me3
  JOURNAL   EMBO Rep 25 (9), 3970-3989 (2024)
   PUBMED   39090319
  REMARK    GeneRIF: SPIN1 facilitates chemoresistance and HR repair by
            promoting Tip60 binding to H3K9me3.
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Zhao,F., Deng,Y., Yang,F., Yan,Y., Feng,F., Peng,B., Gao,J.,
            Bedford,M.T. and Li,H.
  TITLE     Molecular Basis for SPINDOC-Spindlin1 Engagement and Its Role in
            Transcriptional Attenuation
  JOURNAL   J Mol Biol 436 (7), 168371 (2024)
   PUBMED   37977297
  REMARK    GeneRIF: Molecular Basis for SPINDOC-Spindlin1 Engagement and Its
            Role in Transcriptional Attenuation.
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Li,D., Guo,J. and Jia,R.
  TITLE     Epigenetic Control of Cancer Cell Proliferation and Cell Cycle
            Progression by HNRNPK via Promoting Exon 4 Inclusion of Histone
            Code Reader SPIN1
  JOURNAL   J Mol Biol 435 (6), 167993 (2023)
   PUBMED   36736887
  REMARK    GeneRIF: Epigenetic Control of Cancer Cell Proliferation and Cell
            Cycle Progression by HNRNPK via Promoting Exon 4 Inclusion of
            Histone Code Reader SPIN1.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Porzberg,M.R.B., Moesgaard,L., Johansson,C., Oppermann,U.,
            Kongsted,J. and Mecinovic,J.
  TITLE     Recognition of Dimethylarginine Analogues by Tandem Tudor Domain
            Protein Spindlin1
  JOURNAL   Molecules 27 (3), 983 (2022)
   PUBMED   35164245
  REMARK    GeneRIF: Recognition of Dimethylarginine Analogues by Tandem Tudor
            Domain Protein Spindlin1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Zhou,L., Wang,H., Fang,Z., Zhong,M., He,Y., Zou,J., Huang,S.,
            Li,J., Xiang,X. and Fang,Z.
  TITLE     The microRNA-381(miR-381)/Spindlin1(SPIN1) axis contributes to cell
            proliferation and invasion of colorectal cancer cells by regulating
            the Wnt/beta-catenin pathway
  JOURNAL   Bioengineered 12 (2), 12036-12048 (2021)
   PUBMED   34753384
  REMARK    GeneRIF: The microRNA-381(miR-381)/Spindlin1(SPIN1) axis
            contributes to cell proliferation and invasion of colorectal cancer
            cells by regulating the Wnt/beta-catenin pathway.
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Jiang,F., Zhao,Q., Qin,L., Pang,H., Pei,X. and Rao,Z.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            analysis of human spindlin1, an ovarian cancer-related protein
  JOURNAL   Protein Pept Lett 13 (2), 203-205 (2006)
   PUBMED   16472086
  REMARK    GeneRIF: recombinant human spindlin1 has been overexpressed in
            Escherichia coli BL21, purified and crystallized using the
            hanging-drop vapour-diffusion method
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Gao,Y., Yue,W., Zhang,P., Li,L., Xie,X., Yuan,H., Chen,L., Liu,D.,
            Yan,F. and Pei,X.
  TITLE     Spindlin1, a novel nuclear protein with a role in the
            transformation of NIH3T3 cells
  JOURNAL   Biochem Biophys Res Commun 335 (2), 343-350 (2005)
   PUBMED   16098913
  REMARK    GeneRIF: spindlin1 gene may contribute to tumorigenesis
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   9  (residues 1 to 262)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 262)
  AUTHORS   Oh,B., Hwang,S.Y., Solter,D. and Knowles,B.B.
  TITLE     Spindlin, a major maternal transcript expressed in the mouse during
            the transition from oocyte to embryo
  JOURNAL   Development 124 (2), 493-503 (1997)
   PUBMED   9053325
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB465491.2, AF087864.1 and AL353748.13.
            
            On Aug 15, 2006 this sequence version replaced NP_006708.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136719.1, SRR1803616.23846.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375859.4/ ENSP00000365019.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.1"
     Protein         1..262
                     /product="spindlin-1"
                     /note="ovarian cancer-related protein; spindlin1"
                     /calculated_mol_wt=29470
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y657.3)"
     Site            44
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q61142; propagated from
                     UniProtKB/Swiss-Prot (Q9Y657.3)"
     Region          53..116
                     /region_name="Tudor-like domain 1.
                     /evidence=ECO:0000269|PubMed:23077255,
                     ECO:0000269|PubMed:24589551"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y657.3)"
     Region          54..102
                     /region_name="Spin-Ssty"
                     /note="Spin/Ssty Family; pfam02513"
                     /db_xref="CDD:460577"
     Region          93..98
                     /region_name="Histone H3K4me3 and H3R8me2a binding.
                     /evidence=ECO:0000269|PubMed:23077255,
                     ECO:0000269|PubMed:24589551"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y657.3)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKA.
                     /evidence=ECO:0000269|PubMed:22258766; propagated from
                     UniProtKB/Swiss-Prot (Q9Y657.3)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKA.
                     /evidence=ECO:0000269|PubMed:22258766,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y657.3)"
     Region          132..193
                     /region_name="Tudor-like domain 2.
                     /evidence=ECO:0000269|PubMed:23077255,
                     ECO:0000269|PubMed:24589551"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y657.3)"
     Region          133..181
                     /region_name="Spin-Ssty"
                     /note="Spin/Ssty Family; pfam02513"
                     /db_xref="CDD:460577"
     Region          142
                     /region_name="Histone H3K4me3 and H3R8me2a binding.
                     /evidence=ECO:0000269|PubMed:23077255,
                     ECO:0000269|PubMed:24589551"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y657.3)"
     Site            173
                     /site_type="other"
                     /note="Histone H3K4me3 and H3R8me2a binding.
                     /evidence=ECO:0000269|PubMed:23077255,
                     ECO:0000269|PubMed:24589551; propagated from
                     UniProtKB/Swiss-Prot (Q9Y657.3)"
     Site            180
                     /site_type="other"
                     /note="Histone H3K4me3 and H3R8me2a binding.
                     /evidence=ECO:0000269|PubMed:23077255,
                     ECO:0000269|PubMed:24589551; propagated from
                     UniProtKB/Swiss-Prot (Q9Y657.3)"
     Site            184
                     /site_type="other"
                     /note="Histone H3K4me3 and H3R8me2a binding.
                     /evidence=ECO:0000269|PubMed:23077255,
                     ECO:0000269|PubMed:24589551; propagated from
                     UniProtKB/Swiss-Prot (Q9Y657.3)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y657.3)"
     Region          213..262
                     /region_name="Tudor-like domain 3.
                     /evidence=ECO:0000269|PubMed:23077255,
                     ECO:0000269|PubMed:24589551"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y657.3)"
     Region          214..258
                     /region_name="Spin-Ssty"
                     /note="Spin/Ssty Family; pfam02513"
                     /db_xref="CDD:460577"
     Region          250..252
                     /region_name="Histone H3K4me3 and H3R8me2a binding.
                     /evidence=ECO:0000269|PubMed:23077255,
                     ECO:0000269|PubMed:24589551"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y657.3)"
     CDS             1..262
                     /gene="SPIN1"
                     /gene_synonym="SPIN; TDRD24"
                     /coded_by="NM_006717.3:254..1042"
                     /db_xref="CCDS:CCDS43843.1"
                     /db_xref="GeneID:10927"
                     /db_xref="HGNC:HGNC:11243"
                     /db_xref="MIM:609936"
ORIGIN      
        1 mktpfgktpg qrsradagha gvsanmmkkr tshkkhrssv gpskpvsqpr rnivgcriqh
       61 gwkegngpvt qwkgtvldqv pvnpslylik ydgfdcvygl elnkdervsa levlpdrvat
      121 srisdahlad tmigkavehm fetedgskde wrgmvlarap vmntwfyity ekdpvlymyq
      181 llddykegdl rimpdsndsp paerepgevv dslvgkqvey akedgskrtg mvihqveakp
      241 svyfikfddd fhiyvydlvk ts
//
LOCUS       NP_001307902             400 aa            linear   PRI 27-APR-2025
DEFINITION  golgin-45 isoform 1 [Homo sapiens].
ACCESSION   NP_001307902
VERSION     NP_001307902.1
DBSOURCE    REFSEQ: accession NM_001320973.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Gao,J., Zhu,L., Yue,X., Jing,S., Tang,S., Lee,I. and Qian,Y.
  TITLE     Golgin45 assists mitosis via its nuclear localization sequence
  JOURNAL   Biochem Biophys Res Commun 735, 150845 (2024)
   PUBMED   39442450
  REMARK    GeneRIF: Golgin45 assists mitosis via its nuclear localization
            sequence.
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Tong,J.H., Fant,X., Benoit,G., Chen,S.J., Chen,Z. and Lanotte,M.
  TITLE     Genomic organization of the JEM-1 (BLZF1) gene on human chromosome
            1q24: molecular cloning and analysis of its promoter region
  JOURNAL   Genomics 69 (3), 380-390 (2000)
   PUBMED   11056056
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Tong,J.H., Duprez,E. and Lanotte,M.
  TITLE     JEM-1, a novel nuclear co-factor: localisation and functional
            interaction with AP-1
  JOURNAL   Leukemia 13 (12), 1982-1992 (1999)
   PUBMED   10602419
REFERENCE   8  (residues 1 to 400)
  AUTHORS   Tong,J.H., Fant,X., Duprez,E., Benoit,G., Uphoff,C.C.,
            Drexler,H.G., Pla,J.C., Lofvenberg,E. and Lanotte,M.
  TITLE     Expression patterns of the JEM-1 gene in normal and tumor cells:
            ubiquity contrasting with a faint, but retinoid-induced, mRNA
            expression in promyelocytic NB4 cells
  JOURNAL   Leukemia 12 (11), 1733-1740 (1998)
   PUBMED   9823948
REFERENCE   9  (residues 1 to 400)
  AUTHORS   Ting,N.S., Kao,P.N., Chan,D.W., Lintott,L.G. and Lees-Miller,S.P.
  TITLE     DNA-dependent protein kinase interacts with antigen receptor
            response element binding proteins NF90 and NF45
  JOURNAL   J Biol Chem 273 (4), 2136-2145 (1998)
   PUBMED   9442054
REFERENCE   10 (residues 1 to 400)
  AUTHORS   Duprez,E., Tong,J.H., Derre,J., Chen,S.J., Berger,R., Chen,Z. and
            Lanotte,M.
  TITLE     JEM-1, a novel gene encoding a leucine-zipper nuclear factor
            upregulated during retinoid-induced maturation of NB4 promyelocytic
            leukaemia
  JOURNAL   Oncogene 14 (13), 1563-1570 (1997)
   PUBMED   9129147
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U79751.1, AL021068.2 and CA336342.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.73068.1,
                                           SRR1660809.144589.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367808.8/ ENSP00000356782.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..400
                     /product="golgin-45 isoform 1"
                     /note="JEM-1short protein; cytoplasmic protein; p45 basic
                     leucine-zipper nuclear factor; leucine zipper nuclear
                     factor"
                     /calculated_mol_wt=44779
     Region          1..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2G9.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H2G9.2)"
     Region          18..22
                     /region_name="Tankyrase-binding motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2G9.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H2G9.2)"
     Region          <121..>260
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          181..226
                     /region_name="DASH_Hsk3"
                     /note="DASH complex subunit Hsk3 like; pfam08227"
                     /db_xref="CDD:429874"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H2G9.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H2G9.2)"
     Region          394..400
                     /region_name="Essential for interaction with GORASP2.
                     /evidence=ECO:0000269|PubMed:11739401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2G9.2)"
     CDS             1..400
                     /gene="BLZF1"
                     /gene_synonym="GOLGIN-45; JEM-1; JEM-1s; JEM1"
                     /coded_by="NM_001320973.2:199..1401"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS1278.1"
                     /db_xref="GeneID:8548"
                     /db_xref="HGNC:HGNC:1065"
                     /db_xref="MIM:608692"
ORIGIN      
        1 mttknletkv tvtsspirga gdgmeteepp ksvevtsgvq srkhhslqsp wkkavpsesp
       61 gvlqlgkmlt ekamevkavr ilvpkaaith dipnkntkvk slghhkgefl gqsegviepn
      121 kelsevknvl eklknserrl lqdkeglsnq lrvqtevnre lkkllvasvg ddlqyhferl
      181 areknqlile nealgrntaq lseqlermsi qcdvwrskfl asrvmadelt nsraalqrqn
      241 rdahgaiqdl lsereqfrqe miatqkllee llvslqwgre qtyspsvqph staelaltnh
      301 klakavnshl lgnvginnqk kipstvefcs tpaekmaetv lrildpvtck esspdnpffe
      361 sspttllatk knigrfhpyt ryenitfncc nhcrgelial
//
LOCUS       NP_001138666              69 aa            linear   PRI 27-APR-2025
DEFINITION  A-kinase anchor protein inhibitor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001138666 XP_001719977 XP_001719979 XP_936477 XP_936482
            XP_950817 XP_950819
VERSION     NP_001138666.1
DBSOURCE    REFSEQ: accession NM_001145194.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Fukuda,M. and Aizawa,Y.
  TITLE     Hypothetical gene C18orf42 encodes a novel protein kinase A-binding
            protein
  JOURNAL   Genes Cells 20 (4), 267-280 (2015)
   PUBMED   25653177
  REMARK    GeneRIF: These findings suggest that C18orf42 may be a novel PKA
            signaling gene that serves as an endogenous disruptor peptide for
            PKA-AKAP interactions.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001496.4 and AP005380.2.
            
            On or before Feb 18, 2009 this sequence version replaced
            XP_950817.1, XP_950819.1, XP_001719977.1, XP_001719979.1,
            XP_936477.1, XP_936482.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.114515.1,
                                           SRR1660805.98491.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2146411
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000434239.4/ ENSP00000399075.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.31"
     Protein         1..69
                     /product="A-kinase anchor protein inhibitor 1 isoform 1"
                     /note="A-kinase anchor protein C18orf42; A-kinase anchor
                     protein inhibitor 1; A kinase (PRKA) anchor inhibitor 1"
                     /calculated_mol_wt=7717
     Region          12..>44
                     /region_name="AKAP7_RIRII_bdg"
                     /note="PKA-RI-RII subunit binding domain of A-kinase
                     anchor protein; pfam10470"
                     /db_xref="CDD:463101"
     Region          17..33
                     /region_name="PKA-RII subunit binding domain.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P0CW23.1)"
     Region          37..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0CW23.1)"
     CDS             1..69
                     /gene="AKAIN1"
                     /gene_synonym="C18orf42"
                     /coded_by="NM_001145194.2:205..414"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54179.1"
                     /db_xref="GeneID:642597"
                     /db_xref="HGNC:HGNC:28285"
                     /db_xref="MIM:616427"
ORIGIN      
        1 mvfapgekpg nepeevklqn askqivqnai lqavqqvsqe sqrreerisd nrdhiqlgvg
       61 eltkkhekk
//
LOCUS       NP_001352751             891 aa            linear   PRI 27-APR-2025
DEFINITION  type II inositol 1,4,5-trisphosphate 5-phosphatase isoform 5 [Homo
            sapiens].
ACCESSION   NP_001352751 XP_016856696
VERSION     NP_001352751.1
DBSOURCE    REFSEQ: accession NM_001365822.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 891)
  AUTHORS   Droubi,A., Wallis,C., Anderson,K.E., Rahman,S., de Sa,A.,
            Rahman,T., Stephens,L.R., Hawkins,P.T. and Lowe,M.
  TITLE     The inositol 5-phosphatase INPP5B regulates B cell receptor
            clustering and signaling
  JOURNAL   J Cell Biol 221 (9) (2022)
   PUBMED   35878408
  REMARK    GeneRIF: The inositol 5-phosphatase INPP5B regulates B cell
            receptor clustering and signaling.
REFERENCE   2  (residues 1 to 891)
  AUTHORS   Nakatsu,F., Messa,M., Nandez,R., Czapla,H., Zou,Y.,
            Strittmatter,S.M. and De Camilli,P.
  TITLE     Sac2/INPP5F is an inositol 4-phosphatase that functions in the
            endocytic pathway
  JOURNAL   J Cell Biol 209 (1), 85-95 (2015)
   PUBMED   25869668
REFERENCE   3  (residues 1 to 891)
  AUTHORS   Montjean,R., Aoidi,R., Desbois,P., Rucci,J., Trichet,M.,
            Salomon,R., Rendu,J., Faure,J., Lunardi,J., Gacon,G., Billuart,P.
            and Dorseuil,O.
  TITLE     OCRL-mutated fibroblasts from patients with Dent-2 disease exhibit
            INPP5B-independent phenotypic variability relatively to Lowe
            syndrome cells
  JOURNAL   Hum Mol Genet 24 (4), 994-1006 (2015)
   PUBMED   25305077
  REMARK    GeneRIF: OCRL-mutated fibroblasts from patients with Dent-2 disease
            exhibit INPP5B-independent phenotypic variability relatively to
            Lowe syndrome cells
REFERENCE   4  (residues 1 to 891)
  AUTHORS   Pirruccello,M., Nandez,R., Idevall-Hagren,O., Alcazar-Roman,A.,
            Abriola,L., Berwick,S.A., Lucast,L., Morel,D. and De Camilli,P.
  TITLE     Identification of inhibitors of inositol 5-phosphatases through
            multiple screening strategies
  JOURNAL   ACS Chem Biol 9 (6), 1359-1368 (2014)
   PUBMED   24742366
REFERENCE   5  (residues 1 to 891)
  AUTHORS   Tresaugues,L., Silvander,C., Flodin,S., Welin,M., Nyman,T.,
            Graslund,S., Hammarstrom,M., Berglund,H. and Nordlund,P.
  TITLE     Structural basis for phosphoinositide substrate recognition,
            catalysis, and membrane interactions in human inositol
            polyphosphate 5-phosphatases
  JOURNAL   Structure 22 (5), 744-755 (2014)
   PUBMED   24704254
  REMARK    GeneRIF: The crystal structures of human INPP5B in complex with
            phosphoinositide substrate analogs revealed a membrane interaction
            patch likely to assist in sequestering substrates from the lipid
            bilayer.
REFERENCE   6  (residues 1 to 891)
  AUTHORS   Speed,C.J., Matzaris,M., Bird,P.I. and Mitchell,C.A.
  TITLE     Tissue distribution and intracellular localisation of the 75-kDa
            inositol polyphosphate 5-phosphatase
  JOURNAL   Eur J Biochem 234 (1), 216-224 (1995)
   PUBMED   8529643
REFERENCE   7  (residues 1 to 891)
  AUTHORS   Jefferson,A.B. and Majerus,P.W.
  TITLE     Properties of type II inositol polyphosphate 5-phosphatase
  JOURNAL   J Biol Chem 270 (16), 9370-9377 (1995)
   PUBMED   7721860
REFERENCE   8  (residues 1 to 891)
  AUTHORS   Janne,P.A., Dutra,A.S., Dracopoli,N.C., Charnas,L.R., Puck,J.M. and
            Nussbaum,R.L.
  TITLE     Localization of the 75-kDa inositol polyphosphate-5-phosphatase
            (INPP5B) to human chromosome band 1p34
  JOURNAL   Cytogenet Cell Genet 66 (3), 164-166 (1994)
   PUBMED   8125013
REFERENCE   9  (residues 1 to 891)
  AUTHORS   Ross,T.S., Jefferson,A.B., Mitchell,C.A. and Majerus,P.W.
  TITLE     Cloning and expression of human 75-kDa inositol
            polyphosphate-5-phosphatase
  JOURNAL   J Biol Chem 266 (30), 20283-20289 (1991)
   PUBMED   1718960
REFERENCE   10 (residues 1 to 891)
  AUTHORS   Mitchell,C.A., Connolly,T.M. and Majerus,P.W.
  TITLE     Identification and isolation of a 75-kDa inositol
            polyphosphate-5-phosphatase from human platelets
  JOURNAL   J Biol Chem 264 (15), 8873-8877 (1989)
   PUBMED   2542294
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL603790.41 and AL929472.21.
            
            On Sep 13, 2018 this sequence version replaced XP_016856696.1.
            
            Summary: This gene encodes a member of a family of inositol
            polyphosphate-5-phosphatases. These enzymes function in the
            regulation of calcium signaling by inactivating inositol
            phosphates. The encoded protein is localized to the cytosol and
            mitochondria, and associates with membranes through an isoprenyl
            modification near the C-terminus. Alternatively spliced transcript
            variants of this gene have been described. [provided by RefSeq, Jul
            2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..891
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..891
                     /product="type II inositol 1,4,5-trisphosphate
                     5-phosphatase isoform 5"
                     /EC_number="3.1.3.36"
                     /note="phosphoinositide 5-phosphatase; type II inositol
                     1,4,5-trisphosphate 5-phosphatase; inositol
                     polyphosphate-5-phosphatase, 75kDa"
                     /calculated_mol_wt=101170
     Region          <63..124
                     /region_name="INPP5B_PH"
                     /note="Type II inositol 1,4,5-trisphosphate 5-phosphatase
                     PH domain; pfam16776"
                     /db_xref="CDD:465268"
     Region          243..536
                     /region_name="INPP5c_INPP5B"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of Type II inositol polyphosphate
                     5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and
                     related proteins; cd09093"
                     /db_xref="CDD:197327"
     Site            order(251,253,281,284,286,289,351,357..358,378,381..382,
                     425,427,429,480..481,494,496,502,526..527)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197327"
     Site            order(251,281,378,425,427,502,526..527)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197327"
     Site            order(253,281,526)
                     /site_type="other"
                     /note="Mg binding site [ion binding]"
                     /db_xref="CDD:197327"
     Site            order(281,284,286,289,351,357..358,378,381..382,429,
                     480..481,494,496,526)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197327"
     Site            order(378,427,527)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197327"
     Region          670..890
                     /region_name="RhoGAP_OCRL1"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain present in OCRL1-like proteins.
                     OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins
                     contain two conserved domains: a central inositol
                     polyphosphate 5-phosphatase domain and...; cd04380"
                     /db_xref="CDD:239845"
     Site            order(750,785,789,852,855..856,881)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239845"
     Site            750
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239845"
     CDS             1..891
                     /gene="INPP5B"
                     /gene_synonym="5PTase"
                     /coded_by="NM_001365822.1:91..2766"
                     /note="isoform 5 is encoded by transcript variant 7"
                     /db_xref="GeneID:3633"
                     /db_xref="HGNC:HGNC:6077"
                     /db_xref="MIM:147264"
ORIGIN      
        1 mtgvcaqqgp awtslwqsrr rwlrgntass rckvccvrgt agraaswdsc atawstaarn
       61 tlspdgelyi lgsdvtvqld taelslvfql pfgsqtrmfl hevaracpgf dsatrdpefl
      121 wlsryrcael elemptprgc nsalvtwpgy atiggggsnf dglrpngkgv pmdqssrgqd
      181 kpeslqprqn kskseitdmv rsstitvsdk ahilsmqkfg lrdtivkshl lqkeedytyi
      241 qnfrffagty nvngqspkec lrlwlsngiq apdvycvgfq eldlskeaff fhdtpkeeew
      301 fkavseglhp dakyakvkli rlvgimllly vkqehaayis eveaetvgtg imgrmgnkgg
      361 vairfqfhnt sicvvnshla ahieeyerrn qdykdicsrm qfcqpdpslp pltisnhdvi
      421 lwlgdlnyri eeldvekvkk lieekdfqml yaydqlkiqv aaktvfegft egeltfqpty
      481 kydtgsddwd tsekcrapaw cdrilwkgkn itqlsyqshm alktsdhkpv ssvfdigvrv
      541 vndelyrktl eeivrsldkm enanipsvsl skrefcfqnv kymqlkvesf tihngqvpch
      601 fefinkpdee syckqwlnan psrgfllpds dveidlelfv nkmtatklns gedkiedilv
      661 lhldrgkdyf lsvsgnylps cfgspihtlc ymrepildlp letiseltlm pvwtgddgsq
      721 ldspmeipke lwmmvdylyr navqqedlfq qpglrsefeh irdcldtgmi dnlsasnhsv
      781 aealllfles lpepvicyst yhnclecsgn ytaskqvist lpifhknvfh ylmaflrell
      841 knsaknhlde nilasifgsl llrnpaghqk ldmtekkkaq efihqflcnp l
//
LOCUS       NP_001001551             187 aa            linear   PRI 27-APR-2025
DEFINITION  probable gluconokinase isoform 1 [Homo sapiens].
ACCESSION   NP_001001551 XP_497063
VERSION     NP_001001551.2
DBSOURCE    REFSEQ: accession NM_001001551.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Rohatgi,N., Guethmundsson,S. and Rolfsson,O.
  TITLE     Kinetic analysis of gluconate phosphorylation by human
            gluconokinase using isothermal titration calorimetry
  JOURNAL   FEBS Lett 589 (23), 3548-3555 (2015)
   PUBMED   26505675
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Rohatgi,N., Nielsen,T.K., Bjorn,S.P., Axelsson,I., Paglia,G.,
            Voldborg,B.G., Palsson,B.O. and Rolfsson,O.
  TITLE     Biochemical characterization of human gluconokinase and the
            proposed metabolic impact of gluconic acid as determined by
            constraint based metabolic network analysis
  JOURNAL   PLoS One 9 (6), e98760 (2014)
   PUBMED   24896608
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Rolfsson,O., Paglia,G., Magnusdottir,M., Palsson,B.O. and Thiele,I.
  TITLE     Inferring the metabolism of human orphan metabolites from their
            metabolic network context affirms human gluconokinase activity
  JOURNAL   Biochem J 449 (2), 427-435 (2013)
   PUBMED   23067238
  REMARK    GeneRIF: Data show that C9orf103 encodes a functional
            gluconokinase.
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC036421.1 and AY615889.1.
            
            On Jun 26, 2010 this sequence version replaced NP_001001551.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.20673.1,
                                           SRR5189664.18512.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376419.5/ ENSP00000365601.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.32"
     Protein         1..187
                     /product="probable gluconokinase isoform 1"
                     /EC_number="2.7.1.12"
                     /note="gluconokinase-like protein; probable gluconokinase;
                     glucokinase-like protein; gluconate kinase; idnK,
                     gluconokinase homolog"
                     /calculated_mol_wt=20447
     Region          4..185
                     /region_name="GntK"
                     /note="Gluconate kinase [Carbohydrate transport and
                     metabolism]; COG3265"
                     /db_xref="CDD:442496"
     CDS             1..187
                     /gene="IDNK"
                     /gene_synonym="bA522I20.2; C9orf103; hGntK"
                     /coded_by="NM_001001551.4:30..593"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35048.2"
                     /db_xref="GeneID:414328"
                     /db_xref="HGNC:HGNC:31367"
                     /db_xref="MIM:611343"
ORIGIN      
        1 maapgallvm gvsgsgkstv gallaselgw kfydaddyhp eenrrkmgkg iplndqdrip
       61 wlcnlhdill rdvasgqrvv lacsalkkty rdiltqgkdg valkceesgk eakqaemqll
      121 vvhlsgsfev isgrllkreg hfmppellqs qfetleppaa penfiqisvd knvseiiati
      181 metlkmk
//
LOCUS       NP_002173                570 aa            linear   PRI 27-APR-2025
DEFINITION  interleukin-1 receptor accessory protein isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_002173
VERSION     NP_002173.1
DBSOURCE    REFSEQ: accession NM_002182.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Mulholland,M., Depuydt,M.A.C., Jakobsson,G., Ljungcrantz,I.,
            Grentzmann,A., To,F., Bengtsson,E., Jaensson Gyllenback,E.,
            Gronberg,C., Rattik,S., Liberg,D., Schiopu,A., Bjorkbacka,H.,
            Kuiper,J., Bot,I., Slutter,B. and Engelbertsen,D.
  TITLE     Interleukin-1 receptor accessory protein blockade limits the
            development of atherosclerosis and reduces plaque inflammation
  JOURNAL   Cardiovasc Res 120 (6), 581-595 (2024)
   PUBMED   38563353
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein blockade limits
            the development of atherosclerosis and reduces plaque inflammation.
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Zarezadeh Mehrabadi,A., Shahba,F., Khorramdelazad,H.,
            Aghamohammadi,N., Karimi,M., Bagherzadeh,K., Khoshmirsafa,M.,
            Massoumi,R. and Falak,R.
  TITLE     Interleukin-1 receptor accessory protein (IL-1RAP): A magic bullet
            candidate for immunotherapy of human malignancies
  JOURNAL   Crit Rev Oncol Hematol 193, 104200 (2024)
   PUBMED   37981104
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein (IL-1RAP): A
            magic bullet candidate for immunotherapy of human malignancies.
            Review article
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Cao,K., Liu,Z., Liu,J., Hu,Q., Shan,W., Hu,B., Shi,H. and Zhang,B.
  TITLE     Constitutive photomorphogenic protein 1 ubiquitinates interleukin-1
            receptor accessory protein in human liver cancer
  JOURNAL   J Cancer Res Clin Oncol 149 (18), 16247-16260 (2023)
   PUBMED   37700160
  REMARK    GeneRIF: Constitutive photomorphogenic protein 1 ubiquitinates
            interleukin-1 receptor accessory protein in human liver cancer.
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Yu,F., Xing,J., Li,L. and Xiang,M.
  TITLE     CircCRIM1 mediates proliferation, migration, and invasion of
            trophoblast cell through regulating miR-942-5p/IL1RAP axis
  JOURNAL   Am J Reprod Immunol 90 (1), e13699 (2023)
   PUBMED   37382169
  REMARK    GeneRIF: CircCRIM1 mediates proliferation, migration, and invasion
            of trophoblast cell through regulating miR-942-5p/IL1RAP axis.
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Agerstam,H., Lilljebjorn,H., Rissler,M., Sanden,C. and Fioretos,T.
  TITLE     IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models
  JOURNAL   Haematologica 108 (2), 599-604 (2023)
   PUBMED   36226493
  REMARK    GeneRIF: IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Wesche,H., Korherr,C., Kracht,M., Falk,W., Resch,K. and Martin,M.U.
  TITLE     The interleukin-1 receptor accessory protein (IL-1RAcP) is
            essential for IL-1-induced activation of interleukin-1
            receptor-associated kinase (IRAK) and stress-activated protein
            kinases (SAP kinases)
  JOURNAL   J Biol Chem 272 (12), 7727-7731 (1997)
   PUBMED   9065432
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Parnet,P., Garka,K.E., Bonnert,T.P., Dower,S.K. and Sims,J.E.
  TITLE     IL-1Rrp is a novel receptor-like molecule similar to the type I
            interleukin-1 receptor and its homologues T1/ST2 and IL-1R AcP
  JOURNAL   J Biol Chem 271 (8), 3967-3970 (1996)
   PUBMED   8626725
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Greenfeder,S.A., Nunes,P., Kwee,L., Labow,M., Chizzonite,R.A. and
            Ju,G.
  TITLE     Molecular cloning and characterization of a second subunit of the
            interleukin 1 receptor complex
  JOURNAL   J Biol Chem 270 (23), 13757-13765 (1995)
   PUBMED   7775431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA024801.1, AB006537.1,
            BM194193.1 and BM973472.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a component of the interleukin 1
            receptor complex, which initiates signalling events that result in
            the activation of interleukin 1-responsive genes. Alternative
            splicing of this gene results in membrane-bound and soluble
            isoforms differing in their C-terminus. The ratio of soluble to
            membrane-bound forms increases during acute-phase induction or
            stress. [provided by RefSeq, Jul 2018].
            
            Transcript Variant: This variant (1) encodes the membrane-bound
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB006537.1, SRR1660803.224601.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000447382.6/ ENSP00000390541.1
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q28"
     Protein         1..570
                     /product="interleukin-1 receptor accessory protein isoform
                     1 precursor"
                     /EC_number="3.2.2.6"
                     /note="interleukin-1 receptor accessory protein beta;
                     interleukin-1 receptor 3; IL-1 receptor accessory protein"
                     /calculated_mol_wt=63114
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2323
     mat_peptide     21..570
                     /product="Interleukin-1 receptor accessory protein.
                     /id=PRO_0000015450"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
                     /calculated_mol_wt=63114
     Region          25..132
                     /region_name="Ig1_IL1R_like"
                     /note="First immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20992"
                     /db_xref="CDD:409584"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409584"
     Site            order(27,29..36)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409584"
     Region          34..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409584"
     Region          42..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409584"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          67..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409584"
     Region          69..85
                     /region_name="Essential for interaction with PTPRD.
                     /evidence=ECO:0000250|UniProtKB:Q61730"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          80..82
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409584"
     Region          91..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409584"
     Region          97..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409584"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          110..118
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409584"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          121..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409584"
     Region          143..235
                     /region_name="Ig2_IL-1RAP_like"
                     /note="Second immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20993"
                     /db_xref="CDD:409585"
     Site            order(143..145,147..150,157,162,164,196,234)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          243..349
                     /region_name="Ig3_IL1RAP"
                     /note="Third immunoglobulin domain of interleukin-1
                     receptor accessory protein (IL1RAP); cd20931"
                     /db_xref="CDD:409525"
     Region          243..246
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409525"
     Region          254..258
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409525"
     Region          260..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409525"
     Region          278..283
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409525"
     Region          286..288
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409525"
     Region          296..304
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409525"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          310..318
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409525"
     Region          329..335
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409525"
     Region          339..345
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409525"
     Site            368..388
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          405..552
                     /region_name="TIR"
                     /note="TIR domain; pfam01582"
                     /db_xref="CDD:396246"
     Region          549..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     CDS             1..570
                     /gene="IL1RAP"
                     /gene_synonym="C3orf13; IL-1RAcP; IL1R3"
                     /coded_by="NM_002182.4:224..1936"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3298.1"
                     /db_xref="GeneID:3556"
                     /db_xref="HGNC:HGNC:5995"
                     /db_xref="MIM:602626"
ORIGIN      
        1 mtllwcvvsl yfygilqsda sercddwgld tmrqiqvfed eparikcplf ehflkfnyst
       61 ahsagltliw ywtrqdrdle epinfrlpen riskekdvlw frptllndtg nytcmlrntt
      121 ycskvafple vvqkdscfns pmklpvhkly ieygiqritc pnvdgyfpss vkptitwymg
      181 cykiqnfnnv ipegmnlsfl ialisnngny tcvvtypeng rtfhltrtlt vkvvgspkna
      241 vppvihspnd hvvyekepge ellipctvyf sflmdsrnev wwtidgkkpd ditidvtine
      301 sishsrtede trtqilsikk vtsedlkrsy vcharsakge vakaakvkqk vpaprytvel
      361 acgfgatvll vvilivvyhv ywlemvlfyr ahfgtdetil dgkeydiyvs yarnaeeeef
      421 vlltlrgvle nefgyklcif drdslpggiv tdetlsfiqk srrllvvlsp nyvlqgtqal
      481 lelkaglenm asrgninvil vqykavketk vkelkraktv ltvikwkgek skypqgrfwk
      541 qlqvampvkk sprrsssdeq glsysslknv
//
LOCUS       NP_060559                726 aa            linear   PRI 27-APR-2025
DEFINITION  tRNA endonuclease ANKZF1 isoform 1 [Homo sapiens].
ACCESSION   NP_060559
VERSION     NP_060559.2
DBSOURCE    REFSEQ: accession NM_018089.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Li,G., Wang,Z., Gao,B., Dai,K., Niu,X., Li,X., Wang,Y., Li,L.,
            Wu,X., Li,H., Yu,Z., Wang,Z. and Chen,G.
  TITLE     ANKZF1 knockdown inhibits glioblastoma progression by promoting
            intramitochondrial protein aggregation through mitoRQC
  JOURNAL   Cancer Lett 591, 216895 (2024)
   PUBMED   38670305
  REMARK    GeneRIF: ANKZF1 knockdown inhibits glioblastoma progression by
            promoting intramitochondrial protein aggregation through mitoRQC.
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Zhang,J., Wang,Y., Hou,S., Chi,X., Ding,D., Xue,M., Zhang,M.,
            Wang,J., Shuai,J., Sun,H., Gao,Q. and Kang,C.
  TITLE     Overexpression of ZNF169 promotes the growth and proliferation of
            colorectal cancer cells via the upregulation of ANKZF1
  JOURNAL   Oncol Rep 51 (6) (2024)
   PUBMED   38666541
  REMARK    GeneRIF: Overexpression of ZNF169 promotes the growth and
            proliferation of colorectal cancer cells via the upregulation of
            ANKZF1.
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Yip,M.C.J., Savickas,S., Gygi,S.P. and Shao,S.
  TITLE     ELAC1 Repairs tRNAs Cleaved during Ribosome-Associated Quality
            Control
  JOURNAL   Cell Rep 30 (7), 2106-2114 (2020)
   PUBMED   32075755
REFERENCE   4  (residues 1 to 726)
  AUTHORS   Zhou,X., Shang,Y.N., Lu,R., Fan,C.W. and Mo,X.M.
  TITLE     High ANKZF1 expression is associated with poor overall survival and
            recurrence-free survival in colon cancer
  JOURNAL   Future Oncol 15 (18), 2093-2106 (2019)
   PUBMED   31257922
  REMARK    GeneRIF: High ANKZF1 is an independent factor of poor survival
            (overall survival and recurrence-free survival) in colon cancer by
            taking part in angiogenesis and some cancer signaling pathways.
REFERENCE   5  (residues 1 to 726)
  AUTHORS   Yip,M.C.J., Keszei,A.F.A., Feng,Q., Chu,V., McKenna,M.J. and
            Shao,S.
  TITLE     Mechanism for recycling tRNAs on stalled ribosomes
  JOURNAL   Nat Struct Mol Biol 26 (5), 343-349 (2019)
   PUBMED   31011209
REFERENCE   6  (residues 1 to 726)
  AUTHORS   Jager,S., Cimermancic,P., Gulbahce,N., Johnson,J.R., McGovern,K.E.,
            Clarke,S.C., Shales,M., Mercenne,G., Pache,L., Li,K., Hernandez,H.,
            Jang,G.M., Roth,S.L., Akiva,E., Marlett,J., Stephens,M., D'Orso,I.,
            Fernandes,J., Fahey,M., Mahon,C., O'Donoghue,A.J., Todorovic,A.,
            Morris,J.H., Maltby,D.A., Alber,T., Cagney,G., Bushman,F.D.,
            Young,J.A., Chanda,S.K., Sundquist,W.I., Kortemme,T.,
            Hernandez,R.D., Craik,C.S., Burlingame,A., Sali,A., Frankel,A.D.
            and Krogan,N.J.
  TITLE     Global landscape of HIV-human protein complexes
  JOURNAL   Nature 481 (7381), 365-370 (2011)
   PUBMED   22190034
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 726)
  AUTHORS   Stapf,C., Cartwright,E., Bycroft,M., Hofmann,K. and Buchberger,A.
  TITLE     The general definition of the p97/valosin-containing protein
            (VCP)-interacting motif (VIM) delineates a new family of p97
            cofactors
  JOURNAL   J Biol Chem 286 (44), 38670-38678 (2011)
   PUBMED   21896481
REFERENCE   8  (residues 1 to 726)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   9  (residues 1 to 726)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 726)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA226194.1, BC008948.2, BC028334.1 and AC068946.4.
            
            On Jun 16, 2006 this sequence version replaced NP_060559.1.
            
            Transcript Variant: This variant (1)represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008948.2, SRR1803613.62256.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323348.10/ ENSP00000321617.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..726
                     /product="tRNA endonuclease ANKZF1 isoform 1"
                     /note="ankyrin repeat and zinc finger domain-containing
                     protein 1; zinc finger protein 744; tRNA endonuclease
                     ANKZF1; ankyrin repeat and zinc finger domain containing
                     1"
                     /calculated_mol_wt=80796
     Region          40..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Region          69..103
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          74..96
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          120..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Region          207..351
                     /region_name="bVLRF1"
                     /note="Bacteroidetes VLRF1 release factor; pfam18826"
                     /db_xref="CDD:465880"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Region          387..409
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Region          436..474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Region          493..526
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Region          <495..600
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          495..532
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Region          534..565
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          534..563
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Region          588..656
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Site            607
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Region          654..666
                     /region_name="VCP/p97-interacting motif (VIM).
                     /evidence=ECO:0000269|PubMed:21896481"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y5.1)"
     Region          683..724
                     /region_name="VATC"
                     /note="Vms1-associating treble clef domain; pfam18716"
                     /db_xref="CDD:465846"
     CDS             1..726
                     /gene="ANKZF1"
                     /gene_synonym="Vms1; ZNF744"
                     /coded_by="NM_018089.3:126..2306"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42821.1"
                     /db_xref="GeneID:55139"
                     /db_xref="HGNC:HGNC:25527"
                     /db_xref="MIM:617541"
ORIGIN      
        1 mspapdaapa pasislfdls adapvfqgls lvshapgeal araprtscsg sgeresperk
       61 llqgpmdise klfcstcdqt fqnhqeqreh ykldwhrfnl kqrlkdkpll saldfekqss
      121 tgdlssisgs edsdsaseed lqtldrerat feklsrppgf yphrvlfqna qgqflyayrc
      181 vlgphqdppe eaelllqnlq srgprdcvvl maaaghfaga ifqgrevvth ktfhrytvra
      241 krgtaqglrd arggpshsag anlrryneat lykdvrdlla gpswakalee agtillrapr
      301 sgrslffggk gaplqrgdpr lwdiplatrr ptfqelqrvl hklttlhvye edpreavrlh
      361 spqthwktvr eerkkpteee irkicrdeke algqneespk qgsgsegedg fqvelelvel
      421 tvgtldlces evlpkrrrrk rnkkeksrdq eagahrtllq qtqeeepstq ssqavaaplg
      481 plldeakapg qpelwnalla acragdvgvl klqlapspad prvlsllsap lgsggftllh
      541 aaaaagrgsv vrllleagad ptvqdsrarp pytvaadkst rnefrrfmek npdaydynka
      601 qvpgpltpem earqatrkre qkaarrqree qqqrqqeqee rereeqrrfa alsdrekral
      661 aaerrlaaql gaptspipds aivntrrcws cgaslqgltp fhyldfsfcs trclqdhrrq
      721 agrpss
//
LOCUS       NP_001503                222 aa            linear   PRI 27-APR-2025
DEFINITION  glutathione S-transferase A4 [Homo sapiens].
ACCESSION   NP_001503
VERSION     NP_001503.1
DBSOURCE    REFSEQ: accession NM_001512.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Bruns,C.M., Hubatsch,I., Ridderstrom,M., Mannervik,B. and
            Tainer,J.A.
  TITLE     Human glutathione transferase A4-4 crystal structures and
            mutagenesis reveal the basis of high catalytic efficiency with
            toxic lipid peroxidation products
  JOURNAL   J Mol Biol 288 (3), 427-439 (1999)
   PUBMED   10329152
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Desmots,F., Rauch,C., Henry,C., Guillouzo,A. and Morel,F.
  TITLE     Genomic organization, 5'-flanking region and chromosomal
            localization of the human glutathione transferase A4 gene
  JOURNAL   Biochem J 336 (Pt 2) (Pt 2), 437-442 (1998)
   PUBMED   9820822
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Liu,S., Stoesz,S.P. and Pickett,C.B.
  TITLE     Identification of a novel human glutathione S-transferase using
            bioinformatics
  JOURNAL   Arch Biochem Biophys 352 (2), 306-313 (1998)
   PUBMED   9587421
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Board,P.G.
  TITLE     Identification of cDNAs encoding two human alpha class glutathione
            transferases (GSTA3 and GSTA4) and the heterologous expression of
            GSTA4-4
  JOURNAL   Biochem J 330 (Pt 2) (Pt 2), 827-831 (1998)
   PUBMED   9480897
REFERENCE   10 (residues 1 to 222)
  AUTHORS   Hubatsch,I., Ridderstrom,M. and Mannervik,B.
  TITLE     Human glutathione transferase A4-4: an alpha class enzyme with high
            catalytic efficiency in the conjugation of 4-hydroxynonenal and
            other genotoxic products of lipid peroxidation
  JOURNAL   Biochem J 330 (Pt 1) (Pt 1), 175-179 (1998)
   PUBMED   9461507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA521337.1, AK315369.1,
            BC063439.1 and AA709059.1.
            
            Summary: Cytosolic and membrane-bound forms of glutathione
            S-transferase are encoded by two distinct supergene families. These
            enzymes are involved in cellular defense against toxic,
            carcinogenic, and pharmacologically active electrophilic compounds.
            At present, eight distinct classes of the soluble cytoplasmic
            mammalian glutathione S-transferases have been identified: alpha,
            kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a
            glutathione S-tranferase belonging to the alpha class. The alpha
            class genes, which are located in a cluster on chromosome 6, are
            highly related and encode enzymes with glutathione peroxidase
            activity that function in the detoxification of lipid peroxidation
            products. Reactive electrophiles produced by oxidative metabolism
            have been linked to a number of degenerative diseases including
            Parkinson's disease, Alzheimer's disease, cataract formation, and
            atherosclerosis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF025887.1, SRR1163655.103801.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370963.9/ ENSP00000360002.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.2"
     Protein         1..222
                     /product="glutathione S-transferase A4"
                     /EC_number="2.5.1.18"
                     /note="glutathione S-alkyltransferase A4; glutathione
                     S-aryltransferase A4; S-(hydroxyalkyl)glutathione lyase
                     A4; glutathione S-aralkyltransferase A4; glutathione
                     transferase A4-4; GST class-alpha member 4; glutathione
                     S-transferase A4-4"
                     /calculated_mol_wt=25573
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P14942; propagated from
                     UniProtKB/Swiss-Prot (O15217.1)"
     Region          4..82
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     Region          86..220
                     /region_name="GST_C_Alpha"
                     /note="C-terminal, alpha helical domain of Class Alpha
                     Glutathione S-transferases; cd03208"
                     /db_xref="CDD:198317"
     Site            order(86..87,89,93..95,97..98,101,131)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(97,104,107,110..111,131..132,135,152..155,158,
                     161..162,165..166,169,193..194,196..201)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(101,107,111,131,208,216,220)
                     /site_type="other"
                     /note="substrate binding pocket (H-site) [chemical
                     binding]"
                     /db_xref="CDD:198317"
     CDS             1..222
                     /gene="GSTA4"
                     /gene_synonym="GSTA4-4; GTA4"
                     /coded_by="NM_001512.4:55..723"
                     /db_xref="CCDS:CCDS4948.1"
                     /db_xref="GeneID:2941"
                     /db_xref="HGNC:HGNC:4629"
                     /db_xref="MIM:605450"
ORIGIN      
        1 maarpklhyp ngrgrmesvr wvlaaagvef deefletkeq lyklqdgnhl lfqqvpmvei
       61 dgmklvqtrs ilhyiadkhn lfgknlkert lidmyvegtl dllellimhp flkpddqqke
      121 vvnmaqkaii ryfpvfekil rghgqsflvg nqlsladvil lqtilaleek ipnilsafpf
      181 lqeytvklsn iptikrflep gskkkpppde iyvrtvynif rp
//
LOCUS       NP_001932                896 aa            linear   PRI 27-APR-2025
DEFINITION  desmocollin-3 isoform Dsc3a preproprotein [Homo sapiens].
ACCESSION   NP_001932
VERSION     NP_001932.2
DBSOURCE    REFSEQ: accession NM_001941.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 896)
  AUTHORS   Saleh,M.A., Said,R.M., Ahmed Rashed,L.A. and El-Kalioby,M.
  TITLE     Upregulation of Anti-Desmocollin 3 Antibodies in Pemphigus
            Diseases: A Case-control Study
  JOURNAL   Acta Dermatovenerol Croat 31 (4), 178-183 (2023)
   PUBMED   38651843
  REMARK    GeneRIF: Upregulation of Anti-Desmocollin 3 Antibodies in Pemphigus
            Diseases: A Case-control Study.
REFERENCE   2  (residues 1 to 896)
  AUTHORS   Kawamura,T., Muramatsu,K., Orita,A., Mai,Y., Sugai,T., Haga,N.,
            Fujimura,Y., Miyauchi,T., Izumi,K., Koga,H., Ishii,N. and Ujiie,H.
  TITLE     Two cases of Hallopeau-type pemphigus vegetans with anti-desmoglein
            1 and anti-desmocollin 3 antibodies without mucosal involvement
  JOURNAL   J Eur Acad Dermatol Venereol 37 (4), e508-e510 (2023)
   PUBMED   36305887
  REMARK    GeneRIF: Two cases of Hallopeau-type pemphigus vegetans with
            anti-desmoglein 1 and anti-desmocollin 3 antibodies without mucosal
            involvement.
REFERENCE   3  (residues 1 to 896)
  AUTHORS   Koga,H., Teye,K., Otsuji,Y., Ishii,N., Hashimoto,T. and Nakama,T.
  TITLE     Autoantibodies to DSC3 in Pemphigus Exclusively Recognize
            Calcium-Dependent Epitope in Extracellular Domain 2
  JOURNAL   J Invest Dermatol 141 (9), 2123-2131 (2021)
   PUBMED   33766509
  REMARK    GeneRIF: Autoantibodies to DSC3 in Pemphigus Exclusively Recognize
            Calcium-Dependent Epitope in Extracellular Domain 2.
REFERENCE   4  (residues 1 to 896)
  AUTHORS   Cui,T., Yang,L., Ma,Y., Petersen,I. and Chen,Y.
  TITLE     Desmocollin 3 has a tumor suppressive activity through inhibition
            of AKT pathway in colorectal cancer
  JOURNAL   Exp Cell Res 378 (2), 124-130 (2019)
   PUBMED   30857973
  REMARK    GeneRIF: DSC3 suppresses colorectal cancer cell growth through
            inhibition of AKT pathway and regulation of E-cadherin
REFERENCE   5  (residues 1 to 896)
  AUTHORS   Gadhavi,P.L., Greenwood,M.D., Strom,M., King,I.A. and Buxton,R.S.
  TITLE     The regulatory region of the human desmocollin 3 promoter forms a
            DNA four-way junction
  JOURNAL   Biochem Biophys Res Commun 281 (2), 520-528 (2001)
   PUBMED   11181078
REFERENCE   6  (residues 1 to 896)
  AUTHORS   Whittock,N.V., Hunt,D.M., Rickman,L., Malhi,S., Vogazianou,A.P.,
            Dawson,L.F., Eady,R.A., Buxton,R.S. and McGrath,J.A.
  TITLE     Genomic organization and amplification of the human desmosomal
            cadherin genes DSC1 and DSC3, encoding desmocollin types 1 and 3
  JOURNAL   Biochem Biophys Res Commun 276 (2), 454-460 (2000)
   PUBMED   11027496
REFERENCE   7  (residues 1 to 896)
  AUTHORS   King,I.A., Sullivan,K.H., Bennett,R. Jr. and Buxton,R.S.
  TITLE     The desmocollins of human foreskin epidermis: identification and
            chromosomal assignment of a third gene and expression patterns of
            the three isoforms
  JOURNAL   J Invest Dermatol 105 (3), 314-321 (1995)
   PUBMED   7665906
REFERENCE   8  (residues 1 to 896)
  AUTHORS   Amagai,M., Wang,Y., Minoshima,S., Kawamura,K., Green,K.J.,
            Nishikawa,T. and Shimizu,N.
  TITLE     Assignment of the human genes for desmocollin 3 (DSC3) and
            desmocollin 4 (DSC4) to chromosome 18q12
  JOURNAL   Genomics 25 (1), 330-332 (1995)
   PUBMED   7774948
REFERENCE   9  (residues 1 to 896)
  AUTHORS   Kawamura,K., Watanabe,K., Suzuki,T., Yamakawa,T., Kamiyama,T.,
            Nakagawa,H. and Tsurufuji,S.
  TITLE     cDNA cloning and expression of a novel human desmocollin
  JOURNAL   J Biol Chem 269 (42), 26295-26302 (1994)
   PUBMED   7929347
REFERENCE   10 (residues 1 to 896)
  AUTHORS   Arnemann,J., Spurr,N.K., Wheeler,G.N., Parker,A.E. and Buxton,R.S.
  TITLE     Chromosomal assignment of the human genes coding for the major
            proteins of the desmosome junction, desmoglein DGI (DSG),
            desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP), and
            plakoglobin DPIII (JUP)
  JOURNAL   Genomics 10 (3), 640-645 (1991)
   PUBMED   1889810
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA860471.1, D17427.1,
            AC025212.5 and AI123917.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 2, 2007 this sequence version replaced NP_001932.1.
            
            Summary: The protein encoded by this gene is a calcium-dependent
            glycoprotein that is a member of the desmocollin subfamily of the
            cadherin superfamily. These desmosomal family members, along with
            the desmogleins, are found primarily in epithelial cells where they
            constitute the adhesive proteins of the desmosome cell-cell
            junction and are required for cell adhesion and desmosome
            formation. The desmosomal family members are arranged in two
            clusters on chromosome 18, occupying less than 650 kb combined.
            Mutations in this gene are a cause of hypotrichosis and recurrent
            skin vesicles disorder. The protein can act as an autoantigen in
            pemphigus diseases, and it is also considered to be a biomarker for
            some cancers. Alternative splicing of this gene results in multiple
            transcript variants. [provided by RefSeq, Apr 2014].
            
            Transcript Variant: This variant (Dsc3a) represents the shorter
            transcript but encodes the longer isoform (Dsc3a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D17427.1, X83929.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360428.9/ ENSP00000353608.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..896
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..896
                     /product="desmocollin-3 isoform Dsc3a preproprotein"
                     /note="desmocollin-4; cadherin family member 3"
                     /calculated_mol_wt=97008
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2980
     Region          27..111
                     /region_name="Cadherin_pro"
                     /note="Cadherin prodomain like; smart01055"
                     /db_xref="CDD:214999"
     mat_peptide     136..896
                     /product="Desmocollin-3. /id=PRO_0000003876"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14574.3)"
                     /calculated_mol_wt=84717
     Region          140..234
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            order(146..147,202,204,235,237..238)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206635"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14574.3)"
     Region          247..351
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(254..255,312,314,347,349..350)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          360..462
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            392
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14574.3)"
     Region          477..573
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(482..483,534,536,569,571..572)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            546
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14574.3)"
     Region          <596..669
                     /region_name="CA_like"
                     /note="Cadherin repeat-like domain; cl46864"
                     /db_xref="CDD:481204"
     Site            629
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14574.3)"
     Site            691..711
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14574.3)"
     Region          841..891
                     /region_name="CADH_Y-type_LIR"
                     /note="Cadherin, Y-type LIR-motif; pfam01049"
                     /db_xref="CDD:460041"
     CDS             1..896
                     /gene="DSC3"
                     /gene_synonym="CDHF3; DSC; DSC1; DSC2; DSC4; HT-CP"
                     /coded_by="NM_001941.5:83..2773"
                     /note="isoform Dsc3a preproprotein is encoded by
                     transcript variant Dsc3a"
                     /db_xref="CCDS:CCDS32810.1"
                     /db_xref="GeneID:1825"
                     /db_xref="HGNC:HGNC:3037"
                     /db_xref="MIM:600271"
ORIGIN      
        1 maaagprrsv rgavclhlll tlvifsrage ackkvilnvp skleadkiig rvnleecfrs
       61 adlirssdpd frvlndgsvy taravalsdk krsftiwlsd krkqtqkevt vllehqkkvs
      121 ktrhtretvl rrakrrwapi pcsmqenslg pfplflqqve sdaaqnytvf ysisgrgvdk
      181 eplnlfyier dtgnlfctrp vdreeydvfd liayastadg ysadlplplp irvedendnh
      241 pvfteaiynf evlessrpgt tvgvvcatdr depdtmhtrl kysilqqtpr spglfsvhps
      301 tgvittvshy ldrevvdkys limkvqdmdg qffgligtst ciitvtdsnd naptfrqnay
      361 eafveenafn veilripied kdlintanwr vnftilkgne nghfkistdk etnegvlsvv
      421 kplnyeenrq vnleigvnne apfardiprv talnralvtv hvrdldegpe ctpaaqyvri
      481 kenlavgski ngykaydpen rngnglrykk lhdpkgwiti deisgsiits kildrevetp
      541 knelynitvl aidkddrsct gtlavniedv ndnppeilqe yvvickpkmg ytdilavdpd
      601 epvhgapfyf slpntspeis rlwsltkvnd taarlsyqkn agfqeytipi tvkdragqaa
      661 tkllrvnlce cthptqcrat srstgvilgk wailaillgi allfsvlltl vcgvfgatkg
      721 krfpedlaqq nliisnteap gddrvcsang fmtqttnnss qgfcgtmgsg mknggqetie
      781 mmkggnqtle scrgaghhht ldscrgghte vdncrytyse whsftqprlg eklhrcnqne
      841 drmpsqdyvl tynyegrgsp agsvgccsek qeedgldfln nlepkfitla eactkr
//
LOCUS       NP_055192                621 aa            linear   PRI 27-APR-2025
DEFINITION  dnaJ homolog subfamily C member 2 isoform 1 [Homo sapiens].
ACCESSION   NP_055192
VERSION     NP_055192.1
DBSOURCE    REFSEQ: accession NM_014377.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            an